#Gene_name pLi pRec pNull Gene_full_name Function_description Disease_description Tissue_specificity(Uniprot) Expression(egenetics) Expression(GNF/Atlas) P(HI) P(rec) RVIS RVIS_percentile GDI GDI-Phred A1BG 9.0649236354772e-05 0.786086131023045 0.2138232197406 alpha-1-B glycoprotein . . TISSUE SPECIFICITY: Plasma.; unclassifiable (Anatomical System);amygdala;prostate;lung;islets of Langerhans;liver;spleen;germinal center;brain;thymus; fetal liver;liver;fetal lung;trigeminal ganglion; 0.07384 0.31615 -0.466531444 23.51380042 79.3774 1.88274 A1BG-AS1 . . . A1BG antisense RNA 1 . . . . . . . . . . . A1CF 0.00361970078438154 0.995993655163751 0.000386644051867698 APOBEC1 complementation factor FUNCTION: Essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. Binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. The complex also protects the edited APOB mRNA from nonsense-mediated decay. {ECO:0000269|PubMed:10669759, ECO:0000269|PubMed:10781591, ECO:0000269|PubMed:12881431}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in brain, liver, pancreas, colon and spleen. {ECO:0000269|PubMed:10669759}.; unclassifiable (Anatomical System);islets of Langerhans;liver;colon;spleen;kidney;stomach; fetal liver;superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.18871 0.35999 -0.378346116 28.01368247 314.85493 3.77246 A2M 0.000540114865271392 0.999459801979781 8.3154947445575e-08 alpha-2-macroglobulin FUNCTION: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase.; . TISSUE SPECIFICITY: Secreted in plasma. {ECO:0000269|PubMed:6203908}.; myocardium;smooth muscle;ovary;skin;retina;prostate;frontal lobe;endometrium;thyroid;brain;gall bladder;tonsil;heart;tongue;adrenal cortex;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach; . 0.27005 0.79618 0.099178678 60.75725407 1920.76046 8.06882 A2M-AS1 . . . A2M antisense RNA 1 (head to head) . . . . . . . . . . . A2ML1 1.32902210264609e-22 0.201298944611439 0.798701055388561 alpha-2-macroglobulin like 1 FUNCTION: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity). Displays inhibitory activity against chymotrypsin, papain, thermolysin, subtilisin A and, to a lesser extent, elastase but not trypsin. May play an important role during desquamation by inhibiting extracellular proteases. {ECO:0000250|UniProtKB:P01023, ECO:0000269|PubMed:16298998}.; . TISSUE SPECIFICITY: In the epidermis, expressed predominantly in the granular layer at the apical edge of keratinocytes (at protein level). Also detected in placenta, testis and thymus but not in epithelia of kidney, lung, small intestine or colon. {ECO:0000269|PubMed:16298998}.; unclassifiable (Anatomical System);breast;frontal lobe;larynx;hypopharynx;colon;head and neck;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;tongue;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.06001 0.08330 2.41990149 98.52559566 7253.67873 18.31932 A2ML1-AS1 . . . A2ML1 antisense RNA 1 . . . . . . . . . . . A2ML1-AS2 . . . A2ML1 antisense RNA 2 . . . . . . . . . . . A2MP1 . . . alpha-2-macroglobulin pseudogene 1 . . . . . . . . . . . A3GALT2 6.50302639229507e-07 0.145666833765185 0.854332515932176 alpha 1,3-galactosyltransferase 2 . . . . . 0.10629 0.09600 . . 272.82681 3.54057 A4GALT 0.111598718084493 0.777534623470403 0.110866658445104 alpha 1,4-galactosyltransferase FUNCTION: Necessary for the biosynthesis of the Pk antigen of blood histogroup P. Catalyzes the transfer of galactose to lactosylceramide and galactosylceramide. Necessary for the synthesis of the receptor for bacterial verotoxins.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in kidney, heart, spleen, liver, testis and placenta.; unclassifiable (Anatomical System);lymphoreticular;cartilage;heart;islets of Langerhans;muscle;skin;uterus;pancreas;prostate;whole body;lung;bone;placenta;iris;liver;spleen;germinal center;brain;mammary gland;bladder; ciliary ganglion;atrioventricular node; 0.10228 0.22182 -0.290161348 33.33923095 67.38232 1.69929 A4GNT 0.598408702159303 0.392305268458394 0.00928602938230314 alpha-1,4-N-acetylglucosaminyltransferase FUNCTION: Necessary for the synthesis of type III mucin. Catalyzes the transfer of N-acetylglucosamine (GlcNAc) to core 2 branched O- glycans.; . TISSUE SPECIFICITY: Detected in stomach and pancreas.; kidney;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cingulate cortex;skin; 0.08072 0.08845 1.107875794 92.03821656 233.66 3.30331 AAAS 4.54287182926272e-10 0.792914348866523 0.20708565067919 aladin WD repeat nucleoporin FUNCTION: Plays a role in the normal development of the peripheral and central nervous system.; . TISSUE SPECIFICITY: Widely expressed. Particularly abundant expression is found in cerebellum, corpus callosum, adrenal gland, pituitary gland, gastrointestinal structures and fetal lung. {ECO:0000269|PubMed:16022285}.; lymphoreticular;medulla oblongata;ovary;colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;iris;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;amnion;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum;thymus; . 0.60947 . -0.911109353 9.961075725 101.66522 2.18230 AACS 4.2456926056096e-12 0.17179010103688 0.828209898958874 acetoacetyl-CoA synthetase FUNCTION: Activates acetoacetate to acetoacetyl-CoA. May be involved in utilizing ketone body for the fatty acid-synthesis during adipose tissue development (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in kidney, heart and brain, but low in liver. {ECO:0000269|PubMed:12623130}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;bile duct;lung;cornea;epididymis;nasopharynx;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; amygdala;whole brain;adipose tissue;temporal lobe;prefrontal cortex;testis;cingulate cortex;parietal lobe; 0.18243 0.23898 -1.170241634 6.039160179 163.63033 2.79374 AACSP1 . . . acetoacetyl-CoA synthetase pseudogene 1 . . . . . . . . . . . AADAC 0.000181834436419695 0.703259060740575 0.296559104823006 arylacetamide deacetylase FUNCTION: Displays cellular triglyceride lipase activity in liver, increases the levels of intracellular fatty acids derived from the hydrolysis of newly formed triglyceride stores and plays a role in very low-density lipoprotein assembly. Displays serine esterase activity in liver. Deacetylates a variety of arylacetamide substrates, including xenobiotic compounds and procarcinogens, converting them to the primary arylamide compounds and increasing their toxicity. {ECO:0000269|PubMed:17936933, ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:23542347}.; . TISSUE SPECIFICITY: Detected in liver (at protein level). Mainly expressed in liver, small intestine, colon, adrenal gland and bladder. {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931}.; unclassifiable (Anatomical System);heart;small intestine;ovary;colon;parathyroid;skeletal muscle;uterus;pancreas;lung;adrenal gland;placenta;liver;testis;spleen;kidney;stomach; fetal liver;superior cervical ganglion;adrenal gland;temporal lobe;liver;adrenal cortex;fetal lung;cingulate cortex;skeletal muscle;parietal lobe; 0.02400 0.07726 -0.091746757 46.91554612 98.58087 2.14611 AADACL2 1.78138870795841e-08 0.230782215605282 0.769217766580831 arylacetamide deacetylase-like 2 . . . uterus;lung;heart;placenta;colon; . 0.06376 0.11585 -0.314027422 31.9297004 62.30478 1.61119 AADACL2-AS1 . . . AADACL2 antisense RNA 1 . . . . . . . . . . . AADACL3 0.00015633351437561 0.43495652549271 0.564887140992915 arylacetamide deacetylase-like 3 . . . . . 0.07474 0.07813 2.131332486 97.92403869 843.85416 5.68691 AADACL4 0.000547686324044419 0.700937101417738 0.298515212258218 arylacetamide deacetylase-like 4 . . . . . 0.05904 0.09282 -0.622676946 17.31540458 51.31876 1.41305 AADACP1 . . . arylacetamide deacetylase pseudogene 1 . . . . . . . . . . . AADAT 0.250802295313827 0.747906651301809 0.0012910533843643 aminoadipate aminotransferase FUNCTION: Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino- group acceptors, with a preference for 2-oxoglutarate, 2- oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro). {ECO:0000269|PubMed:18620547}.; . TISSUE SPECIFICITY: Higher expression in the liver. Also found in heart, brain, kidney, pancreas, prostate, testis and ovary.; unclassifiable (Anatomical System);lymph node;ovary;lacrimal gland;islets of Langerhans;colon;parathyroid;skin;retina;prostate;whole body;lung;cochlea;endometrium;bone;placenta;visual apparatus;liver;testis;spleen;brain;mammary gland;stomach; trigeminal ganglion; 0.07259 0.12828 -0.117432389 44.89266336 7.64128 0.28257 AAED1 9.50774394657092e-08 0.0490058882951403 0.95099401662742 AhpC/TSA antioxidant enzyme domain containing 1 . . . . . 0.20115 0.08675 0.170987912 65.5579146 631.61722 5.06351 AAGAB 0.00810207313151983 0.977864167974257 0.0140337588942233 alpha- and gamma-adaptin binding protein FUNCTION: May be involved in endocytic recycling of growth factor receptors such as EGFR. {ECO:0000269|PubMed:23064416}.; . TISSUE SPECIFICITY: Widely expressed, including in skin and keratinocytes, with highest levels in adrenal gland, rectum and thymus. {ECO:0000269|PubMed:23000146, ECO:0000269|PubMed:23064416}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;iris;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);heart;epidermis;islets of Langerhans;blood;lens;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cingulate cortex; . . 0.020302773 55.60863411 3541.69204 11.48310 AAK1 0.99932042127733 0.000679578553667441 1.69002206897236e-10 AP2 associated kinase 1 FUNCTION: Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Isoform 1 and isoform 2 display similar levels of kinase activity towards AP2M1. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity. {ECO:0000269|PubMed:12952931, ECO:0000269|PubMed:17494869, ECO:0000269|PubMed:18657069, ECO:0000269|PubMed:21464124}.; . TISSUE SPECIFICITY: Detected in brain, heart and liver. Isoform 1 is the predominant isoform in brain. {ECO:0000269|PubMed:17494869}.; . . 0.09908 0.09543 -0.664951379 15.91177164 3996.40242 12.50722 AAMDC 0.000474346768584031 0.434325570839455 0.565200082391962 adipogenesis associated, Mth938 domain containing FUNCTION: May play a role in preadipocyte differentiation and adipogenesis. {ECO:0000250}.; . . . . 0.07691 0.11262 0.281220278 71.07808445 1406.35943 7.00705 AAMP 0.531201269396819 0.468105024546197 0.000693706056983601 angio associated migratory cell protein FUNCTION: Plays a role in angiogenesis and cell migration. In smooth muscle cell migration, may act through the RhoA pathway. {ECO:0000269|PubMed:10329261, ECO:0000269|PubMed:18634987}.; . TISSUE SPECIFICITY: Expressed in metastatic melanoma, liver, skin, kidney, heart, lung, lymph node, skeletal muscle and brain, and also in A2058 melanoma cells and activated T-cells (at protein level). Expressed in blood vessels. Strongly expressed in endothelial cells, cytotrophoblasts, and poorly differentiated. colon adenocarcinoma cells found in lymphatics. {ECO:0000269|PubMed:10329261, ECO:0000269|PubMed:7743515}.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;adrenal cortex;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus;cerebellum; superior cervical ganglion;pons; 0.49551 0.12230 0.040529541 57.15380986 343.13644 3.92709 AANAT 0.0130382386829393 0.65936944025443 0.327592321062631 aralkylamine N-acetyltransferase FUNCTION: Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N- acetylserotonin, the penultimate step in the synthesis of melatonin. {ECO:0000269|PubMed:11313340, ECO:0000305}.; DISEASE: Delayed sleep phase syndrome (DSPS) [MIM:614163]: A circadian rhythm sleep disorder characterized by sleep-onset insomnia and difficulty in awakening at the desired time. Patients with DSPS have chronic difficulty in adjusting their sleep-onset and wake-up times to occupational, school, and social activities. {ECO:0000269|PubMed:12736803}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry. Susceptibility to delayed sleep phase syndrome can be conferred by variant Thr-129. Thr-129 shows a significantly higher frequency in affected individuals than in healthy controls.; TISSUE SPECIFICITY: Highly expressed in pineal gland and at lower levels in the retina. Weak expression in several brain regions and in the pituitary gland. {ECO:0000269|PubMed:18212399, ECO:0000269|PubMed:8661026}.; pineal body;kidney;pineal gland;retina; superior cervical ganglion;subthalamic nucleus;heart;trigeminal ganglion;skeletal muscle;bone marrow; 0.20810 0.21095 -0.069700724 48.54328851 61.04852 1.58969 AAR2 0.000262136180238876 0.541383269914656 0.458354593905105 AAR2 splicing factor homolog . . . . . 0.08372 0.08694 -0.312207497 32.05944798 42.10699 1.22650 AARD 0.328326488367201 0.607804866139538 0.0638686454932607 alanine and arginine rich domain containing protein . . . . . . . . . 1834.49894 7.89444 AARS 4.67831529001667e-05 0.999939421771446 1.37950756542301e-05 alanyl-tRNA synthetase FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain. {ECO:0000255|HAMAP-Rule:MF_03133}.; DISEASE: Charcot-Marie-Tooth disease 2N (CMT2N) [MIM:613287]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. {ECO:0000269|PubMed:20045102, ECO:0000269|PubMed:22009580, ECO:0000269|PubMed:22206013}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epileptic encephalopathy, early infantile, 29 (EIEE29) [MIM:616339]: A form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. EIEE29 patients manifest severe infantile epileptic encephalopathy, clubfoot, absent deep tendon reflexes, extrapyramidal symptoms, and persistently deficient myelination. {ECO:0000269|PubMed:25817015}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; medulla oblongata;superior cervical ganglion;subthalamic nucleus;occipital lobe;cerebellum peduncles;temporal lobe;globus pallidus;caudate nucleus;pons;parietal lobe;cingulate cortex;cerebellum; 0.39793 0.20543 -0.655870776 16.12408587 1228.44466 6.62731 AARS2 1.64858013716987e-07 0.999922898974723 7.69361672633559e-05 alanyl-tRNA synthetase 2, mitochondrial FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain. {ECO:0000255|HAMAP-Rule:MF_03133}.; DISEASE: Combined oxidative phosphorylation deficiency 8 (COXPD8) [MIM:614096]: A mitochondrial disease characterized by a lethal infantile hypertrophic cardiomyopathy, generalized muscle dysfunction and some neurologic involvement. The liver is not affected. {ECO:0000269|PubMed:21549344}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leukoencephalopathy, progressive, with ovarian failure (LKENP) [MIM:615889]: An autosomal recessive neurodegenerative disorder characterized by childhood- to adulthood-onset of signs of neurologic deterioration consisting of ataxia, spasticity, and cognitive decline with features of frontal lobe dysfunction. Brain MRI shows leukoencephalopathy with striking involvement of deep white matter, and cerebellar atrophy. All female patients develop premature ovarian failure. {ECO:0000269|PubMed:24808023}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymphoreticular;cartilage;ovary;islets of Langerhans;colon;skin;breast;lung;endometrium;epididymis;thyroid;placenta;visual apparatus;hippocampus;liver;spleen;germinal center;kidney;brain;mammary gland;stomach; superior cervical ganglion; 0.14300 0.11236 1.14268501 92.37438075 592.72341 4.93503 AARSD1 2.43909906368394e-07 0.477743381323704 0.522256374766389 alanyl-tRNA synthetase domain containing 1 FUNCTION: Functions in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala). {ECO:0000250}.; . . colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;oesophagus;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;macula lutea;liver;kidney;stomach; subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.15995 0.08781 -0.066061882 48.77919321 . . AARSP1 . . . alanyl-tRNA synthetase pseudogene 1 . . . . . . . . . . . AASDH 2.00999745907204e-05 0.998849623075018 0.00113027695039131 aminoadipate-semialdehyde dehydrogenase FUNCTION: Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues. {ECO:0000269|PubMed:15865210}.; ovary;umbilical cord;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;placenta;visual apparatus;liver;spleen;kidney;stomach;cerebellum; superior cervical ganglion;trigeminal ganglion; 0.07506 0.13832 1.054492917 91.3717858 3473.29703 11.34473 AASDHPPT 0.0839417342934132 0.906138752438426 0.009919513268161 aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase FUNCTION: Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'- phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN. {ECO:0000269|PubMed:11286508, ECO:0000269|PubMed:12815048, ECO:0000269|PubMed:18022563}.; . TISSUE SPECIFICITY: Detected in heart, skeletal muscle, placenta, testis, brain, pancreas, liver and kidney. {ECO:0000269|PubMed:11286508, ECO:0000269|PubMed:12815048}.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;thymus; amygdala;whole brain;testis - interstitial;superior cervical ganglion;occipital lobe;thalamus;medulla oblongata;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;testis - seminiferous tubule;fetal brain;prefrontal cortex;globus pallidus;testis;parietal lobe; 0.23809 0.18937 -0.383807564 27.41802312 15.0964 0.54208 AASS 1.35531507533066e-06 0.997781397764295 0.00221724692063012 aminoadipate-semialdehyde synthase FUNCTION: Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-ketoglutarate reductase and saccharopine dehydrogenase activity, respectively.; DISEASE: Hyperlysinemia, 1 (HYPLYS1) [MIM:238700]: An autosomal recessive metabolic condition with variable clinical features. Some patients present with non-specific seizures, hypotonia, or mildly delayed psychomotor development, and increased serum lysine and pipecolic acid on laboratory analysis. However, about half of the probands are reported to be asymptomatic, and hyperlysinemia is generally considered to be a benign metabolic variant. {ECO:0000269|PubMed:10775527}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: 2,4-dienoyl-CoA reductase deficiency (DECRD) [MIM:616034]: A rare, autosomal recessive, inborn error of polyunsaturated fatty acids and lysine metabolism, resulting in mitochondrial dysfunction. Affected individuals have a severe encephalopathy with neurologic and metabolic abnormalities beginning in early infancy. Laboratory studies show increased C10:2 carnitine levels and hyperlysinemia. {ECO:0000269|PubMed:24847004}. Note=The protein represented in this entry is involved in disease pathogenesis. A selective decrease in mitochondrial NADP(H) levels due to NADK2 mutations causes a deficiency of NADPH-dependent mitochondrial enzymes, such as DECR1 and AASS. {ECO:0000269|PubMed:24847004}.; TISSUE SPECIFICITY: Expressed in all 16 tissues examined with highest expression in the liver.; unclassifiable (Anatomical System);lung;endometrium;thyroid;liver;testis;colon;spleen;head and neck;kidney;brain;skeletal muscle;stomach; superior cervical ganglion;atrioventricular node; 0.54672 . -0.905656269 10.12031139 152.77734 2.70342 AATBC . . . apoptosis associated transcript in bladder cancer . . . . . . . . . . . AATF 1.62332337375335e-07 0.845766703047181 0.154233134620481 apoptosis antagonizing transcription factor FUNCTION: May function as a general inhibitor of the histone deacetylase HDAC1. Binding to the pocket region of RB1 may displace HDAC1 from RB1/E2F complexes, leading to activation of E2F target genes and cell cycle progression. Conversely, displacement of HDAC1 from SP1 bound to the CDKN1A promoter leads to increased expression of this CDK inhibitor and blocks cell cycle progression. Also antagonizes PAWR mediated induction of aberrant amyloid peptide production in Alzheimer disease (presenile and senile dementia), although the molecular basis for this phenomenon has not been described to date. {ECO:0000269|PubMed:12450794, ECO:0000269|PubMed:12847090, ECO:0000269|PubMed:14627703, ECO:0000269|PubMed:15207272}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at high levels in brain, heart, kidney, placenta and thymus. {ECO:0000269|PubMed:10783144, ECO:0000269|PubMed:11027528}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.66679 0.29381 -0.286522835 33.47487615 319.73191 3.79794 AATK 0.806763652251614 0.19319225457887 4.40931695156982e-05 apoptosis-associated tyrosine kinase FUNCTION: May be involved in neuronal differentiation. {ECO:0000269|PubMed:10837911}.; . TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:10837911}.; colon;parathyroid;choroid;skin;bone marrow;prostate;frontal lobe;cerebral cortex;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;islets of Langerhans;hypothalamus;muscle;blood;pancreas;lung;adrenal gland;hippocampus;visual apparatus;duodenum;mammary gland;stomach;cerebellum; amygdala;dorsal root ganglion;whole brain;thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;olfactory bulb;hypothalamus;spinal cord;caudate nucleus;pons;subthalamic nucleus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.24713 0.12093 . . 2421.6539 9.14383 AATK-AS1 . . . AATK antisense RNA 1 . . . . . . . . . . . AAVS1 . . . adeno-associated virus integration site 1 . . . . . . . . . . . ABALON . . . apoptotic BCL2L1-antisense long non-coding RNA . . . . . . . . . . . ABAT 0.374368506048295 0.625536380966326 9.51129853789557e-05 4-aminobutyrate aminotransferase FUNCTION: Catalyzes the conversion of gamma-aminobutyrate and L- beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine.; . TISSUE SPECIFICITY: Liver > pancreas > brain > kidney > heart > placenta.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;liver;globus pallidus;ciliary ganglion;kidney;parietal lobe;pituitary;cingulate cortex;cerebellum; 0.40997 . -0.332434268 30.74427931 64.12197 1.64187 ABCA1 0.00165880319635912 0.998341196803411 2.2995914708741e-13 ATP binding cassette subfamily A member 1 FUNCTION: cAMP-dependent and sulfonylurea-sensitive anion transporter. Key gatekeeper influencing intracellular cholesterol transport.; DISEASE: High density lipoprotein deficiency 1 (HDLD1) [MIM:205400]: Recessive disorder characterized by absence of high density lipoprotein (HDL) cholesterol from plasma, accumulation of cholesteryl esters, premature coronary artery disease (CAD), hepatosplenomegaly, recurrent peripheral neuropathy and progressive muscle wasting and weakness. {ECO:0000269|PubMed:10431236, ECO:0000269|PubMed:10431237, ECO:0000269|PubMed:10706591, ECO:0000269|PubMed:10938021, ECO:0000269|PubMed:11086027, ECO:0000269|PubMed:11257260, ECO:0000269|PubMed:11476961, ECO:0000269|PubMed:11476965, ECO:0000269|PubMed:11785958, ECO:0000269|PubMed:12111371, ECO:0000269|PubMed:12111381, ECO:0000269|PubMed:12407001, ECO:0000269|PubMed:14576201, ECO:0000269|PubMed:15019541, ECO:0000269|PubMed:15158913, ECO:0000269|PubMed:15262183, ECO:0000269|PubMed:15297675, ECO:0000269|PubMed:15520867}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: High density lipoprotein deficiency 2 (HDLD2) [MIM:604091]: Inherited as autosomal dominant trait. It is characterized by moderately low HDL cholesterol, predilection toward premature coronary artery disease (CAD) and a reduction in cellular cholesterol efflux. {ECO:0000269|PubMed:10431236, ECO:0000269|PubMed:10533863, ECO:0000269|PubMed:10938021, ECO:0000269|PubMed:11086027, ECO:0000269|PubMed:12009425, ECO:0000269|PubMed:12204794, ECO:0000269|PubMed:15722566}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, but most abundant in macrophages.; . . 0.65897 0.67602 -0.239047284 36.28803963 3823.81697 12.15777 ABCA2 0.999999515728741 4.84271258842093e-07 6.10819372573062e-21 ATP binding cassette subfamily A member 2 FUNCTION: Probable transporter, its natural substrate has not been found yet. May have a role in macrophage lipid metabolism and neural development.; . TISSUE SPECIFICITY: Highly expressed in the brain, whereas lower levels of expression is observed in kidney and liver. {ECO:0000269|PubMed:11309290}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;whole body;optic nerve;frontal lobe;endometrium;bone;thyroid;iris;testis;brain;bladder;amygdala;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;amygdala;thalamus;superior cervical ganglion;occipital lobe;medulla oblongata;spinal cord;pons;atrioventricular node;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.34587 0.29822 -4.237700156 0.123849965 470.40443 4.48778 ABCA3 7.47762721295469e-08 0.999990121958511 9.80326521691456e-06 ATP binding cassette subfamily A member 3 FUNCTION: Plays an important role in the formation of pulmonary surfactant, probably by transporting lipids such as cholesterol.; DISEASE: Pulmonary surfactant metabolism dysfunction 3 (SMDP3) [MIM:610921]: A rare lung disorder due to impaired surfactant homeostasis. It is characterized by alveolar filling with floccular material that stains positive using the periodic acid- Schiff method and is derived from surfactant phospholipids and protein components. Excessive lipoproteins accumulation in the alveoli results in severe respiratory distress. {ECO:0000269|PubMed:15044640}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in lung, followed by brain, pancreas, skeletal muscle and heart. Weakly expressed in placenta, kidney and liver. Also expressed in medullary thyroid carcinoma cells (MTC) and in C-cell carcinoma.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;synovium;testis;brain;unclassifiable (Anatomical System);cartilage;hypothalamus;lens;bile duct;breast;pancreas;lung;macula lutea;hippocampus;visual apparatus;duodenum;kidney;stomach;aorta; . 0.13416 0.16987 -1.477690451 3.709601321 188.10316 2.97844 ABCA4 1.26762782980402e-28 0.894718807468967 0.105281192531033 ATP binding cassette subfamily A member 4 FUNCTION: In the visual cycle, acts as an inward-directed retinoid flipase, retinoid substrates imported by ABCA4 from the extracellular or intradiscal (rod) membrane surfaces to the cytoplasmic membrane surface are all-trans-retinaldehyde (ATR) and N-retinyl-phosphatidyl-ethanolamine (NR-PE). Once transported to the cytoplasmic surface, ATR is reduced to vitamin A by trans- retinol dehydrogenase (tRDH) and then transferred to the retinal pigment epithelium (RPE) where it is converted to 11-cis-retinal. May play a role in photoresponse, removing ATR/NR-PE from the extracellular photoreceptor surfaces during bleach recovery. {ECO:0000269|PubMed:10075733}.; DISEASE: Fundus flavimaculatus (FFM) [MIM:248200]: Autosomal recessive retinal disorder very similar to Stargardt disease. In contrast to Stargardt disease, FFM is characterized by later onset and slowly progressive course. {ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11385708, ECO:0000269|PubMed:9781034}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Macular degeneration, age-related, 2 (ARMD2) [MIM:153800]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. {ECO:0000269|PubMed:19028736, ECO:0000269|PubMed:9295268}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Cone-rod dystrophy 3 (CORD3) [MIM:604116]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. {ECO:0000269|PubMed:10958761, ECO:0000269|PubMed:11385708, ECO:0000269|PubMed:11527935}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa 19 (RP19) [MIM:601718]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP19 is characterized by choroidal atrophy. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Retinal-specific. Seems to be exclusively found in the rims of rod photoreceptor cells.; . . 0.09923 0.38763 0.736662821 86.30573248 3827.03692 12.16874 ABCA5 2.52772496034416e-15 0.99950207064052 0.000497929359477866 ATP binding cassette subfamily A member 5 FUNCTION: May play a role in the processing of autolysosomes. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in testis, skeletal muscle, kidney, liver and placenta. {ECO:0000269|PubMed:12504089, ECO:0000269|Ref.1}.; . . 0.15217 0.11348 0.771533118 86.96036801 3056.32686 10.50775 ABCA6 1.83135791674863e-16 0.979463513500321 0.0205364864996792 ATP binding cassette subfamily A member 6 FUNCTION: Probable transporter which may play a role in macrophage lipid homeostasis.; . TISSUE SPECIFICITY: Widely expressed with higher expression in liver. {ECO:0000269|PubMed:11478798, ECO:0000269|Ref.2}.; unclassifiable (Anatomical System);meninges;lymph node;sympathetic chain;skin;skeletal muscle;retina;bone marrow;uterus;pancreas;pia mater;lung;cerebral cortex;thyroid;liver;testis;spleen;dura mater;germinal center;kidney;brain;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.04657 0.10494 0.264439529 70.44114178 4392.04454 13.23776 ABCA7 1.89160398990449e-36 0.000203956692858879 0.999796043307141 ATP binding cassette subfamily A member 7 FUNCTION: Plays a role in phagocytosis by macrophages of apoptotic cells. Binds APOA1 and may function in apolipoprotein-mediated phospholipid efflux from cells. May also mediate cholesterol efflux. May regulate cellular ceramide homeostasis during keratinocytes differentiation. {ECO:0000269|PubMed:12917409, ECO:0000269|PubMed:12925201, ECO:0000269|PubMed:14570867, ECO:0000269|PubMed:14592415}.; . TISSUE SPECIFICITY: Expressed in leukocytes (at protein level). Widely expressed. Highly expressed in myelo-lymphatic tissues including peripheral leukocytes, thymus, spleen and bone marrow. Isoform 2 is more abundant in lymph node, spleen, thymus and trachea than isoform 1 which is more strongly expressed in brain and bone marrow. {ECO:0000269|PubMed:10873640, ECO:0000269|PubMed:11435699, ECO:0000269|PubMed:14592415}.; unclassifiable (Anatomical System);smooth muscle;lymph node;blood;fovea centralis;lens;retina;bone marrow;prostate;whole body;lung;bone;placenta;macula lutea;liver;spleen;cervix;germinal center;mammary gland;thymus; dorsal root ganglion;superior cervical ganglion; 0.05554 0.15483 -2.151227095 1.462609106 5319.06822 15.08136 ABCA8 1.71937025604407e-33 0.000114648963283913 0.999885351036716 ATP binding cassette subfamily A member 8 FUNCTION: ATP-dependent lipophilic drug transporter. {ECO:0000269|PubMed:12379217}.; . TISSUE SPECIFICITY: Widely expressed with higher expression in heart, skeletal muscle and liver. {ECO:0000269|PubMed:12379217}.; myocardium;medulla oblongata;sympathetic chain;colon;substantia nigra;skin;retina;prostate;optic nerve;whole body;cochlea;endometrium;iris;pituitary gland;testis;dura mater;spinal ganglion;brain;unclassifiable (Anatomical System);meninges;heart;spinal cord;skeletal muscle;pancreas;pia mater;lung;adrenal gland;trabecular meshwork;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; dorsal root ganglion;olfactory bulb;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05674 . 0.909319045 89.47275301 2117.48181 8.47123 ABCA9 1.27777342298461e-26 0.0898157494072025 0.910184250592798 ATP binding cassette subfamily A member 9 FUNCTION: May play a role in monocyte differentiation and lipid homeostasis. {ECO:0000269|PubMed:12150964}.; . TISSUE SPECIFICITY: Widely expressed with higher expression in heart. {ECO:0000269|Ref.1}.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;skin;skeletal muscle;uterus;lung;cerebral cortex;larynx;liver;testis;head and neck;spleen;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07193 . -0.001957219 53.73319179 5531.81651 15.36212 ABCA9-AS1 . . . ABCA9 antisense RNA 1 . . . . . . . . . . . ABCA10 1.20688643660446e-27 0.0119958369911726 0.988004163008827 ATP binding cassette subfamily A member 10 FUNCTION: Probable transporter which may play a role in macrophage lipid homeostasis.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in skeletal muscle, heart, brain and gastrointestinal tract. {ECO:0000269|PubMed:12821155, ECO:0000269|Ref.1}.; unclassifiable (Anatomical System);hypothalamus;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;pancreas;prostate;optic nerve;frontal lobe;cerebral cortex;adrenal gland;macula lutea;liver;testis;germinal center;bladder;aorta; ciliary ganglion;atrioventricular node;skeletal muscle; 0.10188 . 1.037938929 91.14767634 4332.05343 13.10413 ABCA11P . . . ATP binding cassette subfamily A member 11, pseudogene . . . . . 0.03175 . . . . . ABCA12 2.02270864482359e-07 0.999999797728865 2.70254312270528e-13 ATP binding cassette subfamily A member 12 FUNCTION: Probable transporter involved in lipid homeostasis.; DISEASE: Ichthyosis, congenital, autosomal recessive 4A (ARCI4A) [MIM:601277]: A form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non-bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs. {ECO:0000269|PubMed:12915478, ECO:0000269|PubMed:17508018, ECO:0000269|PubMed:18284401, ECO:0000269|PubMed:19262603, ECO:0000269|PubMed:22257947}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ichthyosis, congenital, autosomal recessive 4B (ARCI4B) [MIM:242500]: A rare, very severe form of congenital ichthyosis, in which the neonate is born with a thick covering of armor-like scales. The skin dries out to form hard diamond-shaped plaques separated by fissures, resembling 'armor plating'. The normal facial features are severely affected, with distortion of the lips (eclabion), eyelids (ectropion), ears, and nostrils. Affected babies are often born prematurely and rarely survive the perinatal period. Babies who survive into infancy and beyond develop skin changes resembling severe non-bullous congenital ichthyosiform erythroderma. {ECO:0000269|PubMed:15756637, ECO:0000269|PubMed:16675967, ECO:0000269|PubMed:16902423}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Mainly expressed in the stomach, placenta, testis and fetal brain. {ECO:0000269|PubMed:12697999}.; unclassifiable (Anatomical System);breast;lung;stomach; dorsal root ganglion;occipital lobe;superior cervical ganglion;atrioventricular node;pons;skin;skeletal muscle;subthalamic nucleus;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.16262 0.15786 -0.299763455 32.26586459 2992.15591 10.38229 ABCA13 3.30732765255053e-78 1.65193219415535e-12 0.999999999998348 ATP binding cassette subfamily A member 13 . . TISSUE SPECIFICITY: Significantly expressed in the bone marrow, trachea, testis, thyroid and lung as well as in skin fibroblasts. {ECO:0000269|PubMed:12697998, ECO:0000269|PubMed:23266639}.; . . 0.10497 0.07333 4.730312816 99.78768577 6635.50663 17.23123 ABCA17P . . . ATP binding cassette subfamily A member 17, pseudogene . . . . . . . . . . . ABCB1 0.734473812399813 0.265526186079709 1.52047824193411e-09 ATP binding cassette subfamily B member 1 FUNCTION: Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells.; DISEASE: Inflammatory bowel disease 13 (IBD13) [MIM:612244]: A chronic, relapsing inflammation of the gastrointestinal tract with a complex etiology. It is subdivided into Crohn disease and ulcerative colitis phenotypes. Crohn disease may affect any part of the gastrointestinal tract from the mouth to the anus, but most frequently it involves the terminal ileum and colon. Bowel inflammation is transmural and discontinuous; it may contain granulomas or be associated with intestinal or perianal fistulas. In contrast, in ulcerative colitis, the inflammation is continuous and limited to rectal and colonic mucosal layers; fistulas and granulomas are not observed. Both diseases include extraintestinal inflammation of the skin, eyes, or joints. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in liver, kidney, small intestine and brain.; unclassifiable (Anatomical System);myocardium;heart;islets of Langerhans;sympathetic chain;colon;skin;skeletal muscle;uterus;breast;prostate;lung;placenta;visual apparatus;iris;liver;testis;spleen;kidney;spinal ganglion;brain; superior cervical ganglion;adrenal gland;adrenal cortex;trigeminal ganglion; 0.58236 0.67981 0.099178678 60.75725407 402.73587 4.20979 ABCB4 0.000203043316816073 0.999796617585727 3.39097457360609e-07 ATP binding cassette subfamily B member 4 FUNCTION: Energy-dependent phospholipid efflux translocator that acts as a positive regulator of biliary lipid secretion. Functions as a floppase that translocates specifically phosphatidylcholine (PC) from the inner to the outer leaflet of the canalicular membrane bilayer into the canaliculi of hepatocytes. Translocation of PC makes the biliary phospholipids available for extraction into the canaliculi lumen by bile salt mixed micelles and therefore protects the biliary tree from the detergent activity of bile salts (PubMed:7957936, PubMed:8898203, PubMed:9366571, PubMed:17523162, PubMed:23468132, PubMed:24806754, PubMed:24723470, PubMed:24594635, PubMed:21820390). Plays a role in the recruitment of phosphatidylcholine (PC), phosphatidylethanolamine (PE) and sphingomyelin (SM) molecules to nonraft membranes and to fu rther enrichment of SM and cholesterol in raft membranes in hepatocytes (PubMed:23468132). Required for proper phospholipid bile formation (By similarity). Indirectly involved in cholesterol efflux activity from hepatocytes into the canalicular lumen in the presence of bile salts in an ATP- dependent manner (PubMed:24045840). May promote biliary phospholipid secretion as canaliculi-containing vesicles from the canalicular plasma membrane (PubMed:9366571). In cooperation with ATP8B1, functions to protect hepatocytes from the deleterious detergent activity of bile salts (PubMed:21820390). Does not confer multidrug resistance (By similarity). {ECO:0000250|UniProtKB:P21440, ECO:0000269|PubMed:17523162, ECO:0000269|PubMed:21820390, ECO:0000269|PubMed:23468132, ECO:0000269|PubMed:24045840, ECO:0000269|PubMed:24594635, ECO:0000269|PubMed:24723470, ECO:0000269|PubMed:24806754, ECO:0000269|PubMed:7957936, ECO:0000269|PubMed:8898203, ECO:0000269|PubMed:9366571}.; DISEASE: Cholestasis, progressive familial intrahepatic, 3 (PFIC3) [MIM:602347]: A disorder characterized by early onset of cholestasis that progresses to hepatic fibrosis, cirrhosis, and end-stage liver disease before adulthood. {ECO:0000269|PubMed:11313315, ECO:0000269|PubMed:12671900, ECO:0000269|PubMed:17726488, ECO:0000269|PubMed:21119540, ECO:0000269|PubMed:24045840, ECO:0000269|PubMed:24594635, ECO:0000269|PubMed:24806754, ECO:0000269|PubMed:9419367}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cholestasis of pregnancy, intrahepatic 3 (ICP3) [MIM:614972]: A liver disorder of pregnancy. It presents during the second or, more commonly, the third trimester of pregnancy with intense pruritus which becomes more severe with advancing gestation and cholestasis. It causes fetal distress, spontaneous premature delivery and intrauterine death. Patients have spontaneous and progressive disappearance of cholestasis after delivery. Cholestasis results from abnormal biliary transport from the liver into the small intestine. {ECO:0000269|PubMed:10767346, ECO:0000269|PubMed:12746424, ECO:0000269|PubMed:15077010}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Gallbladder disease 1 (GBD1) [MIM:600803]: One of the major digestive diseases. Gallstones composed of cholesterol (cholelithiasis) are the common manifestations in western countries. Most people with gallstones, however, remain asymptomatic through their lifetimes. {ECO:0000269|PubMed:11313316, ECO:0000269|PubMed:12891548, ECO:0000269|PubMed:22331132, ECO:0000269|PubMed:23533021, ECO:0000269|PubMed:24723470, ECO:0000269|Ref.2}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);breast;pancreas;lymph node;liver;colon;spleen;blood;brain; dorsal root ganglion;liver; 0.08478 0.40689 -0.545632343 20.02241095 3911.66291 12.36329 ABCB5 1.16623512959537e-23 0.0269929301328199 0.97300706986718 ATP binding cassette subfamily B member 5 FUNCTION: Drug efflux transporter present in a number of stem cells that acts as a regulator of cellular differentiation. Able to mediate efflux from cells of the rhodamine dye and of the therapeutic drug doxorubicin. Specifically present in limbal stem cells, where it plays a key role in corneal development and repair. {ECO:0000269|PubMed:12960149, ECO:0000269|PubMed:15205344, ECO:0000269|PubMed:15899824, ECO:0000269|PubMed:22306008}.; . TISSUE SPECIFICITY: Expressed by CD133-expressing progenitor cells among epidermal melanocytes (at protein level). Widely expressed with specific expression in pigment cells. Highly expressed in several malignant tissues: highly expressed in clinical melanomas, with low expression in normal skin. In melanoma, marks malignant melanoma-initiating cells (MMIC), in which clinical virulence resides as a consequence of unlimited self-renewal capacity, resulting in inexorable tumor progression and metastasis. Also highly expressed in a number of leukemia cells. Expressed in basal limbal epithelium. {ECO:0000269|PubMed:12960149, ECO:0000269|PubMed:15760339, ECO:0000269|PubMed:22044138, ECO:0000269|PubMed:22675422, ECO:0000269|PubMed:22784549, ECO:0000269|PubMed:23770371, ECO:0000269|PubMed:24934811, ECO:0000269|PubMed:25030174}.; testis;mammary gland;skin; dorsal root ganglion;ciliary ganglion;atrioventricular node; 0.14704 0.09307 4.176155702 99.69922151 9731.34505 21.45196 ABCB6 2.11132200307841e-17 0.0497999629480226 0.950200037051977 ATP binding cassette subfamily B member 6 (Langereis blood group) FUNCTION: Binds heme and porphyrins and functions in their ATP- dependent uptake into the mitochondria. Plays a crucial role in heme synthesis. {ECO:0000269|PubMed:10837493, ECO:0000269|PubMed:17006453}.; DISEASE: Microphthalmia, isolated, with coloboma, 7 (MCOPCB7) [MIM:614497]: A disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues. Ocular abnormalities like opacities of the cornea and lens, scaring of the retina and choroid, and other abnormalities may also be present. Ocular colobomas are a set of malformations resulting from abnormal morphogenesis of the optic cup and stalk, and the fusion of the fetal fissure (optic fissure). {ECO:0000269|PubMed:22226084}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dyschromatosis universalis hereditaria 3 (DUH3) [MIM:615402]: An autosomal dominant pigmentary genodermatosis characterized by a mixture of hyperpigmented and hypopigmented macules distributed randomly over the body, that appear in infancy or early childhood. The trunk and extremities are the dominant sites of abnormal pigmentation. Facial lesions can be seen in 50% of affected individuals, but involvement of palms and soles is unusual. Abnormalities of hair and nails have also been reported. Dyschromatosis universalis hereditaria may be associated with abnormalities of dermal connective tissue, nerve tissue, or other systemic complications. {ECO:0000269|PubMed:23519333, ECO:0000269|PubMed:24224009, ECO:0000269|PubMed:24498303, ECO:0000269|PubMed:25288164}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=ABCB6 mutations are involved in familial pseudohyperkalemia, a dominantly inherited condition characterized by increased serum potassium levels, measured in whole-blood specimens stored at or below room temperature. This condition is not accompanied by clinical symptoms or biological signs except for borderline abnormalities of red cell shape (PubMed:23180570). {ECO:0000269|PubMed:23180570}.; TISSUE SPECIFICITY: Widely expressed. High expression is detected in the retinal epithelium. {ECO:0000269|PubMed:10837493, ECO:0000269|PubMed:22226084}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;bone;iris;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;epidermis;islets of Langerhans;hypothalamus;muscle;urinary;pharynx;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; . 0.12419 . -0.369255208 28.25548478 401.03419 4.20102 ABCB7 0.995047822845297 0.00495207110968637 1.06045016059627e-07 ATP binding cassette subfamily B member 7 FUNCTION: Could be involved in the transport of heme from the mitochondria to the cytosol. Plays a central role in the maturation of cytosolic iron-sulfur (Fe/S) cluster-containing proteins.; DISEASE: Anemia, sideroblastic, spinocerebellar ataxia (ASAT) [MIM:301310]: A X-linked recessive disorder characterized by an infantile to early childhood onset of non-progressive cerebellar ataxia and mild anemia, with hypochromia and microcytosis. {ECO:0000269|PubMed:10196363, ECO:0000269|PubMed:11050011, ECO:0000269|PubMed:11843825, ECO:0000269|PubMed:22398176}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;parathyroid;choroid;skin;retina;uterus;prostate;whole body;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;cervix;kidney;stomach; superior cervical ganglion;tumor;globus pallidus;ciliary ganglion;white blood cells;trigeminal ganglion;fetal thyroid; 0.41712 0.51712 0.861712133 88.6883699 588.79282 4.91984 ABCB8 4.59594908795322e-06 0.990775898029607 0.00921950602130551 ATP binding cassette subfamily B member 8 . . TISSUE SPECIFICITY: Ubiquitous.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;whole body;optic nerve;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;lens;skeletal muscle;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; cerebellum peduncles;skeletal muscle; 0.19173 0.15536 0.295774947 71.64425572 1119.5958 6.38885 ABCB9 0.00290110755910397 0.984485544541478 0.0126133478994183 ATP binding cassette subfamily B member 9 FUNCTION: ATP-dependent low-affinity peptide transporter which translocates a broad spectrum of peptides from the cytosol to the lysosomal lumen. Displays a broad peptide length specificity from 6-mer up to at least 59-mer peptides with an optimum of 23-mers. Favors positively charged, aromatic or hydrophobic residues in the N- and C-terminal positions whereas negatively charged residues as well as asparagine and methionine are not favored. {ECO:0000269|PubMed:15863492, ECO:0000269|PubMed:17977821, ECO:0000269|PubMed:18434309}.; . TISSUE SPECIFICITY: Highly expressed in testis, and at moderate levels in brain, spinal cord, and thyroid. Not expressed in monocytes but strongly expressed during differentiation of monocytes to dendritic cells and macrophages. {ECO:0000269|PubMed:10748049, ECO:0000269|PubMed:17977821}.; unclassifiable (Anatomical System);medulla oblongata;ovary;fovea centralis;choroid;lens;skin;retina;bile duct;uterus;prostate;optic nerve;lung;placenta;macula lutea;visual apparatus;liver;testis;cervix;kidney;germinal center;mammary gland;brain;stomach; dorsal root ganglion;subthalamic nucleus;testis - interstitial;prefrontal cortex;testis;ciliary ganglion;caudate nucleus;trigeminal ganglion;parietal lobe; 0.26916 0.13285 -1.815166288 2.164425572 136.30539 2.53778 ABCB10 7.9478594059038e-06 0.915409281888748 0.0845827702518465 ATP binding cassette subfamily B member 10 FUNCTION: May mediate critical mitochondrial transport functions related to heme biosynthesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in bone marrow, expressed at intermediate to high levels in skeletal muscle, small intestine, thyroid, heart, brain, placenta, liver, pancreas, prostate, testis, ovary, leukocyte, stomach, spinal cord, lymph node, trachea and adrenal gland, and low levels are found in lung, kidney, spleen, thymus and colon.; . . 0.26156 0.14338 -0.134019284 43.90776126 272.32476 3.53756 ABCB10P1 . . . ATP binding cassette subfamily B member 10 pseudogene 1 . . . . . . . . . . . ABCB10P3 . . . ATP binding cassette subfamily B member 10 pseudogene 3 . . . . . . . . . . . ABCB10P4 . . . ATP binding cassette subfamily B member 10 pseudogene 4 . . . . . . . . . . . ABCB11 2.18849485467569e-10 0.998263926769702 0.00173607301144792 ATP binding cassette subfamily B member 11 FUNCTION: Involved in the ATP-dependent secretion of bile salts into the canaliculus of hepatocytes.; DISEASE: Cholestasis, progressive familial intrahepatic, 2 (PFIC2) [MIM:601847]: A disorder characterized by early onset of cholestasis that progresses to hepatic fibrosis, cirrhosis, and end-stage liver disease before adulthood. {ECO:0000269|PubMed:10579978, ECO:0000269|PubMed:11815775, ECO:0000269|PubMed:24969679, ECO:0000269|PubMed:9806540}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cholestasis, benign recurrent intrahepatic, 2 (BRIC2) [MIM:605479]: A disorder characterized by intermittent episodes of cholestasis without progression to liver failure. There is initial elevation of serum bile acids, followed by cholestatic jaundice which generally spontaneously resolves after periods of weeks to months. The cholestatic attacks vary in severity and duration. Patients are asymptomatic between episodes, both clinically and biochemically. {ECO:0000269|PubMed:15300568, ECO:0000269|PubMed:16039748}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly, if not exclusively in the liver, where it was further localized to the canalicular microvilli and to subcanalicular vesicles of the hepatocytes by in situ.; unclassifiable (Anatomical System);lung;liver; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10912 0.39265 -1.140954241 6.387119604 532.30214 4.70663 ABCC1 0.0194357604713981 0.980564228225471 1.13031306833206e-08 ATP binding cassette subfamily C member 1 FUNCTION: Mediates export of organic anions and drugs from the cytoplasm. Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o- glucuronide, methotrexate, antiviral drugs and other xenobiotics. Confers resistance to anticancer drugs. Hydrolyzes ATP with low efficiency. {ECO:0000269|PubMed:10064732, ECO:0000269|PubMed:11114332, ECO:0000269|PubMed:16230346}.; . TISSUE SPECIFICITY: Lung, testis and peripheral blood mononuclear cells.; unclassifiable (Anatomical System);medulla oblongata;lymph node;ovary;tongue;colon;skeletal muscle;bone marrow;prostate;pancreas;lung;adrenal gland;larynx;thyroid;visual apparatus;duodenum;hypopharynx;testis;amniotic fluid;cervix;head and neck;germinal center;brain;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.23396 . -0.841660883 11.29393725 348.41061 3.95626 ABCC2 3.36341398926312e-29 0.00281196265616683 0.997188037343833 ATP binding cassette subfamily C member 2 FUNCTION: Mediates hepatobiliary excretion of numerous organic anions. May function as a cellular cisplatin transporter.; . TISSUE SPECIFICITY: Expressed by polarized cells in liver, kidney and intestine. The highest expression is found in liver.; . . 0.10813 0.23913 0.955252644 90.09200283 1270.67962 6.71605 ABCC3 2.61612974200613e-14 0.989877187957038 0.0101228120429362 ATP binding cassette subfamily C member 3 FUNCTION: May act as an inducible transporter in the biliary and intestinal excretion of organic anions. Acts as an alternative route for the export of bile acids and glucuronides from cholestatic hepatocytes (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Mainly expressed in the liver. Also expressed in small intestine, colon, prostate, testis, brain and at a lower level in the kidney.; colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;oesophagus;endometrium;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;pancreas;adrenal gland;adrenal cortex;liver;trigeminal ganglion;skeletal muscle; 0.11549 0.27947 0.690669139 85.21467327 889.61134 5.81122 ABCC4 0.0013146830739273 0.998685202568288 1.14357784337428e-07 ATP binding cassette subfamily C member 4 FUNCTION: May be an organic anion pump relevant to cellular detoxification.; . TISSUE SPECIFICITY: Widely expressed, with particularly high levels in prostate, but is barely detectable in liver.; . . 0.17935 0.36953 0.214875663 67.72234017 1639.72468 7.48375 ABCC5 0.896205134921104 0.103794865055437 2.34595639057432e-11 ATP binding cassette subfamily C member 5 FUNCTION: Acts as a multispecific organic anion pump which can transport nucleotide analogs. {ECO:0000269|PubMed:10840050}.; . TISSUE SPECIFICITY: All isoforms are equally expressed in retina. {ECO:0000269|PubMed:17521428}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;synovium;larynx;bone;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;urinary;blood;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;prefrontal cortex;globus pallidus;caudate nucleus;pons;cingulate cortex;parietal lobe;skeletal muscle; 0.38723 0.35905 -1.967739992 1.816466148 80.81009 1.89955 ABCC5-AS1 . . . ABCC5 antisense RNA 1 . . . . . . . . . . . ABCC6 1.4545670403957e-06 0.999981859602571 1.6685830388736e-05 ATP binding cassette subfamily C member 6 FUNCTION: Isoform 1: May participate directly in the active transport of drugs into subcellular organelles or influence drug distribution indirectly. Transports glutathione conjugates as leukotriene-c4 (LTC4) and N-ethylmaleimide S-glutathione (NEM-GS). {ECO:0000269|PubMed:11880368}.; DISEASE: Pseudoxanthoma elasticum (PXE) [MIM:264800]: A multisystem disorder characterized by accumulation of mineralized and fragmented elastic fibers in the skin, vascular walls, and Burch membrane in the eye. Clinically, patients exhibit characteristic lesions of the posterior segment of the eye including peau d'orange, angioid streaks, and choroidal neovascularizations, of the skin including soft, ivory colored papules in a reticular pattern that predominantly affect the neck and large flexor surfaces, and of the cardiovascular system with peripheral and coronary arterial occlusive disease as well as gastrointestinal bleedings. {ECO:0000269|PubMed:10811882, ECO:0000269|PubMed:10835642, ECO:0000269|PubMed:10954200, ECO:0000269|PubMed:11427982, ECO:0000269|PubMed:11536079, ECO:0000269|PubMed:11702217, ECO:0000269|PubMed:15086542, ECO:0000269|PubMed:15098239, ECO:0000269|PubMed:15459974, ECO:0000269|PubMed:16086317, ECO:0000269|PubMed:17617515, ECO:0000269|PubMed:19339160, ECO:0000269|PubMed:20034067, ECO:0000269|PubMed:25615550}. Note=The disease is caused by mutations affecting the gene represented in this entry. Homozygous or compound heterozygous ABCC6 mutations have been found in the overwhelming majority of cases. Individuals carrying heterozygous mutations express limited manifestations of the pseudoxanthoma elasticum phenotype.; DISEASE: Arterial calcification of infancy, generalized, 2 (GACI2) [MIM:614473]: A severe autosomal recessive disorder characterized by calcification of the internal elastic lamina of muscular arteries and stenosis due to myointimal proliferation. The disorder is often fatal within the first 6 months of life because of myocardial ischemia resulting in refractory heart failure. {ECO:0000269|PubMed:22209248}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in kidney and liver. Very low expression in other tissues.; unclassifiable (Anatomical System);breast;medulla oblongata;lung;spinal cord;liver;colon;spleen;kidney;brain;skeletal muscle;stomach; dorsal root ganglion;fetal liver;superior cervical ganglion;cerebellum peduncles;liver;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.12510 . 0.626356326 83.53974994 2678.20897 9.73052 ABCC6P1 . . . ATP binding cassette subfamily C member 6 pseudogene 1 . . . . . . . . . . . ABCC6P2 . . . ATP binding cassette subfamily C member 6 pseudogene 2 . . . . . . 0.14579 . . . . ABCC8 3.93872340599153e-15 0.998700875995371 0.00129912400462509 ATP binding cassette subfamily C member 8 FUNCTION: Subunit of the beta-cell ATP-sensitive potassium channel (KATP). Regulator of ATP-sensitive K(+) channels and insulin release. {ECO:0000269|PubMed:24814349, ECO:0000269|PubMed:25720052}.; DISEASE: Leucine-induced hypoglycemia (LIH) [MIM:240800]: Rare cause of hypoglycemia and is described as a condition in which symptomatic hypoglycemia is provoked by high protein feedings. Hypoglycemia is also elicited by administration of oral or intravenous infusions of a single amino acid, leucine. {ECO:0000269|PubMed:15356046}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Familial hyperinsulinemic hypoglycemia 1 (HHF1) [MIM:256450]: Most common cause of persistent hypoglycemia in infancy. Unless early and aggressive intervention is undertaken, brain damage from recurrent episodes of hypoglycemia may occur. {ECO:0000269|PubMed:10202168, ECO:0000269|PubMed:10334322, ECO:0000269|PubMed:12364426, ECO:0000269|PubMed:12941782, ECO:0000269|PubMed:15562009, ECO:0000269|PubMed:15579781, ECO:0000269|PubMed:15807877, ECO:0000269|PubMed:16357843, ECO:0000269|PubMed:16429405, ECO:0000269|PubMed:24814349, ECO:0000269|PubMed:25720052, ECO:0000269|PubMed:8751851, ECO:0000269|PubMed:8923011, ECO:0000269|PubMed:9618169, ECO:0000269|PubMed:9769320}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, permanent neonatal (PNDM) [MIM:606176]: A rare form of diabetes distinct from childhood- onset autoimmune diabetes mellitus type 1. It is characterized by insulin-requiring hyperglycemia that is diagnosed within the first months of life. Permanent neonatal diabetes requires lifelong therapy. {ECO:0000269|PubMed:16613899, ECO:0000269|PubMed:16885549, ECO:0000269|PubMed:17213273, ECO:0000269|PubMed:17668386}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Transient neonatal diabetes mellitus 2 (TNDM2) [MIM:610374]: Neonatal diabetes is a form of diabetes mellitus defined by the onset of mild-to-severe hyperglycemia within the first months of life. Transient neonatal diabetes remits early, with a possible relapse during adolescence. {ECO:0000269|PubMed:16885549}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;heart;islets of Langerhans;bone;brain;mammary gland;skeletal muscle;cerebellum; whole brain;occipital lobe;superior cervical ganglion;cerebellum peduncles;beta cell islets;prefrontal cortex;parietal lobe;cerebellum; 0.15041 0.43468 -2.091107194 1.568766218 407.27264 4.23150 ABCC9 0.000700542902364641 0.999299454754885 2.34275090763438e-09 ATP binding cassette subfamily C member 9 FUNCTION: Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with KCNJ11. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation. {ECO:0000269|PubMed:9831708}.; DISEASE: Cardiomyopathy, dilated 1O (CMD1O) [MIM:608569]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:15034580}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Atrial fibrillation, familial, 12 (ATFB12) [MIM:614050]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:17245405}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hypertrichotic osteochondrodysplasia (HTOCD) [MIM:239850]: A rare disorder characterized by congenital hypertrichosis, neonatal macrosomia, a distinct osteochondrodysplasia, and cardiomegaly. The hypertrichosis leads to thick scalp hair, which extends onto the forehead, and a general increase in body hair. In addition, macrocephaly and coarse facial features, including a broad nasal bridge, epicanthal folds, a wide mouth, and full lips, can be suggestive of a storage disorder. About half of affected individuals are macrosomic and edematous at birth, whereas in childhood they usually have a muscular appearance with little subcutaneous fat. Thickened calvarium, narrow thorax, wide ribs, flattened or ovoid vertebral bodies, coxa valga, osteopenia, enlarged medullary canals, and metaphyseal widening of long bones have been reported. Cardiac manifestations such as patent ductus arteriosus, ventricular hypertrophy, pulmonary hypertension, and pericardial effusions are present in approximately 80% of cases. Motor development is usually delayed due to hypotonia. Most patients have a mild speech delay, and a small percentage have learning difficulties or intellectual disability. {ECO:0000269|PubMed:22608503, ECO:0000269|PubMed:22610116}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;whole body;frontal lobe;cartilage;liver;testis;brain;mammary gland;retina; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11236 0.15685 -1.967739992 1.816466148 117.11773 2.35297 ABCC10 8.30539108826425e-21 0.091415006773275 0.908584993226725 ATP binding cassette subfamily C member 10 FUNCTION: ATP-dependent transporter probably involved in cellular detoxification through lipophilic anion extrusion. {ECO:0000269|PubMed:12527806, ECO:0000269|PubMed:15256465}.; . TISSUE SPECIFICITY: Isoform 1 is specifically expressed in spleen. Isoform 2 is more widely expressed. {ECO:0000269|PubMed:12566991}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;brain;tonsil;unclassifiable (Anatomical System);cartilage;islets of Langerhans;lens;pancreas;lung;placenta;macula lutea;hypopharynx;cervix;head and neck;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.04246 . -1.705402241 2.512384996 2154.96315 8.54367 ABCC11 5.69831059947564e-25 0.00459725801097295 0.995402741989027 ATP binding cassette subfamily C member 11 FUNCTION: Participates in physiological processes involving bile acids, conjugated steroids and cyclic nucleotides. Enhances the cellular extrusion of cAMP and cGMP. Stimulates the ATP-dependent uptake of a range of physiological and synthetic lipophilic anions, including the glutathione S-conjugates leukotriene C4 and dinitrophenyl S-glutathione, steroid sulfates such as dehydroepiandrosterone 3-sulfate (DHEAS) and estrone 3-sulfate, glucuronides such as estradiol 17-beta-D-glucuronide (E(2)17betaG), the monoanionic bile acids glycocholate and taurocholate, and methotrexate. Probably functions to secrete earwax. {ECO:0000269|PubMed:12764137, ECO:0000269|PubMed:15537867, ECO:0000269|PubMed:16444273}.; . TISSUE SPECIFICITY: Expressed in many tissues. Not expressed in kidney, spleen and colon. Highly expressed in breast cancer. Expressed at moderate levels in normal breast and testis and at very low levels in liver, brain and placenta. {ECO:0000269|PubMed:11483364, ECO:0000269|PubMed:11591886}.; unclassifiable (Anatomical System);breast;prostate;liver;testis;colon;mammary gland; dorsal root ganglion;superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.22415 0.70109 1.624127851 96.03680113 7334.53101 18.42618 ABCC12 2.20535216082614e-26 0.00251272437646729 0.997487275623533 ATP binding cassette subfamily C member 12 FUNCTION: Probable transporter. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis (at protein level). Widely expressed at low level. Isoform 5 is specifically expressed in brain, testis and breast cancer cells. {ECO:0000269|PubMed:11483364, ECO:0000269|PubMed:11688999, ECO:0000269|PubMed:12011458}.; unclassifiable (Anatomical System);lung;testis; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.08005 0.09094 1.111434312 92.06770465 2688.47723 9.75984 ABCC13 . . . ATP binding cassette subfamily C member 13 (pseudogene) . . TISSUE SPECIFICITY: Highest expression in fetal liver and fetal spleen. In the adult, highest levels are found in the colon ascending and transverse. Also expressed in brain, placenta, lung, liver, pancreas and ovary. In bone marrow cells, levels are several fold higher than in peripheral blood leukocytes. {ECO:0000269|PubMed:12036298, ECO:0000269|PubMed:12445816, ECO:0000269|PubMed:15203202}.; . . 0.08540 . . . . . ABCD1 0.982118837885542 0.0178689981752655 1.21639391929071e-05 ATP binding cassette subfamily D member 1 FUNCTION: Probable transporter. The nucleotide-binding fold acts as an ATP-binding subunit with ATPase activity. {ECO:0000269|PubMed:11248239}.; DISEASE: Adrenoleukodystrophy (ALD) [MIM:300100]: A peroxisomal metabolic disorder characterized by progressive multifocal demyelination of the central nervous system and by peripheral adrenal insufficiency (Addison disease). It results in mental deterioration, corticospinal tract dysfunction, and cortical blindness. Different clinical manifestations exist like: cerebral childhood ALD (CALD), adult cerebral ALD (ACALD), adrenomyeloneuropathy (AMN) and 'Addison disease only' (ADO) phenotype. {ECO:0000269|PubMed:10369742, ECO:0000269|PubMed:10480364, ECO:0000269|PubMed:10737980, ECO:0000269|PubMed:10980539, ECO:0000269|PubMed:11438993, ECO:0000269|PubMed:11810273, ECO:0000269|PubMed:15643618, ECO:0000269|PubMed:21700483, ECO:0000269|PubMed:21889498, ECO:0000269|PubMed:7581394, ECO:0000269|PubMed:7717396, ECO:0000269|PubMed:7825602, ECO:0000269|PubMed:7849723, ECO:0000269|PubMed:7904210, ECO:0000269|PubMed:8040304, ECO:0000269|PubMed:8566952, ECO:0000269|PubMed:8651290, ECO:0000269|PubMed:9452087}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=The promoter region of ABCD1 is deleted in the chromosome Xq28 deletion syndrome which involves ABCD1 and the neighboring gene BCAP31. {ECO:0000269|PubMed:11992258}.; . unclassifiable (Anatomical System);lymph node;cartilage;ovary;colon;parathyroid;blood;choroid;skin;skeletal muscle;retina;pancreas;lung;adrenal gland;bone;placenta;alveolus;testis;cervix;kidney;brain;stomach; superior cervical ganglion;skeletal muscle; 0.44245 0.76942 -0.53631094 20.53550366 23.16292 0.77329 ABCD1P1 . . . ATP binding cassette subfamily D member 1 pseudogene 1 . . . . . . . . . . . ABCD1P2 . . . ATP binding cassette subfamily D member 1 pseudogene 2 . . . . . . . . . . . ABCD1P3 . . . ATP binding cassette subfamily D member 1 pseudogene 3 . . . . . . . . . . . ABCD1P4 . . . ATP binding cassette subfamily D member 1 pseudogene 4 . . . . . . . . . . . ABCD1P5 . . . ATP binding cassette subfamily D member 1 pseudogene 5 . . . . . . . . . . . ABCD2 2.96980747420595e-06 0.927390257425474 0.0726067727670515 ATP binding cassette subfamily D member 2 FUNCTION: Probable transporter.; . TISSUE SPECIFICITY: Predominantly expressed in brain and heart.; liver;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.08475 0.19889 -0.091746757 46.91554612 167.46052 2.82724 ABCD3 0.999695622624106 0.000304377374916198 9.775912709387e-13 ATP binding cassette subfamily D member 3 FUNCTION: Probable transporter involved in the transport of branched-chain fatty acids and C27 bile acids into the peroxisome; the latter function is a crucial step in bile acid biosynthesis (PubMed:25168382). The nucleotide-binding fold acts as an ATP- binding subunit with ATPase activity (PubMed:11248239). {ECO:0000269|PubMed:11248239, ECO:0000269|PubMed:25168382}.; DISEASE: Congenital bile acid synthesis defect 5 (CBAS5) [MIM:616278]: An autosomal recessive disorder characterized by hepatosplenomegaly, hepatic fibrosis, progressive liver failure, and accumulation of peroxisomal C27-bile acid intermediates in plasma. {ECO:0000269|PubMed:25168382}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;placenta;testis;kidney;skeletal muscle; amygdala;fetal liver;prefrontal cortex;trigeminal ganglion; 0.71463 0.29732 -0.646543901 16.44255721 34.49232 1.05301 ABCD4 1.39849213579456e-08 0.943627528579004 0.0563724574360747 ATP binding cassette subfamily D member 4 FUNCTION: May be involved in intracellular processing of vitamin B12 (cobalamin). Could play a role in the lysosomal release of vitamin B12 into the cytoplasm. {ECO:0000269|PubMed:22922874}.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;ovary;salivary gland;colon;parathyroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;spleen;cervix;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.14137 0.15259 0.804668134 87.71526303 5678.49686 15.58931 ABCE1 0.999982596858514 1.74031409388042e-05 5.47522732695943e-13 ATP binding cassette subfamily E member 1 FUNCTION: Antagonizes the binding of 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) by RNase L through direct interaction with RNase L and therefore inhibits its endoribonuclease activity. May play a central role in the regulation of mRNA turnover. Antagonizes the anti-viral effect of the interferon-regulated 2-5A/RNase L pathway. May act as a chaperone for post-translational events during HIV-1 capsid assembly. {ECO:0000269|PubMed:11585831, ECO:0000269|PubMed:9660177, ECO:0000269|PubMed:9847332}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;trigeminal ganglion; 0.54899 0.31462 -0.251530012 35.42108988 5.45332 0.20296 ABCF1 2.7302422835602e-06 0.999963882170263 3.33875874534099e-05 ATP binding cassette subfamily F member 1 FUNCTION: Isoform 2 is required for efficient Cap- and IRES- mediated mRNA translation initiation. Isoform 2 is not involved in the ribosome biogenesis. {ECO:0000269|PubMed:19570978}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9790762}.; lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;atrium;frontal lobe;endometrium;oesophagus;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;cerebellum cortex;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;cerebellum; 0.15350 . -0.222203495 37.54423213 246.17443 3.38532 ABCF2 0.995417497143895 0.00458249926364776 3.592457694508e-09 ATP binding cassette subfamily F member 2 . . . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;iris;testis;amniotic fluid;germinal center;brain;amygdala;unclassifiable (Anatomical System);lymph node;heart;cartilage;muscle;blood;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;thalamus;prefrontal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.31492 0.12016 -0.466531444 23.51380042 229.77785 3.27631 ABCF2P1 . . . ATP binding cassette subfamily F member 2 pseudogene 1 . . . . . . . . . . . ABCF2P2 . . . ATP binding cassette subfamily F member 2 pseudogene 2 . . . . . . . . . . . ABCF3 0.00402616582072083 0.995906699374651 6.71348046279091e-05 ATP binding cassette subfamily F member 3 FUNCTION: Displays an antiviral effect against flaviviruses such as west Nile virus (WNV) in the presence of OAS1B. {ECO:0000250}.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;mesenchyma;epididymis;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; medulla oblongata;superior cervical ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe; 0.57953 0.15513 -0.771553417 13.15168672 319.46185 3.79528 ABCG1 0.358875895364322 0.641016840300353 0.000107264335324722 ATP binding cassette subfamily G member 1 FUNCTION: Transporter involved in macrophage lipid homeostasis. Is an active component of the macrophage lipid export complex. Could also be involved in intracellular lipid transport processes. The role in cellular lipid homeostasis may not be limited to macrophages.; . TISSUE SPECIFICITY: Expressed in several tissues. Expressed in macrophages; expression is increased in macrophages from patients with Tangier disease. {ECO:0000269|PubMed:11350058}.; lymphoreticular;colon;parathyroid;retina;bone marrow;uterus;prostate;endometrium;larynx;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;blood;lens;lung;adrenal gland;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus;cerebellum; superior cervical ganglion;adrenal gland;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.09638 0.43722 -1.374132436 4.429110639 376.48662 4.09085 ABCG2 1.37099444079211e-18 0.00525441460805226 0.994745585391948 ATP binding cassette subfamily G member 2 (Junior blood group) FUNCTION: High-capacity urate exporter functioning in both renal and extrarenal urate excretion. Plays a role in porphyrin homeostasis as it is able to mediates the export of protoporhyrin IX (PPIX) both from mitochondria to cytosol and from cytosol to extracellular space, and cellular export of hemin, and heme. Xenobiotic transporter that may play an important role in the exclusion of xenobiotics from the brain. Appears to play a major role in the multidrug resistance phenotype of several cancer cell lines. Implicated in the efflux of numerous drugs and xenobiotics: mitoxantrone, the photosensitizer pheophorbide, camptothecin, methotrexate, azidothymidine (AZT), and the anthracyclines daunorubicin and doxorubicin. {ECO:0000269|PubMed:12958161, ECO:0000269|PubMed:20705604, ECO:0000269|PubMed:22132962, ECO:0000269|PubMed:23189181}.; . TISSUE SPECIFICITY: Highly expressed in placenta. Low expression in small intestine, liver and colon. {ECO:0000269|PubMed:9850061, ECO:0000269|PubMed:9861027}.; unclassifiable (Anatomical System);ovary;hypothalamus;parathyroid;skin;skeletal muscle;uterus;pancreas;prostate;lung;frontal lobe;cochlea;endometrium;epididymis;nasopharynx;placenta;hippocampus;liver;testis;head and neck;spleen;kidney;brain; superior cervical ganglion;placenta;ciliary ganglion; 0.07103 0.55212 -0.198338176 39.17197452 1369.17181 6.94178 ABCG4 0.000455417358401195 0.992033194592249 0.00751138804934938 ATP binding cassette subfamily G member 4 FUNCTION: May be involved in macrophage lipid homeostasis.; . TISSUE SPECIFICITY: Highly expressed in brain tissues with the exception of the spinal cord. {ECO:0000269|PubMed:11856881}.; ganglion;brain;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.18664 0.15734 -0.067881249 48.69072895 196.06202 3.02988 ABCG5 1.89797083861304e-15 0.00728710526367036 0.992712894736328 ATP binding cassette subfamily G member 5 FUNCTION: Transporter that appears to play an indispensable role in the selective transport of the dietary cholesterol in and out of the enterocytes and in the selective sterol excretion by the liver into bile.; . TISSUE SPECIFICITY: Strongly expressed in the liver, lower levels in the small intestine and colon.; unclassifiable (Anatomical System);optic nerve;lung;macula lutea;liver;spleen;fovea centralis;choroid;lens;stomach;retina; fetal liver;testis - interstitial;liver; 0.10278 0.08667 1.161078613 92.64567115 1949.89203 8.12614 ABCG8 3.74527259993631e-16 0.00539899742307175 0.994601002576928 ATP binding cassette subfamily G member 8 FUNCTION: Transporter that appears to play an indispensable role in the selective transport of the dietary cholesterol in and out of the enterocytes and in the selective sterol excretion by the liver into bile.; DISEASE: Sitosterolemia (STSL) [MIM:210250]: Rare autosomal recessive disorder characterized by increased intestinal absorption of all sterols including cholesterol, plant and shellfish sterols, and decreased biliary excretion of dietary sterols into bile. Sitosterolemia patients have hypercholesterolemia, very high levels of plant sterols in the plasma, and frequently develop tendon and tuberous xanthomas, accelerated atherosclerosis and premature coronary artery disease. {ECO:0000269|PubMed:11099417, ECO:0000269|PubMed:11452359}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Strongly expressed in the liver, lower levels in the small intestine and colon. Detectable in a wide variety of human tissues.; unclassifiable (Anatomical System);liver;spleen;skeletal muscle; . 0.13777 0.33303 0.744001103 86.37650389 6759.48039 17.46017 ABHD1 1.06027288753589e-21 2.07743455891404e-05 0.999979225654411 abhydrolase domain containing 1 . . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12735795}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; . 0.02466 0.08409 -0.110153916 45.48832272 1251.23626 6.67558 ABHD2 0.849463720274095 0.150426270846119 0.000110008879785845 abhydrolase domain containing 2 FUNCTION: May play a role in smooth muscle cells migration. {ECO:0000250}.; . . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;larynx;thyroid;bone;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hypopharynx;liver;head and neck;spleen;kidney;mammary gland;stomach; dorsal root ganglion;amygdala;testis - interstitial;superior cervical ganglion;prostate;testis - seminiferous tubule;liver;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.19174 0.12265 -0.025608647 51.91672564 42.87383 1.24066 ABHD3 1.33741470632214e-06 0.603635251375658 0.396363411209635 abhydrolase domain containing 3 FUNCTION: Phospholipase that may play a role in phospholipids remodeling. May selectively cleave myristate (C14)-containing phosphatidylcholines through its predominant phospholipase 1 activity, cleaving preferentially acyl groups in sn1 position. In parallel, may have a minor phospholipase 2 activity acting on acyl groups in position sn2. In addition to (C14)-containing phosphatidylcholines, may also act on other medium-chain- containing and oxidatively truncated phospholipids. {ECO:0000269|PubMed:21926997}.; . . ovary;colon;parathyroid;skin;uterus;whole body;frontal lobe;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pancreas;lung;placenta;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; . 0.57616 0.10262 -0.203796826 38.81811748 60.41464 1.58009 ABHD4 7.5061622204536e-05 0.9173005008146 0.0826244375631956 abhydrolase domain containing 4 FUNCTION: Lysophospholipase selective for N-acyl phosphatidylethanolamine (NAPE). Contributes to the biosynthesis of N-acyl ethanolamines, including the endocannabinoid anandamide by hydrolyzing the sn-1 and sn-2 acyl chains from N-acyl phosphatidylethanolamine (NAPE) generating glycerophospho-N-acyl ethanolamine (GP-NAE), an intermediate for N-acyl ethanolamine biosynthesis. Hydrolyzes substrates bearing saturated, monounsaturated, polyunsaturated N-acyl chains. Shows no significant activity towards other lysophospholipids, including lysophosphatidylcholine, lysophosphatidylethanolamine and lysophosphatidylserine (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;trophoblast;heart;cartilage;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;amnion;spleen;cervix;kidney; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node; 0.31924 0.11145 -0.979072682 8.752064166 27.3891 0.88292 ABHD5 3.45366245550968e-05 0.945149055491663 0.054816407883782 abhydrolase domain containing 5 FUNCTION: Lysophosphatidic acid acyltransferase which functions in phosphatidic acid biosynthesis (PubMed:18606822). May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2 (PubMed:16679289). Involved in keratinocyte differentiation (PubMed:18832586). Regulates lipid droplet fusion (By similarity). {ECO:0000250|UniProtKB:Q9DBL9, ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:18606822, ECO:0000269|PubMed:18832586}.; DISEASE: Chanarin-Dorfman syndrome (CDS) [MIM:275630]: An autosomal recessive inborn error of lipid metabolism with multisystemic accumulation of triglycerides although plasma concentrations are normal. Clinical characteristics are congenital generalized ichthyosis, vacuolated leukocytes, hepatomegaly, myopathy, cataracts, neurosensory hearing loss and developmental delay. The disorder presents at birth with generalized, fine, white scaling of the skin and a variable degree of erythema resembling non-bullous congenital ichthyosiform erythroderma. {ECO:0000269|PubMed:11590543, ECO:0000269|PubMed:17495960}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed in various tissues, including lymphocytes, liver, skeletal muscle and brain. Expressed by upper epidermal layers and dermal fibroblasts in skin, hepatocytes and neurons (at protein level). {ECO:0000269|PubMed:11590543, ECO:0000269|PubMed:18832586}.; ovary;colon;skin;bone marrow;uterus;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.10023 0.16275 -0.424258538 25.56027365 83.57795 1.94414 ABHD6 0.00255991600957779 0.932133869988273 0.065306214002149 abhydrolase domain containing 6 FUNCTION: Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol (PubMed:22969151). Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways. May also have a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (By similarity). {ECO:0000250|UniProtKB:Q8R2Y0, ECO:0000269|PubMed:22969151}.; . . ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;iris;pituitary gland;testis;dura mater;germinal center;brain;pineal gland;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;hypothalamus;breast;pancreas;pia mater;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach;cerebellum; whole brain;superior cervical ganglion;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;liver;parietal lobe;cingulate cortex;skeletal muscle;cerebellum; 0.04853 0.41860 -0.494039303 22.09247464 26.61177 0.86201 ABHD8 0.642340812644093 0.356316559695538 0.00134262766036873 abhydrolase domain containing 8 . . . medulla oblongata;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;adrenal cortex;lens;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum; amygdala;whole brain;medulla oblongata;subthalamic nucleus;temporal lobe;prefrontal cortex;cingulate cortex;cerebellum; 0.25898 0.11050 -0.203796826 38.81811748 863.32946 5.72740 ABHD10 0.000658971112003106 0.911518447915355 0.0878225809726424 abhydrolase domain containing 10 FUNCTION: Catalyzes the deglucuronidation of mycophenolic acid acyl-glucuronide, a metabolite of the immunosuppressant drug mycophenolate. {ECO:0000269|PubMed:22294686}.; . . colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;thyroid;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;adrenal cortex;skeletal muscle;bile duct;breast;lung;adrenal gland;placenta;hippocampus;liver;spleen;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;medulla oblongata;prefrontal cortex;caudate nucleus;kidney;trigeminal ganglion;cingulate cortex;skeletal muscle;parietal lobe; 0.06848 0.09963 0.595326758 82.66100495 53.5992 1.45693 ABHD11 9.03291221619057e-06 0.535113474482685 0.464877492605099 abhydrolase domain containing 11 . . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12073013}.; ovary;salivary gland;intestine;colon;skin;bone marrow;retina;uterus;prostate;endometrium;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.05918 0.10401 -0.404032746 26.53338051 137.53386 2.55215 ABHD11-AS1 . . . ABHD11 antisense RNA 1 (tail to tail) . . . . . . . . . . . ABHD12 1.98295570505197e-06 0.884464310611328 0.115533706432967 abhydrolase domain containing 12 FUNCTION: Lysophosphatidylserine (LPS) lipase that plays a key role in the central nervous system. Represents a major LPS lipase in the brain (By similarity). May also have a 2- arachidonoylglycerol (2-AG) hydrolase activity and act as a regulator of endocannabinoid signaling pathways. {ECO:0000250|UniProtKB:Q99LR1, ECO:0000269|PubMed:22969151, ECO:0000269|PubMed:24027063}.; DISEASE: Polyneuropathy, hearing loss, ataxia, retinitis pigmentosa, and cataract (PHARC) [MIM:612674]: A slowly progressive neurologic disorder with a variable phenotype resembling Refsum disease. Clinical features include sensorineural hearing loss, visual problems related to cataracts, retinitis pigmentosa, pes cavus, ataxic and/or spastic gait disturbances with a progressive sensorimotor peripheral neuropathy. Other features include hyporeflexia, hyperreflexia, extensor plantar responses. {ECO:0000269|PubMed:20797687, ECO:0000269|PubMed:22938382, ECO:0000269|PubMed:24027063}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;smooth muscle;ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;bone;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;muscle;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; whole brain;subthalamic nucleus;medulla oblongata;occipital lobe;hypothalamus;temporal lobe;pons;parietal lobe;cingulate cortex; 0.06962 . -0.157884861 42.05590941 209.86971 3.12687 ABHD12B 3.28064370577763e-13 0.00572108703932612 0.994278912960346 abhydrolase domain containing 12B . . . unclassifiable (Anatomical System);optic nerve;visual apparatus;skin;retina; . 0.05187 0.08315 1.039913547 91.25973107 4353.14362 13.15893 ABHD13 0.637356652288557 0.355950155422842 0.00669319228860032 abhydrolase domain containing 13 . . . . . 0.10818 0.11262 -0.317668748 31.45789101 14.35294 0.51825 ABHD14A 0.000234514195858804 0.51762898851668 0.482136497287461 abhydrolase domain containing 14A FUNCTION: Possible role in granule neuron development. {ECO:0000250}.; . . ovary;parathyroid;fovea centralis;choroid;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;pituitary gland;iris;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; whole brain;superior cervical ganglion;medulla oblongata;cerebellum peduncles;globus pallidus;kidney;pons;atrioventricular node;caudate nucleus;parietal lobe;cingulate cortex;cerebellum; 0.04602 0.08379 0.773521534 87.06062751 569.75218 4.84128 ABHD14A-ACY1 2.24506546646095e-05 0.907764805805396 0.0922127435399397 ABHD14A-ACY1 readthrough . . . . . 0.08140 . . . 183.99327 2.94419 ABHD14B 0.116162846197975 0.778766636561323 0.105070517240702 abhydrolase domain containing 14B FUNCTION: Has hydrolase activity towards p-nitrophenyl butyrate (in vitro). May activate transcription. {ECO:0000269|PubMed:14672934}.; . TISSUE SPECIFICITY: Ubiquitous. Detected in spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocyte, heart, placenta, lung, liver, skeletal muscle, pancreas and kidney. {ECO:0000269|PubMed:14672934}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; liver;kidney; 0.24544 0.08940 0.215080721 67.91696155 140.56801 2.58706 ABHD15 0.00179012571573465 0.898430434579398 0.0997794397048675 abhydrolase domain containing 15 . . . umbilical cord;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;synovium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pineal body;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;trigeminal ganglion; . . -0.246069119 36.06982779 257.51927 3.45167 ABHD15-AS1 . . . ABHD15 antisense RNA 1 . . . . . . . . . . . ABHD16A 0.988882578133094 0.0111174155114859 6.35541997449673e-09 abhydrolase domain containing 16A . . . . . 0.25299 0.10682 -0.336073593 30.55555556 331.75038 3.87258 ABHD16B 0.0330929687901713 0.820444475237819 0.146462555972009 abhydrolase domain containing 16B . . . . . 0.17786 . . . 749.26079 5.42981 ABHD17A 0.0505568745094196 0.860043678141682 0.0893994473488985 abhydrolase domain containing 17A . . . . . . 0.11236 . . 106.70342 2.24142 ABHD17AP1 . . . abhydrolase domain containing 17A pseudogene 1 . . . . . 0.11885 0.11056 . . . . ABHD17AP3 . . . abhydrolase domain containing 17A pseudogene 3 . . . . . . . . . . . ABHD17AP4 . . . abhydrolase domain containing 17A pseudogene P4 . . . . . . . . . . . ABHD17AP5 . . . abhydrolase domain containing 17A pseudogene 5 . . . . . . 0.10989 . . . . ABHD17AP6 . . . abhydrolase domain containing 17A pseudogene 6 . . . . . . . . . . . ABHD17AP7 . . . abhydrolase domain containing 17A pseudogene 7 . . . . . . . . . . . ABHD17AP8 . . . abhydrolase domain containing 17A pseudogene 8 . . . . . . . . . . . ABHD17AP9 . . . abhydrolase domain containing 17A pseudogene 9 . . . . . . . . . . . ABHD17B 0.961448199081918 0.0384706039501616 8.11969679202434e-05 abhydrolase domain containing 17B . . . . . 0.54710 0.11262 -0.339715008 30.06605331 13.7874 0.50102 ABHD17C 0.84082862967754 0.156183588278601 0.00298778204385854 abhydrolase domain containing 17C . . . . . 0.16351 0.10439 . . 3.26444 0.11817 ABHD18 . . . abhydrolase domain containing 18 . . . . . 0.04346 . 0.549415813 81.38122199 . . ABI1 0.632775183188113 0.367164391380334 6.04254315526191e-05 abl interactor 1 FUNCTION: May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. May play a role in regulation of EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons. {ECO:0000269|PubMed:11003655, ECO:0000269|PubMed:18328268}.; DISEASE: Note=A chromosomal aberration involving ABI1 is a cause of acute leukemias. Translocation t(10;11)(p11.2;q23) with KMT2A/MLL1. ABI1 isoform 2 was found to be present in acute leukemia KMT2A/MLL1-ABI1 fusion transcript. {ECO:0000269|PubMed:9694699}.; TISSUE SPECIFICITY: Widely expressed, with highest expression in brain. {ECO:0000269|PubMed:11418237}.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;larynx;bone;testis;dura mater;spinal ganglion;artery;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;pia mater;cornea;mesenchyma;nasopharynx;placenta;head and neck;kidney;stomach;aorta; amygdala;superior cervical ganglion;occipital lobe;prefrontal cortex;whole blood; 0.52357 0.29688 -0.315847836 31.68789809 53.85297 1.46346 ABI1P1 . . . abl-interactor 1 pseudogene 1 . . . . . . . . . . . ABI2 0.953329215745317 0.0466653979151567 5.38633952657031e-06 abl-interactor 2 FUNCTION: May act in regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. Regulates ABL1/c-Abl-mediated phosphorylation of MENA. {ECO:0000269|PubMed:10498863, ECO:0000269|PubMed:7590236, ECO:0000269|PubMed:8649853}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;prostate;whole body;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;tongue;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;cervix;head and neck;spleen;kidney;stomach; amygdala;dorsal root ganglion;testis - interstitial;superior cervical ganglion;occipital lobe;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.48964 0.19195 -0.361761279 28.6329323 21.65188 0.72894 ABI3 0.0277110067491567 0.921540701385427 0.0507482918654161 ABI family member 3 FUNCTION: May inhibit tumor metastasis (By similarity). In vitro, reduces cell motility. {ECO:0000250, ECO:0000269|PubMed:11956071}.; . TISSUE SPECIFICITY: Expressed in heart, lung, liver, pancreas, kidney, placenta and at low levels in brain and skeletal muscle. {ECO:0000269|PubMed:10978530}.; unclassifiable (Anatomical System);smooth muscle;colon;fovea centralis;choroid;lens;skeletal muscle;retina;pancreas;prostate;optic nerve;lung;bone;thyroid;placenta;macula lutea;pituitary gland;testis;spleen;germinal center;kidney;brain;tonsil;stomach; . 0.29455 0.12388 -0.025608647 51.91672564 1174.11094 6.50843 ABI3BP 3.9401554209396e-07 0.999977583514411 2.20224700472546e-05 ABI family member 3 binding protein . . TISSUE SPECIFICITY: Expressed in brain, heart, lung, liver, pancreas kidney and placenta. {ECO:0000269|PubMed:11501947}.; smooth muscle;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;larynx;thyroid;bone;testis;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;nervous;blood;lens;skeletal muscle;pancreas;lung;placenta;head and neck;kidney;mammary gland;stomach;aorta; ciliary ganglion; 0.18580 0.10024 0.45374373 78.05496579 4357.86877 13.16352 ABL1 0.999882701417156 0.000117298571282097 1.15622433940222e-11 ABL proto-oncogene 1, non-receptor tyrosine kinase FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage- induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 acts also as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin- associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. {ECO:0000269|PubMed:10391250, ECO:0000269|PubMed:11971963, ECO:0000269|PubMed:12379650, ECO:0000269|PubMed:12531427, ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:15556646, ECO:0000269|PubMed:15657060, ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:16424036, ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:16943190, ECO:0000269|PubMed:17306540, ECO:0000269|PubMed:17623672, ECO:0000269|PubMed:18328268, ECO:0000269|PubMed:18945674, ECO:0000269|PubMed:19891780, ECO:0000269|PubMed:20357770, ECO:0000269|PubMed:20417104, ECO:0000269|PubMed:9037071, ECO:0000269|PubMed:9144171, ECO:0000269|PubMed:9461559}.; DISEASE: Leukemia, chronic myeloid (CML) [MIM:608232]: A clonal myeloproliferative disorder of a pluripotent stem cell with a specific cytogenetic abnormality, the Philadelphia chromosome (Ph), involving myeloid, erythroid, megakaryocytic, B-lymphoid, and sometimes T-lymphoid cells, but not marrow fibroblasts. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Note=A chromosomal aberration involving ABL1 has been found in patients with chronic myeloid leukemia. Translocation t(9;22)(q34;q11) with BCR. The translocation produces a BCR-ABL found also in acute myeloid leukemia (AML) and acute lymphoblastic leukemia (ALL).; TISSUE SPECIFICITY: Widely expressed.; prostate;lung;placenta;skin; superior cervical ganglion; 0.99317 0.60884 -1.629711314 2.854446803 164.30123 2.79881 ABL2 0.00970257687397593 0.990293633644296 3.78948172840429e-06 ABL proto-oncogene 2, non-receptor tyrosine kinase FUNCTION: Non-receptor tyrosine-protein kinase that plays an ABL1- overlapping role in key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion and receptor endocytosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like MYH10 (involved in movement); CTTN (involved in signaling); or TUBA1 and TUBB (microtubule subunits). Binds directly F-actin and regulates actin cytoskeletal structure through its F-actin- bundling activity. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as CRK, CRKL, DOK1 or ARHGAP35. Adhesion-dependent phosphorylation of ARHGAP35 promotes its association with RASA1, resulting in recruitment of ARHGAP35 to the cell periphery where it inhibits RHO. Phosphorylates multiple receptor tyrosine kinases like PDGFRB and other substrates which are involved in endocytosis regulation such as RIN1. In brain, may regulate neurotransmission by phosphorylating proteins at the synapse. ABL2 acts also as a regulator of multiple pathological signaling cascades during infection. Pathogens can highjack ABL2 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. {ECO:0000269|PubMed:15735735, ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:17306540, ECO:0000269|PubMed:18945674}.; . TISSUE SPECIFICITY: Widely expressed.; unclassifiable (Anatomical System);cartilage;heart;salivary gland;adrenal cortex;skin;skeletal muscle;uterus;breast;prostate;lung;frontal lobe;bone;visual apparatus;hippocampus;liver;testis;spleen;amniotic fluid;kidney;brain;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.88710 0.21266 -0.992035476 8.604623732 182.10584 2.93109 ABLIM1 0.951991965239091 0.048008025066062 9.6948464724981e-09 actin binding LIM protein 1 FUNCTION: May act as scaffold protein (By similarity). May play a role in the development of the retina. Has been suggested to play a role in axon guidance. {ECO:0000250, ECO:0000269|PubMed:9245787}.; . TISSUE SPECIFICITY: Detected in liver, heart, skeletal muscle, brain and retina, where it is concentrated in the inner segment and in the outer plexiform layers. {ECO:0000269|PubMed:9245787}.; ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;lacrimal gland;islets of Langerhans;hypothalamus;oral cavity;bile duct;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; superior cervical ganglion;cerebellum peduncles;trigeminal ganglion;cerebellum; 0.24692 0.11524 -0.24061166 36.28214201 426.69086 4.31466 ABLIM2 0.762415766797037 0.237583577505149 6.55697813706998e-07 actin binding LIM protein family member 2 FUNCTION: May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity. {ECO:0000269|PubMed:17194709}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle. {ECO:0000269|PubMed:17194709}.; unclassifiable (Anatomical System);ovary;tongue;islets of Langerhans;sympathetic chain;colon;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;pancreas;prostate;optic nerve;whole body;lung;endometrium;macula lutea;liver;cervix;head and neck;spleen;kidney;brain;aorta; superior cervical ganglion;parietal lobe;skeletal muscle; 0.23624 0.10583 -1.506435464 3.544468035 74.03715 1.79760 ABLIM3 0.0160253493614536 0.983972835500536 1.81513801039822e-06 actin binding LIM protein family member 3 FUNCTION: May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity. {ECO:0000269|PubMed:17194709}.; . TISSUE SPECIFICITY: Expressed predominantly in heart and brain. {ECO:0000269|PubMed:17194709}.; myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;spinal cord;lens;skeletal muscle;breast;lung;placenta;visual apparatus;macula lutea;liver;spleen;kidney;aorta;stomach;peripheral nerve;thymus; dorsal root ganglion;subthalamic nucleus;adipose tissue;cerebellum peduncles;placenta;globus pallidus;cingulate cortex;cerebellum; 0.44749 0.10843 -1.150005948 6.286860109 169.47144 2.84089 ABO . . . ABO blood group (transferase A, alpha 1-3-N-acetylgalactosaminyltransferase; transferase B, alpha 1-3-galactosyltransferase) FUNCTION: This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.; . . . . 0.13273 0.82949 . . . . ABR 0.999949479085503 5.05209130115113e-05 1.485668146709e-12 active BCR-related FUNCTION: GTPase-activating protein for RAC and CDC42. Promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them.; . TISSUE SPECIFICITY: Highly enriched in the brain. Much weaker expression in heart, lung and muscle.; lymphoreticular;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;brain;tonsil;amygdala;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;peripheral nerve;colon;choroid;fovea centralis;uterus;whole body;oesophagus;bone;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;adrenal gland;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus; amygdala;whole brain;medulla oblongata;thalamus;occipital lobe;superior cervical ganglion;hypothalamus;temporal lobe;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.59342 . -1.03976177 7.802547771 211.79342 3.13829 ABRA 4.06005533531396e-06 0.376711739955722 0.623284199988943 actin binding Rho activating protein FUNCTION: Acts as an activator of serum response factor (SRF)- dependent transcription possibly by inducing nuclear translocation of MKL1 or MKL2 and through a mechanism requiring Rho-actin signaling. {ECO:0000250|UniProtKB:Q8BUZ1}.; . . heart;trabecular meshwork;liver;alveolus;skeletal muscle; dorsal root ganglion;testis - interstitial;testis;atrioventricular node;skeletal muscle; 0.13072 0.11727 -0.201976964 38.98325077 236.44111 3.32092 ABRACL 0.267692921991043 0.636499412701963 0.0958076653069933 ABRA C-terminal like . . . . . 0.73253 0.09747 0.035072054 56.2514744 5.13654 0.19042 ABT1 0.0271055673799205 0.793221171103215 0.179673261516864 activator of basal transcription 1 FUNCTION: Could be a novel TATA-binding protein (TBP) which can function as a basal transcription activator. Can act as a regulator of basal transcription for class II genes (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;iris;germinal center;brain;heart;cartilage;tongue;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; heart;placenta;testis;white blood cells; 0.36988 0.11250 -0.271755481 34.31823543 111.4994 2.29947 ABT1P1 . . . activator of basal transcription 1 pseudogene 1 . . . . . . . . . . . ABTB1 0.00129830665139568 0.990484558316784 0.00821713503182037 ankyrin repeat and BTB domain containing 1 FUNCTION: May act as a mediator of the PTEN growth-suppressive signaling pathway. May play a role in developmental processes. {ECO:0000269|PubMed:10891360, ECO:0000269|PubMed:11494141}.; . TISSUE SPECIFICITY: Ubiquitously expressed in all fetal tissues examined including heart, brain, liver, and kidney. Also expressed at lower levels in both adult heart and hypertrophic heart. {ECO:0000269|PubMed:10891360}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve;thymus; superior cervical ganglion;subthalamic nucleus;cerebellum peduncles;globus pallidus;caudate nucleus;atrioventricular node;pons;whole blood;cerebellum; 0.16173 0.11327 -0.951568548 9.271054494 77.50912 1.85236 ABTB2 0.124650440326371 0.875306745419216 4.28142544122237e-05 ankyrin repeat and BTB domain containing 2 FUNCTION: May be involved in the initiation of hepatocyte growth. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;muscle;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;kidney;stomach;peripheral nerve;cerebellum; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.42150 0.10744 -1.01227212 8.174097665 1552.92717 7.30342 ACAA1 2.6382494578646e-05 0.923671789709145 0.0763018277962767 acetyl-CoA acyltransferase 1 . . . ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;cornea;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;liver;ciliary ganglion;pons;kidney;trigeminal ganglion; 0.07126 0.69540 0.064394823 58.84642604 1342.80459 6.87964 ACAA2 0.0035080415350425 0.952684652329053 0.0438073061359047 acetyl-CoA acyltransferase 2 FUNCTION: Abolishes BNIP3-mediated apoptosis and mitochondrial damage. {ECO:0000269|PubMed:18371312}.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;gum;thyroid;iris;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;testis;dura mater;unclassifiable (Anatomical System);meninges;bile duct;pancreas;lung;pia mater;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; fetal liver;superior cervical ganglion;liver;globus pallidus;ciliary ganglion;atrioventricular node;kidney; 0.17491 0.36635 -0.578583623 18.71903751 396.13986 4.18062 ACACA 0.99999999994361 5.63897032153156e-11 1.32405580579083e-32 acetyl-CoA carboxylase alpha FUNCTION: Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. {ECO:0000269|PubMed:20952656}.; DISEASE: Acetyl-CoA carboxylase 1 deficiency (ACACAD) [MIM:613933]: An inborn error of de novo fatty acid synthesis associated with severe brain damage, persistent myopathy and poor growth. {ECO:0000269|PubMed:6114432}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, placental, skeletal muscle, renal, pancreatic and adipose tissues; expressed at low level in pulmonary tissue; not detected in the liver.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;oral cavity;muscle;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;aorta; thalamus;prostate;superior cervical ganglion;subthalamic nucleus;occipital lobe;adipose tissue;cerebellum peduncles;hypothalamus;prefrontal cortex;atrioventricular node;cingulate cortex; 0.46791 0.73160 -1.613071123 2.960603916 151.5075 2.69102 ACACB 5.12432725817776e-22 0.999983957399087 1.60426009125592e-05 acetyl-CoA carboxylase beta FUNCTION: Catalyzes the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. Involved in inhibition of fatty acid and glucose oxidation and enhancement of fat storage (By similarity). May play a role in regulation of mitochondrial fatty acid oxidation through malonyl- CoA-dependent inhibition of carnitine palmitoyltransferase 1 (By similarity). {ECO:0000250|UniProtKB:E9Q4Z2, ECO:0000269|PubMed:20952656}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in heart, skeletal muscle, liver, adipose tissue, mammary gland, adrenal gland and colon (PubMed:9099716). Isoform 3 is expressed in skeletal muscle, adipose tissue and liver (at protein level) (PubMed:19190759). Isoform 3 is detected at high levels in adipose tissue with lower levels in heart, liver, skeletal muscle and testis (PubMed:19190759). {ECO:0000269|PubMed:19190759, ECO:0000269|PubMed:9099716}.; unclassifiable (Anatomical System);lymph node;ovary;tongue;islets of Langerhans;sympathetic chain;colon;skin;retina;breast;uterus;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;visual apparatus;liver;head and neck;spleen;germinal center;kidney;brain;mammary gland;stomach; superior cervical ganglion;medulla oblongata;adipose tissue;liver;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16354 0.41174 -1.974635129 1.775182826 3979.35991 12.47962 ACAD8 1.16610074814559e-05 0.94700564047016 0.0529826985223586 acyl-CoA dehydrogenase family member 8 FUNCTION: Has very high activity toward isobutyryl-CoA. Is an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Plays a role in transcriptional coactivation within the ARC complex. {ECO:0000269|PubMed:12359132}.; . TISSUE SPECIFICITY: Detected at comparable levels in all tissues examined (heart, lung, brain, skeletal muscle, pancreas and placenta). Weakly expressed in liver and kidney.; ovary;salivary gland;developmental;intestine;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;iris;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;kidney;skeletal muscle; 0.02167 0.24964 -0.380166007 27.88393489 100.42016 2.17093 ACAD9 2.07158412910707e-05 0.994684435615835 0.00529484854287403 acyl-CoA dehydrogenase family member 9 FUNCTION: Required for mitochondrial complex I assembly (PubMed:20816094, PubMed:24158852). Has a dehydrogenase activity on palmitoyl-CoA (C16:0) and stearoyl-CoA (C18:0). It is three times more active on palmitoyl-CoA than on stearoyl-CoA. However, it does not play a primary role in long-chain fatty acid oxidation in vivo (PubMed:20816094, PubMed:24158852). Has little activity on octanoyl-CoA (C8:0), butyryl-CoA (C4:0) or isovaleryl-CoA (5:0). {ECO:0000269|PubMed:20816094, ECO:0000269|PubMed:24158852}.; . TISSUE SPECIFICITY: Ubiquitously expressed in most normal human tissues and cancer cell lines with high level of expression in heart, skeletal muscles, brain, kidney and liver. {ECO:0000269|PubMed:12359260}.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;spinal cord;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;lung;placenta;hypopharynx;head and neck;kidney;stomach;thymus; superior cervical ganglion;globus pallidus; 0.10391 0.22317 -0.841329384 11.36470866 169.80885 2.84303 ACAD10 4.01457480802773e-20 0.0631091758662963 0.936890824133704 acyl-CoA dehydrogenase family member 10 FUNCTION: Acyl-CoA dehydrogenase only active with R- and S-2- methyl-C15-CoA. {ECO:0000269|PubMed:21237683}.; . TISSUE SPECIFICITY: Widely expressed with highest expression in fetal brain, followed by heart, muscle, kidney and adult brain. Expression levels varying from isoform to isoform. {ECO:0000269|PubMed:15560374, ECO:0000269|PubMed:21237683}.; unclassifiable (Anatomical System);ovary;heart;hypothalamus;salivary gland;pharynx;colon;blood;skin;breast;prostate;lung;frontal lobe;endometrium;bone;visual apparatus;liver;cervix;spleen;kidney;spinal ganglion;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.02150 0.49463 -0.538378753 20.05189903 958.90541 5.99536 ACAD11 1.67704087843789e-07 0.998174159812799 0.00182567248311335 acyl-CoA dehydrogenase family member 11 FUNCTION: Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA. {ECO:0000269|PubMed:21237683}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in brain followed by liver, heart and kidney. {ECO:0000269|PubMed:21237683}.; smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;bone;germinal center;pineal gland;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;small intestine;heart;cartilage;lacrimal gland;islets of Langerhans;muscle;adrenal cortex;blood;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;peripheral nerve; . . 0.20501 0.604424343 82.90280727 772.2298 5.50015 ACADL 3.5917982569485e-08 0.542970324488801 0.457029639593217 acyl-CoA dehydrogenase, long chain . DISEASE: Acyl-CoA dehydrogenase very long-chain deficiency (ACADVLD) [MIM:201475]: An inborn error of mitochondrial fatty acid beta-oxidation which leads to impaired long-chain fatty acid beta-oxidation. It is clinically heterogeneous, with three major phenotypes: a severe childhood form characterized by early onset, high mortality and high incidence of cardiomyopathy; a milder childhood form with later onset, characterized by hypoketotic hypoglycemia, low mortality and rare cardiomyopathy; an adult form, with isolated skeletal muscle involvement, rhabdomyolysis and myoglobinuria, usually triggered by exercise or fasting. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);medulla oblongata;prostate;lung;cerebral cortex;bone;placenta;liver;testis;cervix;spleen;kidney;skeletal muscle; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.06718 0.32629 -0.358119787 29.16371786 2093.29217 8.42773 ACADM 8.44476503475977e-10 0.268163092804141 0.731836906351382 acyl-CoA dehydrogenase, C-4 to C-12 straight chain FUNCTION: Acyl-CoA dehydrogenase specific for acyl chain lengths of 4 to 16 that catalyzes the initial step of fatty acid beta- oxidation. Utilizes the electron transfer flavoprotein (ETF) as an electron acceptor to transfer electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). {ECO:0000269|PubMed:25416781}.; DISEASE: Acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:201450]: An inborn error of mitochondrial fatty acid beta- oxidation which causes fasting hypoglycemia, hepatic dysfunction and encephalopathy, often resulting in death in infancy. {ECO:0000269|PubMed:10767181, ECO:0000269|PubMed:11349232, ECO:0000269|PubMed:11409868, ECO:0000269|PubMed:11486912, ECO:0000269|PubMed:1671131, ECO:0000269|PubMed:1684086, ECO:0000269|PubMed:1902818, ECO:0000269|PubMed:2251268, ECO:0000269|PubMed:2393404, ECO:0000269|PubMed:2394825, ECO:0000269|PubMed:7603790, ECO:0000269|PubMed:7929823, ECO:0000269|PubMed:8198141, ECO:0000269|PubMed:9158144}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.15704 0.72174 -0.247889024 35.98726115 43.76588 1.25961 ACADS 0.000162910285908926 0.878896083920661 0.12094100579343 acyl-CoA dehydrogenase, C-2 to C-3 short chain FUNCTION: Introduces a double bond at position 2 in saturated acyl-CoA's of short chain length, i.e. less than 6 carbon atoms. {ECO:0000250|UniProtKB:P15651}.; DISEASE: Acyl-CoA dehydrogenase short-chain deficiency (ACADSD) [MIM:201470]: An inborn error of mitochondrial fatty acid beta- oxidation resulting in acute acidosis and muscle weakness in infants, and a form of lipid-storage myopathy in adults. {ECO:0000269|PubMed:11134486, ECO:0000269|PubMed:1692038, ECO:0000269|PubMed:9499414}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);medulla oblongata;cartilage;heart;ovary;muscle;colon;choroid;lens;skin;skeletal muscle;bone marrow;uterus;pancreas;prostate;lung;bone;placenta;visual apparatus;liver;testis;spleen;kidney;brain;stomach; superior cervical ganglion;liver;globus pallidus;atrioventricular node;skeletal muscle; 0.21732 0.52588 -0.200157416 39.11299835 1714.58162 7.63308 ACADSB 2.98832226560367e-08 0.301001538680302 0.698998431436475 acyl-CoA dehydrogenase, short/branched chain FUNCTION: Has greatest activity toward short branched chain acyl- CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl- CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.50662 0.27521 -0.402212257 26.7338995 1017.15986 6.13626 ACADVL 1.31058372898069e-07 0.944474873499744 0.0555249954418828 acyl-CoA dehydrogenase, very long chain FUNCTION: Active toward esters of long-chain and very long chain fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA. Can accommodate substrate acyl chain lengths as long as 24 carbons, but shows little activity for substrates of less than 12 carbons. {ECO:0000269|PubMed:18227065}.; DISEASE: Acyl-CoA dehydrogenase very long-chain deficiency (ACADVLD) [MIM:201475]: An inborn error of mitochondrial fatty acid beta-oxidation which leads to impaired long-chain fatty acid beta-oxidation. It is clinically heterogeneous, with three major phenotypes: a severe childhood form characterized by early onset, high mortality and high incidence of cardiomyopathy; a milder childhood form with later onset, characterized by hypoketotic hypoglycemia, low mortality and rare cardiomyopathy; an adult form, with isolated skeletal muscle involvement, rhabdomyolysis and myoglobinuria, usually triggered by exercise or fasting. {ECO:0000269|PubMed:10077518, ECO:0000269|PubMed:8554073, ECO:0000269|PubMed:9546340}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;salivary gland;colon;choroid;uterus;whole body;larynx;synovium;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;placenta;hippocampus;hypopharynx;amnion;head and neck;kidney;stomach;aorta;cerebellum; adrenal gland;adrenal cortex;skeletal muscle; 0.09093 0.28643 0.025760883 55.78556263 459.50732 4.44802 ACAN 0.999993944546979 6.05545301955806e-06 1.71315417297619e-15 aggrecan FUNCTION: This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region.; DISEASE: Spondyloepiphyseal dysplasia type Kimberley (SEDK) [MIM:608361]: Spondyloepiphyseal dysplasias are a heterogeneous group of congenital chondrodysplasias that specifically affect epiphyses and vertebrae. The autosomal dominant SEDK is associated with premature degenerative arthropathy. {ECO:0000269|PubMed:16080123}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spondyloepimetaphyseal dysplasia aggrecan type (SEMD- ACAN) [MIM:612813]: A bone disease characterized by severe short stature, macrocephaly, severe midface hypoplasia, short neck, barrel chest and brachydactyly. The radiological findings comprise long bones with generalized irregular epiphyses with widened metaphyses, especially at the knees, platyspondyly, and multiple cervical-vertebral clefts. {ECO:0000269|PubMed:19110214}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteochondritis dissecans short stature and early-onset osteoarthritis (OD) [MIM:165800]: A type of osteochondritis defined as a separation of cartilage and subchondral bone from the surrounding tissue, primarily affecting the knee, ankle and elbow joints. It is clinically characterized by multiple osteochondritic lesions in knees and/or hips and/or elbows, disproportionate short stature and early-onset osteoarthritis. {ECO:0000269|PubMed:20137779}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Restricted to cartilages. {ECO:0000269|PubMed:7524681}.; unclassifiable (Anatomical System);ovary;cartilage;adrenal cortex;colon;parathyroid;fovea centralis;choroid;lens;retina;uterus;optic nerve;whole body;lung;placenta;bone;macula lutea;visual apparatus;testis;head and neck;brain;stomach; superior cervical ganglion;trachea;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.34070 0.57020 1.284310712 93.77211607 15528.89086 26.89264 ACAP1 0.237755774679294 0.762241777917248 2.44740345776545e-06 ArfGAP with coiled-coil, ankyrin repeat and PH domains 1 FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface. Required for regulated export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration. {ECO:0000269|PubMed:11062263, ECO:0000269|PubMed:16256741, ECO:0000269|PubMed:17398097, ECO:0000269|PubMed:17664335, ECO:0000269|PubMed:22645133}.; . TISSUE SPECIFICITY: Highest level in lung and spleen. Low level in heart, kidney, liver and pancreas. {ECO:0000269|PubMed:11062263}.; lymphoreticular;colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;lung;macula lutea;liver;spleen;kidney;stomach;aorta;thymus; superior cervical ganglion;lymph node;globus pallidus;atrioventricular node;whole blood;tonsil;skeletal muscle;thymus; 0.63230 0.09928 0.001895464 54.03397028 504.0071 4.60736 ACAP2 0.999918184975784 8.18150240194082e-05 1.96831066060382e-13 ArfGAP with coiled-coil, ankyrin repeat and PH domains 2 FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6). {ECO:0000269|PubMed:11062263}.; . TISSUE SPECIFICITY: Widely expressed. Highest level in lung. {ECO:0000269|PubMed:11062263}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;thymus; whole blood; 0.35555 0.11517 -0.602450568 17.91106393 40.66494 1.19160 ACAP2-IT1 . . . ACAP2 intronic transcript 1 . . . . . . . . . . . ACAP3 0.0394309302206711 0.960288965972801 0.000280103806527738 ArfGAP with coiled-coil, ankyrin repeat and PH domains 3 FUNCTION: GTPase-activating protein for the ADP ribosylation factor family. {ECO:0000305}.; . . lymphoreticular;ovary;colon;choroid;fovea centralis;skin;bone marrow;retina;uterus;optic nerve;frontal lobe;bone;pituitary gland;testis;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;muscle;urinary;blood;lens;breast;pancreas;lung;placenta;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; . 0.20316 0.11007 -0.352661697 29.48808681 131.90999 2.50129 ACAT1 0.00159951559198285 0.96981057287304 0.0285899115349771 acetyl-CoA acetyltransferase 1 FUNCTION: Plays a major role in ketone body metabolism.; DISEASE: 3-ketothiolase deficiency (3KTD) [MIM:203750]: An inborn error of isoleucine catabolism characterized by intermittent ketoacidotic attacks associated with unconsciousness. Some patients die during an attack or are mentally retarded. Urinary excretion of 2-methyl-3-hydroxybutyric acid, 2-methylacetoacetic acid, triglylglycine, butanone is increased. It seems likely that the severity of this disease correlates better with the environmental or acquired factors than with the ACAT1 genotype. {ECO:0000269|PubMed:1346617, ECO:0000269|PubMed:1715688, ECO:0000269|PubMed:7728148, ECO:0000269|PubMed:9744475}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;salivary gland;intestine;colon;skin;uterus;prostate;cerebral cortex;endometrium;bone;thyroid;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis;kidney;skeletal muscle; 0.33314 0.47999 -0.538132194 20.26421326 1846.33331 7.92876 ACAT2 1.26453863126978e-05 0.608220826535908 0.391766528077779 acetyl-CoA acetyltransferase 2 . . . . . 0.11409 0.25895 -0.359940251 28.93371078 3588.96459 11.60348 ACBD3 0.981823329864037 0.0181761507695956 5.19366367282437e-07 acyl-CoA binding domain containing 3 FUNCTION: Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:11590181}.; . TISSUE SPECIFICITY: Ubiquitous, with highest expression in testis and ovary. {ECO:0000269|PubMed:11590181}.; . . 0.30042 0.13517 0.150760231 64.51403633 76.52126 1.83572 ACBD4 1.82643064951694e-05 0.883792361565605 0.1161893741279 acyl-CoA binding domain containing 4 FUNCTION: Binds medium- and long-chain acyl-CoA esters and may function as an intracellular carrier of acyl-CoA esters.; . . salivary gland;colon;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;cervix;kidney;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;liver;pons;skeletal muscle; 0.08056 0.08115 0.463046108 78.58575136 139.59497 2.57539 ACBD5 0.061645689531942 0.937666667011874 0.000687643456184112 acyl-CoA binding domain containing 5 FUNCTION: Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy but is dispensable for aggrephagy and nonselective autophagy. Binds medium- and long-chain acyl-CoA esters. {ECO:0000269|PubMed:24535825}.; . . . . 0.15865 0.07003 -0.556537043 19.72753008 826.14153 5.63377 ACBD6 0.0649592587219742 0.920160982958555 0.0148797583194709 acyl-CoA binding domain containing 6 FUNCTION: Binds long-chain acyl-coenzyme A molecules with a strong preference for unsaturated C18:1-CoA, lower affinity for unsaturated C20:4-CoA, and very weak affinity for saturated C16:0- CoA. Does not bind fatty acids. {ECO:0000269|PubMed:18268358}.; . TISSUE SPECIFICITY: Detected in placenta and spleen (at protein level). Detected in placenta, umbilical cord blood, CD34-positive hematopoietic progenitor cells and bone marrow. {ECO:0000269|PubMed:18268358}.; . . 0.46704 0.10684 -0.427900189 25.14744043 16.07879 0.56883 ACBD7 0.0863366080379718 0.761384381744349 0.152279010217679 acyl-CoA binding domain containing 7 FUNCTION: Binds medium- and long-chain acyl-CoA esters.; . . . . 0.09215 0.09170 0.147123112 64.11299835 15.27033 0.54938 ACCS 0.00017166582720853 0.970899052158324 0.0289292820144672 1-aminocyclopropane-1-carboxylate synthase homolog (inactive) FUNCTION: Does not catalyze the synthesis of 1-aminocyclopropane- 1-carboxylate but is capable of catalyzing the deamination of L- vinylglycine. {ECO:0000269|PubMed:11470512}.; . . unclassifiable (Anatomical System);lymph node;heart;skeletal muscle;bone marrow;uterus;prostate;lung;endometrium;larynx;bone;thyroid;placenta;liver;testis;head and neck;germinal center;kidney;brain;bladder;stomach; . 0.10508 0.15825 0.290313621 71.56758669 3720.71864 11.91989 ACCSL 2.58324245379256e-11 0.136446773742422 0.863553226231745 1-aminocyclopropane-1-carboxylate synthase (inactive)-like . . . . . . . -0.154246007 42.22694032 72.53949 1.77548 ACD 5.77980161685066e-07 0.868643625704373 0.131355796315465 adrenocortical dysplasia homolog (mouse) FUNCTION: Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Promotes binding of POT1 to single-stranded telomeric DNA. Modulates the inhibitory effects of POT1 on telomere elongation. The ACD-POT1 heterodimer enhances telomere elongation by increasing telomerase processivity. Plays a role in shelterin complex assembly. May play a role in organogenesis. {ECO:0000269|PubMed:15181449, ECO:0000269|PubMed:16166375, ECO:0000269|PubMed:16880378, ECO:0000269|PubMed:17237768, ECO:0000269|PubMed:20231318}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.16210 0.13430 -0.598810865 18.13517339 47.31232 1.33415 ACE 4.63282874453648e-18 0.436637639653135 0.563362360346865 angiotensin I converting enzyme FUNCTION: Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety.; DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. {ECO:0000269|PubMed:15534175}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Renal tubular dysgenesis (RTD) [MIM:267430]: Autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype). {ECO:0000269|PubMed:16116425}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Microvascular complications of diabetes 3 (MVCD3) [MIM:612624]: Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end- stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. {ECO:0000269|PubMed:10099885}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Intracerebral hemorrhage (ICH) [MIM:614519]: A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke. {ECO:0000269|PubMed:15277638}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in lung, kidney, heart, gastrointestinal system and prostate. Isoform Testis-specific is expressed in spermatocytes and adult testis. {ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:10969042, ECO:0000269|PubMed:12459472, ECO:0000269|PubMed:15671045}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;frontal lobe;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;nervous;islets of Langerhans;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - interstitial;ciliary ganglion;skeletal muscle; 0.78058 0.71876 -0.573431473 18.90776126 1006.9095 6.10989 ACE2 0.999070360837032 0.000929637370671652 1.79229658242035e-09 angiotensin I converting enzyme 2 FUNCTION: Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin- 13 and dynorphin-13 with high efficiency. May be an important regulator of heart function. {ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:10969042, ECO:0000269|PubMed:14647384, ECO:0000269|PubMed:24227843}.; . TISSUE SPECIFICITY: Expressed in endothelial cells from small and large arteries, and in arterial smooth muscle cells. Expressed in lung alveolar epithelial cells, enterocytes of the small intestine, Leydig cells and Sertoli cells (at protein level). Expressed in heart, kidney, testis, and gastrointestinal system. {ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:10969042, ECO:0000269|PubMed:12459472, ECO:0000269|PubMed:15141377, ECO:0000269|PubMed:15231706, ECO:0000269|PubMed:15671045}.; unclassifiable (Anatomical System);medulla oblongata;placenta;testis;colon;kidney;brain;skeletal muscle; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.90308 0.28373 0.885576705 89.14248644 62.34343 1.61216 ACE3P . . . angiotensin I converting enzyme (peptidyl-dipeptidase A) 3, pseudogene . . . . . . . . . . . ACER1 0.335356707410971 0.649886707254984 0.0147565853340444 alkaline ceramidase 1 FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 8.0. Has a highly restricted substrate specificity for the natural stereoisomer of ceramide with D-erythro-sphingosine but not D-ribo- phytosphingosine or D-erythro-dihydrosphingosine as a backbone. May have a role in regulating the levels of bioactive lipids ceramide and sphingosine 1-phosphate, as well as complex sphingolipids (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Mainly expressed in epidermis. {ECO:0000269|PubMed:16477081}.; skin; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.09277 0.11016 -0.025608647 51.91672564 1151.46765 6.46492 ACER2 0.146646886780043 0.835306279770407 0.01804683344955 alkaline ceramidase 2 FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid. Unsaturated long-chain ceramides are the best substrates, saturated long-chain ceramides and unsaturated very long-chain ceramides are good substrates, whereas saturated very long-chain ceramides and short-chain ceramides were poor substrates. The substrate preference is D-erythro-C(18:1)-, C(20:1)-, C(20:4)-ceramide > D-erythro-C(16:0)-, C(18:0), C(20:0)- ceramide > D-erythro-C(24:1)-ceramide > D-erythro-C(12:0)- ceramide, D-erythro-C(14:0)-ceramides > D-erythro-C(24:0)-ceramide > D-erythro-C(6:0)-ceramide. Inhibits the maturation of protein glycosylation in the Golgi complex, including that of integrin beta-1 (ITGB1) and of LAMP1, by increasing the levels of sphingosine. Inhibits cell adhesion by reducing the level of ITGB1 in the cell surface. May have a role in cell proliferation and apoptosis that seems to depend on the balance between sphingosine and sphingosine-1-phosphate. {ECO:0000269|PubMed:16940153, ECO:0000269|PubMed:18945876, ECO:0000269|PubMed:20089856}.; . TISSUE SPECIFICITY: Highly expressed in placenta. {ECO:0000269|PubMed:16940153}.; unclassifiable (Anatomical System);liver;parathyroid;spleen;skeletal muscle; . 0.20772 0.08575 0.17280645 65.75843359 281.52605 3.59308 ACER3 0.831594948873275 0.168256053096738 0.000148998029986411 alkaline ceramidase 3 FUNCTION: Hydrolyzes only phytoceramide into phytosphingosine and free fatty acid. Does not have reverse activity.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highest expression in placenta.; smooth muscle;ovary;sympathetic chain;parathyroid;skin;uterus;whole body;thyroid;testis;dura mater;germinal center;spinal ganglion;pineal gland;brain;unclassifiable (Anatomical System);meninges;heart;adrenal cortex;blood;skeletal muscle;breast;pia mater;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;aorta; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.28690 0.12214 0.058937498 58.26256192 4.10513 0.15001 ACHE 0.996674942122373 0.00332485974831818 1.9812930879893e-07 acetylcholinesterase (Yt blood group) FUNCTION: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis. {ECO:0000269|PubMed:11985878, ECO:0000269|PubMed:1517212, ECO:0000269|PubMed:1748670, ECO:0000269|PubMed:2714437}.; . TISSUE SPECIFICITY: Isoform H is highly expressed in erythrocytes. {ECO:0000269|PubMed:2714437}.; ovary;colon;parathyroid;substantia nigra;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;greater omentum;pancreas;lung;placenta;macula lutea;liver;spleen;kidney; amygdala;thalamus;medulla oblongata;adipose tissue;cerebellum peduncles;hypothalamus;spinal cord;prefrontal cortex;pons;caudate nucleus;skeletal muscle;cerebellum; 0.19087 0.44337 -0.598810865 18.13517339 2635.44184 9.63557 ACIN1 0.999998436751071 1.56324892865309e-06 2.59071862768451e-18 apoptotic chromatin condensation inducer 1 FUNCTION: Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP complexes which bind RNA in a sequence- independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets; ACIN1 confers RNA-binding to the complex. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells. {ECO:0000269|PubMed:10490026, ECO:0000269|PubMed:12665594, ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:22388736}.; . TISSUE SPECIFICITY: Ubiquitous. The Ser-1180 phosphorylated form (by SRPK2) is highly expressed and phosphorylated in patients with myeloid hematologic malignancies.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;cerebral cortex;larynx;synovium;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; testis - interstitial;temporal lobe;prefrontal cortex;atrioventricular node; 0.75733 0.42314 -0.435396074 24.70511913 7850.70685 19.11113 ACKR1 . . . atypical chemokine receptor 1 (Duffy blood group) FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Has a promiscuous chemokine-binding profile, interacting with inflammatory chemokines of both the CXC and the CC subfamilies but not with homeostatic chemokines. Acts as a receptor for chemokines including CCL2, CCL5, CCL7, CCL11, CCL13, CCL14, CCL17, CXCL5, CXCL6, IL8/CXCL8, CXCL11, GRO, RANTES, MCP-1, TARC and also for the malaria parasites P.vivax and P.knowlesi. May regulate chemokine bioavailability and, consequently, leukocyte recruitment through two distinct mechanisms: when expressed in endothelial cells, it sustains the abluminal to luminal transcytosis of tissue-derived chemokines and their subsequent presentation to circulating leukocytes; when expressed in erythrocytes, serves as blood reservoir of cognate chemokines but also as a chemokine sink, buffering potential surges in plasma chemokine levels.; . TISSUE SPECIFICITY: Found in adult kidney, adult spleen, bone marrow and fetal liver. In particular, it is expressed along postcapillary venules throughout the body, except in the adult liver. Erythroid cells and postcapillary venule endothelium are the principle tissues expressing duffy. Fy(-A-B) individuals do not express duffy in the bone marrow, however they do, in postcapillary venule endothelium.; . . 0.06025 0.07206 0.284856336 71.40835103 . . ACKR2 0.000376890363248093 0.390971409638054 0.608651699998698 atypical chemokine receptor 2 FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines including CCL2, CCL3, CCL3L1, CCL4, CCL5, CCL7, CCL8, CCL11, CCL13, CCL17, CCL22, CCL23, CCL24, SCYA2/MCP-1, SCY3/MIP-1-alpha, SCYA5/RANTES and SCYA7/MCP-3. Upon active ligand stimulation, activates a beta-arrestin 1 (ARRB1)-dependent, G protein- independent signaling pathway that results in the phosphorylation of the actin-binding protein cofilin (CFL1) through a RAC1-PAK1- LIMK1 signaling pathway. Activation of this pathway results in up- regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. By scavenging chemokines in tissues, on the surfaces of lymphatic vessels, and in placenta, plays an essential role in the resolution (termination) of the inflammatory response and in the regulation of adaptive immune responses. Plays a major role in the immune silencing of macrophages during the resolution of inflammation. Acts as a regulator of inflammatory leukocyte interactions with lymphatic endothelial cells (LECs) and is required for immature/mature dendritic cells discrimination by LECs. {ECO:0000269|PubMed:23479571, ECO:0000269|PubMed:23633677}.; . TISSUE SPECIFICITY: Found in endothelial cells lining afferent lymphatics in dermis and lymph nodes. Also found in lymph nodes subcapsular and medullary sinuses, tonsillar lymphatic sinuses and lymphatics in mucosa and submucosa of small and large intestine and appendix. Also found in some malignant vascular tumors. Expressed at high levels in Kaposi sarcoma-related pathologies. Expressed on apoptotic neutrophils (at protein level). Expressed primarily in placenta and fetal liver, and found at very low levels in the lung and lymph node. {ECO:0000269|PubMed:11238036, ECO:0000269|PubMed:22651933, ECO:0000269|PubMed:23479571}.; . . 0.06726 0.11885 0.464864541 78.69190847 160.60295 2.76720 ACKR3 0.419555701616577 0.545873464213134 0.0345708341702898 atypical chemokine receptor 3 FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein- mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates. {ECO:0000269|PubMed:16107333, ECO:0000269|PubMed:16940167, ECO:0000269|PubMed:17804806, ECO:0000269|PubMed:18653785, ECO:0000269|PubMed:19255243, ECO:0000269|PubMed:19380869, ECO:0000269|PubMed:19641136, ECO:0000269|PubMed:20018651, ECO:0000269|PubMed:20161793, ECO:0000269|PubMed:20388803, ECO:0000269|PubMed:20887389, ECO:0000269|PubMed:22300987}.; . TISSUE SPECIFICITY: Expressed in monocytes, basophils, B-cells, umbilical vein endothelial cells (HUVEC) and B-lymphoblastoid cells. Lower expression detected in CD4+ T-lymphocytes and natural killer cells. In the brain, detected in endothelial cells and capillaries, and in mature neurons of the frontal cortex and hippocampus. Expressed in tubular formation in the kidney. Highly expressed in astroglial tumor endothelial, microglial and glioma cells. Expressed at low levels in normal CD34+ progenitor cells, but at very high levels in several myeloid malignant cell lines. Expressed in breast carcinomas but not in normal breast tissue (at protein level). {ECO:0000269|PubMed:16107333, ECO:0000269|PubMed:16455976, ECO:0000269|PubMed:19641136, ECO:0000269|PubMed:20388803, ECO:0000269|PubMed:20887389, ECO:0000269|PubMed:21655198}.; . . 0.09450 0.18329 0.042348793 57.31304553 73.27932 1.78854 ACKR4 0.0074451081605227 0.773751344418524 0.218803547420953 atypical chemokine receptor 4 FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CCL2, CCL8, CCL13, CCL19, CCL21 and CCL25. Chemokine-binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization. Plays an important role in controlling the migration of immune and cancer cells that express chemokine receptors CCR7 and CCR9, by reducing the availability of CCL19, CCL21, and CCL25 through internalization. Negatively regulates CXCR3-induced chemotaxis. Regulates T-cell development in the thymus. {ECO:0000269|PubMed:10706668, ECO:0000269|PubMed:23121557, ECO:0000269|PubMed:23341447}.; . TISSUE SPECIFICITY: Predominantly expressed in heart. Lower expression in lung, pancreas, spleen, colon, skeletal muscle and small intestine. {ECO:0000269|PubMed:10734104, ECO:0000269|PubMed:10767544, ECO:0000269|PubMed:11981810}.; . . 0.20072 0.08606 0.527368849 80.73248408 45.69268 1.29867 ACLS . . . acrocallosal syndrome . . . . . . . . . . . ACLY 0.996414980364678 0.00358501963201492 3.30709394717358e-12 ATP citrate lyase FUNCTION: ATP-citrate synthase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine. {ECO:0000269|PubMed:23932781}.; . . medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;duodenum;hypopharynx;amnion;head and neck;kidney;stomach;aorta; superior cervical ganglion;adipose tissue;hypothalamus;globus pallidus;ciliary ganglion;atrioventricular node; 0.71968 0.54266 -0.773369631 13.10450578 122.10544 2.40635 ACMSD 1.98871537094846e-07 0.436883259104304 0.563116542024159 aminocarboxymuconate semialdehyde decarboxylase FUNCTION: Converts alpha-amino-beta-carboxymuconate-epsilon- semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal cells which is implicated in the pathogenesis of various neurodegenerative disorders. In the presence of ACMSD, ACMS is converted to AMS, a benign catabolite. ACMSD ultimately controls the metabolic fate of tryptophan catabolism along the kynurenine pathway. {ECO:0000269|PubMed:19843166}.; . . unclassifiable (Anatomical System);liver;spleen;kidney;skeletal muscle; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.16240 0.12787 -0.404032746 26.53338051 73.5044 1.79222 ACO1 3.56928434859223e-08 0.999308721880614 0.000691242426542454 aconitase 1 FUNCTION: Iron sensor. Binds a 4Fe-4S cluster and functions as aconitase when cellular iron levels are high. Functions as mRNA binding protein that regulates uptake, sequestration and utilization of iron when cellular iron levels are low. Binds to iron-responsive elements (IRES) in target mRNA species when iron levels are low. Binding of a 4Fe-4S cluster precludes RNA binding. {ECO:0000269|PubMed:1946430, ECO:0000269|PubMed:8041788}.; . . smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;synovium;bone;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;lung;cornea;mesenchyma;adrenal gland;placenta;head and neck;kidney;stomach;aorta;cerebellum; superior cervical ganglion;fetal liver;adipose tissue;adrenal gland;liver;testis;kidney; 0.23917 0.61151 -1.082044518 7.242274121 557.15552 4.79414 ACO2 0.454377775083461 0.545611779155843 1.04457606966769e-05 aconitase 2 FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. {ECO:0000250}.; DISEASE: Infantile cerebellar-retinal degeneration (ICRD) [MIM:614559]: A severe autosomal recessive neurodegenerative disorder characterized by onset between ages 2 and 6 months of truncal hypotonia, athetosis, seizures, and ophthalmologic abnormalities, particularly optic atrophy and retinal degeneration. Affected individuals show profound psychomotor retardation, with only some achieving rolling, sitting, or recognition of family. Brain MRI shows progressive cerebral and cerebellar degeneration. {ECO:0000269|PubMed:22405087, ECO:0000269|PubMed:25351951}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Optic atrophy 9 (OPA9) [MIM:616289]: A condition that features progressive visual loss in association with optic atrophy. Atrophy of the optic disk indicates a deficiency in the number of nerve fibers which arise in the retina and converge to form the optic disk, optic nerve, optic chiasm and optic tracts. {ECO:0000269|PubMed:25351951}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;bladder;brain;tonsil;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach; whole brain;amygdala;thalamus;occipital lobe;heart;hypothalamus;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;kidney;cingulate cortex;parietal lobe; 0.46098 0.78224 -0.997481928 8.47487615 57.4073 1.52643 ACOD1 . . . aconitate decarboxylase 1 FUNCTION: Involved in the inhibition of the inflammatory response. Acts as a negative regulator of the Toll-like receptors (TLRs)- mediated inflammatory innate response by stimulating the tumor necrosis factor alpha-induced protein TNFAIP3 expression via reactive oxygen species (ROS) in LPS-tolerized macrophages. Involved in antimicrobial response of innate immune cells; IRG1- mediated itaconic acid production contributes to the antimicrobial activity of macrophages. Plays a role in the embryo implantation. {ECO:0000269|PubMed:23609450, ECO:0000269|PubMed:23610393}.; . TISSUE SPECIFICITY: Expressed in LPS-tolerized macrophages (at protein level). Expressed in peripheral blood mononuclear cells (PBMCs), microglia and macrophage cells. {ECO:0000269|PubMed:23609450, ECO:0000269|PubMed:23610393}.; . . 0.12417 0.13233 -3.840064972 0.230007077 . . ACOT1 0.0359991659838093 0.830358558581386 0.133642275434804 acyl-CoA thioesterase 1 FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Active towards fatty acyl-CoA with chain-lengths of C12-C16 (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;parathyroid;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;prostate;optic nerve;whole body;lung;endometrium;placenta;macula lutea;liver;head and neck;kidney;brain;thymus; . 0.12819 0.12290 . . 504.05657 4.60864 ACOT2 0.142294697843995 0.838675016308048 0.0190302858479568 acyl-CoA thioesterase 2 FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Displays high levels of activity on medium- and long chain acyl CoAs. {ECO:0000269|PubMed:10944470}.; . TISSUE SPECIFICITY: Strongest expression in heart, liver, muscle and kidney. Weak in placenta and pancreas. {ECO:0000269|PubMed:16940157}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; . 0.06196 0.10881 . . 303.91986 3.71306 ACOT4 4.21463209007871e-08 0.0582263409445011 0.941773616909178 acyl-CoA thioesterase 4 FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH (By similarity). Succinyl-CoA thioesterase that also hydrolyzes long chain saturated and unsaturated monocarboxylic acyl-CoAs. {ECO:0000250}.; . TISSUE SPECIFICITY: Strongest expression in liver and kidney and weaker expression in placenta, heart, and muscle. {ECO:0000269|PubMed:16940157}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;cochlea;thyroid;bone;testis;brain;unclassifiable (Anatomical System);pharynx;blood;lens;lung;cornea;placenta;visual apparatus;macula lutea;liver;kidney;mammary gland;stomach; . 0.05539 0.10074 0.284856336 71.40835103 2651.03332 9.67248 ACOT6 0.00152388682505152 0.444703615992556 0.553772497182393 acyl-CoA thioesterase 6 . . . . . 0.10668 0.09044 0.547599505 81.2160887 122.29752 2.40829 ACOT7 0.381517901841213 0.616301741605247 0.00218035655353979 acyl-CoA thioesterase 7 FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl- CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA.; . TISSUE SPECIFICITY: Isoform 4 is expressed exclusively in brain. {ECO:0000269|PubMed:12435388}.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;pituitary gland;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;muscle;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; amygdala;whole brain;dorsal root ganglion;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;kidney;cingulate cortex;parietal lobe;cerebellum; 0.07520 0.74467 -0.756778259 13.44656759 16.25413 0.57719 ACOT8 3.56850509972552e-05 0.818110289549535 0.181854025399468 acyl-CoA thioesterase 8 FUNCTION: Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH (PubMed:9299485, PubMed:9153233, PubMed:15194431). Competes with bile acid CoA:amino acid N-acyltransferase (BAAT) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (C2 to C20) (PubMed:9299485, PubMed:9153233). Inactive towards substrates with more than C20 aliphatic chains (PubMed:9153233). Involved in the metabolic regulation of peroxisome proliferation (PubMed:15194431). {ECO:0000269|PubMed:15194431, ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485}.; . TISSUE SPECIFICITY: Detected in a T-cell line (at protein level). Ubiquitous (PubMed:9153233, PubMed:9299485). {ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485}.; colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21106 0.41219 0.110306132 62.00165133 303.18272 3.71097 ACOT9 1.90917714279274e-05 0.88929296524822 0.110687942980352 acyl-CoA thioesterase 9 FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Active on long chain acyl-CoAs.; . . unclassifiable (Anatomical System);lymph node;heart;ovary;tongue;colon;blood;skin;breast;placenta;head and neck;germinal center;brain;mammary gland;bladder;aorta; smooth muscle;lung;white blood cells; 0.14996 0.09121 0.439181676 77.69521113 204.02566 3.08375 ACOT11 1.33339142705338e-10 0.53607299380681 0.463927006059851 acyl-CoA thioesterase 11 FUNCTION: Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates.; . TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in skeletal muscle, liver, testis, stomach, spleen, lung and brain. Isoform 2 is predominantly expressed in kidney, uterus, hibernoma and white adipose tissue.; unclassifiable (Anatomical System);lymph node;ovary;lacrimal gland;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;prostate;optic nerve;nasopharynx;thyroid;placenta;macula lutea;pituitary gland;liver;head and neck;spleen;kidney;mammary gland;stomach; . 0.10496 0.13932 0.720128343 85.85751356 3575.80865 11.56510 ACOT12 1.28596440526683e-11 0.30686709100773 0.69313290897941 acyl-CoA thioesterase 12 FUNCTION: Hydrolyzes acetyl-CoA to acetate and CoA. {ECO:0000269|PubMed:16951743}.; . . lung;liver;spleen; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.13349 0.17900 0.156217551 64.82071243 944.26578 5.95405 ACOT13 3.42929947285046e-05 0.204678036552216 0.795287670453055 acyl-CoA thioesterase 13 FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3- hydroxyphenylacetyl-CoA and 3,4-dihydroxyphenylacetyl-CoA (in vitro). May play a role in controlling adaptive thermogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:16934754, ECO:0000269|PubMed:19170545}.; . . medulla oblongata;ovary;parathyroid;fovea centralis;choroid;retina;bone marrow;prostate;optic nerve;whole body;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;liver;testis;cingulate cortex; 0.01854 0.06886 0.325313577 73.11276244 47.64756 1.34019 ACOX1 0.0944353057008641 0.905495421766291 6.92725328443544e-05 acyl-CoA oxidase 1, palmitoyl FUNCTION: Catalyzes the desaturation of acyl-CoAs to 2-trans- enoyl-CoAs. Isoform 1 shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length. Isoform 2 is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Isoform 2 is twice as active as isoform 1 against 16-hydroxy- palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl- CoA. {ECO:0000269|PubMed:17458872, ECO:0000269|PubMed:17603022}.; . TISSUE SPECIFICITY: Widely expressed with highest levels of isoform 1 and isoform 2 detected in testis. Isoform 1 is expressed at higher levels than isoform 2 in liver and kidney while isoform 2 levels are higher in brain, lung, muscle, white adipose tissue and testis. Levels are almost equal in heart. {ECO:0000269|PubMed:17603022, ECO:0000269|PubMed:20195242}.; lymphoreticular;medulla oblongata;ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;hypopharynx;liver;cervix;head and neck;spleen;kidney;aorta;stomach; superior cervical ganglion;trigeminal ganglion; 0.16046 0.77183 0.134171522 63.57041755 194.54546 3.02364 ACOX2 1.54733558790157e-09 0.585002571056521 0.414997427396143 acyl-CoA oxidase 2, branched chain FUNCTION: Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycholestanoic acids.; . TISSUE SPECIFICITY: Present in all tissues tested: heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Most abundant in heart, liver and kidney.; unclassifiable (Anatomical System);ovary;islets of Langerhans;muscle;colon;vein;skin;skeletal muscle;retina;bone marrow;breast;prostate;lung;bone;thyroid;iris;liver;testis;spleen;kidney;brain;mammary gland; fetal liver;superior cervical ganglion;liver;kidney; 0.10524 0.14775 -0.573127851 18.96083982 165.51083 2.81364 ACOX3 3.03156501744108e-12 0.259265348716655 0.740734651280314 acyl-CoA oxidase 3, pristanoyl FUNCTION: Oxidizes the CoA-esters of 2-methyl-branched fatty acids. {ECO:0000250, ECO:0000269|PubMed:9271077}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;iris;amniotic fluid;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.10720 0.63446 -0.788160233 12.62679877 310.89169 3.75186 ACOXL 6.28385483611373e-10 0.400098611117413 0.599901388254202 acyl-CoA oxidase-like . . . unclassifiable (Anatomical System);islets of Langerhans;placenta; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;fetal thyroid;skeletal muscle; 0.07205 0.07959 1.86668643 97.19863175 3441.02377 11.26674 ACP1 0.00220753415585866 0.757182951411963 0.240609514432178 acid phosphatase 1, soluble FUNCTION: Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Isoform 3 does not possess phosphatase activity.; . TISSUE SPECIFICITY: T-lymphocytes express only isoform 2. {ECO:0000269|PubMed:9038134}.; smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;iris;germinal center;bladder;brain;heart;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;aorta;stomach;thymus; amygdala;occipital lobe;superior cervical ganglion;testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;testis; 0.22267 0.54655 0.260991686 70.25831564 2286.39399 8.84955 ACP2 0.00052597665714545 0.970835017257383 0.0286390060854717 acid phosphatase 2, lysosomal . DISEASE: Note=Lysosomal acid phosphatase has been shown to be deficient in cultured fibroblasts from patients manifesting intermittent vomiting, hypotonia, lethargy, opisthotonos, terminal bleeding and death in early infancy. {ECO:0000269|PubMed:5410815}.; . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;mesenchyma;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;liver; 0.17862 0.46460 0.086440867 60.47416844 78.48884 1.86974 ACP5 0.123568347500175 0.852201267605143 0.0242303848946813 acid phosphatase 5, tartrate resistant FUNCTION: Involved in osteopontin/bone sialoprotein dephosphorylation. Its expression seems to increase in certain pathological states such as Gaucher and Hodgkin diseases, the hairy cell, the B-cell, and the T-cell leukemias.; DISEASE: Spondyloenchondrodysplasia with immune dysregulation (SPENCDI) [MIM:607944]: A disease characterized by vertebral and metaphyseal dysplasia, spasticity with cerebral calcifications, and strong predisposition to autoimmune diseases. The skeletal dysplasia is characterized by radiolucent and irregular spondylar and metaphyseal lesions that represent islands of chondroid tissue within bone. {ECO:0000269|PubMed:21217752, ECO:0000269|PubMed:21217755}. Note=The disease is caused by mutations affecting the gene represented in this entry. ACP5 inactivating mutations result in a functional excess of phosphorylated osteopontin causing deregulation of osteopontin signaling and consequential autoimmune disease.; . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;colon;blood;choroid;skin;retina;uterus;pancreas;whole body;lung;endometrium;oesophagus;bone;placenta;alveolus;liver;testis;spleen;kidney;germinal center;brain;mammary gland;tonsil;stomach; superior cervical ganglion;lung;lymph node;liver;kidney; 0.16084 0.25398 0.354632714 74.58126917 890.93344 5.81715 ACP6 3.14409809921214e-05 0.795961583034546 0.204006975984462 acid phosphatase 6, lysophosphatidic FUNCTION: Hydrolyzes lysophosphatidic acid (LPA) containing a medium length fatty acid chain to the corresponding monoacylglycerol. Has highest activity with lysophosphatidic acid containing myristate (C14:0), monounsaturated oleate (C18:1) or palmitate (C16:0), and lower activity with C18:0 and C6:0 lysophosphatidic acid. {ECO:0000269|PubMed:10506173, ECO:0000269|PubMed:23807634}.; . TISSUE SPECIFICITY: Highly expressed in kidney, heart, small intestine, muscle, liver, prostate, testis, ovary and weakly expressed in thymus and colon. {ECO:0000269|PubMed:10506173, ECO:0000269|PubMed:12010880}.; . . 0.10093 0.23221 0.863528995 88.74144845 144.10699 2.61494 ACP7 . . . acid phosphatase 7, tartrate resistant (putative) . . . . . . . . . . . ACPP 1.75749793157423e-07 0.646514579812543 0.353485244437664 acid phosphatase, prostate FUNCTION: A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma.; . TISSUE SPECIFICITY: Highly expressed in the prostate, restricted to glandular and ductal epithelial cells. Also expressed in bladder, kidney, pancreas, lung, cervix, testis and ovary. Weak expression in a subset of pancreatic islet cells, squamous epithelia, the pilosebaceous unit, colonic neuroendocrine cells and skin adnexal structures. Isoform 2 also expressed in the sarcolemma of skeletal muscle. Levels of this cellular isoform decreased in prostate cancer. {ECO:0000269|PubMed:17638863, ECO:0000269|PubMed:21487525}.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;fovea centralis;skeletal muscle;prostate;larynx;nasopharynx;placenta;macula lutea;head and neck;brain;mammary gland;stomach;peripheral nerve; superior cervical ganglion;prostate;trigeminal ganglion; 0.18544 0.15560 -0.602450568 17.91106393 66.58925 1.68257 ACPT 1.219018604775e-13 0.003195158710039 0.996804841289839 acid phosphatase, testicular FUNCTION: Dephosphorylates receptor tyrosine-protein kinase erbB-4 and inhibits the ligand-induced proteolytic cleavage. {ECO:0000269|PubMed:15219672}.; . TISSUE SPECIFICITY: Expressed mainly in the testis. Also expressed in the brain where they are enriched at the postsynaptic sites. Expressed at lower levels in the trachea, prostate, bone marrow, spinal cord, colon, fetal brain, heart, thymus, fetal liver, spleen, leukocytes, ovary, small intestine, pancreas and skeletal muscle. Expression is significantly lower in testicular cancer tissues than in normal testicular tissues. Isoform 3 is expressed in the testis, trachea, prostate and bone marrow. {ECO:0000269|PubMed:11414767}.; lung;liver;testis;spleen; . 0.17973 0.27670 -0.222203495 37.54423213 2591.79139 9.52868 ACR 0.0154598896615065 0.958422678848741 0.0261174314897528 acrosin FUNCTION: Acrosin is the major protease of mammalian spermatozoa. It is a serine protease of trypsin-like cleavage specificity, it is synthesized in a zymogen form, proacrosin and stored in the acrosome.; . . unclassifiable (Anatomical System);medulla oblongata;ovary;testis; . 0.18603 0.25959 -0.602450568 17.91106393 82.38119 1.92715 ACRBP 1.88089650899479e-07 0.867284817510188 0.132714994400161 acrosin binding protein FUNCTION: May be involved in packaging and condensation of the acrosin zymogen in the acrosomal matrix via its association with proacrosin. {ECO:0000250}.; . TISSUE SPECIFICITY: Expression restricted to testis in normal tissue. Expressed in a wide spectrum of cancers, including bladder, breast, liver, lung and colon cancers. {ECO:0000269|PubMed:11248070}.; unclassifiable (Anatomical System);uterus;medulla oblongata;lung;ovary;heart;nasopharynx;placenta;testis;colon;parathyroid;skin; . 0.51351 0.11007 -0.688817379 15.20405756 116.07393 2.34381 ACRC 0.982862105708704 0.017126936241845 1.09580494514663e-05 acidic repeat containing . . TISSUE SPECIFICITY: Detected in skeletal muscle, liver, kidney, pancreas, heart, lung and brain. {ECO:0000269|PubMed:11714101}.; . . 0.02937 0.06040 -0.354480518 29.42911064 94.79103 2.09833 ACRV1 0.00043284285276665 0.650568503304456 0.348998653842777 acrosomal vesicle protein 1 . . TISSUE SPECIFICITY: Testis.; unclassifiable (Anatomical System);medulla oblongata;lung;placenta;liver;testis;spleen; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;appendix;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08835 0.14951 0.082802743 60.09082331 191.81686 3.00364 ACSBG1 0.00670029816274961 0.992517084314283 0.000782617522967372 acyl-CoA synthetase bubblegum family member 1 FUNCTION: Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Able to activate long-chain fatty acids. Also able to activate very long-chain fatty acids; however, the relevance of such activity is unclear in vivo. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids. {ECO:0000269|PubMed:10954726, ECO:0000269|PubMed:12975357}.; . TISSUE SPECIFICITY: Expressed primarily in brain. Expressed at lower level in testis and adrenal gland. Present in all regions of brain except pituitary. {ECO:0000269|PubMed:10954726, ECO:0000269|PubMed:12975357}.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;tongue;spinal cord;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;pia mater;placenta;head and neck;kidney;stomach;aorta;thymus; whole brain;dorsal root ganglion;amygdala;medulla oblongata;occipital lobe;thalamus;superior cervical ganglion;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.09449 0.21146 -0.372889896 28.20240623 329.18937 3.85690 ACSBG2 3.48441388003295e-07 0.934347818172748 0.0656518333858636 acyl-CoA synthetase bubblegum family member 2 FUNCTION: Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Able to activate long-chain fatty acids. Also able to activate very long-chain fatty acids; however, the relevance of such activity is unclear in vivo. Has increased ability to activate oleic and linoleic acid. May play a role in spermatogenesis.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:15685348, ECO:0000269|PubMed:16371355, ECO:0000269|PubMed:16762313}.; unclassifiable (Anatomical System);medulla oblongata;lung;placenta;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; 0.12623 0.09081 1.715972423 96.47912243 1477.23251 7.15906 ACSF2 0.0838516397148764 0.916063840587603 8.45196975201344e-05 acyl-CoA synthetase family member 2 FUNCTION: Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. Has some preference toward medium-chain substrates. Plays a role in adipocyte differentiation. {ECO:0000269|PubMed:16380219, ECO:0000269|PubMed:17762044}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;adrenal gland;kidney; 0.15736 0.20089 -0.178111357 40.44585987 257.08922 3.44872 ACSF3 1.37225554153478e-15 0.0031289317547496 0.996871068245249 acyl-CoA synthetase family member 3 FUNCTION: Catalyzes the initial reaction in intramitochondrial fatty acid synthesis, by activating malonate and methylmalonate, but not acetate, into their respective CoA thioester. May have some preference toward very-long-chain substrates. {ECO:0000269|PubMed:17762044, ECO:0000269|PubMed:21841779}.; DISEASE: Combined malonic and methylmalonic aciduria (CMAMMA) [MIM:614265]: A metabolic disease characterized by malonic and methylmalonic aciduria, with urinary excretion of much larger amounts of methylmalonic acid than malonic acid, in the presence of normal malonyl-CoA decarboxylase activity. Clinical features include coma, ketoacidosis, hypoglycemia, failure to thrive, microcephaly, dystonia, axial hypotonia and/or developmental delay, and neurologic manifestations including seizures, psychiatric disease and/or cognitive decline. {ECO:0000269|PubMed:21841779}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;heart;sympathetic chain;colon;fovea centralis;choroid;skin;uterus;bile duct;prostate;pancreas;optic nerve;lung;endometrium;bone;macula lutea;liver;testis;spleen;germinal center;kidney;brain;tonsil;stomach;thymus; skeletal muscle; 0.10540 . -0.881793075 10.53904223 252.58527 3.42032 ACSL1 0.0918373313295172 0.908159695313973 2.97335650967281e-06 acyl-CoA synthetase long-chain family member 1 FUNCTION: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate.; . TISSUE SPECIFICITY: Highly expressed in liver, heart, skeletal muscle, kidney and erythroid cells, and to a lesser extent in brain, lung, placenta and pancreas. {ECO:0000269|PubMed:10548543}.; ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;dura mater;germinal center;spinal ganglion;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;lacrimal gland;islets of Langerhans;urinary;adrenal cortex;blood;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; fetal liver;adipose tissue;ciliary ganglion;whole blood;skeletal muscle; 0.24765 0.32858 -0.841329384 11.36470866 62.62006 1.61892 ACSL3 0.530102680564255 0.469891501486291 5.81794945405664e-06 acyl-CoA synthetase long-chain family member 3 FUNCTION: Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL3 mediates hepatic lipogenesis (By similarity). Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates (By similarity). Has mainly an anabolic role in energy metabolism. Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins). {ECO:0000250, ECO:0000269|PubMed:18003621}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;bladder;brain;amygdala;heart;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;bile duct;lung;cornea;placenta;hippocampus;kidney;stomach;cerebellum; whole brain;amygdala;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.82697 0.18562 0.132352165 63.48785091 93.41567 2.08001 ACSL4 0.995767650409894 0.00423227733230709 7.22577993478327e-08 acyl-CoA synthetase long-chain family member 4 FUNCTION: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses arachidonate and eicosapentaenoate as substrates.; DISEASE: Mental retardation, X-linked 63 (MRX63) [MIM:300387]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non- syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. {ECO:0000269|PubMed:11889465}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Alport syndrome with mental retardation, midface hypoplasia and elliptocytosis (ATS-MR) [MIM:300194]: A X-linked contiguous gene deletion syndrome characterized by glomerulonephritis, sensorineural hearing loss, mental retardation, midface hypoplasia and elliptocytosis. {ECO:0000269|PubMed:9480748}. Note=The gene represented in this entry may be involved in disease pathogenesis.; . smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; . 0.91674 0.30801 -0.560178693 19.30879925 15.24987 0.54787 ACSL5 0.0167637112007589 0.983194812346447 4.14764527942343e-05 acyl-CoA synthetase long-chain family member 5 FUNCTION: Acyl-CoA synthetases (ACSL) activate long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage (By similarity). Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids (By similarity). It was suggested that it may also stimulate fatty acid oxidation (By similarity). At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL. May have a role in the survival of glioma cells. {ECO:0000250, ECO:0000269|PubMed:17681178, ECO:0000269|PubMed:18806831, ECO:0000269|PubMed:19459852}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;aorta;stomach; superior cervical ganglion;skeletal muscle; 0.14592 0.15681 0.268267497 70.64166077 551.73015 4.77877 ACSL6 0.088562272207543 0.911422110964566 1.5616827890649e-05 acyl-CoA synthetase long-chain family member 6 FUNCTION: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Plays an important role in fatty acid metabolism in brain and the acyl-CoAs produced may be utilized exclusively for the synthesis of the brain lipid.; DISEASE: Note=A chromosomal aberration involving ACSL6 may be a cause of myelodysplastic syndrome with basophilia. Translocation t(5;12)(q31;p13) with ETV6. {ECO:0000269|PubMed:10502316}.; DISEASE: Note=A chromosomal aberration involving ACSL6 may be a cause of acute myelogenous leukemia with eosinophilia. Translocation t(5;12)(q31;p13) with ETV6. {ECO:0000269|PubMed:10502316}.; DISEASE: Note=A chromosomal aberration involving ACSL6 may be a cause of acute eosinophilic leukemia (AEL). Translocation t(5;12)(q31;p13) with ETV6. {ECO:0000269|PubMed:10502316}.; TISSUE SPECIFICITY: Expressed predominantly in erythrocyte precursors, in particular in reticulocytes, fetal blood cells derived from fetal liver, hemopoietic stem cells from cord blood, bone marrow and brain. {ECO:0000269|PubMed:10548543}.; unclassifiable (Anatomical System);ovary;heart;parathyroid;blood;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;prostate;optic nerve;lung;placenta;macula lutea;hippocampus;liver;testis;spleen;brain; amygdala;superior cervical ganglion;testis;skeletal muscle; 0.05423 0.12209 -0.642904474 16.62538335 97.99912 2.13957 ACSM1 4.36748438392005e-09 0.799693256350476 0.20030673928204 acyl-CoA synthetase medium-chain family member 1 FUNCTION: Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro). Functions as GTP-dependent lipoate- activating enzyme that generates the substrate for lipoyltransferase (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);prostate;thyroid;liver;testis;spleen;kidney; testis - interstitial;superior cervical ganglion;trigeminal ganglion; 0.02377 0.11149 0.115764778 62.17268224 302.56401 3.70471 ACSM2A 2.48680424010888e-06 0.995439760259519 0.00455775293624083 acyl-CoA synthetase medium-chain family member 2A FUNCTION: Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);liver;spleen;kidney;gall bladder; . 0.06209 0.06798 0.407828206 76.50979004 2561.49154 9.45559 ACSM2B 8.65856451993107e-06 0.996228129400628 0.00376321203485225 acyl-CoA synthetase medium-chain family member 2B FUNCTION: Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro). {ECO:0000269|PubMed:12616642}.; . TISSUE SPECIFICITY: Detected in liver. {ECO:0000269|PubMed:10434065, ECO:0000269|PubMed:19634011}.; unclassifiable (Anatomical System);liver;spleen;kidney; . 0.07773 0.07290 0.560331224 81.70559094 158.88296 2.75294 ACSM3 4.97906453643603e-09 0.822359994008418 0.177640001012518 acyl-CoA synthetase medium-chain family member 3 FUNCTION: Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;ovary;colon;parathyroid;skin;skeletal muscle;breast;uterus;prostate;whole body;lung;endometrium;bone;liver;testis;cervix;spleen;germinal center;kidney;brain;bladder;stomach;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.25896 0.45481 1.289723716 93.85468271 993.69947 6.07557 ACSM4 4.67032830619752e-11 0.188565924528515 0.811434075424781 acyl-CoA synthetase medium-chain family member 4 FUNCTION: Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) (By similarity). {ECO:0000250}.; . . . . 0.17056 . -0.464712395 23.5727766 1070.09648 6.27247 ACSM5 5.09254067683109e-08 0.838533957882617 0.161465991191976 acyl-CoA synthetase medium-chain family member 5 FUNCTION: Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in kidney and liver. {ECO:0000269|PubMed:12654705}.; unclassifiable (Anatomical System);prostate;frontal lobe;hippocampus;liver;testis;colon;spleen;kidney;brain;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.05514 0.09249 3.184574415 99.32767162 7462.84206 18.58355 ACSM5P1 . . . acyl-CoA synthetase medium-chain family member 5 pseudogene 1 . . . . . . . . . . . ACSM6 . . . acyl-CoA synthetase medium-chain family member 6 . . . . . 0.03346 . 0.68351529 85.03774475 . . ACSS1 0.00139669613638913 0.997081764407125 0.00152153945648631 acyl-CoA synthetase short-chain family member 1 FUNCTION: Important for maintaining normal body temperature during fasting and for energy homeostasis. Essential for energy expenditure under ketogenic conditions (By similarity). Converts acetate to acetyl-CoA so that it can be used for oxidation through the tricarboxylic cycle to produce ATP and CO(2). {ECO:0000250, ECO:0000269|PubMed:16788062}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;hypopharynx;liver;spleen;head and neck;kidney;stomach;peripheral nerve; superior cervical ganglion;placenta;atrioventricular node; 0.13749 0.19539 -0.949752638 9.32413305 1132.78741 6.42087 ACSS2 8.97239307211796e-11 0.691620979063847 0.308379020846429 acyl-CoA synthetase short-chain family member 2 FUNCTION: Activates acetate so that it can be used for lipid synthesis or for energy generation.; . . medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;gum;thyroid;bladder;brain;heart;cartilage;urinary;spinal cord;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;mesenchyma;adrenal gland;placenta;head and neck;kidney;stomach; adipose tissue; 0.37909 0.45680 -0.486758915 22.69992923 597.75331 4.94750 ACSS3 2.99940752851555e-11 0.457248943830766 0.54275105613924 acyl-CoA synthetase short-chain family member 3 FUNCTION: Activates acetate so that it can be used for lipid synthesis or for energy generation. {ECO:0000250}.; . . unclassifiable (Anatomical System);urinary;muscle;lens;skeletal muscle;skin;uterus;lung;cerebral cortex;endometrium;placenta;liver;testis;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12185 0.09190 -0.422438699 25.64284029 372.17387 4.07096 ACTA1 0.00802663240582685 0.929800746577449 0.0621726210167243 actin, alpha 1, skeletal muscle FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.; DISEASE: Nemaline myopathy 3 (NEM3) [MIM:161800]: A form of nemaline myopathy. Nemaline myopathies are muscular disorders characterized by muscle weakness of varying severity and onset, and abnormal thread-like or rod-shaped structures in muscle fibers on histologic examination. {ECO:0000269|PubMed:10508519, ECO:0000269|PubMed:11166164, ECO:0000269|PubMed:11333380, ECO:0000269|PubMed:15198992, ECO:0000269|PubMed:15236405, ECO:0000269|PubMed:15336687, ECO:0000269|PubMed:15520409, ECO:0000269|PubMed:16427282, ECO:0000269|PubMed:16945537}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myopathy, actin, congenital, with excess of thin myofilaments (MPCETM) [MIM:161800]: A congenital muscular disorder characterized at histological level by areas of sarcoplasm devoid of normal myofibrils and mitochondria, and replaced with dense masses of thin filaments. Central cores, rods, ragged red fibers, and necrosis are absent. {ECO:0000269|PubMed:10508519}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myopathy, congenital, with fiber-type disproportion (CFTD) [MIM:255310]: A genetically heterogeneous disorder in which there is relative hypotrophy of type 1 muscle fibers compared to type 2 fibers on skeletal muscle biopsy. However, these findings are not specific and can be found in many different myopathic and neuropathic conditions. {ECO:0000269|PubMed:15468086}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);myocardium;heart;muscle;lens;vein;skeletal muscle;greater omentum;prostate;lung;visual apparatus;alveolus;testis;kidney;aorta; prostate;heart;tongue;thyroid;testis;fetal thyroid;skeletal muscle; 0.90573 0.93721 -0.295622497 32.61972163 6.81058 0.25140 ACTA2 0.734223241103143 0.265236864045234 0.000539894851622421 actin, alpha 2, smooth muscle, aorta FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.; DISEASE: Note=ACTA2 mutations predispose patients to a variety of diffuse and diverse vascular diseases, premature onset coronary artery disease (CAD), premature ischemic strokes and Moyamoya disease. {ECO:0000269|PubMed:19409525}.; DISEASE: Aortic aneurysm, familial thoracic 6 (AAT6) [MIM:611788]: A disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance. {ECO:0000269|PubMed:17994018, ECO:0000269|PubMed:19409525, ECO:0000269|PubMed:19639654}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Moyamoya disease 5 (MYMY5) [MIM:614042]: A progressive cerebral angiopathy characterized by bilateral intracranial carotid artery stenosis and telangiectatic vessels in the region of the basal ganglia. The abnormal vessels resemble a 'puff of smoke' (moyamoya) on cerebral angiogram. Affected individuals can develop transient ischemic attacks and/or cerebral infarction, and rupture of the collateral vessels can cause intracranial hemorrhage. Hemiplegia of sudden onset and epileptic seizures constitute the prevailing presentation in childhood, while subarachnoid bleeding occurs more frequently in adults. {ECO:0000269|PubMed:20970362}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multisystemic smooth muscle dysfunction syndrome (MSMDYS) [MIM:613834]: A syndrome characterized by dysfunction of smooth muscle cells throughout the body, leading to aortic and cerebrovascular disease, fixed dilated pupils, hypotonic bladder, malrotation, and hypoperistalsis of the gut and pulmonary hypertension. {ECO:0000269|PubMed:20734336}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;testis;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;skeletal muscle;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve;thymus; testis - interstitial;superior cervical ganglion;ovary;heart;uterus;uterus corpus;prostate;testis - seminiferous tubule;trachea;placenta;testis;appendix;fetal lung;ciliary ganglion;trigeminal ganglion; 0.76679 0.15588 -0.273576253 33.97027601 3.60496 0.13143 ACTA2-AS1 . . . ACTA2 antisense RNA 1 . . . . . . . . . . . ACTB 0.935803217105583 0.063906187355641 0.000290595538775797 actin, beta FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.; DISEASE: Dystonia, juvenile-onset (DJO) [MIM:607371]: A form of dystonia with juvenile onset. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. Patients with juvenile-onset dystonia manifest progressive, generalized, dopa-unresponsive dystonia, developmental malformations and sensory hearing loss. {ECO:0000269|PubMed:16685646}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Baraitser-Winter syndrome 1 (BRWS1) [MIM:243310]: A rare developmental disorder characterized by the combination of congenital ptosis, high-arched eyebrows, hypertelorism, ocular colobomata, and a brain malformation consisting of anterior- predominant lissencephaly. Other typical features include postnatal short stature and microcephaly, intellectual disability, seizures, and hearing loss. {ECO:0000269|PubMed:22366783}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;oesophagus;gum;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;alveolus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;thalamus;subthalamic nucleus;occipital lobe;adipose tissue;smooth muscle;heart;globus pallidus;parietal lobe;tonsil; 0.99419 . -0.670411825 15.61689078 1.93092 0.06330 ACTBL2 6.02234434562323e-10 0.0179795191275531 0.982020480270212 actin, beta-like 2 FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. {ECO:0000250}.; . . . . 0.61459 0.62650 0.88921411 89.24274593 282.60784 3.59816 ACTBP1 . . . actin, beta pseudogene 1 . . . . . . . . . . . ACTBP2 . . . actin, beta pseudogene 2 . . . . . . . . . . . ACTBP3 . . . actin, beta pseudogene 3 . . . . . . . . . . . ACTBP4 . . . actin, beta pseudogene 4 . . . . . . . . . . . ACTBP6 . . . actin, beta pseudogene 6 . . . . . . . . . . . ACTBP7 . . . actin, beta pseudogene 7 . . . . . . . . . . . ACTBP8 . . . actin, beta pseudogene 8 . . . . . . . . . . . ACTBP9 . . . actin, beta pseudogene 9 . . . . . . . . . . . ACTBP10 . . . actin, beta pseudogene 10 . . . . . . . . . . . ACTBP11 . . . actin, beta pseudogene 11 . . . . . . . . . . . ACTBP12 . . . actin, beta pseudogene 12 . . . . . . . . . . . ACTBP13 . . . actin, beta pseudogene 13 . . . . . . . . . . . ACTBP14 . . . actin, beta pseudogene 14 . . . . . . . . . . . ACTC1 0.946770308539104 0.0530481269028729 0.000181564558022961 actin, alpha, cardiac muscle 1 FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.; DISEASE: Cardiomyopathy, dilated 1R (CMD1R) [MIM:613424]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:9563954}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, familial hypertrophic 11 (CMH11) [MIM:612098]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:10330430, ECO:0000269|PubMed:10966831, ECO:0000269|PubMed:14729850, ECO:0000269|PubMed:18403758}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Atrial septal defect 5 (ASD5) [MIM:612794]: A congenital heart malformation characterized by incomplete closure of the wall between the atria resulting in blood flow from the left to the right atria. {ECO:0000269|PubMed:17947298}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;fovea centralis;retina;uterus;atrium;whole body;larynx;bone;testis;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;muscle;skeletal muscle;pancreas;lung;placenta;macula lutea;hippocampus;visual apparatus;liver;spleen;head and neck;kidney;stomach;aorta; superior cervical ganglion;heart;fetal thyroid;skeletal muscle; 0.76812 0.90675 -0.207437529 38.2814343 2.4177 0.08589 ACTG1 0.218555803598304 0.773018476768944 0.00842571963275219 actin gamma 1 FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.; DISEASE: Deafness, autosomal dominant, 20 (DFNA20) [MIM:604717]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:13680526, ECO:0000269|PubMed:14684684, ECO:0000269|PubMed:16773128, ECO:0000269|PubMed:18804074, ECO:0000269|PubMed:19477959}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Baraitser-Winter syndrome 2 (BRWS2) [MIM:614583]: A rare developmental disorder characterized by the combination of congenital ptosis, high-arched eyebrows, hypertelorism, ocular colobomata, and a brain malformation consisting of anterior- predominant lissencephaly. Other typical features include postnatal short stature and microcephaly, intellectual disability, seizures, and hearing loss. {ECO:0000269|PubMed:22366783}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;sympathetic chain;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;oesophagus;gum;bone;thyroid;testis;spinal ganglion;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pineal body;muscle;urinary;adrenal cortex;blood;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; . 0.92981 . -1.927246174 1.910828025 13.06854 0.47567 ACTG1P1 . . . actin gamma 1 pseudogene 1 . . . . . . . . . . . ACTG1P2 . . . actin gamma 1 pseudogene 2 . . . . . . . . . . . ACTG1P3 . . . actin gamma 1 pseudogene 3 . . . . . . . . . . . ACTG1P4 . . . actin gamma 1 pseudogene 4 . . . . . . . . . . . ACTG1P6 . . . actin gamma 1 pseudogene 6 . . . . . . . . . . . ACTG1P7 . . . actin gamma 1 pseudogene 7 . . . . . . . . . . . ACTG1P8 . . . actin gamma 1 pseudogene 8 . . . . . . . . . . . ACTG1P9 . . . actin gamma 1 pseudogene 9 . . . . . . . . . . . ACTG1P10 . . . actin gamma 1 pseudogene 10 . . . . . . . . . . . ACTG1P11 . . . actin gamma 1 pseudogene 11 . . . . . . . . . . . ACTG1P12 . . . actin gamma 1 pseudogene 12 . . . . . . . . . . . ACTG1P13 . . . actin gamma 1 pseudogene 13 . . . . . . . . . . . ACTG1P14 . . . actin gamma 1 pseudogene 14 . . . . . . . . . . . ACTG1P15 . . . actin gamma 1 pseudogene 15 . . . . . . . . . . . ACTG1P16 . . . actin gamma 1 pseudogene 16 . . . . . . . . . . . ACTG1P17 . . . actin gamma 1 pseudogene 17 . . . . . . . . . . . ACTG1P18 . . . actin gamma 1 pseudogene 18 . . . . . . . . . . . ACTG1P19 . . . actin gamma 1 pseudogene 19 . . . . . . . . . . . ACTG1P20 . . . actin gamma 1 pseudogene 20 . . . . . . . . . . . ACTG1P21 . . . actin gamma 1 pseudogene 21 . . . . . . . . . . . ACTG1P22 . . . actin gamma 1 pseudogene 22 . . . . . . . . . . . ACTG1P23 . . . actin gamma 1 pseudogene 23 . . . . . . . . . . . ACTG1P24 . . . actin gamma 1 pseudogene 24 . . . . . . . . . . . ACTG2 0.692010864371864 0.307148842778093 0.000840292850042153 actin, gamma 2, smooth muscle, enteric FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.; DISEASE: Visceral myopathy (VSCM) [MIM:155310]: A rare inherited form of myopathic pseudo-obstruction characterized by impaired function of enteric smooth muscle cells, resulting in abnormal intestinal motility, severe abdominal pain, malnutrition, and even death. The disease shows inter- and intrafamilial variability. Most severely affected patients exhibit prenatal bladder enlargement, intestinal malrotation, neonatal functional gastrointestinal obstruction, and dependence on total parenteral nutrition and urinary catheterization. {ECO:0000269|PubMed:22960657, ECO:0000269|PubMed:24337657, ECO:0000269|PubMed:24676022, ECO:0000269|PubMed:24777424}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;testis;spinal ganglion;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;pharynx;blood;breast;lung;epididymis;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; uterus;uterus corpus;prostate;trachea;placenta;appendix;testis; 0.89382 0.67288 -0.361761279 28.6329323 6.21695 0.23472 ACTL6A 0.992221335003384 0.00777834515796699 3.19838648553875e-07 actin like 6A FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for maximal ATPase activity of SMARCA4/BRG1/BAF190A and for association of the SMARCA4/BRG1/BAF190A containing remodeling complex BAF with chromatin/nuclear matrix. Belongs to the neural progenitors- specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a post- mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. {ECO:0000250, ECO:0000269|PubMed:14966270}.; . . . . 0.78479 0.71819 0.283038099 71.26680821 70.2961 1.74318 ACTL6B 0.987130694865973 0.012869082880304 2.22253722609532e-07 actin like 6B FUNCTION: Belongs to the chromatin remodeling brain-specific BAF (bBAF) complex, as such plays a role in remodeling mononucleosomes in an ATP-dependent fashion. Belongs to the neuron-specific chromatin remodeling complex (nBAF complex) and is required for postmitotic neural development and dendritic outgrowth. During neural development a switch from a stem/progenitor to a post- mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. ACTL6B/BAF53B is not essential for assembly of the nBAF complex but is required for targeting the complex and CREST to the promoter of genes essential for dendritic growth (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;lung;frontal lobe;macula lutea;alveolus;testis;brain;aorta;cerebellum; whole brain;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;atrioventricular node;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.62233 0.44836 -0.339715008 30.06605331 19.95387 0.67906 ACTL7A 6.78270698204256e-06 0.280593404643285 0.719399812649733 actin like 7A . . TISSUE SPECIFICITY: Strongly expressed in testis. Also expressed in other tissues. {ECO:0000269|PubMed:10373328}.; unclassifiable (Anatomical System);medulla oblongata;lung;hippocampus;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.31773 0.10816 -0.132199953 43.97853267 579.29773 4.87663 ACTL7B 6.59958139173351e-05 0.287732126343994 0.712201877842088 actin like 7B . . TISSUE SPECIFICITY: Detected only in the testis and, to a lesser extent, in the prostate. {ECO:0000269|PubMed:10373328}.; . . 0.48731 0.48535 -0.290161348 33.33923095 750.79102 5.43447 ACTL8 0.077144245715306 0.872399351104161 0.0504564031805331 actin like 8 . . TISSUE SPECIFICITY: Strongly expressed in testis and pancreas. Weak expression in placenta. {ECO:0000269|PubMed:15905330}.; . . 0.12964 0.44797 -0.067881249 48.69072895 141.20461 2.59310 ACTL9 0.042627929021418 0.847253732795356 0.110118338183226 actin like 9 . . . medulla oblongata;lung;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion; . . 0.330767508 73.53739089 47.96843 1.34594 ACTL10 0.0010526008602134 0.375410156222047 0.62353724291774 actin like 10 . . . unclassifiable (Anatomical System);medulla oblongata;prostate;lymph node; testis - interstitial;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.16929 . . . 42.92503 1.24244 ACTN1 0.999930573576069 6.94264237994885e-05 1.31944466824744e-13 actinin alpha 1 FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.; DISEASE: Bleeding disorder, platelet-type 15 (BDPLT15) [MIM:615193]: An autosomal dominant form of macrothrombocytopenia. Affected individuals usually have no or only mild bleeding tendency, such as epistaxis. Laboratory studies show decreased numbers of large platelets and anisocytosis, but the platelets show no in vitro functional abnormalities. {ECO:0000269|PubMed:23434115, ECO:0000269|PubMed:24069336}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;iris;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;oesophagus;cerebral cortex;larynx;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;placenta;hypopharynx;head and neck;kidney;stomach;aorta; lung; 0.68733 0.31632 -1.328217086 4.712196273 169.2976 2.83833 ACTN1-AS1 . . . ACTN1 antisense RNA 1 . . . . . . . . . . . ACTN2 0.999811915853309 0.000188084139300894 7.39038902788819e-12 actinin alpha 2 FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.; DISEASE: Cardiomyopathy, familial hypertrophic 23, with or without left ventricular non-compaction (CMH23) [MIM:612158]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:20022194, ECO:0000269|PubMed:25173926}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1AA, with or without left ventricular non-compaction (CMD1AA) [MIM:612158]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:14567970, ECO:0000269|PubMed:25224718}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in both skeletal and cardiac muscle.; . . 0.77327 0.39885 -1.723336008 2.465204058 447.74179 4.40066 ACTN3 . . . actinin alpha 3 (gene/pseudogene) FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.; . TISSUE SPECIFICITY: Expressed only in a subset of type 2 skeletal muscle fibers. {ECO:0000269|PubMed:11440986}.; . . 0.90108 . . . . . ACTN4 0.999989804555774 1.01954440770068e-05 1.48848975035834e-13 actinin alpha 4 FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (PubMed:15772161). Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA (PubMed:22351778). {ECO:0000250|UniProtKB:P57780, ECO:0000269|PubMed:15772161, ECO:0000269|PubMed:22351778, ECO:0000305|PubMed:9508771}.; DISEASE: Focal segmental glomerulosclerosis 1 (FSGS1) [MIM:603278]: A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation. {ECO:0000269|PubMed:10700177, ECO:0000269|PubMed:18436095, ECO:0000269|PubMed:23890478}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9508771}.; ovary;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; kidney; 0.47251 0.72890 -0.705410796 14.77942911 118.99593 2.37363 ACTN4P1 . . . actinin alpha 4 pseudogene 1 . . . . . . . . . . . ACTN4P2 . . . actinin alpha 4 pseudogene 2 . . . . . . . . . . . ACTP1 . . . actin family pseudogene 1 . . . . . . . . . . . ACTR1A 0.941234073723515 0.0587639799616829 1.94631480192116e-06 ARP1 actin-related protein 1 homolog A, centractin alpha (yeast) FUNCTION: Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome.; . . . . 0.30412 0.54626 -0.361761279 28.6329323 8.60227 0.31539 ACTR1B 0.0316601262849816 0.966413137577842 0.00192673613717614 ARP1 actin-related protein 1 homolog B, centractin beta (yeast) FUNCTION: Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome.; . . myocardium;smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;kidney;stomach;thymus;cerebellum; whole brain;medulla oblongata;occipital lobe;superior cervical ganglion;globus pallidus;pons;cingulate cortex;skeletal muscle;parietal lobe;cerebellum; 0.30657 0.52974 -0.358119787 29.16371786 1574.86665 7.34540 ACTR2 0.99709654108635 0.00290343011324028 2.88004100948255e-08 ARP2 actin-related protein 2 homolog (yeast) FUNCTION: Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. {ECO:0000269|PubMed:9000076}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;amniotic fluid;germinal center;bladder;brain;tonsil;heart;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; amygdala;superior cervical ganglion;occipital lobe;globus pallidus;white blood cells;whole blood;trigeminal ganglion;parietal lobe; 0.30307 0.10886 -0.09720619 46.20193442 2.21749 0.07413 ACTR3 0.998335663589052 0.00166429978050115 3.6630447233037e-08 ARP3 actin-related protein 3 homolog (yeast) FUNCTION: Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. Plays a role in ciliogenesis. {ECO:0000269|PubMed:20393563, ECO:0000269|PubMed:9000076}.; . . lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;larynx;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;white blood cells;whole blood;tonsil; 0.69156 0.14229 0.125076652 62.7388535 35.92435 1.07884 ACTR3B 0.997547180064581 0.00245272562256058 9.43128584763171e-08 ARP3 actin-related protein 3 homolog B (yeast) FUNCTION: Plays a role in the organization of the actin cytoskeleton. May function as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. May decrease the metastatic potential of tumors. {ECO:0000269|PubMed:14651955}.; . TISSUE SPECIFICITY: Detected in fetal brain. Detected throughout the adult brain, in neurons from gray matter, but not in white matter. Detected in liver, skeletal muscle and pancreas. Detected in lung adenocarcinoma cells with low metastatic potential, but not in lung adenocarcinoma cells with high metastatic potential. {ECO:0000269|PubMed:10806390, ECO:0000269|PubMed:11162478}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;optic nerve;frontal lobe;endometrium;thyroid;bone;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;spleen;mammary gland; whole brain;amygdala;occipital lobe;fetal brain;prefrontal cortex;globus pallidus;caudate nucleus;parietal lobe;cingulate cortex; 0.23921 0.14229 -0.427900189 25.14744043 9.07879 0.33214 ACTR3BP1 . . . ACTR3B pseudogene 1 . . . . . . . . . . . ACTR3BP2 . . . ACTR3B pseudogene 2 . . . . . . . . . . . ACTR3BP3 . . . ACTR3B pseudogene 3 . . . . . . . . . . . ACTR3BP4 . . . ACTR3B pseudogene 4 . . . . . . . . . . . ACTR3BP5 . . . ACTR3B pseudogene 5 . . . . . . . . . . . ACTR3BP6 . . . ACTR3B pseudogene 6 . . . . . . . . . . . ACTR3C 0.00123151135996935 0.63560751422336 0.363160974416671 ARP3 actin-related protein 3 homolog C (yeast) FUNCTION: May play a role in the suppression of metastatic potential in lung adenoma carcinoma cells. {ECO:0000269|PubMed:11162478}.; . TISSUE SPECIFICITY: Expressed in kidney, stomach, spleen, bone marrow, uterus, testis, placenta, skeletal muscle, mammary gland, lung, fetal liver, and fetal kidney, but not detected in small intestine, brain, and thymus. Expressed in low-metastatic lung adenocarcinoma cells but not in high-metastatic ones. {ECO:0000269|PubMed:11162478}.; unclassifiable (Anatomical System);breast;thyroid;liver;brain; . . . 0.479642105 78.95140363 1248.01469 6.67146 ACTR3P1 . . . ACTR3 pseudogene 1 . . . . . . . . . . . ACTR3P2 . . . ACTR3 pseudogene 2 . . . . . . . . . . . ACTR3P3 . . . ACTR3 pseudogene 3 . . . . . . . . . . . ACTR5 1.00014232070039e-12 0.0211314622400033 0.978868537758997 ARP5 actin-related protein 5 homolog (yeast) FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Involved in DNA double-strand break repair and UV-damage excision repair. {ECO:0000269|PubMed:19014934, ECO:0000269|PubMed:20855601}.; . . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;adrenal cortex;colon;skin;uterus;breast;lung;endometrium;placenta;liver;testis;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe;cerebellum; 0.14981 0.10831 0.266447942 70.5826846 288.88575 3.63646 ACTR6 0.00468594297720818 0.988908089569031 0.00640596745376085 ARP6 actin-related protein 6 homolog (yeast) . . . umbilical cord;ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;alveolus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;hypothalamus;prefrontal cortex; 0.56026 0.46610 -0.249709319 35.74545883 24.71314 0.81086 ACTR6P1 . . . ACTR6 pseudogene 1 . . . . . . . . . . . ACTR8 2.01457015209018e-08 0.964771190337865 0.0352287895164338 ARP8 actin-related protein 8 homolog (yeast) FUNCTION: Plays an important role in the functional organization of mitotic chromosomes. Exhibits low basal ATPase activity, and unable to polymerize.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion; 0.56717 0.11105 -0.622676946 17.30950696 1131.54341 6.41795 ACTR10 0.00473623657219373 0.988954519261497 0.00630924416630928 actin-related protein 10 homolog (S. cerevisiae) . . . ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach;aorta;cerebellum;thymus; whole brain;dorsal root ganglion;amygdala;occipital lobe;thalamus;medulla oblongata;hypothalamus;spinal cord;subthalamic nucleus;fetal brain;prefrontal cortex;testis;globus pallidus;cingulate cortex;parietal lobe; 0.23550 0.10564 -0.249709319 35.74545883 33.54228 1.03578 ACTRT1 0.0641129356743066 0.727163399685848 0.208723664639845 actin-related protein T1 . . . . . 0.05738 . 0.374860183 75.43052607 168.61631 2.83449 ACTRT2 0.0187224605335923 0.730881455762693 0.250396083703715 actin related protein T2 . . . . . 0.04694 0.44682 0.486911049 79.46449634 2632.34552 9.62130 ACTRT3 0.000670123620467876 0.504255395053519 0.495074481326014 actin-related protein T3 . . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11750065}.; . . . . 0.949904335 90.00943619 530.24293 4.70007 ACVR1 0.95644819340706 0.0435472765813608 4.53001157960967e-06 activin A receptor type 1 FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin. May be involved for left-right pattern formation during embryogenesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in normal parenchymal cells, endothelial cells, fibroblasts and tumor-derived epithelial cells.; ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;cochlea;synovium;bone;thyroid;testis;brain;artery;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;skeletal muscle;breast;pancreas;lung;epididymis;trabecular meshwork;placenta;macula lutea;liver;hypopharynx;spleen;head and neck;kidney;stomach;aorta;peripheral nerve; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.99535 0.38424 -0.514264485 21.41424864 58.72963 1.55397 ACVR1B 0.998904331171601 0.00109565560801258 1.32203864019754e-08 activin A receptor type 1B FUNCTION: Transmembrane serine/threonine kinase activin type-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas the type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine- threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor such as ACVR1B. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C- terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor. ACVR1B also phosphorylates TDP2. {ECO:0000269|PubMed:12364468, ECO:0000269|PubMed:12639945, ECO:0000269|PubMed:18039968, ECO:0000269|PubMed:20226172, ECO:0000269|PubMed:8196624, ECO:0000269|PubMed:9032295, ECO:0000269|PubMed:9892009}.; DISEASE: Note=ACVRIB is abundantly expressed in systemic sclerosis patient fibroblasts and production of collagen is also induced by activin-A/INHBA. This suggests that the activin/ACRV1B signaling mechanism is involved in systemic sclerosis. {ECO:0000269|PubMed:21377836}.; TISSUE SPECIFICITY: Expressed in many tissues, most strongly in kidney, pancreas, brain, lung, and liver.; ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;hypopharynx;alveolus;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;subthalamic nucleus;prefrontal cortex;appendix;ciliary ganglion;kidney;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.88541 0.29686 -0.405853867 26.23260203 17.03945 0.59931 ACVR1C 0.0448910050879584 0.953978200800952 0.00113079411108909 activin A receptor type 1C FUNCTION: Serine/threonine protein kinase which forms a receptor complex on ligand binding. The receptor complex consisting of 2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators, SMAD2 and SMAD3. Receptor for activin AB, activin B and NODAL. Plays a role in cell differentiation, growth arrest and apoptosis. {ECO:0000269|PubMed:12063393, ECO:0000269|PubMed:15531507}.; . TISSUE SPECIFICITY: Present in pancreas, heart, colon, small intestine, ovary and the hippocampus, medulla oblongata and putamen of the brain. Isoform 1, isoform 2, isoform 3 and isoform 4 are all expressed in the placenta throughout pregnancy. {ECO:0000269|PubMed:12063393, ECO:0000269|PubMed:12606401}.; unclassifiable (Anatomical System);hypothalamus;skin;stomach; superior cervical ganglion;atrioventricular node; 0.75935 0.15405 -0.049474214 50.01179523 1586.75893 7.36956 ACVR2A 0.993932261799491 0.00606756398098532 1.74219524051703e-07 activin A receptor type 2A FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A.; . . unclassifiable (Anatomical System);medulla oblongata;cartilage;heart;ovary;tongue;colon;parathyroid;skeletal muscle;uterus;whole body;lung;frontal lobe;nasopharynx;placenta;liver;testis;spleen;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.69088 0.23984 -0.339715008 30.06605331 11.33135 0.40758 ACVR2B 0.993110896136122 0.00688886623028246 2.37633596019545e-07 activin A receptor type 2B FUNCTION: Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor. {ECO:0000269|PubMed:8622651}.; DISEASE: Heterotaxy, visceral, 4, autosomal (HTX4) [MIM:613751]: A form of visceral heterotaxy, a complex disorder due to disruption of the normal left-right asymmetry of the thoracoabdominal organs. Visceral heterotaxy or situs ambiguus results in randomization of the placement of visceral organs, including the heart, lungs, liver, spleen, and stomach. The organs are oriented randomly with respect to the left-right axis and with respect to one another. It can been associated with variety of congenital defects including cardiac malformations. HTX4 clinical features include dextrocardia, right aortic arch and a right-sided spleen, anomalies of the inferior and the superior vena cava, atrial ventricular canal defect with dextro-transposed great arteries, pulmonary stenosis, polysplenia and midline liver. {ECO:0000269|PubMed:9916847}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);prostate;optic nerve;cartilage;ovary;heart;placenta;macula lutea;adrenal medulla;fovea centralis;choroid;lens;brain;retina; skeletal muscle; 0.85887 0.31462 -0.778825328 12.88039632 47.22568 1.33203 ACVR2B-AS1 . . . ACVR2B antisense RNA 1 . . . . . . . . . . . ACVRL1 0.00794107205683194 0.977623496478128 0.0144354314650395 activin A receptor like type 1 FUNCTION: Type I receptor for TGF-beta family ligands BMP9/GDF2 and BMP10 and important regulator of normal blood vessel development. On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. May bind activin as well. {ECO:0000269|PubMed:22718755, ECO:0000269|PubMed:22799562}.; DISEASE: Telangiectasia, hereditary hemorrhagic, 2 (HHT2) [MIM:600376]: A multisystemic vascular dysplasia leading to dilation of permanent blood vessels and arteriovenous malformations of skin, mucosa, and viscera. The disease is characterized by recurrent epistaxis and gastro-intestinal hemorrhage. Visceral involvement includes arteriovenous malformations of the lung, liver, and brain. {ECO:0000269|PubMed:10694922, ECO:0000269|PubMed:10767348, ECO:0000269|PubMed:11170071, ECO:0000269|PubMed:11484689, ECO:0000269|PubMed:14684682, ECO:0000269|PubMed:15024723, ECO:0000269|PubMed:15712270, ECO:0000269|PubMed:16525724, ECO:0000269|PubMed:16752392, ECO:0000269|PubMed:20414677, ECO:0000269|PubMed:8640225, ECO:0000269|PubMed:9245985}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.92997 0.44126 -1.021348453 7.997169144 141.01923 2.59109 ACY1 7.69184316863466e-05 0.919648939987416 0.0802741415808979 aminoacylase 1 FUNCTION: Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). {ECO:0000269|PubMed:12933810}.; . TISSUE SPECIFICITY: Expression is highest in kidney, strong in brain and weaker in placenta and spleen. {ECO:0000269|PubMed:16465618}.; . . 0.08140 0.27687 0.330767508 73.53739089 571.71377 4.85077 ACY3 1.8844549900242e-07 0.135886661226776 0.864113150327725 aminoacylase 3 FUNCTION: Plays an important role in deacetylating mercapturic acids in kidney proximal tubules. Also acts on N-acetyl-aromatic amino acids (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);prostate;lung;liver;testis;colon;spleen;kidney;mammary gland;stomach; superior cervical ganglion;liver;atrioventricular node;kidney; 0.14142 0.12606 -0.244249595 36.17008728 83.94169 1.95075 ACYP1 0.223001663900667 0.647266185825863 0.12973215027347 acylphosphatase 1 FUNCTION: Its physiological role is not yet clear.; . TISSUE SPECIFICITY: Organ-common type isozyme is found in many different tissues.; ovary;salivary gland;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;breast;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;stomach; . 0.31679 0.08636 -0.031067188 51.03798066 1114.57439 6.37822 ACYP2 0.000220644831166404 0.301669892161657 0.698109463007176 acylphosphatase 2 FUNCTION: Its physiological role is not yet clear.; . . ovary;colon;parathyroid;fovea centralis;skin;uterus;prostate;frontal lobe;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;cerebellum cortex;skeletal muscle;lung;trabecular meshwork;placenta;hippocampus;macula lutea;alveolus;spleen;kidney;stomach; amygdala;whole brain;dorsal root ganglion;superior cervical ganglion;thalamus;occipital lobe;cerebellum peduncles;atrioventricular node;pons;skeletal muscle;skin;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.20016 0.20159 0.080983847 59.76055674 900.98355 5.84521 AD5 . . . Alzheimer disease 5 . . . . . . . . . . . ADA 2.83298527981767e-09 0.15626777593656 0.843732221230454 adenosine deaminase FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2- deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte- epithelial cell adhesion. {ECO:0000269|PubMed:11772392}.; DISEASE: Severe combined immunodeficiency autosomal recessive T- cell-negative/B-cell-negative/NK-cell-negative due to adenosine deaminase deficiency (ADASCID) [MIM:102700]: An autosomal recessive disorder accounting for about 50% of non-X-linked SCIDs. SCID refers to a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients with SCID present in infancy with recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell- mediated cellular immunity due to a defect in T-cell development. ADA deficiency has been diagnosed in chronically ill teenagers and adults (late or adult onset). Population and newborn screening programs have also identified several healthy individuals with normal immunity who have partial ADA deficiency. {ECO:0000269|PubMed:10200056, ECO:0000269|PubMed:1284479, ECO:0000269|PubMed:2166947, ECO:0000269|PubMed:2783588, ECO:0000269|PubMed:3182793, ECO:0000269|PubMed:3839802, ECO:0000269|PubMed:6208479, ECO:0000269|PubMed:7599635, ECO:0000269|PubMed:8227344, ECO:0000269|PubMed:8299233}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in all tissues, occurs in large amounts in T-lymphocytes and, at the time of weaning, in gastrointestinal tissues.; . . 0.11131 0.68435 -0.091746757 46.91554612 812.89077 5.60704 ADAD1 0.974992286651792 0.0250065722656532 1.14108255446672e-06 adenosine deaminase domain containing 1 FUNCTION: Plays a role in spermatogenesis. Binds to RNA but not to DNA (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);bile duct;lung;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10402 0.12427 -0.22584292 37.32012267 57.5578 1.53148 ADAD1P1 . . . adenosine deaminase domain containing 1 pseudogene 1 . . . . . . . . . . . ADAD1P2 . . . adenosine deaminase domain containing 1 pseudogene 2 . . . . . . . . . . . ADAD2 6.70177251389337e-05 0.905678277009936 0.0942547052649253 adenosine deaminase domain containing 2 . . . unclassifiable (Anatomical System);medulla oblongata;optic nerve;lung;thyroid;macula lutea;testis;fovea centralis;choroid;lens;retina; superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.06177 . 0.141451114 63.65298419 3256.58012 10.86933 ADAL 8.52495696643507e-09 0.044008879383272 0.955991112091771 adenosine deaminase-like FUNCTION: Putative nucleoside deaminase. May catalyze the hydrolytic deamination of adenosine or some similar substrate and play a role in purine metabolism (By similarity). {ECO:0000250}.; . . . . 0.06081 0.11351 0.260991686 70.25831564 135.20538 2.52983 ADAM1A . . . ADAM metallopeptidase domain 1A (pseudogene) . . . . . . . . . . . ADAM1B . . . ADAM metallopeptidase domain 1B (pseudogene) . . . . . . . . . . . ADAM2 7.2128414191772e-14 0.114372502622368 0.88562749737756 ADAM metallopeptidase domain 2 FUNCTION: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. Could have a direct role in sperm-zona binding or migration of sperm from the uterus into the oviduct. Interactions with egg membrane could be mediated via binding between its disintegrin-like domain to one or more integrins receptors on the egg. This is a non catalytic metalloprotease-like protein.; . TISSUE SPECIFICITY: Expressed specifically in spermatogenic cells in the seminiferous cells. Not detected in fetal tissues.; unclassifiable (Anatomical System);testis; testis - interstitial;testis - seminiferous tubule;temporal lobe;globus pallidus;testis;trigeminal ganglion; 0.24145 0.11638 0.870809653 88.86529842 460.37141 4.45049 ADAM3A . . . ADAM metallopeptidase domain 3A (pseudogene) . . . . . . . . . . . ADAM3B . . . ADAM metallopeptidase domain 3B (pseudogene) . . . . . . . . . . . ADAM5 . . . ADAM metallopeptidase domain 5 (pseudogene) FUNCTION: This is a non catalytic metalloprotease-like protein. {ECO:0000250, ECO:0000269|PubMed:10417343}.; . TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:10417343}.; . . 0.09807 . . . . . ADAM6 . . . ADAM metallopeptidase domain 6 (pseudogene) . . . . . . . . . . . ADAM7 1.73705605343028e-12 0.5598958791443 0.440104120853963 ADAM metallopeptidase domain 7 FUNCTION: May play an important role in male reproduction including sperm maturation and gonadotrope function. This is a non catalytic metalloprotease-like protein (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Not detected in healthy melanocytes. Expressed in melanoma cells. {ECO:0000269|PubMed:21618342}.; lung;testis;skeletal muscle; superior cervical ganglion;testis;skeletal muscle; 0.32611 0.08967 0.119404819 62.20806794 2343.44208 8.96873 ADAM8 1.47656059828336e-07 0.952266371267968 0.0477334810759718 ADAM metallopeptidase domain 8 FUNCTION: Possible involvement in extravasation of leukocytes.; . TISSUE SPECIFICITY: Expressed on neutrophils and monocytes.; . . 0.35433 0.14301 . . 1193.01078 6.55037 ADAM9 0.828249261024913 0.17175068553127 5.34438166180761e-08 ADAM metallopeptidase domain 9 FUNCTION: Probable zinc protease. May mediate cell-cell or cell- matrix interactions. Isoform 2 displays alpha-secretase activity for APP. {ECO:0000269|PubMed:12054541}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in chondrocytes. Isoform 2 is highly expressed in liver and heart. {ECO:0000269|PubMed:12054541, ECO:0000269|PubMed:7584026, ECO:0000269|PubMed:8647900, ECO:0000269|PubMed:9016778}.; . . 0.23427 0.21827 -0.201976964 38.98325077 410.4595 4.24565 ADAM10 0.999844506827148 0.000155493149876821 2.29750539532457e-11 ADAM metallopeptidase domain 10 FUNCTION: Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth- like factor, ephrin-A2 and for constitutive and regulated alpha- secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B. May regulate the EFNA5-EPHA3 signaling. {ECO:0000269|PubMed:11477090, ECO:0000269|PubMed:11786905, ECO:0000269|PubMed:12475894, ECO:0000269|PubMed:16239146, ECO:0000269|PubMed:17557115, ECO:0000269|PubMed:19114711, ECO:0000269|PubMed:20592283, ECO:0000269|PubMed:21288900}.; DISEASE: Reticulate acropigmentation of Kitamura (RAK) [MIM:615537]: A rare cutaneous pigmentation disorder characterized by reticulate, slightly depressed, sharply demarcated brown macules without hypopigmentation, affecting the dorsa of the hands and feet and appearing in the first or second decade of life. The macules gradually darken and extend to the proximal regions of the extremities. The manifestations tend to progress until middle age, after which progression of the eruptions stops. The pigmentary augmentation is found on the flexor aspects of the wrists, neck, patella and olecranon. Other features include breaks in the epidermal ridges on the palms and fingers, palmoplantar pits, occasionally plantar keratoderma, and partial alopecia. {ECO:0000269|PubMed:23666529}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Alzheimer disease 18 (AD18) [MIM:615590]: A late-onset form of Alzheimer disease, a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C- terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. {ECO:0000269|PubMed:19608551}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in spleen, lymph node, thymus, peripheral blood leukocyte, bone marrow, cartilage, chondrocytes and fetal liver. {ECO:0000269|PubMed:11511685, ECO:0000269|PubMed:9016778}.; lymphoreticular;ovary;colon;parathyroid;skin;retina;uterus;prostate;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);urinary;skeletal muscle;breast;lung;cornea;placenta;liver;spleen;head and neck;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;olfactory bulb;ciliary ganglion;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle; 0.98992 0.37464 -0.381986487 27.68931352 39.95883 1.17527 ADAM11 0.0247363812211132 0.975262666402143 9.52376743974707e-07 ADAM metallopeptidase domain 11 FUNCTION: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein.; . TISSUE SPECIFICITY: Expressed predominantly in brain. Slightly detected or not at all in other tissues.; unclassifiable (Anatomical System);optic nerve;macula lutea;visual apparatus;duodenum;fovea centralis;choroid;lens;stomach;retina; whole brain;subthalamic nucleus;superior cervical ganglion;thalamus;cerebellum peduncles;globus pallidus;ciliary ganglion; 0.14806 0.11452 -1.065444789 7.425100259 91.69001 2.05927 ADAM12 0.341608446907088 0.658390535044096 1.01804881541918e-06 ADAM metallopeptidase domain 12 FUNCTION: Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in placenta and skeletal, cardiac, and smooth muscle. Isoform 2 seems to be expressed only in placenta or in embryo and fetus. Both forms were expressed in some tumor cells lines. Not detected in brain, lung, liver, kidney or pancreas.; . . 0.65368 0.23183 0.009173042 54.15782024 245.04565 3.37758 ADAM15 1.07719204651477e-11 0.974966019158996 0.0250339808302319 ADAM metallopeptidase domain 15 FUNCTION: Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain. {ECO:0000269|PubMed:12091380, ECO:0000269|PubMed:15358598, ECO:0000269|PubMed:15818704, ECO:0000269|PubMed:17416588, ECO:0000269|PubMed:17575078, ECO:0000269|PubMed:18387333, ECO:0000269|PubMed:18434311}.; . TISSUE SPECIFICITY: Expressed in colon and small intestine. Expressed in airway smooth muscle and glomerular mesangial cells (at protein level). Ubiquitously expressed. Overexpressed in atherosclerotic lesions. Constitutively expressed in cultured endothelium and smooth muscle. Expressed in chondrocytes. Expressed in airway smooth muscle and glomerular mesangial cells. {ECO:0000269|PubMed:12091380, ECO:0000269|PubMed:15358598, ECO:0000269|PubMed:17575078, ECO:0000269|PubMed:9016778}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;thyroid;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; uterus corpus;subthalamic nucleus;superior cervical ganglion;lung;heart;placenta; 0.10358 0.13843 -0.571310997 19.01391838 1734.09415 7.68229 ADAM17 0.997367645320671 0.00263235375094992 9.28379498963014e-10 ADAM metallopeptidase domain 17 FUNCTION: Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called Notch extracellular truncation (NEXT). Plays a role in the proteolytic processing of ACE2. {ECO:0000269|PubMed:12441351, ECO:0000269|PubMed:20592283, ECO:0000269|PubMed:24226769, ECO:0000269|PubMed:24227843}.; DISEASE: Inflammatory skin and bowel disease, neonatal, 1 (NISBD1) [MIM:614328]: A disorder characterized by inflammatory features with neonatal onset, involving the skin, hair, and gut. The skin lesions involve perioral and perianal erythema, psoriasiform erythroderma, with flares of erythema, scaling, and widespread pustules. Gastrointestinal symptoms include malabsorptive diarrhea that is exacerbated by intercurrent gastrointestinal infections. The hair is short or broken, and the eyelashes and eyebrows are wiry and disorganized. {ECO:0000269|PubMed:22010916}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at highest levels in adult heart, placenta, skeletal muscle, pancreas, spleen, thymus, prostate, testes, ovary and small intestine, and in fetal brain, lung, liver and kidney.; ovary;parathyroid;choroid;fovea centralis;retina;uterus;prostate;optic nerve;larynx;thyroid;testis;brain;unclassifiable (Anatomical System);cartilage;urinary;lens;skeletal muscle;breast;lung;placenta;visual apparatus;macula lutea;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.26201 0.38139 0.598963042 82.7789573 436.35159 4.35624 ADAM18 1.53440056708128e-19 0.00144733735817272 0.998552662641827 ADAM metallopeptidase domain 18 FUNCTION: Sperm surface membrane protein that may be involved in spermatogenesis and fertilization. This is a non catalytic metalloprotease-like protein (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed specifically in testis.; unclassifiable (Anatomical System);lung;testis; superior cervical ganglion;testis - interstitial;testis;ciliary ganglion;trigeminal ganglion; 0.06892 0.08196 0.586023223 82.34843123 973.36033 6.03350 ADAM19 4.20155244794664e-06 0.999906953244522 8.8845203030023e-05 ADAM metallopeptidase domain 19 FUNCTION: Participates in the proteolytic processing of beta-type neuregulin isoforms which are involved in neurogenesis and synaptogenesis, suggesting a regulatory role in glial cell. Also cleaves alpha-2 macroglobulin. May be involved in osteoblast differentiation and/or osteoblast activity in bone (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in many normal organ tissues and several cancer cell lines.; unclassifiable (Anatomical System);lung;endometrium;bone;placenta;visual apparatus;blood;kidney;brain;bone marrow; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.71514 0.13137 0.918552705 89.5730125 5188.76456 14.82439 ADAM20 1.79696117345216e-09 0.0646883290013475 0.935311669201691 ADAM metallopeptidase domain 20 FUNCTION: May be involved in sperm maturation and/or fertilization.; . TISSUE SPECIFICITY: Testis specific.; unclassifiable (Anatomical System);testis; testis - interstitial;superior cervical ganglion; 0.04260 0.07231 -0.130380821 44.03161123 104.15833 2.20511 ADAM20P1 . . . ADAM metallopeptidase domain 20 pseudogene 1 . . . . . . . . . . . ADAM20P2 . . . ADAM metallopeptidase domain 20 pseudogene 2 . . . . . . . . . . . ADAM20P3 . . . ADAM metallopeptidase domain 20 pseudogene 3 . . . . . . . . . . . ADAM21 0.0146728762806569 0.957258247949801 0.0280688757695424 ADAM metallopeptidase domain 21 FUNCTION: May be involved in sperm maturation and/or fertilization. May also be involved in epithelia functions associated with establishing and maintaining gradients of ions or nutrients.; . . bone;testis; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.09205 -0.108334733 45.57088936 1492.30576 7.18569 ADAM21P1 . . . ADAM metallopeptidase domain 21 pseudogene 1 . . . . . . 0.09205 . . . . ADAM22 0.999388899396346 0.000611100603435579 2.18704406583797e-13 ADAM metallopeptidase domain 22 FUNCTION: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein (PubMed:19692335). Involved in regulation of cell adhesion and spreading and in inhibition of cell proliferation. Neuronal receptor for LGI1. {ECO:0000269|PubMed:12589811, ECO:0000269|PubMed:15882968, ECO:0000269|PubMed:16385342, ECO:0000269|PubMed:19692335}.; . TISSUE SPECIFICITY: Highly expressed in the brain and in some high-grade but not low-grade gliomas. Detected slightly or not at all in other tissues. {ECO:0000269|PubMed:16385342}.; unclassifiable (Anatomical System);hypothalamus;fovea centralis;choroid;lens;skeletal muscle;skin;retina;optic nerve;lung;frontal lobe;bone;macula lutea;pituitary gland;kidney;brain; amygdala;dorsal root ganglion;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;cerebellum peduncles;temporal lobe;caudate nucleus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;uterus corpus;testis - seminiferous tubule;prefrontal cortex;appendix;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.32606 0.10251 -0.551080959 19.93394669 868.56657 5.74070 ADAM23 0.995404041331662 0.00459595852019307 1.4814439442921e-10 ADAM metallopeptidase domain 23 FUNCTION: May play a role in cell-cell and cell-matrix interactions. This is a non-catalytic metalloprotease-like protein.; . TISSUE SPECIFICITY: Highly expressed in the brain and weakly expressed in the heart. In the brain, expressed prominently in the amygdala, caudate nucleus, hypothalamus, thalamus, cerebral cortex and occipital pole. {ECO:0000269|PubMed:14697522}.; unclassifiable (Anatomical System);cerebellum cortex;muscle;substantia nigra;blood;parathyroid;fovea centralis;choroid;lens;skeletal muscle;skin;retina;bone marrow;uterus;optic nerve;lung;frontal lobe;macula lutea;liver;testis;brain;thymus; amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;temporal lobe;caudate nucleus;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.61616 0.08593 -0.044015879 50.44821892 62.38953 1.61345 ADAM24P . . . ADAM metallopeptidase domain 24, pseudogene . . . . . . . . . . . ADAM28 1.96799528021972e-17 0.0250576248525084 0.974942375147492 ADAM metallopeptidase domain 28 FUNCTION: May play a role in the adhesive and proteolytic events that occur during lymphocyte emigration or may function in ectodomain shedding of lymphocyte surface target proteins, such as FASL and CD40L. May be involved in sperm maturation.; . TISSUE SPECIFICITY: Expressed predominantly in secondary lymphoid tissues, such as lymph node, spleen, small intestine, stomach, colon, appendix and trachea. The lymphocyte population is responsible for expression of this protein in these tissues. Isoform 2 is expressed preferentially in spleen.; unclassifiable (Anatomical System);medulla oblongata;lymph node;ovary;colon;parathyroid;blood;pancreas;lung;endometrium;larynx;thyroid;placenta;liver;testis;head and neck;spleen;germinal center;brain; superior cervical ganglion;lymph node;ciliary ganglion;trigeminal ganglion; 0.14473 0.12451 0.762397607 86.8542109 623.46636 5.03510 ADAM29 4.69432338449837e-07 0.388971687121827 0.611027843445834 ADAM metallopeptidase domain 29 FUNCTION: May be involved in spermatogenesis and fertilization. Seems to be a non catalytic metalloprotease-like protein.; . TISSUE SPECIFICITY: Expressed specifically in testes.; testis;kidney; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09089 0.09580 0.113945049 62.14319415 457.13629 4.44060 ADAM30 0.00193807290428196 0.976020330409258 0.02204159668646 ADAM metallopeptidase domain 30 FUNCTION: May be involved in spermatogenesis and fertilization.; . TISSUE SPECIFICITY: Expressed specifically in testis.; . . 0.03172 . -0.306750577 32.23047889 90.09019 2.04324 ADAM32 1.1677289848388e-08 0.929586071911505 0.0704139164112055 ADAM metallopeptidase domain 32 FUNCTION: May play a role in sperm development and fertilization This is a non-catalytic metalloprotease-like protein. {ECO:0000250}.; . TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12568724}.; . . 0.05738 0.07564 0.380318343 75.63104506 768.55107 5.48756 ADAM33 1.31263464951389e-11 0.516330070318339 0.483669929668535 ADAM metallopeptidase domain 33 . DISEASE: Asthma (ASTHMA) [MIM:600807]: The most common chronic disease affecting children and young adults. It is a complex genetic disorder with a heterogeneous phenotype, largely attributed to the interactions among many genes and between these genes and the environment. It is characterized by recurrent attacks of paroxysmal dyspnea, with wheezing due to spasmodic contraction of the bronchi. {ECO:0000269|PubMed:12110844, ECO:0000269|PubMed:16773130, ECO:0000269|PubMed:19237393}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues, except liver, with high expression in placenta, lung, spleen and veins. {ECO:0000269|PubMed:11814695}.; unclassifiable (Anatomical System);medulla oblongata;islets of Langerhans;skeletal muscle;retina;uterus;whole body;endometrium;cerebral cortex;thyroid;placenta;liver;spleen;spinal ganglion;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.11478 0.14638 0.802845857 87.69167256 1650.79695 7.51245 ADAMDEC1 1.76177869055281e-09 0.385126557610553 0.614873440627668 ADAM-like, decysin 1 FUNCTION: May play an important role in the control of the immune response and during pregnancy. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed highly in the small intestine and appendix, moderately in lymph node, mucosal lining of the colon, thymus, spleen and very weakly in the bone marrow. Predominantly expressed in dendritic cells (DC) of the germinal center. Weakly expressed in monocyte and highly expressed in macrophage. Absent in immature DC. {ECO:0000269|PubMed:14632642, ECO:0000269|PubMed:9271581}.; unclassifiable (Anatomical System);pancreas;lymph node;lung;endometrium;nasopharynx;placenta;colon;skeletal muscle;stomach;tonsil; superior cervical ganglion;appendix;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.11349 0.10309 1.39815152 94.71573484 845.45549 5.68773 ADAMTS1 0.594872990656586 0.405110032081342 1.69772620719667e-05 ADAM metallopeptidase with thrombospondin type 1 motif 1 FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover (By similarity). Has angiogenic inhibitor activity. Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture. {ECO:0000250, ECO:0000269|PubMed:10438512}.; . . smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;gall bladder;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;testis;spinal ganglion;artery;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;duodenum;amnion;head and neck;kidney;aorta;stomach; uterus corpus;superior cervical ganglion;ovary;placenta;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.47523 0.16470 0.073492312 59.170795 530.17853 4.69942 ADAMTS2 0.992213475206961 0.00778652425549657 5.37542634593037e-10 ADAM metallopeptidase with thrombospondin type 1 motif 2 FUNCTION: Cleaves the propeptides of type I and II collagen prior to fibril assembly. Does not act on type III collagen. May also play a role in development that is independent of its role in collagen biosynthesis.; DISEASE: Ehlers-Danlos syndrome 7C (EDS7C) [MIM:225410]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. Marked by extremely fragile tissues, hyperextensible skin and easy bruising. Facial skin contains numerous folds, as in the cutis laxa syndrome. {ECO:0000269|PubMed:10417273}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at high level in skin, bone, tendon and aorta and at low levels in thymus and brain.; unclassifiable (Anatomical System);smooth muscle;heart;ovary;cartilage;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;breast;pancreas;optic nerve;cerebral cortex;placenta;bone;macula lutea;kidney; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.33346 0.31484 -1.800772772 2.217504128 5065.97781 14.58177 ADAMTS3 1.7895345062741e-06 0.99998581912419 1.23913413032494e-05 ADAM metallopeptidase with thrombospondin type 1 motif 3 FUNCTION: Cleaves the propeptides of type II collagen prior to fibril assembly. Does not act on types I and III collagens.; . TISSUE SPECIFICITY: Found in cartilage and skin.; unclassifiable (Anatomical System);bile duct;medulla oblongata;lung;whole body;cerebral cortex;placenta;testis;blood;brain;skeletal muscle; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.22292 0.11688 -0.654057602 16.14177872 316.52138 3.77881 ADAMTS4 0.00546593980671702 0.993483192341882 0.00105086785140109 ADAM metallopeptidase with thrombospondin type 1 motif 4 FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Could also be a critical factor in the exacerbation of neurodegeneration in Alzheimer disease. Cleaves aggrecan at the '392-Glu-|-Ala-393' site.; . TISSUE SPECIFICITY: Expressed in brain, lung and heart. Expressed at very low level in placenta and skeletal muscles. Isoform 2 is detected in osteoarthritic synovium. {ECO:0000269|PubMed:23897278}.; . . 0.08465 0.19320 0.093718683 60.71007313 450.79979 4.41169 ADAMTS5 0.118850233550657 0.880919637265919 0.000230129183423667 ADAM metallopeptidase with thrombospondin type 1 motif 5 FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. May play a role in proteolytic processing mostly during the peri-implantation period.; . TISSUE SPECIFICITY: Expressed at low level in placenta primarily but also detected in heart and brain, cervix, uterus, bladder, esophagus, rib cartilage, chondroblastoma, fibrous tissue and a joint capsule from an arthritic patient.; unclassifiable (Anatomical System);prostate;whole body;ovary;heart;endometrium;placenta;liver;parathyroid;cervix;kidney;mammary gland;skeletal muscle; uterus corpus;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.37293 0.25159 0.248041348 69.61547535 2503.4233 9.32438 ADAMTS6 0.998800472645028 0.00119952735384065 1.13154764092226e-12 ADAM metallopeptidase with thrombospondin type 1 motif 6 . . TISSUE SPECIFICITY: Expressed at low levels in placenta and barely detectable in a number of other tissues.; unclassifiable (Anatomical System);heart;colon;skeletal muscle;skin;bile duct;uterus;whole body;lung;placenta;liver;testis;spleen;brain; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.43090 0.11953 -0.574945567 18.90186365 218.20018 3.19214 ADAMTS7 2.98948787387487e-07 0.999966964385075 3.27366661373355e-05 ADAM metallopeptidase with thrombospondin type 1 motif 7 FUNCTION: Metalloprotease that may play a role in the degradation of COMP. {ECO:0000269|PubMed:16585064}.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Detected in meniscus, bone, tendon, cartilage, synovium, fat and ligaments. {ECO:0000269|PubMed:15192113, ECO:0000269|PubMed:16585064}.; . . 0.12246 0.11080 2.519370135 98.68483133 1800.79348 7.82795 ADAMTS7P1 . . . ADAMTS7 pseudogene 1 . . . . . . . . . . . ADAMTS7P3 . . . ADAMTS7 pseudogene 3 . . . . . . . . . . . ADAMTS7P4 . . . ADAMTS7 pseudogene 4 . . . . . . . . . . . ADAMTS8 1.0556522196896e-08 0.519106063434829 0.480893926008649 ADAM metallopeptidase with thrombospondin type 1 motif 8 FUNCTION: Has anti-angiogenic properties.; . TISSUE SPECIFICITY: Highly expressed in adult and fetal lung, lower expression in brain, placenta, heart, stomach and fetal brain and kidney.; unclassifiable (Anatomical System);heart;cartilage;colon;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;lung;endometrium;placenta;macula lutea;liver;testis;spleen;brain; superior cervical ganglion;skeletal muscle; 0.26967 0.12334 0.672386703 84.73696627 4169.48922 12.82299 ADAMTS9 4.22655241635146e-07 0.999999577333435 1.13228883651602e-11 ADAM metallopeptidase with thrombospondin type 1 motif 9 FUNCTION: Cleaves the large aggregating proteoglycans, aggrecan and versican. Has a protease-independent function in promoting the transport from the endoplasmic reticulum to the Golgi apparatus of a variety of secretory cargos. {ECO:0000269|PubMed:12514189, ECO:0000269|PubMed:22419820}.; . TISSUE SPECIFICITY: Highly expressed in all fetal tissues. Expressed in a number of adult tissues with highest expression in heart, placenta and skeletal muscle.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;skin;uterus;prostate;cochlea;cerebral cortex;endometrium;larynx;thyroid;bone;iris;testis;dura mater;spinal ganglion;brain;unclassifiable (Anatomical System);meninges;heart;islets of Langerhans;skeletal muscle;breast;pancreas;pia mater;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.19769 . -2.392891714 1.079263977 1650.36492 7.50995 ADAMTS9-AS1 . . . ADAMTS9 antisense RNA 1 . . . . . . . . . . . ADAMTS9-AS2 . . . ADAMTS9 antisense RNA 2 . . . . . . . . . . . ADAMTS10 0.980346240233128 0.0196537587113703 1.05550174381065e-09 ADAM metallopeptidase with thrombospondin type 1 motif 10 FUNCTION: Metalloprotease that participate in microfibrils assembly. Microfibrils are extracellular matrix components occurring independently or along with elastin in the formation of elastic tissues. {ECO:0000269|PubMed:21402694}.; DISEASE: Weill-Marchesani syndrome 1 (WMS1) [MIM:277600]: A rare connective tissue disorder characterized by short stature, brachydactyly, joint stiffness, and eye abnormalities including microspherophakia, ectopia lentis, severe myopia and glaucoma. {ECO:0000269|PubMed:15368195, ECO:0000269|PubMed:18567016}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed in adult tissues. {ECO:0000269|PubMed:15355968}.; unclassifiable (Anatomical System);medulla oblongata;heart;ovary;islets of Langerhans;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;lung;larynx;placenta;hippocampus;testis;spleen;kidney;brain;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.28833 0.12054 -1.320975027 4.777070064 877.25152 5.76576 ADAMTS12 1.53777100809711e-11 0.999347073456606 0.000652926528016208 ADAM metallopeptidase with thrombospondin type 1 motif 12 FUNCTION: Metalloprotease that may play a role in the degradation of COMP. Cleaves also alpha-2 macroglobulin and aggregan. Has anti-tumorigenic properties. {ECO:0000269|PubMed:16611630, ECO:0000269|PubMed:17895370, ECO:0000269|PubMed:18485748}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle and fat. Detected at significant levels in fetal lung. Widely expressed in gastric carcinomas and in cancer cells of diverse origin. {ECO:0000269|PubMed:11279086, ECO:0000269|PubMed:16611630}.; unclassifiable (Anatomical System);ovary;salivary gland;pharynx;colon;blood;breast;pancreas;prostate;whole body;lung;bone;visual apparatus;liver;testis;kidney;brain;bladder; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.10893 0.12072 0.865222355 88.74734607 1284.68357 6.74639 ADAMTS13 7.88296728194754e-11 0.998477307988055 0.00152269193311512 ADAM metallopeptidase with thrombospondin type 1 motif 13 FUNCTION: Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation. {ECO:0000269|PubMed:19880749}.; DISEASE: Thrombotic thrombocytopenic purpura congenital (TTP) [MIM:274150]: A hematologic disease characterized by hemolytic anemia with fragmentation of erythrocytes, thrombocytopenia, diffuse and non-focal neurologic findings, decreased renal function and fever. recessive. {ECO:0000269|PubMed:11586351, ECO:0000269|PubMed:12181489, ECO:0000269|PubMed:12393505, ECO:0000269|PubMed:12614216, ECO:0000269|PubMed:12753286, ECO:0000269|PubMed:14512317, ECO:0000269|PubMed:14563640, ECO:0000269|PubMed:15009458, ECO:0000269|PubMed:15126318, ECO:0000269|PubMed:15327386, ECO:0000269|PubMed:16449289, ECO:0000269|PubMed:16453338, ECO:0000269|PubMed:16796708, ECO:0000269|PubMed:16807643, ECO:0000269|PubMed:17003922, ECO:0000269|PubMed:18443791, ECO:0000269|PubMed:19055667, ECO:0000269|PubMed:19116307, ECO:0000269|PubMed:22075512}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma. Expressed primarily in liver. {ECO:0000269|PubMed:11574066}.; unclassifiable (Anatomical System);bile duct;lung;ovary;thyroid;liver;testis;colon;spleen;blood;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.06820 0.12877 0.622690987 83.42179759 2255.36428 8.77522 ADAMTS14 2.33178919110162e-06 0.999989194483227 8.47372758187597e-06 ADAM metallopeptidase with thrombospondin type 1 motif 14 FUNCTION: Has a aminoprocollagen type I activity processing activity in the absence of ADAMTS2. Seems to be synthesized as a latent enzyme that requires activation to display aminoprocollagen peptidase activity.; . TISSUE SPECIFICITY: Expressed in retina and at low levels in brain, lung and placenta. High expression in fetal tissues.; . . 0.21639 0.12333 -0.5513802 19.86907289 5123.0958 14.71781 ADAMTS15 0.679914358287786 0.320077747321859 7.89439035514605e-06 ADAM metallopeptidase with thrombospondin type 1 motif 15 . . TISSUE SPECIFICITY: Expressed in fetal liver and kidney, but not in any of the adult tissues examined.; unclassifiable (Anatomical System); superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.34645 0.14568 0.676034544 84.75465912 1106.31138 6.35706 ADAMTS16 0.00108650288416212 0.998912753603857 7.4351198103796e-07 ADAM metallopeptidase with thrombospondin type 1 motif 16 . . TISSUE SPECIFICITY: Expressed in fetal lung and kidney and in adult prostate and ovary.; unclassifiable (Anatomical System);lymph node;brain; superior cervical ganglion;occipital lobe;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.15638 0.13210 0.679686641 84.77235197 6129.25449 16.35226 ADAMTS17 3.82852764002745e-11 0.995733612657531 0.0042663873041835 ADAM metallopeptidase with thrombospondin type 1 motif 17 . DISEASE: Weill-Marchesani-like syndrome (WMLS) [MIM:613195]: A disorder characterized by many of the key features of Weill- Marchesani syndrome, including lenticular myopia, ectopia lentis, glaucoma, spherophakia and short stature. However, the characteristic brachydactyly or decreased joint flexibility of Weill-Marchesani syndrome are absent. {ECO:0000269|PubMed:19836009}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed at high levels in the lung, brain, whole eye and retina. Isoform 1 shows a weaker expression in the heart, kidney and skeletal muscle. Isoform 2 shows a weaker expression in the kidney, bone marrow and skeletal muscle. Isoform 1 and isoform 2 are expressed at high levels in the fetal heart, kidney, and whole eye, whereas a weak expression is seen in the fetal liver. {ECO:0000269|PubMed:19836009}.; unclassifiable (Anatomical System);lung;testis;germinal center;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;caudate nucleus;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.24727 0.12398 -2.267592656 1.262090116 3746.43136 11.97553 ADAMTS18 3.73935058124161e-15 0.998600619877864 0.00139938012213193 ADAM metallopeptidase with thrombospondin type 1 motif 18 . DISEASE: Microcornea, myopic chorioretinal atrophy, and telecanthus (MMCAT) [MIM:615458]: A ocular syndrome characterized by microcornea and myopic chorioretinal atrophy. Microcornea is defined by a corneal diameter inferior to 10 mm in both meridians in an otherwise normal eye. In addition to ocular findings, some patients have telecanthus and posteriorly rotated ears. {ECO:0000269|PubMed:23818446}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in fetal lung, liver, and kidney and in adult brain, prostate, submaxillary gland, and endothelium.; unclassifiable (Anatomical System);optic nerve;lung;heart;endometrium;placenta;macula lutea;fovea centralis;choroid;lens;brain;mammary gland;retina; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.23474 0.09538 -0.088332259 46.99811276 12292.96848 23.77511 ADAMTS19 0.951958940870202 0.0480410590493409 8.04570611301923e-11 ADAM metallopeptidase with thrombospondin type 1 motif 19 . . TISSUE SPECIFICITY: Expressed in fetal lung, but not in any adult tissues examined. Expression was detected in an osteosarcoma cDNA library.; unclassifiable (Anatomical System);endometrium;liver;spleen;brain;retina; dorsal root ganglion;testis - interstitial;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.33648 0.10613 -0.551080959 19.93394669 2267.7401 8.80379 ADAMTS19-AS1 . . . ADAMTS19 antisense RNA 1 . . . . . . . . . . . ADAMTS20 4.85371907276584e-26 0.783183920088199 0.216816079911801 ADAM metallopeptidase with thrombospondin type 1 motif 20 FUNCTION: May play a role in tissue-remodeling process occurring in both normal and pathological conditions. May have a protease- independent function in the transport from the endoplasmic reticulum to the Golgi apparatus of secretory cargos, mediated by the GON domain.; . TISSUE SPECIFICITY: Very sparingly expressed, although is detected at low levels in testis, prostate, ovary, heart, placenta, lung and pancreas. Overexpressed in several brain, colon and breast carcinomas.; . . 0.14489 0.09297 -0.753453827 13.58221279 1152.89729 6.46984 ADAMTSL1 8.82648695835544e-05 0.999911689198669 4.59317470374525e-08 ADAMTS like 1 . . TISSUE SPECIFICITY: Expressed primarily in adult skeletal muscle. {ECO:0000269|PubMed:11805097}.; unclassifiable (Anatomical System);uterus;prostate;lung;cartilage;ovary;heart;bone;duodenum;testis;spleen;brain;skin; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; . . -0.860112269 10.89879689 3092.36494 10.57060 ADAMTSL2 0.0710586670580913 0.916004047794054 0.012937285147855 ADAMTS like 2 . DISEASE: Geleophysic dysplasia 1 (GPHYSD1) [MIM:231050]: An autosomal recessive disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening. Radiologic features include delayed bone age, cone- shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies. Affected individuals have characteristic facial features including a 'happy' face with full cheeks, shortened nose, hypertelorism, long and flat philtrum, and thin upper lip. Other distinctive features include progressive cardiac valvular thickening often leading to an early death, toe walking, tracheal stenosis, respiratory insufficiency, and lysosomal-like storage vacuoles in various tissues. {ECO:0000269|PubMed:18677313, ECO:0000269|PubMed:21415077}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);breast;lung;islets of Langerhans;visual apparatus;colon;spleen;kidney;spinal ganglion;brain;skeletal muscle;stomach; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.26032 0.11516 . . 74.41925 1.80297 ADAMTSL3 9.55133265504144e-09 0.999999674987328 3.15461339613582e-07 ADAMTS like 3 . . TISSUE SPECIFICITY: Expressed in epithelial cells of the colon, fallopian tube, skin, breast, prostate, epididymis, liver, pancreatic islets and bile ducts, as well as by vascular endothelial cells, smooth muscle cells, fibroblasts, cortical and ganglionic neurons and cardiac myocytes. Also expressed by malignant epithelial cells in colon cancer, as well as breast, prostate, renal and skin tumors. Expression is significantly reduced in colon cancer compared to normal colon. {ECO:0000269|PubMed:14667842, ECO:0000269|PubMed:17597111}.; unclassifiable (Anatomical System);heart;colon;skin;skeletal muscle;uterus;prostate;whole body;lung;thyroid;placenta;visual apparatus;iris;liver;testis;spleen;brain;aorta;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;skin; 0.29754 0.10931 0.334233824 73.62585515 5035.60394 14.49965 ADAMTSL4 7.08734668179842e-16 0.34016241960008 0.659837580399919 ADAMTS like 4 FUNCTION: Positive regulation of apoptosis. May facilitate FBN1 microfibril biogenesis. {ECO:0000269|PubMed:16364318, ECO:0000269|PubMed:21989719}.; DISEASE: Ectopia lentis 2, isolated, autosomal recessive (ECTOL2) [MIM:225100]: An ocular abnormality characterized by partial or complete displacement of the lens from its space resulting from defective zonule formation. {ECO:0000269|PubMed:19200529}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ectopia lentis et pupillae (ECTOLP) [MIM:225200]: An ocular abnormality characterized by displacement of the lenses and the pupils, associated with other ocular anomalies, but without systemic manifestations. The condition is usually bilateral, with the lenses and pupils displaced in opposite directions. Additional signs include enlarged corneal diameter, increased corneal astigmatism, increased anterior chamber depth, thinning and flattening of the iris with loss of crypts, angle malformation caused by enlarged iris processes, persistent pupillary membrane, loss of zonular fibers, tilted disk, and increased axial length. Secondary manifestations include refractive errors, glaucoma, early cataract development, and retinal detachment. Membrane formation on the posterior aspect of the iris has been observed both in histologic sections and on ultrasound biomicroscopy. {ECO:0000269|PubMed:20702823}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in colon, heart, leukocyte, liver, lung, skeletal muscle, spleen, testis and placenta. Weaker expression in bone marrow, brain tissue, kidney and pancreas. Expression studies in fetal tissues reveal strong expression in heart, kidney, liver, lung and skeletal muscle, but weaker expression in fetal brain and skin. {ECO:0000269|PubMed:19200529}.; ovary;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;urinary;blood;breast;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;tongue;placenta;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10654 0.09865 -0.00377668 53.51497995 1103.99507 6.35130 ADAMTSL4-AS1 . . . ADAMTSL4 antisense RNA 1 . . . . . 0.16311 . . . 51.27838 1.41213 ADAMTSL5 3.22271116895574e-10 0.0863905009430829 0.913609498734646 ADAMTS like 5 FUNCTION: May play a role in modulation of fibrillin microfibrils in the extracellular matrix (ECM).; . . unclassifiable (Anatomical System);uterus;myocardium;lung;ovary;placenta;testis;parathyroid;cervix;brain;skin; . 0.15136 0.10435 0.442818085 77.8544468 191.46176 3.00098 ADAP1 0.65792685435534 0.341835895046481 0.000237250598179494 ArfGAP with dual PH domains 1 FUNCTION: GTPase-activating protein for the ADP ribosylation factor family (Probable). Binds phosphatidylinositol 3,4,5- trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4). {ECO:0000269|PubMed:10448098, ECO:0000303|PubMed:10333475, ECO:0000305}.; . TISSUE SPECIFICITY: Expressed at highest levels in brain and at lower levels in peripheral blood leukocytes. {ECO:0000269|PubMed:10448098}.; unclassifiable (Anatomical System);amygdala;lymph node;ovary;colon;parathyroid;pancreas;optic nerve;whole body;lung;frontal lobe;endometrium;oesophagus;bone;placenta;liver;testis;cervix;spleen;kidney;brain;mammary gland;stomach;cerebellum; . 0.17754 0.12827 -0.933156985 9.54824251 48.02044 1.34684 ADAP2 3.98271958834599e-05 0.954235132161878 0.0457250406422385 ArfGAP with dual PH domains 2 FUNCTION: GTPase-activating protein for the ADP ribosylation factor family (Potential). Binds phosphatidylinositol 3,4,5- trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4). Possesses a stoichiometry of two binding sites for InsP4 with identical affinity. {ECO:0000269|PubMed:14690521, ECO:0000305}.; . TISSUE SPECIFICITY: Highly expressed in placenta, spleen, kidney, skeletal muscle and adrenal gland. Weakly expressed in thyroid, liver, heart, lung, small intestine, peripheral blood leukocytes. Not detected in spinal cord, brain, stomach, trachea, colon, lymph node and bone marrow. {ECO:0000269|PubMed:14690521}.; unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;choroid;skin;uterus;prostate;whole body;lung;endometrium;oesophagus;bone;placenta;liver;testis;germinal center;kidney;brain;stomach; superior cervical ganglion; 0.08301 0.11577 -0.449946534 24.00330267 116.51213 2.34763 ADAR 0.907595373477161 0.0924045753521101 5.11707289327527e-08 adenosine deaminase, RNA-specific FUNCTION: Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer- associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV), measles virus (MV), hepatitis delta virus (HDV), and human immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV, MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be editing-dependent (HDV and HCV), editing-independent (VSV and MV) or both (HIV-1). Impairs HCV replication via RNA editing at multiple sites. Enhances the replication of MV, VSV and HIV-1 through an editing- independent mechanism via suppression of EIF2AK2/PKR activation and function. Stimulates both the release and infectivity of HIV-1 viral particles by an editing-dependent mechanism where it associates with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat coding sequence. Can enhance viral replication of HDV via A-to-I editing at a site designated as amber/W, thereby changing an UAG amber stop codon to an UIG tryptophan (W) codon that permits synthesis of the large delta antigen (L-HDAg) which has a key role in the assembly of viral particles. However, high levels of ADAR1 inhibit HDV replication. {ECO:0000269|PubMed:15556947, ECO:0000269|PubMed:15858013, ECO:0000269|PubMed:16475990, ECO:0000269|PubMed:17079286, ECO:0000269|PubMed:19605474, ECO:0000269|PubMed:19651874, ECO:0000269|PubMed:19710021, ECO:0000269|PubMed:19908260, ECO:0000269|PubMed:21289159, ECO:0000269|PubMed:22278222}.; DISEASE: Dyschromatosis symmetrica hereditaria (DSH) [MIM:127400]: An autosomal dominant pigmentary genodermatosis characterized by a mixture of hyperpigmented and hypopigmented macules distributed on the face and the dorsal parts of the hands and feet, that appear in infancy or early childhood. {ECO:0000269|PubMed:12916015, ECO:0000269|PubMed:15146470, ECO:0000269|PubMed:15659327}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Aicardi-Goutieres syndrome 6 (AGS6) [MIM:615010]: A form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood. {ECO:0000269|PubMed:23001123}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed, highest levels were found in brain and lung. Isoform 5 is expressed at higher levels in astrocytomas as compared to normal brain tissue and expression increases strikingly with the severity of the tumor, being higher in the most aggressive tumors. {ECO:0000269|PubMed:18178553}.; medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;liver;alveolus;spleen;cervix;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus; amygdala;occipital lobe;medulla oblongata;hypothalamus;prefrontal cortex;pons;caudate nucleus;whole blood;parietal lobe;cingulate cortex; 0.12280 0.23648 -0.639268965 16.70794999 78.80238 1.87521 ADARB1 0.843939346822973 0.155939433304466 0.000121219872560808 adenosine deaminase, RNA specific B1 FUNCTION: Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer- associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2 and GRIK2) and serotonin (HTR2C), GABA receptor (GABRA3) and potassium voltage-gated channel (KCNA1). Site- specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alter their functional activities. Edits GRIA2 at both the Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently. Can exert a proviral effect towards human immunodeficiency virus type 1 (HIV-1) and enhances its replication via both an editing-dependent and editing-independent mechanism. The former involves editing of adenosines in the 5'UTR while the latter occurs via suppression of EIF2AK2/PKR activation and function. Can inhibit cell proliferation and migration and can stimulate exocytosis. {ECO:0000269|PubMed:18178553, ECO:0000269|PubMed:19908260, ECO:0000269|PubMed:21289159}.; . TISSUE SPECIFICITY: Highly expressed in brain and heart and at lower levels in placenta. Fair expression in lung, liver and kidney. Detected in brain, heart, kidney, lung and liver (at protein level). Isoform 5 is high expressed in hippocampus and colon. Isoform 5 is expressed in pediatric astrocytomas and the protein has a decreased RNA-editing activity. The decrease in RNA editing correlates with the grade of malignancy of the tumors, with the high grade tumors showing lower editing is seen. {ECO:0000269|PubMed:18178553, ECO:0000269|PubMed:19156214, ECO:0000269|PubMed:9149227}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;uterus;prostate;frontal lobe;cochlea;cerebral cortex;endometrium;bone;iris;testis;germinal center;brain;amygdala;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum;peripheral nerve; superior cervical ganglion;subthalamic nucleus;thalamus;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle;cerebellum; 0.28156 0.13431 -0.800872469 12.33191791 35.57047 1.07201 ADARB2 0.738168861452959 0.261726193228338 0.000104945318703423 adenosine deaminase, RNA specific B2 (inactive) FUNCTION: Lacks editing activity. It prevents the binding of other ADAR enzymes to targets in vitro, and decreases the efficiency of these enzymes. Capable of binding to dsRNA but also to ssRNA.; . TISSUE SPECIFICITY: Brain specific. Expressed at higher levels in astrocytomas as compared to the normal brain tissue. {ECO:0000269|PubMed:10836796, ECO:0000269|PubMed:18178553}.; . . 0.18882 0.14637 -0.505170032 21.79759377 584.19726 4.90127 ADARB2-AS1 . . . ADARB2 antisense RNA 1 . . . . . . . . . . . ADAT1 6.80340090282039e-11 0.125935813158652 0.874064186773314 adenosine deaminase, tRNA specific 1 FUNCTION: Specifically deaminates adenosine-37 to inosine in tRNA- Ala.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10430867}.; medulla oblongata;ovary;salivary gland;intestine;colon;skin;prostate;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach; . 0.13054 0.10094 0.801024817 87.65628686 851.33605 5.70091 ADAT2 2.09083702776258e-08 0.0737194747924073 0.926280504299222 adenosine deaminase, tRNA specific 2 FUNCTION: Probably participates in deamination of adenosine-34 to inosine in many tRNAs. {ECO:0000250}.; . . smooth muscle;cartilage;ovary;heart;urinary;colon;parathyroid;blood;skin;uterus;pancreas;prostate;lung;endometrium;bone;thyroid;placenta;liver;testis;head and neck;germinal center;kidney; globus pallidus;ciliary ganglion;trigeminal ganglion; 0.33152 0.15545 0.193034296 66.82000472 44.95237 1.28760 ADAT3 0.0011796465942971 0.395969706249408 0.602850647156295 adenosine deaminase, tRNA specific 3 . DISEASE: Mental retardation, autosomal recessive 36 (MRT36) [MIM:615286]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT36 is often associated with esotropia and failure to thrive. Other more variable features included microcephaly, hypotonia, and mild brain abnormalities on MRI, such as dilated ventricles or delayed myelination. {ECO:0000269|PubMed:23620220}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;skin;uterus;pancreas;prostate;lung;endometrium;synovium;bone;placenta;testis;spleen;kidney;brain;stomach;thymus; . 0.22536 0.11591 . . 122.52264 2.41022 ADCK1 4.22838319274286e-09 0.343895614734953 0.656104381036664 aarF domain containing kinase 1 FUNCTION: The function of this protein is not yet clear. It is not known if it has protein kinase activity and what type of substrate it would phosphorylate (Ser, Thr or Tyr).; . . ovary;salivary gland;intestine;colon;skin;retina;bone marrow;optic nerve;frontal lobe;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;pharynx;blood;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.14997 0.13437 -1.151821487 6.269167256 108.84954 2.26530 ADCK2 0.000169237561936908 0.970344681236002 0.0294860812020612 aarF domain containing kinase 2 FUNCTION: The function of this protein is not yet clear. It is not known if it has protein kinase activity and what type of substrate it would phosphorylate (Ser, Thr or Tyr).; . . ovary;colon;parathyroid;skin;bone marrow;prostate;optic nerve;frontal lobe;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;adrenal cortex;blood;pancreas;lung;placenta;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach; dorsal root ganglion;whole brain;superior cervical ganglion;subthalamic nucleus;adrenal cortex;globus pallidus;atrioventricular node;trigeminal ganglion;skin;parietal lobe;skeletal muscle; 0.13361 0.09623 0.692611128 85.26185421 4261.73957 12.98329 ADCK3 1.23500239562904e-05 0.950728500761156 0.0492591492148877 aarF domain containing kinase 3 FUNCTION: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration (PubMed:25498144). Its substrate specificity is unclear: either acts as protein kinase that phosphorylates other proteins in the CoQ complex to stabilize their interactions or acts as a small molecule kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway (PubMed:25498144). Shows an unusual selectivity for binding ADP over ATP (PubMed:25498144). {ECO:0000269|PubMed:25498144, ECO:0000305|PubMed:21296186, ECO:0000305|PubMed:25540914}.; DISEASE: Coenzyme Q10 deficiency, primary, 4 (COQ10D4) [MIM:612016]: An autosomal recessive disorder characterized by childhood-onset of cerebellar ataxia and exercise intolerance. Patient manifest gait ataxia and cerebellar atrophy with slow progression. Additional features include brisk tendon reflexes and Hoffmann sign, variable psychomotor retardation and variable seizures. {ECO:0000269|PubMed:18319072, ECO:0000269|PubMed:18319074, ECO:0000269|PubMed:20580948, ECO:0000269|PubMed:22036850, ECO:0000269|PubMed:24048965, ECO:0000269|PubMed:24218524}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, with highest levels in adrenal gland, heart, pancreas, nasal mucosa, stomach, uterus and skeletal muscle. {ECO:0000269|PubMed:24270420}.; . . 0.12524 0.17185 -1.701282638 2.553668318 307.38989 3.73084 ADCK4 1.82146592255622e-07 0.862776564677841 0.137223253175566 aarF domain containing kinase 4 FUNCTION: May play a role in CoQ10 (COQ10A and/or COQ10B) biosynthesis, which is required for podocyte migration. {ECO:0000269|PubMed:24270420}.; . TISSUE SPECIFICITY: Widely expressed, including renal podocytes. {ECO:0000269|PubMed:24270420}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.13742 0.09814 0.025760883 55.78556263 3460.70894 11.32058 ADCK5 0.908275225235627 0.0916948498456109 2.99249187620909e-05 aarF domain containing kinase 5 FUNCTION: The function of this protein is not yet clear. It is not known if it has protein kinase activity and what type of substrate it would phosphorylate (Ser, Thr or Tyr).; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;synovium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;urinary;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; . 0.17130 0.11136 -0.003562597 53.72729417 44.87494 1.28581 ADCP1 . . . adenosine deaminase complexing protein 1 . . . . . . . . . . . ADCY1 0.999909620125574 9.03798731863082e-05 1.23973728726918e-12 adenylate cyclase 1 (brain) FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates responses to increased cellular Ca(2+)/calmodulin levels (By similarity). May be involved in regulatory processes in the central nervous system. May play a role in memory and learning. Plays a role in the regulation of the circadian rhythm of daytime contrast sensitivity probably by modulating the rhythmic synthesis of cyclic AMP in the retina (By similarity). {ECO:0000250|UniProtKB:O88444, ECO:0000250|UniProtKB:P19754}.; DISEASE: Deafness, autosomal recessive, 44 (DFNB44) [MIM:610154]: A form of non-syndromic deafness characterized by prelingual profound hearing loss affecting all frequencies. {ECO:0000269|PubMed:24482543}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in zona glomerulosa and zona fasciculata in the adrenal gland (at protein level) (PubMed:11549699). Brain, retina and adrenal medulla. {ECO:0000269|PubMed:11549699, ECO:0000269|PubMed:8314585}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;optic nerve;frontal lobe;endometrium;bone;testis;brain;gall bladder;unclassifiable (Anatomical System);amygdala;heart;tongue;islets of Langerhans;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;kidney;aorta;peripheral nerve;cerebellum; amygdala;dorsal root ganglion;whole brain;medulla oblongata;superior cervical ganglion;testis - interstitial;occipital lobe;cerebellum peduncles;temporal lobe;atrioventricular node;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;pancreas;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.28180 0.18088 -1.394367777 4.246284501 147.4195 2.64587 ADCY2 0.999995485664533 4.51433546301327e-06 4.14006687409698e-15 adenylate cyclase 2 (brain) FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:15385642). Down-stream signaling cascades mediate changes in gene expression patterns and lead to increased IL6 production. Functions in signaling cascades downstream of the muscarinic acetylcholine receptors (By similarity). {ECO:0000250|UniProtKB:P26769, ECO:0000269|PubMed:15385642}.; . TISSUE SPECIFICITY: Detected in zona glomerulosa and zona fasciculata in the adrenal gland (at protein level) (PubMed:11549699). Expressed in brain, especially in caudate nucleus, cerebellum and hippocampus. {ECO:0000269|PubMed:11549699, ECO:0000269|PubMed:8476432}.; ovary;sympathetic chain;colon;parathyroid;skin;retina;uterus;prostate;frontal lobe;larynx;bone;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;tongue;skeletal muscle;lung;placenta;hippocampus;liver;head and neck;kidney;mammary gland;stomach; whole brain;dorsal root ganglion;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;olfactory bulb;pons;caudate nucleus;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;amygdala;testis - interstitial;hypothalamus;temporal lobe;spinal cord;atrioventricular node;skeletal muscle;prefrontal cortex;parietal lobe;cerebellum; 0.47816 0.66526 0.115764778 62.17268224 952.7516 5.97422 ADCY3 0.00137930101469091 0.998607816785181 1.28822001276532e-05 adenylate cyclase 3 FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Participates in signaling cascades triggered by odorant receptors via its function in cAMP biosynthesis. Required for the perception of odorants. Required for normal sperm motility and normal male fertility. Plays a role in regulating insulin levels and body fat accumulation in response to a high fat diet. {ECO:0000250|UniProtKB:Q8VHH7}.; . TISSUE SPECIFICITY: Detected in zona glomerulosa and zona fasciculata in the adrenal gland (at protein level) (PubMed:11549699). Expressed in brain, heart, kidney, liver, lung, pancreas islets, placenta, and skeletal muscle (PubMed:9920776). Detected in testis (PubMed:15705663). {ECO:0000269|PubMed:11549699, ECO:0000269|PubMed:15705663, ECO:0000269|PubMed:9920776}.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;nervous;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;medulla oblongata;thalamus;cerebellum peduncles;atrioventricular node;caudate nucleus;pons;skeletal muscle;skin;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.41530 0.17712 -2.166248113 1.421325784 67.64616 1.70126 ADCY4 2.37957783954271e-13 0.833269512155398 0.166730487844364 adenylate cyclase 4 FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. {ECO:0000250|UniProtKB:P26770}.; . TISSUE SPECIFICITY: Detected in the zona glomerulosa and the zona fasciculata in the adrenal gland (at protein level). {ECO:0000269|PubMed:11549699}.; unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;colon;blood;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;prostate;optic nerve;whole body;lung;oesophagus;endometrium;bone;placenta;macula lutea;liver;testis;spinal ganglion;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09003 0.16481 -2.320657243 1.191318707 243.68866 3.36937 ADCY5 0.989940591837607 0.0100594071559776 1.00641517230087e-09 adenylate cyclase 5 FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:15385642, PubMed:26206488, PubMed:24700542). Mediates signaling downstream of ADRB1 (PubMed:24700542). Regulates the increase of free cytosolic Ca(2+) in response to increased blood glucose levels and contributes to the regulation of Ca(2+)-dependent insulin secretion (PubMed:24740569). {ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:24700542, ECO:0000269|PubMed:24740569, ECO:0000269|PubMed:26206488}.; DISEASE: Dyskinesia, familial, with facial myokymia (FDFM) [MIM:606703]: A disorder characterized by predominantly perioral and periorbital myokymia, and face, neck and upper limb dystonic/choreic movements. Initially paroxysmal and worsened by stress, the dyskinetic episodes become nearly constant by the end of the third decade of life, but in some individuals, they may diminish in frequency and severity at older ages. {ECO:0000269|PubMed:22782511, ECO:0000269|PubMed:24700542}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in pancreas islets (at protein level). Detected in pancreas islets. {ECO:0000269|PubMed:24740569}.; unclassifiable (Anatomical System);lung;ovary;heart;placenta;visual apparatus;testis;colon;brain;skeletal muscle; medulla oblongata;superior cervical ganglion;heart;pons;caudate nucleus;cingulate cortex; 0.41750 0.23330 -2.388633592 1.096956829 125.84683 2.44244 ADCY6 0.596680215378215 0.403319099966931 6.84654854130829e-07 adenylate cyclase 6 FUNCTION: Catalyzes the formation of the signaling molecule cAMP downstream of G protein-coupled receptors (PubMed:17916776, PubMed:17110384). Functions in signaling cascades downstream of beta-adrenergic receptors in the heart and in vascular smooth muscle cells (PubMed:17916776). Functions in signaling cascades downstream of the vasopressin receptor in the kidney and has a role in renal water reabsorption. Functions in signaling cascades downstream of PTH1R and plays a role in regulating renal phosphate excretion. Functions in signaling cascades downstream of the VIP and SCT receptors in pancreas and contributes to the regulation of pancreatic amylase and fluid secretion (By similarity). Signaling mediates cAMP-dependent activation of protein kinase PKA. This promotes increased phosphorylation of various proteins, including AKT. Plays a role in regulating cardiac sarcoplasmic reticulum Ca(2+) uptake and storage, and is required for normal heart ventricular contractibility. May contribute to normal heart function (By similarity). Mediates vasodilatation after activation of beta-adrenergic receptors by isoproterenol (PubMed:17916776). Contributes to bone cell responses to mechanical stimuli (By similarity). {ECO:0000250|UniProtKB:Q01341, ECO:0000250|UniProtKB:Q03343, ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:17916776}.; DISEASE: Lethal congenital contracture syndrome 8 (LCCS8) [MIM:616287]: A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy and congenital non-progressive joint contractures. The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth. LCCS8 is an axoglial form of arthrogryposis multiplex congenita, characterized by congenital distal joint contractures, reduced fetal movements, and severe motor paralysis leading to death early in the neonatal period. {ECO:0000269|PubMed:24319099}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in peripheral blood mononuclear leukocytes (at protein level) (PubMed:17916776). Detected in thyroid (PubMed:10978539). {ECO:0000269|PubMed:10978539}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; subthalamic nucleus;superior cervical ganglion;skeletal muscle; 0.64506 0.21882 -1.186862251 5.90351498 416.84443 4.27229 ADCY7 0.0177212075002422 0.982271061033918 7.73146583973407e-06 adenylate cyclase 7 FUNCTION: This is a membrane-bound, calcium-inhibitable adenylyl cyclase.; . . lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;aorta;stomach; fetal liver;white blood cells;atrioventricular node; 0.48075 0.20313 -3.024935465 0.513092711 174.16027 2.87175 ADCY8 0.0029856615213929 0.997010104528867 4.23394973973391e-06 adenylate cyclase 8 (brain) FUNCTION: This is a membrane-bound, calcium-stimulable adenylyl cyclase. May be involved in learning, in memory and in drug dependence (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in brain cortex. {ECO:0000269|PubMed:1715695}.; unclassifiable (Anatomical System);lymphoreticular;lung;frontal lobe;thyroid;spinal cord;testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;skeletal muscle; 0.67666 0.19224 -1.280491183 5.16631281 283.87581 3.60681 ADCY9 0.974310442484441 0.025689507576649 4.99389097554321e-08 adenylate cyclase 9 FUNCTION: Adenylyl cyclase that catalyzes the formation of the signaling molecule cAMP in response to activation of G protein- coupled receptors (PubMed:9628827, PubMed:12972952, PubMed:15879435, PubMed:10987815). Contributes to signaling cascades activated by CRH (corticotropin-releasing factor), corticosteroids and beta-adrenergic receptors (PubMed:9628827). {ECO:0000269|PubMed:10987815, ECO:0000269|PubMed:12972952, ECO:0000269|PubMed:15879435, ECO:0000269|PubMed:9628827}.; . TISSUE SPECIFICITY: Detected in skeletal muscle, pancreas, lung, heart, kidney, liver, brain and placenta (PubMed:9628827, PubMed:10987815). Expressed in multiple cells of the lung, with expression highest in airway smooth muscle (PubMed:12972952). {ECO:0000269|PubMed:10987815, ECO:0000269|PubMed:12972952, ECO:0000269|PubMed:9628827}.; unclassifiable (Anatomical System);cartilage;ovary;heart;islets of Langerhans;colon;skin;skeletal muscle;retina;breast;uterus;pancreas;prostate;lung;endometrium;larynx;thyroid;hippocampus;liver;testis;head and neck;spleen;kidney;brain;mammary gland;stomach;peripheral nerve; superior cervical ganglion;thyroid;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16170 0.17928 -1.780505741 2.282377919 630.16158 5.05923 ADCY10 5.85120000034897e-26 0.0600953778661287 0.939904622133871 adenylate cyclase 10 (soluble) FUNCTION: Catalyzes the formation of the signaling molecule cAMP (PubMed:12609998, PubMed:15659711, PubMed:24616449, PubMed:25040695, PubMed:24567411). May function as sensor that mediates responses to changes in cellular bicarbonate and CO(2) levels (PubMed:15659711, PubMed:17591988). Has a critical role in mammalian spermatogenesis by producing the cAMP which regulates cAMP-responsive nuclear factors indispensable for sperm maturation in the epididymis. Induces capacitation, the maturational process that sperm undergo prior to fertilization (By similarity). Involved in ciliary beat regulation (PubMed:17591988). {ECO:0000250|UniProtKB:Q8C0T9, ECO:0000269|PubMed:15659711, ECO:0000269|PubMed:17591988, ECO:0000269|PubMed:24567411, ECO:0000269|PubMed:24616449, ECO:0000269|PubMed:25040695}.; DISEASE: Hypercalciuria absorptive 2 (HCA2) [MIM:143870]: A common type of hypercalciuria, a condition characterized by excessive urinary calcium excretion. Absorptive hypercalciuria is due to gastrointestinal hyperabsorption of calcium and is a frequent cause of calcium oxalate nephrolithiasis. {ECO:0000269|PubMed:11932268}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in airway epithelial cells and testis (at protein level) (PubMed:17591988). Weakly expressed in multiple tissues. Expressed in brain, heart, kidney, liver, lung, pancreas, peripheral blood leukocytes, placenta, skeletal muscle, stomach, thymus, airway epithelial cells, duodenum, jejunum and ileum. Very low level of expression in bone. {ECO:0000269|PubMed:11932268, ECO:0000269|PubMed:15659711, ECO:0000269|PubMed:17591988}.; unclassifiable (Anatomical System);lung;testis; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.25077 0.06261 0.639248104 83.78744987 738.8812 5.39507 ADCY10P1 . . . adenylate cyclase 10 (soluble) pseudogene 1 . . . . . . . . . . . ADCYAP1 0.133462668533983 0.780096959885555 0.0864403715804617 adenylate cyclase activating polypeptide 1 (pituitary) FUNCTION: Binding to its receptor activates G proteins and stimulates adenylate cyclase in pituitary cells. Promotes neuron projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway. {ECO:0000269|PubMed:11175907, ECO:0000269|PubMed:23800469}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;salivary gland;intestine;pharynx;colon;parathyroid;blood;skin;pancreas;lung;frontal lobe;cornea;placenta;visual apparatus;liver;testis;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.24697 0.31097 -0.185391282 39.67916962 938.17128 5.93746 ADCYAP1R1 0.00133478497077452 0.997041488624372 0.00162372640485392 ADCYAP receptor type I FUNCTION: This is a receptor for PACAP-27 and PACAP-38. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. May regulate the release of adrenocorticotropin, luteinizing hormone, growth hormone, prolactin, epinephrine, and catecholamine. May play a role in spermatogenesis and sperm motility. Causes smooth muscle relaxation and secretion in the gastrointestinal tract.; . TISSUE SPECIFICITY: Most abundant in the brain, low expression in the lung, liver, thymus, spleen, pancreas and placenta.; frontal lobe;brain; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.12974 0.11886 -0.159704656 41.90846898 72.59457 1.77715 ADD1 0.611299255784318 0.388685983735969 1.47604797128538e-05 adducin 1 FUNCTION: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin.; . TISSUE SPECIFICITY: Expressed in all tissues. Found in much higher levels in reticulocytes than the beta subunit.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;duodenum;amnion;hypopharynx;head and neck;kidney;stomach;thymus;cerebellum; amygdala;superior cervical ganglion;occipital lobe;prefrontal cortex;globus pallidus;pons;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.50688 0.39018 -0.929520514 9.683887709 5354.07898 15.11007 ADD2 0.999175206924775 0.000824792804299683 2.70924865899869e-10 adducin 2 FUNCTION: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to the erythrocyte membrane receptor SLC2A1/GLUT1 and may therefore provide a link between the spectrin cytoskeleton to the plasma membrane. Binds to calmodulin. Calmodulin binds preferentially to the beta subunit. {ECO:0000269|PubMed:18347014}.; . TISSUE SPECIFICITY: Expressed mainly in brain, spleen, kidney cortex and medulla, and heart. Also expressed in human umbilical vein endothelial cells, human vascular smooth muscle cells, kidney tubular cells and K-562 cell line. {ECO:0000269|PubMed:12951058}.; unclassifiable (Anatomical System);heart;ovary;parathyroid;fovea centralis;skin;retina;uterus;lung;frontal lobe;synovium;placenta;bone;macula lutea;visual apparatus;liver;testis;spleen;kidney;brain; whole brain;medulla oblongata;thalamus;superior cervical ganglion;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;bone marrow;subthalamic nucleus;fetal liver;fetal brain;prefrontal cortex;liver;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.60812 0.19286 -0.260839617 34.94928049 451.48224 4.41659 ADD3 0.952357436631549 0.0476423310787392 2.32289711505446e-07 adducin 3 FUNCTION: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin.; . TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed. {ECO:0000269|PubMed:8893809}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;urinary;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;larynx;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; amygdala;dorsal root ganglion;occipital lobe;superior cervical ganglion;thalamus;medulla oblongata;olfactory bulb;hypothalamus;spinal cord;caudate nucleus;atrioventricular node;pons;subthalamic nucleus;thyroid;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.71912 0.15282 0.156217551 64.82071243 379.3302 4.10682 ADD3-AS1 . . . ADD3 antisense RNA 1 . . . . . . . . . . . ADFN . . . albinism-deafness syndrome . . . . . . . . . . . ADGB . . . androglobin . . . . . 0.17444 . . . 3189.03112 10.75951 ADGRA1 . . . adhesion G protein-coupled receptor A1 FUNCTION: Orphan receptor.; . . . . 0.12174 . -0.135838822 43.77211607 . . ADGRA1-AS1 . . . adhesion G protein-coupled receptor A1 antisense RNA 1 . . . . . . . . . . . ADGRA2 . . . adhesion G protein-coupled receptor A2 FUNCTION: Endothelial receptor that acts as an essential regulator of CNS angiogenesis. Required for normal endothelial cell sprouting and migration in the forebrain and neural tube (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in endothelial cells (at protein level). Abundantly expressed in tumor vessels, heart, placenta, ovary, small intestine, and colon. {ECO:0000269|PubMed:15021905}.; . . 0.30986 0.12383 -0.143334748 42.35079028 . . ADGRA3 . . . adhesion G protein-coupled receptor A3 FUNCTION: Orphan receptor that may have a role in planar cell polarity pathway. {ECO:0000250|UniProtKB:S4X0Q8}.; . . . . 0.08248 0.11260 -0.073557068 47.80018872 . . ADGRB1 . . . adhesion G protein-coupled receptor B1 FUNCTION: Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Likely to be a potent inhibitor of angiogenesis in brain and may play a significant role as a mediator of the p53 signal in suppression of glioblastoma. May function in cell adhesion and signal transduction in the brain. {ECO:0000269|PubMed:11875720}.; . TISSUE SPECIFICITY: Specifically expressed in brain. Reduced or no expression is observed in some glioblastoma cell lines and cancer tissues. No expression in astrocytes. {ECO:0000269|PubMed:11875720, ECO:0000269|PubMed:12074842, ECO:0000269|PubMed:12507886}.; . . 0.12027 0.19590 . . . . ADGRB2 . . . adhesion G protein-coupled receptor B2 FUNCTION: Orphan receptor involved in cell adhesion and probably in cell-cell interactions. Activates NFAT signaling pathway probably via a G-protein dependent pathway (PubMed:20367554). Might be involved in angiogenesis inhibition (By similarity). {ECO:0000250|UniProtKB:Q8CGM1, ECO:0000269|PubMed:20367554}.; . TISSUE SPECIFICITY: Strongly expressed in brain. Also detected in heart, thymus, skeletal muscle, and different cell lines.; . . 0.46333 0.10587 -1.517642441 3.467799009 . . ADGRB3 . . . adhesion G protein-coupled receptor B3 FUNCTION: Receptor that plays a role in the regulation of synaptogenesis and dendritic spine formation at least partly via interaction with ELMO1 and RAC1 activity (By similarity). Promotes myoblast fusion through ELMO/DOCK1 (PubMed:24567399). {ECO:0000250|UniProtKB:O60242, ECO:0000269|PubMed:24567399}.; . TISSUE SPECIFICITY: Strongly expressed in brain. Also detected in heart. Reduced expression in some glioblastoma cell lines. {ECO:0000269|PubMed:9533023}.; . . 0.46112 . -1.74358502 2.394432649 . . ADGRD1 . . . adhesion G protein-coupled receptor D1 FUNCTION: Orphan receptor. Signals via G(s)-alpha family of G- proteins. {ECO:0000269|PubMed:22025619, ECO:0000269|PubMed:22575658}.; . . . . 0.08353 0.09976 -0.233339999 36.34111819 . . ADGRD2 . . . adhesion G protein-coupled receptor D2 FUNCTION: Orphan receptor.; . . . . 0.13777 0.08880 5.536372465 99.85255957 . . ADGRE1 . . . adhesion G protein-coupled receptor E1 FUNCTION: Orphan receptor involved in cell adhesion and probably in cell-cell interactions specifically involving cells of the immune system. May play a role in regulatory T-cells (Treg) development. {ECO:0000250|UniProtKB:Q61549}.; . TISSUE SPECIFICITY: Expression is restricted to eosinophils. {ECO:0000269|PubMed:17823986, ECO:0000269|PubMed:24530099}.; . . 0.06116 0.09044 2.743343517 98.96791696 . . ADGRE2 . . . adhesion G protein-coupled receptor E2 FUNCTION: Cell surface receptor that binds to the chondroitin sulfate moiety of glycosaminoglycan chains and promotes cell attachment. Promotes granulocyte chemotaxis, degranulation and adhesion. In macrophages, promotes the release of inflammatory cytokines, including IL8 and TNF. Signals probably through G- proteins. {ECO:0000269|PubMed:12829604, ECO:0000269|PubMed:17928360, ECO:0000269|PubMed:22310662, ECO:0000269|PubMed:22575658}.; . TISSUE SPECIFICITY: Expression is restricted to myeloid cells. Highest expression was found in peripheral blood leukocytes, followed by spleen and lymph nodes, with intermediate to low levels in thymus, bone marrow, fetal liver, placenta, and lung, and no expression in heart, brain, skeletal muscle, kidney, or pancreas. Expression is also detected in monocyte/macrophage and Jurkat cell lines but not in other cell lines tested. {ECO:0000269|PubMed:10903844, ECO:0000269|PubMed:11994511}.; . . 0.09608 . 2.36468479 98.44302902 . . ADGRE3 . . . adhesion G protein-coupled receptor E3 FUNCTION: Orphan receptor that may play a role myeloid-myeloid interactions during immune and inflammatory responses. A ligand for the soluble form of this receptor is present at the surface of momocytes-derived macrophages and activated neutrophils. {ECO:0000269|PubMed:11279179}.; . TISSUE SPECIFICITY: Displays a predominantly leukocyte-restricted expression, with highest levels in neutrophils, monocytes and macrophages. {ECO:0000269|PubMed:11279179}.; . . 0.07768 . 1.223576934 93.23543289 . . ADGRE4P . . . adhesion G protein-coupled receptor E4, pseudogene FUNCTION: Could mediated the cellular interaction between myeloid cells and B-cells. {ECO:0000250|UniProtKB:Q91ZE5}.; . . . . 0.04425 . . . . . ADGRE5 . . . adhesion G protein-coupled receptor E5 FUNCTION: Receptor potentially involved in both adhesion and signaling processes early after leukocyte activation. Plays an essential role in leukocyte migration (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Broadly expressed, found on most hematopoietic cells, including activated lymphocytes, monocytes, macrophages, dendritic cells, and granulocytes. Expressed also abundantly by smooth muscle cells. Expressed in thyroid, colorectal, gastric, esophageal and pancreatic carcinomas too. Expression are increased under inflammatory conditions in the CNS of multiple sclerosis and in synovial tissue of patients with rheumatoid arthritis. Increased expression of CD97 in the synovium is accompanied by detectable levels of soluble CD97 in the synovial fluid.; . . 0.13309 0.13687 -1.100469982 6.929700401 . . ADGRF1 . . . adhesion G protein-coupled receptor F1 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Mainly expressed in the kidney. Up-regulated in lung adenocarcinomas and prostate cancers. {ECO:0000269|PubMed:20149256}.; . . 0.06533 . 0.698081425 85.30313753 . . ADGRF2 . . . adhesion G protein-coupled receptor F2 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: High expression in kidney. Up-regulated in lung adenocarcinomas and prostate cancers. {ECO:0000269|PubMed:20149256}.; . . 0.12772 0.07636 . . . . ADGRF3 . . . adhesion G protein-coupled receptor F3 FUNCTION: Orphan receptor.; . . . . 0.06198 0.08587 3.570820201 99.51639538 . . ADGRF4 . . . adhesion G protein-coupled receptor F4 FUNCTION: Orphan receptor.; . . . . 0.05443 0.09240 1.872162724 97.2163246 . . ADGRF5 . . . adhesion G protein-coupled receptor F5 FUNCTION: Receptor that plays a critical role in lung surfactant homeostasis. May play a role in controlling adipocyte function. {ECO:0000250|UniProtKB:G5E8Q8}.; . . . . 0.02005 0.09657 -0.738630771 13.80042463 . . ADGRF5P1 . . . adhesion G protein-coupled receptor F5 pseudogene 1 . . . . . . . . . . . ADGRF5P2 . . . adhesion G protein-coupled receptor F5 pseudogene 2 . . . . . . . . . . . ADGRG1 . . . adhesion G protein-coupled receptor G1 FUNCTION: Involved in cell adhesion and probably in cell-cell interactions. Regulates the migration of neural precursor cells. Receptor for collagen III/COL3A1 in the developing brain and involved in regulation of cortical development, specifically in maintenance of the pial basemant membrane integrity and in cortical lamination. Binding to the COL3A1 ligand inhibits neuronal migration and activates the RhoA pathway by coupling to GNA13 and possibly GNA12. Isoforms show differences in receptor signaling, specifically in serum response element (SRE) transcriptional activation upon overexpression. Overexpression inhibits melanoma tumor growth and metastasis and, during melanoma progression, regulates VEGFA production and angiogenesis through PRKCA; unprocessed GPR56 is inhibiting and GPR56 NT is activating angiogenesis. Required for normal cortical development and regulation of neuroprogenitor cells proliferation. {ECO:0000269|PubMed:16757564, ECO:0000269|PubMed:19572147, ECO:0000269|PubMed:21708946, ECO:0000269|PubMed:21724588, ECO:0000269|PubMed:24531968}.; DISEASE: Polymicrogyria, bilateral frontoparietal (BFPP) [MIM:606854]: A malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination, most severe in the frontoparietal regions. BFPP clinical manifestations include developmental and psychomotor delay, cerebellar and pyramidal signs, truncal ataxia, seizures, hyperreflexia. Polymicrogyria is a heterogeneous disorder, considered to be the result of postmigratory abnormal cortical organization. {ECO:0000269|PubMed:15044805, ECO:0000269|PubMed:16240336, ECO:0000269|PubMed:21723461}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Polymicrogyria, bilateral perisylvian, autosomal recessive (BPPR) [MIM:615752]: A form of polymicrogyria, a malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. BPPR is characterized by strikingly restricted polymicrogyria limited to the cortex surrounding the Sylvian fissure. Affected individuals have intellectual and language difficulty and seizures, but no motor disability. Polymicrogyria is a heterogeneous disorder, considered to be the result of post-migratory abnormal cortical organization. {ECO:0000269|PubMed:24531968}. Note=The disease is caused by mutations affecting the gene represented in this entry. Homozygous deletion of 1 of 2 tandem 15-bp repeats located 144 bp upstream of the GPR56 non-coding exon 1m transcription start site, results in impaired perisylvian GPR56 expression and disruption of perisylvian gyri (PubMed:24531968). {ECO:0000269|PubMed:24531968}.; TISSUE SPECIFICITY: Widely distributed with highest levels found in thyroid gland, brain and heart. Expressed in a great number of tumor cells. Expression is down-regulated in different tumors from highly metastatic cells. {ECO:0000269|PubMed:16757564}.; . . 0.15476 0.14164 -0.506987379 21.76810569 . . ADGRG2 . . . adhesion G protein-coupled receptor G2 FUNCTION: Orphan receptor. Could be involved in a signal transduction pathway controlling epididymal function and male fertility. May regulate fluid exchange within epididymis. {ECO:0000250|UniProtKB:Q8CJ12}.; . TISSUE SPECIFICITY: Epididymis-specific expression (at protein level). Both subunits are associated with apical membranes of efferent ductule and proximal epididymal duct epithelia. Mainly expressed in the nonciliated principal cells of the proximal excurrent ducts. Specifically over-expressed in Ewing sarcomas but also up-regulated in a number of carcinomas derived from prostate, kidney or lung. {ECO:0000269|PubMed:12420295, ECO:0000269|PubMed:18469038, ECO:0000269|PubMed:23338946, ECO:0000269|PubMed:9150425}.; . . 0.53967 0.10442 0.510776592 80.23708422 . . ADGRG3 . . . adhesion G protein-coupled receptor G3 FUNCTION: Orphan receptor that regulates migration of lymphatic endothelial cells in vitro via the small GTPases RhoA and CDC42 (PubMed:24178298). Regulates B-cell development (By similarity). Seems to signal through G-alpha(q)-proteins (PubMed:22575658). {ECO:0000250|UniProtKB:Q8R0T6, ECO:0000269|PubMed:22575658, ECO:0000269|PubMed:24178298}.; . TISSUE SPECIFICITY: Expressed in cultured primary dermal lymphatic endothelial cells. {ECO:0000269|PubMed:24178298}.; . . 0.07054 0.09411 -0.108334733 45.57088936 . . ADGRG4 . . . adhesion G protein-coupled receptor G4 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Detected in fetal retina. Highly expressed in normal enterochromaffin cells and in neuroendocrine carcinoma. Detected in normal liver; highly expressed in primary liver carcinoma. {ECO:0000269|PubMed:18953328}.; . . 0.10204 . 0.078757228 59.2061807 . . ADGRG5 . . . adhesion G protein-coupled receptor G5 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Expressed in immune cells. Primarily found in granulocytes. Found in eosinophils. {ECO:0000269|PubMed:21724806}.; . . 0.06892 . 0.181903047 66.2361406 . . ADGRG6 . . . adhesion G protein-coupled receptor G6 FUNCTION: Orphan receptor. May be required for normal differentiation of promyelinating Schwann cells and for normal myelination of axons. Signals probably through G-proteins to transiently elevate cAMP levels (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in placenta and to a lower extent in pancreas and liver. Detected in aortic endothelial cells but not in skin microvascular endothelial cells. {ECO:0000269|PubMed:15225624}.; . . 0.08820 . -0.169017544 40.67586695 . . ADGRG7 . . . adhesion G protein-coupled receptor G7 FUNCTION: Orphan receptor.; . . . . 0.04884 0.06553 0.806491657 87.72705827 . . ADGRL1 . . . adhesion G protein-coupled receptor L1 FUNCTION: Calcium-independent receptor of high affinity for alpha- latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization. Receptor propably implicated in the regulation of exocytosis (By similarity). {ECO:0000250}.; . . . . 0.25579 0.23096 -2.625946333 0.796178344 . . ADGRL2 . . . adhesion G protein-coupled receptor L2 FUNCTION: Calcium-independent receptor of low affinity for alpha- latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor propably implicated in the regulation of exocytosis. {ECO:0000250|UniProtKB:O88923}.; . TISSUE SPECIFICITY: Expressed very widely in all normal tissues tested. Expression is variable in tumor cell lines, apparently elevated in some lines and absent or markedly reduced in others. {ECO:0000269|PubMed:10030676}.; . . 0.90590 0.26245 -0.189246284 39.30761972 . . ADGRL3 . . . adhesion G protein-coupled receptor L3 FUNCTION: Plays a role in cell-cell adhesion and neuron guidance via its interactions with FLRT2 and FLRT3 that are expressed at the surface of adjacent cells (PubMed:26235030). Plays a role in the development of glutamatergic synapses in the cortex. Important in determining the connectivity rates between the principal neurons in the cortex. {ECO:0000250|UniProtKB:Q80TS3, ECO:0000305|PubMed:26235030}.; . . . . 0.16776 0.14106 -0.369255208 28.25548478 . . ADGRL3-AS1 . . . adhesion G protein-coupled receptor L3 antisense RNA 1 . . . . . . . . . . . ADGRL4 . . . adhesion G protein-coupled receptor L4 FUNCTION: Endothelial orphan receptor that acts as a key regulator of angiogenesis. {ECO:0000269|PubMed:23871637}.; . TISSUE SPECIFICITY: Detected in the majority of epithelial cells in tumor and normal tissues. Expressed also in human umbilical vein endothelial cells. {ECO:0000269|PubMed:23871637}.; . . 0.28225 0.23716 0.99945266 90.6935598 . . ADGRV1 . . . adhesion G protein-coupled receptor V1 FUNCTION: Receptor that may have an important role in the development of the central nervous system.; DISEASE: Usher syndrome 2C (USH2C) [MIM:605472]: USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa with sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). USH2 is characterized by congenital mild hearing impairment with normal vestibular responses. {ECO:0000269|PubMed:14740321, ECO:0000269|PubMed:22147658}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Febrile seizures, familial, 4 (FEB4) [MIM:604352]: Seizures associated with febrile episodes in childhood without any evidence of intracranial infection or defined pathologic or traumatic cause. It is a common condition, affecting 2-5% of children aged 3 months to 5 years. The majority are simple febrile seizures (generally defined as generalized onset, single seizures with a duration of less than 30 minutes). Complex febrile seizures are characterized by focal onset, duration greater than 30 minutes, and/or more than one seizure in a 24 hour period. The likelihood of developing epilepsy following simple febrile seizures is low. Complex febrile seizures are associated with a moderately increased incidence of epilepsy. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at low levels in adult tissues. {ECO:0000269|PubMed:10976914}.; . . 0.07741 0.17025 8.124040712 99.95281906 . . ADH1A 6.68921783131982e-08 0.141801803293592 0.85819812981423 alcohol dehydrogenase 1A (class I), alpha polypeptide . . . unclassifiable (Anatomical System);uterus;lung;nasopharynx;visual apparatus;liver;colon;spleen;germinal center;spinal ganglion;stomach; superior cervical ganglion;fetal liver;liver;pons;trigeminal ganglion;skeletal muscle; . . -0.449946534 24.00330267 21.95267 0.73867 ADH1B 0.193827609463651 0.795439250837574 0.0107331396987754 alcohol dehydrogenase 1B (class I), beta polypeptide . . . unclassifiable (Anatomical System);islets of Langerhans;sympathetic chain;colon;skeletal muscle;pancreas;lung;cerebral cortex;adrenal gland;nasopharynx;liver;testis;spleen;kidney;spinal ganglion;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;adipose tissue;atrioventricular node;skeletal muscle;skin;uterus;adrenal gland;liver;appendix;fetal lung;ciliary ganglion;trigeminal ganglion; 0.10541 0.43559 0.553050905 81.54635527 622.62467 5.03298 ADH1C . . . alcohol dehydrogenase 1C (class I), gamma polypeptide . . . . . . . . . . . ADH4 7.01336073217093e-06 0.481923936222609 0.518069050416659 alcohol dehydrogenase 4 (class II), pi polypeptide . . . unclassifiable (Anatomical System);whole body;small intestine;liver;spleen; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.17370 0.18361 0.174625237 65.9648502 212.21443 3.14150 ADH5 9.11477880080588e-07 0.313157521484844 0.686841567037276 alcohol dehydrogenase 5 (class III), chi polypeptide FUNCTION: Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione.; . . smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;brain;bladder;tonsil;amygdala;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;amnion;head and neck;kidney;stomach;aorta; dorsal root ganglion;amygdala;fetal liver;superior cervical ganglion;adipose tissue;testis;ciliary ganglion;kidney;trigeminal ganglion; 0.26363 0.34407 0.193034296 66.82000472 62.29801 1.61087 ADH5P2 . . . alcohol dehydrogenase 5 (class III), chi polypeptide, pseudogene 2 . . . . . . . . . . . ADH5P3 . . . alcohol dehydrogenase 5 (class III), chi polypeptide, pseudogene 3 . . . . . . . . . . . ADH5P4 . . . alcohol dehydrogenase 5 (class III), chi polypeptide, pseudogene 4 . . . . . . . . . . . ADH6 0.00201652366064819 0.910993316085716 0.0869901602536363 alcohol dehydrogenase 6 (class V) . . TISSUE SPECIFICITY: Stomach and liver.; liver;colon;spleen;kidney;stomach; superior cervical ganglion;fetal liver;liver;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07506 0.09112 -0.315847836 31.68789809 68.95112 1.72069 ADH7 7.33278354117419e-09 0.0765042699227542 0.923495722744462 alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide FUNCTION: Could function in retinol oxidation for the synthesis of retinoic acid, a hormone important for cellular differentiation. Medium-chain (octanol) and aromatic (m-nitrobenzaldehyde) compounds are the best substrates. Ethanol is not a good substrate but at the high ethanol concentrations reached in the digestive tract, it plays a role in the ethanol oxidation and contributes to the first pass ethanol metabolism.; . TISSUE SPECIFICITY: Preferentially expressed in stomach.; lung;oesophagus;larynx;nasopharynx;head and neck;skeletal muscle; superior cervical ganglion;tongue; 0.13439 0.26662 0.220536484 68.38287332 320.99818 3.80593 ADHFE1 3.87814550307822e-05 0.952647751859024 0.047313466685945 alcohol dehydrogenase, iron containing 1 FUNCTION: Catalyzes the cofactor-independent reversible oxidation of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA) coupled to reduction of 2-ketoglutarate (2-KG) to D-2- hydroxyglutarate (D-2-HG). D,L-3-hydroxyisobutyrate and L-3- hydroxybutyrate (L-3-OHB) are also substrates for HOT with 10-fold lower activities. {ECO:0000269|PubMed:16435184}.; . TISSUE SPECIFICITY: Only expressed in adult liver. {ECO:0000269|PubMed:12592711}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;testis;brain;unclassifiable (Anatomical System);heart;cartilage;cerebellum cortex;lacrimal gland;adrenal cortex;lens;skeletal muscle;lung;placenta;macula lutea;hippocampus;liver;spleen;kidney;mammary gland;stomach; . 0.24334 0.59422 -0.446304853 24.33356924 81.68798 1.91506 ADI1 0.00602945066661725 0.733727134737034 0.260243414596349 acireductone dioxygenase 1 FUNCTION: Catalyzes the formation of formate and 2-keto-4- methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5- methylthiopentene (DHK-MTPene). Also down-regulates cell migration mediated by MMP14. Necessary for hepatitis C virus replication in an otherwise non-permissive cell line. {ECO:0000255|HAMAP- Rule:MF_03154, ECO:0000269|PubMed:11602742, ECO:0000269|PubMed:15938715}.; . TISSUE SPECIFICITY: Detected in heart, colon, lung, stomach, brain, spleen, liver, skeletal muscle and kidney. {ECO:0000269|PubMed:11602742, ECO:0000269|PubMed:14718544}.; myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;bladder;brain;cartilage;pharynx;blood;lens;skeletal muscle;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; superior cervical ganglion;prostate;adrenal gland;liver;kidney; 0.22797 0.24818 -0.205617011 38.57631517 130.78073 2.49064 ADIG . . . adipogenin FUNCTION: Plays a role in stimulating adipocyte differentiation and development. {ECO:0000250|UniProtKB:Q8R400}.; . . . . 0.22628 . 0.080983847 59.76055674 11.12436 0.40271 ADIPOQ 5.61889056767483e-07 0.0717576328925993 0.928241805218344 adiponectin, C1Q and collagen domain containing FUNCTION: Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW. {ECO:0000269|PubMed:11479627}.; DISEASE: Adiponectin deficiency (ADPND) [MIM:612556]: A condition that results in very low concentrations of plasma adiponectin. {ECO:0000269|PubMed:10918532}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Synthesized exclusively by adipocytes and secreted into plasma.; unclassifiable (Anatomical System);meninges;pia mater;cerebral cortex;colon;dura mater;spinal ganglion;mammary gland;skin; superior cervical ganglion;adipose tissue;ciliary ganglion;atrioventricular node; 0.16266 0.83603 0.128714042 63.19886766 158.55583 2.75085 ADIPOQ-AS1 . . . ADIPOQ antisense RNA 1 . . . . . . . . . . . ADIPOR1 0.592753905673148 0.405185389608553 0.00206070471829883 adiponectin receptor 1 FUNCTION: Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:25855295, PubMed:12802337). Required for normal glucose and fat homeostasis and for maintaining a normal body weight. ADIPOQ-binding activates a signaling cascade that leads to increased AMPK activity, and ultimately to increased fatty acid oxidation, increased glucose uptake and decreased gluconeogenesis. Has high affinity for globular adiponectin and low affinity for full-length adiponectin (By similarity). {ECO:0000250|UniProtKB:Q91VH1, ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:25855295}.; . TISSUE SPECIFICITY: Widely expressed (PubMed:16044242). Highly expressed in heart and skeletal muscle (PubMed:12802337). Expressed at intermediate level in brain, spleen, kidney, liver, placenta, lung and peripheral blood leukocytes (PubMed:12802337). Weakly expressed in colon, thymus and small intestine (PubMed:12802337). {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:16044242}.; lymphoreticular;ovary;skin;bone marrow;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; superior cervical ganglion;placenta;skeletal muscle;bone marrow; 0.32939 0.26487 -0.295622497 32.61972163 4.82569 0.17698 ADIPOR1P1 . . . adiponectin receptor 1 pseudogene 1 . . . . . . . . . . . ADIPOR1P2 . . . adiponectin receptor 1 pseudogene 2 . . . . . . . . . . . ADIPOR2 0.810597984007902 0.189196325932477 0.000205690059620623 adiponectin receptor 2 FUNCTION: Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:12802337, PubMed:25855295). Required for normal body fat and glucose homeostasis. ADIPOQ-binding activates a signaling cascade that leads to increased PPARA activity, and ultimately to increased fatty acid oxidation and glucose uptake. Has intermediate affinity for globular and full-length adiponectin. Required for normal revascularization after chronic ischemia caused by severing of blood vessels (By similarity). {ECO:0000250|UniProtKB:Q8BQS5, ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:25855295}.; . TISSUE SPECIFICITY: Ubiquitous (PubMed:16044242). Highly expressed in skeletal muscle, liver and placenta (PubMed:12802337). Weakly expressed in brain, heart, colon, spleen, kidney, thymus, small intestine, peripheral blood leukocytes and lung (PubMed:12802337). {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:16044242}.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;head and neck;kidney;stomach;aorta;cerebellum; medulla oblongata;occipital lobe;thalamus;superior cervical ganglion;hypothalamus;spinal cord;caudate nucleus;atrioventricular node;skeletal muscle;adrenal gland;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.23239 0.26635 0.281220278 71.07808445 89.13071 2.02799 ADIRF 0.033386817321431 0.613932293366149 0.352680889312419 adipogenesis regulatory factor FUNCTION: Plays a role in fat cell development; promotes adipogenic differentiation and stimulates transcription initiation of master adipogenesis factors like PPARG and CEBPA at early stages of preadipocyte differentiation. Its overexpression confers resistance to the anticancer chemotherapeutic drug cisplatin. {ECO:0000269|PubMed:19444912, ECO:0000269|PubMed:23239344}.; . TISSUE SPECIFICITY: Expressed in adipose tissue (at protein level). Highly expressed in omental and subcutaneous adipose tissues. Expressed in heart, cornea, liver, kidney and spleen. {ECO:0000269|PubMed:23239344, ECO:0000269|Ref.4}.; . . 0.14816 0.12307 -0.053113545 49.38664779 4.92553 0.18254 ADIRF-AS1 . . . ADIRF antisense RNA 1 . . . . . . . . . . . ADK 0.322841314242593 0.673716069681989 0.00344261607541734 adenosine kinase FUNCTION: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides.; . TISSUE SPECIFICITY: Widely expressed. Highest level in placenta, liver, muscle and kidney.; colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;gum;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;breast;lung;nasopharynx;placenta;macula lutea;liver;spleen;cervix;kidney;stomach; superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.22255 0.68620 -0.339715008 30.06605331 11.08904 0.40149 ADM 0.576630085865165 0.412314558941091 0.0110553551937437 adrenomedullin FUNCTION: AM and PAMP are potent hypotensive and vasodilatator agents. Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis. In the kidney, am is diuretic and natriuretic, and both am and pamp inhibit aldosterone secretion by direct adrenal actions. In pituitary gland, both peptides at physiologically relevant doses inhibit basal ACTH secretion. Both peptides appear to act in brain and pituitary gland to facilitate the loss of plasma volume, actions which complement their hypotensive effects in blood vessels.; . TISSUE SPECIFICITY: Highest levels found in pheochromocytoma and adrenal medulla. Also found in lung, ventricle and kidney tissues.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; superior cervical ganglion;adipose tissue;placenta;ciliary ganglion;trigeminal ganglion;skin; 0.61396 0.43834 0.237127192 68.98443029 244.93594 3.37565 ADM2 0.0153000381093707 0.691915039506612 0.292784922384017 adrenomedullin 2 FUNCTION: IMDL and IMDS may play a role as physiological regulators of gastrointestinal, cardiovascular bioactivities mediated by the CALCRL/RAMPs receptor complexes. Activates the cAMP-dependent pathway. {ECO:0000269|PubMed:14615490}.; . TISSUE SPECIFICITY: Expressed in the esophagus, stomach, jejunum, ileum, ileocecum, ascending colon, transverse colon, descending colon and rectum. Expressed in myocardial cells of the heart, renal tubular cells, hypothalamus, and pituitary. {ECO:0000269|PubMed:14615490, ECO:0000269|PubMed:16359754}.; unclassifiable (Anatomical System);lung;bone;visual apparatus;colon;kidney;gall bladder; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.09264 . . . 1344.67383 6.88613 ADM5 0.0362143986281022 0.629815191343944 0.333970410027954 adrenomedullin 5 (putative) FUNCTION: Probable non-functional remnant of adrenomedullin-5. {ECO:0000269|PubMed:18434369}.; . . . . . . 0.301449681 71.80938901 47.49501 1.33807 ADNP 0.9989040999292 0.00109589739428926 2.67651096393963e-09 activity-dependent neuroprotector homeobox FUNCTION: Potential transcription factor. May mediate some of the neuroprotective peptide VIP-associated effects involving normal growth and cancer proliferation.; . TISSUE SPECIFICITY: Widely expressed. Strong expression in heart, skeletal muscle, kidney and placenta. In brain, expression is stronger in the cerebellum and cortex regions. No expression detected in the colon. Strong increase of expression in colon and breast cancer tissues.; smooth muscle;ovary;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;tongue;urinary;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;uterus;whole body;larynx;bone;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;testis - interstitial;fetal brain;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.90423 0.13270 -1.414605945 4.134229771 99.59449 2.16070 ADNP-AS1 . . . ADNP antisense RNA 1 . . . . . . . . . . . ADNP2 0.346937920967371 0.652481030934223 0.000581048098406264 ADNP homeobox 2 FUNCTION: May be involved in transcriptional regulation.; . . umbilical cord;ovary;salivary gland;sympathetic chain;intestine;colon;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;oesophagus;larynx;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;cervix;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;testis - interstitial;globus pallidus;testis;pons;atrioventricular node;trigeminal ganglion;parietal lobe; 0.17091 0.10580 -1.497391194 3.603444209 154.16578 2.71378 ADO 0.745072785344825 0.244353519895174 0.0105736947600015 2-aminoethanethiol (cysteamine) dioxygenase . . . . . 0.24296 . 0.080983847 59.76055674 3718.35958 11.90954 ADORA1 0.0212580375414267 0.753794339899026 0.224947622559547 adenosine A1 receptor FUNCTION: Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase.; . . unclassifiable (Anatomical System);medulla oblongata;ovary;islets of Langerhans;hypothalamus;muscle;fovea centralis;choroid;lens;retina;optic nerve;lung;placenta;thyroid;visual apparatus;macula lutea;hippocampus;iris;liver;testis;kidney;mammary gland;brain; whole brain;medulla oblongata;superior cervical ganglion;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex;parietal lobe; 0.13638 0.23872 -0.203796826 38.81811748 30.51321 0.97171 ADORA2A 0.331624356227667 0.653193474007538 0.0151821697647949 adenosine A2a receptor FUNCTION: Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.; . . unclassifiable (Anatomical System);lymph node;ovary;heart;islets of Langerhans;colon;blood;lens;skin;skeletal muscle;uterus;optic nerve;whole body;lung;duodenum;liver;testis;spleen;kidney;germinal center;brain;tonsil;stomach; . 0.16812 0.41929 -0.113792788 45.25831564 148.88112 2.66101 ADORA2A-AS1 . . . ADORA2A antisense RNA 1 . . . . . . . . . . . ADORA2B 2.00749888633959e-05 0.276665265825261 0.723314659185875 adenosine A2b receptor FUNCTION: Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.; . . unclassifiable (Anatomical System);lymph node;heart;tongue;colon;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;larynx;placenta;macula lutea;liver;head and neck;spleen;brain;stomach; superior cervical ganglion;atrioventricular node; 0.08265 0.18465 0.639420866 83.8995046 449.84282 4.40801 ADORA2BP1 . . . adenosine A2b receptor pseudogene 1 . . . . . . . . . . . ADORA3 0.00605730645545196 0.906408120183879 0.0875345733606687 adenosine A3 receptor FUNCTION: Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. Possible role in reproduction.; . . unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;hypothalamus;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;lung;adrenal gland;bone;placenta;macula lutea;testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;appendix;atrioventricular node;trigeminal ganglion; 0.10089 0.16754 -0.086288664 47.11606511 28.68541 0.91844 ADPGK 0.0221562951088713 0.962118540872852 0.0157251640182771 ADP-dependent glucokinase FUNCTION: Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor. GDP and CDP can replace ADP, but with reduced efficiency (By similarity). {ECO:0000250}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;gum;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;hypothalamus;pancreas;lung;cornea;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;bone marrow; 0.35271 0.14691 0.128714042 63.19886766 2427.18192 9.14930 ADPGK-AS1 . . . ADPGK antisense RNA 1 . . . . . . . . . . . ADPRH 8.59498396157278e-06 0.316007946275015 0.683983458741024 ADP-ribosylarginine hydrolase FUNCTION: Catalyzes the reverse reaction of mono-ADP-ribosylation.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;peripheral nerve;cerebellum; superior cervical ganglion;cerebellum peduncles;placenta;appendix;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.12470 0.10331 -0.448125345 24.19202642 47.54224 1.33868 ADPRHL1 2.87960164870856e-07 0.307069849870643 0.692929862169192 ADP-ribosylhydrolase like 1 . . . unclassifiable (Anatomical System);prostate;lung;liver;skeletal muscle; subthalamic nucleus; 0.14867 . 0.266447942 70.5826846 404.59018 4.21799 ADPRHL2 6.50306503732575e-05 0.482206183451055 0.517728785898572 ADP-ribosylhydrolase like 2 FUNCTION: Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. Poly(ADP-ribose) metabolism may be required for maintenance of the normal function of neuronal cells. Generates ADP-ribose from poly-(ADP-ribose), but does not hydrolyze ADP- ribose-arginine, -cysteine, -diphthamide, or -asparagine bonds. Due to catalytic inactivity of PARG mitochondrial isoforms, ARH3 is the only PAR hydrolyzing enzyme in mitochondria. {ECO:0000269|PubMed:16278211}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16278211}.; . . 0.25164 0.11284 -0.580403979 18.58928993 1037.65244 6.18673 ADPRM 0.0655967752653321 0.870972800345595 0.063430424389073 ADP-ribose/CDP-alcohol diphosphatase, manganese-dependent FUNCTION: Hydrolyzes ADP-ribose, IDP-ribose, CDP-glycerol, CDP- choline and CDP-ethanolamine, but not other non-reducing ADP- sugars or CDP-glucose. May be involved in immune cell signaling as suggested by the second-messenger role of ADP-ribose, which activates TRPM2 as a mediator of oxidative/nitrosative stress (By similarity). {ECO:0000250}.; . . . . 0.05514 0.09317 0.084621747 60.31493277 2574.24001 9.48902 ADRA1A 4.17186626185209e-07 0.113826965819817 0.886172616993557 adrenoceptor alpha 1A FUNCTION: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine(PE)-stimulated ERK signaling in cardiac myocytes. {ECO:0000269|PubMed:18802028, ECO:0000269|PubMed:22120526}.; . TISSUE SPECIFICITY: Expressed in heart, brain, liver and prostate, but not in kidney, lung, adrenal, aorta and pituitary. Within the prostate, expressed in the apex, base, periurethral and lateral lobe. Isoform 4 is the most abundant isoform expressed in the prostate with high levels also detected in liver and heart. {ECO:0000269|PubMed:7737411, ECO:0000269|PubMed:8196478, ECO:0000269|PubMed:9490024}.; unclassifiable (Anatomical System); subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.04348 0.11771 0.156217551 64.82071243 652.0538 5.12161 ADRA1B 0.182479134837027 0.76493269536748 0.0525881697954929 adrenoceptor alpha 1B FUNCTION: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes. {ECO:0000269|PubMed:18802028, ECO:0000269|PubMed:22120526}.; . . unclassifiable (Anatomical System);lung;bone;colon;kidney; superior cervical ganglion;atrioventricular node; 0.72420 0.24587 -0.60427181 17.74593064 27.75985 0.89163 ADRA1D . . . adrenoceptor alpha 1D FUNCTION: This alpha-adrenergic receptor mediates its effect through the influx of extracellular calcium.; . . . . 0.14449 0.11771 0.156217551 64.82071243 229.7736 3.27584 ADRA2A . . . adrenoceptor alpha 2A FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine- induced inhibition of adenylate cyclase through the action of G proteins. The rank order of potency for agonists of this receptor is oxymetazoline > clonidine > epinephrine > norepinephrine > phenylephrine > dopamine > p-synephrine > p-tyramine > serotonin = p-octopamine. For antagonists, the rank order is yohimbine > phentolamine = mianserine > chlorpromazine = spiperone = prazosin > propanolol > alprenolol = pindolol. {ECO:0000269|PubMed:23105096}.; . . ovary;colon;choroid;fovea centralis;retina;uterus;prostate;optic nerve;whole body;cochlea;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;spleen;cervix;kidney;stomach; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.18963 0.11371 . . 204.06999 3.08511 ADRA2B 0.000244368543397983 0.526369150611134 0.473386480845468 adrenoceptor alpha 2B FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine- induced inhibition of adenylate cyclase through the action of G proteins. The rank order of potency for agonists of this receptor is clonidine > norepinephrine > epinephrine = oxymetazoline > dopamine > p-tyramine = phenylephrine > serotonin > p-synephrine / p-octopamine. For antagonists, the rank order is yohimbine > chlorpromazine > phentolamine > mianserine > spiperone > prazosin > alprenolol > propanolol > pindolol. {ECO:0000269|PubMed:23105096}.; DISEASE: Epilepsy, familial adult myoclonic, 2 (FAME2) [MIM:607876]: A form of cortical myoclonic tremor with epilepsy, a syndrome characterized by cortical myoclonus and variable occurrence of epileptic seizures. Usually, myoclonic tremor is the presenting symptom, characterized by tremulous finger movements and myoclonic jerks of the limbs increased by action and posture. In a minority of patients, seizures are the presenting symptom; both complex partial as well as generalized tonic clonic seizures are described. Some patients exhibit mild cognitive impairment. {ECO:0000269|PubMed:24114805}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . 0.11107 -0.247889024 35.98726115 62.69652 1.61925 ADRA2C 0.645951820563209 0.347840902336794 0.00620727709999678 adrenoceptor alpha 2C FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine- induced inhibition of adenylate cyclase through the action of G proteins.; . . . . 0.03325 0.09956 . . 2173.15437 8.58195 ADRB1 . . . adrenoceptor beta 1 FUNCTION: Beta-adrenergic receptors mediate the catecholamine- induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling. {ECO:0000269|PubMed:12391161}.; . . . . 0.57886 . . . 95.03749 2.10229 ADRB2 0.476493104047244 0.500227172057908 0.023279723894848 adrenoceptor beta 2 FUNCTION: Beta-adrenergic receptors mediate the catecholamine- induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine. {ECO:0000269|PubMed:2831218, ECO:0000269|PubMed:7915137}.; . . unclassifiable (Anatomical System);medulla oblongata;lymph node;cartilage;ovary;parathyroid;fovea centralis;uterus;prostate;lung;thyroid;placenta;macula lutea;hippocampus;alveolus;liver;testis;head and neck;spleen;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.16974 0.80184 0.418953042 77.06416608 2513.68991 9.34152 ADRB3 0.323569934345889 0.610501854306402 0.0659282113477086 adrenoceptor beta 3 FUNCTION: Beta-adrenergic receptors mediate the catecholamine- induced activation of adenylate cyclase through the action of G proteins. Beta-3 is involved in the regulation of lipolysis and thermogenesis.; . TISSUE SPECIFICITY: Expressed mainly in adipose tissues.; unclassifiable (Anatomical System);uterus;optic nerve;ovary;heart;placenta;macula lutea;fovea centralis;choroid;lens;skin;retina; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;temporal lobe;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.30367 0.41964 0.082802743 60.09082331 894.55022 5.82989 ADRBK1 0.998627979474698 0.00137202033578973 1.89512638608988e-10 adrenergic, beta, receptor kinase 1 FUNCTION: Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them. Key regulator of LPAR1 signaling. Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor. Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner. {ECO:0000269|PubMed:19306925}.; . TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes. {ECO:0000269|PubMed:10085131}.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;tonsil;amygdala;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;cornea;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;amygdala;superior cervical ganglion;prefrontal cortex;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle;skin;bone marrow;cerebellum; 0.65543 0.45217 -1.155457828 6.168907761 34.82644 1.06066 ADRBK2 0.793703982799154 0.206295578423999 4.38776846366768e-07 adrenergic, beta, receptor kinase 2 FUNCTION: Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors.; . . unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;colon;parathyroid;blood;skin;skeletal muscle;retina;breast;prostate;pancreas;lung;nasopharynx;placenta;alveolus;liver;testis;spleen;kidney;germinal center;brain;aorta;stomach;cerebellum; superior cervical ganglion;testis - interstitial;testis; 0.16613 0.24974 -0.734731259 14.01863647 36.58495 1.09767 ADRM1 0.981917517015876 0.0180699794149107 1.25035692129799e-05 adhesion regulating molecule 1 FUNCTION: Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity. {ECO:0000269|PubMed:16815440, ECO:0000269|PubMed:16906146, ECO:0000269|PubMed:16990800, ECO:0000269|PubMed:17139257, ECO:0000269|PubMed:18497817}.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;iris;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;cartilage;hypothalamus;muscle;adrenal cortex;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;liver;testis;skeletal muscle; 0.39448 0.11747 0.064394823 58.84642604 219.24477 3.20234 ADSL 0.000212575309664513 0.995213296293996 0.00457412839633915 adenylosuccinate lyase FUNCTION: Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate. {ECO:0000269|PubMed:10888601}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Both isoforms are produced by all tissues. Isoform 2 is 10-fold less abundant than isoform 1.; lymphoreticular;myocardium;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;pituitary gland;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;tongue;hypothalamus;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis;tumor;trigeminal ganglion;skeletal muscle; 0.77056 0.31214 -0.600630256 18.06440198 198.40828 3.04374 ADSS 0.822870227739542 0.177095097669272 3.46745911860389e-05 adenylosuccinate synthase FUNCTION: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.; . . . . 0.71511 0.34803 0.014844891 54.94810097 99.3475 2.15777 ADSSL1 0.000383323420631864 0.990043418976942 0.00957325760242575 adenylosuccinate synthase like 1 FUNCTION: Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and heart, as well as in several hematopoietic cell lines and solid tumors. {ECO:0000269|PubMed:15786719}.; myocardium;parathyroid;skin;retina;uterus;prostate;whole body;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;skeletal muscle;pancreas;lung;placenta;hippocampus;visual apparatus;liver;spleen;cervix;kidney;stomach; liver;testis;kidney;skeletal muscle; 0.25728 0.15503 -0.020150552 52.25288983 212.40167 3.14470 ADTRP 0.000702618266442128 0.751748460956727 0.247548920776831 androgen dependent TFPI regulating protein FUNCTION: Regulates the expression and the cell-associated anticoagulant activity of the inhibitor TFPI in endothelial cells (in vitro). {ECO:0000269|PubMed:21868574}.; . TISSUE SPECIFICITY: Expressed in cultured endothelial cells and in placenta. {ECO:0000269|PubMed:21868574}.; . . 0.03391 0.09745 0.439181676 77.69521113 1559.12031 7.31298 AEBP1 0.000218798556316862 0.999773762404969 7.4390387143512e-06 AE binding protein 1 FUNCTION: May positively regulate MAP-kinase activity in adipocytes, leading to enhanced adipocyte proliferation and reduced adipocyte differentiation. May also positively regulate NF-kappa-B activity in macrophages by promoting the phosphorylation and subsequent degradation of I-kappa-B-alpha (NFKBIA), leading to enhanced macrophage inflammatory responsiveness. Can act as a transcriptional repressor. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in osteoblast and visceral fat. {ECO:0000269|PubMed:8920928}.; myocardium;smooth muscle;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; uterus;uterus corpus;adipose tissue;ciliary ganglion;trigeminal ganglion; 0.88812 0.14965 0.119404819 62.20806794 3547.82162 11.49561 AEBP2 0.950982695744305 0.048987236166086 3.0068089609002e-05 AE binding protein 2 FUNCTION: DNA-binding transcriptional repressor. May interact with and stimulate the activity of the PRC2 complex, which methylates 'Lys-9' and 'Lys-27' residues of histone H3. {ECO:0000269|PubMed:15225548}.; . . developmental;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;oesophagus;endometrium;larynx;thyroid;testis;dura mater;germinal center;brain;pineal gland;artery;unclassifiable (Anatomical System);meninges;cartilage;heart;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;pia mater;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;aorta;stomach;peripheral nerve;thymus; subthalamic nucleus;superior cervical ganglion;globus pallidus;atrioventricular node;kidney;trigeminal ganglion;cerebellum; 0.83172 0.11262 -0.009020804 52.8544468 13.00958 0.47369 AEN 6.06475830868436e-08 0.0717316689761967 0.92826827037622 apoptosis enhancing nuclease FUNCTION: Exonuclease with activity against single- and double- stranded DNA and RNA. Mediates p53-induced apoptosis. When induced by p53 following DNA damage, digests double-stranded DNA to form single-stranded DNA and amplifies DNA damage signals, leading to enhancement of apoptosis. {ECO:0000269|PubMed:16171785, ECO:0000269|PubMed:18264133}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;mammary gland;stomach; superior cervical ganglion;pons; 0.20632 . 0.777157784 87.17857985 1416.11577 7.03389 AES 0.650716677191199 0.343333282686082 0.00595004012271914 amino-terminal enhancer of split FUNCTION: Transcriptional corepressor. Acts as dominant repressor towards other family members. Inhibits NF-kappa-B-regulated gene expression. May be required for the initiation and maintenance of the differentiated state. Essential for the transcriptional repressor activity of SIX3 during retina and lens development. {ECO:0000269|PubMed:10660609, ECO:0000269|PubMed:10748198}.; . TISSUE SPECIFICITY: Found predominantly in muscle, heart and Placenta. In fetal tissues, abundantly expressed in the heart, lung, kidney, brain and liver.; myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;tongue;adrenal cortex;pharynx;lens;skeletal muscle;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus;cerebellum; whole brain;subthalamic nucleus;cerebellum peduncles;thyroid;temporal lobe;prefrontal cortex;globus pallidus;pons; 0.28878 0.16765 -0.273576253 33.97027601 4.73265 0.17236 AF8T . . . AF8 temperature sensitivity complementing . . . . . . . . . . . AFA . . . ankyloblepharon filiforme adnatum . . . . . . . . . . . AFAP1 0.376071779661091 0.623909220708965 1.89996299440042e-05 actin filament associated protein 1 FUNCTION: Can cross-link actin filaments into both network and bundle structures (By similarity). May modulate changes in actin filament integrity and induce lamellipodia formation. May function as an adapter molecule that links other proteins, such as SRC and PKC to the actin cytoskeleton. Seems to play a role in the development and progression of prostate adenocarcinoma by regulating cell-matrix adhesions and migration in the cancer cells. {ECO:0000250, ECO:0000269|PubMed:15485829}.; . TISSUE SPECIFICITY: Low expression in normal breast epithelial cell line MCF-10A and in tumorigenic breast cancer cell lines MCF- 7, T-47D and ZR-75-1. Highly expressed in the invasive breast cancer cell lines MDA-MB-231 and MDA-MB-435. Overexpressed in prostate carcinoma. {ECO:0000269|PubMed:17520695, ECO:0000269|PubMed:17885682}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;amnion;head and neck;cervix;kidney;mammary gland;stomach;aorta;cerebellum; trigeminal ganglion; 0.14735 . -1.964136947 1.840056617 1928.06896 8.08165 AFAP1-AS1 . . . AFAP1 antisense RNA 1 . . . . . . . . . . . AFAP1L1 4.06878415314462e-08 0.986445947085198 0.0135540122269606 actin filament associated protein 1 like 1 FUNCTION: May be involved in podosome and invadosome formation. {ECO:0000269|PubMed:21333378}.; . TISSUE SPECIFICITY: Expressed in breast, colon and brain. In all 3 tissues, expressed in the microvasculature (at protein level). In addition, in the breast, found in the contractile myoepithelial cell layer which surrounds the breast ducts (at protein level). In the colon, expressed in the mucous membrane and colonic crypts and in the smooth muscle cell layer which provide movement of the colon (at protein level). In the cerebellum, localized around the Purkinje neurons and the granule cells of the granular layer, but not inside cell bodies (at protein level). Outside of the cerebellar cortex, expressed in glial cells (at protein level). Highly expressed away from the cell bodies within the dentate nucleus (at protein level). {ECO:0000269|PubMed:21333378}.; ovary;salivary gland;colon;skin;uterus;prostate;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;oral cavity;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta; dorsal root ganglion;superior cervical ganglion;medulla oblongata;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.09622 0.10351 -0.124924535 44.10238264 344.87064 3.93917 AFAP1L2 0.446972663901368 0.553016283965668 1.10521329646852e-05 actin filament associated protein 1 like 2 FUNCTION: May play a role in a signaling cascade by enhancing the kinase activity of SRC. Contributes to SRC-regulated transcription activation. {ECO:0000269|PubMed:17412687}.; . TISSUE SPECIFICITY: Detected in spleen and thyroid, and at lower levels in kidney, brain, lung and pancreas. {ECO:0000269|PubMed:17412687}.; ovary;sympathetic chain;colon;parathyroid;choroid;fovea centralis;skin;retina;prostate;optic nerve;frontal lobe;cochlea;thyroid;iris;testis;brain;unclassifiable (Anatomical System);heart;blood;lens;skeletal muscle;lung;epididymis;placenta;macula lutea;liver;spleen;mammary gland; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.26572 0.10661 0.788095311 87.2965322 1227.50086 6.62323 AFD1 . . . acrofacial dysostosis 1, Nager type . . . . . . . . . . . AFF1 0.47664697267645 0.523352666558806 3.60764743818481e-07 AF4/FMR2 family member 1 . DISEASE: Note=A chromosomal aberration involving AFF1 is associated with acute leukemias. Translocation t(4;11)(q21;q23) with KMT2A/MLL1. The result is a rogue activator protein.; . myocardium;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;lung;pia mater;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;thymus; superior cervical ganglion;thyroid;placenta;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09740 0.18480 -1.183251814 5.909412597 190.31308 2.99434 AFF2 0.998760604472339 0.00123939479665652 7.31004530469742e-10 AF4/FMR2 family member 2 FUNCTION: RNA-binding protein. Might be involved in alternative splicing regulation through an interaction with G-quartet RNA structure. {ECO:0000269|PubMed:19136466}.; . TISSUE SPECIFICITY: Brain (most abundant in hippocampus and amygdala), placenta and lung.; unclassifiable (Anatomical System);whole body;lung;frontal lobe;placenta;testis;colon;blood;germinal center;brain;skeletal muscle;retina;bone marrow; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;temporal lobe;ciliary ganglion;kidney;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.31732 0.27963 -1.083859071 7.195093182 51.11958 1.40875 AFF2-IT1 . . . AFF2 intronic transcript 1 . . . . . . . . . . . AFF3 0.998912591236449 0.0010874087591486 4.40253701941667e-12 AF4/FMR2 family member 3 FUNCTION: Putative transcription activator that may function in lymphoid development and oncogenesis. Binds, in vitro, to double- stranded DNA.; . TISSUE SPECIFICITY: Preferentially expressed in lymphoid tissues, highest levels being found in the thymus.; unclassifiable (Anatomical System);ovary;blood;skeletal muscle;lung;optic nerve;frontal lobe;placenta;bone;iris;testis;head and neck;cervix;germinal center;brain;cerebellum;thymus; medulla oblongata;superior cervical ganglion;pons;trigeminal ganglion; 0.81091 0.12610 -1.455091209 3.886529842 210.2759 3.13007 AFF4 0.999997450786603 2.54921339588029e-06 1.02911407654573e-15 AF4/FMR2 family member 4 FUNCTION: Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression. {ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948, ECO:0000269|PubMed:23251033}.; DISEASE: Note=A chromosomal aberration involving AFF4 is found in acute lymphoblastic leukemia (ALL). Insertion ins(5;11)(q31;q13q23) that forms a KMT2A/MLL1-AFF4 fusion protein.; DISEASE: CHOPS syndrome (CHOPS) [MIM:616368]: A syndrome characterized by cognitive impairment, coarse facies, heart defects, obesity, pulmonary involvement, short stature, and skeletal dysplasia. {ECO:0000269|PubMed:25730767}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. Strongly expressed in heart, placenta, skeletal muscle, pancreas and to a lower extent in brain. {ECO:0000269|PubMed:10588740, ECO:0000269|PubMed:12065898}.; medulla oblongata;ovary;sympathetic chain;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;pituitary gland;testis;amniotic fluid;germinal center;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;appendix;testis;atrioventricular node;skeletal muscle; 0.70552 0.11325 -0.554717505 19.79830149 144.86962 2.62144 AFG3L1P . . . AFG3 like matrix AAA peptidase subunit 1, pseudogene . . . unclassifiable (Anatomical System);islets of Langerhans;blood;skeletal muscle;retina;breast;prostate;lung;frontal lobe;thyroid;placenta;visual apparatus;hippocampus;pituitary gland;hypopharynx;duodenum;liver;testis;head and neck;spleen;brain;mammary gland;bladder; . 0.08873 . . . . . AFG3L2 0.0147221162102033 0.98526771892612 1.01648636764575e-05 AFG3 like matrix AAA peptidase subunit 2 FUNCTION: ATP-dependent protease which is essential for axonal development. {ECO:0000250}.; DISEASE: Spastic ataxia 5, autosomal recessive (SPAX5) [MIM:614487]: A neurodegenerative disorder characterized by early onset spasticity, peripheral neuropathy, ptosis, oculomotor apraxia, dystonia, cerebellar atrophy, and progressive myoclonic epilepsy. {ECO:0000269|PubMed:22022284}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Highly expressed in the cerebellar Purkinje cells. {ECO:0000269|PubMed:20208537}.; myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;gum;thyroid;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;cerebral cortex;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;kidney;stomach; trigeminal ganglion; 0.52970 0.10986 -0.602450568 17.91106393 36.24735 1.08596 AFG3L2P1 . . . AFG3 like AAA ATPase 2 pseudogene 1 . . . . . . . . . . . AFM 2.50671195979513e-12 0.0685753194744558 0.931424680523038 afamin FUNCTION: Vitamin E binding protein. May transport vitamin E in body fluids under conditions where the lipoprotein system is not sufficient. May be involved in the regulation and transport of vitamin E at the blood-brain barrier. {ECO:0000269|PubMed:12463752, ECO:0000269|PubMed:15952736, ECO:0000269|PubMed:19046407}.; . TISSUE SPECIFICITY: High level detected in plasma but also in extravascular fluids such as follicular and cerebrospinal fluids (at protein level). {ECO:0000269|PubMed:15952736}.; unclassifiable (Anatomical System);liver;spleen;kidney; superior cervical ganglion;fetal liver;liver;ciliary ganglion;kidney;atrioventricular node; 0.15202 0.12722 0.486911049 79.46449634 492.22953 4.56205 AFMID 0.0021381282329124 0.978596648328747 0.0192652234383403 arylformamidase FUNCTION: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites. {ECO:0000255|HAMAP-Rule:MF_03014}.; . . unclassifiable (Anatomical System);uterus;frontal lobe;ovary;placenta;hippocampus;bone marrow; superior cervical ganglion;trigeminal ganglion; 0.06561 0.21820 0.619191319 83.36282142 843.45803 5.68526 AFP 4.89578911326565e-05 0.992382704948871 0.00756833715999618 alpha fetoprotein FUNCTION: Binds copper, nickel, and fatty acids as well as, and bilirubin less well than, serum albumin. Only a small percentage (less than 2%) of the human AFP shows estrogen-binding properties.; DISEASE: Alpha-fetoprotein deficiency (AFPD) [MIM:615969]: A benign condition characterized by undetectable AFP levels in the amniotic fluid. Affected individuals are asymptomatic and present normal development. {ECO:0000269|PubMed:15280901, ECO:0000269|PubMed:18854864}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Alpha-fetoprotein, hereditary persistence (HPAFP) [MIM:615970]: A benign autosomal dominant condition characterized by continued expression of alpha-fetoprotein in adult life. {ECO:0000269|PubMed:7684942}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma. Synthesized by the fetal liver and yolk sac.; unclassifiable (Anatomical System);lung;whole body;ovary;heart;adrenal gland;bone;placenta;liver;colon;parathyroid;spleen;brain; fetal liver;fetal lung; 0.57958 0.75000 0.290313621 71.56758669 413.78029 4.26102 AFTPH 0.996888387523368 0.00311157837519335 3.41014382817486e-08 aftiphilin FUNCTION: May play a role in membrane trafficking.; . . ovary;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;muscle;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.53424 0.08484 0.181903047 66.2361406 1906.79944 8.03762 AGA 0.000640803798191545 0.908641016799679 0.0907181794021294 aspartylglucosaminidase FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.; DISEASE: Aspartylglucosaminuria (AGU) [MIM:208400]: An inborn lysosomal storage disease causing excess accumulation of glycoasparagine in the body tissues and its increased excretion in urine. Clinical features include mild to severe mental retardation manifesting from the age of two, coarse facial features and mild connective tissue abnormalities. {ECO:0000269|PubMed:11309371, ECO:0000269|PubMed:1703489, ECO:0000269|PubMed:1904874, ECO:0000269|PubMed:2011603, ECO:0000269|PubMed:8776587, ECO:0000269|PubMed:9137882}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;testis;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.03662 0.22020 0.753291803 86.71266808 137.5941 2.55335 AGAP1 0.999356435740804 0.000643564253136004 6.05969340535091e-12 ArfGAP with GTPase domain, ankyrin repeat and PH domain 1 FUNCTION: GTPase-activating protein for ARF1 and, to a lesser extent, ARF5. Directly and specifically regulates the adapter protein 3 (AP-3)-dependent trafficking of proteins in the endosomal-lysosomal system. {ECO:0000269|PubMed:12640130}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12388557, ECO:0000269|PubMed:12640130, ECO:0000269|PubMed:15381706, ECO:0000269|PubMed:16079295}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;whole body;frontal lobe;oesophagus;endometrium;larynx;bone;testis;amniotic fluid;pineal gland;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;liver;head and neck;kidney;mammary gland;stomach; amygdala;occipital lobe;subthalamic nucleus;parietal lobe;cingulate cortex;cerebellum; 0.85482 0.10720 -2.388633592 1.096956829 1398.47314 6.99370 AGAP1-IT1 . . . AGAP1 intronic transcript 1 . . . . . . . . . . . AGAP2 0.999218902067889 0.000781097922396288 9.71455107967392e-12 ArfGAP with GTPase domain, ankyrin repeat and PH domain 2 FUNCTION: GTPase-activating protein (GAP) for ARF1 and ARF5, which also shows strong GTPase activity. Isoform 1 participates in the prevention of neuronal apoptosis by enhancing PI3 kinase activity. It aids the coupling of metabotropic glutamate receptor 1 (GRM1) to cytoplasmic PI3 kinase by interacting with Homer scaffolding proteins, and also seems to mediate anti-apoptotic effects of NGF by activating nuclear PI3 kinase. Isoform 2 does not stimulate PI3 kinase but may protect cells from apoptosis by stimulating Akt. It also regulates the adapter protein 1 (AP-1)-dependent trafficking of proteins in the endosomal system. It seems to be oncogenic. It is overexpressed in cancer cells, prevents apoptosis and promotes cancer cell invasion. {ECO:0000269|PubMed:12640130, ECO:0000269|PubMed:14761976, ECO:0000269|PubMed:15118108, ECO:0000269|PubMed:16079295}.; . TISSUE SPECIFICITY: Isoform 1 is brain-specific. Isoform 2 is ubiquitously expressed, with highest levels in brain and heart. {ECO:0000269|PubMed:12640130, ECO:0000269|PubMed:14761976, ECO:0000269|PubMed:15118108, ECO:0000269|PubMed:16079295, ECO:0000269|PubMed:16150119}.; amygdala;unclassifiable (Anatomical System);ovary;nervous;skeletal muscle;uterus;lung;frontal lobe;bone;hippocampus;liver;testis;spleen;germinal center;mammary gland;brain; amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;temporal lobe;atrioventricular node;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.81690 0.23301 -0.176292081 40.56381222 265.49784 3.49614 AGAP2-AS1 0.0423449093257325 0.846666162968097 0.110988927706171 AGAP2 antisense RNA 1 . . . . . . . . . 13.31983 0.48435 AGAP3 0.991380425409819 0.00861957118321543 3.40696579418365e-09 ArfGAP with GTPase domain, ankyrin repeat and PH domain 3 FUNCTION: GTPase-activating protein for the ADP ribosylation factor family (Potential). GTPase which may be involved in the degradation of expanded polyglutamine proteins through the ubiquitin-proteasome pathway. {ECO:0000269|PubMed:16461359, ECO:0000305}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15381706, ECO:0000269|PubMed:16461359}.; ovary;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;whole body;optic nerve;frontal lobe;cochlea;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;pineal body;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;cornea;placenta;visual apparatus;macula lutea;liver;duodenum;head and neck;kidney;mammary gland;stomach;cerebellum; amygdala;uterus;fetal brain;hypothalamus; . 0.11189 -0.995664936 8.539749941 95.08252 2.10265 AGAP4 . . . ArfGAP with GTPase domain, ankyrin repeat and PH domain 4 FUNCTION: Putative GTPase-activating protein. {ECO:0000305}.; . . lymphoreticular;smooth muscle;colon;choroid;vein;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.19268 . . . 85.99752 1.98008 AGAP5 . . . ArfGAP with GTPase domain, ankyrin repeat and PH domain 5 FUNCTION: Putative GTPase-activating protein. {ECO:0000305}.; . . . . 0.08138 . . . 363.1212 4.03538 AGAP6 . . . ArfGAP with GTPase domain, ankyrin repeat and PH domain 6 FUNCTION: Putative GTPase-activating protein. {ECO:0000305}.; . . . . 0.11483 . . . 2327.2699 8.93906 AGAP7P . . . ArfGAP with GTPase domain, ankyrin repeat and PH domain 7, pseudogene FUNCTION: Putative GTPase-activating protein. {ECO:0000305}.; . . . . 0.12633 . . . . . AGAP9 . . . ArfGAP with GTPase domain, ankyrin repeat and PH domain 9 FUNCTION: Putative GTPase-activating protein. {ECO:0000305}.; . . lymphoreticular;ovary;colon;choroid;vein;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; . 0.08138 . . . . . AGAP10P . . . ArfGAP with GTPase domain, ankyrin repeat and PH domain 10 pseudogene . . . . . . . . . . . AGAP11 . . . ArfGAP with GTPase domain, ankyrin repeat and PH domain 11 FUNCTION: Putative GTPase-activating protein. {ECO:0000305}.; . . . . . . . . . . AGAP12P . . . ArfGAP with GTPase domain, ankyrin repeat and PH domain 12, pseudogene . . . . . . . . . . . AGAP13P . . . ArfGAP with GTPase domain, ankyrin repeat and PH domain 13, pseudogene . . . . . . . . . . . AGAP14P . . . ArfGAP with GTPase domain, ankyrin repeat and PH domain 14, pseudogene FUNCTION: Putative GTPase-activating protein. {ECO:0000305}.; . . . . . . . . . . AGBL1 3.60066917773009e-23 0.00384183172594205 0.996158168274058 ATP/GTP binding protein-like 1 FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5. {ECO:0000250|UniProtKB:Q09M05}.; . TISSUE SPECIFICITY: Expressed in corneal endothelium. {ECO:0000269|PubMed:24094747}.; . . 0.09186 . . . 872.20884 5.74987 AGBL1-AS1 . . . AGBL1 antisense RNA 1 . . . . . . . . . . . AGBL2 6.81051045839789e-12 0.835791621146818 0.164208378846371 ATP/GTP binding protein-like 2 FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Does not show detyrosinase or deglycylase activities from the carboxy-terminus of tubulin. {ECO:0000250|UniProtKB:Q8CDK2, ECO:0000269|PubMed:21303978}.; . . unclassifiable (Anatomical System);lymph node;lung;whole body;heart;nasopharynx;adrenal medulla;testis;spleen;kidney;skeletal muscle; superior cervical ganglion;testis - interstitial;testis;trigeminal ganglion;skeletal muscle; 0.14776 . 0.360092658 74.68152866 330.85509 3.86717 AGBL3 . . . ATP/GTP binding protein-like 3 FUNCTION: Metallocarboxypeptidase that mediates both deglutamylation and deaspartylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates or polyaspartates from the carboxy-terminus of target proteins such as MYLK. Does not show detyrosinase or deglycylase activities from the carboxy- terminus of tubulin. {ECO:0000269|PubMed:17244817}.; . . pancreas;lung;testis;kidney;brain;skin;bone marrow; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17645 0.10771 1.750970652 96.67374381 928.25427 5.91313 AGBL4 3.57830057240453e-06 0.354700690512765 0.645295731186663 ATP/GTP binding protein-like 4 FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5. {ECO:0000250|UniProtKB:Q09LZ8}.; . . . . 0.29873 0.10435 0.617373774 83.25076669 562.55749 4.81361 AGBL4-IT1 . . . AGBL4 intronic transcript 1 . . . . . . . . . . . AGBL5 0.0206948513459665 0.979299006427241 6.14222679225126e-06 ATP/GTP binding protein-like 5 FUNCTION: Metallocarboxypeptidase that mediates tubulin deglutamylation. Specifically catalyzes the deglutamylation of the branching point glutamate side chains generated by post- translational glutamylation in proteins such as tubulins. In contrast, it is not able to act as a long-chain deglutamylase that shortens long polyglutamate chains, a process catalyzed by AGTPBP1/CCP1, AGBL2/CCP2, AGBL3/CCP3, AGBL1/CCP4 and AGBL4/CCP6. {ECO:0000250|UniProtKB:Q09M02}.; . TISSUE SPECIFICITY: Expressed in brain.; myocardium;medulla oblongata;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.29061 . -0.992035476 8.604623732 248.34564 3.39647 AGBL5-AS1 . . . AGBL5 antisense RNA 1 . . . . . . . . . . . AGBL5-IT1 . . . AGBL5 intronic transcript 1 . . . . . . . . . . . AGER 1.46448261051773e-10 0.191638499297883 0.808361500555669 advanced glycosylation end product-specific receptor FUNCTION: Mediates interactions of advanced glycosylation end products (AGE). These are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes. Acts as a mediator of both acute and chronic vascular inflammation in conditions such as atherosclerosis and in particular as a complication of diabetes. AGE/RAGE signaling plays an important role in regulating the production/expression of TNF- alpha, oxidative stress, and endothelial dysfunction in type 2 diabetes. Interaction with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key proinflammatory mediators. Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Receptor for amyloid beta peptide. Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons. ABPP-initiated RAGE signaling, especially stimulation of p38 mitogen-activated protein kinase (MAPK), has the capacity to drive a transport system delivering ABPP as a complex with RAGE to the intraneuronal space. Can also bind oligonucleotides. {ECO:0000250, ECO:0000269|PubMed:19906677, ECO:0000269|PubMed:20943659, ECO:0000269|PubMed:21559403, ECO:0000269|PubMed:21565706}.; . TISSUE SPECIFICITY: Endothelial cells.; . . 0.41188 0.08293 0.597144447 82.7435716 710.51169 5.29697 AGFG1 0.969265961919115 0.030732136604611 1.90147627395208e-06 ArfGAP with FG repeats 1 FUNCTION: Required for vesicle docking or fusion during acrosome biogenesis (By similarity). May play a role in RNA trafficking or localization. In case of infection by HIV-1, acts as a cofactor for viral Rev and promotes movement of Rev-responsive element- containing RNAs from the nuclear periphery to the cytoplasm. This step is essential for HIV-1 replication. {ECO:0000250, ECO:0000269|PubMed:10613896, ECO:0000269|PubMed:14701878, ECO:0000269|PubMed:15749819}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:7634337}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.16340 0.22163 -0.359940251 28.93371078 68.39989 1.71146 AGFG2 0.00476446377841632 0.966035959796201 0.0291995764253826 ArfGAP with FG repeats 2 . . . unclassifiable (Anatomical System);lymph node;cartilage;ovary;lacrimal gland;islets of Langerhans;thyroid;placenta;visual apparatus;liver;spleen;choroid;brain;mammary gland;skeletal muscle;peripheral nerve; dorsal root ganglion;superior cervical ganglion;globus pallidus;pons;atrioventricular node;trigeminal ganglion; 0.15184 . 0.951720429 90.06251474 543.25842 4.74354 AGGF1 6.09962982121775e-05 0.998804460127464 0.00113454357432338 angiogenic factor with G-patch and FHA domains 1 FUNCTION: Promotes angiogenesis and the proliferation of endothelial cells. Able to bind to endothelial cells and promote cell proliferation, suggesting that it may act in an autocrine fashion. {ECO:0000269|PubMed:14961121}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in endothelial cells, vascular smooth muscle cells and osteoblasts. Expressed in umbilical vein endothelial cells and microvascular endothelial cells. {ECO:0000269|PubMed:14961121}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.49572 0.09500 -0.088107893 47.06298655 1206.53389 6.57957 AGGF1P1 . . . angiogenic factor with G-patch and FHA domains 1 pseudogene 1 . . . . . . . . . . . AGGF1P2 . . . angiogenic factor with G-patch and FHA domains 1 pseudogene 2 . . . . . . . . . . . AGGF1P3 . . . angiogenic factor with G-patch and FHA domains 1 pseudogene 3 . . . . . . . . . . . AGGF1P4 . . . angiogenic factor with G-patch and FHA domains 1 pseudogene 4 . . . . . . . . . . . AGGF1P5 . . . angiogenic factor with G-patch and FHA domains 1 pseudogene 5 . . . . . . . . . . . AGGF1P6 . . . angiogenic factor with G-patch and FHA domains 1 pseudogene 6 . . . . . . . . . . . AGGF1P7 . . . angiogenic factor with G-patch and FHA domains 1 pseudogene 7 . . . . . . . . . . . AGGF1P8 . . . angiogenic factor with G-patch and FHA domains 1 pseudogene 8 . . . . . . . . . . . AGGF1P9 . . . angiogenic factor with G-patch and FHA domains 1 pseudogene 9 . . . . . . . . . . . AGGF1P10 . . . angiogenic factor with G-patch and FHA domains 1 pseudogene 10 . . . . . . . . . . . AGK 2.4706842233331e-06 0.978208278970493 0.0217892503452834 acylglycerol kinase FUNCTION: Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively. Does not phosphorylate sphingosine. Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth. {ECO:0000269|PubMed:15939762}.; DISEASE: Cataract 38 (CTRCT38) [MIM:614691]: An opacification of the crystalline lens of the eye becoming evident at birth. It frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. {ECO:0000269|PubMed:22415731}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in muscle, heart, kidney and brain. {ECO:0000269|PubMed:15939762}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;cingulate cortex;parietal lobe; 0.18005 0.12429 0.395088462 76.15003539 104.35672 2.20843 AGKP1 . . . acylglycerol kinase pseudogene 1 . . . . . . . . . . . AGL 2.30929380571103e-15 0.999885178919044 0.000114821080953519 amylo-alpha-1, 6-glucosidase, 4-alpha-glucanotransferase FUNCTION: Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4- alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6- glucosidase in glycogen degradation.; DISEASE: Glycogen storage disease 3 (GSD3) [MIM:232400]: A metabolic disorder associated with an accumulation of abnormal glycogen with short outer chains. It is clinically characterized by hepatomegaly, hypoglycemia, short stature, and variable myopathy. Glycogen storage disease type 3 includes different forms: GSD type 3A patients lack glycogen debrancher enzyme activity in both liver and muscle, while GSD type 3B patients are enzyme-deficient in liver only. In rare cases, selective loss of only 1 of the 2 debranching activities, glucosidase or transferase, results in GSD type 3C or type 3D, respectively. {ECO:0000269|PubMed:10571954}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver, kidney and lymphoblastoid cells express predominantly isoform 1; whereas muscle and heart express not only isoform 1, but also muscle-specific isoform mRNAs (isoforms 2, 3 and 4). Isoforms 5 and 6 are present in both liver and muscle.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;spinal cord;urinary;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;head and neck;cervix;kidney;stomach; superior cervical ganglion;tongue;thyroid;prefrontal cortex;trigeminal ganglion;skeletal muscle; 0.44349 0.24792 1.859295831 97.15734843 3139.05955 10.67310 AGMAT 0.00367262488905154 0.844985584886359 0.15134179022459 agmatinase . . TISSUE SPECIFICITY: Highly expressed in liver and kidney. Also found in skeletal muscle, fetal liver, brain, testis, skin and the gastrointestinal tract. Within brain, expression is higher in the cerebral cortex with lower levels in the medulla and spinal cord. {ECO:0000269|PubMed:11804860, ECO:0000269|PubMed:11914032}.; . . 0.10285 0.21335 0.108486928 61.90728946 1591.54038 7.37927 AGMO 3.25792688425734e-07 0.774065265660049 0.225934408547263 alkylglycerol monooxygenase FUNCTION: Glyceryl-ether monooxygenase that cleaves the O-alkyl bond of ether lipids. Ether lipids are essential components of brain membranes. {ECO:0000269|PubMed:20643956}.; . . unclassifiable (Anatomical System);colon;kidney;skeletal muscle;stomach; . 0.05711 0.12273 0.402364592 76.45081387 546.90919 4.75481 AGMX2 . . . agammaglobulinemia, X-linked 2 (with growth hormone deficiency) . . . . . . . . . . . AGO1 0.999999463471423 5.36528577125832e-07 1.14227189142122e-16 argonaute 1, RISC catalytic component FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) or short interfering RNAs (siRNAs), and represses the translation of mRNAs which are complementary to them. Lacks endonuclease activity and does not appear to cleave target mRNAs. Also required for transcriptional gene silencing (TGS) of promoter regions which are complementary to bound short antigene RNAs (agRNAs). {ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:16936728, ECO:0000269|PubMed:18771919}.; . . . . 0.08526 0.16113 -0.80269335 12.23755603 8.45278 0.30967 AGO2 0.999992248962312 7.75103761200044e-06 7.63427680807739e-14 argonaute 2, RISC catalytic component FUNCTION: Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. May inhibit translation initiation by binding to the 7-methylguanosine cap, thereby preventing the recruitment of the translation initiation factor eIF4-E. May also inhibit translation initiation via interaction with EIF6, which itself binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur. In some cases RISC-mediated translational repression is also observed for miRNAs that perfectly match the 3' untranslated region (3'-UTR). Can also up-regulate the translation of specific mRNAs under certain growth conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF-alpha) mRNA and up-regulates translation under conditions of serum starvation. Also required for transcriptional gene silencing (TGS), in which short RNAs known as antigene RNAs or agRNAs direct the transcriptional repression of complementary promoter regions. {ECO:0000269|PubMed:15105377, ECO:0000269|PubMed:15260970, ECO:0000269|PubMed:15284456, ECO:0000269|PubMed:15337849, ECO:0000269|PubMed:15800637, ECO:0000269|PubMed:16081698, ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387, ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:16756390, ECO:0000269|PubMed:16936728, ECO:0000269|PubMed:17382880, ECO:0000269|PubMed:17507929, ECO:0000269|PubMed:17524464, ECO:0000269|PubMed:17531811, ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:18048652, ECO:0000269|PubMed:18178619, ECO:0000269|PubMed:18690212, ECO:0000269|PubMed:18771919, ECO:0000269|PubMed:19167051, ECO:0000269|PubMed:23746446}.; . . . . 0.69949 0.13776 -1.42004951 4.104741684 3.51322 0.12822 AGO3 0.999998843614557 1.15638544265931e-06 7.41553644412861e-16 argonaute 3, RISC catalytic component FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) and represses the translation of mRNAs which are complementary to them. Lacks endonuclease activity and does not appear to cleave target mRNAs. Proposed to be involved in stabilization of small RNA derivates (riRNA) derived from processed RNA polymerase III-transcribed Alu repeats containing a DR2 retinoic acid response element (RARE) in stem cells and in the subsequent riRNA-dependent degradation of a subset of RNA polymerase II-transcribed coding mRNAs by recruiting a mRNA decapping complex involving EDC4. {ECO:0000255|HAMAP- Rule:MF_03032, ECO:0000269|PubMed:18771919, ECO:0000269|PubMed:23064648}.; . . . . 0.15509 0.10665 -1.001120478 8.321538099 11.52402 0.41564 AGO4 0.990043812111039 0.00995618690766232 9.81298737322311e-10 argonaute 4, RISC catalytic component FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) and represses the translation of mRNAs which are complementary to them. Lacks endonuclease activity and does not appear to cleave target mRNAs. Also required for RNA-directed transcription and replication of the human hapatitis delta virus (HDV). {ECO:0000255|HAMAP- Rule:MF_03033, ECO:0000269|PubMed:15337849, ECO:0000269|PubMed:18552826, ECO:0000269|PubMed:18771919}.; . . . . 0.08477 0.14026 -0.890882376 10.30313753 19.9687 0.68036 AGPAT1 0.984453681304784 0.0155376947584999 8.62393671629466e-06 1-acylglycerol-3-phosphate O-acyltransferase 1 FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. {ECO:0000269|PubMed:21873652}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in adipose tissue and at high levels in testis and pancreas. Expressed at lower levels in tissues such as heart, brain, placenta, kidney, lung, spleen, thymus, prostate, ovary, intestine, colon, leukocyte and liver. {ECO:0000269|PubMed:21873652}.; lymphoreticular;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;spinal cord;adrenal cortex;lens;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;pancreas;lung;adrenal gland;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus;cerebellum; . 0.38208 . 0.147123112 64.11299835 18.97055 0.65473 AGPAT2 0.000150355052372305 0.662704344834553 0.337145300113074 1-acylglycerol-3-phosphate O-acyltransferase 2 FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. {ECO:0000269|PubMed:15629135, ECO:0000269|PubMed:21873652, ECO:0000269|PubMed:9242711}.; DISEASE: Congenital generalized lipodystrophy 1 (CGL1) [MIM:608594]: An autosomal recessive disorder characterized by a near complete absence of adipose tissue, extreme insulin resistance, hypertriglyceridemia, hepatic steatosis and early onset of diabetes. {ECO:0000269|PubMed:11967537}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly in adipose tissue, pancreas and liver. {ECO:0000269|PubMed:21873652}.; . . 0.10250 0.16015 0.198490371 67.30360934 430.44157 4.33028 AGPAT3 0.994454771437506 0.00554453781791517 6.90744578783821e-07 1-acylglycerol-3-phosphate O-acyltransferase 3 FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Acts on LPA containing saturated or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or C18:2-CoA as the acyl donor. Also acts on lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidylserine using C18:1 or C20:4-CoA (PubMed:21173190). Has a preference for arachidonoyl-CoA as a donor. Has also a modest lysophosphatidylinositol acyltransferase (LPIAT) activity, converts lysophosphatidylinositol (LPI) into phosphatidylinositol (By similarity). {ECO:0000250|UniProtKB:Q9D517, ECO:0000269|PubMed:21173190}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in testis, pancreas and kidney, followed by spleen, lung, adipose tissue and liver. {ECO:0000269|PubMed:21173190}.; myocardium;smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;oesophagus;thyroid;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis;pons;trigeminal ganglion; 0.11198 0.10697 -0.492218069 22.35786742 57.85485 1.53749 AGPAT4 0.674499951839515 0.325297171162999 0.000202876997485756 1-acylglycerol-3-phosphate O-acyltransferase 4 FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in skeletal muscle, followed by heart, liver, prostate and thymus. {ECO:0000269|PubMed:21173190}.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;muscle;colon;pancreas;whole body;lung;frontal lobe;placenta;bone;hippocampus;alveolus;testis;spleen;kidney;brain;stomach; whole brain;amygdala;subthalamic nucleus;thalamus;occipital lobe;hypothalamus;spinal cord;caudate nucleus; 0.32335 0.10604 -0.514264485 21.41424864 13.17386 0.47964 AGPAT4-IT1 . . . AGPAT4 intronic transcript 1 . . . . . . . . . . . AGPAT5 0.00579495332667733 0.97183773349078 0.0223673131825429 1-acylglycerol-3-phosphate O-acyltransferase 5 FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Acts on LPA containing saturated or unsaturated fatty acids C15:0-C20:4 at the sn-1 position using C18:1-CoA as the acyl donor. Also acts on lysophosphatidylethanolamine using oleoyl-CoA, but not arachidonoyl-CoA, and lysophosphatidylinositol using arachidonoyl-CoA, but not oleoyl-CoA. Activity toward lysophosphatidylglycerol not detectable. {ECO:0000269|PubMed:21173190}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16620771, ECO:0000269|PubMed:21173190}.; smooth muscle;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; amygdala;subthalamic nucleus;caudate nucleus;trigeminal ganglion; 0.55788 0.12279 -0.512444034 21.55579146 130.88869 2.49182 AGPAT5P1 . . . 1-acylglycerol-3-phosphate O-acyltransferase 5 pseudogene 1 . . . . . . . . . . . AGPS 0.998805101972043 0.0011948973592847 6.68672706746257e-10 alkylglycerone phosphate synthase FUNCTION: Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids. {ECO:0000250}.; DISEASE: Rhizomelic chondrodysplasia punctata 3 (RCDP3) [MIM:600121]: A disease characterized by rhizomelic shortening of femur and humerus, vertebral disorders, cataract, cutaneous lesions and severe mental retardation. {ECO:0000269|PubMed:11152660, ECO:0000269|PubMed:21990100, ECO:0000269|PubMed:9553082}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;colon;skin;skeletal muscle;retina;breast;uterus;prostate;atrium;lung;frontal lobe;bone;visual apparatus;liver;testis;cervix;spleen;germinal center;kidney;brain;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.51504 0.19677 -0.383807564 27.41802312 14.28274 0.51625 AGR2 0.335455070189878 0.649799384093669 0.0147455457164536 anterior gradient 2, protein disulphide isomerase family member FUNCTION: Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells (By similarity). Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth. {ECO:0000250, ECO:0000269|PubMed:18199544}.; . TISSUE SPECIFICITY: Expressed strongly in trachea, lung, stomach, colon, prostate and small intestine. Expressed weakly in pituitary gland, salivary gland, mammary gland, bladder, appendix, ovary, fetal lung, uterus, pancreas, kidney, fetal kidney, testis, placenta, thyroid gland and in estrogen receptor (ER)-positive breast cancer cell lines. {ECO:0000269|PubMed:9790916}.; . . 0.07543 0.10211 -0.141298762 42.87567823 35.53371 1.07144 AGR3 3.84686825137146e-14 0.000840957152195819 0.999159042847766 anterior gradient 3, protein disulphide isomerase family member FUNCTION: Required for calcium-mediated regulation of ciliary beat frequency and mucociliary clearance in the airway. Might be involved in the regulation of intracellular calcium in tracheal epithelial cells. {ECO:0000250|UniProtKB:Q8R3W7}.; . TISSUE SPECIFICITY: Expressed in the lung, in the ciliated cells of the airway epithelium (PubMed:25751668). Expression increased with differentiation of airway epithelial cells (PubMed:25751668). Not detected in the mucous cells (PubMed:25751668). Expressed in ciliated cells in the oviduct (PubMed:26170690). Also detected in stomach, colon, prostate and liver (PubMed:25751668). Expressed in breast, ovary, prostate and liver cancer (PubMed:26170690). Expression is associated with the level of differentiation of breast cancer (at protein level) (PubMed:26170690). {ECO:0000269|PubMed:25751668, ECO:0000269|PubMed:26170690}.; unclassifiable (Anatomical System);cartilage;ovary;heart;salivary gland;intestine;pharynx;colon;blood;skin;breast;uterus;bile duct;prostate;lung;cornea;visual apparatus;liver;testis;kidney;brain;mammary gland;stomach; . 0.13682 0.11872 -0.185391282 39.67916962 15.72876 0.56023 AGRN 0.17335234048116 0.826647657926747 1.59209302093807e-09 agrin FUNCTION: Isoform 1: heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)- subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This secreted isoform forms a bridge, after release from motor neurons, to basal lamina through binding laminin via the NtA domain.; FUNCTION: Isoform 1, isoform 4 and isoform 5: neuron-specific (z+) isoforms that contain C-terminal insertions of 8-19 AA are potent activators of AChR clustering. Isoform 5, agrin (z+8), containing the 8-AA insert, forms a receptor complex in myotubules containing the neuronal AGRN, the muscle-specific kinase MUSK and LRP4, a member of the LDL receptor family. The splicing factors, NOVA1 and NOVA2, regulate AGRN splicing and production of the 'z' isoforms.; FUNCTION: Agrin N-terminal 110 kDa subunit: is involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling (By similarity). {ECO:0000250, ECO:0000269|PubMed:19631309, ECO:0000269|PubMed:21969364}.; DISEASE: Myasthenic syndrome, congenital, 8 (CMS8) [MIM:615120]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness. CMS8 is an autosomal recessive disease characterized by prominent defects of both the pre- and postsynaptic regions. Affected individuals have onset of muscle weakness in early childhood; the severity of the weakness and muscles affected is variable. {ECO:0000269|PubMed:19631309, ECO:0000269|PubMed:22205389, ECO:0000269|PubMed:24951643}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in basement membranes of lung and kidney. Muscle- and neuron-specific isoforms are found. Isoforms (y+) with the 4 AA insert and (z+8) isoforms with the 8 AA insert are all neuron-specific. Isoforms (z+11) are found in both neuronal and non-neuronal tissues. {ECO:0000269|PubMed:16487930, ECO:0000269|PubMed:20551380, ECO:0000269|PubMed:9652404}.; . . 0.40227 0.64499 -0.224542487 37.33191791 1338.6014 6.86990 AGRP 0.0903872520171276 0.765261002068523 0.14435174591435 agouti related neuropeptide FUNCTION: Plays a role in weight homeostasis. Involved in the control of feeding behavior through the central melanocortin system. Acts as alpha melanocyte-stimulating hormone antagonist by inhibiting cAMP production mediated by stimulation of melanocortin receptors within the hypothalamus and adrenal gland. Has very low activity with MC5R (By similarity). Is an inverse agonist for MC3R and MC4R being able to suppress their constitutive activity. It promotes MC3R and MC4R endocytosis in an arrestin-dependent manner. {ECO:0000250, ECO:0000269|PubMed:10371151, ECO:0000269|PubMed:11145747, ECO:0000269|PubMed:15927146, ECO:0000269|PubMed:17041250, ECO:0000269|PubMed:9892020}.; DISEASE: Obesity (OBESITY) [MIM:601665]: A condition characterized by an increase of body weight beyond the limitation of skeletal and physical requirements, as the result of excessive accumulation of body fat. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed primarily in the adrenal gland, subthalamic nucleus, and hypothalamus, with a lower level of expression occurring in testis, lung, and kidney.; unclassifiable (Anatomical System);liver;spleen;kidney;germinal center; . 0.70220 0.35308 -0.007201372 53.19061099 84.5137 1.95702 AGT 1.57429487936421e-09 0.0314993080309962 0.968500690394709 angiotensinogen FUNCTION: Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis.; FUNCTION: Angiotensin-3: stimulates aldosterone release.; DISEASE: Essential hypertension (EHT) [MIM:145500]: A condition in which blood pressure is consistently higher than normal with no identifiable cause. {ECO:0000269|PubMed:1394429, ECO:0000269|PubMed:8513325}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Renal tubular dysgenesis (RTD) [MIM:267430]: Autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype). {ECO:0000269|PubMed:16116425}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; . . 0.50213 0.62272 0.492370491 79.60603916 587.2068 4.91570 AGTPBP1 0.476341243345348 0.523658741849076 1.48055760354976e-08 ATP/GTP binding protein 1 FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5. {ECO:0000250|UniProtKB:Q641K1}.; . . unclassifiable (Anatomical System);lymph node;cartilage;hypothalamus;colon;blood;skeletal muscle;bone marrow;uterus;prostate;lung;frontal lobe;endometrium;bone;thyroid;liver;testis;cervix;germinal center;brain;mammary gland;stomach; amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;fetal brain;prefrontal cortex;trigeminal ganglion;cingulate cortex; 0.72062 0.14321 -1.083859071 7.195093182 935.85943 5.93224 AGTR1 0.00727625074022701 0.769562881583272 0.223160867676501 angiotensin II receptor type 1 FUNCTION: Receptor for angiotensin II. Mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system.; DISEASE: Renal tubular dysgenesis (RTD) [MIM:267430]: Autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype). {ECO:0000269|PubMed:16116425}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver, lung, adrenal and adrenocortical adenomas.; unclassifiable (Anatomical System);myocardium;cartilage;heart;ovary;parathyroid;breast;whole body;lung;larynx;placenta;liver;testis;head and neck;spleen;kidney;mammary gland;gall bladder; dorsal root ganglion;fetal liver;superior cervical ganglion;adipose tissue;adrenal gland;placenta;liver;adrenal cortex;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.16778 0.82322 0.106667882 61.73036093 49.07123 1.36931 AGTR2 0.0125489579921142 0.651428928078237 0.336022113929648 angiotensin II receptor type 2 FUNCTION: Receptor for angiotensin II. Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation. {ECO:0000269|PubMed:15123706}.; . TISSUE SPECIFICITY: In adult, highly expressed in myometrium with lower levels in adrenal gland and fallopian tube. Expressed in the cerebellum. Very highly expressed in fetal kidney and intestine. {ECO:0000269|PubMed:12089445}.; . . 0.64835 0.42494 0.305084559 72.22811984 78.07929 1.86394 AGTRAP 0.0416634032877011 0.845207744495446 0.113128852216853 angiotensin II receptor associated protein FUNCTION: Appears to be a negative regulator of type-1 angiotensin II receptor-mediated signaling by regulating receptor internalisation as well as mechanism of receptor desensitization such as phosphorylation. Induces also a decrease in cell proliferation and angiotensin II-stimulated transcriptional activity. {ECO:0000269|PubMed:12960423}.; . TISSUE SPECIFICITY: Ubiquitous but more abundant in kidney, heart, pancreas and thyroid. {ECO:0000269|PubMed:11733189}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;brain;artery;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; . 0.11797 . -0.115612493 45.12856806 12.51479 0.45540 AGXT 0.00359436899475076 0.953962700286555 0.0424429307186945 alanine-glyoxylate aminotransferase . DISEASE: Hyperoxaluria primary 1 (HP1) [MIM:259900]: An inborn error of glyoxylate metabolism characterized by increased excretion of oxalate and glycolate, and progressive tissue accumulation of insoluble calcium oxalate. Affected individuals are at risk for nephrolithiasis, nephrocalcinosis and early onset end-stage renal disease. {ECO:0000269|PubMed:10394939, ECO:0000269|PubMed:10453743, ECO:0000269|PubMed:10541294, ECO:0000269|PubMed:10862087, ECO:0000269|PubMed:12559847, ECO:0000269|PubMed:1301173, ECO:0000269|PubMed:1349575, ECO:0000269|PubMed:15253729, ECO:0000269|PubMed:15849466, ECO:0000269|PubMed:15961946, ECO:0000269|PubMed:15963748, ECO:0000269|PubMed:16971151, ECO:0000269|PubMed:1703535, ECO:0000269|PubMed:17495019, ECO:0000269|PubMed:2039493, ECO:0000269|PubMed:23229545, ECO:0000269|PubMed:24055001, ECO:0000269|PubMed:24934730, ECO:0000269|PubMed:26149463, ECO:0000269|PubMed:8101040, ECO:0000269|PubMed:9192270, ECO:0000269|PubMed:9604803}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver.; unclassifiable (Anatomical System);placenta;liver;colon;spleen; superior cervical ganglion;fetal liver;liver;fetal lung;atrioventricular node;kidney;pons;trigeminal ganglion;skeletal muscle; 0.59321 0.59981 0.644875971 84.10002359 526.88786 4.68568 AGXT2 4.66554613813699e-15 0.0123564519056362 0.987643548094359 alanine--glyoxylate aminotransferase 2 FUNCTION: Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure. {ECO:0000269|PubMed:20018850, ECO:0000269|PubMed:23023372, ECO:0000269|PubMed:24586340}.; . . unclassifiable (Anatomical System);whole body;liver;spleen;kidney; dorsal root ganglion;superior cervical ganglion;fetal liver;globus pallidus;ciliary ganglion;kidney;atrioventricular node;pons;trigeminal ganglion;skin; 0.15644 0.18377 0.891034851 89.2663364 3193.72069 10.77276 AHCTF1 0.999999999875185 1.24814676701532e-10 1.33622555195251e-27 AT-hook containing transcription factor 1 FUNCTION: Required for the assembly of a functional nuclear pore complex (NPC) on the surface of chromosomes as nuclei form at the end of mitosis. May initiate NPC assembly by binding to chromatin and recruiting the Nup107-160 subcomplex of the NPC. Also required for the localization of the Nup107-160 subcomplex of the NPC to the kinetochore during mitosis and for the completion of cytokinesis. {ECO:0000269|PubMed:17098863, ECO:0000269|PubMed:17235358}.; . . . . . 0.09467 0.536328158 81.01556971 342.36502 3.92380 AHCTF1P1 . . . AT-hook containing transcription factor 1 pseudogene 1 . . . . . . 0.09467 . . . . AHCY 0.94406980715951 0.0558883060327476 4.18868077425528e-05 adenosylhomocysteinase FUNCTION: Adenosylhomocysteine is a competitive inhibitor of S- adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine. {ECO:0000269|PubMed:12590576}.; DISEASE: Hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD) [MIM:613752]: A metabolic disorder characterized by hypermethioninemia associated with failure to thrive, mental and motor retardation, facial dysmorphism with abnormal hair and teeth, and myocardiopathy. {ECO:0000269|PubMed:15024124, ECO:0000269|PubMed:16736098, ECO:0000269|PubMed:19177456, ECO:0000269|PubMed:20852937}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;epidermis;muscle;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; . 0.81482 0.55936 -0.067881249 48.69072895 113.22609 2.31647 AHCYL1 0.999795279646545 0.000204720308555072 4.48999842169599e-11 adenosylhomocysteinase like 1 FUNCTION: Multifaceted cellular regulator which coordinates several essential cellular functions including regulation of epithelial HCO3(-) and fluid secretion, mRNA processing and DNA replication. Regulates ITPR1 sensitivity to inositol 1,4,5- trisphosphate competing for the common binding site and acting as endogenous 'pseudoligand' whose inhibitory activity can be modulated by its phosphorylation status. In the pancreatic and salivary ducts, at resting state, attenuates inositol 1,4,5- trisphosphate-induced calcium release by interacting with ITPR1 (PubMed:16793548). When extracellular stimuli induce ITPR1 phosphorylation or inositol 1,4,5-trisphosphate production, dissociates of ITPR1 to interact with CFTR and SLC26A6 mediating their synergistic activation by calcium and cAMP that stimulates the epithelial secretion of electrolytes and fluid (By similarity). Also activates basolateral SLC4A4 isoform 1 to coordinate fluid and HCO3(-) secretion (PubMed:16769890). Inhibits the effect of STK39 on SLC4A4 and CFTR by recruiting PP1 phosphatase which activates SLC4A4, SLC26A6 and CFTR through dephosphorylation (By similarity). Mediates the induction of SLC9A3 surface expression produced by Angiotensin-2 (PubMed:20584908). Depending on the cell type, activates SLC9A3 in response to calcium or reverses SLC9A3R2-dependent calcium inhibition (PubMed:18829453). May modulate the polyadenylation state of specific mRNAs, both by controlling the subcellular location of FIP1L1 and by inhibiting PAPOLA activity, in response to a stimulus that alters its phosphorylation state (PubMed:19224921). Acts as a (dATP)-dependent inhibitor of ribonucleotide reductase large subunit RRM1, controlling the endogenous dNTP pool and ensuring normal cell cycle progression (PubMed:25237103). {ECO:0000250|UniProtKB:B5DFN2, ECO:0000250|UniProtKB:Q80SW1, ECO:0000269|PubMed:16769890, ECO:0000269|PubMed:16793548, ECO:0000269|PubMed:18829453, ECO:0000269|PubMed:19224921, ECO:0000269|PubMed:20584908, ECO:0000269|PubMed:25237103}.; . TISSUE SPECIFICITY: Expressed in dendritic cells. {ECO:0000269|PubMed:11904675}.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;spinal cord;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;oesophagus;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;small intestine;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;placenta;head and neck;kidney;stomach; whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.35527 0.19105 -0.427900189 25.14744043 137.59573 2.55375 AHCYL2 0.949258836025037 0.0507408918810474 2.72093915685163e-07 adenosylhomocysteinase like 2 FUNCTION: May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate (PubMed:19220705). {ECO:0000250|UniProtKB:A6QLP2, ECO:0000269|PubMed:19220705}.; . . colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;dura mater;germinal center;ciliary body;brain;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;breast;pancreas;pia mater;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;head and neck;kidney;mammary gland;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;thyroid;spinal cord;prefrontal cortex;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.64769 0.18353 -0.427900189 25.14744043 65.05184 1.65876 AHCYP1 . . . adenosylhomocysteinase pseudogene 1 . . . . . . . . . . . AHCYP2 . . . adenosylhomocysteinase pseudogene 2 . . . . . . . . . . . AHCYP3 . . . adenosylhomocysteinase pseudogene 3 . . . . . . . . . . . AHCYP4 . . . adenosylhomocysteinase pseudogene 4 . . . . . . . . . . . AHCYP5 . . . adenosylhomocysteinase pseudogene 5 . . . . . . . . . . . AHCYP6 . . . adenosylhomocysteinase pseudogene 6 . . . . . . . . . . . AHCYP7 . . . adenosylhomocysteinase pseudogene 7 . . . . . . . . . . . AHCYP8 . . . adenosylhomocysteinase pseudogene 8 . . . . . . . . . . . AHDC1 0.999431447817631 0.00056855164157875 5.40790109816031e-10 AT-hook DNA binding motif containing 1 . DISEASE: Mental retardation, autosomal dominant 25 (MRD25) [MIM:615829]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD25 additional features include mild dysmorphism, hypotonia, delayed psychomotor development with absent or poor expressive language, hypoplasia of the corpus callosum, simplified gyral pattern, and delayed myelination. {ECO:0000269|PubMed:24791903}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;fovea centralis;choroid;skin;bone marrow;retina;optic nerve;oesophagus;thyroid;bone;pituitary gland;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;head and neck;kidney;stomach; prefrontal cortex;skeletal muscle; 0.09286 . -1.095046929 6.97688134 544.59826 4.74752 AHI1 3.25663341010612e-14 0.868666138660539 0.131333861339428 Abelson helper integration site 1 FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. {ECO:0000250}.; DISEASE: Joubert syndrome 3 (JBTS3) [MIM:608629]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. Joubert syndrome type 3 shows minimal extra central nervous system involvement and appears not to be associated with renal dysfunction. {ECO:0000269|PubMed:15322546, ECO:0000269|PubMed:15467982, ECO:0000269|PubMed:16453322, ECO:0000269|PubMed:22425360, ECO:0000269|PubMed:23532844}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in the most primitive normal hematopoietic cells. Expressed in brain, particularly in neurons that give rise to the crossing axons of the corticospinal tract and superior cerebellar peduncles. Expressed in kidney (renal collecting duct cells) (at protein level). {ECO:0000269|PubMed:14751929, ECO:0000269|PubMed:15322546, ECO:0000269|PubMed:18633336}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;pineal body;blood;lens;skeletal muscle;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;cerebellum; dorsal root ganglion;medulla oblongata;testis - interstitial;occipital lobe;superior cervical ganglion;hypothalamus;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;pituitary;parietal lobe; 0.15848 0.12754 0.455567154 78.06676103 597.05433 4.94403 AHNAK 0.344567387106657 0.65543257217315 4.072019275324e-08 AHNAK nucleoprotein FUNCTION: May be required for neuronal cell differentiation.; . . ovary;salivary gland;colon;skin;retina;uterus;prostate;frontal lobe;endometrium;larynx;thyroid;bone;iris;pituitary gland;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;spinal cord;urinary;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;alveolus;hypopharynx;head and neck;spleen;kidney;mammary gland;stomach; superior cervical ganglion;olfactory bulb;tongue;atrioventricular node;trigeminal ganglion; 0.19089 . -2.834287974 0.613352206 5147.67106 14.73759 AHNAK2 . . . AHNAK nucleoprotein 2 . . . smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;bone;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;pharynx;blood;lens;bile duct;breast;pancreas;lung;adrenal gland;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach;aorta;cerebellum; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;tongue;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.04780 . 27.59634509 99.99410238 24654.11397 32.49932 AHR 0.999872136742516 0.000127863243218978 1.42651971936925e-11 aryl hydrocarbon receptor FUNCTION: Ligand-activated transcriptional activator. Binds to the XRE promoter region of genes it activates. Activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons. Involved in cell-cycle regulation. Likely to play an important role in the development and maturation of many tissues. Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1. Inhibits PER1 by repressing the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of PER1. {ECO:0000269|PubMed:10395741, ECO:0000269|PubMed:7961644}.; . TISSUE SPECIFICITY: Expressed in all tissues tested including blood, brain, heart, kidney, liver, lung, pancreas and skeletal muscle. {ECO:0000269|PubMed:7515333, ECO:0000269|PubMed:8246913}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;aorta;stomach;thymus; placenta; 0.43923 0.73985 -0.306750577 32.23047889 881.16676 5.78338 AHRR 6.76187936246612e-05 0.977269884822507 0.0226624963838685 aryl-hydrocarbon receptor repressor FUNCTION: Mediates dioxin toxicity and is involved in regulation of cell growth and differentiation. Represses the transcription activity of AHR by competing with this transcription factor for heterodimer formation with the ARNT and subsequently binding to the xenobiotic response element (XRE) sequence present in the promoter regulatory region of variety of genes. Represses CYP1A1 by binding the XRE sequence and recruiting ANKRA2, HDAC4 and/or HDAC5. Autoregulates its expression by associating with its own XRE site. {ECO:0000269|PubMed:17890447, ECO:0000269|PubMed:18172554}.; . TISSUE SPECIFICITY: Highly expressed in testis, lung, ovary, spleen and pancreas. Highly expressed in mononuclear cells (MNCs) from umbilical cord blood. Isoform 3 is highly expressed in lung, kidney, spleen and thymus. Down-regulated malignant tissue from different anatomical origins, including colon, breast, lung, stomach, cervix, and ovary. {ECO:0000269|PubMed:11835227, ECO:0000269|PubMed:14672759, ECO:0000269|PubMed:18172554}.; unclassifiable (Anatomical System);ovary;colon;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;breast;optic nerve;lung;placenta;macula lutea;testis;cervix;brain; whole brain;amygdala;subthalamic nucleus;superior cervical ganglion;skeletal muscle;skin;cerebellum; . 0.16352 1.004917985 90.78792168 1613.48158 7.43304 AHSA1 0.938521220776593 0.061425606192218 5.31730311890099e-05 AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast) FUNCTION: Cochaperone that stimulates HSP90 ATPase activity (By similarity). May affect a step in the endoplasmic reticulum to Golgi trafficking. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in numerous tissues, including brain, heart, skeletal muscle and kidney and, at lower levels, liver and placenta. {ECO:0000269|PubMed:11554768}.; lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;brain;tonsil;heart;cartilage;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; whole brain;thalamus;medulla oblongata;testis - seminiferous tubule;hypothalamus;testis;globus pallidus;parietal lobe; 0.85170 0.12071 -0.315847836 31.68789809 24.65239 0.80979 AHSA2 5.61437783752719e-06 0.140152677851319 0.859841707770844 AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast) FUNCTION: Co-chaperone that stimulates HSP90 ATPase activity. {ECO:0000250}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;muscle;urinary;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;kidney;stomach;aorta;thymus; . 0.05809 . -0.339715008 30.06605331 275.26294 3.55364 AHSG 2.86452047704873e-08 0.0881809660215622 0.911819005333233 alpha-2-HS-glycoprotein FUNCTION: Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Shows affinity for calcium and barium ions.; . TISSUE SPECIFICITY: Synthesized in liver and selectively concentrated in bone matrix. Secreted in plasma. It is also found in dentin in much higher quantities than other plasma proteins.; unclassifiable (Anatomical System);ovary;heart;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;breast;prostate;whole body;lung;cornea;bone;placenta;visual apparatus;liver;testis;spleen;kidney;brain;mammary gland;bladder;thymus; superior cervical ganglion;fetal liver;liver;globus pallidus;fetal lung;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.47188 0.39186 0.687150476 85.17928757 105.08096 2.21767 AHSP 0.00985693954905296 0.600446608494871 0.389696451956076 alpha hemoglobin stabilizing protein FUNCTION: Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia. {ECO:0000269|PubMed:12066189}.; . TISSUE SPECIFICITY: Expressed in blood and bone marrow. {ECO:0000269|PubMed:11231637, ECO:0000269|PubMed:12066189}.; unclassifiable (Anatomical System);heart;blood;fovea centralis;choroid;lens;retina;bone marrow;uterus;pancreas;optic nerve;whole body;lung;macula lutea;visual apparatus;liver;spleen; fetal liver;atrioventricular node;trigeminal ganglion;bone marrow; 0.30869 0.11948 0.413500896 76.67492333 77.31611 1.84726 AIC . . . Aicardi syndrome . . . . . . . . . . . AICDA 0.00125550164168763 0.852580358852799 0.146164139505514 activation-induced cytidine deaminase FUNCTION: Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation, gene conversion, and class- switch recombination in B-lymphocytes. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. {ECO:0000269|PubMed:18722174, ECO:0000269|PubMed:21385873, ECO:0000269|PubMed:21496894, ECO:0000269|PubMed:21518874}.; DISEASE: Immunodeficiency with hyper-IgM 2 (HIGM2) [MIM:605258]: A rare immunodeficiency syndrome characterized by normal or elevated serum IgM levels with absence of IgG, IgA, and IgE. It results in a profound susceptibility to bacterial infections. {ECO:0000269|PubMed:11007475}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Strongly expressed in lymph nodes and tonsils. {ECO:0000269|PubMed:23166356}.; unclassifiable (Anatomical System);nasopharynx;tonsil; . 0.13659 0.44178 0.038710339 56.92380278 40.97303 1.20008 AIDA 0.0823723820518631 0.9074010134654 0.0102266044827372 axin interactor, dorsalization associated FUNCTION: Acts as a ventralizing factor during embryogenesis. Inhibits axin-mediated JNK activation by binding axin and disrupting axin homodimerization. This in turn antagonizes a Wnt/beta-catenin-independent dorsalization pathway activated by AXIN/JNK-signaling (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed in adult tissues, with highest expression in the heart and skeletal muscle. {ECO:0000269|PubMed:17681137}.; ovary;skin;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;cerebellum; . 0.66962 . -0.119252484 44.53880632 8.19212 0.30204 AIF1 0.0127986482867158 0.857938830785659 0.129262520927625 allograft inflammatory factor 1 FUNCTION: Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T- lymphocytes. Enhances lymphocyte migration. Plays a role in vascular inflammation. {ECO:0000269|PubMed:15117732, ECO:0000269|PubMed:16049345, ECO:0000269|PubMed:18699778}.; . TISSUE SPECIFICITY: Detected in T-lymphocytes and peripheral blood mononuclear cells. {ECO:0000269|PubMed:16049345}.; uterus;lymph node;lung;placenta;blood;brain;aorta;bone marrow; . 0.67340 . 0.147123112 64.11299835 770.95879 5.49385 AIF1L 0.0330739002216349 0.820373270214336 0.146552829564029 allograft inflammatory factor 1-like FUNCTION: Actin-binding protein that promotes actin bundling. May neither bind calcium nor depend on calcium for function. {ECO:0000269|PubMed:18699778}.; . . medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;spinal ganglion;brain;pineal gland;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; . 0.21141 0.09886 0.547599505 81.2160887 460.3247 4.44987 AIFM1 0.98463156763188 0.015368088679948 3.43688172081641e-07 apoptosis inducing factor, mitochondria associated 1 FUNCTION: Functions both as NADH oxidoreductase and as regulator of apoptosis. In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase-independent pathway. In contrast, functions as an antiapoptotic factor in normal mitochondria via its NADH oxidoreductase activity. The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA. Interacts with EIF3G,and thereby inhibits the EIF3 machinery and protein synthesis, and activates casapse-7 to amplify apoptosis. Plays a critical role in caspase- independent, pyknotic cell death in hydrogen peroxide-exposed cells. Binds to DNA in a sequence-independent manner. {ECO:0000269|PubMed:17094969, ECO:0000269|PubMed:19418225, ECO:0000269|PubMed:20362274, ECO:0000269|PubMed:23217327}.; DISEASE: Combined oxidative phosphorylation deficiency 6 (COXPD6) [MIM:300816]: A mitochondrial disease resulting in a neurodegenerative disorder characterized by psychomotor delay, hypotonia, areflexia, muscle weakness and wasting. Some patients manifest prenatal ventriculomegaly and severe postnatal encephalomyopathy. {ECO:0000269|PubMed:20362274, ECO:0000269|PubMed:22019070}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cowchock syndrome (COWCK) [MIM:310490]: An X-linked recessive neuromuscular disorder characterized by early childhood onset of a slowly progressive axonal sensorimotor neuropathy associated in some patients with sensorineural deafness and cognitive impairment. {ECO:0000269|PubMed:23217327}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in muscle and skin fibroblasts (at protein level). Isoform 5 is frequently down-regulated in human cancers. {ECO:0000269|PubMed:16365034, ECO:0000269|PubMed:23217327}.; myocardium;lymphoreticular;medulla oblongata;ovary;umbilical cord;skin;bone marrow;retina;prostate;frontal lobe;endometrium;cochlea;thyroid;germinal center;brain;bladder;heart;cartilage;tongue;adrenal cortex;blood;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;amnion;duodenum;head and neck;kidney;stomach; fetal liver;superior cervical ganglion;appendix;testis;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion; 0.32532 0.37971 -0.26993514 34.59542345 36.75135 1.10167 AIFM1P1 . . . apoptosis inducing factor, mitochondria associated 1 pseudogene 1 . . . . . . . . . . . AIFM2 1.41216409648831e-07 0.212623718733714 0.787376140049876 apoptosis inducing factor, mitochondria associated 2 FUNCTION: Oxidoreductase, which may play a role in mediating a p53/TP53-dependent apoptosis response. Probable oxidoreductase that acts as a caspase-independent mitochondrial effector of apoptotic cell death. Binds to DNA in a sequence-independent manner. May contribute to genotoxin-induced growth arrest. {ECO:0000269|PubMed:11980907, ECO:0000269|PubMed:12135761, ECO:0000269|PubMed:15958387}.; . TISSUE SPECIFICITY: Detected in most normal tissues as two transcripts of 1.8 and 4.0 kb in length, respectively. Highly expressed in heart, moderately in liver and skeletal muscles, and expressed at low levels in placenta, lung, kidney, and pancreas. Both transcripts expressed following p53/TP53 induction. The shorter 1.8 kb transcript seems to be the major transcript in EB1 colon cancer cells. {ECO:0000269|PubMed:12135761}.; smooth muscle;ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;visual apparatus;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;adipose tissue;skeletal muscle; 0.18175 0.13527 -0.398573136 26.92852088 1097.00592 6.34173 AIFM3 1.95828310839448e-10 0.619695870783117 0.380304129021054 apoptosis inducing factor, mitochondria associated 3 FUNCTION: Induces apoptosis through a caspase dependent pathway. Reduces mitochondrial membrane potential. {ECO:0000269|PubMed:15764604}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in bone marrow, cerebral cortex, liver, ovary, thymus, thyroid gland and tongue (at protein level). {ECO:0000269|PubMed:15764604}.; unclassifiable (Anatomical System);colon;fovea centralis;pancreas;lung;endometrium;hippocampus;macula lutea;testis;spleen;germinal center;kidney;brain;cerebellum; . 0.14518 0.13207 -0.194700582 39.24274593 396.16868 4.18120 AIG1 1.90321735888132e-05 0.458666385284702 0.541314582541709 androgen-induced 1 FUNCTION: May play a role in androgen-regulated growth of hair follicles.; . TISSUE SPECIFICITY: Highly expressed in heart, ovary, testis, liver, and kidney, at lower levels in spleen, prostate, brain, skeletal muscle, pancreas, small intestine and colon, and undetected in peripheral blood leukocytes, thymus, lung and placenta. AIG1 expression is higher in hair follicles from males than from females. {ECO:0000269|PubMed:11266118}.; ovary;colon;substantia nigra;parathyroid;fovea centralis;skin;retina;uterus;prostate;atrium;frontal lobe;endometrium;bone;iris;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;small intestine;heart;cartilage;cerebellum cortex;islets of Langerhans;hypothalamus;breast;pancreas;pia mater;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;liver;spleen;kidney;stomach; whole brain;dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion; 0.13616 0.08380 -0.339715008 30.06605331 8.3945 0.30681 AIG1P1 . . . androgen-induced 1 pseudogene 1 . . . . . . . . . . . AIH3 . . . amelogenesis imperfecta 3, hypomaturation or hypoplastic type . . . . . . . . . . . AIM1 7.45739464483608e-20 0.299581324918568 0.700418675081432 absent in melanoma 1 FUNCTION: May function as suppressor of malignant melanoma. It may exert its effects through interactions with the cytoskeleton.; . . unclassifiable (Anatomical System);breast;placenta;colon;blood;germinal center;bladder;skeletal muscle; prostate;superior cervical ganglion;tongue;placenta;kidney;atrioventricular node;skin;tonsil; 0.36462 0.12876 2.11299853 97.90634584 4051.23803 12.61130 AIM1L 3.33461351873646e-07 0.93072980963792 0.069269856900728 absent in melanoma 1-like . . . unclassifiable (Anatomical System);lung;placenta;testis;colon;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;tongue;placenta;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.30654 0.10478 . . 5023.32163 14.48092 AIM2 9.0084267551464e-08 0.0898438178587021 0.91015609205703 absent in melanoma 2 FUNCTION: Involved in innate immune response by recognizing cytosolic double-stranded DNA and inducing caspase-1-activating inflammasome formation in macrophages. Upon binding to DNA is thought to undergo oligomerization and to associate with PYCARD initiating the recruitment of caspase-1 precusrsor and processing of interleukin-1 beta and interleukin-18. Detects cytosolic dsDNA of viral and bacterial origin in a non-sequence-specific manner. Can also trigger PYCARD-dependent, caspase-1-independent cell death that involves caspase-8 (By similarity). Tumor suppressor which may act by repressing NF-kappa-B transcriptional activity. {ECO:0000250, ECO:0000269|PubMed:16432157, ECO:0000269|PubMed:17726700, ECO:0000269|PubMed:19158675, ECO:0000269|PubMed:19158676, ECO:0000269|PubMed:19158679, ECO:0000269|PubMed:20566831}.; . TISSUE SPECIFICITY: Expressed in spleen, small intestine, peripheral blood leukocytes, and testis. {ECO:0000269|PubMed:9242382}.; . . 0.06930 0.09293 0.038710339 56.92380278 212.89479 3.15020 AIMP1 0.000209309476432127 0.732345090578587 0.267445599944981 aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 FUNCTION: Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1- mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7. {ECO:0000269|PubMed:10358004, ECO:0000269|PubMed:11157763, ECO:0000269|PubMed:11306575, ECO:0000269|PubMed:11818442, ECO:0000269|PubMed:12237313, ECO:0000269|PubMed:19362550}.; DISEASE: Leukodystrophy, hypomyelinating, 3 (HLD3) [MIM:260600]: A severe autosomal recessive hypomyelinating leukodystrophy characterized by early infantile onset of global developmental delay, lack of development, lack of speech acquisition, and peripheral spasticity associated with decreased myelination in the central nervous system. {ECO:0000269|PubMed:21092922}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;lung;cornea;adrenal gland;placenta;duodenum;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skin; 0.09329 0.15941 0.084621747 60.31493277 1133.26676 6.42379 AIMP1P1 . . . aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 pseudogene 1 . . . . . . . . . . . AIMP1P2 . . . aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 pseudogene 2 . . . . . . . . . . . AIMP2 0.00146308205811016 0.672818479143005 0.325718438798885 aminoacyl tRNA synthetase complex-interacting multifunctional protein 2 FUNCTION: Required for assembly and stability of the aminoacyl- tRNA synthase complex. Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down- regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor. {ECO:0000269|PubMed:16135753}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; testis - interstitial;superior cervical ganglion;heart;testis - seminiferous tubule;liver;testis;skeletal muscle; . . -0.356299879 29.31115829 235.8663 3.31806 AIP 0.673915913889954 0.325081824417714 0.0010022616923327 aryl hydrocarbon receptor interacting protein FUNCTION: May play a positive role in AHR-mediated (aromatic hydrocarbon receptor) signaling, possibly by influencing its receptivity for ligand and/or its nuclear targeting.; DISEASE: ACTH-secreting pituitary adenoma (ASPA) [MIM:219090]: A pituitary adenoma resulting in excessive production of adrenocorticotropic hormone. This leads to hypersecretion of cortisol by the adrenal glands and ACTH-dependent Cushing syndrome. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes. {ECO:0000269|PubMed:17360484}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Prolactin-secreting pituitary adenoma (PSPA) [MIM:600634]: Most common type of hormonally active pituitary adenoma. {ECO:0000269|PubMed:16728643, ECO:0000305|PubMed:17244780}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Higher levels seen in the heart, placenta and skeletal muscle. Not expressed in the liver.; myocardium;lymphoreticular;medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;tongue;blood;lens;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus;cerebellum; superior cervical ganglion;liver;atrioventricular node;trigeminal ganglion;cerebellum; 0.51148 0.13318 -0.135838822 43.77211607 39.115 1.15958 AIPL1 0.000113410667383106 0.825339756683428 0.174546832649189 aryl hydrocarbon receptor interacting protein-like 1 FUNCTION: May be important in protein trafficking and/or protein folding and stabilization.; . TISSUE SPECIFICITY: Highly expressed in retina. Specifically localized to the developing photoreceptor layer and within the photoreceptors of the adult retina. {ECO:0000269|PubMed:12374762}.; unclassifiable (Anatomical System);optic nerve;macula lutea;visual apparatus;fovea centralis;choroid;pineal gland;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;appendix;pons;atrioventricular node;trigeminal ganglion; 0.13854 0.10568 1.644346333 96.16654871 2355.28685 8.99684 AIRE 1.55048193646196e-06 0.850485217192876 0.149513232325188 autoimmune regulator FUNCTION: Transcriptional regulator that binds to DNA as a dimer or as a tetramer, but not as a monomer. Binds to G-doublets in an A/T-rich environment; the preferred motif is a tandem repeat of 5'-. ATTGGTTA-3' combined with a 5'-TTATTA-3' box. Binds to nucleosomes (By similarity). Binds to chromatin and interacts selectively with histone H3 that is not methylated at 'Lys-4', not phosphorylated at 'Thr-3' and not methylated at 'Arg-2'. Functions as a sensor of histone H3 modifications that are important for the epigenetic regulation of gene expression. Functions as a transcriptional activator and promotes the expression of otherwise tissue-specific self-antigens in the thymus, which is important for self tolerance and the avoidance of autoimmune reactions. {ECO:0000250, ECO:0000269|PubMed:11274163, ECO:0000269|PubMed:18292755}.; DISEASE: Autoimmune polyendocrine syndrome 1, with or without reversible metaphyseal dysplasia (APS1) [MIM:240300]: A rare disease characterized by the combination of chronic mucocutaneous candidiasis, hypoparathyroidism and Addison disease. Symptoms of mucocutaneous candidiasis manifest first, followed by hypotension or fatigue occurring as a result of Addison disease. APS1 is associated with other autoimmune disorders including diabetes mellitus, vitiligo, alopecia, hepatitis, pernicious anemia and primary hypothyroidism. {ECO:0000269|PubMed:10677297, ECO:0000269|PubMed:11275943, ECO:0000269|PubMed:11524731, ECO:0000269|PubMed:11524733, ECO:0000269|PubMed:11600535, ECO:0000269|PubMed:11836330, ECO:0000269|PubMed:12050215, ECO:0000269|PubMed:12173302, ECO:0000269|PubMed:12625412, ECO:0000269|PubMed:15712268, ECO:0000269|PubMed:9398839, ECO:0000269|PubMed:9888391}. Note=The disease is caused by mutations affecting the gene represented in this entry. Most of the mutations alter the nucleus-cytoplasm distribution of AIRE and disturb its association with nuclear dots and cytoplasmic filaments. Most of the mutations also decrease transactivation of the protein. The HSR domain is responsible for the homomultimerization activity of AIRE. All the missense mutations of the HSR and the SAND domains decrease this activity, but those in other domains do not. The AIRE protein is present in soluble high-molecular-weight complexes. Mutations in the HSR domain and deletion of PHD zinc fingers disturb the formation of these complexes (PubMed:14974083). {ECO:0000269|PubMed:14974083}.; TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in thymus (medullary epithelial cells and monocyte-dendritic cells), pancreas, adrenal cortex and testis. Expressed at lower level in the spleen, fetal liver and lymph nodes. Isoform 2 and isoform 3 seem to be less frequently expressed than isoform 1, if at all.; unclassifiable (Anatomical System); ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19564 0.59275 -0.571310997 19.01391838 216.35286 3.17827 AIRN . . . antisense of IGF2R non-protein coding RNA . . . . . . . . . . . AIS1 . . . autoimmune susceptibility 1 . . . . . . . . . . . AIS2 . . . autoimmune susceptibility 2 . . . . . . . . . . . AIS3 . . . autoimmune susceptibility 3 (vitiligo specific) . . . . . . . . . . . AJAP1 0.977592766896285 0.0223860316323285 2.12014713866153e-05 adherens junctions associated protein 1 FUNCTION: Plays a role in cell adhesion and cell migration. {ECO:0000269|PubMed:16410724, ECO:0000269|PubMed:17267690}.; . TISSUE SPECIFICITY: Expressed in uterus and pancreas (at protein level). {ECO:0000269|PubMed:14595118}.; . . 0.15431 0.12412 0.418953042 77.06416608 3783.30469 12.04609 AJUBA 0.83340004755109 0.166570625315053 2.93271338563766e-05 ajuba LIM protein FUNCTION: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, mitosis, cell-cell adhesion, cell differentiation, proliferation and migration. Contributes to the linking and/or strengthening of epithelia cell- cell junctions in part by linking adhesive receptors to the actin cytoskeleton. May be involved in signal transduction from cell adhesion sites to the nucleus. Plays an important role in regulation of the kinase activity of AURKA for mitotic commitment. Also a component of the IL-1 signaling pathway modulating IL-1- induced NFKB1 activation by influencing the assembly and activity of the PRKCZ-SQSTM1-TRAF6 multiprotein signaling complex. Functions as an HDAC-dependent corepressor for a subset of GFI1 target genes. Acts as a transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent repression of E-cadherin transcription. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Positively regulates microRNA (miRNA)-mediated gene silencing. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. {ECO:0000269|PubMed:12417594, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:15870274, ECO:0000269|PubMed:16413547, ECO:0000269|PubMed:17909014, ECO:0000269|PubMed:18805794, ECO:0000269|PubMed:20303269, ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:22286099}.; . . lymphoreticular;smooth muscle;ovary;colon;skin;uterus;prostate;whole body;cerebral cortex;endometrium;synovium;larynx;thyroid;testis;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;stomach; fetal liver;lung;placenta;skin; 0.11613 0.11895 . . 120.81183 2.39516 AK1 0.654809128002237 0.339455084388276 0.00573578760948633 adenylate kinase 1 FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:23416111}.; DISEASE: Hemolytic anemia due to adenylate kinase deficiency (HAAKD) [MIM:612631]: A disease characterized by hemolytic anemia and undetectable erythrocyte adenylate kinase activity. {ECO:0000269|PubMed:12649162, ECO:0000269|PubMed:2542324, ECO:0000269|PubMed:9432020}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;medulla oblongata;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;thyroid;amniotic fluid;bladder;brain;heart;cartilage;tongue;pineal body;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach; superior cervical ganglion;heart;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15139 0.64321 -0.137658575 43.57159707 346.85629 3.94964 AK2 0.00556558560437493 0.897844628098363 0.0965897862972619 adenylate kinase 2 FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis. {ECO:0000255|HAMAP- Rule:MF_03168, ECO:0000269|PubMed:19043416}.; DISEASE: Reticular dysgenesis (RDYS) [MIM:267500]: Most severe form of inborn severe combined immunodeficiencies (SCID) and is characterized by absence of granulocytes and almost complete deficiency of lymphocytes in peripheral blood, hypoplasia of the thymus and secondary lymphoid organs, and lack of innate and adaptive humoral and cellular immune functions, leading to fatal septicemia within days after birth. In bone marrow of individuals with reticular dysgenesis, myeloid differentiation is blocked at the promyelocytic stage, whereas erythro- and megakaryocytic maturation is generally normal. In addition, affected newborns have bilateral sensorineural deafness. Defects may be due to its absence in leukocytes and inner ear, in which its absence can not be compensated by AK1. {ECO:0000269|PubMed:19043416, ECO:0000269|PubMed:19043417}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Present in most tissues. Present at high level in heart, liver and kidney, and at low level in brain, skeletal muscle and skin. Present in thrombocytes but not in erythrocytes, which lack mitochondria. Present in all nucleated cell populations from blood, while AK1 is mostly absent. In spleen and lymph nodes, mononuclear cells lack AK1, whereas AK2 is readily detectable. These results indicate that leukocytes may be susceptible to defects caused by the lack of AK2, as they do not express AK1 in sufficient amounts to compensate for the AK2 functional deficits (at protein level). {ECO:0000269|PubMed:19043417}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;bone marrow; 0.49696 0.35793 0.21689899 68.12927577 82.5936 1.93027 AK2P1 . . . adenylate kinase 2 pseudogene 1 . . . . . . . . . . . AK2P2 . . . adenylate kinase 2 pseudogene 2 . . . . . . . . . . . AK3 5.63208744451123e-05 0.453086226352386 0.546857452773169 adenylate kinase 3 FUNCTION: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities. {ECO:0000255|HAMAP-Rule:MF_03169, ECO:0000269|PubMed:11485571}.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and liver, moderately expressed in pancreas and kidney, and weakly expressed in placenta, brain and lung. {ECO:0000269|PubMed:11485571}.; ovary;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;artery;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;alveolus;liver;spleen;head and neck;kidney;stomach;aorta; atrioventricular node; 0.41612 0.13186 0.062575634 58.74026893 98.88177 2.15085 AK3P2 . . . adenylate kinase 3 pseudogene 2 . . . . . . . . . . . AK3P3 . . . adenylate kinase 3 pseudogene 3 . . . . . . . . . . . AK3P4 . . . adenylate kinase 3 pseudogene 4 . . . . . . . . . . . AK3P5 . . . adenylate kinase 3 pseudogene 5 . . . . . . . . . . . AK3P6 . . . adenylate kinase 3 pseudogene 6 . . . . . . . . . . . AK4 0.23613336099277 0.731312412995822 0.0325542260114077 adenylate kinase 4 FUNCTION: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Efficiently phosphorylates AMP and dAMP using ATP as phosphate donor, but phosphorylates only AMP when using GTP as phosphate donor. Also displays broad nucleoside diphosphate kinase activity. {ECO:0000255|HAMAP-Rule:MF_03170, ECO:0000269|PubMed:19073142, ECO:0000269|PubMed:19766732, ECO:0000269|PubMed:23416111}.; . TISSUE SPECIFICITY: Highly expressed in kidney, moderately expressed in heart and liver and weakly expressed in brain. {ECO:0000269|PubMed:11485571}.; medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;breast;lung;macula lutea;hippocampus;liver;spleen;kidney;stomach; kidney;atrioventricular node; 0.41612 0.13186 -0.075159878 47.78839349 1542.50701 7.28675 AK4P1 . . . adenylate kinase 4 pseudogene 1 . . . . . . . . . . . AK4P2 . . . adenylate kinase 4 pseudogene 2 . . . . . . . . . . . AK4P3 . . . adenylate kinase 4 pseudogene 3 . . . . . . 0.20245 . . . . AK4P4 . . . adenylate kinase 4 pseudogene 4 . . . . . . . . . . . AK4P5 . . . adenylate kinase 4 pseudogene 5 . . . . . . . . . . . AK4P6 . . . adenylate kinase 4 pseudogene 6 . . . . . . . . . . . AK5 0.139499449417184 0.86032794450418 0.000172606078635292 adenylate kinase 5 FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. Also displays broad nucleoside diphosphate kinase activity. {ECO:0000269|PubMed:19647735, ECO:0000269|PubMed:23416111}.; . TISSUE SPECIFICITY: Brain specific. {ECO:0000269|PubMed:10215863}.; unclassifiable (Anatomical System);amygdala;cartilage;hypothalamus;colon;fovea centralis;bone marrow;lung;frontal lobe;cornea;endometrium;bone;macula lutea;hippocampus;testis;kidney;mammary gland;brain;stomach; whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;hypothalamus;temporal lobe;pons;caudate nucleus;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.28987 0.10360 -0.800872469 12.33191791 81.00916 1.90506 AK6 . . . adenylate kinase 6 FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. AMP and dAMP are the preferred substrates, but CMP and dCMP are also good substrates. IMP is phosphorylated to a much lesser extent. All nucleoside triphosphates ATP, GTP, UTP, CTP, dATP, dCTP, dGTP, and TTP are accepted as phosphate donors. CTP is the best phosphate donor, followed by UTP, ATP, GTP and dCTP. May have a role in nuclear energy homeostasis. Has also ATPase activity. May be involved in regulation of Cajal body (CB) formation. {ECO:0000269|PubMed:15630091}.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, chorionic villi and the central nervous system. {ECO:0000269|PubMed:16079131}.; . . 0.95557 . . . . . AK6P1 . . . adenylate kinase 6 pseudogene 1 . . . . . . . . . . . AK6P2 . . . adenylate kinase 6 pseudogene 2 . . . . . . . . . . . AK7 9.78990970793468e-09 0.995611036926429 0.00438895328366091 adenylate kinase 7 FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. Also displays broad nucleoside diphosphate kinase activity. Involved in maintaining ciliary structure and function. {ECO:0000269|PubMed:21080915, ECO:0000269|PubMed:23416111}.; . . unclassifiable (Anatomical System);breast;lung;bone;colon;mammary gland;skeletal muscle; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;testis;ciliary ganglion;pons;trigeminal ganglion;skin; 0.16616 0.15992 -0.24061166 36.28214201 2018.63033 8.26835 AK8 1.50735950671094e-07 0.384769812141322 0.615230037122727 adenylate kinase 8 FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. Also displays broad nucleoside diphosphate kinase activity. {ECO:0000269|PubMed:21080915, ECO:0000269|PubMed:23416111}.; . . unclassifiable (Anatomical System);medulla oblongata;ovary;cartilage;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;optic nerve;lung;cerebral cortex;bone;macula lutea;testis;spleen;mammary gland;brain; . 0.13923 0.15909 0.068033485 59.0351498 497.62894 4.58369 AK9 7.09554971028093e-12 0.956487530817953 0.0435124691749514 adenylate kinase 9 FUNCTION: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has both nucleoside monophosphate and diphosphate kinase activities. Catalyzes the phosphorylation of AMP, dAMP, CMP and dCMP with ATP as phosphate donor and of CMP with GTP as phosphate donor. Also catalyzes the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and TTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donor. Shows substrate preference of CDP > UDP > ADP > GDP > TDP. {ECO:0000269|PubMed:23416111}.; . . . . 0.20706 0.07112 1.723305156 96.49681529 9574.37609 21.15233 AKAP1 0.561768712699788 0.438208969371885 2.23179283275697e-05 A-kinase anchoring protein 1 FUNCTION: Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane.; . TISSUE SPECIFICITY: Isoform 1 is detected in thymus, prostate, testis, ovary, colon and small intestine (PubMed:8769136). Isoform 2 is highly expressed in testis and detected at much lower levels in kidney, pancreas, liver, lung and brain (PubMed:7499250). {ECO:0000269|PubMed:7499250, ECO:0000269|PubMed:8769136}.; myocardium;smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;hypopharynx;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; amygdala;testis - interstitial;superior cervical ganglion;pons;atrioventricular node;fetal thyroid;skeletal muscle;testis - seminiferous tubule;thyroid;liver;prefrontal cortex;testis;trigeminal ganglion; 0.97835 0.13449 0.185543665 66.2715263 1120.33396 6.39078 AKAP2 0.0665164408552921 0.933458592071005 2.49670737031876e-05 A-kinase anchoring protein 2 FUNCTION: Binds to regulatory subunit (RII) of protein kinase A. May be involved in establishing polarity in signaling systems or in integrating PKA-RII isoforms with downstream effectors to capture, amplify and focus diffuse, trans-cellular signals carried by cAMP (By similarity). {ECO:0000250}.; . . breast; . . 0.12902 1.455030861 95.16395376 . . AKAP3 0.0263329788992228 0.961417124456473 0.0122498966443042 A-kinase anchoring protein 3 FUNCTION: May function as a regulator of both motility- and head- associated functions such as capacitation and the acrosome reaction.; . TISSUE SPECIFICITY: Testis specific; only expressed in spermatids.; unclassifiable (Anatomical System);ovary;testis;retina; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.16208 0.10597 1.207001692 93.02901628 2237.90986 8.72692 AKAP4 0.984377750020385 0.015613522200801 8.72777881438281e-06 A-kinase anchoring protein 4 FUNCTION: Major structural component of sperm fibrous sheath. Plays a role in sperm motility. {ECO:0000269|PubMed:9822690}.; . TISSUE SPECIFICITY: Testis specific; only expressed in round spermatids. {ECO:0000269|PubMed:9514854}.; unclassifiable (Anatomical System);testis; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.11292 0.12717 0.665103516 84.6131163 52.95631 1.44422 AKAP5 0.8411295400862 0.155897518177656 0.00297294173614461 A-kinase anchoring protein 5 FUNCTION: May anchor the PKA protein to cytoskeletal and/or organelle-associated proteins, targeting the signal carried by cAMP to specific intracellular effectors. Association with to the beta2-adrenergic receptor (beta2-AR) not only regulates beta2-AR signaling pathway, but also the activation by PKA by switching off the beta2-AR signaling cascade.; . TISSUE SPECIFICITY: Predominantly in the cerebral cortex and the postsynaptic densities of the forebrain, and to a lesser extent in adrenal medulla, lung and anterior pituitary.; unclassifiable (Anatomical System);brain; superior cervical ganglion; 0.09171 . 0.72761005 86.08162302 147.82319 2.64873 AKAP6 0.999936668135418 6.33318645814325e-05 8.73907781650573e-16 A-kinase anchoring protein 6 FUNCTION: Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the nuclear membrane or sarcoplasmic reticulum. May act as an adapter for assembling multiprotein complexes.; . TISSUE SPECIFICITY: Highly expressed in cardiac and skeletal muscle, followed by brain.; ovary;sympathetic chain;colon;parathyroid;choroid;fovea centralis;retina;prostate;whole body;optic nerve;frontal lobe;testis;brain;spinal ganglion;unclassifiable (Anatomical System);amygdala;heart;hypothalamus;lens;skeletal muscle;placenta;macula lutea;liver;alveolus;cerebellum; dorsal root ganglion;superior cervical ganglion;medulla oblongata;testis - interstitial;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;pituitary; 0.66471 0.12721 0.297442613 71.65015334 4015.93624 12.54696 AKAP7 0.00159877310631196 0.885201944678711 0.113199282214977 A-kinase anchoring protein 7 FUNCTION: Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium. {ECO:0000269|PubMed:10613906, ECO:0000269|PubMed:17244820, ECO:0000269|PubMed:9545239}.; . TISSUE SPECIFICITY: Expressed in brain, heart, lung, pancreas and skeletal muscle. {ECO:0000269|PubMed:9545239}.; unclassifiable (Anatomical System);heart;islets of Langerhans;colon;skin;skeletal muscle;uterus;prostate;lung;nasopharynx;placenta;trabecular meshwork;bone;hippocampus;liver;testis;spleen;kidney;brain;thymus; dorsal root ganglion;superior cervical ganglion;fetal brain;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17495 0.09911 1.640710091 96.13116301 2538.17507 9.40495 AKAP8 0.982554657107455 0.0174448734648389 4.69427706484145e-07 A-kinase anchoring protein 8 FUNCTION: Anchoring protein that mediates the subcellular compartmentation of cAMP-dependent protein kinase (PKA type II).; . TISSUE SPECIFICITY: Highly expressed in heart, liver, skeletal muscle, kidney and pancreas.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;alveolus;liver;head and neck;cervix;kidney;stomach;cerebellum; testis - seminiferous tubule;testis;pons;atrioventricular node;skeletal muscle; 0.11133 0.27115 0.497836815 79.65911772 217.34993 3.18705 AKAP8L 0.542386261243836 0.457587657694202 2.60810619617936e-05 A-kinase anchoring protein 8 like FUNCTION: Could play a role in constitutive transport element (CTE)-mediated gene expression. Does not seem to be implicated in the binding of regulatory subunit II of PKA. May be involved in nuclear envelope breakdown and chromatin condensation. May regulate the initiation phase of DNA replication when associated with TMPO-beta.; . TISSUE SPECIFICITY: Expressed in the brain cortex (at protein level). {ECO:0000269|PubMed:16391387}.; . . 0.09475 . -0.336073593 30.55555556 45.99788 1.30586 AKAP8P1 . . . A-kinase anchoring protein 8 pseudogene 1 . . . . . . . . . . . AKAP9 2.29354530903585e-05 0.99997706454691 4.2108628737105e-21 A-kinase anchoring protein 9 FUNCTION: Scaffolding protein that assembles several protein kinases and phosphatases on the centrosome and Golgi apparatus. Required to maintain the integrity of the Golgi apparatus (PubMed:10202149, PubMed:15047863). Recruited to the Golgi apparatus by GM130/GOLGA2 and is required for microtubule nucleation at the cis-side of the Golgi apparatusGM130/GOLGA2. {ECO:0000269|PubMed:10202149, ECO:0000269|PubMed:15047863, ECO:0000269|PubMed:19242490}.; DISEASE: Long QT syndrome 11 (LQT11) [MIM:611820]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. {ECO:0000269|PubMed:18093912}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed (PubMed:10202149). Isoform 4: Highly expressed in skeletal muscle and in pancreas (PubMed:9482789). {ECO:0000269|PubMed:10202149, ECO:0000269|PubMed:9482789}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.14649 0.11060 0.223857359 68.44774711 6014.5693 16.20152 AKAP10 0.932283430642292 0.0677160053808583 5.63976849503227e-07 A-kinase anchoring protein 10 FUNCTION: Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A and anchors them to the mitochondria or the plasma membrane. Although the physiological relevance between PKA and AKAPS with mitochondria is not fully understood, one idea is that BAD, a proapoptotic member, is phosphorylated and inactivated by mitochondria-anchored PKA. It cannot be excluded too that it may facilitate PKA as well as G protein signal transduction, by acting as an adapter for assembling multiprotein complexes. With its RGS domain, it could lead to the interaction to G-alpha proteins, providing a link between the signaling machinery and the downstream kinase (By similarity). {ECO:0000250}.; DISEASE: Sudden cardiac death (SCD) [MIM:115080]: Unexpected rapid death due to cardiovascular collapse in a short time period, generally within one hour of initial symptoms. It is usually caused by the worsening of existing heart diseases. The sudden onset of symptoms, such as chest pain and cardiac arrhythmias, particularly ventricular tachycardia, can lead to the loss of consciousness and cardiac arrest followed by biological death. {ECO:0000269|PubMed:17485678}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Increased susceptibility to sudden cardiac death may be conferred by AKAP10 variants that are associated with markers of low vagus nerve sensitivity, e.g. fast basal heart rate and low heart rate variability.; . ovary;colon;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;cerebellum cortex;islets of Langerhans;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;prefrontal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.45227 0.13055 7.61E-05 53.98089172 5105.66198 14.65898 AKAP11 0.896372711854258 0.103627274210046 1.39356955022328e-08 A-kinase anchoring protein 11 FUNCTION: Binds to type II regulatory subunits of protein kinase A and anchors/targets them.; . TISSUE SPECIFICITY: Expressed in heart, brain, lung, liver, kidney, testis and ovary. Weakly expressed in skeletal muscle, pancreas and spleen.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;amygdala;heart;cartilage;pharynx;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.21312 0.08419 1.44587039 95.09907997 931.34938 5.92007 AKAP12 0.37250182178499 0.627478647069248 1.95311457620226e-05 A-kinase anchoring protein 12 FUNCTION: Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC).; . TISSUE SPECIFICITY: Expressed in endothelial cells, cultured fibroblasts and osteosarcoma, but not in platelets, leukocytes, monocytic cell lines or peripherical blood cells.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;bladder;brain;gall bladder;amygdala;heart;cartilage;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;amnion;head and neck;kidney;stomach; testis - interstitial;testis; 0.40676 0.11841 0.914832296 89.54942203 3581.87772 11.57786 AKAP13 0.849566020351285 0.15043397964871 4.29315475360792e-15 A-kinase anchoring protein 13 FUNCTION: Anchors cAMP-dependent protein kinase (PKA) and acts as an adapter protein to selectively couple G alpha-13 and Rho. Augments gene activation by the estrogen receptor in an element- specific and ligand-dependent manner. Activates estrogen receptor beta by a p38 MAPK-dependent pathway. Stimulates exchange activity on Rho proteins in vitro, but not on CDC42, Ras or Rac and may bind calcium ions. {ECO:0000269|PubMed:11546812, ECO:0000269|PubMed:11579095, ECO:0000269|PubMed:9627117, ECO:0000269|PubMed:9891067}.; . TISSUE SPECIFICITY: Expressed as a 5.3 kb transcript in hematopoietic cells, skeletal muscle, lung, heart, estrogen- responsive reproductive tissues, including breast ductal epithelium. Also found in testis and breast cancer cell lines. Predominantly expressed as a 10 kb transcript in the heart and at lower levels in the lung, placenta, kidney, pancreas, skeletal muscle and liver. Transcripts of between 6-9 kb are also expressed in myeloid and lymphoid lineages, a variety of epithelial tissues, and in skeletal muscle. {ECO:0000269|PubMed:11546812, ECO:0000269|PubMed:9627117, ECO:0000269|PubMed:9891067}.; lymphoreticular;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;optic nerve;oesophagus;endometrium;synovium;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;uterus;superior cervical ganglion;ciliary ganglion;atrioventricular node;skin;skeletal muscle; 0.22240 0.22007 1.988827491 97.64095305 3944.37006 12.42106 AKAP14 0.633383828487056 0.359688540676821 0.00692763083612305 A-kinase anchoring protein 14 FUNCTION: Binds to type II regulatory subunits of protein kinase A and anchors/targets them.; . TISSUE SPECIFICITY: Present in cilia (at protein level). Expressed in tissues containing axoneme-based organelles (cilia and/or flagella): trachea and testis. Highly expressed in airway cilia. {ECO:0000269|PubMed:12475942}.; unclassifiable (Anatomical System);uterus;lung;heart;testis;skin; ciliary ganglion;atrioventricular node; 0.05279 0.08574 0.080983847 59.76055674 19.28263 0.66429 AKAP17A 0.713632077782215 0.285693946357147 0.00067397586063831 A-kinase anchoring protein 17A FUNCTION: Splice factor regulating alternative splice site selection for certain mRNA precursors. Mediates regulation of pre- mRNA splicing in a PKA-dependent manner. {ECO:0000269|PubMed:16982639, ECO:0000269|PubMed:19840947}.; . TISSUE SPECIFICITY: Widely expressed. Found in heart, brain, lung, liver, skeletal muscle, kidney and pancreas. Expressed in activated B-cells and placenta. Expressed in all cell lines tested including Jurkat-TAg, U-937 and HEK293 cells. {ECO:0000269|PubMed:19840947}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;synovium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;thymus; uterus corpus;superior cervical ganglion;testis;globus pallidus;white blood cells; 0.17104 0.12783 -0.632009432 16.78461901 303.14223 3.71045 AKAP17BP . . . A-kinase anchoring protein 17B, pseudogene . . . . . . . . . . . AKIP1 1.85693228183286e-05 0.265853082267251 0.73412834840993 A-kinase interacting protein 1 FUNCTION: Enhances NF-kappa-B transcriptional activity by regulating the nuclear localization of the NF-kappa-B subunit RELA and promoting the phosphorylation of RELA by PRKACA. Regulates the effect of the cAMP-dependent protein kinase signaling pathway on the NF-kappa-B activation cascade. {ECO:0000269|PubMed:18178962, ECO:0000269|PubMed:20562110}.; . TISSUE SPECIFICITY: Expressed at high levels in adult heart and at lower levels in brain, testis, ovary and skeletal muscle. Up- regulated in some breast cancer cell lines. Isoform 1 and isoform 3 are expressed in fetal brain. {ECO:0000269|PubMed:12527432, ECO:0000269|PubMed:15630084}.; lymphoreticular;ovary;parathyroid;skin;uterus;prostate;whole body;endometrium;gum;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;liver;cervix;kidney;stomach; . 0.03648 0.06430 1.060147109 91.46614768 910.85343 5.87002 AKIRIN1 0.672015819577841 0.323084902052453 0.00489927836970611 akirin 1 . . TISSUE SPECIFICITY: Widely expressed with the highest expression in heart, liver, placenta and peripheral blood leukocytes. {ECO:0000269|PubMed:18066067}.; . . 0.43663 0.11262 . . 14.61541 0.52676 AKIRIN1P1 . . . akirin 1 pseudogene 1 . . . . . . . . . . . AKIRIN1P2 . . . akirin 1 pseudogene 2 . . . . . . . . . . . AKIRIN2 0.975340569110996 0.0246325792381138 2.68516508897593e-05 akirin 2 FUNCTION: Required for the innate immune response. Downstream effector of the Toll-like receptor (TLR), TNF and IL-1 beta signaling pathways leading to the production of IL-6. Forms a complex with YWHAB that acts to repress transcription of DUSP1 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed with the highest expression in peripheral blood leukocytes. {ECO:0000269|PubMed:18066067}.; medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;lung;mesenchyma;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;aorta;thymus; amygdala;whole brain;subthalamic nucleus;testis;globus pallidus;ciliary ganglion;cingulate cortex; 0.88131 0.11809 . . 10.09876 0.36849 AKIRIN2P1 . . . akirin 2 pseudogene 1 . . . . . . . . . . . AKNA 0.0285257400281318 0.971473491174711 7.68797157285425e-07 AT-hook transcription factor FUNCTION: Transcription factor that specifically activates the expression of the CD40 receptor and its ligand CD40L/CD154, two cell surface molecules on lymphocytes that are critical for antigen-dependent-B-cell development. Binds to A/T-rich promoters. {ECO:0000269|PubMed:11268217}.; . TISSUE SPECIFICITY: Predominantly expressed by lymphoid tissues. Highly expressed in the spleen, lymph nodes and peripheral blood leukocytes, expressed at lower level in the thymus. Mainly expressed by germinal center B-lymphocytes, a stage in which receptor and ligand interactions are crucial for B-lymphocyte maturation. Expressed by B- and T-lymphocytes, Natural killer cells and CD1a(+)CD14(-) but not CD1a(-)CD14(+) dendritic cells. Weakly or not expressed in fetal liver and in adult bone marrow. {ECO:0000269|PubMed:11268217}.; ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;spleen;kidney;stomach;thymus; fetal liver;superior cervical ganglion;liver;white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle;thymus; 0.06340 0.08240 0.378330486 75.51899033 4847.69941 14.15107 AKNAD1 8.20527848932304e-19 0.0038846652007004 0.9961153347993 AKNA domain containing 1 . . . unclassifiable (Anatomical System);lung;testis; . 0.07859 . 0.828538765 88.1104034 925.80457 5.90967 AKR1A1 0.000107486413477255 0.81633774144861 0.183554772137913 aldo-keto reductase family 1, member A1 (aldehyde reductase) FUNCTION: Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. In vitro substrates include succinic semialdehyde, 4- nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D- glucuronic acid. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN). {ECO:0000269|PubMed:10510318, ECO:0000269|PubMed:11306097, ECO:0000269|PubMed:18276838}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney, salivary gland and liver. Detected in trachea, stomach, brain, lung, prostate, placenta, mammary gland, small intestine and lung. {ECO:0000269|PubMed:10510318, ECO:0000269|PubMed:11306097}.; lymphoreticular;smooth muscle;ovary;skin;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;synovium;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;kidney;stomach; liver;kidney;trigeminal ganglion; 0.27052 0.22307 0.308721233 72.59966973 288.28032 3.63544 AKR1B1 1.07346253038348e-05 0.572420816439669 0.427568448935027 aldo-keto reductase family 1, member B1 (aldose reductase) FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.; . TISSUE SPECIFICITY: Highly expressed in embryonic epithelial cells (EUE) in response to osmotic stress. {ECO:0000269|PubMed:8435445}.; myocardium;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;vein;skin;uterus;prostate;frontal lobe;endometrium;bone;iris;testis;amniotic fluid;germinal center;spinal ganglion;brain;pineal gland;bladder;unclassifiable (Anatomical System);heart;cerebellum cortex;tongue;islets of Langerhans;hypothalamus;pineal body;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;epididymis;trabecular meshwork;placenta;visual apparatus;amnion;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; olfactory bulb;adrenal gland;placenta;adrenal cortex; 0.31505 0.48066 -0.181750739 40.15687662 84.99179 1.96399 AKR1B1P1 . . . aldehyde reductase family 1, member B1 pseudogene 1 . . . . . . . . . . . AKR1B1P2 . . . aldo-keto reductase family 1, member B1 pseudogene 2 . . . . . . . . . . . AKR1B1P3 . . . aldo-keto reductase family 1, member B1 pseudogene 3 . . . . . . . . . . . AKR1B1P4 . . . aldo-keto reductase family 1, member B1 pseudogene 4 . . . . . . . . . . . AKR1B1P5 . . . aldo-keto reductase family 1, member B1 pseudogene 5 . . . . . . . . . . . AKR1B1P6 . . . aldo-keto reductase family 1, member B1 pseudogene 6 . . . . . . . . . . . AKR1B1P7 . . . aldo-keto reductase family 1, member B1 pseudogene 7 . . . . . . . . . . . AKR1B1P8 . . . aldo-keto reductase family 1, member B1 pseudogene 8 . . . . . . . . . . . AKR1B10 1.2180120737993e-05 0.600013778495659 0.399974041383603 aldo-keto reductase family 1, member B10 (aldose reductase) FUNCTION: Acts as all-trans-retinaldehyde reductase. Can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). May be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. {ECO:0000269|PubMed:18087047}.; . TISSUE SPECIFICITY: Found in many tissues. Highly expressed in small intestine, colon and adrenal gland.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;larynx;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;skeletal muscle;bile duct;breast;lung;epididymis;placenta;visual apparatus;liver;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;trachea;tongue;trigeminal ganglion; 0.15356 0.31956 0.374860183 75.43052607 369.36028 4.06189 AKR1B10P1 . . . aldo-keto reductase family 1, member B10 pseudogene 1 . . . . . . . . . . . AKR1B10P2 . . . aldo-keto reductase family 1, member B10 pseudogene 2 . . . . . . . . . . . AKR1B15 4.52992010086282e-15 0.000884906554171526 0.999115093445824 aldo-keto reductase family 1, member B15 FUNCTION: Isoform 1: Mainly acts as a reductive enzyme that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. Has a strong selectivity towards NADP(H) (PubMed:25577493). {ECO:0000269|PubMed:21276782, ECO:0000269|PubMed:25577493}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at highest levels in steroid-sensitive tissues, such as placenta, testis and adipose tissue. {ECO:0000269|PubMed:25577493}.; . . . . 0.022122107 55.69120075 197.55124 3.03882 AKR1C1 8.39898077933769e-06 0.756946589301907 0.243045011717313 aldo-keto reductase family 1, member C1 FUNCTION: Converts progesterone to its inactive form, 20-alpha- dihydroxyprogesterone (20-alpha-OHP). In the liver and intestine, may have a role in the transport of bile. May have a role in monitoring the intrahepatic bile acid concentration. Has a low bile-binding ability. May play a role in myelin formation. {ECO:0000269|PubMed:11013348, ECO:0000269|PubMed:8573067}.; . TISSUE SPECIFICITY: Expressed in all tissues tested including liver, prostate, testis, adrenal gland, brain, uterus, mammary gland and keratinocytes. Highest levels found in liver, mammary gland and brain. {ECO:0000269|PubMed:11013348}.; . . 0.02947 . -0.091746757 46.91554612 139.8212 2.57941 AKR1C2 0.00410317193583082 0.960236616488911 0.035660211575258 aldo-keto reductase family 1, member C2 FUNCTION: Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha- DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol). Has a high bile-binding ability. {ECO:0000269|PubMed:15929998, ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338, ECO:0000269|PubMed:8573067}.; . TISSUE SPECIFICITY: Expressed in fetal testes. Expressed in fetal and adult adrenal glands. {ECO:0000269|PubMed:21802064}.; . . 0.06658 . -0.093566408 46.7386176 216.82023 3.18289 AKR1C3 1.07139398635711e-11 0.0439469252686508 0.956053074720635 aldo-keto reductase family 1, member C3 FUNCTION: Catalyzes the conversion of aldehydes and ketones to alcohols. Catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ) and the oxidation of 9-alpha,11-beta- PGF2 to PGD2. Functions as a bi-directional 3-alpha-, 17-beta- and 20-alpha HSD. Can interconvert active androgens, estrogens and progestins with their cognate inactive metabolites. Preferentially transforms androstenedione (4-dione) to testosterone.; . TISSUE SPECIFICITY: Expressed in many tissues including adrenal gland, brain, kidney, liver, lung, mammary gland, placenta, small intestine, colon, spleen, prostate and testis. The dominant HSD in prostate and mammary gland. In the prostate, higher levels in epithelial cells than in stromal cells. In the brain, expressed in medulla, spinal cord, frontotemporal lobes, thalamus, subthalamic nuclei and amygdala. Weaker expression in the hippocampus, substantia nigra and caudate. {ECO:0000269|PubMed:10557352, ECO:0000269|PubMed:10622721, ECO:0000269|PubMed:11165022, ECO:0000269|PubMed:7650035, ECO:0000269|PubMed:9415401, ECO:0000269|PubMed:9927279}.; . . 0.15764 0.30697 0.775339069 87.13729653 798.09356 5.56765 AKR1C4 1.68467759451019e-10 0.0596426322628655 0.940357367568667 aldo-keto reductase family 1, member C4 FUNCTION: Catalyzes the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5-alpha- androstan-3-alpha,17-beta-diol (3-alpha-diol). Also has some 20- alpha-hydroxysteroid dehydrogenase activity. The biotransformation of the pesticide chlordecone (kepone) to its corresponding alcohol leads to increased biliary excretion of the pesticide and concomitant reduction of its neurotoxicity since bile is the major excretory route.; DISEASE: 46,XY sex reversal 8 (SRXY8) [MIM:614279]: A disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females. {ECO:0000269|PubMed:21802064}. Note=The gene represented in this entry may act as a disease modifier. A splicing mutation resulting in loss of AKR1C4 exon 2 has been found in affected individuals carrying a causative mutation in AKR1C2 (PubMed:21802064). These patients manifest a more severe disease phenotype than individuals only carrying mutations in AKR1C2. {ECO:0000269|PubMed:21802064}.; TISSUE SPECIFICITY: Liver specific. {ECO:0000269|PubMed:11158055, ECO:0000269|PubMed:7650035}.; unclassifiable (Anatomical System);thyroid;liver;stomach; subthalamic nucleus;superior cervical ganglion;liver; 0.17952 0.15444 -0.001743238 53.85114414 526.03991 4.68046 AKR1C5P . . . aldo-keto reductase family 1, member C5, pseudogene . . . . . . . . . . . AKR1C6P . . . aldo-keto reductase family 1, member C6, pseudogene . . . . . . . . . . . AKR1C7P . . . aldo-keto reductase family 1, member C7, pseudogene . . . . . . . . . . . AKR1C8P . . . aldo-keto reductase family 1, member C8, pseudogene . . . . . 0.10616 . . . . . AKR1D1 5.69259631264517e-08 0.236779989836913 0.763219953237123 aldo-keto reductase family 1, member D1 FUNCTION: Efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites. The bile acid intermediates 7- alpha,12-alpha-dihydroxy-4-cholesten-3-one and 7-alpha-hydroxy-4- cholesten-3-one can also act as substrates. {ECO:0000269|PubMed:11342103}.; . TISSUE SPECIFICITY: Highly expressed in liver. Expressed in testis and weakly in colon. {ECO:0000269|PubMed:11342103}.; unclassifiable (Anatomical System);liver;spleen; fetal liver;superior cervical ganglion;liver;appendix;ciliary ganglion;atrioventricular node;skeletal muscle; 0.14370 0.16811 -0.648365105 16.35999056 21.07566 0.71321 AKR1D1P1 . . . aldo-keto reductase family 1, member D1 pseudogene 1 . . . . . . . . . . . AKR1E2 6.35197354907988e-06 0.699990493694644 0.300003154331807 aldo-keto reductase family 1, member E2 FUNCTION: Catalyzes the NADPH-dependent reduction of 1,5-anhydro- D-fructose (AF) to 1,5-anhydro-D-glucitol. Can also catalyze the reduction of various aldehydes and quinones (By similarity). Has low NADPH-dependent reductase activity towards 9,10- phenanthrenequinone (in vitro). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:12604216}.; unclassifiable (Anatomical System);lung;cartilage;thyroid;liver;testis;blood;head and neck;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12644 0.10234 0.619191319 83.36282142 1412.71403 7.02493 AKR7A2 3.55874178311221e-06 0.353766594942708 0.646229846315509 aldo-keto reductase family 7, member A2 FUNCTION: Catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. May have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad substrate specificity. Has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2- nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). Can reduce 1,2-naphthoquinone and 9,10-phenanthrenequinone (in vitro). Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen. {ECO:0000269|PubMed:17591773, ECO:0000269|PubMed:9576847}.; . TISSUE SPECIFICITY: Detected in brain, liver, small intestine and testis, and at lower levels in heart, prostate, skeletal muscle and spleen. Detected in kidney proximal and distal tubules, endothelial cells lining the Bowman's capsules and some cysts. Detected at low levels in lung and pancreas (at protein level). Widely expressed. {ECO:0000269|PubMed:10510318, ECO:0000269|PubMed:9576847}.; ovary;colon;parathyroid;choroid;vein;skin;bone marrow;uterus;prostate;optic nerve;ganglion;frontal lobe;endometrium;bone;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;heart;liver;kidney;trigeminal ganglion;skeletal muscle; 0.14182 . 0.709197509 85.68058504 1410.0677 7.01375 AKR7A2P1 . . . aldo-keto reductase family 7, member A2 pseudogene 1 . . . . . . . . . . . AKR7A3 6.13891503863645e-10 0.0347922742387986 0.96520772514731 aldo-keto reductase family 7, member A3 (aflatoxin aldehyde reductase) FUNCTION: Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen. {ECO:0000269|PubMed:18416522}.; . TISSUE SPECIFICITY: Expressed in colon, kidney, liver, pancreas, adenocarcinoma and endometrium. {ECO:0000269|PubMed:12879023, ECO:0000269|PubMed:18416522}.; unclassifiable (Anatomical System);islets of Langerhans;liver;stomach; pancreas;superior cervical ganglion;heart;liver;kidney;skeletal muscle; 0.17750 0.11388 1.888739204 97.30478887 4825.65232 14.07663 AKR7L 0.00438244228415804 0.668108807915716 0.327508749800126 aldo-keto reductase family 7-like (gene/pseudogene) FUNCTION: Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Mainly expressed in uterus. {ECO:0000269|PubMed:12879023}.; . . . . . . . . AKT1 0.980206587064648 0.0197927722590899 6.40676262475334e-07 v-akt murine thymoma viral oncogene homolog 1 FUNCTION: AKT1 is one of 3 closely related serine/threonine- protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)- response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development. Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr- 117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation. Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity. Phosphorylation of BAD stimulates its pro- apoptotic activity. Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53.; DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:17611497}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Note=Genetic variations in AKT1 may play a role in susceptibility to ovarian cancer.; DISEASE: Proteus syndrome (PROTEUSS) [MIM:176920]: A highly variable, severe disorder of asymmetric and disproportionate overgrowth of body parts, connective tissue nevi, epidermal nevi, dysregulated adipose tissue, and vascular malformations. Many features of Proteus syndrome overlap with other overgrowth syndromes. {ECO:0000269|PubMed:21793738}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cowden syndrome 6 (CWS6) [MIM:615109]: A form of Cowden syndrome, a hamartomatous polyposis syndrome with age-related penetrance. Cowden syndrome is characterized by hamartomatous lesions affecting derivatives of ectodermal, mesodermal and endodermal layers, macrocephaly, facial trichilemmomas (benign tumors of the hair follicle infundibulum), acral keratoses, papillomatous papules, and elevated risk for development of several types of malignancy, particularly breast carcinoma in women and thyroid carcinoma in both men and women. Colon cancer and renal cell carcinoma have also been reported. Hamartomas can be found in virtually every organ, but most commonly in the skin, gastrointestinal tract, breast and thyroid. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in prostate cancer and levels increase from the normal to the malignant state (at protein level). Expressed in all human cell types so far analyzed. The Tyr-176 phosphorylated form shows a significant increase in expression in breast cancers during the progressive stages i.e. normal to hyperplasia (ADH), ductal carcinoma in situ (DCIS), invasive ductal carcinoma (IDC) and lymph node metastatic (LNMM) stages. {ECO:0000269|PubMed:1718748, ECO:0000269|PubMed:17932490, ECO:0000269|PubMed:20333297}.; myocardium;lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; heart;liver; 0.99568 0.99960 -1.001120478 8.321538099 12.57291 0.45861 AKT1S1 0.476648977204292 0.500096977982027 0.0232540448136805 AKT1 substrate 1 (proline rich) FUNCTION: Subunit of mTORC1, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, AKT1S1 negatively regulates mTOR activity in a manner that is dependent on its phosphorylation state and binding to 14-3-3 proteins. Inhibits RHEB-GTP-dependent mTORC1 activation. Substrate for AKT1 phosphorylation, but can also be activated by AKT1-independent mechanisms. May also play a role in nerve growth factor-mediated neuroprotection. {ECO:0000269|PubMed:16174443, ECO:0000269|PubMed:17277771, ECO:0000269|PubMed:17386266}.; . TISSUE SPECIFICITY: Widely expressed with highest levels of expression in liver and heart. Expressed at higher levels in cancer cell lines (e.g. A-549 and HeLa) than in normal cell lines (e.g. HEK293). {ECO:0000269|PubMed:12524439, ECO:0000269|PubMed:16174443}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.23370 0.21441 -0.203796826 38.81811748 39.77427 1.17206 AKT2 0.997816206855922 0.00218372210271295 7.10413655318677e-08 v-akt murine thymoma viral oncogene homolog 2 FUNCTION: AKT2 is one of 3 closely related serine/threonine- protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)- response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development.; DISEASE: Note=Defects in AKT2 are a cause of susceptibility to breast cancer (BC). AKT2 promotes metastasis of tumor cells without affecting the latency of tumor development. With AKT3, plays also a pivotal role in the biology of glioblastoma.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:15166380, ECO:0000269|PubMed:19164855}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hypoinsulinemic hypoglycemia with hemihypertrophy (HIHGHH) [MIM:240900]: A disorder characterized by hypoglycemia, low insulin levels, low serum levels of ketone bodies and branched-chain amino acids, left-sided hemihypertrophy, neonatal macrosomia, reduced consciousness and hypoglycemic seizures. {ECO:0000269|PubMed:21979934}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all cell types so far analyzed.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus;cerebellum; subthalamic nucleus;superior cervical ganglion;thyroid;temporal lobe;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.91994 0.55644 -0.648365105 16.35999056 17.52078 0.61489 AKT3 0.99958539864029 0.000414600121510425 1.23819945657922e-09 v-akt murine thymoma viral oncogene homolog 3 FUNCTION: AKT3 is one of 3 closely related serine/threonine- protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase- dependent apoptosis. {ECO:0000269|PubMed:18524868, ECO:0000269|PubMed:21191416}.; DISEASE: Note=AKT3 is a key modulator of several tumors like melanoma, glioma and ovarian cancer. Active AKT3 increases progressively during melanoma tumor progression with highest levels present in advanced-stage metastatic melanomas. Promotes melanoma tumorigenesis by decreasing apoptosis. Plays a key role in the genesis of ovarian cancers through modulation of G2/M phase transition. With AKT2, plays a pivotal role in the biology of glioblastoma.; DISEASE: Megalencephaly-polymicrogyria-polydactyly-hydrocephalus syndrome 2 (MPPH2) [MIM:615937]: A syndrome characterized by megalencephaly, hydrocephalus, and polymicrogyria; polydactyly may also be seen. There is considerable phenotypic similarity between this disorder and the megalencephaly-capillary malformation syndrome. {ECO:0000269|PubMed:22500628, ECO:0000269|PubMed:22729223, ECO:0000269|PubMed:22729224}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In adult tissues, it is highly expressed in brain, lung and kidney, but weakly in heart, testis and liver. In fetal tissues, it is highly expressed in heart, liver and brain and not at all in kidney.; ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;lung;adrenal gland;placenta;hippocampus;visual apparatus;liver;spleen;kidney;mammary gland;stomach; amygdala;dorsal root ganglion;occipital lobe;superior cervical ganglion;medulla oblongata;pons;atrioventricular node;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.51738 0.24974 -0.251530012 35.42108988 6.85051 0.25446 AKT3-IT1 . . . AKT3 intronic transcript 1 . . . . . . . . . . . AKTIP 0.788012645511726 0.211705677758882 0.000281676729392234 AKT interacting protein FUNCTION: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Regulates apoptosis by enhancing phosphorylation and activation of AKT1. Increases release of TNFSF6 via the AKT1/GSK3B/NFATC1 signaling cascade. {ECO:0000269|PubMed:14749367, ECO:0000269|PubMed:18799622}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;thymus; whole brain;amygdala;thalamus;occipital lobe;subthalamic nucleus;hypothalamus;spinal cord;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.58839 0.17756 0.014844891 54.94810097 12.56256 0.45812 ALAD 0.062950260359489 0.933785175165961 0.00326456447455025 aminolevulinate dehydratase FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen. {ECO:0000269|PubMed:11032836, ECO:0000269|PubMed:19812033}.; DISEASE: Acute hepatic porphyria (AHEPP) [MIM:612740]: A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. AHP is characterized by attacks of gastrointestinal disturbances, abdominal colic, paralyses and peripheral neuropathy. Most attacks are precipitated by drugs, alcohol, caloric deprivation, infections, or endocrine factors. {ECO:0000269|PubMed:10706561, ECO:0000269|PubMed:1309003, ECO:0000269|PubMed:1569184, ECO:0000269|PubMed:2063868}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;choroid;skin;retina;bone marrow;prostate;whole body;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;lung;placenta;hippocampus;liver;spleen;kidney;mammary gland;stomach; fetal liver;thalamus;superior cervical ganglion;olfactory bulb;adrenal gland;hypothalamus;caudate nucleus;parietal lobe; 0.11936 0.55928 -0.558357437 19.54470394 471.54569 4.49402 ALAS1 0.907956554078195 0.0920373324640849 6.11345772019149e-06 5'-aminolevulinate synthase 1 . . . lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;cerebellum; adrenal gland;liver;adrenal cortex;cerebellum; 0.39863 0.44944 -0.110153916 45.48832272 153.9661 2.71295 ALAS2 0.970654597578417 0.0293041279331119 4.12744884708566e-05 5'-aminolevulinate synthase 2 . DISEASE: Erythropoietic protoporphyria, X-linked dominant (XLDPT) [MIM:300752]: A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. XLDPT is characterized biochemically by a high proportion of zinc-protoporphyrin in erythrocytes, in which a mismatch between protoporphyrin production and the heme requirement of differentiating erythroid cells leads to overproduction of protoporphyrin in amounts sufficient to cause photosensitivity and liver disease. {ECO:0000269|PubMed:18760763}. Note=The disease is caused by mutations affecting the gene represented in this entry. Gain of function mutations in ALS2 are responsible for XLDPT, but they can also be a possible aggravating factor in congenital erythropoietic porphyria and other erythropoietic disorders caused by mutations in other genes (PubMed:21309041). {ECO:0000269|PubMed:21309041}.; TISSUE SPECIFICITY: Erythroid specific.; unclassifiable (Anatomical System);heart;cartilage;blood;skin;uterus;pancreas;whole body;lung;placenta;bone;visual apparatus;liver;spleen;spinal ganglion;brain; superior cervical ganglion;fetal liver;fetal lung;skeletal muscle;bone marrow; 0.80443 0.45327 0.130533008 63.35810333 33.4696 1.03212 ALB 0.985726825017932 0.0142731169898081 5.7992259452854e-08 albumin FUNCTION: Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. {ECO:0000269|PubMed:19021548}.; DISEASE: Hyperthyroxinemia, familial dysalbuminemic (FDAH) [MIM:615999]: A disorder characterized by abnormally elevated levels of total serum thyroxine (T4) in euthyroid patients. It is due to abnormal serum albumin that binds T4 with enhanced affinity. {ECO:0000269|PubMed:7852505, ECO:0000269|PubMed:8048949, ECO:0000269|PubMed:9329347, ECO:0000269|PubMed:9589637}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Analbuminemia (ANALBA) [MIM:616000]: A rare autosomal recessive disorder manifested by the presence of a very low amount of circulating serum albumin. Affected individuals manifest mild edema, hypotension, fatigue, and, occasionally, lower body lipodystrophy (mainly in adult females). The most common biochemical finding is hyperlipidemia, with a significant increase in the total and LDL cholesterol concentrations, but normal concentrations of HDL cholesterol and triglycerides. {ECO:0000269|PubMed:8134387}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma.; unclassifiable (Anatomical System);whole body;lung;bone;liver;spleen;gall bladder;skeletal muscle; fetal liver;superior cervical ganglion;pancreas;liver;fetal lung;kidney;pons;fetal thyroid; 0.84285 0.95809 -0.88906181 10.36801132 34.26072 1.04848 ALCAM 0.98833623820425 0.0116635871972854 1.74598464382267e-07 activated leukocyte cell adhesion molecule FUNCTION: Cell adhesion molecule that mediates both heterotypic cell-cell contacts via its interaction with CD6, as well as homotypic cell-cell contacts (PubMed:7760007, PubMed:15496415, PubMed:15048703, PubMed:16352806, PubMed:23169771, PubMed:24945728). Promotes T-cell activation and proliferation via its interactions with CD6 (PubMed:15048703, PubMed:16352806, PubMed:24945728). Contributes to the formation and maturation of the immunological synapse via its interactions with CD6 (PubMed:15294938, PubMed:16352806). Mediates homotypic interactions with cells that express ALCAM (PubMed:15496415, PubMed:16352806). Required for normal hematopoietic stem cell engraftment in the bone marrow (PubMed:24740813). Mediates attachment of dendritic cells onto endothelial cells via homotypic interaction (PubMed:23169771). Inhibits endothelial cell migration and promotes endothelial tube formation via homotypic interactions (PubMed:15496415, PubMed:23169771). Required for normal organization of the lymph vessel network. Required for normal hematopoietic stem cell engraftment in the bone marrow. Plays a role in hematopoiesis; required for normal numbers of hematopoietic stem cells in bone marrow. Promotes in vitro osteoblast proliferation and differentiation (By similarity). Promotes neurite extension, axon growth and axon guidance; axons grow preferentially on surfaces that contain ALCAM. Mediates outgrowth and pathfinding for retinal ganglion cell axons (By similarity). {ECO:0000250|UniProtKB:P42292, ECO:0000269|PubMed:15048703, ECO:0000269|PubMed:15294938, ECO:0000269|PubMed:15496415, ECO:0000269|PubMed:16352806, ECO:0000269|PubMed:24945728, ECO:0000269|PubMed:7760007}.; . TISSUE SPECIFICITY: Detected on hematopoietic stem cells derived from umbilical cord blood (PubMed:24740813). Detected on lymph vessel endothelial cells, skin and tonsil (PubMed:23169771). Detected on peripheral blood monocytes (PubMed:15048703). Detected on monocyte-derived dendritic cells (at protein level) (PubMed:16352806). Detected at low levels in spleen, placenta, liver (PubMed:9502422). Expressed by activated T-cells, B-cells, monocytes and thymic epithelial cells (PubMed:7760007). Isoform 1 and isoform 3 are detected in vein and artery endothelial cells, astrocytes, keratinocytes and artery smooth muscle cells (PubMed:15496415). Expressed by neurons in the brain. Restricted expression in tumor cell lines. Detected in highly metastasizing melanoma cell lines (PubMed:9502422). {ECO:0000269|PubMed:15048703, ECO:0000269|PubMed:24740813, ECO:0000269|PubMed:7760007, ECO:0000269|PubMed:9502422}.; smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;hypothalamus;spinal cord;ciliary ganglion;caudate nucleus;pons;trigeminal ganglion;parietal lobe; 0.73319 0.36495 0.198490371 67.30360934 1020.1348 6.14448 ALDH1A1 0.993850728751138 0.00614909125096185 1.79997899863214e-07 aldehyde dehydrogenase 1 family member A1 FUNCTION: Binds free retinal and cellular retinol-binding protein- bound retinal. Can convert/oxidize retinaldehyde to retinoic acid (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;salivary gland;developmental;intestine;colon;parathyroid;choroid;skin;uterus;prostate;whole body;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;bile duct;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; testis; 0.38428 0.38566 -0.53631094 20.53550366 92.19746 2.06498 ALDH1A2 0.516630055977224 0.48321210592044 0.000157838102336276 aldehyde dehydrogenase 1 family member A2 FUNCTION: Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently (By similarity). {ECO:0000250}.; . . colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;kidney;peripheral nerve; testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;skeletal muscle; 0.42269 0.21959 -0.446304853 24.33356924 3704.90825 11.86496 ALDH1A3 0.924100685142389 0.0758809068734942 1.84079841171702e-05 aldehyde dehydrogenase 1 family member A3 FUNCTION: Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Seems to be the key enzyme in the formation of an RA gradient along the dorso-ventral axis during the early eye development and also in the development of the olfactory system (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at low levels in many tissues and at higher levels in salivary gland, stomach, and kidney.; ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;atrium;whole body;synovium;gum;bone;thyroid;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;lymph node;heart;lacrimal gland;tongue;muscle;skeletal muscle;bile duct;breast;pancreas;pia mater;lung;nasopharynx;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; prostate;testis - interstitial;smooth muscle;lung;trachea; 0.25694 0.26772 -0.578583623 18.71903751 916.25719 5.88722 ALDH1B1 0.000426748675847598 0.647489097167952 0.352084154156201 aldehyde dehydrogenase 1 family member B1 FUNCTION: ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation.; . TISSUE SPECIFICITY: Liver, testis and to a lesser extent in brain.; . . 0.67359 0.45302 -0.044015879 50.44821892 7275.99437 18.36480 ALDH1L1 9.61783695417292e-06 0.999330570126497 0.000659812036549155 aldehyde dehydrogenase 1 family member L1 . . TISSUE SPECIFICITY: Highly expressed in liver, pancreas and kidney. {ECO:0000269|PubMed:20498374}.; medulla oblongata;ovary;colon;fovea centralis;choroid;retina;prostate;optic nerve;thyroid;bone;testis;spinal ganglion;bladder;brain;unclassifiable (Anatomical System);hypothalamus;adrenal cortex;lens;skeletal muscle;lung;nasopharynx;macula lutea;hippocampus;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;adipose tissue;liver;kidney;trigeminal ganglion; 0.13532 0.19904 -0.163564105 40.68176457 5265.95607 14.98933 ALDH1L1-AS1 . . . ALDH1L1 antisense RNA 1 . . . . . . . . . . . ALDH1L1-AS2 . . . ALDH1L1 antisense RNA 2 . . . . . . . . . . . ALDH1L2 3.50010213963042e-11 0.905866641972583 0.0941333579924163 aldehyde dehydrogenase 1 family member L2 . . TISSUE SPECIFICITY: Highly expressed in pancreas, heart, brain and skeletal muscle. {ECO:0000269|PubMed:20498374}.; unclassifiable (Anatomical System);uterus;heart;bone;visual apparatus;liver;testis;colon;skin; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.20443 0.10413 -1.082044518 7.242274121 222.73913 3.22701 ALDH2 1.73245219738394e-06 0.660113840771075 0.339884426776728 aldehyde dehydrogenase 2 family (mitochondrial) . . . ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;skeletal muscle;visual apparatus;liver;cervix;spleen;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; liver;kidney; 0.48585 0.66989 -0.844966979 11.1759849 516.20171 4.64731 ALDH3A1 1.32614029510281e-12 0.0129943681011167 0.987005631897557 aldehyde dehydrogenase 3 family member A1 FUNCTION: ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes.; . TISSUE SPECIFICITY: High levels in stomach, esophagus and lung; low level in the liver and kidney.; unclassifiable (Anatomical System);tongue;salivary gland;colon;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;lung;endometrium;macula lutea;visual apparatus;testis;head and neck;cervix;kidney;brain;stomach; superior cervical ganglion;lung;trachea;tongue;temporal lobe; 0.38989 . 0.113945049 62.14319415 3022.02935 10.43597 ALDH3A2 0.011288383677575 0.979949340904242 0.00876227541818334 aldehyde dehydrogenase 3 family member A2 FUNCTION: Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid. {ECO:0000269|PubMed:22633490}.; DISEASE: Sjoegren-Larsson syndrome (SLS) [MIM:270200]: An autosomal recessive neurocutaneous disorder characterized by a combination of severe mental retardation, spastic di- or tetraplegia and congenital ichthyosis. Ichthyosis is usually evident at birth with varying degrees of erythema and scaling, neurologic symptoms appear in the first or second year of life. Most patients have an IQ of less than 60. Additional clinical features include glistening white spots on the retina, seizures, short stature and speech defects. {ECO:0000269|PubMed:10577908, ECO:0000269|PubMed:10792573, ECO:0000269|PubMed:8528251, ECO:0000269|PubMed:9254849, ECO:0000269|PubMed:9829906}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;skin;retina;prostate;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;oesophagus;bone;pituitary gland;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;adrenal gland;adrenal cortex;kidney;atrioventricular node; 0.07195 0.33841 -0.111973265 45.35857514 85.62922 1.97378 ALDH3B1 3.93511223222023e-05 0.834235047155885 0.165725601721792 aldehyde dehydrogenase 3 family member B1 FUNCTION: Oxidizes medium and long chain saturated and unsaturated aldehydes. Metabolizes also benzaldehyde. Low activity towards acetaldehyde and 3,4-dihydroxyphenylacetaldehyde. May not metabolize short chain aldehydes. May use both NADP(+) and NAD(+) as cofactors. May have a protective role against the cytotoxicity induced by lipid peroxidation. {ECO:0000269|PubMed:17382292, ECO:0000269|PubMed:23721920}.; . TISSUE SPECIFICITY: Highest expression in kidney and lung.; unclassifiable (Anatomical System);ovary;heart;blood;parathyroid;skin;skeletal muscle;bone marrow;uterus;prostate;lung;thyroid;iris;mammary gland;brain; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.27759 0.10950 . . 171.87941 2.85929 ALDH3B2 0.000359298698542525 0.831772568761075 0.167868132540382 aldehyde dehydrogenase 3 family member B2 . . . unclassifiable (Anatomical System);heart;ovary;parathyroid;skin;skeletal muscle;uterus;breast;placenta;hypopharynx;head and neck;cervix;bladder;mammary gland; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;tongue;adrenal cortex;ciliary ganglion;atrioventricular node;skeletal muscle; 0.15065 0.12684 2.090866216 97.85326728 1208.69555 6.58564 ALDH4A1 0.000434043544234141 0.991527810228015 0.00803814622775046 aldehyde dehydrogenase 4 family member A1 FUNCTION: Irreversible conversion of delta-1-pyrroline-5- carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. {ECO:0000269|PubMed:22516612}.; . TISSUE SPECIFICITY: Highest expression is found in liver followed by skeletal muscle, kidney, heart, brain, placenta, lung and pancreas.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;bladder;brain;unclassifiable (Anatomical System);heart;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;cervix;kidney;stomach;thymus;cerebellum; amygdala;whole brain;dorsal root ganglion;prostate;fetal liver;superior cervical ganglion;prefrontal cortex;liver;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion; 0.72198 0.21304 0.207589927 67.52182118 1111.17701 6.37244 ALDH5A1 0.00290426169695016 0.984501555649417 0.0125941826536329 aldehyde dehydrogenase 5 family member A1 FUNCTION: Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA). {ECO:0000269|PubMed:19300440}.; . TISSUE SPECIFICITY: Brain, pancreas, heart, liver, skeletal muscle and kidney. Lower in placenta.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; whole brain;amygdala;medulla oblongata;superior cervical ganglion;occipital lobe;thalamus;hypothalamus;spinal cord;tumor;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;appendix;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.80822 0.21248 0.398725314 76.35645199 1777.9694 7.78507 ALDH6A1 1.62229467445935e-05 0.992502487465627 0.00748128958762895 aldehyde dehydrogenase 6 family member A1 FUNCTION: Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.; DISEASE: Methylmalonate semialdehyde dehydrogenase deficiency (MMSDHD) [MIM:614105]: A metabolic disorder characterized by elevated beta-alanine, 3-hydroxypropionic acid, and both isomers of 3-amino and 3-hydroxyisobutyric acids in urine organic acids. {ECO:0000269|PubMed:10947204}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);amygdala;lymph node;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;bile duct;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; whole brain;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;cerebellum peduncles;temporal lobe;atrioventricular node;caudate nucleus;pons;subthalamic nucleus;fetal liver;testis - seminiferous tubule;liver;prefrontal cortex;globus pallidus;kidney;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.20099 0.21694 -0.402212257 26.7338995 42.69019 1.23859 ALDH7A1 1.95312955165253e-12 0.362501991453821 0.637498008544226 aldehyde dehydrogenase 7 family member A1 FUNCTION: Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism. {ECO:0000269|PubMed:16491085, ECO:0000269|PubMed:20207735}.; . TISSUE SPECIFICITY: Abundant in hepatoma cells and fetal cochlea, ovary, eye, heart, adrenal gland, liver and kidney. Low levels present in adult peripheral blood leukocytes and fetal brain, thymus, spleen, skeletal muscle, lung and tongue. {ECO:0000269|PubMed:8088832, ECO:0000269|PubMed:9417906}.; . . 0.46546 0.37812 -0.468351206 23.42533616 838.40275 5.67131 ALDH7A1P1 . . . aldehyde dehydrogenase 7 family member A1 pseudogene 1 . . . . . . . . . . . ALDH7A1P2 . . . aldehyde dehydrogenase 7 family member A1 pseudogene 2 . . . . . . . . . . . ALDH7A1P3 . . . aldehyde dehydrogenase 7 family member A1 pseudogene 3 . . . . . . . . . . . ALDH7A1P4 . . . aldehyde dehydrogenase 7 family member A1 pseudogene 4 . . . . . . . . . . . ALDH8A1 9.45631299959995e-06 0.544952328230336 0.455038215456665 aldehyde dehydrogenase 8 family member A1 FUNCTION: Converts 9-cis-retinal to 9-cis-retinoic acid. Has lower activity towards 13-cis-retinal. Has much lower activity towards all-trans-retinal. Has highest activity with benzaldehyde and decanal (in vitro). Has a preference for NAD, but shows considerable activity with NADP (in vitro). {ECO:0000269|PubMed:11007799}.; . TISSUE SPECIFICITY: Highly expressed in adult kidney and liver. Detected at lower levels in fetal liver and kidney. {ECO:0000269|PubMed:11007799}.; unclassifiable (Anatomical System);breast;lung;bone;liver;testis;spleen;kidney; fetal liver;liver;ciliary ganglion;kidney;trigeminal ganglion;skeletal muscle; 0.11265 0.10988 -0.574945567 18.90186365 68.72056 1.71673 ALDH9A1 1.29139214945887e-05 0.953462413214546 0.0465246728639597 aldehyde dehydrogenase 9 family member A1 FUNCTION: Converts gamma-trimethylaminobutyraldehyde into gamma- butyrobetaine. Catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction. {ECO:0000269|PubMed:10702312}.; . TISSUE SPECIFICITY: High expression in adult liver, skeletal muscle, and kidney. Low levels in heart, pancreas, lung and brain. Expressed in all regions of the brain. Expression levels are variable in the different brain areas, with the highest levels in the spinal cord and the lowest in the occipital pole. {ECO:0000269|PubMed:8645224}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;pancreas;lung;cornea;nasopharynx;placenta;duodenum;hypopharynx;amnion;head and neck;kidney;stomach;aorta;thymus; . 0.04374 0.24685 -0.021969881 52.14673272 462.50185 4.45730 ALDH16A1 1.35194745543971e-07 0.988008379494253 0.0119914853110012 aldehyde dehydrogenase 16 family member A1 . . . lymphoreticular;myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;spleen;cervix;kidney;mammary gland; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.08466 . 0.435344483 77.36494456 396.68922 4.18411 ALDH18A1 0.855933081745869 0.144066754056828 1.64197302552527e-07 aldehyde dehydrogenase 18 family member A1 FUNCTION: Bifunctional enzyme that converts glutamate to glutamate 5-semialdehyde, an intermediate in the biosynthesis of proline, ornithine and arginine. {ECO:0000269|PubMed:10037775, ECO:0000269|PubMed:11092761}.; DISEASE: Cutis laxa, autosomal recessive, 3A (ARCL3A) [MIM:219150]: A syndrome characterized by facial dysmorphism with a progeroid appearance, large and late-closing fontanel, cutis laxa, joint hyperlaxity, athetoid movements and hyperreflexia, pre- and postnatal growth retardation, intellectual deficit, developmental delay, and ophthalmologic abnormalities. {ECO:0000269|PubMed:11092761, ECO:0000269|PubMed:18478038}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.29356 0.46298 -0.93133804 9.613116301 880.66723 5.78002 ALDOA 0.0248344029134968 0.961826713136046 0.0133388839504577 aldolase, fructose-bisphosphate A FUNCTION: Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein (By similarity). {ECO:0000250}.; DISEASE: Glycogen storage disease 12 (GSD12) [MIM:611881]: A metabolic disorder associated with increased hepatic glycogen and hemolytic anemia. It may lead to myopathy with exercise intolerance and rhabdomyolysis. {ECO:0000269|PubMed:14615364, ECO:0000269|PubMed:14766013, ECO:0000269|PubMed:2825199, ECO:0000269|PubMed:8598869}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;salivary gland;intestine;colon;choroid;skin;retina;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;iris;pituitary gland;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;muscle;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; whole brain;medulla oblongata;subthalamic nucleus;thalamus;adipose tissue;heart;tongue;temporal lobe;pons;skeletal muscle;parietal lobe; 0.30328 0.57075 -0.580403979 18.58928993 48.98564 1.36718 ALDOAP1 . . . aldolase, fructose-bisphosphate A pseudogene 1 . . . . . . . . . . . ALDOAP2 . . . aldolase, fructose-bisphosphate A pseudogene 2 . . . . . . . . . . . ALDOB 0.000813754198789228 0.930904000505963 0.0682822452952474 aldolase, fructose-bisphosphate B . DISEASE: Hereditary fructose intolerance (HFI) [MIM:229600]: Autosomal recessive disease that results in an inability to metabolize fructose and related sugars. Complete exclusion of fructose results in dramatic recovery; however, if not treated properly, HFI subjects suffer episodes of hypoglycemia, general ill condition, and risk of death the remainder of life. {ECO:0000269|PubMed:10024431, ECO:0000269|PubMed:10970798, ECO:0000269|PubMed:12205126, ECO:0000269|PubMed:15532022, ECO:0000269|PubMed:15880727, ECO:0000269|PubMed:1967768, ECO:0000269|PubMed:2336380, ECO:0000269|PubMed:3383242, ECO:0000269|PubMed:8162030, ECO:0000269|PubMed:8299883}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.24770 0.72820 0.062575634 58.74026893 148.49314 2.65732 ALDOC 0.790720531816382 0.209007796598025 0.000271671585592644 aldolase, fructose-bisphosphate C . . . myocardium;smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;ganglion;frontal lobe;thyroid;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;cornea;placenta;hippocampus;head and neck;kidney;aorta;stomach;cerebellum; amygdala;whole brain;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.36112 0.43264 -0.580403979 18.58928993 77.82001 1.86019 ALG1 9.21962630765385e-10 0.280449123595343 0.719550875482694 ALG1, chitobiosyldiphosphodolichol beta-mannosyltransferase FUNCTION: Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER. {ECO:0000269|PubMed:10704531}.; DISEASE: Congenital disorder of glycosylation 1K (CDG1K) [MIM:608540]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:14709599, ECO:0000269|PubMed:14973778, ECO:0000269|PubMed:14973782}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.10757 0.19047 0.044168103 57.40740741 992.70946 6.07018 ALG1L 3.26303190374336e-09 0.0251865749419385 0.974813421795029 ALG1, chitobiosyldiphosphodolichol beta-mannosyltransferase-like FUNCTION: Putative glycosyltransferase. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;pineal body;colon;blood;fovea centralis;choroid;lens;skin;retina;bile duct;uterus;pancreas;prostate;optic nerve;lung;cochlea;bone;placenta;macula lutea;visual apparatus;kidney;stomach; . . . 1.660947774 96.24321774 2852.10956 10.10519 ALG1L2 . . . ALG1, chitobiosyldiphosphodolichol beta-mannosyltransferase-like 2 FUNCTION: Putative glycosyltransferase. {ECO:0000250}.; . . . . . . . . . . ALG1L3P . . . asparagine-linked glycosylation 1-like 3, pseudogene . . . . . . . . . . . ALG1L5P . . . asparagine-linked glycosylation 1-like 5, pseudogene . . . . . . . . . . . ALG1L6P . . . asparagine-linked glycosylation 1-like 6, pseudogene . . . . . . . . . . . ALG1L7P . . . asparagine-linked glycosylation 1-like 7, pseudogene . . . . . . . . . . . ALG1L8P . . . asparagine-linked glycosylation 1-like 8, pseudogene . . . . . . . . . . . ALG1L9P . . . asparagine-linked glycosylation 1-like 9, pseudogene . . . . . . . . . . . ALG1L10P . . . asparagine-linked glycosylation 1-like 10, pseudogene . . . . . . . . . . . ALG1L11P . . . asparagine-linked glycosylation 1-like 11, pseudogene . . . . . . . . . . . ALG1L12P . . . asparagine-linked glycosylation 1-like 12, pseudogene . . . . . . . . . . . ALG1L13P . . . asparagine-linked glycosylation 1-like 13, pseudogene . . . . . . . . . . . ALG1L14P . . . asparagine-linked glycosylation 1-like 14, pseudogene . . . . . . . . . . . ALG1L15P . . . asparagine-linked glycosylation 1-like 15, pseudogene . . . . . . . . . . . ALG2 0.0206692446248705 0.905297077088143 0.0740336782869867 ALG2, alpha-1,3/1,6-mannosyltransferase FUNCTION: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)- dolichol diphosphate. {ECO:0000269|PubMed:12684507}.; DISEASE: Congenital disorder of glycosylation 1I (CDG1I) [MIM:607906]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:12684507}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myasthenic syndrome, congenital, 14 (CMS14) [MIM:616228]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness. CMS14 is an autosomal recessive form characterized by onset of limb-girdle muscle weakness in early childhood. The disorder is slowly progressive, and some patients may become wheelchair-bound. {ECO:0000269|PubMed:23404334}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;bone;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;pharynx;blood;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;amnion;cervix;kidney;mammary gland;stomach;aorta; . 0.07226 0.20173 0.240763792 69.36777542 327.93694 3.84989 ALG3 4.17818824908735e-06 0.609402317703196 0.390593504108555 ALG3, alpha-1,3- mannosyltransferase FUNCTION: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc2-PP-Dol. {ECO:0000269|PubMed:10581255}.; DISEASE: Congenital disorder of glycosylation 1D (CDG1D) [MIM:601110]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:10581255, ECO:0000269|PubMed:15840742}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.22101 . -0.602450568 17.91106393 113.22864 2.31685 ALG3P1 . . . ALG3, alpha-1,3- mannosyltransferase pseudogene 1 . . . . . . . . . . . ALG5 0.00342997463732752 0.994513100008396 0.00205692535427681 ALG5, dolichyl-phosphate beta-glucosyltransferase . . TISSUE SPECIFICITY: Expressed in pancreas, placenta, liver, heart, brain, kidney, skeletal muscle, and lung.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;thyroid;amniotic fluid;germinal center;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;kidney;stomach;aorta;thymus; superior cervical ganglion;thyroid;atrioventricular node; 0.31928 0.15009 0.082802743 60.09082331 31.70282 0.99790 ALG6 0.0553676261725129 0.943817188308809 0.000815185518678409 ALG6, alpha-1,3-glucosyltransferase FUNCTION: Adds the first glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Man(9)GlcNAc(2)-PP-Dol.; DISEASE: Congenital disorder of glycosylation 1C (CDG1C) [MIM:603147]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:10359825, ECO:0000269|PubMed:10914684, ECO:0000269|PubMed:10924277, ECO:0000269|PubMed:11106564, ECO:0000269|PubMed:11134235, ECO:0000269|PubMed:12357336, ECO:0000269|PubMed:14517965}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);blood;lens;skeletal muscle;pancreas;lung;mesenchyma;nasopharynx;placenta;macula lutea;liver;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.30252 0.17567 0.286674996 71.49681529 271.59069 3.53105 ALG8 1.00988304374679e-05 0.985467795448836 0.0145221057207264 ALG8, alpha-1,3-glucosyltransferase FUNCTION: Adds the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol (By similarity). {ECO:0000250}.; DISEASE: Congenital disorder of glycosylation 1H (CDG1H) [MIM:608104]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:15235028}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;muscle;adrenal cortex;blood;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;nasopharynx;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.43977 0.17284 0.486911049 79.46449634 735.17295 5.37971 ALG9 0.00122530850136209 0.989859359975329 0.00891533152330868 ALG9, alpha-1,2-mannosyltransferase FUNCTION: Catalyzes the transfer of mannose from Dol-P-Man to lipid-linked oligosaccharides. {ECO:0000269|PubMed:15148656, ECO:0000269|PubMed:15945070}.; DISEASE: Congenital disorder of glycosylation 1L (CDG1L) [MIM:608776]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:15148656, ECO:0000269|PubMed:15945070}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed; with highest levels in heart, liver and pancreas. {ECO:0000269|PubMed:12030331}.; . . 0.50403 0.21568 0.507139401 80.10143902 2436.80849 9.17310 ALG9-IT1 . . . ALG9 intronic transcript 1 . . . . . . . . . . . ALG10 0.00574913500300478 0.901213072749266 0.0930377922477294 ALG10, alpha-1,2-glucosyltransferase FUNCTION: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.; . . unclassifiable (Anatomical System);medulla oblongata;lymph node;parathyroid;bone marrow;bile duct;lung;placenta;testis;spleen;cervix;kidney;brain; . 0.30191 . -0.291981272 33.20358575 46.28692 1.31006 ALG10B 0.000152772162093977 0.666148033022765 0.333699194815141 ALG10B, alpha-1,2-glucosyltransferase FUNCTION: Putative alpha-1,2-glucosyltransferase, which adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol. When coupled to KCNH2 may reduce KCNH2 sensitivity to classic proarrhythmic drug blockade, possibly by mediating glycosylation of KCNH2. {ECO:0000269|PubMed:14525949}.; . TISSUE SPECIFICITY: Highly expressed in heart, placenta, liver, kidney and pancreas. Weakly expressed in lung, skeletal muscle and brain. {ECO:0000269|PubMed:14525949}.; unclassifiable (Anatomical System);bile duct;medulla oblongata;lymph node;lung;testis;cervix;spleen;kidney;bone marrow; . 0.08813 0.08390 1.552504757 95.63576315 308.27683 3.73609 ALG11 0.000122134567519387 0.617425589975839 0.382452275456641 ALG11, alpha-1,2-mannosyltransferase FUNCTION: Mannosyltransferase involved in the last steps of the synthesis of Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum. Catalyzes the addition of the 4th and 5th mannose residues to the dolichol- linked oligosaccharide chain. {ECO:0000269|PubMed:20080937}.; DISEASE: Congenital disorder of glycosylation 1P (CDG1P) [MIM:613661]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:20080937, ECO:0000269|PubMed:22213132}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . . -0.490397599 22.50530786 116.2613 2.34534 ALG12 0.00788198257903734 0.97753033481469 0.0145876826062724 ALG12, alpha-1,6-mannosyltransferase FUNCTION: Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP- Man(7)GlcNAc(2)) required for protein glycosylation.; . TISSUE SPECIFICITY: Expressed in fibroblasts.; smooth muscle;ovary;developmental;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;muscle;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach;cerebellum; superior cervical ganglion; 0.09456 0.14056 -0.641086234 16.6784619 871.937 5.74904 ALG13 0.997582959543471 0.00241703673067939 3.72585000846799e-09 ALG13, UDP-N-acetylglucosaminyltransferase subunit FUNCTION: Isoform 1: Possible multifunctional enzyme with both glycosyltransferase and deubiquitinase activities.; DISEASE: Congenital disorder of glycosylation 1S (CDG1S) [MIM:300884]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:22492991}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);meninges;cartilage;ovary;heart;colon;parathyroid;skin;skeletal muscle;breast;pancreas;pia mater;lung;endometrium;placenta;hypopharynx;liver;testis;head and neck;spleen;dura mater;kidney;aorta;gall bladder; superior cervical ganglion;testis;pons; . . -0.999300439 8.368719038 48.1604 1.35199 ALG13-AS1 . . . ALG13 antisense RNA 1 . . . . . . . . . . . ALG14 0.000832660846870737 0.784168554913001 0.214998784240128 ALG14, UDP-N-acetylglucosaminyltransferase subunit FUNCTION: May be involved in protein N-glycosylation. May play a role in the second step of the dolichol-linked oligosaccharide pathway. May anchor the catalytic subunit ALG13 to the ER. {ECO:0000269|PubMed:16100110}.; DISEASE: Myasthenic syndrome, congenital, 15 (CMS15) [MIM:616227]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness. {ECO:0000269|PubMed:23404334}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.29417 0.10965 0.193034296 66.82000472 22.28957 0.74789 ALK 0.522362516846561 0.477637482729029 4.24410620352913e-10 anaplastic lymphoma receptor tyrosine kinase FUNCTION: Neuronal orphan receptor tyrosine kinase that is essentially and transiently expressed in specific regions of the central and peripheral nervous systems and plays an important role in the genesis and differentiation of the nervous system. Transduces signals from ligands at the cell surface, through specific activation of the mitogen-activated protein kinase (MAPK) pathway. Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif. Following activation by ligand, ALK induces tyrosine phosphorylation of CBL, FRS2, IRS1 and SHC1, as well as of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Acts as a receptor for ligands pleiotrophin (PTN), a secreted growth factor, and midkine (MDK), a PTN-related factor, thus participating in PTN and MDK signal transduction. PTN-binding induces MAPK pathway activation, which is important for the anti-apoptotic signaling of PTN and regulation of cell proliferation. MDK-binding induces phosphorylation of the ALK target insulin receptor substrate (IRS1), activates mitogen-activated protein kinases (MAPKs) and PI3-kinase, resulting also in cell proliferation induction. Drives NF-kappa-B activation, probably through IRS1 and the activation of the AKT serine/threonine kinase. Recruitment of IRS1 to activated ALK and the activation of NF-kappa-B are essential for the autocrine growth and survival signaling of MDK. {ECO:0000269|PubMed:11121404, ECO:0000269|PubMed:11278720, ECO:0000269|PubMed:11387242, ECO:0000269|PubMed:11809760, ECO:0000269|PubMed:12107166, ECO:0000269|PubMed:12122009, ECO:0000269|PubMed:15226403, ECO:0000269|PubMed:15908427, ECO:0000269|PubMed:16317043, ECO:0000269|PubMed:16878150, ECO:0000269|PubMed:17274988}.; DISEASE: Note=A chromosomal aberration involving ALK is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with NPM1. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated. The constitutively active fusion proteins are responsible for 5-10% of non-Hodgkin lymphomas.; DISEASE: Note=A chromosomal aberration involving ALK is associated with inflammatory myofibroblastic tumors (IMTs). Translocation t(2;11)(p23;p15) with CARS; translocation t(2;4)(p23;q21) with SEC31A.; DISEASE: Note=A chromosomal aberration involving ALK is associated with anaplastic large-cell lymphoma (ALCL). Translocation t(2;17)(p23;q25) with ALO17.; DISEASE: Neuroblastoma 3 (NBLST3) [MIM:613014]: A common neoplasm of early childhood arising from embryonic cells that form the primitive neural crest and give rise to the adrenal medulla and the sympathetic nervous system. {ECO:0000269|PubMed:18724359, ECO:0000269|PubMed:18923523, ECO:0000269|PubMed:18923525}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=The ALK signaling pathway plays an important role in glioblastoma, the most common malignant brain tumor of adults and one of the most lethal cancers. It regulates both glioblastoma migration and growth.; TISSUE SPECIFICITY: Expressed in brain and CNS. Also expressed in the small intestine and testis, but not in normal lymphoid cells. {ECO:0000269|PubMed:9174053}.; . . 0.21536 0.41881 -2.241974905 1.303373437 3502.62553 11.40875 ALKBH1 2.13146607160804e-05 0.720394036672879 0.279584648666405 alkB homolog 1, histone H2A dioxygenase FUNCTION: Dioxygenase that repairs alkylated single-stranded DNA and RNA containing 3-methylcytosine by oxidative demethylation. Requires molecular oxygen, alpha-ketoglutarate and iron. May have a role in placental trophoblast lineage differentiation (By similarity). Has DNA lyase activity and introduces double-stranded breaks at abasic sites. Cleaves both single-stranded DNA and double-stranded DNA at abasic sites, with the greatest activity towards double-stranded DNA with two abasic sites. DNA lyase activity does not require alpha-ketoglutarate and iron. {ECO:0000250, ECO:0000269|PubMed:18603530, ECO:0000269|PubMed:19959401}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17979886, ECO:0000269|PubMed:18603530}.; ovary;colon;choroid;fovea centralis;skin;retina;uterus;optic nerve;endometrium;synovium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lens;lung;adrenal gland;placenta;hippocampus;visual apparatus;macula lutea;cervix;kidney;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;cerebellum; 0.08569 0.08308 0.15257911 64.60839821 548.8598 4.76478 ALKBH2 0.000816686414241077 0.546277328011784 0.452905985573975 alkB homolog 2, alpha-ketoglutarate-dependent dioxygenase FUNCTION: Dioxygenase that repairs alkylated DNA and RNA containing 1-methyladenine and 3-methylcytosine by oxidative demethylation. Can also repair alkylated DNA containing 1- ethenoadenine (in vitro). Has strong preference for double- stranded DNA. Has low efficiency with single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron. {ECO:0000269|PubMed:12486230, ECO:0000269|PubMed:12594517, ECO:0000269|PubMed:16174769, ECO:0000269|PubMed:18432238, ECO:0000269|PubMed:18519673}.; . TISSUE SPECIFICITY: Detected in colon, small intestine, ovary, testis, prostate, skeletal muscle, heart, liver and urinary bladder. {ECO:0000269|PubMed:12486230, ECO:0000269|PubMed:16174769}.; ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;adrenal cortex;blood;lens;lung;placenta;macula lutea;liver;duodenum;spleen;kidney;mammary gland;stomach; superior cervical ganglion; 0.11009 0.14568 0.373041938 75.29488087 143.22523 2.60968 ALKBH3 2.55797163392014e-09 0.267539546711638 0.732460450730391 alkB homolog 3, alpha-ketoglutarate-dependent dioxygenase FUNCTION: Dioxygenase that repairs alkylated DNA containing 1- methyladenine (1meA) and 3-methylcytosine (3meC) by oxidative demethylation. Has a strong preference for single-stranded DNA. Able to process alkylated 3mC within double-stranded regions via its interaction with ASCC3, which promotes DNA unwinding to generate single-stranded substrate needed for ALKHB3. May also act on RNA. Requires molecular oxygen, alpha-ketoglutarate and iron. {ECO:0000269|PubMed:12486230, ECO:0000269|PubMed:12594517, ECO:0000269|PubMed:16174769, ECO:0000269|PubMed:22055184}.; . TISSUE SPECIFICITY: Ubiquitous. Detected in heart, pancreas, skeletal muscle, thymus, testis, ovary, spleen, prostate, small intestine, peripheral blood leukocytes, urinary bladder and colon. {ECO:0000269|PubMed:12486230, ECO:0000269|PubMed:16174769, ECO:0000269|PubMed:17979886}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;iris;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion; 0.14879 0.13882 0.396906589 76.30927105 1429.62423 7.05977 ALKBH3-AS1 . . . ALKBH3 antisense RNA 1 . . . . . . . . . . . ALKBH4 0.496783561003534 0.483076086657482 0.0201403523389839 alkB homolog 4, lysine demethylase FUNCTION: Dioxygenase that mediates demethylation of actin monomethylated at 'Lys-84' (K84me1), thereby acting as a regulator of actomyosin-processes. Demethylation of actin K84me1 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. May be involved in transcription regulation. {ECO:0000269|PubMed:21166655, ECO:0000269|PubMed:23673617}.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in pancreas, ovary and spleen. {ECO:0000269|PubMed:17979886}.; unclassifiable (Anatomical System);lymphoreticular;colon;skin;uterus;prostate;lung;bone;visual apparatus;iris;liver;testis;brain;stomach; cerebellum peduncles;atrioventricular node; 0.13412 0.10903 -0.071520315 48.34866714 451.92669 4.42151 ALKBH5 0.803934845862911 0.194958513517679 0.00110664061940999 alkB homolog 5, RNA demethylase FUNCTION: Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (PubMed:23177736, PubMed:24778178, PubMed:24616105, PubMed:24489119). Can also demethylate N(6)- methyladenosine in single-stranded DNA (in vitro) (PubMed:24616105). Requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:21264265, PubMed:23177736, PubMed:24778178, PubMed:24616105, PubMed:24489119). Demethylation of m6A mRNA affects mRNA processing and export (PubMed:23177736). Required for spermatogenesis (By similarity). {ECO:0000250|UniProtKB:Q3TSG4, ECO:0000269|PubMed:21264265, ECO:0000269|PubMed:23177736, ECO:0000269|PubMed:24489119, ECO:0000269|PubMed:24616105, ECO:0000269|PubMed:24778178}.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in lung, followed by testis, pancreas, spleen and ovary. {ECO:0000269|PubMed:17979886}.; ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;lung;adrenal gland;placenta;visual apparatus;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; medulla oblongata;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;testis;pons;kidney;skeletal muscle;cingulate cortex;cerebellum; 0.27176 . -0.405853867 26.23260203 7.97356 0.29301 ALKBH6 0.468934189734711 0.525627827138878 0.00543798312641128 alkB homolog 6 FUNCTION: Probable dioxygenase that requires molecular oxygen, alpha-ketoglutarate and iron. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in testis and pancreas. {ECO:0000269|PubMed:17979886}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;urinary;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; subthalamic nucleus;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; . 0.10629 . . 40.71267 1.19276 ALKBH7 2.76251331581087e-06 0.174818714326007 0.825178523160677 alkB homolog 7 FUNCTION: May function as protein hydroxylase; can catalyze auto- hydroxylation at Leu-110 (in vitro), but this activity may be due to the absence of the true substrate (PubMed:25122757). Required to induce programmed necrosis in response to DNA damage caused by cytotoxic alkylating agents. Acts by triggering the collapse of mitochondrial membrane potential and loss of mitochondrial function that leads to energy depletion and cell death (PubMed:23666923). ALKBH7-mediated necrosis is probably required to prevent the accumulation of cells with DNA damage (PubMed:23666923). Does not display DNA demethylase activity (PubMed:23666923). Involved in fatty acid metabolism (By similarity). {ECO:0000250|UniProtKB:Q9D6Z0, ECO:0000269|PubMed:23666923, ECO:0000269|PubMed:25122757}.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in pancreas, followed by spleen, prostate, ovary and placenta. {ECO:0000269|PubMed:17979886}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;testis;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;heart;islets of Langerhans;muscle;pharynx;blood;lens;breast;bile duct;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta; . 0.07289 0.09630 . . 190.02248 2.99125 ALKBH8 0.00282934969265518 0.802851908276447 0.194318742030897 alkB homolog 8, tRNA methyltransferase FUNCTION: Catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its methyltransferase domain (PubMed:20123966, PubMed:20308323). Catalyzes the last step in the formation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA (PubMed:20123966, PubMed:20308323). Has a preference for tRNA(Arg) and tRNA(Glu), and does not bind tRNA(Lys)(PubMed:20308323). Binds tRNA and catalyzes the iron and alpha-ketoglutarate dependent hydroxylation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its dioxygenase domain, giving rise to 5-(S)-methoxycarbonylhydroxymethyluridine; has a preference for tRNA(Gly) (PubMed:21285950). Required for normal survival after DNA damage (PubMed:20308323). May inhibit apoptosis and promote cell survival and angiogenesis (PubMed:19293182). {ECO:0000269|PubMed:19293182, ECO:0000269|PubMed:20123966, ECO:0000269|PubMed:20308323, ECO:0000269|PubMed:21285950}.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in spleen, followed by pancreas and lung. {ECO:0000269|PubMed:17979886}.; unclassifiable (Anatomical System);endometrium;islets of Langerhans;larynx;colon;head and neck;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.40729 . 1.243805243 93.41825902 565.52603 4.83046 ALLC 4.60880908473295e-11 0.0536706113989933 0.946329388554919 allantoicase FUNCTION: The function of this enzyme is unclear as allantoicase activity is not known to exist in mammals.; . . unclassifiable (Anatomical System);medulla oblongata;optic nerve;ovary;macula lutea;liver;testis;spleen;fovea centralis;choroid;kidney;lens;brain;retina; testis - interstitial;testis - seminiferous tubule;testis; 0.11041 0.14454 0.99945266 90.6935598 4645.70905 13.72246 ALMS1 3.0369217543731e-39 0.0119878859080824 0.988012114091918 ALMS1, centrosome and basal body associated protein FUNCTION: Involved in PCM1-dependent intracellular transport. Required, directly or indirectly, for the localization of NCAPD2 to the proximal ends of centrioles. Required for proper formation and/or maintenance of primary cilia (PC), microtubule-based structures that protrude from the surface of epithelial cells. {ECO:0000269|PubMed:17954613}.; DISEASE: Alstrom syndrome (ALMS) [MIM:203800]: A rare autosomal recessive disorder characterized by progressive cone-rod retinal dystrophy, neurosensory hearing loss, early childhood obesity and diabetes mellitus type 2. Dilated cardiomyopathy, acanthosis nigricans, male hypogonadism, hypothyroidism, developmental delay and hepatic dysfunction can also be associated with the syndrome. {ECO:0000269|PubMed:11941369, ECO:0000269|PubMed:11941370}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues tested including adipose and pancreas. Expressed by beta-cells of the islets in the pancreas (at protein level). {ECO:0000269|PubMed:11941369, ECO:0000269|PubMed:11941370}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;endometrium;larynx;thyroid;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;pons;atrioventricular node;skin;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.07684 0.11040 2.285276118 98.28379335 13445.86056 25.05995 ALMS1-IT1 . . . ALMS1 intronic transcript 1 . . . . . . . . . . . ALMS1P1 . . . ALMS1, centrosome and basal body associated protein pseudogene 1 . . . . . . . . . . . ALOX5 0.00164439332581691 0.998111454416308 0.000244152257874922 arachidonate 5-lipoxygenase FUNCTION: Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes. {ECO:0000269|PubMed:21233389}.; . . . . 0.58302 0.38768 -0.953385901 9.206180703 89.21156 2.03011 ALOX5AP 0.846184681895041 0.151084602714949 0.00273071539000965 arachidonate 5-lipoxygenase activating protein FUNCTION: Required for leukotriene biosynthesis by ALOX5 (5- lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes. {ECO:0000269|PubMed:2300173, ECO:0000269|PubMed:8440384}.; DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=Genetic variations in ALOX5AP may be associated with susceptibility to myocardial infarction. Involvement in myocardial infarction is however unclear: according to some authors (PubMed:14770184), a 4-SNP haplotype in ALOX5AP confers risk of myocardial infarction, while according to other (PubMed:17304054) ALOX5AP is not implicated in this condition. {ECO:0000269|PubMed:14770184, ECO:0000269|PubMed:17304054}.; . . . 0.17153 0.29071 -0.229483771 36.86010852 12.92759 0.47146 ALOX12 6.34478034828463e-10 0.633422192317588 0.366577807047934 arachidonate 12-lipoxygenase FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Mainly converts arachidonic acid to (12S)- hydroperoxyeicosatetraenoic acid/(12S)-HPETE but can also metabolize linoleic acid. Has a dual activity since it also converts leukotriene A4/LTA4 into both the bioactive lipoxin A4/LXA4 and lipoxin B4/LXB4. Through the production of specific bioactive lipids like (12S)-HPETE it regulates different biological processes including platelet activation. It also probably positively regulates angiogenesis through regulation of the expression of the vascular endothelial growth factor. Plays a role in apoptotic process, promoting the survival of vascular smooth muscle cells for instance. May also play a role in the control of cell migration and proliferation. {ECO:0000269|PubMed:16638750, ECO:0000269|PubMed:22237009, ECO:0000269|PubMed:23578768, ECO:0000269|PubMed:8250832, ECO:0000269|PubMed:9751607}.; DISEASE: Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the esophagus. The most common types are esophageal squamous cell carcinoma and adenocarcinoma. Cancer of the esophagus remains a devastating disease because it is usually not detected until it has progressed to an advanced incurable stage. {ECO:0000269|PubMed:17460548}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry. Gln at position 261 may confer interindividual susceptibility to esophageal cancer (PubMed:17460548). {ECO:0000269|PubMed:17460548}.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:17151091}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry. Gln at position 261 may confer interindividual susceptibility to colorectal cancer (PubMed:17460548). {ECO:0000269|PubMed:17460548}.; TISSUE SPECIFICITY: Expressed in vascular smooth muscle cells. {ECO:0000269|PubMed:23578768}.; unclassifiable (Anatomical System);lung;ovary;epididymis;colon;skeletal muscle; superior cervical ganglion;tongue; 0.23951 0.24283 0.801024817 87.65628686 1985.54853 8.21208 ALOX12-AS1 . . . ALOX12 antisense RNA 1 . . . . . . . . . . . ALOX12B 0.173314447563156 0.826570904208607 0.000114648228236992 arachidonate 12-lipoxygenase, 12R type FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Mainly converts arachidonic acid to (12R)- hydroperoxyeicosatetraenoic acid/(12R)-HPETE and minor stereoisomers. In the skin, acts upstream of ALOXE3 on the lineolate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. May also play a role in the regulation of the expression of airway mucins. {ECO:0000269|PubMed:21558561, ECO:0000269|PubMed:22441738, ECO:0000269|PubMed:9618483}.; . TISSUE SPECIFICITY: Expressed in B-cells, hair follicles, foreskin keratinocytes and adult skin. Also expressed in psoriatic tissue. {ECO:0000269|PubMed:9618483}.; unclassifiable (Anatomical System);hypopharynx;head and neck;germinal center;brain;skin; superior cervical ganglion;subthalamic nucleus;tongue;globus pallidus; 0.20676 . -0.619039275 17.39797122 141.88222 2.59997 ALOX12P1 . . . arachidonate 12-lipoxygenase pseudogene 1 . . . . . . . . . . . ALOX12P2 . . . arachidonate 12-lipoxygenase pseudogene 2 . . . . . 0.09427 . . . . . ALOX15 3.60054517501269e-19 0.00124189484904082 0.998758105150959 arachidonate 15-lipoxygenase FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Converts arachidonic acid into 12- hydroperoxyeicosatetraenoic acid/12-HPETE and 15- hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)- hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3. Probably plays an important role in the immune and inflammatory responses. Through the oxygenation of membrane-bound phosphatidylethanolamine in macrophages may favor clearance of apoptotic cells during inflammation by resident macrophages and prevent an autoimmune response associated with the clearance of apoptotic cells by inflammatory monocytes. In parallel, may regulate actin polymerization which is crucial for several biological processes, including macrophage function. May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway. Finally, it is also involved in the cellular response to IL13/interleukin-13. In addition to its role in the immune and inflammatory responses, may play a role in epithelial wound healing in the cornea maybe through production of lipoxin A4. May also play a role in endoplasmic reticulum stress response and the regulation of bone mass. {ECO:0000269|PubMed:17052953, ECO:0000269|PubMed:21831839}.; DISEASE: Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry. Met at position 560 may confer interindividual susceptibility to coronary artery disease (CAD) (PubMed:17959182). {ECO:0000269|PubMed:17959182}.; TISSUE SPECIFICITY: Detected in monocytes and eosinophils (at protein level). Expressed in airway epithelial cells. {ECO:0000269|PubMed:21831839, ECO:0000269|PubMed:9414270}.; unclassifiable (Anatomical System);prostate;lymph node;lung;cartilage;testis;brain; dorsal root ganglion;superior cervical ganglion;trachea;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09356 0.24480 -0.12856188 44.04930408 504.62918 4.61057 ALOX15B 1.91964555587148e-12 0.110781403071827 0.889218596926253 arachidonate 15-lipoxygenase, type B FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Converts arachidonic acid to 15S- hydroperoxyeicosatetraenoic acid/(15S)-HPETE. Also acts on linoleic acid to produce 13-hydroxyoctadecadienoic acid/13-HPODE. Has no detectable 8S-lipoxygenase activity but reacts with (8S)- HPETE to produce (8S,15S)-diHPETE. May regulate progression through the cell cycle and cell proliferation. May also regulate cytokine secretion by macrophages and therefore play a role in the immune response. May also regulate macrophage differentiation into proatherogenic foam cells. {ECO:0000269|PubMed:10625675, ECO:0000269|PubMed:11839751, ECO:0000269|PubMed:12704195, ECO:0000269|PubMed:16112079, ECO:0000269|PubMed:18067895, ECO:0000269|PubMed:22912809, ECO:0000269|PubMed:24497644}.; . TISSUE SPECIFICITY: Expressed in hair, prostate, lung, ovary, lymph node, spinal cord and cornea. {ECO:0000269|PubMed:10542053, ECO:0000269|PubMed:11350124, ECO:0000269|PubMed:9177185}.; unclassifiable (Anatomical System);uterus;prostate;lung;mammary gland;skin; prostate;superior cervical ganglion;atrioventricular node; 0.11636 . 0.981046964 90.45765511 2525.67053 9.37601 ALOX15P1 . . . arachidonate 15-lipoxygenase pseudogene 1 . . . . . . . . . . . ALOX15P2 . . . arachidonate 15-lipoxygenase pseudogene 2 . . . unclassifiable (Anatomical System); . 0.09427 . . . . . ALOXE3 2.16324720861559e-13 0.208653651322406 0.791346348677377 arachidonate lipoxygenase 3 FUNCTION: Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced dioxygenase activity compared to other lipoxygenases. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols. The dioxygenase activity requires a step of activation of the enzyme by molecular oxygen. In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides. In the skin, acts downstream of ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl- sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites. Plays also a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG. Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia. {ECO:0000269|PubMed:12881489, ECO:0000269|PubMed:17045234, ECO:0000269|PubMed:20921226, ECO:0000269|PubMed:20923767, ECO:0000269|PubMed:21558561}.; . TISSUE SPECIFICITY: Predominantly expressed in skin.; optic nerve;nasopharynx;placenta;macula lutea;colon;fovea centralis;choroid;kidney;lens;bladder;retina; dorsal root ganglion;medulla oblongata;superior cervical ganglion;temporal lobe;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.09931 0.15375 -0.995664936 8.539749941 991.24555 6.06838 ALOXE3P1 . . . arachidonate lipoxygenase 3 pseudogene 1 . . . . . . . . . . . ALPI 4.02971384353915e-16 0.00292832403144265 0.997071675968557 alkaline phosphatase, intestinal . . . unclassifiable (Anatomical System);cervix; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle;cerebellum; 0.16091 0.90971 -0.394936437 27.02878037 160.50719 2.76426 ALPK1 9.99914293624518e-08 0.996182482343844 0.00381741766472644 alpha kinase 1 FUNCTION: Kinase that recognizes phosphorylation sites in which the surrounding peptides have an alpha-helical conformation.; . TISSUE SPECIFICITY: Highly expressed in liver. {ECO:0000269|PubMed:10819331}.; ovary;colon;parathyroid;skin;uterus;prostate;cochlea;endometrium;larynx;thyroid;bone;germinal center;brain;gall bladder;unclassifiable (Anatomical System);heart;cartilage;urinary;skeletal muscle;lung;placenta;liver;hypopharynx;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node; 0.13433 0.09578 1.458702267 95.175749 1017.82107 6.13900 ALPK2 3.561471165346e-13 0.89022525951472 0.109774740484924 alpha kinase 2 FUNCTION: Kinase that recognizes phosphorylation sites in which the surrounding peptides have an alpha-helical conformation.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;whole body;lung;larynx;nasopharynx;placenta;macula lutea;visual apparatus;testis;head and neck;cervix;kidney;gall bladder; superior cervical ganglion;skeletal muscle; 0.03572 0.07481 4.926038688 99.79948101 17557.68576 27.86174 ALPK3 3.54006995242909e-09 0.999218959169167 0.000781037290763196 alpha kinase 3 FUNCTION: Kinase that recognizes phosphorylation sites in which the surrounding peptides have an alpha-helical conformation. Plays a role in cardiomyocyte differentiation (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;spinal cord;colon;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;whole body;lung;macula lutea;hypopharynx;testis;head and neck;stomach; dorsal root ganglion;superior cervical ganglion;heart;atrioventricular node;trigeminal ganglion;pituitary;skeletal muscle;skin; 0.14433 0.11326 0.229465655 68.54800661 3085.49692 10.55039 ALPL 0.00110649599056032 0.988603965313191 0.0102895386962491 alkaline phosphatase, liver/bone/kidney FUNCTION: This isozyme may play a role in skeletal mineralization.; DISEASE: Hypophosphatasia (HOPS) [MIM:146300]: A metabolic bone disease characterized by defective skeletal mineralization and biochemically by deficient activity of the tissue non-specific isoenzyme of alkaline phosphatase. Four forms are distinguished, depending on the age of onset: perinatal, infantile, childhood and adult type. The perinatal form is the most severe and is almost always fatal. The adult form is mild and characterized by recurrent fractures, osteomalacia, rickets, and loss of teeth. Some cases are asymptomatic, while some patients manifest dental features without skeletal manifestations (odontohypophosphatasia). {ECO:0000269|PubMed:10094560, ECO:0000269|PubMed:10332035, ECO:0000269|PubMed:10679946, ECO:0000269|PubMed:10690885, ECO:0000269|PubMed:10834525, ECO:0000269|PubMed:11438998, ECO:0000269|PubMed:11745997, ECO:0000269|PubMed:11760847, ECO:0000269|PubMed:11834095, ECO:0000269|PubMed:11855933, ECO:0000269|PubMed:11999978, ECO:0000269|PubMed:12815606, ECO:0000269|PubMed:12920074, ECO:0000269|PubMed:1409720, ECO:0000269|PubMed:15135428, ECO:0000269|PubMed:15694177, ECO:0000269|PubMed:3174660, ECO:0000269|PubMed:7833929, ECO:0000269|PubMed:8406453, ECO:0000269|PubMed:8954059, ECO:0000269|PubMed:9452105, ECO:0000269|PubMed:9747027, ECO:0000269|PubMed:9781036}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hypophosphatasia childhood type (HOPSC) [MIM:241510]: A bone disease characterized by defective skeletal mineralization and biochemically by deficient activity of the tissue non-specific isoenzyme of alkaline phosphatase. {ECO:0000269|PubMed:11760847}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hypophosphatasia infantile type (HOPSI) [MIM:241500]: A severe bone disease characterized by defective skeletal mineralization and biochemically by deficient activity of the tissue non-specific isoenzyme of alkaline phosphatase. Three more or less distinct types of infantile hypophosphatasia can be identified: (1) type 1 with onset in utero or in early postnatal life, craniostenosis, severe skeletal abnormalities, hypercalcemia, and death in the first year or so of life; (2) type 2 with later, more gradual development of symptoms, moderately severe 'rachitic' skeletal changes and premature loss of teeth; (3) type 3 with no symptoms, the condition being determined on routine studies. {ECO:0000269|PubMed:10834525, ECO:0000269|PubMed:11438998, ECO:0000269|PubMed:7833929, ECO:0000269|PubMed:8954059}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.45580 0.92770 7.61E-05 53.98089172 1799.01779 7.82256 ALPP 1.68537812798331e-06 0.86268209692015 0.137316217701722 alkaline phosphatase, placental . . TISSUE SPECIFICITY: Detected in placenta (at protein level). {ECO:0000269|PubMed:20693656}.; . . 0.11261 0.13673 1.35769336 94.43854683 1957.1571 8.14348 ALPPL2 6.22052907362555e-06 0.695575147786352 0.304418631684574 alkaline phosphatase, placental like 2 . . TISSUE SPECIFICITY: Trace amounts in the testis and thymus, and in elevated amounts in germ cell tumors.; unclassifiable (Anatomical System);uterus;pancreas;lung;endometrium;placenta;testis;colon;stomach;aorta; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;medulla oblongata;placenta;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.06594 0.18722 0.468503535 78.79806558 485.30454 4.53799 ALPPP . . . alkaline phosphatase, pseudogene . . . . . . . . . . . ALS2 0.000769641354733604 0.999230358231185 4.14081107587641e-10 ALS2, alsin Rho guanine nucleotide exchange factor FUNCTION: May act as a GTPase regulator. Controls survival and growth of spinal motoneurons (By similarity). {ECO:0000250}.; DISEASE: Amyotrophic lateral sclerosis 2 (ALS2) [MIM:205100]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. {ECO:0000269|PubMed:11586298}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Juvenile primary lateral sclerosis (JPLS) [MIM:606353]: A neurodegenerative disorder which is closely related to but clinically distinct from amyotrophic lateral sclerosis. It is a progressive paralytic disorder which results from dysfunction of the upper motor neurons while the lower neurons are unaffected. {ECO:0000269|PubMed:11586297}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Infantile-onset ascending spastic paralysis (IAHSP) [MIM:607225]: Characterized by progressive spasticity and weakness of limbs. {ECO:0000269|PubMed:12145748}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;tongue;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;cerebellum peduncles;cerebellum; 0.23951 . -1.455091209 3.886529842 476.17155 4.50717 ALS2CL 2.72979618994274e-18 0.0552413408076501 0.94475865919235 ALS2 C-terminal like FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for Rab5 GTPase. Regulates the ALS2-mediated endosome dynamics. {ECO:0000269|PubMed:15388334, ECO:0000269|PubMed:16473597, ECO:0000269|PubMed:17239822}.; . TISSUE SPECIFICITY: Expressed in heart and kidney. {ECO:0000269|PubMed:15388334}.; unclassifiable (Anatomical System);cartilage;ovary;lacrimal gland;pharynx;colon;skin;uterus;prostate;optic nerve;lung;nasopharynx;thyroid;placenta;liver;cervix;spleen;kidney;brain;aorta;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;ciliary ganglion;pons;kidney;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle;parietal lobe;cerebellum; 0.14490 0.10583 -0.918644703 9.807737674 4706.22743 13.83913 ALS2CR11 7.66191254911719e-11 0.422951775169414 0.577048224753967 amyotrophic lateral sclerosis 2 chromosome region candidate 11 . . . unclassifiable (Anatomical System);lung;pineal body;hippocampus;testis;skeletal muscle; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22302 . 2.535637851 98.7084218 653.81059 5.13101 ALS2CR12 1.66284147135039e-10 0.20511778001597 0.794882219817746 amyotrophic lateral sclerosis 2 chromosome region candidate 12 . . . unclassifiable (Anatomical System);uterus;medulla oblongata;lung;nasopharynx;liver;testis;spleen; . 0.01855 0.05854 -0.732911333 14.07761264 59.99054 1.57243 ALS3 . . . amyotrophic lateral sclerosis 3 (autosomal dominant) . . . . . . . . . . . ALS5 . . . amyotrophic lateral sclerosis 5 . . . . . . . . . . . ALS7 . . . amyotrophic lateral sclerosis 7 . . . . . . . . . . . ALX1 0.600326160302233 0.397739734220174 0.00193410547759256 ALX homeobox 1 FUNCTION: Sequence-specific DNA-binding transcription factor that binds palindromic sequences within promoters and may activate or repress the transcription of a subset of genes (PubMed:9753625, PubMed:8756334). Most probably regulates the expression of genes involved in the development of mesenchyme-derived craniofacial structures. Early on in development, it plays a role in forebrain mesenchyme survival (PubMed:20451171). May also induce epithelial to mesenchymal transition (EMT) through the expression of SNAI1 (PubMed:23288509). {ECO:0000269|PubMed:20451171, ECO:0000269|PubMed:23288509, ECO:0000269|PubMed:8756334, ECO:0000269|PubMed:9753625}.; DISEASE: Frontonasal dysplasia 3 (FND3) [MIM:613456]: The term frontonasal dysplasia describes an array of abnormalities affecting the eyes, forehead and nose and linked to midfacial dysraphia. The clinical picture is highly variable. Major findings include true ocular hypertelorism; broadening of the nasal root; median facial cleft affecting the nose and/or upper lip and palate; unilateral or bilateral clefting of the alae nasi; lack of formation of the nasal tip; anterior cranium bifidum occultum; a V-shaped or widow's peak frontal hairline. {ECO:0000269|PubMed:20451171}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Cartilage and cervix tissue. {ECO:0000269|PubMed:8756334}.; unclassifiable (Anatomical System);uterus;bile duct;whole body;heart;skin; superior cervical ganglion;medulla oblongata;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.65422 0.10311 0.306902668 72.38145789 153.29937 2.70756 ALX3 0.208670051874219 0.74998866092841 0.0413412871973711 ALX homeobox 3 FUNCTION: Transcriptional regulator with a possible role in patterning of mesoderm during development. {ECO:0000250}.; DISEASE: Frontonasal dysplasia 1 (FND1) [MIM:136760]: The term frontonasal dysplasia describes an array of abnormalities affecting the eyes, forehead and nose and linked to midfacial dysraphia. The clinical picture is highly variable. Major findings include true ocular hypertelorism; broadening of the nasal root; median facial cleft affecting the nose and/or upper lip and palate; unilateral or bilateral clefting of the alae nasi; lack of formation of the nasal tip; anterior cranium bifidum occultum; a V-shaped or widow's peak frontal hairline. {ECO:0000269|PubMed:19409524}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.52130 0.09992 -0.249709319 35.74545883 42.10694 1.22621 ALX4 0.23488770388706 0.757872347882317 0.00723994823062278 ALX homeobox 4 FUNCTION: Transcription factor involved in skull and limb development. Plays an essential role in craniofacial development, skin and hair follicle development. {ECO:0000269|PubMed:19692347}.; DISEASE: Frontonasal dysplasia 2 (FND2) [MIM:613451]: The term frontonasal dysplasia describes an array of abnormalities affecting the eyes, forehead and nose and linked to midfacial dysraphia. The clinical picture is highly variable. Major findings include true ocular hypertelorism; broadening of the nasal root; median facial cleft affecting the nose and/or upper lip and palate; unilateral or bilateral clefting of the alae nasi; lack of formation of the nasal tip; anterior cranium bifidum occultum; a V-shaped or widow's peak frontal hairline. {ECO:0000269|PubMed:19692347}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Potocki-Shaffer syndrome (POSHS) [MIM:601224]: A syndrome characterized by foramina parietalia permagna, multiple exostoses, and craniofacial dysostosis and mental retardation in some cases. {ECO:0000305|PubMed:11017806, ECO:0000305|PubMed:11903336}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Craniosynostosis 5 (CRS5) [MIM:615529]: A primary abnormality of skull growth involving premature fusion of one or more cranial sutures. The growth velocity of the skull often cannot match that of the developing brain resulting in an abnormal head shape and, in some cases, increased intracranial pressure, which must be treated promptly to avoid permanent neurodevelopmental disability. {ECO:0000269|PubMed:22829454}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expression is likely to be restricted to bone. Found in parietal bone.; unclassifiable (Anatomical System);retina; uterus corpus;superior cervical ganglion; 0.78445 0.21643 -0.446304853 24.33356924 6688.59361 17.32616 ALYREF 0.831865499534863 0.164682391212089 0.00345210925304791 Aly/REF export factor FUNCTION: Export adapter involved in nuclear export of spliced and unspliced mRNA. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway). Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm. TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production; ALYREF/THOC4 mediates the recruitment of the TREX complex to the intronless viral mRNA. Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC). In conjunction with THOC5 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim. Involved in the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B. Involved in transcription elongation and genome stability. {ECO:0000269|PubMed:25662211}.; . TISSUE SPECIFICITY: Expressed in a wide variety of cancer types. {ECO:0000269|PubMed:25662211}.; ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;lung;placenta;visual apparatus;macula lutea;kidney;mammary gland;stomach; prostate;thyroid;tumor;testis;white blood cells;thymus; 0.54930 0.28383 . . 29.02711 0.92805 AMACR 0.125255655188202 0.85105876852591 0.0236855762858875 alpha-methylacyl-CoA racemase FUNCTION: Racemization of 2-methyl-branched fatty acid CoA esters. Responsible for the conversion of pristanoyl-CoA and C27-bile acyl-CoAs to their (S)-stereoisomers.; DISEASE: Alpha-methylacyl-CoA racemase deficiency (AMACRD) [MIM:614307]: A rare autosomal recessive peroxisomal disorder characterized by elevated plasma concentrations of pristanic acid C27-bile-acid intermediates, and adult onset of variable neurodegenerative symptoms affecting the central and peripheral nervous systems. Features may include seizures, visual failure, sensorimotor neuropathy, spasticity, migraine, and white matter hyperintensities on brain imaging. {ECO:0000269|PubMed:10655068}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Congenital bile acid synthesis defect 4 (CBAS4) [MIM:214950]: A disorder characterized by the presence of trihydroxycoprostanic acid in the bile and absence of cholic acid. Patients manifest neonatal jaundice, intrahepatic cholestasis and bile duct deficiency. {ECO:0000269|PubMed:10655068, ECO:0000269|PubMed:12512044}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;islets of Langerhans;muscle;lens;pancreas;lung;placenta;macula lutea;hippocampus;liver;hypopharynx;head and neck;cervix;kidney;stomach; . . 0.31390 1.418384579 94.89266336 3974.7764 12.47177 AMBN 1.8551891948061e-05 0.885754156541975 0.114227291566077 ameloblastin FUNCTION: Involved in the mineralization and structural organization of enamel.; . TISSUE SPECIFICITY: Ameloblast-specific. Located at the Tomes processes of secretory ameloblasts and in the sheath space between rod-interrod enamel.; unclassifiable (Anatomical System); superior cervical ganglion;uterus corpus;ciliary ganglion;trigeminal ganglion;skin;skeletal muscle; 0.11933 0.06650 1.554322597 95.64166077 4497.77172 13.46842 AMBP 4.48294573237029e-10 0.104104573436301 0.895895426115405 alpha-1-microglobulin/bikunin precursor FUNCTION: Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization. {ECO:0000269|PubMed:7676539}.; . TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. Alpha-1-microglobulin occurs in many physiological fluids including plasma, urine, and cerebrospinal fluid. Inter-alpha- trypsin inhibitor is present in plasma and urine.; unclassifiable (Anatomical System);heart;islets of Langerhans;colon;skin;skeletal muscle;uterus;whole body;lung;liver;testis;spleen;kidney;brain;stomach;gall bladder; superior cervical ganglion;fetal liver;beta cell islets;liver;fetal lung;atrioventricular node;skeletal muscle; 0.32112 0.34303 -0.488577883 22.64685067 164.09787 2.79712 AMBRA1 0.999971640508962 2.83594909641456e-05 7.36477996054105e-14 autophagy/beclin-1 regulator 1 FUNCTION: Regulates autophagy and development of the nervous system. Involved in autophagy in controlling protein turnover during neuronal development, and in regulating normal cell survival and proliferation (By similarity). {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;vein;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;pharynx;blood;lens;bile duct;breast;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;kidney;stomach;peripheral nerve; whole brain;globus pallidus; 0.36907 0.10363 -0.971800989 8.946685539 137.80881 2.55655 AMCN . . . arthrogryposis multiplex congenita, neurogenic . . . . . . . . . . . AMD1 0.903413517651479 0.0964180513038043 0.000168431044717145 adenosylmethionine decarboxylase 1 FUNCTION: Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels (By similarity). {ECO:0000250}.; . . . . 0.76646 0.29043 -0.09720619 46.20193442 19.21749 0.66222 AMD1P1 . . . adenosylmethionine decarboxylase 1 pseudogene 1 . . . . . . . . . . . AMD1P2 . . . adenosylmethionine decarboxylase 1 pseudogene 2 . . . . . . . . . . . AMD1P3 . . . adenosylmethionine decarboxylase 1 pseudogene 3 . . . . . . . . . . . AMD1P4 . . . adenosylmethionine decarboxylase 1 pseudogene 4 . . . . . . . . . . . AMDHD1 2.46953918892759e-06 0.496206359944714 0.503791170516097 amidohydrolase domain containing 1 . . . unclassifiable (Anatomical System);lymph node;heart;ovary;islets of Langerhans;lens;skin;bone marrow;uterus;prostate;lung;liver;testis;spleen;kidney;brain; superior cervical ganglion;fetal liver;ciliary ganglion; 0.10939 0.11408 -0.001743238 53.85114414 244.5349 3.37372 AMDHD2 2.64249958224576e-07 0.494271532819726 0.505728202930316 amidohydrolase domain containing 2 FUNCTION: Hydrolyzes the N-glycolyl group from N- glycolylglucosamine 6-phosphate (GlcNGc-6-P) in the N- glycolylneuraminic acid (Neu5Gc) degradation pathway. Although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded. {ECO:0000269|PubMed:22692205}.; . . unclassifiable (Anatomical System);medulla oblongata;heart;islets of Langerhans;colon;blood;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;lung;placenta;macula lutea;alveolus;liver;testis;spleen;germinal center;kidney;brain;stomach;cerebellum; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;bone marrow; 0.17173 0.15363 -0.196519234 39.20736023 27.79097 0.89245 AMELX 0.187525654901344 0.762325064173111 0.0501492809255453 amelogenin, X-linked FUNCTION: Plays a role in biomineralization. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel.; DISEASE: Amelogenesis imperfecta 1E (AI1E) [MIM:301200]: A X- linked defect of dental enamel formation. Teeth have only a thin layer of enamel with normal hardness. The thinness of the enamel makes the teeth appear small. {ECO:0000269|PubMed:10669095, ECO:0000269|PubMed:15111628, ECO:0000269|PubMed:7599636, ECO:0000269|PubMed:7782077, ECO:0000269|PubMed:9188994}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.14574 0.24801 0.058937498 58.26256192 155.06754 2.72000 AMELY 0.00205505416408899 0.302286318116914 0.695658627718997 amelogenin, Y-linked FUNCTION: Plays a role in biomineralization. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel.; . . . . 0.14226 . . . 5.09572 0.18903 AMER1 0.953441252971679 0.0465533930287297 5.35399959106712e-06 APC membrane recruitment protein 1 FUNCTION: Regulator of the canonical Wnt signaling pathway. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex. Acts both as a positive and negative regulator of the Wnt signaling pathway, depending on the context: acts as a positive regulator by promoting LRP6 phosphorylation. Also acts as a negative regulator by acting as a scaffold protein for the beta- catenin destruction complex and promoting stabilization of Axin at the cell membrane. Promotes CTNNB1 ubiquitination and degradation. Involved in kidney development. {ECO:0000269|PubMed:17510365, ECO:0000269|PubMed:17925383, ECO:0000269|PubMed:19416806, ECO:0000269|PubMed:21304492, ECO:0000269|PubMed:21498506}.; . TISSUE SPECIFICITY: Detected in fetal and adult kidney, brain and spleen. {ECO:0000269|PubMed:19416806}.; . . . 0.08523 -0.394936437 27.02878037 88.95926 2.02444 AMER2 . . . APC membrane recruitment protein 2 FUNCTION: Negative regulator of the canonical Wnt signaling pathway involved in neuroectodermal patterning. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex. {ECO:0000269|PubMed:22128170}.; . . . . 0.34447 0.10461 0.130533008 63.35810333 488.56421 4.55000 AMER3 0.000112022874748601 0.949334972519144 0.0505530046061074 APC membrane recruitment protein 3 FUNCTION: Regulator of the canonical Wnt signaling pathway. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane (By similarity). {ECO:0000250}.; . . . . 0.13690 . -1.082044518 7.242274121 653.10592 5.12811 AMFR 0.00142575921262617 0.997096980770004 0.00147726001736977 autocrine motility factor receptor, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase that mediates the polyubiquitination of a number of proteins such as CD3D, CYP3A4, CFTR and APOB for proteasomal degradation. Component of a VCP/p97- AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD). The VCP/p97- AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG complex at the ER membrane and initiating ubiquitination of HMGCR. The ubiquitinated HMGCR is then released from the ER by the complex into the cytosol for subsequent destruction. Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation. Mediates tumor invasion and metastasis as a receptor for the GPI/autocrine motility factor. {ECO:0000269|PubMed:10456327, ECO:0000269|PubMed:11724934, ECO:0000269|PubMed:16168377, ECO:0000269|PubMed:19103148}.; . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hypopharynx;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;placenta;liver;kidney;atrioventricular node; 0.31726 0.17249 -1.089312628 7.047652748 24.87307 0.81595 AMH 4.8954693456369e-05 0.425631187669798 0.574319857636746 anti-Mullerian hormone FUNCTION: This glycoprotein, produced by the Sertoli cells of the testis, causes regression of the Muellerian duct. It is also able to inhibit the growth of tumors derived from tissues of Muellerian duct origin.; DISEASE: Persistent Muellerian duct syndrome 1 (PMDS1) [MIM:261550]: A form of male pseudohermaphroditism characterized by a failure of Muellerian duct regression in otherwise normal males. {ECO:0000269|PubMed:8162013, ECO:0000269|PubMed:8872466}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);medulla oblongata;prostate;lung;endometrium;hippocampus;testis;colon;brain;stomach; superior cervical ganglion;testis;skeletal muscle; 0.34555 . . . 94.57913 2.09401 AMHR2 5.93082108191015e-07 0.966759053928051 0.0332403529898409 anti-Mullerian hormone receptor type II FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for anti-Muellerian hormone.; DISEASE: Persistent Muellerian duct syndrome 2 (PMDS2) [MIM:261550]: A form of male pseudohermaphroditism characterized by a failure of Muellerian duct regression in otherwise normal males. {ECO:0000269|PubMed:11549681, ECO:0000269|PubMed:8872466}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;muscle;testis;spleen; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.32915 0.15847 -0.934977358 9.465675867 43.34161 1.25102 AMIGO1 0.888492588974354 0.110323722167703 0.00118368885794294 adhesion molecule with Ig-like domain 1 FUNCTION: Promotes growth and fasciculation of neurites from cultured hippocampal neurons. May be involved in fasciculation as well as myelination of developing neural axons. May have a role in regeneration as well as neural plasticity in the adult nervous system. May mediate homophilic as well as heterophilic cell-cell interaction and contribute to signal transduction through its intracellular domain. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. {ECO:0000250|UniProtKB:Q80ZD7, ECO:0000250|UniProtKB:Q80ZD8}.; . . . . 0.27618 0.11809 0.038710339 56.92380278 123.92652 2.42339 AMIGO2 0.545241647080824 0.440670798372426 0.0140875545467494 adhesion molecule with Ig-like domain 2 FUNCTION: Required for depolarization-dependent survival of cultured cerebellar granule neurons. May mediate homophilic as well as heterophilic cell-cell interaction with AMIGO1 or AMIGO3. May contribute to signal transduction through its intracellular domain. May be required for tumorigenesis of a subset of gastric adenocarcinomas.; . TISSUE SPECIFICITY: Highest levels in breast, ovary, cervix, and uterus. Lower levels in lung, colon, and rectum. Differentially expressed in 56% of thyroid, 57% of pancreatic and 45% of stomach cancers. {ECO:0000269|PubMed:15107827}.; lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lacrimal gland;bile duct;pancreas;lung;nasopharynx;placenta;kidney;stomach;aorta; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.11993 0.12758 -0.824740496 11.67728238 58.75095 1.55524 AMIGO3 7.50516210752013e-06 0.16436699184146 0.835625502996433 adhesion molecule with Ig-like domain 3 FUNCTION: May mediate heterophilic cell-cell interaction. May contribute to signal transduction through its intracellular domain (By similarity). {ECO:0000250|UniProtKB:Q80ZD5}.; . . unclassifiable (Anatomical System);pancreas;frontal lobe;salivary gland; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.08870 0.10047 -0.025608647 51.91672564 77.80269 1.85916 AMLCR2 . . . acute myeloid leukemia chromosome region 2 . . . . . . . . . . . AMMECR1 0.910792997313756 0.088538552466586 0.000668450219658442 Alport syndrome, mental retardation, midface hypoplasia and elliptocytosis chromosomal region gene 1 . DISEASE: Alport syndrome with mental retardation, midface hypoplasia and elliptocytosis (ATS-MR) [MIM:300194]: A X-linked contiguous gene deletion syndrome characterized by glomerulonephritis, sensorineural hearing loss, mental retardation, midface hypoplasia and elliptocytosis. {ECO:0000269|PubMed:10049589}. Note=The gene represented in this entry may be involved in disease pathogenesis.; . unclassifiable (Anatomical System);liver;spleen;brain;skeletal muscle;aorta; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.89609 0.33817 -0.09720619 46.20193442 15.37972 0.55190 AMMECR1-IT1 . . . AMMECR1 intronic transcript 1 . . . . . . . . . . . AMMECR1L 0.995586601652785 0.00441300285159619 3.95495618655464e-07 AMMECR1 like . . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;globus pallidus;testis;ciliary ganglion;atrioventricular node;skin; 0.41124 0.07590 0.193034296 66.82000472 33.84681 1.04114 AMMECR1LP1 . . . AMMECR1 like pseudogene 1 . . . . . . . . . . . AMN 0.0923578355683243 0.869041267846767 0.0386008965849083 amnion associated transmembrane protein FUNCTION: Necessary for efficient absorption of vitamin B12. May direct the production of trunk mesoderm during development by modulating a bone morphogenetic protein (BMP) signaling pathway in the underlying visceral endoderm (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Long isoforms are highly expressed in small intestine, colon and kidney (renal proximal tubule epithelial cells). Shorter isoforms are detected at lower levels in testis, thymus and peripheral blood leukocytes. {ECO:0000269|PubMed:12590260, ECO:0000269|PubMed:14576052}.; unclassifiable (Anatomical System);lung;heart;islets of Langerhans;colon;cervix;blood;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.08071 . . . 240.30971 3.34868 AMN1 0.0201026561840101 0.903269075925975 0.0766282678900151 antagonist of mitotic exit network 1 homolog . . . colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;endometrium;oesophagus;bone;testis;germinal center;brain;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;lens;breast;pancreas;lung;placenta;hippocampus;visual apparatus;macula lutea;kidney;mammary gland;stomach; . 0.16099 0.10863 -0.09720619 46.20193442 8.21651 0.30300 AMOT 0.988710202830408 0.0112890006777473 7.9649184501178e-07 angiomotin FUNCTION: Plays a central role in tight junction maintenance via the complex formed with ARHGAP17, which acts by regulating the uptake of polarity proteins at tight junctions. Appears to regulate endothelial cell migration and tube formation. May also play a role in the assembly of endothelial cell-cell junctions. {ECO:0000269|PubMed:11257124, ECO:0000269|PubMed:16678097}.; . TISSUE SPECIFICITY: Expressed in placenta and skeletal muscle. Found in the endothelial cells of capillaries as well as larger vessels of the placenta. {ECO:0000269|PubMed:11257124}.; unclassifiable (Anatomical System);cartilage;heart;ovary;tongue;islets of Langerhans;spinal cord;colon;parathyroid;skin;skeletal muscle;uterus;prostate;whole body;lung;frontal lobe;endometrium;placenta;pituitary gland;liver;testis;head and neck;germinal center;kidney;brain;mammary gland; superior cervical ganglion;pons;skeletal muscle; 0.37835 0.09490 0.222355725 68.44184949 308.53332 3.73924 AMOTL1 0.31122818605871 0.688765394924795 6.41901649495341e-06 angiomotin like 1 FUNCTION: Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. {ECO:0000269|PubMed:22362771}.; . . unclassifiable (Anatomical System);cartilage;heart;muscle;skin;breast;uterus;pancreas;prostate;lung;endometrium;larynx;placenta;hypopharynx;testis;head and neck;brain;bladder;aorta;thymus; . 0.32669 0.10659 -0.437212558 24.67563105 554.4241 4.78411 AMOTL2 0.207914897262679 0.79200554642643 7.95563108912244e-05 angiomotin like 2 FUNCTION: Regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Required for proper architecture of actin filaments. Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. Participates in angiogenesis. May play a role in the polarity, proliferation and migration of endothelial cells. Selectively promotes FGF-induced MAPK activation through SRC. {ECO:0000269|PubMed:17293535, ECO:0000269|PubMed:21937427, ECO:0000269|PubMed:22362771}.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;testis;amniotic fluid;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pineal body;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach; . 0.08123 0.10718 0.804668134 87.71526303 520.58331 4.66028 AMPD1 3.77976185034765e-12 0.488664243014858 0.511335756981363 adenosine monophosphate deaminase 1 FUNCTION: AMP deaminase plays a critical role in energy metabolism.; . TISSUE SPECIFICITY: Three isoforms are present in mammals: AMP deaminase 1 is the predominant form in skeletal muscle; AMP deaminase 2 predominates in smooth muscle, non-muscle tissue, embryonic muscle and undifferentiated myoblasts; AMP deaminase 3 is found in erythrocytes.; unclassifiable (Anatomical System);greater omentum;pancreas;lung;thyroid;spinal cord;liver;skeletal muscle;bone marrow; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;cingulate cortex;skeletal muscle; 0.27146 0.44922 0.073492312 59.170795 1051.80051 6.22939 AMPD2 0.0085424965783861 0.991346093086706 0.000111410334907348 adenosine monophosphate deaminase 2 FUNCTION: AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle. {ECO:0000269|PubMed:23911318}.; DISEASE: Spastic paraplegia 63, autosomal recessive (SPG63) [MIM:615686]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. {ECO:0000269|PubMed:24482476}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in cerebellum. Three isoforms are present in mammals: AMP deaminase 1 is the predominant form in skeletal muscle; AMP deaminase 2 predominates in smooth muscle, non-muscle tissue, embryonic muscle and undifferentiated myoblasts; AMP deaminase 3 is found in erythrocytes. {ECO:0000269|PubMed:23911318}.; umbilical cord;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;heart;pineal body;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; amygdala;whole brain;medulla oblongata;subthalamic nucleus;superior cervical ganglion;hypothalamus;globus pallidus;caudate nucleus;pons;cingulate cortex;parietal lobe; 0.23763 0.21683 -1.462333834 3.786270347 1844.00657 7.92050 AMPD3 1.3313454680315e-08 0.940056902974642 0.0599430837119034 adenosine monophosphate deaminase 3 FUNCTION: AMP deaminase plays a critical role in energy metabolism.; . TISSUE SPECIFICITY: Isoform 1 is the predominant form in skeletal muscle; Isoform 2 predominates in smooth muscle, non-muscle tissue, embryonic muscle and undifferentiated myoblasts; Isoform 3 is found in erythrocytes.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;testis;spinal ganglion;brain;pineal gland;bladder;unclassifiable (Anatomical System);heart;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;testis - seminiferous tubule;trigeminal ganglion; 0.15592 0.30685 -0.214928658 37.7388535 527.98702 4.68895 AMPH 0.0322665655002833 0.967717850030128 1.55844695890889e-05 amphiphysin FUNCTION: May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton.; . TISSUE SPECIFICITY: Neurons, certain endocrine cell types and spermatocytes.; unclassifiable (Anatomical System);amygdala;heart;cerebellum cortex;islets of Langerhans;retina;atrium;lung;frontal lobe;placenta;bone;hippocampus;pituitary gland;testis;kidney;pineal gland;brain; whole brain;amygdala;thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;cerebellum peduncles;temporal lobe;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.23196 0.19053 0.225995239 68.51851852 678.4813 5.20472 AMT 0.000569475286585638 0.895662805708056 0.103767719005358 aminomethyltransferase FUNCTION: The glycine cleavage system catalyzes the degradation of glycine.; DISEASE: Non-ketotic hyperglycinemia (NKH) [MIM:605899]: Autosomal recessive disease characterized by accumulation of a large amount of glycine in body fluid and by severe neurological symptoms. {ECO:0000269|PubMed:10873393, ECO:0000269|PubMed:11286506, ECO:0000269|PubMed:26371980, ECO:0000269|PubMed:8005589, ECO:0000269|PubMed:9600239, ECO:0000269|PubMed:9621520}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;choroid;retina;bone marrow;prostate;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;artery;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;urinary;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;liver;ciliary ganglion;kidney;trigeminal ganglion;skeletal muscle;cerebellum; 0.39114 0.27728 -0.378346116 28.01368247 117.95799 2.36176 AMTN 1.12206536324357e-06 0.195968514436512 0.804030363498125 amelotin FUNCTION: Is a promoter of calcium phosphate mineralization, playing a critical role in the formation of the compact, mineralized, aprismatic enamel surface layer during the maturation stage of amelogenesis. {ECO:0000269|PubMed:25407797}.; . . optic nerve; . 0.04477 0.05467 1.304504747 93.94904459 1860.05162 7.94810 AMY1A 0.365183316916371 0.584893941801149 0.0499227412824803 amylase, alpha 1A (salivary) . . . . . 0.15126 0.48083 . . 5.53081 0.20622 AMY1B . . . amylase, alpha 1B (salivary) . . . ovary;parathyroid;fovea centralis;retina;bone marrow;uterus;frontal lobe;endometrium;cerebral cortex;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;skeletal muscle;bile duct;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;thymus; . 0.17574 0.40177 . . 16.83707 0.59269 AMY1C 0.844157662030798 0.153016090426583 0.0028262475426183 amylase, alpha 1C (salivary) . . . . . 0.17026 0.37631 . . 5.59633 0.20902 AMY2A 0.00560391741240498 0.898566185766073 0.0958298968215215 amylase, alpha 2A (pancreatic) . . TISSUE SPECIFICITY: Detected in pancreas (at protein level). {ECO:0000269|PubMed:8528071}.; . . 0.13172 0.48922 . . 1231.4964 6.63242 AMY2B 7.64543781687526e-09 0.690335157634563 0.30966483472 amylase, alpha 2B (pancreatic) . . . ovary;parathyroid;fovea centralis;retina;bone marrow;uterus;frontal lobe;endometrium;cerebral cortex;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;skeletal muscle;bile duct;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;thymus; . 0.12126 0.38738 0.110306132 62.00165133 318.05085 3.78784 AMYP1 . . . amylase, alpha pseudogene 1 . . . . . . . . . . . AMZ1 5.11962566427904e-18 0.000116039032111932 0.999883960967888 archaelysin family metallopeptidase 1 FUNCTION: Zinc metalloprotease. Exhibits aminopeptidase activity against neurogranin in vitro. Does not hydrolyze angiotensin-2. {ECO:0000269|PubMed:15972818}.; . TISSUE SPECIFICITY: Predominantly expressed in heart and liver. Also expressed at lower level in kidney, pancreas and testis. Expressed in fetal tissues such as kidney, liver, lung and brain. {ECO:0000269|PubMed:15972818}.; kidney;skin; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.19147 0.10588 0.258969574 69.83958481 2097.02586 8.43546 AMZ2 1.54653236502662e-08 0.116628489157258 0.883371495377419 archaelysin family metallopeptidase 2 FUNCTION: Zinc metalloprotease. Exhibits activity against angiotensin-3 in vitro. Does not hydrolyze either neurogranin or angiotensin-2. {ECO:0000269|PubMed:15972818}.; . TISSUE SPECIFICITY: Predominantly expressed in heart and testis. Also expressed at lower levels in kidney, liver, pancreas, lung, brain and placenta. Expressed in fetal tissues such as kidney, liver, lung and brain. Down-regulated in testis from patients with maturation arrest (MA) or Sertoli cell-only syndrome (SCOS). {ECO:0000269|PubMed:15972818, ECO:0000269|PubMed:17074343}.; ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;thymus; amygdala;subthalamic nucleus;occipital lobe;medulla oblongata;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;pons;caudate nucleus;parietal lobe; 0.13213 0.10068 0.507139401 80.10143902 66.56149 1.68126 AMZ2P1 . . . archaelysin family metallopeptidase 2 pseudogene 1 . . . . . . . . . . . AMZ2P2 . . . archaelysin family metallopeptidase 2 pseudogene 2 . . . . . . . . . . . ANAPC1 . . . anaphase promoting complex subunit 1 FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:18485873}.; . . ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; . 0.55585 0.09577 . . 199.72138 3.05270 ANAPC1P1 . . . anaphase promoting complex subunit 1 pseudogene 1 . . . . . . . . . . . ANAPC2 0.987268624004797 0.0127311595424454 2.1645275818505e-07 anaphase promoting complex subunit 2 FUNCTION: Together with the RING-H2 protein ANAPC11, constitutes the catalytic component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 drives presynaptic differentiation. {ECO:0000269|PubMed:11739784, ECO:0000269|PubMed:18485873}.; . . medulla oblongata;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;urinary;muscle;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;stomach;thymus; amygdala;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;cingulate cortex; 0.16054 0.11683 -1.658985203 2.724699222 72.57812 1.77615 ANAPC4 0.463847640731492 0.536152278758489 8.05100186636599e-08 anaphase promoting complex subunit 4 FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:18485873}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;head and neck;kidney;stomach;peripheral nerve; . 0.64914 0.12481 -0.800872469 12.33191791 677.04369 5.19957 ANAPC5 4.18001522765e-05 0.998009990181843 0.00194820966588037 anaphase promoting complex subunit 5 FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:18485873}.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;tongue;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;cerebral cortex;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);trophoblast;lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;hypothalamus;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.36079 . -0.554717505 19.79830149 76.22212 1.83030 ANAPC7 0.999257869586772 0.000742125297717887 5.1155103207623e-09 anaphase promoting complex subunit 7 FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:18485873}.; . . . . 0.61718 0.16480 0.463046108 78.58575136 159.89983 2.76049 ANAPC10 0.0575682391681918 0.866810934229556 0.0756208266022519 anaphase promoting complex subunit 10 FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:18485873}.; . . ovary;salivary gland;colon;skin;bone marrow;uterus;prostate;endometrium;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;kidney;aorta; testis - interstitial;testis;appendix;ciliary ganglion; . 0.15588 0.235309407 68.71903751 8.00863 0.29443 ANAPC10P1 . . . anaphase promoting complex subunit 10 pseudogene 1 . . . . . . . . . . . ANAPC11 0.192592194411128 0.759566240908476 0.0478415646803962 anaphase promoting complex subunit 11 FUNCTION: Together with the cullin protein ANAPC2, constitutes the catalytic component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May recruit the E2 ubiquitin-conjugating enzymes to the complex. {ECO:0000269|PubMed:11739784, ECO:0000269|PubMed:18485873}.; . TISSUE SPECIFICITY: Expressed at high levels in skeletal muscle and heart; in moderate levels in brain, kidney, and liver; and at low levels in colon, thymus, spleen, small intestine, placenta, lung and peripheral blood leukocyte. {ECO:0000269|PubMed:11573242}.; ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;larynx;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pineal body;muscle;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;cervix;head and neck;spleen;kidney;mammary gland;stomach; testis; 0.31540 0.06106 0.25917371 70.05779665 20.8868 0.70667 ANAPC13 0.00134979464058177 0.421193545468389 0.577456659891029 anaphase promoting complex subunit 13 FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:15060174, ECO:0000269|PubMed:18485873}.; . . myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;germinal center;bladder;brain;heart;cartilage;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;atrium;larynx;bone;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;amnion;head and neck;kidney;stomach;aorta; dorsal root ganglion;medulla oblongata;superior cervical ganglion;hypothalamus;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.46769 0.11262 -0.053113545 49.38664779 8.56989 0.31372 ANAPC15 0.564413605348492 0.423423146847391 0.0121632478041171 anaphase promoting complex subunit 15 FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. In the complex, plays a role in the release of the mitotic checkpoint complex (MCC) from the APC/C: not required for APC/C activity itself, but promotes the turnover of CDC20 and MCC on the APC/C, thereby participating in the responsiveness of the spindle assembly checkpoint. Also required for degradation of CDC20. {ECO:0000269|PubMed:21926987}.; . . . . 0.39459 0.11262 0.079165051 59.43029016 5.13875 0.19088 ANAPC16 0.0725864981457658 0.743220966573649 0.184192535280586 anaphase promoting complex subunit 16 FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:20360068}.; . . myocardium;ovary;sympathetic chain;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; . 0.19730 0.11262 0.457594962 78.16112291 5.97949 0.22466 ANCR . . . Angelman syndrome chromosome region . . . . . . . . . . . ANG 0.224577463484553 0.647083627225812 0.128338909289635 angiogenin, ribonuclease, RNase A family, 5 FUNCTION: Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus. Stimulates ribosomal RNA synthesis including that containing the initiation site sequences of 45S rRNA. Cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs) which inhibit protein synthesis and triggers the assembly of stress granules (SGs). Angiogenin induces vascularization of normal and malignant tissues. Angiogenic activity is regulated by interaction with RNH1 in vivo. {ECO:0000269|PubMed:12051708, ECO:0000269|PubMed:1400510, ECO:0000269|PubMed:19354288, ECO:0000269|PubMed:21855800}.; DISEASE: Amyotrophic lateral sclerosis 9 (ALS9) [MIM:611895]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. {ECO:0000269|PubMed:15557516, ECO:0000269|PubMed:16501576, ECO:0000269|PubMed:17703939, ECO:0000269|PubMed:17886298, ECO:0000269|PubMed:18087731, ECO:0000269|PubMed:22292843, ECO:0000269|PubMed:25372031}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly in the liver. Also detected in endothelial cells and spinal cord neurons. {ECO:0000269|PubMed:17886298, ECO:0000269|PubMed:2440105}.; unclassifiable (Anatomical System);smooth muscle;heart;tongue;colon;choroid;skin;skeletal muscle;retina;uterus;prostate;pancreas;whole body;lung;nasopharynx;bone;placenta;liver;testis;head and neck;spleen;kidney;brain;mammary gland;artery;aorta;stomach; fetal liver;trachea;liver;ciliary ganglion; 0.19005 . 0.237127192 68.98443029 5.00553 0.18624 ANGEL1 3.05586566551492e-10 0.476608150795038 0.523391848899375 angel homolog 1 (Drosophila) . . . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;kidney;stomach;cerebellum; testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;parietal lobe; 0.21857 0.08746 0.578735925 82.29535268 2501.69889 9.32248 ANGEL2 0.121064258682459 0.878712995776901 0.000222745540640599 angel homolog 2 (Drosophila) . . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;ganglion;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;prefrontal cortex;pons;trigeminal ganglion; 0.09135 . -0.111973265 45.35857514 117.41795 2.35564 ANGPT1 0.993331323979084 0.00666845655370838 2.19467207194337e-07 angiopoietin 1 FUNCTION: Binds and activates TEK/TIE2 receptor by inducing its dimerization and tyrosine phosphorylation. Plays an important role in the regulation of angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Required for normal angiogenesis and heart development during embryogenesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. Mediates blood vessel maturation/stability. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme. {ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:18425119, ECO:0000269|PubMed:18425120, ECO:0000269|PubMed:9204896}.; . . unclassifiable (Anatomical System);lymph node;cartilage;ovary;heart;adrenal cortex;parathyroid;skeletal muscle;retina;bone marrow;prostate;lung;adrenal gland;larynx;bone;thyroid;placenta;liver;testis;head and neck;spleen;kidney;pineal gland;artery;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.27062 0.39747 -0.337894035 30.37272942 69.07554 1.72234 ANGPT2 0.454891016173085 0.544855128996921 0.000253854829993581 angiopoietin 2 FUNCTION: Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal. {ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:19116766, ECO:0000269|PubMed:19223473, ECO:0000269|PubMed:9204896}.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;colon;skin;skeletal muscle;retina;uterus;whole body;lung;endometrium;thyroid;placenta;alveolus;liver;testis;spleen;kidney;stomach; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;skeletal muscle; 0.43501 0.10710 -0.420619508 25.72540694 100.43917 2.17130 ANGPT4 2.06397344414755e-09 0.131223018079611 0.868776979856416 angiopoietin 4 FUNCTION: Binds to TEK/TIE2, modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2. Promotes endothelial cell survival, migration and angiogenesis. {ECO:0000269|PubMed:15284220}.; . TISSUE SPECIFICITY: Highly expressed in the lung with much lower levels found in other tissues.; . . 0.08768 0.11828 0.090079492 60.64519934 277.1539 3.56523 ANGPTL1 1.52668512765821e-08 0.115789023551378 0.884210961181771 angiopoietin like 1 . . TISSUE SPECIFICITY: Highly expressed in adrenal gland, placenta, thyroid gland, heart, skeletal muscle and small intestine. Weakly expressed in testis, ovary, colon, pancreas, kidney and stomach. {ECO:0000269|PubMed:10025962}.; unclassifiable (Anatomical System);smooth muscle;lymph node;heart;islets of Langerhans;colon;skin;skeletal muscle;uterus;prostate;pancreas;optic nerve;whole body;lung;placenta;liver;testis;spleen;kidney;brain;artery;aorta; . 0.17096 0.12123 -0.600630256 18.06440198 72.48891 1.77414 ANGPTL2 0.182258216688379 0.815223036145592 0.0025187471660297 angiopoietin like 2 FUNCTION: Induces sprouting in endothelial cells through an autocrine and paracrine action.; . TISSUE SPECIFICITY: Widely expressed in heart, small intestine, spleen and stomach. Also found in lower levels in colon, ovary, adrenal gland, skeletal muscle and in prostate.; . . 0.77972 0.13443 -0.867014353 10.72776598 1182.6259 6.52636 ANGPTL3 2.12015609401708e-07 0.449484320429663 0.550515467554727 angiopoietin like 3 . . TISSUE SPECIFICITY: Expressed principally in liver. Weakly expressed in kidney. {ECO:0000269|PubMed:10644446}.; . . 0.61076 . -0.113792788 45.25831564 115.97808 2.34229 ANGPTL4 9.46497214192654e-09 0.16445937835471 0.835540612180318 angiopoietin like 4 FUNCTION: Protein with hypoxia-induced expression in endothelial cells. May act as a regulator of angiogenesis and modulate tumorigenesis. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. May exert a protective function on endothelial cells through an endocrine action. It is directly involved in regulating glucose homeostasis, lipid metabolism, and insulin sensitivity. In response to hypoxia, the unprocessed form of the protein accumulates in the subendothelial extracellular matrix (ECM). The matrix-associated and immobilized unprocessed form limits the formation of actin stress fibers and focal contacts in the adhering endothelial cells and inhibits their adhesion. It also decreases motility of endothelial cells and inhibits the sprouting and tube formation (By similarity). {ECO:0000250, ECO:0000269|PubMed:12015030, ECO:0000269|PubMed:14583458}.; . TISSUE SPECIFICITY: Expressed at high levels in the placenta, heart, liver, muscle, pancreas and lung but expressed poorly in the brain and kidney. {ECO:0000269|PubMed:10698685, ECO:0000269|PubMed:12015030}.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;synovium;bone;testis;spinal ganglion;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;stomach; dorsal root ganglion;placenta;temporal lobe;liver;ciliary ganglion;trigeminal ganglion; 0.06742 . 0.108486928 61.90728946 1333.38747 6.85804 ANGPTL5 1.75089935363839e-11 0.0159975611768682 0.984002438805623 angiopoietin like 5 . . TISSUE SPECIFICITY: Mainly expressed in adult heart. {ECO:0000269|PubMed:12624729}.; cartilage;hypothalamus;skin; . 0.14304 0.10715 0.374860183 75.43052607 415.57896 4.26813 ANGPTL6 2.76981473339532e-08 0.160992551391419 0.839007420910434 angiopoietin like 6 FUNCTION: May play a role in the wound healing process. May promote epidermal proliferation, remodeling and regeneration. May promote the chemotactic activity of endothelial cells and induce neovascularization. May counteract high-fat diet-induced obesity and related insulin resistance through increased energy expenditure.; . . colon;skin;bone marrow;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;testis;germinal center;dura mater;brain;unclassifiable (Anatomical System);cartilage;bile duct;pancreas;lung;adrenal gland;placenta;liver;spleen;head and neck;kidney; . 0.11090 . . . 89.90353 2.03969 ANGPTL7 8.44492793664119e-09 0.0829077402651316 0.91709225128994 angiopoietin like 7 . . TISSUE SPECIFICITY: Highly and specifically expressed in the cornea where is confined to the stromal layer. {ECO:0000269|PubMed:9727400}.; . . 0.80276 0.12577 0.17280645 65.75843359 419.9653 4.28061 ANGPTL8 . . . angiopoietin like 8 FUNCTION: Hormone that acts as a blood lipid regulator by regulating serum triglyceride levels (PubMed:22569073, PubMed:22809513, PubMed:23150577). May be involved in the metabolic transition between fasting and refeeding: required to direct fatty acids to adipose tissue for storage in the fed state (By similarity). {ECO:0000250|UniProtKB:Q8R1L8, ECO:0000269|PubMed:22569073, ECO:0000269|PubMed:22809513, ECO:0000269|PubMed:23150577}.; DISEASE: Diabetes mellitus, insulin-dependent (IDDM) [MIM:222100]: A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000305|PubMed:24078058}. Note=The gene represented in this entry may be involved in disease pathogenesis. Increased protein levels are observed in the serum of patients. This result should however be reinvestigated in light of recent advances that suggest that this protein is not promoting pancreatic beta cell proliferation. {ECO:0000305|PubMed:24078058}.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000305|PubMed:24852694, ECO:0000305|PubMed:24963292, ECO:0000305|PubMed:25024395, ECO:0000305|PubMed:25303484}. Note=The gene represented in this entry may be involved in disease pathogenesis. Increased protein levels are observed in the serum of patients and are associated with insulin resistance (PubMed:25024395, PubMed:25303484, PubMed:24963292, PubMed:24852694). According to another report, protein levels are decreased in the serum of patients (PubMed:25050901). Discrepancies between increased and decreased levels of proteins levels in NIDDM patients may be explained by the use of different kits developed on the market that either use antibodies recognizing the N-terminal or the C-terminal part of the protein (PubMed:25099942). These results should however be reinvestigated in light of recent advances that suggest that this protein is not promoting pancreatic beta cell proliferation. {ECO:0000305|PubMed:24852694, ECO:0000305|PubMed:24963292, ECO:0000305|PubMed:25024395, ECO:0000305|PubMed:25050901, ECO:0000305|PubMed:25099942, ECO:0000305|PubMed:25303484}.; TISSUE SPECIFICITY: Predominantly expressed in liver. Also expressed in adipose tissues. {ECO:0000269|PubMed:22569073, ECO:0000269|PubMed:22809513, ECO:0000269|PubMed:23150577, ECO:0000269|PubMed:23623304}.; . . . . 0.659651797 84.35362114 . . ANHX . . . anomalous homeobox . . . . . . . . . 3540.54114 11.47997 ANIB1 . . . aneurysm, intracranial berry 1 . . . . . . . . . . . ANIB2 . . . aneurysm, intracranial berry 2 . . . . . . . . . . . ANIB3 . . . aneurysm, intracranial berry 3 . . . . . . . . . . . ANIB4 . . . aneurysm, intracranial berry 4 . . . . . . . . . . . ANK1 0.999999999957629 4.23711851271793e-11 2.34865003674243e-27 ankyrin 1 FUNCTION: Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. {ECO:0000269|PubMed:12456646}.; DISEASE: Spherocytosis 1 (SPH1) [MIM:182900]: Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH1 is characterized by severe hemolytic anemia. Inheritance is autosomal recessive. {ECO:0000269|PubMed:11102985, ECO:0000269|PubMed:8640229}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform Mu17, isoform Mu18, isoform Mu19 and isoform Mu20 are expressed in skeletal muscle. Isoform Br21 is expressed in brain. {ECO:0000269|PubMed:9430667}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;thymus;cerebellum; medulla oblongata;superior cervical ganglion;fetal liver;tongue;cerebellum peduncles;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle;bone marrow;cerebellum; 0.75287 0.74808 -3.143373593 0.454116537 1000.57458 6.09450 ANK2 0.999999999999808 1.92138365459067e-13 3.15578290665686e-37 ankyrin 2, neuronal FUNCTION: In skeletal muscle, required for proper localization of DMD and DCTN4 and for the formation and/or stability of a special subset of microtubules associated with costameres and neuromuscular junctions (By similarity). Attaches integral membrane proteins to cytoskeletal elements. Also binds to cytoskeletal proteins. Required for coordinate assembly of Na/Ca exchanger, Na/K ATPase and InsP3 receptor at sarcoplasmic reticulum sites in cardiomyocytes. Required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) in the inner segment of rod photoreceptors. Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate. {ECO:0000250, ECO:0000269|PubMed:12571597}.; DISEASE: Long QT syndrome 4 (LQT4) [MIM:600919]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. Long QT syndrome type 4 shows many atypical features compared to classical long QT syndromes, including pronounced sinus bradycardia, polyphasic T waves and atrial fibrillation. Cardiac repolarization defects may be not as severe as in classical LQT syndromes and prolonged QT interval on EKG is not a consistent feature. {ECO:0000269|PubMed:12571597, ECO:0000269|PubMed:15178757}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Present in plasma membrane of neurons as well as glial cells throughout the brain. Expressed in fetal brain and in temporal cortex of adult brain. Also expressed in the inner segments of rod photoreceptors in retina. {ECO:0000269|PubMed:1830053, ECO:0000269|PubMed:1833308, ECO:0000269|PubMed:19007774}.; sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;testis;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;hypothalamus;spinal cord;lens;skeletal muscle;lung;adrenal gland;nasopharynx;trabecular meshwork;visual apparatus;hippocampus;macula lutea;liver;spleen;head and neck;kidney;aorta;stomach;peripheral nerve; amygdala;dorsal root ganglion;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.96488 0.13210 -3.328508946 0.412833215 4153.94899 12.79331 ANK3 0.999999999999921 7.91608437076065e-14 8.88951028904629e-37 ankyrin 3, node of Ranvier (ankyrin G) FUNCTION: In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments. Regulates KCNA1 channel activity in function of dietary Mg(2+) levels, and thereby contributes to the regulation of renal Mg(2+) reabsorption (PubMed:23903368). {ECO:0000250, ECO:0000269|PubMed:17974005}.; DISEASE: Note=Genetic variations in ANK3 may be associated with autism spectrum disorders susceptibility. {ECO:0000269|PubMed:22865819}.; DISEASE: Mental retardation, autosomal recessive 37 (MRT37) [MIM:615493]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT37 patients manifest delayed global development with speech delay, hypotonia, spasticity, and a sleep disorder. Severe behavioral abnormalities include aggression, hyperactivity, and grinding of the teeth. Note=The disease is caused by mutations affecting the gene represented in this entry. A homozygous deletion in ANK3 predicted to result in frameshift and premature truncation, has been shown to be the cause of moderate intellectual disability, an ADHD-like phenotype and behavioral problems in a consanguineous family (PubMed:23390136). {ECO:0000269|PubMed:23390136}.; TISSUE SPECIFICITY: Expressed in brain, neurons, muscles and other tissues. {ECO:0000269|PubMed:21223964, ECO:0000269|PubMed:7836469}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;larynx;thyroid;pituitary gland;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;alveolus;liver;spleen;head and neck;kidney;mammary gland;peripheral nerve; amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;thalamus;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.85781 0.22949 -3.496995436 0.33616419 2889.35508 10.18323 ANKAR 6.6124241759396e-24 0.00272744547647663 0.997272554523523 ankyrin and armadillo repeat containing . . TISSUE SPECIFICITY: Ubiquitously expressed with highest level in pancreas and lowest in skeletal muscle. {ECO:0000269|PubMed:15110750}.; unclassifiable (Anatomical System);testis;bone marrow; testis - interstitial;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.24662 0.09697 2.941884491 99.15664072 1089.51045 6.31979 ANKDD1A 1.16107189225281e-15 0.00545850874515069 0.994541491254848 ankyrin repeat and death domain containing 1A . . . ovary;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;frontal lobe;testis;unclassifiable (Anatomical System);amygdala;heart;hypothalamus;urinary;lens;bile duct;breast;lung;placenta;macula lutea;liver;spleen;kidney; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.10053 0.09163 -0.24061166 36.28214201 2935.68232 10.27688 ANKDD1B . . . ankyrin repeat and death domain containing 1B . . . . . . 0.06688 . . 5244.17915 14.91984 ANKEF1 2.75187176643953e-09 0.470942228825135 0.529057768422994 ankyrin repeat and EF-hand domain containing 1 . . . . . 0.17443 0.09325 -0.369255208 28.25548478 2476.18213 9.27712 ANKFN1 4.03101640243908e-06 0.997705324939036 0.00229064404456172 ankyrin repeat and fibronectin type III domain containing 1 . . . adrenal cortex;stomach; medulla oblongata;superior cervical ganglion;pons;cerebellum; 0.45099 . 0.600782551 82.82613824 1412.40698 7.02381 ANKFY1 0.994632887688137 0.00536711226807576 4.37873236131078e-11 ankyrin repeat and FYVE domain containing 1 FUNCTION: Proposed effector of Rab5. Binds to phosphatidylinositol 3-phosphate (PI(3)P). Involved in homotypic early endosome fusion and to a lesser extend in heterotypic fusion of chlathrin-coated vesicles with early endosomes. Involved in macropinocytosis; the function is dependent on Rab5-GTP. Required for correct endosomal localization. Involved in the internalization and trafficking of activated tyrosine kinase receptors such as PDGFRB. Regulates the sucellular localization of the retromer complex in a EHD1- dependent manner. Involved in endosome-to-Golgi transport and biosynthetic transport to late endosomes and lysosomes indicative for a regulation of retromer complex-mediated retrograde transport. {ECO:0000269|PubMed:15328530, ECO:0000269|PubMed:22284051, ECO:0000269|PubMed:24102721}.; . TISSUE SPECIFICITY: High expression in whole adult brain and intermediate expression in all other tissues and specific brain regions examined, including fetal brain. {ECO:0000269|PubMed:10574462, ECO:0000269|PubMed:10940552}.; ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;testis;amniotic fluid;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;alveolus;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;stomach;thymus; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.08266 0.12393 -1.747196778 2.359046945 105.49516 2.22545 ANKH 0.167376865709729 0.829652434883441 0.00297069940682956 ANKH inorganic pyrophosphate transport regulator FUNCTION: Regulates intra- and extracellular levels of inorganic pyrophosphate (PPi), probably functioning as PPi transporter.; DISEASE: Craniometaphyseal dysplasia, autosomal dominant (CMDD) [MIM:123000]: An osteochondrodysplasia characterized by hyperostosis and sclerosis of the craniofacial bones associated with abnormal modeling of the metaphyses. Sclerosis of the skull may lead to asymmetry of the mandible, as well as to cranial nerve compression, that may finally result in hearing loss and facial palsy. {ECO:0000269|PubMed:11326272, ECO:0000269|PubMed:11326338}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in osteoblasts from mandibular bone and from iliac bone; not detected in osteoclastic cells.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; dorsal root ganglion;cerebellum peduncles;prefrontal cortex;cerebellum; 0.12170 . -0.378346116 28.01368247 46.77893 1.32209 ANKHD1 0.999999999937697 6.23033434860623e-11 2.4595628697849e-28 ankyrin repeat and KH domain containing 1 FUNCTION: May play a role as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. Isoform 2 may possess an antiapoptotic effect and protect cells during normal cell survival through its regulation of caspases. {ECO:0000269|PubMed:16098192}.; . TISSUE SPECIFICITY: Ubiquitous with high expression in cervix, spleen and brain. Expressed in hematopoietic cells with increased expression in leukemia cells. Isoform 2 is highly expressed in spleen with almost no expression in muscle and brain. {ECO:0000269|PubMed:14557257, ECO:0000269|PubMed:16098192, ECO:0000269|PubMed:16956752}.; lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;duodenum;head and neck;kidney;stomach;cerebellum;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; . 0.11167 -2.357622074 1.138240151 265.86376 3.49714 ANKHD1-EIF4EBP3 0.999999999937697 6.23033434860623e-11 2.4595628697849e-28 ANKHD1-EIF4EBP3 readthrough FUNCTION: May play a role as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. Isoform 2 may possess an antiapoptotic effect and protect cells during normal cell survival through its regulation of caspases. {ECO:0000269|PubMed:16098192}.; . TISSUE SPECIFICITY: Ubiquitous with high expression in cervix, spleen and brain. Expressed in hematopoietic cells with increased expression in leukemia cells. Isoform 2 is highly expressed in spleen with almost no expression in muscle and brain. {ECO:0000269|PubMed:14557257, ECO:0000269|PubMed:16098192, ECO:0000269|PubMed:16956752}.; . . . . -2.53413058 0.890540222 . . ANKIB1 0.999885674650132 0.000114325347670046 2.19771618545104e-12 ankyrin repeat and IBR domain containing 1 FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin- conjugating enzymes and then transfers it to substrates. {ECO:0000250}.; . . ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;larynx;gum;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;bile duct;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; . 0.52768 . -0.732911333 14.07761264 2919.04971 10.25328 ANKK1 2.51117065910348e-08 0.275665420275128 0.724334554613165 ankyrin repeat and kinase domain containing 1 . . TISSUE SPECIFICITY: Highly expressed in brain and weakly expressed in placenta and spinal cord. {ECO:0000269|PubMed:14741327, ECO:0000269|PubMed:15146457}.; . . 0.06330 0.10965 3.852160142 99.64024534 2575.69309 9.49099 ANKLE1 8.12214719428193e-14 0.00484314836061271 0.995156851639306 ankyrin repeat and LEM domain containing 1 . . . . . 0.06468 0.09439 2.804006769 99.0504836 7647.36009 18.79705 ANKLE2 7.47280326815163e-07 0.975610221456584 0.0243890312630888 ankyrin repeat and LEM domain containing 2 FUNCTION: Involved in mitotic nuclear envelope reassembly by promoting dephosphorylation of BAF/BANF1 during mitotic exit. Coordinates the control of BAF/BANF1 dephosphorylation by inhibiting VRK1 kinase and promoting dephosphorylation of BAF/BANF1 by protein phosphatase 2A (PP2A), thereby facilitating nuclear envelope assembly. It is unclear whether it acts as a real PP2A regulatory subunit or whether it is involved in recruitment of the PP2A complex. {ECO:0000269|PubMed:22770216}.; . . medulla oblongata;ovary;salivary gland;sympathetic chain;colon;choroid;skin;bone marrow;uterus;prostate;endometrium;gum;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;hippocampus;alveolus;liver;head and neck;kidney;mammary gland; testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.31542 . -0.080831688 47.22222222 3708.58725 11.87863 ANKMY1 7.81266990643975e-14 0.119596137298066 0.880403862701856 ankyrin repeat and MYND domain containing 1 . . . unclassifiable (Anatomical System);medulla oblongata;pancreas;lung;endometrium;thyroid;placenta;testis;colon;germinal center;brain; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.08636 . -0.226073511 37.1255013 790.22098 5.54530 ANKMY2 0.00022375835823033 0.979569977949228 0.0202062636925419 ankyrin repeat and MYND domain containing 2 FUNCTION: May be involved in the trafficking of signaling proteins to the cilia. {ECO:0000250}.; . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;lens;bile duct;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;kidney;mammary gland;stomach;cerebellum; amygdala;occipital lobe;medulla oblongata;subthalamic nucleus;superior cervical ganglion;globus pallidus;pons;trigeminal ganglion;cingulate cortex;parietal lobe; 0.35783 . -0.023789244 52.09365416 388.32355 4.14991 ANKRA2 0.0035050375875932 0.952638872528775 0.0438560898836315 ankyrin repeat family A member 2 FUNCTION: May facilitate endocytosis by linking megalin to components of the cytoskeleton or endocytic machinery.; . . parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;pituitary gland;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;adrenal cortex;skeletal muscle;pancreas;lung;placenta;visual apparatus;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion; 0.39769 0.12080 -0.317668748 31.45789101 16.17323 0.57364 ANKRD1 0.000250275507071081 0.925671851159085 0.0740778733338437 ankyrin repeat domain 1 FUNCTION: May play an important role in endothelial cell activation. May act as a nuclear transcription factor that negatively regulates the expression of cardiac genes. Induction seems to be correlated with apoptotic cell death in hepatoma cells. {ECO:0000269|PubMed:15805281, ECO:0000269|PubMed:7730328}.; DISEASE: Total anomalous pulmonary venous return (TAPVR) [MIM:106700]: Rare congenital heart disease (CHD) in which the pulmonary veins fail to connect to the left atrium during cardiac development, draining instead into either the right atrium or one of its venous tributaries. This disease accounts for 1.5% of all CHDs and has a prevalence of approximately 1 out of 15'000 live births. {ECO:0000269|PubMed:18273862}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Mainly expressed in activated vascular endothelial cells. To a lower extent, also expressed in hepatoma cells. {ECO:0000269|PubMed:15805281, ECO:0000269|PubMed:7730328}.; . . 0.26452 0.15692 0.17280645 65.75843359 61.79565 1.60219 ANKRD2 1.00825852488919e-06 0.329151310813296 0.670847680928179 ankyrin repeat domain 2 FUNCTION: Functions as a negative regulator of myocyte differentiation. May interact with both sarcoplasmic structural proteins and nuclear proteins to regulate gene expression during muscle development and in response to muscle stress. {ECO:0000269|PubMed:21737686, ECO:0000269|PubMed:22016770}.; . TISSUE SPECIFICITY: Mostly expressed in skeletal and cardiac muscles. Found in slow fibers. Also expressed in kidney, but to a lower extent (at protein level). {ECO:0000269|PubMed:11444853, ECO:0000269|PubMed:11453652}.; unclassifiable (Anatomical System);breast;greater omentum;myocardium;prostate;lung;heart;muscle;kidney;skeletal muscle; heart;atrioventricular node;fetal thyroid;skeletal muscle; 0.31371 0.13116 -0.047654689 50.22410946 69.31311 1.72597 ANKRD6 3.48769137996221e-07 0.934423454746439 0.0655761964844227 ankyrin repeat domain 6 FUNCTION: Recruits CKI-epsilon to the beta-catenin degradation complex that consists of AXN1 or AXN2 and GSK3-beta and allows efficient phosphorylation of beta-catenin, thereby inhibiting beta-catenin/Tcf signals. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;skin;bone marrow;whole body;lung;cornea;larynx;visual apparatus;liver;testis;head and neck;kidney;spinal ganglion;brain;mammary gland; amygdala;dorsal root ganglion;superior cervical ganglion; 0.39801 0.11010 0.07167258 59.15899976 1603.80799 7.40851 ANKRD7 0.00752456912905973 0.925098241493659 0.0673771893772808 ankyrin repeat domain 7 . . TISSUE SPECIFICITY: Testis specific.; unclassifiable (Anatomical System);medulla oblongata;lung;bone;hippocampus;testis;kidney; testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.34853 . 0.747842143 86.47676339 12.30437 0.44629 ANKRD9 0.180354468492622 0.64511234552067 0.174533185986708 ankyrin repeat domain 9 . . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;fovea centralis;choroid;lens;skin;retina;optic nerve;lung;cornea;endometrium;bone;macula lutea;visual apparatus;liver;testis;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;temporal lobe;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.17935 . . . 12.43252 0.45121 ANKRD10 0.127073151881964 0.849809062924718 0.0231177851933185 ankyrin repeat domain 10 . . . lymphoreticular;smooth muscle;ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;placenta;head and neck;kidney;stomach;aorta;thymus;cerebellum; uterus;superior cervical ganglion;trigeminal ganglion; 0.53409 . 0.040529541 57.15380986 60.34636 1.57881 ANKRD10-IT1 . . . ANKRD10 intronic transcript 1 . . . . . . . . . . . ANKRD11 0.999999821632236 1.78367763587875e-07 6.47207458553239e-20 ankyrin repeat domain 11 FUNCTION: May recruit HDACs to the p160 coactivators/nuclear receptor complex to inhibit ligand-dependent transactivation.; DISEASE: KBG syndrome (KBGS) [MIM:148050]: A syndrome characterized by macrodontia of the upper central incisors, distinctive craniofacial findings, short stature, skeletal anomalies, and neurologic involvement that includes global developmental delay, seizures, and intellectual disability. {ECO:0000269|PubMed:21782149}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;urinary;blood;lens;breast;pancreas;lung;placenta;macula lutea;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;ciliary ganglion;atrioventricular node;cingulate cortex;parietal lobe; 0.24940 0.10736 -4.377281501 0.094361878 1162.32436 6.48860 ANKRD12 0.999985243734791 1.47562652090186e-05 1.24258766912771e-16 ankyrin repeat domain 12 FUNCTION: May recruit HDACs to the p160 coactivators/nuclear receptor complex to inhibit ligand-dependent transactivation.; . . medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;occipital lobe;white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.67410 0.10098 -0.110381106 45.36447275 2134.60639 8.49944 ANKRD13A 0.350624808697698 0.649352032411301 2.31588910001787e-05 ankyrin repeat domain 13A FUNCTION: Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Does not bind 'Lys-48'-linked ubiquitin. Positively regulates the internalization of ligand- activated EGFR by binding to the Ub moiety of ubiquitinated EGFR at the cell membrane. {ECO:0000269|PubMed:22298428}.; . . smooth muscle;ovary;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.44603 0.09264 -0.600630256 18.06440198 499.55841 4.58943 ANKRD13B 0.970860715744696 0.0291376181446374 1.66611066688686e-06 ankyrin repeat domain 13B FUNCTION: Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Does not bind 'Lys-48'-linked ubiquitin. Positively regulates the internalization of ligand- activated EGFR by binding to the Ub moiety of ubiquitinated EGFR at the cell membrane. {ECO:0000269|PubMed:22298428}.; . . . . 0.61211 0.11059 -0.758599262 13.32861524 35.96275 1.07969 ANKRD13C 0.999095558403675 0.000904439920126964 1.67619805177179e-09 ankyrin repeat domain 13C FUNCTION: Acts as a molecular chaperone for G protein-coupled receptors, regulating their biogenesis and exit from the ER. {ECO:0000269|PubMed:20959461}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;vein;skeletal muscle;uterus;lung;endometrium;bone;thyroid;placenta;visual apparatus;hippocampus;liver;testis;germinal center;brain;bladder;mammary gland; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.53203 . -0.404032746 26.53338051 19.53373 0.66999 ANKRD13D 0.984538263546097 0.0154600128354109 1.72361849191652e-06 ankyrin repeat domain 13 family member D FUNCTION: Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Does not bind 'Lys-48'-linked ubiquitin. Positively regulates the internalization of ligand- activated EGFR by binding to the Ub moiety of ubiquitinated EGFR at the cell membrane. {ECO:0000269|PubMed:22298428}.; . . smooth muscle;ovary;colon;fovea centralis;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;urinary;blood;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;cervix;kidney;aorta;thymus; . 0.12259 0.10410 -0.977252525 8.799245105 40.07568 1.17789 ANKRD16 2.5777043745873e-06 0.505168379044095 0.49482904325153 ankyrin repeat domain 16 . . . unclassifiable (Anatomical System);bile duct;prostate;cartilage;islets of Langerhans;hippocampus;urinary;brain; superior cervical ganglion;atrioventricular node;parietal lobe; 0.09505 . 0.707379532 85.62750649 1385.5909 6.96821 ANKRD17 0.999999999649327 3.50673240600117e-10 8.17695011907454e-26 ankyrin repeat domain 17 FUNCTION: Could play pivotal roles in cell cycle and DNA regulation (PubMed:19150984). Involved in innate immune defense against viruse by positively regulating the viral dsRNA receptors DDX58 and IFIH1 signaling pathways (PubMed:22328336). Involves in NOD2- and NOD1-mediated responses to bacteria suggesting a role in innate antibacterial immune pathways too (PubMed:23711367). Target of enterovirus 71 which is the major etiological agent of HFMD (hand, foot and mouth disease) (PubMed:17276651). Could play a central role for the formation and/or maintenance of the blood vessels of the circulation system (By similarity). {ECO:0000250|UniProtKB:Q99NH0, ECO:0000269|PubMed:17276651, ECO:0000269|PubMed:19150984, ECO:0000269|PubMed:22328336, ECO:0000269|PubMed:23711367}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:17276651, ECO:0000269|PubMed:19150984}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;ciliary body;heart;cartilage;pharynx;blood;lens;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;pons;atrioventricular node;skin;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.30304 . -2.938435282 0.548478415 117.58974 2.35717 ANKRD18A 0.000945591321948718 0.578001567064323 0.421052841613728 ankyrin repeat domain 18A . . . prostate;frontal lobe;islets of Langerhans;testis;colon;brain;stomach; . 0.01878 . 2.704844505 98.90894079 4407.02172 13.26594 ANKRD18B 0.00748014663853119 0.774603155611951 0.217916697749518 ankyrin repeat domain 18B . . . unclassifiable (Anatomical System);uterus;prostate;islets of Langerhans; . 0.02598 . . . 890.38818 5.81376 ANKRD18CP . . . ankyrin repeat domain 18C, pseudogene . . . unclassifiable (Anatomical System);uterus;prostate;islets of Langerhans; . 0.02598 . . . . . ANKRD18DP . . . ankyrin repeat domain 18D, pseudogene . . . testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;trigeminal ganglion; . . . . . . ANKRD18EP . . . ankyrin repeat domain 18E, pseudogene . . . . . . . . . . . ANKRD19P . . . ankyrin repeat domain 19, pseudogene . . . unclassifiable (Anatomical System);pancreas;ovary; . 0.14222 0.08931 . . . . ANKRD20A1 0.864283491882154 0.13374796968115 0.00196853843669599 ankyrin repeat domain 20 family member A1 . . . . . . . . . 1008.82222 6.11715 ANKRD20A2 0.118527454191844 0.606782665700419 0.274689880107737 ankyrin repeat domain 20 family member A2 . . . . . . . . . 229.66451 3.27442 ANKRD20A3 . . . ankyrin repeat domain 20 family member A3 . . . unclassifiable (Anatomical System);uterus;pancreas;lymph node;lung;frontal lobe;ovary;placenta;testis;spleen;germinal center;skeletal muscle; . . . . . 1.01398 0.02561 ANKRD20A4 0.319603989806576 0.663749782087053 0.0166462281063708 ankyrin repeat domain 20 family member A4 . . . unclassifiable (Anatomical System);germinal center; . . . . . 292.93973 3.65858 ANKRD20A5P . . . ankyrin repeat domain 20 family member A5, pseudogene . . . . . . . . . . . ANKRD20A6P . . . ankyrin repeat domain 20 family member A6, pseudogene . . . . . . . . . . . ANKRD20A7P . . . ankyrin repeat domain 20 family member A7, pseudogene . . . . . . . . . . . ANKRD20A8P . . . ankyrin repeat domain 20 family member A8, pseudogene . . . . . . . . . . . ANKRD20A9P . . . ankyrin repeat domain 20 family member A9, pseudogene . . . . . . . . . . . ANKRD20A10P . . . ankyrin repeat domain 20 family member A10, pseudogene . . . . . . . . . . . ANKRD20A11P . . . ankyrin repeat domain 20 family member A11, pseudogene . . . testis; . 0.00688 . . . . . ANKRD20A12P . . . ankyrin repeat domain 20 family member A12, pseudogene . . . . . . . . . . . ANKRD20A13P . . . ankyrin repeat domain 20 family member A13, pseudogene . . . . . . . . . . . ANKRD20A14P . . . ankyrin repeat domain 20 family member A14, pseudogene . . . . . . . . . . . ANKRD20A15P . . . ankyrin repeat domain 20 family member A15, pseudogene . . . . . . . . . . . ANKRD20A16P . . . ankyrin repeat domain 20 family member A16, pseudogene . . . . . . . . . . . ANKRD20A17P . . . ankyrin repeat domain 20 family member A17, pseudogene . . . . . . . . . . . ANKRD20A18P . . . ankyrin repeat domain 20 family member A18, pseudogene . . . testis; subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . . . . . ANKRD20A19P . . . ankyrin repeat domain 20 family member A19, pseudogene . . . . . . . . . . . ANKRD20A20P . . . ankyrin repeat domain 20 family member A20, pseudogene . . . . . . . . . . . ANKRD22 2.03180312966558e-05 0.471876374074693 0.52810330789401 ankyrin repeat domain 22 . . . . . 0.26948 . 0.681699246 84.93158764 877.65555 5.76911 ANKRD23 8.66315090908555e-16 0.000643188247169456 0.99935681175283 ankyrin repeat domain 23 FUNCTION: May be involved in the energy metabolism. Could be a molecular link between myofibrillar stretch-induced signaling pathways and muscle gene expression.; . TISSUE SPECIFICITY: Mainly expressed in heart, skeletal muscle and brown adipose tissues. {ECO:0000269|PubMed:12456686}.; unclassifiable (Anatomical System);heart;tongue;muscle;skin;skeletal muscle;greater omentum;uterus;pancreas;prostate;lung;larynx;testis;head and neck;peripheral nerve; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.13854 0.11770 0.128714042 63.19886766 249.09183 3.40036 ANKRD24 1.87439154445724e-06 0.993195817007332 0.00680230860112326 ankyrin repeat domain 24 . . . frontal lobe;placenta;stomach; subthalamic nucleus;superior cervical ganglion;medulla oblongata;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08458 0.08226 1.877664966 97.22811984 2701.83295 9.78513 ANKRD26 7.08727863800569e-15 0.999440089149152 0.000559910850840408 ankyrin repeat domain 26 . . . . . 0.32245 0.10156 2.151528517 97.98301486 2539.26757 9.40883 ANKRD26P1 . . . ankyrin repeat domain 26 pseudogene 1 . . . . . . . . . . . ANKRD26P2 . . . ankyrin repeat domain 26 pseudogene 2 . . . . . . . . . . . ANKRD26P3 . . . ankyrin repeat domain 26 pseudogene 3 . . . . . . . . . . . ANKRD26P4 . . . ankyrin repeat domain 26 pseudogene 4 . . . . . . . . . . . ANKRD27 7.78948328153526e-16 0.577251658708205 0.422748341291794 ankyrin repeat domain 27 FUNCTION: May be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and regulate endosome dynamics (PubMed:16525121, PubMed:18477474). May regulate the participation of VAMP7 in membrane fusion events; in vitro inhibits VAMP7-mediated SNARE complex formation by trapping VAMP7 in a closed, fusogenically inactive conformation (PubMed:23104059). Involved in peripheral melanosomal distribution of TYRP1 in melanocytes; the function, which probably is implicating vesicle-trafficking, includes cooperation with Rab32, Rab38 and VAMP7 (By similarity). Involved in the regulation of neurite growth; the function seems to require its GEF activity, probably towards Rab21, and VAMP7 but not Rab32/38 (By similarity). Proposed to be involved in Golgi sorting of VAMP7 and transport of VAMP7 vesicles to the cell surface; the function seems to implicate kinesin heavy chain isoform 5 proteins, GOLGA4, RAB21 and MACF1 (PubMed:22705394). Required for the colocalization of VAMP7 and Rab21, probably on TGN sites (PubMed:19745841). Involved in GLUT1 endosome-to-plasma membrane trafficking; the function is dependent of association with VPS29 (PubMed:24856514). {ECO:0000250|UniProtKB:Q3UMR0, ECO:0000269|PubMed:23104059, ECO:0000269|PubMed:24856514, ECO:0000305|PubMed:16525121, ECO:0000305|PubMed:18477474, ECO:0000305|PubMed:22705394}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; . 0.60087 0.10353 -1.563550352 3.208303845 1770.79593 7.77308 ANKRD28 0.99992881046712 7.11895321866021e-05 6.93155095351262e-13 ankyrin repeat domain 28 FUNCTION: Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. Selectively inhibits the phosphatase activity of PPP1C. Targets PPP1C to modulate HNRPK phosphorylation. {ECO:0000269|PubMed:16564677, ECO:0000269|PubMed:18186651}.; . . . . 0.35162 0.09683 -0.797234383 12.48525596 219.64528 3.20606 ANKRD29 2.59982243312639e-05 0.760279745204692 0.239694256570977 ankyrin repeat domain 29 . . . unclassifiable (Anatomical System);lymph node;heart;ovary;hypothalamus;colon;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;prostate;optic nerve;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;testis;kidney;brain; medulla oblongata;superior cervical ganglion; 0.08975 0.07399 -0.381986487 27.68931352 36.12232 1.08425 ANKRD30A 1.26066166278999e-23 0.00398767928660609 0.996012320713394 ankyrin repeat domain 30A . . TISSUE SPECIFICITY: Mainly expressed in breast and testis. A very faint signal is detected in placenta. Also expressed in many breast cancer cells. {ECO:0000269|PubMed:11280766}.; breast;lung;liver;testis;spleen; testis - interstitial;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.05405 . 2.702925512 98.90304317 3097.8543 10.58328 ANKRD30B 1.4946934567636e-09 0.942883690005466 0.0571163084998401 ankyrin repeat domain 30B . . TISSUE SPECIFICITY: Expressed in brain, breast and testis. {ECO:0000269|PubMed:11280766}.; breast;unclassifiable (Anatomical System);lung;thyroid;liver;testis;spleen; . . . 1.06196211 91.507431 2417.32649 9.13836 ANKRD30BL . . . ankyrin repeat domain 30B-like . . . lung;testis; . . . . . 119.69689 2.38131 ANKRD30BP1 . . . ankyrin repeat domain 30B pseudogene 1 . . . thyroid; . . . . . . . ANKRD30BP2 . . . ankyrin repeat domain 30B pseudogene 2 . . . . . . . . . . . ANKRD30BP3 . . . ankyrin repeat domain 30B pseudogene 3 . . . . . . . . . . . ANKRD31 . . . ankyrin repeat domain 31 . . . . . 0.12894 . . . 3232.48321 10.82883 ANKRD33 1.96179306102665e-14 0.00209850634668942 0.997901493653291 ankyrin repeat domain 33 . . . optic nerve;ovary;placenta;macula lutea;parathyroid;fovea centralis;choroid;lens;retina; atrioventricular node; 0.10423 . 1.111513261 92.07360226 5715.26433 15.67869 ANKRD33B . . . ankyrin repeat domain 33B . . . . . . . . . 245.21895 3.37855 ANKRD33B-AS1 . . . ANKRD33B antisense RNA 1 . . . . . . . . . . . ANKRD34A 0.974591387104345 0.0253797021685812 2.89107270739566e-05 ankyrin repeat domain 34A . . . colon;choroid;fovea centralis;lens;retina;prostate;optic nerve;lung;bone;hippocampus;macula lutea;testis;brain; whole brain;amygdala;subthalamic nucleus;globus pallidus;cingulate cortex;cerebellum; 0.13979 . -0.494039303 22.09247464 13.82839 0.50202 ANKRD34B 2.52690094900488e-09 0.021694857509744 0.978305139963355 ankyrin repeat domain 34B . . . hypothalamus; . 0.30745 0.09306 0.332586472 73.61405992 118.44783 2.36788 ANKRD34C . . . ankyrin repeat domain 34C . . . . . . . 0.12325821 62.38499646 68.51931 1.71310 ANKRD34C-AS1 . . . ANKRD34C antisense RNA 1 . . . . . . . . . . . ANKRD35 4.67636131494537e-13 0.754644989753669 0.245355010245863 ankyrin repeat domain 35 . . . unclassifiable (Anatomical System);medulla oblongata;cartilage;lens;skeletal muscle;skin;retina;uterus;lung;oesophagus;placenta;thyroid;bone;brain; superior cervical ganglion;atrioventricular node;trigeminal ganglion;bone marrow; 0.17231 . 0.878111845 88.89478651 3525.04577 11.44886 ANKRD36 2.11660484589104e-19 0.0863629312463256 0.913637068753674 ankyrin repeat domain 36 . . . smooth muscle;colon;choroid;fovea centralis;retina;uterus;prostate;whole body;optic nerve;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;tongue;lens;skeletal muscle;pancreas;nasopharynx;visual apparatus;macula lutea;liver;head and neck;kidney;stomach; . . . . . 4272.72254 12.99655 ANKRD36B . . . ankyrin repeat domain 36B . . . smooth muscle;colon;choroid;fovea centralis;retina;uterus;prostate;whole body;optic nerve;pituitary gland;testis;germinal center;brain;artery;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;nasopharynx;placenta;visual apparatus;macula lutea;liver;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; . 0.28221 . . . . . ANKRD36BP1 . . . ankyrin repeat domain 36B pseudogene 1 . . . unclassifiable (Anatomical System);heart;tongue;colon;skeletal muscle;breast;uterus;pancreas;prostate;placenta;pituitary gland;liver;testis;head and neck;germinal center;brain;mammary gland;artery;aorta;stomach; . . . . . . . ANKRD36BP2 . . . ankyrin repeat domain 36B pseudogene 2 . . . . . . . . . . . ANKRD36C . . . ankyrin repeat domain 36C . . . unclassifiable (Anatomical System);lymph node;colon;skeletal muscle;retina;breast;uterus;prostate;whole body;lung;cornea;endometrium;larynx;nasopharynx;liver;testis;head and neck;germinal center;kidney;pineal gland;mammary gland;stomach; . . . . . 2676.37542 9.72635 ANKRD36P1 . . . ankyrin repeat domain 36 pseudogene 1 . . . bone; . . . . . . . ANKRD37 0.00570485150514028 0.722717532162444 0.271577616332416 ankyrin repeat domain 37 . . TISSUE SPECIFICITY: Mainly expressed in testis, small intestine, colon, blood leukocytes and in pancreatic adenocarcinoma cells. {ECO:0000269|PubMed:15809689}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;bone;testis;amniotic fluid;germinal center;spinal ganglion;brain;artery;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;spleen;kidney;mammary gland;stomach;aorta; . 0.07995 . 0.503505267 79.88912479 188.93239 2.98462 ANKRD39 0.0573082907278283 0.866618945186791 0.0760727640853805 ankyrin repeat domain 39 . . . . . 0.26675 . -0.139478553 43.29440906 19.05397 0.65808 ANKRD40 0.313648021576856 0.682646589091873 0.00370538933127153 ankyrin repeat domain 40 . . . colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;cervix;spleen;kidney;mammary gland;stomach; cerebellum peduncles; 0.15849 . -0.095386216 46.48502005 487.52925 4.54494 ANKRD42 2.60039143890093e-08 0.280607543353494 0.719392430642592 ankyrin repeat domain 42 . . . unclassifiable (Anatomical System);prostate;pancreas;lung;cartilage;islets of Langerhans;thyroid;hippocampus;testis;spleen; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14777 0.10447 0.062575634 58.74026893 98.9949 2.15376 ANKRD44 0.775902811645404 0.223767559326481 0.000329629028114741 ankyrin repeat domain 44 FUNCTION: Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates.; . . unclassifiable (Anatomical System);lymph node;skeletal muscle;skin;breast;lung;cerebral cortex;nasopharynx;liver;testis;spleen;germinal center;kidney;brain;stomach; . 0.35969 0.10832 -0.381986487 27.68931352 320.06038 3.80060 ANKRD44-IT1 . . . ANKRD44 intronic transcript 1 . . . . . . . . . . . ANKRD45 0.0198872747296348 0.902459795459516 0.0776529298108492 ankyrin repeat domain 45 . . . unclassifiable (Anatomical System);medulla oblongata;lung;islets of Langerhans;hypothalamus;testis;brain; superior cervical ganglion;subthalamic nucleus;globus pallidus;trigeminal ganglion;skeletal muscle; 0.13076 0.09469 0.659651797 84.35362114 179.66642 2.91064 ANKRD46 0.918715846360714 0.0807565049546509 0.000527648684634729 ankyrin repeat domain 46 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;urinary;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;stomach;aorta;peripheral nerve; dorsal root ganglion;amygdala;superior cervical ganglion;medulla oblongata;thalamus;occipital lobe;hypothalamus;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus; 0.13873 0.09029 0.125076652 62.7388535 317.28556 3.78200 ANKRD49 0.173264896104373 0.769295168090264 0.0574399358053626 ankyrin repeat domain 49 FUNCTION: Induces HBG1 expression (PubMed:16131492, PubMed:11162141). May have a role in spermatogenesis where it promotes autophagy in response to serum starvation, via the NF- kappaB pathway (By similarity). {ECO:0000250|UniProtKB:Q8VE42, ECO:0000269|PubMed:11162141, ECO:0000269|PubMed:16131492}.; . TISSUE SPECIFICITY: Widely expressed in fetus, at a high level in fetal liver, brain and lung. {ECO:0000269|PubMed:11162141}.; ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;adrenal cortex;pharynx;blood;skeletal muscle;bile duct;breast;lung;adrenal gland;placenta;visual apparatus;liver;kidney;stomach;thymus; white blood cells; 0.15040 0.11237 -0.229483771 36.86010852 11.19806 0.40441 ANKRD50 0.918119608798956 0.0818803537108341 3.74902103322079e-08 ankyrin repeat domain 50 FUNCTION: Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1 (PubMed:25278552).; . . . . 0.08479 0.10870 -1.74358502 2.394432649 169.32935 2.83875 ANKRD52 0.999987966825373 1.20331745817893e-05 4.50977450091289e-14 ankyrin repeat domain 52 FUNCTION: Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates.; . . unclassifiable (Anatomical System);heart;ovary;muscle;colon;blood;parathyroid;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;breast;prostate;optic nerve;placenta;bone;macula lutea;visual apparatus;testis;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.79153 . -0.909290275 10.03184713 158.3001 2.74876 ANKRD53 0.000455607586717175 0.86735492933264 0.132189463080642 ankyrin repeat domain 53 . . . medulla oblongata;heart;cartilage;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;placenta;macula lutea;visual apparatus;testis;brain; . 0.06661 0.09362 1.26585432 93.59518754 1459.41609 7.12227 ANKRD54 0.0153084731551182 0.958216275634215 0.026475251210667 ankyrin repeat domain 54 FUNCTION: Plays an important role in regulating intracellular signaling events associated with erythroid terminal differentiation. {ECO:0000250}.; . . colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;cerebellum cortex;hypothalamus;muscle;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.16020 0.11262 . . 23.55316 0.78232 ANKRD54P1 . . . ankyrin repeat domain 54 pseudogene 1 . . . . . . . . . . . ANKRD55 2.4350104791824e-07 0.899803593421729 0.100196163077223 ankyrin repeat domain 55 . . . unclassifiable (Anatomical System);medulla oblongata;lung;placenta;liver;testis;spleen;head and neck;brain;skeletal muscle; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.10140 . 0.158037129 64.85020052 148.38001 2.65527 ANKRD57P1 . . . ankyrin repeat domain 57 pseudogene 1 . . . . . . . . . . . ANKRD60 . . . ankyrin repeat domain 60 . . . . . 0.05768 . . . 1707.98349 7.62022 ANKRD61 . . . ankyrin repeat domain 61 . . . . . . . . . 3317.81737 11.00993 ANKRD62 0.458132580584637 0.448539344631583 0.0933280747837801 ankyrin repeat domain 62 . . . unclassifiable (Anatomical System); superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion; . . . . 84.93054 1.96330 ANKRD62P1 . . . ankyrin repeat domain 62 pseudogene 1 . . . unclassifiable (Anatomical System); . . . . . . . ANKRD62P1-PARP4P3 . . . ANKRD62P1-PARP4P3 readthrough, transcribed pseudogene . . . . . . . . . . . ANKRD63 . . . ankyrin repeat domain 63 . . . . . . . . . 104.72601 2.21176 ANKRD65 . . . ankyrin repeat domain 65 . . . . . . . . . 2410.25308 9.11656 ANKRD66 . . . ankyrin repeat domain 66 . . . . . . . . . 891.09073 5.81800 ANKS1A 0.84685967793139 0.153140282920134 3.91484761176882e-08 ankyrin repeat and sterile alpha motif domain containing 1A FUNCTION: Regulator of different signaling pathways. Regulates EPHA8 receptor tyrosine kinase signaling to control cell migration and neurite retraction (By similarity). {ECO:0000250, ECO:0000269|PubMed:17875921}.; . TISSUE SPECIFICITY: Widely expressed (at protein level).; ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;adrenal cortex;pharynx;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; dorsal root ganglion;superior cervical ganglion;olfactory bulb;placenta;testis;atrioventricular node; 0.44722 0.11641 -1.254821849 5.355036565 700.58074 5.26551 ANKS1B 0.992771667778122 0.00722833213120767 9.0669819455964e-11 ankyrin repeat and sterile alpha motif domain containing 1B FUNCTION: Isoform 2 may participate in the regulation of nucleoplasmic coilin protein interactions in neuronal and transformed cells.; FUNCTION: Isoform 4 may play a role as a modulator of APP processing. Overexpression can down-regulate APP processing.; . TISSUE SPECIFICITY: Highly expressed in marrow from patients with pre-B ALL associated with the t(1;19) translocation. Strongly expressed in brain and testis. Expressed in fetal brain. Isoform 4 is highly expressed in brain (at protein level). Isoform 6 is expressed in brain and several cancer cell lines. {ECO:0000269|PubMed:10490826, ECO:0000269|PubMed:15347684}.; unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;hypothalamus;sympathetic chain;blood;choroid;skin;bone marrow;breast;uterus;lung;frontal lobe;cochlea;hippocampus;testis;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21201 0.20962 -1.216154 5.667610285 347.70248 3.95239 ANKS3 0.0123556103986193 0.987323467885526 0.00032092171585497 ankyrin repeat and sterile alpha motif domain containing 3 . . . unclassifiable (Anatomical System);lymph node;islets of Langerhans;salivary gland;colon;pancreas;prostate;optic nerve;lung;frontal lobe;oesophagus;endometrium;bone;placenta;visual apparatus;testis;kidney;brain;stomach; . 0.06247 0.09911 0.009173042 54.15782024 413.22725 4.25569 ANKS4B 3.41490609436488e-06 0.195987577016088 0.804009008077817 ankyrin repeat and sterile alpha motif domain containing 4B . . TISSUE SPECIFICITY: Expressed in kidney and small intestine. {ECO:0000269|PubMed:12588794}.; unclassifiable (Anatomical System);colon; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.28311 0.08980 0.17280645 65.75843359 131.04319 2.49340 ANKS6 0.000273308458823526 0.996527811361501 0.00319888017967496 ankyrin repeat and sterile alpha motif domain containing 6 FUNCTION: Required for renal function. {ECO:0000269|PubMed:23793029}.; DISEASE: Nephronophthisis 16 (NPHP16) [MIM:615382]: A form of nephronophthisis, a chronic tubulo-interstitial nephritis that progresses to end-stage renal failure. Some patients have cystic kidneys of normal size and no extrarenal manifestations, whereas others have enlarged renal size and severe extrarenal defects, including hypertrophic obstructive cardiomyopathy, aortic stenosis, pulmonary stenosis, patent ductus arteriosus, situs inversus, and periportal liver fibrosis. {ECO:0000269|PubMed:23793029}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;ovary;heart;sympathetic chain;adrenal cortex;colon;parathyroid;blood;lens;skin;breast;uterus;pancreas;prostate;whole body;lung;bone;placenta;liver;testis;cervix;spleen;kidney;brain;mammary gland;stomach; . 0.13402 0.10372 -0.347208386 29.59424393 237.30571 3.32569 ANKUB1 . . . ankyrin repeat and ubiquitin domain containing 1 . . . . . 0.36605 . . . 610.65036 4.99423 ANKZF1 4.83243050013918e-14 0.303827131864325 0.696172868135627 ankyrin repeat and zinc finger domain containing 1 FUNCTION: Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway. {ECO:0000250}.; . . ovary;sympathetic chain;colon;skin;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;gum;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;trigeminal ganglion; 0.32333 0.07466 0.606246644 82.93229535 979.91713 6.04331 ANLN 0.923521451884595 0.0764785468264311 1.28897423006887e-09 anillin actin binding protein FUNCTION: Required for cytokinesis (PubMed:16040610). Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. May play a significant role in podocyte cell migration (PubMed:24676636). {ECO:0000269|PubMed:10931866, ECO:0000269|PubMed:12479805, ECO:0000269|PubMed:15496454, ECO:0000269|PubMed:16040610, ECO:0000269|PubMed:16357138, ECO:0000269|PubMed:24676636}.; DISEASE: Focal segmental glomerulosclerosis 8 (FSGS8) [MIM:616032]: A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation. {ECO:0000269|PubMed:24676636}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. Present at highest levels in the brain, at high levels in the placenta and testis, at intermediate levels in the intestine, ovary, skeletal muscle and thymus and at lower levels in heart, kidney, liver, lung, pancreas, prostate and spleen. In the kidney, it is widely expressed in tubules, but sparsely expressed in the glomerulus (PubMed:24676636). Expression is significantly increased in renal biopsy specimens from idiopathic FSGS (PubMed:24676636). Overexpressed in many tumor types including breast, colorectal, endometrial, hepatic, kidney, lung, ovarian and pancreatic tumors. {ECO:0000269|PubMed:16203764, ECO:0000269|PubMed:24676636}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;prostate;frontal lobe;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;pharynx;blood;skeletal muscle;breast;bile duct;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach;thymus; occipital lobe;medulla oblongata;hypothalamus;prefrontal cortex;parietal lobe; 0.52557 0.15234 -1.146380093 6.334041047 5386.34454 15.13898 ANO1 0.993084640132559 0.00691535946532664 4.02114859641631e-10 anoctamin 1 FUNCTION: Calcium-activated chloride channel (CaCC) which plays a role in transepithelial anion transport and smooth muscle contraction. Required for the normal functioning of the interstitial cells of Cajal (ICCs) which generate electrical pacemaker activity in gastrointestinal smooth muscles. Acts as a major contributor to basal and stimulated chloride conductance in airway epithelial cells and plays an important role in tracheal cartilage development. {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:21984732, ECO:0000269|PubMed:22178883, ECO:0000269|PubMed:22946059}.; . TISSUE SPECIFICITY: Broadly expressed with higher levels in liver, skeletal muscle and gastrointestinal muscles. {ECO:0000269|PubMed:15215166, ECO:0000269|PubMed:16906560}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;colon;parathyroid;breast;uterus;bile duct;prostate;pancreas;lung;endometrium;larynx;placenta;hypopharynx;liver;testis;head and neck;kidney;brain;mammary gland;artery;aorta;stomach; superior cervical ganglion; 0.29465 0.12257 -1.521247944 3.44420854 826.58674 5.63458 ANO1-AS1 . . . ANO1 antisense RNA 1 . . . . . . . . . . . ANO1-AS2 . . . ANO1 antisense RNA 2 (head to head) . . . . . . . . . . . ANO2 2.8480469622138e-18 0.106663921929168 0.893336078070832 anoctamin 2 FUNCTION: Calcium-activated chloride channel (CaCC) which may play a role in olfactory signal transduction. Odorant molecules bind to odor-sensing receptors (OSRs), leading to an increase in calcium entry that activates CaCC current which amplifies the depolarization of the OSR cells, ANO2 seems to be the underlying chloride channel involved in this process. May mediate light perception amplification in retina. {ECO:0000269|PubMed:19474308, ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:21890523, ECO:0000269|PubMed:21984732}.; . TISSUE SPECIFICITY: Retina, especially in the photoreceptor synaptic terminals. {ECO:0000269|PubMed:19474308}.; ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;endometrium;larynx;testis;pineal gland;artery;brain;unclassifiable (Anatomical System);lymph node;cartilage;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion; 0.23624 . -0.341759628 29.62962963 1740.1693 7.69925 ANO3 4.08913851953925e-13 0.995164804377118 0.00483519562247272 anoctamin 3 FUNCTION: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylcholine and galactosylceramide. Seems to act as potassium channel regulator and may inhibit pain signaling; can facilitate KCNT1/Slack channel activity by promoting its full single-channel conductance at very low sodium concentrations and by increasing its sodium sensitivity (By similarity). Does not exhibit calcium-activated chloride channel (CaCC) activity. {ECO:0000250|UniProtKB:A2AHL1, ECO:0000269|PubMed:21984732}.; . TISSUE SPECIFICITY: Highly expressed in the forebrain striatum. {ECO:0000269|PubMed:23200863}.; unclassifiable (Anatomical System);amygdala;uterus;lung;placenta;hippocampus;testis;brain;thymus; amygdala;occipital lobe;subthalamic nucleus;superior cervical ganglion;medulla oblongata;temporal lobe;prefrontal cortex;caudate nucleus;pons;parietal lobe; 0.28055 0.12864 -1.352082458 4.582448691 54.45516 1.47467 ANO4 0.844044636742629 0.155955362916701 3.40670546069189e-10 anoctamin 4 FUNCTION: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide. Does not exhibit calcium-activated chloride channel (CaCC) activity. {ECO:0000250|UniProtKB:Q8C5H1}.; . . unclassifiable (Anatomical System);heart;ovary;parathyroid;skin;uterus;prostate;lung;placenta;liver;pituitary gland;testis;spleen;kidney;brain; superior cervical ganglion;atrioventricular node; 0.33900 0.13272 -0.777005578 12.9747582 1079.9216 6.30080 ANO5 9.89423115964736e-16 0.629566310679112 0.370433689320887 anoctamin 5 FUNCTION: Does not exhibit calcium-activated chloride channel (CaCC) activity.; DISEASE: Limb-girdle muscular dystrophy 2L (LGMD2L) [MIM:611307]: An autosomal recessive degenerative myopathy characterized by proximal weakness, weakness of the hip and shoulder girdles and prominent asymmetrical quadriceps femoris and biceps brachii atrophy. {ECO:0000269|PubMed:20096397}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Miyoshi muscular dystrophy 3 (MMD3) [MIM:613319]: A late- onset muscular dystrophy characterized by distal muscle weakness of the lower limbs, calf muscle discomfort and weakness, quadriceps atrophy. Muscle weakness and atrophy may be asymmetric. {ECO:0000269|PubMed:20096397, ECO:0000269|PubMed:22499103}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney, lung, and skeletal muscle. Weakly expressed in bone marrow, fetal liver, placenta, spleen, thymus, osteoblasts and periodontal ligament cells. {ECO:0000269|PubMed:15067359, ECO:0000269|PubMed:15124103}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;parathyroid;skin;skeletal muscle;retina;prostate;whole body;lung;cochlea;endometrium;placenta;visual apparatus;liver;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;cerebellum; 0.11025 0.11663 0.584200036 82.336636 354.17365 3.98229 ANO6 4.52445486156544e-20 0.0355624933443801 0.96443750665562 anoctamin 6 FUNCTION: Small-conductance calcium-activated nonselective cation (SCAN) channel which acts as a regulator of phospholipid scrambling in platelets and osteoblasts. Phospholipid scrambling results in surface exposure of phosphatidylserine which in platelets is essential to trigger the clotting system whereas in osteoblasts is essential for the deposition of hydroxyapatite during bone mineralization. Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide (By similarity). Can generate outwardly rectifying chloride channel currents in airway epithelial cells and Jurkat T lymphocytes. {ECO:0000250|UniProtKB:Q6P9J9, ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:21107324, ECO:0000269|PubMed:21908539, ECO:0000269|PubMed:22006324, ECO:0000269|PubMed:22946059}.; . TISSUE SPECIFICITY: Expressed in embryonic stem cell, fetal liver, retina, chronic myologenous leukemia and intestinal cancer. {ECO:0000269|PubMed:15067359}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;spleen;kidney;aorta;stomach;thymus; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18671 . -0.08265057 47.20452937 619.32231 5.02026 ANO7 1.87089456161351e-30 1.92980212804542e-05 0.99998070197872 anoctamin 7 FUNCTION: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide (By similarity). Does not exhibit calcium- activated chloride channel (CaCC) activity. May play a role in cell-cell interactions. {ECO:0000250|UniProtKB:Q14AT5, ECO:0000269|PubMed:17308099}.; . TISSUE SPECIFICITY: Specifically expressed in epithelial cells of the prostate (at protein level). {ECO:0000269|PubMed:14981236, ECO:0000269|PubMed:15761874, ECO:0000269|PubMed:17308099}.; unclassifiable (Anatomical System);medulla oblongata;prostate;lung;bone;placenta;liver;colon;spleen;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;occipital lobe;subthalamic nucleus;superior cervical ganglion;prostate;fetal liver;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10367 0.10570 0.268088483 70.58858221 3536.57926 11.46750 ANO7P1 . . . anoctamin 7 pseudogene 1 . . . . . . . . . . . ANO8 0.99293631682763 0.00706368107921519 2.09315474680186e-09 anoctamin 8 FUNCTION: Does not exhibit calcium-activated chloride channel (CaCC) activity.; . TISSUE SPECIFICITY: Expressed in embryonic stem cells, fetal brain and neural tissues. {ECO:0000269|PubMed:15647853}.; unclassifiable (Anatomical System);adrenal cortex;colon;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;optic nerve;lung;frontal lobe;endometrium;bone;macula lutea;visual apparatus;liver;spleen;germinal center;kidney;brain;mammary gland;peripheral nerve; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.23425 0.09396 -1.42004951 4.104741684 373.43185 4.07663 ANO9 4.59377788263046e-11 0.780774475648772 0.21922552430529 anoctamin 9 FUNCTION: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide (By similarity). Does not exhibit calcium- activated chloride channel (CaCC) activity. Can inhibit the activity of ANO1. {ECO:0000250|UniProtKB:P86044, ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}.; . . unclassifiable (Anatomical System);lymph node;heart;ovary;colon;blood;skin;uterus;optic nerve;lung;endometrium;thyroid;liver;pituitary gland;testis;stomach;thymus; . 0.09289 0.09691 -0.257204135 34.97876858 382.46252 4.12286 ANO10 1.92259540732638e-06 0.880526515938814 0.119471561465778 anoctamin 10 FUNCTION: Does not exhibit calcium-activated chloride channel (CaCC) activity. Can inhibit the activity of ANO1. {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}.; . TISSUE SPECIFICITY: Highly expressed in the brain. Intermediate levels in the retina and heart and low levels in the placenta, liver, lung, duodenum, kidney, testis and spleen. In brain areas, highest expression in the frontal and occipital cortices and in the cerebellum. Lower expression in the fetal brain than in the adult brain. {ECO:0000269|PubMed:21092923}.; ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;oesophagus;endometrium;bone;thyroid;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; whole brain;superior cervical ganglion;testis - interstitial;kidney; 0.13961 0.09565 0.957177419 90.14508139 912.19278 5.87260 ANOP1 . . . anophthalmos 1 (with mental retardation, without limb anomalies or dental or urogenital abnormalities) . . . . . . . . . . . ANOS1 . . . anosmin 1 FUNCTION: Has a dual branch-promoting and guidance activity, which may play an important role in the patterning of mitral and tufted cell collaterals to the olfactory cortex (By similarity). Chemoattractant for fetal olfactory epithelial cells. {ECO:0000250, ECO:0000269|PubMed:19696444}.; DISEASE: Hypogonadotropic hypogonadism 1 with or without anosmia (HH1) [MIM:308700]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:11297579, ECO:0000269|PubMed:15001591, ECO:0000269|PubMed:15605412, ECO:0000269|PubMed:17054399, ECO:0000269|PubMed:17213338, ECO:0000269|PubMed:17223984, ECO:0000269|PubMed:20530987, ECO:0000269|PubMed:21168128, ECO:0000269|PubMed:23643382, ECO:0000269|PubMed:25077900, ECO:0000269|PubMed:8504298, ECO:0000269|PubMed:8989261, ECO:0000269|PubMed:9589672}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. The genetics of hypogonadotropic hypogonadism involves various modes of transmission. Oligogenic inheritance has been reported in some patients carrying mutations in ANOS1 as well as in other HH-associated genes including FGFR1 and TACR3 (PubMed:23643382). {ECO:0000269|PubMed:23643382}.; TISSUE SPECIFICITY: Expressed in the cerebellum (at protein level). {ECO:0000269|PubMed:12007408}.; . . 0.49441 0.20646 0.154398214 64.73814579 . . ANOS2P . . . anosmin 2, pseudogene . . . . . . . . . . . ANP32A 0.973870035856712 0.0260989839179103 3.09802253775619e-05 acidic nuclear phosphoprotein 32 family member A FUNCTION: Implicated in a number of cellular processes, including proliferation, differentiation, caspase-dependent and caspase- independent apoptosis, suppression of transformation (tumor suppressor), inhibition of protein phosphatase 2A, regulation of mRNA trafficking and stability in association with ELAVL1, and inhibition of acetyltransferases as part of the INHAT (inhibitor of histone acetyltransferases) complex. Plays a role in E4F1- mediated transcriptional repression. {ECO:0000269|PubMed:10400610, ECO:0000269|PubMed:11360199, ECO:0000269|PubMed:15642345, ECO:0000269|PubMed:17557114}.; . TISSUE SPECIFICITY: Expressed in all tissues tested. Highly expressed in kidney and skeletal muscle, moderate levels of expression in brain, placenta and pancreas, and weakly expressed in lung. Found in all regions of the brain examined (amygdala, caudate nucleus, corpus callosum, hippocampus and thalamus), with highest levels in amygdala. {ECO:0000269|PubMed:15642345}.; ovary;adrenal medulla;skin;bone marrow;retina;prostate;optic nerve;thyroid;bladder;brain;tonsil;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;lung;cornea;mesenchyma;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;cerebellum peduncles;pons;caudate nucleus;bone marrow;globus pallidus;whole blood;parietal lobe;cerebellum; 0.54777 0.25991 -0.075159878 47.78839349 4.49266 0.16267 ANP32A-IT1 . . . ANP32A intronic transcript 1 . . . . . . . . . . . ANP32AP1 . . . acidic nuclear phosphoprotein 32 family member A pseudogene 1 . . . . . . . . . . . ANP32B 0.957395492721211 0.0425003817701858 0.000104125508603088 acidic nuclear phosphoprotein 32 family member B FUNCTION: Multifunctional protein working as a cell cycle progression factor as well as a cell survival factor. Required for the progression from the G1 to the S phase. Anti-apoptotic protein which functions as a caspase-3 inhibitor. Has no phosphatase 2A (PP2A) inhibitor activity (By similarity). Exhibits histone chaperone properties, stimulating core histones to assemble into a nucleosome. {ECO:0000250, ECO:0000269|PubMed:20538007}.; . TISSUE SPECIFICITY: Expressed in heart, lung, pancreas, prostate and in spleen, thymus and placenta. {ECO:0000269|PubMed:9473664}.; myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;urinary;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; fetal liver;spinal cord;tumor;white blood cells;bone marrow;thymus; 0.82716 0.10874 -0.163345027 41.24793583 31.817 1.00097 ANP32BP1 . . . acidic nuclear phosphoprotein 32 family member B pseudogene 1 . . . . . . . . . . . ANP32BP2 . . . acidic nuclear phosphoprotein 32 family member B pseudogene 2 . . . . . . . . . . . ANP32BP3 . . . acidic nuclear phosphoprotein 32 family member B pseudogene 3 . . . . . . . . . . . ANP32C . . . acidic nuclear phosphoprotein 32 family member C . . TISSUE SPECIFICITY: Expressed in activated stem cells, such as mobilized CD34+ cells and cord blood CD34+ cells, but not in resting bone marrow CD34+ cells. Expressed in a variety of neoplastic cell lines, mainly in prostatic adenocarcinoma cell lines. Not expressed in normal prostatic tissue. {ECO:0000269|PubMed:10086381, ECO:0000269|PubMed:15146458}.; . . 0.07530 0.06113 . . . . ANP32D 0.147937099023862 0.631681710264539 0.220381190711599 acidic nuclear phosphoprotein 32 family member D . . . . . 0.11687 . 0.703746784 85.42108988 30.52241 0.97199 ANP32E 0.976918663468077 0.0230585274715904 2.28090603328952e-05 acidic nuclear phosphoprotein 32 family member E FUNCTION: Histone chaperone that specifically mediates the genome- wide removal of histone H2A.Z/H2AFZ from the nucleosome: removes H2A.Z/H2AFZ from its normal sites of deposition, especially from enhancer and insulator regions. Not involved in deposition of H2A.Z/H2AFZ in the nucleosome. May stabilize the evicted H2A.Z/H2AFZ-H2B dimer, thus shifting the equilibrium towards dissociation and the off-chromatin state (PubMed:24463511). Inhibits activity of protein phosphatase 2A (PP2A). Does not inhibit protein phosphatase 1. May play a role in cerebellar development and synaptogenesis. {ECO:0000269|PubMed:24463511}.; . TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes, colon, small intestine, prostate, thymus, spleen, skeletal muscle, liver and kidney. {ECO:0000269|PubMed:12438741}.; smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;cerebellum peduncles;prefrontal cortex;trigeminal ganglion;cerebellum; 0.77993 0.13603 0.169169615 65.33380514 3690.10379 11.83775 ANPEP 0.00024424182711579 0.999724369303467 3.13888694169317e-05 alanyl aminopeptidase, membrane FUNCTION: Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection. {ECO:0000269|PubMed:10605003, ECO:0000269|PubMed:10676659, ECO:0000269|PubMed:11384645, ECO:0000269|PubMed:12473585, ECO:0000269|PubMed:9056417}.; . TISSUE SPECIFICITY: Expressed in epithelial cells of the kidney, intestine, and respiratory tract; granulocytes, monocytes, fibroblasts, endothelial cells, cerebral pericytes at the blood- brain barrier, synaptic membranes of cells in the CNS. Also expressed in endometrial stromal cells, but not in the endometrial glandular cells. Found in the vasculature of tissues that undergo angiogenesis and in malignant gliomas and lymph node metastases from multiple tumor types but not in blood vessels of normal tissues. A soluble form has been found in plasma. It is found to be elevated in plasma and effusions of cancer patients.; lymphoreticular;smooth muscle;ovary;colon;choroid;vein;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;amniotic fluid;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;small intestine;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; pancreas;prostate;adipose tissue;liver;kidney; 0.21614 0.85672 -0.984794421 8.651804671 401.80751 4.20336 ANTXR1 0.98528320310747 0.0147167343710442 6.25214858083699e-08 anthrax toxin receptor 1 FUNCTION: Plays a role in cell attachment and migration. Interacts with extracellular matrix proteins and with the actin cytoskeleton. Mediates adhesion of cells to type 1 collagen and gelatin, reorganization of the actin cytoskeleton and promotes cell spreading. Plays a role in the angiogenic response of cultured umbilical vein endothelial cells. {ECO:0000269|PubMed:15777794, ECO:0000269|PubMed:16762926}.; DISEASE: Hemangioma, capillary infantile (HCI) [MIM:602089]: A condition characterized by dull red, firm, dome-shaped hemangiomas, sharply demarcated from surrounding skin, usually presenting at birth or occurring within the first two or three months of life. They result from highly proliferative, localized growth of capillary endothelium and generally undergo regression and involution without scarring. {ECO:0000269|PubMed:18931684}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: GAPO syndrome (GAPO) [MIM:230740]: A disease characterized by growth retardation, alopecia, failure of tooth eruption, and progressive optic atrophy in some patients. {ECO:0000269|PubMed:23602711}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in umbilical vein endothelial cells (at protein level). Highly expressed in tumor endothelial cells. {ECO:0000269|PubMed:15777794}.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;brain;heart;cartilage;tongue;urinary;adrenal cortex;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;vein;uterus;whole body;oesophagus;larynx;bone;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lacrimal gland;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; superior cervical ganglion;uterus corpus;pons;atrioventricular node;trigeminal ganglion; 0.51987 0.13588 -0.909290275 10.03184713 205.61691 3.09642 ANTXR2 0.405188748060346 0.594440676129883 0.000370575809771033 anthrax toxin receptor 2 FUNCTION: Necessary for cellular interactions with laminin and the extracellular matrix. {ECO:0000269|PubMed:11683410, ECO:0000269|PubMed:12973667}.; DISEASE: Hyaline fibromatosis syndrome (HFS) [MIM:228600]: An autosomal recessive syndrome characterized by abnormal growth of hyalinized fibrous tissue usually affecting subcutaneous regions on the scalp, ears, neck, face, hands, and feet. The lesions appear as pearly papules or fleshy nodules. Additional features include gingival hypertrophy, progressive joint contractures resulting in severe limitation of mobility, osteopenia, and osteoporosis. Disease severity is variable. Some individuals manifest symptoms in infancy and have additional visceral or systemic involvement. Hyaline deposits in multiple organs, recurrent infections and intractable diarrhea often lead to early death. Surviving children may suffer from severely reduced mobility due to joint contractures. Other patients have later onset of a milder disorder affecting only the face and digits. {ECO:0000269|PubMed:12973667, ECO:0000269|PubMed:14508707, ECO:0000269|PubMed:15725249}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in prostate, thymus, ovary, testis, pancreas, colon, heart, kidney, lung, liver, peripheral blood leukocytes, placenta, skeletal muscle, small intestine and spleen. {ECO:0000269|PubMed:14508707}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;brain;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;blood;lens;skeletal muscle;bile duct;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;kidney;aorta;stomach; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.29739 0.10893 0.573279816 82.08303845 200.14281 3.05718 ANTXRL 0.317924027109247 0.48821363227719 0.193862340613563 anthrax toxin receptor-like . . . . . . . . . 4299.36795 13.04553 ANTXRLP1 . . . anthrax toxin receptor-like pseudogene 1 . . . . . . . . . . . ANXA1 0.000442370109951712 0.963508790702885 0.0360488391871629 annexin A1 FUNCTION: Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity (PubMed:8425544). Plays a role in glucocorticoid-mediated down- regulation of the early phase of the inflammatory response (By similarity). Promotes resolution of inflammation and wound healing (PubMed:25664854). Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades (PubMed:15187149, PubMed:25664854). Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors (PubMed:15187149). Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T- cell activation, regulates differentiation and proliferation of activated T-cells (PubMed:17008549). Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (PubMed:17008549). Has no effect on unstimulated T cells (PubMed:17008549). Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration (PubMed:15187149). Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (PubMed:19625660). Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)-dependent binding to phospholipid membranes (PubMed:2532504, PubMed:8557678). Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (By similarity). {ECO:0000250|UniProtKB:P10107, ECO:0000250|UniProtKB:P19619, ECO:0000269|PubMed:15187149, ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:19625660, ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:25664854, ECO:0000269|PubMed:2936963, ECO:0000269|PubMed:8425544, ECO:0000269|PubMed:8557678}.; . TISSUE SPECIFICITY: Detected in resting neutrophils (PubMed:10772777). Detected in peripheral blood T-cells (PubMed:17008549). Detected in extracellular vesicles in blood serum from patients with inflammatory bowel disease, but not in serum from healthy donors (PubMed:25664854). Detected in placenta (at protein level) (PubMed:2532504). Detected in liver. {ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:2936963}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;prostate;bone;thyroid;dura mater;brain;artery;bladder;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;adrenal cortex;pharynx;blood;skeletal muscle;bile duct;breast;pia mater;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;stomach;aorta; adipose tissue;tongue;placenta;ciliary ganglion;tonsil; 0.79692 0.51979 -0.315847836 31.68789809 49.46157 1.37601 ANXA2 0.00984346288196249 0.979501810508003 0.0106547266100346 annexin A2 FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:18799458, PubMed:24808179, PubMed:22848640). {ECO:0000269|PubMed:18799458, ECO:0000269|PubMed:22848640, ECO:0000269|PubMed:24808179}.; . . myocardium;ovary;foreskin;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;oesophagus;larynx;gum;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;epidermis;islets of Langerhans;adrenal cortex;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;aorta;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;adipose tissue;smooth muscle;lung;tongue;ciliary ganglion;trigeminal ganglion; 0.37850 0.85056 0.018483465 55.44939844 481.6043 4.52287 ANXA2P1 . . . annexin A2 pseudogene 1 . . . . . . . . . . . ANXA2P2 . . . annexin A2 pseudogene 2 FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. {ECO:0000250}.; . . . . . 0.85056 . . . . ANXA2P3 . . . annexin A2 pseudogene 3 . . . . . . . . . . . ANXA2R 3.08027490605399e-06 0.100233541950212 0.899763377774881 annexin A2 receptor FUNCTION: May act as a receptor for annexin II on marrow stromal cells to induce osteoclast formation.; . . . . 0.03280 0.06910 0.569646743 81.88841708 476.48768 4.50905 ANXA3 2.04254227340065e-09 0.238124033468032 0.761875964489426 annexin A3 FUNCTION: Inhibitor of phospholipase A2, also possesses anti- coagulant properties. Also cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate.; . . ovary;colon;parathyroid;bone marrow;prostate;endometrium;thyroid;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;bile duct;breast;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;cervix;kidney;stomach;aorta; superior cervical ganglion;skeletal muscle; 0.13359 0.16951 1.24016994 93.34748762 323.76847 3.82411 ANXA4 0.000342406647441912 0.988444164528574 0.0112134288239839 annexin A4 FUNCTION: Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. {ECO:0000250}.; . . . . 0.19832 0.19622 0.663285274 84.55414013 1918.83509 8.06313 ANXA5 3.81587630791735e-06 0.81643744792345 0.183558736200242 annexin A5 FUNCTION: This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.; DISEASE: Pregnancy loss, recurrent, 3 (RPRGL3) [MIM:614391]: A common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions. {ECO:0000269|PubMed:17339269}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;oral cavity;muscle;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;thymus; superior cervical ganglion;adipose tissue;smooth muscle;placenta;ciliary ganglion; 0.43918 0.46357 0.128714042 63.19886766 56.42294 1.50974 ANXA6 0.000183002363281359 0.998659643930734 0.00115735370598455 annexin A6 FUNCTION: May associate with CD21. May regulate the release of Ca(2+) from intracellular stores.; . . myocardium;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;gum;thyroid;brain;heart;cartilage;pineal body;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;thymus;cerebellum; . 0.09413 0.20865 -1.129772626 6.505071951 122.71608 2.41254 ANXA7 4.616142141031e-08 0.822579079620899 0.17742087421768 annexin A7 FUNCTION: Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis.; . TISSUE SPECIFICITY: Isoform 1 is expressed in brain, heart and skeletal muscle. Isoform 2 is more abundant in liver, lung, kidney, spleen, fibroblasts and placenta. {ECO:0000269|PubMed:1825209}.; . . 0.16467 0.32743 -0.156065314 42.16206653 149.62286 2.66716 ANXA8 . . . annexin A8 FUNCTION: This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.; . . choroid;fovea centralis;skin;retina;uterus;optic nerve;larynx;thyroid;bladder;brain;unclassifiable (Anatomical System);tongue;urinary;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;hypopharynx;spleen;head and neck;stomach; . 0.14981 0.13434 . . . . ANXA8L1 . . . annexin A8-like 1 . . . smooth muscle;ovary;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;epidermis;tongue;urinary;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;macula lutea;liver;hypopharynx;cervix;spleen;head and neck;stomach; . 0.53040 . . . . . ANXA9 3.36086004793863e-14 0.0106644732881841 0.989335526711782 annexin A9 FUNCTION: Low affinity receptor for acetylcholine known to be targeted by disease-causing pemphigus vulgaris antibodies in keratinocytes. {ECO:0000269|PubMed:10899159}.; . TISSUE SPECIFICITY: Expressed in the stratified squamous skin epithelium, but not in epithelia of other types (at protein level). {ECO:0000269|PubMed:10899159}.; . . 0.13797 0.09770 0.531004228 80.87992451 807.14518 5.59575 ANXA10 1.28390900106885e-08 0.561130781051249 0.438869206109661 annexin A10 . . . unclassifiable (Anatomical System);prostate;pancreas;lung;islets of Langerhans;liver;colon;bladder;stomach; fetal liver;superior cervical ganglion;smooth muscle;ciliary ganglion;trigeminal ganglion; . 0.09365 0.817616644 87.95116773 140.03091 2.58142 ANXA11 3.45820449578136e-06 0.939736783927994 0.0602597578675104 annexin A11 FUNCTION: Binds specifically to calcyclin in a calcium-dependent manner (By similarity). Required for midbody formation and completion of the terminal phase of cytokinesis. {ECO:0000250, ECO:0000269|PubMed:15197175}.; . . medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta;cerebellum; heart;placenta;white blood cells;whole blood; 0.16699 0.13939 0.492370491 79.60603916 6250.3857 16.55841 ANXA13 0.00725652255849584 0.989321183323901 0.00342229411760366 annexin A13 . . TISSUE SPECIFICITY: Gut specific.; unclassifiable (Anatomical System);prostate;colon;kidney;gall bladder;stomach; thalamus;trigeminal ganglion; 0.18246 0.12791 0.488730112 79.52347252 2139.07547 8.50573 AOAH 6.14602362973613e-11 0.60961335673288 0.39038664320566 acyloxyacyl hydrolase FUNCTION: Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides.; . . unclassifiable (Anatomical System);cartilage;umbilical cord;ovary;heart;colon;blood;bone marrow;uterus;pancreas;whole body;lung;nasopharynx;placenta;liver;testis;spleen;kidney;brain;tonsil; dorsal root ganglion;superior cervical ganglion;white blood cells;whole blood; 0.08323 0.11522 0.957177419 90.14508139 929.95297 5.91660 AOAH-IT1 . . . AOAH intronic transcript 1 . . . . . . . . . . . AOC1 1.2402397245546e-08 0.190385331753382 0.809614655844221 amine oxidase, copper containing 1 FUNCTION: Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. Placental DAO is thought to play a role in the regulation of the female reproductive function.; . TISSUE SPECIFICITY: Placenta and kidney.; . . 0.46312 0.72014 -0.591542347 18.24722812 4236.21603 12.94813 AOC2 5.13940212237188e-10 0.206831012894094 0.793168986591966 amine oxidase, copper containing 2 FUNCTION: Has a monoamine oxidase activity with substrate specificity for 2-phenylethylamine and tryptamine. May play a role in adipogenesis. May be a critical modulator of signal transmission in retina. {ECO:0000269|PubMed:17400359, ECO:0000269|PubMed:19588076}.; . TISSUE SPECIFICITY: Expressed in many tissues with much higher expression in retina. Isoform 1 and isoform 2 are expressed in adipose tissue, whereas isoform 1 only seems to be present in thymus, and isoform 2 only in testis. {ECO:0000269|PubMed:12755418, ECO:0000269|PubMed:17400359, ECO:0000269|PubMed:19588076}.; unclassifiable (Anatomical System);optic nerve;cartilage;bone;placenta;macula lutea;fovea centralis;choroid;lens;brain;retina; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;appendix;pons;atrioventricular node;trigeminal ganglion; 0.35454 0.83225 -0.124924535 44.10238264 237.8858 3.33095 AOC3 6.4699578127283e-09 0.42006318455303 0.579936808977012 amine oxidase, copper containing 3 FUNCTION: Cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has semicarbazide-sensitive (SSAO) monoamine oxidase activity. May play a role in adipogenesis. {ECO:0000269|PubMed:17400359, ECO:0000269|PubMed:19588076, ECO:0000269|PubMed:23349812, ECO:0000269|PubMed:9653080}.; . TISSUE SPECIFICITY: Strongly expressed on the high endothelial venules of peripheral lymph nodes and on hepatic endothelia. Also highly expressed in appendix, lung and small intestine. Expressed also in adipose tissue, in bone marrow, colon, heart, kidney, ovary, pancreas, placenta, prostate, skeletal muscle, spleen and testis. Isoform 2 seems to be the predominant transcript in fetal kidneys, fetal cartilage and fetal tonsils. The highest relative expression of isoform 2 occurs in skeletal muscle, heart, pancreas, kidney, and lung. {ECO:0000269|PubMed:17400359, ECO:0000269|PubMed:23349812, ECO:0000269|PubMed:9653080}.; unclassifiable (Anatomical System);cartilage;heart;colon;skin;skeletal muscle;retina;breast;uterus;prostate;optic nerve;lung;cerebral cortex;nasopharynx;placenta;testis;spleen;kidney;spinal ganglion;brain;aorta;stomach; uterus;adipose tissue;adrenal gland;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10367 0.20240 0.782621089 87.25524888 1004.97534 6.10264 AOC4P . . . amine oxidase, copper containing 4, pseudogene . . . . . . . . . . . AOX1 2.67936726161947e-22 0.488410343348547 0.511589656651453 aldehyde oxidase 1 FUNCTION: Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and N- methylphthalazinium, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis. {ECO:0000269|PubMed:20444863, ECO:0000269|PubMed:22031625, ECO:0000269|PubMed:22279051, ECO:0000269|PubMed:22522748, ECO:0000269|PubMed:22996261, ECO:0000269|PubMed:23857892, ECO:0000269|PubMed:7786031, ECO:0000269|PubMed:9224775}.; . TISSUE SPECIFICITY: Abundant in liver, expressed in adipose tissue and at lower levels in lung, skeletal muscle, pancreas. In contrast to mice, no significant gender difference in AOX1 expression level (at protein level). {ECO:0000269|PubMed:18066686, ECO:0000269|PubMed:18671973, ECO:0000269|PubMed:20444863, ECO:0000269|PubMed:22031625, ECO:0000269|PubMed:22522748, ECO:0000269|PubMed:23857892, ECO:0000269|PubMed:8248161}.; colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;gum;thyroid;bone;testis;dura mater;artery;brain;gall bladder;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;pia mater;lung;adrenal gland;placenta;macula lutea;liver;kidney;stomach;aorta; superior cervical ganglion;adipose tissue;adrenal gland;adrenal cortex;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.15056 0.40109 -1.229158719 5.555555556 905.65387 5.85546 AOX2P . . . aldehyde oxidase 2 pseudogene . . . . . . . . . . . AOX3P . . . aldehyde oxidase 3, pseudogene . . . . . . . . . . . AP1AR 0.511166928930552 0.488021686184408 0.000811384885039602 adaptor related protein complex 1 associated regulatory protein FUNCTION: Necessary for adaptor protein complex 1 (AP-1)-dependent transport between the trans-Golgi network and endosomes. Regulates the membrane association of AP1G1/gamma1-adaptin, one of the subunits of the AP-1 adaptor complex. The direct interaction with AP1G1/gamma1-adaptin attenuates the release of the AP-1 complex from membranes. Regulates endosomal membrane traffic via association with AP-1 and KIF5B thus linking kinesin-based plus- end-directed microtubular transport to AP-1-dependent membrane traffic. May act as effector of AP-1 in calcium-induced endo- lysosome secretion. Inhibits Arp2/3 complex function; negatively regulates cell spreading, size and motility via intracellular sequestration of the Arp2/3 complex. {ECO:0000269|PubMed:15775984, ECO:0000269|PubMed:19706427, ECO:0000269|PubMed:21525240, ECO:0000269|PubMed:22689987}.; . . unclassifiable (Anatomical System);ovary;heart;hypothalamus;colon;skin;skeletal muscle;bone marrow;breast;uterus;prostate;whole body;lung;endometrium;bone;placenta;hippocampus;liver;testis;germinal center;kidney;stomach;gall bladder; amygdala;superior cervical ganglion;temporal lobe;globus pallidus;pons;trigeminal ganglion;skeletal muscle; 0.14777 0.14109 0.327131069 73.27199811 63.26348 1.62796 AP1B1 0.99158312872111 0.00841686806474375 3.21414638491478e-09 adaptor related protein complex 1 beta 1 subunit FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.; . TISSUE SPECIFICITY: Widely expressed.; lymphoreticular;umbilical cord;colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;nervous;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;trigeminal ganglion; 0.55032 0.22545 -1.52667341 3.408822836 64.52415 1.64803 AP1B1P1 . . . adaptor related protein complex 1 beta 1 subunit pseudogene 1 . . . . . . . . . . . AP1B1P2 . . . adaptor related protein complex 1 beta 1 subunit pseudogene 2 . . . . . . . . . . . AP1G1 0.999975846160012 2.41538399779649e-05 1.00795550757157e-14 adaptor related protein complex 1 gamma 1 subunit FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.; . TISSUE SPECIFICITY: Widely expressed.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;ganglion;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;amnion;head and neck;kidney;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.47274 0.11928 -0.756778259 13.44656759 2492.12785 9.31110 AP1G2 8.93514525478059e-14 0.408304022162022 0.591695977837888 adaptor related protein complex 1 gamma 2 subunit FUNCTION: May function in protein sorting in late endosomes or multivesucular bodies (MVBs). Involved in MVB-assisted maturation of hepatitis B virus (HBV). {ECO:0000269|PubMed:16867982, ECO:0000269|PubMed:17553870, ECO:0000269|PubMed:9733768}.; . TISSUE SPECIFICITY: Expressed in all but one (skeletal muscle) tissues examined.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;oesophagus;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;prefrontal cortex;testis;ciliary ganglion;caudate nucleus;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.10043 0.09722 -1.236390924 5.520169851 492.87629 4.56522 AP1M1 0.842349723177368 0.157625029563779 2.52472588533492e-05 adaptor related protein complex 1 mu 1 subunit FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.; . . lymphoreticular;myocardium;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;synovium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach; testis - interstitial;ciliary ganglion;atrioventricular node; 0.42033 0.17821 -0.868835007 10.65109696 4.88829 0.18115 AP1M2 0.00134595247967371 0.962676606112087 0.0359774414082388 adaptor related protein complex 1 mu 2 subunit FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;larynx;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;thyroid;placenta;kidney;fetal thyroid; 0.55795 . -0.867014353 10.72776598 52.57422 1.43586 AP1S1 0.52022703354864 0.462792989576895 0.0169799768744653 adaptor related protein complex 1 sigma 1 subunit FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. {ECO:0000269|PubMed:9733768}.; DISEASE: Mental retardation, enteropathy, deafness, peripheral neuropathy, ichthyosis, and keratoderma (MEDNIK) [MIM:609313]: A disorder characterized by erythematous skin lesions and hyperkeratosis, severe psychomotor retardation, peripheral neuropathy, sensorineural hearing loss, together with elevated very-long-chain fatty acids and severe congenital diarrhea. {ECO:0000269|PubMed:19057675}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9733768}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;gum;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;adrenal cortex;lens;lung;placenta;macula lutea;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach; whole brain;medulla oblongata;subthalamic nucleus;superior cervical ganglion;temporal lobe;prefrontal cortex;globus pallidus;pons;cingulate cortex;skeletal muscle;parietal lobe; 0.28085 0.13803 -0.09720619 46.20193442 . . AP1S2 0.792611169503459 0.201350872188625 0.00603795830791608 adaptor related protein complex 1 sigma 2 subunit FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.; . TISSUE SPECIFICITY: Widely expressed.; ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;lung;pia mater;adrenal gland;placenta;hippocampus;kidney;stomach;thymus;cerebellum; superior cervical ganglion;whole blood;trigeminal ganglion;skeletal muscle; 0.74914 0.05068 0.057118534 57.99716914 1.21425 0.03993 AP1S2P1 . . . adaptor related protein complex 1 sigma 2 subunit pseudogene 1 . . . . . . . . . . . AP1S3 0.167450176735496 0.771753753042861 0.0607960702216433 adaptor related protein complex 1 sigma 3 subunit FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. Involved in TLR3 trafficking (PubMed:24791904). {ECO:0000269|PubMed:24791904}.; . TISSUE SPECIFICITY: Widely expressed.; unclassifiable (Anatomical System);breast;prostate;placenta;liver;colon;cervix;blood;germinal center;bone marrow; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14506 0.10315 1.302692676 93.93724935 140.64371 2.58746 AP2A1 0.9998472799622 0.000152720015810561 2.19896377337437e-11 adaptor related protein complex 2 alpha 1 subunit FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin- coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C- terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity). {ECO:0000250, ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:19033387}.; . TISSUE SPECIFICITY: Isoform A expressed in forebrain, skeletal muscle, spinal cord, cerebellum, salivary gland, heart and colon. Isoform B is widely expressed in tissues and also in breast cancer and in prostate carcinoma cells.; lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;aorta; . 0.11452 0.35783 -1.464150033 3.780372729 80.51074 1.89612 AP2A2 0.999932214597942 6.77853990175968e-05 3.04020304708129e-12 adaptor related protein complex 2 alpha 2 subunit FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin- coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C- terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity). {ECO:0000250, ECO:0000269|PubMed:12960147, ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:19033387}.; . . medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;amnion;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum; whole brain;amygdala;occipital lobe;superior cervical ganglion;testis - interstitial;cerebellum peduncles;atrioventricular node;skeletal muscle;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.15747 0.15173 -1.771059651 2.300070771 31.30469 0.98701 AP2B1 0.999667233317167 0.0003327666531623 2.96705635602641e-11 adaptor related protein complex 2 beta 1 subunit FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin- coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin- associated sorting proteins (CLASPs) are recognized by their [DE]- X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly. {ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:14985334, ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:19033387}.; . . myocardium;lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;pineal body;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;developmental;colon;parathyroid;uterus;whole body;larynx;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; amygdala;subthalamic nucleus;testis - interstitial;medulla oblongata;testis - seminiferous tubule;temporal lobe;globus pallidus;testis;kidney;skeletal muscle;cingulate cortex;parietal lobe;cerebellum; 0.71824 0.31324 -0.957024976 9.088228356 7.40151 0.27523 AP2M1 0.993893174243241 0.00610664878097485 1.7697578408164e-07 adaptor related protein complex 2 mu 1 subunit FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin- coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs. The surface region interacting with to the Y-X- X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane- associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled family members upon Wnt signaling (By similarity). {ECO:0000250, ECO:0000269|PubMed:12694563, ECO:0000269|PubMed:12952941, ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:14985334, ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:16581796, ECO:0000269|PubMed:19033387}.; . . smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;cervix;mammary gland;salivary gland;colon;parathyroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;cerebellum; whole brain;amygdala;occipital lobe;medulla oblongata;subthalamic nucleus;temporal lobe;prefrontal cortex;globus pallidus;pons;parietal lobe;cingulate cortex; 0.23681 0.24700 -0.141298762 42.87567823 32.02466 1.00657 AP2S1 0.919495985397116 0.0799891236976843 0.000514890905199509 adaptor related protein complex 2 sigma 1 subunit FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein Transport via Transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin- coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity). May also play a role in extracellular calcium homeostasis. {ECO:0000250, ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:19033387, ECO:0000269|PubMed:23222959}.; DISEASE: Hypocalciuric hypercalcemia, familial 3 (HHC3) [MIM:600740]: A form of hypocalciuric hypercalcemia, a disorder of mineral homeostasis that is transmitted as an autosomal dominant trait with a high degree of penetrance. It is characterized biochemically by lifelong elevation of serum calcium concentrations and is associated with inappropriately low urinary calcium excretion and a normal or mildly elevated circulating parathyroid hormone level. Hypermagnesemia is typically present. Affected individuals are usually asymptomatic and the disorder is considered benign. However, chondrocalcinosis and pancreatitis occur in some adults. {ECO:0000269|PubMed:23222959, ECO:0000269|PubMed:24081735}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;oesophagus;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;placenta;duodenum;kidney;stomach;thymus; whole brain;amygdala;medulla oblongata;prostate;lung;heart;temporal lobe;liver;globus pallidus;parietal lobe; 0.21863 0.16306 0.013025609 54.62962963 1.16568 0.03254 AP3B1 0.995386030171841 0.00461396979789535 3.02639375296319e-11 adaptor related protein complex 3 beta 1 subunit FUNCTION: Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.; DISEASE: Hermansky-Pudlak syndrome 2 (HPS2) [MIM:608233]: A form of Hermansky-Pudlak syndrome, a genetically heterogeneous autosomal recessive disorder characterized by oculocutaneous albinism, bleeding due to platelet storage pool deficiency, and lysosomal storage defects. This syndrome results from defects of diverse cytoplasmic organelles including melanosomes, platelet dense granules and lysosomes. Ceroid storage in the lungs is associated with pulmonary fibrosis, a common cause of premature death in individuals with HPS. HPS2 differs from the other forms of HPS in that it includes immunodeficiency in its phenotype and patients with HPS2 have an increased susceptibility to infections. {ECO:0000269|PubMed:10024875}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9151686, ECO:0000269|PubMed:9182526}.; smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;duodenum;hypopharynx;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;caudate nucleus;trigeminal ganglion;skin;skeletal muscle; 0.35326 0.31608 0.42623145 77.29417315 585.39595 4.90676 AP3B2 0.990065569960768 0.00993442906317966 9.76052519671278e-10 adaptor related protein complex 3 beta 2 subunit FUNCTION: Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.; . TISSUE SPECIFICITY: Expression is specific to nervous system. Expressed in nerve terminal and cell body, and is associated with nerve-terminal vesicles. Expression seen in Purkinje cells, cortical neurons, neuroectodermal tumors and graded in cerebral cortex (deeper layers exhibit stronger expression). {ECO:0000269|PubMed:1851215}.; unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;lung;frontal lobe;placenta;macula lutea;visual apparatus;pituitary gland;testis;kidney;brain; whole brain;occipital lobe;subthalamic nucleus;cerebellum peduncles;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.28285 0.19352 -1.618506764 2.925218212 232.03675 3.29287 AP3D1 0.798002533603789 0.20199744946122 1.69349916098482e-08 adaptor related protein complex 3 delta 1 subunit FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.; . TISSUE SPECIFICITY: Present in all adult tissues examined with the highest levels in skeletal muscle, heart, pancreas and testis. {ECO:0000269|PubMed:9151686}.; ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;urinary;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;cerebellum; amygdala;whole brain;occipital lobe;white blood cells;caudate nucleus;skeletal muscle;prostate;lung;placenta;prefrontal cortex;globus pallidus;kidney;cingulate cortex;parietal lobe;cerebellum; 0.31495 0.18846 -2.276539041 1.244397264 383.53183 4.12975 AP3M1 0.768617879575058 0.231020997887395 0.000361122537547039 adaptor related protein complex 3 mu 1 subunit FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;adrenal cortex;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.23894 0.12717 -0.404032746 26.53338051 26.99108 0.87204 AP3M2 4.4000015278485e-05 0.851540787973098 0.148415212011624 adaptor related protein complex 3 mu 2 subunit FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.; . . myocardium;smooth muscle;ovary;umbilical cord;sympathetic chain;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach;peripheral nerve;cerebellum; amygdala;superior cervical ganglion;thalamus;medulla oblongata;occipital lobe;hypothalamus;temporal lobe;caudate nucleus;atrioventricular node;pons;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;parietal lobe;cingulate cortex; 0.06667 0.09422 -0.538132194 20.26421326 25.73556 0.83771 AP3S1 0.00185372377308681 0.722406109419439 0.275740166807474 adaptor related protein complex 3 sigma 1 subunit FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.; . TISSUE SPECIFICITY: Present in all adult tissues examined. {ECO:0000269|PubMed:8697810, ECO:0000269|PubMed:9118953, ECO:0000269|PubMed:9151686}.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;pharynx;blood;lens;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;vein;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;oral cavity;bile duct;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta; . 0.53380 0.14229 0.391453969 75.87284737 20.45346 0.69649 AP3S2 0.000230909983075112 0.514353847819435 0.485415242197489 adaptor related protein complex 3 sigma 2 subunit FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.; . TISSUE SPECIFICITY: Present in all adult tissues examined. {ECO:0000269|PubMed:9118953}.; lymphoreticular;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;testis;dura mater;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);meninges;heart;hypothalamus;pineal body;muscle;adrenal cortex;blood;lens;pancreas;pia mater;lung;adrenal gland;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; medulla oblongata;superior cervical ganglion;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;cerebellum; 0.08187 0.11809 -0.183570861 39.95046001 1.15488 0.03165 AP4B1 2.69463741752042e-08 0.902527070884322 0.0974729021693042 adaptor related protein complex 4 beta 1 subunit FUNCTION: Subunit of novel type of clathrin- or non-clathrin- associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system.; . TISSUE SPECIFICITY: Widely expressed.; ovary;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;oral cavity;blood;breast;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach; . 0.17088 0.11086 -0.130380821 44.03161123 4515.95276 13.49813 AP4B1-AS1 . . . AP4B1 antisense RNA 1 . . . . . . . . . . . AP4E1 0.979862099052625 0.0201378998266214 1.12075368439735e-09 adaptor related protein complex 4 epsilon 1 subunit FUNCTION: Subunit of novel type of clathrin- or non-clathrin- associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system.; . TISSUE SPECIFICITY: Widely expressed.; breast;uterus;lung;umbilical cord;visual apparatus;testis;blood;germinal center;skeletal muscle; superior cervical ganglion;temporal lobe;trigeminal ganglion;skeletal muscle; 0.45354 0.09957 -0.659500046 16.07100731 3652.51436 11.74385 AP4M1 2.36166196366206e-11 0.237029181213156 0.762970818763228 adaptor related protein complex 4 mu 1 subunit FUNCTION: Component of the AP-4 complex, a novel type of clathrin- or non-clathrin-associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal- lysosomal system. Plays a role in the intracellular trafficking of APP from the trans-Golgi network (TGN) to endosomes, and thereby inhibits amyloidogenic processing of APP. {ECO:0000269|PubMed:11139587, ECO:0000269|PubMed:20230749}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in testis and lowly expressed in brain and lung. {ECO:0000269|PubMed:10436028, ECO:0000269|PubMed:9013859}.; ovary;salivary gland;colon;parathyroid;skin;uterus;prostate;optic nerve;larynx;bone;testis;brain;artery;tonsil;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;bile duct;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta; subthalamic nucleus;cingulate cortex;parietal lobe; . 0.13809 -1.175687564 5.974286388 277.05611 3.56321 AP4S1 1.33545575036575e-07 0.112162615121504 0.887837251332921 adaptor related protein complex 4 sigma 1 subunit FUNCTION: Subunit of novel type of clathrin- or non-clathrin- associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system.; . TISSUE SPECIFICITY: Widely expressed.; unclassifiable (Anatomical System);medulla oblongata;lung;ovary;placenta;hippocampus;parathyroid;germinal center;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.16394 . -0.361761279 28.6329323 21.32182 0.71950 AP5B1 6.97158289196506e-06 0.48069646043769 0.519296567979418 adaptor related protein complex 5 beta 1 subunit FUNCTION: As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. {ECO:0000269|PubMed:22022230}.; . . . . . . . . 3816.63131 12.14684 AP5M1 0.000108637306093947 0.947332117616342 0.0525592450775645 adaptor related protein complex 5 mu 1 subunit FUNCTION: As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. According to PubMed:18395520, it may play a role in cell death. {ECO:0000269|PubMed:18395520, ECO:0000269|PubMed:22022230}.; . TISSUE SPECIFICITY: Expressed in various tumor cell lines including Jurkat, Hep-G2 and HeLa. {ECO:0000269|PubMed:18395520}.; . . 0.79554 . 0.663285274 84.55414013 978.94501 6.04242 AP5S1 0.000277046194039352 0.337578573886894 0.662144379919066 adaptor related protein complex 5 sigma 1 subunit FUNCTION: As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. According to PubMed:20613862, it is required for efficient homologous recombination DNA double-strand break repair. {ECO:0000269|PubMed:20613862, ECO:0000269|PubMed:22022230}.; . . . . 0.07962 . 0.084621747 60.31493277 125.5033 2.43816 AP5Z1 . . . adaptor related protein complex 5 zeta 1 subunit FUNCTION: As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. According to PubMed:20613862 it is a putative helicase required for efficient homologous recombination DNA double-strand break repair. {ECO:0000269|PubMed:20613862, ECO:0000269|PubMed:22022230}.; DISEASE: Spastic paraplegia 48, autosomal recessive (SPG48) [MIM:613647]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. {ECO:0000269|PubMed:20613862}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.13548 0.10205 -0.604525442 17.51592357 1128.74058 6.41017 APAF1 3.82072122629714e-05 0.999958059359172 3.73342856532368e-06 apoptotic peptidase activating factor 1 FUNCTION: Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP. Isoform 6 is less effective in inducing apoptosis. {ECO:0000269|PubMed:10393175, ECO:0000269|PubMed:12804598}.; . TISSUE SPECIFICITY: Ubiquitous. Highest levels of expression in adult spleen and peripheral blood leukocytes, and in fetal brain, kidney and lung. Isoform 1 is expressed in heart, kidney and liver.; smooth muscle;ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;pineal body;pharynx;blood;skeletal muscle;breast;lung;placenta;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11074 0.54535 -0.08265057 47.20452937 265.4513 3.49465 APBA1 0.865841338704799 0.134155345380194 3.31591500674707e-06 amyloid beta precursor protein binding family A member 1 FUNCTION: Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the beta- amyloid precursor protein (APP) and hence formation of beta-APP.; . TISSUE SPECIFICITY: Brain and spinal cord. Isoform 2 is expressed in testis and brain, but not detected in lung, liver or spleen. {ECO:0000269|PubMed:23737971}.; unclassifiable (Anatomical System);heart;ovary;tongue;islets of Langerhans;parathyroid;fovea centralis;skeletal muscle;skin;uterus;frontal lobe;placenta;macula lutea;head and neck;brain; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.13442 0.22137 -1.440283256 3.963198868 1205.88424 6.57856 APBA2 0.0735269721652979 0.925955226307096 0.000517801527606442 amyloid beta precursor protein binding family A member 2 FUNCTION: Putative function in synaptic vesicle exocytosis by binding to STXBP1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the beta-amyloid precursor protein (APP) and hence formation of beta-APP.; . TISSUE SPECIFICITY: Brain.; unclassifiable (Anatomical System);ovary;tongue;nervous;sympathetic chain;blood;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;optic nerve;whole body;frontal lobe;endometrium;thyroid;macula lutea;visual apparatus;head and neck;kidney;brain; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.25480 0.20524 -1.390744555 4.305260675 2303.99849 8.88719 APBA3 2.11553616288552e-11 0.0342003265260916 0.965799673452753 amyloid beta precursor protein binding family A member 3 FUNCTION: May modulate processing of the beta-amyloid precursor protein (APP) and hence formation of beta-APP. May enhance the activity of HIF1A in macrophages by inhibiting the activity of HIF1AN. {ECO:0000269|PubMed:19726677}.; . TISSUE SPECIFICITY: Expressed in all tissues examined with lower levels in brain and testis.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland; . 0.13559 0.12876 0.891034851 89.2663364 565.42478 4.82978 APBB1 0.986993652220937 0.0130061196709182 2.28108145065172e-07 amyloid beta precursor protein binding family B member 1 FUNCTION: Transcription coregulator that can have both coactivator and corepressor functions. Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain. Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis. May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro- apoptosis factors such as MAPK8/JNK1. Required for histone H4 acetylation at double-strand breaks (DSBs). Its ability to specifically bind modified histones and chromatin modifying enzymes such as KAT5/TIP60, probably explains its trancription activation activity. Function in association with TSHZ3, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s). {ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:18468999, ECO:0000269|PubMed:18922798, ECO:0000269|PubMed:19234442, ECO:0000269|PubMed:19343227}.; . TISSUE SPECIFICITY: Highly expressed in brain; strongly reduced in post-mortem elderly subjects with Alzheimer disease. {ECO:0000269|PubMed:19343227}.; myocardium;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;cerebellum cortex;islets of Langerhans;hypothalamus;pineal body;muscle;adrenal cortex;lens;skeletal muscle;pancreas;lung;adrenal gland;trabecular meshwork;hippocampus;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; subthalamic nucleus;cerebellum peduncles;temporal lobe;globus pallidus;pons;trigeminal ganglion;cingulate cortex; 0.21033 0.35953 -0.551080959 19.93394669 161.71105 2.77855 APBB1IP 0.594392028430969 0.405523762176188 8.42093928430846e-05 amyloid beta precursor protein binding family B member 1 interacting protein FUNCTION: Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Suppresses insulin- induced promoter activities through AP1 and SRE. Mediates Rap1- induced adhesion. {ECO:0000269|PubMed:14530287, ECO:0000269|PubMed:15469846}.; . TISSUE SPECIFICITY: Widely expressed with high expression in thymus, spleen, lymph node, bone marrow and peripheral leukocytes. {ECO:0000269|PubMed:14530287, ECO:0000269|PubMed:15469846}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;heart;skin;bone marrow;uterus;lung;endometrium;nasopharynx;placenta;testis;germinal center; . 0.09114 0.10771 -0.069700724 48.54328851 307.8485 3.73347 APBB2 0.0398888659197788 0.960055421558902 5.5712521319201e-05 amyloid beta precursor protein binding family B member 2 FUNCTION: May modulate the internalization of beta-amyloid precursor protein.; . . colon;skin;retina;uterus;prostate;whole body;frontal lobe;cerebral cortex;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;tongue;islets of Langerhans;lens;skeletal muscle;breast;lung;placenta;visual apparatus;liver;amnion;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;pons;atrioventricular node;skeletal muscle;skin;subthalamic nucleus;placenta;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.40782 0.23652 -0.374708069 28.15522529 147.87116 2.64955 APBB3 1.54051117620328e-05 0.962984600010038 0.0369999948781995 amyloid beta precursor protein binding family B member 3 FUNCTION: May modulate the internalization of beta-amyloid precursor protein.; . TISSUE SPECIFICITY: Expressed in various tissues, highest expression in brain. {ECO:0000269|PubMed:12153398}.; smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;endometrium;synovium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;lacrimal gland;tongue;blood;pancreas;lung;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;cerebellum; temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node; 0.47859 0.14066 0.178263593 66.12998349 370.93774 4.06699 APC 0.999999927739402 7.22605979150577e-08 1.20102861496063e-23 adenomatous polyposis coli FUNCTION: Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization. {ECO:0000269|PubMed:10947987, ECO:0000269|PubMed:17599059, ECO:0000269|PubMed:19151759, ECO:0000269|PubMed:19893577, ECO:0000269|PubMed:20937854}.; DISEASE: Familial adenomatous polyposis (FAP) [MIM:175100]: A cancer predisposition syndrome characterized by adenomatous polyps of the colon and rectum, but also of upper gastrointestinal tract (ampullary, duodenal and gastric adenomas). This is a viciously premalignant disease with one or more polyps progressing through dysplasia to malignancy in untreated gene carriers with a median age at diagnosis of 40 years. {ECO:0000269|PubMed:10470088, ECO:0000269|PubMed:1338691, ECO:0000269|PubMed:1338764, ECO:0000269|PubMed:1338904, ECO:0000269|PubMed:1651563, ECO:0000269|PubMed:7833149, ECO:0000269|PubMed:7833931, ECO:0000269|PubMed:8990002}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hereditary desmoid disease (HDD) [MIM:135290]: Autosomal dominant trait with 100% penetrance and possible variable expression among affected relatives. HDD patients show multifocal fibromatosis of the paraspinal muscles, breast, occiput, arms, lower ribs, abdominal wall, and mesentery. Desmoid tumors appears also as a complication of familial adenomatous polyposis. {ECO:0000269|PubMed:10782927, ECO:0000269|PubMed:8940264}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. {ECO:0000269|PubMed:10666372}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Mismatch repair cancer syndrome (MMRCS) [MIM:276300]: An autosomal recessive, rare, childhood cancer predisposition syndrome encompassing a broad tumor spectrum. This includes hematological malignancies, central nervous system tumors, Lynch syndrome-associated malignancies such as colorectal tumors as well as multiple intestinal polyps, embryonic tumors and rhabdomyosarcoma. Multiple cafe-au-lait macules, a feature reminiscent of neurofibromatosis type 1, are often found as first manifestation of the underlying cancer. Areas of skin hypopigmentation have also been reported in MMRCS patients. {ECO:0000269|PubMed:7661930}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Hepatocellular carcinoma (HCC) [MIM:114550]: A primary malignant neoplasm of epithelial liver cells. The major risk factors for HCC are chronic hepatitis B virus (HBV) infection, chronic hepatitis C virus (HCV) infection, prolonged dietary aflatoxin exposure, alcoholic cirrhosis, and cirrhosis due to other causes. Note=The gene represented in this entry may be involved in disease pathogenesis.; TISSUE SPECIFICITY: Expressed in a variety of tissues.; myocardium;smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta; amygdala;medulla oblongata;superior cervical ganglion;occipital lobe;thalamus;temporal lobe;atrioventricular node;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.53216 0.57092 -2.523543479 0.902335456 395.17068 4.17713 APC2 0.999980518341102 1.94816587516986e-05 1.45829781258825e-13 adenomatosis polyposis coli 2 FUNCTION: Promotes rapid degradation of CTNNB1 and may function as a tumor suppressor. May function in Wnt signaling. {ECO:0000269|PubMed:10021369, ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:9823329}.; . TISSUE SPECIFICITY: Widely expressed (at protein level). Specifically expressed in the CNS. {ECO:0000269|PubMed:10021369, ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:9823329}.; sympathetic chain;colon;fovea centralis;choroid;skin;bone marrow;retina;optic nerve;whole body;frontal lobe;bone;pituitary gland;iris;testis;brain;unclassifiable (Anatomical System);lymph node;tongue;blood;lens;lung;macula lutea;hippocampus;visual apparatus;head and neck;kidney;mammary gland;stomach;thymus; amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;cerebellum peduncles;spinal cord;temporal lobe;atrioventricular node;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.47667 0.14249 . . 2614.89208 9.57474 APCDD1 0.000654607968648686 0.910841435195192 0.0885039568361597 adenomatosis polyposis coli down-regulated 1 FUNCTION: Negative regulator of the Wnt signaling pathway. Inhibits Wnt signaling in a cell-autonomous manner and functions upstream of beta-catenin. May act via its interaction with Wnt and LRP proteins. May play a role in colorectal tumorigenesis. {ECO:0000269|PubMed:12384519, ECO:0000269|PubMed:20393562}.; DISEASE: Hypotrichosis 1 (HYPT1) [MIM:605389]: A rare form of non- syndromic hereditary hypotrichosis without characteristic hair shaft anomalies. Affected individuals typically show normal hair at birth, but hair loss and thinning of the hair shaft start during early childhood and progress with age. {ECO:0000269|PubMed:20393562}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Abundantly expressed in heart, pancreas, prostate and ovary. Moderately expressed in lung, liver, kidney, spleen, thymus, colon and peripheral lymphocytes. Abundantly expressed in both the epidermal and dermal compartments of the hair follicle. Present in scalp skin Highly expressed in the hair follicle dermal papilla, the matrix, and the hair shaft (at protein level). {ECO:0000269|PubMed:12384519, ECO:0000269|PubMed:20393562}.; smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cerebral cortex;endometrium;larynx;thyroid;bone;testis;dura mater;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);meninges;heart;islets of Langerhans;lens;breast;pancreas;pia mater;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;mammary gland;stomach;cerebellum; . 0.21038 0.10984 -1.372317395 4.446803491 634.70125 5.07135 APCDD1L 0.0175592164085508 0.892150808979574 0.0902899746118754 adenomatosis polyposis coli down-regulated 1-like . . . . . 0.44207 . 0.420771676 77.15852795 1143.54286 6.44725 APCDD1L-AS1 . . . APCDD1L antisense RNA 1 (head to head) . . . . . . . . . . . APCS 0.0386375435691614 0.837927437472282 0.123435018958557 amyloid P component, serum FUNCTION: Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin.; DISEASE: Note=SAP is a precursor of amyloid component P which is found in basement membrane and associated with amyloid deposits.; TISSUE SPECIFICITY: Found in serum and urine. {ECO:0000269|PubMed:15174148}.; unclassifiable (Anatomical System);lung;islets of Langerhans;bone;liver;spleen;gall bladder; superior cervical ganglion;liver;fetal lung;trigeminal ganglion;skeletal muscle; 0.07963 0.23713 -0.05129383 49.75819769 14.18841 0.51300 APEH 0.0132157073381975 0.986725423802916 5.88688588860812e-05 acylaminoacyl-peptide hydrolase FUNCTION: This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N- acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser. {ECO:0000269|PubMed:1861871, ECO:0000269|PubMed:2006156}.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;larynx;bone;iris;pituitary gland;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;hypothalamus;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;amnion;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; heart;liver;kidney; 0.11616 0.30420 -0.777005578 12.9747582 129.21963 2.47844 APELA . . . apelin receptor early endogenous ligand FUNCTION: Hormone required during early development for endoderm differentiation and heart morphogenesis by acting as a ligand for the apelin receptor (APLNR). Acts as a motogen by promoting endoderm and mesendoderm cell migration during gastrulation by binding and activating the apelin receptor, thereby driving internalization of the apelin receptor. Plays a key role during heart development by acting as a ligand for the apelin receptor (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Most highly expressed in undifferentiated embryonic stem cell and is rapidly down-regulated during differentiation. {ECO:0000269|PubMed:24316148}.; . . . . . . . . APEX1 0.000103582180068405 0.809978950818198 0.189917467001733 apurinic/apyrimidinic endodeoxyribonuclease 1 FUNCTION: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'- phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA. {ECO:0000269|PubMed:10023679, ECO:0000269|PubMed:11118054, ECO:0000269|PubMed:11452037, ECO:0000269|PubMed:11809897, ECO:0000269|PubMed:11832948, ECO:0000269|PubMed:12524539, ECO:0000269|PubMed:16617147, ECO:0000269|PubMed:1719477, ECO:0000269|PubMed:18179823, ECO:0000269|PubMed:18439621, ECO:0000269|PubMed:18579163, ECO:0000269|PubMed:18809583, ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:19401441, ECO:0000269|PubMed:19934257, ECO:0000269|PubMed:20699270, ECO:0000269|PubMed:21496894, ECO:0000269|PubMed:21762700, ECO:0000269|PubMed:8355688, ECO:0000269|PubMed:8621488, ECO:0000269|PubMed:8932375, ECO:0000269|PubMed:9108029, ECO:0000269|PubMed:9207062, ECO:0000269|PubMed:9560228, ECO:0000269|PubMed:9804799}.; . . medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;cerebellum; 0.90033 0.75993 0.084621747 60.31493277 2444.74575 9.19703 APEX2 0.889124800888643 0.109708710988224 0.001166488123133 apurinic/apyrimidinic endodeoxyribonuclease 2 FUNCTION: Function as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Displays also double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes. {ECO:0000269|PubMed:11376153, ECO:0000269|PubMed:16687656, ECO:0000269|PubMed:19443450}.; . TISSUE SPECIFICITY: Highly expressed in brain and kidney. Weakly expressed in the fetal brain. {ECO:0000269|PubMed:11376153}.; . . 0.07453 0.13544 -0.558357437 19.54470394 50.55025 1.39924 APH1A 0.132136061884529 0.846230778305422 0.0216331598100487 aph-1 homolog A, gamma secretase subunit FUNCTION: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors and APP (beta-amyloid precursor protein). It probably represents a stabilizing cofactor for the presenilin homodimer that promotes the formation of a stable complex. {ECO:0000269|PubMed:12297508, ECO:0000269|PubMed:12522139, ECO:0000269|PubMed:12763021}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in leukocytes, lung, placenta, small intestine, liver, kidney, spleen thymus, skeletal muscle, heart and brain. Isoform 1 and isoform 2 are nearly expressed at the same level. {ECO:0000269|PubMed:12110170}.; medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;liver;kidney;trigeminal ganglion;skeletal muscle; 0.09513 0.10574 0.125076652 62.7388535 487.10045 4.54304 APH1B 0.000234972220416475 0.755441753216268 0.244323274563315 aph-1 homolog B, gamma secretase subunit FUNCTION: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors and APP (beta-amyloid precursor protein). It probably represents a stabilizing cofactor for the presenilin homodimer that promotes the formation of a stable complex. Probably present in a minority of gamma-secretase complexes compared to APH1A. {ECO:0000269|PubMed:12297508}.; . TISSUE SPECIFICITY: Weakly or not expressed in leukocytes, lung, placenta, small intestine, liver, kidney, spleen thymus, colon, skeletal muscle, heart and brain. {ECO:0000269|PubMed:12740439}.; unclassifiable (Anatomical System);medulla oblongata;heart;islets of Langerhans;adrenal cortex;colon;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;bone;placenta;thyroid;macula lutea;hippocampus;iris;liver;testis;germinal center;kidney; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.35427 0.17170 0.527368849 80.73248408 641.866 5.09067 API5 0.9995550190637 0.000444980638648005 2.97652335482444e-10 apoptosis inhibitor 5 FUNCTION: Antiapoptotic factor that may have a role in protein assembly. Negatively regulates ACIN1. By binding to ACIN1, it suppresses ACIN1 cleavage from CASP3 and ACIN1-mediated DNA fragmentation. Also known to efficiently suppress E2F1-induced apoptosis. Its depletion enhances the cytotoxic action of the chemotherapeutic drugs. {ECO:0000269|PubMed:10780674, ECO:0000269|PubMed:17112319, ECO:0000269|PubMed:19387494}.; . TISSUE SPECIFICITY: Expressed in all tissues tested, including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Highest levels in heart, pancreas and placenta. Highly expressed in several cancers. Preferentially expressed in squamous cell carcinoma versus adenocarcinoma in non-small cell lung cancer. {ECO:0000269|PubMed:10780674, ECO:0000269|PubMed:11075807, ECO:0000269|PubMed:11557113, ECO:0000269|PubMed:17827341, ECO:0000269|PubMed:19387494}.; . . 0.73412 0.11262 -0.339715008 30.06605331 24.0593 0.79110 API5P1 . . . apoptosis inhibitor 5 pseudogene 1 . . . . . . . . . . . API5P2 . . . apoptosis inhibitor 5 pseudogene 2 . . . . . . . . . . . APIP 4.19693047731044e-10 0.0278867813707392 0.972113218209568 APAF1 interacting protein FUNCTION: Catalyzes the dehydration of methylthioribulose-1- phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1- phosphate (DK-MTP-1-P). Functions in the methionine salvage pathway, which plays a key role in cancer, apoptosis, microbial proliferation and inflammation. May inhibit the CASP1-related inflammatory response (pyroptosis), the CASP9-dependent apoptotic pathway and the cytochrome c-dependent and APAF1-mediated cell death. {ECO:0000255|HAMAP-Rule:MF_03116, ECO:0000269|PubMed:15262985, ECO:0000269|PubMed:22837397, ECO:0000269|PubMed:23285211}.; . TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed. Isoform 2 is expressed at lower levels and detected in heart, brain, pancreas, liver, placenta, skeletal muscle and kidney. {ECO:0000269|PubMed:15262985, ECO:0000269|PubMed:23285211}.; ovary;salivary gland;intestine;colon;vein;skin;bone marrow;uterus;prostate;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);tongue;islets of Langerhans;adrenal cortex;pharynx;blood;breast;lung;nasopharynx;placenta;visual apparatus;liver;head and neck;kidney;stomach;aorta; . 0.20908 0.11983 0.68351529 85.03774475 6133.20242 16.36186 APITD1 0.00852090111528864 0.797466431746616 0.194012667138095 apoptosis-inducing, TAF9-like domain 1 FUNCTION: DNA-binding component of the FA core complex involved in DNA damage repair and genome maintenance. Required for optimal chromatin association of the FA core complex. Required for efficient damage-induced monoubiquitination and focus formation of FANCD2. Stabilizes FAAD24, FANCM and STRA13/CENPX in the FA core complex. Plays a role in DNA interstrand cross-linking (ICL) repair and in recovery of replication forks stalled by topoisomerase I-DNA cleavage intermediates induced by camptothecin. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. Component of the APITD1/CENPS complex that is essential for the stable assembly of the outer kinetochore. Plays an important role in mitotic progression and chromosome segregation. Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. {ECO:0000269|PubMed:19620631, ECO:0000269|Ref.7, ECO:0000269|Ref.8}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15328517}.; medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;lens;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;kidney;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; . 0.26604 0.21326276 67.71644256 . . APITD1-CORT 0.00852090111528864 0.797466431746616 0.194012667138095 APITD1-CORT readthrough FUNCTION: DNA-binding component of the FA core complex involved in DNA damage repair and genome maintenance. Required for optimal chromatin association of the FA core complex. Required for efficient damage-induced monoubiquitination and focus formation of FANCD2. Stabilizes FAAD24, FANCM and STRA13/CENPX in the FA core complex. Plays a role in DNA interstrand cross-linking (ICL) repair and in recovery of replication forks stalled by topoisomerase I-DNA cleavage intermediates induced by camptothecin. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. Component of the APITD1/CENPS complex that is essential for the stable assembly of the outer kinetochore. Plays an important role in mitotic progression and chromosome segregation. Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. {ECO:0000269|PubMed:19620631, ECO:0000269|Ref.7, ECO:0000269|Ref.8}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15328517}.; . . . . -0.163345027 41.24793583 8.85818 0.32639 APLF 1.13610489937719e-17 0.000357681873522644 0.999642318126477 aprataxin and PNKP like factor FUNCTION: Nuclease involved in single-strand and double-strand DNA break repair. Recruited to sites of DNA damage through interaction with poly(ADP-ribose), a polymeric post-translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions. Displays apurinic- apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro. Also able to introduce nicks at hydroxyuracil and other types of pyrimidine base damage. {ECO:0000269|PubMed:17353262, ECO:0000269|PubMed:17396150}.; . . unclassifiable (Anatomical System);uterus;frontal lobe;endometrium;liver;testis;parathyroid;spleen;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.05767 0.07325 1.065596954 91.61358811 2797.04688 9.97962 APLN 0.377456159057367 0.478364545108366 0.144179295834267 apelin FUNCTION: Endogenous ligand for APJ, an alternative coreceptor with CD4 for HIV-1 infection. Inhibits HIV-1 entry in cells coexpressing CD4 and APJ. Apelin-36 has a greater inhibitory activity on HIV infection than other synthetic apelin derivatives. The oral intake in the colostrum and the milk could have a role in the modulation of the immune responses in neonates. May also have a role in the central control of body fluid homeostasis by influencing AVP release and drinking behavior. {ECO:0000269|PubMed:11090199}.; . TISSUE SPECIFICITY: Expressed in the brain with highest levels in the frontal cortex, thalamus, hypothalamus and midbrain. Secreted by the mammary gland into the colostrum and the milk.; unclassifiable (Anatomical System);cartilage;heart;colon;vein;skin;uterus;lung;placenta;pituitary gland;liver;testis;head and neck;spleen;kidney;brain;aorta;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.01170 0.02875 . . 935.47718 5.92963 APLNR 0.432459659997125 0.535895393336301 0.0316449466665745 apelin receptor FUNCTION: Receptor for apelin coupled to G proteins that inhibit adenylate cyclase activity and plays a role in various processes in adults such as regulation of blood pressure, heart contractility, and heart failure. Also plays a key role in early development such as gastrulation and heart morphogenesis by acting as a receptor for APELA hormone. Alternative coreceptor with CD4 for HIV-1 infection; may be involved in the development of AIDS dementia.; . TISSUE SPECIFICITY: Widely expressed in the brain, in glial cells, astrocytes and neuronal subpopulations, as well as in the spleen, thymus, ovary, small intestine and colon.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;skin;uterus;pancreas;lung;endometrium;placenta;thyroid;visual apparatus;hippocampus;spleen;kidney;spinal ganglion;brain;mammary gland; amygdala;subthalamic nucleus;superior cervical ganglion;thalamus;olfactory bulb;hypothalamus;placenta;spinal cord;prefrontal cortex; 0.13024 0.19129 -0.622676946 17.30950696 105.96832 2.23213 APLP1 0.525926955621001 0.474067031807532 6.01257146777706e-06 amyloid beta precursor like protein 1 FUNCTION: May play a role in postsynaptic function. The C-terminal gamma-secretase processed fragment, ALID1, activates transcription activation through APBB1 (Fe65) binding (By similarity). Couples to JIP signal transduction through C-terminal binding. May interact with cellular G-protein signaling pathways. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the cerebral cortex where it is localized to the postsynaptic density (PSD). {ECO:0000269|PubMed:7494461}.; ovary;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;spleen;head and neck;cervix;kidney;cerebellum; whole brain;amygdala;occipital lobe;medulla oblongata;thalamus;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;pituitary;cingulate cortex;parietal lobe;cerebellum; 0.33364 0.61664 -0.683363435 15.36329323 122.57773 2.41099 APLP2 0.521618002879557 0.478375777531586 6.21958885730459e-06 amyloid beta precursor like protein 2 FUNCTION: May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5'-GTCACATG-3'(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kallikrein. Modulates the Cu/Zn nitric oxide-catalyzed autodegradation of GPC1 heparan sulfate side chains in fibroblasts (By similarity). {ECO:0000250, ECO:0000269|PubMed:8307156}.; . TISSUE SPECIFICITY: Expressed in placenta, brain, heart, lung, liver, kidney and endothelial tissues.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;brain;bladder;cartilage;heart;tongue;blood;lens;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;larynx;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta;cerebellum;thymus; dorsal root ganglion;subthalamic nucleus;medulla oblongata;thyroid;ciliary ganglion;atrioventricular node;cerebellum; 0.25600 0.20036 -0.709045403 14.673272 1494.60193 7.19150 APMAP 2.35566376172495e-07 0.70919657628449 0.290803188149134 adipocyte plasma membrane associated protein FUNCTION: Exhibits strong arylesterase activity with beta-naphthyl acetate and phenyl acetate. May play a role in adipocyte differentiation. {ECO:0000269|PubMed:18513186}.; . TISSUE SPECIFICITY: Liver, glomerular and tubular structures of the kidney, endothelial cells, arterial wall and pancreatic islets of Langerhans (at protein level). Found ubiquitously in adult as well as in embryonic tissues. In adult tissue, the highest expression is found in the liver, placenta and heart. Found on the cell surface of monocytes. In embryonic tissue, the highest expression levels is found in the liver and the kidney. {ECO:0000269|PubMed:18513186}.; . . 0.10489 0.10546 0.578735925 82.29535268 582.05286 4.89030 APOA1 0.0487383759438174 0.857667107395602 0.0935945166605809 apolipoprotein A-I FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. {ECO:0000269|PubMed:1909888}.; DISEASE: High density lipoprotein deficiency 2 (HDLD2) [MIM:604091]: Inherited as autosomal dominant trait. It is characterized by moderately low HDL cholesterol, predilection toward premature coronary artery disease (CAD) and a reduction in cellular cholesterol efflux. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: High density lipoprotein deficiency 1 (HDLD1) [MIM:205400]: Recessive disorder characterized by absence of high density lipoprotein (HDL) cholesterol from plasma, accumulation of cholesteryl esters, premature coronary artery disease (CAD), hepatosplenomegaly, recurrent peripheral neuropathy and progressive muscle wasting and weakness. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=APOA1 mutations may be involved in the pathogenesis of amyloid polyneuropathy-nephropathy Iowa type, also known as amyloidosis van Allen type or familial amyloid polyneuropathy type III (PubMed:3142462 and PubMed:2123470). The clinical picture is dominated by neuropathy in the early stages of the disease and nephropathy late in the course. Death is due in most cases to renal amyloidosis.; DISEASE: Amyloidosis 8 (AMYL8) [MIM:105200]: A hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash. {ECO:0000269|PubMed:1502149, ECO:0000269|PubMed:2123470, ECO:0000269|PubMed:3142462, ECO:0000269|PubMed:8208902}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Major protein of plasma HDL, also found in chylomicrons. Synthesized in the liver and small intestine. The oxidized form at Met-110 and Met-136 is increased in individuals with increased risk for coronary artery disease, such as in carrier of the eNOSa/b genotype and exposure to cigarette smoking. It is also present in increased levels in aortic lesions relative to native ApoA-I and increased levels are seen with increasing severity of disease. {ECO:0000269|PubMed:12576517}.; lymphoreticular;unclassifiable (Anatomical System);myocardium;medulla oblongata;ovary;colon;parathyroid;pancreas;whole body;lung;placenta;liver;testis;spleen;brain;gall bladder;thymus; fetal liver;testis - interstitial;testis - seminiferous tubule;heart;liver;testis;fetal lung;skeletal muscle; 0.34295 . -0.471992905 23.03609342 41.96842 1.22268 APOA1-AS . . . APOA1 antisense RNA . . . . . . . . . . . APOA2 0.00943705539989373 0.59116994591114 0.399392998688966 apolipoprotein A-II FUNCTION: May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism.; . TISSUE SPECIFICITY: Plasma; synthesized in the liver and intestine.; . . 0.65547 0.43086 -0.031067188 51.03798066 1.71247 0.05610 APOA4 3.57595118139907e-05 0.592175436933719 0.407788803554467 apolipoprotein A-IV FUNCTION: May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.; . TISSUE SPECIFICITY: Synthesized primarily in the intestine and secreted in plasma.; pancreas;liver;colon;stomach; trigeminal ganglion; 0.09504 0.09686 0.358272123 74.66383581 246.2813 3.38677 APOA5 1.37735073361006e-06 0.218565344209404 0.781433278439863 apolipoprotein A-V FUNCTION: Minor apolipoprotein mainly associated with HDL and to a lesser extent with VLDL. May also be associated with chylomicrons. Important determinant of plasma triglyceride (TG) levels by both being a potent stimulator of apo-CII lipoprotein lipase (LPL) TG hydrolysis and a inhibitor of the hepatic VLDL-TG production rate (without affecting the VLDL-apoB production rate) (By similarity). Activates poorly lecithin:cholesterol acyltransferase (LCAT) and does not enhance efflux of cholesterol from macrophages. {ECO:0000250, ECO:0000269|PubMed:11588264, ECO:0000269|PubMed:12899628, ECO:0000269|PubMed:15528295}.; DISEASE: Hypertriglyceridemia, familial (FHTR) [MIM:145750]: A common inherited disorder in which the concentration of very low density lipoprotein (VLDL) is elevated in the plasma. This leads to increased risk of heart disease, obesity, and pancreatitis. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Hyperlipoproteinemia 5 (HLPP5) [MIM:144650]: Characterized by increased amounts of chylomicrons and very low density lipoprotein (VLDL) and decreased low density lipoprotein (LDL) and high density lipoprotein (HDL) in the plasma after a fast. Numerous conditions cause this phenotype, including insulin- dependent diabetes mellitus, contraceptive steroids, alcohol abuse, and glycogen storage disease type 1A (GSD1A). {ECO:0000269|PubMed:16200213}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver and plasma. {ECO:0000269|PubMed:11577099, ECO:0000269|PubMed:11588264, ECO:0000269|PubMed:15528295}.; liver; dorsal root ganglion;superior cervical ganglion;liver;trigeminal ganglion; 0.27368 0.35715 0.418953042 77.06416608 831.91915 5.65168 APOB 5.49085163436995e-16 0.999999987453892 1.2546107885403e-08 apolipoprotein B FUNCTION: Apolipoprotein B is a major protein constituent of chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-100 functions as a recognition signal for the cellular binding and internalization of LDL particles by the apoB/E receptor.; DISEASE: Hypobetalipoproteinemia, familial, 1 (FHBL1) [MIM:615558]: A disorder of lipid metabolism characterized by less than 5th percentile age- and sex-specific levels of low density lipoproteins, and dietary fat malabsorption. Clinical presentation may vary from no symptoms to severe gastrointestinal and neurological dysfunction similar to abetalipoproteinemia. {ECO:0000269|PubMed:12551903, ECO:0000269|PubMed:21981844}. Note=The disease is caused by mutations affecting the gene represented in this entry. Most cases of FHBL1 result from nonsense mutations in the APOB gene that lead to a premature stop codon, which generate prematurely truncated apo B protein products (PubMed:21981844). {ECO:0000269|PubMed:21981844}.; DISEASE: Familial ligand-defective apolipoprotein B-100 (FDB) [MIM:144010]: Dominantly inherited disorder of lipoprotein metabolism leading to hypercholesterolemia and increased proneness to coronary artery disease (CAD). The plasma cholesterol levels are dramatically elevated due to impaired clearance of LDL particles by defective APOB/E receptors. {ECO:0000269|PubMed:21382890, ECO:0000269|PubMed:2563166, ECO:0000269|PubMed:7883971, ECO:0000269|PubMed:9259199}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in APOB associated with defects in other genes (polygenic) can contribute to hypocholesterolemia.; . ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;bone;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);small intestine;heart;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; fetal liver;superior cervical ganglion;liver;fetal lung; 0.45035 0.88273 1.41604242 94.84548243 12742.91619 24.16263 APOBEC1 0.000144861579102738 0.65464515072722 0.345209987693677 apolipoprotein B mRNA editing enzyme catalytic subunit 1 FUNCTION: Catalytic component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in the APOB mRNA. Also involved in CGA (Arg) to UGA (Stop) editing in the NF1 mRNA. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. {ECO:0000269|PubMed:11727199}.; . TISSUE SPECIFICITY: Expressed exclusively in the small intestine.; colon;blood; superior cervical ganglion; 0.12544 0.14891 1.126294249 92.16206653 82.9695 1.93477 APOBEC2 0.132007272868405 0.780162685562718 0.0878300415688774 apolipoprotein B mRNA editing enzyme catalytic subunit 2 FUNCTION: Probable C to U editing enzyme whose physiological substrate is not yet known. Does not display detectable apoB mRNA editing. Has a low intrinsic cytidine deaminase activity. May play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation. {ECO:0000269|PubMed:17187054, ECO:0000269|PubMed:21496894}.; . TISSUE SPECIFICITY: Expressed exclusively in heart and skeletal muscle.; unclassifiable (Anatomical System);myocardium;heart;ovary;islets of Langerhans;muscle;parathyroid;skeletal muscle;prostate;whole body;lung;placenta;visual apparatus;liver;testis;brain; superior cervical ganglion;tongue;ciliary ganglion;pons;atrioventricular node;skeletal muscle; 0.70533 0.12032 0.549415813 81.38122199 1216.14196 6.59779 APOBEC3A 0.22634791867463 0.738253031425622 0.0353990498997487 apolipoprotein B mRNA editing enzyme catalytic subunit 3A FUNCTION: DNA deaminase (cytidine deaminase) with restriction activity against viruses, foreign DNA and mobility of retrotransposons. Exhibits antiviral activity against adeno- associated virus (AAV) and human T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons. Selectively targets single-stranded DNA and can deaminate both methylcytosine and cytosine in foreign DNA. Can induce somatic hypermutation in the nuclear and mitochondrial DNA. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation. {ECO:0000269|PubMed:10469298, ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:19461882, ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:20615867, ECO:0000269|PubMed:21123384, ECO:0000269|PubMed:21368204, ECO:0000269|PubMed:21460793, ECO:0000269|PubMed:21496894, ECO:0000269|PubMed:22457529, ECO:0000269|PubMed:22896697}.; . TISSUE SPECIFICITY: Expressed in peripheral leukocytes with higher expression in CD14-positive phagocytic cells. Highly expressed in keratinocytes and in periphery blood monocytes. Also detected in non-lymphoid tissues including lung and adipose tissues. Found at high levels in colorectal adenocarcinoma, Burkitt's lymphoma and chronic myelogenous leukemia. {ECO:0000269|PubMed:11863358, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:20308164}.; unclassifiable (Anatomical System);larynx;visual apparatus;blood;head and neck;pons;bone marrow; superior cervical ganglion;whole blood; 0.03694 . 0.371224249 75.12384996 17.04918 0.60008 APOBEC3AP1 . . . apolipoprotein B mRNA editing enzyme catalytic subunit 3A pseudogene 1 . . . . . . . . . . . APOBEC3A_B . . . APOBEC3A and APOBEC3B deletion hybrid FUNCTION: DNA deaminase (cytidine deaminase) with restriction activity against viruses, foreign DNA and mobility of retrotransposons. Exhibits antiviral activity against adeno- associated virus (AAV) and human T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons. Selectively targets single-stranded DNA and can deaminate both methylcytosine and cytosine in foreign DNA. Can induce somatic hypermutation in the nuclear and mitochondrial DNA. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation. {ECO:0000269|PubMed:10469298, ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:19461882, ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:20615867, ECO:0000269|PubMed:21123384, ECO:0000269|PubMed:21368204, ECO:0000269|PubMed:21460793, ECO:0000269|PubMed:21496894, ECO:0000269|PubMed:22457529, ECO:0000269|PubMed:22896697}.; . TISSUE SPECIFICITY: Expressed in peripheral leukocytes with higher expression in CD14-positive phagocytic cells. Highly expressed in keratinocytes and in periphery blood monocytes. Also detected in non-lymphoid tissues including lung and adipose tissues. Found at high levels in colorectal adenocarcinoma, Burkitt's lymphoma and chronic myelogenous leukemia. {ECO:0000269|PubMed:11863358, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:20308164}.; . . . . . . . . APOBEC3B 2.50835391870874e-05 0.918953352643358 0.0810215638174553 apolipoprotein B mRNA editing enzyme catalytic subunit 3B FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination- independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double- stranded RNA. Exhibits antiviral activity against simian immunodeficiency virus (SIV), hepatitis B virus (HBV) and human T- cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons. {ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:15466872, ECO:0000269|PubMed:16060832, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:22457529}.; . TISSUE SPECIFICITY: Expressed at high and moderate levels in peripheral blood leukocytes, spleen, testes, heart, thymus, prostate and ovary. Also expressed at low levels in several other tissues. {ECO:0000269|PubMed:11863358, ECO:0000269|PubMed:20308164}.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;parathyroid;blood;skin;uterus;prostate;larynx;bone;thyroid;placenta;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;brain;bladder;stomach; atrioventricular node;trigeminal ganglion; 0.11372 . 2.201139331 98.12455768 954.69441 5.98125 APOBEC3B-AS1 . . . APOBEC3B antisense RNA 1 . . . . . . . . . . . APOBEC3C 0.0926245609517721 0.868944472783029 0.0384309662651994 apolipoprotein B mRNA editing enzyme catalytic subunit 3C FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination- independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double- stranded RNA. Exhibits antiviral activity against simian immunodeficiency virus (SIV), hepatitis B virus (HBV), herpes simplex virus 1 (HHV-1) and Epstein-Barr virus (EBV) and may inhibit the mobility of LTR and non-LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation. {ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:15466872, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:21496894, ECO:0000269|PubMed:21632763}.; . TISSUE SPECIFICITY: Expressed in spleen, testes, peripherical blood lymphocytes, heart, thymus, prostate and ovary. {ECO:0000269|PubMed:11863358, ECO:0000269|PubMed:20308164}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;larynx;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;lung;nasopharynx;placenta;hippocampus;liver;head and neck;spleen;kidney;mammary gland;aorta;stomach; testis; . 0.05922 -0.271755481 34.31823543 21.19902 0.71583 APOBEC3D 2.35516694213337e-05 0.912736699282701 0.0872397490478774 apolipoprotein B mRNA editing enzyme catalytic subunit 3D FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination- independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double- stranded RNA. May inhibit the mobility of LTR and non-LTR retrotransposons. {ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:22807680, ECO:0000269|PubMed:23097438, ECO:0000269|PubMed:23152537}.; . TISSUE SPECIFICITY: Expressed in lymphoid organs. Also detected in non-lymphoid tissues including lung. {ECO:0000269|PubMed:20308164}.; lung;thyroid;head and neck; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; . 0.04922 -0.157884861 42.05590941 49.3236 1.37327 APOBEC3F 0.0139601925830727 0.979586884378321 0.0064529230386064 apolipoprotein B mRNA editing enzyme catalytic subunit 3F FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination- independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double- stranded RNA. Exhibits antiviral activity also against hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV) and may inhibit the mobility of LTR and non-LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation. {ECO:0000269|PubMed:15152192, ECO:0000269|PubMed:16378963, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:19458006, ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:20219927, ECO:0000269|PubMed:20335265, ECO:0000269|PubMed:21496894, ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:22807680, ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:23097438, ECO:0000269|PubMed:23152537}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in ovary. {ECO:0000269|PubMed:11863358, ECO:0000269|PubMed:15152192, ECO:0000269|PubMed:20308164}.; unclassifiable (Anatomical System);prostate;pancreas;lung;colon;germinal center;skin;tonsil; globus pallidus; . 0.05074 1.177658736 92.77541873 726.67398 5.35373 APOBEC3G 1.47030454091374e-06 0.624373291772858 0.375625237922601 apolipoprotein B mRNA editing enzyme catalytic subunit 3G FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits potent antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination- independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double- stranded RNA. Exhibits antiviral activity also against simian immunodeficiency viruses (SIVs), hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV). May inhibit the mobility of LTR and non-LTR retrotransposons. {ECO:0000269|PubMed:12167863, ECO:0000269|PubMed:12808465, ECO:0000269|PubMed:12808466, ECO:0000269|PubMed:12809610, ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:12970355, ECO:0000269|PubMed:14528300, ECO:0000269|PubMed:14557625, ECO:0000269|PubMed:15031497, ECO:0000269|PubMed:16378963, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:18288108, ECO:0000269|PubMed:19458006, ECO:0000269|PubMed:20219927, ECO:0000269|PubMed:20335265, ECO:0000269|PubMed:21123384, ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:22791714, ECO:0000269|PubMed:22807680, ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:23097438, ECO:0000269|PubMed:23152537}.; . TISSUE SPECIFICITY: Expressed in spleen, testes, ovary and peripheral blood leukocytes and CD4+ lymphocytes. Also expressed in non-permissive peripheral blood mononuclear cells, and several tumor cell lines; no expression detected in permissive lymphoid and non-lymphoid cell lines. Exists only in the LMM form in peripheral blood-derived resting CD4 T-cells and monocytes, both of which are refractory to HIV-1 infection. LMM is converted to a HMM complex when resting CD4 T-cells are activated or when monocytes are induced to differentiate into macrophages. This change correlates with increased susceptibility of these cells to HIV-1 infection. {ECO:0000269|PubMed:11863358, ECO:0000269|PubMed:12167863, ECO:0000269|PubMed:20308164}.; . . . 0.05680 0.066214104 58.95848077 300.63427 3.69638 APOBEC3H 0.637623187325877 0.355699122507337 0.00667769016678615 apolipoprotein B mRNA editing enzyme catalytic subunit 3H FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. The A3H- var/haplotype 2 exhibits antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single- stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. Exhibits antiviral activity also against T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons. {ECO:0000269|PubMed:16571802, ECO:0000269|PubMed:16920826, ECO:0000269|PubMed:18299330, ECO:0000269|PubMed:18779051, ECO:0000269|PubMed:18827027, ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:22457529, ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:23097438}.; . TISSUE SPECIFICITY: Expressed in lymphoid organs. Also detected in non-lymphoid tissues including lung, testis, ovary, fetal liver and skin. {ECO:0000269|PubMed:16571802, ECO:0000269|PubMed:20308164}.; unclassifiable (Anatomical System);thyroid;placenta;blood;nose;thymus; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.03807 0.11857 0.705562627 85.52724699 3553.79975 11.52391 APOBEC4 0.000618475417657442 0.487577358084444 0.511804166497899 apolipoprotein B mRNA editing enzyme catalytic polypeptide like 4 FUNCTION: Putative C to U editing enzyme whose physiological substrate is not yet known. {ECO:0000250}.; . TISSUE SPECIFICITY: Predominantly expressed in testis. {ECO:0000269|PubMed:16082223}.; unclassifiable (Anatomical System);medulla oblongata;lung;ovary;endometrium;nasopharynx;thyroid;placenta;testis;parathyroid;spleen;brain; . 0.09989 0.08973 2.107460923 97.88275537 2245.63605 8.74518 APOBR 6.29744462573012e-06 0.698172076796568 0.301821625758806 apolipoprotein B receptor FUNCTION: Macrophage receptor that binds to the apolipoprotein B48 (APOB) of dietary triglyceride (TG)-rich lipoproteins (TRL) or to a like domain of APOB in hypertriglyceridemic very low density lipoprotein (HTG-VLDL). Binds and internalizes TRL when out of the context of the macrophage. May provide essential lipids to reticuloendothelial cells. Could also be involved in foam cell formation with elevated TRL and remnant lipoprotein (RLP). Mediates the rapid high-affinity uptake of chylomicrons (CM), HTG- VLDL, and trypsinized (tryp) VLDL devoid of APOE in vitro in macrophages. {ECO:0000269|PubMed:10852956, ECO:0000269|PubMed:15591219, ECO:0000269|PubMed:9633939}.; . TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes > bone marrow = spleen > lymph node, and only faintly visible in appendix and thymus. Expressed in the brain, heart, kidney, liver, lung, pancreas, and placenta. Expressed primarily by reticuloendothelial cells: monocytes, macrophages, and endothelial cells. Expressed in atherosclerotic lesion foam cells. {ECO:0000269|PubMed:10191299, ECO:0000269|PubMed:10852956}.; unclassifiable (Anatomical System);uterus;lung;adrenal gland;liver;colon;blood;brain;bone marrow; whole blood; . . . . 2747.21109 9.88128 APOC1 0.0507382728810443 0.691173387480155 0.258088339638801 apolipoprotein C-I FUNCTION: Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein. {ECO:0000269|PubMed:17339654, ECO:0000303|PubMed:25160599}.; . TISSUE SPECIFICITY: Synthesized mainly in liver and to a minor degree in intestine. Also found in the lung and spleen. {ECO:0000269|PubMed:2835369}.; ovary;salivary gland;intestine;colon;skin;retina;uterus;prostate;thyroid;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;trophoblast;heart;pineal body;pharynx;blood;skeletal muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus; fetal liver;adipose tissue;adrenal gland;liver;adrenal cortex;fetal lung;caudate nucleus; 0.09440 0.47132 -0.053113545 49.38664779 30.95619 0.97866 APOC1P1 . . . apolipoprotein C-I pseudogene 1 . . . . . . . . . . . APOC2 0.0227961322934307 0.765763861998575 0.211440005707994 apolipoprotein C-II FUNCTION: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein lipase. In normolipidemic individuals, it is mainly distributed in the HDL, whereas in hypertriglyceridemic individuals, predominantly found in the VLDL and LDL. {ECO:0000269|PubMed:2209608, ECO:0000303|PubMed:22304839}.; DISEASE: Hyperlipoproteinemia 1B (HLPP1B) [MIM:207750]: Autosomal recessive trait characterized by hypertriglyceridemia, xanthomas, and increased risk of pancreatitis and early atherosclerosis. {ECO:0000269|PubMed:8323539}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver and intestine. {ECO:0000269|PubMed:6546757}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;pharynx;blood;lens;breast;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland; amygdala;thalamus;fetal liver;hypothalamus;spinal cord;liver;fetal lung; 0.08282 0.10297 0.769889969 86.95447039 . . APOC3 0.00067802640410586 0.506712772333524 0.49260920126237 apolipoprotein C-III FUNCTION: Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors. {ECO:0000303|PubMed:18201179, ECO:0000303|PubMed:22510806}.; DISEASE: Hyperalphalipoproteinemia 2 (HALP2) [MIM:614028]: A condition characterized by high levels of high density lipoprotein (HDL) and increased HDL cholesterol levels. {ECO:0000269|PubMed:2022742}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:6328445}.; unclassifiable (Anatomical System);uterus;pancreas;whole body;heart;liver;spleen;kidney;brain;skin; superior cervical ganglion;fetal liver;prostate;liver;fetal lung;skin;skeletal muscle; 0.33135 0.73068 0.369407109 74.95281906 21.59679 0.72605 APOC4 0.000150692347626422 0.248345294803309 0.751504012849064 apolipoprotein C-IV FUNCTION: May participate in lipoprotein metabolism.; . TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; . . 0.15467 0.29589 0.815800671 87.8744987 1530.66665 7.27132 APOC4-APOC2 . . . APOC4-APOC2 readthrough (NMD candidate) . . . . . . . . . 73.32352 1.78921 APOD 0.000853904292818293 0.55588390299401 0.443262192713172 apolipoprotein D FUNCTION: APOD occurs in the macromolecular complex with lecithin- cholesterol acyltransferase. It is probably involved in the transport and binding of bilin. Appears to be able to transport a variety of ligands in a number of different contexts.; . TISSUE SPECIFICITY: Expressed in liver, intestine, pancreas, kidney, placenta, adrenal, spleen, fetal brain tissue and tears.; lymphoreticular;myocardium;ovary;sympathetic chain;parathyroid;choroid;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;testis;dura mater;brain;pineal gland;unclassifiable (Anatomical System);meninges;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;pineal body;spinal cord;muscle;adrenal cortex;skeletal muscle;breast;pia mater;lung;cornea;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;medulla oblongata;superior cervical ganglion;occipital lobe;thalamus;adipose tissue;olfactory bulb;spinal cord;caudate nucleus;atrioventricular node;skeletal muscle;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.03147 0.41760 0.77170517 87.00754895 93.19434 2.07679 APOE 0.0345335830833016 0.825584386696493 0.139882030220206 apolipoprotein E FUNCTION: Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues. {ECO:0000303|PubMed:3283935}.; DISEASE: Hyperlipoproteinemia 3 (HLPP3) [MIM:107741]: A disorder characterized by the accumulation of intermediate-density lipoprotein particles (IDL or broad-beta-lipoprotein) rich in cholesterol. Clinical features include xanthomas, yellowish lipid deposits in the palmar crease, or less specific on tendons and on elbows. The disorder rarely manifests before the third decade in men. In women, it is usually expressed only after the menopause. {ECO:0000269|PubMed:1674745, ECO:0000269|PubMed:22481068, ECO:0000269|PubMed:2556398, ECO:0000269|PubMed:8287539}. Note=The disease is caused by mutations affecting the gene represented in this entry. The vast majority of the patients are homozygous for APOE*2 alleles. More severe cases of HLPP3 have also been observed in individuals heterozygous for rare APOE variants. The influence of APOE on lipid levels is often suggested to have major implications for the risk of coronary artery disease (CAD). Individuals carrying the common APOE*4 variant are at higher risk of CAD.; DISEASE: Alzheimer disease 2 (AD2) [MIM:104310]: A late-onset neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. The APOE*4 allele is genetically associated with the common late onset familial and sporadic forms of Alzheimer disease. Risk for AD increased from 20% to 90% and mean age at onset decreased from 84 to 68 years with increasing number of APOE*4 alleles in 42 families with late onset AD. Thus APOE*4 gene dose is a major risk factor for late onset AD and, in these families, homozygosity for APOE*4 was virtually sufficient to cause AD by age 80. The mechanism by which APOE*4 participates in pathogenesis is not known.; DISEASE: Sea-blue histiocyte disease (SBHD) [MIM:269600]: Characterized by splenomegaly, mild thrombocytopenia and, in the bone marrow, numerous histiocytes containing cytoplasmic granules which stain bright blue with the usual hematologic stains. The syndrome is the consequence of an inherited metabolic defect analogous to Gaucher disease and other sphingolipidoses. {ECO:0000269|PubMed:11095479, ECO:0000269|PubMed:16094309}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Lipoprotein glomerulopathy (LPG) [MIM:611771]: Uncommon kidney disease characterized by proteinuria, progressive kidney failure, and distinctive lipoprotein thrombi in glomerular capillaries. {ECO:0000269|PubMed:10432380, ECO:0000269|PubMed:18077821, ECO:0000269|PubMed:9176854}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Familial hypercholesterolemia (FH) [MIM:143890]: Common autosomal semi-dominant disease that affects about 1 in 500 individuals. The receptor defect impairs the catabolism of LDL, and the resultant elevation in plasma LDL-cholesterol promotes deposition of cholesterol in the skin (xanthelasma), tendons (xanthomas), and coronary arteries (atherosclerosis). {ECO:0000269|PubMed:22949395}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Occurs in all lipoprotein fractions in plasma. It constitutes 10-20% of very low density lipoproteins (VLDL) and 1-2% of high density lipoproteins (HDL). APOE is produced in most organs. Significant quantities are produced in liver, brain, spleen, lung, adrenal, ovary, kidney and muscle.; medulla oblongata;ovary;colon;skin;retina;uterus;prostate;frontal lobe;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; amygdala;fetal liver;adipose tissue;adrenal gland;hypothalamus;liver;adrenal cortex;ciliary ganglion;caudate nucleus;pons;kidney; 0.27537 0.99756 . . 1533.87452 7.27606 APOF 0.0193380084394216 0.90029435417243 0.0803676373881482 apolipoprotein F FUNCTION: Minor apolipoprotein that associates with LDL. Inhibits cholesteryl ester transfer protein (CETP) activity and appears to be an important regulator of cholesterol transport. Also associates to a lesser degree with VLDL, Apo-AI and Apo-AII. {ECO:0000269|PubMed:9880564}.; . TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. {ECO:0000269|PubMed:8093033}.; . . 0.24502 0.14509 0.72761005 86.08162302 780.95405 5.52861 APOH 1.28717988796445e-10 0.0510831269751235 0.948916872896159 apolipoprotein H FUNCTION: Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells.; . TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;salivary gland;intestine;pharynx;colon;parathyroid;blood;skin;skeletal muscle;breast;prostate;whole body;lung;placenta;visual apparatus;liver;spleen;kidney;brain;bladder; superior cervical ganglion;fetal liver;beta cell islets;liver;fetal lung;kidney; 0.26884 0.64999 0.953537969 90.08610521 798.50918 5.56925 APOL1 3.75078410438376e-08 0.189758347729351 0.810241614762808 apolipoprotein L1 FUNCTION: May play a role in lipid exchange and transport throughout the body. May participate in reverse cholesterol transport from peripheral cells to the liver.; DISEASE: Focal segmental glomerulosclerosis 4 (FSGS4) [MIM:612551]: A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation. {ECO:0000269|PubMed:20635188, ECO:0000269|PubMed:20647424}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma. Found on APOA-I-containing high density lipoprotein (HDL3). Expressed in pancreas, lung, prostate, liver, placenta and spleen.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;ileum;prostate;optic nerve;frontal lobe;endometrium;oesophagus;synovium;larynx;motor;bone;penis;globus pallidus;testis;brain;artery;bladder;tonsil;gall bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;hypopharynx;liver;head and neck;kidney;aorta;stomach; liver;ciliary ganglion;skeletal muscle; 0.01629 . 1.445891753 95.12267044 598.01645 4.95097 APOL2 0.000139187047584769 0.645963099667123 0.353897713285292 apolipoprotein L2 FUNCTION: May affect the movement of lipids in the cytoplasm or allow the binding of lipids to organelles.; . TISSUE SPECIFICITY: Widely expressed; the highest levels are found in lung, thymus, pancreas, placenta, adult brain and prostate; also detected in spleen, liver, kidney, colon, small intestine, uterus, spinal cord, adrenal gland, salivary gland, trachea, mammary gland, skeletal muscle, testis and fetal brain and liver.; ovary;salivary gland;intestine;colon;choroid;skin;uterus;prostate;atrium;frontal lobe;endometrium;bone;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;mesenchyma;placenta;visual apparatus;hippocampus;amnion;duodenum;liver;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; superior cervical ganglion;globus pallidus;atrioventricular node;skeletal muscle; 0.02665 0.05082 0.198490371 67.30360934 2545.43831 9.42241 APOL3 2.87221559841753e-05 0.544556418018931 0.455414859825085 apolipoprotein L3 FUNCTION: May affect the movement of lipids in the cytoplasm or allow the binding of lipids to organelles.; . TISSUE SPECIFICITY: Widely expressed; the highest levels are in prostate, lung and placenta; also detected in kidney, bone marrow, spleen, thymus, spinal cord, adrenal gland, salivary gland, trachea and mammary gland; levels are low in brain, heart, fetal liver, pancreas and testis.; ovary;colon;parathyroid;choroid;skin;uterus;endometrium;penis;thyroid;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;breast;lung;placenta;liver;alveolus;spleen;cervix;kidney;stomach; ciliary ganglion;skeletal muscle; 0.04356 . 1.177658736 92.77541873 452.89073 4.42766 APOL4 9.93032452582808e-05 0.572196259139752 0.42770443761499 apolipoprotein L4 FUNCTION: May play a role in lipid exchange and transport throughout the body. May participate in reverse cholesterol transport from peripheral cells to the liver (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed; the highest levels are in spinal cord, placenta, adrenal gland; also detected in spleen, bone marrow, uterus, trachea, mammary gland and testis; levels are low in brain, heart and pancreas.; unclassifiable (Anatomical System);placenta;liver; pancreas;atrioventricular node;trigeminal ganglion; 0.07185 0.07955 . . 397.8891 4.19110 APOL5 1.00622472238021e-08 0.17003207318269 0.829967916755063 apolipoprotein L5 FUNCTION: May affect the movement of lipids in the cytoplasm or allow the binding of lipids to organelles.; . TISSUE SPECIFICITY: Low level of expression; detected in uterus, testis, skeletal muscle and stomach.; unclassifiable (Anatomical System);ovary;placenta;parathyroid;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle;parietal lobe;bone marrow; 0.05935 . 0.887394731 89.18966737 7067.29 18.01366 APOL6 0.00070410760470988 0.514655619709329 0.484640272685961 apolipoprotein L6 FUNCTION: May affect the movement of lipids in the cytoplasm or allow the binding of lipids to organelles.; . TISSUE SPECIFICITY: Widely expressed; highly expressed in the uterus, fetal brain and spinal cord, also detected in heart, liver, lung, colon, spleen, thymus, prostate, placenta, adrenal gland, salivary and mammary gland.; . . . . -0.201976964 38.98325077 59.45366 1.56415 APOLD1 0.000507905443363466 0.447736382389936 0.5517557121667 apolipoprotein L domain containing 1 FUNCTION: May be involved in angiogenesis. May play a role in activity-dependent changes of brain vasculature. May affect blood- brain permeability. {ECO:0000269|PubMed:15102925}.; . TISSUE SPECIFICITY: Expressed in neonatal dermal microvascular endothelial cells. {ECO:0000269|PubMed:15102925}.; colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;oesophagus;endometrium;bone;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;pia mater;lung;placenta;macula lutea;hippocampus;liver;kidney;stomach; superior cervical ganglion;placenta;prefrontal cortex;atrioventricular node; 0.15760 . . . 512.24211 4.63309 APOM 0.00854307555982986 0.797906805064143 0.193550119376027 apolipoprotein M FUNCTION: Probably involved in lipid transport. Can bind sphingosine-1-phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-trans-retinoic acid and 9-cis-retinoic acid. {ECO:0000269|PubMed:17525477, ECO:0000269|PubMed:19733574}.; . TISSUE SPECIFICITY: Plasma protein. Expressed in liver and kidney.; . . 0.68759 . 0.125076652 62.7388535 41.6362 1.21298 APOO 0.754113198235746 0.243795678456359 0.00209112330789503 apolipoprotein O FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a crucial role in crista junction formation and mitochondrial function (PubMed:25764979). Can promote cardiac lipotoxicity by enhancing mitochondrial respiration and fatty acid metabolism in cardiac myoblasts (PubMed:24743151). Promotes cholesterol efflux from macrophage cells. Detected in HDL, LDL and VLDL. Secreted by a microsomal triglyceride transfer protein (MTTP)-dependent mechanism, probably as a VLDL-associated protein that is subsequently transferred to HDL (PubMed:16956892). {ECO:0000269|PubMed:16956892, ECO:0000269|PubMed:24743151, ECO:0000269|PubMed:25764979}.; . TISSUE SPECIFICITY: Expressed in all tissues examined. Up- regulated in diabetic heart. {ECO:0000269|PubMed:16956892}.; . . 0.37074 0.11532 0.525552348 80.57914603 137.43655 2.54975 APOOL 0.86631270153769 0.13179444755454 0.00189285090777011 apolipoprotein O like FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Specifically binds to cardiolipin (in vitro) but not to the precursor lipid phosphatidylglycerol. Plays a crucial role in crista junction formation and mitochondrial function (PubMed:23704930), (PubMed:25764979). {ECO:0000269|PubMed:23704930, ECO:0000269|PubMed:25764979}.; . . . . 0.12091 . -0.073340031 48.11866006 35.01323 1.06264 APOOP1 . . . apolipoprotein O pseudogene 1 . . . . . . . . . . . APOOP2 . . . apolipoprotein O pseudogene 2 . . . . . . . . . . . APOOP3 . . . apolipoprotein O pseudogene 3 . . . . . . . . . . . APOOP4 . . . apolipoprotein O pseudogene 4 . . . . . . . . . . . APOOP5 . . . apolipoprotein O pseudogene 5 . . . . . . . . . . . APOPT1 0.000361375806098766 0.61120197153549 0.388436652658411 apoptogenic 1, mitochondrial FUNCTION: Plays a role in the regulation of apoptosis. Mediates mitochondria-induced cell death in vascular smooth muscle cells through the release of cytochrome c from mitochondria, followed by the activation of the caspase cascade. {ECO:0000250|UniProtKB:Q9CQW7}.; . . . . 0.11985 0.10135 0.014844891 54.94810097 903.08755 5.85033 APP 0.331710617165879 0.668288281579227 1.1012548939501e-06 amyloid beta precursor protein FUNCTION: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER- dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. {ECO:0000250}.; FUNCTION: Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain. {ECO:0000250}.; FUNCTION: N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).; DISEASE: Alzheimer disease 1 (AD1) [MIM:104300]: A familial early- onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. {ECO:0000269|PubMed:10097173, ECO:0000269|PubMed:10631141, ECO:0000269|PubMed:10665499, ECO:0000269|PubMed:10867787, ECO:0000269|PubMed:11063718, ECO:0000269|PubMed:11528419, ECO:0000269|PubMed:12034808, ECO:0000269|PubMed:1302033, ECO:0000269|PubMed:1303239, ECO:0000269|PubMed:1303275, ECO:0000269|PubMed:1415269, ECO:0000269|PubMed:15201367, ECO:0000269|PubMed:15365148, ECO:0000269|PubMed:15668448, ECO:0000269|PubMed:1671712, ECO:0000269|PubMed:1678058, ECO:0000269|PubMed:1908231, ECO:0000269|PubMed:1925564, ECO:0000269|PubMed:1944558, ECO:0000269|PubMed:8267572, ECO:0000269|PubMed:8290042, ECO:0000269|PubMed:8476439, ECO:0000269|PubMed:8577393, ECO:0000269|PubMed:9328472, ECO:0000269|PubMed:9754958}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cerebral amyloid angiopathy, APP-related (CAA-APP) [MIM:605714]: A hereditary localized amyloidosis due to amyloid- beta A4 peptide(s) deposition in the cerebral vessels. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque- like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease. Some affected individuals manifest progressive aphasic dementia, leukoencephalopathy, and occipital calcifications. {ECO:0000269|PubMed:11409420, ECO:0000269|PubMed:12654973, ECO:0000269|PubMed:16178030, ECO:0000269|PubMed:20697050, ECO:0000269|PubMed:2111584}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all fetal tissues examined with highest levels in brain, kidney, heart and spleen. Weak expression in liver. In adult brain, highest expression found in the frontal lobe of the cortex and in the anterior perisylvian cortex- opercular gyri. Moderate expression in the cerebellar cortex, the posterior perisylvian cortex-opercular gyri and the temporal associated cortex. Weak expression found in the striate, extra- striate and motor cortices. Expressed in cerebrospinal fluid, and plasma. Isoform APP695 is the predominant form in neuronal tissue, isoform APP751 and isoform APP770 are widely expressed in non- neuronal cells. Isoform APP751 is the most abundant form in T- lymphocytes. Appican is expressed in astrocytes. {ECO:0000269|PubMed:12859342, ECO:0000269|PubMed:1406936}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;ganglion;cochlea;endometrium;thyroid;amniotic fluid;bladder;brain;heart;cartilage;tongue;spinal cord;urinary;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;alveolus;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;dura mater;pineal gland;artery;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;aorta;stomach;cerebellum; whole brain;amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;spinal cord;prefrontal cortex;globus pallidus;pons;atrioventricular node;skeletal muscle; 0.95878 0.55740 -0.977252525 8.799245105 97.47421 2.13339 APPBP2 0.99907128300278 0.000928715209252783 1.78796667689751e-09 amyloid beta precursor protein binding protein 2 FUNCTION: May play a role in intracellular protein transport. May be involved in the translocation of APP along microtubules toward the cell surface. {ECO:0000269|PubMed:9843960}.; . . smooth muscle;ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;occipital lobe;medulla oblongata;adrenal cortex;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.77594 0.16862 -0.404032746 26.53338051 1169.86004 6.50148 APPL1 0.18416100961266 0.815834822969965 4.16741737493743e-06 adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 1 FUNCTION: Required for the regulation of cell proliferation in response to extracellular signals from an early endosomal compartment. Links Rab5 to nuclear signal transduction. {ECO:0000269|PubMed:10490823, ECO:0000269|PubMed:15016378}.; . TISSUE SPECIFICITY: High levels in heart, ovary, pancreas and skeletal muscle. {ECO:0000269|PubMed:10490823}.; myocardium;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);amygdala;meninges;lymph node;cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;pancreas;pia mater;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; . 0.34156 . 0.044168103 57.40740741 670.45747 5.17611 APPL2 3.52822991386898e-09 0.922102777783028 0.0778972186887426 adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 2 FUNCTION: Required for the regulation of cell proliferation in response to extracellular signals mediated by an early endosomal compartment. Links Rab5 to nuclear signal transduction. {ECO:0000269|PubMed:15016378}.; . TISSUE SPECIFICITY: High levels in brain, heart, kidney and skeletal muscle. {ECO:0000269|PubMed:11431708}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;oesophagus;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; . 0.14767 0.09559 -1.017713296 8.103326256 1171.95131 6.50644 APRT 4.71819943938473e-10 0.0155860272219192 0.984413972306261 adenine phosphoribosyltransferase FUNCTION: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.; DISEASE: Adenine phosphoribosyltransferase deficiency (APRTD) [MIM:614723]: An enzymatic deficiency that can lead to urolithiasis and renal failure. Patients have 2,8-dihydroxyadenine (DHA) urinary stones. {ECO:0000269|PubMed:11243733, ECO:0000269|PubMed:1353080, ECO:0000269|PubMed:15571218, ECO:0000269|PubMed:1746557, ECO:0000269|PubMed:21635362, ECO:0000269|PubMed:3343350, ECO:0000269|PubMed:3680503, ECO:0000269|PubMed:7915931}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.61214 0.09463 -0.095386216 46.48502005 51.16668 1.40998 APTR . . . Alu-mediated CDKN1A/p21 transcriptional regulator (non-protein coding) . . . . . . . . . . . APTX 7.72907188264723e-06 0.740449586579761 0.259542684348356 aprataxin FUNCTION: DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair and base excision repair. Resolves abortive DNA ligation intermediates formed either at base excision sites, or when DNA ligases attempt to repair non- ligatable breaks induced by reactive oxygen species. Catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined. Also able to hydrolyze adenosine 5'- monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity. {ECO:0000269|PubMed:14755728, ECO:0000269|PubMed:15044383, ECO:0000269|PubMed:16547001, ECO:0000269|PubMed:16964241, ECO:0000269|PubMed:17276982}.; DISEASE: Ataxia-oculomotor apraxia syndrome (AOA) [MIM:208920]: An autosomal recessive syndrome characterized by early-onset cerebellar ataxia, oculomotor apraxia, early areflexia and late peripheral neuropathy. {ECO:0000269|PubMed:11586299, ECO:0000269|PubMed:11586300, ECO:0000269|PubMed:12196655, ECO:0000269|PubMed:12629250, ECO:0000269|PubMed:14506070, ECO:0000269|PubMed:15699391, ECO:0000269|PubMed:15852392}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. In brain, it is expressed in the posterior cortex, cerebellum, hippocampus and olfactory bulb. Isoform 1 is highly expressed in the cerebral cortex and cerebellum, compared to isoform 2. {ECO:0000269|PubMed:11586299, ECO:0000269|PubMed:11586300, ECO:0000269|PubMed:14755728}.; umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;cerebellum cortex;pharynx;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07205 0.29287 0.463046108 78.58575136 86.51936 1.98569 AQP1 0.0499256381399427 0.859251575727823 0.0908227861322348 aquaporin 1 (Colton blood group) FUNCTION: Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. {ECO:0000269|PubMed:1373524}.; . TISSUE SPECIFICITY: Detected in erythrocytes (at protein level). Expressed in a number of tissues including erythrocytes, renal tubules, retinal pigment epithelium, heart, lung, skeletal muscle, kidney and pancreas. Weakly expressed in brain, placenta and liver. {ECO:0000269|PubMed:23219802}.; myocardium;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;endometrium;thyroid;iris;brain;gall bladder;heart;cartilage;pineal body;urinary;lens;skeletal muscle;liver;spleen;mammary gland;peripheral nerve;colon;parathyroid;uterus;cerebral cortex;larynx;synovium;bone;testis;pineal gland;spinal ganglion;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;aorta;stomach;thymus;cerebellum; spinal cord;kidney; 0.70453 0.40588 0.040529541 57.15380986 3332.8913 11.04933 AQP2 4.17696058293906e-06 0.218175500126541 0.781820322912876 aquaporin 2 FUNCTION: Forms a water-specific channel that provides the plasma membranes of renal collecting duct with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.; DISEASE: Diabetes insipidus, nephrogenic, autosomal (ANDI) [MIM:125800]: A disorder caused by the inability of the renal collecting ducts to absorb water in response to arginine vasopressin. Characterized by excessive water drinking (polydipsia), excessive urine excretion (polyuria), persistent hypotonic urine, and hypokalemia. Inheritance can be autosomal dominant or recessive. {ECO:0000269|PubMed:12050236, ECO:0000269|PubMed:12191971, ECO:0000269|PubMed:15509592, ECO:0000269|PubMed:16120822, ECO:0000269|PubMed:16361827, ECO:0000269|PubMed:16845277, ECO:0000269|PubMed:19585583, ECO:0000269|PubMed:24944815, ECO:0000269|PubMed:7524315, ECO:0000269|PubMed:8882880, ECO:0000269|PubMed:9048343, ECO:0000269|PubMed:9302264, ECO:0000269|PubMed:9402087, ECO:0000269|PubMed:9550615, ECO:0000269|PubMed:9649557, ECO:0000269|PubMed:9745427}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in renal collecting tubules.; unclassifiable (Anatomical System);colon;choroid;fovea centralis;lens;retina;prostate;optic nerve;lung;macula lutea;cervix;kidney;brain;stomach; dorsal root ganglion;ciliary ganglion;kidney; 0.22652 0.60646 -0.516085732 21.20193442 10.60227 0.38544 AQP3 0.504827505452393 0.491028537314853 0.00414395723275436 aquaporin 3 (Gill blood group) FUNCTION: Water channel required to promote glycerol permeability and water transport across cell membranes. Acts as a glycerol transporter in skin and plays an important role in regulating SC (stratum corneum) and epidermal glycerol content. Involved in skin hydration, wound healing, and tumorigenesis. Provides kidney medullary collecting duct with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. Slightly permeable to urea and may function as a water and urea exit mechanism in antidiuresis in collecting duct cells. It may play an important role in gastrointestinal tract water transport and in glycerol metabolism (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed in epithelial cells of kidney (collecting ducts) and airways, in keratinocytes, immature dendritic cells and erythrocytes. Isoform 2 is not detectable in erythrocytes at the protein level.; colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;testis;amniotic fluid;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;liver;hypopharynx;alveolus;spleen;head and neck;cervix;kidney;stomach;thymus; prostate;lung;trachea;tongue;salivary gland;beta cell islets;liver;kidney;tonsil;skin;skeletal muscle;thymus; 0.36135 0.33901 -0.295622497 32.61972163 10.88584 0.39443 AQP4 0.0181490424325557 0.895058884979584 0.0867920725878599 aquaporin 4 FUNCTION: Forms a water-specific channel. Osmoreceptor which regulates body water balance and mediates water flow within the central nervous system.; . TISSUE SPECIFICITY: Brain - muscle >> heart, kidney, lung, and trachea.; . . 0.27293 0.34547 -0.069700724 48.54328851 138.0763 2.55855 AQP4-AS1 . . . AQP4 antisense RNA 1 . . . . . . . . . . . AQP5 0.00438548410684657 0.668256126649884 0.32735838924327 aquaporin 5 FUNCTION: Forms a water-specific channel. Implicated in the generation of saliva, tears, and pulmonary secretions. Required for TRPV4 activation by hypotonicity (PubMed:16571723). Together with TRPV4, controls regulatory volume decrease in salivary epithelial cells (PubMed:16571723). {ECO:0000269|PubMed:16571723}.; DISEASE: Keratoderma, palmoplantar, Bothnian type (PPKB) [MIM:600231]: A dermatological disorder characterized by diffuse non-epidermolytic hyperkeratosis of the skin of palms and soles. PPKB is frequently complicated by fungal infections. {ECO:0000269|PubMed:23830519}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);medulla oblongata;heart;ovary;lacrimal gland;adrenal cortex;colon;parathyroid;lens;skin;retina;uterus;optic nerve;lung;endometrium;larynx;placenta;testis;kidney;brain;stomach; testis - interstitial;trachea;testis - seminiferous tubule;appendix;testis;trigeminal ganglion;skeletal muscle; 0.37930 0.24105 -0.337894035 30.37272942 49.83838 1.38455 AQP6 0.211427984634698 0.748233671046008 0.0403383443192945 aquaporin 6 FUNCTION: Forms a water-specific channel that participates in distinct physiological functions such as glomerular filtration, tubular endocytosis and acid-base metabolism. {ECO:0000250}.; . . . . 0.07348 0.13983 0.418953042 77.06416608 851.72723 5.70256 AQP7 1.86009112555737e-09 0.0347068328137193 0.96529316532619 aquaporin 7 FUNCTION: Forms a channel for water and glycerol.; . . unclassifiable (Anatomical System);myocardium;liver;colon;spleen;kidney;mammary gland;stomach; . 0.06240 0.13240 0.108486928 61.90728946 500.92929 4.59263 AQP7P1 . . . aquaporin 7 pseudogene 1 . . . unclassifiable (Anatomical System);breast;liver;spleen;mammary gland;skeletal muscle; . 0.02901 0.08100 . . . . AQP7P2 . . . aquaporin 7 pseudogene 2 . . . . . 0.02901 . . . . . AQP7P3 . . . aquaporin 7 pseudogene 3 . . . unclassifiable (Anatomical System);myocardium;liver;spleen;kidney;mammary gland;skeletal muscle; . . 0.07873 . . . . AQP7P4 . . . aquaporin 7 pseudogene 4 . . . unclassifiable (Anatomical System);myocardium;liver;spleen;kidney;mammary gland;skeletal muscle; . . 0.08108 . . . . AQP7P5 . . . aquaporin 7 pseudogene 5 . . . . . . . . . . . AQP8 0.00384821561717584 0.851820929826306 0.144330854556518 aquaporin 8 FUNCTION: Forms a water-specific channel; mercury-sensitive. Not permeable to glycerol or urea.; . TISSUE SPECIFICITY: Expressed only in pancreas and colon.; unclassifiable (Anatomical System);islets of Langerhans;colon;kidney;stomach; dorsal root ganglion;pancreas;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.06963 0.13569 0.262810045 70.43524416 141.60561 2.59633 AQP9 0.446614670928057 0.546959480431329 0.00642584864061399 aquaporin 9 FUNCTION: Forms a channel with a broad specificity. Mediates passage of a wide variety of non-charged solutes including carbamides, polyols, purines, and pyrimidines in a phloretin- and mercury-sensitive manner, whereas amino acids, cyclic sugars, Na(+), K(+), Cl(-), and deprotonated monocarboxylates are excluded. Also permeable to urea and glycerol. {ECO:0000269|PubMed:10564231}.; . TISSUE SPECIFICITY: Highly expressed in peripheral leukocytes. Also expressed in liver, lung, and spleen.; unclassifiable (Anatomical System);cartilage;heart;colon;blood;skin;bone marrow;uterus;lung;bone;alveolus;liver;kidney;brain;aorta;gall bladder; liver;whole blood;bone marrow; 0.79150 0.11664 -0.22584292 37.32012267 30.66006 0.97532 AQP10 0.0152782932027765 0.878522242818559 0.106199463978665 aquaporin 10 FUNCTION: Water channel required to promote glycerol permeability and water transport across cell membranes. May contribute to water transport in the upper portion of small intestine. Isoform 2 is not permeable to urea and glycerol. {ECO:0000269|PubMed:11573934, ECO:0000269|PubMed:12084581}.; . TISSUE SPECIFICITY: Expressed exclusively in duodenum and jejunum. Highest expression in absorptive epithelial cells at the tips of villi in the jejunum.; unclassifiable (Anatomical System);lung;liver;testis;spleen;skeletal muscle; . 0.10780 0.10375 0.104848986 61.49445624 4035.92542 12.59512 AQP11 0.0591720470749302 0.867908224335687 0.0729197285893824 aquaporin 11 FUNCTION: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;lung;whole body;frontal lobe;endometrium;islets of Langerhans;testis;parathyroid;kidney;stomach;retina; testis;trigeminal ganglion; 0.12960 0.11109 0.505321956 80.00707714 1452.674 7.11198 AQP12A 0.0462663637441815 0.675299151381386 0.278434484874433 aquaporin 12A FUNCTION: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. {ECO:0000250}.; . TISSUE SPECIFICITY: Restricted to the pancreas. {ECO:0000269|Ref.2}.; pancreas;islets of Langerhans; . 0.11518 0.08857 . . 1447.7357 7.09716 AQP12B 0.00435864786698477 0.431917162997045 0.563724189135971 aquaporin 12B FUNCTION: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. {ECO:0000250}.; . . . . 0.16011 . . . 3743.83383 11.95806 AQR 0.999998819889607 1.1801103932918e-06 5.34779214904111e-20 aquarius intron-binding spliceosomal factor FUNCTION: Intron-binding spliceosomal protein required to link pre-mRNA splicing and snoRNP (small nucleolar ribonucleoprotein) biogenesis. Plays a key role in position-dependent assembly of intron-encoded box C/D small snoRNP, splicing being required for snoRNP assembly. May act by helping the folding of the snoRNA sequence. Binds to intron of pre-mRNAs in a sequence-independent manner, contacting the region between snoRNA and the branchpoint of introns (40 nucleotides upstream of the branchpoint) during the late stages of splicing. {ECO:0000269|PubMed:16949364}.; . . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.13918 0.09949 -1.015898037 8.144609578 267.74625 3.51007 AR 0.99490980991855 0.00508962971755996 5.60363889421893e-07 androgen receptor FUNCTION: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins. Transcription activation is down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3. {ECO:0000269|PubMed:14664718, ECO:0000269|PubMed:15563469, ECO:0000269|PubMed:17591767, ECO:0000269|PubMed:17911242, ECO:0000269|PubMed:18084323, ECO:0000269|PubMed:19345326, ECO:0000269|PubMed:20980437}.; DISEASE: Androgen insensitivity syndrome (AIS) [MIM:300068]: An X- linked recessive form of pseudohermaphroditism due end-organ resistance to androgen. Affected males have female external genitalia, female breast development, blind vagina, absent uterus and female adnexa, and abdominal or inguinal testes, despite a normal 46,XY karyotype. {ECO:0000269|PubMed:10022458, ECO:0000269|PubMed:10221692, ECO:0000269|PubMed:10221770, ECO:0000269|PubMed:10404311, ECO:0000269|PubMed:10458483, ECO:0000269|PubMed:10571951, ECO:0000269|PubMed:10590024, ECO:0000269|PubMed:10690872, ECO:0000269|PubMed:11587068, ECO:0000269|PubMed:11744994, ECO:0000269|PubMed:1307250, ECO:0000269|PubMed:1316540, ECO:0000269|PubMed:1426313, ECO:0000269|PubMed:1430233, ECO:0000269|PubMed:1464650, ECO:0000269|PubMed:1480178, ECO:0000269|PubMed:1487249, ECO:0000269|PubMed:1569163, ECO:0000269|PubMed:1609793, ECO:0000269|PubMed:1775137, ECO:0000269|PubMed:1999491, ECO:0000269|PubMed:2082179, ECO:0000269|PubMed:2594783, ECO:0000269|PubMed:7537149, ECO:0000269|PubMed:7581399, ECO:0000269|PubMed:7633398, ECO:0000269|PubMed:7641413, ECO:0000269|PubMed:7671849, ECO:0000269|PubMed:7929841, ECO:0000269|PubMed:7962294, ECO:0000269|PubMed:7970939, ECO:0000269|PubMed:7981687, ECO:0000269|PubMed:7981689, ECO:0000269|PubMed:7993455, ECO:0000269|PubMed:8040309, ECO:0000269|PubMed:8096390, ECO:0000269|PubMed:8103398, ECO:0000269|PubMed:8162033, ECO:0000269|PubMed:8224266, ECO:0000269|PubMed:8281140, ECO:0000269|PubMed:8325950, ECO:0000269|PubMed:8413310, ECO:0000269|PubMed:8446106, ECO:0000269|PubMed:8626869, ECO:0000269|PubMed:8647313, ECO:0000269|PubMed:8683794, ECO:0000269|PubMed:8723113, ECO:0000269|PubMed:8768864, ECO:0000269|PubMed:8809734, ECO:0000269|PubMed:8830623, ECO:0000269|PubMed:8918984, ECO:0000269|PubMed:8990010, ECO:0000269|PubMed:9001799, ECO:0000269|PubMed:9007482, ECO:0000269|PubMed:9039340, ECO:0000269|PubMed:9106550, ECO:0000269|PubMed:9160185, ECO:0000269|PubMed:9252933, ECO:0000269|PubMed:9255042, ECO:0000269|PubMed:9302173, ECO:0000269|PubMed:9328206, ECO:0000269|PubMed:9544375, ECO:0000269|PubMed:9554754, ECO:0000269|PubMed:9610419, ECO:0000269|PubMed:9627582, ECO:0000269|PubMed:9698822, ECO:0000269|PubMed:9788719, ECO:0000269|PubMed:9851768, ECO:0000269|PubMed:9856504, ECO:0000269|Ref.109, ECO:0000269|Ref.175}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spinal and bulbar muscular atrophy X-linked 1 (SMAX1) [MIM:313200]: An X-linked recessive form of spinal muscular atrophy. Spinal muscular atrophy refers to a group of neuromuscular disorders characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. SMAX1 occurs only in men. Age at onset is usually in the third to fifth decade of life, but earlier involvement has been reported. It is characterized by slowly progressive limb and bulbar muscle weakness with fasciculations, muscle atrophy, and gynecomastia. The disorder is clinically similar to classic forms of autosomal spinal muscular atrophy. {ECO:0000269|PubMed:15851746}. Note=The disease is caused by mutations affecting the gene represented in this entry. Caused by trinucleotide CAG repeat expansion. In SMAX1 patients the number of Gln ranges from 38 to 62. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.; DISEASE: Note=Defects in AR may play a role in metastatic prostate cancer. The mutated receptor stimulates prostate growth and metastases development despite of androgen ablation. This treatment can reduce primary and metastatic lesions probably by inducing apoptosis of tumor cells when they express the wild-type receptor.; DISEASE: Androgen insensitivity, partial (PAIS) [MIM:312300]: A disorder that is characterized by hypospadias, hypogonadism, gynecomastia, genital ambiguity, normal XY karyotype, and a pedigree pattern consistent with X-linked recessive inheritance. Some patients present azoospermia or severe oligospermia without other clinical manifestations. {ECO:0000269|PubMed:10022458, ECO:0000269|PubMed:10221692, ECO:0000269|PubMed:10470409, ECO:0000269|PubMed:10502786, ECO:0000269|PubMed:10543676, ECO:0000269|PubMed:11587068, ECO:0000269|PubMed:1303262, ECO:0000269|PubMed:1307250, ECO:0000269|PubMed:1316540, ECO:0000269|PubMed:1424203, ECO:0000269|PubMed:1430233, ECO:0000269|PubMed:2010552, ECO:0000269|PubMed:7581399, ECO:0000269|PubMed:7649358, ECO:0000269|PubMed:7671849, ECO:0000269|PubMed:7909256, ECO:0000269|PubMed:7910529, ECO:0000269|PubMed:7929841, ECO:0000269|PubMed:7970939, ECO:0000269|PubMed:7981687, ECO:0000269|PubMed:8033918, ECO:0000269|PubMed:8097257, ECO:0000269|PubMed:8126121, ECO:0000269|PubMed:8205256, ECO:0000269|PubMed:8281139, ECO:0000269|PubMed:8325932, ECO:0000269|PubMed:8325950, ECO:0000269|PubMed:8446106, ECO:0000269|PubMed:8550758, ECO:0000269|PubMed:8809734, ECO:0000269|PubMed:8823308, ECO:0000269|PubMed:8824883, ECO:0000269|PubMed:9039340, ECO:0000269|PubMed:9196614, ECO:0000269|PubMed:9302173, ECO:0000269|PubMed:9329414, ECO:0000269|PubMed:9543136, ECO:0000269|PubMed:9607727, ECO:0000269|PubMed:9768671, ECO:0000269|PubMed:9856504, ECO:0000269|Ref.117}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 2 is mainly expressed in heart and skeletal muscle. {ECO:0000269|PubMed:15634333}.; . . 0.98848 0.97465 -0.622676946 17.30950696 1670.25439 7.54387 ARAF 0.618988518165058 0.380674899023438 0.000336582811504316 A-Raf proto-oncogene, serine/threonine kinase FUNCTION: Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signaling cascade. {ECO:0000269|PubMed:22609986}.; . TISSUE SPECIFICITY: Predominantly in urogenital tissues.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;greater omentum;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;developmental;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;muscle;pancreas;lung;placenta;duodenum;hypopharynx;head and neck;kidney;stomach; liver;skeletal muscle; 0.96395 0.35300 -0.492218069 22.35786742 38.37658 1.13846 ARAFP1 . . . ARAF pseudogene 1 . . . . . . . . . . . ARAFP2 . . . ARAF pseudogene 2 . . . . . . . . . . . ARAFP3 . . . ARAF pseudogene 3 . . . . . . . . . . . ARAP1 1.50377669733894e-05 0.999984379090857 5.83142169592711e-07 ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 1 FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Has a preference for ARF1 and ARF5 (By similarity). {ECO:0000250, ECO:0000269|PubMed:11804590}.; . TISSUE SPECIFICITY: Detected in heart, skeletal muscle, spleen, kidney, liver, placenta, lung, peripheral blood leukocytes, adrenal gland, bone marrow, brain, lymph node, mammary gland, prostate, spinal cord, stomach, thyroid and trachea. {ECO:0000269|PubMed:11804590}.; lymphoreticular;myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;pineal gland;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;small intestine;islets of Langerhans;adrenal cortex;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;stomach;thymus; prostate;testis - interstitial;testis - seminiferous tubule;adrenal gland;liver;testis; 0.24613 0.17391 -1.446087194 3.933710781 2533.75935 9.39142 ARAP1-AS1 . . . ARAP1 antisense RNA 1 . . . . . . . . . . . ARAP1-AS2 . . . ARAP1 antisense RNA 2 . . . . . . . . . . . ARAP2 7.56157160220884e-13 0.999983232831812 1.67671674315779e-05 ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 2 FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in brain, thymus, lymph node, thyroid, spinal cord, trachea, heart, skeletal muscle, spleen, kidney, liver, placenta, lung and peripheral blood leukocytes. {ECO:0000269|PubMed:11804590}.; ovary;parathyroid;skin;uterus;prostate;thyroid;testis;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;medulla oblongata;prefrontal cortex;pons;atrioventricular node;caudate nucleus;cingulate cortex;parietal lobe; 0.14993 . -0.180160811 40.17456947 579.69503 4.88004 ARAP3 0.967505028947346 0.032494971046517 6.1370460471866e-12 ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 3 FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Acts on ARF6, RAC1, RHOA and CDC42. Plays a role in the internalization of anthrax toxin. {ECO:0000269|PubMed:11804589, ECO:0000269|PubMed:15569923}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;thymus; amygdala;dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.15138 0.12582 -0.712964275 14.40787922 1264.79016 6.70356 ARC 0.920765733774356 0.0787397268629155 0.000494539362728168 activity-regulated cytoskeleton-associated protein FUNCTION: Required for consolidation of synaptic plasticity as well as formation of long-term memory. Regulates endocytosis of AMPA receptors in response to synaptic activity. Required for homeostatic synaptic scaling of AMPA receptors (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the stress fiber dynamics and cell migration. {ECO:0000250, ECO:0000269|PubMed:21834987}.; . . unclassifiable (Anatomical System);prostate;lung;bone;placenta;adrenal medulla;liver;blood;brain;retina; whole brain;superior cervical ganglion;adrenal cortex;globus pallidus;trigeminal ganglion;skeletal muscle;bone marrow; 0.11599 0.13982 -0.361761279 28.6329323 19.29175 0.66455 ARCN1 0.999850871289472 0.000149128607974156 1.02553441764106e-10 archain 1 FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;cornea;mesenchyma;adrenal gland;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta; pituitary; 0.31441 0.17611 -0.626318434 17.03231894 55.4936 1.49655 AREG 0.652354960633584 0.322490880579438 0.025154158786979 amphiregulin FUNCTION: Ligand of the EGF receptor/EGFR. Autocrine growth factor as well as a mitogen for a broad range of target cells including astrocytes, Schwann cells and fibroblasts.; . . unclassifiable (Anatomical System);lymph node;colon;skin;skeletal muscle;bone marrow;breast;bile duct;uterus;prostate;lung;placenta;liver;cervix;kidney;aorta;stomach; . 0.20226 0.10275 . . 98.56697 2.14538 AREL1 0.0118020841149469 0.988183852687461 1.40631975920897e-05 apoptosis resistant E3 ubiquitin protein ligase 1 FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Inhibits apoptosis by ubiquitinating and targeting for degradation a number of proapoptotic proteins including DIABLO/SMAC, HTRA2 and SEPT4/ARTS which are released from the mitochondrion into the cytosol following apoptotic stimulation. {ECO:0000269|PubMed:23479728}.; . . . . 0.24429 0.12378 -0.775187015 13.05142722 143.57869 2.61251 ARF1 0.819433490606023 0.176396237473814 0.00417027192016248 ADP ribosylation factor 1 FUNCTION: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP- ribosyltransferase. Involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles. The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasicity of excitatory synapses and spine shrinkage during long-term depression (LTD).; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;duodenum;kidney;stomach;thymus;cerebellum; whole brain;prostate;heart;placenta;liver;prefrontal cortex;testis; 0.38135 0.22085 -0.141298762 42.87567823 1.21425 0.03971 ARF1P1 . . . ADP ribosylation factor 1 pseudogene 1 . . . . . . . . . . . ARF1P2 . . . ADP ribosylation factor 1 pseudogene 2 . . . . . . . . . . . ARF1P3 . . . ADP ribosylation factor 1 pseudogene 3 . . . . . . . . . . . ARF3 0.622731323606937 0.369680329819893 0.00758834657317062 ADP ribosylation factor 3 FUNCTION: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP- ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.; . . ovary;skin;retina;bone marrow;prostate;subthalamic nucleus;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; amygdala;whole brain;superior cervical ganglion;occipital lobe;medulla oblongata;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.87350 . -0.031067188 51.03798066 . . ARF4 0.931562500213935 0.0680960716878694 0.000341428098195888 ADP ribosylation factor 4 FUNCTION: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP- ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.; . . smooth muscle;ovary;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;testis;amniotic fluid;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;greater omentum;pancreas;lung;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;adrenal gland;placenta; 0.32094 0.36254 0.057118534 57.99716914 . . ARF4-AS1 . . . ARF4 antisense RNA 1 . . . . . . . . . . . ARF4P1 . . . ADP ribosylation factor 4 pseudogene 1 . . . . . . . . . . . ARF4P2 . . . ADP ribosylation factor 4 pseudogene 2 . . . . . . . . . . . ARF4P3 . . . ADP ribosylation factor 4 pseudogene 3 . . . . . . . . . . . ARF4P4 . . . ADP ribosylation factor 4 pseudogene 4 . . . . . . . . . . . ARF4P5 . . . ADP ribosylation factor 4 pseudogene 5 . . . . . . . . . . . ARF5 0.234001126600504 0.7328488490273 0.0331500243721965 ADP ribosylation factor 5 FUNCTION: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP- ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.; . . medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;cerebellum; . 0.18785 0.13588 0.013025609 54.62962963 3.32434 0.12160 ARF6 0.600609559476142 0.361887013263993 0.0375034272598645 ADP ribosylation factor 6 FUNCTION: GTP-binding protein involved in protein trafficking that regulates endocytic recycling and cytoskeleton remodeling. Required for normal completion of mitotic cytokinesis. Plays a role in the reorganization of the actin cytoskeleton and the formation of stress fibers. May also modulate vesicle budding and uncoating within the Golgi apparatus. Involved in the regulation of dendritic spine development, contributing to the regulation of dendritic branching and filopodia extension. Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. {ECO:0000269|PubMed:11266366, ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:16099990, ECO:0000269|PubMed:16737952, ECO:0000269|PubMed:18400762, ECO:0000269|PubMed:21170023, ECO:0000269|PubMed:7589240}.; . TISSUE SPECIFICITY: Ubiquitous, with higher levels in heart, substantia nigra, and kidney. {ECO:0000269|PubMed:14659046}.; umbilical cord;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;trachea;kidney;atrioventricular node;trigeminal ganglion;whole blood;thymus; 0.43767 0.41336 -0.141298762 42.87567823 . . ARFGAP1 0.0166821066209427 0.982300008409468 0.00101788496958914 ADP ribosylation factor GTPase activating protein 1 FUNCTION: GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine (By similarity). {ECO:0000250}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;pancreas;lung;pia mater;mesenchyma;placenta;duodenum;head and neck;kidney;stomach;thymus;cerebellum; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion; 0.30602 0.10729 -0.110153916 45.48832272 85.57401 1.97273 ARFGAP2 0.562990971385505 0.436986931049597 2.20975648983131e-05 ADP ribosylation factor GTPase activating protein 2 FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes. {ECO:0000269|PubMed:17760859}.; . . lymphoreticular;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;peripheral nerve;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus; superior cervical ganglion;cerebellum peduncles;prefrontal cortex;pons; 0.45415 0.12888 0.531004228 80.87992451 3477.91758 11.35381 ARFGAP3 2.27855257372515e-06 0.975676682180242 0.0243210392671846 ADP ribosylation factor GTPase activating protein 3 FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes. {ECO:0000269|PubMed:11172815}.; . TISSUE SPECIFICITY: Widely expressed. Highest expression in endocrine glands (pancreas, pituitary gland, salivary gland, and prostate) and testis with a much higher expression in the testis than in the ovary. {ECO:0000269|PubMed:10704287}.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach;thymus; prostate;testis;trigeminal ganglion; 0.12759 0.10665 1.067416815 91.66666667 581.99135 4.88961 ARFGEF1 0.999999909436541 9.05634594252828e-08 1.02872339015834e-22 ADP ribosylation factor guanine nucleotide exchange factor 1 FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competetive RhoA binding. The function in the nucleus remains to be determined. {ECO:0000269|PubMed:12571360, ECO:0000269|PubMed:15644318, ECO:0000269|PubMed:17227842, ECO:0000269|PubMed:20360857, ECO:0000269|PubMed:22084092}.; . TISSUE SPECIFICITY: Expressed in placenta, lung, heart, brain, kidney and pancreas.; lymphoreticular;ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;spleen;head and neck;kidney;aorta;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;occipital lobe;pons;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;appendix;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.89864 0.28270 -1.745389579 2.37084218 294.25109 3.66374 ARFGEF2 0.999999938266667 6.17333330704198e-08 4.04478658616306e-23 ADP ribosylation factor guanine nucleotide exchange factor 2 FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extend on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles; the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. {ECO:0000269|PubMed:12051703, ECO:0000269|PubMed:12571360, ECO:0000269|PubMed:15385626, ECO:0000269|PubMed:16477018, ECO:0000269|PubMed:17276987, ECO:0000269|PubMed:18625701, ECO:0000269|PubMed:20360857}.; DISEASE: Periventricular nodular heterotopia 2 (PVNH2) [MIM:608097]: A developmental disorder characterized by the presence of periventricular nodules of cerebral gray matter, resulting from a failure of neurons to migrate normally from the lateral ventricular proliferative zone, where they are formed, to the cerebral cortex. PVNH2 is an autosomal recessive form characterized by microcephaly (small brain), severe developmental delay and recurrent infections. No anomalies extrinsic to the central nervous system, such as dysmorphic features or grossly abnormal endocrine or other conditions, are associated with PVNH2. {ECO:0000269|PubMed:14647276}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in placenta, lung, heart, brain, kidney and pancreas.; . . 0.60497 0.15011 -2.385043169 1.102854447 151.96563 2.69556 ARFGEF3 . . . ARFGEF family member 3 FUNCTION: Participates in the regulation of systemic glucose homeostasis, where it negatively regulates insulin granule biogenesis in pancreatic islet beta cells (By similarity). Also regulates glucagon granule production in pancreatic alpha cells (By similarity). Inhibits nuclear translocation of the transcriptional coregulator PHB2 and may enhance estrogen receptor alpha (ESR1) transcriptional activity in breast cancer cells (PubMed:19496786). {ECO:0000250|UniProtKB:Q3UGY8, ECO:0000269|PubMed:19496786}.; . TISSUE SPECIFICITY: Expressed in breast cancer cell lines. Not expressed in normal tissues such as duct, mammary gland, lung, heart, liver, kidnay, bone marrow. {ECO:0000269|PubMed:19496786}.; . . . 0.12485 -2.2199121 1.338759141 . . ARFIP1 0.00372902323812407 0.955819977463737 0.0404509992981389 ADP ribosylation factor interacting protein 1 FUNCTION: Putative target protein of ADP-ribosylation factor.; . TISSUE SPECIFICITY: Ubiquitously expressed. Higher levels in liver, pancreas, placenta, skeletal muscle and heart.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;atrium;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;tonsil;gall bladder;unclassifiable (Anatomical System);heart;small intestine;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.37212 0.11323 0.106667882 61.73036093 134.78172 2.52387 ARFIP2 0.942932710427979 0.0570232243887886 4.40651832323034e-05 ADP ribosylation factor interacting protein 2 FUNCTION: Putative target protein of ADP-ribosylation factor. Involved in membrane ruffling.; . . lymphoreticular;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;lens;breast;pancreas;lung;epididymis;nasopharynx;placenta;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; whole brain;subthalamic nucleus;occipital lobe;liver;testis;kidney;cingulate cortex;parietal lobe;cerebellum; 0.14975 0.14609 -0.427900189 25.14744043 14.33009 0.51775 ARFRP1 0.135717560060112 0.84362031898797 0.0206621209519178 ADP ribosylation factor related protein 1 FUNCTION: Trans-Golgi-associated GTPase that regulates protein sorting. Controls the targeting of ARL1 and its effector to the trans-Golgi. Required for the lipidation of chylomicrons in the intestine and required for VLDL lipidation in the liver. {ECO:0000250|UniProtKB:Q8BXL7}.; . TISSUE SPECIFICITY: Found in most tissues.; myocardium;medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;spleen;cervix;kidney;mammary gland;aorta;stomach;cerebellum;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;caudate nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex;cerebellum; 0.12050 0.23508 -0.139478553 43.29440906 29.85832 0.95259 ARG1 0.000499882512051677 0.879729161106299 0.119770956381649 arginase 1 . DISEASE: Argininemia (ARGIN) [MIM:207800]: A rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia and progressive spastic quadriplegia. {ECO:0000269|PubMed:1463019, ECO:0000269|PubMed:22959135, ECO:0000269|PubMed:23859858, ECO:0000269|PubMed:7649538}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;lung;heart;visual apparatus;liver;testis;spleen;blood;skin;bone marrow; dorsal root ganglion;fetal liver;superior cervical ganglion;liver;fetal lung;atrioventricular node;trigeminal ganglion;bone marrow; 0.65628 0.43126 -0.249709319 35.74545883 25.18835 0.82346 ARG2 0.542999038189075 0.456369106416088 0.00063185539483739 arginase 2 FUNCTION: May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to NO synthase. Since NO synthase is found in the penile corpus cavernosum smooth muscle, the clitoral corpus cavernosum and the vagina, arginase II plays a role in both male and female sexual arousal. It is therefore a potential target for the treatment of male and female sexual arousal disorders. {ECO:0000269|PubMed:12859189}.; . TISSUE SPECIFICITY: Expressed most strongly in kidney and prostate, much less strongly in the brain, skeletal muscle, placenta, lung, mammary gland, macrophage, uterus, testis and gut, but apparently not in the liver, heart and pancreas.; lymphoreticular;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; dorsal root ganglion;prostate;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.11918 0.48725 -0.047654689 50.22410946 97.57094 2.13557 ARGFX 1.03484051516333e-05 0.346100909276152 0.653888742318697 arginine-fifty homeobox FUNCTION: Putative transcription factor. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at low level in testis and undifferentiated embryonic stem cells. {ECO:0000269|PubMed:17005330}.; unclassifiable (Anatomical System); ciliary ganglion;atrioventricular node; 0.02245 0.05215 0.327131069 73.27199811 235.08793 3.31330 ARGFXP1 . . . arginine-fifty homeobox pseudogene 1 . . . . . . . . . . . ARGFXP2 . . . arginine-fifty homeobox pseudogene 2 . . . . . . . . . . . ARGLU1 0.992267193125092 0.00773249163040894 3.15244499490482e-07 arginine and glutamate rich 1 FUNCTION: Required for the estrogen-dependent expression of ESR1 target genes. Can act in cooperation with MED1. {ECO:0000269|PubMed:21454576}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;epididymis;visual apparatus;macula lutea;liver;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;placenta;amnion;head and neck;kidney;stomach;thymus; fetal brain; 0.77668 0.06833 -0.09720619 46.20193442 2 0.06510 ARHGAP1 0.185564722294501 0.812004260072597 0.00243101763290249 Rho GTPase activating protein 1 FUNCTION: GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;ovary;salivary gland;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;hypopharynx;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;occipital lobe;placenta;ciliary ganglion;caudate nucleus;trigeminal ganglion;parietal lobe;skeletal muscle; 0.38242 0.30784 -0.137658575 43.57159707 82.23058 1.92404 ARHGAP4 0.983661940481215 0.0163376600352129 3.99483572050395e-07 Rho GTPase activating protein 4 FUNCTION: Inhibitory effect on stress fiber organization. May down-regulate Rho-like GTPase in hematopoietic cells.; . TISSUE SPECIFICITY: Predominantly in hematopoietic cells (spleen, thymus and leukocytes); low levels in placenta, lung and various fetal tissues.; lymphoreticular;ovary;colon;choroid;skin;retina;bone marrow;uterus;endometrium;bone;iris;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;blood;pancreas;lung;placenta;duodenum;hypopharynx;liver;spleen;head and neck;mammary gland;stomach;thymus; . 0.12713 0.23338 0.159856957 64.91507431 333.94271 3.88180 ARHGAP5 0.98705369807694 0.0129462926886714 9.23438893897642e-09 Rho GTPase activating protein 5 FUNCTION: GTPase-activating protein for Rho family members. May play a role in the reduction of the p21rasGTPase-activating potential of RASA1/p120GAP.; . TISSUE SPECIFICITY: Expressed in kidney, brain, liver and lung.; unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;skin;skeletal muscle;breast;uterus;prostate;whole body;lung;frontal lobe;larynx;nasopharynx;thyroid;placenta;visual apparatus;liver;testis;head and neck;spleen;kidney;brain;stomach; amygdala;occipital lobe;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex; 0.23723 0.16401 -0.545632343 20.02241095 177.4302 2.89547 ARHGAP5-AS1 . . . ARHGAP5 antisense RNA 1 (head to head) . . . . . 0.13314 . . . . . ARHGAP6 0.991844364940163 0.00815527594965916 3.59110177346405e-07 Rho GTPase activating protein 6 FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing the cell morphology. {ECO:0000269|PubMed:10699171}.; . TISSUE SPECIFICITY: Highly expressed in kidney, heart and skeletal muscle followed by retina, lymphoblast, placenta, lung, brain, pancreas and liver.; unclassifiable (Anatomical System);heart;colon;blood;skeletal muscle;skin;uterus;prostate;lung;endometrium;trabecular meshwork;liver;spleen;kidney; superior cervical ganglion;prostate;thyroid;trigeminal ganglion;skeletal muscle; 0.20190 0.13979 -0.556537043 19.72753008 85.98487 1.97973 ARHGAP8 . . . Rho GTPase activating protein 8 FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in kidney and placenta. Also expressed in colon, skeletal muscle, small intestine, stomach, and testis. Not detected in brain, liver or spleen. Overexpressed in the majority of colorectal tumors examined. {ECO:0000269|PubMed:15225876}.; unclassifiable (Anatomical System);ovary;colon;parathyroid;blood;skin;breast;prostate;lung;endometrium;larynx;placenta;liver;head and neck;kidney;mammary gland;stomach; . . 0.13931 2.302206513 98.32507667 . . ARHGAP9 2.89131295292005e-09 0.901799549682901 0.0982004474257858 Rho GTPase activating protein 9 FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has a substantial GAP activity toward CDC42 and RAC1 and less toward RHOA. Has a role in regulating adhesion of hematopoietic cells to the extracellular matrix. Binds phosphoinositides, and has the highest affinity for phosphatidylinositol 3,4,5-trisphosphate, followed by phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate. {ECO:0000269|PubMed:11396949}.; . TISSUE SPECIFICITY: Predominantly expressed in peripheral blood leukocytes, spleen, and thymus. {ECO:0000269|PubMed:11396949}.; fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;tongue;muscle;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;macula lutea;alveolus;liver;spleen;head and neck;cervix;stomach;aorta;cerebellum; . 0.14121 0.21298 -0.326979057 30.90351498 2099.04192 8.43856 ARHGAP10 1.21711064000628e-10 0.980910404512816 0.0190895953654725 Rho GTPase activating protein 10 FUNCTION: GTPase activator for the small GTPases RhoA and Cdc42 by converting them to an inactive GDP-bound state. Essential for PTKB2 regulation of cytoskeletal organization via Rho family GTPases. Inhibits PAK2 proteolytic fragment PAK-2p34 kinase activity and changes its localization from the nucleus to the perinuclear region. Stabilizes PAK-2p34 thereby increasing stimulation of cell death (By similarity). {ECO:0000250, ECO:0000269|PubMed:11432776}.; . TISSUE SPECIFICITY: High levels of expression in heart and skeletal muscle. {ECO:0000269|PubMed:11432776}.; sympathetic chain;colon;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;cerebral cortex;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;pharynx;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;kidney; superior cervical ganglion;medulla oblongata;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15341 0.12272 1.09310945 91.90846898 222.91944 3.22888 ARHGAP11A 0.124921593849902 0.875035757446313 4.26487037848195e-05 Rho GTPase activating protein 11A . . . ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;bone marrow;uterus;whole body;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;pharynx;blood;skeletal muscle;lung;cornea;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;appendix;atrioventricular node; 0.23766 0.08058 -0.214928658 37.7388535 219.03859 3.19956 ARHGAP11B 0.0721323428905467 0.872315297326153 0.0555523597833005 Rho GTPase activating protein 11B FUNCTION: Hominin-specific protein that promotes development and evolutionary expansion of the brain neocortex. Able to promote amplification of basal progenitors in the subventricular zone, producing more neurons during fetal corticogenesis (PubMed:25721503). Does not posses GTPase activator activity (PubMed:25721503). {ECO:0000269|PubMed:25721503}.; . . . . 0.11527 . 0.170987912 65.5579146 41.04962 1.20271 ARHGAP12 0.00231777174845934 0.997652082001484 3.0146250056777e-05 Rho GTPase activating protein 12 FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.; . . umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; 0.59182 0.13510 -0.819281839 11.93677754 2139.4248 8.50730 ARHGAP15 5.25405675416054e-06 0.96475652230248 0.0352382236407659 Rho GTPase activating protein 15 FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has activity toward RAC1. Overexpression results in an increase in actin stress fibers and cell contraction. {ECO:0000269|PubMed:12650940}.; . TISSUE SPECIFICITY: Expressed in lung, liver and lymphoid cells. {ECO:0000269|PubMed:12650940}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;cerebral cortex;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;blood;lens;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;aorta;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;olfactory bulb;testis - seminiferous tubule;testis;white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle;thymus; 0.77364 0.12676 -0.624497208 17.16206653 736.83485 5.38892 ARHGAP16P . . . Rho GTPase activating protein 16 pseudogene . . . . . . . . . . . ARHGAP17 0.990465510536605 0.00953448510164262 4.36175267808343e-09 Rho GTPase activating protein 17 FUNCTION: Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex formed with AMOT acts by regulating the uptake of polarity proteins at tight junctions, possibly by deciding whether tight junction transmembrane proteins are recycled back to the plasma membrane or sent elsewhere. Participates in the Ca(2+)-dependent regulation of exocytosis, possibly by catalyzing GTPase activity of Rho family proteins and by inducing the reorganization of the cortical actin filaments. Acts as a GTPase activator in vitro for RAC1. {ECO:0000269|PubMed:11431473, ECO:0000269|PubMed:16678097}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at higher level in heart and placenta. {ECO:0000269|PubMed:11431473}.; smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;head and neck;spleen;kidney;aorta;stomach; dorsal root ganglion;superior cervical ganglion;placenta;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21814 . -1.5928285 3.066761029 181.49315 2.92804 ARHGAP18 2.45958437535249e-06 0.995368002982463 0.00462953743316131 Rho GTPase activating protein 18 FUNCTION: Rho GTPase activating protein that suppresses F-actin polymerization by inhibiting Rho. Rho GTPase activating proteins act by converting Rho-type GTPases to an inactive GDP-bound state (PubMed:21865595). Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation. Acts downstream of YAP1 and inhibits actin polymerization, which in turn reduces nuclear localization of YAP1 (PubMed:25778702). Regulates cell shape, spreading, and migration (PubMed:21865595). {ECO:0000269|PubMed:21865595, ECO:0000269|PubMed:25778702}.; . . lymphoreticular;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;blood;skeletal muscle;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;stomach;thymus; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.09701 0.11308 -0.797234383 12.48525596 144.42294 2.61697 ARHGAP19 1.63035988922819e-07 0.84642902985396 0.153570807110051 Rho GTPase activating protein 19 FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.; . TISSUE SPECIFICITY: Strong expression in fetal heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Weak expression in adult pancreas, spleen, thymus, and ovary. {ECO:0000269|PubMed:17454002}.; salivary gland;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;blood;skeletal muscle;lung;placenta;visual apparatus;alveolus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;olfactory bulb;testis - seminiferous tubule;testis;white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion;thymus; 0.57466 . 0.352813824 74.49280491 . . ARHGAP19-SLIT1 2.95389171915188e-07 0.919880250511505 0.0801194540993229 ARHGAP19-SLIT1 readthrough (NMD candidate) . . . . . . . . . 514.02292 4.64020 ARHGAP20 0.00902004672136777 0.990959123541366 2.0829737266006e-05 Rho GTPase activating protein 20 FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.; DISEASE: Note=A chromosomal aberration involving ARHGAP20 may be a cause of B-cell chronic lymphocytic leukemia (B-CLL) (PubMed:15543602). Translocation t(X;11)(q21;q23) with BRWD3 does not result in fusion transcripts but disrupts both genes (PubMed:15543602). {ECO:0000269|PubMed:15543602}.; TISSUE SPECIFICITY: Expressed predominantly in the brain. Lower expression is found in lymph nodes. {ECO:0000269|PubMed:15543602}.; unclassifiable (Anatomical System);heart;cartilage;skeletal muscle;skin;uterus;pancreas;whole body;lung;frontal lobe;placenta;testis;mammary gland;brain; superior cervical ganglion;trachea;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.26615 0.13312 -0.393118976 27.05237084 190.16897 2.99346 ARHGAP21 0.999946673207153 5.3326792847183e-05 4.76248231155282e-18 Rho GTPase activating protein 21 FUNCTION: Functions as a GTPase-activating protein (GAP) for RHOA and CDC42. Downstream partner of ARF1 which may control Golgi apparatus structure and function. Also required for CTNNA1 recruitment to adherens junctions. {ECO:0000269|PubMed:15793564, ECO:0000269|PubMed:16184169}.; . TISSUE SPECIFICITY: Widely expressed with higher expression in brain, heart, skeletal muscle and placenta. {ECO:0000269|PubMed:12056806}.; . . 0.34248 0.15472 -0.779115343 12.78013682 423.78679 4.29850 ARHGAP22 0.000724652276522939 0.980744857922464 0.0185304898010128 Rho GTPase activating protein 22 FUNCTION: Rho GTPase-activating protein involved in the signal transduction pathway that regulates endothelial cell capillary tube formation during angiogenesis. Acts as a GTPase activator for the RAC1 by converting it to an inactive GDP-bound state. Inhibits RAC1-dependent lamellipodia formation. May also play a role in transcription regulation via its interaction with VEZF1, by regulating activity of the endothelin-1 (EDN1) promoter (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);myocardium;ovary;cartilage;hypothalamus;salivary gland;parathyroid;bone marrow;lung;endometrium;placenta;bone;visual apparatus;kidney;brain;aorta; subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12203 0.13515 -0.396754488 26.97570182 185.07105 2.95338 ARHGAP22-IT1 . . . ARHGAP22 intronic transcript 1 . . . . . . . . . . . ARHGAP23 . . . Rho GTPase activating protein 23 FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in placenta, prostate, hippocampus and brain medulla. Also expressed in brain tumor, salivary gland tumor, head and neck tumor. {ECO:0000269|PubMed:15254754}.; . . 0.32675 0.09642 . . 576.78624 4.86912 ARHGAP23P1 . . . Rho GTPase activating protein 23 pseudogene 1 . . . . . . . . . . . ARHGAP24 0.00469608080576638 0.995038484689666 0.000265434504567334 Rho GTPase activating protein 24 FUNCTION: Rho GTPase-activating protein involved in cell polarity, cell morphology and cytoskeletal organization. Acts as a GTPase activator for the Rac-type GTPase by converting it to an inactive GDP-bound state. Controls actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity. Able to suppress RAC1 and CDC42 activity in vitro. Overexpression induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. Isoform 2 is a vascular cell-specific GAP involved in modulation of angiogenesis. {ECO:0000269|PubMed:15302923, ECO:0000269|PubMed:15611138, ECO:0000269|PubMed:16862148}.; . TISSUE SPECIFICITY: Isoform 1 is widely expressed with a higher level in kidney. Isoform 2 is mainly expressed in endothelial cells. {ECO:0000269|PubMed:15302923, ECO:0000269|PubMed:15611138, ECO:0000269|PubMed:16862148}.; myocardium;medulla oblongata;smooth muscle;ovary;parathyroid;fovea centralis;skin;uterus;whole body;cochlea;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;kidney;pons;atrioventricular node;trigeminal ganglion; 0.39284 0.12435 -0.617221851 17.44515216 242.67907 3.36262 ARHGAP25 0.438207321068152 0.561734300627413 5.83783044357252e-05 Rho GTPase activating protein 25 FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;frontal lobe;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;lymph node;white blood cells;atrioventricular node;trigeminal ganglion;whole blood;tonsil; 0.82588 0.12015 0.75875178 86.82472281 1845.81859 7.92463 ARHGAP26 0.998859800147404 0.00114019982817286 2.44227102159874e-11 Rho GTPase activating protein 26 FUNCTION: GTPase-activating protein for RHOA and CDC42.; DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal translocation t(5;11)(q31;q23) with KMT2A/MLL1 has been found in leukemic cells from JMML patients, also carrying inactivating mutations on the second allele (PubMed:10908648). {ECO:0000269|PubMed:10908648}.; . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;thyroid;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;heart;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;stomach;cerebellum; superior cervical ganglion;heart;placenta;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.36857 0.36135 -0.867014353 10.72776598 31.37458 0.98924 ARHGAP26-AS1 . . . ARHGAP26 antisense RNA 1 . . . . . . . . . . . ARHGAP26-IT1 . . . ARHGAP26 intronic transcript 1 . . . . . . . . . . . ARHGAP27 0.00125584382196987 0.996972196360709 0.0017719598173209 Rho GTPase activating protein 27 FUNCTION: Rho GTPase-activating protein which may be involved in clathrin-mediated endocytosis. GTPase activators for the Rho-type GTPases act by converting them to an inactive GDP-bound state. Has activity toward CDC42 and RAC1 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in germinal center B-cell, spleen, chronic lymphocytic leukemia, pancreatic cancer and lung cancer. {ECO:0000269|PubMed:15492870}.; unclassifiable (Anatomical System);prostate;lymph node;bone;colon;kidney;germinal center;mammary gland;stomach; . 0.17546 0.09516 . . 971.7069 6.02549 ARHGAP28 0.0029584189440561 0.996524364839434 0.000517216216509965 Rho GTPase activating protein 28 FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis. Expressed at moderate level in kidney and ovary, and weakly expressed in spleen and skeletal muscle. {ECO:0000269|PubMed:10718198}.; unclassifiable (Anatomical System);medulla oblongata;ovary;parathyroid;lens;skeletal muscle;retina;prostate;lung;placenta;bone;liver;testis;spleen;brain; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;pons;trigeminal ganglion;skeletal muscle; 0.11041 0.11329 -0.352661697 29.48808681 512.59116 4.63503 ARHGAP29 0.999986514079404 1.34859205936962e-05 2.43732146503826e-15 Rho GTPase activating protein 29 FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. May act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. {ECO:0000269|PubMed:15752761, ECO:0000269|PubMed:9305890}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in skeletal muscle and heart. Expressed at intermediate level in placenta, liver and pancreas. Weakly expressed in brain, lung and kidney. {ECO:0000269|PubMed:9305890}.; sympathetic chain;colon;skin;retina;uterus;prostate;whole body;cerebral cortex;endometrium;bone;testis;amniotic fluid;brain;gall bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;skeletal muscle;breast;pancreas;lung;placenta;hippocampus;liver;spleen;kidney;aorta;cerebellum; superior cervical ganglion;appendix;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.08761 0.08872 -1.480759435 3.686010852 122.89049 2.41370 ARHGAP30 0.968957887758364 0.0310420324264323 7.98152041874685e-08 Rho GTPase activating protein 30 FUNCTION: GTPase-activating protein (GAP) for RAC1 and RHOA, but not for CDC42. {ECO:0000269|PubMed:21565175}.; . . . . 0.05654 . -0.968173992 8.982071243 2706.09644 9.78724 ARHGAP31 0.999634465686628 0.000365534305824752 7.54728886599796e-12 Rho GTPase activating protein 31 FUNCTION: Functions as a GTPase-activating protein (GAP) for RAC1 and CDC42. Required for cell spreading, polarized lamellipodia formation and cell migration. {ECO:0000269|PubMed:12192056, ECO:0000269|PubMed:16519628}.; DISEASE: Adams-Oliver syndrome 1 (AOS1) [MIM:100300]: A disorder characterized by the congenital absence of skin (aplasia cutis congenita) in combination with transverse limb defects. Aplasia cutis congenita can be located anywhere on the body, but in the vast majority of the cases, it is present on the posterior parietal region where it is often associated with an underlying defect of the parietal bones. Limb abnormalities are typically limb truncation defects affecting the distal phalanges or entire digits (true ectrodactyly). Only rarely, metatarsals/metacarpals or more proximal limb structures are also affected. Apart from transverse limb defects, syndactyly, most commonly of second and third toes, can also be observed. The clinical features are highly variable and can also include cardiovascular malformations, brain abnormalities and vascular defects such as cutis marmorata and dilated scalp veins. {ECO:0000269|PubMed:21565291}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;sympathetic chain;developmental;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;testis;amniotic fluid;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;hypothalamus;pharynx;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . 0.587847333 82.35432885 223.53392 3.23262 ARHGAP31-AS1 . . . ARHGAP31 antisense RNA 1 . . . . . . . . . . . ARHGAP32 0.987088519508478 0.0129114804884106 3.11167564364185e-12 Rho GTPase activating protein 32 FUNCTION: GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:12446789, ECO:0000269|PubMed:12454018, ECO:0000269|PubMed:12531901, ECO:0000269|PubMed:12788081, ECO:0000269|PubMed:12819203, ECO:0000269|PubMed:12857875, ECO:0000269|PubMed:17663722}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed in brain and testis. Isoform 1 is also expressed in other tissues such as lung, liver and spleen. {ECO:0000269|PubMed:12446789}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; amygdala;superior cervical ganglion;subthalamic nucleus;occipital lobe;medulla oblongata;temporal lobe;globus pallidus;pons;parietal lobe;cingulate cortex; . . -2.151949495 1.450813871 693.40551 5.25060 ARHGAP33 0.212248410336133 0.787750958143849 6.31520017772911e-07 Rho GTPase activating protein 33 FUNCTION: May be involved in several stages of intracellular trafficking. Could play an important role in the regulation of glucose transport by insulin. May act as a downstream effector of RHOQ/TC10 in the regulation of insulin-stimulated glucose transport (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;ovary;lacrimal gland;blood;skeletal muscle;bone marrow;uterus;whole body;lung;testis;spleen;kidney;brain;thymus; amygdala;dorsal root ganglion;occipital lobe;superior cervical ganglion;spinal cord;caudate nucleus;atrioventricular node;pons;skin;skeletal muscle;testis - seminiferous tubule;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.40232 0.13342 -1.456898556 3.862939372 201.41522 3.06572 ARHGAP35 0.999989834870149 1.01651297031019e-05 1.47773228280921e-13 Rho GTPase activating protein 35 FUNCTION: Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'- GAGAAAAGAAACTGGAGAAACTC-3'. May participate in the regulation of retinal development and degeneration. May transduce signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP). May also act as a tumor suppressor. {ECO:0000269|PubMed:1894621}.; . . medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;larynx;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;breast;lung;cornea;mesenchyma;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;stomach; testis - interstitial;medulla oblongata;superior cervical ganglion;testis - seminiferous tubule;testis;pons;parietal lobe;skeletal muscle; 0.63484 0.16728 -1.813357534 2.170323189 80.89225 1.90231 ARHGAP36 0.989879513869536 0.0101174769497864 3.00918067729878e-06 Rho GTPase activating protein 36 FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.; . . unclassifiable (Anatomical System);whole body;heart;thyroid;placenta;pituitary gland;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;pituitary; . . -0.758599262 13.32861524 16.41062 0.58176 ARHGAP39 0.00168179647156594 0.997152661445608 0.00116554208282559 Rho GTPase activating protein 39 . . . unclassifiable (Anatomical System);fovea centralis;choroid;lens;retina;uterus;prostate;optic nerve;lung;endometrium;macula lutea;visual apparatus;liver;testis;spleen;cervix;brain;stomach; . . . -1.390744555 4.305260675 202.55456 3.07112 ARHGAP40 . . . Rho GTPase activating protein 40 FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.; . . unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.08879 0.10941 . . 884.50678 5.79264 ARHGAP42 . . . Rho GTPase activating protein 42 FUNCTION: May influence blood pressure by functioning as a GTPase- activating protein for RHOA in vascular smooth muscle. {ECO:0000269|PubMed:24335996}.; . . unclassifiable (Anatomical System);hypothalamus;sympathetic chain;colon; superior cervical ganglion;globus pallidus;ciliary ganglion;skeletal muscle; . . . . 2146.95556 8.52466 ARHGAP42P1 . . . Rho GTPase activating protein 42 pseudogene 1 . . . . . . . . . . . ARHGAP42P2 . . . Rho GTPase activating protein 42 pseudogene 2 . . . . . . . . . . . ARHGAP42P3 . . . Rho GTPase activating protein 42 pseudogene 3 . . . . . . . . . . . ARHGAP42P4 . . . Rho GTPase activating protein 42 pseudogene 4 . . . . . . . . . . . ARHGAP42P5 . . . Rho GTPase activating protein 42 pseudogene 5 . . . . . . . . . . . ARHGAP44 0.999299004436186 0.0007009953815376 1.82276101827456e-10 Rho GTPase activating protein 44 FUNCTION: GTPase-activating protein (GAP) that stimulates the GTPase activity of Rho-type GTPases. Thereby, controls Rho-type GTPases cycling between their active GTP-bound and inactive GDP- bound states. May act as a GAP for CDC42 and RAC1. Endosomal recycling protein which, in association with SHANK3, is involved in synaptic plasticity. Promotes GRIA1 exocytosis from recycling endosomes and spine morphological changes associated to long-term potentiation. {ECO:0000269|PubMed:11431473}.; . TISSUE SPECIFICITY: Highly expressed in brain. Expressed at weak level in other tissues. {ECO:0000269|PubMed:11431473}.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;kidney;stomach; whole brain;amygdala;occipital lobe;subthalamic nucleus;thalamus;medulla oblongata;temporal lobe;prefrontal cortex;globus pallidus;cingulate cortex;cerebellum; . . -1.48620052 3.632932295 96.51325 2.12216 ARHGDIA 0.727995864276251 0.269203650724266 0.00280048499948289 Rho GDP dissociation inhibitor (GDI) alpha FUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1. {ECO:0000269|PubMed:20400958, ECO:0000269|PubMed:23434736}.; DISEASE: Nephrotic syndrome 8 (NPHS8) [MIM:615244]: A form of nephrotic syndrome, a renal disease clinically characterized by progressive renal failure, severe proteinuria, hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show diffuse mesangial sclerosis, with small glomeruli, hypercellularity, increased extracellular matrix, and contracted/collapsed glomerular tufts surrounded by immature or abnormal podocytes. {ECO:0000269|PubMed:23434736}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;sympathetic chain;intestine;colon;choroid;skin;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;epididymis;placenta;visual apparatus;alveolus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach;thymus; amygdala;superior cervical ganglion;caudate nucleus;trigeminal ganglion; 0.10851 . -0.251530012 35.42108988 53.81777 1.46221 ARHGDIB 0.000280473501044255 0.555960934125232 0.443758592373724 Rho GDP dissociation inhibitor (GDI) beta FUNCTION: Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.; . . myocardium;lymphoreticular;smooth muscle;ovary;umbilical cord;skin;bone marrow;prostate;endometrium;thyroid;germinal center;brain;bladder;gall bladder;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;larynx;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; lymph node;tumor;white blood cells;whole blood;tonsil;bone marrow;thymus; 0.18465 0.15699 -0.05129383 49.75819769 17.3747 0.61003 ARHGDIG 0.486229755044962 0.492047122915518 0.0217231220395203 Rho GDP dissociation inhibitor (GDI) gamma FUNCTION: Inhibits GDP/GTP exchange reaction of RhoB. Interacts specifically with the GDP- and GTP-bound forms of post- translationally processed Rhob and Rhog proteins, both of which show a growth-regulated expression in mammalian cells. Stimulates the release of the GDP-bound but not the GTP-bound RhoB protein. Also inhibits the GDP/GTP exchange of RhoB but shows less ability to inhibit the dissociation of prebound GTP.; . TISSUE SPECIFICITY: Primarily expressed in pancreas and brain.; unclassifiable (Anatomical System);uterus;pancreas;optic nerve;frontal lobe;islets of Langerhans;colon;spleen;choroid;brain; amygdala;whole brain;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;cerebellum peduncles;temporal lobe;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.14720 0.12238 -0.159704656 41.90846898 22.62314 0.75687 ARHGEF1 0.909497463749542 0.0905025264373826 9.81307560042448e-09 Rho guanine nucleotide exchange factor 1 FUNCTION: Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase. Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12. Mediates angiotensin-2- induced RhoA activation. {ECO:0000269|PubMed:20098430, ECO:0000269|PubMed:8810315, ECO:0000269|PubMed:9641915, ECO:0000269|PubMed:9641916}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:8810315, ECO:0000269|PubMed:9135076}.; ovary;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;larynx;bone;thyroid;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;muscle;urinary;blood;breast;bile duct;pancreas;lung;epididymis;placenta;visual apparatus;liver;cervix;head and neck;spleen;kidney;mammary gland;stomach; trigeminal ganglion;skeletal muscle; 0.10869 0.15030 -1.837219906 2.070063694 124.73358 2.42844 ARHGEF2 0.99999323549835 6.76450164958184e-06 4.53967943611207e-16 Rho/Rac guanine nucleotide exchange factor 2 FUNCTION: Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases, which was uniquely reported in PubMed:9857026. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIP2 dependent NF-kappaB signaling pathways activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides through NOD1 that is independent of its GEF activity, but also in the activation of NF-kappaB by Shigella effector proteins (IpgB2 and OspB) which requires its GEF activity and the activation of RhoA. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF- alpha secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. {ECO:0000269|PubMed:19043560, ECO:0000269|PubMed:21887730, ECO:0000269|PubMed:9857026}.; . . myocardium;lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;urinary;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach;aorta; superior cervical ganglion;occipital lobe;medulla oblongata;thalamus;caudate nucleus;pons;atrioventricular node;subthalamic nucleus;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;parietal lobe;cerebellum; 0.22628 0.11124 -0.93133804 9.613116301 94.75814 2.09761 ARHGEF3 0.991271357501421 0.00872855668707193 8.58115069685777e-08 Rho guanine nucleotide exchange factor 3 FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RhoA and RhoB GTPases. {ECO:0000269|PubMed:12221096}.; . TISSUE SPECIFICITY: Widely expressed. Highest levels are found in adult brain and skeletal muscle. Lower levels are found in heart and kidney. {ECO:0000269|PubMed:10873612, ECO:0000269|PubMed:12221096}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;bone;thyroid;testis;brain;pineal gland;tonsil;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;spinal cord;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum; subthalamic nucleus;globus pallidus;cingulate cortex; 0.32682 0.12378 -0.290161348 33.33923095 2959.45549 10.30538 ARHGEF3-AS1 . . . ARHGEF3 antisense RNA 1 . . . . . . . . . . . ARHGEF4 0.0685948768686647 0.930825680470557 0.000579442660778403 Rho guanine nucleotide exchange factor 4 FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RHOA, RAC1 and CDC42 GTPases. Binding of APC may activate RAC1 GEF activity. The APC-ARHGEF4 complex seems to be involved in cell migration as well as in E-cadherin-mediated cell-cell adhesion. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Involved in tumor angiogenesis and may play a role in intestinal adenoma formation and tumor progression. {ECO:0000269|PubMed:10947987, ECO:0000269|PubMed:12598901, ECO:0000269|PubMed:17145773, ECO:0000269|PubMed:17599059, ECO:0000269|PubMed:19893577}.; . TISSUE SPECIFICITY: Expressed at high levels in the brain, skeletal muscle and testis and at low levels in the kidney, lung, small intestine, ovary and prostate. Expression is aberrantly enhanced in most colorectal tumors. {ECO:0000269|PubMed:10873612, ECO:0000269|PubMed:17145773, ECO:0000269|PubMed:19893577}.; unclassifiable (Anatomical System);heart;ovary;hypothalamus;colon;skin;uterus;pancreas;prostate;optic nerve;lung;frontal lobe;iris;testis;bladder;brain;stomach; whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;temporal lobe;spinal cord;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.31304 . -0.551080959 19.93394669 1764.34786 7.75981 ARHGEF5 . . . Rho guanine nucleotide exchange factor 5 FUNCTION: Guanine nucleotide exchange factor which activates Rho GTPases (PubMed:15601624). Strongly activates RHOA (PubMed:15601624). Also strongly activates RHOB, weakly activates RHOC and RHOG and shows no effect on RHOD, RHOV, RHOQ or RAC1 (By similarity). Involved in regulation of cell shape and actin cytoskeletal organization (PubMed:15601624). Plays a role in actin organization by generating a loss of actin stress fibers and the formation of membrane ruffles and filopodia (PubMed:14662653). Required for SRC-induced podosome formation (By similarity). Involved in positive regulation of immature dendritic cell migration (By similarity). {ECO:0000250|UniProtKB:E9Q7D5, ECO:0000269|PubMed:14662653, ECO:0000269|PubMed:15601624}.; . TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in placenta. High levels are also found in colon, kidney, trachea, prostate, liver, pancreas, pituitary gland, thyroid gland and mammary gland. In fetal tissues, expressed at high levels in kidney, lung and liver (PubMed:15601624). Expressed at low levels in lung and heart (PubMed:14662653). {ECO:0000269|PubMed:14662653, ECO:0000269|PubMed:15601624}.; smooth muscle;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;thyroid;bone;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;placenta;thyroid;kidney;trigeminal ganglion; 0.07867 0.09335 . . 86.93739 1.99130 ARHGEF6 0.998212122551167 0.00178787566287874 1.78595419441707e-09 Rac/Cdc42 guanine nucleotide exchange factor 6 FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF).; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;uterus;prostate;atrium;frontal lobe;cochlea;thyroid;testis;germinal center;spinal ganglion;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;adrenal cortex;blood;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;mammary gland;stomach;thymus; . 0.33163 0.26601 0.64123826 83.97617363 96.69035 2.12469 ARHGEF7 0.953985930517112 0.0460138565842199 2.12898667965723e-07 Rho guanine nucleotide exchange factor 7 FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions (By similarity). May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons. {ECO:0000250, ECO:0000269|PubMed:18184567, ECO:0000269|PubMed:18716323, ECO:0000269|PubMed:19041750}.; . . medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;cerebellum;thymus; superior cervical ganglion;prefrontal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.22379 0.62409 -1.03976177 7.802547771 94.43621 2.09150 ARHGEF7-AS1 . . . ARHGEF7 antisense RNA 1 . . . . . . . . . . . ARHGEF7-AS2 . . . ARHGEF7 antisense RNA 2 . . . . . . . . . . . ARHGEF7-IT1 . . . ARHGEF7 intronic transcript 1 . . . . . . . . . . . ARHGEF9 0.983065394323285 0.0169239644278082 1.06412489067244e-05 Cdc42 guanine nucleotide exchange factor 9 FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for CDC42. Promotes formation of GPHN clusters. {ECO:0000269|PubMed:10559246}.; . TISSUE SPECIFICITY: Detected in brain. Detected at low levels in heart. {ECO:0000269|PubMed:10559246}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;gum;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;aorta;cerebellum; amygdala;whole brain;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;atrioventricular node;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.24185 0.11483 -0.117432389 44.89266336 11.70426 0.42469 ARHGEF9-IT1 . . . ARHGEF9 intronic transcript 1 . . . . . . . . . . . ARHGEF10 1.10804741351534e-13 0.993645093874128 0.00635490612576131 Rho guanine nucleotide exchange factor 10 FUNCTION: May play a role in developmental myelination of peripheral nerves. {ECO:0000269|PubMed:14508709}.; DISEASE: Slowed nerve conduction velocity (SNCV) [MIM:608236]: Affected individuals present a reduction in nerve conduction velocities without any clinical signs of peripheral or central nervous system dysfunction. SNCV inheritance is autosomal dominant. {ECO:0000269|PubMed:14508709}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;cerebral cortex;larynx;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;thymus; dorsal root ganglion;testis - interstitial;olfactory bulb;spinal cord;testis;atrioventricular node;trigeminal ganglion; 0.21968 . -1.016286421 8.109223874 709.76209 5.29246 ARHGEF10L 0.0383062935578488 0.96169321522449 4.91217661058066e-07 Rho guanine nucleotide exchange factor 10 like FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RHOA, RHOB and RHOC. {ECO:0000269|PubMed:16112081}.; . TISSUE SPECIFICITY: Detected in heart, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:16112081}.; smooth muscle;colon;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;brain;unclassifiable (Anatomical System);islets of Langerhans;lens;skeletal muscle;breast;lung;trabecular meshwork;placenta;macula lutea;liver;alveolus;kidney;stomach; cerebellum; 0.15756 0.10710 -0.755258792 13.4524652 746.76247 5.42207 ARHGEF11 0.999945339206174 5.46607938256793e-05 5.05791811783985e-18 Rho guanine nucleotide exchange factor 11 FUNCTION: May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in neurotrophin-induced neurite outgrowth. {ECO:0000269|PubMed:21670212}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10026210}.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pineal body;blood;lens;pancreas;lung;placenta;macula lutea;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; . 0.31017 0.15072 -1.714337031 2.500589762 1596.56628 7.39387 ARHGEF12 0.99999892582633 1.07417367028587e-06 8.6053136673698e-21 Rho guanine nucleotide exchange factor 12 FUNCTION: May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. {ECO:0000269|PubMed:11094164}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 2 is found in jejunum and testis.; myocardium;ovary;skin;retina;prostate;optic nerve;ganglion;frontal lobe;cochlea;endometrium;gum;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;placenta;head and neck;kidney;stomach;aorta; superior cervical ganglion;skeletal muscle; 0.47120 . -0.323344668 30.9447983 743.24174 5.41202 ARHGEF15 0.00447718051318209 0.995238415279764 0.00028440420705374 Rho guanine nucleotide exchange factor 15 FUNCTION: Specific GEF for RhoA activation. Does not activate RAC1 or CDC42. Regulates vascular smooth muscle contractility. Negatively regulates excitatory synapse development by suppressing the synapse-promoting activity of EPHB2. {ECO:0000269|PubMed:12775584}.; . TISSUE SPECIFICITY: Expressed in the vascular smooth muscle of coronary artery. {ECO:0000269|PubMed:12775584}.; myocardium;fovea centralis;choroid;retina;prostate;optic nerve;whole body;larynx;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.25422 0.10102 0.538284722 81.08634112 534.99928 4.71583 ARHGEF16 9.36505312388017e-08 0.510068048308037 0.489931858041432 Rho guanine nucleotide exchange factor 16 FUNCTION: Guanyl-nucleotide exchange factor of the RHOG GTPase stimulating the exchange of RHOG-associated GDP for GTP. May play a role in chemotactic cell migration by mediating the activation of RAC1 by EPHA2. May also activate CDC42 and mediate activation of CDC42 by the viral protein HPV16 E6. {ECO:0000269|PubMed:20679435}.; . . . . 0.16223 0.14120 0.246221394 69.56829441 336.90376 3.89866 ARHGEF17 0.995257098833384 0.00474290116656141 5.42658599777922e-14 Rho guanine nucleotide exchange factor 17 FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. {ECO:0000269|PubMed:12071859}.; . . myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;iris;testis;brain;unclassifiable (Anatomical System);cartilage;heart;nervous;islets of Langerhans;pineal body;pharynx;blood;lens;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;liver;amnion;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; amygdala;superior cervical ganglion;thalamus;cerebellum peduncles;hypothalamus;placenta;prefrontal cortex;caudate nucleus; 0.30241 0.10400 -0.748045379 13.74734607 3511.2966 11.43648 ARHGEF18 0.90836751633667 0.0916322361942471 2.47469082709312e-07 Rho/Rac guanine nucleotide exchange factor 18 FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. Its activation induces formation of actin stress fibers. Also act as a GEF for RAC1, inducing production of reactive oxygen species (ROS). Does not act as a GEF for CDC42. The G protein beta-gamma (Gbetagamma) subunits of heterotrimeric G proteins act as activators, explaining the integrated effects of LPA and other G-protein coupled receptor agonists on actin stress fiber formation, cell shape change and ROS production. Required for EPB41L4B-mediated regulation of the circumferential actomyosin belt in epithelial cells (PubMed:22006950). {ECO:0000269|PubMed:11085924, ECO:0000269|PubMed:14512443, ECO:0000269|PubMed:15558029, ECO:0000269|PubMed:22006950}.; . TISSUE SPECIFICITY: Expressed in all tissues tested with highest expression in kidney and pancreas. Weakly or not expressed in liver, skeletal muscle and testis. {ECO:0000269|PubMed:11085924, ECO:0000269|PubMed:14512443, ECO:0000269|PubMed:15558029}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;stomach;aorta;thymus; whole brain;lung;white blood cells;thymus; 0.10895 0.10442 0.655813101 84.18848785 444.31169 4.38418 ARHGEF19 7.63919108459289e-09 0.885084394057774 0.114915598303035 Rho guanine nucleotide exchange factor 19 FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase. {ECO:0000250}.; . . ovary;colon;skin;retina;uterus;prostate;endometrium;thyroid;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;lacrimal gland;bile duct;lung;adrenal gland;placenta;liver;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve;thymus; dorsal root ganglion;ciliary ganglion;atrioventricular node;skin; 0.09806 . 1.001272896 90.72304789 3323.95871 11.02396 ARHGEF19-AS1 . . . ARHGEF19 antisense RNA 1 . . . . . . . . . . . ARHGEF25 5.17606707704438e-06 0.992194775303211 0.00780004862971155 Rho guanine nucleotide exchange factor 25 FUNCTION: May play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. It works as a guanine nucleotide exchange factor for Rho family of small GTPases. Links specifically G alpha q/11- coupled receptors to RHOA activation. May be an important regulator of processes involved in axon and dendrite formation. In neurons seems to be an exchange factor primarily for RAC1. Involved in skeletal myogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:11861769, ECO:0000269|PubMed:12547822, ECO:0000269|PubMed:15069594, ECO:0000269|PubMed:15632174, ECO:0000269|PubMed:16314529, ECO:0000269|PubMed:17606614}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed in excitable tissues, such as brain, heart and muscle. Also detected in kidney and liver. {ECO:0000269|PubMed:11861769, ECO:0000269|PubMed:12547822, ECO:0000269|PubMed:15069594}.; colon;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;pituitary gland;testis;brain;spinal ganglion;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;lens;lung;placenta;macula lutea;stomach;cerebellum; . . . -0.021969881 52.14673272 191.33923 2.99965 ARHGEF26 5.99162897861342e-06 0.993649364191842 0.00634464417917966 Rho guanine nucleotide exchange factor 26 FUNCTION: Activates RhoG GTPase by promoting the exchange of GDP by GTP. Required for the formation of membrane ruffles during macropinocytosis. Required for the formation of cup-like structures during trans-endothelial migration of leukocytes. In case of Salmonella enterica infection, activated by SopB, which induces cytoskeleton rearrangements and promotes bacterial entry. {ECO:0000269|PubMed:15133129, ECO:0000269|PubMed:17074883, ECO:0000269|PubMed:17875742}.; . TISSUE SPECIFICITY: Isoform 1 is broadly expressed, with highest levels in liver (at protein level). Certain mRNA species appear to be specifically expressed in prostate and liver. {ECO:0000269|PubMed:12697679, ECO:0000269|PubMed:15133129}.; unclassifiable (Anatomical System);ovary;hypothalamus;parathyroid;fovea centralis;choroid;lens;retina;prostate;optic nerve;whole body;lung;adrenal gland;placenta;macula lutea;liver;testis;brain;artery;mammary gland;aorta;stomach; superior cervical ganglion;globus pallidus;atrioventricular node;skeletal muscle; . . 0.580556395 82.31304553 2005.54992 8.24753 ARHGEF26-AS1 . . . ARHGEF26 antisense RNA 1 . . . . . . . . . . . ARHGEF28 1.82695073178584e-10 0.999907511533398 9.24882839074167e-05 Rho guanine nucleotide exchange factor 28 FUNCTION: Functions as a RHOA-specific guanine nucleotide exchange factor regulating signaling pathways downstream of integrins and growth factor receptors. Functions in axonal branching, synapse formation and dendritic morphogenesis. Functions also in focal adhesion formation, cell motility and B-lymphocytes activation. May regulate NEFL expression and aggregation and play a role in apoptosis (By similarity). {ECO:0000250}.; . . . . . . -0.270169915 34.32413305 6772.25337 17.47256 ARHGEF33 . . . Rho guanine nucleotide exchange factor 33 FUNCTION: May act as a guanine-nucleotide releasing factor. {ECO:0000250}.; . . . . . . 1.060147109 91.46614768 99.11115 2.15413 ARHGEF34P . . . Rho guanine nucleotide exchange factor 34, pseudogene . . . . . . . . . . . ARHGEF35 0.12761661654485 0.780177866381832 0.0922055170733173 Rho guanine nucleotide exchange factor 35 . . . . . . . . . 43.02776 1.24510 ARHGEF37 1.08240046485854e-13 0.0211567222284534 0.978843277771438 Rho guanine nucleotide exchange factor 37 FUNCTION: May act as a guanine nucleotide exchange factor (GEF). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;endometrium;cerebral cortex;bone;pituitary gland;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;spinal cord;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;kidney;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; . . 1.183126933 92.82849729 8667.38708 20.12571 ARHGEF38 0.00563171745432905 0.720124338850708 0.274243943694963 Rho guanine nucleotide exchange factor 38 FUNCTION: May act as a guanine-nucleotide releasing factor. {ECO:0000250}.; . . unclassifiable (Anatomical System);colon;stomach; dorsal root ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . . . . 2057.23092 8.35870 ARHGEF38-IT1 . . . ARHGEF38 intronic transcript 1 . . . . . . . . . . . ARHGEF39 2.22010112867739e-08 0.258791434506644 0.741208543292345 Rho guanine nucleotide exchange factor 39 FUNCTION: Promotes cell proliferation. {ECO:0000269|PubMed:22327280}.; . TISSUE SPECIFICITY: Strongly expressed in hepatocellular carcinoma (HCC) compared with their non-cancerous counterparts. {ECO:0000269|PubMed:22327280}.; . . 0.09800 0.08791 0.861712133 88.6883699 2541.91734 9.42047 ARHGEF40 7.1856790203222e-05 0.999928130722455 1.24873420209165e-08 Rho guanine nucleotide exchange factor 40 FUNCTION: May act as a guanine nucleotide exchange factor (GEF). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at higher level in the central nervous system and skeletal muscle and greater abundance in fetal than adult brain (at protein level). {ECO:0000269|PubMed:16143467}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;brain;gall bladder;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;muscle;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland; superior cervical ganglion;trigeminal ganglion; . . -0.226073511 37.1255013 1688.98262 7.57807 ARID1A 0.999999996642687 3.35731302964182e-09 9.91437781621639e-23 AT-rich interaction domain 1A FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Binds DNA non-specifically. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon, and PBL, and at a much lower level in heart, brain, placenta, lung, liver, skeletal muscle, kidney, and pancreas. {ECO:0000269|PubMed:11073988, ECO:0000269|PubMed:11318604, ECO:0000269|PubMed:12200431}.; myocardium;ovary;colon;parathyroid;skin;bone marrow;prostate;frontal lobe;endometrium;larynx;thyroid;pituitary gland;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;tongue;muscle;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hypopharynx;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; amygdala;superior cervical ganglion;subthalamic nucleus;prefrontal cortex;globus pallidus;pons;trigeminal ganglion;cerebellum; 0.54895 0.15082 -2.670076378 0.743099788 409.71816 4.24329 ARID1B 0.999949930200412 5.00697995874118e-05 4.93048584287307e-16 AT-rich interaction domain 1B FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Binds DNA non-specifically. {ECO:0000250}.; DISEASE: Mental retardation, autosomal dominant 12 (MRD12) [MIM:614562]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD12 patients present with moderate to severe psychomotor retardation, and most show evidence of muscular hypotonia. In many patients, expressive speech is more severely affected than receptive function. Additional common findings include short stature, abnormal head shape and low-set, posteriorly rotated, and abnormally shaped ears, downslanting palpebral fissures, a bulbous nasal tip, a thin upper lip, minor teeth anomalies, and brachydactyly or single palmar creases. Autistic features are uncommon. {ECO:0000269|PubMed:22405089, ECO:0000269|PubMed:22426308, ECO:0000269|PubMed:22426309}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed with high levels in heart, skeletal muscle and kidney. {ECO:0000269|PubMed:11988099, ECO:0000269|PubMed:12200431, ECO:0000269|PubMed:12665591}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;hippocampus;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus;cerebellum; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;cerebellum; 0.15152 0.12645 -2.622392448 0.802075961 623.55868 5.03581 ARID2 0.999999053128101 9.46871899211288e-07 3.77536281541501e-18 AT-rich interaction domain 2 FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). May be involved in targeting the complex to different genes. May be involved in regulating transcriptional activation of cardiac genes. {ECO:0000269|PubMed:16782067}.; . TISSUE SPECIFICITY: Highly expressed in heart and testis. {ECO:0000269|PubMed:16782067}.; unclassifiable (Anatomical System);lymph node;ovary;heart;muscle;colon;parathyroid;retina;bone marrow;breast;uterus;prostate;lung;endometrium;nasopharynx;thyroid;placenta;visual apparatus;liver;testis;head and neck;germinal center;kidney;brain;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.52953 0.10241 -1.762038945 2.329558858 319.93598 3.79954 ARID3A 0.425084301076406 0.573350100752573 0.00156559817102125 AT-rich interaction domain 3A FUNCTION: Transcription factor which may be involved in the control of cell cycle progression by the RB1/E2F1 pathway and in B-cell differentiation. {ECO:0000269|PubMed:11812999, ECO:0000269|PubMed:12692263}.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in skeletal muscle, thalamus, and colon.; unclassifiable (Anatomical System);heart;colon;blood;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;placenta;bone;macula lutea;visual apparatus;iris;liver;spleen;germinal center;kidney;brain; placenta;atrioventricular node; 0.33312 0.11128 -0.422438699 25.64284029 110.18988 2.28254 ARID3B 0.964041164914236 0.0359449637994907 1.38712862734394e-05 AT-rich interaction domain 3B FUNCTION: Transcription factor which may be involved in neuroblastoma growth and malignant transformation. Favors nuclear targeting of ARID3A. {ECO:0000269|PubMed:16951138, ECO:0000269|PubMed:17400556}.; . TISSUE SPECIFICITY: Expressed in placenta, testis and leukocytes. Expressed in neuroblastoma. Present in K-562 erythrocytic leukemia cell line (at protein level). {ECO:0000269|PubMed:10446990, ECO:0000269|PubMed:16951138}.; ovary;colon;fovea centralis;skin;bone marrow;retina;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;cartilage;tongue;blood;pancreas;lung;placenta;visual apparatus;macula lutea;spleen;head and neck;kidney;stomach; superior cervical ganglion;placenta;globus pallidus;testis;ciliary ganglion;skeletal muscle; 0.26646 0.10644 -0.224023033 37.4321774 162.58733 2.78403 ARID3C 6.787321200931e-07 0.269883999078818 0.730115322189061 AT-rich interaction domain 3C . . . . . 0.32423 0.08104 0.52918614 80.81505072 546.80485 4.75348 ARID4A 0.999999263100059 7.36899940927966e-07 1.01308902551897e-17 AT-rich interaction domain 4A FUNCTION: Interacts with the viral protein-binding domain of the retinoblastoma protein.; . . unclassifiable (Anatomical System);lymph node;heart;hypothalamus;developmental;colon;blood;skin;skeletal muscle;retina;breast;uterus;lung;cochlea;nasopharynx;trabecular meshwork;thyroid;placenta;visual apparatus;pituitary gland;liver;testis;kidney;aorta;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex; 0.62595 0.21087 -1.194104514 5.850436424 256.34754 3.44479 ARID4B 0.999976459226573 2.3540773417338e-05 9.46768578585301e-15 AT-rich interaction domain 4B FUNCTION: Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the Sin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes. {ECO:0000269|PubMed:12724404}.; . TISSUE SPECIFICITY: Highly expressed in the testis and in breast, lung, colon, pancreatic and ovarian cancers. Expressed at low levels in the thymus, prostate and ovary. {ECO:0000269|PubMed:11481388, ECO:0000269|PubMed:12724404, ECO:0000269|PubMed:15247124}.; lymphoreticular;myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; amygdala;testis - interstitial;superior cervical ganglion;spinal cord;prefrontal cortex;atrioventricular node;trigeminal ganglion; 0.65284 0.25920 -0.43902969 24.63434772 428.736 4.32366 ARID4B-IT1 . . . ARID4B intronic transcript 1 . . . unclassifiable (Anatomical System);lymph node;ovary;heart;islets of Langerhans;urinary;colon;blood;skin;breast;uterus;prostate;whole body;lung;frontal lobe;endometrium;trabecular meshwork;bone;thyroid;liver;testis;kidney;brain;stomach; . . . . . . . ARID5A 0.971125743700561 0.0288346018303151 3.96544691235467e-05 AT-rich interaction domain 5A FUNCTION: Binds to AT-rich stretches in the modulator region upstream of the human cytomegalovirus major intermediate early gene enhancer. May act as repressor and down-regulate enhancer- dependent gene expressison. {ECO:0000269|PubMed:8649988}.; . . medulla oblongata;ovary;sympathetic chain;colon;choroid;skin;bone marrow;prostate;optic nerve;whole body;endometrium;synovium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;islets of Langerhans;blood;pancreas;lung;nasopharynx;placenta;spleen;head and neck;kidney;stomach; ciliary ganglion;trigeminal ganglion; 0.09671 0.09711 -0.422438699 25.64284029 110.9881 2.29684 ARID5B 0.999889943413299 0.000110056537775791 4.89249223518836e-11 AT-rich interaction domain 5B FUNCTION: Transcription coactivator that binds to the 5'-AATA[CT]- 3' core sequence and plays a key role in adipogenesis and liver development. Acts by forming a complex with phosphorylated PHF2, which mediates demethylation at Lys-336, leading to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes. The PHF2- ARID5B complex acts as a coactivator of HNF4A in liver. Required for adipogenesis: regulates triglyceride metabolism in adipocytes by regulating expression of adipogenic genes. Overexpression leads to induction of smooth muscle marker genes, suggesting that it may also act as a regulator of smooth muscle cell differentiation and proliferation. Represses the cytomegalovirus enhancer. {ECO:0000269|PubMed:21532585}.; DISEASE: Note=Defects in ARID5B may be a cause of susceptibility to coronary atherosclerosis in the Japanese population.; DISEASE: Leukemia, acute lymphoblastic (ALL) [MIM:613065]: A subtype of acute leukemia, a cancer of the white blood cells. ALL is a malignant disease of bone marrow and the most common malignancy diagnosed in children. The malignant cells are lymphoid precursor cells (lymphoblasts) that are arrested in an early stage of development. The lymphoblasts replace the normal marrow elements, resulting in a marked decrease in the production of normal blood cells. Consequently, anemia, thrombocytopenia, and neutropenia occur to varying degrees. The lymphoblasts also proliferate in organs other than the marrow, particularly the liver, spleen, and lymphonodes. {ECO:0000269|PubMed:19684603, ECO:0000269|PubMed:19684604, ECO:0000269|PubMed:20042726, ECO:0000269|PubMed:20054350, ECO:0000269|PubMed:20189245, ECO:0000269|PubMed:20460642, ECO:0000269|PubMed:21098271}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, including in liver (at protein level). {ECO:0000269|PubMed:21532585}.; smooth muscle;ovary;colon;bone marrow;uterus;larynx;thyroid;testis;germinal center;bladder;tonsil;unclassifiable (Anatomical System);cartilage;blood;lens;skeletal muscle;breast;lung;cornea;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland; uterus corpus;placenta;ciliary ganglion;skeletal muscle; 0.79023 0.11360 -1.03794674 7.832035858 133.85694 2.51593 ARIH1 0.999665081826237 0.000334918024808368 1.48954296375603e-10 ariadne RBR E3 ubiquitin protein ligase 1 FUNCTION: E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin- conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation. Acts as the ligase involved in ISGylation of EIF4E2. {ECO:0000269|PubMed:14623119, ECO:0000269|PubMed:15236971, ECO:0000269|PubMed:17289916, ECO:0000269|PubMed:21532592}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10521492}.; ovary;sympathetic chain;colon;skin;retina;bone marrow;uterus;frontal lobe;thyroid;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;tongue;islets of Langerhans;blood;skeletal muscle;lung;placenta;visual apparatus;liver;head and neck;cervix;kidney; dorsal root ganglion;testis - interstitial;superior cervical ganglion;medulla oblongata;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.41959 . -0.141298762 42.87567823 26.15209 0.84822 ARIH2 0.987412494790781 0.0125874626145247 4.25946941001203e-08 ariadne RBR E3 ubiquitin protein ligase 2 FUNCTION: E3 ubiquitin-protein ligase mediating 'Lys-48'-and 'Lys- 63'-linked polyubiquitination and subsequent proteasomal degradation of modified proteins. May play a role in myelopoiesis. {ECO:0000269|PubMed:16118314, ECO:0000269|PubMed:17646546, ECO:0000269|PubMed:19340006}.; . TISSUE SPECIFICITY: Widely expressed with higher expression in granulocytes. {ECO:0000269|PubMed:16118314}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;epididymis;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach; medulla oblongata;superior cervical ganglion;subthalamic nucleus;occipital lobe;prefrontal cortex;testis;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.06095 0.08179 -0.293801652 32.93819297 9.87647 0.36221 ARIH2OS 0.437613435241329 0.531845014591598 0.0305415501670736 ariadne homolog 2 opposite strand . . . . . . . . . 50.65279 1.40108 ARIH2P1 . . . ariadne RBR E3 ubiquitin protein ligase 2 pseudogene 1 . . . . . . . . . . . ARL1 0.480262743398917 0.514743615620293 0.0049936409807897 ADP ribosylation factor like GTPase 1 FUNCTION: GTP-binding protein that has very low efficiency as allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Can activate phospholipase D with very low efficiency. Important for normal function of the Golgi apparatus. {ECO:0000269|PubMed:9624189}.; . TISSUE SPECIFICITY: Detected in heart, liver, lung and liver (at protein level). Detected in fetal heart, lung, liver and kidney. Detected in adult heart, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:9624189}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;bile duct;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;kidney;stomach;aorta; uterus corpus;superior cervical ganglion;globus pallidus;pons;atrioventricular node;trigeminal ganglion; 0.29849 0.28487 0.057118534 57.99716914 10.46372 0.38083 ARL2 0.00739853976623839 0.772610125877446 0.219991334356316 ADP ribosylation factor like GTPase 2 FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. Component of a regulated secretory pathway involved in Ca(2+)-dependent release of acetylcholine. Required for normal progress through the cell cycle. {ECO:0000269|PubMed:10831612, ECO:0000269|PubMed:16525022, ECO:0000269|PubMed:18234692, ECO:0000269|PubMed:18588884, ECO:0000269|PubMed:20740604}.; . . ovary;umbilical cord;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;synovium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; whole brain;superior cervical ganglion;caudate nucleus; 0.33310 . -0.073340031 48.11866006 3879.18797 12.29119 ARL2-SNX15 . . . ARL2-SNX15 readthrough (NMD candidate) . . . . . . . . . . . ARL2BP 0.000774155836962192 0.770515849525309 0.228709994637729 ADP ribosylation factor like GTPase 2 binding protein FUNCTION: Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. May play a role as an effector of ARL2. {ECO:0000269|PubMed:18234692}.; . TISSUE SPECIFICITY: Expressed in retina pigment epithelial cells (at protein level). Widely expressed. {ECO:0000269|PubMed:10488091, ECO:0000269|PubMed:23849777}.; ovary;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.04825 0.06823 0.125076652 62.7388535 . . ARL2BPP1 . . . ADP ribosylation factor like GTPase 2 binding protein pseudogene 1 . . . . . . . . . . . ARL2BPP2 . . . ADP ribosylation factor like GTPase 2 binding protein pseudogene 2 . . . . . . . . . . . ARL2BPP3 . . . ADP ribosylation factor like GTPase 2 binding protein pseudogene 3 . . . . . . . . . . . ARL2BPP4 . . . ADP ribosylation factor like GTPase 2 binding protein pseudogene 4 . . . . . . . . . . . ARL2BPP5 . . . ADP ribosylation factor like GTPase 2 binding protein pseudogene 5 . . . . . . . . . . . ARL2BPP6 . . . ADP ribosylation factor like GTPase 2 binding protein pseudogene 6 . . . . . . . . . . . ARL2BPP7 . . . ADP ribosylation factor like GTPase 2 binding protein pseudogene 7 . . . . . . . . . . . ARL2BPP8 . . . ADP ribosylation factor like GTPase 2 binding protein pseudogene 8 . . . . . . . . . . . ARL2BPP9 . . . ADP ribosylation factor like GTPase 2 binding protein pseudogene 9 . . . . . . . . . . . ARL2BPP10 . . . ADP ribosylation factor like GTPase 2 binding protein pseudogene 10 . . . . . . . . . . . ARL3 0.716101006738786 0.280723345842669 0.00317564741854472 ADP ribosylation factor like GTPase 3 FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). Required for normal cytokinesis and cilia signaling. Requires assistance from GTPase- activating proteins (GAPs) like RP2 and PDE6D, in order to cycle between inactive GDP-bound and active GTP-bound forms. Required for targeting proteins such as NPHP3 to the ciliary membrane by releasing myristoylated NPHP3 from UNC119B cargo adapter into the cilium. Does not act as an allosteric activator of the cholera toxin catalytic subunit. {ECO:0000269|PubMed:16525022, ECO:0000269|PubMed:18588884, ECO:0000269|PubMed:22085962}.; . TISSUE SPECIFICITY: Expressed in the retina. Strongly expressed in connecting cilium, the myoid region of the inner segments (IS) and in cone photoreceptors (at protein level). {ECO:0000269|PubMed:12417528}.; myocardium;ovary;umbilical cord;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;ciliary body;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;bone;pituitary gland;testis;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;kidney;stomach;thymus;cerebellum; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;medulla oblongata;testis - seminiferous tubule;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.52849 0.14256 -0.119252484 44.53880632 11.09012 0.40173 ARL4A 0.640299399643897 0.331973812745421 0.0277267876106814 ADP ribosylation factor like GTPase 4A FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Recruits CYTH1, CYTH2, CYTH3 and CYTH4 to the plasma membrane in GDP-bound form. {ECO:0000269|PubMed:10980193, ECO:0000269|PubMed:17398095}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;cochlea;oesophagus;endometrium;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;trophoblast;heart;islets of Langerhans;blood;lens;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;mammary gland;aorta;stomach; . 0.52930 0.10703 -0.075159878 47.78839349 4.70588 0.16959 ARL4AP1 . . . ADP ribosylation factor like GTPase 4A pseudogene 1 . . . . . . . . . . . ARL4AP2 . . . ADP ribosylation factor like GTPase 4A pseudogene 2 . . . . . . . . . . . ARL4C 0.607389355262414 0.356926814918803 0.0356838298187825 ADP ribosylation factor like GTPase 4C FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. May be involved in transport between a perinuclear compartment and the plasma membrane, apparently linked to the ABCA1-mediated cholesterol secretion pathway. Recruits CYTH1, CYTH2, CYTH3 and CYTH4 to the plasma membrane in the GDP- bound form. Regulates the microtubule-dependent intracellular vesicular transport from early endosome to recycling endosome process. {ECO:0000269|PubMed:15147902, ECO:0000269|PubMed:17398095, ECO:0000269|PubMed:19409876}.; . TISSUE SPECIFICITY: Expressed in several tumor cell lines (at protein level). Expressed in lung, brain, leukocytes and placenta. {ECO:0000269|PubMed:19409876}.; unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;colon;blood;skin;skeletal muscle;breast;uterus;bile duct;pancreas;prostate;lung;larynx;visual apparatus;testis;head and neck;germinal center;kidney;brain;pineal gland;mammary gland;thymus; subthalamic nucleus;white blood cells;cingulate cortex; 0.67810 0.12910 0.035072054 56.2514744 1.39352 0.04935 ARL4D 0.132429775556647 0.780146623905247 0.0874236005381059 ADP ribosylation factor like GTPase 4D FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Recruits CYTH1, CYTH2, CYTH3 and CYTH4 to the plasma membrane in GDP-bound form. {ECO:0000269|PubMed:17398095}.; . . medulla oblongata;ovary;salivary gland;sympathetic chain;developmental;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;iris;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05933 0.12971 -0.273576253 33.97027601 . . ARL5A 0.0173648434841349 0.891142806201279 0.0914923503145858 ADP ribosylation factor like GTPase 5A FUNCTION: Lacks ADP-ribosylation enhancing activity. {ECO:0000250}.; . . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;alveolus;cervix;kidney;mammary gland;stomach;aorta; placenta;prefrontal cortex;ciliary ganglion;trigeminal ganglion; 0.14164 0.12378 -0.031067188 51.03798066 12.27739 0.44408 ARL5AP1 . . . ADP ribosylation factor like GTPase 5A pseudogene 1 . . . . . . . . . . . ARL5AP2 . . . ADP ribosylation factor like GTPase 5A pseudogene 2 . . . . . . . . . . . ARL5AP3 . . . ADP ribosylation factor like GTPase 5A pseudogene 3 . . . . . . . . . . . ARL5AP4 . . . ADP ribosylation factor like GTPase 5A pseudogene 4 . . . . . . . . . . . ARL5B 0.463976138130045 0.530379863556664 0.00564399831329043 ADP ribosylation factor like GTPase 5B FUNCTION: Binds and exchanges GTP and GDP.; . . . . 0.70675 0.12378 -0.053113545 49.38664779 4.3864 0.15921 ARL5C . . . ADP ribosylation factor like GTPase 5C FUNCTION: Binds and exchanges GTP and GDP. {ECO:0000250}.; . . . . 0.14337 . 1.725294477 96.5027129 4693.71419 13.81234 ARL6 0.0042708684124606 0.866261447411492 0.129467684176047 ADP ribosylation factor like GTPase 6 FUNCTION: Involved in membrane protein trafficking at the base of the ciliary organelle. Mediates recruitment onto plasma membrane of the BBSome complex which would constitute a coat complex required for sorting of specific membrane proteins to the primary cilia (PubMed:20603001). Together with BBS1, is necessary for correct trafficking of PKD1 to primary cilia (By similarity). Together with the BBSome complex and LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation (PubMed:22072986). May regulate cilia assembly and disassembly and subsequent ciliary signaling events such as the Wnt signaling cascade (PubMed:20207729). Isoform 2 may be required for proper retinal function and organization (By similarity). {ECO:0000250|UniProtKB:O88848, ECO:0000269|PubMed:20207729, ECO:0000269|PubMed:20603001, ECO:0000269|PubMed:22072986}.; DISEASE: Bardet-Biedl syndrome 3 (BBS3) [MIM:600151]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:15258860, ECO:0000269|PubMed:15314642, ECO:0000269|PubMed:23219996}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa 55 (RP55) [MIM:613575]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:19956407}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lung;islets of Langerhans;testis;germinal center;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.08372 0.20815 -0.09720619 46.20193442 24.13311 0.79243 ARL6IP1 0.00667568860937067 0.915350405124011 0.0779739062666188 ADP ribosylation factor like GTPase 6 interacting protein 1 FUNCTION: May be involved in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation.; DISEASE: Spastic paraplegia 61, autosomal recessive (SPG61) [MIM:615685]: A complicated form of spastic paraplegia with polysensory and motor neuropathy. Spastic paraplegia is a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. {ECO:0000269|PubMed:24482476}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all hematopoietic cell lineages, but the highest level of expression is found in early myeloid progenitor cells. Expressed in brain, bone marrow, thymus and lung. Expressed at low level in liver, kidney and spleen. Not detected in heart. {ECO:0000269|PubMed:10995579}.; lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;bladder;brain;gall bladder;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; amygdala;occipital lobe;subthalamic nucleus;thalamus;hypothalamus;temporal lobe;prefrontal cortex;globus pallidus;pons;cingulate cortex; 0.25617 0.10772 -0.141298762 42.87567823 . . ARL6IP1P1 . . . ADP ribosylation factor like GTPase 6 interacting protein 1 pseudogene 1 . . . . . . . . . . . ARL6IP1P2 . . . ADP ribosylation factor like GTPase 6 interacting protein 1 pseudogene 2 . . . . . . . . . . . ARL6IP1P3 . . . ADP ribosylation factor like GTPase 6 interacting protein 1 pseudogene 3 . . . . . . . . . . . ARL6IP4 0.0112342008018869 0.948493034884904 0.0402727643132093 ADP ribosylation factor like GTPase 6 interacting protein 4 FUNCTION: Involved in modulating alternative pre-mRNA splicing with either 5' distal site activation or preferential use of 3' proximal site. In case of infection by Herpes simplex virus (HSVI), may act as a splicing inhibitor of HSVI pre-mRNA. {ECO:0000269|PubMed:19582790}.; . TISSUE SPECIFICITY: Isoforms 3 and 7 were identified in brain, pancreas, prostate, and testis, but little or no message could be detected in other tissues. {ECO:0000269|PubMed:19582790}.; lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;pituitary gland;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; temporal lobe;atrioventricular node;pons;cingulate cortex;parietal lobe;skeletal muscle; 0.11852 . . . 959.39716 5.99713 ARL6IP5 0.313164924329023 0.61616688717384 0.070668188497137 ADP ribosylation factor like GTPase 6 interacting protein 5 FUNCTION: Regulates intracellular concentrations of taurine and glutamate. Negatively modulates SLC1A1/EAAC1 glutamate transport activity by decreasing its affinity for glutamate. May be involved in membrane traffic. {ECO:0000250|UniProtKB:Q9ES40}.; . . myocardium;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;gall bladder;amygdala;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pia mater;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;dorsal root ganglion;whole brain;medulla oblongata;occipital lobe;thalamus;subthalamic nucleus;adipose tissue;globus pallidus;ciliary ganglion;caudate nucleus;parietal lobe; 0.21756 0.11576 -0.139478553 43.29440906 16.15719 0.57263 ARL6IP6 0.170955560789642 0.770300557065606 0.0587438821447514 ADP ribosylation factor like GTPase 6 interacting protein 6 . . . ovary;salivary gland;sympathetic chain;developmental;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;kidney;aorta;stomach; . 0.09079 0.09509 -0.005381972 53.50908233 74.76534 1.80937 ARL8A 0.630040288339089 0.368461856772542 0.00149785488836897 ADP ribosylation factor like GTPase 8A FUNCTION: May play a role in lysosomes motility. Alternatively, may play a role in chromosome segregation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15331635}.; ovary;salivary gland;colon;skin;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach; whole brain;amygdala; 0.08537 0.07567 -0.075159878 47.78839349 2.39611 0.08272 ARL8B 0.622356589003264 0.376041414014817 0.00160199698191859 ADP ribosylation factor like GTPase 8B FUNCTION: May play a role in lysosome motility (PubMed:16537643). May play a role in chromosome segregation (PubMed:15331635). {ECO:0000269|PubMed:15331635, ECO:0000269|PubMed:16537643}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15331635}.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;amnion;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;hypothalamus;caudate nucleus;pons;subthalamic nucleus;placenta;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex; 0.33304 0.15588 0.279402865 70.86577023 13.06818 0.47543 ARL9 0.397380993748074 0.562424356325043 0.0401946499268837 ADP ribosylation factor like GTPase 9 . . . unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;whole body;macula lutea;liver;testis;brain;stomach; superior cervical ganglion;testis - interstitial;testis;trigeminal ganglion; 0.12853 0.08565 . . 49.08924 1.36961 ARL10 4.90395449664771e-05 0.425964377836876 0.573986582618158 ADP ribosylation factor like GTPase 10 . . . lung;whole body;ovary;placenta;visual apparatus;testis;parathyroid; . 0.34084 . -0.05129383 49.75819769 24.49093 0.80498 ARL11 8.09182009706795e-06 0.0922497560478889 0.907742152132014 ADP ribosylation factor like GTPase 11 FUNCTION: May play a role in apoptosis. May act as a tumor suppressor. {ECO:0000269|PubMed:15843669}.; . TISSUE SPECIFICITY: Expressed in lung and leukocytes. {ECO:0000269|PubMed:15843669}.; unclassifiable (Anatomical System);uterus;lymph node;lung;testis;blood;bone marrow; superior cervical ganglion;globus pallidus; 0.07084 0.09957 0.703746784 85.42108988 267.65156 3.50858 ARL13A 0.00753187853335742 0.775850166376646 0.216617955089996 ADP ribosylation factor like GTPase 13A . . . . . 0.12879 . 0.058937498 58.26256192 264.73145 3.49118 ARL13B 1.39144766800328e-06 0.833651588155302 0.16634702039703 ADP ribosylation factor like GTPase 13B FUNCTION: Cilium-specific protein required to control the microtubule-based, ciliary axoneme structure. May act by maintaining the association between IFT subcomplexes A and B. Binds GTP but is not able to hydrolyze it; the GTPase activity remains unclear. Required to pattern the neural tube. Involved in cerebral cortex development: required for the initial formation of a polarized radial glial scaffold, the first step in the construction of the cerebral cortex, by regulating ciliary signaling. Regulates the migration and placement of postmitotic interneurons in the developing cerebral cortex. May regulate endocytic recycling traffic; however, additional evidences are required to confirm these data. {ECO:0000269|PubMed:23150559}.; DISEASE: Joubert syndrome 8 (JBTS8) [MIM:612291]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. {ECO:0000269|PubMed:18674751}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;bone;thyroid;testis;dura mater;germinal center;brain;artery;gall bladder;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;pia mater;lung;macula lutea;liver;alveolus;aorta; . 0.06719 0.09956 -0.047654689 50.22410946 555.80587 4.78946 ARL14 2.57323247313565e-06 0.0905480321195572 0.90944939464797 ADP ribosylation factor like GTPase 14 FUNCTION: GTPase that recruits MYO1E to MHC class II-containing vesicles via the effector protein ARL14EP and hence controls the movement of these vesicles along the actin cytoskeleton in dendritic cells. {ECO:0000269|PubMed:21458045}.; . TISSUE SPECIFICITY: Expressed in immature dendritic cells. {ECO:0000269|PubMed:21458045}.; unclassifiable (Anatomical System);pancreas;lymph node;liver;colon;bladder;skin;stomach; appendix;pons;atrioventricular node;cingulate cortex; 0.48070 0.08980 0.305084559 72.22811984 324.40884 3.82893 ARL14EP 0.151697478147144 0.777061040638348 0.0712414812145081 ADP ribosylation factor like GTPase 14 effector protein FUNCTION: Through its interaction with ARL14 and MYO1E, may connect MHC class II-containing cytoplasmic vesicles to the actin network and hence controls the movement of these vesicles along the actin cytoskeleton in dendritic cells. {ECO:0000269|PubMed:21458045}.; . TISSUE SPECIFICITY: Expressed in the immune system. {ECO:0000269|PubMed:21458045}.; . . 0.15816 . -0.073340031 48.11866006 8.48324 0.31134 ARL14EPL . . . ADP ribosylation factor like GTPase 14 effector protein like . . . . . . . . . 39.97085 1.17556 ARL15 0.00886642197401129 0.804130997763244 0.187002580262744 ADP ribosylation factor like GTPase 15 . . . . . 0.61156 0.10510 -0.163345027 41.24793583 6.04468 0.22863 ARL16 0.0215720542657569 0.756346226322257 0.222081719411986 ADP ribosylation factor like GTPase 16 . . . . . 0.08610 . -0.007201372 53.19061099 1141.46967 6.44333 ARL17A . . . ADP ribosylation factor like GTPase 17A FUNCTION: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP- ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus (By similarity). {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;thyroid;testis;bladder;brain;unclassifiable (Anatomical System);cartilage;pharynx;blood;lens;skeletal muscle;bile duct;breast;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; . . . . . . . ARL17B . . . ADP ribosylation factor like GTPase 17B FUNCTION: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP- ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus (By similarity). {ECO:0000250}.; . . . . . . . . . . ARMC1 0.876351937073404 0.123327597336226 0.000320465590370069 armadillo repeat containing 1 . . . smooth muscle;ovary;colon;skin;bone marrow;uterus;prostate;cochlea;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;breast;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;duodenum;cervix;kidney;mammary gland;stomach; amygdala;superior cervical ganglion;medulla oblongata;prefrontal cortex;globus pallidus;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.21876 0.12378 -0.317668748 31.45789101 19.96006 0.67958 ARMC2 2.20161046716889e-08 0.878128853117472 0.121871124866423 armadillo repeat containing 2 . . . unclassifiable (Anatomical System);medulla oblongata;lung;frontal lobe;endometrium;hypothalamus;testis;kidney;brain; superior cervical ganglion;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion; 0.09057 0.08344 -0.551080959 19.93394669 185.89713 2.96040 ARMC2-AS1 . . . ARMC2 antisense RNA 1 . . . . . . . . . . . ARMC3 4.53373054750587e-08 0.988341849200191 0.0116581054625035 armadillo repeat containing 3 . . TISSUE SPECIFICITY: Isoform 2 is expressed in skeletal muscle, brain, lung, kidney, prostate and testis. Isoform 3 is mainly expressed in skeletal muscle, liver, spleen and thymus. Expressed in many cancer tissues and cell lines. {ECO:0000269|PubMed:16397042, ECO:0000269|PubMed:16915934}.; unclassifiable (Anatomical System);breast;uterus;meninges;pia mater;lung;ovary;endometrium;testis;dura mater;skin;skeletal muscle; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; 0.15922 0.09858 0.558509856 81.67020524 2304.3013 8.89063 ARMC4 3.96230149060258e-15 0.0780588304904471 0.921941169509549 armadillo repeat containing 4 FUNCTION: Ciliary protein that may be involved in a late step of axonemal outer dynein arm assembly. {ECO:0000269|PubMed:23849778}.; . TISSUE SPECIFICITY: Expressed in respiratory epithelial cells (at protein level). {ECO:0000269|PubMed:23849778}.; unclassifiable (Anatomical System);uterus;medulla oblongata;lung;bone;liver;testis;kidney;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07694 0.09088 1.118808695 92.0853975 1726.12768 7.66539 ARMC4P1 . . . armadillo repeat containing 4 pseudogene 1 . . . . . . . . . . . ARMC5 0.0462924745566781 0.952629282028146 0.00107824341517559 armadillo repeat containing 5 . DISEASE: ACTH-independent macronodular adrenal hyperplasia 2 (AIMAH2) [MIM:615954]: A form of macronodular adrenal hyperplasia characterized by multiple, bilateral, non-pigmented, benign, adrenocortical nodules. It results in excessive production of cortisol leading to ACTH-independent Cushing syndrome. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes. {ECO:0000269|PubMed:24283224, ECO:0000269|PubMed:24601692, ECO:0000269|PubMed:24905064}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;colon;blood;lens;skin;bone marrow;uterus;pancreas;lung;endometrium;bone;thyroid;liver;testis;spleen;kidney;brain;tonsil;peripheral nerve;thymus; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.20799 . 0.251682437 69.69214437 691.66399 5.24540 ARMC6 7.24407726209859e-07 0.711401092991889 0.288598182600384 armadillo repeat containing 6 . . . medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;larynx;bone;iris;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;liver;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.09654 0.10202 -0.843147538 11.2762444 74.29734 1.80028 ARMC7 0.0149468934826879 0.687241817217174 0.297811289300138 armadillo repeat containing 7 . . . ovary;umbilical cord;foreskin;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;epidermis;islets of Langerhans;muscle;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;spleen;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;medulla oblongata;temporal lobe;globus pallidus;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.06218 0.10661 0.373041938 75.29488087 118.44625 2.36750 ARMC8 0.999883770038606 0.00011622995910619 2.28797469388419e-12 armadillo repeat containing 8 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;endometrium;bone;testis;brain;unclassifiable (Anatomical System);cartilage;pharynx;blood;skeletal muscle;pancreas;lung;cornea;trabecular meshwork;placenta;visual apparatus;liver;kidney;mammary gland;stomach; dorsal root ganglion;fetal liver;superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;pons;atrioventricular node;cerebellum; 0.31859 0.11262 -0.249709319 35.74545883 39.0134 1.15610 ARMC8P1 . . . armadillo repeat containing 8 pseudogene 1 . . . . . . . . . . . ARMC9 1.03024252062501e-08 0.91820298287571 0.0817970068218645 armadillo repeat containing 9 . . TISSUE SPECIFICITY: Strongly expressed in most melanomas and melanocytes. Weakly expressed in the testis. {ECO:0000269|PubMed:11691810}.; unclassifiable (Anatomical System);cartilage;heart;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;breast;prostate;optic nerve;lung;endometrium;bone;placenta;macula lutea;liver;amnion;testis;spleen;brain;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle; 0.34673 0.24308 0.248041348 69.61547535 307.46337 3.73242 ARMC10 0.0312022174247536 0.925544884292048 0.0432528982831985 armadillo repeat containing 10 FUNCTION: May play a role in cell survival and cell growth. May suppress the transcriptional activity of p53/TP53. {ECO:0000269|PubMed:12839973, ECO:0000269|PubMed:17904127}.; . TISSUE SPECIFICITY: Expressed in all tissues tested with higher expression in placenta, liver, kidney, heart and brain. {ECO:0000269|PubMed:12839973}.; myocardium;ovary;salivary gland;developmental;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach;aorta; . 0.09028 0.10643 0.128714042 63.19886766 529.24484 4.69484 ARMC10P1 . . . armadillo repeat containing 10 pseudogene 1 . . . . . . . . . . . ARMC12 0.000270201697673098 0.932218809196294 0.0675109891060331 armadillo repeat containing 12 . . . unclassifiable (Anatomical System);medulla oblongata;pancreas;lung;bone;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;temporal lobe;testis;globus pallidus;pons; 0.28791 . -0.066061882 48.77919321 90.74725 2.05000 ARMCX1 0.395796527068072 0.563575706885504 0.0406277660464239 armadillo repeat containing, X-linked 1 . . TISSUE SPECIFICITY: Expressed at high levels ovary, heart, testis, prostate, brain, spleen and colon. Expressed at very low levels in liver and thymus. Not expressed in peripheral blood leukocytes. Not or reduced expressed in lung, prostate, colon, pancreas and ovarian carcinomas. {ECO:0000269|PubMed:11162520}.; . . 0.08741 0.10417 -0.405853867 26.23260203 8.73022 0.32137 ARMCX2 0.730479736461147 0.257196334904231 0.0123239286346222 armadillo repeat containing, X-linked 2 . . TISSUE SPECIFICITY: Expressed at high levels ovary, heart, testis, prostate, brain, spleen and colon. Expressed at very low levels in liver and thymus. Not expressed in peripheral blood leukocytes. Not expressed in pancreas and ovarian carcinomas. {ECO:0000269|PubMed:11162520}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;adrenal cortex;skeletal muscle;lung;adrenal gland;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; subthalamic nucleus;pons; 0.20334 0.09825 -0.492218069 22.35786742 27.38177 0.88210 ARMCX3 0.249589238901881 0.642159878225949 0.10825088287217 armadillo repeat containing, X-linked 3 . . . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;superior cervical ganglion;parietal lobe; 0.29245 0.10687 0.125076652 62.7388535 28.53458 0.91432 ARMCX3-AS1 . . . ARMCX3 antisense RNA 1 . . . . . . . . . . . ARMCX4 . . . armadillo repeat containing, X-linked 4 . . . unclassifiable (Anatomical System);blood;brain;bone marrow; . . . . . 1487.53197 7.17757 ARMCX5 0.550666214123304 0.435814905787794 0.0135188800889023 armadillo repeat containing, X-linked 5 . . . ovary;parathyroid;fovea centralis;skin;bone marrow;prostate;whole body;larynx;thyroid;bone;germinal center;dura mater;brain;unclassifiable (Anatomical System);meninges;skeletal muscle;breast;pancreas;pia mater;lung;nasopharynx;placenta;macula lutea;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.05846 . -0.249709319 35.74545883 18.8892 0.65189 ARMCX5-GPRASP2 . . . ARMCX5-GPRASP2 readthrough FUNCTION: May play a role in regulation of a variety of G-protein coupled receptors. {ECO:0000269|PubMed:15086532}.; . TISSUE SPECIFICITY: Expressed in the brain. {ECO:0000269|PubMed:15086532}.; . . . . . . . . ARMCX6 0.259563477582888 0.639238274370679 0.101198248046434 armadillo repeat containing, X-linked 6 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;thymus; . 0.15275 . . . 466.38729 4.47407 ARMCX7P . . . armadillo repeat containing, X-linked 7, pseudogene . . . . . . . . . . . ARMS2 0.0391826461982656 0.644883511001034 0.3159338428007 age-related maculopathy susceptibility 2 . . TISSUE SPECIFICITY: Detected in retina and placenta. {ECO:0000269|PubMed:17884985}.; . . . . 0.72397987 85.91648974 2588.6288 9.51674 ARMT1 . . . acidic residue methyltransferase 1 FUNCTION: O-methyltransferase that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues. Methylates PCNA, suggesting it is involved in the DNA damage response. {ECO:0000269|PubMed:25732820}.; . . . . 0.62908 0.08819 0.284856336 71.40835103 . . ARNT 0.976348195268955 0.0236517964934275 8.23761768385443e-09 aryl hydrocarbon receptor nuclear translocator FUNCTION: Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens. The heterodimer with HIF1A or EPAS1/HIF2A functions as a transcriptional regulator of the adaptive response to hypoxia.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;spinal cord;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;placenta;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.28663 0.22862 -0.534490515 20.70063694 99.66528 2.16216 ARNT2 0.959019737658223 0.0409801029994765 1.59342300886731e-07 aryl hydrocarbon receptor nuclear translocator 2 FUNCTION: Transcription factor that plays a role in the development of the hypothalamo-pituitary axis, postnatal brain growth, and visual and renal function (PubMed:24022475). Specifically recognizes the xenobiotic response element (XRE). {ECO:0000269|PubMed:24022475}.; DISEASE: Webb-Dattani syndrome (WEDAS) [MIM:615926]: A disorder characterized by postnatal microcephaly with fronto-temporal lobe hypoplasia, multiple pituitary hormone deficiency, global developmental delay, seizures, severe visual impairment and abnormalities of the kidneys and urinary tract. {ECO:0000269|PubMed:24022475}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;sympathetic chain;intestine;colon;substantia nigra;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;larynx;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; whole brain;amygdala;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.16608 0.18581 -0.841329384 11.36470866 903.6659 5.85290 ARNTL 0.987642966676249 0.012356992617467 4.07062837656019e-08 aryl hydrocarbon receptor nuclear translocator like FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time- keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. ARNTL/BMAL1 positively regulates myogenesis and negatively regulates adipogenesis via the transcriptional control of the genes of the canonical Wnt signaling pathway. Plays a role in normal pancreatic beta-cell function; regulates glucose-stimulated insulin secretion via the regulation of antioxidant genes NFE2L2/NRF2 and its targets SESN2, PRDX3, CCLC and CCLM. Negatively regulates the mTORC1 signaling pathway; regulates the expression of MTOR and DEPTOR. Controls diurnal oscillations of Ly6C inflammatory monocytes; rhythmic recruitment of the PRC2 complex imparts diurnal variation to chemokine expression that is necessary to sustain Ly6C monocyte rhythms. Regulates the expression of HSD3B2, STAR, PTGS2, CYP11A1, CYP19A1 and LHCGR in the ovary and also the genes involved in hair growth. Plays an important role in adult hippocampal neurogenesis by regulating the timely entry of neural stem/progenitor cells (NSPCs) into the cell cycle and the number of cell divisions that take place prior to cell-cycle exit. Regulates the circadian expression of CIART and KLF11. The CLOCK-ARNTL/BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The NPAS2-ARNTL/BMAL1 heterodimer positively regulates the expression of MAOA, F7 and LDHA and modulates the circadian rhythm of daytime contrast sensitivity by regulating the rhythmic expression of adenylate cyclase type 1 (ADCY1) in the retina. {ECO:0000269|PubMed:11441146, ECO:0000269|PubMed:12738229, ECO:0000269|PubMed:18587630, ECO:0000269|PubMed:23785138, ECO:0000269|PubMed:23955654, ECO:0000269|PubMed:24005054}.; . TISSUE SPECIFICITY: Hair follicles (at protein level). Highly expressed in the adult brain, skeletal muscle and heart. {ECO:0000269|PubMed:24005054}.; ovary;parathyroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;whole body;frontal lobe;endometrium;bone;brain;unclassifiable (Anatomical System);heart;skeletal muscle;pancreas;lung;placenta;hippocampus;visual apparatus;macula lutea;liver;spleen;kidney;stomach; whole brain;subthalamic nucleus;medulla oblongata;globus pallidus; 0.78112 0.39466 -0.337894035 30.37272942 28.86459 0.92228 ARNTL2 2.37204609554434e-06 0.976967049079397 0.0230305788745075 aryl hydrocarbon receptor nuclear translocator like 2 FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time- keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. The CLOCK-ARNTL2/BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. {ECO:0000269|PubMed:11018023, ECO:0000269|PubMed:12738229, ECO:0000269|PubMed:14672706}.; . TISSUE SPECIFICITY: Expressed in fetal brain. Highly expressed in brain and placenta. Lower levels in heart, liver, thymus, kidney and lung. Located to endothelial cells and neuronal cells of the suprachiasmatic nucleus (SCN). Also detected in endothelial cells of the heart, lung and kidney. In the brain, specifically expressed in the thalamus, hippocampus and amygdala. {ECO:0000269|PubMed:10864977, ECO:0000269|PubMed:10964693, ECO:0000269|PubMed:11018023}.; unclassifiable (Anatomical System);cartilage;colon;skin;bile duct;uterus;lung;endometrium;placenta;bone;hypopharynx;testis;head and neck; superior cervical ganglion;trigeminal ganglion; 0.32532 0.09651 0.553050905 81.54635527 424.91448 4.30627 ARNTL2-AS1 . . . ARNTL2 antisense RNA 1 . . . . . . . . . . . ARPC1A 0.734759682759801 0.265131292785209 0.000109024454990132 actin related protein 2/3 complex subunit 1A FUNCTION: Probably functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.; . . medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;atrium;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;cerebellum; . 0.39087 0.10381 -0.516085732 21.20193442 44.60173 1.28044 ARPC1B 0.156070499348014 0.840539011618878 0.00339048903310833 actin related protein 2/3 complex subunit 1B FUNCTION: Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.; . . lymphoreticular;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;endometrium;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; lung;heart;tumor;white blood cells;whole blood;tonsil; 0.41263 0.12897 -0.336073593 30.55555556 315.92345 3.77511 ARPC2 0.990984291645615 0.00901344100262779 2.26735175704907e-06 actin related protein 2/3 complex subunit 2 FUNCTION: Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament.; . . myocardium;lymphoreticular;smooth muscle;ovary;skin;bone marrow;prostate;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;cartilage;heart;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;amnion;head and neck;kidney;stomach;aorta; testis - interstitial;smooth muscle;lung;placenta;testis;white blood cells;whole blood;tonsil;bone marrow; 0.47982 0.17821 -0.251530012 35.42108988 8.05181 0.29538 ARPC3 0.931506660806945 0.0681512078771207 0.000342131315933794 actin related protein 2/3 complex subunit 3 FUNCTION: Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;pia mater;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; white blood cells;whole blood; 0.39540 0.17605 0.125076652 62.7388535 10.19968 0.37163 ARPC3P1 . . . actin related protein 2/3 complex subunit 3 pseudogene 1 . . . . . . . . . . . ARPC3P2 . . . actin related protein 2/3 complex subunit 3 pseudogene 2 . . . . . . . . . . . ARPC3P3 . . . actin related protein 2/3 complex subunit 3 pseudogene 3 . . . . . . . . . . . ARPC3P4 . . . actin related protein 2/3 complex subunit 3 pseudogene 4 . . . . . . . . . . . ARPC3P5 . . . actin related protein 2/3 complex subunit 3 pseudogene 5 . . . . . . . . . . . ARPC4 0.937798821155646 0.0619327810563193 0.000268397788034668 actin related protein 2/3 complex subunit 4 FUNCTION: Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament.; . . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);trophoblast;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; thalamus;superior cervical ganglion;smooth muscle;temporal lobe;liver;white blood cells;whole blood;trigeminal ganglion;tonsil; . 0.09890 0.145304857 63.81221986 3.73967 0.13899 ARPC4-TTLL3 1.37468731036407e-12 0.0917813147225403 0.908218685276085 ARPC4-TTLL3 readthrough . . . . . . . -0.709045403 14.673272 3805.21185 12.12505 ARPC5 0.772685974822978 0.219579286090528 0.00773473908649371 actin related protein 2/3 complex subunit 5 FUNCTION: Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.; . . smooth muscle;ovary;sympathetic chain;skin;bone marrow;prostate;optic nerve;endometrium;thyroid;bladder;brain;heart;cartilage;tongue;pineal body;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;placenta;whole blood;bone marrow; 0.09161 . -0.251530012 35.42108988 6.54074 0.24200 ARPC5L 0.775599153315343 0.216931774383467 0.00746907230119068 actin related protein 2/3 complex subunit 5-like FUNCTION: May function as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pineal body;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;head and neck;kidney;stomach;aorta; amygdala;whole brain;testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;temporal lobe;testis; 0.07894 0.17050 -0.075159878 47.78839349 8.80248 0.32496 ARPIN . . . actin-related protein 2/3 complex inhibitor FUNCTION: Regulates actin polymerization by inhibiting the actin- nucleating activity of the Arp2/3 complex; the function is competetive with nucleation promoting factors. Participates in an incoherent feedforward loop at the lamellipodium tip where it inhibits the ARP2/2 complex in response to Rac signaling and where Rac also stimulates actin polymerization through the WAVE complex. Involved in steering cell migration by controlling its directional persistence. {ECO:0000269|PubMed:24132237}.; . . . . 0.06899 0.09268 -0.560178693 19.30879925 . . ARPP19 0.269804297590526 0.635738377498126 0.0944573249113479 cAMP regulated phosphoprotein 19kDa FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression. {ECO:0000269|PubMed:21164014}.; . . smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;amygdala;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;oral cavity;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; whole brain;amygdala;occipital lobe;medulla oblongata;thalamus;superior cervical ganglion;olfactory bulb;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; . . -0.009020804 52.8544468 7.54992 0.28044 ARPP21 0.00367693074803101 0.996246529119336 7.65401326328975e-05 cAMP regulated phosphoprotein 21kDa FUNCTION: Isoform 2 may act as a competitive inhibitor of calmodulin-dependent enzymes such as calcineurin in neurons. {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 2 is expressed in brain. Isoform 1 is present in immature thymocytes (at protein level). {ECO:0000269|PubMed:15096520, ECO:0000269|PubMed:8120638}.; unclassifiable (Anatomical System);amygdala;heart;ovary;parathyroid;skeletal muscle;skin;uterus;whole body;lung;frontal lobe;placenta;visual apparatus;hippocampus;hypopharynx;testis;head and neck;brain; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; . . -0.176292081 40.56381222 963.20115 6.00774 ARPP21-AS1 . . . ARPP21 antisense RNA 1 . . . . . . . . . . . ARR3 0.137242313191003 0.85846477383937 0.00429291296962702 arrestin 3, retinal (X-arrestin) FUNCTION: May play a role in an as yet undefined retina-specific signal transduction. Could binds to photoactivated-phosphorylated red/green opsins.; . TISSUE SPECIFICITY: Inner and outer segments, and the inner plexiform regions of the retina.; unclassifiable (Anatomical System);optic nerve;macula lutea;visual apparatus;fovea centralis;choroid;lens;skeletal muscle;retina; superior cervical ganglion;skeletal muscle; 0.66223 0.19245 -0.22584292 37.32012267 28.84914 0.92200 ARRB1 0.986801821116486 0.0131970105033691 1.16838014470558e-06 arrestin, beta 1 FUNCTION: Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G- protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta- arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Involved in internalization of P2RY4 and UTP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 ands subsequent recycling. Involved in the degradation of cAMP by recruiting cAMP phosphodiesterases to ligand-activated receptors. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2). ERK1/2 activated by the beta- arrestin scaffold is largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Recruits c-Src/SRC to ADRB2 resulting in ERK activation. GPCRs for which the beta-arrestin- mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Inhibits ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Is required for SP-stimulated endocytosis of NK1R and recruits c-Src/SRC to internalized NK1R resulting in ERK1/2 activation, which is required for the antiapoptotic effects of SP. Is involved in proteinase-activated F2RL1-mediated ERK activity. Acts as signaling scaffold for the AKT1 pathway. Is involved in alpha- thrombin-stimulated AKT1 signaling. Is involved in IGF1-stimulated AKT1 signaling leading to increased protection from apoptosis. Involved in activation of the p38 MAPK signaling pathway and in actin bundle formation. Involved in F2RL1-mediated cytoskeletal rearrangement and chemotaxis. Involved in AGTR1-mediated stress fiber formation by acting together with GNAQ to activate RHOA. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. May serve as nuclear messenger for GPCRs. Involved in OPRD1- stimulated transcriptional regulation by translocating to CDKN1B and FOS promoter regions and recruiting EP300 resulting in acetylation of histone H4. Involved in regulation of LEF1 transcriptional activity via interaction with DVL1 and/or DVL2 Also involved in regulation of receptors other than GPCRs. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Binds phosphoinositides. Binds inositolhexakisphosphate (InsP6) (By similarity). Involved in IL8-mediated granule release in neutrophils. Required for atypical chemokine receptor ACKR2- induced RAC1-LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Involved in the internalization of the atypical chemokine receptor ACKR3. {ECO:0000250, ECO:0000269|PubMed:12464600, ECO:0000269|PubMed:14711824, ECO:0000269|PubMed:15475570, ECO:0000269|PubMed:15611106, ECO:0000269|PubMed:15671180, ECO:0000269|PubMed:15878855, ECO:0000269|PubMed:16144840, ECO:0000269|PubMed:16280323, ECO:0000269|PubMed:16378096, ECO:0000269|PubMed:16492667, ECO:0000269|PubMed:16709866, ECO:0000269|PubMed:18337459, ECO:0000269|PubMed:18419762, ECO:0000269|PubMed:19620252, ECO:0000269|PubMed:19643177, ECO:0000269|PubMed:22457824, ECO:0000269|PubMed:23341447, ECO:0000269|PubMed:23633677}.; . . unclassifiable (Anatomical System);cartilage;heart;colon;blood;choroid;skin;bone marrow;uterus;prostate;lung;frontal lobe;cerebral cortex;bone;placenta;hypopharynx;liver;testis;head and neck;spleen;kidney;brain;stomach;gall bladder; superior cervical ganglion;skeletal muscle; 0.26736 0.17451 -0.844966979 11.1759849 138.55265 2.56415 ARRB2 0.769282968108594 0.23064434093159 7.26909598158238e-05 arrestin, beta 2 FUNCTION: Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G- protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta- arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Mediates endocytosis of CCR7 following ligation of CCL19 but not CCL21. Involved in internalization of P2RY1, P2RY4, P2RY6 and P2RY11 and ATP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 and subsequent recycling or degradation. Involved in ubiquitination of IGF1R. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2) and MAPK10 (JNK3). ERK1/2 and JNK3 activated by the beta-arrestin scaffold are largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Acts as signaling scaffold for the AKT1 pathway. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin- mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Increases ERK1/2 signaling in AGTR1- and AVPR2- mediated activation (reciprocal regulation). Involved in CCR7- mediated ERK1/2 signaling involving ligand CCL19. Is involved in type-1A angiotensin II receptor/AGTR1-mediated ERK activity. Is involved in type-1A angiotensin II receptor/AGTR1-mediated MAPK10 activity. Is involved in dopamine-stimulated AKT1 activity in the striatum by disrupting the association of AKT1 with its negative regulator PP2A. Involved in AGTR1-mediated chemotaxis. Appears to function as signaling scaffold involved in regulation of MIP-1- beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. Suppresses UV-induced NF-kappa-B-dependent activation by interacting with CHUK. The function is promoted by stimulation of ADRB2 and dephosphorylation of ARRB2. Involved in p53/TP53- mediated apoptosis by regulating MDM2 and reducing the MDM2- mediated degradation of p53/TP53. May serve as nuclear messenger for GPCRs. Upon stimulation of OR1D2, may be involved in regulation of gene expression during the early processes of fertilization. Also involved in regulation of receptors other than GPCRs. Involved in endocytosis of TGFBR2 and TGFBR3 and down- regulates TGF-beta signaling such as NF-kappa-B activation. Involved in endocytosis of low-density lipoprotein receptor/LDLR. Involved in endocytosis of smoothened homolog/Smo, which also requires ADRBK1. Involved in endocytosis of SLC9A5. Involved in endocytosis of ENG and subsequent TGF-beta-mediated ERK activation and migration of epithelial cells. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Involved in insulin resistance by acting as insulin-induced signaling scaffold for SRC, AKT1 and INSR. Involved in regulation of inhibitory signaling of natural killer cells by recruiting PTPN6 and PTPN11 to KIR2DL1. Involved in IL8-mediated granule release in neutrophils. Involved in the internalization of the atypical chemokine receptor ACKR3. {ECO:0000269|PubMed:10644702, ECO:0000269|PubMed:11877451, ECO:0000269|PubMed:12488444, ECO:0000269|PubMed:12582207, ECO:0000269|PubMed:12949261, ECO:0000269|PubMed:12958365, ECO:0000269|PubMed:14711824, ECO:0000269|PubMed:15054093, ECO:0000269|PubMed:15125834, ECO:0000269|PubMed:15205453, ECO:0000269|PubMed:15475570, ECO:0000269|PubMed:15618519, ECO:0000269|PubMed:15635042, ECO:0000269|PubMed:15671180, ECO:0000269|PubMed:15699339, ECO:0000269|PubMed:15878855, ECO:0000269|PubMed:16144840, ECO:0000269|PubMed:16280323, ECO:0000269|PubMed:16378096, ECO:0000269|PubMed:16492667, ECO:0000269|PubMed:16820410, ECO:0000269|PubMed:17540773, ECO:0000269|PubMed:18419762, ECO:0000269|PubMed:18604210, ECO:0000269|PubMed:19325136, ECO:0000269|PubMed:19620252, ECO:0000269|PubMed:19643177, ECO:0000269|PubMed:20048153, ECO:0000269|PubMed:22457824}.; . . lymphoreticular;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;blood;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum;thymus; white blood cells;whole blood;bone marrow; 0.58827 0.57942 -0.670411825 15.61689078 141.04803 2.59189 ARRDC1 0.000232262782397713 0.753163088449268 0.246604648768334 arrestin domain containing 1 . . . . . 0.09209 . 0.112125503 62.09601321 367.33074 4.05116 ARRDC1-AS1 . . . ARRDC1 antisense RNA 1 . . . . . 0.09840 . 0.12689526 63.00424628 . . ARRDC2 5.13482607596469e-05 0.873458438194699 0.126490213544542 arrestin domain containing 2 . . . lymphoreticular;ovary;colon;choroid;uterus;prostate;optic nerve;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;placenta;hippocampus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.35560 . 0.446457185 77.97829677 1904.40788 8.03056 ARRDC3 0.978746961781062 0.021249266051371 3.77216756709287e-06 arrestin domain containing 3 FUNCTION: Adapter protein that plays a role in regulating cell- surface expression of adrenergic receptors and probably also other G protein-coupled receptors (PubMed:20559325, PubMed:21982743, PubMed:23208550). Plays a role in NEDD4-mediated ubiquitination and endocytosis af activated ADRB2 and subsequent ADRB2 degradation (PubMed:20559325, PubMed:23208550). May recruit NEDD4 to ADRB2 (PubMed:20559325). Alternatively, may function as adapter protein that does not play a major role in recruiting NEDD4 to ADRB2, but rather plays a role in a targeting ADRB2 to endosomes (PubMed:23208550). {ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:23208550}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle, placenta, kidney, lung, liver, blood, adrenal gland, lymph node, mammary gland, thyroid, and trachea (PubMed:16269462, PubMed:21982743). Very low levels in colon, thymus, spleen, small intestine, bladder and bone marrow (PubMed:16269462). Strong expression in differentiated adipocytes compared to preadipocytes (PubMed:16269462). Detected in omental fat and subcutaneous fat tissue (PubMed:21982743). {ECO:0000269|PubMed:16269462}.; ovary;umbilical cord;sympathetic chain;rectum;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;mammary gland;developmental;colon;parathyroid;fovea centralis;choroid;uterus;oesophagus;bone;pituitary gland;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;adrenal gland;placenta;hippocampus;kidney;aorta;stomach;thymus; dorsal root ganglion;adrenal cortex;trigeminal ganglion; 0.79620 0.13881 -0.095386216 46.48502005 15.79241 0.56251 ARRDC3-AS1 . . . ARRDC3 antisense RNA 1 . . . . . . . . . . . ARRDC4 0.000815443122975903 0.931074843453772 0.0681097134232515 arrestin domain containing 4 FUNCTION: Adapter protein that may play a role in endocytosis and/or ubiquitination of activated G protein-coupled receptors (GPCRs) (Probable). When overexpressed, inhibits glucose uptake (PubMed:19605364). {ECO:0000269|PubMed:19605364, ECO:0000305}.; . . lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;spinal ganglion;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;cerebrum;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney; superior cervical ganglion; 0.61153 0.10975 0.463046108 78.58575136 4696.45685 13.81768 ARRDC5 1.97507105170421e-06 0.145516464596484 0.854481560332464 arrestin domain containing 5 . . . . . 0.07853 . -0.356299879 29.31115829 119.66578 2.38092 ARSA 8.51321818711031e-08 0.291195894702315 0.708804020165503 arylsulfatase A FUNCTION: Hydrolyzes cerebroside sulfate.; DISEASE: Leukodystrophy metachromatic (MLD) [MIM:250100]: A leukodystrophy due to a lysosomal storage defect. Characterized by intralysosomal storage of cerebroside-3-sulfate in neural and non- neural tissues, with a diffuse loss of myelin in the central nervous system. Progressive demyelination causes a variety of neurological symptoms, including gait disturbances, ataxias, optical atrophy, dementia, seizures, and spastic tetraparesis. Three forms of the disease can be distinguished according to the age at onset: late-infantile, juvenile and adult. {ECO:0000269|PubMed:10220151, ECO:0000269|PubMed:10381328, ECO:0000269|PubMed:10477432, ECO:0000269|PubMed:10533072, ECO:0000269|PubMed:10751093, ECO:0000269|PubMed:11020646, ECO:0000269|PubMed:11061266, ECO:0000269|PubMed:11456299, ECO:0000269|PubMed:11941485, ECO:0000269|PubMed:1353340, ECO:0000269|PubMed:14517960, ECO:0000269|PubMed:14680985, ECO:0000269|PubMed:15026521, ECO:0000269|PubMed:15326627, ECO:0000269|PubMed:15710861, ECO:0000269|PubMed:1670590, ECO:0000269|PubMed:1673291, ECO:0000269|PubMed:1678251, ECO:0000269|PubMed:18693274, ECO:0000269|PubMed:19606494, ECO:0000269|PubMed:20339381, ECO:0000269|PubMed:21265945, ECO:0000269|PubMed:7581401, ECO:0000269|PubMed:7825603, ECO:0000269|PubMed:7860068, ECO:0000269|PubMed:7902317, ECO:0000269|PubMed:7906588, ECO:0000269|PubMed:7909527, ECO:0000269|PubMed:8095918, ECO:0000269|PubMed:8101038, ECO:0000269|PubMed:8101083, ECO:0000269|PubMed:8104633, ECO:0000269|PubMed:8891236, ECO:0000269|PubMed:9090526, ECO:0000269|PubMed:9272717, ECO:0000269|PubMed:9452102, ECO:0000269|PubMed:9490297, ECO:0000269|PubMed:9600244, ECO:0000269|PubMed:9819708}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multiple sulfatase deficiency (MSD) [MIM:272200]: A clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post- translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. {ECO:0000269|PubMed:15146462}. Note=The protein represented in this entry is involved in disease pathogenesis. Arylsulfatase A activity is impaired in multiple sulfatase deficiency due to mutations in SUMF1 (PubMed:15146462). SUMF1 mutations result in defective post-translational modification of ARSA at residue Cys-69 that is not converted to 3- oxoalanine (PubMed:7628016). {ECO:0000269|PubMed:15146462, ECO:0000269|PubMed:7628016}.; . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;iris;testis;amniotic fluid;brain;tonsil;unclassifiable (Anatomical System);heart;nervous;islets of Langerhans;blood;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;liver;cervix;spleen;kidney;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.15293 0.69768 0.156217551 64.82071243 3502.02917 11.40568 ARSB 0.00126175276165402 0.990183494889165 0.00855475234918157 arylsulfatase B FUNCTION: Removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation (PubMed:19306108). Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium (PubMed:19306108). In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity, acting through the control of sulfate glycosaminoglycans and neurocan levels (By similarity). {ECO:0000250|UniProtKB:P50430, ECO:0000269|PubMed:19306108}.; DISEASE: Mucopolysaccharidosis 6 (MPS6) [MIM:253200]: An autosomal recessive lysosomal storage disease characterized by intracellular accumulation of dermatan sulfate. Clinical features can include abnormal growth, short stature, stiff joints, skeletal malformations, corneal clouding, hepatosplenomegaly, and cardiac abnormalities. A wide variation in clinical severity is observed. {ECO:0000269|PubMed:10036316, ECO:0000269|PubMed:10738004, ECO:0000269|PubMed:11802522, ECO:0000269|PubMed:14974081, ECO:0000269|PubMed:1550123, ECO:0000269|PubMed:1718978, ECO:0000269|PubMed:8116615, ECO:0000269|PubMed:8125475, ECO:0000269|PubMed:8541342, ECO:0000269|PubMed:8651289}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multiple sulfatase deficiency (MSD) [MIM:272200]: A clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post- translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. {ECO:0000269|PubMed:15146462}. Note=The protein represented in this entry is involved in disease pathogenesis. Arylsulfatase B activity is impaired in multiple sulfatase deficiency due to mutations in SUMF1. SUMF1 mutations result in defective post-translational modification of ARSB at residue Cys-91 that is not converted to 3-oxoalanine.; . ovary;colon;skin;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;pancreas;lung;placenta;visual apparatus;liver;alveolus;spleen;cervix;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.06229 0.25636 0.020302773 55.60863411 4529.62881 13.52305 ARSC2 . . . arylsulfatase C, isozyme F . . . . . . . . . . . ARSD 0.292872844082226 0.702739259685643 0.00438789623213087 arylsulfatase D . . TISSUE SPECIFICITY: Expressed in the pancreas, kidney, liver, lung, placenta, brain and heart.; unclassifiable (Anatomical System);lung;ovary;placenta;blood;brain;mammary gland;vein; prostate;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.42366 0.14372 0.176444282 66.07100731 612.96979 5.00406 ARSD-AS1 . . . ARSD antisense RNA 1 . . . . . . . . . . . ARSDP1 . . . arylsulfatase D pseudogene 1 . . . . . . . . . . . ARSE 0.120625324518616 0.873977397032944 0.00539727844843954 arylsulfatase E (chondrodysplasia punctata 1) FUNCTION: May be essential for the correct composition of cartilage and bone matrix during development. Has no activity toward steroid sulfates.; DISEASE: Chondrodysplasia punctata 1, X-linked recessive (CDPX1) [MIM:302950]: A clinically and genetically heterogeneous disorder characterized by punctiform calcification of the bones. CDPX1 is a congenital defect of bone and cartilage development characterized by aberrant bone mineralization, severe underdevelopment of nasal cartilage, and distal phalangeal hypoplasia. This disease can also be induced by inhibition with the drug warfarin. {ECO:0000269|PubMed:12567415, ECO:0000269|PubMed:7720070, ECO:0000269|PubMed:9409863}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the pancreas, liver and kidney.; . . 0.16729 0.09780 0.288494088 71.50861052 43.07178 1.24628 ARSEP1 . . . arylsulfatase E pseudogene 1 . . . . . . . . . . . ARSF 4.0838492730915e-07 0.587558358725498 0.412441232889575 arylsulfatase F . . . prostate;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.12163 0.12262 0.358272123 74.66383581 220.71762 3.21257 ARSFP1 . . . arylsulfatase F pseudogene 1 . . . . . . . . . . . ARSG 1.55401104160652e-05 0.86208074969914 0.137903710190444 arylsulfatase G FUNCTION: Displays arylsulfatase activity at acidic pH with pseudosubstrates, such as p-nitrocatechol sulfate and also, but with lower activity, p-nitrophenyl sulfate and 4- methylumbelliferyl sulfate. {ECO:0000269|PubMed:18283100}.; . TISSUE SPECIFICITY: Widely expressed, with very low expression in brain, lung, heart and skeletal muscle. {ECO:0000269|PubMed:12461688, ECO:0000269|PubMed:18283100}.; . . 0.14635 0.12602 0.314179756 72.75300778 3707.52836 11.87521 ARSH 0.00160023102984739 0.885313752953739 0.113086016016414 arylsulfatase family member H . . . . . 0.06296 . 1.445891753 95.12267044 662.35638 5.15714 ARSI 1.05161485653303e-09 0.0898826682553554 0.91011733069303 arylsulfatase family member I FUNCTION: Displays arylsulfatase activity at neutral pH, when co- expressed with SUMF1; arylsulfatase activity is measured in the secretion medium of retinal cell line, but no activity is recorded when measured in cell extracts. {ECO:0000269|PubMed:16500042, ECO:0000269|PubMed:19262745}.; . TISSUE SPECIFICITY: Expressed in placenta, in embryonic stem cells, fetal eyes and lens. {ECO:0000269|PubMed:16500042, ECO:0000269|PubMed:19262745}.; unclassifiable (Anatomical System);heart;colon;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;whole body;lung;placenta;bone;macula lutea;iris;spleen;tonsil; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.12230 0.15805 -1.03976177 7.802547771 156.19896 2.73165 ARSJ 0.00345579904808939 0.951875447404408 0.0446687535475028 arylsulfatase family member J . . . unclassifiable (Anatomical System);bile duct;prostate;pancreas;heart;muscle;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;caudate nucleus;pons;trigeminal ganglion;parietal lobe; 0.06974 0.10996 -0.091746757 46.91554612 52.86267 1.44205 ARSK 0.00461420992933416 0.988837487313671 0.00654830275699448 arylsulfatase family member K . . . . . 0.04508 . -0.26629572 34.81953291 87.35964 1.99657 ART1 1.54462673964299e-09 0.0593078342038821 0.940692164251491 ADP-ribosyltransferase 1 FUNCTION: Has ADP-ribosyltransferase activity toward GLP1R. {ECO:0000269|PubMed:21901419}.; . . . . 0.07207 0.18162 1.043548753 91.30691201 494.79174 4.57285 ART2BP . . . ADP-ribosyltransferase 2B, pseudogene . . . . . . . . . . . ART2P . . . ADP-ribosyltransferase 2, pseudogene . . . . . . . . . . . ART3 2.26602612517891e-08 0.261535259283254 0.738464718056485 ADP-ribosyltransferase 3 . . TISSUE SPECIFICITY: Testis specific.; unclassifiable (Anatomical System);heart;colon;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;whole body;lung;frontal lobe;macula lutea;liver;testis;brain; superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.25800 0.11097 0.218717575 68.27081859 2234.29932 8.71204 ART4 0.00145180854137921 0.671162778460889 0.327385412997731 ADP-ribosyltransferase 4 (Dombrock blood group) . . TISSUE SPECIFICITY: Expressed in spleen and T-cells.; heart;liver;colon;spleen;blood;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.06743 0.20381 0.92967242 89.79122435 1732.36072 7.68098 ART5 0.0172264751087272 0.89040953491927 0.092363989972003 ADP-ribosyltransferase 5 . . . unclassifiable (Anatomical System);optic nerve;lung;cochlea;macula lutea;testis;fovea centralis;choroid;lens;skeletal muscle;retina; superior cervical ganglion;fetal liver;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.19165 0.13717 2.173627394 98.05378627 1119.68962 6.38981 ARTN 0.293100341552423 0.62609689411188 0.0808027643356973 artemin FUNCTION: Ligand for the GFR-alpha-3-RET receptor complex but can also activate the GFR-alpha-1-RET receptor complex. Supports the survival of sensory and sympathetic peripheral neurons in culture and also supports the survival of dopaminergic neurons of the ventral mid-brain. Strong attractant of gut hematopoietic cells thus promoting the formation Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. {ECO:0000269|PubMed:10583383, ECO:0000269|PubMed:9883723}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in peripheral tissues including prostate, placenta, pancreas, heart, kidney, pituitary gland, lung and testis. Expressed at low levels in the brain. {ECO:0000269|PubMed:10583383, ECO:0000269|PubMed:9883723}.; . . 0.03603 0.18028 1.644346333 96.16654871 4.82839 0.17721 ARV1 1.54945904545113e-06 0.232544147721868 0.767454302819086 ARV1 homolog, fatty acid homeostasis modulator FUNCTION: May act as a mediator of sterol homeostasis. {ECO:0000305}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;kidney;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node; 0.10128 . 0.327131069 73.27199811 . . ARVCF 8.21839210300339e-07 0.978565829581306 0.0214333485794841 armadillo repeat gene deleted in velocardiofacial syndrome FUNCTION: Involved in protein-protein interactions at adherens junctions.; . TISSUE SPECIFICITY: Found in all the examined tissues including heart, brain, liver and kidney. Found at low level in lung.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.26337 0.12771 -0.053328617 48.95022411 2305.0631 8.89579 ARVD3 . . . arrhythmogenic right ventricular dysplasia 3 . . . . . . . . . . . ARVD4 . . . arrhythmogenic right ventricular dysplasia 4 . . . . . . . . . . . ARX 0.75306908332634 0.237240976393997 0.00968994027966388 aristaless related homeobox FUNCTION: Transcription factor required for normal brain development. May be important for maintenance of specific neuronal subtypes in the cerebral cortex and axonal guidance in the floor plate.; DISEASE: Epileptic encephalopathy, early infantile, 1 (EIEE1) [MIM:308350]: A severe form of epilepsy characterized by frequent tonic seizures or spasms beginning in infancy with a specific EEG finding of suppression-burst patterns, characterized by high- voltage bursts alternating with almost flat suppression phases. Patients may progress to West syndrome, which is characterized by tonic spasms with clustering, arrest of psychomotor development, and hypsarrhythmia on EEG. {ECO:0000269|PubMed:11889467, ECO:0000269|PubMed:12376946}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Partington syndrome (PRTS) [MIM:309510]: Characterized by mental retardation, episodic dystonic hand movements, and dysarthria. {ECO:0000269|PubMed:11889467}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mental retardation, X-linked, ARX-related (MRXARX) [MIM:300419]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. {ECO:0000269|PubMed:11971879}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Agenesis of the corpus callosum, with abnormal genitalia (ACCAG) [MIM:300004]: A X-linked syndrome with variable expression in females. It is characterized by agenesis of corpus callosum, mental retardation and seizures. Manifestations in surviving males include severe acquired micrencephaly, mental retardation, limb contractures, scoliosis, tapered fingers with hyperconvex nails, a characteristic face with large eyes, prominent supraorbital ridges, synophrys, optic atrophy, broad alveolar ridges, and seizures. Urologic anomalies include renal dysplasia, cryptorchidism, and hypospadias. {ECO:0000269|PubMed:14722918}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly in fetal and adult brain and skeletal muscle. Expression is specific to the telencephalon and ventral thalamus. There is an absence of expression in the cerebellum throughout development and also in adult. {ECO:0000269|PubMed:11889467, ECO:0000269|PubMed:11971879, ECO:0000269|PubMed:12359145}.; . . 0.82611 0.14662 . . 6.00108 0.22536 AS3MT 5.09137965873753e-07 0.403914503707579 0.596084987154455 arsenite methyltransferase FUNCTION: Catalyzes the transfer of a methyl group from AdoMet to trivalent arsenicals producing methylated and dimethylated arsenicals. It methylates arsenite to form methylarsonate, Me- AsO(3)H(2), which is reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2. Methylarsonite is also a substrate and it is converted into the much less toxic compound dimethylarsinate (cacodylate), Me(2)As(O)-OH (By similarity). {ECO:0000250}.; . . . . 0.09060 0.12625 0.549415813 81.38122199 162.29015 2.78276 ASAH1 5.35814510968979e-11 0.110203595268477 0.889796404677942 N-acylsphingosine amidohydrolase (acid ceramidase) 1 FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid.; DISEASE: Spinal muscular atrophy with progressive myoclonic epilepsy (SMAPME) [MIM:159950]: An autosomal recessive neuromuscular disorder characterized by childhood onset of motor deficits and progressive myoclonic seizures, after normal developmental milestones. Proximal muscle weakness and generalized muscular atrophy are due to degeneration of spinal motor neurons. Myoclonic epilepsy is generally resistant to conventional therapy. The disease course is progressive and leads to respiratory muscle involvement and severe handicap or early death from respiratory insufficiency. {ECO:0000269|PubMed:22703880, ECO:0000269|PubMed:24164096}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Broadly expressed with highest expression in heart.; lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; amygdala;superior cervical ganglion;thyroid;spinal cord;kidney;whole blood; 0.16517 0.28903 0.514416907 80.31375324 457.27798 4.44122 ASAH2 0.015900691207307 0.882662215767239 0.101437093025454 N-acylsphingosine amidohydrolase (non-lysosomal ceramidase) 2 FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 6.5-8.5. Acts as a key regulator of sphingolipid signaling metabolites by generating sphingosine at the cell surface. Acts as a repressor of apoptosis both by reducing C16-ceramide, thereby preventing ceramide-induced apoptosis, and generating sphingosine, a precursor of the antiapoptotic factor sphingosine 1-phosphate. Probably involved in the digestion of dietary sphingolipids in intestine by acting as a key enzyme for the catabolism of dietary sphingolipids and regulating the levels of bioactive sphingolipid metabolites in the intestinal tract. {ECO:0000269|PubMed:15946935, ECO:0000269|PubMed:16061940}.; . TISSUE SPECIFICITY: Primarily expressed in the intestine (PubMed:17334805). Ubiquitously expressed with higher levels in kidney, skeletal muscle and heart (PubMed:10781606). According to PubMed:17334805, ubiquitous expression attributed to ASAH2 may be actually that of the paralog ASAH2B. {ECO:0000269|PubMed:10781606, ECO:0000269|PubMed:17334805}.; unclassifiable (Anatomical System);lung;testis;bladder; . . 0.12895 . . 98.01893 2.14029 ASAH2B 0.154867549921384 0.635622529808473 0.209509920270143 N-acylsphingosine amidohydrolase (non-lysosomal ceramidase) 2B . . TISSUE SPECIFICITY: Ubiquitous. Expression is reduced with increasing age and in late-onset Alzheimer disease (LOAD) patients. This reduction is even more pronounced in patients with an affected mother. {ECO:0000269|PubMed:17334805}.; unclassifiable (Anatomical System);lung;testis;bladder; . 0.21872 0.12895 . . 381.94202 4.11999 ASAP1 0.999983091251179 1.69087488201494e-05 8.55617898028023e-16 ArfGAP with SH3 domain, ankyrin repeat and PH domain 1 FUNCTION: Possesses phosphatidylinositol 4,5-bisphosphate- dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types (By similarity). Plays a role in ciliogenesis. {ECO:0000250, ECO:0000269|PubMed:20393563}.; . . lymphoreticular;ovary;substantia nigra;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;germinal center;brain;heart;cartilage;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.41578 0.17656 -1.240018202 5.461193678 937.06285 5.93485 ASAP1-IT1 . . . ASAP1 intronic transcript 1 . . . . . . . . . . . ASAP1-IT2 . . . ASAP1 intronic transcript 2 . . . . . . . . . . . ASAP2 0.99998604336681 1.39566331877996e-05 2.64976352967083e-15 ArfGAP with SH3 domain, ankyrin repeat and PH domain 2 FUNCTION: Activates the small GTPases ARF1, ARF5 and ARF6. Regulates the formation of post-Golgi vesicles and modulates constitutive secretion. Modulates phagocytosis mediated by Fc gamma receptor and ARF6. Modulates PXN recruitment to focal contacts and cell migration. {ECO:0000269|PubMed:10022920, ECO:0000269|PubMed:10749932, ECO:0000269|PubMed:11304556}.; . TISSUE SPECIFICITY: Detected in heart, brain, placenta, kidney, monocytes and pancreas. {ECO:0000269|PubMed:10022920}.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;iris;testis;spinal ganglion;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;hypothalamus;urinary;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; testis; 0.15521 0.11177 -1.258440978 5.307855626 3851.31014 12.23139 ASAP3 2.35907220968951e-10 0.992406373000852 0.00759362676324047 ArfGAP with SH3 domain, ankyrin repeat and PH domain 3 FUNCTION: Promotes cell proliferation. {ECO:0000269|PubMed:14654939}.; . TISSUE SPECIFICITY: Highly expressed in primary hepatocarcinoma. Detected in lung, liver and blood leukocytes. {ECO:0000269|PubMed:14654939}.; myocardium;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;iris;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;stomach; superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion; 0.22465 . -0.192882212 39.25454117 390.5941 4.16205 ASB1 0.350835778789251 0.636040238537805 0.0131239826729438 ankyrin repeat and SOCS box containing 1 FUNCTION: May play a role in testis development (By similarity). Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250, ECO:0000269|PubMed:16325183}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;larynx;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;pharynx;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland; dorsal root ganglion;medulla oblongata;superior cervical ganglion;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.24079 0.10990 -0.516085732 21.20193442 35.14145 1.06548 ASB2 4.58910505820339e-05 0.961912537573796 0.0380415713756224 ankyrin repeat and SOCS box containing 2 FUNCTION: Substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000269|PubMed:15590664, ECO:0000269|PubMed:16325183}.; FUNCTION: Isoform 2: Involved in myogenic differentiation and targets filamin FLNB for proteasomal degradation but not filamin FLNA. {ECO:0000269|PubMed:19300455}.; . . unclassifiable (Anatomical System);lymphoreticular;lymph node;heart;ovary;islets of Langerhans;muscle;colon;parathyroid;blood;skin;skeletal muscle;bone marrow;uterus;prostate;lung;endometrium;placenta;testis;germinal center;thymus; superior cervical ganglion;skeletal muscle; 0.11015 0.13532 -0.394936437 27.02878037 519.29061 4.65574 ASB3 0.247642059161546 0.751029752425599 0.00132818841285466 ankyrin repeat and SOCS box containing 3 FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes TNFRSF1B. {ECO:0000269|PubMed:15899873}.; . . myocardium;ovary;developmental;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;pineal body;muscle;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; . 0.14210 0.10709 0.154398214 64.73814579 287.72717 3.63236 ASB4 0.0110197125961939 0.947665225582845 0.0413150618209607 ankyrin repeat and SOCS box containing 4 FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes differentiation and maturation of the vascular lineage by an oxygen-dependent mechanism (By similarity). {ECO:0000250}.; . . lung;liver;skeletal muscle;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.68228 0.09762 -0.580403979 18.58928993 176.32112 2.88813 ASB5 1.82587478491106e-11 0.031394366059601 0.96860563392214 ankyrin repeat and SOCS box containing 5 FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. May play a role in the initiation of arteriogenesis (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;prostate;lung;whole body;heart;larynx;hypothalamus;head and neck;skin;skeletal muscle;peripheral nerve; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.35517 0.12633 -0.512444034 21.55579146 103.96794 2.20364 ASB6 0.00464633688363772 0.877108791205548 0.118244871910814 ankyrin repeat and SOCS box containing 6 FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000269|PubMed:16325183}.; . . lymphoreticular;myocardium;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;kidney;mammary gland;stomach;cerebellum;thymus; superior cervical ganglion;cingulate cortex; 0.16444 0.10958 -0.089927255 46.99221515 37.56607 1.11830 ASB7 0.993244100438513 0.00675478027984371 1.11928164328861e-06 ankyrin repeat and SOCS box containing 7 FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250, ECO:0000269|PubMed:16325183}.; . . unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;colon;parathyroid;blood;bone marrow;breast;prostate;lung;bone;placenta;testis;cervix;germinal center;brain;stomach; skeletal muscle; 0.57199 0.11262 -0.339715008 30.06605331 8.86508 0.32687 ASB8 0.0180285302816205 0.8944825444886 0.08748892522978 ankyrin repeat and SOCS box containing 8 FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}.; . TISSUE SPECIFICITY: Highest level of expression in skeletal muscle. Also expressed in heart, brain, placenta, liver, kidney and pancreas. {ECO:0000269|PubMed:12559969}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; superior cervical ganglion;atrioventricular node;skeletal muscle;cingulate cortex; 0.27062 0.12378 -0.293801652 32.93819297 145.93452 2.63241 ASB9 0.887238949040102 0.111542781997103 0.00121826896279557 ankyrin repeat and SOCS box containing 9 FUNCTION: Substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes at least two forms of creatine kinase, CKB and CKMT1A. {ECO:0000269|PubMed:22418839}.; . TISSUE SPECIFICITY: Predominantly expressed in testis, kidney, and liver. {ECO:0000269|PubMed:20302626}.; . . 0.01584 0.07827 -0.119252484 44.53880632 11.20654 0.40465 ASB9P1 . . . ankyrin repeat and SOCS box containing 9 pseudogene 1 . . . . . . . . . . . ASB10 0.000421836172303841 0.644972130742411 0.354606033085286 ankyrin repeat and SOCS box containing 10 FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}.; DISEASE: Glaucoma 1, open angle, F (GLC1F) [MIM:603383]: A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. {ECO:0000269|PubMed:22156576}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the eye. The highest expression is observed in the iris, with moderate levels in the trabecular meshwork (TM), the lamina, and the optic nerve; slightly lower levels in the ciliary body, retina, and choroid; and very low levels in the lens. {ECO:0000269|PubMed:22156576}.; unclassifiable (Anatomical System);skeletal muscle; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13858 0.09699 0.20394914 67.45694739 3056.78765 10.51025 ASB11 0.155409012919734 0.828323057469089 0.0162679296111773 ankyrin repeat and SOCS box containing 11 FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}.; . . skeletal muscle; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;skin; 0.17322 0.10311 0.15257911 64.60839821 179.62192 2.91021 ASB12 1.61933516638744e-05 0.136063785473904 0.863920021174432 ankyrin repeat and SOCS box containing 12 FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250, ECO:0000269|PubMed:16325183}.; . . unclassifiable (Anatomical System);heart;liver;spleen;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;skeletal muscle; 0.18204 0.10591 0.485092724 79.37603208 108.07202 2.25707 ASB13 0.25715636307997 0.715532006444693 0.0273116304753364 ankyrin repeat and SOCS box containing 13 FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;pharynx;blood;lens;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; liver; 0.23953 0.11999 -0.179930907 40.35739561 138.44434 2.56215 ASB14 6.07961312910373e-10 0.0180793514589624 0.981920647933076 ankyrin repeat and SOCS box containing 14 FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}.; . . . . 0.22215 . -0.734731259 14.01863647 131.61722 2.49695 ASB15 6.00806210432932e-08 0.655082047130476 0.344917892788903 ankyrin repeat and SOCS box containing 15 FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}.; . . . . 0.11815 0.10383 0.488730112 79.52347252 373.26182 4.07606 ASB16 2.42234553349084e-10 0.0734331683765891 0.926566831381176 ankyrin repeat and SOCS box containing 16 FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;frontal lobe;ovary;larynx;placenta;muscle;liver;parathyroid;head and neck;brain;bladder; . 0.22798 0.10536 1.580015895 95.77140835 5016.34156 14.46226 ASB16-AS1 . . . ASB16 antisense RNA 1 . . . . . 0.17492 . . . . . ASB17 0.00615869575211394 0.737895776878706 0.25594552736918 ankyrin repeat and SOCS box containing 17 FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}.; . . medulla oblongata;lung;testis; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;skeletal muscle; 0.19852 0.07743 0.148941568 64.31941496 2908.65649 10.23215 ASB18 0.00457337421001374 0.677134471212527 0.318292154577459 ankyrin repeat and SOCS box containing 18 FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}.; . . . . . . . . 5477.12129 15.27148 ASCC1 1.30497571091109e-05 0.835698671519612 0.164288278723279 activating signal cointegrator 1 complex subunit 1 FUNCTION: Enhances NF-kappa-B, SRF and AP1 transactivation. In cells responding to gastrin-activated paracrine signals, it is involved in the induction of SERPINB2 expression by gastrin. {ECO:0000269|PubMed:19074642}.; . TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;colon;vein;bone marrow;uterus;prostate;larynx;bone;thyroid;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach;thymus; tongue;placenta;trigeminal ganglion;parietal lobe; 0.06665 0.07613 0.795569043 87.49115357 1216.45119 6.59982 ASCC2 0.178384955691887 0.821593111858079 2.19324500333046e-05 activating signal cointegrator 1 complex subunit 2 FUNCTION: Enhances NF-kappa-B, SRF and AP1 transactivation.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;muscle;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; testis - interstitial;testis; 0.15025 0.12233 0.582377763 82.32484076 3384.58648 11.14365 ASCC3 1.42788116112326e-10 0.999999999782276 7.4935911109297e-11 activating signal cointegrator 1 complex subunit 3 FUNCTION: 3'-5' DNA helicase involved in repair of alkylated DNA. Promotes DNA unwinding to generate single-stranded substrate needed for ALKHB3, enabling ALKHB3 to process alkylated N3- methylcytosine (3mC) within double-stranded regions. Enhances NF- kappa-B, SRF and AP1 transactivation. {ECO:0000269|PubMed:22055184}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;amnion;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; trigeminal ganglion; 0.37580 0.11285 0.130330208 63.21066289 5476.08217 15.25656 ASCL1 0.364739460004734 0.585189060000184 0.0500714799950825 achaete-scute family bHLH transcription factor 1 FUNCTION: Transcription factor that controls transcriptional expression of its target genes by binding to the E box (5'-CANNTG- 3'). Plays a role at early stages of development of specific neural lineages in most regions of the CNS, and of several lineages in the PNS. Acts synergistically with FOXN4 to specify the identity of V2b neurons rather than V2a from bipotential p2 progenitors during spinal cord neurogenesis, probably through DLL4-NOTCH signaling activation. Essential for the generation of olfactory and autonomic neurons (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;ovary;placenta;visual apparatus;testis;parathyroid;head and neck;kidney;brain;retina;thymus; amygdala;whole brain;superior cervical ganglion;pons;skeletal muscle;fetal brain;prefrontal cortex;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;thymus; 0.85612 0.47584 . . 52.30709 1.42969 ASCL2 0.388900409868869 0.475193001534811 0.13590658859632 achaete-scute family bHLH transcription factor 2 FUNCTION: AS-C proteins are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system.; . TISSUE SPECIFICITY: Expressed specifically in the extravillous trophoblasts of the developing placenta.; unclassifiable (Anatomical System);tongue;islets of Langerhans;placenta;colon;blood;stomach; atrioventricular node; 0.37501 0.09970 . . 21.92423 0.73735 ASCL3 0.00828397093918885 0.56339889323975 0.428317135821061 achaete-scute family bHLH transcription factor 3 FUNCTION: Transcriptional repressor. Inhibits myogenesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues. {ECO:0000269|PubMed:15475265}.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.60175 0.09912 0.593509966 82.51356452 76.54252 1.83606 ASCL4 0.24741188917303 0.642729670385837 0.109858440441133 achaete-scute family bHLH transcription factor 4 FUNCTION: Could be a transcriptional regulator involved in skin development. {ECO:0000269|PubMed:15475265}.; . TISSUE SPECIFICITY: Expressed in skin. 7-fold higher expression in fetal skin than in adult skin. Weak expression also detected in fetal lung, aorta and brain, and in adult stomach, kidney, ovary and breast. {ECO:0000269|PubMed:15475265}.; uterus;heart;skin; globus pallidus;ciliary ganglion;trigeminal ganglion; 0.08002 0.08792 . . 189.79328 2.98948 ASCL5 . . . achaete-scute family bHLH transcription factor 5 . . . . . . . . . 1558.34243 7.31179 ASD1 . . . atrial septal defect 1 . . . . . . . . . . . ASF1A 0.138785136666823 0.779616719072665 0.0815981442605116 anti-silencing function 1A histone chaperone FUNCTION: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit. {ECO:0000269|PubMed:10759893, ECO:0000269|PubMed:11897662, ECO:0000269|PubMed:12842904, ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15664198, ECO:0000269|PubMed:16151251}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12842904}.; unclassifiable (Anatomical System);cartilage;heart;colon;blood;cerebrum;lens;skin;breast;uterus;optic nerve;lung;cochlea;bone;placenta;visual apparatus;liver;testis;spleen;cervix;germinal center;kidney;brain; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.99427 0.12971 0.035072054 56.2514744 1.1279 0.03075 ASF1B 0.565696011085809 0.422261192090084 0.0120427968241074 anti-silencing function 1B histone chaperone FUNCTION: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly. Does not participate in replication-independent nucleosome deposition which is mediated by ASF1A and HIRA. Required for spermatogenesis. {ECO:0000269|PubMed:11897662, ECO:0000269|PubMed:12842904, ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:15664198, ECO:0000269|PubMed:16151251}.; . TISSUE SPECIFICITY: Highly expressed in testis and at lower levels in colon, small intestine and thymus. {ECO:0000269|PubMed:12842904}.; lymphoreticular;ovary;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;muscle;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.90878 0.12386 -0.427900189 25.14744043 14.36535 0.51875 ASGR1 0.000452323588660795 0.866353396396734 0.133194280014605 asialoglycoprotein receptor 1 FUNCTION: Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface.; . TISSUE SPECIFICITY: Expressed exclusively in hepatic parenchymal cells.; unclassifiable (Anatomical System);optic nerve;lung;whole body;liver;testis;colon;spleen;brain;skeletal muscle;cerebellum; fetal liver;liver; 0.16007 0.38484 -0.271755481 34.31823543 14.55779 0.52476 ASGR2 6.63907703485809e-06 0.470712566545029 0.529280794377936 asialoglycoprotein receptor 2 FUNCTION: Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface.; . TISSUE SPECIFICITY: Expressed exclusively in hepatic parenchymal cells.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;parathyroid;blood;skin;skeletal muscle;breast;prostate;lung;placenta;visual apparatus;liver;spleen;kidney;brain;bladder; fetal liver;liver;fetal lung; 0.18473 . -0.358119787 29.16371786 1320.56637 6.83441 ASH1L 0.999999999999834 1.66217650870229e-13 1.32262956600663e-34 ash1 (absent, small, or homeotic)-like (Drosophila) FUNCTION: Histone methyltransferase specifically methylating 'Lys- 36' of histone H3 (H3K36me). {ECO:0000269|PubMed:21239497}.; . TISSUE SPECIFICITY: Widely expressed, with highest level in brain, heart and kidney. {ECO:0000269|PubMed:10860993}.; . . 0.35554 . -1.798985783 2.223401746 588.79734 4.92053 ASH1L-AS1 . . . ASH1L antisense RNA 1 . . . . . . . . . . . ASH1L-IT1 . . . ASH1L intronic transcript 1 . . . . . . . . . . . ASH2L 0.995792115553242 0.00420787003083704 1.44159213661441e-08 ash2 (absent, small, or homeotic)-like (Drosophila) FUNCTION: Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis. {ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:19556245}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Predominantly expressed in adult heart and testis and fetal lung and liver, with barely detectable expression in adult lung, liver, kidney, prostate, and peripheral leukocytes. {ECO:0000269|PubMed:10393421}.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;germinal center;bladder;brain;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;synovium;bone;testis;unclassifiable (Anatomical System);pancreas;lung;mesenchyma;placenta;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.14146 0.11705 -0.26993514 34.59542345 107.32611 2.24775 ASH2LP1 . . . ash2 (absent, small, or homeotic)-like (Drosophila) pseudogene 1 . . . . . . . . . . . ASIC1 0.988325492354336 0.0116743326523946 1.74993269353537e-07 acid sensing ion channel subunit 1 FUNCTION: Isoform 2 and isoform 3 function as proton-gated sodium channels; they are activated by a drop of the extracellular pH and then become rapidly desensitized. The channel generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Isoform 2 can also transport potassium, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. Isoform 3 can also transport calcium ions. Mediates glutamate-independent Ca(2+) entry into neurons upon acidosis. This Ca(2+) overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties. Functions as a postsynaptic proton receptor that influences intracellular Ca(2+) concentration and calmodulin-dependent protein kinase II phosphorylation and thereby the density of dendritic spines. Modulates activity in the circuits underlying innate fear. {ECO:0000269|PubMed:22760635}.; . TISSUE SPECIFICITY: Expressed in most or all neurons.; . . 0.23718 0.17458 -0.492218069 22.35786742 49.92327 1.38608 ASIC2 0.989195648597493 0.0108036362706578 7.15131849005308e-07 acid sensing ion channel subunit 2 FUNCTION: Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Also permeable for Li(+) and K(+). Generates a biphasic current with a fast inactivating and a slow sustained phase. Heteromeric channel assembly seems to modulate.; . TISSUE SPECIFICITY: Brain and spinal cord. Isoform 1 is also detected in testis, liver, colon and ovary. {ECO:0000269|PubMed:10842183, ECO:0000269|PubMed:8631835}.; . . 0.10649 0.14442 -0.490397599 22.50530786 1677.07222 7.55271 ASIC3 7.95974781199542e-07 0.907663088025025 0.0923361160001936 acid sensing ion channel subunit 3 FUNCTION: Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Generates a biphasic current with a fast inactivating and a slow sustained phase. In sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damaged or inflamed tissue. May be involved in hyperalgesia. May play a role in mechanoreception. Heteromeric channel assembly seems to modulate channel properties. {ECO:0000269|PubMed:9744806, ECO:0000269|PubMed:9886053}.; . TISSUE SPECIFICITY: Expressed by sensory neurons. Strongly expressed in brain, spinal chord, lung, lymph nodes, kidney, pituitary, heart and testis. {ECO:0000269|PubMed:9571199, ECO:0000269|PubMed:9886053}.; . . 0.03659 . 0.248041348 69.61547535 180.70058 2.92150 ASIC4 0.72851478269818 0.271368416929188 0.000116800372631155 acid sensing ion channel subunit family member 4 FUNCTION: Probable cation channel with high affinity for sodium. In vitro, has no proton-gated channel activity. {ECO:0000269|PubMed:10852210}.; . TISSUE SPECIFICITY: Expressed in pituitary gland. Weakly expressed in brain, vestibular system and organ of Corti. {ECO:0000269|PubMed:10852210}.; . . 0.35620 0.10783 0.402364592 76.45081387 1068.91123 6.26682 ASIC5 2.25727206903282e-07 0.462011951346624 0.537987822926169 acid sensing ion channel subunit family member 5 FUNCTION: Cation channel that gives rise to very low constitutive currents in the absence of activation. The activated channel exhibits selectivity for sodium, and is inhibited by amiloride. {ECO:0000269|PubMed:10767424}.; . TISSUE SPECIFICITY: Detected in small intestine, duodenum and jejunum. Detected at very low levels in testis and rectum. {ECO:0000269|PubMed:10767424}.; . . 0.10814 0.09151 -0.50880549 21.72682236 95.96988 2.11637 ASIP 0.0696266962093715 0.738100345299579 0.19227295849105 agouti signaling protein FUNCTION: Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment). In higher primates, agouti may affect the quality of hair pigmentation rather than its pattern of deposition. Could well play a role in neuroendocrine aspects of melanocortin action. May have some functional role in regulating the lipid metabolism with adipocytes.; . TISSUE SPECIFICITY: Expressed in adipose tissue, testis, ovary and heart and at lower levels in liver, kidney and foreskin.; . . 0.46657 . . . 24.15406 0.79323 ASL 3.8494991468686e-08 0.790795731135669 0.209204230369339 argininosuccinate lyase . DISEASE: Argininosuccinic aciduria (ARGINSA) [MIM:207900]: An autosomal recessive disorder of the urea cycle. The disease is characterized by mental and physical retardation, liver enlargement, skin lesions, dry and brittle hair showing trichorrhexis nodosa microscopically and fluorescing red, convulsions, and episodic unconsciousness. {ECO:0000269|PubMed:12408190, ECO:0000269|PubMed:1705937, ECO:0000269|PubMed:17326097, ECO:0000269|PubMed:2263616, ECO:0000269|PubMed:24166829}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;colon;skin;retina;bone marrow;prostate;frontal lobe;bone;iris;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;liver;spleen;cervix;kidney;stomach; liver;kidney; 0.08654 0.45435 -0.975433863 8.852323661 25.64812 0.83555 ASLP1 . . . argininosuccinate lyase pseudogene 1 . . . . . . . . . . . ASMT 2.57526101207604e-13 0.00496180734783768 0.995038192651905 acetylserotonin O-methyltransferase FUNCTION: Isoform 1 catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5- methoxytryptamine). Isoform 2 and isoform 3 lack enzyme activity. {ECO:0000269|PubMed:22775292}.; . TISSUE SPECIFICITY: Expressed in the pineal gland (at protein level). In the retina, very low expression is found at the mRNA level (PubMed:7989373), and not at the protein level (PubMed:8574683). {ECO:0000269|PubMed:22775292, ECO:0000269|PubMed:7989373, ECO:0000269|PubMed:8574683}.; . . 0.09450 . 0.134171522 63.57041755 1809.77389 7.84955 ASMTL 1.21964663235068e-05 0.949937330237553 0.0500504732961231 acetylserotonin O-methyltransferase-like FUNCTION: Unknown. The presence of the putative catalytic domain of S-adenosyl-L-methionine binding argues for a methyltransferase activity.; . TISSUE SPECIFICITY: Widely expressed. In adult, highly expressed in pancreas, placenta, fibroblast, thymus, prostate, testis, ovary and colon. Expressed at lower levels in spleen, small intestine and leukocytes. In fetus, expressed at high levels in the lung and kidney and at lower level in brain and liver.; . . 0.09069 . 2.168034562 98.03609342 2516.07403 9.34725 ASMTL-AS1 . . . ASMTL antisense RNA 1 . . . . . . . . . . . ASNA1 0.415776038206036 0.576141688714816 0.00808227307914754 arsA arsenite transporter, ATP-binding, homolog 1 (bacterial) FUNCTION: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail- anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting (By similarity). May be involved in insulin signaling. {ECO:0000255|HAMAP-Rule:MF_03112, ECO:0000269|PubMed:17382883, ECO:0000269|PubMed:18477612}.; . TISSUE SPECIFICITY: Expressed in the epithelial cells of the liver, kidney, and stomach wall, in the adrenal medulla, in the islet cells of the pancreas, in the red pulp of the spleen, and in cardiac and skeletal muscle. {ECO:0000269|PubMed:9774623}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; testis;globus pallidus;kidney;parietal lobe;cerebellum; 0.39047 0.17821 -0.538132194 20.26421326 12.62454 0.46034 ASNS 0.00166592807757199 0.99256022963263 0.00577384228979827 asparagine synthetase (glutamine-hydrolyzing) . DISEASE: Asparagine synthetase deficiency (ASNSD) [MIM:615574]: An inborn error of asparagine biosynthesis that results in a severe neurologic disorder characterized by microcephaly, severely delayed psychomotor development, progressive encephalopathy, cortical atrophy, and seizure or hyperekplexic activity. {ECO:0000269|PubMed:24139043}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;alveolus;liver;cervix;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;cerebellum; tumor; 0.47881 0.25994 -0.025608647 51.91672564 104.79104 2.21250 ASNSD1 1.63756463401646e-08 0.220777798413009 0.779222185211345 asparagine synthetase domain containing 1 . . . myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;bone;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; medulla oblongata;superior cervical ganglion;globus pallidus;trigeminal ganglion;skeletal muscle; 0.05116 0.08996 0.222355725 68.44184949 96.67201 2.12433 ASNSP1 . . . asparagine synthetase pseudogene 1 . . . . . . . . . . . ASNSP2 . . . asparagine synthetase pseudogene 2 . . . . . . . . . . . ASNSP3 . . . asparagine synthetase pseudogene 3 . . . . . . . . . . . ASNSP4 . . . asparagine synthetase pseudogene 4 . . . . . . . . . . . ASNSP5 . . . asparagine synthetase pseudogene 5 . . . . . . . . . . . ASNSP6 . . . asparagine synthetase (glutamine-hydrolyzing) pseudogene 6 . . . . . . . . . . . ASPA 0.0148801566444315 0.875683095035755 0.109436748319813 aspartoacylase FUNCTION: Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it act as a scavenger of NAA from body fluids.; . TISSUE SPECIFICITY: Brain white matter, skeletal muscle, kidney, adrenal glands, lung and liver.; unclassifiable (Anatomical System);lung;endometrium;adrenal gland;liver;testis;spleen;kidney;brain;mammary gland;skin;skeletal muscle; dorsal root ganglion;amygdala;occipital lobe;medulla oblongata;thalamus;olfactory bulb;hypothalamus;spinal cord;caudate nucleus;prefrontal cortex;ciliary ganglion;kidney;parietal lobe; 0.41320 . -0.115612493 45.12856806 63.51257 1.63281 ASPDH 0.00111133387539319 0.613226481131422 0.385662184993185 aspartate dehydrogenase domain containing FUNCTION: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. {ECO:0000250}.; . . . . . . 0.681699246 84.93158764 315.7131 3.77405 ASPG 1.18217261186296e-06 0.576666352266981 0.423332465560407 asparaginase FUNCTION: Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities.; . . ovary;colon;choroid;fovea centralis;lens;retina;optic nerve;lung;epididymis;macula lutea;liver;testis;kidney; . . 0.11691 0.560331224 81.70559094 4760.58672 13.97008 ASPH 1.01766195600599e-08 0.995846117919517 0.00415387190386389 aspartate beta-hydroxylase FUNCTION: Isoform 1: specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins. {ECO:0000269|PubMed:11773073}.; . TISSUE SPECIFICITY: Isoform 1 is detected in all tissues tested. Isoform 8 is mainly expressed in pancreas, heart, brain, kidney and liver. Isoform 8 is expressed in kidney (at protein level). {ECO:0000269|PubMed:11007777}.; unclassifiable (Anatomical System);heart;liver; amygdala;dorsal root ganglion;whole brain;superior cervical ganglion;adipose tissue;cerebellum peduncles;pons;atrioventricular node;skeletal muscle;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;cerebellum; 0.09780 0.18131 -1.236390924 5.520169851 189.544 2.98859 ASPHD1 0.120035612549071 0.854534742598418 0.0254296448525103 aspartate beta-hydroxylase domain containing 1 . . . unclassifiable (Anatomical System);uterus;pancreas;cartilage;islets of Langerhans;bone;visual apparatus;colon;kidney;brain;mammary gland;stomach; amygdala;whole brain;superior cervical ganglion;spinal cord;prefrontal cortex;globus pallidus;pons;skeletal muscle; 0.12683 . -0.359940251 28.93371078 2140.1327 8.51203 ASPHD2 0.526013415728331 0.470466704668254 0.00351987960341494 aspartate beta-hydroxylase domain containing 2 FUNCTION: May function as 2-oxoglutarate-dependent dioxygenase. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;pineal body;colon;lung;placenta;visual apparatus;hippocampus;liver;testis;spleen;germinal center;kidney;brain;stomach;cerebellum; . 0.16318 0.10673 -0.424258538 25.56027365 203.6924 3.08014 ASPM 6.16438991946625e-26 0.99999984137136 1.58628639604561e-07 abnormal spindle microtubule assembly FUNCTION: Probable role in mitotic spindle regulation and coordination of mitotic processes. May have a preferential role in regulating neurogenesis. {ECO:0000269|PubMed:12355089, ECO:0000269|PubMed:15972725}.; DISEASE: Microcephaly 5, primary, autosomal recessive (MCPH5) [MIM:608716]: A disease defined as a head circumference more than 3 standard deviations below the age-related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. Despite this marked reduction in size, the gyral pattern is relatively well preserved, with no major abnormality in cortical architecture. Affected individuals are mentally retarded. Primary microcephaly is further defined by the absence of other syndromic features or significant neurological deficits due to degenerative brain disorder. {ECO:0000269|PubMed:12355089, ECO:0000269|PubMed:14574646, ECO:0000269|PubMed:16673149, ECO:0000269|PubMed:22989186}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;cartilage;heart;colon;skin;skeletal muscle;uterus;prostate;whole body;lung;endometrium;bone;placenta;visual apparatus;duodenum;liver;testis;germinal center;kidney;brain;thymus; testis - interstitial;superior cervical ganglion;fetal liver;testis - seminiferous tubule;tumor;atrioventricular node; 0.34412 0.08672 1.76062236 96.74451522 4776.21455 14.00345 ASPN 0.0233215368712169 0.962070788382964 0.014607674745819 asporin FUNCTION: Negatively regulates periodontal ligament (PDL) differentiation and mineralization to ensure that the PDL is not ossified and to maintain homeostasis of the tooth-supporting system. Inhibits BMP2-induced cytodifferentiation of PDL cells by preventing its binding to BMPR1B/BMP type-1B receptor, resulting in inhibition of BMP-dependent activation of SMAD proteins (By similarity). Critical regulator of TGF-beta in articular cartilage and plays an essential role in cartilage homeostasis and osteoarthritis (OA) pathogenesis. Negatively regulates chondrogenesis in the articular cartilage by blocking the TGF- beta/receptor interaction on the cell surface and inhibiting the canonical TGF-beta/Smad signal. Binds calcium and plays a role in osteoblast-driven collagen biomineralization activity. {ECO:0000250, ECO:0000269|PubMed:17827158, ECO:0000269|PubMed:19589127}.; DISEASE: Osteoarthritis 3 (OS3) [MIM:607850]: A degenerative disease of the joints characterized by degradation of the hyaline articular cartilage and remodeling of the subchondral bone with sclerosis. Clinical symptoms include pain and joint stiffness often leading to significant disability and joint replacement. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Susceptibility to osteoarthritis is conferred by a triplet repeat expansion polymorphism. ASPN allele having 14 aspartic acid repeats in the N-terminal region of the protein (D14), is overrepresented relative to the common allele having 13 aspartic acid repeats (D13). The frequency of the D14 allele increases with disease severity. The D14 allele is also overrepresented in individuals with hip osteoarthritis.; DISEASE: Intervertebral disc disease (IDD) [MIM:603932]: A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain. {ECO:0000269|PubMed:18304494}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Susceptibility to intervertebral disk disease, particularly lumbar disk degeneration, is conferred by a triplet repeat expansion polymorphism. ASPN allele having 14 aspartic acid repeats in the N-terminal region of the protein (D14), is associated with the disorder in some populations (PubMed:18304494). {ECO:0000269|PubMed:18304494}.; TISSUE SPECIFICITY: Higher levels in osteoarthritic articular cartilage, aorta, uterus. Moderate expression in small intestine, heart, liver, bladder, ovary, stomach, and in the adrenal, thyroid, and mammary glands. Low expression in trachea, bone marrow, and lung. Colocalizes with TGFB1 in chondrocytes within osteoarthritic (OA) lesions of articular cartilage. {ECO:0000269|PubMed:17827158}.; . . 0.77853 0.16399 . . 52.00083 1.42413 ASPRV1 0.0918052632340838 0.766483598002296 0.14171113876362 aspartic peptidase, retroviral-like 1 . . TISSUE SPECIFICITY: Expressed primarily in the granular layer of the epidermis and inner root sheath of hair follicles. In psoriatic skin, expressed throughout the stratum corneum. In ulcerated skin, expressed in the stratum granulosum of intact epidermis but almost absent from ulcerated regions. Expressed in differentiated areas of squamous cell carcinomas but not in undifferentiated tumors. {ECO:0000269|PubMed:16098038, ECO:0000269|PubMed:16565508}.; unclassifiable (Anatomical System);optic nerve;heart;endometrium;macula lutea;fovea centralis;choroid;lens;brain;skin;retina; . 0.18328 0.10518 -0.246069119 36.06982779 29.64182 0.94651 ASPSCR1 6.0743019973141e-08 0.864844452523817 0.135155486733164 alveolar soft part sarcoma chromosome region, candidate 1 FUNCTION: Tethering protein that sequesters GLUT4-containing vesicles in the cytoplasm in the absence of insulin. Modulates the amount of GLUT4 that is available at the cell surface (By similarity). Enhances VCP methylation catalyzed by VCPKMT. {ECO:0000250, ECO:0000269|PubMed:23349634}.; DISEASE: Note=A chromosomal aberration involving ASPSCR1 has been found in two patients with of papillary renal cell carcinoma. Translocation t(X;17)(p11.2;q25). {ECO:0000269|PubMed:11358836}.; TISSUE SPECIFICITY: Ubiquitous. Highly expressed in testis, heart, skeletal muscle and pancreas. {ECO:0000269|PubMed:11244503, ECO:0000269|PubMed:11358836}.; colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);hypothalamus;lens;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;stomach;thymus; . . 0.43917 -0.685180376 15.32200991 2902.61447 10.21112 ASRGL1 0.000386788119196688 0.626060265304743 0.373552946576061 asparaginase like 1 FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L- Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. {ECO:0000269|PubMed:19839645}.; . TISSUE SPECIFICITY: Expressed in brain, kidney, testis and tissues of the gastrointestinal tract. Present in sperm (at protein level). Over-expressed in uterine, mammary, prostatic and ovarian carcinoma. {ECO:0000269|PubMed:11984834, ECO:0000269|PubMed:14654938}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;testis;dura mater;brain;bladder;tonsil;unclassifiable (Anatomical System);meninges;hypothalamus;pharynx;blood;lens;skeletal muscle;pia mater;lung;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.09435 0.27804 -0.314027422 31.9297004 41.01491 1.20213 ASS1 0.000493337976371257 0.992797603934801 0.00670905808882754 argininosuccinate synthase 1 FUNCTION: Is indirectly involved in the control of blood pressure. {ECO:0000250}.; DISEASE: Citrullinemia 1 (CTLN1) [MIM:215700]: The classic form of citrullinemia, an autosomal recessive disease characterized primarily by elevated serum and urine citrulline levels. Ammonia intoxication is another manifestation. It is a disorder of the urea cycle, usually manifesting in the first few days of life. Affected infants appear normal at birth, but as ammonia builds up in the body they present symptoms such as lethargy, poor feeding, vomiting, seizures and loss of consciousness. Less commonly, a milder form can develop later in childhood or adulthood. {ECO:0000269|PubMed:11708871, ECO:0000269|PubMed:11941481, ECO:0000269|PubMed:12815590, ECO:0000269|PubMed:14680976, ECO:0000269|PubMed:16475226, ECO:0000269|PubMed:1943692, ECO:0000269|PubMed:2358466, ECO:0000269|PubMed:25179242, ECO:0000269|PubMed:7977368}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;parathyroid;uterus;whole body;frontal lobe;cerebral cortex;endometrium;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;adrenal cortex;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;alveolus;spleen;cervix;kidney;stomach; fetal liver;adipose tissue;liver;fetal lung;kidney; 0.48724 0.80840 -0.510624372 21.65015334 146.81822 2.63893 ASS1P1 . . . argininosuccinate synthetase 1 pseudogene 1 . . . . . . . . . . . ASS1P2 . . . argininosuccinate synthetase 1 pseudogene 2 . . . . . . . . . . . ASS1P3 . . . argininosuccinate synthetase 1 pseudogene 3 . . . . . . . . . . . ASS1P4 . . . argininosuccinate synthetase 1 pseudogene 4 . . . . . . . . . . . ASS1P5 . . . argininosuccinate synthetase 1 pseudogene 5 . . . . . . . . . . . ASS1P6 . . . argininosuccinate synthetase 1 pseudogene 6 . . . . . . . . . . . ASS1P7 . . . argininosuccinate synthetase 1 pseudogene 7 . . . . . . . . . . . ASS1P8 . . . argininosuccinate synthetase 1 pseudogene 8 . . . . . . . . . . . ASS1P9 . . . argininosuccinate synthetase 1 pseudogene 9 . . . . . . . . . . . ASS1P10 . . . argininosuccinate synthetase 1 pseudogene 10 . . . . . . . . . . . ASS1P11 . . . argininosuccinate synthetase 1 pseudogene 11 . . . . . . . . . . . ASS1P12 . . . argininosuccinate synthetase 1 pseudogene 12 . . . . . . . . . . . ASS1P13 . . . argininosuccinate synthetase 1 pseudogene 13 . . . . . . . . . . . ASS1P14 . . . argininosuccinate synthetase 1 pseudogene 14 . . . . . . . . . . . ASTE1 3.39138941425054e-12 0.0225114431316303 0.977488556864978 asteroid homolog 1 (Drosophila) FUNCTION: Possible role in EGF receptor signaling. {ECO:0000250}.; . . ovary;fovea centralis;skin;bone marrow;uterus;prostate;whole body;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; parietal lobe;skeletal muscle; 0.13505 0.08341 7.61E-05 53.98089172 60.16998 1.57498 ASTL 3.67008336651582e-05 0.822828432995594 0.177134866170741 astacin-like metallo-endopeptidase (M12 family) FUNCTION: Oocyte-specific oolemmal receptor involved in sperm and egg adhesion and fertilization. Plays a role in the polyspermy inhibition. Probably acts as a protease for the post-fertilization cleavage of ZP2. Cleaves the sperm-binding ZP2 at the surface of the zona pellucida after fertilization and cortical granule exocytosis, rendering the zona pellucida unable to support further sperm binding (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in promyelocytic leukemia HL-60 cells, Burkitt's lymphoma Raji cells, and also in some ovarian carcinomas. Not detected in normal tissues. {ECO:0000269|PubMed:15087446}.; uterus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.08019 0.09622 0.711016566 85.72776598 2406.21675 9.10932 ASTN1 0.999415997291979 0.000584002707053689 9.67762336583381e-13 astrotactin 1 FUNCTION: Neuronal adhesion molecule that is required for glial- guided migration of young postmitotic neuroblasts in cortical regions of developing brain, including cerebrum, hippocampus, cerebellum and olfactory bulb.; . . unclassifiable (Anatomical System);heart;ovary;hypothalamus;sympathetic chain;adrenal cortex;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;optic nerve;whole body;lung;frontal lobe;bone;macula lutea;visual apparatus;hippocampus;testis;brain; amygdala;dorsal root ganglion;whole brain;medulla oblongata;superior cervical ganglion;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.12514 0.11666 -1.095046929 6.97688134 570.07336 4.84399 ASTN2 0.989172283780343 0.0108277159757561 2.43900457628111e-10 astrotactin 2 . . . ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;frontal lobe;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;hypothalamus;pineal body;muscle;lens;lung;adrenal gland;placenta;visual apparatus;macula lutea;head and neck;spleen;kidney; dorsal root ganglion;superior cervical ganglion;thalamus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;cerebellum; 0.28632 0.11008 -2.271160931 1.256192498 1146.31095 6.45411 ASTN2-AS1 . . . ASTN2 antisense RNA 1 . . . . . . . . . . . ASUN 0.998587603501794 0.00141239629480888 2.03397280952374e-10 asunder, spermatogenesis regulator FUNCTION: Crucial regulator of the mitotic cell cycle and development. At prophase, required for dynein anchoring to the nuclear envelope important for proper centrosome-nucleus coupling. At G2/M phase, may be required for proper spindle formation and execution of cytokinesis. {ECO:0000269|PubMed:15737938, ECO:0000269|PubMed:23097494}.; . TISSUE SPECIFICITY: Widely expressed. Tends to be up-regulated in seminomas compared to normal testis. {ECO:0000269|PubMed:12414650}.; ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;thyroid;iris;amniotic fluid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; . 0.64237 0.09081 -0.203796826 38.81811748 115.83879 2.34153 ASXL1 1.37370457058834e-18 0.0705391207985284 0.929460879201472 additional sex combs like 1, transcriptional regulator FUNCTION: Probable Polycomb group (PcG) protein involved in transcriptional regulation mediated by ligand-bound nuclear hormone receptors, such as retinoic acid receptors (RARs) and peroxisome proliferator-activated receptor gamma (PPARG). Acts as coactivator of RARA and RXRA through association with NCOA1. Acts as corepressor through recruitment of KDM1A and CBX5 to target genes in a cell-type specific manner; the function seems to involve differential recruitment of methylated histone H3 to respective promoters. Acts as corepressor for PPARG and suppresses its adipocyte differentiation-inducing activity (By similarity). Non-catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). {ECO:0000250, ECO:0000269|PubMed:16606617, ECO:0000269|PubMed:20436459}.; DISEASE: Bohring-Opitz syndrome (BOPS) [MIM:605039]: A syndrome characterized by severe intrauterine growth retardation, poor feeding, profound mental retardation, trigonocephaly, prominent metopic suture, exophthalmos, nevus flammeus of the face, upslanting palpebral fissures, hirsutism, and flexion of the elbows and wrists with deviation of the wrists and metacarpophalangeal joints. {ECO:0000269|PubMed:21706002}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myelodysplastic syndrome (MDS) [MIM:614286]: A heterogeneous group of closely related clonal hematopoietic disorders. All are characterized by a hypercellular or hypocellular bone marrow with impaired morphology and maturation, dysplasia of the myeloid, megakaryocytic and/or erythroid lineages, and peripheral blood cytopenias resulting from ineffective blood cell production. Included diseases are: refractory anemia (RA), refractory anemia with ringed sideroblasts (RARS), refractory anemia with excess blasts (RAEB), refractory cytopenia with multilineage dysplasia and ringed sideroblasts (RCMD-RS); chronic myelomonocytic leukemia (CMML) is a myelodysplastic/myeloproliferative disease. MDS is considered a premalignant condition in a subgroup of patients that often progresses to acute myeloid leukemia (AML). {ECO:0000269|PubMed:19388938, ECO:0000269|PubMed:20182461}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed at low level. Expressed in heart, brain, skeletal muscle, placenta, pancreas, spleen, prostate, small intestine, colon, peripheral blood, leukocytes, bone marrow and fetal liver. Highly expressed in testes. {ECO:0000269|PubMed:10231032, ECO:0000269|PubMed:12657473}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;placenta;duodenum;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.14735 0.07872 0.17442557 65.77022883 833.4544 5.65494 ASXL2 0.992738818422806 0.00726117933797246 2.23922153478909e-09 additional sex combs like 2, transcriptional regulator FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via methylation of histones, rendering chromatin heritably changed in its expressibility (By similarity). Involved in transcriptional regulation mediated by ligand-bound nuclear hormone receptors, such as peroxisome proliferator-activated receptor gamma (PPARG). Acts as coactivator for PPARG and enhances its adipocyte differentiation-inducing activity; the function seems to involve differential recruitment of acetylated and methylated histone H3. {ECO:0000250, ECO:0000269|PubMed:21047783}.; DISEASE: Note=A chromosomal aberration involving ASXL2 is a cause of therapy-related myelodysplastic syndrome. Translocation t(2;8)(p23;p11.2) with KAT6A generates a KAT6A-ASXL2 fusion protein.; . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;artery;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;whole blood; 0.33803 0.07709 . . 425.16 4.30807 ASXL3 0.999977048473461 2.29515265299539e-05 8.90075938214378e-15 additional sex combs like 3, transcriptional regulator FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via methylation of histones, rendering chromatin heritably changed in its expressibility (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in pancreatic islets, testis, neuroblastoma, head and neck tumor. {ECO:0000269|PubMed:15138607}.; unclassifiable (Anatomical System);prostate;pancreas;lung;islets of Langerhans;testis;cervix; occipital lobe;temporal lobe;skeletal muscle;cingulate cortex; 0.10816 . -0.66524926 15.87048832 636.60276 5.07564 ASZ1 1.71628994930091e-06 0.865247890690712 0.134750393019338 ankyrin repeat, SAM and basic leucine zipper domain containing 1 FUNCTION: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Its association with pi- bodies suggests a participation in the primary piRNAs metabolic process. Required prior to the pachytene stage to facilitate the production of multiple types of piRNAs, including those associated with repeats involved in the regulation of retrotransposons. May act by mediating protein-protein interactions during germ cell maturation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed exclusively in the testis and ovary and at higher levels in the adult testis compared with the adult ovary. {ECO:0000269|PubMed:12040005}.; testis; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.11526 0.16997 -0.336073593 30.55555556 1496.44973 7.19732 ATAD1 0.5363543151617 0.462979631808977 0.000666053029322485 ATPase family, AAA domain containing 1 FUNCTION: ATPase that plays a critical role in regulating the surface expression of AMPA receptors (AMPAR), thereby regulating synaptic plasticity and learning and memory. Required for NMDA- stimulated AMPAR internalization and inhibition of GRIA1 and GRIA2 recycling back to the plasma membrane; these activities are ATPase-dependent (By similarity). {ECO:0000250}.; . . . . 0.35103 0.12971 -0.207437529 38.2814343 11.15326 0.40319 ATAD2 0.999997953114707 2.04688529321833e-06 2.04528753927849e-19 ATPase family, AAA domain containing 2 FUNCTION: May be a transcriptional coactivator of the nuclear receptor ESR1 required to induce the expression of a subset of estradiol target genes, such as CCND1, MYC and E2F1. May play a role in the recruitment or occupancy of CREBBP at some ESR1 target gene promoters. May be required for histone hyperacetylation. Involved in the estrogen-induced cell proliferation and cell cycle progression of breast cancer cells. {ECO:0000269|PubMed:17998543}.; . TISSUE SPECIFICITY: Highly expressed in estrogen receptor positive breast tumors and in osteosarcoma tumors. {ECO:0000269|PubMed:15721472, ECO:0000269|PubMed:17076897, ECO:0000269|PubMed:17660802}.; lymphoreticular;ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;bile duct;lung;cornea;visual apparatus;liver;amnion;spleen;cervix;kidney;mammary gland;stomach; fetal liver;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;tumor;atrioventricular node;trigeminal ganglion; 0.42398 0.12895 -0.925889687 9.754659118 150.87158 2.68443 ATAD2B 0.999998682086859 1.31791314101407e-06 4.17485913002385e-17 ATPase family, AAA domain containing 2B . . . unclassifiable (Anatomical System);heart;ovary;cerebellum cortex;developmental;colon;skin;skeletal muscle;retina;uterus;prostate;lung;cochlea;endometrium;bone;placenta;visual apparatus;pituitary gland;testis;head and neck;germinal center;kidney;brain;mammary gland;bladder; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.90276 . 0.246221394 69.56829441 267.59066 3.50808 ATAD3A 0.0401305978810457 0.959596762816073 0.000272639302880951 ATPase family, AAA domain containing 3A FUNCTION: Essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organism and cellular level. May play an important in mitochondrial protein synthesis. May also participate in mitochondrial DNA replication. May bind to mitochondrial DNA D-loops and contribute to nucleoid stability. Required for enhanced channeling of cholesterol for hormone- dependent steroidogenesis. {ECO:0000269|PubMed:17210950, ECO:0000269|PubMed:20154147, ECO:0000269|PubMed:22453275}.; . TISSUE SPECIFICITY: Overexpressed in lung adenocarcinomas (at protein level). {ECO:0000269|PubMed:20332122}.; tongue;head and neck;germinal center;mammary gland; superior cervical ganglion;skeletal muscle; 0.30120 0.10317 0.119404819 62.20806794 1511.84536 7.22185 ATAD3B 1.92301228016303e-13 0.056353553568157 0.943646446431651 ATPase family, AAA domain containing 3B FUNCTION: May play a role in a mitochondrial network organization typical for stem cells, characterized by reduced mitochondrial metabolism, low mtDNA copies and fragmentated mitochondrial network. may act by suppressing ATAD3A function, interfering with ATAD3A interaction with matrix nucleoid complexes. {ECO:0000269|PubMed:22664726}.; . TISSUE SPECIFICITY: Tends to be down-regulated in differentiated cells and re-expressed in pluripotent stem cells or cancer cells (at protein level). {ECO:0000269|PubMed:16909202, ECO:0000269|PubMed:22664726}.; myocardium;colon;skin;uterus;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;muscle;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; . 0.08529 0.12376 2.166192036 98.0301958 6153.92777 16.40046 ATAD3C 4.90849565539176e-05 0.867306383831225 0.132644531212221 ATPase family, AAA domain containing 3C . . . . . 0.16989 . 2.888598189 99.14484548 3860.31144 12.24254 ATAD5 0.999999945408971 5.45910290504845e-08 8.83831697078779e-20 ATPase family, AAA domain containing 5 FUNCTION: Involved in DNA damage response. Involved in a RAD9A- related damage checkpoint, a pathway that is important in determining whether DNA damage is compatible with cell survival or whether it requires cell elimination by apoptosis. Modulates the RAD9A interaction with BCL2 and thereby induces DNA damages- induced apoptosis. {ECO:0000269|PubMed:15983387}.; . . unclassifiable (Anatomical System);islets of Langerhans;colon;bile duct;uterus;breast;prostate;lung;thyroid;placenta;visual apparatus;liver;testis;spleen;germinal center;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.36789 . -0.053328617 48.95022411 8284.30154 19.69105 ATAT1 0.0143739247782645 0.985369063458761 0.00025701176297399 alpha tubulin acetyltransferase 1 FUNCTION: Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Required for normal sperm flagellar function. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Promotes directional cell locomotion and chemotaxis, through AP2A2-dependent acetylation of alpha-tubulin at clathrin-coated pits that are concentrated at the leading edge of migrating cells. May facilitate primary cilium assembly. {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:20829795, ECO:0000269|PubMed:21068373, ECO:0000269|PubMed:24097348}.; . . ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;cerebral cortex;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;adrenal cortex;blood;lens;breast;pancreas;lung;adrenal gland;placenta;hippocampus;macula lutea;liver;hypopharynx;spleen;head and neck;kidney;mammary gland; . 0.07758 . -0.159704656 41.90846898 151.29878 2.68979 ATCAY 0.0874733261874534 0.903249537547732 0.00927713626481414 ataxia, cerebellar, Cayman type FUNCTION: Functions in the development of neural tissues, particularly the postnatal maturation of the cerebellar cortex. May play a role in neurotransmission through regulation of glutaminase/GLS, an enzyme responsible for the production in neurons of the glutamate neurotransmitter. Alternatively, may regulate the localization of mitochondria within axons and dendrites. {ECO:0000269|PubMed:16899818}.; DISEASE: Cerebellar ataxia, cayman type (ATCAY) [MIM:601238]: Found in a population isolate on Grand Cayman Island and causes a marked psychomotor retardation and prominent nonprogressive cerebellar dysfunction including nystagmus, intention tremor, dysarthria, and wide-based ataxic gait. Hypotonia is present from early childhood. {ECO:0000269|PubMed:14556008}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);frontal lobe;colon;brain;mammary gland;skeletal muscle; dorsal root ganglion;whole brain;superior cervical ganglion;globus pallidus;pons;parietal lobe;skeletal muscle;cerebellum; 0.19898 . -0.53631094 20.53550366 21.24378 0.71845 ATD . . . asphixiating thoracic dystrophy (chondroectodermal dysplasia-like syndrome) . . . . . . . . . . . ATE1 0.511356720482748 0.488609978882895 3.3300634357322e-05 arginyltransferase 1 FUNCTION: Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;heart;ovary;islets of Langerhans;spinal cord;colon;parathyroid;blood;skin;retina;uterus;whole body;lung;placenta;visual apparatus;testis;germinal center;kidney;brain;stomach; ciliary ganglion; 0.36448 0.11687 -0.490397599 22.50530786 49.8139 1.38425 ATE1-AS1 . . . ATE1 antisense RNA 1 . . . . . . . . . . . ATF1 0.663831053655397 0.335066428504027 0.00110251784057587 activating transcription factor 1 FUNCTION: This protein binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Binds to the Tax-responsive element (TRE) of HTLV-I. Mediates PKA-induced stimulation of CRE-reporter genes. Represses the expression of FTH1 and other antioxidant detoxification genes. Triggers cell proliferation and transformation. {ECO:0000269|PubMed:18794154, ECO:0000269|PubMed:20980392}.; DISEASE: Angiomatoid fibrous histiocytoma (AFH) [MIM:612160]: A distinct variant of malignant fibrous histiocytoma that typically occurs in children and adolescents and is manifest by nodular subcutaneous growth. Characteristic microscopic features include lobulated sheets of histiocyte-like cells intimately associated with areas of hemorrhage and cystic pseudovascular spaces, as well as a striking cuffing of inflammatory cells, mimicking a lymph node metastasis. Note=The gene represented in this entry may be involved in disease pathogenesis. Chromosomal aberrations involving ATF1 are found in patients with angiomatoid fibrous histiocytoma. Translocation t(12;16)(q13;p11.2) with FUS generates a chimeric ATF1/FUS protein. Translocation t(12;22)(q13;q12) with EWSR1 generates a chimeric ATF1/EWSR1 protein.; . ovary;colon;choroid;skin;bone marrow;uterus;prostate;larynx;synovium;thyroid;bone;testis;dura mater;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);meninges;small intestine;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;pia mater;lung;mesenchyma;placenta;liver;spleen;head and neck;stomach; thyroid;white blood cells; 0.89892 0.18118 0.25917371 70.05779665 91.37091 2.05535 ATF1P1 . . . activating transcription factor 1 pseudogene 1 . . . . . . . . . . . ATF2 0.89224439257863 0.107746405523594 9.20189777533612e-06 activating transcription factor 2 FUNCTION: Transcriptional activator which regulates the transcription of various genes, including those involved in anti- apoptosis, cell growth, and DNA damage response. Dependent on its binding partner, binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1) consensus sequences (5'-TGACTCA-3'). In the nucleus, contributes to global transcription and the DNA damage response, in addition to specific transcriptional activities that are related to cell development, proliferation and death. In the cytoplasm, interacts with and perturbs HK1- and VDAC1-containing complexes at the mitochondrial outer membrane, thereby impairing mitochondrial membrane potential, inducing mitochondrial leakage and promoting cell death. The phosphorylated form (mediated by ATM) plays a role in the DNA damage response and is involved in the ionizing radiation (IR)-induced S phase checkpoint control and in the recruitment of the MRN complex into the IR-induced foci (IRIF). Exhibits histone acetyltransferase (HAT) activity which specifically acetylates histones H2B and H4 in vitro. In concert with CUL3 and RBX1, promotes the degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. Can elicit oncogenic or tumor suppressor activities depending on the tissue or cell type. {ECO:0000269|PubMed:10821277, ECO:0000269|PubMed:15916964, ECO:0000269|PubMed:18397884, ECO:0000269|PubMed:22304920}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with more abundant expression in the brain.; smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;bladder;brain;amygdala;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;amnion;liver;alveolus;cervix;spleen;kidney;stomach; amygdala;medulla oblongata;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.88198 0.28104 -0.714505427 14.4019816 21.91257 0.73683 ATF3 0.276113481429884 0.700471687111428 0.0234148314586878 activating transcription factor 3 FUNCTION: This protein binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Represses transcription from promoters with ATF sites. It may repress transcription by stabilizing the binding of inhibitory cofactors at the promoter. Isoform 2 activates transcription presumably by sequestering inhibitory cofactors away from the promoters.; . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; superior cervical ganglion;placenta; 0.44816 0.56655 0.103030231 61.2762444 32.34224 1.01105 ATF4 0.411468430246377 0.55200105514654 0.0365305146070834 activating transcription factor 4 FUNCTION: Transcriptional activator. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Cooperates with FOXO1 in osteoblasts to regulate glucose homeostasis through suppression of beta-cell production and decrease in insulin production (By similarity). It binds to a Tax-responsive enhancer element in the long terminal repeat of HTLV-I. Regulates the induction of DDIT3/CHOP and asparagine synthetase (ASNS) in response to endoplasmic reticulum (ER) stress. In concert with DDIT3/CHOP, activates the transcription of TRIB3 and promotes ER stress-induced neuronal apoptosis by regulating the transcriptional induction of BBC3/PUMA. Activates transcription of SIRT4. Regulates the circadian expression of the core clock component PER2 and the serotonin transporter SLC6A4. Binds in a circadian time-dependent manner to the cAMP response elements (CRE) in the SLC6A4 and PER2 promoters and periodically activates the transcription of these genes. During ER stress response, activates the transcription of NLRP1, possibly in concert with other factors (PubMed:26086088). {ECO:0000250, ECO:0000269|PubMed:15775988, ECO:0000269|PubMed:16682973, ECO:0000269|PubMed:18940792, ECO:0000269|PubMed:26086088}.; . . lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;tonsil;heart;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; . 0.12249 0.56830 1.021500656 91.01792876 2596.58697 9.54065 ATF4P1 . . . activating transcription factor 4 pseudogene 1 . . . . . . . . . . . ATF4P2 . . . activating transcription factor 4 pseudogene 2 . . . . . . . . . . . ATF4P3 . . . activating transcription factor 4 pseudogene 3 . . . . . . . . . . . ATF4P4 . . . activating transcription factor 4 pseudogene 4 . . . . . . . . . . . ATF5 0.0226677802943902 0.764814323775801 0.212517895929808 activating transcription factor 5 FUNCTION: Transcription factor that either stimulates or represses gene transcription through binding of different DNA regulatory elements such as cAMP response element (CRE) (consensus: 5'- GTGACGT[AC][AG]-3'), ATF5-specific response element (ARE) (consensus: 5'-C[CT]TCT[CT]CCTT[AT]-3') but also the amino acid response element (AARE), present in many viral and cellular promoters. Critically involved, often in a cell type-dependent manner, in cell survival, proliferation, and differentiation (PubMed:10373550, PubMed:15358120, PubMed:21212266, PubMed:20654631). Its transcriptional activity is enhanced by CCND3 and slightly inhibited by CDK4 (PubMed:15358120). Important regulator of the cerebral cortex formation, functions in cerebral cortical neuroprogenitor cells to maintain proliferation and to block differentiation into neurons. Must be down-regulated in order for such cells to exit the cycle and differentiate (By similarity). Participates in the pathways by which SHH promotes cerebellar granule neuron progenitor cells proliferation (By similarity). Critical for survival of mature olfactory sensory neurons (OSN), directs expression of OSN-specific genes (By similarity). May be involved in osteogenic differentiation (PubMed:22442021). Promotes cell proliferation and survival by inducing the expression of EGR1 sinergistically with ELK1. Once acetylated by EP300, binds to ARE sequences on target genes promoters, such as BCL2 and EGR1 (PubMed:21791614). Plays an anti- apoptotic role through the transcriptional regulation of BCL2, this function seems to be cell type-dependent (By similarity). Cooperates with NR1I3/CAR in the transcritpional activation of CYP2B6 in liver (PubMed:18332083). In hepatic cells, represses CRE-dependent transcription and inhibits proliferation by blocking at G2/M phase (PubMed:22528486, PubMed:18701499). May act as a negative regulator of IL1B transduction pathway in liver (PubMed:24379400). Upon IL1B stimulus, cooperates with NLK to activate the transactivation activity of C/EBP subfamily members (PubMed:25512613). Besides its function of transcription factor, acts as a cofactor of CEBPB to activate CEBPA and promote adipocyte differentiation (PubMed:24216764). Regulates centrosome dynamics in a cell-cycle- and centriole-age-dependent manner. Forms 9-foci symmetrical ring scaffold around the mother centriole to control centrosome function and the interaction between centrioles and pericentriolar material (PubMed:26213385). {ECO:0000250|UniProtKB:O70191, ECO:0000250|UniProtKB:Q6P788, ECO:0000269|PubMed:10373550, ECO:0000269|PubMed:15358120, ECO:0000269|PubMed:18332083, ECO:0000269|PubMed:18701499, ECO:0000269|PubMed:20654631, ECO:0000269|PubMed:21212266, ECO:0000269|PubMed:21791614, ECO:0000269|PubMed:22442021, ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:24216764, ECO:0000269|PubMed:24379400, ECO:0000269|PubMed:25512613, ECO:0000269|PubMed:26213385}.; . TISSUE SPECIFICITY: Widely expressed with higher expression levels in liver. {ECO:0000269|PubMed:18332083}.; . . 0.54803 0.13429 0.062575634 58.74026893 167.4423 2.82682 ATF6 3.10664680607037e-05 0.996993053420145 0.00297588011179448 activating transcription factor 6 FUNCTION: Transcription factor that acts during endoplasmic reticulum stress by activating unfolded protein response target genes. Binds DNA on the 5'-CCAC[GA]-3'half of the ER stress response element (ERSE) (5'-CCAAT-N(9)-CCAC[GA]-3') and of ERSE II (5'-ATTGG-N-CCACG-3'). Binding to ERSE requires binding of NF-Y to ERSE. Could also be involved in activation of transcription by the serum response factor. {ECO:0000269|PubMed:11158310, ECO:0000269|PubMed:11779464}.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.24087 0.27985 0.42259095 77.22929936 3604.57589 11.62279 ATF6B 1.6770144203098e-06 0.992040228611914 0.00795809437366602 activating transcription factor 6 beta FUNCTION: Transcriptional factor that acts in the unfolded protein response (UPR) pathway by activating UPR target genes induced during ER stress. Binds DNA on the 5'-CCAC[GA]-3' half of the ER stress response element (ERSE) (5'-CCAATN(9)CCAC[GA]-3') when NF-Y is bound to ERSE.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.21760 . 0.134171522 63.57041755 91.39595 2.05570 ATF7 0.983314715299326 0.0166832061116709 2.07858900302932e-06 activating transcription factor 7 FUNCTION: Plays important functions in early cell signaling. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]- 3'), a sequence present in many viral and cellular promoters. Activator of the NF-ELAM1/delta-A site of the E-selectin promoter. Has no intrinsic transcriptional activity, but activates transcription on formation of JUN or FOS heterodimers. Also can bind TRE promoter sequences when heterodimerized with members of the JUN family.; FUNCTION: Isoform 5/ATF-4 acts as a negative regulator, inhibiting both ATF2 and ATF7 transcriptional activities. It may exert these effects by sequestrating in the cytoplasm the Thr-53 phosphorylating kinase, preventing activation.; . TISSUE SPECIFICITY: Expressed in heart, lung and skeletal muscle. Isoform 4 is expressed in various tissues including heart, brain, placenta, lung and skeletal muscle. Highest levels in skeletal muscle. Lowest in lung and placenta. {ECO:0000269|PubMed:8288576}.; unclassifiable (Anatomical System);medulla oblongata;lymph node;cartilage;ovary;heart;hypothalamus;salivary gland;colon;skin;bone marrow;uterus;bile duct;prostate;lung;frontal lobe;nasopharynx;bone;placenta;liver;cervix;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.26951 0.11887 -0.648365105 16.35999056 3.94452 0.14610 ATF7IP 0.99974103814101 0.00025896185573054 3.25911408179635e-12 activating transcription factor 7 interacting protein FUNCTION: Recruiter that couples transcriptional factors to general transcription apparatus and thereby modulates transcription regulation and chromatin formation. Can both act as an activator or a repressor depending on the context. Mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1. Required to stimulate histone methyltransferase activity of SETDB1 and facilitate the conversion of dimethylated to trimethylated H3 'Lys-9' (H3K9me3). The complex formed with MBD1 and SETDB1 represses transcription and couples DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3). Facilitates telomerase TERT and TERC gene expression by SP1 in cancer cells. {ECO:0000269|PubMed:12665582, ECO:0000269|PubMed:14536086, ECO:0000269|PubMed:19106100}.; . TISSUE SPECIFICITY: Detected at low levels in breast, lung and stomach; highly up-regulated in the corresponding cancerous tissues (at protein level). {ECO:0000269|PubMed:19106100}.; myocardium;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.67749 0.10619 0.473967469 78.86293937 7630.06967 18.76351 ATF7IP2 0.797518042342298 0.202431725826885 5.02318308170841e-05 activating transcription factor 7 interacting protein 2 FUNCTION: Recruiter that couples transcriptional factors to general transcription apparatus and thereby modulates transcription regulation and chromatin formation. Can both act as an activator or a repressor depending on the context. Mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1. The complex formed with MBD1 and SETDB1 represses transcription and probably couples DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3) activity (Probable). {ECO:0000305}.; . . unclassifiable (Anatomical System);islets of Langerhans;colon;fovea centralis;pancreas;prostate;nasopharynx;macula lutea;liver;testis;spleen;germinal center;bladder;mammary gland;brain; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node; 0.06581 0.08435 0.069852974 59.10592121 914.09649 5.87775 ATG2A 0.999922729645369 7.72703546312521e-05 5.8088440446127e-17 autophagy related 2A FUNCTION: Required for both autophagosome formation and regulation of lipid droplet morphology and dispersion. {ECO:0000269|PubMed:22219374}.; . . lymphoreticular;ovary;colon;skin;bone marrow;uterus;prostate;optic nerve;endometrium;bone;iris;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lung;placenta;visual apparatus;liver;cervix;kidney;stomach;cerebellum; superior cervical ganglion;adrenal cortex;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.19577 0.11121 -1.055017884 7.584335928 2428.34078 9.15295 ATG2B 8.12742750734489e-05 0.999918725707387 1.75399996560164e-11 autophagy related 2B FUNCTION: Required for both autophagosome formation and regulation of lipid droplet morphology and dispersion. {ECO:0000269|PubMed:22219374}.; . . ovary;colon;fovea centralis;skin;retina;bone marrow;uterus;frontal lobe;endometrium;cerebral cortex;bone;testis;germinal center;brain;unclassifiable (Anatomical System);small intestine;heart;cartilage;islets of Langerhans;blood;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;kidney;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.31648 . 0.486743222 79.3819297 1250.48072 6.67455 ATG3 0.978991920554431 0.0210044135972181 3.66584835088741e-06 autophagy related 3 FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12- ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway. {ECO:0000269|PubMed:11825910, ECO:0000269|PubMed:12207896, ECO:0000269|PubMed:12890687, ECO:0000269|PubMed:16704426, ECO:0000269|PubMed:20723759}.; . TISSUE SPECIFICITY: Widely expressed, with a highest expression in heart, skeletal muscle, kidney, liver and placenta. {ECO:0000269|PubMed:11825910}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;breast;trabecular meshwork;macula lutea;visual apparatus;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;thymus; amygdala;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;whole blood;skeletal muscle; 0.34371 0.11934 0.03689118 56.64071715 38.41144 1.13990 ATG3P1 . . . autophagy related 3 pseudogene 1 . . . . . . . . . . . ATG4A 0.988883246902227 0.0111129655765926 3.78752118020642e-06 autophagy related 4A cysteine peptidase FUNCTION: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Preferred substrate is GABARAPL2 followed by MAP1LC3A and GABARAP. Has also an activity of delipidating enzyme for the PE-conjugated forms. {ECO:0000269|PubMed:12473658, ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:17347651, ECO:0000269|PubMed:21177865, ECO:0000269|PubMed:21245471, ECO:0000269|PubMed:22302004}.; . TISSUE SPECIFICITY: Widely expressed, at a low level, and the highest expression is observed in skeletal muscle and brain. Also detected in fetal liver. {ECO:0000269|PubMed:12446702, ECO:0000269|PubMed:15169837}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;lung;placenta;macula lutea;liver;alveolus;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.23305 0.09809 0.03689118 56.64071715 95.77853 2.11492 ATG4AP1 . . . autophagy related 4A cysteine peptidase pseudogene 1 . . . . . . . . . . . ATG4B 0.988495912592781 0.0114999682152645 4.11919195482458e-06 autophagy related 4B cysteine peptidase FUNCTION: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal glycine. Exposure of the glycine at the C- terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms. {ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:17347651, ECO:0000269|PubMed:19322194, ECO:0000269|PubMed:21177865, ECO:0000269|PubMed:22302004}.; . TISSUE SPECIFICITY: Mainly expressed in the skeletal muscle, followed by brain, heart, liver and pancreas. {ECO:0000269|PubMed:12446702, ECO:0000269|PubMed:15169837}.; medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;oesophagus;larynx;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;muscle;adrenal cortex;blood;lens;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;testis - interstitial;prostate;testis - seminiferous tubule;thyroid;prefrontal cortex;testis; . 0.10738 0.284856336 71.40835103 488.90283 4.55127 ATG4C 3.32761781234443e-09 0.305635431407027 0.694364565265355 autophagy related 4C cysteine peptidase FUNCTION: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Is not essential for autophagy development under normal conditions but is required for a proper autophagic response under stressful conditions such as prolonged starvation (By similarity). Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms. {ECO:0000250, ECO:0000269|PubMed:21177865}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart, liver and testis. {ECO:0000269|PubMed:12446702}.; unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;hypothalamus;sympathetic chain;parathyroid;blood;skin;skeletal muscle;bone marrow;uterus;whole body;lung;endometrium;bone;placenta;visual apparatus;liver;testis;germinal center;kidney;brain;stomach;thymus; subthalamic nucleus;medulla oblongata;superior cervical ganglion;occipital lobe;hypothalamus;prefrontal cortex;globus pallidus;caudate nucleus;trigeminal ganglion;parietal lobe; 0.12912 0.09693 -0.003562597 53.72729417 70.35901 1.74451 ATG4D 0.000323903626106917 0.945773922715218 0.0539021736586753 autophagy related 4D cysteine peptidase FUNCTION: Cysteine protease ATG4D: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms.; . TISSUE SPECIFICITY: Mainly expressed in skeletal muscle and, to a lower extent, in testis. {ECO:0000269|PubMed:12446702}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;thymus; . 0.15091 0.10598 -0.578583623 18.71903751 85.56652 1.97238 ATG5 0.981561830973196 0.0184250517025704 1.31173242336038e-05 autophagy related 5 FUNCTION: Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. The ATG12- ATG5 conjugate also negatively regulates the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Also plays a role in translation or delivery of incoming viral RNA to the translation apparatus. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for MHC II. Involved in the maintenance of axon morphology and membrane structures, as well as in normal adipocyte differentiation. Promotes primary ciliogenesis through removal of OFD1 from centriolar satellites and degradation of IFT20 via the autophagic pathway.; . TISSUE SPECIFICITY: Ubiquitous. The mRNA is present at similar levels in viable and apoptotic cells, whereas the protein is dramatically highly expressed in apoptotic cells.; lymphoreticular;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;breast;pancreas;pia mater;lung;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.36057 0.17050 0.103030231 61.2762444 64.05281 1.64090 ATG7 1.52666137074291e-05 0.991834841198253 0.00814989218803985 autophagy related 7 FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin- like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 as well as the ATG8 family proteins for their conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Required for autophagic death induced by caspase-8 inhibition. Required for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Modulates p53/TP53 activity to regulate cell cycle and survival during metabolic stress. Plays also a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration, the maintenance of hematopoietic stem cells, the formation of Paneth cell granules, as well as in adipose differentiation. {ECO:0000269|PubMed:11096062, ECO:0000269|PubMed:16303767, ECO:0000269|PubMed:22170151}.; . TISSUE SPECIFICITY: Widely expressed, especially in kidney, liver, lymph nodes and bone marrow. {ECO:0000269|PubMed:11890701}.; medulla oblongata;ovary;colon;skin;bone marrow;uterus;prostate;optic nerve;endometrium;cerebral cortex;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;heart;skeletal muscle;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;liver;cervix;kidney;stomach; superior cervical ganglion; 0.10213 0.17266 -0.510624372 21.65015334 346.12918 3.94578 ATG9A 0.714827712943686 0.28516674181475 5.54524156416264e-06 autophagy related 9A FUNCTION: Involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Plays a key role in the organization of the preautophagosomal structure/phagophore assembly site (PAS), the nucleating site for formation of the sequestering vesicle. Cycles between a juxta-nuclear trans-Golgi network compartment and late endosomes. Nutrient starvation induces accumulation on autophagosomes. Starvation-dependent trafficking requires ULK1, ATG13 and SUPT20H. {ECO:0000269|PubMed:16940348}.; . . myocardium;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;larynx;bone;iris;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;muscle;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;atrioventricular node; 0.16507 0.10992 -0.352661697 29.48808681 617.21016 5.01462 ATG9B 1.85392629019537e-11 0.113429971947108 0.886570028034352 autophagy related 9B FUNCTION: Involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Plays a key role in the organization of the preautophagosomal structure/phagophore assembly site (PAS), the nucleating site for formation of the sequestering vesicle (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in placenta (trophoblast cells) and pituitary gland. Not expressed in vascular endothelial. {ECO:0000269|PubMed:15234981}.; . . 0.08155 0.14778 . . 2475.8399 9.27524 ATG10 0.00168505422151429 0.891512221294845 0.106802724483641 autophagy related 10 FUNCTION: E2-like enzyme involved in autophagy. Acts as an E2-like enzyme that catalyzes the conjugation of ATG12 to ATG5. ATG12 conjugation to ATG5 is required for autophagy. Likely serves as an ATG5-recognition molecule. Not involved in ATG12 conjugation to ATG3 (By similarity). Plays a role in adenovirus-mediated cell lysis. {ECO:0000250, ECO:0000269|PubMed:21367888}.; . . unclassifiable (Anatomical System);heart;adrenal cortex;parathyroid;skin;uterus;whole body;lung;frontal lobe;nasopharynx;placenta;thyroid;visual apparatus;testis;germinal center;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.06588 0.08777 1.082196027 91.79641425 321.33299 3.80753 ATG10-AS1 . . . ATG10 antisense RNA 1 . . . . . . . . . . . ATG10-IT1 . . . ATG10 intronic transcript 1 . . . . . . . . . . . ATG12 0.00165807110195777 0.699322448359732 0.29901948053831 autophagy related 12 FUNCTION: Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. The ATG12-ATG5 conjugate also regulates negatively the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Plays also a role in translation or delivery of incoming viral RNA to the translation apparatus. {ECO:0000269|PubMed:12207896, ECO:0000269|PubMed:17709747, ECO:0000269|PubMed:17999726, ECO:0000269|PubMed:19074260, ECO:0000269|PubMed:19164948, ECO:0000269|PubMed:19666601, ECO:0000269|PubMed:23202584}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9852036}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;subthalamic nucleus;atrioventricular node;trigeminal ganglion; 0.10345 0.10587 0.147123112 64.11299835 58.06341 1.54097 ATG12P1 . . . autophagy related 12 pseudogene 1 . . . . . . . . . . . ATG12P2 . . . autophagy related 12 pseudogene 2 . . . . . . . . . . . ATG13 0.984296607292859 0.0157030303098784 3.62397262806244e-07 autophagy related 13 FUNCTION: Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1- RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation. {ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:19211835, ECO:0000269|PubMed:19225151, ECO:0000269|PubMed:19287211, ECO:0000269|PubMed:21795849, ECO:0000269|PubMed:21855797}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;mesenchyma;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;occipital lobe;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;pons;atrioventricular node;kidney;trigeminal ganglion;parietal lobe;skeletal muscle; 0.34196 0.10514 -0.622676946 17.30950696 130.93647 2.49222 ATG14 0.326846073593547 0.673015797868631 0.000138128537822281 autophagy related 14 FUNCTION: Required for both basal and inducible autophagy. Determines the localization of the autophagy-specific PI3-kinase complex PI3KC3-C1 (PubMed:18843052, PubMed:19050071). Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine (PubMed:19270696, PubMed:20713597). Promotes BECN1 translocation from the trans-Golgi network to autophagosomes (PubMed:20713597). Enhances PIK3C3 activity in a BECN1-dependent manner. Essential for the autophagy-dependent phosphorylation of BECN1 (PubMed:23878393). Stimulates the phosphorylation of BECN1, but suppresses the phosphorylation PIK3C3 by AMPK (PubMed:23878393). Binds to STX17-SNAP29 binary t- SNARE complex on autophagosomes and primes it for VAMP8 interaction to promote autophagosome-endolysosome fusion (PubMed:25686604). Modulates the hepatic lipid metabolism (By similarity). {ECO:0000250|UniProtKB:Q8CDJ3, ECO:0000269|PubMed:18843052, ECO:0000269|PubMed:19050071, ECO:0000269|PubMed:19270696, ECO:0000269|PubMed:20713597, ECO:0000269|PubMed:23878393, ECO:0000269|PubMed:25686604}.; . . unclassifiable (Anatomical System);ovary;heart;hypothalamus;pineal body;parathyroid;blood;skin;skeletal muscle;breast;uterus;prostate;whole body;atrium;lung;endometrium;nasopharynx;bone;thyroid;placenta;liver;testis;cervix;head and neck;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.29828 . -0.314027422 31.9297004 531.875 4.70532 ATG16L1 0.999737382504978 0.000262617478355571 1.66663093562357e-11 autophagy related 16 like 1 FUNCTION: Plays an essential role in autophagy: interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine (PE) to LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C), to produce a membrane-bound activated form of LC3 named LC3-II. Thereby, controls the elongation of the nascent autophagosomal membrane. {ECO:0000269|PubMed:23376921, ECO:0000269|PubMed:24553140, ECO:0000269|PubMed:24954904}.; DISEASE: Inflammatory bowel disease 10 (IBD10) [MIM:611081]: A chronic, relapsing inflammation of the gastrointestinal tract with a complex etiology. It is subdivided into Crohn disease and ulcerative colitis phenotypes. Crohn disease may affect any part of the gastrointestinal tract from the mouth to the anus, but most frequently it involves the terminal ileum and colon. Bowel inflammation is transmural and discontinuous; it may contain granulomas or be associated with intestinal or perianal fistulas. In contrast, in ulcerative colitis, the inflammation is continuous and limited to rectal and colonic mucosal layers; fistulas and granulomas are not observed. Both diseases include extraintestinal inflammation of the skin, eyes, or joints. {ECO:0000269|PubMed:17200669, ECO:0000269|PubMed:17435756}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;amnion;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.24630 0.10646 0.150760231 64.51403633 2440.04938 9.18597 ATG16L2 8.94242667912362e-09 0.723129666331932 0.276870324725641 autophagy related 16 like 2 FUNCTION: May play a role in autophagy. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;hypothalamus;adrenal cortex;colon;blood;bone marrow;uterus;prostate;pancreas;lung;endometrium;larynx;bone;placenta;visual apparatus;liver;testis;head and neck;spleen;kidney;germinal center;brain;mammary gland;tonsil;stomach;peripheral nerve; white blood cells;trigeminal ganglion;whole blood;bone marrow; 0.08065 . -0.666770504 15.86459071 340.45082 3.91504 ATG101 . . . autophagy related 101 FUNCTION: Autophagy factor required for autophagosome formation. Stabilizes ATG13, protecting it from proteasomal degradation. {ECO:0000269|PubMed:19287211, ECO:0000269|PubMed:19597335}.; . . . . 0.05244 0.11262 -0.427900189 25.14744043 . . ATHL1 3.53241578008574e-09 0.522934748565119 0.477065247902466 ATH1, acid trehalase-like 1 (yeast) . . . . . 0.11348 0.09640 -0.701780438 14.81481481 618.82243 5.01814 ATHS . . . atherosclerosis susceptibility (lipoprotein associated) . . . . . . . . . . . ATIC 2.48609470825841e-13 0.0653081452913855 0.934691854708366 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase FUNCTION: Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis. {ECO:0000269|PubMed:14966129}.; DISEASE: AICAR transformylase/IMP cyclohydrolase deficiency (AICAR) [MIM:608688]: A neurologically devastating inborn error of purine biosynthesis. Patients excrete massive amounts of AICA- riboside in the urine and accumulate AICA-ribotide and its derivatives in erythrocytes and fibroblasts. AICAR causes profound mental retardation, epilepsy, dysmorphic features and congenital blindness. {ECO:0000269|PubMed:15114530}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;cochlea;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;spinal cord;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;amnion;head and neck;kidney;stomach; tumor;parietal lobe; 0.86437 0.69972 0.248041348 69.61547535 3411.60183 11.19306 ATL1 0.99211803597583 0.00788189717785162 6.68463182352203e-08 atlastin GTPase 1 FUNCTION: GTPase tethering membranes through formation of trans- homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. May also regulate Golgi biogenesis. May regulate axonal development. {ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:17321752, ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:21220294, ECO:0000269|PubMed:23334294, ECO:0000269|PubMed:25751282}.; DISEASE: Neuropathy, hereditary sensory, 1D (HSN1D) [MIM:613708]: A disease characterized by adult-onset distal axonal sensory neuropathy leading to mutilating ulcerations as well as hyporeflexia. Some patients may show features suggesting upper neuron involvement. {ECO:0000269|PubMed:21194679}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly in the adult and fetal central nervous system. Measurable expression in all tissues examined, although expression in adult brain is at least 50-fold higher than in other tissues. Detected predominantly in pyramidal neurons in the cerebral cortex and the hippocampus of the brain. Expressed in upper and lower motor neurons (at protein level). {ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:17321752, ECO:0000269|PubMed:18270207}.; ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;thyroid;bone;iris;testis;pineal gland;brain;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;hypothalamus;skeletal muscle;bile duct;breast;lung;placenta;hippocampus;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; whole brain;amygdala;dorsal root ganglion;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.58111 0.15924 -0.582225231 18.44184949 12.62871 0.46059 ATL2 0.980197371048562 0.0198024991571572 1.29794280593012e-07 atlastin GTPase 2 FUNCTION: GTPase tethering membranes through formation of trans- homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. {ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:19665976}.; . TISSUE SPECIFICITY: Expressed in peripheral tissues (at protein level). {ECO:0000269|PubMed:18270207}.; unclassifiable (Anatomical System);retina;uterus;lung;cochlea;placenta;thyroid;hypopharynx;liver;testis;head and neck;brain;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.50505 0.11563 -0.067881249 48.69072895 3458.2471 11.29657 ATL3 0.000317251708826362 0.997096736283295 0.00258601200787897 atlastin GTPase 3 FUNCTION: GTPase tethering membranes through formation of trans- homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. {ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:19665976}.; . TISSUE SPECIFICITY: Expressed in the central nervous system and in dorsal root ganglia neurons. Expressed in peripheral tissues (at protein level). {ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:24459106}.; unclassifiable (Anatomical System);cartilage;ovary;tongue;islets of Langerhans;blood;skeletal muscle;bone marrow;breast;prostate;lung;bone;thyroid;placenta;duodenum;liver;testis;head and neck;cervix;brain;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;trigeminal ganglion;skin; . . -0.137658575 43.57159707 706.5004 5.28046 ATM 2.71064232749178e-30 0.999996031177404 3.96882259622307e-06 ATM serine/threonine kinase FUNCTION: Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism. Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN), TERF1, RAD9 and DCLRE1C. May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Plays a role in replication-dependent histone mRNA degradation. Binds DNA ends. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation. Phosphorylates ATF2 which stimulates its function in DNA damage response. {ECO:0000269|PubMed:10973490, ECO:0000269|PubMed:12556884, ECO:0000269|PubMed:14871926, ECO:0000269|PubMed:15916964, ECO:0000269|PubMed:16086026, ECO:0000269|PubMed:16858402, ECO:0000269|PubMed:17923702, ECO:0000269|PubMed:19965871}.; DISEASE: Ataxia telangiectasia (AT) [MIM:208900]: A rare recessive disorder characterized by progressive cerebellar ataxia, dilation of the blood vessels in the conjunctiva and eyeballs, immunodeficiency, growth retardation and sexual immaturity. Patients have a strong predisposition to cancer; about 30% of patients develop tumors, particularly lymphomas and leukemias. Cells from affected individuals are highly sensitive to damage by ionizing radiation and resistant to inhibition of DNA synthesis following irradiation. {ECO:0000269|PubMed:10234507, ECO:0000269|PubMed:10425038, ECO:0000269|PubMed:10817650, ECO:0000269|PubMed:10873394, ECO:0000269|PubMed:7792600, ECO:0000269|PubMed:8698354, ECO:0000269|PubMed:8755918, ECO:0000269|PubMed:8789452, ECO:0000269|PubMed:8797579, ECO:0000269|PubMed:8808599, ECO:0000269|PubMed:8845835, ECO:0000269|PubMed:9043869, ECO:0000269|PubMed:9150358, ECO:0000269|PubMed:9443866, ECO:0000269|PubMed:9450874, ECO:0000269|PubMed:9463314, ECO:0000269|PubMed:9497252, ECO:0000269|PubMed:9521587, ECO:0000269|PubMed:9711876, ECO:0000269|PubMed:9792409, ECO:0000269|PubMed:9792410, ECO:0000269|PubMed:9872980, ECO:0000269|PubMed:9887333}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in ATM contribute to T-cell acute lymphoblastic leukemia (TALL) and T-prolymphocytic leukemia (TPLL). TPLL is characterized by a high white blood cell count, with a predominance of prolymphocytes, marked splenomegaly, lymphadenopathy, skin lesions and serous effusion. The clinical course is highly aggressive, with poor response to chemotherapy and short survival time. TPLL occurs both in adults as a sporadic disease and in younger AT patients. {ECO:0000269|PubMed:9288106, ECO:0000269|PubMed:9334731, ECO:0000269|PubMed:9463314, ECO:0000269|PubMed:9488043, ECO:0000269|PubMed:9573030}.; DISEASE: Note=Defects in ATM contribute to B-cell non-Hodgkin lymphomas (BNHL), including mantle cell lymphoma (MCL). {ECO:0000269|PubMed:10397742, ECO:0000269|PubMed:10706620, ECO:0000269|PubMed:9288106}.; DISEASE: Note=Defects in ATM contribute to B-cell chronic lymphocytic leukemia (BCLL). BCLL is the commonest form of leukemia in the elderly. It is characterized by the accumulation of mature CD5+ B-lymphocytes, lymphadenopathy, immunodeficiency and bone marrow failure. {ECO:0000269|PubMed:10023947, ECO:0000269|PubMed:10397742, ECO:0000269|PubMed:9892178}.; TISSUE SPECIFICITY: Found in pancreas, kidney, skeletal muscle, liver, lung, placenta, brain, heart, spleen, thymus, testis, ovary, small intestine, colon and leukocytes.; smooth muscle;colon;skin;retina;uterus;prostate;thyroid;iris;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;lymph node;heart;cartilage;lacrimal gland;islets of Langerhans;blood;skeletal muscle;breast;pia mater;lung;adrenal gland;nasopharynx;placenta;visual apparatus;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.17033 0.15782 1.526898538 95.50601557 5697.19625 15.62160 ATMIN 0.000970632527072967 0.944159315853564 0.054870051619363 ATM interactor FUNCTION: Transcription factor. Plays a crucial role in cell survival and RAD51 foci formation in response to methylating DNA damage. Involved in regulating the activity of ATM in the absence of DNA damage. May play a role in stabilizing ATM. Binds to the DYNLL1 promoter and activates its transcription. {ECO:0000269|PubMed:15933716, ECO:0000269|PubMed:17525732, ECO:0000269|PubMed:22167198}.; . TISSUE SPECIFICITY: Ubiquitously expressed in normal tissues and cancer cell lines with highest levels in placenta and skeletal muscle. {ECO:0000269|PubMed:15933716}.; lymphoreticular;medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;cerebellum; amygdala;superior cervical ganglion;occipital lobe;thalamus;testis - interstitial;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.57860 0.10995 -0.883608246 10.50365652 1345.54391 6.88722 ATN1 0.998533107154739 0.0014668917428677 1.10239320811968e-09 atrophin 1 FUNCTION: Transcriptional corepressor. Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation (By similarity). Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of poly-Asn (polyQ) repeats. {ECO:0000250, ECO:0000269|PubMed:10085113, ECO:0000269|PubMed:10973986}.; DISEASE: Dentatorubral-pallidoluysian atrophy (DRPLA) [MIM:125370]: Autosomal dominant neurodegenerative disorder characterized by a loss of neurons in the dentate nucleus, rubrum, glogus pallidus and Luys'body. Clinical features are myoclonus epilepsy, dementia, and cerebellar ataxia. Onset of the disease occurs usually in the second decade of life and death in the fourth. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed in various tissues including heart, lung, kidney, ovary, testis, prostate, placenta, skeletal Low levels in the liver, thymus and leukocytes. In the adult brain, broadly expressed in amygdala, caudate nucleus, corpus callosum, hippocampus, hypothalamus, substantia nigra, subthalamic nucleus, and thalamus. High levels in fetal tissues, especially brain. {ECO:0000269|PubMed:7485154, ECO:0000269|PubMed:7842016, ECO:0000269|PubMed:8965642}.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;nervous;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;muscle;pancreas;lung;cornea;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; superior cervical ganglion;prefrontal cortex;atrioventricular node;caudate nucleus;trigeminal ganglion; 0.48946 0.52345 -0.947938165 9.341825902 746.86669 5.42284 ATOH1 0.767526002722777 0.224253354608401 0.00822064266882192 atonal bHLH transcription factor 1 FUNCTION: Transcriptional regulator. Activates E box-dependent transcription in collaboration with TCF3/E47, but the activity is completely antagonized by the negative regulator of neurogenesis HES1. Plays a role in the differentiation of subsets of neural cells by activating E box-dependent transcription (By similarity). {ECO:0000250}.; . . . . 0.76824 0.28312 -0.113792788 45.25831564 241.72664 3.35733 ATOH7 0.0430200322640268 0.662243022890188 0.294736944845785 atonal bHLH transcription factor 7 FUNCTION: Transcription factor involved in the differentiation of retinal ganglion cells. {ECO:0000250}.; DISEASE: Persistent hyperplastic primary vitreous, autosomal recessive (PHPVAR) [MIM:221900]: A developmental eye malformation associated with microphthalmia, cataract, glaucoma, and congenital retinal non-attachment. It is due to failure of the primary vitreous to regress in utero, resulting in the presence of a retrolental fibrovascular membrane with persistence of the posterior portion of the tunica vasculosa lentis and hyaloid artery. Disease manifestations range from a trivial remnant of hyaloid vessels to a dense fibrovascular mass causing lens opacity and retinal detachment. {ECO:0000269|PubMed:21441919, ECO:0000269|PubMed:22068589, ECO:0000269|PubMed:22645276}. Note=The disease is caused by mutations affecting the gene represented in this entry. A 6.5 kb deletion that spans a remote cis regulatory element 20 kb upstream from ATOH7 has been found in PHPVAR patients (PubMed:21441919). {ECO:0000269|PubMed:21441919}.; . . . 0.71262 . 0.125076652 62.7388535 32.94095 1.02003 ATOH8 0.888203282317987 0.110605104474522 0.00119161320749075 atonal bHLH transcription factor 8 FUNCTION: Transcription factor that binds a palindromic (canonical) core consensus DNA sequence 5'-CANNTG- 3' known as an E-box element, possibly as a heterodimer with other bHLH proteins (PubMed:24236640). Regulates endothelial cell proliferation, migration and tube-like structures formation (PubMed:24463812). Modulates endothelial cell differentiation through NOS3 (PubMed:24463812). May be implicated in specification and differentiation of neuronal cell lineages in the brain (By similarity). May participate in kidney development and may be involved in podocyte differentiation (By similarity). During early embryonic development is involved in tissue-specific differentiation processes that are dependent on class II bHLH factors and namely modulates the differentiation program initiated by the pro-endocrine factor NEUROG3 (By similarity). During myogenesis, may play a role during the transition of myoblasts from the proliferative phase to the differentiation phase (By similarity). Positively regulates HAMP transcription in two ways, firstly by acting directly on the HAMP promoter via E-boxes binding and indirectly through increased phosphorylation of SMAD protein complex (PubMed:24236640). Repress NEUROG3-dependent gene activation in a gene-specific manner through at least two mechanisms; requires only either the sequestering of a general partner such as TCF3 through heterodimerization, either also requires binding of the bHLH domain to DNA via a basic motif (By similarity). {ECO:0000250|UniProtKB:Q99NA2, ECO:0000269|PubMed:24236640, ECO:0000269|PubMed:24463812}.; . TISSUE SPECIFICITY: Expressed in lung, liver, kidney, heart and pancreas. Expressed in endothel of umbilical vessels. {ECO:0000269|PubMed:12419857}.; unclassifiable (Anatomical System);heart;ovary;cartilage;muscle;skin;skeletal muscle;retina;uterus;optic nerve;lung;cerebral cortex;endometrium;thyroid;iris;testis;brain;bladder;stomach; . 0.56852 0.11878 . . 1291.19209 6.76533 ATOX1 0.17740157925531 0.644375611728191 0.178222809016499 antioxidant 1 copper chaperone FUNCTION: Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;ovary;salivary gland;intestine;colon;choroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;synovium;thyroid;pituitary gland;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);trophoblast;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; thalamus;spinal cord;liver; 0.08373 0.09191 0.145304857 63.81221986 7.4258 0.27617 ATP1A1 0.999993850305473 6.14969451805646e-06 8.79107662360649e-15 ATPase Na+/K+ transporting subunit alpha 1 FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.; . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;muscle;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; whole brain;medulla oblongata;subthalamic nucleus;cerebellum peduncles;thyroid;globus pallidus;kidney;pons;fetal thyroid;cingulate cortex;cerebellum; 0.70086 0.33303 -0.999300439 8.368719038 39.64671 1.16887 ATP1A1-AS1 . . . ATP1A1 antisense RNA 1 . . . . . . . . . . . ATP1A2 0.600219587089565 0.399780278463133 1.34447302186979e-07 ATPase Na+/K+ transporting subunit alpha 2 FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport of various nutrients.; DISEASE: Migraine, familial hemiplegic, 2 (FHM2) [MIM:602481]: A subtype of migraine with aura associated with hemiparesis in some families. Migraine is a disabling symptom complex of periodic headaches, usually temporal and unilateral. Headaches are often accompanied by irritability, nausea, vomiting and photophobia, preceded by constriction of the cranial arteries. Migraine with aura is characterized by recurrent attacks of reversible neurological symptoms (aura) that precede or accompany the headache. Aura may include a combination of sensory disturbances, such as blurred vision, hallucinations, vertigo, numbness and difficulty in concentrating and speaking. {ECO:0000269|PubMed:12539047, ECO:0000269|PubMed:12953268, ECO:0000269|PubMed:21352219, ECO:0000269|PubMed:23838748, ECO:0000269|PubMed:23918834}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Alternating hemiplegia of childhood 1 (AHC1) [MIM:104290]: A rare syndrome of episodic hemi- or quadriplegia lasting minutes to days. Most cases are accompanied by dystonic posturing, choreoathetoid movements, nystagmus, other ocular motor abnormalities, autonomic disturbances, and progressive cognitive impairment. It is typically distinguished from familial hemiplegic migraine by infantile onset and high prevalence of associated neurological deficits that become increasingly obvious with age. {ECO:0000269|PubMed:15174025}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;iris;testis;pineal gland;brain;unclassifiable (Anatomical System);amygdala;heart;cerebellum cortex;nervous;hypothalamus;spinal cord;muscle;blood;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;hippocampus;hypopharynx;head and neck;mammary gland;peripheral nerve;cerebellum; whole brain;dorsal root ganglion;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;thalamus;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;atrioventricular node;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.53654 0.22867 -1.374132436 4.429110639 48.50463 1.35867 ATP1A3 0.999994323017881 5.67698208289241e-06 3.57552203778713e-14 ATPase Na+/K+ transporting subunit alpha 3 FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.; DISEASE: Dystonia 12 (DYT12) [MIM:128235]: An autosomal dominant dystonia-parkinsonism disorder. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. DYT12 patients develop dystonia and parkinsonism between 15 and 45 years of age. The disease is characterized by an unusually rapid evolution of signs and symptoms. The sudden onset of symptoms over hours to a few weeks, often associated with physical or emotional stress, suggests a trigger initiating a nervous system insult resulting in permanent neurologic disability. {ECO:0000269|PubMed:15260953, ECO:0000269|PubMed:19351654, ECO:0000269|PubMed:19652145}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Alternating hemiplegia of childhood 2 (AHC2) [MIM:614820]: A rare syndrome of episodic hemi- or quadriplegia lasting minutes to days. Most cases are accompanied by dystonic posturing, choreoathetoid movements, nystagmus, other ocular motor abnormalities, autonomic disturbances, and progressive cognitive impairment. It is typically distinguished from familial hemiplegic migraine by infantile onset and high prevalence of associated neurological deficits that become increasingly obvious with age. {ECO:0000269|PubMed:22842232, ECO:0000269|PubMed:22850527, ECO:0000269|PubMed:23409136}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cerebellar ataxia, areflexia, pes cavus, optic atrophy, and sensorineural hearing loss (CAPOS) [MIM:601338]: An autosomal dominant neurologic disorder characterized by relapsing and partially remitting, early-onset cerebellar ataxia following a febrile illness. Other features include progressive optic atrophy and sensorineural hearing loss, generalized hypotonia, areflexia and pes cavus without evidence of a peripheral neuropathy on neurophysiological studies. {ECO:0000269|PubMed:24468074}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);amygdala;lymph node;heart;hypothalamus;muscle;colon;fovea centralis;choroid;lens;skeletal muscle;retina;breast;optic nerve;frontal lobe;macula lutea;visual apparatus;hippocampus;testis;germinal center;brain;cerebellum; whole brain;amygdala;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.93219 0.18422 -1.530301957 3.367539514 13.31894 0.48410 ATP1A4 1.89733270588042e-11 0.988515007438887 0.0114849925421394 ATPase Na+/K+ transporting subunit alpha 4 FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. Plays a role in sperm motility.; . TISSUE SPECIFICITY: Specifically expressed in testis. Found in very low levels in skeletal muscle. Expressed in mature sperm (at protein level).; . . 0.11816 0.11048 0.547404288 81.13352206 617.99318 5.01673 ATP1B1 0.995564605006206 0.00443499466746811 4.00326325478918e-07 ATPase Na+/K+ transporting subunit beta 1 FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane. {ECO:0000269|PubMed:19694409}.; . TISSUE SPECIFICITY: Found in most tissues.; . . 0.38527 0.24812 -0.449946534 24.00330267 4.44425 0.16128 ATP1B1P1 . . . ATPase Na+/K+ transporting subunit beta 1 pseudogene 1 . . . . . . . . . . . ATP1B2 0.179758869110773 0.81765325290113 0.00258787798809735 ATPase Na+/K+ transporting subunit beta 2 FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-2 subunit is not known.; . . ovary;fovea centralis;choroid;retina;bone marrow;optic nerve;frontal lobe;larynx;bone;iris;pineal gland;brain;unclassifiable (Anatomical System);amygdala;nervous;hypothalamus;spinal cord;blood;lens;skeletal muscle;lung;macula lutea;hippocampus;visual apparatus;liver;spleen;head and neck;kidney;cerebellum; amygdala;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.25555 0.12094 -0.337894035 30.37272942 86.54469 1.98674 ATP1B3 0.641391596618863 0.357254280451702 0.00135412292943512 ATPase Na+/K+ transporting subunit beta 3 FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known.; . . smooth muscle;ovary;sympathetic chain;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;uterus;whole body;larynx;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus; . 0.38429 0.11956 -0.207437529 38.2814343 2.63913 0.09632 ATP1B3-AS1 . . . ATP1B3 antisense RNA 1 . . . . . . . . . . . ATP1B3P1 . . . ATPase Na+/K+ transporting subunit beta 3 pseudogene 1 . . . . . . . . . . . ATP1B4 0.00278062464065032 0.938288111043578 0.0589312643157714 ATPase Na+/K+ transporting family member beta 4 FUNCTION: May act as a transcriptional coregulator during muscle development through its interaction with SNW1. Has lost its ancestral function as a Na,K-ATPase beta-subunit. {ECO:0000269|PubMed:17592128}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle and at a lower level in heart. {ECO:0000269|PubMed:10456317}.; unclassifiable (Anatomical System);uterus;prostate;whole body;heart;skin;skeletal muscle;retina; superior cervical ganglion;globus pallidus;appendix;trigeminal ganglion;skeletal muscle; 0.17751 0.10044 0.17280645 65.75843359 56.45726 1.51131 ATP2A1 7.03974863284906e-09 0.998563754361824 0.00143623859842789 ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting 1 FUNCTION: Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction.; DISEASE: Brody myopathy (BRM) [MIM:601003]: A disorder of muscle function that is characterized by painless muscle cramping and exercise-induced impairment of muscle relaxation. {ECO:0000269|PubMed:10914677}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Skeletal muscle, fast twitch muscle (type II) fibers.; colon;fovea centralis;choroid;skin;retina;corpus callosum;uterus;prostate;optic nerve;whole body;endometrium;larynx;thyroid;bone;testis;dura mater;brain;tonsil;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;muscle;blood;lens;skeletal muscle;greater omentum;pia mater;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;tongue;thyroid;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.78274 . -1.392555112 4.269874971 168.67085 2.83491 ATP2A1-AS1 . . . ATP2A1 antisense RNA 1 . . . . . . . . . . . ATP2A2 0.998230938512269 0.0017690614164708 7.1260687677231e-11 ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting 2 FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform 2 is involved in the regulation of the contraction/relaxation cycle. {ECO:0000269|PubMed:16402920}.; DISEASE: Acrokeratosis verruciformis (AKV) [MIM:101900]: A localized disorder of keratinization, which is inherited as an autosomal dominant trait. Its onset is early in life with multiple flat-topped, flesh-colored papules on the hands and feet, punctate keratoses on the palms and soles, with varying degrees of nail involvement. The histopathology shows a distinctive pattern of epidermal features with hyperkeratosis, hypergranulosis and acanthosis together with papillomatosis. These changes are frequently associated with circumscribed elevations of the epidermis that are said to resemble church spires. There are no features of dyskeratosis or acantholysis, the typical findings in lesions of Darier disease. {ECO:0000269|PubMed:12542527}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Darier disease (DD) [MIM:124200]: A skin disorder characterized by warty papules and plaques in seborrheic areas (central trunk, flexures, scalp and forehead), palmoplantar pits and distinctive nail abnormalities. It is due to loss of adhesion between epidermal cells (acantholysis) and abnormal keratinization. Patients with mild disease may have no more than a few scattered keratotic papules or subtle nail changes, whereas those with severe disease are handicapped by widespread malodorous keratotic plaques. Some patients present with hemorrhage into acantholytic vesicles on the palms and dorsal aspects of the fingers which gives rise to black macules. In a few families affected by Darier disease, neuropsychiatric abnormalities such as mild mental retardation, schizophrenia, bipolar disorder and epilepsy have been reported. Stress, UV exposure, heat, sweat, friction and oral contraception exacerbate disease symptoms. Clinical variants of Darier disease include hypertrophic, vesicobullous, hypopigmented, cornifying, zosteriform or linear, acute and comedonal subtypes. Comedonal Darier disease is characterized by the coexistence of acne-like comedonal lesions with typical Darier hyperkeratotic papules on light-exposed areas. At histopathologic level, comedonal Darier disease differs from classic Darier disease in the prominent follicular involvement and the presence of greatly elongated dermal villi. {ECO:0000269|PubMed:10080178, ECO:0000269|PubMed:10441323, ECO:0000269|PubMed:10441324, ECO:0000269|PubMed:10441325, ECO:0000269|PubMed:19995371}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is widely expressed in smooth muscle and nonmuscle tissues such as in adult skin epidermis, with highest expression in liver, pancreas and lung, and intermediate expression in brain, kidney and placenta. Also expressed at lower levels in heart and skeletal muscle. Isoforms 2 and 3 are highly expressed in the heart and slow twitch skeletal muscle. Expression of isoform 3 is predominantly restricted to cardiomyocytes and in close proximity to the sarcolemma. Both isoforms are mildly expressed in lung, kidney, liver, pancreas and placenta. Expression of isoform 3 is amplified during monocytic differentiation and also observed in the fetal heart. {ECO:0000269|PubMed:10441324, ECO:0000269|PubMed:12659872, ECO:0000269|PubMed:16402920}.; myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;amygdala;heart;cartilage;tongue;spinal cord;urinary;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;small intestine;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; amygdala;whole brain;thalamus;superior cervical ganglion;medulla oblongata;occipital lobe;tongue;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.26556 0.46129 -1.596455314 3.037272942 21.95162 0.73840 ATP2A3 0.0644500302496063 0.93554465479408 5.3149563139002e-06 ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting 3 FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports calcium ions from the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction. {ECO:0000269|PubMed:11956212, ECO:0000269|PubMed:15028735}.; . TISSUE SPECIFICITY: Found in most tissues. Most abundant in thymus, trachea, salivary gland, spleen, bone marrow, lymph node, peripheral leukocytes, pancreas and colon. Also detected in fetal tissues. Expressed in cell lineages of hematopoietic, epithelial, or embryonic origin and also expressed in several cancer cell lines. {ECO:0000269|PubMed:11956212, ECO:0000269|PubMed:15028735}.; ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;endometrium;synovium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;thymus; superior cervical ganglion;lymph node;white blood cells;skeletal muscle;bone marrow;prostate;trachea;trigeminal ganglion;whole blood;tonsil;cingulate cortex;thymus;cerebellum; 0.12887 0.19795 -1.471735692 3.739089408 775.92328 5.51515 ATP2B1 0.999997542188065 2.45781193385555e-06 9.41536584192614e-16 ATPase plasma membrane Ca2+ transporting 1 FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell.; . TISSUE SPECIFICITY: Isoform B is ubiquitously expressed. Isoform C is found in brain cortex, skeletal muscle and heart muscle. Isoform D has only been found in fetal skeletal muscle. Isoform K has been found in small intestine and liver.; ovary;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;amygdala;heart;cartilage;tongue;urinary;adrenal cortex;skeletal muscle;breast;macula lutea;liver;alveolus;spleen;mammary gland;developmental;colon;parathyroid;fovea centralis;uterus;whole body;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus; whole brain;amygdala;superior cervical ganglion;medulla oblongata;thalamus;occipital lobe;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.93195 0.23021 -1.023168368 7.944090587 35.43011 1.06974 ATP2B2 0.999921506473264 7.84935258569991e-05 8.79340811994955e-13 ATPase plasma membrane Ca2+ transporting 2 FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell.; . TISSUE SPECIFICITY: Mainly expressed in brain cortex. Found in low levels in skeletal muscle, heart muscle, stomach, liver, kidney and lung. Isoforms containing segment B are found in brain cortex and at low levels in other tissues. Isoforms containing segments X and W are found at low levels in all tissues. Isoforms containing segment A and segment Z are found at low levels in skeletal muscle and heart muscle.; amygdala;unclassifiable (Anatomical System);ovary;cerebellum cortex;lacrimal gland;hypothalamus;pineal body;fovea centralis;skeletal muscle;retina;subthalamic nucleus;lung;frontal lobe;adrenal gland;thyroid;macula lutea;hippocampus;liver;testis;spleen;kidney;brain;cerebellum; whole brain;amygdala;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.69922 0.18045 -1.943881244 1.893135173 96.26442 2.12107 ATP2B2-IT1 . . . ATP2B2 intronic transcript 1 . . . . . . . . . . . ATP2B2-IT2 . . . ATP2B2 intronic transcript 2 . . . . . . . . . . . ATP2B3 0.998768934027877 0.00123106241836752 3.55375565362763e-09 ATPase plasma membrane Ca2+ transporting 3 FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell.; . TISSUE SPECIFICITY: Highly expressed in the cerebellum, particulary in the presynaptic terminals of parallel fibers- Purkinje neurons. Isoform XE and isoform XB are the most abundant isoforms and are detected at low levels in brain and fetal skeletal muscle. The other isoforms are only found at lower levels and not in fetal tissues. {ECO:0000269|PubMed:22912398}.; unclassifiable (Anatomical System);islets of Langerhans;choroid;fovea centralis;lens;skin;retina;lung;optic nerve;ganglion;frontal lobe;macula lutea;liver;testis;brain;spinal ganglion; amygdala;dorsal root ganglion;whole brain;medulla oblongata;superior cervical ganglion;cerebellum peduncles;temporal lobe;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.36639 0.14753 -1.679229468 2.677518283 105.23057 2.22026 ATP2B4 0.521756389409679 0.478243559117524 5.14727978519182e-08 ATPase plasma membrane Ca2+ transporting 4 FUNCTION: Calcium/calmodulin-regulated and magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell (PubMed:8530416). By regulating sperm cell calcium homeostasis, may play a role in sperm motility (By similarity). {ECO:0000250|UniProtKB:Q6Q477, ECO:0000269|PubMed:8530416}.; . TISSUE SPECIFICITY: Isoform XB is the most abundant isoform and is expressed ubiquitously. Isoforms containing segment Z have only been detected in heart, while isoforms containing segment a have been found in heart, stomach and brain cortex. {ECO:0000269|PubMed:1531651}.; smooth muscle;ovary;colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;oesophagus;cochlea;cerebral cortex;endometrium;synovium;larynx;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;artery;unclassifiable (Anatomical System);amygdala;cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; uterus;amygdala;uterus corpus;superior cervical ganglion;adipose tissue;adrenal gland;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.39529 0.17922 -0.832257622 11.50625147 202.8817 3.07518 ATP2C1 0.999798834520344 0.00020116547929931 3.56440800076697e-13 ATPase secretory pathway Ca2+ transporting 1 FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium.; . TISSUE SPECIFICITY: Found in most tissues except colon, thymus, spleen and leukocytes. Most abundant in keratinocytes and kidney.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;gall bladder;cartilage;heart;urinary;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; amygdala;dorsal root ganglion;thalamus;superior cervical ganglion;occipital lobe;medulla oblongata;hypothalamus;temporal lobe;pons;caudate nucleus;skeletal muscle;fetal brain;prefrontal cortex;trigeminal ganglion;parietal lobe;cingulate cortex; 0.90393 0.20899 -0.290161348 33.33923095 603.64769 4.97394 ATP2C2 . . . ATPase secretory pathway Ca2+ transporting 2 FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;parathyroid;skeletal muscle;breast;pancreas;prostate;lung;larynx;placenta;testis;head and neck;brain;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;prostate;trachea;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14491 0.10508 -0.345679342 29.60014154 3878.8827 12.28367 ATP4A 6.98616960990842e-08 0.993651431969596 0.0063484981687081 ATPase H+/K+ transporting alpha subunit FUNCTION: Catalyzes the hydrolysis of ATP coupled with the exchange of H(+) and K(+) ions across the plasma membrane. Responsible for acid production in the stomach.; . TISSUE SPECIFICITY: Found in gastric mucosa.; pancreas;spleen;brain;stomach; superior cervical ganglion;adrenal cortex;ciliary ganglion; 0.07834 0.13523 -0.966362676 8.993866478 110.04734 2.27916 ATP4B 1.84084732787283e-05 0.452008641921668 0.547972949605053 ATPase H+/K+ transporting beta subunit FUNCTION: Required for stabilization and maturation of the catalytic proton pump alpha subunit and may also involved in cell adhesion and establishing epithelial cell polarity. {ECO:0000269|PubMed:19694409}.; . . unclassifiable (Anatomical System);colon;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.11926 0.13908 -0.045835247 50.34206181 184.69806 2.94944 ATP5A1 0.998862483879488 0.0011375016354416 1.44850702892854e-08 ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). {ECO:0000250, ECO:0000269|PubMed:10077593, ECO:0000269|PubMed:19285951}.; DISEASE: Combined oxidative phosphorylation deficiency 22 (COXPD22) [MIM:616045]: A mitochondrial disorder characterized by intrauterine growth retardation, microcephaly, hypotonia, pulmonary hypertension, failure to thrive, encephalopathy, and heart failure. {ECO:0000269|PubMed:23596069}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial complex V deficiency, nuclear 4 (MC5DN4) [MIM:615228]: A mitochondrial disorder with heterogeneous clinical manifestations including dysmorphic features, psychomotor retardation, hypotonia, growth retardation, cardiomyopathy, enlarged liver, hypoplastic kidneys and elevated lactate levels in urine, plasma and cerebrospinal fluid. {ECO:0000269|PubMed:23599390}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Fetal lung, heart, liver, gut and kidney. Expressed at higher levels in the fetal brain, retina and spinal cord. {ECO:0000269|PubMed:8428659}.; myocardium;lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;ganglion;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;ciliary body;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;vein;uterus;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;placenta;head and neck;kidney;stomach;thymus; amygdala;thalamus;occipital lobe;subthalamic nucleus;hypothalamus;globus pallidus;kidney;cingulate cortex; 0.27304 0.58400 -0.380166007 27.88393489 283.33028 3.60426 ATP5A1P1 . . . ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1 pseudogene 1 . . . . . . . . . . . ATP5A1P2 . . . ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1 pseudogene 2 . . . . . . . . . . . ATP5A1P3 . . . ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1 pseudogene 3 . . . . . . . . . . . ATP5A1P4 . . . ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1 pseudogene 4 . . . . . . . . . . . ATP5A1P5 . . . ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1 pseudogene 5 . . . . . . . . . . . ATP5A1P7 . . . ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1 pseudogene 7 . . . . . . . . . . . ATP5A1P8 . . . ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1 pseudogene 8 . . . . . . . . . . . ATP5A1P10 . . . ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1 pseudogene 10 . . . . . . . . . . . ATP5B 0.991635070003861 0.00836304252205015 1.88747408878412e-06 ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.; . . myocardium;ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;choroid;uterus;cerebral cortex;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;placenta;duodenum;kidney;stomach;thymus; whole brain;thalamus;medulla oblongata;occipital lobe;heart;cerebellum peduncles;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;globus pallidus;kidney;cingulate cortex;parietal lobe;cerebellum; 0.85270 0.70543 0.038710339 56.92380278 323.93914 3.82571 ATP5BP1 . . . ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide pseudogene 1 . . . . . . . . . . . ATP5C1 0.425803630820125 0.572639279376597 0.00155708980327898 ATP synthase, H+ transporting, mitochondrial F1 complex, gamma polypeptide 1 FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.; . TISSUE SPECIFICITY: Isoform Heart is expressed specifically in the heart and skeletal muscle, which require rapid energy supply. Isoform Liver is expressed in the brain, liver and kidney. Isoform Heart and Isoform Liver are expressed in the skin, intestine, stomach and aorta.; ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta; thalamus;superior cervical ganglion;heart;pons;kidney;trigeminal ganglion;parietal lobe;skeletal muscle; 0.31179 0.56962 -0.317668748 31.45789101 19.26228 0.66377 ATP5C1P1 . . . ATP synthase, H+ transporting, mitochondrial F1 complex, gamma polypeptide 1 pseudogene 1 . . . . . . . . . . . ATP5D 0.00118323811959957 0.396528053047928 0.602288708832472 ATP synthase, H+ transporting, mitochondrial F1 complex, delta subunit FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach; heart;thyroid;liver;globus pallidus;cingulate cortex;skeletal muscle; 0.19494 0.14451 -0.317668748 31.45789101 40.99259 1.20154 ATP5E 0.0060568330836871 0.497643957954306 0.496299208962007 ATP synthase, H+ transporting, mitochondrial F1 complex, epsilon subunit FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;cochlea;endometrium;thyroid;bladder;brain;tonsil;heart;pineal body;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;oral cavity;muscle;pancreas;lung;cornea;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; . 0.26372 . 0.257356108 69.83368719 8.86239 0.32663 ATP5EP1 . . . ATP synthase, H+ transporting, mitochondrial F1 complex, epsilon subunit pseudogene 1 . . . . . . . . . . . ATP5EP2 0.0224816072745641 0.534165557925256 0.44335283480018 ATP synthase, H+ transporting, mitochondrial F1 complex, epsilon subunit pseudogene 2 FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity). {ECO:0000250}.; . . . . . . . . 40.77653 1.19510 ATP5F1 0.0128675263722768 0.953558714299233 0.0335737593284897 ATP synthase, H+ transporting, mitochondrial Fo complex subunit B1 FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.; . . . . 0.41626 0.10622 -0.271755481 34.31823543 31.62565 0.99510 ATP5F1P1 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit B1 pseudogene 1 . . . . . . . . . . . ATP5F1P2 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit B1 pseudogene 2 . . . . . . . . . . . ATP5F1P3 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit B1 pseudogene 3 . . . . . . . . . . . ATP5F1P4 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit B1 pseudogene 4 . . . . . . . . . . . ATP5F1P5 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit B1 pseudogene 5 . . . . . . . . . . . ATP5F1P6 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit B1 pseudogene 6 . . . . . . . . . . . ATP5F1P7 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit B1 pseudogene 7 . . . . . . . . . . . ATP5G1 0.327525828609274 0.608263389500849 0.0642107818898766 ATP synthase, H+ transporting, mitochondrial Fo complex subunit C1 (subunit 9) FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.; . . myocardium;ovary;salivary gland;developmental;intestine;colon;parathyroid;vein;skin;uterus;prostate;whole body;larynx;bone;pituitary gland;testis;brain;bladder;artery;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;aorta;stomach;peripheral nerve; subthalamic nucleus;heart;pons;parietal lobe;skeletal muscle; 0.54109 0.11227 0.035072054 56.2514744 3.48084 0.12639 ATP5G1P1 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit C1 (subunit 9) pseudogene 1 . . . . . . . . . . . ATP5G1P2 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit C1 (subunit 9) pseudogene 2 . . . . . . . . . . . ATP5G1P3 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit C1 (subunit 9) pseudogene 3 . . . . . . . . . . . ATP5G1P4 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit C1 (subunit 9) pseudogene 4 . . . . . . . . . . . ATP5G1P5 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit C1 (subunit 9) pseudogene 5 . . . . . . . . . . . ATP5G1P6 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit C1 (subunit 9) pseudogene 6 . . . . . . . . . . . ATP5G1P7 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit C1 (subunit 9) pseudogene 7 . . . . . . . . . . . ATP5G1P8 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit C1 (subunit 9) pseudogene 8 . . . . . . . . . . . ATP5G2 0.000275239005290865 0.551889251528199 0.447835509466511 ATP synthase, H+ transporting, mitochondrial Fo complex subunit C2 (subunit 9) FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.; . . ovary;umbilical cord;skin;retina;bone marrow;prostate;endometrium;iris;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;larynx;synovium;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; skeletal muscle; 0.68553 0.09843 0.014844891 54.94810097 131.25366 2.49498 ATP5G2P1 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit C2 (subunit 9) pseudogene 1 . . . . . . . . . . . ATP5G2P2 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit C2 (subunit 9) pseudogene 2 . . . . . . . . . . . ATP5G2P3 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit C2 (subunit 9) pseudogene 3 . . . . . . . . . . . ATP5G2P4 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit C2 (subunit 9) pseudogene 4 . . . . . . . . . . . ATP5G3 0.538092564469556 0.447039679525596 0.0148677560048478 ATP synthase, H+ transporting, mitochondrial Fo complex subunit C3 (subunit 9) FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.; . . lymphoreticular;myocardium;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;endometrium;oesophagus;gum;bone;testis;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;trabecular meshwork;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;kidney;mammary gland;aorta;stomach; whole brain;amygdala;heart;liver;kidney; 0.22266 0.10445 -0.09720619 46.20193442 35.06268 1.06406 ATP5H 0.0108715653767665 0.835811293159691 0.153317141463543 ATP synthase, H+ transporting, mitochondrial Fo complex subunit D FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.; . . smooth muscle;ovary;developmental;colon;parathyroid;choroid;vein;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;hypothalamus;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;thymus; whole brain;subthalamic nucleus;thalamus;heart;temporal lobe;globus pallidus;pons;parietal lobe;cingulate cortex;skeletal muscle; 0.08883 0.13052 -0.207437529 38.2814343 5.75769 0.21625 ATP5HP1 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit D pseudogene 1 . . . . . . . . . . . ATP5HP2 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit D pseudogene 2 . . . . . . . . . . . ATP5HP3 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit D pseudogene 3 . . . . . . . . . . . ATP5HP4 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit D pseudogene 4 . . . . . . . . . . . ATP5I 0.207299098398329 0.648149693060615 0.144551208541056 ATP synthase, H+ transporting, mitochondrial Fo complex subunit E FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.; . . ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;frontal lobe;thyroid;pituitary gland;testis;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;heart;tongue;islets of Langerhans;pineal body;adrenal cortex;pharynx;blood;cerebrum;skeletal muscle;breast;lung;cornea;adrenal gland;nasopharynx;trabecular meshwork;macula lutea;visual apparatus;hippocampus;amnion;alveolus;liver;cervix;head and neck;kidney;mammary gland;aorta;stomach;cerebellum; whole brain;thalamus;medulla oblongata;heart;hypothalamus;temporal lobe;prefrontal cortex;caudate nucleus;parietal lobe;skeletal muscle;cingulate cortex; 0.68055 . 0.191216164 66.57230479 30.57521 0.97254 ATP5J 0.100188831785232 0.772433795998523 0.127377372216245 ATP synthase, H+ transporting, mitochondrial Fo complex subunit F6 FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes.; . . myocardium;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; whole brain;amygdala;adrenal gland;kidney;cingulate cortex; 0.03388 0.12052 0.479642105 78.95140363 190.58917 2.99523 ATP5J2 0.348503040158147 0.595678292881708 0.0558186669601447 ATP synthase, H+ transporting, mitochondrial Fo complex subunit F2 FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.; . . myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;cochlea;pituitary gland;testis;dura mater;brain;bladder;tonsil;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;cartilage;heart;epidermis;islets of Langerhans;oral cavity;muscle;pharynx;blood;skeletal muscle;breast;pancreas;pia mater;lung;cornea;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; . 0.12212 0.32778 0.347360312 73.97381458 8.72151 0.32041 ATP5J2-PTCD1 1.77777327849927e-09 0.386760912200586 0.613239086021641 ATP5J2-PTCD1 readthrough . . . . . . . 0.299418187 71.70323189 435.77622 4.35321 ATP5J2LP . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit F2-like pseudogene . . . . . . . . . . . ATP5J2P2 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit F2 pseudogene 2 . . . . . . . . . . . ATP5J2P3 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit F2 pseudogene 3 . . . . . . . . . . . ATP5J2P4 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit F2 pseudogene 4 . . . . . . . . . . . ATP5J2P5 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit F2 pseudogene 5 . . . . . . . . . . . ATP5J2P6 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit F2 pseudogene 6 . . . . . . . . . . . ATP5JP1 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit F6 pseudogene 1 . . . . . . . . . . . ATP5L 0.337891181698725 0.602189955274197 0.0599188630270772 ATP synthase, H+ transporting, mitochondrial Fo complex subunit G FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.; . . myocardium;medulla oblongata;ovary;umbilical cord;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;brain;bladder;gall bladder;tonsil;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum;thymus; whole brain;amygdala;medulla oblongata;heart;caudate nucleus;skeletal muscle;parietal lobe; 0.04786 0.12971 -0.075159878 47.78839349 10.2013 0.37187 ATP5L2 0.166948561167818 0.641036009721808 0.192015429110374 ATP synthase, H+ transporting, mitochondrial Fo complex subunit G2 FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). {ECO:0000250}.; . . . . . . 0.323496558 72.93583392 7.94254 0.29134 ATP5LP1 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit G pseudogene 1 . . . . . . . . . . . ATP5LP2 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit G pseudogene 2 . . . . . . . . . . . ATP5LP3 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit G pseudogene 3 . . . . . . . . . . . ATP5LP4 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit G pseudogene 4 . . . . . . . . . . . ATP5LP5 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit G pseudogene 5 . . . . . . . . . . . ATP5LP6 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit G pseudogene 6 . . . . . . . . . . . ATP5LP7 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit G pseudogene 7 . . . . . . . . . . . ATP5LP8 . . . ATP synthase, H+ transporting, mitochondrial Fo complex subunit G pseudogene 8 . . . . . . . . . . . ATP5O 0.434076662830685 0.558868726154379 0.00705461101493536 ATP synthase, H+ transporting, mitochondrial F1 complex, O subunit FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.; . . myocardium;medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;urinary;pharynx;blood;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;thymus; whole brain;amygdala;medulla oblongata;thalamus;testis - interstitial;occipital lobe;hypothalamus;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.08128 0.30022 -0.049474214 50.01179523 585.42964 4.90745 ATP5S 6.3043463659782e-05 0.475845362067508 0.524091594468832 ATP synthase, H+ transporting, mitochondrial Fo complex subunit s (factor B) FUNCTION: Involved in regulation of mitochondrial membrane ATP synthase. Necessary for H(+) conduction of ATP synthase. Facilitates energy-driven catalysis of ATP synthesis by blocking a proton leak through an alternative proton exit pathway (By similarity). {ECO:0000250}.; . . lymphoreticular;colon;parathyroid;skin;bone marrow;uterus;cerebral cortex;thyroid;testis;pineal gland;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;skeletal muscle;lung;adrenal gland;nasopharynx;placenta;visual apparatus;cervix;kidney;mammary gland; dorsal root ganglion;testis - interstitial;superior cervical ganglion;globus pallidus;testis;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06361 0.07062 0.104848986 61.49445624 84.78047 1.96155 ATP5SL 5.83218953056788e-05 0.698197984802202 0.301743693302492 ATP5S-like . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;heart;prefrontal cortex;kidney;skeletal muscle; 0.04463 0.07881 1.330184494 94.17315405 235.66496 3.31711 ATP6AP1 0.827633657438673 0.171588637963284 0.000777704598043546 ATPase H+ transporting accessory protein 1 FUNCTION: Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.07505 0.08671 0.439181676 77.69521113 223.33901 3.23075 ATP6AP1L 0.139629451145235 0.840701261667187 0.0196692871875783 ATPase H+ transporting accessory protein 1 like . . . . . . . 0.593509966 82.51356452 94.25044 2.08862 ATP6AP2 0.785047267980171 0.213523653562432 0.00142907845739734 ATPase H+ transporting accessory protein 2 FUNCTION: Functions as a renin and prorenin cellular receptor. May mediate renin-dependent cellular responses by activating ERK1 and ERK2. By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, it may also play a role in the renin-angiotensin system (RAS). {ECO:0000269|PubMed:12045255}.; DISEASE: Mental retardation, X-linked, with epilepsy (MRXE) [MIM:300423]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXE patients manifest mild to moderate mental retardation associated with epilepsy, delays in motor milestones and speech acquisition in infancy. {ECO:0000269|PubMed:15746149}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Parkinsonism with spasticity, X-linked (XPDS) [MIM:300911]: A syndrome characterized by parkinsonian features, such as cogwheel rigidity, resting tremor and bradykinesia, and variably penetrant spasticity. {ECO:0000269|PubMed:23595882}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, heart, placenta, liver, kidney and pancreas. Barely detectable in lung and skeletal muscles. In the kidney cortex it is restricted to the mesangium of glomeruli. In the coronary and kidney artery it is expressed in the subendothelium, associated to smooth muscles where it colocalizes with REN. Expressed in vascular structures and by syncytiotrophoblast cells in the mature fetal placenta. {ECO:0000269|PubMed:12045255, ECO:0000269|PubMed:15746149}.; . . 0.15953 0.19966 0.12689526 63.00424628 31.39695 0.98980 ATP6V1A 0.986543791938074 0.0134561578852729 5.01766528384694e-08 ATPase H+ transporting V1 subunit A FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.; . TISSUE SPECIFICITY: Present in all tissues analyzed.; myocardium;smooth muscle;ovary;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;hypothalamus;temporal lobe;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.25905 0.23728 -0.427900189 25.14744043 22.70912 0.75978 ATP6V1B1 0.000244050365843846 0.995997233947054 0.00375871568710207 ATPase H+ transporting V1 subunit B1 FUNCTION: Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.; DISEASE: Renal tubular acidosis, distal, with progressive nerve deafness (dRTA-D) [MIM:267300]: An autosomal recessive disease characterized by the association of renal distal tubular acidosis with sensorineural hearing loss. Distal renal tubular acidosis is characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. It is due to functional failure of alpha- intercalated cells of the cortical collecting duct of the distal nephron, where vectorial proton transport is required for urinary acidification. {ECO:0000269|PubMed:12414817, ECO:0000269|PubMed:12579397, ECO:0000269|PubMed:9916796}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the cochlea and endolymphatic sac. {ECO:0000269|PubMed:9916796}.; unclassifiable (Anatomical System);ovary;colon;parathyroid;fovea centralis;choroid;lens;retina;uterus;optic nerve;lung;endometrium;placenta;macula lutea;testis;spleen;kidney;brain;mammary gland;stomach; superior cervical ganglion;kidney;atrioventricular node;skeletal muscle; 0.16583 0.32362 -0.484940685 22.75300778 4381.39275 13.20978 ATP6V1B1-AS1 . . . ATP6V1B1 antisense RNA 1 . . . . . . . . . . . ATP6V1B2 0.991448562707497 0.00855142077910828 1.6513394933546e-08 ATPase H+ transporting V1 subunit B2 FUNCTION: Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.; DISEASE: Zimmermann-Laband syndrome 2 (ZLS2) [MIM:616455]: A disorder characterized by gingival fibromatosis, dysplastic or absent nails, finger abnormalities, hepatosplenomegaly, and abnormalities of the cartilage of the nose and/or ears. {ECO:0000269|PubMed:24913193, ECO:0000269|PubMed:25915598}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;thymus;cerebellum; whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;subthalamic nucleus;hypothalamus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.82107 0.27926 -0.446304853 24.33356924 125.9849 2.44322 ATP6V1C1 0.142543167612395 0.85663844478361 0.000818387603995116 ATPase H+ transporting V1 subunit C1 FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12384298}.; . . 0.31459 0.14896 -0.516085732 21.20193442 6.21695 0.23449 ATP6V1C2 2.2580233090132e-06 0.899975378939105 0.100022363037586 ATPase H+ transporting V1 subunit C2 FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.; . TISSUE SPECIFICITY: Kidney and placenta. {ECO:0000269|PubMed:12384298}.; myocardium;ovary;salivary gland;developmental;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;alveolus;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;stomach;peripheral nerve;cerebellum; dorsal root ganglion;superior cervical ganglion;salivary gland;placenta;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13413 0.11825 -0.023789244 52.09365416 2899.9886 10.20646 ATP6V1D 0.00315144323792958 0.985617158594917 0.0112313981671535 ATPase H+ transporting V1 subunit D FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium. {ECO:0000250, ECO:0000269|PubMed:21844891}.; . . myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;oesophagus;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach; amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;thalamus;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.30739 0.16306 -0.029247611 51.40363293 8.64004 0.31778 ATP6V1E1 0.882471622602822 0.117247858215169 0.000280519182009607 ATPase H+ transporting V1 subunit E1 FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12036578}.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;bladder;tonsil;heart;cartilage;tongue;nervous;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum;thymus; medulla oblongata;subthalamic nucleus;occipital lobe;thalamus;hypothalamus;temporal lobe;prefrontal cortex;globus pallidus;pons;cingulate cortex;parietal lobe; 0.17870 0.11846 0.035072054 56.2514744 35.33668 1.06775 ATP6V1E1P1 . . . ATPase H+ transporting V1 subunit E1 pseudogene 1 . . . . . . . . . . . ATP6V1E1P2 . . . ATPase H+ transporting V1 subunit E1 pseudogene 2 . . . . . . . . . . . ATP6V1E1P3 . . . ATPase H+ transporting V1 subunit E1 pseudogene 3 . . . . . . . . . . . ATP6V1E2 9.71403129278788e-05 0.567406155886837 0.432496703800235 ATPase H+ transporting V1 subunit E2 FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. This isoform is essential for energy coupling involved in acidification of acrosome (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12036578}.; unclassifiable (Anatomical System);medulla oblongata;heart;islets of Langerhans;colon;fovea centralis;choroid;lens;retina;optic nerve;lung;macula lutea;testis;kidney;brain; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;cingulate cortex;skeletal muscle; 0.13930 0.12131 0.084621747 60.31493277 126.2993 2.44673 ATP6V1F 0.563002529826286 0.388178949054287 0.0488185211194274 ATPase H+ transporting V1 subunit F FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.; . . myocardium;lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;pineal body;adrenal cortex;pharynx;blood;lens;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;duodenum;kidney;stomach;aorta; . 0.10770 . 0.014844891 54.94810097 49.07043 1.36900 ATP6V1G1 0.0451736710316889 0.671058580477894 0.283767748490417 ATPase H+ transporting V1 subunit G1 FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12384298}.; . . 0.15510 0.12549 0.413500896 76.67492333 20.79006 0.70432 ATP6V1G1P1 . . . ATPase H+ transporting V1 subunit G1 pseudogene 1 . . . . . . . . . . . ATP6V1G1P2 . . . ATPase H+ transporting V1 subunit G1 pseudogene 2 . . . . . . . . . . . ATP6V1G1P3 . . . ATPase H+ transporting V1 subunit G1 pseudogene 3 . . . . . . . . . . . ATP6V1G1P4 . . . ATPase H+ transporting V1 subunit G1 pseudogene 4 . . . . . . . . . . . ATP6V1G1P5 . . . ATPase H+ transporting V1 subunit G1 pseudogene 5 . . . . . . . . . . . ATP6V1G1P6 . . . ATPase H+ transporting V1 subunit G1 pseudogene 6 . . . . . . . . . . . ATP6V1G1P7 . . . ATPase H+ transporting V1 subunit G1 pseudogene 7 . . . . . . . . . . . ATP6V1G2 0.224789736223208 0.739331063592676 0.0358792001841162 ATPase H+ transporting V1 subunit G2 FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.; . TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:12384298}.; unclassifiable (Anatomical System);breast;frontal lobe;hippocampus;testis;brain;skeletal muscle;stomach;cerebellum; . 0.13180 . -0.009020804 52.8544468 11.59849 0.41979 ATP6V1G2-DDX39B . . . ATP6V1G2-DDX39B readthrough (NMD candidate) . . . . . . . . . . . ATP6V1G3 0.0305017788865879 0.809935236872529 0.159562984240883 ATPase H+ transporting V1 subunit G3 FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.; . TISSUE SPECIFICITY: Kidney. {ECO:0000269|PubMed:12384298}.; unclassifiable (Anatomical System);prostate;alveolus;kidney; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.09616 0.11651 1.102432221 91.93205945 304.83429 3.71723 ATP6V1H 3.85908994314964e-05 0.98938886150669 0.0105725475938787 ATPase H+ transporting V1 subunit H FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates the ATPase activity of the enzyme and couples ATPase activity to proton flow. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity). Involved in the endocytosis mediated by clathrin-coated pits, required for the formation of endosomes. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9620685}.; lymphoreticular;smooth muscle;ovary;sympathetic chain;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;frontal lobe;bone;thyroid;testis;dura mater;germinal center;spinal ganglion;brain;pineal gland;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;breast;bile duct;pancreas;pia mater;lung;nasopharynx;placenta;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.13691 0.18223 -0.734731259 14.01863647 56.40584 1.50942 ATP6V0A1 0.997249734540438 0.00275026541726216 4.2299631207696e-11 ATPase H+ transporting V0 subunit a1 FUNCTION: Required for assembly and activity of the vacuolar ATPase. Potential role in differential targeting and regulation of the enzyme for a specific organelle (By similarity). {ECO:0000250}.; . . lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;tongue;spinal cord;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus;cerebellum; amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.44599 0.50341 -0.688817379 15.20405756 53.36179 1.45103 ATP6V0A2 4.73810629233338e-06 0.999626027355911 0.000369234537797003 ATPase H+ transporting V0 subunit a2 FUNCTION: Part of the proton channel of V-ATPases. Essential component of the endosomal pH-sensing machinery. May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH. {ECO:0000269|PubMed:16415858, ECO:0000269|PubMed:18157129}.; DISEASE: Cutis laxa, autosomal recessive, 2A (ARCL2A) [MIM:219200]: A disorder characterized by an excessive congenital skin wrinkling, a large fontanelle with delayed closure, a typical facial appearance with downslanting palpebral fissures, a general connective tissue weakness, and varying degrees of growth and developmental delay and neurological abnormalities. Some affected individuals develop seizures and mental deterioration later in life, whereas the skin phenotype tends to become milder with age. At the molecular level, an abnormal glycosylation of serum proteins is observed in many cases. {ECO:0000269|PubMed:18157129}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Wrinkly skin syndrome (WSS) [MIM:278250]: A rare autosomal recessive disorder characterized by wrinkling of the skin of the dorsum of the hands and feet, an increased number of palmar and plantar creases, wrinkled abdominal skin, multiple musculoskeletal abnormalities, microcephaly, growth failure and developmental delay. {ECO:0000269|PubMed:18157129}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;uterus;prostate;endometrium;thyroid;bone;testis;amniotic fluid;germinal center;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;kidney; testis; 0.25637 0.37408 -0.615405356 17.47464025 564.74234 4.82506 ATP6V0A4 1.94342756038366e-12 0.945100202495782 0.0548997975022746 ATPase H+ transporting V0 subunit a4 FUNCTION: Part of the proton channel of the V-ATPase that is involved in normal vectorial acid transport into the urine by the kidney. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in adult and fetal kidney. Found in the inner ear. {ECO:0000269|PubMed:12414817}.; unclassifiable (Anatomical System);prostate;whole body;kidney;skeletal muscle;skin;stomach; superior cervical ganglion;kidney; 0.23229 0.22304 -0.169017544 40.67586695 1425.59356 7.05075 ATP6V0B 0.927635231427402 0.0719716804000241 0.000393088172573898 ATPase H+ transporting V0 subunit b FUNCTION: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;gall bladder;heart;cartilage;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;kidney;stomach; whole brain;amygdala;thalamus;liver;kidney;parietal lobe;cerebellum; 0.36214 0.11457 -0.053113545 49.38664779 26.0163 0.84553 ATP6V0C 0.729144944239477 0.258361881262603 0.0124931744979195 ATPase H+ transporting V0 subunit c FUNCTION: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.; . . smooth muscle;ovary;salivary gland;sympathetic chain;colon;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;breast;pancreas;lung;adrenal gland;epididymis;trabecular meshwork;placenta;visual apparatus;hippocampus;duodenum;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; amygdala;whole brain;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.15716 0.16113 -0.141298762 42.87567823 . . ATP6V0CP1 . . . ATPase H+ transporting V0 subunit c pseudogene 1 . . . . . . . . . . . ATP6V0CP2 . . . ATPase H+ transporting V0 subunit c pseudogene 2 . . . . . . . . . . . ATP6V0CP3 . . . ATPase H+ transporting V0 subunit c pseudogene 3 . . . . . . . . . . . ATP6V0CP4 . . . ATPase H+ transporting V0 subunit c pseudogene 4 . . . . . . . . . . . ATP6V0D1 0.988131750847399 0.01186380292239 4.44623021090481e-06 ATPase H+ transporting V0 subunit d1 FUNCTION: Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. May play a role in coupling of proton transport and ATP hydrolysis (By similarity). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12384298, ECO:0000269|PubMed:8250920}.; lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;brain;heart;cartilage;blood;lens;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;thymus; amygdala;whole brain;thalamus;parietal lobe; 0.18002 0.25991 -0.361761279 28.6329323 8.62148 0.31611 ATP6V0D2 2.36746090830609e-08 0.267484373179556 0.732515603145835 ATPase H+ transporting V0 subunit d2 FUNCTION: Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. May play a role in coupling of proton transport and ATP hydrolysis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Kidney, osteoclast and lung. {ECO:0000269|PubMed:12384298}.; unclassifiable (Anatomical System);lung;alveolus;colon;blood;kidney;skin;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;kidney; 0.26682 0.13647 0.130533008 63.35810333 343.88437 3.93148 ATP6V0E1 0.277597261020232 0.632760467146229 0.0896422718335396 ATPase H+ transporting V0 subunit e1 FUNCTION: Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17350184}.; myocardium;lymphoreticular;medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;bladder;brain;gall bladder;tonsil;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;bone;pituitary gland;testis;unclassifiable (Anatomical System);trophoblast;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach; superior cervical ganglion;adipose tissue;adrenal gland;placenta;kidney;atrioventricular node;whole blood;pituitary;bone marrow; 0.17120 0.13401 0.035072054 56.2514744 1.21425 0.03948 ATP6V0E1P1 . . . ATPase H+ transporting V0 subunit e1 pseudogene 1 . . . . . . . . . . . ATP6V0E1P2 . . . ATPase H+ transporting V0 subunit e1 pseudogene 2 . . . . . . . . . . . ATP6V0E1P3 . . . ATPase H+ transporting V0 subunit e1 pseudogene 3 . . . . . . . . . . . ATP6V0E1P4 . . . ATPase H+ transporting V0 subunit e1 pseudogene 4 . . . . . . . . . . . ATP6V0E2 2.0563161489236e-05 0.155204905158912 0.844774531679598 ATPase H+ transporting V0 subunit e2 FUNCTION: Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is expressed at high levels in heart, brain and kidney and also detected in inner ear epithelium, vestibule, testis, epididymis and bladder. Isoform 2 is expressed in heart, kidney, placenta and pancreas. Isoform 2 is not detected in frontal cortex, but is prevalent in all other brain areas. {ECO:0000269|PubMed:17350184}.; ovary;sympathetic chain;colon;parathyroid;choroid;retina;prostate;optic nerve;ganglion;frontal lobe;endometrium;larynx;thyroid;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach;cerebellum; amygdala;whole brain;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;thyroid;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; . . . . 649.37059 5.11295 ATP6V0E2-AS1 . . . ATP6V0E2 antisense RNA 1 . . . . . . . . . . . ATP7A 0.999634377087713 0.000365622874965512 3.73212349762216e-11 ATPase copper transporting alpha FUNCTION: May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells.; DISEASE: Menkes disease (MNKD) [MIM:309400]: An X-linked recessive disorder of copper metabolism characterized by generalized copper deficiency. MNKD results in progressive neurodegeneration and connective-tissue disturbances: focal cerebral and cerebellar degeneration, early growth retardation, peculiar hair, hypopigmentation, cutis laxa, vascular complications and death in early childhood. The clinical features result from the dysfunction of several copper-dependent enzymes. A mild form of the disease has been described, in which cerebellar ataxia and moderate developmental delay predominate. {ECO:0000269|PubMed:10079817, ECO:0000269|PubMed:10319589, ECO:0000269|PubMed:10401004, ECO:0000269|PubMed:11241493, ECO:0000269|PubMed:11350187, ECO:0000269|PubMed:15981243, ECO:0000269|PubMed:22992316, ECO:0000269|PubMed:7977350, ECO:0000269|PubMed:8981948}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Occipital horn syndrome (OHS) [MIM:304150]: An X-linked recessive disorder of copper metabolism. Common features are unusual facial appearance, skeletal abnormalities, chronic diarrhea and genitourinary defects. The skeletal abnormalities include occipital horns, short, broad clavicles, deformed radii, ulnae and humeri, narrowing of the rib cage, undercalcified long bones with thin cortical walls and coxa valga. {ECO:0000269|PubMed:11431706, ECO:0000269|PubMed:17108763, ECO:0000269|PubMed:9246006}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Distal spinal muscular atrophy, X-linked, 3 (DSMAX3) [MIM:300489]: A neuromuscular disorder. Distal spinal muscular atrophy, also known as distal hereditary motor neuronopathy, represents a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. {ECO:0000269|PubMed:20170900}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in most tissues except liver. Isoform 3 is widely expressed including in liver cell lines. Isoform 1 is expressed in fibroblasts, choriocarcinoma, colon carcinoma and neuroblastoma cell lines. Isoform 2 is expressed in fibroblasts, colon carcinoma and neuroblastoma cell lines.; unclassifiable (Anatomical System);uterus;umbilical cord;ovary;heart;bone;blood;germinal center;brain;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21692 . 0.406006364 76.49209719 2933.24166 10.26979 ATP7B 5.23092252901538e-20 0.00548256643290595 0.994517433567094 ATPase copper transporting beta FUNCTION: Involved in the export of copper out of the cells, such as the efflux of hepatic copper into the bile.; DISEASE: Wilson disease (WD) [MIM:277900]: An autosomal recessive disorder of copper metabolism in which copper cannot be incorporated into ceruloplasmin in liver, and cannot be excreted from the liver into the bile. Copper accumulates in the liver and subsequently in the brain and kidney. The disease is characterized by neurologic manifestations and signs of cirrhosis. {ECO:0000269|PubMed:10051024, ECO:0000269|PubMed:10194254, ECO:0000269|PubMed:10447265, ECO:0000269|PubMed:10453196, ECO:0000269|PubMed:10502776, ECO:0000269|PubMed:10502777, ECO:0000269|PubMed:10544227, ECO:0000269|PubMed:10721669, ECO:0000269|PubMed:10790207, ECO:0000269|PubMed:11043508, ECO:0000269|PubMed:11093740, ECO:0000269|PubMed:11180609, ECO:0000269|PubMed:11216666, ECO:0000269|PubMed:11243728, ECO:0000269|PubMed:11690702, ECO:0000269|PubMed:11954751, ECO:0000269|PubMed:12325021, ECO:0000269|PubMed:12376745, ECO:0000269|PubMed:12544487, ECO:0000269|PubMed:14639035, ECO:0000269|PubMed:14966923, ECO:0000269|PubMed:14986826, ECO:0000269|PubMed:15024742, ECO:0000269|PubMed:15557537, ECO:0000269|PubMed:15811015, ECO:0000269|PubMed:15845031, ECO:0000269|PubMed:15952988, ECO:0000269|PubMed:15967699, ECO:0000269|PubMed:16088907, ECO:0000269|PubMed:16207219, ECO:0000269|PubMed:16283883, ECO:0000269|PubMed:17718866, ECO:0000269|PubMed:18373411, ECO:0000269|PubMed:21682854, ECO:0000269|PubMed:7626145, ECO:0000269|PubMed:8298641, ECO:0000269|PubMed:8533760, ECO:0000269|PubMed:8782057, ECO:0000269|PubMed:8931691, ECO:0000269|PubMed:8938442, ECO:0000269|PubMed:8980283, ECO:0000269|PubMed:9222767, ECO:0000269|PubMed:9311736, ECO:0000269|PubMed:9452121, ECO:0000269|PubMed:9482578, ECO:0000269|PubMed:9554743, ECO:0000269|PubMed:9671269, ECO:0000269|PubMed:9772425, ECO:0000269|PubMed:9829905, ECO:0000269|PubMed:9887381}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Most abundant in liver and kidney and also found in brain. Isoform 2 is expressed in brain but not in liver. The cleaved form WND/140 kDa is found in liver cell lines and other tissues.; unclassifiable (Anatomical System);heart;colon;skin;skeletal muscle;breast;uterus;prostate;whole body;lung;endometrium;synovium;thyroid;placenta;visual apparatus;liver;testis;kidney;spinal ganglion;brain;stomach; dorsal root ganglion;superior cervical ganglion;appendix;atrioventricular node;pons;trigeminal ganglion; 0.30819 0.63604 -0.3363152 30.37862703 2480.95753 9.28654 ATP7BP1 . . . ATPase copper transporting beta pseudogene 1 . . . . . . . . . . . ATP8A1 0.999804445776751 0.000195554223248747 5.57727346986793e-16 ATPase phospholipid transporting 8A1 FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. In vitro, its ATPase activity is selectively and stereospecifically stimulated by phosphatidylserine (PS). The flippase complex ATP8A1:TMEM30A seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Acts as aminophospholipid translocase at the plasma membrane in neuronal cells.; . TISSUE SPECIFICITY: Found in most adult tissues except liver, testis and placenta. Most abundant in heart, brain and skeletal muscle. Also detected in fetal tissues. Isoform 1 is only detected in brain, skeletal muscle and heart and is the most abundant form in skeletal muscle.; unclassifiable (Anatomical System);amygdala;ovary;islets of Langerhans;colon;blood;parathyroid;skeletal muscle;retina;bone marrow;prostate;lung;nasopharynx;visual apparatus;hippocampus;testis;germinal center; dorsal root ganglion;amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;spinal cord;prefrontal cortex;caudate nucleus;parietal lobe; 0.79910 0.11110 -0.641086234 16.6784619 389.36969 4.15685 ATP8A2 0.418077899724509 0.581922099330203 9.45288845810739e-10 ATPase phospholipid transporting 8A2 FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. Reconstituted to liposomes, the ATP8A2:TMEM30A flippase complex predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). Proposed to function in the generation and maintenance of phospholipid asymmetry in photoreceptor disk membranes and neuronal axon membranes. May be involved in vesicle trafficking in neuronal cells. Involved in regulation of neurite outgrowth; acting in synergy with TMEM30A. Required for normal visual and auditory function; involved in photoreceptor and inner ear spiral ganglion cell survival.; DISEASE: Note=A chromosomal aberration disrupting ATP8A2 has been found in a patient with severe mental retardation and major hypotonia. Translocation t(10;13)(p12.1;q12.13) (PubMed:20683487). {ECO:0000269|PubMed:20683487}.; TISSUE SPECIFICITY: Strongly expressed in the brain, cerebellum, retina and testis. {ECO:0000269|PubMed:20683487, ECO:0000269|PubMed:22892528}.; unclassifiable (Anatomical System);optic nerve;lung;macula lutea;pituitary gland;testis;fovea centralis;choroid;lens;brain;retina; whole brain;amygdala;superior cervical ganglion;medulla oblongata;thalamus;testis - interstitial;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;pons;atrioventricular node;skin;subthalamic nucleus;fetal brain;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;pituitary;cingulate cortex; 0.33216 0.22285 -1.104093597 6.894314697 112.54149 2.30702 ATP8A2P1 . . . ATPase phospholipid transporting 8A2 pseudogene 1 . . . . . . . . . . . ATP8A2P2 . . . ATPase phospholipid transporting 8A2 pseudogene 2 . . . . . . . . . . . ATP8A2P3 . . . ATPase phospholipid transporting 8A2 pseudogene 3 . . . . . . . . . . . ATP8B1 3.6650370597666e-07 0.999994689129379 4.94436691445026e-06 ATPase phospholipid transporting 8B1 FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. May play a role in asymmetric distribution of phospholipids in the canicular membrane. May have a role in transport of bile acids into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both. In cooperation with ABCB4 may be involved in establishing integrity of the canalicular membrane thus protecting hepatocytes from bile salts. Together with TMEM30A is involved in uptake of the synthetic drug alkylphospholipid perifosine. Involved in the microvillus formation in polarized epithelial cells; the function seems to be independent from its flippase activity. Required for the preservation of cochlear hair cells in the inner ear. May act as cardiolipin transporter during inflammatory injury. {ECO:0000269|PubMed:17948906, ECO:0000269|PubMed:20510206, ECO:0000269|PubMed:20512993}.; DISEASE: Cholestasis, benign recurrent intrahepatic, 1 (BRIC1) [MIM:243300]: A disorder characterized by intermittent episodes of cholestasis without progression to liver failure. There is initial elevation of serum bile acids, followed by cholestatic jaundice which generally spontaneously resolves after periods of weeks to months. The cholestatic attacks vary in severity and duration. Patients are asymptomatic between episodes, both clinically and biochemically. {ECO:0000269|PubMed:15239083, ECO:0000269|PubMed:9500542, ECO:0000269|PubMed:9918928}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cholestasis of pregnancy, intrahepatic 1 (ICP1) [MIM:147480]: A liver disorder of pregnancy. It presents during the second or, more commonly, the third trimester of pregnancy with intense pruritus which becomes more severe with advancing gestation and cholestasis. Cholestasis results from abnormal biliary transport from the liver into the small intestine. ICP1 causes fetal distress, spontaneous premature delivery and intrauterine death. ICP1 patients have spontaneous and progressive disappearance of cholestasis after delivery. {ECO:0000269|PubMed:15657619, ECO:0000269|PubMed:15888793}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in most tissues except brain and skeletal muscle. Most abundant in pancreas and small intestine.; unclassifiable (Anatomical System);cartilage;ovary;lacrimal gland;urinary;colon;blood;skeletal muscle;retina;breast;uterus;lung;endometrium;epididymis;bone;thyroid;liver;testis;germinal center;mammary gland;stomach; superior cervical ganglion;prostate;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe; 0.14419 0.16680 0.099178678 60.75725407 773.9349 5.50409 ATP8B2 0.999564591733884 0.000435408265642631 4.7322046472425e-13 ATPase phospholipid transporting 8B2 FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable). {ECO:0000305}.; . TISSUE SPECIFICITY: Isoform 3 is ubiquitous, with highest expression in aorta, cerebellum and uterus. {ECO:0000269|PubMed:12880872}.; unclassifiable (Anatomical System);prostate;frontal lobe;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle;cerebellum; 0.36637 . -1.655370293 2.754187308 159.00297 2.75420 ATP8B3 9.18832885175999e-22 0.00362440409617302 0.996375595903827 ATPase phospholipid transporting 8B3 FUNCTION: P4-ATPase flippase which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. May be responsible for the maintenance of asymmetric distribution of phosphatidylserine (PS) in spermatozoa membranes. Involved in acrosome reactions and binding of spermatozoa to zona pellucida. {ECO:0000250|UniProtKB:Q6UQ17}.; . TISSUE SPECIFICITY: Isoform 3 was only detected in testis. {ECO:0000269|PubMed:12880872}.; unclassifiable (Anatomical System);prostate;pancreas;lung;cartilage;liver;testis;colon;cervix;germinal center; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;trigeminal ganglion; 0.07662 . -0.44655933 24.21561689 4172.41798 12.83150 ATP8B4 2.42164394305674e-27 0.000683849523660963 0.999316150476339 ATPase phospholipid transporting 8B4 (putative) FUNCTION: Component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable). {ECO:0000305}.; . TISSUE SPECIFICITY: Ubiquitously expressed at moderate levels.; unclassifiable (Anatomical System);prostate;lymph node;ovary;placenta;liver;parathyroid;spleen;blood;brain;bone marrow; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.10236 0.08514 1.122466798 92.11488559 2982.33619 10.36535 ATP8B5P . . . ATPase phospholipid transporting 8B5, pseudogene . . . lung;testis; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;skeletal muscle; . . . . . . ATP9A 0.999980637361735 1.93626382634439e-05 1.1902477578875e-15 ATPase phospholipid transporting 9A (putative) . . . ovary;skin;retina;bone marrow;prostate;optic nerve;ganglion;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;amygdala;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;pancreas;lung;adrenal gland;placenta;hippocampus;duodenum;hypopharynx;amnion;head and neck;kidney;stomach;thymus; amygdala;whole brain;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.13853 0.11774 -1.638744339 2.801368247 81.80933 1.91713 ATP9B 7.02414710042202e-12 0.997995332969668 0.00200466702330806 ATPase phospholipid transporting 9B (putative) . . . ovary;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;optic nerve;endometrium;bone;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;muscle;blood;lens;skeletal muscle;bile duct;breast;lung;macula lutea;hippocampus;spleen;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.24270 0.10686 -1.137345532 6.398914838 2145.56837 8.51992 ATP10A 0.611013499237766 0.388986495742668 5.01956598163428e-09 ATPase phospholipid transporting 10A (putative) FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable). {ECO:0000305}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in kidney, followed by lung, brain, prostate, testis, ovary and small intestine.; unclassifiable (Anatomical System);heart;tongue;colon;blood;skeletal muscle;skin;retina;bone marrow;bile duct;uterus;head and neck;brain;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion; 0.11760 0.15831 1.291519174 93.86058033 7442.03783 18.53574 ATP10B 1.3436999038052e-23 0.0153025942581443 0.984697405741856 ATPase phospholipid transporting 10B (putative) FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable). {ECO:0000305}.; . TISSUE SPECIFICITY: Found in brain and in low levels in testis.; unclassifiable (Anatomical System);spinal cord;colon;choroid;fovea centralis;lens;skeletal muscle;retina;uterus;optic nerve;lung;placenta;macula lutea;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;pons;atrioventricular node;trigeminal ganglion; 0.14291 0.09980 1.376027048 94.52111347 906.19881 5.85888 ATP10D 2.24183562738568e-11 0.999619731486492 0.00038026849109012 ATPase phospholipid transporting 10D (putative) FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable). {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in placenta and, to a lesser extent, in kidney. {ECO:0000269|PubMed:12532265}.; myocardium;smooth muscle;colon;skin;uterus;prostate;cochlea;endometrium;larynx;thyroid;bone;testis;dura mater;germinal center;brain;pineal gland;unclassifiable (Anatomical System);meninges;heart;cartilage;spinal cord;adrenal cortex;skeletal muscle;breast;pia mater;lung;nasopharynx;placenta;visual apparatus;liver;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.05559 0.09450 0.304886748 72.01580561 8226.34926 19.58886 ATP11A 0.967333743318821 0.0326662566504506 3.07284035838027e-11 ATPase phospholipid transporting 11A FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable). May be involved in the uptake of farnesyltransferase inhibitor drugs, such as lonafarnib. {ECO:0000269|PubMed:15860663, ECO:0000305}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;lens;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;cervix;kidney;stomach;thymus; superior cervical ganglion;atrioventricular node; 0.22056 0.10642 -1.605857744 3.007784855 269.18999 3.51905 ATP11A-AS1 . . . ATP11A antisense RNA 1 . . . . . . . . . . . ATP11AUN . . . ATP11A upstream neighbor . . . . . 0.09810 . 0.503505267 79.88912479 . . ATP11B 0.992834850949756 0.00716514904661013 3.63344164736379e-12 ATPase phospholipid transporting 11B (putative) FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable). Involved in regulation of sensitivity to cisplatin; may contribute to secretory vesicle transport of cisplatin from Golgi to plasma membrane. {ECO:0000269|PubMed:23585472, ECO:0000305}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus;cerebellum; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skin;skeletal muscle; 0.22960 0.11076 -0.440847477 24.59896202 300.7301 3.69690 ATP11C 0.999724526368115 0.000275473628096394 3.78876625946235e-12 ATPase phospholipid transporting 11C FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. Required for B cell differentiation past the pro-B cell stage. Seems to mediate phosphatidylserine (PS) flipping in pro-B cells. May be involved in the transport of cholestatic bile acids (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15533723}.; smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;cochlea;larynx;bone;thyroid;testis;amniotic fluid;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;adrenal cortex;breast;pancreas;lung;adrenal gland;placenta;liver;duodenum;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.47993 0.10205 -0.312207497 32.05944798 297.46779 3.67873 ATP12A 9.71336645553994e-10 0.97662214727716 0.0233778517515029 ATPase H+/K+ transporting non-gastric alpha2 subunit FUNCTION: Catalyzes the hydrolysis of ATP coupled with the exchange of H(+) and K(+) ions across the plasma membrane. Responsible for potassium absorption in various tissues.; . TISSUE SPECIFICITY: Found in skin and kidney. Detected in prostate basal cells (at protein level). Expression is increased in benign prostate hyperplasia and tumor tissues (at protein level). {ECO:0000269|PubMed:22179016, ECO:0000269|PubMed:9872395}.; unclassifiable (Anatomical System);pancreas;lung;placenta;testis; superior cervical ganglion;trachea;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12819 0.23463 -1.317365938 4.782967681 557.27679 4.79481 ATP13A1 0.994473888962369 0.00552611080522852 2.32402305168644e-10 ATPase 13A1 FUNCTION: Mediates manganese transport into the endoplasmic reticulum. The ATPase activity is required for cellular manganese homeostasis. {ECO:0000269|PubMed:24392018}.; . . medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;synovium;thyroid;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;tongue;lacrimal gland;islets of Langerhans;blood;lens;breast;pancreas;lung;cornea;epididymis;placenta;macula lutea;liver;head and neck;spleen;kidney;mammary gland;stomach;cerebellum;thymus; superior cervical ganglion; 0.19052 . -1.256630467 5.343241331 177.5161 2.89634 ATP13A2 0.00120495054739301 0.998791883204951 3.16624765619446e-06 ATPase 13A2 FUNCTION: May play a role in intracellular cation homeostasis and the maintenance of neuronal integrity. {ECO:0000269|PubMed:22186024}.; DISEASE: Ceroid lipofuscinosis, neuronal, 12 (CLN12) [MIM:606693]: A form of neuronal ceroid lipofuscinosis characterized by rapidly progressive visual loss due to retinal dystrophy, seizures, cerebellar ataxia, and cerebellar atrophy. Cognitive decline may also occur. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material. {ECO:0000269|PubMed:22388936}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain; protein levels are markedly increased in brain from subjects with Parkinson disease and subjects with dementia with Lewy bodies. Detected in pyramidal neurons located throughout the cingulate cortex (at protein level). In the substantia nigra, it is found in neuromelanin- positive dopaminergic neurons (at protein level). {ECO:0000269|PubMed:22186024}.; ovary;adrenal medulla;colon;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;hippocampus;liver;cervix;spleen;kidney;cerebellum; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.15955 0.16122 -1.159397299 6.098136353 202.72703 3.07383 ATP13A3 0.999967444596667 3.25554033289205e-05 4.21998791290568e-15 ATPase 13A3 . . . myocardium;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;smooth muscle;thyroid;globus pallidus;ciliary ganglion;trigeminal ganglion;skin; 0.77644 0.09695 -0.971800989 8.946685539 102.60373 2.19038 ATP13A4 6.07648654021509e-10 0.999598041426712 0.000401957965638992 ATPase 13A4 . DISEASE: Note=A chromosomal aberration involving ATP13A4 is found in 2 patients with specific language impairment (SLI) disorders. Paracentric inversion inv(3)(q25;q29). The inversion produces a disruption of the protein. {ECO:0000269|PubMed:15925480}.; TISSUE SPECIFICITY: Expressed in heart, placenta, liver, skeletal muscles, and pancreas. Lower levels of expression are also detected in brain, lung and kidney. Weakly expressed in the adult brain. Expression in fetal brain is higher than in adult brain, with levels similar to several other fetal tissues including spleen and skeletal muscle. In adult brain expressed at low levels in all tissues examined, including the temporal lobe and putamen. {ECO:0000269|PubMed:15925480}.; unclassifiable (Anatomical System);frontal lobe;larynx;thyroid;oral cavity;pituitary gland;head and neck;brain;skeletal muscle;stomach;tonsil; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.08132 0.09862 -1.383523256 4.358339231 5510.00677 15.30149 ATP13A4-AS1 . . . ATP13A4 antisense RNA 1 . . . . . . . . . . . ATP13A5 6.22871619777347e-28 0.000591888645944594 0.999408111354055 ATPase 13A5 . . . unclassifiable (Anatomical System);optic nerve;lung;larynx;macula lutea;head and neck;fovea centralis;choroid;lens;mammary gland;retina; superior cervical ganglion; 0.08819 0.07983 2.035714332 97.7235197 9429.75387 21.03804 ATP13A5-AS1 . . . ATP13A5 antisense RNA 1 . . . . . . . . . . . ATP23 . . . ATP23 metallopeptidase and ATP synthase assembly factor homolog (S. cerevisiae) . . . . . 0.12751 0.11458 0.305084559 72.22811984 . . ATPAF1 0.236382638181407 0.756475237711192 0.00714212410740061 ATP synthase mitochondrial F1 complex assembly factor 1 FUNCTION: May play an essential role for the assembly of the mitochondrial F1-F0 complex. {ECO:0000250}.; . TISSUE SPECIFICITY: Weakly expressed in muscle. {ECO:0000269|PubMed:12965202}.; unclassifiable (Anatomical System);myocardium;heart;ovary;colon;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;lung;macula lutea;liver;testis;kidney;brain;mammary gland; superior cervical ganglion;parietal lobe;skeletal muscle; 0.20480 0.09937 -0.449946534 24.00330267 90.33026 2.04502 ATPAF2 0.00143053764737735 0.870930742075727 0.127638720276895 ATP synthase mitochondrial F1 complex assembly factor 2 FUNCTION: May play a role in the assembly of the F1 component of the mitochondrial ATP synthase (ATPase). {ECO:0000269|PubMed:11410595}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11410595}.; ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;skeletal muscle;pancreas;lung;placenta;liver;spleen;head and neck;cervix;kidney;stomach;cerebellum; . 0.14597 0.14592 -0.291981272 33.20358575 88.18307 2.01102 ATPIF1 0.0593535041039216 0.868023214177609 0.0726232817184697 ATPase inhibitory factor 1 FUNCTION: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase. Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme. {ECO:0000269|PubMed:12110673, ECO:0000269|PubMed:15528193, ECO:0000269|PubMed:19559621, ECO:0000269|PubMed:23135403}.; . . myocardium;lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;thymus;cerebellum; whole brain;amygdala;thalamus;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;heart;hypothalamus;temporal lobe;prefrontal cortex;testis;globus pallidus; 0.12984 0.09670 0.080983847 59.76055674 7.166 0.26884 ATR 0.701297833041861 0.298702166958139 5.0391074256713e-17 ATR serine/threonine kinase FUNCTION: Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates BRCA1, CHEK1, MCM2, RAD17, RPA2, SMC1 and p53/TP53, which collectively inhibit DNA replication and mitosis and promote DNA repair, recombination and apoptosis. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at sites of DNA damage, thereby regulating DNA damage response mechanism. Required for FANCD2 ubiquitination. Critical for maintenance of fragile site stability and efficient regulation of centrosome duplication. {ECO:0000269|PubMed:10597277, ECO:0000269|PubMed:10608806, ECO:0000269|PubMed:10859164, ECO:0000269|PubMed:11114888, ECO:0000269|PubMed:11418864, ECO:0000269|PubMed:11673449, ECO:0000269|PubMed:11721054, ECO:0000269|PubMed:11865061, ECO:0000269|PubMed:12526805, ECO:0000269|PubMed:12791985, ECO:0000269|PubMed:12814551, ECO:0000269|PubMed:14657349, ECO:0000269|PubMed:14729973, ECO:0000269|PubMed:14742437, ECO:0000269|PubMed:15210935, ECO:0000269|PubMed:15314022, ECO:0000269|PubMed:15496423, ECO:0000269|PubMed:16260606, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:9427750, ECO:0000269|PubMed:9636169, ECO:0000269|PubMed:9925639}.; DISEASE: Seckel syndrome 1 (SCKL1) [MIM:210600]: A rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and mental retardation. {ECO:0000269|PubMed:12640452}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cutaneous telangiectasia and cancer syndrome, familial (FCTCS) [MIM:614564]: A disease characterized by cutaneous telangiectases in infancy with patchy alopecia over areas of affected skin, thinning of the lateral eyebrows, and mild dental and nail anomalies. Affected individuals are at increased risk of developing oropharyngeal cancer, and other malignancies have been reported as well. {ECO:0000269|PubMed:22341969}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous, with highest expression in testis. Isoform 2 is found in pancreas, placenta and liver but not in heart, testis and ovary. {ECO:0000269|PubMed:11470508, ECO:0000269|PubMed:8610130, ECO:0000269|PubMed:8843195}.; ovary;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;alveolus;head and neck;kidney;mammary gland;stomach;peripheral nerve; amygdala;superior cervical ganglion;medulla oblongata;testis - interstitial;thyroid;globus pallidus;white blood cells;ciliary ganglion;pons;skeletal muscle;pituitary; 0.81267 0.14325 -1.639226005 2.789573013 836.25678 5.66230 ATRAID 0.00791394898030435 0.928803979884424 0.063282071135272 all-trans retinoic acid induced differentiation factor FUNCTION: Promotes osteoblast cell differentiation and terminal mineralization. Plays a role in inducing the cell cycle arrest via inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal pathway. {ECO:0000269|PubMed:21723284}.; . TISSUE SPECIFICITY: Weakly expressed in hematopoietic cell lines. {ECO:0000269|PubMed:11042152}.; . . 0.05596 0.06793 0.527368849 80.73248408 726.23535 5.34993 ATRIP 0.00148697990787471 0.997122212550173 0.00139080754195261 ATR interacting protein FUNCTION: Required for checkpoint signaling after DNA damage. Required for ATR expression, possibly by stabilizing the protein. {ECO:0000269|PubMed:12791985}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11721054}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;colon;choroid;skin;uterus;lung;endometrium;placenta;iris;liver;testis;spleen;brain;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; . 0.20525 -0.749505784 13.74144845 572.61213 4.85824 ATRN 0.999999975840269 2.41597305593378e-08 2.45530999030624e-21 attractin FUNCTION: Involved in the initial immune cell clustering during inflammatory response and may regulate chemotactic activity of chemokines. May play a role in melanocortin signaling pathways that regulate energy homeostasis and hair color. Low-affinity receptor for agouti (By similarity). Has a critical role in normal myelination in the central nervous system (By similarity). {ECO:0000250, ECO:0000269|PubMed:9736737}.; . TISSUE SPECIFICITY: Isoform 2 is detected in plasma (at protein level). Expressed and secreted by activated T-lymphocytes. Expressed at low to moderate levels in peripheral blood leukocytes, spleen, lymph node, tonsil, bone marrow and fetal liver. At very low levels found in thymus. Isoform 2 is the major isoform in peripheral blood leukocytes. {ECO:0000269|PubMed:10811918, ECO:0000269|PubMed:17261078}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;frontal lobe;endometrium;synovium;larynx;bone;thyroid;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;spinal cord;urinary;adrenal cortex;pharynx;blood;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;amnion;liver;cervix;spleen;head and neck;kidney;mammary gland;nose;stomach;cerebellum; amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;temporal lobe;caudate nucleus;skeletal muscle;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.27789 0.17365 0.117584698 62.19037509 3379.60468 11.13499 ATRNL1 0.995631864108185 0.0043681358915953 2.1934349774107e-13 attractin like 1 FUNCTION: May play a role in melanocortin signaling pathways that regulate energy homeostasis. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;colon;skin;uterus;pancreas;prostate;lung;frontal lobe;endometrium;bone;placenta;visual apparatus;pituitary gland;alveolus;hypopharynx;liver;testis;head and neck;spleen;kidney;brain;peripheral nerve; dorsal root ganglion;amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.59947 0.10764 -1.5928285 3.066761029 94.60853 2.09473 ATRX 0.99999998229899 1.77010100986311e-08 2.32879727055664e-22 alpha thalassemia/mental retardation syndrome X-linked FUNCTION: Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3- containing nucleosomes. Catalytic component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S- phase and telomeres, and the in vitro remodeling of H3.3- containing nucleosomes. Its heterochromatin targeting is proposed to involve a combinatorial readout of histone H3 modifications (specifically methylation states of H3K9 and H3K4) and association with CBX5. Involved in maintaining telomere structural integrity in embryonic stem cells which probably implies recruitment of CBX5 to telomers. Reports on the involvement in transcriptional regulation of telomeric repeat-containing RNA (TERRA) are conflicting; according (PubMed:24500201) is not sufficient to decrease chromatin condensation at telomers nor to increase expression of telomeric RNA in fibroblasts. May be involved in telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines. Acts as negative regulator of chromatin incorporation of transcriptionally repressive histone H2AFY, particularily at telomeres and the alpha-globin cluster in erythroleukemic cells. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, required for the chromatin occupancy of SMC1 and CTCTF within the H19 imprinting control region (ICR) and involved in esatblishment of histone tails modifications in the ICR. May be involved in brain development and facial morphogenesis. {ECO:0000269|PubMed:12953102, ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:20504901, ECO:0000269|PubMed:20651253, ECO:0000269|PubMed:21029860, ECO:0000269|PubMed:22391447, ECO:0000269|PubMed:22829774, ECO:0000269|PubMed:24500201}.; DISEASE: Alpha-thalassemia mental retardation syndrome, X-linked (ATRX) [MIM:301040]: A disorder characterized by severe psychomotor retardation, facial dysmorphism, urogenital abnormalities, and alpha-thalassemia. An essential phenotypic trait are hemoglobin H erythrocyte inclusions. {ECO:0000269|PubMed:10204841, ECO:0000269|PubMed:10417298, ECO:0000269|PubMed:10660327, ECO:0000269|PubMed:10995512, ECO:0000269|PubMed:12116232, ECO:0000269|PubMed:16955409, ECO:0000269|PubMed:7697714, ECO:0000269|PubMed:8968741, ECO:0000269|PubMed:9043863, ECO:0000269|PubMed:9326931}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) [MIM:309580]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXSHF1 is a syndromic mental retardation. Clinical features include severe mental retardation, dysmorphic facies, and a highly skewed X-inactivation pattern in carrier women. Other more variable features include hypogonadism, deafness, renal anomalies, and mild skeletal defects. {ECO:0000269|PubMed:10398237, ECO:0000269|PubMed:10751095, ECO:0000269|PubMed:11050622, ECO:0000269|PubMed:15565397, ECO:0000269|PubMed:16222662, ECO:0000269|PubMed:8630485}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Alpha-thalassemia myelodysplasia syndrome (ATMDS) [MIM:300448]: A disorder characterized by hypochromic, microcytic red blood cells, hemoglobin H detected in peripheral blood, and multilineage myelodysplasia. {ECO:0000269|PubMed:12858175}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; . . . 0.56316 -0.925889687 9.754659118 107.54684 2.25148 ATXN1 0.398661149433984 0.599425706431175 0.00191314413484115 ataxin 1 FUNCTION: Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Binds RNA in vitro. May be involved in RNA metabolism. {ECO:0000269|PubMed:21475249}.; DISEASE: Spinocerebellar ataxia 1 (SCA1) [MIM:164400]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA1 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. SCA1 is caused by expansion of a CAG repeat in the coding region of ATXN1. Longer expansions result in earlier onset and more severe clinical manifestations of the disease. {ECO:0000269|PubMed:7647801, ECO:0000269|PubMed:7951322, ECO:0000269|PubMed:8634720}. Note=The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by expansion of the polyglutamine tract to about 40-83 repeats, causing accumulation in neurons and exerting toxicity. {ECO:0000269|PubMed:7647801, ECO:0000269|PubMed:8634720}.; TISSUE SPECIFICITY: Widely expressed throughout the body. {ECO:0000269|PubMed:12062018}.; lymphoreticular;ovary;salivary gland;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;blood;cerebrum;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; occipital lobe;subthalamic nucleus;temporal lobe;prefrontal cortex;globus pallidus;caudate nucleus;skeletal muscle; 0.97273 0.42931 -0.523584927 20.93654164 313.64901 3.76558 ATXN1L . . . ataxin 1 like FUNCTION: Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Can suppress ATXN1 cytotoxicity in spinocerebellar ataxia type 1 (SCA1) (By similarity). {ECO:0000250, ECO:0000269|PubMed:21475249}.; . TISSUE SPECIFICITY: Expressed in cerebellum and cerebral cortex. {ECO:0000269|PubMed:16121196}.; . . . . 0.637604436 83.77565464 1685.42189 7.56537 ATXN2 0.999862271558356 0.000137728440943969 6.99987097021896e-13 ataxin 2 FUNCTION: Involved in EGFR trafficking, acting as negative regulator of endocytic EGFR internalization at the plasma membrane. {ECO:0000269|PubMed:18602463}.; DISEASE: Spinocerebellar ataxia 2 (SCA2) [MIM:183090]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA2 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. SCA2 is characterized by hyporeflexia, myoclonus and action tremor and dopamine-responsive parkinsonism. In some patients, SCA2 presents as pure familial parkinsonism without cerebellar signs. {ECO:0000269|PubMed:8896555, ECO:0000269|PubMed:8896556, ECO:0000269|PubMed:8896557}. Note=The disease is caused by mutations affecting the gene represented in this entry. SCA2 is caused by expansion of a CAG repeat resulting in about 36 to 52 repeats in some patients. Longer expansions result in earlier the expansion, onset of the disease.; DISEASE: Amyotrophic lateral sclerosis 13 (ALS13) [MIM:183090]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. {ECO:0000269|PubMed:20740007}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. An increased risk for developing amyotrophic lateral sclerosis seems to be conferred by CAG repeat intermediate expansions greater than 23 but below the threshold for developing spinocerebellar ataxia.; TISSUE SPECIFICITY: Expressed in the brain, heart, liver, skeletal muscle, pancreas and placenta. Isoform 1 is predominant in the brain and spinal cord. Isoform 4 is more abundant in the cerebellum. In the brain, broadly expressed in the amygdala, caudate nucleus, corpus callosum, hippocampus, hypothalamus, substantia nigra, subthalamic nucleus and thalamus. {ECO:0000269|PubMed:8896555, ECO:0000269|PubMed:8896556, ECO:0000269|PubMed:8896557, ECO:0000269|PubMed:9480749}.; . . 0.90140 0.25008 -0.995664936 8.539749941 5321.63293 15.08852 ATXN2L 0.999950395532872 4.96044670696151e-05 5.81752214460669e-14 ataxin 2 like FUNCTION: Involved in the regulation of stress granule and P-body formation. {ECO:0000269|PubMed:23209657}.; . TISSUE SPECIFICITY: Expressed at high levels in thymus, lymph node, spleen, fetal kidney and adult testis. Constitutively associated with MPL and EPOR in hematopoietic cells. {ECO:0000269|PubMed:11784712}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;oesophagus;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;thymus;cerebellum; dorsal root ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.45112 0.12083 -1.725143594 2.447511205 101.85413 2.18340 ATXN3 0.176363907956847 0.823089158866112 0.00054693317704127 ataxin 3 FUNCTION: Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates. Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins. Involved in degradation of misfolded chaperone substrates via its interaction with STUB1/CHIP: recruited to monoubiquitinated STUB1/CHIP, and restricts the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. In response to misfolded substrate ubiquitination, mediates deubiquitination of monoubiquitinated STUB1/CHIP. Interacts with key regulators of transcription and represses transcription: acts as a histone- binding protein that regulates transcription. {ECO:0000269|PubMed:12297501, ECO:0000269|PubMed:16118278, ECO:0000269|PubMed:17696782, ECO:0000269|PubMed:23625928}.; DISEASE: Spinocerebellar ataxia 3 (SCA3) [MIM:109150]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA3 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. The molecular defect in SCA3 is the a CAG repeat expansion in ATX3 coding region. Longer expansions result in earlier onset and more severe clinical manifestations of the disease. {ECO:0000269|PubMed:7874163}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; colon;choroid;fovea centralis;skin;retina;uterus;optic nerve;bone;testis;germinal center;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;spinal cord;lens;skeletal muscle;lung;nasopharynx;placenta;visual apparatus;macula lutea;liver;spleen;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;temporal lobe;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15932 0.34757 0.283038099 71.26680821 4218.49197 12.91759 ATXN3L 4.31613107316262e-09 0.0154762051990041 0.984523790484865 ataxin 3 like FUNCTION: Deubiquitinating enzyme that cleaves both 'Lys-48'- linked and 'Lys-63'-linked poly-ubiquitin chains (in vitro).; . . . . 0.20889 0.10379 0.815800671 87.8744987 103.93709 2.20216 ATXN7 0.928556027503616 0.0714407786580683 3.19383831573931e-06 ataxin 7 FUNCTION: Acts as component of the STAGA transcription coactivator-HAT complex. Mediates the interaction of STAGA complex with the CRX and is involved in CRX-dependent gene activation. Necessary for microtubule cytoskeleton stabilization. {ECO:0000269|PubMed:22100762}.; DISEASE: Spinocerebellar ataxia 7 (SCA7) [MIM:164500]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA7 belongs to the autosomal dominant cerebellar ataxias type II (ADCA II) which are characterized by cerebellar ataxia with retinal degeneration and pigmentary macular dystrophy. {ECO:0000269|PubMed:9288099}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform a and isoform b are expressed in CNS, but isoform a is expressed predominantly in the peripherical tissues. Isoform b is also highly expressed in the frontal lobe, skeletal muscle and spinal cord and is expressed at a lower level in the lung, lymphoblast and intestine.; unclassifiable (Anatomical System);cartilage;ovary;spinal cord;colon;parathyroid;skin;skeletal muscle;breast;prostate;lung;endometrium;placenta;hypopharynx;liver;testis;head and neck;spleen;cervix;germinal center;brain;stomach;thymus; placenta; 0.40116 0.43982 0.205769367 67.49823071 3924.42931 12.38246 ATXN7L1 0.11109157508575 0.7773714013099 0.11153702360435 ataxin 7 like 1 . . . unclassifiable (Anatomical System);lung;hypothalamus;nasopharynx;bone;spinal cord;muscle;liver;colon;bladder;skin; medulla oblongata;superior cervical ganglion;temporal lobe;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.93840 0.09337 0.174625237 65.9648502 250.63523 3.41154 ATXN7L2 0.718954812432385 0.280915690672269 0.000129496895345702 ataxin 7 like 2 . . . . . 0.26286 0.07430 -0.909290275 10.03184713 323.63888 3.82196 ATXN7L3 0.955238890019342 0.0447562586932642 4.85128739407105e-06 ataxin 7 like 3 FUNCTION: Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B. The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation. Within the complex, it is required to recruit USP22 and ENY2 into the SAGA complex. {ECO:0000255|HAMAP- Rule:MF_03047, ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:21746879}.; . . . . 0.69497 0.11262 -0.626318434 17.03231894 13.69563 0.49678 ATXN7L3B 0.0979606124442928 0.579363606215299 0.322675781340408 ataxin 7 like 3B . . . . . . . 0.079165051 59.43029016 1.94981 0.06353 ATXN8 . . . ataxin 8 . DISEASE: Spinocerebellar ataxia 8 (SCA8) [MIM:608768]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA8 is an autosomal dominant cerebellar ataxia (ADCA). It is caused by expansion of a CAG repeat in ATXN8, which is translated into a nearly pure polyglutamine protein which forms 1C2-positive inclusions in Purkinje cells and other neurons. {ECO:0000269|PubMed:16804541}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Specifically found in brains from SCA8 patients (at protein level). {ECO:0000269|PubMed:16804541}.; . . . . . . . . ATXN8OS . . . ATXN8 opposite strand (non-protein coding) . . TISSUE SPECIFICITY: Expressed in brain (PubMed:10192387). Expressed in muscle tissues (at protein level). {ECO:0000269|PubMed:10192387, ECO:0000269|PubMed:24040107}.; . . . . . . . . ATXN10 0.745162923489296 0.254740145639095 9.69308716091215e-05 ataxin 10 FUNCTION: Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis. {ECO:0000250}.; DISEASE: Note=Defects in ATXN1 may be a cause of nephronophthisis a chronic tubulo-interstitial nephropathy that leads to anemia, polyuria, polydipsia, isosthenuria and death in uremia. {ECO:0000269|PubMed:21565611}.; TISSUE SPECIFICITY: Expressed in the central nervous system. {ECO:0000269|PubMed:15201271}.; lymphoreticular;ovary;umbilical cord;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;hypothalamus;muscle;temporal lobe;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; whole brain;dorsal root ganglion;amygdala;medulla oblongata;thalamus;occipital lobe;superior cervical ganglion;hypothalamus;pons;atrioventricular node;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.16218 0.16168 -1.023168368 7.944090587 41.65693 1.21327 AUH 0.00725253971720532 0.97635615974302 0.0163913005397746 AU RNA binding protein/enoyl-CoA hydratase FUNCTION: Catalyzes the conversion of 3-methylglutaconyl-CoA to 3- hydroxy-3-methylglutaryl-CoA. Has very low enoyl-CoA hydratase activity. Was originally identified as RNA-binding protein that binds in vitro to clustered 5'-AUUUA-3' motifs. {ECO:0000269|PubMed:11738050, ECO:0000269|PubMed:12434311, ECO:0000269|PubMed:12655555, ECO:0000269|PubMed:7892223}.; DISEASE: 3-methylglutaconic aciduria 1 (MGA1) [MIM:250950]: An inborn error of leucine metabolism. It leads to an autosomal recessive syndrome with variable clinical phenotype, ranging from delayed speech development to severe psychomotor retardation, coma, failure to thrive, metabolic acidosis and dystonia. MGA1 can be distinguished from other forms of MGA by the pattern of metabolite excretion: 3-methylglutaconic acid levels are higher than those detected in other forms, whereas methylglutaric acid levels are usually only slightly elevated and there is a high level of 3-hydroxyisovaleric acid excretion (not present in other MGA forms). {ECO:0000269|PubMed:12655555}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;bone;pituitary gland;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;lymph node;heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;lung;pia mater;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland; dorsal root ganglion;amygdala;superior cervical ganglion;globus pallidus;pons;trigeminal ganglion;cingulate cortex; 0.13140 0.33290 -0.383807564 27.41802312 47.66926 1.34049 AUNIP 5.49329871865606e-08 0.067784776513311 0.932215168553702 aurora kinase A and ninein interacting protein FUNCTION: Required for the dynamic movement of AURKA at the centrosomes and spindle apparatus during the cell cycle. {ECO:0000269|PubMed:20596670}.; . TISSUE SPECIFICITY: Expressed in heart, skeletal muscles, placenta and testis.; . . 0.24641 . 0.284856336 71.40835103 185.19192 2.95558 AUNX1 . . . auditory neuropathy, X-linked recessive 1 . . . . . . . . . . . AUP1 0.0241550475219776 0.972956419696408 0.00288853278161428 ancient ubiquitous protein 1 FUNCTION: May play a role in the translocation of terminally misfolded proteins from the endoplasmic reticulum lumen to the cytoplasm and their degradation by the proteasome. {ECO:0000269|PubMed:18711132}.; . TISSUE SPECIFICITY: Detected in blood platelets and leukocytes (at protein level). Ubiquitous. Highly expressed in placenta, liver, kidney, skeletal muscle, heart and brain. {ECO:0000269|PubMed:12042322}.; medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus;cerebellum; thalamus;liver; 0.38699 0.12045 0.218717575 68.27081859 204.40645 3.08918 AURKA 0.435603931095833 0.562950388723161 0.00144568018100625 aurora kinase A FUNCTION: Mitotic serine/threonine kinases that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity. Required for normal axon formation. Plays a role in microtubule remodeling during neurite extension. Important for microtubule formation and/or stabilization. Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and stabilizing p53/TP53. Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity. Necessary for proper cilia disassembly prior to mitosis. {ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:11551964, ECO:0000269|PubMed:12390251, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14523000, ECO:0000269|PubMed:14702041, ECO:0000269|PubMed:14990569, ECO:0000269|PubMed:15128871, ECO:0000269|PubMed:15147269, ECO:0000269|PubMed:15987997, ECO:0000269|PubMed:17125279, ECO:0000269|PubMed:17360485, ECO:0000269|PubMed:17604723, ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19357306, ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:19812038, ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:9606188}.; . TISSUE SPECIFICITY: Highly expressed in testis and weakly in skeletal muscle, thymus and spleen. Also highly expressed in colon, ovarian, prostate, neuroblastoma, breast and cervical cancer cell lines.; ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;bone;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis;tumor;trigeminal ganglion;skeletal muscle; 0.85128 0.22853 0.903992902 89.39018636 72.1192 1.76914 AURKAIP1 0.00247538764889321 0.544889583001888 0.452635029349218 aurora kinase A interacting protein 1 FUNCTION: May act as a negative regulator of Aurora-A kinase, by down-regulation through proteasome-dependent degradation.; . TISSUE SPECIFICITY: Ubiquitously expressed and especially highly expressed in heart, skeletal muscle and testis.; myocardium;lymphoreticular;umbilical cord;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;germinal center;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;choroid;fovea centralis;uterus;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;placenta;hippocampus;kidney;stomach;thymus; whole brain;testis - interstitial;testis - seminiferous tubule;heart;liver;testis; 0.06072 0.09873 -0.071520315 48.34866714 221.34313 3.21862 AURKAPS1 . . . aurora kinase A pseudogene 1 . . . . . . . . . . . AURKAPS2 . . . aurora kinase A pseudogene 2 . . . . . . . . . . . AURKB 0.00588233863615652 0.972205698730534 0.0219119626333096 aurora kinase B FUNCTION: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission- competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis (PubMed:22422861, PubMed:24814515). AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPT1, VIM/vimentin, GSG2/Haspin, and histone H3. A positive feedback loop involving GSG2 and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively). A positive feedback between GSG2 and AURKB contributes to CPC localization. AURKB is also required for kinetochore localization of BUB1 and SGOL1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes. {ECO:0000269|PubMed:11516652, ECO:0000269|PubMed:11756469, ECO:0000269|PubMed:11784863, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12458200, ECO:0000269|PubMed:12686604, ECO:0000269|PubMed:12689593, ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:14602875, ECO:0000269|PubMed:14610074, ECO:0000269|PubMed:14722118, ECO:0000269|PubMed:15020684, ECO:0000269|PubMed:15249581, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:17617734, ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:21658950, ECO:0000269|PubMed:22422861, ECO:0000269|PubMed:24814515}.; DISEASE: Note=Disruptive regulation of expression is a possible mechanism of the perturbation of chromosomal integrity in cancer cells through its dominant-negative effect on cytokinesis.; TISSUE SPECIFICITY: High level expression seen in the thymus. It is also expressed in the spleen, lung, testis, colon, placenta and fetal liver. Expressed during S and G2/M phase and expression is up-regulated in cancer cells during M phase. {ECO:0000269|PubMed:9809983, ECO:0000269|PubMed:9858806}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;muscle;pharynx;blood;lens;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;tumor;ciliary ganglion; 0.84245 0.20793 -0.159704656 41.90846898 105.891 2.23064 AURKBPS1 . . . aurora kinase B pseudogene 1 . . . . . . . . . . . AURKC 0.151759586463599 0.831262008769731 0.0169784047666705 aurora kinase C FUNCTION: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Plays also a role in meiosis and more particularly in spermatogenesis. Has redundant cellular functions with AURKB and can rescue an AURKB knockdown. Like AURKB, AURKC phosphorylates histone H3 at 'Ser-10' and 'Ser-28'. Phosphorylates TACC1, another protein involved in cell division, at 'Ser-228'. {ECO:0000269|PubMed:15316025, ECO:0000269|PubMed:15499654, ECO:0000269|PubMed:15670791, ECO:0000269|PubMed:15938719, ECO:0000269|PubMed:21493633, ECO:0000269|PubMed:21531210}.; DISEASE: Spermatogenic failure 5 (SPGF5) [MIM:243060]: An infertility disorder caused by spermatogenesis defects. Semen from affected men show close to 100% morphologically abnormal multiflagellar spermatozoa with low motility, oversized irregular heads, and abnormal midpiece and acrosome. {ECO:0000269|PubMed:17435757, ECO:0000269|PubMed:21733974}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in testis. Elevated expression levels were seen only in a subset of cancer cell lines such as Hep-G2, Huh-7 and HeLa. Expression is maximum at M phase. {ECO:0000269|PubMed:15670791}.; unclassifiable (Anatomical System);testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07295 0.09546 -0.205617011 38.57631517 21.72885 0.73157 AUTS1 . . . autism susceptibility 1 . . . . . . . . . . . AUTS2 0.996187482008472 0.0038125178976658 9.3862583484727e-11 autism susceptibility candidate 2 . . TISSUE SPECIFICITY: Strongly expressed in brain, skeletal muscle and kidney. Also expressed in placenta, lung and leukocytes. {ECO:0000269|PubMed:12160723, ECO:0000269|PubMed:23332918}.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;skeletal muscle;whole body;nasopharynx;bone;visual apparatus;testis;cervix;amniotic fluid;brain;artery;mammary gland;aorta; . 0.83083 0.10750 -1.967739992 1.816466148 320.02805 3.80007 AVEN 5.70186245131166e-08 0.129799703049474 0.870200239931901 apoptosis and caspase activation inhibitor FUNCTION: Protects against apoptosis mediated by Apaf-1.; . TISSUE SPECIFICITY: Highly expressed in testis, ovary, thymus, prostate, spleen, small intestine, colon, heart, skeletal muscle, liver, kidney and pancreas.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;thyroid;bone;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;urinary;pharynx;blood;lung;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach; lung;placenta; 0.07537 0.13990 0.797386419 87.53833451 951.56366 5.97070 AVIL 1.03036255351714e-10 0.976044571813728 0.023955428083236 advillin FUNCTION: Ca(2+)-regulated actin-binding protein. May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1-mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis. {ECO:0000269|PubMed:20393563}.; . TISSUE SPECIFICITY: Most highly expressed in the small intestine and colonic lining. Weaker expression also detected in the thymus, prostate, testes and uterus. {ECO:0000269|PubMed:12034507}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;endometrium;larynx;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;lens;skeletal muscle;pancreas;lung;nasopharynx;macula lutea;liver;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.10761 0.12246 -0.749505784 13.74144845 187.26695 2.97227 AVL9 0.00032549454622102 0.997181485933672 0.00249301952010655 AVL9 cell migration associated FUNCTION: Functions in cell migration. {ECO:0000269|PubMed:22595670}.; . . unclassifiable (Anatomical System);islets of Langerhans;colon;blood;lens;skin;skeletal muscle;bone marrow;pancreas;prostate;lung;adrenal gland;bone;placenta;liver;testis;spleen;germinal center;kidney;brain;stomach; dorsal root ganglion;amygdala;medulla oblongata;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.20914 0.10089 -0.356299879 29.31115829 90.87931 2.05107 AVP 0.183145102453943 0.645729404484881 0.171125493061176 arginine vasopressin FUNCTION: Neurophysin 2 specifically binds vasopressin.; DISEASE: Diabetes insipidus, neurohypophyseal (NDI) [MIM:125700]: A disease characterized by persistent thirst, polydipsia and polyuria. Affected individuals are apparently normal at birth, but characteristically develop symptoms of vasopressin deficiency during childhood. {ECO:0000269|PubMed:10369876, ECO:0000269|PubMed:10487710, ECO:0000269|PubMed:10677561, ECO:0000269|PubMed:11017955, ECO:0000269|PubMed:11150885, ECO:0000269|PubMed:11161827, ECO:0000269|PubMed:11443218, ECO:0000269|PubMed:11748489, ECO:0000269|PubMed:11980620, ECO:0000269|PubMed:12012274, ECO:0000269|PubMed:12107248, ECO:0000269|PubMed:12359138, ECO:0000269|PubMed:12519420, ECO:0000269|PubMed:12931042, ECO:0000269|PubMed:14510916, ECO:0000269|PubMed:14673472, ECO:0000269|PubMed:15538939, ECO:0000269|PubMed:1740104, ECO:0000269|PubMed:7714110, ECO:0000269|PubMed:8045958, ECO:0000269|PubMed:8103767, ECO:0000269|PubMed:8370682, ECO:0000269|PubMed:8514868, ECO:0000269|PubMed:8554046, ECO:0000269|PubMed:9360520, ECO:0000269|PubMed:9580132, ECO:0000269|PubMed:9814475}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.32884 . . . 43.68918 1.25813 AVPI1 1.07449770214276e-05 0.108241405654053 0.891747849368926 arginine vasopressin induced 1 FUNCTION: May be involved in MAP kinase activation, epithelial sodium channel (ENaC) down-regulation and cell cycling. {ECO:0000250}.; . . . . 0.04592 . 0.415317661 76.81056853 2610.17736 9.56067 AVPR1A 1.28646095006851e-05 0.38396001031857 0.616027125071929 arginine vasopressin receptor 1A FUNCTION: Receptor for arginine vasopressin. The activity of this receptor is mediated by G proteins which activate a phosphatidyl- inositol-calcium second messenger system. Has been involved in social behaviors, including affiliation and attachment. {ECO:0000269|PubMed:12082568}.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;parathyroid;skin;skeletal muscle;uterus;prostate;lung;placenta;testis;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;uterus corpus;globus pallidus;ciliary ganglion;pons;atrioventricular node;caudate nucleus;trigeminal ganglion; 0.11241 0.16482 -0.247889024 35.98726115 360.41032 4.01799 AVPR1B 2.82255376407223e-05 0.328117052721059 0.6718547217413 arginine vasopressin receptor 1B FUNCTION: Receptor for arginine vasopressin. The activity of this receptor is mediated by G proteins which activate a phosphatidyl- inositol-calcium second messenger system.; . . . . 0.09061 0.10168 0.644875971 84.10002359 1403.1573 7.00371 AVPR2 0.119885620397291 0.779474281954155 0.100640097648554 arginine vasopressin receptor 2 FUNCTION: Receptor for arginine vasopressin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Involved in renal water reabsorption. {ECO:0000269|PubMed:19440390}.; DISEASE: Diabetes insipidus, nephrogenic, X-linked (XNDI) [MIM:304800]: A disorder caused by the inability of the renal collecting ducts to absorb water in response to arginine vasopressin. Characterized by excessive water drinking (polydipsia), excessive urine excretion (polyuria), persistent hypotonic urine, and hypokalemia. {ECO:0000269|PubMed:10694923, ECO:0000269|PubMed:10770218, ECO:0000269|PubMed:11232028, ECO:0000269|PubMed:11916004, ECO:0000269|PubMed:1303257, ECO:0000269|PubMed:1303271, ECO:0000269|PubMed:1356229, ECO:0000269|PubMed:16845277, ECO:0000269|PubMed:7560098, ECO:0000269|PubMed:7833930, ECO:0000269|PubMed:7984150, ECO:0000269|PubMed:7987330, ECO:0000269|PubMed:7999078, ECO:0000269|PubMed:8037205, ECO:0000269|PubMed:8045948, ECO:0000269|PubMed:8078903, ECO:0000269|PubMed:8267567, ECO:0000269|PubMed:8479490, ECO:0000269|PubMed:8514744, ECO:0000269|PubMed:9402087, ECO:0000269|PubMed:9452109, ECO:0000269|PubMed:9711877}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Kidney.; unclassifiable (Anatomical System);uterus;pancreas;lung;testis;brain; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.17911 0.58893 1.087645262 91.8494928 240.65849 3.35204 AVSD1 . . . atrioventricular septal defect 1 . . . . . . . . . . . AWAT1 0.0150959038854437 0.877240921357064 0.107663174757492 acyl-CoA wax alcohol acyltransferase 1 FUNCTION: Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has a preference for arachidyl alcohol as well as decyl alcohol, demonstrating its relatively poor activity using saturated long chain alcohols (C16, C18, and C20). {ECO:0000269|PubMed:15671038}.; . TISSUE SPECIFICITY: Predominantly expressed in skin, where it is limited to the sebaceous gland. Expressed in more mature, centrally located cells just before their rupture and sebum release. Also expressed in all tissues except spleen. Expressed at higher level in thymus, prostate and testis. {ECO:0000269|PubMed:15671038}.; . . 0.23575 0.09482 -0.205617011 38.57631517 87.57293 1.99798 AWAT2 0.603147993992504 0.387918631362412 0.00893337464508458 acyl-CoA wax alcohol acyltransferase 2 FUNCTION: Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has no activity using decyl alcohol and significantly prefers the C16 and C18 alcohols. May also have 2-acylglycerol O-acyltransferase (MGAT) and acyl- CoA:retinol acyltransferase (ARAT) activities, to catalyze the synthesis of diacylglycerols and retinyl esters; however this activity is unclear in vivo. {ECO:0000269|PubMed:15220349, ECO:0000269|PubMed:15671038, ECO:0000269|PubMed:16106050}.; . TISSUE SPECIFICITY: Abundant in tissues rich in sebaceous glands such as the preputial gland and eyelid. Highly expressed in skin, where it is primarily restricted to undifferentiated peripheral sebocytes. Also expressed at lower level in other tissues except pancreas. {ECO:0000269|PubMed:15220349, ECO:0000269|PubMed:15671038, ECO:0000269|PubMed:16106050}.; uterus;lung;heart;testis;brain;skin; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.03656 0.07074 0.569646743 81.88841708 21.22315 0.71714 AXDND1 1.80353379874149e-15 0.755830161420467 0.244169838579531 axonemal dynein light chain domain containing 1 . . . smooth muscle;testis;colon;kidney;skeletal muscle;stomach; . 0.07633 0.08385 0.606246644 82.93229535 1082.91305 6.31028 AXIN1 0.247772063902675 0.752173394896085 5.45412012401211e-05 axin 1 FUNCTION: Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling. Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt- independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7. Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development. {ECO:0000269|PubMed:12192039, ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17210684}.; DISEASE: Hepatocellular carcinoma (HCC) [MIM:114550]: A primary malignant neoplasm of epithelial liver cells. The major risk factors for HCC are chronic hepatitis B virus (HBV) infection, chronic hepatitis C virus (HCV) infection, prolonged dietary aflatoxin exposure, alcoholic cirrhosis, and cirrhosis due to other causes. {ECO:0000269|PubMed:12101426}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Caudal duplication anomaly (CADUA) [MIM:607864]: A condition characterized by the occurrence of duplications of different organs in the caudal region. {ECO:0000269|PubMed:16773576}. Note=The disease is caused by mutations affecting the gene represented in this entry. Caudal duplication anomaly is associated with hypermethylation of the AXIN1 promoter.; TISSUE SPECIFICITY: Ubiquitously expressed.; ovary;salivary gland;colon;skin;bone marrow;uterus;optic nerve;endometrium;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;blood;skeletal muscle;breast;pancreas;lung;placenta;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;cerebellum peduncles;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.28628 0.09781 -1.431233765 4.016277424 262.11752 3.47434 AXIN2 0.119052193328808 0.880718365556729 0.000229441114462421 axin 2 FUNCTION: Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta- catenin and APC by GSK3B (By similarity). {ECO:0000250}.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:11017067}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Oligodontia-colorectal cancer syndrome (ODCRCS) [MIM:608615]: Affected individuals manifest severe tooth agenesis and colorectal cancer or precancerous lesions of variable types. {ECO:0000269|PubMed:15042511}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain and lymphoblast.; unclassifiable (Anatomical System);lymphoreticular;heart;ovary;colon;parathyroid;skin;breast;uterus;whole body;lung;endometrium;thyroid;placenta;duodenum;liver;testis;spleen;kidney;brain;stomach;cerebellum;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.32472 0.28913 0.321464691 72.85326728 1890.70172 7.99683 AXL 0.76630115087899 0.233698223817305 6.25303704977935e-07 AXL receptor tyrosine kinase FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding growth factor GAS6 and which is thus regulating many physiological processes including cell survival, cell proliferation, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of AXL. Following activation by ligand, ALX binds and induces tyrosine phosphorylation of PI3- kinase subunits PIK3R1, PIK3R2 and PIK3R3; but also GRB2, PLCG1, LCK and PTPN11. Other downstream substrate candidates for AXL are CBL, NCK2, SOCS1 and TNS2. Recruitment of GRB2 and phosphatidylinositol 3 kinase regulatory subunits by AXL leads to the downstream activation of the AKT kinase. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response. {ECO:0000269|PubMed:10403904, ECO:0000269|PubMed:11484958, ECO:0000269|PubMed:12364394, ECO:0000269|PubMed:12490074, ECO:0000269|PubMed:15507525, ECO:0000269|PubMed:15733062, ECO:0000269|PubMed:1656220, ECO:0000269|PubMed:18840707}.; DISEASE: Note=AXL and its ligand GAS6 are highly expressed in thyroid carcinoma tissues, and might thus be involved in thyroid tumorigenesis. Overexpression of AXL and its ligand was also detected in many other cancers such as myeloproliferative disorders, prostatic carcinoma cells, or breast cancer.; TISSUE SPECIFICITY: Highly expressed in metastatic colon tumors. Expressed in primary colon tumors. Weakly expressed in normal colon tissue. {ECO:0000269|PubMed:7896447}.; myocardium;smooth muscle;ovary;skin;retina;prostate;optic nerve;thyroid;iris;amniotic fluid;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;synovium;bone;testis;unclassifiable (Anatomical System);bile duct;pancreas;lung;cornea;mesenchyma;placenta;head and neck;kidney;stomach;aorta; superior cervical ganglion;testis;trigeminal ganglion;skeletal muscle; 0.31627 0.23288 -0.949752638 9.32413305 128.32814 2.46902 AZF1 . . . azoospermia factor 1 . . . . . . . . . . . AZGP1 0.0175975830278723 0.892346785771423 0.0900556312007043 alpha-2-glycoprotein 1, zinc-binding FUNCTION: Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids.; . TISSUE SPECIFICITY: Blood plasma, seminal plasma, urine, saliva, sweat, epithelial cells of various human glands, liver.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;thyroid;bone;iris;testis;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;prostate;fetal liver;pancreas;olfactory bulb;trachea;salivary gland;liver;kidney;atrioventricular node;skin; 0.05989 0.13441 -0.558357437 19.54470394 62.3994 1.61377 AZGP1P1 . . . alpha-2-glycoprotein 1, zinc-binding pseudogene 1 . . . . . . . . . . . AZGP1P2 . . . alpha-2-glycoprotein 1, zinc-binding pseudogene 2 . . . . . . . . . . . AZI2 0.185308909021358 0.812253432240787 0.00243765873785527 5-azacytidine induced 2 FUNCTION: Adapter protein which binds TBK1 and IKBKE playing a role in antiviral innate immunity. Activates serine/threonine- protein kinase TBK1 and facilitates its oligomerization. Enhances the phosphorylation of NF-kappa-B p65 subunit RELA by TBK1. Promotes TBK1-induced as well as TNF-alpha or PMA-induced activation of NF-kappa-B. Participates in IFNB promoter activation via TICAM1. {ECO:0000269|PubMed:14560022, ECO:0000269|PubMed:15611223, ECO:0000269|PubMed:21931631}.; . TISSUE SPECIFICITY: Widely expressed. Abundant expression seen in the pancreas and testis. {ECO:0000269|PubMed:14560022}.; ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;cochlea;thyroid;germinal center;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;atrium;larynx;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; superior cervical ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.47993 0.11092 -0.405853867 26.23260203 14.46843 0.52075 AZIN1 0.991669446644311 0.00832868480701077 1.8685486786619e-06 antizyme inhibitor 1 FUNCTION: Antizyme inhibitor protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake by counteracting the negative effect of antizyme OAZ1, OAZ2 and OAZ3 on ODC1 activity (PubMed:17900240). Inhibits antizyme-dependent ODC degradation by binding to antizymes. Releases ODC1 from its inactive complex with antizymes, leading to formation of the catalytically active ODC1. {ECO:0000269|PubMed:17900240}.; . TISSUE SPECIFICITY: Expressed in liver.; smooth muscle;ovary;sympathetic chain;skin;retina;prostate;endometrium;gum;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;cerebral cortex;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;pia mater;nasopharynx;placenta;hippocampus;head and neck;kidney;aorta;stomach;thymus;cerebellum; amygdala;dorsal root ganglion;occipital lobe;superior cervical ganglion;placenta;globus pallidus;atrioventricular node;pons;parietal lobe;cerebellum; 0.69128 0.11497 -0.359940251 28.93371078 18.95596 0.65447 AZIN1-AS1 . . . AZIN1 antisense RNA 1 . . . . . . . . . . . AZIN2 . . . antizyme inhibitor 2 FUNCTION: Antizyme inhibitor protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake by counteracting the negative effect of antizymes OAZ1, OAZ2 and OAZ3 on ODC1 activity (PubMed:17900240). Inhibits antizyme-dependent ODC1 degradation by binding to antizymes. Releases ODC1 from its inactive complex with antizymes, leading to formation of the catalytically active ODC1. Participates in the morphological integrity of the trans-Golgi network (TGN) and functions as a regulator of intracellular secretory vesicle trafficking (PubMed:20188728). {ECO:0000269|PubMed:14738999, ECO:0000269|PubMed:17900240, ECO:0000269|PubMed:20188728}.; . TISSUE SPECIFICITY: Expressed in the neocortex, thalamus, hippocampus, cerebellum, medulla oblongata, gray and white matter. Expressed in neurons, oligodendrocytes, basket, Purkinje and pyramidal cells. Expressed in spermatocytes and Leydig cells of the testis. Expressed in luteal theca cells lining corpus luteum cysts and in hilus cells of the ovary. Expressed in primary and neoplastic mast cells (MC) (at protein level). Highly expressed in brain. Also expressed in testis. {ECO:0000269|PubMed:11587527, ECO:0000269|PubMed:14738999, ECO:0000269|PubMed:19718454, ECO:0000269|PubMed:19756694, ECO:0000269|PubMed:19832840}.; . . 0.42712 0.32350 7.61E-05 53.98089172 . . AZU1 8.74467686278012e-05 0.544658945038512 0.45525360819286 azurocidin 1 FUNCTION: This is a neutrophil granule-derived antibacterial and monocyte- and fibroblast-specific chemotactic glycoprotein. Binds heparin. The cytotoxic action is limited to many species of Gram- negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. It may play a role in mediating recruitment of monocytes in the second wave of inflammation. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa. Acting alone, it does not have antimicrobial activity against the Gram-negative bacteria A.actinomycetemcomitans ATCC 29532, A.actinomycetemcomitans NCTC 9709, A.actinomycetemcomitans FDC-Y4, H.aphrophilus ATCC 13252, E.corrodens ATCC 23834, C.sputigena ATCC 33123, Capnocytophaga sp ATCC 33124, Capnocytophaga sp ATCC 27872 or E.coli ML-35. Has antibacterial activity against C.sputigena ATCC 33123 when acting synergistically with either elastase or cathepsin G. {ECO:0000269|PubMed:1399008, ECO:0000269|PubMed:1937776, ECO:0000269|PubMed:2312733}.; . . unclassifiable (Anatomical System);uterus;lung;cartilage;heart;bone;spleen;blood;mammary gland;skin;bone marrow; bone marrow; 0.11563 0.40048 0.396906589 76.30927105 208.74623 3.11776 AZU1P1 . . . azurocidin 1 pseudogene 1 . . . . . . . . . . . B2M 0.856561948026764 0.141163861426739 0.002274190546497 beta-2-microglobulin FUNCTION: Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.; DISEASE: Immunodeficiency 43 (IMD43) [MIM:241600]: A disorder characterized by marked reduction in serum concentrations of immunoglobulins and albumin, and hypoproteinemia due to hypercatabolism. Patients may suffer from recurrent respiratory tract infections and severe skin disease. {ECO:0000269|PubMed:16549777}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis. {ECO:0000269|PubMed:7918443}.; . breast;larynx;nasopharynx;hippocampus;pituitary gland;hypopharynx;blood;head and neck;bone marrow; dorsal root ganglion;superior cervical ganglion;salivary gland;white blood cells;skin;bone marrow;prostate;trachea;adrenal gland;placenta;ciliary ganglion;whole blood;trigeminal ganglion;tonsil; 0.14687 0.78296 0.101211609 60.95777306 . . B2MR . . . beta-2-microglobulin regulator . . . . . . . . . . . B3GALNT1 0.248006524456185 0.722533021646685 0.0294604538971299 beta-1,3-N-acetylgalactosaminyltransferase 1 (globoside blood group) FUNCTION: Transfers N-acetylgalactosamine onto globotriaosylceramide. {ECO:0000269|PubMed:10993897}.; . TISSUE SPECIFICITY: Higher expression in heart and brain, and to a lesser extent in lung, placenta, kidney and testis. Lower expression in liver, spleen and stomach. No expression in skeletal muscle. {ECO:0000269|PubMed:10993897, ECO:0000269|PubMed:9582303}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;cerebral cortex;bone;testis;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;lung;visual apparatus;macula lutea;liver;spleen;kidney;mammary gland; amygdala;superior cervical ganglion;pons;trigeminal ganglion; 0.76346 0.17987 -0.249709319 35.74545883 420.04835 4.28180 B3GALNT1P1 . . . beta-1,3-N-acetylgalactosaminyltransferase 1 pseudogene 1 . . . . . . . . . . . B3GALNT2 4.87048529360604e-06 0.961069592722448 0.0389255367922585 beta-1,3-N-acetylgalactosaminyltransferase 2 FUNCTION: Beta-1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAc-beta-1- 3GlcNAc, on N- and O-glycans. Has no galactose nor galactosaminyl transferase activity toward any acceptor substrate. Involved in alpha-dystroglycan (DAG1) glycosylation: acts coordinately with GTDC2/POMGnT2 to synthesize a GalNAc-beta3-GlcNAc-beta-terminus at the 4-position of protein O-mannose in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine- beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan, which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. {ECO:0000269|PubMed:14724282, ECO:0000269|PubMed:23453667, ECO:0000269|PubMed:23929950}.; DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A11 (MDDGA11) [MIM:615181]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with cobblestone lissencephaly and other brain anomalies, eye malformations, profound mental retardation, and death usually in the first years of life. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease. {ECO:0000269|PubMed:23453667}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues examined, but at highest levels in testis, adipose tissue, skeletal muscle and ovary. {ECO:0000269|PubMed:14724282}.; unclassifiable (Anatomical System);prostate;muscle;liver;testis;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.09259 . -0.712684326 14.49634348 134.80463 2.52466 B3GALNT2P1 . . . beta-1,3-N-acetylgalactosaminyltransferase 2 pseudogene 1 . . . . . . . . . . . B3GALT1 0.329724363511517 0.654871716172612 0.0154039203158711 Beta-1,3-galactosyltransferase 1 FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-N- acetylglucosamine (beta-GlcNAc) residue. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. Inactive towards substrates with terminal alpha-N- acetylglucosamine (alpha-GlcNAc) or alpha-N-acetylgalactosamine (alpha-GalNAc) residues. {ECO:0000269|PubMed:9582303}.; . TISSUE SPECIFICITY: Detected in brain and colon mucosa and to a lesser extent in colon adenocarcinoma cells. {ECO:0000269|PubMed:10356986, ECO:0000269|PubMed:9582303}.; unclassifiable (Anatomical System); superior cervical ganglion;trigeminal ganglion;parietal lobe;skeletal muscle; 0.21113 0.14896 -0.227663163 37.11370606 285.54451 3.61854 B3GALT2 0.491100476141356 0.504298907715645 0.00460061614299928 Beta-1,3-galactosyltransferase 2 FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-N- acetylglucosamine (beta-GlcNAc) residue. Can also utilize substrates with a terminal galactose residue, albeit with lower efficiency. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. Inactive towards substrates with terminal alpha-N-acetylglucosamine (alpha-GlcNAc) or alpha-N-acetylgalactosamine (alpha-GalNAc) residues. {ECO:0000269|PubMed:9417100, ECO:0000269|PubMed:9582303}.; . TISSUE SPECIFICITY: Detected in heart and brain. {ECO:0000269|PubMed:9417100, ECO:0000269|PubMed:9582303}.; . . 0.28757 0.11659 -0.271755481 34.31823543 17.96384 0.62796 B3GALT4 0.236708748288266 0.756170249393848 0.00712100231788641 Beta-1,3-galactosyltransferase 4 FUNCTION: Involved in GM1/GD1B/GA1 ganglioside biosynthesis. {ECO:0000269|PubMed:9582303}.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and pancreas and, to a lesser extent, in brain, placenta, kidney, liver and lung. {ECO:0000269|PubMed:10663566, ECO:0000269|PubMed:9582303}.; . . 0.14986 . -0.381986487 27.68931352 15.65048 0.55846 B3GALT5 0.00358396705517524 0.624921039951468 0.371494992993357 Beta-1,3-galactosyltransferase 5 FUNCTION: Catalyzes the transfer of Gal to GlcNAc-based acceptors with a preference for the core3 O-linked glycan GlcNAc(beta1,3)GalNAc structure. Can use glycolipid LC3Cer as an efficient acceptor.; . TISSUE SPECIFICITY: Expressed in stomach, jejunum, colon, pancreas, small intestine, testis and gastrointestinal and pancreatic cancer cell lines. Hardly detected in lung, liver, adrenal gland and peripheral blood leukocytes.; unclassifiable (Anatomical System);frontal lobe;colon; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.08594 0.11493 -0.314027422 31.9297004 33.85455 1.04142 B3GALT5-AS1 . . . B3GALT5 antisense RNA 1 . . TISSUE SPECIFICITY: Ubiquitous.; . . 0.07565 . . . . . B3GALT6 0.0481044658297901 0.682101787079335 0.269793747090875 Beta-1,3-galactosyltransferase 6 FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-linked galactose residue. Has a preference for galactose-beta-1,4-xylose that is found in the linker region of glycosaminoglycans, such as heparan sulfate and chondroitin sulfate. Has no activity towards substrates with terminal glucosamine or galactosamine residues. {ECO:0000269|PubMed:11551958}.; DISEASE: Spondyloepimetaphyseal dysplasia with joint laxity, 1, with or without fractures (SEMDJL1) [MIM:271640]: A bone disease characterized by vertebral abnormalities and ligamentous laxity that result in spinal misalignment and progressive severe kyphoscoliosis, thoracic asymmetry, and respiratory compromise resulting in early death. Additional skeletal features include elbow deformities with radial head dislocation, dislocated hips, clubfeet, and tapered fingers with spatulate distal phalanges. Many affected children have an oval face, flat midface, prominent eyes with blue sclerae, and a long philtrum. Palatal abnormalities and congenital heart disease are also observed. {ECO:0000269|PubMed:23664117, ECO:0000269|PubMed:23664118}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11551958}.; . . 0.15263 . . . 720.15343 5.32791 B3GAT1 0.78915280663019 0.209493114410935 0.00135407895887475 beta-1,3-glucuronyltransferase 1 FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo- orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl- sphingomyelin was the most effective, followed by palmitoyl- sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Mainly expressed in the brain.; unclassifiable (Anatomical System);heart;nervous;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;frontal lobe;macula lutea;visual apparatus;iris;brain; dorsal root ganglion;amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.72670 0.44838 -0.205617011 38.57631517 333.65384 3.88017 B3GAT2 7.03605213348901e-07 0.152116764682781 0.847882531712005 beta-1,3-glucuronyltransferase 2 FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the trachea, retina, spinal cord, hippocampus and other brain regions, and, at lower levels, in testis and ovary.; colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;dura mater;germinal center;brain;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;spinal cord;blood;lens;skeletal muscle;breast;pia mater;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;aorta; . 0.25421 0.16235 -0.029247611 51.40363293 38.08721 1.13182 B3GAT3 0.000286974910106167 0.793216544723748 0.206496480366146 beta-1,3-glucuronyltransferase 3 FUNCTION: Glycosaminoglycans biosynthesis. Involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. Transfers a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans. Can also play a role in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins. Shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc. Stimulates 2-phosphoxylose phosphatase activity of PXYLP1 in presence of uridine diphosphate-glucuronic acid (UDP- GlcUA) during completion of linkage region formation. {ECO:0000269|PubMed:24425863}.; DISEASE: Multiple joint dislocations short stature craniofacial dysmorphism and congenital heart defects (JDSSDHD) [MIM:245600]: An autosomal recessive disease characterized by dysmorphic facies, bilateral dislocations of the elbows, hips, and knees, clubfeet, and short stature, as well as cardiovascular defects. {ECO:0000269|PubMed:21763480}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous (but weakly expressed in all tissues examined).; lymphoreticular;medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;endometrium;larynx;iris;brain;tonsil;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;hypothalamus;blood;lens;breast;pancreas;lung;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;stomach;thymus; whole brain;superior cervical ganglion;prefrontal cortex;trigeminal ganglion; 0.24819 0.13137 -0.203796826 38.81811748 71.71337 1.76280 B3GAT3P1 . . . beta-1,3-glucuronyltransferase 3 pseudogene 1 . . . . . . . . . . . B3GLCT . . . beta 3-glucosyltransferase FUNCTION: O-glucosyltransferase that transfers glucose toward fucose with a beta-1,3 linkage. Specifically glucosylates O-linked fucosylglycan on TSP type-1 domains of proteins, thereby contributing to elongation of O-fucosylglycan. {ECO:0000269|PubMed:16899492}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in testis and uterus. {ECO:0000269|PubMed:12943678, ECO:0000269|PubMed:16899492}.; . . 0.22185 0.13753 0.066214104 58.95848077 . . B3GNT2 0.696953713886218 0.299190352364985 0.00385593374879655 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Catalyzes the initiation and elongation of poly-N-acetyllactosamine chains. Shows a marked preference for Gal(beta1-4)Glc(NAc)-based acceptors (PubMed:9892646). Probably constitutes the main polylactosamine synthase. {ECO:0000269|PubMed:11042166, ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:9892646}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11042166}.; lymphoreticular;ovary;colon;parathyroid;vein;skin;retina;uterus;whole body;endometrium;bone;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;tongue;islets of Langerhans;hypothalamus;blood;pancreas;adrenal gland;placenta;hippocampus;liver;spleen;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; . 0.12321 -0.071520315 48.34866714 25.32515 0.82776 B3GNT2P1 . . . UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 pseudogene 1 . . . . . . . . . . . B3GNT3 0.200971950070002 0.754720585208315 0.0443074647216834 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3 FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Has activity for type 2 oligosaccharides (PubMed:11042166). Also acts as a core1-1,3-N- acetylglucosaminyltransferase (Core1-beta3GlcNAcT) to form the 6- sulfo sialyl Lewis x on extended core1 O-glycans (PubMed:11439191). {ECO:0000269|PubMed:11042166, ECO:0000269|PubMed:11439191}.; . TISSUE SPECIFICITY: Expressed in colon, jejunum, stomach, esophagus, placenta and trachea. {ECO:0000269|PubMed:11042166}.; unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;colon;parathyroid;skeletal muscle;uterus;prostate;lung;placenta;visual apparatus;hypopharynx;liver;head and neck;spleen;cervix;stomach; occipital lobe;superior cervical ganglion;placenta;cingulate cortex; 0.10141 0.11146 0.52918614 80.81505072 160.13043 2.76216 B3GNT4 3.93670006882859e-06 0.211432380902185 0.788563682397746 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 4 FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Has activity for type 2 oligosaccharides. {ECO:0000269|PubMed:11042166}.; . TISSUE SPECIFICITY: Mainly expressed in brain tissues such as whole brain, hippocampus, amygdala, cerebellum and caudate nucleus. Also expressed in colon, esophagus and kidney. {ECO:0000269|PubMed:11042166}.; unclassifiable (Anatomical System);pancreas;lung;endometrium;bone;kidney;brain; atrioventricular node;trigeminal ganglion; 0.13967 0.15291 1.065596954 91.61358811 2964.63752 10.31970 B3GNT5 0.630704047253903 0.362206568999003 0.00708938374709359 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5 FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase that plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids, notably by participating in biosynthesis of HNK-1 and Lewis X carbohydrate structures. Has strong activity toward lactosylceramide (LacCer) and neolactotetraosylceramide (nLc(4)Cer; paragloboside), resulting in the synthesis of Lc(3)Cer and neolactopentaosylceramide (nLc(5)Cer), respectively. Probably plays a central role in regulating neolacto-series glycolipid synthesis during embryonic development.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in lung, colon, placenta, testis, pituitary gland and cerebellum. Weakly expressed in brain, liver, spleen, lymph node and thymus. {ECO:0000269|PubMed:11283017}.; ovary;sympathetic chain;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;tongue;islets of Langerhans;adrenal cortex;blood;skeletal muscle;bile duct;breast;lung;adrenal gland;trabecular meshwork;placenta;liver;hypopharynx;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10301 0.12230 0.038710339 56.92380278 51.47262 1.41644 B3GNT6 2.42261009335967e-06 0.162765317187021 0.837232260202885 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 6 FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase that synthesizes the core 3 structure of the O-glycan, an important precursor in the biosynthesis of mucin-type glycoproteins. Plays an important role in the synthesis of mucin-type O-glycans in digestive organs.; . TISSUE SPECIFICITY: Present in stomach and colon (at protein level). Restricted in the stomach, colon and small intestine, where core 3 structure is present. {ECO:0000269|PubMed:15755813}.; cervix;skeletal muscle; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . . . . 3333.98191 11.05216 B3GNT7 0.620845260079446 0.371444381099349 0.00771035882120539 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 7 FUNCTION: May be involved in keratane sulfate biosynthesis. Transfers N-acetylgalactosamine on to keratan sulfate-related glycans. May play a role in preventing cells from migrating out of the original tissues and invading surrounding tissues. {ECO:0000269|PubMed:12061784}.; . . unclassifiable (Anatomical System); atrioventricular node; 0.43158 0.10472 -0.045835247 50.34206181 1722.7167 7.65891 B3GNT8 3.49055727461861e-07 0.190278434274967 0.809721216669306 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 8 FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase that plays a role in the elongation of specific branch structures of multiantennary N-glycans. Has strong activity towards tetraantennary N-glycans and 2,6 triantennary glycans. {ECO:0000269|PubMed:15620693, ECO:0000269|PubMed:15917431}.; . TISSUE SPECIFICITY: Highly expressed in small intestine, pancreas, spleen, bone marrow, lung, throat, and ileum, and weakly in fetal brain, cerebellum, heart, liver, tongue, breast, uteri, and testis. Not detected in colon. Differentially expressed in human tumor cell lines. {ECO:0000269|PubMed:15486459, ECO:0000269|PubMed:15620693}.; unclassifiable (Anatomical System);optic nerve;cartilage;nervous;bone;macula lutea;colon;blood;fovea centralis;choroid;lens;brain;retina;bone marrow; . 0.11717 . 0.733063566 86.27034678 106.70344 2.24179 B3GNT9 0.0228246541729955 0.765973700995524 0.211201644831481 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 9 . . . . . . . . . 26.74653 0.86581 B3GNTL1 2.14222358700744e-11 0.0655000159889588 0.934499983989619 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like 1 FUNCTION: Putative glycosyltransferase. {ECO:0000305}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;blood;pancreas;lung;placenta;macula lutea;visual apparatus;spleen;cervix;kidney;mammary gland; superior cervical ganglion;atrioventricular node;skeletal muscle;parietal lobe; 0.15779 0.10445 0.113945049 62.14319415 2466.85643 9.25275 B3GNTL1P1 . . . UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like 1 pseudogene 1 . . . . . . . . . . . B3GNTL1P2 . . . UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like 1 pseudogene 2 . . . . . . . . . . . B4GALNT1 0.0560737731652395 0.94000893929846 0.00391728753630009 beta-1,4-N-acetyl-galactosaminyltransferase 1 FUNCTION: Involved in the biosynthesis of gangliosides GM2, GD2 and GA2.; DISEASE: Spastic paraplegia 26, autosomal recessive (SPG26) [MIM:609195]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG26 is a complicated form characterized by onset in the first 2 decades of life of gait abnormalities due to lower limb spasticity and muscle weakness. Some patients have upper limb involvement. Additional features include intellectual disability, peripheral neuropathy, dysarthria, cerebellar signs, extrapyramidal signs, and cortical atrophy. The disorder is slowly progressive. {ECO:0000269|PubMed:23746551}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);muscle;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;pancreas;prostate;optic nerve;whole body;lung;frontal lobe;endometrium;bone;macula lutea;hippocampus;liver;testis;cervix;brain; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.12226 0.24746 0.264628794 70.5178108 1155.97829 6.47674 B4GALNT2 9.64033158743695e-07 0.768740675707458 0.231258360259384 beta-1,4-N-acetyl-galactosaminyltransferase 2 FUNCTION: Involved in the synthesis of the Sd(a) antigen (Sia- alpha2,3-[GalNAc-beta1,4]Gal-beta1,4-GlcNAc), a carbohydrate determinant expressed on erythrocytes, the colonic mucosa and other tissues. Transfers a beta-1,4-linked GalNAc to the galactose residue of an alpha-2,3-sialylated chain. {ECO:0000269|PubMed:12678917, ECO:0000269|PubMed:14688233}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in colon and to a lesser extent in kidney, stomach, ileum and rectum. {ECO:0000269|PubMed:12678917}.; heart; superior cervical ganglion;globus pallidus;ciliary ganglion; 0.05778 0.28364 0.802845857 87.69167256 3125.19031 10.63438 B4GALNT2P1 . . . beta-1,4-N-acetyl-galactosaminyltransferase 2 pseudogene 1 . . . . . . . . . . . B4GALNT3 1.06179854846531e-07 0.999285881101964 0.000714012718180677 beta-1,4-N-acetyl-galactosaminyltransferase 3 FUNCTION: Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked glycans and probably O-linked glycans. Mediates the N,N'- diacetyllactosediamine formation on gastric mucosa. {ECO:0000269|PubMed:16728562}.; . TISSUE SPECIFICITY: Highly expressed in testis, colon and stomach. Weakly expressed in other tissues. {ECO:0000269|PubMed:12966086}.; unclassifiable (Anatomical System);medulla oblongata;heart;colon;skeletal muscle;uterus;whole body;lung;frontal lobe;endometrium;placenta;hypopharynx;testis;head and neck;brain;stomach; whole brain;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19181 0.10323 0.483089098 79.05166313 5053.46764 14.55634 B4GALNT4 0.816930490785275 0.183069194512396 3.14702329353592e-07 beta-1,4-N-acetyl-galactosaminyltransferase 4 FUNCTION: Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked glycans and probably O-linked glycans.; . TISSUE SPECIFICITY: Highly expressed in ovary, adult and fetal brain. Also expressed in fetal kidney and lung. {ECO:0000269|PubMed:15044014}.; unclassifiable (Anatomical System);lymph node;heart;ovary;developmental;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;placenta;macula lutea;liver;testis;brain;mammary gland; amygdala;occipital lobe;medulla oblongata;prefrontal cortex;globus pallidus;caudate nucleus; 0.13468 0.09235 . . 1517.92316 7.24180 B4GALT1 0.486324787710792 0.508905105119333 0.00477010716987471 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1 FUNCTION: The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.; DISEASE: Congenital disorder of glycosylation 2D (CDG2D) [MIM:607091]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:11901181}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed, but at very low levels in fetal and adult brain.; . . 0.60852 0.20954 -0.516085732 21.20193442 50.29547 1.39434 B4GALT1-AS1 . . . B4GALT1 antisense RNA 1 . . . . . . . . . . . B4GALT2 0.295417380860886 0.700285652011272 0.00429696712784149 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 2 FUNCTION: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Can produce lactose.; . TISSUE SPECIFICITY: Weakly expressed in various tissues. Highest expression in prostate, testis, ovary, intestine, muscle, and in fetal brain.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;oesophagus;larynx;bone;thyroid;iris;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;occipital lobe;medulla oblongata;temporal lobe;ciliary ganglion;pons;trigeminal ganglion;parietal lobe; 0.06365 0.10739 -0.358119787 29.16371786 600.31031 4.95931 B4GALT3 0.0208228744149612 0.975578897416981 0.00359822816805782 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 3 FUNCTION: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.; . TISSUE SPECIFICITY: Found in various tissues. Highest expression in placenta, prostate, testis, ovary, intestine and muscle, and in fetal brain.; myocardium;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;urinary;adrenal cortex;blood;skeletal muscle;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;alveolus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;placenta;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.30605 0.12043 -0.159704656 41.90846898 59.97959 1.57211 B4GALT4 2.32860130735228e-06 0.484033688397015 0.515963983001678 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 4 FUNCTION: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. {ECO:0000269|PubMed:9792633}.; . TISSUE SPECIFICITY: High expression in heart, placenta, kidney and pancreas; lower in brain, colon, lung, muscle, ovary, testis and uterus.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle;skin; 0.50050 0.12469 0.260991686 70.25831564 1296.95673 6.77905 B4GALT4-AS1 . . . B4GALT4 antisense RNA 1 . . . . . . . . . . . B4GALT5 0.991657870655178 0.00834025443583348 1.87490898804645e-06 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 5 FUNCTION: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. {ECO:0000269|PubMed:9435216}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9435216}.; . . 0.28395 0.13952 0.194852702 67.03231894 659.94619 5.15059 B4GALT6 0.995466887687435 0.00453269010556743 4.22206997419764e-07 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 6 FUNCTION: Required for the biosynthesis of glycosphingolipids. {ECO:0000269|PubMed:1551920, ECO:0000269|PubMed:3099851}.; . TISSUE SPECIFICITY: High expression in brain and adrenal gland, lower in liver, lung, colon and peripheral white blood cells.; unclassifiable (Anatomical System);ovary;salivary gland;pharynx;colon;blood;retina;bone marrow;breast;pancreas;prostate;lung;frontal lobe;visual apparatus;liver;testis;cervix;kidney;brain;bladder; superior cervical ganglion;occipital lobe;appendix;atrioventricular node;trigeminal ganglion;skin;cerebellum; 0.61409 0.26694 0.194852702 67.03231894 147.53428 2.64669 B4GALT7 0.00319749562629115 0.823421757117217 0.173380747256492 xylosylprotein beta 1,4-galactosyltransferase, polypeptide 7 FUNCTION: Required for the biosynthesis of the tetrasaccharide linkage region of proteoglycans, especially for small proteoglycans in skin fibroblasts. {ECO:0000269|PubMed:24052259}.; . TISSUE SPECIFICITY: High expression in heart, pancreas and liver, medium in placenta and kidney, low in brain, skeletal muscle and lung.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;pineal body;pharynx;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node; 0.27929 0.11796 -0.734731259 14.01863647 51.619 1.41797 B4GAT1 . . . beta-1,4-glucuronyltransferase 1 FUNCTION: Beta-1,4-glucuronyltransferase involved in O- mannosylation of alpha-dystroglycan (DAG1). Transfers a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose-beta disaccharide primer, which is further elongated by LARGE, during synthesis of phosphorylated O- mannosyl glycan (PubMed:25279699, PubMed:25279697). Phosphorylated O-mannosyl glycan is a carbohydrate is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (PubMed:25279699, PubMed:25279697). Required for axon guidance; via its function in O-mannosylation of alpha- dystroglycan (DAG1) (By similarity). {ECO:0000250|UniProtKB:Q8BWP8, ECO:0000269|PubMed:19587235, ECO:0000269|PubMed:23359570, ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699}.; . TISSUE SPECIFICITY: In the adult, highly expressed in heart, brain, skeletal muscle and kidney and to a lesser extent in placenta, pancreas, spleen, prostate, testis, ovary, small intestine and colon. Very weak expression in lung, liver, thymus and peripheral blood leukocytes. In fetal highly expressed in brain and kidney and to a lesser extent in lung and liver. {ECO:0000269|PubMed:9405606}.; . . . 0.12321 -0.273576253 33.97027601 . . B9D1 0.119139655847397 0.855113258212041 0.0257470859405617 B9 protein domain 1 FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling (By similarity). {ECO:0000250}.; DISEASE: Meckel syndrome 9 (MKS9) [MIM:614209]: A disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly. {ECO:0000269|PubMed:21493627}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;lens;skeletal muscle;lung;epididymis;placenta;macula lutea;liver;kidney;stomach; subthalamic nucleus;superior cervical ganglion;testis - interstitial;heart;testis - seminiferous tubule;liver;testis;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10045 . -0.139478553 43.29440906 2644.99446 9.64579 B9D2 0.000844599441510728 0.553518239352052 0.445637161206437 B9 protein domain 2 FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. {ECO:0000269|PubMed:21763481}.; DISEASE: Meckel syndrome 10 (MKS10) [MIM:614175]: A disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly. {ECO:0000269|PubMed:21763481}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;lens;pancreas;lung;placenta;macula lutea;liver;alveolus;spleen;kidney;stomach; . 0.14199 0.13270 -0.117432389 44.89266336 16.31191 0.57795 BAALC 5.01827896369176e-05 0.250067344605417 0.749882472604947 brain and acute leukemia, cytoplasmic FUNCTION: May play a synaptic role at the postsynaptic lipid rafts by interacting with CAMK2A. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed by neural and hematopoietic cells. Expression is found both in normal early progenitor cells and in the most immature type of blasts in acute leukemia but not in mature hematopoietic cells. Isoform 2 and isoform 6 are expressed in the brain. Isoform 2 shows a low expression in neuroectoderm- derived tissues such as adrenal gland and no expression in bone marrow, peripheral blood lymphocytes or lymph nodes, or in tumors or cancer cell lines of nonneural tissue origin. {ECO:0000269|PubMed:11707601}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;optic nerve;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;cerebellum cortex;islets of Langerhans;hypothalamus;adrenal cortex;lens;lung;placenta;macula lutea;hippocampus;visual apparatus;spleen;kidney; whole brain;amygdala;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.02356 0.06078 . . 182.38421 2.93327 BAALC-AS1 . . . BAALC antisense RNA 1 . . . . . . . . . . . BAALC-AS2 . . . BAALC antisense RNA 2 . . . . . . . . . . . BAAT 7.96375042041763e-06 0.508361400928261 0.491630635321319 bile acid-CoA:amino acid N-acyltransferase FUNCTION: Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs. {ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:8034703}.; . TISSUE SPECIFICITY: Expressed in liver, gallbladder mucosa and pancreas. {ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:2037576}.; unclassifiable (Anatomical System);heart;liver;spleen;skin; superior cervical ganglion;heart;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04469 0.10577 0.707379532 85.62750649 45.87208 1.30226 BAATP1 . . . bile acid-CoA: amino acid N-acyltransferase pseudogene 1 . . . . . . . . . . . BABAM1 0.729375765332217 0.267865060387773 0.00275917428001052 BRISC and BRCA1 A complex member 1 FUNCTION: Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys- 63'-linked ubiquitin in various substrates (PubMed:24075985, PubMed:26195665). In these 2 complexes, it is probably required to maintain the stability of BRE/BRCC45 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1 (PubMed:26195665). Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (PubMed:24075985). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985). {ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;oesophagus;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;muscle;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; whole brain;globus pallidus; 0.10671 0.10867 -0.315847836 31.68789809 38.74926 1.14712 BACE1 0.944278809144277 0.0557127826570294 8.40819869321655e-06 beta-site APP-cleaving enzyme 1 FUNCTION: Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. {ECO:0000269|PubMed:10677483, ECO:0000269|PubMed:20354142}.; . TISSUE SPECIFICITY: Expressed at high levels in the brain and pancreas. In the brain, expression is highest in the substantia nigra, locus coruleus and medulla oblongata. {ECO:0000269|PubMed:10677483, ECO:0000269|PubMed:11083922}.; myocardium;medulla oblongata;umbilical cord;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; medulla oblongata;thalamus;occipital lobe;hypothalamus;spinal cord;globus pallidus;caudate nucleus;pons;parietal lobe; 0.32571 0.32145 -0.758599262 13.32861524 36.43549 1.09195 BACE1-AS . . . BACE1 antisense RNA . . . . . . . . . . . BACE2 0.952644808591658 0.0473276137981541 2.75776101880006e-05 beta-site APP-cleaving enzyme 2 FUNCTION: Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves APP, between residues 690 and 691, leading to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C- terminal fragment which is later released by gamma-secretase. It has also been shown that it can cleave APP between residues 671 and 672. {ECO:0000269|PubMed:10591213, ECO:0000269|PubMed:11083922, ECO:0000269|PubMed:11423558, ECO:0000269|PubMed:15857888, ECO:0000269|PubMed:16816112}.; . TISSUE SPECIFICITY: Brain. Present in neurons within the hippocampus, frontal cortex and temporal cortex (at protein level). Expressed at low levels in most peripheral tissues and at higher levels in colon, kidney, pancreas, placenta, prostate, stomach and trachea. Expressed at low levels in the brain. Found in spinal cord, medulla oblongata, substantia nigra and locus coruleus. Expressed in the ductal epithelium of both normal and malignant prostate. {ECO:0000269|PubMed:10591213, ECO:0000269|PubMed:10677483, ECO:0000269|PubMed:10683441, ECO:0000269|PubMed:10749877, ECO:0000269|PubMed:10838186, ECO:0000269|PubMed:10965118, ECO:0000269|PubMed:11083922}.; myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;larynx;bone;thyroid;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;blood;lens;skeletal muscle;breast;pancreas;pia mater;lung;cornea;adrenal gland;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion; 0.24187 0.35536 -0.358119787 29.16371786 23.71112 0.78418 BACE2-IT1 . . . BACE2 intronic transcript 1 . . . . . . . . . . . BACH1 0.01418640000584 0.979509119854133 0.00630448014002652 BTB domain and CNC homolog 1 FUNCTION: Transcriptional regulator that acts as repressor or activator. Binds, in vitro, to NF-E2 binding sites. Play important roles in coordinating transcription activation and repression by MAFK.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;mesenchyma;placenta;hypopharynx;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;testis - interstitial;ciliary ganglion;atrioventricular node;whole blood;trigeminal ganglion; 0.79735 0.12879 -0.33061537 30.82094834 185.3439 2.95733 BACH1-AS1 . . . BACH1 antisense RNA 1 . . . . . . . . . . . BACH1-IT1 . . . BACH1 intronic transcript 1 . . . . . . . . . . . BACH1-IT2 . . . BACH1 intronic transcript 2 . . . . . . . . . . . BACH1-IT3 . . . BACH1 intronic transcript 3 . . . . . . . . . . . BACH2 0.874039851139597 0.125891712208917 6.84366514861527e-05 BTB domain and CNC homolog 2 FUNCTION: Transcriptional regulator that acts as repressor or activator. Binds to Maf recognition elements (MARE). Play important roles in coordinating transcription activation and repression by MAFK (By similarity). Induces apoptosis in response to oxidative stress through repression of the antiapoptotic factor HMOX1. {ECO:0000250, ECO:0000269|PubMed:17018862}.; . TISSUE SPECIFICITY: B-cell specific.; ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen; dorsal root ganglion;superior cervical ganglion;fetal brain;adrenal cortex;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.96608 0.17631 -0.617221851 17.44515216 137.00389 2.54456 BAD 0.000414578843999332 0.408595665462622 0.590989755693379 BCL2 associated agonist of cell death FUNCTION: Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in a wide variety of tissues.; medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; whole brain;dorsal root ganglion;superior cervical ganglion;liver;globus pallidus; 0.18488 0.53379 -0.317668748 31.45789101 10.31085 0.37599 BAG1 . . . BCL2 associated athanogene 1 FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli. {ECO:0000269|PubMed:12724406, ECO:0000269|PubMed:9305631, ECO:0000269|PubMed:9873016}.; . TISSUE SPECIFICITY: Isoform 4 is the most abundantly expressed isoform. It is ubiquitously expressed throughout most tissues, except the liver, colon, breast and uterine myometrium. Isoform 1 is expressed in the ovary and testis. Isoform 4 is expressed in several types of tumor cell lines, and at consistently high levels in leukemia and lymphoma cell lines. Isoform 1 is expressed in the prostate, breast and leukemia cell lines. Isoform 3 is the least abundant isoform in tumor cell lines (at protein level). {ECO:0000269|PubMed:9679980}.; . . 0.26684 0.43483 -0.049474214 50.01179523 181.92309 2.92934 BAG2 0.0883361376691997 0.763371149946406 0.148292712384394 BCL2 associated athanogene 2 FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release.; . . . . 0.23206 0.17302 -0.075159878 47.78839349 11.50072 0.41466 BAG3 0.53203443022702 0.467276403589878 0.00068916618310187 BCL2 associated athanogene 3 FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity.; DISEASE: Myopathy, myofibrillar, 6 (MFM6) [MIM:612954]: A neuromuscular disorder that results in early-onset, severe, progressive, diffuse muscle weakness associated with cardiomyopathy, severe respiratory insufficiency during adolescence, and a rigid spine in some patients. At ultrastructural level, muscle fibers display structural alterations consisting of replacement of the normal myofibrillar markings by small, dense granules, or larger hyaline masses, or amorphous material. {ECO:0000269|PubMed:19085932, ECO:0000269|PubMed:21361913}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1HH (CMD1HH) [MIM:613881]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:21353195, ECO:0000269|PubMed:21459883, ECO:0000269|PubMed:21898660}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.59120 0.21092 0.113945049 62.14319415 2633.8734 9.62741 BAG4 0.0237409026699778 0.962022234600091 0.014236862729931 BCL2 associated athanogene 4 FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release (By similarity). Prevents constitutive TNFRSF1A signaling. Negative regulator of PARK2 translocation to damaged mitochondria. {ECO:0000250, ECO:0000269|PubMed:24270810}.; . TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;urinary;blood;lens;placenta;macula lutea;visual apparatus;liver;duodenum;hypopharynx;alveolus;spleen;head and neck;cervix;kidney; superior cervical ganglion; 0.25912 0.15318 -0.049474214 50.01179523 53.58492 1.45631 BAG5 0.0432181879837962 0.92941132177904 0.0273704902371636 BCL2 associated athanogene 5 FUNCTION: Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 (By similarity). May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. {ECO:0000250, ECO:0000269|PubMed:20223214}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;medulla oblongata;testis - interstitial;prefrontal cortex;testis;globus pallidus;ciliary ganglion; 0.34694 0.20397 -0.069700724 48.54328851 39.74206 1.17119 BAG6 0.999987885791662 1.21142083284766e-05 9.27568929752214e-15 BCL2 associated athanogene 6 FUNCTION: Chaperone that plays a key role in various processes such as apoptosis, insertion of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane and regulation of chromatin. Key component of the BAG6/BAT3 complex, a cytosolic multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. BAG6/BAT3 acts by facilitating TA membrane proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins and transfers them to ASNA1/TRC40 for targeting to the endoplasmic reticulum membrane. Moreover, it regulates the stability and the degradation of proteins by the proteasome. For instance, it is required for selective ubiquitin- mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, may play a role in immuno- proteasomes to generate antigenic peptides via targeted degradation, thereby playing a role in antigen presentation in immune response. It is also involved in ubiquitin-mediated proteasomal degradation of proteins of the secretory pathway that are mislocalized to the cytosol. Binds the mislocalized proteins, preventing their aggregation in the cytosol, and promotes their ubiquitination. Participates in endoplasmic reticulum stress- induced apoptosis via its interaction with AIFM1/AIF by regulating AIFM1/AIF stability and preventing its degradation. Also required during spermatogenesis for synaptonemal complex assembly via its interaction with HSPA2, by inhibiting polyubiquitination and subsequent proteasomal degradation of HSPA2. {ECO:0000269|PubMed:14960581, ECO:0000269|PubMed:20516149, ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:24981174}.; FUNCTION: Can be released from tumor and dendritic cells in membrane vesicles or exosomes, and engage NCR3 thereby promoting natural killer cells (NK) activation and cytotoxicity. {ECO:0000269|PubMed:18055229, ECO:0000269|PubMed:18852879}.; . . lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; . 0.56416 . -1.394367777 4.246284501 116.8306 2.35182 BAGE . . . B melanoma antigen FUNCTION: Unknown. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes.; . TISSUE SPECIFICITY: Not expressed in normal tissues, except in testis. Expressed with significant proportion in melanomas, but also in tumors of various histological origins, such as bladder carcinomas, head and neck squamous cell carcinomas, lung and breast carcinomas. Not expressed in renal, colorectal and prostatic carcinomas, leukemias and lymphomas. More frequently expressed in metastatic melanomas than in primary melanomas.; . . . . . . . . BAGE2 . . . B melanoma antigen family member 2 FUNCTION: Unknown. Candidate gene encoding tumor antigens.; . TISSUE SPECIFICITY: Not expressed in normal tissues except in testis. Expressed in 22% of melanomas, in bladder and lung carcinomas.; . . . . . . . . BAGE3 . . . B melanoma antigen family member 3 FUNCTION: Unknown. Candidate gene encoding tumor antigens.; . TISSUE SPECIFICITY: Not expressed in normal tissues except in testis. Expressed in melanoma, bladder and lung carcinomas.; . . . . . . . . BAGE4 . . . B melanoma antigen family member 4 FUNCTION: Unknown. Candidate gene encoding tumor antigens.; . TISSUE SPECIFICITY: Not expressed in normal tissues except in testis. Expressed in melanoma, bladder and lung carcinomas.; . . . . . . . . BAGE5 . . . B melanoma antigen family member 5 FUNCTION: Unknown. Candidate gene encoding tumor antigens.; . TISSUE SPECIFICITY: Not expressed in normal tissues except in testis. Expressed in melanoma, bladder and lung carcinomas.; . . . . . . . . BAHCC1 . . . BAH domain and coiled-coil containing 1 . . . unclassifiable (Anatomical System);uterus;lung;ovary;heart;testis;brain;skin;thymus;bone marrow; . 0.35312 . . . . . BAHD1 0.991930031952242 0.00806989723168626 7.08160716158558e-08 bromo adjacent homology domain containing 1 FUNCTION: Heterochromatin protein that acts as a transcription repressor and has the ability to promote the formation of large heterochromatic domains. May act by recruiting heterochromatin proteins such as CBX5 (HP1 alpha), HDAC5 and MBD1. Represses IGF2 expression by binding to its CpG-rich P3 promoter and recruiting heterochromatin proteins. At specific stages of Listeria infection, in complex with TRIM28, corepresses interferon- stimulated genes, including IFNL1, IFNL2 and IFNL3. {ECO:0000269|PubMed:19666599, ECO:0000269|PubMed:21252314}.; . . . . 0.18499 0.10583 -0.927704399 9.719273414 580.11257 4.88277 BAIAP2 0.464202488604374 0.535561055938733 0.000236455456893393 BAI1 associated protein 2 FUNCTION: Adapter protein that links membrane-bound small G- proteins to cytoplasmic effector proteins. Necessary for CDC42- mediated reorganization of the actin cytoskeleton and for RAC1- mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. Participates in actin bundling when associated with EPS8, promoting filopodial protrusions. {ECO:0000269|PubMed:11130076, ECO:0000269|PubMed:11696321, ECO:0000269|PubMed:14752106, ECO:0000269|PubMed:17115031, ECO:0000269|PubMed:19366662}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 4 are expressed almost exclusively in brain. Isoform 4 is barely detectable in placenta, prostate and testis. A short isoform is ubiquitous, with the highest expression in liver, prostate, testis and placenta. {ECO:0000269|PubMed:10332026, ECO:0000269|PubMed:10343108, ECO:0000269|PubMed:11157984}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;bone;iris;testis;spinal ganglion;brain;amygdala;unclassifiable (Anatomical System);heart;cartilage;nervous;islets of Langerhans;hypothalamus;pharynx;blood;lens;bile duct;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; amygdala;dorsal root ganglion;whole brain;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;atrioventricular node;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;liver;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.14294 0.16015 -1.39618256 4.222694032 17.45132 0.61233 BAIAP2-AS1 . . . BAIAP2 antisense RNA 1 (head to head) . . . . . . . . . . . BAIAP2L1 0.042773725631072 0.956979145036324 0.000247129332603702 BAI1 associated protein 2 like 1 FUNCTION: May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. {ECO:0000269|PubMed:17430976, ECO:0000269|PubMed:19366662, ECO:0000269|PubMed:22921828}.; . . . . 0.11587 0.12001 -0.552898813 19.86317528 136.18478 2.53619 BAIAP2L2 0.000100357855733205 0.941833474208361 0.0580661679359053 BAI1 associated protein 2 like 2 FUNCTION: Phosphoinositides-binding protein that induces the formation of planar or gently curved membrane structures. Binds to phosphoinositides, including to phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2) headgroups. There seems to be no clear preference for a specific phosphoinositide (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the epithelial layer of the intestine (at protein level). {ECO:0000269|PubMed:21743456}.; unclassifiable (Anatomical System);colon;kidney;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13163 . -0.448125345 24.19202642 7043.00826 17.91637 BAIAP3 2.20929624637849e-19 0.0884880307169486 0.911511969283051 BAI1 associated protein 3 . . TISSUE SPECIFICITY: Predominantly expressed in brain. {ECO:0000269|PubMed:9790924}.; ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;hypothalamus;lens;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;spleen;kidney;mammary gland;stomach;aorta; amygdala;occipital lobe;subthalamic nucleus;thalamus;hypothalamus;temporal lobe;spinal cord;prefrontal cortex;globus pallidus;pons;cingulate cortex;pituitary;parietal lobe; 0.29593 0.09988 -2.150176731 1.468506723 719.07294 5.32413 BAK1 0.00348654810029572 0.83711563795003 0.159397813949675 BCL2 antagonist/killer 1 FUNCTION: In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti- apoptotic action of BCL2 or its adenovirus homolog E1B 19k protein. Low micromolar levels of zinc ions inhibit the promotion of apoptosis. {ECO:0000269|PubMed:17157251, ECO:0000269|PubMed:8521816}.; . TISSUE SPECIFICITY: Expressed in a wide variety of tissues, with highest levels in the heart and skeletal muscle.; unclassifiable (Anatomical System);uterus;bile duct;lymphoreticular;lung;liver;cervix;germinal center;brain;bladder;skin;stomach; superior cervical ganglion; . 0.41698 -0.317668748 31.45789101 54.85267 1.48435 BAK1P1 . . . BCL2 antagonist/killer 1 pseudogene 1 . . . . . . 0.41698 . . . . BAK1P2 . . . BCL2 antagonist/killer 1 pseudogene 2 . . . . . . . . . . . BAMBI 0.00217665588048022 0.754450452471375 0.243372891648145 BMP and activin membrane-bound inhibitor FUNCTION: Negatively regulates TGF-beta signaling.; . TISSUE SPECIFICITY: High expression in kidney medulla, placenta and spleen; low in kidney cortex, liver, prostate and gut. Not expressed in normal skin, expression is high in melanocytes and in 3 out of 11 melanoma metastases tested.; . . 0.11857 0.28082 -0.115612493 45.12856806 62.22057 1.60894 BANCR . . . BRAF-activated non-protein coding RNA . . . . . . . . . . . BANF1 0.739287243394207 0.249466809931527 0.0112459466742663 barrier to autointegration factor 1 FUNCTION: Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging. Exploited by retroviruses for inhibiting self- destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. {ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:16680152}.; DISEASE: Nestor-Guillermo progeria syndrome (NGPS) [MIM:614008]: An atypical progeroid syndrome characterized by normal development in the first years of life, later followed by the emergence of generalized lipoatrophy, severe osteoporosis, and marked osteolysis. The atrophic facial subcutaneous fat pad and the marked osteolysis of the maxilla and mandible result in a typical pseudosenile facial appearance with micrognathia, prominent subcutaneous venous patterning, a convex nasal ridge, and proptosis. Cognitive development is completely normal. Patients do not have cardiovascular dysfunction, atherosclerosis, or metabolic anomalies. {ECO:0000269|PubMed:21549337}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Expressed in colon, brain, heart, kidney, liver, lung, ovary, pancreas, placenta, prostate, skeletal muscle, small intestine, spleen and testis. Not detected in thymus and peripheral blood leukocytes.; myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;heart;tongue;nervous;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;larynx;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;trophoblast;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; . 0.08396 0.37501 -0.009020804 52.8544468 1.20345 0.03635 BANF1P1 . . . barrier to autointegration factor 1 pseudogene 1 . . . . . . . . . . . BANF1P2 . . . barrier to autointegration factor 1 pseudogene 2 . . . . . . . . . . . BANF1P3 . . . barrier to autointegration factor 1 pseudogene 3 . . . . . . . . . . . BANF1P4 . . . barrier to autointegration factor 1 pseudogene 4 . . . . . . . . . . . BANF1P5 . . . barrier to autointegration factor 1 pseudogene 5 . . . . . . . . . . . BANF2 0.0481236094609711 0.68217053103044 0.269705859508589 barrier to autointegration factor 2 FUNCTION: May play a role in BANF1 regulation and influence tissue-specific roles of BANF1.; . TISSUE SPECIFICITY: Expressed strongly in testis and pancreas. Also detected in brain, colon, liver, lung, ovary, placenta, prostate, small intestine, spleen and thymus. Not detected in heart, kidney and skeletal muscle.; unclassifiable (Anatomical System);testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.13106 0.10330 0.503505267 79.88912479 2785.4291 9.97079 BANK1 1.76433043896144e-10 0.822080839500567 0.177919160323 B-cell scaffold protein with ankyrin repeats 1 FUNCTION: Involved in B-cell receptor (BCR)-induced Ca(2+) mobilization from intracellular stores. Promotes Lyn-mediated phosphorylation of IP3 receptors 1 and 2. {ECO:0000269|PubMed:11782428}.; DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:18204447}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in B-cell but not T-cell or myeloid cell lines. Highest expression in CD19(+) B-cells, with very low expression in other cell populations. {ECO:0000269|PubMed:11782428, ECO:0000269|PubMed:18204447}.; unclassifiable (Anatomical System);prostate;pancreas;lymph node;lung;endometrium;thyroid;testis;germinal center;aorta; lymph node;skeletal muscle;tonsil; 0.12325 0.11022 0.448277766 77.99598962 3005.30459 10.40173 BANP 0.958647667807905 0.0413483524582544 3.97973384075122e-06 BTG3 associated nuclear protein FUNCTION: Controls V(D)J recombination during T-cell development by repressing T-cell receptor (TCR) beta enhancer function. Binds to scaffold/matrix attachment region beta (S/MARbeta), an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Represses cyclin D1 transcription by recruiting HDAC1 to its promoter, thereby diminishing H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 'Ser-15' phosphorylation and nuclear accumulation, which causes cell cycle arrest (By similarity). {ECO:0000250, ECO:0000269|PubMed:16166625}.; . TISSUE SPECIFICITY: Down-regulated in breast cancer cell lines. {ECO:0000269|PubMed:16166625}.; unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;colon;blood;skin;bone marrow;uterus;prostate;cochlea;cerebral cortex;endometrium;bone;placenta;visual apparatus;liver;spleen;kidney;spinal ganglion;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;cerebellum peduncles;placenta;testis;trigeminal ganglion; 0.64532 0.13415 -0.822919685 11.76574664 798.42168 5.56845 BAP1 0.385637503937077 0.614275293576839 8.72024860841888e-05 BRCA1 associated protein 1 FUNCTION: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'- linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration (PubMed:24703950). Acts as a tumor suppressor. {ECO:0000269|PubMed:12485996, ECO:0000269|PubMed:18757409, ECO:0000269|PubMed:19117993, ECO:0000269|PubMed:19188440, ECO:0000269|PubMed:19815555, ECO:0000269|PubMed:20436459, ECO:0000269|PubMed:24703950, ECO:0000269|PubMed:9528852}.; DISEASE: Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive neoplasm of the serosal lining of the chest. It appears as broad sheets of cells, with some regions containing spindle- shaped, sarcoma-like cells and other regions showing adenomatous patterns. Pleural mesotheliomas have been linked to exposure to asbestos. {ECO:0000269|PubMed:21642991, ECO:0000269|PubMed:21874000}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Tumor predisposition syndrome (TPDS) [MIM:614327]: A condition characterized by predisposition to develop a variety of tumors, including benign melanocytic tumors as well as several malignant tumors, including uveal melanoma, cutaneous melanoma, malignant mesothelioma on exposure to asbestos, lung adenocarcinoma and meningioma. {ECO:0000269|PubMed:21874003}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in testis, placenta and ovary. Expressed in breast. {ECO:0000269|PubMed:9528852}.; ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;nervous;tongue;islets of Langerhans;hypothalamus;muscle;urinary;blood;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;alveolus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; whole brain;amygdala;superior cervical ganglion;medulla oblongata;testis - interstitial;testis - seminiferous tubule;temporal lobe;prefrontal cortex;testis;parietal lobe; 0.27232 0.10613 -0.975433863 8.852323661 211.96427 3.14058 BARD1 1.17553778280862e-11 0.163183983369394 0.836816016618851 BRCA1 associated RING domain 1 FUNCTION: Probable E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage. {ECO:0000269|PubMed:12890688, ECO:0000269|PubMed:14976165, ECO:0000269|PubMed:20351172}.; . . lymphoreticular;colon;skin;bone marrow;prostate;optic nerve;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;skeletal muscle;bile duct;pancreas;lung;placenta;alveolus;liver;spleen;head and neck;cervix;mammary gland;stomach; testis;tumor;thymus; 0.72203 0.28245 0.935129812 89.86199575 4731.20509 13.90957 BARHL1 0.0384385890309819 0.837398973178336 0.124162437790682 BarH like homeobox 1 . . . whole body; superior cervical ganglion;cerebellum peduncles;testis;cerebellum; 0.80566 0.16046 -0.361761279 28.6329323 12.52617 0.45664 BARHL2 0.222344944286557 0.741006535418934 0.0366485202945089 BarH like homeobox 2 FUNCTION: Potential regulator of neural basic helix-loop-helix genes. {ECO:0000250}.; . . . . 0.70792 0.10225 -0.560178693 19.30879925 43.82051 1.26110 BARX1 0.69051609142232 0.291377463338738 0.0181064452389417 BARX homeobox 1 FUNCTION: Transcription factor, which is involved in craniofacial development, in odontogenesis and in stomach organogenesis. May have a role in the differentiation of molars from incisors. Plays a role in suppressing endodermal Wnt activity (By similarity). Binds to a regulatory module of the NCAM promoter. {ECO:0000250, ECO:0000269|PubMed:9804553}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher levels in testis and heart. Detected in craniofacial tissue and adult iris, but not in lymphocytes, fibroblasts, choroid retina, retinal pigment epithelium, kidney, or fetal liver.; uterus;pancreas;lung;oesophagus;bone;duodenum;testis;cervix;kidney;stomach; superior cervical ganglion;testis;ciliary ganglion;trigeminal ganglion; 0.20006 0.17821 . . 518.2931 4.65314 BARX1-AS1 . . . BARX1 antisense RNA 1 (head to head) . . . . . . . . . . . BARX2 0.123464487684471 0.8522710188184 0.0242644934971289 BARX homeobox 2 FUNCTION: Transcription factor. Binds optimally to the DNA consensus sequence 5'-YYTAATGRTTTTY-3'. May control the expression of neural adhesion molecules such as L1 or Ng-CAM during embryonic development of both the central and peripherical nervous system. May be involved in controlling adhesive processes in keratinizing epithelia (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in adult salivary gland and at much lower levels in mammary gland, kidney and placenta.; prostate;lacrimal gland;kidney;mammary gland; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle;cingulate cortex;skin; 0.24029 0.10931 -0.181750739 40.15687662 97.06934 2.12940 BASP1 0.539222352506789 0.403650732596534 0.0571269148966764 brain abundant membrane attached signal protein 1 . . TISSUE SPECIFICITY: Brain.; smooth muscle;ovary;sympathetic chain;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;aorta;stomach;peripheral nerve; whole brain;amygdala;medulla oblongata;occipital lobe;thalamus;hypothalamus;temporal lobe;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;whole blood;cingulate cortex;parietal lobe; 0.20195 0.13818 . . 157.19188 2.73957 BASP1P1 . . . brain abundant, membrane attached signal protein 1 pseudogene 1 . . . . . . . . . . . BATF 0.744904919744278 0.244502273009886 0.0105928072458354 basic leucine zipper ATF-like transcription factor FUNCTION: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune- specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8(+) T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at highest levels in lung, and at lower levels in placenta, liver, kidney, spleen, and peripheral blood. Detected in SW480 colorectal cancer cell line and several hematopoietic tumor cell lines, including Raji Burkitt's lymphoma. Strongly expressed in mature B- and T-lymphocytes. Also expressed in moderate levels in lymph node and appendix and at low levels in thymus and bone marrow (PubMed:10777209). {ECO:0000269|PubMed:10777209, ECO:0000269|PubMed:8570175, ECO:0000269|PubMed:8630063}.; unclassifiable (Anatomical System);cartilage;ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;uterus;prostate;lung;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland;bladder;tonsil;stomach; testis - interstitial;globus pallidus;appendix;ciliary ganglion;white blood cells;tonsil; 0.91421 0.16306 0.191216164 66.57230479 13.17845 0.47989 BATF2 0.0295318774859601 0.805531965746637 0.164936156767403 basic leucine zipper ATF-like transcription factor 2 FUNCTION: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system. Following infection, participates in the differentiation of CD8(+) thymic conventional dendritic cells in the immune system. Acts via the formation of a heterodimer with JUN family proteins that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3' and regulates expression of target genes (By similarity). Selectively suppresses CYR61/CCN1 transcription and hence blocks the downstream cell proliferation signals produced by CYR61 and inhibits CYR61-induced anchorage-independent growth and invasion in several cancer types, such as breast cancer, malignant glioma and metastatic melanoma. Possibly acts by interfering with AP-1 binding to CYR61 promoter. {ECO:0000250, ECO:0000269|PubMed:20531301}.; . . ovary;salivary gland;intestine;colon;fovea centralis;skin;uterus;prostate;testis;bladder;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;alveolus;cervix;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07665 0.07615 0.17280645 65.75843359 87.73153 2.00009 BATF3 0.0307613819993955 0.811067999213921 0.158170618786683 basic leucine zipper ATF-like transcription factor 3 FUNCTION: AP-1 family transcription factor that controls the differentiation of CD8(+) thymic conventional dendritic cells in the immune system. Required for development of CD8-alpha(+) classical dendritic cells (cDCs) and related CD103(+) dendritic cells that cross-present antigens to CD8 T-cells and produce interleukin-12 (IL12) in response to pathogens (By similarity). Acts via the formation of a heterodimer with JUN family proteins that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3' and regulates expression of target genes. {ECO:0000250, ECO:0000269|PubMed:10878360, ECO:0000269|PubMed:12087103, ECO:0000269|PubMed:15467742}.; . . unclassifiable (Anatomical System);uterus;lung;tongue;islets of Langerhans;placenta;colon;head and neck;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;pons;cingulate cortex; 0.38279 0.10578 0.079165051 59.43029016 1760.70624 7.74657 BAX 0.167938540925625 0.817947544600603 0.0141139144737717 BCL2-associated X protein FUNCTION: Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. {ECO:0000269|PubMed:10772918, ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:18948948, ECO:0000269|PubMed:21199865, ECO:0000269|PubMed:8358790, ECO:0000269|PubMed:8521816}.; . TISSUE SPECIFICITY: Expressed in a wide variety of tissues. Isoform Psi is found in glial tumors. Isoform Alpha is expressed in spleen, breast, ovary, testis, colon and brain, and at low levels in skin and lung. Isoform Sigma is expressed in spleen, breast, ovary, testis, lung, colon, brain and at low levels in skin. Isoform Alpha and isoform Sigma are expressed in pro- myelocytic leukemia, histiocytic lymphoma, Burkitt's lymphoma, T- cell lymphoma, lymphoblastic leukemia, breast adenocarcinoma, ovary adenocarcinoma, prostate carcinoma, prostate adenocarcinoma, lung carcinoma, epidermoid carcinoma, small cell lung carcinoma and colon adenocarcinoma cell lines. {ECO:0000269|PubMed:10772918, ECO:0000269|PubMed:11912183}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;parathyroid;choroid;skin;uterus;prostate;optic nerve;lung;frontal lobe;placenta;visual apparatus;hypopharynx;liver;head and neck;mammary gland; superior cervical ganglion;heart;tumor;white blood cells;trigeminal ganglion;whole blood; 0.84572 0.85150 -0.60427181 17.74593064 11.99833 0.43548 BAZ1A 0.999999774015725 2.2598427452113e-07 4.71559451883999e-21 bromodomain adjacent to zinc finger domain 1A FUNCTION: Component of the ACF complex, an ATP-dependent chromatin remodeling complex, that regulates spacing of nucleosomes using ATP to generate evenly spaced nucleosomes along the chromatin. The ATPase activity of the complex is regulated by the length of flanking DNA. Also involved in facilitating the DNA replication process. BAZ1A is the accessory, non-catalytic subunit of the complex which can enhance and direct the process provided by the ATPase subunit, SMARCA5, probably through targeting pericentromeric heterochromatin in late S phase. Moves end- positioned nucleosomes to a predominantly central position. May have a role in nuclear receptor-mediated transcription repression.; . TISSUE SPECIFICITY: Highly expressed in testis and at low or undetectable levels in other tissues analyzed.; lymphoreticular;medulla oblongata;smooth muscle;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;alveolus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;tumor;white blood cells;whole blood; 0.69881 0.10212 -0.659500046 16.07100731 635.33409 5.07349 BAZ1B 0.999999562861573 4.37138426511854e-07 2.83940223985962e-18 bromodomain adjacent to zinc finger domain 1B FUNCTION: Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator. Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. In the complex, it mediates the recruitment of the WICH complex to replication foci during DNA replication. {ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:16603771, ECO:0000269|PubMed:19092802, ECO:0000269|PubMed:19234442}.; DISEASE: Note=BAZ1B is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of BAZ1B may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease.; TISSUE SPECIFICITY: Ubiquitously expressed with high levels of expression in heart, brain, placenta, skeletal muscle and ovary.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;amniotic fluid;germinal center;bladder;brain;amygdala;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;mesenchyma;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;skeletal muscle;parietal lobe; 0.44577 0.14002 -1.614880551 2.948808681 88.97635 2.02515 BAZ2A 0.999999725956371 2.74043629242324e-07 3.72756405044236e-20 bromodomain adjacent to zinc finger domain 2A FUNCTION: Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription. Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H4 acetylated on 'Lys- 16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac. Specifically binds pRNAs, 150-250 nucleotide RNAs that are complementary in sequence to the rDNA promoter; pRNA- binding is required for heterochromatin formation and rDNA silencing (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at moderate levels in most tissues analyzed, including heart, brain, placenta, lung, skeletal muscle, kidney and pancreas.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;larynx;bone;thyroid;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;spinal cord;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;amnion;hypopharynx;liver;spleen;head and neck;kidney;stomach;peripheral nerve; globus pallidus;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.11513 0.10013 -1.387129737 4.322953527 326.9189 3.84505 BAZ2B 0.999921440363501 7.85596364988583e-05 5.01036871823624e-19 bromodomain adjacent to zinc finger domain 2B FUNCTION: May play a role in transcriptional regulation interacting with ISWI.; . TISSUE SPECIFICITY: Expressed at varying levels in several tissues, whereas a smaller transcript was expressed specifically in testis.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; ciliary ganglion; 0.31025 0.09491 -1.424032938 4.063458363 4391.38778 13.23309 BBC3 0.0712435383459735 0.740958221243888 0.187798240410139 BCL2 binding component 3 FUNCTION: Essential mediator of p53/TP53-dependent and p53/TP53- independent apoptosis. Isoform 3 fails to show any growth- inhibitory or apoptotic activity.; . . unclassifiable (Anatomical System);ovary;colon;fovea centralis;choroid;lens;retina;optic nerve;lung;thyroid;macula lutea;testis;head and neck;cervix;kidney; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.75970 . . . 20.81379 0.70511 BBIP1 . . . BBSome interacting protein 1 FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. Required for primary cilia assembly and BBSome stability. Regulates cytoplasmic microtubule stability and acetylation. {ECO:0000269|Ref.4}.; DISEASE: Bardet-Biedl syndrome 18 (BBS18) [MIM:615995]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:24026985}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . . . . 3.14301 0.11247 BBOF1 . . . basal body orientation factor 1 FUNCTION: Basal body protein required in multiciliate cells to align and maintain cilia orientation in response to flow. May act by mediating a maturation step that stabilizes and aligns cilia orientation. Not required to respond to planar cell polarity (PCP) or flow-based orientation cues (By similarity). {ECO:0000250}.; . . . . 0.13104 . 1.418384579 94.89266336 . . BBOX1 1.50172844518235e-12 0.00727347439690179 0.992726525601597 gamma-butyrobetaine hydroxylase 1 FUNCTION: Catalyzes the formation of L-carnitine from gamma- butyrobetaine.; . TISSUE SPECIFICITY: Highly expressed in kidney; moderately expressed in liver; very low expression in brain.; unclassifiable (Anatomical System);heart;ovary;oral cavity;skin;uterus;lung;cochlea;placenta;hippocampus;liver;head and neck;spleen;kidney;brain; amygdala;hypothalamus;spinal cord;kidney; 0.16162 0.19132 -0.558357437 19.54470394 25.4204 0.82991 BBOX1-AS1 . . . BBOX1 antisense RNA 1 . . . . . . . . . . . BBS1 1.77866932252961e-07 0.962498133924306 0.0375016882087613 Bardet-Biedl syndrome 1 FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization. {ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986}.; DISEASE: Bardet-Biedl syndrome 1 (BBS1) [MIM:209900]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:12118255, ECO:0000269|PubMed:12524598, ECO:0000269|PubMed:12567324, ECO:0000269|PubMed:12677556, ECO:0000269|PubMed:12920096, ECO:0000269|PubMed:15770229, ECO:0000269|PubMed:21052717, ECO:0000269|PubMed:21344540}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in the kidney. Also found in fetal tissue, testis, retina, adipose tissue, heart, skeletal muscle and pancreas.; medulla oblongata;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;pharynx;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;kidney;aorta;stomach;thymus; superior cervical ganglion;liver;prefrontal cortex;ciliary ganglion;pons;atrioventricular node;kidney;caudate nucleus;trigeminal ganglion;cingulate cortex;cerebellum; . . -0.264476624 34.8844067 2.96492 0.10746 BBS2 1.8525443177165e-10 0.952013149757708 0.0479868500570371 Bardet-Biedl syndrome 2 FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization. {ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986}.; . TISSUE SPECIFICITY: Widely expressed.; sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;thyroid;bone;pituitary gland;testis;dura mater;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;meninges;cartilage;heart;islets of Langerhans;adrenal cortex;lens;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; amygdala;dorsal root ganglion;superior cervical ganglion;occipital lobe;hypothalamus;adrenal cortex;prefrontal cortex;globus pallidus;ciliary ganglion;caudate nucleus;trigeminal ganglion;cingulate cortex; 0.17988 0.09548 -0.841329384 11.36470866 556.34466 4.79147 BBS4 0.000141017368072284 0.991684261845702 0.00817472078622574 Bardet-Biedl syndrome 4 FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization. Required for microtubule anchoring at the centrosome but not for microtubule nucleation. May be required for the dynein-mediated transport of pericentriolar proteins to the centrosome. {ECO:0000269|PubMed:15107855, ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986}.; . TISSUE SPECIFICITY: Ubiquitously expressed. The highest level of expression is found in the kidney.; medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;lymph node;heart;hypothalamus;blood;lens;skeletal muscle;pancreas;pia mater;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;cervix;kidney;stomach; medulla oblongata;testis - seminiferous tubule;testis; 0.12886 0.32774 0.112125503 62.09601321 2325.46088 8.93211 BBS5 0.00259936459879345 0.982698102682545 0.0147025327186617 Bardet-Biedl syndrome 5 FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for BBSome complex ciliary localization but not for the proper complex assembly. {ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986}.; DISEASE: Bardet-Biedl syndrome 5 (BBS5) [MIM:615983]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:15137946, ECO:0000269|PubMed:18203199, ECO:0000269|PubMed:21344540}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;colon;choroid;retina;breast;whole body;lung;endometrium;thyroid;bone;visual apparatus;testis;brain; testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.37185 0.22488 0.038710339 56.92380278 . . BBS7 0.00117874565612182 0.998427164282151 0.000394090061727507 Bardet-Biedl syndrome 7 FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization. {ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986}.; DISEASE: Bardet-Biedl syndrome 7 (BBS7) [MIM:615984]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:12567324, ECO:0000269|PubMed:12677556, ECO:0000269|PubMed:15770229, ECO:0000269|PubMed:21344540}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 2 is ubiquitously expressed. Isoform 1 is expressed in retina, lung, liver, testis, ovary, prostate, small intestine, liver, brain, heart and pancreas.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;frontal lobe;endometrium;larynx;gum;bone;testis;brain;gall bladder;unclassifiable (Anatomical System);trophoblast;cartilage;heart;hypothalamus;pharynx;blood;skeletal muscle;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;aorta; . 0.18181 0.17949 -0.402212257 26.7338995 79.1851 1.87931 BBS9 6.37524189346244e-10 0.998152307227318 0.00184769213515839 Bardet-Biedl syndrome 9 FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. Required for proper BBSome complex assembly and its ciliary localization. {ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986}.; DISEASE: Note=A chromosomal aberration involving PTHB1 has been found in Wilms tumor. Translocation t(1;7)(q42;p15) with OBSCN. {ECO:0000269|PubMed:12618763}.; DISEASE: Bardet-Biedl syndrome 9 (BBS9) [MIM:615986]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:16380913}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Expressed in adult heart, skeletal muscle, lung, liver, kidney, placenta and brain, and in fetal kidney, lung, liver and brain. {ECO:0000269|PubMed:10221542, ECO:0000269|PubMed:16380913}.; choroid;fovea centralis;skin;retina;uterus;optic nerve;cochlea;endometrium;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney; dorsal root ganglion;testis - interstitial;superior cervical ganglion;medulla oblongata;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.41184 0.20084 1.050838371 91.36588818 1873.24703 7.96197 BBS10 6.78247357873408e-09 0.0731738789269657 0.926826114290561 Bardet-Biedl syndrome 10 FUNCTION: Probable molecular chaperone. Assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Involved in adipogenic differentiation. {ECO:0000269|PubMed:19190184, ECO:0000269|PubMed:20080638}.; DISEASE: Bardet-Biedl syndrome 10 (BBS10) [MIM:615987]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:16582908, ECO:0000269|PubMed:20120035, ECO:0000269|PubMed:21344540, ECO:0000269|PubMed:23219996}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.09846 0.14899 -0.354480518 29.42911064 81.48109 1.91161 BBS12 3.92874770167448e-07 0.357513401559753 0.642486205565477 Bardet-Biedl syndrome 12 FUNCTION: Probable molecular chaperone. Assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Involved in adipogenic differentiation. {ECO:0000269|PubMed:19190184, ECO:0000269|PubMed:20080638}.; DISEASE: Bardet-Biedl syndrome 12 (BBS12) [MIM:615989]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:17160889, ECO:0000269|PubMed:20120035, ECO:0000269|PubMed:21344540}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;blood;parathyroid;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;optic nerve;lung;cochlea;bone;placenta;macula lutea;hippocampus;testis;spleen;kidney;brain;bladder; dorsal root ganglion;testis - interstitial;superior cervical ganglion;medulla oblongata;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.05489 0.17283 1.379742765 94.60368011 623.03254 5.03368 BBX 0.958097848857497 0.041902117057814 3.40846888469325e-08 bobby sox homolog (Drosophila) FUNCTION: Transcription factor that is necessary for cell cycle progression from G1 to S phase. {ECO:0000269|PubMed:11680820}.; . . umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;adrenal cortex;atrioventricular node;caudate nucleus;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;pituitary; 0.48561 0.09034 0.005534202 54.09884407 1368.93611 6.93849 BCAM 0.0368511835228543 0.962838134431876 0.000310682045269997 basal cell adhesion molecule (Lutheran blood group) FUNCTION: Laminin alpha-5 receptor. May mediate intracellular signaling. {ECO:0000269|PubMed:9616226}.; . TISSUE SPECIFICITY: Wide tissue distribution (highest in the pancreas and very low in brain). Closely associated with the basal layer of cells in epithelia and the endothelium of blood vessel walls.; ovary;sympathetic chain;colon;skin;uterus;prostate;optic nerve;cerebral cortex;endometrium;larynx;thyroid;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;breast;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;thyroid;kidney;fetal thyroid;skeletal muscle; 0.15140 0.15985 1.252926935 93.48313281 349.93518 3.96510 BCAN 0.00361212462845155 0.996309343776489 7.85315950591839e-05 brevican FUNCTION: May play a role in the terminally differentiating and the adult nervous system during postnatal development. Could stabilize interactions between hyaluronan (HA) and brain proteoglycans.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;colon;fovea centralis;choroid;skin;retina;uterus;lung;frontal lobe;cochlea;endometrium;macula lutea;visual apparatus;hippocampus;kidney;pineal gland;brain;stomach;cerebellum; amygdala;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.28078 0.15677 -1.056370776 7.578438311 2276.03232 8.82237 BCAP29 0.220058296267505 0.771634792279971 0.00830691145252368 B-cell receptor-associated protein 29 FUNCTION: May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. May be involved in CASP8-mediated apoptosis (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach;aorta; testis - interstitial;medulla oblongata;subthalamic nucleus;testis - seminiferous tubule;testis;parietal lobe; 0.08739 0.08176 0.17280645 65.75843359 329.90016 3.85960 BCAP31 0.869367470623907 0.128850068618979 0.00178246075711406 B-cell receptor-associated protein 31 FUNCTION: Functions as a chaperone protein. Is one of the most abundant endoplasmic reticulum (ER) proteins. Plays a role in the export of secreted proteins in the ER, the recognition of abnormally folded protein and their targeting to the ER associated-degradation (ERAD). Also serves as a cargo receptor for the export of transmembrane proteins. May be involved in CASP8- mediated apoptosis. {ECO:0000269|PubMed:10958671, ECO:0000269|PubMed:18287538, ECO:0000269|PubMed:9396746}.; DISEASE: Deafness, dystonia, and cerebral hypomyelination (DDCH) [MIM:300475]: An X-linked recessive mental retardation syndrome characterized by almost no psychomotor development, dysmorphic facial features, sensorineural deafness, dystonia, pyramidal signs, and hypomyelination on brain imaging. {ECO:0000269|PubMed:24011989}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=BCAP31 is deleted in the chromosome Xq28 deletion syndrome which involves BCAP31 and the and the promoter region of ABCD1. {ECO:0000269|PubMed:11992258}.; TISSUE SPECIFICITY: Ubiquitous. Highly expressed in neurons and discrete endocrine cells. {ECO:0000269|PubMed:11561007}.; myocardium;ovary;umbilical cord;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;synovium;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus; . 0.20772 0.16918 -0.007201372 53.19061099 14.21644 0.51425 BCAP31P1 . . . B-cell receptor-associated protein 31 pseudogene 1 . . . . . . . . . . . BCAP31P2 . . . B-cell receptor-associated protein 31 pseudogene 2 . . . . . . . . . . . BCAR1 0.992956578294104 0.00704317084176697 2.50864128589487e-07 breast cancer anti-estrogen resistance 1 FUNCTION: Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells. {ECO:0000269|PubMed:12832404, ECO:0000269|PubMed:17038317}.; . TISSUE SPECIFICITY: Widely expressed with an abundant expression in the testis. Low level of expression seen in the liver, thymus, and peripheral blood leukocytes. The protein has been detected in a B-cell line.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;iris;testis;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;pineal body;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;cervix;kidney;mammary gland;stomach; atrioventricular node; 0.47335 . 1.53037684 95.51191319 778.41129 5.52069 BCAR1P1 . . . breast cancer anti-estrogen resistance 1 pseudogene 1 . . . . . . . . . . . BCAR1P2 . . . breast cancer anti-estrogen resistance 1 pseudogene 2 . . . . . . . . . . . BCAR3 0.916779854975838 0.0832191904640294 9.54560132118277e-07 breast cancer anti-estrogen resistance 3 FUNCTION: May act as an adapter protein and couple activated growth factor receptors to a signaling pathway that regulates the proliferation in breast cancer cells. When overexpressed, it confers anti-estrogen resistance in breast cancer cell lines. May also be regulated by cellular adhesion to extracellular matrix proteins. {ECO:0000269|PubMed:9582273}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Found in several cancer cell lines, but not in nonmalignant breast tissue. {ECO:0000269|PubMed:10187783, ECO:0000269|PubMed:9582273}.; ovary;colon;skin;uterus;endometrium;cerebral cortex;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lens;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;stomach; placenta;atrioventricular node; 0.29066 0.16494 0.255325157 69.71573484 597.29767 4.94542 BCAR4 . . . breast cancer anti-estrogen resistance 4 (non-protein coding) . . . . . . . . . . . BCAS1 0.0136569957373472 0.979681820637667 0.00666118362498538 breast carcinoma amplified sequence 1 . . TISSUE SPECIFICITY: Expressed in brain and prostate, and at lower levels in testis, intestine and colon. Overexpressed in most breast cancer cell lines and down-regulated in some colorectal tumors. {ECO:0000269|PubMed:10857754, ECO:0000269|PubMed:14567997}.; . . 0.15155 0.08909 1.469764896 95.28190611 2626.21477 9.61114 BCAS2 6.52504489211884e-05 0.721617361666745 0.278317387884334 breast carcinoma amplified sequence 2 FUNCTION: Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR). {ECO:0000269|PubMed:24332808}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10403562}.; . . 0.16168 0.11809 0.125076652 62.7388535 253.36456 3.42520 BCAS2P1 . . . breast carcinoma amplified sequence 2 pseudogene 1 . . . . . . . . . . . BCAS2P2 . . . breast carcinoma amplified sequence 2 pseudogene 2 . . . . . . . . . . . BCAS2P3 . . . breast carcinoma amplified sequence 2 pseudogene 3 . . . . . . . . . . . BCAS3 0.998848201672345 0.00115179832663025 1.02492087629103e-12 breast carcinoma amplified sequence 3 FUNCTION: Plays a role in angiogenesis. Participates in the regulation of cell polarity and directional endothelial cell migration by mediating both the activation and recruitment of CDC42 and the reorganization of the actin cytoskeleton at the cell leading edge. Promotes filipodia formation (By similarity). Functions synergistically with PELP1 as a transcriptional coactivator of estrogen receptor-responsive genes. Stimulates histone acetyltransferase activity. Binds to chromatin. {ECO:0000250|UniProtKB:Q8CCN5, ECO:0000269|PubMed:17505058}.; DISEASE: Note=A chromosomal aberration involving BCAS3 has been found in some breast carcinoma cell lines. Translocation t(17;20)(q23;q13) with BCAS4.; TISSUE SPECIFICITY: Expressed in stomach, liver, lung, kidney, prostate, testis, thyroid gland, adrenal gland, brain, heart, skeletal muscle, colon, spleen, small intestine, placenta, blood leukocyte and mammary epithelial cells. Expressed in undifferentiated ES cells. Expressed in blood islands and nascent blood vessels derived from differentiated ES cells into embryoid bodies (BD). Expressed in endothelial cells. Not detected in brain. Expressed in brain tumors (at protein level). Expressed in brain. Highly expressed in breast cancers and in glioma cell lines. {ECO:0000269|PubMed:12378525, ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:18030336}.; unclassifiable (Anatomical System);medulla oblongata;ovary;colon;skeletal muscle;skin;uterus;optic nerve;lung;nasopharynx;bone;placenta;iris;liver;testis;spleen;brain;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.63691 . -0.753139731 13.67067705 343.97696 3.93313 BCAS4 0.0466393235045461 0.854541806051859 0.0988188704435948 breast carcinoma amplified sequence 4 . . TISSUE SPECIFICITY: Brain, thymus, spleen, kidney and placenta. Overexpressed in most breast cancer cell lines. {ECO:0000269|PubMed:12378525}.; unclassifiable (Anatomical System);uterus;prostate;lymph node;lung;ovary;colon;kidney;germinal center;brain;skin; . 0.14628 0.09488 . . 1035.53215 6.17935 BCAT1 7.04875662949652e-06 0.721690467397959 0.278302483845411 branched chain amino acid transaminase 1 FUNCTION: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.; . TISSUE SPECIFICITY: During embryogenesis, expressed in the brain and kidney. Overexpressed in MYC-induced tumors such as Burkitt's lymphoma.; lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;head and neck;kidney;stomach;aorta; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.67216 0.17808 0.483275131 79.25218212 36.46306 1.09281 BCAT2 1.71339042998067e-11 0.057617731551677 0.942382268431189 branched chain amino acid transaminase 2 FUNCTION: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;bone;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; thalamus;superior cervical ganglion;testis - seminiferous tubule;adrenal gland; 0.18009 0.17987 0.174625237 65.9648502 258.16382 3.45561 BCCIP 0.00165485845540064 0.889372806520918 0.108972335023682 BRCA2 and CDKN1A interacting protein FUNCTION: May promote cell cycle arrest by enhancing the inhibition of CDK2 activity by CDKN1A. May be required for repair of DNA damage by homologous recombination in conjunction with BRCA2. May not be involved in non-homologous end joining (NHEJ). {ECO:0000269|PubMed:10878006, ECO:0000269|PubMed:14726710, ECO:0000269|PubMed:15539944, ECO:0000269|PubMed:15713648, ECO:0000269|PubMed:17947333}.; . TISSUE SPECIFICITY: Expressed at high levels in testis and skeletal muscle and at lower levels in brain, heart, kidney, liver, lung, ovary, pancreas, placenta, and spleen. {ECO:0000269|PubMed:10878006, ECO:0000269|PubMed:11313963}.; ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;pineal gland;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; testis - interstitial;testis - seminiferous tubule;testis;white blood cells;trigeminal ganglion;skeletal muscle; 0.31124 0.08875 -0.714505427 14.4019816 27.65375 0.88918 BCDIN3D 0.00503914777207975 0.886852076214323 0.108108776013597 BCDIN3 domain containing RNA methyltransferase FUNCTION: O-methyltransferase that specifically dimethylates the 5' monophosphate of pre-miRNAs, acting as a negative regulator of miRNA processing. The 5' monophosphate of pre-miRNAs is recognized by DICER1 and is required for pre-miRNAs processing: methylation at this position reduces the processing of pre-miRNAs by DICER1. Able to mediate methylation of pre-miR-145, as well as other pre- miRNAs. {ECO:0000269|PubMed:23063121}.; . . unclassifiable (Anatomical System);ovary;adrenal cortex;colon;parathyroid;skin;retina;breast;uterus;prostate;lung;endometrium;nasopharynx;placenta;liver;testis;spleen;germinal center;kidney;brain;tonsil;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12160 . 0.128714042 63.19886766 1376.50648 6.95608 BCDIN3D-AS1 . . . BCDIN3D antisense RNA 1 . . . . . . . . . . . BCHE 4.44441991561661e-11 0.0275685533713455 0.97243144658421 butyrylcholinesterase FUNCTION: Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters. {ECO:0000269|PubMed:19452557, ECO:0000269|PubMed:19542320}.; DISEASE: Butyrylcholinesterase deficiency (BChE deficiency) [MIM:177400]: A metabolic disorder characterized by prolonged apnea after the use of certain anesthetic drugs, including the muscle relaxants succinylcholine or mivacurium and other ester local anesthetics. The duration of the prolonged apnea varies significantly depending on the extent of the enzyme deficiency. {ECO:0000269|PubMed:10404729, ECO:0000269|PubMed:11928765, ECO:0000269|PubMed:12881446, ECO:0000269|PubMed:1306123, ECO:0000269|PubMed:1349196, ECO:0000269|PubMed:1415224, ECO:0000269|PubMed:15563885, ECO:0000269|PubMed:15781196, ECO:0000269|PubMed:1611188, ECO:0000269|PubMed:16788378, ECO:0000269|PubMed:17700357, ECO:0000269|PubMed:18075469, ECO:0000269|PubMed:18300943, ECO:0000269|PubMed:25054547, ECO:0000269|PubMed:25264279, ECO:0000269|PubMed:2915989, ECO:0000269|PubMed:7634491, ECO:0000269|PubMed:8554068, ECO:0000269|PubMed:8680411, ECO:0000269|PubMed:9110359, ECO:0000269|PubMed:9191541, ECO:0000269|PubMed:9388484, ECO:0000269|PubMed:9543549, ECO:0000269|PubMed:9694584}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in blood plasma (at protein level). Present in most cells except erythrocytes. {ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:19542320}.; unclassifiable (Anatomical System);smooth muscle;heart;ovary;hypothalamus;muscle;adrenal cortex;colon;parathyroid;skin;skeletal muscle;retina;uterus;pancreas;prostate;whole body;lung;thyroid;placenta;liver;testis;head and neck;brain;mammary gland;peripheral nerve; superior cervical ganglion;fetal liver;appendix; 0.24308 0.50530 0.778977686 87.21396556 1717.79021 7.64210 BCKDHA 7.66463791783609e-08 0.468614120759903 0.531385802593717 branched chain keto acid dehydrogenase E1, alpha polypeptide FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).; DISEASE: Maple syrup urine disease 1A (MSUD1A) [MIM:248600]: A metabolic disorder due to an enzyme defect in the catabolic pathway of the branched-chain amino acids leucine, isoleucine, and valine. Accumulation of these 3 amino acids and their corresponding keto acids leads to encephalopathy and progressive neurodegeneration. Clinical features include mental and physical retardation, feeding problems, and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine. If untreated, maple syrup urine disease can lead to seizures, coma, and death. The disease is often classified by its pattern of signs and symptoms. The most common and severe form of the disease is the classic type, which becomes apparent soon after birth. Variant forms of the disorder become apparent later in infancy or childhood and are typically milder, but they still involve developmental delay and other medical problems if not treated. {ECO:0000269|PubMed:1867199, ECO:0000269|PubMed:1885764, ECO:0000269|PubMed:2060625, ECO:0000269|PubMed:21844576, ECO:0000269|PubMed:2241958, ECO:0000269|PubMed:2703538, ECO:0000269|PubMed:7883996, ECO:0000269|PubMed:8037208, ECO:0000269|PubMed:8161368}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;myocardium;medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;iris;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;cervix;head and neck;spleen;kidney;mammary gland;stomach;cerebellum; liver;ciliary ganglion;skeletal muscle; . 0.10939 -1.019530098 8.038452465 . . BCKDHB 2.91008815830628e-06 0.767207619382806 0.232789470529036 branched chain keto acid dehydrogenase E1, beta polypeptide FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).; DISEASE: Maple syrup urine disease 1B (MSUD1B) [MIM:248600]: A metabolic disorder due to an enzyme defect in the catabolic pathway of the branched-chain amino acids leucine, isoleucine, and valine. Accumulation of these 3 amino acids and their corresponding keto acids leads to encephalopathy and progressive neurodegeneration. Clinical features include mental and physical retardation, feeding problems, and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine. If untreated, maple syrup urine disease can lead to seizures, coma, and death. The disease is often classified by its pattern of signs and symptoms. The most common and severe form of the disease is the classic type, which becomes apparent soon after birth. Variant forms of the disorder become apparent later in infancy or childhood and are typically milder, but they still involve developmental delay and other medical problems if not treated. {ECO:0000269|PubMed:11509994, ECO:0000269|PubMed:22326532, ECO:0000269|PubMed:8161368}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;skin;retina;uterus;prostate;whole body;cochlea;endometrium;synovium;bone;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;tongue;hypothalamus;urinary;lung;mesenchyma;placenta;liver;spleen;kidney;stomach; superior cervical ganglion;subthalamic nucleus;liver;testis;atrioventricular node;skeletal muscle; 0.21382 0.37665 -0.449946534 24.00330267 37.41729 1.11457 BCKDK 0.00580435804002904 0.971878089631323 0.0223175523286478 branched chain ketoacid dehydrogenase kinase FUNCTION: Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways. Key enzyme that regulate the activity state of the BCKD complex. {ECO:0000269|PubMed:24449431}.; DISEASE: Branched-chain ketoacid dehydrogenase kinase deficiency (BCKDKD) [MIM:614923]: A metabolic disorder characterized by autism, epilepsy, intellectual disability, and reduced branched- chain amino acids. {ECO:0000269|PubMed:22956686, ECO:0000269|PubMed:24449431}. Note=The disease is caused by mutations affecting the gene represented in this entry. A diet enriched in branched amino acids (BCAAs) allows to normalize plasma BCAA levels. This suggests that it may be possible to treat patients with mutations in BCKDK with BCAA supplementation.; TISSUE SPECIFICITY: Ubiquitous.; ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;brain;bladder;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);small intestine;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;head and neck;kidney;stomach; liver; 0.19254 0.12253 -0.53631094 20.53550366 34.68489 1.05782 BCL2 0.337855763889345 0.602211203178345 0.0599330329323097 B-cell CLL/lymphoma 2 FUNCTION: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785). {ECO:0000269|PubMed:17418785, ECO:0000269|PubMed:18570871}.; DISEASE: Note=A chromosomal aberration involving BCL2 has been found in chronic lymphatic leukemia. Translocation t(14;18)(q32;q21) with immunoglobulin gene regions. BCL2 mutations found in non-Hodgkin lymphomas carrying the chromosomal translocation could be attributed to the Ig somatic hypermutation mechanism resulting in nucleotide transitions. {ECO:0000269|PubMed:2875799, ECO:0000269|PubMed:3285301}.; TISSUE SPECIFICITY: Expressed in a variety of tissues.; lymphoreticular;ovary;colon;parathyroid;skin;uterus;prostate;whole body;cochlea;bone;thyroid;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;blood;skeletal muscle;breast;lung;placenta;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;olfactory bulb;thyroid;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.95405 0.98331 -0.185391282 39.67916962 463.55581 4.46164 BCL2A1 0.481233411410349 0.496256630762706 0.0225099578269452 BCL2 related protein A1 FUNCTION: Retards apoptosis induced by IL-3 deprivation. May function in the response of hemopoietic cells to external signals and in maintaining endothelial survival during infection (By similarity). Can inhibit apoptosis induced by serum starvation in the mammary epithelial cell line HC11 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q07440}.; . TISSUE SPECIFICITY: Seems to be restricted to the hematopoietic compartment. Expressed in peripheral blood, spleen, and bone marrow, at moderate levels in lung, small intestine and testis, at a minimal levels in other tissues. Also found in vascular smooth muscle cells and hematopoietic malignancies.; unclassifiable (Anatomical System);myocardium;lymph node;ovary;salivary gland;intestine;pharynx;colon;blood;skin;bone marrow;prostate;visual apparatus;liver;germinal center;kidney;brain;bladder; whole blood; 0.17419 0.33842 0.505321956 80.00707714 2722.97267 9.83615 BCL2L1 0.823684827507086 0.172400468540287 0.0039147039526272 BCL2 like 1 FUNCTION: Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage- dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.; FUNCTION: Isoform Bcl-X(S) promotes apoptosis.; . TISSUE SPECIFICITY: Bcl-X(S) is expressed at high levels in cells that undergo a high rate of turnover, such as developing lymphocytes. In contrast, Bcl-X(L) is found in tissues containing long-lived postmitotic cells, such as adult brain.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;amnion;alveolus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach;cerebellum; superior cervical ganglion;skeletal muscle;bone marrow; 0.69868 0.75783 -0.207437529 38.2814343 3.26282 0.11794 BCL2L2 0.312495747576068 0.616519757231816 0.0709844951921167 BCL2 like 2 FUNCTION: Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX. {ECO:0000269|PubMed:8761287}.; . TISSUE SPECIFICITY: Expressed (at protein level) in a wide range of tissues with highest levels in brain, spinal cord, testis, pancreas, heart, spleen and mammary glands. Moderate levels found in thymus, ovary and small intestine. Not detected in salivary gland, muscle or liver. Also expressed in cell lines of myeloid, fibroblast and epithelial origin. Not detected in most lymphoid cell lines. {ECO:0000269|PubMed:11423909}.; ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;iris;testis;germinal center;brain;artery;pineal gland;unclassifiable (Anatomical System);amygdala;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;muscle;adrenal cortex;skeletal muscle;lung;adrenal gland;mesenchyma;trabecular meshwork;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; amygdala;whole brain;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.68867 0.20084 -0.029247611 51.40363293 13.09822 0.47666 BCL2L2-PABPN1 0.425968450134784 0.572476403022178 0.00155514684303793 BCL2L2-PABPN1 readthrough FUNCTION: Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX. {ECO:0000269|PubMed:8761287}.; . TISSUE SPECIFICITY: Expressed (at protein level) in a wide range of tissues with highest levels in brain, spinal cord, testis, pancreas, heart, spleen and mammary glands. Moderate levels found in thymus, ovary and small intestine. Not detected in salivary gland, muscle or liver. Also expressed in cell lines of myeloid, fibroblast and epithelial origin. Not detected in most lymphoid cell lines. {ECO:0000269|PubMed:11423909}.; . . . . -0.404032746 26.53338051 6.03346 0.22817 BCL2L10 0.000387594966865579 0.396098548484486 0.603513856548649 BCL2 like 10 FUNCTION: Promotes cell survival. Suppresses apoptosis induced by BAX but not BAK. {ECO:0000269|PubMed:11278245}.; . TISSUE SPECIFICITY: Widely expressed in adult tissues. Preferentially expressed in lung, liver and kidney. {ECO:0000269|PubMed:11593390}.; uterus;islets of Langerhans;liver;spleen;kidney;brain; superior cervical ganglion;temporal lobe;globus pallidus;trigeminal ganglion;skeletal muscle; 0.07304 0.13570 . . 452.59573 4.42643 BCL2L11 0.950822922206983 0.0490281409111263 0.000148936881891281 BCL2 like 11 FUNCTION: Induces apoptosis and anoikis. Isoform BimL is more potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3 induce apoptosis, although less potent than isoform BimEL, isoform BimL and isoform BimS. Isoform Bim-gamma induces apoptosis. Isoform Bim-alpha3 induces apoptosis possibly through a caspase-mediated pathway. Isoform BimAC and isoform BimABC lack the ability to induce apoptosis. {ECO:0000269|PubMed:11997495, ECO:0000269|PubMed:15486195, ECO:0000269|PubMed:9430630}.; . TISSUE SPECIFICITY: Isoform BimEL, isoform BimL and isoform BimS are the predominant isoforms and are ubiquitously expressed with a tissue-specific variation. Isoform Bim-gamma is most abundantly expressed in small intestine and colon, and in lower levels in spleen, prostate, testis, heart, liver and kidney. {ECO:0000269|PubMed:12019181}.; unclassifiable (Anatomical System);heart;parathyroid;blood;uterus;prostate;lung;cochlea;endometrium;placenta;thyroid;liver;testis;spleen;cervix;germinal center;brain;thymus; testis - interstitial;testis;globus pallidus;trigeminal ganglion;skeletal muscle; 0.17650 0.48182 -0.249709319 35.74545883 6.90383 0.25658 BCL2L12 1.55699450949424e-05 0.653650073510929 0.346334356543976 BCL2 like 12 . . TISSUE SPECIFICITY: Expressed mainly in breast, thymus, prostate, fetal liver, colon, placenta, pancreas, small intestine, spinal cord, kidney, and bone marrow and to a lesser extent in many other tissues. Isoform 2 is primarily expressed in skeletal muscle.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;muscle;urinary;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.31004 0.09727 0.861712133 88.6883699 323.66686 3.82304 BCL2L12P1 . . . BCL2 like 12 pseudogene 1 . . . . . . . . . . . BCL2L13 0.070274402040073 0.916561026036749 0.0131645719231779 BCL2 like 13 FUNCTION: May promote the activation of caspase-3 and apoptosis.; . TISSUE SPECIFICITY: Ubiquitous, with the highest levels of expression in heart, placenta and pancreas.; medulla oblongata;smooth muscle;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;thymus;cerebellum; testis; 0.05910 . 0.50895761 80.20169851 191.37406 3.00010 BCL2L14 0.14312358632999 0.838039015515275 0.0188373981547356 BCL2 like 14 FUNCTION: Plays a role in apoptosis.; . TISSUE SPECIFICITY: Isoform 1 is widely expressed. Isoform 2 is testis-specific. {ECO:0000269|PubMed:11054413}.; unclassifiable (Anatomical System);pancreas;lung;liver;testis;colon;spleen;skeletal muscle;stomach;peripheral nerve; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.05877 0.08159 0.907624513 89.46685539 673.80776 5.18563 BCL2L15 0.00361468827063082 0.626767931459423 0.369617380269946 BCL2 like 15 . . . . . . 0.07577 -0.007201372 53.19061099 8.70097 0.32017 BCL3 0.86217268510329 0.137400478202566 0.000426836694144332 B-cell CLL/lymphoma 3 FUNCTION: Contributes to the regulation of transcriptional activation of NF-kappa-B target genes. In the cytoplasm, inhibits the nuclear translocation of the NF-kappa-B p50 subunit. In the nucleus, acts as transcriptional activator that promotes transcription of NF-kappa-B target genes. Contributes to the regulation of cell proliferation (By similarity). {ECO:0000250, ECO:0000269|PubMed:8453667}.; DISEASE: Note=A chromosomal aberration involving BCL3 may be a cause of B-cell chronic lymphocytic leukemia (B-CLL). Translocation t(14;19)(q32;q13.1) with immunoglobulin gene regions. {ECO:0000269|PubMed:2180580, ECO:0000269|PubMed:7896265}.; . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;retina;optic nerve;thyroid;bone;brain;unclassifiable (Anatomical System);cartilage;lacrimal gland;islets of Langerhans;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;whole blood;skeletal muscle; 0.52579 0.28802 . . 48.07549 1.34896 BCL5 . . . B-cell CLL/lymphoma 5 . . . . . . . . . . . BCL6 0.982525139432015 0.0174743891829515 4.71385033832435e-07 B-cell CLL/lymphoma 6 FUNCTION: Transcriptional repressor mainly required for germinal center (GC) formation and antibody affinity maturation which has different mechanisms of action specific to the lineage and biological functions. Forms complexes with different corepressors and histone deacetylases to repress the transcriptional expression of different subsets of target genes. Represses its target genes by binding directly to the DNA sequence 5'-TTCCTAGAA-3' (BCL6- binding site) or indirectly by repressing the transcriptional activity of transcription factors. In GC B-cells, represses genes that function in differentiation, inflammation, apoptosis and cell cycle control, also autoregulates its transcriptional expression and up-regulates, indirectly, the expression of some genes important for GC reactions, such as AICDA, through the repression of microRNAs expression, like miR155. An important function is to allow GC B-cells to proliferate very rapidly in response to T-cell dependent antigens and tolerate the physiological DNA breaks required for immunglobulin class switch recombination and somatic hypermutation without inducing a p53/TP53-dependent apoptotic response. In follicular helper CD4(+) T-cells (T(FH) cells), promotes the expression of T(FH)-related genes but inhibits the differentiation of T(H)1, T(H)2 and T(H)17 cells. Also required for the establishment and maintenance of immunological memory for both T- and B-cells. Suppresses macrophage proliferation through competition with STAT5 for STAT-binding motifs binding on certain target genes, such as CCL2 and CCND2. In response to genotoxic stress, controls cell cycle arrest in GC B-cells in both p53/TP53- dependedent and -independent manners. Besides, also controls neurogenesis through the alteration of the composition of NOTCH- dependent transcriptional complexes at selective NOTCH targets, such as HES5, including the recruitment of the deacetylase SIRT1 and resulting in an epigenetic silencing leading to neuronal differentiation. {ECO:0000269|PubMed:10981963, ECO:0000269|PubMed:12402037, ECO:0000269|PubMed:12414651, ECO:0000269|PubMed:12504096, ECO:0000269|PubMed:15454082, ECO:0000269|PubMed:15577913, ECO:0000269|PubMed:16142238, ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:18212045, ECO:0000269|PubMed:18280243, ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:23166356, ECO:0000269|PubMed:23911289, ECO:0000269|PubMed:9649500}.; DISEASE: Note=Chromosomal aberrations involving BCL6 are a cause of B-cell non-Hodgkin lymphomas (B-cell NHL), including diffuse large B-cell lymphoma and follicular lymphoma. Approximately 40% of diffuse large B-cell lymphomas and 5 to 10% of follicular lymphomas are associated with chromosomal translocations that deregulate expression of BCL6 by juxtaposing heterologous promoters to the BCL6 coding domain. Translocation t(3;14)(q27;q32). Translocation t(3;22)(q27;q11) with immunoglobulin gene regions. Translocation t(3;7)(q27;p12) with IKZF1 gene 5'non-coding region. Translocation t(3;6)(q27;p21) with Histone H4. Translocation t(3;16)(q27;p11) with IL21R. Translocation t(3;13)(q27;q14) with LCP1.; DISEASE: Note=A chromosomal aberration involving BCL6 may be a cause of a form of B-cell leukemia. Translocation t(3;11)(q27;q23) with POU2AF1/OBF1.; DISEASE: Note=A chromosomal aberration involving BCL6 may be a cause of lymphoma. Translocation t(3;4)(q27;p11) with ARHH/TTF.; TISSUE SPECIFICITY: Expressed in germinal center T- and B-cells and in primary immature dendritic cells. {ECO:0000269|PubMed:10981963, ECO:0000269|PubMed:12402037, ECO:0000269|PubMed:15454082, ECO:0000269|PubMed:16142238, ECO:0000269|PubMed:16455075, ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:18212045, ECO:0000269|PubMed:9649500}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;liver;spleen;head and neck;cervix;mammary gland;stomach;aorta;peripheral nerve;cerebellum; superior cervical ganglion;ciliary ganglion;skeletal muscle;cerebellum; 0.34370 0.51690 -0.464712395 23.5727766 1225.27484 6.61711 BCL6B 0.151089911885991 0.845308679206819 0.00360140890719003 B-cell CLL/lymphoma 6, member B FUNCTION: Acts as a sequence-specific transcriptional repressor in association with BCL6. May function in a narrow stage or be related to some events in the early B-cell development. {ECO:0000269|PubMed:11855826}.; . TISSUE SPECIFICITY: Ubiquitously expressed with higher expression found in heart and placenta. {ECO:0000269|PubMed:11855826}.; unclassifiable (Anatomical System);lung;ovary;placenta;testis;kidney;skeletal muscle; dorsal root ganglion;superior cervical ganglion;globus pallidus; 0.44204 0.11985 -0.734731259 14.01863647 215.21396 3.16583 BCL7A 0.215729268155923 0.775615626668 0.00865510517607703 B-cell CLL/lymphoma 7A . DISEASE: Note=Chromosomal aberrations involving BCL7A may be a cause of B-cell non-Hodgkin lymphoma. Three-way translocation t(8;14;12)(q24.1;q32.3;q24.1) with MYC and with immunoglobulin gene regions. {ECO:0000269|PubMed:8605326}.; . unclassifiable (Anatomical System);prostate;lymph node;lung;placenta;testis;blood;kidney;germinal center;brain;stomach;peripheral nerve; prefrontal cortex;cerebellum; 0.12134 0.12760 0.082802743 60.09082331 8.12338 0.29824 BCL7B 0.706637383924404 0.289862997161816 0.00349961891377983 B-cell CLL/lymphoma 7B FUNCTION: Positive regulator of apoptosis. Plays a role in the Wnt signaling pathway, negatively regulating the expression of Wnt signaling components CTNNB1 and HMGA1 (PubMed:25569233). Involved in cell cycle progression, maintenance of the nuclear structure and stem cell differentiation (PubMed:25569233). May play a role in lung tumor development or progression (By similarity). {ECO:0000250|UniProtKB:Q921K9, ECO:0000269|PubMed:25569233}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9860302, ECO:0000269|PubMed:9931421}.; smooth muscle;ovary;salivary gland;developmental;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;nervous;tongue;islets of Langerhans;hypothalamus;pineal body;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; testis; 0.37552 0.13588 -0.207437529 38.2814343 3.62169 0.13280 BCL7C 0.150443662576109 0.83231138028474 0.0172449571391514 B-cell CLL/lymphoma 7C FUNCTION: May play an anti-apoptotic role. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9931421}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;testis;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;hypothalamus;blood;lens;pancreas;lung;macula lutea;kidney;stomach;peripheral nerve; ciliary ganglion; 0.33188 . -0.185391282 39.67916962 . . BCL9 0.831846216932657 0.168152551054785 1.23201255805031e-06 B-cell CLL/lymphoma 9 FUNCTION: Involved in signal transduction through the Wnt pathway. Promotes beta-catenin's transcriptional activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:11955446}.; . TISSUE SPECIFICITY: Detected at low levels in thymus, prostate, testis, ovary and small intestine, and at lower levels in spleen, colon and blood.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;pineal body;muscle;adrenal cortex;blood;lens;bile duct;breast;lung;placenta;macula lutea;visual apparatus;cervix;kidney;mammary gland; . 0.80794 0.11906 -1.626115313 2.878037273 2074.08236 8.39078 BCL9L 0.998124598837792 0.00187539915550019 2.00670734580285e-09 B-cell CLL/lymphoma 9-like FUNCTION: Transcriptional regulator that acts as an activator. Promotes beta-catenin transcriptional activity. Plays a role in tumorigenesis. Enhances the neoplastic transforming activity of CTNNB1 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in breast, ductal and invasive ductal carcinomas of the breast, sporadic colorectal adenomas and carcinomas (at protein level). Expressed in fetal brain. Expressed in lung, amygdala, eye, prostate, pancreatic and prostate cancers, head and neck tumors and embryonal tumor. {ECO:0000269|PubMed:12964048, ECO:0000269|PubMed:17129358, ECO:0000269|PubMed:17309600}.; colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;head and neck;kidney;mammary gland;stomach;peripheral nerve; . 0.49572 0.20000 -1.473536006 3.727294173 883.69076 5.78927 BCL9P1 . . . B-cell CLL/lymphoma 9 pseudogene 1 . . . . . . . . . . . BCL10 0.118213218716406 0.855705530094449 0.0260812511891448 B-cell CLL/lymphoma 10 FUNCTION: Involved in adaptive immune response (PubMed:25365219). Promotes apoptosis, pro-caspase-9 maturation and activation of NF- kappa-B via NIK and IKK. May be an adapter protein between upstream TNFR1-TRADD-RIP complex and the downstream NIK-IKK-IKAP complex. Is a substrate for MALT1 (PubMed:18264101). {ECO:0000269|PubMed:18264101, ECO:0000269|PubMed:25365219}.; DISEASE: Note=A chromosomal aberration involving BCL10 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(1;14)(p22;q32). Although the BCL10/IgH translocation leaves the coding region of BCL10 intact, frequent BCL10 mutations could be attributed to the Ig somatic hypermutation mechanism resulting in nucleotide transitions.; DISEASE: Immunodeficiency 37 (IMD37) [MIM:616098]: A form of primary combined immunodeficiency, a group of disorders characterized by severe recurrent infections, with normal numbers or an absence of T and B lymphocytes, and impaired cellular and humoral immunity. IMD37 is characterized by hypogammaglobulinemia without lymphopenia, but with profoundly reduced memory B cells and memory T cells, and increased numbers of circulating naive lymphocytes. Inheritance is autosomal recessive. {ECO:0000269|PubMed:25365219}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; unclassifiable (Anatomical System);cartilage;heart;ovary;colon;skin;skeletal muscle;bone marrow;breast;uterus;pancreas;lung;endometrium;bone;visual apparatus;liver;testis;amniotic fluid;cervix;spleen;germinal center;kidney;peripheral nerve; atrioventricular node;whole blood; 0.75946 0.26603 0.281220278 71.07808445 749.70865 5.43059 BCL11A 0.828999684744843 0.170844975411558 0.000155339843598259 B-cell CLL/lymphoma 11A FUNCTION: Functions as a myeloid and B-cell proto-oncogene. May play important roles in leukemogenesis and hematopoiesis. An essential factor in lymphopoiesis, is required for B-cell formation in fetal liver. May function as a modulator of the transcriptional repression activity of ARP1 (By similarity). {ECO:0000250}.; DISEASE: Note=Chromosomal aberrations involving BCL11A may be a cause of lymphoid malignancies. Translocation t(2;14)(p13;q32.3) causes BCL11A deregulation and amplification. {ECO:0000269|PubMed:11719382}.; TISSUE SPECIFICITY: Expressed at high levels in brain, spleen thymus, bone marrow and testis. Expressed in CD34-positive myeloid precursor cells, B-cells, monocytes and megakaryocytes. Expression is tightly regulated during B-cell development. {ECO:0000269|PubMed:11161790, ECO:0000269|PubMed:11719382}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;frontal lobe;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;pharynx;blood;lung;cornea;placenta;hippocampus;visual apparatus;liver;head and neck;kidney;mammary gland;thymus; medulla oblongata;superior cervical ganglion;fetal brain;globus pallidus;caudate nucleus;pons;skeletal muscle;parietal lobe; 0.66876 0.16967 -1.155457828 6.168907761 22.77118 0.76110 BCL11B 0.929785241868294 0.0701403070405991 7.44510911067505e-05 B-cell CLL/lymphoma 11B FUNCTION: Tumor-suppressor protein involved in T-cell lymphomas. May function on the P53-signaling pathway. May be a key regulator of both differentiation and survival during thymocyte development. Repress transcription through direct, TFCOUP2-independent binding to a GC-rich response element (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in brain and in malignant T- cell lines derived from patients with adult T-cell leukemia/lymphoma.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;blood;skin;bone marrow;whole body;lung;frontal lobe;larynx;nasopharynx;bone;placenta;testis;head and neck;brain; superior cervical ganglion;thymus; 0.70076 0.16232 . . 29.1619 0.93217 BCLAF1 . . . BCL2 associated transcription factor 1 FUNCTION: Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269|PubMed:18794151}.; . TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;gall bladder;amygdala;cartilage;heart;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;pineal gland;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;small intestine;islets of Langerhans;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;amnion;hypopharynx;duodenum;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;occipital lobe;superior cervical ganglion;subthalamic nucleus;smooth muscle;prefrontal cortex;globus pallidus;white blood cells;atrioventricular node;trigeminal ganglion; 0.85841 0.18154 1.987926294 97.63505544 3652.78199 11.74717 BCLAF1P1 . . . BCL2 associated transcription factor 1 pseudogene 1 . . . . . . . . . . . BCLAF1P2 . . . BCL2 associated transcription factor 1 pseudogene 2 . . . . . . . . . . . BCO1 . . . beta-carotene oxygenase 1 FUNCTION: Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism. {ECO:0000269|PubMed:24668807}.; DISEASE: Hypercarotenemia and vitamin A deficiency, autosomal dominant (ADHVAD) [MIM:115300]: A disorder characterized by increased serum beta-carotene, decreased conversion of beta- carotene to vitamin A and decreased serum vitamin A. {ECO:0000269|PubMed:17951468}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.09269 . 0.404185162 76.48619958 . . BCO2 1.83157881067306e-13 0.0547954540966985 0.945204545903118 beta-carotene oxygenase 2 FUNCTION: Asymmetrically cleaves beta-carotene at the 9',10' double bond resulting in the formation of beta-apo-10'-carotenal and beta-ionone. Besides beta-carotene, lycopene is also oxidatively cleaved. The apocarotenals formed by this enzyme may be the precursors for the biosynthesis of retinoic acid or exert unknown physiological effects. {ECO:0000269|PubMed:21106934}.; . TISSUE SPECIFICITY: Highly expressed in retinal pigment epithelium. Also expressed in stomach, small intestine, liver, testis, kidney, adrenal gland, pancreas, heart, skeletal muscle and prostate (at protein level). {ECO:0000269|PubMed:15983114}.; unclassifiable (Anatomical System);meninges;ovary;islets of Langerhans;adrenal cortex;fovea centralis;choroid;lens;skin;retina;pancreas;optic nerve;pia mater;lung;endometrium;nasopharynx;thyroid;bone;macula lutea;hippocampus;liver;cervix;dura mater;brain; dorsal root ganglion;superior cervical ganglion;hypothalamus;globus pallidus;ciliary ganglion;atrioventricular node; 0.04988 0.10872 1.690270544 96.40835103 109.59768 2.27466 BCOR 0.999945621390125 5.43786010909912e-05 8.78363540231984e-12 BCL6 corepressor FUNCTION: Transcriptional corepressor. May specifically inhibit gene expression when recruited to promoter regions by sequence- specific DNA-binding proteins such as BCL6 and MLLT3. This repression may be mediated at least in part by histone deacetylase activities which can associate with this corepressor. Involved in the repression of TFAP2A; impairs binding of BCL6 and KDM2B to TFAP2A promoter regions. Via repression of TFAP2A acts as a negative regulator of osteo-dentiogenic capacity in adult stem cells; the function implies inhibition of methylation on histone H3 'Lys-4' (H3K4me3) and 'Lys-36' (H3K36me2). {ECO:0000269|PubMed:10898795, ECO:0000269|PubMed:15004558, ECO:0000269|PubMed:18280243, ECO:0000269|PubMed:19578371, ECO:0000269|PubMed:23911289}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10898795}.; smooth muscle;colon;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;testis;germinal center;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.36796 0.12570 -3.028489223 0.507195093 113.75272 2.32443 BCORL1 0.981790311640066 0.0182096669987023 2.1361231844055e-08 BCL6 corepressor-like 1 FUNCTION: Transcriptional corepressor. May specifically inhibit gene expression when recruited to promoter regions by sequence- specific DNA-binding proteins such as BCL6. This repression may be mediated at least in part by histone deacetylase activities which can associate with this corepressor. {ECO:0000269|PubMed:17379597}.; . TISSUE SPECIFICITY: Detected in testis and prostate. Detected at lower levels in peripheral blood leukocytes and spleen. {ECO:0000269|PubMed:17379597}.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;optic nerve;larynx;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;lens;pancreas;lung;placenta;macula lutea;hippocampus;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.19294 0.10464 -2.120333794 1.52158528 206.9996 3.10957 BCORP1 . . . BCL6 corepressor pseudogene 1 . . . . . . . . . . . BCR 0.999967224797783 3.27752021126173e-05 1.04772411112926e-13 breakpoint cluster region FUNCTION: GTPase-activating protein for RAC1 and CDC42. Promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them. Displays serine/threonine kinase activity. {ECO:0000269|PubMed:1657398, ECO:0000269|PubMed:1903516}.; DISEASE: Leukemia, chronic myeloid (CML) [MIM:608232]: A clonal myeloproliferative disorder of a pluripotent stem cell with a specific cytogenetic abnormality, the Philadelphia chromosome (Ph), involving myeloid, erythroid, megakaryocytic, B-lymphoid, and sometimes T-lymphoid cells, but not marrow fibroblasts. {ECO:0000269|PubMed:2407300, ECO:0000269|PubMed:3107980, ECO:0000269|PubMed:3540951}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Note=A chromosomal aberration involving BCR has been found in patients with chronic myeloid leukemia. Translocation t(9;22)(q34;q11) with ABL1. The translocation produces a BCR-ABL found also in acute myeloid leukemia (AML) and acute lymphoblastic leukemia (ALL). {ECO:0000269|PubMed:3107980, ECO:0000269|PubMed:7665185}.; . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;cartilage;heart;urinary;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;aorta; amygdala;superior cervical ganglion;medulla oblongata;placenta;globus pallidus;ciliary ganglion;pons;atrioventricular node;caudate nucleus; 0.27882 0.76444 -1.253015116 5.360934183 625.45504 5.04431 BCRP1 . . . breakpoint cluster region pseudogene 1 . . . . . . . . . . . BCRP2 . . . breakpoint cluster region pseudogene 2 . . . . . . . . . . . BCRP3 . . . breakpoint cluster region pseudogene 3 . . . . . . . . . . . BCRP4 . . . breakpoint cluster region pseudogene 4 . . . . . . . . . . . BCRP5 . . . breakpoint cluster region pseudogene 5 . . . . . . . . . . . BCRP6 . . . breakpoint cluster region pseudogene 6 . . . . . . . . . . . BCRP7 . . . breakpoint cluster region pseudogene 7 . . . . . . . . . . . BCRP8 . . . breakpoint cluster region pseudogene 8 . . . . . . . . . . . BCRP9 . . . breakpoint cluster region pseudogene 9 . . . . . . . . . . . BCS1L 2.2774208943895e-08 0.685806779917177 0.314193197308614 BCS1 homolog, ubiquinol-cytochrome c reductase complex chaperone FUNCTION: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III. Plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. {ECO:0000269|PubMed:18628306}.; DISEASE: Mitochondrial complex III deficiency, nuclear 1 (MC3DN1) [MIM:124000]: A disorder of the mitochondrial respiratory chain resulting in a highly variable phenotype depending on which tissues are affected. Clinical features include mitochondrial encephalopathy, psychomotor retardation, ataxia, severe failure to thrive, liver dysfunction, renal tubulopathy, muscle weakness and exercise intolerance. {ECO:0000269|PubMed:11528392, ECO:0000269|PubMed:12910490, ECO:0000269|PubMed:17314340, ECO:0000269|PubMed:17403714, ECO:0000269|PubMed:19162478, ECO:0000269|PubMed:22991165}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bjoernstad syndrome (BJS) [MIM:262000]: An autosomal recessive disease characterized by congenital sensorineural hearing loss and twisted hairs (pili torti). Pili torti is a condition in which the hair shafts are flattened at irregular intervals and twisted 180 degrees from the normal axis, making the hair extremely brittle. {ECO:0000269|PubMed:17314340, ECO:0000269|PubMed:24172246}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9878253}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;thyroid;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.18102 0.65370 -0.624497208 17.16206653 591.5681 4.93019 BCYRN1 . . . brain cytoplasmic RNA 1 . . . . . . . . . . . BCYRN1P1 . . . brain cytoplasmic RNA 1, pseudogene 1 . . . . . . . . . . . BCYRN1P2 . . . brain cytoplasmic RNA 1, pseudogene 2 . . . . . . . . . . . BCYRN1P3 . . . brain cytoplasmic RNA 1, pseudogene 3 . . . . . . . . . . . BDH1 0.000383112941167296 0.841931335480589 0.157685551578244 3-hydroxybutyrate dehydrogenase, type 1 . . . colon;fovea centralis;choroid;skin;retina;optic nerve;frontal lobe;endometrium;larynx;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;lacrimal gland;muscle;lens;pancreas;lung;macula lutea;liver;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; liver; 0.16316 0.26949 0.420771676 77.15852795 75.82268 1.82489 BDH2 4.05062122865546e-06 0.376298011660851 0.62369793771792 3-hydroxybutyrate dehydrogenase, type 2 FUNCTION: Dehydrogenase that mediates the formation of 2,5- dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural similarities with bacterial enterobactin and associates with LCN2, thereby playing a key role in iron homeostasis and transport. Also acts as a 3-hydroxybutyrate dehydrogenase (By similarity). {ECO:0000250, ECO:0000269|PubMed:16380372}.; . . myocardium;smooth muscle;ovary;developmental;colon;parathyroid;choroid;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;spinal cord;adrenal cortex;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;mesenchyma;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; thyroid;kidney; 0.14543 0.13572 0.21689899 68.12927577 187.57451 2.97448 BDH2P1 . . . 3-hydroxybutyrate dehydrogenase, type 2 pseudogene 1 . . . . . . . . . . . BDKRB1 0.07010469248697 0.872062337390892 0.0578329701221382 bradykinin receptor B1 FUNCTION: This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation.; . . unclassifiable (Anatomical System);cartilage;bone;liver;skin; superior cervical ganglion;atrioventricular node; 0.09114 0.18561 -0.044015879 50.44821892 145.62454 2.62997 BDKRB2 0.269901202726925 0.70548256254783 0.0246162347252455 bradykinin receptor B2 FUNCTION: Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system.; . TISSUE SPECIFICITY: Ubiquitous. Widespread in normal smooth muscle tissue and neurons. {ECO:0000269|PubMed:7835885}.; unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;skin;skeletal muscle;uterus;lung;larynx;placenta;thyroid;testis;head and neck;kidney;stomach; trigeminal ganglion; 0.12832 0.33012 0.398725314 76.35645199 232.12245 3.29382 BDNF 0.946719308479018 0.0530986910465837 0.000182000474398723 brain-derived neurotrophic factor FUNCTION: During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. Participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability. {ECO:0000269|PubMed:12553913}.; DISEASE: Bulimia nervosa 2 (BULN2) [MIM:610269]: A psychiatric disorder characterized by eating an unusually large amount of food in a short period of time, followed by inappropriate acts (purging) to avert weight gain. Compensatory behavior includes self-induced vomiting, laxative abuse, and excessive exercise. {ECO:0000269|PubMed:15115760}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Congenital central hypoventilation syndrome (CCHS) [MIM:209880]: Rare disorder characterized by abnormal control of respiration in the absence of neuromuscular or lung disease, or an identifiable brain stem lesion. A deficiency in autonomic control of respiration results in inadequate or negligible ventilatory and arousal responses to hypercapnia and hypoxemia. {ECO:0000269|PubMed:11840487}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Brain. Highly expressed in hippocampus, amygdala, cerebral cortex and cerebellum. Also expressed in heart, lung, skeletal muscle, testis, prostate and placenta. {ECO:0000269|PubMed:17629449}.; unclassifiable (Anatomical System);cartilage;heart;ovary;parathyroid;skin;uterus;prostate;lung;adrenal gland;placenta;thyroid;visual apparatus;liver;testis;spleen;brain; . 0.87407 0.82123 0.43736446 77.56546355 2261.17843 8.78528 BDNF-AS . . . BDNF antisense RNA . . . . . . . . . . . BDP1 4.37097990000324e-11 0.999999989940482 1.00158085371442e-08 B double prime 1, subunit of RNA polymerase III transcription initiation factor IIIB FUNCTION: General activator of RNA polymerase III transcription. Requires for transcription from all three types of polymerase III promoters. Requires for transcription of genes with internal promoter elements and with promoter elements upstream of the initiation site. {ECO:0000269|PubMed:11040218}.; . TISSUE SPECIFICITY: Isoform 2 is highly expressed in cerebellum. {ECO:0000269|PubMed:11161782}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;cervix;kidney;mammary gland;stomach;aorta;cerebellum; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;fetal brain;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.23466 0.06953 2.388915264 98.48431234 3262.01073 10.89109 BDP1P . . . B double prime 1 pseudogene . . . . . . . . . . . BEAN1 . . . brain expressed, associated with NEDD4, 1 . DISEASE: Spinocerebellar ataxia 31 (SCA31) [MIM:117210]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA31 belongs to the autosomal dominant cerebellar ataxias type III (ADCA III) which are characterized by pure cerebellar ataxia without additional signs. {ECO:0000269|PubMed:19878914}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;lung;tongue;placenta;visual apparatus;liver;testis;spleen;head and neck;brain;thymus; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . . . 81.67643 1.91471 BEAN1-AS1 . . . BEAN1 antisense RNA 1 . . . . . . . . . . . BECN1 0.998697775912791 0.00130220394661343 2.0140595508516e-08 beclin 1, autophagy related FUNCTION: Plays a central role in autophagy (PubMed:23184933). Acts as core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3- C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20643123, PubMed:20208530). Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis (PubMed:25275521). Protects against infection by a neurovirulent strain of Sindbis virus (PubMed:9765397). May play a role in antiviral host defense. {ECO:0000269|PubMed:20208530, ECO:0000269|PubMed:20643123, ECO:0000269|PubMed:23184933, ECO:0000269|PubMed:25275521, ECO:0000269|PubMed:9765397, ECO:0000305}.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;oesophagus;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;placenta;head and neck;kidney;stomach;aorta;thymus;cerebellum; amygdala;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.51202 0.11124 -0.183570861 39.95046001 28.42549 0.90994 BECN1P2 . . . beclin 1, autophagy related, pseudogene 2 . . . . . . . . . . . BECN2 . . . beclin 2 FUNCTION: Involved in 2 distinct lysosomal degradation pathways: acts as a regulator of autophagy and as a regulator of G-protein coupled receptors turnover. Regulates degradation in lysosomes of a variety of G-protein coupled receptors via its interaction with GPRASP1/GASP1. {ECO:0000269|PubMed:23954414}.; . TISSUE SPECIFICITY: Present in fetal and adult brain (at protein level). {ECO:0000269|PubMed:23954414}.; . . . . . . . . BEGAIN 0.890710074727172 0.109057883315808 0.000232041957019886 brain enriched guanylate kinase associated FUNCTION: May sustain the structure of the postsynaptic density (PSD).; . . unclassifiable (Anatomical System);islets of Langerhans;blood;bone marrow;uterus;lung;optic nerve;frontal lobe;placenta;hippocampus;testis;cervix;brain; superior cervical ganglion;prefrontal cortex;globus pallidus;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.15443 0.10913 -0.600630256 18.06440198 2832.62632 10.04643 BEND2 0.348216589536089 0.651208166102952 0.000575244360959144 BEN domain containing 2 . . . . . 0.04574 0.05824 0.687150476 85.17928757 177.40866 2.89504 BEND3 0.498328912747109 0.500774943327924 0.000896143924966531 BEN domain containing 3 FUNCTION: Transcriptional repressor which associates with the NoRC (nucleolar remodeling complex) complex and plays a key role in repressing rDNA transcription. The sumoylated form modulates the stability of the NoRC complex component BAZ2A/TIP5 by controlling its USP21-mediated deubiquitination (PubMed:21914818, PubMed:26100909). Binds to unmethylated major satellite DNA and is involved in the recruitment of the Polycomb repressive complex 2 (PRC2) to major satellites (By similarity). {ECO:0000250|UniProtKB:Q6PAL0, ECO:0000269|PubMed:21914818, ECO:0000269|PubMed:26100909}.; . TISSUE SPECIFICITY: Expressed at least in heart, kidney, liver, ovary and spleen, with highest levels in spleen and lowest in heart. Expressed on the surface of T cells. {ECO:0000269|PubMed:21914818, ECO:0000269|PubMed:25400923}.; . . 0.76000 0.11113 -1.059995566 7.537154989 70.36421 1.74484 BEND3P1 . . . BEN domain containing 3 pseudogene 1 . . . . . . . . . . . BEND3P2 . . . BEN domain containing 3 pseudogene 2 . . . . . . . . . . . BEND3P3 . . . BEN domain containing 3 pseudogene 3 . . . . . . . . . . . BEND4 0.986764685888198 0.0132295048913445 5.80922045698344e-06 BEN domain containing 4 . . . . . 0.40364 0.10688 0.240763792 69.36777542 153.07148 2.70632 BEND5 0.114990689141033 0.857716611807692 0.0272926990512748 BEN domain containing 5 FUNCTION: Acts as a transcriptional repressor (PubMed:23468431). {ECO:0000269|PubMed:23468431}.; . . unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;whole body;lung;cochlea;thyroid;bone;macula lutea;iris;head and neck;germinal center;brain;tonsil; . 0.62579 0.11262 -0.271755481 34.31823543 38.21221 1.13413 BEND6 0.135146272891265 0.844040833119173 0.0208128939895622 BEN domain containing 6 FUNCTION: Acts as a corepressor of recombining binding protein suppressor hairless (RBPJ) and inhibits Notch signaling in neural stem cells, thereby opposing their self-renewal and promoting neurogenesis (PubMed:23571214). {ECO:0000269|PubMed:23571214}.; . . unclassifiable (Anatomical System);uterus;prostate;lung;heart;larynx;hippocampus;head and neck;brain;skin; . 0.24501 . -0.339715008 30.06605331 48.9948 1.36748 BEND7 0.01119032203323 0.97993721050799 0.00887246745877974 BEN domain containing 7 . . . unclassifiable (Anatomical System);whole body;visual apparatus;adrenal medulla;kidney; testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion; 0.11532 . -0.334253673 30.70299599 400.83401 4.20043 BEND7P1 . . . BEN domain containing 7 pseudogene 1 . . . . . . . . . . . BEST1 4.88561552823397e-08 0.382275053416834 0.617724897727011 bestrophin 1 FUNCTION: Forms calcium-sensitive chloride channels. Highly permeable to bicarbonate. {ECO:0000269|PubMed:11904445, ECO:0000269|PubMed:12907679, ECO:0000269|PubMed:18400985}.; DISEASE: Macular dystrophy, vitelliform, 2 (VMD2) [MIM:153700]: An autosomal dominant form of macular degeneration that usually begins in childhood or adolescence. VMD2 is characterized by typical 'egg-yolk' macular lesions due to abnormal accumulation of lipofuscin within and beneath the retinal pigment epithelium cells. Progression of the disease leads to destruction of the retinal pigment epithelium and vision loss. {ECO:0000269|PubMed:10331951, ECO:0000269|PubMed:10394929, ECO:0000269|PubMed:10453731, ECO:0000269|PubMed:10682987, ECO:0000269|PubMed:10798642, ECO:0000269|PubMed:11241846, ECO:0000269|PubMed:11449320, ECO:0000269|PubMed:12187431, ECO:0000269|PubMed:12324875, ECO:0000269|PubMed:13129869, ECO:0000269|PubMed:14517959, ECO:0000269|PubMed:15176385, ECO:0000269|PubMed:18766995, ECO:0000269|PubMed:19357557, ECO:0000269|PubMed:9662395, ECO:0000269|PubMed:9700209}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa 50 (RP50) [MIM:613194]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:19853238}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bestrophinopathy, autosomal recessive (ARB) [MIM:611809]: A retinopathy characterized by loss of central vision, an absent electro-oculogram light rise, and electroretinogram anomalies. {ECO:0000269|PubMed:18179881}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Vitreoretinochoroidopathy, autosomal dominant (ADVIRC) [MIM:193220]: A disorder characterized by vitreoretinochoroidal dystrophy. The clinical presentation is variable. VRCP may be associated with cataract, nanophthalmos, microcornea, shallow anterior chamber, and glaucoma. {ECO:0000269|PubMed:15452077}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in the basolateral membrane of the retinal pigment epithelium.; ovary;salivary gland;colon;substantia nigra;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;thyroid;bone;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;blood;lens;breast;pancreas;pia mater;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.13360 0.15669 -0.21856543 37.66218448 827.66408 5.64109 BEST2 9.01637143288031e-11 0.078836196442374 0.921163803467462 bestrophin 2 FUNCTION: Forms calcium-sensitive chloride channels. Permeable to bicarbonate. {ECO:0000269|PubMed:11904445, ECO:0000269|PubMed:12907679, ECO:0000269|PubMed:18400985}.; . TISSUE SPECIFICITY: Mainly confined to the retinal pigment epithelium and colon. {ECO:0000269|PubMed:12032738}.; unclassifiable (Anatomical System);iris;testis;colon;stomach; superior cervical ganglion;medulla oblongata;caudate nucleus;trigeminal ganglion; 0.14885 0.11494 0.308721233 72.59966973 539.74211 4.73363 BEST3 3.69441601591338e-17 0.00138060637331172 0.998619393626688 bestrophin 3 FUNCTION: Forms calcium-sensitive chloride channels. Permeable to bicarbonate. {ECO:0000269|PubMed:12907679}.; . TISSUE SPECIFICITY: Present in skeletal muscle and weakly in brain, spinal cord, bone marrow and retina. {ECO:0000269|PubMed:12032738}.; unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;skin;skeletal muscle;uterus;whole body;lung;larynx;alveolus;liver;head and neck;spleen;brain;peripheral nerve; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;ovary;tongue;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.14764 0.10434 0.134171522 63.57041755 1059.3782 6.24526 BEST4 0.00309511388143714 0.9454345301037 0.0514703560148628 bestrophin 4 FUNCTION: Forms calcium-sensitive chloride channels. Permeable to bicarbonate. {ECO:0000269|PubMed:12907679, ECO:0000269|PubMed:18400985}.; . TISSUE SPECIFICITY: Predominantly found in colon and the weakly in fetal brain, spinal cord, retina, lung, trachea, testis and placenta. {ECO:0000269|PubMed:12032738}.; . . 0.16251 0.13791 -0.60427181 17.74593064 1100.45975 6.34843 BET1 0.00201119979865631 0.50098006285712 0.497008737344224 Bet1 golgi vesicular membrane trafficking protein FUNCTION: Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE involved in the docking process of ER-derived vesicles with the cis-Golgi membrane (By similarity). {ECO:0000250}.; . . medulla oblongata;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;placenta;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06250 0.09037 -0.009020804 52.8544468 . . BET1L 0.378367596560038 0.575938362137659 0.0456940413023023 Bet1 golgi vesicular membrane trafficking protein like FUNCTION: Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex (By similarity). {ECO:0000250|UniProtKB:O35152}.; . . medulla oblongata;umbilical cord;ovary;salivary gland;intestine;colon;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pineal body;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;placenta;visual apparatus;alveolus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12389 . -0.383807564 27.41802312 130.06232 2.48473 BET1P1 . . . Bet1 golgi vesicular membrane trafficking protein pseudogene 1 . . . . . . . . . . . BEX1 0.572647843193304 0.381640927354703 0.0457112294519933 brain expressed X-linked 1 FUNCTION: Signaling adapter molecule involved in p75NTR/NGFR signaling. Plays a role in cell cycle progression and neuronal differentiation. Inhibits neuronal differentiation in response to nerve growth factor (NGF). May act as a link between the cell cycle and neurotrophic factor signaling, possibly by functioning as an upstream modulator of receptor signaling, coordinating biological responses to external signals with internal cellular states (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in central nervous system, with high level in pituitary, cerebellum and temporal lobe. Expressed in lung, skeletal muscle, peripheral blood leukocyte, stomach, lymph node, trachea and bone marrow. Highly expressed in acute myeloid leukemia. {ECO:0000269|PubMed:11989783, ECO:0000269|PubMed:15920485, ECO:0000269|PubMed:15958283}.; . . 0.16417 0.43058 -0.053113545 49.38664779 5.34317 0.19855 BEX2 0.592514905495088 0.367723968902919 0.0397611256019934 brain expressed X-linked 2 FUNCTION: Regulator of mitochondrial apoptosis and G1 cell cycle in breast cancer. Protects the breast cancer cells against mitochondrial apoptosis and this effect is mediated through the modulation of BCL2 protein family, which involves the positive regulation of anti-apoptotic member BCL2 and the negative regulation of pro-apoptotic members BAD, BAK1 and PUMA. Required for the normal cell cycle progression during G1 in breast cancer cells through the regulation of CCND1 and CDKN1A. Regulates the level of PP2A regulatory subunit B and PP2A phosphatase activity. {ECO:0000269|PubMed:19711341}.; . TISSUE SPECIFICITY: Expressed in central nervous system, with high level in pituitary, cerebellum and temporal lobe. Widely expressed in breast cancer cell lines. {ECO:0000269|PubMed:15958283, ECO:0000269|PubMed:19711341}.; . . 0.15554 0.09529 0.635788962 83.63411182 48.01922 1.34654 BEX3 . . . brain expressed X-linked 3 FUNCTION: May be a signaling adapter molecule involved in p75NTR- mediated apoptosis induced by NGF. Plays a role in zinc-triggered neuronal death (By similarity). May play an important role in the pathogenesis of neurogenetic diseases. {ECO:0000250}.; . TISSUE SPECIFICITY: Found in ovarian granulosa cells, testis, prostate and seminal vesicle tissue. High levels also detected in liver. {ECO:0000269|PubMed:15958283}.; . . 0.16160 . -0.009020804 52.8544468 . . BEX4 0.673985987212613 0.30505092534552 0.0209630874418667 brain expressed X-linked 4 . . . . . 0.28142 . -0.031067188 51.03798066 1.29244 0.04666 BEX5 0.0163388827467428 0.470094536268737 0.513566580984521 brain expressed X-linked 5 . . . unclassifiable (Anatomical System);ovary;cerebellum cortex;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;whole body;endometrium;placenta;macula lutea;kidney;brain; amygdala;whole brain;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;pituitary;cingulate cortex; 0.06841 0.06745 0.079165051 59.43029016 1.56449 0.05182 BFAR 0.00230974824450457 0.98037036382008 0.0173198879354159 bifunctional apoptosis regulator FUNCTION: Apoptosis regulator. Has anti-apoptotic activity, both for apoptosis triggered via death-receptors and via mitochondrial factors. {ECO:0000269|PubMed:14502241}.; . TISSUE SPECIFICITY: Expressed highly in brain, moderately in small intestine, weakly in testes and only faintly in liver and skeletal muscle. Not expressed in heart, kidney, lung and spleen. {ECO:0000269|PubMed:10716992, ECO:0000269|PubMed:14502241}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;medulla oblongata;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.36833 0.10433 0.064394823 58.84642604 2191.44041 8.62057 BFSP1 0.000105944351029142 0.813868683385158 0.186025372263813 beaded filament structural protein 1 . . TISSUE SPECIFICITY: Lens.; . . 0.16061 0.12426 0.044168103 57.40740741 471.46095 4.49340 BFSP2 6.66210219090541e-05 0.905035916230917 0.0948974627471739 beaded filament structural protein 2 FUNCTION: Involved in stabilization of lens fiber cell cytoskeleton. {ECO:0000250|UniProtKB:Q6NVD9}.; . TISSUE SPECIFICITY: Lens.; unclassifiable (Anatomical System);lung;visual apparatus;testis;lens; superior cervical ganglion;temporal lobe;trigeminal ganglion; 0.33546 0.11314 -0.380166007 27.88393489 276.51947 3.56019 BFSP2-AS1 . . . BFSP2 antisense RNA 1 . . . . . . . . . . . BGLAP 1.75722490280257e-05 0.142350943895568 0.857631483855404 bone gamma-carboxyglutamate protein FUNCTION: Constitutes 1-2% of the total bone protein. It binds strongly to apatite and calcium.; . . . . . 0.26210 0.481458261 79.03986789 103.96446 2.20327 BGLT3 . . . beta globin locus transcript 3 (non-protein coding) . . . . . . . . . . . BGN 0.916364713344778 0.0830680073799688 0.000567279275253473 biglycan FUNCTION: May be involved in collagen fiber assembly. {ECO:0000250}.; . TISSUE SPECIFICITY: Found in several connective tissues, especially in articular cartilages.; smooth muscle;ovary;salivary gland;sympathetic chain;colon;choroid;skin;retina;bone marrow;uterus;whole body;endometrium;synovium;larynx;bone;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;urinary;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;epididymis;placenta;visual apparatus;hippocampus;hypopharynx;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;heart;adrenal gland;placenta;adrenal cortex;ciliary ganglion;trigeminal ganglion; 0.96548 0.11669 -0.159704656 41.90846898 67.21095 1.69600 BHLHA9 . . . basic helix-loop-helix family member a9 FUNCTION: Transcription factor, which play a role in limb development. Is an essential player in the regulatory network governing transcription of genes implicated in limb morphogenesis. {ECO:0000269|PubMed:22147889, ECO:0000269|PubMed:25466284}.; DISEASE: Split-hand/foot malformation with long bone deficiency 3 (SHFLD3) [MIM:612576]: A disease characterized by the association of split-hand/foot malformation with long bone deficiency involving the tibia and fibula. Split-hand/foot malformation is a limb malformation involving the central rays of the autopod. Phenotypic expression is extremely variable between and within families, and even between limbs of a single patient, ranging from syndactyly and oligodactyly to the most severe monodactyly with only a single phalanx. Limb features include median clefts of the hands and feet, and aplasia and/or hypoplasia of the phalanges, metacarpals, and metatarsals. {ECO:0000269|PubMed:22147889}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry. A copy number variation (CNV) resulting in BHLHA9 duplications is a necessary but not sufficient susceptibility factor for Split-hand/foot malformation with long bone deficiency, a highly variable phenotype with reduced penetrance, particularly in females (PubMed:22147889). {ECO:0000269|PubMed:22147889}.; DISEASE: Syndactyly, mesoaxial synostotic, with phalangeal reduction (MSSD) [MIM:609432]: An autosomal recessive, non- syndromic digit anomaly characterized by mesoaxial osseous synostosis at a metacarpal level, reduction of one or more phalanges, hypoplasia of distal phalanges of preaxial and postaxial digits, clinodactyly of fifth fingers, and preaxial fusion of toes. {ECO:0000269|PubMed:25466284}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . . . . 13.47449 0.48957 BHLHA15 0.14284139616861 0.628359636054921 0.228798967776469 basic helix-loop-helix family member a15 FUNCTION: Plays a role in controlling the transcriptional activity of MYOD1, ensuring that expanding myoblast populations remain undifferentiated. Repression may occur through muscle-specific E- box occupancy by homodimers. May also negatively regulate bHLH- mediated transcription through an N-terminal repressor domain. Serves as a key regulator of acinar cell function, stability, and identity. Also required for normal organelle localization in exocrine cells and for mitochondrial calcium ion transport. May function as a unique regulator of gene expression in several different embryonic and postnatal cell lineages. Binds to the E- box consensus sequence 5'-CANNTG-3' (By similarity). {ECO:0000250|UniProtKB:Q9QYC3}.; . TISSUE SPECIFICITY: Expressed in brain, liver, spleen and skeletal muscle. {ECO:0000269|PubMed:14516699}.; germinal center; . 0.48841 0.14967 . . 15.18166 0.54636 BHLHB9 0.370497960484996 0.581327407923377 0.0481746315916266 basic helix-loop-helix domain containing, class B, 9 FUNCTION: May play a role in the control of cellular aging and survival.; . TISSUE SPECIFICITY: Highly expressed in brain. Not expressed in lung or liver. Down-regulated in brain from patients suffering from Alzheimer disease. {ECO:0000269|PubMed:15034937}.; unclassifiable (Anatomical System);prostate;lung;whole body;larynx;testis;spleen;head and neck;brain;stomach; . 0.09401 0.10311 0.284856336 71.40835103 25.62443 0.83529 BHLHB9P1 . . . basic helix-loop-helix domain containing, class B, 9 pseudogene 1 . . . . . . . . . . . BHLHE22 0.677980336838841 0.301773469140902 0.0202461940202565 basic helix-loop-helix family member e22 FUNCTION: Inhibits DNA binding of TCF3/E47 homodimers and TCF3 (E47)/NEUROD1 heterodimers and acts as a strong repressor of Neurod1 and Myod-responsive genes, probably by heterodimerization with class a basic helix-loop-helix factors. Despite the presence of an intact basic domain, does not bind to DNA (By similarity). In the brain, may function as an area-specific transcription factor that regulates the postmitotic acquisition of area identities and elucidate the genetic hierarchy between progenitors and postmitotic neurons driving neocortical arealization. May be required for the survival of a specific population of inhibitory neurons in the superficial laminae of the spinal chord dorsal horn that may regulate pruritis. Seems to play a crucial role in the retinogenesis, in the specification of amacrine and bipolar subtypes. Forms with PRDM8 a transcriptional repressor complex controlling genes involved in neural development and neuronal differentiation. {ECO:0000250|UniProtKB:Q8C6A8}.; . TISSUE SPECIFICITY: Brain-specific, with the highest expression in the cerebellum. {ECO:0000269|PubMed:12213201}.; unclassifiable (Anatomical System);heart;colon;blood;fovea centralis;skin;retina;uterus;prostate;lung;placenta;macula lutea;hippocampus;testis;kidney;brain; . 0.83732 0.19325 . . 465.53138 4.46972 BHLHE23 0.0601229173842303 0.717967514687074 0.221909567928695 basic helix-loop-helix family member e23 FUNCTION: May function as transcriptional repressor. May modulate the expression of genes required for the differentiation and/or maintenance of pancreatic and neuronal cell types. May be important for rod bipolar cell maturation (By similarity). {ECO:0000250}.; . . . . 0.09965 . . . 148.53648 2.65855 BHLHE40 0.941607017631946 0.0581639823765673 0.000228999991486491 basic helix-loop-helix family member e40 FUNCTION: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop). Both these loops are interlocked as it represses the expression of PER1/2 and in turn is repressed by PER1/2 and CRY1/2. Represses the activity of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes. Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2. Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA and NR1H3/LXRA transactivation activity. May be involved in the regulation of chondrocyte differentiation via the cAMP pathway. {ECO:0000269|PubMed:12397359, ECO:0000269|PubMed:14672706, ECO:0000269|PubMed:15193144, ECO:0000269|PubMed:15560782, ECO:0000269|PubMed:18411297, ECO:0000269|PubMed:19786558}.; . TISSUE SPECIFICITY: Expressed in cartilage, spleen, intestine, lung, and to a lesser extent in heart, brain, liver, muscle and stomach.; lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;amygdala;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;amnion;head and neck;kidney;stomach;aorta; superior cervical ganglion; 0.26036 0.29030 -0.314027422 31.9297004 37.76023 1.12347 BHLHE40-AS1 . . . BHLHE40 antisense RNA 1 . . . . . . . . . . . BHLHE41 . . . basic helix-loop-helix family member e41 FUNCTION: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop). Both these loops are interlocked as it represses the expression of PER1 and in turn is repressed by PER1/2 and CRY1/2. Represses the activity of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes. Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2. Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA/B/G, NR1H3/LXRA, NR1H4 and VDR transactivation activity. {ECO:0000269|PubMed:11278948, ECO:0000269|PubMed:14672706, ECO:0000269|PubMed:15193144, ECO:0000269|PubMed:15560782, ECO:0000269|PubMed:18411297, ECO:0000269|PubMed:19786558}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle and brain, moderately expressed in pancreas and heart, weakly expressed in placenta, lung, liver and kidney.; ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;thyroid;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;islets of Langerhans;hypothalamus;pineal body;urinary;lens;skeletal muscle;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;hippocampus;liver;kidney;mammary gland;cerebellum; amygdala;whole brain;medulla oblongata;occipital lobe;hypothalamus;spinal cord;prefrontal cortex;caudate nucleus;cerebellum; 0.16781 . . . 2859.42498 10.11886 BHMG1 . . . basic helix-loop-helix and HMG-box containing 1 . . . . . . . . . . . BHMT 0.000316952447729784 0.944288005921279 0.055395041630991 betaine--homocysteine S-methyltransferase FUNCTION: Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline.; . TISSUE SPECIFICITY: Found exclusively in liver and kidney. {ECO:0000269|PubMed:9281325}.; unclassifiable (Anatomical System);optic nerve;macula lutea;visual apparatus;liver;spleen;fovea centralis;choroid;kidney;lens;brain;retina; fetal liver;superior cervical ganglion;liver;appendix;kidney;trigeminal ganglion; 0.11067 0.22464 -0.047654689 50.22410946 1865.32323 7.95364 BHMT2 2.73916876646438e-12 0.0103527036164579 0.989647296380803 betaine--homocysteine S-methyltransferase 2 FUNCTION: Involved in the regulation of homocysteine metabolism. Converts homocysteine to methionine using S-methylmethionine (SMM) as a methyl donor. {ECO:0000269|PubMed:18230605}.; . TISSUE SPECIFICITY: Expressed in liver and kidney and at reduced levels in the brain, heart, and skeletal muscle. {ECO:0000269|PubMed:11087663}.; unclassifiable (Anatomical System);uterus;bile duct;hypothalamus;liver;testis;spleen;kidney;skeletal muscle; fetal liver;superior cervical ganglion;liver;ciliary ganglion;kidney;trigeminal ganglion; 0.05535 . 0.174625237 65.9648502 203.91543 3.08285 BICC1 0.571303026474837 0.428696802437991 1.71087171028843e-07 BicC family RNA binding protein 1 FUNCTION: Putative RNA-binding protein. Acts as a negative regulator of Wnt signaling. May be involved in regulating gene expression during embryonic development. {ECO:0000269|PubMed:21922595}.; DISEASE: Renal dysplasia, cystic (CYSRD) [MIM:601331]: An anomaly of the kidney characterized by numerous renal cysts and apparent disorder of differentiation of the renal parenchyma. Kidney of affected individuals lack the normal renal bean shape, and the collection drainage system. The cystic, dysplastic kidney contains undifferentiated mesenchyme, cartilaginous tissue, and immature collecting ducts. {ECO:0000269|PubMed:21922595}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . uterus;lung;heart;kidney;skin; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;skin; 0.20727 0.11765 0.602602982 82.87331918 407.95455 4.23562 BICD1 0.144785241366813 0.855182129176946 3.26294562412035e-05 bicaudal D homolog 1 (Drosophila) FUNCTION: Regulates coat complex coatomer protein I (COPI)- independent Golgi-endoplasmic reticulum transport by recruiting the dynein-dynactin motor complex.; . TISSUE SPECIFICITY: Expressed in the brain, heart and skeletal muscle.; lymphoreticular;ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; subthalamic nucleus;occipital lobe;olfactory bulb;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.30988 0.10044 -1.506435464 3.544468035 59.96654 1.57147 BICD1P1 . . . bicaudal D homolog 1 (Drosophila) pseudogene 1 . . . . . . . . . . . BICD2 0.332593897219712 0.666755321619814 0.000650781160473287 bicaudal D homolog 2 (Drosophila) FUNCTION: May play a role in the dynein-dynactin interactions on the surface of membranous organelles, by associating with these complexes. Regulates coat complex coatomer protein I (COPI)- independent Golgi-endoplasmic reticulum transport by recruiting the dynein-dynactin motor complex (By similarity). {ECO:0000250}.; DISEASE: Spinal muscular atrophy, lower extremity-predominant 2, autosomal dominant (SMALED2) [MIM:615290]: An autosomal dominant form of spinal muscular atrophy characterized by early-childhood onset of muscle weakness and atrophy predominantly affecting the proximal and distal muscles of the lower extremity, although some patients may show upper extremity involvement. The disorder results in delayed walking, waddling gait, difficulty walking, and loss of distal reflexes. Some patients may have foot deformities or hyperlordosis, and some show mild upper motor signs, such as spasticity. Sensation, bulbar function, and cognitive function are preserved. The disorder shows very slow progression throughout life. {ECO:0000269|PubMed:23664116, ECO:0000269|PubMed:23664119, ECO:0000269|PubMed:23664120}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;oral cavity;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach; whole brain;amygdala;occipital lobe;superior cervical ganglion;lung;prefrontal cortex;white blood cells;trigeminal ganglion;whole blood;skin;skeletal muscle;cerebellum; 0.21848 0.11049 -1.394367777 4.246284501 70.28513 1.74285 BID 2.67829587669192e-07 0.0886709022418343 0.911328829928578 BH3 interacting domain death agonist FUNCTION: The major proteolytic product p15 BID allows the release of cytochrome c (By similarity). Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2. {ECO:0000250, ECO:0000269|PubMed:14583606}.; . TISSUE SPECIFICITY: Isoform 2 and isoform 3 are expressed in spleen, bone marrow, cerebral and cerebellar cortex. Isoform 2 is expressed in spleen, pancreas and placenta (at protein level). Isoform 3 is expressed in lung, pancreas and spleen (at protein level). Isoform 4 is expressed in lung and pancreas (at protein level). {ECO:0000269|PubMed:14583606}.; myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; whole brain;liver;globus pallidus;white blood cells;whole blood;trigeminal ganglion; 0.06027 0.11574 -0.137658575 43.57159707 33.63104 1.03804 BIK 2.5374926599392e-05 0.174062785369988 0.825911839703413 BCL2-interacting killer FUNCTION: Accelerates programmed cell death. Association to the apoptosis repressors Bcl-X(L), BHRF1, Bcl-2 or its adenovirus homolog E1B 19k protein suppresses this death-promoting activity. Does not interact with BAX. {ECO:0000269|PubMed:8521816}.; . . unclassifiable (Anatomical System);prostate;lymph node;lung;testis;colon;blood;kidney;germinal center;brain;skin;stomach;bone marrow; superior cervical ganglion;tumor; 0.07884 0.20009 0.215080721 67.91696155 53.17474 1.44793 BIN1 0.474193121768888 0.525762514445149 4.43637859629206e-05 bridging integrator 1 FUNCTION: May be involved in regulation of synaptic vesicle endocytosis. May act as a tumor suppressor and inhibits malignant cell transformation.; DISEASE: Myopathy, centronuclear, 2 (CNM2) [MIM:255200]: A congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers. {ECO:0000269|PubMed:17676042}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Highest expression in the brain and muscle. Isoform IIA is expressed only in the brain where it is concentrated in axon initial segments and nodes of Ranvier. Isoform BIN1 is widely expressed with highest expression in skeletal muscle. {ECO:0000269|PubMed:10903846}.; ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;brain;tonsil;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;placenta;hippocampus;amnion;head and neck;kidney;stomach;thymus; whole brain;amygdala;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;spinal cord;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;thyroid;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.22561 0.20155 -0.754958418 13.57631517 298.1041 3.68288 BIN2 0.000209938130106231 0.99513410963734 0.00465595223255405 bridging integrator 2 FUNCTION: Promotes cell motility and migration, probably via its interaction with the cell membrane and with podosome proteins that mediate interaction with the cytoskeleton. Modulates membrane curvature and mediates membrane tubulation. Plays a role in podosome formation. Inhibits phagocytosis. {ECO:0000269|PubMed:23285027}.; . TISSUE SPECIFICITY: Detected in natural killer cells (at protein level). Highest level expression seen in spleen and peripheral blood leukocytes and is also expressed at high levels in thymus, colon and placenta, suggesting preferential expression in hematopoietic tissues. {ECO:0000269|PubMed:10903846, ECO:0000269|PubMed:23285027}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;colon;blood;choroid;skin;bone marrow;uterus;whole body;lung;nasopharynx;placenta;liver;testis;head and neck;spleen;kidney;germinal center;brain;thymus; superior cervical ganglion;lymph node;white blood cells;whole blood;tonsil; 0.07076 0.06104 0.687150476 85.17928757 875.4025 5.75572 BIN2P1 . . . bridging integrator 2 pseudogene 1 . . . . . . . . . . . BIN2P2 . . . bridging integrator 2 pseudogene 2 . . . . . . . . . . . BIN3 5.99066271257055e-06 0.450060753833044 0.549933255504244 bridging integrator 3 FUNCTION: Involved in cytokinesis and septation where it has a role in the localization of F-actin.; . TISSUE SPECIFICITY: Ubiquitously expressed except in brain. {ECO:0000269|PubMed:11274158}.; medulla oblongata;ovary;colon;parathyroid;skin;uterus;prostate;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;skeletal muscle; 0.64748 0.10904 -0.446304853 24.33356924 75.29781 1.81543 BIN3-IT1 . . . BIN3 intronic transcript 1 . . . . . . . . . . . BIRC2 0.40445564763058 0.595171697814646 0.000372654554773988 baculoviral IAP repeat containing 2 FUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling, and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin- protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin- protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1, IKBKG/NEMO, IKBKE and MXD1/MAD1. Can also function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase- dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Can stimulate the transcriptional activity of E2F1. Plays a role in the modulation of the cell cycle. {ECO:0000269|PubMed:15665297, ECO:0000269|PubMed:18082613, ECO:0000269|PubMed:21145488, ECO:0000269|PubMed:21653699, ECO:0000269|PubMed:21931591, ECO:0000269|PubMed:23453969}.; . TISSUE SPECIFICITY: Present in many fetal and adult tissues. Mainly expressed in adult skeletal muscle, thymus, testis, ovary, and pancreas, low or absent in brain and peripheral blood leukocytes.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.13023 0.29692 -0.246069119 36.06982779 262.66183 3.47682 BIRC3 0.886667092506474 0.113281064924801 5.18425687250095e-05 baculoviral IAP repeat containing 3 FUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin- protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin- protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, IKBKE, TRAF1, and BCL10. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase- independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. {ECO:0000269|PubMed:21931591, ECO:0000269|PubMed:23453969}.; DISEASE: Note=A chromosomal aberration involving BIRC3 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(11;18)(q21;q21) with MALT1. This translocation is found in approximately 50% of cytogenetically abnormal low-grade MALT lymphoma.; TISSUE SPECIFICITY: Highly expressed in fetal lung, and kidney. In the adult, expression is mainly seen in lymphoid tissues, including spleen, thymus and peripheral blood lymphocytes.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;cerebral cortex;endometrium;oesophagus;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;visual apparatus;amnion;liver;spleen;head and neck;kidney;aorta;stomach;thymus; . 0.36052 0.28580 -0.534490515 20.70063694 76.6367 1.83741 BIRC5 0.215847836777704 0.745359830041678 0.0387923331806177 baculoviral IAP repeat containing 5 FUNCTION: Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform. {ECO:0000269|PubMed:10626797, ECO:0000269|PubMed:12773388, ECO:0000269|PubMed:16291752, ECO:0000269|PubMed:16322459, ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:20826784, ECO:0000269|PubMed:21536684, ECO:0000269|PubMed:9859993}.; . TISSUE SPECIFICITY: Expressed only in fetal kidney and liver, and to lesser extent, lung and brain. Abundantly expressed in adenocarcinoma (lung, pancreas, colon, breast, and prostate) and in high-grade lymphomas. Also expressed in various renal cell carcinoma cell lines. {ECO:0000269|PubMed:10626797, ECO:0000269|PubMed:14741722, ECO:0000269|PubMed:16329164}.; medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;tumor;atrioventricular node;trigeminal ganglion; 0.75829 0.62587 0.793752871 87.40268931 3.19676 0.11475 BIRC6 0.999999999999996 4.09006167782942e-15 2.21287640605679e-43 baculoviral IAP repeat containing 6 FUNCTION: Anti-apoptotic protein which can regulate cell death by controlling caspases and by acting as an E3 ubiquitin-protein ligase. Has an unusual ubiquitin conjugation system in that it could combine in a single polypeptide, ubiquitin conjugating (E2) with ubiquitin ligase (E3) activity, forming a chimeric E2/E3 ubiquitin ligase. Its tragets include CASP9 and DIABLO/SMAC. Acts as an inhibitor of CASP3, CASP7 and CASP9. Important regulator for the final stages of cytokinesis. Crucial for normal vesicle targeting to the site of abscission, but also for the integrity of the midbody and the midbody ring, and its striking ubiquitin modification. {ECO:0000269|PubMed:14765125, ECO:0000269|PubMed:15200957, ECO:0000269|PubMed:18329369}.; . TISSUE SPECIFICITY: Expressed in brain cancer cells.; . . 0.23071 0.09582 -4.329772159 0.106157113 518.6518 4.65379 BIRC6-AS1 . . . BIRC6 antisense RNA 1 . . . . . . . . . . . BIRC6-AS2 . . . BIRC6 antisense RNA 2 . . . . . . . . . . . BIRC7 0.00380290601773512 0.850108568926968 0.146088525055297 baculoviral IAP repeat containing 7 FUNCTION: Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity. As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival. May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions. Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine. Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2. This activation depends on TAB1 and NR2C2/TAK1. In vitro, inhibits CASP3 and proteolytic activation of pro-CASP9. Isoform 1 blocks staurosporine-induced apoptosis. Isoform 2 blocks etoposide-induced apoptosis. Isoform 2 protects against natural killer (NK) cell killing whereas isoform 1 augments killing. {ECO:0000269|PubMed:11084335, ECO:0000269|PubMed:16729033, ECO:0000269|PubMed:17294084, ECO:0000269|PubMed:18034418}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed at very low levels or not detectable in most adult tissues. Detected in adult heart, placenta, lung, lymph node, spleen and ovary, and in several carcinoma cell lines. Isoform 2 is detected in fetal kidney, heart and spleen, and at lower levels in adult brain, skeletal muscle and peripheral blood leukocytes.; unclassifiable (Anatomical System);lung;optic nerve;trophoblast;macula lutea;liver;fovea centralis;choroid;lens;skin;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07293 0.12989 0.643056625 84.05284265 597.06889 4.94473 BIRC8 6.54421950188215e-07 0.0782776893866306 0.921721656191419 baculoviral IAP repeat containing 8 FUNCTION: Protects against apoptosis mediated by BAX.; . TISSUE SPECIFICITY: Testis specific in normal tissues.; . . 0.24489 . 1.861235856 97.16914367 170.60625 2.84901 BISPR . . . BST2 interferon stimulated positive regulator (non-protein coding) . . . . . . . . . . . BIVM 6.43353311511258e-06 0.892328036484321 0.107665529982563 basic, immunoglobulin-like variable motif containing . . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in spleen, ovary, small intestine, colon, peripheral blood leukocytes and liver. Also expressed in testis, ovary, aorta, appendix, trachea, pituitary gland, bladder, uterus, spinal cord, salivary gland, stomach, mammary gland and bone marrow. Weakly or not expressed in fetal spleen, adult thymus and certain cancer cell lines. {ECO:0000269|PubMed:12036287}.; ovary;umbilical cord;foreskin;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;whole body;cochlea;cerebral cortex;larynx;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; . 0.20662 . -0.181750739 40.15687662 44.40443 1.27388 BIVM-ERCC5 . . . BIVM-ERCC5 readthrough . . . . . . . . . . . BLACAT1 . . . bladder cancer associated transcript 1 (non-protein coding) . . . . . . . . . . . BLACE . . . B-cell acute lymphoblastic leukemia expressed . . . . . . . . . 17.57081 0.61617 BLCAP 0.468529446393196 0.44353695345694 0.0879336001498643 bladder cancer associated protein FUNCTION: May regulate cell proliferation and coordinate apoptosis and cell cycle progression via a novel mechanism independent of both p53/TP53 and NF-kappa-B. {ECO:0000269|PubMed:17031575}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in cervical tissues. Down-regulated in bladder invasive carcinoma, renal cell carcinoma and in primary cervical carcinoma. {ECO:0000269|PubMed:10197429, ECO:0000269|PubMed:16675915, ECO:0000269|PubMed:19908260}.; . . 0.73808 0.15588 0.035072054 56.2514744 2.37453 0.08068 BLID 0.590165692367457 0.369400252098733 0.0404340555338108 BH3-like motif containing, cell death inducer FUNCTION: Functions as a proapoptotic molecule through the caspase-dependent mitochondrial pathway of cell death. {ECO:0000269|PubMed:15069058}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15069058}.; . . . . 0.237127192 68.98443029 7.76731 0.28636 BLK 2.86165843035065e-07 0.748886045987327 0.25111366784683 BLK proto-oncogene, Src family tyrosine kinase FUNCTION: Non-receptor tyrosine kinase involved in B-lymphocyte development, differentiation and signaling. B-cell receptor (BCR) signaling requires a tight regulation of several protein tyrosine kinases and phosphatases, and associated coreceptors. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. Signaling through BLK plays an important role in transmitting signals through surface immunoglobulins and supports the pro-B to pre-B transition, as well as the signaling for growth arrest and apoptosis downstream of B-cell receptor. Specifically binds and phosphorylates CD79A at 'Tyr-188'and 'Tyr-199', as well as CD79B at 'Tyr-196' and 'Tyr- 207'. Phosphorylates also the immunoglobulin G receptors FCGR2A, FCGR2B and FCGR2C. With FYN and LYN, plays an essential role in pre-B-cell receptor (pre-BCR)-mediated NF-kappa-B activation. Contributes also to BTK activation by indirectly stimulating BTK intramolecular autophosphorylation. In pancreatic islets, acts as a modulator of beta-cells function through the up-regulation of PDX1 and NKX6-1 and consequent stimulation of insulin secretion in response to glucose. {ECO:0000269|PubMed:19667185, ECO:0000269|PubMed:8756631}.; DISEASE: Maturity-onset diabetes of the young 11 (MODY11) [MIM:613375]: A form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease. {ECO:0000269|PubMed:19667185}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in lymphatic organs, pancreatic islets, Leydig cells, striate ducts of salivary glands and hair follicles. {ECO:0000269|PubMed:19667185}.; unclassifiable (Anatomical System);lymph node;salivary gland;colon;blood;pancreas;lung;nasopharynx;thyroid;testis;spleen;germinal center;kidney;brain;tonsil;stomach; tonsil; 0.18195 0.24392 -0.349025639 29.55885822 175.48813 2.88166 BLM 4.13859674040892e-11 0.981782817658362 0.0182171823002517 Bloom syndrome RecQ like helicase FUNCTION: Participates in DNA replication and repair. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction. Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA. Negatively regulates sister chromatid exchange (SCE). {ECO:0000269|PubMed:12019152, ECO:0000269|PubMed:21325134, ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:9388193}.; DISEASE: Bloom syndrome (BLM) [MIM:210900]: An autosomal recessive disorder. It is characterized by proportionate pre- and postnatal growth deficiency, sun-sensitive telangiectatic hypo- and hyperpigmented skin, predisposition to malignancy, and chromosomal instability. {ECO:0000269|PubMed:10862105, ECO:0000269|PubMed:7585968, ECO:0000269|PubMed:9285778}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;skin;uterus;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;pharynx;blood;skeletal muscle;lung;cornea;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.75964 0.61682 -0.14151689 42.36258552 934.18644 5.92615 BLMH 0.00956068971702177 0.988142630036378 0.00229668024660047 bleomycin hydrolase FUNCTION: The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B- aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity. {ECO:0000250}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion; 0.53505 0.38742 -0.093566408 46.7386176 1907.62332 8.04328 BLNK 0.990011101848006 0.00998887399145554 2.41605382377534e-08 B-cell linker FUNCTION: Functions as a central linker protein, downstream of the B-cell receptor (BCR), bridging the SYK kinase to a multitude of signaling pathways and regulating biological outcomes of B-cell function and development. Plays a role in the activation of ERK/EPHB2, MAP kinase p38 and JNK. Modulates AP1 activation. Important for the activation of NF-kappa-B and NFAT. Plays an important role in BCR-mediated PLCG1 and PLCG2 activation and Ca(2+) mobilization and is required for trafficking of the BCR to late endosomes. However, does not seem to be required for pre-BCR- mediated activation of MAP kinase and phosphatidyl-inositol 3 (PI3) kinase signaling. May be required for the RAC1-JNK pathway. Plays a critical role in orchestrating the pro-B cell to pre-B cell transition. May play an important role in BCR-induced B-cell apoptosis. {ECO:0000269|PubMed:10583958, ECO:0000269|PubMed:15270728, ECO:0000269|PubMed:16912232, ECO:0000269|PubMed:9697839}.; DISEASE: Agammaglobulinemia 4, autosomal recessive (AGM4) [MIM:613502]: A primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life. {ECO:0000269|PubMed:10583958}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in B-cell lineage and fibroblast cell lines (at protein level). Highest levels of expression in the spleen, with lower levels in the liver, kidney, pancreas, small intestines and colon.; ovary;salivary gland;intestine;colon;skin;prostate;endometrium;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;placenta;hypopharynx;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion; 0.25084 0.28432 -0.380166007 27.88393489 85.6321 1.97448 BLOC1S1 0.205801576114329 0.751781327662837 0.042417096222835 biogenesis of lysosomal organelles complex 1 subunit 1 FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. May negatively regulate aerobic respiration through mitochondrial protein lysine-acetylation. May counteract the action of the deacetylase SIRT3 by acetylating and regulating proteins of the mitochondrial respiratory chain including ATP5A1 and NDUFA9. {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:22309213}.; . . myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;iris;amniotic fluid;germinal center;bladder;brain;tonsil;heart;tongue;pineal body;pharynx;blood;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;kidney;stomach;aorta; superior cervical ganglion;subthalamic nucleus;pons;skeletal muscle;cingulate cortex; 0.16279 0.13588 -0.163345027 41.24793583 2.39611 0.08249 BLOC1S2 0.0560249302301392 0.865610391305826 0.0783646784640354 biogenesis of lysosomal organelles complex 1 subunit 2 FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. May play a role in cell proliferation. {ECO:0000269|PubMed:15102850, ECO:0000269|PubMed:15381421, ECO:0000269|PubMed:17182842}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are widely expressed. Expressed in various malignant tumor tissues (at protein level). {ECO:0000269|PubMed:15381421}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach;aorta; whole brain;amygdala;occipital lobe;subthalamic nucleus;hypothalamus;cingulate cortex;parietal lobe; 0.16263 0.14746 0.147123112 64.11299835 368.19948 4.05568 BLOC1S2P1 . . . biogenesis of lysosomal organelles complex-1, subunit 2 pseudogene 1 . . . . . . . . . . . BLOC1S3 0.0184297702580611 0.494019383703834 0.487550846038105 biogenesis of lysosomal organelles complex 1 subunit 3 FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. {ECO:0000269|PubMed:16385460, ECO:0000269|PubMed:17182842}.; DISEASE: Hermansky-Pudlak syndrome 8 (HPS8) [MIM:614077]: A form of Hermansky-Pudlak syndrome, a genetically heterogeneous autosomal recessive disorder characterized by oculocutaneous albinism, bleeding due to platelet storage pool deficiency, and lysosomal storage defects. This syndrome results from defects of diverse cytoplasmic organelles including melanosomes, platelet dense granules and lysosomes. Ceroid storage in the lungs is associated with pulmonary fibrosis, a common cause of premature death in individuals with HPS. {ECO:0000269|PubMed:16385460}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.05380 0.23912 . . 73.74289 1.79457 BLOC1S4 0.158972119673534 0.637661058939783 0.203366821386683 biogenesis of lysosomal organelles complex 1 subunit 4 FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. {ECO:0000269|PubMed:17182842}.; . . . . 0.07252 0.11881 . . 42.22969 1.22915 BLOC1S5 1.60196837053719e-05 0.424815685383463 0.575168294932832 biogenesis of lysosomal organelles complex 1 subunit 5 FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. {ECO:0000269|PubMed:17182842}.; . . . . . 0.25772 -0.205617011 38.57631517 38.63623 1.14481 BLOC1S5-TXNDC5 . . . BLOC1S5-TXNDC5 readthrough (NMD candidate) . . . . . . . . . . . BLOC1S6 9.82041840454567e-06 0.337405284014652 0.662584895566943 biogenesis of lysosomal organelles complex 1 subunit 6 FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. May play a role in intracellular vesicle trafficking, particularly in the vesicle-docking and fusion process. {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:21998198}.; DISEASE: Hermansky-Pudlak syndrome 9 (HPS9) [MIM:614171]: A form of Hermansky-Pudlak syndrome, a genetically heterogeneous autosomal recessive disorder characterized by oculocutaneous albinism, bleeding due to platelet storage pool deficiency, and lysosomal storage defects. This syndrome results from defects of diverse cytoplasmic organelles including melanosomes, platelet dense granules and lysosomes. Ceroid storage in the lungs is associated with pulmonary fibrosis, a common cause of premature death in individuals with HPS. {ECO:0000269|PubMed:21665000}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12019270, ECO:0000269|PubMed:12191018}.; . . 0.06159 0.23227 0.125076652 62.7388535 4.42472 0.16059 BLVRA 0.0832220297693768 0.906719372007726 0.0100585982228977 biliverdin reductase A FUNCTION: Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor.; . TISSUE SPECIFICITY: Liver.; umbilical cord;ovary;salivary gland;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pharynx;blood;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;kidney;mammary gland;stomach;thymus; superior cervical ganglion;trigeminal ganglion; 0.18096 0.12749 0.062575634 58.74026893 88.03961 2.00749 BLVRB 4.13261164472061e-05 0.39380793182604 0.606150742057512 biliverdin reductase B FUNCTION: Broad specificity oxidoreductase that catalyzes the NADPH-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles. Can also reduce the complexed Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. In the liver, converts biliverdin to bilirubin. {ECO:0000269|PubMed:10620517}.; . TISSUE SPECIFICITY: Predominantly expressed in liver and erythrocytes. At lower levels in heart, lung, adrenal gland and cerebrum. {ECO:0000269|PubMed:7929092}.; myocardium;smooth muscle;ovary;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; fetal liver;lung;liver;bone marrow; 0.16790 0.24232 0.306902668 72.38145789 157.01611 2.73749 BLZF1 7.04847210432784e-06 0.721682150104368 0.278310801423528 basic leucine zipper nuclear factor 1 FUNCTION: Required for normal Golgi structure and for protein transport from the endoplasmic reticulum (ER) through the Golgi apparatus to the cell surface.; . TISSUE SPECIFICITY: Ubiquitous. Also found in cell lines derived from several hematopoietic pathologies, such as T-cell leukemia, pro-B, pre-B, myeloma, and plasmacytoma cell lines, but not in Burkitt lymphoma cells. {ECO:0000269|PubMed:11056056, ECO:0000269|PubMed:11739401, ECO:0000269|PubMed:9129147}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;larynx;thyroid;pituitary gland;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;pharynx;blood;lens;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.27077 0.10337 1.284269037 93.76621845 1756.24457 7.73205 BLZF2P . . . basic leucine zipper nuclear factor 2 pseudogene . . . . . . . . . . . BMF 0.354021066182312 0.633166286255609 0.0128126475620793 Bcl2 modifying factor FUNCTION: May play a role in apoptosis. Isoform 1 seems to be the main initiator.; . TISSUE SPECIFICITY: Isoform 1 is mainly expressed in B-lymphoid cells. Isoform 2 and isoform 3 are mainly expressed in B-CLL and normal B-cells. {ECO:0000269|PubMed:14574334}.; lymphoreticular;smooth muscle;ovary;colon;skin;bone marrow;uterus;prostate;endometrium;larynx;synovium;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;pancreas;lung;placenta;visual apparatus;liver;head and neck;kidney; . 0.10921 0.10880 -0.229483771 36.86010852 9.98435 0.36607 BMI1 0.515144747396546 0.484068588606544 0.000786663996909644 BMI1 proto-oncogene, polycomb ring finger FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. In the PRC1 complex, it is required to stimulate the E3 ubiquitin-protein ligase activity of RNF2/RING2. {ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16714294, ECO:0000269|PubMed:16882984}.; . . . . 0.24247 0.38765 -0.207437529 38.2814343 . . BMI1P1 . . . BMI1 proto-oncogene, polycomb ring finger pseudogene 1 . . . . . . . . . . . BMIQ1 . . . body mass index QTL 1 . . . . . . . . . . . BMIQ2 . . . body mass index QTL 2 . . . . . . . . . . . BMIQ3 . . . body mass index QTL 3 . . . . . . . . . . . BMIQ5 . . . body mass index QTL 5 . . . . . . . . . . . BMIQ6 . . . body mass index QTL 6 . . . . . . . . . . . BMP1 0.868760693373601 0.131239280712637 2.59137624428976e-08 bone morphogenetic protein 1 FUNCTION: Cleaves the C-terminal propeptides of procollagen I, II and III. Induces cartilage and bone formation. May participate in dorsoventral patterning during early development by cleaving chordin (CHRD). Responsible for the proteolytic activation of lysyl oxidase LOX.; DISEASE: Osteogenesis imperfecta 13 (OI13) [MIM:614856]: An autosomal recessive form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI13 is characterized by normal teeth, faint blue sclerae, severe growth deficiency, borderline osteoporosis, severe bone deformity, and recurrent fractures affecting both upper and lower limbs. {ECO:0000269|PubMed:22052668, ECO:0000269|PubMed:22482805, ECO:0000269|PubMed:25402547}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;whole body;oesophagus;endometrium;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;liver;duodenum;hypopharynx;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;smooth muscle;heart;pons;atrioventricular node;subthalamic nucleus;placenta;liver;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.74981 0.47505 -1.964136947 1.840056617 714.38217 5.30827 BMP2 0.938086415869115 0.0616482963275902 0.000265287803294795 bone morphogenetic protein 2 FUNCTION: Induces cartilage and bone formation (PubMed:3201241). Stimulates the differentiation of myoblasts into osteoblasts via the EIF2AK3-EIF2A- ATF4 pathway. BMP2 activation of EIF2AK3 stimulates phosphorylation of EIF2A which leads to increased expression of ATF4 which plays a central role in osteoblast differentiation. In addition stimulates TMEM119, which upregulates the expression of ATF4 (PubMed:24362451). {ECO:0000269|PubMed:24362451, ECO:0000269|PubMed:3201241}.; . TISSUE SPECIFICITY: Particularly abundant in lung, spleen and colon and in low but significant levels in heart, brain, placenta, liver, skeletal muscle, kidney, pancreas, prostate, ovary and small intestine.; . . 0.99953 0.77481 -0.26993514 34.59542345 77.49644 1.85202 BMP2K 0.00191652482552986 0.99804383046795 3.96447065202295e-05 BMP2 inducible kinase FUNCTION: May be involved in osteoblast differentiation.; . . unclassifiable (Anatomical System);lung;ovary;heart;endometrium;adrenal gland;placenta;liver;testis;germinal center;brain;aorta; superior cervical ganglion; 0.78082 . 0.273728691 70.74781788 1787.12697 7.80244 BMP2KL . . . BMP2 inducible kinase-like, pseudogene . . . . . 0.15608 . . . . . BMP3 0.110241117911489 0.860529903687185 0.029228978401326 bone morphogenetic protein 3 FUNCTION: Negatively regulates bone density. Antagonizes the ability of certain osteogenic BMPs to induce osteoprogenitor differentitation and ossification. {ECO:0000269|PubMed:11138004, ECO:0000269|PubMed:15269709}.; . TISSUE SPECIFICITY: Expressed in adult and fetal cartilage. {ECO:0000269|PubMed:15475196}.; lung;nasopharynx;visual apparatus;skeletal muscle; superior cervical ganglion;globus pallidus;pons;atrioventricular node;skeletal muscle; 0.33056 0.20254 1.065596954 91.61358811 1369.3409 6.94288 BMP4 0.967466005226941 0.0324807095204252 5.32852526338349e-05 bone morphogenetic protein 4 FUNCTION: Induces cartilage and bone formation. Also act in mesoderm induction, tooth development, limb formation and fracture repair. Acts in concert with PTHLH/PTHRP to stimulate ductal outgrowth during embryonic mammary development and to inhibit hair follicle induction (By similarity). {ECO:0000250}.; DISEASE: Non-syndromic orofacial cleft 11 (OFC11) [MIM:600625]: A birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum. {ECO:0000269|PubMed:19249007}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the lung and lower levels seen in the kidney. Present also in normal and neoplastic prostate tissues, and prostate cancer cell lines.; ovary;salivary gland;intestine;colon;fovea centralis;skin;uterus;prostate;optic nerve;whole body;bone;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;pharynx;blood;bile duct;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.99178 0.93124 0.327131069 73.27199811 3182.9169 10.74895 BMP5 0.000107433236892632 0.946587642322938 0.0533049244401699 bone morphogenetic protein 5 FUNCTION: Induces cartilage and bone formation.; . TISSUE SPECIFICITY: Expressed in the lung and liver.; . . 0.92935 0.25991 0.352813824 74.49280491 159.17943 2.75713 BMP6 0.895081718104266 0.104875894079622 4.2387816112151e-05 bone morphogenetic protein 6 FUNCTION: Induces cartilage and bone formation.; . . ovary;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; superior cervical ganglion; 0.74302 0.37312 -0.336073593 30.55555556 2165.73211 8.56596 BMP6P1 . . . bone morphogenetic protein 6 pseudogene 1 . . . . . . . . . . . BMP7 0.98128676800379 0.018699627940667 1.36040555429486e-05 bone morphogenetic protein 7 FUNCTION: Induces cartilage and bone formation. May be the osteoinductive factor responsible for the phenomenon of epithelial osteogenesis. Plays a role in calcium regulation and bone homeostasis.; . TISSUE SPECIFICITY: Expressed in the kidney and bladder. Lower levels seen in the brain.; . . 0.99448 0.67288 -0.514264485 21.41424864 29.85236 0.95231 BMP7-AS1 . . . BMP7 antisense RNA 1 . . . . . . . . . . . BMP8A 0.456963119276428 0.537088737820325 0.00594814290324657 bone morphogenetic protein 8a FUNCTION: Induces cartilage and bone formation. May be the osteoinductive factor responsible for the phenomenon of epithelial osteogenesis. Plays a role in calcium regulation and bone homeostasis (By similarity). Signaling protein involved in regulation of thermogenesis and energy balance. Proposed to increase the peripheral response of brown adipose tissue (BAT) to adrenergic stimulation while acting centrally in the hypothalamus to increase sympathetic output to BAT. {ECO:0000250, ECO:0000269|PubMed:22579288}.; . . lung;whole body;frontal lobe;ovary;placenta;testis;mammary gland;skin; . 0.18341 0.13901 . . 3792.02101 12.07822 BMP8B 0.774529935806127 0.2238356567099 0.00163440748397293 bone morphogenetic protein 8b FUNCTION: Induces cartilage and bone formation. May be the osteoinductive factor responsible for the phenomenon of epithelial osteogenesis. Plays a role in calcium regulation and bone homeostasis (By similarity). {ECO:0000250}.; . . . . 0.41674 0.26179 . . 458.09062 4.44369 BMP10 0.722716219511508 0.274321046093909 0.00296273439458305 bone morphogenetic protein 10 FUNCTION: Required for maintaining the proliferative activity of embryonic cardiomyocytes by preventing premature activation of the negative cell cycle regulator CDKN1C/p57KIP and maintaining the required expression levels of cardiogenic factors such as MEF2C and NKX2-5. Acts as a ligand for ACVRL1/ALK1, BMPR1A/ALK3 and BMPR1B/ALK6, leading to activation of SMAD1, SMAD5 and SMAD8 transcription factors. Inhibits endothelial cell migration and growth. May reduce cell migration and cell matrix adhesion in breast cancer cell lines. {ECO:0000269|PubMed:16049014, ECO:0000269|PubMed:17068149, ECO:0000269|PubMed:20608934}.; . TISSUE SPECIFICITY: Detected in mammary epithelia (at protein level). {ECO:0000269|PubMed:20608934}.; stomach; superior cervical ganglion;atrioventricular node; 0.20491 0.22087 0.086440867 60.47416844 137.094 2.54696 BMP15 0.0535439236113694 0.863355284683544 0.0831007917050865 bone morphogenetic protein 15 FUNCTION: May be involved in follicular development. Oocyte- specific growth/differentiation factor that stimulates folliculogenesis and granulosa cell (GC) growth. {ECO:0000269|PubMed:18227435}.; DISEASE: Ovarian dysgenesis 2 (ODG2) [MIM:300510]: A disorder characterized by lack of spontaneous pubertal development, primary amenorrhea, uterine hypoplasia, and hypergonadotropic hypogonadism as a result of streak gonads. {ECO:0000269|PubMed:15136966}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Premature ovarian failure 4 (POF4) [MIM:300510]: An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol. {ECO:0000269|PubMed:16464940, ECO:0000269|PubMed:16508750, ECO:0000269|PubMed:16645022, ECO:0000269|PubMed:19263482, ECO:0000269|PubMed:19438907}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.41269 0.19135 0.595326758 82.66100495 1548.61203 7.29985 BMPER 0.00107085516215034 0.998476761257395 0.00045238358045474 BMP binding endothelial regulator FUNCTION: Inhibitor of bone morphogenetic protein (BMP) function, it may regulate BMP responsiveness of osteoblasts and chondrocytes. {ECO:0000269|PubMed:14766204}.; . TISSUE SPECIFICITY: Highly expressed in lung, and brain and also in primary chondrocytes. {ECO:0000269|PubMed:14766204}.; unclassifiable (Anatomical System);uterus;prostate;lung;cartilage;hypothalamus;bone;placenta;developmental;pituitary gland;testis;brain; . 0.16544 0.13130 0.069852974 59.10592121 351.02238 3.97175 BMPR1A 0.768624359128999 0.23136080247985 1.48383911509633e-05 bone morphogenetic protein receptor type 1A FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP2 and BMP4. Positively regulates chondrocyte differentiation through GDF5 interaction (By similarity). {ECO:0000250|UniProtKB:P36895}.; DISEASE: Polyposis syndrome, mixed hereditary 2 (HMPS2) [MIM:610069]: A disease is characterized by atypical juvenile polyps, colonic adenomas, and colorectal carcinomas. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A microdeletion of chromosome 10q23 involving BMPR1A and PTEN is a cause of chromosome 10q23 deletion syndrome, which shows overlapping features of the following three disorders: Bannayan-Zonana syndrome, Cowden disease and juvenile polyposis syndrome. {ECO:0000269|PubMed:11381269, ECO:0000269|PubMed:16525031}.; TISSUE SPECIFICITY: Highly expressed in skeletal muscle.; unclassifiable (Anatomical System);heart;hypothalamus;colon;parathyroid;blood;skin;skeletal muscle;breast;pancreas;whole body;larynx;thyroid;placenta;duodenum;testis;head and neck;cervix;germinal center;kidney;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.98203 0.53920 -0.404032746 26.53338051 3489.79211 11.37814 BMPR1APS1 . . . bone morphogenetic protein receptor type 1A pseudogene 1 . . . . . . . . . . . BMPR1APS2 . . . bone morphogenetic protein receptor type 1A pseudogene 2 . . . . . . . . . . . BMPR1B 0.991704371391891 0.00829525422259072 3.74385517917684e-07 bone morphogenetic protein receptor type 1B FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1 and GDF5. Positively regulates chondrocyte differentiation through GDF5 interaction (By similarity). {ECO:0000250|UniProtKB:P36898}.; DISEASE: Acromesomelic dysplasia, Demirhan type (AMDD) [MIM:609441]: A form of chondrodysplasia. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). {ECO:0000269|PubMed:15805157}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Brachydactyly A2 (BDA2) [MIM:112600]: A form of brachydactyly. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. In brachydactyly type A2 shortening of the middle phalanges is confined to the index finger and the second toe, all other digits being more or less normal. Because of a rhomboid or triangular shape of the affected middle phalanx, the end of the second finger usually deviates radially. {ECO:0000269|PubMed:14523231, ECO:0000269|PubMed:16957682}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;islets of Langerhans;choroid;fovea centralis;lens;retina;prostate;optic nerve;lung;visual apparatus;macula lutea;kidney;mammary gland;peripheral nerve; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.89549 0.33888 -0.756778259 13.44656759 95.45994 2.10914 BMPR1B-AS1 . . . BMPR1B antisense RNA 1 (head to head) . . . . . . . . . . . BMPR2 0.996668086457278 0.00333191320886496 3.33856685358656e-10 bone morphogenetic protein receptor type II FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Binds to BMP-7, BMP-2 and, less efficiently, BMP-4. Binding is weak but enhanced by the presence of type I receptors for BMPs.; DISEASE: Pulmonary venoocclusive disease 1, autosomal dominant (PVOD1) [MIM:265450]: A disease characterized by widespread fibrous obstruction and intimal thickening of septal veins and preseptal venules, a low diffusing capacity for carbon monoxide, occult alveolar hemorrhage, and nodular ground-glass opacities, septal lines and lymph node enlargement showed by high-resolution computed tomography of the chest. It is frequently associated with pulmonary capillary dilatation and proliferation, and is a rare and devastating cause of pulmonary hypertension. {ECO:0000269|PubMed:12446270, ECO:0000269|PubMed:16429395}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in heart and liver.; . . 0.85302 0.50140 -0.93133804 9.613116301 121.17099 2.39825 BMS1 0.995287036407563 0.00471296358598741 6.4496402333826e-12 BMS1, ribosome biogenesis factor FUNCTION: May act as a molecular switch during maturation of the 40S ribosomal subunit in the nucleolus. {ECO:0000250|UniProtKB:Q08965}.; DISEASE: Aplasia cutis congenita, non-syndromic (ACC) [MIM:107600]: A disorder characterized by congenital absence of a portion of skin in a localized or widespread area of the body. The lesions are most commonly localized on the scalp, however aplasia cutis congenita can affect any part of the body. {ECO:0000269|PubMed:23785305}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . . 0.099178678 60.75725407 2238.17745 8.72857 BMS1P1 . . . BMS1, ribosome biogenesis factor pseudogene 1 . . . . . . 0.03268 . . . . BMS1P2 . . . BMS1, ribosome biogenesis factor pseudogene 2 . . . . . . . . . . . BMS1P3 . . . BMS1, ribosome biogenesis factor pseudogene 3 . . . . . . . . . . . BMS1P4 . . . BMS1, ribosome biogenesis factor pseudogene 4 . . . . . . . . . . . BMS1P5 . . . BMS1, ribosome biogenesis factor pseudogene 5 . . . . . . 0.03268 . . . . BMS1P6 . . . BMS1, ribosome biogenesis factor pseudogene 6 . . . . . . . . . . . BMS1P7 . . . BMS1, ribosome biogenesis factor pseudogene 7 . . . . . . . . . . . BMS1P8 . . . BMS1, ribosome biogenesis factor pseudogene 8 . . . . . . . . . . . BMS1P9 . . . BMS1, ribosome biogenesis factor pseudogene 9 . . . . . . . . . . . BMS1P10 . . . BMS1, ribosome biogenesis factor pseudogene 10 . . . . . . . . . . . BMS1P11 . . . BMS1, ribosome biogenesis factor pseudogene 11 . . . . . . . . . . . BMS1P12 . . . BMS1, ribosome biogenesis factor pseudogene 12 . . . . . . . . . . . BMS1P13 . . . BMS1, ribosome biogenesis factor pseudogene 13 . . . . . . . . . . . BMS1P14 . . . BMS1, ribosome biogenesis factor pseudogene 14 . . . . . . . . . . . BMS1P15 . . . BMS1, ribosome biogenesis factor pseudogene 15 . . . . . . . . . . . BMS1P16 . . . BMS1, ribosome biogenesis factor pseudogene 16 . . . . . . . . . . . BMS1P17 . . . BMS1, ribosome biogenesis factor pseudogene 17 . . . . . . . . . . . BMS1P18 . . . BMS1, ribosome biogenesis factor pseudogene 18 . . . . . . . . . . . BMS1P19 . . . BMS1, ribosome biogenesis factor pseudogene 19 . . . . . . . . . . . BMS1P20 . . . BMS1, ribosome biogenesis factor pseudogene 20 . . . . . . . . . . . BMS1P21 . . . BMS1, ribosome biogenesis factor pseudogene 21 . . . . . . . . . . . BMS1P22 . . . BMS1, ribosome biogenesis factor pseudogene 22 . . . . . . . . . . . BMX 0.583862245065186 0.416045793771684 9.19611631297639e-05 BMX non-receptor tyrosine kinase FUNCTION: Non-receptor tyrosine kinase that plays central but diverse modulatory roles in various signaling processes involved in the regulation of actin reorganization, cell migration, cell proliferation and survival, cell adhesion, and apoptosis. Participates in signal transduction stimulated by growth factor receptors, cytokine receptors, G-protein coupled receptors, antigen receptors and integrins. Induces tyrosine phosphorylation of BCAR1 in response to integrin regulation. Activation of BMX by integrins is mediated by PTK2/FAK1, a key mediator of integrin signaling events leading to the regulation of actin cytoskeleton and cell motility. Plays a critical role in TNF-induced angiogenesis, and implicated in the signaling of TEK and FLT1 receptors, 2 important receptor families essential for angiogenesis. Required for the phosphorylation and activation of STAT3, a transcription factor involved in cell differentiation. Also involved in interleukin-6 (IL6) induced differentiation. Plays also a role in programming adaptive cytoprotection against extracellular stress in different cell systems, salivary epithelial cells, brain endothelial cells, and dermal fibroblasts. May be involved in regulation of endocytosis through its interaction with an endosomal protein RUFY1. May also play a role in the growth and differentiation of hematopoietic cells; as well as in signal transduction in endocardial and arterial endothelial cells. {ECO:0000269|PubMed:10688651, ECO:0000269|PubMed:11331870, ECO:0000269|PubMed:12370298, ECO:0000269|PubMed:12832404, ECO:0000269|PubMed:15788485, ECO:0000269|PubMed:18292575, ECO:0000269|PubMed:9520419}.; . TISSUE SPECIFICITY: Highly expressed in cells with great migratory potential, including endothelial cells and metastatic carcinoma cell lines.; unclassifiable (Anatomical System);lymph node;heart;colon;skeletal muscle;skin;uterus;pancreas;endometrium;thyroid;placenta;spinal ganglion;brain;aorta; dorsal root ganglion;superior cervical ganglion;skeletal muscle; 0.48018 0.16263 -0.115612493 45.12856806 34.18209 1.04679 BNC1 0.886168665378858 0.113778893026482 5.24415946601071e-05 basonuclin 1 FUNCTION: Likely to be a transcription factor specific for squamous epithelium and for the constituent keratinocytes at a stage either prior to or at the very beginning of terminal differentiation. May play a role in the differentiation of spermatozoa and oocytes.; . TISSUE SPECIFICITY: Expressed in epidermis, testis and foreskin, and to a lower extent in thymus, spleen, mammary glands, placenta, brain and heart. {ECO:0000269|PubMed:9687312}.; unclassifiable (Anatomical System);uterus;lung;placenta;testis;colon;cervix;skin; superior cervical ganglion;testis;skeletal muscle; 0.23181 0.14442 -1.280491183 5.16631281 177.37371 2.89461 BNC2 0.999465645265111 0.000534354269962316 4.64926852977321e-10 basonuclin 2 FUNCTION: Probable transcription factor specific for skin keratinocytes. May play a role in the differentiation of spermatozoa and oocytes.; . TISSUE SPECIFICITY: Highly expressed in testis, uterus and small intestine, and weakly expressed in colon and prostate. Also expressed in skin, primary keratinocytes, immortalized keratinocytes, and HeLa and HEK293 cells. Not detected in blood, thymus, spleen or Hep-G2 cells. {ECO:0000269|PubMed:14988505, ECO:0000269|PubMed:15081112}.; . . 0.60614 0.12171 0.631940882 83.58103326 398.58782 4.19343 BNIP1 0.00143692768334693 0.871526966600402 0.127036105716251 BCL2/adenovirus E1B 19kDa interacting protein 1 FUNCTION: SNARE that may be involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER. Required for maintenance of ER network. Implicated in the suppression of cell death. May be involved in mitochondrial autophagy. {ECO:0000269|PubMed:15272311, ECO:0000269|PubMed:21931693}.; . TISSUE SPECIFICITY: Isoform 1 is highly expressed in heart, brain, liver skeletal muscle and pancreas. Isoform 3 is moderately expressed in placenta, lung and kidney. Isoform 4 is highly expressed in testis and small intestine. {ECO:0000269|PubMed:10217402}.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;optic nerve;whole body;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;muscle;pharynx;blood;lens;lung;cornea;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;liver;globus pallidus;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.26308 0.14515 -0.115612493 45.12856806 26.59592 0.86174 BNIP2 1.6929996956937e-05 0.671754446487022 0.328228623516021 BCL2/adenovirus E1B 19kDa interacting protein 2 FUNCTION: Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins.; . . myocardium;smooth muscle;ovary;skin;retina;prostate;optic nerve;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;uterus;atrium;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;hippocampus;duodenum;head and neck;kidney;stomach; . 0.59599 0.12477 -0.336073593 30.55555556 3900.56272 12.33278 BNIP3 0.0487268463399347 0.857651095094764 0.0936220585653013 BCL2/adenovirus E1B 19kDa interacting protein 3 FUNCTION: Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates to mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. Plays an important role in the calprotectin (S100A8/A9)-induced cell death pathway. {ECO:0000269|PubMed:19935772, ECO:0000269|PubMed:22292033}.; . . . . 0.17083 0.31043 -0.007201372 53.19061099 19.77173 0.67517 BNIP3L 0.330817931436664 0.6539062067556 0.0152758618077365 BCL2/adenovirus E1B 19kDa interacting protein 3-like FUNCTION: Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates to mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. May function as a tumor suppressor. {ECO:0000269|PubMed:10381623, ECO:0000269|PubMed:21264228}.; . . colon;fovea centralis;vein;skin;retina;bone marrow;uterus;bone;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;mammary gland;stomach; amygdala;occipital lobe;fetal liver;bone marrow; 0.72934 0.09761 -0.207437529 38.2814343 13.46854 0.48932 BNIP3P1 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 1 . . . . . . . . . . . BNIP3P2 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 2 . . . . . . . . . . . BNIP3P3 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 3 . . . . . . . . . . . BNIP3P4 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 4 . . . . . . . . . . . BNIP3P5 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 5 . . . . . . . . . . . BNIP3P6 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 6 . . . . . . . . . . . BNIP3P7 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 7 . . . . . . . . . . . BNIP3P8 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 8 . . . . . . . . . . . BNIP3P9 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 9 . . . . . . . . . . . BNIP3P10 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 10 . . . . . . . . . . . BNIP3P11 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 11 . . . . . . . . . . . BNIP3P12 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 12 . . . . . . . . . . . BNIP3P13 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 13 . . . . . . . . . . . BNIP3P14 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 14 . . . . . . . . . . . BNIP3P15 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 15 . . . . . . . . . . . BNIP3P16 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 16 . . . . . . . . . . . BNIP3P17 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 17 . . . . . . . . . . . BNIP3P18 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 18 . . . . . . . . . . . BNIP3P19 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 19 . . . . . . . . . . . BNIP3P20 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 20 . . . . . . . . . . . BNIP3P21 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 21 . . . . . . . . . . . BNIP3P22 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 22 . . . . . . . . . . . BNIP3P23 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 23 . . . . . . . . . . . BNIP3P24 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 24 . . . . . . . . . . . BNIP3P25 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 25 . . . . . . . . . . . BNIP3P26 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 26 . . . . . . . . . . . BNIP3P27 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 27 . . . . . . . . . . . BNIP3P28 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 28 . . . . . . . . . . . BNIP3P29 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 29 . . . . . . . . . . . BNIP3P30 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 30 . . . . . . . . . . . BNIP3P31 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 31 . . . . . . . . . . . BNIP3P32 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 32 . . . . . . . . . . . BNIP3P33 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 33 . . . . . . . . . . . BNIP3P34 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 34 . . . . . . . . . . . BNIP3P35 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 35 . . . . . . . . . . . BNIP3P36 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 36 . . . . . . . . . . . BNIP3P37 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 37 . . . . . . . . . . . BNIP3P38 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 38 . . . . . . . . . . . BNIP3P39 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 39 . . . . . . . . . . . BNIP3P40 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 40 . . . . . . . . . . . BNIP3P41 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 41 . . . . . . . . . . . BNIP3P42 . . . BCL2/adenovirus E1B 19kDa interacting protein 3 pseudogene 42 . . . . . . . . . . . BNIPL 1.0279554795193e-09 0.164959207559917 0.835040791412127 BCL2/adenovirus E1B 19kD interacting protein like FUNCTION: May be a bridge molecule between BCL2 and ARHGAP1/CDC42 in promoting cell death. {ECO:0000269|PubMed:12901880}.; . TISSUE SPECIFICITY: Isoform 2 is expressed in placenta and lung. {ECO:0000269|PubMed:12681488}.; unclassifiable (Anatomical System);ovary;heart;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;retina;breast;prostate;lung;larynx;nasopharynx;thyroid;visual apparatus;liver;testis;head and neck;spleen;kidney;brain;bladder; ciliary ganglion;atrioventricular node; 0.12616 0.09032 0.531004228 80.87992451 1069.67582 6.27153 BOC 0.00472748578589258 0.995261744080771 1.0770133336139e-05 BOC cell adhesion associated, oncogene regulated FUNCTION: Component of a cell-surface receptor complex that mediates cell-cell interactions between muscle precursor cells. Promotes differentiation of myogenic cells.; . TISSUE SPECIFICITY: Detected in skeletal muscle, heart, thymus, kidney and small intestine. Detected at lower levels in brain, placenta, lung and colon mucosa. {ECO:0000269|PubMed:11782431}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;muscle;lens;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.11911 0.99316 -1.626115313 2.878037273 629.09229 5.05497 BOD1 0.031829615385069 0.815536469493735 0.152633915121196 biorientation of chromosomes in cell division 1 FUNCTION: Required for proper chromosome biorientation through the detection or correction of syntelic attachments in mitotic spindles. {ECO:0000269|PubMed:17938248}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum; testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.30911 0.10448 . . 16.89266 0.59473 BOD1L1 0.999528154229673 0.000471845770322145 4.76846817422079e-15 biorientation of chromosomes in cell division 1 like 1 FUNCTION: Component of the fork protection machinery required to protect stalled/damaged replication forks from uncontrolled DNA2- dependent resection. Acts by stabilizing RAD51 at stalled replication forks and protecting RAD51 nucleofilaments from the antirecombinogenic activities of FBXO18/FBH1 and BLM (PubMed:26166705). Does not regulate spindle orientation (PubMed:26166705). {ECO:0000269|PubMed:26166705}.; . . . . 0.44566 0.08925 -0.63057096 16.79051663 1099.59021 6.34651 BOD1L2 0.510146461496365 0.421226807618925 0.0686267308847108 biorientation of chromosomes in cell division 1 like 2 FUNCTION: May play a role in proper chromosome biorientation through the detection or correction of syntelic attachments in mitotic spindles. {ECO:0000250|UniProtKB:Q96IK1}.; . . . . . . . . 275.92113 3.55716 BOD1P1 . . . biorientation of chromosomes in cell division 1 pseudogene 1 . . . . . . . . . . . BOD1P2 . . . biorientation of chromosomes in cell division 1 pseudogene 2 . . . . . . . . . . . BOK 0.318891848354031 0.613089638656278 0.0680185129896909 BCL2-related ovarian killer FUNCTION: Induces apoptosis in a manner dependent on BAX and BAK. {ECO:0000269|PubMed:23429263}.; . TISSUE SPECIFICITY: Expressed in brain, liver, appendix and lymphoid tissues. {ECO:0000269|PubMed:9535847}.; ovary;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;thyroid;testis;amniotic fluid;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; liver;prefrontal cortex; 0.18540 0.28104 . . 106.03185 2.23324 BOK-AS1 . . . BOK antisense RNA 1 . . . . . . . . . . . BOLA1 0.634184000881994 0.336716256012686 0.0290997431053202 bolA family member 1 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18548201}.; . . 0.09733 0.10528 0.459411326 78.28497287 163.91566 2.79669 BOLA2 . . . bolA family member 2 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;iris;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;heart;tongue;hypothalamus;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; . . 0.10181 . . . . BOLA2B . . . bolA family member 2B . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;iris;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;trophoblast;heart;tongue;hypothalamus;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; . . 0.10181 . . . . BOLA2P1 . . . bolA family member 2 pseudogene 1 . . . . . . . . . . . BOLA2P2 . . . bolA family member 2 pseudogene 2 . . . . . . . . . . . BOLA2P3 . . . bolA family member 2 pseudogene 3 . . . . . . . . . . . BOLA3 0.418296316493259 0.546834259026651 0.0348694244800895 bolA family member 3 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18548201}.; ovary;salivary gland;developmental;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;testis;bladder;brain;unclassifiable (Anatomical System);heart;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;lung;trabecular meshwork;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; . 0.26354 0.11348 0.013025609 54.62962963 18.55403 0.64235 BOLA3-AS1 . . . BOLA3 antisense RNA 1 (head to head) . . . . . . . . . . . BOLA3P1 . . . bolA family member 3 pseudogene 1 . . . . . . . . . . . BOLA3P2 . . . bolA family member 3 pseudogene 2 . . . . . . . . . . . BOLA3P3 . . . bolA family member 3 pseudogene 3 . . . . . . . . . . . BOLA3P4 . . . bolA family member 3 pseudogene 4 . . . . . . . . . . . BOLL 0.00790218351286136 0.977562483989522 0.0145353324976165 boule homolog, RNA binding protein FUNCTION: Probable RNA-binding protein, which may be required during spermatogenesis. May act by binding to the 3'-UTR of mRNAs and regulating their translation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis specific. Not expressed in early embryos, primordial germ cells and spermatogonial cells. First expressed in the cytoplasm of spermatocytes and then persists through meiosis. {ECO:0000269|PubMed:11390979, ECO:0000269|PubMed:17114206}.; unclassifiable (Anatomical System);lung;testis; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.20999 0.09311 0.170987912 65.5579146 298.79356 3.68599 BOP1 0.526839488528947 0.411323621157336 0.0618368903137168 block of proliferation 1 FUNCTION: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. {ECO:0000255|HAMAP-Rule:MF_03027, ECO:0000269|PubMed:17353269}.; . . unclassifiable (Anatomical System);lymphoreticular;lymph node;ovary;hypothalamus;muscle;adrenal cortex;colon;skin;bone marrow;pancreas;lung;endometrium;visual apparatus;testis;cervix;kidney;brain;mammary gland;stomach; . 0.65365 0.13948 . . 5.59978 0.20925 BORA 0.000692705153335445 0.979593960695279 0.0197133341513855 bora, aurora kinase A activator FUNCTION: Required for the activation of AURKA at the onset of mitosis. {ECO:0000269|PubMed:16890155}.; . . . . 0.25011 0.12092 -0.025608647 51.91672564 103.55945 2.19847 BORCS5 . . . BLOC-1 related complex subunit 5 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11896457}.; . . 0.19209 0.11117 0.238945317 69.20853975 . . BORCS6 . . . BLOC-1 related complex subunit 6 . . . . . 0.38193 0.10905 . . . . BORCS7 . . . BLOC-1 related complex subunit 7 . . . . . 0.17524 . -0.163345027 41.24793583 . . BORCS7-ASMT . . . BORCS7-ASMT readthrough (NMD candidate) . . . . . . . . . . . BORCS8 . . . BLOC-1 related complex subunit 8 . . . . . . . 0.145304857 63.81221986 . . BORCS8-MEF2B . . . BORCS8-MEF2B readthrough FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle- specific genes. Activates transcription via this element. May be involved in muscle-specific and/or growth factor-related transcription.; . TISSUE SPECIFICITY: Expressed in skeletal and cardiac muscle and brain.; . . 0.16431 . . . . . BPESC1 . . . blepharophimosis, epicanthus inversus and ptosis, candidate 1 (non-protein coding) . . TISSUE SPECIFICITY: Seems to be expressed only in testis.; . . . . . . . . BPGM 0.126322243893593 0.780127397916303 0.0935503581901044 bisphosphoglycerate mutase FUNCTION: Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3- bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities.; DISEASE: Bisphosphoglycerate mutase deficiency (BPGMD) [MIM:222800]: A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis. {ECO:0000269|PubMed:1421379, ECO:0000269|PubMed:15054810}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in red blood cells. Expressed in non-erythroid cells of the placenta; present in the syncytiotrophoblast layer of the placental villi at the feto- maternal interface (at protein level). {ECO:0000269|PubMed:16246416, ECO:0000269|PubMed:3023066, ECO:0000269|PubMed:6313356}.; ovary;salivary gland;intestine;colon;parathyroid;vein;skin;uterus;prostate;whole body;frontal lobe;larynx;thyroid;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cerebellum cortex;tongue;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;fetal liver;placenta;globus pallidus;ciliary ganglion;bone marrow; 0.71913 0.18569 -0.339715008 30.06605331 31.42111 0.99092 BPHL 0.000194971395463508 0.717797928002433 0.282007100602103 biphenyl hydrolase-like (serine hydrolase) FUNCTION: Serine hydrolase that catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs such as valacyclovir and valganciclovir. Activates valacyclovir to acyclovir. May play a role in detoxification processes. It is a specific alpha-amino acid ester hydrolase that prefers small, hydrophobic, and aromatic side chains and does not have a stringent requirement for the leaving group other than preferring a primary alcohol. {ECO:0000269|PubMed:18256025}.; . TISSUE SPECIFICITY: Expressed at high levels in liver and kidney and lower levels in heart, intestine and skeletal muscle. {ECO:0000269|PubMed:7759552}.; . . 0.13974 0.10225 0.729426781 86.17008728 915.30761 5.88463 BPI 8.85642713755215e-09 0.482407774773101 0.517592216370472 bactericidal/permeability-increasing protein FUNCTION: The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa. {ECO:0000269|PubMed:1937776, ECO:0000269|PubMed:2722846}.; . TISSUE SPECIFICITY: Restricted to cells of the myeloid series.; unclassifiable (Anatomical System);ovary;bone;liver;testis;blood;kidney;brain;bone marrow; testis - interstitial;testis;trigeminal ganglion;bone marrow; 0.28269 0.12505 2.601812899 98.76739797 3462.38062 11.32359 BPIFA1 3.60154382988658e-05 0.593735068308639 0.406228916253062 BPI fold containing family A member 1 FUNCTION: Plays a role in the innate immune responses of the upper airways. Reduces the surface tension in secretions from airway epithelia and inhibits the formation of biofilm by pathogenic Gram-negative bacteria, such as P.aeruginosa and K.pneumoniae. Binds bacterial lipopolysaccharide (LPS). Negatively regulates proteolytic cleavage of SCNN1G, an event that is required for activation of the epithelial sodium channel (ENaC), and thereby contributes to airway surface liquid homeostasis and proper clearance of mucus. Plays a role in the airway inflammatory response after exposure to irritants. May attract macrophages and neutrophils. May be associated with tumor progression. {ECO:0000269|PubMed:11425234, ECO:0000269|PubMed:23132494, ECO:0000269|PubMed:23499554, ECO:0000269|PubMed:24043776, ECO:0000269|PubMed:24124190}.; . TISSUE SPECIFICITY: Lung, upper airways and nasopharyngeal regions, including trachea and nasal epithelium. Specifically expressed in the secretory ducts and submucosal glands of tracheobronchial tissues. Highest expression in the trachea and progressive decrease from proximal (bronchial) to distal (bronchiolar) airways. Also expressed in lung cancers and some other types of cancer. {ECO:0000269|PubMed:11018263, ECO:0000269|PubMed:11251963, ECO:0000269|PubMed:12409287, ECO:0000269|PubMed:12920053}.; unclassifiable (Anatomical System);lung;nasopharynx;thyroid;pituitary gland;head and neck; superior cervical ganglion;trachea;trigeminal ganglion; 0.09168 0.34103 -0.293801652 32.93819297 18.05735 0.62975 BPIFA2 0.00266486348314627 0.792288724652687 0.205046411864167 BPI fold containing family A member 2 FUNCTION: Has strong antibacterial activity against P. aeruginosa. {ECO:0000269|PubMed:24581853}.; . TISSUE SPECIFICITY: Detected in submandibular gland. Secreted into saliva. {ECO:0000269|PubMed:11971875, ECO:0000269|PubMed:24581853}.; unclassifiable (Anatomical System);breast;lung;adrenal gland;thyroid;adrenal cortex;parathyroid;pineal gland;skeletal muscle; superior cervical ganglion;salivary gland;ciliary ganglion;trigeminal ganglion; 0.03243 0.07013 0.751474114 86.64779429 913.99615 5.87689 BPIFA3 0.000409260412041777 0.851966685051909 0.147624054536049 BPI fold containing family A member 3 . . . . . 0.10821 . 0.995816767 90.62278839 451.2978 4.41598 BPIFA4P . . . BPI fold containing family A member 4, pseudogene FUNCTION: Major protein in sweat, has surfactant properties. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in breast cancer and salivary gland. {ECO:0000269|PubMed:12538848}.; . . . . . . . . BPIFB1 5.76895247746317e-07 0.868384481978954 0.131614941125798 BPI fold containing family B member 1 FUNCTION: May play a role in innate immunity in mouth, nose and lungs. Binds bacterial lipopolysaccharide (LPS) and modulates the cellular responses to LPS. {ECO:0000269|PubMed:21900486}.; . TISSUE SPECIFICITY: Detected in duodenum mucosal crypts of cholera patients, near Paneth cells (at protein level). Detected in trachea, nasal septal epithelium and lung. {ECO:0000269|PubMed:21900486}.; lung;nasopharynx;skeletal muscle; lung;trachea;thymus; 0.06268 0.09059 1.489991751 95.35857514 879.99138 5.77666 BPIFB2 7.68879584989142e-08 0.46925255038875 0.530747372723292 BPI fold containing family B member 2 . . TISSUE SPECIFICITY: Highly expressed in tonsils, especially in hypertrophic tonsils. Detected at very low levels in fetal liver. {ECO:0000269|PubMed:12837268}.; unclassifiable (Anatomical System);lung;trachea;tongue;larynx;nasopharynx;testis;head and neck;brain;skeletal muscle; superior cervical ganglion;trachea;ciliary ganglion;atrioventricular node; 0.15404 0.09530 -0.064242613 48.844067 817.49956 5.61674 BPIFB3 1.27011210022581e-05 0.952461122061479 0.0475261768175182 BPI fold containing family B member 3 FUNCTION: May have the capacity to recognize and bind specific classes of odorants. May act as a carrier molecule, transporting odorants across the mucus layer to access receptor sites. May serve as a primary defense mechanism by recognizing and removing potentially harmful odorants or pathogenic microorganisms from the mucosa or clearing excess odorant from mucus to enable new odorant stimuli to be received (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in nasal septal epithelium. {ECO:0000269|PubMed:11971875}.; . . 0.14497 0.08786 1.137205722 92.32719981 8881.73483 20.36052 BPIFB4 3.46594612665667e-17 0.00948205952182381 0.990517940478176 BPI fold containing family B member 4 FUNCTION: May have the capacity to recognize and bind specific classes of odorants. May act as a carrier molecule, transporting odorants across the mucus layer to access receptor sites. May serve as a primary defense mechanism by recognizing and removing potentially harmful odorants or pathogenic microorganisms from the mucosa or clearing excess odorant from mucus to enable new odorant stimuli to be received (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in nasal tissue. {ECO:0000269|PubMed:11971875}.; . . 0.12854 0.07741 0.942426495 89.89148384 12796.44151 24.22093 BPIFB5P . . . BPI fold containing family B member 5, pseudogene . . . . . . . . . . . BPIFB6 1.20126828012269e-11 0.0888226020221402 0.911177397965847 BPI fold containing family B member 6 . . TISSUE SPECIFICITY: Detected at very low levels in normal tonsils, and at higher levels in hypertrophic tonsils.; . . 0.13027 0.08873 1.067416815 91.66666667 1025.58398 6.15546 BPIFB9P . . . BPI fold containing family B member 9, pseudogene . . . . . . . . . . . BPIFC 3.12823000785522e-06 0.931823490533644 0.068173381236348 BPI fold containing family C . . TISSUE SPECIFICITY: Detected in the basal layer of the epidermis from inflammatory skin from psoriasis patients, but not in normal skin.; islets of Langerhans;skin; . 0.15001 0.09878 0.88921411 89.24274593 1608.4105 7.42321 BPNT1 0.00021897484271604 0.913000828599207 0.0867801965580766 3'(2'), 5'-bisphosphate nucleotidase 1 FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4- trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6. {ECO:0000269|PubMed:10224133}.; . TISSUE SPECIFICITY: Highly expressed in kidney, liver, pancreas and heart. Detected at lower levels in brain, placenta, lung and skeletal muscle. {ECO:0000269|PubMed:10224133}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;cartilage;ovary;islets of Langerhans;colon;bone marrow;breast;pancreas;lung;nasopharynx;bone;placenta;liver;testis;head and neck;kidney;germinal center;aorta;stomach; . 0.18723 0.09636 0.459411326 78.28497287 64.03435 1.63993 BPTF 0.999999999995241 4.75903490584663e-12 9.46556937257347e-32 bromodomain PHD finger transcription factor FUNCTION: Histone-binding component of NURF (nucleosome-remodeling factor), a complex which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin. Specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes. May also regulate transcription through direct binding to DNA or transcription factors.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in testis. Present in kidney, liver and brain. In the brain, highest levels are found in motor cortex (at protein level). {ECO:0000269|PubMed:10662542, ECO:0000269|PubMed:10727212, ECO:0000269|PubMed:7621746, ECO:0000269|PubMed:9225734}.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach;aorta; superior cervical ganglion;occipital lobe; 0.45585 0.13135 -2.550887261 0.855154518 471.82655 4.49652 BPY2 . . . basic charge, Y-linked, 2 . . TISSUE SPECIFICITY: Expressed exclusively in testis. Expressed in ejaculated spermatozoa of germ cell. Expressed in the nuclei of spermatogonia, spermatocytes, and round spermatids, except elongated spermatids (at protein level). {ECO:0000269|PubMed:12207887, ECO:0000269|PubMed:12724276, ECO:0000269|PubMed:14627543}.; . . . . . . . . BPY2B . . . basic charge, Y-linked, 2B . . TISSUE SPECIFICITY: Expressed exclusively in testis. Expressed in ejaculated spermatozoa of germ cell. Expressed in the nuclei of spermatogonia, spermatocytes, and round spermatids, except elongated spermatids (at protein level). {ECO:0000269|PubMed:12207887, ECO:0000269|PubMed:12724276, ECO:0000269|PubMed:14627543}.; . . . . . . . . BPY2C . . . basic charge, Y-linked, 2C . . TISSUE SPECIFICITY: Expressed exclusively in testis. Expressed in ejaculated spermatozoa of germ cell. Expressed in the nuclei of spermatogonia, spermatocytes, and round spermatids, except elongated spermatids (at protein level). {ECO:0000269|PubMed:12207887, ECO:0000269|PubMed:12724276, ECO:0000269|PubMed:14627543}.; . . . . . . . . BPY2DP . . . basic charge, Y-linked, 2D, pseudogene . . . . . . . . . . . BRAF 0.999978196041997 2.18039579639691e-05 3.88216441101404e-14 B-Raf proto-oncogene, serine/threonine kinase FUNCTION: Protein kinase involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May play a role in the postsynaptic responses of hippocampal neuron. Phosphorylates MAP2K1, and thereby contributes to the MAP kinase signal transduction pathway. {ECO:0000269|PubMed:21441910}.; DISEASE: Note=Defects in BRAF are found in a wide range of cancers. {ECO:0000269|PubMed:18974108}.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:12198537, ECO:0000269|PubMed:23263490, ECO:0000269|PubMed:24455489}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis. {ECO:0000269|PubMed:12460919}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Familial non-Hodgkin lymphoma (NHL) [MIM:605027]: Cancer that starts in cells of the lymph system, which is part of the body's immune system. NHLs can occur at any age and are often marked by enlarged lymph nodes, fever and weight loss. {ECO:0000269|PubMed:14612909}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Cardiofaciocutaneous syndrome 1 (CFC1) [MIM:115150]: A multiple congenital anomaly disorder characterized by a distinctive facial appearance, heart defects and mental retardation. Heart defects include pulmonic stenosis, atrial septal defects and hypertrophic cardiomyopathy. Some affected individuals present with ectodermal abnormalities such as sparse, friable hair, hyperkeratotic skin lesions and a generalized ichthyosis-like condition. Typical facial features are similar to Noonan syndrome. They include high forehead with bitemporal constriction, hypoplastic supraorbital ridges, downslanting palpebral fissures, a depressed nasal bridge, and posteriorly angulated ears with prominent helices. {ECO:0000269|PubMed:16439621, ECO:0000269|PubMed:16474404, ECO:0000269|PubMed:18042262, ECO:0000269|PubMed:19206169}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Noonan syndrome 7 (NS7) [MIM:613706]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. {ECO:0000269|PubMed:19206169}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: LEOPARD syndrome 3 (LPRD3) [MIM:613707]: A disorder characterized by lentigines, electrocardiographic conduction abnormalities, ocular hypertelorism, pulmonic stenosis, abnormalities of genitalia, retardation of growth, and sensorineural deafness. {ECO:0000269|PubMed:19206169}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving BRAF is found in pilocytic astrocytomas. A tandem duplication of 2 Mb at 7q34 leads to the expression of a KIAA1549-BRAF fusion protein with a constitutive kinase activity and inducing cell transformation. {ECO:0000269|PubMed:18974108}.; TISSUE SPECIFICITY: Brain and testis.; unclassifiable (Anatomical System);amygdala;islets of Langerhans;whole body;lung;frontal lobe;placenta;thyroid;liver;testis;head and neck;spleen;germinal center;brain;stomach; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.95401 . -0.60427181 17.74593064 63.2093 1.62731 BRAFP1 . . . BRAF pseudogene 1 . . . . . . . . . . . BRAP 0.0157033106581831 0.984071057710771 0.000225631631046005 BRCA1 associated protein FUNCTION: Negatively regulates MAP kinase activation by limiting the formation of Raf/MEK complexes probably by inactivation of the KSR1 scaffold protein. Also acts as a Ras responsive E3 ubiquitin ligase that, on activation of Ras, is modified by auto- polyubiquitination resulting in the release of inhibition of Raf/MEK complex formation. May also act as a cytoplasmic retention protein with a role in regulating nuclear transport. {ECO:0000269|PubMed:14724641, ECO:0000303|PubMed:10777491}.; . TISSUE SPECIFICITY: Expressed in breast epithelial cell lines. {ECO:0000269|PubMed:9497340}.; medulla oblongata;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;endometrium;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;spinal cord;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;spleen;kidney;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;white blood cells;trigeminal ganglion;pituitary;skeletal muscle; 0.54049 0.33876 -0.512444034 21.55579146 60.64855 1.58361 BRAT1 3.85834781380314e-09 0.541807215883696 0.458192780257956 BRCA1 associated ATM activator 1 FUNCTION: Involved in DNA damage response; activates kinases ATM, SMC1A and PRKDC by modulating their phosphorylation status following ionizing radiation (IR) stress (PubMed:16452482, PubMed:22977523). Plays a role in regulating mitochondrial function and cell proliferation (PubMed:25070371). Required for protein stability of MTOR and MTOR-related proteins, and cell cycle progress by growth factors (PubMed:25657994). {ECO:0000269|PubMed:16452482, ECO:0000269|PubMed:22977523, ECO:0000269|PubMed:25070371, ECO:0000269|PubMed:25657994}.; DISEASE: Rigidity and multifocal seizure syndrome, lethal neonatal (RMFSL) [MIM:614498]: A lethal, neonatal, neurologic disorder characterized by episodic jerking that is apparent in utero, lack of psychomotor development, axial and limb rigidity, frequent multifocal seizures, and dysautonomia. At birth, affected individuals have small heads, overlapping cranial sutures, small or absent fontanels, and depressed frontal bones. Infants show poorly responsive focal jerks of the tongue, face and arms in a nearly continuous sequence throughout life. {ECO:0000269|PubMed:22279524}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:16452482}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;stomach;cerebellum;thymus; superior cervical ganglion; 0.12411 . 0.769703589 86.90728946 1941.59065 8.11030 BRCA1 3.28742187416399e-20 0.106035252853558 0.893964747146442 breast cancer 1 FUNCTION: E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The E3 ubiquitin-protein ligase activity is required for its tumor suppressor function. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for normal cell cycle progression from G2 to mitosis. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8. Acts as a transcriptional activator (PubMed:20160719). {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:10724175, ECO:0000269|PubMed:11836499, ECO:0000269|PubMed:12887909, ECO:0000269|PubMed:12890688, ECO:0000269|PubMed:14976165, ECO:0000269|PubMed:14990569, ECO:0000269|PubMed:16326698, ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19369211, ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:20351172, ECO:0000269|PubMed:20364141}.; DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:10323242, ECO:0000269|PubMed:12442275, ECO:0000269|PubMed:12938098, ECO:0000269|PubMed:14722926, ECO:0000269|PubMed:18285836, ECO:0000269|PubMed:7545954, ECO:0000269|PubMed:7894491, ECO:0000269|PubMed:7894493, ECO:0000269|PubMed:7939630, ECO:0000269|PubMed:8554067, ECO:0000269|PubMed:8723683, ECO:0000269|PubMed:8776600, ECO:0000269|PubMed:9482581, ECO:0000269|PubMed:9609997, ECO:0000269|PubMed:9760198}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Mutations in BRCA1 are thought to be responsible for 45% of inherited breast cancer. Moreover, BRCA1 carriers have a 4-fold increased risk of colon cancer, whereas male carriers face a 3- fold increased risk of prostate cancer. Cells lacking BRCA1 show defects in DNA repair by homologous recombination.; DISEASE: Breast-ovarian cancer, familial, 1 (BROVCA1) [MIM:604370]: A condition associated with familial predisposition to cancer of the breast and ovaries. Characteristic features in affected families are an early age of onset of breast cancer (often before age 50), increased chance of bilateral cancers (cancer that develop in both breasts, or both ovaries, independently), frequent occurrence of breast cancer among men, increased incidence of tumors of other specific organs, such as the prostate. {ECO:0000269|PubMed:12938098, ECO:0000269|PubMed:14722926, ECO:0000269|PubMed:8968716}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Mutations in BRCA1 are thought to be responsible for more than 80% of inherited breast-ovarian cancer.; DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease. {ECO:0000269|PubMed:10196379, ECO:0000269|PubMed:10486320, ECO:0000269|PubMed:14746861}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Pancreatic cancer 4 (PNCA4) [MIM:614320]: A malignant neoplasm of the pancreas. Tumors can arise from both the exocrine and endocrine portions of the pancreas, but 95% of them develop from the exocrine portion, including the ductal epithelium, acinar cells, connective tissue, and lymphatic tissue. {ECO:0000269|PubMed:18762988}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 and isoform 3 are widely expressed. Isoform 3 is reduced or absent in several breast and ovarian cancer cell lines.; unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;colon;skin;skeletal muscle;breast;bile duct;prostate;lung;endometrium;bone;placenta;visual apparatus;liver;testis;cervix;spleen;germinal center;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis;appendix;tumor;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.99897 0.94795 0.464695413 78.59754659 3823.01219 12.15413 BRCA1P1 . . . BRCA1 pseudogene 1 . . . . . . . . . . . BRCA2 2.21312120661867e-15 0.999975297905801 2.47020941970335e-05 breast cancer 2 FUNCTION: Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and SHFM1/DSS1, and is required to prevent R-loop- associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180). {ECO:0000269|PubMed:15115758, ECO:0000269|PubMed:15199141, ECO:0000269|PubMed:15671039, ECO:0000269|PubMed:18317453, ECO:0000269|PubMed:20729832, ECO:0000269|PubMed:20729858, ECO:0000269|PubMed:20729859, ECO:0000269|PubMed:21084279, ECO:0000269|PubMed:24485656, ECO:0000269|PubMed:24896180}.; DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:10399947, ECO:0000269|PubMed:10978364, ECO:0000269|PubMed:11139248, ECO:0000269|PubMed:11241844, ECO:0000269|PubMed:11948477, ECO:0000269|PubMed:12145750, ECO:0000269|PubMed:12373604, ECO:0000269|PubMed:12442274, ECO:0000269|PubMed:12442275, ECO:0000269|PubMed:12938098, ECO:0000269|PubMed:14722926, ECO:0000269|PubMed:15026808, ECO:0000269|PubMed:15172753, ECO:0000269|PubMed:15365993, ECO:0000269|PubMed:8640237, ECO:0000269|PubMed:9150152, ECO:0000269|PubMed:9609997, ECO:0000269|PubMed:9654203, ECO:0000269|PubMed:9971877}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Pancreatic cancer 2 (PNCA2) [MIM:613347]: A malignant neoplasm of the pancreas. Tumors can arise from both the exocrine and endocrine portions of the pancreas, but 95% of them develop from the exocrine portion, including the ductal epithelium, acinar cells, connective tissue, and lymphatic tissue. {ECO:0000269|PubMed:9140390}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Breast-ovarian cancer, familial, 2 (BROVCA2) [MIM:612555]: A condition associated with familial predisposition to cancer of the breast and ovaries. Characteristic features in affected families are an early age of onset of breast cancer (often before age 50), increased chance of bilateral cancers (cancer that develop in both breasts, or both ovaries, independently), frequent occurrence of breast cancer among men, increased incidence of tumors of other specific organs, such as the prostate. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Fanconi anemia complementation group D1 (FANCD1) [MIM:605724]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:12065746, ECO:0000269|PubMed:14670928, ECO:0000269|PubMed:16825431}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Glioma 3 (GLM3) [MIM:613029]: Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes. {ECO:0000269|PubMed:15689453}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest levels of expression in breast and thymus, with slightly lower levels in lung, ovary and spleen.; . . 0.97144 0.70346 3.731883424 99.58716678 775.59808 5.51436 BRCA3 . . . breast cancer 3 . . . . . . . . . . . BRCC3 0.0339670741642349 0.927542468908574 0.0384904569271916 BRCA1/BRCA2-containing complex subunit 3 FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'- linked polyubiquitin chains (PubMed:19214193, PubMed:20656690, PubMed:24075985, PubMed:26344097). Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double- strand breaks (DSBs) (PubMed:20656690). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates (PubMed:20656690, PubMed:24075985, PubMed:26344097, PubMed:26195665). Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex (PubMed:19214193). The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1 (PubMed:26195665). Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (PubMed:24075985, PubMed:26344097). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985). {ECO:0000269|PubMed:14636569, ECO:0000269|PubMed:16707425, ECO:0000269|PubMed:17525341, ECO:0000269|PubMed:19202061, ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749, ECO:0000269|PubMed:20656690, ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:26344097}.; . TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Aberrantly expressed in the vast majority of breast tumors. {ECO:0000269|PubMed:16707425}.; unclassifiable (Anatomical System);lung;endometrium;colon;cervix;germinal center;brain; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.15581 0.19351 0.21326276 67.71644256 9.43605 0.34751 BRCC3P1 . . . BRCA1/BRCA2-containing complex subunit 3 pseudogene 1 . . . . . . . . . . . BRD1 0.994534773397455 0.00546522548467638 1.11786907851701e-09 bromodomain containing 1 FUNCTION: Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. {ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:21880731}.; . TISSUE SPECIFICITY: Highly expressed in testis.; ovary;colon;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;breast;lung;epididymis;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle;cerebellum; 0.56855 0.11513 -1.719728651 2.488794527 545.41716 4.74951 BRD2 0.999530880243209 0.000469119418252866 3.38538338591965e-10 bromodomain containing 2 FUNCTION: May play a role in spermatogenesis or folliculogenesis (By similarity). Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling. Regulates transcription of the CCND1 gene. Plays a role in nucleosome assembly. {ECO:0000250, ECO:0000269|PubMed:18406326}.; . . . . 0.41159 0.54184 -0.020150552 52.25288983 1065.99604 6.26213 BRD2-IT1 . . . BRD2 intronic transcript 1 . . . . . . . . . . . BRD3 0.766979379296961 0.232945828884611 7.47918184280725e-05 bromodomain containing 3 FUNCTION: Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling and interaction with transcription factors. Regulates transcription by promoting the binding of the transcription factor GATA1 to its targets (By similarity). Regulates transcription of the CCND1 gene. {ECO:0000250, ECO:0000269|PubMed:18406326}.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;ovary;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;lung;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;cerebellum; 0.48114 0.18088 -0.705410796 14.77942911 163.3189 2.79036 BRD4 0.999993446254695 6.55374529494431e-06 1.02649992733659e-14 bromodomain containing 4 FUNCTION: Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P- TEFb complex and recruiting it to promoters: BRD4 is required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P- TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II. Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II. According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo (PubMed:22509028). In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B. Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters. {ECO:0000269|PubMed:22509028}.; DISEASE: Note=A chromosomal aberration involving BRD4 is found in a rare, aggressive, and lethal carcinoma arising in midline organs of young people. Translocation t(15;19)(q14;p13) with NUT which produces a BRD4-NUT fusion protein. {ECO:0000269|PubMed:11733348, ECO:0000269|PubMed:12543779}.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12543779}.; ovary;salivary gland;foreskin;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;testis - seminiferous tubule;placenta;temporal lobe;prefrontal cortex;testis;cingulate cortex;skeletal muscle; 0.42814 0.18694 -1.480759435 3.686010852 185.92351 2.96128 BRD7 0.944865043331553 0.0551346213455819 3.35322865077642e-07 bromodomain containing 7 FUNCTION: Acts both as coactivator and as corepressor. May play a role in chromatin remodeling. Activator of the Wnt signaling pathway in a DVL1-dependent manner by negatively regulating the GSK3B phosphotransferase activity. Induces dephosphorylation of GSK3B at 'Tyr-216'. Down-regulates TRIM24-mediated activation of transcriptional activation by AR (By similarity). Transcriptional corepressor that down-regulates the expression of target genes. Binds to target promoters, leading to increased histone H3 acetylation at 'Lys-9' (H3K9ac). Binds to the ESR1 promoter. Recruits BRCA1 and POU2F1 to the ESR1 promoter. Coactivator for TP53-mediated activation of transcription of a set of target genes. Required for TP53-mediated cell-cycle arrest in response to oncogene activation. Promotes acetylation of TP53 at 'Lys-382', and thereby promotes efficient recruitment of TP53 to target promoters. Inhibits cell cycle progression from G1 to S phase. {ECO:0000250, ECO:0000269|PubMed:16265664, ECO:0000269|PubMed:16475162, ECO:0000269|PubMed:20215511, ECO:0000269|PubMed:20228809, ECO:0000269|PubMed:20660729}.; . . . . . 0.18022 0.354632714 74.58126917 274.30815 3.54710 BRD7P1 . . . bromodomain containing 7 pseudogene 1 . . . . . . . . . . . BRD7P2 . . . bromodomain containing 7 pseudogene 2 . . . . . . . . . . . BRD7P3 . . . bromodomain containing 7 pseudogene 3 . . . . . . . . . . . BRD7P4 . . . bromodomain containing 7 pseudogene 4 . . . . . . . . . . . BRD7P5 . . . bromodomain containing 7 pseudogene 5 . . . smooth muscle;ovary;salivary gland;intestine;colon;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; . . . . . . . BRD7P6 . . . bromodomain containing 7 pseudogene 6 . . . . . . . . . . . BRD8 0.000590819287003113 0.999408819477291 3.61235706442662e-07 bromodomain containing 8 FUNCTION: May act as a coactivator during transcriptional activation by hormone-activated nuclear receptors (NR). Isoform 2 stimulates transcriptional activation by AR/DHTR, ESR1/NR3A1, RXRA/NR2B1 and THRB/ERBA2. At least isoform 1 and isoform 2 are components of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1- like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. {ECO:0000269|PubMed:10517671, ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:24463511}.; . TISSUE SPECIFICITY: Expressed in adipose tissue, brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. {ECO:0000269|PubMed:8611617}.; myocardium;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex; 0.17308 0.11543 0.159856957 64.91507431 1921.62369 8.07167 BRD9 0.249187873857174 0.749502263913387 0.00130986222943831 bromodomain containing 9 FUNCTION: May play a role in chromatin remodeling and regulation of transcription.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;head and neck;kidney;mammary gland;stomach; thalamus;prefrontal cortex;testis;pons; 0.12337 0.10817 -0.797234383 12.48525596 290.83161 3.64776 BRD9P1 . . . bromodomain containing 9 pseudogene 1 . . . . . . . . . . . BRD9P2 . . . bromodomain containing 9 pseudogene 2 . . . . . . . . . . . BRDT 2.47163040334459e-06 0.999058891196653 0.000938637172943878 bromodomain testis associated FUNCTION: Testis-specific chromatin protein that specifically binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) and plays a key role in spermatogenesis. Required in late pachytene spermatocytes: plays a role in meiotic and post-meiotic cells by binding to acetylated histones at the promoter of specific meiotic and post-meiotic genes, facilitating their activation at the appropriate time. In the post-meiotic phase of spermatogenesis, binds to hyperacetylated histones and participates in their general removal from DNA. Also acts as a component of the splicing machinery in pachytene spermatocytes and round spermatids and participates in 3'-UTR truncation of specific mRNAs in post-meiotic spermatids. Required for chromocenter organization, a structure comprised of peri-centromeric heterochromatin. {ECO:0000269|PubMed:15647849, ECO:0000269|PubMed:22901802, ECO:0000269|PubMed:9367677}.; . TISSUE SPECIFICITY: Testis-specific. A 3-fold higher expression is seen in adult testis than in embryo testis. Expression seems to be correlated with histone H4 hyperacetylation during the haploid phase of spermatogenesis (spermiogenesis). No expression, or very low expression is seen in patients' testes with abnormal spermatogenesis. Expressed in cancers such as non-small cell lung cancer and squamous cell carcinomas of the head and neck as well as of esophagus, but not in melanoma or in cancers of the colon, breast, kidney and bladder. {ECO:0000269|PubMed:10704737, ECO:0000269|PubMed:15647849, ECO:0000269|PubMed:9367677}.; unclassifiable (Anatomical System);medulla oblongata;lung;adrenal gland;thyroid;adrenal cortex;testis;parathyroid;pineal gland; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.14403 0.30507 0.782621089 87.25524888 2880.26845 10.16474 BRDTP1 . . . bromodomain testis associated pseudogene 1 . . . . . . . . . . . BRE 0.279976282823241 0.71982051590611 0.000203201270649171 brain and reproductive organ-expressed (TNFRSF1A modulator) FUNCTION: Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX (PubMed:17525341, PubMed:19261746, PubMed:19261749, PubMed:19261748). In the BRCA1-A complex, it acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex, thereby being required for the complex integrity and modulating the E3 ubiquitin ligase activity of the BRCA1-BARD1 heterodimer (PubMed:21282113, PubMed:19261748). Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates (PubMed:19214193, PubMed:24075985, PubMed:25283148, PubMed:26195665). Within the BRISC complex, acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex, thereby being required for the complex integrity (PubMed:21282113). The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1 (PubMed:26195665). The BRISC complex plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (PubMed:24075985). Down- regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985). May play a role in homeostasis or cellular differentiation in cells of neural, epithelial and germline origins. May also act as a death receptor-associated anti-apoptotic protein, which inhibits the mitochondrial apoptotic pathway. May regulate TNF-alpha signaling through its interactions with TNFRSF1A; however these effects may be indirect (PubMed:15465831). {ECO:0000269|PubMed:14636569, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749, ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:26195665, ECO:0000305|PubMed:15465831}.; . TISSUE SPECIFICITY: Expressed in all cell lines examined. Highly expressed in placenta. {ECO:0000269|PubMed:11676476}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;bone;iris;pituitary gland;testis;ciliary body;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; amygdala;dorsal root ganglion;superior cervical ganglion;adrenal gland;adrenal cortex;prefrontal cortex;testis;atrioventricular node;kidney;parietal lobe; 0.15997 0.23605 0.350995466 74.37485256 18.0279 0.62950 BRE-AS1 . . . BRE antisense RNA 1 . . . . . . . . . . . BRF1 0.634632788081496 0.365355182140273 1.20297782318215e-05 BRF1, RNA polymerase III transcription initiation factor 90 kDa subunit FUNCTION: General activator of RNA polymerase which utilizes different TFIIIB complexes at structurally distinct promoters. The isoform 1 is involved in the transcription of tRNA, adenovirus VA1, 7SL and 5S RNA. Isoform 2 is required for transcription of the U6 promoter.; DISEASE: Cerebellofaciodental syndrome (CFDS) [MIM:616202]: An autosomal recessive disorder characterized by cerebellar hypoplasia, delayed development and intellectual disability, as well as facial dysmorphic features, short stature, microcephaly, and dental anomalies. {ECO:0000269|PubMed:25561519}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;lens;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle;skin; 0.31021 . -2.059575132 1.621844775 62.41909 1.61441 BRF2 1.88281642938786e-09 0.397249213088143 0.602750785029041 BRF2, RNA polymerase III transcription initiation factor 50 kDa subunit FUNCTION: General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites. {ECO:0000269|PubMed:11040218, ECO:0000269|PubMed:11121026, ECO:0000269|PubMed:11564744}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;pons;caudate nucleus;trigeminal ganglion;skeletal muscle;parietal lobe; 0.76186 0.10052 -0.488577883 22.64685067 96.72557 2.12578 BRI3 0.0152584135023695 0.691371396290662 0.293370190206968 brain protein I3 . . . unclassifiable (Anatomical System);heart;ovary;hypothalamus;colon;parathyroid;blood;skin;uterus;pancreas;prostate;lung;frontal lobe;bone;placenta;visual apparatus;testis;kidney;brain;stomach; . . 0.21177 . . 5.02295 0.18671 BRI3BP 0.125132504957692 0.780057944748467 0.0948095502938407 BRI3 binding protein FUNCTION: Involved in tumorigenesis and may function by stabilizing p53/TP53. {ECO:0000269|PubMed:17943721}.; . TISSUE SPECIFICITY: Most abundantly expressed in brain, liver and kidney. Overexpressed in leukemia and lymphoma cell lines, as well as in various carcinomas. {ECO:0000269|PubMed:11860200, ECO:0000269|PubMed:17943721}.; unclassifiable (Anatomical System);lung;ovary;urinary;hypopharynx;testis;colon;cervix;head and neck;kidney;brain;skin; cerebellum peduncles;atrioventricular node; 0.15682 0.11133 -0.361761279 28.6329323 23.69353 0.78365 BRI3BPP1 . . . BRI3 binding protein pseudogene 1 . . . . . . . . . . . BRI3P1 . . . brain protein I3 pseudogene 1 . . . . . . . . . . . BRI3P2 . . . brain protein I3 pseudogene 2 . . . . . . . . . . . BRI3P3 . . . brain protein I3 pseudogene 3 . . . . . . . . . . . BRICD5 1.62461586129841e-10 0.0160175831285609 0.983982416708978 BRICHOS domain containing 5 . . . . . 0.06199 . 0.933309256 89.82661005 252.75722 3.42130 BRINP1 0.995424257691719 0.00457565488570478 8.74225764749391e-08 BMP/retinoic acid inducible neural specific 1 FUNCTION: Inhibits cell proliferation by negative regulation of the G1/S transition. Mediates cell death which is not of the classical apoptotic type and regulates expression of components of the plasminogen pathway. {ECO:0000269|PubMed:11420708, ECO:0000269|PubMed:14712213, ECO:0000269|PubMed:16369496}.; . TISSUE SPECIFICITY: Highly expressed in brain. Weakly expressed in heart, lung, skeletal muscle, kidney, thymus, prostate, testis and small intestine. {ECO:0000269|PubMed:9545632}.; . . 0.80204 0.13588 -0.927704399 9.719273414 561.62921 4.81159 BRINP2 0.999086308312748 0.000913683195521584 8.49173054086906e-09 BMP/retinoic acid inducible neural specific 2 FUNCTION: Inhibits neuronal cell proliferation by negative regulation of the cell cycle transition. {ECO:0000250}.; . . . . 0.26036 . -1.151821487 6.269167256 1852.05387 7.93290 BRINP3 0.00375909281013884 0.99443787364512 0.00180303354474153 BMP/retinoic acid inducible neural specific 3 FUNCTION: Inhibits neuronal cell proliferation by negative regulation of the cell cycle transition. Promotes pituitary gonadotrope cell proliferation, migration and invasion, when overexpressed. May play a role in cell pituitary tumor development. {ECO:0000269|PubMed:17138656}.; . TISSUE SPECIFICITY: Strongly expressed in oral keratinocytes compared to the weak expression in tongue squamous cell carcinoma (SCC). Expressed in endothelial and aortic smooth muscle cells. Overexpressed in gonadotropinomas compared to normal pituitarie tissues. {ECO:0000269|PubMed:17138656, ECO:0000269|PubMed:18430236, ECO:0000269|PubMed:19787213}.; . . 0.93585 0.11558 -1.155457828 6.168907761 50.74004 1.40353 BRIP1 5.37815596396534e-13 0.932068250980266 0.0679317490191963 BRCA1 interacting protein C-terminal helicase 1 FUNCTION: DNA-dependent ATPase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Acts late in the Fanconi anemia pathway, after FANCD2 ubiquitination. Involved in the repair of DNA double-strand breaks by homologous recombination in a manner that depends on its association with BRCA1. {ECO:0000269|PubMed:11301010, ECO:0000269|PubMed:14983014, ECO:0000269|PubMed:16116421, ECO:0000269|PubMed:16153896}.; DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:11301010}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Fanconi anemia complementation group J (FANCJ) [MIM:609054]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:16116423, ECO:0000269|PubMed:16116424, ECO:0000269|PubMed:20639400}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in testis. {ECO:0000269|PubMed:11301010}.; unclassifiable (Anatomical System);breast;medulla oblongata;prostate;lung;testis;colon;blood;germinal center;skin;skeletal muscle; dorsal root ganglion; 0.20765 0.27124 -0.637452658 16.73743808 155.97826 2.72998 BRIX1 0.981126894231147 0.0188592139305118 1.38918383412199e-05 BRX1, biogenesis of ribosomes FUNCTION: Required for biogenesis of the 60S ribosomal subunit.; . . ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;alveolus;cervix;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion; 0.87611 0.16759 0.082802743 60.09082331 1483.24875 7.16830 BRIX1P1 . . . BRX1, biogenesis of ribosomes pseudogene 1 . . . . . . . . . . . BRK1 0.604508693799594 0.359042190505369 0.0364491156950376 BRICK1, SCAR/WAVE actin-nucleating complex subunit FUNCTION: Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex. {ECO:0000269|PubMed:18560548}.; . . ovary;substantia nigra;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;placenta;kidney;stomach;aorta;thymus;cerebellum; . . . 0.145304857 63.81221986 6.0076 0.22583 BRK1P2 . . . BRICK1, SCAR/WAVE actin-nucleating complex subunit pseudogene 2 . . . . . . . . . . . BRMS1 0.00107652477429526 0.950817287609244 0.0481061876164603 breast cancer metastasis suppressor 1 FUNCTION: Transcriptional repressor. Down-regulates transcription activation by NF-kappa-B by promoting the deacetylation of RELA at 'Lys-310'. Promotes HDAC1 binding to promoter regions. Down- regulates expression of anti-apoptotic genes that are controlled by NF-kappa-B. Promotes apoptosis in cells that have inadequate adherence to a substrate, a process called anoikis, and may thereby inhibit metastasis. May be a mediator of metastasis suppression in breast carcinoma. {ECO:0000269|PubMed:14581478, ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:20830743}.; . TISSUE SPECIFICITY: Expression levels are higher in term placentas than in early placentas. Low levels of expression observed in normal pregnancies and in molar pregnancies. {ECO:0000269|PubMed:12414911}.; lymphoreticular;ovary;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);islets of Langerhans;muscle;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;atrioventricular node;parietal lobe; 0.14288 0.13540 -0.137658575 43.57159707 1191.74841 6.54636 BRMS1L 0.368282761115449 0.631225260756638 0.000491978127912849 breast cancer metastasis-suppressor 1-like FUNCTION: Involved in the histone deacetylase (HDAC1)-dependent transcriptional repression activity. When overexpressed in lung cancer cell line that lacks p53/TP53 expression, inhibits cell growth. {ECO:0000269|PubMed:15451426}.; . . unclassifiable (Anatomical System);amygdala;heart;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;breast;optic nerve;whole body;lung;macula lutea;alveolus;testis;brain; . 0.27865 0.10763 -0.007201372 53.19061099 23.92102 0.78844 BROX 2.4755364239274e-05 0.980414278396455 0.0195609662393056 BRO1 domain and CAAX motif containing . . . uterus;bile duct;pancreas;lung;ovary;islets of Langerhans;placenta;testis;colon;brain;bladder;skeletal muscle; superior cervical ganglion;globus pallidus;ciliary ganglion;skeletal muscle; 0.21095 0.10574 -0.115612493 45.12856806 98.56438 2.14502 BRPF1 0.999626031304734 0.00037396868728763 7.97862821458177e-12 bromodomain and PHD finger containing 1 FUNCTION: Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Positively regulates the transcription of RUNX1 and RUNX2. {ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:18794358}.; . TISSUE SPECIFICITY: High levels in testis.; colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;bile duct;breast;lung;placenta;hippocampus;liver;duodenum;spleen;cervix;mammary gland;stomach;cerebellum; testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;testis;ciliary ganglion;trigeminal ganglion; 0.62190 0.12281 -2.25808393 1.267987733 57.40076 1.52580 BRPF3 0.993940981411932 0.00605901147950515 7.10856295957761e-09 bromodomain and PHD finger containing 3 FUNCTION: Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. {ECO:0000269|PubMed:16387653}.; . . lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;frontal lobe;cochlea;larynx;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;peripheral nerve;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.23528 0.10053 -1.059995566 7.537154989 446.92674 4.39883 BRS3 0.888203115182751 0.110605267022127 0.00119161779512261 bombesin like receptor 3 FUNCTION: Role in sperm cell division, maturation, or function. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.; . TISSUE SPECIFICITY: In germ cells in testis. Lung carcinoma cells.; . . 0.36800 0.08777 -0.361761279 28.6329323 11.9225 0.43253 BRSK1 0.993996393197224 0.00600359985208511 6.95069134933509e-09 BR serine/threonine kinase 1 FUNCTION: Serine/threonine-protein kinase that plays a key role in polarization of neurons and centrosome duplication. Phosphorylates CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in post-mitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. In neurons, localizes to synaptic vesicles and plays a role in neurotransmitter release, possibly by phosphorylating RIMS1. Also acts as a positive regulator of centrosome duplication by mediating phosphorylation of gamma- tubulin (TUBG1 and TUBG2) at 'Ser-131', leading to translocation of gamma-tubulin and its associated proteins to the centrosome. Involved in the UV-induced DNA damage checkpoint response, probably by inhibiting CDK1 activity through phosphorylation and activation of WEE1, and inhibition of CDC25B and CDC25C. {ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15150265, ECO:0000269|PubMed:20026642, ECO:0000269|PubMed:21985311}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in brain and testis. Protein levels remain constant throughout the cell cycle. {ECO:0000269|PubMed:15150265}.; unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;fovea centralis;choroid;lens;retina;optic nerve;lung;frontal lobe;endometrium;bone;macula lutea;visual apparatus;brain;cerebellum; whole brain;amygdala;subthalamic nucleus; 0.38503 0.11286 -0.80269335 12.23755603 324.11953 3.82625 BRSK2 0.779570081093511 0.220416997550985 1.2921355503886e-05 BR serine/threonine kinase 2 FUNCTION: Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Plays a role in the regulation of the mitotic cell cycle progress and the onset of mitosis. Plays a role in the regulation of insulin secretion in response to elevated glucose levels, probably via phosphorylation of CDK16 and PAK1. While BRSK2 phosphorylated at Thr-174 can inhibit insulin secretion (PubMed:22798068), BRSK2 phosphorylated at Thr-260 can promote insulin secretion (PubMed:22669945). Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmatic reticulum (ER) stress. {ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:20026642, ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:22798068, ECO:0000269|PubMed:23029325}.; . TISSUE SPECIFICITY: Detected in pancreas islets (at protein level). {ECO:0000269|PubMed:22798068}.; unclassifiable (Anatomical System);medulla oblongata;optic nerve;ovary;epididymis;macula lutea;visual apparatus;liver;fovea centralis;choroid;lens;brain;retina; whole brain;amygdala;cerebellum peduncles;prefrontal cortex;parietal lobe;cerebellum; 0.16676 0.10676 -1.506435464 3.544468035 64.45039 1.64641 BRWD1 0.999999462325348 5.37674651724079e-07 6.52902891382071e-23 bromodomain and WD repeat domain containing 1 FUNCTION: May be a transcriptional activator. May be involved in chromatin remodeling (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. {ECO:0000250, ECO:0000269|PubMed:21834987}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12359327}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;testis;germinal center;brain;amygdala;unclassifiable (Anatomical System);small intestine;heart;cartilage;tongue;islets of Langerhans;spinal cord;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve;thymus; superior cervical ganglion;uterus corpus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.64569 0.10719 -0.821412236 11.77164426 5050.46205 14.54368 BRWD1-AS1 . . . BRWD1 antisense RNA 1 . . . . . . . . . . . BRWD1-AS2 . . . BRWD1 antisense RNA 2 . . . . . . . . . . . BRWD1-IT1 . . . BRWD1 intronic transcript 1 . . . . . . . . . . . BRWD1P1 . . . bromodomain and WD repeat domain containing 1 pseudogene 1 . . . . . . . . . . . BRWD1P2 . . . bromodomain and WD repeat domain containing 1 pseudogene 2 . . . . . . . . . . . BRWD1P3 . . . bromodomain and WD repeat domain containing 1 pseudogene 3 . . . . . . . . . . . BRWD3 0.999999995988904 4.01109623126731e-09 7.55777022524614e-22 bromodomain and WD repeat domain containing 3 FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. {ECO:0000269|PubMed:21834987}.; DISEASE: Note=A chromosomal aberration involving BRWD3 can be found in patients with B-cell chronic lymphocytic leukemia (B- CLL). Translocation t(X;11)(q21;q23) with ARHGAP20 does not result in fusion transcripts but disrupts both genes.; DISEASE: Mental retardation, X-linked 93 (MRX93) [MIM:300659]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non- syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. MRX93 is associated with macrocephaly. {ECO:0000269|PubMed:17668385}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in most adult tissues. Down-regulated in a majority of the B-CLL cases examined. {ECO:0000269|PubMed:15543602}.; . . 0.72124 0.09906 -0.488577883 22.64685067 56.92691 1.51886 BSCL2 0.00852541052442389 0.988762954307341 0.00271163516823519 Berardinelli-Seip congenital lipodystrophy 2 (seipin) FUNCTION: Is a regulator of lipid catabolism essential for adipocyte differentiation. May also be involved in the central regulation of energy homeostasis (By similarity). Necessary for correct lipid storage and lipid droplets maintenance; may play a tissue-autonomous role in controlling lipid storage in adipocytes and in preventing ectopic lipid droplet formation in non-adipose tissues. {ECO:0000250, ECO:0000269|PubMed:19278620, ECO:0000269|PubMed:21533227}.; DISEASE: Spastic paraplegia 17, autosomal dominant (SPG17) [MIM:270685]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG17 is characterized by prominent amyotrophy of the hand muscles, the presence of mild to severe pyramidal tract signs and spastic paraplegia. SPG17 is a motor neuron disease overlapping with distal spinal muscular atrophy type 5. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Neuronopathy, distal hereditary motor, 5A (HMN5A) [MIM:600794]: A disorder characterized by distal muscular atrophy mainly affecting the upper extremities, in contrast to other distal motor neuronopathies. These constitute a heterogeneous group of neuromuscular diseases caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. {ECO:0000269|PubMed:14981520}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Encephalopathy, progressive, with or without lipodystrophy (PELD) [MIM:615924]: A neurodegenerative disease characterized by developmental regression of motor and cognitive skills in the first years of life, often leading to death in the first decade, hyperactive behavior, seizures, tremor and ataxic gait. Patients may show a mild or typical lipodystrophic appearance. {ECO:0000269|PubMed:23564749}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in motor neurons in the spinal cord and cortical neurons in the frontal lobe (at protein level). Highly expressed in brain, testis and adipose tissue. {ECO:0000269|PubMed:11479539, ECO:0000269|PubMed:18458148, ECO:0000269|PubMed:18585921}.; ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;larynx;synovium;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;placenta;hippocampus;duodenum;head and neck;kidney;aorta;stomach;thymus;cerebellum; amygdala;whole brain;thalamus;medulla oblongata;occipital lobe;testis - interstitial;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;testis - seminiferous tubule;fetal brain;prefrontal cortex;globus pallidus;testis;cingulate cortex;pituitary;parietal lobe;cerebellum; 0.07750 . -0.179930907 40.35739561 114.98915 2.33354 BSDC1 0.482345221176286 0.516641558390496 0.00101322043321791 BSD domain containing 1 . . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;bile duct;lung;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; superior cervical ganglion;testis - seminiferous tubule;placenta;prefrontal cortex;testis;cingulate cortex;cerebellum; 0.63323 0.09047 -0.47017169 23.25430526 20.76497 0.70406 BSG 0.0573043629421646 0.924667538017764 0.0180280990400717 basigin (Ok blood group) FUNCTION: Plays an important role in targeting the monocarboxylate transporters SLC16A1, SLC16A3 and SLC16A8 to the plasma membrane. Plays pivotal roles in spermatogenesis, embryo implantation, neural network formation and tumor progression. Stimulates adjacent fibroblasts to produce matrix metalloproteinases (MMPS). Seems to be a receptor for oligomannosidic glycans. In vitro, promotes outgrowth of astrocytic processes. {ECO:0000269|PubMed:17127621}.; . TISSUE SPECIFICITY: Present only in vascular endothelium in non- neoplastic regions of the brain, whereas it is present in tumor cells but not in proliferating blood vessels in malignant gliomas.; myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;cochlea;thyroid;iris;germinal center;ciliary body;bladder;brain;gall bladder;tonsil;amygdala;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;alveolus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus; . 0.15647 0.35769 -1.043396569 7.71408351 64.76165 1.65193 BSN 0.999999992077176 7.92282401269756e-09 1.34562019606116e-24 bassoon presynaptic cytomatrix protein FUNCTION: Is thought to be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. Seems to act through binding to ERC2/CAST1. Essential in regulated neurotransmitter release from a subset of brain glutamatergic synapses. Involved in the formation of the retinal photoreceptor ribbon synapses (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Exclusively expressed in brain. {ECO:0000269|PubMed:9806829}.; colon;choroid;fovea centralis;skin;bone marrow;retina;uterus;optic nerve;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);amygdala;cerebellum cortex;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;visual apparatus;macula lutea;kidney;stomach;cerebellum; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.32316 0.22292 -3.964560865 0.194621373 1440.10971 7.07899 BSN-AS1 . . . BSN antisense RNA 1 . . . . . . . . . . . BSN-AS2 . . . BSN antisense RNA 2 (head to head) . . . . . . . . . . . BSND 4.41379060688424e-07 0.117473728895923 0.882525829725016 barttin CLCNK type accessory beta subunit FUNCTION: Functions as a beta-subunit for CLCNKA and CLCNKB chloride channels. In the kidney CLCNK/BSND heteromers mediate chloride reabsorption by facilitating its basolateral efflux. In the stria, CLCNK/BSND channels drive potassium secretion by recycling chloride for the basolateral SLC12A2 cotransporter. {ECO:0000269|PubMed:11734858, ECO:0000269|PubMed:12111250}.; DISEASE: Bartter syndrome 4A (BS4A) [MIM:602522]: An autosomal recessive disorder characterized by impaired salt reabsorption in the thick ascending loop of Henle with pronounced salt wasting, hypokalemic metabolic alkalosis, and varying degrees of hypercalciuria. Bartter syndrome type 4 is associated with sensorineural deafness. {ECO:0000269|PubMed:11687798, ECO:0000269|PubMed:12574213}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed primarily in kidney. Expressed in specific nephron segments and in the stria vascularis of the inner ear. {ECO:0000269|PubMed:11687798}.; . . 0.07478 0.36521 -0.358119787 29.16371786 38.75161 1.14741 BSNDP1 . . . barttin CLCNK type accessory beta subunit pseudogene 1 . . . . . . . . . . . BSNDP2 . . . barttin CLCNK type accessory beta subunit pseudogene 2 . . . . . . . . . . . BSNDP3 . . . barttin CLCNK type accessory beta subunit pseudogene 3 . . . . . . . . . . . BSNDP4 . . . barttin CLCNK type accessory beta subunit pseudogene 4 . . . . . . . . . . . BSPH1 . . . binder of sperm protein homolog 1 FUNCTION: Binds sperm in vitro and promotes sperm capacitation. Specifically promotes capacitation induced by high density lipoproteins (HDLs). Also binds heparin, phospholipid liposomes, and weakly to gelatin. Does not bind chondroitin sulfate B. {ECO:0000250|UniProtKB:Q3UW26}.; . TISSUE SPECIFICITY: Expressed only in the epididymis. {ECO:0000269|PubMed:17085770}.; . . . 0.09904 0.501689326 79.7888653 151.58548 2.69226 BSPRY 9.78555675234067e-05 0.569001074693782 0.430901069738694 B-box and SPRY domain containing FUNCTION: May regulate epithelial calcium transport by inhibiting TRPV5 activity. {ECO:0000250}.; . . . . 0.54535 0.10489 0.220536484 68.38287332 916.02868 5.88635 BST1 2.81284355269231e-08 0.291985672674602 0.708014299196963 bone marrow stromal cell antigen 1 FUNCTION: Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger that elicits calcium release from intracellular stores. May be involved in pre-B-cell growth. {ECO:0000269|PubMed:11866528}.; . TISSUE SPECIFICITY: Widely expressed.; unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;skin;skeletal muscle;bone marrow;uterus;prostate;optic nerve;lung;frontal lobe;endometrium;mesenchyma;larynx;placenta;visual apparatus;hippocampus;amnion;head and neck;kidney;mammary gland;gall bladder; whole blood;bone marrow; 0.12690 0.19823 0.861712133 88.6883699 1705.28413 7.61637 BST2 0.000608698681329368 0.484293075558421 0.51509822576025 bone marrow stromal cell antigen 2 FUNCTION: IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted. Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), human immunodeficiency virus type 2 (HIV-2), simian immunodeficiency viruses (SIVs), equine infectious anemia virus (EIAV), feline immunodeficiency virus (FIV), prototype foamy virus (PFV), Mason- Pfizer monkey virus (MPMV), human T-cell leukemia virus type 1 (HTLV-1), Rous sarcoma virus (RSV) and murine leukemia virus (MLV), flavivirideae: hepatitis C virus (HCV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), arenaviridae: lassa virus (LASV) and machupo virus (MACV), herpesviridae: kaposis sarcoma- associated herpesvirus (KSHV), rhabdoviridae: vesicular stomatitis virus (VSV), orthomyxoviridae: influenza A virus, and paramyxoviridae: nipah virus. Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration. Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection. Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells. Isoform 1 and isoform 2 are both effective viral restriction factors but have differing antiviral and signaling activities. Isoform 2 is resistant to HIV-1 Vpu-mediated degradation and restricts HIV-1 viral budding in the presence of Vpu. Isoform 1 acts as an activator of NF-kappa-B and this activity is inhibited by isoform 2. {ECO:0000269|PubMed:18200009, ECO:0000269|PubMed:18342597, ECO:0000269|PubMed:19036818, ECO:0000269|PubMed:19179289, ECO:0000269|PubMed:19564354, ECO:0000269|PubMed:19879838, ECO:0000269|PubMed:20399176, ECO:0000269|PubMed:20419159, ECO:0000269|PubMed:20686043, ECO:0000269|PubMed:20940320, ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:21529378, ECO:0000269|PubMed:21621240, ECO:0000269|PubMed:22065321, ECO:0000269|PubMed:22520941, ECO:0000269|PubMed:23028328}.; . TISSUE SPECIFICITY: Predominantly expressed in liver, lung, heart and placenta. Lower levels in pancreas, kidney, skeletal muscle and brain. Overexpressed in multiple myeloma cells. Highly expressed during B-cell development, from pro-B precursors to plasma cells. Highly expressed on T-cells, monocytes, NK cells and dendritic cells (at protein level). {ECO:0000269|PubMed:10329429, ECO:0000269|PubMed:16157322}.; lymphoreticular;ovary;sympathetic chain;skin;retina;prostate;optic nerve;endometrium;bladder;brain;tonsil;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;oesophagus;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; ovary;adrenal gland;placenta;adrenal cortex;liver;white blood cells; 0.35967 0.09418 -0.119252484 44.53880632 3.60338 0.13120 BSX 0.136321314394079 0.77988461038662 0.0837940752193009 brain specific homeobox FUNCTION: DNA binding protein that function as transcriptional activator. Is essentiel for normal postnatal growth and nursing. Is an essential factor for neuronal neuropeptide Y and agouti- related peptide function and locomotory behavior in the control of energy balance (By similarity). {ECO:0000250}.; . . . . 0.19034 . 0.170987912 65.5579146 159.03212 2.75504 BTAF1 0.999999999938298 6.17019687482319e-11 1.18715136416501e-27 B-TFIID TATA-box binding protein associated factor 1 FUNCTION: Regulates transcription in association with TATA binding protein (TBP). Removes TBP from the TATA box in an ATP-dependent manner.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;urinary;blood;lens;breast;pancreas;lung;placenta;macula lutea;liver;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - seminiferous tubule;white blood cells; 0.95381 0.14507 -1.723336008 2.465204058 106.61318 2.24068 BTBD1 0.0149464237355017 0.979208616859636 0.00584495940486258 BTB domain containing 1 FUNCTION: Probable substrate-specific adapter of an E3 ubiquitin- protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000269|PubMed:14528312}.; . TISSUE SPECIFICITY: Ubiquitous; higher levels in heart and skeletal muscle. {ECO:0000269|PubMed:11179693}.; myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;blood;lens;skeletal muscle;breast;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta;thymus;cerebellum; amygdala;occipital lobe;medulla oblongata;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;cingulate cortex;parietal lobe;skeletal muscle; 0.22175 0.11147 -0.161524709 41.6430762 99.13934 2.15486 BTBD2 0.98767894213597 0.0123161840892528 4.87377477675391e-06 BTB domain containing 2 . . . ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;lens;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;stomach; whole brain;amygdala;dorsal root ganglion;medulla oblongata;subthalamic nucleus;temporal lobe;prefrontal cortex;skeletal muscle;cingulate cortex;cerebellum; 0.16014 0.11161 -0.622676946 17.30950696 3774.01478 12.02834 BTBD3 0.0614215773226243 0.92235885935359 0.0162195633237853 BTB domain containing 3 FUNCTION: Acts as a key regulator of dendritic field orientation during development of sensory cortex. Also directs dendrites toward active axon terminals when ectopically expressed (By similarity). {ECO:0000250}.; . . colon;fovea centralis;choroid;skin;retina;uterus;subthalamic nucleus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;bone;iris;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;hypothalamus;spinal cord;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; amygdala;cerebellum peduncles;prefrontal cortex;parietal lobe;cerebellum; 0.24723 0.11646 -0.025608647 51.91672564 77.08743 1.84386 BTBD6 0.000422096018258331 0.856513603979356 0.143064300002386 BTB domain containing 6 FUNCTION: Adapter protein for the CUL3 E3 ubiquitin-protein ligase complex. Involved in late neuronal development and muscle formation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in lens. {ECO:0000269|PubMed:12107413}.; lymphoreticular;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;trigeminal ganglion;skeletal muscle;cerebellum; 0.15911 0.11022 -0.88906181 10.36801132 51.18951 1.41029 BTBD6P1 . . . BTB domain containing 6 pseudogene 1 . . . . . . . . . . . BTBD7 0.682366256826822 0.317633427565916 3.15607262838321e-07 BTB domain containing 7 FUNCTION: Acts as a mediator of epithelial dynamics and organ branching by promoting cleft progression. Induced following accumulation of fibronectin in forming clefts, leading to local expression of the cell-scattering SNAIL2 and suppression of E- cadherin levels, thereby altering cell morphology and reducing cell-cell adhesion. This stimulates cell separation at the base of forming clefts by local, dynamic intercellular gap formation and promotes cleft progression (By similarity). {ECO:0000250}.; . . ovary;salivary gland;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;parietal lobe;skeletal muscle; 0.40570 . -0.947938165 9.341825902 455.53339 4.43320 BTBD7P1 . . . BTB domain containing 7 pseudogene 1 . . . . . . . . . . . BTBD7P2 . . . BTB domain containing 7 pseudogene 2 . . . . . . . . . . . BTBD8 1.30361769669498e-06 0.37258991443293 0.627408781949373 BTB domain containing 8 . . TISSUE SPECIFICITY: Highly expressed in fetal brain. Weakly expressed in adult brain and prostate. {ECO:0000269|PubMed:14654994}.; skeletal muscle; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.00047 0.01177 0.639420866 83.8995046 141.96036 2.60158 BTBD9 0.00573299396733052 0.993286178262532 0.000980827770137838 BTB domain containing 9 . . TISSUE SPECIFICITY: Highly expressed in kidney and moderately expressed in all other adult and fetal tissues. Moderately expressed in all specific brain regions examined. {ECO:0000269|PubMed:11572484}.; unclassifiable (Anatomical System);lung;nasopharynx;placenta;testis;skeletal muscle; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.31062 0.12220 -0.957024976 9.088228356 18.76686 0.64776 BTBD9-AS1 . . . BTBD9 antisense RNA 1 . . . . . . . . . . . BTBD10 0.477320145122737 0.522636541546413 4.33133308504479e-05 BTB domain containing 10 FUNCTION: Plays a major role as an activator of AKT family members by inhibiting PPP2CA-mediated dephosphorylation, thereby keeping AKTs activated. Plays a role in preventing motor neuronal death and accelerating the growth of pancreatic beta cells. {ECO:0000250|UniProtKB:Q80X66}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in adult brain, testis, aorta and small intestine and weakly expressed in the heart, lung, liver, kidney, pancreas, spleen, thymus, prostate, ovary and colon. Down-regulated in glioma. {ECO:0000269|PubMed:15556295, ECO:0000269|PubMed:21267538}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; . 0.42632 0.11581 -0.227663163 37.11370606 65.35906 1.66397 BTBD10P1 . . . BTB domain containing 10 pseudogene 1 . . . . . . . . . . . BTBD10P2 . . . BTB domain containing 10 pseudogene 2 . . . . . . . . . . . BTBD11 0.99343298086277 0.00656701048213895 8.65509091523511e-09 BTB domain containing 11 . . . unclassifiable (Anatomical System);heart;islets of Langerhans;parathyroid;whole body;lung;frontal lobe;cochlea;endometrium;adrenal gland;thyroid;visual apparatus;testis;spleen;kidney;brain;bladder;tonsil; . 0.42445 0.12301 -0.462894052 23.62585515 7389.82344 18.45720 BTBD16 3.41362084542176e-12 0.0817851334430378 0.918214866553549 BTB domain containing 16 . . . lung;placenta;testis; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.06774 0.06961 0.604424343 82.90280727 1433.42927 7.06880 BTBD17 0.0108349364889999 0.835322528937996 0.153842534573004 BTB domain containing 17 . . . . . . . . . 729.22708 5.36060 BTBD18 . . . BTB domain containing 18 . . . . . . . 0.169169615 65.33380514 49.62892 1.37997 BTBD19 . . . BTB domain containing 19 . . . . . . . . . 60.43881 1.58041 BTC 0.116138687032558 0.778761199191269 0.105100113776173 betacellulin FUNCTION: Growth factor that binds to EGFR, ERBB4 and other EGF receptor family members. Potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. {ECO:0000269|PubMed:8570211}.; . TISSUE SPECIFICITY: Synthesized in several tissues and tumor cells. Predominantly expressed in pancreas and small intestine. {ECO:0000269|PubMed:8919026}.; . . 0.39487 0.23899 0.327131069 73.27199811 3378.31462 11.12923 BTD 1.28845384445698e-06 0.210972260112517 0.789026451433638 biotinidase FUNCTION: Catalytic release of biotin from biocytin, the product of biotin-dependent carboxylases degradation.; DISEASE: Biotinidase deficiency (BTD deficiency) [MIM:253260]: A juvenile form of multiple carboxylase deficiency, an autosomal recessive disorder of biotin metabolism, characterized by ketoacidosis, hyperammonemia, excretion of abnormal organic acid metabolites, and dermatitis. Biotinidase deficiency is characterized by seizures, hypotonia, skin rash, alopecia, ataxia, hearing loss, and optic atrophy. If untreated, symptoms usually become progressively worse, and coma and death may occur. {ECO:0000269|PubMed:10206677, ECO:0000269|PubMed:9099842, ECO:0000269|PubMed:9654207}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;vein;skin;retina;uterus;prostate;optic nerve;cerebral cortex;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;adrenal gland;placenta;visual apparatus;liver;spleen;kidney;stomach; dorsal root ganglion;placenta;liver;testis;trigeminal ganglion; 0.06254 0.23561 0.023941474 55.75607455 282.72952 3.59917 BTF3 0.904371539633102 0.0948302739845624 0.000798186382335167 basic transcription factor 3 FUNCTION: When associated with NACA, prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. BTF3 is also a general transcription factor that can form a stable complex with RNA polymerase II. Required for the initiation of transcription. {ECO:0000269|PubMed:10982809}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;pituitary gland;testis;germinal center;brain;artery;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pineal body;muscle;adrenal cortex;pharynx;blood;cerebrum;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;kidney;mammary gland;aorta;stomach;thymus; uterus;placenta;thyroid;white blood cells; 0.40567 0.10783 -0.141298762 42.87567823 16.96823 0.59753 BTF3L4 0.451300212005922 0.520919921555233 0.0277798664388453 basic transcription factor 3-like 4 . . . . . 0.35480 0.10717 0.057118534 57.99716914 2.48786 0.09156 BTF3L4P1 . . . basic transcription factor 3-like 4 pseudogene 1 . . . . . . . . . . . BTF3L4P2 . . . basic transcription factor 3-like 4 pseudogene 2 . . . . . . . . . . . BTF3L4P3 . . . basic transcription factor 3-like 4 pseudogene 3 . . . . . . . . . . . BTF3L4P4 . . . basic transcription factor 3-like 4 pseudogene 4 . . . . . . . . . . . BTF3P1 . . . basic transcription factor 3, pseudogene 1 . . . . . . . . . . . BTF3P2 . . . basic transcription factor 3, pseudogene 2 . . . . . . . . . . . BTF3P3 . . . basic transcription factor 3, pseudogene 3 . . . . . . . . . . . BTF3P4 . . . basic transcription factor 3 pseudogene 4 . . . . . . . . . . . BTF3P5 . . . basic transcription factor 3 pseudogene 5 . . . . . . . . . . . BTF3P6 . . . basic transcription factor 3 pseudogene 6 . . . . . . . . . . . BTF3P7 . . . basic transcription factor 3 pseudogene 7 . . . . . . . . . . . BTF3P8 . . . basic transcription factor 3 pseudogene 8 . . . . . . . . . . . BTF3P9 . . . basic transcription factor 3 pseudogene 9 . . . . . . . . . . . BTF3P10 . . . basic transcription factor 3 pseudogene 10 . . . . . . . . . . . BTF3P11 . . . basic transcription factor 3 pseudogene 11 FUNCTION: Acts as decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis. {ECO:0000269|PubMed:22664871, ECO:0000269|PubMed:9168977}.; DISEASE: Paget disease of bone 5, juvenile-onset (PDB5) [MIM:239000]: An autosomal recessive, juvenile-onset form of Paget disease, a disorder of bone remodeling characterized by increased bone turnover affecting one or more sites throughout the skeleton, primarily the axial skeleton. Osteoclastic overactivity followed by compensatory osteoblastic activity leads to a structurally disorganized mosaic of bone (woven bone), which is mechanically weaker, larger, less compact, more vascular, and more susceptible to fracture than normal adult lamellar bone. PDB5 clinical manifestations include short stature, progressive long bone deformities, fractures, vertebral collapse, skull enlargement, and hyperostosis with progressive deafness. {ECO:0000269|PubMed:12189164}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in adult lung, heart, kidney, liver, spleen, thymus, prostate, ovary, small intestine, thyroid, lymph node, trachea, adrenal gland, testis, and bone marrow. Detected at very low levels in brain, placenta and skeletal muscle. Highly expressed in fetal kidney, liver and lung.; . . 0.32500 0.05891 -0.291981272 33.20358575 . . BTF3P12 . . . basic transcription factor 3 pseudogene 12 . . . . . . . . . . . BTF3P13 . . . basic transcription factor 3 pseudogene 13 . . . . . . . . . . . BTF3P14 . . . basic transcription factor 3 pseudogene 14 . . . . . . . . . . . BTF3P15 . . . basic transcription factor 3 pseudogene 15 . . . . . . . . . . . BTF3P16 . . . basic transcription factor 3 pseudogene 16 . . . . . . . . . . . BTG1 0.483157589180579 0.494638413683172 0.0222039971362484 B-cell translocation gene 1, anti-proliferative FUNCTION: Anti-proliferative protein. {ECO:0000269|PubMed:1373383}.; DISEASE: Note=A chromosomal aberration involving BTG1 may be a cause of a form of B-cell chronic lymphocytic leukemia. Translocation t(8;12)(q24;q22) with MYC. {ECO:0000269|PubMed:2069907}.; . myocardium;lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;cervix;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;aorta; prostate;placenta;white blood cells;whole blood;thymus;cerebellum;bone marrow; 0.72874 0.21177 0.125076652 62.7388535 77.70532 1.85678 BTG1P1 . . . B-cell translocation gene 1 pseudogene 1 . . . . . . . . . . . BTG2 0.0489784871870145 0.685197566370051 0.265823946442935 BTG family member 2 FUNCTION: Anti-proliferative protein; the function is mediated by association with deadenylase subunits of the CCR4-NOT complex. Activates mRNA deadenylation in a CNOT6 and CNOT7-dependent manner. In vitro can inhibit deadenylase activity of CNOT7 and CNOT8. Involved in cell cycle regulation. Could be involved in the growth arrest and differentiation of the neuronal precursors (By similarity). Modulates transcription regulation mediated by ESR1. Involved in mitochondrial depolarization and neurite outgrowth. {ECO:0000250, ECO:0000269|PubMed:12771185, ECO:0000269|PubMed:15788397, ECO:0000269|PubMed:18337750, ECO:0000269|PubMed:18773938, ECO:0000269|PubMed:23236473}.; . . lymphoreticular;smooth muscle;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;oesophagus;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;urinary;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;adrenal cortex;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.59042 0.11110 -0.207437529 38.2814343 44.13231 1.26674 BTG3 0.696545555394833 0.299582920447585 0.00387152415758237 BTG family member 3 FUNCTION: Overexpression impairs serum-induced cell cycle progression from the G0/G1 to S phase.; . TISSUE SPECIFICITY: Ubiquitous. High expression in the ventricular zone of the developing central nervous system. High in ovary, testis, prostate, thymus and lung. {ECO:0000269|PubMed:9067576}.; myocardium;medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;uterus;prostate;frontal lobe;cochlea;endometrium;bone;thyroid;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;breast;pancreas;lung;epididymis;nasopharynx;trabecular meshwork;placenta;hippocampus;visual apparatus;liver;hypopharynx;alveolus;cervix;spleen;head and neck;kidney;stomach; fetal liver;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.46652 0.13320 -0.163345027 41.24793583 10.97144 0.39638 BTG3P1 . . . BTG family member 3 pseudogene 1 . . . . . . . . . . . BTG4 0.256389240572353 0.716126204773292 0.0274845546543555 BTG family member 4 FUNCTION: Shows marked antiproliferative activity, being able to induce G(1) arrest.; . TISSUE SPECIFICITY: Highly expressed in testis and in olfactory epithelium.; unclassifiable (Anatomical System);lung;testis; testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;skeletal muscle; 0.21733 0.13745 -0.295622497 32.61972163 10.78111 0.39103 BTG4P1 . . . B-cell translocation gene 4 pseudogene 1 . . . . . . . . . . . BTK 0.999563220319725 0.000436778274450126 1.40582466063449e-09 Bruton tyrosine kinase FUNCTION: Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members. PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK. BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways. Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway. The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense. Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells. Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation. BTK plays also a critical role in transcription regulation. Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes. BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B. Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR. GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression. ARID3A and NFAT are other transcriptional target of BTK. BTK is required for the formation of functional ARID3A DNA-binding complexes. There is however no evidence that BTK itself binds directly to DNA. BTK has a dual role in the regulation of apoptosis. {ECO:0000269|PubMed:11606584, ECO:0000269|PubMed:16415872, ECO:0000269|PubMed:16517732, ECO:0000269|PubMed:16738337, ECO:0000269|PubMed:17932028, ECO:0000269|PubMed:9012831}.; DISEASE: X-linked agammaglobulinemia (XLA) [MIM:300755]: Humoral immunodeficiency disease which results in developmental defects in the maturation pathway of B-cells. Affected boys have normal levels of pre-B-cells in their bone marrow but virtually no circulating mature B-lymphocytes. This results in a lack of immunoglobulins of all classes and leads to recurrent bacterial infections like otitis, conjunctivitis, dermatitis, sinusitis in the first few years of life, or even some patients present overwhelming sepsis or meningitis, resulting in death in a few hours. Treatment in most cases is by infusion of intravenous immunoglobulin. {ECO:0000269|PubMed:10220140, ECO:0000269|PubMed:10612838, ECO:0000269|PubMed:10678660, ECO:0000269|PubMed:7627183, ECO:0000269|PubMed:7633420, ECO:0000269|PubMed:7633429, ECO:0000269|PubMed:7711734, ECO:0000269|PubMed:7809124, ECO:0000269|PubMed:7849006, ECO:0000269|PubMed:7849697, ECO:0000269|PubMed:7849721, ECO:0000269|PubMed:7880320, ECO:0000269|PubMed:7897635, ECO:0000269|PubMed:8013627, ECO:0000269|PubMed:8162018, ECO:0000269|PubMed:8162056, ECO:0000269|PubMed:8634718, ECO:0000269|PubMed:8695804, ECO:0000269|PubMed:8723128, ECO:0000269|PubMed:8834236, ECO:0000269|PubMed:9260159, ECO:0000269|PubMed:9280283, ECO:0000269|PubMed:9445504, ECO:0000269|PubMed:9545398}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: X-linked hypogammaglobulinemia and isolated growth hormone deficiency (XLA-IGHD) [MIM:307200]: In rare cases XLA is inherited together with isolated growth hormone deficiency (IGHD). Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in B-lymphocytes.; unclassifiable (Anatomical System);lymphoreticular;lymph node;cartilage;colon;blood;bone marrow;uterus;lung;thyroid;bone;liver;spleen;germinal center;brain; superior cervical ganglion;ciliary ganglion; 0.57908 0.55976 -0.117432389 44.89266336 11.53848 0.41735 BTLA 0.430977023003583 0.561803875371244 0.00721910162517311 B and T lymphocyte associated FUNCTION: Lymphocyte inhibitory receptor which inhibits lymphocytes during immune response. {ECO:0000269|PubMed:12796776}.; . . unclassifiable (Anatomical System);lung;nasopharynx;testis;blood;kidney;brain;bone marrow; . 0.06425 0.12695 0.813985927 87.81552253 2.21801 0.07436 BTN1A1 1.14088369109076e-09 0.0941241388035704 0.905875860055546 butyrophilin subfamily 1 member A1 FUNCTION: May function in the secretion of milk-fat droplets. May act as a specific membrane-associated receptor for the association of cytoplasmic droplets with the apical plasma membrane (By similarity). Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);germinal center; superior cervical ganglion; 0.13191 0.19958 0.841481379 88.35810333 177.56691 2.89677 BTN1A1P1 . . . butyrophilin subfamily 1 member A1 pseudogene 1 . . . . . . . . . . . BTN2A1 1.07467588553941e-18 0.00017167758924748 0.999828322410752 butyrophilin subfamily 2 member A1 . . TISSUE SPECIFICITY: Highly expressed in brain, bone marrow, small intestine, muscle, spleen and pancreas. Moderate expression was seen in lung, liver and kidney. {ECO:0000269|PubMed:9149941}.; ovary;colon;parathyroid;retina;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;duodenum;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cerebellum; 0.06939 0.08981 0.870809653 88.86529842 1075.87119 6.28661 BTN2A2 0.000150288420483044 0.965321502405181 0.0345282091743356 butyrophilin subfamily 2 member A2 FUNCTION: Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in brain, bone marrow, small intestine, muscle, spleen and pancreas. Moderate expression was seen in lung, liver and kidney. {ECO:0000269|PubMed:9149941}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;colon;parathyroid;blood;skeletal muscle;uterus;prostate;lung;thyroid;placenta;visual apparatus;liver;spleen;germinal center;kidney;brain;mammary gland;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.09643 0.12481 2.245250033 98.19532909 691.12014 5.24317 BTN2A3P . . . butyrophilin subfamily 2 member A3, pseudogene . . . colon; superior cervical ganglion; 0.08337 . . . . . BTN3A1 8.65113669435817e-07 0.747593221414351 0.252405913471979 butyrophilin subfamily 3 member A1 FUNCTION: Plays a role in T-cell activation and in the adaptive immune response. Regulates the proliferation of activated T-cells. Regulates the release of cytokines and IFNG by activated T-cells. Mediates the response of T-cells toward infected and transformed cells that are characterized by high levels of phosphorylated metabolites, such as isopentenyl pyrophosphate. {ECO:0000269|PubMed:21113407, ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497, ECO:0000269|PubMed:22846996}.; . TISSUE SPECIFICITY: Detected on T-cells, natural killer cells, dendritic cells and macrophages (at protein level). Ubiquitous. Highly expressed in heart, pancreas and lung, Moderately expressed in placenta, liver and muscle. {ECO:0000269|PubMed:20610803, ECO:0000269|PubMed:21113407, ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:9149941}.; colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;dura mater;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);meninges;lymph node;cartilage;blood;breast;pia mater;lung;placenta;hippocampus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;skeletal muscle; 0.06787 0.07707 0.531004228 80.87992451 647.15095 5.10575 BTN3A2 0.000124518814289725 0.840379954155929 0.159495527029782 butyrophilin subfamily 3 member A2 FUNCTION: Plays a role in T-cell responses in the adaptive immune response. Inhibits the release of IFNG from activated T-cells. {ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}.; . TISSUE SPECIFICITY: Detected in T-cells and natural killer cells. {ECO:0000269|PubMed:21918970}.; unclassifiable (Anatomical System);lymph node;islets of Langerhans;skin;bone marrow;breast;lung;endometrium;nasopharynx;thyroid;placenta;visual apparatus;cervix;kidney;brain;aorta;stomach; white blood cells;whole blood;skeletal muscle; 0.06491 0.07172 0.795569043 87.49115357 1740.69093 7.70186 BTN3A3 7.19024879190517e-10 0.246806884963541 0.753193114317435 butyrophilin subfamily 3 member A3 FUNCTION: Plays a role in T-cell responses in the adaptive immune response. {ECO:0000269|PubMed:22767497}.; . TISSUE SPECIFICITY: Detected in peripheral blood mononuclear cells and in T-cells (at protein level). Detected in spleen and lymphocytes. {ECO:0000269|PubMed:20610803}.; ovary;colon;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;white blood cells; 0.11114 0.09582 -0.28470423 33.48667138 154.38227 2.71544 BTNL2 2.02725572868094e-07 0.256945600116021 0.743054197158406 butyrophilin like 2 FUNCTION: Negative regulator of T-cell proliferation. {ECO:0000250}.; DISEASE: Sarcoidosis 2 (SS2) [MIM:612387]: An idiopathic, systemic, inflammatory disease characterized by the formation of immune granulomas in involved organs. Granulomas predominantly invade the lungs and the lymphatic system, but also skin, liver, spleen, eyes and other organs may be involved. {ECO:0000269|PubMed:15735647}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. A nucleotide transition affecting a splice donor site results in the use of an alternative splice site and the production of isoform 3. Individuals expressing isoform 3 have a higher risk for sarcoidosis.; TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, pancreas, ovary, leukocyte, small intestine, testis and thymus. {ECO:0000269|PubMed:15735647}.; . . 0.05667 . . . 12487.13218 23.99230 BTNL3 0.0396371481687155 0.953685804761489 0.00667704706979559 butyrophilin like 3 . . TISSUE SPECIFICITY: Expressed in small intestine, colon, testis, spleen, and leukocyte. {ECO:0000269|PubMed:10429365}.; unclassifiable (Anatomical System); dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.03468 0.06141 1.2860853 93.80160415 332.85405 3.87746 BTNL8 0.000235087769484238 0.919937414122037 0.0798274981084783 butyrophilin like 8 FUNCTION: May stimulate primary immune response. Acts on T-cell stimulated sub-optimally through the TCR/CD3 complex stimulating their proliferation and cytokine production. {ECO:0000269|PubMed:24036152}.; . TISSUE SPECIFICITY: Expressed in neutrophils. Isoforms 1 and 5 are expressed at high levels in the colon, lung,testis, lymph nodes and thyroid tissue. Isoform 5, but not isoform 1, is detected in spleen. {ECO:0000269|PubMed:24036152}.; unclassifiable (Anatomical System);lung;testis;colon;skeletal muscle;stomach; superior cervical ganglion;appendix;whole blood;skeletal muscle; . . 2.513579985 98.67303609 433.67457 4.34596 BTNL9 6.53404156111455e-10 0.128525451815584 0.871474547531012 butyrophilin like 9 . . . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;colon;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;pancreas;optic nerve;lung;endometrium;larynx;placenta;macula lutea;testis;head and neck;germinal center;kidney;spinal ganglion;brain;stomach; globus pallidus;ciliary ganglion;atrioventricular node; 0.12916 . -0.134019284 43.90776126 185.79362 2.95953 BTNL10 . . . butyrophilin like 10 . . . . . . . . . . . BTRC 0.863167823590213 0.136832033318443 1.43091343463084e-07 beta-transducin repeat containing E3 ubiquitin protein ligase FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds to phosphorylated target proteins. SCF(BTRC) mediates the ubiquitination of CTNNB1 and participates in Wnt signaling. SCF(BTRC) mediates the ubiquitination of NFKBIA, NFKBIB and NFKBIE; the degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. Ubiquitination of NFKBIA occurs at 'Lys- 21' and 'Lys-22'. SCF(BTRC) mediates the ubiquitination of CEP68; this is required for centriole separation during mitosis (PubMed:25704143, PubMed:25503564). SCF(BTRC) mediates the ubiquitination of phosphorylated NFKB1/nuclear factor NF-kappa-B p105 subunit, ATF4, CDC25A, DLG1, FBXO5, PER1, SMAD3, SMAD4, SNAI1 and probably NFKB2. Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and PER2. May be involved in ubiquitination and subsequent proteasomal degradation through a DBB1-CUL4 E3 ubiquitin-protein ligase. Required for activation of NFKB-mediated transcription by IL1B, MAP3K14, MAP3K1, IKBKB and TNF. Required for proteolytic processing of GLI3. {ECO:0000269|PubMed:10066435, ECO:0000269|PubMed:10497169, ECO:0000269|PubMed:10644755, ECO:0000269|PubMed:10835356, ECO:0000269|PubMed:11238952, ECO:0000269|PubMed:11359933, ECO:0000269|PubMed:11994270, ECO:0000269|PubMed:12791267, ECO:0000269|PubMed:12902344, ECO:0000269|PubMed:14603323, ECO:0000269|PubMed:14681206, ECO:0000269|PubMed:14988407, ECO:0000269|PubMed:15448698, ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:16371461, ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:25704143, ECO:0000269|PubMed:9859996}.; . TISSUE SPECIFICITY: Expressed in epididymis (at protein level). {ECO:0000269|PubMed:20736409}.; . . 0.30019 0.54005 -0.380166007 27.88393489 234.394 3.30949 BTRCP1 . . . beta-transducin repeat containing E3 ubiquitin protein ligase pseudogene 1 . . . . . . . . . . . BTS1 . . . bladder tumor susceptibility 1 . . . . . . . . . . . BUB1 4.49651698196957e-06 0.999914903747358 8.05997356603042e-05 BUB1 mitotic checkpoint serine/threonine kinase FUNCTION: Serine/threonine-protein kinase that performs 2 crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Has a key role in the assembly of checkpoint proteins at the kinetochore, being required for the subsequent localization of CENPF, BUB1B, CENPE and MAD2L1. Required for the kinetochore localization of PLK1. Plays an important role in defining SGOL1 localization and thereby affects sister chromatid cohesion. Acts as a substrate for anaphase-promoting complex or cyclosome (APC/C) in complex with its activator CDH1 (APC/C-Cdh1). Necessary for ensuring proper chromosome segregation and binding to BUB3 is essential for this function. Can regulate chromosome segregation in a kinetochore-independent manner. Can phosphorylate BUB3. The BUB1-BUB3 complex plays a role in the inhibition of APC/C when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1. Kinase activity is essential for inhibition of APC/CCDC20 and for chromosome alignment but does not play a major role in the spindle-assembly checkpoint activity. Mediates cell death in response to chromosome missegregation and acts to suppress spontaneous tumorigenesis. {ECO:0000269|PubMed:10198256, ECO:0000269|PubMed:15020684, ECO:0000269|PubMed:15525512, ECO:0000269|PubMed:15723797, ECO:0000269|PubMed:16760428, ECO:0000269|PubMed:17158872, ECO:0000269|PubMed:19487456}.; . TISSUE SPECIFICITY: High expression in testis and thymus, less in colon, spleen, lung and small intestine. Expressed in fetal thymus, bone marrow, heart, liver, spleen and thymus. Expression is associated with cells/tissues with a high mitotic index.; unclassifiable (Anatomical System);lymph node;ovary;adrenal cortex;colon;skin;skeletal muscle;breast;uterus;bile duct;whole body;lung;nasopharynx;bone;duodenum;liver;testis;cervix;spleen;germinal center;brain;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;tumor;testis;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.99564 0.25794 -1.217968826 5.638122199 65.21176 1.66169 BUB1B 0.00263162333228221 0.997368168690492 2.07977225617177e-07 BUB1 mitotic checkpoint serine/threonine kinase B FUNCTION: Essential component of the mitotic checkpoint. Required for normal mitosis progression. The mitotic checkpoint delays anaphase until all chromosomes are properly attached to the mitotic spindle. One of its checkpoint functions is to inhibit the activity of the anaphase-promoting complex/cyclosome (APC/C) by blocking the binding of CDC20 to APC/C, independently of its kinase activity. The other is to monitor kinetochore activities that depend on the kinetochore motor CENPE. Required for kinetochore localization of CENPE. Negatively regulates PLK1 activity in interphase cells and suppresses centrosome amplification. Also implicated in triggering apoptosis in polyploid cells that exit aberrantly from mitotic arrest. May play a role for tumor suppression. {ECO:0000269|PubMed:10477750, ECO:0000269|PubMed:11702782, ECO:0000269|PubMed:14706340, ECO:0000269|PubMed:15020684, ECO:0000269|PubMed:19411850, ECO:0000269|PubMed:19503101}.; DISEASE: Note=Defects in BUB1B are associated with tumor formation.; DISEASE: Premature chromatid separation trait (PCS) [MIM:176430]: Consists of separate and splayed chromatids with discernible centromeres and involves all or most chromosomes of a metaphase. It is found in up to 2% of metaphases in cultured lymphocytes from approximately 40% of normal individuals. When PCS is present in 5% or more of cells, it is known as the heterozygous PCS trait and has no obvious phenotypic effect, although some have reported decreased fertility. Inheritance is autosomal dominant. {ECO:0000269|PubMed:16411201}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mosaic variegated aneuploidy syndrome 1 (MVA1) [MIM:257300]: A severe developmental disorder characterized by mosaic aneuploidies, predominantly trisomies and monosomies, involving multiple different chromosomes and tissues. Affected individuals typically present with severe intrauterine growth retardation and microcephaly. Eye anomalies, mild dysmorphism, variable developmental delay, and a broad spectrum of additional congenital abnormalities and medical conditions may also occur. The risk of malignancy is high, with rhabdomyosarcoma, Wilms tumor and leukemia reported in several cases. {ECO:0000269|PubMed:15475955}. Note=The disease is caused by mutations affecting the gene represented in this entry. MVA1 is caused by biallelic mutations in the BUB1B gene.; TISSUE SPECIFICITY: Highly expressed in thymus followed by spleen. Preferentially expressed in tissues with a high mitotic index. {ECO:0000269|PubMed:10593653}.; unclassifiable (Anatomical System);ovary;heart;adrenal cortex;colon;parathyroid;blood;skin;skeletal muscle;bone marrow;breast;uterus;bile duct;whole body;lung;bone;placenta;liver;testis;cervix;spleen;germinal center;brain;mammary gland;stomach; superior cervical ganglion;tumor;testis; 0.92121 0.26315 -0.062423436 48.86765747 874.14286 5.75321 BUB1P1 . . . BUB1 mitotic checkpoint serine/threonine kinase pseudogene 1 . . . . . . . . . . . BUB3 0.554686126711163 0.444738394619099 0.000575478669738312 BUB3 mitotic checkpoint protein FUNCTION: Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. Regulates chromosome segregation during oocyte meiosis. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1. {ECO:0000269|PubMed:10198256, ECO:0000269|PubMed:15525512, ECO:0000269|PubMed:18199686}.; . . . . 0.95603 0.20297 -0.207437529 38.2814343 7.12358 0.26577 BUB3P1 . . . BUB3 mitotic checkpoint protein pseudogene 1 . . . . . . . . . . . BUD13 0.00229542848916745 0.994047189278359 0.00365738223247342 BUD13 homolog . . . unclassifiable (Anatomical System);medulla oblongata;cartilage;sympathetic chain;adrenal cortex;colon;choroid;skin;skeletal muscle;uterus;prostate;whole body;lung;frontal lobe;endometrium;nasopharynx;bone;placenta;visual apparatus;hippocampus;testis;cervix;germinal center;kidney;brain;stomach; superior cervical ganglion;testis;ciliary ganglion; 0.20921 0.07302 0.778977686 87.21396556 1508.32155 7.21483 BUD13P1 . . . BUD13 homolog pseudogene 1 . . . . . . . . . . . BUD31 0.417010233438905 0.547812947673638 0.0351768188874579 BUD31 homolog . . . lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.22373 0.12378 -0.031067188 51.03798066 6.06044 0.22934 BUD31P1 . . . BUD31 homolog pseudogene 1 . . . . . . . . . . . BUD31P2 . . . BUD31 homolog pseudogene 2 . . . . . . . . . . . BVES 0.000308542708446569 0.942396253846492 0.0572952034450615 blood vessel epicardial substance FUNCTION: Cell adhesion molecule involved in the establishment and/or maintenance of cell integrity. Involved in the formation and regulation of the tight junction (TJ) paracellular permeability barrier in epithelial cells. Plays a role in VAMP3- mediated vesicular transport and recycling of different receptor molecules through its interaction with VAMP3. Plays a role in the regulation of cell shape and movement by modulating the Rho-family GTPase activity through its interaction with ARHGEF25/GEFT. Induces primordial adhesive contact and aggregation of epithelial cells in a Ca(2+)-independent manner. Also involved in striated muscle regeneration and repair and in the regulation of cell spreading. {ECO:0000269|PubMed:16188940}.; . TISSUE SPECIFICITY: Expressed in epithelial cells (at protein level). Expressed in fetal and adult heart and skeletal muscle. {ECO:0000269|PubMed:10441744, ECO:0000269|PubMed:10882522, ECO:0000269|PubMed:16188940}.; unclassifiable (Anatomical System);cartilage;heart;urinary;parathyroid;skeletal muscle;skin;uterus;breast;lung;whole body;frontal lobe;liver;testis;brain; dorsal root ganglion;testis - interstitial;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.30426 0.13165 0.062575634 58.74026893 234.70637 3.31092 BVES-AS1 . . . BVES antisense RNA 1 . . . . . . . . . . . BVR1 . . . Burkitt lymphoma variant rearranging region 1 . . . . . . . . . . . BYSL 0.0673214421779635 0.929745128857109 0.00293342896492708 bystin like FUNCTION: Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits. May be required for trophinin-dependent regulation of cell adhesion during implantation of human embryos. {ECO:0000269|PubMed:17360433, ECO:0000269|PubMed:17381424}.; . TISSUE SPECIFICITY: Found in the placenta from the sixth week of pregnancy. Was localized in the cytoplasm of the syncytiotrophoblast in the chorionic villi and in endometrial decidual cells at the uteroplacental interface. After week 10, the level decreased and then disappeared from placental villi.; lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach; skeletal muscle; 0.60341 0.15537 0.442818085 77.8544468 1256.33001 6.68385 BZRAP1 0.0566264084919234 0.943373591059783 4.48293856534019e-10 benzodiazepine receptor (peripheral) associated protein 1 . . TISSUE SPECIFICITY: Predominantly expressed in brain, pituitary gland and thymus in adults. In adult brain, highest expression found in temporal lobe and the putamen, followed by amygdala, caudate nucleus, cerebral cortex, occipital and frontal lobe. A high expression level is also observed in fetal tissues like brain, heart, kidney and thymus. {ECO:0000269|PubMed:9915832}.; unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;parathyroid;fovea centralis;retina;breast;lung;frontal lobe;endometrium;placenta;macula lutea;visual apparatus;brain;gall bladder; superior cervical ganglion; 0.23672 0.12463 2.278633089 98.27199811 3139.02127 10.67050 BZRAP1-AS1 . . . BZRAP1 antisense RNA 1 . . . . . . . . . . . BZW1 0.744805846771698 0.254714900221493 0.000479253006809217 basic leucine zipper and W2 domains 1 FUNCTION: Enhances histone H4 gene transcription but does not seem to bind DNA directly. {ECO:0000269|PubMed:11524015}.; . . unclassifiable (Anatomical System);prostate;pancreas;lung;cartilage;oesophagus;adrenal gland;larynx;bone;testis;parathyroid;blood;head and neck;brain;stomach; . 0.81847 . -0.185391282 39.67916962 74.81411 1.81004 BZW1P1 . . . basic leucine zipper and W2 domains 1 pseudogene 1 . . . . . . . . . . . BZW1P2 . . . basic leucine zipper and W2 domains 1 pseudogene 2 . . . . . . . . . . . BZW2 0.995822418135325 0.00417723599604285 3.45868631739275e-07 basic leucine zipper and W2 domains 2 FUNCTION: May be involved in neuronal differentiation. {ECO:0000250}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; placenta;skeletal muscle; 0.21920 0.12378 -0.404032746 26.53338051 1412.98537 7.02605 C1D 0.365972886685355 0.58436790432353 0.0496592089911158 C1D nuclear receptor corepressor FUNCTION: Plays a role in the recruitment of the RNA exosome complex to pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA; this function may include MPHOSPH6. Can activate PRKDC not only in the presence of linear DNA but also in the presence of supercoiled DNA. Can induce apoptosis in a p53/TP53 dependent manner. May regulate the TRAX/TSN complex formation. Potentiates transcriptional repression by NR1D1 and THRB (By similarity). {ECO:0000250, ECO:0000269|PubMed:10362552, ECO:0000269|PubMed:11801738, ECO:0000269|PubMed:17412707, ECO:0000269|PubMed:9679063}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed at very high levels in the hippocampus, medulla oblongata, mammary gland, thyroid and salivary gland. Expressed at high levels in the fetal; lung, liver and kidney. Expressed at low levels in skeletal muscle, appendix, heart, lung and colon. {ECO:0000269|PubMed:10362552}.; ovary;colon;parathyroid;skin;bone marrow;retina;uterus;prostate;whole body;cochlea;endometrium;testis;brain;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;skeletal muscle;pancreas;lung;placenta;liver;hypopharynx;spleen;kidney;aorta; . 0.65439 0.76644 0.147123112 64.11299835 788.33126 5.54291 C1DP1 . . . C1D nuclear receptor corepressor pseudogene 1 . . . . . . . . . . . C1DP2 . . . C1D nuclear receptor corepressor pseudogene 2 . . . . . . . . . . . C1DP3 . . . C1D nuclear receptor corepressor pseudogene 3 . . . . . . . . . . . C1DP4 . . . C1D nuclear receptor corepressor pseudogene 4 . . . . . . . . . . . C1DP5 . . . C1D nuclear receptor corepressor pseudogene 5 . . . . . . . . . . . C1GALT1 0.679379972140309 0.31604869363137 0.00457133422832172 core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1 FUNCTION: Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney, heart, placenta and liver. {ECO:0000269|PubMed:11677243}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;optic nerve;lung;endometrium;bone;placenta;macula lutea;liver;kidney;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17672 0.18814 0.082802743 60.09082331 105.00582 2.21619 C1GALT1C1 0.688732363511784 0.292866730662289 0.0184009058259273 C1GALT1 specific chaperone 1 FUNCTION: Probable chaperone required for the generation of 1 O- glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Probably acts as a specific molecular chaperone assisting the folding/stability of core 1 beta-3-galactosyltransferase (C1GALT1). {ECO:0000269|PubMed:12464682}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Abundantly expressed in salivary gland, stomach, small intestine, kidney, and testis and at intermediate levels in whole brain, cerebellum, spinal cord, thymus, spleen, trachea, lung, pancreas, ovary, and uterus. {ECO:0000269|PubMed:12361956}.; lymphoreticular;medulla oblongata;ovary;colon;parathyroid;skin;bone marrow;prostate;whole body;endometrium;larynx;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;skeletal muscle;bile duct;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.25938 0.14512 0.525552348 80.57914603 451.69887 4.41966 C1GALT1C1L . . . C1GALT1-specific chaperone 1 like . . . . . . . . . . . C1GALT1P1 . . . core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1 pseudogene 1 . . . . . . . . . . . C1GALT1P2 . . . ore 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1 pseudogene 2 . . . . . . . . . . . C1GALT1P3 . . . core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1 pseudogene 3 . . . . . . . . . . . C1orf21 0.81911661413853 0.176693640644878 0.00418974521659191 chromosome 1 open reading frame 21 . . TISSUE SPECIFICITY: Expressed in spleen, prostate, testis and uterus. {ECO:0000269|PubMed:11318611}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;bone;thyroid;iris;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;trabecular meshwork;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; amygdala;whole brain;occipital lobe;cerebellum peduncles;temporal lobe;prefrontal cortex;globus pallidus;cingulate cortex;skeletal muscle;parietal lobe; 0.25872 . -0.031067188 51.03798066 4.01295 0.14771 C1orf27 1.38118318297717e-06 0.610686166159859 0.389312452656958 chromosome 1 open reading frame 27 FUNCTION: May play a role in the trafficking of a subset of G- protein coupled receptors. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15718105}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;brain;artery;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;spinal cord;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;kidney;stomach;aorta;cerebellum; . 0.42092 0.09558 0.64123826 83.97617363 2150.67182 8.52624 C1orf35 0.0740070368474459 0.872432403145544 0.0535605600070103 chromosome 1 open reading frame 35 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;optic nerve;frontal lobe;oesophagus;endometrium;bone;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.12721 0.10787 0.813985927 87.81552253 136.86852 2.54257 C1orf43 0.173985957447014 0.823256495356019 0.00275754719696783 chromosome 1 open reading frame 43 . . . umbilical cord;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;testis;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; whole brain;medulla oblongata;caudate nucleus;parietal lobe; 0.12321 0.08084 0.058937498 58.26256192 48.7828 1.36231 C1orf50 0.00701592646307591 0.762823282420693 0.230160791116231 chromosome 1 open reading frame 50 . . . . . 0.04169 0.08926 0.569646743 81.88841708 . . C1orf52 0.359076551650837 0.588916166605624 0.0520072817435395 chromosome 1 open reading frame 52 . . TISSUE SPECIFICITY: Expressed in all tissues tested including heart, placenta, liver, skeletal muscle, kidney and pancreas. Weak expression in brain and lung. {ECO:0000269|PubMed:11891061}.; ovary;parathyroid;choroid;fovea centralis;skin;retina;uterus;whole body;optic nerve;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;kidney;mammary gland; whole brain;amygdala;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node; 0.14540 0.10285 -0.141298762 42.87567823 20.88942 0.70693 C1orf53 0.10469872738464 0.774824101114726 0.120477171500634 chromosome 1 open reading frame 53 . . TISSUE SPECIFICITY: Expressed in retina and retinoblastoma. {ECO:0000269|PubMed:15897902}.; . . 0.06951 . 0.191216164 66.57230479 74.09044 1.79827 C1orf54 0.178651547006617 0.766810305202412 0.054538147790971 chromosome 1 open reading frame 54 . . . . . 0.05802 . 0.191216164 66.57230479 108.74365 2.26343 C1orf56 0.00131728385359755 0.650219074215278 0.348463641931125 chromosome 1 open reading frame 56 FUNCTION: Involved in control of cellular proliferation. Onconcogenic modifier contributing to the tumor suppressor function of DNMT3B. {ECO:0000269|PubMed:22133874}.; . TISSUE SPECIFICITY: Plasma. Overexpressed in lymphomas. {ECO:0000269|PubMed:22133874}.; . . 0.07271 0.07189 0.327131069 73.27199811 200.14551 3.05763 C1orf61 0.104422489726842 0.774692493516338 0.12088501675682 chromosome 1 open reading frame 61 FUNCTION: May play a role in FOS signaling pathways involved in development and remodeling of neurons. Promotes transcription of the FOS promoter. {ECO:0000269|PubMed:10995546}.; . TISSUE SPECIFICITY: Expressed throughout the brain in the thalamus, subthalamic nucleus, corpus callosum, hippocampus, substantia nigra, caudate nucleus, and amygdala. {ECO:0000269|PubMed:10995546}.; unclassifiable (Anatomical System);whole body;lung;frontal lobe;hypothalamus;hippocampus;testis;germinal center;brain;skeletal muscle;aorta;retina; whole brain;dorsal root ganglion;amygdala;occipital lobe;superior cervical ganglion;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.02938 0.06789 -0.075159878 47.78839349 . . C1orf64 0.0105592094696203 0.615082732165787 0.374358058364592 chromosome 1 open reading frame 64 . . . unclassifiable (Anatomical System);myocardium;bone;pituitary gland;kidney;brain;mammary gland; subthalamic nucleus;atrioventricular node; 0.14624 . 0.193034296 66.82000472 35.27111 1.06718 C1orf68 . . . chromosome 1 open reading frame 68 . . TISSUE SPECIFICITY: Expressed at high levels in normal and psoriatic skin, but not in normal keratinocytes, A-431 cells, or any of the other cell lines or tissues tested. {ECO:0000269|PubMed:9344646}.; unclassifiable (Anatomical System); superior cervical ganglion;prefrontal cortex;parietal lobe; 0.17340 . 1.058333711 91.42486435 2358.51669 9.00743 C1orf74 0.489345231114962 0.489409884516117 0.0212448843689205 chromosome 1 open reading frame 74 . . . unclassifiable (Anatomical System);islets of Langerhans;colon;blood;bile duct;prostate;lung;endometrium;bone;testis;germinal center;kidney;brain;stomach; . 0.12648 . -0.095386216 46.48502005 1005.81156 6.10626 C1orf87 1.57688017827745e-17 0.000836017105177103 0.999163982894823 chromosome 1 open reading frame 87 . . . . . 0.05803 . 1.732552414 96.59707478 1349.54826 6.89808 C1orf94 0.00437226006687605 0.962858994288204 0.03276874564492 chromosome 1 open reading frame 94 . . . . . 0.15077 0.07960 1.089464986 91.87308327 1440.7657 7.08012 C1orf95 0.0920540809601597 0.766691258768372 0.141254660271469 chromosome 1 open reading frame 95 . . . . . 0.40385 . 0.013025609 54.62962963 27.70147 0.89054 C1orf100 3.53989017733453e-08 0.18393454922529 0.816065415375808 chromosome 1 open reading frame 100 . . . lung;testis; . 0.28623 . 0.014844891 54.94810097 33.01578 1.02199 C1orf101 5.88680638235274e-07 0.992747310332861 0.00725210098650072 chromosome 1 open reading frame 101 . . . . . 0.06458 . 0.848762413 88.48195329 140.98938 2.59028 C1orf105 0.000319847693203247 0.58451762475461 0.415162527552186 chromosome 1 open reading frame 105 . . . . . 0.05315 . 0.725794416 85.98136353 406.68154 4.22798 C1orf106 0.555282612544487 0.444144662881747 0.000572724573766499 chromosome 1 open reading frame 106 . . . . . 0.11765 0.09723 . . 814.70302 5.60865 C1orf109 6.27363023706354e-08 0.136862559326994 0.863137377936704 chromosome 1 open reading frame 109 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;kidney;stomach; superior cervical ganglion; 0.08312 . -0.029247611 51.40363293 31.26397 0.98562 C1orf111 2.10439313677877e-05 0.283374120295014 0.716604835773618 chromosome 1 open reading frame 111 . . . . . 0.27919 0.10215 0.418953042 77.06416608 57.70428 1.53464 C1orf112 5.98150986824657e-08 0.992096256977333 0.00790368320756798 chromosome 1 open reading frame 112 . . . unclassifiable (Anatomical System);smooth muscle;cartilage;ovary;heart;colon;parathyroid;blood;skin;bone marrow;uterus;bile duct;lung;cerebral cortex;oesophagus;placenta;liver;testis;cervix;germinal center;kidney;brain;aorta; superior cervical ganglion;testis - interstitial;testis;atrioventricular node;skin; 0.45663 . -0.196519234 39.20736023 683.3862 5.22243 C1orf115 0.283640867396314 0.63027558303758 0.086083549566106 chromosome 1 open reading frame 115 . . . ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;skeletal muscle;bile duct;breast;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;whole brain;medulla oblongata;occipital lobe;temporal lobe;caudate nucleus;pons;subthalamic nucleus;placenta;prefrontal cortex;globus pallidus;kidney;parietal lobe;cingulate cortex; 0.12612 0.11831 . . 32.67551 1.01553 C1orf116 0.371958031808421 0.625695823361752 0.00234614482982679 chromosome 1 open reading frame 116 FUNCTION: Putative androgen-specific receptor. {ECO:0000269|PubMed:15525603}.; . TISSUE SPECIFICITY: Highly expressed in prostate. {ECO:0000269|PubMed:15525603}.; lung; superior cervical ganglion;prostate;lung;temporal lobe;globus pallidus;fetal lung;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.04516 0.09308 2.804006769 99.0504836 958.7412 5.99359 C1orf122 0.123246499727265 0.611788457798415 0.264965042474321 chromosome 1 open reading frame 122 . . . . . 0.08947 0.05820 . . 10.43033 0.37890 C1orf123 1.26488229435833e-07 0.108798586788999 0.891201286722771 chromosome 1 open reading frame 123 . . . medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;salivary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;kidney;stomach;aorta; testis - interstitial;occipital lobe;testis; 0.19309 0.10466 0.215080721 67.91696155 21.87473 0.73604 C1orf127 1.33454849505904e-05 0.955388216648633 0.0445984378664161 chromosome 1 open reading frame 127 . . . . . 0.16480 . 0.986521626 90.48124558 1056.79352 6.24152 C1orf131 1.77283464318131e-07 0.131364033610489 0.868635789106047 chromosome 1 open reading frame 131 . . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;brain;pineal gland;unclassifiable (Anatomical System);heart;adrenal cortex;pharynx;blood;lens;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.07415 . 0.705562627 85.52724699 426.76694 4.31526 C1orf132 . . . chromosome 1 open reading frame 132 . . . . . 0.12724 . . . . . C1orf134 . . . chromosome 1 open reading frame 134 . . . . . 0.06999 . . . 2.76441 0.09859 C1orf137 . . . chromosome 1 open reading frame 137 . . . . . 0.06734 . . . 1.82362 0.05722 C1orf141 2.70036597974712e-05 0.531321038176278 0.468651958163925 chromosome 1 open reading frame 141 . . . . . 0.11027 . 0.883760026 89.07171503 276.1524 3.55817 C1orf143 . . . chromosome 1 open reading frame 143 . . . . . . . . . 264.75217 3.49168 C1orf145 0.097680709474626 0.578919591124281 0.323399699401093 chromosome 1 open reading frame 145 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;pancreas;lung;cornea;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; . 0.13548 . . . 308.95126 3.74239 C1orf146 0.0240479302432628 0.914841819193227 0.06111025056351 chromosome 1 open reading frame 146 . . . . . 0.05636 . 0.103030231 61.2762444 69.04862 1.72201 C1orf147 0.0120639015558244 0.412052076788119 0.575884021656056 chromosome 1 open reading frame 147 . . . . . 0.05339 . . . 698.79553 5.26252 C1orf158 1.57145922132303e-08 0.0329071789523662 0.967092805333042 chromosome 1 open reading frame 158 . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; . 0.11405 . 1.216305531 93.13517339 342.83347 3.92599 C1orf159 0.0908776364218918 0.765691410287669 0.143430953290439 chromosome 1 open reading frame 159 . . . unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;colon;skeletal muscle;breast;prostate;lung;endometrium;bone;testis;kidney;brain; superior cervical ganglion;trigeminal ganglion; 0.09477 . -0.227663163 37.11370606 56.85253 1.51792 C1orf162 0.00613131644818344 0.7370224716268 0.256846211925016 chromosome 1 open reading frame 162 . . . unclassifiable (Anatomical System);smooth muscle;heart;ovary;umbilical cord;cartilage;urinary;blood;skin;skeletal muscle;uterus;breast;lung;nasopharynx;germinal center;kidney;brain; . 0.03929 . 0.03689118 56.64071715 1193.93521 6.55539 C1orf167 0.155526802173754 0.635964349081526 0.20850884874472 chromosome 1 open reading frame 167 . . . unclassifiable (Anatomical System);prostate;lung;ovary;larynx;placenta;visual apparatus;testis;choroid;germinal center;brain; . 0.07693 . . . 5049.90069 14.53736 C1orf168 2.35652055532321e-30 8.32173965124508e-07 0.999999167826035 chromosome 1 open reading frame 168 . . . unclassifiable (Anatomical System);ovary;colon;parathyroid;retina;whole body;lung;endometrium;placenta;thyroid;liver;testis;head and neck;spleen;kidney; whole brain;dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skin; 0.05027 0.07240 0.824892996 88.06912008 1128.84019 6.41114 C1orf174 0.0187425021060312 0.897770945446998 0.0834865524469707 chromosome 1 open reading frame 174 . . . unclassifiable (Anatomical System);cartilage;heart;colon;skin;skeletal muscle;breast;uterus;pancreas;prostate;lung;cerebral cortex;nasopharynx;bone;placenta;visual apparatus;liver;testis;amniotic fluid;cervix;kidney;brain;stomach; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.16575 0.09230 1.063778722 91.58410002 230.70238 3.28387 C1orf185 . . . chromosome 1 open reading frame 185 . . . . . 0.12567 . 0.567831482 81.78225997 53.83478 1.46284 C1orf186 0.00189512675148331 0.726903727079523 0.271201146168994 chromosome 1 open reading frame 186 . . . . . 0.13912 . 0.25917371 70.05779665 170.0644 2.84602 C1orf189 0.000114764896185549 0.37727760518785 0.622607629915965 chromosome 1 open reading frame 189 . . . . . 0.00618 . -0.119252484 44.53880632 36.19648 1.08482 C1orf194 2.50029511352176e-07 0.0852781996792727 0.914721550291216 chromosome 1 open reading frame 194 . . . . . . . 0.99218692 90.51663128 437.63377 4.36169 C1orf195 . . . chromosome 1 open reading frame 195 . . . . . 0.06682 . . . 350.06101 3.96621 C1orf196 . . . chromosome 1 open reading frame 196 . . . . . . . . . . . C1orf198 0.0273752757183558 0.921047694063834 0.0515770302178103 chromosome 1 open reading frame 198 . . . . . 0.23574 . 0.194852702 67.03231894 31.69042 0.99734 C1orf204 0.0933681491982905 0.571806623629601 0.334825227172108 chromosome 1 open reading frame 204 . . . . . . 0.09395 . . 109.77177 2.27653 C1orf210 0.00121963583096512 0.402120303126583 0.596660061042452 chromosome 1 open reading frame 210 FUNCTION: May be involved in membrane trafficking between endosomes and plasma membrane.; . . . . 0.19448 . 0.547599505 81.2160887 101.5176 2.18193 C1orf216 0.128378757752275 0.780195606272369 0.0914256359753558 chromosome 1 open reading frame 216 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;thyroid;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland; . 0.14662 0.09333 0.505321956 80.00707714 43.33044 1.25072 C1orf220 . . . chromosome 1 open reading frame 220 . . . unclassifiable (Anatomical System);lung;islets of Langerhans;testis;blood; . . . . . . . C1orf226 0.723357168775303 0.263397511792677 0.01324531943202 chromosome 1 open reading frame 226 . . . . . . . -0.185391282 39.67916962 7.36353 0.27428 C1orf228 . . . chromosome 1 open reading frame 228 . . . unclassifiable (Anatomical System);ovary;heart;salivary gland;intestine;pharynx;colon;blood;skin;bone marrow;uterus;prostate;lung;endometrium;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland;bladder;thymus; . . . 0.591694063 82.45458835 50.27056 1.39342 C1orf229 0.520799629104626 0.414966348336524 0.0642340225588501 chromosome 1 open reading frame 229 . . . . . . . . . 956.26342 5.98566 C1orf233 . . . chromosome 1 open reading frame 233 . . . . . . . . . 9.806 0.35931 C1orf234 . . . chromosome 1 open reading frame 234 . . . . . . . . . . . C1QA 0.0497899792321254 0.859076867698721 0.0911331530691537 complement component 1, q subcomponent, A chain FUNCTION: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.; DISEASE: Complement component C1q deficiency (C1QD) [MIM:613652]: A disorder caused by impaired activation of the complement classical pathway. It generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;colon;parathyroid;choroid;skin;uterus;prostate;oesophagus;thyroid;bone;pituitary gland;brain;unclassifiable (Anatomical System);lymph node;heart;pancreas;lung;placenta;visual apparatus;liver;alveolus;spleen;kidney;aorta; placenta; 0.18608 . -0.139478553 43.29440906 8.46561 0.31014 C1QB 0.0858810485832231 0.760911037333916 0.153207914082861 complement component 1, q subcomponent, B chain FUNCTION: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.; DISEASE: Complement component C1q deficiency (C1QD) [MIM:613652]: A disorder caused by impaired activation of the complement classical pathway. It generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis. {ECO:0000269|PubMed:9476130}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;iris;testis;brain;pineal gland;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;oral cavity;adrenal cortex;lens;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus; . 0.16519 . -0.049474214 50.01179523 22.63593 0.75740 C1QBP 0.0720502387914283 0.872307670075572 0.055642091133 complement component 1, q subcomponent binding protein FUNCTION: Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular "heads" of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. Stabilizes mitochondrial CDKN2A isoform smARF. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. In infection processes acts as an attachment site for microbial proteins, including Listeria monocytogenes internalin B and Staphylococcus aureus protein A. May play a role in antibacterial defense as it can bind to cell surface hyaluronan and inhibit Streptococcus pneumoniae hyaluronate lyase. Involved in replication of Rubella virus. May be involved in modulation of the immune response; ligation by HCV core protein is resulting in suppresion of interleukin-12 production in monocyte-derived dendritic cells. Involved in regulation of antiviral response by inhibiting DDX58- and IFIH1- mediated signaling pathways probably involving its association with MAVS after viral infection. Involved in HIV-1 replication, presumably by contributing to splicing of viral RNA. {ECO:0000269|PubMed:10022843, ECO:0000269|PubMed:10479529, ECO:0000269|PubMed:10722602, ECO:0000269|PubMed:10747014, ECO:0000269|PubMed:11086025, ECO:0000269|PubMed:11859136, ECO:0000269|PubMed:12833064, ECO:0000269|PubMed:15243141, ECO:0000269|PubMed:16140380, ECO:0000269|PubMed:16177118, ECO:0000269|PubMed:17881511, ECO:0000269|PubMed:18676636, ECO:0000269|PubMed:19004836, ECO:0000269|PubMed:19164550, ECO:0000269|PubMed:20810993, ECO:0000269|PubMed:21536856, ECO:0000269|PubMed:21544310, ECO:0000269|PubMed:22700724, ECO:0000269|PubMed:8662673, ECO:0000269|PubMed:8710908, ECO:0000269|PubMed:9461517}.; . TISSUE SPECIFICITY: Expressed on cell surface of peripheral blood cells (at protein level); Surface expression is reported for macrophages and monocyte-derived dendritic cells. {ECO:0000269|PubMed:12574814, ECO:0000269|PubMed:8662673}.; lymphoreticular;medulla oblongata;ovary;umbilical cord;skin;bone marrow;prostate;ganglion;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;placenta;hippocampus;head and neck;kidney;stomach; whole brain;amygdala;lung;tumor; 0.75031 0.95702 -0.029247611 51.40363293 75.58069 1.81982 C1QBPP1 . . . complement component 1, q subcomponent binding protein, pseudogene 1 . . . . . . . . . . . C1QBPP2 . . . complement component 1, q subcomponent binding protein, pseudogene 2 . . . . . . . . . . . C1QBPP3 . . . complement component 1, q subcomponent binding protein, pseudogene 3 . . . . . . . . . . . C1QC 0.0173819025149602 0.716867304369013 0.265750793116027 complement component 1, q subcomponent, C chain FUNCTION: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.; DISEASE: Complement component C1q deficiency (C1QD) [MIM:613652]: A disorder caused by impaired activation of the complement classical pathway. It generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis. {ECO:0000269|PubMed:8630118}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.18335 0.19575 -0.582225231 18.44184949 26.35597 0.85444 C1QL1 . . . complement component 1, q subcomponent-like 1 FUNCTION: May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brainstem.; unclassifiable (Anatomical System);ovary;islets of Langerhans;hypothalamus;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;endometrium;bone;macula lutea;hippocampus;testis;kidney;brain; superior cervical ganglion;medulla oblongata;pons;parietal lobe;skeletal muscle; 0.21429 0.12151 . . 13.77957 0.50052 C1QL1P1 . . . complement component 1, q subcomponent-like 1 pseudogene 1 . . . . . . . . . . . C1QL2 0.396068457162213 0.563378421618778 0.0405531212190085 complement component 1, q subcomponent-like 2 FUNCTION: May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);optic nerve;lung;hypothalamus;macula lutea;iris;testis;fovea centralis;retina; amygdala;subthalamic nucleus;occipital lobe;atrioventricular node;parietal lobe; 0.14411 0.11788 . . 24.91921 0.81836 C1QL3 0.718803251749119 0.267338416905846 0.0138583313450343 complement component 1, q subcomponent-like 3 FUNCTION: May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses (By similarity). Plays a role in glucose homeostasis. Via AMPK signaling pathway, stimulates glucose uptake in adipocytes, myotubes and hepatocytes and enhances insulin-stimulated glucose uptake. In a hepatoma cell line, reduces the expression of gluconeogenic enzymes G6PC and PCK1 and hence decreases de novo glucose production (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in adipose tissue, with expression levels at least 2 orders of magnitude higher than in other tissues, including brain and kidney. {ECO:0000269|PubMed:21378161}.; hypothalamus;kidney; . 0.58092 0.12378 . . 0.76147 0.01334 C1QL4 0.621177258193781 0.346645125859063 0.0321776159471553 complement component 1, q subcomponent-like 4 FUNCTION: May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses (By similarity). May inhibit adipocyte differentiation at an early stage of the process (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highest expression levels in testis and adipose tissue, lower levels in skeletal muscle and kidney. {ECO:0000269|PubMed:23449976}.; stomach; . 0.26643 0.12244 . . 52.36135 1.43061 C1QTNF1 7.24017785005128e-05 0.504506996516215 0.495420601705285 C1q and tumor necrosis factor related protein 1 . . . smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;brain;artery;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;heart;muscle;urinary;adrenal cortex;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve;cerebellum; dorsal root ganglion;superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.34557 0.12013 -0.358119787 29.16371786 33.51466 1.03494 C1QTNF1-AS1 . . . C1QTNF1 antisense RNA 1 . . . . . . . . . 3.27382 0.11863 C1QTNF2 0.00135853504128362 0.656884060181133 0.341757404777584 C1q and tumor necrosis factor related protein 2 . . . . . 0.16500 0.14447 -0.53631094 20.53550366 92.10344 2.06427 C1QTNF3 0.000296343818969862 0.798997178258103 0.200706477922927 C1q and tumor necrosis factor related protein 3 . . TISSUE SPECIFICITY: Expressed in colon and small intestine. {ECO:0000269|PubMed:14654242}.; ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;liver;alveolus;spleen;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;testis - interstitial;superior cervical ganglion;globus pallidus;atrioventricular node;pons;trigeminal ganglion;cerebellum; . 0.31390 -0.073340031 48.11866006 29.89715 0.95425 C1QTNF3-AMACR . . . C1QTNF3-AMACR readthrough (NMD candidate) . . . . . . . . . . . C1QTNF4 0.679081390678169 0.300867004891373 0.0200516044304578 C1q and tumor necrosis factor related protein 4 FUNCTION: May act as a pro-inflammatory cytokine, that induces the activation of NF-kappa-B signaling pathway and up-regulates IL6 production. {ECO:0000269|PubMed:21658842}.; . TISSUE SPECIFICITY: Widely expressed at low levels. {ECO:0000269|PubMed:21658842}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;hypothalamus;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;whole body;frontal lobe;placenta;macula lutea;pituitary gland;testis;kidney;brain; . 0.09375 . . . 145.12074 2.62387 C1QTNF5 0.830646789327775 0.165834575430807 0.00351863524141773 C1q and tumor necrosis factor related protein 5 . DISEASE: Late-onset retinal degeneration (LORD) [MIM:605670]: Autosomal dominant disorder characterized by onset in the fifth to sixth decade with night blindness and punctate yellow-white deposits in the retinal fundus, progressing to severe central and peripheral degeneration, with choroidal neovascularization and chorioretinal atrophy. {ECO:0000269|PubMed:12944416, ECO:0000269|PubMed:22892318}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.10641 . . . 17.68431 0.61873 C1QTNF6 0.0237893847295441 0.772830028328865 0.203380586941591 C1q and tumor necrosis factor related protein 6 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;skin;uterus;pancreas;lung;bone;placenta;visual apparatus;liver;spleen;cervix;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.16098 0.10962 1.063778722 91.58410002 6403.98275 16.72231 C1QTNF7 0.0199101310745169 0.742152128936129 0.237937739989354 C1q and tumor necrosis factor related protein 7 . . . unclassifiable (Anatomical System);heart;ovary;cartilage;parathyroid;skin;skeletal muscle;uterus;lung;frontal lobe;placenta;bone;visual apparatus;testis;kidney;aorta; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.49950 0.12076 -0.558357437 19.54470394 63.69295 1.63637 C1QTNF8 8.97840847891757e-11 0.00588479143906207 0.994115208471154 C1q and tumor necrosis factor related protein 8 . . TISSUE SPECIFICITY: Expressed predominantly in lung and testis. {ECO:0000269|PubMed:19666007}.; . . 0.16306 0.11777 . . 344.88121 3.93972 C1QTNF9 0.169231075575943 0.816854909168689 0.0139140152553682 C1q and tumor necrosis factor related protein 9 FUNCTION: Probable adipokine. Activates AMPK, AKT, and p44/42 MAPK signaling pathways (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed predominantly in adipose tissue. {ECO:0000269|PubMed:19666007}.; unclassifiable (Anatomical System);prostate;pancreas;lung;placenta;hypopharynx;testis;spleen;head and neck;bone marrow; . 0.04496 0.08803 0.240763792 69.36777542 2754.34715 9.89643 C1QTNF9-AS1 . . . C1QTNF9 antisense RNA 1 . . . . . . . . . . . C1QTNF9B 0.0400104739852192 0.929413889204741 0.0305756368100397 C1q and tumor necrosis factor related protein 9B . . TISSUE SPECIFICITY: Expressed at low levels. Not expressed in adipose tissues. {ECO:0000269|PubMed:19666007}.; . . . . 0.597144447 82.7435716 3643.33377 11.72069 C1QTNF9B-AS1 . . . C1QTNF9B antisense RNA 1 FUNCTION: May be involved in growth and survival of prostate cancer cells through the TAF-Ibeta pathway.; . TISSUE SPECIFICITY: Expressed in prostate and testis. Weakly or not expressed in other tissues. Overexpressed in prostate cancers. {ECO:0000269|PubMed:15930275}.; . . . . . . . . C1R . . . complement C1r subcomponent FUNCTION: C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system.; . . ovary;sympathetic chain;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;cerebral cortex;endometrium;oesophagus;larynx;bone;thyroid;testis;spinal ganglion;brain;artery;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;skeletal muscle;pancreas;lung;cornea;nasopharynx;trabecular meshwork;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve; adipose tissue;ovary;liver;atrioventricular node;trigeminal ganglion; . . . . 1727.97053 7.67058 C1RL 0.000277416754917204 0.787029954865609 0.212692628379474 complement C1r subcomponent like FUNCTION: Mediates the proteolytic cleavage of HP/haptoglobin in the endoplasmic reticulum. {ECO:0000269|PubMed:15358180, ECO:0000269|PubMed:15385675, ECO:0000269|PubMed:15527420}.; . TISSUE SPECIFICITY: Highly expressed in placenta, liver, kidney, pancreas, moderately in lung, spleen, prostate, ovary, colon, and PBL, and weakly in heart, skeletal muscle, thymus, testis, and small intestine. Expressed in PC-3 (prostate adenocarcinoma) and SK-OV-3 (ovary adenocarcinoma) cells, but not in LoVo and HT-29 (colon adenocarcinoma), SMMC7721 (hepatocellular carcinoma), CaoV- 3 (ovary adenocarcinoma), HeLa (cervix epithelioid carcinoma), MCF-7 (breast adenocarcinoma), U-251MG (glioma) or A-549 (lung carcinoma) cells. Widely expressed in myeloid leukemia cell lines, including K-562 (chronic myelogenous leukemia), THP-1 (myelomonocytic leukemia), HL-60 and NB4 (promyelocytic leukemia), and KG-1 (acute myelogenous leukemia) cells. Expressed mainly in the liver and in serum (at protein level). {ECO:0000269|PubMed:15358180, ECO:0000269|PubMed:15527420}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;bone;thyroid;iris;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland; liver; 0.08590 0.10398 -0.200157416 39.11299835 3698.60974 11.84794 C1RL-AS1 . . . C1RL antisense RNA 1 . . . . . . . . . . . C1S 0.863410048494588 0.136586473296936 3.47820847608405e-06 complement component 1, s subcomponent FUNCTION: C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4.; DISEASE: Complement component C1s deficiency (C1SD) [MIM:613783]: A rare defect resulting in C1 deficiency and impaired activation of the complement classical pathway. C1 deficiency generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis. {ECO:0000269|PubMed:11390518}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;amniotic fluid;bladder;brain;gall bladder;amygdala;heart;cartilage;tongue;urinary;blood;skeletal muscle;breast;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;choroid;uterus;oesophagus;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;adipose tissue;olfactory bulb;ovary;liver;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.18965 0.44275 -0.044015879 50.44821892 1211.71237 6.58867 C2 1.37888637170214e-06 0.997835307780925 0.00216331333270286 complement component 2 FUNCTION: Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor C4b to generate the C3 or C5 convertase.; DISEASE: Complement component 2 deficiency (C2D) [MIM:217000]: A rare defect of the complement classical pathway associated with the development of autoimmune disorders, mainly systemic lupus erythematosus. Skin and joint manifestations are common and renal disease is relatively rare. Patients with complement component 2 deficiency are also reported to have recurrent invasive infections. {ECO:0000269|PubMed:8621452, ECO:0000269|PubMed:9670930}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;endometrium;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; . 0.21942 0.13298 -0.066061882 48.77919321 204.24581 3.08646 C2-AS1 . . . C2 antisense RNA 1 . . . . . . . . . . . C2CD2 0.0600282483313238 0.939254399122531 0.000717352546144941 C2 calcium-dependent domain containing 2 . . . ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;lens;skeletal muscle;bile duct;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;stomach; adrenal gland;adrenal cortex; 0.08398 0.09255 -0.949752638 9.32413305 151.19965 2.68855 C2CD2L 0.998151740074915 0.00184825035424867 9.57083584953528e-09 C2CD2 like . . . unclassifiable (Anatomical System);smooth muscle;heart;ovary;islets of Langerhans;colon;parathyroid;blood;fovea centralis;skin;skeletal muscle;retina;bone marrow;uterus;breast;optic nerve;lung;placenta;macula lutea;visual apparatus;pituitary gland;testis;kidney;brain;mammary gland; amygdala;superior cervical ganglion;prefrontal cortex;cingulate cortex;cerebellum; 0.49382 0.12603 -0.310388054 32.14791224 1150.72396 6.46295 C2CD3 8.07884267817138e-10 0.99999955110387 4.48088245863576e-07 C2 calcium-dependent domain containing 3 FUNCTION: Component of the centrioles that acts as a positive regulator of centriole elongation (PubMed:24997988). Promotes assembly of centriolar distal appendage, a structure at the distal end of the mother centriole that acts as an anchor of the cilium, and is required for recruitment of centriolar distal appendages proteins CEP83, SCLT1, CEP89, FBF1 and CEP164. Not required for centriolar satellite integrity or RAB8 activation. Required for primary cilium formation (PubMed:23769972). Required for sonic hedgehog/SHH signaling and for proteolytic processing of GLI3. {ECO:0000269|PubMed:23769972, ECO:0000269|PubMed:24997988}.; DISEASE: Orofaciodigital syndrome 14 (OFD14) [MIM:615948]: A form of orofaciodigital syndrome, a group of heterogeneous disorders characterized by malformations of the oral cavity, face and digits, and associated phenotypic abnormalities that lead to the delineation of various subtypes. OFD14 patients show severe microcephaly, cerebral malformations the molar tooth sign, and intellectual disability in addition to canonical OFDS features. {ECO:0000269|PubMed:24997988}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;breast;lung;epididymis;placenta;macula lutea;visual apparatus;alveolus;liver;head and neck;spleen;kidney;stomach; subthalamic nucleus;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.37109 . 2.177297739 98.07737674 7679.56022 18.83084 C2CD4A 0.0888058026911242 0.763816870097905 0.14737732721097 C2 calcium-dependent domain containing 4A FUNCTION: May be involved in inflammatory process. May regulate cell architecture and adhesion. {ECO:0000269|PubMed:15527968}.; . TISSUE SPECIFICITY: Specifically expressed in endothelial cells. {ECO:0000269|PubMed:15527968}.; unclassifiable (Anatomical System);uterus;prostate;lung;islets of Langerhans;colon;stomach; . 0.10343 0.10324 . . 189.88579 2.99036 C2CD4B 0.496545386662587 0.428904030849193 0.0745505824882194 C2 calcium-dependent domain containing 4B FUNCTION: May be involved in inflammatory process. May regulate cell architecture and adhesion. {ECO:0000269|PubMed:15527968}.; . TISSUE SPECIFICITY: Specifically expressed in endothelial cells. {ECO:0000269|PubMed:15527968}.; . . 0.11645 0.10125 . . 1735.99911 7.68880 C2CD4C . . . C2 calcium-dependent domain containing 4C . . . unclassifiable (Anatomical System); superior cervical ganglion;kidney; 0.23271 0.10673 . . 102.44599 2.18744 C2CD4D . . . C2 calcium-dependent domain containing 4D . . . . . . . . . 139.06253 2.56937 C2CD5 8.69478577467222e-07 0.999826561091829 0.000172569429593274 C2 calcium-dependent domain containing 5 FUNCTION: Required for insulin-stimulated glucose transport and glucose transporter SLC2A4/GLUT4 translocation from intracellular glucose storage vesicle (GSV) to the plasma membrane (PM) in adipocytes. Binds phospholipid membranes in a calcium-dependent manner and is necessary for the optimal membrane fusion between SLC2A4/GLUT4 GSV and the PM. {ECO:0000269|PubMed:21907143}.; . . . . 0.61743 0.10262 -0.734731259 14.01863647 63.10137 1.62505 C2orf15 0.543252452898348 0.442446467781108 0.0143010793205438 chromosome 2 open reading frame 15 . . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;pharynx;blood;breast;bile duct;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;spleen;kidney;mammary gland;stomach; globus pallidus;trigeminal ganglion;skeletal muscle; . . 0.279402865 70.86577023 . . C2orf16 3.91661992667067e-17 0.13302930086407 0.86697069913593 chromosome 2 open reading frame 16 . . . . . . . 1.308035764 94.00212314 3171.06724 10.73577 C2orf27A 0.419684826011534 0.464849074828954 0.115466099159513 chromosome 2 open reading frame 27A . . . unclassifiable (Anatomical System);uterus;lung;whole body;heart;placenta;testis;brain;skin; . . . . . . . C2orf27AP1 . . . chromosome 2 open reading frame 27A pseudogene 1 . . . . . . . . . . . C2orf27AP2 . . . chromosome 2 open reading frame 27A pseudogene 2 . . . . . . . . . . . C2orf27AP3 . . . chromosome 2 open reading frame 27A pseudogene 3 . . . . . . . . . . . C2orf27B 0.0140708907504597 0.441044705315388 0.544884403934152 chromosome 2 open reading frame 27B . . . pancreas;spleen;brain; . . . . . 2.38802 0.08136 C2orf40 0.00167864098073389 0.701902187286627 0.296419171732639 chromosome 2 open reading frame 40 FUNCTION: Probable hormone that may induce senescence of oligodendrocyte and neural precursor cells, characterized by G1 arrest, RB1 dephosphorylation and accelerated CCND1 and CCND3 proteasomal degradation. {ECO:0000250, ECO:0000269|PubMed:17284679}.; . . unclassifiable (Anatomical System);meninges;cartilage;colon;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;prostate;optic nerve;pia mater;whole body;lung;trabecular meshwork;macula lutea;hippocampus;iris;testis;dura mater;kidney;brain;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;trachea;thyroid;testis;trigeminal ganglion;pituitary;cerebellum; 0.16064 0.11278 0.769889969 86.95447039 208.65902 3.11685 C2orf42 0.134381994203355 0.86470674882148 0.000911256975164694 chromosome 2 open reading frame 42 . . . unclassifiable (Anatomical System);medulla oblongata;islets of Langerhans;sympathetic chain;colon;fovea centralis;choroid;lens;retina;breast;uterus;prostate;optic nerve;lung;endometrium;nasopharynx;bone;placenta;macula lutea;liver;testis;spleen;germinal center;kidney;brain;stomach; medulla oblongata;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node; 0.21649 . 0.242582624 69.45623968 624.80288 5.04289 C2orf44 0.0014413481942125 0.871936700264016 0.126621951541771 chromosome 2 open reading frame 44 . . . fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach;aorta; atrioventricular node;trigeminal ganglion; 0.24289 0.08413 0.178263593 66.12998349 479.70439 4.51972 C2orf47 0.00977968048221656 0.941903489593375 0.0483168299244085 chromosome 2 open reading frame 47 . . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;skeletal muscle;breast;lung;placenta;visual apparatus;duodenum;liver;spleen;cervix;kidney;stomach;thymus; atrioventricular node;trigeminal ganglion; 0.02846 0.04936 -0.117432389 44.89266336 40.51649 1.18838 C2orf48 0.0318183705555399 0.815490996960621 0.152690632483839 chromosome 2 open reading frame 48 . . . . . 0.06660 . 0.193034296 66.82000472 118.8787 2.37210 C2orf49 0.192673532038566 0.759520857518089 0.0478056104433452 chromosome 2 open reading frame 49 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;bile duct;breast;lung;cornea;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; trigeminal ganglion; 0.32760 0.10665 0.571462851 81.99457419 345.4313 3.94192 C2orf50 0.00360224822906377 0.626022056547759 0.370375695223177 chromosome 2 open reading frame 50 . . . . . 0.20084 . 0.903992902 89.39018636 1596.37834 7.39265 C2orf54 6.76852841899048e-06 0.280295194479402 0.719698036992179 chromosome 2 open reading frame 54 . . . lung;kidney;mammary gland;skin;stomach; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.10670 . 0.801024817 87.65628686 677.29799 5.20031 C2orf57 0.00229596523789253 0.528842112155084 0.468861922607024 chromosome 2 open reading frame 57 . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; . 0.07179 . 1.021500656 91.01792876 673.66452 5.18416 C2orf61 0.0141003474837281 0.869645075672893 0.116254576843379 chromosome 2 open reading frame 61 . . . testis; . 0.19857 . 1.194256079 92.88747346 690.87952 5.24169 C2orf66 0.00454708436823975 0.440112703760241 0.555340211871519 chromosome 2 open reading frame 66 . . . lung;testis;colon;retina; . 0.08178 . 0.147123112 64.11299835 5.60464 0.20948 C2orf68 0.0124864992399887 0.854782899941174 0.132730600818837 chromosome 2 open reading frame 68 . . . unclassifiable (Anatomical System);lymph node;ovary;muscle;uterus;breast;prostate;lung;frontal lobe;synovium;hypopharynx;testis;head and neck;kidney; uterus;superior cervical ganglion;appendix;white blood cells;atrioventricular node;fetal thyroid; . . 0.503505267 79.88912479 109.71072 2.27578 C2orf69 0.432171539151161 0.536120760886525 0.0317076999623146 chromosome 2 open reading frame 69 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;skin;skeletal muscle;retina;uterus;prostate;lung;endometrium;placenta;hippocampus;pituitary gland;testis;germinal center;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;atrioventricular node;trigeminal ganglion;cingulate cortex; . . 0.391453969 75.87284737 773.05911 5.50252 C2orf69P1 . . . chromosome 2 open reading frame 69 pseudogene 1 . . . . . . . . . . . C2orf69P2 . . . chromosome 2 open reading frame 69 pseudogene 2 . . . . . . . . . . . C2orf69P3 . . . chromosome 2 open reading frame 69 pseudogene 3 . . . . . . . . . . . C2orf69P4 . . . chromosome 2 open reading frame 69 pseudogene 4 . . . . . . . . . . . C2orf69P5 . . . chromosome 2 open reading frame 69 pseudogene 5 . . . . . . . . . . . C2orf70 0.000944694394683253 0.577795106175619 0.421260199429698 chromosome 2 open reading frame 70 . . . unclassifiable (Anatomical System);lung;testis;colon; skeletal muscle; . . 0.106667882 61.73036093 821.76633 5.62727 C2orf71 5.64897460026644e-10 0.380694281684784 0.619305717750319 chromosome 2 open reading frame 71 FUNCTION: May play an important role in the development of normal vision. {ECO:0000269|PubMed:20398886}.; . TISSUE SPECIFICITY: Specifically expressed in retina. {ECO:0000269|PubMed:20398884}.; prostate;optic nerve;macula lutea;visual apparatus;fovea centralis;choroid;lens;retina; . . . 1.622275522 96.01910828 7852.61767 19.12927 C2orf72 . . . chromosome 2 open reading frame 72 . . . . . . . . . 1348.36629 6.89156 C2orf73 0.000860167631538041 0.557463099486385 0.441676732882077 chromosome 2 open reading frame 73 . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis;kidney; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; . . 0.617373774 83.25076669 1022.80392 6.14997 C2orf74 . . . chromosome 2 open reading frame 74 . . . . . . . . . 2685.12932 9.74516 C2orf76 0.00333205633699219 0.609126325636586 0.387541618026422 chromosome 2 open reading frame 76 . . . unclassifiable (Anatomical System);uterus;lung;heart;liver;testis;germinal center;skin; . . 0.05220 0.657836546 84.27105449 35.71966 1.07429 C2orf78 6.9191452153743e-05 0.909074012808167 0.0908567957396797 chromosome 2 open reading frame 78 . . . . . . . -0.086288664 47.11606511 42.05249 1.22474 C2orf80 7.49151434788534e-05 0.749551553993258 0.250373530863263 chromosome 2 open reading frame 80 . . . unclassifiable (Anatomical System);brain; . . . 0.77170517 87.00754895 101.21881 2.17753 C2orf81 . . . chromosome 2 open reading frame 81 . . . unclassifiable (Anatomical System);prostate;lung;heart;endometrium;testis;kidney;germinal center;retina;thymus; testis - interstitial;superior cervical ganglion;testis;ciliary ganglion;trigeminal ganglion; . . . . 145.36454 2.62550 C2orf82 0.466831048732835 0.444370473402558 0.0887984778646075 chromosome 2 open reading frame 82 . . . unclassifiable (Anatomical System);bone;hippocampus;liver;colon;blood;kidney;brain;stomach;retina; . . . . . . . C2orf83 0.0501106068636758 0.689080499778688 0.260808893357636 chromosome 2 open reading frame 83 . . . placenta; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; . . 0.924227736 89.61429582 3701.49462 11.86155 C2orf88 0.023588526845881 0.543938732937736 0.432472740216384 chromosome 2 open reading frame 88 FUNCTION: Binds to type I regulatory subunits of protein kinase A (PKA-RI) and may anchor/target them to the plasma membrane. {ECO:0000269|PubMed:23115245}.; . TISSUE SPECIFICITY: Expressed in heart (at protein level). {ECO:0000269|PubMed:23115245}.; unclassifiable (Anatomical System);lung;placenta;testis;spleen;kidney;germinal center;skeletal muscle; testis - interstitial;testis - seminiferous tubule;testis; . . 0.323496558 72.93583392 584.1061 4.89989 C2orf91 . . . chromosome 2 open reading frame 91 . . . . . . . . . 1561.5661 7.32016 C3 0.999590151258431 0.000409848741569154 2.80284292086751e-17 complement component 3 FUNCTION: C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates.; FUNCTION: C3-beta-c: Acts as a chemoattractant for neutrophils in chronic inflammation. {ECO:0000250}.; DISEASE: Complement component 3 deficiency (C3D) [MIM:613779]: A rare defect of the complement classical pathway. Patients develop recurrent, severe, pyogenic infections because of ineffective opsonization of pathogens. Some patients may also develop autoimmune disorders, such as arthralgia and vasculitic rashes, lupus-like syndrome and membranoproliferative glomerulonephritis. {ECO:0000269|PubMed:7961791}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Macular degeneration, age-related, 9 (ARMD9) [MIM:611378]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. {ECO:0000269|PubMed:17634448, ECO:0000269|PubMed:24036952}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Hemolytic uremic syndrome atypical 5 (AHUS5) [MIM:612925]: An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. {ECO:0000269|PubMed:18796626, ECO:0000269|PubMed:20513133}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype.; DISEASE: Note=Increased levels of C3 and its cleavage product ASP, are associated with obesity, diabetes and coronary heart disease. Short-term endurance training reduces baseline ASP levels and subsequently fat storage.; TISSUE SPECIFICITY: Plasma. The acylation stimulating protein (ASP) is expressed in adipocytes and released into the plasma during both the fasting and postprandial periods. {ECO:0000269|PubMed:15833747, ECO:0000269|PubMed:9555951}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;lens;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; fetal liver;superior cervical ganglion;ovary;adrenal gland;liver;appendix;ciliary ganglion;fetal lung;atrioventricular node;trigeminal ganglion;skeletal muscle; . . -1.688698506 2.618542109 457.09361 4.43999 C3AR1 4.69335718249232e-05 0.417567355969427 0.582385710458748 complement component 3a receptor 1 FUNCTION: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production.; . TISSUE SPECIFICITY: Widely expressed in several differentiated hematopoietic cell lines, in the lung, spleen, ovary, placenta, small intestine, throughout the brain, heart, and endothelial cells. Mostly expressed in lymphoid tissues.; smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;bone;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;islets of Langerhans;blood;lens;skeletal muscle;lung;pia mater;nasopharynx;trabecular meshwork;placenta;macula lutea;liver;spleen;cervix;kidney;stomach; superior cervical ganglion; 0.02898 0.09952 -0.290161348 33.33923095 49.68131 1.38120 C3CER1 . . . chromosome 3 common eliminated region 1 FUNCTION: Cytokine that may play a role in anterior neural induction and somite formation during embryogenesis in part through a BMP-inhibitory mechanism. Can regulate Nodal signaling during gastrulation as well as the formation and patterning of the primitive streak (By similarity). {ECO:0000250}.; . . . . 0.33165 0.15720 0.15257911 64.60839821 . . C3orf14 1.59540116585515e-06 0.129304203166981 0.870694201431853 chromosome 3 open reading frame 14 . . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;uterus;prostate;endometrium;testis;bladder;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;lung;cornea;nasopharynx;placenta;visual apparatus;liver;alveolus;kidney;mammary gland;stomach; amygdala;whole brain;occipital lobe;medulla oblongata;temporal lobe;pons;caudate nucleus;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;cingulate cortex;parietal lobe; 0.11231 . 0.679884223 84.81363529 161.176 2.77350 C3orf17 9.41502116744778e-05 0.937049176957123 0.0628566728312021 chromosome 3 open reading frame 17 FUNCTION: May play a role in cortex development as part of the Notch signaling pathway. Downstream of Notch may repress the expression of proneural genes and inhibit neuronal differentiation thereby maintaining neural progenitors. May also play a role in preimplentation embryo development. {ECO:0000250|UniProtKB:Q8R2U2}.; . . medulla oblongata;ovary;colon;vein;skin;retina;bone marrow;uterus;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;hippocampus;liver;head and neck;kidney;mammary gland;stomach; . 0.06662 0.07077 0.734883636 86.29983487 2436.23519 9.16943 C3orf18 0.0143080084934581 0.678422996918357 0.307268994588185 chromosome 3 open reading frame 18 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;cerebellum cortex;islets of Langerhans;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;cerebellum peduncles;hypothalamus;caudate nucleus; 0.34058 0.10289 0.080983847 59.76055674 12.48354 0.45417 C3orf20 2.35749782524757e-14 0.114023006039164 0.885976993960813 chromosome 3 open reading frame 20 . . . . . 0.23531 . 1.120636874 92.10309035 8484.24533 19.88128 C3orf22 0.127310951022659 0.780168273531036 0.0925207754463047 chromosome 3 open reading frame 22 . . . medulla oblongata;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.01084 . -0.229483771 36.86010852 13.7421 0.49902 C3orf30 1.64784502765984e-06 0.415511995425453 0.584486356729519 chromosome 3 open reading frame 30 . . . medulla oblongata;testis; . 0.04106 . 3.199316096 99.33946686 2760.18176 9.91164 C3orf33 1.52110426864005e-07 0.120631634103638 0.879368213785936 chromosome 3 open reading frame 33 FUNCTION: Isoform 2: Secreted protein may play a role in transcription regulation via the MAPK3/MAPK1 pathway through an unidentified receptor on the plasma membrane.; . TISSUE SPECIFICITY: Highly expressed in ileocecal tissue and endometrium. {ECO:0000269|PubMed:20680465}.; whole body;frontal lobe;ovary;endometrium;testis;cervix;skeletal muscle; globus pallidus;trigeminal ganglion;skin; 0.11513 . 0.549415813 81.38122199 977.06855 6.04063 C3orf35 0.014135320099321 0.675954956431767 0.309909723468912 chromosome 3 open reading frame 35 . . TISSUE SPECIFICITY: Isoform 1 is expressed at high levels in the pancreas and placenta. Isoform 2 is expressed at high levels in the kidney. {ECO:0000269|PubMed:12543795}.; optic nerve;endometrium;macula lutea;fovea centralis;choroid;lens;retina; . 0.07247 0.06740 0.994001092 90.5579146 124.78994 2.42921 C3orf36 0.00367253659454535 0.399651664292044 0.59667579911341 chromosome 3 open reading frame 36 . . . . . . . 0.926041233 89.65557915 82.17422 1.92335 C3orf38 0.00699878324708333 0.919362896104515 0.0736383206484017 chromosome 3 open reading frame 38 FUNCTION: May be involved in apoptosis regulation. {ECO:0000269|PubMed:17464193}.; . . lymphoreticular;medulla oblongata;ovary;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;lens;bile duct;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;atrioventricular node;skeletal muscle; 0.05291 0.08633 -0.203796826 38.81811748 60.85578 1.58585 C3orf49 . . . chromosome 3 open reading frame 49 . . . unclassifiable (Anatomical System);uterus;lung;whole body;placenta;testis; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.11088 . . . 1468.35326 7.14177 C3orf52 1.27244581516247e-08 0.0151921388754055 0.984807848400136 chromosome 3 open reading frame 52 . . . unclassifiable (Anatomical System);lymph node;ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;germinal center;brain;bladder;stomach; superior cervical ganglion;skeletal muscle; 0.04698 0.06314 1.24016994 93.34748762 52.8122 1.44050 C3orf56 2.51567990011522e-07 0.0452040623381165 0.954795686093893 chromosome 3 open reading frame 56 . . . . . 0.08986 . . . 22.57141 0.75502 C3orf58 0.162503916327723 0.82249821090875 0.0149978727635268 chromosome 3 open reading frame 58 FUNCTION: May play a role in cardiomyocyte proliferation through paracrine signaling and activation of the PPI3K-AKT-CDK7 signaling cascade. {ECO:0000269|PubMed:23784961}.; DISEASE: Note=Genetic variations in C3orf58 may be associated with susceptibility to autism (PubMed:18621663). {ECO:0000269|PubMed:18621663}.; . ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);heart;cerebellum cortex;pharynx;blood;breast;lung;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;aorta;stomach; atrioventricular node; 0.61024 0.11809 -0.139478553 43.29440906 37.74447 1.12319 C3orf62 0.00712465933483595 0.765681169815254 0.227194170849909 chromosome 3 open reading frame 62 . . . unclassifiable (Anatomical System);uterus;medulla oblongata;heart;cerebral cortex;placenta;liver;testis;colon;spleen;skin;peripheral nerve; . 0.07587 . 0.881944684 89.02453409 512.80781 4.63568 C3orf67 1.50533862917062e-05 0.991672113467694 0.00831283314601457 chromosome 3 open reading frame 67 . . . unclassifiable (Anatomical System);lung;cerebral cortex;bone;testis;germinal center;brain; . 0.37849 . 0.490549924 79.54706299 672.44389 5.18123 C3orf67-AS1 . . . C3orf67 antisense RNA 1 . . . . . . . . . . . C3orf70 0.00239094751008584 0.537470696790996 0.460138355698918 chromosome 3 open reading frame 70 . . . kidney; superior cervical ganglion;ciliary ganglion;skeletal muscle; . . 0.637604436 83.77565464 534.2634 4.71386 C3orf79 0.260312468461099 0.638998972497632 0.100688559041269 chromosome 3 open reading frame 79 . . . . . . . 0.545784012 81.11582921 202.41314 3.07022 C3orf80 . . . chromosome 3 open reading frame 80 . . . pancreas;lung;ovary;endometrium;hypothalamus;placenta;parathyroid;kidney;brain; . . . . . 79.86559 1.88822 C3orf84 0.000221291799515334 0.505397796386295 0.494380911814189 chromosome 3 open reading frame 84 . . . . . . . . . 22.32724 0.74974 C3P1 . . . complement component 3 precursor pseudogene . . . . . . . . . . . C4A . . . complement component 4A (Rodgers blood group) FUNCTION: Non-enzymatic component of C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. C4A isotype is responsible for effective binding to form amide bonds with immune aggregates or protein antigens, while C4B isotype catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens.; DISEASE: Complement component 4A deficiency (C4AD) [MIM:614380]: A rare defect of the complement classical pathway associated with the development of autoimmune disorders, mainly systemic lupus with or without associated glomerulonephritis. {ECO:0000269|PubMed:8473511}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:10092831, ECO:0000269|PubMed:17503323}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Interindividual copy-number variation (CNV) of complement component C4 and associated polymorphisms result in different susceptibilities to SLE. The risk of SLE susceptibility has been shown to be significantly increased among subjects with only two copies of total C4. A high copy number is a protective factor against SLE.; TISSUE SPECIFICITY: Complement component C4 is expressed at highest levels in the liver, at moderate levels in the adrenal cortex, adrenal medulla, thyroid gland,and the kidney, and at lowest levels in the heart, ovary, small intestine, thymus, pancreas and spleen. The extra-hepatic sites of expression may be important for the local protection and inflammatory response. {ECO:0000269|PubMed:11367523}.; . . 0.18507 . . . 46.75554 1.32179 C4A-AS1 . . . C4A antisense RNA 1 . . . . . . . . . . . C4B . . . complement component 4B (Chido blood group) FUNCTION: Non-enzymatic component of the C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. C4A isotype is responsible for effective binding to form amide bonds with immune aggregates or protein antigens, while C4B isotype catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens.; DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:10092831, ECO:0000269|PubMed:17503323}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Interindividual copy-number variation (CNV) of complement component C4 and associated polymorphisms result in different susceptibilities to SLE. The risk of SLE susceptibility has been shown to be significantly increased among subjects with only two copies of total C4. A high copy number is a protective factor against SLE.; DISEASE: Complement component 4B deficiency (C4BD) [MIM:614379]: A rare defect of the complement classical pathway associated with the development of autoimmune disorders, mainly systemic lupus with or without associated glomerulonephritis. {ECO:0000269|PubMed:3265961}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Complement component C4 is expressed at highest levels in the liver, at moderate levels in the adrenal cortex, adrenal medulla, thyroid gland,and the kidney, and at lowest levels in the heart, ovary, small intestine, thymus, pancreas and spleen. The extra-hepatic sites of expression may be important for the local protection and inflammatory response. {ECO:0000269|PubMed:11367523}.; . . 0.27695 . . . 23.02648 0.76798 C4B-AS1 . . . C4B antisense RNA 1 . . . . . . . . . . . C4BPA 0.0127393583379383 0.98574866006748 0.00151198159458153 complement component 4 binding protein alpha FUNCTION: Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It interacts also with anticoagulant protein S and with serum amyloid P component.; . TISSUE SPECIFICITY: Chylomicrons in the plasma.; . . 0.06468 0.15434 1.17583962 92.75182826 204.17258 3.08601 C4BPAP1 . . . complement component 4 binding protein, alpha pseudogene 1 . . . . . . . . . . . C4BPAP2 . . . complement component 4 binding protein, alpha pseudogene 2 . . . . . . . . . . . C4BPAP3 . . . complement component 4 binding protein, alpha pseudogene 3 . . . . . . . . . . . C4BPB 2.57853683497245e-06 0.301982214230291 0.698015207232874 complement component 4 binding protein beta FUNCTION: Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. It also interacts with anticoagulant protein S and with serum amyloid P component. The beta chain binds protein S.; . . unclassifiable (Anatomical System);pancreas;lung;placenta;liver;testis;colon;cervix;spleen; fetal liver;superior cervical ganglion;liver;atrioventricular node;trigeminal ganglion; 0.06896 0.13339 0.12689526 63.00424628 16.16102 0.57339 C4B_2 . . . complement component 4B (Chido blood group), copy 2 FUNCTION: Non-enzymatic component of the C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. C4A isotype is responsible for effective binding to form amide bonds with immune aggregates or protein antigens, while C4B isotype catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens.; DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:10092831, ECO:0000269|PubMed:17503323}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Interindividual copy-number variation (CNV) of complement component C4 and associated polymorphisms result in different susceptibilities to SLE. The risk of SLE susceptibility has been shown to be significantly increased among subjects with only two copies of total C4. A high copy number is a protective factor against SLE.; DISEASE: Complement component 4B deficiency (C4BD) [MIM:614379]: A rare defect of the complement classical pathway associated with the development of autoimmune disorders, mainly systemic lupus with or without associated glomerulonephritis. {ECO:0000269|PubMed:3265961}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Complement component C4 is expressed at highest levels in the liver, at moderate levels in the adrenal cortex, adrenal medulla, thyroid gland,and the kidney, and at lowest levels in the heart, ovary, small intestine, thymus, pancreas and spleen. The extra-hepatic sites of expression may be important for the local protection and inflammatory response. {ECO:0000269|PubMed:11367523}.; . . . . . . . . C4orf3 0.868030873638966 0.130138886036914 0.00183024032411982 chromosome 4 open reading frame 3 . . . . . . . 0.501689326 79.7888653 27.17826 0.87585 C4orf17 5.65209813902781e-09 0.0659282912160651 0.934071703131837 chromosome 4 open reading frame 17 . . . lung;testis; . 0.07641 0.06993 0.751474114 86.64779429 811.19615 5.60300 C4orf19 0.00416046038426668 0.657032813187533 0.3388067264282 chromosome 4 open reading frame 19 . . . unclassifiable (Anatomical System);ovary;colon;blood;parathyroid;skeletal muscle;pancreas;frontal lobe;endometrium;placenta;liver;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node; 0.12716 . 0.463046108 78.58575136 407.36232 4.23209 C4orf22 1.12464982894466e-05 0.360252430375004 0.639736323126707 chromosome 4 open reading frame 22 . . . unclassifiable (Anatomical System);lung;ovary;placenta;testis;parathyroid; superior cervical ganglion;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09517 . 0.527368849 80.73248408 98.861 2.14975 C4orf26 0.124857081122354 0.78003866005634 0.0951042588213062 chromosome 4 open reading frame 26 FUNCTION: Might promote nucleation of hydroxyapatite. {ECO:0000269|PubMed:22901946}.; . TISSUE SPECIFICITY: Highly expressed in placenta. {ECO:0000269|PubMed:22901946}.; ovary;placenta;parathyroid;kidney; . 0.20684 . 0.970138239 90.23354565 2086.38341 8.41692 C4orf27 0.000423306504309246 0.856930466529299 0.142646226966392 chromosome 4 open reading frame 27 . . . . . 0.07088 0.08138 0.483275131 79.25218212 58.84525 1.55651 C4orf32 0.285815911901643 0.629345351780707 0.0848387363176495 chromosome 4 open reading frame 32 . . . unclassifiable (Anatomical System);cartilage;heart;muscle;parathyroid;skin;retina;bile duct;uterus;pancreas;whole body;lung;endometrium;thyroid;placenta;visual apparatus;hippocampus;pituitary gland;liver;testis;germinal center;kidney;brain; . 0.09842 0.07841 . . 28.0983 0.90119 C4orf33 0.000824304469823587 0.782302680714315 0.216873014815862 chromosome 4 open reading frame 33 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;bone marrow;prostate;lung;endometrium;placenta;liver;testis;kidney;brain;gall bladder; . 0.13626 . 0.837848571 88.22835574 3197.41125 10.77807 C4orf36 0.00148486509394954 0.439615580875993 0.558899554030058 chromosome 4 open reading frame 36 . . . uterus;lung;heart;adrenal cortex;testis;skin; . 0.06763 . 1.058333711 91.42486435 1169.50966 6.50049 C4orf45 1.27822060379936e-05 0.218830261617999 0.781156956175963 chromosome 4 open reading frame 45 . . . . . . . 1.526824688 95.50011795 694.25547 5.25358 C4orf46 0.25900301841022 0.639415568155125 0.101581413434654 chromosome 4 open reading frame 46 . . TISSUE SPECIFICITY: Expressed in the kidney, in epithelial cells in both proximal tubules and distal convoluted tubules. {ECO:0000269|PubMed:25059753}.; . . . . 0.169169615 65.33380514 54.17613 1.46844 C4orf47 . . . chromosome 4 open reading frame 47 . . TISSUE SPECIFICITY: Detected in testis and fetal liver. {ECO:0000269|PubMed:15809229}.; . . . . 0.791937896 87.33781552 289.50351 3.63954 C4orf48 . . . chromosome 4 open reading frame 48 . . TISSUE SPECIFICITY: Brain-specific (at protein level). {ECO:0000269|PubMed:21287218}.; . . . . . . 13.36438 0.48634 C4orf50 6.34225080498418e-10 0.0354569954272051 0.96454300393857 chromosome 4 open reading frame 50 . . . frontal lobe;kidney;brain; . . . . . 3712.33587 11.89234 C4orf51 0.0151808801541665 0.958036056973885 0.0267830628719483 chromosome 4 open reading frame 51 . . . . . . . 0.637604436 83.77565464 465.07709 4.46723 C5 5.61068968015523e-11 0.999999829018884 1.70925009246444e-07 complement component 5 FUNCTION: Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled.; DISEASE: Complement component 5 deficiency (C5D) [MIM:609536]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=An association study of C5 haplotypes and genotypes in individuals with chronic hepatitis C virus infection shows that individuals homozygous for the C5_1 haplotype have a significantly higher stage of liver fibrosis than individuals carrying at least 1 other allele. {ECO:0000269|PubMed:15995705}.; . ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;optic nerve;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;hypothalamus;lens;skeletal muscle;lung;placenta;macula lutea;liver;cervix;spleen;kidney; superior cervical ganglion;fetal liver; 0.25448 0.15814 -0.051509809 49.39254541 5639.16587 15.54132 C5AR1 0.000416365501777882 0.642131978082623 0.357451656415599 complement component 5a receptor 1 FUNCTION: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a (PubMed:1847994, PubMed:8182049, PubMed:7622471, PubMed:9553099, PubMed:10636859, PubMed:15153520). The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events (PubMed:8182049, PubMed:7622471, PubMed:9553099). Receptor activation stimulates chemotaxis, granule enzyme release, intracellular calcium release and superoxide anion production (PubMed:10636859, PubMed:15153520). {ECO:0000269|PubMed:10636859, ECO:0000269|PubMed:15153520, ECO:0000269|PubMed:1847994, ECO:0000269|PubMed:7622471, ECO:0000269|PubMed:8182049, ECO:0000269|PubMed:9553099}.; . . unclassifiable (Anatomical System);cartilage;colon;blood;bone marrow;uterus;prostate;lung;frontal lobe;endometrium;epididymis;placenta;testis;kidney;brain;mammary gland;stomach; whole blood;bone marrow; 0.13565 0.46572 -0.598810865 18.13517339 26.00885 0.84526 C5AR2 0.0231409770825171 0.768272944250958 0.208586078666525 complement component 5a receptor 2 FUNCTION: Receptor for the chemotactic and inflammatory C3a, C4a and C5a anaphylatoxin peptides and also for their dearginated forms ASP/C3adesArg, C4adesArg and C5adesArg respectively. Couples weakly to G(i)-mediated signaling pathways. {ECO:0000269|PubMed:11773063, ECO:0000269|PubMed:15833747, ECO:0000269|PubMed:19615750}.; . TISSUE SPECIFICITY: Frontal cortex, hippocampus, hypothalamus, pons and liver. {ECO:0000269|PubMed:11090875, ECO:0000269|PubMed:11165367}.; . . 0.05201 0.15302 -0.334253673 30.70299599 88.19648 2.01172 C5orf15 0.0159999377606089 0.700779960522882 0.283220101716509 chromosome 5 open reading frame 15 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12752121}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; placenta;ciliary ganglion; 0.26296 0.08432 0.194852702 67.03231894 151.43482 2.69020 C5orf17 . . . chromosome 5 open reading frame 17 . . . . . . . . . 575.78992 4.86708 C5orf22 0.169565363421206 0.827536910815753 0.00289772576304168 chromosome 5 open reading frame 22 . . . lymphoreticular;ovary;colon;parathyroid;skin;bone marrow;prostate;frontal lobe;larynx;thyroid;bone;bladder;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;adrenal cortex;blood;bile duct;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;aorta;stomach; amygdala;subthalamic nucleus;superior cervical ganglion;parietal lobe; 0.14043 0.10007 0.729426781 86.17008728 429.0409 4.32607 C5orf24 0.640813736011774 0.33157283554946 0.0276134284387663 chromosome 5 open reading frame 24 . . . ovary;sympathetic chain;skin;retina;bone marrow;uterus;whole body;endometrium;thyroid;bone;testis;germinal center;spinal ganglion;brain;artery;unclassifiable (Anatomical System);small intestine;heart;lacrimal gland;islets of Langerhans;adrenal cortex;skeletal muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach;aorta; medulla oblongata;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.34193 . 0.058937498 58.26256192 19.20533 0.66119 C5orf28 1.49355055551377e-05 0.23749331813671 0.762491746357735 chromosome 5 open reading frame 28 . . . . . 0.63044 . -0.163345027 41.24793583 16.3891 0.58074 C5orf30 0.778880851929595 0.213941987005601 0.00717716106480392 chromosome 5 open reading frame 30 FUNCTION: Probably plays a role in trafficking of proteins via its interaction with UNC119 and UNC119B cargo adapters: may help the release of UNC119 and UNC119B cargo or the recycling of UNC119 and UNC119B (PubMed:22085962). May play a role in ciliary membrane localization via its interaction with UNC119B and protein transport into photoreceptor cells (PubMed:22085962). {ECO:0000269|PubMed:22085962}.; . TISSUE SPECIFICITY: High expression in normal macrophages, monocytes, and cultured rheumatoid arthritis synovial fibroblasts (RASFs), with lower expression in B and T cells, and little to no expression in other tissues and cell lines (PubMed:26316022). {ECO:0000269|PubMed:26316022}.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;gum;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; subthalamic nucleus; 0.32987 0.11262 -0.427900189 25.14744043 12.84566 0.46899 C5orf34 9.91326958657609e-11 0.279814884171683 0.720185115729184 chromosome 5 open reading frame 34 . . . unclassifiable (Anatomical System);ovary;urinary;pharynx;colon;parathyroid;skin;whole body;placenta;visual apparatus;liver;testis;germinal center;brain;mammary gland;stomach; . 0.20836 . -0.26629572 34.81953291 89.53523 2.03472 C5orf38 0.162071502267242 0.77380194925483 0.0641265484779287 chromosome 5 open reading frame 38 . . TISSUE SPECIFICITY: Isoform 1 is highly expressed in small intestine, testis and kidney, medium expressed in brain and heart and low expressed in colon; it could not be detected in liver, adrenal gland and pancreas. {ECO:0000269|PubMed:16515847}.; unclassifiable (Anatomical System); superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.04281 0.09563 -0.029247611 51.40363293 1738.75342 7.69663 C5orf42 6.320876617357e-19 0.994979973547798 0.00502002645220152 chromosome 5 open reading frame 42 . DISEASE: Joubert syndrome 17 (JBTS17) [MIM:614615]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. {ECO:0000269|PubMed:22425360, ECO:0000269|PubMed:23012439}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Orofaciodigital syndrome 6 (OFD6) [MIM:277170]: A form of orofaciodigital syndrome, a group of heterogeneous disorders characterized by malformations of the oral cavity, face and digits, and associated phenotypic abnormalities that lead to the delineation of various subtypes. OFD6 is characterized by metacarpal abnormalities with central polydactyly, cerebellar abnormalities including the molar tooth sign, tongue hamartomas, additional frenula, and upper lip notch. {ECO:0000269|PubMed:24178751}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;heart;ovary;parathyroid;blood;skin;skeletal muscle;breast;uterus;pancreas;lung;frontal lobe;endometrium;bone;thyroid;placenta;liver;testis;cervix;spleen;germinal center;kidney;stomach; superior cervical ganglion;prefrontal cortex;caudate nucleus;atrioventricular node;trigeminal ganglion; 0.10988 . -0.549573058 19.9398443 2506.02862 9.33009 C5orf45 3.28629116657157e-06 0.557021144516696 0.442975569192137 chromosome 5 open reading frame 45 . . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;gum;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;bile duct;lung;adrenal gland;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;kidney;mammary gland;stomach; . . . 1.107875794 92.03821656 94.77772 2.09797 C5orf46 0.29942489197858 0.623116997054355 0.077458110967066 chromosome 5 open reading frame 46 . . . uterus;ovary;heart;skin; testis - interstitial;salivary gland;testis;skin; . . 0.3032669 72.009908 5706.20734 15.63783 C5orf47 . . . chromosome 5 open reading frame 47 . . . lung;testis;skeletal muscle; . . . 0.389637587 75.75489502 241.68035 3.35637 C5orf49 0.346800140585866 0.596742332102529 0.0564575273116042 chromosome 5 open reading frame 49 . . . . . . . 0.815800671 87.8744987 2329.49343 8.94254 C5orf51 0.00388889950519938 0.957830833511929 0.038280266982872 chromosome 5 open reading frame 51 . . . . . . . 0.104848986 61.49445624 180.03222 2.91542 C5orf52 . . . chromosome 5 open reading frame 52 . . . . . . . 1.012423333 90.829205 2035.44724 8.31028 C5orf56 0.107649237505837 0.776115750029672 0.116235012464491 chromosome 5 open reading frame 56 . . . unclassifiable (Anatomical System);lymph node;brain;bone marrow; . . . . . 27.21312 0.87612 C5orf58 0.0389421300224031 0.643718873490481 0.317338996487116 chromosome 5 open reading frame 58 . . . . . . . 0.257356108 69.83368719 4.99363 0.18532 C5orf60 . . . chromosome 5 open reading frame 60 . . . . . . . 0.813985927 87.81552253 989.09912 6.06300 C5orf63 . . . chromosome 5 open reading frame 63 . . . unclassifiable (Anatomical System);parathyroid; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . 0.279402865 70.86577023 43.41951 1.25368 C5orf64 0.0411009097234592 0.65384037844404 0.305058711832501 chromosome 5 open reading frame 64 . . . . . . . 0.681699246 84.93158764 4623.74769 13.67562 C5orf66 . . . chromosome 5 open reading frame 66 . . . . . . . . . 37.27076 1.11113 C5orf66-AS1 . . . C5orf66 antisense RNA 1 . . . . . . . . . . . C5orf66-AS2 . . . C5orf66 antisense RNA 2 . . . . . . . . . . . C5orf67 . . . chromosome 5 open reading frame 67 . . . . . . . . . . . C6 1.2016606841251e-14 0.450685888215516 0.549314111784472 complement component 6 FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells.; DISEASE: Complement component 6 deficiency (C6D) [MIM:612446]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis. {ECO:0000269|PubMed:15565285}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);pancreas;lung;islets of Langerhans;liver;testis;spleen;kidney;gall bladder; dorsal root ganglion;fetal liver;superior cervical ganglion;liver;trigeminal ganglion; 0.06098 0.10515 1.319073185 94.07289455 846.02843 5.69020 C6orf1 0.29871864309512 0.623456865980363 0.0778244909245167 chromosome 6 open reading frame 1 . . TISSUE SPECIFICITY: Expressed in spleen, thymus, prostate, testis, uterus, small intestine, colon and peripheral blood leukocytes. {ECO:0000269|PubMed:10036196}.; smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;spinal cord;urinary;blood;lens;breast;pancreas;lung;placenta;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.12929 0.08012 0.082802743 60.09082331 101.78276 2.18303 C6orf10 1.22806574585252e-13 0.470531124965607 0.52946887503427 chromosome 6 open reading frame 10 . . . unclassifiable (Anatomical System);lung;testis; . 0.07590 0.07442 4.266124392 99.7287096 12835.27934 24.33992 C6orf15 0.00142769734419249 0.66757230214912 0.331000000506687 chromosome 6 open reading frame 15 . . TISSUE SPECIFICITY: Expressed in skin and tonsils. {ECO:0000269|PubMed:15217361}.; unclassifiable (Anatomical System); . 0.07034 . 1.752786166 96.68553904 1441.95482 7.08239 C6orf25 0.0040376920872826 0.858621408829335 0.137340899083382 chromosome 6 open reading frame 25 FUNCTION: Inhibits platelet aggregation and activation by agonists such as ADP and collagen-related peptide. Appears to operate in a calcium-independent manner. Isoform B is a putative inhibitory receptor. Isoform A may be its activating counterpart. {ECO:0000269|PubMed:17311996}.; . TISSUE SPECIFICITY: Expressed in a restricted set of hematopoietic cell lines including the erythroleukemia cell line K-562 and the T-cell leukemia cell lines MOLT-4 and Jurkat. Not detected in the monocyte-like cell line U-937, the B-cell-like cell line Raji, the fibroblast cell lines TK and HeLa, or the natural killer cell lines NKL, NK 62 and YT. Expressed in platelets. {ECO:0000269|PubMed:11544253, ECO:0000269|PubMed:17311996}.; . . 0.07225 0.06904 0.238945317 69.20853975 305.90417 3.72403 C6orf47 0.16984783307713 0.770769451640348 0.0593827152825224 chromosome 6 open reading frame 47 . . . . . 0.37464 . 0.994001092 90.5579146 1089.03988 6.31693 C6orf47-AS1 . . . C6orf47 antisense RNA 1 . . . . . . . . . . . C6orf48 5.82446544381436e-05 0.149216234737871 0.850725520607691 chromosome 6 open reading frame 48 . . . . . 0.04714 . 0.169169615 65.33380514 15.54921 0.55443 C6orf52 . . . chromosome 6 open reading frame 52 . . . unclassifiable (Anatomical System);lung;ovary;heart;testis; . . . 0.479642105 78.95140363 2821.14229 10.01735 C6orf58 1.61255593750847e-10 0.030543143861758 0.969456855976986 chromosome 6 open reading frame 58 FUNCTION: May be involved in early liver development. {ECO:0000250|UniProtKB:A5PF61, ECO:0000250|UniProtKB:Q4QRF7}.; . TISSUE SPECIFICITY: Detected in saliva and in hypomineralized dental enamel (at protein level). {ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20651090}.; lung;larynx;head and neck;stomach; superior cervical ganglion;trachea; 0.06000 . 0.106667882 61.73036093 108.44678 2.25969 C6orf62 0.946557424258141 0.0532591873479423 0.000183388393916244 chromosome 6 open reading frame 62 . . . . . 0.67792 0.11262 -0.163345027 41.24793583 11.66217 0.42297 C6orf89 8.22352243978553e-05 0.767740916459619 0.232176848315983 chromosome 6 open reading frame 89 FUNCTION: Exhibits histone deacetylase (HDAC) enhancer properties (PubMed:23460338). May play a role in cell cycle progression and wound repair of bronchial epithelial cells (PubMed:21857995). {ECO:0000269|PubMed:21857995, ECO:0000269|PubMed:23460338}.; . . medulla oblongata;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;amygdala;heart;cartilage;pharynx;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;kidney;aorta;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;parietal lobe;cerebellum; 0.32158 0.33876 0.130533008 63.35810333 65.32857 1.66364 C6orf99 . . . chromosome 6 open reading frame 99 . . . . . 0.09510 . . . 16.39499 0.58100 C6orf106 0.454029671085684 0.539890363430746 0.00607996548357033 chromosome 6 open reading frame 106 . . . . . 0.28834 . -0.295622497 32.61972163 9.79493 0.35835 C6orf118 1.45572025749264e-17 0.000413950193012371 0.999586049806988 chromosome 6 open reading frame 118 . . . unclassifiable (Anatomical System);uterus;lung;heart;testis;brain;skin;thymus; . 0.05882 . 0.935129812 89.86199575 1170.66372 6.50346 C6orf120 0.0463401176945872 0.675579981199699 0.278079901105714 chromosome 6 open reading frame 120 FUNCTION: May be involved in induction of apoptosis in CD4(+) T- cells, but not CD8(+) T-cells or hepatocytes. {ECO:0000269|PubMed:22340178}.; . TISSUE SPECIFICITY: Mainly expressed in hepatocytes and some weak expression in germinal center cells of lymph nodes. {ECO:0000269|PubMed:22340178}.; ovary;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;urinary;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;stomach;cerebellum; amygdala;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.30195 . 0.170987912 65.5579146 54.33196 1.47249 C6orf132 . . . chromosome 6 open reading frame 132 . . . prostate;lung;tongue;visual apparatus;colon;head and neck;stomach; dorsal root ganglion;superior cervical ganglion;pons;trigeminal ganglion; 0.20222 . . . 2239.84233 8.73355 C6orf136 0.87389420310306 0.125768304605672 0.00033749229126871 chromosome 6 open reading frame 136 . . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;germinal center;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; . 0.29622 . . . 268.61508 3.51506 C6orf141 . . . chromosome 6 open reading frame 141 . . . . . 0.73978 0.06449 0.924227736 89.61429582 547.78177 4.76012 C6orf163 . . . chromosome 6 open reading frame 163 . . . . . 0.00233 . 1.102432221 91.93205945 381.49169 4.11655 C6orf183 . . . chromosome 6 open reading frame 183 . . . . . . . . . . . C6orf201 0.0922482847224992 0.766851935604551 0.14089977967295 chromosome 6 open reading frame 201 . . . unclassifiable (Anatomical System);medulla oblongata;heart;hypothalamus;blood;skin;skeletal muscle;bile duct;uterus;prostate;adrenal gland;nasopharynx;hypopharynx;liver;testis;head and neck;cervix; . 0.10331 . 1.414757139 94.83958481 1518.5566 7.24416 C6orf203 0.00178692275457031 0.714876685009249 0.28333639223618 chromosome 6 open reading frame 203 . . . unclassifiable (Anatomical System);heart;ovary;parathyroid;lens;skin;uterus;prostate;lung;trabecular meshwork;placenta;liver;testis;spleen;kidney;brain;stomach;thymus; . 0.13118 0.08646 -0.161524709 41.6430762 38.78647 1.14799 C6orf222 1.39401452747336e-13 0.0468121371188994 0.953187862880961 chromosome 6 open reading frame 222 . . . . . 0.09589 . -0.148789446 42.29771172 3048.92392 10.49778 C6orf223 0.0204906742338502 0.747307931055855 0.232201394710294 chromosome 6 open reading frame 223 . . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;fovea centralis;choroid;lens;skin;retina;optic nerve;lung;cornea;macula lutea;visual apparatus;liver;cervix;kidney;brain;mammary gland;stomach; . 0.04575 . 1.550689283 95.62396792 872.70364 5.75071 C6orf226 0.494949271877891 0.429781104043163 0.0752696240789464 chromosome 6 open reading frame 226 . . . . . . . 0.393270925 76.04977589 101.0791 2.17606 C6orf229 . . . chromosome 6 open reading frame 229 . . . . . . . . . 723.27125 5.33852 C7 1.26145650921317e-11 0.50794029347847 0.492059706508915 complement component 7 FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C7 serves as a membrane anchor.; DISEASE: Complement component 7 deficiency (C7D) [MIM:610102]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis. {ECO:0000269|PubMed:8871666, ECO:0000269|PubMed:9218625, ECO:0000269|PubMed:9856499}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);smooth muscle;cartilage;ovary;heart;salivary gland;urinary;colon;skeletal muscle;retina;uterus;prostate;lung;cerebral cortex;adrenal gland;nasopharynx;thyroid;placenta;liver;testis;spleen;kidney;spinal ganglion;tonsil;stomach; uterus;pancreas;lymph node;ovary;adrenal gland;placenta;adrenal cortex;appendix;fetal lung;kidney; 0.47789 0.10803 -0.214928658 37.7388535 3835.00708 12.19075 C7orf25 0.352368932691872 0.63465793035509 0.0129731369530379 chromosome 7 open reading frame 25 . . . ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;cochlea;oesophagus;endometrium;bone;iris;testis;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach; . 0.13650 0.10234 -0.249709319 35.74545883 99.98462 2.16837 C7orf26 0.82656655995323 0.172642584747037 0.000790855299732906 chromosome 7 open reading frame 26 . . . lymphoreticular;smooth muscle;ovary;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;cervix;kidney;mammary gland;stomach;aorta; thyroid;trigeminal ganglion; 0.15371 0.10416 -0.336073593 30.55555556 176.14971 2.88770 C7orf31 7.44109236489478e-08 0.700891740600694 0.299108184988382 chromosome 7 open reading frame 31 . . . unclassifiable (Anatomical System);lung;bone;placenta;testis;blood;kidney;brain;retina;bone marrow; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.10185 . 1.315418981 94.0552017 6429.09835 16.80664 C7orf33 0.000634926247300206 0.493009770091875 0.506355303660824 chromosome 7 open reading frame 33 . . . . . 0.18666 . 0.681699246 84.93158764 125.57575 2.43933 C7orf34 0.000149478331950413 0.247304604429096 0.752545917238954 chromosome 7 open reading frame 34 . . . . . 0.08289 . 0.681699246 84.93158764 . . C7orf43 0.300413006639945 0.698742758369147 0.000844234990907515 chromosome 7 open reading frame 43 . . . unclassifiable (Anatomical System);lymphoreticular;cartilage;islets of Langerhans;colon;skin;retina;breast;pancreas;lung;frontal lobe;liver;testis;spleen;germinal center;brain;mammary gland;stomach; . 0.17356 0.10790 -0.53631094 20.53550366 39.8756 1.17381 C7orf49 0.335421676073075 0.603663482884814 0.0609148410421111 chromosome 7 open reading frame 49 FUNCTION: May act as a regulator of proteasome. {ECO:0000250}.; . . . . 0.05301 . -0.007201372 53.19061099 5.96498 0.22419 C7orf50 0.00139620778717545 0.662779097246935 0.335824694965889 chromosome 7 open reading frame 50 . . . myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;thymus; globus pallidus; 0.08973 0.09920 0.327131069 73.27199811 175.57039 2.88295 C7orf55 0.0170096837393943 0.712708133483188 0.270282182777418 chromosome 7 open reading frame 55 . . . unclassifiable (Anatomical System);uterus;bile duct;heart;skin;skeletal muscle; whole brain;testis - interstitial;heart;liver;testis; 0.01284 . 0.435547893 77.45340882 4033.74349 12.58706 C7orf55-LUC7L2 0.995965817862567 0.00403411786374737 6.42736857373367e-08 C7orf55-LUC7L2 readthrough . . . . . . . . . . . C7orf57 4.29144419573902e-05 0.632085409641691 0.367871675916351 chromosome 7 open reading frame 57 . . . endometrium; . 0.08167 0.07655 1.039913547 91.25973107 3913.77649 12.37095 C7orf60 0.99081083987417 0.00918678449231365 2.37563351647646e-06 chromosome 7 open reading frame 60 FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase. {ECO:0000255|HAMAP-Rule:MF_03044}.; . . unclassifiable (Anatomical System);myocardium;meninges;cartilage;heart;ovary;lacrimal gland;urinary;skin;uterus;prostate;pia mater;whole body;lung;bone;thyroid;alveolus;testis;spleen;dura mater;kidney;brain;stomach; . . . -0.295622497 32.61972163 5.42202 0.20087 C7orf61 0.0120812493963009 0.850457977602926 0.137460773000773 chromosome 7 open reading frame 61 . . . unclassifiable (Anatomical System);lung;cartilage;ovary;liver;testis;brain; . . . -0.161524709 41.6430762 12.52095 0.45639 C7orf62 0.0235072221293244 0.770872222575959 0.205620555294717 chromosome 7 open reading frame 62 . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node; . . 0.350995466 74.37485256 891.31004 5.81970 C7orf65 2.78279603971715e-06 0.0946490514656688 0.905348165738291 chromosome 7 open reading frame 65 . . . . . . . 0.547599505 81.2160887 95.02987 2.10193 C7orf66 0.00581436531098041 0.489253895008842 0.504931739680178 chromosome 7 open reading frame 66 . . . . . . . 0.657836546 84.27105449 34.56175 1.05499 C7orf69 0.051049199904848 0.692194703201275 0.256756096893877 chromosome 7 open reading frame 69 . . . . . . . 0.167351552 65.04482189 1.60631 0.05205 C7orf71 . . . chromosome 7 open reading frame 71 . . . . . . . 1.146531275 92.39797122 539.14473 4.73165 C7orf72 . . . chromosome 7 open reading frame 72 . . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;lung;cornea;visual apparatus;liver;testis;kidney;brain;mammary gland; . . . 1.170393003 92.68105685 2390.96845 9.07689 C7orf73 . . . chromosome 7 open reading frame 73 . . . . . . . 0.189398298 66.31870724 19.00658 0.65653 C7orf76 . . . chromosome 7 open reading frame 76 . . . . . . . 0.790124109 87.30242982 10.2338 0.37308 C7orf77 . . . chromosome 7 open reading frame 77 . . . . . . . . . . . C8A 5.355640730752e-11 0.202923357853565 0.797076642092878 complement component 8 alpha subunit FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C8A inserts into the target membrane, but does not form pores by itself. {ECO:0000269|PubMed:17872444, ECO:0000269|PubMed:7440581}.; DISEASE: Complement component 8 deficiency, 1 (C8D1) [MIM:613790]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;lung;liver;spleen;kidney;brain;bladder;gall bladder; superior cervical ganglion;fetal liver;liver;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10455 0.10694 1.581840753 95.7891012 2893.50809 10.18787 C8B 1.49406934497858e-09 0.577357222432194 0.422642776073737 complement component 8, beta polypeptide FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells.; DISEASE: Complement component 8 deficiency, 2 (C8D2) [MIM:613789]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . . . 0.05295 0.12134 0.558509856 81.67020524 596.12337 4.94126 C8G 1.63182991085726e-09 0.032163822002696 0.967836176365474 complement component 8, gamma polypeptide FUNCTION: C8 is a constituent of the membrane attack complex. C8 binds to the C5B-7 complex, forming the C5B-8 complex. C5-B8 binds C9 and acts as a catalyst in the polymerization of C9. The gamma subunit seems to be able to bind retinol.; . . lung;liver;testis;colon;kidney;gall bladder;stomach; superior cervical ganglion;liver;trigeminal ganglion;skeletal muscle; 0.04668 . 0.196671391 67.19155461 801.2629 5.57646 C8orf4 0.0652714996147049 0.729623346169074 0.205105154216222 chromosome 8 open reading frame 4 FUNCTION: Seems to be involved in the regulation of cell growth an differentiation, may play different and opposite roles depending on the tissue or cell type. May enhance the WNT-CTNNB1 pathway by relieving antagonistic activity of CBY1 (PubMed:16424001, PubMed:16730711). Enhances the proliferation of follicular dendritic cells (PubMed:16730711). Plays a role in the mitogen- activated MAPK2/3 signaling pathway, positively regulates G1-to-S- phase transition of the cell cycle (PubMed:18959821). In endothelial cells, enhances key inflammatory mediators and inflammatory response through the modulation of NF-kappaB transcriptional regulatory activity (PubMed:19684084). Involved in the regulation of heat shock response, seems to play a positive feedback with HSF1 to modulate heat-shock downstream gene expression (PubMed:17603013). Plays a role in the regulation of hematopoiesis even if the mechanisms are unknown (By similarity). In cancers such as thyroid or lung cancer, it has been described as promoter of cell proliferation, G1-to-S-phase transition and inhibitor of apoptosis (PubMed:15087392, PubMed:24941347). However, it negatively regulates self-renewal of liver cancer cells via suppresion of NOTCH2 signaling (PubMed:25985737). {ECO:0000250|UniProtKB:Q9D915, ECO:0000269|PubMed:15087392, ECO:0000269|PubMed:16424001, ECO:0000269|PubMed:16730711, ECO:0000269|PubMed:17603013, ECO:0000269|PubMed:18959821, ECO:0000269|PubMed:19684084, ECO:0000269|PubMed:24941347, ECO:0000269|PubMed:25985737, ECO:0000305}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in thyroid papillary carcinoma. Expressed in liver, expression levels decrease in hepatocellular carcinoma (PubMed:25985737). Slightly detected in normal lung, its expression is highly induced in lung cancer cells (at protein level) (PubMed:24941347). {ECO:0000269|PubMed:11056052, ECO:0000269|PubMed:24941347, ECO:0000269|PubMed:25985737}.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;bone;thyroid;testis;brain;bladder;pineal gland;gall bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;skeletal muscle;pancreas;lung;adrenal gland;placenta;liver;spleen;head and neck;cervix;kidney;stomach; appendix;ciliary ganglion;atrioventricular node; 0.27727 0.36088 0.080983847 59.76055674 7.42202 0.27570 C8orf17 . . . chromosome 8 open reading frame 17 FUNCTION: May be involved in cell survival, proliferation and progression of cancer cells. {ECO:0000269|PubMed:12665628}.; . TISSUE SPECIFICITY: Expressed in the heart, kidney, liver, pancreas, small intestine, ovary, testis, prostate and thymus. Expressed in all of the cancer cell lines tested. {ECO:0000269|PubMed:12665628}.; . . 0.01837 . . . 34.76483 1.05924 C8orf22 0.375401958677392 0.577983970441892 0.0466140708807151 chromosome 8 open reading frame 22 . . . lung;muscle;liver;skeletal muscle; . 0.07891 . 0.413500896 76.67492333 12.29383 0.44506 C8orf31 1.08582352031841e-05 0.200653878094473 0.799335263670324 chromosome 8 open reading frame 31 . . . . . 0.13743 . 0.613741468 83.06794055 10.36165 0.37744 C8orf33 6.35413220057411e-05 0.477453799033436 0.522482659644558 chromosome 8 open reading frame 33 . . . ovary;salivary gland;intestine;colon;choroid;skin;retina;uterus;prostate;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;bile duct;breast;lung;cornea;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; occipital lobe;thalamus;adrenal gland;cerebellum peduncles;temporal lobe;pons;trigeminal ganglion;parietal lobe;cerebellum; 0.12130 0.08621 0.395088462 76.15003539 66.19948 1.67603 C8orf34 9.85328956909529e-06 0.934637284649424 0.0653528620610073 chromosome 8 open reading frame 34 . . . vestibule;unclassifiable (Anatomical System);optic nerve;frontal lobe;hypothalamus;macula lutea;fovea centralis;choroid;lens;brain;stomach;retina; whole brain;occipital lobe;skeletal muscle; 0.26234 . -0.314027422 31.9297004 1665.9654 7.53631 C8orf34-AS1 . . . C8orf34 antisense RNA 1 . . . . . . . . . . . C8orf37 0.0021844296064522 0.755143291271852 0.242672279121696 chromosome 8 open reading frame 37 . DISEASE: Retinitis pigmentosa 64 (RP64) [MIM:614500]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:22177090}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, with highest levels in heart and brain. Also expressed in the retina (at protein level). {ECO:0000269|PubMed:22177090}.; unclassifiable (Anatomical System);lung;ovary;placenta;testis;parathyroid;brain;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13411 . 0.193034296 66.82000472 126.62587 2.45220 C8orf37-AS1 . . . C8orf37 antisense RNA 1 . . . . . . . . . . . C8orf44 0.0169402857224386 0.71191898262284 0.271140731654721 chromosome 8 open reading frame 44 . . . . . 0.13167 . 0.613741468 83.06794055 471.74199 4.49590 C8orf44-SGK3 0.136791140818748 0.863029963974725 0.000178895206526427 C8orf44-SGK3 readthrough FUNCTION: Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cell growth, proliferation, survival and migration. Up-regulates Na(+) channels: SCNN1A/ENAC and SCN5A, K(+) channels: KCNA3/KV1.3, KCNE1, KCNQ1 and KCNH2/HERG, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channel: BSND, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, amino acid transporters: SLC1A5/ASCT2 and SLC6A19, glutamate transporters: SLC1A3/EAAT1, SLC1A6/EAAT4 and SLC1A7/EAAT5, glutamate receptors: GRIA1/GLUR1 and GRIK2/GLUR6, Na(+)/H(+) exchanger: SLC9A3/NHE3, and the Na(+)/K(+) ATPase. Plays a role in the regulation of renal tubular phosphate transport and bone density. Phosphorylates NEDD4L and GSK3B. Positively regulates ER transcription activity through phosphorylation of FLII. Negatively regulates the function of ITCH/AIP4 via its phosphorylation and thereby prevents CXCR4 from being efficiently sorted to lysosomes. {ECO:0000269|PubMed:12054501, ECO:0000269|PubMed:12397388, ECO:0000269|PubMed:12590200, ECO:0000269|PubMed:12632189, ECO:0000269|PubMed:12634932, ECO:0000269|PubMed:12650886, ECO:0000269|PubMed:12911626, ECO:0000269|PubMed:14706641, ECO:0000269|PubMed:15040001, ECO:0000269|PubMed:15044175, ECO:0000269|PubMed:15319523, ECO:0000269|PubMed:15496163, ECO:0000269|PubMed:15737648, ECO:0000269|PubMed:15845389, ECO:0000269|PubMed:16036218, ECO:0000269|PubMed:16888620, ECO:0000269|PubMed:17167223, ECO:0000269|PubMed:18005662, ECO:0000269|PubMed:19293151, ECO:0000269|PubMed:20511718, ECO:0000269|PubMed:21865597}.; . TISSUE SPECIFICITY: Expressed in most tissues with highest levels in pancreas, kidney liver, heart and brain and lower levels in lung, placenta and skeletal muscle. Expression is higher in ER- positive breast tumors than ER-negative breast tumors. {ECO:0000269|PubMed:21084382}.; . . . . . . 17.46689 0.61310 C8orf46 0.639231507537227 0.35418374781656 0.00658474464621256 chromosome 8 open reading frame 46 . . . unclassifiable (Anatomical System);amygdala;heart;hypothalamus;skin;retina;bone marrow;uterus;prostate;lung;frontal lobe;bone;hippocampus;liver;spleen;kidney;brain; . 0.62560 . -0.207437529 38.2814343 57.11604 1.52233 C8orf48 . . . chromosome 8 open reading frame 48 . . . unclassifiable (Anatomical System);lung;whole body;heart;larynx;bone;thyroid;liver;testis;head and neck;kidney; . 0.04924 . 1.991751729 97.64685067 130.50415 2.48906 C8orf49 . . . chromosome 8 open reading frame 49 . . . . . . . . . 878.64131 5.77330 C8orf58 7.25833522609638e-07 0.279282221821131 0.720717052345347 chromosome 8 open reading frame 58 . . . unclassifiable (Anatomical System);medulla oblongata;ovary;hypothalamus;parathyroid;blood;retina;uterus;prostate;lung;frontal lobe;endometrium;larynx;bone;placenta;hypopharynx;liver;testis;cervix;head and neck;spleen;kidney;brain; . 0.11805 . 0.775339069 87.13729653 146.34089 2.63608 C8orf59 0.0427259485219979 0.660989938278895 0.296284113199107 chromosome 8 open reading frame 59 . . . unclassifiable (Anatomical System); . . . 0.279402865 70.86577023 18.09798 0.63155 C8orf59P1 . . . chromosome 8 open reading frame 59 pseudogene 1 . . . . . . . . . . . C8orf59P2 . . . chromosome 8 open reading frame 59 pseudogene 2 . . . . . . . . . . . C8orf74 1.01040579381024e-11 0.00313238422312976 0.996867615766766 chromosome 8 open reading frame 74 . . . testis; testis; 0.08287 . 0.308721233 72.59966973 628.96948 5.05354 C8orf76 1.71944218858493e-05 0.675085867899803 0.324896937678311 chromosome 8 open reading frame 76 . . . colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;tongue;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;spleen;cervix;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.28162 . -0.448125345 24.19202642 37.97178 1.12779 C8orf82 0.00666763298298849 0.517578880171678 0.475753486845333 chromosome 8 open reading frame 82 . . . ovary;colon;choroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;optic nerve;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;blood;lens;lung;placenta;macula lutea;liver;cervix;kidney;stomach; . . . . . . . C8orf86 6.34747718357808e-05 0.477239375649264 0.5226971495789 chromosome 8 open reading frame 86 . . . . . . . 0.505321956 80.00707714 497.3274 4.58241 C8orf87 . . . chromosome 8 open reading frame 87 . . . . . . . . . 1370.94756 6.94617 C8orf88 . . . chromosome 8 open reading frame 88 . . . . . . . . . 8.66487 0.31850 C8orf89 . . . chromosome 8 open reading frame 89 . . . . . . . . . . . C9 6.82499306595342e-17 0.00381623571070802 0.996183764289292 complement component 9 FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC.; DISEASE: Complement component 9 deficiency (C9D) [MIM:613825]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections predominantly by Neisseria gonorrhoeae or Neisseria meningitidis. Some patients may develop dermatomyositis. {ECO:0000269|PubMed:9634479}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Macular degeneration, age-related, 15 (ARMD15) [MIM:615591]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. {ECO:0000269|PubMed:24036952}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma.; placenta;liver; superior cervical ganglion;liver;atrioventricular node;trigeminal ganglion; 0.14000 0.12151 1.445891753 95.12267044 304.83542 3.71776 C9orf3 5.19688494998789e-12 0.191615179906347 0.808384820088456 chromosome 9 open reading frame 3 FUNCTION: Aminopeptidases catalyze the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. Able to cleave angiotensin III to generate angiotensin IV, a bioactive peptide of the renin-angiotensin pathway. Not able to cleave angiotensin I and angiotensin II. May play a role in the proteolytic processing of bioactive peptides in tissues such as testis and heart. {ECO:0000269|PubMed:15687497}.; . TISSUE SPECIFICITY: Predominantly expressed in pancreas, placenta, liver, testis and heart. Expressed at lower level in brain, lung and kidney. {ECO:0000269|PubMed:15687497}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;bladder;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.15497 0.18663 -0.108334733 45.57088936 741.30574 5.40662 C9orf9 0.212814053223936 0.747340403500775 0.0398455432752882 chromosome 9 open reading frame 9 . . . unclassifiable (Anatomical System);medulla oblongata;ovary;islets of Langerhans;uterus;pancreas;prostate;whole body;lung;placenta;thyroid;hippocampus;testis;cervix;germinal center;mammary gland; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;pons;trigeminal ganglion;skeletal muscle; 0.13662 0.10088 -0.427900189 25.14744043 44.28169 1.26972 C9orf16 0.0164936296194712 0.471952482304679 0.51155388807585 chromosome 9 open reading frame 16 . . . . . . . 0.145304857 63.81221986 49.95369 1.38669 C9orf24 1.68680241907127e-05 0.670965180928708 0.329017951047101 chromosome 9 open reading frame 24 FUNCTION: May play a role in spermatogenesis (By similarity). May be involved in differentiation or function of ciliated cells. {ECO:0000250, ECO:0000269|PubMed:15242845}.; . TISSUE SPECIFICITY: Expressed in epithelial cells of nasal polyps and in intact epithelium of bronchial biopsies from subjects with and without asthma. Strong expression in columnar cells with little or no expression in basal epithelial cells along the basement membrane. Strongly expressed in ciliated epithelial cells with lower levels in goblet cells (at protein level). {ECO:0000269|PubMed:15242845}.; unclassifiable (Anatomical System);uterus;lung;whole body;cartilage;heart;islets of Langerhans;testis;brain;skin; . 0.16076 0.09309 0.016664174 55.21939137 25.18503 0.82319 C9orf40 0.263986200149246 0.637786510358871 0.0982272894918833 chromosome 9 open reading frame 40 . . . . . 0.26857 . . . 15.93662 0.56504 C9orf41-AS1 . . . C9orf41 antisense RNA 1 . . . . . . . . . . . C9orf43 2.99765253312802e-08 0.742791193130479 0.257208776892996 chromosome 9 open reading frame 43 . . . unclassifiable (Anatomical System);lung;whole body;testis;cervix; trigeminal ganglion; 0.02568 . 1.442251694 95.08138712 1224.26495 6.61304 C9orf47 0.0850920101967428 0.76007253443653 0.154835455366727 chromosome 9 open reading frame 47 . . . unclassifiable (Anatomical System);prostate;optic nerve;islets of Langerhans;macula lutea;visual apparatus;blood;fovea centralis;choroid;lens;brain;retina; . 0.07426 . . . 70.56397 1.74783 C9orf50 7.27866245193078e-10 0.0729074223291746 0.927092576942959 chromosome 9 open reading frame 50 . . . . . 0.09607 . . . 886.63879 5.80108 C9orf57 . . . chromosome 9 open reading frame 57 . . . . . 0.06397 . 0.635788962 83.63411182 133.99852 2.51791 C9orf62 . . . chromosome 9 open reading frame 62 . . . brain; . 0.12158 . . . 9.25247 0.33886 C9orf64 0.00113820304494202 0.837670890329582 0.161190906625476 chromosome 9 open reading frame 64 . . . unclassifiable (Anatomical System);lymph node;cartilage;small intestine;islets of Langerhans;hypothalamus;skin;uterus;pancreas;whole body;lung;endometrium;placenta;liver;testis;cervix;germinal center;brain;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.12609 0.08733 0.729426781 86.17008728 298.81513 3.68703 C9orf66 0.000775174366698502 0.535088369565142 0.46413645606816 chromosome 9 open reading frame 66 . . . . . . . . . 4564.52887 13.55817 C9orf69 0.496755436370346 0.428788228765908 0.0744563348637459 chromosome 9 open reading frame 69 FUNCTION: Plays a role in cell proliferation by promoting progression into S phase. Promotes human herpesvirus 1 (HHV-1) proliferation. {ECO:0000269|PubMed:21667337}.; . . . . . . . . 20.40171 0.69571 C9orf72 0.000715131762650573 0.980414626813187 0.0188702414241624 chromosome 9 open reading frame 72 FUNCTION: May play a role in endosomal trafficking and autophagy. {ECO:0000269|PubMed:24549040}.; . TISSUE SPECIFICITY: Both isoforms are widely expressed, including kidney, lung, liver, heart, testis and several brain regions, such as cerebellum. Also expressed in the frontal cortex and in lymphoblasts (at protein level). {ECO:0000269|PubMed:21944778, ECO:0000269|PubMed:21944779}.; . . 0.27122 . -0.558357437 19.54470394 360.65146 4.01911 C9orf78 0.117679601576605 0.876685774648724 0.00563462377467143 chromosome 9 open reading frame 78 . . . . . 0.16424 0.11262 -0.141298762 42.87567823 13.49973 0.49056 C9orf84 4.96930426660693e-16 0.720308628182783 0.279691371817216 chromosome 9 open reading frame 84 . . . unclassifiable (Anatomical System);pancreas;lung;testis;blood;kidney;skeletal muscle;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14196 . 2.500707945 98.64944562 8068.81679 19.37216 C9orf85 0.00692105108649798 0.760277702713479 0.232801246200023 chromosome 9 open reading frame 85 . . . unclassifiable (Anatomical System);lung;endometrium;tongue;bone;visual apparatus;liver;testis;head and neck;kidney; superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node; 0.17432 0.08631 0.347360312 73.97381458 38.47218 1.14163 C9orf91 0.000442176335696461 0.863178165230138 0.136379658434166 chromosome 9 open reading frame 91 . . . colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;breast;lung;placenta;macula lutea;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;medulla oblongata;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.14566 . 0.240763792 69.36777542 70.0056 1.73622 C9orf92 . . . chromosome 9 open reading frame 92 . . . larynx;thyroid;head and neck;brain; . 0.51697 . . . 166.78446 2.82171 C9orf106 . . . chromosome 9 open reading frame 106 . . . prostate;pituitary gland; . . . . . . . C9orf114 0.104849793965415 0.893739876741256 0.00141032929332798 chromosome 9 open reading frame 114 FUNCTION: Required both for chromosome alignment and for association of the centrosomes with the poles of the bipolar spindle during metaphase. {ECO:0000269|PubMed:20813266}.; . . ovary;colon;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;adrenal cortex;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; skeletal muscle; 0.13909 . 0.308721233 72.59966973 3609.33844 11.63248 C9orf116 0.0100326018329181 0.604207600386382 0.3857597977807 chromosome 9 open reading frame 116 . . . . . 0.12643 . 0.080983847 59.76055674 21.24053 0.71792 C9orf118 . . . chromosome 9 open reading frame 118 . . . . . 0.00157 . . . . . C9orf129 0.375838563772169 0.577683920848242 0.0464775153795891 chromosome 9 open reading frame 129 . . . . . . . 0.659651797 84.35362114 2711.85714 9.80419 C9orf131 3.48248704048122e-13 0.0218573677878427 0.978142632211809 chromosome 9 open reading frame 131 . . . lymphoreticular;smooth muscle;rectum;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;spinal ganglion;brain;amygdala;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;oral cavity;muscle;blood;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.04535 . 0.608069891 82.94409059 734.51296 5.37588 C9orf135 1.84473133938082e-05 0.452428247655519 0.547553305031088 chromosome 9 open reading frame 135 . . . . . 0.07014 . -0.003562597 53.72729417 297.49506 3.67925 C9orf135-AS1 . . . C9orf135 antisense RNA 1 (head to head) . . . . . . . . . . . C9orf139 1.55539634643458e-06 0.0679784252774632 0.93202001932619 chromosome 9 open reading frame 139 . . . unclassifiable (Anatomical System);spleen;mammary gland; . 0.07421 . 0.617373774 83.25076669 204.76077 3.09098 C9orf142 0.569785721445569 0.418549018394421 0.0116652601600092 chromosome 9 open reading frame 142 FUNCTION: Involved in non-homologous end joining (NHEJ), a major pathway to repair double-strand breaks in DNA. May act as a scaffold required to stabilize the Ku heterodimer, composed of XRCC5/Ku80 and XRCC6/Ku70, at double-strand break sites and promote the assembly and/or stability of the NHEJ machinery. {ECO:0000269|PubMed:25574025, ECO:0000269|PubMed:25670504, ECO:0000269|PubMed:25941166}.; . . . . 0.10650 . 0.058937498 58.26256192 116.47925 2.34724 C9orf147 . . . chromosome 9 open reading frame 147 . . . . . . . . . . . C9orf152 0.00474768063508639 0.684998823379696 0.310253495985218 chromosome 9 open reading frame 152 . . . . . 0.06325 . -0.161524709 41.6430762 113.35629 2.31837 C9orf153 0.23330732490067 0.645785224156439 0.12090745094289 chromosome 9 open reading frame 153 . . . testis; . 0.06727 . 0.523736627 80.45529606 99.90176 2.16618 C9orf163 0.0550466033843523 0.704463942868828 0.24048945374682 chromosome 9 open reading frame 163 . . . lung;testis;kidney; . 0.06350 . 0.147123112 64.11299835 932.37329 5.92268 C9orf170 1.76428978941079e-06 0.0730562872051652 0.926941948505045 chromosome 9 open reading frame 170 . . . . . . . 0.237127192 68.98443029 10.88559 0.39419 C9orf172 . . . chromosome 9 open reading frame 172 . . . . . . . . . 67.12643 1.69469 C9orf173 3.9371530786687e-11 0.0133996133259798 0.986600386634649 chromosome 9 open reading frame 173 . . . . . . . 0.573279816 82.08303845 432.00191 4.33751 C9orf173-AS1 . . . C9orf173 antisense RNA 1 . . . . . . . . . . . C10orf2 0.990313030047165 0.00968694754252451 2.24103102087424e-08 chromosome 10 open reading frame 2 FUNCTION: Involved in mitochondrial DNA (mtDNA) metabolism. Could function as an adenine nucleotide-dependent DNA helicase. Function inferred to be critical for lifetime maintenance of mtDNA integrity. In vitro, forms in combination with POLG, a processive replication machinery, which can use double-stranded DNA (dsDNA) as template to synthesize single-stranded DNA (ssDNA) molecules. May be a key regulator of mtDNA copy number in mammals. {ECO:0000269|PubMed:15167897}.; DISEASE: Sensory ataxic neuropathy dysarthria and ophthalmoparesis (SANDO) [MIM:607459]: A systemic disorder resulting from mitochondrial dysfunction associated with mitochondrial depletion in skeletal muscle and peripheral nerve tissue. The clinical triad of symptoms consists of sensory ataxic neuropathy, dysarthria, and ophthalmoparesis. However, the phenotype varies widely, even within the same family, and can also include myopathy, seizures, and hearing loss. An atypical form of the disease is characterized by headaches and/or seizures manifesting in childhood or adolescence, followed by development of cerebellar and sensory ataxia, dysarthria, progressive external ophthalmoplegia, and myoclonus in early adulthood. {ECO:0000269|PubMed:15668446}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial DNA depletion syndrome 7 (MTDPS7) [MIM:271245]: A severe disease associated with mitochondrial dysfunction. Some patients are affected by progressive atrophy of the cerebellum, brain stem, the spinal cord, and sensory axonal neuropathy. Clinical features include hypotonia, athetosis, ataxia, ophthalmoplegia, sensorineural hearing deficit, sensory axonal neuropathy, epileptic encephalopathy and female hypogonadism. In some individuals liver dysfunction and multi- organ failure is present. {ECO:0000269|PubMed:16135556, ECO:0000269|PubMed:17722119, ECO:0000269|PubMed:17921179, ECO:0000269|PubMed:19853444, ECO:0000269|PubMed:22353293}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Perrault syndrome 5 (PRLTS5) [MIM:616138]: A form of Perrault syndrome, a sex-influenced disorder characterized by sensorineural deafness in both males and females, and ovarian dysgenesis in females. Affected females have primary amenorrhea, streak gonads, and infertility, whereas affected males show normal pubertal development and are fertile. {ECO:0000269|PubMed:25355836}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: High relative levels in skeletal muscle, testis and pancreas. Lower levels of expression in the heart, brain, placenta, lung, liver, kidney, spleen, thymus, prostate, ovary, small intestine, colon and leukocytes. Expression is coregulated with MRPL43. {ECO:0000269|PubMed:11431692, ECO:0000269|PubMed:15509589}.; lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;gum;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;adrenal cortex;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;kidney;stomach; dorsal root ganglion; . 0.15369 -0.777005578 12.9747582 378.82083 4.10397 C10orf10 3.86908584231525e-05 0.218221418560518 0.781739890581059 chromosome 10 open reading frame 10 FUNCTION: May play a role in autophagy. {ECO:0000269|PubMed:24530860}.; . TISSUE SPECIFICITY: Expressed in various tissues, including pancreas, placenta, ovary, testis and kidney. {ECO:0000269|PubMed:16123073}.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;oesophagus;endometrium;thyroid;bone;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; uterus corpus;olfactory bulb;placenta;beta cell islets;appendix;ciliary ganglion;trigeminal ganglion; 0.04714 0.08904 -0.0274281 51.65723048 48.92717 1.36657 C10orf11 0.0410566177922973 0.929475385120675 0.0294679970870279 chromosome 10 open reading frame 11 FUNCTION: Required for melanocyte differentiation. {ECO:0000269|PubMed:23395477}.; DISEASE: Albinism, oculocutaneous, 7 (OCA7) [MIM:615179]: A disorder of pigmentation characterized by reduced biosynthesis of melanin in the skin, hair and eyes. Patients show reduced or lacking pigmentation associated with classic albinism ocular abnormalities, including decreased visual acuity, macular hypoplasia, optic dysplasia, atypical choroidal vessels, and nystagmus. {ECO:0000269|PubMed:23395477}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;uterus;prostate;oesophagus;thyroid;bone;iris;testis;brain;bladder;pineal gland;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;urinary;muscle;pancreas;lung;placenta;visual apparatus;alveolus;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.09675 0.08448 0.170987912 65.5579146 811.10686 5.60219 C10orf12 0.979876887411768 0.0201224452847995 6.6730343277897e-07 chromosome 10 open reading frame 12 . . . unclassifiable (Anatomical System);sympathetic chain;colon;blood;skin;bone marrow;bile duct;uterus;breast;lung;placenta;testis;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.27459 0.07594 -0.121287852 44.12007549 963.72519 6.00863 C10orf25 0.012567313038728 0.651733281668159 0.335699405293113 chromosome 10 open reading frame 25 . . . unclassifiable (Anatomical System);lung;placenta;liver;testis;amniotic fluid;spleen;kidney;brain; . 0.08296 . 0.591694063 82.45458835 254.43069 3.43205 C10orf35 0.0683715809117433 0.735777099894179 0.195851319194078 chromosome 10 open reading frame 35 . . . . . 0.01412 0.03197 0.080983847 59.76055674 14.64819 0.52827 C10orf53 0.00106876991334412 0.378118409585072 0.620812820501584 chromosome 10 open reading frame 53 . . . . . 0.06202 . 0.393270925 76.04977589 109.17356 2.26866 C10orf54 0.385978707698929 0.603934712067521 0.0100865802335497 chromosome 10 open reading frame 54 FUNCTION: May stimulate MMP14-mediated MMP2 activation. {ECO:0000269|PubMed:20666777}.; . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; placenta;white blood cells;whole blood; 0.10860 0.09892 0.130533008 63.35810333 2157.61959 8.54526 C10orf55 0.00506563580969443 0.461392657011453 0.533541707178853 chromosome 10 open reading frame 55 . . . . . . . 0.679884223 84.81363529 51.37121 1.41367 C10orf62 9.87003275729534e-05 0.19867852301505 0.801222776657377 chromosome 10 open reading frame 62 . . . . . 0.26739 . 0.060756528 58.52795471 1650.61509 7.51120 C10orf67 1.97204391780943e-06 0.145393542194079 0.854604485762003 chromosome 10 open reading frame 67 . . . lung;kidney; . 0.10777 . 0.03689118 56.64071715 344.76912 3.93862 C10orf71 9.35244270248519e-05 0.936530559068521 0.0633759165044536 chromosome 10 open reading frame 71 . . . skeletal muscle; . . . 2.588936006 98.75560274 7514.38546 18.63190 C10orf71-AS1 . . . C10orf71 antisense RNA 1 . . . . . . . . . . . C10orf76 0.0553398070733845 0.944653419933297 6.7729933189735e-06 chromosome 10 open reading frame 76 . . . smooth muscle;ovary;salivary gland;intestine;colon;choroid;skin;uterus;prostate;endometrium;larynx;thyroid;bone;testis;bladder;brain;unclassifiable (Anatomical System);cartilage;heart;pineal body;muscle;pharynx;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;uterus corpus;white blood cells;pons;atrioventricular node;skeletal muscle; 0.23140 0.09323 -0.426079032 25.36565228 52.22383 1.42814 C10orf82 0.00387838131040333 0.641967208010598 0.354154410678998 chromosome 10 open reading frame 82 . . . . . 0.08739 0.09326 -0.0274281 51.65723048 79.84864 1.88788 C10orf88 0.0385850029121195 0.92922081188822 0.0321941851996601 chromosome 10 open reading frame 88 . . . . . 0.42546 0.07632 -0.179930907 40.35739561 87.31136 1.99552 C10orf90 6.05506924127418e-11 0.118012319800516 0.881987680138933 chromosome 10 open reading frame 90 FUNCTION: Tumor suppressor that is required to sustain G2/M checkpoint after DNA damage. Mediates CDKN1A/p21 protein stability in a ubiquitin-independent manner (By similarity). May have a role in the assembly of primary cilia. {ECO:0000250}.; . . unclassifiable (Anatomical System);bone;placenta;testis;mammary gland;skin; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.04282 . 0.804668134 87.71526303 327.79933 3.84882 C10orf91 0.0743076347528587 0.745979844633471 0.17971252061367 chromosome 10 open reading frame 91 . . . bladder; . 0.09445 . 0.038710339 56.92380278 64.54004 1.64836 C10orf95 0.0113912343253953 0.631134471029771 0.357474294644833 chromosome 10 open reading frame 95 . . . unclassifiable (Anatomical System);prostate;lung;ovary;islets of Langerhans;placenta;colon;choroid; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.09553 . . . 2025.59632 8.27879 C10orf99 0.0824467096075278 0.757083050312045 0.160470240080427 chromosome 10 open reading frame 99 FUNCTION: Potential cytokine proposed to be a ligand of SUSD2; can induce SUSD2 internalization upon binding. May be a tumor suppressor; together with SUSD2 has a growth inhibitory effect on colon cancer cells which includes G1 cell cycle arrest (PubMed:25351403). Specifically inhibits cell growth of lymphoblastoid Raji cell line (PubMed:25585381). {ECO:0000269|PubMed:25351403, ECO:0000269|PubMed:25585381}.; . TISSUE SPECIFICITY: Expressed at high levels in colon and at moderate level in tonsil. Highly reduced expression in primary colon cancer tissues compared with that in adjacent tissues (PubMed:25351403). Highest levels of expression detected in stomach and colon; expressed in epithelium of skin and esophagus, and in some tumor and/or tumor adjacent tissues (TAT), including TAT of esophagus cancer, hepatocellular carcinoma (HCC), squamous cell carcinoma (SCC), basal cell carcinoma (BCC) and invasive ductal carcinoma (IDC) tissues (at protein level) (PubMed:25585381). {ECO:0000269|PubMed:25585381}.; . . 0.12006 . 0.103030231 61.2762444 21.54372 0.72526 C10orf105 . . . chromosome 10 open reading frame 105 . . . . . 0.13959 . 1.212680927 93.0702996 92.87332 2.07142 C10orf107 0.000790930288586529 0.774574838254892 0.224634231456522 chromosome 10 open reading frame 107 . . . unclassifiable (Anatomical System);uterus;lung;hypothalamus;sympathetic chain;testis; superior cervical ganglion;globus pallidus;ciliary ganglion; 0.07541 . -0.404032746 26.53338051 18.06284 0.63027 C10orf111 0.035674990458653 0.62690647136192 0.337418538179427 chromosome 10 open reading frame 111 . . . . . 0.09601 . 0.68351529 85.03774475 547.01428 4.75548 C10orf113 0.00753778234040987 0.543370120844701 0.449092096814889 chromosome 10 open reading frame 113 . . . . . 0.26739 . 1.282454727 93.71313989 2590.75554 9.52470 C10orf120 1.29529424187308e-06 0.371460051740236 0.628538652965522 chromosome 10 open reading frame 120 . . . testis; . 0.05700 . 0.110306132 62.00165133 406.89605 4.22974 C10orf126 . . . chromosome 10 open reading frame 126 . . . . . 0.14245 . . . 21.41851 0.72212 C10orf128 0.045128477576212 0.852013172347899 0.102858350075889 chromosome 10 open reading frame 128 . . . . . 0.25552 . 0.681699246 84.93158764 142.62746 2.60401 C10orf131 . . . chromosome 10 open reading frame 131 . . . . . 0.07563 . . . 46.47293 1.31547 C10orf142 . . . chromosome 10 open reading frame 142 . . . . . . . . . . . C11orf1 7.80824715195598e-07 0.161045188613443 0.838954030561842 chromosome 11 open reading frame 1 . . . myocardium;ovary;colon;parathyroid;skin;uterus;prostate;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);trophoblast;cerebellum cortex;adrenal cortex;bile duct;lung;adrenal gland;placenta;liver;spleen;head and neck;kidney;aorta; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;trigeminal ganglion; 0.11040 0.08671 0.148941568 64.31941496 200.68134 3.06302 C11orf16 4.79365943685803e-06 0.40703931312569 0.592955893214873 chromosome 11 open reading frame 16 . . . unclassifiable (Anatomical System);uterus;lung;endometrium;bone;testis;spleen; superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.19004 . 1.600244264 95.8893607 2404.61874 9.10571 C11orf21 . . . chromosome 11 open reading frame 21 . . TISSUE SPECIFICITY: Expressed exclusively in heart.; . . 0.12372 . 0.880130671 88.9596603 484.52242 4.53231 C11orf24 0.0307663209865782 0.811089368169034 0.158144310844388 chromosome 11 open reading frame 24 . . TISSUE SPECIFICITY: Highest expression in heart, placenta, liver, pancreas and colon. Also detected in brain, lung, skeletal muscle, kidney, spleen, prostate, testis, ovary and small intestine. Lowest expression in thymus and leukocytes. {ECO:0000269|PubMed:11401438}.; medulla oblongata;smooth muscle;ovary;salivary gland;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;synovium;larynx;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;liver;trigeminal ganglion;cingulate cortex; 0.04211 0.06373 0.156217551 64.82071243 3195.74518 10.77541 C11orf31 0.000781712087900896 0.325241881277093 0.673976406635006 chromosome 11 open reading frame 31 FUNCTION: May be involved in a redox-related process. {ECO:0000305}.; . . . . 0.18554 . 0.215080721 67.91696155 95.29135 2.10734 C11orf40 4.84556312500488e-08 0.0331618782740022 0.966838073270367 chromosome 11 open reading frame 40 . . . . . 0.08219 . 0.795569043 87.49115357 464.3754 4.46475 C11orf42 3.04760565776035e-06 0.32807613821147 0.671920814182872 chromosome 11 open reading frame 42 . . . unclassifiable (Anatomical System);medulla oblongata; . 0.30855 . -0.003562597 53.72729417 50.65986 1.40169 C11orf44 . . . chromosome 11 open reading frame 44 . . . . . 0.02224 . . . 4.71837 0.17097 C11orf45 0.0137112878913203 0.6697347288478 0.316553983260879 chromosome 11 open reading frame 45 . . . unclassifiable (Anatomical System);lung;heart;bone;thyroid;spleen;kidney;brain; . 0.17363 . 0.058937498 58.26256192 43.76914 1.25991 C11orf49 5.45467879227827e-07 0.650818143221783 0.349181311310338 chromosome 11 open reading frame 49 . . . lymphoreticular;ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;synovium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; whole brain;amygdala;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;parietal lobe;cingulate cortex;cerebellum; 0.25098 0.10416 -0.532670911 20.78320359 53.14985 1.44731 C11orf52 0.0237243779473785 0.772382368394287 0.203893253658334 chromosome 11 open reading frame 52 . . . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;sympathetic chain;colon;parathyroid;fovea centralis;choroid;lens;retina;pancreas;prostate;optic nerve;lung;nasopharynx;thyroid;placenta;macula lutea;liver;spleen;kidney;mammary gland; superior cervical ganglion;atrioventricular node; 0.07586 . 0.413500896 76.67492333 923.54961 5.90102 C11orf53 7.52888554833811e-05 0.307408860787309 0.692515850357207 chromosome 11 open reading frame 53 . . . unclassifiable (Anatomical System);prostate;lung;testis; . 0.33310 0.09879 -0.181750739 40.15687662 442.77162 4.37991 C11orf54 0.00735855500344581 0.923384509267401 0.0692569357291538 chromosome 11 open reading frame 54 FUNCTION: Exhibits ester hydrolase activity on the substrate p- nitrophenyl acetate. {ECO:0000269|PubMed:16522806}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;fetal liver;superior cervical ganglion;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion; 0.09933 0.10173 0.349177632 74.18023119 183.88378 2.94200 C11orf57 0.913210185651405 0.0861665266057932 0.000623287742802257 chromosome 11 open reading frame 57 . . . lymphoreticular;myocardium;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;retina;uterus;prostate;whole body;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.10557 0.09671 -0.205617011 38.57631517 27.58951 0.88782 C11orf58 0.709037215515083 0.287547536006794 0.00341524847812285 chromosome 11 open reading frame 58 . . . ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;oesophagus;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;nervous;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;alveolus;liver;cervix;head and neck;kidney;mammary gland;stomach; amygdala;superior cervical ganglion;caudate nucleus; 0.46512 0.13942 0.035072054 56.2514744 5.6395 0.21112 C11orf63 1.16452328608552e-11 0.162347532368995 0.837652467619359 chromosome 11 open reading frame 63 . . . unclassifiable (Anatomical System);lymphoreticular;medulla oblongata;islets of Langerhans;parathyroid;lung;endometrium;bone;thyroid;testis;head and neck;kidney;mammary gland; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07315 . -1.284117362 5.113234253 229.21125 3.27159 C11orf65 8.78129550119407e-17 0.000321570922719219 0.999678429077281 chromosome 11 open reading frame 65 . . . . . 0.10302 0.09502 0.661468037 84.4420854 134.28471 2.51990 C11orf68 0.409498865109943 0.553477906478686 0.0370232284113704 chromosome 11 open reading frame 68 . . . . . 0.36879 0.10806 0.569646743 81.88841708 64.97427 1.65616 C11orf70 8.92573228629031e-06 0.532558584018189 0.467432490249525 chromosome 11 open reading frame 70 . . . . . 0.19619 0.09466 -0.229483771 36.86010852 22.70772 0.75951 C11orf71 0.00842481501256066 0.566986814537717 0.424588370449722 chromosome 11 open reading frame 71 . . . unclassifiable (Anatomical System);medulla oblongata;islets of Langerhans;hypothalamus;colon;parathyroid;fovea centralis;choroid;lens;retina;bile duct;pancreas;prostate;optic nerve;lung;adrenal gland;epididymis;placenta;macula lutea;testis;kidney;brain;mammary gland;stomach; testis; 0.08711 . 0.281220278 71.07808445 49.68604 1.38181 C11orf72 0.00104922449953811 0.374841062075424 0.624109713425038 chromosome 11 open reading frame 72 . . . . . 0.08850 . . . 716.3207 5.31204 C11orf73 0.769988210012451 0.228282617478851 0.00172917250869799 chromosome 11 open reading frame 73 FUNCTION: Acts as a specific nuclear import carrier for HSP70 proteins following heat-shock stress: acts by mediating the nucleoporin-dependent translocation of ATP-bound HSP70 proteins into the nucleus. HSP70 proteins import is required to protect cells from heat shock damages. Does not translocate ADP-bound HSP70 proteins into the nucleus. {ECO:0000269|PubMed:22541429}.; . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;cochlea;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;cerebellum cortex;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.81282 0.11262 0.03689118 56.64071715 8.17857 0.30133 C11orf74 0.00762075072953251 0.777963318820547 0.21441593044992 chromosome 11 open reading frame 74 . . . unclassifiable (Anatomical System);myocardium;heart;islets of Langerhans;parathyroid;vein;pancreas;lung;endometrium;nasopharynx;trabecular meshwork;bone;placenta;testis;cervix;brain;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.05960 0.07345 0.193034296 66.82000472 129.47178 2.48001 C11orf80 0.00846259594390007 0.97833846187349 0.0131989421826099 chromosome 11 open reading frame 80 . . TISSUE SPECIFICITY: Detected in lung, spleen,colon and in skeletal muscle. {ECO:0000269|PubMed:18160775}.; ovary;colon;parathyroid;choroid;fovea centralis;retina;prostate;optic nerve;endometrium;larynx;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;blood;lens;lung;placenta;macula lutea;duodenum;head and neck;kidney;mammary gland;stomach;peripheral nerve; testis - interstitial;tongue;testis; 0.03682 . 0.106667882 61.73036093 116.69248 2.34991 C11orf84 0.471418765181543 0.52324378638431 0.00533744843414652 chromosome 11 open reading frame 84 . . . unclassifiable (Anatomical System);medulla oblongata;cartilage;heart;ovary;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;endometrium;placenta;bone;macula lutea;visual apparatus;iris;testis;cervix;kidney;brain;pineal gland; superior cervical ganglion;atrioventricular node; . 0.13470 0.018483465 55.44939844 96.11033 2.11926 C11orf85 0.00735718824902867 0.923370045168703 0.0692727665822677 chromosome 11 open reading frame 85 FUNCTION: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the complex, MAJIN acts as the anchoring subunit to the nucleus inner membrane. MAJIN shows DNA-binding activity, possibly for the stabilization of telomere attachment on the nucleus inner membrane. {ECO:0000250|UniProtKB:Q9D992}.; . . unclassifiable (Anatomical System);lung;pituitary gland;testis; . . . -0.427900189 25.14744043 18.91511 0.65318 C11orf86 . . . chromosome 11 open reading frame 86 . . . stomach; . . . 0.057118534 57.99716914 67.05597 1.69305 C11orf87 0.245098740734549 0.643307213595794 0.111594045669657 chromosome 11 open reading frame 87 . . . unclassifiable (Anatomical System);frontal lobe;hippocampus;brain;retina;bone marrow; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; . . 0.03689118 56.64071715 33.06075 1.02340 C11orf88 0.0986136578440954 0.86650179010107 0.0348845520548348 chromosome 11 open reading frame 88 . . . unclassifiable (Anatomical System);lung;cartilage;endometrium; . . . 1.148343558 92.42745931 224.45577 3.24011 C11orf91 . . . chromosome 11 open reading frame 91 . . . . . . . . . 881.028 5.78254 C11orf94 0.000289638176341335 0.344948710784913 0.654761651038745 chromosome 11 open reading frame 94 . . . . . . . 0.058937498 58.26256192 31.88611 1.00293 C11orf95 . . . chromosome 11 open reading frame 95 . DISEASE: Note=A chromosomal aberration involving MKL2 is found in 3 chondroid lipomas. Translocation t(11;16)(q13;p13) with MKL2 produces a C11orf95-MKL2 fusion protein (PubMed:20607705). {ECO:0000269|PubMed:20607705}.; DISEASE: Note=A chromosomal aberration involving RELA is found in more than two-thirds of supratentorial ependymomas. Translocation with RELA produces a C11orf95-RELA fusion protein. C11orf95-RELA translocations are potent oncogenes that probably transform neural stem cells by driving an aberrant NF-kappa-B transcription program (PubMed:24553141). {ECO:0000269|PubMed:24553141}.; . unclassifiable (Anatomical System);endometrium;kidney; whole brain;superior cervical ganglion;subthalamic nucleus;fetal brain;prefrontal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . . . . . C11orf96 . . . chromosome 11 open reading frame 96 . . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;lung;placenta;macula lutea;cervix;kidney;mammary gland;stomach;aorta;thymus; . . . . . 2093.98428 8.42927 C11orf97 . . . chromosome 11 open reading frame 97 . . . . . . . . . . . C11orf98 . . . chromosome 11 open reading frame 98 . . . . . 0.06000 . 0.593509966 82.51356452 . . C11orf98P1 . . . chromosome 11 open reading frame 98 pseudogene 1 . . . . . . . . . . . C12orf4 9.82515157241538e-05 0.997085701127406 0.00281604735687032 chromosome 12 open reading frame 4 FUNCTION: Plays a role in mast cell degranulation. {ECO:0000250|UniProtKB:D4A770}.; . . smooth muscle;colon;parathyroid;skin;retina;bone marrow;uterus;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;urinary;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;uterus corpus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex; . . -0.60427181 17.74593064 37.65895 1.12175 C12orf10 2.43605474737215e-06 0.908273478157933 0.0917240857873196 chromosome 12 open reading frame 10 . . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in testis. {ECO:0000269|PubMed:19014353}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;bone;thyroid;iris;testis;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;bile duct;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; testis - interstitial;testis; 0.22388 0.09636 0.777157784 87.17857985 74.44642 1.80331 C12orf29 2.45710284617945e-05 0.511277920515376 0.488697508456162 chromosome 12 open reading frame 29 . . . ovary;salivary gland;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;cochlea;endometrium;bone;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach;aorta; amygdala;dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;occipital lobe;medulla oblongata;temporal lobe;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.25136 0.07797 -0.095386216 46.48502005 35.43929 1.07002 C12orf40 1.15273949503851e-19 0.000329459479294808 0.999670540520705 chromosome 12 open reading frame 40 . . . lung;testis;skeletal muscle; . . . 1.065596954 91.61358811 1095.22172 6.33027 C12orf42 2.29275590874033e-07 0.0811804525793355 0.918819318145074 chromosome 12 open reading frame 42 . . . lung;testis; . 0.09069 . 1.596607091 95.87166785 230.01706 3.27820 C12orf43 2.5600625299979e-07 0.160838260287405 0.839161483706342 chromosome 12 open reading frame 43 . . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;adrenal cortex;colon;fovea centralis;lens;vein;skin;retina;uterus;prostate;lung;endometrium;placenta;macula lutea;hippocampus;testis;spleen;kidney;brain;stomach;cerebellum; . 0.13007 . 0.262810045 70.43524416 179.77744 2.91151 C12orf45 0.389486545133401 0.568116592956825 0.0423968619097736 chromosome 12 open reading frame 45 . . . ovary;salivary gland;intestine;colon;fovea centralis;skin;uterus;prostate;whole body;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;pharynx;blood;lung;nasopharynx;macula lutea;visual apparatus;duodenum;liver;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16566 0.08891 0.283038099 71.26680821 1106.00549 6.35514 C12orf49 0.0452103165858912 0.852156519817112 0.102633163596997 chromosome 12 open reading frame 49 . . . ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;pancreas;lung;placenta;head and neck;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.13575 . 0.194852702 67.03231894 262.23682 3.47533 C12orf50 0.000154448367602554 0.992654754225816 0.00719079740658108 chromosome 12 open reading frame 50 . . . medulla oblongata;lung;testis; . 0.44826 . 0.352813824 74.49280491 410.92596 4.24860 C12orf54 0.00416735395983964 0.862963044418493 0.132869601621667 chromosome 12 open reading frame 54 . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; . 0.14503 . 0.569646743 81.88841708 967.04382 6.01394 C12orf56 2.90933463847163e-11 0.0215300017886202 0.978469998182286 chromosome 12 open reading frame 56 . . . unclassifiable (Anatomical System);placenta;liver;testis;spleen;choroid;kidney; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node; 0.11629 . -0.246069119 36.06982779 4960.51902 14.35200 C12orf57 0.0603360644826819 0.718488582964094 0.221175352553224 chromosome 12 open reading frame 57 FUNCTION: In brain, may be required for corpus callusum development. {ECO:0000269|PubMed:23453666}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with higher expression in lung and fetal brain. {ECO:0000269|PubMed:23453666}.; myocardium;ovary;skin;prostate;optic nerve;frontal lobe;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;kidney;stomach;aorta;thymus; . 0.04682 0.10923 -0.117432389 44.89266336 27.23377 0.87693 C12orf60 0.00629216814365261 0.505520573029725 0.488187258826622 chromosome 12 open reading frame 60 . . . unclassifiable (Anatomical System);uterus;medulla oblongata;lung;whole body;cartilage;placenta;testis;parathyroid;kidney;germinal center;skin; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion; 0.05292 . 0.415317661 76.81056853 2517.40305 9.36065 C12orf65 0.17232858993411 0.769707276235097 0.0579641338307934 chromosome 12 open reading frame 65 FUNCTION: May act as a codon-independent translation release factor that has lost all stop codon specificity and directs the termination of translation in mitochondrion. May help rescuing stalled mitoribosomes during translation (By similarity). {ECO:0000250}.; DISEASE: Combined oxidative phosphorylation deficiency 7 (COXPD7) [MIM:613559]: A mitochondrial disease resulting in encephalomyopathy. Clinical manifestations include psychomotor delay and regression, ataxia, optic atrophy, nystagmus and muscle atrophy and weakness. {ECO:0000269|PubMed:20598281}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spastic paraplegia 55, autosomal recessive (SPG55) [MIM:615035]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. Complicated forms are recognized by additional variable features including spastic quadriparesis, seizures, dementia, amyotrophy, extrapyramidal disturbance, cerebral or cerebellar atrophy, optic atrophy, and peripheral neuropathy, as well as by extra neurological manifestations. {ECO:0000269|PubMed:23188110}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;urinary;pharynx;blood;lens;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;cerebellum; 0.05651 0.07479 0.12689526 63.00424628 43.81128 1.26080 C12orf66 0.757788499527866 0.240208563668473 0.00200293680366131 chromosome 12 open reading frame 66 . . . unclassifiable (Anatomical System);heart;colon;skin;uterus;lung;placenta;thyroid;liver;testis;cervix;kidney;brain;stomach; . . . 0.349177632 74.18023119 57.25218 1.52422 C12orf71 0.360330750091633 0.588096868804526 0.0515723811038411 chromosome 12 open reading frame 71 . . . . . . . 0.661468037 84.4420854 786.23737 5.53893 C12orf73 . . . chromosome 12 open reading frame 73 . . . . . . . 0.834220813 88.15758434 770.3657 5.49228 C12orf74 0.000522237109268262 0.45325998875882 0.546217774131911 chromosome 12 open reading frame 74 . . . . . . . 0.549415813 81.38122199 164.76253 2.80389 C12orf75 . . . chromosome 12 open reading frame 75 . . TISSUE SPECIFICITY: High expression in placenta, skeletal muscle, kidney and pancreas tissues. Absent or very faint expression in heart, brain, lung and liver. Expressed during adipogenic differentiation of mesenchymal stem cells (at protein level). {ECO:0000269|PubMed:11890990, ECO:0000269|PubMed:19531736}.; . . . . 0.12325821 62.38499646 5.54069 0.20669 C12orf76 0.000101301333532111 0.20146015924177 0.798438539424698 chromosome 12 open reading frame 76 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;pharynx;blood;breast;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; amygdala;whole brain;occipital lobe;globus pallidus;cingulate cortex; . . -0.09720619 46.20193442 4.3306 0.15760 C12orf77 0.00286773857994041 0.576584819412509 0.42054744200755 chromosome 12 open reading frame 77 . . . . . . . 0.659651797 84.35362114 95.7308 2.11456 C12orf80 . . . chromosome 12 open reading frame 80 . . . . . . . . . . . C14orf1 0.891783234105691 0.107120877221924 0.00109588867238562 chromosome 14 open reading frame 1 . . TISSUE SPECIFICITY: Ubiquitous; strongly expressed in testis and some cancer cell lines.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion; 0.41820 0.15588 0.013025609 54.62962963 8.15434 0.30109 C14orf2 0.658634629667739 0.317482896203621 0.0238824741286405 chromosome 14 open reading frame 2 . . . myocardium;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;trophoblast;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; whole brain;amygdala;medulla oblongata;occipital lobe;thalamus;heart;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.06946 0.09630 0.301449681 71.80938901 251.16233 3.41398 C14orf28 2.0845213544728e-10 0.035459074288874 0.964540925502674 chromosome 14 open reading frame 28 . . . uterus;ovary;heart;bone;placenta;testis;parathyroid;lens;brain;skin;stomach; dorsal root ganglion;testis;atrioventricular node; 0.53991 0.10452 0.549415813 81.38122199 424.12409 4.30089 C14orf37 8.27235953361938e-05 0.926321535847241 0.0735957405574226 chromosome 14 open reading frame 37 . . . unclassifiable (Anatomical System);cartilage;islets of Langerhans;fovea centralis;choroid;lens;skin;retina;prostate;optic nerve;lung;placenta;macula lutea;visual apparatus;liver;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.12497 . 0.428052693 77.31186601 5907.40301 15.95843 C14orf39 0.00852079034470034 0.990927165862194 0.000552043793105361 chromosome 14 open reading frame 39 FUNCTION: May be involved in eye development through regulation of the SIX6 transcription factor.; . . lung;testis; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11284 . 1.177658736 92.77541873 2583.95244 9.50682 C14orf79 5.1346210352029e-08 0.12244707079092 0.877552877862869 chromosome 14 open reading frame 79 . . . . . 0.03915 . -0.156065314 42.16206653 58.52682 1.54953 C14orf80 0.00122228120574754 0.848598336189045 0.150179382605207 chromosome 14 open reading frame 80 . . . unclassifiable (Anatomical System);lymph node;ovary;muscle;colon;skin;skeletal muscle;uterus;pancreas;prostate;placenta;bone;visual apparatus;liver;cervix;kidney;bladder;stomach;peripheral nerve; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion; 0.10678 . 0.933309256 89.82661005 758.75641 5.45625 C14orf93 0.0321277715658725 0.958728112440144 0.00914411599398358 chromosome 14 open reading frame 93 . . . colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.35382 . -0.53631094 20.53550366 487.60013 4.54557 C14orf105 0.000136147483752656 0.853968099341741 0.145895753174506 chromosome 14 open reading frame 105 . . . unclassifiable (Anatomical System);prostate;endometrium;liver;kidney;brain; ciliary ganglion;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.73273 . 0.52918614 80.81505072 236.92352 3.32426 C14orf119 0.0027616618278927 0.568434736261977 0.42880360191013 chromosome 14 open reading frame 119 . . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; . 0.31663 0.09213 0.169169615 65.33380514 52.30513 1.42938 C14orf132 . . . chromosome 14 open reading frame 132 . . . . . . . . . 9.86635 0.36148 C14orf142 0.190974080812774 0.647067743699482 0.161958175487744 chromosome 14 open reading frame 142 . . . lymphoreticular;medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;blood;lens;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;ciliary ganglion; 0.11616 . 0.035072054 56.2514744 9.93726 0.36414 C14orf144 . . . chromosome 14 open reading frame 144 . . . . . . . . . 24.44047 0.80391 C14orf159 2.06971538888579e-14 0.00802249886695434 0.991977501133025 chromosome 14 open reading frame 159 . . . smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;heart;cartilage;blood;lens;skeletal muscle;bile duct;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; . 0.12193 0.09037 1.894214943 97.33427695 2364.95065 9.02513 C14orf166 0.666285715823714 0.332636862904812 0.00107742127147364 chromosome 14 open reading frame 166 FUNCTION: RNA-binding protein involved in modulation of mRNA transcription by Polymerase II. In case of infection by influenza virus A, is involved in viral replication. Component of the tRNA- splicing ligase complex and is required for tRNA ligation (PubMed:24870230). May be required for RNA transport (PubMed:24608264). {ECO:0000269|PubMed:16950395, ECO:0000269|PubMed:24608264, ECO:0000269|PubMed:24870230}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at high level in heart and skeletal muscle. Expressed at intermediate level in liver, pancreas, fetal brain and fetal lung. Weakly expressed in adult brain, adult lung, placenta, fetal liver and fetal kidney. Overexpressed in many brain tumors. {ECO:0000269|PubMed:15147888}.; myocardium;lymphoreticular;ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;brain;bladder;tonsil;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;amnion;head and neck;kidney;stomach;aorta;thymus; testis - interstitial;testis - seminiferous tubule;testis;tumor;white blood cells; 0.56732 0.14229 -0.317668748 31.45789101 22.63143 0.75713 C14orf169 . . . chromosome 14 open reading frame 169 FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC- induced transcriptional activation. {ECO:0000250, ECO:0000269|PubMed:14742713, ECO:0000269|PubMed:17308053, ECO:0000269|PubMed:23103944}.; . TISSUE SPECIFICITY: Widely expressed. Overexpressed in lung carcinomas. {ECO:0000269|PubMed:14742713, ECO:0000269|PubMed:17308053}.; . . . . . . . . C14orf177 0.00674701538541544 0.520052382257989 0.473200602356596 chromosome 14 open reading frame 177 . . . heart; superior cervical ganglion;trigeminal ganglion;cerebellum; 0.05460 . 0.459411326 78.28497287 191.00077 2.99788 C14orf178 0.00852342418083104 0.569464622349725 0.422011953469444 chromosome 14 open reading frame 178 . . . . . 0.01947 . 0.479642105 78.95140363 291.25393 3.65085 C14orf180 0.0134314304920118 0.665500298518981 0.321068270989008 chromosome 14 open reading frame 180 . . . unclassifiable (Anatomical System);optic nerve;placenta;brain;skeletal muscle;stomach;retina; . . . . . 58.21294 1.54414 C15orf32 0.00550955422560942 0.71569501499216 0.27879543078223 chromosome 15 open reading frame 32 . . . unclassifiable (Anatomical System); . 0.06521 . 0.459411326 78.28497287 292.37957 3.65703 C15orf38-AP3S2 1.03619222630726e-09 0.08913339836572 0.910866600598088 C15orf38-AP3S2 readthrough FUNCTION: Regulates actin polymerization by inhibiting the actin- nucleating activity of the Arp2/3 complex; the function is competetive with nucleation promoting factors. Participates in an incoherent feedforward loop at the lamellipodium tip where it inhibits the ARP2/2 complex in response to Rac signaling and where Rac also stimulates actin polymerization through the WAVE complex. Involved in steering cell migration by controlling its directional persistence. {ECO:0000269|PubMed:24132237}.; . . . . . . -0.867014353 10.72776598 122.99134 2.41525 C15orf39 0.919030415254172 0.0809478668481698 2.17178976576548e-05 chromosome 15 open reading frame 39 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;synovium;thyroid;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;islets of Langerhans;urinary;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;cervix;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.13795 0.09069 0.723780906 85.87520642 1855.04575 7.93842 C15orf40 0.268492643273296 0.636213510016169 0.0952938467105355 chromosome 15 open reading frame 40 . . . unclassifiable (Anatomical System);pancreas;lymph node;lung;ovary;islets of Langerhans;larynx;placenta;testis;parathyroid;head and neck;skeletal muscle; superior cervical ganglion;liver;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06603 0.08071 1.038098315 91.20665251 469.53715 4.48466 C15orf41 0.0155525648224664 0.958545112349425 0.0259023228281091 chromosome 15 open reading frame 41 . DISEASE: Anemia, congenital dyserythropoietic, 1B (CDAN1B) [MIM:615631]: An autosomal recessive blood disorder characterized by morphological abnormalities of erythroblasts, ineffective erythropoiesis, macrocytic anemia and secondary hemochromatosis. It is occasionally associated with bone abnormalities, especially of the hands and feet (acrodysostosis), nail hypoplasia, and scoliosis. Ultrastructural features include internuclear chromatin bridges connecting some nearly completely separated erythroblasts and an abnormal appearance (spongy or Swiss-cheese appearance) of the heterochromatin in a high proportion of the erythroblasts. {ECO:0000269|PubMed:23716552}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);myocardium;lymph node;heart;ovary;adrenal cortex;parathyroid;skin;skeletal muscle;uterus;whole body;lung;adrenal gland;thyroid;placenta;testis;kidney;brain;pineal gland;bladder;stomach; ciliary ganglion;atrioventricular node; 0.20546 0.10734 -0.005381972 53.50908233 4297.62941 13.04105 C15orf43 0.000137584911341295 0.643442777406568 0.35641963768209 chromosome 15 open reading frame 43 FUNCTION: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. {ECO:0000250|UniProtKB:Q9D494}.; . . lung;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule; 0.10937 . 0.769889969 86.95447039 152.15743 2.69846 C15orf48 0.000404124925714789 0.403824372018415 0.59577150305587 chromosome 15 open reading frame 48 . . TISSUE SPECIFICITY: Expressed mainly in stomach, placenta, small intestine and colon, as well as in normal mucosa of esophagus. Down-regulated in esophageal squamous cell carcinoma.; unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;oral cavity;colon;parathyroid;blood;bone marrow;uterus;prostate;lung;cerebral cortex;placenta;testis;head and neck;kidney;mammary gland;tonsil;stomach; testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node; 0.06934 . 0.079165051 59.43029016 583.12577 4.89578 C15orf52 0.0025769414685249 0.994323306296981 0.00309975223449387 chromosome 15 open reading frame 52 . . . . . 0.09350 0.08190 -0.242430445 36.22906346 525.76821 4.67850 C15orf53 0.0936098085913799 0.767944340500372 0.138445850908248 chromosome 15 open reading frame 53 . . . . . 0.08249 . 0.237127192 68.98443029 264.89166 3.49267 C15orf54 0.000115195661974805 0.215714149482993 0.784170654855032 chromosome 15 open reading frame 54 . . . . . 0.08768 . 0.749657564 86.56522765 49.31948 1.37296 C15orf56 0.0517037024480086 0.694311763591265 0.253984533960727 chromosome 15 open reading frame 56 . . . unclassifiable (Anatomical System);lung;ovary;placenta;parathyroid; . . . . . 952.94322 5.97510 C15orf57 0.611394297335686 0.380260171850134 0.0083455308141797 chromosome 15 open reading frame 57 . . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;breast;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;stomach; . 0.06085 . 0.03689118 56.64071715 2166.55295 8.56915 C15orf59 0.244691481801632 0.725020777811331 0.0302877403870375 chromosome 15 open reading frame 59 . . . . . . . 0.238945317 69.20853975 47.6831 1.34079 C15orf59-AS1 . . . C15orf59 antisense RNA 1 . . . . . . . . . . . C15orf61 . . . chromosome 15 open reading frame 61 . . . unclassifiable (Anatomical System);myocardium;islets of Langerhans;muscle;colon;blood;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;lung;placenta;macula lutea;visual apparatus;testis;kidney;stomach; whole brain;testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle;cerebellum; . . . . 57.59866 1.53306 C15orf62 . . . chromosome 15 open reading frame 62 . . . unclassifiable (Anatomical System);lung;cervix;kidney;germinal center;lens;skeletal muscle;stomach; . . . 0.501689326 79.7888653 94.52721 2.09365 C15orf65 0.360932047574078 0.482254260553147 0.156813691872775 chromosome 15 open reading frame 65 . . . . . . . . . 1385.63444 6.96932 C16orf13 0.00453725397293647 0.675460854209733 0.32000189181733 chromosome 16 open reading frame 13 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;hypothalamus;urinary;pharynx;blood;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; whole brain;heart;temporal lobe;liver;tumor;caudate nucleus; 0.08262 0.11123 0.060756528 58.52795471 27.25005 0.87775 C16orf45 0.214680178058486 0.746126192914804 0.0391936290267099 chromosome 16 open reading frame 45 . . . ovary;salivary gland;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;thyroid;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;hypothalamus;muscle;skeletal muscle;breast;pancreas;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;stomach;aorta;cerebellum; amygdala;whole brain;occipital lobe;subthalamic nucleus;medulla oblongata;temporal lobe;prefrontal cortex;globus pallidus;pons;cingulate cortex;parietal lobe; 0.32224 0.11057 -0.005381972 53.50908233 30.22262 0.96394 C16orf46 5.35421701391956e-06 0.248495520027786 0.7514991257552 chromosome 16 open reading frame 46 . . . unclassifiable (Anatomical System);lung;testis;skin; superior cervical ganglion;trigeminal ganglion;cerebellum; 0.05038 . 1.021500656 91.01792876 994.84282 6.07737 C16orf47 . . . chromosome 16 open reading frame 47 . . . lung;testis; . 0.07596 . . . 29.78673 0.94982 C16orf52 . . . chromosome 16 open reading frame 52 . . . unclassifiable (Anatomical System);uterus;lung;cartilage;heart;placenta;testis;brain;skin;retina; . . . . . 1116.87851 6.38208 C16orf54 0.668080507728988 0.309864563552239 0.0220549287187734 chromosome 16 open reading frame 54 . . . nasopharynx; . 0.14301 . . . 93.86512 2.08396 C16orf58 1.17704527811772e-10 0.0917174159391841 0.908282583943111 chromosome 16 open reading frame 58 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;pineal body;oral cavity;muscle;adrenal cortex;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;liver;cingulate cortex; 0.10294 0.10376 0.020302773 55.60863411 109.82472 2.27691 C16orf59 1.91727702821914e-08 0.23983416308089 0.76016581774634 chromosome 16 open reading frame 59 . . . unclassifiable (Anatomical System);fovea centralis;choroid;lens;skin;retina;pancreas;optic nerve;lung;placenta;macula lutea;visual apparatus;liver;testis;spleen;cervix;mammary gland;brain;stomach; fetal liver;superior cervical ganglion;skeletal muscle;pituitary; 0.33077 0.07928 0.464864541 78.69190847 47.31292 1.33445 C16orf62 1.28585119520756e-05 0.999983533143218 3.60834482976074e-06 chromosome 16 open reading frame 62 FUNCTION: Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes. Seems not to be required for CCC complex stability (PubMed:25355947). {ECO:0000269|PubMed:25355947}.; . . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;larynx;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; testis - interstitial;superior cervical ganglion;testis;pons;cingulate cortex;parietal lobe; 0.17516 . -1.212529868 5.691200755 233.63681 3.30283 C16orf70 0.80354551663145 0.196445137523182 9.34584536716984e-06 chromosome 16 open reading frame 70 . . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;synovium;thyroid;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;lens;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; . 0.17969 0.11473 0.038710339 56.92380278 94.90509 2.10049 C16orf71 1.37813829884911e-13 0.0127040746752116 0.98729592532465 chromosome 16 open reading frame 71 . . . unclassifiable (Anatomical System);medulla oblongata;colon;fovea centralis;choroid;lens;retina;optic nerve;lung;placenta;macula lutea;duodenum;testis;spleen;kidney;brain;stomach; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;pons;trigeminal ganglion; 0.07990 . 1.405441678 94.77471102 1280.28787 6.73800 C16orf72 0.98608139706383 0.0139120299133377 6.57302283242042e-06 chromosome 16 open reading frame 72 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;cerebellum; . 0.16479 . 0.237127192 68.98443029 179.80542 2.91238 C16orf74 0.0240486458910046 0.547868561487523 0.428082792621473 chromosome 16 open reading frame 74 . . . unclassifiable (Anatomical System);lymph node;heart;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;placenta;macula lutea;visual apparatus;hypopharynx;testis;head and neck;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.15390 . 0.03689118 56.64071715 49.97686 1.38730 C16orf78 4.18701427806165e-06 0.382216919071952 0.61777889391377 chromosome 16 open reading frame 78 . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;pons;skeletal muscle; 0.03660 . 1.107875794 92.03821656 579.35944 4.87731 C16orf82 . . . chromosome 16 open reading frame 82 . . TISSUE SPECIFICITY: Preferentially expressed in teratocarcinoma rather than in normal testis.; . . . . . . . . C16orf86 0.652428951452165 0.3417113935084 0.00585965503943525 chromosome 16 open reading frame 86 . . . . . 0.09611 . -0.317668748 31.45789101 37.55182 1.11801 C16orf87 0.097478781929178 0.867002138808298 0.0355190792625237 chromosome 16 open reading frame 87 . . . ovary;salivary gland;colon;parathyroid;skin;bone marrow;prostate;frontal lobe;testis;brain;artery;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;stomach;aorta; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;pons; . . 0.035072054 56.2514744 . . C16orf89 2.03997402633687e-14 0.00214736356945935 0.99785263643052 chromosome 16 open reading frame 89 . . TISSUE SPECIFICITY: Predominantly expressed in thyroid tissue. {ECO:0000269|PubMed:20578903}.; unclassifiable (Anatomical System);heart;hypothalamus;colon;choroid;skin;skeletal muscle;uterus;pancreas;optic nerve;lung;oesophagus;endometrium;thyroid;bone;hippocampus;testis;spleen;kidney;brain;mammary gland;stomach;thymus; superior cervical ganglion;thyroid;atrioventricular node;trigeminal ganglion; . . 0.801024817 87.65628686 1415.69165 7.03277 C16orf90 0.00240644832042289 0.538849957189899 0.458743594489678 chromosome 16 open reading frame 90 . . . . . . . 0.060756528 58.52795471 . . C16orf91 3.85106439476045e-07 0.354099014781568 0.645900600111993 chromosome 16 open reading frame 91 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; . . . 0.86534717 88.80042463 155.12166 2.72042 C16orf92 0.018925440394968 0.73288003059434 0.248194529010692 chromosome 16 open reading frame 92 . . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;fovea centralis;choroid;lens;skin;retina;optic nerve;whole body;lung;cornea;macula lutea;visual apparatus;liver;testis;kidney;brain;mammary gland; . . . 0.237127192 68.98443029 15.03136 0.53982 C16orf95 . . . chromosome 16 open reading frame 95 . . . . . . . . . 1680.25293 7.55524 C16orf96 0.0702878052319574 0.523578171464285 0.406134023303757 chromosome 16 open reading frame 96 . . . . . . . 3.557878487 99.49870252 2809.76477 10.00400 C16orf97 . . . chromosome 16 open reading frame 97 . . . . . . . . . 66.75646 1.68584 C17orf47 1.30236935252049e-05 0.835379603241998 0.164607373064476 chromosome 17 open reading frame 47 . . . unclassifiable (Anatomical System);endometrium;testis; . 0.04011 0.07577 7.61E-05 53.98089172 245.02417 3.37661 C17orf49 0.00762293080428993 0.778014698368659 0.214362370827052 chromosome 17 open reading frame 49 FUNCTION: Component of chromatin complexes such as the MLL1/MLL and NURF complexes.; . . myocardium;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;atrium;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;pancreas;lung;pia mater;placenta;hippocampus;kidney;aorta; . 0.41661 . -0.119252484 44.53880632 10.5877 0.38496 C17orf50 0.00795276378704014 0.554726984141474 0.437320252071486 chromosome 17 open reading frame 50 . . . lung;testis; . 0.18714 . . . 2000.414 8.24012 C17orf51 . . . chromosome 17 open reading frame 51 . . . . . . . 0.079165051 59.43029016 350.85075 3.97119 C17orf53 5.99401321600703e-08 0.654574047505555 0.345425892554313 chromosome 17 open reading frame 53 . . . unclassifiable (Anatomical System);medulla oblongata;ovary;salivary gland;intestine;pharynx;colon;blood;skin;prostate;pancreas;lung;bone;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland;bladder;tonsil;stomach; superior cervical ganglion;pons;trigeminal ganglion; 0.04023 0.07442 0.202129237 67.42745931 247.16575 3.39016 C17orf58 0.0821564161266073 0.756737725009856 0.161105858863537 chromosome 17 open reading frame 58 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;tongue;islets of Langerhans;colon;parathyroid;skin;uterus;lung;frontal lobe;larynx;bone;thyroid;placenta;testis;cervix;head and neck;kidney;brain;mammary gland;artery;aorta;stomach; . . . 0.657836546 84.27105449 1262.65696 6.69940 C17orf62 0.00095506373303246 0.580170707962171 0.418874228304797 chromosome 17 open reading frame 62 . . . myocardium;lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; white blood cells;skeletal muscle; 0.09353 . -0.093566408 46.7386176 164.91251 2.80685 C17orf64 0.0138040924538792 0.671115942605402 0.315079964940719 chromosome 17 open reading frame 64 . . . unclassifiable (Anatomical System);medulla oblongata;islets of Langerhans;alveolus;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.14302 . 0.371224249 75.12384996 421.89775 4.29193 C17orf67 2.47630048065969e-05 0.171771407285594 0.8282038297096 chromosome 17 open reading frame 67 . . . . . 0.09391 . 0.613741468 83.06794055 40.25249 1.18313 C17orf74 2.15480274190153e-06 0.468180847047462 0.531816998149796 chromosome 17 open reading frame 74 . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis;brain; . 0.03831 . 0.668743049 84.68388771 855.57884 5.71165 C17orf75 0.980996282608687 0.019000854206571 2.8631847425036e-06 chromosome 17 open reading frame 75 FUNCTION: May have a role in spermatogenesis.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;kidney;aorta; testis - seminiferous tubule;trigeminal ganglion; 0.46962 0.09625 . . 18.50944 0.64029 C17orf77 0.00124631276721521 0.40614443497777 0.592609252255015 chromosome 17 open reading frame 77 . . . unclassifiable (Anatomical System);ovary;kidney; . 0.08014 . 1.196071381 92.92285916 1016.59046 6.13535 C17orf78 0.00407528276770115 0.859905062672311 0.136019654559988 chromosome 17 open reading frame 78 . . . unclassifiable (Anatomical System);colon;kidney;stomach; . 0.28105 . 0.349177632 74.18023119 706.57381 5.28121 C17orf80 2.53809595414424e-07 0.485921178581311 0.514078567609094 chromosome 17 open reading frame 80 . . . medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;ganglion;endometrium;thyroid;germinal center;brain;bladder;tonsil;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;bone marrow; . 0.07388 0.648517637 84.14720453 308.46775 3.73766 C17orf82 7.35000906630045e-05 0.303740765856979 0.696185734052358 chromosome 17 open reading frame 82 . . . . . 0.04284 . . . 1037.24623 6.18580 C17orf89 0.372022649415276 0.479735284321453 0.148242066263271 chromosome 17 open reading frame 89 . . . . . . . . . . . C17orf96 . . . chromosome 17 open reading frame 96 . . . lung;ovary;colon;parathyroid;cervix; . . . . . 2601.34635 9.54465 C17orf97 2.02508049711868e-05 0.15390777493757 0.846071974257459 chromosome 17 open reading frame 97 FUNCTION: May be involved in ATE1-mediated N-terminal arginylation. {ECO:0000250|UniProtKB:Q810M6}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;cartilage;islets of Langerhans;macula lutea;testis;colon;blood;fovea centralis;kidney;brain;mammary gland; . . . 1.15197334 92.52182118 2031.70576 8.29526 C17orf98 0.457750608232201 0.515690650742541 0.0265587410252576 chromosome 17 open reading frame 98 . . . . . . . 0.12689526 63.00424628 681.6827 5.21873 C17orf99 . . . chromosome 17 open reading frame 99 . . . liver;spleen;blood; fetal liver; . . 0.99218692 90.51663128 278.16802 3.57432 C17orf100 0.00377834208828826 0.40489842986544 0.591323228046272 chromosome 17 open reading frame 100 . . . . . . . . . 25.89477 0.84229 C17orf102 0.000161803441056396 0.257657346351104 0.742180850207839 chromosome 17 open reading frame 102 . . . . . . . 1.058333711 91.42486435 562.81928 4.81630 C17orf105 . . . chromosome 17 open reading frame 105 . . . . . . . 0.057118534 57.99716914 27.83919 0.89436 C17orf107 . . . chromosome 17 open reading frame 107 . . . . . . . 0.61192669 82.99716914 1773.93126 7.77974 C17orf112 . . . chromosome 17 open reading frame 112 . . . . . . . . . 0.12143 0.00222 C18orf8 0.999882357316615 0.000117642681028446 2.35631025655791e-12 chromosome 18 open reading frame 8 . . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis;skeletal muscle; 0.08971 . -0.134019284 43.90776126 54.2532 1.47093 C18orf12 . . . chromosome 18 open reading frame 12 . . . . . . . . . . . C18orf15 . . . chromosome 18 open reading frame 15 . . . . . . . . . . . C18orf21 0.00277151818065711 0.79924493473526 0.197983547084083 chromosome 18 open reading frame 21 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;optic nerve;endometrium;bone;testis;germinal center;pineal gland;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;bile duct;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;cingulate cortex; 0.05581 0.10249 0.369407109 74.95281906 42.56206 1.23505 C18orf25 0.901996340401965 0.0978287688270183 0.000174890771016813 chromosome 18 open reading frame 25 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;iris;testis;pineal gland;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;duodenum;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.44755 0.10432 0.238945317 69.20853975 110.61179 2.29043 C18orf32 0.18275268888643 0.645647202170362 0.171600108943208 chromosome 18 open reading frame 32 FUNCTION: May activate the NF-kappa-B signaling pathway. {ECO:0000269|PubMed:12761501}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;oesophagus;bone;thyroid;pituitary gland;testis;dura mater;brain;bladder;pineal gland;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;lens;skeletal muscle;bile duct;breast;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;cervix;kidney;mammary gland;aorta; . 0.16829 . 0.147123112 64.11299835 1.62876 0.05295 C18orf42 . . . chromosome 18 open reading frame 42 FUNCTION: Protein kinase A (PKA)-binding protein. Binds to type II regulatory subunits of protein kinase A (PKA) and may block the A- kinase anchoring protein (AKAP)-mediated subcellular localization of PKA (PubMed:25653177). {ECO:0000269|PubMed:25653177}.; . TISSUE SPECIFICITY: Preferentially expressed in the neural tissues (PubMed:25653177). {ECO:0000269|PubMed:25653177}.; . . . . 0.12325821 62.38499646 8.0804 0.29610 C18orf54 6.01291582416808e-06 0.450797345173227 0.549196641910949 chromosome 18 open reading frame 54 FUNCTION: Might play a role in cell proliferation. {ECO:0000250}.; . . unclassifiable (Anatomical System);hypothalamus;colon;skin;retina;bone marrow;uterus;lung;endometrium;placenta;bone;liver;testis;germinal center; . 0.05794 0.07864 -0.067881249 48.69072895 195.00781 3.02721 C18orf63 . . . chromosome 18 open reading frame 63 . . . . . . . . . 384.62295 4.13262 C18orf65 . . . chromosome 18 open reading frame 65 . . . . . . . . . . . C19orf12 0.667745724331567 0.310136294221687 0.0221179814467469 chromosome 19 open reading frame 12 . DISEASE: Neurodegeneration with brain iron accumulation 4 (NBIA4) [MIM:614298]: A neurodegenerative disorder associated with iron accumulation in the brain, primarily in the basal ganglia. NBIA4 results in speech difficulty, extrapyramidal signs, oromandibular and generalized dystonia, and parkinsonism. Most patients have progressive involvement of the corticospinal tract, with spasticity, hyperreflexia, and extensor plantar responses. {ECO:0000269|PubMed:21981780, ECO:0000269|PubMed:22508347, ECO:0000269|PubMed:22584950, ECO:0000269|PubMed:23269600, ECO:0000269|PubMed:23521069, ECO:0000269|PubMed:23857908}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spastic paraplegia 43, autosomal recessive (SPG43) [MIM:615043]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SP43 is characterized by childhood onset of progressive spasticity affecting the lower and upper limbs. {ECO:0000269|PubMed:23857908}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;muscle;adrenal cortex;blood;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;cervix;head and neck;spleen;kidney;mammary gland;cerebellum; globus pallidus;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.11911 . 0.25917371 70.05779665 113.78286 2.32481 C19orf18 6.22105573112122e-05 0.473131823807634 0.526805965635055 chromosome 19 open reading frame 18 . . . unclassifiable (Anatomical System);uterus;pancreas;lung;bone;testis; . 0.13770 . 0.349177632 74.18023119 6.81724 0.25257 C19orf24 . . . chromosome 19 open reading frame 24 . . . . . 0.06402 . . . 15.97376 0.56605 C19orf25 0.0343632220806308 0.61959798995923 0.346038787960139 chromosome 19 open reading frame 25 . . . unclassifiable (Anatomical System);heart;urinary;skin;uterus;pancreas;whole body;lung;larynx;liver;testis;cervix;head and neck;brain;tonsil;stomach; . . 0.08775 . . 24.53564 0.80658 C19orf33 0.269214271948265 0.635953059059225 0.0948326689925103 chromosome 19 open reading frame 33 . . . unclassifiable (Anatomical System);trophoblast;lymph node;ovary;tongue;salivary gland;intestine;pharynx;colon;blood;skin;uterus;bile duct;prostate;pancreas;lung;cornea;visual apparatus;liver;head and neck;kidney;brain;mammary gland;bladder;stomach; . 0.09309 0.12141 -0.031067188 51.03798066 2398.88072 9.09127 C19orf35 0.00635456730822442 0.743995003497359 0.249650429194416 chromosome 19 open reading frame 35 . . . colon;blood;germinal center;brain; . 0.22523 . . . 1975.46512 8.18714 C19orf38 . . . chromosome 19 open reading frame 38 . . . . . . . 0.591694063 82.45458835 366.41714 4.04947 C19orf43 0.310238874056668 0.617699289237651 0.0720618367056812 chromosome 19 open reading frame 43 . . . lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hypopharynx;duodenum;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;stomach; . 0.17094 0.10400 . . 2.89584 0.10564 C19orf44 4.21594047842148e-07 0.369761634306497 0.630237944099455 chromosome 19 open reading frame 44 . . . unclassifiable (Anatomical System);lymph node;islets of Langerhans;colon;choroid;lens;skin;skeletal muscle;uterus;prostate;lung;bone;thyroid;placenta;testis;spleen;germinal center;kidney;brain;stomach; trigeminal ganglion; 0.05221 . -0.997481928 8.47487615 34.70155 1.05811 C19orf45 2.71015896406554e-15 0.00125950482230326 0.998740495177694 chromosome 19 open reading frame 45 . . . medulla oblongata;optic nerve;lung;macula lutea;testis;colon;fovea centralis;choroid;lens;retina; . 0.10943 . 0.819433854 87.98655343 8217.30567 19.56871 C19orf47 0.802242558770503 0.196624204992893 0.001133236236604 chromosome 19 open reading frame 47 . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;muscle;pharynx;blood;lens;skeletal muscle;lung;cornea;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; cerebellum; 0.15984 . . . 103.77449 2.20069 C19orf48 0.551060129678645 0.396066788664724 0.0528730816566306 chromosome 19 open reading frame 48 . . . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;adrenal cortex;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; prostate;tumor; 0.11070 . 0.970138239 90.23354565 1154.18655 6.47280 C19orf52 0.00198991933916563 0.498766436136437 0.499243644524397 chromosome 19 open reading frame 52 . . . ovary;colon;choroid;fovea centralis;skin;retina;uterus;optic nerve;cerebral cortex;bone;bladder;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;adrenal cortex;lens;pancreas;lung;placenta;macula lutea;spleen;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.11823 . . . 28.53614 0.91460 C19orf53 0.236661551576513 0.645162085257612 0.118176363165875 chromosome 19 open reading frame 53 FUNCTION: May have a potential role in hypercalcemia of malignancy. {ECO:0000250}.; . . ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach; . 0.11852 0.10190 0.103030231 61.2762444 3800.51651 12.10698 C19orf54 0.00126594510562578 0.641600493886704 0.35713356100767 chromosome 19 open reading frame 54 . . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;retina;bone marrow;prostate;pancreas;endometrium;placenta;visual apparatus;liver;testis;spleen;kidney;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;atrioventricular node;trigeminal ganglion; 0.08254 . -0.47017169 23.25430526 63.85473 1.63896 C19orf57 7.18269130933177e-05 0.91292762971521 0.087000543371697 chromosome 19 open reading frame 57 . . . unclassifiable (Anatomical System);uterus;lung;bone;testis;colon;spleen;blood;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06931 0.07027 2.050415361 97.77070064 3198.91219 10.78072 C19orf60 0.249879077699029 0.642082142775503 0.108038779525469 chromosome 19 open reading frame 60 . . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;iris;testis;brain;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; amygdala;whole brain;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;pons;skeletal muscle;prostate;prefrontal cortex;liver;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.11766 . . . 32.748 1.01722 C19orf66 0.930534705136745 0.0691107797580789 0.000354515105176616 chromosome 19 open reading frame 66 . . . smooth muscle;ovary;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);cartilage;pharynx;blood;bile duct;pancreas;lung;adrenal gland;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . -0.295622497 32.61972163 18.09066 0.63129 C19orf67 . . . chromosome 19 open reading frame 67 . . . . . . . . . 57.28221 1.52485 C19orf68 . . . chromosome 19 open reading frame 68 . . . uterus;iris;colon;mammary gland; . . . . . 25.02193 0.82024 C19orf70 0.0159221835622921 0.69982023489203 0.284257581545678 chromosome 19 open reading frame 70 FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Constituent of mature MICOS complex, it is required for the formation of cristae junction (CJ) and maintenance of cristae morphology. Required for the incorporation of MINOS1/MIC10 into the MICOS complex. {ECO:0000269|PubMed:25997101}.; . . myocardium;medulla oblongata;ovary;salivary gland;developmental;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;iris;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;trophoblast;heart;islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;alveolus;liver;spleen;kidney;mammary gland;stomach;cerebellum; heart;liver;testis;cingulate cortex; . 0.11386 -0.053113545 49.38664779 5.81355 0.21905 C19orf71 . . . chromosome 19 open reading frame 71 . . . unclassifiable (Anatomical System);lymph node;thyroid;placenta;muscle;testis;skin;stomach; . . . 0.926041233 89.65557915 999.90286 6.09089 C19orf73 0.48401312075747 0.435651858060013 0.0803350211825174 chromosome 19 open reading frame 73 . . . . . . . 0.657836546 84.27105449 52.91372 1.44329 C19orf81 . . . chromosome 19 open reading frame 81 . . . . . . . . . 72.37299 1.77247 C19orf84 . . . chromosome 19 open reading frame 84 . . . . . . . . . 2524.65974 9.36832 C20orf24 0.856745481043852 0.140987923716808 0.00226659523934009 chromosome 20 open reading frame 24 . . . lymphoreticular;smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; whole brain;whole blood;bone marrow; 0.07763 . -0.229483771 36.86010852 4.10648 0.15024 C20orf27 0.0270989162488399 0.79318465459779 0.17971642915337 chromosome 20 open reading frame 27 . . . medulla oblongata;ovary;salivary gland;colon;choroid;skin;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;urinary;blood;lens;bile duct;pancreas;lung;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;caudate nucleus;pons;trigeminal ganglion; 0.16010 . -0.271755481 34.31823543 22.65805 0.75819 C20orf78 . . . chromosome 20 open reading frame 78 . . . lung;placenta;testis; superior cervical ganglion; 0.10022 . . . 35.87654 1.07798 C20orf85 1.38449977889469e-05 0.228240626859525 0.771745528142686 chromosome 20 open reading frame 85 . . . . . 0.19124 . 0.61555716 83.13871196 524.33074 4.67264 C20orf96 7.45279920330834e-13 0.0177925167705778 0.982207483228677 chromosome 20 open reading frame 96 . . . unclassifiable (Anatomical System);ovary;colon;bone marrow;uterus;breast;prostate;lung;bone;thyroid;visual apparatus;liver;testis;spleen;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle;cerebellum; 0.02739 . -0.314027422 31.9297004 25.57746 0.83421 C20orf141 0.000122910761361037 0.223231285349471 0.776645803889168 chromosome 20 open reading frame 141 . . . . . 0.00570 . 0.415317661 76.81056853 27.70366 0.89081 C20orf144 0.00309357257059548 0.36888568736388 0.628020740065525 chromosome 20 open reading frame 144 . . TISSUE SPECIFICITY: Preferentially expressed in the testis. {ECO:0000269|Ref.1}.; . . 0.24801 . . . 1107.91755 6.36282 C20orf166-AS1 . . . C20orf166 antisense RNA 1 . . . . . . . . . . . C20orf173 . . . chromosome 20 open reading frame 173 . . . unclassifiable (Anatomical System); . 0.05904 . 0.858082312 88.55862232 383.42336 4.12918 C20orf181 . . . chromosome 20 open reading frame 181 . . . . . . . . . . . C20orf187 . . . chromosome 20 open reading frame 187 . . . . . 0.01771 . . . 2.90826 0.10587 C20orf194 0.00600469217397855 0.993995295058299 1.27677223359567e-08 chromosome 20 open reading frame 194 FUNCTION: May act as an effector for ARL3.; . . ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;oesophagus;larynx;thyroid;iris;testis;brain;pineal gland;unclassifiable (Anatomical System);heart;hypothalamus;muscle;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach;aorta; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.42872 . -0.812021021 12.07242274 478.23078 4.51532 C20orf195 0.000298557497544344 0.569512162812135 0.430189279690321 chromosome 20 open reading frame 195 . . . . . 0.17115 0.10823 -0.843147538 11.2762444 48.3585 1.35563 C20orf196 0.333004444219793 0.605089947525651 0.0619056082545567 chromosome 20 open reading frame 196 . . . unclassifiable (Anatomical System);lymph node;heart;pineal body;blood;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;prostate;optic nerve;lung;nasopharynx;bone;macula lutea;testis;germinal center;kidney;aorta;stomach; . 0.06887 . 0.793752871 87.40268931 126.31818 2.44751 C20orf197 0.0552321459200376 0.704996544762169 0.239771309317794 chromosome 20 open reading frame 197 . . . unclassifiable (Anatomical System);kidney; . 0.04902 . 0.103030231 61.2762444 7.58678 0.28115 C20orf202 . . . chromosome 20 open reading frame 202 . . . . . . . 0.479642105 78.95140363 123.01655 2.41564 C20orf203 . . . chromosome 20 open reading frame 203 . . TISSUE SPECIFICITY: Expressed most abundantly in the brain at protein level. Present in cortex, cerebellum and midbrain. Found in neurons. Elevated expressions detected in Alzheimer brain samples. Also expressed in testis. {ECO:0000269|PubMed:20376170}.; . . . . . . . . C21orf2 0.0135303834414265 0.864790118406216 0.121679498152357 chromosome 21 open reading frame 2 FUNCTION: May play roles in cilia formation and/or maintenance (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000250, ECO:0000269|PubMed:21834987}.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;muscle;blood;pancreas;lung;nasopharynx;placenta;hippocampus;liver;spleen;kidney;mammary gland;thymus; . 0.07367 0.10413 1.418384579 94.89266336 528.42212 4.69156 C21orf33 0.00117212805596081 0.84223442595206 0.156593445991979 chromosome 21 open reading frame 33 . . TISSUE SPECIFICITY: Ubiquitous, but strongly expressed in heart and skeletal muscle.; lymphoreticular;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cerebellum cortex;lens;lung;placenta;macula lutea;visual apparatus;spleen;cervix;kidney;mammary gland;stomach; whole brain;thalamus;cerebellum peduncles;liver;globus pallidus;kidney;skeletal muscle;cerebellum; 0.11230 0.20950 0.218717575 68.27081859 543.78605 4.74553 C21orf58 3.74077237894162e-09 0.0520055404396974 0.94799445581953 chromosome 21 open reading frame 58 . . TISSUE SPECIFICITY: Expressed in skin and fetal lung.; unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;developmental;colon;blood;skeletal muscle;bone marrow;breast;uterus;lung;endometrium;larynx;duodenum;testis;head and neck;cervix;brain;peripheral nerve; . 0.08455 . 0.308721233 72.59966973 4142.67552 12.77224 C21orf59 0.000141358025835822 0.859450390763364 0.1404082512108 chromosome 21 open reading frame 59 FUNCTION: May play a role in motile cilia function, possibly by acting on dynein arm assembly. {ECO:0000269|PubMed:24094744}.; DISEASE: Ciliary dyskinesia, primary, 26 (CILD26) [MIM:615500]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia. Patients may exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:24094744}. Note=The disease is caused by mutations affecting the gene represented in this entry. Cilia in nasal epithelia show the absence of both outer and inner dynein- arm components and complete paralysis.; . lymphoreticular;medulla oblongata;ovary;salivary gland;developmental;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;muscle;blood;lens;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;cerebellum peduncles;testis;globus pallidus;pons;trigeminal ganglion; 0.16639 . -0.071520315 48.34866714 5.77442 0.21671 C21orf62 0.0576278443415897 0.711600291405547 0.230771864252863 chromosome 21 open reading frame 62 . . . . . 0.05385 . -0.227663163 37.11370606 19.84867 0.67673 C21orf62-AS1 . . . C21orf62 antisense RNA 1 . . . . . 0.07624 . . . . . C21orf91 0.00484582012569912 0.882241759357395 0.112912420516906 chromosome 21 open reading frame 91 . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;appendix;testis;ciliary ganglion;trigeminal ganglion; 0.32383 0.09777 0.793752871 87.40268931 2323.15622 8.92517 C21orf91-OT1 . . . C21orf91 overlapping transcript 1 . . . . . . . . . . . C21orf140 . . . chromosome 21 open reading frame 140 . . . . . . . . . 50.29989 1.39464 C22orf15 0.0813466462823027 0.755755821212879 0.162897532504818 chromosome 22 open reading frame 15 . . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;urinary;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach;thymus; . 0.16620 . 0.591694063 82.45458835 128.31773 2.46863 C22orf23 2.51126071127562e-06 0.499700892029335 0.500296596709954 chromosome 22 open reading frame 23 . . . unclassifiable (Anatomical System);medulla oblongata;heart;ovary;cartilage;parathyroid;skin;uterus;pancreas;prostate;lung;placenta;testis;spleen;kidney; . 0.04188 . 0.238945317 69.20853975 219.82409 3.20745 C22orf24 1.2513284860103e-05 0.117884524571571 0.882102962143569 chromosome 22 open reading frame 24 . . . unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.02212 0.04730 0.237127192 68.98443029 1005.6535 6.10355 C22orf29 5.80709519233968e-06 0.259153938354194 0.740840254550614 chromosome 22 open reading frame 29 FUNCTION: Could induce apoptosis in a BH3 domain-dependent manner. The direct interaction network of Bcl-2 family members may play a key role in modulation BOP intrinsic apoptotic signaling activity. {ECO:0000269|PubMed:23055042}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:23055042}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;liver;head and neck;kidney;stomach;thymus; . 0.07427 0.09171 0.396906589 76.30927105 170.89416 2.85158 C22orf31 2.31877898310653e-05 0.49912058082368 0.500856231386489 chromosome 22 open reading frame 31 . . . unclassifiable (Anatomical System);lung;ovary;placenta;testis;parathyroid; skeletal muscle; 0.39454 . 0.240763792 69.36777542 853.85828 5.70586 C22orf34 . . . chromosome 22 open reading frame 34 . . . . . 0.11977 . . . 79.24792 1.88137 C22orf39 3.69004562054558e-07 0.0563832536638846 0.943616377331553 chromosome 22 open reading frame 39 . . . unclassifiable (Anatomical System);medulla oblongata;lung;synovium;hypothalamus;bone;placenta;testis;colon;kidney;lens;brain;stomach;peripheral nerve; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14785 . . . 63.1989 1.62667 C22orf42 1.42223733805271e-06 0.3881843570856 0.611814220677062 chromosome 22 open reading frame 42 . . . . . . . 1.039913547 91.25973107 120.54665 2.39169 C22orf46 . . . chromosome 22 open reading frame 46 . . . . . . . 0.435547893 77.45340882 99.87876 2.16545 CA1 3.77366091172667e-05 0.603950956395979 0.396011306994904 carbonic anhydrase I FUNCTION: Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea. {ECO:0000269|PubMed:10550681}.; . . unclassifiable (Anatomical System);uterus;frontal lobe;cartilage;heart;colon;blood;kidney;skin;stomach; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;bone marrow; 0.39450 0.16413 0.571462851 81.99457419 275.69616 3.55616 CA2 0.100369922719721 0.865695637082174 0.0339344401981052 carbonic anhydrase II FUNCTION: Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6. {ECO:0000250, ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:11831900, ECO:0000269|PubMed:15990874}.; DISEASE: Osteopetrosis, autosomal recessive 3 (OPTB3) [MIM:259730]: A rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Recessive osteopetrosis commonly manifests in early infancy with macrocephaly, feeding difficulties, evolving blindness and deafness, bone marrow failure, severe anemia, and hepatosplenomegaly. Deafness and blindness are generally thought to represent effects of pressure on nerves. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation. {ECO:0000269|PubMed:15300855, ECO:0000269|PubMed:1542674, ECO:0000269|PubMed:1928091, ECO:0000269|PubMed:8834238, ECO:0000269|PubMed:9143915}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;larynx;thyroid;bone;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;trophoblast;heart;cartilage;hypothalamus;spinal cord;blood;lens;breast;pancreas;pia mater;lung;trabecular meshwork;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach; whole brain;amygdala;occipital lobe;medulla oblongata;thalamus;trachea;hypothalamus;caudate nucleus;kidney;parietal lobe;bone marrow; 0.23005 0.37216 -0.139478553 43.29440906 163.06398 2.78740 CA3 4.68813817881995e-05 0.651352236783089 0.348600881835122 carbonic anhydrase III FUNCTION: Reversible hydration of carbon dioxide.; . TISSUE SPECIFICITY: Muscle specific.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;larynx;testis;unclassifiable (Anatomical System);heart;tongue;muscle;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;alveolus;head and neck;kidney;stomach; thyroid;trigeminal ganglion;skeletal muscle; 0.22413 0.24844 0.327131069 73.27199811 3799.0179 12.09617 CA3-AS1 . . . CA3 antisense RNA 1 . . . . . . . . . . . CA4 0.0108088499819045 0.946807511232314 0.0423836387857817 carbonic anhydrase IV FUNCTION: Reversible hydration of carbon dioxide. May stimulate the sodium/bicarbonate transporter activity of SLC4A4 that acts in pH homeostasis. It is essential for acid overload removal from the retina and retina epithelium, and acid release in the choriocapillaris in the choroid. {ECO:0000269|PubMed:15563508}.; . TISSUE SPECIFICITY: Expressed in the endothelium of the choriocapillaris in eyes (at protein level). Not expressed in the retinal epithelium at detectable levels. {ECO:0000269|PubMed:15563508}.; unclassifiable (Anatomical System);heart;cartilage;colon;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;placenta;macula lutea;testis;kidney;spinal ganglion;brain;stomach; superior cervical ganglion;cerebellum peduncles;thyroid;trigeminal ganglion;cerebellum; 0.08533 0.21640 0.218717575 68.27081859 99.7081 2.16362 CA5A 0.0107231379680564 0.946445827093308 0.0428310349386352 carbonic anhydrase VA, mitochondrial FUNCTION: Reversible hydration of carbon dioxide. Low activity.; DISEASE: Hyperammonemia due to carbonic anhydrase VA deficiency (CA5AD) [MIM:615751]: An autosomal recessive inborn error of metabolism, clinically characterized by infantile hyperammonemic encephalopathy. Metabolic abnormalities include hypoglycemia, hyperlactatemia, metabolic acidosis and respiratory alkalosis. {ECO:0000269|PubMed:24530203}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);liver;spleen;germinal center; dorsal root ganglion;superior cervical ganglion;liver;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11209 0.10917 -0.001743238 53.85114414 62.38928 1.61312 CA5AP1 . . . carbonic anhydrase VA pseudogene 1 . . . . . . . . . . . CA5B 0.00331242978898846 0.829097911771415 0.167589658439597 carbonic anhydrase VB, mitochondrial FUNCTION: Reversible hydration of carbon dioxide.; . TISSUE SPECIFICITY: Strongest expression in heart, pancreas, kidney, placenta, lung, and skeletal muscle. Not expressed in liver.; unclassifiable (Anatomical System);uterus;prostate;heart;nasopharynx;placenta;kidney;germinal center;brain;skin;skeletal muscle; superior cervical ganglion;temporal lobe;appendix;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.08747 . -0.073340031 48.11866006 33.76923 1.04029 CA5BP1 . . . carbonic anhydrase VB pseudogene 1 . . . . . 0.03143 . . . . . CA6 0.00802362076493995 0.929774522091703 0.0622018571433569 carbonic anhydrase VI FUNCTION: Reversible hydration of carbon dioxide. Its role in saliva is unknown.; . TISSUE SPECIFICITY: Major constituent of saliva.; unclassifiable (Anatomical System); superior cervical ganglion;salivary gland; 0.13243 0.11366 0.773521534 87.06062751 6002.37709 16.16463 CA7 0.77537597388821 0.223006857429607 0.0016171686821831 carbonic anhydrase VII FUNCTION: Reversible hydration of carbon dioxide.; . . unclassifiable (Anatomical System);colon;kidney;brain;stomach; globus pallidus;ciliary ganglion;atrioventricular node; 0.33625 0.12971 -0.05129383 49.75819769 5.07717 0.18740 CA8 0.783927466808709 0.215775274635827 0.000297258555463627 carbonic anhydrase VIII FUNCTION: Does not have a carbonic anhydrase catalytic activity.; DISEASE: Cerebellar ataxia, mental retardation, and dysequilibrium syndrome 3 (CMARQ3) [MIM:613227]: A congenital cerebellar ataxia associated with dysarthia, quadrupedal gait and mental retardation. {ECO:0000269|PubMed:19461874}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);breast;uterus;pancreas;lung;frontal lobe;islets of Langerhans;placenta;testis;brain;skin; superior cervical ganglion;trigeminal ganglion;skeletal muscle;cerebellum; 0.43521 0.13588 -0.007201372 53.19061099 79.99996 1.89165 CA9 4.38501915523555e-07 0.603124583144944 0.396874978353141 carbonic anhydrase IX FUNCTION: Reversible hydration of carbon dioxide. Participates in pH regulation. May be involved in the control of cell proliferation and transformation. Appears to be a novel specific biomarker for a cervical neoplasia. {ECO:0000269|PubMed:18703501}.; . TISSUE SPECIFICITY: Expressed primarily in carcinoma cells lines. Expression is restricted to very few normal tissues and the most abundant expression is found in the epithelial cells of gastric mucosa.; . . 0.37275 0.16262 0.086440867 60.47416844 3464.31922 11.32962 CA10 0.973117501696163 0.0268757579395459 6.74036429114539e-06 carbonic anhydrase X FUNCTION: Does not have a catalytic activity.; . TISSUE SPECIFICITY: Strong expression in brain and central nervous system. {ECO:0000269|PubMed:11311946}.; unclassifiable (Anatomical System);cerebellum cortex;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;whole body;frontal lobe;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;testis;kidney;pineal gland;brain; amygdala;dorsal root ganglion;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;temporal lobe;atrioventricular node;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.40823 0.09764 -0.582225231 18.44184949 63.01651 1.62408 CA11 0.976097038480165 0.0238979201537965 5.04136603798991e-06 carbonic anhydrase XI FUNCTION: Does not have a catalytic activity.; . TISSUE SPECIFICITY: Expressed abundantly in the brain with moderate expression also present in spinal cord and thyroid.; colon;fovea centralis;skin;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;larynx;synovium;testis;germinal center;artery;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pineal body;muscle;blood;lung;hippocampus;macula lutea;head and neck;aorta;peripheral nerve;cerebellum; amygdala;whole brain;medulla oblongata;occipital lobe;superior cervical ganglion;cerebellum peduncles;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.70627 0.11276 -0.251530012 35.42108988 11.89854 0.43130 CA12 9.91295957492359e-09 0.168655224815075 0.831344765271965 carbonic anhydrase XII FUNCTION: Reversible hydration of carbon dioxide.; . TISSUE SPECIFICITY: Highly expressed in colon, kidney, prostate, intestine and activated lymphocytes. Expressed at much higher levels in the renal cell cancers than in surrounding normal kidney tissue. Moderately expressed in pancreas, ovary and testis.; smooth muscle;ovary;rectum;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;tongue;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;pia mater;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;smooth muscle;tongue;pons;atrioventricular node;caudate nucleus;skin;skeletal muscle;subthalamic nucleus;uterus corpus;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion; 0.21265 0.12840 -0.622676946 17.30950696 40.85482 1.19656 CA13 0.000339444426113696 0.822449644821836 0.177210910752051 carbonic anhydrase XIII FUNCTION: Reversible hydration of carbon dioxide.; . TISSUE SPECIFICITY: Expressed in thymus, small intestine, spleen, prostate, ovary, colon and testis. {ECO:0000269|PubMed:14600151}.; unclassifiable (Anatomical System);lung;ovary;adrenal gland;placenta;liver;parathyroid;spleen;stomach; . 0.14745 0.10170 0.637604436 83.77565464 79.88684 1.88891 CA14 1.43471644090703e-09 0.197529638667084 0.8024703598982 carbonic anhydrase XIV FUNCTION: Reversible hydration of carbon dioxide.; . TISSUE SPECIFICITY: High expression in all parts of the central nervous system and lower expression in adult liver, heart, small intestine, colon, kidney, urinary bladder and skeletal muscle.; . . 0.19548 0.09497 -0.60427181 17.74593064 39.4025 1.16480 CA15P1 . . . carbonic anhydrase XV, pseudogene 1 . . . . . . . . . . . CA15P2 . . . carbonic anhydrase XV, pseudogene 2 . . . . . . . . . . . CA15P3 . . . carbonic anhydrase XV, pseudogene 3 . . . . . . . . . . . CAAP1 0.708931875446252 0.287649204686477 0.00341891986727055 caspase activity and apoptosis inhibitor 1 FUNCTION: Anti-apoptotic protein that modulates a caspase-10 dependent mitochondrial caspase-3/9 feedback amplification loop. {ECO:0000269|PubMed:21980415}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:21980415}.; . . 0.21584 0.10336 0.238945317 69.20853975 505.4594 4.61378 CAB39 0.0621795964046071 0.921903161684767 0.0159172419106263 calcium binding protein 39 FUNCTION: Component of a complex that binds and activates STK11/LKB1. In the complex, required to stabilize the interaction between CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta) and STK11/LKB1. {ECO:0000269|PubMed:19892943}.; . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; dorsal root ganglion;occipital lobe;subthalamic nucleus;temporal lobe;globus pallidus;pons;whole blood;cingulate cortex;parietal lobe; 0.65337 0.11791 -0.05129383 49.75819769 29.39386 0.94016 CAB39L 0.0164205539395948 0.959558434519989 0.0240210115404163 calcium binding protein 39 like FUNCTION: Component of a complex that binds and activates STK11/LKB1. In the complex, required to stabilize the interaction between CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta) and STK11/LKB1 (By similarity). {ECO:0000250}.; . . colon;parathyroid;skin;retina;uterus;prostate;whole body;thyroid;bone;testis;dura mater;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;hypothalamus;spinal cord;skeletal muscle;pancreas;pia mater;lung;placenta;liver;kidney;mammary gland;stomach;aorta; prostate;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.42751 0.10919 -0.626318434 17.03231894 17.44798 0.61208 CAB39P1 . . . calcium binding protein 39 pseudogene 1 . . . . . . . . . . . CABIN1 8.54365661226281e-08 0.999999900991535 1.35718986192055e-08 calcineurin binding protein 1 FUNCTION: May be required for replication-independent chromatin assembly. May serve as a negative regulator of T-cell receptor (TCR) signaling via inhibition of calcineurin. Inhibition of activated calcineurin is dependent on both PKC and calcium signals. Acts as a negative regulator of p53/TP53 by keeping p53 in an inactive state on chromatin at promoters of a subset of it's target genes. {ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:9655484}.; . TISSUE SPECIFICITY: Widely expressed in different tissues. {ECO:0000269|PubMed:9655484}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; amygdala;cerebellum peduncles;thyroid;prefrontal cortex;globus pallidus;caudate nucleus;pons;cingulate cortex;skeletal muscle;cerebellum; . . -0.661638049 15.95305497 1310.30766 6.81090 CABLES1 0.445044394222778 0.554681990100601 0.000273615676620849 Cdk5 and Abl enzyme substrate 1 FUNCTION: Cyclin-dependent kinase binding protein. Enhances cyclin-dependent kinase tyrosine phosphorylation by nonreceptor tyrosine kinases, such as that of CDK5 by activated ABL1, which leads to increased CDK5 activity and is critical for neuronal development, and that of CDK2 by WEE1, which leads to decreased CDK2 activity and growth inhibition. Positively affects neuronal outgrowth. Plays a role as a regulator for p53/p73-induced cell death (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in breast, pancreas, colon, head and neck (at protein level). Strongly decreased in more than half of cases of atypical endometrial hyperplasia and in more than 90% of endometrial cancers. {ECO:0000269|PubMed:11585773, ECO:0000269|PubMed:14729625}.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;blood;lens;skin;retina;prostate;optic nerve;lung;adrenal gland;larynx;placenta;visual apparatus;liver;head and neck;kidney;brain;stomach; . 0.26184 0.10942 . . 1905.02643 8.03197 CABLES2 0.000167846578276169 0.882730159926653 0.117101993495071 Cdk5 and Abl enzyme substrate 2 FUNCTION: Unknown. Probably involved in G1-S cell cycle transition.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;fovea centralis;skin;skeletal muscle;retina;uterus;prostate;lung;frontal lobe;larynx;placenta;macula lutea;visual apparatus;liver;testis;head and neck;spleen;kidney;brain;stomach; testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19499 0.12111 -0.067881249 48.69072895 837.55114 5.66803 CABP1 0.994401234059643 0.0055980587870285 7.07153328531873e-07 calcium binding protein 1 FUNCTION: Modulates calcium-dependent activity of inositol 1,4,5- triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling. Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels. Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but resulting in an opposit effects on channel function. Suppresses the calcium-dependent inactivation of CACNA1D (By similarity). Inhibits TRPC5 channels. Prevents NMDA receptor- induced cellular degeneration (By similarity). {ECO:0000250, ECO:0000269|PubMed:11865310, ECO:0000269|PubMed:14570872, ECO:0000269|PubMed:15140941, ECO:0000269|PubMed:15895247, ECO:0000269|PubMed:15980432}.; . TISSUE SPECIFICITY: Retina and brain. Somatodendritic compartment of neurons. Calbrain was found exclusively in brain where it is abundant in the hippocampus, habenular area in the epithalamus and in the cerebellum.; unclassifiable (Anatomical System);hypothalamus;pineal body;colon;fovea centralis;choroid;lens;retina;optic nerve;lung;frontal lobe;macula lutea;testis;kidney;pineal gland;brain; amygdala;whole brain;occipital lobe;medulla oblongata;temporal lobe;pons;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.31275 . . . 9.98381 0.36583 CABP2 0.0212095370479509 0.907102508116667 0.0716879548353816 calcium binding protein 2 . . TISSUE SPECIFICITY: Retina. {ECO:0000269|PubMed:11108966}.; optic nerve; dorsal root ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.08504 0.11476 0.283038099 71.26680821 4181.66942 12.84858 CABP4 1.84429317413404e-05 0.690062738415876 0.309918818652383 calcium binding protein 4 FUNCTION: Involved in normal synaptic function through regulation of Ca(2+) influx and neurotransmitter release in photoreceptor synaptic terminals and in auditory transmission. Modulator of CACNA1D and CACNA1F, suppressing the calcium-dependent inactivation and shifting the activation range to more hyperpolarized voltages (By similarity). {ECO:0000250}.; DISEASE: Cone-rod synaptic disorder, congenital non-progressive (CRSD) [MIM:610427]: A non-progressive retinal disorder characterized by stable low vision, nystagmus, photophobia, a normal or near-normal fundus appearance, and no night blindness. {ECO:0000269|PubMed:16960802}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in retina and in the inner hair cells (IHC) of the cochlea.; unclassifiable (Anatomical System);uterus;liver;spleen;choroid; superior cervical ganglion;ciliary ganglion;kidney; 0.18229 0.11212 -0.047654689 50.22410946 54.31901 1.47217 CABP5 0.00422080325588394 0.864684113891402 0.131095082852714 calcium binding protein 5 FUNCTION: Inhibits calcium-dependent inactivation of L-type calcium channel and shifts voltage dependence of activation to more depolarized membrane potentials. Involved in the transmission of light signals (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Retina. {ECO:0000269|PubMed:11108966}.; optic nerve;macula lutea;fovea centralis;choroid;lens;skeletal muscle;retina; dorsal root ganglion;occipital lobe;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;parietal lobe; 0.35156 0.12664 1.216305531 93.13517339 1299.91454 6.78329 CABP7 0.89963339213873 0.0994632910537944 0.000903316807475256 calcium binding protein 7 FUNCTION: Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. {ECO:0000250}.; . . colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;kidney;mammary gland; superior cervical ganglion; 0.23461 0.11809 -0.075159878 47.78839349 10.62062 0.38641 CABS1 0.0541377125884707 0.701809318465452 0.244052968946077 calcium binding protein, spermatid associated 1 . . . medulla oblongata;lung;hippocampus;testis; testis - interstitial;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion; 0.22450 . 0.328949044 73.41354093 1425.99869 7.05413 CABYR 0.000210501288958305 0.733497463016404 0.266292035694637 calcium binding tyrosine phosphorylation regulated FUNCTION: May function as a regulator of both motility- and head- associated functions such as capacitation and the acrosome reaction. Isoform 1 binds calcium in vitro. Isoform 2 and isoform 6 probably bind calcium. Isoform 3 and isoform 5 do not bind calcium in vitro. Isoform 4 probably does not bind calcium.; . TISSUE SPECIFICITY: Expressed in elongating spermatids and spermatozoa (at protein level). Isoform 1 is expressed in testis. Isoform 3 and isoform 5 are also expressed in brain, pancreas and numerous brain tumors. {ECO:0000269|PubMed:11820818, ECO:0000269|PubMed:15752768, ECO:0000269|PubMed:16139264}.; unclassifiable (Anatomical System);medulla oblongata;lung;frontal lobe;heart;testis;colon;kidney; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.03207 0.05458 0.106667882 61.73036093 134.93156 2.52625 CABYRP1 . . . calcium binding tyrosine phosphorylation regulated pseudogene 1 . . . . . . . . . . . CACD . . . central areolar choroidal dystrophy . . . . . . . . . . . CACFD1 0.00574676872876184 0.724184596161631 0.270068635109607 calcium channel flower domain containing 1 . . . . . 0.18701 . -0.271755481 34.31823543 58.30376 1.54667 CACHD1 0.838036969203847 0.161963028931134 1.86501827236635e-09 cache domain containing 1 FUNCTION: May regulate voltage-dependent calcium channels. {ECO:0000250}.; . . smooth muscle;ovary;salivary gland;developmental;colon;parathyroid;skin;retina;prostate;whole body;larynx;bone;thyroid;iris;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;pancreas;pia mater;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.66214 0.10885 -1.741783094 2.418023119 764.17371 5.47815 CACNA1A 0.999999999776293 2.23706856981785e-10 1.12006530976621e-27 calcium voltage-gated channel subunit alpha1 A FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by the funnel toxin (Ftx) and by the omega-agatoxin- IVA (omega-Aga-IVA). They are however insensitive to dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).; DISEASE: Spinocerebellar ataxia 6 (SCA6) [MIM:183086]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA6 is an autosomal dominant cerebellar ataxia (ADCA), mainly caused by expansion of a CAG repeat in the coding region of CACNA1A. There seems to be a correlation between the repeat number and earlier onset of the disorder. {ECO:0000269|PubMed:16325861, ECO:0000269|PubMed:20682717, ECO:0000269|PubMed:8988170, ECO:0000269|PubMed:9345107}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Migraine, familial hemiplegic, 1 (FHM1) [MIM:141500]: A subtype of migraine with aura associated with ictal hemiparesis and, in some families, cerebellar ataxia and atrophy. Migraine is a disabling symptom complex of periodic headaches, usually temporal and unilateral. Headaches are often accompanied by irritability, nausea, vomiting and photophobia, preceded by constriction of the cranial arteries. Migraine with aura is characterized by recurrent attacks of reversible neurological symptoms (aura) that precede or accompany the headache. Aura may include a combination of sensory disturbances, such as blurred vision, hallucinations, vertigo, numbness and difficulty in concentrating and speaking. {ECO:0000269|PubMed:10408532, ECO:0000269|PubMed:11409427, ECO:0000269|PubMed:11439943, ECO:0000269|PubMed:15032980, ECO:0000269|PubMed:18400034, ECO:0000269|PubMed:8898206}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Episodic ataxia 2 (EA2) [MIM:108500]: An autosomal dominant disorder characterized by acetozolamide-responsive attacks of ataxia, migraine-like symptoms, interictal nystagmus, and cerebellar atrophy. {ECO:0000269|PubMed:10987655, ECO:0000269|PubMed:11176968, ECO:0000269|PubMed:11723274, ECO:0000269|PubMed:12420090, ECO:0000269|PubMed:14718690, ECO:0000269|PubMed:15173248, ECO:0000269|PubMed:15293273, ECO:0000269|PubMed:18602318, ECO:0000269|PubMed:19232643, ECO:0000269|PubMed:20129625, ECO:0000269|PubMed:21696515, ECO:0000269|PubMed:8898206, ECO:0000269|PubMed:9302278}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Brain specific; mainly found in cerebellum, cerebral cortex, thalamus and hypothalamus. Expressed in the small cell lung carcinoma cell line SCC-9. No expression in heart, kidney, liver or muscle. Purkinje cells contain predominantly P- type VSCC, the Q-type being a prominent calcium current in cerebellar granule cells. {ECO:0000269|PubMed:1335101}.; unclassifiable (Anatomical System);amygdala;ovary;islets of Langerhans;blood;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;optic nerve;lung;frontal lobe;macula lutea;testis;germinal center;kidney;brain; amygdala;superior cervical ganglion;cerebellum peduncles;pons;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.58636 0.55905 -1.782298694 2.270582685 4523.77922 13.50808 CACNA1B 0.982603443138066 0.0173965568619229 1.08544589481033e-14 calcium voltage-gated channel subunit alpha1 B FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1B gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin- IIIA (omega-Aga-IIIA). They are however insensitive to dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons.; DISEASE: Dystonia 23 (DYT23) [MIM:614860]: A form of dystonia, a disorder defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. DYT23 is an autosomal dominant dystonia affecting the face, neck, limbs. Some DYT23 patients manifest generalized myoclonus in addition to progressive action-induced multifocal dystonia. {ECO:0000269|PubMed:25296916}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform Alpha-1b-1 and isoform Alpha-1b-2 are expressed in the central nervous system, but not in skeletal muscle or aorta.; unclassifiable (Anatomical System);lung;frontal lobe;ovary;visual apparatus;brain;skeletal muscle; atrioventricular node;kidney;parietal lobe; 0.36417 0.21506 . . 6649.54659 17.26658 CACNA1C 0.99999843310185 1.5668981500091e-06 4.36769282620476e-21 calcium voltage-gated channel subunit alpha1 C FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1C gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin- GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. The various isoforms display marked differences in the sensitivity to DHP compounds. Binding of calmodulin or CABP1 at the same regulatory sites results in an opposit effects on the channel function. {ECO:0000269|PubMed:12176756, ECO:0000269|PubMed:17071743, ECO:0000269|PubMed:7737988, ECO:0000269|PubMed:8392192, ECO:0000269|PubMed:9013606, ECO:0000269|PubMed:9607315}.; DISEASE: Timothy syndrome (TS) [MIM:601005]: Disorder characterized by multiorgan dysfunction including lethal arrhythmias, webbing of fingers and toes, congenital heart disease, immune deficiency, intermittent hypoglycemia, cognitive abnormalities and autism. {ECO:0000269|PubMed:15454078, ECO:0000269|PubMed:15863612, ECO:0000269|PubMed:25260352}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Brugada syndrome 3 (BRGDA3) [MIM:611875]: A heart disease characterized by the association of Brugada syndrome with shortened QT intervals. Brugada syndrome is a tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs, the individual will faint and may die in a few minutes if the heart is not reset. {ECO:0000269|PubMed:17224476}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, heart, jejunum, ovary, pancreatic beta-cells and vascular smooth muscle. Overall expression is reduced in atherosclerotic vascular smooth muscle. {ECO:0000269|PubMed:12176756, ECO:0000269|PubMed:17071743, ECO:0000269|PubMed:8392192}.; unclassifiable (Anatomical System);ovary;colon;uterus;prostate;whole body;lung;frontal lobe;placenta;thyroid;testis;spleen;brain;gall bladder;cerebellum; superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.66288 0.13071 -2.087541484 1.574663836 257.23512 3.44970 CACNA1C-AS1 . . . CACNA1C antisense RNA 1 . . . . . . . . . . . CACNA1C-AS2 . . . CACNA1C antisense RNA 2 . . . . . . . . . . . CACNA1C-AS3 . . . CACNA1C antisense RNA 3 . . . . . . . . . . . CACNA1C-AS4 . . . CACNA1C antisense RNA 4 . . . . . . . . . . . CACNA1C-IT1 . . . CACNA1C intronic transcript 1 . . . . . . . . . . . CACNA1C-IT2 . . . CACNA1C intronic transcript 2 . . . . . . . . . . . CACNA1C-IT3 . . . CACNA1C intronic transcript 3 . . . . . . . . . . . CACNA1D 0.99999999998943 1.05701389150024e-11 1.33783731932459e-31 calcium voltage-gated channel subunit alpha1 D FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1D gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin- GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). {ECO:0000269|PubMed:18482979}.; DISEASE: Sinoatrial node dysfunction and deafness (SANDD) [MIM:614896]: A disease characterized by congenital severe to profound deafness without vestibular dysfunction, associated with episodic syncope due to intermittent pronounced bradycardia. {ECO:0000269|PubMed:21131953}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Primary aldosteronism, seizures, and neurologic abnormalities (PASNA) [MIM:615474]: A disorder characterized by hypertension, hypokalemia, and high aldosterone levels with low plasma renin activity and an elevated aldosterone/renin ratio. Other features include generalized seizures, cerebral palsy, spasticity, intellectual disability, and developmental delay. {ECO:0000269|PubMed:23913001}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in pancreatic islets and in brain, where it has been seen in cerebral cortex, hippocampus, basal ganglia, habenula and thalamus. Expressed in the small cell lung carcinoma cell line SCC-9. No expression in skeletal muscle. {ECO:0000269|PubMed:1335101}.; unclassifiable (Anatomical System);prostate;optic nerve;lung;heart;adrenal gland;islets of Langerhans;macula lutea;colon;spleen;fovea centralis;choroid;lens;brain;retina; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;parietal lobe; 0.53996 0.14577 -3.512328228 0.324368955 728.73949 5.35831 CACNA1E 0.999999999999934 6.60028318524918e-14 1.68313067676785e-33 calcium voltage-gated channel subunit alpha1 E FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1E gives rise to R-type calcium currents. R-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by nickel, and partially by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to dihydropyridines (DHP), omega- conotoxin-GVIA (omega-CTx-GVIA), and omega-agatoxin-IVA (omega- Aga-IVA). Calcium channels containing alpha-1E subunit could be involved in the modulation of firing patterns of neurons which is important for information processing.; . TISSUE SPECIFICITY: Expressed in neuronal tissues and in kidney.; unclassifiable (Anatomical System);lung;frontal lobe;ovary;brain; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.53292 0.32174 -2.708891704 0.713611701 325.12803 3.83322 CACNA1F 0.873703604496026 0.126296394545538 9.58435657256867e-10 calcium voltage-gated channel subunit alpha1 F FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1F gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin- GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).; DISEASE: Night blindness, congenital stationary, 2A (CSNB2A) [MIM:300071]: A non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia. {ECO:0000269|PubMed:11281458, ECO:0000269|PubMed:12111638, ECO:0000269|PubMed:12187427, ECO:0000269|PubMed:15897456, ECO:0000269|PubMed:22194652, ECO:0000269|PubMed:9662399, ECO:0000269|PubMed:9662400}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cone-rod dystrophy, X-linked 3 (CORDX3) [MIM:300476]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. {ECO:0000269|PubMed:16505158}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Aaland island eye disease (AIED) [MIM:300600]: A retinal disease characterized by a combination of fundus hypopigmentation, decreased visual acuity due to foveal hypoplasia, nystagmus, astigmatism, protan color vision defect, myopia, and defective dark adaptation. Except for progression of axial myopia, the disease can be considered to be a stationary condition. Electroretinography reveals abnormalities in both photopic and scotopic functions. {ECO:0000269|PubMed:17525176, ECO:0000269|PubMed:22194652}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expression in skeletal muscle and retina. {ECO:0000269|PubMed:10873387}.; optic nerve;lung;bone;macula lutea;fovea centralis;choroid;lens;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;beta cell islets;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.25864 0.19789 -0.830447013 11.52984194 2026.4426 8.28029 CACNA1G 0.999996517362333 3.48263766725387e-06 7.4641540124881e-19 calcium voltage-gated channel subunit alpha1 G FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1G gives rise to T-type calcium currents. T-type calcium channels belong to the "low-voltage activated (LVA)" group and are strongly blocked by mibefradil. A particularity of this type of channel is an opening at quite negative potentials and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons which is important for information processing as well as in cell growth processes.; . TISSUE SPECIFICITY: Highly expressed in brain, in particular in the amygdala, subthalamic nuclei, cerebellum and thalamus. Moderate expression in heart; low expression in placenta, kidney and lung. Also expressed in colon and bone marrow and in tumoral cells to a lesser extent. Highly expressed in fetal brain, but also in peripheral fetal tissues as heart, kidney and lung, suggesting a developmentally regulated expression.; unclassifiable (Anatomical System);uterus;lung;heart;visual apparatus;testis;colon;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;thalamus;cerebellum peduncles;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cerebellum; 0.50605 0.17372 -2.374358198 1.114649682 288.88842 3.63697 CACNA1G-AS1 . . . CACNA1G antisense RNA 1 . . . . . . . . . . . CACNA1H 0.755916975722347 0.244083023089266 1.18838673866792e-09 calcium voltage-gated channel subunit alpha1 H FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1H gives rise to T-type calcium currents. T-type calcium channels belong to the "low-voltage activated (LVA)" group and are strongly blocked by nickel and mibefradil. A particularity of this type of channels is an opening at quite negative potentials, and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons which is important for information processing as well as in cell growth processes.; DISEASE: Epilepsy, idiopathic generalized 6 (EIG6) [MIM:611942]: A disorder characterized by recurring generalized seizures in the absence of detectable brain lesions and/or metabolic abnormalities. Generalized seizures arise diffusely and simultaneously from both hemispheres of the brain. {ECO:0000269|PubMed:15048902}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Epilepsy, childhood absence 6 (ECA6) [MIM:611942]: A subtype of idiopathic generalized epilepsy characterized by an onset at age 6-7 years, frequent absence seizures (several per day) and bilateral, synchronous, symmetric 3-Hz spike waves on EEG. Tonic-clonic seizures often develop in adolescence. Absence seizures may either remit or persist into adulthood. {ECO:0000269|PubMed:12891677}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in kidney, liver, heart, brain. Isoform 2 seems to be testis-specific.; unclassifiable (Anatomical System);medulla oblongata;smooth muscle;ovary;tongue;islets of Langerhans;hypothalamus;muscle;developmental;colon;skeletal muscle;retina;uterus;prostate;lung;optic nerve;frontal lobe;endometrium;bone;thyroid;visual apparatus;liver;testis;cervix;spleen;brain; superior cervical ganglion;testis - seminiferous tubule;pons; 0.12150 0.15825 -2.059460781 1.627742392 3476.91536 11.35078 CACNA1I 0.999998893513202 1.10648679744773e-06 1.11646761129101e-18 calcium voltage-gated channel subunit alpha1 I FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. Isoform alpha-1I gives rise to T-type calcium currents. T-type calcium channels belong to the "low-voltage activated (LVA)" group and are strongly blocked by nickel and mibefradil. A particularity of this type of channels is an opening at quite negative potentials, and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons which is important for information processing as well as in cell growth processes. Gates in voltage ranges similar to, but higher than alpha 1G or alpha 1H (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Brain specific.; lung;thyroid; dorsal root ganglion;superior cervical ganglion;liver;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21592 0.12445 -0.826829473 11.5475348 6560.80975 17.05864 CACNA1S 9.55874082626219e-08 0.999999892861208 1.15513842595839e-08 calcium voltage-gated channel subunit alpha1 S FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1S gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin- GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle.; DISEASE: Periodic paralysis hypokalemic 1 (HOKPP1) [MIM:170400]: An autosomal dominant disorder manifested by episodic flaccid generalized muscle weakness associated with falls of serum potassium levels. {ECO:0000269|PubMed:17418573, ECO:0000269|PubMed:18162704, ECO:0000269|PubMed:19118277, ECO:0000269|PubMed:7987325, ECO:0000269|PubMed:8004673}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Malignant hyperthermia 5 (MHS5) [MIM:601887]: Autosomal dominant disorder that is potentially lethal in susceptible individuals on exposure to commonly used inhalational anesthetics and depolarizing muscle relaxants. {ECO:0000269|PubMed:9199552}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Thyrotoxic periodic paralysis 1 (TTPP1) [MIM:188580]: A sporadic muscular disorder characterized by episodic weakness and hypokalemia during a thyrotoxic state. It is clinically similar to hereditary hypokalemic periodic paralysis, except for the fact that hyperthyroidism is an absolute requirement for disease manifestation. The disease presents with recurrent episodes of acute muscular weakness of the four extremities that vary in severity from paresis to complete paralysis. Attacks are triggered by ingestion of a high carbohydrate load or strenuous physical activity followed by a period of rest. Thyrotoxic periodic paralysis can occur in association with any cause of hyperthyroidism, but is most commonly associated with Graves disease. {ECO:0000269|PubMed:15001631}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Skeletal muscle specific.; unclassifiable (Anatomical System);prostate;ovary;heart;larynx;thyroid;placenta;muscle;liver;parathyroid;blood;head and neck;skeletal muscle; skeletal muscle; 0.22642 . -1.20942002 5.714791224 6599.51391 17.17293 CACNA2D1 0.999995804404225 4.19559577516183e-06 5.8064753547162e-18 calcium voltage-gated channel auxiliary subunit alpha2delta 1 FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Plays an important role in excitation-contraction coupling (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in skeletal muscle. Isoform 2 is expressed in the central nervous system. Isoform 2, isoform 4 and isoform 5 are expressed in neuroblastoma cells. Isoform 3, isoform 4 and isoform 5 are expressed in the aorta. {ECO:0000269|PubMed:1309651, ECO:0000269|PubMed:8107964}.; unclassifiable (Anatomical System);lung;heart;spinal cord;visual apparatus;adrenal cortex;colon;testis;kidney;brain;skeletal muscle; superior cervical ganglion;skeletal muscle; 0.36263 . -0.754958418 13.57631517 137.26388 2.54775 CACNA2D2 0.999693296855458 0.000306703144501033 4.07749937315773e-14 calcium voltage-gated channel auxiliary subunit alpha2delta 2 FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Acts as a regulatory subunit for P/Q-type calcium channel (CACNA1A), N-type (CACNA1B), L-type (CACNA1C OR CACNA1D) and possibly T-type (CACNA1G). Overexpression induces apoptosis. {ECO:0000269|PubMed:12555074, ECO:0000269|PubMed:15111129}.; . TISSUE SPECIFICITY: Predominantly present in cerebellar cortex. Present in various lung tumor cell lines, while it is absent in normal lung (at protein level). Highly expressed in heart, lung, testis, pancreas and skeletal muscle. Also expressed in kidney, liver, placenta and brain. {ECO:0000269|PubMed:10766861, ECO:0000269|PubMed:11687876, ECO:0000269|PubMed:9880589}.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;fovea centralis;choroid;lens;skin;retina;uterus;breast;prostate;optic nerve;whole body;lung;placenta;macula lutea;testis;kidney;brain;mammary gland; . 0.48941 0.15443 -0.549263935 19.95163954 590.52071 4.92605 CACNA2D3 0.998032255145607 0.00196774485362752 7.65325865565944e-13 calcium voltage-gated channel auxiliary subunit alpha2delta 3 FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Acts as a regulatory subunit for P/Q-type calcium channel (CACNA1A), N-type (CACNA1B), L-type (CACNA1C OR CACNA1D) but not T-type (CACNA1G) (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Only detected in brain. Not present in lung, testis, aorta, spleen, jejunum, ventricular muscle and kidney (at protein level). According to PubMed:11687876, it is brain- specific, while according to PubMed:11245980, it is widely expressed. {ECO:0000269|PubMed:11687876}.; unclassifiable (Anatomical System);heart;hypothalamus;skin;uterus;pancreas;whole body;lung;frontal lobe;endometrium;bone;pituitary gland;alveolus;hypopharynx;testis;head and neck;spleen;kidney;brain; amygdala;occipital lobe;caudate nucleus; 0.66118 . -0.837696902 11.45317292 106.33657 2.23770 CACNA2D3-AS1 . . . CACNA2D3 antisense RNA 1 . . . . . . . . . . . CACNA2D4 4.57168482146793e-22 0.0622448119611419 0.937755188038858 calcium voltage-gated channel auxiliary subunit alpha2delta 4 FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. {ECO:0000269|PubMed:12181424}.; DISEASE: Retinal cone dystrophy 4 (RCD4) [MIM:610478]: Characterized by minimal symptoms except for slowly progressive reduction in visual acuity. {ECO:0000269|PubMed:17033974}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in certain types of endocrine cells. Present in the Paneth cells of the small intestine. Also present in the erythroblasts in the fetal liver, in the cells of the zona reticularis of the adrenal gland and in the basophils of the pituitary. Present at low level in some brain regions such as the cerebellum (at protein level). {ECO:0000269|PubMed:12181424}.; unclassifiable (Anatomical System);lymph node;heart;fovea centralis;skin;skeletal muscle;retina;bone marrow;lung;cerebral cortex;bone;placenta;macula lutea;liver;testis;spleen;germinal center;kidney;pineal gland;thymus; superior cervical ganglion;appendix;trigeminal ganglion; 0.24173 0.12929 0.927698756 89.66147676 685.52007 5.22834 CACNB1 0.99395962249096 0.00604034264206195 3.48669780609693e-08 calcium voltage-gated channel auxiliary subunit beta 1 FUNCTION: The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.; . TISSUE SPECIFICITY: Isoform 1 and isoform 3 are expressed in brain, heart, spleen, central nervous system and neuroblastoma cells. Isoform 2 is expressed in skeletal muscle. {ECO:0000269|PubMed:8107964}.; unclassifiable (Anatomical System);prostate;lung;heart;hippocampus;muscle;liver;spleen;brain;skeletal muscle; amygdala;superior cervical ganglion;medulla oblongata;tongue;prefrontal cortex;globus pallidus;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cingulate cortex; 0.09797 0.11854 -0.556537043 19.72753008 42.92536 1.24273 CACNB2 0.00182033784193924 0.997139377637894 0.0010402845201672 calcium voltage-gated channel auxiliary subunit beta 2 FUNCTION: The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.; DISEASE: Brugada syndrome 4 (BRGDA4) [MIM:611876]: A heart disease characterized by the association of Brugada syndrome with shortened QT intervals. Brugada syndrome is a tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs, the individual will faint and may die in a few minutes if the heart is not reset. {ECO:0000269|PubMed:17224476}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues.; unclassifiable (Anatomical System);myocardium;heart;ovary;islets of Langerhans;parathyroid;fovea centralis;breast;uterus;pancreas;prostate;lung;frontal lobe;bone;placenta;macula lutea;hippocampus;pituitary gland;liver;spleen;kidney;brain;mammary gland;aorta; superior cervical ganglion;subthalamic nucleus;medulla oblongata;occipital lobe;cerebellum peduncles;temporal lobe;prefrontal cortex;globus pallidus;pons;pituitary;cingulate cortex;parietal lobe; 0.18213 0.15589 -0.705410796 14.77942911 766.55161 5.48442 CACNB3 0.0495836525739543 0.949447290441446 0.000969056984600077 calcium voltage-gated channel auxiliary subunit beta 3 FUNCTION: The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.; . TISSUE SPECIFICITY: Expressed mostly in brain, smooth muscle and ovary.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; amygdala;whole brain;occipital lobe;medulla oblongata;cerebellum peduncles;temporal lobe;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.33252 0.11612 -0.756778259 13.44656759 51.20317 1.41090 CACNB4 0.0113635817076805 0.988273668140282 0.000362750152036981 calcium voltage-gated channel auxiliary subunit beta 4 FUNCTION: The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.; DISEASE: Juvenile myoclonic epilepsy 6 (EJM6) [MIM:607682]: A subtype of idiopathic generalized epilepsy. Patients have afebrile seizures only, with onset in adolescence (rather than in childhood) and myoclonic jerks which usually occur after awakening and are triggered by sleep deprivation and fatigue. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Episodic ataxia 5 (EA5) [MIM:613855]: A disorder characterized by episodes of vertigo and ataxia that last for several hours. Interictal examination show spontaneous downbeat and gaze-evoked nystagmus, mild dysarthria and truncal ataxia. {ECO:0000269|PubMed:10762541}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly in the cerebellum and kidney.; colon;parathyroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;bone;pituitary gland;testis;germinal center;pineal gland;brain;amygdala;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;occipital lobe;cerebellum peduncles;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.19944 0.13941 0.082802743 60.09082331 22.57919 0.75555 CACNG1 4.77504657244384e-07 0.122747218081721 0.877252304413622 calcium voltage-gated channel auxiliary subunit gamma 1 FUNCTION: This protein is a subunit of the dihydropyridine (DHP) sensitive calcium channel. Plays a role in excitation-contraction coupling. The skeletal muscle DHP-sensitive Ca(2+) channel may function only as a multiple subunit complex.; . TISSUE SPECIFICITY: Skeletal muscle.; unclassifiable (Anatomical System);whole body;heart;kidney;skeletal muscle; tongue;trigeminal ganglion;skeletal muscle; 0.24345 0.09976 -0.159704656 41.90846898 917.45222 5.88808 CACNG2 0.958056003336912 0.0418438450747183 0.000100151588369655 calcium voltage-gated channel auxiliary subunit gamma 2 FUNCTION: Regulates the trafficking and gating properties of AMPA- selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state. {ECO:0000269|PubMed:20805473}.; DISEASE: Mental retardation, autosomal dominant 10 (MRD10) [MIM:614256]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:21376300}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Brain.; unclassifiable (Anatomical System);lung;frontal lobe;ovary;placenta;macula lutea;parathyroid;fovea centralis;brain;cerebellum; superior cervical ganglion;cerebellum peduncles;atrioventricular node;trigeminal ganglion; 0.63044 0.17219 -0.163345027 41.24793583 24.71448 0.81113 CACNG3 0.987801232112246 0.0121940118839741 4.75600378020999e-06 calcium voltage-gated channel auxiliary subunit gamma 3 FUNCTION: Regulates the trafficking and gating properties of AMPA- selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);optic nerve;lung;whole body;frontal lobe;macula lutea;hippocampus;testis;fovea centralis;choroid;lens;brain;retina; amygdala;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;caudate nucleus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.64286 0.11262 -0.119252484 44.53880632 5.82299 0.21975 CACNG4 0.21577447263925 0.775574152504625 0.00865137485612531 calcium voltage-gated channel auxiliary subunit gamma 4 FUNCTION: Regulates the trafficking and gating properties of AMPA- selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization and by mediating their resensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state. {ECO:0000269|PubMed:21172611}.; . . unclassifiable (Anatomical System);heart;colon;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;breast;pancreas;prostate;optic nerve;lung;macula lutea;visual apparatus;hippocampus;kidney;mammary gland;brain;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;kidney;caudate nucleus;trigeminal ganglion;parietal lobe;skeletal muscle;skin;cerebellum; 0.66279 0.11734 -0.181750739 40.15687662 63.88195 1.63928 CACNG5 0.0535604442272795 0.863371714690779 0.0830678410819414 calcium voltage-gated channel auxiliary subunit gamma 5 FUNCTION: Regulates the gating properties of AMPA-selective glutamate receptors (AMPARs). Modulates their gating properties by accelerating their rates of activation, deactivation and desensitization. Displays subunit-specific AMPA receptor regulation. Shows specificity for GRIA1, GRIA4 and the long isoform of GRIA2. Thought to stabilize the calcium channel in an inactivated (closed) state (By similarity). {ECO:0000250}.; . . . . 0.17194 . -0.135838822 43.77211607 82.33632 1.92646 CACNG6 0.180522903079776 0.765903504696993 0.0535735922232309 calcium voltage-gated channel auxiliary subunit gamma 6 FUNCTION: Thought to stabilize the calcium channel in an inactivated (closed) state. {ECO:0000250}.; . . medulla oblongata;whole body;ovary;placenta;visual apparatus;parathyroid; . 0.03315 0.05099 . . 405.22245 4.22093 CACNG7 0.712700867147393 0.284009763727266 0.0032893691253412 calcium voltage-gated channel auxiliary subunit gamma 7 FUNCTION: Regulates the trafficking and gating properties of AMPA- selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization and by mediating their resensitization. Displays subunit-specific AMPA receptor regulation. Shows specificity only for GRIA1 and GRIA2. Thought to stabilize the calcium channel in an inactivated (closed) state. {ECO:0000269|PubMed:21172611}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11170751}.; unclassifiable (Anatomical System);frontal lobe;brain; . 0.27890 0.11809 -0.317668748 31.45789101 14.09174 0.51100 CACNG8 . . . calcium voltage-gated channel auxiliary subunit gamma 8 FUNCTION: Regulates the trafficking and gating properties of AMPA- selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization and by mediating their resensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state. {ECO:0000269|PubMed:20805473, ECO:0000269|PubMed:21172611}.; . . . . 0.11452 . . . 18.30866 0.63592 CACTIN 0.999345095775966 0.000654900452098358 3.77193575768561e-09 cactin, spliceosome C complex subunit FUNCTION: Involved in the regulation of innate immune response. Acts as negative regulator of Toll-like receptor and interferon- regulatory factor (IRF) signaling pathways. Contributes to the regulation of transcriptional activation of NF-kappa-B target genes in response to endogenous proinflammatory stimuli. May play a role during early embryonic development. Probably involved in pre-mRNA splicing. {ECO:0000269|PubMed:20829348}.; . . . . 0.11116 . -0.753139731 13.67067705 1251.44006 6.67662 CACTIN-AS1 . . . CACTIN antisense RNA 1 . . . . . . . . . . . CACUL1 0.84668696675278 0.153197480433812 0.000115552813407946 CDK2 associated cullin domain 1 FUNCTION: Cell cycle associated protein capable of promoting cell proliferation through the activation of CDK2 at the G1/S phase transition. {ECO:0000269|PubMed:19829063}.; . TISSUE SPECIFICITY: Ubiquitously expressed with highest expression in the mammary gland and large intestine. Highly expressed in cancer tissues and cancer cell lines. During cell cycle progression expression is high in G1/S, low in the middle of S phase, and increases again in S/G2 phase. {ECO:0000269|PubMed:19829063}.; . . 0.36251 . -0.626318434 17.03231894 8.48624 0.31158 CACYBP 0.943386849157678 0.0564012648062792 0.000211886036042907 calcyclin binding protein FUNCTION: May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1). {ECO:0000269|PubMed:16085652}.; . . . . 0.50100 0.10131 0.03689118 56.64071715 49.62991 1.38028 CACYBPP1 . . . calcyclin binding protein pseudogene 1 . . . . . . . . . . . CACYBPP2 . . . calcyclin binding protein pseudogene 2 . . . . . . . . . . . CACYBPP3 . . . calcyclin binding protein pseudogene 3 . . . . . . . . . . . CAD 0.999999701880854 2.98119145798896e-07 1.55224524052493e-23 carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase FUNCTION: This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase). {ECO:0000269|PubMed:24332717}.; DISEASE: Congenital disorder of glycosylation 1Z (CDG1Z) [MIM:616457]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. CDG1Z patients show abnormal glycosylation of red blood cell proteins, but glycosylation of serum transferrin is normal. {ECO:0000269|PubMed:25678555}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;aorta; tumor; 0.66742 0.13233 -3.840064972 0.230007077 212.36557 3.14379 CADM1 0.99438640410443 0.00561288415660614 7.11738963443634e-07 cell adhesion molecule 1 FUNCTION: Mediates homophilic cell-cell adhesion in a Ca(2+)- independent manner. Also mediates heterophilic cell-cell adhesion with CADM3 and PVRL3 in a Ca(2+)-independent manner. Acts as a tumor suppressor in non-small-cell lung cancer (NSCLC) cells. Interaction with CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM3 in vivo. May contribute to the less invasive phenotypes of lepidic growth tumor cells. In mast cells, may mediate attachment to and promote communication with nerves. CADM1, together with MITF, is essential for development and survival of mast cells in vivo. Acts as a synaptic cell adhesion molecule and plays a role in the formation of dendritic spines and in synapse assembly (By similarity). May be involved in neuronal migration, axon growth, pathfinding, and fasciculation on the axons of differentiating neurons. May play diverse roles in the spermatogenesis including in the adhesion of spermatocytes and spermatids to Sertoli cells and for their normal differentiation into mature spermatozoa. {ECO:0000250, ECO:0000269|PubMed:11279526, ECO:0000269|PubMed:12050160, ECO:0000269|PubMed:12234973, ECO:0000269|PubMed:12920246, ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:15905536, ECO:0000269|PubMed:22438059}.; . . ovary;developmental;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;thyroid;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;cerebellum cortex;nervous;islets of Langerhans;hypothalamus;pineal body;adrenal cortex;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;aorta;peripheral nerve;cerebellum; dorsal root ganglion;amygdala;superior cervical ganglion;occipital lobe;cerebellum peduncles;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;cerebellum; 0.76816 0.11049 -0.137658575 43.57159707 246.74906 3.38920 CADM2 0.984668909563275 0.0153294023945765 1.68804214797314e-06 cell adhesion molecule 2 FUNCTION: Adhesion molecule that engages in homo- and heterophilic interactions with the other nectin-like family members, leading to cell aggregation. Important for synapse organization, providing regulated trans-synaptic adhesion. Preferentially binds to oligodendrocytes. {ECO:0000269|PubMed:17967169}.; . . . . 0.51798 0.11638 -0.60427181 17.74593064 430.67561 4.33088 CADM2-AS1 . . . CADM2 antisense RNA 1 . . . . . . . . . . . CADM2-AS2 . . . CADM2 antisense RNA 2 . . . . . . . . . . . CADM3 0.975630650500283 0.0243640616166765 5.28788304046564e-06 cell adhesion molecule 3 FUNCTION: Involved in the cell-cell adhesion. Has both calcium- independent homophilic cell-cell adhesion activity and calcium- independent heterophilic cell-cell adhesion activity with IGSF4, PVRL1 and PVRL3. Interaction with EPB41L1 may regulate structure or function of cell-cell junctions (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is expressed mainly in adult and fetal brain. Isoform 2 is highly expressed in adult brain and weakly expressed in placenta. In brain, Isoform 2 is highly expressed in cerebellum. {ECO:0000269|PubMed:11536053, ECO:0000269|PubMed:15893517, ECO:0000269|PubMed:18420026}.; . . 0.23520 0.45900 -0.492218069 22.35786742 53.98676 1.46501 CADM3-AS1 . . . CADM3 antisense RNA 1 . . . . . . . . . . . CADM4 0.979491544538579 0.0204914100554576 1.70454059634177e-05 cell adhesion molecule 4 FUNCTION: Involved in the cell-cell adhesion. Has calcium- and magnesium-independent cell-cell adhesion activity. May have tumor- suppressor activity. {ECO:0000269|PubMed:16261159}.; . TISSUE SPECIFICITY: Expressed in brain, prostate, brain, kidney and some other organs. {ECO:0000269|PubMed:11536053, ECO:0000269|PubMed:16261159}.; unclassifiable (Anatomical System);heart;hypothalamus;fovea centralis;choroid;lens;retina;breast;prostate;optic nerve;whole body;lung;frontal lobe;thyroid;macula lutea;testis;amniotic fluid;kidney;brain; superior cervical ganglion;uterus corpus;medulla oblongata;hypothalamus;prefrontal cortex;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.28494 0.08883 0.148941568 64.31941496 413.28674 4.25628 CADPS 0.0528164675314738 0.947183529995843 2.47268361559339e-09 Ca2+ dependent secretion activator FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates catecholamine loading of DCVs. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles by acting as a PtdIns(4,5)P2-binding protein that acts at prefusion step following ATP-dependent priming and participates in DCVs-membrane fusion. However, it may also participate in small clear synaptic vesicles (SVs) exocytosis and it is unclear whether its function is related to Ca(2+) triggering (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in neural and endocrine secretory tissues. Expressed in brain and pancreas and at low level in heart. Also expressed in fetal heart, cerebellum, cerebral cortex, medulla, occipital pole, frontal and temporal lobes, and putamen, as well as weak expression in spinal cord. {ECO:0000269|PubMed:12659812}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;hypothalamus;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;lung;frontal lobe;cochlea;adrenal gland;macula lutea;visual apparatus;pituitary gland;head and neck;germinal center;kidney;brain;mammary gland; . 0.46523 . -1.346642726 4.62962963 108.92082 2.26567 CADPS2 0.997778954042416 0.00222104595250176 5.08171821623575e-12 Ca2+ dependent secretion activator 2 FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates neurotrophin release from granule cells leading to regulate cell differentiation and survival during cerebellar development. May specifically mediate the Ca(2+)- dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in all adult and fetal tissues examined, with the strongest expression in kidney and pancreas. In brain, it is expressed at high levels in cerebellum, to a lesser degree in cerebral cortex, occipital pole, and frontal and temporal lobes. Only weakly expressed in medulla, spinal cord and putamen. {ECO:0000269|PubMed:12659812}.; unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;colon;parathyroid;blood;choroid;skin;retina;uterus;pancreas;prostate;lung;frontal lobe;endometrium;placenta;bone;visual apparatus;head and neck;germinal center;kidney;mammary gland;brain;stomach; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;temporal lobe;atrioventricular node;pons;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cerebellum; 0.45062 0.12261 -0.661316159 16.02382637 194.52292 3.02320 CAGE1 2.62440972757105e-06 0.746986415386687 0.253010960203586 cancer antigen 1 . . TISSUE SPECIFICITY: Testis-specific expression in normal tissues, but wide expression among cancer tissues and cell lines.; unclassifiable (Anatomical System);lung;testis; superior cervical ganglion;atrioventricular node; 0.03109 0.07696 1.021500656 91.01792876 1077.8617 6.29323 CAHM . . . colon adenocarcinoma hypermethylated (non-protein coding) . . . . . . . . . . . CALB1 0.898924669499301 0.101036860761224 3.84697394745875e-05 calbindin 1 FUNCTION: Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase.; . . unclassifiable (Anatomical System);lymph node;hypothalamus;colon;blood;skeletal muscle;retina;bile duct;breast;optic nerve;lung;frontal lobe;internal ear;hippocampus;liver;pituitary gland;testis;middle ear;kidney;brain;bladder;stomach; amygdala;whole brain;superior cervical ganglion;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;pons;kidney;atrioventricular node;caudate nucleus;cerebellum; 0.46919 0.60081 -0.163345027 41.24793583 9.1714 0.33478 CALB2 0.00123890128989255 0.95864903644726 0.0401120622628475 calbindin 2 FUNCTION: Calretinin is a calcium-binding protein which is abundant in auditory neurons.; . . unclassifiable (Anatomical System);lymph node;heart;ovary;hypothalamus;colon;choroid;skin;retina;uterus;whole body;lung;frontal lobe;pituitary gland;testis;brain;stomach; amygdala;thalamus;superior cervical ganglion;cerebellum peduncles;hypothalamus;cerebellum; 0.32852 . -0.271755481 34.31823543 1337.16079 6.86666 CALCA 0.00139555682902756 0.427581876709416 0.571022566461557 calcitonin related polypeptide alpha FUNCTION: Calcitonin causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones.; . . unclassifiable (Anatomical System);prostate;thyroid;pineal gland; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;thyroid;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06668 0.61553 0.905808022 89.4373673 414.3263 4.26398 CALCB 0.0578761947440093 0.712256743211904 0.229867062044087 calcitonin related polypeptide beta FUNCTION: CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role.; . . hypothalamus;bone;brain; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04009 0.11558 -0.141298762 42.87567823 7.25364 0.27239 CALCOCO1 0.171891880753814 0.828084539806011 2.35794401756688e-05 calcium binding and coiled-coil domain 1 FUNCTION: Functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). Recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. Involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1- mediated transcriptional activation via its interaction with CTNNB1. Coactivator function for nuclear receptors and LEF1/CTNNB1 involves differential utilization of two different activation regions (By similarity). In association with CCAR1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). {ECO:0000250|UniProtKB:Q8CGU1, ECO:0000269|PubMed:24245781}.; . . myocardium;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;brain;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus;cerebellum; . 0.14010 0.19662 0.957177419 90.14508139 1989.47131 8.21650 CALCOCO2 0.0317624526733932 0.966320166784931 0.00191738054167619 calcium binding and coiled-coil domain 2 FUNCTION: Xenophagy-specific receptor required for autophagy- mediated intracellular bacteria degradation. Acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens such as Salmonella typhimurium upon entry into the cytosol by targeting galectin-8- associated bacteria for autophagy (PubMed:22246324). Initially orchestrates bacteria targeting to autophagosomes and subsequently ensures pathogen degradation by regulating pathogen-containing autophagosome maturation (PubMed:23022382, PubMed:25771791). Bacteria targeting to autophagosomes relies on its interaction with MAP1LC3A, MAP1LC3B and/or GABARAPL2, whereas regulation of pathogen-containing autophagosome maturation requires the interaction with MAP3LC3C (PubMed:23022382, PubMed:25771791). May play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion (PubMed:17635994). {ECO:0000269|PubMed:17635994, ECO:0000269|PubMed:22246324, ECO:0000269|PubMed:23022382, ECO:0000269|PubMed:23386746, ECO:0000269|PubMed:25771791}.; . TISSUE SPECIFICITY: Expressed in all tissues tested with highest expression in skeletal muscle and lowest in brain. {ECO:0000269|PubMed:7540613}.; myocardium;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;nervous;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05012 0.05838 0.617373774 83.25076669 3332.75453 11.04651 CALCP . . . calcitonin pseudogene . . . . . . . . . . . CALCR 3.37646968831731e-05 0.987226089935183 0.0127401453679336 calcitonin receptor FUNCTION: This is a receptor for calcitonin. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. The calcitonin receptor is thought to couple to the heterotrimeric guanosine triphosphate-binding protein that is sensitive to cholera toxin.; . . unclassifiable (Anatomical System);uterus;whole body;heart;bone;kidney;skin; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.18131 0.47452 0.088260113 60.56853031 61.05178 1.59001 CALCRL 0.926324873613011 0.0736580633933896 1.70629935991989e-05 calcitonin receptor like receptor FUNCTION: Receptor for calcitonin-gene-related peptide (CGRP) together with RAMP1 and receptor for adrenomedullin together with RAMP3 (By similarity). Receptor for adrenomedullin together with RAMP2. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. {ECO:0000250, ECO:0000269|PubMed:22102369}.; . TISSUE SPECIFICITY: Predominantly expressed in the lung and heart.; . . 0.37301 0.10736 0.17280645 65.75843359 91.02186 2.05249 CALD1 0.99909770368326 0.000902295979526348 3.37213299139284e-10 caldesmon 1 FUNCTION: Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). {ECO:0000250, ECO:0000269|PubMed:8227296}.; . TISSUE SPECIFICITY: High-molecular-weight caldesmon (isoform 1) is predominantly expressed in smooth muscles, whereas low-molecular- weight caldesmon (isoforms 2, 3, 4 and 5) are widely distributed in non-muscle tissues and cells. Not expressed in skeletal muscle or heart.; myocardium;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;brain;amygdala;heart;cartilage;adrenal cortex;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;bone;pituitary gland;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;amnion;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;olfactory bulb;adipose tissue;smooth muscle;adrenal cortex;atrioventricular node;skeletal muscle;uterus;prostate;uterus corpus;appendix;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.85572 0.26033 1.46612072 95.25241802 361.61985 4.02471 CALHM1 9.35701997314557e-05 0.342128956833621 0.657777472966647 calcium homeostasis modulator 1 FUNCTION: Pore-forming subunit of a voltage-gated ion channel required for sensory perception of sweet, bitter and umami tastes. Specifically present in type II taste bud cells, where it plays a central role in sweet, bitter and umami taste perception by inducing ATP release from the cell, ATP acting as a neurotransmitter to activate afferent neural gustatory pathways. Acts both as a voltage-gated and calcium-activated ion channel: mediates neuronal excitability in response to changes in extracellular Ca(2+) concentration. Has poor ion selectivity and forms a wide pore (around 14 Angstroms) that mediates permeation of Ca(2+), Na(+) and K(+), as well as permeation of monovalent anions. Acts as an activator of the ERK1 and ERK2 cascade. Triggers endoplasmic reticulum stress by reducing the calcium content of the endoplasmic reticulum. May indirectly control amyloid precursor protein (APP) proteolysis and aggregated amyloid-beta (Abeta) peptides levels in a Ca(2+) dependent manner. {ECO:0000269|PubMed:18585350, ECO:0000269|PubMed:21574960, ECO:0000269|PubMed:22711817, ECO:0000269|PubMed:23300080, ECO:0000269|PubMed:23345406}.; . TISSUE SPECIFICITY: Predominantly expressed in adult brain. Detected also in retinoic acid-differentiated SH-SY5Y cells. Specifically expressed in circumvallate taste bud cells. {ECO:0000269|PubMed:18585350, ECO:0000269|PubMed:19997627}.; unclassifiable (Anatomical System);hippocampus; . 0.20672 0.10990 -0.108334733 45.57088936 259.73729 3.46299 CALHM2 5.29267890521713e-07 0.0693456932236304 0.930653777508479 calcium homeostasis modulator 2 FUNCTION: Pore-forming subunit of a voltage-gated ion channel. {ECO:0000250}.; . . ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;urinary;muscle;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;alveolus;spleen;head and neck;kidney;mammary gland; ciliary ganglion; 0.14492 0.11080 0.062575634 58.74026893 188.38838 2.98153 CALHM3 . . . calcium homeostasis modulator 3 FUNCTION: Pore-forming subunit of a voltage-gated ion channel. {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in circumvallate taste bud cells. {ECO:0000269|PubMed:19997627}.; . . 0.16112 0.09628 -0.053113545 49.38664779 1546.87575 7.29389 CALM1 0.894820172867617 0.104161218949336 0.00101860818304697 calmodulin 1 (phosphorylase kinase, delta) FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. {ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:23893133}.; DISEASE: Ventricular tachycardia, catecholaminergic polymorphic, 4 (CPVT4) [MIM:614916]: An arrhythmogenic disorder characterized by stress-induced, bidirectional ventricular tachycardia that may degenerate into cardiac arrest and cause sudden death. Patients present with recurrent syncope, seizures, or sudden death after physical activity or emotional stress. {ECO:0000269|PubMed:23040497}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Long QT syndrome 14 (LQT14) [MIM:616247]: A form of long QT syndrome, a heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. {ECO:0000269|PubMed:23388215, ECO:0000269|PubMed:24076290}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Long QT syndrome 15 (LQT15) [MIM:616249]: A form of long QT syndrome, a heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. {ECO:0000269|PubMed:23388215, ECO:0000269|PubMed:24917665}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;amygdala;heart;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; amygdala;whole brain;medulla oblongata;superior cervical ganglion;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; . 0.36254 0.035072054 56.2514744 . . CALM1P1 . . . calmodulin 1 (phosphorylase kinase, delta) pseudogene 1 . . . . . . . . . . . CALM1P2 . . . calmodulin 1 (phosphorylase kinase, delta) pseudogene 2 . . . . . . . . . . . CALM2 0.856387218811605 0.141331344499975 0.00228143668842079 calmodulin 2 (phosphorylase kinase, delta) FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. {ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:23893133}.; DISEASE: Ventricular tachycardia, catecholaminergic polymorphic, 4 (CPVT4) [MIM:614916]: An arrhythmogenic disorder characterized by stress-induced, bidirectional ventricular tachycardia that may degenerate into cardiac arrest and cause sudden death. Patients present with recurrent syncope, seizures, or sudden death after physical activity or emotional stress. {ECO:0000269|PubMed:23040497}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Long QT syndrome 14 (LQT14) [MIM:616247]: A form of long QT syndrome, a heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. {ECO:0000269|PubMed:23388215, ECO:0000269|PubMed:24076290}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Long QT syndrome 15 (LQT15) [MIM:616249]: A form of long QT syndrome, a heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. {ECO:0000269|PubMed:23388215, ECO:0000269|PubMed:24917665}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;substantia nigra;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;brain;cartilage;tongue;pineal body;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;oesophagus;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;parietal lobe;cingulate cortex; 0.69728 0.32162 0.12325821 62.38499646 8.57012 0.31396 CALM2P1 . . . calmodulin 2 pseudogene 1 . . . . . . . . . . . CALM2P2 . . . calmodulin 2 pseudogene 2 . . . . . . . . . . . CALM2P3 . . . calmodulin 2 pseudogene 3 . . . . . . . . . . . CALM2P4 . . . calmodulin 2 pseudogene 4 . . . . . . . . . . . CALM3 0.580172431977243 0.409077396373215 0.0107501716495422 calmodulin 3 (phosphorylase kinase, delta) FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. {ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:23893133}.; DISEASE: Ventricular tachycardia, catecholaminergic polymorphic, 4 (CPVT4) [MIM:614916]: An arrhythmogenic disorder characterized by stress-induced, bidirectional ventricular tachycardia that may degenerate into cardiac arrest and cause sudden death. Patients present with recurrent syncope, seizures, or sudden death after physical activity or emotional stress. {ECO:0000269|PubMed:23040497}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Long QT syndrome 14 (LQT14) [MIM:616247]: A form of long QT syndrome, a heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. {ECO:0000269|PubMed:23388215, ECO:0000269|PubMed:24076290}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Long QT syndrome 15 (LQT15) [MIM:616249]: A form of long QT syndrome, a heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. {ECO:0000269|PubMed:23388215, ECO:0000269|PubMed:24917665}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;thyroid;iris;bladder;brain;tonsil;amygdala;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach;cerebellum; amygdala;whole brain;medulla oblongata;occipital lobe;testis - interstitial;thalamus;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;cingulate cortex;parietal lobe;cerebellum; . 0.93503 -0.09720619 46.20193442 . . CALML3 0.0379249704063146 0.638686379691182 0.323388649902503 calmodulin like 3 FUNCTION: May function as a specific light chain of unconventional myosin-10 (MYO10), also enhances MYO10 translation, possibly by acting as a chaperone for the emerging MYO10 heavy chain protein. May compete with calmodulin by binding, with different affinities, to cellular substrates. {ECO:0000269|PubMed:11278607, ECO:0000269|PubMed:18295593}.; . TISSUE SPECIFICITY: Expressed in normal mammary, prostate, cervical, and epidermal tissues. It is greatly reduced or undetectable in transformed cells. {ECO:0000269|PubMed:2217169}.; unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;larynx;thyroid;macula lutea;hypopharynx;testis;head and neck;cervix;kidney;mammary gland;thymus; dorsal root ganglion;superior cervical ganglion;tongue;caudate nucleus;tonsil;thymus; 0.26798 . 0.391453969 75.87284737 103.25433 2.19479 CALML3-AS1 . . . CALML3 antisense RNA 1 . . . . . . . . . . . CALML4 0.0102090578324751 0.826503874478676 0.163287067688849 calmodulin like 4 . . TISSUE SPECIFICITY: Expressed in breast cancer cell lines. {ECO:0000269|PubMed:12747765}.; unclassifiable (Anatomical System);ovary;colon;fovea centralis;choroid;lens;retina;bone marrow;uterus;optic nerve;whole body;lung;endometrium;placenta;macula lutea;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland;tonsil; superior cervical ganglion;trachea;kidney;trigeminal ganglion;skeletal muscle; 0.13671 0.08963 0.238945317 69.20853975 105.54792 2.22619 CALML5 0.53657959921762 0.405310973782559 0.0581094269998214 calmodulin like 5 FUNCTION: Binds calcium. May be involved in terminal differentiation of keratinocytes.; . TISSUE SPECIFICITY: Particularly abundant in the epidermis where its expression is directly related to keratinocyte differentiation. Very low expression in lung.; . . 0.06118 0.08724 0.637604436 83.77565464 113.58846 2.32102 CALML6 0.000127436926421093 0.396237669097266 0.603634893976313 calmodulin like 6 . . TISSUE SPECIFICITY: Expressed in prostate, thymus, heart, skeleton muscle, bone marrow and ovary. {ECO:0000269|PubMed:15621662}.; optic nerve;whole body;macula lutea;fovea centralis;choroid;lens;stomach;retina; . 0.12055 0.14977 0.128714042 63.19886766 1517.43214 7.24063 CALN1 0.153650290078419 0.829744545580459 0.016605164341122 calneuron 1 FUNCTION: Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity (By similarity). May play a role in the physiology of neurons and is potentially important in memory and learning. {ECO:0000250}.; . TISSUE SPECIFICITY: Brain specific.; optic nerve;macula lutea;fovea centralis;choroid;lens;retina; . 0.34357 0.10075 -0.029247611 51.40363293 22.71328 0.76004 CALR 0.93872855492894 0.061218723935862 5.27211351981369e-05 calreticulin FUNCTION: Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). {ECO:0000250, ECO:0000269|PubMed:11149926, ECO:0000269|PubMed:7876246}.; . . lymphoreticular;ovary;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);trophoblast;lymph node;heart;tongue;islets of Langerhans;hypothalamus;muscle;urinary;blood;breast;pancreas;lung;adrenal gland;epididymis;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; smooth muscle;adipose tissue;trachea;placenta;thyroid;kidney;fetal thyroid;skeletal muscle; 0.89810 0.86884 -0.624497208 17.16206653 79.72032 1.88685 CALR3 8.79344302331144e-08 0.496871815334281 0.503128096731289 calreticulin 3 FUNCTION: During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR. {ECO:0000250, ECO:0000269|PubMed:21590275}.; DISEASE: Cardiomyopathy, familial hypertrophic 19 (CMH19) [MIM:613875]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:17655857}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12384296}.; unclassifiable (Anatomical System);medulla oblongata;lung;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.09922 . 0.154398214 64.73814579 88.80833 2.02303 CALR4P . . . calreticulin 4, pseudogene . . . . . . . . . . . CALU 0.447140101291407 0.54645917287485 0.00640072583374235 calumenin FUNCTION: Involved in regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. Seems to inhibit gamma-carboxylase GGCX. Binds 7 calcium ions with a low affinity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at high levels in heart, placenta and skeletal muscle, at lower levels in lung, kidney and pancreas and at very low levels in brain and liver.; ovary;umbilical cord;sympathetic chain;skin;bone marrow;prostate;cochlea;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;oesophagus;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;pia mater;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; dorsal root ganglion;uterus corpus;superior cervical ganglion;smooth muscle;adipose tissue;placenta;ciliary ganglion; 0.65705 0.42019 0.12689526 63.00424628 1766.02314 7.76511 CALY 0.706613402268371 0.277792655272703 0.0155939424589258 calcyon neuron specific vesicular protein FUNCTION: Interacts with clathrin light chain A and stimulates clathrin self-assembly and clathrin-mediated endocytosis. {ECO:0000269|PubMed:16595675}.; . TISSUE SPECIFICITY: Expressed in the pyramidal cells of the prefrontal cortex, in hippothalamus and in caudate nucleus. No expression in spleen. Up-regulated in the prefrontal cortex of schizophrenic patients with nearly twice the levels of non- schizophrenics. {ECO:0000269|PubMed:12622665}.; unclassifiable (Anatomical System);optic nerve;adrenal gland;islets of Langerhans;hypothalamus;macula lutea;hippocampus;pituitary gland;fovea centralis;choroid;lens;brain;retina;cerebellum; amygdala;whole brain;occipital lobe;medulla oblongata;thalamus;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;pituitary;parietal lobe;cingulate cortex; 0.15370 0.13077 . . 177.87988 2.89850 CAMK1 0.00474654619158076 0.988963733943594 0.00628971986482491 calcium/calmodulin-dependent protein kinase I FUNCTION: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, regulates transcription activators activity, cell cycle, hormone production, cell differentiation, actin filament organization and neurite outgrowth. Recognizes the substrate consensus sequence [MVLIF]-x-R-x(2)-[ST]-x(3)-[MVLIF]. Regulates axonal extension and growth cone motility in hippocampal and cerebellar nerve cells. Upon NMDA receptor-mediated Ca(2+) elevation, promotes dendritic growth in hippocampal neurons and is essential in synapses for full long-term potentiation (LTP) and ERK2-dependent translational activation. Downstream of NMDA receptors, promotes the formation of spines and synapses in hippocampal neurons by phosphorylating ARHGEF7/BETAPIX on 'Ser- 694', which results in the enhancement of ARHGEF7 activity and activation of RAC1. Promotes neuronal differentiation and neurite outgrowth by activation and phosphorylation of MARK2 on 'Ser-91', 'Ser-92', 'Ser-93' and 'Ser-294'. Promotes nuclear export of HDAC5 and binding to 14-3-3 by phosphorylation of 'Ser-259' and 'Ser- 498' in the regulation of muscle cell differentiation. Regulates NUMB-mediated endocytosis by phosphorylation of NUMB on 'Ser-276' and 'Ser-295'. Involved in the regulation of basal and estrogen- stimulated migration of medulloblastoma cells through ARHGEF7/BETAPIX phosphorylation (By similarity). Is required for proper activation of cyclin-D1/CDK4 complex during G1 progression in diploid fibroblasts. Plays a role in K(+) and ANG2-mediated regulation of the aldosterone synthase (CYP11B2) to produce aldosterone in the adrenal cortex. Phosphorylates EIF4G3/eIF4GII. In vitro phosphorylates CREB1, ATF1, CFTR, MYL9 and SYN1/synapsin I. {ECO:0000250, ECO:0000269|PubMed:11114197, ECO:0000269|PubMed:12193581, ECO:0000269|PubMed:14507913, ECO:0000269|PubMed:14754892, ECO:0000269|PubMed:17056143, ECO:0000269|PubMed:17442826, ECO:0000269|PubMed:18184567, ECO:0000269|PubMed:20181577}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in cells of the zona glomerulosa of the adrenal cortex. {ECO:0000269|PubMed:12193581, ECO:0000269|PubMed:17056143}.; colon;parathyroid;fovea centralis;choroid;retina;prostate;optic nerve;whole body;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;pineal body;muscle;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; . 0.24435 0.18664 -0.516085732 21.20193442 37.56906 1.11859 CAMK1D 0.99380705214431 0.00619204302544642 9.04830243141457e-07 calcium/calmodulin dependent protein kinase ID FUNCTION: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, activates CREB-dependent gene transcription, regulates calcium-mediated granulocyte function and respiratory burst and promotes basal dendritic growth of hippocampal neurons. In neutrophil cells, required for cytokine- induced proliferative responses and activation of the respiratory burst. Activates the transcription factor CREB1 in hippocampal neuron nuclei. May play a role in apoptosis of erythroleukemia cells. In vitro, phosphorylates transcription factor CREM isoform Beta. {ECO:0000269|PubMed:11050006, ECO:0000269|PubMed:15840691, ECO:0000269|PubMed:16324104, ECO:0000269|PubMed:17056143}.; . TISSUE SPECIFICITY: Widely expressed. Highly and mostly expressed in polymorphonuclear leukocytes (neutrophilic and eosinophilic granulocytes) while little or no expression is observed in monocytes and lymphocytes. {ECO:0000269|PubMed:11050006, ECO:0000269|PubMed:12935886, ECO:0000269|PubMed:15840691}.; . . 0.18445 0.13388 -0.271755481 34.31823543 16.76649 0.58938 CAMK1G 0.101614386605182 0.896897634945689 0.00148797844912907 calcium/calmodulin dependent protein kinase IG FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. In vitro phosphorylates transcription factor CREB1 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Mainly expressed in brain with small amounts in skeletal muscles, kidney, spleen and liver. Strongly expressed in forebrain neocortex, striatum and limbic system. {ECO:0000269|PubMed:12637513}.; unclassifiable (Anatomical System);lung;frontal lobe;islets of Langerhans;hypothalamus;salivary gland;placenta;testis;colon;kidney;brain; amygdala;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;prefrontal cortex;globus pallidus;caudate nucleus;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle; 0.43449 0.13483 -0.867014353 10.72776598 408.0278 4.23621 CAMK2A 0.998004220808766 0.00199577685578083 2.33545295148197e-09 calcium/calmodulin-dependent protein kinase II alpha FUNCTION: CaM-kinase II (CAMK2) is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. Member of the NMDAR signaling complex in excitatory synapses it may regulate NMDAR-dependent potentiation of the AMPAR and synaptic plasticity (By similarity). {ECO:0000250}.; . . amygdala;unclassifiable (Anatomical System);heart;ovary;hypothalamus;parathyroid;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;optic nerve;lung;whole body;frontal lobe;placenta;macula lutea;hippocampus;testis;brain; amygdala;whole brain;medulla oblongata;superior cervical ganglion;occipital lobe;thalamus;hypothalamus;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.69570 0.38769 -0.538132194 20.26421326 1.83486 0.05790 CAMK2B 0.468620194092365 0.531370436426168 9.36948146719951e-06 calcium/calmodulin-dependent protein kinase II beta FUNCTION: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplasmic reticulum Ca(2+) transport in skeletal muscle. In neurons, plays an essential structural role in the reorganization of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner. This structural function is required for correct targeting of CaMK2A, which acts downstream of NMDAR to promote dendritic spine and synapse formation and maintain synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In developing hippocampal neurons, promotes arborization of the dendritic tree and in mature neurons, promotes dendritic remodeling. Participates in the modulation of skeletal muscle function in response to exercise. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2. {ECO:0000269|PubMed:16690701}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in adult and fetal brain. Expression is slightly lower in fetal brain. Expressed in skeletal muscle. {ECO:0000269|PubMed:16690701}.; unclassifiable (Anatomical System);nervous;islets of Langerhans;hypothalamus;muscle;skeletal muscle;retina;prostate;optic nerve;lung;frontal lobe;cerebral cortex;visual apparatus;hippocampus;alveolus;testis;mammary gland;brain;peripheral nerve; whole brain;amygdala;dorsal root ganglion;thalamus;superior cervical ganglion;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;pons;atrioventricular node;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.30429 0.29938 -0.624497208 17.16206653 1301.92267 6.78858 CAMK2D 0.016661668817136 0.983131579237254 0.000206751945610239 calcium/calmodulin-dependent protein kinase II delta FUNCTION: Calcium/calmodulin-dependent protein kinase involved in the regulation of Ca(2+) homeostatis and excitation-contraction coupling (ECC) in heart by targeting ion channels, transporters and accessory proteins involved in Ca(2+) influx into the myocyte, Ca(2+) release from the sarcoplasmic reticulum (SR), SR Ca(2+) uptake and Na(+) and K(+) channel transport. Targets also transcription factors and signaling molecules to regulate heart function. In its activated form, is involved in the pathogenesis of dilated cardiomyopathy and heart failure. Contributes to cardiac decompensation and heart failure by regulating SR Ca(2+) release via direct phosphorylation of RYR2 Ca(2+) channel on 'Ser- 2808'. In the nucleus, phosphorylates the MEF2 repressor HDAC4, promoting its nuclear export and binding to 14-3-3 protein, and expression of MEF2 and genes involved in the hypertrophic program. Is essential for left ventricular remodeling responses to myocardial infarction. In pathological myocardial remodeling acts downstream of the beta adrenergic receptor signaling cascade to regulate key proteins involved in ECC. Regulates Ca(2+) influx to myocytes by binding and phosphorylating the L-type Ca(2+) channel subunit beta-2 CACNB2. In addition to Ca(2+) channels, can target and regulate the cardiac sarcolemmal Na(+) channel Nav1.5/SCN5A and the K+ channel Kv4.3/KCND3, which contribute to arrhythmogenesis in heart failure. Phosphorylates phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2, contributing to the enhancement of SR Ca(2+) uptake that may be important in frequency-dependent acceleration of relaxation (FDAR) and maintenance of contractile function during acidosis. May participate in the modulation of skeletal muscle function in response to exercise, by regulating SR Ca(2+) transport through phosphorylation of PLN/PLB and triadin, a ryanodine receptor- coupling factor. {ECO:0000269|PubMed:16690701, ECO:0000269|PubMed:17179159}.; . TISSUE SPECIFICITY: Expressed in cardiac muscle and skeletal muscle. Isoform Delta 3, isoform Delta 2, isoform Delta 8 and isoform Delta 9 are expressed in cardiac muscle. Isoform Delta 11 is expressed in skeletal muscle. {ECO:0000269|PubMed:10189359, ECO:0000269|PubMed:16690701}.; myocardium;smooth muscle;colon;parathyroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;atrium;whole body;frontal lobe;cochlea;cerebral cortex;bone;testis;germinal center;brain;amygdala;unclassifiable (Anatomical System);lymph node;heart;cartilage;cerebellum cortex;islets of Langerhans;hypothalamus;urinary;blood;skeletal muscle;pancreas;lung;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;cerebellum; trigeminal ganglion;cerebellum; 0.11605 0.23984 0.016664174 55.21939137 134.90959 2.52585 CAMK2G 0.994506145969444 0.00549384843499668 5.59555895042012e-09 calcium/calmodulin-dependent protein kinase II gamma FUNCTION: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in sarcoplsamic reticulum Ca(2+) transport in skeletal muscle and may function in dendritic spine and synapse formation and neuronal plasticity. In slow- twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of the ryanodine receptor-coupling factor triadin. In neurons, may participate in the promotion of dendritic spine and synapse formation and maintenance of synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. {ECO:0000269|PubMed:16690701}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle. {ECO:0000269|PubMed:16690701}.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;pineal body;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;mammary gland;colon;parathyroid;uterus;whole body;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; whole brain;dorsal root ganglion;amygdala;thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.54349 0.60885 -0.560178693 19.30879925 14.92715 0.53756 CAMK2N1 0.138563181790624 0.625274890278808 0.236161927930568 calcium/calmodulin-dependent protein kinase II inhibitor 1 FUNCTION: Potent and specific inhibitor of CaM-kinase II (CAMK2). {ECO:0000250, ECO:0000269|PubMed:18305109}.; . TISSUE SPECIFICITY: Widely expressed. Nor detected in skeletal muscle. {ECO:0000269|PubMed:18305109}.; . . 0.32405 . 0.101211609 60.95777306 . . CAMK2N2 0.320487800680099 0.612214156105321 0.06729804321458 calcium/calmodulin-dependent protein kinase II inhibitor 2 FUNCTION: Potent and specific cellular inhibitor of CaM-kinase II (CAMK2). Traps Ca(2+)/calmodulin on CAMK2. May play an important role in the regulation of cell growth when overexpressed in colon adenocarcinoma LoVo cells. Traps Ca(2+)/calmodulin on CAMK2. {ECO:0000269|PubMed:11444830}.; . TISSUE SPECIFICITY: Expressed in cell lines including hemopoietic cell lines and some tumor cell lines. Highly Expressed in stimulated dendritic cell (DC) and weakly expressed in unstimulated mature and immature DC. Highly expressed in kidney, liver, in cell lines HeLaS3, lymphoblastic leukemia MOLT-4, and Burkitt's lymphoma Raji. Moderately expressed in heart, skeletal muscle, placenta, and chronic myelogenous leukemia K-562 cells. Weakly expressed in small intestine, colorectal adenocarcinoma SW480, and lung carcinoma A-549 cells. {ECO:0000269|PubMed:11444830}.; islets of Langerhans;brain; amygdala;superior cervical ganglion;medulla oblongata;temporal lobe;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.34324 . 0.12325821 62.38499646 3.51322 0.12799 CAMK4 0.0158296697612448 0.978793440754874 0.00537688948388152 calcium/calmodulin-dependent protein kinase IV FUNCTION: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK4 signaling cascade and regulates, mainly by phosphorylation, the activity of several transcription activators, such as CREB1, MEF2D, JUN and RORA, which play pivotal roles in immune response, inflammation, and memory consolidation. In the thymus, regulates the CD4(+)/CD8(+) double positive thymocytes selection threshold during T-cell ontogeny. In CD4 memory T-cells, is required to link T-cell antigen receptor (TCR) signaling to the production of IL2, IFNG and IL4 (through the regulation of CREB and MEF2). Regulates the differentiation and survival phases of osteoclasts and dendritic cells (DCs). Mediates DCs survival by linking TLR4 and the regulation of temporal expression of BCL2. Phosphorylates the transcription activator CREB1 on 'Ser-133' in hippocampal neuron nuclei and contribute to memory consolidation and long term potentiation (LTP) in the hippocampus. Can activate the MAP kinases MAPK1/ERK2, MAPK8/JNK1 and MAPK14/p38 and stimulate transcription through the phosphorylation of ELK1 and ATF2. Can also phosphorylate in vitro CREBBP, PRM2, MEF2A and STMN1/OP18. {ECO:0000269|PubMed:10617605, ECO:0000269|PubMed:17909078, ECO:0000269|PubMed:18829949, ECO:0000269|PubMed:7961813, ECO:0000269|PubMed:8065343, ECO:0000269|PubMed:8855261, ECO:0000269|PubMed:8980227, ECO:0000269|PubMed:9154845}.; . TISSUE SPECIFICITY: Expressed in brain, thymus, CD4 T-cells, testis and epithelial ovarian cancer tissue. {ECO:0000269|PubMed:12065094, ECO:0000269|PubMed:7961813, ECO:0000269|PubMed:8397199}.; unclassifiable (Anatomical System);bile duct;frontal lobe;hippocampus;testis;germinal center;skin; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;cerebellum peduncles;testis;ciliary ganglion;atrioventricular node;pons; 0.17354 0.13207 -0.26993514 34.59542345 177.22596 2.89202 CAMKK1 0.0632390899315781 0.936100700240601 0.000660209827820812 calcium/calmodulin-dependent protein kinase kinase 1 FUNCTION: Calcium/calmodulin-dependent protein kinase that belongs to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1, CAMK1D, CAMK1G and CAMK4. Involved in regulating cell apoptosis. Promotes cell survival by phosphorylating AKT1/PKB that inhibits pro-apoptotic BAD/Bcl2-antagonist of cell death. {ECO:0000269|PubMed:12935886}.; . . ovary;colon;parathyroid;fovea centralis;choroid;bone marrow;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;lens;skeletal muscle;lung;placenta;hippocampus;macula lutea;cervix;peripheral nerve;cerebellum; amygdala;whole brain;superior cervical ganglion;medulla oblongata;temporal lobe;pons;atrioventricular node;caudate nucleus;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.59947 0.14339 -0.576764155 18.7839113 3948.95281 12.43271 CAMKK2 0.503475917086193 0.496488678345773 3.54045680342841e-05 calcium/calmodulin-dependent protein kinase kinase 2 FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin- binding domain are inactive. Efficiently phosphorylates 5'-AMP- activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching. {ECO:0000250, ECO:0000269|PubMed:11395482, ECO:0000269|PubMed:12935886, ECO:0000269|PubMed:21957496, ECO:0000269|PubMed:9662074}.; . TISSUE SPECIFICITY: Ubiquitously expressed with higher levels in the brain. Intermediate levels are detected in spleen, prostate, thyroid and leukocytes. The lowest level is in lung. {ECO:0000269|PubMed:9662074}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;tongue;urinary;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; amygdala;whole brain;occipital lobe;superior cervical ganglion;medulla oblongata;cerebellum peduncles;temporal lobe;pons;caudate nucleus;subthalamic nucleus;liver;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.51790 0.23396 -0.26629572 34.81953291 2630.25871 9.61927 CAMKMT 5.14965805552299e-13 0.0143295330000154 0.985670466999469 calmodulin-lysine N-methyltransferase FUNCTION: Catalyzes the trimethylation of 'Lys-116' in calmodulin. {ECO:0000269|PubMed:20975703}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in brain,liver, muscle colon and lung. Isoform 2 is expressed in colon, testis, kidney and brain. Isoform 1 and isoform 2 are expressed in normal lymphoblastoid cells but not in lymphoblastoid cells from patients with hypotonia-cystinuria syndrome. {ECO:0000269|PubMed:15913950}.; . . 0.13884 . -0.449946534 24.00330267 23.97282 0.78897 CAMKV 0.996846171233152 0.00315365461947915 1.74147368968833e-07 CaM kinase-like vesicle-associated FUNCTION: Does not appear to have detectable kinase activity.; . . unclassifiable (Anatomical System);hypothalamus;fovea centralis;choroid;lens;retina;optic nerve;lung;frontal lobe;epididymis;hippocampus;visual apparatus;macula lutea;testis;brain; amygdala;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;temporal lobe;pons;atrioventricular node;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.91392 0.14754 -0.494039303 22.09247464 19.95748 0.67932 CAMLG 0.00402053963029354 0.85802871868775 0.137950741681956 calcium modulating ligand FUNCTION: Likely involved in the mobilization of calcium as a result of the TCR/CD3 complex interaction. Binds to cyclophilin B.; . TISSUE SPECIFICITY: Ubiquitous. Highest levels in brain, testis and ovary.; ovary;salivary gland;intestine;colon;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;oesophagus;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland; amygdala;whole brain;testis - interstitial;subthalamic nucleus;superior cervical ganglion;prefrontal cortex;globus pallidus;testis;ciliary ganglion;cingulate cortex; 0.08511 0.19493 -0.381986487 27.68931352 49.50924 1.37632 CAMP 0.0896557021569683 0.764603723310476 0.145740574532556 cathelicidin antimicrobial peptide FUNCTION: Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity. {ECO:0000269|PubMed:16637646, ECO:0000269|PubMed:18818205}.; . TISSUE SPECIFICITY: Expressed in bone marrow and testis and neutrophils.; myocardium;pancreas;lung;thyroid;testis;blood;germinal center;lens;bone marrow; testis;whole blood;skeletal muscle;bone marrow; 0.22459 0.17514 0.104848986 61.49445624 41.19222 1.20506 CAMSAP1 0.753664482005709 0.246334789932947 7.28061344115984e-07 calmodulin regulated spectrin associated protein 1 FUNCTION: Probable microtubule-binding protein that plays a role in the regulation of cell morphology and cytoskeletal organization. Through interaction with spectrin may regulate neurite outgrowth. {ECO:0000269|PubMed:19508979, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:24117850}.; . . ovary;parathyroid;skin;retina;bone marrow;uterus;whole body;bone;iris;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;epididymis;visual apparatus;liver;spleen;head and neck;cervix;mammary gland;stomach;peripheral nerve;thymus; amygdala;whole brain;dorsal root ganglion;testis - interstitial;superior cervical ganglion;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.19289 0.10292 -2.648011194 0.772587874 215.35431 3.16675 CAMSAP2 0.999973881501979 2.61184980087073e-05 1.21946191407261e-14 calmodulin regulated spectrin associated protein family member 2 FUNCTION: Microtubule minus-end binding protein that may regulate the organization of non-centrosomal microtubules. May regulate the nucleation and the polymerization of microtubules. Indirectly, through the microtubule cytoskeleton, may regulate the organization of cellular organelles including the Golgi and the early endosomes. {ECO:0000269|PubMed:23169647}.; DISEASE: Note=Defects in CAMSAP2 may be a cause of susceptibility to epilepsy in the Chinese population. {ECO:0000305|PubMed:22116939}.; . salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;larynx;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;stomach;aorta;thymus; medulla oblongata;superior cervical ganglion;occipital lobe;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe; 0.20006 0.10960 -0.437212558 24.67563105 187.99711 2.97712 CAMSAP3 0.999943968611488 5.60313865996979e-05 1.91179161265269e-12 calmodulin regulated spectrin associated protein family member 3 FUNCTION: Microtubule minus-end binding protein that acts as a regulator of non-centrosomal microtubule dynamics and organization. Specifically required for the biogenesis and the maintenance of zonula adherens by anchoring the minus-end of microtubules to zonula adherens and by recruiting the kinesin KIFC3 to those junctional sites. May regulate the nucleation and the polymerization of microtubules. Indirectly, through the microtubule cytoskeleton, may regulate the organization of cellular organelles including the Golgi and the early endosomes. {ECO:0000269|PubMed:19041755, ECO:0000269|PubMed:23169647}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;endometrium;bone;iris;testis;brain;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;lens;lung;cornea;placenta;macula lutea;hippocampus;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;pons;atrioventricular node;trigeminal ganglion; 0.15439 0.10718 . . 276.25374 3.55868 CAMTA1 0.999999955418418 4.45815820402636e-08 5.3963476260107e-20 calmodulin binding transcription activator 1 FUNCTION: Transcriptional activator. May act as a tumor suppressor. {ECO:0000269|PubMed:11925432, ECO:0000269|PubMed:15709179}.; DISEASE: Cerebellar ataxia, non-progressive, with mental retardation (CANPMR) [MIM:614756]: A neurodevelopmental disorder characterized by mildly delayed psychomotor development, early onset of cerebellar ataxia, and intellectual disability later in childhood and adult life. Other features may include neonatal hypotonia, dysarthria, and dysmetria. Brain imaging in some patients shows cerebellar atrophy. Dysmorphic facial features are variable. {ECO:0000269|PubMed:22693284}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Normally expressed in non-neoplastic adult central nervous system tissues: detected in whole brain, cerebellum, brain cortex, occipital lobe, frontal lobe, temporal lobe, putamen. Expression levels are low in oligodendroglial tumors, and are reduced by half in oligodendroglioma and astrocytoma cases with 1p loss of heterozygosity. Detected in neuroblastic-type cultured neuroblastoma cells. Expressed in heart and kidney. {ECO:0000269|PubMed:11925432, ECO:0000269|PubMed:15138581, ECO:0000269|PubMed:15709179}.; unclassifiable (Anatomical System);heart;hypothalamus;sympathetic chain;fovea centralis;skeletal muscle;retina;whole body;lung;frontal lobe;macula lutea;hippocampus;iris;kidney;pineal gland;brain; whole brain;amygdala;thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;liver;testis;globus pallidus;kidney;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.23599 . -2.133443765 1.503892427 1106.61409 6.35898 CAMTA1-IT1 . . . CAMTA1 intronic transcript 1 . . . . . . . . . . . CAMTA2 0.999991613720089 8.38627991057911e-06 1.55046532776624e-16 calmodulin binding transcription activator 2 FUNCTION: Transcription activator. May act as tumor suppressor. {ECO:0000269|PubMed:11925432}.; . TISSUE SPECIFICITY: Detected in brain. Expressed at constant levels throughout the cell cycle in neuroblastoma cell lines. {ECO:0000269|PubMed:11925432, ECO:0000269|PubMed:15138581}.; lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; amygdala;medulla oblongata;subthalamic nucleus;cerebellum peduncles;prefrontal cortex;globus pallidus;caudate nucleus;pons;cingulate cortex;parietal lobe;cerebellum; 0.32188 0.08974 -0.968173992 8.982071243 559.42386 4.80420 CAND1 0.999927001146307 7.29988500519133e-05 3.64158522224947e-12 cullin-associated and neddylation-dissociated 1 FUNCTION: Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor. The exchange activity of CAND1 is coupled with cycles of neddylation conjugation: in the deneddylated state, cullin-binding CAND1 binds CUL1-RBX1, increasing dissociation of the SCF complex and promoting exchange of the F-box protein. Probably plays a similar role in other cullin-RING E3 ubiquitin ligase complexes. {ECO:0000269|PubMed:12504025, ECO:0000269|PubMed:12504026, ECO:0000269|PubMed:12609982, ECO:0000269|PubMed:16449638, ECO:0000269|PubMed:21249194, ECO:0000269|PubMed:23453757}.; . . smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;pia mater;cornea;placenta;head and neck;kidney;stomach;thymus; amygdala;superior cervical ganglion;occipital lobe;fetal brain;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex; 0.34487 0.17050 -1.043396569 7.71408351 65.69716 1.67016 CAND2 4.5328114836349e-09 0.806271649262972 0.193728346204217 cullin-associated and neddylation-dissociated 2 (putative) FUNCTION: Probable assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in epididymis (at protein level). {ECO:0000269|PubMed:20736409}.; unclassifiable (Anatomical System);heart;ovary;parathyroid;fovea centralis;choroid;lens;skin;retina;optic nerve;whole body;lung;endometrium;adrenal gland;thyroid;macula lutea;visual apparatus;liver;testis;brain; testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.25408 0.11518 1.526690916 95.49422033 6172.51432 16.42964 CANDN1 . . . candidiasis, nail 1 (with ICAM1 deficiency) . . . . . . . . . . . CANT1 0.00290923611890276 0.807654984933772 0.189435778947326 calcium activated nucleotidase 1 FUNCTION: Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis. {ECO:0000269|PubMed:12234496, ECO:0000269|PubMed:15248776, ECO:0000269|PubMed:22539336}.; DISEASE: Desbuquois dysplasia 1 (DBQD1) [MIM:251450]: A chondrodysplasia characterized by severe prenatal and postnatal growth retardation (less than -5 SD), joint laxity, short extremities, progressive scoliosis, round face, midface hypoplasia, prominent bulging eyes. The main radiologic features are short long bones with metaphyseal splay, a 'Swedish key' appearance of the proximal femur (exaggerated trochanter), and advance carpal and tarsal bone age. Two forms of Desbuquois dysplasia are distinguished on the basis of the presence or absence of characteristic hand anomalies: an extra ossification center distal to the second metacarpal, delta phalanx, bifid distal thumb phalanx, and phalangeal dislocations. {ECO:0000269|PubMed:19853239, ECO:0000269|PubMed:20425819, ECO:0000269|PubMed:21037275, ECO:0000269|PubMed:21412251, ECO:0000269|PubMed:21654728, ECO:0000269|PubMed:22539336}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12234496}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;prostate;placenta;liver;testis;ciliary ganglion;trigeminal ganglion;whole blood; 0.15204 0.14174 0.022122107 55.69120075 102.29804 2.18633 CANX 0.86247386009449 0.13752259783098 3.54207453006636e-06 calnexin FUNCTION: Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor- mediated endocytosis at the synapse.; . . smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;cartilage;heart;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;amnion;head and neck;kidney;stomach; thalamus;hypothalamus;placenta;spinal cord; 0.78419 0.89499 -0.159704656 41.90846898 163.62404 2.79331 CAP1 0.585940925968321 0.413968689581175 9.03844505038787e-05 CAP, adenylate cyclase-associated protein 1 (yeast) FUNCTION: Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity.; . . lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;heart;tongue;adrenal cortex;pharynx;blood;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;cerebellum; olfactory bulb;white blood cells;whole blood; 0.21153 0.11357 -0.780646273 12.77423921 110.71742 2.29232 CAP1P1 . . . CAP1 pseudogene 1 . . . . . . . . . . . CAP1P2 . . . CAP1 pseudogene 2 . . . . . . . . . . . CAP2 0.410487087790501 0.58915700966929 0.000355902540209639 CAP, adenylate cyclase-associated protein, 2 (yeast) FUNCTION: May have a regulatory bifunctional role.; . . myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;iris;testis;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;bile duct;breast;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach; whole brain;amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;atrioventricular node;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.32334 0.10525 -0.047654689 50.22410946 486.9546 4.54178 CAP2P1 . . . CAP, adenylate cyclase-associated protein, 2 (yeast) pseudogene 1 . . . . . . . . . . . CAPG 5.32548826021192e-09 0.119711633226635 0.880288361447876 capping actin protein, gelsolin like FUNCTION: Calcium-sensitive protein which reversibly blocks the barbed ends of actin filaments but does not sever preformed actin filaments. May play an important role in macrophage function. May play a role in regulating cytoplasmic and/or nuclear structures through potential interactions with actin. May bind DNA.; . TISSUE SPECIFICITY: Macrophages and macrophage-like cells.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;cornea;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion; 0.14168 0.28063 0.50895761 80.20169851 222.11671 3.22328 CAPN1 5.00439517393622e-05 0.999644313487044 0.000305642561216693 calpain 1 FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;medulla oblongata;smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;tongue;blood;lens;breast;bile duct;pancreas;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; . 0.57188 0.34038 -0.33061537 30.82094834 627.81832 5.05141 CAPN2 1.61617931384536e-11 0.79333333055656 0.206666669427279 calpain 2 FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (PubMed:17650508). {ECO:0000269|PubMed:17650508}.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;endometrium;thyroid;amniotic fluid;brain;bladder;amygdala;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;oesophagus;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hypopharynx;amnion;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.21160 0.29838 0.7164803 85.82802548 3510.65552 11.43339 CAPN3 9.73741042585956e-09 0.995577385141066 0.00442260512152352 calpain 3 FUNCTION: Calcium-regulated non-lysosomal thiol-protease.; . TISSUE SPECIFICITY: Isoform I is skeletal muscle specific.; medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);small intestine;heart;cerebellum cortex;muscle;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;adrenal gland;macula lutea;visual apparatus;hippocampus;liver;head and neck;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;whole brain;medulla oblongata;thalamus;testis - interstitial;superior cervical ganglion;occipital lobe;tongue;hypothalamus;spinal cord;atrioventricular node;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion;parietal lobe;cingulate cortex; 0.78952 0.10758 -0.701780438 14.81481481 2863.48714 10.12571 CAPN5 3.53957426282048e-07 0.935601785871717 0.0643978601708565 calpain 5 . . TISSUE SPECIFICITY: Expressed in many tissues. Strong expression in the photoreceptor cells of the retina, with a punctate pattern of labeling over the nuclei and inner segments with less expression along the other segments and outer plexiform layer. {ECO:0000269|PubMed:23055945}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;testis;spinal ganglion;pineal gland;brain;gall bladder;unclassifiable (Anatomical System);amygdala;heart;lens;bile duct;lung;epididymis;nasopharynx;macula lutea;hippocampus;visual apparatus;liver;spleen;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.23811 0.11589 -0.903841325 10.14390186 410.70074 4.24742 CAPN6 0.984532250609268 0.0154660241241836 1.72526654841126e-06 calpain 6 FUNCTION: Microtubule-stabilizing protein that may be involved in the regulation of microtubule dynamics and cytoskeletal organization. May act as a regulator of RAC1 activity through interaction with ARHGEF2 to control lamellipodial formation and cell mobility. Does not seem to have protease activity as it has lost the active site residues (By similarity). {ECO:0000250, ECO:0000269|PubMed:17210638}.; . TISSUE SPECIFICITY: Expressed only in placenta.; unclassifiable (Anatomical System);cartilage;heart;muscle;colon;skin;skeletal muscle;retina;uterus;prostate;whole body;lung;endometrium;larynx;bone;thyroid;placenta;visual apparatus;alveolus;liver;testis;head and neck;spleen;kidney;aorta;stomach; superior cervical ganglion;uterus corpus;placenta;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.63626 0.14666 0.128714042 63.19886766 1122.4492 6.39659 CAPN7 5.28615018685299e-07 0.999647032065226 0.000352439319755565 calpain 7 FUNCTION: Calcium-regulated non-lysosomal thiol-protease. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;testis - interstitial;trigeminal ganglion; 0.09928 0.10755 -0.486758915 22.69992923 373.19203 4.07493 CAPN8 0.0151809363825236 0.455705816568418 0.529113247049058 calpain 8 FUNCTION: Calcium-regulated non-lysosomal thiol-protease. Involved in membrane trafficking in the gastric surface mucus cells (pit cells) and may involve the membrane trafficking of mucus cells via interactions with coat protein. Proteolytically cleaves the beta- subunit of coatomer complex (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Stomach.; . . 0.06577 . . . 11836.63705 23.51805 CAPN9 1.73327533297539e-11 0.805828751134411 0.194171248848256 calpain 9 FUNCTION: Calcium-regulated non-lysosomal thiol-protease.; . TISSUE SPECIFICITY: Expressed predominantly in stomach.; unclassifiable (Anatomical System);prostate;whole body;endometrium;nasopharynx;colon;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.06312 0.09013 1.120636874 92.10309035 4397.74449 13.25652 CAPN10 2.37881013810975e-08 0.695060209575177 0.304939766636721 calpain 10 FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. May play a role in insulin-stimulated glucose uptake. {ECO:0000269|PubMed:17572128}.; . TISSUE SPECIFICITY: Detected in primary skeletal muscle cells (at protein level). Ubiquitous. {ECO:0000269|PubMed:17572128}.; lymphoreticular;colon;choroid;fovea centralis;skin;retina;uterus;prostate;whole body;optic nerve;endometrium;larynx;thyroid;testis;brain;tonsil;unclassifiable (Anatomical System);lacrimal gland;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;hippocampus;macula lutea;head and neck;spleen;cervix; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;adrenal cortex;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06932 0.21140 -0.325161626 30.92120783 177.2342 2.89245 CAPN10-AS1 . . . CAPN10 antisense RNA 1 (head to head) . . . . . . . . . . . CAPN11 2.97448051307409e-10 0.709669547457523 0.290330452245029 calpain 11 FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.; . TISSUE SPECIFICITY: Highest expression in testis. {ECO:0000269|PubMed:10409436}.; . . 0.16393 0.08897 0.780798785 87.24345364 2981.33534 10.36052 CAPN12 7.47956767719308e-20 0.0004919439260608 0.999508056073939 calpain 12 FUNCTION: Calcium-regulated non-lysosomal thiol-protease. {ECO:0000250}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; . 0.38998 0.11824 -0.523584927 20.93654164 2537.68423 9.40302 CAPN13 1.83080779880556e-09 0.840543318568473 0.159456679600719 calpain 13 FUNCTION: Probable non-lysosomal thiol-protease. {ECO:0000250}.; . TISSUE SPECIFICITY: Weakly expressed in lung and testis. Weakly or not expressed in other tissues. {ECO:0000269|PubMed:11675017}.; unclassifiable (Anatomical System);ovary;tongue;islets of Langerhans;colon;skeletal muscle;uterus;breast;prostate;lung;endometrium;nasopharynx;head and neck;kidney; . 0.06067 0.07796 -0.28106828 33.55744279 1213.56215 6.59272 CAPN14 . . . calpain 14 FUNCTION: Calcium-regulated non-lysosomal thiol-protease. {ECO:0000250}.; . TISSUE SPECIFICITY: Not expressed in tissues tested.; . . . . 2.664347924 98.844067 6196.21935 16.44921 CAPN15 0.965209511170234 0.0347899652363703 5.23593396158669e-07 calpain 15 . . TISSUE SPECIFICITY: Widely expressed with higher expression in brain. {ECO:0000269|PubMed:9722942}.; . . 0.17839 0.12009 . . 1406.85106 7.00817 CAPNS1 0.000124379798692998 0.955664808847942 0.0442108113533651 calpain small subunit 1 FUNCTION: Regulatory subunit of the calcium-regulated non- lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.; . . myocardium;lymphoreticular;ovary;sympathetic chain;skin;retina;prostate;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;tonsil;heart;tongue;adrenal cortex;pharynx;blood;lens;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;vein;uterus;whole body;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus;cerebellum; heart;kidney; 0.08365 0.34122 -0.273576253 33.97027601 297.0565 3.67821 CAPNS1P1 . . . calpain small subunit 1 pseudogene 1 . . . . . . . . . . . CAPNS2 0.131736738431294 0.780171659007117 0.0880916025615886 calpain small subunit 2 FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. This small subunit may act as a tissue-specific chaperone of the large subunit, possibly by helping it fold into its correct conformation for activity.; . . . . . . 0.791937896 87.33781552 150.71612 2.68154 CAPRIN1 0.999767661808702 0.000232338178932306 1.23659372184872e-11 cell cycle associated protein 1 FUNCTION: May regulate the transport and translation of mRNAs of proteins involved in synaptic plasticity in neurons and cell proliferation and migration in multiple cell types. {ECO:0000250, ECO:0000269|PubMed:17210633}.; . TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.46723 0.08832 -0.516085732 21.20193442 47.96186 1.34563 CAPRIN2 0.0120891274382742 0.98790812532863 2.74723309555731e-06 caprin family member 2 FUNCTION: May regulate the transport and translation of mRNAs, modulating for instance the expression of proteins involved in synaptic plasticity in neurons. Involved in regulation of growth as erythroblasts shift from a highly proliferative state towards their terminal phase of differentiation. May be involved in apoptosis. {ECO:0000269|PubMed:14593112}.; . TISSUE SPECIFICITY: Detected in all tissues tested with highest levels of expression in brain and spleen. {ECO:0000269|PubMed:14593112}.; smooth muscle;ovary;sympathetic chain;colon;substantia nigra;parathyroid;vein;skin;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;colorectal;blood;lens;skeletal muscle;bile duct;lung;placenta;visual apparatus;hippocampus;duodenum;alveolus;liver;head and neck;spleen;kidney;mammary gland;stomach;aorta; dorsal root ganglion;hypothalamus;prefrontal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.74395 0.09642 -0.525400547 20.91295117 497.73137 4.58496 CAPS 5.18362462737594e-07 0.0685246466028812 0.931474835034656 calcyphosine FUNCTION: Calcium-binding protein. May play a role in cellular signaling events (Potential). {ECO:0000305}.; . . colon;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;pharynx;lens;breast;lung;placenta;macula lutea;liver;spleen;kidney; superior cervical ganglion;trachea;thyroid;temporal lobe;atrioventricular node;caudate nucleus;skeletal muscle; 0.13335 . 0.464864541 78.69190847 599.62745 4.95583 CAPS2 2.65069655043534e-09 0.272459498296026 0.727540499053277 calcyphosine 2 . . TISSUE SPECIFICITY: Abundantly expressed in many tissues. Expressed in brain, colon, heart, kidney, liver, lung, liver, pancreas, placenta, skeletal muscle, testis and thymus. Highest expression in colon, testis, lung, placenta and brain. {ECO:0000269|PubMed:11846421}.; unclassifiable (Anatomical System);prostate;lung;cochlea;endometrium;pituitary gland;brain;mammary gland; ciliary ganglion;atrioventricular node; 0.07900 0.09221 0.198490371 67.30360934 2043.71225 8.33443 CAPSL 0.000440614569244343 0.654428139627352 0.345131245803404 calcyphosine like . . . . . 0.10216 0.11830 -0.093566408 46.7386176 148.53852 2.65896 CAPZA1 0.983027524743633 0.0169617754125063 1.06998438606411e-05 capping actin protein of muscle Z-line alpha subunit 1 FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.; . . smooth muscle;ovary;sympathetic chain;rectum;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;blood;lens;skeletal muscle;breast;macula lutea;liver;alveolus;cervix;mammary gland;developmental;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;head and neck;kidney;stomach;cerebellum; testis;white blood cells;whole blood; 0.74477 0.17622 0.349177632 74.18023119 128.49375 2.46981 CAPZA1P . . . capping actin protein of muscle Z-line alpha subunit 1 pseudogene . . . . . . . . . . . CAPZA2 0.986605820644033 0.0133881975509945 5.98180497200088e-06 capping actin protein of muscle Z-line alpha subunit 2 FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;ganglion;endometrium;germinal center;bladder;brain;heart;cartilage;urinary;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;dura mater;spinal ganglion;artery;unclassifiable (Anatomical System);meninges;small intestine;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;kidney;aorta;stomach; amygdala;whole blood; 0.52411 0.22085 0.193034296 66.82000472 40.992 1.20125 CAPZA3 0.000212651606249841 0.497071195683642 0.502716152710108 capping actin protein of muscle Z-line alpha subunit 3 FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the morphogenesis of spermatid (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed exclusively in testis and sperm. Highest expression is found in the neck region of ejaculated sperm with lower levels found in the tail and postacrosome region. {ECO:0000269|PubMed:12029070}.; unclassifiable (Anatomical System);medulla oblongata;lung;testis; testis - interstitial;testis - seminiferous tubule;testis; 0.25246 0.09986 0.086440867 60.47416844 68.37274 1.71080 CAPZB 0.592160351133202 0.40576873324393 0.00207091562286798 capping actin protein of muscle Z-line beta subunit FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:21834987}.; . . myocardium;lymphoreticular;ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; amygdala;superior cervical ganglion;testis - interstitial;prostate;testis - seminiferous tubule;thyroid;testis;cerebellum; 0.20910 0.12018 -0.163345027 41.24793583 18.76827 0.64802 CARD6 1.45631048490053e-16 0.00309678185804033 0.996903218141959 caspase recruitment domain family member 6 FUNCTION: May be involved in apoptosis.; . . unclassifiable (Anatomical System);lacrimal gland;urinary;colon;skeletal muscle;uterus;breast;pancreas;lung;larynx;nasopharynx;bone;thyroid;liver;head and neck;spleen;aorta; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.03526 0.06855 1.785787059 96.86836518 665.78631 5.16443 CARD8 0.0162893753878883 0.959419920598632 0.0242907040134795 caspase recruitment domain family member 8 FUNCTION: Inhibits NF-kappa-B activation. May participate in a regulatory mechanism that coordinates cellular responses controlled by NF-kappa-B transcription factor. May be a component of the inflammasome, a protein complex which also includes PYCARD, NALP2 and CASP1 and whose function would be the activation of proinflammatory caspases.; . TISSUE SPECIFICITY: High expression in lung, ovary, testis and placenta. Lower expression in heart, kidney and liver. Also expressed in spleen, lymph node and bone marrow.; medulla oblongata;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;lens;skeletal muscle;bile duct;lung;placenta;macula lutea;liver;head and neck;kidney;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.06736 0.06344 1.179479654 92.79311158 583.37004 4.89784 CARD8-AS1 . . . CARD8 antisense RNA 1 . . . . . . . . . . . CARD9 2.29038097230092e-11 0.0358146675831327 0.964185332393963 caspase recruitment domain family member 9 FUNCTION: Adapter protein that plays a key role in innate immune response to a number of intracellular pathogens, such as C.albicans and L.monocytogenes. Is at the crossroads of ITAM- tyrosine kinase and the Toll-like receptors (TLR) and NOD2 signaling pathways. Probably controls various innate immune response pathways depending on the intracellular pathogen. In response to L.monocytogenes infection, acts by connecting NOD2 recognition of peptidoglycan to downstream activation of MAP kinases (MAPK) without activating NF-kappa-B. Also involved in activation of myeloid cells via classical ITAM-associated receptors and TLR: required for TLR-mediated activation of MAPK, while it is not required for TLR-induced activation of NF-kappa-B (By similarity). Controls CLEC7A (dectin-1)-mediated myeloid cell activation induced by the yeast cell wall component zymosan, leading to cytokine production and innate anti-fungal immunity: acts by regulating BCL10-MALT1-mediated NF-kappa-B activation pathway. Activates NF-kappa-B via BCL10. In response to the hyphal form of C.albicans, mediates CLEC6A (dectin-2)-induced I-kappa-B kinase ubiquitination, leading to NF-kappa-B activation via interaction with BCL10. In response to fungal infection, may be required for the development and subsequent differentiation of interleukin 17-producing T helper (TH-17) cells. {ECO:0000250, ECO:0000269|PubMed:11053425}.; DISEASE: Candidiasis, familial, 2 (CANDF2) [MIM:212050]: A primary immunodeficiency disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans. {ECO:0000269|PubMed:19864672, ECO:0000269|PubMed:23335372, ECO:0000269|PubMed:24131138}. Note=The disease is caused by mutations affecting the gene represented in this entry. Defects induce reduced numbers of CD4(+) Th17 lymphocytes as well as a lack of monocyte-derived cytokines in response to Candida strains. Neutrophils show a selective Candida albicans killing defect with abnormal ultrastructural phagolysosomes and outgrowth of hyphae (PubMed:23335372). {ECO:0000269|PubMed:23335372}.; TISSUE SPECIFICITY: Highly expressed in spleen. Also detected in liver, placenta, lung, peripheral blood leukocytes and in brain.; unclassifiable (Anatomical System);uterus;lung;lacrimal gland;placenta;visual apparatus;testis;spleen;kidney;brain;bone marrow; superior cervical ganglion;skeletal muscle; 0.09281 0.13929 -0.593358137 18.22953527 1504.351 7.21015 CARD10 0.10891986887678 0.891069149144053 1.09819791671696e-05 caspase recruitment domain family member 10 FUNCTION: Activates NF-kappa-B via BCL10 and IKK.; . TISSUE SPECIFICITY: Detected in adult heart, kidney and liver; lower levels in intestine, placenta, muscle and lung. Also found in fetal lung, liver and kidney.; unclassifiable (Anatomical System);heart;islets of Langerhans;colon;blood;fovea centralis;choroid;lens;skin;retina;bile duct;pancreas;prostate;optic nerve;lung;endometrium;placenta;macula lutea;visual apparatus;liver;testis;cervix;kidney;stomach; superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.12545 0.09374 -1.148192153 6.316348195 2535.91579 9.39915 CARD11 0.999939282123249 6.07178767318184e-05 1.92615753264165e-14 caspase recruitment domain family member 11 FUNCTION: Involved in the costimulatory signal essential for T- cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Activates NF-kappa-B via BCL10 and IKK. Stimulates the phosphorylation of BCL10.; DISEASE: B-cell expansion with NFKB and T-cell anergy (BENTA) [MIM:616452]: An autosomal dominant condition characterized by onset in infancy of splenomegaly and polyclonal expansion of B cells, resulting in peripheral lymphocytosis. Affected individuals also show mild immune dysfunction, including some defective antibody responses and T-cell anergy. There may be a predisposition to the development of B-cell malignancy. {ECO:0000269|PubMed:23129749}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Immunodeficiency 11 (IMD11) [MIM:615206]: An autosomal recessive primary immunodeficiency characterized by normal numbers of T and B-lymphocytes, but defective intracellular signaling. There is a block in B-cell differentiation with increased numbers of transitional B-cells and hypogammaglobulinemia, as well as decreased numbers of regulatory T-cells and defects in T-cell function. {ECO:0000269|PubMed:23374270}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in adult peripheral blood leukocytes, thymus, spleen and liver. Also found in promyelocytic leukemia HL- 60 cells, chronic myelogenous leukemia K-562 cells, Burkitt's lymphoma Raji cells and colorectal adenocarcinoma SW480 cells. Not detected in HeLaS3, MOLT-4, A-549 and G431 cells. {ECO:0000269|PubMed:11278692}.; lymphoreticular;ovary;parathyroid;skin;uterus;prostate;cerebral cortex;thyroid;testis;germinal center;bladder;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;stomach;thymus; white blood cells; 0.09614 0.27346 -1.385325458 4.334748762 173.34725 2.86659 CARD14 3.14969356207765e-14 0.244176906374707 0.755823093625262 caspase recruitment domain family member 14 FUNCTION: Plays a role in signaling mediated by TRAF2, TRAF3 and TRAF6 and protects cells against apoptosis. Activates NF-kappa-B via BCL10 and IKK. Stimulates the phosphorylation of BCL10. {ECO:0000269|PubMed:21302310}.; DISEASE: Pityriasis rubra pilaris (PRP) [MIM:173200]: A rare, papulosquamous skin disease characterized by the appearance of keratotic follicular papules, well-demarcated salmon-colored erythematous plaques covered with fine powdery scales interspersed with distinct islands of uninvolved skin, and palmoplantar keratoderma. Most cases are sporadic. The rare familial cases show autosomal dominant inheritance with incomplete penetrance and variable expression. Familial PRP usually presents at birth or appears during the first years of life and runs a chronic course. It is characterized by prominent follicular hyperkeratosis, diffuse palmoplantar keratoderma, and erythema. {ECO:0000269|PubMed:22703878}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is detected in placenta and epidermal keratinocytes. Isoform 2 is detected in leukocytes and fetal brain. {ECO:0000269|PubMed:22521418}.; unclassifiable (Anatomical System);uterus;pancreas;bone;placenta;liver;cervix;spleen;brain;mammary gland;skeletal muscle; superior cervical ganglion;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.09251 0.12826 0.885436112 89.07761264 2580.56011 9.49890 CARD16 0.0401643320693458 0.841772363544825 0.118063304385829 caspase recruitment domain family member 16 FUNCTION: Caspase inhibitor. Acts as a regulator of procaspase- 1/CASP1 activation implicated in the regulation of the proteolytic maturation of pro-interleukin-1 beta (IL1B) and its release during inflammation. Inhibits the release of IL1B in response to LPS in monocytes. Also induces NF-kappa-B activation during the pro- inflammatory cytokine response. Also able to inhibit CASP1- mediated neuronal cell death, TNF-alpha, hypoxia-, UV-, and staurosporine-mediated cell death but not ER stress-mediated cell death. Acts by preventing activation of caspases CASP1 and CASP4, possibly by preventing the interaction between CASP1 and RIPK2. {ECO:0000269|PubMed:11432859, ECO:0000269|PubMed:11536016, ECO:0000269|PubMed:16920334}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in placenta, spleen, lymph node and bone marrow. Weakly or not expressed in thymus. {ECO:0000269|PubMed:11432859, ECO:0000269|PubMed:11536016}.; . . . . 0.194852702 67.03231894 401.50773 4.20277 CARD17 0.000301791817816637 0.351868070723695 0.647830137458489 caspase recruitment domain family member 17 FUNCTION: Regulator of procaspase-1/CASP1 activation implicated in the regulation of the proteolytic maturation of pro-IL-1beta/IL1B and its release during inflammation. Inhibits the release of IL1B in response to LPS in monocytes. However, unlike CASP1, do not induce NF-kappa-B activation. {ECO:0000269|PubMed:15383541}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15383541}.; . . . 0.09171 1.23654218 93.29440906 330.87485 3.86771 CARD18 0.0487537469113847 0.68440983153577 0.266836421552845 caspase recruitment domain family member 18 FUNCTION: Inhibits generation of IL-1-beta by interacting with caspase-1 and preventing its association with RIP2. Down-regulates the release of IL1B. {ECO:0000269|PubMed:11051551}.; . TISSUE SPECIFICITY: Primarily expressed in the heart and placenta. {ECO:0000269|PubMed:11051551}.; . . . . 0.169169615 65.33380514 22.28015 0.74684 CARD19 . . . caspase recruitment domain family member 19 FUNCTION: Plays a role in inhibiting the effects of BCL10-induced activation of NF-kappa-B. May inhibit the phosphorylation of BCL10 in a CARD-dependent manner. {ECO:0000269|PubMed:15637807}.; . TISSUE SPECIFICITY: Expressed in ovary, testis, placenta, skeletal muscle, kidney, lung, heart and liver (at protein level). Expressed in thymus and brain. {ECO:0000269|PubMed:15637807}.; . . 0.10019 . -0.249709319 35.74545883 . . CARF 0.00454103717523082 0.994085592595259 0.00137337022951009 calcium responsive transcription factor FUNCTION: Acts as a transcriptional activator that mediates the calcium- and neuron-selective induction of BDNF exon III transcription. Binds to the consensus calcium-response element CaRE1 5'-CTATTTCGAG-3' sequence. {ECO:0000269|PubMed:11832226, ECO:0000269|PubMed:22174809}.; . . . . 0.21457 0.10537 0.156217551 64.82071243 431.63079 4.33690 CARHSP1 . . . calcium regulated heat stable protein 1 FUNCTION: Binds mRNA and regulates the stability of target mRNA. Binds single-stranded DNA (in vitro). {ECO:0000269|PubMed:21078874, ECO:0000269|PubMed:21177848}.; . . smooth muscle;ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;prostate;whole body;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; testis - seminiferous tubule;placenta;testis;trigeminal ganglion; 0.41374 0.11479 -0.780646273 12.77423921 15.39514 0.55241 CARM1 0.999357708272541 0.000642288130091109 3.59736812658103e-09 coactivator associated arginine methyltransferase 1 FUNCTION: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg- 2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA- stabilizing properties and the half-life of their target mRNAs. {ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:19405910}.; . TISSUE SPECIFICITY: Overexpressed in prostate adenocarcinomas and high-grade prostatic intraepithelial neoplasia. {ECO:0000269|PubMed:15221992}.; medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;larynx;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; testis - seminiferous tubule;testis;globus pallidus;skeletal muscle; 0.18041 0.28339 -1.001120478 8.321538099 107.90227 2.25595 CARM1P1 . . . coactivator associated arginine methyltransferase 1 pseudogene 1 . . . . . . . . . . . CARMN . . . cardiac mesoderm enhancer-associated non-coding RNA . . . . . . . . . . . CARNMT1 . . . carnosine N-methyltransferase 1 FUNCTION: N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L- histidine), is an abundant constituent of vertebrate skeletal muscles. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA- His). {ECO:0000269|PubMed:26001783}.; . TISSUE SPECIFICITY: Expressed at higher level in kidney. Expressed at lower level in brain and skeletal musclea. {ECO:0000269|PubMed:26001783}.; . . 0.46262 0.11262 -0.295622497 32.61972163 . . CARNS1 0.0221290003969173 0.909911021109618 0.0679599784934644 carnosine synthase 1 FUNCTION: Catalyzes the synthesis of carnosine and homocarnosine. Carnosine is synthesized more efficiently than homocarnosine. {ECO:0000269|PubMed:20097752}.; . . uterus;lung;frontal lobe;ovary;thyroid;kidney;brain;skeletal muscle; occipital lobe;medulla oblongata;superior cervical ganglion;hypothalamus;spinal cord;prefrontal cortex;pons;caudate nucleus;parietal lobe;cingulate cortex; . . . . 1966.8205 8.17108 CARS 2.96288607598974e-06 0.999273135194712 0.000723901919212392 cysteinyl-tRNA synthetase . DISEASE: Note=A chromosomal aberration involving CARS is associated with inflammatory myofibroblastic tumors (IMTs). Translocation t(2;11)(p23;p15) with ALK.; . lymphoreticular;smooth muscle;ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;muscle;adrenal cortex;pharynx;blood;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex; 0.17352 0.23298 -0.394936437 27.02878037 1461.59792 7.13029 CARS-AS1 . . . CARS antisense RNA 1 . . . . . . . . . . . CARS2 0.0404651180857425 0.958208132878404 0.0013267490358537 cysteinyl-tRNA synthetase 2, mitochondrial (putative) . . . lymphoreticular;ovary;colon;substantia nigra;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;bone;iris;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion; 0.09137 0.20773 0.091899012 60.68058504 1175.1742 6.51340 CARSP1 . . . cysteinyl-tRNA synthetase pseudogene 1 . . . . . . . . . . . CARSP2 . . . cysteinyl-tRNA synthetase pseudogene 2 . . . . . . . . . . . CARTPT 0.420347162514966 0.545268434704769 0.0343844027802653 CART prepropeptide FUNCTION: Satiety factor closely associated with the actions of leptin and neuropeptide y; this anorectic peptide inhibits both normal and starvation-induced feeding and completely blocks the feeding response induced by neuropeptide Y and regulated by leptin in the hypothalamus. It promotes neuronal development and survival in vitro. {ECO:0000269|PubMed:9590691}.; . TISSUE SPECIFICITY: Hypothalamus. Found in neurons of the ventrolateral part of the arcuate nucleus, in the external zone of the median eminence, and also found in terminals in the periventricular part of the paraventricular nucleus.; unclassifiable (Anatomical System);medulla oblongata;heart;hypothalamus;spinal cord;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;whole body;lung;adrenal gland;macula lutea;hippocampus;pituitary gland; amygdala;superior cervical ganglion;thalamus;hypothalamus;adrenal cortex;pons; 0.36401 0.16875 0.325313577 73.11276244 24.39966 0.80284 CASC1 8.0583173448997e-12 0.651961264791286 0.348038735200655 cancer susceptibility candidate 1 . . . unclassifiable (Anatomical System);lymph node;ovary;heart;salivary gland;intestine;colon;pharynx;blood;skin;breast;prostate;lung;endometrium;visual apparatus;liver;testis;head and neck;spleen;kidney;germinal center;brain;bladder; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;skin; 0.14848 0.08573 -0.396754488 26.97570182 2959.57853 10.30776 CASC2 . . . cancer susceptibility candidate 2 (non-protein coding) FUNCTION: May act as a potential tumor suppressor. {ECO:0000269|PubMed:15024726, ECO:0000269|PubMed:17352238}.; . TISSUE SPECIFICITY: Expressed in normal and neoplastic endometrial tissues. {ECO:0000269|PubMed:15024726}.; . . 0.11540 . . . . . CASC3 0.913674728687448 0.0863250590992821 2.12213270049658e-07 cancer susceptibility candidate 3 FUNCTION: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA- helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Binds poly(G) and poly(U) RNA homopolymer. {ECO:0000269|PubMed:17375189, ECO:0000269|PubMed:17652158}.; . TISSUE SPECIFICITY: Widely expressed. Overexpressed in breast cancers and metastasis, as well as in gastric cancers. {ECO:0000269|PubMed:12080473}.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;pineal body;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta;cerebellum;thymus; parietal lobe; 0.09632 0.11080 -0.88906181 10.36801132 550.62876 4.77143 CASC4 0.000967729828290193 0.986620591261443 0.0124116789102666 cancer susceptibility candidate 4 . . . smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;tongue;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;lung;adrenal gland;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta;cerebellum; occipital lobe;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;skeletal muscle; 0.09204 . 0.018483465 55.44939844 79.9354 1.89097 CASC4P1 . . . cancer susceptibility candidate 4 pseudogene 1 . . . . . . . . . . . CASC5 0.0237167187203929 0.976283272876529 8.40307783416755e-09 cancer susceptibility candidate 5 FUNCTION: Performs two crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Required for attachment of the kinetochores to the spindle microtubules. Directly links BUB1 and BUB1B to kinetochores. Part of the MIS12 complex, which may be fundamental for kinetochore formation and proper chromosome segregation during mitosis. Acts in coordination with CENPK to recruit the NDC80 complex to the outer kinetochore. {ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:17981135, ECO:0000269|PubMed:18045986}.; DISEASE: Microcephaly 4, primary, autosomal recessive (MCPH4) [MIM:604321]: A disease defined as a head circumference more than 3 standard deviations below the age-related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. Despite this marked reduction in size, the gyral pattern is relatively well preserved, with no major abnormality in cortical architecture. Affected individuals are mentally retarded. Primary microcephaly is further defined by the absence of other syndromic features or significant neurological deficits due to degenerative brain disorder. {ECO:0000269|PubMed:22983954}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in testis, where it is localized in germ cells, in particular in spermatocytes and in the pre-acrosome of round spermatids. Detected in the acrosome of ejaculated spermatozoa. Detected in adult thymus, bone marrow, colon, small intestine, appendix and placenta, and in fetal liver and thymus. {ECO:0000269|PubMed:10980622, ECO:0000269|PubMed:12087463, ECO:0000269|PubMed:12618768}.; unclassifiable (Anatomical System);tongue;liver;testis;colon;blood;head and neck;kidney;germinal center;skeletal muscle; dorsal root ganglion;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08184 0.10206 1.646179058 96.19013918 3263.34266 10.90201 CASC6 . . . cancer susceptibility candidate 6 (non-protein coding) . . . . . . . . . . . CASC7 . . . cancer susceptibility candidate 7 (non-protein coding) . . . . . . . . . . . CASC8 . . . cancer susceptibility candidate 8 (non-protein coding) . . . . . . . . . . . CASC9 . . . cancer susceptibility candidate 9 (non-protein coding) . . . . . . . . . . . CASC10 0.02005486166772 0.743458278808238 0.236486859524042 cancer susceptibility candidate 10 . . . . . 0.06304 . . . 34.39249 1.05159 CASC11 . . . cancer susceptibility candidate 11 (non-protein coding) . . . . . . . . . . . CASC15 . . . cancer susceptibility candidate 15 (non-protein coding) . . . . . . . . . . . CASC16 . . . cancer susceptibility candidate 16 (non-protein coding) . . . . . . . . . . . CASC17 . . . cancer susceptibility candidate 17 (non-protein coding) . . . . . . . . . . . CASC18 . . . cancer susceptibility candidate 18 (non-protein coding) . . . . . . . . . . . CASC19 . . . cancer susceptibility candidate 19 (non-protein coding) . . . . . . . . . . . CASC20 . . . cancer susceptibility candidate 20 (non-protein coding) . . . . . . . . . . . CASC21 . . . cancer susceptibility candidate 21 (non-protein coding) . . . . . . . . . . . CASC22 . . . cancer susceptibility candidate 22 (non-protein coding) . . . . . . . . . . . CASC23 . . . cancer susceptibility candidate 23 (non-protein coding) . . . . . . . . . . . CASD1 0.0367943378808448 0.963142609288369 6.30528307860991e-05 CAS1 domain containing 1 . . . ovary;colon;fovea centralis;choroid;retina;optic nerve;whole body;endometrium;bone;pituitary gland;testis;germinal center;artery;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;kidney;stomach;aorta;cerebellum; amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;parietal lobe; 0.33049 . -0.642904474 16.62538335 189.4322 2.98771 CASK 0.999885704504806 0.000114295484339965 1.08543522289349e-11 calcium/calmodulin-dependent serine protein kinase (MAGUK family) FUNCTION: Multidomain scaffolding protein with a role in synaptic transmembrane protein anchoring and ion channel trafficking. Contributes to neural development and regulation of gene expression via interaction with the transcription factor TBR1. Binds to cell-surface proteins, including amyloid precursor protein, neurexins and syndecans. May mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1.; DISEASE: Mental retardation and microcephaly with pontine and cerebellar hypoplasia (MICPCH) [MIM:300749]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Affected individuals can manifest a severe phenotype consisting of severe intellectual deficit, congenital or postnatal microcephaly, disproportionate brainstem and cerebellar hypoplasia. A milder phenotype consists of mental retardation alone or associated with nystagmus. {ECO:0000269|PubMed:19165920, ECO:0000269|PubMed:19377476}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: FG syndrome 4 (FGS4) [MIM:300422]: FG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation. {ECO:0000269|PubMed:19200522}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Expression is significantly greater in brain relative to kidney, lung, and liver and in fetal brain and kidney relative to lung and liver. {ECO:0000269|PubMed:11003712}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;cochlea;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;medulla oblongata;superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skin; 0.99640 0.27748 -0.714505427 14.4019816 13.18672 0.48013 CASK-AS1 . . . CASK antisense RNA 1 . . . . . . . . . . . CASKIN1 0.999956295373995 4.3704624961439e-05 1.04375183858822e-12 CASK interacting protein 1 FUNCTION: May link the scaffolding protein CASK to downstream intracellular effectors. {ECO:0000250}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;iris;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;uterus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;thymus; . 0.23556 0.11347 . . 504.89212 4.61185 CASKIN2 0.999986554679267 1.34453204405202e-05 2.92044665084405e-13 CASK interacting protein 2 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;testis;brain;pineal gland;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach;thymus; dorsal root ganglion;olfactory bulb;adrenal gland;placenta;prefrontal cortex;ciliary ganglion;kidney;skeletal muscle;cerebellum; 0.22834 0.10646 -0.516330081 20.97192734 355.4194 3.99007 CASKP1 . . . calcium/calmodulin-dependent serine protein kinase (MAGUK family) pseudogene 1 . . . . . . . . . . . CASP1 0.13679833104076 0.858883609461115 0.00431805949812465 caspase 1 FUNCTION: Thiol protease that cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. Important for defense against pathogens. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Can also promote apoptosis. {ECO:0000269|PubMed:15498465, ECO:0000269|PubMed:7876192}.; . TISSUE SPECIFICITY: Expressed in larger amounts in spleen and lung. Detected in liver, heart, small intestine, colon, thymus, prostate, skeletal muscle, peripheral blood leukocytes, kidney and testis. No expression in the brain. {ECO:0000269|PubMed:15498465}.; unclassifiable (Anatomical System);heart;colon;skin;uterus;prostate;lung;nasopharynx;liver;testis;head and neck;spleen;germinal center;kidney;stomach; dorsal root ganglion;superior cervical ganglion;white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle; 0.09657 0.58605 0.440999548 77.79547063 64.19975 1.64317 CASP1P1 . . . caspase 1 pseudogene 1 . . . . . . . . . . . CASP1P2 . . . caspase 1 pseudogene 2 . . . . . . . . . . . CASP1P3 . . . caspase 1 pseudogene 3 . . . . . . . . . . . CASP2 0.4231010544127 0.57657563318907 0.000323312398230724 caspase 2 FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival.; . TISSUE SPECIFICITY: Expressed at higher levels in the embryonic lung, liver and kidney than in the heart and brain. In adults, higher level expression is seen in the placenta, lung, kidney, and pancreas than in the heart, brain, liver and skeletal muscle.; lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;larynx;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.25637 0.21269 -0.646543901 16.44255721 301.85438 3.70054 CASP3 0.184808404916883 0.803415675045184 0.0117759200379335 caspase 3 FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage. {ECO:0000269|PubMed:21357690, ECO:0000269|PubMed:7596430}.; . TISSUE SPECIFICITY: Highly expressed in lung, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;pharynx;blood;skeletal muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.94154 0.98740 -0.383807564 27.41802312 26.97618 0.87123 CASP3P1 . . . caspase 3 pseudogene 1 . . . . . . . . . . . CASP4 8.20826546130762e-07 0.498566998417837 0.501432180755617 caspase 4 FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Involved in ER-stress induced apoptosis. Cleaves caspase-1. {ECO:0000269|PubMed:15123740, ECO:0000269|Ref.15}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in spleen and lung. Moderate expression in heart and liver, low expression in skeletal muscle, kidney and testis. Not found in the brain.; ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;whole blood;skeletal muscle; 0.26187 0.24599 0.222355725 68.44184949 47.17407 1.33022 CASP5 8.10674722109889e-09 0.273167234956693 0.72683275693656 caspase 5 FUNCTION: Mediator of programmed cell death (apoptosis).; . TISSUE SPECIFICITY: Expressed in barely detectable amounts in most tissues except brain, highest levels being found in lung, liver and skeletal muscle.; unclassifiable (Anatomical System);pancreas;heart;colon; superior cervical ganglion;tongue;pons; 0.11930 0.11456 1.199707453 92.98183534 431.34997 4.33449 CASP6 0.000855157619243091 0.789061340122651 0.210083502258106 caspase 6 FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves poly(ADP-ribose) polymerase in vitro, as well as lamins. Overexpression promotes programmed cell death.; . . ovary;parathyroid;choroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;alveolus;cervix;kidney;stomach; trigeminal ganglion; 0.29152 0.25312 0.305084559 72.22811984 84.99268 1.96434 CASP7 0.000373926384361289 0.954747132481425 0.0448789411342139 caspase 7 FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly- 217' bond. Overexpression promotes programmed cell death.; . TISSUE SPECIFICITY: Highly expressed in lung, skeletal muscle, liver, kidney, spleen and heart, and moderately in testis. No expression in the brain.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;adrenal cortex;pharynx;blood;breast;pancreas;lung;adrenal gland;mesenchyma;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.41337 0.40317 0.619191319 83.36282142 1516.60298 7.23945 CASP8 0.00484502421758434 0.989046750691143 0.00610822509127217 caspase 8 FUNCTION: Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death- inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex. {ECO:0000269|PubMed:23516580, ECO:0000269|PubMed:9006941}.; DISEASE: Caspase-8 deficiency (CASP8D) [MIM:607271]: Disorder resembling autoimmune lymphoproliferative syndrome (ALPS). It is characterized by lymphadenopathy, splenomegaly, and defective CD95-induced apoptosis of peripheral blood lymphocytes (PBLs). It leads to defects in activation of T-lymphocytes, B-lymphocytes, and natural killer cells leading to immunodeficiency characterized by recurrent sinopulmonary and herpes simplex virus infections and poor responses to immunization. {ECO:0000269|PubMed:12353035}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1, isoform 5 and isoform 7 are expressed in a wide variety of tissues. Highest expression in peripheral blood leukocytes, spleen, thymus and liver. Barely detectable in brain, testis and skeletal muscle.; unclassifiable (Anatomical System);lymph node;heart;ovary;colon;skeletal muscle;skin;bone marrow;uterus;pancreas;lung;nasopharynx;placenta;trabecular meshwork;bone;amnion;liver;testis;spleen;germinal center;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;white blood cells;ciliary ganglion;atrioventricular node;whole blood;skeletal muscle; 0.21787 0.67074 0.042348793 57.31304553 95.54434 2.11059 CASP8AP2 . . . caspase 8 associated protein 2 FUNCTION: Participates in TNF-alpha-induced blockade of glucocorticoid receptor (GR) transactivation at the nuclear receptor coactivator level, upstream and independently of NF- kappa-B. Suppresses both NCOA2- and NCOA3-induced enhancement of GR transactivation. Involved in TNF-alpha-induced activation of NF-kappa-B via a TRAF2-dependent pathway. Acts as a downstream mediator for CASP8-induced activation of NF-kappa-B. Required for the activation of CASP8 in FAS-mediated apoptosis. Required for histone gene transcription and progression through S phase. {ECO:0000269|PubMed:12477726, ECO:0000269|PubMed:15698540, ECO:0000269|PubMed:17003125, ECO:0000269|PubMed:17245429}.; . . lymphoreticular;colon;choroid;fovea centralis;skin;retina;uterus;optic nerve;frontal lobe;testis;germinal center;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;lung;trabecular meshwork;placenta;visual apparatus;macula lutea;liver;spleen;cervix;kidney;stomach; . 0.12076 0.15094 . . . . CASP9 0.00319395567190647 0.947362466602922 0.0494435777251712 caspase 9 FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf- 1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP- ribose) polymerase (PARP).; . TISSUE SPECIFICITY: Ubiquitous, with highest expression in the heart, moderate expression in liver, skeletal muscle, and pancreas. Low levels in all other tissues. Within the heart, specifically expressed in myocytes. {ECO:0000269|PubMed:16857965}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;pharynx;blood;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;aorta; dorsal root ganglion;thalamus;superior cervical ganglion;adrenal cortex;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18813 0.73428 0.821252311 88.01604152 1917.48114 8.05887 CASP10 8.53789597425533e-12 0.0385314704649409 0.961468529526521 caspase 10 FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Recruited to both Fas- and TNFR-1 receptors in a FADD dependent manner. May participate in the granzyme B apoptotic pathways. Cleaves and activates caspase- 3, -4, -6, -7, -8, and -9. Hydrolyzes the small- molecule substrates, Tyr-Val-Ala-Asp-|-AMC and Asp-Glu-Val-Asp-|-AMC. {ECO:0000269|PubMed:11717445}.; DISEASE: Autoimmune lymphoproliferative syndrome 2A (ALPS2A) [MIM:603909]: A disorder of apoptosis that manifests in early childhood and results in the accumulation of autoreactive lymphocytes. It is characterized by non-malignant lymphadenopathy with hepatosplenomegaly, and autoimmune hemolytic anemia, thrombocytopenia and neutropenia. {ECO:0000269|PubMed:10412980, ECO:0000269|PubMed:16446975}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Familial non-Hodgkin lymphoma (NHL) [MIM:605027]: Cancer that starts in cells of the lymph system, which is part of the body's immune system. NHLs can occur at any age and are often marked by enlarged lymph nodes, fever and weight loss. {ECO:0000269|PubMed:12010812}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease. {ECO:0000269|PubMed:11973654}. Note=The gene represented in this entry is involved in disease pathogenesis.; TISSUE SPECIFICITY: Detectable in most tissues. Lowest expression is seen in brain, kidney, prostate, testis and colon.; unclassifiable (Anatomical System);cartilage;heart;colon;blood;skin;skeletal muscle;bone marrow;uterus;whole body;lung;nasopharynx;placenta;liver;testis;spleen;germinal center;kidney;spinal ganglion;brain;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.11187 . -0.089927255 46.99221515 615.62717 5.01039 CASP12 0.0877124851163816 0.56166111919729 0.350626395686329 caspase 12 (gene/pseudogene) FUNCTION: Has no protease activity. May reduce cytokine release in response to bacterial lipopolysaccharide during infections. Reduces activation of NF-kappa-B in response to TNF. {ECO:0000269|PubMed:12054529, ECO:0000269|PubMed:15129283}.; . TISSUE SPECIFICITY: Detected in heart, kidney, liver, lung, pancreas, small intestine, spleen, stomach, thymus and testis. {ECO:0000269|PubMed:12054529}.; . . 0.05795 . . . 234.35021 3.30854 CASP14 0.00123388115759124 0.850009100321036 0.148757018521372 caspase 14 FUNCTION: Non-apoptotic caspase involved in epidermal differentiation. Is the predominant caspase in epidermal stratum corneum (PubMed:15556625). Seems to play a role in keratinocyte differentiation and is required for cornification. Regulates maturation of the epidermis by proteolytically processing filaggrin (By similarity). In vitro has a preference for the substate [WY]-X-X-D motif and is active on the synthetic caspase substrate WEHD-ACF (PubMed:16854378, PubMed:19960512). Involved in processing of prosaposin in the epidermis (By similarity). May be involved in retinal pigment epithelium cell barrier function (PubMed:25121097). Involved in DNA degradation in differentiated keratinocytes probably by cleaving DFFA/ICAD leading to liberation of DFFB/CAD (PubMed:24743736). {ECO:0000250|UniProtKB:O89094, ECO:0000269|PubMed:15301553, ECO:0000269|PubMed:15556625, ECO:0000269|PubMed:16854378, ECO:0000269|PubMed:19960512, ECO:0000269|PubMed:22825846, ECO:0000269|PubMed:24743736, ECO:0000305|PubMed:25121097}.; . TISSUE SPECIFICITY: Expressed in keratinocytes of adult skin suprabasal layers (from spinous layers to the stratum granulosum and stratum corneum) (at protein level). Expressed in keratinocytes of hair shaft and sebaceous glands (at protein level). In psoriatic skin only expressed at very low levels (PubMed:11175259). The p17/10 mature form is expressed in epidermis stratum corneum, the p20/p8 intermediate form in epidermis upper granular cells of the stratum granulosum (PubMed:22825846). {ECO:0000269|PubMed:11175259, ECO:0000269|PubMed:15556625, ECO:0000269|PubMed:22825846}.; uterus;thyroid;bladder; . 0.34859 0.09799 -0.201976964 38.98325077 48.10319 1.35078 CASP16P . . . caspase 16, pseudogene . . . . . . . . . . . CASQ1 1.03907088565768e-09 0.165929134481788 0.834070864479141 calsequestrin 1 FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR1; this plays an important role in triggering muscle contraction. {ECO:0000269|PubMed:22337878, ECO:0000303|PubMed:22337878}.; DISEASE: Myopathy, vacuolar, with CASQ1 aggregates (VMCQA) [MIM:616231]: An autosomal dominant mild muscle disorder characterized by adult onset of muscle cramping and weakness as well as increased levels of serum creatine kinase. The disorder is not progressive, and some patients may be asymptomatic. {ECO:0000269|PubMed:25116801}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.49777 0.20075 0.597144447 82.7435716 382.53766 4.12343 CASQ2 1.06548301273598e-06 0.554092469882277 0.44590646463471 calsequestrin 2 FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats. {ECO:0000269|PubMed:16908766, ECO:0000269|PubMed:17881003, ECO:0000269|PubMed:18399795, ECO:0000269|PubMed:21416293}.; DISEASE: Ventricular tachycardia, catecholaminergic polymorphic, 2 (CPVT2) [MIM:611938]: An arrhythmogenic disorder characterized by stress-induced, bidirectional ventricular tachycardia that may degenerate into cardiac arrest and cause sudden death. Patients present with recurrent syncope, seizures, or sudden death after physical activity or emotional stress. {ECO:0000269|PubMed:11704930, ECO:0000269|PubMed:16908766, ECO:0000269|PubMed:18399795}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);myocardium;heart;ovary;colon;parathyroid;skeletal muscle;prostate;whole body;lung;trabecular meshwork;placenta;visual apparatus;liver;testis;stomach; thalamus;superior cervical ganglion;heart;tongue;skeletal muscle; 0.12110 0.15260 -0.157884861 42.05590941 588.11833 4.91846 CASR 0.366508674072432 0.633470866368765 2.04595588031623e-05 calcium sensing receptor FUNCTION: Senses changes in the extracellular concentration of calcium ions. The activity of this receptor is mediated by a G- protein that activates a phosphatidylinositol-calcium second messenger system.; DISEASE: Hypocalciuric hypercalcemia, familial 1 (HHC1) [MIM:145980]: A form of hypocalciuric hypercalcemia, a disorder of mineral homeostasis that is transmitted as an autosomal dominant trait with a high degree of penetrance. It is characterized biochemically by lifelong elevation of serum calcium concentrations and is associated with inappropriately low urinary calcium excretion and a normal or mildly elevated circulating parathyroid hormone level. Hypermagnesemia is typically present. Affected individuals are usually asymptomatic and the disorder is considered benign. However, chondrocalcinosis and pancreatitis occur in some adults. {ECO:0000269|PubMed:11762699, ECO:0000269|PubMed:15572418, ECO:0000269|PubMed:15579740, ECO:0000269|PubMed:15879434, ECO:0000269|PubMed:16598859, ECO:0000269|PubMed:17473068, ECO:0000269|PubMed:17698911, ECO:0000269|PubMed:21643651, ECO:0000269|PubMed:7673400, ECO:0000269|PubMed:7726161, ECO:0000269|PubMed:7916660, ECO:0000269|PubMed:9298824}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hyperparathyroidism, neonatal severe (NSHPT) [MIM:239200]: A disorder characterized by severe hypercalcemia, bone demineralization, and failure to thrive usually manifesting in the first 6 months of life. If untreated, NSHPT can be a devastating neurodevelopmental disorder, which in some cases is lethal without parathyroidectomy. {ECO:0000269|PubMed:8675635, ECO:0000269|PubMed:9253359}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hypocalcemia, autosomal dominant 1 (HYPOC1) [MIM:601198]: A disorder of mineral homeostasis characterized by blood calcium levels below normal, and low or normal serum parathyroid hormone concentrations. Disease manifestations include mild or asymptomatic hypocalcemia, paresthesias, carpopedal spasm, seizures, hypercalciuria with nephrocalcinosis or kidney stones, and ectopic and basal ganglia calcifications. Few patients manifest hypocalcemia and features of Bartter syndrome, including hypomagnesemia, hypokalemia, metabolic alkalosis, hyperreninemia, and hyperaldosteronemia. {ECO:0000269|PubMed:10487661, ECO:0000269|PubMed:12050233, ECO:0000269|PubMed:12107202, ECO:0000269|PubMed:12241879, ECO:0000269|PubMed:12574188, ECO:0000269|PubMed:12915654, ECO:0000269|PubMed:15551332, ECO:0000269|PubMed:16608894, ECO:0000269|PubMed:7874174, ECO:0000269|PubMed:8733126, ECO:0000269|PubMed:8813042, ECO:0000269|PubMed:9253358, ECO:0000269|PubMed:9661634, ECO:0000269|PubMed:9920108}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epilepsy, idiopathic generalized 8 (EIG8) [MIM:612899]: A disorder characterized by recurring generalized seizures in the absence of detectable brain lesions and/or metabolic abnormalities. Seizure types are variable, but include myoclonic seizures, absence seizures, febrile seizures, complex partial seizures, and generalized tonic-clonic seizures. {ECO:0000269|PubMed:18756473}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=Homozygous defects in CASR can be a cause of primary hyperparathyroidism in adulthood. Patients suffer from osteoporosis and renal calculi, have marked hypercalcemia and increased serum PTH concentrations.; TISSUE SPECIFICITY: Expressed in the temporal lobe, frontal lobe, parietal lobe, hippocampus, and cerebellum. Also found in kidney, lung, liver, heart, skeletal muscle, placenta. {ECO:0000269|PubMed:18756473}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;placenta;parathyroid;kidney; superior cervical ganglion;testis - seminiferous tubule;temporal lobe;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.26152 0.66150 -0.108334733 45.57088936 2617.72548 9.58482 CASS4 0.296175209094422 0.702950464411796 0.000874326493782645 Cas scaffolding protein family member 4 FUNCTION: Docking protein that plays a role in tyrosine kinase- based signaling related to cell adhesion and cell spreading. Regulates PTK2/FAK1 activity, focal adhesion integrity, and cell spreading. {ECO:0000269|PubMed:18256281}.; . TISSUE SPECIFICITY: Expressed abundantly in lung and spleen. Also highly expressed in ovarian and leukemia cell lines. {ECO:0000269|PubMed:18256281}.; unclassifiable (Anatomical System);lung;spleen;brain;stomach; superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;pons;cingulate cortex;skeletal muscle; 0.12766 0.08393 -0.10469683 45.64755839 558.21824 4.79883 CAST 1.55575755785131e-06 0.998177797334112 0.00182064690833045 calpastatin FUNCTION: Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue.; DISEASE: Peeling skin with leukonychia, acral punctate keratoses, cheilitis, and knuckle pads (PLACK) [MIM:616295]: An autosomal recessive disease characterized by generalized, continuous shedding of the outer layers of the epidermis, leukonychia, acral punctate keratosis, cheilitis, knuckle pads with multiple hyperkeratotic micropapules involving the interphalangeal joints, and palmoplantar keratoderma. {ECO:0000269|PubMed:25683118}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;cornea;nasopharynx;placenta;amnion;head and neck;kidney;aorta;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;medulla oblongata;testis - seminiferous tubule;tongue;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.28032 0.33847 0.714657953 85.81623024 804.17478 5.58770 CASZ1 0.999938476327784 6.15236717305971e-05 4.85798796094016e-13 castor zinc finger 1 FUNCTION: Transcription factor involved in vascular assembly and morphogenesis through direct transcriptional regulation of EGFL7. {ECO:0000269|PubMed:23639441}.; . TISSUE SPECIFICITY: Expressed in heart, lung, skeletal muscle, pancreas, testis, small intestine, and stomach, but it is not detectable in the adult brain. {ECO:0000269|PubMed:16631614}.; unclassifiable (Anatomical System);medulla oblongata;ovary;cartilage;colon;fovea centralis;choroid;lens;retina;uterus;breast;pancreas;prostate;optic nerve;macula lutea;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.71675 0.27528 -2.416721768 1.055673508 1083.53567 6.31123 CAT 1.47983086096776e-06 0.843369117527108 0.156629402642031 catalase FUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells. {ECO:0000269|PubMed:7882369}.; DISEASE: Acatalasemia (ACATLAS) [MIM:614097]: A metabolic disorder characterized by a total or near total loss of catalase activity in red cells. It is often associated with ulcerating oral lesions. {ECO:0000269|PubMed:2308162}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;trabecular meshwork;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;pancreas;lung;pia mater;mesenchyma;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta; fetal liver;adipose tissue;liver;white blood cells;kidney;bone marrow; 0.49631 0.94977 -0.310388054 32.14791224 76.9554 1.84114 CATIP . . . ciliogenesis associated TTC17 interacting protein FUNCTION: Plays a role in primary ciliogenesis by modulating actin polymerization. {ECO:0000269|PubMed:24475127}.; . TISSUE SPECIFICITY: Strongly expressed in round and elongating spermatids, weakly in pachytene spermatocytes. Expressed in Leydig cells (at protein level). Expressed in testis, placenta, prostate and lung, and moderately in ovary and brain. {ECO:0000269|PubMed:24475127}.; . . 0.18103 . -0.578583623 18.71903751 . . CATIP-AS1 . . . CATIP antisense RNA 1 . . . . . . . . . . . CATIP-AS2 . . . CATIP antisense RNA 2 . . . . . . . . . . . CATR1 . . . CATR tumorigenicity conversion 1 . . . . . . . . . . . CATSPER1 1.14276525299487e-08 0.536011661182662 0.463988327389685 cation channel sperm associated 1 FUNCTION: Voltage-gated calcium channel that plays a central role in calcium-dependent physiological responses essential for successful fertilization, such as sperm hyperactivation, acrosome reaction and chemotaxis towards the oocyte. Activated by extracellular progesterone and prostaglandins following the sequence: progesterone > PGF1-alpha = PGE1 > PGA1 > PGE2 >> PGD2. The primary effect of progesterone activation is to shift voltage dependence towards more physiological, negative membrane potentials; it is not mediated by metabotropic receptors and second messengers. Sperm capacitation enhances the effect of progesterone by providing additional negative shift. Also activated by the elevation of intracellular pH. {ECO:0000269|PubMed:21412338, ECO:0000269|PubMed:21412339}.; DISEASE: Spermatogenic failure 7 (SPGF7) [MIM:612997]: An infertility disorder characterized by non-motile sperm or sperm motility below the normal threshold, low sperm count, increased abnormally structured spermatozoa, and reduced semen volume. {ECO:0000269|PubMed:19344877}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:11595941, ECO:0000269|PubMed:16625279, ECO:0000269|PubMed:17347248}.; unclassifiable (Anatomical System);uterus;lung;heart;bone;testis;skin; superior cervical ganglion;ciliary ganglion; 0.02177 . -0.479490344 22.81788158 367.23704 4.05003 CATSPER2 3.0443890998245e-05 0.985259193373504 0.0147103627354982 cation channel sperm associated 2 FUNCTION: Voltage-gated calcium channel that plays a central role in calcium-dependent physiological responses essential for successful fertilization, such as sperm hyperactivation, acrosome reaction and chemotaxis towards the oocyte. Activated by extracellular progesterone and prostaglandins following the sequence: progesterone > PGF1-alpha = PGE1 > PGA1 > PGE2 >> PGD2. The primary effect of progesterone activation is to shift voltage dependence towards more physiological, negative membrane potentials; it is not mediated by metabotropic receptors and second messengers. Sperm capacitation enhances the effect of progesterone by providing additional negative shift. Also activated by the elevation of intracellular pH. {ECO:0000269|PubMed:21412338, ECO:0000269|PubMed:21412339}.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:11675491, ECO:0000269|PubMed:17347248}.; unclassifiable (Anatomical System);medulla oblongata;ovary;cartilage;blood;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;prostate;optic nerve;lung;endometrium;macula lutea;alveolus;testis;germinal center; superior cervical ganglion;testis - interstitial;ciliary ganglion;atrioventricular node; 0.03720 0.06508 0.911261639 89.50813871 1059.79018 6.24713 CATSPER2P1 . . . cation channel sperm associated 2 pseudogene 1 . . . . . . . . . . . CATSPER3 0.000487201544072685 0.876387272399766 0.123125526056161 cation channel sperm associated 3 FUNCTION: Voltage-gated calcium channel that plays a central role in calcium-dependent physiological responses essential for successful fertilization, such as sperm hyperactivation, acrosome reaction and chemotaxis towards the oocyte. Activated by extracellular progesterone and prostaglandins following the sequence: progesterone > PGF1-alpha = PGE1 > PGA1 > PGE2 >> PGD2. The primary effect of progesterone activation is to shift voltage dependence towards more physiological, negative membrane potentials; it is not mediated by metabotropic receptors and second messengers. Sperm capacitation enhances the effect of progesterone by providing additional negative shift. Also activated by the elevation of intracellular pH. {ECO:0000269|PubMed:21412338, ECO:0000269|PubMed:21412339}.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:12646162, ECO:0000269|PubMed:12932298, ECO:0000269|PubMed:17347248}.; unclassifiable (Anatomical System);uterus;lung;testis;colon;germinal center; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11031 0.08641 0.845119304 88.4170795 278.51799 3.57736 CATSPER4 3.16436332178783e-05 0.938823604461427 0.0611447519053555 cation channel sperm associated 4 FUNCTION: Voltage-gated calcium channel that plays a central role in calcium-dependent physiological responses essential for successful fertilization, such as sperm hyperactivation, acrosome reaction and chemotaxis towards the oocyte. Activated by extracellular progesterone and prostaglandins following the sequence: progesterone > PGF1-alpha = PGE1 > PGA1 > PGE2 >> PGD2. The primary effect of progesterone activation is to shift voltage dependence towards more physiological, negative membrane potentials; it is not mediated by metabotropic receptors and second messengers. Sperm capacitation enhances the effect of progesterone by providing additional negative shift. Also activated by the elevation of intracellular pH. {ECO:0000269|PubMed:21412338, ECO:0000269|PubMed:21412339}.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:12932298, ECO:0000269|PubMed:17347248}.; testis; . 0.07448 0.08341 0.402364592 76.45081387 2303.92204 8.88547 CATSPERB 4.2621545768236e-13 0.910415575274234 0.0895844247253398 cation channel sperm associated auxiliary subunit beta FUNCTION: Probably involved in sperm cell hyperactivation via its association with CATSPER1. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization (By similarity). {ECO:0000250}.; . . uterus;ovary;heart;islets of Langerhans;placenta;liver;testis;skin; testis - interstitial;superior cervical ganglion; 0.04869 0.05922 -0.793601146 12.57372022 761.54173 5.47110 CATSPERD 1.06714268717347e-08 0.981490443038352 0.018509546290221 cation channel sperm associated auxiliary subunit delta FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for CATSPER1 stability before intraflagellar transport and/or incorporation of the CatSper complex channel into the flagellar membrane (By similarity). {ECO:0000250}.; . . . . 0.06965 . 1.897880003 97.34607219 2039.12612 8.32234 CATSPERG 1.31477258507678e-11 0.754237372776625 0.245762627210227 cation channel sperm associated auxiliary subunit gamma FUNCTION: Probably involved in sperm cell hyperactivation via its association with CATSPER1. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;thyroid;testis;brain; medulla oblongata;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.21807 . -0.657684922 16.09459778 542.61244 4.74222 CAV1 0.0187079719750825 0.730737612899321 0.250554415125596 caveolin 1 FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)- mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3- dependent manner. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway. {ECO:0000250, ECO:0000269|PubMed:11751885, ECO:0000269|PubMed:17287217}.; DISEASE: Congenital generalized lipodystrophy 3 (CGL3) [MIM:612526]: An autosomal recessive disorder characterized by a near complete absence of adipose tissue, extreme insulin resistance, hypertriglyceridemia, hepatic steatosis and early onset of diabetes. {ECO:0000269|PubMed:18211975}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pulmonary hypertension, primary, 3 (PPH3) [MIM:615343]: A rare disorder characterized by plexiform lesions of proliferating endothelial cells in pulmonary arterioles. The lesions lead to elevated pulmonary arterial pression, right ventricular failure, and death. The disease can occur from infancy throughout life and it has a mean age at onset of 36 years. Penetrance is reduced. Although familial pulmonary hypertension is rare, cases secondary to known etiologies are more common and include those associated with the appetite-suppressant drugs. {ECO:0000269|PubMed:22474227}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Partial lipodystrophy, congenital cataracts, and neurodegeneration syndrome (LCCNS) [MIM:606721]: A form of familial partial lipodystrophy associated with congenital cataracts and neurodegeneration leading to cerebellar and spinal cord dysfunction. {ECO:0000269|PubMed:18237401}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in muscle and lung, less so in liver, brain and kidney.; ovary;sympathetic chain;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;atrium;whole body;frontal lobe;cerebral cortex;larynx;gum;bone;thyroid;pituitary gland;testis;dura mater;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;pancreas;pia mater;lung;mesenchyma;trabecular meshwork;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;adipose tissue;smooth muscle;olfactory bulb;heart;atrioventricular node;uterus;lung;placenta;thyroid;appendix;testis;ciliary ganglion;fetal lung;trigeminal ganglion; 0.48727 0.86293 -0.317668748 31.45789101 11.5877 0.41881 CAV2 0.00411638498497318 0.654754529386809 0.341129085628218 caveolin 2 FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity). {ECO:0000250, ECO:0000269|PubMed:15504032, ECO:0000269|PubMed:18081315}.; . TISSUE SPECIFICITY: Expressed in endothelial cells, smooth muscle cells, skeletal myoblasts and fibroblasts. {ECO:0000269|PubMed:9361015}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;cerebral cortex;larynx;bone;thyroid;testis;amniotic fluid;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;olfactory bulb;adipose tissue;lung;thyroid;fetal lung;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12871 0.29252 0.014844891 54.94810097 1195.08779 6.55941 CAV3 0.339836385676367 0.601017924272671 0.0591456900509625 caveolin 3 FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. May also regulate voltage-gated potassium channels. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress.; DISEASE: Limb-girdle muscular dystrophy 1C (LGMD1C) [MIM:607801]: A degenerative myopathy characterized by calf hypertrophy and mild to moderate proximal muscle weakness. Inheritance can be autosomal dominant or recessive. {ECO:0000269|PubMed:11001938, ECO:0000269|PubMed:11532985, ECO:0000269|PubMed:12557291, ECO:0000269|PubMed:12939441, ECO:0000269|PubMed:15564037, ECO:0000269|PubMed:15580566, ECO:0000269|PubMed:9537420}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: HyperCKmia (HYPCK) [MIM:123320]: Characterized by persistent elevated levels of serum creatine kinase without muscle weakness. {ECO:0000269|PubMed:10746614, ECO:0000269|PubMed:12082049, ECO:0000269|PubMed:14663034, ECO:0000269|PubMed:15099591, ECO:0000269|PubMed:15580566}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Rippling muscle disease (RMD) [MIM:606072]: Rare disorder characterized by mechanically triggered contractions of skeletal muscle. In RMD, mechanical stimulation leads to electrically silent muscle contractions that spread to neighboring fibers that cause visible ripples to move over the muscle. {ECO:0000269|PubMed:11431690, ECO:0000269|PubMed:11756609, ECO:0000269|PubMed:12557291, ECO:0000269|PubMed:12666119, ECO:0000269|PubMed:15668980, ECO:0000269|PubMed:16458928}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, familial hypertrophic (CMH) [MIM:192600]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:14672715}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Long QT syndrome 9 (LQT9) [MIM:611818]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. {ECO:0000269|PubMed:17060380, ECO:0000269|PubMed:17275750}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Sudden infant death syndrome (SIDS) [MIM:272120]: SIDS is the sudden death of an infant younger than 1 year that remains unexplained after a thorough case investigation, including performance of a complete autopsy, examination of the death scene, and review of clinical history. Pathophysiologic mechanisms for SIDS may include respiratory dysfunction, cardiac dysrhythmias, cardiorespiratory instability, and inborn errors of metabolism, but definitive pathogenic mechanisms precipitating an infant sudden death remain elusive. {ECO:0000269|PubMed:17275750}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Myopathy, distal, Tateyama type (MPDT) [MIM:614321]: A disorder characterized by progressive muscular atrophy and muscle weakness beginning in the hands, the legs, or the feet. Muscle atrophy may be restricted to the small muscles of the hands and feet. {ECO:0000269|PubMed:11805270, ECO:0000269|PubMed:15580566}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly in muscle. {ECO:0000269|PubMed:9545514}.; uterus;prostate;lung;whole body;heart;placenta;testis;skin;skeletal muscle; superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.38282 0.55696 0.439181676 77.69521113 353.1686 3.98007 CBARP . . . CACN beta subunit associated regulatory protein . . . . . 0.11111 0.20828 0.688969636 85.20877565 . . CBFA2T2 0.999355101452129 0.000644894914821568 3.63304911668757e-09 core-binding factor, runt domain, alpha subunit 2; translocated to, 2 FUNCTION: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes (PubMed:12559562, PubMed:15203199). Can repress the expression of MMP7 in a ZBTB33-dependent manner (PubMed:23251453). May function as a complex with the chimeric protein RUNX1/AML1-CBFA2T1/MTG8 which is produced in acute myeloid leukemia with the chromosomal translocation t(8;21). May thus be involved in the repression of AML1-dependent transcription and the induction of G-CSF/CSF3-dependent cell growth. May be a tumor suppressor gene candidate involved in myeloid tumors with the deletion of the 20q11 region. {ECO:0000269|PubMed:23251453, ECO:0000303|PubMed:12559562, ECO:0000303|PubMed:15203199}.; . TISSUE SPECIFICITY: Ubiquitously expressed in fetal and adult tissues. Highly expressed in adult brain, heart, lung, kidney, lymph node, appendix, thymus, testis, uterus, small intestine, prostate and thymus. {ECO:0000269|PubMed:10675041, ECO:0000269|PubMed:9447981, ECO:0000269|PubMed:9787195, ECO:0000269|PubMed:9790752}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;subthalamic nucleus;occipital lobe;prefrontal cortex;skeletal muscle;parietal lobe;cerebellum; 0.37829 0.27695 -0.356299879 29.31115829 63.05038 1.62441 CBFA2T3 0.454440081718265 0.545305189895428 0.000254728386307447 core-binding factor, runt domain, alpha subunit 2; translocated to, 3 FUNCTION: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes (PubMed:12559562, PubMed:15203199). Can repress the expression of MMP7 in a ZBTB33-dependent manner (PubMed:23251453). Reduces the protein levels and stability of the transcriptinal regulator HIF1A; interacts with EGLN1 and promotes the HIF1A prolyl hydroxylation-dependent ubiquitination and proteasomal degradation pathway (PubMed:25974097). Contributes to inhibition of glycolysis and stimulation of mitochondrial respiration by down-regulating the expression of glycolytic genes including PFKFB3, PFKFB4, PDK1, PFKP, LDHA and HK1 which are direct targets of HIF1A (PubMed:23840896, PubMed:25974097). Regulates the proliferation and the differentiation of erythroid progenitors by repressing the expression of TAL1 target genes (By similarity). Plays a role in granulocyte differentiation (PubMed:15231665). {ECO:0000250|UniProtKB:O54972, ECO:0000269|PubMed:12183414, ECO:0000269|PubMed:15231665, ECO:0000269|PubMed:16966434, ECO:0000269|PubMed:23251453, ECO:0000269|PubMed:23840896, ECO:0000269|PubMed:25974097, ECO:0000303|PubMed:12559562, ECO:0000303|PubMed:15203199}.; DISEASE: Note=A chromosomal aberration involving CBFA2T3 is found in therapy-related myeloid malignancies. Translocation t(16;21)(q24;q22) that forms a RUNX1-CBFA2T3 fusion protein. {ECO:0000269|PubMed:10995019, ECO:0000269|PubMed:11224496, ECO:0000269|PubMed:9596646}.; TISSUE SPECIFICITY: Widely expressed with higher expression in heart, pancreas, skeletal muscle, spleen, thymus and peripheral blood leukocytes. Expressed in hematopoietic cells (at protein level). {ECO:0000269|PubMed:15231665, ECO:0000269|PubMed:9596646, ECO:0000269|PubMed:9790752}.; lymphoreticular;ovary;colon;fovea centralis;choroid;bone marrow;retina;optic nerve;testis;germinal center;brain;ciliary body;unclassifiable (Anatomical System);lymph node;blood;lens;bile duct;pancreas;lung;placenta;visual apparatus;macula lutea;liver;spleen;cervix;stomach;cerebellum; . 0.50170 0.18130 -1.015898037 8.144609578 345.59186 3.94358 CBFB 0.905733874306119 0.0941079396240771 0.000158186069804442 core-binding factor, beta subunit FUNCTION: CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM- CSF promoters. CBFB enhances DNA binding by RUNX1.; DISEASE: Note=A chromosomal aberration involving CBFB is associated with acute myeloid leukemia of M4EO subtype. Pericentric inversion inv(16)(p13;q22). The inversion produces a fusion protein that consists of the 165 N-terminal residues of CBF-beta (PEPB2) with the tail region of MYH11. {ECO:0000269|PubMed:8351518}.; . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;lens;bile duct;breast;pancreas;pia mater;lung;placenta;macula lutea;visual apparatus;liver;alveolus;head and neck;cervix;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;white blood cells;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.85519 0.21981 -0.009020804 52.8544468 11.84242 0.42885 CBL 0.00678735718516732 0.99320626741059 6.375404242897e-06 Cbl proto-oncogene, E3 ubiquitin protein ligase FUNCTION: Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation. Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis. Essential for osteoclastic bone resorption. The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. {ECO:0000269|PubMed:10514377, ECO:0000269|PubMed:11896602, ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:14739300, ECO:0000269|PubMed:15190072, ECO:0000269|PubMed:17509076, ECO:0000269|PubMed:18374639, ECO:0000269|PubMed:19689429, ECO:0000269|PubMed:21596750}.; DISEASE: Noonan syndrome-like disorder with or without juvenile myelomonocytic leukemia (NSLL) [MIM:613563]: A syndrome characterized by a phenotype reminiscent of Noonan syndrome. Clinical features are highly variable, including facial dysmorphism, short neck, developmental delay, hyperextensible joints and thorax abnormalities with widely spaced nipples. The facial features consist of triangular face with hypertelorism, large low-set ears, ptosis, and flat nasal bridge. Some patients manifest cardiac defects. Some have an increased risk for certain malignancies, particularly juvenile myelomonocytic leukemia. {ECO:0000269|PubMed:20619386}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);breast;lung;testis;colon;blood;skeletal muscle;bone marrow; testis - interstitial;superior cervical ganglion;testis;skeletal muscle; 0.99670 0.47784 -1.041578376 7.773059684 223.45333 3.23169 CBLB 0.913125166981959 0.0868748241863056 8.83173556005148e-09 Cbl proto-oncogene B, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B- cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T- cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. Slightly promotes SRC ubiquitination. May be involved in EGFR ubiquitination and internalization. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. {ECO:0000269|PubMed:10022120, ECO:0000269|PubMed:10086340, ECO:0000269|PubMed:11087752, ECO:0000269|PubMed:11526404, ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:20525694}.; . TISSUE SPECIFICITY: Expressed in placenta, heart, lung, kidney, spleen, ovary and testis, as well as fetal brain and liver and hematopoietic cell lines, but not in adult brain, liver, pancreas, salivary gland, or skeletal muscle. Present in lymphocytes (at protein level). {ECO:0000269|PubMed:10022120, ECO:0000269|PubMed:9399639}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;pia mater;lung;placenta;macula lutea;visual apparatus;duodenum;hypopharynx;liver;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;appendix;atrioventricular node;trigeminal ganglion; 0.48496 0.38173 -0.839512508 11.40009436 332.72726 3.87692 CBLC 0.000182989540193376 0.973266053407877 0.0265509570519297 Cbl proto-oncogene C, E3 ubiquitin protein ligase FUNCTION: Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Functionally coupled with the E2 ubiquitin-protein ligases UB2D1, UB2D2 and UB2D3. Regulator of EGFR mediated signal transduction; upon EGF activation, ubiquitinates EGFR. Isoform 1, but not isoform 2, inhibits EGF stimulated MAPK1 activation. Promotes ubiquitination of SRC phosphorylated at 'Tyr-419'. In collaboration with CD2AP may act as regulatory checkpoint for Ret signaling by modulating the rate of RET degradation after ligand activation; CD2AP converts it from an inhibitor to a promoter of RET degradation; the function limits the potency of GDNF on neuronal survival. {ECO:0000269|PubMed:10362357, ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:18753381, ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:23145173}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10362357}.; unclassifiable (Anatomical System);uterus;lung;epidermis;endometrium;larynx;placenta;head and neck;mammary gland;skin;stomach; trigeminal ganglion; 0.07843 0.37224 0.997633954 90.65227648 1926.68142 8.07880 CBLL1 0.997784847703943 0.00221507874091106 7.35551459626854e-08 Cbl proto-oncogene like 1, E3 ubiquitin protein ligase FUNCTION: Promotes ubiquitination of several tyrosine- phosphorylated Src substrates, including CDH1, CTTN and DOK1. Targets CDH1 for endocytosis and degradation (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);breast;lymph node;lung;larynx;thyroid;colon;head and neck;germinal center;brain;skin;skeletal muscle; trigeminal ganglion; 0.29297 0.11049 -0.516085732 21.20193442 14.90934 0.53680 CBLN1 0.814123266644296 0.181372230092915 0.00450450326278948 cerebellin 1 precursor FUNCTION: Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the formation and maintenance of parallel fiber and Purkinje cell synapses. When parallel fibers make contact with Purkinje spines, CBLN1 interaction with GRID2 triggers the recruitment of NRXN1 and secretory vesicles to the sites of contact. NRXN1-CBLN1-GRID2 signaling induces presynaptic morphological changes, which may further accumulate pre- and postsynaptic components to promote bidirectional maturation of parallel fiber - Purkinje cell functionnally active synapses by a positive feedback mechanism. Required for CBLN3 export from the endoplasmic reticulum and secretion (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: In the Purkinje cells postsynaptic structures. In the cerebellum, cerebellin is much less abundant than [des- Ser1]-cerebellin.; unclassifiable (Anatomical System);uterus;medulla oblongata;lung;ovary;heart;testis;brain;skin;cerebellum; superior cervical ganglion;cerebellum peduncles;testis;pons;trigeminal ganglion;cerebellum; 0.84701 0.14663 0.013025609 54.62962963 18.56197 0.64312 CBLN2 0.318302604444597 0.613410926770971 0.0682864687844318 cerebellin 2 precursor FUNCTION: May play role in synaptogenesis induction. {ECO:0000250}.; . . unclassifiable (Anatomical System);whole body;frontal lobe;ovary;placenta;parathyroid;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.50237 0.11451 -0.09720619 46.20193442 56.81201 1.51729 CBLN3 0.000188310725826416 0.472033525550468 0.527778163723706 cerebellin 3 precursor FUNCTION: May be involved in synaptic functions in the CNS. {ECO:0000250}.; . . breast;uterus;lung;cartilage;bone;liver;spleen;blood;kidney;brain;aorta;cerebellum; . 0.11514 0.12150 -0.229483771 36.86010852 8.6503 0.31802 CBLN4 0.348291542584304 0.595810832297401 0.0558976251182954 cerebellin 4 precursor FUNCTION: May be involved in synaptic functions in the CNS. May play a role in CBLN3 export from the endoplasmic reticulum and secretion (By similarity). {ECO:0000250}.; . . lung;islets of Langerhans;hypothalamus;hippocampus;liver;testis;brain;retina; dorsal root ganglion;amygdala;whole brain;medulla oblongata;occipital lobe;ciliary ganglion;pons;trigeminal ganglion;parietal lobe; 0.33923 0.12032 -0.009020804 52.8544468 3.25418 0.11749 CBR1 0.00646220210275156 0.747239370165406 0.246298427731843 carbonyl reductase 1 FUNCTION: NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione. {ECO:0000269|PubMed:15799708, ECO:0000269|PubMed:17912391, ECO:0000269|PubMed:18449627, ECO:0000269|PubMed:18826943}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;hypothalamus;spinal cord;urinary;adrenal cortex;pharynx;blood;lens;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; amygdala;whole brain;occipital lobe;thalamus;hypothalamus;liver;globus pallidus;parietal lobe; 0.04387 0.26657 -0.0274281 51.65723048 55.40426 1.49405 CBR3 8.02768561586313e-06 0.170502480256301 0.829489492058083 carbonyl reductase 3 FUNCTION: Has low NADPH-dependent oxidoreductase activity towards 4-benzoylpyridine and menadione (in vitro). {ECO:0000269|PubMed:18493841}.; . TISSUE SPECIFICITY: Detected in ovary, pancreas, intestine, colon, kidney, brain, thymus, lung, heart, liver, spleen, leukocyte, prostate and testis. {ECO:0000269|PubMed:18493841}.; unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;hypothalamus;salivary gland;colon;skin;bile duct;uterus;prostate;whole body;larynx;bone;placenta;head and neck;stomach; subthalamic nucleus;trachea;tongue; 0.16819 0.13986 0.461228372 78.46190139 7916.09802 19.22109 CBR3-AS1 . . . CBR3 antisense RNA 1 . . . . . . . . . . . CBR4 8.22221600155339e-06 0.309124031912312 0.690867745871687 carbonyl reductase 4 FUNCTION: The heteroteramer with HSD17B8 has NADH-dependent 3- ketoacyl-acyl carrier protein reductase activity. May play a role in biosynthesis of fatty acids in mitochondria. The homotetramer may act as NADPH-dependent quinone reductase. Has broad substrate specificity and reduces 9,10-phenanthrenequinone, 1,4-benzoquinone and various other o-quinones and p-quinones (in vitro). {ECO:0000269|PubMed:19000905, ECO:0000269|PubMed:19571038}.; . TISSUE SPECIFICITY: Detected in liver and kidney (at protein level). {ECO:0000269|PubMed:19000905}.; unclassifiable (Anatomical System);lymph node;ovary;heart;islets of Langerhans;developmental;colon;parathyroid;blood;skeletal muscle;bone marrow;uterus;whole body;lung;endometrium;adrenal gland;larynx;bone;placenta;visual apparatus;liver;testis;cervix;head and neck;kidney;germinal center;brain;stomach; amygdala;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.21573 . 0.305084559 72.22811984 65.06366 1.65973 CBS 0.00677205373062702 0.989447535398095 0.00378041087127811 cystathionine-beta-synthase FUNCTION: Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L- homocysteine (PubMed:23981774, PubMed:20506325, PubMed:23974653). Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons (By similarity). {ECO:0000250|UniProtKB:P32232, ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:23974653, ECO:0000269|PubMed:23981774}.; . TISSUE SPECIFICITY: In the adult strongly expressed in liver and pancreas, some expression in heart and brain, weak expression in lung and kidney. In the fetus, expressed in brain, liver and kidney.; lymphoreticular;ovary;colon;skin;bone marrow;uterus;prostate;frontal lobe;cerebral cortex;bone;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;skeletal muscle;breast;pancreas;lung;cornea;epididymis;placenta;visual apparatus;liver;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;liver; 0.53216 0.84775 -0.795417163 12.5324369 182.79557 2.93632 CBSL . . . cystathionine-beta-synthase like FUNCTION: Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L- homocysteine. Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons. {ECO:0000250|UniProtKB:P32232, ECO:0000250|UniProtKB:P35520}.; . . . . . . . . . . CBWD1 0.642141452095713 0.35651351246747 0.00134503543681637 COBW domain containing 1 . . TISSUE SPECIFICITY: Ubiquitously expressed. Up-regulated in cultured astrocytes treated with dopamine. {ECO:0000269|PubMed:15233989}.; lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; . 0.14650 0.09079 . . 228.50043 3.26546 CBWD2 0.967070795623724 0.0328743004174018 5.49039588742764e-05 COBW domain containing 2 . . . lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; . 0.14970 0.09412 . . 356.95895 4.00233 CBWD3 0.358916974871045 0.589020154118356 0.0520628710105994 COBW domain containing 3 . . . lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach;thymus; . . 0.09807 . . 7163.3464 18.21502 CBWD4P . . . COBW domain containing 4 pseudogene . . . . . . . . . . . CBWD5 0.534115235923079 0.406848139151238 0.0590366249256828 COBW domain containing 5 . . . . . 0.14650 0.09515 . . 8.51795 0.31253 CBWD6 0.26744134859198 0.707447151277403 0.0251115001306163 COBW domain containing 6 . . . . . . . . . 1085.1749 6.31218 CBWD7 . . . COBW domain containing 7 . . . . . . . . . . . CBX1 0.949842677925257 0.0500008532129904 0.000156468861753051 chromobox 1 FUNCTION: Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane.; . TISSUE SPECIFICITY: Expressed in all adult and embryonic tissues.; myocardium;lymphoreticular;smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;head and neck;kidney;stomach;aorta;thymus; amygdala;testis - interstitial;superior cervical ganglion;occipital lobe;hypothalamus;pons;testis - seminiferous tubule;fetal brain;prefrontal cortex;globus pallidus;testis;parietal lobe;cingulate cortex; 0.18535 . 0.057118534 57.99716914 . . CBX1P1 . . . chromobox 1 pseudogene 1 . . . . . . . . . . . CBX1P2 . . . chromobox 1 pseudogene 2 . . . . . . . . . . . CBX1P3 . . . chromobox 1 pseudogene 3 . . . . . . . . . . . CBX1P4 . . . chromobox 1 pseudogene 4 . . . . . . . . . . . CBX1P5 . . . chromobox 1 pseudogene 5 . . . . . . . . . . . CBX2 0.954823918488159 0.0450555788718336 0.000120502640007476 chromobox 2 FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Involved in sexual development, acting as activator of NR5A1 expression. {ECO:0000269|PubMed:19361780, ECO:0000269|PubMed:21282530}.; DISEASE: 46,XY sex reversal 5 (SRXY5) [MIM:613080]: A disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females. {ECO:0000269|PubMed:19361780}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;pancreas;smooth muscle;endometrium;visual apparatus;colon;kidney; testis - interstitial;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.13339 0.12407 -0.659500046 16.07100731 390.83079 4.16263 CBX3 0.633200403003169 0.359860988164988 0.0069386088318435 chromobox 3 FUNCTION: Seems to be involved in transcriptional silencing in heterochromatin-like complexes. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. May contribute to the association of the heterochromatin with the inner nuclear membrane through its interaction with lamin B receptor (LBR). Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. Contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation, mediates the recruitment of the mehtyltransferases SUV39H1 and/or SUV39H2 by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1.; . . ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;duodenum;kidney;stomach;aorta;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;tumor; 0.65881 0.20660 0.057118534 57.99716914 6.1306 0.23144 CBX3P1 . . . chromobox 3 pseudogene 1 . . . . . . . . . . . CBX3P2 . . . chromobox 3 pseudogene 2 . . . . . . . . . . . CBX3P3 . . . chromobox 3 pseudogene 3 . . . . . . . . . . . CBX3P4 . . . chromobox 3 pseudogene 4 . . . . . . . . . . . CBX3P5 . . . chromobox 3 pseudogene 5 . . . . . . . . . . . CBX3P6 . . . chromobox 3 pseudogene 6 . . . . . . . . . . . CBX3P7 . . . chromobox 3 pseudogene 7 . . . . . . . . . . . CBX3P8 . . . chromobox 3 pseudogene 8 . . . . . . . . . . . CBX3P9 . . . chromobox 3 pseudogene 9 . . . . . . . . . . . CBX4 0.381198481678265 0.608349045334697 0.0104524729870372 chromobox 4 FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression. Monosumoylates ZNF131.; . TISSUE SPECIFICITY: Ubiquitous.; colon;skin;retina;pancreas;prostate;lung;placenta;visual apparatus;cervix;mammary gland;brain;stomach;thymus; ciliary ganglion; 0.87942 0.10350 0.106667882 61.73036093 1044.2776 6.20429 CBX5 0.835000939076987 0.161714337050619 0.00328472387239398 chromobox 5 FUNCTION: Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. {ECO:0000269|PubMed:19783980}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;bone;thyroid;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);heart;pharynx;blood;lens;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;cerebellum peduncles;prefrontal cortex;globus pallidus;testis;cingulate cortex;parietal lobe; 0.78596 0.41336 0.035072054 56.2514744 1.9007 0.05925 CBX5P1 . . . chromobox 5 pseudogene 1 . . . . . . . . . . . CBX6 0.610925095502502 0.380696783391478 0.0083781211060193 chromobox 6 FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. {ECO:0000269|PubMed:21282530}.; . . lymphoreticular;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;myometrium;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;peripheral nerve; amygdala;whole brain;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; . 0.09061 . . 40.22071 1.18226 CBX7 0.837455380362367 0.16188110535651 0.000663514281123205 chromobox 7 FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Promotes histone H3 trimethylation at 'Lys-9' (H3K9me3). Binds to trimethylated lysine residues in histones, and possibly also other proteins. Regulator of cellular lifespan by maintaining the repression of CDKN2A, but not by inducing telomerase activity. {ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:21047797, ECO:0000269|PubMed:21060834, ECO:0000269|PubMed:21282530}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;bone;iris;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;spinal cord;temporal lobe;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;head and neck;kidney;nose;stomach;cerebellum; . 0.68646 0.12378 -0.229483771 36.86010852 11.3463 0.40831 CBX8 0.994625905090376 0.00537345509472408 6.39814899551191e-07 chromobox 8 FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. {ECO:0000269|PubMed:21282530}.; . . unclassifiable (Anatomical System);lacrimal gland;muscle;colon;skin;skeletal muscle;bone marrow;uterus;lung;frontal lobe;endometrium;larynx;placenta;visual apparatus;testis;head and neck;cervix;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.92567 0.17506 -0.003562597 53.72729417 55.97296 1.50251 CBY1 0.0274301810457834 0.794983987270204 0.177585831684013 chibby homolog 1 (Drosophila) FUNCTION: Inhibits the Wnt/Wingless pathway by binding to CTNNB1/beta-catenin and inhibiting beta-catenin-mediated transcriptional activation through competition with TCF/LEF transcription factors. Has also been shown to play a role in regulating the intracellular trafficking of polycystin-2/PKD2 and possibly of other intracellular proteins. Promotes adipocyte and cardiomyocyte differentiation. {ECO:0000269|PubMed:12712206, ECO:0000269|PubMed:15194699}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher levels in heart, skeletal muscle, kidney and placenta. Also found in brain, lung, liver and testis. Significantly down-regulated in thyroid and metastatic uterine tumors. {ECO:0000269|PubMed:12712206}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;gum;bone;thyroid;iris;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach; . 0.09054 0.13156 -0.207437529 38.2814343 18.73118 0.64621 CBY3 . . . chibby homolog 3 (Drosophila) . . . . . 0.22458 . 0.746027844 86.40599198 313.91833 3.76611 CC2D1A 2.25920260836964e-05 0.999938176237096 3.92317368206409e-05 coiled-coil and C2 domain containing 1A FUNCTION: Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells. The combination of calcium and ATP specifically inactivates the binding with FRE. May play a role in the altered regulation of HTR1A associated with anxiety and major depression. Mediates HDAC-independent repression of HTR1A promoter in neuronal cell. Performs essential function in controlling functional maturation of synapses (By similarity). Plays distinct roles depending on its localization. When cytoplasmic, acts as a scaffold protein in the PI3K/PDK1/AKT pathway. Repressor of HTR1A when nuclear. In the centrosome, regulates spindle pole localization of the cohesin subunit SCC1/RAD21, thereby mediating centriole cohesion during mitosis. {ECO:0000250, ECO:0000269|PubMed:20171170}.; DISEASE: Mental retardation, autosomal recessive 3 (MRT3) [MIM:608443]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs. {ECO:0000269|PubMed:16033914}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;bile duct;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; amygdala;superior cervical ganglion;prefrontal cortex;ciliary ganglion;skeletal muscle;parietal lobe;cingulate cortex; 0.09564 0.10252 1.453198553 95.15805615 2170.49657 8.57875 CC2D1B 4.76314820582514e-10 0.98651316626162 0.0134868332620653 coiled-coil and C2 domain containing 1B FUNCTION: Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells. {ECO:0000269|PubMed:19423080}.; . TISSUE SPECIFICITY: Widely distributed in brain and peripheral tissues. {ECO:0000269|PubMed:19423080}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;tongue;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09590 . 0.187364432 66.28921916 1014.46059 6.13079 CC2D2A 5.49406447707416e-15 0.996044426113797 0.00395557388619735 coiled-coil and C2 domain containing 2A FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling (By similarity). {ECO:0000250, ECO:0000269|PubMed:18513680}.; DISEASE: Meckel syndrome 6 (MKS6) [MIM:612284]: A disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly. {ECO:0000269|PubMed:19466712}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Joubert syndrome 9 (JBTS9) [MIM:612285]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. {ECO:0000269|PubMed:18387594, ECO:0000269|PubMed:18950740, ECO:0000269|PubMed:19777577, ECO:0000269|PubMed:22425360, ECO:0000269|PubMed:23012439}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: COACH syndrome (COACHS) [MIM:216360]: A disorder characterized by mental retardation, ataxia due to cerebellar hypoplasia, and hepatic fibrosis. Patients present the molar tooth sign, a midbrain-hindbrain malformation pathognomonic for Joubert syndrome and related disorders. Other features, such as coloboma and renal cysts, may be variable. {ECO:0000269|PubMed:19574260}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Strongly expressed in prostate, pancreas, kidney, lung, liver, retina, kidney, fetal brain and fetal kidney. Lower expression in spleen, small intestine, colon, skeletal muscle, ovary, thymus and heart. {ECO:0000269|PubMed:18387594, ECO:0000269|PubMed:18950740}.; . . 0.09921 0.13205 -0.916836882 9.831328143 895.42999 5.83159 CC2D2B 2.5176722476543e-05 0.753995316361063 0.24597950691646 coiled-coil and C2 domain containing 2B . . . ovary;heart;alveolus;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.43967 . 0.350995466 74.37485256 938.4793 5.93834 CCA1 . . . cataract, congenital, cerulean type, 1 . . . . . . . . . . . CCAL1 . . . chondrocalcinosis 1 (calcium pyrophosphate-deposition disease, early onset osteoarthritis) . . . . . . . . . . . CCAR1 0.998746219854088 0.00125378014586032 5.16041482734757e-14 cell division cycle and apoptosis regulator 1 FUNCTION: Associates with components of the Mediator and p160 coactivator complexes that play a role as intermediaries transducing regulatory signals from upstream transcriptional activator proteins to basal transcription machinery at the core promoter. Recruited to endogenous nuclear receptor target genes in response to the appropriate hormone. Also functions as a p53 coactivator. May thus play an important role in transcriptional regulation (By similarity). May be involved in apoptosis signaling in the presence of the reinoid CD437. Apoptosis induction involves sequestration of 14-3-3 protein(s) and mediated altered expression of multiple cell cycle regulatory genes including MYC, CCNB1 and CDKN1A. Plays a role in cell cycle progression and/or cell proliferation (PubMed:12816952). In association with CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). Can act as a both a coactivator and corepressor of AR-mediated transcription. Contributes to chromatin looping and AR transcription complex assembly by stabilizing AR-GATA2 association on chromatin and facilitating MED1 and RNA polymerase II recruitment to AR-binding sites. May play an important role in the growth and tumorigenesis of prostate cancer cells (PubMed:23887938). {ECO:0000250|UniProtKB:Q8CH18, ECO:0000269|PubMed:12816952, ECO:0000269|PubMed:23887938, ECO:0000269|PubMed:24245781}.; . TISSUE SPECIFICITY: Expressed in various epithelial cancer cell lines, including breast, colon, prostate, pancreatic and leukemia. Expression is regulated by growth factors. {ECO:0000269|PubMed:12816952}.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;amygdala;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;duodenum;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;subthalamic nucleus;testis - interstitial;ciliary ganglion;atrioventricular node;pons; 0.68559 0.15921 -1.087493118 7.106628922 139.07966 2.57017 CCAR2 0.960454889427648 0.0395450810750771 2.94972751126885e-08 cell cycle and apoptosis regulator 2 FUNCTION: Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis. Inhibits SUV39H1 methyltransferase activity. As part of a histone H3- specific methyltransferase complex may mediate ligand-dependent transcriptional activation by nuclear hormone receptors. Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress. Regulates the circadian expression of the core clock components NR1D1 and ARNTL/BMAL1. Enhances the transcriptional repressor activity of NR1D1 through stabilization of NR1D1 protein levels by preventing its ubiquitination and subsequent degradation (PubMed:18235501, PubMed:18235502, PubMed:19131338, PubMed:19218236, PubMed:22446626, PubMed:23352644, PubMed:23398316). Represses the ligand-dependent transcriptional activation function of ESR2 (PubMed:20074560). Acts as a regulator of PCK1 expression and gluconeogenesis by a mechanism that involves, at least in part, both NR1D1 and SIRT1 (PubMed:24415752). Negatively regulates the deacetylase activity of HDAC3 and can alter its subcellular localization (PubMed:21030595). Positively regulates the beta- catenin pathway (canonical Wnt signaling pathway) and is required for MCC-mediated repression of the beta-catenin pathway (PubMed:24824780). Represses ligand-dependent transcriptional activation function of NR1H2 and NR1H3 and inhibits the interaction of SIRT1 with NR1H3 (PubMed:25661920). Plays an important role in tumor suppression through p53/TP53 regulation; stabilizes p53/TP53 by affecting its interaction with ubiquitin ligase MDM2 (PubMed:25732823). Represses the transcriptional activator activity of BRCA1 (PubMed:20160719). Inhibits SIRT1 in a CHEK2 and PSEM3-dependent manner and inhibits the activity of CHEK2 in vitro (PubMed:25361978). {ECO:0000269|PubMed:18235501, ECO:0000269|PubMed:18235502, ECO:0000269|PubMed:19131338, ECO:0000269|PubMed:19218236, ECO:0000269|PubMed:20074560, ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:22446626, ECO:0000269|PubMed:23352644, ECO:0000269|PubMed:23398316, ECO:0000269|PubMed:24415752, ECO:0000269|PubMed:24824780, ECO:0000269|PubMed:25361978, ECO:0000269|PubMed:25661920, ECO:0000269|PubMed:25732823}.; . TISSUE SPECIFICITY: Expressed in gastric carcinoma tissue and the expression gradually increases with the progression of the carcinoma (at protein level). Expressed ubiquitously in normal tissues. Expressed in 84 to 100% of neoplastic breast, lung, and colon tissues. {ECO:0000269|PubMed:12370419, ECO:0000269|PubMed:24962073}.; . . 0.70931 0.23392 -0.812021021 12.07242274 166.56911 2.82001 CCAT1 . . . colon cancer associated transcript 1 (non-protein coding) . . . . . . . . . . . CCAT2 . . . colon cancer associated transcript 2 (non-protein coding) . . . . . . . . . . . CCBE1 1.66521605518147e-06 0.651528421374705 0.34846991340924 collagen and calcium binding EGF domains 1 FUNCTION: Required for lymphangioblast budding and angiogenic sprouting from venous endothelium during embryogenesis. {ECO:0000269|PubMed:19935664}.; . TISSUE SPECIFICITY: Not expressed in blood or lymphatic endothelial cells. {ECO:0000269|PubMed:19287381}.; . . 0.16662 0.11306 -0.045835247 50.34206181 158.28616 2.74793 CCBL1 6.50937611869334e-08 0.436095607515433 0.563904327390805 cysteine conjugate-beta lyase, cytoplasmic FUNCTION: Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta- elimination of S-conjugates and Se-conjugates of L- (seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond. {ECO:0000269|PubMed:19338303}.; . . unclassifiable (Anatomical System);heart;ovary;tongue;muscle;urinary;parathyroid;fovea centralis;skin;uterus;lung;frontal lobe;nasopharynx;bone;placenta;macula lutea;liver;testis;cervix;head and neck;spleen;brain;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle;parietal lobe;cerebellum; 0.15245 0.45952 -0.26629572 34.81953291 107.83627 2.25558 CCBL2 3.04636359623202e-08 0.50791272183689 0.492087247699474 cysteine conjugate-beta lyase 2 FUNCTION: Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se- conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2- oxoglutarate as amino group acceptor (in vitro) (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;spinal ganglion;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion; 0.06535 0.15255 -0.047654689 50.22410946 234.28648 3.30806 CCDC3 0.000821908073152066 0.547648659002214 0.451529432924634 coiled-coil domain containing 3 . . TISSUE SPECIFICITY: Expressed in umbilical vein endothelial cells (HUVEC), and at lower levels in aortic smooth muscle cells (HASMC). {ECO:0000269|PubMed:20043878}.; . . 0.15992 0.11029 -0.271755481 34.31823543 162.20237 2.78192 CCDC6 0.967799855640717 0.0321980097080286 2.13465125475563e-06 coiled-coil domain containing 6 . DISEASE: Note=A chromosomal aberration involving CCDC6 is found in papillary thyroid carcinomas (PTCs). Inversion inv(10)(q11.2;q21) generates the RET/CCDC6 (PTC1) oncogene. {ECO:0000269|PubMed:2406025}.; TISSUE SPECIFICITY: Ubiquitously expressed.; unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;breast;uterus;prostate;frontal lobe;larynx;nasopharynx;thyroid;placenta;visual apparatus;liver;cervix;head and neck;kidney;brain;bladder; dorsal root ganglion;medulla oblongata;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.43670 0.16675 -0.137658575 43.57159707 4670.49647 13.75925 CCDC7 3.52388170883264e-09 0.759543088865829 0.240456907610289 coiled-coil domain containing 7 FUNCTION: May play a role in tumorigenesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in epithelium of normal cervix and cervical cancer. Overexpressed in early and interim cervical cancer. {ECO:0000269|PubMed:21109960}.; unclassifiable (Anatomical System);medulla oblongata;smooth muscle;thyroid;testis;brain; . 0.07858 0.07242 0.222355725 68.44184949 2589.1036 9.51873 CCDC8 0.16739700306093 0.818404187373483 0.0141988095655871 coiled-coil domain containing 8 FUNCTION: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695, PubMed:24793696). Required for localization of CUL7 to the centrosome (PubMed:24793695). {ECO:0000269|PubMed:24793695, ECO:0000269|PubMed:24793696}.; . TISSUE SPECIFICITY: Widely expressed with low levels in spleen, skeletal muscle, small intestine, kidney and liver. {ECO:0000269|PubMed:21737058}.; unclassifiable (Anatomical System);pancreas;lung;whole body;cartilage;ovary;thyroid;placenta;cervix;spleen;kidney;brain;stomach;thymus; dorsal root ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10639 0.06833 1.444070618 95.09318235 2463.65782 9.24155 CCDC9 1.56831799563654e-06 0.852198034726703 0.147800396955302 coiled-coil domain containing 9 . . . unclassifiable (Anatomical System);prostate;tongue;islets of Langerhans;larynx;bone;thyroid;duodenum;testis;blood;head and neck;brain;skin;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.23802 . 0.113945049 62.14319415 1532.11774 7.27488 CCDC11P1 . . . coiled-coil domain containing 11 pseudogene 1 . . . . . . . . . . . CCDC12 0.774130719749877 0.224226693574845 0.00164258667527767 coiled-coil domain containing 12 . . . lymphoreticular;ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;cartilage;heart;muscle;urinary;pharynx;blood;lens;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; cerebellum peduncles;placenta;pons; 0.08569 0.10124 0.104848986 61.49445624 117.06413 2.35259 CCDC13 1.15875211638949e-07 0.985142035768799 0.0148578483559892 coiled-coil domain containing 13 FUNCTION: Required for primary cilia formation and promotes the localization of the ciliopathy protein BBS4 to both centriolar satellites and cilia. {ECO:0000269|PubMed:24816561}.; . . unclassifiable (Anatomical System);optic nerve;lung;ovary;macula lutea;testis;fovea centralis;choroid;lens;retina; dorsal root ganglion;ciliary ganglion;pons;atrioventricular node; 0.08168 . 0.868987491 88.84760557 2247.98436 8.75517 CCDC13-AS1 . . . CCDC13 antisense RNA 1 . . . . . 0.08168 . . . . . CCDC14 3.40559309548439e-07 0.782396387674285 0.217603271766405 coiled-coil domain containing 14 FUNCTION: Negatively regulates centriole duplication. Negatively regulates CEP63 and CDK2 centrosomal localization. {ECO:0000269|PubMed:24613305, ECO:0000269|PubMed:26297806}.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;atrium;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;duodenum;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;testis - interstitial;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07379 0.08174 -0.376526807 28.10804435 445.97967 4.39638 CCDC15 3.21210263109898e-16 0.0182153988018179 0.981784601198182 coiled-coil domain containing 15 . . . unclassifiable (Anatomical System);testis;brain;skeletal muscle; dorsal root ganglion;testis - interstitial;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.03961 . -0.661316159 16.02382637 1881.71893 7.97727 CCDC17 3.58916148308353e-13 0.00603159109637954 0.993968408903262 coiled-coil domain containing 17 . . . lung;heart;hypothalamus;liver;spleen; . 0.04571 0.07831 0.396906589 76.30927105 308.99966 3.74344 CCDC18 . . . coiled-coil domain containing 18 . . . unclassifiable (Anatomical System);lymph node;lung;ovary;hypothalamus;thyroid;urinary;liver;testis;spleen;head and neck;blood;germinal center;mammary gland;bone marrow; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10485 0.09565 . . . . CCDC18-AS1 . . . CCDC18 antisense RNA 1 . . . . . . . . . . . CCDC22 0.995198908362386 0.00480060585391013 4.85783703866044e-07 coiled-coil domain containing 22 FUNCTION: Involved in regulation of NF-kappa-B signaling. Promotes ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent proteasomal degradation leading to NF-kappa-B activation; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. May down-regulate NF- kappa-B activity via assocation with COMMD1 and involving a CUL2- dependent E3 ubiquitin ligase complex. Regulates the cellular localization of COMM domain-containing proteins, such as COMMD1 and COMMD10 (PubMed:23563313). Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes (PubMed:25355947). {ECO:0000269|PubMed:23563313, ECO:0000269|PubMed:25355947}.; . TISSUE SPECIFICITY: Widely expressed in adult tissues and in fetal liver and brain, with highest levels in prostate and lowest in skeletal muscle. {ECO:0000269|PubMed:21826058}.; . . 0.09117 0.15035 0.709197509 85.68058504 86.31638 1.98428 CCDC24 2.01106420911485e-08 0.13498887526569 0.865011104623668 coiled-coil domain containing 24 . . . . . 0.06240 0.08575 0.306902668 72.38145789 267.06626 3.50410 CCDC25 0.051834010875526 0.927204983395743 0.0209610057287307 coiled-coil domain containing 25 . . . lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;aorta;stomach; caudate nucleus; 0.09520 0.07186 0.014844891 54.94810097 15.41906 0.55367 CCDC26 . . . CCDC26 long non-coding RNA . . TISSUE SPECIFICITY: Based on cell line studies, may be restricted to the myelocyte-monocyte lineage. {ECO:0000269|PubMed:16449964}.; . . . . . . . . CCDC27 1.60569656764963e-19 0.000771687660836762 0.999228312339163 coiled-coil domain containing 27 . . . testis; . 0.07703 0.09509 2.627531447 98.79688606 946.58435 5.96018 CCDC28A 1.49777690050185e-05 0.412012090989885 0.58797293124111 coiled-coil domain containing 28A . DISEASE: Note=A chromosomal aberration involving CCDC28A has been identified in acute leukemias. Translocation t(6;11)(q24.1;p15.5) with NUP98. The chimeric transcript is an in-frame fusion of NUP98 exon 13 to CCDC28A exon 2. Ectopic expression of NUP98-CCDC28A in mouse promotes the proliferative capacity and self-renewal potential of hematopoietic progenitors and rapidly induced fatal myeloproliferative neoplasms and defects in the differentiation of the erythro-megakaryocytic lineage. {ECO:0000269|PubMed:16028218}.; . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;artery;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;blood;lens;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;superior cervical ganglion;medulla oblongata;subthalamic nucleus;occipital lobe;trigeminal ganglion;parietal lobe;cingulate cortex; 0.04758 0.07704 0.350995466 74.37485256 918.02542 5.88980 CCDC28B 9.96843350374975e-08 0.0503624521717882 0.949637448143877 coiled-coil domain containing 28B FUNCTION: Involved in ciliogenesis. Regulates cilia length through its interaction with MAPKAP1/SIN1 but independently of mTORC2 complex. Modulates mTORC2 complex assembly and function, possibly enhances AKT1 phosphorylation. Does not seem to modulate assembly and function of mTORC1 complex. {ECO:0000269|PubMed:23015189, ECO:0000269|PubMed:23727834}.; DISEASE: Bardet-Biedl syndrome (BBS) [MIM:209900]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:16327777}. Note=The gene represented in this entry acts as a disease modifier.; . . . 0.17087 0.18345 0.25917371 70.05779665 340.90955 3.91778 CCDC30 6.06674580228951e-12 0.816726995363567 0.183273004630367 coiled-coil domain containing 30 . . TISSUE SPECIFICITY: Expressed in brain, kidney, pancreas, placenta, liver, thymus and prostate. {ECO:0000269|PubMed:16710767}.; unclassifiable (Anatomical System);lung;frontal lobe;ovary;testis;kidney; superior cervical ganglion;globus pallidus;trigeminal ganglion;skeletal muscle; . . 0.424410872 77.25878745 295.2174 3.66683 CCDC33 8.63487200520327e-09 0.97529710922535 0.0247028821397779 coiled-coil domain containing 33 . . . unclassifiable (Anatomical System);medulla oblongata;lung;endometrium;spleen; superior cervical ganglion;trigeminal ganglion; 0.08776 0.08702 1.139030387 92.34489266 4456.19559 13.38048 CCDC34 4.91354825835912e-07 0.228226898237574 0.7717726104076 coiled-coil domain containing 34 . DISEASE: Note=A chromosomal aberration involving CCDC34 is found in a patient with hamartoma of the retinal pigment epithelium and retina. Translocation t(11;18) (p13;p11.2). {ECO:0000269|PubMed:11173847}.; . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;thyroid;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;lens;breast;lung;cornea;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;trigeminal ganglion; 0.10209 0.09559 1.106059595 91.985138 2293.91406 8.87175 CCDC34P1 . . . coiled-coil domain containing 34 pseudogene 1 . . . . . . . . . . . CCDC36 0.509348612076541 0.489828466642529 0.000822921280929277 coiled-coil domain containing 36 . . . uterus;lung;cerebral cortex;larynx;placenta;testis;head and neck; . 0.08891 . -0.512444034 21.55579146 372.65459 4.07266 CCDC37-AS1 . . . CCDC37 antisense RNA 1 (head to head) . . . . . . . . . . . CCDC38 1.56677307281946e-08 0.827917917036778 0.172082067295491 coiled-coil domain containing 38 . . . optic nerve;lung;macula lutea;testis;fovea centralis;choroid;kidney;lens;retina; . 0.09545 . 0.446457185 77.97829677 2255.31221 8.77354 CCDC39 5.10298688091632e-05 0.998484337525323 0.00146463260586805 coiled-coil domain containing 39 FUNCTION: Required for assembly of dynein regulatory complex (DRC) and inner dynein arm (IDA) complexes, which are responsible for ciliary beat regulation, thereby playing a central role in motility in cilia and flagella (PubMed:21131972). Probably acts together with CCDC40 to form a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella (By similarity). Not required for outer dynein arm complexes assembly (PubMed:21131972). {ECO:0000250|UniProtKB:A8IQT2, ECO:0000269|PubMed:21131972}.; . TISSUE SPECIFICITY: Mainly expressed in nasal brushings and, to a lesser extent, in lungs and testis. {ECO:0000269|PubMed:21131972}.; testis; . 0.20304 . 1.249272484 93.46543996 854.34469 5.70834 CCDC39-AS1 . . . CCDC39 antisense RNA 1 . . . . . . . . . . . CCDC40 6.32159262183706e-11 0.989883744333487 0.0101162556032973 coiled-coil domain containing 40 FUNCTION: Required for assembly of dynein regulatory complex (DRC) and inner dynein arm (IDA) complexes, which are responsible for ciliary beat regulation, thereby playing a central role in motility in cilia and flagella (PubMed:21131974). Probably acts together with CCDC39 to form a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella (By similarity). Not required for outer dynein arm complexes assembly. Required for axonemal recruitment of CCDC39 (PubMed:21131974). {ECO:0000250|UniProtKB:A8IQT2, ECO:0000269|PubMed:21131974}.; DISEASE: Ciliary dyskinesia, primary, 15 (CILD15) [MIM:613808]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:21131974, ECO:0000269|PubMed:22693285, ECO:0000269|PubMed:23255504, ECO:0000269|PubMed:23402890, ECO:0000269|PubMed:25186273}. Note=The disease is caused by mutations affecting the gene represented in this entry. The disease is characterized by primary ciliary dyskinesia with inner dynein arm (IDA) defects and axonemal dizorganisation: defects in CCDC39 and CCDC40 constitute the major cause of this phenotype. {ECO:0000269|PubMed:22693285, ECO:0000269|PubMed:23255504}.; . unclassifiable (Anatomical System);uterus;prostate;endometrium;liver;testis;colon;kidney;mammary gland;skin;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22262 . 1.886893658 97.2811984 1499.71528 7.20782 CCDC42 1.68964027106202e-05 0.671327004777083 0.328656098820206 coiled-coil domain containing 42 . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; . 0.09334 0.10027 0.731244617 86.21137061 892.69554 5.82479 CCDC43 0.000257178261367413 0.928055348856618 0.0716874728820144 coiled-coil domain containing 43 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;endometrium;thyroid;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.20834 0.08257 -0.251530012 35.42108988 22.78453 0.76163 CCDC47 0.00258817681450808 0.994331312908287 0.00308051027720443 coiled-coil domain containing 47 . . . myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;cornea;placenta;hippocampus;duodenum;head and neck;kidney;stomach; amygdala;superior cervical ganglion; 0.46552 0.10992 -0.624497208 17.16206653 32.82785 1.01862 CCDC50 9.33289305733199e-06 0.983794370595387 0.0161962965115559 coiled-coil domain containing 50 FUNCTION: Involved in EGFR signaling. {ECO:0000269|PubMed:15314609}.; DISEASE: Deafness, autosomal dominant, 44 (DFNA44) [MIM:607453]: A form of non-syndromic deafness characterized by initially moderate hearing loss that affects mainly low to mid frequencies. Later, it progresses to involve all the frequencies and leads to a profound hearing loss by the 6th decade. {ECO:0000269|PubMed:17503326}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 and isoform 2 are coexpressed in placenta, liver, lung, kidney and pancreas. Only isoform 1 is detected in skeletal muscle, brain and heart. {ECO:0000269|PubMed:14527723}.; . . 0.04690 0.09305 1.264035907 93.58339231 267.95986 3.51256 CCDC51 1.46055955445772e-06 0.622918420828266 0.37708011861218 coiled-coil domain containing 51 . . . . . 0.09891 0.10830 0.130533008 63.35810333 164.1155 2.79754 CCDC53 0.0351259294423371 0.827566748437168 0.137307322120495 coiled-coil domain containing 53 FUNCTION: Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes seems to inhibit WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization, and which is involved in regulation of the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:19922875, PubMed:20498093). {ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093}.; . . smooth muscle;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;whole body;optic nerve;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;lens;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;macula lutea;liver;spleen;head and neck;kidney;mammary gland;aorta; thalamus;testis - interstitial;occipital lobe;superior cervical ganglion;hypothalamus;spinal cord;white blood cells;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;trigeminal ganglion;parietal lobe;pituitary;cerebellum; 0.22102 . 0.103030231 61.2762444 4.29196 0.15599 CCDC54 8.5500859196346e-08 0.0460909438981926 0.953908970600948 coiled-coil domain containing 54 . . . unclassifiable (Anatomical System);lung;testis; . 0.05437 . 1.128108522 92.19155461 1057.96509 6.24432 CCDC57 2.63627612154765e-13 0.12669149614854 0.873308503851197 coiled-coil domain containing 57 . . . unclassifiable (Anatomical System);heart;lacrimal gland;salivary gland;colon;parathyroid;skin;breast;uterus;optic nerve;lung;larynx;epididymis;thyroid;pituitary gland;liver;testis;head and neck;spleen;germinal center;kidney;brain;stomach;cerebellum; amygdala;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.11345 . . . 6440.44336 16.84943 CCDC58 0.0802761221198354 0.872108393793176 0.0476154840869887 coiled-coil domain containing 58 . . . unclassifiable (Anatomical System);prostate;lung;endometrium;nasopharynx;testis;germinal center;stomach;retina; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.59208 0.11262 -0.09720619 46.20193442 9.0286 0.33094 CCDC58P1 . . . coiled-coil domain containing 58 pseudogene 1 . . . . . . . . . . . CCDC58P2 . . . coiled-coil domain containing 58 pseudogene 2 . . . . . . . . . . . CCDC58P3 . . . coiled-coil domain containing 58 pseudogene 3 . . . . . . . . . . . CCDC58P4 . . . coiled-coil domain containing 58 pseudogene 4 . . . . . . . . . . . CCDC58P5 . . . coiled-coil domain containing 58 pseudogene 5 . . . . . . . . . . . CCDC59 0.000680494758463173 0.745417966869702 0.253901538371835 coiled-coil domain containing 59 FUNCTION: Component of the transcription complexes of the pulmonary surfactant-associated protein-B (SFTPB) and -C (SFTPC). Enhances homeobox protein Nkx-2.1-activated SFTPB and SFTPC promoter activities. {ECO:0000269|PubMed:12882447, ECO:0000269|PubMed:16630564}.; . TISSUE SPECIFICITY: Ubiquitously expressed. In lung, expression is restricted to the alveolar epithelial cells. {ECO:0000269|PubMed:11152647}.; ovary;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;duodenum;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;thyroid;testis;white blood cells;trigeminal ganglion; 0.34082 0.09590 1.060147109 91.46614768 94.89472 2.10013 CCDC60 8.62068411387964e-06 0.98192372080994 0.0180676585059458 coiled-coil domain containing 60 . . . optic nerve;lung;hypothalamus;macula lutea;visual apparatus;testis;fovea centralis;choroid;lens;retina; . 0.07956 0.07603 0.714657953 85.81623024 1958.48978 8.14783 CCDC61 2.17088367458532e-05 0.724166755458239 0.275811535705015 coiled-coil domain containing 61 . . . unclassifiable (Anatomical System);lymph node;smooth muscle;heart;islets of Langerhans;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;bone;macula lutea;testis;cervix;germinal center;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.08341 . 0.688969636 85.20877565 1802.87858 7.83603 CCDC62 1.43534739270012e-12 0.094050787173188 0.905949212825377 coiled-coil domain containing 62 FUNCTION: Nuclear receptor coactivator that can enhance preferentially estrogen receptors ESR1 and ESR2 transactivation. Modulates also progesterone/PGR, glucocorticoid/NR3C1 and androgen/AR receptors transactivation, although at lower level; little effect on vitamin D receptor/VDR. {ECO:0000269|PubMed:19126643}.; . TISSUE SPECIFICITY: Highly expressed in adult testis. Expressed in both prostate epithelial and stromal cells, with predominant expression in epithelial cells (at protein level) (PubMed:19126643). Not detected in prostate by RT-PCR (PubMed:19165854). Overexpressed in various cancers. {ECO:0000269|PubMed:19126643, ECO:0000269|PubMed:19165854, ECO:0000269|Ref.1, ECO:0000269|Ref.4}.; unclassifiable (Anatomical System);prostate;lung;placenta;hippocampus;testis;blood;bone marrow; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11133 0.14603 0.578735925 82.29535268 495.50149 4.57476 CCDC63 4.48038323358414e-10 0.557449334449297 0.442550665102665 coiled-coil domain containing 63 . . . unclassifiable (Anatomical System);medulla oblongata;lung;cerebral cortex;testis; . 0.06887 . 0.780798785 87.24345364 289.79492 3.64108 CCDC64 0.549254948786093 0.450720363455877 2.46877580299545e-05 coiled-coil domain containing 64 FUNCTION: Component of secretory vesicle machinery in developing neurons that acts as a regulator of neurite outgrowth. Regulates the secretory vesicle transport by controlling the accumulation of Rab6-containing secretory vesicles in the pericentrosomal region restricting anterograde secretory transport during the early phase of neuronal differentiation, thereby inhibiting neuritogenesis (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;ovary;sympathetic chain;colon;fovea centralis;choroid;lens;skin;retina;pancreas;optic nerve;lung;frontal lobe;endometrium;thyroid;macula lutea;testis;head and neck;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.06748 . -0.582225231 18.44184949 43.43177 1.25457 CCDC64B 5.72990223004394e-06 0.678075302654001 0.321918967443769 coiled-coil domain containing 64B . . . . . . 0.09584 . . 5786.56101 15.76995 CCDC65 9.59689476863394e-07 0.767874570927462 0.232124469383061 coiled-coil domain containing 65 FUNCTION: May play a role in motile cilia function, possibly by acting on the assembly of the nexin-dynein regulatory complex. {ECO:0000269|PubMed:24094744}.; . TISSUE SPECIFICITY: Highly expressed in adult testis, in spermatocytes and spermatids. Also observed in spermatogonia. Not detected in Leydig cells, nor in fetal testis (at protein level). {ECO:0000269|PubMed:17089017}.; unclassifiable (Anatomical System);breast;meninges;pia mater;lung;whole body;nasopharynx;testis;kidney;dura mater;skin;stomach; . 0.14032 0.09346 1.399970837 94.72753008 4074.89006 12.66428 CCDC66 8.98685926047288e-28 5.32943044591586e-05 0.999946705695541 coiled-coil domain containing 66 . . . ovary;colon;bone marrow;uterus;prostate;whole body;endometrium;larynx;thyroid;bone;pituitary gland;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;pharynx;blood;lung;nasopharynx;visual apparatus;liver;head and neck;kidney;stomach;aorta;peripheral nerve; . 0.06976 . 0.808316435 87.73295589 3801.22948 12.11059 CCDC67 2.60445763225589e-11 0.249421573514221 0.750578426459734 coiled-coil domain containing 67 FUNCTION: Key structural component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells and can generate more than 100 centrioles. Probably sufficient for the specification and formation of the deuterosome inner core. Interacts with CEP152 and recruits PLK4 to activate centriole biogenesis (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);prostate;lung;testis; superior cervical ganglion;testis - interstitial;adrenal gland;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08811 0.08226 1.377921151 94.56829441 1327.65052 6.84621 CCDC68 6.41317549868977e-07 0.448308195784666 0.551691162897784 coiled-coil domain containing 68 . . TISSUE SPECIFICITY: Expressed in bone marrow, colon, small intestine, spleen, testis, trachea and cutaneous T-cell lymphoma (CTCL). {ECO:0000269|PubMed:11149944, ECO:0000269|PubMed:15142679}.; unclassifiable (Anatomical System);lung;whole body;placenta;pituitary gland;alveolus;testis;cervix;kidney;brain;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07169 0.08382 0.52918614 80.81505072 313.54751 3.76453 CCDC69 3.78649706533996e-08 0.338359517456597 0.661640444678432 coiled-coil domain containing 69 . . . lymphoreticular;myocardium;ovary;colon;parathyroid;vein;bone marrow;uterus;cerebral cortex;endometrium;larynx;bone;testis;germinal center;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;heart;blood;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;head and neck;spleen;mammary gland;thymus; adipose tissue;adrenal gland;adrenal cortex;white blood cells;skeletal muscle; 0.07796 . 0.797386419 87.53833451 3410.22371 11.18722 CCDC70 0.0531534616697279 0.862961184223468 0.0838853541068044 coiled-coil domain containing 70 . . . unclassifiable (Anatomical System);lung;testis; testis - interstitial;testis - seminiferous tubule;testis; 0.05430 0.07770 0.174625237 65.9648502 226.62861 3.25324 CCDC71 0.0169896394893115 0.960104426261335 0.0229059342493534 coiled-coil domain containing 71 . . . unclassifiable (Anatomical System);prostate;pancreas;lung;ovary;placenta;testis;colon;parathyroid;spleen;head and neck;brain; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;ciliary ganglion;caudate nucleus;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.33082 . 0.064394823 58.84642604 54.37742 1.47436 CCDC71L 0.482182658122372 0.436610465058279 0.0812068768193497 coiled-coil domain containing 71-like . . . . . . . . . 3.25401 0.11726 CCDC73 1.19030024122162e-13 0.151016715354846 0.848983284645035 coiled-coil domain containing 73 . . . ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;bladder;brain;heart;cartilage;pineal body;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;kidney;stomach;aorta;thymus; . 0.25663 . 0.248041348 69.61547535 146.14973 2.63445 CCDC74A 1.16806309975737e-05 0.590852955184721 0.409135364184281 coiled-coil domain containing 74A . . . unclassifiable (Anatomical System);medulla oblongata;lymph node;heart;ovary;colon;parathyroid;blood;lens;skin;uterus;pancreas;prostate;lung;endometrium;bone;placenta;liver;testis;cervix;spleen;brain;mammary gland;stomach; . 0.08413 . 1.844633838 97.09837226 1294.94009 6.77377 CCDC74B 1.19190170799534e-06 0.357002129569881 0.642996678528411 coiled-coil domain containing 74B . . . unclassifiable (Anatomical System);medulla oblongata;heart;colon;lens;skin;uterus;pancreas;prostate;lung;endometrium;bone;placenta;iris;pituitary gland;liver;testis;spleen;cervix;kidney;brain;pineal gland;mammary gland;stomach; . . . 0.913082291 89.54352442 2169.74246 8.57555 CCDC74BP1 . . . coiled-coil domain containing 74B pseudogene 1 . . . . . . . . . . . CCDC75P1 . . . coiled-coil domain containing 75 pseudogene 1 . . . . . . . . . . . CCDC77 9.40308683942061e-15 0.0186282195186333 0.981371780481357 coiled-coil domain containing 77 . . . unclassifiable (Anatomical System);heart;cerebellum cortex;tongue;adrenal cortex;colon;skin;uterus;prostate;whole body;lung;frontal lobe;oesophagus;bone;placenta;liver;testis;head and neck;spleen;kidney;mammary gland; testis - interstitial; 0.05492 . 0.622829232 83.47487615 1387.09143 6.97153 CCDC78 1.71263612100492e-19 0.00041604001507477 0.999583959984925 coiled-coil domain containing 78 FUNCTION: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells (G1/0) and not in S phase. Essential for centriole amplification and is required for CEP152 localization to the deuterosome. {ECO:0000269|PubMed:24075808}.; . TISSUE SPECIFICITY: Expressed primarily in skeletal muscle. {ECO:0000269|PubMed:22818856}.; unclassifiable (Anatomical System);lymph node;islets of Langerhans;colon;blood;lens;lung;placenta;bone;testis;spleen;kidney;brain; superior cervical ganglion;ciliary ganglion;skeletal muscle;parietal lobe; 0.08318 . 1.423841958 94.96933239 109.12402 2.26754 CCDC79 . . . coiled-coil domain containing 79 FUNCTION: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the MAJIN-TERB1- TERB2 complex, TERB1 probably mediates association with the shelterin/telosome complex via interaction with TERF1, promoting priming telomeric DNA attachment'. Promotes telomere association with the nuclear envelope and deposition of the SUN-KASH/LINC complex. Also recruits cohesin to telomeres to develop structural rigidity. {ECO:0000250|UniProtKB:Q8C0V1}.; . . testis; . . . . . 1617.34475 7.43919 CCDC80 0.00584309877267669 0.99320269687857 0.000954204348753192 coiled-coil domain containing 80 FUNCTION: Promotes cell adhesion and matrix assembly. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in dermal papilla and dermal fibroblasts (at protein level). Expressed in heart, thymus, placenta, pancreas, colon, epithelium, spleen and osteoblasts. {ECO:0000269|PubMed:15325258, ECO:0000269|PubMed:15563452, ECO:0000269|PubMed:15998583}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pineal body;lens;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; uterus;superior cervical ganglion;smooth muscle;adipose tissue;heart;testis;ciliary ganglion; 0.60637 0.14040 -0.191064116 39.27813163 660.85004 5.15423 CCDC81 2.78823114302232e-09 0.897689747858359 0.10231024935341 coiled-coil domain containing 81 . . . unclassifiable (Anatomical System);medulla oblongata;prostate;lung;cartilage;testis;blood;retina; superior cervical ganglion;testis; 0.06368 . 1.155610133 92.59259259 889.04414 5.80784 CCDC82 1.73421696254218e-07 0.643610670936301 0.356389155642002 coiled-coil domain containing 82 . . . myocardium;ovary;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;tongue;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;medulla oblongata;globus pallidus;parietal lobe; 0.09931 . 0.821252311 88.01604152 2363.16637 9.01804 CCDC83 6.83032869950337e-07 0.699068335301507 0.300930981665623 coiled-coil domain containing 83 . . . unclassifiable (Anatomical System);lung;testis; testis - interstitial;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.02816 0.07783 1.129924507 92.23283793 1027.35274 6.16004 CCDC84 4.70436509120475e-06 0.850051155297292 0.149944140337616 coiled-coil domain containing 84 . . . myocardium;lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;placenta;kidney;stomach;aorta; . 0.09744 . -0.381986487 27.68931352 38.22504 1.13528 CCDC85A 0.00173520517334067 0.894912274886586 0.103352519940074 coiled-coil domain containing 85A . . . . . 0.11972 0.09438 0.040529541 57.15380986 1143.32157 6.44627 CCDC85B 0.491379557770827 0.431724165112664 0.0768962771165092 coiled-coil domain containing 85B FUNCTION: Functions as a transcriptional repressor. May inhibit the activity of CTNNB1 in a TP53-dependent manner and thus regulate cell growth. May function in adipocyte differentiation, negatively regulating mitotic clonal expansion. {ECO:0000269|PubMed:17014843, ECO:0000269|PubMed:17873903}.; . TISSUE SPECIFICITY: Widely expressed including liver.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;cerebellum peduncles;temporal lobe;caudate nucleus;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex; 0.20127 0.13478 . . 40.55287 1.18897 CCDC85C . . . coiled-coil domain containing 85C FUNCTION: May play an important role in cortical development, especially in the maintenance of radial glia. {ECO:0000250}.; . . . . 0.06758 . . . 502.28745 4.59775 CCDC86 0.00147735697356089 0.966725865626923 0.0317967773995161 coiled-coil domain containing 86 . . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node; 0.18348 0.09415 0.707379532 85.62750649 359.74826 4.01631 CCDC87 3.05913441954035e-06 0.541564505871106 0.458432434994474 coiled-coil domain containing 87 . . . unclassifiable (Anatomical System);blood;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;placenta;macula lutea;hippocampus;liver;testis;cervix;kidney;brain; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.12243 0.08922 0.202129237 67.42745931 213.95782 3.15617 CCDC88A 0.999999956100474 4.3899526335792e-08 8.71275956737586e-23 coiled-coil domain containing 88A FUNCTION: Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Enhances phosphoinositide 3-kinase (PI3K)-dependent phosphorylation and kinase activity of AKT1/PKB, but does not possess kinase activity itself. Phosphorylation of AKT1/PKB thereby induces the phosphorylation of downstream effectors GSK3 and FOXO1/FKHR, and regulates DNA replication and cell proliferation (By similarity). Essential for the integrity of the actin cytoskeleton and for cell migration. Required for formation of actin stress fibers and lamellipodia. May be involved in membrane sorting in the early endosome. {ECO:0000250, ECO:0000269|PubMed:15882442, ECO:0000269|PubMed:16139227}.; . TISSUE SPECIFICITY: Expressed ubiquitously. {ECO:0000269|PubMed:16139227}.; lymphoreticular;smooth muscle;ovary;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;atrium;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;hippocampus;macula lutea;visual apparatus;liver;cervix;head and neck;kidney;aorta; superior cervical ganglion;testis - interstitial;subthalamic nucleus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.22232 0.13422 -1.567158756 3.190610993 248.0021 3.39453 CCDC88B 0.000929045236295006 0.999070023479384 9.31284320452798e-07 coiled-coil domain containing 88B . . . lymphoreticular;unclassifiable (Anatomical System);lymph node;ovary;colon;blood;skeletal muscle;bone marrow;uterus;pancreas;prostate;lung;bone;thyroid;placenta;iris;alveolus;testis;spleen;brain; white blood cells;ciliary ganglion;atrioventricular node;skeletal muscle;cerebellum; 0.13890 . 0.282839608 71.08398207 2110.34993 8.45720 CCDC88C 2.17322769994979e-06 0.999997442906594 3.83865705821721e-07 coiled-coil domain containing 88C FUNCTION: Negative regulator of the canonical Wnt signaling pathway, acting downstream of DVL to inhibit CTNNB1/Beta-catenin stabilization (By similarity). May also activate the JNK signaling pathway (PubMed:25062847). {ECO:0000250|UniProtKB:Q6VGS5, ECO:0000269|PubMed:25062847}.; DISEASE: Hydrocephalus, non-syndromic, autosomal recessive 1 (HYC1) [MIM:236600]: A disease characterized by a disturbance of cerebrospinal fluid circulation causing accumulation of ventricular cerebrospinal fluid, which results in progressive ventricular dilatation with onset in utero. Affected individuals may have neurologic impairment. {ECO:0000269|PubMed:21031079, ECO:0000269|PubMed:23042809}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spinocerebellar ataxia 40 (SCA40) [MIM:616053]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA38 is an autosomal dominant form characterized by adult-onset of slowly progressive gait ataxia accompanied by nystagmus. Brain MRI shows cerebellar atrophy. {ECO:0000269|PubMed:25062847}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;bone;blood;germinal center;bone marrow; superior cervical ganglion;white blood cells;ciliary ganglion;caudate nucleus;atrioventricular node;skeletal muscle; 0.12404 0.10177 1.142713576 92.38027837 906.05602 5.85803 CCDC89 0.00582182407300908 0.726777139319969 0.267401036607022 coiled-coil domain containing 89 . . . unclassifiable (Anatomical System);medulla oblongata;lung;bone;testis;colon;brain; testis - interstitial;testis - seminiferous tubule; 0.33228 0.08354 -0.314027422 31.9297004 56.77066 1.51634 CCDC90AP1 . . . coiled-coil domain containing 90A pseudogene 1 . . . . . . . . . . . CCDC90B 0.0090638207534691 0.937639501506812 0.0532966777397193 coiled-coil domain containing 90B . . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;stomach; amygdala;testis - interstitial;medulla oblongata;superior cervical ganglion;fetal brain;testis - seminiferous tubule;spinal cord;testis;ciliary ganglion;atrioventricular node;pons; 0.14281 0.09698 0.549415813 81.38122199 88.38564 2.01561 CCDC91 3.15157303302004e-05 0.938516164539176 0.0614523197304935 coiled-coil domain containing 91 FUNCTION: Involved in the regulation of membrane traffic through the trans-Golgi network (TGN).; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12808037}.; colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;larynx;thyroid;bone;testis;germinal center;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;breast;lung;adrenal gland;placenta;macula lutea;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; amygdala;medulla oblongata;superior cervical ganglion;trigeminal ganglion; 0.14552 0.08447 1.039913547 91.25973107 1889.87639 7.99403 CCDC92 0.368849605751602 0.619687629385028 0.01146276486337 coiled-coil domain containing 92 . . . myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;cerebellum; amygdala;thalamus;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;cingulate cortex; 0.33278 0.10777 0.066214104 58.95848077 2196.97617 8.62866 CCDC92B . . . coiled-coil domain containing 92B . . . . . . . . . . . CCDC93 0.064375261486792 0.935623661045723 1.07746748473906e-06 coiled-coil domain containing 93 FUNCTION: Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes and is dependent on its interaction with FAM21C (PubMed:25355947). {ECO:0000269|PubMed:25355947}.; . . lymphoreticular;cerebral cortex;endometrium;larynx;visual apparatus;liver;colon;spleen;head and neck;brain; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08209 0.08601 -0.088107893 47.06298655 799.6596 5.57245 CCDC94 0.00096047083699541 0.94343768415848 0.0556018450045248 coiled-coil domain containing 94 . . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;cartilage;heart;lacrimal gland;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; superior cervical ganglion;cerebellum peduncles;placenta;white blood cells; 0.09717 . -0.492218069 22.35786742 28.13525 0.90173 CCDC96 2.70543466349121e-06 0.515356607992416 0.48464068657292 coiled-coil domain containing 96 . . . unclassifiable (Anatomical System);pancreas;optic nerve;cartilage;ovary;endometrium;placenta;macula lutea;parathyroid;fovea centralis;choroid;lens;brain;retina; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion; 0.08434 . -0.514264485 21.41424864 130.46018 2.48788 CCDC97 2.83817318207507e-08 0.0877201569698856 0.912279814648382 coiled-coil domain containing 97 . . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;muscle;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.09346 . -0.88906181 10.36801132 38.90288 1.15262 CCDC102A 9.21570601625823e-05 0.789120793384499 0.210787049555339 coiled-coil domain containing 102A . . . unclassifiable (Anatomical System);cartilage;pancreas;prostate;lung;cerebral cortex;endometrium;larynx;placenta;bone;head and neck;spleen;cervix;kidney;brain;mammary gland; superior cervical ganglion;trigeminal ganglion; 0.15489 . . . 59.69648 1.56860 CCDC102B 3.31193608462394e-09 0.304915311599463 0.695084685088601 coiled-coil domain containing 102B . . . unclassifiable (Anatomical System);lung;whole body;cartilage;islets of Langerhans;larynx;testis;spleen;head and neck;kidney;mammary gland;retina; superior cervical ganglion;uterus corpus;skeletal muscle; 0.71689 0.08539 1.822581424 97.02170323 3864.66325 12.25371 CCDC103 0.00218552270508304 0.755240447160889 0.242574030134028 coiled-coil domain containing 103 FUNCTION: Dynein-attachment factor required for cilia motility. {ECO:0000269|PubMed:22581229}.; DISEASE: Ciliary dyskinesia, primary, 17 (CILD17) [MIM:614679]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:22581229, ECO:0000269|PubMed:25186273}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;cartilage;parathyroid;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;prostate;optic nerve;lung;endometrium;placenta;bone;macula lutea;testis;brain; superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;skeletal muscle; 0.10907 . -0.383807564 27.41802312 7.00426 0.26176 CCDC105 2.33924477325218e-10 0.0379129163870659 0.96208708337901 coiled-coil domain containing 105 . . . . . 0.11587 . 1.530453833 95.52960604 2555.99385 9.43994 CCDC106 0.010803208229833 0.834896814723538 0.154299977046629 coiled-coil domain containing 106 FUNCTION: Promotes the degradation of p53/TP53 protein and inhibits its transactivity. {ECO:0000269|PubMed:20159018}.; . . salivary gland;colon;skin;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;bone;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;hypothalamus;muscle;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; whole brain;subthalamic nucleus;prefrontal cortex;ciliary ganglion; 0.11500 0.10594 -0.22584292 37.32012267 2072.22067 8.38618 CCDC107 1.69816301679586e-07 0.128261354320056 0.871738475863643 coiled-coil domain containing 107 . . . . . 0.00702 0.04817 0.17280645 65.75843359 751.4715 5.43757 CCDC109B 0.00614925695036299 0.907855771259678 0.085994971789959 coiled-coil domain containing 109B FUNCTION: Negatively regulates the activity of MCU, the mitochondrial inner membrane calcium uniporter, and thereby modulates calcium uptake into the mitochondrion. Does not form functional calcium channels by itself. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways. {ECO:0000250|UniProtKB:Q810S1}.; . . . . 0.10395 0.08737 0.395088462 76.15003539 2458.3126 9.22852 CCDC110 1.34679613842264e-08 0.571522479453222 0.428477507078817 coiled-coil domain containing 110 . . TISSUE SPECIFICITY: Expressed specifically in testis. Also expressed in tumors of different origins. {ECO:0000269|PubMed:15447989}.; unclassifiable (Anatomical System);uterus;pancreas;lung;heart;cochlea;islets of Langerhans;testis;kidney;skin; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;appendix;testis;ciliary ganglion; 0.09113 0.08327 3.004392866 99.21561689 2433.27149 9.16393 CCDC112 0.821147626124143 0.178816765454547 3.56084213102203e-05 coiled-coil domain containing 112 . . . . . 0.26944 0.09900 -0.203796826 38.81811748 330.76803 3.86663 CCDC113 3.94970170501918e-13 0.0235246091127678 0.976475390886837 coiled-coil domain containing 113 FUNCTION: Component of centriolar satellites contributing to primary cilium formation. {ECO:0000269|PubMed:25074808}.; . . myocardium;medulla oblongata;ovary;umbilical cord;salivary gland;intestine;colon;parathyroid;skin;prostate;cochlea;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);pharynx;blood;breast;lung;nasopharynx;placenta;hippocampus;liver;spleen;cervix;kidney;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion; 0.05168 0.08022 -0.336073593 30.55555556 127.02556 2.45806 CCDC114 0.00270689727205249 0.936351114310288 0.0609419884176594 coiled-coil domain containing 114 FUNCTION: Probable component of the outer dynein arm complex required along the entire axoneme for tethering of outer dynein arms. {ECO:0000305|PubMed:23261302, ECO:0000305|PubMed:23261303}.; DISEASE: Ciliary dyskinesia, primary, 20 (CILD20) [MIM:615067]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia. Patients may exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. Unlike other forms of CILD characterized by reduced fertility, patients with CILD20 do not appear to be infertile. {ECO:0000269|PubMed:23261302, ECO:0000269|PubMed:23261303}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lung;cartilage;testis;spleen; dorsal root ganglion;temporal lobe;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.09978 . 1.42749112 94.99292286 2463.6872 9.24341 CCDC115 1.51132252418088e-05 0.413712291670279 0.586272595104479 coiled-coil domain containing 115 . . TISSUE SPECIFICITY: Expressed throughout the brain. {ECO:0000269|PubMed:16378758}.; lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;ganglion;frontal lobe;endometrium;germinal center;brain;heart;cartilage;tongue;urinary;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.10954 0.09943 -0.251530012 35.42108988 17.91292 0.62591 CCDC116 3.97673357670938e-05 0.615426427607614 0.384533805056619 coiled-coil domain containing 116 . . . unclassifiable (Anatomical System);medulla oblongata;lung;thyroid;testis; . 0.08694 0.09640 2.627531447 98.79688606 2918.90932 10.25093 CCDC117 0.619564484902431 0.37264141515937 0.00779409993819867 coiled-coil domain containing 117 . . . ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;uterus;prostate;frontal lobe;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;small intestine;heart;urinary;pharynx;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;kidney;stomach;thymus; globus pallidus;ciliary ganglion; 0.16945 . -0.029247611 51.40363293 54.53812 1.47685 CCDC120 0.691311336063518 0.304612985678745 0.00407567825773714 coiled-coil domain containing 120 FUNCTION: Required for neurite growth. Localizes CYTH2 to vesicles to allow its transport along neurites, and subsequent ARF6 activation and neurite growth. {ECO:0000269|PubMed:25326380}.; . . . . 0.20757 0.10346 -0.025608647 51.91672564 88.84333 2.02374 CCDC121 9.72713578876563e-05 0.567699181941003 0.432203546701109 coiled-coil domain containing 121 . . . unclassifiable (Anatomical System);prostate;lung;endometrium;placenta;visual apparatus;hippocampus;testis;germinal center;brain;retina; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.01369 . -0.181750739 40.15687662 66.00812 1.67375 CCDC122 8.65057685310611e-08 0.163299096805915 0.836700816688317 coiled-coil domain containing 122 . . . uterus;lung;heart;testis;kidney;germinal center;skin; . 0.24754 0.09428 0.237127192 68.98443029 85.78159 1.97763 CCDC124 0.316957011367778 0.614140640121372 0.0689023485108504 coiled-coil domain containing 124 FUNCTION: Required for proper progression of late cytokinetic stages. {ECO:0000269|PubMed:23894443}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:23894443}.; . . 0.23567 . -0.293801652 32.93819297 161.0951 2.77266 CCDC125 8.05457406388208e-06 0.916723154835866 0.0832687905900698 coiled-coil domain containing 125 FUNCTION: May be involved in the regulation of cell migration. {ECO:0000269|PubMed:19787194}.; . . . . 0.13944 . 0.885576705 89.14248644 2879.04177 10.15783 CCDC126 0.351142326713522 0.594015184322855 0.0548424889636222 coiled-coil domain containing 126 . . . unclassifiable (Anatomical System);heart;islets of Langerhans;urinary;colon;skin;skeletal muscle;uterus;breast;prostate;lung;thyroid;testis;germinal center;kidney;brain;mammary gland;aorta;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.24249 0.10038 0.080983847 59.76055674 35.3147 1.06747 CCDC127 0.0209574915978507 0.90627529920313 0.0727672091990191 coiled-coil domain containing 127 . . . ovary;salivary gland;intestine;colon;parathyroid;retina;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion; 0.13067 0.10050 0.016664174 55.21939137 132.58028 2.50524 CCDC129 2.61411786914665e-17 0.00803444583961254 0.991965554160387 coiled-coil domain containing 129 . . . unclassifiable (Anatomical System);lung;testis;kidney; dorsal root ganglion;superior cervical ganglion;temporal lobe;ciliary ganglion;atrioventricular node; 0.05478 . 1.83172441 97.03939608 3581.71245 11.57466 CCDC130 0.0250490309774666 0.961777522855995 0.0131734461665382 coiled-coil domain containing 130 . . . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;skin;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; . 0.08853 0.09446 0.176444282 66.07100731 341.94368 3.92106 CCDC134 0.000741172780034662 0.762168993293845 0.23708983392612 coiled-coil domain containing 134 . . . unclassifiable (Anatomical System);fovea centralis;choroid;lens;skeletal muscle;retina;pancreas;prostate;optic nerve;whole body;lung;frontal lobe;thyroid;bone;macula lutea;visual apparatus;head and neck;cervix;germinal center;kidney; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.08136 0.10647 -0.337894035 30.37272942 83.87529 1.95005 CCDC136 4.88758232322395e-08 0.952703993969738 0.0472959571544386 coiled-coil domain containing 136 . . TISSUE SPECIFICITY: Expressed in gastric tissues. Down-regulated in gastric cancer. {ECO:0000269|PubMed:15112360}.; unclassifiable (Anatomical System);cartilage;fovea centralis;choroid;lens;skin;retina;pancreas;optic nerve;lung;frontal lobe;endometrium;nasopharynx;macula lutea;liver;testis;spleen;cervix;kidney;brain;mammary gland;aorta; dorsal root ganglion;testis - interstitial;thalamus;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;pons; 0.11110 0.09982 0.297596326 71.67964142 695.17998 5.25507 CCDC137 0.0001014857442089 0.806413265148472 0.193485249107319 coiled-coil domain containing 137 . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;hypothalamus;muscle;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node; 0.04020 0.09039 1.063778722 91.58410002 2953.01048 10.29824 CCDC137P . . . coiled-coil domain containing 137 pseudogene . . . . . . . . . . . CCDC138 1.08334074018145e-05 0.986815955496533 0.0131732110960653 coiled-coil domain containing 138 . . . unclassifiable (Anatomical System);heart;ovary;cartilage;pharynx;colon;skeletal muscle;skin;uterus;lung;liver;testis;kidney; . 0.15822 . -0.464712395 23.5727766 2253.24012 8.76685 CCDC140 0.0630857519946017 0.724905646269007 0.212008601736392 coiled-coil domain containing 140 . . . . . 0.04624 . 0.369407109 74.95281906 40.8557 1.19686 CCDC141 1.4276211576785e-09 0.7987306526053 0.201269345967078 coiled-coil domain containing 141 FUNCTION: Plays a critical role in radial migration and centrosomal function. {ECO:0000250|UniProtKB:A2AST1}.; . . lung;whole body;heart;spinal cord;visual apparatus;adrenal cortex;liver;germinal center;skeletal muscle; . 0.21191 0.08688 . . 2581.13384 9.50088 CCDC142 0.000167047986406049 0.998514109481962 0.00131884253163157 coiled-coil domain containing 142 . . . unclassifiable (Anatomical System);lung;frontal lobe;placenta;visual apparatus;liver;testis;brain;peripheral nerve; . 0.11145 . 1.201528238 93.00542581 355.29089 3.98785 CCDC144A . . . coiled-coil domain containing 144A . . . amygdala;unclassifiable (Anatomical System);lung;frontal lobe;endometrium;thyroid;testis;blood;germinal center;brain;skeletal muscle;bone marrow; superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion; 0.01642 . . . 839.461 5.67541 CCDC144B . . . coiled-coil domain containing 144B (pseudogene) . . . unclassifiable (Anatomical System);amygdala;uterus;frontal lobe;endometrium;islets of Langerhans;blood;skeletal muscle;stomach;bone marrow; . 0.01974 . . . . . CCDC144CP . . . coiled-coil domain containing 144C, pseudogene . . . . . . . . . . . CCDC144NL 8.14314604314923e-06 0.171830685529798 0.828161171324159 coiled-coil domain containing 144 family, N-terminal like . . . amygdala;testis;skeletal muscle; . . . 1.26585432 93.59518754 271.43253 3.53005 CCDC144NL-AS1 . . . CCDC144NL antisense RNA 1 . . . . . . . . . . . CCDC146 3.02024489245997e-18 0.0585495044455099 0.94145049555449 coiled-coil domain containing 146 . . . unclassifiable (Anatomical System);meninges;smooth muscle;cartilage;heart;colon;skin;retina;uterus;bile duct;pia mater;lung;endometrium;nasopharynx;placenta;liver;testis;spleen;dura mater;kidney;brain;mammary gland;artery;aorta;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.05010 . 0.672386703 84.73696627 2257.00654 8.77857 CCDC148 7.95012569570602e-19 0.00102807677288018 0.99897192322712 coiled-coil domain containing 148 . . . unclassifiable (Anatomical System);prostate;ovary;placenta;colon;parathyroid;kidney;brain;bladder; dorsal root ganglion;superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion; 0.09452 . 1.001272896 90.72304789 362.85535 4.03426 CCDC148-AS1 . . . CCDC148 antisense RNA 1 . . . . . . . . . . . CCDC149 0.0020492844117992 0.977529377597412 0.0204213379907883 coiled-coil domain containing 149 . . . unclassifiable (Anatomical System);breast;prostate;islets of Langerhans;salivary gland;placenta;iris;pituitary gland; . 0.16007 0.09800 -0.47017169 23.25430526 5120.65553 14.70466 CCDC150 3.80375071750666e-24 0.00379212710594784 0.996207872894052 coiled-coil domain containing 150 . . . . . 0.18588 . 0.163497395 64.97405048 1965.24994 8.16962 CCDC150P1 . . . coiled-coil domain containing 150 pseudogene 1 . . . . . . . . . . . CCDC151 8.76721164897311e-07 0.917488336744698 0.0825107865341374 coiled-coil domain containing 151 FUNCTION: Ciliary protein involved in outer dynein arm assembly and required for motile cilia function. {ECO:0000250|UniProtKB:Q8BSN3}.; DISEASE: Ciliary dyskinesia, primary, 30 (CILD30) [MIM:616037]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia. Patients may exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:25192045, ECO:0000269|PubMed:25224326}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);prostate;lung;ovary;thyroid;visual apparatus;hippocampus;testis;parathyroid;brain; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.09897 . 0.821252311 88.01604152 273.66873 3.54459 CCDC152 . . . coiled-coil domain containing 152 . . TISSUE SPECIFICITY: Detected in stomach. {ECO:0000269|PubMed:15809229}.; ovary;skin;prostate;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;testis;middle ear;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;pia mater;adrenal gland;internal ear;placenta;head and neck;kidney;stomach;aorta; . . . 0.301449681 71.80938901 70.78554 1.75049 CCDC153 0.154452992851167 0.776290816747225 0.069256190401608 coiled-coil domain containing 153 . . . . . . . 0.705562627 85.52724699 1092.48742 6.32550 CCDC154 0.311572586421122 0.488540297616643 0.199887115962235 coiled-coil domain containing 154 . . . . . . . . . 1702.60076 7.60997 CCDC155 7.22301101921984e-07 0.896888585213909 0.103110692484989 coiled-coil domain containing 155 FUNCTION: May be involved in meiotic chromosome dynamics and homolog pairing. {ECO:0000250}.; . . . . . 0.07875 -0.176292081 40.56381222 104.6039 2.21065 CCDC157 2.42416018108272e-15 0.00437365914802161 0.995626340851976 coiled-coil domain containing 157 . . . lung;visual apparatus;testis;spleen; . . . 0.299418187 71.70323189 2243.61637 8.74185 CCDC158 2.98525360726236e-13 0.965155175621492 0.0348448243782093 coiled-coil domain containing 158 . . . unclassifiable (Anatomical System);uterus;lung;visual apparatus;liver;testis;blood; testis - interstitial;testis;atrioventricular node; . . 0.146913314 63.8240151 995.3777 6.08007 CCDC159 9.21303782326294e-05 0.789067712474308 0.210840157147459 coiled-coil domain containing 159 . . . . . . . -0.005381972 53.50908233 1295.60504 6.77483 CCDC160 0.0294628814590456 0.589016082019042 0.381521036521913 coiled-coil domain containing 160 . . . . . . . 0.014844891 54.94810097 18.55575 0.64287 CCDC162P . . . coiled-coil domain containing 162, pseudogene . . . . . 0.08175 . . . . . CCDC163P 0.143398568804261 0.778916284440675 0.0776851467550639 coiled-coil domain containing 163, pseudogene . . . . . . . . . 880.28921 5.77918 CCDC166 . . . coiled-coil domain containing 166 . . . . . . . . . 735.37074 5.38125 CCDC167 0.00208987937449307 0.508997907907258 0.488912212718249 coiled-coil domain containing 167 . . . . . 0.22412 . -0.119252484 44.53880632 13.15699 0.47914 CCDC168 . . . coiled-coil domain containing 168 . . . testis; . . . . . 2716.16143 9.81694 CCDC169 . . . coiled-coil domain containing 169 . . . placenta;testis;lens;peripheral nerve; . . . 0.880130671 88.9596603 521.70663 4.66288 CCDC169-SOHLH2 0.429898601119812 0.568591868544297 0.00150953033589015 CCDC169-SOHLH2 readthrough FUNCTION: Probable transcription factor, which may be involved in spermatogenesis and oogenesis. {ECO:0000250}.; . . . . . . 0.553050905 81.54635527 2513.73983 9.34343 CCDC170 1.02112361613873e-19 0.000591009260296174 0.999408990739704 coiled-coil domain containing 170 . . . . . 0.07510 0.07882 1.359517207 94.45034206 3619.70136 11.66494 CCDC171 . . . coiled-coil domain containing 171 . . . . . 0.17958 . -0.86731883 10.65699457 7618.40229 18.74684 CCDC172 0.00832961563746814 0.932327897959087 0.0593424864034446 coiled-coil domain containing 172 . . . . . 0.06787 . -0.05129383 49.75819769 13.05764 0.47518 CCDC173 1.08459309632037e-15 0.00524407533998449 0.994755924660014 coiled-coil domain containing 173 . . . . . . . 0.863528995 88.74144845 1239.36062 6.64676 CCDC174 2.94812141217999e-05 0.984591011891779 0.015379506894099 coiled-coil domain containing 174 . . . . . 0.05873 0.09792 0.090079492 60.64519934 270.85592 3.52855 CCDC175 . . . coiled-coil domain containing 175 . . . . . 0.05335 . 2.127703147 97.91224345 636.0595 5.07421 CCDC177 . . . coiled-coil domain containing 177 . . . . . . . . . 148.04706 2.65118 CCDC178 4.11143333531655e-29 4.48912376491766e-06 0.999995510876235 coiled-coil domain containing 178 . . . . . 0.71144 . 1.449540683 95.14626091 1397.05643 6.99037 CCDC179 . . . coiled-coil domain containing 179 . . . . . . . . . 3591.93724 11.60669 CCDC180 5.35201684379183e-22 0.851536030319716 0.148463969680284 coiled-coil domain containing 180 . . . . . 0.33974 0.08294 -0.134247113 43.77801368 3949.44499 12.44050 CCDC181 3.80247233403694e-07 0.802443205207209 0.197556414545557 coiled-coil domain containing 181 . . . . . 0.15761 0.09136 0.308721233 72.59966973 652.52705 5.12450 CCDC182 . . . coiled-coil domain containing 182 . . . . . . . . . 2817.6053 10.01290 CCDC183 . . . coiled-coil domain containing 183 . . . . . . . 2.645930833 98.82637414 246.05056 3.38435 CCDC183-AS1 . . . CCDC183 antisense RNA 1 . . . . . . . . . . . CCDC184 . . . coiled-coil domain containing 184 . . . . . . . 0.080983847 59.76055674 . . CCDC185 . . . coiled-coil domain containing 185 . . . . . 0.10351 0.10002 -0.134019284 43.90776126 . . CCDC186 . . . coiled-coil domain containing 186 . . . . . 0.11801 0.09559 -0.308569083 32.17150271 . . CCDC187 . . . coiled-coil domain containing 187 . . . . . . . . . . . CCDC188 . . . coiled-coil domain containing 188 . . . . . . . . . . . CCDC189 . . . coiled-coil domain containing 189 . . . . . . . -0.115612493 45.12856806 . . CCDC190 . . . coiled-coil domain containing 190 . . . . . 0.00869 . 0.52918614 80.81505072 . . CCDC191 . . . coiled-coil domain containing 191 . . . . . 0.04892 . 0.316000233 72.80018872 . . CCDC192 . . . coiled-coil domain containing 192 . . . . . . . . . . . CCEPR . . . cervical carcinoma expressed PCNA regulatory lncRNA . . . . . . . . . . . CCER1 4.84730770012203e-07 0.226603589969787 0.773395925299443 coiled-coil glutamate rich protein 1 . . . . . 0.28974 0.08537 0.084621747 60.31493277 302.41546 3.70367 CCER2 . . . coiled-coil glutamate rich protein 2 . . . . . . . . . 1702.25498 7.60741 CCHCR1 6.50103692455086e-08 0.998558309614817 0.00144162537481379 coiled-coil alpha-helical rod protein 1 FUNCTION: May be a regulator of keratinocyte proliferation or differentiation.; . TISSUE SPECIFICITY: Found in all tissues tested, abundantly expressed in heart, liver, skeletal muscle, kidney and pancreas, and to a lesser extent in lung and placenta. Overexpressed in keratinocytes of psoriatic lesions.; . . 0.08663 . 3.537641465 99.48690729 19252.75947 29.69105 CCIN 0.0104920413784341 0.83060338451077 0.158904574110795 calicin FUNCTION: Possible morphogenetic cytoskeletal element in spermiogenic differentiation.; . TISSUE SPECIFICITY: Testis. Not detectable or shows a drastically altered pattern of arrangement in the heads of malformed spermatozoa. {ECO:0000269|PubMed:7641791}.; unclassifiable (Anatomical System);medulla oblongata;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.54797 0.10575 0.047806932 57.51946214 696.52437 5.25730 CCK 0.0231054020414021 0.768016900774034 0.208877697184564 cholecystokinin FUNCTION: This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion.; . . unclassifiable (Anatomical System);ovary;hypothalamus;parathyroid;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;frontal lobe;placenta;macula lutea;visual apparatus;brain;stomach; whole brain;amygdala;occipital lobe;medulla oblongata;temporal lobe;pons;subthalamic nucleus;prostate;placenta;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.07500 0.19392 -0.031067188 51.03798066 31.7441 0.99985 CCKAR 0.0174084828953902 0.891371339905553 0.0912201771990565 cholecystokinin A receptor FUNCTION: Receptor for cholecystokinin. Mediates pancreatic growth and enzyme secretion, smooth muscle contraction of the gall bladder and stomach. Has a 1000-fold higher affinity for CCK rather than for gastrin. It modulates feeding and dopamine-induced behavior in the central and peripheral nervous system. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.; . . . . 0.40067 0.10427 -0.134019284 43.90776126 175.0724 2.87735 CCKBR 9.67009048154741e-05 0.939091766207358 0.0608115328878267 cholecystokinin B receptor FUNCTION: Receptor for gastrin and cholecystokinin. The CKK-B receptors occur throughout the central nervous system where they modulate anxiety, analgesia, arousal, and neuroleptic activity. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.; . TISSUE SPECIFICITY: Isoform 1 is expressed in brain, pancreas, stomach, the colon cancer cell line LoVo and the T-lymphoblastoma Jurkat, but not in heart, placenta, liver, lung, skeletal muscle, kidney or the stomach cancer cell line AGS. Expressed at high levels in the small cell lung cancer cell line NCI-H510, at lower levels in NCI-H345, NCI-H69 and GLC-28 cell lines, not expressed in GLC-19 cell line. Within the stomach, expressed at high levels in the mucosa of the gastric fundus and at low levels in the antrum and duodenum. Isoform 2 is present in pancreatic cancer cells and colorectal cancer cells, but not in normal pancreas or colonic mucosa. Isoform 3 is expressed in brain, pancreas, stomach, the stomach cancer cell line AGS and the colon cancer cell line LoVo. {ECO:0000269|PubMed:10913157, ECO:0000269|PubMed:12429993, ECO:0000269|PubMed:7848914, ECO:0000269|PubMed:7887934, ECO:0000269|PubMed:8185170, ECO:0000269|PubMed:8349705}.; unclassifiable (Anatomical System);optic nerve;lung;placenta;iris;brain; whole brain;superior cervical ganglion;medulla oblongata;cerebellum peduncles;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.44332 0.15553 -0.26993514 34.59542345 435.38052 4.35140 CCL1 0.0630408408804656 0.724805248227107 0.212153910892427 C-C motif chemokine ligand 1 FUNCTION: Cytokine that is chemotactic for monocytes but not for neutrophils. Binds to CCR8. {ECO:0000269|PubMed:1557400}.; . . lung; dorsal root ganglion;superior cervical ganglion;medulla oblongata;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.00673 . 0.125076652 62.7388535 25.99725 0.84472 CCL2 0.667686004742637 0.310184753154304 0.0221292421030591 C-C motif chemokine ligand 2 FUNCTION: Chemotactic factor that attracts monocytes and basophils but not neutrophils or eosinophils. Augments monocyte anti-tumor activity. Has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like psoriasis, rheumatoid arthritis or atherosclerosis. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis.; . . lymphoreticular;ovary;salivary gland;intestine;colon;substantia nigra;parathyroid;choroid;vein;skin;retina;uterus;prostate;whole body;bone;thyroid;iris;testis;amniotic fluid;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; smooth muscle;heart;fetal brain;spinal cord;beta cell islets;fetal lung;pons;trigeminal ganglion; 0.46084 0.88583 -0.09720619 46.20193442 2.53751 0.09405 CCL3 0.145338664435048 0.778548432668519 0.0761129028964324 C-C motif chemokine ligand 3 FUNCTION: Monokine with inflammatory and chemokinetic properties. Binds to CCR1, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-alpha induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). {ECO:0000269|PubMed:8525373}.; . . lymphoreticular;smooth muscle;ovary;colon;fovea centralis;choroid;retina;prostate;optic nerve;endometrium;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;pancreas;lung;adrenal gland;placenta;visual apparatus;macula lutea;liver;hypopharynx;spleen;head and neck; . 0.13680 0.67562 0.281220278 71.07808445 149.93525 2.66962 CCL3L1 . . . C-C motif chemokine ligand 3 like 1 FUNCTION: Chemotactic for lymphocytes and monocytes. Is a ligand for CCR1, CCR3 and CCR5. Is an inhibitor of HIV-1-infection. The processed form LD78-beta(3-70) shows a 20-fold to 30-fold higher chemotactic activity and is a very potent inhibitor of HIV-1- infection. LD78-beta(3-70) is also a ligand for CCR1, CCR3 and CCR5. {ECO:0000269|PubMed:10961862, ECO:0000269|PubMed:11449371}.; . . . . 0.19466 0.16866 . . 0.22671 0.00511 CCL3L3 . . . C-C motif chemokine ligand 3 like 3 FUNCTION: Chemotactic for lymphocytes and monocytes. Is a ligand for CCR1, CCR3 and CCR5. Is an inhibitor of HIV-1-infection. The processed form LD78-beta(3-70) shows a 20-fold to 30-fold higher chemotactic activity and is a very potent inhibitor of HIV-1- infection. LD78-beta(3-70) is also a ligand for CCR1, CCR3 and CCR5. {ECO:0000269|PubMed:10961862, ECO:0000269|PubMed:11449371}.; . . . . . 0.18422 . . . . CCL3P1 . . . C-C motif chemokine ligand 3 pseudogene 1 . . . . . . . . . . . CCL4 0.264898889441608 0.637475462255601 0.097625648302791 C-C motif chemokine ligand 4 FUNCTION: Monokine with inflammatory and chemokinetic properties. Binds to CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-beta induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form MIP-1-beta(3-69) retains the abilities to induce down-modulation of surface expression of the chemokine receptor CCR5 and to inhibit the CCR5- mediated entry of HIV-1 in T-cells. MIP-1-beta(3-69) is also a ligand for CCR1 and CCR2 isoform B. {ECO:0000269|PubMed:10540332, ECO:0000269|PubMed:12070155, ECO:0000269|PubMed:8525373}.; . . unclassifiable (Anatomical System);lymphoreticular;ovary;heart;colon;blood;skin;bone marrow;uterus;prostate;pancreas;lung;nasopharynx;placenta;liver;testis;spleen;kidney;brain;gall bladder; . 0.17903 0.37232 0.103030231 61.2762444 161.08883 2.77182 CCL4L1 0.480860804707283 0.437298365706403 0.0818408295863143 C-C motif chemokine ligand 4 like 1 FUNCTION: Chemokine that induces chemotaxis of cells expressing CCR5 or CCR1. Inhibits HIV replication in peripheral blood monocytes that express CCR5. {ECO:0000269|PubMed:15240137}.; . TISSUE SPECIFICITY: Detected in B-cells. {ECO:0000269|PubMed:14673550}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;ovary;salivary gland;intestine;pharynx;colon;blood;skin;bone marrow;breast;prostate;lung;nasopharynx;placenta;visual apparatus;liver;testis;spleen;kidney;brain;bladder;stomach; . . . . . 954.01982 5.97685 CCL4L2 0.489937310110051 0.432501897185011 0.0775607927049386 C-C motif chemokine ligand 4 like 2 FUNCTION: Chemokine that induces chemotaxis of cells expressing CCR5 or CCR1. Inhibits HIV replication in peripheral blood monocytes that express CCR5. {ECO:0000269|PubMed:15240137}.; . TISSUE SPECIFICITY: Detected in B-cells. {ECO:0000269|PubMed:14673550}.; unclassifiable (Anatomical System);lymphoreticular;lung;nasopharynx;placenta;testis;colon;blood;kidney;bone marrow; . . 0.11336 . . 14.06407 0.51075 CCL5 0.0129094216451699 0.657313117542928 0.329777460811902 C-C motif chemokine ligand 5 FUNCTION: Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. May activate several chemokine receptors including CCR1, CCR3, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant RANTES protein induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form RANTES(3-68) acts as a natural chemotaxis inhibitor and is a more potent inhibitor of HIV-1- infection. The second processed form RANTES(4-68) exhibits reduced chemotactic and HIV-suppressive activity compared with RANTES(1- 68) and RANTES(3-68) and is generated by an unidentified enzyme associated with monocytes and neutrophils (PubMed:16791620, PubMed:1380064, PubMed:8525373, PubMed:9516414, PubMed:15923218). May also be an agonist of the G protein-coupled receptor GPR75, stimulating inositol trisphosphate production and calcium mobilization through its activation. Together with GPR75, may play a role in neuron survival through activation of a downstream signaling pathway involving the PI3, Akt and MAP kinases. By activating GPR75 may also play a role in insulin secretion by islet cells (PubMed:23979485). {ECO:0000269|PubMed:1380064, ECO:0000269|PubMed:15923218, ECO:0000269|PubMed:16791620, ECO:0000269|PubMed:17001303, ECO:0000269|PubMed:23979485, ECO:0000269|PubMed:8525373, ECO:0000269|PubMed:9516414}.; . TISSUE SPECIFICITY: T-cell and macrophage specific.; lymphoreticular;ovary;skin;bone marrow;uterus;prostate;endometrium;bone;testis;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; lymph node;white blood cells;whole blood;bone marrow; 0.09052 0.46655 -0.119252484 44.53880632 . . CCL7 0.00926233756877491 0.587185596478407 0.403552065952818 C-C motif chemokine ligand 7 FUNCTION: Chemotactic factor that attracts monocytes and eosinophils, but not neutrophils. Augments monocyte anti-tumor activity. Also induces the release of gelatinase B. This protein can bind heparin. Binds to CCR1, CCR2 and CCR3.; . . unclassifiable (Anatomical System);lung;umbilical cord;placenta;blood;skin; smooth muscle;skeletal muscle; 0.05130 0.33622 -0.075159878 47.78839349 7.13351 0.26695 CCL8 0.052901133609649 0.698072658915254 0.249026207475096 C-C motif chemokine ligand 8 FUNCTION: Chemotactic factor that attracts monocytes, lymphocytes, basophils and eosinophils. May play a role in neoplasia and inflammatory host responses. This protein can bind heparin. The processed form MCP-2(6-76) does not show monocyte chemotactic activity, but inhibits the chemotactic effect most predominantly of CCL7, and also of CCL2 and CCL5 and CCL8. {ECO:0000269|PubMed:9558113}.; . TISSUE SPECIFICITY: Highest expression found in the small intestine and peripheral blood cells. Intermediate levels seen in the heart, placenta, lung, skeletal muscle, thymus, colon, ovary, spinal cord and pancreas. Low levels seen in the brain, liver, spleen and prostate.; unclassifiable (Anatomical System);heart;cartilage;colon;blood;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;endometrium;adrenal gland;bone;macula lutea;liver;kidney; trigeminal ganglion; 0.04606 0.20522 0.703746784 85.42108988 2276.82551 8.82745 CCL11 0.0830410038618592 0.757779173551822 0.159179822586319 C-C motif chemokine ligand 11 FUNCTION: In response to the presence of allergens, this protein directly promotes the accumulation of eosinophils, a prominent feature of allergic inflammatory reactions. Binds to CCR3.; . . unclassifiable (Anatomical System);uterus;smooth muscle;heart;islets of Langerhans;kidney; superior cervical ganglion;appendix;trigeminal ganglion;skeletal muscle; 0.01450 0.26580 0.3032669 72.009908 68.14667 1.70751 CCL13 0.0511332837068313 0.692469160775261 0.256397555517908 C-C motif chemokine ligand 13 FUNCTION: Chemotactic factor that attracts monocytes, lymphocytes, basophils and eosinophils, but not neutrophils. Signals through CCR2B and CCR3 receptors. Plays a role in the accumulation of leukocytes at both sides of allergic and non-allergic inflammation. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis. May play a role in the monocyte attraction in tissues chronically exposed to exogenous pathogens.; . TISSUE SPECIFICITY: Widely expressed. Found in small intestine, thymus, colon, lung, trachea, stomach and lymph node. Low levels seen in the pulmonary artery smooth muscle cells.; unclassifiable (Anatomical System);lung;whole body;islets of Langerhans;bone;placenta;colon;brain; superior cervical ganglion;appendix; 0.02243 0.27560 0.369407109 74.95281906 16.91842 0.59600 CCL14 0.000121911835168333 0.38813862124219 0.611739466922642 C-C motif chemokine ligand 14 FUNCTION: Has weak activities on human monocytes and acts via receptors that also recognize MIP-1 alpha. It induced intracellular Ca(2+) changes and enzyme release, but no chemotaxis, at concentrations of 100-1,000 nM, and was inactive on T-lymphocytes, neutrophils, and eosinophil leukocytes. Enhances the proliferation of CD34 myeloid progenitor cells. The processed form HCC-1(9-74) is a chemotactic factor that attracts monocytes eosinophils, and T-cells and is a ligand for CCR1, CCR3 and CCR5. {ECO:0000269|PubMed:11085751}.; . TISSUE SPECIFICITY: Expressed constitutively in several normal tissues: spleen, liver, skeletal and heart muscle, gut, and bone marrow, present at high concentrations (1-80 nM) in plasma. {ECO:0000269|PubMed:9600961}.; . . 0.07779 0.19298 0.569646743 81.88841708 324.12689 3.82679 CCL15 0.0767077045897299 0.74957528628812 0.17371700912215 C-C motif chemokine ligand 15 FUNCTION: Chemotactic factor that attracts T-cells and monocytes, but not neutrophils, eosinophils, or B-cells. Acts mainly via CC chemokine receptor CCR1. Also binds to CCR3. CCL15(22-92), CCL15(25-92) and CCL15(29-92) are more potent chemoattractants than the small-inducible cytokine A15. {ECO:0000269|PubMed:15905581}.; . TISSUE SPECIFICITY: Most abundant in heart, skeletal muscle and adrenal gland. Lower levels in placenta, liver, pancreas and bone marrow. CCL15(22-92), CCL15(25-92) and CCL15(29-92) are found in high levels in synovial fluids from rheumatoid patients. {ECO:0000269|PubMed:15905581, ECO:0000269|PubMed:9558365}.; unclassifiable (Anatomical System);myocardium;heart;colon;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;pancreas;prostate;optic nerve;lung;thyroid;macula lutea;liver;testis;spleen;kidney;brain;stomach;gall bladder; liver;atrioventricular node; 0.03343 0.07496 0.347360312 73.97381458 9.24127 0.33838 CCL15-CCL14 . . . CCL15-CCL14 readthrough (NMD candidate) . . . . . . . . . . . CCL16 0.092061459649855 0.766697386061325 0.14124115428882 C-C motif chemokine ligand 16 FUNCTION: Shows chemotactic activity for lymphocytes and monocytes but not neutrophils. Also shows potent myelosuppressive activity, suppresses proliferation of myeloid progenitor cells. Recombinant SCYA16 shows chemotactic activity for monocytes and THP-1 monocytes, but not for resting lymphocytes and neutrophils. Induces a calcium flux in THP-1 cells that were desensitized by prior expression to RANTES.; . TISSUE SPECIFICITY: Mainly expressed in liver, also found in spleen and thymus. Highly expressed in LPS- and IFN-gamma- activated monocytes, weakly in some lymphocytes, including natural killer cells, gamma-delta T-cells, and some T-cell clones.; liver;blood; superior cervical ganglion;skeletal muscle; 0.12867 . 0.347360312 73.97381458 89.54694 2.03543 CCL17 0.0771247220885551 0.750171305818859 0.172703972092586 C-C motif chemokine ligand 17 FUNCTION: Chemotactic factor for T-lymphocytes but not monocytes or granulocytes. May play a role in T-cell development in thymus and in trafficking and activation of mature T-cells. Binds to CCR4. {ECO:0000269|PubMed:10540332}.; . TISSUE SPECIFICITY: Expressed at high levels in thymus and at low levels in the lung, colon and small intestine.; . . 0.07999 0.23927 0.435547893 77.45340882 88.10776 2.00925 CCL18 0.0103066152116527 0.609939405108249 0.379753979680099 C-C motif chemokine ligand 18 FUNCTION: Chemotactic factor that attracts lymphocytes but not monocytes or granulocytes. May be involved in B-cell migration into B-cell follicles in lymph nodes. Attracts naive T-lymphocytes toward dendritic cells and activated macrophages in lymph nodes, has chemotactic activity for naive T-cells, CD4+ and CD8+ T-cells and thus may play a role in both humoral and cell-mediated immunity responses. {ECO:0000269|PubMed:11745396, ECO:0000269|PubMed:11978786}.; . TISSUE SPECIFICITY: Expressed at high levels in lung, lymph nodes, placenta, bone marrow, dendritic cells present in germinal centers and T-cell areas of secondary lymphoid organs and macrophages derived from peripheral blood monocytes. Not expressed by peripheral blood monocytes and a monocyte-to-macrophage differentiation is a prerequisite for expression. Expressed in synovial fluids from patients with rheumatoid and septic arthritis and in ovarian carcinoma ascitic fluid. {ECO:0000269|PubMed:11745396}.; unclassifiable (Anatomical System);uterus;lung;cartilage;heart;epididymis;bone;placenta;colon;mammary gland;skin;aorta; superior cervical ganglion;uterus corpus;lymph node;tonsil;thymus; 0.06696 0.28090 0.191216164 66.57230479 2.13212 0.07119 CCL19 0.317197583093149 0.61401058627786 0.0687918306289909 C-C motif chemokine ligand 19 FUNCTION: May play a role not only in inflammatory and immunological responses but also in normal lymphocyte recirculation and homing. May play an important role in trafficking of T-cells in thymus, and T-cell and B-cell migration to secondary lymphoid organs. Binds to chemokine receptor CCR7. Recombinant CCL19 shows potent chemotactic activity for T-cells and B-cells but not for granulocytes and monocytes. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4. {ECO:0000269|PubMed:9498785}.; . TISSUE SPECIFICITY: Expressed at high levels in the lymph nodes, thymus and appendix. Intermediate levels seen in colon and trachea, while low levels found in spleen, small intestine, lung, kidney and stomach.; unclassifiable (Anatomical System);cartilage;heart;hypothalamus;colon;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;lung;nasopharynx;macula lutea;liver;spleen;mammary gland;aorta;stomach;thymus; lymph node;trigeminal ganglion;tonsil;thymus; 0.03996 0.22494 0.057118534 57.99716914 3.51808 0.12845 CCL20 0.0877400024034262 0.762794062615112 0.149465934981462 C-C motif chemokine ligand 20 FUNCTION: Chemotactic factor that attracts lymphocytes and, slightly, neutrophils, but not monocytes. Inhibits proliferation of myeloid progenitors in colony formation assays. May be involved in formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. Possesses antibacterial activity E.coli ATCC 25922 and S.aureus ATCC 29213. {ECO:0000269|PubMed:12149255}.; . TISSUE SPECIFICITY: Expressed predominantly in the liver, lymph nodes, appendix, peripheral blood lymphocytes, and fetal lung. Low levels seen in thymus, prostate, testis, small intestine and colon.; unclassifiable (Anatomical System);colon;blood;uterus;lung;oesophagus;larynx;nasopharynx;head and neck;kidney;tonsil;stomach;gall bladder; superior cervical ganglion;fetal lung;trigeminal ganglion;tonsil; 0.28191 0.20693 0.301449681 71.80938901 6.54338 0.24223 CCL21 0.110386513859901 0.777135371830923 0.112478114309176 C-C motif chemokine ligand 21 FUNCTION: Inhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, macrophages, or neutrophils. Shows preferential activity towards naive T-cells. May play a role in mediating homing of lymphocytes to secondary lymphoid organs. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4.; . TISSUE SPECIFICITY: Highly expressed in high endothelial venules of lymph nodes, spleen and appendix. Intermediate levels found in small intestine, thyroid gland and trachea. Low level expression in thymus, bone marrow, liver, and pancreas. Also found in tonsil, fetal heart and fetal spleen.; myocardium;ovary;colon;parathyroid;choroid;skin;uterus;prostate;whole body;endometrium;thyroid;testis;unclassifiable (Anatomical System);lymph node;heart;skeletal muscle;pancreas;lung;nasopharynx;placenta;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;lymph node;appendix;pons;fetal thyroid;tonsil;skeletal muscle; 0.04483 0.59766 -0.075159878 47.78839349 3.70221 0.13807 CCL22 0.279053454796883 0.632175412424466 0.0887711327786513 C-C motif chemokine ligand 22 FUNCTION: May play a role in the trafficking of activated/effector T-lymphocytes to inflammatory sites and other aspects of activated T-lymphocyte physiology. Chemotactic for monocytes, dendritic cells and natural killer cells. Mild chemoattractant for primary activated T-lymphocytes and a potent chemoattractant for chronically activated T-lymphocytes but has no chemoattractant activity for neutrophils, eosinophils, and resting T-lymphocytes. Binds to CCR4. Processed forms MDC(3-69), MDC(5-69) and MDC(7-69) seem not be active.; . TISSUE SPECIFICITY: Highly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. Also found in lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression in lung and spleen. Very weak expression in small intestine. In lymph node expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+). Expressed in Langerhans' cell histiocytosis but not in dermatopathic lymphadenopathy. Expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. {ECO:0000269|PubMed:11241286}.; unclassifiable (Anatomical System);lung;lacrimal gland;nasopharynx;bone;blood; dorsal root ganglion;placenta;ciliary ganglion; 0.10070 . 0.260991686 70.25831564 23.03791 0.76878 CCL23 0.0428120139562607 0.847630333810678 0.109557652233062 C-C motif chemokine ligand 23 FUNCTION: Shows chemotactic activity for monocytes, resting T- lymphocytes, and neutrophils, but not for activated lymphocytes. Inhibits proliferation of myeloid progenitor cells in colony formation assays. This protein can bind heparin. Binds CCR1. CCL23(19-99), CCL23(22-99), CCL23(27-99), CCL23(30-99) are more potent chemoattractants than the small-inducible cytokine A23. {ECO:0000269|PubMed:15905581}.; . TISSUE SPECIFICITY: High levels in adult lung, liver, skeletal muscle and pancreas. Moderate levels in fetal liver, adult bone marrow and placenta. The short form is the major species and the longer form was detected only in very low abundance. CCL23(19-99), CCL23(22-99), CCL23(27-99), CCL23(30-99) are found in high levels in synovial fluids from rheumatoid patients. {ECO:0000269|PubMed:15905581}.; unclassifiable (Anatomical System);uterus;lung;heart;skin; superior cervical ganglion;globus pallidus;ciliary ganglion; 0.08846 0.06651 0.281220278 71.07808445 5.68144 0.21321 CCL24 0.0171892202994171 0.714729600133307 0.268081179567276 C-C motif chemokine ligand 24 FUNCTION: Chemotactic for resting T-lymphocytes, and eosinophils. Has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. Is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line. Binds to CCR3.; . TISSUE SPECIFICITY: Activated monocytes and activated T lymphocytes.; liver; testis - interstitial;skeletal muscle; 0.05755 0.18806 0.902179145 89.34890304 714.34001 5.30751 CCL25 0.169939684464423 0.770730906819447 0.0593294087161307 C-C motif chemokine ligand 25 FUNCTION: Potentially involved in T-cell development. Recombinant protein shows chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritics cells but is inactive on peripheral blood lymphocytes and neutrophils. Binds to CCR9. Isoform 2 is an antagonist of isoform 1. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4.; . TISSUE SPECIFICITY: Specifically expressed by thymic dendritic cells. High levels in thymus and small intestine.; lung;ovary;placenta;parathyroid;thymus; superior cervical ganglion;trigeminal ganglion;thymus; 0.06236 0.19432 1.038098315 91.20665251 298.57445 3.68495 CCL26 0.019786154155303 0.741022043054371 0.239191802790326 C-C motif chemokine ligand 26 FUNCTION: Chemotactic for eosinophils and basophils. Binds to CCR3.; . TISSUE SPECIFICITY: Ubiquitously expressed at low levels in various tissues including heart and ovary.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;placenta;macula lutea;kidney; . 0.21312 0.21728 0.523736627 80.45529606 53.60407 1.45724 CCL27 0.0168894105374168 0.711337679043763 0.27177291041882 C-C motif chemokine ligand 27 FUNCTION: Chemotactic factor that attracts skin-associated memory T-lymphocytes. May play a role in mediating homing of lymphocytes to cutaneous sites. Binds to CCR10.; . TISSUE SPECIFICITY: Testis, thymus, placenta, ovary and skin.; unclassifiable (Anatomical System);heart;ovary;parathyroid;fovea centralis;choroid;lens;retina;uterus;optic nerve;whole body;lung;placenta;macula lutea;testis;brain; skin; 0.16201 0.26402 0.347360312 73.97381458 361.8243 4.02583 CCL28 0.281065700553635 0.631352570601271 0.0875817288450943 C-C motif chemokine ligand 28 FUNCTION: Chemotactic activity for resting CD4, CD8 T-cells and eosinophils. Binds to CCR3 and CCR10 and induces calcium mobilization in a dose-dependent manner.; . TISSUE SPECIFICITY: Preferentially expressed by epithelial cells of diverse tissues including normal and pathological colon, salivary gland, mammary gland, trachea and rectum. Also found in prostate, spleen, thyroid, psoriasis skin and in lower levels in peripheral blood leukocytes, small intestine, Peyer patches, stomach and normal skin.; breast;skeletal muscle; . 0.14929 0.10163 0.25917371 70.05779665 27.97723 0.89818 CCM2 0.483088350953085 0.515904176926862 0.00100747212005355 CCM2 scaffolding protein FUNCTION: Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions (By similarity). May function as a scaffold protein for MAP2K3-MAP3K3 signaling. Seems to play a major role in the modulation of MAP3K3- dependent p38 activation induced by hyperosmotic shock (By similarity). {ECO:0000250}.; DISEASE: Cerebral cavernous malformations 2 (CCM2) [MIM:603284]: A congenital vascular anomaly of the central nervous system that can result in hemorrhagic stroke, seizures, recurrent headaches, and focal neurologic deficits. The lesions are characterized by grossly enlarged blood vessels consisting of a single layer of endothelium and without any intervening neural tissue, ranging in diameter from a few millimeters to several centimeters. {ECO:0000269|PubMed:14624391, ECO:0000269|PubMed:14740320, ECO:0000269|PubMed:22415356}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;urinary;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;oesophagus;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;thymus; medulla oblongata;subthalamic nucleus;temporal lobe;globus pallidus;caudate nucleus;pons;cingulate cortex;parietal lobe; 0.17979 0.11593 -0.376526807 28.10804435 1216.01154 6.59576 CCM2L 0.00053799849805507 0.888920588001051 0.110541413500894 CCM2 like scaffolding protein . . . . . 0.74290 . . . 204.38511 3.08827 CCNA1 0.00990629608655128 0.987912428056168 0.00218127585728107 cyclin A1 FUNCTION: May be involved in the control of the cell cycle at the G1/S (start) and G2/M (mitosis) transitions. May primarily function in the control of the germline meiotic cell cycle and additionally in the control of mitotic cell cycle in some somatic cells. {ECO:0000269|PubMed:10022926}.; . TISSUE SPECIFICITY: Very high levels in testis and very low levels in brain. Also found in myeloid leukemia cell lines.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;retina;bone marrow;uterus;pancreas;optic nerve;lung;placenta;macula lutea;alveolus;testis;spleen;brain;peripheral nerve; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion; 0.73655 0.38561 -0.492218069 22.35786742 39.03162 1.15697 CCNA2 0.994683049578133 0.00531632710112679 6.23320740343355e-07 cyclin A2 FUNCTION: Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.; . . sympathetic chain;colon;fovea centralis;skin;uterus;prostate;whole body;endometrium;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;fetal liver;tumor;trigeminal ganglion; 0.99861 0.52166 0.371224249 75.12384996 53.82847 1.46252 CCNB1 0.0239694449209668 0.961989361561136 0.0140411935178973 cyclin B1 FUNCTION: Essential for the control of the cell cycle at the G2/M (mitosis) transition. {ECO:0000269|PubMed:17495531, ECO:0000269|PubMed:17495533}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;vein;skin;uterus;prostate;endometrium;larynx;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; fetal liver;testis;trigeminal ganglion; 0.99904 0.10188 -0.183570861 39.95046001 51.03958 1.40783 CCNB1IP1 0.183416412334859 0.804635076058632 0.011948511606509 cyclin B1 interacting protein 1, E3 ubiquitin protein ligase FUNCTION: Ubiquitin E3 ligase that acts as a limiting factor for crossing-over during meiosis: required during zygonema to limit the colocalization of RNF212 with MutS-gamma-associated recombination sites and thereby establish early differentiation of crossover and non-crossover sites. Later, it is directed by MutL- gamma to stably accumulate at designated crossover sites. Probably promotes the dissociation of RNF212 and MutS-gamma to allow the progression of recombination and the implementation of the final steps of crossing over (By similarity). Modulates cyclin-B levels and participates in the regulation of cell cycle progression through the G2 phase. Overexpression causes delayed entry into mitosis. {ECO:0000250, ECO:0000269|PubMed:12612082, ECO:0000269|PubMed:17297447}.; . TISSUE SPECIFICITY: Highly expressed in heart. Detected at intermediate levels in liver and kidney, and at low levels in placenta, brain and lung. {ECO:0000269|PubMed:12612082}.; ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;trophoblast;lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;breast;pia mater;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;tumor;skeletal muscle; 0.12977 0.11280 -0.159704656 41.90846898 57.96636 1.53907 CCNB1IP1P1 . . . cyclin B1 interacting protein 1 pseudogene 1 . . . . . . . . . . . CCNB1IP1P2 . . . cyclin B1 interacting protein 1 pseudogene 2 . . . . . . . . . . . CCNB1IP1P3 . . . cyclin B1 interacting protein 1 pseudogene 3 . . . . . . . . . . . CCNB2 1.58542348538884e-06 0.85381063456478 0.146187780011735 cyclin B2 FUNCTION: Essential for the control of the cell cycle at the G2/M (mitosis) transition.; . . medulla oblongata;smooth muscle;ovary;salivary gland;developmental;intestine;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;tumor; 0.86851 0.17715 0.130533008 63.35810333 135.61225 2.53261 CCNB2P1 . . . cyclin B2 pseudogene 1 . . . . . . . . . . . CCNB3 0.57088694342555 0.429010708227065 0.000102348347385454 cyclin B3 FUNCTION: Cyclins are positive regulatory subunits of the cyclin- dependent kinases (CDKs), and thereby play an essential role in the control of the cell cycle, notably via their destruction during cell division. Its tissue specificity suggest that it may be required during early meiotic prophase I. {ECO:0000269|PubMed:12185076}.; . TISSUE SPECIFICITY: Testis specific. In testis, it is expressed in developing germ cells, but not in Leydig cells. Weakly or not expressed in other tissues. {ECO:0000269|PubMed:11846420, ECO:0000269|PubMed:12185076}.; unclassifiable (Anatomical System);lung;placenta;bone;pituitary gland;testis;skeletal muscle; superior cervical ganglion;atrioventricular node; 0.14946 . -0.440847477 24.59896202 69.04476 1.72168 CCNB3P1 . . . cyclin B3 pseudogene 1 . . . . . . . . . . . CCNC 0.990104533528106 0.00989261853409757 2.84793779676472e-06 cyclin C FUNCTION: Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Binds to and activates cyclin-dependent kinase CDK8 that phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex. {ECO:0000269|PubMed:16595664, ECO:0000269|PubMed:8700522}.; . TISSUE SPECIFICITY: Highest levels in pancreas. High levels in heart, liver, skeletal muscle and kidney. Low levels in brain.; myocardium;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;tonsil;gall bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;bile duct;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;trachea;thyroid; 0.95079 0.19444 -0.09720619 46.20193442 1.05127 0.02651 CCND1 0.238186361767522 0.729821021286137 0.031992616946341 cyclin D1 FUNCTION: Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner. {ECO:0000269|PubMed:15241418, ECO:0000269|PubMed:16569215, ECO:0000269|PubMed:18417529, ECO:0000269|PubMed:9106657}.; DISEASE: Note=A chromosomal aberration involving CCND1 may be a cause of B-lymphocytic malignancy, particularly mantle-cell lymphoma (MCL). Translocation t(11;14)(q13;q32) with immunoglobulin gene regions. Activation of CCND1 may be oncogenic by directly altering progression through the cell cycle.; DISEASE: Note=A chromosomal aberration involving CCND1 may be a cause of parathyroid adenomas. Translocation t(11;11)(q13;p15) with the parathyroid hormone (PTH) enhancer.; DISEASE: Multiple myeloma (MM) [MIM:254500]: A malignant tumor of plasma cells usually arising in the bone marrow and characterized by diffuse involvement of the skeletal system, hyperglobulinemia, Bence-Jones proteinuria and anemia. Complications of multiple myeloma are bone pain, hypercalcemia, renal failure and spinal cord compression. The aberrant antibodies that are produced lead to impaired humoral immunity and patients have a high prevalence of infection. Amyloidosis may develop in some patients. Multiple myeloma is part of a spectrum of diseases ranging from monoclonal gammopathy of unknown significance (MGUS) to plasma cell leukemia. {ECO:0000269|PubMed:8695815}. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving CCND1 is found in multiple myeloma. Translocation t(11;14)(q13;q32) with the IgH locus.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;iris;testis;amniotic fluid;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; pons; 0.99915 0.96333 -0.317668748 31.45789101 11.551 0.41759 CCND2 0.949000818432094 0.0508360622522926 0.000163119315613716 cyclin D2 FUNCTION: Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D2/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity). {ECO:0000250}.; DISEASE: Megalencephaly-polymicrogyria-polydactyly-hydrocephalus syndrome 3 (MPPH3) [MIM:615938]: A syndrome characterized by megalencephaly, ventriculomegaly that may lead to hydrocephalus, and polymicrogyria; polydactyly may also be seen. There is considerable phenotypic similarity between this disorder and the megalencephaly-capillary malformation syndrome. {ECO:0000269|PubMed:24705253}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;colon;choroid;fovea centralis;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;stomach;thymus;cerebellum; superior cervical ganglion;lung;adrenal gland; 0.93215 0.74954 -0.185391282 39.67916962 14.77663 0.53228 CCND2-AS1 . . . CCND2 antisense RNA 1 . . . . . . . . . . . CCND2-AS2 . . . CCND2 antisense RNA 2 . . . . . . . . . . . CCND2P1 . . . cyclin D2 pseudogene 1 . . . . . . . . . . . CCND3 0.946445162222962 0.0533704831142814 0.000184354662756259 cyclin D3 FUNCTION: Regulatory component of the cyclin D3-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D3/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. {ECO:0000269|PubMed:15358120}.; . . . . 0.88302 0.46749 0.371224249 75.12384996 112.94478 2.31269 CCND3P1 . . . cyclin D3 pseudogene 1 . . . . . . . . . . . CCND3P2 . . . cyclin D3 pseudogene 2 . . . . . . . . . . . CCNDBP1 0.0372725464260417 0.955401873178609 0.00732558039534942 cyclin D-type binding-protein 1 FUNCTION: May negatively regulate cell cycle progression. May act at least in part via inhibition of the cyclin-D1/CDK4 complex, thereby preventing phosphorylation of RB1 and blocking E2F- dependent transcription. {ECO:0000269|PubMed:10801854}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Expression is down- regulated in a variety of tumor types including breast, colon, prostate and rectal tumors, and is up-regulated in certain hepatic carcinomas. {ECO:0000269|PubMed:10801854, ECO:0000269|PubMed:10854051, ECO:0000269|PubMed:10915743, ECO:0000269|PubMed:15887118, ECO:0000269|PubMed:17131381}.; ovary;skin;retina;bone marrow;prostate;optic nerve;ganglion;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; placenta;bone marrow; 0.04519 0.10800 -0.381986487 27.68931352 82.27639 1.92542 CCNE1 0.268926805475888 0.729972267035969 0.00110092748814332 cyclin E1 FUNCTION: Essential for the control of the cell cycle at the G1/S (start) transition. {ECO:0000269|PubMed:7739542}.; . TISSUE SPECIFICITY: Highly expressed in testis and placenta. Low levels in bronchial epithelial cells. {ECO:0000269|PubMed:9840943}.; unclassifiable (Anatomical System);cartilage;ovary;heart;salivary gland;intestine;pharynx;colon;blood;skin;retina;breast;prostate;lung;endometrium;placenta;visual apparatus;hypopharynx;duodenum;liver;testis;cervix;head and neck;kidney;brain;bladder;stomach; testis - seminiferous tubule;placenta;testis; 0.99976 0.28689 -0.359940251 28.93371078 38.51875 1.14221 CCNE2 0.338179975892655 0.661197446183618 0.000622577923726904 cyclin E2 FUNCTION: Essential for the control of the cell cycle at the late G1 and early S phase.; . TISSUE SPECIFICITY: According to PubMed:9858585, highest levels of expression in adult testis, thymus and brain. Lower levels in placenta, spleen and colon. Consistently elevated levels in tumor- derived cells compared to non-transformed proliferating cells. According to PubMed:9840927: low levels in thymus, prostate, brain, skeletal muscle, and kidney. Elevated levels in lung. According to PubMed:9840943 highly expressed in testis, placenta, thymus and brain. In a lesser extent in small intestine and colon.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;urinary;skeletal muscle;breast;lung;placenta;liver;cervix;kidney;stomach;aorta; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.99576 0.16847 -0.005381972 53.50908233 124.43094 2.42611 CCNF 0.0243519280324674 0.975624260509877 2.38114576550844e-05 cyclin F FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of CP110 during G2 phase, thereby acting as an inhibitor of centrosome reduplication. {ECO:0000269|PubMed:20596027}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:7813445}.; lymphoreticular;ovary;developmental;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.57237 0.13128 -1.216154 5.667610285 136.16697 2.53540 CCNG1 0.359162745208338 0.628510736179381 0.012326518612281 cyclin G1 FUNCTION: May play a role in growth regulation. Is associated with G2/M phase arrest in response to DNA damage. May be an intermediate by which p53 mediates its role as an inhibitor of cellular proliferation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: High levels in skeletal muscle, ovary, kidney and colon.; ovary;salivary gland;sympathetic chain;developmental;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;aorta;stomach;thymus; adipose tissue;tumor;skeletal muscle; 0.64795 0.21581 -0.005381972 53.50908233 170.05268 2.84559 CCNG1P1 . . . cyclin G1 pseudogene 1 . . . . . . . . . . . CCNG2 0.893204360024237 0.106577124925159 0.000218515050603852 cyclin G2 FUNCTION: May play a role in growth regulation and in negative regulation of cell cycle progession.; . TISSUE SPECIFICITY: High levels in cerebellum, thymus, spleen and prostate. Low levels in skeletal muscle.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;atrioventricular node;prostate;subthalamic nucleus;fetal brain;thyroid;ciliary ganglion;kidney;whole blood;trigeminal ganglion;cerebellum; 0.33256 0.14909 0.238945317 69.20853975 89.33315 2.03153 CCNG2P1 . . . cyclin G2 pseudogene 1 . . . . . . . . . . . CCNH 0.00472976282475442 0.965781501976408 0.0294887351988374 cyclin H FUNCTION: Regulates CDK7, the catalytic subunit of the CDK- activating kinase (CAK) enzymatic complex. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II. Its expression and activity are constant throughout the cell cycle. {ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:7533895}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;pituitary gland;testis;dura mater;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);meninges;lacrimal gland;cerebellum cortex;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;visual apparatus;alveolus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; amygdala;superior cervical ganglion;occipital lobe;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;parietal lobe;skeletal muscle;cingulate cortex; 0.68027 0.13330 0.106667882 61.73036093 1653.808 7.51621 CCNHP1 . . . cyclin H pseudogene 1 . . . . . . . . . . . CCNI 0.789094042870787 0.209550824504691 0.00135513262452277 cyclin I . . TISSUE SPECIFICITY: Highest levels in adult heart, brain and skeletal muscle. Lower levels in adult placenta, lung, kidney and pancreas. Also high levels in fetal brain and lower levels in fetal lung, liver and kidney. Also abundant in testis and thyroid. {ECO:0000269|PubMed:7493655}.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;breast;pancreas;lung;cornea;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;aorta;stomach;peripheral nerve; whole brain;medulla oblongata;occipital lobe;subthalamic nucleus;fetal brain;cerebellum peduncles;thyroid;temporal lobe;prefrontal cortex;globus pallidus;pons;parietal lobe;cingulate cortex;cerebellum; 0.26347 0.16383 0.104848986 61.49445624 48.69159 1.36080 CCNI2 4.53255419093452e-05 0.410970357685402 0.588984316772689 cyclin I family member 2 . . . . . 0.09740 . . . 875.71216 5.75822 CCNJ 0.983940395518084 0.0160502640871064 9.34039480971696e-06 cyclin J . . . unclassifiable (Anatomical System);ovary;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;breast;uterus;optic nerve;lung;placenta;macula lutea;liver;testis;head and neck;spleen;germinal center;kidney;brain;tonsil;stomach;thymus; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.51792 . -0.383807564 27.41802312 21.42364 0.72290 CCNJL 1.94749657136305e-05 0.463291682837118 0.536688842197169 cyclin J like . . . unclassifiable (Anatomical System);trophoblast;heart;ovary;colon;parathyroid;fovea centralis;choroid;lens;retina;breast;optic nerve;lung;placenta;macula lutea;liver;testis;spleen;kidney;brain; superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node;skeletal muscle; 0.17277 . 0.154398214 64.73814579 1120.91099 6.39175 CCNJP1 . . . cyclin J pseudogene 1 . . . . . . . . . . . CCNJP2 . . . cyclin J pseudogene 2 . . . . . . . . . . . CCNK 0.997144332155116 0.00285553117277432 1.36672109151816e-07 cyclin K FUNCTION: Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A). {ECO:0000269|PubMed:10574912, ECO:0000269|PubMed:22012619, ECO:0000269|PubMed:9632813}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highest levels in testis. {ECO:0000269|PubMed:9632813}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;pharynx;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion; 0.88116 0.11977 -0.361761279 28.6329323 38.13805 1.13298 CCNL1 0.942872593157657 0.0571255946037204 1.81223862243254e-06 cyclin L1 FUNCTION: Transcriptional regulator which participates in regulating the pre-mRNA splicing process. Seems to be involved in the regulation of RNA polymerase II (pol II). Functions in association with cyclin-dependent kinases (CDKs) and has a role in the second step of splicing. May be a candidate proto-oncogene in head and neck squamous cell carcinomas (HNSCC). Inhibited by the CDK-specific inhibitor p21. {ECO:0000269|PubMed:11980906, ECO:0000269|PubMed:12414649, ECO:0000269|PubMed:15700036}.; . TISSUE SPECIFICITY: Ubiquitous with higher level in thymus. Overexpression in primary tumors of head and neck squamous cell carcinomas (HNSCC). {ECO:0000269|PubMed:11980906, ECO:0000269|PubMed:12414649, ECO:0000269|PubMed:15700036}.; lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;brain;bladder;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta; superior cervical ganglion;ciliary ganglion;white blood cells; 0.46646 0.08191 -0.449946534 24.00330267 17.56611 0.61566 CCNL2 0.104548195351159 0.895164135963453 0.000287668685387911 cyclin L2 FUNCTION: Transcriptional regulator which participates in regulating the pre-mRNA splicing process. Also modulates the expression of critical apoptotic factor, leading to cell apoptosis. {ECO:0000269|PubMed:14684736}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with a higher expression level observed in ovary, heart, liver and pancreas. {ECO:0000269|PubMed:14684736}.; . . . 0.10669 7.61E-05 53.98089172 763.45124 5.47580 CCNL2P1 . . . cyclin L2 pseudogene 1 . . . . . . . . . . . CCNO 0.0407101250551045 0.84306051074313 0.116229364201765 cyclin O FUNCTION: Specifically required for generation of multiciliated cells, possibly by promoting a cell cycle state compatible with centriole amplification and maturation. Acts downstream of MCIDAS to promote mother centriole amplification and maturation in preparation for apical docking. {ECO:0000269|PubMed:24747639}.; DISEASE: Ciliary dyskinesia, primary, 29 (CILD29) [MIM:615872]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia. CILD29 patients do not exhibit situs inversus, a congenital abnormality in which visceral organs are opposite to their normal positions (situs solitus) due to lateral transposition. {ECO:0000269|PubMed:24747639}. Note=The disease is caused by mutations affecting the gene represented in this entry. Marked reduction of cilia in multiciliate cells due to defective mother centriole generation and placement. Remaining cilia correctly express axonemal motor proteins, are motile and do not show beating defects. Defects are probably caused by a strong reduction in the number of multiple motile cilia covering the cell surface in respiratory epithelial cells (PubMed:24747639). {ECO:0000269|PubMed:24747639}.; TISSUE SPECIFICITY: Present in respiratory cells (at protein level). {ECO:0000269|PubMed:24747639}.; unclassifiable (Anatomical System);medulla oblongata;lung;ovary;endometrium;bone;liver;testis;colon;cervix;kidney;brain;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis;atrioventricular node;skeletal muscle; 0.08032 0.19498 0.483275131 79.25218212 97.40203 2.13267 CCNT1 0.995809373034455 0.00419055643477364 7.05307713469696e-08 cyclin T1 FUNCTION: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) complex, also called positive transcription elongation factor B (P-TEFb), which is proposed to facilitate the transition from abortive to productive elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNA Pol II). In case of HIV or SIV infections, binds to the transactivation domain of the viral nuclear transcriptional activator, Tat, thereby increasing Tat's affinity for the transactivating response RNA element (TAR RNA). Serves as an essential cofactor for Tat, by promoting RNA Pol II activation, allowing transcription of viral genes. {ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:16109377}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; lymphoreticular;fovea centralis;choroid;lens;retina;prostate;optic nerve;frontal lobe;placenta;thyroid;macula lutea;liver;head and neck;spleen;stomach; subthalamic nucleus;globus pallidus;testis;trigeminal ganglion;parietal lobe; 0.60285 0.15179 -0.023789244 52.09365416 230.68463 3.28340 CCNT2 0.49810408150126 0.501713641619454 0.00018227687928694 cyclin T2 FUNCTION: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin T) complex, also called positive transcription elongation factor B (P-TEFB), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNAP II). {ECO:0000269|PubMed:10364329}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; unclassifiable (Anatomical System);lung;cartilage;nasopharynx;liver;hypopharynx;testis;colon;blood;head and neck;germinal center;mammary gland;skeletal muscle; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;temporal lobe;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.93408 0.15417 -0.890882376 10.30313753 25.9733 0.84418 CCNT2-AS1 . . . CCNT2 antisense RNA 1 . . . . . . . . . . . CCNT2P1 . . . cyclin T2 pseudogene 1 . . . . . . . . . . . CCNY 0.384469091192146 0.613399196531155 0.00213171227669859 cyclin Y FUNCTION: Positive regulatory subunit of the cyclin-dependent kinases CDK14/PFTK1 and CDK16. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by recruiting CDK14/PFTK1 to the plasma membrane and promoting phosphorylation of LRP6, leading to the activation of the Wnt signaling pathway. Recruits CDK16 to the plasma membrane. Isoform 3 might play a role in the activation of MYC-mediated transcription. {ECO:0000269|PubMed:18060517, ECO:0000269|PubMed:19524571, ECO:0000269|PubMed:20059949, ECO:0000269|PubMed:22184064}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18060517}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;pineal body;adrenal cortex;blood;lens;pancreas;lung;adrenal gland;placenta;macula lutea;duodenum;liver;spleen;head and neck;kidney;stomach; whole brain;amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;testis - interstitial;atrioventricular node;caudate nucleus;subthalamic nucleus;testis - seminiferous tubule;testis;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.21014 0.12378 -0.516085732 21.20193442 27.22892 0.87666 CCNYL1 0.977770143814808 0.0222090660643771 2.07901208152665e-05 cyclin Y like 1 . . . medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;optic nerve;whole body;oesophagus;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.62342 0.07638 -0.361761279 28.6329323 44.05929 1.26436 CCNYL2 . . . cyclin Y-like 2 (pseudogene) . . . . . . . . . . . CCNYL3 . . . cyclin Y-like 3 . . . . . . . . . . . CCP110 0.015731918368029 0.984222528405366 4.55532266052089e-05 centriolar coiled-coil protein 110kDa FUNCTION: Necessary for centrosome duplication at different stages of procentriole formation. Acts as a key negative regulator of ciliogenesis in collaboration with CEP97 by capping the mother centriole thereby preventing cilia formation. Required for correct spindle formation and has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CETN2. {ECO:0000269|PubMed:12361598, ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:23486064}.; . TISSUE SPECIFICITY: Highly expressed in testis. Detected at intermediate levels in spleen, thymus, prostate, small intestine, colon and peripheral blood leukocytes. {ECO:0000269|PubMed:12361598}.; . . . . -0.350843407 29.54116537 2467.6188 9.25462 CCPG1 0.962563038904312 0.0374338558208201 3.1052748675079e-06 cell cycle progression 1 FUNCTION: Acts as an assembly platform for Rho protein signaling complexes. Limits guanine nucleotide exchange activity of MCF2L toward RHOA, which results in an inhibition of both its transcriptional activation ability and its transforming activity. Does not inhibit activity of MCF2L toward CDC42, or activity of MCF2 toward either RHOA or CDC42 (By similarity). May be involved in cell cycle regulation. {ECO:0000250, ECO:0000269|PubMed:9383053}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;dura mater;brain;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;hypopharynx;head and neck;cervix;kidney;mammary gland; amygdala;superior cervical ganglion;hypothalamus;prefrontal cortex;pons;caudate nucleus;trigeminal ganglion;cingulate cortex; 0.14661 0.10303 0.602602982 82.87331918 397.64631 4.19052 CCR1 0.891828751553939 0.10707654442346 0.00109470402260091 C-C motif chemokine receptor 1 FUNCTION: Receptor for a C-C type chemokine. Binds to MIP-1-alpha, MIP-1-delta, RANTES, and MCP-3 and, less efficiently, to MIP-1- beta or MCP-1 and subsequently transduces a signal by increasing the intracellular calcium ions level. Responsible for affecting stem cell proliferation.; . TISSUE SPECIFICITY: Widely expressed in different hematopoietic cells.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;blood;bone marrow;uterus;pancreas;lung;endometrium;placenta;germinal center;kidney;brain;mammary gland;aorta;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;whole blood; 0.24949 0.29709 0.551232944 81.48148148 50.65848 1.40139 CCR2 0.0114633179449999 0.843323512628208 0.145213169426792 C-C motif chemokine receptor 2 FUNCTION: Receptor for the CCL2, CCL7 and CCL13 chemokines. Transduces a signal by increasing intracellular calcium ion levels. Alternative coreceptor with CD4 for HIV-1 infection. {ECO:0000269|PubMed:23408426}.; . . unclassifiable (Anatomical System);prostate;liver;spleen; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.18220 . -0.091746757 46.91554612 877.8773 5.77079 CCR3 0.0318930527902387 0.815792394174555 0.152314553035207 C-C motif chemokine receptor 3 FUNCTION: Receptor for a C-C type chemokine. Binds to eotaxin, eotaxin-3, MCP-3, MCP-4, RANTES and MIP-1 delta. Subsequently transduces a signal by increasing the intracellular calcium ions level. Alternative coreceptor with CD4 for HIV-1 infection.; . TISSUE SPECIFICITY: In eosinophils as well as trace amounts in neutrophils and monocytes.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.08552 0.34692 0.885576705 89.14248644 92.67619 2.06927 CCR4 0.760806752827452 0.230309831888803 0.00888341528374559 C-C motif chemokine receptor 4 FUNCTION: High affinity receptor for the C-C type chemokines CCL17/TARC, CCL22/MDC and CKLF isoform 1/CKLF1. The activity of this receptor is mediated by G(i) proteins which activate a phosphatidylinositol-calcium second messenger system. Can function as a chemoattractant homing receptor on circulating memory lymphocytes and as a coreceptor for some primary HIV-2 isolates. In the CNS, could mediate hippocampal-neuron survival. {ECO:0000269|PubMed:10466728, ECO:0000269|PubMed:10754297, ECO:0000269|PubMed:16137713, ECO:0000269|PubMed:9169480, ECO:0000269|PubMed:9430724}.; . TISSUE SPECIFICITY: Predominantly expressed in the thymus, in peripheral blood leukocytes, including T-cells, mostly CD4+ cells, and basophils, and in platelets; at lower levels, in the spleen and in monocytes. Detected also in macrophages, IL-2-activated natural killer cells and skin-homing memory T-cells, mostly the ones expressing the cutaneous lymphocyte antigen (CLA). Expressed in brain microvascular and coronary artery endothelial cells. {ECO:0000269|PubMed:10754297}.; unclassifiable (Anatomical System);blood; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.16412 0.12421 -0.293801652 32.93819297 27.69178 0.89000 CCR5 3.51208840566472e-08 0.0524242904848429 0.947575674394273 C-C motif chemokine receptor 5 (gene/pseudogene) FUNCTION: Receptor for a number of inflammatory CC-chemokines including MIP-1-alpha, MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Acts as a coreceptor (CD4 being the primary receptor) for HIV-1 R5 isolates. {ECO:0000269|PubMed:11323418, ECO:0000269|PubMed:8639485, ECO:0000269|PubMed:8649511, ECO:0000269|PubMed:8649512, ECO:0000269|PubMed:8663314, ECO:0000269|PubMed:8699119}.; DISEASE: Diabetes mellitus, insulin-dependent, 22 (IDDM22) [MIM:612522]: A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:19073967}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in spleen, thymus, in the myeloid cell line THP-1, in the promyeloblastic cell line KG-1a and on CD4+ and CD8+ T-cells. Medium levels in peripheral blood leukocytes and in small intestine. Low levels in ovary and lung. {ECO:0000269|PubMed:8639485, ECO:0000269|PubMed:8663314}.; unclassifiable (Anatomical System);colon;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;optic nerve;nasopharynx;macula lutea;germinal center;kidney;brain;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.12070 . 0.488730112 79.52347252 390.30193 4.16032 CCR6 0.0664814988844572 0.871248567267682 0.0622699338478608 C-C motif chemokine receptor 6 FUNCTION: Receptor for a C-C type chemokine. Binds to MIP-3- alpha/LARC and subsequently transduces a signal by increasing the intracellular calcium ions level. {ECO:0000269|PubMed:9169459}.; . TISSUE SPECIFICITY: Spleen, lymph nodes, appendix, and fetal liver. Expressed in lymphocytes, T-cells and B-cells but not in natural killer cells, monocytes or granulocytes.; unclassifiable (Anatomical System);lung;nasopharynx;liver;testis;colon;spleen;germinal center;bone marrow; skeletal muscle; 0.34279 0.09378 -0.071520315 48.34866714 13.39899 0.48708 CCR7 0.647008605028774 0.346841903134606 0.0061494918366204 C-C motif chemokine receptor 7 FUNCTION: Receptor for the MIP-3-beta chemokine. Probable mediator of EBV effects on B-lymphocytes or of normal lymphocyte functions.; . TISSUE SPECIFICITY: Expressed in various lymphoid tissues and activated B- and T-lymphocytes, strongly up-regulated in B-cells infected with Epstein-Barr virus and T-cells infected with herpesvirus 6 or 7.; unclassifiable (Anatomical System);lymph node;cartilage;umbilical cord;islets of Langerhans;colon;blood;fovea centralis;choroid;lens;retina;bone marrow;pancreas;optic nerve;whole body;lung;nasopharynx;macula lutea;testis;spleen;germinal center;brain;thymus; superior cervical ganglion; 0.21171 0.62206 -0.514264485 21.41424864 74.66252 1.80701 CCR8 0.0176258189185473 0.719527251278346 0.262846929803106 C-C motif chemokine receptor 8 FUNCTION: Receptor for the chemokine CCL1/SCYA1/I-309. May regulate monocyte chemotaxis and thymic cell line apoptosis. Alternative coreceptor with CD4 for HIV-1 infection. {ECO:0000269|PubMed:10540332, ECO:0000269|PubMed:9207005, ECO:0000269|PubMed:9469461, ECO:0000269|PubMed:9521068}.; . . unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.03250 0.11325 0.393270925 76.04977589 123.94938 2.42378 CCR9 0.00464030866963606 0.680195440541208 0.315164250789156 C-C motif chemokine receptor 9 FUNCTION: Receptor for chemokine SCYA25/TECK. Subsequently transduces a signal by increasing the intracellular calcium ions level. Alternative coreceptor with CD4 for HIV-1 infection.; . TISSUE SPECIFICITY: Highly expressed in the thymus and low in lymph nodes and spleen. {ECO:0000269|PubMed:10229797, ECO:0000269|PubMed:10640743}.; unclassifiable (Anatomical System);kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;thymus; 0.23307 0.11956 0.461228372 78.46190139 54.34666 1.47280 CCR10 0.00620605308801029 0.739394121394598 0.254399825517392 C-C motif chemokine receptor 10 FUNCTION: Receptor for chemokines SCYA27 and SCYA28. Subsequently transduces a signal by increasing the intracellular calcium ions level and stimulates chemotaxis in a pre-B cell line.; . TISSUE SPECIFICITY: Expressed at high levels in adult testis, small intestine, fetal lung, fetal kidney. Weaker expression was observed in many other adult tissues including spleen, thymus, lymph node, Peyer patches, colon, heart, ovary, peripheral blood lymphocytes, thyroid and spinal cord. Also expressed by melanocytes, dermal fibroblasts, dermal microvascular endothelial cells. Also detected in T-cells and in skin-derived Langerhans cells. {ECO:0000269|PubMed:10781587}.; optic nerve;islets of Langerhans;bone;macula lutea;urinary;fovea centralis;choroid;lens;brain;retina; superior cervical ganglion; 0.22358 0.11885 0.3032669 72.009908 216.88577 3.18428 CCR12P . . . C-C motif chemokine receptor 12, pseudogene . . . . . . . . . . . CCRL1P1 . . . C-C motif chemokine receptor like 1 pseudogene 1 . . . . . . . . . . . CCRL2 0.00216377842930582 0.516299537149168 0.481536684421526 C-C motif chemokine receptor like 2 FUNCTION: Receptor for CCL19 and chemerin/RARRES2. Does not appear to be a signaling receptor, but may have a role in modulating chemokine-triggered immune responses by capturing and internalizing CCL19 or by presenting RARRES2 ligand to CMKLR1, a functional signaling receptors. Plays a critical role for the development of Th2 responses.; . TISSUE SPECIFICITY: Expressed abundantly in immunal tissues such as spleen, fetal liver, lymph node and bone marrow. Strong expression also in lung and heart. Expressed in almost all hematopoietic cells including monocytes, macrophages, PMNs, T- cells (both CD4+ and CD8+), monocyte-derived iDCs, NK cells, and CD34+ progenitor cells. B-cells expressed isoform 1 but not isoform 2. Up-regulated on synovial neutrophils of rheumatoid arthritis patients. {ECO:0000269|PubMed:11828366, ECO:0000269|PubMed:15188357, ECO:0000269|PubMed:18397265, ECO:0000269|PubMed:9473515}.; unclassifiable (Anatomical System);colon;kidney;skin; . 0.07726 0.08929 1.264035907 93.58339231 1416.59573 7.03726 CCS 3.77236487706065e-06 0.587044974756967 0.412951252878156 copper chaperone for superoxide dismutase FUNCTION: Delivers copper to copper zinc superoxide dismutase (SOD1).; . TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; liver; 0.06760 0.32574 -0.22584292 37.32012267 94.60639 2.09437 CCSAP 0.11178307102521 0.859637443075638 0.0285794858991511 centriole, cilia and spindle associated protein FUNCTION: Plays a role in microtubule (MT) stabilization and this stabilization involves the maintenance of NUMA1 at the spindle poles. Colocalizes with polyglutamylated MTs to promote MT stabilization and regulate bipolar spindle formation in mitosis. Binding of CCSAP to centrosomes and the spindle around centrosomes during mitosis inhibits MT depolymerization, thereby stabilizing the mitotic spindle (PubMed:26562023). May play a role in embryonic development. May be required for proper cilia beating (By similarity). {ECO:0000250|UniProtKB:Q6P3G4, ECO:0000269|PubMed:26562023}.; . . . . 0.22263 . . . 15.25824 0.54812 CCSER1 0.211350847441148 0.786781609600959 0.00186754295789259 coiled-coil serine rich protein 1 . . . . . . . 0.824892996 88.06912008 1550.18523 7.30104 CCSER2 0.475105131344699 0.524850813731654 4.40549236473446e-05 coiled-coil serine rich protein 2 . . . . . 0.12919 0.09413 0.446457185 77.97829677 433.04009 4.34294 CCT . . . cataract, congenital, total . . . . . . . . . . . CCT2 0.999501007213571 0.000498990841795458 1.94463331293253e-09 chaperonin containing TCP1 subunit 2 FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. {ECO:0000269|PubMed:20080638}.; . . ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; testis - interstitial;testis - seminiferous tubule;tumor;testis; 0.30244 0.50622 -0.626318434 17.03231894 32.54284 1.01357 CCT3 0.998745412971341 0.00125458330711353 3.72154587617087e-09 chaperonin containing TCP1 subunit 3 FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. {ECO:0000269|PubMed:20080638}.; . . lymphoreticular;ovary;substantia nigra;skin;prostate;optic nerve;cochlea;endometrium;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;oesophagus;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; testis - interstitial;testis - seminiferous tubule;tumor;testis;cingulate cortex; 0.92111 0.69617 -0.380166007 27.88393489 753.2878 5.44224 CCT3P1 . . . chaperonin containing TCP1 subunit 3 pseudogene 1 . . . . . . . . . . . CCT4 0.999184050209255 0.000815948486535998 1.30420898401687e-09 chaperonin containing TCP1 subunit 4 FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. {ECO:0000269|PubMed:20080638}.; . . . . 0.72634 0.51286 -0.979072682 8.752064166 46.33361 1.31186 CCT4P1 . . . chaperonin containing TCP1 subunit 4 pseudogene 1 . . . . . . . . . . . CCT4P2 . . . chaperonin containing TCP1 subunit 4 pseudogene 2 . . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;aorta; . . . . . . . CCT5 0.998786782216759 0.00121320083502449 1.69482161429887e-08 chaperonin containing TCP1 subunit 5 FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. {ECO:0000269|PubMed:20080638}.; DISEASE: Neuropathy, hereditary sensory, with spastic paraplegia, autosomal recessive (HSNSP) [MIM:256840]: A disease characterized by spastic paraplegia and progressive distal sensory neuropathy leading to mutilating ulcerations of the upper and lower limbs. {ECO:0000269|PubMed:16399879}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;umbilical cord;ovary;salivary gland;sympathetic chain;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;bone;iris;pituitary gland;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;testis;tumor; 0.81284 0.35026 -0.424258538 25.56027365 206.73609 3.10776 CCT5P1 . . . chaperonin containing TCP1 subunit 5 pseudogene 1 . . . . . . . . . . . CCT5P2 . . . chaperonin containing TCP1 subunit 5 pseudogene 2 . . . . . . . . . . . CCT6A 0.998661755000443 0.00133822347379735 2.1525759570463e-08 chaperonin containing TCP1 subunit 6A FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.; . . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;germinal center;bladder;brain;tonsil;amygdala;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;placenta;hippocampus;head and neck;kidney;stomach;thymus; tumor; 0.24693 0.43796 -0.291981272 33.20358575 345.9113 3.94523 CCT6B 8.8551551033681e-05 0.98425597368313 0.0156554747658367 chaperonin containing TCP1 subunit 6B FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis specific.; unclassifiable (Anatomical System);medulla oblongata;lung;endometrium;islets of Langerhans;nasopharynx;liver;testis;cervix;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.11522 0.11925 0.198490371 67.30360934 5479.30528 15.27896 CCT6P1 . . . chaperonin containing TCP1 subunit 6 pseudogene 1 . . . . . . . . . . . CCT6P2 . . . chaperonin containing TCP1 subunit 6 pseudogene 2 . . . . . . . . . . . CCT6P3 . . . chaperonin containing TCP1 subunit 6 pseudogene 3 . . . . . . . . . . . CCT6P4 . . . chaperonin containing TCP1 subunit 6 pseudogene 4 . . . . . . . . . . . CCT6P5 . . . chaperonin containing TCP1 subunit 6 pseudogene 5 . . . . . . . . . . . CCT7 0.989844502127012 0.010154883452649 6.14420339040455e-07 chaperonin containing TCP1 subunit 7 FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;skin;uterus;prostate;cerebral cortex;endometrium;bone;pituitary gland;testis;brain;bladder;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; whole brain;prostate;testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;testis;tumor; 0.47644 0.22854 -0.800872469 12.33191791 64.48065 1.64739 CCT7P1 . . . chaperonin containing TCP1 subunit 7 pseudogene 1 . . . . . . . . . . . CCT7P2 . . . chaperonin containing TCP1 subunit 7 pseudogene 2 . . . . . . . . . . . CCT8 0.982792760113934 0.0172067860693985 4.53816667874714e-07 chaperonin containing TCP1 subunit 8 FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. {ECO:0000269|PubMed:20080638}.; . . lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;uterus;oesophagus;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;internal ear;placenta;duodenum;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;skeletal muscle; 0.89566 0.47642 -0.246069119 36.06982779 254.13959 3.42911 CCT8L1P . . . chaperonin containing TCP1 subunit 8 like 1, pseudogene FUNCTION: Possible molecular chaperone; assists the folding of proteins upon ATP hydrolysis. {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; . 0.17508 . . . . . CCT8L2 0.00183334326021415 0.720145372265148 0.278021284474638 chaperonin containing TCP1 subunit 8 like 2 FUNCTION: Possible molecular chaperone; assists the folding of proteins upon ATP hydrolysis. {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; testis - interstitial;testis;ciliary ganglion; 0.44923 . 0.314179756 72.75300778 163.41963 2.79120 CCT8P1 . . . chaperonin containing TCP1 subunit 8 pseudogene 1 . . . . . . . . . . . CCV . . . cataract, congenital, Volkmann type . . . . . . . . . . . CCZ1 0.99469468815396 0.00530469185343507 6.19992605231915e-07 CCZ1 homolog, vacuolar protein trafficking and biogenesis associated . . . ovary;salivary gland;developmental;intestine;colon;parathyroid;choroid;vein;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;dura mater;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;pharynx;blood;skeletal muscle;breast;bile duct;pia mater;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; . 0.20290 . -0.159704656 41.90846898 84.72538 1.96050 CCZ1B . . . CCZ1 homolog B, vacuolar protein trafficking and biogenesis associated . . . ovary;salivary gland;developmental;intestine;colon;parathyroid;choroid;vein;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;dura mater;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;pharynx;blood;skeletal muscle;breast;bile duct;pia mater;lung;placenta;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;stomach; . 0.24310 . 0.881944684 89.02453409 2277.99326 8.83084 CD1A 5.0115630563305e-17 0.000231051371615473 0.999768948628385 CD1a molecule FUNCTION: Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells. {ECO:0000269|PubMed:11231314, ECO:0000269|PubMed:16272286, ECO:0000269|PubMed:18178838}.; . TISSUE SPECIFICITY: Expressed on cortical thymocytes, epidermal Langerhans cells, dendritic cells, on certain T-cell leukemias, and in various other tissues. {ECO:0000269|PubMed:11231314, ECO:0000269|PubMed:18178838}.; unclassifiable (Anatomical System);skin;thymus; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;thymus; 0.07715 0.26367 0.110306132 62.00165133 738.55475 5.39353 CD1B 1.15095187891101e-07 0.338184418823189 0.661815466081623 CD1b molecule FUNCTION: Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells. {ECO:0000269|PubMed:10981968, ECO:0000269|PubMed:14716313}.; . TISSUE SPECIFICITY: Expressed on cortical thymocytes, on certain T-cell leukemias, and in various other tissues.; . . 0.05923 0.16741 0.308721233 72.59966973 89.24999 2.03047 CD1C 6.43880889369437e-07 0.449099020444466 0.550900335674645 CD1c molecule FUNCTION: Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells. {ECO:0000269|PubMed:10786796, ECO:0000269|PubMed:10890914, ECO:0000269|PubMed:10899914, ECO:0000269|PubMed:21167756}.; . TISSUE SPECIFICITY: Expressed on cortical thymocytes, on certain T-cell leukemias, and in various other tissues.; . . 0.04660 0.19557 -0.091746757 46.91554612 75.93463 1.82624 CD1D 0.000899328621662704 0.938731579324673 0.0603690920536642 CD1d molecule FUNCTION: Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells. {ECO:0000269|PubMed:17475845}.; . TISSUE SPECIFICITY: Expressed on cortical thymocytes, on certain T-cell leukemias, and in various other tissues.; . . 0.06827 0.51173 0.018483465 55.44939844 66.06602 1.67473 CD1E 8.77644488499941e-13 0.0101996652724215 0.989800334726701 CD1e molecule FUNCTION: T-cell surface glycoprotein CD1e, soluble binds diacetylated lipids, including phosphatidyl inositides and diacylated sulfoglycolipids, and is required for the presentation of glycolipid antigens on the cell surface. The membrane- associated form is not active. {ECO:0000269|PubMed:10948205, ECO:0000269|PubMed:16311334, ECO:0000269|PubMed:21788486}.; . TISSUE SPECIFICITY: Expressed on cortical thymocytes, dendritic cells, Langerhans cells, on certain T-cell leukemias, and in various other tissues. {ECO:0000269|PubMed:10948205}.; . . 0.17215 0.09735 0.088260113 60.56853031 78.77775 1.87452 CD2 0.768323768543511 0.229911378038311 0.00176485341817738 CD2 molecule FUNCTION: CD2 interacts with lymphocyte function-associated antigen (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T- cells, the cytoplasmic domain is implicated in the signaling function.; . . . . 0.29965 0.26486 0.395088462 76.15003539 203.87998 3.08195 CD2AP 0.813221347122531 0.186777009043776 1.64383369352415e-06 CD2-associated protein FUNCTION: Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton. In collaboration with CBLC, modulates the rate of RET turnover and may act as regulatory checkpoint that limits the potency of GDNF on neuronal survival. Controls CBLC function, converting it from an inhibitor to a promoter of RET degradation. May play a role in receptor clustering and cytoskeletal polarity in the junction between T- cell and antigen-presenting cell. May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus. Also required for cytokinesis. {ECO:0000269|PubMed:15800069}.; DISEASE: Focal segmental glomerulosclerosis 3 (FSGS3) [MIM:607832]: A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation. {ECO:0000269|PubMed:12764198}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues.; ovary;colon;skin;retina;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;duodenum;cervix;kidney;mammary gland;stomach; tumor; 0.69543 0.37908 -0.354480518 29.42911064 262.95445 3.47978 CD2BP2 0.000336174209255009 0.82083211826139 0.178831707529355 CD2 (cytoplasmic tail) binding protein 2 FUNCTION: Involved in pre-mRNA splicing as component of the U5 snRNP complex that is involved in spliceosome assembly. {ECO:0000269|PubMed:15840814}.; . . lymphoreticular;ovary;salivary gland;colon;parathyroid;choroid;skin;bone marrow;uterus;whole body;cerebral cortex;endometrium;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;bile duct;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion;heart;cerebellum peduncles;placenta;white blood cells;atrioventricular node;fetal thyroid;trigeminal ganglion;skeletal muscle; 0.33354 0.12478 0.062575634 58.74026893 961.46464 6.00155 CD3D 0.00662794601075922 0.914722088930564 0.0786499650586774 CD3d molecule FUNCTION: The CD3 complex mediates signal transduction.; DISEASE: Severe combined immunodeficiency autosomal recessive T- cell-negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+) SCID) [MIM:608971]: A form of severe combined immunodeficiency (SCID), a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development. {ECO:0000269|PubMed:14602880}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Immunodeficiency 19 (IMD19) [MIM:615617]: An autosomal recessive form of severe combined immunodeficiency characterized by onset in early infancy of recurrent bacterial, viral, and fungal infections. Patients usually have chronic diarrhea, recurrent respiratory infections, and failure to thrive. Immunologic work-up shows a T-cell negative, B-cell positive, NK- cell positive phenotype. {ECO:0000269|PubMed:15546002, ECO:0000269|PubMed:21883749}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymphoreticular;heart;blood;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;prostate;optic nerve;lung;synovium;nasopharynx;thyroid;macula lutea;testis;spleen;germinal center;kidney;aorta;thymus; thymus; 0.05886 0.38242 -0.207437529 38.2814343 16.78676 0.59015 CD3E 0.302672925327359 0.693277660616761 0.00404941405587938 CD3e molecule FUNCTION: The CD3 complex mediates signal transduction, resulting in T cell activation and proliferation. Required for normal immune responses (PubMed:15546002, PubMed:8490660). {ECO:0000269|PubMed:15546002, ECO:0000269|PubMed:8490660, ECO:0000305|PubMed:15294938}.; DISEASE: Immunodeficiency 18 (IMD18) [MIM:615615]: An autosomal recessive primary immunodeficiency characterized by onset in infancy or early childhood of recurrent infections. The severity is variable, encompassing both a mild immunodeficiency and severe combined immunodeficiency (SCID), resulting in early death without bone marrow transplantation in some patients. Immunologic work-up of the IMD18 SCID patients shows a T cell-negative, B cell- positive, natural killer (NK) cell-positive phenotype, whereas T- cell development is not impaired in the mild form of IMD18. {ECO:0000269|PubMed:15546002, ECO:0000269|PubMed:8490660}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;islets of Langerhans;blood;choroid;uterus;pancreas;lung;nasopharynx;placenta;liver;spleen;germinal center;kidney;brain;mammary gland;tonsil;thymus; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.01665 0.04095 0.371224249 75.12384996 43.29527 1.24983 CD3EAP 5.68877488151799e-05 0.45508427672296 0.544858835528225 CD3e molecule associated protein FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Isoform 1 is involved in UBTF-activated transcription, presumably at a step following PIC formation.; . . ovary;colon;skin;bone marrow;uterus;prostate;frontal lobe;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.23032 0.12223 1.732552414 96.59707478 3239.78666 10.84229 CD3G 0.0250305279644512 0.916949666361235 0.0580198056743142 CD3g molecule FUNCTION: The CD3 complex mediates signal transduction.; DISEASE: Immunodeficiency 17 (IMD17) [MIM:615607]: An autosomal recessive primary immunodeficiency characterized by highly variable clinical severity. Some patients have onset of severe recurrent infections in early infancy that may be lethal, whereas others may be only mildly affected or essentially asymptomatic into young adulthood. More severely affected patients may have evidence of autoimmune disease or enteropathy. The immunologic pattern is similar among patients, showing partial T-cell lymphopenia, decreased amounts of the CD3 complex, and impaired proliferative responses to T-cell receptor dependent stimuli. The phenotype in some patients is reminiscent of severe combined immunodeficiency. {ECO:0000269|PubMed:1635567, ECO:0000269|PubMed:17277165}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);medulla oblongata;lymph node;lung;liver;testis;spleen;mammary gland; thymus; 0.06530 0.20660 0.525552348 80.57914603 3211.60894 10.80204 CD4 0.00150688725929523 0.96752492852292 0.0309681842177845 CD4 molecule FUNCTION: Accessory protein for MHC class-II antigen/T-cell receptor interaction. May regulate T-cell activation. Induces the aggregation of lipid rafts.; . . smooth muscle;ovary;colon;parathyroid;bone marrow;uterus;optic nerve;whole body;oesophagus;bone;thyroid;iris;testis;dura mater;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;arterial adventitia;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;stomach;thymus; liver; 0.44678 0.98357 0.575097644 82.1656051 186.18673 2.96304 CD5 2.72798403763384e-05 0.926671940143552 0.0733007800160716 CD5 molecule FUNCTION: May act as a receptor in regulating T-cell proliferation.; . . unclassifiable (Anatomical System);prostate;ovary;heart;endometrium;macula lutea;spleen;blood;fovea centralis;brain;skeletal muscle; superior cervical ganglion; 0.17728 0.46704 0.801024817 87.65628686 296.93684 3.67770 CD5L 7.09602208888946e-07 0.468595970874738 0.531403319523053 CD5 molecule like FUNCTION: Secreted protein that acts as a key regulator of lipid synthesis: mainly expressed by macrophages in lymphoid and inflammed tissues and regulates mechanisms in inflammatory responses, such as infection or atherosclerosis. Able to inhibit lipid droplet size in adipocytes. Following incorporation into mature adipocytes via CD36-mediated endocytosis, associates with cytosolic FASN, inhibiting fatty acid synthase activity and leading to lipolysis, the degradation of triacylglycerols into glycerol and free fatty acids (FFA). CD5L-induced lipolysis occurs with progression of obesity: participates to obesity-associated inflammation following recruitment of inflammatory macrophages into adipose tissues, a cause of insulin resistance and obesity- related metabolic disease. Regulation of intracellular lipids mediated by CD5L has a direct effect on transcription regulation mediated by nuclear receptors ROR-gamma (RORC). Acts as a key regulator of metabolic switch in T-helper Th17 cells. Regulates the expression of pro-inflammatory genes in Th17 cells by altering the lipid content and limiting synthesis of cholesterol ligand of RORC, the master transcription factor of Th17-cell differentiation. CD5L is mainly present in non-pathogenic Th17 cells, where it decreases the content of polyunsaturated fatty acyls (PUFA), affecting two metabolic proteins MSMO1 and CYP51A1, which synthesize ligands of RORC, limiting RORC activity and expression of pro-inflammatory genes. Participates in obesity- associated autoimmunity via its association with IgM, interfering with the binding of IgM to Fcalpha/mu receptor and enhancing the development of long-lived plasma cells that produce high-affinity IgG autoantibodies (By similarity). Also acts as an inhibitor of apoptosis in macrophages: promotes macrophage survival from the apoptotic effects of oxidized lipids in case of atherosclerosis (PubMed:24295828). Involved in early response to microbial infection against various pathogens by acting as a pattern recognition receptor and by promoting autophagy (PubMed:16030018, PubMed:24223991, PubMed:24583716, PubMed:25713983). {ECO:0000250|UniProtKB:Q9QWK4, ECO:0000269|PubMed:16030018, ECO:0000269|PubMed:24223991, ECO:0000269|PubMed:24295828, ECO:0000269|PubMed:24583716, ECO:0000269|PubMed:25713983}.; . TISSUE SPECIFICITY: Expressed in spleen, lymph node, thymus, bone marrow, and fetal liver, but not in non-lymphoid tissues. {ECO:0000269|PubMed:9045627}.; . . 0.05274 0.25315 0.328949044 73.41354093 83.16256 1.93859 CD6 0.00430465847629855 0.988467060175931 0.00722828134777063 CD6 molecule FUNCTION: Cell adhesion molecule that mediates cell-cell contacts and regulates T cell responses via its interaction with ALCAM/CD166 (PubMed:15048703, PubMed:15294938, PubMed:16352806, PubMed:16914752, PubMed:24945728, PubMed:24584089). Contributes to signaling cascades triggered by activation of the TCR/CD3 complex (PubMed:24584089). Functions as costimulatory molecule; promotes T-cell activation and proliferation (PubMed:15294938, PubMed:16352806, PubMed:16914752). Contributes to the formation and maturation of the immunological synapse (PubMed:15294938, PubMed:16352806). Functions as calcium-dependent pattern receptor that binds and aggregates both Gram-positive and Gram-negative bacteria. Binds both lipopolysaccharide (LPS) from Gram-negative bacteria and lipoteichoic acid from Gram-positive bacteria (PubMed:17601777). LPS binding leads to the activation of signaling cascades and down-stream MAP kinases (PubMed:17601777). Mediates activation of the inflammatory response and the secretion of pro-inflammatory cytokines in response to LPS (PubMed:17601777). {ECO:0000269|PubMed:15048703, ECO:0000269|PubMed:15294938, ECO:0000269|PubMed:16352806, ECO:0000269|PubMed:16914752, ECO:0000269|PubMed:17601777, ECO:0000269|PubMed:24584089, ECO:0000269|PubMed:24945728}.; . TISSUE SPECIFICITY: Detected on thymocytes (PubMed:15294938). Detected on peripheral blood T cells (PubMed:15048703, PubMed:16352806). Detected on natural killer (NK) cells (PubMed:16352806). Soluble CD6 is detected in blood serum (at protein level) (PubMed:17601777). Detected in spleen, thymus, appendix, lymph node and peripheral blood leukocytes (PubMed:9013954). Expressed by thymocytes, mature T-cells, a subset of B-cells known as B-1 cells, and by some cells in the brain. {ECO:0000269|PubMed:15048703, ECO:0000269|PubMed:15294938, ECO:0000269|PubMed:16352806, ECO:0000269|PubMed:17601777, ECO:0000269|PubMed:9013954}.; unclassifiable (Anatomical System);lymph node;blood;fovea centralis;choroid;lens;retina;optic nerve;lung;endometrium;larynx;macula lutea;testis;head and neck;germinal center;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.24185 . 0.821252311 88.01604152 3740.49434 11.95458 CD7 0.445277573901799 0.525756674366808 0.0289657517313931 CD7 molecule FUNCTION: Not yet known.; . . unclassifiable (Anatomical System);lymph node;cartilage;muscle;colon;blood;choroid;uterus;pancreas;lung;endometrium;placenta;liver;spleen;germinal center;kidney;aorta;tonsil;stomach; thymus; 0.11722 . 0.551232944 81.48148148 266.85657 3.50310 CD8A 0.0241810989781012 0.915142705701098 0.0606761953208008 CD8a molecule FUNCTION: Identifies cytotoxic/suppressor T-cells that interact with MHC class I bearing targets. CD8 is thought to play a role in the process of T-cell mediated killing. CD8 alpha chains binds to class I MHC molecules alpha-3 domains.; DISEASE: CD8 deficiency, familial (CD8 deficiency) [MIM:608957]: An immunologic defect characterized by absence of CD8+ cells, leading to recurrent bacterial infections. {ECO:0000269|PubMed:11435463}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;blood;parathyroid;prostate;lung;frontal lobe;nasopharynx;placenta;testis;kidney;brain;mammary gland;stomach;thymus; thymus; 0.08437 0.97198 0.014844891 54.94810097 264.64687 3.49019 CD8B 0.412381162991474 0.551314569548324 0.0363042674602021 CD8b molecule FUNCTION: Identifies cytotoxic/suppressor T-cells that interact with MHC class I bearing targets. CD8 is thought to play a role in the process of T-cell mediated killing.; . TISSUE SPECIFICITY: Isoform 1, isoform 3, isoform 5, isoform 6, isoform 7 and isoform 8 are expressed in both thymus and peripheral CD8+ T-cells. Expression of isoform 1 is higher in thymus CD8+ T-cells than in peripheral CD8+ T-cells. Expression of isoform 6 is higher in peripheral CD8+ T-cells than in thymus CD8+ T-cells. {ECO:0000269|PubMed:8436166}.; unclassifiable (Anatomical System);lymphoreticular;lung;cartilage;ovary;islets of Langerhans;testis;kidney; skeletal muscle; 0.08555 0.20078 1.548876169 95.60037745 627.07937 5.04715 CD8BP . . . CD8b molecule pseudogene FUNCTION: Identifies cytotoxic/suppressor T-cells that interact with MHC class I bearing targets. CD8 is thought to play a role in the process of T-cell mediated killing (By similarity). {ECO:0000250}.; . . . . . 0.08810 . . . . CD9 0.147688594875406 0.834489575075976 0.0178218300486176 CD9 molecule FUNCTION: Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis. Required for sperm-egg fusion. {ECO:0000269|PubMed:14575715, ECO:0000269|PubMed:7511626, ECO:0000269|PubMed:8478605}.; . TISSUE SPECIFICITY: Detected in platelets (at protein level). Expressed by a variety of hematopoietic and epithelial cells. {ECO:0000269|PubMed:19640571}.; myocardium;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;bladder;brain;heart;cartilage;spinal cord;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;cerebral cortex;synovium;testis;dura mater;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; . 0.48736 0.48993 -0.427900189 25.14744043 7.46789 0.27688 CD14 6.68636589803062e-05 0.289637598561117 0.710295537779903 CD14 molecule FUNCTION: Coreceptor for bacterial lipopolysaccharide (PubMed:1698311, PubMed:23264655). In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS) (PubMed:20133493, PubMed:23264655). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:8612135). Acts as a coreceptor for TLR2:TLR6 heterodimer in response to diacylated lipopeptides and for TLR2:TLR1 heterodimer in response to triacylated lipopeptides, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway (PubMed:16880211). Binds electronegative LDL (LDL(-)) and mediates the cytokine release induced by LDL(-) (PubMed:23880187). {ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:1698311, ECO:0000269|PubMed:20133493, ECO:0000269|PubMed:23264655, ECO:0000269|PubMed:23880187, ECO:0000269|PubMed:8612135}.; . TISSUE SPECIFICITY: Detected on macrophages (at protein level) (PubMed:1698311). Expressed strongly on the surface of monocytes and weakly on the surface of granulocytes; also expressed by most tissue macrophages. {ECO:0000269|PubMed:1698311, ECO:0000269|PubMed:25497142}.; lymphoreticular;ovary;colon;parathyroid;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;cerebral cortex;endometrium;bone;iris;testis;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; liver; 0.08630 0.33318 -0.714505427 14.4019816 96.52715 2.12252 CD19 0.853622376519338 0.14635694768834 2.06757923216388e-05 CD19 molecule FUNCTION: Assembles with the antigen receptor of B-lymphocytes in order to decrease the threshold for antigen receptor-dependent stimulation.; DISEASE: Immunodeficiency, common variable, 3 (CVID3) [MIM:613493]: A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low. {ECO:0000269|PubMed:16672701}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymphoreticular;lymph node;lung;testis;spleen;blood;germinal center;tonsil; tonsil; 0.75448 0.51750 -0.179930907 40.35739561 143.92285 2.61413 CD22 0.0308498751154716 0.969133443347564 1.66815369638536e-05 CD22 molecule FUNCTION: Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules.; . TISSUE SPECIFICITY: B-lymphocytes.; unclassifiable (Anatomical System);lymphoreticular;lymph node;cartilage;blood;skin;bone marrow;uterus;pancreas;prostate;lung;frontal lobe;placenta;visual apparatus;testis;spleen;germinal center;brain;tonsil; superior cervical ganglion;atrioventricular node;trigeminal ganglion;tonsil; 0.36800 0.28242 -0.549263935 19.95163954 538.1053 4.72901 CD24 . . . CD24 molecule FUNCTION: Modulates B-cell activation responses. Signaling could be triggered by the binding of a lectin-like ligand to the CD24 carbohydrates, and transduced by the release of second messengers derived from the GPI-anchor. Promotes AG-dependent proliferation of B-cells, and prevents their terminal differentiation into antibody-forming cells. {ECO:0000269|PubMed:11313396}.; DISEASE: Multiple sclerosis (MS) [MIM:126200]: A multifactorial, inflammatory, demyelinating disease of the central nervous system. Sclerotic lesions are characterized by perivascular infiltration of monocytes and lymphocytes and appear as indurated areas in pathologic specimens (sclerosis in plaques). The pathological mechanism is regarded as an autoimmune attack of the myelin sheath, mediated by both cellular and humoral immunity. Clinical manifestations include visual loss, extra-ocular movement disorders, paresthesias, loss of sensation, weakness, dysarthria, spasticity, ataxia and bladder dysfunction. Genetic and environmental factors influence susceptibility to the disease. {ECO:0000269|PubMed:14657362}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: B-cells. Expressed in a number of B-cell lines including P32/ISH and Namalwa. Expressed in erythroleukemia cell and small cell lung carcinoma cell lines. Also expressed on the surface of T-cells. {ECO:0000269|PubMed:14657362, ECO:0000269|PubMed:8753773}.; . . . 0.06333 . . . . CD24P1 . . . CD24 molecule pseudogene 1 . . . . . . . . . . . CD24P2 . . . CD24 molecule pseudogene 2 . . . . . . . . . . . CD24P3 . . . CD24 molecule pseudogene 3 . . . . . . . . . . . CD24P4 . . . CD24 molecule pseudogene 4 . . . . . . 0.06333 . . . . CD27 0.266793352840931 0.727744039581183 0.00546260757788531 CD27 molecule FUNCTION: Receptor for CD70/CD27L. May play a role in survival of activated T-cells. May play a role in apoptosis through association with SIVA1.; DISEASE: Lymphoproliferative syndrome 2 (LPFS2) [MIM:615122]: An autosomal recessive immunodeficiency disorder associated with persistent symptomatic EBV viremia, hypogammaglobulinemia, and impaired T-cell-dependent B-cell responses and T-cell dysfunction. The phenotype is highly variable, ranging from asymptomatic borderline-low hypogammaglobulinemia, to a full-blown symptomatic systemic inflammatory response with life-threatening EBV-related complications, including hemophagocytic lymphohistiocytosis, a lymphoproliferative disorder, and malignant lymphoma requiring stem cell transplantation. {ECO:0000269|PubMed:22197273, ECO:0000269|PubMed:22801960}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in most T-lymphocytes.; unclassifiable (Anatomical System);lymphoreticular;lymph node;cartilage;islets of Langerhans;blood;bile duct;pancreas;lung;liver;spleen;germinal center;brain;mammary gland;tonsil; superior cervical ganglion; 0.15177 0.43205 -0.0274281 51.65723048 1127.45049 6.40434 CD27-AS1 . . . CD27 antisense RNA 1 . . . . . . . . . . . CD28 0.511989197368705 0.469973262640526 0.0180375399907698 CD28 molecule FUNCTION: Involved in T-cell activation, the induction of cell proliferation and cytokine production and promotion of T-cell survival.; . TISSUE SPECIFICITY: Expressed in T-cells and plasma cells, but not in less mature B-cells.; unclassifiable (Anatomical System);uterus;whole body;cartilage;heart;nasopharynx;blood;skin; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.22209 0.54001 -0.073340031 48.11866006 12.43867 0.45146 CD33 2.30635094021775e-05 0.497999065986178 0.50197787050442 CD33 molecule FUNCTION: Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro). {ECO:0000269|PubMed:10556798, ECO:0000269|PubMed:11320212}.; . TISSUE SPECIFICITY: Monocytic/myeloid lineage cells.; unclassifiable (Anatomical System);cartilage;blood;parathyroid;bone marrow;uterus;lung;bone;liver;spleen;kidney;brain;thymus; superior cervical ganglion; 0.03502 0.08119 2.289361599 98.30738382 1143.30228 6.44529 CD34 0.00344956865429019 0.951777066480641 0.0447733648650691 CD34 molecule FUNCTION: Possible adhesion molecule with a role in early hematopoiesis by mediating the attachment of stem cells to the bone marrow extracellular matrix or directly to stromal cells. Could act as a scaffold for the attachment of lineage specific glycans, allowing stem cells to bind to lectins expressed by stromal cells or other marrow components. Presents carbohydrate ligands to selectins.; . TISSUE SPECIFICITY: Selectively expressed on hematopoietic progenitor cells and the small vessel endothelium of a variety of tissues.; smooth muscle;ovary;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;ganglion;cochlea;cerebral cortex;endometrium;thyroid;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;alveolus;spleen;kidney;mammary gland;stomach; superior cervical ganglion;placenta;appendix;trigeminal ganglion;skeletal muscle; 0.04221 0.87870 0.218717575 68.27081859 102.49867 2.18817 CD36 8.31103233660849e-46 4.57340998333625e-13 0.999999999999543 CD36 molecule FUNCTION: Multifunctional glycoprotein that acts as receptor for a broad range of ligands. Ligands can be of proteinaceous nature like thrombospondin, fibronectin, collagen or amyloid-beta as well as of lipidic nature such as oxidized low-density lipoprotein (oxLDL), anionic phospholipids, long-chain fatty acids and bacterial diacylated lipopeptides. They are generally multivalent and can therefore engage multiple receptors simultaneously, the resulting formation of CD36 clusters initiates signal transduction and internalization of receptor-ligand complexes. The dependency on coreceptor signaling is strongly ligand specific. Cellular responses to these ligands are involved in angiogenesis, inflammatory response, fatty acid metabolism, taste and dietary fat processing in the intestine (Probable). Binds long-chain fatty acids and facilitates their transport into cells, thus participating in muscle lipid utilization, adipose energy storage, and gut fat absorption (By similarity) (PubMed:18353783, PubMed:21610069). In the small intestine, plays a role in proximal absorption of dietary fatty acid and cholesterol for optimal chylomicron formation, possibly through the activation of MAPK1/3 (ERK1/2) signaling pathway (By similarity) (PubMed:18753675). Involved in oral fat perception and preferences (PubMed:22240721, PubMed:25822988). Detection into the tongue of long-chain fatty acids leads to a rapid and sustained rise in flux and protein content of pancreatobiliary secretions (By similarity). In taste receptor cells, mediates the induction of an increase in intracellulare calcium levels by long-chain fatty acids, leading to the activation of the gustatory neurons in the nucleus of the solitary tract (By similarity). Important factor in both ventromedial hypothalamus neuronal sensing of long-chain fatty acid and the regulation of energy and glucose homeostasis (By similarity). Receptor for thombospondins, THBS1 and THBS2, mediating their antiangiogenic effects (By similarity). As a coreceptor for TLR4:TLR6 heterodimer, promotes inflammation in monocytes/macrophages. Upon ligand binding, such as oxLDL or amyloid-beta 42, interacts with the heterodimer TLR4:TLR6, the complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion, through the priming and activation of the NLRP3 inflammasome (By similarity) (PubMed:20037584). Selective and nonredundant sensor of microbial diacylated lipopeptide that signal via TLR2:TLR6 heterodimer, this cluster triggers signaling from the cell surface, leading to the NF-kappa-B-dependent production of TNF, via MYD88 signaling pathway and subsequently is targeted to the Golgi in a lipid-raft dependent pathway (By similarity) (PubMed:16880211). {ECO:0000250|UniProtKB:Q07969, ECO:0000250|UniProtKB:Q08857, ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:18353783, ECO:0000269|PubMed:18753675, ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:21610069, ECO:0000269|PubMed:22240721, ECO:0000269|PubMed:25822988, ECO:0000305|PubMed:19471024}.; DISEASE: Platelet glycoprotein IV deficiency (PG4D) [MIM:608404]: A disorder characterized by macrothrombocytopenia without notable hemostatic problems and bleeding tendency. Platelet glycoprotein IV deficiency can be divided into 2 subgroups. The type I phenotype is characterized by platelets and monocytes/macrophages exhibiting complete CD36 deficiency. The type II phenotype lacks the surface expression of CD36 in platelets, but expression in monocytes/macrophages is near normal. {ECO:0000269|PubMed:11950861, ECO:0000269|PubMed:7533783}. Note=The disease is caused by mutations affecting the gene represented in this entry. Patients also have postprandial hypertriglyceridemia, insulin resistance and hypertension increasing atherosclerotic risk. {ECO:0000269|PubMed:18753675}.; DISEASE: Coronary heart disease 7 (CHDS7) [MIM:610938]: A multifactorial disease characterized by an imbalance between myocardial functional requirements and the capacity of the coronary vessels to supply sufficient blood flow. Decreased capacity of the coronary vessels is often associated with thickening and loss of elasticity of the coronary arteries. {ECO:0000269|PubMed:15282206}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . lymphoreticular;myocardium;smooth muscle;ovary;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;whole body;cerebral cortex;larynx;bone;testis;dura mater;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);meninges;heart;cartilage;urinary;adrenal cortex;blood;skeletal muscle;pia mater;lung;placenta;liver;spleen;head and neck;kidney;stomach; fetal liver;adipose tissue; 0.88408 . -1.701282638 2.553668318 678.68388 5.20914 CD37 0.00640181376663543 0.974101060371597 0.0194971258617679 CD37 molecule . . TISSUE SPECIFICITY: B-lymphocytes.; lymphoreticular;myocardium;ovary;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;liver;spleen;kidney;aorta;peripheral nerve; lymph node;white blood cells;whole blood;tonsil;bone marrow; 0.12025 0.16415 -0.359940251 28.93371078 22.56348 0.75423 CD38 7.65670798329562e-05 0.753858820927602 0.246064611992565 CD38 molecule FUNCTION: Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger for glucose-induced insulin secretion. Also has cADPr hydrolase activity. Also moonlights as a receptor in cells of the immune system.; . TISSUE SPECIFICITY: Expressed at high levels in pancreas, liver, kidney, brain, testis, ovary, placenta, malignant lymphoma and neuroblastoma. {ECO:0000269|PubMed:9074508}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;skeletal muscle;bone marrow;pancreas;prostate;nasopharynx;liver;testis;spleen;germinal center;brain; prostate;thymus; 0.05400 0.35476 -0.602450568 17.91106393 39.99224 1.17585 CD40 0.658237503542853 0.340601065641034 0.00116143081611265 CD40 molecule FUNCTION: Receptor for TNFSF5/CD40LG. Transduces TRAF6- and MAP3K8-mediated signals that activate ERK in macrophages and B cells, leading to induction of immunoglobulin secretion.; . TISSUE SPECIFICITY: B-cells and in primary carcinomas.; . . 0.16893 0.72844 0.327131069 73.27199811 32.77151 1.01750 CD40LG 0.864433712674486 0.133603417122612 0.00196287020290154 CD40 ligand FUNCTION: Mediates B-cell proliferation in the absence of co- stimulus as well as IgE production in the presence of IL-4. Involved in immunoglobulin class switching. {ECO:0000269|PubMed:15193700}.; DISEASE: X-linked immunodeficiency with hyper-IgM 1 (HIGM1) [MIM:308230]: Immunoglobulin isotype switch defect characterized by elevated concentrations of serum IgM and decreased amounts of all other isotypes. Affected males present at an early age (usually within the first year of life) recurrent bacterial and opportunistic infections, including Pneumocystis carinii pneumonia and intractable diarrhea due to cryptosporidium infection. Despite substitution treatment with intravenous immunoglobulin, the overall prognosis is rather poor, with a death rate of about 10% before adolescence. {ECO:0000269|PubMed:7532185, ECO:0000269|PubMed:7678782, ECO:0000269|PubMed:7679206, ECO:0000269|PubMed:7679801, ECO:0000269|PubMed:7717401, ECO:0000269|PubMed:8094231, ECO:0000269|PubMed:8550833, ECO:0000269|PubMed:8889581, ECO:0000269|PubMed:9150729, ECO:0000269|PubMed:9746782}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Specifically expressed on activated CD4+ T- lymphocytes.; . . 0.60959 0.76078 -0.029247611 51.40363293 47.69074 1.34110 CD44 0.0082693846811732 0.991613807211119 0.00011680810770841 CD44 molecule (Indian blood group) FUNCTION: Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events. Receptor for LGALS9; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function (By similarity). {ECO:0000250|UniProtKB:P15379, ECO:0000269|PubMed:16541107}.; . TISSUE SPECIFICITY: Isoform 10 (epithelial isoform) is expressed by cells of epithelium and highly expressed by carcinomas. Expression is repressed in neuroblastoma cells.; lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;oesophagus;larynx;bone;testis;dura mater;spinal ganglion;artery;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;cornea;mesenchyma;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;smooth muscle;adipose tissue;spinal cord;white blood cells;skin;bone marrow;uterus;uterus corpus;lung;trachea;ciliary ganglion;whole blood;trigeminal ganglion;tonsil; 0.16066 0.94901 0.225995239 68.51851852 110.78047 2.29344 CD46 0.000191603012709758 0.974855327387266 0.024953069600024 CD46 molecule FUNCTION: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement- mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T- cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity. {ECO:0000269|PubMed:10843656, ECO:0000269|PubMed:12540904}.; DISEASE: Hemolytic uremic syndrome atypical 2 (AHUS2) [MIM:612922]: An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. {ECO:0000269|PubMed:16386793, ECO:0000269|PubMed:16621965, ECO:0000269|PubMed:20513133}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype. Patients with CD46 mutations seem to have an overall better prognosis compared to patients carrying CFH mutations.; TISSUE SPECIFICITY: Expressed by all cells except erythrocytes.; ovary;skin;bone marrow;retina;prostate;endometrium;thyroid;bladder;brain;heart;tongue;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;testis;artery;pineal gland;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus; prostate;superior cervical ganglion;placenta;adrenal cortex;whole blood; 0.10479 0.17659 0.439181676 77.69521113 55.53796 1.49781 CD46P1 . . . CD46 molecule pseudogene 1 . . . . . . . . . . . CD47 0.886113810883053 0.113627833588434 0.000258355528512751 CD47 molecule FUNCTION: Has a role in both cell adhesion by acting as an adhesion receptor for THBS1 on platelets, and in the modulation of integrins. Plays an important role in memory formation and synaptic plasticity in the hippocampus (By similarity). Receptor for SIRPA, binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. Interaction with SIRPG mediates cell-cell adhesion, enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation. May play a role in membrane transport and/or integrin dependent signal transduction. May prevent premature elimination of red blood cells. May be involved in membrane permeability changes induced following virus infection. {ECO:0000250, ECO:0000269|PubMed:11509594, ECO:0000269|PubMed:15383453, ECO:0000269|PubMed:7691831}.; . TISSUE SPECIFICITY: Very broadly distributed on normal adult tissues, as well as ovarian tumors, being especially abundant in some epithelia and the brain.; smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;developmental;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;small intestine;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;nasopharynx;placenta;head and neck;kidney;stomach;aorta; prostate;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.08326 0.47352 -0.229483771 36.86010852 11.36972 0.41075 CD48 0.000152358839925206 0.429957241570745 0.56989039958933 CD48 molecule FUNCTION: Ligand for CD2. Might facilitate interaction between activated lymphocytes. Probably involved in regulating T-cell activation.; . . . . 0.06950 0.37297 0.52918614 80.81505072 291.45757 3.65188 CD52 0.530686211965741 0.40896918000682 0.0603446080274398 CD52 molecule FUNCTION: May play a role in carrying and orienting carbohydrate, as well as having a more specific role.; . . . . 0.12237 0.12853 0.72397987 85.91648974 242.51257 3.36118 CD53 0.0240198281448552 0.914777690265069 0.0612024815900761 CD53 molecule FUNCTION: Required for efficient formation of myofibers in regenerating muscle at the level of cell fusion. May be involved in growth regulation in hematopoietic cells (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: B-cells, monocytes, macrophages, neutrophils, single (CD4 or CD8) positive thymocytes and peripheral T-cells.; lymphoreticular;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;alveolus;liver;spleen;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;lymph node;white blood cells;atrioventricular node;whole blood;trigeminal ganglion;tonsil;bone marrow; 0.33876 0.21887 -0.207437529 38.2814343 18.38787 0.63695 CD55 2.49092265860477e-07 0.482056835185893 0.517942915721841 CD55 molecule (Cromer blood group) FUNCTION: This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. {ECO:0000269|PubMed:7525274}.; . TISSUE SPECIFICITY: Expressed on the plasma membranes of all cell types that are in intimate contact with plasma complement proteins. It is also found on the surfaces of epithelial cells lining extracellular compartments, and variants of the molecule are present in body fluids and in extracellular matrix.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;nose;stomach; salivary gland;placenta;adrenal cortex;fetal lung; 0.13954 0.36392 0.350995466 74.37485256 52.05403 1.42506 CD58 0.299199171430379 0.681299599322526 0.0195012292470954 CD58 molecule FUNCTION: Ligand of the T-lymphocyte CD2 glycoprotein. This interaction is important in mediating thymocyte interactions with thymic epithelial cells, antigen-independent and -dependent interactions of T-lymphocytes with target cells and antigen- presenting cells and the T-lymphocyte rosetting with erythrocytes. In addition, the LFA-3/CD2 interaction may prime response by both the CD2+ and LFA-3+ cells.; . . . . 0.16155 0.20638 0.61555716 83.13871196 82.3264 1.92612 CD59 0.0683809188352026 0.735794731888275 0.195824349276522 CD59 molecule FUNCTION: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore. This inhibitor appears to be species-specific. Involved in signal transduction for T-cell activation complexed to a protein tyrosine kinase.; DISEASE: Hemolytic anemia, CD59-mediated, with or without polyneuropathy (HACD59) [MIM:612300]: An autosomal recessive disorder characterized by infantile onset of chronic hemolysis and a relapsing-remitting polyneuropathy, often exacerbated by infection, and manifested as hypotonia, limb muscle weakness, and hyporeflexia. {ECO:0000269|PubMed:1382994, ECO:0000269|PubMed:23149847}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;sympathetic chain;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;gum;thyroid;iris;germinal center;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;islets of Langerhans;muscle;pancreas;lung;pia mater;cornea;placenta;amnion;head and neck;kidney;stomach;aorta; dorsal root ganglion;smooth muscle;trachea;placenta;ciliary ganglion; 0.02026 0.20606 -0.273576253 33.97027601 1.03934 0.02628 CD63 0.00716077580833122 0.921228264456978 0.0716109597346905 CD63 molecule FUNCTION: Functions as cell surface receptor for TIMP1 and plays a role in the activation of cellular signaling cascades. Plays a role in the activation of ITGB1 and integrin signaling, leading to the activation of AKT, FAK/PTK2 and MAP kinases. Promotes cell survival, reorganization of the actin cytoskeleton, cell adhesion, spreading and migration, via its role in the activation of AKT and FAK/PTK2. Plays a role in VEGFA signaling via its role in regulating the internalization of KDR/VEGFR2. Plays a role in intracellular vesicular transport processes, and is required for normal trafficking of the PMEL luminal domain that is essential for the development and maturation of melanocytes. Plays a role in the adhesion of leukocytes onto endothelial cells via its role in the regulation of SELP trafficking. May play a role in mast cell degranulation in response to Ms4a2/FceRI stimulation, but not in mast cell degranulation in response to other stimuli. {ECO:0000269|PubMed:16917503, ECO:0000269|PubMed:21803846, ECO:0000269|PubMed:21962903, ECO:0000269|PubMed:23632027, ECO:0000269|PubMed:24635319}.; . TISSUE SPECIFICITY: Detected in platelets (at protein level). Dysplastic nevi, radial growth phase primary melanomas, hematopoietic cells, tissue macrophages. {ECO:0000269|PubMed:19640571}.; ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;cartilage;pineal body;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;uterus;whole body;oesophagus;larynx;bone;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;muscle;pancreas;lung;pia mater;cornea;adrenal gland;placenta;head and neck;kidney;stomach;aorta;thymus; placenta; 0.45927 0.74955 -0.251530012 35.42108988 66.42873 1.67898 CD68 0.000599774358695153 0.901531071339594 0.0978691543017106 CD68 molecule FUNCTION: Could play a role in phagocytic activities of tissue macrophages, both in intracellular lysosomal metabolism and extracellular cell-cell and cell-pathogen interactions. Binds to tissue- and organ-specific lectins or selectins, allowing homing of macrophage subsets to particular sites. Rapid recirculation of CD68 from endosomes and lysosomes to the plasma membrane may allow macrophages to crawl over selectin-bearing substrates or other cells.; . TISSUE SPECIFICITY: Highly expressed by blood monocytes and tissue macrophages. Also expressed in lymphocytes, fibroblasts and endothelial cells. Expressed in many tumor cell lines which could allow them to attach to selectins on vascular endothelium, facilitating their dissemination to secondary sites. {ECO:0000269|PubMed:18405323}.; smooth muscle;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.10934 0.80674 0.463046108 78.58575136 1140.50435 6.44039 CD69 0.0188833577598224 0.898385097377067 0.0827315448631111 CD69 molecule FUNCTION: Involved in lymphocyte proliferation and functions as a signal transmitting receptor in lymphocytes, natural killer (NK) cells, and platelets.; . TISSUE SPECIFICITY: Expressed on the surface of activated T-cells, B-cells, natural killer cells, neutrophils, eosinophils, epidermal Langerhans cells and platelets.; lymphoreticular;ovary;parathyroid;skin;bone marrow;uterus;prostate;thyroid;testis;dura mater;germinal center;brain;bladder;pineal gland;tonsil;unclassifiable (Anatomical System);meninges;lymph node;cartilage;islets of Langerhans;adrenal cortex;blood;pia mater;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;liver;kidney;aorta;thymus; superior cervical ganglion;white blood cells; 0.13478 0.39636 0.080983847 59.76055674 40.25857 1.18342 CD70 0.045752208268171 0.853086954827837 0.101160836903992 CD70 molecule FUNCTION: Cytokine that binds to CD27. Plays a role in T-cell activation. Induces the proliferation of costimulated T-cells and enhances the generation of cytolytic T-cells.; . . unclassifiable (Anatomical System);prostate;pancreas;lymph node;lung;ovary;visual apparatus;testis;kidney;stomach; tumor; 0.10496 0.21491 -0.427900189 25.14744043 72.7718 1.78083 CD72 0.956612026422468 0.0433658179567191 2.21556208132244e-05 CD72 molecule FUNCTION: Plays a role in B-cell proliferation and differentiation.; . TISSUE SPECIFICITY: Pre-B-cells and B-cells but not terminally differentiated plasma cells.; lymphoreticular;ovary;salivary gland;intestine;colon;skin;uterus;prostate;optic nerve;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;visual apparatus;duodenum;liver;spleen;kidney;mammary gland;stomach; . 0.53841 0.09890 0.373041938 75.29488087 290.24801 3.64622 CD74 0.0500580580449508 0.927866653653259 0.0220752883017904 CD74 molecule FUNCTION: Plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha/beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to the endosomal/lysosomal system where the antigen processing and binding of antigenic peptides to MHC class II takes place. Serves as cell surface receptor for the cytokine MIF.; DISEASE: Note=A chromosomal aberration involving CD74 is found in a non-small cell lung tumor. Results in the formation of a CD74- ROS1 chimeric protein. {ECO:0000269|PubMed:12661006}.; . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;endometrium;thyroid;germinal center;bladder;brain;tonsil;cartilage;heart;urinary;pharynx;blood;lens;breast;epididymis;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;choroid;uterus;cerebral cortex;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach;thymus; white blood cells; 0.31067 0.35414 -0.137658575 43.57159707 . . CD79A 0.948567759868244 0.0512656337732896 0.000166606358466223 CD79a molecule FUNCTION: Required in cooperation with CD79B for initiation of the signal transduction cascade activated by binding of antigen to the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Also required for BCR surface expression and for efficient differentiation of pro- and pre-B-cells. Stimulates SYK autophosphorylation and activation. Binds to BLNK, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK. Also interacts with and increases activity of some Src- family tyrosine kinases. Represses BCR signaling during development of immature B-cells. {ECO:0000269|PubMed:8617796, ECO:0000269|PubMed:9057631}.; DISEASE: Agammaglobulinemia 3, autosomal recessive (AGM3) [MIM:613501]: A primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life. {ECO:0000269|PubMed:10525050, ECO:0000269|PubMed:11920841}. Note=The disease is caused by mutations affecting the gene represented in this entry. Two different mutations, one at the splice donor site of intron 2 and the other at the splice acceptor site for exon 3, have been identified. Both mutations give rise to a truncated protein.; TISSUE SPECIFICITY: B-cells.; lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;pharynx;blood;lens;breast;pancreas;lung;nasopharynx;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; . 0.12648 . 0.12689526 63.00424628 46.0972 1.30856 CD79B 0.950002656747314 0.0498421191242836 0.000155224128402775 CD79b molecule FUNCTION: Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation. {ECO:0000269|PubMed:12097390, ECO:0000269|PubMed:8617796, ECO:0000269|PubMed:9057631}.; DISEASE: Agammaglobulinemia 6, autosomal recessive (AGM6) [MIM:612692]: A primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life. {ECO:0000269|PubMed:17675462}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: B-cells.; unclassifiable (Anatomical System);lymphoreticular;lymph node;heart;blood;skin;uterus;pancreas;prostate;lung;endometrium;bone;placenta;pituitary gland;testis;spleen;germinal center;brain;mammary gland;aorta;tonsil; superior cervical ganglion;tonsil;skeletal muscle; 0.24113 0.32190 -0.449946534 24.00330267 9.1864 0.33550 CD80 0.25522458111489 0.717025870340107 0.0277495485450028 CD80 molecule FUNCTION: Involved in the costimulatory signal essential for T- lymphocyte activation. T-cell proliferation and cytokine production is induced by the binding of CD28, binding to CTLA-4 has opposite effects and inhibits T-cell activation. {ECO:0000269|PubMed:10583602}.; . TISSUE SPECIFICITY: Expressed on activated B-cells, macrophages and dendritic cells.; unclassifiable (Anatomical System);breast;lung;cartilage;testis;brain;tonsil; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.08954 0.63401 0.61555716 83.13871196 78.41717 1.86871 CD81 0.950521598051911 0.0493271738601781 0.00015122808791123 CD81 molecule FUNCTION: May play an important role in the regulation of lymphoma cell growth. Interacts with a 16-kDa Leu-13 protein to form a complex possibly involved in signal transduction. May act as the viral receptor for HCV.; DISEASE: Immunodeficiency, common variable, 6 (CVID6) [MIM:613496]: A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low. {ECO:0000269|PubMed:20237408}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Hematolymphoid, neuroectodermal and mesenchymal tumor cell lines.; myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;amniotic fluid;germinal center;brain;tonsil;heart;cartilage;pineal body;urinary;blood;breast;epididymis;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;choroid;whole body;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;kidney;stomach;aorta;cerebellum; uterus;thyroid;spinal cord;liver; 0.14177 0.39216 -0.339715008 30.06605331 20.70447 0.70276 CD81-AS1 . . . CD81 antisense RNA 1 . . . . . . . . . . . CD82 0.00496183334104084 0.967397085924393 0.0276410807345663 CD82 molecule FUNCTION: Associates with CD4 or CD8 and delivers costimulatory signals for the TCR/CD3 pathway.; . TISSUE SPECIFICITY: Lymphoid specific.; lymphoreticular;ovary;colon;skin;retina;uterus;prostate;endometrium;thyroid;brain;tonsil;unclassifiable (Anatomical System);tongue;islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;head and neck;stomach; superior cervical ganglion;parietal lobe; 0.27187 0.41985 -0.534490515 20.70063694 13.87258 0.50351 CD83 0.0177806863985442 0.893268780240295 0.0889505333611605 CD83 molecule FUNCTION: May play a significant role in antigen presentation or the cellular interactions that follow lymphocyte activation.; . TISSUE SPECIFICITY: Expressed by activated lymphocytes, Langerhans cells and interdigitating reticulum cells.; . . 0.27227 0.40580 0.43736446 77.56546355 89.9344 2.04147 CD83P1 . . . CD83 molecule pseudogene 1 . . . . . . . . . . . CD84 0.000390056564945539 0.84470367588636 0.154906267548695 CD84 molecule FUNCTION: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Can mediate natural killer (NK) cell cytotoxicity dependent on SH2D1A and SH2D1B (By similarity). Increases proliferative responses of activated T- cells and SH2D1A/SAP does not seem be required for this process. Homophilic interactions enhance interferon gamma/IFNG secretion in lymphocytes and induce platelet stimulation via a SH2D1A-dependent pathway. May serve as a marker for hematopoietic progenitor cells (PubMed:11564780, PubMed:12115647. PubMed:12928397, PubMed:12962726, PubMed:16037392) Required for a prolonged T- cell:B-cell contact, optimal T follicular helper function, and germinal center formation. In germinal centers involved in maintaining B-cell tolerance and in preventing autoimmunity (By similarity). In mast cells negatively regulates high affinity immunoglobulin epsilon receptor signaling; independent of SH2D1A and SH2D1B but implicating FES and PTPN6/SHP-1 (PubMed:22068234). In macrophages enhances LPS-induced MAPK phosphorylation and NF- kappaB activation and modulates LPS-induced cytokine secretion; involving ITSM 2 (By similarity). {ECO:0000250|UniProtKB:Q18PI6, ECO:0000269|PubMed:11564780, ECO:0000269|PubMed:12115647, ECO:0000269|PubMed:12928397, ECO:0000269|PubMed:12962726, ECO:0000269|PubMed:16037392, ECO:0000269|PubMed:22068234, ECO:0000305}.; . TISSUE SPECIFICITY: Predominantly expressed in hematopoietic tissues, such as lymph node, spleen and peripheral leukocytes. Expressed in macrophages, B-cells, monocytes, platelets, thymocytes, T-cells and dendritic cells. Highly expressed in memory T-cells. Expressed in mast cells. {ECO:0000269|PubMed:10698700, ECO:0000269|PubMed:11564780, ECO:0000269|PubMed:12115647, ECO:0000269|PubMed:12962726, ECO:0000269|PubMed:15245368, ECO:0000269|PubMed:22068234, ECO:0000269|PubMed:9310491}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;prostate;larynx;thyroid;bone;visual apparatus;liver;testis;head and neck;spleen;germinal center;kidney;brain;bladder; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.06617 0.13802 0.040529541 57.15380986 19.7083 0.67439 CD86 0.962700436186593 0.0372247635742197 7.48002391872673e-05 CD86 molecule FUNCTION: Receptor involved in the costimulatory signal essential for T-lymphocyte proliferation and interleukin-2 production, by binding CD28 or CTLA-4. May play a critical role in the early events of T-cell activation and costimulation of naive T-cells, such as deciding between immunity and anergy that is made by T- cells within 24 hours after activation. Isoform 2 interferes with the formation of CD86 clusters, and thus acts as a negative regulator of T-cell activation.; . TISSUE SPECIFICITY: Expressed by activated B-lymphocytes and monocytes.; unclassifiable (Anatomical System);cartilage;ovary;parathyroid;blood;choroid;lung;nasopharynx;placenta;alveolus;testis;spleen;cervix;germinal center;kidney;brain;mammary gland;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.05687 0.62329 0.705562627 85.52724699 1818.59328 7.86446 CD93 7.81902169131146e-10 0.0759484156828739 0.924051583535224 CD93 molecule FUNCTION: Receptor (or element of a larger receptor complex) for C1q, mannose-binding lectin (MBL2) and pulmonary surfactant protein A (SPA). May mediate the enhancement of phagocytosis in monocytes and macrophages upon interaction with soluble defense collagens. May play a role in intercellular adhesion.; . TISSUE SPECIFICITY: Highly expressed in endothelial cells, platelets, cells of myeloid origin, such as monocytes and neutrophils. Not expressed in cells of lymphoid origin.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; placenta;trigeminal ganglion; 0.15486 0.28768 -0.148789446 42.29771172 256.90385 3.44823 CD96 1.00320569768936e-05 0.985333732769841 0.0146562351731819 CD96 molecule FUNCTION: May be involved in adhesive interactions of activated T and NK cells during the late phase of the immune response. Promotes NK cell-target adhesion by interacting with PVR present on target cells. May function at a time after T and NK cells have penetrated the endothelium using integrins and selectins, when they are actively engaging diseased cells and moving within areas of inflammation.; DISEASE: C syndrome (CSYN) [MIM:211750]: A syndrome characterized by trigonocephaly, severe mental retardation, hypotonia, variable cardiac defects, redundant skin, and dysmorphic facial features, including upslanted palpebral fissures, epicanthal folds, depressed nasal bridge, and low-set, posteriorly rotated ears. {ECO:0000269|PubMed:17847009}. Note=The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving CD96 has been found in a patient with C syndrome. Translocation t(3;18)(q13.13;q12.1). CD96 gene was located at the 3q13.13 breakpoint. Precise structural analysis around the breakpoint showed that the gene was disrupted by the translocation in exon 5, probably leading to premature termination or loss of expression of CD96 protein. No gene was detected at the chromosome 18 breakpoint.; TISSUE SPECIFICITY: Expressed on normal T-cell lines and clones, and some transformed T-cells, but no other cultured cell lines tested. It is expressed at very low levels on activated B-cells.; unclassifiable (Anatomical System);lymphoreticular;lymph node;ovary;blood;skin;bone marrow;lung;nasopharynx;spleen;germinal center;kidney;bladder;aorta; superior cervical ganglion; 0.19826 0.07625 -0.596992387 18.18825195 166.8244 2.82214 CD99 0.21761289792797 0.773885725951012 0.00850137612101785 CD99 molecule FUNCTION: Involved in T-cell adhesion processes and in spontaneous rosette formation with erythrocytes. Plays a role in a late step of leukocyte extravasation helping leukocytes to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1. Involved in T-cell adhesion processes (By similarity). {ECO:0000250}.; . . . . 0.11895 0.28667 0.859896574 88.62349611 91.61965 2.05855 CD99L2 0.0033413380678308 0.950001092657254 0.046657569274915 CD99 molecule like 2 FUNCTION: Plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1 (By similarity). Homophilic adhesion molecule, but these interactions may not be required for cell aggregation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in many tissues, with low expression in thymus. {ECO:0000269|PubMed:12706889}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; . 0.07606 0.09120 -0.271755481 34.31823543 24.35838 0.80150 CD99P1 . . . CD99 molecule pseudogene 1 . . . . . . . . . . . CD101 5.54031092302461e-10 0.603753942456812 0.396246056989157 CD101 molecule FUNCTION: Plays a role as inhibitor of T-cells proliferation induced by CD3. Inhibits expression of IL2RA on activated T-cells and secretion of IL2. Inhibits tyrosine kinases that are required for IL2 production and cellular proliferation. Inhibits phospholipase C-gamma-1/PLCG1 phosphorylation and subsequent CD3- induced changes in intracellular free calcium. Prevents nuclear translocation of nuclear factor of activated T-cell to the nucleus. Plays a role in the inhibition of T-cell proliferation via IL10 secretion by cutaneous dendritic cells. May be a marker of CD4(+) CD56(+) leukemic tumor cells. {ECO:0000269|PubMed:11093127, ECO:0000269|PubMed:15737213, ECO:0000269|PubMed:7722299, ECO:0000269|PubMed:9233604, ECO:0000269|PubMed:9389317, ECO:0000269|PubMed:9647226}.; . TISSUE SPECIFICITY: Expressed in lung, thymus and small intestine. Detected in cutaneous dendritic cells, activated T-cells, monocytes and granulocytes as well as with epithelial cells with dendritic morphology. Expressed in some leukemic cells, the CD4(+) CD56(+) blastic tumor cells, as well as in Langerhans cells from LCH (Langerhans cell histiocytosis) patients. {ECO:0000269|PubMed:10692025, ECO:0000269|PubMed:15737213, ECO:0000269|PubMed:7722299, ECO:0000269|PubMed:7722300, ECO:0000269|PubMed:9389317}.; lung;ovary;endometrium;blood;bone marrow; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skin; 0.12804 0.16214 1.679203534 96.34347724 586.63316 4.91295 CD109 2.28792087896417e-32 3.8236506981716e-05 0.999961763493018 CD109 molecule FUNCTION: Modulates negatively TGFB1 signaling in keratinocytes. {ECO:0000269|PubMed:16754747}.; . TISSUE SPECIFICITY: Widely expressed with high level in uterus, aorta, heart, lung, trachea, placenta and in fetal heart, kidney, liver, spleen and lung. Expressed by CD34(+) acute myeloid leukemia cell lines, T-cell lines, activated T-lymphoblasts, endothelial cells and activated platelets. Isoform 5 is expressed in placenta. Isoform 1 is expressed in keratinocytes and placenta. {ECO:0000269|PubMed:11861284, ECO:0000269|PubMed:14980714, ECO:0000269|PubMed:16754747}.; unclassifiable (Anatomical System);cartilage;ovary;heart;colon;parathyroid;vein;skin;skeletal muscle;breast;uterus;bile duct;lung;endometrium;larynx;bone;placenta;visual apparatus;alveolus;testis;head and neck;kidney;artery;aorta;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.26940 0.12444 4.683992598 99.77589054 3031.3422 10.45565 CD151 0.00164311219240346 0.888520950740172 0.109835937067424 CD151 molecule (Raph blood group) FUNCTION: Essential for the proper assembly of the glomerular and tubular basement membranes in kidney. {ECO:0000269|PubMed:15265795}.; DISEASE: Nephropathy with pretibial epidermolysis bullosa and deafness (NPEBD) [MIM:609057]: A disorder characterized by the association of hereditary nephritis, epidermolysis bullosa, deafness, and beta-thalassemia minor. {ECO:0000269|PubMed:15265795}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in a variety of tissues including vascular endothelium and epidermis. Expressed on erythroid cells, with a higher level of expression in erythroid precursors than on mature erythrocytes. {ECO:0000269|PubMed:15265795}.; myocardium;medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;bile duct;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; uterus;adipose tissue;lung;heart;liver; 0.16202 0.24853 -0.359940251 28.93371078 40.39696 1.18546 CD160 1.90559903419166e-05 0.269401807774886 0.730579136234772 CD160 molecule FUNCTION: Receptor showing broad specificity for both classical and non-classical MHC class I molecules. {ECO:0000269|PubMed:9973372}.; . TISSUE SPECIFICITY: Expressed in spleen, peripheral blood, and small intestine. Expression is restricted to functional NK and T cytotoxic lymphocytes.; unclassifiable (Anatomical System);lung;whole body;frontal lobe;adrenal gland;hypothalamus;macula lutea;liver;fovea centralis;kidney;retina; skeletal muscle; 0.08714 0.08945 -0.073340031 48.11866006 20.99906 0.71059 CD163 0.0151369036126436 0.984853339064261 9.75732309540769e-06 CD163 molecule FUNCTION: Acute phase-regulated receptor involved in clearance and endocytosis of hemoglobin/haptoglobin complexes by macrophages and may thereby protect tissues from free hemoglobin-mediated oxidative damage. May play a role in the uptake and recycling of iron, via endocytosis of hemoglobin/haptoglobin and subsequent breakdown of heme. Binds hemoglobin/haptoglobin complexes in a calcium-dependent and pH-dependent manner. Exhibits a higher affinity for complexes of hemoglobin and multimeric haptoglobin of HP*1F phenotype than for complexes of hemoglobin and dimeric haptoglobin of HP*1S phenotype. Induces a cascade of intracellular signals that involves tyrosine kinase-dependent calcium mobilization, inositol triphosphate production and secretion of IL6 and CSF1. Isoform 3 exhibits the higher capacity for ligand endocytosis and the more pronounced surface expression when expressed in cells.; . TISSUE SPECIFICITY: Expressed in monocytes and mature macrophages such as Kupffer cells in the liver, red pulp macrophages in the spleen, cortical macrophages in the thymus, resident bone marrow macrophages and meningeal macrophages of the central nervous system. Expressed also in blood. Isoform 1 is the lowest abundant in the blood. Isoform 2 is the lowest abundant in the liver and the spleen. Isoform 3 is the predominant isoform detected in the blood. {ECO:0000269|PubMed:10577520, ECO:0000269|PubMed:11196644, ECO:0000269|PubMed:16434690}.; lymphoreticular;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;cochlea;endometrium;bone;thyroid;testis;dura mater;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);meninges;cartilage;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;epididymis;placenta;liver;alveolus;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;appendix; 0.22744 0.23364 -0.106515707 45.60627506 949.73058 5.96719 CD163L1 2.21693679765122e-17 0.766016647861261 0.233983352138739 CD163 molecule like 1 . . TISSUE SPECIFICITY: Isoform 1 is highly expressed in the spleen, lymph nodes, thymus, and fetal liver and weakly expressed in bone marrow and no expression was found in peripheral blood leukocytes. Isoform 1 expression is restricted to the monocyte and macrophage cell lines. Isoform 2 is only expressed in spleen. {ECO:0000269|PubMed:11086079}.; unclassifiable (Anatomical System);ovary;heart;salivary gland;intestine;pharynx;colon;parathyroid;blood;skin;skeletal muscle;breast;uterus;prostate;lung;bone;placenta;liver;testis;cervix;spleen;kidney;brain;bladder; superior cervical ganglion; 0.05267 0.07614 0.396725594 76.155933 657.41077 5.14115 CD164 0.401084248143714 0.589901405164446 0.0090143466918404 CD164 molecule FUNCTION: Sialomucin that may play a key role in hematopoiesis by facilitating the adhesion of CD34(+) cells to the stroma and by negatively regulating CD34(+)CD38(lo/-) cell proliferation. Modulates the migration of umbilical cord blood CD133+ cells and this is mediated through the CXCL12/CXCR4 axis. May play an important role in prostate cancer metastasis and the infiltration of bone marrow by cancer cells. Promotes myogenesis by enhancing CXCR4-dependent cell motility. Positively regulates myoblast migration and promotes myoblast fusion into myotubes (By similarity). {ECO:0000250, ECO:0000269|PubMed:16859559, ECO:0000269|PubMed:17077324, ECO:0000269|PubMed:9763543}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 3 are expressed in hematopoietic and non-hematopoietic tissues. Isoform 1 is expressed by prostate cancer tumors and prostate cancer cell lines. The expression is greater in bone metastases than in primary tumors. Expression in osseous metastasis is greater than that in soft tissue metastasis. Isoform 2 is expressed in the small intestine, colon, lung, thyroid and in colorectal and pancreatic adenocarcinoma. Isoform 4 is expressed by both hematopoietic progenitor cells and bone marrow stromal cells. {ECO:0000269|PubMed:10878358, ECO:0000269|PubMed:11027692, ECO:0000269|PubMed:1478919, ECO:0000269|PubMed:16859559, ECO:0000269|PubMed:9763543}.; ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;pia mater;adrenal gland;placenta;head and neck;kidney;aorta;stomach; fetal liver;trachea;thyroid;placenta;kidney; 0.29339 0.11544 -0.095386216 46.48502005 24.70973 0.81059 CD164L2 0.0337448656970662 0.822828045725248 0.143427088577685 CD164 molecule like 2 . . . . . 0.18978 . 0.148941568 64.31941496 349.6621 3.96289 CD177 . . . CD177 molecule . . TISSUE SPECIFICITY: Highly expressed in normal bone marrow and weakly expressed in fetal liver. Expressed on neutrophils. Expressed in granulocytes of patients with polycythemia vera (PV) and with essential thrombocythemia (ET). {ECO:0000269|PubMed:10753836, ECO:0000269|PubMed:12377969}.; . . 0.04981 . . . . . CD177P1 . . . CD177 molecule pseudogene 1 . . . . . . . . . . . CD180 1.35095566898906e-05 0.392842945006987 0.607143545436323 CD180 molecule FUNCTION: May cooperate with MD-1 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) in B-cells. Leads to NF-kappa-B activation. Also involved in the life/death decision of B-cells (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed mainly on mature peripherical B cells. Detected in spleen, lymph node and appendix. Not detected in pre-B and -T cells.; unclassifiable (Anatomical System);lymph node;placenta;germinal center;bone marrow; superior cervical ganglion;temporal lobe;appendix;trigeminal ganglion; 0.06117 0.10692 0.069852974 59.10592121 973.2995 6.03261 CD200 0.160238630083487 0.824373024579196 0.0153883453373169 CD200 molecule FUNCTION: Costimulates T-cell proliferation. May regulate myeloid cell activity in a variety of tissues.; . . ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;optic nerve;frontal lobe;cochlea;endometrium;thyroid;pituitary gland;spinal ganglion;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;urinary;blood;lens;skeletal muscle;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;amnion;spleen;kidney;stomach; amygdala;superior cervical ganglion;occipital lobe;placenta;trigeminal ganglion; 0.31211 0.16734 0.483275131 79.25218212 1608.46586 7.42444 CD200R1 7.03843365792991e-09 0.0747374460362238 0.925262546925342 CD200 receptor 1 FUNCTION: Inhibitory receptor for the CD200/OX2 cell surface glycoprotein. Limits inflammation by inhibiting the expression of proinflammatory molecules including TNF-alpha, interferons, and inducible nitric oxide synthase (iNOS) in response to selected stimuli. Also binds to HHV-8 K14 viral CD200 homolog with identical affinity and kinetics as the host CD200. {ECO:0000269|PubMed:12960329}.; . TISSUE SPECIFICITY: Expressed in granulocytes, monocytes, most T- cells, neutrophils, basophils and a subset of NK, NKT and B-cells (at protein level). Expressed in bone marrow, lymph nodes, spleen, lung, liver, spinal cord, kidney. Expressed in monocyte-derived dendritic and mast cells. {ECO:0000269|PubMed:12960329}.; lung;liver;testis;skeletal muscle; subthalamic nucleus; 0.03961 0.09470 0.817616644 87.95116773 62.1194 1.60701 CD200R1L 0.00306227329023055 0.816314072458181 0.180623654251589 CD200 receptor 1 like FUNCTION: May be a receptor for the CD200/OX2 cell surface glycoprotein. {ECO:0000250}.; . . . . . . -0.049474214 50.01179523 1673.4278 7.55019 CD207 1.65311921220204e-06 0.41611812417187 0.583880222708918 CD207 molecule FUNCTION: Calcium-dependent lectin displaying mannose-binding specificity. Induces the formation of Birbeck granules (BGs); is a potent regulator of membrane superimposition and zippering. Binds to sulfated as well as mannosylated glycans, keratan sulfate (KS) and beta-glucans. Facilitates uptake of antigens and is involved in the routing and/or processing of antigen for presentation to T cells. Major receptor on primary Langerhans cells for Candida species, Saccharomyces species, and Malassezia furfur. Protects against human immunodeficiency virus-1 (HIV-1) infection. Binds to high-mannose structures present on the envelope glycoprotein which is followed by subsequent targeting of the virus to the Birbeck granules leading to its rapid degradation. {ECO:0000269|PubMed:10661407, ECO:0000269|PubMed:17334373, ECO:0000269|PubMed:20026605, ECO:0000269|PubMed:20097424}.; DISEASE: Birbeck granule deficiency (BIRGD) [MIM:613393]: A condition characterized by the absence of Birbeck granules in epidermal Langerhans cells. Despite the lack of Birbeck granules, Langerhans cells are present in normal numbers and have normal morphologic characteristics and antigen-presenting capacity. {ECO:0000269|PubMed:15816828}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Exclusively expressed by Langerhans cells. Expressed in astrocytoma and malignant ependymoma, but not in normal brain tissues. {ECO:0000269|PubMed:10661407, ECO:0000269|PubMed:20026605}.; . . 0.03809 0.16044 . . 3842.81686 12.20179 CD209 2.95624746711489e-08 0.299377924405363 0.700622046032163 CD209 molecule FUNCTION: Pathogen-recognition receptor expressed on the surface of immature dendritic cells (DCs) and involved in initiation of primary immune response. Thought to mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. The receptor returns to the cell membrane surface and the pathogen-derived antigens are presented to resting T-cells via MHC class II proteins to initiate the adaptive immune response. {ECO:0000269|PubMed:11859097}.; FUNCTION: (Microbial infection) Acts as an attachment receptor for HIV-1 and HIV-2 (PubMed:11799126, PubMed:12502850, PubMed:1518869). Acts as an attachment receptor for ebolavirus (PubMed:12502850, PubMed:12504546). Acts as an attachment receptor for cytomegalovirus (PubMed:12433371, PubMed:22496863). Acts as an attachment receptor for HCV (PubMed:15371595, PubMed:16816373). Acts as an attachment receptor for dengue virus (PubMed:12682107). Acts as an attachment receptor for measles virus (PubMed:16537615). Acts as an attachment receptor for herpes simplex virus 1 (PubMed:18796707). Acts as an attachment receptor for Influenzavirus A (PubMed:21191006). Acts as an attachment receptor for SARS coronavirus (PubMed:15140961). Acts as an attachment receptor for Japanese encephalitis virus (PubMed:24623090). Acts as an attachment receptor for Lassa virus (PubMed:23966408). Acts as an attachment receptor for marburg virusn (PubMed:15479853). Acts as an attachment receptor for Respiratory syncytial virus (PubMed:22090124). Acts as an attachment receptor for Rift valley fever virus and uukuniemi virus (PubMed:21767814). Acts as an attachment receptor for west- nile virus (PubMed:16415006). Probably recognizes in a calcium- dependent manner high mannose N-linked oligosaccharides in a variety of bacterial pathogen antigens, including Leishmania pifanoi LPG, Lewis-x antigen in Helicobacter pylori LPS, mannose in Klebsiella pneumonae LPS, di-mannose and tri-mannose in Mycobacterium tuberculosis ManLAM and Lewis-x antigen in Schistosoma mansoni SEA (PubMed:16379498). {ECO:0000269|PubMed:11799126, ECO:0000269|PubMed:12433371, ECO:0000269|PubMed:12502850, ECO:0000269|PubMed:12504546, ECO:0000269|PubMed:12682107, ECO:0000269|PubMed:15140961, ECO:0000269|PubMed:1518869, ECO:0000269|PubMed:15371595, ECO:0000269|PubMed:15479853, ECO:0000269|PubMed:16379498, ECO:0000269|PubMed:16415006, ECO:0000269|PubMed:16537615, ECO:0000269|PubMed:16816373, ECO:0000269|PubMed:18796707, ECO:0000269|PubMed:21191006, ECO:0000269|PubMed:21767814, ECO:0000269|PubMed:22090124, ECO:0000269|PubMed:22496863, ECO:0000269|PubMed:23966408, ECO:0000269|PubMed:24623090}.; . TISSUE SPECIFICITY: Predominantly expressed in dendritic cells and in DC-residing tissues. Also found in placental macrophages, endothelial cells of placental vascular channels, peripheral blood mononuclear cells, and THP-1 monocytes. {ECO:0000269|PubMed:11257134, ECO:0000269|PubMed:11337487}.; unclassifiable (Anatomical System);uterus;ovary;heart;islets of Langerhans;placenta;parathyroid;choroid;skin;skeletal muscle; superior cervical ganglion;lymph node;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.11395 0.26806 0.308721233 72.59966973 63.20389 1.62699 CD226 0.505154014855792 0.490712363680102 0.00413362146410612 CD226 molecule FUNCTION: Receptor involved in intercellular adhesion, lymphocyte signaling, cytotoxicity and lymphokine secretion mediated by cytotoxic T-lymphocyte (CTL) and NK cell. {ECO:0000269|PubMed:8673704}.; . TISSUE SPECIFICITY: Expressed by peripheral blood T-lymphocytes. {ECO:0000269|PubMed:8673704}.; unclassifiable (Anatomical System);brain; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.06474 0.23607 1.128108522 92.19155461 526.74483 4.68503 CD244 0.00174717204516475 0.972873035515568 0.0253797924392674 CD244 molecule FUNCTION: Heterophilic receptor of the signaling lymphocytic activation molecule (SLAM) family; its ligand is CD48. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Acts as activating natural killer (NK) cell receptor (PubMed:10359122, PubMed:8376943, PubMed:11714776). Activating function implicates association with SH2D1A and FYN (PubMed:15713798). Downstreaming signaling involves predominantly VAV1, and, to a lesser degree, INPP5D/SHIP1 and CBL. Signal attenuation in the absence of SH2D1A is proposed to be dependent on INPP5D and to a lesser extent PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed:10934222, PubMed:15713798). Stimulates NK cell cytotoxicity, production of IFN-gamma and granule exocytosis (PubMed:8376943, PubMed:11714776). Optimal expansion and activation of NK cells seems to be dependent on the engagement of CD244 with CD48 expressed on neighboring NK cells (By similarity). Acts as costimulator in NK activation by enhancing signals by other NK receptors such as NCR3 and NCR1 (PubMed:10741393). At early stages of NK cell differentiation may function as an inhibitory receptor possibly ensuring the self- tolerance of developing NK cells (PubMed:11917118). Involved in the regulation of CD8(+) T-cell proliferation; expression on activated T-cells and binding to CD488 provides costimulatory-like function for neighboring T-cells (By similarity). Inhibits inflammatory responses in dendritic cells (DCs) (By similarity). {ECO:0000250|UniProtKB:Q07763, ECO:0000269|PubMed:10359122, ECO:0000269|PubMed:10741393, ECO:0000269|PubMed:10934222, ECO:0000269|PubMed:11714776, ECO:0000269|PubMed:11917118, ECO:0000269|PubMed:8376943, ECO:0000305|PubMed:15713798}.; . TISSUE SPECIFICITY: Expressed in spleen, PBL, followed by lung, liver, testis and small intestine. Expressed in all natural killer (NK) cells, monocytes and basophils, TCR-gamma/delta+ T-cells, monocytes, basophils, and on a subset of CD8(+) T-cells. {ECO:0000269|PubMed:10556801, ECO:0000269|PubMed:11714776, ECO:0000269|PubMed:8376943}.; unclassifiable (Anatomical System);uterus;heart;endometrium;placenta;colon;brain;skin; superior cervical ganglion;trigeminal ganglion; 0.03072 0.27473 0.374860183 75.43052607 78.66055 1.87145 CD247 0.661382967025913 0.337489029128807 0.0011280038452792 CD247 molecule FUNCTION: Probable role in assembly and expression of the TCR complex as well as signal transduction upon antigen triggering.; DISEASE: Immunodeficiency 25 (IMD25) [MIM:610163]: An immunological deficiency characterized by T-cells impaired immune response to alloantigens, tetanus toxoid and mitogens. {ECO:0000269|PubMed:16672702}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymphoreticular;lymph node;heart;tongue;blood;skin;uterus;prostate;pancreas;lung;larynx;pituitary gland;liver;testis;head and neck;spleen;kidney;germinal center;brain;thymus; thymus; 0.46248 . -0.339715008 30.06605331 17.16137 0.60314 CD248 0.541815274554495 0.455073864222046 0.00311086122345841 CD248 molecule FUNCTION: May play a role in tumor angiogenesis. {ECO:0000269|PubMed:15862292}.; . TISSUE SPECIFICITY: Expressed in tumor endothelial cells but absent or barely detectable in normal endothelial cells. Expressed in metastatic lesions of the liver and during angiogenesis of corpus luteum formation and wound healing. Expressed in vascular endothelial cells of malignant tumors but not in normal blood vessels. Expressed in stromal fibroblasts. {ECO:0000269|PubMed:10947988, ECO:0000269|PubMed:11084048, ECO:0000269|PubMed:1438285, ECO:0000269|PubMed:15862292, ECO:0000269|PubMed:16076089}.; smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;cerebral cortex;bone;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;muscle;lens;pancreas;lung;placenta;macula lutea;visual apparatus;cervix;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;adipose tissue;placenta;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22239 0.12885 0.317821209 72.81198396 1194.20372 6.55640 CD274 0.00468160279332483 0.878045757832547 0.117272639374128 CD274 molecule FUNCTION: Involved in the costimulatory signal, essential for T- cell proliferation and production of IL10 and IFNG, in an IL2- dependent and a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation and cytokine production. {ECO:0000269|PubMed:10581077, ECO:0000269|PubMed:11015443}.; . TISSUE SPECIFICITY: Highly expressed in the heart, skeletal muscle, placenta and lung. Weakly expressed in the thymus, spleen, kidney and liver. Expressed on activated T- and B-cells, dendritic cells, keratinocytes and monocytes. {ECO:0000269|PubMed:10581077, ECO:0000269|PubMed:11015443}.; . . 0.03242 0.22011 0.371224249 75.12384996 41.36169 1.20945 CD276 2.0220262891725e-05 0.70945101658487 0.290528763152238 CD276 molecule FUNCTION: May participate in the regulation of T-cell-mediated immune response. May play a protective role in tumor cells by inhibiting natural-killer mediated cell lysis as well as a role of marker for detection of neuroblastoma cells. May be involved in the development of acute and chronic transplant rejection and in the regulation of lymphocytic activity at mucosal surfaces. Could also play a key role in providing the placenta and fetus with a suitable immunological environment throughout pregnancy. Both isoform 1 and isoform 2 appear to be redundant in their ability to modulate CD4 T-cell responses. Isoform 2 is shown to enhance the induction of cytotoxic T-cells and selectively stimulates interferon gamma production in the presence of T-cell receptor signaling. {ECO:0000269|PubMed:11224528, ECO:0000269|PubMed:12906861, ECO:0000269|PubMed:14764704, ECO:0000269|PubMed:15314238, ECO:0000269|PubMed:15682454, ECO:0000269|PubMed:15961727}.; . TISSUE SPECIFICITY: Ubiquitous but not detectable in peripheral blood lymphocytes or granulocytes. Weakly expressed in resting monocytes. Expressed in dendritic cells derived from monocytes. Expressed in epithelial cells of sinonasal tissue. Expressed in extravillous trophoblast cells and Hofbauer cells of the first trimester placenta and term placenta. {ECO:0000269|PubMed:11224528, ECO:0000269|PubMed:14764704, ECO:0000269|PubMed:15961727, ECO:0000269|PubMed:16049332, ECO:0000269|PubMed:16274630}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;hypopharynx;alveolus;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; . 0.09767 0.14799 0.450099045 78.01958009 6835.12654 17.61125 CD300A 8.94314660641978e-07 0.310212462481207 0.689786643204132 CD300a molecule FUNCTION: Inhibitory receptor which may contribute to the down- regulation of cytolytic activity in natural killer (NK) cells, and to the down-regulation of mast cell degranulation. {ECO:0000269|PubMed:10746781, ECO:0000269|PubMed:16339535, ECO:0000269|PubMed:9701027}.; . TISSUE SPECIFICITY: Expressed not only by natural killer (NK) cells but also by T-cell subsets, B-cells, dendritic cells, mast cells, granulocytes and monocytes. {ECO:0000269|PubMed:10540326, ECO:0000269|PubMed:16339535, ECO:0000269|PubMed:9701027}.; unclassifiable (Anatomical System);ovary;colon;blood;skeletal muscle;retina;bone marrow;uterus;pancreas;lung;cochlea;nasopharynx;placenta;bone;liver;testis;spleen;kidney;brain; superior cervical ganglion;white blood cells;trigeminal ganglion;whole blood;bone marrow; 0.28328 . -0.247889024 35.98726115 25.74296 0.83852 CD300C 0.000578295782438879 0.712299856787878 0.287121847429683 CD300c molecule . . TISSUE SPECIFICITY: Present on the surface of monocytes, neutrophils, a proportion of peripheral blood T- and B-lymphocytes and lymphocytic cell lines.; unclassifiable (Anatomical System);lung;visual apparatus;alveolus;testis;colon;spleen;choroid;kidney;brain;mammary gland; superior cervical ganglion; 0.06110 . 0.238945317 69.20853975 211.51947 3.13601 CD300E 0.0804606661426047 0.872083834392769 0.0474554994646261 CD300e molecule FUNCTION: Probably acts as an activating receptor. {ECO:0000269|PubMed:15557162}.; . TISSUE SPECIFICITY: Present on the surface of mature hematopoietic cells of the monocyte and myeloid lineages (at protein level). {ECO:0000269|PubMed:15557162}.; unclassifiable (Anatomical System);lung;cartilage;bone;alveolus;colon;blood;skeletal muscle;bone marrow; . 0.06391 0.08733 0.661468037 84.4420854 27.49666 0.88537 CD300LB 0.000639117802263442 0.732823999918426 0.266536882279311 CD300 molecule like family member b FUNCTION: Acts as an activating immune receptor through its interaction with ITAM-bearing adapter TYROBP, and also independently by recruitment of GRB2. {ECO:0000269|PubMed:16920917, ECO:0000269|PubMed:17928527}.; . TISSUE SPECIFICITY: Expressed exclusively in myeloid lineages. {ECO:0000269|PubMed:16920917}.; unclassifiable (Anatomical System);lung;testis;skeletal muscle; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.04032 . 0.12689526 63.00424628 19.37612 0.66584 CD300LD 0.0462193913168544 0.85386350708389 0.099917101599256 CD300 molecule like family member d . . TISSUE SPECIFICITY: Expression seems restricted to cells of myeloid lineage. {ECO:0000269|PubMed:22291008}.; . . . . 0.305084559 72.22811984 686.29642 5.23056 CD300LF 4.96998888405705e-06 0.413836131942884 0.586158898068232 CD300 molecule like family member f FUNCTION: Acts as an inhibitory receptor for myeloid cells and mast cells. Inhibits osteoclast formation. {ECO:0000269|PubMed:15549731}.; . TISSUE SPECIFICITY: Highly expressed in spleen, peripheral blood leukocyte and monocyte, and lung. Weakly expressed in thymus, heart, brain, placenta, liver, skeletal muscle, kidney, pancreas, prostate, testis, ovary, small intestine or colon. Expressed selectively in monocytes and monocyte-related cells. {ECO:0000269|PubMed:15184070, ECO:0000269|PubMed:15549731}.; unclassifiable (Anatomical System);optic nerve;lung;nasopharynx;macula lutea;spleen;fovea centralis;choroid;lens;retina;cerebellum;bone marrow; . 0.03366 0.10025 0.352813824 74.49280491 23.97502 0.78950 CD300LG 0.0299351091325868 0.924308414899752 0.0457564759676612 CD300 molecule like family member g FUNCTION: Receptor which may mediate L-selectin-dependent lymphocyte rollings. Binds SELL in a calcium dependent manner. Binds lymphocyte (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and placenta. {ECO:0000269|PubMed:16876123}.; unclassifiable (Anatomical System);lung;placenta;testis; . 0.05996 . -0.290161348 33.33923095 133.91687 2.51672 CD302 0.0093852868835867 0.813397848784695 0.177216864331718 CD302 molecule FUNCTION: Potential multifunctional C-type lectin receptor that may play roles in endocytosis and phagocytosis as well as in cell adhesion and migration. {ECO:0000269|PubMed:17947679}.; . TISSUE SPECIFICITY: Expressed at moderate levels in monocytes, myeloid blood dendritic cells and granulocytes and at low levels in plasmacytoid blood dendritic cells, monocyte-derived ma crophages and monocyte-derived dendritic cells, with no expression detected in T-lymphocytes, B-lymphocytes and natural killer cells (at protein level). Expressed widely in different tissues, with highest expression levels in liver, lung, peripheral blood leukocytes and spleen, and lowest levels in neuronal tissues, skeletal muscle and ovary. Isoform 2 and isoform 3 are expressed in malignant Hodgkin lymphoma cells called Hodgkin and Reed- Sternberg (HRS) cells. {ECO:0000269|PubMed:12824192, ECO:0000269|PubMed:17947679}.; lymphoreticular;smooth muscle;ovary;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;atrium;whole body;cerebral cortex;endometrium;larynx;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);islets of Langerhans;pineal body;adrenal cortex;blood;lens;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach;aorta; whole blood; 0.32499 0.37130 0.325313577 73.11276244 302.77051 3.70679 CD320 0.0599265597352726 0.868374572465402 0.0716988677993255 CD320 molecule FUNCTION: Germinal center-B (GC-B) cells differentiate into memory B-cells and plasma cells (PC) through interaction with T-cells and follicular dendritic cells (FDC). CD320 augments the proliferation of PC precursors generated by IL-10. Receptor for the cellular uptake of transcobalamin bound cobalamin. {ECO:0000269|PubMed:11418631, ECO:0000269|PubMed:18779389}.; . TISSUE SPECIFICITY: Expressed abundantly on follicular dendritic cells (FDCs). {ECO:0000269|PubMed:10727470}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;muscle;urinary;blood;lens;bile duct;pancreas;lung;placenta;visual apparatus;macula lutea;liver;spleen;cervix;kidney;stomach; heart;placenta;testis; 0.05398 0.19055 -0.003562597 53.72729417 1211.94021 6.58968 CDA 0.787227682049009 0.206303216446435 0.00646910150455672 cytidine deaminase FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.; . TISSUE SPECIFICITY: Highly expressed in granulocytes while expression is very low in fibroblasts, chondrocytes, monocytes, and T- as well as B-cell lines.; . . 0.19135 0.55306 -0.249709319 35.74545883 1411.79974 7.01933 CDADC1 6.88626543443745e-08 0.447155911162994 0.552844019974352 cytidine and dCMP deaminase domain containing 1 FUNCTION: May play an important role in testicular development and spermatogenesis. {ECO:0000269|PubMed:16955368}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in the testis. {ECO:0000269|PubMed:16955368}.; ovary;parathyroid;skin;retina;bone marrow;uterus;optic nerve;endometrium;cerebral cortex;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;cerebellum cortex;islets of Langerhans;urinary;spinal cord;lung;placenta;visual apparatus;liver;spleen;kidney;stomach; appendix; 0.17994 . -0.712684326 14.49634348 41.85958 1.21915 CDAN1 0.928144193175439 0.071855805725115 1.09944597211363e-09 codanin 1 FUNCTION: May act as a negative regulator of ASF1 in chromatin assembly. {ECO:0000269|PubMed:22407294}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 3 is not found in erythroid cells. {ECO:0000269|PubMed:12434312}.; unclassifiable (Anatomical System);heart;ovary;blood;skeletal muscle;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;placenta;thyroid;liver;spleen;germinal center;kidney;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;adrenal gland;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.11601 0.18383 -0.828637633 11.54163718 8611.31398 20.08023 CDAN3 . . . congenital dyserythropoietic anemia, type III . . . . . . . . . . . CDB2 . . . corneal dystrophy of Bowman layer type II (Thiel-Behnke) . . . . . . . . . . . CDC5L 0.999992549267724 7.45073226208911e-06 1.40300120544147e-14 cell division cycle 5 like FUNCTION: DNA-binding protein involved in cell cycle control. May act as a transcription activator. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR). {ECO:0000269|PubMed:10570151, ECO:0000269|PubMed:11082045, ECO:0000269|PubMed:11101529, ECO:0000269|PubMed:11544257, ECO:0000269|PubMed:12927788, ECO:0000269|PubMed:18583928, ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:9038199, ECO:0000269|PubMed:9468527, ECO:0000269|PubMed:9632794}.; DISEASE: Note=A chromosomal aberration involving CDC5L is found in multicystic renal dysplasia. Translocation t(6;19)(p21;q13.1) with USF2.; TISSUE SPECIFICITY: Ubiquitously expressed in both fetal and adult tissues. {ECO:0000269|PubMed:9038199, ECO:0000269|PubMed:9598309, ECO:0000269|PubMed:9632794}.; . . 0.82165 0.15974 -0.799052816 12.45576787 81.93083 1.91920 CDC6 1.81284406664719e-06 0.872775563442433 0.1272226237135 cell division cycle 6 FUNCTION: Involved in the initiation of DNA replication. Also participates in checkpoint controls that ensure DNA replication is completed before mitosis is initiated.; DISEASE: Meier-Gorlin syndrome 5 (MGORS5) [MIM:613805]: A syndrome characterized by bilateral microtia, aplasia/hypoplasia of the patellae, and severe intrauterine and postnatal growth retardation with short stature and poor weight gain. Additional clinical findings include anomalies of cranial sutures, microcephaly, apparently low-set and simple ears, microstomia, full lips, highly arched or cleft palate, micrognathia, genitourinary tract anomalies, and various skeletal anomalies. While almost all cases have primordial dwarfism with substantial prenatal and postnatal growth retardation, not all cases have microcephaly, and microtia and absent/hypoplastic patella are absent in some. Despite the presence of microcephaly, intellect is usually normal. {ECO:0000269|PubMed:21358632}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;ovary;heart;muscle;colon;parathyroid;lens;skin;skeletal muscle;breast;uterus;prostate;pancreas;whole body;lung;bone;visual apparatus;liver;testis;cervix;spleen;germinal center;kidney;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;trigeminal ganglion; 0.99704 0.17463 0.262810045 70.43524416 2757.86941 9.90512 CDC7 0.352414094259261 0.647029271100188 0.000556634640550002 cell division cycle 7 FUNCTION: Seems to phosphorylate critical substrates that regulate the G1/S phase transition and/or DNA replication. Can phosphorylates MCM2 and MCM3. {ECO:0000269|PubMed:12065429}.; . . unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;parathyroid;skin;uterus;lung;endometrium;bone;placenta;visual apparatus;duodenum;testis;head and neck;germinal center;kidney;brain;bladder;stomach;gall bladder;thymus; atrioventricular node;skeletal muscle; 0.89839 0.19373 -0.201976964 38.98325077 122.3243 2.40906 CDC14A 0.0156184793096619 0.984154080620198 0.000227440070140092 cell division cycle 14A FUNCTION: Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis. {ECO:0000269|PubMed:11901424, ECO:0000269|PubMed:12134069, ECO:0000269|PubMed:17488717, ECO:0000269|PubMed:9367992}.; . . unclassifiable (Anatomical System);cartilage;ovary;heart;developmental;colon;parathyroid;blood;skin;skeletal muscle;bone marrow;uterus;pancreas;lung;whole body;frontal lobe;placenta;bone;liver;testis;spleen;germinal center;bladder;brain;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;appendix;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.85508 0.12634 -0.398573136 26.92852088 97.62648 2.13630 CDC14B 0.576306678785861 0.4235954284247 9.78927894388329e-05 cell division cycle 14B FUNCTION: Dual-specificity phosphatase involved in DNA damage response. Essential regulator of the G2 DNA damage checkpoint: following DNA damage, translocates to the nucleus and dephosphorylates FZR1/CDH1, a key activator of the anaphase promoting complex/cyclosome (APC/C). Dephosphorylates SIRT2 around early anaphase. Dephosphorylation of FZR1/CDH1 activates the APC/C, leading to the ubiquitination of PLK1, preventing entry into mitosis. Preferentially dephosphorylates proteins modified by proline-directed kinases. {ECO:0000269|PubMed:17488717, ECO:0000269|PubMed:18662541, ECO:0000269|PubMed:9367992}.; . . ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;urinary;lens;skeletal muscle;bile duct;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;occipital lobe;medulla oblongata;superior cervical ganglion;temporal lobe;atrioventricular node;caudate nucleus;pons;skeletal muscle;appendix;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; . 0.09972 -0.314027422 31.9297004 212.51008 3.14562 CDC14C . . . cell division cycle 14C FUNCTION: Dual-specificity phosphatase. Preferentially dephosphorylates proteins modified by proline-directed kinases (By similarity). {ECO:0000250}.; . . . . . 0.09972 . . . . CDC16 0.952255349904704 0.0477444165553702 2.33539925824256e-07 cell division cycle 16 FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:18485873}.; . . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;gall bladder;heart;cartilage;pineal body;urinary;adrenal cortex;blood;skeletal muscle;breast;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;amygdala;superior cervical ganglion;testis - interstitial;occipital lobe;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.75289 0.15103 -0.47017169 23.25430526 13.23475 0.48138 CDC20 0.000181853834795088 0.99411032128756 0.0057078248776447 cell division cycle 20 FUNCTION: Required for full ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) and may confer substrate specificity upon the complex. Is regulated by MAD2L1: in metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the CDC20-APC/C binary complex is active in degrading substrates. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces presynaptic differentiation. {ECO:0000269|PubMed:9637688, ECO:0000269|PubMed:9734353, ECO:0000269|PubMed:9811605}.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;muscle;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;tumor;testis; 0.99678 0.20838 -0.404032746 26.53338051 55.18431 1.49029 CDC20B 1.44458294596898e-11 0.0985870561885572 0.901412943796997 cell division cycle 20B . . . lung;spleen;kidney; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.13927 0.08133 0.933309256 89.82661005 1377.34214 6.95718 CDC20P1 . . . cell division cycle 20 pseudogene 1 . . . . . . . . . . . CDC23 0.999307693129197 0.00069230599695052 8.73852150967702e-10 cell division cycle 23 FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:18485873}.; . . . . 0.80825 0.14086 -0.005381972 53.50908233 136.88847 2.54297 CDC25A 0.979698044533755 0.0203012734465495 6.82019695308876e-07 cell division cycle 25A FUNCTION: Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;muscle;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; testis - seminiferous tubule;testis;globus pallidus; 0.99898 0.37326 -0.291981272 33.20358575 96.05413 2.11781 CDC25B 0.590733232372986 0.409249189359373 1.75782676409337e-05 cell division cycle 25B FUNCTION: Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Directly dephosphorylates CDK1 and stimulates its kinase activity. The three isoforms seem to have a different level of activity. {ECO:0000269|PubMed:17332740}.; . . medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;nervous;islets of Langerhans;muscle;adrenal cortex;blood;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion; 0.60793 0.18264 -1.131590109 6.481481481 93.10563 2.07464 CDC25C 3.00948392905045e-08 0.505353984725813 0.494645985179347 cell division cycle 25C FUNCTION: Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. When phosphorylated, highly effective in activating G2 cells into prophase. Directly dephosphorylates CDK1 and activates its kinase activity. {ECO:0000269|PubMed:8119945}.; . . unclassifiable (Anatomical System);lymph node;ovary;heart;colon;skin;skeletal muscle;breast;uterus;bile duct;lung;endometrium;larynx;bone;placenta;visual apparatus;liver;testis;cervix;head and neck;spleen;germinal center;brain;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.98808 0.42032 -0.023789244 52.09365416 3676.42803 11.79055 CDC26 0.646600813692917 0.327038950889503 0.0263602354175808 cell division cycle 26 FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May recruit the E2 ubiquitin-conjugating enzymes to the complex. {ECO:0000269|PubMed:18485873}.; . . . . 0.43736 0.10017 0.301449681 71.80938901 10.18241 0.37091 CDC26P1 . . . cell division cycle 26 pseudogene 1 . . . . . . . . . . . CDC27 0.486673202422918 0.51332514680758 1.65076950150842e-06 cell division cycle 27 FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:18485873}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;pineal gland;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;fetal liver;prefrontal cortex;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.94354 0.15358 -0.117432389 44.89266336 13.5224 0.49131 CDC27P1 . . . cell division cycle 27 pseudogene 1 . . . . . . . . . . . CDC27P2 . . . cell division cycle 27 pseudogene 2 . . . . . . . . . . . CDC27P3 . . . cell division cycle 27 pseudogene 3 . . . . . . . . . . . CDC27P4 . . . cell division cycle 27 pseudogene 4 . . . . . . . . . . . CDC27P5 . . . cell division cycle 27 pseudogene 5 . . . . . . . . . . . CDC27P6 . . . cell division cycle 27 pseudogene 6 . . . . . . . . . . . CDC27P7 . . . cell division cycle 27 pseudogene 7 . . . . . . . . . . . CDC27P8 . . . cell division cycle 27 pseudogene 8 . . . . . . . . . . . CDC27P9 . . . cell division cycle 27 pseudogene 9 . . . . . . . . . . . CDC27P10 . . . cell division cycle 27 pseudogene 10 . . . . . . . . . . . CDC27P11 . . . cell division cycle 27 pseudogene 11 . . . . . . . . . . . CDC34 0.56046297683146 0.426996390779269 0.0125406323892714 cell division cycle 34 FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 48'-linked polyubiquitination. Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgamma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5- mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation. Also involved in the degradation of beta-catenin. Is target of human herpes virus 1 protein ICP0, leading to ICP0-dependent dynamic interaction with proteasomes. {ECO:0000269|PubMed:10329681, ECO:0000269|PubMed:10373550, ECO:0000269|PubMed:10871850, ECO:0000269|PubMed:11675391, ECO:0000269|PubMed:12037680, ECO:0000269|PubMed:15652359, ECO:0000269|PubMed:17461777, ECO:0000269|PubMed:17698585, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:19126550, ECO:0000269|PubMed:19945379, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20347421}.; . TISSUE SPECIFICITY: Expressed in testes during spermatogenesis to regulate repression of cAMP-induced transcription. {ECO:0000269|PubMed:10373550}.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;testis; 0.23849 . -0.648365105 16.35999056 9.05947 0.33166 CDC37 0.96235789574322 0.0376265598760777 1.55443807025673e-05 cell division cycle 37 FUNCTION: Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. {ECO:0000269|PubMed:8666233}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;oesophagus;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;adrenal cortex;pharynx;blood;skeletal muscle;bile duct;pancreas;lung;cornea;epididymis;placenta;visual apparatus;duodenum;liver;cervix;spleen;kidney;mammary gland;stomach;peripheral nerve;thymus; whole brain;cerebellum peduncles;prefrontal cortex;white blood cells; 0.28927 0.22085 -0.336073593 30.55555556 98.87697 2.15048 CDC37L1 0.935601045748761 0.0643391601964933 5.97940547459473e-05 cell division cycle 37-like 1 FUNCTION: Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, placenta and skeletal muscle. {ECO:0000269|PubMed:11413142}.; . . 0.12251 0.11297 -0.339715008 30.06605331 21.27415 0.71897 CDC37L1-AS1 . . . CDC37L1 antisense RNA 1 (head to head) . . . . . . . . . . . CDC37P1 . . . cell division cycle 37 pseudogene 1 . . . . . . . . . . . CDC37P2 . . . cell division cycle 37 pseudogene 2 . . . . . . . . . . . CDC40 0.973128081365404 0.0268716427692026 2.75865393459343e-07 cell division cycle 40 FUNCTION: Associates with the spliceosome late in the splicing pathway and may function in the second step of pre-mRNA splicing. {ECO:0000269|PubMed:9830021}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;aorta;stomach; testis - interstitial;superior cervical ganglion;pons;atrioventricular node;skeletal muscle; 0.28064 0.15280 -0.159704656 41.90846898 72.25218 1.77114 CDC42 0.656574472233884 0.337780292998427 0.00564523476768873 cell division cycle 42 FUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Plays a role in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. Mediates CDC42-dependent cell migration. {ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:15642749, ECO:0000269|PubMed:17038317}.; . . lymphoreticular;ovary;umbilical cord;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; whole brain;amygdala;dorsal root ganglion;thalamus;superior cervical ganglion;occipital lobe;medulla oblongata;hypothalamus;temporal lobe;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;whole blood;cingulate cortex;parietal lobe; . 0.91381 -0.09720619 46.20193442 13.98795 0.50800 CDC42-IT1 . . . CDC42 intronic transcript 1 . . . . . . . . . . . CDC42BPA 0.99992014796463 7.9852035369634e-05 2.57656286820024e-18 CDC42 binding protein kinase alpha FUNCTION: Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2. In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Phosphorylates: PPP1R12A, LIMK1 and LIMK2. May play a role in TFRC-mediated iron uptake. {ECO:0000269|PubMed:11340065, ECO:0000269|PubMed:11399775, ECO:0000269|PubMed:15723050, ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:20188707, ECO:0000269|PubMed:21457715, ECO:0000269|PubMed:9092543, ECO:0000269|PubMed:9418861}.; . TISSUE SPECIFICITY: Abundant in the heart, brain, skeletal muscle, kidney, and pancreas, with little or no expression in the lung and liver. {ECO:0000269|PubMed:9092543}.; lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;spleen;kidney;stomach;peripheral nerve; dorsal root ganglion;thalamus;superior cervical ganglion;occipital lobe;subthalamic nucleus;prefrontal cortex;ciliary ganglion;atrioventricular node;caudate nucleus;trigeminal ganglion;skeletal muscle;parietal lobe; 0.34666 0.16052 -1.543300564 3.320358575 2561.99615 9.45755 CDC42BPB 0.999999999630375 3.69624474937762e-10 9.29543575592032e-26 CDC42 binding protein kinase beta FUNCTION: Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2. In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Phosphorylates PPP1R12A. {ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:21457715, ECO:0000269|PubMed:21949762}.; . TISSUE SPECIFICITY: Expressed in all tissues examined, with high levels in heart, brain, placenta and lung. {ECO:0000269|PubMed:10198171}.; medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; amygdala; 0.24850 0.11601 -3.291569382 0.42462845 159.11353 2.75671 CDC42BPG 1.40627803289603e-17 0.874375116138811 0.125624883861189 CDC42 binding protein kinase gamma FUNCTION: May act as a downstream effector of CDC42 in cytoskeletal reorganization. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q5VT25, ECO:0000269|PubMed:15194684}.; . TISSUE SPECIFICITY: Expressed in heart and skeletal muscle. {ECO:0000269|PubMed:15194684}.; thyroid;placenta;head and neck;germinal center;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.12008 0.10369 -1.464556369 3.75678226 2467.86866 9.25649 CDC42EP1 1.05708648523099e-05 0.197795982371278 0.80219344676387 CDC42 effector protein 1 FUNCTION: Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts. {ECO:0000269|PubMed:10430899}.; . TISSUE SPECIFICITY: Endothelial and bone marrow stromal cells.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;islets of Langerhans;salivary gland;muscle;colon;choroid;skin;bone marrow;uterus;pancreas;prostate;lung;bone;visual apparatus;testis;spleen;brain;mammary gland;stomach; . 0.08861 0.10603 -0.442665927 24.53408823 193.55365 3.01830 CDC42EP2 0.150921493212549 0.633457826668447 0.215620680119005 CDC42 effector protein 2 FUNCTION: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts in a CDC42-dependent manner. {ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:11035016}.; . TISSUE SPECIFICITY: Highly expressed in the heart. Weakly expressed in the pancreas and liver. {ECO:0000269|PubMed:10490598}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;bone marrow;prostate;oesophagus;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;muscle;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12770 0.10994 0.106667882 61.73036093 69.63772 1.73126 CDC42EP3 0.275699032932777 0.633509808380523 0.0907911586867002 CDC42 effector protein 3 FUNCTION: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts. {ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:11035016}.; . TISSUE SPECIFICITY: Highly expressed in the heart and weakly in the brain. {ECO:0000269|PubMed:10490598}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;cochlea;germinal center;bladder;brain;amygdala;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;uterus;oesophagus;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;muscle;lung;placenta;hippocampus;head and neck;kidney;stomach;aorta; uterus;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.11937 0.11406 -0.293801652 32.93819297 23.24582 0.77568 CDC42EP3P1 . . . CDC42 effector protein 3 pseudogene 1 . . . . . . . . . . . CDC42EP4 0.0975901833443728 0.770810384492394 0.131599432163233 CDC42 effector protein 4 FUNCTION: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts.; . TISSUE SPECIFICITY: Not detected in any of the adult tissues tested. May be expressed only in fetal or embryonic tissues.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.16421 0.11360 -0.556537043 19.72753008 83.52066 1.94345 CDC42EP5 0.359353006035898 0.482581794731726 0.158065199232376 CDC42 effector protein 5 FUNCTION: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts. Inhibits MAPK8 independently of CDC42 binding. Controls septin organization and this effect is negatively regulated by CDC42 (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;lung;placenta;visual apparatus;macula lutea;kidney;stomach; . 0.14598 . . . 242.95751 3.36503 CDC42P1 . . . cell division cycle 42 pseudogene 1 . . . . . . . . . . . CDC42P2 . . . cell division cycle 42 pseudogene 2 . . . . . . . . . . . CDC42P3 . . . cell division cycle 42 pseudogene 3 . . . . . . . . . . . CDC42P4 . . . cell division cycle 42 pseudogene 4 . . . . . . . . . . . CDC42P5 . . . cell division cycle 42 pseudogene 5 . . . . . . . . . . . CDC42P6 . . . cell division cycle 42 pseudogene 6 . . . . . . . . . . . CDC42SE1 0.0135194909211455 0.666844068587922 0.319636440490932 CDC42 small effector 1 FUNCTION: Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly. Alters CDC42-induced cell shape changes. In activated T-cells, may play a role in CDC42-mediated F-actin accumulation at the immunological synapse. May play a role in early contractile events in phagocytosis in macrophages. {ECO:0000269|PubMed:10816584, ECO:0000269|PubMed:15840583, ECO:0000269|PubMed:17045588}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in T-lymphocytes, dendritic and whole blood cells. {ECO:0000269|PubMed:15840583}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; lymph node;whole blood;bone marrow; 0.21852 0.12378 0.057118534 57.99716914 1.20885 0.03836 CDC42SE2 0.753728627374484 0.236652021637092 0.00961935098842438 CDC42 small effector 2 FUNCTION: Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly. Alters CDC42-induced cell shape changes. In activated T-cells, may play a role in CDC42-mediated F-actin accumulation at the immunological synapse. May play a role in early contractile events in phagocytosis in macrophages. {ECO:0000269|PubMed:10816584, ECO:0000269|PubMed:15840583}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in T-lymphocytes. Highly expressed in CCRF-CEM T-lymphocytes, Jurkat T-lymphocytes, and Raji B-lymphocytes compared (at protein level). {ECO:0000269|PubMed:15840583}.; lymphoreticular;smooth muscle;ovary;skin;prostate;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;duodenum;head and neck;kidney;stomach; trigeminal ganglion; 0.27557 0.12378 -0.09720619 46.20193442 1.83486 0.05767 CDC45 0.0691043589822534 0.930779647144889 0.000115993872857286 cell division cycle 45 FUNCTION: Required for initiation of chromosomal DNA replication.; . TISSUE SPECIFICITY: Widely expressed, highest levels are found in adult testis and thymus and in fetal liver.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;prostate;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; tumor; 0.98565 0.23629 -0.26629572 34.81953291 112.93059 2.31231 CDC73 0.999958508392824 4.14916062559694e-05 9.19657587018405e-13 cell division cycle 73 FUNCTION: Tumor suppressor probably involved in transcriptional and post-transcriptional control pathways. May be involved in cell cycle progression through the regulation of cyclin D1/PRAD1 expression. Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non- phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Connects PAF1C with the cleavage and polyadenylation specificity factor (CPSF) complex and the cleavage stimulation factor (CSTF) complex, and with Wnt signaling. Involved in polyadenylation of mRNA precursors. {ECO:0000269|PubMed:15580289, ECO:0000269|PubMed:15632063, ECO:0000269|PubMed:15923622, ECO:0000269|PubMed:16630820, ECO:0000269|PubMed:16989776, ECO:0000269|PubMed:19136632, ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742, ECO:0000269|PubMed:20541477, ECO:0000269|PubMed:21329879}.; DISEASE: Hyperparathyroidism-jaw tumor syndrome (HPT-JT) [MIM:145001]: Autosomal dominant, multiple neoplasia syndrome primarily characterized by hyperparathyroidism due to parathyroid tumors. Thirty percent of individuals with HPT-JT may also develop ossifying fibromas, primarily of the mandible and maxilla, which are distinct from the brown tumors associated with severe hyperparathyroidism. Kidney lesions may also occur in HPT-JT as bilateral cysts, renal hamartomas or Wilms tumors. {ECO:0000269|PubMed:12434154, ECO:0000269|PubMed:15613436, ECO:0000269|PubMed:16487440}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Parathyroid carcinoma (PRTC) [MIM:608266]: These cancers characteristically result in more profound clinical manifestations of hyperparathyroidism than do parathyroid adenomas, the most frequent cause of primary hyperparathyroidism. Early en bloc resection of the primary tumor is the only curative treatment. {ECO:0000269|PubMed:14585940}. Note=The gene represented in this entry is involved in disease pathogenesis.; TISSUE SPECIFICITY: Found in adrenal and parathyroid glands, kidney and heart. {ECO:0000269|PubMed:15580289}.; . . 0.25430 0.15588 -0.383807564 27.41802312 6.11441 0.23098 CDC123 0.239628030246869 0.760081875869237 0.00029009388389393 cell division cycle 123 FUNCTION: Required for S phase entry of the cell cycle. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocytes with the highest expression in testis. {ECO:0000269|PubMed:9683532}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus; superior cervical ganglion;caudate nucleus;pons;atrioventricular node; 0.17349 . -0.427900189 25.14744043 652.29048 5.12378 CDCA2 1.61084700624997e-05 0.998432272489314 0.00155161904062331 cell division cycle associated 2 FUNCTION: Regulator of chromosome structure during mitosis required for condensin-depleted chromosomes to retain their compact architecture through anaphase. Acts by mediating the recruitment of phopsphatase PP1-gamma subunit (PPP1CC) to chromatin at anaphase and into the following interphase. At anaphase onset, its association with chromatin targets a pool of PPP1CC to dephosphorylate substrates. {ECO:0000269|PubMed:16492807, ECO:0000269|PubMed:16998479}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:16492807}.; ovary;salivary gland;intestine;colon;skin;prostate;whole body;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;pharynx;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach; . 0.04668 0.10444 1.032445072 91.12408587 1835.56655 7.89991 CDCA3 0.913578465420915 0.0862950303800672 0.000126504199017641 cell division cycle associated 3 FUNCTION: F-box-like protein which is required for entry into mitosis. Acts by participating in E3 ligase complexes that mediate the ubiquitination and degradation of WEE1 kinase at G2/M phase (By similarity). {ECO:0000250}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;blood;lens;skeletal muscle;bile duct;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;thymus; testis - interstitial;testis - seminiferous tubule;testis;tumor; 0.65031 0.11875 0.393270925 76.04977589 46.09515 1.30826 CDCA4 0.499553162512056 0.480704687395948 0.0197421500919962 cell division cycle associated 4 FUNCTION: May participate in the regulation of cell proliferation through the E2F/RB pathway. May be involved in molecular regulation of hematopoietic stem cells and progenitor cell lineage commitment and differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:16984923}.; . TISSUE SPECIFICITY: Highest levels of expression in the pancreas, thymus, testis, spleen, liver, placenta and leukocytes. Relatively low levels in the lung, kidney, prostate, ovary, small intestine and colon. Hardly detectable, if at all, in the brain, skeletal muscle and heart. {ECO:0000269|PubMed:16984923}.; ovary;colon;skin;retina;uterus;prostate;whole body;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis;skeletal muscle; 0.26668 0.11598 0.040529541 57.15380986 50.58689 1.39985 CDCA4P1 . . . cell division cycle associated 4 pseudogene 1 . . . . . . . . . . . CDCA4P2 . . . cell division cycle associated 4 pseudogene 2 . . . . . . . . . . . CDCA4P3 . . . cell division cycle associated 4 pseudogene 3 . . . . . . . . . . . CDCA4P4 . . . cell division cycle associated 4 pseudogene 4 . . . . . . . . . . . CDCA5 0.0707160812169158 0.872153044039064 0.0571308747440201 cell division cycle associated 5 FUNCTION: Regulator of sister chromatid cohesion in mitosis stabilizing cohesin complex association with chromatin. May antagonize the action of WAPL which stimulates cohesin dissociation from chromatin. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Required for efficient DNA double-stranded break repair. {ECO:0000269|PubMed:15837422, ECO:0000269|PubMed:17349791, ECO:0000269|PubMed:21111234}.; . . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;muscle;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; tumor; 0.64912 . 0.148941568 64.31941496 128.50799 2.47059 CDCA7 0.141954502881666 0.857220868213025 0.000824628905308692 cell division cycle associated 7 FUNCTION: Participates in MYC-mediated cell transformation and apoptosis; induces anchorage-independent growth and clonogenicity in lymphoblastoid cells. Insufficient to induce tumorigenicity when overexpressed but contributes to MYC-mediated tumorigenesis. May play a role as transcriptional regulator. {ECO:0000269|PubMed:11598121, ECO:0000269|PubMed:15994934, ECO:0000269|PubMed:16580749, ECO:0000269|PubMed:23166294}.; . TISSUE SPECIFICITY: Ubiquitous with higher level in thymus and small intestine. Overexpressed in a large number of tumors, in blood from patients with acute myelogenous leukemia (AML) and in chronic myelogenous leukemia (CML) blast crisis. {ECO:0000269|PubMed:11598121, ECO:0000269|PubMed:15994934}.; smooth muscle;ovary;colon;parathyroid;vein;skin;bone marrow;uterus;whole body;frontal lobe;endometrium;synovium;larynx;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;small intestine;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; atrioventricular node;trigeminal ganglion;skeletal muscle; 0.42177 0.10089 -0.692458599 14.96815287 32.113 1.00797 CDCA7L 0.120661404768047 0.879114531908875 0.000224063323077596 cell division cycle associated 7 like FUNCTION: Plays a role in transcriptional regulation as a repressor that inhibits monoamine oxidase A (MAOA) activity and gene expression by binding to the promoter. Plays an important oncogenic role in mediating the full transforming effect of MYC in medulloblastoma cells. Involved in apoptotic signaling pathways; May act downstream of P38-kinase and BCL-2, but upstream of CASP3/caspase-3 as well as CCND1/cyclin D1 and E2F1. {ECO:0000269|PubMed:15654081, ECO:0000269|PubMed:15994933, ECO:0000269|PubMed:16829576}.; . TISSUE SPECIFICITY: Ubiquitous. Overexpressed in medulloblastoma. {ECO:0000269|PubMed:15654081, ECO:0000269|PubMed:15994933}.; ovary;salivary gland;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;cochlea;endometrium;gum;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;muscle;adrenal cortex;pharynx;blood;skeletal muscle;bile duct;pancreas;lung;adrenal gland;epididymis;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; . 0.34931 0.11906 -1.065444789 7.425100259 47.28403 1.33354 CDCA8 0.0971532321701097 0.901240925918612 0.00160584191127845 cell division cycle associated 8 FUNCTION: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. In the complex, it may be required to direct the CPC to centromeric DNA. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment. {ECO:0000269|PubMed:15249581, ECO:0000269|PubMed:15260989, ECO:0000269|PubMed:16571674, ECO:0000269|PubMed:18243099}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;pharynx;blood;lens;bile duct;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;kidney;mammary gland;stomach; testis;tumor;thymus; 0.51900 0.10193 -0.183570861 39.95046001 30.19698 0.96339 CDCP1 0.0211525261340679 0.9781310842818 0.00071638958413213 CUB domain containing protein 1 FUNCTION: May be involved in cell adhesion and cell matrix association. May play a role in the regulation of anchorage versus migration or proliferation versus differentiation via its phosphorylation. May be a novel marker for leukemia diagnosis and for immature hematopoietic stem cell subsets. Belongs to the tetraspanin web involved in tumor progression and metastasis. {ECO:0000269|PubMed:11466621, ECO:0000269|PubMed:12799299, ECO:0000269|PubMed:15153610, ECO:0000269|PubMed:16007225, ECO:0000269|PubMed:16404722, ECO:0000269|PubMed:8647901}.; . TISSUE SPECIFICITY: Highly expressed in mitotic cells with low expression during interphase. Detected at highest levels in skeletal muscle and colon with lower levels in kidney, small intestine, placenta and lung. Up-regulated in a number of human tumor cell lines, as well as in colorectal cancer, breast carcinoma and lung cancer. Also expressed in cells with phenotypes reminiscent of mesenchymal stem cells and neural stem cells. {ECO:0000269|PubMed:11466621, ECO:0000269|PubMed:12660814, ECO:0000269|PubMed:15153610, ECO:0000269|PubMed:16007225}.; ovary;salivary gland;foreskin;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;epidermis;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;alveolus;cervix;kidney;mammary gland;stomach; . 0.11285 0.36226 0.271907863 70.73012503 283.83697 3.60630 CDCP2 6.92291104064707e-10 0.0195063833882518 0.980493615919457 CUB domain containing protein 2 . . . . . 0.06472 . -0.132199953 43.97853267 3871.63056 12.26492 CDH1 0.338547688109087 0.661426839739286 2.54721516269318e-05 cadherin 1 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7. {ECO:0000269|PubMed:16417575}.; DISEASE: Hereditary diffuse gastric cancer (HDGC) [MIM:137215]: A cancer predisposition syndrome with increased susceptibility to diffuse gastric cancer. Diffuse gastric cancer is a malignant disease characterized by poorly differentiated infiltrating lesions resulting in thickening of the stomach. Malignant tumors start in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. {ECO:0000269|PubMed:10319582, ECO:0000269|PubMed:12216071}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Heterozygous CDH1 germline mutations are responsible for familial cases of diffuse gastric cancer. Somatic mutations has also been found in patients with sporadic diffuse gastric cancer and lobular breast cancer.; DISEASE: Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of endometrium, the mucous lining of the uterus. Most endometrial cancers are adenocarcinomas, cancers that begin in cells that make and release mucus and other fluids. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease. {ECO:0000269|PubMed:8075649}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Breast cancer, lobular (LBC) [MIM:137215]: A type of breast cancer that begins in the milk-producing glands (lobules) of the breast. {ECO:0000269|PubMed:17660459}. Note=The gene represented in this entry may be involved in disease pathogenesis.; TISSUE SPECIFICITY: Non-neural epithelial tissues.; ovary;rectum;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;larynx;thyroid;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;epididymis;placenta;macula lutea;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;olfactory bulb;salivary gland;beta cell islets;fetal thyroid;skin;prostate;pancreas;fetal liver;lung;trachea;thyroid;placenta;fetal lung;kidney; 0.82520 0.93422 -1.061810361 7.519462137 122.67172 2.41215 CDH2 0.897440931236462 0.102558737450379 3.31313158619067e-07 cadherin 2 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;developmental;adrenal cortex;lens;skin;skeletal muscle;retina;bone marrow;uterus;prostate;lung;frontal lobe;bone;thyroid;visual apparatus;hippocampus;liver;testis;amniotic fluid;kidney;brain; dorsal root ganglion;amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;testis - interstitial;smooth muscle;heart;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.94298 0.26817 -1.061810361 7.519462137 579.92018 4.88141 CDH3 1.8060327648012e-08 0.850272492467357 0.149727489472315 cadherin 3 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.; DISEASE: Hypotrichosis congenital with juvenile macular dystrophy (HJMD) [MIM:601553]: A disorder characterized by congenital hypotrichosis, early hair loss, and severe degenerative changes of the retinal macula that culminate in blindness during the second to third decade of life. {ECO:0000269|PubMed:11544476, ECO:0000269|PubMed:12445216}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ectodermal dysplasia, ectrodactyly, and macular dystrophy syndrome (EEMS) [MIM:225280]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. It is an autosomal recessive condition characterized by features of ectodermal dysplasia such as sparse eyebrows and scalp hair, and selective tooth agenesis associated with macular dystrophy and ectrodactyly. {ECO:0000269|PubMed:15805154}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in some normal epithelial tissues and in some carcinoma cell lines. {ECO:0000269|PubMed:2702654}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;gum;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;head and neck;kidney;mammary gland;stomach; lung;thymus; 0.12891 0.09965 -0.102878093 45.65935362 2041.45904 8.32838 CDH4 0.966988413982154 0.0330114930297004 9.29881455927779e-08 cadherin 4 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. May play an important role in retinal development.; . TISSUE SPECIFICITY: Expressed mainly in brain but also found in other tissues.; unclassifiable (Anatomical System);optic nerve;lung;islets of Langerhans;muscle;brain; whole brain;dorsal root ganglion;amygdala;subthalamic nucleus;occipital lobe;prefrontal cortex;globus pallidus;ciliary ganglion;caudate nucleus;cingulate cortex;parietal lobe; 0.14101 0.14318 -2.070835943 1.615947157 232.04773 3.29334 CDH5 0.146020817838369 0.853820497871794 0.000158684289836531 cadherin 5 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. This cadherin may play a important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. It associates with alpha-catenin forming a link to the cytoskeleton. Acts in concert with KRIT1 to establish and maintain correct endothelial cell polarity and vascular lumen. These effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for activation of PRKCZ and for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction. {ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:21269602}.; . TISSUE SPECIFICITY: Endothelial tissues and brain.; smooth muscle;ovary;sympathetic chain;parathyroid;vein;skin;uterus;prostate;optic nerve;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach;aorta; heart;placenta;fetal lung; 0.50298 0.22234 -1.056370776 7.578438311 286.34813 3.62366 CDH6 0.980834799201761 0.0191651765692539 2.42289855274847e-08 cadherin 6 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.; . TISSUE SPECIFICITY: Highly expressed in brain, cerebellum, and kidney. Lung, pancreas, and gastric mucosa show a weak expression. Also expressed in certain liver and kidney carcinomas.; unclassifiable (Anatomical System);ovary;cartilage;muscle;parathyroid;skeletal muscle;uterus;breast;prostate;whole body;lung;endometrium;placenta;testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;thalamus;medulla oblongata;atrioventricular node;caudate nucleus;trigeminal ganglion; 0.85734 0.08171 -1.3098007 4.847841472 49.63788 1.38059 CDH7 0.763007122581869 0.236989660195214 3.21722291657838e-06 cadherin 7 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.; . . unclassifiable (Anatomical System);frontal lobe;brain; subthalamic nucleus;superior cervical ganglion;olfactory bulb;cerebellum peduncles;temporal lobe;appendix;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.38021 0.13194 -0.885424753 10.4623732 47.11557 1.32841 CDH8 0.997463771271808 0.00253620802099409 2.07071979694781e-08 cadherin 8 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.; . TISSUE SPECIFICITY: Mainly expressed in brain. Found in certain nerve cell lines, such as retinoblasts, glioma cells and neuroblasts.; unclassifiable (Anatomical System);brain;mammary gland;peripheral nerve; superior cervical ganglion;globus pallidus;appendix;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.76728 0.12299 -0.488577883 22.64685067 57.63769 1.53338 CDH9 0.992483590378092 0.00751635010891187 5.95129960300399e-08 cadherin 9 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.; . . kidney; superior cervical ganglion;atrioventricular node;skeletal muscle;parietal lobe; 0.42489 0.09429 -0.376526807 28.10804435 3357.77748 11.10339 CDH10 0.309152977089917 0.690814760865389 3.22620446940498e-05 cadherin 10 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.; . TISSUE SPECIFICITY: Predominantly expressed in brain. Also found in adult and fetal kidney. Very low levels detected in prostate and fetal lung. {ECO:0000269|PubMed:10386616}.; unclassifiable (Anatomical System);adrenal gland;islets of Langerhans;visual apparatus;brain;skeletal muscle; dorsal root ganglion;amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.42021 0.11113 -0.800872469 12.33191791 34.27199 1.04877 CDH11 0.999267144964547 0.000732850074347386 4.96110520051185e-09 cadherin 11 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.; DISEASE: Note=A chromosomal aberration involving CDH11 is a common genetic feature of aneurysmal bone cyst, a benign osseous neoplasm. Translocation t(16;17)(q22;p13) with USP6. The translocation generates a fusion gene in which the strong CDH11 promoter is fused to the entire USP6 coding sequence, resulting in USP6 transcriptional up-regulation.; TISSUE SPECIFICITY: Expressed mainly in brain but also found in other tissues. Expressed in neuroblasts.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;muscle;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;smooth muscle;adipose tissue;globus pallidus; 0.16535 0.24272 0.069852974 59.10592121 5021.70227 14.46847 CDH12 0.00145119382648096 0.997108538750607 0.0014402674229118 cadherin 12 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.; . TISSUE SPECIFICITY: Brain.; . . 0.26046 0.12596 -0.352661697 29.48808681 4076.94377 12.67249 CDH12P1 . . . cadherin 12 pseudogene 1 . . . . . . . . . . . CDH12P2 . . . cadherin 12 pseudogene 2 . . . . . . . . . . . CDH12P3 . . . cadherin 12 pseudogene 3 . . . . . . . . . . . CDH12P4 . . . cadherin 12 pseudogene 4 . . . . . . . . . . . CDH13 0.217594377239137 0.78204849416179 0.000357128599072674 cadherin 13 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. May act as a negative regulator of neural cell growth. {ECO:0000269|PubMed:10737605}.; . TISSUE SPECIFICITY: Highly expressed in heart. In the CNS, expressed in cerebral cortex, medulla, hippocampus, amygdala, thalamus and substantia nigra. No expression detected in cerebellum or spinal cord. {ECO:0000269|PubMed:10737605, ECO:0000269|PubMed:8673923}.; ovary;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;bone;testis;spinal ganglion;artery;brain;unclassifiable (Anatomical System);heart;cartilage;lung;nasopharynx;placenta;liver;spleen;head and neck;kidney;aorta; dorsal root ganglion;superior cervical ganglion;occipital lobe;heart;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin; 0.32022 0.40347 0.305084559 72.22811984 147.30048 2.64464 CDH15 5.96232075451435e-12 0.0595434016339287 0.940456598360109 cadherin 15 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. M-cadherin is part of the myogenic program and may provide a trigger for terminal muscle differentiation.; DISEASE: Note=A chromosomal aberration involving CDH15 and KIRREL3 is found in a patient with severe mental retardation and dysmorphic facial features. Translocation t(11;16)(q24.2;q24).; DISEASE: Mental retardation, autosomal dominant 3 (MRD3) [MIM:612580]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:19012874}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the brain and cerebellum. {ECO:0000269|PubMed:19012874}.; unclassifiable (Anatomical System);heart;ovary;cartilage;muscle;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;placenta;macula lutea;testis;kidney;brain; superior cervical ganglion;cerebellum peduncles;globus pallidus;pons;trigeminal ganglion;cingulate cortex;skeletal muscle;cerebellum; 0.12643 0.12266 -1.080231599 7.277659825 1650.24792 7.50870 CDH16 6.80363206242921e-13 0.21234998335281 0.787650016646509 cadherin 16 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.; . TISSUE SPECIFICITY: Kidney specific.; unclassifiable (Anatomical System);lung;testis;colon;spleen;kidney;skeletal muscle;stomach; thyroid;ciliary ganglion;kidney; 0.09081 0.12844 -0.946125119 9.377211607 998.46283 6.08909 CDH17 2.80756011028863e-06 0.996161293977457 0.00383589846243275 cadherin 17 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. LI-cadherin may have a role in the morphological organization of liver and intestine. Involved in intestinal peptide transport. {ECO:0000269|PubMed:8153632}.; . TISSUE SPECIFICITY: Expressed in the gastrointestinal tract and pancreatic duct. Not detected in kidney, lung, liver, brain, adrenal gland and skin. {ECO:0000269|PubMed:8153632}.; unclassifiable (Anatomical System);bile duct;pancreas;small intestine;lacrimal gland;liver;colon;skeletal muscle;stomach; pancreas;superior cervical ganglion; 0.10125 0.14859 -0.303114925 32.25406936 133.70401 2.51276 CDH18 0.463926460278232 0.535836585557351 0.000236954164416395 cadherin 18 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.; . . unclassifiable (Anatomical System);bile duct;lung;frontal lobe;ovary;hypothalamus;bone;testis;brain;mammary gland; dorsal root ganglion;subthalamic nucleus;medulla oblongata;superior cervical ganglion;cerebellum peduncles;temporal lobe;prefrontal cortex;globus pallidus;ciliary ganglion;pons;cingulate cortex;parietal lobe; 0.54248 0.12333 -1.219785504 5.602736494 56.6821 1.51414 CDH19 1.92476251537999e-09 0.401323390859762 0.598676607215475 cadherin 19 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.; . TISSUE SPECIFICITY: Expressed in many tissues, with the exception of uterus.; unclassifiable (Anatomical System);uterus;myocardium;whole body;heart;trabecular meshwork;liver;kidney;brain;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;olfactory bulb;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.04142 0.09564 1.401792296 94.75112055 596.89832 4.94265 CDH20 0.980513136445033 0.019486247055693 6.16499273574634e-07 cadherin 20 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.; . TISSUE SPECIFICITY: Expressed in placenta, adult brain, and fetal brain.; unclassifiable (Anatomical System); superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.41102 0.09740 -0.619039275 17.39797122 686.47702 5.23130 CDH22 . . . cadherin 22 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. PB-cadherins may have a role in the morphological organization of pituitary gland and brain tissues (By similarity). {ECO:0000250}.; . . . . 0.17458 0.10691 -1.151821487 6.269167256 514.92861 4.64214 CDH23 0.0506929591139338 0.949268622794338 3.84180917276542e-05 cadherin-related 23 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells. CDH23 is required for establishing and/or maintaining the proper organization of the stereocilia bundle of hair cells in the cochlea and the vestibule during late embryonic/early postnatal development. It is part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal hearing.; DISEASE: Usher syndrome 1D (USH1D) [MIM:601067]: USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa with sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). USH1 is characterized by profound congenital sensorineural deafness, absent vestibular function and prepubertal onset of progressive retinitis pigmentosa leading to blindness. {ECO:0000269|PubMed:11138009, ECO:0000269|PubMed:12075507, ECO:0000269|PubMed:15660226, ECO:0000269|PubMed:16679490, ECO:0000269|PubMed:18429043}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Usher syndrome 1D/F (USH1DF) [MIM:601067]: USH1DF patients are heterozygous for mutations in CDH23 and PCDH15, indicating a digenic inheritance pattern. {ECO:0000269|PubMed:15537665}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry.; DISEASE: Deafness, autosomal recessive, 12 (DFNB12) [MIM:601386]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:11090341, ECO:0000269|PubMed:12075507, ECO:0000269|PubMed:12522556, ECO:0000269|PubMed:15829536, ECO:0000269|PubMed:16679490, ECO:0000269|PubMed:17850630, ECO:0000269|PubMed:22899989, ECO:0000269|PubMed:24767429}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Particularly strong expression in the retina. Found also in the cochlea.; medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;bone marrow;retina;prostate;optic nerve;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;pharynx;blood;lens;breast;pancreas;lung;macula lutea;visual apparatus;liver;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - interstitial;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cerebellum; 0.32126 0.20307 -1.837761842 2.05826846 23222.44281 31.45196 CDH23-AS1 . . . CDH23 antisense RNA 1 . . . . . . . . . . . CDH24 6.70386871764034e-05 0.995081431396943 0.00485152991588105 cadherin 24 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Cadherin-24 mediate strong cell-cell adhesion. {ECO:0000269|PubMed:12734196}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;larynx;bone;placenta;colon;head and neck;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skeletal muscle;cerebellum; 0.32088 0.10136 0.023941474 55.75607455 417.10017 4.27466 CDH26 5.55635014833331e-23 0.000694275516457122 0.999305724483543 cadherin 26 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.; . . uterus;prostate;lung;heart;endometrium;nasopharynx;placenta;testis;blood;germinal center;brain;bladder;skin; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.02935 0.06826 0.920379023 89.57891012 467.10581 4.47718 CDHR1 5.14858122982389e-10 0.364320956871133 0.635679042614009 cadherin related family member 1 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be required for the structural integrity of the outer segment (OS) of photoreceptor cells (By similarity). {ECO:0000250}.; DISEASE: Cone-rod dystrophy 15 (CORD15) [MIM:613660]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. {ECO:0000269|PubMed:20805371}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);optic nerve;tongue;thyroid;macula lutea;colon;head and neck;fovea centralis;bladder;retina; superior cervical ganglion;caudate nucleus;trigeminal ganglion;cingulate cortex;skeletal muscle;skin; 0.44263 0.14397 0.010992521 54.17551309 730.71163 5.36670 CDHR2 6.36801969145907e-10 0.999624173632852 0.000375825730345512 cadherin related family member 2 FUNCTION: Role in contact inhibition at the lateral surface of epithelial cells. {ECO:0000269|PubMed:12117771}.; . TISSUE SPECIFICITY: Highly expressed in liver, kidney and colon. Moderately expressed in small intestine. Down-regulated in a number of liver and colon cancers. {ECO:0000269|PubMed:12117771, ECO:0000269|PubMed:15534908}.; unclassifiable (Anatomical System);medulla oblongata;small intestine;tongue;colon;fovea centralis;choroid;lens;skeletal muscle;retina;pancreas;optic nerve;whole body;macula lutea;liver;testis;head and neck;spleen;brain; superior cervical ganglion;testis - interstitial;liver;testis;pons; 0.09203 0.08985 0.957091004 90.1155933 2653.10231 9.68072 CDHR3 6.98636378515767e-13 0.215355302807547 0.784644697191754 cadherin related family member 3 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.; . TISSUE SPECIFICITY: Expressed in bronchial epithelium from adults and in fetal lung tissue. {ECO:0000269|PubMed:24241537}.; unclassifiable (Anatomical System);lung;cartilage;nasopharynx;liver;testis;brain;mammary gland; superior cervical ganglion;medulla oblongata;thalamus;spinal cord;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; . . 0.321464691 72.85326728 4054.55827 12.62753 CDHR4 0.0134739491219744 0.666150432289075 0.320375618588951 cadherin related family member 4 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types (By similarity). {ECO:0000250}.; . . lung; . . . 0.262810045 70.43524416 227.14099 3.25652 CDHR5 1.31307026997115e-10 0.322129806697009 0.677870193171684 cadherin related family member 5 FUNCTION: Acts as a calcium-dependent cell adhesion protein. {ECO:0000250|UniProtKB:Q9JIK1}.; . TISSUE SPECIFICITY: Highest expression in kidney, liver, colon and small intestine. In kidney, expressed apically along brush border of proximal convoluted tubule but not in cortical collecting ducts. Isoform 1 is expressed primarily in adult small intestine and colon. Isoform 2 is highly expressed in fetal liver. {ECO:0000269|PubMed:12167596}.; unclassifiable (Anatomical System);small intestine;colon;fovea centralis;choroid;lens;retina;breast;pancreas;optic nerve;placenta;macula lutea;liver;spleen;kidney;bladder;stomach; fetal liver;uterus corpus;superior cervical ganglion;liver;globus pallidus;appendix;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09192 0.11495 0.394900016 76.06157113 1884.8054 7.98424 CDIP1 0.734505012174229 0.253672021533387 0.0118229662923842 cell death-inducing p53 target 1 FUNCTION: Acts as an important p53/TP53-apoptotic effector. Regulates TNF-alpha-mediated apoptosis in a p53/TP53-dependent manner. {ECO:0000269|PubMed:17599062}.; . TISSUE SPECIFICITY: Highly expressed in brain. Expressed at lower level in heart, skeletal muscle, kidney, pancreas and liver. Weakly or not expressed in placenta and lung. {ECO:0000269|PubMed:10570909}.; . . 0.16271 0.12434 -0.229483771 36.86010852 161.48919 2.77687 CDIPT 0.193882539034725 0.758842328427184 0.0472751325380909 CDP-diacylglycerol--inositol 3-phosphatidyltransferase FUNCTION: Catalyzes the biosynthesis of phosphatidylinositol (PtdIns) as well as PtdIns:inositol exchange reaction. May thus act to reduce an excessive cellular PtdIns content. The exchange activity is due to the reverse reaction of PtdIns synthase and is dependent on CMP, which is tightly bound to the enzyme. {ECO:0000269|PubMed:8110188}.; . TISSUE SPECIFICITY: Detected in placenta (at protein level). Widely expressed. Higher expression in adult liver and skeletal muscle, slightly lower levels seen in pancreas, kidney, lung, placenta, brain, heart, leukocyte, colon, small intestine, ovary, testis, prostate, thymus and spleen. In fetus, expressed in kidney, liver, lung and brain. {ECO:0000269|PubMed:8110188}.; myocardium;lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;adrenal cortex;blood;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;thymus; amygdala;thyroid; 0.14180 0.36178 -0.251530012 35.42108988 254.32243 3.43058 CDIPT-AS1 . . . CDIPT antisense RNA 1 (head to head) . . . . . . . . . . . CDK1 0.970572339309587 0.029386099349574 4.15613408387723e-05 cyclin-dependent kinase 1 FUNCTION: Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition, and regulates G1 progress and G1-S transition via association with multiple interphase cyclins. Required in higher cells for entry into S-phase and mitosis. Phosphorylates PARVA/actopaxin, APC, AMPH, APC, BARD1, Bcl- xL/BCL2L1, BRCA2, CALD1, CASP8, CDC7, CDC20, CDC25A, CDC25C, CC2D1A, CSNK2 proteins/CKII, FZR1/CDH1, CDK7, CEBPB, CHAMP1, DMD/dystrophin, EEF1 proteins/EF-1, EZH2, KIF11/EG5, EGFR, FANCG, FOS, GFAP, GOLGA2/GM130, GRASP1, UBE2A/hHR6A, HIST1H1 proteins/histone H1, HMGA1, HIVEP3/KRC, LMNA, LMNB, LMNC, LBR, LATS1, MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MYB, NEFH, NFIC, NPC/nuclear pore complex, PITPNM1/NIR2, NPM1, NCL, NUCKS1, NPM1/numatrin, ORC1, PRKAR2A, EEF1E1/p18, EIF3F/p47, p53/TP53, NONO/p54NRB, PAPOLA, PLEC/plectin, RB1, UL40/R2, RAB4A, RAP1GAP, RCC1, RPS6KB1/S6K1, KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin, STIP1, TEX14, beta-tubulins, MAPT/TAU, NEDD1, VIM/vimentin, TK1, FOXO1, RUNX1/AML1, SIRT2 and RUNX2. CDK1/CDC2-cyclin-B controls pronuclear union in interphase fertilized eggs. Essential for early stages of embryonic development. During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes which phosphorylate several substrates that trigger at least centrosome separation, Golgi dynamics, nuclear envelope breakdown and chromosome condensation. Once chromosomes are condensed and aligned at the metaphase plate, CDK1 activity is switched off by WEE1- and PKMYT1-mediated phosphorylation to allow sister chromatid separation, chromosome decondensation, reformation of the nuclear envelope and cytokinesis. Inactivated by PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage to stop cell cycle and genome replication at the G2 checkpoint thus facilitating DNA repair. Reactivated after successful DNA repair through WIP1-dependent signaling leading to CDC25A/B/C- mediated dephosphorylation and restoring cell cycle progression. In proliferating cells, CDK1-mediated FOXO1 phosphorylation at the G2-M phase represses FOXO1 interaction with 14-3-3 proteins and thereby promotes FOXO1 nuclear accumulation and transcription factor activity, leading to cell death of postmitotic neurons. The phosphorylation of beta-tubulins regulates microtubule dynamics during mitosis. NEDD1 phosphorylation promotes PLK1-mediated NEDD1 phosphorylation and subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. In addition, CC2D1A phosphorylation regulates CC2D1A spindle pole localization and association with SCC1/RAD21 and centriole cohesion during mitosis. The phosphorylation of Bcl- xL/BCL2L1 after prolongated G2 arrest upon DNA damage triggers apoptosis. In contrast, CASP8 phosphorylation during mitosis prevents its activation by proteolysis and subsequent apoptosis. This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. CALD1 phosphorylation promotes Schwann cell migration during peripheral nerve regeneration. CDK1-cyclin-B complex phosphorylates NCKAP5L and mediates its dissociation from centrosomes during mitosis (PubMed:26549230). {ECO:0000269|PubMed:16371510, ECO:0000269|PubMed:16407259, ECO:0000269|PubMed:16933150, ECO:0000269|PubMed:17459720, ECO:0000269|PubMed:18356527, ECO:0000269|PubMed:18480403, ECO:0000269|PubMed:19509060, ECO:0000269|PubMed:19917720, ECO:0000269|PubMed:20171170, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:20395957, ECO:0000269|PubMed:20935635, ECO:0000269|PubMed:20937773, ECO:0000269|PubMed:21063390, ECO:0000269|PubMed:26549230}.; . TISSUE SPECIFICITY: Isoform 2 is found in breast cancer tissues.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;breast;uterus;prostate;whole body;lung;cornea;synovium;bone;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland;bladder; superior cervical ganglion;fetal liver;testis;tumor;ciliary ganglion;atrioventricular node; 0.99999 0.82218 -0.09720619 46.20193442 3.23745 0.11657 CDK2 0.958299189494179 0.041680744569042 2.00659367791929e-05 cyclin-dependent kinase 2 FUNCTION: Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Interacts with cyclins A, B1, B3, D, or E. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT- mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization. Phosphorylates FOXP3 and negatively regulates its transcriptional activity and protein stability (By similarity). {ECO:0000250|UniProtKB:P97377, ECO:0000269|PubMed:10499802, ECO:0000269|PubMed:10884347, ECO:0000269|PubMed:10995386, ECO:0000269|PubMed:10995387, ECO:0000269|PubMed:11051553, ECO:0000269|PubMed:11113184, ECO:0000269|PubMed:15800615, ECO:0000269|PubMed:17495531, ECO:0000269|PubMed:18372919, ECO:0000269|PubMed:19966300, ECO:0000269|PubMed:20079829, ECO:0000269|PubMed:20147522, ECO:0000269|PubMed:20195506, ECO:0000269|PubMed:20935635, ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:21319273, ECO:0000269|PubMed:21596315}.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;brain;unclassifiable (Anatomical System);lymph node;trophoblast;heart;cartilage;tongue;muscle;adrenal cortex;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;kidney;caudate nucleus;trigeminal ganglion; 0.99998 0.86471 -0.163345027 41.24793583 38.64334 1.14510 CDK2AP1 0.74236102805821 0.246753667257514 0.0108853046842766 cyclin-dependent kinase 2 associated protein 1 FUNCTION: specific inhibitor of the cell-cycle kinase CDK2. {ECO:0000250}.; . . ovary;skin;retina;prostate;frontal lobe;cochlea;endometrium;iris;amniotic fluid;bladder;brain;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;bile duct;pancreas;lung;placenta;head and neck;kidney;stomach;aorta; spinal cord; 0.69677 0.15588 -0.031067188 51.03798066 6.69725 0.24693 CDK2AP2 0.25647477386357 0.640196285134751 0.103328941001679 cyclin-dependent kinase 2 associated protein 2 . . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;islets of Langerhans;pineal body;urinary;pharynx;blood;skeletal muscle;bile duct;pancreas;lung;cornea;epididymis;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach; liver;trigeminal ganglion; 0.47788 0.10817 0.101211609 60.95777306 6.04965 0.22887 CDK2AP2P1 . . . cyclin-dependent kinase 2 associated protein 2 pseudogene 1 . . . . . . . . . . . CDK2AP2P2 . . . cyclin-dependent kinase 2 associated protein 2 pseudogene 2 . . . . . . . . . . . CDK2AP2P3 . . . cyclin-dependent kinase 2 associated protein 2 pseudogene 3 . . . . . . . . . . . CDK3 0.000751722980772095 0.92408963566029 0.0751586413589383 cyclin-dependent kinase 3 FUNCTION: Serine/threonine-protein kinase that plays a critical role in the control of the eukaryotic cell cycle; involved in G0- G1 and G1-S cell cycle transitions. Interacts with CCNC/cyclin-C during interphase. Phosphorylates histone H1, ATF1, RB1 and CABLES1. ATF1 phosphorylation triggers ATF1 transactivation and transcriptional activities, and promotes cell proliferation and transformation. CDK3/cyclin-C mediated RB1 phosphorylation is required for G0-G1 transition. Promotes G1-S transition probably by contributing to the activation of E2F1, E2F2 and E2F3 in a RB1- independent manner. {ECO:0000269|PubMed:15084261, ECO:0000269|PubMed:18794154, ECO:0000269|PubMed:8846921}.; . TISSUE SPECIFICITY: Expressed in cancer cell lines and glioblastoma tissue. {ECO:0000269|PubMed:18794154}.; . . 0.96801 0.20777 -0.159704656 41.90846898 101.44848 2.18083 CDK4 0.93201691552067 0.0679691784012567 1.39060780734014e-05 cyclin-dependent kinase 4 FUNCTION: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. {ECO:0000269|PubMed:15241418, ECO:0000269|PubMed:18827403, ECO:0000269|PubMed:9003781}.; DISEASE: Melanoma, cutaneous malignant 3 (CMM3) [MIM:609048]: A malignant neoplasm of melanocytes, arising de novo or from a pre- existing benign nevus, which occurs most often in the skin but also may involve other sites. {ECO:0000269|PubMed:7652577, ECO:0000269|PubMed:8528263, ECO:0000269|PubMed:9311594, ECO:0000269|PubMed:9425228}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . ovary;salivary gland;adrenal medulla;intestine;colon;choroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;synovium;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;pharynx;blood;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;duodenum;alveolus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.99997 0.77439 -0.295622497 32.61972163 10.51106 0.38180 CDK4PS . . . cyclin-dependent kinase 4 pseudogene . . . . . . . . . . . CDK5 0.94751618934918 0.0524481164269854 3.56942238341685e-05 cyclin-dependent kinase 5 FUNCTION: Proline-directed serine/threonine-protein kinase essential for neuronal cell cycle arrest and differentiation and may be involved in apoptotic cell death in neuronal diseases by triggering abortive cell cycle re-entry. Interacts with D1 and D3- type G1 cyclins. Phosphorylates SRC, NOS3, VIM/vimentin, p35/CDK5R1, MEF2A, SIPA1L1, SH3GLB1, PXN, PAK1, MCAM/MUC18, SEPT5, SYN1, DNM1, AMPH, SYNJ1, CDK16, RAC1, RHOA, CDC42, TONEBP/NFAT5, MAPT/TAU, MAP1B, histone H1, p53/TP53, HDAC1, APEX1, PTK2/FAK1, huntingtin/HTT, ATM, MAP2, NEFH and NEFM. Regulates several neuronal development and physiological processes including neuronal survival, migration and differentiation, axonal and neurite growth, synaptogenesis, oligodendrocyte differentiation, synaptic plasticity and neurotransmission, by phosphorylating key proteins. Activated by interaction with CDK5R1 (p35) and CDK5R2 (p39), especially in post-mitotic neurons, and promotes CDK5R1 (p35) expression in an autostimulation loop. Phosphorylates many downstream substrates such as Rho and Ras family small GTPases (e.g. PAK1, RAC1, RHOA, CDC42) or microtubule-binding proteins (e.g. MAPT/TAU, MAP2, MAP1B), and modulates actin dynamics to regulate neurite growth and/or spine morphogenesis. Phosphorylates also exocytosis associated proteins such as MCAM/MUC18, SEPT5, SYN1, and CDK16/PCTAIRE1 as well as endocytosis associated proteins such as DNM1, AMPH and SYNJ1 at synaptic terminals. In the mature central nervous system (CNS), regulates neurotransmitter movements by phosphorylating substrates associated with neurotransmitter release and synapse plasticity; synaptic vesicle exocytosis, vesicles fusion with the presynaptic membrane, and endocytosis. Promotes cell survival by activating anti-apoptotic proteins BCL2 and STAT3, and negatively regulating of JNK3/MAPK10 activity. Phosphorylation of p53/TP53 in response to genotoxic and oxidative stresses enhances its stabilization by preventing ubiquitin ligase-mediated proteasomal degradation, and induces transactivation of p53/TP53 target genes, thus regulating apoptosis. Phosphorylation of p35/CDK5R1 enhances its stabilization by preventing calpain-mediated proteolysis producing p25/CDK5R1 and avoiding ubiquitin ligase-mediated proteasomal degradation. During aberrant cell-cycle activity and DNA damage, p25/CDK5 activity elicits cell-cycle activity and double-strand DNA breaks that precedes neuronal death by deregulating HDAC1. DNA damage triggered phosphorylation of huntingtin/HTT in nuclei of neurons protects neurons against polyglutamine expansion as well as DNA damage mediated toxicity. Phosphorylation of PXN reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation. Negative regulator of Wnt/beta-catenin signaling pathway. Activator of the GAIT (IFN-gamma-activated inhibitor of translation) pathway, which suppresses expression of a post-transcriptional regulon of proinflammatory genes in myeloid cells; phosphorylates the linker domain of glutamyl-prolyl tRNA synthetase (EPRS) in a IFN-gamma- dependent manner, the initial event in assembly of the GAIT complex. Phosphorylation of SH3GLB1 is required for autophagy induction in starved neurons. Phosphorylation of TONEBP/NFAT5 in response to osmotic stress mediates its rapid nuclear localization. MEF2 is inactivated by phosphorylation in nucleus in response to neurotoxin, thus leading to neuronal apoptosis. APEX1 AP-endodeoxyribonuclease is repressed by phosphorylation, resulting in accumulation of DNA damage and contributing to neuronal death. NOS3 phosphorylation down regulates NOS3-derived nitrite (NO) levels. SRC phosphorylation mediates its ubiquitin- dependent degradation and thus leads to cytoskeletal reorganization. May regulate endothelial cell migration and angiogenesis via the modulation of lamellipodia formation. Involved in dendritic spine morphogenesis by mediating the EFNA1- EPHA4 signaling. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer in association with altered stability and subcellular distribution. {ECO:0000269|PubMed:12393264, ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:15992363, ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:17121855, ECO:0000269|PubMed:17591690, ECO:0000269|PubMed:17611284, ECO:0000269|PubMed:17671990, ECO:0000269|PubMed:18042622, ECO:0000269|PubMed:19081376, ECO:0000269|PubMed:19693690, ECO:0000269|PubMed:20061803, ECO:0000269|PubMed:20213743, ECO:0000269|PubMed:20826806, ECO:0000269|PubMed:21209322, ECO:0000269|PubMed:21220307, ECO:0000269|PubMed:21442427, ECO:0000269|PubMed:21465480, ECO:0000269|PubMed:21499257, ECO:0000269|PubMed:24235147, ECO:0000269|PubMed:9822744}.; DISEASE: Lissencephaly 7, with cerebellar hypoplasia (LIS7) [MIM:616342]: A form of lissencephaly, a disorder of cortical development characterized by agyria or pachygyria and disorganization of the clear neuronal lamination of normal six- layered cortex. LIS7 patients manifest lack of psychomotor development, facial dysmorphism, arthrogryposis, and early-onset intractable seizures resulting in death in infancy. {ECO:0000269|PubMed:25560765}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed. Accumulates in cortical neurons (at protein level). Isoform 2 has only been detected in testis, skeletal muscle, colon, bone marrow and ovary. {ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:19693690}.; unclassifiable (Anatomical System);ovary;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;prostate;optic nerve;lung;frontal lobe;nasopharynx;macula lutea;liver;testis;brain;stomach; whole brain;amygdala;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.53284 0.56595 -0.031067188 51.03798066 4.73826 0.17305 CDK5PS . . . cyclin-dependent kinase 5 pseudogene . . . . . . . . . . . CDK5R1 0.738441122386799 0.250212258343078 0.0113466192701235 cyclin-dependent kinase 5, regulatory subunit 1 (p35) FUNCTION: p35 is a neuron specific activator of CDK5. The complex p35/CDK5 is required for neurite outgrowth and cortical lamination. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. Activator of TPKII. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer in association with altered stability and subcellular distribution. {ECO:0000269|PubMed:24235147}.; . TISSUE SPECIFICITY: Brain and neuron specific.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;hypothalamus;colon;fovea centralis;skeletal muscle;skin;uterus;whole body;lung;synovium;macula lutea;visual apparatus;hippocampus;liver;testis;brain; amygdala;whole brain;occipital lobe;superior cervical ganglion;medulla oblongata;temporal lobe;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.54497 0.18399 -0.141298762 42.87567823 4.68969 0.16820 CDK5R2 . . . cyclin-dependent kinase 5, regulatory subunit 2 (p39) FUNCTION: Activator of CDK5/TPKII.; . TISSUE SPECIFICITY: Brain and neuron specific.; unclassifiable (Anatomical System);islets of Langerhans;choroid;fovea centralis;lens;retina;optic nerve;lung;frontal lobe;hippocampus;macula lutea;testis;brain;cerebellum; amygdala;whole brain;superior cervical ganglion;subthalamic nucleus;medulla oblongata;thalamus;occipital lobe;temporal lobe;prefrontal cortex;pons;caudate nucleus;cingulate cortex; 0.44177 0.11161 . . 35.94 1.07912 CDK5RAP1 1.07824217963136e-14 0.0105148867885196 0.98948511321147 CDK5 regulatory subunit associated protein 1 FUNCTION: Specifically inhibits CDK5 activation by CDK5R1.; . TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:10721722}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;unclassifiable (Anatomical System);lymph node;muscle;pancreas;lung;cornea;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta;cerebellum; ciliary ganglion;trigeminal ganglion;parietal lobe; 0.10112 0.12410 -0.799052816 12.45576787 939.45075 5.94182 CDK5RAP2 5.70875541213003e-16 0.999965025824632 3.4974175366928e-05 CDK5 regulatory subunit associated protein 2 FUNCTION: Potential regulator of CDK5 activity via its interaction with CDK5R1. Negative regulator of centriole disengagement (licensing) which maintains centriole engagement and cohesion. Involved in regulation of mitotic spindle orientation (By similarity). Plays a role in the spindle checkpoint activation by acting as a transcriptional regulator of both BUBR1 and MAD2 promoter. Together with MAPRE1, it may promote microtubule polymerization, bundle formation, growth and dynamics at the plus ends. Regulates centrosomal maturation by recruitment of a gamma- tubulin ring complex onto centrosomes (PubMed:26485573). {ECO:0000250|UniProtKB:Q8K389, ECO:0000269|PubMed:17959831, ECO:0000269|PubMed:18042621, ECO:0000269|PubMed:19282672, ECO:0000269|PubMed:19553473, ECO:0000269|PubMed:26485573}.; DISEASE: Microcephaly 3, primary, autosomal recessive (MCPH3) [MIM:604804]: A disease defined as a head circumference more than 3 standard deviations below the age-related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. Despite this marked reduction in size, the gyral pattern is relatively well preserved, with no major abnormality in cortical architecture. Affected individuals are mentally retarded. Primary microcephaly is further defined by the absence of other syndromic features or significant neurological deficits due to degenerative brain disorder. {ECO:0000269|PubMed:15793586}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:10721722}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;germinal center;spinal ganglion;brain;artery;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; superior cervical ganglion;testis - interstitial;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.03779 0.08467 -1.951619288 1.869544704 868.61481 5.74153 CDK5RAP3 2.8653949299435e-12 0.138474787412978 0.861525212584157 CDK5 regulatory subunit associated protein 3 FUNCTION: Probable tumor suppressor initially identified as a CDK5R1 interactor controlling cell proliferation (PubMed:12054757, PubMed:12737517). Negatively regulates NF-kappa-B-mediated gene transcription through the control of RELA phosphorylation (PubMed:17785205, PubMed:20228063). Also regulates mitotic G2/M transition checkpoint and mitotic G2 DNA damage checkpoint (PubMed:15790566, PubMed:19223857). Through its interaction with CDKN2A/ARF and MDM2 may induce MDM2-dependent p53/TP53 ubiquitination, stabilization and activation in the nucleus, thereby promoting G1 cell cycle arrest and inhibition of cell proliferation (PubMed:16173922). May play a role in the unfolded protein response, mediating the ufmylation of multiple proteins in response to endoplasmic reticulum stress (PubMed:23152784). May also play a role in the rupture of the nuclear envelope during apoptosis (PubMed:23478299). May regulate MAPK14 activity by regulating its dephosphorylation by PPM1D/WIP1 (PubMed:21283629). {ECO:0000269|PubMed:12054757, ECO:0000269|PubMed:12737517, ECO:0000269|PubMed:15790566, ECO:0000269|PubMed:16173922, ECO:0000269|PubMed:17785205, ECO:0000269|PubMed:19223857, ECO:0000269|PubMed:20228063, ECO:0000269|PubMed:21283629, ECO:0000269|PubMed:23152784, ECO:0000269|PubMed:23478299}.; . TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:12054757, PubMed:10721722). Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Isoform 3 is expressed in kidney, liver, skeletal muscle and placenta (PubMed:12737517). {ECO:0000269|PubMed:10721722, ECO:0000269|PubMed:12054757, ECO:0000269|PubMed:12737517}.; ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;cartilage;tongue;pineal body;pharynx;blood;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;cerebellum; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;testis;caudate nucleus; 0.22673 0.12287 0.622829232 83.47487615 584.11515 4.90058 CDK6 0.923677276455166 0.0762306647005339 9.20588443003271e-05 cyclin-dependent kinase 6 FUNCTION: Serine/threonine-protein kinase involved in the control of the cell cycle and differentiation; promotes G1/S transition. Phosphorylates pRB/RB1 and NPM1. Interacts with D-type G1 cyclins during interphase at G1 to form a pRB/RB1 kinase and controls the entrance into the cell cycle. Involved in initiation and maintenance of cell cycle exit during cell differentiation; prevents cell proliferation and regulates negatively cell differentiation, but is required for the proliferation of specific cell types (e.g. erythroid and hematopoietic cells). Essential for cell proliferation within the dentate gyrus of the hippocampus and the subventricular zone of the lateral ventricles. Required during thymocyte development. Promotes the production of newborn neurons, probably by modulating G1 length. Promotes, at least in astrocytes, changes in patterns of gene expression, changes in the actin cytoskeleton including loss of stress fibers, and enhanced motility during cell differentiation. Prevents myeloid differentiation by interfering with RUNX1 and reducing its transcription transactivation activity, but promotes proliferation of normal myeloid progenitors. Delays senescence. Promotes the proliferation of beta-cells in pancreatic islets of Langerhans. May play a role in the centrosome organization during the cell cycle phases (PubMed:23918663). {ECO:0000269|PubMed:12833137, ECO:0000269|PubMed:14985467, ECO:0000269|PubMed:15254224, ECO:0000269|PubMed:15809340, ECO:0000269|PubMed:17420273, ECO:0000269|PubMed:17431401, ECO:0000269|PubMed:20333249, ECO:0000269|PubMed:20668294, ECO:0000269|PubMed:23918663, ECO:0000269|PubMed:8114739}.; DISEASE: Microcephaly 12, primary, autosomal recessive (MCPH12) [MIM:616080]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age- related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. {ECO:0000269|PubMed:23918663}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed ubiquitously. Accumulates in squamous cell carcinomas, proliferating hematopoietic progenitor cells, beta-cells of pancreatic islets of Langerhans, and neuroblastomas. Reduced levels in differentiating cells. {ECO:0000269|PubMed:20668294, ECO:0000269|PubMed:8114739}.; umbilical cord;ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;spinal cord;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; testis; 0.99538 0.40044 0.193034296 66.82000472 15.47446 0.55417 CDK7 0.00161852539016363 0.970241998277212 0.028139476332624 cyclin-dependent kinase 7 FUNCTION: Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Cyclin- dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Phosphorylation of POLR2A in complex with DNA promotes transcription initiation by triggering dissociation from DNA. Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition. {ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:11113184, ECO:0000269|PubMed:16327805, ECO:0000269|PubMed:17373709, ECO:0000269|PubMed:17386261, ECO:0000269|PubMed:17901130, ECO:0000269|PubMed:19015234, ECO:0000269|PubMed:19071173, ECO:0000269|PubMed:19136461, ECO:0000269|PubMed:19450536, ECO:0000269|PubMed:19667075, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:9372954, ECO:0000269|PubMed:9840937}.; . TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;breast;pia mater;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; . 0.69632 0.48758 0.058937498 58.26256192 93.09514 2.07428 CDK7PS . . . cyclin-dependent kinase 7 pseudogene . . . . . . . . . . . CDK8 0.946653349022173 0.053346342372358 3.08605468826832e-07 cyclin-dependent kinase 8 FUNCTION: Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex. Phosphorylates CCNH leading to down-regulation of the TFIIH complex and transcriptional repression. Recruited through interaction with MAML1 to hyperphosphorylate the intracellular domain of NOTCH, leading to its degradation. {ECO:0000269|PubMed:10993082, ECO:0000269|PubMed:15546612}.; . . . . 0.83531 0.20297 -0.251530012 35.42108988 6.69941 0.24716 CDK8PS . . . cyclin-dependent kinase 8 pseudogene . . . . . . . . . . . CDK9 0.000275105560710601 0.785487886318718 0.214237008120571 cyclin-dependent kinase 9 FUNCTION: Protein kinase involved in the regulation of transcription. Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP. This complex is inactive when in the 7SK snRNP complex form. Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR, and the negative elongation factors DSIF and NELF. Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e.g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3 signaling). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis. P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export. Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing. The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro. Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single- stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage. In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6. Promotes cardiac myocyte enlargement. RPB1/POLR2A phosphorylation on 'Ser-2' in CTD activates transcription. AR phosphorylation modulates AR transcription factor promoter selectivity and cell growth. DSIF and NELF phosphorylation promotes transcription by inhibiting their negative effect. The phosphorylation of MYOD1 enhances its transcriptional activity and thus promotes muscle differentiation. {ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:10574912, ECO:0000269|PubMed:10757782, ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11112772, ECO:0000269|PubMed:11145967, ECO:0000269|PubMed:11575923, ECO:0000269|PubMed:11809800, ECO:0000269|PubMed:11884399, ECO:0000269|PubMed:12037670, ECO:0000269|PubMed:14701750, ECO:0000269|PubMed:15564463, ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:16109377, ECO:0000269|PubMed:17956865, ECO:0000269|PubMed:18362169, ECO:0000269|PubMed:19575011, ECO:0000269|PubMed:19844166, ECO:0000269|PubMed:20081228, ECO:0000269|PubMed:20493174, ECO:0000269|PubMed:20930849, ECO:0000269|PubMed:20980437, ECO:0000269|PubMed:21127351, ECO:0000269|PubMed:9857195}.; DISEASE: Note=Chronic activation of CDK9 causes cardiac myocyte enlargement leading to cardiac hypertrophy, and confers predisposition to heart failure.; TISSUE SPECIFICITY: Ubiquitous.; . . 0.51278 0.35859 -0.582225231 18.44184949 9.01961 0.33070 CDK10 2.3367075460824e-10 0.134696808757945 0.865303191008384 cyclin-dependent kinase 10 FUNCTION: Cyclin-dependent kinase that phosphorylates the transcription factor ETS2 (in vitro) and positively controls its proteasomal degradation (in cells). {ECO:0000269|PubMed:24218572}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;muscle;urinary;adrenal cortex;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;liver;trigeminal ganglion;skeletal muscle; 0.17840 . 0.066214104 58.95848077 89.14865 2.02834 CDK11A 5.23535259576534e-05 0.96797697651184 0.0319706699622026 cyclin-dependent kinase 11A FUNCTION: Appears to play multiple roles in cell cycle progression, cytokinesis and apoptosis. The p110 isoforms have been suggested to be involved in pre-mRNA splicing, potentially by phosphorylating the splicing protein SFRS7. The p58 isoform may act as a negative regulator of normal cell cycle progression. {ECO:0000269|PubMed:12501247, ECO:0000269|PubMed:12624090}.; . TISSUE SPECIFICITY: Expressed ubiquitously. Some evidence of isoform-specific tissue distribution. {ECO:0000269|PubMed:8195233, ECO:0000269|PubMed:9750192}.; lymphoreticular;ovary;foreskin;colon;skin;retina;bone marrow;uterus;prostate;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;epidermis;tongue;islets of Langerhans;blood;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;amnion;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;heart;testis;white blood cells;trigeminal ganglion;skeletal muscle;parietal lobe; . 0.14135 . . 5998.47991 16.15546 CDK11B 0.72829443952872 0.271588478407017 0.000117082064263447 cyclin-dependent kinase 11B FUNCTION: Appears to play multiple roles in cell cycle progression, cytokinesis and apoptosis. The p110 isoforms have been suggested to be involved in pre-mRNA splicing, potentially by phosphorylating the splicing protein SFRS7. The p58 isoform may act as a negative regulator of normal cell cycle progression. {ECO:0000269|PubMed:12501247, ECO:0000269|PubMed:12624090, ECO:0000269|PubMed:2217177}.; . TISSUE SPECIFICITY: Expressed ubiquitously. Some evidence of isoform-specific tissue distribution. {ECO:0000269|PubMed:8195233, ECO:0000269|PubMed:9750192}.; lymphoreticular;ovary;foreskin;colon;skin;bone marrow;uterus;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;bladder;brain;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;epidermis;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;amnion;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;heart;testis;white blood cells;trigeminal ganglion;skeletal muscle;parietal lobe; . 0.14135 . . 147.53387 2.64628 CDK12 0.999991812947639 8.18705236060111e-06 7.22663664170294e-16 cyclin-dependent kinase 12 FUNCTION: Cyclin-dependent kinase that phosphorylates the C- terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors. {ECO:0000269|PubMed:11683387, ECO:0000269|PubMed:19651820, ECO:0000269|PubMed:20952539, ECO:0000269|PubMed:22012619, ECO:0000269|PubMed:24662513}.; DISEASE: Note=Chromosomal aberrations involving CDK12 may be a cause gastric cancer. Deletions within 17q12 region producing fusion transcripts with ERBB2, leading to CDK12-ERBB2 fusion leading to trunctated CDK12 protein not in-frame with ERBB2.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11683387}.; . . 0.58820 0.16128 -1.168429872 6.062750649 241.23657 3.35492 CDK13 0.751250538151318 0.2487494556434 6.20528162358449e-09 cyclin-dependent kinase 13 FUNCTION: Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys- 51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef. {ECO:0000269|PubMed:16721827, ECO:0000269|PubMed:1731328, ECO:0000269|PubMed:18480452, ECO:0000269|PubMed:20952539}.; . TISSUE SPECIFICITY: Expressed in fetal brain, liver, muscle and in adult brain. Also expressed in neuroblastoma and glioblastoma tumors.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;tongue;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;subthalamic nucleus;testis - interstitial;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;cerebellum; 0.25758 0.22620 -1.080231599 7.277659825 1273.10966 6.72022 CDK14 0.476260128391186 0.523524240267732 0.000215631341081727 cyclin-dependent kinase 14 FUNCTION: Serine/threonine-protein kinase involved in the control of the eukaryotic cell cycle, whose activity is controlled by an associated cyclin. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by mediating the phosphorylation of LRP6 at 'Ser-1490', leading to the activation of the Wnt signaling pathway. Acts as a regulator of cell cycle progression and cell proliferation via its interaction with CCDN3. Phosphorylates RB1 in vitro, however the relevance of such result remains to be confirmed in vivo. May also play a role in meiosis, neuron differentiation and may indirectly act as a negative regulator of insulin-responsive glucose transport. {ECO:0000269|PubMed:16461467, ECO:0000269|PubMed:17517622, ECO:0000269|PubMed:19524571, ECO:0000269|PubMed:20059949}.; . TISSUE SPECIFICITY: Highly expressed in brain, pancreas, kidney, heart, testis and ovary. Also detected at lower levels in other tissues except in spleen and thymus where expression is barely detected. {ECO:0000269|PubMed:11313143}.; fovea centralis;choroid;retina;bone marrow;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;stomach; amygdala;dorsal root ganglion;medulla oblongata;superior cervical ganglion;occipital lobe;subthalamic nucleus;prefrontal cortex;globus pallidus;pons;parietal lobe;cingulate cortex; 0.45755 0.11073 -0.514264485 21.41424864 102.95947 2.19295 CDK15 5.05622865918498e-13 0.0271695700622667 0.972830429937228 cyclin-dependent kinase 15 FUNCTION: Serine/threonine-protein kinase that acts like an antiapoptotic protein that counters TRAIL/TNFSF10-induced apoptosis by inducing phosphorylation of BIRC5 at 'Thr-34'. {ECO:0000269|PubMed:24866247}.; . . unclassifiable (Anatomical System);testis;kidney; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;temporal lobe;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16207 0.08286 -0.023789244 52.09365416 171.90123 2.85972 CDK16 0.995702615689421 0.00429701372147499 3.70589103477667e-07 cyclin-dependent kinase 16 FUNCTION: Protein kinase that plays a role in vesicle-mediated transport processes and exocytosis. Regulates GH1 release by brain neurons. Phosphorylates NSF, and thereby regulates NSF oligomerization. Required for normal spermatogenesis. Regulates neuron differentiation and dendrite development (By similarity). Plays a role in the regulation of insulin secretion in response to changes in blood glucose levels. Can phosphorylate CCNY at 'Ser- 336' (in vitro). {ECO:0000250, ECO:0000269|PubMed:22184064, ECO:0000269|PubMed:22796189, ECO:0000269|PubMed:22798068}.; . TISSUE SPECIFICITY: Detected in pancreas islets (at protein level). Detected in brain and pancreas. {ECO:0000269|PubMed:22798068}.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;amygdala;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;cerebellum; thalamus;superior cervical ganglion;cerebellum peduncles;prefrontal cortex;globus pallidus;pons;trigeminal ganglion;skeletal muscle;cingulate cortex;cerebellum; 0.32991 0.14960 0.082802743 60.09082331 449.04533 4.40678 CDK17 0.988843485373774 0.0111564829459831 3.16802428517887e-08 cyclin-dependent kinase 17 FUNCTION: May play a role in terminally differentiated neurons. Has a Ser/Thr-phosphorylating activity for histone H1 (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;colon;parathyroid;vein;skin;retina;endometrium;thyroid;bone;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);amygdala;meninges;lymph node;heart;blood;pancreas;pia mater;lung;placenta;hippocampus;liver;head and neck;kidney;mammary gland;stomach;aorta;cerebellum; amygdala;whole brain;dorsal root ganglion;occipital lobe;medulla oblongata;superior cervical ganglion;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;trigeminal ganglion;parietal lobe;cingulate cortex; 0.20942 0.14229 -0.514264485 21.41424864 26.55309 0.85822 CDK18 7.15896735407714e-08 0.692723340806217 0.307276587604109 cyclin-dependent kinase 18 FUNCTION: May play a role in signal transduction cascades in terminally differentiated cells.; . TISSUE SPECIFICITY: Isoform 3 expression is limited to several subcortical nuclei of the basal gangli and the spinal cord. Isoform 2 is widely expressed. {ECO:0000269|PubMed:15019984}.; unclassifiable (Anatomical System);myocardium;lymph node;frontal lobe;ovary;endometrium;visual apparatus;hippocampus;brain;skin;retina; medulla oblongata;thalamus;occipital lobe;spinal cord;prefrontal cortex;cingulate cortex;parietal lobe; 0.32808 0.13832 0.198490371 67.30360934 867.92025 5.73904 CDK19 0.99801709140742 0.00198289723141767 1.13611623159951e-08 cyclin-dependent kinase 19 . . . unclassifiable (Anatomical System);lung;frontal lobe;testis;colon;skin; dorsal root ganglion;amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;testis - interstitial;hypothalamus;spinal cord;caudate nucleus;atrioventricular node;pons;skeletal muscle;prostate;subthalamic nucleus;uterus corpus;fetal brain;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.57977 0.08498 -0.229483771 36.86010852 12.58509 0.45935 CDK20 7.19398847298015e-12 0.00949563102811231 0.990504368964694 cyclin-dependent kinase 20 FUNCTION: Required for high-level Shh responses in the developing neural tube. Together with TBC1D32, controls the structure of the primary cilium by coordinating assembly of the ciliary membrane and axoneme, allowing GLI2 to be properly activated in response to SHH signaling (By similarity). Involved in cell growth. Activates CDK2, a kinase involved in the control of the cell cycle, by phosphorylating residue 'Thr-160'. {ECO:0000250, ECO:0000269|PubMed:14597612}.; . . unclassifiable (Anatomical System);ovary;hypothalamus;parathyroid;skin;retina;uterus;prostate;lung;frontal lobe;endometrium;adrenal gland;placenta;thyroid;visual apparatus;hippocampus;testis;spleen;kidney;brain;pineal gland;gall bladder; superior cervical ganglion;testis;trigeminal ganglion; 0.18461 0.10522 -0.554717505 19.79830149 58.03541 1.54034 CDKAL1 0.577650480843115 0.422329920579637 1.95985772472756e-05 CDK5 regulatory subunit associated protein 1 like 1 FUNCTION: Catalyzes the methylthiolation of N6- threonylcarbamoyladenosine (t(6)A), leading to the formation of 2- methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine. {ECO:0000269|PubMed:20584901}.; . TISSUE SPECIFICITY: Expressed in pancreatic islets. {ECO:0000269|PubMed:23048041}.; unclassifiable (Anatomical System);prostate;lung;frontal lobe;ovary;heart;nasopharynx;bone;visual apparatus;colon;germinal center;brain;mammary gland;skeletal muscle; superior cervical ganglion;trigeminal ganglion; 0.23384 0.24681 -0.578583623 18.71903751 656.55651 5.13753 CDKL1 3.60337409896438e-05 0.819752959432031 0.180211006826979 cyclin dependent kinase like 1 . . TISSUE SPECIFICITY: Highly expressed in kidney, and to a lower extent in ovary. {ECO:0000269|PubMed:9000130}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;hypothalamus;parathyroid;lens;skin;skeletal muscle;uterus;lung;frontal lobe;bone;liver;testis;head and neck;cervix;germinal center;kidney; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;uterus corpus;ovary;trachea;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.19022 . 0.595326758 82.66100495 291.44464 3.65136 CDKL2 1.86965524979377e-09 0.227336452342649 0.772663545787696 cyclin dependent kinase like 2 . . TISSUE SPECIFICITY: Expressed in testis and kidney, and at lower level in brain and lung. {ECO:0000269|PubMed:9000130}.; lung;frontal lobe;nasopharynx;thyroid;testis;skeletal muscle; dorsal root ganglion;superior cervical ganglion;medulla oblongata;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09938 0.17829 -0.069700724 48.54328851 158.42474 2.74960 CDKL3 4.32898502493702e-07 0.600309181846894 0.399690385254604 cyclin dependent kinase like 3 . . . unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;whole body;lung;macula lutea;testis;kidney;brain; testis; 0.18586 0.10438 0.328949044 73.41354093 99.29071 2.15668 CDKL4 3.68817176201996e-08 0.188047455466537 0.811952507651745 cyclin dependent kinase like 4 . . . . . 0.09335 0.08693 0.040529541 57.15380986 224.2135 3.23776 CDKL5 0.997790054805334 0.00220994220008243 2.99458398577151e-09 cyclin dependent kinase like 5 FUNCTION: Mediates phosphorylation of MECP2. {ECO:0000269|PubMed:15917271, ECO:0000269|PubMed:16935860}.; DISEASE: Note=Chromosomal aberrations involving CDKL5 are found in patients manifesting early-onset seizures and spams and psychomotor impairment. Translocation t(X;6)(p22.3;q14); translocation t(X;7)(p22.3;p15).; DISEASE: Epileptic encephalopathy, early infantile, 2 (EIEE2) [MIM:300672]: A severe form of epilepsy characterized by seizures or spasms beginning in infancy. Patients with epileptic encephalopathy early infantile type 2 manifest features resembling Rett syndrome such as microcephaly, lack of speech development, stereotypic hand movements. However, EIEE2 and Rett syndrome are considered two distinct entities. {ECO:0000269|PubMed:12736870, ECO:0000269|PubMed:15492925, ECO:0000269|PubMed:15499549, ECO:0000269|PubMed:15689447, ECO:0000269|PubMed:15917271, ECO:0000269|PubMed:16015284, ECO:0000269|PubMed:16611748, ECO:0000269|PubMed:17993579, ECO:0000269|PubMed:18790821, ECO:0000269|PubMed:18809835, ECO:0000269|PubMed:19241098, ECO:0000269|PubMed:19253388, ECO:0000269|PubMed:24564546}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, lung, kidney, prostate, ovary, placenta, pancreas and testis.; . . 0.49775 . -0.666770504 15.86459071 140.81183 2.58907 CDKN1A 0.0272025507564846 0.793751812029109 0.179045637214406 cyclin-dependent kinase inhibitor 1A FUNCTION: May be the important intermediate by which p53/TP53 mediates its role as an inhibitor of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin- dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D- CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex. {ECO:0000269|PubMed:8242751, ECO:0000269|PubMed:9106657}.; . TISSUE SPECIFICITY: Expressed in all adult tissues, with 5-fold lower levels observed in the brain.; smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;larynx;bone;thyroid;iris;testis;amniotic fluid;brain;unclassifiable (Anatomical System);cartilage;small intestine;heart;islets of Langerhans;lens;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;alveolus;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; ciliary ganglion; 0.96907 0.09080 0.461228372 78.46190139 899.40808 5.84095 CDKN1A-AS1 . . . CDKN1A antisense RNA 1 . . . . . . . . . . . CDKN1B 0.847005306213341 0.150302052621055 0.00269264116560331 cyclin-dependent kinase inhibitor 1B FUNCTION: Important regulator of cell cycle progression. Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1- CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry. {ECO:0000269|PubMed:10831586, ECO:0000269|PubMed:12244301, ECO:0000269|PubMed:16782892, ECO:0000269|PubMed:17254966, ECO:0000269|PubMed:19075005}.; DISEASE: Multiple endocrine neoplasia 4 (MEN4) [MIM:610755]: Multiple endocrine neoplasia (MEN) syndromes are inherited cancer syndromes of the thyroid. MEN4 is a MEN-like syndrome with a phenotypic overlap of both MEN1 and MEN2. {ECO:0000269|PubMed:17030811}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues tested. Highest levels in skeletal muscle, lowest in liver and kidney.; ovary;sympathetic chain;skin;retina;prostate;cochlea;endometrium;thyroid;germinal center;bladder;brain;ciliary body;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;aorta;stomach;thymus;cerebellum; whole brain;cerebellum peduncles;cerebellum; 0.80863 0.68893 -0.005381972 53.50908233 2616.41863 9.58079 CDKN1C 0.522821690107795 0.413754231203942 0.063424078688263 cyclin-dependent kinase inhibitor 1C FUNCTION: Potent tight-binding inhibitor of several G1 cyclin/CDK complexes (cyclin E-CDK2, cyclin D2-CDK4, and cyclin A-CDK2) and, to lesser extent, of the mitotic cyclin B-CDC2. Negative regulator of cell proliferation. May play a role in maintenance of the non- proliferative state throughout life.; DISEASE: Beckwith-Wiedemann syndrome (BWS) [MIM:130650]: A disorder characterized by anterior abdominal wall defects including exomphalos (omphalocele), pre- and postnatal overgrowth, and macroglossia. Additional less frequent complications include specific developmental defects and a predisposition to embryonal tumors. {ECO:0000269|PubMed:10424811}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Intrauterine growth retardation, metaphyseal dysplasia, adrenal hypoplasia congenita, and genital anomalies (IMAGE) [MIM:614732]: A rare condition characterized by intrauterine growth restriction, metaphyseal dysplasia, congenital adrenal hypoplasia, and genital anomalies. Patients with this condition may present shortly after birth with severe adrenal insufficiency, which can be life-threatening if not recognized early and commenced on steroid replacement therapy. Other reported features in this condition include, hypercalciuria and/or hypercalcemia, craniosynostosis, cleft palate, and scoliosis. {ECO:0000269|PubMed:22634751}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the heart, brain, lung, skeletal muscle, kidney, pancreas and testis. Expressed in the eye. High levels are seen in the placenta while low levels are seen in the liver. {ECO:0000269|PubMed:22634751}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;olfactory bulb;adrenal gland;placenta;spinal cord;trigeminal ganglion;parietal lobe; 0.74963 . . . 1380.49227 6.96159 CDKN2A 0.357648776382819 0.589844509816247 0.0525067138009338 cyclin-dependent kinase inhibitor 2A FUNCTION: Acts as a negative regulator of the proliferation of normal cells by interacting strongly with CDK4 and CDK6. This inhibits their ability to interact with cyclins D and to phosphorylate the retinoblastoma protein. {ECO:0000269|PubMed:16782892, ECO:0000269|PubMed:7972006}.; DISEASE: Note=The association between cutaneous and uveal melanomas in some families suggests that mutations in CDKN2A may account for a proportion of uveal melanomas. However, CDKN2A mutations are rarely found in uveal melanoma patients.; DISEASE: Melanoma, cutaneous malignant 2 (CMM2) [MIM:155601]: A malignant neoplasm of melanocytes, arising de novo or from a pre- existing benign nevus, which occurs most often in the skin but also may involve other sites. {ECO:0000269|PubMed:10651484, ECO:0000269|PubMed:10874641, ECO:0000269|PubMed:11506491, ECO:0000269|PubMed:12019208, ECO:0000269|PubMed:14646619, ECO:0000269|PubMed:19260062, ECO:0000269|PubMed:7987387, ECO:0000269|PubMed:8595405, ECO:0000269|PubMed:8653684, ECO:0000269|PubMed:8710906, ECO:0000269|PubMed:9328469, ECO:0000269|PubMed:9425228}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Familial atypical multiple mole melanoma-pancreatic carcinoma syndrome (FAMMMPC) [MIM:606719]: An inherited cancer predisposition syndrome characterized by an increased risk of developing malignant melanoma and/or pancreatic cancer. Mutation carriers within families may develop either or both types of cancer. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Li-Fraumeni syndrome (LFS) [MIM:151623]: Autosomal dominant familial cancer syndrome that in its classic form is defined by the existence of a proband affected by a sarcoma before 45 years with a first degree relative affected by any tumor before 45 years and another first degree relative with any tumor before 45 years or a sarcoma at any age. Other clinical definitions for LFS have been proposed (PubMed:8118819 and PubMed:8718514) and called Li-Fraumeni like syndrome (LFL). In these families affected relatives develop a diverse set of malignancies at unusually early ages. Four types of cancers account for 80% of tumors occurring in TP53 germline mutation carriers: breast cancers, soft tissue and bone sarcomas, brain tumors (astrocytomas) and adrenocortical carcinomas. Less frequent tumors include choroid plexus carcinoma or papilloma before the age of 15, rhabdomyosarcoma before the age of 5, leukemia, Wilms tumor, malignant phyllodes tumor, colorectal and gastric cancers. {ECO:0000269|PubMed:10484981}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Melanoma-astrocytoma syndrome (MASTS) [MIM:155755]: Characterized by a dual predisposition to melanoma and neural system tumors, commonly astrocytoma. {ECO:0000269|PubMed:11136714}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed but not detected in brain or skeletal muscle. Isoform 3 is pancreas-specific. {ECO:0000269|PubMed:10445844}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;optic nerve;bone;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;urinary;pharynx;blood;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.03037 0.06846 0.725794416 85.98136353 20.60127 0.70067 CDKN2A-AS1 . . . CDKN2A antisense RNA 1 (head to head) . . . . . . . . . . . CDKN2AIP 0.987251415538184 0.012743285406404 5.2990554122193e-06 CDKN2A interacting protein FUNCTION: Regulates DNA damage response in a dose-dependent manner through a number of signaling pathways involved in cell proliferation, apoptosis and senescence. {ECO:0000269|PubMed:15109303, ECO:0000269|PubMed:24825908}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12581788}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland; skeletal muscle; 0.66693 0.09860 -0.490397599 22.50530786 3844.49248 12.21656 CDKN2AIPNL 0.0582451914681328 0.713222648440013 0.228532160091854 CDKN2A interacting protein N-terminal like . . . . . 0.12159 0.09990 0.057118534 57.99716914 5.07933 0.18763 CDKN2AIPNLP1 . . . CDKN2A interacting protein N-terminal like pseudogene 1 . . . . . . . . . . . CDKN2AIPNLP2 . . . CDKN2A interacting protein N-terminal like pseudogene 2 . . . unclassifiable (Anatomical System);lymphoreticular;cartilage;ovary;lacrimal gland;blood;skin;bone marrow;lung;endometrium;placenta;bone;visual apparatus;testis;spleen;kidney;brain;mammary gland; . 0.12159 . . . . . CDKN2AIPNLP3 . . . CDKN2A interacting protein N-terminal like pseudogene 3 . . . . . . . . . . . CDKN2B 0.281057556695991 0.63135593408986 0.0875865092141492 cyclin-dependent kinase inhibitor 2B FUNCTION: Interacts strongly with CDK4 and CDK6. Potent inhibitor. Potential effector of TGF-beta induced cell cycle arrest.; . TISSUE SPECIFICITY: Isoform 2 is expressed in normal (keratinocytes, fibroblasts) and tumor cell lines. {ECO:0000269|PubMed:9230210}.; unclassifiable (Anatomical System);cartilage;ovary;urinary;colon;parathyroid;skin;skeletal muscle;breast;uterus;pancreas;prostate;lung;placenta;amnion;hypopharynx;liver;testis;cervix;head and neck;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.50224 0.40590 0.103030231 61.2762444 7.72261 0.28494 CDKN2B-AS1 . . . CDKN2B antisense RNA 1 . . . . . . . . . . . CDKN2C 0.315707026353853 0.614813508667862 0.069479464978285 cyclin-dependent kinase inhibitor 2C FUNCTION: Interacts strongly with CDK6, weakly with CDK4. Inhibits cell growth and proliferation with a correlated dependence on endogenous retinoblastoma protein RB.; . TISSUE SPECIFICITY: Highest levels found in skeletal muscle. Also found in pancreas and heart.; lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;stomach; superior cervical ganglion;adipose tissue;globus pallidus;ciliary ganglion;skeletal muscle; 0.82580 0.23021 0.058937498 58.26256192 26.23471 0.84984 CDKN2D 0.147286959437682 0.631278458766658 0.221434581795659 cyclin-dependent kinase inhibitor 2D FUNCTION: Interacts strongly with CDK4 and CDK6 and inhibits them. {ECO:0000269|PubMed:7739548, ECO:0000269|PubMed:8741839}.; . . unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;colon;substantia nigra;blood;skin;retina;bone marrow;prostate;whole body;lung;bone;placenta;hypopharynx;liver;testis;head and neck;spleen;germinal center;brain;cerebellum; amygdala;superior cervical ganglion;fetal brain; 0.26517 0.18055 -0.031067188 51.03798066 5.86886 0.22115 CDKN3 0.0662974565528495 0.919285587459009 0.0144169559881409 cyclin-dependent kinase inhibitor 3 FUNCTION: May play a role in cell cycle regulation. Dual specificity phosphatase active toward substrates containing either phosphotyrosine or phosphoserine residues. Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner. {ECO:0000269|PubMed:7569954, ECO:0000269|PubMed:8127873, ECO:0000269|PubMed:8242750}.; DISEASE: Hepatocellular carcinoma (HCC) [MIM:114550]: A primary malignant neoplasm of epithelial liver cells. The major risk factors for HCC are chronic hepatitis B virus (HBV) infection, chronic hepatitis C virus (HCV) infection, prolonged dietary aflatoxin exposure, alcoholic cirrhosis, and cirrhosis due to other causes. {ECO:0000269|PubMed:10987270}. Note=The gene represented in this entry may be involved in disease pathogenesis.; . ovary;salivary gland;intestine;colon;vein;skin;uterus;prostate;whole body;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;adrenal cortex;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; testis - interstitial;testis - seminiferous tubule;testis;tumor;skeletal muscle; 0.58572 0.13525 -0.185391282 39.67916962 18.98713 0.65524 CDL1 . . . Cornelia de Lange syndrome 1 . . . . . . . . . . . CDL2 . . . Cornelia de Lange syndrome 2 . . . . . . . . . . . CDNF 0.000111034121691279 0.371424174255463 0.628464791622845 cerebral dopamine neurotrophic factor FUNCTION: Trophic factor for dopamine neurons. Prevents the 6- hydroxydopamine (6-OHDA)-induced degeneration of dopaminergic neurons. When administered after 6-OHDA-lesioning, restores the dopaminergic function and prevents the degeneration of dopaminergic neurons in substantia nigra (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed in neuronal and non-neuronal tissues. In the brain, highest levels in the optic nerve and corpus callosum. {ECO:0000269|PubMed:17611540}.; . . 0.11747 0.12571 0.104848986 61.49445624 194.57877 3.02409 CDO1 0.0200728003981878 0.903158190602139 0.0767690089996728 cysteine dioxygenase type 1 FUNCTION: Initiates several important metabolic pathways related to pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. Critical regulator of cellular cysteine concentrations. Has an important role in maintaining the hepatic concentation of intracellular free cysteine within a proper narrow range.; . TISSUE SPECIFICITY: Highly expressed in liver and placenta. Low expression in heart, brain and pancreas. Also detected in hepatoblastoma Hep-G2 cells. {ECO:0000269|PubMed:10427686}.; ovary;developmental;parathyroid;choroid;skin;retina;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;testis;germinal center;brain;artery;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta; amygdala;dorsal root ganglion;superior cervical ganglion;fetal liver;adipose tissue;ciliary ganglion;atrioventricular node; 0.25046 0.24306 -0.163345027 41.24793583 23.32434 0.77860 CDON 3.04906879944482e-12 0.969409275381 0.030590724615951 cell adhesion associated, oncogene regulated FUNCTION: Component of a cell-surface receptor complex that mediates cell-cell interactions between muscle precursor cells. Promotes differentiation of myogenic cells (By similarity). {ECO:0000250}.; DISEASE: Holoprosencephaly 11 (HPE11) [MIM:614226]: A structural anomaly of the brain, in which the developing forebrain fails to correctly separate into right and left hemispheres. Holoprosencephaly is genetically heterogeneous and associated with several distinct facies and phenotypic variability. {ECO:0000269|PubMed:21802063}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);breast;testis; superior cervical ganglion;skeletal muscle;cerebellum; 0.12453 0.17736 0.835845825 88.16348195 2210.61704 8.65464 CDPF1 0.00113893126522692 0.389555241712991 0.609305827021782 cysteine rich, DPF motif domain containing 1 . . . . . . . 0.657836546 84.27105449 1804.13948 7.83873 CDR1 0.0595616098313709 0.71657844798196 0.223859942186669 cerebellar degeneration related protein 1 . . TISSUE SPECIFICITY: Brain; predominantly expressed in normal neuroectodermal tissues and in certain malignant tumors.; . . 0.04456 . 0.148941568 64.31941496 46.72516 1.32058 CDR1-AS . . . CDR1 antisense RNA . . . . . . . . . . . CDR2 5.60529124829684e-06 0.673355390802253 0.326639003906499 cerebellar degeneration related protein 2 . . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;pharynx;blood;lens;bile duct;breast;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.22784 0.22516 -0.979072682 8.752064166 77.67433 1.85542 CDR2L 0.00132717884607588 0.651838404473777 0.346834416680147 cerebellar degeneration-related protein 2-like . . . myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;uterus;prostate;optic nerve;bone;testis;brain;unclassifiable (Anatomical System);cartilage;urinary;pancreas;lung;placenta;visual apparatus;macula lutea;cervix;kidney;mammary gland;stomach;aorta;cerebellum; thalamus;cerebellum peduncles;placenta;prefrontal cortex;caudate nucleus;cingulate cortex;parietal lobe;cerebellum; 0.12545 0.08963 -0.183570861 39.95046001 85.74567 1.97728 CDRT1 . . . CMT1A duplicated region transcript 1 . . TISSUE SPECIFICITY: Expressed in pancreas, heart and skeletal muscle. {ECO:0000269|PubMed:11381029, ECO:0000269|PubMed:9403059}.; unclassifiable (Anatomical System);breast;optic nerve;macula lutea;testis;fovea centralis;choroid;lens;brain;retina; . . . 0.846940207 88.47605567 5108.29652 14.68503 CDRT2 . . . CMT1A duplicated region transcript 2 . . . . . . . . . . . CDRT3 . . . CMT1A duplicated region transcript 3 . . . . . . . . . . . CDRT4 0.244291013523455 0.643502041014943 0.112206945461602 CMT1A duplicated region transcript 4 . . TISSUE SPECIFICITY: Expressed in fetal skeletal muscle and kidney. {ECO:0000269|PubMed:11381029}.; breast;lung;thyroid;head and neck;brain;stomach;bone marrow; superior cervical ganglion;atrioventricular node; 0.07321 . . . 68.37967 1.71113 CDRT5 . . . CMT1A duplicated region transcript 5 . . . . . . . . . . . CDRT7 . . . CMT1A duplicated region transcript 7 (non-protein coding) . . . . . . . . . . . CDRT8 . . . CMT1A duplicated region transcript 8 . . . . . . . . . . . CDRT10 . . . CMT1A duplicated region transcript 10 . . . . . . . . . . . CDRT11 . . . CMT1A duplicated region transcript 11 . . . . . . . . . . . CDRT12 . . . CMT1A duplicated region transcript 12 . . . . . . . . . . . CDRT13 . . . CMT1A duplicated region transcript 13 . . . . . . . . . . . CDRT15 0.00750643849425516 0.775238502927118 0.217255058578626 CMT1A duplicated region transcript 15 . . TISSUE SPECIFICITY: Expressed in fetal heart, kidney, liver, lung and spleen. {ECO:0000269|PubMed:11381029}.; . . 0.07767 0.02699 . . 203.35726 3.07788 CDRT15L2 0.321628091846862 0.611583946531025 0.0667879616221132 CMT1A duplicated region transcript 15-like 2 . . . . . . . . . 41.54695 1.21209 CDRT15P1 . . . CMT1A duplicated region transcript 15 pseudogene 1 . . . . . 0.07767 . . . . . CDRT15P2 . . . CMT1A duplicated region transcript 15 pseudogene 2 . . . . . . . . . . . CDS1 0.00532553324506115 0.989337911501316 0.00533655525362239 CDP-diacylglycerol synthase 1 FUNCTION: Provides CDP-diacylglycerol, an important precursor for the synthesis of phosphatidylinositol (PtdIns), phosphatidylglycerol, and cardiolipin. Overexpression may amplify cellular signaling responses from cytokines. May also play an important role in the signal transduction mechanism of retina and neural cells.; . TISSUE SPECIFICITY: Expressed in adult tissues such as placenta, brain, small intestine, ovary, testis and prostate. Highly expressed in fetal kidney, lung and brain. Lower level in fetal liver.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;bile duct;lung;placenta;macula lutea;liver;head and neck;kidney;stomach; whole brain;amygdala;thalamus;subthalamic nucleus;prostate;occipital lobe;trachea;thyroid;placenta;temporal lobe;prefrontal cortex;globus pallidus;cerebellum; 0.12746 0.09264 0.483275131 79.25218212 252.10799 3.41837 CDS2 6.78080961217838e-05 0.977355656154555 0.0225765357493234 CDP-diacylglycerol synthase 2 FUNCTION: Provides CDP-diacylglycerol, an important precursor for the synthesis of phosphatidylinositol, phosphatidylglycerol, and cardiolipin.; . TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain and retina, and to a lesser extent in placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:9889000}.; . . 0.08157 0.08152 -0.315847836 31.68789809 624.29254 5.04006 CDSN 0.499451801068193 0.480791597855989 0.019756601075819 corneodesmosin FUNCTION: Important for the epidermal barrier integrity. {ECO:0000269|PubMed:20691404}.; DISEASE: Hypotrichosis 2 (HYPT2) [MIM:146520]: A condition characterized by the presence of less than the normal amount of hair. Affected individuals have normal hair in early childhood but experience progressive hair loss limited to the scalp beginning in the middle of the first decade and almost complete baldness by the third decade. Body hair, beard, eyebrows, axillary hair, teeth, and nails develop normally. {ECO:0000269|PubMed:12754508}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peeling skin syndrome 1 (PSS1) [MIM:270300]: A genodermatosis characterized by generalized, continuous shedding of the outer layers of the epidermis. Two main PSS subtypes have been suggested. Patients with non-inflammatory PSS (type A) manifest white scaling, with painless and easy removal of the skin, irritation when in contact with water, dust and sand, and no history of erythema, pruritis or atopy. Inflammatory PSS (type B) is associated with generalized erythema, pruritus and atopy. It is an ichthyosiform erythroderma characterized by lifelong patchy peeling of the entire skin with onset at birth or shortly after. Several patients have been reported with high IgE levels. {ECO:0000269|PubMed:20691404}. Note=The disease is caused by mutations affecting the gene represented in this entry. CDNS mutations are responsible for generalized, inflammatory peeling skin syndrome type B (PubMed:20691404). {ECO:0000269|PubMed:20691404}.; TISSUE SPECIFICITY: Exclusively expressed in skin.; . . 0.09249 . 2.109277534 97.88865298 5162.02788 14.77077 CDT1 7.76436067319038e-09 0.147546790000729 0.85245320223491 chromatin licensing and DNA replication factor 1 FUNCTION: Cooperates with CDC6 to promote the loading of the mini- chromosome maintenance complex onto chromatin to form the pre- replication complex necessary to initiate DNA replication. Binds DNA in a sequence-, strand-, and conformation-independent manner. Potential oncogene. {ECO:0000250|UniProtKB:Q8R4E9, ECO:0000269|PubMed:11125146, ECO:0000269|PubMed:14672932, ECO:0000269|PubMed:14993212, ECO:0000269|PubMed:21856198}.; DISEASE: Meier-Gorlin syndrome 4 (MGORS4) [MIM:613804]: A syndrome characterized by bilateral microtia, aplasia/hypoplasia of the patellae, and severe intrauterine and postnatal growth retardation with short stature and poor weight gain. Additional clinical findings include anomalies of cranial sutures, microcephaly, apparently low-set and simple ears, microstomia, full lips, highly arched or cleft palate, micrognathia, genitourinary tract anomalies, and various skeletal anomalies. While almost all cases have primordial dwarfism with substantial prenatal and postnatal growth retardation, not all cases have microcephaly, and microtia and absent/hypoplastic patella are absent in some. Despite the presence of microcephaly, intellect is usually normal. {ECO:0000269|PubMed:21358631, ECO:0000269|PubMed:21358632}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymphoreticular;ovary;adrenal cortex;colon;uterus;pancreas;prostate;optic nerve;lung;endometrium;bone;placenta;visual apparatus;liver;testis;cervix;germinal center;kidney;brain;mammary gland;stomach;thymus; superior cervical ganglion;tumor;pons; 0.96985 0.14861 1.18495331 92.84029252 248.60148 3.39744 CDV3 0.201907143848833 0.754159429286573 0.0439334268645942 CDV3 homolog (mouse) . . TISSUE SPECIFICITY: Expression levels correlate with those of HER- 2/neu in breast cancer cells. {ECO:0000269|PubMed:10497265}.; smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;brain;bladder;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;testis;white blood cells;ciliary ganglion;skeletal muscle; 0.07987 0.06758 0.014844891 54.94810097 126.9371 2.45689 CDV3P1 . . . CDV3 pseudogene 1 . . . . . . . . . . . CDX1 0.702597062757003 0.281206108329187 0.0161968289138103 caudal type homeobox 1 FUNCTION: Could play a role in the terminal differentiation of the intestine.; . TISSUE SPECIFICITY: Intestinal epithelium.; unclassifiable (Anatomical System);lung;testis;colon;stomach; superior cervical ganglion;liver;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.32065 0.19642 . . 100.5993 2.17313 CDX2 0.553145867415221 0.43358869817617 0.0132654344086091 caudal type homeobox 2 FUNCTION: Involved in the transcriptional regulation of multiple genes expressed in the intestinal epithelium. Important in broad range of functions from early differentiation to maintenance of the intestinal epithelial lining of both the small and large intestine.; . . . . 0.89959 0.55078 0.148941568 64.31941496 284.0769 3.60732 CDX4 0.0135584478091119 0.667435188110885 0.319006364080003 caudal type homeobox 4 . . . . . 0.11991 0.12890 0.03689118 56.64071715 11.16789 0.40368 CDY1 . . . chromodomain protein, Y-linked, 1 FUNCTION: Has histone acetyltransferase activity, with a preference for histone H4. {ECO:0000269|PubMed:12072557}.; . TISSUE SPECIFICITY: Testis-specific. Detected in spermatids (at protein level). {ECO:0000269|PubMed:12072557}.; testis; . . . . . . . CDY1B . . . chromodomain protein, Y-linked, 1B FUNCTION: Has histone acetyltransferase activity, with a preference for histone H4. {ECO:0000269|PubMed:12072557}.; . TISSUE SPECIFICITY: Testis-specific. Detected in spermatids (at protein level). {ECO:0000269|PubMed:12072557}.; testis; . . . . . . . CDY2A . . . chromodomain protein, Y-linked, 2A FUNCTION: May have histone acetyltransferase activity. {ECO:0000250}.; . TISSUE SPECIFICITY: Testis specific.; testis; . . . . . . . CDY2B . . . chromodomain protein, Y-linked, 2B FUNCTION: May have histone acetyltransferase activity. {ECO:0000250}.; . TISSUE SPECIFICITY: Testis specific.; . . . . . . . . CDY3P . . . chromodomain protein, Y-linked 3 pseudogene . . . . . . . . . . . CDY4P . . . chromodomain protein, Y-linked 4 pseudogene . . . . . . . . . . . CDY5P . . . chromodomain protein, Y-linked 5 pseudogene . . . . . . . . . . . CDY6P . . . chromodomain protein, Y-linked 6 pseudogene . . . . . . . . . . . CDY7P . . . chromodomain protein, Y-linked 7 pseudogene . . . . . . . . . . . CDY8P . . . chromodomain protein, Y-linked 8 pseudogene . . . . . . . . . . . CDY9P . . . chromodomain protein, Y-linked 9 pseudogene . . . . . . . . . . . CDY10P . . . chromodomain protein, Y-linked 10 pseudogene . . . . . . . . . . . CDY11P . . . chromodomain protein, Y-linked 11 pseudogene . . . . . . . . . . . CDY12P . . . chromodomain protein, Y-linked 12 pseudogene . . . . . . . . . . . CDY13P . . . chromodomain protein, Y-linked 13 pseudogene . . . . . . . . . . . CDY14P . . . chromodomain protein, Y-linked 14 pseudogene . . . . . . . . . . . CDY15P . . . chromodomain protein, Y-linked 15 pseudogene . . . . . . . . . . . CDY16P . . . chromodomain protein, Y-linked 16 pseudogene . . . . . . . . . . . CDY17P . . . chromodomain protein, Y-linked 17 pseudogene . . . . . . . . . . . CDY18P . . . chromodomain protein, Y-linked 18 pseudogene . . . . . . . . . . . CDY19P . . . chromodomain protein, Y-linked 19 pseudogene . . . . . . . . . . . CDY20P . . . chromodomain protein, Y-linked 20 pseudogene . . . . . . . . . . . CDY21P . . . chromodomain protein, Y-linked 21 pseudogene . . . . . . . . . . . CDY22P . . . chromodomain protein, Y-linked 22 pseudogene . . . . . . . . . . . CDY23P . . . chromodomain protein, Y-linked 23 pseudogene . . . . . . . . . . . CDYL 0.946570708320529 0.0533919590722831 3.7332607187562e-05 chromodomain protein, Y-like FUNCTION: Acts as a RE1-silencing transcription factor (REST) corepressor that facilitates histone-lysine N-methyltransferase EHMT2 recruitment and H3K9 dimethylation at REST target genes for repression. Required for chromatin targeting and maximal enzymatic activity of polycomb repressive complex 2 (PRC2); acts as a positive regulator of PRC2 activity by bridging the pre-existing histone H3K27me3 and newly recruited PRC2 on neighboring nucleosomes. Has histone acetyltransferase activity, with a preference for histone H4. {ECO:0000269|PubMed:12072557, ECO:0000269|PubMed:19061646, ECO:0000269|PubMed:22009739}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed at moderate levels in all tissues examined. Isoform 2 is the most abundantly expressed isoform. {ECO:0000269|PubMed:19808672}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;breast;pancreas;pia mater;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; whole brain;superior cervical ganglion;placenta;skeletal muscle; 0.52021 0.10834 -1.574404032 3.143430054 66.98178 1.69141 CDYL2 0.624960005081721 0.374720526797705 0.000319468120574338 chromodomain protein, Y-like 2 . . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12837688}.; unclassifiable (Anatomical System);prostate;placenta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.56930 0.10716 -1.173870472 5.99197924 48.15422 1.35169 CEACAM1 0.658400054661812 0.34136373614149 0.000236209196697623 carcinoembryonic antigen related cell adhesion molecule 1 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;skeletal muscle;bile duct;lung;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;skeletal muscle;skin;bone marrow;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cerebellum; 0.08882 . 0.220536484 68.38287332 629.0016 5.05425 CEACAM3 1.50184928682074e-07 0.219670509845713 0.780329339969359 carcinoembryonic antigen related cell adhesion molecule 3 FUNCTION: Major granulocyte receptor mediating recognition and efficient opsonin-independent phagocytosis of CEACAM-binding microorganisms, including Neissiria, Moxarella and Haemophilus species, thus playing an important role in the clearance of pathogens by the innate immune system. Responsible for RAC1 stimulation in the course of pathogen phagocytosis. {ECO:0000269|PubMed:12864848, ECO:0000269|PubMed:14707113}.; . TISSUE SPECIFICITY: CGM1a, the predominant CGM1 transcript, is granulocyte-specific. Not detected out of the granulocytic lineage, such as monocytes, lymphocytes, spleen, testis, colon, brain, liver, pancreas, thymus, ovary, placenta, skeletal muscle, prostate, small intestine, heart, lung and kidney. {ECO:0000269|PubMed:11708798}.; unclassifiable (Anatomical System);cartilage;placenta;colon;blood;stomach;bone marrow; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.06835 . 0.41713504 76.95800896 69.72688 1.73225 CEACAM4 1.67959503585306e-06 0.419139914494332 0.580858405910632 carcinoembryonic antigen related cell adhesion molecule 4 FUNCTION: Granulocyte orphan receptor that acts as an trigger efficient phagocytosis of attached particles. {ECO:0000269|PubMed:25567962}.; . TISSUE SPECIFICITY: Granulocytes. {ECO:0000269|PubMed:2050678}.; unclassifiable (Anatomical System);optic nerve;lung;macula lutea;testis;colon;fovea centralis;choroid;kidney;lens;retina; superior cervical ganglion;globus pallidus;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.05354 0.08358 1.0178651 90.91766926 743.97705 5.41511 CEACAM5 3.66899588817934e-05 0.949182457066286 0.0507808529748326 carcinoembryonic antigen related cell adhesion molecule 5 FUNCTION: Cell surface glycoprotein that plays a role in cell adhesion and in intracellular signaling. Receptor for E.coli Dr adhesins. {ECO:0000269|PubMed:10864933}.; . TISSUE SPECIFICITY: Found in adenocarcinomas of endodermally derived digestive system epithelium and fetal colon.; unclassifiable (Anatomical System);smooth muscle;tongue;colon;blood;skeletal muscle;bone marrow;breast;pancreas;lung;larynx;nasopharynx;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;trachea;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04831 . 1.918098272 97.44043406 525.99201 4.67981 CEACAM6 0.191109811032251 0.797855975185679 0.0110342137820697 carcinoembryonic antigen related cell adhesion molecule 6 . . . unclassifiable (Anatomical System);islets of Langerhans;colon;blood;skeletal muscle;bone marrow;uterus;breast;pancreas;lung;nasopharynx;testis;brain;stomach; superior cervical ganglion;lung;trachea;tongue;trigeminal ganglion;skeletal muscle;bone marrow; 0.04123 0.06896 -0.045835247 50.34206181 32.11486 1.00825 CEACAM7 9.14464756921175e-07 0.175506285301968 0.824492800233275 carcinoembryonic antigen related cell adhesion molecule 7 . . TISSUE SPECIFICITY: Strongly down-regulated in colonic adenocarcinomas.; unclassifiable (Anatomical System);pancreas;lung;islets of Langerhans;nasopharynx;testis;colon;skeletal muscle; dorsal root ganglion;superior cervical ganglion;tongue;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15090 . 0.973768544 90.33970276 239.82924 3.34676 CEACAM8 1.24548133374918e-07 0.198860031810902 0.801139843640965 carcinoembryonic antigen related cell adhesion molecule 8 . . TISSUE SPECIFICITY: Expressed in leukocytes of chronic myeloid Leukemia patients and bone marrow.; colon;blood;brain;bone marrow; superior cervical ganglion;skeletal muscle;bone marrow; 0.05067 0.16057 0.220536484 68.38287332 214.00768 3.15709 CEACAM16 0.0295802581415047 0.923920630573491 0.0464991112850041 carcinoembryonic antigen related cell adhesion molecule 16 FUNCTION: Required for proper hearing, it may play a role in maintaining the integrity of the tectorial membrane. {ECO:0000269|PubMed:21368133, ECO:0000269|PubMed:25589040}.; DISEASE: Deafness, autosomal dominant, 4B (DFNA4B) [MIM:614614]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:21368133, ECO:0000269|PubMed:25589040}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.11131 . -0.400392389 26.85185185 75.72401 1.82185 CEACAM18 4.11404429372682e-10 0.0275645610280916 0.972435438560504 carcinoembryonic antigen related cell adhesion molecule 18 . . . . . 0.08161 . 1.399970837 94.72753008 1321.17145 6.83762 CEACAM19 5.7765093789489e-07 0.248356945749355 0.751642476599707 carcinoembryonic antigen related cell adhesion molecule 19 . . TISSUE SPECIFICITY: Ubiquitous with highest expression in prostate, uterus, fetal brain, mammary gland, adrenal gland, skeletal muscle, small intestine, and kidney, and lower expression in lung, cerebellum, testis, liver, pancreas, bone marrow and ovary. {ECO:0000269|PubMed:12801635}.; unclassifiable (Anatomical System);whole body;tongue;colon;head and neck;brain;stomach;retina; amygdala;superior cervical ganglion;fetal liver;pons; 0.14148 . -0.003562597 53.72729417 225.41131 3.24667 CEACAM20 . . . carcinoembryonic antigen related cell adhesion molecule 20 . . . . . 0.08850 . . . . . CEACAM21 2.37927718675089e-10 0.0200235091171669 0.979976490644905 carcinoembryonic antigen related cell adhesion molecule 21 . . . unclassifiable (Anatomical System);lung;alveolus; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.07402 . 1.084010791 91.8141071 1244.77896 6.66321 CEACAM22P . . . carcinoembryonic antigen related cell adhesion molecule 22, pseudogene . . . . . . . . . . . CEACAMP1 . . . carcinoembryonic antigen related cell adhesion molecule pseudogene 1 . . . . . . . . . . . CEACAMP2 . . . carcinoembryonic antigen related cell adhesion molecule pseudogene 2 . . . . . . . . . . . CEACAMP3 . . . carcinoembryonic antigen related cell adhesion molecule pseudogene 3 . . . . . . . . . . . CEACAMP4 . . . carcinoembryonic antigen related cell adhesion molecule pseudogene 4 . . . . . . . . . . . CEACAMP5 . . . carcinoembryonic antigen related cell adhesion molecule pseudogene 5 . . . . . . . . . . . CEACAMP6 . . . carcinoembryonic antigen related cell adhesion molecule pseudogene 6 . . . . . . . . . . . CEACAMP7 . . . carcinoembryonic antigen related cell adhesion molecule pseudogene 7 . . . . . . . . . . . CEACAMP8 . . . carcinoembryonic antigen related cell adhesion molecule pseudogene 8 . . . . . . . . . . . CEACAMP9 . . . carcinoembryonic antigen related cell adhesion molecule pseudogene 9 . . . . . . . . . . . CEACAMP10 . . . carcinoembryonic antigen related cell adhesion molecule pseudogene 10 . . . . . . . . . . . CEACAMP11 . . . carcinoembryonic antigen related cell adhesion molecule pseudogene 11 . . . . . . . . . . . CEBPA . . . CCAAT/enhancer binding protein alpha FUNCTION: Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta. Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes (PubMed:11242107). During early embryogenesis, plays essential and redundant functions with CEBPB. Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP). Critical for the proper development of the liver and the lung (By similarity). Necessary for terminal adipocyte differentiation, is required for postnatal maintenance of systemic energy homeostasis and lipid storage (By similarity). To regulate these different processes at the proper moment and tissue, interplays with other transcription factors and modulators. Downregulates the expression of genes that maintain cells in an undifferentiated and proliferative state through E2F1 repression, which is critical for its ability to induce adipocyte and granulocyte terminal differentiation. Reciprocally E2F1 blocks adipocyte differentiation by binding to specific promoters and repressing CEBPA binding to its target gene promoters. Proliferation arrest also depends on a functional binding to SWI/SNF complex (PubMed:14660596). In liver, regulates gluconeogenesis and lipogenesis through different mechanisms. To regulate gluconeogenesis, functionally cooperates with FOXO1 binding to IRE-controlled promoters and regulating the expression of target genes such as PCK1 or G6PC. To modulate lipogenesis, interacts and transcriptionally synergizes with SREBF1 in promoter activation of specific lipogenic target genes such as ACAS2. In adipose tissue, seems to act as FOXO1 coactivator accessing to ADIPOQ promoter through FOXO1 binding sites (By similarity). {ECO:0000250|UniProtKB:P05554, ECO:0000250|UniProtKB:P53566, ECO:0000269|PubMed:11242107, ECO:0000269|PubMed:14660596}.; FUNCTION: Isoform 4: Directly and specifically enhances ribosomal DNA transcription interacting with RNA polymerase I-specific cofactors and inducing histone acetylation. {ECO:0000269|PubMed:20075868}.; DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. {ECO:0000269|PubMed:11242107, ECO:0000269|PubMed:12661007, ECO:0000269|PubMed:15575056}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . 0.10750 . . 9.16298 0.33430 CEBPA-AS1 . . . CEBPA antisense RNA 1 (head to head) . . . . . . . . . . . CEBPB 0.184473672069434 0.64599676575415 0.169529562176416 CCAAT/enhancer binding protein beta FUNCTION: Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:1741402, PubMed:9374525, PubMed:12048245, PubMed:18647749). Plays also a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'- T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant functions with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Plays also a role in intracellular bacteria killing (By similarity). During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation (PubMed:20829347). Essential for female reproduction because of a critical role in ovarian follicle development (By similarity). Restricts osteoclastogenesis (By similarity). {ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:12048245, ECO:0000269|PubMed:18647749, ECO:0000269|PubMed:20829347, ECO:0000269|PubMed:9374525, ECO:0000303|PubMed:25451943}.; FUNCTION: Isoform 3: Acts as a dominant negative through heterodimerization with isoform 2 (PubMed:11741938). Promotes osteoblast differentiation and osteoclastogenesis (By similarity). {ECO:0000250|UniProtKB:P21272, ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:11741938}.; . TISSUE SPECIFICITY: Expressed at low levels in the lung, kidney and spleen.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;urinary;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach; uterus corpus;lung;adrenal gland;placenta;liver;adrenal cortex;whole blood;skeletal muscle; 0.98075 0.10718 . . 7.44522 0.27641 CEBPB-AS1 . . . CEBPB antisense RNA 1 . . . . . . . . . . . CEBPD 0.540717582035749 0.402706021285456 0.0565763966787952 CCAAT/enhancer binding protein delta FUNCTION: Transcription activator that recognizes two different DNA motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers (PubMed:16397300). Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:1741402, PubMed:16397300). Transcriptional activator that enhances IL6 transcription alone and as heterodimer with CEBPB (PubMed:1741402). {ECO:0000269|PubMed:1741402}.; . . . . . . . . 72.04659 1.76747 CEBPE 0.00239237618926747 0.772510144981299 0.225097478829434 CCAAT/enhancer binding protein epsilon FUNCTION: C/EBP are DNA-binding proteins that recognize two different motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers.; . TISSUE SPECIFICITY: Strongest expression occurs in promyelocyte and late-myeloblast-like cell lines.; unclassifiable (Anatomical System);lymph node;bone;testis; . 0.48261 0.21317 -0.381986487 27.68931352 35.67973 1.07343 CEBPG 0.0693755459843514 0.737642917576512 0.192981536439136 CCAAT/enhancer binding protein gamma FUNCTION: Transcription factor that binds to the promoter and the enhancer regions of target genes. Binds to the enhancer element PRE-I (positive regulatory element-I) of the IL-4 gene (PubMed:7665092). Binds to the promoter and the enhancer of the immunoglobulin heavy chain. Binds to GPE1, a cis-acting element in the G-CSF gene promoter. {ECO:0000250|UniProtKB:P26801, ECO:0000250|UniProtKB:P53568, ECO:0000269|PubMed:7665092}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;cerebral cortex;bone;thyroid;iris;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion; 0.30339 0.16547 -0.007201372 53.19061099 3.69034 0.13669 CEBPZ 1.78414032435548e-05 0.998641579796446 0.00134057880031047 CCAAT/enhancer binding protein zeta FUNCTION: Stimulates transcription from the HSP70 promoter.; . . medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;head and neck;kidney;stomach;thymus; . 0.85991 0.09035 0.251682437 69.69214437 1121.3598 6.39465 CEBPZOS . . . CEBPZ opposite strand . . . . . . . . . . . CECR . . . cat eye syndrome chromosome region . . . . . . . . . . . CECR1 5.25343969690408e-05 0.876497568431626 0.123449897171405 cat eye syndrome chromosome region, candidate 1 FUNCTION: Adenosine deaminase that may contribute to the degradation of extracellular adenosine, a signaling molecule that controls a variety of cellular responses. Requires elevated adenosine levels for optimal enzyme activity. Binds to cell surfaces via proteoglycans and may play a role in the regulation of cell proliferation and differentiation, independently of its enzyme activity. {ECO:0000269|PubMed:20147294, ECO:0000269|PubMed:20453107}.; DISEASE: Polyarteritis nodosa (PAN) [MIM:615688]: A systemic necrotizing vasculitis that affects medium and small arteries. The ensuing tissue ischemia can affect any organ, including the skin, musculoskeletal system, kidneys, gastrointestinal tract, and the cardiovascular and nervous systems. Organ involvement and disease severity are highly variable. Clinical features include recurrent ischemic stroke affecting the small vessels of the brain and resulting in neurologic dysfunction, recurrent fever, myalgias, livedoid rash, gastrointestinal pain and hepatosplenomegaly. {ECO:0000269|PubMed:24552284, ECO:0000269|PubMed:24552285}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Sneddon syndrome (SNDDS) [MIM:182410]: A systemic non- inflammatory thrombotic vasculopathy characterized by the association of livedo racemosa, and in some cases livedo reticularis, with cerebrovascular disease. Livedo racemosa is a persistent net-like violaceous-cyanotic, mottled discoloration of the skin affecting the legs, the arms, the buttocks and the trunk; livedo reticularis is limited to the extremities and is visible only in the cold. Cerebrovascular features include recurrent transient ischemic attacks, infarcts, and rarely spinal strokes or intracranial or subarachnoid hemorrhages. Headache and vertigo may precede the onset of livedo racemosa and cerebrovascular manifestations by several years. Rare neurologic symptoms include seizures, chorea, or myelopathies. {ECO:0000269|PubMed:25075847}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in blood plasma (at protein level). Widely expressed, with most abundant expression in human adult heart, lung, lymphoblasts, and placenta as well as fetal lung, liver, and kidney. In embryo, expressed in the outflow tract and atrium of the developing heart, the VII/VIII cranial nerve ganglion, and the notochord. {ECO:0000269|PubMed:15926889}.; unclassifiable (Anatomical System);breast;uterus;lymph node;lung;heart;ovary;nasopharynx;placenta;iris;testis;brain;skeletal muscle; white blood cells;whole blood; 0.30844 0.09314 -0.354480518 29.42911064 1077.71442 6.29133 CECR2 . . . cat eye syndrome chromosome region, candidate 2 FUNCTION: Part of the CERF (CECR2-containing-remodeling factor) complex, which facilitates the perturbation of chromatin structure in an ATP-dependent manner. May be involved through its interaction with LRPPRC in the integration of cytoskeletal network with vesicular trafficking, nucleocytosolic shuttling, transcription, chromosome remodeling and cytokinesis. {ECO:0000269|PubMed:15640247}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle, thymus, placenta and lung. Expressed at lower level in brain, heart, colon, spleen, kidney.; unclassifiable (Anatomical System);heart;adrenal medulla;fovea centralis;choroid;lens;skin;retina;breast;uterus;prostate;optic nerve;lung;larynx;macula lutea;visual apparatus;testis;head and neck;brain; atrioventricular node; 0.16499 0.11157 . . 3143.21637 10.67829 CECR3 . . . cat eye syndrome chromosome region, candidate 3 (non-protein coding) . . . . . . . . . . . CECR5 2.10878542968906e-08 0.252003449877138 0.747996529035008 cat eye syndrome chromosome region, candidate 5 . . TISSUE SPECIFICITY: Widely expressed.; medulla oblongata;colon;choroid;skin;retina;uterus;prostate;whole body;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;hippocampus;visual apparatus;duodenum;liver;spleen;head and neck;cervix;mammary gland;stomach; heart;trigeminal ganglion;skeletal muscle; 0.12692 0.09414 -0.023789244 52.09365416 1043.95289 6.20152 CECR5-AS1 . . . CECR5 antisense RNA 1 . . . . . . . . . . . CECR6 . . . cat eye syndrome chromosome region, candidate 6 . . TISSUE SPECIFICITY: Widely expressed, especially in adult heart, brain, prostate, testes, peripherical blood leukocytes and fetal brain.; unclassifiable (Anatomical System); . 0.92691 . . . 161.33717 2.77434 CECR7 . . . cat eye syndrome chromosome region, candidate 7 (non-protein coding) . . . . . . . . . . . CECR9 . . . cat eye syndrome chromosome region, candidate 9 (non-protein coding) . . TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in heart. {ECO:0000269|PubMed:11381032}.; . . . . . . . . CEL 6.34004798807079e-05 0.899541953717426 0.100394645802693 carboxyl ester lipase FUNCTION: Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides.; . TISSUE SPECIFICITY: Mammary gland and pancreas. Expressed by eosinophils. {ECO:0000269|PubMed:11834744}.; unclassifiable (Anatomical System);breast;pancreas;lung;ovary;endometrium;islets of Langerhans;liver;colon;kidney;stomach; fetal liver;pancreas;beta cell islets;pituitary; 0.36881 0.36793 . . 277.82312 3.57079 CELA1 0.129951931571659 0.847791286920034 0.022256781508307 chymotrypsin like elastase family member 1 FUNCTION: Acts upon elastin.; . TISSUE SPECIFICITY: Basal layers of epidermis (at protein level). Not expressed in the pancreas. {ECO:0000269|PubMed:10620133}.; . . 0.10224 0.56378 0.485092724 79.37603208 14277.48236 26.10083 CELA2A 1.98449208206109e-06 0.451643215025987 0.548354800481931 chymotrypsin like elastase family member 2A FUNCTION: Acts upon elastin.; . TISSUE SPECIFICITY: Pancreas. Not detected in keratinocytes. {ECO:0000269|PubMed:10620133}.; unclassifiable (Anatomical System);pancreas;islets of Langerhans;muscle;liver; . . . -0.446304853 24.33356924 54.83822 1.48372 CELA2B 0.000617208883252854 0.904661969475438 0.094720821641309 chymotrypsin like elastase family member 2B FUNCTION: Acts upon elastin.; . TISSUE SPECIFICITY: Pancreas.; . . . . 0.306902668 72.38145789 111.85533 2.30249 CELA3A 9.82224694641128e-08 0.312809271369934 0.687190630407597 chymotrypsin like elastase family member 3A FUNCTION: Efficient protease with alanine specificity but only little elastolytic activity.; . . unclassifiable (Anatomical System);prostate;pancreas;lung;islets of Langerhans;liver;spleen;skin; superior cervical ganglion;pancreas;beta cell islets;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.69428 0.10766 -0.356299879 29.31115829 985.05923 6.05314 CELA3B 2.11744211573648e-10 0.035783175659494 0.964216824128762 chymotrypsin like elastase family member 3B FUNCTION: Efficient protease with alanine specificity but only little elastolytic activity.; . TISSUE SPECIFICITY: Pancreas. Not detectable in keratinocytes. {ECO:0000269|PubMed:10620133}.; unclassifiable (Anatomical System);prostate;pancreas;lung;islets of Langerhans;liver;spleen;skin; dorsal root ganglion;pancreas;superior cervical ganglion;beta cell islets;globus pallidus;trigeminal ganglion;bone marrow; 0.26327 . 1.732552414 96.59707478 690.96911 5.24243 CELF1 0.998616884875254 0.00138309179697098 2.33277754375919e-08 CUGBP, Elav-like family member 1 FUNCTION: RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Acts as both an activator and repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre- mRNAs. Activates SM exon 5 inclusion by antagonizing the repressive effect of PTB. Promotes exclusion of exon 11 of the INSR pre-mRNA. Inhibits, together with HNRNPH1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Increases translation and controls the choice of translation initiation codon of CEBPB mRNA. Increases mRNA translation of CEBPB in aging liver (By similarity). Increases translation of CDKN1A mRNA by antagonizing the repressive effect of CALR3. Mediates rapid cytoplasmic mRNA deadenylation. Recruits the deadenylase PARN to the poly(A) tail of EDEN-containing mRNAs to promote their deadenylation. Required for completion of spermatogenesis (By similarity). Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK and to Bruno response elements (BREs). Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA. Binds to AU-rich sequences (AREs or EDEN-like) localized in the 3'-UTR of JUN and FOS mRNAs. Binds to the IR RNA. Binds to the 5'-region of CDKN1A and CEBPB mRNAs. Binds with the 5'-region of CEBPB mRNA in aging liver. {ECO:0000250, ECO:0000269|PubMed:10536163, ECO:0000269|PubMed:11124939, ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:12649496, ECO:0000269|PubMed:12799066, ECO:0000269|PubMed:14726956, ECO:0000269|PubMed:16601207, ECO:0000269|PubMed:16946708}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10893231, ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:16862542}.; ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;oral cavity;pancreas;lung;adrenal gland;placenta;hippocampus;amnion;head and neck;kidney;stomach; dorsal root ganglion;occipital lobe;superior cervical ganglion;cerebellum peduncles;pons;atrioventricular node;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.91262 0.15588 -0.494039303 22.09247464 17.8381 0.62360 CELF2 0.998785801473528 0.00121418154484091 1.69816311743088e-08 CUGBP, Elav-like family member 2 FUNCTION: RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of TNNT2 in embryonic, but not adult, skeletal muscle. Activates TNNT2 exon 5 inclusion by antagonizing the repressive effect of PTB. Acts as both an activator and repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs. Promotes inclusion of exonS 21 and exclusion of exon 5 of the NMDA receptor R1 pre- mRNA. Involved in the apoB RNA editing activity. Increases COX2 mRNA stability and inhibits COX2 mRNA translation in epithelial cells after radiation injury (By similarity). Modulates the cellular apoptosis program by regulating COX2-mediated prostaglandin E2 (PGE2) expression (By similarity). Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK. Binds to the muscle-specific splicing enhancer (MSE) intronic sites flanking the TNNT2 alternative exon 5. Binds preferentially to UG-rich sequences, in particular UG repeat and UGUU motifs. Binds to apoB mRNA, specifically to AU-rich sequences located immediatly upstream of the edited cytidine. Binds AU-rich sequences in the 3'-UTR of COX2 mRNA (By similarity). Binds to an intronic RNA element responsible for the silencing of exon 21 splicing (By similarity). Binds to (CUG)n repeats (By similarity). {ECO:0000250, ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:11577082, ECO:0000269|PubMed:11931771, ECO:0000269|PubMed:12649496, ECO:0000269|PubMed:14973222, ECO:0000269|PubMed:15657417, ECO:0000269|PubMed:15894795}.; . TISSUE SPECIFICITY: Expressed in frontal cortex. Isoform 1 is expressed in brain and lung. Isoform 2 is expressed in heart, brain, placenta, lung, liver, kidney, skeletal muscle and pancreas. Isoform 4 is expressed in heart, lung, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:10524244, ECO:0000269|PubMed:10893231, ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:11414768, ECO:0000269|PubMed:16862542}.; lymphoreticular;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);amygdala;meninges;lymph node;heart;hypothalamus;blood;lens;skeletal muscle;pia mater;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; amygdala;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;subthalamic nucleus;prefrontal cortex;globus pallidus;white blood cells;pons;trigeminal ganglion;cingulate cortex; 0.21260 0.14915 -0.404032746 26.53338051 10.93402 0.39540 CELF2-AS1 . . . CELF2 antisense RNA 1 . . . . . 0.03536 . . . . . CELF2-AS2 . . . CELF2 antisense RNA 2 . . . . . . . . . . . CELF3 0.2931429110507 0.705960463908328 0.000896625040971878 CUGBP, Elav-like family member 3 FUNCTION: RNA-binding protein involved in the regulation of pre- mRNA alternative splicing. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Activates the splicing of MAPT/Tau exon 10. Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA. {ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:15009664}.; . TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:11158314}.; unclassifiable (Anatomical System);frontal lobe;islets of Langerhans;kidney;brain;retina; dorsal root ganglion;superior cervical ganglion;occipital lobe;globus pallidus;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.70964 0.12663 -0.05129383 49.75819769 20.03326 0.68374 CELF4 0.974364730195216 0.0256340565952709 1.21320951343614e-06 CUGBP, Elav-like family member 4 FUNCTION: RNA-binding protein implicated in the regulation of pre- mRNA alternative splicing. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Promotes exclusion of both the smooth muscle (SM) and non-muscle (NM) exons in actinin pre-mRNAs. Activates the splicing of MAPT/Tau exon 10. Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA. {ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:12649496, ECO:0000269|PubMed:14973222, ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:15894795}.; . TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in the cerebellum, hippocampus, amygdala, temporal and frontal cortex and frontal lobes. {ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:12438720, ECO:0000269|PubMed:16862542}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;whole body;lung;macula lutea;hippocampus;pituitary gland;testis;brain; whole brain;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;skin;subthalamic nucleus;fetal brain;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.51622 0.11809 -0.514264485 21.41424864 24.35294 0.80044 CELF5 0.996405707329076 0.00359405307722876 2.39593695088252e-07 CUGBP, Elav-like family member 5 FUNCTION: RNA-binding protein implicated in the regulation of pre- mRNA alternative splicing. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA. {ECO:0000269|PubMed:11158314}.; . TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:11158314}.; amygdala;unclassifiable (Anatomical System);hypothalamus;choroid;fovea centralis;lens;retina;prostate;lung;optic nerve;frontal lobe;visual apparatus;macula lutea;testis;brain; . 0.15787 0.08486 -0.714505427 14.4019816 13.01241 0.47419 CELF6 0.376807001276073 0.620932552642121 0.00226044608180686 CUGBP, Elav-like family member 6 FUNCTION: RNA-binding protein implicated in the regulation of pre- mRNA alternative splicing. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of TNNT2 in a muscle-specific splicing enhancer (MSE)-dependent manner. Promotes also exon exclusion of INSR pre-mRNA. {ECO:0000269|PubMed:14761971}.; . TISSUE SPECIFICITY: Expressed mainly in kidney, brain and testis and present in other tissues albeit at lower levels. Also expressed in fetal kidney. {ECO:0000269|PubMed:14761971}.; unclassifiable (Anatomical System);heart;islets of Langerhans;blood;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;frontal lobe;adrenal gland;macula lutea;visual apparatus;pituitary gland;liver;testis;spleen;germinal center;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.27846 . 0.193034296 66.82000472 109.21547 2.26904 CELIAC2 . . . celiac disease 2 . . . . . . . . . . . CELP . . . carboxyl ester lipase pseudogene . . . . . 0.12402 . . . . . CELSR1 0.999990747432086 9.25256791345768e-06 6.68208238423401e-20 cadherin EGF LAG seven-pass G-type receptor 1 FUNCTION: Receptor that may have an important role in cell/cell signaling during nervous system formation.; DISEASE: Neural tube defects (NTD) [MIM:182940]: Congenital malformations of the central nervous system and adjacent structures related to defective neural tube closure during the first trimester of pregnancy. Failure of neural tube closure can occur at any level of the embryonic axis. Common NTD forms include anencephaly, myelomeningocele and spina bifida, which result from the failure of fusion in the cranial and spinal region of the neural tube. NTDs have a multifactorial etiology encompassing both genetic and environmental components. {ECO:0000269|PubMed:22095531}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lens;breast;pancreas;lung;placenta;macula lutea;duodenum;hypopharynx;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;lung;tongue;thyroid;appendix;kidney;trigeminal ganglion;skeletal muscle; 0.50392 0.14795 -2.815757777 0.631045058 7612.06127 18.73023 CELSR2 0.999999199832348 8.00167652378161e-07 3.479475319291e-23 cadherin EGF LAG seven-pass G-type receptor 2 FUNCTION: Receptor that may have an important role in cell/cell signaling during nervous system formation.; . TISSUE SPECIFICITY: Highest expression in brain and testis.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;lacrimal gland;tongue;muscle;pharynx;blood;lens;skeletal muscle;bile duct;breast;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach;aorta;cerebellum; amygdala;whole brain;occipital lobe;medulla oblongata;thalamus;superior cervical ganglion;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.21690 0.14994 -1.813160269 2.176220807 1933.01574 8.08880 CELSR3 0.999656221390747 0.0003437786092534 1.51310379494085e-19 cadherin EGF LAG seven-pass G-type receptor 3 FUNCTION: Receptor that may have an important role in cell/cell signaling during nervous system formation.; . . unclassifiable (Anatomical System);heart;adrenal cortex;colon;blood;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;frontal lobe;placenta;thyroid;macula lutea;testis;cervix;brain;mammary gland;stomach;cerebellum; . . 0.24490 -4.265082462 0.11205473 3038.6677 10.47295 CELSR3-AS1 . . . CELSR3 antisense RNA 1 (head to head) . . . . . . . . . . . CEMIP . . . cell migration inducing protein, hyaluronan binding FUNCTION: Mediates depolymerization of hyaluronic acid (HA) via the cell membrane-associated clathrin-coated pit endocytic pathway. Binds to hyaluronic acid. Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product, a process that may occur through rapid vesicle endocytosis and recycling without intracytoplasmic accumulation or digestion in lysosomes. Involved in hyaluronan catabolism in the dermis of the skin and arthritic synovium. Positively regulates epithelial- mesenchymal transition (EMT), and hence tumor cell growth, invasion and cancer dissemination. In collaboration with HSPA5/BIP, promotes cancer cell migration in a calcium and PKC- dependent manner. May be involved in hearing. {ECO:0000269|PubMed:23509262, ECO:0000269|PubMed:23990668, ECO:0000269|PubMed:24269685}.; . TISSUE SPECIFICITY: Expressed in dermal and in synovial fibroblasts. Strongly expressed in gastric cancers compared with the paired normal tissues. Strongly expressed in both ductal carcinoma and invasive breast cancer cells compared with benign epithelial cells (at protein level). Strongly expressed in brain, placenta, prostate, breast, lung and testis. Expressed in fibroblasts, epithelial cells and cancer cells. In ear, it is specifically expressed in inner ear. Expressed in cochlea and vestibule tissues. Strongly expressed in gastric cancers compared with the paired normal tissues. Strongly expressed in colon adenocarcinomas compared with normal colonic mucosas. Strongly expressed in breast cancer as compared to normal breast tissue. {ECO:0000269|PubMed:10574462, ECO:0000269|PubMed:12471561, ECO:0000269|PubMed:16157444, ECO:0000269|PubMed:19434458, ECO:0000269|PubMed:21772334, ECO:0000269|PubMed:22970280, ECO:0000269|PubMed:23936024, ECO:0000269|PubMed:23990668}.; . . 0.12233 0.14658 -1.049140158 7.631516867 . . CEMP1 4.83642669335331e-09 0.0165427736010102 0.983457221562563 cementum protein 1 . . TISSUE SPECIFICITY: Detected in periodontal ligament, cementum, cementoblasts and cementoblastoma. {ECO:0000269|PubMed:16263347}.; . . 0.08067 . 0.306902668 72.38145789 89.92705 2.04076 CEND1 0.584353271222879 0.37351284350011 0.0421338852770107 cell cycle exit and neuronal differentiation 1 FUNCTION: Involved in neuroblastoma cell differentiation. {ECO:0000250}.; . TISSUE SPECIFICITY: Neuron specific. {ECO:0000269|PubMed:11311134}.; unclassifiable (Anatomical System);hypothalamus;sympathetic chain;colon;fovea centralis;lens;skeletal muscle;lung;optic nerve;frontal lobe;macula lutea;testis;brain;spinal ganglion; amygdala;whole brain;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;prefrontal cortex;globus pallidus;cingulate cortex;cerebellum; 0.11784 0.10597 -0.207437529 38.2814343 14.76525 0.53178 CEND1P1 . . . cell cycle exit and neuronal differentiation 1 pseudogene 1 . . . . . . . . . . . CEND1P2 . . . cell cycle exit and neuronal differentiation 1 pseudogene 2 . . . . . . . . . . . CENPA 0.139975206060218 0.779460292490092 0.0805645014496905 centromere protein A FUNCTION: Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro). {ECO:0000269|PubMed:20739937, ECO:0000269|PubMed:21478274}.; . . unclassifiable (Anatomical System);cartilage;ovary;salivary gland;muscle;adrenal cortex;colon;parathyroid;skin;lung;bone;placenta;visual apparatus;liver;testis;cervix;germinal center;kidney;brain;mammary gland;tonsil;stomach; superior cervical ganglion;tumor;atrioventricular node;trigeminal ganglion; 0.67763 0.07898 -0.031067188 51.03798066 7.35119 0.27381 CENPB 0.973451328276556 0.0265164506536621 3.2221069781484e-05 centromere protein B FUNCTION: Interacts with centromeric heterochromatin in chromosomes and binds to a specific 17 bp subset of alphoid satellite DNA, called the CENP-B box. May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes.; . . . . 0.61872 0.10479 -0.381986487 27.68931352 205.82219 3.10095 CENPBD1 0.0200720946377584 0.743612868650349 0.236315036711893 CENPB DNA-binding domain containing 1 . . . . . . . 0.170987912 65.5579146 337.59367 3.90193 CENPBD1P1 . . . CENPB DNA-binding domains containing 1 pseudogene 1 . . . . . . . . . . . CENPC 0.0671173857252203 0.932761030082067 0.000121584192712394 centromere protein C FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions. {ECO:0000269|PubMed:19482874, ECO:0000269|PubMed:21529714}.; . . . . 0.06726 0.08876 1.335644081 94.24982307 141.18152 2.59270 CENPCP1 . . . centromere protein C pseudogene 1 FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions. {ECO:0000269|PubMed:19482874, ECO:0000269|PubMed:21529714}.; . . . . . . . . . . CENPE 0.64584064374891 0.35415935625109 4.24411243503223e-16 centromere protein E FUNCTION: Essential for the maintenance of chromosomal stability through efficient stabilization of microtubule capture at kinetochores. Plays a key role in the movement of chromosomes toward the metaphase plate during mitosis. Is a slow plus end- directed motor whose activity is essential for metaphase chromosome alignment. Couples chromosome position to microtubule depolymerizing activity. The highly processive microtubule- dependent motor activity of CENPE serves to power chromosome congression and provides a flexible, motile tether linking kinetochores to dynamic spindle microtubules. Necessary for the mitotic checkpoint signal at individual kinetochores to prevent aneuploidy due to single chromosome loss. Required for the efficient recruitment of BUBR1, MAD1 and MAD2 to attached and newly unattached kinetochores. Stimulates mammalian BUBR1 kinase activity. Accumulates just before mitosis at the G2 phase of the cell cycle. {ECO:0000269|PubMed:17535814, ECO:0000269|PubMed:7889940}.; DISEASE: Microcephaly 13, primary, autosomal recessive (MCPH13) [MIM:616051]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age- related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. {ECO:0000269|PubMed:24748105}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;skin;uterus;prostate;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;spinal cord;pharynx;blood;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach;thymus; superior cervical ganglion;tumor; 0.79930 0.10675 -0.547766672 19.96933239 1117.40097 6.38305 CENPF 2.12598447439069e-25 0.95756828313802 0.0424317168619804 centromere protein F FUNCTION: Required for kinetochore function and chromosome segregation in mitosis. Required for kinetochore localization of dynein, LIS1, NDE1 and NDEL1. Regulates recycling of the plasma membrane by acting as a link between recycling vesicles and the microtubule network though its association with STX4 and SNAP25. Acts as a potential inhibitor of pocket protein-mediated cellular processes during development by regulating the activity of RB proteins during cell division and proliferation. May play a regulatory or permissive role in the normal embryonic cardiomyocyte cell cycle and in promoting continued mitosis in transformed, abnormally dividing neonatal cardiomyocytes. Interaction with RB directs embryonic stem cells toward a cardiac lineage. Involved in the regulation of DNA synthesis and hence cell cycle progression, via its C-terminus. Has a potential role regulating skeletal myogenesis and in cell differentiation in embryogenesis. Involved in dendritic cell regulation of T-cell immunity against chlamydia. {ECO:0000269|PubMed:12974617, ECO:0000269|PubMed:17600710, ECO:0000269|PubMed:7542657, ECO:0000269|PubMed:7651420}.; DISEASE: Ciliary dyskinesia, primary, 31 (CILD31) [MIM:616369]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia. Patients may exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:25564561}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.82148 0.14847 4.962087784 99.81127624 9346.01342 20.92667 CENPH 7.52859796072614e-05 0.917590267529032 0.0823344464913607 centromere protein H FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate. {ECO:0000269|PubMed:14536089, ECO:0000269|PubMed:16875666, ECO:0000269|PubMed:18007590}.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;prostate;cochlea;endometrium;bone;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;pharynx;blood;pancreas;lung;placenta;visual apparatus;liver;head and neck;cervix;kidney; testis;tumor; 0.17285 0.09314 0.014844891 54.94810097 21.20796 0.71661 CENPI 0.996692510858043 0.00330744956201844 3.95799380973455e-08 centromere protein I FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Required for the localization of CENPF, MAD1L1 and MAD2 (MAD2L1 or MAD2L2) to kinetochores. Involved in the response of gonadal tissues to follicle-stimulating hormone. {ECO:0000269|PubMed:12640463, ECO:0000269|PubMed:16622420}.; . . unclassifiable (Anatomical System);uterus;heart;kidney;brain;skin; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.05518 0.13124 0.018483465 55.44939844 40.72092 1.19306 CENPIP1 . . . centromere protein I pseudogene 1 . . . . . . . . . . . CENPJ 3.02634315768328e-21 0.0269107336004143 0.973089266399586 centromere protein J FUNCTION: Plays an important role in cell division and centrosome function by participating in centriole duplication. Inhibits microtubule nucleation from the centrosome. {ECO:0000269|PubMed:15047868, ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:20531387}.; DISEASE: Microcephaly 6, primary, autosomal recessive (MCPH6) [MIM:608393]: A disease defined as a head circumference more than 3 standard deviations below the age-related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. Despite this marked reduction in size, the gyral pattern is relatively well preserved, with no major abnormality in cortical architecture. Affected individuals are mentally retarded. Primary microcephaly is further defined by the absence of other syndromic features or significant neurological deficits due to degenerative brain disorder. {ECO:0000269|PubMed:15793586}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Seckel syndrome 4 (SCKL4) [MIM:613676]: A rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and mental retardation. {ECO:0000269|PubMed:20522431}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.16687 . 0.832189686 88.12809625 662.2364 5.15568 CENPK 1.66228604969503e-08 0.121425931628115 0.878574051749025 centromere protein K FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Acts in coordination with CASC5/KNL1 to recruit the NDC80 complex to the outer kinetochore. {ECO:0000269|PubMed:16622420, ECO:0000269|PubMed:16716197, ECO:0000269|PubMed:18045986}.; . TISSUE SPECIFICITY: Detected in several fetal organs with highest levels in fetal liver. In adults, it is weakly expressed in lung and placenta. {ECO:0000269|PubMed:8950979}.; unclassifiable (Anatomical System);lymph node;skin;skeletal muscle;bone marrow;breast;uterus;whole body;lung;gum;thyroid;placenta;testis;germinal center;kidney;brain;mammary gland;bladder;stomach; superior cervical ganglion; 0.53239 0.17509 0.305084559 72.22811984 47.05113 1.32660 CENPL 0.513926394303849 0.482209020912496 0.00386458478365485 centromere protein L FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. {ECO:0000269|PubMed:16716197}.; . . uterus;unclassifiable (Anatomical System);prostate;lung;visual apparatus;liver;testis;germinal center;skin; superior cervical ganglion;skin; 0.11032 0.07805 0.305084559 72.22811984 99.96163 2.16764 CENPM 0.213983560470949 0.746580987704285 0.039435451824766 centromere protein M FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. {ECO:0000269|PubMed:16716197}.; . TISSUE SPECIFICITY: Isoform 3 is highly expressed in spleen, and intermediately in heart, prostate and ovary. Isoform 3 is highly expressed in resting CD19 B-cells and B-lineage chronic lymphocytic leukemia (B-CLL) cells and weakly expressed in activated B-cells. Isoform 1 is selectively expressed in activated CD19 cells and weakly in resting CD19 B-cells.; lymphoreticular;ovary;colon;parathyroid;skin;uterus;prostate;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;muscle;blood;lung;placenta;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach; fetal liver;tumor;white blood cells;tonsil;bone marrow;thymus; 0.56176 0.11451 -0.095386216 46.48502005 26.74988 0.86608 CENPN 3.16047315352104e-05 0.938730367604948 0.0612380276635168 centromere protein N FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPN is the first protein to bind specifically to CENPA nucleosomes and the direct binding of CENPA nucleosomes by CENPN is required for centromere assembly. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate. {ECO:0000269|PubMed:16622419, ECO:0000269|PubMed:16716197, ECO:0000269|PubMed:18007590, ECO:0000269|PubMed:19543270}.; . . ovary;salivary gland;intestine;colon;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;pharynx;blood;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;head and neck;kidney;mammary gland;stomach; prostate;superior cervical ganglion;tumor;skeletal muscle; 0.24334 0.08106 1.129924507 92.23283793 89.93372 2.04111 CENPO 6.62948080155535e-06 0.70896414640009 0.291029224119109 centromere protein O FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Modulates the kinetochore-bound levels of NDC80 complex. {ECO:0000269|PubMed:16622420, ECO:0000269|PubMed:16716197, ECO:0000269|PubMed:16932742, ECO:0000269|PubMed:18007590}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.09625 0.06395 0.020302773 55.60863411 61.158 1.59225 CENPP 0.0239284606585644 0.961995580303947 0.0140759590374888 centromere protein P FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. {ECO:0000269|PubMed:16622420}.; . . . . 0.06200 0.07547 0.440999548 77.79547063 83.54036 1.94380 CENPQ 6.26744705048062e-07 0.259060346590387 0.740939026664908 centromere protein Q FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. {ECO:0000269|PubMed:16622420}.; . . unclassifiable (Anatomical System);ovary;adrenal cortex;parathyroid;fovea centralis;uterus;whole body;lung;endometrium;adrenal gland;bone;thyroid;placenta;macula lutea;pituitary gland;liver;testis;spleen;germinal center;kidney;brain;pineal gland; superior cervical ganglion;appendix;pons;trigeminal ganglion; 0.18667 0.10488 0.703746784 85.42108988 4826.41378 14.08231 CENPT 0.0553623518797919 0.943822340250042 0.000815307870166207 centromere protein T FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome- associated complex that binds specifically to histone H3- containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis. {ECO:0000269|PubMed:16716197, ECO:0000269|PubMed:21529714, ECO:0000269|PubMed:21695110}.; . . myocardium;medulla oblongata;ovary;developmental;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;synovium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;hypothalamus;urinary;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;skeletal muscle; 0.04935 0.06599 1.287903524 93.83698986 362.97688 4.03482 CENPU . . . centromere protein U FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Plays an important role in the correct PLK1 localization to the mitotic kinetochores. A scaffold protein responsible for the initial recruitment and maintenance of the kinetochore PLK1 population until its degradation. Involved in transcriptional repression. {ECO:0000269|PubMed:12941884, ECO:0000269|PubMed:16716197, ECO:0000269|PubMed:17081991}.; . TISSUE SPECIFICITY: Expressed at high levels in the testis, fetal liver, thymus, bone marrow and at lower levels in the lymph nodes, placenta, colon and spleen. Present in all cell lines examined, including B-cells, T-cells, epithelial cells and fibroblast cells. Expressed at high levels in glioblastoma cell lines. {ECO:0000269|PubMed:12941884, ECO:0000269|PubMed:15116101, ECO:0000269|PubMed:15893739}.; . . 0.56474 0.07819 0.486911049 79.46449634 1963.63245 8.16380 CENPUP1 . . . centromere protein U pseudogene 1 . . . . . . . . . . . CENPUP2 . . . centromere protein U pseudogene 2 . . . . . . . . . . . CENPV 0.31332786522461 0.669200459277613 0.0174716754977776 centromere protein V FUNCTION: Required for distribution of pericentromeric heterochromatin in interphase nuclei and for centromere formation and organization, chromosome alignment and cytokinesis. {ECO:0000269|PubMed:18772885}.; . . ovary;colon;parathyroid;retina;uterus;prostate;whole body;frontal lobe;larynx;bone;thyroid;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;adrenal cortex;lung;placenta;visual apparatus;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.44769 0.15588 . . 9.4075 0.34607 CENPVP1 . . . centromere protein V pseudogene 1 . . . . . . . . . . . CENPVP2 . . . centromere protein V pseudogene 2 . . . . . . . . . . . CENPVP3 . . . centromere protein V pseudogene 3 . . . . . . . . . . . CENPW 0.50013630684411 0.480204501929844 0.0196591912260467 centromere protein W FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation (By similarity). The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres (By similarity). Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPW has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis. {ECO:0000250, ECO:0000269|PubMed:19070575, ECO:0000269|PubMed:19533040, ECO:0000269|PubMed:21695110, ECO:0000269|PubMed:22002061, ECO:0000269|PubMed:22304917}.; . TISSUE SPECIFICITY: Highly expressed in ovary, liver, lung and pancreas and to a lower extent in breast and gastrointestinal tract cancers; such as those of the colon, rectum and stomach. Overexpressed in high grade breast invasive tumors. Expressed in many cancer cell types. {ECO:0000269|PubMed:17079448, ECO:0000269|PubMed:17610844}.; . . 0.07826 0.09143 0.501689326 79.7888653 274.5218 3.54962 CEP19 0.0526189332458462 0.862403408462093 0.0849776582920607 centrosomal protein 19kDa . DISEASE: Morbid obesity and spermatogenic failure (MOSPGF) [MIM:615703]: An autosomal recessive morbid obesity syndrome characterized by hypertension, fatty liver disease, insulin resistance, and decreased sperm counts. Variable clinical manifestations are early coronary artery disease with myocardial infarction before 45 years of age, type II diabetes mellitus, and intellectual disability. Morbid obese individuals are defined as having a BMI greater than 40. {ECO:0000269|PubMed:24268657}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.13669 0.09263 0.014844891 54.94810097 1978.13486 8.19446 CEP41 0.000125629303655449 0.9562306676167 0.0436437030796448 centrosomal protein 41kDa FUNCTION: Required during ciliogenesis for tubulin glutamylation in cilium. Probably acts by participating in the transport of TTLL6, a tubulin polyglutamylase, between the basal body and the cilium. {ECO:0000269|PubMed:22246503}.; DISEASE: Joubert syndrome 15 (JBTS15) [MIM:614464]: An autosomal recessive disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy, renal disease, liver fibrosis and polydactyly. {ECO:0000269|PubMed:22246503}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Genetic variations in CEP41 may be associated with susceptibility to autism (PubMed:21438139). {ECO:0000269|PubMed:21438139}.; TISSUE SPECIFICITY: Isoform 1 and isoform 4 are expressed in testis and fetal tissues. {ECO:0000269|PubMed:12034494}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.35352 0.12266 0.551232944 81.48148148 110.55518 2.28931 CEP44 0.000569744896364766 0.895717584770956 0.10371267033268 centrosomal protein 44kDa . . . unclassifiable (Anatomical System);ovary;heart;small intestine;islets of Langerhans;hypothalamus;developmental;colon;parathyroid;skin;skeletal muscle;uterus;prostate;lung;endometrium;bone;thyroid;placenta;hippocampus;liver;testis;spleen;germinal center;kidney;brain;stomach;cerebellum; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15155 0.09923 1.330184494 94.17315405 150.60431 2.67907 CEP55 1.30065957563854e-07 0.809470368232619 0.190529501701423 centrosomal protein 55kDa FUNCTION: Plays a role in mitotic exit and cytokinesis. Not required for microtubule nucleation. Recruits PDCD6IP and TSG101 to midbody during cytokinesis. {ECO:0000269|PubMed:16198290, ECO:0000269|PubMed:17853893}.; . TISSUE SPECIFICITY: Widely expressed, mostly in proliferative tissues. Highly expressed in testis. Intermediate levels in adult and fetal thymus, as well as in various cancer cell lines. Low levels in different parts of the digestive tract, bone marrow, lymph nodes, placenta, fetal heart and fetal spleen. Hardly detected in brain. {ECO:0000269|PubMed:16198290, ECO:0000269|PubMed:16406728}.; unclassifiable (Anatomical System);cartilage;ovary;heart;colon;parathyroid;blood;skin;uterus;bile duct;prostate;pancreas;whole body;lung;endometrium;bone;placenta;liver;testis;cervix;spleen;germinal center;brain;stomach; testis - interstitial;testis - seminiferous tubule;heart;testis;tumor;trigeminal ganglion; 0.39036 0.09216 1.618658506 95.99551781 2637.09733 9.63761 CEP57 0.565432341176635 0.434545995725858 2.16630975076239e-05 centrosomal protein 57kDa FUNCTION: Centrosomal protein which may be required for microtubule attachment to centrosomes. May act by forming ring- like structures around microtubules. Mediates nuclear translocation and mitogenic activity of the internalized growth factor FGF2, but that of FGF1. {ECO:0000269|PubMed:22321063}.; DISEASE: Mosaic variegated aneuploidy syndrome 2 (MVA2) [MIM:614114]: A severe developmental disorder characterized by mosaic aneuploidies, predominantly trisomies and monosomies, involving multiple different chromosomes and tissues. Affected individuals typically present with severe intrauterine growth retardation and microcephaly. Eye anomalies, mild dysmorphism, variable developmental delay, and a broad spectrum of additional congenital abnormalities and medical conditions may also occur. The risk of malignancy is high, with rhabdomyosarcoma, Wilms tumor and leukemia reported in several cases. {ECO:0000269|PubMed:21552266}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12717444}.; myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;tumor;white blood cells;atrioventricular node;trigeminal ganglion; 0.53304 0.13617 -0.045835247 50.34206181 1703.25045 7.61253 CEP57L1 4.26476293249987e-09 0.34532688893228 0.654673106802957 centrosomal protein 57kDa-like 1 FUNCTION: Centrosomal protein which may be required for microtubule attachment to centrosomes. {ECO:0000250}.; . . unclassifiable (Anatomical System);islets of Langerhans;blood;parathyroid;fovea centralis;choroid;lens;skin;retina;prostate;optic nerve;lung;adrenal gland;placenta;macula lutea;germinal center;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;atrioventricular node;skeletal muscle; 0.11229 0.08640 0.973768544 90.33970276 321.04194 3.80647 CEP57L1P1 . . . centrosomal protein 57kDa-like 1 pseudogene 1 . . . . . . . . . . . CEP63 8.50276907222801e-21 0.000507020964396162 0.999492979035604 centrosomal protein 63kDa FUNCTION: Required for normal spindle assembly. Plays a key role in mother-centriole-dependent centriole duplication; the function seems also to involve CEP152, CDK5RAP2 and WDR62 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication. Reported to be required for centrosomal recruitment of CEP152; however, this function has been questioned (PubMed:21983783, PubMed:26297806). Also recruits CDK1 to centrosomes (PubMed:21406398). Plays a role in DNA damage response. Following DNA damage, such as double-strand breaks (DSBs), is removed from centrosomes; this leads to the inactivation of spindle assembly and delay in mitotic progression (PubMed:21406398). {ECO:0000269|PubMed:21406398, ECO:0000269|PubMed:21983783, ECO:0000269|PubMed:26297806}.; DISEASE: Seckel syndrome 6 (SCKL6) [MIM:614728]: A rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and mental retardation. {ECO:0000269|PubMed:21983783}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;oesophagus;larynx;bone;thyroid;iris;testis;dura mater;brain;artery;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;medulla oblongata;pons;atrioventricular node;skeletal muscle;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;whole blood;trigeminal ganglion;parietal lobe; 0.18348 0.10797 -0.420619508 25.72540694 2719.18427 9.82120 CEP68 0.371622601856965 0.62602519873408 0.00235219940895516 centrosomal protein 68kDa FUNCTION: Involved in maintenance of centrosome cohesion, probably as part of a linker structure which prevents centrosome splitting (PubMed:18042621). Required for localization of CDK5RAP2 to the centrosome during interphase (PubMed:24554434, PubMed:25503564). {ECO:0000269|PubMed:18042621, ECO:0000269|PubMed:24554434, ECO:0000269|PubMed:25503564}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;muscle;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;occipital lobe;medulla oblongata;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cerebellum; 0.05976 0.09504 0.718303761 85.85161595 1991.18812 8.21944 CEP70 5.9520361020633e-11 0.602591086674767 0.397408913265712 centrosomal protein 70kDa FUNCTION: Plays a role in the organization of both preexisting and nascent microtubules in interphase cells. During mitosis, required for the organization and orientation of the mitotic spindle.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);hypothalamus;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.31153 0.10699 0.112125503 62.09601321 118.92949 2.37325 CEP72 1.05831804132716e-09 0.300665456320541 0.69933454262114 centrosomal protein 72kDa FUNCTION: Involved in the recruitment of key centrosomal proteins to the centrosome. Provides centrosomal microtubule-nucleation activity on the gamma-tubulin ring complexes (gamma-TuRCs) and has critical roles in forming a focused bipolar spindle, which is needed for proper tension generation between sister chromatids. Required for localization of KIZ, AKAP9 and gamma-tubulin ring complexes (gamma-TuRCs) (PubMed:19536135). Involved in centriole duplication. Required for CDK5RAP22, CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:26297806). {ECO:0000269|PubMed:19536135, ECO:0000269|PubMed:26297806}.; . . unclassifiable (Anatomical System);lymph node;islets of Langerhans;colon;retina;optic nerve;lung;frontal lobe;placenta;bone;testis;germinal center;brain;stomach; ciliary ganglion;skeletal muscle; 0.08108 0.11633 -0.169017544 40.67586695 848.24275 5.69267 CEP76 0.0188226507122001 0.981142406819055 3.4942468744655e-05 centrosomal protein 76kDa FUNCTION: Centrosomal protein involved in regulation of centriole duplication. Required to limit centriole duplication to once per cell cycle by preventing centriole reduplication. {ECO:0000269|PubMed:19460342}.; . . unclassifiable (Anatomical System);heart;hypothalamus;blood;skin;skeletal muscle;uterus;pancreas;whole body;lung;frontal lobe;larynx;bone;thyroid;visual apparatus;hypopharynx;liver;testis;head and neck;germinal center;kidney;brain;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;appendix;testis;trigeminal ganglion;skeletal muscle; 0.13755 0.14516 0.262810045 70.43524416 273.37169 3.54409 CEP78 5.36028026344908e-06 0.868866201009798 0.131128438709939 centrosomal protein 78kDa . . . salivary gland;colon;choroid;fovea centralis;skin;retina;uterus;optic nerve;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;lens;skeletal muscle;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19168 0.11133 -0.088107893 47.06298655 147.55581 2.64709 CEP83 . . . centrosomal protein 83kDa FUNCTION: Component of the distal appendage region of the centriole involved in the initiation of primary cilium assembly. May collaborate with IFT20 in the trafficking of ciliary membrane proteins from the Golgi complex to the cilium during the initiation of primary cilium assembly. {ECO:0000269|PubMed:23348840, ECO:0000269|PubMed:23530209}.; DISEASE: Nephronophthisis 18 (NPHP18) [MIM:615862]: An autosomal recessive disorder characterized by chronic tubulointerstitial nephritis resulting in end-stage renal disease in early childhood. Extrarenal manifestations, including intellectual disability or liver changes, may occur in some patients. {ECO:0000269|PubMed:24882706}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.15826 0.10533 -0.110153916 45.48832272 . . CEP83-AS1 . . . CEP83 antisense RNA 1 (head to head) . . . . . . . . . . . CEP85 0.00585126875456993 0.993955684215432 0.000193047029998006 centrosomal protein 85kDa FUNCTION: Acts as a negative regulator of NEK2 to maintain the centrosome integrity in interphase. Suppresses centrosome disjunction by inhibiting NEK2 kinase activity (PubMed:26220856). {ECO:0000269|PubMed:26220856}.; . . lymphoreticular;myocardium;colon;skin;bone marrow;uterus;prostate;endometrium;synovium;larynx;bone;thyroid;testis;germinal center;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;skeletal muscle;pancreas;lung;epididymis;placenta;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;pons;trigeminal ganglion; 0.18415 . -0.108334733 45.57088936 1642.88347 7.48872 CEP85L 0.00496390705689714 0.994791125704818 0.000244967238284499 centrosomal protein 85kDa-like . . TISSUE SPECIFICITY: Isoform 1 and isoform 4 are expressed in spleen, lymph, thymus, tonsil and peripheral blood leukocytes, with isoform 1 expressed at higher levels. Isoform 4 is detected in K-562 leukemia cells and in the blood of precursor T lymphoblastic lymphoma (T-ALL) patients. {ECO:0000269|PubMed:21938754}.; lung;testis;mammary gland;skeletal muscle; dorsal root ganglion;superior cervical ganglion;testis - interstitial;pons;atrioventricular node;skin;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion; 0.27844 0.09342 0.846940207 88.47605567 750.8512 5.43524 CEP89 4.17121506628981e-20 0.00479902507235755 0.995200974927642 centrosomal protein 89kDa FUNCTION: Required for ciliogenesis. Also plays a role in mitochondrial metabolism where it may modulate complex IV activity. {ECO:0000269|PubMed:23348840, ECO:0000269|PubMed:23575228}.; DISEASE: Note=Homozygous deletion comprising CEP89 and SLC7A9 genes has been reported in a patient with isolated complex IV deficiency, intellectual disability and multisystemic problems that include cystinuria, cataract, broad based walking pattern and deafness. {ECO:0000269|PubMed:23575228}.; . unclassifiable (Anatomical System);cartilage;colon;fovea centralis;breast;lung;frontal lobe;larynx;thyroid;bone;macula lutea;testis;head and neck;kidney;brain;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.03753 0.07440 1.824404405 97.02760085 4359.67089 13.17735 CEP95 9.43885980506812e-12 0.686024060844821 0.31397593914574 centrosomal protein 95kDa . . . . . 0.26971 0.08509 -0.310388054 32.14791224 103.8788 2.20179 CEP97 1.32650017854034e-06 0.988939884922332 0.0110587885774896 centrosomal protein 97kDa FUNCTION: Acts as a key negative regulator of ciliogenesis in collaboration with CCP110 by capping the mother centriole thereby preventing cilia formation. Required for recruitment of CCP110 to the centrosome. {ECO:0000269|PubMed:17719545}.; . . ovary;colon;skin;bone marrow;uterus;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;hypopharynx;spleen;head and neck;cervix;mammary gland; superior cervical ganglion;testis;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.39973 0.09879 -0.595174814 18.21184242 175.1978 2.87864 CEP104 2.63081806867216e-08 0.998929779459491 0.00107019423232876 centrosomal protein 104kDa . . . . . 0.12403 . -0.145152788 42.33899505 2524.76603 9.37024 CEP112 3.05841247613028e-18 0.582472354926836 0.417527645073164 centrosomal protein 112kDa . . . unclassifiable (Anatomical System);fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;oesophagus;bone;macula lutea;liver;testis;spleen;kidney;artery;aorta; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.28474 . -0.459259448 23.69072895 4016.49111 12.55095 CEP120 4.34470692506916e-11 0.98296102823655 0.0170389717200026 centrosomal protein 120kDa FUNCTION: Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors and for proper positioning of neurons during brain development. Also implicated in the migration and selfrenewal of neural progenitors. May play a role in centriole duplication during mitosis (By similarity). {ECO:0000250|UniProtKB:Q7TSG1}.; DISEASE: Short-rib thoracic dysplasia 13 with or without polydactyly (SRTD13) [MIM:616300]: A form of short-rib thoracic dysplasia, a group of autosomal recessive ciliopathies that are characterized by a constricted thoracic cage, short ribs, shortened tubular bones, and a 'trident' appearance of the acetabular roof. Polydactyly is variably present. Non-skeletal involvement can include cleft lip/palate as well as anomalies of major organs such as the brain, eye, heart, kidneys, liver, pancreas, intestines, and genitalia. Some forms of the disease are lethal in the neonatal period due to respiratory insufficiency secondary to a severely restricted thoracic cage, whereas others are compatible with life. Disease spectrum encompasses Ellis-van Creveld syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-Saldino syndrome, and short rib-polydactyly syndrome. {ECO:0000269|PubMed:25361962}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;lymphoreticular;lung;cartilage;placenta;testis;germinal center;skeletal muscle;retina; . 0.20235 . 0.007353605 54.12243454 6832.03941 17.58570 CEP126 . . . centrosomal protein 126kDa FUNCTION: Participates in cytokinesis (PubMed:19799413). Necessary for microtubules and mitotic spindle organization (PubMed:24867236). Involved in primary cilium formation (PubMed:24867236). {ECO:0000269|PubMed:19799413, ECO:0000269|PubMed:24867236}.; . TISSUE SPECIFICITY: Expressed in brain, lung, skeletal muscle, kidney, pancreas, testis and ovary. {ECO:0000269|PubMed:10718198}.; . . 0.09396 0.08382 0.45192103 78.03727294 . . CEP128 4.09190040207887e-18 0.857371450590361 0.142628549409639 centrosomal protein 128kDa . . . unclassifiable (Anatomical System);lung;endometrium;adrenal gland;thyroid;liver;colon;testis;kidney;brain;bone marrow; subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.13348 . -0.677918753 15.39867893 3131.04861 10.65240 CEP131 . . . centrosomal protein 131kDa FUNCTION: Component of centriolar satellites contributing to build a complex and dynamic network required to regulate cilia/flagellum formation (PubMed:17954613). In proliferating cells, MIB1-mediated ubiquitination induces its sequestration within centriolar satellites, precluding untimely cilia formation initiation. In contrast, during normal and ultraviolet or heat shock cellular stress-induced ciliogenesis, its non-ubiquitinated form is rapidly displaced from centriolar satellites and recruited to centrosome/basal bodies in a microtubule- and p38 MAPK-dependent manner (PubMed:24121310). Acts also as a negative regulator of BBSome ciliary trafficking (PubMed:24550735). Plays a role in sperm flagellar formation; may be involved in the regulation of intraflagellar transport (IFT) and/or intramanchette (IMT) trafficking, which are important for axoneme extension and/or cargo delivery to the nascent sperm tail (By similarity). Required for optimal cell proliferation and cell cycle progression; may play a role in the regulation of genome stability and centriole duplication in non-ciliogenic cells (PubMed:22797915). Involved in centriole duplication. Required for CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:26297806). {ECO:0000250|UniProtKB:Q62036, ECO:0000269|PubMed:17954613, ECO:0000269|PubMed:22797915, ECO:0000269|PubMed:24121310, ECO:0000269|PubMed:24185901, ECO:0000269|PubMed:24550735, ECO:0000269|PubMed:26297806}.; . . . . 0.11345 0.14275 2.688316751 98.8794527 . . CEP135 4.85411343707254e-17 0.972516179714832 0.0274838202851676 centrosomal protein 135kDa FUNCTION: Centrosomal protein involved in centriole biogenesis. Acts as a scaffolding protein during early centriole biogenesis. Also required for centriole-centriole cohesion during interphase by acting as a platform protein for CEP250 at the centriole. {ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:18851962}.; DISEASE: Microcephaly 8, primary, autosomal recessive (MCPH8) [MIM:614673]: A disease defined as a head circumference more than 3 standard deviations below the age-related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. Despite this marked reduction in size, the gyral pattern is relatively well preserved, with no major abnormality in cortical architecture. Affected individuals are mentally retarded. Primary microcephaly is further defined by the absence of other syndromic features or significant neurological deficits due to degenerative brain disorder. {ECO:0000269|PubMed:22521416}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;heart;ovary;fovea centralis;vein;skin;skeletal muscle;breast;uterus;lung;cochlea;mesenchyma;bone;thyroid;placenta;macula lutea;liver;testis;head and neck;spleen;germinal center;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;temporal lobe;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.65762 0.11694 0.433520496 77.34725171 248.14339 3.39550 CEP152 4.42004196778011e-21 0.612502995011682 0.387497004988318 centrosomal protein 152kDa FUNCTION: Necessary for centrosome duplication; the function seems also to involve CEP63, CDK5RAP2 and WDR62 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (PubMed:26297806). Acts as a molecular scaffold facilitating the interaction of PLK4 and CENPJ, 2 molecules involved in centriole formation (PubMed:21059844, PubMed:20852615). Proposed to snatch PLK4 away from PLK4:CEP92 complexes in early G1 daughter centriole and to reposition PLK4 at the outer boundary of a newly forming CEP152 ring structure (PubMed:24997597). Also plays a key role in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles (By similarity). Overexpression of CEP152 can drive amplification of centrioles (PubMed:20852615). {ECO:0000250|UniProtKB:A2AUM9, ECO:0000250|UniProtKB:Q498G2, ECO:0000269|PubMed:20852615, ECO:0000269|PubMed:21059844, ECO:0000269|PubMed:21131973}.; DISEASE: Microcephaly 9, primary, autosomal recessive (MCPH9) [MIM:614852]: A disease defined as a head circumference more than 3 standard deviations below the age-related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. Despite this marked reduction in size, the gyral pattern is relatively well preserved, with no major abnormality in cortical architecture. Affected individuals are mentally retarded. Primary microcephaly is further defined by the absence of other syndromic features or significant neurological deficits due to degenerative brain disorder. {ECO:0000269|PubMed:20598275}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Seckel syndrome 5 (SCKL5) [MIM:613823]: A rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and mental retardation. {ECO:0000269|PubMed:21131973}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;ovary;cochlea;bone;placenta;liver;testis;spleen;blood; superior cervical ganglion;temporal lobe;appendix;atrioventricular node;pons; 0.16634 0.09998 0.971794703 90.23944326 1499.53511 7.20548 CEP162 . . . centrosomal protein 162kDa FUNCTION: Required to promote assembly of the transition zone in primary cilia. Acts by specifically recognizing and binding the axonemal microtubule. Localizes to the distal ends of centrioles before ciliogenesis and directly binds to axonemal microtubule, thereby promoting and restricting transition zone formation specifically at the cilia base. Required to mediate CEP290 association with microtubules. {ECO:0000269|PubMed:23644468}.; . . . . 0.38609 0.08909 1.126131915 92.12668082 . . CEP164 9.66879225304467e-18 0.947117400362492 0.0528825996375076 centrosomal protein 164kDa FUNCTION: Plays a role in microtubule organization and/or maintenance for the formation of primary cilia (PC), a microtubule-based structure that protrudes from the surface of epithelial cells. Plays a critical role in G2/M checkpoint and nuclear divisions. A key player in the DNA damage-activated ATR/ATM signaling cascade since it is required for the proper phosphorylation of H2AX, RPA, CHEK2 and CHEK1. Plays a critical role in chromosome segregation, acting as a mediator required for the maintenance of genomic stability through modulation of MDC1, RPA and CHEK1. {ECO:0000269|PubMed:17954613, ECO:0000269|PubMed:18283122, ECO:0000269|PubMed:23348840}.; DISEASE: Nephronophthisis 15 (NPHP15) [MIM:614845]: An autosomal recessive disorder characterized by the association of nephronophthisis with Leber congenital amaurosis and retinal degeneration, often resulting in blindness during childhood. Additional features include seizures, cerebellar vermis hypoplasia, facial dysmorphism, bronchiectasis and liver failure. Nephronophthisis is a chronic tubulo-interstitial nephritis that progresses to end-stage renal failure. {ECO:0000269|PubMed:22863007}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in several cell lines. {ECO:0000269|PubMed:17954613}.; smooth muscle;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pharynx;blood;lens;skeletal muscle;lung;macula lutea;liver;spleen;kidney;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis;ciliary ganglion; 0.40076 0.11341 0.086234637 60.326728 3228.09595 10.82346 CEP164P1 . . . centrosomal protein 164kDa pseudogene 1 . . . . . . . . . . . CEP170 . . . centrosomal protein 170kDa FUNCTION: Plays a role in microtubule organization. {ECO:0000269|PubMed:15616186}.; . . lymphoreticular;medulla oblongata;ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;head and neck;kidney;aorta;thymus; amygdala;dorsal root ganglion;medulla oblongata;thalamus;superior cervical ganglion;occipital lobe;hypothalamus;spinal cord;pons;caudate nucleus;skeletal muscle;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.51507 0.12994 -0.26629572 34.81953291 653.42753 5.12884 CEP170B 0.870509859679243 0.129489529526842 6.10793915082654e-07 centrosomal protein 170B FUNCTION: Plays a role in microtubule organization. {ECO:0000250}.; . . . . 0.17272 . -1.690488621 2.600849257 961.44284 6.00066 CEP170P1 . . . centrosomal protein 170kDa pseudogene 1 . . . . . 0.08761 . . . . . CEP192 7.43868591651398e-10 0.99999989717772 1.02078411014346e-07 centrosomal protein 192kDa FUNCTION: Required for mitotic centrosome and spindle assembly. Appears to be a major regulator of pericentriolar material (PCM) recruitment, centrosome maturation, and centriole duplication. {ECO:0000269|PubMed:17980596, ECO:0000269|PubMed:18207742}.; . . ovary;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;bone;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;spleen;cervix;kidney;stomach; fetal liver;thyroid;testis;tumor; 0.09044 0.10852 1.493675397 95.37037037 4911.21175 14.29193 CEP250 8.25125524749097e-17 0.999999809292468 1.90707531708993e-07 centrosomal protein 250kDa FUNCTION: Probably plays an important role in centrosome cohesion during interphase.; . TISSUE SPECIFICITY: Ubiquitously and weakly expressed.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;synovium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;parietal lobe;skeletal muscle;cingulate cortex; 0.14382 0.11236 -0.768298658 13.16937957 892.52783 5.82394 CEP290 1.03912081117924e-34 0.00416172990767305 0.995838270092327 centrosomal protein 290kDa FUNCTION: Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition (By similarity). Activates ATF4-mediated transcription. Required for the correct localization of ciliary and phototransduction proteins in retinal photoreceptor cells; may play a role in ciliary transport processes. {ECO:0000250|UniProtKB:Q6A078, ECO:0000269|PubMed:16682973}.; DISEASE: Joubert syndrome 5 (JBTS5) [MIM:610188]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. Joubert syndrome type 5 shares the neurologic and neuroradiologic features of Joubert syndrome together with severe retinal dystrophy and/or progressive renal failure characterized by nephronophthisis. {ECO:0000269|PubMed:16682970, ECO:0000269|PubMed:16682973, ECO:0000269|PubMed:22425360}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Senior-Loken syndrome 6 (SLSN6) [MIM:610189]: A renal- retinal disorder characterized by progressive wasting of the filtering unit of the kidney (nephronophthisis), with or without medullary cystic renal disease, and progressive eye disease. Typically this disorder becomes apparent during the first year of life. {ECO:0000269|PubMed:20683928}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leber congenital amaurosis 10 (LCA10) [MIM:611755]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:16909394}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Meckel syndrome 4 (MKS4) [MIM:611134]: A disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly. {ECO:0000269|PubMed:17564974}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Antibodies against CEP290 are present in sera from patients with cutaneous T-cell lymphomas, but not in the healthy control population. {ECO:0000269|PubMed:11149944}.; DISEASE: Bardet-Biedl syndrome 14 (BBS14) [MIM:615991]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:18327255}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Expressed strongly in placenta and weakly in brain. {ECO:0000269|PubMed:11149944, ECO:0000269|PubMed:16682973}.; myocardium;ovary;salivary gland;colon;fovea centralis;skin;retina;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;breast;lung;nasopharynx;trabecular meshwork;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.48442 0.31068 0.374677996 75.3066761 2616.79176 9.58280 CEP295 . . . centrosomal protein 295kDa FUNCTION: Centriole-enriched protein that mediates centriole-to- centrosome conversion at late mitosis, but is dispensable for cartwheel removal or centriole disengagement. {ECO:0000269|PubMed:20844083, ECO:0000269|PubMed:25131205}.; . . . . 0.09788 0.08300 5.120160174 99.8289691 . . CEP295NL . . . CEP295 N-terminal like . . . . . . . . . . . CEP350 0.999996390363333 3.60963666747566e-06 2.76265738956894e-22 centrosomal protein 350kDa FUNCTION: Plays an essential role in centriole growth by stabilizing a procentriolar seed composed of at least, SASS6 and CENPJ. Required for anchoring microtubules to the centrosomes and for the integrity of the microtubule network. Recruits PPARA to discrete subcellular compartments and thereby modulates PPARA activity. {ECO:0000269|PubMed:15615782, ECO:0000269|PubMed:16314388, ECO:0000269|PubMed:17878239, ECO:0000269|PubMed:18412956, ECO:0000269|PubMed:19052644}.; . TISSUE SPECIFICITY: Detected in heart, brain, skeletal muscle, testis, placenta, lung, liver, kidney and pancreas. {ECO:0000269|PubMed:11891061, ECO:0000269|PubMed:15615782}.; smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;pons;atrioventricular node;skeletal muscle;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.48662 0.10030 0.078757228 59.2061807 2380.41884 9.05718 CEPA . . . congenital episodic primary apnea . . . . . . . . . . . CEPT1 0.946564689940993 0.0533979668777396 3.7343181267533e-05 choline/ethanolamine phosphotransferase 1 FUNCTION: Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP- ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity. {ECO:0000269|PubMed:10191259, ECO:0000269|PubMed:10893425}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10191259}.; smooth muscle;ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; . 0.14977 0.25410 0.305084559 72.22811984 58.30796 1.54699 CER1 2.57822812120588e-05 0.175572567198034 0.824401650520754 cerberus 1, DAN family BMP antagonist FUNCTION: Cytokine that may play a role in anterior neural induction and somite formation during embryogenesis in part through a BMP-inhibitory mechanism. Can regulate Nodal signaling during gastrulation as well as the formation and patterning of the primitive streak (By similarity). {ECO:0000250}.; . . . . 0.33165 0.15720 0.15257911 64.60839821 444.40089 4.38540 CERCAM 0.0182542487737662 0.977379235074904 0.00436651615132997 cerebral endothelial cell adhesion molecule FUNCTION: Probable cell adhesion protein involved in leukocyte transmigration across the blood-brain barrier. Has apparently no beta-galactosyltransferase activity. {ECO:0000269|PubMed:10608765, ECO:0000269|PubMed:19075007}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in secretory and nervous tissues. {ECO:0000269|PubMed:10608765, ECO:0000269|PubMed:19075007}.; . . 0.07275 0.09562 0.361913759 74.69922151 915.00557 5.88291 CERK 1.60283834611446e-05 0.964865626296688 0.0351183453198507 ceramide kinase FUNCTION: Catalyzes specifically the phosphorylation of ceramide to form ceramide 1-phosphate. Acts efficiently on natural and analog ceramides (C6, C8, C16 ceramides, and C8-dihydroceramide), to a lesser extent on C2-ceramide and C6-dihydroceramide, but not on other lipids, such as various sphingosines. Binds phosphoinositides. {ECO:0000269|PubMed:19168031}.; . TISSUE SPECIFICITY: High level expression in heart, brain, skeletal muscle, kidney and liver; moderate in peripheral blood leukocytes and thymus; very low in spleen, small intestine, placenta and lung.; ovary;salivary gland;intestine;colon;substantia nigra;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;muscle;pharynx;blood;lens;breast;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;pituitary;cerebellum; 0.21667 0.15746 0.270087468 70.69473933 373.76189 4.07777 CERKL 5.39719665583234e-11 0.203761942772006 0.796238057174022 ceramide kinase like FUNCTION: Has no detectable ceramide-kinase activity. Overexpression of CERKL protects cells from apoptosis in oxidative stress conditions. {ECO:0000269|PubMed:15708351, ECO:0000269|PubMed:19158957}.; DISEASE: Retinitis pigmentosa 26 (RP26) [MIM:608380]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:14681825, ECO:0000269|PubMed:18978954}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in adult retina, liver and pancreas as well as in fetal brain, lung and kidney. Isoform 3 is expressed in adult retina as well as in fetal lung and liver. Isoform 4 is expressed in adult retina, lung and kidney as well as in fetal lung and liver. Moderately expressed in retina, kidney, lung, testis, trachea, and pancreas. Weakly expressed in brain, placenta and liver. {ECO:0000269|PubMed:14681825, ECO:0000269|PubMed:15708351, ECO:0000269|PubMed:19158957}.; unclassifiable (Anatomical System);lymph node;lung;whole body;cartilage;islets of Langerhans;placenta;peripheral nerve; . 0.34480 0.09757 0.711016566 85.72776598 1722.63428 7.65761 CERS1 0.0454570437212016 0.852584164872656 0.101958791406142 ceramide synthase 1 FUNCTION: May be either a bona fide (dihydro)ceramide synthase or a modulator of its activity. When overexpressed in cells is involved in the production of sphingolipids containing mainly one fatty acid donor (N-linked stearoyl- (C18) ceramide) in a fumonisin B1-independent manner (By similarity). {ECO:0000250|UniProtKB:P27545}.; DISEASE: Epilepsy, progressive myoclonic 8 (EPM8) [MIM:616230]: A severe form of progressive myoclonic epilepsy characterized by myoclonus, generalized tonic-clonic seizures and moderate to severe cognitive impairment. {ECO:0000269|PubMed:24782409}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . . -0.670411825 15.61689078 8.47404 0.31086 CERS2 0.91016304279668 0.0898312146155522 5.74258776790398e-06 ceramide synthase 2 FUNCTION: Suppresses the growth of cancer cells. May be involved in sphingolipid synthesis.; . TISSUE SPECIFICITY: Expressed in kidney, liver, brain, heart, placenta and lung. {ECO:0000269|PubMed:11543633}.; myocardium;medulla oblongata;ovary;skin;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; fetal liver;adrenal gland;spinal cord;liver;atrioventricular node;kidney; 0.23454 0.14526 -0.137658575 43.57159707 571.98844 4.85280 CERS3 0.000441004567942562 0.963363110859921 0.0361958845721359 ceramide synthase 3 FUNCTION: Has (dihydro)ceramide synthesis activity with relatively broad substrate specificity, but a preference for C18:0 and other middle- to long-chain fatty acyl-CoAs (By similarity). It is crucial for the synthesis of very long-chain ceramides in the epidermis, to maintain epidermal lipid homeostasis and terminal differentiation. {ECO:0000250, ECO:0000269|PubMed:23754960}.; . TISSUE SPECIFICITY: Expressed in the epidermis, where it localizes at the interface between the stratum granulosum and the stratum corneum (at protein level). {ECO:0000269|PubMed:23754960}.; unclassifiable (Anatomical System);lung;developmental;testis;cervix;skin;tonsil; . 0.08964 0.07851 0.753291803 86.71266808 256.21767 3.44283 CERS3-AS1 . . . CERS3 antisense RNA 1 . . . . . . . . . . . CERS4 2.04162899798769e-13 0.0159940950901237 0.984005904909672 ceramide synthase 4 FUNCTION: May be either a bona fide (dihydro)ceramide synthase or a modulator of its activity. When overexpressed in cells is involved in the production of sphingolipids containing different fatty acid donors (N-linked stearoyl- (C18) or arachidoyl- (C20) ceramides) in a fumonisin B1-independent manner (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;thyroid;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;muscle;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland; prostate;thyroid;liver;trigeminal ganglion; 0.14114 0.13072 0.090079492 60.64519934 3493.40433 11.38120 CERS5 1.31067685318133e-05 0.95433979214805 0.0456471010834186 ceramide synthase 5 FUNCTION: Dihydroceramide synthase. Catalyzes the acylation of sphingosine to form dihydroceramide, with high selectivity toward palmitoyl-CoA as acyl donor compared to stearoyl-CoA. Inhibited by fumonisin B1 (By similarity). {ECO:0000250}.; . . ovary;sympathetic chain;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;oesophagus;larynx;bone;testis;artery;pineal gland;spinal ganglion;unclassifiable (Anatomical System);lymph node;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; atrioventricular node; 0.38524 0.11124 0.349177632 74.18023119 38.45678 1.14077 CERS6 0.684541332373748 0.315421385931555 3.72816946973672e-05 ceramide synthase 6 FUNCTION: May be involved in sphingolipid synthesis or its regulation. {ECO:0000250}.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;oesophagus;endometrium;larynx;bone;thyroid;testis;dura mater;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pia mater;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;cerebellum; amygdala;medulla oblongata;occipital lobe;subthalamic nucleus;superior cervical ganglion;prefrontal cortex;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.54479 0.12018 0.218717575 68.27081859 125.72577 2.44166 CERS6-AS1 . . . CERS6 antisense RNA 1 . . . . . . . . . . . CES1 6.76997200580057e-14 0.00837053964664442 0.991629460353288 carboxylesterase 1 FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester. Hydrolyzes the methyl ester group of cocaine to form benzoylecgonine. Catalyzes the transesterification of cocaine to form cocaethylene. Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate. {ECO:0000269|PubMed:7980644, ECO:0000269|PubMed:9169443}.; . TISSUE SPECIFICITY: Expressed predominantly in liver with lower levels in heart and lung. {ECO:0000269|PubMed:10562416}.; smooth muscle;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;larynx;bone;testis;brain;gall bladder;unclassifiable (Anatomical System);cartilage;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; . 0.47190 0.33344 1.912614283 97.42863883 1302.69006 6.79071 CES1P1 . . . carboxylesterase 1 pseudogene 1 FUNCTION: Has no esterase activity. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in placenta. {ECO:0000269|PubMed:10452915}.; . . . . . . . . CES1P2 . . . carboxylesterase 1 pseudogene 2 . . . . . . . . . . . CES2 1.07504051110477e-10 0.162085407726094 0.837914592166402 carboxylesterase 2 FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Shows high catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl acetate, heroin and 6-monoacetylmorphine. {ECO:0000269|PubMed:9169443}.; . TISSUE SPECIFICITY: Preferentially expressed in intestine with moderate expression in liver. Within the intestine, highest expression is found in small intestine with lower expression in colon and rectum. {ECO:0000269|PubMed:9144407}.; lymphoreticular;myocardium;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;brain;unclassifiable (Anatomical System);cartilage;small intestine;islets of Langerhans;hypothalamus;adrenal cortex;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;tongue;adrenal gland;liver;globus pallidus;pons;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex;cerebellum; 0.07261 0.14132 -0.863377021 10.84571833 45.73853 1.29986 CES3 2.05758710215349e-08 0.664009541113114 0.335990438311015 carboxylesterase 3 FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Shows low catalytic efficiency for hydrolysis of CPT-11 (7-ethyl-10-[4-(1-piperidino)- 1-piperidino]-carbonyloxycamptothecin), a prodrug for camptothecin used in cancer therapeutics.; . TISSUE SPECIFICITY: Expressed in liver, colon and small intestine. {ECO:0000269|PubMed:14581373, ECO:0000269|PubMed:15100172, ECO:0000269|PubMed:15687373}.; unclassifiable (Anatomical System);placenta;visual apparatus;hippocampus;colon;brain;mammary gland;stomach; superior cervical ganglion;liver;atrioventricular node;kidney;trigeminal ganglion;cingulate cortex; 0.05604 . 0.225995239 68.51851852 418.80163 4.27764 CES4A 0.000495399061913583 0.968477995646596 0.0310266052914907 carboxylesterase 4A FUNCTION: Probable carboxylesterase. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;hypothalamus;colon;blood;parathyroid;skin;skeletal muscle;bone marrow;pancreas;whole body;lung;frontal lobe;cochlea;endometrium;thyroid;bone;placenta;hippocampus;testis;kidney;brain;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . -0.314027422 31.9297004 527.91507 4.68829 CES5A 5.95161189606759e-19 0.00166981423817833 0.998330185761822 carboxylesterase 5A FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. {ECO:0000250}.; . . . . 0.14648 0.13628 1.806007038 96.95093182 5513.75245 15.30902 CES5AP1 . . . carboxylesterase 5A pseudogene 1 . . . . . . . . . . . CETN1 0.531422796741771 0.408515322138647 0.0600618811195822 centrin 1 FUNCTION: Plays a fundamental role in microtubule-organizing center structure and function.; . . unclassifiable (Anatomical System);medulla oblongata;placenta;testis; testis - seminiferous tubule;testis;trigeminal ganglion; 0.05222 0.10552 0.169169615 65.33380514 970.42874 6.02193 CETN2 0.451744392143999 0.520561431118761 0.0276941767372403 centrin 2 FUNCTION: Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110.; FUNCTION: The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair.; . . . . 0.25596 0.16700 -0.053113545 49.38664779 0.92715 0.02003 CETN3 0.0113207798625902 0.841577959929804 0.147101260207606 centrin 3 FUNCTION: Plays a fundamental role in microtubule-organizing center structure and function.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;liver;head and neck;kidney;mammary gland;aorta;stomach; testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.95702 0.13588 0.191216164 66.57230479 1757.48004 7.73469 CETN4P . . . centrin 4, pseudogene . . . . . . . . . . . CETP 5.18056762742226e-12 0.19129172204496 0.80870827794986 cholesteryl ester transfer protein, plasma FUNCTION: Involved in the transfer of neutral lipids, including cholesteryl ester and triglyceride, among lipoprotein particles. Allows the net movement of cholesteryl ester from high density lipoproteins/HDL to triglyceride-rich very low density lipoproteins/VLDL, and the equimolar transport of triglyceride from VLDL to HDL (PubMed:3600759, PubMed:24293641). Regulates the reverse cholesterol transport, by which excess cholesterol is removed from peripheral tissues and returned to the liver for elimination (PubMed:17237796). {ECO:0000269|PubMed:24293641, ECO:0000303|PubMed:17237796, ECO:0000305|PubMed:3600759}.; DISEASE: Hyperalphalipoproteinemia 1 (HALP1) [MIM:143470]: A condition characterized by high levels of high density lipoprotein (HDL) and increased HDL cholesterol levels. {ECO:0000269|PubMed:12091484, ECO:0000269|PubMed:2215607, ECO:0000269|PubMed:8408659}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; unclassifiable (Anatomical System);pancreas;lung;nasopharynx;placenta;liver;testis;parathyroid;spleen;choroid;kidney;spinal ganglion;brain; superior cervical ganglion;fetal liver;lymph node;placenta;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16082 0.36962 -0.064242613 48.844067 320.75729 3.80433 CFAP20 . . . cilia and flagella associated protein 20 FUNCTION: Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility. Involved in the regulation of the size and morphology of cilia (PubMed:24414207). Required for axonemal microtubules polyglutamylation (PubMed:24414207). {ECO:0000269|PubMed:24414207}.; . . . . 0.28277 0.13588 0.013025609 54.62962963 . . CFAP36 . . . cilia and flagella associated protein 36 FUNCTION: May act as an effector for ARL3.; . TISSUE SPECIFICITY: Expressed in several human tissues including brain, testis, heart, lung, pancreas and spleen (at protein level). {ECO:0000303|PubMed:19680650}.; . . 0.07632 . 0.194852702 67.03231894 . . CFAP43 . . . cilia and flagella associated protein 43 . . . . . 0.12032 0.07938 -1.464556369 3.75678226 . . CFAP44 . . . cilia and flagella associated protein 44 . . . . . 0.19098 . 2.434539058 98.54328851 . . CFAP44-AS1 . . . CFAP44 antisense RNA 1 . . . . . . . . . . . CFAP45 . . . cilia and flagella associated protein 45 . . TISSUE SPECIFICITY: Expressed in nasopharyngeal epithelium and trachea but not in esophagus, stomach, large intestine, liver, cerebrum, heart, bladder, kidney, thymus, or lung. {ECO:0000269|PubMed:10524255}.; . . 0.12417 0.12031 0.358272123 74.66383581 . . CFAP46 . . . cilia and flagella associated protein 46 FUNCTION: As part of the central apparatus of the cilium axoneme plays a role in cilium movement. {ECO:0000250|UniProtKB:A8ICS9}.; . . . . 0.13752 . . . . . CFAP47 . . . cilia and flagella associated protein 47 . . . . . 0.06402 . 0.371224249 75.12384996 . . CFAP52 . . . cilia and flagella associated protein 52 FUNCTION: May play a role in cell growth and/or survival. {ECO:0000269|PubMed:15967112}.; . TISSUE SPECIFICITY: Highly expressed in testis. Up-regulated in hepatocellular carcinoma (HCC). {ECO:0000269|PubMed:15967112}.; . . 0.04801 0.09789 -0.617221851 17.44515216 . . CFAP53 . . . cilia and flagella associated protein 53 . . TISSUE SPECIFICITY: Expressed in skin fibroblasts (at protein level). {ECO:0000269|PubMed:22577226}.; . . 0.05858 0.07179 0.378498378 75.58386412 . . CFAP54 . . . cilia and flagella associated 54 FUNCTION: Required for assembly and function of cilia and flagella. {ECO:0000250|UniProtKB:Q8C6S9}.; . . . . 0.31434 . . . . . CFAP57 . . . cilia and flagella associated protein 57 . . . . . 0.22855 0.09210 0.404185162 76.48619958 . . CFAP58 . . . cilia and flagella associated protein 58 . . . . . 0.10404 . -0.347208386 29.59424393 . . CFAP58-AS1 . . . CFAP58 antisense RNA 1 (head to head) . . . . . . . . . . . CFAP61 . . . cilia and flagella associated protein 61 . . . . . 0.10925 . -0.227889677 36.86600613 . . CFAP65 . . . cilia and flagella associated protein 65 . . . . . 0.07665 . -1.85098044 2.040575607 . . CFAP69 . . . cilia and flagella associated protein 69 . . . . . . . 0.248041348 69.61547535 . . CFAP70 . . . cilia and flagella associated protein 70 . . . . . 0.10800 . 0.293954043 71.62066525 . . CFAP73 . . . cilia and flagella associated protein 73 . . . . . 0.18559 0.10293 1.133561642 92.28591649 . . CFAP74 . . . cilia and flagella associated protein 74 FUNCTION: As part of the central apparatus of the cilium axoneme may play a role in cilium movement. {ECO:0000250|UniProtKB:D4P3R7}.; . . . . 0.12614 0.09843 . . . . CFAP77 . . . cilia and flagella associated protein 77 . . . . . . . -0.310388054 32.14791224 . . CFAP97 . . . cilia and flagella associated protein 97 . . . . . 0.14344 . 0.356452144 74.62845011 . . CFAP99 . . . cilia and flagella associated protein 99 . . . . . . . . . . . CFAP100 . . . cilia and flagella associated protein 100 . . . . . 0.07433 0.08836 1.339294051 94.29700401 . . CFAP126 . . . cilia and flagella associated protein 126 FUNCTION: Acts as a regulator of cilium basal body docking and positioning in mono- and multiciliated cells. Regulates basal body docking and cilia formation in multiciliated lung cells. Regulates kinocilium positioning and stereocilia bundle morphogenesis in the inner ear. {ECO:0000250|UniProtKB:Q6P8X9}.; . . . . 0.03612 . 0.413500896 76.67492333 . . CFAP157 . . . cilia and flagella associated protein 157 . . . . . 0.29708 . -0.134019284 43.90776126 . . CFAP161 . . . cilia and flagella associated protein 161 FUNCTION: May play a role for motile cilia function, possibly by acting on dynein arm assembly. {ECO:0000250}.; . . . . 0.14057 . -0.648365105 16.35999056 . . CFAP206 . . . cilia and flagella associated protein 206 . . . . . 0.08121 0.34620 2.111097368 97.8945506 . . CFAP221 . . . cilia and flagella associated protein 221 FUNCTION: May play a role in cilium morphogenesis. {ECO:0000250|UniProtKB:A9Q751}.; . TISSUE SPECIFICITY: Expressed in ciliated respiratory epithelial cells and brain ependymal cells (at protein level). {ECO:0000269|PubMed:18039845}.; . . . . -0.220384297 37.6032083 . . CFB 0.000978859412496618 0.998916890451702 0.000104250135801357 complement factor B FUNCTION: Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase. It has also been implicated in proliferation and differentiation of preactivated B- lymphocytes, rapid spreading of peripheral blood monocytes, stimulation of lymphocyte blastogenesis and lysis of erythrocytes. Ba inhibits the proliferation of preactivated B-lymphocytes.; DISEASE: Hemolytic uremic syndrome atypical 4 (AHUS4) [MIM:612924]: An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. {ECO:0000269|PubMed:17182750, ECO:0000269|PubMed:20513133}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype.; DISEASE: Complement factor B deficiency (CFBD) [MIM:615561]: An immunologic disorder characterized by increased susceptibility to bacterial infections, particularly Neisseria infections, due to a defect in the alternative complement pathway. {ECO:0000269|PubMed:24152280}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.42920 . 1.642526957 96.14885586 579.86625 4.88072 CFC1 0.682601111382939 0.297960651922929 0.0194382366941312 cripto, FRL-1, cryptic family 1 FUNCTION: NODAL coreceptor involved in the correct establishment of the left-right axis. May play a role in mesoderm and/or neural patterning during gastrulation. {ECO:0000269|PubMed:11062482}.; DISEASE: Heterotaxy, visceral, 2, autosomal (HTX2) [MIM:605376]: A form of visceral heterotaxy, a complex disorder due to disruption of the normal left-right asymmetry of the thoracoabdominal organs. Visceral heterotaxy or situs ambiguus results in randomization of the placement of visceral organs, including the heart, lungs, liver, spleen, and stomach. The organs are oriented randomly with respect to the left-right axis and with respect to one another. It can been associated with variety of congenital defects including cardiac malformations. {ECO:0000269|PubMed:11062482, ECO:0000269|PubMed:11799476}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;islets of Langerhans;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;lung;macula lutea;testis;brain; . . 0.12797 . . 40.04529 1.17701 CFC1B . . . cripto, FRL-1, cryptic family 1B . . . unclassifiable (Anatomical System);heart;islets of Langerhans;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;lung;macula lutea;testis;brain; . . . . . 78.29011 1.86667 CFD 0.0195668736380904 0.738997461366736 0.241435664995173 complement factor D (adipsin) FUNCTION: Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway.; DISEASE: Complement factor D deficiency (CFDD) [MIM:613912]: An immunologic disorder characterized by increased susceptibility to bacterial infections, particularly Neisseria infections, due to a defect in the alternative complement pathway. {ECO:0000269|PubMed:16527897}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;choroid;skin;bone marrow;uterus;prostate;optic nerve;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;muscle;skeletal muscle;lung;trabecular meshwork;placenta;visual apparatus;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; adipose tissue;tongue;thyroid;appendix;skin; 0.15736 0.50020 . . 240.48233 3.35060 CFDP1 0.0849395818350133 0.905329010253314 0.00973140791167235 craniofacial development protein 1 FUNCTION: May play a role during embryogenesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9602175}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve;cerebellum; amygdala;testis - interstitial;subthalamic nucleus;medulla oblongata;olfactory bulb;hypothalamus;temporal lobe;prefrontal cortex;testis;globus pallidus;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.69235 0.12239 -0.115612493 45.12856806 45.52056 1.29597 CFH 0.99963096815145 0.000369031848233687 3.16263920963065e-13 complement factor H FUNCTION: Factor H functions as a cofactor in the inactivation of C3b by factor I and also increases the rate of dissociation of the C3bBb complex (C3 convertase) and the (C3b)NBB complex (C5 convertase) in the alternative complement pathway.; DISEASE: Complement factor H deficiency (CFHD) [MIM:609814]: A disorder that can manifest as several different phenotypes, including asymptomatic, recurrent bacterial infections, and renal failure. Laboratory features usually include decreased serum levels of factor H, complement component C3, and a decrease in other terminal complement components, indicating activation of the alternative complement pathway. It is associated with a number of renal diseases with variable clinical presentation and progression, including membranoproliferative glomerulonephritis and atypical hemolytic uremic syndrome. {ECO:0000269|PubMed:10803850, ECO:0000269|PubMed:11158219, ECO:0000269|PubMed:11170895, ECO:0000269|PubMed:11170896, ECO:0000269|PubMed:12020532, ECO:0000269|PubMed:14978182, ECO:0000269|PubMed:16612335, ECO:0000269|PubMed:9312129}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hemolytic uremic syndrome atypical 1 (AHUS1) [MIM:235400]: An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. {ECO:0000269|PubMed:10577907, ECO:0000269|PubMed:10762557, ECO:0000269|PubMed:11851332, ECO:0000269|PubMed:12960213, ECO:0000269|PubMed:14583443, ECO:0000269|PubMed:14978182, ECO:0000269|PubMed:20513133, ECO:0000269|PubMed:9551389}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype.; DISEASE: Macular degeneration, age-related, 4 (ARMD4) [MIM:610698]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. {ECO:0000269|PubMed:22019782}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; unclassifiable (Anatomical System);lymph node;cartilage;colon;skin;skeletal muscle;retina;uterus;prostate;lung;mesenchyma;nasopharynx;thyroid;placenta;liver;testis;head and neck;spleen;kidney;mammary gland;tonsil;stomach; fetal liver;olfactory bulb;tongue;liver;atrioventricular node;trigeminal ganglion; 0.10048 0.13588 0.519883383 80.37272942 1002.72313 6.09993 CFHR1 0.000909321621156627 0.939546192103835 0.0595444862750081 complement factor H related 1 FUNCTION: Involved in complement regulation. The dimerized forms have avidity for tissue-bound complement fragments and efficiently compete with the physiological complement inhibitor CFH. Can associate with lipoproteins and may play a role in lipid metabolism. {ECO:0000269|PubMed:23487775}.; . TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; myocardium;prostate;lung;heart;liver;hypopharynx;testis;spleen;head and neck;kidney;skeletal muscle;tonsil; . . . 0.773521534 87.06062751 76.68881 1.83843 CFHR2 8.62005163564686e-09 0.0442922045266078 0.95570778685334 complement factor H related 2 FUNCTION: Involved in complement regulation. The dimerized forms have avidity for tissue-bound complement fragments and efficiently compete with the physiological complement inhibitor CFH. Can associate with lipoproteins and may play a role in lipid metabolism. {ECO:0000269|PubMed:23487775}.; . TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; . . 0.04470 0.09243 1.348605238 94.30879925 356.0498 3.99341 CFHR3 1.21901547639532e-05 0.600194018750492 0.399793791094744 complement factor H related 3 FUNCTION: Might be involved in complement regulation.; . TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; . . 0.08896 . 1.728918179 96.55579146 393.42938 4.17191 CFHR4 1.898128871656e-13 0.0293589234003701 0.97064107659944 complement factor H related 4 FUNCTION: Involved in complement regulation. Can associate with lipoproteins and may play a role in lipid metabolism.; . TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; liver; . 0.06884 0.13477 . . 170.94001 2.85244 CFHR5 9.56874096632543e-22 7.26108602749637e-05 0.999927389139725 complement factor H related 5 FUNCTION: Involved in complement regulation. The dimerized forms have avidity for tissue-bound complement fragments and efficiently compete with the physiological complement inhibitor CFH. {ECO:0000269|PubMed:23487775}.; DISEASE: CFHR5 deficiency (CFHR5D) [MIM:614809]: A progressive disease characterized by glomerulonephritis, hematuria, renal failure, end-stage renal disease, subendothelial and mesangial glomerular C3 deposits, mesangial matrix expansion, increased glomerular cellularity, and segmental capillary wall thickening. Hematuria may become apparent after respiratory infections. {ECO:0000269|PubMed:20800271, ECO:0000269|PubMed:22503529}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; unclassifiable (Anatomical System);liver; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.04032 . 0.181903047 66.2361406 451.78199 4.42028 CFI 2.2377327985363e-05 0.995231631213004 0.00474599145901114 complement factor I FUNCTION: Responsible for cleaving the alpha-chains of C4b and C3b in the presence of the cofactors C4-binding protein and factor H respectively.; DISEASE: Complement factor I deficiency (CFI deficiency) [MIM:610984]: Autosomal recessive condition associated with a propensity to pyogenic infections. {ECO:0000269|PubMed:12562389, ECO:0000269|PubMed:17018561, ECO:0000269|PubMed:8613545}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Macular degeneration, age-related, 13 (ARMD13) [MIM:615439]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. {ECO:0000269|PubMed:23685748}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma.; . . 0.05419 . 0.823072022 88.03963199 104.98207 2.21508 CFL1 0.731049774850236 0.25669809836708 0.0122521267826839 cofilin 1 FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. {ECO:0000269|PubMed:15580268, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:23633677}.; . TISSUE SPECIFICITY: Widely distributed in various tissues.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;gum;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; subthalamic nucleus;thalamus;occipital lobe;fetal brain;cerebellum peduncles;spinal cord;temporal lobe;caudate nucleus;parietal lobe;cerebellum;bone marrow; 0.32676 0.14839 -0.185391282 39.67916962 25.72014 0.83717 CFL1P1 . . . cofilin 1 pseudogene 1 . . . . . . . . . . . CFL1P2 . . . cofilin 1 pseudogene 2 . . . . . . . . . . . CFL1P3 . . . cofilin 1 pseudogene 3 . . . . . . . . . . . CFL1P4 . . . cofilin 1 pseudogene 4 . . . . . . . . . . . CFL1P5 . . . cofilin 1 pseudogene 5 . . . . . . . . . . . CFL1P6 . . . cofilin 1 pseudogene 6 . . . . . . . . . . . CFL1P7 . . . cofilin 1 pseudogene 7 . . . . . . . . . . . CFL1P8 . . . cofilin 1 pseudogene 8 . . . . . . . . . . . CFL2 0.164507783006843 0.772902421761769 0.0625897952313883 cofilin 2 FUNCTION: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods (By similarity). {ECO:0000250}.; DISEASE: Nemaline myopathy 7 (NEM7) [MIM:610687]: A form of nemaline myopathy. Nemaline myopathies are muscular disorders characterized by muscle weakness of varying severity and onset, and abnormal thread-like or rod-shaped structures in muscle fibers on histologic examination. Nemaline myopathy type 7 presents at birth with hypotonia and generalized weakness. Major motor milestones are delayed, but independent ambulation is achieved. {ECO:0000269|PubMed:17160903}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform CFL2b is expressed predominantly in skeletal muscle and heart. Isoform CFL2a is expressed in various tissues.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;atrium;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;artery;spinal ganglion;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;hypothalamus;pineal body;lens;skeletal muscle;greater omentum;breast;lung;trabecular meshwork;placenta;hippocampus;macula lutea;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; medulla oblongata;trigeminal ganglion;skeletal muscle; 0.54857 0.17050 0.013025609 54.62962963 2.11009 0.06916 CFLAR 0.999719869699545 0.00028012982406973 4.76384868220149e-10 CASP8 and FADD like apoptosis regulator FUNCTION: Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells. Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruitment and processing of caspase-8 at the complex. Full length and shorter isoforms have been shown either to induce apoptosis or to reduce TNFRSF-triggered apoptosis. Lacks enzymatic (caspase) activity. {ECO:0000269|PubMed:9880531}.; . TISSUE SPECIFICITY: Widely expressed. Higher expression in skeletal muscle, pancreas, heart, kidney, placenta, and peripheral blood leukocytes. Also detected in diverse cell lines. Isoform 8 is predominantly expressed in testis and skeletal muscle.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;testis;bladder;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;breast;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;alveolus;hypopharynx;duodenum;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11181 0.48654 0.17280645 65.75843359 167.83206 2.82895 CFLAR-AS1 . . . CFLAR antisense RNA 1 . . . . . . . . . . . CFM1 . . . cystic fibrosis modifier 1 . . . . . . . . . . . CFM2 . . . cystic fibrosis modifier 2 . . . . . . . . . . . CFP 0.944168669031185 0.0557896303442584 4.17006245570596e-05 complement factor properdin FUNCTION: A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes. {ECO:0000269|PubMed:20382442}.; DISEASE: Properdin deficiency (PFD) [MIM:312060]: Results in higher susceptibility to bacterial infections; especially to meningococcal infections. Three phenotypes have been reported: complete deficiency (type I), incomplete deficiency (type II), and dysfunction of properdin (type III). {ECO:0000269|PubMed:10909851, ECO:0000269|PubMed:8871668, ECO:0000269|PubMed:9710744}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;ovary;nasopharynx;bone;pituitary gland;colon;spleen;blood;skeletal muscle;tonsil;aorta;bone marrow; white blood cells;whole blood;bone marrow; 0.14504 0.26817 0.350995466 74.37485256 78.28928 1.86633 CFTR 2.96390764420065e-36 5.19139474609909e-06 0.999994808605254 cystic fibrosis transmembrane conductance regulator FUNCTION: Involved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter. Can inhibit the chloride channel activity of ANO1. Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation. {ECO:0000269|PubMed:22178883}.; DISEASE: Cystic fibrosis (CF) [MIM:219700]: A common generalized disorder of the exocrine glands which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes. It is the most common genetic disease in Caucasians, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive. {ECO:0000269|PubMed:10094564, ECO:0000269|PubMed:1284466, ECO:0000269|PubMed:1284468, ECO:0000269|PubMed:1284529, ECO:0000269|PubMed:1284530, ECO:0000269|PubMed:1695717, ECO:0000269|PubMed:1710600, ECO:0000269|PubMed:2236053, ECO:0000269|PubMed:7504969, ECO:0000269|PubMed:7505694, ECO:0000269|PubMed:7513296, ECO:0000269|PubMed:7517264, ECO:0000269|PubMed:7520022, ECO:0000269|PubMed:7522211, ECO:0000269|PubMed:7524909, ECO:0000269|PubMed:7524913, ECO:0000269|PubMed:7525450, ECO:0000269|PubMed:7537150, ECO:0000269|PubMed:7541273, ECO:0000269|PubMed:7541510, ECO:0000269|PubMed:7543567, ECO:0000269|PubMed:7544319, ECO:0000269|PubMed:7581407, ECO:0000269|PubMed:7680525, ECO:0000269|PubMed:7683628, ECO:0000269|PubMed:7683954, ECO:0000269|PubMed:8081395, ECO:0000269|PubMed:8522333, ECO:0000269|PubMed:8723693, ECO:0000269|PubMed:8723695, ECO:0000269|PubMed:8800923, ECO:0000269|PubMed:8829633, ECO:0000269|PubMed:8956039, ECO:0000269|PubMed:9101301, ECO:0000269|PubMed:9222768, ECO:0000269|PubMed:9375855, ECO:0000269|PubMed:9401006, ECO:0000269|PubMed:9443874, ECO:0000269|PubMed:9452048, ECO:0000269|PubMed:9452054, ECO:0000269|PubMed:9452073, ECO:0000269|PubMed:9482579, ECO:0000269|PubMed:9521595, ECO:0000269|PubMed:9554753, ECO:0000269|PubMed:9736778, ECO:0000269|PubMed:9921909}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Congenital bilateral absence of the vas deferens (CBAVD) [MIM:277180]: Important cause of sterility in men and could represent an incomplete form of cystic fibrosis, as the majority of men suffering from cystic fibrosis lack the vas deferens. {ECO:0000269|PubMed:10651488, ECO:0000269|PubMed:7529962, ECO:0000269|PubMed:7539342, ECO:0000269|PubMed:9067761, ECO:0000269|Ref.77}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the respiratory airway, including bronchial epithelium, and in the female reproductive tract, including oviduct (at protein level). {ECO:0000269|PubMed:22207244}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;skeletal muscle;bile duct;uterus;pancreas;lung;endometrium;thyroid;liver;testis;kidney;brain;stomach; superior cervical ganglion;pancreas;salivary gland;beta cell islets;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.76593 0.87681 -0.50727808 21.73271998 637.50803 5.08064 CFTRP1 . . . cystic fibrosis transmembrane conductance regulator pseudogene 1 . . . . . . . . . . . CFTRP2 . . . cystic fibrosis transmembrane conductance regulator pseudogene 2 . . . . . . . . . . . CFTRP3 . . . cystic fibrosis transmembrane conductance regulator pseudogene 3 . . . . . . . . . . . CGA 0.251018987056367 0.641772158166849 0.107208854776784 glycoprotein hormones, alpha polypeptide . . . . . 0.00193 0.40525 -0.053113545 49.38664779 . . CGB1 0.267464648266522 0.636580491490247 0.0959548602432311 chorionic gonadotropin beta subunit 1 . . TISSUE SPECIFICITY: Expressed in placenta, testis and pituitary. {ECO:0000269|PubMed:16123088, ECO:0000269|PubMed:18048458}.; unclassifiable (Anatomical System);heart;ovary;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;lung;optic nerve;whole body;bone;placenta;macula lutea;liver;testis;spleen;mammary gland; . . 0.10495 0.591694063 82.45458835 1440.0355 7.07786 CGB2 0.0694219778865575 0.737727763754216 0.192850258359227 chorionic gonadotropin beta subunit 2 . . TISSUE SPECIFICITY: Expressed in placenta, testis and pituitary. {ECO:0000269|PubMed:16123088, ECO:0000269|PubMed:18048458}.; unclassifiable (Anatomical System);whole body;ovary;placenta;parathyroid; . 0.14166 . . . 1703.49158 7.61509 CGB3 . . . chorionic gonadotropin beta subunit 3 FUNCTION: Stimulates the ovaries to synthesize the steroids that are essential for the maintenance of pregnancy.; . TISSUE SPECIFICITY: Placenta.; . . . 0.09666 . . . . CGB5 . . . chorionic gonadotropin beta subunit 5 FUNCTION: Stimulates the ovaries to synthesize the steroids that are essential for the maintenance of pregnancy.; . TISSUE SPECIFICITY: Placenta.; unclassifiable (Anatomical System);heart;ovary;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;whole body;lung;placenta;bone;macula lutea;liver;testis;spleen;mammary gland; . . 0.14992 . . 16.20965 0.57491 CGB7 0.0131018383509561 0.660375879419502 0.326522282229542 chorionic gonadotropin beta subunit 7 FUNCTION: Stimulates the ovaries to synthesize the steroids that are essential for the maintenance of pregnancy.; . TISSUE SPECIFICITY: Placenta.; unclassifiable (Anatomical System);heart;ovary;parathyroid;skin;uterus;whole body;lung;placenta;bone;liver;testis;spleen;mammary gland; . 0.13856 0.10426 . . 1267.08809 6.70772 CGB8 0.0917779548101803 0.569050720769912 0.339171324419908 chorionic gonadotropin beta subunit 8 FUNCTION: Stimulates the ovaries to synthesize the steroids that are essential for the maintenance of pregnancy.; . TISSUE SPECIFICITY: Placenta.; unclassifiable (Anatomical System);heart;ovary;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;lung;optic nerve;whole body;bone;placenta;macula lutea;liver;testis;spleen;mammary gland; . . 0.08080 . . 2.44485 0.08929 CGF1 . . . cognitive function 1, social . . . . . . . . . . . CGGBP1 0.777631517643376 0.215081104287522 0.00728737806910147 CGG triplet repeat binding protein 1 FUNCTION: Binds to nonmethylated 5'-d(CGG)(n)-3' trinucleotide repeats in the FMR1 promoter. May play a role in regulating FMR1 promoter. {ECO:0000269|PubMed:9201980}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in placenta, thymus, lymph nodes, cerebellum and cerebral cortex. Low expression in other regions of the brain. {ECO:0000269|PubMed:14667814}.; unclassifiable (Anatomical System);smooth muscle;heart;ovary;islets of Langerhans;colon;parathyroid;blood;skin;skeletal muscle;uterus;lung;bone;placenta;liver;testis;spleen;germinal center;kidney;brain;mammary gland;bladder; dorsal root ganglion;testis - interstitial;medulla oblongata;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.22371 0.11109 0.013025609 54.62962963 . . CGN 1.82319246593754e-22 0.237908153615225 0.762091846384775 cingulin FUNCTION: Probably plays a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier.; . TISSUE SPECIFICITY: Localized on the cytoplasmic face of tight junctions of polarized epithelia and some endothelia. Expressed in pancreas, kidney, liver and lung, but not in skeletal muscle, placenta, brain or heart.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;larynx;thyroid;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;urinary;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;macula lutea;liver;spleen;head and neck;kidney;stomach;cerebellum; . 0.15256 0.40474 1.971402205 97.57018165 2222.88681 8.68735 CGNL1 9.04937499888625e-14 0.855742963998934 0.144257036000976 cingulin-like 1 FUNCTION: May be involved in anchoring the apical junctional complex, especially tight junctions, to actin-based cytoskeletons. {ECO:0000250}.; DISEASE: Aromatase excess syndrome (AEXS) [MIM:139300]: An autosomal dominant disorder characterized by increased extraglandular aromatization of steroids that presents with heterosexual precocity in males and isosexual precocity in females. {ECO:0000269|PubMed:12736278}. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration inv(15)(q21.2;q21.3) has been found in patients with aromatase excess syndrome. The inversion moves the promoter of the CGNL1 gene into a 5-prime position in relation to the aromatase coding region.; TISSUE SPECIFICITY: Smooth muscle, spleen, testis, fetal brain, amygdala, corpus callosum, cerebellum, thalamus and subthalamic nucleus of adult brain. {ECO:0000269|PubMed:11214970}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;cerebral cortex;thyroid;testis;amniotic fluid;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;cerebellum; 0.13429 0.11653 0.330582712 73.42533616 3729.74686 11.93373 CGREF1 5.50290788195318e-08 0.0678526181998291 0.932147326771092 cell growth regulator with EF-hand domain 1 FUNCTION: Mediates cell-cell adhesion in a calcium-dependent manner (By similarity). Able to inhibit growth in several cell lines. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;lacrimal gland;colon;fovea centralis;choroid;lens;skin;retina;bile duct;uterus;breast;prostate;optic nerve;larynx;placenta;macula lutea;liver;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05854 . 0.440999548 77.79547063 155.37089 2.72374 CGRRF1 0.00522692652830377 0.891018947381102 0.103754126090595 cell growth regulator with ring finger domain 1 FUNCTION: Able to inhibit growth in several cell lines. {ECO:0000250}.; . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;skin;retina;uterus;prostate;bone;pituitary gland;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;lymph node;heart;cartilage;islets of Langerhans;hypothalamus;pineal body;pancreas;pia mater;lung;nasopharynx;placenta;liver;spleen;kidney;stomach;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05190 0.10999 0.194852702 67.03231894 376.98998 4.09426 CH25H 0.342292545785796 0.599523979851094 0.0581834743631092 cholesterol 25-hydroxylase FUNCTION: Catalyzes the formation of 25-hydroxycholesterol from cholesterol, leading to repress cholesterol biosynthetic enzymes. May play an important role in regulating lipid metabolism by synthesizing a corepressor that blocks sterol regulatory element binding protein (SREBP) processing. In testis, production of 25- hydroxycholesterol by macrophages may play a role in Leydig cell differentiation. {ECO:0000269|PubMed:9852097}.; . . . . 0.07423 0.17210 -0.295622497 32.61972163 15.13195 0.54435 CHAC1 0.000276505596595412 0.552880868014169 0.446842626389236 ChaC glutathione-specific gamma-glutamylcyclotransferase 1 FUNCTION: Catalyzes the cleavage glutathione into 5-oxoproline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. Glutathione depletion is an important factor for apoptosis initiation and execution (PubMed:23070364). Acts as a pro-apoptotic component of the unfolded protein response pathway by mediating the pro-apoptotic effects of the ATF4-ATF3-DDIT3/CHOP cascade (PubMed:19109178). Negative regulator of Notch signaling pathway involved in embryonic neurogenesis: acts by inhibiting Notch cleavage by furin, maintaining Notch in an immature inactive form, thereby promoting neurogenesis in embryos (PubMed:22445366). {ECO:0000269|PubMed:19109178, ECO:0000269|PubMed:22445366, ECO:0000269|PubMed:23070364}.; . . . . 0.46912 0.13009 0.861712133 88.6883699 256.09913 3.44185 CHAC2 0.00282189031328415 0.573097879687431 0.424080229999285 ChaC, cation transport regulator homolog 2 (E. coli) FUNCTION: Catalyzes the cleavage glutathione into 5-oxoproline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. {ECO:0000250|UniProtKB:P32656}.; . . unclassifiable (Anatomical System);uterus;lung;cartilage;placenta;pituitary gland;testis;colon;germinal center;mammary gland;bladder;skin; ciliary ganglion;atrioventricular node; 0.09701 0.10581 -0.071520315 48.34866714 30.15884 0.96172 CHAD 0.0337024141100405 0.822675784739731 0.143621801150228 chondroadherin FUNCTION: Promotes attachment of chondrocytes, fibroblasts, and osteoblasts. This binding is mediated (at least for chondrocytes and fibroblasts) by the integrin alpha(2)beta(1). May play an important role in the regulation of chondrocyte growth and proliferation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Present in chondrocytes at all ages.; unclassifiable (Anatomical System);lung;whole body;cartilage;ovary;bone;placenta;liver;parathyroid;blood;kidney;brain; superior cervical ganglion;trachea;cerebellum peduncles;globus pallidus;pons;trigeminal ganglion;skeletal muscle; 0.30334 0.22429 0.330767508 73.53739089 425.4487 4.30986 CHADL 0.080813456311772 0.547907223446003 0.371279320242226 chondroadherin like FUNCTION: Potential negative modulator of chondrocyte differentiation. Inhibits collagen fibrillogenesis in vitro. May influence chondrocyte's differentiation by acting on its cellular collagenous microenvironment. {ECO:0000269|PubMed:25451920}.; . . unclassifiable (Anatomical System);heart;hypothalamus;sympathetic chain;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;endometrium;bone;macula lutea;hippocampus;iris;brain; dorsal root ganglion;whole brain;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node; 0.18127 . . . 1244.24795 6.66115 CHAF1A 0.996226225687986 0.00377376326141161 1.10506025927215e-08 chromatin assembly factor 1 subunit A FUNCTION: Core component of the CAF-1 complex, a complex thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. CHAF1A binds to histones H3 and H4. It may play a role in heterochromatin maintenance in proliferating cells by bringing newly synthesized cbx proteins to heterochromatic DNA replication foci (By similarity). {ECO:0000250, ECO:0000269|PubMed:15327775}.; . . ovary;foreskin;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;adrenal cortex;blood;lens;bile duct;breast;pancreas;lung;placenta;visual apparatus;macula lutea;liver;spleen;head and neck;stomach;thymus; superior cervical ganglion;tumor;testis;white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skin;skeletal muscle; 0.92481 0.11264 0.321464691 72.85326728 349.85937 3.96455 CHAF1B 0.536697059074058 0.463168158754694 0.000134782171248338 chromatin assembly factor 1 subunit B FUNCTION: Complex that is thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. {ECO:0000269|PubMed:9813080}.; . . unclassifiable (Anatomical System);lymph node;ovary;colon;skin;skeletal muscle;bone marrow;breast;uterus;prostate;lung;liver;testis;cervix;spleen;germinal center;brain;stomach;peripheral nerve; ciliary ganglion; 0.66554 0.08318 0.222355725 68.44184949 576.76315 4.86844 CHAMP1 0.985193951059278 0.0147983988635575 7.65007716419249e-06 chromosome alignment maintaining phosphoprotein 1 FUNCTION: Required for proper alignment of chromosomes at metaphase and their accurate segregation during mitosis. Involved in the maintenance of spindle microtubules attachment to the kinetochore during sister chromatid biorientation. May recruit CENPE and CENPF to the kinetochore. {ECO:0000269|PubMed:21063390}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;pharynx;blood;lens;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.12730 0.17514 -0.751322189 13.71196037 155.81284 2.72749 CHAT 0.014030306190231 0.985703376218921 0.000266317590848265 choline O-acetyltransferase FUNCTION: Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses.; DISEASE: Myasthenic syndrome, congenital, 6, presynaptic (CMS6) [MIM:254210]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS6 affected individuals have myasthenic symptoms since birth or early infancy, negative tests for anti-AChR antibodies, and abrupt episodic crises with increased weakness, bulbar paralysis, and apnea precipitated by undue exertion, fever, or excitement. CMS6 inheritance is autosomal recessive. {ECO:0000269|PubMed:11172068, ECO:0000269|PubMed:12756141}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.07895 0.53482 1.627768939 96.05449398 2403.82842 9.10029 CHCHD1 0.10383118057353 0.774404457936541 0.121764361489929 coiled-coil-helix-coiled-coil-helix domain containing 1 . . . . . 0.07868 0.08094 -0.031067188 51.03798066 5.33783 0.19785 CHCHD2 0.000221319937862802 0.505424469374743 0.494354210687394 coiled-coil-helix-coiled-coil-helix domain containing 2 FUNCTION: Transcription factor. Binds to the oxygen responsive element of COX4I2 and activates its transcription under hypoxia conditions (4% oxygen), as well as normoxia conditions (20% oxygen) (PubMed:23303788). {ECO:0000269|PubMed:23303788}.; . . . . 0.01573 0.10031 -0.119252484 44.53880632 46.6785 1.31938 CHCHD2P1 . . . coiled-coil-helix-coiled-coil-helix domain containing 2 pseudogene 1 . . . . . . . . . . . CHCHD2P2 . . . coiled-coil-helix-coiled-coil-helix domain containing 2 pseudogene 2 . . . . . . . . . . . CHCHD2P3 . . . coiled-coil-helix-coiled-coil-helix domain containing 2 pseudogene 3 . . . . . . . . . . . CHCHD2P4 . . . coiled-coil-helix-coiled-coil-helix domain containing 2 pseudogene 4 . . . . . . . . . . . CHCHD2P5 . . . coiled-coil-helix-coiled-coil-helix domain containing 2 pseudogene 5 . . . . . . . . . . . CHCHD2P6 . . . coiled-coil-helix-coiled-coil-helix domain containing 2 pseudogene 6 . . . . . . . . . . . CHCHD2P7 . . . coiled-coil-helix-coiled-coil-helix domain containing 2 pseudogene 7 . . . . . . . . . . . CHCHD2P8 . . . coiled-coil-helix-coiled-coil-helix domain containing 2 pseudogene 8 . . . . . . . . . . . CHCHD2P9 . . . coiled-coil-helix-coiled-coil-helix domain containing 2 pseudogene 9 . . . . . 0.15527 0.05549 . . . . CHCHD2P10 . . . coiled-coil-helix-coiled-coil-helix domain containing 2 pseudogene 10 . . . . . . . . . . . CHCHD2P11 . . . coiled-coil-helix-coiled-coil-helix domain containing 2 pseudogene 11 . . . . . . . . . . . CHCHD3 0.0404016311674061 0.953111503910602 0.00648686492199175 coiled-coil-helix-coiled-coil-helix domain containing 3 FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Has also been shown to function as a transcription factor which binds to the BAG1 promoter and represses BAG1 transcription. Plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology (PubMed:25781180). {ECO:0000269|PubMed:22567091, ECO:0000269|PubMed:25781180}.; . TISSUE SPECIFICITY: Detected at low levels in brain, placenta, lung, liver, kidney and pancreas with increased levels in heart and skeletal muscle. Higher expression in primary lung cancers than in normal lung tissue. {ECO:0000269|PubMed:22567091}.; myocardium;ovary;colon;parathyroid;skin;bone marrow;uterus;optic nerve;atrium;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;muscle;urinary;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.11621 0.10674 0.014844891 54.94810097 42.00576 1.22356 CHCHD3P1 . . . coiled-coil-helix-coiled-coil-helix domain containing 3 pseudogene 1 . . . . . . . . . . . CHCHD3P2 . . . coiled-coil-helix-coiled-coil-helix domain containing 3 pseudogene 2 . . . . . . . . . . . CHCHD3P3 . . . coiled-coil-helix-coiled-coil-helix domain containing 3 pseudogene 3 . . . . . . . . . . . CHCHD4 0.144674862711758 0.778679005618046 0.0766461316701954 coiled-coil-helix-coiled-coil-helix domain containing 4 FUNCTION: Functions as chaperone and catalyzes the formation of disulfide bonds in substrate proteins, such as COX17. Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS. Reduced CHCHD4/MIA40 is then reoxidized by GFER/ERV1 via a disulfide relay system. {ECO:0000269|PubMed:16185709, ECO:0000269|PubMed:19182799, ECO:0000269|PubMed:21059946, ECO:0000269|PubMed:23186364}.; . TISSUE SPECIFICITY: Expressed in all tissues tested, suggesting an ubiquitous expression. {ECO:0000269|PubMed:16185709}.; lymph node;heart;colon;blood;skin;breast;uterus;pancreas;prostate;lung;thyroid;placenta;iris;liver;testis;cervix;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.11564 0.09588 -0.007201372 53.19061099 24.3259 0.79910 CHCHD4P1 . . . coiled-coil-helix-coiled-coil-helix domain containing 4 pseudogene 1 . . . . . . . . . . . CHCHD4P2 . . . coiled-coil-helix-coiled-coil-helix domain containing 4 pseudogene 2 . . . . . . . . . . . CHCHD4P3 . . . coiled-coil-helix-coiled-coil-helix domain containing 4 pseudogene 3 . . . . . . . . . . . CHCHD4P4 . . . coiled-coil-helix-coiled-coil-helix domain containing 4 pseudogene 4 . . . . . . . . . . . CHCHD4P5 . . . coiled-coil-helix-coiled-coil-helix domain containing 4 pseudogene 5 . . . . . . . . . . . CHCHD5 0.0336410132342975 0.822454838498808 0.143904148266895 coiled-coil-helix-coiled-coil-helix domain containing 5 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland; testis - interstitial;testis;ciliary ganglion; 0.05169 . 0.125076652 62.7388535 44.38332 1.27239 CHCHD6 1.0801836127763e-08 0.0504583764801382 0.949541612718026 coiled-coil-helix-coiled-coil-helix domain containing 6 FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. {ECO:0000269|PubMed:22228767}.; . . colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;breast;lung;placenta;macula lutea;liver;duodenum;spleen;kidney;mammary gland;stomach; whole brain;testis - interstitial;subthalamic nucleus;superior cervical ganglion;occipital lobe;testis - seminiferous tubule;fetal brain;temporal lobe;testis;ciliary ganglion;atrioventricular node;parietal lobe; 0.11987 0.07959 0.751474114 86.64779429 2818.06229 10.01513 CHCHD7 0.387975837016134 0.569193029344385 0.0428311336394806 coiled-coil-helix-coiled-coil-helix domain containing 7 . DISEASE: Note=A chromosomal aberration involving CHCHD7 is found in salivary gland pleiomorphic adenomas, the most common benign epithelial tumors of the salivary gland. Translocation t(6;8)(p21.3-22;q13) with PLAG1. {ECO:0000269|PubMed:16736500}.; . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;testis;germinal center;bladder;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pineal body;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; amygdala;prefrontal cortex;pons;caudate nucleus; 0.19941 . -0.185391282 39.67916962 5.23664 0.19529 CHCHD10 0.000132412414863812 0.232143983884559 0.767723603700577 coiled-coil-helix-coiled-coil-helix domain containing 10 FUNCTION: May be involved in the maintenance of mitochondrial organization and mitochondrial cristae structure. {ECO:0000269|PubMed:24934289}.; DISEASE: Spinal muscular atrophy, Jokela type (SMAJ) [MIM:615048]: An autosomal dominant, slowly progressive, lower motor neuron disease. SMAJ is characterized by adult-onset of muscle cramps and fasciculations affecting the proximal and distal muscles of the upper and lower limbs. The disorder results in weakness and mild muscle atrophy later in life. {ECO:0000269|PubMed:25428574}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myopathy, isolated mitochondrial, autosomal dominant (IMMD) [MIM:616209]: A mitochondrial myopathy presenting with severe exercise intolerance, progressive proximal weakness, and lactic acidemia. The disorder is slowly progressive, with later involvement of facial muscles, muscles of the upper limbs, and distal muscles. {ECO:0000269|PubMed:25193783}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. Higher expression is observed in heart and liver. {ECO:0000269|PubMed:24934289}.; . . 0.22198 . . . 448.53321 4.40433 CHD1 0.999999999362856 6.37143867661318e-10 3.5017629230383e-25 chromodomain helicase DNA binding protein 1 FUNCTION: ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Is also associated with histone deacetylase (HDAC) activity (By similarity). Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3. Required for maintaining open chromatin and pluripotency in embryonic stem cells. {ECO:0000250, ECO:0000269|PubMed:18042460}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;artery;unclassifiable (Anatomical System);heart;hypothalamus;urinary;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;stomach;aorta;thymus; superior cervical ganglion;white blood cells;trigeminal ganglion;skeletal muscle; 0.88289 0.17305 -0.813834387 12.05472989 1749.76488 7.72416 CHD1L 1.05042366445767e-20 0.0151665061019938 0.984833493898006 chromodomain helicase DNA binding protein 1-like FUNCTION: DNA helicase which plays a role in chromatin-remodeling following DNA damage. Targeted to sites of DNA damage through interaction with poly(ADP-ribose) and functions to regulate chromatin during DNA repair. Able to catalyze nucleosome sliding in an ATP-dependent manner. Helicase activity is strongly stimulated upon poly(ADP-ribose)-binding. {ECO:0000269|PubMed:18023026, ECO:0000269|PubMed:19661379}.; . TISSUE SPECIFICITY: Frequently overexpressed in hepatomacellular carcinomas. {ECO:0000269|PubMed:18023026}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;salivary gland;colon;fovea centralis;skin;uterus;prostate;whole body;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.17016 0.12748 1.094934207 91.9143666 3413.85133 11.20476 CHD2 0.999999998845422 1.15457803976173e-09 1.23440328444422e-26 chromodomain helicase DNA binding protein 2 FUNCTION: DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. Involved in myogenesis via interaction with MYOD1: binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression (By similarity). {ECO:0000250}.; DISEASE: Epileptic encephalopathy, childhood-onset (EEOC) [MIM:615369]: A severe form of epilepsy characterized by onset of multiple seizure types in the first few years of life and associated with poor prognosis. Affected individuals have cognitive regression and intellectual disability. {ECO:0000269|PubMed:23708187}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;larynx;bone;thyroid;testis;dura mater;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);amygdala;meninges;heart;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pia mater;lung;adrenal gland;nasopharynx;placenta;liver;spleen;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.56985 0.10377 -1.745389579 2.37084218 175.7961 2.88554 CHD3 0.999999995517971 4.48202898706469e-09 1.37552354098271e-26 chromodomain helicase DNA binding protein 3 FUNCTION: Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. {ECO:0000269|PubMed:17626165, ECO:0000269|PubMed:9804427}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9688266}.; lymphoreticular;ovary;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;urinary;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;visual apparatus;hippocampus;liver;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;amygdala;prostate;thalamus;occipital lobe;fetal brain;prefrontal cortex;globus pallidus;caudate nucleus;parietal lobe;cingulate cortex; 0.81281 0.12928 -2.475079584 0.973106865 670.89222 5.17831 CHD4 0.999999998385354 1.61464556805023e-09 5.65374720227085e-27 chromodomain helicase DNA binding protein 4 FUNCTION: Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. {ECO:0000269|PubMed:17626165, ECO:0000269|PubMed:9804427}.; . . lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;muscle;blood;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; occipital lobe;superior cervical ganglion;medulla oblongata;tongue;cerebellum peduncles;caudate nucleus;pons;skeletal muscle;globus pallidus;kidney;trigeminal ganglion;parietal lobe;cerebellum; 0.80213 0.31816 -1.636932785 2.824958717 204.99058 3.09325 CHD5 0.999999995117076 4.88292427431668e-09 1.01094747486235e-23 chromodomain helicase DNA binding protein 5 FUNCTION: Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non- methylated 'Lys-4' of histone H3. Plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys- 27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. Tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. Downstream activated genes may include CDKN2A that positively regulates the p53/TP53 pathway, which in turn, prevents cell proliferation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. {ECO:0000269|PubMed:23948251}.; DISEASE: Note=Defects in CHD5 may be a cause of the development of cancers from epithelial, neural and hematopoietic origin. CHD5 is one of the missing genes in the del(1p36), a deletion which is extremely common in this type of cancers. A decrease of its expression, results in increased susceptibility of cells to Ras- mediated transformation in vitro and in vivo (PubMed:17289567). {ECO:0000269|PubMed:17289567}.; TISSUE SPECIFICITY: Preferentially expressed in total brain, fetal brain, and cerebellum. It is also moderately expressed in the adrenal gland and detected in testis. {ECO:0000269|PubMed:12592387, ECO:0000269|PubMed:21931736}.; unclassifiable (Anatomical System);hypothalamus;colon;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;lung;frontal lobe;placenta;macula lutea;testis;brain; amygdala;whole brain;superior cervical ganglion;testis - interstitial;occipital lobe;medulla oblongata;temporal lobe;atrioventricular node;pons;subthalamic nucleus;testis - seminiferous tubule;fetal brain;prefrontal cortex;globus pallidus;testis;parietal lobe;cingulate cortex; 0.29125 0.11641 -3.065544169 0.489502241 139.76253 2.57740 CHD6 0.99999999999754 2.46040166873133e-12 9.37905516820512e-32 chromodomain helicase DNA binding protein 6 FUNCTION: Probable chromatin-remodeling protein with a DNA- dependent ATPase activity. May play a role in transcription regulation, activating for instance, the transcription of specific genes in response to oxidative stress through interaction with NFE2L2. {ECO:0000269|PubMed:16314513}.; . TISSUE SPECIFICITY: Widely expressed.; unclassifiable (Anatomical System);cartilage;colon;blood;skeletal muscle;bone marrow;lung;thyroid;bone;hypopharynx;liver;head and neck;brain;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.82188 0.09955 -0.972178525 8.911299835 935.73763 5.93137 CHD7 0.999999999999751 2.49119737651019e-13 1.75144923185452e-33 chromodomain helicase DNA binding protein 7 FUNCTION: Probable transcription regulator. Maybe involved in the in 45S precursor rRNA production. {ECO:0000269|PubMed:22646239}.; DISEASE: Idiopathic scoliosis 3 (IS3) [MIM:608765]: An abnormality of the vertebral column in which patients develop lateral curvature of the spine of at least 10 degrees. {ECO:0000269|PubMed:17436250}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Hypogonadotropic hypogonadism 5 with or without anosmia (HH5) [MIM:612370]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:18834967, ECO:0000269|PubMed:21158681, ECO:0000269|PubMed:25077900}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues. {ECO:0000269|PubMed:15300250, ECO:0000269|PubMed:22646239}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;muscle;blood;skin;skeletal muscle;bone marrow;breast;lung;cerebral cortex;visual apparatus;liver;testis;spleen;germinal center;kidney;brain;thymus; superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.14151 0.13965 -2.924339304 0.566171267 549.4743 4.76744 CHD8 0.999999999998095 1.90551347864159e-12 5.03265001946919e-32 chromodomain helicase DNA binding protein 8 FUNCTION: DNA helicase that acts as a chromatin remodeling factor and regulates transcription. Acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. Suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity. Acts as a negative regulator of Wnt signaling pathway by regulating beta-catenin (CTNNB1) activity. Negatively regulates CTNNB1- targeted gene expression by being recruited specifically to the promoter regions of several CTNNB1 responsive genes. Involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. Acts as a suppressor of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. Also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. {ECO:0000269|PubMed:17938208, ECO:0000269|PubMed:18378692}.; DISEASE: Autism 18 (AUTS18) [MIM:615032]: A complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation. {ECO:0000269|PubMed:23160955}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . ovary;adrenal medulla;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;alveolus;liver;amnion;spleen;head and neck;cervix;kidney;stomach; subthalamic nucleus;prefrontal cortex;testis;skeletal muscle; 0.71112 0.12031 -2.337343807 1.179523473 1658.00577 7.52499 CHD9 0.999999928588994 7.14110061851142e-08 9.66753834020148e-26 chromodomain helicase DNA binding protein 9 FUNCTION: Acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. Proposed to be a ATP-dependent chromatin remodeling protein. Has DNA-dependent ATPase activity and binds to A/T-rich DNA. Associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:16095617, ECO:0000269|PubMed:16554032}.; . TISSUE SPECIFICITY: Widely expressed at low levels. In bone marrow, expression is restricted to osteoprogenitor cells adjacent to mature osteoblasts. {ECO:0000269|PubMed:16095617, ECO:0000269|PubMed:16554032}.; ovary;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;prefrontal cortex;globus pallidus;atrioventricular node;trigeminal ganglion;skin; 0.85887 0.14890 -2.179347661 1.403632932 1762.91651 7.75186 CHDH 0.00530866013391797 0.96947436631611 0.0252169735499723 choline dehydrogenase . . . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;retina;lung;placenta;liver;testis;spleen;cervix;kidney;brain;mammary gland;stomach;cerebellum; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.15161 0.17742 -0.490397599 22.50530786 2539.65628 9.41076 CHED1 . . . corneal endothelial dystrophy 1 (autosomal dominant) . . . . . . . . . . . CHEK1 0.000249110252826237 0.982312119245349 0.0174387705018243 checkpoint kinase 1 FUNCTION: Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome. Recognizes the substrate consensus sequence [R-X-X-S/T]. Binds to and phosphorylates CDC25A, CDC25B and CDC25C. Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C. Phosphorylation of CDC25A at 'Ser-76', 'Ser- 124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A. Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A. Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. Also phosphorylates NEK6. Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination. Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation. Also promotes repair of DNA cross-links through phosphorylation of FANCE. Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A. This may enhance chromatin assembly both in the presence or absence of DNA damage. May also play a role in replication fork maintenance through regulation of PCNA. May regulate the transcription of genes that regulate cell- cycle progression through the phosphorylation of histones. Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes. May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest.; . TISSUE SPECIFICITY: Expressed ubiquitously with the most abundant expression in thymus, testis, small intestine and colon. {ECO:0000269|PubMed:9278511, ECO:0000269|PubMed:9382850}.; unclassifiable (Anatomical System);prostate;pancreas;lymph node;lung;bone;placenta;visual apparatus;liver;testis;colon;cervix;spleen;germinal center;brain; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.99413 0.52680 -0.315847836 31.68789809 581.70191 4.88824 CHEK2 1.18301128459806e-15 0.00551893618037752 0.994481063819621 checkpoint kinase 2 FUNCTION: Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest, activation of DNA repair and apoptosis in response to the presence of DNA double-strand breaks. May also negatively regulate cell cycle progression during unperturbed cell cycles. Following activation, phosphorylates numerous effectors preferentially at the consensus sequence [L-X- R-X-X-S/T]. Regulates cell cycle checkpoint arrest through phosphorylation of CDC25A, CDC25B and CDC25C, inhibiting their activity. Inhibition of CDC25 phosphatase activity leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. May also phosphorylate NEK6 which is involved in G2/M cell cycle arrest. Regulates DNA repair through phosphorylation of BRCA2, enhancing the association of RAD51 with chromatin which promotes DNA repair by homologous recombination. Also stimulates the transcription of genes involved in DNA repair (including BRCA2) through the phosphorylation and activation of the transcription factor FOXM1. Regulates apoptosis through the phosphorylation of p53/TP53, MDM4 and PML. Phosphorylation of p53/TP53 at 'Ser-20' by CHEK2 may alleviate inhibition by MDM2, leading to accumulation of active p53/TP53. Phosphorylation of MDM4 may also reduce degradation of p53/TP53. Also controls the transcription of pro-apoptotic genes through phosphorylation of the transcription factor E2F1. Tumor suppressor, it may also have a DNA damage-independent function in mitotic spindle assembly by phosphorylating BRCA1. Its absence may be a cause of the chromosomal instability observed in some cancer cells. Promotes the CCAR2-SIRT1 association and is required for CCAR2-mediated SIRT1 inhibition (PubMed:25361978). {ECO:0000250|UniProtKB:Q9Z265, ECO:0000269|PubMed:10097108, ECO:0000269|PubMed:10724175, ECO:0000269|PubMed:11298456, ECO:0000269|PubMed:12402044, ECO:0000269|PubMed:12607004, ECO:0000269|PubMed:12717439, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:16163388, ECO:0000269|PubMed:17101782, ECO:0000269|PubMed:17380128, ECO:0000269|PubMed:17715138, ECO:0000269|PubMed:18317453, ECO:0000269|PubMed:18644861, ECO:0000269|PubMed:18728393, ECO:0000269|PubMed:20364141, ECO:0000269|PubMed:25361978, ECO:0000269|PubMed:25619829, ECO:0000269|PubMed:9836640, ECO:0000269|PubMed:9889122}.; DISEASE: Li-Fraumeni syndrome 2 (LFS2) [MIM:609265]: A highly penetrant familial cancer syndrome that in its classic form is defined by the existence of a proband affected by a sarcoma before 45 years with a first degree relative affected by any tumor before 45 years and another first degree relative with any tumor before 45 years or a sarcoma at any age. Other clinical definitions for LFS have been proposed (PubMed:8118819 and PubMed:8718514) and called Li-Fraumeni like syndrome (LFL). In these families affected relatives develop a diverse set of malignancies at unusually early ages. Four types of cancers account for 80% of tumors occurring in TP53 germline mutation carriers: breast cancers, soft tissue and bone sarcomas, brain tumors (astrocytomas) and adrenocortical carcinomas. Less frequent tumors include choroid plexus carcinoma or papilloma before the age of 15, rhabdomyosarcoma before the age of 5, leukemia, Wilms tumor, malignant phyllodes tumor, colorectal and gastric cancers. {ECO:0000269|PubMed:11719428}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Prostate cancer (PC) [MIM:176807]: A malignancy originating in tissues of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma. {ECO:0000269|PubMed:12533788}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Osteogenic sarcoma (OSRC) [MIM:259500]: A sarcoma originating in bone-forming cells, affecting the ends of long bones. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:12094328, ECO:0000269|PubMed:21618645, ECO:0000269|PubMed:25619829}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. {ECO:0000269|PubMed:12094328}.; TISSUE SPECIFICITY: High expression is found in testis, spleen, colon and peripheral blood leukocytes. Low expression is found in other tissues.; lymphoreticular;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;thyroid;testis;brain;unclassifiable (Anatomical System);heart;lacrimal gland;muscle;lens;skeletal muscle;breast;lung;placenta;visual apparatus;macula lutea;duodenum;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.98514 0.65565 -0.134019284 43.90776126 138.54243 2.56375 CHEK2P1 . . . checkpoint kinase 2 pseudogene 1 . . . . . . . . . . . CHEK2P2 . . . checkpoint kinase 2 pseudogene 2 . . . . . . . . . . . CHEK2P3 . . . checkpoint kinase 2 pseudogene 3 . . . . . . . . . . . CHEK2P4 . . . checkpoint kinase 2 pseudogene 4 . . . . . . . . . . . CHEK2P5 . . . checkpoint kinase 2 pseudogene 5 . . . . . . . . . . . CHERP 0.999988395698518 1.16043012783678e-05 2.0401946648845e-13 calcium homeostasis endoplasmic reticulum protein FUNCTION: Involved in calcium homeostasis, growth and proliferation. {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674}.; . TISSUE SPECIFICITY: Expressed in brain, placenta, lung, liver, kidney, pancreas, cardiac and skeletal muscle, and in cultured HEL and Dami cells. {ECO:0000269|PubMed:10794731}.; myocardium;medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;muscle;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.24899 0.11740 -1.087493118 7.106628922 30.28923 0.96588 CHES1L1 . . . checkpoint suppressor 1-like 1 . . . . . . . . . . . CHFR 0.636712516541035 0.363229145348761 5.83381102039556e-05 checkpoint with forkhead and ring finger domains, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress. {ECO:0000269|PubMed:10935642, ECO:0000269|PubMed:11807090, ECO:0000269|PubMed:11912157, ECO:0000269|PubMed:14562038, ECO:0000269|PubMed:14694445, ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:19182791}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10935642}.; smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;urinary;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.09139 0.16119 -0.398573136 26.92852088 5112.56665 14.69811 CHGA 0.000145486160271026 0.863557512538814 0.136297001300915 chromogranin A FUNCTION: Pancreastatin: Strongly inhibits glucose induced insulin release from the pancreas.; FUNCTION: Serpinin: Regulates granule biogenesis in endocrine cells by up-regulating the transcription of protease nexin 1 (SERPINE2) via a cAMP-PKA-SP1 pathway. This leads to inhibition of granule protein degradation in the Golgi complex which in turn promotes granule formation. {ECO:0000250|UniProtKB:P26339}.; . TISSUE SPECIFICITY: GE-25 is found in the brain. {ECO:0000269|PubMed:7535395}.; unclassifiable (Anatomical System);medulla oblongata;ovary;islets of Langerhans;hypothalamus;colon;parathyroid;skeletal muscle;breast;pancreas;prostate;lung;oesophagus;endometrium;adrenal gland;thyroid;placenta;visual apparatus;hippocampus;pituitary gland;testis;brain; amygdala;whole brain;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;beta cell islets;adrenal cortex;pons;subthalamic nucleus;adrenal gland;thyroid;prefrontal cortex;globus pallidus;testis;parietal lobe;pituitary;cingulate cortex; 0.49169 0.48671 2.107460923 97.88275537 2325.30715 8.93037 CHGB 3.81635895457789e-07 0.803089035200301 0.196910583163803 chromogranin B FUNCTION: Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides.; . TISSUE SPECIFICITY: Expressed in the adrenal medulla, and in pheochromocytoma. Not expressed in liver. {ECO:0000269|PubMed:3608978}.; . . 0.20044 0.28630 1.936492053 97.50530786 1056.95038 6.24245 CHI3L1 0.00112581158404786 0.953457130781124 0.0454170576348277 chitinase 3 like 1 FUNCTION: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia-induced injury, inflammation and epithelial apoptosis in lung. {ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:19414556, ECO:0000269|PubMed:20558631, ECO:0000269|PubMed:9492324}.; DISEASE: Asthma-related traits 7 (ASRT7) [MIM:611960]: Asthma- related traits include clinical symptoms of asthma, such as coughing, wheezing, dyspnea, bronchial hyperresponsiveness as assessed by methacholine challenge test, serum IgE levels, atopy and atopic dermatitis. {ECO:0000269|PubMed:18403759}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Present in activated macrophages, articular chondrocytes, synovial cells as well as in liver. Very low or undetectable expression in non-inflammatory colon. Undetectable in muscle tissues, lung, pancreas, mononuclear cells, or fibroblasts. {ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:9492324}.; lymphoreticular;ovary;adrenal medulla;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;endometrium;thyroid;bone;iris;pituitary gland;brain;unclassifiable (Anatomical System);cartilage;nervous;islets of Langerhans;blood;breast;pancreas;lung;cornea;nasopharynx;trabecular meshwork;placenta;liver;alveolus;spleen;cervix;kidney;mammary gland; subthalamic nucleus;uterus corpus;fetal brain;trachea;temporal lobe;prefrontal cortex;whole blood;bone marrow; 0.15781 0.34859 -0.132199953 43.97853267 3958.24154 12.44829 CHI3L2 6.54220595861069e-07 0.452264863189023 0.547734482590381 chitinase 3 like 2 FUNCTION: Lectin that binds chitooligosaccharides and other glycans with high affinity, but not heparin. Has no chitinase activity. {ECO:0000269|PubMed:22742450}.; . TISSUE SPECIFICITY: Highest expression in chondrocytes, followed by synoviocytes, lung and heart. Not detected in spleen, pancreas, and liver. May also be expressed in developing brain and placenta. {ECO:0000269|PubMed:8702629}.; . . 0.22006 0.11479 0.154398214 64.73814579 837.33597 5.66721 CHIA 2.25649100389894e-15 0.00419303678363615 0.995806963216362 chitinase, acidic FUNCTION: Degrades chitin and chitotriose. May participate in the defense against nematodes, fungi and other pathogens. Plays a role in T-helper cell type 2 (Th2) immune response. Contributes to the response to IL-13 and inflammation in response to IL-13. Stimulates chemokine production by pulmonary epithelial cells. Protects lung epithelial cells against apoptosis and promotes phosphorylation of AKT1. Its function in the inflammatory response and in protecting cells against apoptosis is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding. {ECO:0000269|PubMed:11085997, ECO:0000269|PubMed:18824549, ECO:0000269|PubMed:19342690, ECO:0000269|PubMed:19435888}.; . TISSUE SPECIFICITY: Detected in lung epithelial cells from asthma patients (at protein level). Highly expressed in stomach. Detected at lower levels in lung. {ECO:0000269|PubMed:11085997, ECO:0000269|PubMed:15192232}.; unclassifiable (Anatomical System);thyroid;colon;kidney;stomach; superior cervical ganglion;trigeminal ganglion; 0.07747 0.21748 2.094522466 97.86506251 6584.17877 17.13833 CHIAP1 . . . chitinase, acidic pseudogene 1 . . . . . . . . . . . CHIAP2 . . . chitinase, acidic pseudogene 2 . . . . . . . . . . . CHIAP3 . . . chitinase, acidic pseudogene 3 . . . . . . . . . . . CHIC1 0.684233596256066 0.296608202844851 0.0191582008990833 cysteine rich hydrophobic domain 1 . . TISSUE SPECIFICITY: Equally expressed in various parts of the brain. {ECO:0000269|PubMed:9321471}.; . . 0.37183 0.10564 0.057118534 57.99716914 3.30005 0.11954 CHIC2 0.344123665599696 0.642069564419272 0.0138067699810317 cysteine rich hydrophobic domain 2 . DISEASE: Note=A chromosomal aberration involving CHIC2 is found in a form of acute myeloid leukemia (AML). Translocation t(4;12)(q12;p13) with ETV6. {ECO:0000269|PubMed:10477709}.; . unclassifiable (Anatomical System);medulla oblongata;smooth muscle;cartilage;heart;ovary;colon;skin;uterus;breast;prostate;lung;frontal lobe;internal ear;trabecular meshwork;bone;placenta;thyroid;testis;germinal center;kidney;brain; testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node; 0.73395 0.17050 -0.163345027 41.24793583 4.8354 0.17814 CHID1 0.000725517070552349 0.980774344381303 0.0185001385481445 chitinase domain containing 1 FUNCTION: Saccharide- and LPS-binding protein with possible roles in pathogen sensing and endotoxin neutralization. Ligand-binding specificity relates to the length of the oligosaccharides, with preference for chitotetraose (in vitro). {ECO:0000269|PubMed:20724479}.; . TISSUE SPECIFICITY: Expressed in cells of monocytic, T, B and epithelial origin. {ECO:0000269|PubMed:16357325, ECO:0000269|PubMed:20724479}.; myocardium;medulla oblongata;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;liver;testis;ciliary ganglion;trigeminal ganglion; 0.17908 0.11620 -0.178111357 40.44585987 202.72224 3.07292 CHIT1 1.39253489248215e-09 0.194396164480591 0.805603834126874 chitinase 1 FUNCTION: Degrades chitin, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens. Isoform 3 has no enzymatic activity. {ECO:0000269|PubMed:7592832, ECO:0000269|PubMed:7836450}.; . TISSUE SPECIFICITY: Detected in spleen. Secreted by cultured macrophages. {ECO:0000269|PubMed:7836450}.; lung;cartilage;heart;thyroid;adrenal cortex;blood;brain;bone marrow; superior cervical ganglion;lymph node;globus pallidus;appendix;caudate nucleus;bone marrow; 0.10775 0.26370 1.045368744 91.31870724 6092.53872 16.32360 CHKA 0.787088146901824 0.212854003968981 5.7849129195517e-05 choline kinase alpha FUNCTION: Has a key role in phospholipid biosynthesis and may contribute to tumor cell growth. Catalyzes the first step in phosphatidylcholine biosynthesis. Contributes to phosphatidylethanolamine biosynthesis. Phosphorylates choline and ethanolamine. Has higher activity with choline. {ECO:0000269|PubMed:19915674}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland; occipital lobe;thalamus;testis - interstitial;testis - seminiferous tubule;hypothalamus;prefrontal cortex;testis;caudate nucleus;parietal lobe; 0.21037 0.26106 -0.426079032 25.36565228 36.30666 1.08739 CHKB 0.000644971493148547 0.977620566480545 0.0217344620263065 choline kinase beta FUNCTION: Has a key role in phospholipid biosynthesis. Catalyzes the first step in phosphatidylethanolamine biosynthesis. Phosphorylates ethanolamine, and can also act on choline (in vitro). Has higher activity with ethanolamine. May not significantly contribute to in vivo phosphatidylcholine biosynthesis. {ECO:0000269|PubMed:19915674}.; . . . . 0.11329 0.12116 -0.314027422 31.9297004 31.52304 0.99287 CHKB-AS1 . . . CHKB antisense RNA 1 (head to head) . . . . . . . . . . . CHKB-CPT1B . . . CHKB-CPT1B readthrough (NMD candidate) . . . . . . . . . . . CHL1 2.05381563644969e-06 0.999947701118656 5.02450657077711e-05 cell adhesion molecule L1 like FUNCTION: Extracellular matrix and cell adhesion protein that plays a role in nervous system development and in synaptic plasticity. Both soluble and membranous forms promote neurite outgrowth of cerebellar and hippocampal neurons and suppress neuronal cell death. Plays a role in neuronal positioning of pyramidal neurons and in regulation of both the number of interneurons and the efficacy of GABAergic synapses. May play a role in regulating cell migration in nerve regeneration and cortical development. Potentiates integrin-dependent cell migration towards extracellular matrix proteins. Recruits ANK3 to the plasma membrane (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the fetal and adult brain as well as in Schwann cell culture. Also detected in adult peripheral tissues. {ECO:0000269|PubMed:9799093}.; unclassifiable (Anatomical System);amygdala;medulla oblongata;ovary;fovea centralis;choroid;lens;skeletal muscle;skin;retina;optic nerve;whole body;lung;frontal lobe;placenta;bone;macula lutea;amniotic fluid;kidney;spinal ganglion;mammary gland;brain;aorta;peripheral nerve; amygdala;superior cervical ganglion;medulla oblongata;subthalamic nucleus;occipital lobe;olfactory bulb;fetal brain;prefrontal cortex;globus pallidus;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex; 0.39224 0.09664 -0.158112528 41.92026421 1165.89885 6.49553 CHL1-AS1 . . . CHL1 antisense RNA 1 . . . . . . . . . . . CHL1-AS2 . . . CHL1 antisense RNA 2 . . . . . . . . . . . CHM 0.997851014105269 0.00214891758331524 6.83114153841495e-08 CHM, Rab escort protein 1 FUNCTION: Substrate-binding subunit of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B composed of RABGGTA and RABGGTB, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Besides, a pre-formed complex consisting of CHM and the Rab GGTase dimer (RGGT or component B) can bind to and prenylate Rab proteins; this alternative pathway is proposed to be the predominant pathway for Rab protein geranylgeranylation. {ECO:0000269|PubMed:18532927, ECO:0000269|PubMed:7957092}.; DISEASE: Choroideremia (CHM) [MIM:303100]: An X-linked recessive disease characterized by a slowly progressive degeneration of the choroid, photoreceptors, and retinal pigment epithelium. Affected males develop night blindness in their teenage years followed by loss of peripheral vision and complete blindness at middle age. Carrier females are generally asymptomatic but funduscopic examination often shows patchy areas of chorioretinal atrophy. {ECO:0000269|PubMed:19427510, ECO:0000269|PubMed:21905166, ECO:0000269|PubMed:7951216}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);breast;uterus;lung;nasopharynx;urinary;blood;kidney;mammary gland;bladder;skeletal muscle; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.13327 0.24490 0.174625237 65.9648502 151.57478 2.69185 CHML 0.0011577797146624 0.840330863639818 0.158511356645519 choroideremia-like (Rab escort protein 2) FUNCTION: Substrate-binding subunit (component A) of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Less effective than CHM in supporting prenylation of Rab3 family. {ECO:0000269|PubMed:12356470, ECO:0000269|PubMed:15186776, ECO:0000269|PubMed:8294464}.; . . . . 0.15030 . -0.376526807 28.10804435 160.16455 2.76258 CHMP1A 0.252036809419505 0.719472861586133 0.0284903289943623 charged multivesicular body protein 1A FUNCTION: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT- III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. May also be involved in chromosome condensation. Targets the Polycomb group (PcG) protein BMI1/PCGF4 to regions of condensed chromatin. May play a role in stable cell cycle progression and in PcG gene silencing. {ECO:0000269|PubMed:11559747, ECO:0000269|PubMed:11559748, ECO:0000269|PubMed:19129479, ECO:0000269|PubMed:23045692}.; DISEASE: Pontocerebellar hypoplasia 8 (PCH8) [MIM:614961]: An autosomal recessive neurodevelopmental disorder characterized by severe psychomotor retardation, abnormal movements, hypotonia, spasticity, and variable visual defects. Brain MRI shows pontocerebellar hypoplasia, decreased cerebral white matter, and a thin corpus callosum. {ECO:0000269|PubMed:23023333}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in placenta, cultured skin fibroblasts and in osteoblast cell line MG-63. {ECO:0000269|PubMed:8863740}.; lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;gum;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;epididymis;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;pancreas;lung;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; temporal lobe;testis; 0.08801 . 0.150760231 64.51403633 463.07131 4.46040 CHMP1AP1 . . . charged multivesicular body protein 1A pseudogene 1 . . . . . . . . . . . CHMP1B 0.682019462509046 0.298441845976941 0.0195386915140122 charged multivesicular body protein 1B FUNCTION: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT- III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells. Involved in HIV-1 p6- and p9-dependent virus release. {ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:19129479}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in pancreas, kidney, skeletal muscle, liver, lung, placenta and brain. {ECO:0000269|PubMed:11474171}.; . . 0.11336 . -0.053113545 49.38664779 24.44413 0.80418 CHMP1B2P . . . charged multivesicular body protein 1B2, pseudogene . . . . . . . . . . . CHMP2A 0.906239123113201 0.0930019102923397 0.000758966594459612 charged multivesicular body protein 2A FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV- 1 p6- and p9-dependent virus release. {ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844}.; . . ovary;skin;bone marrow;retina;prostate;cochlea;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;placenta;hippocampus;duodenum;kidney;stomach;aorta; liver; 0.12954 0.12971 -0.207437529 38.2814343 . . CHMP2B 0.0130803147575514 0.95408338040058 0.0328363048418688 charged multivesicular body protein 2B FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4.; DISEASE: Frontotemporal dementia, chromosome 3-linked (FTD3) [MIM:600795]: Characterized by an onset of dementia in the late 50's initially characterized by behavioral and personality changes including apathy, restlessness, disinhibition and hyperorality, progressing to stereotyped behaviors, non-fluent aphasia, mutism and dystonia, with a marked lack of insight. The brains of individuals with FTD3 have no distinctive neuropathological features. They show global cortical and central atrophy, but no beta-amyloid deposits. {ECO:0000269|PubMed:16041373}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Amyotrophic lateral sclerosis 17 (ALS17) [MIM:614696]: An adult-onset progressive neurodegenerative disorder with predominantly lower motor neuron involvement, manifest as muscle weakness and wasting of the upper and lower limbs, bulbar signs, and respiratory insufficiency. {ECO:0000269|PubMed:16807408, ECO:0000269|PubMed:20352044}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart, skeletal muscle, spleen, kidney, liver, small intestine, pancreas, lung, placenta and leukocytes. In brain, it is expressed in cerebellum, cerebral cortex, medulla, spinal chord, occipital lobe, frontal lobe, temporal lobe and putamen. {ECO:0000269|PubMed:16041373}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;urinary;adrenal cortex;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;dorsal root ganglion;superior cervical ganglion;thyroid; 0.34759 0.14616 -0.161524709 41.6430762 64.34083 1.64511 CHMP3 0.036245866120423 0.928593238160349 0.0351608957192276 charged multivesicular body protein 3 FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor. Isoform 2 prevents stress- mediated cell death and accumulation of reactive oxygen species when expressed in yeast cells. {ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:15707591, ECO:0000269|PubMed:16740483, ECO:0000269|PubMed:17331679, ECO:0000269|PubMed:18076377}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:15632132}.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;uterus;whole body;oesophagus;cerebral cortex;larynx;bone;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; amygdala;superior cervical ganglion;globus pallidus;caudate nucleus;trigeminal ganglion; 0.19301 0.10828 -0.273576253 33.97027601 11.92132 0.43229 CHMP4A 1.26405702868177e-06 0.20883957342649 0.791159162516481 charged multivesicular body protein 4A FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4A filaments can promote or stabilize negative curvature and outward budding. Via its interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus release. {ECO:0000269|PubMed:12860994, ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:14583093, ECO:0000269|PubMed:18209100}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in heart, kidney, liver and skeletal muscle. Also expressed in brain, placenta, lung and pancreas. {ECO:0000269|PubMed:14678797}.; unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;blood;skin;uterus;prostate;lung;testis;germinal center;kidney; thalamus;hypothalamus;prefrontal cortex;white blood cells;pons;caudate nucleus;trigeminal ganglion;parietal lobe; 0.13642 0.07991 0.262810045 70.43524416 555.64646 4.78812 CHMP4B 0.881585919417872 0.117031954575512 0.00138212600661601 charged multivesicular body protein 4B FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. Via its interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus release. {ECO:0000269|PubMed:12860994, ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:18209100}.; DISEASE: Cataract 31, multiple types (CTRCT31) [MIM:605387]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT31 includes posterior polar, progressive posterior subcapsular, nuclear, and anterior subcapsular cataracts. {ECO:0000269|PubMed:17701905}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in heart and skeletal muscle. Also expressed in brain, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood lymphocytes. {ECO:0000269|PubMed:14678797}.; myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach; whole brain;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.64334 0.10911 -0.075159878 47.78839349 4.93362 0.18300 CHMP4BP1 . . . charged multivesicular body protein 4B pseudogene 1 . . . . . . . . . . . CHMP4C 0.00183040997493416 0.900883906987094 0.097285683037972 charged multivesicular body protein 4C FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: upon phosphorylation by AURKB, together with ZFYVE19/ANCHR, retains abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. Deactivation of AURKB results in dephosphorylation of CHMP4C followed by its dissociation from ANCHR and VPS4 and subsequent abscission (PubMed:22422861, PubMed:24814515). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV- 1 p6- and p9-dependent virus release. {ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:22422861, ECO:0000269|PubMed:24814515}.; . TISSUE SPECIFICITY: Expressed in heart, spleen and kidney. {ECO:0000269|PubMed:14583093, ECO:0000269|PubMed:14678797}.; unclassifiable (Anatomical System);lymph node;islets of Langerhans;colon;parathyroid;blood;skeletal muscle;breast;uterus;pancreas;prostate;lung;endometrium;bone;thyroid;placenta;head and neck;spleen;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.23325 0.12570 0.104848986 61.49445624 426.98874 4.31706 CHMP5 0.259054926516174 0.735105231768753 0.00583984171507293 charged multivesicular body protein 5 FUNCTION: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT- III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release. {ECO:0000269|PubMed:14519844}.; . . smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;ciliary ganglion; 0.72124 0.11262 -0.09720619 46.20193442 3.68591 0.13624 CHMP6 0.765888301098665 0.232293700338992 0.00181799856234275 charged multivesicular body protein 6 FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. In the ESCRT-III complex, it probably serves as an acceptor for the ESCRT-II complex on endosomal membranes.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15511219}.; medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.27320 0.12971 -0.471992905 23.03609342 450.98462 4.41291 CHMP7 0.980739996928141 0.0192570438312147 2.95924064431206e-06 charged multivesicular body protein 7 FUNCTION: Plays a role in the endosomal sorting pathway. {ECO:0000269|PubMed:16856878}.; . . myocardium;ovary;salivary gland;colon;substantia nigra;parathyroid;skin;uterus;prostate;whole body;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;cerebellum; superior cervical ganglion;skeletal muscle; 0.12168 0.10664 -0.361761279 28.6329323 57.06537 1.52107 CHN1 0.837424430279943 0.162440171876105 0.000135397843951826 chimerin 1 FUNCTION: GTPase-activating protein for p21-rac and a phorbol ester receptor. Involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance.; DISEASE: Duane retraction syndrome 2 (DURS2) [MIM:604356]: Duane retraction syndrome is a congenital eye movement disorder characterized by a failure of cranial nerve VI (the abducens nerve) to develop normally, resulting in restriction or absence of abduction, adduction, or both, and narrowing of the palpebral fissure and retraction of the globe on attempted adduction. Undiagnosed in children, it can lead to amblyopia, a permanent uncorrectable loss of vision. {ECO:0000269|PubMed:18653847}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In neurons in brain regions that are involved in learning and memory processes.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;endometrium;thyroid;bone;pituitary gland;testis;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;lens;skeletal muscle;bile duct;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;hippocampus;liver;spleen;kidney;stomach; amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.29582 0.15284 -0.538132194 20.26421326 18.57043 0.64364 CHN2 0.0255023240305153 0.971833209863898 0.00266446610558681 chimerin 2 FUNCTION: GTPase-activating protein for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low-grade to high-grade tumors.; . TISSUE SPECIFICITY: Highest levels in the brain and pancreas. Also expressed in the heart, placenta, and weakly in the kidney and liver. Expression is much reduced in the malignant gliomas, compared to normal brain or low-grade astrocytomas.; unclassifiable (Anatomical System);heart;blood;skin;bone marrow;uterus;pancreas;whole body;frontal lobe;endometrium;liver;testis;spleen;brain;stomach; dorsal root ganglion;medulla oblongata;occipital lobe;superior cervical ganglion;cerebellum peduncles;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.26539 . -0.380166007 27.88393489 1077.81846 6.29228 CHODL 0.00128507754633277 0.855979708969132 0.142735213484535 chondrolectin . . TISSUE SPECIFICITY: Found in spleen, testis, prostate and fetal liver. Expression limited to vascular muscle of testis, smooth muscle of prostate stroma, heart muscle, skeletal muscle, crypts of small intestine, and red pulp of spleen. {ECO:0000269|PubMed:11707072, ECO:0000269|PubMed:12079284}.; unclassifiable (Anatomical System);heart;ovary;cartilage;hypothalamus;parathyroid;skeletal muscle;skin;bone marrow;uterus;lung;placenta;testis;brain; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.16038 0.10721 -0.249709319 35.74545883 160.47364 2.76384 CHODL-AS1 . . . CHODL antisense RNA 1 . . . . . . . . . . . CHORDC1 0.531116383359684 0.468189446531558 0.000694170108758348 cysteine and histidine rich domain containing 1 FUNCTION: Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis. {ECO:0000269|PubMed:20230755}.; . TISSUE SPECIFICITY: Underexpressed in many breast and lung cancers. {ECO:0000269|PubMed:20230755}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;iris;testis;dura mater;germinal center;brain;pineal gland;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;liver;cervix;kidney;stomach; . 0.64332 0.10733 0.080983847 59.76055674 12.30329 0.44604 CHORDC2P . . . cysteine and histidine rich domain containing 2, pseudogene . . . . . . . . . . . CHP1 0.228123191828265 0.764172823175553 0.0077039849961819 calcineurin like EF-hand protein 1 FUNCTION: Calcium-binding protein involved in different processes such as regulation of vesicular trafficking, plasma membrane Na(+)/H(+) exchanger and gene transcription. Involved in the constitutive exocytic membrane traffic. Mediates the association between microtubules and membrane-bound organelles of the endoplasmic reticulum and Golgi apparatus and is also required for the targeting and fusion of transcytotic vesicles (TCV) with the plasma membrane. Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Affects the pH sensitivity of SLC9A1/NHE1 by increasing its sensitivity at acidic pH. Required for the stabilization and localization of SLC9A1/NHE1 at the plasma membrane. Inhibits serum- and GTPase-stimulated Na(+)/H(+) exchange. Plays a role as an inhibitor of ribosomal RNA transcription by repressing the nucleolar UBF1 transcriptional activity. May sequester UBF1 in the nucleoplasm and limit its translocation to the nucleolus. Associates to the ribosomal gene promoter. Acts as a negative regulator of the calcineurin/NFAT signaling pathway. Inhibits NFAT nuclear translocation and transcriptional activity by suppressing the calcium-dependent calcineurin phosphatase activity. Also negatively regulates the kinase activity of the apoptosis-induced kinase STK17B. Inhibits both STK17B auto- and substrate- phosphorylations in a calcium-dependent manner. {ECO:0000269|PubMed:10593895, ECO:0000269|PubMed:11350981, ECO:0000269|PubMed:15035633, ECO:0000269|PubMed:8901634}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Has been found in fetal eye, lung, liver, muscle, heart, kidney, thymus and spleen. {ECO:0000269|PubMed:8901634}.; . . . . -0.053113545 49.38664779 1.90232 0.05947 CHP2 0.00659125634654492 0.914232692369616 0.0791760512838388 calcineurin like EF-hand protein 2 FUNCTION: Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Binds to and activates SLC9A1/NHE1 in a serum-independent manner, thus increasing pH and protecting cells from serum deprivation- induced death. Also plays a role in the regulation of cell proliferation and tumor growth by increasing the phosphatase activity of PPP3CA in a calcium-dependent manner. Activator of the calcineurin/NFAT signaling pathway. Involved in the cytoplasmic translocation of the transcription factor NFATC3 to the nucleus. {ECO:0000269|PubMed:12226101, ECO:0000269|PubMed:18815128}.; . TISSUE SPECIFICITY: Expressed in malignantly transformed cells but not detected in normal tissues. {ECO:0000269|PubMed:12097419, ECO:0000269|PubMed:12226101}.; . . . . 0.393270925 76.04977589 293.20091 3.66064 CHPF 0.231251265748001 0.767205244193763 0.00154349005823552 chondroitin polymerizing factor FUNCTION: Has both beta-1,3-glucuronic acid and beta-1,4-N- acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Isoform 2 may facilitate PARK2 transport into the mitochondria. In collaboration with PARK2, isoform 2 may enhance cell viability and protect cells from oxidative stress. {ECO:0000269|PubMed:12761225}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in pancreas, ovary, brain, heart, skeletal muscle, colon, kidney, liver, stomach, spleen and placenta. Isoform 3 is also ubiquitous. Isoform 2 is expressed in brain, spleen, ovary, testis, lung and peripheral mononuclear cells. {ECO:0000269|PubMed:12716890, ECO:0000269|PubMed:12761225, ECO:0000269|PubMed:22082830}.; lymphoreticular;medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;pineal body;muscle;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;amnion;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;placenta;globus pallidus;testis;pons;trigeminal ganglion; 0.13997 0.19598 -0.861560326 10.89289927 243.88919 3.37034 CHPF2 7.24132491401232e-17 0.00760309530804331 0.992396904691957 chondroitin polymerizing factor 2 FUNCTION: Transfers glucuronic acid (GlcUA) from UDP-GlcUA to N- acetylgalactosamine residues on the non-reducing end of the elongating chondroitin polymer. Has no N- acetylgalactosaminyltransferase activity. {ECO:0000269|PubMed:12145278, ECO:0000269|PubMed:18316376}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in placenta, small intestine and pancreas. {ECO:0000269|PubMed:12145278}.; ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;synovium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;stomach;peripheral nerve; . . . 0.167138932 64.99174334 296.01683 3.67355 CHPT1 0.0035704767848813 0.953616118685123 0.0428134045299961 choline phosphotransferase 1 FUNCTION: Catalyzes phosphatidylcholine biosynthesis from CDP- choline. It thereby plays a central role in the formation and maintenance of vesicular membranes.; . TISSUE SPECIFICITY: Highly expressed in testis, colon, small intestine, heart, prostate and spleen. Also detected in kidney, skeletal muscle, pancreas, leukocytes, ovary and thymus. Weakly expressed in the brain, placenta and lung. Overexpressed in cancerous breast epithelial cell lines. {ECO:0000269|PubMed:10893425, ECO:0000269|PubMed:12359261}.; medulla oblongata;ovary;umbilical cord;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;testis;spinal ganglion;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;blood;lens;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;hippocampus;liver;cervix;kidney;stomach; testis;atrioventricular node; 0.08237 0.09015 -0.0274281 51.65723048 2974.05814 10.34366 CHR . . . chromate resistance; sulfate transport . . . . . . . . . . . CHRAC1 0.658094860543726 0.317915158756653 0.0239899806996207 chromatin accessibility complex 1 FUNCTION: Forms a complex with DNA polymerase epsilon subunit POLE3 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodeling activity of ISWI/SNF2H and ACF1.; . TISSUE SPECIFICITY: Expressed in all tissues tested, including, heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; unclassifiable (Anatomical System);smooth muscle;lacrimal gland;colon;skin;skeletal muscle;bone marrow;lung;nasopharynx;placenta;thyroid;visual apparatus;hippocampus;liver;testis;head and neck;spleen;cervix;brain;stomach; . 0.15287 0.11432 0.569646743 81.88841708 126.68763 2.45376 CHRD 0.00038124723708207 0.999602195969548 1.65567933703692e-05 chordin FUNCTION: Dorsalizing factor. Key developmental protein that dorsalizes early vertebrate embryonic tissues by binding to ventralizing TGF-beta family bone morphogenetic proteins (BMPs) and sequestering them in latent complexes (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at the highest level in liver.; heart;ovary;islets of Langerhans;muscle;colon;skeletal muscle;uterus;prostate;whole body;lung;frontal lobe;endometrium;hippocampus;liver;testis;kidney;mammary gland;spinal ganglion;brain;stomach;cerebellum; dorsal root ganglion;cerebellum peduncles;globus pallidus;atrioventricular node;skeletal muscle;cerebellum; 0.26131 0.35825 -0.683363435 15.36329323 2239.997 8.73521 CHRDL1 0.0536284936083553 0.942171786439636 0.00419971995200876 chordin-like 1 FUNCTION: Antagonizes the function of BMP4 by binding to it and preventing its interaction with receptors. Alters the fate commitment of neural stem cells from gliogenesis to neurogenesis. Contributes to neuronal differentiation of neural stem cells in the brain by preventing the adoption of a glial fate. May play a crucial role in dorsoventral axis formation. May play a role in embryonic bone formation (By similarity). May also play an important role in regulating retinal angiogenesis through modulation of BMP4 actions in endothelial cells. Plays a role during anterior segment eye development. {ECO:0000250, ECO:0000269|PubMed:18587495, ECO:0000269|PubMed:22284829}.; DISEASE: Megalocornea 1, X-linked (MGC1) [MIM:309300]: An eye disorder in which the corneal diameter is bilaterally enlarged (greater than 13 mm) without an increase in intraocular pressure. It may also be referred to as anterior megalophthalmos, since the entire anterior segment is larger than normal. Features of megalocornea in addition to a deep anterior chamber include astigmatic refractive errors, atrophy of the iris stroma, miosis secondary to decreased function of the dilator muscle, iridodonesis, and tremulousness, subluxation, or dislocation of the lens. Whereas most affected individuals exhibit normal ocular function, complications include cataract development and glaucoma following lenticular dislocation or subluxation. {ECO:0000269|PubMed:22284829}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the developing cornea and in the eye anterior segment in addition to the retina. Differentially expressed in the fetal brain. There is high expression in cerebellum and neocortex. Expressed in retinal pericytes. {ECO:0000269|PubMed:18587495, ECO:0000269|PubMed:22284829}.; unclassifiable (Anatomical System);heart;ovary;sympathetic chain;urinary;parathyroid;skin;retina;uterus;placenta;thyroid;testis;mammary gland;brain; dorsal root ganglion;uterus;superior cervical ganglion;uterus corpus;olfactory bulb;adipose tissue;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.40707 0.37988 -0.005381972 53.50908233 155.92032 2.72874 CHRDL2 2.13642145685107e-05 0.902382837782377 0.0975957980030546 chordin-like 2 FUNCTION: May inhibit BMPs activity by blocking their interaction with their receptors. Has a negative regulator effect on the cartilage formation/regeneration from immature mesenchymal cells, by preventing or reducing the rate of matrix accumulation (By similarity). Implicated in tumor angiogenesis. May play a role during myoblast and osteoblast differentiation, and maturation. {ECO:0000250, ECO:0000269|PubMed:12853144, ECO:0000269|PubMed:15094188}.; . TISSUE SPECIFICITY: Highly expressed in uterus. Moderately expressed in heart, liver, prostate, testis and ovary. Weakly expressed in skeletal muscle, kidney, spleen, small intestine and colon. Expressed in the secretory epithelial cells of uterine endometrium, fallopian tubes, endocervical glands, bladder and prostate, as well as the transitional epithelium of the urinary bladder, and in bone osteoblasts (at protein level). In normal cartilage, expression was confined in a few chondrocytes in the superficial zone as well as in the middle zone. In diseased cartilage coming from osteoarthritic patients, expression was limited to the middle zone of chondrocytes. Isoform 1 and isoform 2 are expressed in fetal cerebellum and heart, while only isoform 2 is detected in fetal spleen. Isoform 2 present in plasma. {ECO:0000269|PubMed:12853144, ECO:0000269|PubMed:14660436, ECO:0000269|PubMed:15094188}.; prostate;testis;colon;skeletal muscle; uterus;superior cervical ganglion;uterus corpus;atrioventricular node; 0.31594 0.12800 0.378498378 75.58386412 186.00922 2.96260 CHRFAM7A . . . CHRNA7 (exons 5-10) and FAM7A (exons A-E) fusion . . TISSUE SPECIFICITY: Expressed in hippocampus. {ECO:0000269|PubMed:9782083}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;sympathetic chain;colon;parathyroid;skin;bile duct;uterus;whole body;lung;bone;thyroid;placenta;visual apparatus;liver;testis;spleen;brain; . 0.09772 . . . 3293.32624 10.95425 CHRFAM7AP1 . . . CHRFAM7A pseudogene 1 . . . . . . . . . . . CHRFAM7AP2 . . . CHRFAM7A pseudogene 2 . . . . . . . . . . . CHRM1 0.931378496611047 0.0682777546513088 0.00034374873764395 cholinergic receptor muscarinic 1 FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.; . . unclassifiable (Anatomical System);prostate;optic nerve;macula lutea;iris;fovea centralis;choroid;lens;brain;retina; . 0.25764 0.53109 -0.692458599 14.96815287 12.14409 0.43940 CHRM2 0.00587059361264825 0.728438524981138 0.265690881406214 cholinergic receptor muscarinic 2 FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipase C activity, leading to the release of inositol trisphosphate (IP3); this then triggers calcium ion release into the cytosol. {ECO:0000269|PubMed:24256733, ECO:0000269|PubMed:3443095}.; DISEASE: Major depressive disorder (MDD) [MIM:608516]: A common psychiatric disorder. It is a complex trait characterized by one or more major depressive episodes without a history of manic, mixed, or hypomanic episodes. A major depressive episode is characterized by at least 2 weeks during which there is a new onset or clear worsening of either depressed mood or loss of interest or pleasure in nearly all activities. Four additional symptoms must also be present including changes in appetite, weight, sleep, and psychomotor activity; decreased energy; feelings of worthlessness or guilt; difficulty thinking, concentrating, or making decisions; or recurrent thoughts of death or suicidal ideation, plans, or attempts. The episode must be accompanied by distress or impairment in social, occupational, or other important areas of functioning. {ECO:0000269|PubMed:15229186}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;liver;testis;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.31194 . 0.194852702 67.03231894 63.5868 1.63378 CHRM3 0.937026128208817 0.0629173690388682 5.65027523143088e-05 cholinergic receptor muscarinic 3 FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover. {ECO:0000269|PubMed:7565628}.; DISEASE: Prune belly syndrome (PBS) [MIM:100100]: A syndrome characterized by thin abdominal musculature with overlying lax skin, cryptorchism, megacystis with disorganized detrusor muscle, and urinary tract abnormalities. {ECO:0000269|PubMed:22077972}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);thyroid;colon;head and neck;brain;retina;bone marrow; whole brain;amygdala;subthalamic nucleus;occipital lobe;medulla oblongata;superior cervical ganglion;temporal lobe;prefrontal cortex;globus pallidus;pons;parietal lobe; 0.20539 0.10448 -0.135838822 43.77211607 97.64234 2.13666 CHRM3-AS1 . . . CHRM3 antisense RNA 1 . . . . . . . . . . . CHRM3-AS2 . . . CHRM3 antisense RNA 2 . . . . . . . . . . . CHRM4 0.916843942226412 0.0825970014210816 0.000559056352506492 cholinergic receptor muscarinic 4 FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is inhibition of adenylate cyclase.; . . . . . . -0.957024976 9.088228356 13.36595 0.48659 CHRM5 0.00383197171202466 0.957137486464693 0.0390305418232827 cholinergic receptor muscarinic 5 FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.; . . . . 0.28572 0.08287 0.376678994 75.50719509 267.67625 3.50908 CHRNA1 8.79556820389947e-06 0.765909011550562 0.234082192881234 cholinergic receptor nicotinic alpha 1 subunit FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.; DISEASE: Note=The alpha subunit is the main focus for antibody binding in myasthenia gravis. Myasthenia gravis is characterized by sporadic muscular fatigability and weakness, occurring chiefly in muscles innervated by cranial nerves, and characteristically improved by cholinesterase-inhibiting drugs.; DISEASE: Myasthenic syndrome, congenital, 1A, slow-channel (CMS1A) [MIM:601462]: A common congenital myasthenic syndrome. Congenital myasthenic syndromes are characterized by muscle weakness affecting the axial and limb muscles (with hypotonia in early- onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS1A is a slow-channel myasthenic syndrome. It is caused by kinetic abnormalities of the AChR, resulting in prolonged AChR channel opening episodes, prolonged endplate currents, and depolarization block. This is associated with calcium overload, which may contribute to subsequent degeneration of the endplate and postsynaptic membrane. {ECO:0000269|PubMed:16685696, ECO:0000269|PubMed:7619526, ECO:0000269|PubMed:8872460, ECO:0000269|PubMed:9158151, ECO:0000269|PubMed:9221765}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myasthenic syndrome, congenital, 1B, fast-channel (CMS1B) [MIM:608930]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS1B is a fast-channel myasthenic syndrome. It is caused by kinetic abnormalities of the AChR, resulting in brief opening and activity of the channel, with a rapid decay in endplate current, failure to achieve threshold depolarization of the endplate and consequent failure to fire an action potential. {ECO:0000269|PubMed:10195214, ECO:0000269|PubMed:12588888, ECO:0000269|PubMed:15079006}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is only expressed in skeletal muscle. Isoform 2 is constitutively expressed in skeletal muscle, brain, heart, kidney, liver, lung and thymus.; unclassifiable (Anatomical System);ovary;heart;tongue;larynx;bone;placenta;visual apparatus;muscle;liver;parathyroid;head and neck;skin; dorsal root ganglion;uterus corpus;superior cervical ganglion;appendix;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.10721 0.38059 -0.334253673 30.70299599 241.66802 3.35589 CHRNA2 0.00176647920423662 0.89694092868652 0.101292592109243 cholinergic receptor nicotinic alpha 2 subunit FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.; DISEASE: Epilepsy, nocturnal frontal lobe, 4 (ENFL4) [MIM:610353]: An autosomal dominant focal epilepsy characterized by nocturnal seizures associated with fear sensation, tongue movements, and nocturnal wandering, closely resembling nightmares and sleep walking. {ECO:0000269|PubMed:16826524}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . peripheral nerve; superior cervical ganglion;trigeminal ganglion; 0.04594 0.17832 -0.753139731 13.67067705 44.83603 1.28342 CHRNA3 0.00706163755884019 0.920097699448344 0.0728406629928161 cholinergic receptor nicotinic alpha 3 subunit FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.; . . ovary;sympathetic chain;colon;choroid;fovea centralis;retina;prostate;optic nerve;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cerebellum cortex;adrenal cortex;lens;lung;visual apparatus;macula lutea;duodenum;head and neck;stomach;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;thymus; 0.28677 0.25204 -1.109541557 6.782259967 115.42015 2.33620 CHRNA4 0.0208678880743461 0.961999536728699 0.0171325751969545 cholinergic receptor nicotinic alpha 4 subunit FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane permeable to sodium ions. {ECO:0000269|PubMed:22361591}.; DISEASE: Epilepsy, nocturnal frontal lobe, 1 (ENFL1) [MIM:600513]: An autosomal dominant focal epilepsy characterized by nocturnal seizures with hyperkinetic automatisms and poorly organized stereotyped movements. {ECO:0000269|PubMed:10563623, ECO:0000269|PubMed:14623738, ECO:0000269|PubMed:7550350}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.12554 0.10854 -1.969545983 1.786978061 54.0249 1.46563 CHRNA5 2.40946932670794e-06 0.291867461661812 0.708130128868862 cholinergic receptor nicotinic alpha 5 subunit FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.; . . unclassifiable (Anatomical System);lung;ovary;larynx;bone;thyroid;sympathetic chain;pituitary gland;testis;head and neck;brain;stomach; dorsal root ganglion;superior cervical ganglion;temporal lobe;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07467 0.09224 -0.222203495 37.54423213 1316.23977 6.82264 CHRNA6 2.0439355054386e-06 0.457535564916005 0.542462391148489 cholinergic receptor nicotinic alpha 6 subunit FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.; . . unclassifiable (Anatomical System);optic nerve;lymph node;macula lutea;fovea centralis;choroid;lens;brain;skin;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.05657 0.14812 -0.777005578 12.9747582 115.95545 2.34191 CHRNA7 . . . cholinergic receptor nicotinic alpha 7 subunit FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is blocked by alpha-bungarotoxin.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;sympathetic chain;colon;parathyroid;skin;bile duct;uterus;whole body;lung;bone;thyroid;placenta;visual apparatus;liver;testis;spleen;brain; . 0.45152 0.34457 . . 45.84242 1.30166 CHRNA9 0.000411143835005301 0.852648693472363 0.146940162692631 cholinergic receptor nicotinic alpha 9 subunit FUNCTION: Ionotropic receptor with a probable role in the modulation of auditory stimuli. Agonist binding induces a conformation change that leads to the opening of an ion-conducting channel across the plasma membrane (PubMed:11752216, PubMed:25282151). The channel is permeable to a range of divalent cations including calcium, the influx of which may activate a potassium current which hyperpolarizes the cell membrane (PubMed:11752216, PubMed:25282151). In the ear, this may lead to a reduction in basilar membrane motion, altering the activity of auditory nerve fibers and reducing the range of dynamic hearing. This may protect against acoustic trauma. May also regulate keratinocyte adhesion (PubMed:11021840). {ECO:0000269|PubMed:11021840, ECO:0000269|PubMed:11752216, ECO:0000269|PubMed:25282151, ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in cochlea, keratinocytes, pituitary gland, B-cells and T-cells. {ECO:0000269|PubMed:11021840, ECO:0000269|PubMed:11752216, ECO:0000269|PubMed:15531379}.; kidney; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.14960 0.16692 0.42259095 77.22929936 1967.83361 8.17546 CHRNA10 1.04066746022543e-05 0.565672143856965 0.434317449468433 cholinergic receptor nicotinic alpha 10 subunit FUNCTION: Ionotropic receptor with a probable role in the modulation of auditory stimuli. Agonist binding may induce an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is permeable to a range of divalent cations including calcium, the influx of which may activate a potassium current which hyperpolarizes the cell membrane. In the ear, this may lead to a reduction in basilar membrane motion, altering the activity of auditory nerve fibers and reducing the range of dynamic hearing. This may protect against acoustic trauma. {ECO:0000269|PubMed:11752216}.; . TISSUE SPECIFICITY: Expressed in inner-ear tissue, tonsil, immortalized B-cells, cultured T-cells and peripheral blood lymphocytes. {ECO:0000269|PubMed:11752216, ECO:0000269|PubMed:15531379}.; unclassifiable (Anatomical System);cartilage;ovary;heart;liver;spleen;germinal center;brain;retina;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.03490 0.15559 0.843299698 88.37579618 464.51004 4.46537 CHRNB1 4.33630397665382e-06 0.837461082260562 0.162534581435461 cholinergic receptor nicotinic beta 1 subunit FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.; DISEASE: Myasthenic syndrome, congenital, 2A, slow-channel (CMS2A) [MIM:616313]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS2A is a slow-channel myasthenic syndrome. It is caused by kinetic abnormalities of the AChR, resulting in prolonged AChR channel opening episodes, prolonged endplate currents, and depolarization block. This is associated with calcium overload, which may contribute to subsequent degeneration of the endplate and postsynaptic membrane. {ECO:0000269|PubMed:8651643, ECO:0000269|PubMed:8872460}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myasthenic syndrome, congenital, 2C, associated with acetylcholine receptor deficiency (CMS2C) [MIM:616314]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS2C is an autosomal recessive disorder of postsynaptic neuromuscular transmission, due to deficiency of AChR at the endplate that results in low amplitude of the miniature endplate potential and current. CMS2C is clinically characterized by early-onset muscle weakness with variable severity. {ECO:0000269|PubMed:10562302}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;islets of Langerhans;parathyroid;blood;skin;retina;uterus;breast;pancreas;prostate;frontal lobe;nasopharynx;placenta;liver;germinal center;kidney;brain; superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.33567 0.14592 -0.402212257 26.7338995 1354.17252 6.90787 CHRNB2 0.720254345017317 0.279117238474064 0.000628416508618252 cholinergic receptor nicotinic beta 2 subunit FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane permeable to sodiun ions. {ECO:0000269|PubMed:22361591}.; DISEASE: Epilepsy, nocturnal frontal lobe, 3 (ENFL3) [MIM:605375]: An autosomal dominant focal epilepsy characterized by nocturnal seizures with hyperkinetic automatisms and poorly organized stereotyped movements. {ECO:0000269|PubMed:11062464, ECO:0000269|PubMed:11104662}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.21029 0.27753 -0.692458599 14.96815287 25.07801 0.82078 CHRNB3 0.000131863319539552 0.849191403596873 0.150676733083588 cholinergic receptor nicotinic beta 3 subunit FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.; . . unclassifiable (Anatomical System);visual apparatus; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.17518 -0.336073593 30.55555556 227.99732 3.26123 CHRNB4 0.0186266094522454 0.961243497443596 0.0201298931041583 cholinergic receptor nicotinic beta 4 subunit FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.; . . unclassifiable (Anatomical System);brain; superior cervical ganglion;trigeminal ganglion; 0.14292 0.13789 0.734883636 86.29983487 550.72501 4.77210 CHRND 7.26421538921512e-07 0.897544916734249 0.102454356844212 cholinergic receptor nicotinic delta subunit FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.; DISEASE: Multiple pterygium syndrome, lethal type (LMPS) [MIM:253290]: Multiple pterygia are found infrequently in children with arthrogryposis and in fetuses with fetal akinesia syndrome. In lethal multiple pterygium syndrome there is intrauterine growth retardation, multiple pterygia, and flexion contractures causing severe arthrogryposis and fetal akinesia. Subcutaneous edema can be severe, causing fetal hydrops with cystic hygroma and lung hypoplasia. Oligohydramnios and facial anomalies are frequent. {ECO:0000269|PubMed:18252226}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myasthenic syndrome, congenital, 3A, slow-channel (CMS3A) [MIM:616321]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS3A is a slow-channel myasthenic syndrome. It is caused by kinetic abnormalities of the AChR, resulting in prolonged AChR channel opening episodes, prolonged endplate currents, and depolarization block. This is associated with calcium overload, which may contribute to subsequent degeneration of the endplate and postsynaptic membrane. {ECO:0000269|PubMed:11782989, ECO:0000269|PubMed:8872460}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myasthenic syndrome, congenital, 3B, fast-channel (CMS3B) [MIM:616322]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS3B is a fast-channel myasthenic syndrome. It is caused by kinetic abnormalities of the AChR, resulting in brief opening and activity of the channel, with a rapid decay in endplate current, failure to achieve threshold depolarization of the endplate and consequent failure to fire an action potential. {ECO:0000269|PubMed:11435464, ECO:0000269|PubMed:12499478, ECO:0000269|PubMed:18398509}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myasthenic syndrome, congenital, 3C, associated with acetylcholine receptor deficiency (CMS3C) [MIM:616323]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS3C is an autosomal recessive disorder of postsynaptic neuromuscular transmission, due to deficiency of AChR at the endplate that results in low amplitude of the miniature endplate potential and current. {ECO:0000269|PubMed:16916845, ECO:0000269|PubMed:18398509}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System); superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.16756 0.17222 -0.398573136 26.92852088 107.43573 2.25073 CHRNE 0.00034790045891714 0.988685522581574 0.0109665769595091 cholinergic receptor nicotinic epsilon subunit FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.; DISEASE: Note=The muscle AChR is the major target antigen in the autoimmune disease myasthenia gravis. Myasthenia gravis is characterized by sporadic muscular fatigability and weakness, occurring chiefly in muscles innervated by cranial nerves, and characteristically improved by cholinesterase-inhibiting drugs.; DISEASE: Myasthenic syndrome, congenital, 4A, slow-channel (CMS4A) [MIM:605809]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS4A is a slow-channel myasthenic syndrome. It is caused by kinetic abnormalities of the AChR, resulting in prolonged AChR channel opening episodes, prolonged endplate currents, and depolarization block. This is associated with calcium overload, which may contribute to subsequent degeneration of the endplate and postsynaptic membrane. {ECO:0000269|PubMed:12141316, ECO:0000269|PubMed:7531341, ECO:0000269|PubMed:7538206, ECO:0000269|PubMed:8872460}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myasthenic syndrome, congenital, 4B, fast-channel (CMS4B) [MIM:616324]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS4B is a fast-channel myasthenic syndrome. It is caused by kinetic abnormalities of the AChR, resulting in brief opening and activity of the channel, with a rapid decay in endplate current, failure to achieve threshold depolarization of the endplate and consequent failure to fire an action potential. {ECO:0000269|PubMed:10962020, ECO:0000269|PubMed:22592360, ECO:0000269|PubMed:8755487}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myasthenic syndrome, congenital, 4C, associated with acetylcholine receptor deficiency (CMS4C) [MIM:608931]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS4C is an autosomal recessive disorder of postsynaptic neuromuscular transmission, due to deficiency of AChR at the endplate that results in low amplitude of the miniature endplate potential and current. {ECO:0000269|PubMed:9158150}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;fovea centralis;choroid;vein;skin;retina;uterus;optic nerve;endometrium;larynx;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;thymus; atrioventricular node; 0.51041 0.10048 -0.909290275 10.03184713 146.24216 2.63486 CHRNG 1.12925757682932e-09 0.517073586559867 0.482926412310876 cholinergic receptor nicotinic gamma subunit FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.; DISEASE: Multiple pterygium syndrome, lethal type (LMPS) [MIM:253290]: Multiple pterygia are found infrequently in children with arthrogryposis and in fetuses with fetal akinesia syndrome. In lethal multiple pterygium syndrome there is intrauterine growth retardation, multiple pterygia, and flexion contractures causing severe arthrogryposis and fetal akinesia. Subcutaneous edema can be severe, causing fetal hydrops with cystic hygroma and lung hypoplasia. Oligohydramnios and facial anomalies are frequent. {ECO:0000269|PubMed:16826520, ECO:0000269|PubMed:16826531}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multiple pterygium syndrome, Escobar variant (EVMPS) [MIM:265000]: Non-lethal form of arthrogryposis multiplex congenita. It is an autosomal recessive condition characterized by excessive webbing (pterygia), congenital contractures (arthrogryposis), and scoliosis. Variable other features include intrauterine death, congenital respiratory distress, short stature, faciocranial dysmorphism, ptosis, low-set ears, arachnodactyly and cryptorchism in males. Congenital contractures are common and may be caused by reduced fetal movements at sensitive times of development. Possible causes of decreased fetal mobility include space constraints such as oligohydramnion, drugs, metabolic conditions or neuromuscular disorders including myasthenia gravis. {ECO:0000269|PubMed:16826520, ECO:0000269|PubMed:16826531}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.06654 0.08497 -0.418800956 25.79028073 505.40763 4.61314 CHST1 0.820990319101784 0.178147648296028 0.00086203260218772 carbohydrate sulfotransferase 1 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of galactose (Gal) residues of keratan. Has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal Gal residues are sulfated. May function in the sulfation of sialyl N- acetyllactosamine oligosaccharide chains attached to glycoproteins. Participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. {ECO:0000269|PubMed:10330415, ECO:0000269|PubMed:10642612}.; . TISSUE SPECIFICITY: Widely expressed at low level. Expressed in brain and skeletal muscle. Expressed by high endothelial cells (HEVs) and leukocytes. {ECO:0000269|PubMed:11310842, ECO:0000269|PubMed:9405439}.; myocardium;salivary gland;sympathetic chain;colon;retina;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;hypothalamus;cerebrum;skeletal muscle;lung;hippocampus;visual apparatus;head and neck;kidney;mammary gland; amygdala;whole brain;superior cervical ganglion;thalamus;medulla oblongata;occipital lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.26991 0.14896 -0.249709319 35.74545883 39.69525 1.17003 CHST2 0.123805841170553 0.852041516130145 0.0241526426993022 carbohydrate (N-acetylglucosamine-6-O) sulfotransferase 2 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues within keratan-like structures on N-linked glycans and within mucin-associated glycans that can ultimately serve as SELL ligands. SELL ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Participates in biosynthesis of the SELL ligand sialyl 6-sulfo Lewis X and in lymphocyte homing to Peyer patches. Has no activity toward O-linked sugars. Its substrate specificity may be influenced by its subcellular location. Sulfates GlcNAc residues at terminal, non-reducing ends of oligosaccharide chains. {ECO:0000269|PubMed:11042394}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in bone marrow, peripheral blood leukocytes, spleen, brain, spinal cord, ovary and placenta. Expressed by high endothelial cells (HEVs) and leukocytes. {ECO:0000269|PubMed:10049591, ECO:0000269|PubMed:11310842, ECO:0000269|PubMed:9722682}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;oesophagus;endometrium;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;islets of Langerhans;hypothalamus;lens;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;kidney;stomach; pons; 0.15266 0.14391 0.018483465 55.44939844 157.07921 2.73832 CHST3 0.165928594453581 0.77235608529548 0.0617153202509391 carbohydrate (chondroitin 6) sulfotransferase 3 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues of keratan sulfate, another glycosaminoglycan, and the Gal residues in sialyl N- acetyllactosamine (sialyl LacNAc) oligosaccharides. May play a role in the maintenance of naive T-lymphocytes in the spleen. {ECO:0000269|PubMed:9714738, ECO:0000269|PubMed:9883891}.; . TISSUE SPECIFICITY: Widely expressed in adult tissues. Expressed in heart, placenta, skeletal muscle and pancreas. Also expressed in various immune tissues such as spleen, lymph node, thymus and appendix. {ECO:0000269|PubMed:9714738}.; . . 0.23975 0.13861 -0.337894035 30.37272942 1915.97152 8.05603 CHST4 5.59232486282113e-09 0.0655279373114056 0.934472057096269 carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 4 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues within mucin-associated glycans that ultimately serve as SELL ligands. SELL ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Participates in biosynthesis of the SELL ligand sialyl 6-sulfo Lewis X on receptors SPN/CD43, GLYCAM1 and MADCAM1. Also involved in biosynthesis of SELL ligand recognized by MECA-79 antibody. Plays a central role in lymphocyte trafficking during chronic inflammation. Has a catalytic preference for core 2- branched mucin-type O-glycans. Can use GlcNAcbeta1-6[Galbeta1- 3]GalNAc-pNP (core 2), GlcNAcbeta1-6ManOMe and GlcNAcbeta1-2Man oligosaccharide structures as acceptors. Has also activity toward core 3 of GlcNAcbeta1-3GalNAc-pNP. Its substrate specificity may be influenced by its subcellular location. {ECO:0000269|PubMed:10330415}.; . TISSUE SPECIFICITY: Specifically expressed in HEV. Weakly expressed in spleen. Not expressed in other tissues. Expressed in colonic mucinous adenocarcinoma. {ECO:0000269|PubMed:10330415, ECO:0000269|PubMed:11310842, ECO:0000269|PubMed:12107080}.; unclassifiable (Anatomical System);lung;endometrium;islets of Langerhans;colon; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;medulla oblongata;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.32786 0.13367 -0.023789244 52.09365416 79.52391 1.88445 CHST5 0.00538022490291957 0.894212584623397 0.100407190473683 carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 5 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues and O-linked sugars of mucin-type acceptors. Acts on the non-reducing terminal GlcNAc of short carbohydrate substrates. However, it does not transfer sulfate to longer carbohydrate substrates that have poly-N-acetyllactosamine structures. Has no activity toward keratan. Not involved in generating HEV-expressed ligands for SELL. Its substrate specificity may be influenced by its subcellular location. {ECO:0000269|PubMed:10491328, ECO:0000269|PubMed:11352640, ECO:0000269|PubMed:12218059, ECO:0000269|PubMed:12626414}.; . TISSUE SPECIFICITY: Predominantly expressed in small and large intestines and colon. Weakly expressed in lymphocytes. Not expressed in other tissues. Down-regulated in colonic adenocarcinomas. {ECO:0000269|PubMed:10491328, ECO:0000269|PubMed:11017086, ECO:0000269|PubMed:11352640, ECO:0000269|PubMed:12107080, ECO:0000269|PubMed:12626414}.; unclassifiable (Anatomical System);lung;testis;colon;kidney;brain; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.07608 0.11764 0.220536484 68.38287332 850.00192 5.69761 CHST6 0.000606606828678051 0.722173160726717 0.277220232444604 carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 6 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues of keratan. Mediates sulfation of keratan in cornea. Keratan sulfate plays a central role in maintaining corneal transparency. Acts on the non-reducing terminal GlcNAc of short and long carbohydrate substrates that have poly-N- acetyllactosamine structures. {ECO:0000269|PubMed:11352640, ECO:0000269|PubMed:12218059}.; . TISSUE SPECIFICITY: Expressed in cornea. Mainly expressed in brain. Also expressed in spinal cord and trachea. {ECO:0000269|PubMed:11017086, ECO:0000269|PubMed:11181564, ECO:0000269|PubMed:11352640}.; unclassifiable (Anatomical System);prostate;optic nerve;lung;cartilage;lacrimal gland;larynx;macula lutea;head and neck;fovea centralis;choroid;lens;retina; . 0.13663 0.13913 -0.642904474 16.62538335 125.71515 2.44127 CHST7 0.0985193527095849 0.77141248845392 0.130068158836495 carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 7 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues. Preferentially acts on mannose-linked GlcNAc. Also able to catalyze the transfer of sulfate to position 6 of the N- acetylgalactosamine (GalNAc) residue of chondroitin. Also acts on core 2 mucin-type oligosaccharide and N-acetyllactosamine oligomer with a lower efficiency. Has weak or no activity toward keratan sulfate and oligosaccharides containing the Galbeta1-4GlcNAc. Catalyzes 6-O-sulfation of beta-benzyl GlcNAc but not alpha- or beta-benzyl GalNAc. {ECO:0000269|PubMed:10781596, ECO:0000269|PubMed:10913333, ECO:0000269|PubMed:10956661}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart, spleen, liver and ovary. Expressed at lower level in brain, placenta, thyroid, spinal cord and peripheral blood leukocytes. Not expressed in adult skin. {ECO:0000269|PubMed:10781596, ECO:0000269|PubMed:10913333, ECO:0000269|PubMed:10956661}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bladder;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;liver;kidney;aorta;thymus; superior cervical ganglion;ovary;whole blood; 0.53214 0.14237 . . 30.85586 0.97782 CHST8 0.00422201568083706 0.864722705336931 0.131055278982232 carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 8 FUNCTION: Catalyzes the transfer of sulfate to position 4 of non- reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Required for biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Only active against terminal GalNAcbeta1,GalNAcbeta. Not active toward chondroitin. {ECO:0000269|PubMed:10988300, ECO:0000269|PubMed:11445554}.; DISEASE: Peeling skin syndrome 3 (PSS3) [MIM:616265]: A form of peeling skin syndrome, a genodermatosis characterized by generalized, continuous shedding of the outer layers of the epidermis. Two main PSS subtypes have been suggested. Patients with non-inflammatory PSS (type A) manifest white scaling, with painless and easy removal of the skin, irritation when in contact with water, dust and sand, and no history of erythema, pruritis or atopy. Inflammatory PSS (type B) is associated with generalized erythema, pruritus and atopy. It is an ichthyosiform erythroderma characterized by lifelong patchy peeling of the entire skin with onset at birth or shortly after. Several patients have been reported with high IgE levels. PSS3 is characterized by generalized white scaling occurring over the upper and lower extremities. Symptoms start during the second half of the first decade of life. {ECO:0000269|PubMed:22289416}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in pituitary gland. In brain, it is expressed in pituitary gland, cerebellum, medulla oblongata, pons, thalamus and spinal cord. Expressed in the epidermis. Expressed at lower level in lung, spleen, adrenal gland, placenta, prostate, testis, mammary gland and trachea. {ECO:0000269|PubMed:10988300, ECO:0000269|PubMed:11001942, ECO:0000269|PubMed:11445554, ECO:0000269|PubMed:22289416}.; unclassifiable (Anatomical System);lymph node;islets of Langerhans;pituitary gland;brain; thalamus;pons;trigeminal ganglion;cingulate cortex; 0.88558 0.10958 -0.315847836 31.68789809 39.28138 1.16248 CHST9 5.84291419980849e-07 0.430067290152249 0.569932125556331 carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 9 FUNCTION: Catalyzes the transfer of sulfate to position 4 of non- reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Participates in biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Has a higher activity toward carbonic anhydrase VI than toward lutropin. Only active against terminal GalNAcbeta1,GalNAcbeta. Isoform 2, but not isoform 1, is active toward chondroitin.; . TISSUE SPECIFICITY: Highly expressed in trachea. Also expressed in fetal lung, adult pancreas, testis and salivary gland. Expressed at low level in pituitary gland, apex of the heart, adult lung, prostate and mammary gland. Weakly or not expressed in heart, liver and spinal cord. {ECO:0000269|PubMed:11139592, ECO:0000269|PubMed:11445554}.; unclassifiable (Anatomical System);myocardium;prostate;lung;islets of Langerhans;liver;testis;spleen;kidney;brain; dorsal root ganglion;uterus corpus;trachea;appendix;ciliary ganglion;atrioventricular node; 0.29878 0.08972 -0.049474214 50.01179523 91.77625 2.06105 CHST10 0.00330306267127204 0.949341321285593 0.047355616043135 carbohydrate sulfotransferase 10 FUNCTION: Catalyzes the transfer of sulfate to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult. May be indirectly involved in synapse plasticity of the hippocampus, via its role in HNK-1 biosynthesis. {ECO:0000269|PubMed:9478973}.; . TISSUE SPECIFICITY: In fetal tissues, it is predominantly expressed in brain, and weakly expressed in lung, kidney and liver. In adult, it is highly expressed in brain, testis, ovary, expressed at intermediate level in heart, pancreas, skeletal muscle, spleen and thymus, and weakly expressed in other tissues. In brain, it is expressed at higher level in the frontal lobe. {ECO:0000269|PubMed:9478973}.; myocardium;ovary;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;pancreas;lung;placenta;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;liver;ciliary ganglion;pons;cingulate cortex; 0.10661 0.11918 0.531004228 80.87992451 2126.55729 8.49001 CHST11 0.398388040805651 0.592415121820045 0.00919683737430422 carbohydrate sulfotransferase 11 FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues in desulfated dermatan sulfate. Preferentially sulfates in GlcA->GalNAc unit than in IdoA->GalNAc unit. Does not form 4, 6- di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor.; DISEASE: Note=A chromosomal aberration involving CHST11 is found in B-cell chronic lymphocytic leukemias. Translocation t(12;14)(q23;q32) with IgH. {ECO:0000269|PubMed:15273723}.; TISSUE SPECIFICITY: Widely expressed. Highly expressed in spleen, thymus, bone marrow, peripheral blood leukocytes, lymph node, heart, brain, lung and placenta. {ECO:0000269|PubMed:10781601, ECO:0000269|PubMed:11056388}.; unclassifiable (Anatomical System);cartilage;ovary;colon;blood;uterus;prostate;lung;bone;thyroid;placenta;iris;amnion;alveolus;liver;testis;head and neck;spleen;germinal center;mammary gland;aorta; superior cervical ganglion; 0.30803 0.14896 -0.381986487 27.68931352 567.30676 4.83587 CHST12 0.000240662916934188 0.523118598695303 0.476640738387763 carbohydrate sulfotransferase 12 FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin and desulfated dermatan sulfate. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Activity toward partially desulfated dermatan sulfate is however lower. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor.; . TISSUE SPECIFICITY: Widely expressed. Expressed a high level in spinal chord, heart, spleen, thyroid, pituitary gland, adrenal gland, peripheral blood leukocytes, thymus, lung, small intestine, fetal kidney, fetal spleen and fetal lung. {ECO:0000269|PubMed:10781601}.; medulla oblongata;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;pharynx;blood;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; white blood cells; 0.16437 0.11561 0.266447942 70.5826846 684.24994 5.22317 CHST13 0.000159791662950939 0.25599887624136 0.743841332095689 carbohydrate (chondroitin 4) sulfotransferase 13 FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Transfers sulfate to the C4 hydroxyl of beta1,4-linked GalNAc that is substituted with a beta-linked glucuronic acid at the C-3 hydroxyl. No activity toward dermatan.; . TISSUE SPECIFICITY: Highly expressed in adult liver. Expressed at lower level in kidney, lymph nodes and fetal kidney. {ECO:0000269|PubMed:12080076}.; unclassifiable (Anatomical System);lung;placenta;liver;testis;colon;spleen;kidney; . 0.09406 0.11277 . . 3261.22783 10.88564 CHST14 0.594619350621838 0.395804616993215 0.00957603238494644 carbohydrate sulfotransferase 14 FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of dermatan sulfate. Plays a pivotal role in the formation of 4-0-sulfated IdoA blocks in dermatan sulfate. Transfers sulfate to the C-4 hydroxyl of beta1,4-linked GalNAc that is substituted with an alpha-linked iduronic acid (IdoUA) at the C-3 hydroxyl. Transfers sulfate more efficiently to GalNAc residues in -IdoUA-GalNAc-IdoUA- than in -GlcUA-GalNAc-GlcUA-sequences. Has preference for partially desulfated dermatan sulfate. Addition of sulfate to GalNAc may occur immediately after epimerization of GlcUA to IdoUA. GlcUA to IdoUA. Appears to have an important role in the formation of the cerbellar neural network during postnatal brain development. {ECO:0000269|PubMed:19661164}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at high level in pituitary gland, placenta, uterus and thyroid. {ECO:0000269|PubMed:11470797}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;adrenal cortex;lens;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;spleen;stomach; dorsal root ganglion;pons;trigeminal ganglion;skeletal muscle; 0.31260 0.10716 -0.139478553 43.29440906 37.40524 1.11399 CHST15 0.177822119661987 0.819534679993972 0.00264320034404048 carbohydrate (N-acetylgalactosamine 4-sulfate 6-O) sulfotransferase 15 FUNCTION: Sulfotransferase that transfers sulfate from 3'- phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4)) repeating units. It also transfers sulfate to a unique non- reducing terminal sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. May also act as a B- cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B-cell development and/or regulation of B-cell-specific RAG expression; however such results are unclear in vivo. {ECO:0000269|PubMed:11572857, ECO:0000269|PubMed:12874280}.; . TISSUE SPECIFICITY: Expressed in B-cell-enriched tissues but not in fetal or adult thymus. Expressed in fetal and adult spleen, lymph node, tonsil, bone marrow and peripheral leukocytes. Not expressed in T-cells. In pro-B, pre-B, and mature B-cell lines, it colocalizes with RAG1. {ECO:0000269|PubMed:9754571}.; lymphoreticular;smooth muscle;ovary;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;hypopharynx;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; whole blood; . . -0.086288664 47.11606511 147.96514 2.64996 CHSY1 0.913667234012375 0.0863071633687752 2.56026188501537e-05 chondroitin sulfate synthase 1 FUNCTION: Has both beta-1,3-glucuronic acid and beta-1,4-N- acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Involved in the negative control of osteogenesis likely through the modulation of NOTCH signaling. {ECO:0000269|PubMed:11514575, ECO:0000269|PubMed:21129727}.; . TISSUE SPECIFICITY: Ubiquitous, with the highest levels in placenta. Detected at low levels in brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, adrenal gland, mammary gland, stomach, small intestine, lung and peripheral blood leukocytes. {ECO:0000269|PubMed:11514575, ECO:0000269|PubMed:12907687}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;larynx;bone;thyroid;testis;germinal center;brain;artery;bladder;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;alveolus;liver;head and neck;spleen;kidney;aorta;stomach; dorsal root ganglion;superior cervical ganglion;placenta;adrenal cortex;trigeminal ganglion;skeletal muscle; 0.37712 0.11323 -0.771553417 13.15168672 1764.58025 7.76113 CHSY3 0.011861287143968 0.986460513889474 0.00167819896655842 chondroitin sulfate synthase 3 FUNCTION: Has both beta-1,3-glucuronic acid and beta-1,4-N- acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Specific activity is much reduced compared to CHSY1. {ECO:0000269|PubMed:12907687}.; . TISSUE SPECIFICITY: Detected at low levels in brain, cerebral cortex, uterus and small intestine. {ECO:0000269|PubMed:12907687}.; unclassifiable (Anatomical System);uterus;lung;heart;iris;testis;brain;skin;stomach; . 0.27016 0.11034 -0.731092527 14.13658882 397.48513 4.18935 CHTF8 0.275816998725164 0.633463683173034 0.0907193181018023 chromosome transmission fidelity factor 8 FUNCTION: Potential tumor suppressor. Inhibits prostate tumor cell growth, when overexpressed. {ECO:0000269|PubMed:12477976}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with abundant expression in kidney, skeletal muscle, testis, liver, ovary, and heart and moderate expression in prostate. Expression is significantly reduced in renal and prostate tumors. No differential expression in breast cancer cells, between lobular carcinoma and normal lobules. {ECO:0000269|PubMed:12477976, ECO:0000269|PubMed:18213475}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;urinary;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; . . . -0.119252484 44.53880632 282.20918 3.59714 CHTF8P1 . . . chromosome transmission fidelity factor 8 pseudogene 1 . . . . . . . . . . . CHTF18 . . . chromosome transmission fidelity factor 18 FUNCTION: Chromosome cohesion factor involved in sister chromatid cohesion and fidelity of chromosome transmission. Component of one of the cell nuclear antigen loader complexes, CTF18-replication factor C (CTF18-RFC), which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. The CTF18-RFC complex binds to single- stranded and primed DNAs and has weak ATPase activity that is stimulated by the presence of primed DNA, replication protein A (RPA) and by proliferating cell nuclear antigen (PCNA). The CTF18- RFC complex catalyzes the ATP-dependent loading of PCNA onto primed and gapped DNA. It also interacts with and stimulates DNA polymerase POLH. {ECO:0000269|PubMed:12766176, ECO:0000269|PubMed:12930902, ECO:0000269|PubMed:17545166}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;urinary;blood;fovea centralis;choroid;lens;retina;bone marrow;uterus;pancreas;optic nerve;frontal lobe;endometrium;bone;thyroid;placenta;macula lutea;liver;testis;brain;mammary gland;stomach; . 0.94697 0.25548 1.076560794 91.73154046 3313.24164 10.99873 CHTOP 0.998109469154056 0.00189048086734574 4.99785981500103e-08 chromatin target of PRMT1 FUNCTION: Plays an important role in the ligand-dependent activation of estrogen receptor target genes (PubMed:19858291). May play a role in the silencing of fetal globin genes (PubMed:20688955). Recruits the 5FMC complex to ZNF148, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (By similarity). Plays an important role in the tumorigenicity of glioblastoma cells. Binds to 5- hydroxymethylcytosine (5hmC) and associates with the methylosome complex containing PRMT1, PRMT5, MEP50 and ERH. The CHTOP- methylosome complex associated with 5hmC is recruited to selective sites on the chromosome, where it methylates H4R3 and activates the transcription of genes involved in glioblastomagenesis (PubMed:25284789). {ECO:0000250|UniProtKB:Q9CY57, ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:20688955, ECO:0000269|PubMed:25284789}.; . TISSUE SPECIFICITY: Expressed in an erythroid progenitor cell line derived from peripheral blood. Expressed in glioblastoma cells (PubMed:25284789). {ECO:0000269|PubMed:20688955, ECO:0000269|PubMed:25284789}.; . . 0.32021 0.10725 -0.183570861 39.95046001 77.44923 1.84998 CHUK 0.998703705142778 0.00129629469220426 1.65017930241066e-10 conserved helix-loop-helix ubiquitous kinase FUNCTION: Serine kinase that plays an essential role in the NF- kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Negatively regulates the pathway by phosphorylating the scaffold protein TAXBP1 and thus promoting the assembly of the A20/TNFAIP3 ubiquitin-editing complex (composed of A20/TNFAIP3, TAX1BP1, and the E3 ligases ITCH and RNF11). Therefore, CHUK plays a key role in the negative feedback of NF-kappa-B canonical signaling to limit inflammatory gene activation. As part of the non-canonical pathway of NF-kappa-B activation, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa- B RelB-p52 complexes. In turn, these complexes regulate genes encoding molecules involved in B-cell survival and lymphoid organogenesis. Participates also in the negative feedback of the non-canonical NF-kappa-B signaling pathway by phosphorylating and destabilizing MAP3K14/NIK. Within the nucleus, phosphorylates CREBBP and consequently increases both its transcriptional and histone acetyltransferase activities. Modulates chromatin accessibility at NF-kappa-B-responsive promoters by phosphorylating histones H3 at 'Ser-10' that are subsequently acetylated at 'Lys-14' by CREBBP. Additionally, phosphorylates the CREBBP-interacting protein NCOA3. Also phosphorylates FOXO3 and may regulate this pro-apoptotic transcription factor (PubMed:15084260). {ECO:0000269|PubMed:12789342, ECO:0000269|PubMed:15084260, ECO:0000269|PubMed:17434128, ECO:0000269|PubMed:20434986, ECO:0000269|PubMed:20501937, ECO:0000269|PubMed:21765415}.; DISEASE: Cocoon syndrome (COCOS) [MIM:613630]: A lethal syndrome characterized by multiple fetal malformations including defective face and seemingly absent limbs, which are bound to the trunk and encased under the skin. {ECO:0000269|PubMed:20961246}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed.; . . 0.84106 0.63405 -0.201976964 38.98325077 135.45191 2.53221 CHURC1 3.13272051464755e-05 0.345236356795496 0.654732315999358 churchill domain containing 1 FUNCTION: Transcriptional activator that mediates FGF signaling during neural development. Plays a role in the regulation of cell movement (By similarity). Does not bind DNA by itself. {ECO:0000250}.; . . myocardium;ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;macula lutea;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;spinal cord;testis;ciliary ganglion;atrioventricular node;skeletal muscle;cerebellum; 0.17982 0.12378 0.503505267 79.88912479 35.65553 1.07258 CHURC1-FNTB . . . CHURC1-FNTB readthrough FUNCTION: Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C- terminus of several proteins having the C-terminal sequence Cys- aliphatic-aliphatic-X. {ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937, ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:8494894}.; . . . . 0.22283 . -0.159704656 41.90846898 . . CIAO1 0.0147161304906565 0.957328386596572 0.0279554829127713 cytosolic iron-sulfur assembly component 1 FUNCTION: Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. Seems to specifically modulate the transactivation activity of WT1. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation. {ECO:0000255|HAMAP-Rule:MF_03037, ECO:0000269|PubMed:17937914, ECO:0000269|PubMed:20797633}.; . . ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;nervous;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;muscle;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus; . 0.25054 0.14731 -0.26993514 34.59542345 37.15981 1.10969 CIAPIN1 0.296605891863902 0.699138863346945 0.00425524478915301 cytokine induced apoptosis inhibitor 1 FUNCTION: Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells (By similarity). Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis. Electrons are transferred to the Fe-S cluster from NADPH via the FAD- and FMN-containing protein NDOR1. {ECO:0000250, ECO:0000269|PubMed:23596212}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in heart, liver and pancreas. {ECO:0000269|PubMed:14970183}.; . . 0.12971 0.11434 0.150760231 64.51403633 300.58485 3.69586 CIAPIN1P . . . cytokine induced apoptosis inhibitor 1 pseudogene . . . . . . . . . . . CIART . . . circadian associated repressor of transcription FUNCTION: Transcriptional repressor which forms a negative regulatory component of the circadian clock and acts independently of the circadian transcriptional repressors: CRY1, CRY2 and BHLHE41. In a histone deacetylase-dependent manner represses the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Abrogates the interaction of ARNTL/BMAL1 with the transcriptional coactivator CREBBP and can repress the histone acetyl-transferase activity of the CLOCK-ARNTL/BMAL1 heterodimer, reducing histone acetylation of its target genes. Rhythmically binds the E-box elements (5'-CACGTG-3') on circadian gene promoters and its occupancy shows circadian oscillation antiphasic to ARNTL/BMAL1. Interacts with the glucocorticoid receptor (NR3C1) and contributes to the repressive function in the glucocorticoid response (By similarity). {ECO:0000250}.; . . . . . . -0.249709319 35.74545883 . . CIB1 0.0161029646482789 0.883934356211315 0.0999626791404064 calcium and integrin binding 1 FUNCTION: Calcium-binding protein that plays a role in the regulation of numerous cellular processes, such as cell differentiation, cell division, cell proliferation, cell migration, thrombosis, angiogenesis, cardiac hypertrophy and apoptosis. Involved in bone marrow megakaryocyte differentiation by negatively regulating thrombopoietin-mediated signaling pathway. Participates in the endomitotic cell cycle of megakaryocyte, a form of mitosis in which both karyokinesis and cytokinesis are interrupted. Plays a role in integrin signaling by negatively regulating alpha-IIb/beta3 activation in thrombin- stimulated megakaryocytes preventing platelet aggregation. Up- regulates PTK2/FAK1 activity, and is also needed for the recruitment of PTK2/FAK1 to focal adhesions; it thus appears to play an important role in focal adhesion formation. Positively regulates cell migration on fibronectin in a CDC42-dependent manner, the effect being negatively regulated by PAK1. Functions as a negative regulator of stress activated MAP kinase (MAPK) signaling pathways. Down-regulates inositol 1,4,5-trisphosphate receptor-dependent calcium signaling. Involved in sphingosine kinase SPHK1 translocation to the plasma membrane in a N- myristoylation-dependent manner preventing TNF-alpha-induced apoptosis. Regulates serine/threonine-protein kinase PLK3 activity for proper completion of cell division progression. Plays a role in microtubule (MT) dynamics during neuronal development; disrupts the MT depolymerization activity of STMN2 attenuating NGF-induced neurite outgrowth and the MT reorganization at the edge of lamellipodia. Promotes cardiomyocyte hypertrophy via activation of the calcineurin/NFAT signaling pathway. Stimulates calcineurin PPP3R1 activity by mediating its anchoring to the sarcolemma. In ischemia-induced (pathological or adaptive) angiogenesis, stimulates endothelial cell proliferation, migration and microvessel formation by activating the PAK1 and ERK1/ERK2 signaling pathway. Promotes also cancer cell survival and proliferation. May regulate cell cycle and differentiation of spermatogenic germ cells, and/or differentiation of supporting Sertoli cells.; . TISSUE SPECIFICITY: Detected in platelets and in cell lines of megakaryocytic and erythrocytic lineages. Both isoform 1 and isoform 2 are detected in various cancer cell lines, with isoform 2 being the predominant form (at protein level). Ubiquitously expressed. {ECO:0000269|PubMed:10477286, ECO:0000269|PubMed:11856312, ECO:0000269|PubMed:23503467, ECO:0000269|PubMed:9030514, ECO:0000269|PubMed:9372844}.; myocardium;smooth muscle;ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;blood;lens;skeletal muscle;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta; testis - interstitial;prostate;heart;testis - seminiferous tubule;liver;adrenal cortex;testis;skeletal muscle; 0.16210 0.27055 -0.295622497 32.61972163 38.05583 1.13067 CIB2 0.000468492983005407 0.667683032899504 0.331848474117491 calcium and integrin binding family member 2 FUNCTION: Calcium-binding protein critical for proper photoreceptor cell maintenance and function. Plays a role in intracellular calcium homeostasis by decreasing ATP-induced calcium release (PubMed:23023331, PubMed:26173970). May be involved in the mechanotransduction process (By similarity). {ECO:0000250, ECO:0000269|PubMed:23023331, ECO:0000269|PubMed:26173970}.; DISEASE: Usher syndrome 1J (USH1J) [MIM:614869]: USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa with sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). USH1 is characterized by profound congenital sensorineural deafness, absent vestibular function and prepubertal onset of progressive retinitis pigmentosa leading to blindness. {ECO:0000269|PubMed:23023331}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed (PubMed:23023331). {ECO:0000269|PubMed:23023331}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;iris;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;pharynx;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion; 0.40943 0.13588 -0.293801652 32.93819297 57.97419 1.53939 CIB3 4.43323180861714e-07 0.117762629322968 0.882236927353851 calcium and integrin binding family member 3 . . . unclassifiable (Anatomical System); medulla oblongata;atrioventricular node;skeletal muscle; 0.16030 0.10939 -0.161524709 41.6430762 25.81487 0.83986 CIB4 2.30345990608051e-06 0.285306408549183 0.714691287990911 calcium and integrin binding family member 4 . . . unclassifiable (Anatomical System);placenta;testis;kidney; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07874 . 0.128714042 63.19886766 33.28019 1.02790 CIC 0.99990294666404 9.70533344847396e-05 1.47467149607037e-12 capicua transcriptional repressor FUNCTION: Transcriptional repressor which may play a role in development of the central nervous system (CNS).; . TISSUE SPECIFICITY: Expressed in fetal brain. {ECO:0000269|PubMed:15981098}.; lymphoreticular;myocardium;smooth muscle;ovary;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;muscle;adrenal cortex;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;skeletal muscle; 0.23629 0.17563 -3.381635251 0.383345129 222.23333 3.22421 CICP1 . . . capicua transcriptional repressor pseudogene 1 . . . . . . . . . . . CICP2 . . . capicua transcriptional repressor pseudogene 2 . . . . . . . . . . . CICP3 . . . capicua transcriptional repressor pseudogene 3 . . . . . . . . . . . CICP4 . . . capicua transcriptional repressor pseudogene 4 . . . . . . . . . . . CICP5 . . . capicua transcriptional repressor pseudogene 5 . . . . . . . . . . . CICP6 . . . capicua transcriptional repressor pseudogene 6 . . . . . . . . . . . CICP7 . . . capicua transcriptional repressor pseudogene 7 . . . . . . . . . . . CICP8 . . . capicua transcriptional repressor pseudogene 8 . . . . . . . . . . . CICP9 . . . capicua transcriptional repressor pseudogene 9 . . . . . . . . . . . CICP10 . . . capicua transcriptional repressor pseudogene 10 . . . . . . . . . . . CICP11 . . . capicua transcriptional repressor pseudogene 11 . . . . . . . . . . . CICP12 . . . capicua transcriptional repressor pseudogene 12 . . . . . . . . . . . CICP13 . . . capicua transcriptional repressor pseudogene 13 . . . . . . . . . . . CICP14 . . . capicua transcriptional repressor pseudogene 14 . . . . . . . . . . . CICP15 . . . capicua transcriptional repressor pseudogene 15 . . . . . . . . . . . CICP16 . . . capicua transcriptional repressor pseudogene 16 . . . . . . . . . . . CICP17 . . . capicua transcriptional repressor pseudogene 17 . . . . . . . . . . . CICP18 . . . capicua transcriptional repressor pseudogene 18 . . . . . . . . . . . CICP19 . . . capicua transcriptional repressor pseudogene 19 . . . . . . . . . . . CICP20 . . . capicua transcriptional repressor pseudogene 20 . . . . . . . . . . . CICP21 . . . capicua transcriptional repressor pseudogene 21 . . . . . . . . . . . CICP22 . . . capicua transcriptional repressor pseudogene 22 . . . . . . . . . . . CICP23 . . . capicua transcriptional repressor pseudogene 23 . . . . . . . . . . . CICP24 . . . capicua transcriptional repressor pseudogene 24 . . . . . . . . . . . CICP25 . . . capicua transcriptional repressor pseudogene 25 . . . . . . . . . . . CICP26 . . . capicua transcriptional repressor pseudogene 26 . . . . . . . . . . . CICP27 . . . capicua transcriptional repressor pseudogene 27 . . . . . . . . . . . CICP28 . . . capicua transcriptional repressor pseudogene 28 . . . . . . . . . . . CIDEA 0.0146284389438315 0.873805652282564 0.111565908773604 cell death-inducing DFFA-like effector a FUNCTION: Acts as a CEBPB coactivator in mammary epithelial cells to control the expression of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH, but not casein. By interacting with CEBPB, strengthens the association of CEBPB with the XDH promoter, increases histone acetylation and dissociates HDAC1 from the promoter (By similarity). Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair and occurs at a lower rate than that promoted by CIDEC. When overexpressed, induces apoptosis. The physiological significance of its role in apoptosis is unclear. {ECO:0000250, ECO:0000269|PubMed:19843876}.; . TISSUE SPECIFICITY: Expressed in omental and subcutaneous adipose tissue (at protein level). {ECO:0000269|PubMed:18509062}.; unclassifiable (Anatomical System);lung;heart;testis;mammary gland;skin; . 0.15442 0.18847 0.595326758 82.66100495 171.63036 2.85715 CIDEB 1.51797420711163e-11 0.00765839665174819 0.992341603333072 cell death-inducing DFFA-like effector b FUNCTION: Activates apoptosis.; . TISSUE SPECIFICITY: Highly expressed in liver and small intestine and, at lower levels, in colon, kidney and spleen. {ECO:0000269|PubMed:12429024}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;hippocampus;liver;duodenum;alveolus;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;fetal liver;liver;kidney; 0.15793 0.08429 -0.780646273 12.77423921 45.396 1.29448 CIDEC 0.00141663238797231 0.66590165347219 0.332681714139838 cell death inducing DFFA like effector c FUNCTION: Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair. Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1. May act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment. As mature adipocytes, that express high CIDEC levels, are quite resistant to apoptotic stimuli, the physiological significance of its role in apoptosis is unclear. May play a role in the modulation of the response to osmotic stress by preventing NFAT5 to translocate into the nucleus and activate its target genes expression. {ECO:0000269|PubMed:12429024, ECO:0000269|PubMed:18334488, ECO:0000269|PubMed:19843876, ECO:0000269|PubMed:20049731, ECO:0000269|PubMed:23399566}.; DISEASE: Note=In omental adipose tissue of obese patients matched for BMI, expression levels tend to correlate with insulin sensitivity. Expression is increased 2-3 fold in the group of patients with high insulin sensitivity, compared to the insulin- resistant group. This observation is consistent with the idea that triglyceride storage in adipocytes plays an important role in sequestering triglycerides and fatty acids away from the circulation and peripheral tissues, thus enhancing insulin sensitivity in liver and muscle. This effect is not significant in subcutaneous adipose tissue (PubMed:18509062). In subcutaneous adipose tissue of diabetic patients, tends to negatively correlate with body mass index and total fat mass, independently of insulin sensitivity (PubMed:18334488). {ECO:0000269|PubMed:18334488, ECO:0000269|PubMed:18509062}.; DISEASE: Lipodystrophy, familial partial, 5 (FPLD5) [MIM:615238]: A form of lipodystrophy characterized by loss of subcutaneous adipose tissue affecting limb, femorogluteal and subcutaneous abdominal fat, preservation of visceral, neck and axilliary fat, hepatomegaly, hepatic steatosis and insulin-resistant diabetes. {ECO:0000269|PubMed:20049731}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed mainly in adipose tissue, small intestine, heart, colon and stomach and, at lower levels, in brain, kidney and liver. {ECO:0000269|PubMed:12429024, ECO:0000269|PubMed:18334488}.; unclassifiable (Anatomical System);prostate;cerebral cortex;bone;colon;brain;mammary gland;skin;skeletal muscle;bone marrow; superior cervical ganglion;adipose tissue;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.20849 . 0.262810045 70.43524416 157.22556 2.74041 CIDECP . . . cell death-inducing DFFA-like effector c pseudogene . . . liver;colon;blood;germinal center;brain;mammary gland;skeletal muscle;retina;bone marrow; . . . . . . . CIITA 5.54341952880924e-05 0.99989113669237 5.34291123419534e-05 class II, major histocompatibility complex, transactivator FUNCTION: Essential for transcriptional activity of the HLA class II promoter; activation is via the proximal promoter. No DNA binding of in vitro translated CIITA was detected. May act in a coactivator-like fashion through protein-protein interactions by contacting factors binding to the proximal MHC class II promoter, to elements of the transcription machinery, or both. Alternatively it may activate HLA class II transcription by modifying proteins that bind to the MHC class II promoter. Also mediates enhanced MHC class I transcription; the promoter element requirements for CIITA-mediated transcription are distinct from those of constitutive MHC class I transcription, and CIITA can functionally replace TAF1 at these genes. Exhibits intrinsic GTP-stimulated acetyltransferase activity. Exhibits serine/threonine protein kinase activity: can phosphorylate the TFIID component TAF7, the RAP74 subunit of the general transcription factor TFIIF, histone H2B at 'Ser-37' and other histones (in vitro). {ECO:0000269|PubMed:11172716, ECO:0000269|PubMed:16600381, ECO:0000269|PubMed:17493635, ECO:0000269|PubMed:24036077}.; DISEASE: Bare lymphocyte syndrome 2 (BLS2) [MIM:209920]: A severe combined immunodeficiency disease with early onset. It is characterized by a profound defect in constitutive and interferon- gamma induced MHC II expression, absence of cellular and humoral T-cell response to antigen challenge, hypogammaglobulinemia and impaired antibody production. The consequence include extreme susceptibility to viral, bacterial and fungal infections. {ECO:0000269|PubMed:10501838, ECO:0000269|PubMed:11466404, ECO:0000269|PubMed:11862382, ECO:0000269|PubMed:7749984, ECO:0000269|PubMed:8402893}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;ovary;salivary gland;intestine;pharynx;colon;blood;skin;bone marrow;breast;uterus;prostate;pancreas;lung;thyroid;visual apparatus;liver;testis;kidney;germinal center;brain;mammary gland;bladder;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.18899 0.51457 -0.891174372 10.18518519 402.15375 4.20745 CILP 1.39584747557031e-19 0.00136885179311487 0.998631148206885 cartilage intermediate layer protein FUNCTION: Probably plays a role in cartilage scaffolding. May act by antagonizing TGF-beta1 (TGFB1) and IGF1 functions. Has the ability to suppress IGF1-induced proliferation and sulfated proteoglycan synthesis, and inhibits ligand-induced IGF1R autophosphorylation. May inhibit TGFB1-mediated induction of cartilage matrix genes via its interaction with TGFB1. Overexpression may lead to impair chondrocyte growth and matrix repair and indirectly promote inorganic pyrophosphate (PPi) supersaturation in aging and osteoarthritis cartilage. {ECO:0000269|PubMed:12746903, ECO:0000269|PubMed:15864306}.; DISEASE: Intervertebral disc disease (IDD) [MIM:603932]: A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain. {ECO:0000269|PubMed:15864306}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. {ECO:0000269|PubMed:15864306}.; TISSUE SPECIFICITY: Specifically expressed in cartilage. Localizes in the intermediates layer of articular cartilage but neither in the superficial nor in the deepest regions. Specifically and highly expressed in intervertebral disk tissue. Expression increases with aging in hip articular cartilage. Overexpressed in articular hyaline cartilage from patients with calcium pyrophosphate dihydrate crystal deposition disease (CPPD). Expression in intervertebral disk tissue from individuals with lumbar disk disease increases as disk degeneration progresses. {ECO:0000269|PubMed:12483726, ECO:0000269|PubMed:15864306, ECO:0000269|PubMed:9722583, ECO:0000269|PubMed:9722584}.; unclassifiable (Anatomical System);heart;ovary;cartilage;skeletal muscle;skin;uterus;pancreas;prostate;lung;liver;testis;spinal ganglion;mammary gland; dorsal root ganglion;testis - interstitial;superior cervical ganglion;adipose tissue;tongue;appendix;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.25090 0.13916 -1.534306349 3.343949045 4110.02331 12.73040 CILP2 0.000278936233123941 0.999088514485695 0.000632549281181463 cartilage intermediate layer protein 2 FUNCTION: May play a role in cartilage scaffolding. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in articular chondrocytes but not in knee meniscal cartilage cells. {ECO:0000269|PubMed:12746903}.; unclassifiable (Anatomical System);cartilage;hypopharynx;testis;head and neck;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.16316 0.11129 -1.082044518 7.242274121 113.50816 2.31988 CINP 0.00276924897730325 0.799101101084107 0.19812964993859 cyclin-dependent kinase 2 interacting protein FUNCTION: Interacts with the components of the replication complex and 2 kinases, CDK2 and CDC7, thereby providing a functional and physical link between CDK2 and CDC7 during firing of the origins of replication. Regulates ATR-mediated checkpoint signaling. {ECO:0000269|PubMed:16082200, ECO:0000269|PubMed:19889979}.; . . medulla oblongata;ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;mesenchyma;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; . . . 0.461228372 78.46190139 1713.33084 7.63051 CIPC . . . CLOCK-interacting pacemaker FUNCTION: Transcriptional repressor which acts as a negative- feedback regulator of CLOCK-ARNTL/BMAL1 transcriptional activity in the circadian-clock mechanism. Stimulates ARNTL/BMAL1-dependent phosphorylation of CLOCK (By similarity). {ECO:0000250}.; . . . . 0.22245 . -0.404032746 26.53338051 328.2509 3.85097 CIR1 0.0121190516591458 0.986254588943139 0.00162635939771571 corepressor interacting with RBPJ, 1 FUNCTION: May modulate splice site selection during alternative splicing of pre-mRNAs (By similarity). Regulates transcription and acts as corepressor for RBPJ. Recruits RBPJ to the Sin3-histone deacetylase complex (HDAC). Required for RBPJ-mediated repression of transcription. {ECO:0000250, ECO:0000269|PubMed:19409814, ECO:0000269|PubMed:9874765}.; . TISSUE SPECIFICITY: Highly expressed in heart, brain, placenta, liver, skeletal muscle and pancreas. {ECO:0000269|PubMed:9874765}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;epidermis;islets of Langerhans;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; testis; . . -0.117432389 44.89266336 95.21349 2.10554 CIR1P1 . . . corepressor interacting with RBPJ, 1 pseudogene 1 . . . . . . . . . . . CIR1P2 . . . corepressor interacting with RBPJ, 1 pseudogene 2 . . . . . . . . . . . CIR1P3 . . . corepressor interacting with RBPJ, 1 pseudogene 3 . . . . . . . . . . . CIRBP 0.622585655314118 0.375815535637149 0.00159880904873303 cold inducible RNA binding protein FUNCTION: Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Acts as a translational activator. Seems to play an essential role in cold- induced suppression of cell proliferation. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN. Acts as a translational repressor (By similarity). Promotes assembly of stress granules (SGs), when overexpressed. {ECO:0000250, ECO:0000269|PubMed:11574538, ECO:0000269|PubMed:16513844}.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;prostate;frontal lobe;cerebral cortex;endometrium;synovium;thyroid;iris;pituitary gland;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;mesenchyma;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;subthalamic nucleus;occipital lobe;cerebellum peduncles;hypothalamus;thyroid;globus pallidus;testis;pituitary;parietal lobe;cerebellum; 0.13777 0.11983 -0.163345027 41.24793583 25.59069 0.83448 CIRBP-AS1 . . . CIRBP antisense RNA 1 . . . . . . . . . . . CISD1 0.464700956103008 0.510001666232885 0.0252973776641074 CDGSH iron sulfur domain 1 FUNCTION: Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation (By similarity). May be involved in Fe-S cluster shuttling and/or in redox reactions. {ECO:0000250, ECO:0000269|PubMed:17584744, ECO:0000269|PubMed:17766440}.; . TISSUE SPECIFICITY: Expression is reduced in cells derived from cystic fibrosis patients. {ECO:0000269|PubMed:18047834}.; . . 0.56195 . 0.057118534 57.99716914 4.45764 0.16197 CISD1P1 . . . CDGSH iron sulfur domain 1 pseudogene 1 . . . . . . . . . . . CISD2 0.649111068534367 0.325059703271898 0.0258292281937359 CDGSH iron sulfur domain 2 FUNCTION: Regulator of autophagy that contributes to antagonize BECN1-mediated cellular autophagy at the endoplasmic reticulum. Participates in the interaction of BCL2 with BECN1 and is required for BCL2-mediated depression of endoplasmic reticulum Ca(2+) stores during autophagy. Contributes to BIK-initiated autophagy, while it is not involved in BIK-dependent activation of caspases. Involved in life span control, probably via its function as regulator of autophagy. {ECO:0000269|PubMed:17846994, ECO:0000269|PubMed:20010695}.; . TISSUE SPECIFICITY: Testis, small intestine, kidney, lung, brain, heart, pancreas and platelets. {ECO:0000269|PubMed:17846994}.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach;aorta;cerebellum; fetal liver;atrioventricular node; 0.18630 0.10986 -0.053113545 49.38664779 98.65522 2.14830 CISD3 . . . CDGSH iron sulfur domain 3 . . . . . . . 0.389637587 75.75489502 1591.44868 7.37806 CISH 0.00144425763962849 0.670045636033782 0.328510106326589 cytokine inducible SH2-containing protein FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. CIS is involved in the negative regulation of cytokines that signal through the JAK-STAT5 pathway such as erythropoietin, prolactin and interleukin 3 (IL3) receptor. Inhibits STAT5 trans-activation by suppressing its tyrosine phosphorylation. May be a substrate- recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in various epithelial tissues. Abundantly expressed in liver and kidney, and to a lesser extent in lung. The tissue distribution of isoforms 1 and 1B is distinct. {ECO:0000269|PubMed:11032736}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;colon;parathyroid;blood;skin;bone marrow;breast;uterus;prostate;lung;frontal lobe;endometrium;larynx;nasopharynx;bone;placenta;testis;head and neck;kidney;brain;mammary gland;stomach;thymus; superior cervical ganglion;placenta; 0.47294 0.11730 -0.492218069 22.35786742 44.25896 1.26882 CISTR . . . chondrogenesis-associated transcript . . . . . . . . . . . CIT 0.999998739281467 1.26071853313229e-06 4.31141446977079e-24 citron rho-interacting serine/threonine kinase FUNCTION: Plays a role in cytokinesis. Required for KIF14 localization to the central spindle and midbody. Putative RHO/RAC effector that binds to the GTP-bound forms of RHO and RAC1. It probably binds p21 with a tighter specificity in vivo. Displays serine/threonine protein kinase activity. Plays an important role in the regulation of cytokinesis and the development of the central nervous system. Phosphorylates MYL9/MLC2. {ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:21457715}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;oesophagus;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;nervous;tongue;blood;lens;skeletal muscle;bile duct;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; amygdala;dorsal root ganglion;occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;pons;caudate nucleus;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.38018 0.37052 -2.354066177 1.144137768 351.69768 3.97507 CITED1 0.0454033926143545 0.671962679540734 0.282633927844912 Cbp/p300 interacting transactivator with Glu/Asp rich carboxy-terminal domain 1 FUNCTION: Transcriptional coactivator of the p300/CBP-mediated trancription complex. Enhances SMAD-mediated transcription by strengthening the functional link between the DNA-binding SMAD transcription factors and the p300/CBP transcription coactivator complex. Stimulates estrogen-dependent transactivation activity mediated by estrogen receptors signaling; stabilizes the interaction of estrogen receptor ESR1 and histone acetyltransferase EP300. Positively regulates TGF-beta signaling through its association with the SMAD/p300/CBP-mediated transcriptional coactivator complex. Induces transcription from estrogen-responsive promoters and protection against cell death. Potentiates EGR2-mediated transcriptional activation activity from the ERBB2 promoter. Acts as an inhibitor of osteoblastic mineralization through a cAMP-dependent parathyroid hormone receptor signaling. May play a role in pigmentation of melanocytes. Associates with chromatin to the estrogen-responsive TGF-alpha promoter region in a estrogen-dependent manner. {ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:11581164, ECO:0000269|PubMed:21172805}.; . TISSUE SPECIFICITY: Expressed only in melanocytes and testis.; unclassifiable (Anatomical System);ovary;hypothalamus;colon;fovea centralis;choroid;lens;skin;retina;optic nerve;whole body;lung;thyroid;macula lutea;iris;testis;kidney;brain; whole brain;thalamus;testis - interstitial;testis - seminiferous tubule;hypothalamus;testis;pituitary;parietal lobe;cingulate cortex;skeletal muscle; 0.39454 0.14988 0.459411326 78.28497287 9.11134 0.33286 CITED2 0.706861723944729 0.277581096026204 0.0155571800290674 Cbp/p300 interacting transactivator with Glu/Asp rich carboxy-terminal domain 2 FUNCTION: Transcriptional coactivator of the p300/CBP-mediated trancription complex. Acts as a bridge, linking TFAP2 transcription factors and the p300/CBP transcriptional coactivator complex in order to stimulate TFAP2-mediated transcriptional activation. Positively regulates TGF-beta signaling through its association with the SMAD/p300/CBP-mediated transcriptional coactivator complex. Stimulates the peroxisome proliferator- activated receptors PPARA transcriptional activity. Enhances estrogen-dependent transactivation mediated by estrogen receptors. Acts also as a transcriptional corepressor; interferes with the binding of the transcription factors HIF1A or STAT2 and the p300/CBP transcriptional coactivator complex. Participates in sex determination and early gonad development by stimulating transcription activation of SRY. Plays a role in controlling left- right patterning during embryogenesis; potentiates transcriptional activation of NODAL-mediated gene transcription in the left lateral plate mesoderm (LPM). Plays an essential role in differentiation of the adrenal cortex from the adrenogonadal primordium (AGP); stimulates WT1-mediated transcription activation thereby up-regulating the nuclear hormone receptor NR5A1 promoter activity. Associates with chromatin to the PITX2 P1 promoter region. {ECO:0000269|PubMed:11581164, ECO:0000269|PubMed:12586840, ECO:0000269|PubMed:15051727}.; DISEASE: Ventricular septal defect 2 (VSD2) [MIM:614431]: A common form of congenital cardiovascular anomaly that may occur alone or in combination with other cardiac malformations. It can affect any portion of the ventricular septum, resulting in abnormal communications between the two lower chambers of the heart. Classification is based on location of the communication, such as perimembranous, inlet, outlet (infundibular), central muscular, marginal muscular, or apical muscular defect. Large defects that go unrepaired may give rise to cardiac enlargement, congestive heart failure, pulmonary hypertension, Eisenmenger's syndrome, delayed fetal brain development, arrhythmias, and even sudden cardiac death. {ECO:0000269|PubMed:16287139}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Atrial septal defect 8 (ASD8) [MIM:614433]: A congenital heart malformation characterized by incomplete closure of the wall between the atria resulting in blood flow from the left to the right atria. {ECO:0000269|PubMed:16287139}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.74428 0.37204 -0.293801652 32.93819297 64.10056 1.64155 CITED4 0.358265028581015 0.482802882642258 0.158932088776727 Cbp/p300 interacting transactivator with Glu/Asp rich carboxy-terminal domain 4 FUNCTION: Acts as transcriptional coactivator for TFAP2/AP-2. Enhances estrogen-dependent transactivation mediated by estrogen receptors. May function as an inhibitor of transactivation by HIF1A by disrupting HIF1A interaction with CREBBP. May be involved in regulation of gene expression during development and differentiation of blood cells, endothelial cells and mammary epithelial cells. {ECO:0000269|PubMed:11744733, ECO:0000269|PubMed:15342390}.; . TISSUE SPECIFICITY: Expressed in most tissues examined with highest levels of expression in heart, liver, skeletal muscle and pancreas. Also expressed in bladder cell line ECV-304 and in various breast cancer cell lines. Also detected in both in situ and invasive breast tumors where its expression is down-regulated and mostly restricted to the cytoplasm of malignant epithelium. Down-regulation of expression is associated with elevated levels of HIF1A and increased tumor growth and angiogenesis. {ECO:0000269|PubMed:11744733, ECO:0000269|PubMed:15342390}.; . . 0.23880 . . . 3280.66773 10.93493 CIZ1 0.993095776092735 0.00690422192780482 1.97945984246903e-09 CDKN1A interacting zinc finger protein 1 FUNCTION: May regulate the subcellular localization of CIP/WAF1.; DISEASE: Note=Defects in CIZ1 may be a cause of adult onset primary cervical dystonia. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. Cervical dystonia or spasmodic torticollis, the most common form of focal dystonia, is characterized by involuntary contractions of the neck muscles, which produce abnormal posturing of the head upon the trunk.; . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;testis - interstitial;subthalamic nucleus;prefrontal cortex;testis;ciliary ganglion;skeletal muscle; 0.10121 0.09070 -0.350843407 29.54116537 422.14014 4.29312 CKAP2 3.96231847753185e-08 0.564196281744878 0.435803678631937 cytoskeleton associated protein 2 FUNCTION: Possesses microtubule stabilizing properties. Involved in regulating aneuploidy, cell cycling, and cell death in a p53/TP53-dependent manner (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Abundant in testis, thymus, and in tumor derived cell lines, while barely detectable in liver, prostate, and kidney. {ECO:0000269|PubMed:9771967}.; medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;cornea;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; fetal liver;superior cervical ganglion;testis - seminiferous tubule;testis;skeletal muscle; 0.36857 0.99304 1.223576934 93.23543289 106.17181 2.23584 CKAP2L 0.218393604055394 0.781252023037621 0.000354372906985688 cytoskeleton associated protein 2 like FUNCTION: Microtubule-associated protein required for mitotic spindle formation and cell-cycle progression in neural progenitor cells. {ECO:0000269|PubMed:25439729}.; DISEASE: Filippi syndrome (FLPIS) [MIM:272440]: A rare disorder characterized by microcephaly, pre- and postnatal growth failure, syndactyly, and distinctive facial features, including a broad nasal bridge and underdeveloped alae nasi. Some affected individuals have intellectual disability, seizures, undescended testicles in males, and teeth and hair abnormalities. {ECO:0000269|PubMed:25439729}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);adrenal cortex;colon;uterus;breast;whole body;lung;bone;placenta;liver;testis;spleen;cervix;germinal center;kidney;brain; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.04464 0.07489 1.381566496 94.62137297 2966.9101 10.32687 CKAP2P1 . . . cytoskeleton associated protein 2 pseudogene 1 . . . . . . . . . . . CKAP4 0.891862493984838 0.10704367966096 0.00109382635420114 cytoskeleton-associated protein 4 FUNCTION: High-affinity epithelial cell surface receptor for APF.; . . . . 0.38998 0.10822 -0.909290275 10.03184713 349.83122 3.96399 CKAP5 0.99999999753418 2.46581965337628e-09 7.83709816948967e-26 cytoskeleton associated protein 5 FUNCTION: Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Plays a major role in organizing spindle poles. {ECO:0000269|PubMed:12569123, ECO:0000269|PubMed:21646404}.; . TISSUE SPECIFICITY: Overexpressed in hepatomas and colonic tumors. Also expressed in skeletal muscle, brain, heart, placenta, lung, liver, kidney and pancreas.; medulla oblongata;smooth muscle;ovary;substantia nigra;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;kidney;stomach;aorta;cerebellum; occipital lobe;subthalamic nucleus;medulla oblongata;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;pons;trigeminal ganglion;parietal lobe;cingulate cortex; 0.84878 0.18825 -1.611264137 2.984194385 164.46097 2.80050 CKB 0.85084546139957 0.148627795297947 0.000526743302483326 creatine kinase, brain FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.; . . myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;brain;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;epididymis;visual apparatus;macula lutea;liver;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);epidermis;cerebellum cortex;islets of Langerhans;muscle;pancreas;lung;cornea;placenta;head and neck;kidney;stomach; . 0.48985 0.83418 -0.405853867 26.23260203 25.11031 0.82185 CKBE . . . creatine kinase, ectopic expression . . . . . . . . . . . CKBP1 . . . creatine kinase B pseudogene 1 . . . . . . . . . . . CKLF 0.0270931084047075 0.793152754796435 0.179754136798857 chemokine-like factor FUNCTION: May play an important role in inflammation and regeneration of skeletal muscle. Partly inhibited by interleukin 10. {ECO:0000269|PubMed:11415443}.; . TISSUE SPECIFICITY: Isoform 1, isoform 2, isoform 3 and isoform 4 have highest expression levels in adult spleen, lung, testis, ovary, peripheral blood leukocyte, placenta, pancreas, and in fetal brain, skeletal muscle, thymus and heart. Lower expression levels in adult skeletal muscle, liver, thymus colon, prostate and fetal spleen and liver. {ECO:0000269|PubMed:11415443}.; ovary;umbilical cord;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;testis;bladder;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;adrenal cortex;pharynx;blood;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; testis - interstitial;superior cervical ganglion;testis;white blood cells;whole blood;trigeminal ganglion;bone marrow; 0.10901 0.09549 -0.207437529 38.2814343 14.53697 0.52325 CKLF-CMTM1 0.00802844948907333 0.556738384459605 0.435233166051322 CKLF-CMTM1 readthrough . . . . . . . 0.281220278 71.07808445 26.88279 0.86906 CKM 0.00505058616928749 0.887114368069828 0.107835045760884 creatine kinase, M-type FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.; . . unclassifiable (Anatomical System);myocardium;heart;muscle;skin;skeletal muscle;retina;greater omentum;uterus;whole body;lung;larynx;bone;placenta;visual apparatus;alveolus;liver;head and neck;spleen;kidney; prostate;heart;tongue;thyroid;testis;fetal thyroid;skeletal muscle; 0.29357 0.79524 -0.111973265 45.35857514 59.58012 1.56701 CKMT1A 0.0141217929367762 0.869820144402519 0.116058062660705 creatine kinase, mitochondrial 1A FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.; . . . . 0.35189 0.67614 . . 39.02629 1.15668 CKMT1B 0.0732106469813755 0.872395807803641 0.0543935452149835 creatine kinase, mitochondrial 1B FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.; . . ovary;colon;parathyroid;skin;retina;uterus;prostate;frontal lobe;larynx;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cerebellum cortex;islets of Langerhans;hypothalamus;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; . 0.09829 0.66519 . . 101.35902 2.17899 CKMT2 7.87308868812856e-10 0.258673217343711 0.74132678186898 creatine kinase, mitochondrial 2 FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.; . TISSUE SPECIFICITY: Sarcomere-specific. Found only in heart and skeletal muscles.; unclassifiable (Anatomical System);myocardium;heart;ovary;muscle;colon;parathyroid;skin;skeletal muscle;uterus;pancreas;prostate;optic nerve;whole body;lung;adrenal gland;placenta;liver;testis;spleen;kidney;brain;mammary gland; superior cervical ganglion;heart;tongue;skeletal muscle; 0.15786 0.61541 -0.624497208 17.16206653 43.35555 1.25279 CKMT2-AS1 . . . CKMT2 antisense RNA 1 . . . . . . . . . . . CKS1B 0.723280936456517 0.263463637268446 0.0132554262750368 CDC28 protein kinase regulatory subunit 1B FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;testis;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;heart;lacrimal gland;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; . 0.93472 . 0.101211609 60.95777306 168.37294 2.83278 CKS1BP1 . . . CDC28 protein kinase regulatory subunit 1B pseudogene 1 . . . . . . . . . . . CKS1BP2 . . . CDC28 protein kinase regulatory subunit 1B pseudogene 2 . . . . . . . . . . . CKS1BP3 . . . CDC28 protein kinase regulatory subunit 1B pseudogene 3 . . . . . . . . . . . CKS1BP4 . . . CDC28 protein kinase regulatory subunit 1B pseudogene 4 . . . . . . . . . . . CKS1BP5 . . . CDC28 protein kinase regulatory subunit 1B pseudogene 5 . . . . . . . . . . . CKS1BP6 . . . CDC28 protein kinase regulatory subunit 1B pseudogene 6 . . . . . . . . . . . CKS1BP7 . . . CDC28 protein kinase regulatory subunit 1B pseudogene 7 . . . . . . . . . . . CKS2 0.383050486929908 0.572672909750533 0.0442766033195587 CDC28 protein kinase regulatory subunit 2 FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function.; . . . . 0.95198 0.22085 0.035072054 56.2514744 1.20885 0.03814 CLA3 . . . cerebellar ataxia 3 (cerebellar parenchyma disorder 1) . . . . . . . . . . . CLAM . . . cerebellar atrophy with progressive microcephaly . . . . . . . . . . . CLASP1 0.999999988870922 1.11290777987194e-08 7.51999369369508e-23 cytoplasmic linker associated protein 1 FUNCTION: Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. {ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:12837247, ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514, ECO:0000269|PubMed:17543864}.; . . ovary;salivary gland;developmental;intestine;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach; amygdala;whole brain;medulla oblongata;fetal brain;cerebellum peduncles;prefrontal cortex;caudate nucleus;cingulate cortex;cerebellum; 0.29685 0.14697 -1.905192093 1.940316112 204.91732 3.09189 CLASP2 0.999948359508774 5.16404912259731e-05 1.07561651771381e-16 cytoplasmic linker associated protein 2 FUNCTION: Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2- dependent stabilization of microtubules at the cell cortex. {ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:16824950, ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514, ECO:0000269|PubMed:17543864, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:26003921}.; . TISSUE SPECIFICITY: Brain-specific.; ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;brain;heart;cartilage;tongue;spinal cord;blood;lens;skeletal muscle;breast;greater omentum;macula lutea;visual apparatus;liver;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;thymus; amygdala;medulla oblongata;superior cervical ganglion;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.48367 0.14642 . . 656.28546 5.13608 CLASRP 0.964966482147783 0.035033513438495 4.41372178274413e-09 CLK4-associating serine/arginine rich protein FUNCTION: Probably functions as an alternative splicing regulator. May regulate the mRNA splicing of genes such as CLK1. May act by regulating members of the CLK kinase family (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;skin;retina;uterus;whole body;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lacrimal gland;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;hypopharynx;spleen;head and neck;kidney;stomach; superior cervical ganglion;testis;atrioventricular node; 0.18785 0.14723 -0.758599262 13.32861524 238.99747 3.33909 CLC 3.41778388787621e-05 0.360028298856551 0.639937523304571 Charcot-Leyden crystal galectin FUNCTION: Regulates immune responses through the recognition of cell-surface glycans. Essential for the anergy and suppressive function of CD25-positive regulatory T-cells (Treg). {ECO:0000269|PubMed:17502455}.; . TISSUE SPECIFICITY: Expressed abundantly in the bone marrow. Expressed exclusively by eosinophils and basophils. Not detected in monocytes and neutrophils. Expressed in CD25-positive regulatory T-cells (Treg) (at protein level). Found in intestinal tissue from patients with Celiac disease, expression is directly related to the histological grade of mucosal damage and to the number of eosinophils found in the duodenal lesion (at protein level). Found in sputum of patients with eosinophilic inflammatory diseases such as asthma (at protein level). {ECO:0000269|PubMed:17502455, ECO:0000269|PubMed:19497882, ECO:0000269|PubMed:19758173, ECO:0000269|PubMed:22880030}.; unclassifiable (Anatomical System);lung;whole body;heart;testis;spleen; whole blood;bone marrow; 0.04310 0.08784 0.525552348 80.57914603 152.55485 2.70177 CLCA1 6.08038432284723e-06 0.998721251539757 0.00127266807592013 chloride channel accessory 1 FUNCTION: May be involved in mediating calcium-activated chloride conductance. May play critical roles in goblet cell metaplasia, mucus hypersecretion, cystic fibrosis and AHR. May be involved in the regulation of mucus production and/or secretion by goblet cells. Involved in the regulation of tissue inflammation in the innate immune response. May play a role as a tumor suppressor. Induces MUC5AC. {ECO:0000269|PubMed:11445004, ECO:0000269|PubMed:11842292, ECO:0000269|PubMed:11956057, ECO:0000269|PubMed:23112050, ECO:0000269|PubMed:9828122}.; . TISSUE SPECIFICITY: Highly expressed in small intestine and colon namely in intestinal basal crypt epithelia and goblet cells, and appendix. Weakly expressed in uterus, testis and kidney. Expressed in the airways epithelium of both asthmatic and healthy patients. Expressed in the bronchial epithelium, especially in mucus- producing goblet cells. Expressed in normal turbinate mucosa and nasal polyp. Expressed in. {ECO:0000269|PubMed:10437792, ECO:0000269|PubMed:11842292, ECO:0000269|PubMed:11956057, ECO:0000269|PubMed:16012037, ECO:0000269|PubMed:9828122}.; unclassifiable (Anatomical System);lung;testis;colon;skeletal muscle; dorsal root ganglion;superior cervical ganglion;appendix;pons;atrioventricular node;trigeminal ganglion; 0.04515 0.14318 0.249861693 69.66265629 286.69998 3.62673 CLCA2 1.90835519560536e-20 0.00302891115175848 0.996971088848241 chloride channel accessory 2 FUNCTION: Plays a role in modulating chloride current across the plasma membrane in a calcium-dependent manner, and cell adhesion. Involved in basal cell adhesion and/or stratification of squamous epithelia. May act as a tumor suppressor in breast and colorectal cancer. Plays a key role for cell adhesion in the beginning stages of lung metastasis via the binding to ITGB4. {ECO:0000269|PubMed:10554024, ECO:0000269|PubMed:11320086, ECO:0000269|PubMed:11445004, ECO:0000269|PubMed:15707651, ECO:0000269|PubMed:16158324}.; . TISSUE SPECIFICITY: Expressed in cornea, skin, vagina, esophagus, and larynx (at protein level). Expressed in trachea and mammary gland. Weakly expressed in testis and kidney. Highly expressed in corneal epithelium, colon and trachea. Moderately expressed in brain, urogenital organs, bladder, uterus and prostate. Highly expressed in tissues containing stratified epithelium including cornea, esophagus, larynx, skin and vagina than those tissues which contain only epithelial monolayers. Expressed in normal breast epithelium but not in breast cancer. Highly expressed during epithelial stratification. Expressed in endothelial cells of lung. Expressed selectively in endothelia of small pulmonary arteries, arterioles, and subpleural and interlobular venules. {ECO:0000269|PubMed:10362588, ECO:0000269|PubMed:10437792, ECO:0000269|PubMed:10554024, ECO:0000269|PubMed:11262615, ECO:0000269|PubMed:11320086, ECO:0000269|PubMed:14966209, ECO:0000269|PubMed:15707651, ECO:0000269|PubMed:16158324}.; . . 0.17798 0.15716 -0.036738982 50.53668318 3264.55081 10.90748 CLCA3P . . . chloride channel accessory 3, pseudogene . . TISSUE SPECIFICITY: Expressed in the lung, trachea, spleen, thymus and mammary gland. {ECO:0000269|PubMed:10095065}.; unclassifiable (Anatomical System);lung; . 0.09368 . . . . . CLCA4 3.19440293023477e-09 0.740096655765701 0.259903341039896 chloride channel accessory 4 FUNCTION: May be involved in mediating calcium-activated chloride conductance.; . TISSUE SPECIFICITY: Primarily expressed in the digestive tract, mainly in colon. Detected in smaller amounts in brain, urogenital organs, testis, and salivary and mammary glands. Highly expressed in the epithelial layer and submucosal gland of the inferior turbinate mucosa. Lower levels in the epithelial layer of nasal polyp. {ECO:0000269|PubMed:10437792, ECO:0000269|PubMed:15490240, ECO:0000269|PubMed:16012037}.; unclassifiable (Anatomical System);prostate;lung;endometrium;thyroid;colon;head and neck;brain;bladder;skeletal muscle;tonsil; appendix;ciliary ganglion;skin; 0.11919 0.12223 -0.751322189 13.71196037 680.37144 5.21430 CLCC1 0.0267100875839262 0.970803148364674 0.00248676405139942 chloride channel CLIC like 1 FUNCTION: Seems to act as a chloride ion channel. {ECO:0000250}.; . . sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;spinal cord;trigeminal ganglion;skeletal muscle; 0.13110 0.12667 1.043548753 91.30691201 1176.15749 6.51440 CLCF1 0.860488104474125 0.13739665116023 0.00211524436564564 cardiotrophin-like cytokine factor 1 FUNCTION: Cytokine with B-cell stimulating capability. Binds to and activates the ILST/gp130 receptor. {ECO:0000269|PubMed:10448081, ECO:0000269|PubMed:10500198}.; . TISSUE SPECIFICITY: Expressed predominantly in lymph nodes, spleen, peripheral blood lymphocytes, bone marrow, and fetal liver. {ECO:0000269|PubMed:10448081, ECO:0000269|PubMed:10500198}.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;blood;skin;bone marrow;uterus;lung;bone;placenta;hypopharynx;head and neck;germinal center;kidney;brain;stomach; appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.38031 0.24760 -0.005381972 53.50908233 143.12981 2.60806 CLCN1 6.82240250810421e-13 0.823526407581218 0.1764735924181 chloride voltage-gated channel 1 FUNCTION: Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume; membrane potential stabilization, signal transduction and transepithelial transport.; DISEASE: Myotonia congenita, autosomal recessive (MCAR) [MIM:255700]: A non-dystrophic skeletal muscle disorder characterized by muscle stiffness and an inability of the muscle to relax after voluntary contraction. Most patients have symptom onset in the legs, which later progresses to the arms, neck, and facial muscles. Many patients show marked hypertrophy of the lower limb muscles. The autosomal recessive form (Becker disease) is more severe than the autosomal dominant one (Thomsen disease). {ECO:0000269|PubMed:10215406, ECO:0000269|PubMed:1379744, ECO:0000269|PubMed:7874130, ECO:0000269|PubMed:7951242, ECO:0000269|PubMed:7981681, ECO:0000269|PubMed:8571958}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in skeletal muscles.; . . 0.42478 . 0.207589927 67.52182118 2276.75462 8.82576 CLCN2 2.26513810859121e-07 0.99881222888228 0.00118754460390946 chloride voltage-gated channel 2 FUNCTION: Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume; membrane potential stabilization, signal transduction and transepithelial transport. {ECO:0000269|PubMed:19153159, ECO:0000269|PubMed:19191339}.; DISEASE: Epilepsy, idiopathic generalized 11 (EIG11) [MIM:607628]: A disorder characterized by recurring generalized seizures in the absence of detectable brain lesions and/or metabolic abnormalities. Generalized seizures arise diffusely and simultaneously from both hemispheres of the brain. {ECO:0000269|PubMed:19191339}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Juvenile absence epilepsy 2 (JAE2) [MIM:607628]: A subtype of idiopathic generalized epilepsy characterized by onset occurring around puberty, absence seizures, generalized tonic- clonic seizures (GTCS), GTCS on awakening, and myoclonic seizures. {ECO:0000269|PubMed:12612585, ECO:0000269|PubMed:19710712}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; DISEASE: Juvenile myoclonic epilepsy 8 (EJM8) [MIM:607628]: A subtype of idiopathic generalized epilepsy. Patients have afebrile seizures only, with onset in adolescence (rather than in childhood) and myoclonic jerks which usually occur after awakening and are triggered by sleep deprivation and fatigue. {ECO:0000269|PubMed:19191339}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Leukoencephalopathy with ataxia (LKPAT) [MIM:615651]: An autosomal recessive neurologic disorder with a characteristic pattern of white matter abnormalities on brain MRI. Affected individuals have prominent signal abnormalities and decreased apparent diffusion coefficient values in the posterior limbs of the internal capsules, middle cerebral peduncles, pyramidal tracts in the pons, and middle cerebellar peduncles, suggesting myelin microvacuolation. Clinical features include ataxia and unstable gait. More variable abnormalities may include visual field defects, headaches, and learning disabilities. {ECO:0000269|PubMed:23707145}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. Moderately expressed in aortic and coronary vascular smooth muscle cells and expressed at a low level in aortic endothelial cells. {ECO:0000269|PubMed:10198195}.; colon;choroid;fovea centralis;skin;retina;uterus;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach;thymus; testis;atrioventricular node; 0.19630 0.18747 0.497836815 79.65911772 3684.52461 11.81746 CLCN3 0.993264929284599 0.0067350615086253 9.20677575738198e-09 chloride voltage-gated channel 3 FUNCTION: Mediates the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the endosome and synaptic vesicle lumen, and may thereby affect vesicle trafficking and exocytosis. May play an important role in neuronal cell function through regulation of membrane excitability by protein kinase C. It could help neuronal cells to establish short-term memory. {ECO:0000269|PubMed:11967229}.; . TISSUE SPECIFICITY: Expressed primarily in tissues derived from neuroectoderm. Within the brain, its expression is particularly evident in the hippocampus, olfactory cortex, and olfactory bulb. Highly expressed in aortic and coronary vascular smooth muscle cells, and aortic endothelial cells. Also expressed in tracheal and alveolar epithelial cells, and intima and media of the pulmonary vessels. Expressed in bronchus and colon (at protein level). {ECO:0000269|PubMed:10198195, ECO:0000269|PubMed:11967229, ECO:0000269|PubMed:12471024}.; smooth muscle;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;spinal cord;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;aorta;stomach;peripheral nerve; amygdala;medulla oblongata;thalamus;occipital lobe;superior cervical ganglion;hypothalamus;temporal lobe;spinal cord;caudate nucleus;skeletal muscle;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.48647 0.24527 -0.580403979 18.58928993 61.92777 1.60444 CLCN3P1 . . . chloride voltage-gated channel 3 pseudogene 1 . . . . . . . . . . . CLCN4 0.988787920457612 0.0112082119272173 3.86761517115471e-06 chloride voltage-gated channel 4 FUNCTION: Proton-coupled chloride transporter. Functions as antiport system and exchanges chloride ions against protons. {ECO:0000269|PubMed:18063579}.; . TISSUE SPECIFICITY: Abundant in skeletal muscle and also detectable in brain and heart.; . . 0.31959 0.18328 -1.089312628 7.047652748 12.98219 0.47295 CLCN5 0.9942416657125 0.00575818098873484 1.53298764717873e-07 chloride voltage-gated channel 5 FUNCTION: Proton-coupled chloride transporter. Functions as antiport system and exchanges chloride ions against protons. Important for normal acidification of the endosome lumen. May play an important role in renal tubular function.; DISEASE: Hypophosphatemic rickets, X-linked recessive (XLRHR) [MIM:300554]: A renal disease belonging to the 'Dent disease complex', a group of disorders characterized by proximal renal tubular defect, hypercalciuria, nephrocalcinosis, and renal insufficiency. The spectrum of phenotypic features is remarkably similar in the various disorders, except for differences in the severity of bone deformities and renal impairment. XLRH patients present with rickets or osteomalacia, hypophosphatemia due to decreased renal tubular phosphate reabsorption, hypercalciuria, and low molecular weight proteinuria. Patients develop nephrocalcinosis with progressive renal failure in adulthood. Female carriers may have asymptomatic hypercalciuria or hypophosphatemia only. {ECO:0000269|PubMed:8559248}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Nephrolithiasis 2 (NPHL2) [MIM:300009]: An X-linked recessive renal disease belonging to the 'Dent disease complex', a group of disorders characterized by proximal renal tubular defect, hypercalciuria, nephrocalcinosis, and renal insufficiency. The spectrum of phenotypic features is remarkably similar in the various disorders, except for differences in the severity of bone deformities and renal impairment. Nephrolithiasis type 2 patients manifest hypercalciuria, hypophosphatemia, aminoaciduria, nephrocalcinosis and nephrolithiasis, renal insufficiency leading to renal failure in adulthood, rickets (33% of patients) and osteomalacia. {ECO:0000269|PubMed:15086899, ECO:0000269|PubMed:16247550, ECO:0000269|PubMed:16416111, ECO:0000269|PubMed:16822791, ECO:0000269|PubMed:17262170, ECO:0000269|PubMed:19657328, ECO:0000269|PubMed:8559248, ECO:0000269|PubMed:9187673, ECO:0000269|PubMed:9259268, ECO:0000269|PubMed:9602200, ECO:0000269|PubMed:9853249}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Nephrolithiasis 1 (NPHL1) [MIM:310468]: An X-linked recessive renal disease belonging to the 'Dent disease complex', a group of disorders characterized by proximal renal tubular defect, hypercalciuria, nephrocalcinosis and renal insufficiency. The spectrum of phenotypic features is remarkably similar in the various disorders, except for differences in the severity of bone deformities and renal impairment. Nephrolithiasis type 1 presents with hypercalciuria, nephrocalcinosis, renal stones and renal insufficiency. Patients lack urinary acidification defects, rickets, and osteomalacia. {ECO:0000269|PubMed:8559248}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Low molecular weight proteinuria with hypercalciuria and nephrocalcinosis (LMWPHN) [MIM:308990]: An X-linked renal disease belonging to the 'Dent disease complex', a group of disorders characterized by proximal renal tubular defect, hypercalciuria, nephrocalcinosis, and renal insufficiency. The spectrum of phenotypic features is remarkably similar in the various disorders, except for differences in the severity of bone deformities and renal impairment. LMWPHN is a slowly progressive disorder. Patients tend to have hypercalciuric nephrocalcinosis without rickets or renal failure. {ECO:0000269|PubMed:11136179, ECO:0000269|PubMed:9062355}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Kidney. Moderately expressed in aortic vascular smooth muscle and endothelial cells, and at a slightly higher level in the coronary vascular smooth muscle. {ECO:0000269|PubMed:10198195}.; unclassifiable (Anatomical System);visual apparatus;testis;blood;kidney;skin;skeletal muscle;bone marrow; dorsal root ganglion;superior cervical ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.51707 0.45685 0.018483465 55.44939844 74.64626 1.80634 CLCN6 0.163974191293187 0.836024751361391 1.05734542226292e-06 chloride voltage-gated channel 6 FUNCTION: Chloride transport protein, initially identified as voltage-gated chloride channel. The presence of the conserved gating glutamate residues suggests that is functions as antiporter.; . TISSUE SPECIFICITY: Testis, ovary, small intestine, brain and skeletal muscle. Low level expression in aortic and coronary vascular smooth muscle cells, and aortic endothelial cells. Isoform 3 is only detected in kidney. {ECO:0000269|PubMed:10198195, ECO:0000269|PubMed:8543009, ECO:0000269|PubMed:9224655}.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;stomach;thymus; whole brain;amygdala;thalamus;medulla oblongata;subthalamic nucleus;hypothalamus;spinal cord;prefrontal cortex;globus pallidus;pons;caudate nucleus;cingulate cortex;cerebellum; 0.43875 0.19623 -1.570776628 3.172918141 371.5394 4.06812 CLCN7 0.981282976462541 0.0187170006805023 2.28569564670678e-08 chloride voltage-gated channel 7 FUNCTION: Slowly voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the lysosome lumen. {ECO:0000269|PubMed:18449189, ECO:0000269|PubMed:21527911}.; DISEASE: Osteopetrosis, autosomal dominant 2 (OPTA2) [MIM:166600]: A rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. OPTA2 is the most common form of osteopetrosis, occurring in adolescence or adulthood. It is characterized by sclerosis, predominantly involving the spine, the pelvis and the skull base. {ECO:0000269|PubMed:11741829, ECO:0000269|PubMed:14584882, ECO:0000269|PubMed:19953639}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Brain, testis, muscle and kidney.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;oesophagus;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland; amygdala;adrenal gland;prefrontal cortex;adrenal cortex;globus pallidus;trigeminal ganglion;cingulate cortex; 0.23813 0.29785 -1.636932785 2.824958717 1046.80561 6.20986 CLCNKA 2.74927659103062e-14 0.0661983059816697 0.933801694018303 chloride voltage-gated channel Ka FUNCTION: Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume; membrane potential stabilization, signal transduction and transepithelial transport. May be important in urinary concentrating mechanisms.; . TISSUE SPECIFICITY: Expressed predominantly in the kidney. All nephron segments expressing BSND also express CLCNK proteins. {ECO:0000269|PubMed:11734858}.; prostate;lung;ovary;heart;thyroid;placenta;parathyroid;spleen;kidney;brain; . 0.11960 0.19227 1.539567688 95.57678698 1257.07472 6.68592 CLCNKB 7.80835912699469e-12 0.411913167741263 0.588086832250929 chloride voltage-gated channel Kb FUNCTION: Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume; membrane potential stabilization, signal transduction and transepithelial transport. May be important in urinary concentrating mechanisms. {ECO:0000269|PubMed:11734858}.; DISEASE: Bartter syndrome 4B (BS4B) [MIM:613090]: A digenic, recessive disorder characterized by impaired salt reabsorption in the thick ascending loop of Henle with pronounced salt wasting, hypokalemic metabolic alkalosis, and varying degrees of hypercalciuria. Bartter syndrome type 4B is associated with sensorineural deafness. {ECO:0000269|PubMed:15044642, ECO:0000269|PubMed:18310267}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. Loss-of-function of both CLCNKA and CLCNKB results in the disease phenotype (PubMed:18310267). {ECO:0000269|PubMed:18310267}.; TISSUE SPECIFICITY: Expressed predominantly in the kidney. {ECO:0000269|PubMed:11734858}.; unclassifiable (Anatomical System);prostate;ovary;heart;thyroid;placenta;parathyroid;kidney;brain; superior cervical ganglion;thyroid;globus pallidus;atrioventricular node;kidney; 0.13874 0.30007 0.698081425 85.30313753 1051.72265 6.22752 CLCP1 . . . Charcot-Leyden crystal protein pseudogene 1 . . . . . . . . . . . CLCP2 . . . Charcot-Leyden crystal protein pseudogene 2 . . . . . . . . . . . CLDN1 0.0581349308262247 0.867215583377384 0.0746494857963918 claudin 1 FUNCTION: Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN1 is required to prevent the paracellular diffusion of small molecules through tight junctions in the epidermis and is required for the normal barrier function of the skin. Required for normal water homeostasis and to prevent excessive water loss through the skin, probably via an indirect effect on the expression levels of other proteins, since CLDN1 itself seems to be dispensable for water barrier formation in keratinocyte tight junctions (PubMed:23407391). {ECO:0000269|PubMed:23407391}.; . TISSUE SPECIFICITY: Strongly expressed in liver and kidney. Expressed in heart, brain, spleen, lung and testis. {ECO:0000269|PubMed:9931503}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;oesophagus;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;oral cavity;urinary;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;visual apparatus;amnion;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;fetal liver;ciliary ganglion;trigeminal ganglion; 0.22855 0.23494 -0.117432389 44.89266336 796.30708 5.56205 CLDN2 0.605106671731875 0.358604021375596 0.0362893068925288 claudin 2 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}.; . . unclassifiable (Anatomical System);meninges;smooth muscle;tongue;islets of Langerhans;colon;skin;retina;prostate;pia mater;lung;liver;testis;head and neck;spleen;dura mater;kidney;stomach; . 0.31239 0.10659 0.147123112 64.11299835 184.13575 2.94550 CLDN3 0.678537320145956 0.301315084096108 0.0201475957579362 claudin 3 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}.; DISEASE: Note=CLDN3 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region.; . . . 0.19570 0.11142 0.415317661 76.81056853 40.15919 1.18022 CLDN4 0.00013715830896755 0.236464038050909 0.763398803640124 claudin 4 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space. {ECO:0000250}.; DISEASE: Note=CLDN4 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region.; . unclassifiable (Anatomical System);lymph node;ovary;heart;lacrimal gland;colon;skin;breast;uterus;pancreas;prostate;lung;endometrium;thyroid;placenta;liver;testis;cervix;spleen;kidney;brain;mammary gland;bladder;stomach; prostate;placenta;thyroid;fetal thyroid; 0.24625 0.25713 -0.582225231 18.44184949 35.5133 1.07087 CLDN5 0.74051961882886 0.248379981265283 0.0111003999058578 claudin 5 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space. {ECO:0000250}.; . . . . 0.20514 0.28644 . . 1789.94394 7.80913 CLDN6 0.0104295146810942 0.612458371702858 0.377112113616048 claudin 6 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space (By similarity). May act as a coreceptor for HCV entry into hepatic cells. {ECO:0000250, ECO:0000269|PubMed:17804490}.; . TISSUE SPECIFICITY: Expressed in the liver, in peripheral blood mononuclear cells and hepatocarcinoma cell lines. {ECO:0000269|PubMed:17804490}.; unclassifiable (Anatomical System);lung;ovary;placenta;duodenum;spleen;brain;stomach; . 0.52356 0.14726 0.150760231 64.51403633 1846.15663 7.92738 CLDN7 0.0413847351651376 0.844593230680556 0.114022034154306 claudin 7 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in kidney, lung and prostate. Isoform 1 seems to be predominant, except in some normal prostate samples, where isoform 2 is the major form. Down-regulated in breast cancers, including ductal carcinoma in situ (DCIS), lobular carcinoma in situ (LCIS) and invasive ductal carcinoma (IDC) (at protein level), as well as in several cancer cell lines. Loss of expression correlates with histological grade, occurring predominantly in high-grade lesions. {ECO:0000269|PubMed:12673207, ECO:0000269|PubMed:14502431}.; ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;oesophagus;endometrium;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;heart;skeletal muscle;breast;pancreas;lung;cornea;epididymis;nasopharynx;placenta;liver;spleen;cervix;kidney;mammary gland;stomach; prostate;lung;trachea;thyroid;placenta; 0.23428 0.08685 -0.005381972 53.50908233 34.53437 1.05442 CLDN8 0.0576343766009805 0.711617623710263 0.230747999688757 claudin 8 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the epididymis, mainly in the caput segment. {ECO:0000269|PubMed:17287494}.; unclassifiable (Anatomical System);breast;prostate;lung;thyroid;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skin; 0.11919 0.12867 1.038098315 91.20665251 3058.62081 10.51525 CLDN9 0.0599270027261919 0.717485475139604 0.222587522134204 claudin 9 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity (By similarity). May act as a coreceptor for HCV entry into hepatic cells. {ECO:0000250, ECO:0000269|PubMed:17804490}.; . TISSUE SPECIFICITY: Expressed in the liver, in peripheral blood mononuclear cells and hepatocarcinoma cell lines. {ECO:0000269|PubMed:17804490}.; . . 0.20808 . -0.824740496 11.67728238 27.50846 0.88591 CLDN10 0.0459304128904221 0.853385927202268 0.100683659907309 claudin 10 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. May form permselective paracellular pores; isoform 1 appears to create pores preferentially permeable to cations and isoform 2 for anions. Plays a key role in controlling cation selectivity and transport in the thick ascending limb (TAL) of Henle's loop in kidney. {ECO:0000269|PubMed:19383724}.; . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;frontal lobe;oesophagus;endometrium;bone;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);tongue;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;stomach; amygdala;whole brain;dorsal root ganglion;superior cervical ganglion;occipital lobe;salivary gland;pons;atrioventricular node;skin;skeletal muscle;trachea;globus pallidus;kidney;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.44377 0.15317 -0.516085732 21.20193442 6.90664 0.25705 CLDN10-AS1 . . . CLDN10 antisense RNA 1 . . . . . . . . . . . CLDN11 0.32891224511477 0.607468263621729 0.0636194912635012 claudin 11 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;hypothalamus;pineal body;colon;parathyroid;skeletal muscle;pancreas;lung;cochlea;cerebral cortex;placenta;thyroid;bone;testis;head and neck;brain;pineal gland; superior cervical ganglion; 0.17823 0.26924 -0.185391282 39.67916962 7.37992 0.27452 CLDN12 0.10092139715214 0.772858009400862 0.126220593446998 claudin 12 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;cochlea;endometrium;thyroid;brain;bladder;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;skeletal muscle;pancreas;lung;cornea;adrenal gland;visual apparatus;hippocampus;hypopharynx;liver;head and neck;kidney;mammary gland;stomach; . 0.54795 0.12378 -0.029247611 51.40363293 12.63249 0.46108 CLDN14 0.000330686692861074 0.367613779598283 0.632055533708855 claudin 14 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}.; . TISSUE SPECIFICITY: Liver, kidney. Also found in ear.; unclassifiable (Anatomical System);pancreas;liver;spleen;kidney; superior cervical ganglion;liver;trigeminal ganglion;skeletal muscle; 0.13752 0.12776 -0.602450568 17.91106393 306.88054 3.72875 CLDN15 0.889708635311524 0.109140620100363 0.00115074458811345 claudin 15 FUNCTION: Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members function as impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN15 forms tight junctions that mediate the paracellular transport of small monovalent cations along a concentration gradient, due to selective permeability for Na(+), Li(+) and K(+) ions, but selects against Cl(-) ions. Plays an important role in paracellular Na(+) transport in the intestine and in Na(+) homeostasis. Required for normal Na(+)-dependent intestinal nutrient uptake. {ECO:0000269|PubMed:12055082, ECO:0000269|PubMed:13129853}.; . TISSUE SPECIFICITY: Detected in colon (at protein level). {ECO:0000269|PubMed:12055082}.; colon;choroid;fovea centralis;bone marrow;retina;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;blood;lens;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach;thymus; liver;trigeminal ganglion; 0.11402 0.13988 -0.339715008 30.06605331 16.69619 0.58786 CLDN16 0.0333869032212615 0.927194677234571 0.0394184195441673 claudin 16 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors.; . TISSUE SPECIFICITY: Kidney-specific, including the thick ascending limb of Henle (TAL).; unclassifiable (Anatomical System);ovary;liver;colon;spleen;kidney;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.25918 0.19409 -0.137658575 43.57159707 1015.55051 6.13170 CLDN17 0.000147441730490406 0.423637859817474 0.576214698452035 claudin 17 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}.; . . . . 0.04282 0.10084 0.483275131 79.25218212 1505.00273 7.21132 CLDN18 0.0126449337520513 0.856403128064739 0.13095193818321 claudin 18 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}.; . TISSUE SPECIFICITY: Concentrated at the cell-cell borders of epithelial cells.; unclassifiable (Anatomical System);pancreas;lung;cartilage;cerebral cortex;pituitary gland;testis;brain;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;fetal lung;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.14802 0.12758 0.440999548 77.79547063 607.65659 4.98653 CLDN19 0.175565901482529 0.768257069030034 0.0561770294874372 claudin 19 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}.; DISEASE: Hypomagnesemia 5 (HOMG5) [MIM:248190]: A progressive renal disease characterized by primary renal magnesium wasting with hypomagnesemia, hypercalciuria and nephrocalcinosis associated with severe ocular abnormalities such as bilateral chorioretinal scars, macular colobomata, significant myopia and nystagmus. The renal phenotype is virtually undistinguishable from that of patients with HOMG3. {ECO:0000269|PubMed:17033971}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . optic nerve;cerebral cortex;placenta;macula lutea;fovea centralis;choroid;kidney;lens;retina; dorsal root ganglion;superior cervical ganglion; 0.17672 0.14229 0.681699246 84.93158764 174.5966 2.87433 CLDN20 0.000765369094942534 0.321876941968657 0.6773576889364 claudin 20 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}.; . . . . 0.08837 0.10939 0.41713504 76.95800896 132.09393 2.50208 CLDN22 0.000437370884697617 0.418707287519474 0.580855341595829 claudin 22 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}.; . . bile duct; . . 0.08501 0.325313577 73.11276244 87.27496 1.99517 CLDN23 2.46842024128337e-05 0.171474242707298 0.828501073090289 claudin 23 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in germinal center B-cells, placenta, stomach as well as in colon tumor. {ECO:0000269|PubMed:12736707}.; . . . . . . 2834.13754 10.05317 CLDN24 0.000259988316035725 0.327244499474073 0.672495512209891 claudin 24 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}.; . . . . . . . . 954.81503 5.98301 CLDN25 2.36412438667322e-09 0.0108741727128296 0.989125824923046 claudin 25 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}.; . . . . . . -0.095386216 46.48502005 29.94995 0.95646 CLDN34 . . . claudin 34 FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250|UniProtKB:O88552}.; . . . . . . . . . . CLDND1 0.590515429063808 0.407385134678588 0.002099436257604 claudin domain containing 1 . . TISSUE SPECIFICITY: Widely distributed in the adult CNS with highest expression in the corpus callosum, caudate nucleus, cerebral cortex, medulla, putamen, spinal cord, substantia nigra and subthalamic nucleus. Weak expression was detected in the adult heart.; ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;hypothalamus;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.64126 . -0.426079032 25.36565228 13.87586 0.50426 CLDND2 3.86931508471866e-05 0.218228256079157 0.781733050769996 claudin domain containing 2 . . . unclassifiable (Anatomical System);lung;thyroid;testis; testis - interstitial;superior cervical ganglion;testis;globus pallidus; 0.24518 . 0.793752871 87.40268931 639.35017 5.08565 CLEC1A 2.08332477642767e-10 0.0185270941434097 0.981472905648258 C-type lectin domain family 1 member A . . TISSUE SPECIFICITY: Expressed preferentially in dendritic cells. {ECO:0000269|PubMed:10671229}.; unclassifiable (Anatomical System);uterus;lung;whole body;placenta;liver;spleen;kidney;spinal ganglion; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05805 0.07539 0.527368849 80.73248408 91.70012 2.05962 CLEC1B 0.00010417075731215 0.58262756266004 0.417268266582648 C-type lectin domain family 1 member B . . TISSUE SPECIFICITY: Expressed preferentially in the liver. Also expressed in immune cells of myeloid origin and on the surface of platelets. {ECO:0000269|PubMed:10671229, ECO:0000269|PubMed:16174766, ECO:0000269|PubMed:16940507}.; unclassifiable (Anatomical System);lung;liver;testis;spleen; fetal liver;appendix; 0.09796 0.09898 0.68351529 85.03774475 821.7982 5.62808 CLEC2A . . . C-type lectin domain family 2 member A FUNCTION: Plays a role in modulating the extent of T-cell expansion. Enhances the expansion of TCR-stimulated T-cells by increasing their survival through enhanced expression of anti- apoptotic proteins. May modulate the capacity of T-cells to home to lymph nodes through SELL. Facilitates dedicated immune recognition of keratinocytes via interaction with its receptor KLRF2 by stimulating natural killer cell mediated cytotoxicity. {ECO:0000269|PubMed:18550855, ECO:0000269|PubMed:20194751}.; . TISSUE SPECIFICITY: Mainly expressed in skin. Also expressed in keratinocytes, spleen, thymus, small intestine, peripheral blood monocytes, bone marrow, ovary, testis and skin. High expression in CD8(+), B-lymphocytes and naive CD4(+) T-cells. Restricted mostly to proliferating lymphocytes. Not detected in myeloid leukocytes or natural killer (NK) cells. {ECO:0000269|PubMed:18046548, ECO:0000269|PubMed:18550855, ECO:0000269|PubMed:20194751}.; . . 0.07051 0.04643 1.747347614 96.64425572 269.64935 3.52305 CLEC2B 0.00273195547397739 0.79671172726969 0.200556317256332 C-type lectin domain family 2 member B . . TISSUE SPECIFICITY: Expressed preferentially in lymphoid tissues, and in most hematopoietic cell types.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;blood;skeletal muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach;peripheral nerve;thymus; white blood cells;whole blood; 0.06311 0.14802 0.169169615 65.33380514 22.3129 0.74895 CLEC2D 0.767944822366651 0.23028212841973 0.00177304921361851 C-type lectin domain family 2 member D FUNCTION: Receptor for KLRB1 that protects target cells against natural killer cell-mediated lysis. Inhibits osteoclast formation. Inhibits bone resorption. Modulates the release of interferon- gamma. Binds high molecular weight sulfated glycosaminoglycans. {ECO:0000269|PubMed:14753741, ECO:0000269|PubMed:15104121, ECO:0000269|PubMed:16339513}.; . TISSUE SPECIFICITY: Detected in peripheral blood leukocytes, osteoblasts, lymph node, thymus and spleen. Isoform 1, isoform 2 and isoform 4 are expressed in T- and B-lymphocytes, and at lower levels in NK cells. They are also expressed in B-cell lines and LPS-matured monocyte-derived dendritic cells. {ECO:0000269|PubMed:10541800, ECO:0000269|PubMed:20843815}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;pineal gland;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.08838 0.08692 0.859896574 88.62349611 452.07114 4.42274 CLEC2L 0.0175943800770233 0.719187261366232 0.263218358556744 C-type lectin domain family 2 member L . . . . . . . -0.163345027 41.24793583 81.19107 1.90747 CLEC3A 5.3221672233597e-07 0.130383584796644 0.869615882986633 C-type lectin domain family 3 member A FUNCTION: Promotes cell adhesion to laminin-332 and fibronectin.; . TISSUE SPECIFICITY: Restricted to cartilage and breast. Also expressed in breast cancers. {ECO:0000269|PubMed:19173304}.; breast;prostate;whole body;cartilage;bone;testis; . 0.21458 0.10398 0.595326758 82.66100495 627.36112 5.04857 CLEC3B 0.000380110335261023 0.392524218298358 0.607095671366381 C-type lectin domain family 3 member B FUNCTION: Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis.; . TISSUE SPECIFICITY: Found in plasma.; myocardium;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;macula lutea;spleen;kidney; . 0.32239 0.23190 0.058937498 58.26256192 3.96492 0.14656 CLEC4A 7.43752503067102e-07 0.282763430606549 0.717235825640948 C-type lectin domain family 4 member A FUNCTION: May be involved in regulating immune reactivity. May play a role in modulating dendritic cells (DC) differentiation and/or maturation. May be involved via its ITIM motif (immunoreceptor tyrosine-based inhibitory motifs) in the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation. {ECO:0000269|PubMed:10438934}.; . TISSUE SPECIFICITY: Expressed in dendritic cells, myeloid cells, B-cells and HL-60 cells (at protein level). TNF alpha, IL-1 alpha, and LPS, down-regulated expression at the surface of neutrophils (at protein level). Expressed preferentially in hematopoietic tissues. Expressed in peripheral blood leukocytes, neutrophils, moderate quantities in spleen, lymph node, and bone marrow, and at very low levels in thymus. Expressed in Ag-presenting cells (DC, monocytes, macrophages and B-cells), as well as on granulocytes. Expression was decreased in DC by signals inducing its maturation (e.g. CD40 ligand, LPS, and TNF alpha). {ECO:0000269|PubMed:10438934, ECO:0000269|PubMed:11178971, ECO:0000269|PubMed:11994513}.; unclassifiable (Anatomical System);uterus;lung;whole body;cartilage;heart;nasopharynx;liver;testis;spleen;kidney;skin; superior cervical ganglion;atrioventricular node;whole blood;skeletal muscle; 0.02367 0.08097 0.705562627 85.52724699 71.33982 1.75814 CLEC4C 0.000999349230166641 0.94611442514167 0.0528862256281628 C-type lectin domain family 4 member C FUNCTION: Involved in antigen-capturing. Target ligand into antigen processing and peptide-loading compartments for presentation to T-cells. May mediate potent inhibition of induction of IFN-alpha/beta expression in plasmacytoid dendritic cells. May act as a signaling receptor that activates protein- tyrosine kinases and mobilizes intracellular calcium. Does not seem to bind mannose. {ECO:0000269|PubMed:11031109, ECO:0000269|PubMed:11748283}.; . TISSUE SPECIFICITY: Expressed in plasmacytoid dendritic cells (PDCs). Constitutively expressed in immature monocyte-derived dendritic cells (iMDDC) and is significantly down-regulated upon maturation with LPS but not with TNF-alpha. {ECO:0000269|PubMed:11031109, ECO:0000269|PubMed:11536172, ECO:0000269|PubMed:11748283}.; . . 0.06363 . 0.747842143 86.47676339 141.03042 2.59149 CLEC4D 0.000109415250448658 0.593359166114591 0.40653141863496 C-type lectin domain family 4 member D FUNCTION: Functions as an endocytic receptor. May be involved in antigen uptake at the site of infection, either for clearance of the antigen, or for processing and further presentation to T cells. {ECO:0000269|PubMed:14971047}.; . TISSUE SPECIFICITY: Expressed weakly in peripheral blood leukocytes, bone marrow and spleen. Expression is confined mostly in monocytes and macrophage and seems to be up-regulated by IL-6, IL-10, TNF-alpha and IFN-gamma. {ECO:0000269|PubMed:14971047}.; unclassifiable (Anatomical System);bone;colon;bone marrow; superior cervical ganglion; 0.04753 0.07066 0.350995466 74.37485256 789.62058 5.54370 CLEC4E 0.00355802800557527 0.840219747460856 0.156222224533568 C-type lectin domain family 4 member E FUNCTION: C-type lectin that functions as cell-surface receptor for a wide variety of ligands such as damaged cells, fungi and mycobacteria. Plays a role in the recognition of pathogenic fungi, such as Candida albicans. The detection of mycobacteria is via trehalose 6,6'-dimycolate (TDM), a cell wall glycolipid. Specifically recognizes alpha-mannose residues on pathogenic fungi of the genus Malassezia. Recognizes also SAP130, a nuclear protein, that is released by dead or dying cells. Transduces signals through an ITAM-containing adapter protein, Fc receptor gamma chain /FCER1G. Induces secretion of inflammatory cytokines through a pathway that depends on SYK, CARD9 and NF-kappa-B. {ECO:0000269|PubMed:18509109}.; . . unclassifiable (Anatomical System);lung;alveolus;colon;amniotic fluid;blood;kidney;brain;bone marrow; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.38794 . 0.082802743 60.09082331 44.54698 1.27716 CLEC4F 4.19038841935212e-12 0.0254695195720725 0.974530480423737 C-type lectin domain family 4 member F FUNCTION: Receptor with an affinity for galactose and fucose. Could be involved in endocytosis (By similarity). {ECO:0000250}.; . . optic nerve;cerebellum cortex;nasopharynx;macula lutea;fovea centralis;choroid;lens;skeletal muscle;retina; ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.05340 0.08548 3.138607529 99.2863883 3574.13101 11.56192 CLEC4G 0.00112276684554795 0.835520742282883 0.163356490871569 C-type lectin domain family 4 member G FUNCTION: Binds mannose, N-acetylglucosamine (GlcNAc) and fucose, but not galactose, in a Ca(2+)-dependent manner, in vitro. {ECO:0000269|PubMed:14711836}.; . TISSUE SPECIFICITY: Expressed exclusively in fetal and adult liver and in lymph nodes. Specifically expressed by endothelial cells lining lymph node and liver sinuses (at protein level). {ECO:0000269|PubMed:14711836}.; frontal lobe;islets of Langerhans;placenta;liver;spleen;brain; superior cervical ganglion;liver;ciliary ganglion;pons;atrioventricular node; 0.10805 0.10715 0.327131069 73.27199811 53.55037 1.45476 CLEC4GP1 . . . C-type lectin domain family 4 member G pseudogene 1 . . . . . . . . . . . CLEC4M 3.08704615217908e-05 0.79264582358443 0.207323305954049 C-type lectin domain family 4 member M FUNCTION: Probable pathogen-recognition receptor involved in peripheral immune surveillance in liver. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates. {ECO:0000269|PubMed:11257134}.; . TISSUE SPECIFICITY: Predominantly highly expressed in liver sinusoidal endothelial cells and in lymph node. Found in placental endothelium but not in macrophages. Expressed in type II alveolar cells and lung endothelial cells. {ECO:0000269|PubMed:11226297, ECO:0000269|PubMed:11257134, ECO:0000269|PubMed:15496474}.; unclassifiable (Anatomical System);medulla oblongata;cartilage;placenta;liver;testis;colon;spleen; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;lymph node;globus pallidus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.14511 . 0.066214104 58.95848077 360.36467 4.01743 CLEC5A 0.238602268127914 0.729517476238677 0.0318802556334084 C-type lectin domain family 5 member A FUNCTION: Functions as a positive regulator of osteoclastogenesis. Cell surface receptor that signals via TYROBP. Regulates inflammatory responses. Acts as a key regulator of synovial injury and bone erosion during autoimmune joint inflammation (By similarity). Critical macrophage receptor for dengue virus serotypes 1-4. {ECO:0000250, ECO:0000269|PubMed:10449773}.; . TISSUE SPECIFICITY: Expressed in peripheral blood monocytes and in the monocyte/macrophage cell lines U-937 and Mono-Mac-6, but not in cell lines of other origins. Expression is down-regulated when monocytes differentiate into dendritic cells. {ECO:0000269|PubMed:10449773}.; . . 0.09973 0.09481 0.215080721 67.91696155 56.35884 1.50816 CLEC6A 1.79122751588445e-06 0.250802130414543 0.749196078357941 C-type lectin domain family 6 member A FUNCTION: Binds high-mannose carbohydrates in a Ca(2+)-dependent manner. Functional receptor for alpha-mannans on C.albicans hypheas. Plays an important role in the host defense against C.albicans infection by inducing TH17 cell differentiation. Recognizes also, in a mannose-dependent manner, allergens from house dust mite and fungi, by promoting cysteinyl leukotriene production. Recognizes soluble elements from the eggs of Shistosoma mansoni altering adaptive immune responses. Transduces signals through an Fc receptor gamma chain /FCER1G and Syk-CARD9- NF-kappa-B-dependent pathway (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in lung, spleen, lymph node, leukocytes, bone marrow, tonsils and dendritic cells. Strongly expressed in purified monocytes and weakly in B-cells. In peripheral blood cells, preferentially expressed in plasmacytoids rather than myeloids. {ECO:0000269|PubMed:15175046, ECO:0000269|PubMed:15368084, ECO:0000269|PubMed:15810886}.; . . 0.02816 0.05964 0.948089677 89.95635763 257.11656 3.44921 CLEC7A 7.98974757902589e-08 0.0839309997481975 0.916068920354327 C-type lectin domain family 7 member A FUNCTION: Lectin that functions as pattern receptor specific for beta-1,3-linked and beta-1,6-linked glucans, such as cell wall constituents from pathogenic bacteria and fungi. Necessary for the TLR2-mediated inflammatory response and for TLR2-mediated activation of NF-kappa-B. Enhances cytokine production in macrophages and dendritic cells. Mediates production of reactive oxygen species in the cell. Mediates phagocytosis of C.albicans conidia. Binds T-cells in a way that does not involve their surface glycans and plays a role in T-cell activation. Stimulates T-cell proliferation (By similarity). {ECO:0000250, ECO:0000269|PubMed:11567029, ECO:0000269|PubMed:12423684, ECO:0000269|PubMed:17230442}.; DISEASE: Candidiasis, familial, 4 (CANDF4) [MIM:613108]: A primary immunodeficiency disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans. {ECO:0000269|PubMed:19864674}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in peripheral blood leukocytes and dendritic cells. Detected in spleen, bone marrow, lung, muscle, stomach and placenta. {ECO:0000269|PubMed:11470510, ECO:0000269|PubMed:11491532, ECO:0000269|PubMed:11567029, ECO:0000269|PubMed:11745369, ECO:0000269|PubMed:12423684}.; unclassifiable (Anatomical System);ovary;adrenal cortex;blood;parathyroid;skeletal muscle;bone marrow;whole body;adrenal gland;placenta;thyroid;pineal gland;brain;aorta; superior cervical ganglion;whole blood; 0.08049 0.14791 0.350995466 74.37485256 668.10269 5.16880 CLEC9A 2.45378474312192e-05 0.5109930648922 0.488982397260369 C-type lectin domain family 9 member A FUNCTION: Functions as an endocytic receptor on a small subset of myeloid cells specialized for the uptake and processing of material from dead cells. Recognizes filamentous form of actin in association with particular actin-binding domains of cytoskeletal proteins, including spectrin, exposed when cell membranes are damaged, and mediate the cross-presentation of dead-cell associated antigens in a Syk-dependent manner. {ECO:0000269|PubMed:18497879, ECO:0000269|PubMed:22483802}.; . TISSUE SPECIFICITY: In peripheral blood highly restricted on the surface of BDCA31(+) dendritic cells and on a small subset of CD14(+) and CD16(-) monocytes. {ECO:0000269|PubMed:18408006, ECO:0000269|PubMed:18497879}.; ovary;placenta;testis;parathyroid;kidney; . 0.07136 0.07653 1.038098315 91.20665251 24.23827 0.79670 CLEC10A 4.25495920863582e-08 0.203022745961051 0.796977211489357 C-type lectin domain family 10 member A FUNCTION: Probable role in regulating adaptive and innate immune responses. Binds in a calcium-dependent manner to terminal galactose and N-acetylgalactosamine units, linked to serine or threonine. These sugar moieties are known as Tn-Ag and are expressed in a variety of carcinoma cells. {ECO:0000269|PubMed:8598452}.; . . unclassifiable (Anatomical System);heart;ovary;skin;uterus;pancreas;lung;endometrium;bone;testis;spleen;mammary gland;brain; superior cervical ganglion;skeletal muscle; 0.05732 0.10980 1.218120595 93.15876386 329.25844 3.85744 CLEC11A 0.00226672639831053 0.762278372067351 0.235454901534339 C-type lectin domain family 11 member A FUNCTION: Stimulates the proliferation and differentiation of hematopoietic precursor cells from various lineages, including erythrocytes, lymphocytes, granulocytes and macrophages. Acts synergistically with other cytokines, including IL-3, GCSF, GMCSF and FLT3 ligand. Suppresses SCF-stimulated erythrocyte proliferation. {ECO:0000269|PubMed:11920266}.; . TISSUE SPECIFICITY: Expressed in skeletal tissues including bone marrow, chondrocytes, primary ossification center-associated cells, the perichondrium and periosteum. Lower levels of expression were detected in spleen, thymus, appendix and fetal liver. {ECO:0000269|PubMed:11803813, ECO:0000269|PubMed:11920266, ECO:0000269|PubMed:9442024, ECO:0000269|PubMed:9705843}.; ovary;colon;fovea centralis;choroid;retina;bone marrow;optic nerve;whole body;endometrium;larynx;bone;iris;testis;brain;unclassifiable (Anatomical System);cartilage;urinary;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;bone marrow; 0.25173 0.17253 . . 83.9445 1.95110 CLEC12A 6.28346136908363e-06 0.269863773051976 0.730129943486654 C-type lectin domain family 12 member A FUNCTION: Cell surface receptor that modulates signaling cascades and mediates tyrosine phosphorylation of target MAP kinases. {ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:16239426}.; . TISSUE SPECIFICITY: Detected in normal myeloid cells and in acute myeloid leukemia cells. Detected in neutrophils, eosinophils, monocytes and dendritic cells. Detected in spleen macrophage-rich red pulp and in lymph node (at protein level). Detected in peripheral blood leukocytes, dendritic cells, bone marrow, monocytes, mononuclear leukocytes and macrophages. {ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:15548716, ECO:0000269|PubMed:16239426, ECO:0000269|PubMed:16838277}.; unclassifiable (Anatomical System);pancreas;lung;cartilage;testis;spleen;blood;brain;bone marrow; . . 0.12795 0.194852702 67.03231894 28.5633 0.91514 CLEC12B 0.000124715849356653 0.622001495339659 0.377873788810985 C-type lectin domain family 12 member B FUNCTION: Cell surface receptor that protects target cells against natural killer cell-mediated lysis. Modulates signaling cascades and mediates tyrosine phosphorylation of target MAP kinases. {ECO:0000269|PubMed:17562706}.; . TISSUE SPECIFICITY: Detected in colon, heart, kidney, liver, lung, mammary gland, ovary, spleen and testis. {ECO:0000269|PubMed:17562706}.; unclassifiable (Anatomical System);lung;testis;skin; . . 0.12795 0.749657564 86.56522765 2999.32384 10.39200 CLEC14A 0.000668541235966075 0.7418838355024 0.257447623261634 C-type lectin domain family 14 member A . . . unclassifiable (Anatomical System);cartilage;heart;ovary;pineal body;colon;parathyroid;choroid;skin;skeletal muscle;retina;uterus;pancreas;lung;bone;placenta;liver;testis;spleen;kidney;spinal ganglion;brain;stomach; . 0.16795 . 0.330767508 73.53739089 66.51148 1.67996 CLEC16A 0.0101389568529136 0.989843481133116 1.75620139705563e-05 C-type lectin domain family 16 member A FUNCTION: Regulator of mitophagy through the upstream regulation of the RNF41/NRDP1-PARK2 pathway. Mitophagy is a selective form of autophagy necessary for mitochondrial quality control. The RNF41/NRDP1-PARK2 pathway regulates autophagosome-lysosome fusion during late mitophagy. May protect RNF41/NRDP1 from proteosomal degradation, RNF41/NRDP1 which regulates proteosomal degradation of PARK2. Plays a key role in beta cells functions by regulating mitophagy/autophagy and mitochondrial health. {ECO:0000269|PubMed:24949970}.; . TISSUE SPECIFICITY: Almost exclusively expressed in immune cells, including dendritic cells, B-lymphocytes and natural killer cells. {ECO:0000269|PubMed:17632545}.; lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; amygdala;testis;pons; 0.33524 0.17783 -1.010461444 8.197688134 250.55243 3.41106 CLEC17A 0.00261885555437633 0.982830690258726 0.0145504541868977 C-type lectin domain family 17 member A FUNCTION: Cell surface receptor which may be involved in carbohydrate-mediated communication between cells in the germinal center. Binds glycans with terminal alpha-linked mannose or fucose residues. {ECO:0000269|PubMed:19419970}.; . TISSUE SPECIFICITY: Expressed on dividing B-cells of germinal centers in various tissues, including lymph nodes, tonsils, stomach, intestine, appendix and spleen. {ECO:0000269|PubMed:19419970}.; unclassifiable (Anatomical System);uterus;blood; . . . 0.12689526 63.00424628 1162.7628 6.48959 CLEC18A 0.144113695415487 0.778785582302064 0.0771007222824487 C-type lectin domain family 18 member A FUNCTION: Binds polysaccharides in a Ca(2+)-independent manner with a preferentially binding to fucoidan, beta-glucans and galactans (PubMed:26170455). {ECO:0000269|PubMed:26170455}.; . TISSUE SPECIFICITY: Dectected in all cell lines tested and in peripheral blood cells. {ECO:0000269|PubMed:26170455}.; unclassifiable (Anatomical System);heart;cartilage;sympathetic chain;colon;choroid;optic nerve;lung;thyroid;bone;iris;testis;kidney;brain;stomach; . . . . . 3437.51904 11.25783 CLEC18B . . . C-type lectin domain family 18 member B FUNCTION: Binds polysaccharides in a Ca(2+)-independent manner (By similarity). {ECO:0000250|UniProtKB:A5D8T8}.; . . unclassifiable (Anatomical System);optic nerve;lung;cartilage;heart;bone;thyroid;sympathetic chain;testis;choroid;kidney;brain; testis - seminiferous tubule;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion; . . . . 153.27971 2.70715 CLEC18C 0.876992461970907 0.121482474304615 0.00152506372447871 C-type lectin domain family 18 member C FUNCTION: Binds polysaccharidesin a Ca(2+)-independent manner with a preferentially binding to fucoidan, beta-glucans and galactans. {ECO:0000269|PubMed:26170455}.; . TISSUE SPECIFICITY: Detected in peripheral blood cells. {ECO:0000269|PubMed:26170455}.; unclassifiable (Anatomical System);lung;cartilage;bone;thyroid;sympathetic chain;testis;colon;choroid;kidney;lens;brain;stomach; . . . . . 165.82602 2.81704 CLEC19A . . . C-type lectin domain family 19 member A . . . . . . . . . 1672.58531 7.54766 CLECL1 1.65162875088135e-06 0.0703532680877831 0.929645080283466 C-type lectin like 1 FUNCTION: May function in mediating immune cell-cell interactions. May act as a T-cell costimulatory molecule, enhancing anti-CD3- induced proliferation. May play a role in the interaction of dendritic cells with T-cells and the cells of the adaptive immune response. {ECO:0000269|PubMed:12421943}.; . TISSUE SPECIFICITY: Expressed in spleen, lymph node, and tonsil. Lower expression in peripheral blood, bone marrow, and colon. No expression detected in thymus. Highly expressed in dendritic and B-cells. {ECO:0000269|PubMed:12421943}.; unclassifiable (Anatomical System);uterus;prostate;heart;blood;kidney;skin;aorta; . 0.04659 . 0.61555716 83.13871196 53.67068 1.45973 CLGN 2.8539583939315e-07 0.916559811620422 0.0834399029837384 calmegin FUNCTION: Functions during spermatogenesis as a chaperone for a range of client proteins that are important for sperm adhesion onto the egg zona pellucida and for subsequent penetration of the zona pellucida. Required for normal sperm migration from the uterus into the oviduct. Required for normal male fertility. Binds calcium ions (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in testis (at protein level). Detected in testis. {ECO:0000269|PubMed:9434179}.; unclassifiable (Anatomical System);myocardium;medulla oblongata;islets of Langerhans;hypothalamus;pineal body;adrenal cortex;blood;fovea centralis;choroid;lens;retina;prostate;optic nerve;whole body;lung;endometrium;nasopharynx;macula lutea;liver;testis;germinal center;brain; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.15991 0.13130 0.556689353 81.63481953 1936.85001 8.09739 CLHC1 4.15102363149147e-15 0.0115379295880478 0.988462070411948 clathrin heavy chain linker domain containing 1 . . . . . 0.09581 . 1.157431179 92.60438783 4339.61671 13.11776 CLIC1 0.0124562134918973 0.854468770652761 0.133075015855342 chloride intracellular channel 1 FUNCTION: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle. {ECO:0000269|PubMed:10834939, ECO:0000269|PubMed:11195932, ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11940526, ECO:0000269|PubMed:11978800, ECO:0000269|PubMed:14613939, ECO:0000269|PubMed:9139710}.; . TISSUE SPECIFICITY: Expression is prominent in heart, placenta, liver, kidney and pancreas. {ECO:0000269|PubMed:10793131}.; . . 0.48732 . -0.141298762 42.87567823 229.46258 3.27348 CLIC1P1 . . . chloride intracellular channel 1 pseudogene 1 . . . . . . . . . . . CLIC2 0.493262623526124 0.486080648463231 0.0206567280106446 chloride intracellular channel 2 FUNCTION: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Modulates the activity of RYR2 and inhibits calcium influx. {ECO:0000269|PubMed:15147738, ECO:0000269|PubMed:15916532, ECO:0000269|PubMed:17945253}.; DISEASE: Mental retardation, X-linked, syndromic, 32 (MRXS32) [MIM:300886]: A mental retardation syndrome characterized by profound intellectual deficit, delayed psychomotor development beginning in infancy and little or no speech development. Additional features include seizures, large joint contractures, and abnormal positioning of the thumbs. Mental retardation is defined by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:22814392}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in adult and fetal brain, heart, skeletal muscle, liver, lung, and spleen. Detected in adult stomach and testis. Expressed in fetal thymus and kidney. {ECO:0000269|PubMed:15147738, ECO:0000269|PubMed:22814392}.; unclassifiable (Anatomical System);whole body;ovary;placenta;spinal cord;colon;parathyroid;lens; superior cervical ganglion;thyroid;skeletal muscle; 0.22626 0.13985 0.191216164 66.57230479 13.42332 0.48858 CLIC3 0.000387773349058043 0.396183145415676 0.603429081235266 chloride intracellular channel 3 FUNCTION: Can insert into membranes and form chloride ion channels. May participate in cellular growth control. {ECO:0000269|PubMed:9880541}.; . TISSUE SPECIFICITY: Detected in placenta (at protein level). Widely expressed. High expression is found in placenta followed by lung and heart. Low expression in skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:17027078, ECO:0000269|PubMed:9880541}.; . . 0.48825 0.10951 0.038710339 56.92380278 226.43026 3.25136 CLIC4 0.00946200366501209 0.814697870219437 0.175840126115551 chloride intracellular channel 4 FUNCTION: Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Promotes cell- surface expression of HRH3. Has alternate cellular functions like a potential role in angiogenesis or in maintaining apical- basolateral membrane polarity during mitosis and cytokinesis. Could also promote endothelial cell proliferation and regulate endothelial morphogenesis (tubulogenesis). {ECO:0000269|PubMed:12163372, ECO:0000269|PubMed:14569596, ECO:0000269|PubMed:16176272, ECO:0000269|PubMed:16239224, ECO:0000269|PubMed:18302930, ECO:0000269|PubMed:19247789}.; . TISSUE SPECIFICITY: Detected in epithelial cells from colon, esophagus and kidney (at protein level). Expression is prominent in heart, kidney, placenta and skeletal muscle. {ECO:0000269|PubMed:10793131, ECO:0000269|PubMed:17200346, ECO:0000269|PubMed:17636002}.; . . 0.50248 0.10939 -0.229483771 36.86010852 6.95629 0.25893 CLIC4P1 . . . chloride intracellular channel 4 pseudogene 1 . . . . . . . . . . . CLIC4P2 . . . chloride intracellular channel 4 pseudogene 2 . . . . . . . . . . . CLIC4P3 . . . chloride intracellular channel 4 pseudogene 3 . . . . . . . . . . . CLIC5 0.00187685115916181 0.724933929762025 0.273189219078813 chloride intracellular channel 5 FUNCTION: Required for normal hearing (PubMed:24781754). It is necessary for the formation of stereocilia in the inner ear and normal development of the organ of Corti (By similarity). Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. May play a role in the regulation of transepithelial ion absorption and secretion. Is required for the development and/or maintenance of the proper glomerular endothelial cell and podocyte architecture (PubMed:15184393, PubMed:18028448, PubMed:20335315). {ECO:0000250|UniProtKB:Q8BXK9, ECO:0000269|PubMed:15184393, ECO:0000269|PubMed:18028448, ECO:0000269|PubMed:20335315, ECO:0000269|PubMed:24781754}.; DISEASE: Deafness, autosomal recessive, 103 (DFNB103) [MIM:616042]: A form of sensorineural deafness with onset in early childhood. Hearing impairment progresses from mild to severe or even profound before the second decade, and is accompanied by vestibular areflexia. {ECO:0000269|PubMed:24781754}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed in both fetal and adult human tissues (PubMed:24781754). Isoform 1 is expressed in renal glomeruli endothelial cells and podocytes (at protein level). {ECO:0000269|PubMed:20335315, ECO:0000269|PubMed:24781754}.; unclassifiable (Anatomical System);ovary;spinal cord;colon;fovea centralis;choroid;lens;retina;uterus;lung;optic nerve;whole body;placenta;macula lutea;liver;testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;kidney;trigeminal ganglion;skeletal muscle; 0.25637 0.09418 1.019682101 90.97664544 213.77513 3.15479 CLIC6 0.00053522352566409 0.696090065294311 0.303374711180025 chloride intracellular channel 6 FUNCTION: May insert into membranes and form chloride ion channels. May play a critical role in water-secreting cells, possibly through the regulation of chloride ion transport (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, placenta, pancreas and liver. {ECO:0000269|PubMed:12226712}.; unclassifiable (Anatomical System);cartilage;colon;blood;fovea centralis;choroid;lens;retina;uterus;breast;prostate;optic nerve;lung;endometrium;bone;thyroid;macula lutea;testis;head and neck;spleen;kidney;spinal ganglion;brain;stomach; . 0.08923 0.13138 1.019682101 90.97664544 3444.27872 11.27567 CLINT1 0.800888476219691 0.199101821039234 9.70274107489788e-06 clathrin interactor 1 FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly. {ECO:0000269|PubMed:12429846, ECO:0000269|PubMed:12538641}.; . TISSUE SPECIFICITY: Ubiquitously expressed at low to intermediate levels. {ECO:0000269|PubMed:12429846, ECO:0000269|PubMed:12538641}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; subthalamic nucleus;fetal liver;superior cervical ganglion;trachea;thyroid;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.66779 0.13728 -0.291981272 33.20358575 40.87237 1.19744 CLIP1 0.96849601373118 0.0315039861300243 1.3879534636548e-10 CAP-Gly domain containing linker protein 1 FUNCTION: Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. {ECO:0000269|PubMed:12433698, ECO:0000269|PubMed:17563362, ECO:0000269|PubMed:17889670}.; . TISSUE SPECIFICITY: Detected in dendritic cells (at protein level). Highly expressed in the Reed-Sternberg cells of Hodgkin disease. {ECO:0000269|PubMed:12433698, ECO:0000269|PubMed:1600942}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;atrium;endometrium;larynx;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;epidermis;tongue;islets of Langerhans;spinal cord;pharynx;blood;lens;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;aorta;stomach; amygdala;occipital lobe;superior cervical ganglion;placenta;thyroid;prefrontal cortex;ciliary ganglion;pons;skeletal muscle;cingulate cortex; 0.46737 0.32290 -1.098660656 6.95329087 8478.17859 19.85973 CLIP1-AS1 . . . CLIP1 antisense RNA 1 . . . . . . . . . . . CLIP2 0.999881647285659 0.00011835270252381 1.1816995575238e-11 CAP-Gly domain containing linker protein 2 FUNCTION: Seems to link microtubules to dendritic lamellar body (DLB), a membranous organelle predominantly present in bulbous dendritic appendages of neurons linked by dendrodendritic gap junctions. May operate in the control of brain-specific organelle translocations (By similarity). {ECO:0000250}.; DISEASE: Note=CLIP2 is located in the Williams-Beuren syndrome (WBS) critical region (PubMed:9799601). WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of CLIP2 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease. However, it has been demonstrated that haploinsufficiency of this gene alone is not sufficient to cause any of the cognitive or facial features of WBS (PubMed:22608712). {ECO:0000305|PubMed:22608712, ECO:0000305|PubMed:9799601}.; . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;endometrium;bone;thyroid;testis;germinal center;brain;bladder;amygdala;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;amnion;spleen;kidney;mammary gland;stomach;thymus; prefrontal cortex; 0.13125 . -1.186862251 5.90351498 632.85889 5.06850 CLIP3 0.99856772100268 0.0014322535961971 2.54011225398221e-08 CAP-Gly domain containing linker protein 3 FUNCTION: Functions as a cytoplasmic linker protein. Involved in TGN-endosome dynamics. May modulate the cellular compartmentalization of AKT kinase family and promote its cell membrane localization, thereby playing a role in glucose transport in adipocytes. {ECO:0000269|PubMed:19139280}.; . . ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;breast;lung;placenta;macula lutea;hippocampus;visual apparatus;kidney;mammary gland;cerebellum; whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.30836 0.11719 -0.736552314 13.93606983 16.50621 0.58405 CLIP4 0.000288887942474729 0.996755346540456 0.00295576551706962 CAP-Gly domain containing linker protein family member 4 . . . smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;larynx;pituitary gland;testis;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;cartilage;tongue;islets of Langerhans;hypothalamus;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney; testis - interstitial;subthalamic nucleus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.17101 0.10331 -0.198338176 39.17197452 134.02736 2.51831 CLK1 0.0953474554277548 0.904315958035315 0.000336586536930449 CDC like kinase 1 FUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates: SRSF1, SRSF3 and PTPN1. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells and adenovirus E1A pre-mRNA. {ECO:0000269|PubMed:10480872, ECO:0000269|PubMed:19168442}.; . TISSUE SPECIFICITY: Endothelial cells. {ECO:0000269|PubMed:19168442}.; smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;gall bladder;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;small intestine;islets of Langerhans;hypothalamus;pancreas;pia mater;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; prefrontal cortex; 0.50063 0.15400 -0.337894035 30.37272942 64.6035 1.64868 CLK2 0.999952949082341 4.70509164095218e-05 1.24923739262342e-12 CDC like kinase 2 FUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. {ECO:0000269|PubMed:10480872, ECO:0000269|PubMed:19168442, ECO:0000269|PubMed:8910305, ECO:0000269|PubMed:9637771}.; . TISSUE SPECIFICITY: Endothelial cells. {ECO:0000269|PubMed:19168442}.; medulla oblongata;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);heart;lacrimal gland;tongue;islets of Langerhans;muscle;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; . 0.34978 0.14525 -0.402212257 26.7338995 48.00741 1.34624 CLK2P1 . . . CDC like kinase 2, pseudogene 1 . . . . . . . . . . . CLK3 0.928146533223461 0.0718528109892685 6.55787270108671e-07 CDC like kinase 3 FUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. {ECO:0000269|PubMed:19168442, ECO:0000269|PubMed:9637771}.; . TISSUE SPECIFICITY: Endothelial cells. {ECO:0000269|PubMed:19168442}.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pineal body;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;skeletal muscle; 0.20278 0.10945 -0.670411825 15.61689078 2284.8936 8.84444 CLK3P1 . . . CDC like kinase 3 pseudogene 1 . . . . . . . . . . . CLK3P2 . . . CDC like kinase 3 pseudogene 2 . . . . . . . . . . . CLK4 0.449835920959239 0.550110647200107 5.34318406539734e-05 CDC like kinase 4 FUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates SRSF1 and SRSF3. Required for the regulation of alternative splicing of MAPT/TAU. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. {ECO:0000269|PubMed:11170754, ECO:0000269|PubMed:19168442}.; . TISSUE SPECIFICITY: Expressed in liver, kidney, heart, muscle, brain and endothelial cells. {ECO:0000269|PubMed:11170754, ECO:0000269|PubMed:19168442}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;germinal center;brain;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;lung;trabecular meshwork;placenta;macula lutea;alveolus;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;atrioventricular node;pons;trigeminal ganglion; 0.20117 0.10400 -0.047654689 50.22410946 37.88937 1.12491 CLLU1 0.0413682841967756 0.655043533399558 0.303588182403666 chronic lymphocytic leukemia up-regulated 1 . . TISSUE SPECIFICITY: Specifically expressed in chronic lymphocytic leukemia (CLL) cells from patients without immunoglobulin heavy- chain hypermutations. Expression is detected in all CLL cells and levels are similar in patients before and after treatment. {ECO:0000269|PubMed:16339396, ECO:0000269|PubMed:17284524, ECO:0000269|PubMed:19212335}.; . . 0.10079 . . . 328.75219 3.85475 CLLU1OS 0.0527318795262529 0.697549711387225 0.249718409086522 chronic lymphocytic leukemia up-regulated 1 opposite strand . . . . . 0.14943 . -0.009020804 52.8544468 3.27787 0.11886 CLMN 2.06352661935763e-07 0.993378889546731 0.00662090410060659 calmin (calponin-like, transmembrane) . . TISSUE SPECIFICITY: Widely expressed at intermediate level. {ECO:0000269|PubMed:10574461}.; lymphoreticular;ovary;sympathetic chain;colon;fovea centralis;skin;retina;prostate;whole body;oesophagus;cerebral cortex;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;muscle;blood;breast;lung;placenta;macula lutea;hippocampus;visual apparatus;liver;spleen;mammary gland;stomach; testis - interstitial;thalamus;testis - seminiferous tubule;hypothalamus;testis;kidney; 0.16522 0.08725 -0.74406331 13.77683416 269.98491 3.52505 CLMP 3.02178689371524e-05 0.935245330634424 0.0647244514966391 CXADR-like membrane protein FUNCTION: May be involved in the cell-cell adhesion. May play a role in adipocyte differentiation and development of obesity. Is required for normal small intestine development. {ECO:0000269|PubMed:14573622, ECO:0000269|PubMed:15563274, ECO:0000269|PubMed:22155368}.; DISEASE: Congenital short bowel syndrome (CSBS) [MIM:615237]: A disease characterized by a shortened small intestine, intestinal malrotation, and malabsorption. The mean length of the small intestine in CSBS patients is approximately 50 cm, compared with a normal length at birth of 190-280 cm. Patients with CSBS may develop severe malnutrition as a result of the hugely reduced absorptive surface of the small intestine. Infants require parenteral nutrition for survival. However, parenteral nutrition itself causes life-threatening complications such as sepsis and liver failure which are associated with a high rate of mortality early in life. {ECO:0000269|PubMed:22155368}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in epithelial cells within different tissues and in the white adipose tissue. Expressed at high levels in small intestine and placenta, at intermediate levels in the heart, skeletal muscle, colon, spleen, kidney and lung and at low levels in the liver and peripheral blood leukocytes. Highly abundant in the intestine during embryo and fetal development (at protein level). {ECO:0000269|PubMed:14573622, ECO:0000269|PubMed:15563274, ECO:0000269|PubMed:22155368}.; . . . . 0.040529541 57.15380986 260.50672 3.46694 CLN3 9.99316042821659e-07 0.775582044252699 0.224416956431258 ceroid-lipofuscinosis, neuronal 3 FUNCTION: Involved in microtubule-dependent, anterograde transport of late endosomes and lysosomes. {ECO:0000269|PubMed:22261744}.; DISEASE: Ceroid lipofuscinosis, neuronal, 3 (CLN3) [MIM:204200]: A form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The hallmark of CLN3 is the ultrastructural pattern of lipopigment with a fingerprint profile, which can have 3 different appearances: pure within a lysosomal residual body; in conjunction with curvilinear or rectilinear profiles; and as a small component within large membrane-bound lysosomal vacuoles. The combination of fingerprint profiles within lysosomal vacuoles is a regular feature of blood lymphocytes from patients with neuronal ceroid lipofuscinosis type 3. {ECO:0000269|PubMed:21990111, ECO:0000269|PubMed:9311735, ECO:0000269|PubMed:9490299}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;whole body;optic nerve;oesophagus;endometrium;bone;iris;pituitary gland;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;cerebellum cortex;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;placenta;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion; 0.37571 0.28449 -0.156065314 42.16206653 1769.25898 7.77042 CLN5 5.08087125944432e-06 0.418022085459388 0.581972833669352 ceroid-lipofuscinosis, neuronal 5 . DISEASE: Ceroid lipofuscinosis, neuronal, 5 (CLN5) [MIM:256731]: A form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment patterns observed most often in neuronal ceroid lipofuscinosis type 5 comprise mixed combinations of granular, curvilinear, and fingerprint profiles. {ECO:0000269|PubMed:15728307, ECO:0000269|PubMed:16814585, ECO:0000269|PubMed:17607606, ECO:0000269|PubMed:19309691, ECO:0000269|PubMed:21990111, ECO:0000269|PubMed:9662406}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; . . 0.09426 0.16580 0.062575634 58.74026893 2513.68519 9.33961 CLN6 0.381706051281562 0.607880968253419 0.0104129804650191 ceroid-lipofuscinosis, neuronal 6, late infantile, variant . DISEASE: Ceroid lipofuscinosis, neuronal, 6 (CLN6) [MIM:601780]: A form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment patterns observed most often in neuronal ceroid lipofuscinosis type 6 comprise mixed combinations of granular, curvilinear, and fingerprint profiles. {ECO:0000269|PubMed:11727201, ECO:0000269|PubMed:11791207, ECO:0000269|PubMed:12673792, ECO:0000269|PubMed:12815591, ECO:0000269|PubMed:19201763, ECO:0000269|PubMed:21990111, ECO:0000269|Ref.2}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ceroid lipofuscinosis, neuronal, 4A (CLN4A) [MIM:204300]: An adult-onset neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. CLN4A has no visual involvement and is characterized by progressive myoclonic epilepsy. {ECO:0000269|PubMed:21549341}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;choroid;skin;retina;bone marrow;uterus;larynx;bone;testis;germinal center;brain;bladder;pineal gland;tonsil;unclassifiable (Anatomical System);cartilage;heart;urinary;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach; kidney;parietal lobe;cingulate cortex; 0.21720 0.20490 -0.069700724 48.54328851 69.55835 1.73093 CLN8 0.000747073250102511 0.527210631300883 0.472042295449014 ceroid-lipofuscinosis, neuronal 8 FUNCTION: Could play a role in cell proliferation during neuronal differentiation and in protection against cell death. {ECO:0000269|PubMed:19431184}.; DISEASE: Ceroid lipofuscinosis, neuronal, 8 (CLN8) [MIM:600143]: A form of neuronal ceroid lipofuscinosis with onset in childhood. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment patterns observed most often in neuronal ceroid lipofuscinosis type 8 comprise mixed combinations of granular, curvilinear, and fingerprint profiles. {ECO:0000269|PubMed:15024724, ECO:0000269|PubMed:16570191, ECO:0000269|PubMed:19201763, ECO:0000269|PubMed:19431184, ECO:0000269|PubMed:21990111}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ceroid lipofuscinosis, neuronal, 8, Northern epilepsy variant (CLN8NE) [MIM:610003]: A form of neuronal ceroid lipofuscinosis clinically characterized by epilepsy that presents between 5 and 10 years of age with frequent tonic-clonic seizures followed by progressive mental retardation. Visual loss is not a prominent feature. Intracellular accumulation of autofluorescent material results in curvilinear and granular profiles on ultrastructural analysis. {ECO:0000269|PubMed:10508524, ECO:0000269|PubMed:21990111}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;skin;uterus;prostate;frontal lobe;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;hypothalamus;blood;skeletal muscle;pancreas;lung;epididymis;placenta;liver;hypopharynx;amnion;spleen;head and neck;kidney;stomach; amygdala;superior cervical ganglion;caudate nucleus;atrioventricular node; 0.13188 . -0.135838822 43.77211607 83.44763 1.94310 CLN9 . . . ceroid-lipofuscinosis, neuronal 9 . . . . . . . . . . . CLNK 1.34591221879556e-20 9.29061266491921e-05 0.999907093873351 cytokine dependent hematopoietic cell linker FUNCTION: Plays a role in the regulation of immunoreceptor signaling, including PLC-gamma-mediated B-cell antigen receptor (BCR) signaling and FC-epsilon R1-mediated mast cell degranulation. Involved in phosphorylation of LAT (By similarity). {ECO:0000250}.; . . kidney; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; . 0.10284 0.688969636 85.20877565 274.38096 3.54911 CLNS1A 0.0950296158150142 0.86802374115813 0.0369466430268552 chloride nucleotide-sensitive channel 1A FUNCTION: Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. May also indirectly participate in cellular volume control by activation of a swelling-induced chloride conductance pathway. {ECO:0000269|PubMed:10330151, ECO:0000269|PubMed:11713266, ECO:0000269|PubMed:18984161}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;head and neck;kidney;mammary gland;stomach;thymus; tumor;trigeminal ganglion; 0.10581 0.20350 -0.229483771 36.86010852 18.65228 0.64467 CLNS1AP1 . . . chloride nucleotide-sensitive channel 1A pseudogene 1 . . . . . . . . . . . CLOCK 0.998479650515238 0.00152034943551089 4.92513747630222e-11 clock circadian regulator FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time- keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. CLOCK has an intrinsic acetyltransferase activity, which enables circadian chromatin remodeling by acetylating histones and nonhistone proteins, including its own partner ARNTL/BMAL1. Regulates the circadian expression of ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of the transactivation potential of NF-kappaB. Plays an important role in the homeostatic regulation of sleep. The CLOCK- ARNTL/BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The CLOCK-ARNTL2/BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. {ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:18587630, ECO:0000269|PubMed:21659603, ECO:0000269|PubMed:21980503, ECO:0000269|PubMed:22284746, ECO:0000269|PubMed:23785138, ECO:0000269|PubMed:24005054}.; . TISSUE SPECIFICITY: Hair follicles (at protein level). Expressed in all tissues examined including spleen, thymus, prostate, testis, ovary, small intestine, colon, leukocytes, heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Highest levels in testis and skeletal muscle. Low levels in thymus, lung and liver. Expressed in all brain regions with highest levels in cerebellum. Highly expressed in the suprachiasmatic nucleus (SCN). {ECO:0000269|PubMed:10198158, ECO:0000269|PubMed:24005054}.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;cochlea;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;blood;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;liver;alveolus;head and neck;kidney; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;cingulate cortex; 0.45361 0.24055 -0.532670911 20.78320359 702.63417 5.27074 CLP1 0.937604668403125 0.0623401321795064 5.5199417368802e-05 cleavage and polyadenylation factor I subunit 1 FUNCTION: Polynucleotide kinase that can phosphorylate the 5'- hydroxyl groups of double-stranded RNA (dsRNA), single-stranded RNA (ssRNA), double-stranded DNA (dsDNA) and double-stranded DNA:RNA hybrids. dsRNA is phosphorylated more efficiently than dsDNA, and the RNA component of a DNA:RNA hybrid is phosphorylated more efficiently than the DNA component. Plays a key role in both tRNA splicing and mRNA 3'-end formation. Component of the tRNA splicing endonuclease complex: phosphorylates the 5'-terminus of the tRNA 3'-exon during tRNA splicing; this phosphorylation event is a prerequisite for the subsequent ligation of the two exon halves and the production of a mature tRNA (PubMed:24766809, PubMed:24766810). Its role in tRNA splicing and maturation is required for cerebellar development (PubMed:24766809, PubMed:24766810). Component of the pre-mRNA cleavage complex II (CF-II), which seems to be required for mRNA 3'-end formation. Also phosphorylates the 5'-terminus of exogenously introduced short interfering RNAs (siRNAs), which is a necessary prerequisite for their incorporation into the RNA-induced silencing complex (RISC). However, endogenous siRNAs and microRNAs (miRNAs) that are produced by the cleavage of dsRNA precursors by DICER1 already contain a 5'-phosphate group, so this protein may be dispensible for normal RNA-mediated gene silencing. {ECO:0000269|PubMed:17495927, ECO:0000269|PubMed:18648070, ECO:0000269|PubMed:24766809, ECO:0000269|PubMed:24766810}.; DISEASE: Pontocerebellar hypoplasia 10 (PCH10) [MIM:615803]: A form of pontocerebellar hypoplasia, a disorder characterized by structural defects of the pons and cerebellum, evident upon brain imaging. PCH10 features include cortical dysgenesis marked by a simplified gyral pattern, cortical atrophy, mild or focal cerebellar vermian volume loss, delayed myelination, progressive microcephaly, global growth and developmental delays, severe intellectual disabilities, and seizures refractory to treatment. {ECO:0000269|PubMed:24766809, ECO:0000269|PubMed:24766810}. Note=The disease is caused by mutations affecting the gene represented in this entry. Neurodegeneration is due to defects in tRNA splicing (PubMed:24766809, PubMed:24766810). {ECO:0000269|PubMed:24766809, ECO:0000269|PubMed:24766810}.; . umbilical cord;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;atrium;whole body;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;medulla oblongata;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15671 0.14229 -0.049474214 50.01179523 31.81705 1.00125 CLPB 9.1324224431567e-06 0.996502479793053 0.00348838778450343 ClpB homolog, mitochondrial AAA ATPase chaperonin FUNCTION: May function as a regulatory ATPase and be related to secretion/protein trafficking process.; . TISSUE SPECIFICITY: Widely expressed (at protein level) (PubMed:25597511). Expressed in fetal, as well as in adult tissues, with highest levels in adult brain, including thalamus, hippocampus, occipital cortex and parietal cortex. Low expression in granulocytes (PubMed:25597510). {ECO:0000269|PubMed:25597510, ECO:0000269|PubMed:25597511}.; medulla oblongata;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;thyroid;bone;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;tongue;muscle;adrenal cortex;pharynx;blood;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.13166 0.18562 0.248041348 69.61547535 379.68763 4.10911 CLPP 0.587942370870824 0.401952706403676 0.0101049227254997 caseinolytic mitochondrial matrix peptidase proteolytic subunit FUNCTION: Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. {ECO:0000269|PubMed:11923310, ECO:0000269|PubMed:15522782}.; . TISSUE SPECIFICITY: Detected in liver (at protein level). Predominantly expressed in skeletal muscle. Intermediate levels in heart, liver and pancreas. Low in brain, placenta, lung and kidney. {ECO:0000269|PubMed:10525407, ECO:0000269|PubMed:8543061}.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; prostate;lung;heart;liver;testis;tumor;kidney;skeletal muscle; 0.17566 0.36174 -0.339715008 30.06605331 3.65823 0.13532 CLPS 0.0562747598072514 0.707931989917256 0.235793250275492 colipase FUNCTION: Colipase is a cofactor of pancreatic lipase. It allows the lipase to anchor itself to the lipid-water interface. Without colipase the enzyme is washed off by bile salts, which have an inhibitory effect on the lipase.; . TISSUE SPECIFICITY: Expressed by the pancreas.; unclassifiable (Anatomical System);uterus;pancreas;lung;heart;islets of Langerhans;spleen;skin; dorsal root ganglion;fetal liver;pancreas;superior cervical ganglion;beta cell islets;ciliary ganglion;atrioventricular node; 0.38818 0.19714 0.481458261 79.03986789 232.33467 3.29571 CLPSL1 0.00164846548972643 0.460309051742351 0.538042482767923 colipase like 1 . . TISSUE SPECIFICITY: Exclusively expressed in epididymis, in the corpus region. {ECO:0000269|PubMed:18390568}.; . . . . 0.25917371 70.05779665 120.34733 2.39015 CLPSL2 0.146625366873331 0.630862007757947 0.222512625368723 colipase like 2 . . . . . 0.08842 . 0.323496558 72.93583392 933.22632 5.92441 CLPTM1 0.98048307691788 0.0195167978544676 1.25227652028054e-07 cleft lip and palate associated transmembrane protein 1 FUNCTION: May play a role in T-cell development. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9828125}.; lymphoreticular;smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;lens;bile duct;breast;pancreas;lung;placenta;visual apparatus;macula lutea;hippocampus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach; whole brain;amygdala;medulla oblongata;superior cervical ganglion;liver;prefrontal cortex;cingulate cortex;parietal lobe; 0.59598 0.12206 -1.151821487 6.269167256 84.24366 1.95423 CLPTM1L 0.311319339054671 0.688524082287194 0.000156578658135127 CLPTM1-like FUNCTION: Enhances cisplatin-mediated apoptosis, when overexpressed. {ECO:0000269|PubMed:11162647}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; liver; 0.22539 0.12562 -0.596992387 18.18825195 148.89252 2.66142 CLPTM1LP1 . . . CLPTM1L pseudogene 1 . . . . . . . . . . . CLPX 0.766826744088607 0.233170185622817 3.07028857568027e-06 caseinolytic mitochondrial matrix peptidase chaperone subunit FUNCTION: ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex (PubMed:11923310, PubMed:22710082). Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure (PubMed:22841477). ATP- dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis. Important for efficient erythropoiesis through upregulation of heme biosynthesis (PubMed:25957689). {ECO:0000269|PubMed:11923310, ECO:0000269|PubMed:22710082, ECO:0000269|PubMed:22841477, ECO:0000269|PubMed:25957689}.; . TISSUE SPECIFICITY: Higher expression in skeletal muscle and heart and to a lesser extent in liver, brain, placenta, lung, kidney and pancreas. {ECO:0000269|PubMed:11003706}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;pineal body;pharynx;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;aorta;stomach;peripheral nerve;thymus; superior cervical ganglion;testis - interstitial;globus pallidus;parietal lobe;skeletal muscle; 0.48574 0.20473 -0.246069119 36.06982779 48.09581 1.35048 CLRN1 0.000915821935109622 0.571048141832426 0.428036036232464 clarin 1 FUNCTION: May have a role in the excitatory ribbon synapse junctions between hair cells and cochlear ganglion cells and presumably also in analogous synapses within the retina. {ECO:0000269|PubMed:12080385}.; DISEASE: Retinitis pigmentosa 61 (RP61) [MIM:614180]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:21310491}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Found in the retina.; skeletal muscle; superior cervical ganglion;occipital lobe;atrioventricular node;skeletal muscle; 0.18168 0.14671 -0.60427181 17.74593064 19.82253 0.67595 CLRN1-AS1 . . . CLRN1 antisense RNA 1 . . . . . . . . . . . CLRN2 0.000289450029462047 0.562784908010542 0.436925641959996 clarin 2 . . . . . 0.14144 0.10174 -0.137658575 43.57159707 961.58325 6.00243 CLRN3 0.140040446356922 0.779451219520013 0.0805083341230658 clarin 3 . . . . . 0.04331 0.08843 0.617373774 83.25076669 511.59557 4.63051 CLSPN 0.991559393439728 0.00844060655484618 5.42531776728658e-12 claspin FUNCTION: Required for checkpoint mediated cell cycle arrest in response to inhibition of DNA replication or to DNA damage induced by both ionizing and UV irradiation. Adapter protein which binds to BRCA1 and the checkpoint kinase CHEK1 and facilitates the ATR- dependent phosphorylation of both proteins. Can also bind specifically to branched DNA structures and may associate with S- phase chromatin following formation of the pre-replication complex (pre-RC). This may indicate a role for this protein as a sensor which monitors the integrity of DNA replication forks. {ECO:0000269|PubMed:12766152, ECO:0000269|PubMed:15096610, ECO:0000269|PubMed:15190204, ECO:0000269|PubMed:15226314, ECO:0000269|PubMed:15707391}.; . . unclassifiable (Anatomical System);pharynx;colon;blood;skin;skeletal muscle;retina;uterus;breast;epididymis;visual apparatus;duodenum;liver;testis;germinal center;brain;bladder;stomach; . 0.45114 . 0.744001103 86.37650389 5854.71385 15.86316 CLSTN1 0.844214450133216 0.155785347243185 2.02623598916076e-07 calsyntenin 1 FUNCTION: Induces KLC1 association with vesicles and functions as a cargo in axonal anterograde transport. Complex formation with APBA2 and APP, stabilizes APP metabolism and enhances APBA2- mediated suppression of beta-APP40 secretion, due to the retardation of intracellular APP maturation. In complex with APBA2 and C99, a C-terminal APP fragment, abolishes C99 interaction with PSEN1 and thus APP C99 cleavage by gamma-secretase, most probably through stabilization of the direct interaction between APBA2 and APP. The intracellular fragment AlcICD suppresses APBB1-dependent transactivation stimulated by APP C-terminal intracellular fragment (AICD), most probably by competing with AICD for APBB1- binding. May modulate calcium-mediated postsynaptic signals (By similarity). {ECO:0000250, ECO:0000269|PubMed:12972431}.; . TISSUE SPECIFICITY: Expressed in the brain and, a lower level, in the heart, skeletal muscle, kidney and placenta. Accumulates in dystrophic neurites around the amyloid core of Alzheimer disease senile plaques (at protein level). {ECO:0000269|PubMed:12498782, ECO:0000269|PubMed:12972431}.; lymphoreticular;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;muscle;bile duct;pancreas;pia mater;lung;adrenal gland;placenta;head and neck;kidney;stomach;thymus;cerebellum; whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.63818 0.13776 -1.054560763 7.60202878 278.07434 3.57331 CLSTN2 4.5392971229794e-05 0.998223023780062 0.00173158324870806 calsyntenin 2 FUNCTION: May modulate calcium-mediated postsynaptic signals. {ECO:0000250}.; . TISSUE SPECIFICITY: Restricted to the brain. {ECO:0000269|PubMed:12498782}.; . . 0.47893 0.26477 -0.433580228 24.71691437 460.97449 4.45111 CLSTN2-AS1 . . . CLSTN2 antisense RNA 1 . . . . . . . . . . . CLSTN3 0.997857932255683 0.00214206496912635 2.77519047726971e-09 calsyntenin 3 FUNCTION: May modulate calcium-mediated postsynaptic signals. Complex formation with APBA2 and APP, stabilizes APP metabolism and enhances APBA2-mediated suppression of beta-APP40 secretion, due to the retardation of intracellular APP maturation. {ECO:0000250}.; . TISSUE SPECIFICITY: According to PubMed:12498782, expressed predominantly in the brain and in kidney. Low levels in heart, skeletal muscle, liver, placenta, pancreas and lung. According to PubMed:12972431, predominant expression in brain, and only marginal in kidney. In brain, present throughout all cortical layers, highest levels in GABAergic neurons (based on morphology and distribution pattern). {ECO:0000269|PubMed:12498782, ECO:0000269|PubMed:12972431}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;frontal lobe;thyroid;testis;amniotic fluid;bladder;brain;unclassifiable (Anatomical System);amygdala;cartilage;islets of Langerhans;pineal body;breast;pancreas;lung;adrenal gland;placenta;macula lutea;hippocampus;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; whole brain;medulla oblongata;occipital lobe;globus pallidus;pons;atrioventricular node;cingulate cortex;cerebellum; 0.35946 0.10330 -1.653566591 2.760084926 302.14905 3.70210 CLTA 0.961296504131539 0.0386215023538836 8.1993514577028e-05 clathrin light chain A FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.; . . lymphoreticular;ovary;skin;retina;prostate;optic nerve;ganglion;frontal lobe;endometrium;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; whole brain;amygdala;occipital lobe;thalamus;subthalamic nucleus;placenta;prefrontal cortex;globus pallidus;kidney;cingulate cortex;cerebellum; 0.18609 0.35616 0.014844891 54.94810097 43.24079 1.24806 CLTB 0.115492460175414 0.857408649748734 0.0270988900758523 clathrin light chain B FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;hippocampus;visual apparatus;hypopharynx;cervix;head and neck;kidney;mammary gland;stomach;thymus;cerebellum; whole brain;superior cervical ganglion;thalamus;cerebellum peduncles;temporal lobe;pons;skeletal muscle;skin;subthalamic nucleus;placenta;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;cerebellum; 0.42524 0.24613 -0.229483771 36.86010852 6.86616 0.25469 CLTC 0.99999999331335 6.6866504571628e-09 1.07447833991745e-22 clathrin heavy chain FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network.; . . smooth muscle;ovary;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;spinal cord;blood;skeletal muscle;breast;bile duct;lung;adrenal gland;mesenchyma;nasopharynx;placenta;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; amygdala;occipital lobe;subthalamic nucleus;thalamus;medulla oblongata;hypothalamus;globus pallidus;pons;parietal lobe;cingulate cortex; 0.64701 0.94571 -1.3098007 4.847841472 29.64323 0.94706 CLTCL1 1.24075567829919e-26 0.00179073417867916 0.998209265821321 clathrin heavy chain like 1 FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Maximal levels in skeletal muscle. High levels in heart and testis. Low expression detected in all other tissues.; unclassifiable (Anatomical System);cartilage;heart;ovary;lacrimal gland;muscle;colon;parathyroid;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;cerebral cortex;synovium;placenta;thyroid;bone;macula lutea;pituitary gland;testis;germinal center;stomach;peripheral nerve; testis - interstitial;testis; 0.26676 0.76568 2.353734945 98.41943855 6979.97645 17.78107 CLU 0.453463613311341 0.545273784796619 0.00126260189204046 clusterin FUNCTION: Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress- induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. Secreted isoform 1 protects cells against apoptosis and against cytolysis by complement. Intracellular isoforms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Nuclear isoforms promote apoptosis. Mitochondrial isoforms suppress BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation. {ECO:0000269|PubMed:11123922, ECO:0000269|PubMed:12047389, ECO:0000269|PubMed:12176985, ECO:0000269|PubMed:12551933, ECO:0000269|PubMed:12882985, ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:17260971, ECO:0000269|PubMed:17407782, ECO:0000269|PubMed:17412999, ECO:0000269|PubMed:17689225, ECO:0000269|PubMed:19137541, ECO:0000269|PubMed:19535339, ECO:0000269|PubMed:19996109, ECO:0000269|PubMed:20068069, ECO:0000269|PubMed:21505792}.; . TISSUE SPECIFICITY: Detected in blood plasma, cerebrospinal fluid, milk, seminal plasma and colon mucosa. Detected in the germinal center of colon lymphoid nodules and in colon parasympathetic ganglia of the Auerbach plexus (at protein level). Ubiquitous. Detected in brain, testis, ovary, liver and pancreas, and at lower levels in kidney, heart, spleen and lung. {ECO:0000269|PubMed:11123922, ECO:0000269|PubMed:17260971, ECO:0000269|PubMed:17322305, ECO:0000269|PubMed:17412999, ECO:0000269|PubMed:1974459, ECO:0000269|PubMed:2387851, ECO:0000269|PubMed:2780565, ECO:0000269|PubMed:3154963, ECO:0000269|PubMed:8181474, ECO:0000269|PubMed:8292612, ECO:0000269|PubMed:8328966}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;small intestine;heart;islets of Langerhans;adrenal cortex;lens;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;amygdala;uterus corpus;superior cervical ganglion;olfactory bulb;trachea;spinal cord;prefrontal cortex;liver;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13499 0.83713 0.156217551 64.82071243 583.18916 4.89715 CLUAP1 0.000219540497279212 0.979041737756151 0.0207387217465695 clusterin associated protein 1 FUNCTION: Required for cilia biogenesis. Appears to function within the multiple intraflagellar transport complex B (IFT-B). Key regulator of hedgehog signaling (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis, thyroid and trachea and to a lower extent in spinal cord and adrenal gland. Highly expressed in colon cancer and osteosarcoma cell lines. {ECO:0000269|PubMed:15480429, ECO:0000269|PubMed:17203229}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;frontal lobe;cochlea;bone;lymph;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06099 0.10694 0.176444282 66.07100731 2078.778 8.40152 CLUH 0.999701830275383 0.000298169720022127 4.59477567379334e-12 clustered mitochondria (cluA/CLU1) homolog FUNCTION: mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria. Specifically binds mRNAs of nuclear- encoded mitochondrial proteins in the cytoplasm and regulates transport or translation of these transcripts close to mitochondria, playing a role in mitochondrial biogenesis. {ECO:0000255|HAMAP-Rule:MF_03013, ECO:0000269|PubMed:25349259}.; . . . . 0.28056 0.11024 -2.227040428 1.332861524 2171.23755 8.58035 CLUHP1 . . . clustered mitochondria (cluA/CLU1) homolog pseudogene 1 . . . . . . . . . . . CLUHP2 . . . clustered mitochondria (cluA/CLU1) homolog pseudogene 2 . . . . . . . . . . . CLUHP3 . . . clustered mitochondria (cluA/CLU1) homolog pseudogene 3 . . . . . 0.04632 . . . . . CLUHP4 . . . clustered mitochondria (cluA/CLU1) homolog pseudogene 4 . . . . . . . . . . . CLUHP5 . . . clustered mitochondria (cluA/CLU1) homolog pseudogene 5 . . . . . . . . . . . CLUHP6 . . . clustered mitochondria (cluA/CLU1) homolog pseudogene 6 . . . . . . . . . . . CLUHP7 . . . clustered mitochondria (cluA/CLU1) homolog pseudogene 7 . . . . . . . . . . . CLUHP8 . . . clustered mitochondria (cluA/CLU1) homolog pseudogene 8 . . . . . . . . . . . CLUHP9 . . . clustered mitochondria (cluA/CLU1) homolog pseudogene 9 . . . . . . . . . . . CLUHP10 . . . clustered mitochondria (cluA/CLU1) homolog pseudogene 10 . . . . . . . . . . . CLUHP11 . . . clustered mitochondria (cluA/CLU1) homolog pseudogene 11 . . . . . . . . . . . CLUL1 3.21487861579903e-06 0.552268350224194 0.44772843489719 clusterin like 1 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;developmental;colon;parathyroid;fovea centralis;skeletal muscle;retina;optic nerve;lung;placenta;thyroid;macula lutea;pituitary gland;testis;head and neck;kidney;brain;mammary gland; superior cervical ganglion; 0.09532 0.08808 0.663285274 84.55414013 467.24389 4.47842 CLVS1 0.853643444640218 0.145855788528114 0.00050076683166803 clavesin 1 FUNCTION: Required for normal morphology of late endosomes and/or lysosomes in neurons (By similarity). Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). {ECO:0000250, ECO:0000269|PubMed:19651769}.; . TISSUE SPECIFICITY: Expressed mainly in the brain. {ECO:0000269|PubMed:16802092}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.64937 . -0.494039303 22.09247464 26.81975 0.86743 CLVS2 0.125512834104803 0.850883113630408 0.0236040522647893 clavesin 2 FUNCTION: Required for normal morphology of late endosomes and/or lysosomes in neurons (By similarity). Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). {ECO:0000250, ECO:0000269|PubMed:19651769}.; . . . . 0.20055 . -0.007201372 53.19061099 21.63648 0.72841 CLYBL 8.32420361913943e-06 0.75519278289758 0.244798892898801 citrate lyase beta like FUNCTION: Mitochondrial malate and beta-methylmalate synthase, which may be involved in vitamin B12 metabolism (Probable). Acts both as a malate synthase, converting glyoxylate and acetyl-CoA to malate. Also acts as a beta-methylmalate synthase by mediating conversion of glyoxylate and propionyl-CoA to beta-methylmalate (PubMed:24334609). {ECO:0000269|PubMed:24334609}.; . . unclassifiable (Anatomical System);myocardium;ovary;cartilage;islets of Langerhans;colon;skin;retina;lung;bone;liver;testis;kidney;brain;stomach; subthalamic nucleus;liver;ciliary ganglion;kidney; 0.19529 0.32284 0.773521534 87.06062751 1528.33408 7.26304 CLYBL-AS1 . . . CLYBL antisense RNA 1 . . . . . . . . . . . CLYBL-AS2 . . . CLYBL antisense RNA 2 . . . . . . . . . . . CMA1 4.1077240038228e-08 0.0573724788938985 0.942627480028862 chymase 1 FUNCTION: Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion.; . TISSUE SPECIFICITY: Mast cells in lung, heart, skin and placenta. Expressed in both normal skin and in urticaria pigmentosa lesions. {ECO:0000269|PubMed:8144971}.; unclassifiable (Anatomical System); atrioventricular node; 0.13108 0.62648 0.196671391 67.19155461 132.19888 2.50248 CMAHP . . . cytidine monophospho-N-acetylneuraminic acid hydroxylase, pseudogene FUNCTION: Sialic acids are components of carbohydrate chains of glycoconjugates and are involved in cell-cell recognition and cell-pathogen interactions. That protein has no CMP-N- acetylneuraminate monooxygenase activity and is not able to convert CMP-N-acetylneuraminic acid (CMP-Neu5Ac) into its hydroxylated derivative CMP-N-glycolylneuraminic acid (CMP- Neu5Gc), a sialic acid abundantly expressed at the surface of many cells in vertebrates (PubMed:9624188). However, it may play a role in Wnt signaling (PubMed:19890979). {ECO:0000269|PubMed:19890979, ECO:0000269|PubMed:9624188, ECO:0000303|PubMed:11562455, ECO:0000303|PubMed:12192086, ECO:0000303|PubMed:9751737}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in thymus. Not expressed in brain. May be expressed in adult stem cells (at protein level) (PubMed:19890979). {ECO:0000269|PubMed:19890979, ECO:0000269|PubMed:9624188}.; . . 0.18190 0.13388 . . . . CMAS 0.472364310654414 0.527413530504619 0.000222158840967365 cytidine monophosphate N-acetylneuraminic acid synthetase FUNCTION: Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN).; . TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in pancreas, kidney, liver, skeletal muscle, lung, placenta, brain, heart, colon, PBL, small intestine, ovary, testis, prostate, thymus and spleen. {ECO:0000269|PubMed:11602804}.; myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;ganglion;frontal lobe;cochlea;cerebral cortex;endometrium;bone;thyroid;iris;testis;amniotic fluid;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;cerebellum cortex;islets of Langerhans;hypothalamus;pharynx;blood;breast;pancreas;pia mater;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;stomach; amygdala;testis;cingulate cortex; 0.36486 0.14268 -0.383807564 27.41802312 25.85541 0.84148 CMBL 0.00776530380841664 0.927438683285046 0.0647960129065377 carboxymethylenebutenolidase homolog (Pseudomonas) FUNCTION: Cysteine hydrolase. Can convert the prodrug olmesartan medoxomil into its pharmacologically active metabolite olmerstatan, an angiotensin receptor blocker, in liver and intestine. May also activate beta-lactam antibiotics faropenem medoxomil and lenampicillin. {ECO:0000269|PubMed:20177059}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in liver, followed by kidney, small intestine and colon. Present in liver and intestine (at protein level). {ECO:0000269|PubMed:20177059}.; unclassifiable (Anatomical System);cartilage;lacrimal gland;islets of Langerhans;spinal cord;adrenal cortex;colon;parathyroid;skin;skeletal muscle;prostate;lung;cochlea;adrenal gland;bone;placenta;thyroid;liver;cervix;kidney;spinal ganglion;brain;mammary gland;pineal gland;stomach; superior cervical ganglion;liver;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10719 0.08618 0.150760231 64.51403633 88.01618 2.00678 CMC1 0.00144188642781411 0.433893860829561 0.564664252742625 C-x(9)-C motif containing 1 FUNCTION: Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration. {ECO:0000250}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;atrium;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;trabecular meshwork;placenta;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; . 0.04797 0.05904 -0.031067188 51.03798066 . . CMC2 0.00149210999958192 0.4405678098548 0.557940080145618 C-x(9)-C motif containing 2 FUNCTION: May be involved in cytochrome c oxidase biogenesis. {ECO:0000250}.; . . . . 0.10156 0.09334 0.147123112 64.11299835 43.40234 1.25309 CMC4 0.164577983805174 0.640111092163785 0.195310924031041 C-x(9)-C motif containing 4 . DISEASE: Note=Overexpressed in T-cell leukemia bearing a t(X;14) translocation. {ECO:0000269|PubMed:8361760}.; TISSUE SPECIFICITY: Expressed in many tissues with a relatively high level in skeletal muscle.; . . 0.21172 . 0.145304857 63.81221986 12.93618 0.47171 CMD1B . . . cardiomyopathy, dilated 1B (autosomal dominant) . . . . . . . . . . . CMD1F . . . cardiomyopathy, dilated 1F (autosomal dominant) . . . . . . . . . . . CMD1H . . . cardiomyopathy, dilated 1H (autosomal dominant) . . . . . . . . . . . CMD1K . . . cardiomyopathy, dilated 1K (autosomal dominant) . . . . . . . . . . . CMD1Q . . . cardiomyopathy, dilated 1Q (autosomal dominant) . . . . . . . . . . . CMIP 0.999886587184176 0.000113412763184678 5.26393198914349e-11 c-Maf inducing protein FUNCTION: Plays a role in T-cell signaling pathway. Isoform 2 may play a role in T-helper 2 (Th2) signaling pathway and seems to represent the first proximal signaling protein that links T-cell receptor-mediated signal to the activation of c-Maf Th2 specific factor. {ECO:0000269|PubMed:12939343, ECO:0000269|PubMed:15128042}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in peripheral blood mononuclear cells and kidney. Lower expression in brain and liver. Expression is down-regulated in activated cells. Isoform 2 is expressed in lymphocyte precursors, however, expression shuts down during maturation and differentiation in thymus and fetal liver. {ECO:0000269|PubMed:12939343}.; . . . . -1.530301957 3.367539514 21.62477 0.72736 CMKLR1 0.0685269634408008 0.73606981069896 0.195403225860239 chemerin chemokine-like receptor 1 FUNCTION: Receptor for the chemoattractant adipokine chemerin/RARRES2 and for the omega-3 fatty acid derived molecule resolvin E1. Interaction with RARRES2 induces activation of intracellular signaling molecules, such as SKY, MAPK1/3 (ERK1/2), MAPK14/P38MAPK and PI3K leading to multifunctional effects, like, reduction of immune responses, enhancing of adipogenesis and angionesis. Resolvin E1 down-regulates cytokine production in macrophages by reducing the activation of MAPK1/3 (ERK1/2) and NF- kappa-B. Positively regulates adipogenesis and adipocyte metabolism. Acts as a coreceptor for several SIV strains (SIVMAC316, SIVMAC239, SIVMACL7E-FR and SIVSM62A), as well as a primary HIV-1 strain (92UG024-2). {ECO:0000269|PubMed:15728234, ECO:0000269|PubMed:15753205, ECO:0000269|PubMed:20044979, ECO:0000269|PubMed:9603476}.; . TISSUE SPECIFICITY: Prominently expressed in developing osseous and cartilaginous tissue. Also found in adult parathyroid glands. Expressed in cardiovascular system, brain, kidney, gastrointestinal tissues and myeloid tissues. Expressed in a broad array of tissues associated with hematopoietic and immune function including, spleen, thymus, appendix, lymph node, bone marrow and fetal liver. Among leukocyte populations abundant expression in monocyte-derived macrophage and immature dendritic cells (DCs). High expression in blood monocytes and low levels in polymorphonuclear cells and T-cells. Expressed on endothelial cells. Highly expressed in differentiating adipocytes. {ECO:0000269|PubMed:14530373, ECO:0000269|PubMed:15728234, ECO:0000269|PubMed:15753205, ECO:0000269|PubMed:18242188, ECO:0000269|PubMed:20044979, ECO:0000269|PubMed:8976386}.; nasopharynx;testis;kidney; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04562 . 0.440999548 77.79547063 104.9837 2.21545 CMM . . . cutaneous malignant melanoma/dysplastic nevus . . . . . . . . . . . CMPK1 0.319273509909851 0.664037884969374 0.016688605120775 cytidine/uridine monophosphate kinase 1 FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase activity. {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:10462544, ECO:0000269|PubMed:11912132, ECO:0000269|PubMed:23416111}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11681623}.; . . 0.20329 0.20007 0.369407109 74.95281906 536.7809 4.72307 CMPK2 0.00180796531822905 0.71728587844157 0.280906156240201 cytidine/uridine monophosphate kinase 2 FUNCTION: May participate in dUTP and dCTP synthesis in mitochondria. Is able to phosphorylate dUMP, dCMP, CMP, UMP and monophosphates of the pyrimidine nucleoside analogs ddC, dFdC, araC, BVDU and FdUrd with ATP as phosphate donor. Efficacy is highest for dUMP followed by dCMP; CMP and UMP are poor substrates. May be involved in mtDNA depletion caused by long term treatment with ddC or other pyrimidine analogs. Also displays broad nucleoside diphosphate kinase activity. {ECO:0000269|PubMed:17999954, ECO:0000269|PubMed:23416111}.; . TISSUE SPECIFICITY: Among all investigated tumors, leukemia cells show the most abundant expression. {ECO:0000269|PubMed:17999954}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;parathyroid;skin;bone marrow;uterus;prostate;lung;endometrium;adrenal gland;placenta;liver;testis;spleen;germinal center;brain;mammary gland;stomach; superior cervical ganglion;ciliary ganglion; 0.07192 0.11137 . . 153.38875 2.70880 CMR1A . . . cardiomyopathy, restrictive 1A (autosomal dominant) . . . . . . . . . . . CMR2A . . . cardiomyopathy, restrictive 2A (autosomal recessive) . . . . . . . . . . . CMR3A . . . cardiomyopathy, restrictive 3A (X-linked) . . . . . . . . . . . CMSS1 0.000665484679606108 0.912513157701145 0.0868213576192489 cms1 ribosomal small subunit homolog (yeast) . . . . . 0.08753 0.09666 0.237127192 68.98443029 75.79735 1.82388 CMT1A . . . Charcot-Marie-Tooth neuropathy 1A (greatly reduced nerve conduction velocity, hereditary motor sensory neuropathy Ia) . . . . . . . . . . . CMT2B . . . Charcot-Marie-Tooth neuropathy 2B . . . . . . . . . . . CMTM1 0.00129753085731742 0.646946600287837 0.351755868854846 CKLF like MARVEL transmembrane domain containing 1 . . TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:12782130, ECO:0000269|PubMed:15147728}.; uterus;ovary;heart;kidney;skin; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.02656 0.05828 -0.314027422 31.9297004 29.60962 0.94568 CMTM2 2.07069164121887e-05 0.281061717485753 0.718917575597835 CKLF like MARVEL transmembrane domain containing 2 . . TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:12782130}.; unclassifiable (Anatomical System);medulla oblongata;lung;hippocampus;muscle;testis; . 0.05005 0.07051 0.527368849 80.73248408 805.67785 5.59172 CMTM3 0.107243308615464 0.77595016927362 0.116806522110915 CKLF like MARVEL transmembrane domain containing 3 . . TISSUE SPECIFICITY: Expressed in the leukocytes, placenta and testis. {ECO:0000269|PubMed:12782130}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;pituitary gland;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;trigeminal ganglion; 0.16257 0.11143 -0.163345027 41.24793583 11.05451 0.40076 CMTM4 0.0393834626167364 0.83985154261536 0.120764994767903 CKLF like MARVEL transmembrane domain containing 4 . . TISSUE SPECIFICITY: Highly expressed in testis and prostate. {ECO:0000269|PubMed:12782130}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;thyroid;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.20706 0.08979 0.082802743 60.09082331 20.18691 0.69076 CMTM5 0.0600876421893113 0.868470157510514 0.0714422003001751 CKLF like MARVEL transmembrane domain containing 5 . . TISSUE SPECIFICITY: Highly expressed in the brain. {ECO:0000269|PubMed:12782130}.; unclassifiable (Anatomical System);hypothalamus;fovea centralis;choroid;lens;retina;prostate;optic nerve;whole body;lung;hippocampus;macula lutea;testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;spinal cord;globus pallidus;atrioventricular node;cingulate cortex;parietal lobe; 0.14482 0.08592 0.148941568 64.31941496 138.0685 2.55815 CMTM6 0.822756767085209 0.1732736375197 0.00396959539509028 CKLF like MARVEL transmembrane domain containing 6 . . TISSUE SPECIFICITY: Expressed in the leukocytes, placenta and testis. {ECO:0000269|PubMed:12782130}.; lymphoreticular;ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;testis;dura mater;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;bile duct;pancreas;pia mater;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; testis;white blood cells;atrioventricular node;whole blood;bone marrow; 0.15264 0.09433 0.080983847 59.76055674 58.18288 1.54350 CMTM7 0.426220205435479 0.540749949542215 0.0330298450223058 CKLF like MARVEL transmembrane domain containing 7 . . TISSUE SPECIFICITY: Highly expressed in leukocytes. {ECO:0000269|PubMed:12782130}.; lymphoreticular;smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;endometrium;testis;brain;unclassifiable (Anatomical System);lymph node;lacrimal gland;blood;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; white blood cells;thymus; 0.10227 . -0.075159878 47.78839349 13.5481 0.49206 CMTM8 0.847881588243377 0.149466047128642 0.00265236462798138 CKLF like MARVEL transmembrane domain containing 8 . . TISSUE SPECIFICITY: Highly expressed in liver and pancreas. {ECO:0000269|PubMed:12782130}.; unclassifiable (Anatomical System);islets of Langerhans;adrenal cortex;colon;fovea centralis;choroid;lens;retina;optic nerve;lung;larynx;macula lutea;liver;testis;head and neck;kidney;brain;aorta;stomach; superior cervical ganglion;liver; 0.09889 0.09242 0.170987912 65.5579146 87.87774 2.00361 CMTR1 0.999294924067237 0.000705075925193886 7.56928692103742e-12 cap methyltransferase 1 FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) to produce m(7)GpppRm (cap1). Displays a preference for cap0 transcripts. Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway. {ECO:0000269|PubMed:18533109, ECO:0000269|PubMed:20713356, ECO:0000269|PubMed:21310715}.; . . . . 0.31610 0.11198 -1.087493118 7.106628922 28.34808 0.90802 CMTR2 1.4241642942685e-07 0.213580302989898 0.786419554593672 cap methyltransferase 2 FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the second nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) (cap0) to produce m(7)GpppRmpNm (cap2). Recognizes a guanosine cap on RNA independently of its N(7) methylation status. Display cap2 methylation on both cap0 and cap1. Displays a preference for cap1 RNAs. {ECO:0000269|PubMed:21310715}.; . . . . . . 0.090079492 60.64519934 1582.48573 7.35867 CMTX2 . . . Charcot-Marie-Tooth neuropathy, X-linked 2 (recessive) . . . . . . . . . . . CMTX3 . . . Charcot-Marie-Tooth neuropathy, X-linked 3 (dominant) . . . . . . . . . . . CMYA5 3.80676086686769e-43 1.17931164946004e-06 0.999998820688351 cardiomyopathy associated 5 FUNCTION: May serve as an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) via binding to PRKAR2A (By similarity). May function as a repressor of calcineurin-mediated transcriptional activity. May attenuate calcineurin ability to induce slow-fiber gene program in muscle and may negatively modulate skeletal muscle regeneration (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle; at a strong level and in heart. {ECO:0000269|PubMed:11297942}.; . . 0.09185 . 10.42976423 99.97051191 21940.08961 31.15233 CNA1 . . . cornea plana 1 (autosomal dominant) . . . . . . . . . . . CNBD1 2.81654403463771e-10 0.0422203557170827 0.957779644001263 cyclic nucleotide binding domain containing 1 . . . . . 0.08553 . 0.821252311 88.01604152 419.68402 4.28002 CNBD2 2.29296795546672e-07 0.892824754153356 0.107175016549848 cyclic nucleotide binding domain containing 2 . . . . . 0.10488 . 0.112125503 62.09601321 3832.59601 12.18340 CNBP 0.92057305466698 0.0789293504626798 0.00049759487034046 CCHC-type zinc finger, nucleic acid binding protein FUNCTION: Single-stranded DNA-binding protein, with specificity to the sterol regulatory element (SRE). Involved in sterol-mediated repression.; DISEASE: Dystrophia myotonica 2 (DM2) [MIM:602668]: A multisystem disease characterized by the association of proximal muscle weakness with myotonia, cardiac manifestations and cataract. Additional features can include hyperhidrosis, testicular atrophy, insulin resistance and diabetes and central nervous system anomalies in rare cases. Note=The disease is caused by mutations affecting the gene represented in this entry. The causative mutation is a CCTG expansion (mean approximately 5000 repeats) located in intron 1 of the CNBP gene.; TISSUE SPECIFICITY: Present in all tissues examined.; . . 0.87038 0.43956 0.301449681 71.80938901 8.44571 0.30943 CNC2 . . . Carney complex type 2, multiple neoplasia and lentiginosis . . . . . . . . . . . CNDP1 1.90969167167883e-05 0.972165890077105 0.0278150130061787 carnosine dipeptidase 1 (metallopeptidase M20 family) . . TISSUE SPECIFICITY: Found in serum and adult nervous central system. Absent in serum from patients with homocarnosinosis. {ECO:0000269|PubMed:12473676, ECO:0000269|PubMed:6616870}.; unclassifiable (Anatomical System);lung;ganglion;frontal lobe;hypothalamus;visual apparatus;hippocampus;testis;choroid;kidney;brain;skin;skeletal muscle; amygdala;whole brain;medulla oblongata;occipital lobe;subthalamic nucleus;thalamus;hypothalamus;prefrontal cortex;globus pallidus;caudate nucleus;pons;parietal lobe;cingulate cortex; 0.11983 0.24162 1.247448154 93.43595188 1273.96612 6.72127 CNDP2 0.00119100825592748 0.989530221396845 0.00927877034722698 CNDP dipeptidase 2 (metallopeptidase M20 family) FUNCTION: Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Isoform 2 may be play a role as tumor suppressor in hepatocellular carcinoma (HCC) cells. {ECO:0000269|PubMed:17121880, ECO:0000269|PubMed:19346245}.; . TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed with higher levels in kidney and liver (at protein level). Isoform 2 is expressed in fetal tissues, it is only expressed in adult liver and placental tissues. {ECO:0000269|PubMed:12473676, ECO:0000269|PubMed:17121880}.; lymphoreticular;ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;aorta;stomach;thymus;cerebellum; superior cervical ganglion;prostate;occipital lobe;hypothalamus;thyroid;prefrontal cortex;kidney;cingulate cortex; 0.27378 0.41801 -0.753139731 13.67067705 2551.72508 9.43409 CNEP1R1 0.291176144907272 0.688053378935279 0.0207704761574493 CTD nuclear envelope phosphatase 1 regulatory subunit 1 FUNCTION: Forms with the serine/threonine protein phosphatase CTDNEP1 an active complex which dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at differents levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. {ECO:0000269|PubMed:22134922}.; . TISSUE SPECIFICITY: Muscle specific with lower expression in other metabolic tissues. {ECO:0000269|PubMed:22134922}.; . . . . 0.58987904 82.3720217 27.2753 0.87911 CNFN 0.347229317263347 0.596474838474147 0.0562958442625063 cornifelin FUNCTION: Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia. {ECO:0000269|PubMed:15147942}.; . TISSUE SPECIFICITY: Abundant in the cervix. Moderately abundant in the uterus and fetal skin. Expression is markedly increased in psoriatic skin (18.5 fold increase in comparison with normal skin) and its overexpression alters the protein composition of cornified cell envelope (CE), but does not affect keratinocyte differentiation. Expressed in the granular cell layer of epidermis in uninvolved psoriatic skin and in the psoriatic lesions it is found in the upper-spinous layer. Increased expression also seen in atopic dermatitis (14.3 fold increase in comparison with normal skin) and mycosis fungoides (4.6 fold increase in comparison with normal skin) and in both conditions expressed in the granular cell layer of epidermis. {ECO:0000269|PubMed:15147942}.; unclassifiable (Anatomical System);uterus;prostate;lung;larynx;hypopharynx;colon;head and neck; superior cervical ganglion;tongue;skin;tonsil; 0.26740 . -0.075159878 47.78839349 13.65731 0.49579 CNGA1 5.70944542887735e-10 0.382605442464728 0.617394556964328 cyclic nucleotide gated channel alpha 1 FUNCTION: Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors.; DISEASE: Retinitis pigmentosa 49 (RP49) [MIM:613756]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:15570217, ECO:0000269|PubMed:7479749}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Rod cells in the retina.; unclassifiable (Anatomical System);optic nerve;heart;macula lutea;liver;spleen;blood;fovea centralis;choroid;kidney;lens;retina; dorsal root ganglion; 0.68196 0.13253 -0.045835247 50.34206181 1631.06539 7.46636 CNGA2 0.0815316936822351 0.908071273302831 0.0103970330149337 cyclic nucleotide gated channel alpha 2 FUNCTION: Odorant signal transduction is probably mediated by a G- protein coupled cascade using cAMP as second messenger. The olfactory channel can be shown to be activated by cyclic nucleotides which leads to a depolarization of olfactory sensory neurons.; . . . . 0.29013 0.11368 0.492370491 79.60603916 1456.93951 7.12113 CNGA3 1.18045078044952e-08 0.329746703133037 0.670253285062455 cyclic nucleotide gated channel alpha 3 FUNCTION: Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of cone photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficacy of the channel when coexpressed with CNGB3 (By similarity). Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones. {ECO:0000250, ECO:0000269|PubMed:10888875}.; DISEASE: Achromatopsia 2 (ACHM2) [MIM:216900]: An ocular stationary disorder due to the absence of functioning cone photoreceptors in the retina. It is characterized by total colorblindness, low visual acuity, photophobia and nystagmus. {ECO:0000269|PubMed:11536077, ECO:0000269|PubMed:14757870, ECO:0000269|PubMed:15712225, ECO:0000269|PubMed:18521937, ECO:0000269|PubMed:24903488, ECO:0000269|PubMed:9662398}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in CNGA3 may be a cause of Leber congenital amaurosis (LCA), a severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near- absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:21901789}.; TISSUE SPECIFICITY: Prominently expressed in retina.; islets of Langerhans;visual apparatus;pituitary gland; dorsal root ganglion;superior cervical ganglion;spinal cord;appendix;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;pituitary;skeletal muscle; 0.29835 0.18259 -0.655870776 16.12408587 753.63869 5.44301 CNGA4 9.8597680152566e-05 0.940540110617114 0.0593612917027331 cyclic nucleotide gated channel alpha 4 FUNCTION: Second messenger, cAMP, causes the opening of cation- selective cyclic nucleotide-gated (CNG) channels and depolarization of the neuron (olfactory sensory neurons, OSNs). CNGA4 is the modulatory subunit of this channel which is known to play a central role in the transduction of odorant signals and subsequent adaptation. By accelerating the calcium-mediated negative feedback in olfactory signaling it allows rapid adaptation to odor stimulation and extends its range of odor detection (By similarity). {ECO:0000250}.; . . . . 0.44276 0.11034 0.180083178 66.16536919 833.307 5.65413 CNGB1 6.63008798434668e-25 0.00261065425828832 0.997389345741712 cyclic nucleotide gated channel beta 1 FUNCTION: Subunit of cyclic nucleotide-gated (CNG) channels, nonselective cation channels, which play important roles in both visual and olfactory signal transduction. When associated with CNGA1, it is involved in the regulation of ion flow into the rod photoreceptor outer segment (ROS), in response to light-induced alteration of the levels of intracellular cGMP.; DISEASE: Retinitis pigmentosa 45 (RP45) [MIM:613767]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:11379879}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);optic nerve;frontal lobe;placenta;visual apparatus;testis;brain;retina; amygdala;medulla oblongata;subthalamic nucleus;superior cervical ganglion;temporal lobe;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.73096 0.14143 1.330085127 94.13776834 2197.11704 8.63028 CNGB3 8.86463595476286e-11 0.884429905885428 0.115570094025925 cyclic nucleotide gated channel beta 3 FUNCTION: Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cGMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficiency of the channel when coexpressed with CNGA3 (By similarity). Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones. {ECO:0000250, ECO:0000269|PubMed:10888875}.; DISEASE: Achromatopsia 3 (ACHM3) [MIM:262300]: An ocular stationary disorder due to the absence of functioning cone photoreceptors in the retina. It is characterized by total colorblindness, low visual acuity, photophobia and nystagmus. Achromatopsia type 3 patients manifest severe myopia. {ECO:0000269|PubMed:10888875, ECO:0000269|PubMed:10958649, ECO:0000269|PubMed:12357335, ECO:0000269|PubMed:14757870, ECO:0000269|PubMed:15657609, ECO:0000269|PubMed:15712225}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed specifically in the retina. {ECO:0000269|PubMed:10958649}.; medulla oblongata;hypothalamus;iris;pineal gland;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;medulla oblongata;atrioventricular node;trigeminal ganglion; 0.08889 . 1.673699792 96.331682 696.97117 5.25879 CNIH1 0.843993720425153 0.153172212643376 0.0028340669314712 cornichon family AMPA receptor auxiliary protein 1 FUNCTION: Involved in the selective transport and maturation of TGF-alpha family proteins. {ECO:0000269|PubMed:17607000}.; . TISSUE SPECIFICITY: Highly expressed in heart, liver, skeletal muscle, pancreas, adrenal medulla and cortex, thyroid, testis, spleen, appendix, peripheral blood lymphocytes and bone marrow. Lower expression found in brain, placenta, lung, kidney, ovary, small intestine, stomach, lymph node, thymus and fetal liver. Expression is up-regulated in dorsolateral prefrontal cortex of patients with schizophrenia (postmortem brain study). {ECO:0000269|PubMed:23103966}.; . . 0.44164 0.13588 0.057118534 57.99716914 3.72369 0.13853 CNIH2 0.894540206775537 0.10443420938235 0.00102558384211257 cornichon family AMPA receptor auxiliary protein 2 FUNCTION: Regulates the trafficking and gating properties of AMPA- selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by regulating their rates of activation, deactivation and desensitization. Blocks CACNG8-mediated resensitization of AMPA receptors. {ECO:0000269|PubMed:20805473}.; . TISSUE SPECIFICITY: Expression is up-regulated in dorsolateral prefrontal cortex of patients with schizophrenia (postmortem brain study). {ECO:0000269|PubMed:23103966}.; unclassifiable (Anatomical System);medulla oblongata;lung;frontal lobe;islets of Langerhans;visual apparatus;hippocampus;testis;brain;retina; . 0.16073 0.11262 -0.119252484 44.53880632 2.28818 0.07752 CNIH3 0.381818439065843 0.607777304166916 0.010404256767241 cornichon family AMPA receptor auxiliary protein 3 FUNCTION: Regulates the trafficking and gating properties of AMPA- selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by regulating their rates of activation, deactivation and desensitization. {ECO:0000269|PubMed:20805473}.; . TISSUE SPECIFICITY: Expression is up-regulated in dorsolateral prefrontal cortex of patients with schizophrenia (postmortem brain study). {ECO:0000269|PubMed:23103966}.; unclassifiable (Anatomical System);bile duct;medulla oblongata;lung;testis;kidney;brain;skin; whole brain;amygdala;occipital lobe;prefrontal cortex;trigeminal ganglion; 0.24655 0.10216 -0.053113545 49.38664779 12.84423 0.46874 CNIH4 0.0847249901890333 0.871306606625009 0.0439684031859571 cornichon family AMPA receptor auxiliary protein 4 FUNCTION: Involved in G protein-coupled receptors (GPCRs) trafficking from the endoplasmic reticulum to the cell surface; it promotes the exit of GPCRs from the early secretory pathway, likely through interaction with the COPII machinery (PubMed:24405750). {ECO:0000269|PubMed:24405750}.; . . . . 0.73420 0.11023 0.25917371 70.05779665 17.45461 0.61259 CNKSR1 3.79048704121579e-16 0.136331852971289 0.863668147028711 connector enhancer of kinase suppressor of Ras 1 FUNCTION: May function as an adapter protein or regulator of Ras signaling pathways.; . . unclassifiable (Anatomical System);ovary;tongue;islets of Langerhans;colon;parathyroid;pancreas;prostate;lung;frontal lobe;endometrium;placenta;testis;amniotic fluid;head and neck;spleen;kidney;brain;mammary gland;bladder;stomach; parietal lobe;skeletal muscle; 0.16583 0.10675 0.516238257 80.33734371 811.05923 5.60139 CNKSR2 0.999748049373382 0.000251950611552683 1.5064955993892e-11 connector enhancer of kinase suppressor of Ras 2 FUNCTION: May function as an adapter protein or regulator of Ras signaling pathways. {ECO:0000269|PubMed:14597674}.; . . unclassifiable (Anatomical System);macula lutea;liver;spleen;fovea centralis;brain;peripheral nerve; amygdala;medulla oblongata;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion; 0.74699 0.12286 -0.47017169 23.25430526 119.59093 2.38054 CNKSR3 0.211063418499667 0.788859474830469 7.71066698639359e-05 CNKSR family member 3 FUNCTION: Probably involved in transepithelial sodium transport. Regulates aldosterone-induced and ENaC-mediated sodium transport possibly through regulation of the ERK pathway (By similarity). {ECO:0000250}.; . . . . . 0.11362 -0.021969881 52.14673272 56.74786 1.51540 CNN1 0.861520643189048 0.138047141053954 0.000432215756998461 calponin 1 FUNCTION: Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Smooth muscle, and tissues containing significant amounts of smooth muscle.; myocardium;medulla oblongata;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; uterus;testis - interstitial;prostate;superior cervical ganglion;uterus corpus;trachea;testis - seminiferous tubule;appendix;testis; 0.31953 0.14336 -0.336073593 30.55555556 38.63481 1.14452 CNN2 0.212309400922857 0.778747265250528 0.00894333382661586 calponin 2 FUNCTION: Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.; . TISSUE SPECIFICITY: Heart and smooth muscle.; myocardium;lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;choroid;fovea centralis;uterus;whole body;oesophagus;cerebral cortex;larynx;bone;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;aorta;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;bone marrow; 0.15623 0.14470 -0.780646273 12.77423921 27.26201 0.87829 CNN2P1 . . . calponin 2 pseudogene 1 . . . . . . . . . . . CNN2P2 . . . calponin 2 pseudogene 2 . . . . . . . . . . . CNN2P3 . . . calponin 2 pseudogene 3 . . . . . . . . . . . CNN2P4 . . . calponin 2 pseudogene 4 . . . . . . . . . . . CNN2P6 . . . calponin 2 pseudogene 6 . . . . . . . . . . . CNN2P7 . . . calponin 2 pseudogene 7 . . . . . . . . . . . CNN2P8 . . . calponin 2 pseudogene 8 . . . . . . . . . . . CNN2P9 . . . calponin 2 pseudogene 9 . . . . . . . . . . . CNN2P10 . . . calponin 2 pseudogene 10 . . . . . . . . . . . CNN2P11 . . . calponin 2 pseudogene 11 . . . . . . . . . . . CNN2P12 . . . calponin 2 pseudogene 12 . . . uterus; . . . . . . . CNN3 0.864370512768343 0.135220457113983 0.000409030117674492 calponin 3 FUNCTION: Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.; . TISSUE SPECIFICITY: Expressed in both non-smooth muscle tissues as well as smooth muscle tissues.; . . 0.46723 0.13805 0.3032669 72.009908 69.9614 1.73556 CNN3P1 . . . calponin 3 pseudogene 1 . . . . . . . . . . . CNNM1 0.906070593117324 0.0939229646303293 6.44225234667531e-06 cyclin and CBS domain divalent metal cation transport mediator 1 FUNCTION: Probable metal transporter. {ECO:0000250}.; . TISSUE SPECIFICITY: Restricted to brain and testis. {ECO:0000269|PubMed:12657465}.; unclassifiable (Anatomical System);optic nerve;bone;macula lutea;liver;testis;fovea centralis;choroid;lens;brain;retina;cerebellum; testis - interstitial;medulla oblongata;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;trigeminal ganglion;cingulate cortex;parietal lobe; 0.17650 0.09844 . . 425.44476 4.30927 CNNM2 0.994106430518482 0.00589340723349558 1.62248022242238e-07 cyclin and CBS domain divalent metal cation transport mediator 2 FUNCTION: Divalent metal cation transporter. Mediates transport of divalent metal cations in an order of Mg(2+) > Co(2+) > Mn(2+) > Sr(2+) > Ba(2+) > Cu(2+) > Fe(2+) (By similarity). {ECO:0000250|UniProtKB:Q3TWN3}.; DISEASE: Hypomagnesemia, seizures, and mental retardation (HOMGSMR) [MIM:616418]: A disease characterized by renal wasting of magnesium, low serum magnesium, seizures, and variable degrees of delayed psychomotor development. {ECO:0000269|PubMed:24699222}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in brain, kidney and placenta, while it is weakly expressed in skeletal muscle. In the kidney, it is expressed in the distal convoluted tubule and the thick ascending limb of Henle loop. {ECO:0000269|PubMed:21397062}.; unclassifiable (Anatomical System);cartilage;colon;fovea centralis;choroid;lens;retina;optic nerve;lung;frontal lobe;nasopharynx;placenta;thyroid;bone;macula lutea;visual apparatus;hippocampus;liver;testis;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle;cerebellum; 0.33332 0.12106 -0.979072682 8.752064166 266.20712 3.50012 CNNM3 . . . cyclin and CBS domain divalent metal cation transport mediator 3 FUNCTION: Probable metal transporter. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in heart and spleen. {ECO:0000269|PubMed:12657465}.; lymphoreticular;smooth muscle;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;cerebellum;thymus; superior cervical ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.25818 0.10796 . . 61.42965 1.59706 CNNM4 0.000338908702685108 0.948762530013012 0.0508985612843028 cyclin and CBS domain divalent metal cation transport mediator 4 FUNCTION: Probable metal transporter. The interaction with the metal ion chaperone COX11 suggests that it may play a role in sensory neuron functions (By similarity). May play a role in biomineralization and retinal function. {ECO:0000250, ECO:0000269|PubMed:19200525, ECO:0000269|PubMed:19200527}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart. {ECO:0000269|PubMed:12657465}.; . . 0.14788 0.10947 -1.153638777 6.233781552 47.18845 1.33052 CNOT1 0.99999999999948 5.19681416924867e-13 2.12480845272865e-33 CCR4-NOT transcription complex subunit 1 FUNCTION: Scaffolding component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA- mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Its scaffolding function implies its interaction with the catalytic complex module and diverse RNA-binding proteins mediating the complex recruitment to selected mRNA 3'UTRs. Involved in degradation of AU-rich element (ARE)-containing mRNAs probably via association with ZFP36. Mediates the recruitment of the CCR4-NOT complex to miRNA targets and to the RISC complex via association with TNRC6A, TNRC6B or TNRC6C. Acts as a transcriptional repressor. Represses the ligand-dependent transcriptional activation by nuclear receptors. Involved in the maintenance of emryonic stem (ES) cell identity. {ECO:0000269|PubMed:10637334, ECO:0000269|PubMed:16778766, ECO:0000269|PubMed:21278420, ECO:0000269|PubMed:21976065, ECO:0000269|PubMed:21984185, ECO:0000269|PubMed:22367759, ECO:0000269|PubMed:23644599}.; . TISSUE SPECIFICITY: Strongly expressed in brain, heart, thymus, spleen, kidney, liver, placenta and lung. Weakly expressed in skeletal muscle and colon. {ECO:0000269|PubMed:10637334}.; ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;cerebral cortex;larynx;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.46774 0.13485 -1.897968997 1.969804199 96.14268 2.11962 CNOT2 0.999868597154773 0.000131402769878082 7.5348514022765e-11 CCR4-NOT transcription complex subunit 2 FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Required for the CCR4-NOT complex structural integrity. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may specificly involve the N-Cor repressor complex containing HDAC3, NCOR1 and NCOR2. Involved in the maintenance of emryonic stem (ES) cell identity. {ECO:0000269|PubMed:14707134, ECO:0000269|PubMed:16712523, ECO:0000269|PubMed:21299754, ECO:0000269|PubMed:22367759}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, heart, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocytes. {ECO:0000269|PubMed:10637334}.; ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;atrium;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;medulla oblongata;prefrontal cortex; 0.28744 0.14229 -0.117432389 44.89266336 17.74579 0.62027 CNOT3 0.999967222421856 3.27775755841756e-05 2.5594162322019e-12 CCR4-NOT transcription complex subunit 3 FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. May be involved in metabolic regulation; may be involved in recruitment of the CCR4-NOT complex to deadenylation target mRNAs involved in energy metabolism. Involved in mitotic progression and regulation of the spindle assembly checkpoint by regulating the stability of MAD1L1 mRNA. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may involve histone deacetylases. Involved in the maintenance of emryonic stem (ES) cell identity. {ECO:0000269|PubMed:14707134, ECO:0000269|PubMed:22342980, ECO:0000269|PubMed:22367759}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, heart, thymus, spleen, kidney, liver, small intestine, lung and peripheral blood leukocytes. {ECO:0000269|PubMed:10637334}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - interstitial;testis;pons;parietal lobe; 0.73088 0.10155 -0.598810865 18.13517339 98.27185 2.14320 CNOT4 0.996013724617981 0.00398626275006778 1.26319514342354e-08 CCR4-NOT transcription complex subunit 4 FUNCTION: Has E3 ubiquitin ligase activity. Involved in activation of the JAK/STAT pathway. {ECO:0000269|PubMed:11823428, ECO:0000269|PubMed:22159038}.; . . parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;amygdala;unclassifiable (Anatomical System);lymph node;blood;lens;breast;lung;nasopharynx;macula lutea;hippocampus;liver;hypopharynx;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.63799 0.13304 0.042348793 57.31304553 2482.62773 9.29031 CNOT4P1 . . . CCR4-NOT transcription complex subunit 4 pseudogene 1 . . . . . . . . . . . CNOT6 0.478458001419819 0.521329968440911 0.000212030139269293 CCR4-NOT transcription complex subunit 6 FUNCTION: Poly(A) nuclease with 3'-5' RNase activity. Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Involved in mRNA decay mediated by the major-protein- coding determinant of instability (mCRD) of the FOS gene in the cytoplasm. In the presence of ZNF335, enhances ligand-dependent transcriptional activity of nuclear hormone receptors, including RARA. The increase of ligand-dependent ESR1-mediated transcription is much smaller, if any. Mediates cell proliferation and cell survival and prevents cellular senescence. {ECO:0000269|PubMed:11889047, ECO:0000269|PubMed:18180299, ECO:0000269|PubMed:20065043, ECO:0000269|PubMed:21233283}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;kidney;stomach; superior cervical ganglion;atrioventricular node; 0.46135 0.12733 -0.291981272 33.20358575 52.51247 1.43432 CNOT6L 0.954497484149675 0.0454974609001354 5.05495018932963e-06 CCR4-NOT transcription complex subunit 6 like FUNCTION: Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. May be involved in the deadenylation-dependent degradation of mRNAs through the 3'-UTR AU-rich element-mediated mechanism. Involved in deadenylation-dependent degradation of CDKN1B mRNA. Its mRNA deadenylase activity can be inhibited by TOB1. Mediates cell proliferation and cell survival and prevents cellular senescence. {ECO:0000269|PubMed:17452450, ECO:0000269|PubMed:21233283}.; . TISSUE SPECIFICITY: Highly expressed in placenta, skeletal muscle, pancreas, testis and leukocytes. Weakly expressed in heart, spleen and thymus. {ECO:0000269|PubMed:17452450}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach;thymus; . 0.48431 . -0.383807564 27.41802312 10.65084 0.38666 CNOT6LP1 . . . CCR4-NOT transcription complex subunit 6-like pseudogene 1 . . . . . . . . . . . CNOT7 0.986495484302418 0.0134984122538764 6.10344370605082e-06 CCR4-NOT transcription complex subunit 7 FUNCTION: Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Its function seems to be partially redundant with that of CNOT8. Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. During miRNA-mediated repression the complex seems also to act as translational repressor during translational initiation. Additional complex functions may be a consequence of its influence on mRNA expression. Associates with members of the BTG family such as TOB1 and BTG2 and is required for their anti- proliferative activity. {ECO:0000269|PubMed:19605561, ECO:0000269|PubMed:20065043, ECO:0000269|PubMed:20634287, ECO:0000269|PubMed:23236473}.; . . ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; occipital lobe;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;trigeminal ganglion;skeletal muscle; 0.82396 0.11262 -0.141298762 42.87567823 5.94172 0.22349 CNOT7P1 . . . CCR4-NOT transcription complex subunit 7 pseudogene 1 . . . . . . . . . . . CNOT7P2 . . . CCR4-NOT transcription complex subunit 7 pseudogene 2 . . . . . . . . . . . CNOT8 0.675125645478961 0.323883621970298 0.000990732550740999 CCR4-NOT transcription complex subunit 8 FUNCTION: Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Its function seems to be partially redundant with that of CNOT7. Catalytic component of the CCR4-NOT complex which is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. During miRNA-mediated repression the complex seems also to act as translational repressor during translational initiation. Additional complex functions may be a consequence of its influence on mRNA expression. Associates with members of the BTG family such as TOB1 and BTG2 and is required for their anti-proliferative activity. {ECO:0000269|PubMed:12771185, ECO:0000269|PubMed:19605561, ECO:0000269|PubMed:20065043, ECO:0000269|PubMed:23236473}.; . . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;cochlea;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;placenta;hippocampus;kidney;stomach;aorta;thymus; testis - interstitial;superior cervical ganglion;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;bone marrow; 0.65460 0.15588 -0.229483771 36.86010852 11.84674 0.42910 CNOT10 0.999834446356576 0.000165553616658122 2.67660404137269e-11 CCR4-NOT transcription complex subunit 10 FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Is not required for association of CNOT7 to the CCR4- NOT complex. {ECO:0000269|PubMed:23221646}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.20801 0.11262 -0.510624372 21.65015334 251.95312 3.41739 CNOT10-AS1 . . . CNOT10 antisense RNA 1 . . . . . . . . . . . CNOT11 0.993507645349384 0.00649133912635084 1.01552426547214e-06 CCR4-NOT transcription complex subunit 11 FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Is required for the association of CNOT10 with the CCR4-NOT complex. Seems not to be required for complex deadenylase function.; . . . . 0.50975 0.09076 -0.361761279 28.6329323 24.35814 0.80124 CNP 0.890888252106868 0.108880689575611 0.000231058317521353 2',3'-cyclic nucleotide 3' phosphodiesterase FUNCTION: May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin. {ECO:0000250}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;ganglion;frontal lobe;endometrium;thyroid;iris;germinal center;brain;amygdala;heart;cartilage;urinary;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;oesophagus;cerebral cortex;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;kidney;stomach;aorta;thymus; dorsal root ganglion;amygdala;whole brain;thalamus;medulla oblongata;occipital lobe;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.19281 0.22435 -0.424258538 25.56027365 82.50337 1.92854 CNPPD1 1.63494195830923e-05 0.869185627293852 0.130798023286565 cyclin Pas1/PHO80 domain containing 1 . . . myocardium;medulla oblongata;ovary;salivary gland;sympathetic chain;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;oesophagus;synovium;bone;thyroid;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;alveolus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22713 . 1.153790856 92.55720689 3997.83614 12.51118 CNPY1 0.00874565540084683 0.574948300381441 0.416306044217712 canopy FGF signaling regulator 1 . . . breast;brain; subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.07541 . 0.235309407 68.71903751 7.78877 0.28707 CNPY2 0.0300953472407302 0.92447735394832 0.0454272988109501 canopy FGF signaling regulator 2 FUNCTION: Positive regulator of neurite outgrowth by stabilizing myosin regulatory light chain (MRLC). It prevents MIR-mediated MRLC ubiquitination and its subsequent proteasomal degradation.; . TISSUE SPECIFICITY: Expressed in different tissues. Highest levels are detected in adult placenta, liver and pancreas. {ECO:0000269|PubMed:12826659}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;amniotic fluid;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; whole brain;superior cervical ganglion;placenta;pituitary;cingulate cortex;parietal lobe; 0.55438 0.11671 0.014844891 54.94810097 3.58338 0.13028 CNPY3 0.466081200956065 0.528363159690254 0.00555563935368132 canopy FGF signaling regulator 3 FUNCTION: Toll-like receptor (TLR)-specific co-chaperone for HSP90B1. Required for proper TLR folding, except that of TLR3, and hence controls TLR exit from the endoplasmic reticulum. Consequently, required for both innate and adaptive immune responses (By similarity). {ECO:0000250}.; . . . . 0.07071 0.11499 0.03689118 56.64071715 2078.45989 8.39845 CNPY4 3.6762305295632e-09 0.0972202387179529 0.902779757605817 canopy FGF signaling regulator 4 FUNCTION: Plays a role in the regulation of the cell surface expression of TLR4. {ECO:0000269|PubMed:16338228}.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;liver;duodenum;kidney;cerebellum; superior cervical ganglion;subthalamic nucleus;adrenal gland;globus pallidus;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle;cerebellum; 0.12613 0.10572 0.260991686 70.25831564 503.72189 4.60479 CNR1 0.155072221772085 0.776107848886241 0.0688199293416741 cannabinoid receptor 1 (brain) FUNCTION: Involved in cannabinoid-induced CNS effects. Acts by inhibiting adenylate cyclase. Could be a receptor for anandamide. Inhibits L-type Ca(2+) channel current. Isoform 2 and isoform 3 have altered ligand binding. {ECO:0000269|PubMed:15620723}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15620723}.; . . 0.44350 0.20297 -0.957024976 9.088228356 11.91527 0.43204 CNR2 0.00011072577844674 0.370934490737128 0.628954783484425 cannabinoid receptor 2 FUNCTION: Heterotrimeric G protein-coupled receptor for endocannabinoid 2-arachidonoylglycerol mediating inhibition of adenylate cyclase. May function in inflammatory response, nociceptive transmission and bone homeostasis. {ECO:0000269|PubMed:10051546, ECO:0000269|PubMed:12663043, ECO:0000269|PubMed:12711605, ECO:0000269|PubMed:18692962}.; . TISSUE SPECIFICITY: Preferentially expressed in cells of the immune system with higher expression in B-cells and NK cells (at protein level). Expressed in skin in suprabasal layers and hair follicles (at protein level). Highly expressed in tonsil and to a lower extent in spleen, peripheral blood mononuclear cells, and thymus. PubMed:14657172 could not detect expression in normal brain. Expressed in brain by perivascular microglial cells and dorsal root ganglion sensory neurons (at protein level). Two isoforms are produced by alternative promoter usage and differ only in the 5' UTR: isoform CB2A is observed predominantly in testis with some expression in brain, while isoform CB2B is predominant in spleen and leukocytes. {ECO:0000269|PubMed:12153574, ECO:0000269|PubMed:12511587, ECO:0000269|PubMed:14657172, ECO:0000269|PubMed:15266552, ECO:0000269|PubMed:18692962, ECO:0000269|PubMed:19496827, ECO:0000269|PubMed:7556170}.; . . 0.13510 0.45200 0.086440867 60.47416844 101.19462 2.17679 CNRIP1 0.299559964908186 0.623051795491132 0.0773882396006819 cannabinoid receptor interacting protein 1 FUNCTION: Isoform 1 suppresses cannabinoid receptor CNR1-mediated tonic inhibition of voltage-gated calcium channels. Isoform 2 does not have this effect. {ECO:0000269|PubMed:17895407}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;hypothalamus;sympathetic chain;parathyroid;choroid;skin;bone marrow;uterus;pancreas;whole body;lung;frontal lobe;nasopharynx;bone;placenta;visual apparatus;hippocampus;liver;testis;kidney;brain; whole brain;subthalamic nucleus;occipital lobe;globus pallidus;cingulate cortex; 0.52864 0.11262 -0.161524709 41.6430762 35.5523 1.07173 CNST 0.925062821549835 0.074933571347008 3.60710315740182e-06 consortin, connexin sorting protein FUNCTION: Required for targeting of connexins to the plasma membrane. {ECO:0000269|PubMed:19864490}.; . . . . 0.38150 0.08328 0.75875178 86.82472281 410.25255 4.24447 CNTD1 0.0218345110656651 0.962106978674681 0.0160585102596542 cyclin N-terminal domain containing 1 . . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;synovium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;alveolus;liver;head and neck;cervix;kidney;stomach;aorta;thymus; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; 0.10905 . 0.260991686 70.25831564 3023.85578 10.44088 CNTD2 0.114056188535974 0.778249884126257 0.107693927337769 cyclin N-terminal domain containing 2 . . . optic nerve;lung;ovary;colon;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05142 . 0.347360312 73.97381458 47.20632 1.33173 CNTF 0.000349252208597215 0.377251053826765 0.622399693964638 ciliary neurotrophic factor FUNCTION: CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.; . TISSUE SPECIFICITY: Nervous system.; cerebral cortex;nasopharynx;spinal cord;alveolus; . . 0.28128 0.41713504 76.95800896 215.89598 3.17274 CNTFR 0.906207074768488 0.0936367784948437 0.000156146736667991 ciliary neurotrophic factor receptor FUNCTION: Binds to CNTF. The alpha subunit provides the receptor specificity.; . TISSUE SPECIFICITY: Nervous system and skeletal muscle.; unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skeletal muscle;skin;retina;optic nerve;whole body;placenta;macula lutea;visual apparatus;testis;kidney;mammary gland;brain; superior cervical ganglion;pons; 0.44536 0.34537 -0.824740496 11.67728238 37.95207 1.12693 CNTFR-AS1 . . . CNTFR antisense RNA 1 . . . . . . . . . . . CNTLN . . . centlein FUNCTION: Required for centrosome cohesion and recruitment of CEP68 to centrosomes. {ECO:0000269|PubMed:24554434}.; . . unclassifiable (Anatomical System);bone;liver;retina; superior cervical ganglion;ciliary ganglion;pons; 0.20604 0.17905 0.461041847 78.29087049 3754.49948 11.98604 CNTN1 0.999989199613199 1.08003867996182e-05 1.41904661606564e-15 contactin 1 FUNCTION: Contactins mediate cell surface interactions during nervous system development. Involved in the formation of paranodal axo-glial junctions in myelinated peripheral nerves and in the signaling between axons and myelinating glial cells via its association with CNTNAP1. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Interaction with TNR induces a repulsion of neurons and an inhibition of neurite outgrowth (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Strongly expressed in brain and in neuroblastoma and retinoblastoma cell lines. Lower levels of expression in lung, pancreas, kidney and skeletal muscle. {ECO:0000269|PubMed:2026173, ECO:0000269|PubMed:8164510}.; unclassifiable (Anatomical System);amygdala;islets of Langerhans;spinal cord;sympathetic chain;skin;retina;whole body;frontal lobe;hippocampus;visual apparatus;liver;pituitary gland;testis;spleen;brain; dorsal root ganglion;occipital lobe;subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;pons;atrioventricular node;cerebellum; 0.27116 0.35635 -1.063626766 7.484076433 163.39635 2.79078 CNTN2 0.129621135189604 0.870378534055588 3.30754807776125e-07 contactin 2 FUNCTION: In conjunction with another transmembrane protein, CNTNAP2, contributes to the organization of axonal domains at nodes of Ranvier by maintaining voltage-gated potassium channels at the juxtaparanodal region. May be involved in cell adhesion. {ECO:0000269|PubMed:23518707}.; DISEASE: Epilepsy, familial adult myoclonic, 5 (FAME5) [MIM:615400]: A form of cortical myoclonic tremor with epilepsy, a syndrome characterized by cortical myoclonus and variable occurrence of epileptic seizures. Usually, myoclonic tremor is the presenting symptom, characterized by tremulous finger movements and myoclonic jerks of the limbs increased by action and posture. In a minority of patients, seizures are the presenting symptom; both complex partial as well as generalized tonic clonic seizures are described. Some patients exhibit mild cognitive impairment. {ECO:0000269|PubMed:23518707}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);amygdala;ovary;spinal cord;fovea centralis;whole body;optic nerve;nasopharynx;hippocampus;macula lutea;pituitary gland;testis;brain; amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;superior cervical ganglion;hypothalamus;spinal cord;caudate nucleus;subthalamic nucleus;prefrontal cortex;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.39019 0.18821 -0.189246284 39.30761972 2533.66697 9.38949 CNTN3 0.0141417862555819 0.985856031504516 2.18223990180744e-06 contactin 3 FUNCTION: Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: In brain, it is expressed in frontal lobe, occipital lobe, cerebellum and amygdala. {ECO:0000269|PubMed:11013081}.; unclassifiable (Anatomical System);prostate;lung;endometrium;hypothalamus;pituitary gland;kidney;brain;aorta; superior cervical ganglion;atrioventricular node; 0.27019 0.43019 0.316000233 72.80018872 1496.00916 7.19616 CNTN4 0.996606387924368 0.00339361206133643 1.42952331420817e-11 contactin 4 FUNCTION: Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity. May be involved in synaptogenesis.; DISEASE: Note=A chromosomal aberration involving CNTN4 has been found in a boy with characteristic physical features of 3p deletion syndrome (3PDS). Translocation t(3;10)(p26;q26). 3PDS is a rare contiguous gene disorder involving the loss of the telomeric portion of the short arm of chromosome 3 and characterized by developmental delay, growth retardation, and dysmorphic features. {ECO:0000269|PubMed:15106122}.; TISSUE SPECIFICITY: Mainly expressed in brain. Highly expressed in cerebellum and weakly expressed in corpus callosum, caudate nucleus, amygdala and spinal cord. Also expressed in testis, pancreas, thyroid, uterus, small intestine and kidney. Not expressed in skeletal muscle. Isoform 2 is weakly expressed in cerebral cortex. {ECO:0000269|PubMed:11013081, ECO:0000269|PubMed:14571131}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;retina;prostate;whole body;lung;frontal lobe;nasopharynx;bone;placenta;visual apparatus;alveolus;testis;kidney;brain;aorta; dorsal root ganglion;testis - interstitial;subthalamic nucleus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.12484 0.10463 -1.478950235 3.703703704 345.74915 3.94468 CNTN4-AS1 . . . CNTN4 antisense RNA 1 . . . . . . . . . . . CNTN4-AS2 . . . CNTN4 antisense RNA 2 . . . . . . . . . . . CNTN5 0.00135406144303263 0.998643261637962 2.67691900566282e-06 contactin 5 FUNCTION: Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity in the cerebral cortical neurons but not in hippocampal neurons. Probably involved in neuronal activity in the auditory system (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain and kidney and at very low level in placenta. Not expressed in other tissues. In brain, it is highly expressed in the occipital lobe, amygdala, cerebral cortex, frontal lobe, thalamus and temporal lobe. Expressed at moderate level in the cerebellum, substantia nigra, putamen, medulla and hippocampus. Weakly expressed in the spinal cord and caudate nucleus. Weakly or not expressed in the corpus callosum. {ECO:0000269|PubMed:11013081}.; unclassifiable (Anatomical System);cartilage;brain; skeletal muscle; 0.29361 0.20972 -0.080831688 47.22222222 849.40801 5.69596 CNTN6 3.58671135173889e-22 0.00401073846632942 0.995989261533671 contactin 6 FUNCTION: Contactins mediate cell surface interactions during nervous system development. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Involved in motor coordination (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in nervous system. Highly expressed in cerebellum. Expressed at intermediate level in thalamus, subthalamic nucleus. Weakly expressed in corpus callosum, caudate nucleus and spinal cord.; unclassifiable (Anatomical System);uterus;optic nerve;placenta;macula lutea;liver;spleen;fovea centralis;choroid;lens;brain;retina; superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.44656 0.13084 -0.918644703 9.807737674 343.14195 3.92764 CNTNAP1 0.0041087576230276 0.995891241471431 9.05540989562125e-10 contactin associated protein 1 FUNCTION: Seems to play a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibers. Seems to demarcate the paranodal region of the axo-glial junction. In association with contactin may have a role in the signaling between axons and myelinating glial cells.; . TISSUE SPECIFICITY: Predominantly expressed in brain. Weak expression detected in ovary, pancreas, colon, lung, heart, intestine and testis.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;duodenum;hypopharynx;head and neck;cerebellum; amygdala;superior cervical ganglion;subthalamic nucleus;medulla oblongata;thalamus;cerebellum peduncles;prefrontal cortex;pons;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.25092 0.10843 -2.298598009 1.214909177 324.56029 3.83000 CNTNAP2 3.82882607342169e-05 0.999957989653322 3.72208594330327e-06 contactin associated protein-like 2 FUNCTION: May play a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibers. Seems to demarcate the juxtaparanodal region of the axo-glial junction (By similarity). {ECO:0000250}.; DISEASE: Autism 15 (AUTS15) [MIM:612100]: A complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving CNTNAP2 is found in a patient with autism spectrum disorder. Paracentric inversion 46,XY,inv(7)(q11.22;q35). The inversion breakpoints disrupt the genes AUTS2 and CNTNAP2.; TISSUE SPECIFICITY: Predominantly expressed in nervous system. {ECO:0000269|PubMed:10624965}.; unclassifiable (Anatomical System);amygdala;heart;sympathetic chain;colon;blood;fovea centralis;choroid;lens;retina;optic nerve;lung;frontal lobe;macula lutea;testis;kidney;brain; amygdala;whole brain;dorsal root ganglion;superior cervical ganglion;occipital lobe;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.59066 0.10874 -2.24910054 1.29747582 193.23796 3.01430 CNTNAP3 0.0725663655548519 0.927411946952093 2.16874930548644e-05 contactin associated protein-like 3 . . . unclassifiable (Anatomical System);hypothalamus;blood;skin;retina;bone marrow;lung;frontal lobe;cochlea;placenta;bone;visual apparatus;liver;kidney;brain;aorta; . . 0.09431 . . 1921.26515 8.07025 CNTNAP3B . . . contactin associated protein-like 3B . . . unclassifiable (Anatomical System);cartilage;liver;testis;blood;kidney;brain;stomach;retina;bone marrow; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.16981 . . . 8497.62815 19.92471 CNTNAP3P1 . . . contactin associated protein-like 3 pseudogene 1 . . . . . . . . . . . CNTNAP3P2 . . . contactin associated protein-like 3 pseudogene 2 . . . . . . . . . . . CNTNAP3P3 . . . contactin associated protein-like 3 pseudogene 3 . . . . . . . . . . . CNTNAP3P4 . . . contactin associated protein-like 3 pseudogene 4 . . . . . . . . . . . CNTNAP3P5 . . . contactin associated protein-like 3 pseudogene 5 . . . . . . . . . . . CNTNAP3P6 . . . contactin associated protein-like 3 pseudogene 6 . . . . . . . . . . . CNTNAP3P7 . . . contactin associated protein-like 3 pseudogene 7 . . . . . . . . . . . CNTNAP3P8 . . . contactin associated protein-like 3 pseudogene 8 . . . . . . . . . . . CNTNAP3P9 . . . contactin associated protein-like 3 pseudogene 9 . . . . . . . . . . . CNTNAP4 2.3431154940654e-05 0.999939338473767 3.72303712927122e-05 contactin associated protein-like 4 FUNCTION: Presynaptic protein involved in both dopaminergic synaptic transmission and GABAergic system, thereby participating in the structural maturation of inhibitory interneuron synapses. Involved in the dopaminergic synaptic transmission by attenuating dopamine release through a presynaptic mechanism. Also participates in the GABAergic system (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;whole body;frontal lobe;heart;hypothalamus;hippocampus;brain;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.22950 0.09803 -0.229706142 36.37060628 3131.43469 10.65757 CNTNAP5 0.0972729242803616 0.902726965254368 1.10465269894147e-07 contactin associated protein-like 5 FUNCTION: May play a role in the correct development and proper functioning of the peripheral and central nervous system and be involved in cell adhesion and intercellular communication.; . . . . 0.28988 0.10318 -0.986602472 8.645907054 325.79675 3.83698 CNTRL 4.16998709620411e-35 0.217149551796364 0.782850448203636 centriolin FUNCTION: Involved in cell cycle progression and cytokinesis. During the late steps of cytokinesis, anchors exocyst and SNARE complexes at the midbody, thereby allowing secretory vesicle- mediated abscission. {ECO:0000269|PubMed:12732615, ECO:0000269|PubMed:16213214}.; . TISSUE SPECIFICITY: Highly expressed in testis and trachea. {ECO:0000269|PubMed:10688839}.; lymphoreticular;ovary;colon;fovea centralis;choroid;retina;bone marrow;uterus;optic nerve;bone;testis;germinal center;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;aorta;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;cerebellum peduncles;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.09284 0.10978 -0.079243514 47.22811984 5189.22799 14.83113 CNTROB 1.23732873376122e-11 0.979262512297534 0.0207374876900928 centrobin, centrosomal BRCA2 interacting protein FUNCTION: Required for centriole duplication. Inhibition of centriole duplication leading to defects in cytokinesis. {ECO:0000269|PubMed:16275750}.; . TISSUE SPECIFICITY: Widely expressed (at protein level). Highly expressed in testis. Also expressed in spleen, thymus, prostate, small intestine, colon and peripheral blood leukocytes. {ECO:0000269|PubMed:16275750}.; . . 0.09488 0.10426 -0.014692675 52.35314933 596.04077 4.94057 COA1 0.0384625323456856 0.837462918165919 0.124074549488395 cytochrome c oxidase assembly factor 1 homolog FUNCTION: Component of some MITRAC complex, a cytochrome c oxidase (COX) assembly intermediate complex that regulates COX assembly. MITRAC complexes regulate both translation of mitochondrial encoded components and assembly of nuclear-encoded components imported in mitochondrion. Required for assembly of mitochondrial respiratory chain complex I and complex IV. {ECO:0000269|PubMed:23260140}.; . . . . 0.03844 . -0.229483771 36.86010852 7.99359 0.29372 COA3 0.00470837762889433 0.683255585195548 0.312036037175558 cytochrome c oxidase assembly factor 3 FUNCTION: Component of some MITRAC complex, a cytochrome c oxidase (COX) assembly intermediate complex that regulates COX assembly. MITRAC complexes regulate both translation of mitochondrial encoded components and assembly of nuclear-encoded components imported in mitochondrion. Required for efficient translation of MT-CO1 and mitochondrial respiratory chain complex IV assembly. {ECO:0000269|PubMed:23260140}.; . . . . 0.36777 0.09294 -0.075159878 47.78839349 5.09282 0.18879 COA4 0.000586606150848862 0.281769196304242 0.717644197544909 cytochrome c oxidase assembly factor 4 homolog FUNCTION: Putative COX assembly factor. {ECO:0000250}.; . . . . 0.00937 0.02934 0.501689326 79.7888653 33.38278 1.03071 COA5 0.239646156062635 0.644552102205814 0.115801741731551 cytochrome c oxidase assembly factor 5 FUNCTION: Involved in an early step of the mitochondrial complex IV assembly process. {ECO:0000269|PubMed:21457908}.; DISEASE: Cardioencephalomyopathy, fatal infantile, due to cytochrome c oxidase deficiency 3 (CEMCOX3) [MIM:616500]: An infantile disorder with a fatal course in the first weeks of life, characterized by hypertrophic cardiomyopathy and mitochondrial complex IV deficiency. Postmortem microscopic investigations show accumulation of lipid droplets in cardiomyocytes and mitochondrial proliferation. {ECO:0000269|PubMed:21457908}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;lung;adrenal gland;nasopharynx;placenta;liver;spleen;head and neck;kidney;aorta;stomach;cerebellum; . 0.11810 . 0.057118534 57.99716914 4.99352 0.18509 COA6 0.0885473096033926 0.763572524009225 0.147880166387382 cytochrome c oxidase assembly factor 6 FUNCTION: Involved in the maturation of the mitochondrial respiratory chain complex IV subunit MT-CO2/COX2. Thereby, may regulate early steps of complex IV assembly. Mitochondrial respiratory chain complex IV or cytochrome c oxidase is the component of the respiratory chain that catalyzes the transfer of electrons from intermembrane space cytochrome c to molecular oxygen in the matrix and as a consequence contributes to the proton gradient involved in mitochondrial ATP synthesis. May also be required for efficient formation of respiratory supercomplexes comprised of complexes III and IV. {ECO:0000269|PubMed:24549041, ECO:0000269|PubMed:25959673, ECO:0000269|PubMed:26160915}.; DISEASE: Cardioencephalomyopathy, fatal infantile, due to cytochrome c oxidase deficiency 4 (CEMCOX4) [MIM:616501]: An infantile disorder with a fatal course in the first weeks of life, characterized by hypertrophic cardiomyopathy, left ventricular non-compaction, lactic acidosis, metabolic hypotonia, and mitochondrial complex IV deficiency. {ECO:0000269|PubMed:24549041, ECO:0000269|PubMed:25339201}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.05896 . 0.369407109 74.95281906 27.52947 0.88700 COA7 . . . cytochrome c oxidase assembly factor 7 (putative) FUNCTION: Required for assembly of mitochondrial respiratory chain complex I and complex IV. {ECO:0000269|PubMed:24333015}.; . . . . 0.36474 . 0.237127192 68.98443029 1776.73562 7.78373 COASY 1.04516297649836e-07 0.769470408550515 0.230529486933187 Coenzyme A synthase FUNCTION: Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation. {ECO:0000269|PubMed:11923312}.; . TISSUE SPECIFICITY: Expressed in all tissues examined including brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocyte. Lowest expression in peripheral blood leukocytes and highest in kidney and liver. Isoform 2 is expressed mainly in the brain. {ECO:0000269|PubMed:11923312}.; . . 0.02146 0.10351 -0.709045403 14.673272 104.38113 2.20880 COBL 0.982698636920497 0.0173013442464696 1.88330334507055e-08 cordon-bleu WH2 repeat protein FUNCTION: Plays an important role in the reorganization of the actin cytoskeleton. Regulates neuron morphogenesis and increases branching of axons and dendrites. Regulates dendrite branching in Purkinje cells (By similarity). Binds to and sequesters actin monomers (G actin). Nucleates actin polymerization by assembling three actin monomers in cross-filament orientation and thereby promotes growth of actin filaments at the barbed end. Can also mediate actin depolymerization at barbed ends and severing of actin filaments. Promotes formation of cell ruffles. {ECO:0000250, ECO:0000269|PubMed:21816349}.; . . ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;cerebral cortex;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;cerebellum; amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.36124 0.11214 0.554715755 81.55225289 758.96902 5.45703 COBLL1 0.0121973641922403 0.987736418600746 6.62172070134117e-05 cordon-bleu WH2 repeat protein like 1 . . . lymphoreticular;ovary;sympathetic chain;colon;parathyroid;skin;retina;uterus;prostate;endometrium;larynx;thyroid;testis;dura mater;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);meninges;lymph node;heart;lacrimal gland;pancreas;pia mater;lung;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;placenta;globus pallidus;appendix;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;parietal lobe;skeletal muscle; 0.60988 0.08604 0.409650696 76.53927813 2197.61027 8.63190 COCH 0.000262849456488043 0.983542807336405 0.0161943432071074 cochlin FUNCTION: Plays a role in the control of cell shape and motility in the trabecular meshwork. {ECO:0000269|PubMed:21886777}.; DISEASE: Deafness, autosomal dominant, 9 (DFNA9) [MIM:601369]: A form of non-syndromic hearing loss characterized by onset in the fourth or fifth decade of life and initially involves the high frequencies. Hearing loss is progressive and usually complete by the sixth decade. In addition to cochlear involvement, DFNA9 patients also exhibit a spectrum of vestibular dysfunctions. Penetrance of the vestibular symptoms is often incomplete, and some patients are minimally affected, whereas others suffer from severe balance disturbances and episodes of vertigo. Affected individuals have mucopolysaccharide depositions in the channels of the cochlear and vestibular nerves. These depositions apparently cause strangulation and degeneration of dendritic fibers. {ECO:0000269|PubMed:10400989, ECO:0000269|PubMed:11295836, ECO:0000269|PubMed:14512963, ECO:0000269|PubMed:16835921, ECO:0000269|PubMed:17561763, ECO:0000269|PubMed:18312449, ECO:0000269|PubMed:22610276, ECO:0000269|PubMed:22931125, ECO:0000269|PubMed:23993205, ECO:0000269|PubMed:9806553, ECO:0000269|PubMed:9931344}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in inner ear structures; the cochlea and the vestibule.; unclassifiable (Anatomical System);cartilage;ovary;hypothalamus;colon;parathyroid;retina;prostate;lung;cochlea;adrenal gland;larynx;trabecular meshwork;placenta;visual apparatus;liver;testis;head and neck;spleen;kidney;brain;stomach; pons;caudate nucleus; 0.53303 0.13199 0.286674996 71.49681529 2772.50763 9.93783 COD2 . . . cone dystrophy 2 (X-linked) . . . . . . . . . . . COG1 0.10252799642341 0.897459815028055 1.21885485349058e-05 component of oligomeric golgi complex 1 FUNCTION: Required for normal Golgi function. {ECO:0000250}.; DISEASE: Congenital disorder of glycosylation 2G (CDG2G) [MIM:611209]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. Clinical features of CDG2G include failure to thrive, generalized hypotonia, growth retardation and mild psychomotor retardation. CDG2G is biochemically characterized by a defect in O-glycosylation as well as N-glycosylation. {ECO:0000269|PubMed:16537452}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; . 0.16361 0.13388 0.031219447 55.84453881 476.66447 4.51093 COG2 0.000167564985575961 0.999566073643871 0.000266361370553116 component of oligomeric golgi complex 2 FUNCTION: Required for normal Golgi morphology and function.; . . . . 0.14368 0.25108 -0.33061537 30.82094834 941.66479 5.94881 COG3 0.999142795814268 0.000857204125513347 6.02191601578081e-11 component of oligomeric golgi complex 3 FUNCTION: Involved in ER-Golgi transport. {ECO:0000269|PubMed:11929878}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in pancreas and testis and lowest levels in lung. {ECO:0000269|PubMed:11292827}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney; pancreas;prostate; 0.25804 0.11876 -0.26629572 34.81953291 302.945 3.70940 COG4 4.38858303424531e-06 0.997966813753685 0.00202879766328127 component of oligomeric golgi complex 4 FUNCTION: Required for normal Golgi function. Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1. {ECO:0000269|PubMed:19536132}.; DISEASE: Congenital disorder of glycosylation 2J (CDG2J) [MIM:613489]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:19494034}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;tonsil;heart;cartilage;tongue;pineal body;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach; skeletal muscle; 0.26914 0.11324 -0.995664936 8.539749941 119.45307 2.37823 COG5 1.13576699864644e-11 0.904490337504118 0.0955096624845241 component of oligomeric golgi complex 5 FUNCTION: Required for normal Golgi function. {ECO:0000250}.; DISEASE: Congenital disorder of glycosylation 2I (CDG2I) [MIM:613612]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. Congenital disorder of glycosylation type 2I is characterized by mild neurological impairments. {ECO:0000269|PubMed:19690088}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;thyroid;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pineal body;blood;bile duct;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.69254 0.10021 -0.016511957 52.31776362 860.42254 5.72159 COG6 6.7206281668635e-10 0.857273886369144 0.142726112958793 component of oligomeric golgi complex 6 FUNCTION: Required for normal Golgi function. {ECO:0000250}.; DISEASE: Congenital disorder of glycosylation 2L (CDG2L) [MIM:614576]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. Clinical features of CDG2L include neonatal intractable focal seizures, vomiting, loss of consciousness, intracranial bleeding due to vitamin K deficiency, and death in infancy. {ECO:0000269|PubMed:20605848}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Shaheen syndrome (SHNS) [MIM:615328]: An autosomal recessive form of syndromic mental retardation. Affected individuals show severe intellectual disability, hypohidrosis, dental enamel hypoplasia, and hyperkeratosis of the palms and soles. Some may develop mild microcephaly. {ECO:0000269|PubMed:23606727}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;uterus;prostate;whole body;bone;thyroid;testis;germinal center;brain;pineal gland;spinal ganglion;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;adrenal cortex;lens;skeletal muscle;bile duct;lung;adrenal gland;placenta;visual apparatus;hippocampus;alveolus;liver;cervix;head and neck;kidney;stomach;aorta; superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.17793 0.10516 0.624649618 83.53385232 8807.1494 20.24153 COG7 1.28698924936735e-06 0.997611504691113 0.00238720831963722 component of oligomeric golgi complex 7 FUNCTION: Required for normal Golgi function. {ECO:0000250}.; DISEASE: Congenital disorder of glycosylation 2E (CDG2E) [MIM:608779]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:15107842}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;skin;retina;prostate;optic nerve;whole body;cochlea;cerebral cortex;endometrium;larynx;thyroid;pituitary gland;brain;bladder;unclassifiable (Anatomical System);lymph node;tongue;adrenal cortex;pharynx;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve;cerebellum; hypothalamus;parietal lobe; 0.13523 0.10171 -1.238203625 5.490681765 622.19044 5.02873 COG8 1.87304071695129e-05 0.693345213341349 0.306636056251482 component of oligomeric golgi complex 8 FUNCTION: Required for normal Golgi function. {ECO:0000250}.; DISEASE: Congenital disorder of glycosylation 2H (CDG2H) [MIM:611182]: CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:17331980}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;skin;retina;uterus;prostate;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.28449 0.10981 -0.222203495 37.54423213 266.21683 3.50111 COIL 0.0156002339592544 0.978907412258847 0.00549235378189898 coilin FUNCTION: Component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs. {ECO:0000269|PubMed:7679389}.; . TISSUE SPECIFICITY: Found in all the cell types examined.; ovary;colon;parathyroid;uterus;prostate;whole body;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;kidney;stomach; testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;cingulate cortex;skeletal muscle; 0.34771 0.12844 -0.356299879 29.31115829 639.36833 5.08637 COILP1 . . . coilin pseudogene 1 . . . . . . . . . . . COILP2 . . . coilin pseudogene 2 . . . . . . . . . . . COL1A1 0.999999998983348 1.01665205171818e-09 2.2115287069838e-25 collagen type I alpha 1 FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen).; DISEASE: Caffey disease (CAFFD) [MIM:114000]: Characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age. {ECO:0000269|PubMed:15864348}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ehlers-Danlos syndrome, classic type (EDS) [MIM:130000]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. {ECO:0000269|PubMed:10739762, ECO:0000269|PubMed:17211858}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ehlers-Danlos syndrome 7A (EDS7A) [MIM:130060]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. Marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteogenesis imperfecta 1 (OI1) [MIM:166200]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI1 is a non-deforming form with normal height or mild short stature, and no dentinogenesis imperfecta. {ECO:0000269|PubMed:1634225, ECO:0000269|PubMed:16638323, ECO:0000269|PubMed:16705691, ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:1718984, ECO:0000269|PubMed:1737847, ECO:0000269|PubMed:17875077, ECO:0000269|PubMed:18670065, ECO:0000269|PubMed:24682174, ECO:0000269|PubMed:2794057, ECO:0000269|PubMed:3244312, ECO:0000269|PubMed:8223589}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteogenesis imperfecta 2 (OI2) [MIM:166210]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI2 is characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. {ECO:0000269|PubMed:10627137, ECO:0000269|PubMed:1460047, ECO:0000269|PubMed:1511982, ECO:0000269|PubMed:1613761, ECO:0000269|PubMed:16566045, ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:18670065, ECO:0000269|PubMed:1874719, ECO:0000269|PubMed:18996919, ECO:0000269|PubMed:1939261, ECO:0000269|PubMed:1953667, ECO:0000269|PubMed:2035536, ECO:0000269|PubMed:2036375, ECO:0000269|PubMed:2037280, ECO:0000269|PubMed:2116413, ECO:0000269|PubMed:2211725, ECO:0000269|PubMed:2339700, ECO:0000269|PubMed:2470760, ECO:0000269|PubMed:25958000, ECO:0000269|PubMed:2777764, ECO:0000269|PubMed:2794057, ECO:0000269|PubMed:2913053, ECO:0000269|PubMed:3016737, ECO:0000269|PubMed:3108247, ECO:0000269|PubMed:3403550, ECO:0000269|PubMed:3667599, ECO:0000269|PubMed:7520724, ECO:0000269|PubMed:7679635, ECO:0000269|PubMed:7691343, ECO:0000269|PubMed:7961597, ECO:0000269|PubMed:8100209, ECO:0000269|PubMed:8349697, ECO:0000269|PubMed:8349698, ECO:0000269|PubMed:8364588, ECO:0000269|PubMed:8456808, ECO:0000269|PubMed:8786074, ECO:0000269|PubMed:9143923, ECO:0000269|Ref.47, ECO:0000269|Ref.50}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteogenesis imperfecta 3 (OI3) [MIM:259420]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI3 is characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera and dentinogenesis imperfecta. {ECO:0000269|PubMed:10408781, ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:1770532, ECO:0000269|PubMed:18670065, ECO:0000269|PubMed:2037280, ECO:0000269|PubMed:2511192, ECO:0000269|PubMed:2794057, ECO:0000269|PubMed:7691343, ECO:0000269|PubMed:7881420, ECO:0000269|PubMed:8019571, ECO:0000269|PubMed:8364588, ECO:0000269|PubMed:8456809, ECO:0000269|PubMed:8669434, ECO:0000269|PubMed:8723681, ECO:0000269|PubMed:9101304}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteogenesis imperfecta 4 (OI4) [MIM:166220]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI4 is characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. {ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:1770532, ECO:0000269|PubMed:17875077, ECO:0000269|PubMed:1988452, ECO:0000269|PubMed:2745420, ECO:0000269|PubMed:7691343, ECO:0000269|PubMed:7982948, ECO:0000269|PubMed:8094076, ECO:0000269|PubMed:8339541, ECO:0000269|PubMed:9600458}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal disorder characterized by decreased bone mass and deterioration of bone microarchitecture without alteration in the composition of bone. The result is fragile bones and an increased risk of fractures, even after minimal trauma. Osteoporosis is a chronic condition of multifactorial etiology and is usually clinically silent until a fracture occurs. {ECO:0000269|PubMed:8841196, ECO:0000269|PubMed:9535665}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF.; TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.; smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;cochlea;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;dura mater;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; uterus;superior cervical ganglion;uterus corpus;smooth muscle;adipose tissue;heart;placenta;fetal lung;atrioventricular node;fetal thyroid; 0.99194 0.99087 -1.785892633 2.25878745 137.3096 2.54895 COL1A2 0.99975494444276 0.000245055557239053 9.66401519419966e-16 collagen type I alpha 2 FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen).; DISEASE: Ehlers-Danlos syndrome 7B (EDS7B) [MIM:130060]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. Marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations. {ECO:0000269|PubMed:1577745, ECO:0000269|PubMed:2394758, ECO:0000269|PubMed:3680255}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteogenesis imperfecta 1 (OI1) [MIM:166200]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI1 is a non-deforming form with normal height or mild short stature, and no dentinogenesis imperfecta. {ECO:0000269|PubMed:16705691, ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:1990009, ECO:0000269|PubMed:8456807, ECO:0000269|PubMed:8829649}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteogenesis imperfecta 2 (OI2) [MIM:166210]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI2 is characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. {ECO:0000269|PubMed:10627137, ECO:0000269|PubMed:1284475, ECO:0000269|PubMed:1339453, ECO:0000269|PubMed:1385413, ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:1874719, ECO:0000269|PubMed:18996919, ECO:0000269|PubMed:2777764, ECO:0000269|PubMed:2914942, ECO:0000269|PubMed:7693712, ECO:0000269|PubMed:7891382, ECO:0000269|PubMed:7906591, ECO:0000269|PubMed:7959683, ECO:0000269|PubMed:8182080, ECO:0000269|Ref.33}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ehlers-Danlos syndrome, autosomal recessive, cardiac valvular form (EDSCV) [MIM:225320]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. In addition to joint laxity, skin hyperextensibility and friability, and abnormal scar formation, patients have mitral valve prolapse and insufficiency, mitral regurgitation, and aortic insufficiency. {ECO:0000269|PubMed:16816023}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteogenesis imperfecta 3 (OI3) [MIM:259420]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI3 is characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera and dentinogenesis imperfecta. {ECO:0000269|PubMed:10408781, ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:1990009, ECO:0000269|PubMed:7520724, ECO:0000269|PubMed:7720740, ECO:0000269|PubMed:7749416, ECO:0000269|PubMed:7860070, ECO:0000269|PubMed:7881420, ECO:0000269|PubMed:8081394, ECO:0000269|PubMed:8444468, ECO:0000269|PubMed:8456807, ECO:0000269|PubMed:8723681, ECO:0000269|PubMed:8800927, ECO:0000269|PubMed:8829649}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteogenesis imperfecta 4 (OI4) [MIM:166220]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI4 is characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. {ECO:0000269|PubMed:1642148, ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:2052622, ECO:0000269|PubMed:2064612, ECO:0000269|PubMed:2897363, ECO:0000269|PubMed:7693712, ECO:0000269|PubMed:8094076, ECO:0000269|PubMed:8401517, ECO:0000269|PubMed:8800927}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving COL1A2 may be a cause of lipoblastomas, which are benign tumors resulting from transformation of adipocytes, usually diagnosed in children. Translocation t(7;8)(p22;q13) with PLAG1.; TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.; unclassifiable (Anatomical System);smooth muscle;heart;ovary;colon;skeletal muscle;retina;breast;uterus;whole body;lung;bone;thyroid;placenta;visual apparatus;testis;head and neck;kidney;brain;mammary gland;bladder;stomach;peripheral nerve; uterus;uterus corpus;superior cervical ganglion;adipose tissue;smooth muscle;heart;placenta;testis;fetal lung;ciliary ganglion;fetal thyroid;trigeminal ganglion; 0.99859 . -1.144569759 6.363529134 161.91131 2.78024 COL1AR . . . collagen type I alpha receptor . . . . . . . . . . . COL2A1 0.999999986012304 1.39876958109356e-08 2.65555275785157e-23 collagen type II alpha 1 FUNCTION: Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.; DISEASE: Spondyloepiphyseal dysplasia congenital type (SEDC) [MIM:183900]: Disorder characterized by disproportionate short stature and pleiotropic involvement of the skeletal and ocular systems. {ECO:0000269|PubMed:10678662, ECO:0000269|PubMed:11746045, ECO:0000269|PubMed:2339128, ECO:0000269|PubMed:2543071, ECO:0000269|PubMed:7757086, ECO:0000269|PubMed:8019561, ECO:0000269|PubMed:8325895, ECO:0000269|PubMed:8423604}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spondyloepimetaphyseal dysplasia, Strudwick type (SEMDSTWK) [MIM:184250]: A bone disease characterized by disproportionate short stature from birth, with a very short trunk and shortened limbs, and skeletal abnormalities including lordosis, scoliosis, flattened vertebrae, pectus carinatum, coxa vara, clubfoot, and abnormal epiphyses or metaphyses. A distinctive radiographic feature is irregular sclerotic changes, described as dappled in the metaphyses of the long bones. {ECO:0000269|PubMed:16088915, ECO:0000269|PubMed:7550321, ECO:0000269|Ref.38}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Achondrogenesis 2 (ACG2) [MIM:200610]: A disease characterized by the absence of ossification in the vertebral column, sacrum and pubic bones. {ECO:0000269|PubMed:10745044, ECO:0000269|PubMed:10797431, ECO:0000269|PubMed:17994563, ECO:0000269|PubMed:2572591, ECO:0000269|PubMed:7757081, ECO:0000269|PubMed:7757086, ECO:0000269|PubMed:7829510}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Legg-Calve-Perthes disease (LCPD) [MIM:150600]: Characterized by loss of circulation to the femoral head, resulting in avascular necrosis in a growing child. Clinical pictures of the disease vary, depending on the phase of disease progression through ischemia, revascularization, fracture and collapse, and repair and remodeling of the bone. {ECO:0000269|PubMed:17394019}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Kniest dysplasia (KD) [MIM:156550]: Moderately severe chondrodysplasia phenotype that results from mutations in the COL2A1 gene. Characteristics of the disorder include a short trunk and extremities, mid-face hypoplasia, cleft palate, myopia, retinal detachment, and hearing loss. {ECO:0000269|PubMed:7874117, ECO:0000269|PubMed:8863156}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Avascular necrosis of the femoral head, primary (ANFH) [MIM:608805]: A disease characterized by mechanical failure of the subchondral bone, and degeneration of the hip joint. It usually leads to destruction of the hip joint in the third to fifth decade of life. The clinical manifestations, such as pain on exertion, a limping gait, and a discrepancy in leg length, cause considerable disability. {ECO:0000269|PubMed:15930420}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteoarthritis with mild chondrodysplasia (OSCDP) [MIM:604864]: Osteoarthritis is a common disease that produces joint pain and stiffness together with radiologic evidence of progressive degeneration of joint cartilage. {ECO:0000269|PubMed:1975693, ECO:0000269|PubMed:1985108, ECO:0000269|PubMed:7757086, ECO:0000269|PubMed:8507190}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Platyspondylic lethal skeletal dysplasia Torrance type (PLSD-T) [MIM:151210]: Platyspondylic lethal skeletal dysplasias (PLSDs) are a heterogeneous group of chondrodysplasias characterized by severe platyspondyly and limb shortening. PLSD-T is characterized by varying platyspondyly, short ribs with anterior cupping, hypoplasia of the lower ilia with broad ischial and pubic bones, and shortening of the tubular bones with splayed and cupped metaphyses. Histology of the growth plate typically shows focal hypercellularity with slightly enlarged chondrocytes in the resting cartilage and relatively well-preserved columnar formation and ossification at the chondro-osseous junction. PLSD-T is generally a perinatally lethal disease, but a few long-term survivors have been reported. {ECO:0000269|PubMed:10745044, ECO:0000269|PubMed:14729840, ECO:0000269|PubMed:15643621}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multiple epiphyseal dysplasia with myopia and conductive deafness (EDMMD) [MIM:132450]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. EDMMD is an autosomal dominant disorder characterized by epiphyseal dysplasia associated with progressive myopia, retinal thinning, crenated cataracts, conductive deafness. {ECO:0000269|PubMed:9800905}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spondyloperipheral dysplasia (SPD) [MIM:271700]: SPD patients manifest short stature, midface hypoplasia, sensorineural hearing loss, spondyloepiphyseal dysplasia, platyspondyly and brachydactyly. {ECO:0000269|PubMed:15316962}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Stickler syndrome 1 (STL1) [MIM:108300]: An autosomal dominant form of Stickler syndrome, an inherited disorder that associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular disorders may include juvenile cataract, myopia, strabismus, vitreoretinal or chorioretinal degeneration, retinal detachment, and chronic uveitis. Pierre Robin sequence includes an opening in the roof of the mouth (a cleft palate), a large tongue (macroglossia), and a small lower jaw (micrognathia). Bones are affected by slight platyspondylisis and large, often defective epiphyses. Juvenile joint laxity is followed by early signs of arthrosis. The degree of hearing loss varies among affected individuals and may become more severe over time. Syndrome expressivity is variable. {ECO:0000269|PubMed:11007540, ECO:0000269|PubMed:20513134, ECO:0000269|PubMed:7977371}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Stickler syndrome 1 non-syndromic ocular (STL1O) [MIM:609508]: An autosomal dominant form of Stickler syndrome characterized by the ocular signs typically seen in Stickler syndrome type 1 such as cataract, myopia, retinal detachment. Systemic features of premature osteoarthritis, cleft palate, hearing impairment, and craniofacial abnormalities are either absent or very mild. {ECO:0000269|PubMed:16752401, ECO:0000269|PubMed:17721977, ECO:0000269|PubMed:8317498}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Rhegmatogenous retinal detachment autosomal dominant (DRRD) [MIM:609508]: A eye disease that most frequently results from a break or tear in the retina that allows fluid from the vitreous humor to enter the potential space beneath the retina. It is often associated with pathologic myopia and in most cases leads to visual impairment or blindness if untreated. {ECO:0000269|PubMed:11007540, ECO:0000269|PubMed:15671297}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Czech dysplasia (CZECHD) [MIM:609162]: A skeletal dysplasia characterized by early-onset, progressive pseudorheumatoid arthritis, platyspondyly, and short third and fourth toes. {ECO:0000269|PubMed:18553548, ECO:0000269|PubMed:19764028, ECO:0000269|PubMed:7757086, ECO:0000269|PubMed:8244341}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 2 is highly expressed in juvenile chondrocyte and low in fetal chondrocyte. {ECO:0000269|PubMed:2355003}.; ovary;fovea centralis;choroid;retina;optic nerve;whole body;cochlea;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;muscle;adrenal cortex;pharynx;lens;breast;lung;epididymis;placenta;hippocampus;visual apparatus;macula lutea;liver;spleen;kidney;mammary gland; dorsal root ganglion;fetal liver;superior cervical ganglion;uterus corpus;trachea;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.96554 0.92693 -1.804354835 2.205708894 2337.43468 8.95474 COL3A1 0.999999998393609 1.60639142495558e-09 1.36374140409695e-25 collagen type III alpha 1 FUNCTION: Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of GPR56 in the developing brain and binding to GPR56 inhibits neuronal migration and activates the RhoA pathway by coupling GPR56 to GNA13 and possibly GNA12.; DISEASE: Ehlers-Danlos syndrome 3 (EDS3) [MIM:130020]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. It is a form of Ehlers-Danlos syndrome characterized by marked joint hyperextensibility without skeletal deformity. {ECO:0000269|PubMed:7833919}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ehlers-Danlos syndrome 4 (EDS4) [MIM:130050]: The most severe form of Ehlers-Danlos syndrome, a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. Characterized by the joint and dermal manifestations as in other forms of the syndrome, characteristic facial features (acrogeria) in most patients, and by proneness to spontaneous rupture of bowel and large arteries. The vascular complications may affect all anatomical areas. {ECO:0000269|PubMed:10706896, ECO:0000269|PubMed:10923041, ECO:0000269|PubMed:11168790, ECO:0000269|PubMed:12694234, ECO:0000269|PubMed:12786757, ECO:0000269|PubMed:1352273, ECO:0000269|PubMed:1357232, ECO:0000269|PubMed:1370809, ECO:0000269|PubMed:1496983, ECO:0000269|PubMed:1895316, ECO:0000269|PubMed:2492273, ECO:0000269|PubMed:2808425, ECO:0000269|PubMed:7749417, ECO:0000269|PubMed:7912131, ECO:0000269|PubMed:8019562, ECO:0000269|PubMed:8098182, ECO:0000269|PubMed:8411057, ECO:0000269|PubMed:8664902, ECO:0000269|PubMed:8680408, ECO:0000269|PubMed:8884076, ECO:0000269|PubMed:8990011, ECO:0000269|PubMed:9036918, ECO:0000269|PubMed:9147870, ECO:0000269|PubMed:9452103, ECO:0000269|Ref.46, ECO:0000269|Ref.51}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Aortic aneurysm, familial abdominal (AAA) [MIM:100070]: A common multifactorial disorder characterized by permanent dilation of the abdominal aorta, usually due to degenerative changes in the aortic wall. Histologically, AAA is characterized by signs of chronic inflammation, destructive remodeling of the extracellular matrix, and depletion of vascular smooth muscle cells. {ECO:0000269|PubMed:2243125, ECO:0000269|PubMed:2349939, ECO:0000269|PubMed:8514866}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . medulla oblongata;smooth muscle;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;testis;amniotic fluid;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;urinary;muscle;spinal cord;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; uterus;uterus corpus;superior cervical ganglion;fetal liver;smooth muscle;adipose tissue;heart;placenta;appendix;fetal lung;ciliary ganglion;fetal thyroid; 0.99739 0.87801 -0.233339999 36.34111819 2256.82813 8.77689 COL4A1 0.99999998123739 1.87626098743128e-08 1.09882639661377e-23 collagen type IV alpha 1 FUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.; DISEASE: Brain small vessel disease with or without ocular anomalies (BSVD) [MIM:607595]: An autosomal dominant disease characterized by weakening of the blood vessels in the brain and retinal arteriolar tortuosity. In affected individuals, stroke is often the first symptom and is usually caused by bleeding in the brain (hemorrhagic stroke) rather than a lack of blood flow in the brain (ischemic stroke). Patients also have leukoencephalopathy and may experience seizures and migraine headaches accompanied by visual sensations known as auras. {ECO:0000269|PubMed:16598045, ECO:0000269|PubMed:17379824, ECO:0000269|PubMed:17696175, ECO:0000269|PubMed:19477666, ECO:0000269|PubMed:20385946, ECO:0000269|PubMed:22574627, ECO:0000269|PubMed:23394911, ECO:0000269|PubMed:24628545}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hereditary angiopathy with nephropathy aneurysms and muscle cramps (HANAC) [MIM:611773]: The clinical renal manifestations include hematuria and bilateral large cysts. Histologic analysis revealed complex basement membrane defects in kidney and skin. The systemic angiopathy appears to affect both small vessels and large arteries. {ECO:0000269|PubMed:18160688, ECO:0000269|PubMed:20818663}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Porencephaly 1 (POREN1) [MIM:175780]: A neurologic disorder characterized by a fluid-filled cysts or cavities within the cerebral hemispheres, neurologic manifestations, facial paresis, and visual defects. Affected individuals typically have hemiplegia, seizures, and intellectual disability. Porencephaly type 1 is usually unilateral and results from focal destructive lesions such as fetal vascular occlusion or birth trauma. {ECO:0000269|PubMed:15905400, ECO:0000269|PubMed:16107487, ECO:0000269|PubMed:19194877}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Intracerebral hemorrhage (ICH) [MIM:614519]: A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke. {ECO:0000269|PubMed:22522439}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Tortuosity of retinal arteries (RATOR) [MIM:180000]: A disease characterized by marked tortuosity of second- and third- order retinal arteries with normal first-order arteries and venous system. Most patients manifest variable degrees of symptomatic transient vision loss due to retinal hemorrhage following minor stress or trauma. {ECO:0000269|PubMed:25228067}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Schizencephaly (SCHZC) [MIM:269160]: Extremely rare human congenital disorder characterized by a full-thickness cleft within the cerebral hemispheres. These clefts are lined with gray matter and most commonly involve the parasylvian regions. Large portions of the cerebral hemispheres may be absent and replaced by cerebro- spinal fluid. {ECO:0000269|PubMed:23225343}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in placenta. {ECO:0000269|PubMed:10811134, ECO:0000269|PubMed:16481288}.; . . 0.85262 0.49245 -2.824541933 0.619249823 4320.3445 13.08601 COL4A2 2.10928692329967e-06 0.999997874307765 1.64053114849808e-08 collagen type IV alpha 2 FUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.; DISEASE: Porencephaly 2 (POREN2) [MIM:614483]: A neurologic disorder characterized by a fluid-filled cysts or cavities within the cerebral hemispheres. Affected individuals typically have hemiplegia, seizures, and intellectual disability. Porencephaly type 2, or schizencephalic porencephaly, is usually symmetric and represents a primary defect in the development of the cerebral ventricles. {ECO:0000269|PubMed:22209246}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Intracerebral hemorrhage (ICH) [MIM:614519]: A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke. {ECO:0000269|PubMed:22209247}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . myocardium;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;urinary;adrenal cortex;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum; dorsal root ganglion;superior cervical ganglion;adipose tissue;heart;placenta;globus pallidus;fetal lung;ciliary ganglion;atrioventricular node;fetal thyroid;trigeminal ganglion;skeletal muscle;skin; 0.26795 . -0.643198486 16.53102147 2430.98324 9.15844 COL4A2-AS1 . . . COL4A2 antisense RNA 1 . . . . . . . . . . . COL4A2-AS2 . . . COL4A2 antisense RNA 2 . . . . . . . . . . . COL4A3 7.57550007722727e-05 0.999924244525307 4.73920603265086e-10 collagen type IV alpha 3 FUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.; DISEASE: Note=Autoantibodies against the NC1 domain of alpha 3(IV) are found in Goodpasture syndrome, an autoimmune disease of lung and kidney.; DISEASE: Alport syndrome, autosomal recessive (APSAR) [MIM:203780]: A syndrome characterized by progressive glomerulonephritis, glomerular basement membrane defects, renal failure, sensorineural deafness and specific eye abnormalities (lenticonous and macular flecks). The disorder shows considerable heterogeneity in that families differ in the age of end-stage renal disease and the occurrence of deafness. {ECO:0000269|PubMed:11134255, ECO:0000269|PubMed:15954103}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hematuria, benign familial (BFH) [MIM:141200]: An autosomal dominant condition characterized by non-progressive isolated microscopic hematuria that does not result in renal failure. It is characterized pathologically by thinning of the glomerular basement membrane. {ECO:0000269|PubMed:11961012}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Alport syndrome, autosomal dominant (APSAD) [MIM:104200]: A syndrome characterized by progressive glomerulonephritis, glomerular basement membrane defects, renal failure, sensorineural deafness and specific eye abnormalities (lenticonous and macular flecks). The disorder shows considerable heterogeneity in that families differ in the age of end-stage renal disease and the occurrence of deafness. {ECO:0000269|PubMed:11044206, ECO:0000269|PubMed:11134255}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Alpha 3 and alpha 4 type IV collagens are colocalized and present in kidney, eye, basement membranes of lens capsule, cochlea, lung, skeletal muscle, aorta, synaptic fibers, fetal kidney and fetal lung. PubMed:8083201 reports similar levels of expression of alpha 3 and alpha 4 type IV collagens in kidney, but PubMed:7523402 reports that in kidney levels of alpha 3 type IV collagen are significantly lower than those of alpha 4 type IV collagen. According to PubMed:8083201, alpha 3 type IV collagen is not detected in heart, brain, placenta, liver, pancreas, extrasynaptic muscle fibers, endoneurial and perineurial nerves, fetal brain, fetal heart and fetal liver. According to PubMed:7523402, alpha 3 type IV collagen is strongly expressed in pancreas, neuroretina and calvaria and not expressed in adrenal, ileum and skin. Isoform 1 and isoform 3 are strongly expressed in kidney, lung, suprarenal capsule, muscle and spleen, in each of these tissues isoform 1 is more abundant than isoform 3. Isoform 1 and isoform 3 are expressed at low levels in artery, fat, pericardium and peripherical nerve, but not in placenta, mesangium, skin, pleura and cultured umbilical endothelial cells. {ECO:0000269|PubMed:7523402, ECO:0000269|PubMed:8083201, ECO:0000269|PubMed:8505332}.; unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;choroid;fovea centralis;lens;skeletal muscle;retina;optic nerve;macula lutea;liver;testis;spleen;brain; superior cervical ganglion;kidney;trigeminal ganglion;skeletal muscle; 0.29220 0.33981 1.350293882 94.31469686 5517.171 15.33170 COL4A3BP 0.979474243191344 0.0205257281171203 2.86915358866761e-08 collagen type IV alpha 3 binding protein FUNCTION: Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner. {ECO:0000269|PubMed:14685229, ECO:0000269|PubMed:17591919, ECO:0000269|PubMed:18184806, ECO:0000269|PubMed:20036255}.; DISEASE: Mental retardation, autosomal dominant 34 (MRD34) [MIM:616351]: A form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:25533962}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed.; unclassifiable (Anatomical System);medulla oblongata;heart;colon;parathyroid;blood;fovea centralis;skin;skeletal muscle;retina;breast;uterus;pancreas;prostate;whole body;lung;frontal lobe;placenta;bone;thyroid;macula lutea;visual apparatus;testis;germinal center;kidney;brain;stomach; amygdala;testis - interstitial;occipital lobe;prefrontal cortex;skeletal muscle;parietal lobe; 0.23233 0.09621 -0.60427181 17.74593064 94.06557 2.08575 COL4A4 1.68977859995688e-08 0.999999295867498 6.87234715642658e-07 collagen type IV alpha 4 FUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.; DISEASE: Alport syndrome, autosomal recessive (APSAR) [MIM:203780]: A syndrome characterized by progressive glomerulonephritis, glomerular basement membrane defects, renal failure, sensorineural deafness and specific eye abnormalities (lenticonous and macular flecks). The disorder shows considerable heterogeneity in that families differ in the age of end-stage renal disease and the occurrence of deafness. {ECO:0000269|PubMed:7987396, ECO:0000269|PubMed:9792860}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hematuria, benign familial (BFH) [MIM:141200]: An autosomal dominant condition characterized by non-progressive isolated microscopic hematuria that does not result in renal failure. It is characterized pathologically by thinning of the glomerular basement membrane. {ECO:0000269|PubMed:11961012, ECO:0000269|PubMed:12631110, ECO:0000269|PubMed:8787673}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Alpha 3 and alpha 4 type IV collagens are colocalized and present in kidney, eye, basement membranes of lens capsule, cochlea, lung, skeletal muscle, aorta, synaptic fibers, fetal kidney and fetal lung. PubMed:8083201 reports similar levels of expression of alpha 3 and alpha 4 type IV collagens in kidney, but PubMed:7523402 reports that in kidney levels of alpha 3 type IV collagen are significantly lower than those of alpha 4 type IV collagen. Highest levels of expression of alpha 4 type IV collagen are detected in kidney, calvaria, neuroretina and cardiac muscle. Lower levels of expression are observed in brain, lung and thymus, and no expression is detected in choroid plexus, liver, adrenal, pancreas, ileum or skin. {ECO:0000269|PubMed:7523402, ECO:0000269|PubMed:8083201}.; unclassifiable (Anatomical System);pancreas;lung;nasopharynx;macula lutea;visual apparatus;pituitary gland;liver;spleen;blood;fovea centralis;kidney;germinal center; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;medulla oblongata;appendix;globus pallidus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.09807 0.24901 1.041609675 91.26562869 4900.23196 14.26220 COL4A5 0.999918348283007 8.16517169853827e-05 8.01978082453147e-15 collagen type IV alpha 5 FUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.; DISEASE: Alport syndrome, X-linked (APSX) [MIM:301050]: A syndrome that is characterized by progressive glomerulonephritis, renal failure, sensorineural deafness, specific eye abnormalities (lenticonous and macular flecks), and glomerular basement membrane defects. The disorder shows considerable heterogeneity in that families differ in the age of end-stage renal disease and the occurrence of deafness. {ECO:0000269|PubMed:10094548, ECO:0000269|PubMed:10561141, ECO:0000269|PubMed:10563487, ECO:0000269|PubMed:10684360, ECO:0000269|PubMed:10862091, ECO:0000269|PubMed:11004279, ECO:0000269|PubMed:11223851, ECO:0000269|PubMed:1352287, ECO:0000269|PubMed:1363780, ECO:0000269|PubMed:1376965, ECO:0000269|PubMed:1672282, ECO:0000269|PubMed:24522658, ECO:0000269|PubMed:7599631, ECO:0000269|PubMed:7853788, ECO:0000269|PubMed:8406498, ECO:0000269|PubMed:8651292, ECO:0000269|PubMed:8651296, ECO:0000269|PubMed:8829632, ECO:0000269|PubMed:8940267, ECO:0000269|PubMed:9150741, ECO:0000269|PubMed:9452056, ECO:0000269|PubMed:9848783}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Deletions covering the N-terminal regions of COL4A5 and COL4A6, which are localized in a head-to-head manner, are found in the chromosome Xq22.3 centromeric deletion syndrome. This results in a phenotype with features of diffuse leiomyomatosis and Alport syndrome (DL-ATS).; TISSUE SPECIFICITY: Isoform 2 is found in kidney.; fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;pituitary gland;testis;amniotic fluid;bladder;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;urinary;lens;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;kidney;mammary gland;stomach;aorta;thymus; uterus;superior cervical ganglion;uterus corpus;spinal cord;parietal lobe; 0.87803 . -1.148192153 6.316348195 776.06095 5.51594 COL4A6 0.990988266205785 0.00901173378784683 6.36863722656426e-12 collagen type IV alpha 6 FUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.; DISEASE: Note=Deletions covering the N-terminal regions of COL4A5 and COL4A6, which are localized in a head-to-head manner, are found in the chromosome Xq22.3 centromeric deletion syndrome. This results in a phenotype with features of diffuse leiomyomatosis and Alport syndrome (DL-ATS).; DISEASE: Deafness, X-linked, 6 (DFNX6) [MIM:300914]: A non- syndromic form of sensorineural hearing loss with prelingual onset. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:23714752}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;prostate;optic nerve;whole body;lung;endometrium;macula lutea;visual apparatus;testis;cervix;brain;mammary gland;stomach; dorsal root ganglion;thalamus;uterus corpus;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14684 0.07461 0.36555769 74.7287096 361.2174 4.02247 COL5A1 0.999999999999752 2.48389711769055e-13 8.5941255414674e-33 collagen type V alpha 1 FUNCTION: Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin.; DISEASE: Ehlers-Danlos syndrome, classic type (EDS) [MIM:130000]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. {ECO:0000269|PubMed:10602121, ECO:0000269|PubMed:11992482, ECO:0000269|PubMed:15580559, ECO:0000269|PubMed:18972565, ECO:0000269|PubMed:9042913}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;synovium;larynx;bone;testis;amniotic fluid;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;lens;breast;pancreas;lung;epididymis;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; uterus;adipose tissue;smooth muscle;heart;placenta;fetal lung;ciliary ganglion;atrioventricular node; 0.69297 . -3.009169053 0.524887945 863.84203 5.72906 COL5A1-AS1 . . . COL5A1 antisense RNA 1 . . . . . 0.09600 . . . . . COL5A2 0.999999999884353 1.15647220666227e-10 5.48388499037232e-27 collagen type V alpha 2 FUNCTION: Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue- specific matrices (By similarity). {ECO:0000250}.; DISEASE: Ehlers-Danlos syndrome, classic type (EDS) [MIM:130000]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. {ECO:0000269|PubMed:9425231, ECO:0000269|PubMed:9783710}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.46242 0.39055 -0.872736979 10.59212078 660.02289 5.15132 COL5A3 7.11903366992312e-07 0.999999288070164 2.64693941213878e-11 collagen type V alpha 3 FUNCTION: Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin.; . . unclassifiable (Anatomical System);medulla oblongata;cartilage;heart;ovary;muscle;urinary;colon;parathyroid;choroid;skin;retina;whole body;lung;adrenal gland;bone;placenta;liver;testis;spleen;kidney;spinal ganglion;brain;mammary gland; amygdala;dorsal root ganglion;subthalamic nucleus;occipital lobe;superior cervical ganglion;adipose tissue;prefrontal cortex;globus pallidus;pons;caudate nucleus;cingulate cortex; 0.45391 . 0.135796279 63.57631517 15615.64674 27.11541 COL6A1 0.999994534766207 5.46523379289367e-06 2.7002296650166e-16 collagen type VI alpha 1 FUNCTION: Collagen VI acts as a cell-binding protein.; DISEASE: Bethlem myopathy 1 (BTHLM1) [MIM:158810]: A benign proximal myopathy characterized by early childhood onset and joint contractures most frequently affecting the elbows and ankles. {ECO:0000269|PubMed:11865138, ECO:0000269|PubMed:15689448, ECO:0000269|PubMed:15955946, ECO:0000269|PubMed:8782832}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ullrich congenital muscular dystrophy 1 (UCMD1) [MIM:254090]: A congenital myopathy characterized by muscle weakness and multiple joint contractures, generally noted at birth or early infancy. The clinical course is more severe than in Bethlem myopathy. {ECO:0000269|PubMed:15689448, ECO:0000269|PubMed:16130093}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;choroid;skin;retina;uterus;prostate;endometrium;larynx;bone;thyroid;testis;amniotic fluid;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;mesenchyma;epididymis;trabecular meshwork;placenta;visual apparatus;amnion;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; superior cervical ganglion;adipose tissue;smooth muscle;heart;pons;atrioventricular node;uterus;subthalamic nucleus;thyroid;placenta;appendix;globus pallidus;ciliary ganglion;fetal lung;trigeminal ganglion;cingulate cortex; 0.64130 0.53998 -1.486612255 3.621137061 4373.32252 13.19585 COL6A2 0.00213375739441823 0.997859369904797 6.87270078477367e-06 collagen type VI alpha 2 FUNCTION: Collagen VI acts as a cell-binding protein.; DISEASE: Bethlem myopathy 1 (BTHLM1) [MIM:158810]: A benign proximal myopathy characterized by early childhood onset and joint contractures most frequently affecting the elbows and ankles. {ECO:0000269|PubMed:11865138, ECO:0000269|PubMed:15689448, ECO:0000269|PubMed:17886299, ECO:0000269|PubMed:8782832}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ullrich congenital muscular dystrophy 1 (UCMD1) [MIM:254090]: A congenital myopathy characterized by muscle weakness and multiple joint contractures, generally noted at birth or early infancy. The clinical course is more severe than in Bethlem myopathy. {ECO:0000269|PubMed:15563506, ECO:0000269|PubMed:15689448}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myosclerosis autosomal recessive (MYOSAR) [MIM:255600]: A condition characterized by chronic inflammation of skeletal muscle with hyperplasia of the interstitial connective tissue. The clinical picture includes slender muscles with firm 'woody' consistency and restriction of movement of many joints because of muscle contractures. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;salivary gland;colon;skin;retina;uterus;prostate;endometrium;cerebral cortex;thyroid;bone;iris;testis;spinal ganglion;bladder;brain;unclassifiable (Anatomical System);tongue;urinary;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;smooth muscle;adipose tissue;caudate nucleus;atrioventricular node;pons;skeletal muscle;uterus;uterus corpus;subthalamic nucleus;placenta;globus pallidus;ciliary ganglion;kidney; 0.50744 0.37851 -1.001964775 8.221278603 5707.29483 15.65413 COL6A3 7.79330849282056e-11 0.999999999743307 1.78759937059759e-10 collagen type VI alpha 3 FUNCTION: Collagen VI acts as a cell-binding protein.; DISEASE: Bethlem myopathy 1 (BTHLM1) [MIM:158810]: A benign proximal myopathy characterized by early childhood onset and joint contractures most frequently affecting the elbows and ankles. {ECO:0000269|PubMed:10399756, ECO:0000269|PubMed:15689448, ECO:0000269|PubMed:17886299, ECO:0000269|PubMed:9536084}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ullrich congenital muscular dystrophy 1 (UCMD1) [MIM:254090]: A congenital myopathy characterized by muscle weakness and multiple joint contractures, generally noted at birth or early infancy. The clinical course is more severe than in Bethlem myopathy. {ECO:0000269|PubMed:15689448}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dystonia 27 (DYT27) [MIM:616411]: A form of dystonia, a disorder defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. DYT27 is an autosomal recessive form characterized by segmental isolated dystonia involving the face, neck, bulbar muscles, and upper limbs. {ECO:0000269|PubMed:26004199}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;colon;skin;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;thyroid;bone;testis;amniotic fluid;brain;gall bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; uterus;uterus corpus;smooth muscle;adipose tissue;heart;placenta;testis;appendix;fetal lung;atrioventricular node;fetal thyroid; 0.93588 0.40359 -2.550505158 0.861052135 5032.39412 14.49340 COL6A4P1 . . . collagen type VI alpha 4 pseudogene 1 . . . . . . . . . . . COL6A4P2 . . . collagen type VI alpha 4 pseudogene 2 . . . . . . . . . . . COL6A5 9.56358791513705e-12 0.0411502140271574 0.958849785963279 collagen type VI alpha 5 FUNCTION: Collagen VI acts as a cell-binding protein. {ECO:0000250}.; DISEASE: Note=Patients affected by atopic dermatitis display an abnormal distribution of COL29A1 mRNA and protein in skin suggesting that COL29A1 may be involved in the pathogenesis of the disease.; TISSUE SPECIFICITY: Expressed in skin, followed by lung, small intestine, colon and testis. In skin, it is expressed in the epidermis with strongest staining in suprabasal viable layers. In ATOD patients, it is absent in the most differentiated upper spinous and granular layers (at protein level). {ECO:0000269|PubMed:17850181}.; unclassifiable (Anatomical System);cartilage;ovary;thyroid;placenta;parathyroid; dorsal root ganglion;superior cervical ganglion;adipose tissue;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.06307 . . 13360.06109 24.98933 COL6A6 3.59168701863295e-45 1.45442790475401e-07 0.99999985455721 collagen type VI alpha 6 FUNCTION: Collagen VI acts as a cell-binding protein. {ECO:0000250}.; . . . . . . -0.671084654 15.4222694 5102.99637 14.65250 COL7A1 2.10611122198023e-18 1 4.89243750008085e-19 collagen type VII alpha 1 FUNCTION: Stratified squamous epithelial basement membrane protein that forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence by interacting with extracellular matrix (ECM) proteins such as type IV collagen.; DISEASE: Note=Epidermolysis bullosa acquisita (EBA) is an autoimmune acquired blistering skin disease resulting from autoantibodies to type VII collagen.; DISEASE: Epidermolysis bullosa dystrophica, autosomal dominant (DDEB) [MIM:131750]: A group of autosomal dominant blistering skin diseases characterized by tissue separation which occurs below the dermal-epidermal basement membrane at the level of the anchoring fibrils. Various clinical types with different severity are recognized, ranging from severe mutilating forms to mild forms with limited and localized scarring, and less frequent extracutaneous manifestations. {ECO:0000269|PubMed:10084325, ECO:0000269|PubMed:10232406, ECO:0000269|PubMed:10232407, ECO:0000269|PubMed:10232408, ECO:0000269|PubMed:10836608, ECO:0000269|PubMed:11142768, ECO:0000269|PubMed:20598510, ECO:0000269|PubMed:7861014, ECO:0000269|PubMed:9215684, ECO:0000269|PubMed:9668111, ECO:0000269|PubMed:9740253, ECO:0000269|PubMed:9856843}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa dystrophica, autosomal recessive (RDEB) [MIM:226600]: A group of autosomal recessive blistering skin diseases characterized by tissue separation which occurs below the dermal-epidermal basement membrane at the level of the anchoring fibrils. Various clinical types with different severity are recognized, ranging from severe mutilating forms to mild forms with limited and localized scarring, and less frequent extracutaneous manifestations. Mild forms include epidermolysis bullosa mitis and epidermolysis bullosa localisata. {ECO:0000269|PubMed:10084325, ECO:0000269|PubMed:10620140, ECO:0000269|PubMed:11167698, ECO:0000269|PubMed:20598510, ECO:0000269|PubMed:8618018, ECO:0000269|PubMed:8757758, ECO:0000269|PubMed:9215684, ECO:0000269|PubMed:9444387, ECO:0000269|PubMed:9740253, ECO:0000269|PubMed:9804332}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa dystrophica, Pasini type (P-DEB) [MIM:131750]: A severe, dominantly inherited form of dystrophic epidermolysis bullosa characterized by albopapuloid Pasini papule, dorsal extremity blistering, milia formation and red atrophic scarring after recurrent blisters. {ECO:0000269|PubMed:10233777, ECO:0000269|PubMed:8170945}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa dystrophica, Hallopeau-Siemens type (HS-DEB) [MIM:226600]: The most severe recessive form of dystrophic epidermolysis bullosa. It manifests with mutilating scarring, joint contractures, corneal erosions, esophagus structures, and propensity to formation of cutaneous squamous cell carcinomas leading to premature demise of the affected individuals. {ECO:0000269|PubMed:10084325, ECO:0000269|PubMed:8513326, ECO:0000269|PubMed:8592061, ECO:0000269|PubMed:9326325, ECO:0000269|PubMed:9740253}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Transient bullous dermolysis of the newborn (TBDN) [MIM:131705]: TBDN is a neonatal form of dystrophic epidermolysis bullosa characterized by sub-epidermal blisters, reduced or abnormal anchoring fibrils at the dermo-epidermal junction, and electron-dense inclusions in keratinocytes. TBDN heals spontaneously or strongly improves within the first months and years of life. {ECO:0000269|PubMed:9856844}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa dystrophica, pretibial type (PR- DEB) [MIM:131850]: A form of dystrophic epidermolysis bullosa characterized by pretibial blisters that develop into prurigo-like hyperkeratotic lesions. It predominantly affects the pretibial areas, sparing the knees and other parts of the skin. Other clinical features include nail dystrophy, albopapuloid skin lesions, and hypertrophic scars without pretibial predominance. The phenotype shows considerable interindividual variability. Inheritance is autosomal dominant. {ECO:0000269|PubMed:8541842}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa dystrophica, Bart type (B-DEB) [MIM:132000]: An autosomal dominant form of dystrophic epidermolysis bullosa characterized by congenital localized absence of skin, skin fragility and deformity of nails. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa pruriginosa (EBP) [MIM:604129]: A distinct clinical subtype of epidermolysis bullosa dystrophica. It is characterized by skin fragility, blistering, scar formation, intense pruritus and excoriated prurigo nodules. Onset is in early childhood, but in some cases is delayed until the second or third decade of life. Inheritance can be autosomal dominant or recessive. {ECO:0000269|PubMed:10383749, ECO:0000269|PubMed:11142768}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Nail disorder, non-syndromic congenital, 8 (NDNC8) [MIM:607523]: A nail disorder characterized by isolated toenail dystrophy. The nail changes are most severe in the great toes and consist of the nail plate being buried in the nail bed with a deformed and narrow free edge. {ECO:0000269|PubMed:11843659}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa dystrophica, with subcorneal cleavage (EBDSC) [MIM:131750]: A bullous skin disorder with variable sized clefts just beneath the level of the stratum corneum. Clinical features include blisters, milia, atrophic scarring, nail dystrophy, and oral and conjunctival involvement, as seen in dystrophic epidermolysis bullosa. {ECO:0000269|PubMed:11874498, ECO:0000269|PubMed:2653224}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;larynx;testis;bladder;unclassifiable (Anatomical System);amygdala;heart;cartilage;tongue;urinary;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney; trigeminal ganglion;cingulate cortex;skin; 0.14584 0.25273 -4.236423245 0.129747582 892.33092 5.82224 COL8A1 0.0381673646294114 0.929138491754513 0.032694143616076 collagen type VIII alpha 1 FUNCTION: Macromolecular component of the subendothelium. Major component of the Descemet's membrane (basement membrane) of corneal endothelial cells. Also component of the endothelia of blood vessels. Necessary for migration and proliferation of vascular smooth muscle cells and thus, has a potential role in the maintenance of vessel wall integrity and structure, in particular in atherogenesis. {ECO:0000269|PubMed:11708810}.; . TISSUE SPECIFICITY: Expressed primarily in the subendothelium of large blood vessels. Also expressed in arterioles and venules in muscle, heart, kidney, spleen, umbilical cord, liver and lung and is also found in connective tissue layers around hair follicles, around nerve bundles in muscle, in the dura of the optic nerve, in cornea and sclera, and in the perichondrium of cartilaginous tissues. In the kidney, expressed in mesangial cells, glomerular endothelial cells, and tubular epithelial cells. Also expressed in mast cells, and in astrocytes during the repair process. Expressed in Descemet's membrane. Specifically expressed in peritoneal fibroblasts and mesothelial cells. {ECO:0000269|PubMed:10686422, ECO:0000269|PubMed:2376131, ECO:0000269|PubMed:7734329}.; unclassifiable (Anatomical System);heart;ovary;cartilage;urinary;colon;skin;skeletal muscle;bone marrow;uterus;lung;cochlea;bone;visual apparatus;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.43053 0.17306 -1.464150033 3.780372729 50.21273 1.39189 COL8A2 0.699343492871063 0.296890914121518 0.00376559300741876 collagen type VIII alpha 2 FUNCTION: Macromolecular component of the subendothelium. Major component of the Descemet's membrane (basement membrane) of corneal endothelial cells. Also component of the endothelia of blood vessels. Necessary for migration and proliferation of vascular smooth muscle cells and thus, has a potential role in the maintenance of vessel wall integrity and structure, in particular in atherogenesis (By similarity). {ECO:0000250}.; DISEASE: Corneal dystrophy, Fuchs endothelial, 1 (FECD1) [MIM:136800]: A corneal disease caused by loss of endothelium of the central cornea. It is characterized by focal wart-like guttata that arise from Descemet membrane and develop in the central cornea, epithelial blisters, reduced vision and pain. Descemet membrane is thickened by abnormal collagenous deposition. {ECO:0000269|PubMed:11689488}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, posterior polymorphous, 2 (PPCD2) [MIM:609140]: A rare mild subtype of posterior corneal dystrophy characterized by alterations of Descemet membrane presenting as vesicles, opacities or band-like lesions on slit-lamp examination and specular microscopy. Affected patient typically are asymptomatic. {ECO:0000269|PubMed:11689488}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed primarily in the subendothelium of large blood vessels. Also expressed in arterioles and venules in muscle, heart, kidney, spleen, umbilical cord, liver and lung and is also found in connective tissue layers around hair follicles, around nerve bundles in muscle, in the dura of the optic nerve, in cornea and sclera, and in the perichondrium of cartilaginous tissues. In the kidney, expressed in mesangial cells, glomerular endothelial cells, and tubular epithelial cells. Also expressed in mast cells, and in astrocytes during the repair process. Expressed in Descemet's membrane. {ECO:0000269|PubMed:10686422, ECO:0000269|PubMed:17888087}.; ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;thyroid;bone;testis;unclassifiable (Anatomical System);amygdala;heart;cartilage;urinary;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;spleen;kidney; superior cervical ganglion;olfactory bulb;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.55358 0.18510 . . 722.29291 5.33397 COL9A1 4.77422931673328e-15 0.977172691861338 0.0228273081386574 collagen type IX alpha 1 FUNCTION: Structural component of hyaline cartilage and vitreous of the eye.; DISEASE: Multiple epiphyseal dysplasia 6 (EDM6) [MIM:614135]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal. {ECO:0000269|PubMed:11565064}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Stickler syndrome 4 (STL4) [MIM:614134]: An autosomal recessive form of Stickler syndrome, an inherited disorder that associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular disorders may include juvenile cataract, myopia, strabismus, vitreoretinal or chorioretinal degeneration, retinal detachment, and chronic uveitis. Pierre Robin sequence includes an opening in the roof of the mouth (a cleft palate), a large tongue (macroglossia), and a small lower jaw (micrognathia). Bones are affected by slight platyspondylisis and large, often defective epiphyses. Juvenile joint laxity is followed by early signs of arthrosis. The degree of hearing loss varies among affected individuals and may become more severe over time. Syndrome expressivity is variable. {ECO:0000269|PubMed:16909383}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;whole body;optic nerve;endometrium;cochlea;bone;amniotic fluid;middle ear;bladder;brain;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;spinal cord;lens;lung;placenta;internal ear;visual apparatus;macula lutea;head and neck;kidney;mammary gland; superior cervical ganglion;hypothalamus;ciliary ganglion;caudate nucleus;trigeminal ganglion;skeletal muscle;cingulate cortex;skin; 0.49846 0.17535 -0.856118029 10.95777306 7049.10534 17.93014 COL9A2 0.182801205838876 0.817194565040543 4.22912058107295e-06 collagen type IX alpha 2 FUNCTION: Structural component of hyaline cartilage and vitreous of the eye.; DISEASE: Multiple epiphyseal dysplasia 2 (EDM2) [MIM:600204]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal. {ECO:0000269|PubMed:10364514}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Intervertebral disc disease (IDD) [MIM:603932]: A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain. {ECO:0000269|PubMed:10411504}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Stickler syndrome 5 (STL5) [MIM:614284]: An autosomal recessive form of Stickler syndrome, an inherited disorder that associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. STL5 is characterized by high myopia, vitreoretinal degeneration, retinal detachment, mild to moderate sensorineural hearing loss, short stature in childhood, and absence of cleft palate and Pierre Robin sequence. {ECO:0000269|PubMed:21671392}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.10977 0.16297 1.690270544 96.40835103 4219.57468 12.92194 COL9A3 3.24916588705806e-05 0.999944224954322 2.32833868068383e-05 collagen type IX alpha 3 FUNCTION: Structural component of hyaline cartilage and vitreous of the eye.; DISEASE: Multiple epiphyseal dysplasia 3 (EDM3) [MIM:600969]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal. {ECO:0000269|PubMed:10090888}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Intervertebral disc disease (IDD) [MIM:603932]: A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain. {ECO:0000269|PubMed:11308397, ECO:0000269|PubMed:25381065}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Susceptibility to intervertebral disk disease is conferred by variant p.Arg103Trp (PubMed:11308397). {ECO:0000269|PubMed:11308397}.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;endometrium;thyroid;bone;testis;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;head and neck;kidney;stomach; olfactory bulb;hypothalamus;thyroid;spinal cord;caudate nucleus; 0.49770 . 0.611719262 82.96768106 2646.06911 9.64989 COL10A1 6.35839564298384e-05 0.716270969068816 0.283665446974754 collagen type X alpha 1 FUNCTION: Type X collagen is a product of hypertrophic chondrocytes and has been localized to presumptive mineralization zones of hyaline cartilage.; DISEASE: Schmid type metaphyseal chondrodysplasia (SMCD) [MIM:156500]: Dominantly inherited disorder of the osseous skeleton. The cardinal features of the phenotype are mild short stature, coxa vara and a waddling gait. Radiography usually shows sclerosis of the ribs, flaring of the metaphyses, and a wide irregular growth plate, especially of the knees. A variant form of SMCD is spondylometaphyseal dysplasia Japanese type. It is characterized by spinal involvement comprising mild platyspondyly, vertebral body abnormalities, and end-plate irregularity. {ECO:0000269|PubMed:15880705, ECO:0000269|PubMed:7607655, ECO:0000269|PubMed:7876225, ECO:0000269|PubMed:8004099, ECO:0000269|PubMed:8304336, ECO:0000269|PubMed:8782043, ECO:0000269|PubMed:9067753, ECO:0000269|PubMed:9852679}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);smooth muscle;cartilage;colon;blood;retina;bone marrow;pancreas;lung;larynx;bone;visual apparatus;liver;testis;spleen;head and neck;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06187 0.36607 -0.020150552 52.25288983 4256.65546 12.96567 COL11A1 0.999980608468386 1.93915316141051e-05 6.79260867159636e-22 collagen type XI alpha 1 FUNCTION: May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.; DISEASE: Stickler syndrome 2 (STL2) [MIM:604841]: An autosomal dominant form of Stickler syndrome, an inherited disorder that associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular disorders may include juvenile cataract, myopia, strabismus, vitreoretinal or chorioretinal degeneration, retinal detachment, and chronic uveitis. Pierre Robin sequence includes an opening in the roof of the mouth (a cleft palate), a large tongue (macroglossia), and a small lower jaw (micrognathia). Bones are affected by slight platyspondylisis and large, often defective epiphyses. Juvenile joint laxity is followed by early signs of arthrosis. The degree of hearing loss varies among affected individuals and may become more severe over time. Syndrome expressivity is variable. {ECO:0000269|PubMed:20513134, ECO:0000269|PubMed:8872475}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Marshall syndrome (MRSHS) [MIM:154780]: An autosomal dominant disorder characterized by ocular abnormalities, deafness, craniofacial anomalies, and anhidrotic ectodermal dysplasia. Clinical features include short stature; flat or retruded midface with short, depressed nose, flat nasal bridge and anteverted nares; cleft palate with or without the Pierre Robin sequence; appearance of large eyes with ocular hypertelorism; cataracts, either congenital or juvenile; esotropia; high myopia; sensorineural hearing loss; spondyloepiphyseal abnormalities; calcification of the falx cerebri; ectodermal abnormalities, including defects in sweating and dental structures. {ECO:0000269|PubMed:10486316}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Fibrochondrogenesis 1 (FBCG1) [MIM:228520]: A severe short-limbed skeletal dysplasia characterized by broad long-bone metaphyses, pear-shaped vertebral bodies, and characteristic morphology of the growth plate, in which the chondrocytes have a fibroblastic appearance and there are regions of fibrous cartilage extracellular matrix. Clinical features include a flat midface with a small nose and anteverted nares, significant shortening of all limb segments but relatively normal hands and feet, and a small bell-shaped thorax with a protuberant abdomen. {ECO:0000269|PubMed:21035103}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Cartilage, placenta and some tumor or virally transformed cell lines. Isoforms using exon IIA or IIB are found in the cartilage while isoforms using only exon IIB are found in the tendon.; unclassifiable (Anatomical System);cartilage;heart;tongue;adrenal cortex;colon;skin;skeletal muscle;retina;bone marrow;breast;uterus;pancreas;whole body;lung;cochlea;larynx;bone;placenta;visual apparatus;testis;head and neck;brain;mammary gland;stomach; amygdala;superior cervical ganglion;adipose tissue;trachea;fetal brain;prefrontal cortex;ciliary ganglion;skeletal muscle;parietal lobe; 0.35429 0.34658 -0.360177779 28.64472753 7076.86232 18.07025 COL11A2 0.999999324603711 6.75396288947378e-07 9.42681387571073e-25 collagen type XI alpha 2 FUNCTION: May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.; DISEASE: Stickler syndrome 3 (STL3) [MIM:184840]: An autosomal dominant non-ocular form of Stickler syndrome. Classical Stickler syndrome associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular symptoms are absent. Pierre Robin sequence includes an opening in the roof of the mouth (a cleft palate), a large tongue (macroglossia), and a small lower jaw (micrognathia). Bones are affected by slight platyspondylisis and large, often defective epiphyses. Juvenile joint laxity is followed by early signs of arthrosis. The degree of hearing loss varies among affected individuals and may become more severe over time. Syndrome expressivity is variable. {ECO:0000269|PubMed:9506662}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Otospondylomegaepiphyseal dysplasia (OSMED) [MIM:215150]: A skeletal dysplasia characterized by enlarged epiphyses, disproportionate shortness of the limbs, abnormalities in vertebral bodies, and sensorineural hearing loss. Patients have typical facial features, including mid-face hypoplasia with a short upturned nose and depressed nasal bridge. Cleft palate and a small mandible are also common findings. {ECO:0000269|PubMed:7859284}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Weissenbacher-Zweymueller syndrome (WZS) [MIM:277610]: An autosomal dominant disorder characterized by neonatal micrognathia and rhizomelic chondrodysplasia with dumbbell-shaped femora and humeri, and regression of bone changes and normal growth in later years. WZS is also referred to as heterozygous OSMED. {ECO:0000269|PubMed:9805126}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal dominant, 13 (DFNA13) [MIM:601868]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:10581026}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal recessive, 53 (DFNB53) [MIM:609706]: A form of non-syndromic sensorineural deafness characterized by prelingual, profound, non-progressive hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:16033917, ECO:0000269|PubMed:25633957}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Fibrochondrogenesis 2 (FBCG2) [MIM:614524]: A severe skeletal dysplasia characterized by a flat midface, short long bones, short ribs with broad metaphyses, and vertebral bodies that show distinctive hypoplastic posterior ends and rounded anterior ends, giving the vertebral bodies a pinched appearance on lateral radiographic views. The chest is small, causing perinatal respiratory problems which usually, but not always, result in lethality. Affected individuals who survive the neonatal period have high myopia, mild to moderate hearing loss, and severe skeletal dysplasia. {ECO:0000269|PubMed:22246659}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;heart;ovary;adrenal cortex;colon;parathyroid;fovea centralis;choroid;lens;retina;uterus;optic nerve;whole body;lung;frontal lobe;cochlea;nasopharynx;bone;placenta;macula lutea;testis;head and neck;brain; . 0.13696 . -1.052752328 7.619721632 4503.08544 13.47830 COL11A2P1 . . . collagen type XI alpha 2 pseudogene 1 . . . . . . . . . . . COL12A1 0.999999611399328 3.88600671497958e-07 8.31932542843415e-29 collagen type XII alpha 1 FUNCTION: Type XII collagen interacts with type I collagen- containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix. {ECO:0000250}.; DISEASE: Ullrich congenital muscular dystrophy 2 (UCMD2) [MIM:616470]: A form of Ullrich muscular dystrophy, a congenital myopathy characterized by muscle weakness and multiple joint contractures, generally noted at birth or early infancy. The clinical course is more severe than in Bethlem myopathy. {ECO:0000269|PubMed:24334604}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bethlem myopathy 2 (BTHLM2) [MIM:616471]: A form of Bethlem myopathy, a benign proximal myopathy characterized by early childhood onset and joint contractures most frequently affecting the elbows and ankles. {ECO:0000269|PubMed:24334604, ECO:0000269|PubMed:24334769}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in collagen I-containing tissues: both isoform 1 and isoform 2 appear in amnion, chorion, skeletal muscle, small intestine, and in cell culture of dermal fibroblasts, keratinocytes and endothelial cells. Only isoform 2 is found in lung, placenta, kidney and a squamous cell carcinoma cell line. Isoform 1 is also present in the corneal epithelial Bowman's membrane (BM) and the interfibrillar matrix of the corneal stroma, but it is not detected in the limbal BM. {ECO:0000269|PubMed:9344363}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;endometrium;oesophagus;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pharynx;blood;breast;pancreas;lung;cornea;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;adipose tissue;ciliary ganglion;atrioventricular node; 0.92484 0.14383 -1.625040811 2.88393489 1491.01427 7.18337 COL13A1 0.0039289675922385 0.996068184403554 2.84800420771284e-06 collagen type XIII alpha 1 FUNCTION: Involved in cell-matrix and cell-cell adhesion interactions that are required for normal development. May participate in the linkage between muscle fiber and basement membrane. May play a role in endochondral ossification of bone and branching morphogenesis of lung. Binds heparin. {ECO:0000250|UniProtKB:Q9R1N9, ECO:0000269|PubMed:10865988, ECO:0000269|PubMed:11956183}.; . TISSUE SPECIFICITY: Widely expressed in both fetal and adult ocular tissues (at protein level). In the eye, expression is accentuated in the ciliary muscle, optic nerve and the neural retina. In early placenta, localized to fibroblastoid stromal cells of the placental villi, to endothelial cells of developing capillaries and to cells of the cytotrophoblastic columns. Also detected in large decidual cells of the decidual membrane and to stromal cells of the gestational endometrium, but not in the epithelial cells in the endometrial glands. {ECO:0000269|PubMed:10865988, ECO:0000269|PubMed:8246446}.; unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;skin;uterus;prostate;lung;placenta;bone;testis;kidney;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle;cerebellum; 0.28276 0.14899 -0.440847477 24.59896202 250.76638 3.41203 COL14A1 0.00136791753453828 0.998632082463962 1.50001850463645e-12 collagen type XIV alpha 1 FUNCTION: Plays an adhesive role by integrating collagen bundles. It is probably associated with the surface of interstitial collagen fibrils via COL1. The COL2 domain may then serve as a rigid arm which sticks out from the fibril and protrudes the large N-terminal globular domain into the extracellular space, where it might interact with other matrix molecules or cell surface receptors (By similarity). {ECO:0000250, ECO:0000269|PubMed:2187872}.; . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;retina;bone marrow;uterus;prostate;whole body;cochlea;bone;thyroid;testis;brain;unclassifiable (Anatomical System);cartilage;heart;small intestine;islets of Langerhans;muscle;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;aorta;stomach; uterus;dorsal root ganglion;superior cervical ganglion;olfactory bulb;thyroid;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15473 0.18616 -1.109891924 6.723283793 1168.31521 6.49949 COL15A1 3.68385885743904e-06 0.999996136217107 1.79924035563316e-07 collagen type XV alpha 1 FUNCTION: Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle. {ECO:0000269|PubMed:10049780}.; . TISSUE SPECIFICITY: Expressed predominantly in internal organs such as adrenal gland, pancreas and kidney.; . . 0.21122 . 1.844643849 97.10426987 3519.49319 11.44267 COL16A1 3.38473511158888e-15 0.999999977499779 2.25002178266578e-08 collagen type XVI alpha 1 FUNCTION: Involved in mediating cell attachment and inducing integrin-mediated cellular reactions, such as cell spreading and alterations in cell morphology. {ECO:0000269|PubMed:16754661}.; . TISSUE SPECIFICITY: In papillary dermis, is a component of specialized fibrillin-1-containing microfibrils, whereas in territorial cartilage matrix, it is localized to a discrete population of thin, weakly banded collagen fibrils in association with other collagens (at protein level). In the placenta, where it is found in the amnion, a membranous tissue lining the amniotic cavity. Within the amnion, it is found in an acellular, relatively dense layer of a complex network of reticular fibers. Also located to a fibroblast layer beneath this dense layer. Exists in tissues in association with other types of collagen. {ECO:0000269|PubMed:12782140}.; ovary;foreskin;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;oesophagus;endometrium;larynx;bone;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;hypothalamus;spinal cord;lens;pancreas;lung;epididymis;trabecular meshwork;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; hypothalamus; 0.12704 0.12671 0.576763804 82.17740033 3012.83848 10.42371 COL17A1 5.82447151365916e-11 0.999999993309364 6.63239147352453e-09 collagen type XVII alpha 1 FUNCTION: May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane.; DISEASE: Generalized atrophic benign epidermolysis bullosa (GABEB) [MIM:226650]: A non-lethal, adult form of junctional epidermolysis bullosa characterized by life-long blistering of the skin, associated with hair and tooth abnormalities. {ECO:0000269|PubMed:10652291, ECO:0000269|PubMed:10951237, ECO:0000269|PubMed:11912005, ECO:0000269|PubMed:8669466, ECO:0000269|PubMed:9199555}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epithelial recurrent erosion dystrophy (ERED) [MIM:122400]: A corneal dystrophy characterized by recurrent episodes of epithelial erosions from childhood, with occasional impairment of vision. Most patients have attacks of redness, photophobia, epiphora, and ocular pain. Exposure to sunlight or draught, dust and smoke and lack of sleep can precipitate attacks. {ECO:0000269|PubMed:25676728}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in skin (PubMed:8618013). In the cornea, it is detected in the epithelial basement membrane, the epithelial cells, and at a lower level in stromal cells (at protein level) (PubMed:25676728). Stratified squamous epithelia. Found in hemidesmosomes. Expressed in cornea, oral mucosa, esophagus, intestine, kidney collecting ducts, ureter, bladder, urethra and thymus but is absent in lung, blood vessels, skeletal muscle and nerves. {ECO:0000269|PubMed:1748679, ECO:0000269|PubMed:25676728, ECO:0000269|PubMed:8618013}.; colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;testis;bladder;brain;unclassifiable (Anatomical System);heart;tongue;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;hypopharynx;liver;spleen;head and neck;stomach; lung;placenta;skin;bone marrow; 0.25310 0.28257 -0.709351243 14.57891012 2369.25671 9.03757 COL18A1 1.23766303264373e-05 0.999986852074155 7.71295518743136e-07 collagen type XVIII alpha 1 FUNCTION: COLA18A probably plays a major role in determining the retinal structure as well as in the closure of the neural tube.; DISEASE: Knobloch syndrome 1 (KNO1) [MIM:267750]: A developmental disorder primarily characterized by typical eye abnormalities, including high myopia, cataracts, dislocated lens, vitreoretinal degeneration, and retinal detachment, with occipital skull defects, which can range from occipital encephalocele to occult cutis aplasia. {ECO:0000269|PubMed:10942434, ECO:0000269|PubMed:23667181}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Present in multiple organs with highest levels in liver, lung and kidney.; myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;amniotic fluid;spinal ganglion;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;breast;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; liver;trigeminal ganglion; 0.35149 . 0.743953846 86.36470866 5515.49068 15.31657 COL18A1-AS1 . . . COL18A1 antisense RNA 1 . . . . . 0.10430 . . . . . COL18A1-AS2 . . . COL18A1 antisense RNA 2 . . . . . . . . . . . COL19A1 5.55032017757713e-17 0.999008905415671 0.000991094584329417 collagen type XIX alpha 1 FUNCTION: May act as a cross-bridge between fibrils and other extracellular matrix molecules. Involved in skeletal myogenesis in the developing esophagus. May play a role in organization of the pericellular matrix or the sphinteric smooth muscle. {ECO:0000269|PubMed:12788917}.; . TISSUE SPECIFICITY: Localized to vascular, neuronal, mesenchymal, and some epithelial basement membrane zones in umbilical cord. {ECO:0000269|PubMed:12788917}.; lung;nasopharynx;testis;kidney;germinal center;skeletal muscle;retina; cerebellum peduncles;globus pallidus;ciliary ganglion; . 0.12613 -0.121287852 44.12007549 3154.15403 10.69128 COL20A1 1.26872087443005e-24 0.00103137801774797 0.998968621982252 collagen type XX alpha 1 FUNCTION: Probable collagen protein.; . TISSUE SPECIFICITY: High expression in heart, lung, liver, skeletal muscle, kidney, pancreas, spleen, testis, ovary, subthalamic nucleus and fetal liver. Weak expression in other tissues tested.; lung;testis;choroid;brain; dorsal root ganglion;subthalamic nucleus;occipital lobe;adrenal gland;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.09250 0.08222 -0.374974929 28.11983958 1065.33487 6.25837 COL21A1 1.1540367820735e-20 0.00834302182100024 0.991656978179 collagen type XXI alpha 1 . . TISSUE SPECIFICITY: Highly expressed in lymph node, jejunum, pancreas, stomach, trachea, testis, uterus and placenta; moderately expressed in brain, colon, lung, prostate, spinal cord, salivary gland and vascular smooth-muscle cells and very weakly expressed in heart, liver, kidney, bone marrow, spleen, thymus, skeletal muscle, adrenal gland and peripheral leukocytes. Expression in heart was higher in the right ventricle and atrium than in the left ventricle and atrium. {ECO:0000269|PubMed:11566190, ECO:0000269|PubMed:11863369}.; unclassifiable (Anatomical System);meninges;heart;skeletal muscle;skin;retina;uterus;pia mater;whole body;lung;frontal lobe;endometrium;trabecular meshwork;placenta;visual apparatus;liver;testis;dura mater;kidney;spinal ganglion;brain;stomach; fetal lung;atrioventricular node; 0.53496 0.13586 0.718303761 85.85161595 1315.10669 6.81730 COL22A1 8.25832618148535e-32 0.345789429985902 0.654210570014098 collagen type XXII alpha 1 FUNCTION: Acts as a cell adhesion ligand for skin epithelial cells and fibroblasts.; . TISSUE SPECIFICITY: Restrictive expression is observed at tissue junctions such as the myotendinous junction in skeletal and heart muscle, the articular cartilage-synovial fluid junction, or the border between the anagen hair follicle and the dermis in the skin. It is deposited in the basement membrane zone of the myotendinous junction and the hair follicle and associated with the extrafibrillar matrix in cartilage. {ECO:0000269|PubMed:15016833}.; unclassifiable (Anatomical System);medulla oblongata;ovary;heart;parathyroid;fovea centralis;choroid;lens;skin;retina;pancreas;prostate;optic nerve;whole body;lung;adrenal gland;macula lutea;alveolus;pituitary gland;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.08309 . 0.161491526 64.92686954 2203.69391 8.64163 COL23A1 9.57449236414112e-10 0.90264393009584 0.0973560689467103 collagen type XXIII alpha 1 . . . . . 0.07258 0.08141 0.75875178 86.82472281 1444.11081 7.08807 COL24A1 1.06341054664097e-25 0.975699922440243 0.024300077559757 collagen type XXIV alpha 1 FUNCTION: May participate in regulating type I collagen fibrillogenesis at specific anatomical locations during fetal development. {ECO:0000269|PubMed:12874293}.; . . . . 0.15994 0.11186 0.79541165 87.41448455 9574.81397 21.18138 COL25A1 7.11571993838381e-08 0.999947908924767 5.20199180332166e-05 collagen type XXV alpha 1 FUNCTION: Inhibits fibrillization of beta amyloid peptide during the elongation phase. Has also been shown to assemble amyloid fibrils into protease-resistant aggregates. Binds heparin. {ECO:0000269|PubMed:15522881, ECO:0000269|PubMed:15615705, ECO:0000269|PubMed:15853808, ECO:0000269|PubMed:16300410}.; DISEASE: Fibrosis of extraocular muscles, congenital, 5 (CFEOM5) [MIM:616219]: An ocular motility disorder characterized by congenital dysinnervation of various cranial nerves to ocular muscles. Clinical features are ophthalmoplegia, anchoring of the eyes in downward gaze, ptosis, and backward tilt of the head. {ECO:0000269|PubMed:25500261}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly in brain. Deposited preferentially in primitive or neuritic amyloid plaques which are typical of Alzheimer disease. {ECO:0000269|PubMed:11927537}.; unclassifiable (Anatomical System);lung;testis; . 0.15107 0.10457 -0.356299879 29.31115829 142.01068 2.60199 COL26A1 0.000191086087413664 0.974764546277321 0.0250443676352656 collagen type XXVI alpha 1 . . . . . 0.19198 . . . . . COL27A1 0.999999360727437 6.39272562687969e-07 9.95271098667894e-23 collagen type XXVII alpha 1 FUNCTION: Plays a role during the calcification of cartilage and the transition of cartilage to bone. {ECO:0000269|PubMed:17693149}.; DISEASE: Steel syndrome (STLS) [MIM:615155]: A syndrome characterized by dislocated hips and radial heads, fusion of carpal bones, short stature, scoliosis, and cervical spine anomalies. Facial features include prominent forehead, long oval- shaped face, hypertelorism and broad nasal bridge. {ECO:0000269|PubMed:24986830}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;colon;parathyroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;cerebellum cortex;islets of Langerhans;urinary;muscle;skeletal muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;olfactory bulb;cerebellum peduncles;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion;cerebellum; 0.70075 . 0.170613481 65.33970276 8956.48219 20.50775 COL28A1 1.89303475564036e-20 0.144912682944934 0.855087317055066 collagen type XXVIII alpha 1 FUNCTION: May act as a cell-binding protein.; . . . . 0.18947 . 2.03756027 97.72941732 6380.32597 16.69110 COLCA1 0.0266155404570166 0.568479178149752 0.404905281393232 colorectal cancer associated 1 . . TISSUE SPECIFICITY: Expressed in gastrointestinal and immune tissue, as well as prostate, testis and ovary. Expressed in lamina propria and eosinophils but not in epithelial cells. Expression is greater in benign adjacent tissues than in colon tumors. {ECO:0000269|PubMed:24154973}.; . . . . . . 40.69872 1.19247 COLCA2 . . . colorectal cancer associated 2 . . TISSUE SPECIFICITY: Expressed in many cell types of epithelial, mesenchymal and hematopoietic origins. {ECO:0000269|PubMed:24154973}.; . . . . 0.035072054 56.2514744 13.70918 0.49703 COLEC10 0.09853673511482 0.866536224146744 0.0349270407384364 collectin subfamily member 10 FUNCTION: Lectin that binds to various sugars: galactose > mannose = fucose > N-acetylglucosamine > N-acetylgalactosamine. {ECO:0000269|PubMed:10224141}.; . TISSUE SPECIFICITY: Highly expressed in liver, placenta and adrenal gland. Moderately expressed in small intestine, lung, stomach and prostate. Weakly expressed in trachea and spleen. {ECO:0000269|PubMed:10224141}.; liver;spleen;skin; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.26958 0.13784 -0.115612493 45.12856806 56.82362 1.51760 COLEC11 0.0720344752709555 0.872306181068642 0.055659343660403 collectin subfamily member 11 FUNCTION: Lectin that binds to various sugars including fucose and mannose. Has a higher affinity for fucose compared to mannose. Does not bind to glucose, N-acetylglucosamine and N- acetylgalactosamine. Also binds lipopolysaccharides (LPS). Involved in fundamental development serving as a guidance cue for neural crest cell migration (By similarity). {ECO:0000250, ECO:0000269|PubMed:17179669}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17179669}.; unclassifiable (Anatomical System);heart;ovary;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;macula lutea;liver;kidney;mammary gland;brain; fetal liver;superior cervical ganglion;adrenal gland;liver;adrenal cortex;trigeminal ganglion; 0.15344 0.11083 -0.113792788 45.25831564 1270.03702 6.71501 COLEC12 0.991466232637133 0.00853336612049565 4.01242371514677e-07 collectin subfamily member 12 FUNCTION: Scavenger receptor that displays several functions associated with host defense. Promotes binding and phagocytosis of Gram-positive, Gram-negative bacteria and yeast. Mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. Binds to several carbohydrates including Gal-type ligands, D-galactose, L- and D-fucose, GalNAc, T and Tn antigens in a calcium-dependent manner and internalizes specifically GalNAc in nurse-like cells. Binds also to sialyl Lewis X or a trisaccharide and asialo-orosomucoid (ASOR). May also play a role in the clearance of amyloid beta in Alzheimer disease. {ECO:0000269|PubMed:11162630, ECO:0000269|PubMed:11564734, ECO:0000269|PubMed:12761161, ECO:0000269|PubMed:15845541, ECO:0000269|PubMed:16868960}.; . TISSUE SPECIFICITY: Expressed in perivascular macrophages. Expressed in plaques-surrounding reactive astrocytes and in perivascular astrocytes associated with cerebral amyloid angiopathy (CAA) in the temporal cortex of Alzheimer patient (at protein level). Strongly expressed in placenta. Moderately expressed in heart, skeletal muscle, small intestine and lung. Weakly expressed in brain, colon, thymus and kidney. Expressed in nurse-like cells. Expressed in reactive astrocytes and vascular/perivascular cells in the brain of Alzheimer patient. {ECO:0000269|PubMed:11162630, ECO:0000269|PubMed:11564734, ECO:0000269|PubMed:12761161, ECO:0000269|PubMed:16868960}.; . . 0.27899 0.18008 1.335644081 94.24982307 3329.25085 11.03240 COLGALT1 0.00373035647810141 0.987414415505877 0.00885522801602143 collagen beta(1-O)galactosyltransferase 1 FUNCTION: Has a beta-galactosyltransferase activity; transfers beta-galactose to hydroxylysine residues of collagen. {ECO:0000269|PubMed:19075007}.; . TISSUE SPECIFICITY: Ubiquitous with higher levels in placenta, heart, lung and spleen. {ECO:0000269|PubMed:19075007}.; . . 0.15494 0.10163 -1.50462206 3.568058504 229.16943 3.27112 COLGALT2 5.01784059691338e-07 0.958604920962875 0.0413945772530655 collagen beta(1-O)galactosyltransferase 2 FUNCTION: Has a beta-galactosyltransferase activity; transfers beta-galactose to hydroxylysine residues on collagen. {ECO:0000269|PubMed:19075007}.; . TISSUE SPECIFICITY: Expressed in brain and skeletal muscle. {ECO:0000269|PubMed:19075007}.; . . 0.12554 0.09957 -0.642904474 16.62538335 297.73119 3.68132 COLQ 1.42517319859713e-07 0.950058962410409 0.0499408950722715 collagen-like tail subunit (single strand of homotrimer) of asymmetric acetylcholinesterase FUNCTION: Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina.; DISEASE: Myasthenic syndrome, congenital, 5 (CMS5) [MIM:603034]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS5 inheritance is autosomal recessive. {ECO:0000269|PubMed:10665486, ECO:0000269|PubMed:11865139, ECO:0000269|PubMed:24938146, ECO:0000269|PubMed:9758617}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found at the end plate of skeletal muscle.; . . 0.08375 0.22610 -0.534490515 20.70063694 404.85361 4.21917 COMMD1 0.372793786323877 0.579768324678997 0.047437888997126 copper metabolism domain containing 1 FUNCTION: Proposed scaffold protein that is implicated in diverse physiological processes and whose function may be in part linked to its ability to regulate ubiquitination of specific cellular proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1; in vitro promotes CRL E3 activity and dissociates CAND1 from CUL1 and CUL2 (PubMed:21778237). Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity (PubMed:15799966, PubMed:17183367, PubMed:20048074). Involved in the regulation of membrane expression and ubiquitination of SLC12A2 (PubMed:23515529). Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits and by promoting their ubiquitination presumably involving NEDD4L. Promotes the localization of SCNN1D to recycling endosomes (PubMed:14645214, PubMed:20237237, PubMed:21741370). Promotes CFTR cell surface expression through regulation of its ubiquitination (PubMed:21483833). Down-regulates SOD1 activity by interfering with its homodimerization (PubMed:20595380). Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans- Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes (PubMed:25355947). Can bind one copper ion per monomer (PubMed:17309234). May function to facilitate biliary copper excretion within hepatocytes. Binds to phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2) (PubMed:18940794). Involved in the regulation of HIF1A-mediated transcription; competes with ARNT/Hif-1-beta for binding to HIF1A resulting in decreased DNA binding and impaired transcriptional activation by HIF-1 (PubMed:20458141). {ECO:0000269|PubMed:14645214, ECO:0000269|PubMed:14685266, ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:16573520, ECO:0000269|PubMed:17183367, ECO:0000269|PubMed:17309234, ECO:0000269|PubMed:20048074, ECO:0000269|PubMed:20237237, ECO:0000269|PubMed:20458141, ECO:0000269|PubMed:20595380, ECO:0000269|PubMed:21483833, ECO:0000269|PubMed:21741370, ECO:0000269|PubMed:21778237, ECO:0000269|PubMed:23515529, ECO:0000269|PubMed:25355947}.; . TISSUE SPECIFICITY: Ubiquitous. Highest expression in the liver, with lower expression in brain, lung, placenta, pancreas, small intestine, heart, skeletal muscle, kidney and placenta. Down- regulated in cancer tissues. {ECO:0000269|PubMed:11809725, ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:16573520, ECO:0000269|PubMed:20458141}.; ovary;umbilical cord;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;whole body;frontal lobe;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;adrenal cortex;pharynx;blood;skeletal muscle;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;parietal lobe; 0.11391 . -0.05129383 49.75819769 50.88674 1.40568 COMMD2 3.65344719758037e-07 0.105660219089619 0.894339415565662 COMM domain containing 2 FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). May down-regulate activation of NF-kappa-B (PubMed:15799966). {ECO:0000269|PubMed:15799966, ECO:0000305|PubMed:21778237}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15799966}.; . . 0.18300 0.10788 0.281220278 71.07808445 1969.53174 8.17837 COMMD3 0.00742011460272826 0.924029886568938 0.0685499988283337 COMM domain containing 3 FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). May down-regulate activation of NF-kappa-B (PubMed:15799966). Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits (PubMed:23637203). {ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:23637203, ECO:0000305|PubMed:21778237}.; . TISSUE SPECIFICITY: Widely expressed with highest expression in thymus. {ECO:0000269|PubMed:15799966}.; . . 0.36829 0.11457 0.082802743 60.09082331 1305.3608 6.79707 COMMD3-BMI1 0.0225993476495416 0.976751421041651 0.000649231308807799 COMMD3-BMI1 readthrough FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. In the PRC1 complex, it is required to stimulate the E3 ubiquitin-protein ligase activity of RNF2/RING2. {ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16714294, ECO:0000269|PubMed:16882984}.; . . . . . . . . 5.61252 0.21018 COMMD4 0.237758189788472 0.730133024703832 0.0321087855076958 COMM domain containing 4 FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). Down-regulates activation of NF-kappa-B. {ECO:0000269|PubMed:15799966, ECO:0000305|PubMed:21778237}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15799966}.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;placenta;hippocampus;head and neck;kidney;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;heart;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11718 0.10755 -0.073340031 48.11866006 22.40743 0.75185 COMMD5 0.000302003112131852 0.351986744645712 0.647711252242156 COMM domain containing 5 FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). Negatively regulates cell proliferation. Negatively regulates cell cycle G2/M phase transition probably by transactivating p21/CDKN1A through the p53/TP53-independent signaling pathway. Involved in kidney proximal tubule morphogenesis (By similarity). Down-regulates activation of NF-kappa-B (PubMed:15799966). {ECO:0000250|UniProtKB:Q9ERR2, ECO:0000269|PubMed:15799966, ECO:0000305|PubMed:21778237}.; . TISSUE SPECIFICITY: Highly expressed in heart, stomach, jejunum, kidney, liver, and adrenal gland. Expression was generally higher in adult organs than in fetal tissues, particularly in heart, kidney, and liver. {ECO:0000269|PubMed:10918053, ECO:0000269|PubMed:15799966}.; ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; . 0.07910 0.09845 0.659651797 84.35362114 1020.25234 6.14539 COMMD6 0.131043402998848 0.780189942132038 0.0887666548691147 COMM domain containing 6 FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). Down-regulates activation of NF-kappa-B. Inhibits TNF-induced NFKB1 activation. {ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:16573520, ECO:0000305|PubMed:21778237}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in brain, heart, skeletal muscle, lung, pancreas, liver, kidney, small intestine and placenta. {ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:16573520}.; unclassifiable (Anatomical System);uterus;lung;heart;endometrium;placenta;visual apparatus;testis;colon;parathyroid;brain; . 0.38002 0.10077 0.21326276 67.71644256 5.45937 0.20320 COMMD7 6.04653686013292e-06 0.4519062934796 0.54808765998354 COMM domain containing 7 FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). Associates with the NF-kappa-B complex and suppresses its transcriptional activity (PubMed:15799966). {ECO:0000269|PubMed:15799966, ECO:0000305|PubMed:21778237}.; . TISSUE SPECIFICITY: Widely expressed with highest expression in lung. {ECO:0000269|PubMed:15799966}.; salivary gland;colon;choroid;vein;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;parietal lobe;skeletal muscle;cerebellum; 0.07383 0.09741 -0.163345027 41.24793583 8.41662 0.30752 COMMD8 9.08074870529186e-07 0.174840297783093 0.825158794142037 COMM domain containing 8 FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). May down-regulate activation of NF-kappa-B (PubMed:15799966). {ECO:0000269|PubMed:15799966, ECO:0000305|PubMed:21778237}.; . TISSUE SPECIFICITY: Widely expressed with highest expression in thyroid. {ECO:0000269|PubMed:15799966}.; . . 0.12930 0.09348 0.813985927 87.81552253 139.6485 2.57659 COMMD9 0.635260481804229 0.35792342099355 0.00681609720222079 COMM domain containing 9 FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). May down-regulate activation of NF-kappa-B (PubMed:15799966). Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits (PubMed:23637203). {ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:23637203, ECO:0000305|PubMed:21778237}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15799966}.; ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;larynx;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; medulla oblongata;occipital lobe;testis; 0.10604 0.10785 0.148941568 64.31941496 61.12413 1.59161 COMMD10 7.83686369938315e-06 0.301803272271904 0.698188890864396 COMM domain containing 10 FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). May down-regulate activation of NF-kappa-B (PubMed:15799966). {ECO:0000269|PubMed:15799966, ECO:0000305|PubMed:21778237}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15799966}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;pharynx;blood;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;occipital lobe; 0.24460 0.11020 0.193034296 66.82000472 893.61877 5.82649 COMP . . . cartilage oligomeric matrix protein FUNCTION: May play a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 (By similarity). {ECO:0000250, ECO:0000269|PubMed:16051604, ECO:0000269|PubMed:16542502, ECO:0000269|PubMed:17993464}.; DISEASE: Multiple epiphyseal dysplasia 1 (EDM1) [MIM:132400]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal. {ECO:0000269|PubMed:11565064, ECO:0000269|PubMed:21922596, ECO:0000269|PubMed:7670472, ECO:0000269|PubMed:9021009, ECO:0000269|PubMed:9184241, ECO:0000269|PubMed:9452026, ECO:0000269|PubMed:9463320, ECO:0000269|PubMed:9921895}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pseudoachondroplasia (PSACH) [MIM:177170]: A skeletal dysplasia usually manifesting in the second year of life and characterized by moderate to severe disproportionate short stature, deformity of the lower limbs, brachydactyly, ligamentous laxity, and degenerative joint disease. {ECO:0000269|PubMed:11746044, ECO:0000269|PubMed:11746045, ECO:0000269|PubMed:21922596, ECO:0000269|PubMed:7670471, ECO:0000269|PubMed:7670472, ECO:0000269|PubMed:9184241, ECO:0000269|PubMed:9452026, ECO:0000269|PubMed:9452063, ECO:0000269|PubMed:9463320}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Abundantly expressed in the chondrocyte extracellular matrix, and is also found in bone, tendon, ligament and synovium and blood vessels. Increased amounts are produced during late stages of osteoarthritis in the area adjacent to the main defect. {ECO:0000269|PubMed:16542502}.; unclassifiable (Anatomical System);cartilage;ovary;colon;blood;skin;uterus;pancreas;prostate;cerebral cortex;endometrium;larynx;thyroid;bone;head and neck;brain;mammary gland; testis - interstitial;adipose tissue;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.69623 0.72248 -0.488577883 22.64685067 524.39964 4.67329 COMT 0.000846657832012693 0.554043598750617 0.44510974341737 catechol-O-methyltransferase FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.; . TISSUE SPECIFICITY: Brain, liver, placenta, lymphocytes and erythrocytes.; medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pineal body;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;duodenum;head and neck;kidney;aorta;stomach;thymus; superior cervical ganglion;adrenal gland;placenta;spinal cord;liver;skeletal muscle; 0.13725 0.75048 -0.181750739 40.15687662 2143.59556 8.51834 COMTD1 5.22496817166168e-06 0.245360812138329 0.754633962893499 catechol-O-methyltransferase domain containing 1 FUNCTION: Putative O-methyltransferase. {ECO:0000305}.; . . . . 0.23565 0.17097 . . 97.13052 2.13085 COPA 0.999999997609881 2.39011931544717e-09 2.14147689765785e-22 coatomer protein complex subunit alpha FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.; DISEASE: Autoimmune interstitial lung, joint, and kidney disease (AILJK) [MIM:616414]: An autoimmune disease characterized by inflammatory arthritis, interstitial lung disease, and immune complex-mediated renal disease. {ECO:0000269|PubMed:25894502}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Uniformly expressed in a wide range of adult and fetal tissues. Xenin is found in gastric, duodenal and jejunal mucosa. Circulates in the blood. Seems to be confined to specific endocrine cells.; lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;oral cavity;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;amnion;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;placenta;prefrontal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.12949 0.18436 -0.975433863 8.852323661 486.59691 4.54052 COPB1 0.999763440028058 0.000236559969327949 2.61439260628931e-12 coatomer protein complex subunit beta 1 FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Plays a functional role in facilitating the transport of kappa- type opioid receptor mRNAs into axons and enhances translation of these proteins. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte surface triglyceride lipase (PNPLA2) with the lipid droplet to mediate lipolysis (By similarity). Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1. Promotes degradation of Nef cellular targets CD4 and MHC class I antigens by facilitating their trafficking to degradative compartments. {ECO:0000250, ECO:0000269|PubMed:18385291, ECO:0000269|PubMed:18725938, ECO:0000269|PubMed:19364919, ECO:0000269|PubMed:20056612}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;artery;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;pharynx;blood;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; amygdala;superior cervical ganglion;thyroid; 0.52388 0.25831 -1.111360919 6.717386176 64.74861 1.65161 COPB2 0.999998457069596 1.54293040284087e-06 1.49697685822137e-15 coatomer protein complex subunit beta 2 (beta prime) FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;oral cavity;bile duct;pancreas;pia mater;lung;mesenchyma;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;trigeminal ganglion; 0.51577 0.19561 -0.934977358 9.465675867 73.10436 1.78585 COPE 0.6166479413462 0.381668913032408 0.00168314562139193 coatomer protein complex subunit epsilon FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated with ADP- ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.; . . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;visual apparatus;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;placenta;duodenum;kidney;stomach;aorta;cerebellum;thymus; whole brain;prostate;testis - interstitial;testis - seminiferous tubule;testis; 0.23031 0.15439 0.066214104 58.95848077 2254.64754 8.76852 COPG1 0.998499313833563 0.0015006859306375 2.35799862702398e-10 coatomer protein complex subunit gamma 1 FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis (By similarity). {ECO:0000250, ECO:0000269|PubMed:20674546}.; . . . . 0.17437 0.22852 -1.017713296 8.103326256 644.00146 5.09928 COPG2 0.0560373568810472 0.925314655323206 0.0186479877957469 coatomer protein complex subunit gamma 2 FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;visual apparatus;testis;brain;skeletal muscle; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.54002 . . . 27.4635 0.88482 COPG2IT1 . . . COPG2 imprinted transcript 1 (non-protein coding) . . . . . . . . . . . COPRS 0.832459192767082 0.164120807631137 0.0034199996017815 coordinator of PRMT5, differentiation stimulator FUNCTION: Histone-binding protein required for histone H4 methyltransferase activity of PRMT5. Specifically required for histone H4 'Arg-3' methylation mediated by PRMT5, but not histone H3 'Arg-8' methylation, suggesting that it modulates the substrate specificity of PRMT5. Specifically interacts with the N-terminus of histone H4 but not with histone H3, suggesting that it acts by promoting the association between histone H4 and PRMT5. Involved in CCNE1 promoter repression. Plays a role in muscle cell differentiation by modulating the recruitment of PRMT5 to the promoter of genes involved in the coordination between cell cycle exit and muscle differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:18404153}.; . . . . 0.03084 0.06300 0.103030231 61.2762444 7.16622 0.26932 COPS2 0.999572843395694 0.000427155272754306 1.33155124375722e-09 COP9 signalosome subunit 2 FUNCTION: Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN- dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Involved in early stage of neuronal differentiation via its interaction with NIF3L1. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:9535219}.; . . myocardium;ovary;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;oesophagus;bone;pituitary gland;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;pia mater;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.80747 0.15588 -0.141298762 42.87567823 2.46087 0.09020 COPS3 0.992904074102341 0.00709567043489507 2.5546276354979e-07 COP9 signalosome subunit 3 FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:9535219}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at high level in heart and skeletal muscle. {ECO:0000269|PubMed:10191102}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;epididymis;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis; 0.48376 0.12104 -0.538132194 20.26421326 14.78144 0.53253 COPS4 0.997696128383201 0.00230379066830764 8.09484914948806e-08 COP9 signalosome subunit 4 FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. Also involved in the deneddylation of non-cullin subunits such as STON2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1, IRF8/ICSBP and SNAPIN, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:21102408, ECO:0000269|PubMed:9535219}.; . . lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;lung;pia mater;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach;aorta;thymus; amygdala;thalamus;occipital lobe;superior cervical ganglion;testis - interstitial;medulla oblongata;hypothalamus;temporal lobe;pons;caudate nucleus;testis;globus pallidus;trigeminal ganglion;parietal lobe;pituitary; 0.45990 0.11809 -0.163345027 41.24793583 16.10112 0.57010 COPS5 0.994339560596831 0.00565971306410216 7.2633906698632e-07 COP9 signalosome subunit 5 FUNCTION: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex. Promotes the proteasomal degradation of BRSK2. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:22609399, ECO:0000269|PubMed:9535219}.; . . smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; amygdala;superior cervical ganglion;thalamus;occipital lobe;testis - interstitial;hypothalamus;spinal cord;caudate nucleus;testis - seminiferous tubule;globus pallidus;testis;trigeminal ganglion;parietal lobe;cingulate cortex; 0.96445 0.31462 -0.119252484 44.53880632 3.38694 0.12342 COPS5P1 . . . COP9 signalosome subunit 5 pseudogene 1 . . . . . . . . . . . COPS5P2 . . . COP9 signalosome subunit 5 pseudogene 2 . . . . . . . . . . . COPS6 0.84586120251302 0.154021560617305 0.000117236869675381 COP9 signalosome subunit 6 FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Has some glucocorticoid receptor- responsive activity. Stabilizes RFWD2/COP1 through reducing RFWD2 auto-ubiquitination and decelerating RFWD2 turnover rate, hence regulates the ubiquitination of RFWD2 targets. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:21625211, ECO:0000269|PubMed:9535219}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9520381}.; myocardium;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;cingulate cortex; 0.46293 0.15226 -0.207437529 38.2814343 28.94352 0.92502 COPS7A 0.922072581433795 0.0778303409555231 9.70776106821646e-05 COP9 signalosome subunit 7A FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:9535219}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at high level in brain, heart and skeletal muscle. {ECO:0000269|PubMed:12020345}.; lymphoreticular;ovary;sympathetic chain;skin;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;trachea;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta; whole brain;superior cervical ganglion;thalamus;occipital lobe;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.53766 0.12327 -0.317668748 31.45789101 18.82591 0.65060 COPS7B 0.207502332172099 0.7831281979227 0.00936946990520181 COP9 signalosome subunit 7B FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143}.; . . ovary;developmental;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;nervous;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach;thymus; . 0.49504 0.08191 -0.117432389 44.89266336 59.3707 1.56192 COPS8 0.138824250988609 0.841307588651541 0.01986816035985 COP9 signalosome subunit 8 FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:9535219}.; . . lymphoreticular;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;salivary gland;colon;parathyroid;vein;uterus;whole body;larynx;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; whole brain;amygdala;dorsal root ganglion;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;adipose tissue;hypothalamus;spinal cord;temporal lobe;caudate nucleus;atrioventricular node;pons;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.25298 0.18619 0.058937498 58.26256192 18.77437 0.64853 COPS8P1 . . . COP9 signalosome subunit 8 pseudogene 1 . . . . . . . . . . . COPS8P2 . . . COP9 signalosome subunit 8 pseudogene 2 . . . . . . . . . . . COPS8P3 . . . COP9 signalosome subunit 8 pseudogene 3 . . . . . . . . . . . COPZ1 0.890701152776699 0.10906675594144 0.000232091281861618 coatomer protein complex subunit zeta 1 FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.; . . lymphoreticular;myocardium;ovary;umbilical cord;skin;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;amniotic fluid;germinal center;brain;bladder;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;pia mater;lung;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;cerebellum; superior cervical ganglion;kidney;cerebellum; 0.16613 0.12378 -0.09720619 46.20193442 3.96945 0.14679 COPZ2 0.0017094888551626 0.705700239623912 0.292590271520925 coatomer protein complex subunit zeta 2 FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;parathyroid;choroid;fovea centralis;skin;retina;uterus;optic nerve;whole body;thyroid;bone;testis;brain;heart;cartilage;lens;skeletal muscle;lung;placenta;macula lutea;liver;spleen;kidney;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.32230 0.10761 . . 26.87836 0.86879 COQ2 0.000224020159654837 0.74600851768591 0.253767462154435 coenzyme Q2 4-hydroxybenzoate polyprenyltransferase FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate. {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000269|PubMed:15153069}.; DISEASE: Multiple system atrophy 1 (MSA1) [MIM:146500]: A progressive neurodegenerative disorder clinically characterized by parkinsonism, cerebellar ataxia, and autonomic, urogenital, and pyramidal dysfunction in various combinations. Pathologically, it is characterized by degeneration of striatonigral and olivopontocerebellar structures, and glial cytoplasmic inclusions that consist of abnormally phosphorylated alpha-synuclein or tau. {ECO:0000269|PubMed:23758206}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Present in all of the tissues tested. Expressed at higher level in skeletal muscle, adrenal glands and the heart. {ECO:0000269|PubMed:15153069}.; ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;pharynx;blood;lens;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;alveolus;cervix;kidney;mammary gland;stomach; superior cervical ganglion;skeletal muscle; 0.10659 0.12964 0.148941568 64.31941496 96.70846 2.12541 COQ3 7.05935714539158e-10 0.0377314769482705 0.962268522345794 coenzyme Q3 methyltransferase FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. {ECO:0000255|HAMAP- Rule:MF_03190}.; . . unclassifiable (Anatomical System);trophoblast;lymph node;hypothalamus;muscle;colon;blood;skeletal muscle;bone marrow;breast;uterus;prostate;whole body;lung;nasopharynx;bone;placenta;liver;testis;spleen;kidney;brain;mammary gland;stomach; superior cervical ganglion;parietal lobe; 0.34519 0.10776 0.617373774 83.25076669 3226.88875 10.81809 COQ4 0.000292854581816104 0.796875920822841 0.202831224595343 coenzyme Q4 FUNCTION: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides. {ECO:0000255|HAMAP- Rule:MF_03111, ECO:0000269|PubMed:18474229}.; . TISSUE SPECIFICITY: Expressed ubiquitously, but at high levels in liver, lung and pancreas. {ECO:0000269|PubMed:18474229}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;hypothalamus;pharynx;blood;skeletal muscle;bile duct;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; thyroid;liver; 0.13610 0.10664 0.505321956 80.00707714 335.79652 3.89376 COQ5 7.95018460631921e-05 0.761213457819244 0.238707040334693 coenzyme Q5, methyltransferase FUNCTION: Methyltransferase required for the conversion of 2- polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3- methyl-6-methoxy-1,4-benzoquinol (DMQH2). {ECO:0000255|HAMAP- Rule:MF_03191}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in liver, lung, placenta and skeletal muscle. {ECO:0000269|PubMed:25152161}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;ganglion;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; . 0.07328 0.17273 -0.093566408 46.7386176 1490.84473 7.18221 COQ6 2.31087652552578e-07 0.705178616453474 0.294821152458873 coenzyme Q6 monooxygenase FUNCTION: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3- polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferredoxin/ferredoxin reductase system to COQ6. {ECO:0000255|HAMAP-Rule:MF_03193}.; . TISSUE SPECIFICITY: Widely epressed. {ECO:0000269|PubMed:21540551}.; medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; atrioventricular node; 0.15940 0.22002 0.709197509 85.68058504 4612.46252 13.63954 COQ7 4.67860434510292e-05 0.416968957079192 0.582984256877357 coenzyme Q7 homolog, ubiquinone (yeast) FUNCTION: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6- methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides. Involved in lifespan determination in a ubiquinone-independent manner. {ECO:0000255|HAMAP-Rule:MF_03194}.; . TISSUE SPECIFICITY: Expressed dominantly in heart and skeletal muscle.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;lens;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;spleen;cervix;kidney;mammary gland;thymus; subthalamic nucleus;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.15929 0.14294 -0.115612493 45.12856806 146.5872 2.63730 COQ9 0.000172325245964419 0.886038515653899 0.113789159100137 coenzyme Q9 FUNCTION: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Binds a phospholipid of at least 10 carbons in each acyl group. May be required to present its bound-lipid to COQ7. {ECO:0000269|PubMed:25339443}.; DISEASE: Coenzyme Q10 deficiency, primary, 5 (COQ10D5) [MIM:614654]: A form of coenzyme Q10 deficiency, an autosomal recessive disorder with variable manifestations consistent with 5 major phenotypes. The phenotypes include an encephalomyopathic form with seizures and ataxia; a multisystem infantile form with encephalopathy, cardiomyopathy and renal failure; a predominantly cerebellar form with ataxia and cerebellar atrophy; Leigh syndrome with growth retardation; and an isolated myopathic form. {ECO:0000269|PubMed:19375058}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;hypothalamus;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach; testis;kidney;skeletal muscle; 0.12806 0.08647 0.68351529 85.03774475 243.425 3.36744 COQ10A 0.12109648380279 0.853842639645117 0.0250608765520926 coenzyme Q10A FUNCTION: Required for the function of coenzyme Q in the respiratory chain. May serve as a chaperone or may be involved in the transport of Q6 from its site of synthesis to the catalytic sites of the respiratory complexes (Probable). {ECO:0000305}.; . . ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;thyroid;bone;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;blood;skeletal muscle;lung;placenta;liver;spleen;kidney;stomach;thymus; . 0.24144 0.12122 -0.405853867 26.23260203 286.0537 3.61957 COQ10B 0.140032716980132 0.840396563518373 0.019570719501495 coenzyme Q10B FUNCTION: Required for the function of coenzyme Q in the respiratory chain. May serve as a chaperone or may be involved in the transport of Q6 from its site of synthesis to the catalytic sites of the respiratory complexes (By similarity). {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;cerebellum cortex;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.12177 0.11803 0.014844891 54.94810097 6.81651 0.25234 COQ10BP1 . . . coenzyme Q10B pseudogene 1 . . . . . . . . . . . COQ10BP2 . . . coenzyme Q10B pseudogene 2 . . . . . . . . . . . CORD1 . . . cone rod dystrophy 1 (autosomal dominant) . . . . . . . . . . . CORD4 . . . cone rod dystrophy 4 . . . . . . . . . . . CORD8 . . . cone rod dystrophy 8 . . . . . . . . . . . CORD17 . . . cone rod dystrophy 17 (autosomal dominant) . . . . . . . . . . . CORIN 6.35410439875821e-20 0.0118172341498627 0.988182765850137 corin, serine peptidase FUNCTION: Serine-type endopeptidase involved in atrial natriuretic peptide hormone (NPPA) processing. Converts through proteolytic cleavage the non-functional propeptide NPPA into the active hormone, thereby regulating blood pressure in heart and promoting natriuresis, diuresis and vasodilation. Proteolytic cleavage of pro-NPPA also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus. Also acts as a regulator of sodium reabsorption in kidney. May also process pro-NPPB the B-type natriuretic peptide.; DISEASE: Pre-eclampsia/eclampsia 5 (PEE5) [MIM:614595]: A hypertensive disorder of pregnancy characterized by new hypertension (blood pressure 140/90 or greater) presenting after 20 weeks' gestation with clinically relevant proteinuria. It impacts 2 individuals, the mother and her child, both of whom can be severely affected. Preeclampsia is one of the causes of maternal mortality and morbidity worldwide. {ECO:0000269|PubMed:22437503}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in heart. Expressed in heart myocytes. Also expressed in pregnant uterus. Detected in blood, in plasma as well as in serum (at protein level). {ECO:0000269|PubMed:10329693, ECO:0000269|PubMed:19751717, ECO:0000269|PubMed:22437503}.; unclassifiable (Anatomical System);smooth muscle;heart;colon;skeletal muscle;skin;uterus;pancreas;whole body;lung;bone;visual apparatus;testis; superior cervical ganglion;appendix;trigeminal ganglion; 0.12664 . -0.145152788 42.33899505 519.7225 4.65704 CORO1A 0.954491479297814 0.0454835571625837 2.49635396024939e-05 coronin 1A FUNCTION: May be a crucial component of the cytoskeleton of highly motile cells, functioning both in the invagination of large pieces of plasma membrane, as well as in forming protrusions of the plasma membrane involved in cell locomotion. In mycobacteria- infected cells, its retention on the phagosomal membrane prevents fusion between phagosomes and lysosomes. {ECO:0000269|PubMed:10338208}.; DISEASE: Immunodeficiency 8 (IMD8) [MIM:615401]: A disease of the immune system leading to recurrent infections, and characterized by CD4+ T-cells lymphopenia. Patients can develop B-cell lymphoproliferation associated with Epstein-Barr virus infection. {ECO:0000269|PubMed:19097825, ECO:0000269|PubMed:23522482}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, thymus, spleen, bone marrow and lymph node. Low in lung and gut.; lymphoreticular;colon;choroid;bone marrow;uterus;prostate;frontal lobe;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;aorta;peripheral nerve;thymus; lymph node;tumor;white blood cells;whole blood;tonsil;thymus;bone marrow; 0.77787 0.15858 -0.514264485 21.41424864 23.13331 0.77143 CORO1B 0.260249265031264 0.738563357214646 0.00118737775408966 coronin 1B FUNCTION: Regulates leading edge dynamics and cell motility in fibroblasts. May be involved in cytokinesis and signal transduction (By similarity). {ECO:0000250, ECO:0000269|PubMed:16027158}.; . . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;iris;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.53527 0.16798 -0.843147538 11.2762444 89.58877 2.03649 CORO1C 0.997273678156858 0.00272619978474487 1.22058397360021e-07 coronin 1C FUNCTION: May be involved in cytokinesis, motility, and signal transduction. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;hypopharynx;duodenum;liver;head and neck;kidney;mammary gland;aorta;stomach; . 0.91587 0.10818 -0.670411825 15.61689078 57.44586 1.52738 CORO2A 2.57251247711706e-06 0.913893629245312 0.0861037982422107 coronin 2A . . . unclassifiable (Anatomical System);ovary;colon;parathyroid;blood;bone marrow;uterus;prostate;lung;frontal lobe;endometrium;bone;placenta;visual apparatus;liver;testis;spleen;germinal center;mammary gland;stomach; . 0.15298 0.11042 -0.729274834 14.15428167 140.92704 2.58947 CORO2B 0.779053736737647 0.220882015298199 6.42479641537831e-05 coronin 2B FUNCTION: May play a role in the reorganization of neuronal actin structure.; . TISSUE SPECIFICITY: Expressed predominantly in brain.; sympathetic chain;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;cerebellum cortex;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;macula lutea;visual apparatus;hippocampus;head and neck;kidney;stomach; whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.50461 0.11034 -0.380166007 27.88393489 54.48241 1.47592 CORO6 3.14028875176378e-05 0.795742922467084 0.204225674645398 coronin 6 . . . unclassifiable (Anatomical System);heart;ovary;muscle;parathyroid;skin;skeletal muscle;uterus;optic nerve;whole body;lung;frontal lobe;larynx;bone;thyroid;placenta;alveolus;liver;head and neck;spleen;brain;mammary gland;peripheral nerve; . 0.29434 . -0.249709319 35.74545883 87.4322 1.99693 CORO7 7.31151184071541e-12 0.958144842079815 0.0418551579128736 coronin 7 FUNCTION: F-actin regulator involved in anterograde Golgi to endosome transport: upon ubiquitination via 'Lys-33'-linked ubiquitin chains by the BCR(KLHL20) E3 ubiquitin ligase complex, interacts with EPS15 and localizes to the trans-Golgi network, where it promotes actin polymerization, thereby facilitating post- Golgi trafficking. May play a role in the maintenance of the Golgi apparatus morphology. {ECO:0000269|PubMed:16905771, ECO:0000269|PubMed:24768539}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in the spleen, peripheral leukocytes, testes, brain, thymus and small intestine. {ECO:0000269|PubMed:21130766}.; lymphoreticular;ovary;salivary gland;colon;skin;bone marrow;prostate;optic nerve;frontal lobe;endometrium;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;spleen;kidney; adrenal cortex;white blood cells;ciliary ganglion;caudate nucleus;whole blood; 0.10277 . 0.124866463 62.3967917 . . CORO7-PAM16 1.62821439778502e-12 0.984191520458522 0.0158084795398496 CORO7-PAM16 readthrough FUNCTION: F-actin regulator involved in anterograde Golgi to endosome transport: upon ubiquitination via 'Lys-33'-linked ubiquitin chains by the BCR(KLHL20) E3 ubiquitin ligase complex, interacts with EPS15 and localizes to the trans-Golgi network, where it promotes actin polymerization, thereby facilitating post- Golgi trafficking. May play a role in the maintenance of the Golgi apparatus morphology. {ECO:0000269|PubMed:16905771, ECO:0000269|PubMed:24768539}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in the spleen, peripheral leukocytes, testes, brain, thymus and small intestine. {ECO:0000269|PubMed:21130766}.; . . 0.10277 . . . 354.46462 3.98284 CORT 0.0098377909618654 0.60003244390907 0.390129765129065 cortistatin FUNCTION: Binds to all human somatostatin receptor (SSTR) subtypes. It also inhibits cAMP production induced by forskolin through SSTRs.; . TISSUE SPECIFICITY: Expressed in a subset of GABAergic cells in the cortex and hippocampus.; unclassifiable (Anatomical System);medulla oblongata;ovary;colon;blood;parathyroid;fovea centralis;choroid;lens;skin;retina;optic nerve;lung;placenta;macula lutea;pituitary gland;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; . 0.26604 -0.141298762 42.87567823 2.07555 0.06758 COTL1 0.0667591515201751 0.732652244322143 0.200588604157682 coactosin-like F-actin binding protein 1 FUNCTION: Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization. Acts as a chaperone for ALOX5 (5LO), influencing both its stability and activity in leukotrienes synthesis. {ECO:0000269|PubMed:11583571, ECO:0000269|PubMed:19807693}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in placenta, lung, kidney and peripheral blood leukocytes and lower levels in brain, liver and pancreas. {ECO:0000269|PubMed:11583571}.; ovary;skin;bone marrow;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;choroid;uterus;whole body;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;nasopharynx;placenta;duodenum;kidney;stomach;aorta;thymus; white blood cells;whole blood; 0.21636 0.14468 -0.229483771 36.86010852 15.10739 0.54334 COTL1P1 . . . coactosin-like F-actin binding protein 1 pseudogene 1 . . . . . . . . . . . COTL1P2 . . . coactosin-like F-actin binding protein 1 pseudogene 2 . . . . . . . . . . . COX4I1 0.722238025462968 0.27478421204201 0.00297776249502212 cytochrome c oxidase subunit 4I1 FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;bladder;brain;tonsil;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;pia mater;lung;nasopharynx;placenta;hippocampus;kidney;stomach;aorta;thymus; whole brain;medulla oblongata;thalamus;occipital lobe;heart;hypothalamus;temporal lobe;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;liver;prefrontal cortex;globus pallidus;kidney;parietal lobe;cingulate cortex;cerebellum; 0.12851 0.18904 -0.073340031 48.11866006 1278.29291 6.73172 COX4I1P1 . . . cytochrome c oxidase subunit 4I1 pseudogene 1 . . . . . . . . . . . COX4I1P2 . . . cytochrome c oxidase subunit 4I1 pseudogene 2 . . . . . . . . . . . COX4I2 0.00147571485756203 0.674656668300366 0.323867616842072 cytochrome c oxidase subunit 4I2 FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.; . TISSUE SPECIFICITY: Highly expressed in lung.; . . 0.08987 0.11076 0.859896574 88.62349611 333.76044 3.88072 COX5A 0.324238692730719 0.61012662046289 0.0656346868063907 cytochrome c oxidase subunit 5A FUNCTION: This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.; . . myocardium;medulla oblongata;ovary;skin;retina;bone marrow;prostate;frontal lobe;thyroid;iris;germinal center;bladder;brain;heart;urinary;pharynx;blood;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;larynx;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;placenta;hippocampus;duodenum;head and neck;kidney;stomach; amygdala;whole brain;heart;liver;testis;skeletal muscle; 0.12532 0.28848 -0.163345027 41.24793583 8.88764 0.32735 COX5AP1 . . . cytochrome c oxidase subunit 5A pseudogene 1 . . . . . . . . . . . COX5AP2 . . . cytochrome c oxidase subunit 5A pseudogene 2 . . . . . . . . . . . COX5B 0.412576836067639 0.551167228932409 0.0362559349999513 cytochrome c oxidase subunit 5B FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.; . . myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;kidney;stomach;aorta; whole brain;amygdala;thalamus;subthalamic nucleus;medulla oblongata;heart;temporal lobe;liver;cingulate cortex;skeletal muscle; 0.55043 0.12112 0.235309407 68.71903751 43.95859 1.26288 COX5BP1 . . . cytochrome c oxidase subunit 5B pseudogene 1 . . . . . . . . . . . COX5BP2 . . . cytochrome c oxidase subunit 5B pseudogene 2 . . . . . . . . . . . COX5BP3 . . . cytochrome c oxidase subunit 5B pseudogene 3 . . . . . . . . . . . COX5BP4 . . . cytochrome c oxidase subunit 5B pseudogene 4 . . . . . . . . . . . COX5BP5 . . . cytochrome c oxidase subunit 5B pseudogene 5 . . . . . . . . . . . COX5BP6 . . . cytochrome c oxidase subunit 5B pseudogene 6 . . . . . . . . . . . COX5BP7 . . . cytochrome c oxidase subunit 5B pseudogene 7 . . . . . . . . . . . COX5BP8 . . . cytochrome c oxidase subunit 5B pseudogene 8 . . . . . . . . . . . COX6A1 0.0609575623120839 0.719988080470643 0.219054357217273 cytochrome c oxidase subunit 6A1 FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.; DISEASE: Charcot-Marie-Tooth disease, recessive, intermediate type, D (CMTRID) [MIM:616039]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Recessive intermediate forms of Charcot-Marie-Tooth disease are characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. {ECO:0000269|PubMed:25152455}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;bone;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;placenta;hippocampus;kidney;stomach;aorta; . 0.45335 0.08994 -0.317668748 31.45789101 9.71344 0.35642 COX6A1P1 . . . cytochrome c oxidase subunit 6A1 pseudogene 1 . . . . . . . . . . . COX6A1P2 0.139600415963223 0.626048364446027 0.23435121959075 cytochrome c oxidase subunit 6A1 pseudogene 2 . . . . . . . . . 179.81977 2.91368 COX6A1P3 . . . cytochrome c oxidase subunit 6A1 pseudogene 3 . . . . . . . . . . . COX6A2 0.549091486087313 0.397344465111364 0.0535640488013229 cytochrome c oxidase subunit 6A2 FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.; . TISSUE SPECIFICITY: Expressed specifically in heart and muscle. {ECO:0000269|PubMed:1327966}.; unclassifiable (Anatomical System);myocardium;heart;muscle;colon;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;prostate;optic nerve;lung;macula lutea;liver;testis;kidney;brain;stomach; superior cervical ganglion;heart;tongue;skeletal muscle; 0.14223 0.12499 0.257356108 69.83368719 11.24447 0.40563 COX6B1 0.0816220932965698 0.756092919063099 0.162284987640331 cytochrome c oxidase subunit 6B1 FUNCTION: Connects the two COX monomers into the physiological dimeric form. {ECO:0000250}.; DISEASE: Mitochondrial complex IV deficiency (MT-C4D) [MIM:220110]: A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs. Features include hypertrophic cardiomyopathy, hepatomegaly and liver dysfunction, hypotonia, muscle weakness, exercise intolerance, developmental delay, delayed motor development and mental retardation. Some affected individuals manifest a fatal hypertrophic cardiomyopathy resulting in neonatal death. A subset of patients manifest Leigh syndrome. {ECO:0000269|PubMed:18499082}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;larynx;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus; medulla oblongata;subthalamic nucleus;thalamus;heart;temporal lobe;globus pallidus;pons;skeletal muscle;cingulate cortex; 0.11335 0.14225 -0.031067188 51.03798066 3.30437 0.12000 COX6B1P1 . . . cytochrome c oxidase subunit 6B1 pseudogene 1 . . . . . . . . . . . COX6B1P2 . . . cytochrome c oxidase subunit 6B1 pseudogene 2 . . . . . . . . . . . COX6B1P3 . . . cytochrome c oxidase subunit 6B1 pseudogene 3 . . . . . . . . . . . COX6B1P4 . . . cytochrome c oxidase subunit 6B1 pseudogene 4 . . . . . . . . . . . COX6B1P5 . . . cytochrome c oxidase subunit 6B1 pseudogene 5 . . . . . . . . . . . COX6B1P6 . . . cytochrome c oxidase subunit 6B1 pseudogene 6 . . . . . . . . . . . COX6B1P7 . . . cytochrome c oxidase subunit 6B1 pseudogene 7 . . . . . . . . . . . COX6B2 0.0487105755786073 0.684257859503509 0.267031564917884 cytochrome c oxidase subunit 6B2 FUNCTION: Connects the two COX monomers into the physiological dimeric form. {ECO:0000250}.; . TISSUE SPECIFICITY: Testis specific. Weak expression in thymus and heart. Expressed in cancer cell lines. {ECO:0000269|PubMed:12874793, ECO:0000269|PubMed:15905330}.; medulla oblongata;pancreas;pharynx;blood; . 0.07552 . 0.391453969 75.87284737 43.00825 1.24362 COX6C 0.230650731334253 0.646230672190783 0.123118596474965 cytochrome c oxidase subunit 6C FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.; . . myocardium;lymphoreticular;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;kidney;stomach;aorta; amygdala;whole brain;medulla oblongata;occipital lobe;testis - interstitial;thalamus;tongue;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;cingulate cortex;parietal lobe; 0.18186 0.08000 0.169169615 65.33380514 2321.07212 8.92170 COX6CP1 . . . cytochrome c oxidase subunit 6C pseudogene 1 . . . . . . . . . . . COX6CP2 . . . cytochrome c oxidase subunit 6C pseudogene 2 . . . . . . . . . . . COX6CP3 . . . cytochrome c oxidase subunit 6C pseudogene 3 . . . . . . . . . . . COX6CP4 . . . cytochrome c oxidase subunit 6C pseudogene 4 . . . . . . . . . . . COX6CP5 . . . cytochrome c oxidase subunit 6C pseudogene 5 . . . . . . . . . . . COX6CP6 . . . cytochrome c oxidase subunit 6C pseudogene 6 . . . . . . . . . . . COX6CP7 . . . cytochrome c oxidase subunit 6C pseudogene 7 . . . . . . . . . . . COX6CP8 . . . cytochrome c oxidase subunit 6C pseudogene 8 . . . . . . . . . . . COX6CP9 . . . cytochrome c oxidase subunit 6C pseudogene 9 . . . . . . . . . . . COX6CP10 . . . cytochrome c oxidase subunit 6C pseudogene 10 . . . . . . . . . . . COX6CP11 . . . cytochrome c oxidase subunit 6C pseudogene 11 . . . . . . . . . . . COX6CP12 . . . cytochrome c oxidase subunit 6C pseudogene 12 . . . . . . . . . . . COX6CP13 . . . cytochrome c oxidase subunit 6C pseudogene 13 . . . . . . . . . . . COX6CP14 . . . cytochrome c oxidase subunit 6C pseudogene 14 . . . . . . . . . . . COX6CP15 . . . cytochrome c oxidase subunit 6C pseudogene 15 . . . . . . . . . . . COX6CP16 . . . cytochrome c oxidase subunit 6C pseudogene 16 . . . . . . . . . . . COX6CP17 . . . cytochrome c oxidase subunit 6C pseudogene 17 . . . . . . . . . . . COX6CP18 . . . cytochrome c oxidase subunit 6C pseudogene 18 . . . . . . . . . . . COX7A1 0.00356251777188197 0.623621691694775 0.372815790533343 cytochrome c oxidase subunit 7A1 FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.; . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);trophoblast;heart;tongue;islets of Langerhans;urinary;muscle;lens;skeletal muscle;lung;placenta;macula lutea;alveolus;kidney; heart;tongue;skeletal muscle; 0.12471 0.12678 -0.009020804 52.8544468 54.18292 1.46875 COX7A2 0.3755612546357 0.577874541538967 0.0465642038253324 cytochrome c oxidase subunit 7A2 FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;cochlea;oesophagus;endometrium;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;cornea;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; whole brain;thalamus;occipital lobe;testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;temporal lobe;testis;pons;caudate nucleus;parietal lobe;cerebellum; 0.14003 . 0.080983847 59.76055674 42.08158 1.22562 COX7A2L 0.00041024940040515 0.406630152575054 0.592959598024541 cytochrome c oxidase subunit 7A2 like FUNCTION: Involved in the regulation of oxidative phosphorylation and energy metabolism (By similarity). Necessary for the assembly of mitochondrial respiratory supercomplex (By similarity). {ECO:0000250|UniProtKB:Q61387}.; . . medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;thymus; subthalamic nucleus;occipital lobe;adrenal gland;cerebellum peduncles;globus pallidus;pituitary; 0.15615 0.10837 -0.229483771 36.86010852 44.46888 1.27537 COX7A2P1 . . . cytochrome c oxidase subunit 7A2 pseudogene 1 . . . . . . . . . . . COX7A2P2 . . . cytochrome c oxidase subunit 7A2 pseudogene 2 . . . . . . . . . . . COX7B 0.656619051877437 0.319095308162576 0.0242856399599865 cytochrome c oxidase subunit 7B FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. Plays a role in proper central nervous system (CNS) development in vertebrates. {ECO:0000269|PubMed:23122588}.; DISEASE: Linear skin defects with multiple congenital anomalies 2 (LSDMCA2) [MIM:300887]: A distinct form of aplasia cutis congenita presenting as multiple linear skin defects on the face and neck associated with poor growth, microcephaly, and facial dysmorphism. Additional features include intellectual disability, nail dystrophy, short stature and cardiac abnormalities. {ECO:0000269|PubMed:23122588}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.06926 0.08399 0.279402865 70.86577023 89.85413 2.03933 COX7B2 0.474554621396108 0.440529412223779 0.0849159663801129 cytochrome c oxidase subunit 7B2 FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.; . . unclassifiable (Anatomical System);lung;testis;skin; . 0.07219 . 0.013025609 54.62962963 7.14566 0.26790 COX7BP1 . . . cytochrome c oxidase subunit 7B pseudogene 1 . . . . . . . . . . . COX7BP2 . . . cytochrome c oxidase subunit 7B pseudogene 2 . . . . . . . . . . . COX7C 0.545791853002404 0.399471357097815 0.0547367898997805 cytochrome c oxidase subunit 7C FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.; . . myocardium;lymphoreticular;ovary;rectum;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;tonsil;heart;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;kidney;stomach;aorta;cerebellum; whole brain;subthalamic nucleus;medulla oblongata;occipital lobe;thalamus;hypothalamus;temporal lobe;globus pallidus;kidney;parietal lobe;skeletal muscle; 0.00072 . 0.12325821 62.38499646 . . COX7CP1 . . . cytochrome c oxidase subunit 7C pseudogene 1 . . . . . . . . . . . COX8A 0.491407579691412 0.431709012467885 0.0768834078407035 cytochrome c oxidase subunit 8A FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.; . . myocardium;lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;nasopharynx;placenta;duodenum;kidney;stomach;thymus;cerebellum; whole brain;superior cervical ganglion;heart;liver;globus pallidus;ciliary ganglion;atrioventricular node;kidney; 0.04184 0.12726 0.257356108 69.83368719 18.76036 0.64750 COX8BP . . . cytochrome c oxidase subunit 8B, pseudogene . . . . . . . . . . . COX8C 0.144098451101148 0.629213967375124 0.226687581523729 cytochrome c oxidase subunit 8C FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.; . TISSUE SPECIFICITY: It is not yet known where COX8C is expressed.; unclassifiable (Anatomical System);lung;testis; . 0.06755 . 0.035072054 56.2514744 70.88445 1.75282 COX10 0.646572545927849 0.352135124420682 0.00129232965146916 COX10 heme A:farnesyltransferase cytochrome c oxidase assembly factor FUNCTION: Converts protoheme IX and farnesyl diphosphate to heme O. {ECO:0000250}.; DISEASE: Mitochondrial complex IV deficiency (MT-C4D) [MIM:220110]: A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs. Features include hypertrophic cardiomyopathy, hepatomegaly and liver dysfunction, hypotonia, muscle weakness, exercise intolerance, developmental delay, delayed motor development and mental retardation. Some affected individuals manifest a fatal hypertrophic cardiomyopathy resulting in neonatal death. A subset of patients manifest Leigh syndrome. {ECO:0000269|PubMed:10767350, ECO:0000269|PubMed:12928484}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;optic nerve;whole body;endometrium;synovium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;hypothalamus;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;medulla oblongata;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.03466 0.19518 0.755110637 86.7539514 5896.38929 15.92354 COX10-AS1 . . . COX10 antisense RNA 1 . . . . . . . . . . . COX11 0.402262800633254 0.588801464604158 0.00893573476258797 COX11 cytochrome c oxidase copper chaperone FUNCTION: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9878253}.; myocardium;ovary;skin;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;alveolus;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;pia mater;cornea;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; amygdala;subthalamic nucleus;superior cervical ganglion;globus pallidus;pons;trigeminal ganglion;parietal lobe;cingulate cortex;skeletal muscle; 0.09355 0.17027 0.014844891 54.94810097 42.54693 1.23476 COX11P1 . . . COX11 cytochrome c oxidase copper chaperone pseudogene 1 . . . . . . . . . . . COX14 0.193248416761832 0.647352464643779 0.159399118594389 COX14 cytochrome c oxidase assembly factor FUNCTION: Plays a role in the assembly or stability of the cytochrome c oxidase complex (COX). Requires for coordination of the early steps of COX assembly with the synthesis of MT-CO1. {ECO:0000269|PubMed:22243966, ECO:0000269|PubMed:22356826}.; DISEASE: Note=Defects in COX14 may be a cause of a mitochondrial disorder presenting with severe congenital lactic acidosis and dysmorphic features associated with a COX assembly defect. Other features include brain hypertrophy, diffuse alteration of the white-matter myelination, and numerous cavities in the parieto- occipital region, brainstem, and cerebellum, as well as hepatomegaly, hypertrophic cardiomyopathy, renal hypoplasia, and adrenal-gland hyperplasia. {ECO:0000269|PubMed:22243966}.; . . . 0.08763 . -0.031067188 51.03798066 2.29897 0.07797 COX15 2.16295028243055e-09 0.245340645474579 0.754659352362471 COX15 cytochrome c oxidase assembly homolog FUNCTION: May be involved in the biosynthesis of heme A. {ECO:0000269|PubMed:12474143}.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. {ECO:0000269|PubMed:15235026, ECO:0000269|PubMed:15863660}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly found in tissues characterized by high rates of oxidative phosphorylation (OxPhos), including muscle, heart, and brain. {ECO:0000269|PubMed:9878253}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;bile duct;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;adrenal cortex;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.40736 0.14741 -0.246069119 36.06982779 123.8909 2.42262 COX16 0.0304599840487893 0.809751099886092 0.159788916065119 COX16 cytochrome c oxidase assembly homolog . . . . . 0.17282 . -0.09720619 46.20193442 12.68708 0.46306 COX17 0.515141893437219 0.418317679961683 0.0665404266010981 COX17 cytochrome c oxidase copper chaperone FUNCTION: Copper chaperone for cytochrome c oxidase (COX). Binds two copper ions and deliver them to the Cu(A) site of COX (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10982038}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; . 0.28472 0.19420 0.101211609 60.95777306 712.96801 5.30525 COX17P1 . . . COX17 cytochrome c oxidase copper chaperone pseudogene 1 . . . . . . . . . . . COX18 3.71187019873397e-05 0.600337047631391 0.399625833666622 COX18 cytochrome c oxidase assembly factor FUNCTION: Required for the insertion of integral membrane proteins into the mitochondrial inner membrane. Essential for the activity and assembly of cytochrome c oxidase. Plays a central role in the translocation and export of the C-terminal part of the COX2 protein into the mitochondrial intermembrane space. {ECO:0000269|PubMed:16911509}.; . . unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;pineal body;developmental;colon;parathyroid;blood;fovea centralis;skin;prostate;whole body;lung;endometrium;bone;placenta;macula lutea;visual apparatus;liver;testis;spleen;kidney;brain;mammary gland;stomach; atrioventricular node; 0.06193 0.09770 -0.227663163 37.11370606 38.53686 1.14279 COX19 0.000108651204575146 0.209121863833483 0.790769484961942 COX19 cytochrome c oxidase assembly factor FUNCTION: May be required for the assembly of mitochondrial cytochrome c oxidase. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in skeletal muscle. {ECO:0000269|PubMed:16212937}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;sympathetic chain;colon;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;pancreas;prostate;optic nerve;lung;placenta;macula lutea;visual apparatus;liver;testis;spleen;germinal center;kidney;brain;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.02931 0.08845 0.369407109 74.95281906 61.78605 1.60187 COX20 0.0118854356661511 0.640070274975507 0.348044289358342 COX20 cytochrome c oxidase assembly factor . . . . . 0.15623 . 0.080983847 59.76055674 22.69107 0.75925 COX20P1 . . . COX20 cytochrome c oxidase assembly factor pseudogene 1 . . . . . . . . . . . COX20P2 . . . COX20 cytochrome c oxidase assembly factor pseudogene 2 . . . . . . . . . . . CP 0.000168752233046611 0.999777867092282 5.33806746714859e-05 ceruloplasmin (ferroxidase) FUNCTION: Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity). {ECO:0000250}.; DISEASE: Note=Ceruloplasmin levels are decreased in Wilson disease, in which copper cannot be incorporated into ceruloplasmin in liver because of defects in the copper-transporting ATPase 2.; TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; ovary;fovea centralis;choroid;bone marrow;retina;uterus;prostate;optic nerve;whole body;endometrium;testis;brain;gall bladder;unclassifiable (Anatomical System);cartilage;lacrimal gland;hypothalamus;blood;lens;skeletal muscle;breast;lung;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;kidney;stomach; fetal liver;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.43314 0.67252 0.253503589 69.70393961 528.1974 4.68960 CPA1 1.10123631470328e-05 0.807292049051256 0.192696938585597 carboxypeptidase A1 FUNCTION: Carboxypeptidase that catalyzes the release of a C- terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro. {ECO:0000269|PubMed:8806703}.; . . unclassifiable (Anatomical System);pancreas;lung;adrenal gland;islets of Langerhans;placenta;liver;spleen; superior cervical ganglion;fetal liver;pancreas;beta cell islets;atrioventricular node;skeletal muscle; 0.46709 0.37133 0.154398214 64.73814579 55.055 1.48685 CPA2 1.7428258238813e-08 0.397200064245282 0.60279991832646 carboxypeptidase A2 . . . unclassifiable (Anatomical System);pancreas;lung;islets of Langerhans;liver;colon;spleen;kidney;brain;stomach; dorsal root ganglion;pancreas;superior cervical ganglion;beta cell islets;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.61113 0.12860 -0.378346116 28.01368247 185.19923 2.95602 CPA3 1.2834341428345e-12 0.0466594465510439 0.953340553447673 carboxypeptidase A3 . . . unclassifiable (Anatomical System);heart;islets of Langerhans;skin;retina;bone marrow;uterus;prostate;lung;endometrium;cerebral cortex;nasopharynx;kidney;stomach; superior cervical ganglion;trigeminal ganglion; 0.17006 0.14718 1.510221359 95.4470394 414.09291 4.26220 CPA4 3.54914778603255e-07 0.79002006189438 0.209979583190842 carboxypeptidase A4 FUNCTION: Metalloprotease that could be involved in the histone hyperacetylation pathway. {ECO:0000269|PubMed:10383164}.; . TISSUE SPECIFICITY: Fetal expression in the adrenal gland, brain, heart, intestine, kidney, liver and lung. Except for fetal brain that shows no imprinting, expression was found preferentially from the maternal allele.; unclassifiable (Anatomical System);heart;lacrimal gland;tongue;skin;breast;pancreas;endometrium;mesenchyma;bone;visual apparatus;hypopharynx;amnion;head and neck;kidney;stomach; superior cervical ganglion;testis - seminiferous tubule;temporal lobe;atrioventricular node;skin;skeletal muscle; 0.27010 0.11448 -0.308569083 32.17150271 5589.7378 15.46250 CPA5 0.0474887384414102 0.94744205284274 0.00506920871584992 carboxypeptidase A5 . . TISSUE SPECIFICITY: Expression is very low or not detectable.; optic nerve;lung;macula lutea;testis;fovea centralis;choroid;lens;retina; . 0.19249 0.16405 0.356452144 74.62845011 2645.82422 9.64784 CPA6 1.6994617793848e-09 0.605516600603126 0.394483397697412 carboxypeptidase A6 FUNCTION: May be involved in the proteolytic inactivation of enkephalins and neurotensin in some brain areas. May convert inactive angiotensin I into the biologically active angiotensin II. {ECO:0000269|PubMed:18178555}.; DISEASE: Epilepsy, familial temporal lobe, 5 (ETL5) [MIM:614417]: A focal form of epilepsy characterized by recurrent seizures that arise from foci within the temporal lobe. Seizures are usually accompanied by sensory symptoms, most often auditory in nature. {ECO:0000269|PubMed:21922598}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Febrile seizures, familial, 11 (FEB11) [MIM:614418]: Seizures associated with febrile episodes in childhood without any evidence of intracranial infection or defined pathologic or traumatic cause. It is a common condition, affecting 2-5% of children aged 3 months to 5 years. The majority are simple febrile seizures (generally defined as generalized onset, single seizures with a duration of less than 30 minutes). Complex febrile seizures are characterized by focal onset, duration greater than 30 minutes, and/or more than one seizure in a 24 hour period. The likelihood of developing epilepsy following simple febrile seizures is low. Complex febrile seizures are associated with a moderately increased incidence of epilepsy. {ECO:0000269|PubMed:21922598}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the hippocampus, nucleus raphe, and cortex. {ECO:0000269|PubMed:21922598}.; unclassifiable (Anatomical System);prostate;brain;retina;bone marrow; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.23633 0.13365 0.733063566 86.27034678 3844.35561 12.21287 CPAMD8 2.01801525841884e-14 0.999974749452667 2.52505473128029e-05 C3 and PZP like, alpha-2-macroglobulin domain containing 8 . . TISSUE SPECIFICITY: Highly expressed in the kidney, brain and testis and to a lower extent in heart, liver and small intestine. {ECO:0000269|PubMed:15177561}.; unclassifiable (Anatomical System);ovary;cartilage;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;endometrium;larynx;placenta;bone;macula lutea;visual apparatus;iris;testis;head and neck;kidney;brain; . 0.10307 0.10452 2.440614487 98.54918613 4982.63255 14.40066 CPAT1 . . . cerebral palsy, ataxic 1 . . . . . . . . . . . CPB1 2.26972023407954e-14 0.00846923545394225 0.991530764546035 carboxypeptidase B1 . . TISSUE SPECIFICITY: Pancreas. {ECO:0000269|PubMed:2920728}.; unclassifiable (Anatomical System);breast;pancreas;lung;islets of Langerhans;placenta;liver;spleen;mammary gland; dorsal root ganglion;pancreas;superior cervical ganglion;adrenal gland;beta cell islets;adrenal cortex;atrioventricular node;trigeminal ganglion; 0.60431 0.15975 0.442818085 77.8544468 263.77113 3.48473 CPB2 2.80849135453329e-06 0.922362960204773 0.0776342313038719 carboxypeptidase B2 FUNCTION: Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down- regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin. {ECO:0000269|PubMed:10574983}.; . TISSUE SPECIFICITY: Plasma; synthesized in the liver.; unclassifiable (Anatomical System);uterus;whole body;heart;liver;spleen;brain;skin;gall bladder; superior cervical ganglion;fetal liver;liver;fetal lung; 0.04116 0.21242 -0.224023033 37.4321774 1915.89895 8.05461 CPB2-AS1 . . . CPB2 antisense RNA 1 . . . . . . . . . . . CPD 0.247131561049324 0.752868346973316 9.19773597847951e-08 carboxypeptidase D . . TISSUE SPECIFICITY: Highly expressed in placenta, pancreas and hepatoma cells. Lower levels found in skeletal muscle, heart and colon carcinoma and melanoma cell lines.; lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;bile duct;lung;placenta;head and neck;kidney;stomach; testis - interstitial;trachea;testis - seminiferous tubule;placenta;testis;skeletal muscle; 0.86256 . -0.020150552 52.25288983 414.83764 4.26576 CPE 0.997846906408955 0.00215302496074487 6.86302998914627e-08 carboxypeptidase E FUNCTION: Removes residual C-terminal Arg or Lys remaining after initial endoprotease cleavage during prohormone processing. Processes proinsulin.; . TISSUE SPECIFICITY: Isoform 2, but not isoform 1, is overexpressed in hepatocellular carcinoma (at protein level), as well as in other tumors, including pheochromocytomas and paragangliomas. {ECO:0000269|PubMed:21285511}.; sympathetic chain;colon;skin;retina;uterus;prostate;whole body;frontal lobe;larynx;thyroid;bone;pituitary gland;testis;dura mater;ciliary body;brain;artery;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;hypothalamus;spinal cord;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;nasopharynx;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach;aorta; whole brain;amygdala;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;prostate;subthalamic nucleus;thyroid;prefrontal cortex;globus pallidus;ciliary ganglion;pituitary;cingulate cortex;parietal lobe;cerebellum; 0.71178 0.25258 -0.047654689 50.22410946 45.06523 1.28909 CPEB1 0.999591314438397 0.000408684366008655 1.19559457168537e-09 cytoplasmic polyadenylation element binding protein 1 FUNCTION: Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU- 3') within the mRNA 3'-UTR. In absence of phosphorylation and in association with TACC3 is also involved as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation (By similarity). Involved in the transport of CPE-containing mRNA to dendrites; those mRNAs may be transported to dendrites in a translationally dormant form and translationally activated at synapses (By similarity). Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation (By similarity). Induces the assembly of stress granules in the absence of stress. {ECO:0000250, ECO:0000269|PubMed:15731006, ECO:0000269|PubMed:15966895}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in immature oocytes, ovary, brain and heart. Isoform 2 is expressed in brain and heart. Isoform 3 and isoform 4 are expressed in brain. Expressed in breast tumors and several tumor cell lines. {ECO:0000269|PubMed:11223249, ECO:0000269|PubMed:15731006, ECO:0000269|PubMed:15966895}.; unclassifiable (Anatomical System);hypothalamus;choroid;fovea centralis;lens;skin;retina;pancreas;optic nerve;lung;adrenal gland;macula lutea;testis;brain; amygdala;whole brain;occipital lobe;superior cervical ganglion;testis - seminiferous tubule;hypothalamus;prefrontal cortex;testis; 0.40504 0.10369 -0.556537043 19.72753008 3672.85414 11.77381 CPEB1-AS1 . . . CPEB1 antisense RNA 1 . . . . . . . . . . . CPEB2 0.992723048645125 0.00727689637399888 5.49808757477837e-08 cytoplasmic polyadenylation element binding protein 2 FUNCTION: May play a role in translational regulation of stored mRNAs in transcriptionally inactive haploid spermatids. Binds to poly(U) RNA oligomers (By similarity). {ECO:0000250}.; . . colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;testis;germinal center;artery;brain;unclassifiable (Anatomical System);lymph node;small intestine;heart;islets of Langerhans;lens;skeletal muscle;breast;lung;visual apparatus;macula lutea;liver;alveolus;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13810 0.08827 . . 7117.46893 18.15653 CPEB2-AS1 . . . CPEB2 antisense RNA 1 (head to head) . . . . . . . . . . . CPEB3 0.994664051960669 0.00533582078087633 1.27258455198747e-07 cytoplasmic polyadenylation element binding protein 3 . . . skin;endometrium;thyroid;bone;testis;dura mater;brain;unclassifiable (Anatomical System);amygdala;meninges;cartilage;islets of Langerhans;lens;skeletal muscle;bile duct;lung;pia mater;nasopharynx;visual apparatus;liver;cervix;spleen;head and neck;kidney;cerebellum; superior cervical ganglion;thyroid;pons;kidney;trigeminal ganglion;skeletal muscle;cerebellum; 0.78253 0.11140 -0.426079032 25.36565228 524.24587 4.67134 CPEB4 0.996854727820052 0.00314526509598533 7.08396234479541e-09 cytoplasmic polyadenylation element binding protein 4 . . . lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;tonsil;heart;cartilage;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;kidney;stomach;aorta; globus pallidus;atrioventricular node; 0.67807 0.11104 -0.22584292 37.32012267 29.93649 0.95618 CPED1 8.34882400764031e-17 0.200982771537398 0.799017228462602 cadherin like and PC-esterase domain containing 1 . . . . . 0.05718 0.08454 -0.014692675 52.35314933 880.81478 5.78086 CPHL1P . . . ceruloplasmin and hephaestin-like 1 pseudogene . . . . . . . . . . . CPHXL . . . cytoplasmic polyadenylated homeobox like . . . . . . . . . . . CPLX1 0.795789957123327 0.198417498217487 0.0057925446591862 complexin 1 FUNCTION: Positively regulates a late step in synaptic vesicle exocytosis. Organizes the SNAREs into a cross-linked zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion, thereby preventing SNAREs from releasing neurotransmitters until an action potential arrives at the synapse. Also involved in glucose-induced secretion of insulin by pancreatic beta-cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:21785414}.; . TISSUE SPECIFICITY: Nervous system. In hippocampus and cerebellum, expressed mainly by inhibitory neurons. Overexpressed in substantia nigra from patients with Parkinson disease. {ECO:0000269|PubMed:11483314, ECO:0000269|PubMed:15526345, ECO:0000269|PubMed:9853440}.; unclassifiable (Anatomical System);ovary;cerebellum cortex;islets of Langerhans;colon;fovea centralis;choroid;lens;retina;optic nerve;lung;macula lutea;visual apparatus;hippocampus;testis;germinal center;mammary gland;pineal gland;brain;thymus;cerebellum; amygdala;subthalamic nucleus;medulla oblongata;atrioventricular node;caudate nucleus;trigeminal ganglion;cerebellum; . . -0.163345027 41.24793583 14.87804 0.53555 CPLX2 0.717836321082537 0.268172746425247 0.0139909324922154 complexin 2 FUNCTION: Negatively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. Positively regulates a late step in synaptic vesicle exocytosis. Also involved in mast cell exocytosis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Nervous system. In hippocampus and cerebellum, expressed mainly by excitatory neurons. Down-regulated in brain cortex from patients suffering from Huntington disease, bipolar disorder or major depression. Down-regulated in cerebellum from patients with schizophrenia. {ECO:0000269|PubMed:11483314, ECO:0000269|PubMed:11576753, ECO:0000269|PubMed:15906159, ECO:0000269|PubMed:16162394, ECO:0000269|PubMed:9853440}.; skeletal muscle; amygdala;whole brain;superior cervical ganglion;occipital lobe;medulla oblongata;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.35548 0.11262 0.013025609 54.62962963 6.77928 0.25022 CPLX3 0.385406550550488 0.571014001651166 0.0435794477983457 complexin 3 FUNCTION: Positively regulates a late step in synaptic vesicle exocytosis. {ECO:0000250}.; . . . . 0.21631 . 0.014844891 54.94810097 29.6682 0.94734 CPLX4 0.00218941569433162 0.518782922611977 0.479027661693692 complexin 4 FUNCTION: Positively regulates a late step in synaptic vesicle exocytosis. {ECO:0000250}.; . . unclassifiable (Anatomical System);pineal body;macula lutea;visual apparatus;fovea centralis;skeletal muscle; superior cervical ganglion; 0.20703 0.09644 -0.09720619 46.20193442 28.81864 0.92145 CPM 8.0712082035317e-07 0.495058126472182 0.504941066406998 carboxypeptidase M FUNCTION: Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins. {ECO:0000269|PubMed:12457462}.; . . ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;lens;bile duct;lung;placenta;macula lutea;liver;cervix;spleen;kidney; adipose tissue; 0.16436 0.19109 0.483275131 79.25218212 1875.42019 7.96474 CPN1 1.32620038323609e-06 0.60179180968284 0.398206864116777 carboxypeptidase N subunit 1 FUNCTION: Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation.; . TISSUE SPECIFICITY: Synthesized in the liver and secreted in plasma.; . . 0.11193 0.27340 -0.556537043 19.72753008 239.62681 3.34532 CPN2 0.00023179534317588 0.515162369396546 0.484605835260278 carboxypeptidase N subunit 2 FUNCTION: The 83 kDa subunit binds and stabilizes the catalytic subunit at 37 degrees Celsius and keeps it in circulation. Under some circumstances it may be an allosteric modifier of the catalytic subunit.; . . unclassifiable (Anatomical System);liver;colon;spleen;kidney;stomach; superior cervical ganglion;liver;kidney;skeletal muscle; 0.20326 0.17204 0.293954043 71.62066525 1612.26961 7.43058 CPNE1 3.87095095726686e-07 0.94236479886134 0.0576348140435642 copine 1 FUNCTION: Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes (PubMed:14674885). Involved in the TNF-alpha receptor signaling pathway in a calcium-dependent manner (PubMed:14674885). Exhibits calcium-dependent phospholipid binding properties (PubMed:9430674, PubMed:19539605). Plays a role in neuronal progenitor cell differentiation; induces neurite outgrowth via a AKT-dependent signaling cascade and calcium-independent manner (PubMed:23263657, PubMed:25450385). May recruit target proteins to the cell membrane in a calcium-dependent manner (PubMed:12522145). May function in membrane trafficking (PubMed:9430674). Involved in TNF-alpha- induced NF-kappa-B transcriptional repression by inducing endoprotease processing of the transcription factor NF-kappa-B p65/RELA subunit (PubMed:18212740). Also induces endoprotease processing of NF-kappa-B p50/NFKB1, p52/NFKB2, RELB and REL (PubMed:18212740). {ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:14674885, ECO:0000269|PubMed:18212740, ECO:0000269|PubMed:19539605, ECO:0000269|PubMed:23263657, ECO:0000269|PubMed:25450385, ECO:0000269|PubMed:9430674}.; . TISSUE SPECIFICITY: Expressed in neutrophils (at protein level) (PubMed:12949241). Widely expressed. Expressed in the brain. Expressed in neutrophil precursors from bone marrow and peripheral blood (PubMed:12949241). {ECO:0000269|PubMed:12949241}.; ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;colon;choroid;fovea centralis;vein;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;hypopharynx;amnion;head and neck;kidney;stomach;aorta; superior cervical ganglion; 0.11193 0.18648 1.001272896 90.72304789 5735.67228 15.69514 CPNE2 0.544003069972159 0.455971183090322 2.57469375189379e-05 copine 2 FUNCTION: Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes. Exhibits calcium-dependent cell membrane binding properties. {ECO:0000250|UniProtKB:P59108}.; . TISSUE SPECIFICITY: Expressed in the brain. Expressed in neutrophil precursors from the bone marrow and peripheral blood (PubMed:12949241).; ovary;umbilical cord;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;blood;lens;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney; . 0.19896 0.11604 -0.955204708 9.170794999 29.12037 0.93107 CPNE3 5.16184252829367e-13 0.0524276603701238 0.94757233962936 copine 3 FUNCTION: Calcium-dependent phospholipid-binding protein that plays a role in ERBB2-mediated tumor cell migration in response to growth factor heregulin stimulation (PubMed:20010870). {ECO:0000269|PubMed:20010870}.; . TISSUE SPECIFICITY: Expressed in breast and weakly in prostate and ovarian tissues (PubMed:20010870). Expressed in neutrophils (at protein level) (PubMed:12949241). Widely expressed (PubMed:11041869). Expressed in the brain. Expressed in neutrophil precursors from the bone marrow and peripheral blood (PubMed:12949241). Expressed in primary breast tumors and ovarian endometrioid adenocarcinoma (PubMed:20010870). {ECO:0000269|PubMed:11041869, ECO:0000269|PubMed:12949241, ECO:0000269|PubMed:20010870}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;placenta;head and neck;kidney;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle;bone marrow; 0.33166 0.11755 0.378498378 75.58386412 3378.31953 11.13211 CPNE4 0.775139285096664 0.224847040354468 1.36745488681503e-05 copine 4 FUNCTION: Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes. {ECO:0000250|UniProtKB:Q99829}.; . TISSUE SPECIFICITY: Widely expressed (PubMed:12670487, PubMed:12949241). Expressed strongly in the brain, heart and prostate (PubMed:12670487, PubMed:12949241). Expressed strongly in peripheral blood leukocytes (PubMed:12949241). {ECO:0000269|PubMed:12670487, ECO:0000269|PubMed:12949241}.; . . 0.35306 0.10522 -0.80269335 12.23755603 19.03654 0.65757 CPNE5 0.0778897502698332 0.922090931029995 1.93187001716865e-05 copine 5 FUNCTION: Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes (By similarity). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000250|UniProtKB:Q99829, ECO:0000269|PubMed:23999003}.; . TISSUE SPECIFICITY: Expressed in the brain, heart, stomach, spleen, lymph node and testis (PubMed:12949241). Expressed in melanocytes (PubMed:23999003). {ECO:0000269|PubMed:12949241, ECO:0000269|PubMed:23999003}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;heart;ovary;colon;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;lung;macula lutea;testis;germinal center;kidney;brain;stomach; . 0.27410 0.10478 -0.999300439 8.368719038 56.11112 1.50471 CPNE6 0.918263625967071 0.0817354625178832 9.1151504577917e-07 copine 6 FUNCTION: Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes. Binds phospholipid membranes in a calcium-dependent manner (By similarity). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000250|UniProtKB:Q9Z140, ECO:0000269|PubMed:23999003}.; . TISSUE SPECIFICITY: Widely expressed in the brain (PubMed:9645480, PubMed:10403379, PubMed:12949241). Expressed weakly in the kidney, liver and fetal heart (PubMed:12949241). Expressed in melanocytes (PubMed:23999003). {ECO:0000269|PubMed:10403379, ECO:0000269|PubMed:12949241, ECO:0000269|PubMed:23999003, ECO:0000269|PubMed:9645480}.; unclassifiable (Anatomical System);lung;frontal lobe;hypothalamus;hippocampus;testis;blood;choroid;kidney;brain;skeletal muscle; whole brain;amygdala;thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;atrioventricular node;skin;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex; 0.19884 0.11036 -0.644723694 16.52512385 62.30557 1.61152 CPNE7 1.63023438294019e-13 0.0268687744232942 0.973131225576543 copine 7 FUNCTION: Calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes. {ECO:0000250|UniProtKB:Q99829}.; . TISSUE SPECIFICITY: Expressed in the brain, testis, thymus and small intestine (PubMed:10534407, PubMed:12949241). {ECO:0000269|PubMed:10534407, ECO:0000269|PubMed:12949241}.; unclassifiable (Anatomical System);cartilage;colon;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;frontal lobe;placenta;bone;macula lutea;testis;brain;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.10022 . -1.343026423 4.647322482 1754.91457 7.73074 CPNE8 0.07800427323508 0.921900501559329 9.52252055915567e-05 copine 8 FUNCTION: Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes. {ECO:0000250|UniProtKB:Q99829}.; . . smooth muscle;colon;parathyroid;vein;skin;uterus;prostate;thyroid;testis;dura mater;brain;gall bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;urinary;blood;lens;pancreas;lung;pia mater;visual apparatus;liver;head and neck;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.10316 0.12678 -0.404032746 26.53338051 55.25086 1.49185 CPNE9 0.0010321031792749 0.998871291674588 9.66051461366837e-05 copine family member 9 FUNCTION: Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes (By similarity). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000250|UniProtKB:Q99829, ECO:0000269|PubMed:23999003}.; . TISSUE SPECIFICITY: Expressed in melanocytes (PubMed:23999003). {ECO:0000269|PubMed:23999003}.; islets of Langerhans;brain; thalamus;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle;cerebellum; 0.25543 . 0.084621747 60.31493277 44.06764 1.26466 CPO 1.82892275396605e-13 0.00780541686220111 0.992194583137616 carboxypeptidase O FUNCTION: Probable carboxypeptidase which may cleave proteins with C-terminal acidic residues. {ECO:0000250}.; . . brain; . 0.09527 0.09424 0.665103516 84.6131163 5008.21771 14.45606 CPOX 0.0232273467536485 0.962079525403287 0.0146931278430646 coproporphyrinogen oxidase FUNCTION: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.; DISEASE: Hereditary coproporphyria (HCP) [MIM:121300]: A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. Hereditary coproporphyria is an acute hepatic porphyria characterized by skin photosensitivity, attacks of abdominal pain, neurological disturbances, and psychiatric symptoms. Most attacks are precipitated by drugs, alcohol, caloric deprivation, infections, or endocrine factors. Hereditary coproporphyria is biochemically characterized by overexcretion of coproporphyrin III in the urine and in the feces. {ECO:0000269|PubMed:12181641, ECO:0000269|PubMed:15896662, ECO:0000269|PubMed:16398658, ECO:0000269|PubMed:7757079, ECO:0000269|PubMed:7849704, ECO:0000269|PubMed:8012360, ECO:0000269|PubMed:8990017, ECO:0000269|PubMed:9048920, ECO:0000269|PubMed:9298818, ECO:0000269|PubMed:9888388}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;colon;blood;skeletal muscle;uterus;bile duct;prostate;pancreas;lung;endometrium;bone;placenta;visual apparatus;duodenum;liver;testis;cervix;spleen;kidney;brain;mammary gland;stomach; superior cervical ganglion;fetal liver; 0.54329 0.14172 0.41713504 76.95800896 3622.54592 11.67473 CPP . . . ceruloplasmin (ferroxidase) pseudogene . . . . . . . . . . . CPPED1 3.25892031250431e-10 0.024062528853431 0.975937470820677 calcineurin-like phosphoesterase domain containing 1 FUNCTION: Protein phosphatase that dephosphorylates AKT family kinase specifically at 'Ser-473', blocking cell cycle progression and promoting cell apoptosis. May play an inhibitory role in glucose uptake by adipocytes. {ECO:0000269|PubMed:23799035, ECO:0000269|PubMed:23939394}.; . TISSUE SPECIFICITY: Expressed in subcutaneous adipose tissue. {ECO:0000269|PubMed:23939394}.; myocardium;ovary;sympathetic chain;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; ciliary ganglion; . . 1.287903524 93.83698986 3059.82701 10.52025 CPQ 7.3007030738252e-10 0.0730334035594705 0.926966595710459 carboxypeptidase Q FUNCTION: Carboxypeptidase that may play an important role in the hydrolysis of circulating peptides. Catalyzes the hydrolysis of dipeptides with unsubstituted terminals into amino acids. May play a role in the liberation of thyroxine hormone from its thyroglobulin (Tg) precursor.; . TISSUE SPECIFICITY: Mainly detected in blood plasma. Abundant in placenta and kidney. Present at low level in muscles, liver and skin fibroblasts. Not detected in brain or white blood cells (at protein level). {ECO:0000269|PubMed:10206990}.; . . . . 0.86534717 88.80042463 469.95991 4.48715 CPS1 0.0833573677195577 0.916642631094805 1.18563737508237e-09 carbamoyl-phosphate synthase 1 FUNCTION: Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell.; DISEASE: Carbamoyl phosphate synthetase 1 deficiency (CPS1D) [MIM:237300]: An autosomal recessive disorder of the urea cycle causing hyperammonemia. It can present as a devastating metabolic disease dominated by severe hyperammonemia in neonates or as a more insidious late-onset condition, generally manifesting as life-threatening hyperammonemic crises under catabolic situations. Clinical features include protein intolerance, intermittent ataxia, seizures, lethargy, developmental delay and mental retardation. {ECO:0000269|PubMed:11388595, ECO:0000269|PubMed:11474210, ECO:0000269|PubMed:12655559, ECO:0000269|PubMed:12955727, ECO:0000269|PubMed:15164414, ECO:0000269|PubMed:15617192, ECO:0000269|PubMed:16737834, ECO:0000269|PubMed:17310273, ECO:0000269|PubMed:20578160, ECO:0000269|PubMed:21120950, ECO:0000269|PubMed:9711878}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pulmonary hypertension, neonatal (PHN) [MIM:615371]: A disease characterized by elevated pulmonary artery pressure. Pulmonary hypertension in the neonate is associated with multiple underlying problems such as respiratory distress syndrome, meconium aspiration syndrome, congenital diaphragmatic hernia, bronchopulmonary dysplasia, sepsis, or congenital heart disease. {ECO:0000269|PubMed:11407344}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. CPS1 variants influence the availability of precursors for nitric oxide (NO) synthesis and play a role in clinical situations where endogenous NO production is critically important, such as neonatal pulmonary hypertension, increased pulmonary artery pressure following surgical repair of congenital heart defects or hepatovenocclusive disease following bone marrow transplantation. Infants with neonatal pulmonary hypertension homozygous for Thr- 1406 have lower L-arginine concentrations than neonates homozygous for Asn-1406 (PubMed:11407344). {ECO:0000269|PubMed:11407344}.; TISSUE SPECIFICITY: Primarily in the liver and small intestine.; unclassifiable (Anatomical System);heart;skin;skeletal muscle;uterus;pancreas;whole body;lung;bone;placenta;liver;testis;spleen;cervix;kidney;brain;stomach;gall bladder; dorsal root ganglion;fetal liver;superior cervical ganglion;liver;fetal lung;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.70374 0.26404 -0.630196893 16.8141071 6992.13025 17.82122 CPS1-IT1 . . . CPS1 intronic transcript 1 . . . . . . . . . . . CPSF1 0.0011044541536769 0.998895398905529 1.46940794557014e-07 cleavage and polyadenylation specific factor 1 FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre- mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. This subunit is involved in the RNA recognition step of the polyadenylation reaction. {ECO:0000269|PubMed:14749727}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;placenta;hippocampus;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.24423 0.13079 -3.400182535 0.371549894 168.25385 2.83150 CPSF1P1 . . . cleavage and polyadenylation specific factor 1 pseudogene 1 . . . . . . . . . . . CPSF2 7.81001536480669e-05 0.996016736330282 0.0039051635160703 cleavage and polyadenylation specific factor 2 FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Involved in the histone 3' end pre-mRNA processing. {ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:18688255}.; . . ovary;skin;retina;uterus;prostate;cerebral cortex;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;spinal cord;muscle;blood;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;thymus; dorsal root ganglion;subthalamic nucleus;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.18633 0.14783 -0.66859065 15.76433121 28.99401 0.92722 CPSF3 3.4570475120286e-05 0.997410280445909 0.00255514907897106 cleavage and polyadenylation specific factor 3 FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Has endonuclease activity, and functions as mRNA 3'-end-processing endonuclease. Also involved in the histone 3'-end pre-mRNA processing. U7 snRNP- dependent protein that induces both the 3'-endoribonucleolytic cleavage of histone pre-mRNAs and acts as a 5' to 3' exonuclease for degrading the subsequent downstream cleavage product (DCP) of mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3' sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the upstream fragment containing the stem loop (SL) and 5' phosphate on the downstream cleavage product (DCP) starting with CU nucleotides. The U7-dependent 5' to 3' exonuclease activity is processive and degrades the DCP RNA substrate even after complete removal of the U7-binding site. Binds to the downstream cleavage product (DCP) of histone pre-mRNAs and the cleaved DCP RNA substrate in a U7 snRNP dependent manner. {ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:15037765, ECO:0000269|PubMed:17128255, ECO:0000269|PubMed:18688255}.; . . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;bile duct;lung;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;tumor;testis; 0.16707 . -0.558357437 19.54470394 35.81924 1.07713 CPSF3L 5.7881402380741e-09 0.846463747518153 0.153536246693706 cleavage and polyadenylation specific factor 3-like FUNCTION: Catalytic component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates the snRNAs 3' cleavage. {ECO:0000269|PubMed:16239144}.; . . lymphoreticular;myocardium;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;muscle;blood;lens;breast;bile duct;pancreas;lung;adrenal gland;mesenchyma;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - seminiferous tubule;testis;parietal lobe; 0.15963 0.12052 -1.815166288 2.164425572 40.61404 1.19043 CPSF4 0.629613784158072 0.368882728904794 0.00150348693713435 cleavage and polyadenylation specific factor 4 FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. CPSF4 binds RNA polymers with a preference for poly(U). {ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:9224719}.; . . lymphoreticular;medulla oblongata;ovary;colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;skeletal muscle;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;testis;trigeminal ganglion; 0.31460 0.17050 -0.163345027 41.24793583 12.32758 0.44703 CPSF4L . . . cleavage and polyadenylation specific factor 4-like . . . . . 0.14110 . -0.119252484 44.53880632 19.0294 0.65705 CPSF6 0.999113680151761 0.000886318252716417 1.59552279344357e-09 cleavage and polyadenylation specific factor 6 FUNCTION: Component of the cleavage factor Im complex (CFIm) that plays a key role in pre-mRNA 3'-processing. Involved in association with NUDT21/CPSF5 in pre-MRNA 3'-end poly(A) site cleavage and poly(A) addition. CPSF6 binds to cleavage and polyadenylation RNA substrates and promotes RNA looping. {ECO:0000269|PubMed:14690600, ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:21295486, ECO:0000269|PubMed:8626397, ECO:0000269|PubMed:9659921}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;mesenchyma;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;cervix;spleen;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;white blood cells; 0.46318 0.14229 -0.361761279 28.6329323 7.75283 0.28565 CPSF7 0.991330175057795 0.00866940785755102 4.17084654110575e-07 cleavage and polyadenylation specific factor 7 FUNCTION: Component of the cleavage factor Im complex (CFIm) that plays a key role in pre-mRNA 3'-processing. Binds to cleavage and polyadenylation RNA substrates. {ECO:0000269|PubMed:8626397}.; . . myocardium;ovary;salivary gland;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;amnion;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; occipital lobe;superior cervical ganglion;testis;caudate nucleus;trigeminal ganglion;skeletal muscle;cerebellum; . . -0.626318434 17.03231894 16.33135 0.57846 CPT1A 0.9391397334386 0.0608602489434432 1.76179567452108e-08 carnitine palmitoyltransferase 1A FUNCTION: Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Plays an important role in triglyceride metabolism.; DISEASE: Carnitine palmitoyltransferase 1A deficiency (CPT1AD) [MIM:255120]: Rare autosomal recessive metabolic disorder of long- chain fatty acid oxidation characterized by severe episodes of hypoketotic hypoglycemia usually occurring after fasting or illness. Onset is in infancy or early childhood. {ECO:0000269|PubMed:11350182, ECO:0000269|PubMed:11441142, ECO:0000269|PubMed:12189492, ECO:0000269|PubMed:14517221, ECO:0000269|PubMed:15110323, ECO:0000269|PubMed:15669684, ECO:0000269|PubMed:9691089}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Strong expression in kidney and heart, and lower in liver and skeletal muscle.; colon;skin;retina;bone marrow;uterus;prostate;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);blood;skeletal muscle;breast;lung;mesenchyma;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11869 0.57549 -0.483123186 22.78249587 317.78824 3.78518 CPT1B 2.03406716145902e-09 0.85649175152972 0.143508246436213 carnitine palmitoyltransferase 1B . . TISSUE SPECIFICITY: Strong expression in heart and skeletal muscle. No expression in liver and kidney.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;germinal center;brain;heart;cartilage;tongue;blood;skeletal muscle;breast;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;bile duct;pancreas;lung;pia mater;placenta;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.11227 0.34846 -0.661316159 16.02382637 3798.40045 12.09258 CPT1C 0.0002846277169503 0.999590885853401 0.000124486429648468 carnitine palmitoyltransferase 1C FUNCTION: May play a role in lipid metabolic process. {ECO:0000269|PubMed:25751282}.; . TISSUE SPECIFICITY: Expressed predominantly in brain and testis. Expressed in motor neurons. {ECO:0000269|PubMed:12376098, ECO:0000269|PubMed:25751282}.; unclassifiable (Anatomical System);cartilage;heart;ovary;pineal body;colon;parathyroid;choroid;skeletal muscle;uterus;prostate;optic nerve;lung;frontal lobe;bone;placenta;hippocampus;duodenum;testis;kidney;brain;pineal gland;stomach; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.20362 . -0.705410796 14.77942911 101.01814 2.17533 CPT2 4.77178075381137e-07 0.391954088476973 0.608045434344952 carnitine palmitoyltransferase 2 . DISEASE: Carnitine palmitoyltransferase 2 deficiency late-onset (CPT2D) [MIM:255110]: Autosomal recessive disorder characterized by recurrent myoglobinuria, episodes of muscle pain, stiffness, and rhabdomyolysis. These symptoms are triggered by prolonged exercise, fasting or viral infection and patients are usually young adults. In addition to this classical, late-onset, muscular type, a hepatic or hepatocardiomuscular form has been reported in infants. Clinical pictures in these children or neonates include hypoketotic hypoglycemia, liver dysfunction, cardiomyopathy and sudden death. {ECO:0000269|PubMed:10090476, ECO:0000269|PubMed:11477613, ECO:0000269|PubMed:14605500, ECO:0000269|PubMed:14615409, ECO:0000269|PubMed:1528846, ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15622536, ECO:0000269|PubMed:7711730, ECO:0000269|PubMed:8358442, ECO:0000269|PubMed:8651281, ECO:0000269|PubMed:9600456, ECO:0000269|PubMed:9758712, ECO:0000269|Ref.13, ECO:0000269|Ref.17}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Carnitine palmitoyltransferase 2 deficiency infantile (CPT2DI) [MIM:600649]: A disorder of mitochondrial long-chain fatty acid oxidation characterized by hepatic or hepato-cardio- muscular manifestations with onset in infancy. Clinical features include hypoketotic hypoglycemia, lethargy, seizures, hepatomegaly, liver dysfunction, cardiomegaly and dilated cardiomyopathy. {ECO:0000269|PubMed:1528846, ECO:0000269|PubMed:8651281}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Carnitine palmitoyltransferase 2 deficiency lethal neonatal (CPT2D-LN) [MIM:608836]: Lethal neonatal form of CPT2D. This rarely presentation is antenatal with cerebral periventricular cysts and cystic dysplastic kidneys. The clinical variability of the disease is likely attributed to the variable residual enzymatic activity. {ECO:0000269|PubMed:11477613}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Encephalopathy, acute, infection-induced, 4 (IIAE4) [MIM:614212]: A severe neurologic complication of an infection. It manifests within days in otherwise healthy children after common viral infections, without evidence of viral infection of the brain or inflammatory cell infiltration. In affected children, high- grade fever is accompanied within 12 to 48 hours by febrile convulsions, often leading to coma, multiple-organ failure, brain edema, and high morbidity and mortality. The infections are usually viral, particularly influenza, although other viruses and even mycoplasma have been found to cause the disorder. {ECO:0000269|PubMed:15811315, ECO:0000269|PubMed:21697855}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. CPT2 polymorphic variants do not cause classical carnitine palmitoyltransferase 2 deficiency, and patients harboring any of them are asymptomatic most of the time. However, they are prone to viral infection (high fever)-related encephalopathy (PubMed:21697855). {ECO:0000269|PubMed:21697855}.; . . . 0.13981 0.10129 0.514416907 80.31375324 2392.92369 9.08048 CPT2P1 . . . carnitine palmitoyltransferase 2 pseudogene 1 . . . . . . . . . . . CPTP . . . ceramide-1-phosphate transfer protein FUNCTION: Mediates the intracellular transfer of ceramide-1- phosphate between organelle membranes and the cell membrane. Required for normal structure of the Golgi stacks. Can bind phosphoceramides with a variety of aliphatic chains, but has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains, and is inefficient with phosphoceramides containing lignoceryl (C24:0). Plays a role in the regulation of the cellular levels of ceramide-1-phosphate, and thereby contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid. Has no activity with galactosylceramide, lactosylceramide, sphingomyelin, phosphatidylcholine, phosphatidic acid and ceramide. {ECO:0000269|PubMed:23863933}.; . TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes. {ECO:0000269|PubMed:23863933}.; . . . . 0.106667882 61.73036093 . . CPVL 4.06683849640159e-07 0.814167022951326 0.185832570364824 carboxypeptidase, vitellogenic like FUNCTION: May be involved in the digestion of phagocytosed particles in the lysosome, participation in an inflammatory protease cascade, and trimming of peptides for antigen presentation.; . . lymphoreticular;myocardium;medulla oblongata;ovary;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;thyroid;bone;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;hypothalamus;blood;skeletal muscle;pancreas;pia mater;lung;nasopharynx;placenta;hippocampus;alveolus;liver;spleen;kidney;stomach; thyroid;whole blood;trigeminal ganglion; 0.06999 0.10188 1.332002318 94.20853975 4577.86455 13.58344 CPXCR1 0.0774718472474688 0.750661133824139 0.171867018928392 CPX chromosome region, candidate 1 . . TISSUE SPECIFICITY: Expressed in a variety of fetal tissues. {ECO:0000269|PubMed:11499681}.; unclassifiable (Anatomical System);lung;testis; . 0.02192 0.03628 0.881944684 89.02453409 1181.51332 6.52436 CPXM1 2.33840235512205e-11 0.408914535359441 0.591085464617175 carboxypeptidase X (M14 family), member 1 FUNCTION: May be involved in cell-cell interactions. No carboxypeptidase activity was found yet (By similarity). {ECO:0000250}.; . . . . 0.18143 0.10724 -1.172055164 6.027364945 255.56198 3.43842 CPXM2 1.82592014923893e-10 0.604373293881444 0.395626705935964 carboxypeptidase X (M14 family), member 2 FUNCTION: May be involved in cell-cell interactions.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;synovium;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.25569 0.10387 -0.282886048 33.53385232 334.56649 3.88669 CPZ 4.50799530429476e-21 4.87571258764968e-05 0.999951242874124 carboxypeptidase Z FUNCTION: Cleaves substrates with C-terminal arginine residues. Probably modulates the Wnt signaling pathway, by cleaving some undefined protein. May play a role in cleavage during prohormone processing. {ECO:0000269|PubMed:11766880, ECO:0000269|PubMed:12417617, ECO:0000269|PubMed:9099699}.; . TISSUE SPECIFICITY: In placenta, it is present within invasive trophoblasts and in the surrounding extracellular space. Also present in amnion cells, but is not readily apparent in the extracellular matrix of this cell type. Present in normal pituitary gland and neoplastic pituitary gland (especially POMC-, GH- and PRL-producing adenomas) (at protein level). Widely expressed. {ECO:0000269|PubMed:10671522, ECO:0000269|PubMed:12417617, ECO:0000269|PubMed:9099699}.; unclassifiable (Anatomical System);cartilage;ovary;heart;tongue;colon;parathyroid;skin;uterus;pancreas;prostate;optic nerve;lung;oesophagus;epididymis;bone;placenta;visual apparatus;testis;head and neck;kidney;brain;mammary gland;stomach; superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.24610 0.12229 -1.49019634 3.615239443 1475.68527 7.15559 CR1 9.34032929712518e-08 0.999999847582546 5.90141610044612e-08 complement component 3b/4b receptor 1 (Knops blood group) FUNCTION: Mediates cellular binding of particles and immune complexes that have activated complement.; . TISSUE SPECIFICITY: Present on erythrocytes, leukocytes, glomerular podocytes, and splenic follicular dendritic cells.; . . 0.08780 . . . 3621.79634 11.67146 CR1L 3.55709649735169e-15 0.0202255642137517 0.979774435786245 complement component 3b/4b receptor 1-like . . TISSUE SPECIFICITY: Expressed in fetal liver and to a lesser extent in fetal spleen and thymus. Expression appears to be limited to hematopoietic and fetal lymphoid tissue. {ECO:0000269|PubMed:14687939}.; unclassifiable (Anatomical System);liver;spleen;kidney;stomach;aorta; . 0.06963 . 3.872389272 99.64614296 2178.56335 8.59961 CR2 2.16539872051034e-11 0.990454563266266 0.00954543671207967 complement component 3d receptor 2 FUNCTION: Receptor for complement C3Dd, for the Epstein-Barr virus on human B-cells and T-cells and for HNRPU. Participates in B lymphocytes activation. {ECO:0000269|PubMed:7753047}.; DISEASE: Immunodeficiency, common variable, 7 (CVID7) [MIM:614699]: A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low. {ECO:0000269|PubMed:22035880}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Mature B-lymphocytes, T-lymphocytes, pharyngeal epithelial cells, astrocytes and follicular dendritic cells of the spleen.; . . 0.13376 0.45815 0.056905614 57.56074546 5458.93987 15.21947 CRABP1 0.12550489400582 0.780082091780974 0.0944130142132061 cellular retinoic acid binding protein 1 FUNCTION: Cytosolic CRABPs may regulate the access of retinoic acid to the nuclear retinoic acid receptors.; . . ovary;developmental;choroid;fovea centralis;bone marrow;retina;prostate;whole body;larynx;synovium;thyroid;bone;brain;unclassifiable (Anatomical System);heart;hypothalamus;blood;lung;trabecular meshwork;placenta;visual apparatus;macula lutea;alveolus;spleen;head and neck;stomach; superior cervical ganglion;thyroid;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.51280 0.35026 -0.163345027 41.24793583 9.97302 0.36559 CRABP2 0.00816686942900527 0.790186532747872 0.201646597823123 cellular retinoic acid binding protein 2 FUNCTION: Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors.; . . . . 0.78286 0.19831 -0.185391282 39.67916962 5.17485 0.19227 CRACR2A . . . calcium release activated channel regulator 2A FUNCTION: Ca(2+)-binding protein that plays a key role in store- operated Ca(2+) entry (SOCE) in T-cells by regulating CRAC channel activation. Acts as a cytoplasmic calcium-sensor that facilitates the clustering of ORAI1 and STIM1 at the junctional regions between the plasma membrane and the endoplasmic reticulum upon low Ca(2+) concentration. It thereby regulates CRAC channel activation, including translocation and clustering of ORAI1 and STIM1. Upon increase of cytoplasmic Ca(2+) resulting from opening of CRAC channels, dissociates from ORAI1 and STIM1, thereby destabilizing the ORAI1-STIM1 complex. {ECO:0000269|PubMed:20418871}.; . . . . 0.10919 0.10015 1.846456612 97.11606511 . . CRACR2B . . . calcium release activated channel regulator 2B FUNCTION: Plays a role in store-operated Ca(2+) entry (SOCE). {ECO:0000269|PubMed:20418871}.; . . . . 0.20188 . . . . . CRADD 0.731812881349657 0.256030667635808 0.0121564510145358 CASP2 and RIPK1 domain containing adaptor with death domain FUNCTION: Apoptotic adaptor molecule specific for caspase-2 and FASL/TNF receptor-interacting protein RIP. In the presence of RIP and TRADD, CRADD recruits caspase-2 to the TNFR-1 signalling complex.; DISEASE: Mental retardation, autosomal recessive 34 (MRT34) [MIM:614499]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT34 is a non-syndromic form. Affected individuals have mildly delayed development and significantly impaired cognitive function, precluding independent living and self-care. Speech is rudimentary, but articulate; autism is not present. {ECO:0000269|PubMed:22279524}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Constitutively expressed in most tissues, with particularly high expression in adult heart, testis, liver, skeletal muscle, fetal liver and kidney.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;skin;skeletal muscle;uterus;optic nerve;whole body;lung;endometrium;nasopharynx;bone;placenta;liver;testis;germinal center;kidney;brain;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.17997 0.14607 -0.005381972 53.50908233 60.3284 1.57786 CRAMP1 . . . cramped chromatin regulator homolog 1 . . . . . 0.14109 0.77410 -1.256630467 5.343241331 . . CRAT 3.45790827945061e-07 0.933730777995625 0.066268876213547 carnitine O-acetyltransferase FUNCTION: Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria.; . TISSUE SPECIFICITY: Mostly in skeletal muscle, less in heart, liver and pancreas, only weakly detectable in brain, placenta, lung and kidney.; lymphoreticular;medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;liver;testis;kidney; 0.09860 0.50853 -1.082044518 7.242274121 397.15206 4.18644 CRB1 3.35697504496476e-09 0.980346774624146 0.0196532220188794 crumbs 1, cell polarity complex component FUNCTION: Plays a role in photoreceptor morphogenesis in the retina. May maintain cell polarization and adhesion.; DISEASE: Note=CRB1 mutations have been found in various retinal dystrophies, chronic and disabling disorders of visual function. They predominantly involve the posterior portion of the ocular fundus, due to degeneration in the sensory layer of the retina, retinal pigment epithelium, Bruch membrane, choroid, or a combination of these tissues. Onset of inherited retinal dystrophies is painless, bilateral and typically progressive. Most people experience gradual peripheral vision loss or tunnel vision, and difficulties with poor illumination and night vision. Central vision is usually unaffected, so the person may still be able to read. However, it can also deteriorate to cause total blindness. Examples of retinal dystrophies are retinitis pigmentosa, Leber congenital amaurosis, cone-rod dystrophy among others. {ECO:0000269|PubMed:20683928, ECO:0000269|PubMed:22065545}.; DISEASE: Retinitis pigmentosa 12 (RP12) [MIM:600105]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP12 is an autosomal recessive, severe form often manifesting in early childhood. Patients experiment progressive visual field loss with severe visual impairment before the age of twenty. Some patients have a preserved paraarteriolar retinal pigment epithelium (PPRPE) and hypermetropia. {ECO:0000269|PubMed:10508521, ECO:0000269|PubMed:11389483, ECO:0000269|PubMed:11559858, ECO:0000269|PubMed:12573663, ECO:0000269|PubMed:12843338, ECO:0000269|PubMed:15459956, ECO:0000269|PubMed:19140180, ECO:0000269|PubMed:19956407, ECO:0000269|PubMed:20591486, ECO:0000269|PubMed:20956273, ECO:0000269|PubMed:21987686, ECO:0000269|PubMed:22065545, ECO:0000269|PubMed:22128245, ECO:0000269|PubMed:22334370}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leber congenital amaurosis 8 (LCA8) [MIM:613835]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:11231775, ECO:0000269|PubMed:11389483, ECO:0000269|PubMed:12567265, ECO:0000269|PubMed:12573663, ECO:0000269|PubMed:12700176, ECO:0000269|PubMed:15024725, ECO:0000269|PubMed:15691574, ECO:0000269|PubMed:16205573, ECO:0000269|PubMed:16936081, ECO:0000269|PubMed:17128490, ECO:0000269|PubMed:17438615, ECO:0000269|PubMed:17724218, ECO:0000269|PubMed:18055821, ECO:0000269|PubMed:18682808, ECO:0000269|PubMed:20108431, ECO:0000269|PubMed:20956273, ECO:0000269|PubMed:21602930}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pigmented paravenous chorioretinal atrophy (PPCRA) [MIM:172870]: Unusual retinal degeneration characterized by accumulation of pigmentation along retinal veins. PPCRA is dominantly inherited, but exhibited variable expressivity. Males are more likely to exhibit a severe phenotype, whereas females may remain virtually asymptomatic even in later years. The PPCRA phenotype is associated with a mutation in CRB1 gene which is likely to affect the structure of the CRB1 protein. {ECO:0000269|PubMed:15623792}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Preferential expression in retina, also expressed in brain, testis, fetal brain and fetal eye. {ECO:0000269|PubMed:15914641}.; . . 0.27985 0.19528 -2.563327215 0.843359283 137.7212 2.55575 CRB2 3.46014603004443e-05 0.997413513994272 0.00255188454542802 crumbs 2, cell polarity complex component FUNCTION: May play a role in polarized cells morphogenesis.; DISEASE: Ventriculomegaly with cystic kidney disease (VMCKD) [MIM:219730]: A severe autosomal recessive developmental disorder manifesting in utero. It is characterized by cerebral ventriculomegaly, echogenic kidneys, microscopic renal tubular cysts and findings of congenital nephrosis. {ECO:0000269|PubMed:25557780}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in retina, fetal eye and brain. Also expressed in kidney, ARPE-19 and RPE/choroid cell lines, and at low levels in lung, placenta, and heart. {ECO:0000269|PubMed:15851977}.; unclassifiable (Anatomical System);brain; dorsal root ganglion;superior cervical ganglion;fetal liver;placenta;globus pallidus;ciliary ganglion;pons;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13969 0.12074 0.104640324 61.28214201 3359.54974 11.10625 CRB3 0.369971428667681 0.581683424739807 0.0483451465925115 crumbs 3, cell polarity complex component FUNCTION: Involved in the establishment of cell polarity in mammalian epithelial cells. Regulates the morphogenesis of tight junctions. {ECO:0000269|PubMed:12771187, ECO:0000269|PubMed:14718572}.; . TISSUE SPECIFICITY: Preferentially expressed in epithelial tissues. Expressed at high levels in lung, kidney, retina, colon and mammary glands. Expressed at moderate levels in liver, spleen, pancreas, placenta and prostate. {ECO:0000269|PubMed:12527193, ECO:0000269|PubMed:14718572}.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;uterus;prostate;pancreas;lung;oesophagus;placenta;liver;testis;spleen;germinal center;kidney;stomach;aorta;thymus; . 0.08886 0.08658 -0.273576253 33.97027601 3.19838 0.11498 CRB3P1 . . . crumbs cell polarity complex component 3 pseudogene 1 . . . . . . . . . . . CRBN 0.0384944384873777 0.960073443143809 0.00143211836881361 cereblon FUNCTION: Substrate recognition component of a DCX (DDB1-CUL4-X- box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2. Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8. May play a role in memory and learning by regulating the assembly and neuronal surface expression of large-conductance calcium-activated potassium channels in brain regions involved in memory and learning via its interaction with KCNT1. Binding of pomalidomide and other thalidomide-related drugs changes the substrate specificity of the human protein, leading to decreased degradation of MEIS2 and other target proteins and increased degradation of MYC, IRF4, IKZF1 and IKZF3. {ECO:0000269|PubMed:18414909, ECO:0000269|PubMed:20223979, ECO:0000269|PubMed:24328678, ECO:0000269|PubMed:25043012, ECO:0000269|PubMed:25108355, ECO:0000305}.; DISEASE: Mental retardation, autosomal recessive 2A (MRT2A) [MIM:607417]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs. MRT2A patients display mild mental retardation with a standard IQ ranged from 50 to 70. IQ scores are lower in males than females. Developmental milestones are mildly delayed. There are no dysmorphic or autistic features. {ECO:0000269|PubMed:15557513}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain. {ECO:0000269|PubMed:15557513, ECO:0000269|PubMed:17380424}.; medulla oblongata;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;oesophagus;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;hypothalamus;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;amygdala;occipital lobe;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;white blood cells;cingulate cortex;parietal lobe; 0.19482 . -0.580403979 18.58928993 30.23873 0.96422 CRCP 0.00139892682926566 0.663197723172823 0.335403349997912 CGRP receptor component FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts induce type I interferon and NF- Kappa- B through the RIG-I pathway (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. Most prevalent in testis. {ECO:0000269|PubMed:10067875}.; unclassifiable (Anatomical System);cartilage;ovary;hypothalamus;skin;skeletal muscle;retina;uterus;mesenchyma;nasopharynx;bone;visual apparatus;hippocampus;liver;testis;cervix;kidney;brain;bladder;artery;mammary gland;aorta; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.11165 0.325313577 73.11276244 29.15373 0.93190 CRCT1 0.00367304007975833 0.399676885672416 0.596650074247825 cysteine rich C-terminal 1 . . . . . 0.43200 0.11285 . . 1072.28947 6.27906 CREB1 0.969960676573643 0.0300304494308356 8.87399552088378e-06 cAMP responsive element binding protein 1 FUNCTION: Phosphorylation-dependent transcription factor that stimulates transcription upon binding to the DNA cAMP response element (CRE), a sequence present in many viral and cellular promoters. Transcription activation is enhanced by the TORC coactivators which act independently of Ser-133 phosphorylation. Involved in different cellular processes including the synchronization of circadian rhythmicity and the differentiation of adipose cells.; DISEASE: Angiomatoid fibrous histiocytoma (AFH) [MIM:612160]: A distinct variant of malignant fibrous histiocytoma that typically occurs in children and adolescents and is manifest by nodular subcutaneous growth. Characteristic microscopic features include lobulated sheets of histiocyte-like cells intimately associated with areas of hemorrhage and cystic pseudovascular spaces, as well as a striking cuffing of inflammatory cells, mimicking a lymph node metastasis. Note=The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving CREB1 is found in a patient with angiomatoid fibrous histiocytoma. Translocation t(2;22)(q33;q12) with CREB1 generates a EWSR1/CREB1 fusion gene that is most common genetic abnormality in this tumor type.; DISEASE: Note=A CREB1 mutation has been found in a patient with multiple congenital anomalies consisting of agenesis of the corpus callosum, cerebellar hypoplasia, severe neonatal respiratory distress refractory to surfactant, thymus hypoplasia, and thyroid follicular hypoplasia. {ECO:0000269|PubMed:22267179}.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;spinal cord;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;hippocampus;macula lutea;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.99423 0.94870 0.080983847 59.76055674 117.91791 2.36061 CREB3 8.86997227194125e-07 0.514853837617907 0.485145275384866 cAMP responsive element binding protein 3 FUNCTION: Endoplasmic reticulum (ER)-bound transcription factor that plays a role in the unfolded protein response (UPR). Involved in cell proliferation and migration, tumor suppression and inflammatory gene expression. Plays also a role in the human immunodeficiency virus type 1 (HIV-1) virus protein expression and in the herpes simplex virus-1 (HSV-1) latent infection and reactivation from latency. Isoform 2 plays a role in the unfolded protein response (UPR). Isoform 2 acts as a positive regulator of LKN-1/CCL15-induced chemotaxis signaling of leukocyte cell migration. Isoform 2 may play a role as a cellular tumor suppressor that is targeted by the hepatitis C virus (HSV) core protein. Isoform 2 represses the VP16-mediated transactivation of immediate early genes of the HSV-1 virus by sequestring host cell factor-1 HCFC1 in the ER membrane of sensory neurons, thereby preventing the initiation of the replicative cascade leading to latent infection. Isoform 3 functions as a negative transcriptional regulator in ligand-induced transcriptional activation of the glucocorticoid receptor NR3C1 by recruiting and activating histone deacetylases (HDAC1, HDAC2 and HDAC6). Isoform 3 decreases the acetylation level of histone H4. Isoform 3 does not promote the chemotactic activity of leukocyte cells.; . TISSUE SPECIFICITY: Expressed in dendritic cells (DC). Weakly expressed in monocytes (at protein level). Ubiquitous. {ECO:0000269|PubMed:10675342, ECO:0000269|PubMed:19779205, ECO:0000269|PubMed:20546900, ECO:0000269|PubMed:9271389, ECO:0000269|PubMed:9389645}.; medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;salivary gland;developmental;intestine;colon;parathyroid;choroid;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;placenta;hippocampus;duodenum;hypopharynx;amnion;head and neck;kidney;stomach; . 0.21289 0.08709 -0.247889024 35.98726115 38.70342 1.14683 CREB3L1 0.399379409918579 0.59871786829579 0.0019027217856301 cAMP responsive element binding protein 3-like 1 FUNCTION: Transcription factor involved in unfolded protein response (UPR). In the absence of endoplasmic reticulum (ER) stress, inserted into ER membranes, with N-terminal DNA-binding and transcription activation domains oriented toward the cytosolic face of the membrane. In response to ER stress, transported to the Golgi, where it is cleaved in a site-specific manner by resident proteases S1P/MBTPS1 and S2P/MBTPS2. The released N-terminal cytosolic domain is translocated to the nucleus to effect transcription of specific target genes. Plays a critical role in bone formation through the transcription of COL1A1, and possibly COL1A2, and the secretion of bone matrix proteins. Directly binds to the UPR element (UPRE)-like sequence in an osteoblast-specific COL1A1 promoter region and induces its transcription. Does not regulate COL1A1 in other tissues, such as skin (By similarity). Required to protect astrocytes from ER stress-induced cell death. In astrocytes, binds to the cAMP response element (CRE) of the BiP/HSPA5 promoter and participate in its transcriptional activation (By similarity). May play a role in limiting virus spread by inhibiting proliferation of virus-infected cells. Upon infection with diverse DNA and RNA viruses, inhibits cell-cycle progression by binding to promoters and activating transcription of genes encoding cell-cycle inhibitors, such as p21/CDKN1A (PubMed:21767813). Binds the DNA consensus sequence 5'-GTGXGCXGC- 3' (PubMed:21767813). {ECO:0000250|UniProtKB:Q9Z125, ECO:0000269|PubMed:12054625, ECO:0000269|PubMed:21767813}.; DISEASE: Osteogenesis imperfecta 16 (OI16) [MIM:616229]: An autosomal recessive form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI16 is a severe form. {ECO:0000269|PubMed:24079343}. Note=The disease may be caused by mutations affecting the gene represented in this entry. OI16 affected patients show a genomic deletion encompassing CREB3L1 and the first exon of DGKZ. The absence of this exon does not affect all DGKZ isoforms, some are still produced at normal level. It cannot be ruled out that DGKZ could contribute to the phenotype, but in view of its role in bone formation, CREB3L1 is a strong OI16-causing candidate (PubMed:24079343). This hypothesis is corroborated by the observation of CREB3L1 knockout mice which exhibit features reminiscent of severe human osteogenesis imperfecta. {ECO:0000269|PubMed:24079343}.; TISSUE SPECIFICITY: Expressed in several tissues, with highest levels in pancreas and prostate. Expressed at relatively lower levels in brain. {ECO:0000269|PubMed:12054625}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;cochlea;endometrium;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;prostate;superior cervical ganglion;heart;trachea;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.56315 0.13761 0.286674996 71.49681529 613.68462 5.00687 CREB3L2 0.609225183555282 0.390408619083598 0.000366197361119408 cAMP responsive element binding protein 3-like 2 FUNCTION: Transcription factor involved in unfolded protein response (UPR). In the absence of endoplasmic reticulum (ER) stress, inserted into ER membranes, with N-terminal DNA-binding and transcription activation domains oriented toward the cytosolic face of the membrane. In response to ER stress, transported to the Golgi, where it is cleaved in a site-specific manner by resident proteases S1P/MBTPS1 and S2P/MBTPS2. The released N-terminal cytosolic domain is translocated to the nucleus to effect transcription of specific target genes. Plays a critical role in chondrogenesis by activating the transcription of SEC23A, which promotes the transport and secretion of cartilage matrix proteins, and possibly that of ER biogenesis-related genes (By similarity). In a neuroblastoma cell line, protects cells from ER stress- induced death (PubMed:17178827). In vitro activates transcription of target genes via direct binding to the CRE site (PubMed:17178827). {ECO:0000250|UniProtKB:Q8BH52, ECO:0000269|PubMed:17178827}.; DISEASE: Note=A chromosomal aberration involving CREB3L2 is found in low grade fibromyxoid sarcoma (LGFMS). Translocation t(7;16)(q33;p11) with FUS.; TISSUE SPECIFICITY: Widely expressed with highest levels in placenta, lung, spleen and intestine, and lowest levels in heart, brain, skeletal muscle, thymus, colon and leukocytes. In fetal tissues, the weakest expression is detected in brain and heart. {ECO:0000269|PubMed:12915480}.; unclassifiable (Anatomical System);cartilage;ovary;colon;blood;fovea centralis;choroid;lens;skin;skeletal muscle;retina;optic nerve;lung;frontal lobe;placenta;thyroid;macula lutea;liver;testis;head and neck;spleen;cervix;kidney;brain; dorsal root ganglion;superior cervical ganglion;medulla oblongata;olfactory bulb;adrenal gland;placenta;thyroid;adrenal cortex;ciliary ganglion;atrioventricular node;pituitary; 0.27206 0.13635 -0.688817379 15.20405756 81.88749 1.91782 CREB3L3 1.58659746321972e-09 0.366526578999545 0.633473419413858 cAMP responsive element binding protein 3-like 3 FUNCTION: Transcription factor that may act during endoplasmic reticulum stress by activating unfolded protein response target genes. Activated in response to cAMP stimulation. In vitro, binds to the cAMP response element (CRE) and box-B element. Activates transcription through box-B element. Activates transcription through CRE (By similarity). Seems to function synergistically with ATF6. In acute inflammatory response, may activate expression of acute phase response (APR) genes. May be involved in growth suppression. {ECO:0000250, ECO:0000269|PubMed:11353085, ECO:0000269|PubMed:15800215, ECO:0000269|PubMed:16469704}.; . TISSUE SPECIFICITY: Exclusively expressed in liver. Underexpressed in hepatocellular carcinoma tissues. {ECO:0000269|PubMed:11353085, ECO:0000269|PubMed:15800215}.; skeletal muscle;stomach; . 0.08138 0.13410 -0.709045403 14.673272 63.68751 1.63604 CREB3L4 8.06202744664506e-05 0.763920697804371 0.235998681921163 cAMP responsive element binding protein 3-like 4 FUNCTION: Transcriptional activator that may play a role in the unfolded protein response. Binds to the UPR element (UPRE) but not to CRE element. Preferentially binds DNA with to the consensus sequence 5'-T[GT]ACGT[GA][GT]-3' and has transcriptional activation activity from UPRE. Binds to NF-kappa-B site and has transcriptional activation activity from NF-kappa-B-containing regulatory elements (By similarity). {ECO:0000250, ECO:0000269|PubMed:16236796}.; . TISSUE SPECIFICITY: According to PubMed:11830526, exclusively expressed in the prostate. Expressed in breast and prostate cancer cell lines. Expressed in prostatic luminal epithelial cells (at protein level). Expression is significantly more abundant in prostate cancer than in benign prostatic tissue (prostatic hyperplasia). According to PubMed:12111373, also expressed in brain, pancreas and skeletal muscle, and at lower levels in small intestine, testis, leukocyte and thymus. {ECO:0000269|PubMed:11830526, ECO:0000269|PubMed:12111373, ECO:0000269|PubMed:17270658}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;islets of Langerhans;lens;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; . 0.04507 0.08885 1.39815152 94.71573484 2634.63657 9.63149 CREB5 0.989844564730837 0.0101548208581049 6.14411058126493e-07 cAMP responsive element binding protein 5 FUNCTION: Binds to the cAMP response element and activates transcription. {ECO:0000269|PubMed:8378084}.; . . uterus;lung;whole body;ovary;placenta;testis;parathyroid;blood;head and neck;kidney;germinal center;brain;bone marrow; prefrontal cortex; 0.77630 . -0.670411825 15.61689078 30.64753 0.97477 CREBBP 0.999999999999794 2.06414678369328e-13 5.47492328842456e-33 CREB binding protein FUNCTION: Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 and FOXO1. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK- ARNTL/BMAL1 heterodimers. Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902). {ECO:0000269|PubMed:11154691, ECO:0000269|PubMed:12738767, ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:9707565}.; DISEASE: Note=Chromosomal aberrations involving CREBBP may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with KAT6A; translocation t(11;16)(q23;p13.3) with KMT2A/MLL1; translocation t(10;16)(q22;p13) with KAT6B. KAT6A-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription.; DISEASE: Rubinstein-Taybi syndrome 1 (RSTS1) [MIM:180849]: A disorder characterized by craniofacial abnormalities, postnatal growth deficiency, broad thumbs, broad big toes, mental retardation and a propensity for development of malignancies. {ECO:0000269|PubMed:11331617, ECO:0000269|PubMed:12114483, ECO:0000269|PubMed:12566391, ECO:0000269|PubMed:15706485, ECO:0000269|PubMed:20684013, ECO:0000269|PubMed:25388907}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;amnion;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; medulla oblongata;skeletal muscle;cerebellum; 0.99999 0.55070 -2.102511638 1.539278132 350.49854 3.97008 CREBL2 0.623023671533736 0.369406756142758 0.00756957232350643 cAMP responsive element binding protein like 2 FUNCTION: Probable regulator of CREB1 transcriptional activity which is involved in adipose cells differentiation. May also play a regulatory role in the cell cycle. Identification in a chromosomal region frequently deleted in various cancers suggests that it might act as a tumor suppressor. {ECO:0000269|PubMed:9693048}.; . . ovary;skin;retina;bone marrow;prostate;cochlea;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;lacrimal gland;islets of Langerhans;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach;thymus; amygdala;dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;adrenal gland;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.49932 0.13708 0.101211609 60.95777306 2.1225 0.07007 CREBRF 0.998406138401379 0.00159382863543768 3.29631834680336e-08 CREB3 regulatory factor FUNCTION: Acts as a negative regulator of the endoplasmic reticulum stress response or unfolded protein response (UPR). Represses the transcriptional activity of CREB3 during the UPR. Recruits CREB3 into nuclear foci. {ECO:0000269|PubMed:18391022}.; . . . . 0.40707 0.07442 -0.824740496 11.67728238 20.36051 0.69441 CREBZF 0.0366616489719182 0.832377449397193 0.130960901630889 CREB/ATF bZIP transcription factor FUNCTION: Strongly activates transcription when bound to HCFC1. Suppresses the expression of HSV proteins in cells infected with the virus in a HCFC1-dependent manner. Also suppresses the HCFC1- dependent transcriptional activation by CREB3 and reduces the amount of CREB3 in the cell. Able to down-regulate expression of some cellular genes in CREBZF-expressing cells. {ECO:0000269|PubMed:10871379, ECO:0000269|PubMed:15705566}.; . TISSUE SPECIFICITY: In adults, expressed most abundantly in heart, liver and skeletal muscle, moderately abundant in kidney and pancreas, and barely detectable in lung. In fetal tissues, expressed most abundantly in kidney and very low amounts in heart, lung and liver. {ECO:0000269|PubMed:10871379}.; smooth muscle;ovary;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;amniotic fluid;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;breast;pancreas;pia mater;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.37422 0.47084 -0.139478553 43.29440906 117.84489 2.35984 CREG1 0.0170794446011191 0.713497025102269 0.269423530296612 cellular repressor of E1A stimulated genes 1 FUNCTION: May contribute to the transcriptional control of cell growth and differentiation. Antagonizes transcriptional activation and cellular transformation by the adenovirus E1A protein. The transcriptional control activity of cell growth requires interaction with IGF2R. {ECO:0000269|PubMed:12934103, ECO:0000269|PubMed:9710587}.; . . . . 0.58258 0.11475 . . 14.14787 0.51200 CREG2 0.00561130743800167 0.719392910302105 0.274995782259894 cellular repressor of E1A stimulated genes 2 . . TISSUE SPECIFICITY: Brain specific mainly in the limbic system and faintly in the spinal cord but not in cerebellum. {ECO:0000269|PubMed:12408961}.; unclassifiable (Anatomical System);hippocampus;brain; . 0.10085 . . . 546.79461 4.75282 CRELD1 1.4147073999886e-06 0.954314136341221 0.0456844489513785 cysteine rich with EGF like domains 1 . DISEASE: Atrioventricular septal defect 2 (AVSD2) [MIM:606217]: A congenital heart malformation characterized by a common atrioventricular junction coexisting with deficient atrioventricular septation. The complete form involves underdevelopment of the lower part of the atrial septum and the upper part of the ventricular septum; the valve itself is also shared. A less severe form, known as ostium primum atrial septal defect, is characterized by separate atrioventricular valvar orifices despite a common junction. {ECO:0000269|PubMed:12632326, ECO:0000269|PubMed:15857420}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in fetal lung, liver, kidney, adult heart, brain and skeletal muscle. Weakly expressed in placenta, fetal brain, and adult lung, liver, kidney and pancreas. {ECO:0000269|PubMed:12137942}.; ovary;colon;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;oesophagus;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pineal body;adrenal cortex;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; whole brain;superior cervical ganglion;thyroid;globus pallidus;pons;trigeminal ganglion;cingulate cortex; 0.09201 0.09216 0.376678994 75.50719509 253.78401 3.42716 CRELD2 4.95812176033358e-08 0.220198052628944 0.779801897789839 cysteine rich with EGF like domains 2 FUNCTION: May regulate transport of alpha4-beta2 neuronal acetylcholine receptor.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:16238698, ECO:0000269|PubMed:16919896}.; smooth muscle;ovary;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;blood;lens;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; trachea;thyroid;liver;testis; 0.23727 0.10908 0.801024817 87.65628686 1620.87519 7.44658 CREM 0.644423492964678 0.355307954254337 0.000268552780985197 cAMP responsive element modulator FUNCTION: Transcriptional regulator that binds the cAMP response element (CRE), a sequence present in many viral and cellular promoters. Isoforms are either transcriptional activators or repressors. Plays a role in spermatogenesis and is involved in spermatid maturation (PubMed:10373550). {ECO:0000269|PubMed:10373550}.; . TISSUE SPECIFICITY: Expressed in testes (round spermatids) (at protein level). Isoform 14 is the major activator form in testes. {ECO:0000269|PubMed:11044457, ECO:0000269|PubMed:14511788, ECO:0000269|PubMed:16143638}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;liver;head and neck;kidney;mammary gland;stomach; amygdala;medulla oblongata;superior cervical ganglion;testis - interstitial;adrenal cortex;pons;atrioventricular node;skeletal muscle;testis - seminiferous tubule;adrenal gland;testis;trigeminal ganglion;parietal lobe; 0.80005 0.25555 -0.26993514 34.59542345 1081.5186 6.30744 CRH 0.52778935313737 0.410744715056212 0.0614659318064179 corticotropin releasing hormone FUNCTION: Hormone regulating the release of corticotropin from pituitary gland (By similarity). Induces NLRP6 in intestinal epithelial cells, hence may influence gut microbiota profile (By similarity). {ECO:0000250|UniProtKB:P06296, ECO:0000250|UniProtKB:Q8CIT0}.; . TISSUE SPECIFICITY: Produced by the hypothalamus and placenta. {ECO:0000269|PubMed:2783917, ECO:0000269|PubMed:3262120}.; unclassifiable (Anatomical System);uterus;whole body;ovary;endometrium;adrenal gland;islets of Langerhans;placenta;urinary;parathyroid;brain; amygdala;whole brain;thalamus;superior cervical ganglion;occipital lobe;hypothalamus;placenta;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.99999 0.48736 . . 22.45129 0.75264 CRHBP 0.989594470418958 0.0104023085279995 3.22105304206757e-06 corticotropin releasing hormone binding protein FUNCTION: Binds CRF and inactivates it. May prevent inappropriate pituitary-adrenal stimulation in pregnancy.; . . unclassifiable (Anatomical System);ovary;heart;placenta;hippocampus;liver;parathyroid;spleen;kidney;germinal center;brain;mammary gland;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.68030 0.09992 -0.095386216 46.48502005 33.18155 1.02649 CRHR1 0.792134286397601 0.207811644388771 5.40692136282513e-05 corticotropin releasing hormone receptor 1 FUNCTION: G-protein coupled receptor for CRH (corticotropin- releasing factor) and UCN (urocortin). Has high affinity for CRH and UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels. Inhibits the activity of the calcium channel CACNA1H. Required for normal embryonic development of the adrenal gland and for normal hormonal responses to stress. Plays a role in the response to anxiogenic stimuli. {ECO:0000269|PubMed:18292205, ECO:0000269|PubMed:18801728, ECO:0000269|PubMed:23576434, ECO:0000269|PubMed:23863939}.; . TISSUE SPECIFICITY: Predominantly expressed in the cerebellum, pituitary, cerebral cortex and olfactory lobe. {ECO:0000269|PubMed:8243652}.; unclassifiable (Anatomical System);optic nerve;whole body;macula lutea;fovea centralis;choroid;brain;lens;retina; . 0.20832 0.38883 -0.091746757 46.91554612 63.73185 1.63701 CRHR1-IT1 . . . CRHR1 intronic transcript 1 . . . . . 0.09205 . . . . . CRHR2 6.66041350022908e-07 0.693742676430311 0.306256657528339 corticotropin releasing hormone receptor 2 FUNCTION: G-protein coupled receptor for CRH (corticotropin- releasing factor), UCN (urocortin), UCN2 and UCN3. Has high affinity for UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels.; . . brain;retina; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.06804 0.15393 0.687150476 85.17928757 327.17767 3.84612 CRIM1 0.977883078914308 0.022116914105891 6.97980066784347e-09 cysteine rich transmembrane BMP regulator 1 (chordin-like) FUNCTION: May play a role in CNS development by interacting with growth factors implicated in motor neuron differentiation and survival. May play a role in capillary formation and maintenance during angiogenesis. Modulates BMP activity by affecting its processing and delivery to the cell surface. {ECO:0000269|PubMed:12464430, ECO:0000269|PubMed:12805376}.; . TISSUE SPECIFICITY: Expressed in pancreas, kidney, skeletal muscle, lung, placenta, brain, heart, spleen, liver and small intestine. Expressed in blood vessels (at protein level). {ECO:0000269|PubMed:10642437, ECO:0000269|PubMed:12464430}.; lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;ganglion;frontal lobe;cochlea;endometrium;thyroid;brain;gall bladder;heart;cartilage;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;developmental;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;bile duct;pancreas;lung;pia mater;mesenchyma;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; placenta;trigeminal ganglion; 0.26394 . -1.100469982 6.929700401 649.0811 5.11079 CRIP1 0.0013579599192347 0.422344924066143 0.576297116014623 cysteine rich protein 1 FUNCTION: Seems to have a role in zinc absorption and may function as an intracellular zinc transport protein.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;whole body;frontal lobe;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pharynx;blood;skeletal muscle;bile duct;pancreas;lung;cornea;epididymis;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.16635 0.11262 0.281220278 71.07808445 288.32797 3.63595 CRIP1P1 . . . cysteine rich protein 1 pseudogene 1 . . . . . . . . . . . CRIP1P2 . . . cysteine rich protein 1 pseudogene 2 . . . . . . . . . . . CRIP1P3 . . . cysteine rich protein 1 pseudogene 3 . . . . . . . . . . . CRIP1P4 . . . cysteine rich protein 1 pseudogene 4 . . . . . . . . . . . CRIP2 0.00507027849660397 0.698684883924356 0.29624483757904 cysteine rich protein 2 . . TISSUE SPECIFICITY: Widespread tissue expression; highest levels in the heart.; myocardium;medulla oblongata;ovary;colon;choroid;skin;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;aorta;thymus; heart;placenta;thyroid; 0.25250 0.14896 . . 31.56406 0.99371 CRIP3 0.0339026389635781 0.927505563363447 0.0385917976729746 cysteine rich protein 3 . . TISSUE SPECIFICITY: Expressed in most tissues, but not in skeletal muscle. {ECO:0000269|PubMed:15380775}.; unclassifiable (Anatomical System);uterus;heart;skin; . 0.18227 0.10654 -0.073340031 48.11866006 17.63411 0.61822 CRIPAK 2.43127197997244e-12 0.00965282393694073 0.990347176060628 cysteine rich PAK1 inhibitor FUNCTION: Negative regulator of PAK1. It has been suggested that the lost of CRIPAK in breast tumors might contribute to hormonal independence. {ECO:0000269|PubMed:16278681}.; . TISSUE SPECIFICITY: Widely expressed with a highest expression observed in trachea, prostate and adrenal glands. Expressed in many cancer cell lines including breast cancer cells. {ECO:0000269|PubMed:16278681}.; heart;ovary;blood;skin;uterus;pancreas;lung;endometrium;bone;visual apparatus;liver;pituitary gland;testis;spleen;brain;stomach; . 0.12758 . 4.720673514 99.78178816 6222.68408 16.49850 CRIPT 0.0186146204892108 0.72980698782123 0.25157839168956 CXXC repeat containing interactor of PDZ3 domain FUNCTION: Involved in the cytoskeletal anchoring of DLG4 in excitatory synapses. {ECO:0000250|UniProtKB:Q792Q4}.; DISEASE: Short stature with microcephaly and distinctive facies (SSMF) [MIM:615789]: A disease characterized by dwarfism, microcephaly, and distinctive facial dysmorphism involving frontal bossing, high forehead, sparse hair and eyebrows, telecanthus, mild proptosis, anteverted nares, and flat nasal bridge. {ECO:0000269|PubMed:24389050}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; prefrontal cortex; 0.14765 0.11262 -0.119252484 44.53880632 10.24879 0.37357 CRISP1 0.000219401762806872 0.741846921065601 0.257933677171592 cysteine rich secretory protein 1 FUNCTION: May have a role in sperm-egg fusion and maturation.; . TISSUE SPECIFICITY: Caput, corpus, and cauda regions of the epididymis, the ductus deferens, sperm and seminal plasma.; prostate;lung;testis; testis - interstitial;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.02698 0.07066 -0.426079032 25.36565228 232.57631 3.29761 CRISP2 7.55320333504596e-10 0.0392404654633477 0.960759533781332 cysteine rich secretory protein 2 FUNCTION: May regulate some ion channels' activity and therebye regulate calcium fluxes during sperm capacitation. {ECO:0000250}.; . TISSUE SPECIFICITY: Testis and epididymis.; unclassifiable (Anatomical System);medulla oblongata;prostate;lung;hippocampus;testis; testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;skeletal muscle; 0.24553 0.06437 0.949904335 90.00943619 222.54753 3.22515 CRISP3 0.000109838277984035 0.820000954283913 0.179889207438103 cysteine rich secretory protein 3 . . TISSUE SPECIFICITY: Salivary gland, pancreas and prostate > epididymis, ovary, thymus and colon.; unclassifiable (Anatomical System);medulla oblongata;prostate;lung;testis;blood;skeletal muscle;bone marrow; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;trachea;salivary gland;testis;atrioventricular node;skeletal muscle;bone marrow; 0.09493 0.12681 0.128714042 63.19886766 1472.42491 7.14868 CRISPLD1 0.000148412019623545 0.998289460185323 0.00156212779505368 cysteine rich secretory protein LCCL domain containing 1 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;bile duct;pancreas;prostate;whole body;lung;frontal lobe;cochlea;endometrium;bone;placenta;testis;kidney;brain;mammary gland;artery;aorta;stomach; prostate;fetal brain;trachea;ciliary ganglion; 0.39360 0.10059 -0.558357437 19.54470394 66.56913 1.68192 CRISPLD2 7.37608592707666e-06 0.977631394085683 0.02236122982839 cysteine rich secretory protein LCCL domain containing 2 FUNCTION: Promotes matrix assembly. {ECO:0000250}.; . . ovary;sympathetic chain;colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach; adipose tissue;placenta;ciliary ganglion; 0.77714 0.10639 0.448277766 77.99598962 4030.53322 12.57901 CRK 0.864536311467028 0.13505598153368 0.000407706999291227 v-crk avian sarcoma virus CT10 oncogene homolog FUNCTION: The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk- II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling. {ECO:0000269|PubMed:11870224, ECO:0000269|PubMed:1630456, ECO:0000269|PubMed:17515907}.; . . ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;whole body;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;adipose tissue;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.73088 0.53296 -0.339715008 30.06605331 5.16406 0.19181 CRKL 0.163453647364194 0.773297490585036 0.0632488620507694 v-crk avian sarcoma virus CT10 oncogene homolog-like FUNCTION: May mediate the transduction of intracellular signals.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;subthalamic nucleus;occipital lobe;superior cervical ganglion;cerebellum peduncles;prefrontal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.95321 0.43956 -0.317668748 31.45789101 23.30496 0.77780 CRLF1 0.026855594173361 0.961240656843699 0.0119037489829401 cytokine receptor-like factor 1 FUNCTION: Cytokine receptor subunit, possibly playing a regulatory role in the immune system and during fetal development. May be involved in nervous system development.; DISEASE: Cold-induced sweating syndrome 1 (CISS1) [MIM:272430]: An autosomal recessive disorder characterized by profuse sweating induced by cool surroundings (temperatures of 7 to 18 degrees Celsius). Patients manifest, in the neonatal period, orofacial weakness with impaired sucking and swallowing, resulting in poor feeding. Affected infants show a tendency to startle, with contractions of the facial muscles in response to tactile stimuli or during crying, trismus, abundant salivation, and opisthotonus. These features are referred to as Crisponi syndrome and can result in early death in infancy. Patients who survive into childhood have hyperhidrosis, mainly of the upper body, in response to cold temperatures, and sweat very little with heat. Additional abnormalities include a high-arched palate, nasal voice, depressed nasal bridge, inability to fully extend the elbows and kyphoscoliosis. {ECO:0000269|PubMed:12509788, ECO:0000269|PubMed:16952376, ECO:0000269|PubMed:17436251, ECO:0000269|PubMed:17436252, ECO:0000269|PubMed:21326283, ECO:0000269|PubMed:23026229, ECO:0000269|PubMed:24488861}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest levels of expression observed in spleen, thymus, lymph node, appendix, bone marrow, stomach, placenta, heart, thyroid and ovary. Strongly expressed also in fetal lung. {ECO:0000269|PubMed:9686600}.; . . 0.44743 0.19790 -0.648365105 16.35999056 3122.31046 10.62667 CRLF2 0.00278020670397447 0.93827744138307 0.0589423519129555 cytokine receptor-like factor 2 FUNCTION: Receptor for thymic stromal lymphopoietin (TSLP). Forms a functional complex with TSLP and IL7R which is capable of stimulating cell proliferation through activation of STAT3 and STAT5. Also activates JAK2 (By similarity). Implicated in the development of the hematopoietic system. {ECO:0000250, ECO:0000269|PubMed:11418668}.; . TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, kidney and adult and fetal liver. Primarily expressed in dendrites and monocytes. Weakly expressed in T-cells.; . . . . . . 82.80927 1.93269 CRLF3 0.975928566236353 0.0240703953878368 1.03837580978467e-06 cytokine receptor-like factor 3 FUNCTION: May play a role in the negative regulation of cell cycle progression. {ECO:0000269|PubMed:19427400}.; . TISSUE SPECIFICITY: Expressed in several embryonic and adult tissues, including adult and fetal brain, liver, spleen and pancreas. Expressed in adult, but not fetal kidney. Expressed in skin and squamous cell carcinoma (SCC) and in several other cancer types. Also detected in lesion actinic keratosis (AK). {ECO:0000269|PubMed:16865251, ECO:0000269|PubMed:19427400}.; colon;skin;uterus;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;urinary;blood;skeletal muscle;breast;lung;adrenal gland;placenta;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;whole blood;bone marrow; 0.42919 0.10920 -0.47017169 23.25430526 975.05051 6.03795 CRLS1 0.0335080599829462 0.92727022084313 0.0392217191739241 cardiolipin synthase 1 FUNCTION: Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions. {ECO:0000269|PubMed:16547353, ECO:0000269|PubMed:16678169}.; . TISSUE SPECIFICITY: Highly expressed in tissues such as heart, skeletal muscle and liver. {ECO:0000269|PubMed:16547353}.; . . 0.12485 0.13806 . . 749.17245 5.42904 CRMP1 0.953273234767141 0.0467213626895119 5.40254334687058e-06 collapsin response mediator protein 1 FUNCTION: Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. May participate in cytokinesis. {ECO:0000269|PubMed:11562390, ECO:0000269|PubMed:19799413}.; . TISSUE SPECIFICITY: Brain.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;bladder;brain;heart;cartilage;tongue;pineal body;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;testis;pineal gland;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;hypothalamus;oral cavity;muscle;lung;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; amygdala;whole brain;occipital lobe;thalamus;fetal brain;cerebellum peduncles;temporal lobe;globus pallidus;pons;parietal lobe;cingulate cortex;cerebellum; 0.53346 0.16270 -0.753139731 13.67067705 1126.88312 6.40240 CRNDE . . . colorectal neoplasia differentially expressed (non-protein coding) . . . . . . . . . . . CRNKL1 0.881981246509602 0.118018733911444 1.95789542996747e-08 crooked neck pre-mRNA splicing factor 1 FUNCTION: Involved in pre-mRNA splicing process.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis. Not expressed in brain and lung.; . . 0.29171 0.17515 1.049013545 91.34819533 676.59451 5.19663 CRNN 0.000495360508958453 0.878554861127528 0.120949778363513 cornulin FUNCTION: Survival factor that participates in the clonogenicity of squamous esophageal epithelium cell lines, attenuates deoxycholic acid (DCA)-induced apoptotic cell death and release of calcium. When overexpressed in oral squamous carcinom cell lines, regulates negatively cell proliferation by the induction of G1 arrest. {ECO:0000269|PubMed:15896671, ECO:0000269|PubMed:16640557}.; . TISSUE SPECIFICITY: Squamous epithelia cell-specific. Expressed in the esophagus (periphery of the cells of the granular and the upper spinous layers), foreskin (granular and lower cornified cells), scalp skin (granular layer), inner root sheath of the hair follicle and in primary keratinocytes (at protein level). Expressed in the squamous epithelium of the cervix, esophagus, foreskin and larynx. Expressed in the fetal bladder and scalp skin. Expressed at very low levels in the lung, kidney, uterus, skeletal muscle, heart and fetal brain. Undetectable or barely detectable in esophageal and oral squamous cell carcinoma compared with the matched adjacent normal esophageal mucosa. Undetectable or barely detectable in larynx and esophagus from patients with pH-documented laryngopharyngeal reflux (LPR). {ECO:0000269|PubMed:11056050, ECO:0000269|PubMed:11606197, ECO:0000269|PubMed:15854041, ECO:0000269|PubMed:15896671, ECO:0000269|PubMed:16466100, ECO:0000269|PubMed:16640557, ECO:0000269|PubMed:17289885}.; oesophagus;larynx;thyroid;oral cavity;hypopharynx;cervix;head and neck;skeletal muscle; tongue;atrioventricular node;skeletal muscle;tonsil; 0.20084 0.08510 0.753291803 86.71266808 894.83695 5.83074 CROCC 4.70612895871808e-20 0.643040868149548 0.356959131850452 ciliary rootlet coiled-coil, rootletin FUNCTION: Major structural component of the ciliary rootlet, a cytoskeletal-like structure in ciliated cells which originates from the basal body at the proximal end of a cilium and extends proximally toward the cell nucleus. Contributes to centrosome cohesion before mitosis. {ECO:0000250|UniProtKB:Q8CJ40, ECO:0000269|PubMed:16203858}.; . . . . . 0.15832 2.431142199 98.53149328 3783.54242 12.05321 CROCC2 . . . ciliary rootlet coiled-coil, rootletin family member 2 . . . . . . . . . . . CROCCP1 . . . ciliary rootlet coiled-coil, rootletin pseudogene 1 . . . . . . . . . . . CROCCP2 . . . ciliary rootlet coiled-coil, rootletin pseudogene 2 . . . unclassifiable (Anatomical System);uterus;lung;frontal lobe;heart;nasopharynx;adrenal medulla;liver;blood;germinal center;brain;bone marrow; . . . . . . . CROCCP3 . . . ciliary rootlet coiled-coil, rootletin pseudogene 3 . . . unclassifiable (Anatomical System);frontal lobe;cartilage;hypothalamus;liver;spleen;kidney;retina; . 0.06928 . . . . . CROCCP4 . . . ciliary rootlet coiled-coil, rootletin pseudogene 4 . . . . . . . . . . . CROCCP5 . . . ciliary rootlet coiled-coil, rootletin pseudogene 5 . . . . . . . . . . . CROT 6.7490162375597e-21 0.00316259928464714 0.996837400715353 carnitine O-octanoyltransferase FUNCTION: Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate. Converts the end product of pristanic acid beta oxidation, 4,8-dimethylnonanoyl- CoA, to its corresponding carnitine ester. {ECO:0000269|PubMed:10486279}.; . . sympathetic chain;colon;fovea centralis;skin;bone marrow;retina;uterus;prostate;endometrium;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);islets of Langerhans;blood;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; fetal liver;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08801 0.20255 -0.374708069 28.15522529 169.89771 2.84516 CRP 3.06308864362311e-05 0.192677768362788 0.807291600750776 C-reactive protein, pentraxin-related FUNCTION: Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells.; . TISSUE SPECIFICITY: Found in plasma.; unclassifiable (Anatomical System);pancreas;cerebral cortex;liver;skeletal muscle;gall bladder; superior cervical ganglion;subthalamic nucleus;beta cell islets;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.04842 0.44343 -0.117432389 44.89266336 36.61007 1.09881 CRPP1 . . . C-reactive protein pseudogene 1 . . . . . . . . . . . CRSP5 . . . cofactor required for Sp1 transcriptional activation, subunit 5 . . . . . . . . . . . CRTAC1 0.000140635307914693 0.991653360960028 0.00820600373205704 cartilage acidic protein 1 . . TISSUE SPECIFICITY: Expressed in the interterritorial matrix of articular deep zone cartilage (at protein level). Isoform 1 and isoform 2 are expressed in brain. Isoform 1 is detected in lung and chondrocytes. Detected in cartilage, bone, cultured chondrocytes and lung, and at low levels in heart. Not detected in osteoblasts. {ECO:0000269|PubMed:11139377, ECO:0000269|PubMed:17074475}.; colon;choroid;fovea centralis;skin;retina;uterus;optic nerve;thyroid;bone;iris;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;pineal body;lens;lung;visual apparatus;hippocampus;macula lutea;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14185 0.12392 -0.769738365 13.16348195 545.54373 4.75083 CRTAM 1.15272875885834e-06 0.57117203841123 0.428826808860011 cytotoxic and regulatory T-cell molecule FUNCTION: Interaction with CADM1 promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM3 in vivo. {ECO:0000250|UniProtKB:Q149L7, ECO:0000269|PubMed:15811952}.; . TISSUE SPECIFICITY: In the immune system, expression is restricted to activated class-I MHC-restricted cells, including NKT and CD8 cells. Strongly expressed in spleen, thymus, small intestine, peripheral blood leukocyte, and in Purkinje neurons in cerebellum. Expressed at much lower levels in testis, ovary, colon, lung and lymphoid tissues. {ECO:0000269|PubMed:10811014, ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:16300832}.; unclassifiable (Anatomical System);lung;cerebellum cortex;blood;kidney;skeletal muscle;cerebellum; superior cervical ganglion;cerebellum peduncles;ciliary ganglion;cerebellum; 0.20353 0.11606 0.598963042 82.7789573 1108.20566 6.36474 CRTAP 5.34389142589516e-05 0.679606292449112 0.32034026863663 cartilage associated protein FUNCTION: Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues. {ECO:0000269|PubMed:17055431}.; . TISSUE SPECIFICITY: Found in articular chondrocytes. Expressed in a variety of tissues.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;oesophagus;cerebral cortex;larynx;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;mesenchyma;adrenal gland;placenta;duodenum;hypopharynx;amnion;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.15856 0.10994 . . 1344.52242 6.88505 CRTC1 0.980548236291021 0.0194511499424776 6.13766501393763e-07 CREB regulated transcription coactivator 1 FUNCTION: Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PGC1alpha and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR). In the hippocampus, involved in late-phase long- term potentiation (L-LTP) maintenance at the Schaffer collateral- CA1 synapses. May be required for dendritic growth of developing cortical neurons (By similarity). In concert with SIK1, regulates the light-induced entrainment of the circadian clock. In response to light stimulus, coactivates the CREB-mediated transcription of PER1 which plays an important role in the photic entrainment of the circadian clock. {ECO:0000250|UniProtKB:Q157S1, ECO:0000250|UniProtKB:Q68ED7, ECO:0000269|PubMed:23699513}.; DISEASE: Note=A chromosomal aberration involving CRTC1 is found in mucoepidermoid carcinomas, benign Warthin tumors and clear cell hidradenomas. Translocation t(11;19)(q21;p13) with MAML2. The fusion protein consists of the N-terminus of CRTC1 joined to the C-terminus of MAML2. The reciprocal fusion protein consisting of the N-terminus of MAML2 joined to the C-terminus of CRTC1 has been detected in a small number of mucoepidermoid carcinomas.; TISSUE SPECIFICITY: Highly expressed in adult and fetal brain. Located to specific regions such as the prefrontal cortex and cerebellum. Very low expression in other tissues such as heart, spleen, lung, skeletal muscle, salivary gland, ovary and kidney. {ECO:0000269|PubMed:14720503, ECO:0000269|PubMed:16980408}.; ovary;adrenal medulla;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;synovium;bone;thyroid;testis;germinal center;brain;amygdala;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;hippocampus;visual apparatus;liver;kidney;cerebellum; amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;cerebellum peduncles;pons;atrioventricular node;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.23783 0.22982 -0.400392389 26.85185185 1186.85367 6.53335 CRTC2 0.996361791046642 0.00363819884687368 1.01064847668257e-08 CREB regulated transcription coactivator 2 FUNCTION: Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates gluconeogenesis as a component of the LKB1/AMPK/TORC2 signaling pathway. Regulates the expression of specific genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR). {ECO:0000269|PubMed:14506290, ECO:0000269|PubMed:14536081, ECO:0000269|PubMed:15454081, ECO:0000269|PubMed:16809310, ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:16980408, ECO:0000269|PubMed:17210223}.; . TISSUE SPECIFICITY: Most abundantly expressed in the thymus. Present in both B and T-lymphocytes. Highly expressed in HEK293T cells and in insulinomas. High levels also in spleen, ovary, muscle and lung, with highest levels in muscle. Lower levels found in brain, colon, heart, kidney, prostate, small intestine and stomach. Weak expression in liver and pancreas. {ECO:0000269|PubMed:14536081, ECO:0000269|PubMed:15454081, ECO:0000269|PubMed:16980408}.; lymphoreticular;ovary;colon;parathyroid;skin;uterus;optic nerve;whole body;endometrium;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;urinary;blood;lens;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion; 0.25674 0.23695 -0.690637458 15.12149092 1834.62554 7.89581 CRTC3 0.983929956417642 0.0160699659677388 7.76146196514015e-08 CREB regulated transcription coactivator 3 FUNCTION: Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR). {ECO:0000269|PubMed:14506290, ECO:0000269|PubMed:15454081, ECO:0000269|PubMed:15466468, ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:16980408, ECO:0000269|PubMed:17210223, ECO:0000269|PubMed:17644518}.; . TISSUE SPECIFICITY: Predominantly expressed in B and T lymphocytes. Highest levels in lung. Also expressed in brain, colon, heart, kidney, ovary, and prostate. Weak expression in liver, pancreas, muscle, small intestine, spleen and stomach. {ECO:0000269|PubMed:14536081, ECO:0000269|PubMed:16980408}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;tongue;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14323 0.12691 -1.240018202 5.461193678 2714.46242 9.81269 CRTC3-AS1 . . . CRTC3 antisense RNA 1 . . . . . . . . . . . CRX 0.623714816368051 0.368759849176976 0.00752533445497271 cone-rod homeobox FUNCTION: Transcription factor that binds and transactivates the sequence 5'-TAATC[CA]-3' which is found upstream of several photoreceptor-specific genes, including the opsin genes. Acts synergistically with other transcription factors, such as NRL, RORB and RAX, to regulate photoreceptor cell-specific gene transcription. Essential for the maintenance of mammalian photoreceptors. {ECO:0000269|PubMed:10625658}.; DISEASE: Cone-rod dystrophy 2 (CORD2) [MIM:120970]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. {ECO:0000269|PubMed:9390563, ECO:0000269|PubMed:9427255, ECO:0000269|PubMed:9792858}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa (RP) [MIM:268000]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:9427255, ECO:0000269|PubMed:9792858}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Retina.; unclassifiable (Anatomical System);optic nerve;pineal body;macula lutea;visual apparatus;fovea centralis;choroid;lens;pineal gland;skeletal muscle;retina; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.78537 0.33817 0.084621747 60.31493277 183.8471 2.94157 CRY1 4.24281789472779e-07 0.988513955987975 0.0114856197302354 cryptochrome circadian clock 1 FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time- keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. CRY1 and CRY2 have redundant functions but also differential and selective contributions at least in defining the pace of the SCN circadian clock and its circadian transcriptional outputs. More potent transcriptional repressor in cerebellum and liver than CRY2, though more effective in lengthening the period of the SCN oscillator. On its side, CRY2 seems to play a critical role in tuning SCN circadian period by opposing the action of CRY1. With CRY2, is dispensable for circadian rhythm generation but necessary for the development of intercellular networks for rhythm synchrony. Capable of translocating circadian clock core proteins such as PER proteins to the nucleus. Interacts with CLOCK-ARNTL/BMAL1 independently of PER proteins and is found at CLOCK-ARNTL/BMAL1-bound sites, suggesting that CRY may act as a molecular gatekeeper to maintain CLOCK-ARNTL/BMAL1 in a poised and repressed state until the proper time for transcriptional activation. Represses the CLOCK- ARNTL/BMAL1 induced transcription of BHLHE40/DEC1. Represses the CLOCK-ARNTL/BMAL1 induced transcription of ATF4, MTA1, KLF10 and NAMPT (By similarity). May repress circadian target genes expression in collaboration with HDAC1 and HDAC2 through histone deacetylation. Mediates the clock-control activation of ATR and modulates ATR-mediated DNA damage checkpoint. In liver, mediates circadian regulation of cAMP signaling and gluconeogenesis by binding to membrane-coupled G proteins and blocking glucagon- mediated increases in intracellular cAMP concentrations and CREB1 phosphorylation. Besides its role in the maintenance of the circadian clock, is also involved in the regulation of other processes. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by binding to glucocorticoid response elements (GREs). Plays a key role in glucose and lipid metabolism modulation, in part, through the transcriptional regulation of genes involved in these pathways, such as LEP or ACSL4. {ECO:0000250|UniProtKB:P97784, ECO:0000269|PubMed:10531061, ECO:0000269|PubMed:14672706, ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:23133559}.; . . medulla oblongata;colon;parathyroid;fovea centralis;skin;retina;uterus;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;trophoblast;heart;cartilage;islets of Langerhans;adrenal cortex;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;stomach; testis; 0.54876 0.22335 -0.890882376 10.30313753 20.79741 0.70484 CRY2 0.993283035571508 0.00671691922713641 4.52013554002214e-08 cryptochrome circadian clock 2 FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time- keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. CRY1 and CRY2 have redundant functions but also differential and selective contributions at least in defining the pace of the SCN circadian clock and its circadian transcriptional outputs. Less potent transcriptional repressor in cerebellum and liver than CRY1, though less effective in lengthening the period of the SCN oscillator. Seems to play a critical role in tuning SCN circadian period by opposing the action of CRY1. With CRY1, dispensable for circadian rhythm generation but necessary for the development of intercellular networks for rhythm synchrony. May mediate circadian regulation of cAMP signaling and gluconeogenesis by blocking glucagon-mediated increases in intracellular cAMP concentrations and in CREB1 phosphorylation. Besides its role in the maintenance of the circadian clock, is also involved in the regulation of other processes. Plays a key role in glucose and lipid metabolism modulation, in part, through the transcriptional regulation of genes involved in these pathways, such as LEP or ACSL4. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by binding to glucocorticoid response elements (GREs). Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1. Represses the CLOCK-ARNTL/BMAL1 induced transcription of NAMPT (By similarity). {ECO:0000250|UniProtKB:Q9R194, ECO:0000269|PubMed:10531061, ECO:0000269|PubMed:14672706, ECO:0000269|PubMed:16790549}.; . TISSUE SPECIFICITY: Expressed in all tissues examined including fetal brain, fibroblasts, heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocytes. Highest levels in heart and skeletal muscle. {ECO:0000269|PubMed:8909283, ECO:0000269|PubMed:9801304}.; . . 0.39499 0.18708 -0.135838822 43.77211607 180.46973 2.91976 CRYAA 0.521020324207416 0.462098658271808 0.016881017520776 crystallin alpha A FUNCTION: Contributes to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. {ECO:0000269|PubMed:22120592}.; DISEASE: Note=Alpha-crystallin A 1-172 is found at nearly twofold higher levels in diabetic lenses than in age-matched control lenses. {ECO:0000269|PubMed:12356833}.; DISEASE: Cataract 9, multiple types (CTRCT9) [MIM:604219]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT9 includes nuclear, zonular central nuclear, anterior polar, cortical, embryonal, anterior subcapsular, fan-shaped, and total cataracts, among others. In some cases cataract is associated with microcornea without any other systemic anomaly or dysmorphism. Microcornea is defined by a corneal diameter inferior to 10 mm in both meridians in an otherwise normal eye. {ECO:0000269|PubMed:14512969, ECO:0000269|PubMed:16453125, ECO:0000269|PubMed:18302245, ECO:0000269|PubMed:18407550, ECO:0000269|PubMed:23508780, ECO:0000269|PubMed:9467006}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in eye lens. {ECO:0000269|PubMed:12356833}.; unclassifiable (Anatomical System);colon;fovea centralis;choroid;lens;retina;optic nerve;whole body;visual apparatus;macula lutea;liver;iris;kidney;stomach;thymus; superior cervical ganglion;kidney;atrioventricular node; 0.16965 0.25991 -0.381986487 27.68931352 20.60065 0.70041 CRYAB 0.00909092009196377 0.583202484455738 0.407706595452298 crystallin alpha B FUNCTION: May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.; DISEASE: Myopathy, myofibrillar, 2 (MFM2) [MIM:608810]: A neuromuscular disorder that results in weakness of the proximal and distal limb muscles, weakness of the neck, velopharynx and trunk muscles, hypertrophic cardiomyopathy, and cataract in a subset of patients. {ECO:0000269|PubMed:14681890, ECO:0000269|PubMed:21920752, ECO:0000269|PubMed:9731540}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cataract 16, multiple types (CTRCT16) [MIM:613763]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT16 includes posterior polar cataract, among others. Posterior polar cataract is a subcapsular opacity, usually disk-shaped, located at the back of the lens. {ECO:0000269|PubMed:11577372}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myopathy, myofibrillar, fatal infantile hypertonic, alpha-B crystallin-related (MFMFIH-CRYAB) [MIM:613869]: A muscular dystrophy with onset in the first weeks of life after a normal neonatal period. Affected infants show rapidly progressive muscular rigidity of the trunk and limbs associated with increasing respiratory difficulty resulting in death before age 3 years. {ECO:0000269|PubMed:21337604}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1II (CMD1II) [MIM:615184]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:16483541, ECO:0000269|PubMed:16793013}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Lens as well as other tissues.; myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;corpus callosum;bone marrow;uterus;prostate;ganglion;cochlea;oesophagus;endometrium;bone;thyroid;testis;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;spinal cord;lens;skeletal muscle;greater omentum;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;spleen;cervix;kidney;mammary gland;aorta; whole brain;occipital lobe;medulla oblongata;thalamus;olfactory bulb;tongue;cerebellum peduncles;hypothalamus;spinal cord;caudate nucleus;skeletal muscle;prefrontal cortex;parietal lobe;cerebellum; 0.51320 0.56457 -0.251530012 35.42108988 19.62169 0.67310 CRYBA1 0.000721666003037628 0.920364815002001 0.0789135189949615 crystallin beta A1 FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.; DISEASE: Cataract 10, multiple types (CTRCT10) [MIM:600881]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT10 includes congenital zonular with sutural opacities, among others. This is a form of zonular cataract with an erect Y-shaped anterior and an inverted Y-shaped posterior sutural opacities. Zonular or lamellar cataracts are opacities, broad or narrow, usually consisting of powdery white dots affecting only certain layers or zones between the cortex and nucleus of an otherwise clear lens. The opacity may be so dense as to render the entire central region of the lens completely opaque, or so translucent that vision is hardly if at all impeded. Zonular cataracts generally do not involve the embryonic nucleus, though sometimes they involve the fetal nucleus. Usually sharply separated from a clear cortex outside them, they may have projections from their outer edges known as riders or spokes. {ECO:0000269|PubMed:15016766, ECO:0000269|PubMed:9788845}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);whole body;visual apparatus;lens;retina; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.58892 0.17689 0.439181676 77.69521113 64.30474 1.64479 CRYBA2 0.000626081708704005 0.728637364832545 0.270736553458751 crystallin beta A2 FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.; DISEASE: Cataract 42 (CTRCT42) [MIM:115900]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. {ECO:0000269|PubMed:23508780}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;islets of Langerhans;placenta;visual apparatus;pituitary gland;testis;blood;lens;brain; superior cervical ganglion;olfactory bulb;beta cell islets;adrenal cortex;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.13978 0.12248 -0.183570861 39.95046001 61.81003 1.60251 CRYBA4 6.69435979827333e-08 0.257581927322445 0.742418005733957 crystallin beta A4 FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.; DISEASE: Cataract 23 (CTRCT23) [MIM:610425]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT23 is a zonular cataract. Zonular or lamellar cataracts are opacities, broad or narrow, usually consisting of powdery white dots affecting only certain layers or zones between the cortex and nucleus of an otherwise clear lens. The opacity may be so dense as to render the entire central region of the lens completely opaque, or so translucent that vision is hardly if at all impeded. Zonular cataracts generally do not involve the embryonic nucleus, though sometimes they involve the fetal nucleus. Usually sharply separated from a clear cortex outside them, they may have projections from their outer edges known as riders or spokes. {ECO:0000269|PubMed:16960806}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . optic nerve;whole body;ovary;placenta;macula lutea;visual apparatus;parathyroid;fovea centralis;choroid;lens;retina; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.20946 0.13306 0.21689899 68.12927577 150.50912 2.67784 CRYBB1 0.000388650496371835 0.844148805109281 0.155462544394347 crystallin beta B1 FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.; DISEASE: Cataract 17, multiple types (CTRCT17) [MIM:611544]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT17 includes nuclear and pulverulent cataracts, among others. Nuclear cataracts affect the central nucleus of the eye, are often not highly visually significant. The density of the opacities varies greatly from fine dots to a dense, white and chalk-like, central cataract. The condition is usually bilateral. Nuclear cataracts are often combined with opacified cortical fibers encircling the nuclear opacity, which are referred to as cortical riders. Pulverulent cataracts are characterized by a dust-like, 'pulverised' appearance of the opacities which can be found in any part of the lens. {ECO:0000269|PubMed:12360425, ECO:0000269|PubMed:17460281, ECO:0000269|PubMed:23508780}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=CRYBB1 mutations may be a cause of congenital cataract and microcornea syndrome, a disease characterized by the association of congenital cataract and microcornea without any other systemic anomaly or dysmorphism. Clinical findings include a corneal diameter inferior to 10 mm in both meridians in an otherwise normal eye, and an inherited cataract, which is most often bilateral posterior polar with opacification in the lens periphery. The cataract progresses to form a total cataract after visual maturity has been achieved, requiring cataract extraction in the first to third decade of life (PubMed:16110300 and PubMed:21972112). {ECO:0000305|PubMed:16110300, ECO:0000305|PubMed:21972112}.; . unclassifiable (Anatomical System);lung;whole body;ovary;placenta;visual apparatus;testis;parathyroid;germinal center;lens;brain;retina; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.06348 0.13405 -0.22584292 37.32012267 46.74188 1.32118 CRYBB2 0.583885170755227 0.413897043301654 0.00221778594311951 crystallin beta B2 FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.; DISEASE: Cataract 3, multiple types (CTRCT3) [MIM:601547]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT3 includes congenital cerulean and sutural cataract with punctate and cerulean opacities, among others. Cerulean cataract is characterized by peripheral bluish and white opacifications organized in concentric layers with occasional central lesions arranged radially. The opacities are observed in the superficial layers of the fetal nucleus as well as the adult nucleus of the lens. Involvement is usually bilateral. Visual acuity is only mildly reduced in childhood. In adulthood, the opacifications may progress, making lens extraction necessary. Histologically the lesions are described as fusiform cavities between lens fibers which contain a deeply staining granular material. Although the lesions may take on various colors, a dull blue is the most common appearance and is responsible for the designation cerulean cataract. Sutural cataract with punctate and cerulean opacities is characterized by white opacification around the anterior and posterior Y sutures, and grayish and bluish, spindle shaped, oval punctate and cerulean opacities of various sizes arranged in lamellar form. The spots are more concentrated towards the peripheral layers and do not delineate the embryonal or fetal nucleus. Phenotypic variation with respect to the size and density of the sutural opacities as well as the number and position of punctate and cerulean spots is observed among affected subjects. {ECO:0000269|PubMed:10634616, ECO:0000269|PubMed:9158139}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.26816 0.13347 0.3032669 72.009908 209.78315 3.12642 CRYBB2P1 . . . crystallin beta B2 pseudogene 1 . . . . . 0.26816 . . . . . CRYBB3 4.07383009403585e-10 0.0274072365310746 0.972592763061542 crystallin beta B3 FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.; DISEASE: Cataract 22, multiple types (CTRCT22) [MIM:609741]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT22 includes nuclear cataract among others. Nuclear cataracts affect the central nucleus of the eye, and are often not highly visually significant. The density of the opacities varies greatly from fine dots to a dense, white and chalk-like, central cataract. The condition is usually bilateral. Nuclear cataracts are often combined with opacified cortical fibers encircling the nuclear opacity, which are referred to as cortical riders. {ECO:0000269|PubMed:15914629, ECO:0000269|PubMed:23508780}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . visual apparatus;lens; dorsal root ganglion;uterus corpus;subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.12131 0.12533 0.819433854 87.98655343 414.22991 4.26280 CRYBG3 0.000473718112503729 0.999466396142981 5.98857445152075e-05 crystallin beta-gamma domain containing 3 FUNCTION: Isoform vlAKAP: Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). {ECO:0000269|PubMed:25097019}.; . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;larynx;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;thyroid;globus pallidus;testis;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; . . . . 3552.09662 11.51760 CRYGA 0.000127117288397655 0.626172345781499 0.373700536930103 crystallin gamma A FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.; . . unclassifiable (Anatomical System);whole body;visual apparatus; superior cervical ganglion;skeletal muscle; 0.16773 0.13686 0.016664174 55.21939137 30.09915 0.96006 CRYGB 2.05606816353459e-09 0.0192317314523181 0.980768266491614 crystallin gamma B FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.; DISEASE: Cataract 39, multiple types (CTRCT39) [MIM:615188]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT39 includes lamellar, anterior polar, and complete cataracts. {ECO:0000269|PubMed:23288985}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . visual apparatus;lens; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.15041 0.11509 0.12689526 63.00424628 76.8106 1.83945 CRYGC 0.0436098458397775 0.849212979486611 0.107177174673611 crystallin gamma C FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.; DISEASE: Cataract 2, multiple types (CTRCT2) [MIM:604307]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT2 includes Coppock-like cataract, among others. Coppock-like cataract is a congenital pulverulent disk-like opacity involving the embryonic nucleus with many tiny white dots in the lamellar portion of the lens. It is usually bilateral and dominantly inherited. In some cases, CTRCT2 is associated with microcornea without any other systemic anomaly or dysmorphism. Microcornea is defined by a corneal diameter inferior to 10 mm in both meridians in an otherwise normal eye. {ECO:0000269|PubMed:10521291, ECO:0000269|PubMed:10914683, ECO:0000269|PubMed:12011157, ECO:0000269|PubMed:22052681, ECO:0000269|PubMed:22876111}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);visual apparatus;lens;retina; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion; 0.11791 0.39607 0.327131069 73.27199811 150.98482 2.68607 CRYGD 0.00822648074513727 0.791445989750453 0.20032752950441 crystallin gamma D FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.; DISEASE: Cataract 4, multiple types (CTRCT4) [MIM:115700]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT4 includes crystalline aculeiform, congenital cerulean and non-nuclear polymorphic cataracts, among others. Crystalline aculeiform cataract is characterized by fiberglass-like or needle-like crystals projecting in different directions, through or close to the axial region of the lens. Non- nuclear polymorphic cataract is a partial opacity with variable location between the fetal nucleus of the lens and the equator. The fetal nucleus is normal. The opacities are irregular and look similar to a bunch of grapes and may be present simultaneously in different lens layers. Congenital cerulean cataract is characterized by peripheral bluish and white opacifications organized in concentric layers with occasional central lesions arranged radially. The opacities are observed in the superficial layers of the fetal nucleus as well as the adult nucleus of the lens. Involvement is usually bilateral. Visual acuity is only mildly reduced in childhood. In adulthood, the opacifications may progress, making lens extraction necessary. Histologically the lesions are described as fusiform cavities between lens fibers which contain a deeply staining granular material. Although the lesions may take on various colors, a dull blue is the most common appearance and is responsible for the designation cerulean cataract. {ECO:0000269|PubMed:10521291, ECO:0000269|PubMed:10915766, ECO:0000269|PubMed:12011157, ECO:0000269|PubMed:12676897, ECO:0000269|PubMed:16943771, ECO:0000269|PubMed:17564961, ECO:0000269|PubMed:21031598, ECO:0000269|PubMed:9927684}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;visual apparatus;lens; superior cervical ganglion;temporal lobe;ciliary ganglion;atrioventricular node;skeletal muscle; 0.29024 0.14720 0.058937498 58.26256192 67.34919 1.69896 CRYGEP . . . crystallin gamma E, pseudogene . . . . . . . . . . . CRYGFP . . . crystallin gamma F, pseudogene . . . . . . . . . . . CRYGGP . . . crystallin gamma G, pseudogene . . . . . . . . . . . CRYGN 4.64269756915624e-05 0.415506809705881 0.584446763318427 crystallin gamma N . . TISSUE SPECIFICITY: Not specifically expressed in eye. {ECO:0000269|PubMed:15853812}.; unclassifiable (Anatomical System); . . 0.09572 -0.005381972 53.50908233 210.15598 3.12824 CRYGS 0.182730047254129 0.764806519162764 0.0524634335831074 crystallin gamma S FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.; DISEASE: Cataract 20, multiple types (CTRCT20) [MIM:116100]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT20 includes progressive polymorphic anterior, posterior, or peripheral cortical. {ECO:0000269|PubMed:16141006}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);fovea centralis;choroid;lens;retina;uterus;pancreas;prostate;optic nerve;bone;macula lutea;visual apparatus;cervix;kidney;artery;brain;aorta; . 0.11636 . -0.251530012 35.42108988 15.28872 0.55039 CRYL1 1.86752538837027e-05 0.692720051756735 0.307261272989381 crystallin lambda 1 . . TISSUE SPECIFICITY: Widely expressed, with highest levels in liver and kidney. {ECO:0000269|PubMed:12527201}.; ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;thyroid;pituitary gland;testis;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;spinal cord;pharynx;blood;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;spinal cord;liver;kidney;atrioventricular node; 0.13011 0.14157 -0.780646273 12.77423921 31.51503 0.99259 CRYM 0.0271487843921294 0.920702837339207 0.0521483782686632 crystallin mu FUNCTION: Specifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. Presumably involved in the regulation of the free intracellular concentration of triiodothyronine and access to its nuclear receptors. {ECO:0000269|PubMed:21332720}.; . TISSUE SPECIFICITY: Expressed in neural tissue, muscle and kidney.; choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;frontal lobe;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;hypothalamus;lens;skeletal muscle;lung;adrenal gland;nasopharynx;hippocampus;macula lutea;liver;spleen;kidney;stomach;cerebellum; whole brain;amygdala;medulla oblongata;superior cervical ganglion;occipital lobe;cerebellum peduncles;temporal lobe;pons;caudate nucleus;subthalamic nucleus;globus pallidus;kidney;cingulate cortex;parietal lobe;cerebellum; 0.48071 0.23311 0.060756528 58.52795471 100.52724 2.17203 CRYM-AS1 . . . CRYM antisense RNA 1 . . . unclassifiable (Anatomical System); . . . . . . . CRYZ 1.14334039127866e-14 0.00294049122756474 0.997059508772424 crystallin zeta FUNCTION: Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. Enhances the stability of mRNA coding for BCL2. NADPH binding interferes with mRNA binding. {ECO:0000269|PubMed:17497241, ECO:0000269|PubMed:20103721}.; . TISSUE SPECIFICITY: Only very low amounts in the lens.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;breast;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;kidney;stomach; . 0.10673 0.42086 0.463046108 78.58575136 3335.56723 11.05782 CRYZL1 0.0906156756788058 0.907578997788516 0.00180532653267808 crystallin zeta like 1 . . TISSUE SPECIFICITY: Ubiquitous.; ovary;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;heart;tongue;islets of Langerhans;spinal cord;blood;bile duct;pia mater;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;head and neck;kidney;stomach; . 0.09871 0.09286 0.194852702 67.03231894 79.56355 1.88514 CRYZP1 . . . crystallin zeta pseudogene 1 . . . . . . . . . . . CRYZP2 . . . crystallin zeta pseudogene 2 . . . . . . . . . . . CS 0.999828375740044 0.000171624115547726 1.4440827779292e-10 citrate synthase . . . myocardium;ovary;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;heart;lacrimal gland;islets of Langerhans;pineal body;muscle;blood;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;stomach; thalamus;subthalamic nucleus;occipital lobe;adipose tissue;heart;adrenal gland;cerebellum peduncles;prefrontal cortex;parietal lobe;cingulate cortex;skeletal muscle;cerebellum; 0.92156 0.80454 -0.029247611 51.40363293 8.73718 0.32209 CSAD 2.4796775415935e-06 0.910134484639411 0.089863035683047 cysteine sulfinic acid decarboxylase . . . ovary;colon;parathyroid;bone marrow;uterus;whole body;endometrium;cochlea;bone;testis;germinal center;brain;unclassifiable (Anatomical System);tongue;islets of Langerhans;blood;breast;lung;epididymis;placenta;hippocampus;visual apparatus;head and neck;kidney;mammary gland; superior cervical ganglion;fetal brain;parietal lobe; 0.20006 0.26003 -0.334253673 30.70299599 105.98321 2.23250 CSAG1 0.000227012408951511 0.305989779985485 0.693783207605564 chondrosarcoma associated gene 1 . . TISSUE SPECIFICITY: Expressed in chondrosarcoma, melanoma, cartilage and testis, but not in other normal tissues. {ECO:0000269|PubMed:12039054}.; unclassifiable (Anatomical System);ovary;salivary gland;adrenal cortex;intestine;pharynx;colon;blood;skin;breast;prostate;lung;liver;kidney;brain;mammary gland;bladder; . 0.01704 . 0.924227736 89.61429582 714.31094 5.30676 CSAG2 . . . CSAG family member 2 FUNCTION: Drug-resistance related protein, its expression is associated with the chemotherapy resistant and neoplastic phenotype. May also be linked to the malignant phenotype.; . TISSUE SPECIFICITY: Weakly expressed in kidney. Expressed in various tumor cell lines including carcinomas, myeloid and lymphoid malignancies, melanomas and prostate cancer. Overexpressed in taxol-resistant breast cancer line MDA 435TR and the doxorubicin-resistant multiple myelanoma lines RPMI-8226/Dox40 and RPMI-8226/MDR10V.; . . 0.06594 . . . . . CSAG3 . . . CSAG family member 3 FUNCTION: Drug-resistance related protein, its expression is associated with the chemotherapy resistant and neoplastic phenotype. May also be linked to the malignant phenotype.; . TISSUE SPECIFICITY: Weakly expressed in kidney. Expressed in various tumor cell lines including carcinomas, myeloid and lymphoid malignancies, melanomas and prostate cancer. Overexpressed in taxol-resistant breast cancer line MDA 435TR and the doxorubicin-resistant multiple myelanoma lines RPMI-8226/Dox40 and RPMI-8226/MDR10V.; unclassifiable (Anatomical System);breast;adrenal gland;epididymis;bone;thyroid;adrenal cortex;parathyroid;pineal gland;mammary gland;skin; . 0.06746 . . . . . CSAG4 . . . CSAG family member 4 (pseudogene) . . . unclassifiable (Anatomical System);breast;lung;bone; . 0.06926 . . . . . CSDC2 0.0798035156205298 0.753807014556474 0.166389469822996 cold shock domain containing C2 FUNCTION: RNA-binding factor which binds specifically to the very 3'-UTR ends of both histone H1 and H3.3 mRNAs, encompassing the polyadenylation signal. Might play a central role in the negative regulation of histone variant synthesis in the developing brain (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;cartilage;colon;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;lung;cerebral cortex;bone;macula lutea;iris;testis;spleen;kidney;brain;stomach; amygdala;thalamus;cerebellum peduncles;adrenal gland;hypothalamus;adrenal cortex;kidney;cerebellum; 0.17597 . -0.251530012 35.42108988 19.62493 0.67336 CSDE1 0.999951563731616 4.84362670434901e-05 1.34073690332789e-12 cold shock domain containing E1 FUNCTION: RNA-binding protein. Required for internal initiation of translation of human rhinovirus RNA. May be involved in translationally coupled mRNA turnover. Implicated with other RNA- binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding- region determinant of instability (mCRD) domain. {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:15314026}.; . . myocardium;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;pia mater;lung;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;aorta;stomach;thymus; dorsal root ganglion;testis - interstitial;thalamus;occipital lobe;superior cervical ganglion;hypothalamus;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.71193 0.17821 -1.001120478 8.321538099 30.92563 0.97838 CSE1L 0.999981566389526 1.84336104487003e-05 2.57892772073954e-14 CSE1 chromosome segregation 1-like (yeast) FUNCTION: Export receptor for importin-alpha. Mediates importin- alpha re-export from the nucleus to the cytoplasm after import substrates (cargos) have been released into the nucleoplasm. In the nucleus binds cooperatively to importin-alpha and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the importin-alpha from the export receptor. CSE1L/XPO2 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000269|PubMed:9323134}.; . TISSUE SPECIFICITY: Highly expressed in proliferating cells.; lymphoreticular;ovary;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;adrenal cortex;blood;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;tumor;testis;ciliary ganglion;trigeminal ganglion; 0.95238 0.38765 -1.021348453 7.997169144 180.17032 2.91629 CSE1L-AS1 . . . CSE1L antisense RNA 1 . . . . . . . . . . . CSF1 0.939718909454486 0.0602304951277747 5.05954177396181e-05 colony stimulating factor 1 FUNCTION: Cytokine that plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of proinflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone development. Required for normal male and female fertility. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration. Plays a role in lipoprotein clearance. {ECO:0000269|PubMed:16337366, ECO:0000269|PubMed:19934330, ECO:0000269|PubMed:20504948, ECO:0000269|PubMed:20829061}.; DISEASE: Note=Aberrant expression of CSF1 or CSF1R can promote cancer cell proliferation, invasion and formation of metastases. Overexpression of CSF1 or CSF1R is observed in a significant percentage of breast, ovarian, prostate, and endometrial cancers.; DISEASE: Note=Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases, such as rheumatoid arthritis, glomerulonephritis, atherosclerosis, and allograft rejection.; . unclassifiable (Anatomical System);lymphoreticular;tongue;islets of Langerhans;blood;skeletal muscle;bone marrow;breast;pancreas;lung;thyroid;liver;iris;cervix;head and neck;spleen;brain;spinal ganglion;stomach; dorsal root ganglion;superior cervical ganglion;medulla oblongata;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.16205 0.60708 0.288494088 71.50861052 204.01063 3.08330 CSF1R 0.993497648111379 0.00650235017917715 1.70944343508137e-09 colony stimulating factor 1 receptor FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of proinflammatory chemokines in response to IL34 and CSF1, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone and tooth development. Required for normal male and female fertility, and for normal development of milk ducts and acinar structures in the mammary gland during pregnancy. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration, and promotes cancer cell invasion. Activates several signaling pathways in response to ligand binding. Phosphorylates PIK3R1, PLCG2, GRB2, SLA2 and CBL. Activation of PLCG2 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5- trisphosphate, that then lead to the activation of protein kinase C family members, especially PRKCD. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to activation of the AKT1 signaling pathway. Activated CSF1R also mediates activation of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1, and of the SRC family kinases SRC, FYN and YES1. Activated CSF1R transmits signals both via proteins that directly interact with phosphorylated tyrosine residues in its intracellular domain, or via adapter proteins, such as GRB2. Promotes activation of STAT family members STAT3, STAT5A and/or STAT5B. Promotes tyrosine phosphorylation of SHC1 and INPP5D/SHIP- 1. Receptor signaling is down-regulated by protein phosphatases, such as INPP5D/SHIP-1, that dephosphorylate the receptor and its downstream effectors, and by rapid internalization of the activated receptor. {ECO:0000269|PubMed:12882960, ECO:0000269|PubMed:15117969, ECO:0000269|PubMed:16170366, ECO:0000269|PubMed:16337366, ECO:0000269|PubMed:16648572, ECO:0000269|PubMed:17121910, ECO:0000269|PubMed:18467591, ECO:0000269|PubMed:18814279, ECO:0000269|PubMed:19193011, ECO:0000269|PubMed:19934330, ECO:0000269|PubMed:20489731, ECO:0000269|PubMed:20504948, ECO:0000269|PubMed:20829061, ECO:0000269|PubMed:7683918}.; DISEASE: Note=Aberrant expression of CSF1 or CSF1R can promote cancer cell proliferation, invasion and formation of metastases. Overexpression of CSF1 or CSF1R is observed in a significant percentage of breast, ovarian, prostate, and endometrial cancers.; DISEASE: Note=Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases, such as rheumatoid arthritis, glomerulonephritis, atherosclerosis, and allograft rejection.; DISEASE: Leukoencephalopathy, diffuse hereditary, with spheroids (HDLS) [MIM:221820]: An autosomal dominant adult-onset rapidly progressive neurodegenerative disorder characterized by variable behavioral, cognitive, and motor changes. Patients often die of dementia within 6 years of onset. Brain imaging shows patchy abnormalities in the cerebral white matter, predominantly affecting the frontal and parietal lobes. {ECO:0000269|PubMed:22197934, ECO:0000269|PubMed:24532199}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in bone marrow and in differentiated blood mononuclear cells.; lymphoreticular;myocardium;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; placenta; 0.42433 0.52469 0.609894095 82.95588582 987.59415 6.06031 CSF2 0.803849286352491 0.19095065858299 0.00520005506451966 colony stimulating factor 2 FUNCTION: Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.; . . unclassifiable (Anatomical System);lymphoreticular;lung;bone;colon;blood; superior cervical ganglion;skeletal muscle; 0.92537 0.81181 0.413500896 76.67492333 2225.33403 8.69556 CSF2RA 0.00186657626375054 0.993221466591926 0.00491195714432338 colony stimulating factor 2 receptor alpha subunit FUNCTION: Low affinity receptor for granulocyte-macrophage colony- stimulating factor. Transduces a signal that results in the proliferation, differentiation, and functional activation of hematopoietic cells.; DISEASE: Pulmonary surfactant metabolism dysfunction 4 (SMDP4) [MIM:300770]: A rare lung disorder due to impaired surfactant homeostasis. It is characterized by alveolar filling with floccular material that stains positive using the periodic acid- Schiff method and is derived from surfactant phospholipids and protein components. Excessive lipoproteins accumulation in the alveoli results in severe respiratory distress. {ECO:0000269|PubMed:18955567, ECO:0000269|PubMed:18955570}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lung;endometrium;nasopharynx;placenta;bone;liver;testis;cervix;blood;kidney;brain;bone marrow; superior cervical ganglion;placenta;trigeminal ganglion; 0.23740 . 1.003094668 90.77022883 827.06033 5.63621 CSF2RB 0.00186665245080198 0.997129945163778 0.00100340238542048 colony stimulating factor 2 receptor beta common subunit FUNCTION: High affinity receptor for interleukin-3, interleukin-5 and granulocyte-macrophage colony-stimulating factor.; DISEASE: Pulmonary surfactant metabolism dysfunction 5 (SMDP5) [MIM:614370]: A rare lung disorder due to impaired surfactant homeostasis. It is characterized by alveolar filling with floccular material that stains positive using the periodic acid- Schiff method and is derived from surfactant phospholipids and protein components. Excessive lipoproteins accumulation in the alveoli results in severe respiratory distress. {ECO:0000269|PubMed:21075760}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);frontal lobe;placenta;liver;spleen;blood;germinal center;skeletal muscle;bone marrow; superior cervical ganglion;placenta;whole blood; 0.31080 0.24942 -1.076610636 7.324840764 1096.75329 6.34077 CSF2RBP1 . . . colony stimulating factor 2 receptor beta common subunit pseudogene 1 . . . . . . . . . . . CSF3 0.480555586092398 0.496825789469865 0.0226186244377369 colony stimulating factor 3 FUNCTION: Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes.; . . unclassifiable (Anatomical System);lung;colon;choroid;skin; dorsal root ganglion;superior cervical ganglion;smooth muscle;globus pallidus;fetal lung;ciliary ganglion;pons;kidney;atrioventricular node;skeletal muscle;cerebellum; 0.79897 0.85003 0.21689899 68.12927577 79.67938 1.88616 CSF3R 1.41619198119671e-06 0.98990737585362 0.0100912079543987 colony stimulating factor 3 receptor FUNCTION: Receptor for granulocyte colony-stimulating factor (CSF3), essential for granulocytic maturation. Plays a crucial role in the proliferation, differientation and survival of cells along the neutrophilic lineage. In addition it may function in some adhesion or recognition events at the cell surface. {ECO:0000269|PubMed:7514305}.; DISEASE: Hereditary neutrophilia (NEUTROPHILIA) [MIM:162830]: A form of lifelong, persistent neutrophilia, a condition characterized by an increase in the number of neutrophils in the blood. {ECO:0000269|PubMed:19620628}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: One or several isoforms have been found in myelogenous leukemia cell line KG-1, leukemia U-937 cell line, in bone marrow cells, placenta, and peripheral blood granulocytes. Isoform GCSFR-2 is found only in leukemia U-937 cells. Isoform GCSFR-3 is highly expressed in placenta.; unclassifiable (Anatomical System);cartilage;ovary;colon;blood;skeletal muscle;bone marrow;pancreas;prostate;lung;placenta;liver;spleen;brain;aorta;stomach; placenta;whole blood;bone marrow; 0.14855 0.33622 1.785787059 96.86836518 642.4902 5.09282 CSGALNACT1 6.87751081149391e-05 0.908439412243404 0.0914918126484807 chondroitin sulfate N-acetylgalactosaminyltransferase 1 FUNCTION: Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP- GalNAc to the non-reducing end of glucuronic acid (GlcUA). Required for addition of the first GalNAc to the core tetrasaccharide linker and for elongation of chondroitin chains. Important role in chondroitin chain biosynthesis in cartilage formation and subsequent endochondral ossification (PubMed:11788602, PubMed:12163485, PubMed:12446672, PubMed:17145758). Moreover, is involved in the metabolism of aggrecan (By similarity). {ECO:0000250|UniProtKB:Q8BJQ9, ECO:0000269|PubMed:11788602, ECO:0000269|PubMed:12163485, ECO:0000269|PubMed:12446672, ECO:0000269|PubMed:17145758}.; . TISSUE SPECIFICITY: Ubiquitous, with the highest levels in placenta, thyroid, bladder, prostate and adrenal gland. Detected at low levels in the other tissues examined. {ECO:0000269|PubMed:11788602, ECO:0000269|PubMed:12163485, ECO:0000269|PubMed:12446672}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;larynx;bone;thyroid;testis;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;liver;head and neck;kidney;mammary gland;stomach;aorta; thyroid; 0.49713 0.11453 -0.10469683 45.64755839 408.26992 4.23680 CSGALNACT2 0.451240634927787 0.548498353594189 0.00026101147802408 chondroitin sulfate N-acetylgalactosaminyltransferase 2 FUNCTION: Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP- GalNAc to the non-reducing end of glucuronic acid (GlcUA). Required for addition of the first GalNAc to the core tetrasaccharide linker and for elongation of chondroitin chains. {ECO:0000269|PubMed:12433924, ECO:0000269|PubMed:12446672}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12433924, ECO:0000269|PubMed:12446672}.; . . 0.32999 0.11194 -0.268115223 34.70747818 1778.77208 7.78907 CSH1 0.741138849069797 0.24783340080478 0.0110277501254234 chorionic somatomammotropin hormone 1 FUNCTION: Produced only during pregnancy and is involved in stimulating lactation, fetal growth and metabolism. Does not interact with GHR but only activates PRLR through zinc-induced dimerization. {ECO:0000269|PubMed:16546209}.; . . unclassifiable (Anatomical System);lung;optic nerve;placenta;macula lutea;pituitary gland;fovea centralis;choroid;brain;lens;aorta;retina; . 0.11533 . . . 99.39399 2.15814 CSH2 0.458223920935805 0.515305000237242 0.0264710788269535 chorionic somatomammotropin hormone 2 FUNCTION: Produced only during pregnancy and is involved in stimulating lactation, fetal growth and metabolism. Does not interact with GHR but only activates PRLR through zinc-induced dimerization. {ECO:0000269|PubMed:16546209}.; . . lung;frontal lobe;cerebral cortex;epididymis;placenta;pituitary gland;colon;brain;aorta; placenta;pituitary; 0.04737 0.07342 -0.139478553 43.29440906 29.18154 0.93272 CSHL1 0.000458792773342202 0.663172409757454 0.336368797469204 chorionic somatomammotropin hormone like 1 FUNCTION: May be a novel gestational hormone required to compensate for absence of other members of the GH/CS cluster during gestation. {ECO:0000269|PubMed:8083227}.; . . unclassifiable (Anatomical System);lung;optic nerve;cerebral cortex;placenta;macula lutea;pituitary gland;fovea centralis;choroid;brain;lens;aorta;retina; . 0.04322 0.08812 1.197888504 92.95234725 2953.70453 10.30062 CSK 0.999458351904314 0.000541645720840728 2.37484481797974e-09 c-src tyrosine kinase FUNCTION: Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN or YES1. Upon tail phosphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T- cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK. {ECO:0000269|PubMed:1639064, ECO:0000269|PubMed:9281320}.; . TISSUE SPECIFICITY: Expressed in lung and macrophages. {ECO:0000269|PubMed:1371489}.; lymphoreticular;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;lacrimal gland;pharynx;blood;lens;breast;pancreas;lung;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;white blood cells;whole blood;tonsil; 0.69070 0.67117 -0.137658575 43.57159707 91.78387 2.06177 CSMD1 . . . CUB and Sushi multiple domains 1 FUNCTION: Potential suppressor of squamous cell carcinomas.; . TISSUE SPECIFICITY: Weakly expressed in most tissues, except in brain. Expressed at intermediate level in brain, including cerebellum, substantia nigra, hippocampus and fetal brain. {ECO:0000269|PubMed:11572484}.; unclassifiable (Anatomical System);lung;placenta;liver;testis;spleen;mammary gland;bone marrow; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; 0.20953 0.12394 -7.110830664 0.023590469 1048.09747 6.21450 CSMD2 . . . CUB and Sushi multiple domains 2 . . TISSUE SPECIFICITY: Weakly expressed in most tissues, except in brain. Expressed at intermediate level in brain, including cerebellum, substantia nigra, hippocampus and fetal brain. Overexpressed in some head and neck cancer cell lines. {ECO:0000269|PubMed:11572484, ECO:0000269|PubMed:12906867}.; unclassifiable (Anatomical System);medulla oblongata;cartilage;colon;choroid;fovea centralis;lens;skeletal muscle;retina;pancreas;optic nerve;frontal lobe;macula lutea;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.56817 0.10766 -1.92180778 1.92262326 4329.11553 13.09506 CSMD2-AS1 . . . CSMD2 antisense RNA 1 . . . . . . . . . . . CSMD3 0.999999995922049 4.07795089857116e-09 1.04161332250208e-35 CUB and Sushi multiple domains 3 . . TISSUE SPECIFICITY: Weakly expressed in most tissues, except in brain. Expressed at intermediate level in brain, including cerebellum, substantia nigra, thalamus, spinal cord, hippocampus and fetal brain. Also expressed in testis. {ECO:0000269|PubMed:11572484, ECO:0000269|PubMed:12943675}.; unclassifiable (Anatomical System);optic nerve;lung;whole body;placenta;macula lutea;liver;testis;spleen;fovea centralis;choroid;lens;brain;retina; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;cerebellum peduncles;temporal lobe;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex; 0.39932 0.10693 -3.486527925 0.347959424 4750.0149 13.94247 CSN1S1 8.3001256244457e-06 0.517092680718277 0.482899019156098 casein alpha s1 FUNCTION: Important role in the capacity of milk to transport calcium phosphate.; . TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.; unclassifiable (Anatomical System); globus pallidus;ciliary ganglion;pons;skeletal muscle; 0.07367 . 1.016049644 90.86459071 172.88391 2.86273 CSN1S2AP . . . casein alpha s2-like A, pseudogene . . . . . . . . . . . CSN1S2BP . . . casein alpha s2-like B, pseudogene . . . . . . . . . . . CSN2 0.0588787964999457 0.867718533938229 0.0734026695618254 casein beta FUNCTION: Important role in determination of the surface properties of the casein micelles.; . TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;ciliary ganglion;caudate nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07782 0.38773 0.104848986 61.49445624 14.52918 0.52225 CSN3 0.000194175276675009 0.282855717145995 0.71695010757733 casein kappa FUNCTION: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.; . TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.; unclassifiable (Anatomical System);brain; dorsal root ganglion;uterus corpus;superior cervical ganglion;testis - seminiferous tubule;salivary gland;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.13908 0.14692 1.126294249 92.16206653 139.90818 2.58062 CSNK1A1 0.993657229734498 0.00634181098991656 9.59275585676678e-07 casein kinase 1 alpha 1 FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates CTNNB1 at 'Ser-45'. May phosphorylate PER1 and PER2. May play a role in segregating chromosomes during mitosis (PubMed:11955436, PubMed:1409656, PubMed:18305108). May play a role in keratin cytoskeleton disassembly and thereby, it may regulate epithelial cell migration (PubMed:23902688). {ECO:0000269|PubMed:11955436, ECO:0000269|PubMed:1409656, ECO:0000269|PubMed:18305108, ECO:0000269|PubMed:23902688}.; . . lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; testis; 0.62323 0.12971 -0.053113545 49.38664779 . . CSNK1A1L 0.000361793544139328 0.611454684719557 0.388183521736304 casein kinase 1 alpha 1 like FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling (By similarity). {ECO:0000250}.; . . . . 0.09568 0.17099 0.551232944 81.48148148 876.94945 5.76324 CSNK1A1P1 . . . casein kinase 1 alpha 1 pseudogene 1 . . . . . . . . . . . CSNK1A1P2 . . . casein kinase 1 alpha 1 pseudogene 2 . . . . . . . . . . . CSNK1A1P3 . . . casein kinase 1 alpha 1 pseudogene 3 . . . . . . . . . . . CSNK1D 0.991910743527009 0.00808751759690807 1.73887608245959e-06 casein kinase 1 delta FUNCTION: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phospohorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. EIF6 phosphorylation promotes its nuclear export. Triggers down-regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate. {ECO:0000269|PubMed:10606744, ECO:0000269|PubMed:12270943, ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:16027726, ECO:0000269|PubMed:17562708, ECO:0000269|PubMed:17962809, ECO:0000269|PubMed:19043076, ECO:0000269|PubMed:19339517, ECO:0000269|PubMed:20041275, ECO:0000269|PubMed:20048001, ECO:0000269|PubMed:20407760, ECO:0000269|PubMed:20637175, ECO:0000269|PubMed:20696890, ECO:0000269|PubMed:20699359, ECO:0000269|PubMed:21084295, ECO:0000269|PubMed:21422228, ECO:0000269|PubMed:23636092}.; DISEASE: Advanced sleep phase syndrome, familial, 2 (FASPS2) [MIM:615224]: A disorder characterized by very early sleep onset and offset. Individuals are 'morning larks' with a 4 hours advance of the sleep, temperature and melatonin rhythms. {ECO:0000269|PubMed:15800623, ECO:0000269|PubMed:23636092}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues examined, including brain, heart, lung, liver, pancreas, kidney, placenta and skeletal muscle. However, kinase activity is not uniform, with highest kinase activity in splenocytes. In blood, highly expressed in hemopoietic cells and mature granulocytes. Also found in monocytes and lymphocytes. {ECO:0000269|PubMed:15070676, ECO:0000269|PubMed:16027726}.; lymphoreticular;medulla oblongata;ovary;salivary gland;sympathetic chain;colon;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;placenta;visual apparatus;alveolus;liver;cervix;head and neck;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.95110 0.54626 -0.560178693 19.30879925 49.61197 1.37967 CSNK1E 0.967319235295747 0.0326698267913037 1.09379129490827e-05 casein kinase 1 epsilon FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates DVL1. Central component of the circadian clock. In balance with PP1, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phospohorylation. Controls PER1 and PER2 nuclear transport and degradation. Inhibits cytokine- induced granuloytic differentiation. {ECO:0000269|PubMed:12556519, ECO:0000269|PubMed:15070676, ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:16790549}.; . TISSUE SPECIFICITY: Expressed in all tissues examined, including brain, heart, lung, liver, pancreas, kidney, placenta and skeletal muscle. Expressed in monocytes and lymphocytes but not in granulocytes.; myocardium;smooth muscle;ovary;peritoneum;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;lens;skeletal muscle;breast;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;duodenum;hypopharynx;amnion;head and neck;kidney;stomach;aorta; superior cervical ganglion;subthalamic nucleus;medulla oblongata;prefrontal cortex;globus pallidus;pons;caudate nucleus;trigeminal ganglion;cingulate cortex;skeletal muscle;parietal lobe;cerebellum; 0.93099 0.58572 -0.339715008 30.06605331 43.28042 1.24924 CSNK1G1 0.999715378765103 0.000284620739691005 4.95205549749537e-10 casein kinase 1 gamma 1 FUNCTION: Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Regulates fast synaptic transmission mediated by glutamate (By similarity). Phosphorylates CLSPN. {ECO:0000250, ECO:0000269|PubMed:21680713}.; . . unclassifiable (Anatomical System);lymphoreticular;medulla oblongata;cartilage;heart;colon;blood;skin;breast;uterus;prostate;lung;endometrium;thyroid;placenta;liver;testis;spleen;cervix;germinal center;brain;mammary gland; superior cervical ganglion;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.46576 0.14486 -0.337894035 30.37272942 258.78315 3.45856 CSNK1G2 0.923449277236984 0.0764579609989865 9.27617640295224e-05 casein kinase 1 gamma 2 FUNCTION: Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates COL4A3BP/CERT, MTA1 and SMAD3. Involved in brain development and vesicular trafficking and neurotransmitter releasing from small synaptic vesicles. Regulates fast synaptic transmission mediated by glutamate. SMAD3 phosphorylation promotes its ligand-dependent ubiquitination and subsequent proteasome degradation, thus inhibiting SMAD3-mediated TGF-beta responses. Hyperphosphorylation of the serine-repeat motif of COL4A3BP/CERT leads to its inactivation by dissociation from the Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide and sphingomyelin synthesis. Triggers PER1 proteasomal degradation probably through phosphorylation. {ECO:0000269|PubMed:15077195, ECO:0000269|PubMed:15342122, ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:18794808, ECO:0000269|PubMed:19005213}.; . TISSUE SPECIFICITY: Testis.; lymphoreticular;medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;iris;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;muscle;urinary;blood;lens;lung;placenta;macula lutea;visual apparatus;duodenum;spleen;head and neck;kidney;stomach;thymus; subthalamic nucleus;testis - interstitial;thalamus;testis - seminiferous tubule;globus pallidus;testis;white blood cells;cingulate cortex; 0.51464 0.16878 -0.22584292 37.32012267 28.91263 0.92310 CSNK1G2-AS1 . . . CSNK1G2 antisense RNA 1 . . . unclassifiable (Anatomical System);lung;testis; . . . . . . . CSNK1G2P1 . . . casein kinase 1 gamma 2 pseudogene 1 . . . . . . . . . . . CSNK1G3 0.996751666329429 0.00324832600670227 7.66386867006088e-09 casein kinase 1 gamma 3 FUNCTION: Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Regulates fast synaptic transmission mediated by glutamate (By similarity). {ECO:0000250}.; . . ovary;parathyroid;skin;uterus;prostate;endometrium;thyroid;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;skeletal muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach; . 0.42585 0.18081 -0.317668748 31.45789101 9.29304 0.34102 CSNK2A1 0.999646697845993 0.000353301984341174 1.69665732196933e-10 casein kinase 2 alpha 1 FUNCTION: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin- mediated degradation. Plays an important role in the circadian clock function by phosphorylating ARNTL/BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry (PubMed:11239457, PubMed:11704824, PubMed:16193064, PubMed:19188443, PubMed:20625391, PubMed:22406621). Phosphorylates CCAR2 at 'Thr-454' in gastric carcinoma tissue (PubMed:24962073). {ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:11704824, ECO:0000269|PubMed:16193064, ECO:0000269|PubMed:19188443, ECO:0000269|PubMed:20625391, ECO:0000269|PubMed:22406621, ECO:0000269|PubMed:24962073}.; . TISSUE SPECIFICITY: Expressed in gastric carcinoma tissue and the expression gradually increases with the progression of the carcinoma (at protein level). {ECO:0000269|PubMed:24962073}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;muscle;lung;mesenchyma;nasopharynx;placenta;amnion;head and neck;kidney;stomach;thymus;cerebellum; superior cervical ganglion;cingulate cortex; 0.99836 0.79641 -0.339715008 30.06605331 7.97086 0.29277 CSNK2A2 0.999154189421807 0.000845803542775178 7.03541798681877e-09 casein kinase 2 alpha 2 FUNCTION: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV. {ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:11704824, ECO:0000269|PubMed:16193064}.; . . medulla oblongata;ovary;colon;skin;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;duodenum;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;testis; 0.99617 0.58572 -0.031067188 51.03798066 10.16945 0.37042 CSNK2A3 1.32371438961756e-11 0.0496591438930825 0.95034085609368 casein kinase 2 alpha 3 FUNCTION: Probable catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Amplification-dependent oncogene; promotes cell proliferation and tumorigenesis by down- regulating expression of the tumor suppressor protein, PML. May play a role in the pathogenesis of the lung cancer development and progression. {ECO:0000269|PubMed:20625391}.; . TISSUE SPECIFICITY: Detected in blood platelets and megakaryocyte cell lines. Poorly expressed in lung. Highly expressed in lung tumor tissues. {ECO:0000269|PubMed:12102635, ECO:0000269|PubMed:20625391}.; . . . . . . 3675.53563 11.78384 CSNK2B 0.943856699084629 0.0559357974872584 0.000207503428112901 casein kinase 2 beta FUNCTION: Participates in Wnt signaling (By similarity). Plays a complex role in regulating the basal catalytic activity of the alpha subunit. {ECO:0000250, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:16818610}.; . . . . . 0.20098 -0.09720619 46.20193442 16.21545 0.57542 CSPG4 8.89722030167291e-05 0.999905546853982 5.48094300110511e-06 chondroitin sulfate proteoglycan 4 FUNCTION: Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N- terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Functions also as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation. May stimulate alpha-4, beta-1 integrin- mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades. {ECO:0000269|PubMed:10587647, ECO:0000269|PubMed:11278606, ECO:0000269|PubMed:15210734}.; . TISSUE SPECIFICITY: Detected only in malignant melanoma cells. {ECO:0000269|PubMed:8790396}.; ovary;sympathetic chain;colon;parathyroid;choroid;skin;uterus;prostate;whole body;optic nerve;oesophagus;thyroid;bone;testis;brain;spinal ganglion;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;lung;placenta;spleen;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14288 0.14191 0.347031518 73.79098844 3644.03559 11.72399 CSPG4P1Y . . . chondroitin sulfate proteoglycan 4 pseudogene 1, Y-linked . . . colon;skeletal muscle; . . . . . . . CSPG4P2Y . . . chondroitin sulfate proteoglycan 4 pseudogene 2, Y-linked . . . colon;skeletal muscle; . . . . . . . CSPG4P3Y . . . chondroitin sulfate proteoglycan 4 pseudogene 3, Y-linked . . . . . . . . . . . CSPG4P4Y . . . chondroitin sulfate proteoglycan 4 pseudogene 4, Y-linked . . . brain;stomach; . . . . . . . CSPG4P5 . . . chondroitin sulfate proteoglycan 4 pseudogene 5 . . . . . . . . . . . CSPG4P8 . . . chondroitin sulfate proteoglycan 4 pseudogene 8 . . . . . . . . . . . CSPG4P9 . . . chondroitin sulfate proteoglycan 4 pseudogene 9 . . . . . . . . . . . CSPG4P10 . . . chondroitin sulfate proteoglycan 4 pseudogene 10 . . . . . . . . . . . CSPG4P11 . . . chondroitin sulfate proteoglycan 4 pseudogene 11 . . . . . . . . . . . CSPG4P12 . . . chondroitin sulfate proteoglycan 4 pseudogene 12 . . . . . . . . . . . CSPG4P13 . . . chondroitin sulfate proteoglycan 4 pseudogene 13 . . . . . . . . . . . CSPG5 0.414829723073552 0.577030996318862 0.00813928060758548 chondroitin sulfate proteoglycan 5 FUNCTION: May function as a growth and differentiation factor involved in neuritogenesis. May induce ERBB3 activation. {ECO:0000269|PubMed:15358134}.; . TISSUE SPECIFICITY: Restricted to brain (at protein level). {ECO:0000269|PubMed:9950058}.; unclassifiable (Anatomical System);hypothalamus;colon;blood;fovea centralis;choroid;lens;retina;bone marrow;optic nerve;whole body;lung;frontal lobe;adrenal gland;nasopharynx;macula lutea;visual apparatus;brain; whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.47217 0.15544 0.018483465 55.44939844 87.96072 2.00538 CSPP1 3.27686488216766e-13 0.999724880496394 0.000275119503277952 centrosome and spindle pole associated protein 1 FUNCTION: May play a role in cell-cycle-dependent microtubule organization. {ECO:0000269|PubMed:16826565}.; DISEASE: Joubert syndrome 21 (JBTS21) [MIM:615636]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy, renal disease, liver fibrosis, and polydactyly. {ECO:0000269|PubMed:24360803, ECO:0000269|PubMed:24360807, ECO:0000269|PubMed:24360808}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in adult and fetal brain with enrichment in the cerebellum. Detected in testis. {ECO:0000269|PubMed:15580290, ECO:0000269|PubMed:24360807}.; ovary;developmental;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;lens;skeletal muscle;breast;lung;epididymis;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08212 . -0.25902169 34.96697334 1764.62174 7.76246 CSRNP1 0.59953098933972 0.398521925205421 0.00194708545485921 cysteine and serine rich nuclear protein 1 FUNCTION: Binds to the consensus sequence 5'-AGAGTG-3' and has transcriptional activator activity (By similarity). May have a tumor-suppressor function. May play a role in apoptosis. {ECO:0000250, ECO:0000269|PubMed:11526492}.; . TISSUE SPECIFICITY: Ubiquitous. Most abundantly expressed in lung, placenta, skeletal muscle, pancreas and leukocyte. Frequently down-regulated in lung, kidney, liver and colon cancers compared with their corresponding normal tissues. {ECO:0000269|PubMed:11526492}.; medulla oblongata;ovary;colon;parathyroid;choroid;vein;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;alveolus;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;adrenal cortex;atrioventricular node;trigeminal ganglion; 0.23152 0.09962 -0.222203495 37.54423213 58.28318 1.54604 CSRNP2 0.950516343514854 0.0494528657986251 3.07906865207917e-05 cysteine and serine rich nuclear protein 2 FUNCTION: Binds to the consensus sequence 5'-AGAGTG-3' and has transcriptional activator activity (By similarity). May play a role in apoptosis. {ECO:0000250}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;synovium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;subthalamic nucleus;medulla oblongata;fetal brain;globus pallidus;testis;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.50361 0.10490 -0.246069119 36.06982779 313.58483 3.76505 CSRNP3 0.832452929930476 0.167517286703447 2.97833660770653e-05 cysteine and serine rich nuclear protein 3 FUNCTION: Binds to the consensus sequence 5'-AGAGTG-3' and has transcriptional activator activity. Plays a role in apoptosis (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;frontal lobe;testis;head and neck; amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;atrioventricular node;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.82712 0.10782 -0.179930907 40.35739561 301.30725 3.69846 CSRP1 0.00342203414248425 0.834222623347273 0.162355342510242 cysteine and glycine rich protein 1 FUNCTION: Could play a role in neuronal development.; . . myocardium;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;thyroid;amniotic fluid;bladder;brain;tonsil;heart;cartilage;pineal body;spinal cord;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;cervix;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus; whole brain;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;thalamus;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;uterus;prefrontal cortex;appendix;globus pallidus;cingulate cortex;parietal lobe; 0.28231 0.13256 0.215080721 67.91696155 102.93096 2.19258 CSRP2 0.000305231930183442 0.574322056037973 0.425372712031844 cysteine and glycine rich protein 2 FUNCTION: Drastically down-regulated in response to PDGF-BB or cell injury, that promote smooth muscle cell proliferation and dedifferentiation. Seems to play a role in the development of the embryonic vascular system.; . TISSUE SPECIFICITY: Highly expressed in the aorta, but not in heart and skeletal muscle.; salivary gland;developmental;colon;skin;retina;uterus;frontal lobe;larynx;bone;pituitary gland;testis;ciliary body;brain;artery;unclassifiable (Anatomical System);lymph node;trophoblast;heart;muscle;skeletal muscle;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;amnion;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; superior cervical ganglion;fetal brain;ciliary ganglion;skeletal muscle; 0.42950 0.10984 -0.141298762 42.87567823 17.04974 0.60059 CSRP2BP 1.34916992593767e-08 0.802379458034576 0.197620528473725 CSRP2 binding protein FUNCTION: Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. May function as a scaffold for the ATAC complex to promote ATAC complex stability. Has also weak histone acetyltransferase activity toward histone H4. Required for the normal progression through G1 and G2/M phases of the cell cycle. {ECO:0000269|PubMed:19103755}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, lung, placenta, brain, liver, pancreas and kidney. High expression in skeletal muscle and heart. Lower expression in lung.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;atrioventricular node;parietal lobe; 0.12194 0.09071 -0.018331246 52.2764803 249.89444 3.40522 CSRP2P1 . . . cysteine and glycine rich protein 2 pseudogene 1 . . . . . . . . . . . CSRP3 0.00220886834015439 0.757299847569078 0.240491284090768 cysteine and glycine rich protein 3 FUNCTION: Positive regulator of myogenesis. Plays a crucial and specific role in the organization of cytosolic structures in cardiomyocytes. Could play a role in mechanical stretch sensing. May be a scaffold protein that promotes the assembly of interacting proteins at Z-line structures. It is essential for calcineurin anchorage to the Z line. Required for stress-induced calcineurin-NFAT activation (By similarity). {ECO:0000250}.; DISEASE: Cardiomyopathy, familial hypertrophic 12 (CMH12) [MIM:612124]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:12642359, ECO:0000269|PubMed:18505755}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Cardiac and slow-twitch skeletal muscles.; unclassifiable (Anatomical System);myocardium;heart;ovary;muscle;parathyroid;skeletal muscle;pancreas;prostate;whole body;lung;placenta;alveolus;testis; heart;tongue;thyroid;fetal thyroid;skeletal muscle; 0.43029 0.21660 -0.359940251 28.93371078 25.21474 0.82453 CST1 2.8669819797472e-08 0.0244282673786607 0.975571703951519 cystatin SN FUNCTION: Human saliva appears to contain several cysteine proteinase inhibitors that are immunologically related to cystatin S but that differ in their specificity due to amino acid sequence differences. Cystatin SN, with a pI of 7.5, is a much better inhibitor of papain and dipeptidyl peptidase I than is cystatin S, although both inhibit ficin equally well.; . TISSUE SPECIFICITY: Expressed in submandibular and sublingual saliva but not in parotid saliva (at protein level). Expressed in saliva, tears, urine and seminal fluid. {ECO:0000269|PubMed:20189825}.; ovary;lacrimal gland;adrenal cortex;colon;parathyroid;skin;breast;pancreas;endometrium;adrenal gland;thyroid;bladder;pineal gland; salivary gland;thyroid;skeletal muscle; 0.35422 0.11185 0.41713504 76.95800896 12.91523 0.47072 CST2 2.1850092249434e-06 0.153826011918128 0.846171803072647 cystatin SA FUNCTION: Thiol protease inhibitor.; . TISSUE SPECIFICITY: Expressed in submandibular and sublingual saliva but not in parotid saliva (at protein level). Expressed in submandibular gland and parotid gland. {ECO:0000269|PubMed:11879580, ECO:0000269|PubMed:20189825}.; unclassifiable (Anatomical System);islets of Langerhans; salivary gland; 0.08059 0.09576 0.973768544 90.33970276 356.86993 4.00066 CST2P1 . . . cystatin SA pseudogene 1 . . . . . . . . . . . CST3 0.0690352137873098 0.737017144432151 0.193947641780539 cystatin C FUNCTION: As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.; DISEASE: Amyloidosis 6 (AMYL6) [MIM:105150]: A hereditary generalized amyloidosis due to cystatin C amyloid deposition. Cystatin C amyloid accumulates in the walls of arteries, arterioles, and sometimes capillaries and veins of the brain, and in various organs including lymphoid tissue, spleen, salivary glands, and seminal vesicles. Amyloid deposition in the cerebral vessels results in cerebral amyloid angiopathy, cerebral hemorrhage and premature stroke. Cystatin C levels in the cerebrospinal fluid are abnormally low. {ECO:0000269|PubMed:1352269, ECO:0000269|PubMed:2541223}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Macular degeneration, age-related, 11 (ARMD11) [MIM:611953]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. {ECO:0000269|PubMed:11815350}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in submandibular and sublingual saliva but not in parotid saliva (at protein level). Expressed in various body fluids, such as the cerebrospinal fluid and plasma. Expressed in highest levels in the epididymis, vas deferens, brain, thymus, and ovary and the lowest in the submandibular gland. {ECO:0000269|PubMed:15274116, ECO:0000269|PubMed:20189825}.; . . 0.16214 0.62540 0.125076652 62.7388535 922.6722 5.89843 CST4 7.30046884128097e-06 0.161904958817661 0.838087740713497 cystatin S FUNCTION: This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively.; . TISSUE SPECIFICITY: Expressed in submandibular and sublingual saliva but not in parotid saliva (at protein level). Expressed in saliva, tears, urine and seminal fluid. {ECO:0000269|PubMed:20189825}.; pancreas;ovary;lacrimal gland;adrenal gland;thyroid;adrenal cortex;parathyroid;pineal gland;skin;skeletal muscle; salivary gland;thyroid; 0.09154 0.10770 0.262810045 70.43524416 20.08609 0.68634 CST5 0.0216483919651051 0.756957914582355 0.22139369345254 cystatin D FUNCTION: Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B. {ECO:0000269|PubMed:8083219}.; . TISSUE SPECIFICITY: Expressed in submandibular and sublingual saliva but not in parotid saliva (at protein level). Expressed in parotid gland but not in seminal vesicle, prostate, epididymis, testis, ovary, placenta, thyroid, gastric corpus, small intestine, liver, or gall bladder tissue. {ECO:0000269|PubMed:20189825}.; adrenal gland;thyroid;adrenal cortex;parathyroid;pineal gland; salivary gland; 0.07072 0.08621 0.527368849 80.73248408 72.69905 1.77949 CST6 0.723124872712649 0.263598993796849 0.0132761334905012 cystatin E/M FUNCTION: Shows moderate inhibition of cathepsin B but is not active against cathepsin C.; . TISSUE SPECIFICITY: Restricted to the stratum granulosum of normal skin, the stratum granulosum/spinosum of psoriatic skin, and the secretory coils of eccrine sweat glands. Low expression levels are found in the nasal cavity. {ECO:0000269|PubMed:11348457}.; unclassifiable (Anatomical System);lymph node;heart;ovary;colon;parathyroid;skin;uterus;pancreas;prostate;lung;placenta;brain; superior cervical ganglion;skin; 0.12114 0.14668 . . 11.98181 0.43474 CST7 9.91887068524384e-07 0.0990890258246385 0.900909982288293 cystatin F FUNCTION: Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system.; . TISSUE SPECIFICITY: Primarily expressed in peripheral blood cells and spleen.; . . 0.09739 0.21451 -0.007201372 53.19061099 163.63628 2.79416 CST8 0.0856291456541582 0.760645928885524 0.153724925460318 cystatin 8 FUNCTION: Performs a specialized role during sperm development and maturation.; . TISSUE SPECIFICITY: Proximal caput region of the epididymis. Lower expression in the testis. Within the testis it is localized to the elongating spermatids, whereas within the epididymis it is exclusively synthesized by the proximal caput epithelium.; lung;testis; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;atrioventricular node;pons;skeletal muscle; 0.04640 0.27547 0.150760231 64.51403633 233.62434 3.30236 CST9 0.0951092949311725 0.769080072649381 0.135810632419446 cystatin 9 (testatin) FUNCTION: May be involved in testis development (By similarity). May play a role in hematopoietic differentiation or inflammation (PubMed:12535658). Has immunomodulatory and antimicrobial functions against Francisella tularensis, a Gram-negative bacteria (PubMed:23922243). {ECO:0000250|UniProtKB:Q9Z0H6, ECO:0000269|PubMed:12535658, ECO:0000269|PubMed:23922243}.; . TISSUE SPECIFICITY: Expressed in heart, placenta, lung, liver, skeletal muscle and pancreas (PubMed:12535658). Not expressed in brain (PubMed:12535658). Expressed in epididymis, kidney, testis, spinal cord, and thymus with a strong expression in epididymis and kidney and a weak expression in the spinal cord and thymus (PubMed:20565543). {ECO:0000269|PubMed:12535658, ECO:0000269|PubMed:20565543}.; . . 0.08285 0.10564 0.505321956 80.00707714 973.5092 6.03439 CST9L 2.08251924122082e-10 0.00501642499079361 0.994983574800954 cystatin 9-like . . TISSUE SPECIFICITY: Specifically espressed in testis. {ECO:0000269|PubMed:11756564, ECO:0000269|PubMed:20565543}.; . . 0.09257 . 0.926041233 89.65557915 205.64404 3.09732 CST9LP1 . . . cystatin 9-like pseudogene 1 . . . . . . . . . . . CST9LP2 . . . cystatin 9-like pseudogene 2 . . . . . . . . . . . CST11 0.00483331194609008 0.688738241978142 0.306428446075768 cystatin 11 FUNCTION: Has antibacterial activity against the Gram-negative bacteria E.coli. May play a role in sperm maturation and fertilization. {ECO:0000269|PubMed:12072414}.; . TISSUE SPECIFICITY: Detected in the epithelium and lumen of the epididymis, and in sperm (at protein level). {ECO:0000269|PubMed:12072414}.; . . 0.01727 0.06785 -0.073340031 48.11866006 21.01492 0.71164 CST12P . . . cystatin 12, pseudogene . . . . . . . . . . . CST13P . . . cystatin 13, pseudogene . . . . . . . . . . . CSTA 0.000533613519559043 0.457562561849709 0.541903824630732 cystatin A FUNCTION: This is an intracellular thiol proteinase inhibitor. Has an important role in desmosome-mediated cell-cell adhesion in the lower levels of the epidermis. {ECO:0000269|PubMed:21944047}.; . TISSUE SPECIFICITY: Expressed in the skin throughout the epidermis. {ECO:0000269|PubMed:21944047}.; unclassifiable (Anatomical System);cartilage;ovary;heart;tongue;oral cavity;skin;skeletal muscle;bone marrow;breast;uterus;prostate;lung;oesophagus;larynx;nasopharynx;placenta;visual apparatus;liver;hypopharynx;testis;cervix;head and neck;kidney;brain;aorta;tonsil; lung;tongue;whole blood;skin;tonsil; 0.14167 0.16133 0.325313577 73.11276244 757.56071 5.45469 CSTB 0.000132259411422296 0.232003297427223 0.767864443161355 cystatin B FUNCTION: This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B.; DISEASE: Epilepsy, progressive myoclonic 1 (EPM1) [MIM:254800]: An autosomal recessive disorder characterized by severe, stimulus- sensitive myoclonus and tonic-clonic seizures. The onset, occurring between 6 and 13 years of age, is characterized by convulsions. Myoclonus begins 1 to 5 years later. The twitchings occur predominantly in the proximal muscles of the extremities and are bilaterally symmetrical, although asynchronous. At first small, they become late in the clinical course so violent that the victim is thrown to the floor. Mental deterioration and eventually dementia develop. {ECO:0000269|PubMed:9012407}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;lymphoreticular;smooth muscle;ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;germinal center;brain;bladder;heart;cartilage;tongue;pineal body;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;synovium;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;oral cavity;muscle;bile duct;pancreas;lung;adrenal gland;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; lung;tongue;tonsil; 0.14565 0.50156 0.257356108 69.83368719 10.92385 0.39516 CSTF1 0.937895869936688 0.0620495795476409 5.45505156710376e-05 cleavage stimulation factor, 3' pre-RNA, subunit 1 FUNCTION: One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. May be responsible for the interaction of CSTF with other factors to form a stable complex on the pre-mRNA.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;skeletal muscle; 0.29284 0.11262 -0.714505427 14.4019816 8.49002 0.31205 CSTF2 0.305798340225873 0.693393950800779 0.000807708973348338 cleavage stimulation factor, 3' pre-RNA, subunit 2 FUNCTION: One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly involved in the binding to pre-mRNAs (By similarity). {ECO:0000250, ECO:0000269|PubMed:9199325}.; . . . . 0.27399 0.11566 0.237127192 68.98443029 18.45486 0.63901 CSTF2T 0.229519703844076 0.762875077956568 0.00760521819935679 cleavage stimulation factor, 3' pre-RNA, subunit 2, tau variant FUNCTION: May play a significant role in AAUAAA-independent mRNA polyadenylation in germ cells. Directly involved in the binding to pre-mRNAs (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;heart;ovary;islets of Langerhans;parathyroid;skin;retina;breast;uterus;pancreas;lung;frontal lobe;endometrium;nasopharynx;bone;placenta;iris;liver;testis;cervix;spleen;brain;bladder;stomach;cerebellum; atrioventricular node;caudate nucleus;parietal lobe; 0.11941 0.10144 -0.624497208 17.16206653 115.9957 2.34267 CSTF3 0.996434299674929 0.00356570024535706 7.97141905312119e-11 cleavage stimulation factor, 3' pre-RNA, subunit 3 FUNCTION: One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs.; . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.63072 0.16306 -0.626318434 17.03231894 8.84997 0.32567 CSTF3-AS1 . . . CSTF3 antisense RNA 1 (head to head) . . . . . . . . . . . CSTL1 0.000159597987763541 0.438992411200295 0.560847990811942 cystatin-like 1 . . . lung;testis; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.11755 0.08778 1.126294249 92.16206653 801.39965 5.57806 CSTP1 . . . cystatin pseudogene 1 . . . . . . . . . . . CSTP2 . . . cystatin pseudogene 2 . . . . . . . . . . . CT45A1 . . . cancer/testis antigen family 45, member A1 . . TISSUE SPECIFICITY: Testis specific. Expressed in cancer cell lines. {ECO:0000269|PubMed:15905330}.; . . . . . . 0.14568 0.00311 CT45A2 . . . cancer/testis antigen family 45, member A2 . . TISSUE SPECIFICITY: Testis specific. Expressed in cancer cell lines. {ECO:0000269|PubMed:15905330}.; . . . . . . . . CT45A3 . . . cancer/testis antigen family 45, member A3 . . TISSUE SPECIFICITY: Testis specific. Expressed in cancer cell lines. {ECO:0000269|PubMed:15905330}.; . . . . . . . . CT45A5 9.3941919310411e-06 0.100362014063019 0.899628591745049 cancer/testis antigen family 45, member A5 . . TISSUE SPECIFICITY: Testis specific. Expressed in cancer cell lines. {ECO:0000269|PubMed:15905330}.; . . . . . . 10.48463 0.38132 CT45A6 . . . cancer/testis antigen family 45, member A6 . . TISSUE SPECIFICITY: Testis specific. Expressed in cancer cell lines. {ECO:0000269|PubMed:15905330}.; . . . . . . 0.42793 0.00756 CT45A7 . . . cancer/testis antigen family 45, member A7 . . . . . . . . . . . CT45A8 . . . cancer/testis antigen family 45, member A8 . . . . . . . . . . . CT45A9 . . . cancer/testis antigen family 45, member A9 . . . . . . . . . . . CT45A10 . . . cancer/testis antigen family 45, member A10 . . . . . . . . . . . CT45A11P . . . cancer/testis antigen family 45, member A11, pseudogene . . . . . . . . . . . CT45B1P . . . cancer/testis antigen family 45, member B1 pseudogene . . . . . . . . . . . CT47A1 . . . cancer/testis antigen family 47, member A1 . . TISSUE SPECIFICITY: Strongly expressed in testis, low expression in placenta, and very low expression in brain. {ECO:0000269|PubMed:16382448}.; . . . . . . . . CT47A2 . . . cancer/testis antigen family 47, member A2 . . TISSUE SPECIFICITY: Strongly expressed in testis, low expression in placenta, and very low expression in brain. {ECO:0000269|PubMed:16382448}.; . . . . . . . . CT47A3 . . . cancer/testis antigen family 47, member A3 . . TISSUE SPECIFICITY: Strongly expressed in testis, low expression in placenta, and very low expression in brain. {ECO:0000269|PubMed:16382448}.; . . . . . . . . CT47A4 . . . cancer/testis antigen family 47, member A4 . . TISSUE SPECIFICITY: Strongly expressed in testis, low expression in placenta, and very low expression in brain. {ECO:0000269|PubMed:16382448}.; . . . . . . . . CT47A5 . . . cancer/testis antigen family 47, member A5 . . TISSUE SPECIFICITY: Strongly expressed in testis, low expression in placenta, and very low expression in brain. {ECO:0000269|PubMed:16382448}.; . . . . . . . . CT47A6 . . . cancer/testis antigen family 47, member A6 . . TISSUE SPECIFICITY: Strongly expressed in testis, low expression in placenta, and very low expression in brain. {ECO:0000269|PubMed:16382448}.; . . . . . . . . CT47A7 . . . cancer/testis antigen family 47, member A7 . . TISSUE SPECIFICITY: Strongly expressed in testis, low expression in placenta, and very low expression in brain. {ECO:0000269|PubMed:16382448}.; . . . . . . . . CT47A8 . . . cancer/testis antigen family 47, member A8 . . TISSUE SPECIFICITY: Strongly expressed in testis, low expression in placenta, and very low expression in brain. {ECO:0000269|PubMed:16382448}.; . . . . . . . . CT47A9 . . . cancer/testis antigen family 47, member A9 . . TISSUE SPECIFICITY: Strongly expressed in testis, low expression in placenta, and very low expression in brain. {ECO:0000269|PubMed:16382448}.; . . . . . . . . CT47A10 . . . cancer/testis antigen family 47, member A10 . . TISSUE SPECIFICITY: Strongly expressed in testis, low expression in placenta, and very low expression in brain. {ECO:0000269|PubMed:16382448}.; . . . . . . . . CT47A11 . . . cancer/testis antigen family 47, member A11 . . TISSUE SPECIFICITY: Strongly expressed in testis, low expression in placenta, and very low expression in brain. {ECO:0000269|PubMed:16382448}.; . . . . . . . . CT47A12 . . . cancer/testis antigen family 47, member A12 . . TISSUE SPECIFICITY: Strongly expressed in testis, low expression in placenta, and very low expression in brain. {ECO:0000269|PubMed:16382448}.; . . . . . . . . CT47B1 0.351018055014695 0.594093869721016 0.0548880752642888 cancer/testis antigen family 47, member B1 . . . . . . . . . 59.69085 1.56829 CT55 . . . cancer/testis antigen 55 . . . . . 0.03848 . . . 2.41349 0.08566 CT62 0.0331981608348203 0.612814519751355 0.353987319413825 cancer/testis antigen 62 . . TISSUE SPECIFICITY: Testis specific. Expressed in cancer cell lines. {ECO:0000269|PubMed:15905330}.; . . . . -0.009020804 52.8544468 5.01338 0.18648 CT83 . . . cancer/testis antigen 83 . . TISSUE SPECIFICITY: Specifically expressed in testis. Expressed by cancer cell lines. {ECO:0000269|PubMed:16651449}.; . . 0.05657 0.05394 -0.009020804 52.8544468 1.10426 0.02896 CTAA1 . . . cataract, anterior polar 1 . . . . . . . . . . . CTAA2 . . . cataract, anterior polar 2 . . . . . . . . . . . CTAG1A . . . cancer/testis antigen 1A . . TISSUE SPECIFICITY: Expressed in testis and ovary and in a wide variety of cancers. Detected in uterine myometrium. Expressed from 18 weeks until birth in human fetal testis. In the adult testis, is strongly expressed in spermatogonia and in primary spermatocytes, but not in post-meiotic cells or in testicular somatic cells (at protein level). {ECO:0000269|PubMed:12065688}.; lung;bone;placenta;testis; . 0.33776 0.07440 . . . . CTAG1B . . . cancer/testis antigen 1B . . TISSUE SPECIFICITY: Expressed in testis and ovary and in a wide variety of cancers. Detected in uterine myometrium. Expressed from 18 weeks until birth in human fetal testis. In the adult testis, is strongly expressed in spermatogonia and in primary spermatocytes, but not in post-meiotic cells or in testicular somatic cells (at protein level). {ECO:0000269|PubMed:12065688}.; lung;bone;placenta;testis; . 0.36952 0.06406 . . . . CTAG2 0.00595438745177886 0.494134005341501 0.49991160720672 cancer/testis antigen 2 . . TISSUE SPECIFICITY: Testis and very low level in placenta and in some uterus samples. Observed in 25-50% of tumor samples of melanomas, non-small-cell lung carcinomas, bladder, prostate and head and neck cancers.; optic nerve;endometrium;bone;placenta;macula lutea;testis;fovea centralis;choroid;lens;mammary gland;skin;stomach;retina; dorsal root ganglion;trigeminal ganglion; 0.13765 . 0.905808022 89.4373673 99.89657 2.16581 CTAGE1 2.09542255826793e-06 0.462533605002153 0.537464299575288 cutaneous T-cell lymphoma-associated antigen 1 . . TISSUE SPECIFICITY: Testis. Not found in tumor.; . . 0.00861 . -0.260839617 34.94928049 456.0088 4.43752 CTAGE3P . . . CTAGE family member 3, pseudogene FUNCTION: Tumor-associated antigen.; . . . . . . . . . . CTAGE4 . . . CTAGE family member 4 FUNCTION: Tumor-associated antigen.; . TISSUE SPECIFICITY: Expressed in testis, placenta and skin. Expressed at lower level in mammary gland and stomach. {ECO:0000269|PubMed:12839582}.; . . . . . . 39.04827 1.15726 CTAGE5 0.00187636795944541 0.99811536106285 8.27097770491871e-06 CTAGE family member 5 FUNCTION: Tumor-associated antigen.; . TISSUE SPECIFICITY: Isoform 5A is expressed only in testis (at the protein level). Other isoforms are expressed in several other normal tissues, including brain, muscle and cranial skin. Isoform 5A (at protein level) and isoform 5B are expressed in cutaneous T- cell lymphoma (CTCL) cell lines, colorectal carcinomas, breast carcinomas and melanoma. Isoform 5B, but not isoform 5A, is expressed in head and neck squamous cell carcinoma.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;pituitary gland;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;pia mater;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion; 0.71219 0.10916 1.692094639 96.42014626 0.76665 0.01379 CTAGE6 0.366836244776785 0.621526848679191 0.0116369065440235 CTAGE family member 6 . . . . . . . . . 126.17664 2.44439 CTAGE7P . . . CTAGE family member 7, pseudogene . . . . . . . . . . . CTAGE8 . . . CTAGE family member 8 . . . . . . . . . . . CTAGE9 . . . CTAGE family member 9 . . . . . . . . . 751.48662 5.43835 CTAGE10P . . . CTAGE family member 10, pseudogene . . . . . . . . . . . CTAGE11P . . . CTAGE family member 11, pseudogene . . . . . . . . . . . CTAGE12P . . . CTAGE family member 12, pseudogene . . . . . . . . . . . CTAGE13P . . . CTAGE family member 13, pseudogene . . . . . . . . . . . CTAGE14P . . . CTAGE family member 14, pseudogene . . . . . . . . . . . CTAGE15 0.784298473587336 0.208989492489686 0.00671203392297796 CTAGE family member 15 . . . . . . . . . 1705.37206 7.61766 CTAGE16P . . . CTAGE family member 16, pseudogene . . . . . . . . . . . CTBP1 0.979763654461024 0.0202198517191743 1.64938198014716e-05 C-terminal binding protein 1 FUNCTION: Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation. {ECO:0000269|PubMed:12419229, ECO:0000269|PubMed:15542832, ECO:0000269|PubMed:18212045, ECO:0000269|PubMed:19103759, ECO:0000269|PubMed:9858600}.; . TISSUE SPECIFICITY: Expressed in germinal center B-cells. {ECO:0000269|PubMed:18212045}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;cerebral cortex;endometrium;bone;iris;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;alveolus;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve;cerebellum; amygdala;whole brain;occipital lobe;prostate;cerebellum peduncles;liver;prefrontal cortex;globus pallidus;pons;parietal lobe;cerebellum; 0.99025 0.38699 -0.736552314 13.93606983 15.96379 0.56529 CTBP1-AS . . . CTBP1 antisense RNA . . . . . . . . . . . CTBP1-AS2 . . . CTBP1 antisense RNA 2 (head to head) . . . . . 0.12776 . . . . . CTBP2 0.655184958473335 0.344805061240602 9.98028606353552e-06 C-terminal binding protein 2 FUNCTION: Corepressor targeting diverse transcription regulators. Functions in brown adipose tissue (BAT) differentiation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. Highest levels in heart, skeletal muscle, and pancreas.; ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;cerebral cortex;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.48235 0.16121 0.371028035 74.95871668 17634.38171 27.99963 CTBP2P1 . . . C-terminal binding protein 2 pseudogene 1 . . . . . . . . . . . CTBP2P2 . . . C-terminal binding protein 2 pseudogene 2 . . . . . . . . . . . CTBP2P3 . . . C-terminal binding protein 2 pseudogene 3 . . . . . . . . . . . CTBP2P4 . . . C-terminal binding protein 2 pseudogene 4 . . . . . . . . . . . CTBP2P5 . . . C-terminal binding protein 2 pseudogene 5 . . . . . . . . . . . CTBP2P6 . . . C-terminal binding protein 2 pseudogene 6 . . . . . . . . . . . CTBP2P7 . . . C-terminal binding protein 2 pseudogene 7 . . . . . . . . . . . CTBP2P8 . . . C-terminal binding protein 2 pseudogene 8 . . . . . . . . . . . CTBS 2.00761188893893e-07 0.255656856772772 0.744342942466039 chitobiase FUNCTION: Involved in the degradation of asparagine-linked glycoproteins. Hydrolyze of N-acetyl-beta-D-glucosamine (1-4)N- acetylglucosamine chitobiose core from the reducing end of the bond, it requires prior cleavage by glycosylasparaginase.; . . . . 0.09078 0.34187 -0.047654689 50.22410946 5600.23192 15.47815 CTC1 3.51222906135356e-07 0.999973673895536 2.59748815583954e-05 CTS telomere maintenance complex component 1 FUNCTION: Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation (PubMed:19854130). However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha (PubMed:22763445). The CST complex facilitates recovery from many forms of exogenous DNA damage; seems to be involved in the re-initiation of DNA replication at repaired forks and/or dormant origins (PubMed:25483097). Involved in telomere maintenance (PubMed:19854131, PubMed:22863775). Involved in genome stability (PubMed:22863775). May be in involved in telomeric C-strand fill- in during late S/G2 phase (By similarity). {ECO:0000250|UniProtKB:Q5SUQ9, ECO:0000269|PubMed:19854130, ECO:0000269|PubMed:19854131, ECO:0000269|PubMed:22763445, ECO:0000269|PubMed:22863775, ECO:0000269|PubMed:25483097}.; DISEASE: Cerebroretinal microangiopathy with calcifications and cysts (CRMCC) [MIM:612199]: An autosomal recessive pleiomorphic disorder characterized primarily by intracranial calcifications, leukodystrophy, and brain cysts, resulting in spasticity, ataxia, dystonia, seizures, and cognitive decline. Patients also have retinal telangiectasia and exudates (Coats disease) as well as extraneurologic manifestations, including osteopenia with poor bone healing and a high risk of gastrointestinal bleeding and portal hypertension caused by vasculature ectasias in the stomach, small intestine, and liver. Some individuals also have hair, skin, and nail changes, as well as anemia and thrombocytopenia. {ECO:0000269|PubMed:22267198, ECO:0000269|PubMed:22387016}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;colon;blood;bone marrow;breast;uterus;whole body;lung;frontal lobe;bone;thyroid;placenta;alveolus;liver;testis;germinal center;kidney;brain;tonsil;thymus; globus pallidus;kidney; 0.12830 . -0.630196893 16.8141071 413.33201 4.25747 CTCF 0.997924957852537 0.00207502945561787 1.26918452271987e-08 CCCTC-binding factor FUNCTION: Chromatin binding factor that binds to DNA sequence specific sites. Involved in transcriptional regulation by binding to chromatin insulators and preventing interaction between promoter and nearby enhancers and silencers. Acts as transcriptional repressor binding to promoters of vertebrate MYC gene and BAG1 gene. Also binds to the PLK and PIM1 promoters. Acts as a transcriptional activator of APP. Regulates APOA1/C3/A4/A5 gene cluster and controls MHC class II gene expression. Plays an essential role in oocyte and preimplantation embryo development by activating or repressing transcription. Seems to act as tumor suppressor. Plays a critical role in the epigenetic regulation. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, binding within the H19 imprinting control region (ICR) mediates maternally inherited higher-order chromatin conformation to restrict enhancer access to IGF2. Plays a critical role in gene silencing over considerable distances in the genome. Preferentially interacts with unmethylated DNA, preventing spreading of CpG methylation and maintaining methylation-free zones. Inversely, binding to target sites is prevented by CpG methylation. Plays a important role in chromatin remodeling. Can dimerize when it is bound to different DNA sequences, mediating long-range chromatin looping. Mediates interchromosomal association between IGF2/H19 and WSB1/NF1 and may direct distant DNA segments to a common transcription factory. Causes local loss of histone acetylation and gain of histone methylation in the beta-globin locus, without affecting transcription. When bound to chromatin, it provides an anchor point for nucleosomes positioning. Seems to be essential for homologous X-chromosome pairing. May participate with Tsix in establishing a regulatable epigenetic switch for X chromosome inactivation. May play a role in preventing the propagation of stable methylation at the escape genes from X- inactivation. Involved in sister chromatid cohesion. Associates with both centromeres and chromosomal arms during metaphase and required for cohesin localization to CTCF sites. Regulates asynchronous replication of IGF2/H19. {ECO:0000269|PubMed:11743158, ECO:0000269|PubMed:16815976, ECO:0000269|PubMed:17827499, ECO:0000269|PubMed:18347100, ECO:0000269|PubMed:18413740, ECO:0000269|PubMed:18550811, ECO:0000269|PubMed:18654629, ECO:0000269|PubMed:19322193, ECO:0000269|PubMed:8649389, ECO:0000269|PubMed:9591631}.; DISEASE: Mental retardation, autosomal dominant 21 (MRD21) [MIM:615502]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Additional MRD21 features include short stature, microcephaly, and developmental delay. {ECO:0000269|PubMed:23746550}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Absent in primary spermatocytes. {ECO:0000269|PubMed:9591631}.; lymphoreticular;myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;cerebellum; subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;globus pallidus;cerebellum; 0.78428 0.25142 -0.293801652 32.93819297 9.66001 0.35497 CTCFL 0.78303184194046 0.216955804226004 1.23538335366956e-05 CCCTC-binding factor like FUNCTION: Testis-specific DNA binding protein responsible for insulator function, nuclear architecture and transcriptional control, which probably acts by recruiting epigenetic chromatin modifiers. Plays a key role in gene imprinting in male germline, by participating in the establishment of differential methylation at the IGF2/H19 imprinted control region (ICR). Directly binds the unmethylated H19 ICR and recruits the PRMT7 methyltransferase, leading to methylate histone H4 'Arg-3' to form H4R3sme2. This probably leads to recruit de novo DNA methyltransferases at these sites (By similarity). Seems to act as tumor suppressor. In association with DNMT1 and DNMT3B, involved in activation of BAG1 gene expression by binding to its promoter. Required for dimethylation of H3 lysine 4 (H3K4me2) of MYC and BRCA1 promoters. {ECO:0000250, ECO:0000269|PubMed:12011441, ECO:0000269|PubMed:18413740, ECO:0000269|PubMed:18765639}.; . TISSUE SPECIFICITY: Testis specific. Specifically expressed in primary spermatocytes.; unclassifiable (Anatomical System);lung;bone;visual apparatus;testis;kidney; dorsal root ganglion;uterus;medulla oblongata;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.11608 0.09123 1.181302384 92.80490682 316.39761 3.77775 CTD . . . Coats disease . . . . . . . . . . . CTDNEP1 0.972679931088588 0.0272854846720319 3.45842393802085e-05 CTD nuclear envelope phosphatase 1 FUNCTION: Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at differents levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling. {ECO:0000269|PubMed:17420445, ECO:0000269|PubMed:22134922}.; . TISSUE SPECIFICITY: Muscle specific with lower expression in other metabolic tissues. {ECO:0000269|PubMed:22134922}.; lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;hippocampus;hypopharynx;amnion;head and neck;kidney;stomach; superior cervical ganglion;medulla oblongata;occipital lobe;heart;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;thyroid;globus pallidus;whole blood;trigeminal ganglion;parietal lobe;cingulate cortex; 0.50417 0.11262 0.03689118 56.64071715 1069.36857 6.26871 CTDP1 0.924155318985366 0.0758439282896338 7.52725000208255e-07 CTD phosphatase subunit 1 FUNCTION: Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II. Plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation. {ECO:0000269|PubMed:22692537}.; DISEASE: Congenital cataracts, facial dysmorphism, and neuropathy (CCFDN) [MIM:604168]: An autosomal recessive developmental disorder characterized by a complex clinical phenotype with seemingly unrelated features involving multiple organs and systems. Developmental abnormalities include congenital cataracts and microcorneae, hypomyelination of the peripheral nervous system, impaired physical growth, delayed early motor and intellectual development, facial dysmorphism and hypogonadism. Central nervous system involvement, with cerebral and spinal cord atrophy, may be the result of disrupted development with superimposed degenerative changes. Affected individuals are prone to severe rhabdomyolysis after viral infections and to serious complications related to general anesthesia (such as pulmonary edema and epileptic seizures). {ECO:0000269|PubMed:14517542}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9765293}.; lymphoreticular;ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;cerebellum; testis; 0.11827 0.23034 -0.835882558 11.47676339 993.37938 6.07377 CTDSP1 0.902026975894043 0.097798274616956 0.000174749489000527 CTD small phosphatase 1 FUNCTION: Preferentially catalyzes the dephosphorylation of 'Ser- 5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells. {ECO:0000269|PubMed:12721286, ECO:0000269|PubMed:15681389}.; . TISSUE SPECIFICITY: Expression is restricted to non-neuronal tissues. Highest expression in skeletal muscle, spleen, lung and placenta. {ECO:0000269|PubMed:15681389}.; myocardium;ovary;skin;retina;prostate;optic nerve;cochlea;endometrium;iris;germinal center;brain;tonsil;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;duodenum;kidney;stomach;aorta;thymus;cerebellum; superior cervical ganglion;placenta;kidney;atrioventricular node;trigeminal ganglion; 0.34862 0.12861 0.060756528 58.52795471 156.37837 2.73332 CTDSP2 0.397665011331897 0.593088578637474 0.00924641003062897 CTD small phosphatase 2 FUNCTION: Preferentially catalyzes the dephosphorylation of 'Ser- 5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells. May contribute to the development of sarcomas. {ECO:0000269|PubMed:12721286, ECO:0000269|PubMed:15681389}.; . TISSUE SPECIFICITY: Expression is restricted to non-neuronal tissues. Highest expression in pancreas and lowest in liver. {ECO:0000269|PubMed:15681389}.; . . 0.49477 0.15355 -0.229483771 36.86010852 13.3864 0.48684 CTDSPL 0.0888481859287146 0.870209144795333 0.0409426692759526 CTD small phosphatase like FUNCTION: Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells (By similarity). Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. {ECO:0000250, ECO:0000269|PubMed:12721286}.; . TISSUE SPECIFICITY: Expression is restricted to non-neuronal tissues. {ECO:0000269|PubMed:15681389}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;iris;testis;amniotic fluid;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;olfactory bulb;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.23991 0.15150 -0.029247611 51.40363293 80.58588 1.89680 CTDSPL2 0.995978213604988 0.00402172260245261 6.37925598700562e-08 CTD small phosphatase like 2 FUNCTION: Probable phosphatase. {ECO:0000250}.; . . ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;optic nerve;whole body;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;heart;blood;lens;skeletal muscle;breast;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.20513 0.11371 -0.0274281 51.65723048 83.72355 1.94762 CTF1 0.138254693826932 0.625041630592784 0.236703675580284 cardiotrophin 1 FUNCTION: Induces cardiac myocyte hypertrophy in vitro. Binds to and activates the ILST/gp130 receptor.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, prostate and ovary. Lower levels in lung, kidney, pancreas, thymus, testis and small intestine. Little or no expression in brain, placenta, liver, spleen, colon or peripheral blood leukocytes.; choroid;fovea centralis;lens;skin;retina;optic nerve;lung;visual apparatus;macula lutea;testis;mammary gland;brain;stomach;peripheral nerve; superior cervical ganglion; 0.17532 0.36561 . . 5.42256 0.20110 CTF2P . . . cardiotrophin 2, pseudogene . . . . . 0.42282 0.35175 . . . . CTGF 0.124048405573342 0.851877992061306 0.0240736023653521 connective tissue growth factor FUNCTION: Major connective tissue mitoattractant secreted by vascular endothelial cells. Promotes proliferation and differentiation of chondrocytes. Mediates heparin- and divalent cation-dependent cell adhesion in many cell types including fibroblasts, myofibroblasts, endothelial and epithelial cells. Enhances fibroblast growth factor-induced DNA synthesis. {ECO:0000269|PubMed:10614647, ECO:0000269|PubMed:12553878}.; . TISSUE SPECIFICITY: Expressed in bone marrow and thymic cells. Also expressed one of two Wilms tumors tested. {ECO:0000269|PubMed:1756408}.; . . 0.72253 0.86146 -0.229483771 36.86010852 31.59133 0.99427 CTH 4.08793061635348e-05 0.955744395324771 0.0442147253690651 cystathionine gamma-lyase FUNCTION: Catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure. Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating their function. {ECO:0000269|PubMed:19019829, ECO:0000269|PubMed:19261609, ECO:0000269|PubMed:22169477}.; DISEASE: Cystathioninuria (CSTNU) [MIM:219500]: Autosomal recessive phenotype characterized by abnormal accumulation of plasma cystathionine, leading to increased urinary excretion. {ECO:0000269|PubMed:12574942}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);colon;blood;fovea centralis;choroid;lens;skeletal muscle;retina;pancreas;prostate;optic nerve;endometrium;bone;macula lutea;liver;spleen;kidney;brain;stomach; superior cervical ganglion;liver;adrenal cortex;ciliary ganglion;trigeminal ganglion; 0.24604 . 0.194852702 67.03231894 1258.99689 6.69110 CTHM . . . cono-truncal heart malformation . . . . . . . . . . . CTHRC1 0.00818066246056197 0.790479196630944 0.201340140908494 collagen triple helix repeat containing 1 FUNCTION: May act as a negative regulator of collagen matrix deposition. {ECO:0000250}.; DISEASE: Barrett esophagus (BE) [MIM:614266]: A condition characterized by a metaplastic change in which normal esophageal squamous epithelium is replaced by a columnar and intestinal-type epithelium. Patients with Barrett esophagus have an increased risk of esophageal adenocarcinoma. The main cause of Barrett esophagus is gastroesophageal reflux. The retrograde movement of acid and bile salts from the stomach into the esophagus causes prolonged injury to the esophageal epithelium and induces chronic esophagitis, which in turn is believed to trigger the pathologic changes. {ECO:0000269|PubMed:21791690}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is expressed in calcified atherosclerotic plaque and chondrocyte-like cells. {ECO:0000269|PubMed:15618538}.; ovary;colon;parathyroid;skin;uterus;optic nerve;whole body;oesophagus;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;blood;breast;pancreas;lung;epididymis;trabecular meshwork;placenta;liver;kidney;mammary gland;stomach;aorta; . 0.23980 0.14506 -0.139478553 43.29440906 51.02413 1.40752 CTHRC1P1 . . . collagen triple helix repeat containing 1 pseudogene 1 . . . . . . . . . . . CTIF 0.982754580423637 0.0172449632777082 4.56298655313399e-07 CBP80/20-dependent translation initiation factor FUNCTION: Specifically required for the pioneer round of mRNA translation mediated by the cap-binding complex (CBC), that takes place during or right after mRNA export via the nuclear pore complex (NPC). Acts via its interaction with the NCBP1/CBP80 component of the CBC complex and recruits the 40S small subunit of the ribosome via eIF3. In contrast, it is not involved in steady state translation, that takes place when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. Also required for nonsense-mediated mRNA decay (NMD), the pioneer round of mRNA translation mediated by the cap-binding complex playing a central role in nonsense-mediated mRNA decay (NMD). {ECO:0000269|PubMed:19648179}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19648179}.; ovary;sympathetic chain;colon;substantia nigra;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;lacrimal gland;pineal body;adrenal cortex;lens;breast;lung;epididymis;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland; temporal lobe;prefrontal cortex;cingulate cortex; 0.46165 . -1.107723888 6.829440906 478.62477 4.51721 CTLA4 0.57732241884153 0.411682426059044 0.0109951550994259 cytotoxic T-lymphocyte associated protein 4 FUNCTION: Inhibitory receptor acting as a major negative regulator of T-cell responses. The affinity of CTLA4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory coreceptor CD28. {ECO:0000269|PubMed:16551244, ECO:0000269|PubMed:1714933}.; DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:15138458, ECO:0000269|PubMed:15688186}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=Genetic variations in CTLA4 may influence susceptibility to Graves disease, an autoimmune disorder associated with overactivity of the thyroid gland and hyperthyroidism. {ECO:0000269|PubMed:10924276}.; DISEASE: Diabetes mellitus, insulin-dependent, 12 (IDDM12) [MIM:601388]: A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:9259273}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Celiac disease 3 (CELIAC3) [MIM:609755]: A multifactorial, chronic disorder of the small intestine caused by intolerance to gluten. It is characterized by immune-mediated enteropathy associated with failed intestinal absorption, and malnutrition. In predisposed individuals, the ingestion of gluten- containing food such as wheat and rye induces a flat jejunal mucosa with infiltration of lymphocytes. {ECO:0000269|PubMed:10189842, ECO:0000269|PubMed:15657618}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Autoimmune lymphoproliferative syndrome 5 (ALPS5) [MIM:616100]: An autosomal dominant primary immunodeficiency characterized by severe autoimmunity, infiltration of non-lymphoid organs, such as the intestine, lungs and brain, by hyperactive T cells and B cells, autoimmune cytopenias, and hypogammaglobulinemia in early childhood. {ECO:0000269|PubMed:25213377, ECO:0000269|PubMed:25329329}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed with highest levels in lymphoid tissues. Detected in activated T-cells where expression levels are 30- to 50-fold less than CD28, the stimulatory coreceptor, on the cell surface following activation. {ECO:0000269|PubMed:10493833, ECO:0000269|PubMed:16551244, ECO:0000269|PubMed:1713603}.; unclassifiable (Anatomical System);breast;prostate;lymph node;lung;blood;kidney;germinal center; superior cervical ganglion;pons; 0.59853 0.75237 -0.007201372 53.19061099 7.82864 0.28755 CTNNA1 0.970554290062812 0.0294456957694366 1.41677517993259e-08 catenin alpha 1 FUNCTION: Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.; DISEASE: Hereditary diffuse gastric cancer (HDGC) [MIM:137215]: A cancer predisposition syndrome with increased susceptibility to diffuse gastric cancer. Diffuse gastric cancer is a malignant disease characterized by poorly differentiated infiltrating lesions resulting in thickening of the stomach. Malignant tumors start in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. {ECO:0000269|PubMed:23208944}. Note=The gene represented in this entry may be involved in disease pathogenesis.; TISSUE SPECIFICITY: Expressed ubiquitously in normal tissues.; lymphoreticular;ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;cerebral cortex;endometrium;bone;thyroid;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;muscle;blood;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; . 0.45557 0.22076 -0.841329384 11.36470866 60.25736 1.57722 CTNNA1P1 . . . catenin alpha 1 pseudogene 1 . . . . . . . . . . . CTNNA2 0.999717952847311 0.00028204714867613 4.01281284339674e-12 catenin alpha 2 FUNCTION: May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation. {ECO:0000250|UniProtKB:Q61301}.; . . unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;sympathetic chain;fovea centralis;choroid;lens;skeletal muscle;retina;breast;optic nerve;lung;frontal lobe;cochlea;endometrium;macula lutea;hippocampus;testis;brain; amygdala;dorsal root ganglion;whole brain;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;testis - interstitial;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;parietal lobe;cingulate cortex; 0.39193 0.11262 -0.642904474 16.62538335 156.4549 2.73415 CTNNA3 6.54257200440676e-08 0.993034919093879 0.0069650154804004 catenin alpha 3 FUNCTION: May be involved in formation of stretch-resistant cell- cell adhesion complexes. {ECO:0000303|PubMed:11590244}.; . TISSUE SPECIFICITY: Predominantly expressed in heart and testis. Expressed at lower levels in brain, kidney, liver and skeletal muscle. {ECO:0000269|PubMed:11590244}.; unclassifiable (Anatomical System);frontal lobe;spinal cord;hippocampus;testis; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.15743 0.18566 -1.010461444 8.197688134 2922.26833 10.25564 CTNNAL1 2.30659700336349e-06 0.994926461159967 0.00507123224302993 catenin alpha-like 1 FUNCTION: May modulate the Rho pathway signaling by providing a scaffold for the Lbc Rho guanine nucleotide exchange factor (ARHGEF1).; . TISSUE SPECIFICITY: Widely expressed. Expressed at lower level in neural tissues and at the highest level in the adrenal gland. {ECO:0000269|PubMed:10542337, ECO:0000269|PubMed:12270917, ECO:0000269|PubMed:9806841}.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;urinary;blood;lens;bile duct;pia mater;lung;placenta;macula lutea;liver;amnion;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;olfactory bulb;adrenal cortex;testis;trigeminal ganglion; 0.22741 0.13914 -0.044015879 50.44821892 2618.16094 9.58886 CTNNB1 0.999812749503708 0.000187250460161459 3.61306746562573e-11 catenin beta 1 FUNCTION: Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22647378, PubMed:22699938, PubMed:22155184). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity). {ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:17524503, ECO:0000269|PubMed:18077326, ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:18957423, ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:22699938}.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:9065402}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Note=Activating mutations in CTNNB1 have oncogenic activity resulting in tumor development. Somatic mutations are found in various tumor types, including colon cancers, ovarian and prostate carcinomas, hepatoblastoma (HB), hepatocellular carcinoma (HCC). HBs are malignant embryonal tumors mainly affecting young children in the first three years of life.; DISEASE: Pilomatrixoma (PTR) [MIM:132600]: Common benign skin tumor. {ECO:0000269|PubMed:10192393, ECO:0000269|PubMed:11703283}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. {ECO:0000269|PubMed:10666372}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease. {ECO:0000269|PubMed:10391090}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving CTNNB1 is found in salivary gland pleiomorphic adenomas, the most common benign epithelial tumors of the salivary gland. Translocation t(3;8)(p21;q12) with PLAG1.; DISEASE: Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive neoplasm of the serosal lining of the chest. It appears as broad sheets of cells, with some regions containing spindle- shaped, sarcoma-like cells and other regions showing adenomatous patterns. Pleural mesotheliomas have been linked to exposure to asbestos. {ECO:0000269|PubMed:11464291}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Mental retardation, autosomal dominant 19 (MRD19) [MIM:615075]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD19 features include severe intellectual disability with absent or very limited speech, microcephaly, and spasticity which severely impaired the ability to walk. {ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:25326669}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in several hair follicle cell types: basal and peripheral matrix cells, and cells of the outer and inner root sheaths. Expressed in colon. Present in cortical neurons (at protein level). {ECO:0000269|PubMed:11703283, ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:17289029}.; smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;spinal cord;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;cerebellum; superior cervical ganglion; 0.99997 0.99630 -0.582225231 18.44184949 10.25364 0.37429 CTNNBIP1 0.0229867402741806 0.767158227506569 0.20985503221925 catenin beta interacting protein 1 FUNCTION: Prevents the interaction between CTNNB1 and TCF family members, and acts as negative regulator of the Wnt signaling pathway. {ECO:0000269|PubMed:12408824}.; . . . . 0.21923 . 0.369407109 74.95281906 36.28223 1.08653 CTNNBL1 0.28580047936403 0.71416036197981 3.91586561603572e-05 catenin beta like 1 FUNCTION: Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. Participates in AID/AICDA-mediated Ig class switching recombination (CSR). May induce apoptosis.; . TISSUE SPECIFICITY: Widely expressed with highest levels in skeletal muscle, placenta, heart, spleen, testis and thyroid. {ECO:0000269|PubMed:12659813}.; lymphoreticular;ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;alveolus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;thalamus;subthalamic nucleus;testis - seminiferous tubule;testis;ciliary ganglion; 0.20271 0.21520 -0.756778259 13.44656759 1617.71639 7.44042 CTNND1 0.995312685088934 0.00468731414286924 7.68196833390676e-10 catenin delta 1 FUNCTION: Binds to and inhibits the transcriptional repressor ZBTB33, which may lead to activation of target genes of the Wnt signaling pathway (By similarity). Associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability. Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors. Promotes GLIS2 C-terminal cleavage. {ECO:0000250, ECO:0000269|PubMed:17344476, ECO:0000269|PubMed:20371349}.; . TISSUE SPECIFICITY: Expressed in vascular endothelium. Melanocytes and melanoma cells primarily express the long isoform 1A, whereas keratinocytes express shorter isoforms, especially 3A. The shortest isoform 4A, is detected in normal keratinocytes and melanocytes, and generally lost from cells derived from squamous cell carcinomas or melanomas. The C-terminal alternatively spliced exon B is present in the p120ctn transcripts in the colon, intestine and prostate, but lost in several tumor tissues derived from these organs. {ECO:0000269|PubMed:11896187, ECO:0000269|PubMed:14699141}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.74895 0.27195 -0.727458245 14.19556499 654.2307 5.13246 CTNND2 0.999999951944472 4.80555284905704e-08 3.20174774359551e-19 catenin delta 2 FUNCTION: Has a critical role in neuronal development, particularly in the formation and/or maintenance of dendritic spines and synapses (PubMed:25807484). Involved in the regulation of Wnt signaling (PubMed:25807484). It probably acts on beta- catenin turnover, facilitating beta-catenin interaction with GSK3B, phosphorylation, ubiquitination and degradation (By similarity). Functions as a transcriptional activator when bound to ZBTB33 (By similarity). May be involved in neuronal cell adhesion and tissue morphogenesis and integrity by regulating adhesion molecules. {ECO:0000250|UniProtKB:O35927, ECO:0000269|PubMed:25807484, ECO:0000269|PubMed:9971746}.; DISEASE: Note=Defects in CTNND2, including deleterious missense and copy number variants (CNVs) are involved in autism, a complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation. {ECO:0000269|PubMed:25807484}.; TISSUE SPECIFICITY: Expressed in brain; highest expression is observed in fetal brain (PubMed:25807484). {ECO:0000269|PubMed:25807484}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;larynx;testis;corpus striatum;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;spinal cord;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;head and neck;kidney;mammary gland; whole brain;amygdala;superior cervical ganglion;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.40078 0.09362 -2.412493531 1.067468743 97.49242 2.13412 CTNS 0.0341220085738078 0.957517111073175 0.00836088035301731 cystinosin, lysosomal cystine transporter FUNCTION: Cystine/H(+) symporter thought to transport cystine out of lysosomes. Plays an important role in melanin synthesis, possibly by preventing melanosome acidification and subsequent degradation of tyrosinase TYR. {ECO:0000269|PubMed:22649030}.; DISEASE: Cystinosis, adult, non-nephropathic type (CTNSANN) [MIM:219750]: A form of cystinosis, a lysosomal storage disease due to defective transport of cystine across the lysosomal membrane. This results in cystine accumulation and crystallization in the cells causing widespread tissue damage. Cystinosis adult non-nephropathic type is characterized by ocular features and a benign course. Patients manifest mild photophobia due to conjunctival and corneal cystine crystals. {ECO:0000269|PubMed:10625078}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cystinosis, late-onset juvenile or adolescent nephropathic type (CTNSJAN) [MIM:219900]: A form of cystinosis, a lysosomal storage disease due to defective transport of cystine across the lysosomal membrane. This results in cystine accumulation and crystallization in the cells causing widespread tissue damage. Late-onset juvenile or adolescent nephropathic cystinosis is an intermediated form, manifesting first at age 10 to 12 years with proteinuria due to glomerular damage rather than with the manifestations of tubular damage that occur first in infantile cystinosis. There is no excess amino aciduria and stature is normal. Photophobia, late development of pigmentary retinopathy, and chronic headaches are features. {ECO:0000269|PubMed:10444339, ECO:0000269|PubMed:12442267, ECO:0000269|PubMed:9792862}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Strongly expressed in pancreas, kidney (adult and fetal), skeletal muscle, melanocytes and keratinocytes. Expressed at lower levels in placenta and heart. Weakly expressed in lung, liver and brain (adult and fetal). Isoform 2 represents 5-20 % of CTNS transcripts, with the exception of the testis that expresses both isoforms in equal proportions. {ECO:0000269|PubMed:22649030}.; colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;skeletal muscle;lung;epididymis;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney; testis; 0.07981 0.36267 -0.176292081 40.56381222 632.45857 5.06707 CTPL1 . . . cataract, pulverulent (autosomal recessive, early-onset) . . . . . . . . . . . CTPS1 0.932192403965688 0.0678070301297325 5.65904579896739e-07 CTP synthase 1 FUNCTION: This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP- dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocytes and therefore in immunity. {ECO:0000269|PubMed:16179339, ECO:0000269|PubMed:24870241}.; DISEASE: Immunodeficiency 24 (IMD24) [MIM:615897]: A life- threatening immunodeficiency, characterized by an impaired capacity of activated T and B cells to proliferate in response to antigen receptor-mediated activation. Patients have early onset of severe chronic viral infections, mostly caused by herpes viruses, including EBV and varicella zooster virus (VZV), and also suffer from recurrent encapsulated bacterial infections, a spectrum of infections typical of a combined deficiency of adaptive immunity. {ECO:0000269|PubMed:24870241}. Note=The disease is caused by mutations affecting the gene represented in this entry. A unique and recessive G to C mutation probably affecting a splice donor site at the junction of intron 17-18 and exon 18 has been identified in all patients. It results in expression of an abnormal transcript lacking exon 18 and a complete loss of the expression of the protein. {ECO:0000269|PubMed:24870241}.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:24870241}.; . . 0.61218 0.26203 -0.736552314 13.93606983 22.57002 0.75449 CTPS2 0.433684610695428 0.566017081736324 0.000298307568247967 CTP synthase 2 FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides. {ECO:0000269|PubMed:10899599, ECO:0000269|PubMed:16179339}.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;parathyroid;skeletal muscle;breast;uterus;prostate;whole body;lung;bone;placenta;liver;testis;germinal center;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.48895 0.16131 -0.183570861 39.95046001 15.25836 0.54863 CTR9 0.999999446978789 5.53021211014741e-07 5.03478197095217e-18 CTR9 homolog, Paf1/RNA polymerase II complex component FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non- phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Required for the trimethylation of histone H3 'Lys- 4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA- association of STAT3 (By similarity). {ECO:0000250, ECO:0000269|PubMed:16024656, ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:19345177, ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742, ECO:0000269|PubMed:20541477, ECO:0000269|PubMed:21329879}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8590280}.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;atrium;whole body;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;cervix;kidney;mammary gland;aorta;stomach; superior cervical ganglion; 0.40215 0.10956 -1.107723888 6.829440906 77.48955 1.85168 CTRB1 0.00179667178430693 0.477719743470844 0.520483584744849 chymotrypsinogen B1 . . . unclassifiable (Anatomical System);pancreas;islets of Langerhans;spleen; . 0.33826 0.15181 . . 129.00424 2.47530 CTRB2 0.283515252776286 0.630328734351039 0.0861560128726751 chymotrypsinogen B2 . . . unclassifiable (Anatomical System);prostate;pancreas;lung;islets of Langerhans;testis;spleen; superior cervical ganglion;pancreas;beta cell islets;trigeminal ganglion;skeletal muscle; 0.02971 0.33983 . . 23.4963 0.78152 CTRC 5.21992306515278e-06 0.423179099996247 0.576815680080688 chymotrypsin C FUNCTION: Regulates activation and degradation of trypsinogens and procarboxypeptidases by targeting specific cleavage sites within their zymogen precursors. Has chymotrypsin-type protease activity and hypocalcemic activity. {ECO:0000269|PubMed:23430245}.; . TISSUE SPECIFICITY: Pancreas.; . . 0.35475 . 0.016664174 55.21939137 145.59143 2.62957 CTRL 7.86917801865378e-06 0.505850838552985 0.494141292268996 chymotrypsin-like . . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney; pancreas;superior cervical ganglion;beta cell islets;ciliary ganglion;pons; 0.12913 0.09904 0.595326758 82.66100495 2011.05152 8.25496 CTSA 4.23467972299143e-05 0.990675696521465 0.00928195668130493 cathepsin A FUNCTION: Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins. {ECO:0000269|PubMed:1907282}.; DISEASE: Galactosialidosis (GSL) [MIM:256540]: A lysosomal storage disease associated with a combined deficiency of beta- galactosidase and neuraminidase, secondary to a defect in cathepsin A. All patients have clinical manifestations typical of a lysosomal disorder, such as coarse facies, cherry red spots, vertebral changes, foam cells in the bone marrow, and vacuolated lymphocytes. Three phenotypic subtypes are recognized. The early infantile form is associated with fetal hydrops, edema, ascites, visceromegaly, skeletal dysplasia, and early death. The late infantile type is characterized by hepatosplenomegaly, growth retardation, cardiac involvement, and a normal or mildly affected mental state. The juvenile/adult form is characterized by myoclonus, ataxia, angiokeratoma, mental retardation, neurologic deterioration, absence of visceromegaly, and long survival. {ECO:0000269|PubMed:10944848, ECO:0000269|PubMed:1756715, ECO:0000269|PubMed:8514852, ECO:0000269|PubMed:8968752}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;bladder;brain;heart;cartilage;pineal body;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;placenta;hippocampus;duodenum;head and neck;kidney;stomach; adrenal gland;placenta;kidney; 0.78932 0.78226 -0.867014353 10.72776598 324.39891 3.82839 CTSB . . . cathepsin B FUNCTION: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.; . . myocardium;ovary;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; thyroid;liver;kidney;fetal thyroid; 0.13833 0.66582 0.003714825 54.06935598 3000.05468 10.39686 CTSC 0.000816868198136731 0.931218435965212 0.0679646958366508 cathepsin C FUNCTION: Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII. {ECO:0000269|PubMed:1586157}.; DISEASE: Papillon-Lefevre syndrome (PLS) [MIM:245000]: An autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees. {ECO:0000269|PubMed:10581027, ECO:0000269|PubMed:10662808, ECO:0000269|PubMed:11106356, ECO:0000269|PubMed:11158173, ECO:0000269|PubMed:11180012, ECO:0000269|PubMed:11180601, ECO:0000269|PubMed:11886537, ECO:0000269|PubMed:12112662, ECO:0000269|PubMed:12809647, ECO:0000269|PubMed:14974080, ECO:0000269|PubMed:15108292, ECO:0000269|PubMed:15991336, ECO:0000269|PubMed:25799584}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Haim-Munk syndrome (HMS) [MIM:245010]: An autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis. {ECO:0000269|PubMed:10662807}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Periodontititis, aggressive, 1 (AP1) [MIM:170650]: A disease characterized by severe and protracted gingival infections, generalized or localized, leading to tooth loss. Amounts of microbial deposits are generally inconsistent with the severity of periodontal tissue destruction and the progression of attachment and bone loss may be self arresting. {ECO:0000269|PubMed:10662808, ECO:0000269|PubMed:14974080}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Highly expressed in lung, kidney and placenta. Detected at intermediate levels in colon, small intestine, spleen and pancreas. {ECO:0000269|PubMed:9092576}.; myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;oral cavity;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; lymph node;lung;trachea;placenta;white blood cells;kidney;whole blood; 0.25625 0.66481 -0.446304853 24.33356924 576.94188 4.87049 CTSD 0.0891858597432503 0.901826295744835 0.00898784451191446 cathepsin D FUNCTION: Acid protease active in intracellular protein breakdown. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease.; DISEASE: Ceroid lipofuscinosis, neuronal, 10 (CLN10) [MIM:610127]: A form of neuronal ceroid lipofuscinosis with onset at birth or early childhood. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. {ECO:0000269|PubMed:16670177, ECO:0000269|PubMed:16685649, ECO:0000269|PubMed:21990111}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the aorta extrcellular space (at protein level). {ECO:0000269|PubMed:20551380}.; lymphoreticular;ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;oesophagus;endometrium;larynx;bone;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; liver; 0.74127 0.90891 -0.578583623 18.71903751 117.3059 2.35488 CTSE 4.86866962963033e-07 0.395637711031465 0.604361802101572 cathepsin E FUNCTION: May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain. {ECO:0000269|PubMed:8765029}.; . TISSUE SPECIFICITY: Expressed abundantly in the stomach, the Clara cells of the lung and activated B-lymphocytes, and at lower levels in lymph nodes, skin and spleen. Not expressed in resting B- lymphocytes. {ECO:0000269|PubMed:11322887, ECO:0000269|PubMed:1370478, ECO:0000269|PubMed:8765029}.; unclassifiable (Anatomical System);pancreas;lung;islets of Langerhans;nasopharynx;liver;testis;colon;spleen;brain;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;appendix;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.28227 0.24183 0.845119304 88.4170795 444.14657 4.38296 CTSF 1.32810650436187e-13 0.0124315574888025 0.987568442511065 cathepsin F FUNCTION: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.; . TISSUE SPECIFICITY: High expression levels in heart, skeletal muscle, brain, testis and ovary; moderate levels in prostate, placenta, liver and colon; and no detectable expression in peripheral leukocytes and thymus.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;synovium;bone;testis;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;pineal body;adrenal cortex;blood;lens;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve;cerebellum; liver;testis; 0.13272 0.15247 0.486911049 79.46449634 161.35046 2.77519 CTSG 0.202072535708407 0.788044883159295 0.00988258113229783 cathepsin G FUNCTION: Serine protease with trypsin- and chymotrypsin-like specificity. Cleaves complement C3. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, antibacterial activity is inhibited by LPS from P.aeruginosa, Z-Gly-Leu-Phe- CH2Cl and phenylmethylsulfonyl fluoride. {ECO:0000269|PubMed:1861080, ECO:0000269|PubMed:1937776, ECO:0000269|PubMed:8194606}.; . . unclassifiable (Anatomical System);cartilage;heart;colon;blood;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;pancreas;prostate;optic nerve;lung;bone;macula lutea;liver;testis;spleen;kidney;brain; skeletal muscle;bone marrow; 0.03093 0.48544 0.549415813 81.38122199 149.68188 2.66757 CTSH 3.17314560149624e-06 0.783566315683755 0.216430511170643 cathepsin H FUNCTION: Important for the overall degradation of proteins in lysosomes.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;synovium;bone;thyroid;iris;testis;germinal center;brain;pineal gland;bladder;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;blood;lens;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; kidney; 0.14462 0.32365 0.15257911 64.60839821 2413.34224 9.12200 CTSK 0.000135210885342523 0.852945292034622 0.146919497080036 cathepsin K FUNCTION: Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.; . TISSUE SPECIFICITY: Predominantly expressed in osteoclasts (bones).; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;lens;breast;pancreas;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; dorsal root ganglion;uterus corpus;superior cervical ganglion;adipose tissue;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.31764 0.09950 -0.339715008 30.06605331 16.13745 0.57212 CTSL 0.00934180847585961 0.939391283818113 0.0512669077060269 cathepsin L FUNCTION: Important for the overall degradation of proteins in lysosomes.; . . . . 0.09920 0.76263 0.128714042 63.19886766 52.79042 1.43957 CTSL3P . . . cathepsin L family member 3, pseudogene . . . . . 0.10968 . . . . . CTSLP1 . . . cathepsin L pseudogene 1 . . . . . . . . . . . CTSLP2 . . . cathepsin L pseudogene 2 . . . . . . . . . . . CTSLP3 . . . cathepsin L pseudogene 3 . . . . . . . . . . . CTSLP4 . . . cathepsin L pseudogene 4 . . . . . . . . . . . CTSLP6 . . . cathepsin L pseudogene 6 . . . . . . . . . . . CTSLP8 . . . cathepsin L pseudogene 8 . . . . . . . . . . . CTSO 6.3496157062382e-06 0.461695517232904 0.538298133151389 cathepsin O FUNCTION: Proteolytic enzyme possibly involved in normal cellular protein degradation and turnover.; . TISSUE SPECIFICITY: Expressed in all tissues examined. High levels seen in the ovary, kidney and placenta while low levels seen in thymus and skeletal muscle.; . . 0.20038 0.12625 -0.005381972 53.50908233 87.98184 2.00573 CTSS 0.628282928532702 0.370195899509527 0.00152117195777153 cathepsin S FUNCTION: Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.; . . . . 0.58124 0.31208 0.215080721 67.91696155 3807.31695 12.12868 CTSV 9.73428954621341e-06 0.551200939234822 0.448789326475632 cathepsin V FUNCTION: Cysteine protease. May have an important role in corneal physiology. {ECO:0000269|PubMed:10029531, ECO:0000269|PubMed:9727401}.; . TISSUE SPECIFICITY: Predominantly expressed in the thymus and testis. Also expressed in corneal epithelium, and to a lesser extent in conjunctival epithelium and skin. {ECO:0000269|PubMed:10029531, ECO:0000269|PubMed:9563472, ECO:0000269|PubMed:9727401}.; . . 0.60412 0.13303 -0.358119787 29.16371786 83.07322 1.93720 CTSW 2.6259020966295e-07 0.492962188256938 0.507037549152853 cathepsin W FUNCTION: May have a specific function in the mechanism or regulation of T-cell cytolytic activity.; . . unclassifiable (Anatomical System);lymphoreticular;cartilage;ovary;colon;blood;fovea centralis;choroid;lens;retina;bone marrow;uterus;pancreas;optic nerve;lung;placenta;macula lutea;spleen;mammary gland;aorta;stomach; whole blood; 0.09853 0.16164 -0.754958418 13.57631517 59.48069 1.56446 CTSZ 1.31534221236972e-09 0.0283707030112586 0.971629295673399 cathepsin Z FUNCTION: Exhibits carboxy-monopeptidase as well as carboxy- dipeptidase activity.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10653163}.; myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.09275 0.14911 0.617373774 83.25076669 114.37882 2.32974 CTTN 0.215776882831596 0.784208218240095 1.489892830946e-05 cortactin FUNCTION: Contributes to the organization of the actin cytoskeleton and cell shape (PubMed:21296879). Plays a role in the formation of lamellipodia and in cell migration. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density (By similarity). Plays a role in the invasiveness of cancer cells, and the formation of metastases (PubMed:16636290). Plays a role in focal adhesion assembly and turnover (By similarity). In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement (PubMed:20861316). Plays a role in intracellular protein transport and endocytosis, and in modulating the levels of potassium channels present at the cell membrane (PubMed:17959782). Plays a role in receptor-mediated endocytosis via clathrin-coated pits (By similarity). Required for stabilization of KCNH1 channels at the cell membrane (PubMed:23144454). {ECO:0000250|UniProtKB:Q60598, ECO:0000250|UniProtKB:Q66HL2, ECO:0000269|PubMed:16636290, ECO:0000269|PubMed:17959782, ECO:0000269|PubMed:21296879, ECO:0000269|PubMed:23144454}.; . . medulla oblongata;smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;bladder;brain;heart;cartilage;tongue;nervous;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;aorta;stomach;cerebellum; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;occipital lobe;adrenal gland;adrenal cortex;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle;skin;parietal lobe; 0.25103 0.58596 -0.50880549 21.72682236 69.84309 1.73391 CTTNBP2 2.59915879681031e-06 0.99999015004884 7.25079236279233e-06 cortactin binding protein 2 FUNCTION: Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, thus controls dendritic spinogenesis and dendritic spine maintenance. {ECO:0000250}.; . TISSUE SPECIFICITY: Highest expression in brain. Also expressed in kidney, pancreas, lung, heart, liver, skeletal muscle and placenta. {ECO:0000269|PubMed:11707066}.; unclassifiable (Anatomical System);ovary;blood;fovea centralis;skeletal muscle;bone marrow;uterus;whole body;lung;endometrium;larynx;trabecular meshwork;placenta;thyroid;macula lutea;testis;head and neck;brain;cerebellum; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.15550 0.12377 -1.449682288 3.904222694 436.81472 4.35745 CTTNBP2NL 0.141381251992425 0.854550661852401 0.00406808615517483 CTTNBP2 N-terminal like . . . ovary;colon;parathyroid;skin;uterus;prostate;whole body;cochlea;cerebral cortex;endometrium;larynx;thyroid;bone;amniotic fluid;brain;gall bladder;unclassifiable (Anatomical System);heart;cartilage;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney; . 0.23525 0.10978 -0.067881249 48.69072895 134.44599 2.52148 CTU1 0.134628145231563 0.622186637972419 0.243185216796018 cytosolic thiouridylase subunit 1 FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. {ECO:0000255|HAMAP-Rule:MF_03053, ECO:0000269|PubMed:19017811}.; . . . . 0.30926 0.11955 . . 1843.58117 7.91912 CTU2 3.21676727020384e-14 0.0199487733303448 0.980051226669623 cytosolic thiouridylase subunit 2 homolog (S. pombe) FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with CTU1/ATPBD3 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. {ECO:0000255|HAMAP-Rule:MF_03054, ECO:0000269|PubMed:19017811}.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;aorta;stomach;thymus; . 0.28000 . 1.431149089 95.02241095 6708.14108 17.35022 CTXN1 0.10505738095457 0.589944102707221 0.304998516338209 cortexin 1 FUNCTION: May mediate extracellular or intracellular signaling of cortical neurons during forebrain development. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;hypothalamus;parathyroid;skin;uterus;prostate;optic nerve;lung;frontal lobe;endometrium;bone;placenta;hippocampus;duodenum;pituitary gland;testis;kidney;brain; . 0.20737 0.11262 . . 9.33612 0.34318 CTXN2 . . . cortexin 2 . . . . . . . 0.3455435 73.78509082 47.12353 1.32871 CTXN3 0.544481267710668 0.400311023370091 0.0552077089192404 cortexin 3 . . . . . 0.61271 0.09746 0.435547893 77.45340882 1276.98678 6.72858 CUBN 3.03432572949695e-28 0.9999999775831 2.24169003645547e-08 cubilin FUNCTION: Cotransporter which plays a role in lipoprotein, vitamin and iron metabolism, by facilitating their uptake. Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the GIF-cobalamin complex. The binding of all ligands requires calcium. Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. Interaction with LRP2 mediates its trafficking throughout vesicles and facilitates the uptake of specific ligands like GC, hemoglobin, ALB, TF and SCGB1A1. Interaction with AMN controls its trafficking to the plasma membrane and facilitates endocytosis of ligands. May play an important role in the development of the peri-implantation embryo through internalization of APOA1 and cholesterol. Binds to LGALS3 at the maternal-fetal interface. {ECO:0000269|PubMed:10371504, ECO:0000269|PubMed:11606717, ECO:0000269|PubMed:11717447, ECO:0000269|PubMed:14576052, ECO:0000269|PubMed:9572993}.; DISEASE: Recessive hereditary megaloblastic anemia 1 (RH-MGA1) [MIM:261100]: Due to selective malabsorption of vitamin B12. Defects in vitamin B12 absorption lead to impaired function of thymidine synthase. As a consequence DNA synthesis is interrupted. Rapidly dividing cells involved in erythropoiesis are particularly affected. {ECO:0000269|PubMed:10080186, ECO:0000269|PubMed:10887099}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in kidney proximal tubule cells, placenta, visceral yolk-sac cells and in absorptive intestinal cells. Expressed in the epithelium of intestine and kidney.; . . 0.16009 0.31630 1.257700362 93.49492805 6532.49526 17.00260 CUBNP1 . . . cubilin (intrinsic factor-cobalamin receptor) pseudogene 1 . . . . . . . . . . . CUBNP2 . . . cubilin (intrinsic factor-cobalamin receptor) pseudogene 2 . . . . . . . . . . . CUBNP3 . . . cubilin (intrinsic factor-cobalamin receptor) pseudogene 3 . . . . . . . . . . . CUEDC1 6.38268720532172e-05 0.900299117513333 0.0996370556146143 CUE domain containing 1 . . . ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;oesophagus;thyroid;bone;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;stomach; atrioventricular node; 0.22102 0.10429 -0.268115223 34.70747818 910.1822 5.86574 CUEDC2 0.0719074383771385 0.91539457608765 0.0126979855352112 CUE domain containing 2 FUNCTION: Down-regulates ESR1 protein levels through the ubiquitination-proteasome pathway, regardless of the presence of 17 beta-estradiol. Also involved in 17 beta-estradiol-induced ESR1 degradation. Controls PGR protein levels through a similar mechanism. {ECO:0000269|PubMed:17347654, ECO:0000269|PubMed:21572428}.; DISEASE: Note=May predict the clinical outcome of tamoxifen therapy of breast cancer patients. Patients with tumors that highly express CUEDC2 do not respond to tamoxifen treatment as effectively as those with tumors with low expression.; TISSUE SPECIFICITY: Significantly up-regulated in breast tumor tissues compared with matched adjacent normal tissues (at protein level). Levels inversely correlate with ESR1 in breast cancers and are lower in low-grade tumors compared to high-grade tumors.; . . 0.26018 0.10816 0.25917371 70.05779665 25.18962 0.82373 CUL1 0.999963289879359 3.67101206133191e-05 2.79435753426692e-14 cullin 1 FUNCTION: Core component of multiple cullin-RING-based SCF (SKP1- CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and exchange of the substrate recognition component is mediated by TIP120A/CAND1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(BTRC) and/or SCF(FBXW11) direct ubiquitination of CEP68 (PubMed:25704143, PubMed:25503564). SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO1) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) directs ubiquitination of TTI1 and TELO2. SCF(FBXO10) directs ubiquitination of BCL2. {ECO:0000269|PubMed:15531760, ECO:0000269|PubMed:15640526, ECO:0000269|PubMed:18644861, ECO:0000269|PubMed:19679664, ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:23263282, ECO:0000269|PubMed:23431138, ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:25704143, ECO:0000269|PubMed:9663463}.; . TISSUE SPECIFICITY: Expressed in lung fibroblasts. {ECO:0000269|PubMed:9663463}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;pons;parietal lobe; 0.43821 0.25583 -0.516085732 21.20193442 6.05181 0.22910 CUL1P1 . . . cullin 1 pseudogene 1 . . . . . . . . . . . CUL2 0.999998410397597 1.58960240183497e-06 1.60968180805768e-15 cullin 2 FUNCTION: Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. May serve as a rigid scaffold in the complex and may contribute to catalysis through positioning of the substrate and the ubiquitin- conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The functional specificity of the ECS complex depends on the substrate recognition component. ECS(VHL) mediates the ubiquitination of hypoxia-inducible factor (HIF). {ECO:0000250}.; . . . . 0.72401 0.19444 -0.580403979 18.58928993 30.29769 0.96644 CUL3 0.974063405438851 0.0259365434257954 5.11353534095903e-08 cullin 3 FUNCTION: Core component of multiple cullin-RING-based BCR (BTB- CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The functional specificity of the BCR complex depends on the BTB domain-containing protein as the substrate recognition component. BCR(KLHL42) is involved in ubiquitination of KATNA1. BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4, BRMS1, H2AFY and DAXX, GLI2 and GLI3. Can also form a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL; these complexes have lower ubiquitin ligase activity. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. BCR(KLHL12) is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B). BCR(KLHL3) acts as a regulator of ion transport in the distal nephron; by mediating ubiquitination of WNK4. The BCR(KLHL20) E3 ubiquitin ligase complex is involved in interferon response and anterograde Golgi to endosome transport: it mediates both ubiquitination leading to degradation and 'Lys-33'-linked ubiquitination (PubMed:20389280, PubMed:21840486, PubMed:21670212, PubMed:24768539). The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of AURKB. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. The BCR(KLHL25) ubiquitin ligase complex is involved in translational homeostasis by mediating ubiquitination and subsequent degradation of hypophosphorylated EIF4EBP1 (4E-BP1). Involved in ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in regulation of G1/S transition. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. In concert with ATF2 and RBX1, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. The BCR(KCTD17) E3 ubiquitin ligase complex mediates ubiquitination and degradation of TCHP, a down-regulator of cilium assembly, thereby inducing ciliogenesis (PubMed:25270598). {ECO:0000250, ECO:0000269|PubMed:10500095, ECO:0000269|PubMed:11311237, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:15983046, ECO:0000269|PubMed:16524876, ECO:0000269|PubMed:17543862, ECO:0000269|PubMed:18397884, ECO:0000269|PubMed:19261606, ECO:0000269|PubMed:19995937, ECO:0000269|PubMed:20389280, ECO:0000269|PubMed:21670212, ECO:0000269|PubMed:21840486, ECO:0000269|PubMed:22085717, ECO:0000269|PubMed:22358839, ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:22632832, ECO:0000269|PubMed:23387299, ECO:0000269|PubMed:23453970, ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:23576762, ECO:0000269|PubMed:24768539, ECO:0000269|PubMed:25270598}.; DISEASE: Pseudohypoaldosteronism 2E (PHA2E) [MIM:614496]: An autosomal dominant disorder characterized by severe hypertension, hyperkalemia, hyperchloremia, hyperchloremic metabolic acidosis, and correction of physiologic abnormalities by thiazide diuretics. {ECO:0000269|PubMed:22266938}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed.; medulla oblongata;ovary;adrenal medulla;skin;retina;bone marrow;prostate;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.25175 0.18619 -0.139478553 43.29440906 1361.02638 6.92534 CUL4A 0.99941287660114 0.000587122814012862 5.84846851863383e-10 cullin 4A FUNCTION: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. DCX(DET1-COP1) directs ubiquitination of JUN. DCX(DDB2) directs ubiquitination of XPC. DCX(DDB2) ubiquitinates histones H3-H4 and is required for efficient histone deposition during replication-coupled (H3.1) and replication-independent (H3.3) nucleosome assembly, probably by facilitating the transfer of H3 from ASF1A/ASF1B to other chaperones involved in histone deposition. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. In association with DDB1 and SKP2 probably is involved in ubiquitination of CDKN1B/p27kip. Is involved in ubiquitination of HOXA9. DCX(DTL) directs autoubiquitination of DTL. {ECO:0000269|PubMed:14578910, ECO:0000269|PubMed:14609952, ECO:0000269|PubMed:15448697, ECO:0000269|PubMed:15548678, ECO:0000269|PubMed:16537899, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:23478445, ECO:0000269|PubMed:24209620}.; . . myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;placenta;duodenum;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;skeletal muscle;skin; 0.61067 0.26405 -0.422438699 25.64284029 1807.63636 7.84549 CUL4AP1 . . . cullin 4A pseudogene 1 . . . . . . . . . . . CUL4B 0.99984667801374 0.000153321876539413 1.09720540223026e-10 cullin 4B FUNCTION: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation- induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8. {ECO:0000269|PubMed:14578910, ECO:0000269|PubMed:16322693, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:18235224, ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:19801544, ECO:0000269|PubMed:22118460}.; DISEASE: Mental retardation, X-linked, syndromic, 15 (MRXS15) [MIM:300354]: A syndromic form of X-linked mental retardation characterized by severe intellectual deficit associated with short stature, craniofacial dysmorphism, small testes, muscle wasting in lower legs, kyphosis, joint hyperextensibility, pes cavus, small feet, and abnormalities of the toes. Additional neurologic manifestations include speech delay and impairment, tremor, seizures, gait ataxia, hyperactivity and decreased attention span. {ECO:0000269|PubMed:17236139, ECO:0000269|PubMed:17273978, ECO:0000269|PubMed:19377476, ECO:0000269|PubMed:20002452}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pineal body;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach;aorta;cerebellum;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;occipital lobe;hypothalamus;atrioventricular node;skeletal muscle;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;pituitary; 0.87445 0.12121 -0.361761279 28.6329323 9.19638 0.33598 CUL5 0.999964792113235 3.52078866405048e-05 1.24735343748836e-13 cullin 5 FUNCTION: Core component of multiple SCF-like ECS (Elongin-Cullin 2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin- conjugating enzyme. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. ECS(SOCS1) seems to direct ubiquitination of JAK2. Seems to be involved in proteosomal degradation of p53/TP53 stimulated by adenovirus E1B-55 kDa protein. May form a cell surface vasopressin receptor.; . . . . 0.24900 0.25991 -0.736552314 13.93606983 12.1932 0.44162 CUL7 2.23525658801241e-11 0.999922672318077 7.73276595703883e-05 cullin 7 FUNCTION: Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediates the ubiquitination of target proteins. Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695). Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5 (PubMed:24793696). Core component of a Cul7-RING ubiquitin-protein ligase with FBXW8, which mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1 (PubMed:21572988, PubMed:24362026). Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite patterning in brain (PubMed:21572988). Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2) (PubMed:18498745). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradatation, thereby affecting cell proliferation and differentiation (PubMed:24362026). Acts as a regulator in trophoblast cell epithelial-mesenchymal transition and placental development (PubMed:20139075). Does not promote polyubiquitination and proteasomal degradation of p53/TP53 (PubMed:16547496, PubMed:17332328). While the Cul7-RING(FBXW8) and the 3M complexes are associated and involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have additional functions. {ECO:0000269|PubMed:16547496, ECO:0000269|PubMed:17332328, ECO:0000269|PubMed:18498745, ECO:0000269|PubMed:20139075, ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24362026, ECO:0000269|PubMed:24793695, ECO:0000269|PubMed:24793696}.; DISEASE: 3M syndrome 1 (3M1) [MIM:273750]: An autosomal recessive disorder characterized by severe pre- and postnatal growth retardation, facial dysmorphism, large head circumference, and normal intelligence and endocrine function. Skeletal changes include long slender tubular bones and tall vertebral bodies. {ECO:0000269|PubMed:16142236, ECO:0000269|PubMed:17675530, ECO:0000269|PubMed:23018678}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in fetal kidney and adult skeletal muscle. Also abundant in fetal brain, as well as in adult pancreas, kidney, placenta and heart. Detected in trophoblasts, lymphoblasts, osteoblasts, chondrocytes and skin fibroblasts. {ECO:0000269|PubMed:16142236}.; ovary;salivary gland;intestine;colon;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;synovium;larynx;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;pancreas;lung;cornea;placenta;visual apparatus;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16639 0.12284 -1.527152158 3.391129983 739.111 5.39737 CUL9 0.967475855018408 0.0325241449815916 8.54214021184151e-17 cullin 9 FUNCTION: Core component of a Cul9-RING ubiquitin-protein ligase complex, a complex that mediates ubiquitination and subsequent degradation of BIRC5 and is required to maintain microtubule dynamics and genome integrity. Acts downstream of the 3M complex, which inhibits CUL9 activity, leading to prevent ubiquitination of BIRC5 (PubMed:24793696). Cytoplasmic anchor protein in p53/TP53- associated protein complex. Regulates the subcellular localization of p53/TP53 and subsequent function (PubMed:12526791, PubMed:17332328). {ECO:0000269|PubMed:12526791, ECO:0000269|PubMed:17332328, ECO:0000269|PubMed:24793696}.; . TISSUE SPECIFICITY: Ubiquitously expressed in all tissues with highest expression in testis brain and kidney. {ECO:0000269|PubMed:12526791}.; ovary;colon;parathyroid;fovea centralis;skin;uterus;whole body;frontal lobe;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;hippocampus;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; whole brain;testis - interstitial;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;atrioventricular node;cingulate cortex; . 0.10680 -2.207565276 1.356451993 3074.2659 10.53781 CUTA 1.14218167340545e-05 0.362927375746124 0.637061202437142 cutA divalent cation tolerance homolog (E. coli) FUNCTION: May form part of a complex of membrane proteins attached to acetylcholinesterase (AChE).; . TISSUE SPECIFICITY: Ubiquitous. Widely expressed in brain. {ECO:0000269|PubMed:10800960}.; . . 0.18030 0.23489 1.126294249 92.16206653 791.44458 5.54848 CUTC 0.0204865647949904 0.961924474948043 0.017588960256967 cutC copper transporter FUNCTION: May play a role in copper homeostasis. Can bind one Cu(1+) per subunit. {ECO:0000269|PubMed:16182249, ECO:0000269|PubMed:19878721}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16182249}.; . . 0.13600 0.17348 -0.295622497 32.61972163 14.93524 0.53781 CUX1 0.999988877535193 1.11224648068841e-05 3.0844204082211e-16 cut like homeobox 1 FUNCTION: Probably has a broad role in mammalian development as a repressor of developmentally regulated gene expression. May act by preventing binding of positively-activing CCAAT factors to promoters. Component of nf-munr repressor; binds to the matrix attachment regions (MARs) (5' and 3') of the immunoglobulin heavy chain enhancer. Represses T-cell receptor (TCR) beta enhancer function by binding to MARbeta, an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Binds to the TH enhancer; may require the basic helix-loop-helix protein TCF4 as a coactivator (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;blood;lens;breast;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;stomach;peripheral nerve; uterus;dorsal root ganglion;superior cervical ganglion;prostate;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.78386 0.44868 -1.868734056 2.011087521 217.29988 3.18613 CUX2 0.999656384592776 0.000343615405910678 1.31356985250931e-12 cut like homeobox 2 FUNCTION: May be a transcription factor involved in neural specification. Binds to DNA in a sequence-specific manner (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);tongue;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;frontal lobe;cochlea;thyroid;macula lutea;visual apparatus;testis;head and neck;brain; whole brain;occipital lobe;medulla oblongata;subthalamic nucleus;superior cervical ganglion;fetal brain;temporal lobe;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.24651 0.11776 -2.076219205 1.598254305 435.46645 4.35260 CUX2P1 . . . cut like homeobox 2 pseudogene 1 . . . . . . . . . . . CUX2P2 . . . cut like homeobox 2 pseudogene 2 . . . . . . . . . . . CUZD1 5.27752199889402e-06 0.866712107644893 0.133282614833108 CUB and zona pellucida like domains 1 FUNCTION: CUZD1 antiserum inhibits cell attachment and proliferation of ovarian cancer cells so may be involved in these processes. May also play a role in the uterus during late pregnancy and/or in trypsin activation in pancreatic acinar cells. {ECO:0000250|UniProtKB:P70412, ECO:0000269|PubMed:15184879}.; . TISSUE SPECIFICITY: Detected in pancreas and epithelium of ovary. Expressed at higher levels in ovarian tumors than in normal tissue. {ECO:0000269|PubMed:15184879}.; unclassifiable (Anatomical System);uterus;pancreas;heart;islets of Langerhans;liver;choroid;germinal center;skin; dorsal root ganglion;subthalamic nucleus;pancreas;beta cell islets;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.08502 0.10468 0.646696306 84.12361406 242.70214 3.36311 CWC15 0.9002772115237 0.0988342376205962 0.000888550855703797 CWC15 spliceosome-associated protein FUNCTION: Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. {ECO:0000269|PubMed:20176811}.; . . ovary;developmental;colon;parathyroid;fovea centralis;skin;retina;bone marrow;endometrium;thyroid;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;macula lutea;liver;spleen;cervix;kidney;stomach; amygdala;whole brain;testis - seminiferous tubule;prefrontal cortex;testis;cingulate cortex; 0.30439 0.11262 . . 2.88829 0.10314 CWC22 0.0181890738297984 0.981803487274102 7.43889609955366e-06 CWC22 homolog, spliceosome-associated protein FUNCTION: Required for pre-mRNA splicing and for exon-junction complex (EJC) assembly. Hinders EIF4A3 from non-specifically binding RNA and escorts it to the splicing machinery to promote EJC assembly on mature mRNAs. Through its role in EJC assembly, required for nonsense-mediated mRNA decay. {ECO:0000269|PubMed:22959432, ECO:0000269|PubMed:22961380, ECO:0000269|PubMed:23236153}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;cervix;kidney;mammary gland;stomach; atrioventricular node;skeletal muscle; . 0.16428 0.069852974 59.10592121 2650.66323 9.66836 CWC25 0.0080101658085688 0.977729099013093 0.0142607351783384 CWC25 spliceosome-associated protein homolog . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;atrium;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.20550 0.10468 -0.115612493 45.12856806 76.64648 1.83775 CWC27 1.01532147516582e-05 0.937004101818205 0.0629857449670431 CWC27 spliceosome associated protein homolog FUNCTION: PPIases accelerate the folding of proteins. {ECO:0000250}.; . . . . 0.07207 . -0.291981272 33.20358575 44.35634 1.27210 CWF19L1 5.68864368127268e-09 0.626391494292987 0.373608500018369 CWF19-like 1, cell cycle control (S. pombe) . . TISSUE SPECIFICITY: Expressed in many brain regions, including cerebellum, thalamus and occipital, parietal and temporal lobes (at protein level). Also expressed in the spinal cord (at protein level). {ECO:0000269|PubMed:25361784}.; ovary;salivary gland;colon;skin;uterus;prostate;whole body;frontal lobe;endometrium;synovium;larynx;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;stomach; dorsal root ganglion;testis - seminiferous tubule;testis;appendix;ciliary ganglion;atrioventricular node;bone marrow; 0.17269 0.08249 0.464864541 78.69190847 3289.19041 10.94872 CWF19L2 9.64691491307459e-09 0.500135179278837 0.499864811074248 CWF19-like 2, cell cycle control (S. pombe) . . . unclassifiable (Anatomical System);smooth muscle;lymph node;cartilage;heart;ovary;islets of Langerhans;sympathetic chain;colon;parathyroid;skin;skeletal muscle;uterus;bile duct;prostate;whole body;lung;frontal lobe;endometrium;nasopharynx;bone;thyroid;placenta;liver;testis;kidney;brain; dorsal root ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node; 0.17764 0.09681 0.626470967 83.55154518 3527.13215 11.45817 CWH43 5.77317899546204e-15 0.0268330160151869 0.973166983984807 cell wall biogenesis 43 C-terminal homolog FUNCTION: Involved in lipid remodeling during GPI-anchor maturation. {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;prostate;heart;endometrium;hypopharynx;head and neck;kidney;skin; subthalamic nucleus;superior cervical ganglion;prostate;skeletal muscle; . . 0.023941474 55.75607455 6450.51777 16.87098 CX3CL1 0.963378216670433 0.0365503136895976 7.14696399695686e-05 C-X3-C motif chemokine ligand 1 FUNCTION: The soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. May play a role in regulating leukocyte adhesion and migration processes at the endothelium. Binds to CX3CR1. {ECO:0000269|PubMed:21829356}.; . TISSUE SPECIFICITY: Small intestine, colon, testis, prostate, heart, brain, lung, skeletal muscle, kidney and pancreas.; colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;testis;spinal ganglion;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;lung;placenta;hippocampus;liver;spleen;kidney;mammary gland;stomach; whole brain;amygdala;thalamus;medulla oblongata;subthalamic nucleus;superior cervical ganglion;globus pallidus;pons;caudate nucleus;parietal lobe;cingulate cortex; 0.13324 0.31896 -0.510624372 21.65015334 36.05221 1.08282 CX3CR1 0.107291641248763 0.775970083501215 0.116738275250022 C-X3-C motif chemokine receptor 1 FUNCTION: Receptor for the CX3C chemokine fractalkine and mediates both its adhesive and migratory functions. Acts as coreceptor with CD4 for HIV-1 virus envelope protein (in vitro). Isoform 2 and isoform 3 seem to be more potent HIV-1 coreceptors than isoform 1.; DISEASE: Macular degeneration, age-related, 12 (ARMD12) [MIM:613784]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. {ECO:0000269|PubMed:15208270}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in lymphoid and neural tissues.; unclassifiable (Anatomical System);cartilage;tongue;spinal cord;blood;uterus;pancreas;prostate;lung;endometrium;thyroid;placenta;testis;head and neck;kidney;brain;mammary gland; amygdala;spinal cord;whole blood; 0.33672 0.36637 0.92967242 89.79122435 996.80543 6.08548 CXADR 0.342891274842555 0.654169915527156 0.00293880963028902 coxsackie virus and adenovirus receptor FUNCTION: Component of the epithelial apical junction complex that may function as an homophilic cell adhesion molecule and is essential for tight junction integrity. Also involved in transepithelial migration of leukocytes through adhesive interactions with AMICA1/JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, AMICA1 induces downstream cell signaling events in gamma-delta T- cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T- cells that in turn stimulate epithelial tissues repair. {ECO:0000269|PubMed:11734628, ECO:0000269|PubMed:12297051, ECO:0000269|PubMed:15800062, ECO:0000269|PubMed:19064666, ECO:0000269|PubMed:9096397}.; . TISSUE SPECIFICITY: Expressed in pancreas, brain, heart, small intestine, testis, prostate and at a lower level in liver and lung. Isoform 5 is ubiquitously expressed. Isoform 3 is expressed in heart, lung and pancreas. In skeletal muscle, isoform 1 is found at the neuromuscular junction and isoform 2 is found in blood vessels. In cardiac muscle, isoform 1 and isoform 2 are found at intercalated disks. In heart expressed in subendothelial layers of the vessel wall but not in the luminal endothelial surface. Expression is elevated in hearts with dilated cardiomyopathy. {ECO:0000269|PubMed:10490761, ECO:0000269|PubMed:11457744, ECO:0000269|PubMed:11549277, ECO:0000269|PubMed:9096397}.; ovary;colon;skin;uterus;prostate;endometrium;thyroid;pituitary gland;testis;bladder;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;skeletal muscle;pancreas;lung;nasopharynx;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; prostate;testis - interstitial;fetal brain;testis - seminiferous tubule;testis; . 0.22810 -0.005381972 53.50908233 105.35884 2.22286 CXADRP1 . . . coxsackie virus and adenovirus receptor pseudogene 1 . . . . . . . . . . . CXADRP2 . . . coxsackie virus and adenovirus receptor pseudogene 2 . . . . . . . . . . . CXADRP3 . . . coxsackie virus and adenovirus receptor pseudogene 3 . . . . . . . . . . . CXB3S . . . coxsackie virus B3 sensitivity . . . . . . . . . . . CXCL1 0.0924102929795663 0.76698503809182 0.140604668928614 C-X-C motif chemokine ligand 1 FUNCTION: Has chemotactic activity for neutrophils. May play a role in inflammation and exerts its effects on endothelial cells in an autocrine fashion. In vitro, the processed forms GRO- alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) show a 30-fold higher chemotactic activity. {ECO:0000269|PubMed:10095777}.; . . . . 0.26557 0.57479 0.435547893 77.45340882 30.83426 0.97755 CXCL1P1 . . . C-X-C motif chemokine ligand 1 pseudogene 1 . . . . . . . . . . . CXCL2 0.00141254997978349 0.429914827494718 0.568672622525499 C-X-C motif chemokine ligand 2 FUNCTION: Produced by activated monocytes and neutrophils and expressed at sites of inflammation. Hematoregulatory chemokine, which, in vitro, suppresses hematopoietic progenitor cell proliferation. GRO-beta(5-73) shows a highly enhanced hematopoietic activity. {ECO:0000269|PubMed:10725737}.; . . unclassifiable (Anatomical System);liver;stomach; smooth muscle;beta cell islets;fetal lung; 0.07014 0.53339 . . 28.16832 0.90310 CXCL3 0.0100002452503271 0.603519993684935 0.386479761064738 C-X-C motif chemokine ligand 3 FUNCTION: Ligand for CXCR2 (By similarity). Has chemotactic activity for neutrophils. May play a role in inflammation and exert its effects on endothelial cells in an autocrine fashion. In vitro, the processed form GRO-gamma(5-73) shows a fivefold higher chemotactic activity for neutrophilic granulocytes. {ECO:0000250, ECO:0000269|PubMed:10095777}.; . . unclassifiable (Anatomical System);pancreas;lung;endometrium;islets of Langerhans;liver;colon;cervix;spleen;blood;stomach; smooth muscle;pons; 0.04042 0.16532 -0.031067188 51.03798066 119.02536 2.37401 CXCL5 0.000222602233631482 0.303005828586343 0.696771569180025 C-X-C motif chemokine ligand 5 FUNCTION: Involved in neutrophil activation. In vitro, ENA-78(8- 78) and ENA-78(9-78) show a threefold higher chemotactic activity for neutrophil granulocytes. {ECO:0000269|PubMed:10095777}.; . . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;colon;skin;uterus;breast;pancreas;lung;alveolus;liver;spleen;kidney;stomach; superior cervical ganglion;smooth muscle;fetal lung;trigeminal ganglion; 0.28528 0.20325 0.21326276 67.71644256 14.25489 0.51575 CXCL6 0.000196265143583925 0.284394904054381 0.715408830802035 C-X-C motif chemokine ligand 6 FUNCTION: Chemotactic for neutrophil granulocytes. Signals through binding and activation of its receptors (CXCR1 and CXCR2). In addition to its chemotactic and angiogenic properties, it has strong antibacterial activity against Gram-positive and Gram- negative bacteria (90-fold-higher when compared to CXCL5 and CXCL7). {ECO:0000269|PubMed:18443119, ECO:0000269|PubMed:8399143, ECO:0000269|PubMed:8423327, ECO:0000269|PubMed:9057843}.; . . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;skin;breast;uterus;prostate;pancreas;lung;bone;placenta;alveolus;liver;testis;spleen;kidney;spinal ganglion;brain;bladder; superior cervical ganglion;smooth muscle;pons;trigeminal ganglion; 0.08173 0.17334 0.014844891 54.94810097 38.33331 1.13759 CXCL8 . . . C-X-C motif chemokine ligand 8 FUNCTION: IL-8 is a chemotactic factor that attracts neutrophils, basophils, and T-cells, but not monocytes. It is also involved in neutrophil activation. It is released from several cell types in response to an inflammatory stimulus. IL-8(6-77) has a 5-10-fold higher activity on neutrophil activation, IL-8(5-77) has increased activity on neutrophil activation and IL-8(7-77) has a higher affinity to receptors CXCR1 and CXCR2 as compared to IL-8(1-77), respectively. {ECO:0000269|PubMed:11978786, ECO:0000269|PubMed:2145175, ECO:0000269|PubMed:2212672}.; . . . . 0.56895 0.90772 -0.207437529 38.2814343 . . CXCL9 0.00533395218084944 0.709105273526269 0.285560774292882 C-X-C motif chemokine ligand 9 FUNCTION: Cytokine that affects the growth, movement, or activation state of cells that participate in immune and inflammatory response. Chemotactic for activated T-cells. Binds to CXCR3.; . . smooth muscle;ovary;colon;parathyroid;uterus;prostate;endometrium;larynx;thyroid;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;adrenal cortex;blood;pancreas;lung;adrenal gland;nasopharynx;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06419 0.35525 0.257356108 69.83368719 4.13391 0.15161 CXCL10 0.731025929703926 0.256718945687922 0.0122551246081519 C-X-C motif chemokine ligand 10 FUNCTION: Chemotactic for monocytes and T-lymphocytes. Binds to CXCR3.; . . lymphoreticular;smooth muscle;ovary;salivary gland;colon;parathyroid;skin;uterus;prostate;endometrium;thyroid;testis;brain;bladder;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;heart;adrenal cortex;pharynx;blood;breast;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe; 0.13044 0.58779 0.301449681 71.80938901 19.14765 0.65989 CXCL11 0.126083380430516 0.780115244071786 0.0938013754976977 C-X-C motif chemokine ligand 11 FUNCTION: Chemotactic for interleukin-activated T-cells but not unstimulated T-cells, neutrophils or monocytes. Induces calcium release in activated T-cells. Binds to CXCR3. May play an important role in CNS diseases which involve T-cell recruitment. May play a role in skin immune responses.; . TISSUE SPECIFICITY: High levels in peripheral blood leukocytes, pancreas and liver astrocytes. Moderate levels in thymus, spleen and lung. Low levels in placenta, prostate and small intestine. Also found in epidermal basal layer keratinocytes in skin disorders.; unclassifiable (Anatomical System);uterus;lung;cartilage;tongue;testis;colon;head and neck;brain;mammary gland;aorta; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.42551 0.23771 0.279402865 70.86577023 16.34136 0.57922 CXCL12 0.118587913081985 0.77925649848724 0.102155588430775 C-X-C motif chemokine ligand 12 FUNCTION: Chemoattractant active on T-lymphocytes, monocytes, but not neutrophils. Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. Also binds to atypical chemokine receptor ACKR3, which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. SDF-1-beta(3-72) and SDF-1- alpha(3-67) show a reduced chemotactic activity. Binding to cell surface proteoglycans seems to inhibit formation of SDF-1-alpha(3- 67) and thus to preserve activity on local sites. Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. Stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. Inhibits CXCR4-mediated infection by T- cell line-adapted HIV-1. Plays a protective role after myocardial infarction. Induces down-regulation and internalization of ACKR3 expressed in various cells. Has several critical functions during embryonic development; required for B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation. {ECO:0000269|PubMed:11069075, ECO:0000269|PubMed:11859124, ECO:0000269|PubMed:16107333, ECO:0000269|PubMed:18802065, ECO:0000269|PubMed:19255243, ECO:0000269|PubMed:8752281}.; . TISSUE SPECIFICITY: Isoform Alpha and isoform Beta are ubiquitously expressed, with highest levels detected in liver, pancreas and spleen. Isoform Gamma is mainly expressed in heart, with weak expression detected in several other tissues. Isoform Delta, isoform Epsilon and isoform Theta have highest expression levels in pancreas, with lower levels detected in heart, kidney, liver and spleen. {ECO:0000269|PubMed:16626895}.; smooth muscle;sympathetic chain;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;cerebral cortex;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;hypothalamus;pineal body;lung;epididymis;visual apparatus;hippocampus;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; uterus;dorsal root ganglion;superior cervical ganglion;heart;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;bone marrow; 0.60976 . 0.014844891 54.94810097 14.81892 0.53379 CXCL13 0.461397954954361 0.512712119067766 0.0258899259778733 C-X-C motif chemokine ligand 13 FUNCTION: Chemotactic for B-lymphocytes but not for T-lymphocytes, monocytes and neutrophils. Does not induce calcium release in B- lymphocytes. Binds to BLR1/CXCR5.; . TISSUE SPECIFICITY: Highest levels in liver, followed by spleen, lymph node, appendix and stomach. Low levels in salivary gland, mammary gland and fetal spleen.; unclassifiable (Anatomical System);lymph node;heart;ovary;parathyroid;skin;skeletal muscle;breast;uterus;pancreas;prostate;whole body;lung;endometrium;nasopharynx;bone;placenta;spleen;kidney;aorta;stomach; dorsal root ganglion;superior cervical ganglion;lymph node;salivary gland;fetal lung;tonsil;skeletal muscle; 0.40970 0.36733 0.21326276 67.71644256 2.48942 0.09178 CXCL14 0.0227861893272512 0.765690611240672 0.211523199432077 C-X-C motif chemokine ligand 14 FUNCTION: Potent chemoattractant for neutrophils, and weaker for dendritic cells. Not chemotactic for T-cells, B-cells, monocytes, natural killer cells or granulocytes. Does not inhibit proliferation of myeloid progenitors in colony formation assays. {ECO:0000269|PubMed:10049774, ECO:0000269|PubMed:10946286}.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Highly expressed in normal tissue without inflammatory stimuli and infrequently expressed in cancer cell lines. Weakly expressed in monocyte- derived dendritic cells. Not detected in lung or unstimulated peripheral blood lymphocytes. {ECO:0000269|PubMed:10049774, ECO:0000269|PubMed:10854217, ECO:0000269|PubMed:10946286}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;lens;skeletal muscle;pancreas;lung;cornea;adrenal gland;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve; whole brain;medulla oblongata;superior cervical ganglion;occipital lobe;tongue;temporal lobe;atrioventricular node;kidney;trigeminal ganglion;skin;parietal lobe;cingulate cortex; 0.31860 0.21387 0.079165051 59.43029016 7.02105 0.26365 CXCL16 0.043211059537913 0.848431868867419 0.108357071594668 C-X-C motif chemokine ligand 16 FUNCTION: Acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis (By similarity). Induces a strong chemotactic response. Induces calcium mobilization. Binds to CXCR6/Bonzo. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in T-cell areas. Expressed in spleen, lymph nodes, lung, kidney, small intestine and thymus. Weak expression in heart and liver and no expression in brain and bone marrow.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pineal body;pharynx;blood;lens;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.01438 0.03448 0.595326758 82.66100495 827.52993 5.63946 CXCL17 0.0285883727188355 0.800975254075825 0.170436373205339 C-X-C motif chemokine ligand 17 FUNCTION: Plays a role in angiogenesis and possibly in the development of tumors. May be a housekeeping chemokine regulating recruitment of nonactivated blood monocytes and immature dendritic cells into tissues. May play a role in the innate defense against infections. {ECO:0000269|PubMed:16455961, ECO:0000269|PubMed:16989774, ECO:0000269|PubMed:17307946}.; . TISSUE SPECIFICITY: Detected in trachea, stomach, lung and skeletal muscle. Detected in intestine and in normal and asthmatic lung (at protein level). Breast tumors showed 3- to 24-fold up- regulation. {ECO:0000269|PubMed:16455961, ECO:0000269|PubMed:16989774}.; unclassifiable (Anatomical System);heart;ovary;lacrimal gland;islets of Langerhans;parathyroid;skin;breast;uterus;pancreas;prostate;optic nerve;lung;larynx;nasopharynx;thyroid;placenta;hypopharynx;testis;head and neck;stomach; . 0.13275 0.08663 -0.119252484 44.53880632 27.62689 0.88863 CXCR1 0.000374556416932971 0.38984011254121 0.609785331041857 C-X-C motif chemokine receptor 1 FUNCTION: Receptor to interleukin-8, which is a powerful neutrophils chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activate a phosphatidylinositol-calcium second messenger system. This receptor binds to IL-8 with a high affinity and to MGSA (GRO) with a low affinity.; . . unclassifiable (Anatomical System);bone;liver;colon;blood;brain;bone marrow; superior cervical ganglion;ciliary ganglion;atrioventricular node;whole blood;trigeminal ganglion;skeletal muscle;bone marrow; 0.06640 0.30694 0.464864541 78.69190847 587.16237 4.91502 CXCR2 0.405284397129407 0.556617076633493 0.0380985262370993 C-X-C motif chemokine receptor 2 FUNCTION: Receptor for interleukin-8 which is a powerful neutrophil chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Binds to IL-8 with high affinity. Also binds with high affinity to CXCL3, GRO/MGSA and NAP-2.; . . unclassifiable (Anatomical System);lung;nasopharynx;bone;placenta;colon;spleen;thymus; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;whole blood; 0.21678 0.32495 0.597144447 82.7435716 55.61045 1.49843 CXCR2P1 . . . C-X-C motif chemokine receptor 2 pseudogene 1 . . . . . . . . . . . CXCR3 0.257493403151663 0.639885508999644 0.102621087848692 C-X-C motif chemokine receptor 3 FUNCTION: Isoform 1: Receptor for the C-X-C chemokine CXCL9, CXCL10 and CXCL11 and mediates the proliferation, survival and angiogenic activity of human mesangial cells (HMC) through a heterotrimeric G-protein signaling pathway (PubMed:12782716). Binds to CCL21. Probably promotes cell chemotaxis response. {ECO:0000269|PubMed:12782716}.; FUNCTION: Isoform 3: Mediates the activity of CXCL11.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are mainly expressed in heart, kidney, liver and skeletal muscle. Isoform 1 is also expressed in placenta. Isoform 2 is expressed in endothelial cells. Expressed in T-cells (at protein level). {ECO:0000269|PubMed:12782716, ECO:0000269|PubMed:23121557}.; . . 0.07304 0.38391 -0.095386216 46.48502005 3.86133 0.14426 CXCR4 0.427450979947767 0.539796705345444 0.0327523147067891 C-X-C motif chemokine receptor 4 FUNCTION: Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation. Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels. Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival. {ECO:0000269|PubMed:10074102, ECO:0000269|PubMed:10644702, ECO:0000269|PubMed:10825158, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:17197449, ECO:0000269|PubMed:20048153, ECO:0000269|PubMed:20228059, ECO:0000269|PubMed:20505072, ECO:0000269|PubMed:8752280, ECO:0000269|PubMed:8752281}.; DISEASE: WHIM syndrome (WHIMS) [MIM:193670]: Immunodeficiency disease characterized by neutropenia, hypogammaglobulinemia and extensive human papillomavirus (HPV) infection. Despite the peripheral neutropenia, bone marrow aspirates from affected individuals contain abundant mature myeloid cells, a condition termed myelokathexis. {ECO:0000269|PubMed:12692554}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in numerous tissues, such as peripheral blood leukocytes, spleen, thymus, spinal cord, heart, placenta, lung, liver, skeletal muscle, kidney, pancreas, cerebellum, cerebral cortex and medulla (in microglia as well as in astrocytes), brain microvascular, coronary artery and umbilical cord endothelial cells. Isoform 1 is predominant in all tissues tested. {ECO:0000269|PubMed:11276205}.; sympathetic chain;colon;parathyroid;vein;skin;retina;bone marrow;uterus;endometrium;synovium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;hypothalamus;adrenal cortex;blood;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;olfactory bulb;lymph node;adrenal gland;adrenal cortex;white blood cells;whole blood;trigeminal ganglion;tonsil;thymus;bone marrow; 0.90261 0.79193 -0.295622497 32.61972163 7.8354 0.28802 CXCR5 0.16025378973425 0.774441435138488 0.0653047751272621 C-X-C motif chemokine receptor 5 FUNCTION: Cytokine receptor that binds to B-lymphocyte chemoattractant (BLC). Involved in B-cell migration into B-cell follicles of spleen and Peyer patches but not into those of mesenteric or peripheral lymph nodes. May have a regulatory function in Burkitt lymphoma (BL) lymphomagenesis and/or B-cell differentiation.; . TISSUE SPECIFICITY: Expression in mature B-cells and Burkitt lymphoma cells.; unclassifiable (Anatomical System);amygdala;lymph node;cartilage;blood;skin;skeletal muscle;pancreas;prostate;optic nerve;lung;endometrium;nasopharynx;bone;liver;testis;spleen;germinal center;spinal ganglion;brain;stomach;peripheral nerve; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.31525 0.29541 -0.402212257 26.7338995 45.98455 1.30526 CXCR6 6.15120183208142e-05 0.277642392203038 0.722296095778642 C-X-C motif chemokine receptor 6 FUNCTION: Receptor for the C-X-C chemokine CXCL16. Used as a coreceptor by SIVs and by strains of HIV-2 and m-tropic HIV-1.; . TISSUE SPECIFICITY: Expressed in lymphoid tissues and activated T cells.; unclassifiable (Anatomical System);uterus;pancreas;endometrium;placenta;liver;spleen;kidney; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.04210 0.17669 -0.271755481 34.31823543 804.38456 5.58931 CXorf21 0.255813631360974 0.640395244610694 0.103791124028332 chromosome X open reading frame 21 . . . . . 0.19647 0.10424 -0.185391282 39.67916962 5.58073 0.20785 CXorf23 0.803897863874202 0.19605619968084 4.59364449579063e-05 chromosome X open reading frame 23 . . . meninges;lymph node;urinary;colon;blood;skeletal muscle;skin;retina;breast;pancreas;pia mater;larynx;placenta;head and neck;dura mater;aorta; . 0.21460 . -0.069700724 48.54328851 63.4816 1.63184 CXorf36 0.00760359252342126 0.777558178642607 0.214838228833972 chromosome X open reading frame 36 . DISEASE: Note=Genetic variations in CXorf36 may be associated with susceptibility to autism. {ECO:0000269|PubMed:21264219}.; . . . 0.13579 . 1.06196211 91.507431 3215.09146 10.81006 CXorf38 0.00516358433779017 0.889645850235256 0.105190565426953 chromosome X open reading frame 38 . . . unclassifiable (Anatomical System);lymphoreticular;islets of Langerhans;colon;blood;breast;prostate;lung;bone;placenta;pituitary gland;alveolus;liver;germinal center;kidney;stomach; . 0.13698 . 0.43736446 77.56546355 24.78071 0.81434 CXorf40A 0.61074124217066 0.354450984610476 0.0348077732188646 chromosome X open reading frame 40A FUNCTION: May have an important role of cell protection in inflammation reaction.; . TISSUE SPECIFICITY: Expressed primarily in heart, skeletal muscle, kidney, liver and placenta. Relatively high level of expression in spleen, colon and small intestine. Almost no expression in brain, thymus, lung and peripheral blood leukocytes. {ECO:0000269|PubMed:15541360}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;bone;brain;unclassifiable (Anatomical System);lymph node;blood;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;stomach; . . 0.07313 0.080983847 59.76055674 4.10291 0.14978 CXorf40B 0.642796581069124 0.330023969544076 0.0271794493868007 chromosome X open reading frame 40B . . . ovary;sympathetic chain;colon;parathyroid;choroid;vein;skin;retina;uterus;prostate;whole body;endometrium;bone;thyroid;testis;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;blood;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; . . . 0.747842143 86.47676339 21.09757 0.71373 CXorf49 . . . chromosome X open reading frame 49 . . . . . . . . . . . CXorf49B . . . chromosome X open reading frame 49B . . . . . . . . . . . CXorf51A . . . chromosome X open reading frame 51A . . . . . . . . . . . CXorf51B . . . chromosome X open reading frame 51B . . . . . . . . . . . CXorf56 0.925801506265085 0.0737797282210153 0.000418765513900237 chromosome X open reading frame 56 . . . myocardium;ovary;salivary gland;intestine;colon;skin;uterus;prostate;frontal lobe;endometrium;iris;brain;bladder;tonsil;unclassifiable (Anatomical System);tongue;islets of Langerhans;pineal body;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;head and neck;cervix;kidney;stomach; superior cervical ganglion;skeletal muscle;cingulate cortex; 0.15463 0.11262 0.035072054 56.2514744 2.94495 0.10655 CXorf57 0.187172500066797 0.812728977540491 9.85223927122071e-05 chromosome X open reading frame 57 . . . . . 0.56981 . -0.402212257 26.7338995 326.40338 3.84182 CXorf58 0.000356507184657727 0.830511217243708 0.169132275571634 chromosome X open reading frame 58 . . . . . 0.11845 . 0.729426781 86.17008728 551.52051 4.77543 CXorf65 0.905102153264171 0.0941151508408886 0.000782695894940585 chromosome X open reading frame 65 . . . . . . . 0.369407109 74.95281906 43.25985 1.24835 CXorf66 0.0183930362804906 0.727571171768725 0.254035791950785 chromosome X open reading frame 66 . . . . . . . 0.793752871 87.40268931 4.19169 0.15322 CXorf67 0.868926865860632 0.129275012106946 0.00179812203242165 chromosome X open reading frame 67 . . . lung;placenta;testis; . . . . . 11.65682 0.42273 CXXC1 0.99786210530366 0.00213789193431709 2.76202311918403e-09 CXXC finger protein 1 FUNCTION: Transcriptional activator that exhibits a unique DNA binding specificity for CpG unmethylated motifs with a preference for CpGG. {ECO:0000269|PubMed:21407193}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;pineal body;muscle;blood;lens;skeletal muscle;breast;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;cerebellum peduncles;pons;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.14457 0.11614 -0.934977358 9.465675867 60.14648 1.57403 CXXC1P1 . . . CXXC finger protein 1 pseudogene 1 . . . . . . . . . . . CXXC4 . . . CXXC finger protein 4 FUNCTION: Acts as a negative regulator of the Wnt signaling pathway via its interaction with DVL1. {ECO:0000250}.; . . . . 0.53604 0.11809 -0.009020804 52.8544468 98.64157 2.14793 CXXC5 0.79535527912222 0.19881901411903 0.00582570675874976 CXXC finger protein 5 FUNCTION: May indirectly participate in activation of the NF- kappa-B and MAPK pathways. Acts as a mediator of BMP4-mediated modulation of canonical Wnt signaling activity in neural stem cells (By similarity). Required for DNA damage-induced ATM phosphorylation, p53 activation and cell cycle arrest. Involved in myelopoiesis. Transcription factor. Binds to the oxygen responsive element of COX4I2 and represses its transcription under hypoxia conditions (4% oxygen), as well as normoxia conditions (20% oxygen) (PubMed:23303788). May repress COX4I2 transactivation induced by CHCHD2 and RBPJ (PubMed:23303788). {ECO:0000250, ECO:0000269|PubMed:19182210, ECO:0000269|PubMed:19557330, ECO:0000269|PubMed:23303788}.; . . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;tonsil;heart;cartilage;pineal body;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;thymus;cerebellum; cerebellum peduncles;cerebellum; 0.44111 0.10324 -0.317668748 31.45789101 11.51236 0.41539 CYB5A 0.0337393159429441 0.82280816350758 0.143452520549476 cytochrome b5 type A (microsomal) FUNCTION: Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases.; DISEASE: Methemoglobinemia CYB5A-related (METHB-CYB5A) [MIM:250790]: A form of methemoglobinemia, a hematologic disease characterized by the presence of excessive amounts of methemoglobin in blood cells, resulting in decreased oxygen carrying capacity of the blood, cyanosis and hypoxia. {ECO:0000269|PubMed:8168836}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;epididymis;nasopharynx;placenta;hippocampus;macula lutea;visual apparatus;liver;spleen;kidney;aorta; fetal liver;superior cervical ganglion;adipose tissue;liver;fetal lung;kidney;trigeminal ganglion; 0.18459 0.33541 0.080983847 59.76055674 38.70304 1.14655 CYB5AP2 . . . cytochrome b5 type A (microsomal) pseudogene 2 . . . . . . . . . . . CYB5AP3 . . . cytochrome b5 type A (microsomal) pseudogene 3 . . . . . . . . . . . CYB5AP4 . . . cytochrome b5 type A (microsomal) pseudogene 4 . . . . . . . . . . . CYB5AP5 . . . cytochrome b5 type A (microsomal) pseudogene 5 . . . . . . . . . . . CYB5B 0.259577989859624 0.713647972857879 0.0267740372824968 cytochrome b5 type B (outer mitochondrial membrane) FUNCTION: Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. {ECO:0000250}.; . . smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;adrenal gland;adrenal cortex;globus pallidus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.23716 0.10842 -0.207437529 38.2814343 80.36516 1.89440 CYB5D1 4.57519538498037e-05 0.412735896326542 0.587218351719608 cytochrome b5 domain containing 1 . . . unclassifiable (Anatomical System);ovary;heart;salivary gland;sympathetic chain;intestine;pharynx;colon;blood;skin;breast;uterus;prostate;lung;endometrium;nasopharynx;bone;placenta;visual apparatus;duodenum;liver;testis;kidney;brain;bladder;stomach; . 0.10161 . 0.260991686 70.25831564 2549.71699 9.43214 CYB5D2 4.57076963496539e-05 0.412553199861217 0.587401092442434 cytochrome b5 domain containing 2 FUNCTION: Heme-binding protein which promotes neuronal but not astrocyte differentiation. {ECO:0000250}.; . . medulla oblongata;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;bone;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach; testis - interstitial;testis; 0.09875 0.21492 -0.602450568 17.91106393 59.57744 1.56669 CYB5R1 9.32776750510642e-09 0.163154384074808 0.836845606597425 cytochrome b5 reductase 1 FUNCTION: NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10611283}.; . . 0.35234 0.13030 -0.137658575 43.57159707 1497.54316 7.19965 CYB5R2 2.70695453986963e-05 0.531841915831408 0.468131014623194 cytochrome b5 reductase 2 FUNCTION: NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction (By similarity). Responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4- disulfophenyl]-2H tetrazolium monosodium salt (WST-1). {ECO:0000250, ECO:0000269|PubMed:15858218}.; . TISSUE SPECIFICITY: Restricted expression. {ECO:0000269|PubMed:10611283}.; smooth muscle;ovary;salivary gland;intestine;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;hypothalamus;pharynx;blood;lens;lung;cornea;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;olfactory bulb;testis - seminiferous tubule;testis;atrioventricular node; 0.23078 0.10588 0.731244617 86.21137061 1858.85138 7.94672 CYB5R3 0.210867104328179 0.780064348849774 0.00906854682204622 cytochrome b5 reductase 3 FUNCTION: Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.; DISEASE: Methemoglobinemia CYB5R3-related (METHB-CYB5R3) [MIM:250800]: A form of methemoglobinemia, a hematologic disease characterized by the presence of excessive amounts of methemoglobin in blood cells, resulting in decreased oxygen carrying capacity of the blood, cyanosis and hypoxia. There are two types of methemoglobinemia CYB5R3-related. In type 1, the defect affects the soluble form of the enzyme, is restricted to red blood cells, and causes well-tolerated methemoglobinemia. In type 2, the defect affects both the soluble and microsomal forms of the enzyme and is thus generalized, affecting red cells, leukocytes and all body tissues. Type 2 methemoglobinemia is associated with mental deficiency and other neurologic symptoms. {ECO:0000269|PubMed:10807796, ECO:0000269|PubMed:12393396, ECO:0000269|PubMed:1400360, ECO:0000269|PubMed:15622768, ECO:0000269|PubMed:1707593, ECO:0000269|PubMed:1898726, ECO:0000269|PubMed:7718898, ECO:0000269|PubMed:8119939, ECO:0000269|PubMed:9695975, ECO:0000269|PubMed:9886302}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 2 is expressed at late stages of erythroid maturation.; smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;skin;retina;uterus;prostate;optic nerve;whole body;ganglion;cerebral cortex;endometrium;oesophagus;larynx;bone;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; adipose tissue;heart;adrenal gland;testis;ciliary ganglion; 0.20580 0.28174 0.50895761 80.20169851 759.24656 5.46093 CYB5R4 0.000343480484234464 0.98849207420932 0.0111644453064458 cytochrome b5 reductase 4 FUNCTION: NADH-cytochrome b5 reductase involved in endoplasmic reticulum stress response pathway. Plays a critical role in protecting pancreatic beta-cells against oxidant stress, possibly by protecting the cell from excess buildup of reactive oxygen species (ROS). Reduces a variety of substrates in vitro, such as cytochrome c, feericyanide and methemoglobin.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10611283}.; . . 0.22261 . 0.284856336 71.40835103 188.34982 2.98109 CYB5RL 4.23010695021034e-05 0.628939524397225 0.371018174533273 cytochrome b5 reductase like FUNCTION: NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. {ECO:0000250}.; . . unclassifiable (Anatomical System);pancreas;optic nerve;cartilage;ovary;heart;endometrium;bone;liver;spleen;germinal center;brain;skin; pons; . . 0.797386419 87.53833451 3586.9037 11.58745 CYB561 0.698896026820601 0.297321586460143 0.0037823867192562 cytochrome b561 FUNCTION: Secretory vesicle-specific electron transport protein.; . . ovary;salivary gland;sympathetic chain;rectum;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;small intestine;heart;islets of Langerhans;urinary;adrenal cortex;lens;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; prostate;superior cervical ganglion;trachea;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.22511 0.15581 -0.538132194 20.26421326 33.02557 1.02255 CYB561A3 0.0587317231678231 0.867621587611716 0.0736466892204607 cytochrome b561 family member A3 FUNCTION: Ferric-chelate reductase that reduces Fe(3+) to Fe(2+) before its transport from the endosome to the cytoplasm. Probably uses ascorbate as electron donor (By similarity). {ECO:0000250}.; . . . . 0.11510 0.10981 -0.337894035 30.37272942 57.6399 1.53369 CYB561D1 0.0158304191038284 0.698679665384415 0.285489915511757 cytochrome b561 family member D1 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;testis;amniotic fluid;germinal center;unclassifiable (Anatomical System);heart;pineal body;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;liver;spleen;stomach; . 0.29399 . 0.104848986 61.49445624 50.68697 1.40231 CYB561D2 0.0147104753856424 0.874424762156621 0.110864762457737 cytochrome b561 family member D2 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; liver;trigeminal ganglion; 0.11901 0.10725 -0.093566408 46.7386176 37.95855 1.12722 CYBA 0.00357298293939449 0.62425666720806 0.372170349852546 cytochrome b-245, alpha polypeptide FUNCTION: Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide. {ECO:0000269|PubMed:15824103}.; DISEASE: Granulomatous disease, chronic, cytochrome-b-negative, autosomal recessive (ARCGD) [MIM:233690]: A disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life-threatening bacterial/fungal infections. {ECO:0000269|PubMed:10759707, ECO:0000269|PubMed:10910929, ECO:0000269|PubMed:10914676, ECO:0000269|PubMed:1415254, ECO:0000269|PubMed:1763037, ECO:0000269|PubMed:18422995, ECO:0000269|PubMed:2243141, ECO:0000269|PubMed:23910690, ECO:0000269|PubMed:8168815}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;head and neck;spleen;kidney;mammary gland;aorta;stomach; lymph node;heart;liver;white blood cells;kidney;whole blood;bone marrow; 0.22721 0.41778 . . 390.29064 4.15974 CYBB 0.99769789816162 0.00230202104146977 8.079691052442e-08 cytochrome b-245, beta polypeptide FUNCTION: Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc.; DISEASE: Granulomatous disease, chronic, X-linked (CGD) [MIM:306400]: A disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life-threatening bacterial/fungal infections. {ECO:0000269|PubMed:10089913, ECO:0000269|PubMed:10914676, ECO:0000269|PubMed:11462241, ECO:0000269|PubMed:11997083, ECO:0000269|PubMed:12139950, ECO:0000269|PubMed:1710153, ECO:0000269|PubMed:18773283, ECO:0000269|PubMed:22125116, ECO:0000269|PubMed:23910690, ECO:0000269|PubMed:2556453, ECO:0000269|PubMed:7927345, ECO:0000269|PubMed:8101486, ECO:0000269|PubMed:8182143, ECO:0000269|PubMed:8916969, ECO:0000269|PubMed:9111587, ECO:0000269|PubMed:9585602, ECO:0000269|PubMed:9667376, ECO:0000269|PubMed:9794433, ECO:0000269|PubMed:9856476, ECO:0000269|PubMed:9888386}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Immunodeficiency 34 (IMD34) [MIM:300645]: A form of Mendelian susceptibility to mycobacterial disease, a rare condition characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. {ECO:0000269|PubMed:21278736}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in neutrophils (at protein level). {ECO:0000269|PubMed:19028840}.; . . 0.16497 0.74918 0.349177632 74.18023119 37.74145 1.12290 CYBRD1 0.351788246409073 0.635181701719592 0.0130300518713353 cytochrome b reductase 1 FUNCTION: Ferric-chelate reductase that reduces Fe(3+) to Fe(2+). Present at the brush border of duodenal enterocytes where it probably reduces dietary Fe(3+) thereby facilitating its transport into the mucosal cells. Uses ascorbate as electron donor. May be involved in extracellular ascorbate recycling in erythrocyte membranes. May also act as a ferrireductase in airway epithelial cells. {ECO:0000269|PubMed:16521311, ECO:0000269|PubMed:16521312, ECO:0000269|PubMed:17068337, ECO:0000269|PubMed:19673882}.; . TISSUE SPECIFICITY: Present in erythrocyte membranes (at protein level). Also expressed in respiratory epithelium. {ECO:0000269|PubMed:16510471, ECO:0000269|PubMed:17068337}.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;bone;testis;dura mater;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;small intestine;pancreas;pia mater;lung;mesenchyma;adrenal gland;placenta;head and neck;kidney;stomach;aorta; uterus corpus;superior cervical ganglion;smooth muscle;adipose tissue;skeletal muscle; 0.10259 0.18266 0.681699246 84.93158764 46.45853 1.31487 CYC1 0.979014367766699 0.0209675932176646 1.80390156366949e-05 cytochrome c1 FUNCTION: This is the heme-containing component of the cytochrome b-c1 complex, which accepts electrons from Rieske protein and transfers electrons to cytochrome c in the mitochondrial respiratory chain.; DISEASE: Mitochondrial complex III deficiency, nuclear 6 (MC3DN6) [MIM:615453]: An autosomal recessive disorder caused by mitochondrial dysfunction. It is characterized by onset in early childhood of episodic acute lactic acidosis, ketoacidosis, and insulin-responsive hyperglycemia, usually associated with infection. Laboratory studies show decreased activity of mitochondrial complex III. Psychomotor development is normal. {ECO:0000269|PubMed:23910460}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;lymphoreticular;smooth muscle;ovary;foreskin;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;brain;bladder;tonsil;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus; heart;liver;kidney;skeletal muscle; 0.39964 0.22293 -0.247889024 35.98726115 26.20568 0.84930 CYCS 0.583556979310405 0.374072354622938 0.0423706660666576 cytochrome c, somatic FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; DISEASE: Thrombocytopenia 4 (THC4) [MIM:612004]: Thrombocytopenia is defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting. {ECO:0000269|PubMed:18345000}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;duodenum;kidney;stomach;aorta; . 0.36614 0.98836 0.079165051 59.43029016 6.40043 0.23965 CYCSP1 . . . cytochrome c, somatic pseudogene 1 . . . . . . . . . . . CYCSP2 . . . cytochrome c, somatic pseudogene 2 . . . . . . . . . . . CYCSP3 . . . cytochrome c, somatic pseudogene 3 . . . . . . . . . . . CYCSP4 . . . cytochrome c, somatic pseudogene 4 . . . . . . . . . . . CYCSP5 . . . cytochrome c, somatic pseudogene 5 . . TISSUE SPECIFICITY: Expressed in lymphoid tissues; Detected in spleen as well as in B-cell lines, NK cell lines and activated lymphocytes. {ECO:0000269|PubMed:8462994}.; . . . . . . . . CYCSP6 . . . cytochrome c, somatic pseudogene 6 . . . . . . . . . . . CYCSP7 . . . cytochrome c, somatic pseudogene 7 . . . . . . . . . . . CYCSP8 . . . cytochrome c, somatic pseudogene 8 . . . . . . . . . . . CYCSP10 . . . cytochrome c, somatic pseudogene 10 . . . . . . . . . . . CYCSP11 . . . cytochrome c, somatic pseudogene 11 . . . . . . . . . . . CYCSP12 . . . cytochrome c, somatic pseudogene 12 . . . . . . . . . . . CYCSP14 . . . cytochrome c, somatic pseudogene 14 . . . . . . . . . . . CYCSP16 . . . cytochrome c, somatic pseudogene 16 . . . . . . . . . . . CYCSP17 . . . cytochrome c, somatic pseudogene 17 . . . . . . . . . . . CYCSP18 . . . cytochrome c, somatic pseudogene 18 . . . . . . . . . . . CYCSP19 . . . cytochrome c, somatic pseudogene 19 . . . . . . . . . . . CYCSP20 . . . cytochrome c, somatic pseudogene 20 . . . . . . . . . . . CYCSP22 . . . cytochrome c, somatic pseudogene 22 . . . . . . . . . . . CYCSP23 . . . cytochrome c, somatic pseudogene 23 . . . . . . . . . . . CYCSP24 . . . cytochrome c, somatic pseudogene 24 . . . . . . . . . . . CYCSP25 . . . cytochrome c, somatic pseudogene 25 . . . . . . . . . . . CYCSP26 . . . cytochrome c, somatic pseudogene 26 . . . . . . . . . . . CYCSP27 . . . cytochrome c, somatic pseudogene 27 . . . . . . . . . . . CYCSP28 . . . cytochrome c, somatic pseudogene 28 . . . . . . . . . . . CYCSP29 . . . cytochrome c, somatic pseudogene 29 . . . . . . . . . . . CYCSP30 . . . cytochrome c, somatic pseudogene 30 . . . . . . . . . . . CYCSP32 . . . cytochrome c, somatic pseudogene 32 . . . . . . . . . . . CYCSP33 . . . cytochrome c, somatic pseudogene 33 . . . . . . . . . . . CYCSP34 . . . cytochrome c, somatic pseudogene 34 . . . . . . . . . . . CYCSP35 . . . cytochrome c, somatic pseudogene 35 . . . . . . . . . . . CYCSP38 . . . cytochrome c, somatic pseudogene 38 . . . . . . . . . . . CYCSP39 . . . cytochrome c, somatic pseudogene 39 . . . . . . . . . . . CYCSP40 . . . cytochrome c, somatic pseudogene 40 . . . . . . . . . . . CYCSP41 . . . cytochrome c, somatic pseudogene 41 . . . . . . . . . . . CYCSP42 . . . cytochrome c, somatic pseudogene 42 . . . . . . . . . . . CYCSP43 . . . cytochrome c, somatic pseudogene 43 . . . . . . . . . . . CYCSP44 . . . cytochrome c, somatic pseudogene 44 . . . . . . . . . . . CYCSP45 . . . cytochrome c, somatic pseudogene 45 . . . . . . . . . . . CYCSP46 . . . cytochrome c, somatic pseudogene 46 . . . . . . . . . . . CYCSP48 . . . cytochrome c, somatic pseudogene 48 . . . . . . . . . . . CYCSP49 . . . cytochrome c, somatic pseudogene 49 . . . . . . . . . . . CYCSP51 . . . cytochrome c, somatic pseudogene 51 . . . . . . . . . . . CYCSP52 . . . cytochrome c, somatic pseudogene 52 . . . . . . . . . . . CYCSP53 . . . cytochrome c, somatic pseudogene 53 . . . . . . . . . . . CYCSP55 . . . cytochrome c, somatic pseudogene 55 . . . . . . . . . . . CYCTP . . . cytochrome c, testis, pseudogene . . . . . . . . . . . CYFIP1 0.994933031618259 0.00506696838018286 1.55763416256504e-12 cytoplasmic FMR1 interacting protein 1 FUNCTION: Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit is an adapter between EIF4E and FMR1. Promotes the translation repression activity of FMR1 in brain probably by mediating its association with EIF4E and mRNA (By similarity). Regulates formation of membrane ruffles and lamellipodia. Plays a role in axon outgrowth. Binds to F-actin but not to RNA. Part of the WAVE complex that regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. Regulator of epithelial morphogenesis. May act as an invasion suppressor in cancers. {ECO:0000250, ECO:0000269|PubMed:16260607, ECO:0000269|PubMed:19524508, ECO:0000269|PubMed:21107423, ECO:0000269|PubMed:9417078}.; . . myocardium;lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus; . 0.18853 0.14087 -1.295313867 4.989384289 2808.37817 9.99956 CYFIP2 0.999998602593714 1.39740628577179e-06 4.81503429920347e-17 cytoplasmic FMR1 interacting protein 2 FUNCTION: Involved in T-cell adhesion and p53/TP53-dependent induction of apoptosis. Does not bind RNA. {ECO:0000269|PubMed:10449408, ECO:0000269|PubMed:15048733, ECO:0000269|PubMed:17245118}.; . TISSUE SPECIFICITY: Expressed in T-cells. Increased expression is observed in CD4(+) T-lymphocytes from patients with multiple sclerosis (at protein level). {ECO:0000269|PubMed:15048733}.; lymphoreticular;smooth muscle;ovary;colon;choroid;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;pituitary gland;testis;germinal center;brain;tonsil;amygdala;unclassifiable (Anatomical System);lymph node;heart;cartilage;tongue;cerebellum cortex;islets of Langerhans;hypothalamus;pineal body;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;visual apparatus;amnion;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;thymus; amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;kidney;parietal lobe;cingulate cortex;cerebellum; 0.44646 0.50538 . . 58.4113 1.54826 CYGB 0.234616769536826 0.732406561146805 0.0329766693163685 cytoglobin FUNCTION: May have a protective function during conditions of oxidative stress. May be involved in intracellular oxygen storage or transfer.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highest expression in heart, stomach, bladder and small intestine. {ECO:0000269|PubMed:11893755}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;bone;pituitary gland;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;lens;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.17936 0.28728 -0.427900189 25.14744043 3550.42848 11.50816 CYHR1 0.0538307875149217 0.700895481865645 0.245273730619433 cysteine/histidine-rich 1 . . . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;colon;fovea centralis;choroid;retina;pancreas;prostate;optic nerve;lung;endometrium;bone;placenta;macula lutea;hippocampus;pituitary gland;liver;testis;spleen;kidney;brain;stomach; atrioventricular node;trigeminal ganglion; 0.14948 . -0.291981272 33.20358575 10.43713 0.37938 CYLC1 0.606280835629087 0.385012913361004 0.00870625100990855 cylicin 1 FUNCTION: Possible architectural role during spermatogenesis. May be involved in spermatid differentiation.; . TISSUE SPECIFICITY: Testis.; testis; dorsal root ganglion;testis - interstitial;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;trigeminal ganglion; . 0.06258 0.773521534 87.06062751 302.73193 3.70627 CYLC2 5.14081582239004e-07 0.127896009021146 0.872103476897272 cylicin, basic protein of sperm head cytoskeleton 2 FUNCTION: Possible architectural role during spermatogenesis. May be involved in spermatid differentiation.; . TISSUE SPECIFICITY: Testis.; . . 0.08393 0.07719 1.776656471 96.82708186 187.28235 2.97271 CYLD 0.994720107012035 0.00527988791003733 5.07792735010748e-09 CYLD lysine 63 deubiquitinase FUNCTION: Protease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Has endodeubiquitinase activity. Plays an important role in the regulation of pathways leading to NF-kappa-B activation (PubMed:12917689, PubMed:12917691). Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation (PubMed:12917690). Negative regulator of Wnt signaling (PubMed:20227366). Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules (PubMed:19893491). Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis (PubMed:18222923, PubMed:20194890). Required for normal cell cycle progress and normal cytokinesis (PubMed:17495026, PubMed:19893491). Inhibits nuclear translocation of NF-kappa-B. Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation (PubMed:18636086). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells. Negatively regulates TNFRSF11A signaling and osteoclastogenesis (By similarity). Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation (By similarity). {ECO:0000250|UniProtKB:Q80TQ2, ECO:0000269|PubMed:12917689, ECO:0000269|PubMed:12917690, ECO:0000269|PubMed:12917691, ECO:0000269|PubMed:14676304, ECO:0000269|PubMed:17495026, ECO:0000269|PubMed:18222923, ECO:0000269|PubMed:18636086, ECO:0000269|PubMed:19893491, ECO:0000269|PubMed:20194890, ECO:0000269|PubMed:20227366}.; DISEASE: Cylindromatosis, familial (FCYL) [MIM:132700]: A disorder characterized by multiple skin tumors that develop from skin appendages, such as hair follicles and sweat glands. Affected individuals typically develop large numbers of tumors called cylindromas that arise predominantly in hairy parts of the body with approximately 90% on the head and neck. In severely affected individuals, cylindromas may combine into a confluent mass which may ulcerate or become infected (turban tumor syndrome). Individuals with familial cylindromatosis occasionally develop other types of tumors including spiradenomas that begin in sweat glands, and trichoepitheliomas arising from hair follicles. {ECO:0000269|PubMed:12190880, ECO:0000269|PubMed:16922728}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multiple familial trichoepithelioma 1 (MFT1) [MIM:601606]: Autosomal dominant dermatosis characterized by the presence of many skin tumors predominantly on the face. Since histologic examination shows dermal aggregates of basaloid cells with connection to or differentiation toward hair follicles, this disorder has been thought to represent a benign hamartoma of the pilosebaceous apparatus. Trichoepitheliomas can degenerate into basal cell carcinoma. {ECO:0000269|PubMed:14632188, ECO:0000269|PubMed:16307661, ECO:0000269|PubMed:16922728}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Brooke-Spiegler syndrome (BRSS) [MIM:605041]: An autosomal dominant disorder characterized by the appearance of multiple skin appendage tumors such as cylindroma, trichoepithelioma, and spiradenoma. These tumors are typically located in the head and neck region, appear in early adulthood, and gradually increase in size and number throughout life. {ECO:0000269|PubMed:12190880, ECO:0000269|PubMed:12950348, ECO:0000269|PubMed:14632188, ECO:0000269|PubMed:15854031}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in fetal brain, testis, and skeletal muscle, and at a lower level in adult brain, leukocytes, liver, heart, kidney, spleen, ovary and lung. Isoform 2 is found in all tissues except kidney. {ECO:0000269|PubMed:10835629}.; ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;bone;thyroid;iris;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; amygdala;dorsal root ganglion;occipital lobe;medulla oblongata;testis - interstitial;thalamus;superior cervical ganglion;hypothalamus;white blood cells;caudate nucleus;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;whole blood;tonsil;cingulate cortex;pituitary;parietal lobe; 0.70026 0.30945 -0.934977358 9.465675867 24.23092 0.79617 CYMD . . . cystoid macular dystrophy . . . . . . . . . . . CYMP . . . chymosin pseudogene . . . . . . . . . . . CYP1A1 1.97289145995058e-07 0.253361342387142 0.746638460323712 cytochrome P450 family 1 subfamily A member 1 FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.; . TISSUE SPECIFICITY: Lung, lymphocytes and placenta.; unclassifiable (Anatomical System);heart;cartilage;urinary;blood;skin;uterus;breast;prostate;lung;bone;liver;spinal ganglion;brain; . 0.08857 0.83499 0.624649618 83.53385232 1996.39253 8.23125 CYP1A2 3.28540807222054e-10 0.0461537644536996 0.95384623521776 cytochrome P450 family 1 subfamily A member 2 FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Most active in catalyzing 2-hydroxylation. Caffeine is metabolized primarily by cytochrome CYP1A2 in the liver through an initial N3-demethylation. Also acts in the metabolism of aflatoxin B1 and acetaminophen. Participates in the bioactivation of carcinogenic aromatic and heterocyclic amines. Catalizes the N-hydroxylation of heterocyclic amines and the O- deethylation of phenacetin. {ECO:0000269|PubMed:14725854}.; . TISSUE SPECIFICITY: Liver.; unclassifiable (Anatomical System);liver; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.10653 0.72184 -0.596992387 18.18825195 141.56503 2.59593 CYP1B1 0.00029647591103164 0.567991534639932 0.431711989449036 cytochrome P450 family 1 subfamily B member 1 FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, retinoid and xenobiotics. Preferentially oxidizes 17beta- estradiol to the carcinogenic 4-hydroxy derivative, and a variety of procarcinogenic compounds to their activated forms, including polycyclic aromatic hydrocarbons. Promotes angiogenesis by removing cellular oxygenation products, thereby decreasing oxidative stress, release of antiangiogenic factor THBS2, then allowing endothelial cells migration, cell adhesion and capillary morphogenesis. These changes are concommitant with the endothelial nitric oxide synthase activity and nitric oxide synthesis. Plays an important role in the regulation of perivascular cell proliferation, migration, and survival through modulation of the intracellular oxidative state and NF-kappa-B expression and/or activity, during angiogenesis. Contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression. {ECO:0000269|PubMed:10426814, ECO:0000269|PubMed:15258110, ECO:0000269|PubMed:22888116, ECO:0000269|PubMed:23821647}.; DISEASE: Peters anomaly (PETAN) [MIM:604229]: Consists of a central corneal leukoma, absence of the posterior corneal stroma and Descemet membrane, and a variable degree of iris and lenticular attachments to the central aspect of the posterior cornea. {ECO:0000269|PubMed:11403040}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Glaucoma 3, primary congenital, A (GLC3A) [MIM:231300]: An autosomal recessive form of primary congenital glaucoma (PCG). PCG is characterized by marked increase of intraocular pressure at birth or early childhood, large ocular globes (buphthalmos) and corneal edema. It results from developmental defects of the trabecular meshwork and anterior chamber angle of the eye that prevent adequate drainage of aqueous humor. {ECO:0000269|PubMed:10227395, ECO:0000269|PubMed:10655546, ECO:0000269|PubMed:11184479, ECO:0000269|PubMed:11527932, ECO:0000269|PubMed:11980847, ECO:0000269|PubMed:12036985, ECO:0000269|PubMed:12525557, ECO:0000269|PubMed:14635112, ECO:0000269|PubMed:14640114, ECO:0000269|PubMed:15255109, ECO:0000269|PubMed:15342693, ECO:0000269|PubMed:15475877, ECO:0000269|PubMed:16490498, ECO:0000269|PubMed:16735994, ECO:0000269|PubMed:9463332, ECO:0000269|PubMed:9497261}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry.; DISEASE: Glaucoma, primary open angle (POAG) [MIM:137760]: A complex and genetically heterogeneous ocular disorder characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. In some cases, POAG shows digenic inheritance involving mutations in CYP1B1 and MYOC genes. {ECO:0000269|PubMed:11774072, ECO:0000269|PubMed:15342693, ECO:0000269|PubMed:16688110, ECO:0000269|PubMed:16862072}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. CYP1B1 mutations have been reported to pose a significant risk for early-onset POAG and also modify glaucoma phenotype in patients who do not carry a MYOC mutation (PubMed:15342693). {ECO:0000269|PubMed:15342693}.; DISEASE: Glaucoma 1, open angle, A (GLC1A) [MIM:137750]: A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. {ECO:0000269|PubMed:11774072}. Note=The gene represented in this entry acts as a disease modifier. Digenic mutations in CYP1B1 and MYOC have been found in a family segregating both primary adult- onset and juvenile forms of open angle glaucoma (PubMed:11774072). All affected family members with mutations in both MYOC and CYP1B1 had juvenile glaucoma, whereas those with only the MYOC mutation had the adult-onset form (PubMed:11774072). {ECO:0000269|PubMed:11774072}.; TISSUE SPECIFICITY: Expressed in many tissues. {ECO:0000269|PubMed:8175734}.; lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;iris;bladder;brain;heart;cartilage;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;dura mater;spinal ganglion;artery;unclassifiable (Anatomical System);meninges;islets of Langerhans;bile duct;pancreas;lung;pia mater;mesenchyma;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;olfactory bulb;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10836 0.61975 0.444637294 77.91342298 3319.87445 11.01273 CYP1B1-AS1 . . . CYP1B1 antisense RNA 1 . . . . . . . . . . . CYP1D1P . . . cytochrome P450 family 1 subfamily D member 1, pseudogene . . . . . . . . . . . CYP2A6 2.17794878373007e-06 0.708893748632634 0.291104073418582 cytochrome P450 family 2 subfamily A member 6 FUNCTION: Exhibits a high coumarin 7-hydroxylase activity. Can act in the hydroxylation of the anti-cancer drugs cyclophosphamide and ifosphamide. Competent in the metabolic activation of aflatoxin B1. Constitutes the major nicotine C-oxidase. Acts as a 1,4- cineole 2-exo-monooxygenase. Possesses low phenacetin O- deethylation activity. {ECO:0000269|PubMed:11695850, ECO:0000269|PubMed:16086027, ECO:0000269|PubMed:17125252, ECO:0000269|PubMed:18779312, ECO:0000269|PubMed:1889415, ECO:0000269|PubMed:1944238}.; . TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:1889415, ECO:0000269|PubMed:1944238}.; unclassifiable (Anatomical System);breast;lung;liver;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;liver;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.23228 0.52146 0.295774947 71.64425572 375.34434 4.08402 CYP2A7 3.01470348763618e-10 0.0831784866833039 0.916821513015226 cytochrome P450 family 2 subfamily A member 7 FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.; . . unclassifiable (Anatomical System);breast;lung;liver;mammary gland; dorsal root ganglion;superior cervical ganglion;liver;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.05723 . 3.427299372 99.46331682 3238.50225 10.83690 CYP2A7P1 . . . cytochrome P450 family 2 subfamily A member 7 pseudogene 1 . . . unclassifiable (Anatomical System); testis - seminiferous tubule;ciliary ganglion;trigeminal ganglion; . . . . . . CYP2A13 0.00143445702978295 0.965497135675519 0.0330684072946982 cytochrome P450 family 2 subfamily A member 13 FUNCTION: Exhibits a coumarin 7-hydroxylase activity. Active in the metabolic activation of hexamethylphosphoramide, N,N- dimethylaniline, 2'-methoxyacetophenone, N- nitrosomethylphenylamine, and the tobacco-specific carcinogen, 4- (methylnitrosamino)-1-(3-pyridyl)-1-butanone. Possesses phenacetin O-deethylation activity. {ECO:0000269|PubMed:18779312}.; . TISSUE SPECIFICITY: Expressed in liver and a number of extrahepatic tissues, including nasal mucosa, lung, trachea, brain, mammary gland, prostate, testis, and uterus, but not in heart, kidney, bone marrow, colon, small intestine, spleen, stomach, thymus, or skeletal muscle. {ECO:0000269|PubMed:11016631}.; unclassifiable (Anatomical System);breast;lung;liver;mammary gland; superior cervical ganglion;pons;trigeminal ganglion;cingulate cortex; 0.08177 0.16895 0.314179756 72.75300778 1363.98033 6.92972 CYP2AB1P . . . cytochrome P450 family 2 subfamily AB member 1, pseudogene . . . . . . . . . . . CYP2AC1P . . . cytochrome P450 family 2 subfamily AC member 1, pseudogene . . . . . . . . . . . CYP2B6 2.29255534734584e-05 0.909965298380758 0.0900117760657685 cytochrome P450 family 2 subfamily B member 6 FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,4-cineole 2-exo-monooxygenase. {ECO:0000269|PubMed:11695850, ECO:0000269|PubMed:20061448, ECO:0000269|PubMed:21875942, ECO:0000269|PubMed:22909231}.; . TISSUE SPECIFICITY: Expressed in liver, lung and heart right ventricle. {ECO:0000269|PubMed:10768437}.; breast;unclassifiable (Anatomical System);lung;frontal lobe;cartilage;liver;colon;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle;skin; 0.14143 . 2.36468479 98.44302902 618.3877 5.01744 CYP2B7P . . . cytochrome P450 family 2 subfamily B member 7, pseudogene . . . . . . . . . . . CYP2C8 5.35039546572966e-12 0.029367483603007 0.970632516391643 cytochrome P450 family 2 subfamily C member 8 FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. In the epoxidation of arachidonic acid it generates only 14,15- and 11,12-cis-epoxyeicosatrienoic acids. It is the principal enzyme responsible for the metabolism the anti- cancer drug paclitaxel (taxol). {ECO:0000269|PubMed:7574697}.; . . . . 0.04493 0.23256 0.444637294 77.91342298 1030.58739 6.16555 CYP2C9 2.53599347417585e-08 0.153402862226517 0.846597112413548 cytochrome P450 family 2 subfamily C member 9 FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. This enzyme contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S- warfarin, diclofenac, phenytoin, tolbutamide and losartan.; . . unclassifiable (Anatomical System);lung;placenta;liver;colon;spleen;kidney; dorsal root ganglion;medulla oblongata;superior cervical ganglion;pons;atrioventricular node;skin;skeletal muscle;subthalamic nucleus;liver;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion; 0.09184 0.38254 0.312359769 72.71172446 974.45332 6.03706 CYP2C18 5.267291853526e-08 0.227331798673534 0.772668148653548 cytochrome P450 family 2 subfamily C member 18 FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.; . . unclassifiable (Anatomical System);pancreas;lung;endometrium;liver;colon;skeletal muscle; dorsal root ganglion;superior cervical ganglion;liver;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.03976 0.24838 1.177658736 92.77541873 2268.87678 8.81391 CYP2C19 2.53768601148421e-10 0.0397458579431934 0.960254141803038 cytochrome P450 family 2 subfamily C member 19 FUNCTION: Responsible for the metabolism of a number of therapeutic agents such as the anticonvulsant drug S-mephenytoin, omeprazole, proguanil, certain barbiturates, diazepam, propranolol, citalopram and imipramine.; . . . . 0.04990 . 0.714657953 85.81623024 378.83872 4.10454 CYP2C23P . . . cytochrome P450 family 2 subfamily C member 23, pseudogene . . . . . . . . . . . CYP2C56P . . . cytochrome P450 family 2 subfamily C member 56, pseudogene . . . . . . . . . . . CYP2C58P . . . cytochrome P450 family 2 subfamily C member 58, pseudogene . . . . . . . . . . . CYP2C59P . . . cytochrome P450 family 2 subfamily C member 59, pseudogene . . . . . . . . . . . CYP2C60P . . . cytochrome P450 family 2 subfamily C member 60, pseudogene . . . . . . . . . . . CYP2C61P . . . cytochrome P450 family 2 subfamily C member 61, pseudogene . . . . . . . . . . . CYP2C63P . . . cytochrome P450 family 2 subfamily C member 63, pseudogene . . . . . . . . . . . CYP2C64P . . . cytochrome P450 family 2 subfamily C member 64, pseudogene . . . . . . . . . . . CYP2C115P . . . cytochrome P450 family 2 subfamily C member 115, pseudogene . . . . . . . . . . . CYP2D6 9.22645796999686e-10 0.0834520589714334 0.916547940105921 cytochrome P450 family 2 subfamily D member 6 FUNCTION: Responsible for the metabolism of many drugs and environmental chemicals that it oxidizes. It is involved in the metabolism of drugs such as antiarrhythmics, adrenoceptor antagonists, and tricyclic antidepressants. {ECO:0000269|PubMed:16352597}.; . . unclassifiable (Anatomical System);prostate;liver;colon;spleen;skin; . . . 1.765570135 96.76810569 3439.97769 11.26377 CYP2D7 . . . cytochrome P450 family 2 subfamily D member 7 (gene/pseudogene) FUNCTION: May be responsible for the metabolism of many drugs and environmental chemicals that it oxidizes. It may be involved in the metabolism of codeine to morphine (PubMed:15051713). However, another study could not confirm it (PubMed:18838503). {ECO:0000269|PubMed:15051713, ECO:0000269|PubMed:18838503}.; . TISSUE SPECIFICITY: Expressed in brain cortex (at protein level). {ECO:0000269|PubMed:15051713}.; . . . . . . . . CYP2D8P . . . ccytochrome P450 family 2 subfamily D member 8, pseudogene . . . . . . . . . . . CYP2E1 0.265925587444093 0.732944472419924 0.00112994013598323 cytochrome P450 family 2 subfamily E member 1 FUNCTION: Metabolizes several precarcinogens, drugs, and solvents to reactive metabolites. Inactivates a number of drugs and xenobiotics and also bioactivates many xenobiotic substrates to their hepatotoxic or carcinogenic forms.; . . unclassifiable (Anatomical System);lung;ovary;bone;placenta;liver;parathyroid;spinal ganglion;brain;thymus; superior cervical ganglion;liver;appendix;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.63417 . -0.288341872 33.41589998 623.57339 5.03651 CYP2F1 2.75609758938668e-05 0.771523766047892 0.228448672976214 cytochrome P450 family 2 subfamily F member 1 FUNCTION: May be involved in the metabolism of various pneumotoxicants including naphthalene. Is able to dealkylate ethoxycoumarin, propoxycoumarin, and pentoxyresorufin but possesses no activity toward ethoxyresorufin and only trace dearylation activity toward benzyloxyresorufin. Bioactivates 3- methylindole (3MI) by dehydrogenation to the putative electrophile 3-methylene-indolenine. {ECO:0000269|PubMed:1974816}.; . TISSUE SPECIFICITY: Expressed in lung. Rarely detected in liver and placenta. {ECO:0000269|PubMed:1974816, ECO:0000269|PubMed:8619884}.; uterus;prostate;lung;brain; . . . 1.003094668 90.77022883 5472.61938 15.24169 CYP2F2P . . . cytochrome P450 family 2 subfamily F member 2, pseudogene . . . . . . . . . . . CYP2G1P . . . cytochrome P450 family 2 subfamily G member 1, pseudogene . . . . . 0.16154 . . . . . CYP2G2P . . . cytochrome P450 family 2 subfamily G member 2, pseudogene . . . . . . . . . . . CYP2J2 4.51201698997771e-12 0.0265917395396382 0.97340826045585 cytochrome P450 family 2 subfamily J member 2 FUNCTION: This enzyme metabolizes arachidonic acid predominantly via a NADPH-dependent olefin epoxidation to all four regioisomeric cis-epoxyeicosatrienoic acids. One of the predominant enzymes responsible for the epoxidation of endogenous cardiac arachidonic acid pools.; . TISSUE SPECIFICITY: Highly expressed in heart, present at lower levels in liver, ileum, jejunum, colon, and kidney.; . . 0.05001 0.23313 -0.666770504 15.86459071 85.87178 1.97903 CYP2R1 3.05144607991638e-09 0.162746601932225 0.837253395016329 cytochrome P450 family 2 subfamily R member 1 FUNCTION: Has a D-25-hydroxylase activity on both forms of vitamin D, vitamin D(2) and D(3). {ECO:0000269|PubMed:12867411, ECO:0000269|PubMed:15465040, ECO:0000269|PubMed:18511070}.; DISEASE: Rickets vitamin D-dependent 1B (VDDR1B) [MIM:600081]: A disorder caused by a selective deficiency of the active form of vitamin D (1,25-dihydroxyvitamin D3) and resulting in defective bone mineralization and clinical features of rickets. The patients sera have low calcium concentrations, low phosphate concentrations, elevated alkaline phosphatase activity and low levels of 25-hydroxyvitamin D. {ECO:0000269|PubMed:15128933}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;tongue;islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis - interstitial;globus pallidus;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.12596 0.18924 -0.091746757 46.91554612 52.88849 1.44236 CYP2S1 0.000914984181302337 0.939999535348766 0.0590854804699316 cytochrome P450 family 2 subfamily S member 1 FUNCTION: Has a potential importance for extrahepatic xenobiotic metabolism.; . TISSUE SPECIFICITY: High level of expression in trachea, lung, stomach, small intestine, and spleen. {ECO:0000269|PubMed:11181079}.; unclassifiable (Anatomical System);trophoblast;cartilage;ovary;heart;colon;prostate;lung;larynx;epididymis;nasopharynx;thyroid;liver;testis;head and neck;kidney;stomach; . 0.18001 . 0.04598748 57.47817882 205.7081 3.09868 CYP2T1P . . . cytochrome P450 family 2 subfamily T member 1, pseudogene . . . . . . . . . . . CYP2T3P . . . cytochrome P450 family 2 subfamily T member 3, pseudogene . . . . . . . . . . . CYP2U1 0.0817830150318557 0.907871346787207 0.0103456381809376 cytochrome P450 family 2 subfamily U member 1 FUNCTION: Catalyzes the hydroxylation of arachidonic acid, docosahexaenoic acid and other long chain fatty acids. May modulate the arachidonic acid signaling pathway and play a role in other fatty acid signaling processes. {ECO:0000269|PubMed:14660610}.; DISEASE: Spastic paraplegia 56, autosomal recessive (SPG56) [MIM:615030]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. Complicated forms are recognized by additional variable features including spastic quadriparesis, seizures, dementia, amyotrophy, extrapyramidal disturbance, cerebral or cerebellar atrophy, optic atrophy, and peripheral neuropathy, as well as by extra neurological manifestations. In SPG56, upper limbs are often also affected. Some SPG56 patients may have a subclinical axonal neuropathy. {ECO:0000269|PubMed:23176821}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed with stronger expression in thymus, heart and cerebellum. {ECO:0000269|PubMed:14660610, ECO:0000269|PubMed:14975754, ECO:0000269|PubMed:15752708}.; unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;whole body;lung;endometrium;macula lutea;iris;testis;germinal center;kidney;brain;stomach;thymus; . 0.19989 0.16777 -0.091746757 46.91554612 53.71136 1.46035 CYP2W1 0.000980916281960337 0.813303503744938 0.185715579973102 cytochrome P450 family 2 subfamily W member 1 FUNCTION: Seems to have broad catalytic activity towards several chemicals, including polycyclic aromatic hydrocarbon dihydrodiols and aromatic amines (PubMed:16551781, PubMed:24278521). Active also in the metabolism of indoline substrates and is able to activate aflatoxin B1 into cytotoxic products (PubMed:20805301). Furthermore, it seems to be involved in the oxydation of lysophospholipids and fatty acids (PubMed:22591743). {ECO:0000269|PubMed:16551781, ECO:0000269|PubMed:20805301, ECO:0000269|PubMed:22591743, ECO:0000269|PubMed:24278521}.; . TISSUE SPECIFICITY: Very low levels are detected in fetal and adult tissues. Highly expressed in several tumor samples, in particular colon and adrenal tumors. {ECO:0000269|PubMed:16426568}.; unclassifiable (Anatomical System);lung;placenta;spleen;head and neck;stomach; skeletal muscle; 0.04973 0.15458 0.53464283 81.00967209 1243.09175 6.65806 CYP3A4 2.81509485996385e-07 0.745621874120896 0.254377844369618 cytochrome P450 family 3 subfamily A member 4 FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It performs a variety of oxidation reactions (e.g. caffeine 8-oxidation, omeprazole sulphoxidation, midazolam 1'-hydroxylation and midazolam 4- hydroxylation) of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,8-cineole 2- exo-monooxygenase. The enzyme also hydroxylates etoposide (PubMed:11159812). Catalyzes 4-beta-hydroxylation of cholesterol. May catalyze 25-hydroxylation of cholesterol in vitro (PubMed:21576599). {ECO:0000269|PubMed:11159812, ECO:0000269|PubMed:21576599}.; . TISSUE SPECIFICITY: Expressed in prostate and liver. According to some authors, it is not expressed in brain (PubMed:19094056). According to others, weak levels of expression are measured in some brain locations (PubMed:19359404 and PubMed:18545703). Also expressed in epithelium of the small intestine and large intestine, bile duct, nasal mucosa, kidney, adrenal cortex, epithelium of the gastric mucosa with intestinal metaplasia, gallbladder, intercalated ducts of the pancreas, chief cells of the parathyroid and the corpus luteum of the ovary (at protein level). {ECO:0000269|PubMed:18545703, ECO:0000269|PubMed:19094056, ECO:0000269|PubMed:19359404, ECO:0000269|PubMed:2732228, ECO:0000269|PubMed:7894497, ECO:0000269|PubMed:8035341}.; unclassifiable (Anatomical System);small intestine;liver;kidney;gall bladder; dorsal root ganglion;superior cervical ganglion;fetal liver;temporal lobe;liver;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.06948 0.58179 -0.488577883 22.64685067 83.02614 1.93581 CYP3A5 5.21037691769514e-11 0.108487591322396 0.8915124086255 cytochrome P450 family 3 subfamily A member 5 FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;blood;skeletal muscle;uterus;lung;placenta;liver;spleen;kidney;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skin; 0.03790 . -0.179930907 40.35739561 283.75653 3.60528 CYP3A7 2.92836029852247e-07 0.753441992354036 0.246557714809935 cytochrome P450 family 3 subfamily A member 7 FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.; . . unclassifiable (Anatomical System);uterus;lung;whole body;small intestine;heart;liver;testis;spleen;kidney;skin; dorsal root ganglion;fetal liver;superior cervical ganglion;liver;ciliary ganglion;fetal lung;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18020 0.20186 -0.314027422 31.9297004 37.42706 1.11486 CYP3A7-CYP3A51P . . . CYP3A7-CYP3A51P readthrough FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.; . . . . . . . . . . CYP3A43 1.47487370812895e-10 0.192367584117598 0.807632415734914 cytochrome P450 family 3 subfamily A member 43 FUNCTION: Exhibits low testosterone 6-beta-hydroxylase activity.; . TISSUE SPECIFICITY: Highest expression level in prostate. Also expressed in liver, kidney, pancreas, fetal liver and fetal skeletal muscle. {ECO:0000269|PubMed:11160876, ECO:0000269|PubMed:11243885}.; unclassifiable (Anatomical System);lung;testis; dorsal root ganglion;superior cervical ganglion;fetal liver;uterus corpus;liver;testis;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.12321 0.15336 0.755110637 86.7539514 2984.14721 10.36776 CYP3A51P . . . cytochrome P450 family 3 subfamily A member 51, pseudogene . . . . . . . . . . . CYP3A52P . . . cytochrome P450 family 3 subfamily A member 52, pseudogene . . . . . . . . . . . CYP3A54P . . . cytochrome P450 family 3 subfamily A member 54, pseudogene . . . . . . . . . . . CYP3A137P . . . cytochrome P450 family 3 subfamily A member 137, pseudogene . . . . . . . . . . . CYP4A11 1.57399320908396e-15 0.0065279364796459 0.993472063520353 cytochrome P450 family 4 subfamily A member 11 FUNCTION: Catalyzes the omega- and (omega-1)-hydroxylation of various fatty acids such as laurate, myristate and palmitate. Has little activity toward prostaglandins A1 and E1. Oxidizes arachidonic acid to 20-hydroxyeicosatetraenoic acid (20-HETE). {ECO:0000269|PubMed:15611369, ECO:0000269|PubMed:1739747, ECO:0000269|PubMed:7679927}.; . TISSUE SPECIFICITY: Kidney and liver. {ECO:0000269|PubMed:7679927}.; unclassifiable (Anatomical System);liver;colon;spleen;kidney;stomach; fetal liver;superior cervical ganglion;liver;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion; 0.23562 0.49739 0.225995239 68.51851852 1328.31098 6.85158 CYP4A22 1.4221825850504e-08 0.583397923395702 0.416602062382472 cytochrome P450 family 4 subfamily A member 22 FUNCTION: Catalyzes the omega- and (omega-1)-hydroxylation of various fatty acids such as laurate and palmitate. Shows no activity towards arachidonic acid and prostaglandin A1. Lacks functional activity in the kidney and does not contribute to renal 20-hydroxyeicosatetraenoic acid (20-HETE) biosynthesis. {ECO:0000269|PubMed:10860550, ECO:0000269|PubMed:15611369}.; . . unclassifiable (Anatomical System);liver;colon;spleen;kidney;stomach; . 0.28066 0.18241 3.202967632 99.35126209 9392.57383 20.98200 CYP4A22-AS1 . . . CYP4A22 antisense RNA 1 . . . . . . . . . . . CYP4A26P . . . cytochrome P450 family 4 subfamily A member 26, pseudogene . . . . . . . . . . . CYP4A27P . . . cytochrome P450 family 4 subfamily A member 27, pseudogene . . . . . . . . . . . CYP4A43P . . . cytochrome P450 family 4 subfamily A member 43, pseudogene . . . . . . . . . . . CYP4A44P . . . cytochrome P450 family 4 subfamily A member 44, pseudogene . . . . . . . . . . . CYP4B1 5.37386386780508e-10 0.115250306457166 0.884749693005448 cytochrome P450 family 4 subfamily B member 1 FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.; . TISSUE SPECIFICITY: Detected in the liver and lung (at protein level). {ECO:0000269|PubMed:12695542}.; unclassifiable (Anatomical System);heart;ovary;cartilage;skin;retina;uterus;prostate;lung;cerebral cortex;nasopharynx;placenta;testis;spinal ganglion;bladder;brain; dorsal root ganglion;trachea;atrioventricular node;trigeminal ganglion; 0.06881 0.24194 2.134974852 97.94762916 9722.09998 21.42105 CYP4F2 3.52044589215636e-11 0.086949617359787 0.913050382605008 cytochrome P450 family 4 subfamily F member 2 FUNCTION: Omega-hydroxylase that oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids and xenobiotics. Plays a key role in vitamin K catabolism by mediating omega-hydroxylation of vitamin K1 (phylloquinone), and menaquinone-4 (MK-4), a form of vitamin K2. Hydroxylation of phylloquinone and MK-4 probably regulates blood coagulation (PubMed:19297519, PubMed:24138531). Also shows arachidonic acid omega-hydroxylase activity in kidney, by mediating conversion of arachidonic acid to 20-hydroxyeicosatetraenoic acid (20-HETE), possibly influencing blood pressure control (PubMed:10660572, PubMed:17341693, PubMed:18574070). Also acts as a leukotriene-B(4) omega-hydroxylase by mediating conversion of leukotriene-B(4) (LTB4) to its omega-hydroxylated metabolite 20-hydroxyleukotriene- B(4) (20-OH LTB4) (PubMed:8026587, PubMed:9799565). {ECO:0000269|PubMed:10660572, ECO:0000269|PubMed:17341693, ECO:0000269|PubMed:18574070, ECO:0000269|PubMed:19297519, ECO:0000269|PubMed:24138531, ECO:0000269|PubMed:8026587, ECO:0000269|PubMed:9799565}.; . TISSUE SPECIFICITY: Liver. Also present in kidney: specifically expressed in the S2 and S3 segments of proximal tubules in cortex and outer medulla (PubMed:10660572). {ECO:0000269|PubMed:10492403, ECO:0000269|PubMed:10660572}.; unclassifiable (Anatomical System);prostate;lung;small intestine;islets of Langerhans;bone;liver;testis;blood;kidney;skeletal muscle;bone marrow; superior cervical ganglion;liver;kidney;atrioventricular node;skeletal muscle;bone marrow; 0.09610 0.21256 0.271907863 70.73012503 3587.43946 11.59385 CYP4F3 6.83107684815361e-14 0.00841483781273387 0.991585162187198 cytochrome P450 family 4 subfamily F member 3 FUNCTION: Isoform CYP4F3A: Catalyzes the omega-hydroxylation of leukotriene-B(4), a potent chemoattractant for polymorphonuclear leukocytes, it has low activity for arachidonic acid. {ECO:0000269|PubMed:11461919, ECO:0000269|PubMed:8486631}.; . TISSUE SPECIFICITY: Isoform CYP4F3A is expressed in the polymorphonuclear leukocytes as well as leukocytes and bone marrow. Isoform CYP4F3B is selectively expressed in liver and kidney and is also the predominant CYP4F isoform in trachea and tissues of the gastrointestinal tract. {ECO:0000269|PubMed:11461919}.; unclassifiable (Anatomical System);lung;small intestine;islets of Langerhans;bone;liver;blood;kidney;skeletal muscle;bone marrow; . 0.43878 . 0.251682437 69.69214437 756.59048 5.45157 CYP4F8 . . . cytochrome P450 family 4 subfamily F member 8 FUNCTION: Hydroxylates arachidonic acid (20:4n-6) to (18R)- hydroxyarachidonate. Shows little activity against prostaglandin (PG) D2, PGE1, PGE2, PGF2alpha, and leukotriene B4. Catalyzes omega-2 and omega-3-hydroxylation of PGH1 and PGH2. Catalyzes epoxidation of 4,7,10,13,16,19-(Z)-docosahexaenoic acid (22:6n-3) and 7,10,13,16,19-(Z)-docosapentaenoic acid (22:5n-3) and omega-3- hydroxylation of 4,7,10,13,16-(Z)-docosapentaenoic acid (22:5n-6). Catalyzes hydroxylation of PGI2 and carbaprostacyclin. {ECO:0000269|PubMed:10791960, ECO:0000269|PubMed:15789615, ECO:0000269|PubMed:16112640}.; . TISSUE SPECIFICITY: Expressed in the epithelium of seminal vesicles, in renal cortex, in adult and fetal liver, in epidermis, in corneal epithelium, in sweat glands, hair follicles, epithelial linings of the ampulla of vas deferens and of the stomach and small intestine, as well as in the transitional epithelium of the bladder and ureter (at protein level). In the epidermis, expressed from the basal cell to the granular cell layers. In the corneal epithelium, expressed in all cell layers. Also detected in prostate. Up-regulated in the epidermis of psoriatic lesions. {ECO:0000269|PubMed:10405341, ECO:0000269|PubMed:12464258, ECO:0000269|PubMed:15789615}.; prostate;skin; dorsal root ganglion;prostate;superior cervical ganglion;adrenal cortex;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.35416 0.13946 . . . . CYP4F9P . . . cytochrome P450 family 4 subfamily F member 9, pseudogene . . . . . . . . . . . CYP4F10P . . . cytochrome P450 family 4 subfamily F member 10, pseudogene . . . . . . . . . . . CYP4F11 8.07506373684772e-15 0.00887321890490523 0.991126781095087 cytochrome P450 family 4 subfamily F member 11 FUNCTION: Omega-hydroxylase that oxidizes a variety of structurally unrelated compounds, including fatty acids and xenobiotics. Plays a key role in vitamin K catabolism by mediating omega-hydroxylation of vitamin K1 (phylloquinone), and menaquinone-4 (MK-4), a form of vitamin K2. Hydroxylation of phylloquinone and MK-4 probably regulates blood coagulation (PubMed:24138531). Catalyzes omega-hydroxylation of 3-hydroxy fatty acids, such as 3-hydroxypalmitate, 3-hydroxyoleate, 3- hydroxyarachidonate, and 3-hydroxystearate (PubMed:18065749, PubMed:19932081). Oxidizes drugs such as erythromycin, benzphetamine, ethylmorphine, chlorpromazine and imipramine (PubMed:15364545). {ECO:0000269|PubMed:15364545, ECO:0000269|PubMed:18065749, ECO:0000269|PubMed:19932081, ECO:0000269|PubMed:24138531}.; . TISSUE SPECIFICITY: Expressed mainly in human liver, followed by kidney, heart, and skeletal muscle. {ECO:0000269|PubMed:10964514, ECO:0000269|PubMed:24138531}.; unclassifiable (Anatomical System);ovary;colon;fovea centralis;choroid;lens;retina;optic nerve;lung;larynx;macula lutea;liver;pituitary gland;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;liver;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.12079 0.13606 -0.637452658 16.73743808 243.35835 3.36648 CYP4F12 1.17932482773986e-09 0.317322174344831 0.682677824475845 cytochrome P450 family 4 subfamily F member 12 FUNCTION: Catalyzes leukotriene B4 omega-hydroxylation and arachidonic acid omega-hydroxylation but with an activity much lower than that of CYP4F2. Catalyzes the hydroxylation of the antihistamine ebastine.; . TISSUE SPECIFICITY: Expressed in small intestine, liver, colon and heart. {ECO:0000269|PubMed:11162607, ECO:0000269|PubMed:11162645}.; unclassifiable (Anatomical System);lung;frontal lobe;cerebral cortex;liver;testis;colon;spleen;kidney;spinal ganglion;stomach; superior cervical ganglion;liver;trigeminal ganglion; 0.12638 0.13897 3.741799815 99.5930644 493.21153 4.56649 CYP4F22 0.000303611080808048 0.986435517462578 0.013260871456614 cytochrome P450 family 4 subfamily F member 22 . DISEASE: Ichthyosis, congenital, autosomal recessive 5 (ARCI5) [MIM:604777]: A form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non-bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs. {ECO:0000269|PubMed:16436457}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;heart;epididymis;skin; atrioventricular node; 0.12249 0.14986 -0.372889896 28.20240623 264.29054 3.48820 CYP4F23P . . . cytochrome P450 family 4 subfamily F member 23, pseudogene . . . . . . . . . . . CYP4F24P . . . cytochrome P450 family 4 subfamily F member 24, pseudogene . . . . . . . . . . . CYP4F25P . . . cytochrome P450 family 4 subfamily F member 25, pseudogene . . . . . . . . . . . CYP4F26P . . . cytochrome P450 family 4 subfamily F member 26, pseudogene . . . . . . . . . . . CYP4F27P . . . cytochrome P450 family 4 subfamily F member 27, pseudogene . . . . . . . . . . . CYP4F29P . . . cytochrome P450 family 4 subfamily F member 29, pseudogene . . . . . . . . . . . CYP4F30P . . . cytochrome P450 family 4 subfamily F member 30, pseudogene . . . . . 0.12963 . . . . . CYP4F31P . . . cytochrome P450 family 4 subfamily F member 31, pseudogene . . . . . . . . . 239.43543 3.34340 CYP4F32P . . . cytochrome P450 family 4 subfamily F member 32, pseudogene . . . . . . . . . . . CYP4F33P . . . cytochrome P450 family 4 subfamily F member 33, pseudogene . . . . . . . . . . . CYP4F34P . . . cytochrome P450 family 4 subfamily F member 34, pseudogene . . . . . . . . . . . CYP4F35P . . . cytochrome P450 family 4 subfamily F member 35, pseudogene . . . . . . . . . . . CYP4F36P . . . cytochrome P450 family 4 subfamily F member 36, pseudogene . . . . . . . . . . . CYP4F44P . . . cytochrome P450 family 4 subfamily F member 44, pseudogene . . . . . . . . . . . CYP4F45P . . . cytochrome P450 family 4 subfamily F member 45, pseudogene . . . . . . . . . . . CYP4F59P . . . cytochrome P450 family 4 subfamily F member 59, pseudogene . . . . . . . . . . . CYP4F60P . . . cytochrome P450 family 4 subfamily F member 60, pseudogene . . . . . . . . . . . CYP4F61P . . . cytochrome P450 family 4 subfamily F member 61, pseudogene . . . . . . . . . . . CYP4F62P . . . cytochrome P450 family 4 subfamily F member 62, pseudogene . . . . . . . . . . . CYP4V2 0.000200713189191236 0.97636788578564 0.0234314010251689 cytochrome P450 family 4 subfamily V member 2 FUNCTION: Omega-hydroxylase that oxidizes medium-chain saturated fatty acids and polyunsaturated omega-3 fatty acids, and which plays a role in fatty acid and steroid metabolism in the eye (PubMed:19661213, PubMed:22772592). Catalyzes the omega- hydroxylation of medium-chain saturated fatty acids such as laurate, myristate and palmitate in an NADPH-dependent pathway. The substrate specificity is higher for myristate > laurate > palmitate (C14>C16>C12) (PubMed:19661213). Acts as a polyunsaturated omega-3 fatty acids hydroxylase by mediating oxidation of docosahexaenoate (DHA) to 22-hydroxydocosahexaenoate (PubMed:22772592). Also produces some 21-hydroxydocosahexaenoate. Also converts eicosapentaenoate (EPA) to 20- hydroxyeicosapentaenoate (20-OH-EPA) (PubMed:22772592). {ECO:0000269|PubMed:19661213, ECO:0000269|PubMed:22772592}.; . TISSUE SPECIFICITY: Broadly expressed. Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, retina, retinal pigment epithelium (RPE) and lymphocytes. {ECO:0000269|PubMed:15042513, ECO:0000269|PubMed:22772592}.; unclassifiable (Anatomical System);uterus;lung;ovary;bone;thyroid;liver;testis;mammary gland;skin; . 0.16962 0.27178 0.42259095 77.22929936 1907.56403 8.04045 CYP4X1 1.72089900913095e-06 0.865623711535244 0.134374567565747 cytochrome P450 family 4 subfamily X member 1 . . TISSUE SPECIFICITY: Expressed in brain, heart and kidney and, at lower levels, in skeletal muscle and liver. In the heart, very high level levels in aorta, but very levels in other heart regions. {ECO:0000269|PubMed:16478468}.; . . 0.04180 . -0.556537043 19.72753008 43.61443 1.25635 CYP4Z1 5.28062048296512e-06 0.86679380244775 0.133200916931767 cytochrome P450 family 4 subfamily Z member 1 . . TISSUE SPECIFICITY: Preferentially detected in breast carcinoma tissue and mammary gland, whereas only marginal expression is found in all other tested tissues. {ECO:0000269|PubMed:15059886}.; unclassifiable (Anatomical System);liver;mammary gland; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.35408 . 0.308721233 72.59966973 136.40042 2.53938 CYP4Z2P . . . cytochrome P450 family 4 subfamily Z member 2, pseudogene . . TISSUE SPECIFICITY: Detected at low levels in mammary gland and mammary carcinoma. {ECO:0000269|PubMed:15059886}.; . . . . . . . . CYP7A1 0.00345536122276857 0.951868547188866 0.0446760915883649 cytochrome P450 family 7 subfamily A member 1 FUNCTION: Catalyzes a rate-limiting step in cholesterol catabolism and bile acid biosynthesis by introducing a hydrophilic moiety at position 7 of cholesterol. Important for cholesterol homeostasis. {ECO:0000269|PubMed:19965590}.; . TISSUE SPECIFICITY: Detected in liver. {ECO:0000269|PubMed:15796896}.; liver; superior cervical ganglion;trigeminal ganglion; 0.72704 0.67187 0.086440867 60.47416844 166.85402 2.82256 CYP7B1 2.13811071901553e-06 0.705028741873861 0.29496912001542 cytochrome P450 family 7 subfamily B member 1 . DISEASE: Congenital bile acid synthesis defect 3 (CBAS3) [MIM:613812]: A disorder resulting in severe cholestasis, cirrhosis and liver synthetic failure. Hepatic microsomal oxysterol 7-alpha-hydroxylase activity is undetectable. {ECO:0000269|PubMed:9802883}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Brain, testis, ovary, prostate, liver, colon, kidney, and small intestine.; unclassifiable (Anatomical System);breast;prostate;lung;colon;kidney;skeletal muscle;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.32142 0.24458 -0.359940251 28.93371078 232.01121 3.29192 CYP8B1 0.00051293164796349 0.687078555123931 0.312408513228106 cytochrome P450 family 8 subfamily B member 1 FUNCTION: Involved in bile acid synthesis and is responsible for the conversion of 7 alpha-hydroxy-4-cholesten-3-one into 7 alpha, 12 alpha-dihydroxy-4-cholesten-3-one. Responsible for the balance between formation of cholic acid and chenodeoxycholic acid. Has a rather broad substrate specificity including a number of 7-alpha- hydroxylated C27 steroids. {ECO:0000250|UniProtKB:O02766}.; . TISSUE SPECIFICITY: Liver.; unclassifiable (Anatomical System);liver; . 0.14098 . -0.398573136 26.92852088 144.68588 2.61981 CYP11A1 6.60264967270784e-09 0.423948634718215 0.576051358679135 cytochrome P450 family 11 subfamily A member 1 FUNCTION: Catalyzes the side-chain cleavage reaction of cholesterol to pregnenolone. {ECO:0000269|PubMed:21636783}.; DISEASE: Adrenal insufficiency, congenital, with 46,XY sex reversal (AICSR) [MIM:613743]: A rare disorder that can present as acute adrenal insufficiency in infancy or childhood. ACTH and plasma renin activity are elevated and adrenal steroids are inappropriately low or absent; the 46,XY patients have female external genitalia, sometimes with clitoromegaly. The phenotypic spectrum ranges from prematurity, complete underandrogenization, and severe early-onset adrenal failure to term birth with clitoromegaly and later-onset adrenal failure. Patients with congenital adrenal insufficiency do not manifest the massive adrenal enlargement typical of congenital lipoid adrenal hyperplasia. {ECO:0000269|PubMed:11502818, ECO:0000269|PubMed:12161514, ECO:0000269|PubMed:16705068, ECO:0000269|PubMed:18182448, ECO:0000269|PubMed:19116240}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;gum;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; superior cervical ganglion;adrenal gland;placenta;adrenal cortex;testis; 0.30797 0.14046 0.020302773 55.60863411 54.70654 1.48122 CYP11B1 0.00143393188162045 0.965481569927714 0.0330844981906657 cytochrome P450 family 11 subfamily B member 1 FUNCTION: Has steroid 11-beta-hydroxylase activity. In addition to this activity, the 18 or 19-hydroxylation of steroids and the aromatization of androstendione to estrone have also been ascribed to cytochrome P450 XIB.; DISEASE: Adrenal hyperplasia 4 (AH4) [MIM:202010]: A form of congenital adrenal hyperplasia, a common recessive disease due to defective synthesis of cortisol. Congenital adrenal hyperplasia is characterized by androgen excess leading to ambiguous genitalia in affected females, rapid somatic growth during childhood in both sexes with premature closure of the epiphyses and short adult stature. Four clinical types: 'salt wasting' (SW, the most severe type), 'simple virilizing' (SV, less severely affected patients), with normal aldosterone biosynthesis, 'non-classic form' or late- onset (NC or LOAH)and 'cryptic' (asymptomatic). {ECO:0000269|PubMed:16046588, ECO:0000269|PubMed:20089618, ECO:0000269|PubMed:2022736, ECO:0000269|PubMed:20331679, ECO:0000269|PubMed:20947076, ECO:0000269|PubMed:23940125, ECO:0000269|PubMed:24022297, ECO:0000269|PubMed:24536089, ECO:0000269|PubMed:26053152, ECO:0000269|PubMed:9302260}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Familial hyperaldosteronism 1 (FH1) [MIM:103900]: A disorder characterized by hypertension, variable hyperaldosteronism, and abnormal adrenal steroid production, including 18-oxocortisol and 18-hydroxycortisol. There is significant phenotypic heterogeneity, and some individuals never develop hypertension. Note=The disease is caused by mutations affecting the gene represented in this entry. The molecular defect causing hyperaldosteronism familial 1 is an anti-Lepore-type fusion of the CYP11B1 and CYP11B2 genes. The hybrid gene has the promoting part of CYP11B1, ACTH-sensitive, and the coding part of CYP11B2.; . unclassifiable (Anatomical System);uterus;medulla oblongata;lung;heart;adrenal gland;placenta;adrenal cortex;testis;mammary gland;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;adrenal gland;adrenal cortex;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.28415 0.24756 -1.194104514 5.850436424 350.77826 3.97064 CYP11B2 3.92718052728051e-13 0.0122245857856654 0.987775414213942 cytochrome P450 family 11 subfamily B member 2 FUNCTION: Preferentially catalyzes the conversion of 11- deoxycorticosterone to aldosterone via corticosterone and 18- hydroxycorticosterone. {ECO:0000269|PubMed:23322723}.; DISEASE: Corticosterone methyloxidase 1 deficiency (CMO-1 deficiency) [MIM:203400]: Autosomal recessive disorder of aldosterone biosynthesis. There are two biochemically different forms of selective aldosterone deficiency be termed corticosterone methyloxidase (CMO) deficiency type 1 and type 2. In CMO-1 deficiency, aldosterone is undetectable in plasma, while its immediate precursor, 18-hydroxycorticosterone, is low or normal. {ECO:0000269|PubMed:11238478, ECO:0000269|PubMed:9177280}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Corticosterone methyloxidase 2 deficiency (CMO-2 deficiency) [MIM:610600]: Autosomal recessive disorder of aldosterone biosynthesis. In CMO-2 deficiency, aldosterone can be low or normal, but at the expense of increased secretion of 18- hydroxycorticosterone. Consequently, patients have a greatly increased ratio of 18-hydroxycorticosterone to aldosterone and a low ratio of corticosterone to 18-hydroxycorticosterone in serum. {ECO:0000269|PubMed:12788848, ECO:0000269|PubMed:1346492, ECO:0000269|PubMed:1594605, ECO:0000269|PubMed:9625333, ECO:0000269|PubMed:9814506}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Familial hyperaldosteronism 1 (FH1) [MIM:103900]: A disorder characterized by hypertension, variable hyperaldosteronism, and abnormal adrenal steroid production, including 18-oxocortisol and 18-hydroxycortisol. There is significant phenotypic heterogeneity, and some individuals never develop hypertension. Note=The disease is caused by mutations affecting the gene represented in this entry. The molecular defect causing hyperaldosteronism familial 1 is an anti-Lepore-type fusion of the CYP11B1 and CYP11B2 genes. The hybrid gene has the promoting part of CYP11B1, ACTH-sensitive, and the coding part of CYP11B2.; . adrenal gland;skeletal muscle; dorsal root ganglion;superior cervical ganglion;adrenal gland;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.45038 0.17204 0.558509856 81.67020524 295.69785 3.67149 CYP17A1 0.0350306078051602 0.956930132145824 0.00803926004901614 cytochrome P450 family 17 subfamily A member 1 FUNCTION: Conversion of pregnenolone and progesterone to their 17- alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved in sexual development during fetal life and at puberty. {ECO:0000269|PubMed:22266943}.; DISEASE: Adrenal hyperplasia 5 (AH5) [MIM:202110]: A form of congenital adrenal hyperplasia, a common recessive disease due to defective synthesis of cortisol. Congenital adrenal hyperplasia is characterized by androgen excess leading to ambiguous genitalia in affected females, rapid somatic growth during childhood in both sexes with premature closure of the epiphyses and short adult stature. Four clinical types: 'salt wasting' (SW, the most severe type), 'simple virilizing' (SV, less severely affected patients), with normal aldosterone biosynthesis, 'non-classic form' or late- onset (NC or LOAH)and 'cryptic' (asymptomatic). {ECO:0000269|PubMed:10720067, ECO:0000269|PubMed:11549685, ECO:0000269|PubMed:11836339, ECO:0000269|PubMed:12466376, ECO:0000269|PubMed:14671162, ECO:0000269|PubMed:1515452, ECO:0000269|PubMed:1714904, ECO:0000269|PubMed:1740503, ECO:0000269|PubMed:19793597, ECO:0000269|PubMed:24140098, ECO:0000269|PubMed:24498484, ECO:0000269|PubMed:25650406, ECO:0000269|PubMed:2808364, ECO:0000269|PubMed:8027220, ECO:0000269|PubMed:8245018, ECO:0000269|PubMed:8345056, ECO:0000269|PubMed:8396144, ECO:0000269|PubMed:8550762, ECO:0000269|Ref.20}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.03631 0.80564 -0.692458599 14.96815287 8.73654 0.32161 CYP17A1-AS1 . . . CYP17A1 antisense RNA 1 . . . . . . . . . . . CYP19A1 0.000559609707897891 0.973091455495645 0.0263489347964575 cytochrome P450 family 19 subfamily A member 1 FUNCTION: Catalyzes the formation of aromatic C18 estrogens from C19 androgens.; DISEASE: Aromatase deficiency (AROD) [MIM:613546]: A rare disease in which fetal androgens are not converted into estrogens due to placental aromatase deficiency. Thus, pregnant women exhibit a hirsutism, which spontaneously resolves after post-partum. At birth, female babies present with pseudohermaphroditism due to virilization of extern genital organs. In adult females, manifestations include delay of puberty, breast hypoplasia and primary amenorrhoea with multicystic ovaries. {ECO:0000269|PubMed:24705274, ECO:0000269|PubMed:8265607, ECO:0000269|PubMed:8530621, ECO:0000269|PubMed:9211678}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Brain, placenta and gonads. {ECO:0000269|PubMed:2040633, ECO:0000269|PubMed:3018730, ECO:0000269|PubMed:7690033, ECO:0000269|PubMed:8117272}.; unclassifiable (Anatomical System);uterus;lung;frontal lobe;heart;placenta;liver;testis;colon;spleen;skin;aorta; dorsal root ganglion;superior cervical ganglion;fetal liver;testis - interstitial;testis - seminiferous tubule;placenta;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.40664 0.85420 -0.556537043 19.72753008 1191.76708 6.54736 CYP20A1 7.40838062967993e-10 0.250664384496871 0.749335614762291 cytochrome P450 family 20 subfamily A member 1 . . . unclassifiable (Anatomical System);lymph node;cartilage;ovary;islets of Langerhans;colon;parathyroid;blood;prostate;lung;adrenal gland;nasopharynx;bone;thyroid;placenta;visual apparatus;liver;testis;head and neck;germinal center;kidney;brain;mammary gland;aorta; testis - interstitial;superior cervical ganglion;white blood cells;trigeminal ganglion;skeletal muscle; 0.17142 0.20477 0.264628794 70.5178108 4123.36118 12.75546 CYP21A1P . . . cytochrome P450 family 21 subfamily A member 1, pseudogene . . . myocardium;ovary;colon;choroid;fovea centralis;retina;uterus;prostate;optic nerve;cerebral cortex;thyroid;testis;brain;spinal ganglion;unclassifiable (Anatomical System);cartilage;adrenal cortex;lens;skeletal muscle;pancreas;lung;adrenal gland;macula lutea;spleen;mammary gland; . . . . . . . CYP21A2 0.672306731067129 0.326675509086934 0.00101775984593676 cytochrome P450 family 21 subfamily A member 2 FUNCTION: Specifically catalyzes the 21-hydroxylation of steroids. Required for the adrenal synthesis of mineralocorticoids and glucocorticoids. {ECO:0000250|UniProtKB:P00191}.; DISEASE: Adrenal hyperplasia 3 (AH3) [MIM:201910]: A form of congenital adrenal hyperplasia, a common recessive disease due to defective synthesis of cortisol. Congenital adrenal hyperplasia is characterized by androgen excess leading to ambiguous genitalia in affected females, rapid somatic growth during childhood in both sexes with premature closure of the epiphyses and short adult stature. Four clinical types: 'salt wasting' (SW, the most severe type), 'simple virilizing' (SV, less severely affected patients), with normal aldosterone biosynthesis, 'non-classic form' or late- onset (NC or LOAH)and 'cryptic' (asymptomatic). {ECO:0000269|PubMed:10051010, ECO:0000269|PubMed:10094562, ECO:0000269|PubMed:10198222, ECO:0000269|PubMed:10364682, ECO:0000269|PubMed:10391209, ECO:0000269|PubMed:10408778, ECO:0000269|PubMed:10408786, ECO:0000269|PubMed:10443693, ECO:0000269|PubMed:10496074, ECO:0000269|PubMed:10720040, ECO:0000269|PubMed:11232002, ECO:0000269|PubMed:11598371, ECO:0000269|PubMed:11600539, ECO:0000269|PubMed:11746135, ECO:0000269|PubMed:12213891, ECO:0000269|PubMed:12222711, ECO:0000269|PubMed:12788866, ECO:0000269|PubMed:12887291, ECO:0000269|PubMed:12915679, ECO:0000269|PubMed:1406699, ECO:0000269|PubMed:1406709, ECO:0000269|PubMed:14676460, ECO:0000269|PubMed:14715874, ECO:0000269|PubMed:1496017, ECO:0000269|PubMed:15110320, ECO:0000269|PubMed:15126570, ECO:0000269|PubMed:16046588, ECO:0000269|PubMed:1644925, ECO:0000269|PubMed:18319307, ECO:0000269|PubMed:18381579, ECO:0000269|PubMed:18445671, ECO:0000269|PubMed:1937474, ECO:0000269|PubMed:20080860, ECO:0000269|PubMed:2072928, ECO:0000269|PubMed:2303461, ECO:0000269|PubMed:3038528, ECO:0000269|PubMed:3257825, ECO:0000269|PubMed:3260007, ECO:0000269|PubMed:3267225, ECO:0000269|PubMed:3497399, ECO:0000269|PubMed:3871526, ECO:0000269|PubMed:7749410, ECO:0000269|PubMed:8478006, ECO:0000269|PubMed:8989258, ECO:0000269|PubMed:9067760, ECO:0000269|PubMed:9187661, ECO:0000269|PubMed:9497336, ECO:0000269|PubMed:9580109}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.27306 0.26404 -0.630196893 16.8141071 2760.21963 9.91382 CYP24A1 3.24300393313511e-10 0.161321081256175 0.838678918419525 cytochrome P450 family 24 subfamily A member 1 FUNCTION: Has a role in maintaining calcium homeostasis. Catalyzes the NADPH-dependent 24-hydroxylation of calcidiol (25- hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin D(3)). The enzyme can perform up to 6 rounds of hydroxylation of calcitriol leading to calcitroic acid. It also shows 23- hydroxylating activity leading to 1-alpha,25-dihydroxyvitamin D(3)-26,23-lactone as end product.; DISEASE: Hypercalcemia infantile (HCAI) [MIM:143880]: A disorder characterized by abnormally high level of calcium in the blood, failure to thrive, vomiting, dehydration, and nephrocalcinosis. {ECO:0000269|PubMed:21675912}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;prostate;heart;cochlea;liver;colon;cervix;blood;kidney;mammary gland;skin; superior cervical ganglion;atrioventricular node; 0.08814 0.42357 0.023941474 55.75607455 403.59318 4.21272 CYP26A1 6.64311184026187e-05 0.904725852251033 0.0952077166305641 cytochrome P450 family 26 subfamily A member 1 FUNCTION: Plays a key role in retinoic acid metabolism. Acts on retinoids, including all-trans-retinoic acid (RA) and its stereoisomer 9-cis-RA. Capable of both 4-hydroxylation and 18- hydroxylation. Responsible for generation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA.; . TISSUE SPECIFICITY: Highest levels in adult liver, heart, pituitary gland, adrenal gland, placenta and regions of the brain. {ECO:0000269|PubMed:9826557}.; unclassifiable (Anatomical System);ovary;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;endometrium;placenta;thyroid;macula lutea;liver;testis;head and neck;brain;stomach; superior cervical ganglion;fetal brain;pons; 0.43762 . -0.179930907 40.35739561 140.35242 2.58464 CYP26B1 0.954353506649453 0.045522836503049 0.000123656847498005 cytochrome P450 family 26 subfamily B member 1 FUNCTION: Involved in the metabolism of retinoic acid (RA), rendering this classical morphogen inactive through oxidation. Involved in the specific inactivation of all-trans-retinoic acid (all-trans-RA), with a preference for the following substrates: all-trans-RA > 9-cis-RA > 13-cis-RA. Generates several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA, and 18-OH- RA. Esential for postnatal survival. Plays a central role in germ cell development: acts by degrading RA in the developing testis, preventing STRA8 expression, thereby leading to delay of meiosis. Required for the maintenance of the undifferentiated state of male germ cells during embryonic development in Sertoli cells, inducing arrest in G0 phase of the cell cycle and preventing meiotic entry. Plays a role in skeletal development, both at the level of patterning and in the ossification of bone and the establishment of some synovial joints. {ECO:0000269|PubMed:10823918, ECO:0000269|PubMed:22019272}.; DISEASE: Radiohumeral fusions with other skeletal and craniofacial anomalies (RHFCA) [MIM:614416]: A disease characterized by craniofacial malformations, occipital encephalocele, radiohumeral fusions, oligodactyly, advanced osseous maturation, and calvarial mineralization defects. {ECO:0000269|PubMed:22019272}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in brain, particularly in the cerebellum and pons. {ECO:0000269|PubMed:10823918}.; unclassifiable (Anatomical System);ovary;hypothalamus;parathyroid;skeletal muscle;skin;retina;prostate;lung;adrenal gland;placenta;bone;testis;kidney;brain;thymus; whole brain;amygdala;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;cerebellum peduncles;prefrontal cortex;testis;thymus;cerebellum; 0.32002 0.15105 0.001895464 54.03397028 1534.97353 7.27962 CYP26C1 0.0229549008545053 0.912176493000037 0.0648686061454575 cytochrome P450 family 26 subfamily C member 1 FUNCTION: Plays a role in retinoic acid metabolism. Acts on retinoids, including all-trans-retinoic acid (RA) and its stereoisomer 9-cis-RA (preferred substrate).; DISEASE: Focal facial dermal dysplasia 4 (FFDD4) [MIM:614974]: A form of focal facial dermal dysplasia, a group of developmental defects characterized by bitemporal or preauricular skin lesions resembling aplasia cutis congenita. Skin defects occur at the sites of facial fusion during embryogenesis, with temporal lesions situated at the junction between the frontonasal and maxillary facial prominences, and preauricular lesions at the meeting point of the maxillary and mandibular prominences. The ectodermal lesions show consistent histologic abnormalities: atrophy and flattening of the epidermis, replacement of the dermis by loose connective tissue, reduced levels of fragmented elastic tissue and absence of the subcutaneous tissues and adnexal structures. FFDD4 is characterized by isolated, preauricular skin lesions. {ECO:0000269|PubMed:23161670}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in most tissues at very low level. {ECO:0000269|PubMed:14532297}.; brain; . 0.22379 . . . 548.74209 4.76345 CYP27A1 3.89681875061633e-11 0.170975310824856 0.829024689136176 cytochrome P450 family 27 subfamily A member 1 FUNCTION: Catalyzes the first step in the oxidation of the side chain of sterol intermediates; the 27-hydroxylation of 5-beta- cholestane-3-alpha,7-alpha,12-alpha-triol. Has also a vitamin D3- 25-hydroxylase activity.; DISEASE: Cerebrotendinous xanthomatosis (CTX) [MIM:213700]: Rare sterol storage disorder characterized clinically by progressive neurologic dysfunction, premature atherosclerosis, and cataracts. {ECO:0000269|PubMed:12000359, ECO:0000269|PubMed:2019602, ECO:0000269|PubMed:7915755, ECO:0000269|PubMed:9186905, ECO:0000269|PubMed:9790667}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;colon;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;liver;alveolus;spleen;kidney;mammary gland;stomach; liver;kidney; 0.41953 0.44852 -0.306750577 32.23047889 269.5604 3.52205 CYP27B1 3.60155144475408e-06 0.806445691851844 0.193550706596711 cytochrome P450 family 27 subfamily B member 1 FUNCTION: Catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D) plays an important role in normal bone growth, calcium metabolism, and tissue differentiation.; . TISSUE SPECIFICITY: Kidney.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;blood;fovea centralis;choroid;lens;retina;uterus;breast;pancreas;optic nerve;endometrium;bone;placenta;macula lutea;visual apparatus;alveolus;kidney;brain;stomach; superior cervical ganglion;appendix;atrioventricular node;kidney;trigeminal ganglion; 0.09767 0.39937 -0.404032746 26.53338051 111.70148 2.30098 CYP27C1 0.000184566831654872 0.894336172024094 0.105479261144251 cytochrome P450 family 27 subfamily C member 1 . . . unclassifiable (Anatomical System);whole body;larynx;head and neck;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.11749 0.14150 -0.047654689 50.22410946 93.00815 2.07213 CYP39A1 2.01302072315531e-12 0.0317724970287148 0.968227502969272 cytochrome P450 family 39 subfamily A member 1 FUNCTION: Involved in the bile acid metabolism. Has a preference for 24-hydroxycholesterol, and converts it into a 7-alpha- hydroxylated product.; . TISSUE SPECIFICITY: Liver specific.; unclassifiable (Anatomical System);colon;parathyroid;skin;retina;uterus;lung;endometrium;liver;testis;spleen;kidney;stomach; parietal lobe; 0.28519 0.14711 2.175443036 98.06558151 2037.14445 8.31630 CYP46A1 0.754693330684111 0.245219924249617 8.67450662721371e-05 cytochrome P450 family 46 subfamily A member 1 FUNCTION: Involved in the turnover of cholesterol. It converts cholesterol into 24S-hydroxycholesterol and, to a lesser extent, 25-hydroxycholesterol. Has also activity with xenobiotic compounds, such as clotrimazole. {ECO:0000269|PubMed:18621681, ECO:0000269|PubMed:20667828}.; . TISSUE SPECIFICITY: Expressed in brain. The mRNA was broadly distributed with higher levels in gray matter zones and lower levels in regions rich in white matter. Not detected in fetal sample but its expression increases linearly with age.; unclassifiable (Anatomical System);optic nerve;lung;islets of Langerhans;macula lutea;hippocampus;testis;fovea centralis;choroid;lens;brain;retina; whole brain;amygdala;superior cervical ganglion;thalamus;medulla oblongata;occipital lobe;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.15713 0.35070 -0.317668748 31.45789101 37.47727 1.11543 CYP46A4P . . . cytochrome P450 family 46 subfamily A member 4, pseudogene . . . . . . . . . . . CYP51A1 9.85961120147983e-06 0.787432953430201 0.212557186958598 cytochrome P450 family 51 subfamily A member 1 FUNCTION: Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. {ECO:0000269|PubMed:20149798}.; . TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in testis, ovary, adrenal, prostate, liver, kidney and lung. {ECO:0000269|PubMed:8619637}.; smooth muscle;ovary;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;amygdala;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;amnion;head and neck;kidney;stomach; fetal liver; 0.33957 . -0.402212257 26.7338995 73.36532 1.78954 CYP51A1-AS1 . . . CYP51A1 antisense RNA 1 . . . . . . . . . . . CYP51A1P1 . . . cytochrome P450 family 51 subfamily A member 1 pseudogene 1 . . . . . . . . . . . CYP51A1P2 . . . cytochrome P450 family 51 subfamily A member 1 pseudogene 2 . . . . . . . . . . . CYP51A1P3 . . . cytochrome P450 family 51 subfamily A member 1 pseudogene 3 . . . . . . . . . . . CYR61 0.882250775888852 0.117467322924289 0.000281901186859546 cysteine rich angiogenic inducer 61 FUNCTION: Promotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up- regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix remodeling including VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and integrins alpha-3 and alpha-5. CYR61-mediated gene regulation is dependent on heparin-binding. Down-regulates the expression of alpha-1 and alpha-2 subunits of collagen type-1. Promotes cell adhesion and adhesive signaling through integrin alpha-6/beta-1, cell migration through integrin alpha-v/beta-5 and cell proliferation through integrin alpha-v/beta-3. {ECO:0000269|PubMed:11584015}.; . . myocardium;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; uterus;lung;adipose tissue;smooth muscle;thyroid;appendix;ciliary ganglion;atrioventricular node; 0.53533 0.78663 -0.115612493 45.12856806 41.25617 1.20593 CYS1 0.00331532008626381 0.381106381342607 0.61557829857113 cystin 1 . . TISSUE SPECIFICITY: Expressed at high levels in the kidney and pancreas. Moderate expression seen in the skeletal muscle, liver and heart. A weak expression seen in the brain, lung, uterus, prostate, testis, small intestine and colon.; . . 0.19191 0.18811 . . 1416.40595 7.03501 CYSLTR1 0.00432046248282026 0.430223941239784 0.565455596277396 cysteinyl leukotriene receptor 1 FUNCTION: Receptor for cysteinyl leukotrienes mediating bronchoconstriction of individuals with and without asthma. Stimulation by LTD4 results in the contraction and proliferation of smooth muscle, edema, eosinophil migration and damage to the mucus layer in the lung. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. The rank order of affinities for the leukotrienes is LTD4 >> LTE4 = LTC4 >> LTB4.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in spleen and peripheral blood leukocytes. Lower expression in several tissues, such as lung (mostly in smooth muscle bundles and alveolar macrophages), placenta, small intestine, pancreas, colon and heart.; . . 0.15646 0.15770 -0.227663163 37.11370606 14.03355 0.50900 CYSLTR2 0.00155402110804489 0.448565643431618 0.549880335460338 cysteinyl leukotriene receptor 2 FUNCTION: Receptor for cysteinyl leukotrienes. The response is mediated via a G-protein that activates a phosphatidylinositol- calcium second messenger system. Stimulation by BAY u9773, a partial agonist, induces specific contractions of pulmonary veins and might also have an indirect role in the relaxation of the pulmonary vascular endothelium. The rank order of affinities for the leukotrienes is LTC4 = LTD4 >> LTE4.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in the heart, placenta, spleen, peripheral blood leukocytes and adrenal gland. In lung, expressed in the interstitial macrophages, and slightly in smooth muscle cells.; unclassifiable (Anatomical System);kidney; dorsal root ganglion;superior cervical ganglion;globus pallidus;trigeminal ganglion; 0.13496 0.10177 1.306318795 93.99622552 202.35008 3.06887 CYSRT1 . . . cysteine rich tail 1 . . . . . . . 0.189398298 66.31870724 . . CYSTM1 0.284309259662413 0.629991711611033 0.0856990287265531 cysteine rich transmembrane module containing 1 . . . . . 0.14434 . -0.053113545 49.38664779 9.39557 0.34583 CYTH1 0.994541234354466 0.00545863111038715 1.34535146582863e-07 cytohesin 1 FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF5. Promotes the activation of ARF factors through replacement of GDP with GTP. {ECO:0000269|PubMed:10652308, ECO:0000269|PubMed:9653114}.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;ovary;salivary gland;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;peripheral nerve;cerebellum; white blood cells;atrioventricular node;pons;whole blood;cingulate cortex; 0.23088 0.21602 -0.53631094 20.53550366 88.28035 2.01349 CYTH2 0.863501033367183 0.136481811753342 1.7154879474469e-05 cytohesin 2 FUNCTION: Acts as a guanine-nucleotide exchange factor (GEF). Promotes guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. The cell membrane form, in association with ARL4 proteins, recruits ARF6 to the plasma membrane. Involved in neurite growth (By similarity). {ECO:0000250|UniProtKB:P63034, ECO:0000269|PubMed:17398095}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000305|PubMed:9417041}.; medulla oblongata;ovary;colon;parathyroid;skin;uterus;prostate;endometrium;bone;pituitary gland;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;cervix;kidney;nose;mammary gland;stomach; superior cervical ganglion;testis - interstitial;heart;testis - seminiferous tubule;testis; 0.62410 0.15491 -0.648365105 16.35999056 9.22828 0.33790 CYTH3 0.356369422651745 0.643090878192107 0.000539699156148061 cytohesin 3 FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. {ECO:0000269|PubMed:23940353, ECO:0000269|PubMed:9707577}.; . TISSUE SPECIFICITY: Almost absent from liver, thymus and peripheral blood lymphocytes.; medulla oblongata;ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;testis;ciliary body;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;alveolus;kidney;stomach;aorta; superior cervical ganglion;placenta;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.12766 0.14626 -0.538132194 20.26421326 22.98729 0.76613 CYTH4 0.572494881980175 0.427404109515981 0.000101008503844123 cytohesin 4 FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF5. Promotes the activation of ARF factors through replacement of GDP with GTP. {ECO:0000269|PubMed:10652308}.; . TISSUE SPECIFICITY: Expressed predominantly in peripheral blood leukocytes. {ECO:0000269|PubMed:10652308}.; colon;choroid;skin;retina;bone marrow;uterus;endometrium;bone;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;tongue;blood;skeletal muscle;pancreas;lung;epididymis;placenta;liver;spleen;head and neck;kidney;mammary gland;thymus; superior cervical ganglion;white blood cells;whole blood;skeletal muscle; 0.24327 0.12192 0.086440867 60.47416844 260.30767 3.46595 CYTIP 0.0487986718847789 0.946340151418333 0.00486117669688809 cytohesin 1 interacting protein FUNCTION: By its binding to cytohesin-1 (CYTH1), it modifies activation of ARFs by CYTH1 and its precise function may be to sequester CYTH1 in the cytoplasm.; . TISSUE SPECIFICITY: Expressed in lymph nodes, thymus, spleen, lung, peripheral blood leukocytes and bone marrow. {ECO:0000269|PubMed:11867758, ECO:0000269|PubMed:12606567}.; medulla oblongata;ovary;colon;skin;bone marrow;uterus;prostate;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;lymph node;heart;cartilage;islets of Langerhans;blood;breast;pancreas;pia mater;lung;nasopharynx;spleen;kidney;stomach;aorta;thymus; superior cervical ganglion;white blood cells;whole blood;trigeminal ganglion; 0.13646 0.12648 -0.736552314 13.93606983 216.25966 3.17689 CYTL1 0.000652770817543667 0.498773741314964 0.500573487867492 cytokine like 1 . . TISSUE SPECIFICITY: Specifically expressed in CD34+ hematopoietic cells. {ECO:0000269|PubMed:10857752}.; cartilage;heart;ovary;colon;parathyroid;skin;uterus;pancreas;whole body;lung;frontal lobe;trabecular meshwork;bone;placenta;liver;spleen;kidney;brain;tonsil;stomach; trachea;skeletal muscle; 0.33340 0.17319 0.25917371 70.05779665 207.71809 3.11276 CYYR1 0.0344265894425975 0.825218417163809 0.140354993393594 cysteine/tyrosine-rich 1 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12036297, ECO:0000269|PubMed:17442112}.; unclassifiable (Anatomical System);meninges;cartilage;heart;ovary;islets of Langerhans;parathyroid;skin;retina;uterus;pia mater;whole body;lung;adrenal gland;placenta;thyroid;liver;testis;dura mater;kidney;brain;mammary gland;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.23179 0.09285 0.72761005 86.08162302 73.32085 1.78887 CYYR1-AS1 . . . cysteine/tyrosine-rich 1 antisense RNA 1 . . . . . . . . . . . D2HGDH 0.000752024031447155 0.924125441676968 0.0751225342915842 D-2-hydroxyglutarate dehydrogenase FUNCTION: Catalyzes the oxidation of D-2-hydroxyglutarate to alpha-ketoglutarate. {ECO:0000269|PubMed:15070399}.; DISEASE: D-2-hydroxyglutaric aciduria 1 (D2HGA1) [MIM:600721]: A rare recessive neurometabolic disorder causing developmental delay, epilepsy, hypotonia, and dysmorphic features. Both a mild and a severe phenotype exist. The severe phenotype is homogeneous and is characterized by early infantile-onset epileptic encephalopathy and cardiomyopathy. The mild phenotype has a more variable clinical presentation. Diagnosis is based on the presence of an excess of D-2-hydroxyglutaric acid in the urine. {ECO:0000269|PubMed:15609246, ECO:0000269|PubMed:16037974, ECO:0000269|PubMed:16081310}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;ovary;blood;fovea centralis;choroid;lens;skin;skeletal muscle;retina;bone marrow;uterus;pancreas;prostate;optic nerve;lung;placenta;thyroid;macula lutea;hippocampus;kidney;brain;stomach; ciliary ganglion; 0.26124 0.14201 -0.064242613 48.844067 3330.39707 11.04086 DAAM1 0.999990849460485 9.15053951398347e-06 9.47619433523742e-16 dishevelled associated activator of morphogenesis 1 FUNCTION: Binds to disheveled (Dvl) and Rho, and mediates Wnt- induced Dvl-Rho complex formation. May play a role as a scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby enhancing Rho-GTP formation. Can direct nucleation and elongation of new actin filaments. {ECO:0000269|PubMed:16630611, ECO:0000269|PubMed:17482208}.; . TISSUE SPECIFICITY: Expressed in all tissues examined.; ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;atrium;cerebral cortex;bone;thyroid;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;oral cavity;spinal cord;adrenal cortex;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.80371 0.12758 -1.550537744 3.249587167 138.50311 2.56335 DAAM2 0.998285962155217 0.00171403751872177 3.26060697444719e-10 dishevelled associated activator of morphogenesis 2 . . TISSUE SPECIFICITY: Expressed in most tissues examined.; ovary;salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;spinal cord;adrenal cortex;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;thymus; whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;olfactory bulb;hypothalamus;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.20558 0.13948 0.036678689 56.26916726 396.35609 4.18295 DAB1 0.98140856728469 0.0185908836754986 5.49039811986908e-07 Dab, reelin signal transducer, homolog 1 (Drosophila) FUNCTION: Adapter molecule functioning in neural development. May regulate SIAH1 activity (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);frontal lobe;lens; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;skeletal muscle;cerebellum; 0.58894 0.16520 -0.023789244 52.09365416 185.20293 2.95645 DAB1-AS1 . . . DAB1 antisense RNA 1 . . . . . . . . . . . DAB2 0.980417113899471 0.019582262088025 6.24012503836098e-07 Dab, mitogen-responsive phosphoprotein, homolog 2 (Drosophila) FUNCTION: Adapter protein that functions as clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containg non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor- mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin- mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr- 419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. May act as a tumor suppressor. {ECO:0000269|PubMed:11387212, ECO:0000269|PubMed:12805222, ECO:0000269|PubMed:16267015, ECO:0000269|PubMed:16984970, ECO:0000269|PubMed:19306879, ECO:0000269|PubMed:21995445, ECO:0000269|PubMed:22323290, ECO:0000269|PubMed:22491013}.; . TISSUE SPECIFICITY: Expressed in deep invaginations, inclusion cysts and the surface epithelial cells of the ovary. Also expressed in breast epithelial cells, spleen, thymus, prostate, testis, macrophages, fibroblasts, lung epithelial cells, placenta, brain stem, heart and small intestine. Expressed in kidney proximal tubular epithelial cells (at protein level). {ECO:0000269|PubMed:10340382, ECO:0000269|PubMed:15134832, ECO:0000269|PubMed:9620555}.; smooth muscle;ovary;skin;bone marrow;retina;optic nerve;frontal lobe;cochlea;endometrium;brain;gall bladder;heart;cartilage;nervous;urinary;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;mesenchyma;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta; . 0.32690 0.31917 1.047190339 91.34229771 1357.85913 6.91441 DAB2IP 0.999652087746425 0.00034791209014624 1.63428511932932e-10 DAB2 interacting protein FUNCTION: Functions as a scaffold protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Involved in several processes such as innate immune response, inflammation and cell growth inhibition, apoptosis, cell survival, angiogenesis, cell migration and maturation. Plays also a role in cell cycle checkpoint control; reduces G1 phase cyclin levels resulting in G0/G1 cell cycle arrest. Mediates signal transduction by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF), interferon (IFN) or lipopolysaccharide (LPS). Modulates the balance between phosphatidylinositol 3-kinase (PI3K)-AKT-mediated cell survival and apoptosis stimulated kinase (MAP3K5)-JNK signaling pathways; sequesters both AKT1 and MAP3K5 and counterbalances the activity of each kinase by modulating their phosphorylation status in response to proinflammatory stimuli. Acts as a regulator of the endoplasmic reticulum (ER) unfolded protein response (UPR) pathway; specifically involved in transduction of the ER stress-response to the JNK cascade through ERN1. Mediates TNF-alpha-induced apoptosis activation by facilitating dissociation of inhibitor 14-3-3 from MAP3K5; recruits the PP2A phosphatase complex which dephosphorylates MAP3K5 on 'Ser-966', leading to the dissociation of 13-3-3 proteins and activation of the MAP3K5-JNK signaling pathway in endothelial cells. Mediates also TNF/TRAF2-induced MAP3K5-JNK activation, while it inhibits CHUK-NF-kappa-B signaling. Acts a negative regulator in the IFN-gamma-mediated JAK-STAT signaling cascade by inhibiting smooth muscle cell (VSMCs) proliferation and intimal expansion, and thus, prevents graft arteriosclerosis (GA). Acts as a GTPase-activating protein (GAP) for the ADP ribosylation factor 6 (ARF6) and Ras. Promotes hydrolysis of the ARF6-bound GTP and thus, negatively regulates phosphatidylinositol 4,5- bisphosphate (PIP2)-dependent TLR4-TIRAP-MyD88 and NF-kappa-B signaling pathways in endothelial cells in response to lipopolysaccharides (LPS). Binds specifically to phosphatidylinositol 4-phosphate (PtdIns4P) and phosphatidylinositol 3-phosphate (PtdIns3P). In response to vascular endothelial growth factor (VEGFA), acts as a negative regulator of the VEGFR2-PI3K-mediated angiogenic signaling pathway by inhibiting endothelial cell migration and tube formation. In the developing brain, promotes both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex in a glial-dependent locomotion process. Probable downstream effector of the Reelin signaling pathway; promotes Purkinje cell (PC) dendrites development and formation of cerebellar synapses. Functions also as a tumor suppressor protein in prostate cancer progression; prevents cell proliferation and epithelial-to-mesenchymal transition (EMT) through activation of the glycogen synthase kinase-3 beta (GSK3B)-induced beta-catenin and inhibition of PI3K-AKT and Ras-MAPK survival downstream signaling cascades, respectively. {ECO:0000269|PubMed:12813029, ECO:0000269|PubMed:17389591, ECO:0000269|PubMed:18292600, ECO:0000269|PubMed:19033661, ECO:0000269|PubMed:19903888, ECO:0000269|PubMed:19948740, ECO:0000269|PubMed:20080667, ECO:0000269|PubMed:20154697, ECO:0000269|PubMed:21700930, ECO:0000269|PubMed:22696229}.; DISEASE: Note=A chromosomal aberration involving DAB2IP is found in a patient with acute myeloid leukemia (AML). Translocation t(9;11)(q34;q23) with KMT2A/MLL1. May give rise to a KMT2A/MLL1- DAB2IP fusion protein lacking the PH domain (PubMed:14978793). {ECO:0000269|PubMed:14978793}.; TISSUE SPECIFICITY: Expressed in endothelial and vascular smooth muscle cells (VSMCs). Expressed in prostate epithelial but poorly in prostate cancer cells. Poorly expressed in medulloblastoma cells compared to cerebellar precursor proliferating progenitor cells (at protein level). Low expression in prostate. Down- regulated in prostate cancer. {ECO:0000269|PubMed:11944990, ECO:0000269|PubMed:17389591, ECO:0000269|PubMed:21700930, ECO:0000269|PubMed:22696229}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;optic nerve;endometrium;bone;thyroid;testis;pineal gland;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.49661 0.13993 -1.517642441 3.467799009 1179.95825 6.52137 DACH1 0.995944076016472 0.00405560219215764 3.21791370724204e-07 dachshund family transcription factor 1 FUNCTION: Transcription factor that is involved in regulation of organogenesis. Seems to be a regulator of SIX1, SIX6 and probably SIX5. Corepression of precursor cell proliferation in myoblasts by SIX1 is switched to coactivation through recruitment of EYA3 to the SIX1-DACH1 complex. Transcriptional activation seems also to involve association of CREBBP. Seems to act as a corepressor of SIX6 in regulating proliferation by directly repressing cyclin- dependent kinase inhibitors, including the p27Kip1 promoter (By similarity). Inhibits TGF-beta signaling through interaction with SMAD4 and NCOR1. Binds to chromatin DNA via its DACHbox-N domain (By similarity). {ECO:0000250, ECO:0000269|PubMed:14525983}.; . TISSUE SPECIFICITY: Widely expressed. Isoform 2 is found in brain, heart, kidney, liver, leukocytes and spleen. Isoform 3 is found in liver and heart. Isoform 4 is found in spleen. {ECO:0000269|PubMed:11543628}.; unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;colon;blood;fovea centralis;retina;bone marrow;uterus;lung;placenta;macula lutea;visual apparatus;testis;head and neck;pineal gland; ciliary ganglion;caudate nucleus;trigeminal ganglion; 0.97653 0.18615 -0.979072682 8.752064166 312.33083 3.76030 DACH2 0.859033207333493 0.140513647038414 0.000453145628092625 dachshund family transcription factor 2 FUNCTION: Transcription factor that is involved in regulation of organogenesis. Seems to be a regulator for SIX1 and SIX6. Seems to act as a corepressor of SIX6 in regulating proliferation by directly repressing cyclin-dependent kinase inhibitors, including the p27Kip1 promoter. Is recruited with SIX6 to the p27Kip1 promoter in embryonal retina. SIX6 corepression seems also to involve NCOR1, TBL1, HDAC1 and HDAC3. May be involved together with PAX3, SIX1, and EYA2 in regulation of myogenesis. In the developing somite, expression of DACH2 and PAX3 is regulated by the overlying ectoderm, and DACH2 and PAX3 positively regulate each other's expression (By similarity). Probably binds to DNA via its DACHbox-N domain. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;frontal lobe;islets of Langerhans;hippocampus;testis;kidney;skeletal muscle; globus pallidus;atrioventricular node; 0.22813 0.13144 -0.492218069 22.35786742 49.75098 1.38272 DACOR1 . . . DNMT1-associated colon cancer repressed lncRNA 1 . . . . . . . . . . . DACT1 0.81659755259209 0.183214244323794 0.000188203084115266 dishevelled-binding antagonist of beta-catenin 1 FUNCTION: Involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins. The activation/inhibition of Wnt signaling may depend on the phosphorylation status. Proposed to regulate the degradation of CTNNB1/beta-catenin, thereby modulating the transcriptional activation of target genes of the Wnt signaling pathway. Its function in stabilizing CTNNB1 may involve inhibition of GSK3B activity. Promotes the membrane localization of CTNNB1. The cytoplasmic form can induce DVL2 degradation via a lysosome- dependent mechanism; the function is inhibited by PKA-induced binding to 14-3-3 proteins, such as YWHAB. Seems to be involved in morphogenesis at the primitive streak by regulating VANGL2 and DVL2; the function seems to be independent of canonical Wnt signaling and rather involves the non-canonical Wnt/planar cell polarity (PCP) pathway (By similarity). The nuclear form may prevent the formation of LEF1:CTNNB1 complex and recruit HDAC1 to LEF1 at target gene promoters to repress transcription thus antagonizing Wnt signaling. May be involved in positive regulation of fat cell differentiation. During neuronal differentiation may be involved in excitatory synapse organization, and dendrite formation and establishment of spines. {ECO:0000250, ECO:0000269|PubMed:15580286, ECO:0000269|PubMed:16446366, ECO:0000269|PubMed:17197390, ECO:0000269|PubMed:18936100, ECO:0000269|PubMed:22470507}.; DISEASE: Neural tube defects (NTD) [MIM:182940]: Congenital malformations of the central nervous system and adjacent structures related to defective neural tube closure during the first trimester of pregnancy. Failure of neural tube closure can occur at any level of the embryonic axis. Common NTD forms include anencephaly, myelomeningocele and spina bifida, which result from the failure of fusion in the cranial and spinal region of the neural tube. NTDs have a multifactorial etiology encompassing both genetic and environmental components. {ECO:0000269|PubMed:22610794}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);smooth muscle;lymph node;cartilage;heart;ovary;developmental;colon;parathyroid;skin;retina;uterus;prostate;whole body;lung;cochlea;larynx;thyroid;placenta;visual apparatus;testis;amniotic fluid;head and neck;brain;mammary gland;stomach;thymus; superior cervical ganglion;fetal brain;trigeminal ganglion; 0.15217 0.12544 0.202129237 67.42745931 2431.69074 9.16027 DACT2 . . . dishevelled-binding antagonist of beta-catenin 2 FUNCTION: Involved in regulation of intracellular signaling pathways during development. Negatively regulates the Nodal signaling pathway, possibly by promoting the lysosomal degradation of Nodal receptors, such as TGFBR1. May be involved in control of the morphogenetic behavior of kidney ureteric bud cells by keeping cells epithelial and restraining their mesenchymal character. May play an inhibitory role in the re-epithelialization of skin wounds by attenuating TGF-beta signaling (By similarity). {ECO:0000250}.; . . . . 0.20047 0.11827 1.284269037 93.76621845 1561.73957 7.32136 DACT3 . . . dishevelled-binding antagonist of beta-catenin 3 FUNCTION: May be involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins. {ECO:0000269|PubMed:18538736}.; . . unclassifiable (Anatomical System);uterus;lung;ovary;placenta;iris;colon;parathyroid;brain;thymus; . 0.39043 . . . 70.53679 1.74717 DACT3-AS1 . . . DACT3 antisense RNA 1 . . . . . . . . . . . DAD1 0.276496725647528 0.633196760089802 0.0903065142626706 defender against cell death 1 FUNCTION: Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). Loss of the DAD1 protein triggers apoptosis (By similarity). {ECO:0000250}.; . . myocardium;lymphoreticular;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;olfactory bulb;spinal cord;testis;kidney;trigeminal ganglion; 0.25035 0.15588 -0.09720619 46.20193442 3.98327 0.14725 DAD1P1 . . . defender against cell death 1 pseudogene 1 . . . . . . . . . . . DAG1 0.940921791331691 0.0590301227780706 4.80858902388211e-05 dystroglycan 1 FUNCTION: The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.; FUNCTION: Beta-dystroglycan is a transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity.; DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C9 (MDDGC9) [MIM:613818]: An autosomal recessive muscular dystrophy showing onset in early childhood, and associated with mental retardation without structural brain anomalies. {ECO:0000269|PubMed:21388311}. Note=The disease is caused by mutations affecting the gene represented in this entry. MDDGC7 is caused by DAG1 mutations that interfere with normal post- translational processing, resulting in defective DAG1 glycosylation and impaired interactions with extracellular-matrix components. Other muscular dystrophy-dystroglycanopathies are caused by defects in enzymes involved in protein O-glycosylation.; TISSUE SPECIFICITY: Expressed in a variety of fetal and adult tissues. In epidermal tissue, located to the basement membrane. Also expressed in keratinocytes and fibroblasts. {ECO:0000269|PubMed:15175026, ECO:0000269|PubMed:8268918}.; ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;bone;thyroid;testis;amniotic fluid;brain;bladder;gall bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;lacrimal gland;islets of Langerhans;muscle;adrenal cortex;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;olfactory bulb;placenta;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.31931 0.62512 -0.569494998 19.04340646 208.10701 3.11458 DAGLA 0.953148342492449 0.0468516124363719 4.50711786941352e-08 diacylglycerol lipase alpha FUNCTION: Catalyzes the hydrolysis of diacylglycerol (DAG) to 2- arachidonoyl-glycerol (2-AG), the most abundant endocannabinoid in tissues. Required for axonal growth during development and for retrograde synaptic signaling at mature synapses. {ECO:0000269|PubMed:14610053}.; . TISSUE SPECIFICITY: Highly expressed in brain and pancreas. {ECO:0000269|PubMed:14610053, ECO:0000269|PubMed:16051747}.; unclassifiable (Anatomical System);pancreas;lung;islets of Langerhans;liver;colon;spleen;brain;mammary gland;skin;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.39271 0.11988 -0.573127851 18.96083982 278.59856 3.57787 DAGLB 1.65016137668239e-06 0.96259511835654 0.0374032314820835 diacylglycerol lipase beta FUNCTION: Catalyzes the hydrolysis of diacylglycerol (DAG) to 2- arachidonoyl-glycerol (2-AG), the most abundant endocannabinoid in tissues. Required for axonal growth during development and for retrograde synaptic signaling at mature synapses. {ECO:0000269|PubMed:14610053}.; . . ovary;sympathetic chain;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12004 0.10395 0.033039107 55.85633404 760.30438 5.46562 DALIR . . . DNMT1-associated long intergenic non-coding RNA . . . . . . . . . . . DALRD3 1.84813920683629e-05 0.8852783038147 0.114703214793231 DALR anticodon binding domain containing 3 . . . medulla oblongata;ovary;colon;choroid;skin;retina;bone marrow;uterus;prostate;oesophagus;endometrium;larynx;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;pineal body;muscle;blood;lens;breast;lung;placenta;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;testis;skeletal muscle; 0.77615 0.08752 -0.291981272 33.20358575 21.66294 0.72947 DANCR . . . differentiation antagonizing non-protein coding RNA . . TISSUE SPECIFICITY: Expressed in keratinocytes. {ECO:0000269|PubMed:22302877}.; . . . . . . . . DAND5 1.6833196311109e-05 0.252738096328346 0.747245070475342 DAN domain family member 5, BMP antagonist FUNCTION: Seems to play a role in the correct specification of the left-right axis. May antagonize NODAL and BMP4 signaling. Cystine knot-containing proteins play important roles during development, organogenesis, tissue growth and differentiation (By similarity). {ECO:0000250}.; . . frontal lobe; . 0.10745 0.20281 -0.029247611 51.40363293 16.50617 0.58379 DANT1 . . . DXZ4 associated non-coding transcript 1, proximal . . . . . . . . . . . DANT2 . . . DXZ4 associated non-coding transcript 2, distal . . . . . . . . . . . DAO 9.26248223544675e-15 0.00500059506370519 0.994999404936286 D-amino-acid oxidase FUNCTION: Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D- amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids. {ECO:0000269|PubMed:17303072}.; . . unclassifiable (Anatomical System);optic nerve;cerebellum cortex;macula lutea;spinal cord;liver;fovea centralis;choroid;kidney;lens;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;spinal cord;liver;ciliary ganglion;pons;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.11751 0.17229 -0.624497208 17.16206653 45.53519 1.29627 DAOA 0.00804524559202352 0.78757288617774 0.204381868230237 D-amino acid oxidase activator FUNCTION: Seems to activate D-amino acid oxidase.; . TISSUE SPECIFICITY: Expressed in amygdala, caudate nucleus, spinal cord and testis.; . . 0.03497 . 0.813985927 87.81552253 1137.92758 6.43355 DAOA-AS1 . . . DAOA antisense RNA 1 . . . . . . . . . . . DAP 0.000324904230614164 0.364538036181341 0.635137059588045 death-associated protein FUNCTION: Negative regulator of autophagy. Involved in mediating interferon-gamma-induced cell death. {ECO:0000269|PubMed:20537536}.; . . ovary;salivary gland;developmental;intestine;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;urinary;pharynx;blood;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach;peripheral nerve; liver;kidney; 0.02873 0.07403 0.257356108 69.83368719 80.75027 1.89818 DAP3 1.9076333934558e-05 0.889194292967612 0.110786630698453 death associated protein 3 FUNCTION: Involved in mediating interferon-gamma-induced cell death.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;sympathetic chain;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;bladder;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; beta cell islets;tumor;testis;white blood cells;whole blood;thymus; 0.26291 0.10317 -0.224023033 37.4321774 223.49171 3.23215 DAP3P1 . . . death associated protein 3 pseudogene 1 . . . . . . . . . . . DAP3P2 . . . death associated protein 3 pseudogene 2 . . . . . . . . . . . DAPK1 0.999700496019786 0.000299503980024268 1.90182691427261e-13 death-associated protein kinase 1 FUNCTION: Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell deaths signal, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Phosphorylates PIN1 resulting in inhibition of its catalytic activity, nuclear localization, and cellular function. Phosphorylates TPM1, enhancing stress fiber formation in endothelial cells. Phosphorylates STX1A and significantly decreases its binding to STXBP1. Phosphorylates PRKD1 and regulates JNK signaling by binding and activating PRKD1 under oxidative stress. Phosphorylates BECN1, reducing its interaction with BCL2 and BCL2L1 and promoting the induction of autophagy. Phosphorylates TSC2, disrupting the TSC1-TSC2 complex and stimulating mTORC1 activity in a growth factor-dependent pathway. Phosphorylates RPS6, MYL9 and DAPK3. Acts as a signaling amplifier of NMDA receptors at extrasynaptic sites for mediating brain damage in stroke. Cerebral ischemia recruits DAPK1 into the NMDA receptor complex and it phosphorylates GRINB at Ser-1303 inducing injurious Ca(2+) influx through NMDA receptor channels, resulting in an irreversible neuronal death. Required together with DAPK3 for phosphorylation of RPL13A upon interferon-gamma activation which is causing RPL13A involvement in transcript- selective translation inhibition.; . TISSUE SPECIFICITY: Isoform 2 is expressed in normal intestinal tissue as well as in colorectal carcinomas. {ECO:0000269|PubMed:18422656}.; smooth muscle;ovary;parathyroid;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;kidney;mammary gland;stomach; superior cervical ganglion;placenta;atrioventricular node; 0.18203 0.10544 -1.275066404 5.189903279 778.17701 5.51989 DAPK1-IT1 . . . DAPK1 intronic transcript 1 . . . . . . . . . . . DAPK2 0.000134613269112973 0.852286489084237 0.14757889764665 death-associated protein kinase 2 FUNCTION: Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell death signals, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Acts as a mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation (PubMed:17347302). Regulates granulocytic motility by controlling cell spreading and polarization (PubMed:24163421). {ECO:0000269|PubMed:17347302, ECO:0000269|PubMed:24163421, ECO:0000269|PubMed:26047703}.; . TISSUE SPECIFICITY: Expressed in neutrophils and eosinophils (PubMed:24163421). Isoform 2 is expressed in embryonic stem cells (at protein level). Isoform 1 is ubiquitously expressed in all tissue types examined with high levels in heart, lung and skeletal muscle. {ECO:0000269|PubMed:10376525, ECO:0000269|PubMed:17347302, ECO:0000269|PubMed:21408167, ECO:0000269|PubMed:24163421}.; unclassifiable (Anatomical System);lymph node;lung;frontal lobe;endometrium;thyroid;testis;colon;blood;kidney;brain;mammary gland;stomach;bone marrow; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.44050 0.12876 0.086440867 60.47416844 4082.56767 12.68072 DAPK3 0.0611344951968641 0.922529125536864 0.0163363792662723 death-associated protein kinase 3 FUNCTION: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Involved in the regulation of smooth muscle contraction. Regulates both type I (caspase- dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in regulation of starvation-induced autophagy. Regulates myosin phosphorylation in both smooth muscle and non-muscle cells. In smooth muscle, regulates myosin either directly by phosphorylating MYL12B and MYL9 or through inhibition of smooth muscle myosin phosphatase (SMPP1M) via phosphorylation of PPP1R12A; the inhibition of SMPP1M functions to enhance muscle responsiveness to Ca(2+) and promote a contractile state. Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton. Isoform 2 can phosphorylate myosin, PPP1R12A and MYL12B. Overexpression leads to condensation of actin stress fibers into thick bundles. Involved in actin filament focal adhesion dynamics. The function in both reorganization of actin cytoskeleton and focal adhesion dissolution is modulated by RhoD. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2. Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Involved in regulation of cell cycle progression and cell proliferation. May be a tumor suppressor. {ECO:0000269|PubMed:10356987, ECO:0000269|PubMed:11384979, ECO:0000269|PubMed:11781833, ECO:0000269|PubMed:12917339, ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:15367680, ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:17126281, ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:18084323, ECO:0000269|PubMed:18995835, ECO:0000269|PubMed:21169990, ECO:0000269|PubMed:21408167, ECO:0000269|PubMed:21454679, ECO:0000269|PubMed:21487036, ECO:0000269|PubMed:23454120}.; . TISSUE SPECIFICITY: Widely expressed. Isoform 1 and isoform 2 are expressed in the bladder smooth muscle. {ECO:0000269|PubMed:15292222, ECO:0000269|PubMed:17126281}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;lung;placenta;macula lutea;liver;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.13863 0.25790 -0.780646273 12.77423921 62.98696 1.62376 DAPL1 0.000268262509293928 0.332309351484865 0.667422386005841 death associated protein like 1 FUNCTION: May play a role in the early stages of epithelial differentiation or in apoptosis. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;pineal body;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;thyroid;macula lutea;alveolus;testis;brain; dorsal root ganglion;adrenal gland;thyroid;ciliary ganglion; 0.43721 . 0.725794416 85.98136353 . . DAPP1 0.183493679964267 0.804567475577261 0.0119388444584721 dual adaptor of phosphotyrosine and 3-phosphoinositides FUNCTION: May act as a B-cell-associated adapter that regulates B- cell antigen receptor (BCR)-signaling downstream of PI3K. {ECO:0000269|PubMed:10770799}.; . TISSUE SPECIFICITY: Highly expressed in placenta and lung, followed by brain, heart, kidney, liver, pancreas and skeletal muscle. Expressed by B-lymphocytes, but not T-lymphocytes or nonhematopoietic cells. {ECO:0000269|PubMed:10432293}.; unclassifiable (Anatomical System);lymph node;umbilical cord;heart;blood;skin;skeletal muscle;breast;uterus;bile duct;lung;cornea;endometrium;oesophagus;larynx;nasopharynx;bone;alveolus;liver;testis;head and neck;kidney;germinal center;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.18283 0.11376 -0.075159878 47.78839349 10.06314 0.36728 DARS 0.00061199920887983 0.998378097435287 0.00100990335583288 aspartyl-tRNA synthetase FUNCTION: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.; . TISSUE SPECIFICITY: Expression in the developing and adult brain shows similar patterns. Highly expressed in the ventricular and subventricular zones, including hippocampal subfields, the midlateral temporaal cortex and the frontal polar cortex. The cerebellum, cereral cortex, hippocampus, and lateral ventricle show preferential neuronal expression. Expression in the peripheral neurons is evident in the colon. {ECO:0000269|PubMed:23643384}.; ovary;skin;retina;bone marrow;prostate;optic nerve;ganglion;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;oesophagus;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; amygdala;thyroid; 0.63432 0.19569 0.262810045 70.43524416 99.15853 2.15559 DARS-AS1 . . . DARS antisense RNA 1 . . . . . . . . . . . DARS2 4.40767877928912e-09 0.940603688994882 0.0593963065974396 aspartyl-tRNA synthetase 2, mitochondrial . DISEASE: Leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation (LBSL) [MIM:611105]: Autosomal recessive disease and is defined on the basis of a highly characteristic constellation of abnormalities observed by magnetic resonance imaging and spectroscopy. Affected individuals develop slowly progressive cerebellar ataxia, spasticity, and dorsal column dysfunction, sometimes with a mild cognitive deficit or decline. {ECO:0000269|PubMed:17384640}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;kidney;stomach;peripheral nerve; superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.36508 0.17238 0.196671391 67.19155461 345.04556 3.94027 DAW1 0.00078594792223416 0.982644868481541 0.0165691835962247 dynein assembly factor with WD repeats 1 FUNCTION: May play a role in axonemal outer row dynein assembly. {ECO:0000250}.; . . . . 0.08054 0.09429 0.440999548 77.79547063 1957.37654 8.14493 DAXX 0.842736879816879 0.157238040196266 2.50799868551433e-05 death-domain associated protein FUNCTION: Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as histone chaperone that facilitates deposition of histone H3.3. Acts as targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML- NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. In case of overexpression of centromeric histone variant CENPA (as found in various tumors) is involved in its mislocalization to chromosomes; the ectopic localization involves a heterotypic tetramer containing CENPA, and histones H3.3 and H4 and decreases binding of CTCF to chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Shows restriction activity towards human cytomegalovirus (HCMV). {ECO:0000269|PubMed:12140263, ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:15364927, ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:17081986, ECO:0000269|PubMed:17942542, ECO:0000269|PubMed:20504901, ECO:0000269|PubMed:20651253, ECO:0000269|PubMed:23222847, ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:24530302}.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;lymphoreticular;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;breast;epididymis;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;kidney;stomach;aorta; . 0.87978 0.10976 -0.821100135 11.88369899 81.37874 1.90988 DAZ1 . . . deleted in azoospermia 1 FUNCTION: RNA-binding protein that plays an essential role in spermatogenesis. May act by binding to the 3'-UTR of mRNAs and regulating their translation. Promotes germ-cell progression to meiosis and formation of haploid germ cells. {ECO:0000269|PubMed:19865085}.; DISEASE: Spermatogenic failure Y-linked 2 (SPGFY2) [MIM:415000]: A disorder resulting in the absence (azoospermia) or reduction (oligozoospermia) of sperm in the semen, leading to male infertility. {ECO:0000269|PubMed:11095434, ECO:0000269|PubMed:11870237, ECO:0000269|PubMed:12801575}. Note=The disease may be caused by mutations affecting the gene represented in this entry. AZFc deletions in the Yq11.23 region including the DAZ genes are the most common known genetic cause of human male infertility.; TISSUE SPECIFICITY: Testis-specific. Expression restricted to premeiotic germ cells, particularly in spermatogonia (at protein level). {ECO:0000269|PubMed:10936047, ECO:0000269|PubMed:18385127, ECO:0000269|PubMed:19223287}.; . . . . . . . . DAZ2 . . . deleted in azoospermia 2 FUNCTION: RNA-binding protein that plays an essential role in spermatogenesis. May act by binding to the 3'-UTR of mRNAs and regulating their translation.; DISEASE: Spermatogenic failure Y-linked 2 (SPGFY2) [MIM:415000]: A disorder resulting in the absence (azoospermia) or reduction (oligozoospermia) of sperm in the semen, leading to male infertility. {ECO:0000269|PubMed:11095434, ECO:0000269|PubMed:11870237, ECO:0000269|PubMed:12801575}. Note=The disease may be caused by mutations affecting the gene represented in this entry. AZFc deletions in the Yq11.23 region including the DAZ genes are the most common known genetic cause of human male infertility.; TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:10936047}.; . . 0.15655 . . . . . DAZ3 . . . deleted in azoospermia 3 FUNCTION: RNA-binding protein that plays an essential role in spermatogenesis. May act by binding to the 3'-UTR of mRNAs and regulating their translation.; DISEASE: Spermatogenic failure Y-linked 2 (SPGFY2) [MIM:415000]: A disorder resulting in the absence (azoospermia) or reduction (oligozoospermia) of sperm in the semen, leading to male infertility. {ECO:0000269|PubMed:11095434, ECO:0000269|PubMed:12801575}. Note=The disease may be caused by mutations affecting the gene represented in this entry. AZFc deletions in the Yq11.23 region including the DAZ genes are the most common known genetic cause of human male infertility.; TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:10936047}.; lung;testis;skeletal muscle;stomach; . . . . . . . DAZ4 . . . deleted in azoospermia 4 FUNCTION: RNA-binding protein that plays an essential role in spermatogenesis. May act by binding to the 3'-UTR of mRNAs and regulating their translation.; DISEASE: Spermatogenic failure Y-linked 2 (SPGFY2) [MIM:415000]: A disorder resulting in the absence (azoospermia) or reduction (oligozoospermia) of sperm in the semen, leading to male infertility. {ECO:0000269|PubMed:11095434, ECO:0000269|PubMed:12801575}. Note=The disease may be caused by mutations affecting the gene represented in this entry. AZFc deletions in the Yq11.23 region including the DAZ genes are the most common known genetic cause of human male infertility.; TISSUE SPECIFICITY: Testis-specific. Expression restricted to premeiotic germ cells, particularly in spermatogonia (at protein level). {ECO:0000269|PubMed:10936047, ECO:0000269|PubMed:18385127, ECO:0000269|PubMed:19223287}.; . . . . . . . . DAZAP1 0.999571003507893 0.000428995146538486 1.34556836495323e-09 DAZ associated protein 1 FUNCTION: RNA-binding protein, which may be required during spermatogenesis.; . TISSUE SPECIFICITY: Mainly expressed in testis. Expressed to a lower level in thymus. Weakly or not expressed in heart, liver, brain, placenta, lung, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:10857750}.; lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;cerebral cortex;endometrium;larynx;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;urinary;adrenal cortex;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;adrenal cortex;testis;trigeminal ganglion; 0.16252 0.11134 -0.538132194 20.26421326 275.74527 3.55666 DAZAP2 0.527543739723783 0.456370402850005 0.0160858574262115 DAZ associated protein 2 . . TISSUE SPECIFICITY: Widely expressed. Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocytes. Down-regulated in multiple myeloma. {ECO:0000269|PubMed:10857750}.; . . 0.17331 0.07119 0.170987912 65.5579146 9.15974 0.33406 DAZAP2P1 . . . DAZ associated protein 2 pseudogene 1 . . . . . . . . . . . DAZL 0.961607975742939 0.0383756969514267 1.63273056339319e-05 deleted in azoospermia like FUNCTION: RNA-binding protein, which is essential for gametogenesis in both males and females. Plays a central role during spermatogenesis. Acts by binding to the 3'-UTR of mRNA, specifically recognizing GUU triplets, and thereby regulating the translation of key transcripts (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:8896558, ECO:0000269|PubMed:8968755, ECO:0000269|PubMed:8968756}.; unclassifiable (Anatomical System);medulla oblongata;lung;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.35806 0.15898 0.237127192 68.98443029 165.92207 2.81831 DBET . . . D4Z4 binding element transcript (non-protein coding) . . . . . . . . . . . DBF4 0.998167681555921 0.00183230907329019 9.37078901538344e-09 DBF4 zinc finger FUNCTION: Regulatory subunit for CDC7 which activates its kinase activity thereby playing a central role in DNA replication and cell proliferation. Required for progression of S phase. The complex CDC7-DBF4A selectively phosphorylates MCM2 subunit at 'Ser-40' and 'Ser-53' and then is involved in regulating the initiation of DNA replication during cell cycle. {ECO:0000269|PubMed:10373557, ECO:0000269|PubMed:10523313, ECO:0000269|PubMed:17062569}.; . TISSUE SPECIFICITY: Highly expressed in testis and thymus. Expressed also in most cancer cells lines. {ECO:0000269|PubMed:10373557}.; ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;kidney;stomach; testis - interstitial;testis - seminiferous tubule;tumor;testis; 0.34632 0.15157 0.154398214 64.73814579 466.19397 4.47158 DBF4B 4.43213751313207e-08 0.815710726750512 0.184289228928113 DBF4 zinc finger B FUNCTION: Regulatory subunit for CDC7 which activates its kinase activity thereby playing a central role in DNA replication and cell proliferation. Required for progression of S and M phases. The complex CDC7-DBF4B selectively phosphorylates MCM2 subunit at 'Ser-40' and then is involved in regulating the initiation of DNA replication during cell cycle. {ECO:0000269|PubMed:12065429, ECO:0000269|PubMed:15668232, ECO:0000269|PubMed:17062569}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis. {ECO:0000269|PubMed:12065429}.; unclassifiable (Anatomical System);lymph node;heart;ovary;islets of Langerhans;hypothalamus;colon;blood;fovea centralis;choroid;lens;retina;bone marrow;optic nerve;lung;frontal lobe;thyroid;macula lutea;head and neck;mammary gland;brain; superior cervical ganglion;atrioventricular node; 0.11452 . 0.244401822 69.50931824 483.2489 4.52601 DBF4P1 . . . DBF4 zinc finger pseudogene 1 . . . . . . . . . . . DBF4P2 . . . DBF4 zinc finger pseudogene 2 . . . . . . . . . . . DBF4P3 . . . DBF4 zinc finger pseudogene 3 . . . . . . . . . . . DBH 2.54160922305115e-06 0.912671566382279 0.0873258920084984 dopamine beta-hydroxylase (dopamine beta-monooxygenase) FUNCTION: Conversion of dopamine to noradrenaline.; DISEASE: Dopamine beta-hydroxylase deficiency (DBH deficiency) [MIM:223360]: Characterized by profound deficits in autonomic and cardiovascular function, but apparently only subtle signs, if any, of central nervous system dysfunction. {ECO:0000269|PubMed:11857564}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);whole body;tongue;adrenal gland;sympathetic chain;head and neck;germinal center;brain; amygdala;superior cervical ganglion;adrenal gland;adrenal cortex;skeletal muscle; 0.23753 0.69486 -0.009234793 52.3767398 637.88987 5.08136 DBH-AS1 . . . DBH antisense RNA 1 . . . . . . . . . . . DBI 0.000164260337073615 0.444650716926823 0.555185022736104 diazepam binding inhibitor (GABA receptor modulator, acyl-CoA binding protein) FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.; . TISSUE SPECIFICITY: Isoform 1 is ubiquitous, with a moderate expression level. Isoform 2 is ubiquitous with high level in liver and adipose tissue. Isoform 3 is ubiquitous with strong expression in adipose tissue and heart. {ECO:0000269|PubMed:16055366, ECO:0000269|PubMed:21698759}.; myocardium;lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;alveolus;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;synovium;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;cerebellum cortex;islets of Langerhans;hypothalamus;oral cavity;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; amygdala;testis - interstitial;prostate;adipose tissue;tongue;hypothalamus;spinal cord;testis; 0.01062 0.07923 . . 1161.87674 6.48662 DBIL5P . . . diazepam binding inhibitor-like 5, pseudogene . . . . . . . . . . . DBIL5P2 . . . diazepam binding inhibitor-like 5 pseudogene 2 . . . . . . . . . . . DBIP1 . . . diazepam binding inhibitor (GABA receptor modulator, acyl-CoA binding protein) pseudogene 1 . . . . . . . . . . . DBIP2 . . . diazepam binding inhibitor (GABA receptor modulator, acyl-CoA binding protein) pseudogene 2 . . . . . . . . . . . DBIP3 . . . diazepam binding inhibitor (GABA receptor modulator, acyl-CoA binding protein) pseudogene 3 . . . . . . . . . . . DBN1 0.962685618555225 0.037313758122593 6.2332218233894e-07 drebrin 1 FUNCTION: Drebrins might play some role in cell migration, extension of neuronal processes and plasticity of dendrites. Required for actin polymerization at immunological synapses (IS) and for CXCR4 recruitment to IS. {ECO:0000269|PubMed:20215400}.; . TISSUE SPECIFICITY: Brain neurons. Also found in the heart, placenta, skeletal muscle, kidney and pancreas. Expressed in peripheral blood lymphocytes, including T-cells (at protein level). {ECO:0000269|PubMed:20215400}.; lymphoreticular;medulla oblongata;ovary;colon;fovea centralis;choroid;vein;skin;retina;uterus;optic nerve;endometrium;larynx;thyroid;bone;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;lens;pancreas;lung;epididymis;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion; 0.24114 0.19461 -0.086288664 47.11606511 845.8418 5.68937 DBNDD1 0.000234996408377196 0.518063924531349 0.481701079060274 dysbindin (dystrobrevin binding protein 1) domain containing 1 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;optic nerve;larynx;gum;bone;germinal center;brain;unclassifiable (Anatomical System);hypothalamus;urinary;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hippocampus;visual apparatus;cervix;head and neck;kidney;mammary gland;stomach; whole brain;prefrontal cortex;trigeminal ganglion;cingulate cortex; 0.30163 . -0.339715008 30.06605331 102.53319 2.18927 DBNDD2 0.0506088642378966 0.860107409756426 0.0892837260056771 dysbindin (dystrobrevin binding protein 1) domain containing 2 FUNCTION: May modulate the activity of casein kinase-1. Inhibits CSNK1D autophosphorylation (in vitro). {ECO:0000269|PubMed:16618118}.; . TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:16618118}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;head and neck;cervix;kidney;stomach;aorta;cerebellum; . 0.09761 0.07151 . . 23.04628 0.76905 DBNL 0.070981914478068 0.926323700802831 0.002694384719101 drebrin like FUNCTION: Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G- actin and promote actin polymerization by itself. Required for the formation of organized podosome rosettes (By similarity). May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes. {ECO:0000250, ECO:0000269|PubMed:14729663}.; . . . . 0.20108 0.72014 -0.023789244 52.09365416 77.70496 1.85644 DBP 0.820194274770572 0.175681964724486 0.00412376050494185 D site of albumin promoter (albumin D-box) binding protein FUNCTION: This transcriptional activator recognizes and binds to the sequence 5'-RTTAYGTAAY-3' found in the promoter of genes such as albumin, CYP2A4 and CYP2A5. It is not essential for circadian rhythm generation, but modulates important clock output genes. May be a direct target for regulation by the circadian pacemaker component clock. May affect circadian period and sleep regulation.; . TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in the suprachiasmatic nuclei (SCN) and in most peripheral tissues, with a strong circadian rhythmicity.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;macula lutea;visual apparatus;hippocampus;spleen;cervix;kidney;mammary gland;stomach;thymus; whole brain;superior cervical ganglion;subthalamic nucleus;globus pallidus;atrioventricular node;pons;skeletal muscle;cerebellum; 0.40179 0.12112 . . 37.64375 1.12089 DBR1 8.70518439226155e-05 0.93071993542074 0.0691930127353378 debranching RNA lariats 1 FUNCTION: Cleaves the 2'-5' phosphodiester linkage at the branch point of lariat intron pre-mRNAs after splicing and converts them into linear molecules that are subsequently degraded. It thereby facilitates ribonucleotide turnover. It may also participate in retrovirus replication via an RNA lariat intermediate in cDNA synthesis. {ECO:0000269|PubMed:10982890, ECO:0000269|PubMed:16232320}.; . . unclassifiable (Anatomical System);smooth muscle;islets of Langerhans;skin;skeletal muscle;bone marrow;uterus;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;testis;germinal center;brain;pineal gland;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.26524 0.11154 -0.466531444 23.51380042 128.83429 2.47412 DBT 0.000147622487439407 0.964498842862472 0.0353535346500882 dihydrolipoamide branched chain transacylase E2 FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component.; DISEASE: Note=Patients with primary biliary cirrhosis (PBC) show autoantibodies against the E2 component of branched-chain alpha- keto acid dehydrogenase complex. PBC is a chronic, progressive cholestatic liver disease characterized by the presence of antimitochondrial autoantibodies in patients serum. It manifests with inflammatory obliteration of intra-hepatic bile duct, leading to liver cell damage and cirrhosis. {ECO:0000269|PubMed:2908870, ECO:0000269|PubMed:7543435, ECO:0000269|PubMed:9141421}.; DISEASE: Maple syrup urine disease 2 (MSUD2) [MIM:248600]: A metabolic disorder due to an enzyme defect in the catabolic pathway of the branched-chain amino acids leucine, isoleucine, and valine. Accumulation of these 3 amino acids and their corresponding keto acids leads to encephalopathy and progressive neurodegeneration. Clinical features include mental and physical retardation, feeding problems, and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine. If untreated, maple syrup urine disease can lead to seizures, coma, and death. The disease is often classified by its pattern of signs and symptoms. The most common and severe form of the disease is the classic type, which becomes apparent soon after birth. Variant forms of the disorder become apparent later in infancy or childhood and are typically milder, but they still involve developmental delay and other medical problems if not treated. {ECO:0000269|PubMed:1847055, ECO:0000269|PubMed:9621512}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.39075 0.32097 0.817616644 87.95116773 173.95713 2.87132 DBX1 0.14778053659514 0.834417307310625 0.0178021560942348 developing brain homeobox 1 FUNCTION: Could have a role in patterning the central nervous system during embryogenesis. Has a key role in regulating the distinct phenotypic features that distinguish two major classes of ventral interneurons, V0 and V1 neurons. Regulates the transcription factor profile, neurotransmitter phenotype, intraspinal migratory path and axonal trajectory of V0 neurons, features that differentiate them from an adjacent set of V1 neurons (By similarity). {ECO:0000250}.; . . . . 0.19100 . . . 857.42367 5.71413 DBX2 4.41842154586426e-08 0.0598279886179303 0.940171967197854 developing brain homeobox 2 . . . brain; . 0.15286 0.09324 . . 169.38045 2.83961 DCAF4 0.00364518370773562 0.994470186454165 0.00188462983809969 DDB1 and CUL4 associated factor 4 FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240}.; . . unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;colon;skin;bile duct;uterus;pancreas;lung;endometrium;visual apparatus;hippocampus;liver;testis;amniotic fluid;cervix;kidney;brain;stomach; . 0.11570 0.10059 1.337468036 94.28520878 1892.30771 7.99823 DCAF4L1 0.851426397412879 0.148052324450394 0.000521278136727325 DDB1 and CUL4 associated factor 4-like 1 . . . lung;testis; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.28342 0.10483 -0.049474214 50.01179523 10.97474 0.39711 DCAF4L2 0.0016494438654563 0.888981522482849 0.109369033651695 DDB1 and CUL4 associated factor 4-like 2 . . . lung;testis; superior cervical ganglion;testis - seminiferous tubule;placenta;ciliary ganglion;trigeminal ganglion; 0.15371 0.09810 -0.001743238 53.85114414 81.67397 1.91437 DCAF5 0.999968932331125 3.10676666286917e-05 2.24627292059606e-12 DDB1 and CUL4 associated factor 5 FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9740667}.; unclassifiable (Anatomical System);lung;placenta;testis;parathyroid;germinal center;lens;skin; testis - interstitial;testis - seminiferous tubule;testis;white blood cells;ciliary ganglion; 0.58383 0.10764 -1.105907904 6.86482661 58.69346 1.55207 DCAF6 0.996908923107335 0.00309107688128251 1.13821236507599e-11 DDB1 and CUL4 associated factor 6 FUNCTION: Ligand-dependent coactivator of nuclear receptors. Enhance transcriptional activity of the nuclear receptors NR3C1 and AR. May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:15784617, ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle and testis. Expressed to a lesser degree in heart, prostate, and adrenal gland. {ECO:0000269|PubMed:15784617}.; myocardium;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;iris;amniotic fluid;germinal center;brain;gall bladder;tonsil;heart;cartilage;blood;lens;skeletal muscle;breast;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach; amygdala;occipital lobe;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;cingulate cortex;skeletal muscle; 0.53934 0.13231 -0.242430445 36.22906346 1387.38336 6.97264 DCAF7 0.875048579312607 0.123363155004559 0.00158826568283393 DDB1 and CUL4 associated factor 7 FUNCTION: Involved in craniofacial development. Acts upstream of the EDN1 pathway and is required for formation of the upper jaw equivalent, the palatoquadrate. The activity required for EDN1 pathway function differs between the first and second arches (By similarity). Associates with DIAPH1 and controls GLI1 transcriptional activity. Could be involved in normal and disease skin development. May function as a substrate receptor for CUL4- DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000250, ECO:0000269|PubMed:16887337, ECO:0000269|PubMed:16949367}.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;oral cavity;muscle;adrenal cortex;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;atrioventricular node;trigeminal ganglion; 0.70030 . . . 1.20345 0.03612 DCAF8 0.999730107307524 0.000269892257398025 4.35077719712579e-10 DDB1 and CUL4 associated factor 8 FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240}.; DISEASE: Giant axonal neuropathy 2, autosomal dominant (GAN2) [MIM:610100]: An autosomal dominant peripheral axonal neuropathy characterized by onset of distal sensory impairment with lower extremity muscle weakness and atrophy after the second decade. Clinical features include foot deformities apparent in childhood, and cardiomyopathy in severely affected individuals. Sural nerve biopsy shows giant axonal swelling with neurofilament accumulation. {ECO:0000269|PubMed:24500646}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . salivary gland;colon;skin;retina;uterus;prostate;frontal lobe;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;small intestine;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.26586 0.10825 -0.648365105 16.35999056 72.2965 1.77147 DCAF8L1 0.119165931149828 0.855096371872504 0.0257376969776673 DDB1 and CUL4 associated factor 8-like 1 . . . . . 0.03137 . 0.354632714 74.58126917 37.57088 1.11888 DCAF8L2 0.575393469012494 0.413442973338201 0.0111635576493054 DDB1 and CUL4 associated factor 8-like 2 . . . . . 0.03137 . . . 1419.66743 7.03950 DCAF10 0.967142660986371 0.0328550945026357 2.24451099321294e-06 DDB1 and CUL4 associated factor 10 FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367}.; . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;testis;amniotic fluid;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;pharynx;blood;lens;skeletal muscle;lung;cornea;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.49527 0.09541 -0.383807564 27.41802312 32.63562 1.01497 DCAF11 0.0714513191790591 0.928526440759772 2.22400611689726e-05 DDB1 and CUL4 associated factor 11 FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;amniotic fluid;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;liver;atrioventricular node;pons;trigeminal ganglion; 0.51309 0.10658 -0.066061882 48.77919321 3236.70264 10.83152 DCAF12 0.00348556415870117 0.986768318880499 0.00974611696079961 DDB1 and CUL4 associated factor 12 FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240}.; . TISSUE SPECIFICITY: Highly expressed in lung cancer tissues and some cancer cell lines. Restricted expression in normal testis. {ECO:0000269|PubMed:18957058}.; lymphoreticular;ovary;developmental;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;endometrium;synovium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; fetal liver;testis - interstitial;testis - seminiferous tubule;adrenal gland;testis;bone marrow; 0.55524 0.10601 -0.381986487 27.68931352 2089.48508 8.42000 DCAF12L1 0.805163159874703 0.189729413557717 0.00510742656757946 DDB1 and CUL4 associated factor 12-like 1 . . . . . 0.16688 . -0.337894035 30.37272942 5.336 0.19762 DCAF12L2 0.162975821797611 0.773473640910968 0.0635505372914213 DDB1 and CUL4 associated factor 12-like 2 . . . . . 0.53699 . -0.22584292 37.32012267 18.78134 0.64905 DCAF13 6.92729531171936e-05 0.998985212141447 0.000945514905435811 DDB1 and CUL4 associated factor 13 FUNCTION: Possible role in ribosomal RNA processing (By similarity). May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000250, ECO:0000269|PubMed:16949367}.; . . lymphoreticular;ovary;developmental;colon;parathyroid;vein;skin;retina;uterus;prostate;frontal lobe;endometrium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;urinary;skeletal muscle;bile duct;breast;pancreas;lung;mesenchyma;placenta;visual apparatus;liver;hypopharynx;head and neck;kidney;mammary gland;stomach;thymus; . 0.87388 0.08975 0.846940207 88.47605567 3332.2896 11.04368 DCAF13P1 . . . DDB1 and CUL4 associated factor 13 pseudogene 1 . . . . . . . . . . . DCAF13P2 . . . DDB1 and CUL4 associated factor 13 pseudogene 2 . . . . . . . . . . . DCAF13P3 . . . DDB1 and CUL4 associated factor 13 pseudogene 3 . . . . . . . . . . . DCAF15 0.995060211995185 0.00493968260672563 1.05398088947534e-07 DDB1 and CUL4 associated factor 15 FUNCTION: May be involved in ubiquitination and degradation through a DBB1-CUL4 E3 protein-ubiquitin ligase. {ECO:0000269|PubMed:16949367}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;bile duct;pancreas;lung;placenta;macula lutea;spleen;kidney;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;white blood cells;trigeminal ganglion; . . -0.574945567 18.90186365 771.36872 5.49700 DCAF16 0.00409865973416999 0.653830627831526 0.342070712434304 DDB1 and CUL4 associated factor 16 FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367}.; . . . . 0.21551 . 0.12689526 63.00424628 335.32468 3.89050 DCAF17 0.000284984948941262 0.985235195461734 0.014479819589325 DDB1 and CUL4 associated factor 17 FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:19026396}.; unclassifiable (Anatomical System);uterus;ovary;liver;testis;brain;skeletal muscle;bone marrow; pons; 0.04615 . -0.47017169 23.25430526 226.74108 3.25465 DCAKD 0.0293860851896359 0.804845941890454 0.16576797291991 dephospho-CoA kinase domain containing . . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;pineal body;colon;skin;skeletal muscle;retina;uterus;pancreas;lung;frontal lobe;endometrium;bone;placenta;visual apparatus;iris;liver;amnion;amniotic fluid;spleen;kidney;brain; superior cervical ganglion;uterus corpus;adrenal gland;liver;globus pallidus;pons;trigeminal ganglion; 0.22700 0.14389 0.240763792 69.36777542 444.32254 4.38479 DCANP1 . . . dendritic cell-associated nuclear protein FUNCTION: Binds with and transactivates the corticotropin- releasing hormone (CRH) promoter. {ECO:0000269|PubMed:20693543}.; . TISSUE SPECIFICITY: Expressed in neurons of the paraventricular nucleus, thalamus and occipital cortex and in glial cells (at protein level). Predominantly expressed in dendritic cells. Detected in brain and skeletal muscle. Highly expressed in mature dendritic cells and at a lower level in immature dendritic cells. Expressed in paraventricular nucleus, supraoptic nucleus and nucleus basalis of Meynert. Strongly expressed in paraventricular nucleus of depressed patients compared to controls. Not expressed in monocytes and B-cells. {ECO:0000269|PubMed:11798177, ECO:0000269|PubMed:20693543}.; . . . 0.08906 1.396334339 94.70393961 . . DCBLD1 8.21257411364962e-05 0.996282235364536 0.0036356388943279 discoidin, CUB and LCCL domain containing 1 . . . unclassifiable (Anatomical System);islets of Langerhans;colon;parathyroid;uterus;larynx;thyroid;placenta;duodenum;alveolus;testis;head and neck;cervix;brain;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17327 0.10218 -0.512444034 21.55579146 1314.8222 6.81517 DCBLD2 0.000553237247244631 0.993742348737186 0.00570441401556986 discoidin, CUB and LCCL domain containing 2 . . TISSUE SPECIFICITY: Highly expressed in testis, heart, skeletal muscle and also in cultured vascular smooth muscle cells. {ECO:0000269|PubMed:11447234, ECO:0000269|PubMed:11973641}.; ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;nasopharynx;placenta;amnion;head and neck;kidney;stomach;aorta; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.17301 0.10048 0.712836712 85.76315169 506.50086 4.61828 DCC 0.99999895681268 1.04318731995894e-06 3.96014074842998e-20 DCC netrin 1 receptor FUNCTION: Receptor for netrin required for axon guidance. Mediates axon attraction of neuronal growth cones in the developing nervous system upon ligand binding. Its association with UNC5 proteins may trigger signaling for axon repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. Implicated as a tumor suppressor gene. {ECO:0000269|PubMed:8187090, ECO:0000269|PubMed:8861902}.; DISEASE: Mirror movements 1 (MRMV1) [MIM:157600]: A disorder characterized by contralateral involuntary movements that mirror voluntary ones. While mirror movements are occasionally found in young children, persistence beyond the age of 10 is abnormal. Mirror movements occur more commonly in the upper extremities. {ECO:0000269|PubMed:20431009}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in axons of the central and peripheral nervous system and in differentiated cell types of the intestine. Not expressed in colorectal tumor cells that lost their capacity to differentiate into mucus producing cells. {ECO:0000269|PubMed:7926722}.; unclassifiable (Anatomical System);lung;testis;skeletal muscle; superior cervical ganglion;atrioventricular node; 0.97673 0.22976 -1.363273289 4.523472517 5178.8331 14.80420 DCD 0.00361067086160127 0.626527352624346 0.369861976514053 dermcidin FUNCTION: DCD-1 displays antimicrobial activity thereby limiting skin infection by potential pathogens in the first few hours after bacterial colonization. Highly effective against E.coli, E.faecalis, S.aureus and C.albicans. Optimal pH and salt concentration resemble the conditions in sweat. Also exhibits proteolytic activity.; . TISSUE SPECIFICITY: Specifically and constitutively expressed in eccrine sweat gland cells. Secreted into the sweat at a concentration of 1-10 micrograms/ml.; unclassifiable (Anatomical System);meninges;pia mater;dura mater;skin; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.05804 0.16541 0.457594962 78.16112291 82.59949 1.93062 DCDC1 9.13494875057035e-05 0.787504378793092 0.212404271719403 doublecortin domain containing 1 . . TISSUE SPECIFICITY: Highly expressed in testis. Lower levels of expression in lung, kidney, and pancreas. Higher expression in fetal brain than in adult brain. {ECO:0000269|PubMed:12820024}.; . . 0.02332 0.03434 -0.624497208 17.16206653 2562.85474 9.45951 DCDC2 1.04848738314639e-05 0.798601653230237 0.201387861895932 doublecortin domain containing 2 FUNCTION: Protein that plays a role in the inhibition of canonical Wnt signaling pathway. May be involved in neuronal migration during development of the cerebral neocortex. Involved in the control of ciliogenesis and ciliary length (PubMed:25601850). {ECO:0000250|UniProtKB:D3ZR10, ECO:0000269|PubMed:25557784, ECO:0000269|PubMed:25601850}.; DISEASE: Nephronophthisis 19 (NPHP19) [MIM:616217]: A form of nephronophthisis, an autosomal recessive disorder characterized by chronic tubulointerstitial nephritis resulting in end-stage renal disease. NPHP19 patients also manifest hepatosplenomegaly, hepatic fibrosis, destruction of the bile ducts, focal bile ductal proliferation, ductal plate malformation, and cholestasis. {ECO:0000269|PubMed:25557784}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal recessive, 66 (DFNB66) [MIM:610212]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:25601850}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. In brain, highly expressed in the entorhinal cortex, inferior temporal cortex, medial temporal cortex, hypothalamus, amygdala and hippocampus. {ECO:0000269|PubMed:10601354, ECO:0000269|PubMed:16278297}.; . . 0.04207 . 0.863528995 88.74144845 1895.65757 8.00664 DCDC2B 8.88085255997303e-08 0.297458269092377 0.702541642099097 doublecortin domain containing 2B . . . . . . . 0.262810045 70.43524416 108.51956 2.26006 DCDC2C . . . doublecortin domain containing 2C . . . . . . . . . 1351.19948 6.90352 DCDC5 . . . doublecortin domain containing 5 . . . unclassifiable (Anatomical System);frontal lobe;ovary;placenta;liver;testis;parathyroid;spleen;retina; whole brain;dorsal root ganglion;testis - interstitial;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.07556 . . . . DCHS1 0.999995437521813 4.56247818706946e-06 5.90022221158793e-20 dachsous cadherin-related 1 FUNCTION: Calcium-dependent cell-adhesion protein. Mediates functions in neuroprogenitor cell proliferation and differentiation. In the heart, has a critical role for proper morphogenesis of the mitral valve, acting in the regulation of cell migration involved in valve formation (PubMed:26258302). {ECO:0000269|PubMed:26258302}.; DISEASE: Mitral valve prolapse 2 (MVP2) [MIM:607829]: A form of mitral valve prolapse, a valvular hearth disease characterized by abnormally elongated and thickened mitral valve leaflets, that typically show myxomatous degeneration with increased leaflet compliance. It is associated with mitral regurgitation. Myxomatous mitral valves have an abnormal layered architecture characterized by loose collagen in fibrosa, expanded spongiosa strongly positive for proteoglycans, and disrupted elastin in atrialis. In classic mitral valve prolapse, leaflets are at least 5 mm thick, whereas in the non-classic form, they are less than 5 mm thick. Severe classic mitral valve prolapse is strongly associated with arrhythmias, endocarditis, heart failure, and need for valve surgery. {ECO:0000269|PubMed:26258302}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in fibroblasts but not in melanocytes or keratinocytes. {ECO:0000269|PubMed:9199196}.; ovary;colon;skin;bone marrow;uterus;prostate;frontal lobe;cerebral cortex;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;adrenal cortex;blood;breast;pancreas;lung;placenta;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;medulla oblongata;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.32953 0.13101 -1.375261521 4.399622552 2403.94476 9.10390 DCHS2 7.24816951158799e-28 0.00462328761116038 0.99537671238884 dachsous cadherin-related 2 FUNCTION: Calcium-dependent cell-adhesion protein. {ECO:0000250}.; . TISSUE SPECIFICITY: Cerebral cortex and testis. {ECO:0000269|PubMed:15003449}.; unclassifiable (Anatomical System);uterus;lung;ovary;heart;testis;brain;skin;skeletal muscle; medulla oblongata;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;caudate nucleus;trigeminal ganglion;skeletal muscle;parietal lobe; 0.06313 . 7.753553704 99.94102383 8535.58316 19.99068 DCK 0.390659944763637 0.607306724629938 0.00203333060642509 deoxycytidine kinase FUNCTION: Required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG) and deoxyadenosine (dA). Has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents. {ECO:0000269|PubMed:18377927, ECO:0000269|PubMed:20614893}.; . . ovary;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;blood;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;thymus; ciliary ganglion; 0.02920 0.23891 0.43736446 77.56546355 330.26484 3.86339 DCLK1 0.961271824270266 0.0387281477290185 2.80007156023422e-08 doublecortin like kinase 1 FUNCTION: Probable kinase that may be involved in a calcium- signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system.; . TISSUE SPECIFICITY: In fetal tissues, highly expressed in brain, detectable in lung and liver, but not in kidney. In adult tissues, expressed ubiquitously in the brain, detectable in the heart, liver, spleen, thymus, prostate, testis, ovary, small intestine and colon. The type A isoforms seem to be expressed predominantly in fetal brain whereas type B isoforms are expressed abundantly in both fetal and adult brain. {ECO:0000269|PubMed:10051403}.; unclassifiable (Anatomical System);hypothalamus;breast;optic nerve;whole body;lung;frontal lobe;cochlea;endometrium;bone;hippocampus;pituitary gland;testis;kidney;mammary gland;brain;stomach; amygdala;whole brain;superior cervical ganglion;occipital lobe;medulla oblongata;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.82958 0.16306 -0.646543901 16.44255721 31.81304 1.00069 DCLK2 0.966310094576242 0.0336898076141033 9.78096545578544e-08 doublecortin like kinase 2 FUNCTION: Protein kinase with a significantly reduced C(a2+)/CAM affinity and dependence compared to other members of the CaMK family. May play a role in the down-regulation of CRE-dependent gene activation probably by phosphorylation of the CREB coactivator CRTC2/TORC2 and the resulting retention of TORC2 in the cytoplasm (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the brain, heart and eyes. {ECO:0000269|PubMed:18075264}.; unclassifiable (Anatomical System);heart;islets of Langerhans;parathyroid;blood;skin;retina;uterus;pancreas;whole body;lung;frontal lobe;cerebral cortex;endometrium;bone;thyroid;liver;testis;spleen;kidney;brain;mammary gland; amygdala;subthalamic nucleus;fetal brain;hypothalamus;prefrontal cortex;globus pallidus;caudate nucleus;cingulate cortex;cerebellum; 0.13998 0.10102 -0.378346116 28.01368247 110.56188 2.28968 DCLK3 0.439315817627167 0.559278592312444 0.00140559006038919 doublecortin like kinase 3 . . . . . 0.19024 0.11320 -0.020150552 52.25288983 85.65098 1.97483 DCLRE1A 4.67768893872676e-08 0.949977696006614 0.0500222572164967 DNA cross-link repair 1A FUNCTION: May be required for DNA interstrand cross-link repair. Also required for checkpoint mediated cell cycle arrest in early prophase in response to mitotic spindle poisons. {ECO:0000269|PubMed:15542852}.; . TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, pancreas, placenta and skeletal muscle. {ECO:0000269|PubMed:12446782}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;larynx;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;stomach; . 0.21885 0.14488 2.294845355 98.31328143 240.92339 3.35300 DCLRE1B 0.107858132118987 0.885596906660388 0.00654496122062503 DNA cross-link repair 1B FUNCTION: 5'-3' exonuclease that plays a central role in telomere maintenance and protection during S-phase. Participates in the protection of telomeres against non-homologous end-joining (NHEJ)- mediated repair, thereby ensuring that telomeres do not fuse. Plays a key role in telomeric loop (T loop) formation by being recruited by TERF2 at the leading end telomeres and by processing leading-end telomeres immediately after their replication via its exonuclease activity: generates 3' single-stranded overhang at the leading end telomeres avoiding blunt leading-end telomeres that are vulnerable to end-joining reactions and expose the telomere end in a manner that activates the DNA repair pathways. Together with TERF2, required to protect telomeres from replicative damage during replication by controlling the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Also involved in response to DNA damage: plays a role in response to DNA interstrand cross-links (ICLs) by facilitating double-strand break formation. In case of spindle stress, involved in prophase checkpoint. {ECO:0000269|PubMed:15467758, ECO:0000269|PubMed:15572677, ECO:0000269|PubMed:16730175, ECO:0000269|PubMed:16730176, ECO:0000269|PubMed:18468965, ECO:0000269|PubMed:18469862, ECO:0000269|PubMed:19197158, ECO:0000269|PubMed:19411856, ECO:0000269|PubMed:20655466}.; DISEASE: Hoyeraal-Hreidarsson syndrome (HHS) [MIM:305000]: A clinically severe variant of dyskeratosis congenita that is characterized by multisystem involvement, early onset in utero, and often results in death in childhood. Affected individuals show intrauterine growth retardation, microcephaly, cerebellar hypoplasia, delayed development, and bone marrow failure resulting in immunodeficiency. {ECO:0000269|PubMed:20479256}. Note=The gene represented in this entry may be involved in disease pathogenesis. An aberrant splice variant of DCLRE1B, designated Apollo-Delta, has been found in a patient with Hoyeraal-Hreidarsson syndrome (PubMed:20479256). Apollo-Delta hampers the proper replication of telomeres, leading to major telomeric dysfunction and cellular senescence, but maintains its DNA interstrand cross-link repair function in the whole genome. {ECO:0000269|PubMed:20479256}.; . . . 0.07921 0.13381 0.042348793 57.31304553 1836.53589 7.90265 DCLRE1C 0.00286935735912744 0.996590134018106 0.000540508622766578 DNA cross-link repair 1C FUNCTION: Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ. {ECO:0000269|PubMed:11336668, ECO:0000269|PubMed:11955432, ECO:0000269|PubMed:12055248, ECO:0000269|PubMed:14744996, ECO:0000269|PubMed:15071507, ECO:0000269|PubMed:15456891, ECO:0000269|PubMed:15468306, ECO:0000269|PubMed:15574326, ECO:0000269|PubMed:15574327, ECO:0000269|PubMed:15811628, ECO:0000269|PubMed:15936993}.; DISEASE: Severe combined immunodeficiency autosomal recessive T- cell-negative/B-cell-negative/NK-cell-positive with sensitivity to ionizing radiation (RSSCID) [MIM:602450]: A form of severe combined immunodeficiency, a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy with recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T- cell-mediated cellular immunity due to a defect in T-cell development. Individuals affected by RS-SCID show defects in the DNA repair machinery necessary for coding joint formation and the completion of V(D)J recombination. A subset of cells from such patients show increased radiosensitivity. {ECO:0000269|PubMed:11336668, ECO:0000269|PubMed:12406895, ECO:0000269|PubMed:12569164, ECO:0000269|PubMed:12592555, ECO:0000269|PubMed:12921762}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Severe combined immunodeficiency Athabaskan type (SCIDA) [MIM:602450]: A variety of SCID with sensitivity to ionizing radiation. A founder mutation has been detected in Athabascan- speaking native Americans, being inherited as an autosomal recessive trait. Affected individuals exhibit clinical symptoms and defects in DNA repair comparable to those seen in RS-SCID. {ECO:0000269|PubMed:12055248}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Omenn syndrome (OS) [MIM:603554]: Severe immunodeficiency characterized by the presence of activated, anergic, oligoclonal T-cells, hypereosinophilia, and high IgE levels. {ECO:0000269|PubMed:15731174}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in the kidney, lung, pancreas and placenta (at the mRNA level). Expression is not increased in thymus or bone marrow, sites of V(D)J recombination. {ECO:0000269|PubMed:11336668}.; fovea centralis;choroid;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;blood;lens;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;tongue;ciliary ganglion;white blood cells;atrioventricular node;trigeminal ganglion;parietal lobe;skin;skeletal muscle; 0.21850 0.20593 0.068033485 59.0351498 2119.4131 8.47749 DCLRE1CP1 . . . DNA cross-link repair 1C pseudogene 1 . . . . . . . . . . . DCN 0.457565652637867 0.541210468794202 0.00122387856793059 decorin FUNCTION: May affect the rate of fibrils formation.; DISEASE: Corneal dystrophy, congenital stromal (CSCD) [MIM:610048]: A corneal dystrophy characterized by congenital corneal opacification consisting of a large number of flakes and spots throughout all layers of the stroma. It results in progressive, painless visual loss. Corneal erosions and photophobia are absent. {ECO:0000269|PubMed:15671264}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;developmental;colon;choroid;skin;bone marrow;uterus;prostate;cochlea;endometrium;bone;pituitary gland;testis;dura mater;spinal ganglion;brain;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;tongue;islets of Langerhans;skeletal muscle;pancreas;pia mater;lung;trabecular meshwork;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; uterus;dorsal root ganglion;superior cervical ganglion;uterus corpus;testis - interstitial;adipose tissue;trachea;ovary;placenta;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.60686 0.86458 -0.049474214 50.01179523 179.81271 2.91281 DCP1A 0.943913887681161 0.0560775646467917 8.54767204780713e-06 decapping mRNA 1A FUNCTION: Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7- methyl guanine cap structure from mRNA molecules, yielding a 5'- phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1. {ECO:0000269|PubMed:11836524, ECO:0000269|PubMed:12417715}.; . TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung, skeletal muscle, liver, kidney and pancreas. {ECO:0000269|PubMed:11836524}.; medulla oblongata;ovary;umbilical cord;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;larynx;bone;testis;brain;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;alveolus;amnion;head and neck;kidney;mammary gland; superior cervical ganglion; 0.44145 0.11103 . . 160.55737 2.76552 DCP1B 5.3210820854203e-07 0.645423767809164 0.354575700082628 decapping mRNA 1B FUNCTION: May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;ovary;heart;salivary gland;colon;skin;skeletal muscle;uterus;prostate;pancreas;whole body;lung;endometrium;bone;placenta;liver;testis;spleen;germinal center;kidney;brain;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.08770 0.08453 0.712836712 85.76315169 312.12633 3.75977 DCP2 0.856306644918669 0.143673679401876 1.96756794548692e-05 decapping mRNA 2 FUNCTION: Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking an RNA moiety. {ECO:0000269|PubMed:12218187, ECO:0000269|PubMed:12417715, ECO:0000269|PubMed:12486012, ECO:0000269|PubMed:12923261, ECO:0000269|PubMed:14527413, ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:21070968}.; . TISSUE SPECIFICITY: Expressed in brain and testis. Not detected in heart (at protein level). {ECO:0000269|PubMed:21070968}.; . . 0.47964 0.10830 -0.890882376 10.30313753 12.91085 0.47047 DCPS 0.00163802399731831 0.888148454953209 0.110213521049472 decapping enzyme, scavenger FUNCTION: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre- mRNAs. Inhibits activation-induced cell death. {ECO:0000269|PubMed:11747811, ECO:0000269|PubMed:12198172, ECO:0000269|PubMed:12871939, ECO:0000269|PubMed:14523240, ECO:0000269|PubMed:15273322, ECO:0000269|PubMed:15383679, ECO:0000269|PubMed:15769464, ECO:0000269|PubMed:16140270, ECO:0000269|PubMed:18426921, ECO:0000269|PubMed:22985415}.; DISEASE: Al-Raqad syndrome (ARS) [MIM:616459]: A syndrome characterized by delayed psychomotor development, moderate to severe intellectual disability, poor or absent speech, microcephaly, congenital hypotonia, and severe growth delay. {ECO:0000269|PubMed:25701870, ECO:0000269|PubMed:25712129}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in liver, brain, kidney, testis and prostate. {ECO:0000269|PubMed:12871939}.; myocardium;medulla oblongata;ovary;colon;choroid;skin;bone marrow;uterus;prostate;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;muscle;blood;lung;placenta;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; liver;white blood cells;skeletal muscle; 0.24119 0.19235 -0.176292081 40.56381222 198.96137 3.04821 DCR . . . Down syndrome chromosome region . . . . . . . . . . . DCST1 3.88695922784292e-15 0.077209640415293 0.922790359584703 DC-STAMP domain containing 1 . . . unclassifiable (Anatomical System);optic nerve;lung;ovary;placenta;macula lutea;testis;cervix;fovea centralis;choroid;lens;brain;retina; . 0.07600 0.09189 -0.927704399 9.719273414 376.76599 4.09199 DCST2 1.45881629274481e-09 0.941124481447648 0.0588755170935354 DC-STAMP domain containing 2 . . . medulla oblongata;lung;placenta;colon; . 0.21478 . -0.990222991 8.634111819 174.27729 2.87304 DCSTAMP 0.00134526640829737 0.862503805003896 0.136150928587807 dendrocyte expressed seven transmembrane protein FUNCTION: Probable cell surface receptor that plays several roles in cellular fusion, cell differentiation, bone and immune homeostasis. Plays a role in TNFSF11-mediated osteoclastogenesis. Cooperates with OCSTAMP in modulating cell-cell fusion in both osteoclasts and foreign body giant cells (FBGCs). Participates in osteoclast bone resorption. Involved in inducing the expression of tartrate-resistant acid phosphatase in osteoclast precursors. Plays a role in haematopoietic stem cell differentiation of bone marrow cells toward the myeloid lineage. Inhibits the development of neutrophilic granulocytes. Plays also a role in the regulation of dendritic cell (DC) antigen presentation activity by controlling phagocytic activity. Involved in the maintenance of immune self-tolerance and avoidance of autoimmune reactions.; . TISSUE SPECIFICITY: Preferentially expressed by dendritic cells (DCs). Detected in both immature and mature DCs. Highly expressed in lymph nodes, lung, kidney and liver. Expressed at lower levels in pancreas, bone marrow, spleen, leukocytes, in freshly isolated peripheral blood mononuclear cells (PBMC) and B-cells. Not expressed in freshly isolated monocytes. {ECO:0000269|PubMed:11169400, ECO:0000269|PubMed:11345586}.; . . 0.11208 0.12565 0.576916344 82.25406936 1486.66093 7.17641 DCT 6.54969970498014e-12 0.118113194205065 0.881886805788386 dopachrome tautomerase FUNCTION: Involved in regulating eumelanin and phaeomelanin levels.; . . . . 0.33975 0.55136 -0.598810865 18.13517339 178.90584 2.90630 DCTD 1.63560551829744e-05 0.248999977399117 0.7509836665457 dCMP deaminase FUNCTION: Supplies the nucleotide substrate for thymidylate synthetase.; . . ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;thyroid;atrioventricular node; 0.20820 0.24133 -0.317668748 31.45789101 5.18079 0.19251 DCTN1 0.291891035522283 0.708108961923695 2.55402203004773e-09 dynactin subunit 1 FUNCTION: Required for the cytoplasmic dynein-driven retrograde movement of vesicles and organelles along microtubules. Dynein- dynactin interaction is a key component of the mechanism of axonal transport of vesicles and organelles.; DISEASE: Neuronopathy, distal hereditary motor, 7B (HMN7B) [MIM:607641]: A neuromuscular disorder. Distal hereditary motor neuronopathies constitute a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. {ECO:0000269|PubMed:12627231}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Amyotrophic lateral sclerosis (ALS) [MIM:105400]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. {ECO:0000269|PubMed:15326253, ECO:0000269|PubMed:16240349}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Perry syndrome (PERRYS) [MIM:168605]: A neuropsychiatric disorder characterized by mental depression not responsive to antidepressant drugs or electroconvulsive therapy, sleep disturbances, exhaustion and marked weight loss. Parkinsonism develops later and respiratory failure occurred terminally. {ECO:0000269|PubMed:19136952, ECO:0000269|PubMed:24676999, ECO:0000269|PubMed:24881494}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Brain.; myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;cerebrum;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;choroid;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;aorta; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;testis;parietal lobe;cingulate cortex;cerebellum; 0.51731 0.50536 -0.87816671 10.58032555 488.32895 4.54937 DCTN1-AS1 . . . DCTN1 antisense RNA 1 . . . . . . . . . . . DCTN2 0.996367311488722 0.00363244262233372 2.45888944457124e-07 dynactin subunit 2 FUNCTION: Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development.; . . lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;spinal cord;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;oral cavity;muscle;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; whole brain;subthalamic nucleus;occipital lobe;thalamus;cerebellum peduncles;pons;parietal lobe;cerebellum; 0.70885 0.34695 -0.0274281 51.65723048 92.57271 2.06855 DCTN3 0.020223961561602 0.903715383495223 0.0760606549431746 dynactin subunit 3 FUNCTION: Together with dynein may be involved in spindle assembly and cytokinesis. {ECO:0000269|PubMed:9722614}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in muscle and pancreas and detected at lower levels in brain. {ECO:0000269|PubMed:9722614}.; lymphoreticular;myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;whole body;frontal lobe;bone;thyroid;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;kidney;stomach; whole brain;medulla oblongata;superior cervical ganglion;globus pallidus;ciliary ganglion;skeletal muscle;parietal lobe;cerebellum; 0.08961 0.11542 0.125076652 62.7388535 19.56698 0.67180 DCTN4 0.953389997662452 0.0466089157515591 1.08658598931832e-06 dynactin subunit 4 FUNCTION: Could have a dual role in dynein targeting and in ACTR1A/Arp1 subunit of dynactin pointed-end capping. Could be involved in ACTR1A pointed-end binding and in additional roles in linking dynein and dynactin to the cortical cytoskeleton.; . . . . 0.38025 0.11977 -0.512444034 21.55579146 2570.86813 9.47719 DCTN5 0.0204374093932638 0.904484508197919 0.0750780824088176 dynactin subunit 5 . . . lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;mesenchyma;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.32718 0.11515 -0.09720619 46.20193442 7.99244 0.29348 DCTN6 0.0262383991081917 0.919211570449395 0.0545500304424129 dynactin subunit 6 . . TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;kidney;aorta;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;thalamus;occipital lobe;medulla oblongata;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;atrioventricular node;subthalamic nucleus;globus pallidus;parietal lobe;cingulate cortex; 0.22872 0.15588 -0.141298762 42.87567823 10.07339 0.36776 DCTPP1 0.184698213695084 0.76380399481114 0.0514977914937764 dCTP pyrophosphatase 1 FUNCTION: Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for modified dCTP. Activity is highest with 5-iodo-dCTP, followed by 5-bromo-dCTP, unmodified dCTP, 5-methyl-dCTP and 5-chloro-dCTP. Hydrolyzes 2-chloro-dATP and 2-hydroxy-dATP with lower efficiency, and has even lower activity with unmodified dATP, dTTP and dUTP (in vitro). Does not hydrolyze ATP, UTP, ITP, GTP, dADP, dCDP or dGTP. May protect DNA or RNA against the incorporation of non- canonical nucleotide triphosphates. May protect cells against inappropriate methylation of CpG islands by DNA methyltransferases (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;oesophagus;larynx;bone;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; . . 0.12422 0.237127192 68.98443029 41.53659 1.21180 DCUN1D1 0.990513001427957 0.00948442996565062 2.56860639231014e-06 defective in cullin neddylation 1 domain containing 1 FUNCTION: Part of an E3 ubiquitin ligase complex for neddylation. Promotes neddylation of cullin components of E3 cullin-RING ubiquitin ligase complexes. Acts by binding to cullin-RBX1 complexes in the cytoplasm and promoting their nuclear translocation, enhancing recruitment of E2-NEDD8 (UBE2M-NEDD8) thioester to the complex, and optimizing the orientation of proteins in the complex to allow efficient transfer of NEDD8 from the E2 to the cullin substrates (PubMed:25349211). Involved in the release of inhibitory effets of CAND1 on cullin-RING ligase E3 complex assembly and activity. Acts also as an oncogene facilitating malignant transformation and carcinogenic progression (By similarity). {ECO:0000250, ECO:0000269|PubMed:25349211}.; . TISSUE SPECIFICITY: Expressed in pancreas, kidney, placenta, brain and heart. Weakly or not expressed in liver, skeletal muscle and lung. Strongly overexpressed in thyroid tumors, bronchioloalveolar carcinomas, and malignant tissues of squamous cell carcinoma of the oral tongue. Not overexpressed in aggressive adrenocortical carcinomas. {ECO:0000269|PubMed:10777668}.; ovary;sympathetic chain;developmental;colon;parathyroid;skin;uterus;prostate;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;adrenal cortex;blood;skeletal muscle;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;fetal liver;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.35170 0.12971 -0.075159878 47.78839349 7.01619 0.26318 DCUN1D2 9.91158372964289e-05 0.571785087870152 0.428115796292552 defective in cullin neddylation 1 domain containing 2 FUNCTION: Potently stimulates the neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes from the NEDD8- conjugating E2 enzyme UBC12. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity. {ECO:0000269|PubMed:23201271}.; . . ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;endometrium;gum;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;hypothalamus;adrenal cortex;lens;skeletal muscle;lung;placenta;macula lutea;liver;spleen;kidney; . 0.08261 0.10879 0.237127192 68.98443029 13.87438 0.50376 DCUN1D2-AS . . . DCUN1D2 antisense RNA . . . . . . . . . . . DCUN1D3 0.89815410326792 0.100908071139001 0.000937825593079046 defective in cullin neddylation 1 domain containing 3 FUNCTION: Antagonizes DCUN1D1-mediated CUL1 neddylation by sequestering CUL1 at the cell membrane (PubMed:25349211). When overexpressed in transformed cells, may promote mesenchymal to epithelial-like changes and inhibit colony formation in soft agar (PubMed:25349211). {ECO:0000269|PubMed:25349211}.; . TISSUE SPECIFICITY: Tends to be down-regulated in different type of cancers, including lung neuroendocrine carcinoma, thyroid Huerthle cell carcinoma and lung squamous cell carcinoma. {ECO:0000269|PubMed:25349211}.; unclassifiable (Anatomical System);meninges;heart;cartilage;skin;uterus;breast;lung;pia mater;placenta;visual apparatus;kidney;dura mater;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.73842 . -0.449946534 24.00330267 14.05127 0.51000 DCUN1D4 0.160650285832102 0.836138461652558 0.00321125251534041 defective in cullin neddylation 1 domain containing 4 . . . lymphoreticular;smooth muscle;ovary;sympathetic chain;developmental;colon;parathyroid;skin;retina;uterus;prostate;whole body;cerebral cortex;endometrium;bone;thyroid;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;heart;tongue;skeletal muscle;bile duct;pia mater;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;medulla oblongata;subthalamic nucleus;hypothalamus;globus pallidus;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.29277 . -0.251530012 35.42108988 17.88872 0.62462 DCUN1D5 0.97199487015266 0.0279683620960282 3.67677513122128e-05 defective in cullin neddylation 1 domain containing 5 . . . ovary;developmental;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;oesophagus;endometrium;larynx;bone;thyroid;testis;brain;pineal gland;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;head and neck;cervix;kidney;mammary gland;stomach; whole brain;testis - interstitial;occipital lobe;testis - seminiferous tubule;tumor;testis;ciliary ganglion;parietal lobe; 0.59345 . -0.009020804 52.8544468 16.76179 0.58913 DCX 0.863196407367064 0.136385112073834 0.000418480559102346 doublecortin FUNCTION: Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May be part with PAFAH1B1/LIS-1 of overlapping, but distinct, signaling pathways that promote neuronal migration. {ECO:0000269|PubMed:22359282}.; DISEASE: Lissencephaly, X-linked 1 (LISX1) [MIM:300067]: A classic lissencephaly characterized by mental retardation and seizures that are more severe in male patients. Affected boys show an abnormally thick cortex with absent or severely reduced gyri. Clinical manifestations include feeding problems, abnormal muscular tone, seizures and severe to profound psychomotor retardation. Female patients display a less severe phenotype referred to as 'doublecortex'. {ECO:0000269|PubMed:11468322, ECO:0000269|PubMed:12552055, ECO:0000269|PubMed:9489699, ECO:0000269|PubMed:9489700, ECO:0000269|PubMed:9668176, ECO:0000269|PubMed:9817918}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Subcortical band heterotopia X-linked (SBHX) [MIM:300067]: SBHX is a mild brain malformation of the lissencephaly spectrum. It is characterized by bilateral and symmetric plates or bands of gray matter found in the central white matter between the cortex and cerebral ventricles, cerebral convolutions usually appearing normal. {ECO:0000269|PubMed:10369164, ECO:0000269|PubMed:10441340, ECO:0000269|PubMed:10807542, ECO:0000269|PubMed:11175293, ECO:0000269|PubMed:11601509, ECO:0000269|PubMed:12390976, ECO:0000269|PubMed:9618162, ECO:0000269|PubMed:9989615}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving DCX is found in lissencephaly. Translocation t(X;2)(q22.3;p25.1).; TISSUE SPECIFICITY: Highly expressed in neuronal cells of fetal brain (in the majority of cells of the cortical plate, intermediate zone and ventricular zone), but not expressed in other fetal tissues. In the adult, highly expressed in the brain frontal lobe, but very low expression in other regions of brain, and not detected in heart, placenta, lung, liver, skeletal muscles, kidney and pancreas.; unclassifiable (Anatomical System);heart;ovary;tongue;parathyroid;skeletal muscle;skin;uterus;whole body;lung;frontal lobe;placenta;bone;visual apparatus;brain;aorta; superior cervical ganglion;fetal brain;ciliary ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.89424 0.79984 -0.09720619 46.20193442 11.70059 0.42420 DCXR 3.46544861989814e-05 0.585315151241433 0.414650194272368 dicarbonyl/L-xylulose reductase FUNCTION: Catalyzes the NADPH-dependent reduction of several pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L- xylulose. Participates in the uronate cycle of glucose metabolism. May play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules.; . TISSUE SPECIFICITY: Highly expressed in kidney, liver and epididymis. In the epididymis, it is mainly expressed in the proximal and distal sections of the corpus region. Weakly or not expressed in brain, lung, heart, spleen and testis. {ECO:0000269|PubMed:10385429, ECO:0000269|PubMed:11882650}.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;atrium;whole body;bone;testis;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;kidney;mammary gland;stomach; whole brain;thalamus;prostate;adipose tissue;liver;prefrontal cortex;kidney;cerebellum; 0.07516 0.15472 0.03689118 56.64071715 118.21228 2.36520 DDA1 0.893417441694708 0.105528697483812 0.00105386082148011 DET1 and DDB1 associated 1 FUNCTION: May be involved in ubiquitination and subsequent proteasomal degradation of target proteins. Component of the DDD- E2 complexes which may provide a platform for interaction with CUL4A and WD repeat proteins. {ECO:0000269|PubMed:17452440}.; . . lymphoreticular;smooth muscle;ovary;colon;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;iris;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;skeletal muscle;pancreas;lung;placenta;hippocampus;liver;alveolus;spleen;kidney;mammary gland;stomach;peripheral nerve;thymus; whole brain;amygdala;occipital lobe;testis - interstitial;testis - seminiferous tubule;heart;placenta;temporal lobe;prefrontal cortex;testis;pons; 0.16008 0.11253 -0.009020804 52.8544468 4.72747 0.17190 DDAH1 0.168276873038356 0.817661907086799 0.014061219874845 dimethylarginine dimethylaminohydrolase 1 FUNCTION: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.; . TISSUE SPECIFICITY: Detected in brain, liver, kidney and pancreas, and at low levels in skeletal muscle. {ECO:0000269|PubMed:10493931}.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;brain;artery;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; amygdala;medulla oblongata;thalamus;occipital lobe;hypothalamus;temporal lobe;prefrontal cortex;globus pallidus;caudate nucleus;kidney;pons;parietal lobe;cingulate cortex; 0.50094 . -0.095386216 46.48502005 77.4528 1.85100 DDAH2 0.842139471278318 0.157247262666088 0.000613266055594 dimethylarginine dimethylaminohydrolase 2 FUNCTION: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation. {ECO:0000269|PubMed:10493931}.; . TISSUE SPECIFICITY: Detected in heart, placenta, lung, liver, skeletal muscle, kidney and pancreas, and at very low levels in brain. {ECO:0000269|PubMed:10493931}.; . . 0.20933 . -0.05129383 49.75819769 117.75523 2.35946 DDB1 0.999992284151209 7.71584878795479e-06 3.09127025579941e-15 damage specific DNA binding protein 1 FUNCTION: Required for DNA repair. Binds to DDB2 to form the UV- damaged DNA-binding protein complex (the UV-DDB complex). The UV- DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the DCX E3 ubiquitin- protein ligase complex is determined by the variable substrate recognition component recruited by DDB1. DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR). May also play a role in ubiquitination of CDKN1B/p27kip when associated with CUL4 and SKP2. {ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:15448697, ECO:0000269|PubMed:15882621, ECO:0000269|PubMed:16260596, ECO:0000269|PubMed:16407242, ECO:0000269|PubMed:16407252, ECO:0000269|PubMed:16473935, ECO:0000269|PubMed:16482215, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:16940174, ECO:0000269|PubMed:17041588, ECO:0000269|PubMed:17079684, ECO:0000269|PubMed:18332868, ECO:0000269|PubMed:18381890, ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:19966799, ECO:0000269|PubMed:22118460, ECO:0000269|PubMed:25043012, ECO:0000269|PubMed:25108355}.; . . ovary;skin;retina;bone marrow;prostate;ganglion;frontal lobe;cochlea;endometrium;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;pineal body;spinal cord;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach; superior cervical ganglion;adrenal gland;placenta;adrenal cortex; 0.37499 0.17803 -1.111360919 6.717386176 20.58446 0.69962 DDB2 0.00511790717237921 0.989233412076804 0.0056486807508169 damage specific DNA binding protein 2 FUNCTION: Required for DNA repair. Binds to DDB1 to form the UV- damaged DNA-binding protein complex (the UV-DDB complex). The UV- DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as the substrate recognition module for the DCX (DDB1- CUL4-X-box) E3 ubiquitin-protein ligase complex DDB1-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1). The DDB1-CUL4- ROC1 complex may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. The DDB1-CUL4-ROC1 complex also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. Isoform D1 and isoform D2 inhibit UV-damaged DNA repair. {ECO:0000269|PubMed:10882109, ECO:0000269|PubMed:11278856, ECO:0000269|PubMed:11705987, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:12944386, ECO:0000269|PubMed:14751237, ECO:0000269|PubMed:15882621, ECO:0000269|PubMed:16260596, ECO:0000269|PubMed:16473935, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:9892649}.; DISEASE: Xeroderma pigmentosum complementation group E (XP-E) [MIM:278740]: An autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. The skin develops marked freckling and other pigmentation abnormalities. XP-E patients show a mild phenotype with minimal or no neurologic features. {ECO:0000269|PubMed:8798680}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed; with highest levels in corneal endothelium and lowest levels in brain. Isoform D1 is highly expressed in brain and heart. Isoform D2, isoform D3 and isoform D4 are weakly expressed. {ECO:0000269|PubMed:14751237}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;blood;lens;skeletal muscle;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;kidney;stomach; atrioventricular node; 0.16639 0.39887 -0.0274281 51.65723048 34.55038 1.05471 DDC 4.60661229193956e-05 0.962101654731751 0.0378522791453294 dopa decarboxylase FUNCTION: Catalyzes the decarboxylation of L-3,4- dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine.; DISEASE: Aromatic L-amino-acid decarboxylase deficiency (AADCD) [MIM:608643]: An inborn error in neurotransmitter metabolism that leads to combined serotonin and catecholamine deficiency. It causes developmental and psychomotor delay, poor feeding, lethargy, ptosis, intermittent hypothermia, gastrointestinal disturbances. The onset is early in infancy and inheritance is autosomal recessive. {ECO:0000269|PubMed:14991824, ECO:0000269|PubMed:15079002, ECO:0000269|Ref.12}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);small intestine;islets of Langerhans;colon;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;macula lutea;liver;testis;spleen;kidney;pineal gland;stomach;peripheral nerve; dorsal root ganglion;fetal liver;testis - interstitial;testis - seminiferous tubule;liver;kidney;trigeminal ganglion;skeletal muscle;parietal lobe; 0.54794 0.41033 0.376678994 75.50719509 385.01199 4.13493 DDC-AS1 . . . DDC antisense RNA 1 . . . . . . . . . . . DDHD1 0.968458213705181 0.0315417694915699 1.68032491801915e-08 DDHD domain containing 1 FUNCTION: Phospholipase that hydrolyzes phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid. The different isoforms may change the substrate specificity. {ECO:0000269|PubMed:22922100}.; . TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in brain, spleen and lung. Only expressed in cerebellum in fetal brain. {ECO:0000269|PubMed:9488669}.; ovary;salivary gland;intestine;colon;skin;uterus;whole body;bone;testis;germinal center;brain;spinal ganglion;unclassifiable (Anatomical System);cartilage;pharynx;blood;skeletal muscle;breast;bile duct;lung;cornea;placenta;visual apparatus;hippocampus;liver;alveolus;spleen;kidney;mammary gland;aorta; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.39470 0.10565 -0.066061882 48.77919321 745.06279 5.41743 DDHD2 3.09639823750121e-08 0.980244081582287 0.0197558874537301 DDHD domain containing 2 FUNCTION: Phospholipase that hydrolyzes preferentially phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid, and phosphatidylethanolamine. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4- phosphate (PI(4)P), phosphatidylinositol 5-phosphate (PI(5)P) and possibly phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). May be involved in the maintenance of the endoplasmic reticulum and/or Golgi structures. May regulate the transport between Golgi apparatus and plasma membrane. {ECO:0000269|PubMed:11788596, ECO:0000269|PubMed:20932832, ECO:0000269|PubMed:22922100}.; DISEASE: Spastic paraplegia 54, autosomal recessive (SPG54) [MIM:615033]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. Complicated forms are recognized by additional variable features including spastic quadriparesis, seizures, dementia, amyotrophy, extrapyramidal disturbance, cerebral or cerebellar atrophy, optic atrophy, and peripheral neuropathy, as well as by extra neurological manifestations. SPG54 patients have delayed psychomotor development, intellectual disability, and early-onset spasticity of the lower limbs. Brain MRI shows a thin corpus callosum and periventricular white matter lesions. {ECO:0000269|PubMed:23176823}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:11788596}.; . . 0.10756 0.08920 -0.154246007 42.22694032 1643.59444 7.49122 DDI1 5.48151682948122e-06 0.432614991974524 0.567379526508646 DNA damage inducible 1 homolog 1 . . . unclassifiable (Anatomical System);uterus;medulla oblongata;lung;heart;testis;skin; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.03898 0.09943 0.775339069 87.13729653 239.4094 3.34292 DDI2 0.941088127387327 0.0589021964376019 9.67617507157841e-06 DNA damage inducible 1 homolog 2 . . . unclassifiable (Anatomical System);uterus;lymph node;lung;larynx;thyroid;liver;colon;head and neck;germinal center;stomach; . 0.19590 . -0.361761279 28.6329323 34.10402 1.04538 DDIAS . . . DNA damage induced apoptosis suppressor FUNCTION: May be an anti-apoptotic protein involved in DNA repair or cell survival. {ECO:0000269|PubMed:24214091}.; . TISSUE SPECIFICITY: Highly expressed in colorectal and lung cancer tissues. {ECO:0000269|PubMed:24214091}.; . . 0.56579 0.07455 0.161677043 64.96225525 . . DDIT3 0.515502016999664 0.466918167191914 0.017579815808422 DNA damage inducible transcript 3 FUNCTION: Multifunctional transcription factor in ER stress response. Plays an essential role in the response to a wide variety of cell stresses and induces cell cycle arrest and apoptosis in response to ER stress. Plays a dual role both as an inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and as an activator of other genes. Acts as a dominant-negative regulator of C/EBP-induced transcription: dimerizes with members of the C/EBP family, impairs their association with C/EBP binding sites in the promoter regions, and inhibits the expression of C/EBP regulated genes. Positively regulates the transcription of TRIB3, IL6, IL8, IL23, TNFRSF10B/DR5, PPP1R15A/GADD34, BBC3/PUMA, BCL2L11/BIM and ERO1L. Negatively regulates; expression of BCL2 and MYOD1, ATF4-dependent transcriptional activation of asparagine synthetase (ASNS), CEBPA-dependent transcriptional activation of hepcidin (HAMP) and CEBPB-mediated expression of peroxisome proliferator-activated receptor gamma (PPARG). Inhibits the canonical Wnt signaling pathway by binding to TCF7L2/TCF4, impairing its DNA-binding properties and repressing its transcriptional activity. Plays a regulatory role in the inflammatory response through the induction of caspase-11 (CASP4/CASP11) which induces the activation of caspase-1 (CASP1) and both these caspases increase the activation of pro-IL1B to mature IL1B which is involved in the inflammatory response. {ECO:0000269|PubMed:15322075, ECO:0000269|PubMed:15775988, ECO:0000269|PubMed:16434966, ECO:0000269|PubMed:17709599, ECO:0000269|PubMed:18940792, ECO:0000269|PubMed:19672300, ECO:0000269|PubMed:20829347, ECO:0000269|PubMed:20876114, ECO:0000269|PubMed:22761832}.; DISEASE: Myxoid liposarcoma (MXLIPO) [MIM:613488]: A soft tissue tumor that tends to occur in the limbs (especially the thigh) of patients ranging in age from 35 to 55 years. It is defined by the presence of a hypocellular spindle cell proliferation set in a myxoid background, often with mucin pooling. Lipoblasts tend to be small and often monovacuolated and to cluster around vessels or at the periphery of the lesion. {ECO:0000269|PubMed:7503811}. Note=The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving DDIT3 has been found in a patient with malignant myxoid liposarcoma. Translocation t(12;16)(q13;p11) with FUS (PubMed:7503811). {ECO:0000269|PubMed:7503811}.; . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;placenta;duodenum;kidney;stomach;aorta;thymus; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.36676 0.37749 0.237127192 68.98443029 126.57588 2.45103 DDIT4 0.0194954678096794 0.900930471281047 0.079574060909274 DNA damage inducible transcript 4 FUNCTION: Regulates cell growth, proliferation and survival via inhibition of the activity of the mammalian target of rapamycin complex 1 (mTORC1). Inhibition of mTORC1 is mediated by a pathway that involves DDIT4/REDD1, AKT1, the TSC1-TSC2 complex and the GTPase RHEB. Plays an important role in responses to cellular energy levels and cellular stress, including responses to hypoxia and DNA damage. Regulates p53/TP53-mediated apoptosis in response to DNA damage via its effect on mTORC1 activity. Its role in the response to hypoxia depends on the cell type; it mediates mTORC1 inhibition in fibroblasts and thymocytes, but not in hepatocytes (By similarity). Required for mTORC1-mediated defense against viral protein synthesis and virus replication (By similarity). Inhibits neuronal differentiation and neurite outgrowth mediated by NGF via its effect on mTORC1 activity. Required for normal neuron migration during embryonic brain development. Plays a role in neuronal cell death. {ECO:0000250, ECO:0000269|PubMed:15545625, ECO:0000269|PubMed:15632201, ECO:0000269|PubMed:15988001, ECO:0000269|PubMed:17005863, ECO:0000269|PubMed:17379067, ECO:0000269|PubMed:19557001, ECO:0000269|PubMed:20166753, ECO:0000269|PubMed:21460850}.; . TISSUE SPECIFICITY: Broadly expressed, with lowest levels in brain, skeletal muscle and intestine. Up-regulated in substantia nigra neurons from Parkinson disease patients (at protein level). {ECO:0000269|PubMed:11884613, ECO:0000269|PubMed:12453409, ECO:0000269|PubMed:17005863, ECO:0000269|PubMed:17379067}.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;choroid;skin;retina;uterus;prostate;cerebral cortex;endometrium;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;muscle;pharynx;blood;breast;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; pancreas;lung;olfactory bulb;atrioventricular node; 0.45428 0.19244 -0.317668748 31.45789101 23.39129 0.77993 DDIT4L 0.000548864407256177 0.463220729535119 0.536230406057625 DNA damage inducible transcript 4 like FUNCTION: Inhibits cell growth by regulating the TOR signaling pathway upstream of the TSC1-TSC2 complex and downstream of AKT1. {ECO:0000269|PubMed:15545625, ECO:0000269|PubMed:15632201}.; . TISSUE SPECIFICITY: Up-regulated in atherosclerotic plaques relative to healthy segments of the same artery. {ECO:0000269|PubMed:15308555}.; unclassifiable (Anatomical System);heart;skeletal muscle;retina;uterus;prostate;whole body;lung;endometrium;placenta;liver;testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.24166 0.12971 -0.117432389 44.89266336 939.34436 5.94095 DDN 0.986679783745218 0.0133199743949755 2.41859806345241e-07 dendrin FUNCTION: Promotes apoptosis of kidney glomerular podocytes. Podocytes are highly specialized cells essential to the ultrafiltration of blood, resulting in the extraction of urine and the retention of protein (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in brain and kidney. Expressed in kidney glomerular capillary loops (at protein level). {ECO:0000269|PubMed:17251388, ECO:0000269|PubMed:18356187}.; . . 0.52105 0.16145 -0.003562597 53.72729417 2045.49656 8.34048 DDO 3.15188059629111e-11 0.043096820841424 0.956903179127057 D-aspartate oxidase FUNCTION: Selectively catalyzes the oxidative deamination of D- aspartate and its N-methylated derivative, N-methyl D-aspartate.; . . . . 0.05518 0.17566 2.245250033 98.19532909 272.58588 3.54007 DDOST 0.134980573644975 0.860596218049823 0.00442320830520201 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit FUNCTION: Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains.; DISEASE: Congenital disorder of glycosylation 1R (CDG1R) [MIM:614507]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:22305527}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.19607 0.24955 -0.400392389 26.85185185 96.64121 2.12397 DDR1 0.0264778570642852 0.973501139528955 2.1003406759627e-05 discoidin domain receptor tyrosine kinase 1 FUNCTION: Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell attachment to the extracellular matrix, remodeling of the extracellular matrix, cell migration, differentiation, survival and cell proliferation. Collagen binding triggers a signaling pathway that involves SRC and leads to the activation of MAP kinases. Regulates remodeling of the extracellular matrix by up-regulation of the matrix metalloproteinases MMP2, MMP7 and MMP9, and thereby facilitates cell migration and wound healing. Required for normal blastocyst implantation during pregnancy, for normal mammary gland differentiation and normal lactation. Required for normal ear morphology and normal hearing (By similarity). Promotes smooth muscle cell migration, and thereby contributes to arterial wound healing. Also plays a role in tumor cell invasion. Phosphorylates PTPN11. {ECO:0000250, ECO:0000269|PubMed:12065315, ECO:0000269|PubMed:16234985, ECO:0000269|PubMed:16337946, ECO:0000269|PubMed:19401332, ECO:0000269|PubMed:20093046, ECO:0000269|PubMed:20432435, ECO:0000269|PubMed:20884741, ECO:0000269|PubMed:21044884, ECO:0000269|PubMed:9659899}.; . TISSUE SPECIFICITY: Detected in T-47D, MDA-MB-175 and HBL-100 breast carcinoma cells, A-431 epidermoid carcinoma cells, SW48 and SNU-C2B colon carcinoma cells and Hs 294T melanoma cells (at protein level). Expressed at low levels in most adult tissues and is highest in the brain, lung, placenta and kidney. Lower levels of expression are detected in melanocytes, heart, liver, skeletal muscle and pancreas. Abundant in breast carcinoma cell lines. In the colonic mucosa, expressed in epithelia but not in the connective tissue of the lamina propria. In the thyroid gland, expressed in the epithelium of the thyroid follicles. In pancreas, expressed in the islets of Langerhans cells, but not in the surrounding epithelial cells of the exocrine pancreas. In kidney, expressed in the epithelia of the distal tubules. Not expressed in connective tissue, endothelial cells, adipose tissue, muscle cells or cells of hematopoietic origin. {ECO:0000269|PubMed:7845687, ECO:0000269|PubMed:7848919, ECO:0000269|PubMed:8247543}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pineal body;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;thymus;cerebellum; . 0.61508 0.34305 -1.258440978 5.307855626 158.21916 2.74709 DDR1-AS1 . . . DDR1 antisense RNA 1 (head to head) . . . . . . . . . . . DDR2 0.990992372312246 0.00900762389289038 3.79486313552698e-09 discoidin domain receptor tyrosine kinase 2 FUNCTION: Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up-regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing. {ECO:0000269|PubMed:16186104, ECO:0000269|PubMed:16186108, ECO:0000269|PubMed:17665456, ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20004161, ECO:0000269|PubMed:20564243, ECO:0000269|PubMed:20734453, ECO:0000269|PubMed:9659899}.; DISEASE: Spondyloepimetaphyseal dysplasia short limb-hand type (SEMD-SL) [MIM:271665]: A bone disease characterized by short- limbed dwarfism, a narrow chest with pectus excavatum, brachydactyly in the hands and feet, a characteristic craniofacial appearance and premature calcifications. The radiological findings are distinctive and comprise short long bones throughout the skeleton with striking epiphyses that are stippled, flattened and fragmented and flared, irregular metaphyses. Platyspondyly in the spine with wide intervertebral spaces is observed and some vertebral bodies are pear-shaped with central humps, anterior protrusions and posterior scalloping. {ECO:0000269|PubMed:19110212, ECO:0000269|PubMed:20223752}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in osteocytes, osteoblastic cells in subchondral bone, bone lining cells, tibia and cartilage (at protein level). Detected at high levels in heart and lung, and at low levels in brain, placenta, liver, skeletal muscle, pancreas, and kidney. {ECO:0000269|PubMed:17665456, ECO:0000269|PubMed:20564243, ECO:0000269|PubMed:8247548}.; . . 0.85011 0.13490 -0.775187015 13.05142722 110.07197 2.27991 DDRGK1 0.000149759368683589 0.867604737319463 0.132245503311853 DDRGK domain containing 1 FUNCTION: Protein which interacts with the E3 UFM1-protein ligase UFL1 and one of its substrates TRIP4 and is required for TRIP4 ufmylation. Through TRIP4 ufmylation may regulate nuclear receptors-mediated transcription (PubMed:25219498). May play a role in NF-kappa-B-mediated transcription through regulation of the phosphorylation and the degradation of NFKBIB, the inhibitor of NF-kappa-B (PubMed:23675531). May also play a role in the cellular response to endoplasmic reticulum stress (By similarity). {ECO:0000250|UniProtKB:Q80WW9, ECO:0000269|PubMed:23675531, ECO:0000269|PubMed:25219498}.; . TISSUE SPECIFICITY: Widely expressed (at protein level). In the brain, highest levels in medulla oblongata, followed by cerebral cortex, cerebellum and frontal lobe. {ECO:0000269|PubMed:20018847, ECO:0000269|PubMed:20036718}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;urinary;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;liver;head and neck;cervix;mammary gland;stomach;thymus; whole brain;dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion; 0.05466 0.08678 0.17280645 65.75843359 528.96149 4.69287 DDT 0.412925623752845 0.467337655904677 0.119736720342478 D-dopachrome tautomerase FUNCTION: Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI).; . . myocardium;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; prostate;liver;kidney; 0.12933 . . . . . DDTL 0.41672757218518 0.465952450541871 0.117319977272949 D-dopachrome tautomerase-like FUNCTION: May have lyase activity. {ECO:0000305}.; . . unclassifiable (Anatomical System);ovary;fovea centralis;choroid;lens;skin;retina;optic nerve;lung;frontal lobe;placenta;macula lutea;liver;testis;kidney;mammary gland; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.09611 0.07772 . . 68.74548 1.71706 DDTP1 . . . D-dopachrome tautomerase pseudogene 1 . . . . . . . . . . . DDU . . . dermo-distortive urticaria . . . . . . . . . . . DDX1 0.998606607070136 0.00139339273307385 1.96790090663434e-10 DEAD/H-box helicase 1 FUNCTION: Acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang nuclease activity. Possesses ATPase activity on various RNA, but not DNA polynucleotides. May play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. Together with RELA, acts as a coactivator to enhance NF-kappa-B-mediated transcriptional activation. Acts as a positive transcriptional regulator of cyclin CCND2 expression. Binds to the cyclin CCND2 promoter region. Associates with chromatin at the NF- kappa-B promoter region via association with RELA. Binds to poly(A) RNA. May be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB: together with archease (ZBTB8OS), acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation (PubMed:24870230). Required for HIV-1 Rev function as well as for HIV-1 replication. Binds to the RRE sequence of HIV-1 mRNAs. {ECO:0000269|PubMed:12183465, ECO:0000269|PubMed:15567440, ECO:0000269|PubMed:18335541, ECO:0000269|PubMed:18710941, ECO:0000269|PubMed:20573827, ECO:0000269|PubMed:24870230}.; . TISSUE SPECIFICITY: Highest levels of transcription in 2 retinoblastoma cell lines and in tissues of neuroectodermal origin including the retina, brain, and spinal cord. {ECO:0000269|PubMed:7689221}.; ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;frontal lobe;bone;thyroid;pituitary gland;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;breast;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;head and neck;kidney;mammary gland;stomach;thymus; subthalamic nucleus;occipital lobe;medulla oblongata;thalamus;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.33127 0.49952 -0.600630256 18.06440198 70.55865 1.74750 DDX3P1 . . . DEAD-box helicase 3 pseudogene 1 . . . . . . . . . . . DDX3P2 . . . DEAD-box helicase 3 pseudogene 2 . . . . . . . . . . . DDX3P3 . . . DEAD-box helicase 3 pseudogene 3 . . . . . . . . . . . DDX3X 0.99893006535012 0.00106992217358162 1.24762984802235e-08 DEAD-box helicase 3, X-linked FUNCTION: Multifunctional ATP-dependent RNA helicase. The ATPase activity can be stimulated by various ribo- and deoxynucleic acids indicative for a relaxed substrate specificity. In vitro can unwind partially double-stranded DNA with a preference for 5'- single-stranded DNA overhangs. Is involved in several steps of gene expression, such as transcription, mRNA maturation, mRNA export and translation. However, the exact mechanisms are not known and some functions may be specific for a subset of mRNAs. Involved in transcriptional regulation. Can enhance transcription from the CDKN1A/WAF1 promoter in a SP1-dependent manner. Found associated with the E-cadherin promoter and can down-regulate transcription from the promoter. Involved in regulation of translation initiation. Proposed to be involved in positive regulation of translation such as of cyclin E1/CCNE1 mRNA and specifically of mRNAs containing complex secondary structures in their 5'UTRs; these functions seem to require RNA helicase activity. Specifically promotes translation of a subset of viral and cellular mRNAs carrying a 5'proximal stem-loop structure in their 5'UTRs and cooperates with the eIF4F complex. Proposed to act prior to 43S ribosomal scanning and to locally destabilize these RNA structures to allow recognition of the mRNA cap or loading onto the 40S subunit. After association with 40S ribosomal subunits seems to be involved in the functional assembly of 80S ribosomes; the function seems to cover translation of mRNAs with structured and non-structured 5'UTRs and is independent of RNA helicase activity. Also proposed to inhibit cap-dependent translation by competetive interaction with EIF4E which can block the EIF4E:EIF4G complex formation. Proposed to be involved in stress response and stress granule assembly; the function is independent of RNA helicase activity and seems to involve association with EIF4E. May be involved in nuclear export of specific mRNAs but not in bulk mRNA export via interactions with XPO1 and NXF1. Also associates with polyadenylated mRNAs independently of NXF1. Associates with spliced mRNAs in an exon junction complex (EJC)-dependent manner and seems not to be directly involved in splicing. May be involved in nuclear mRNA export by association with DDX5 and regulating its nuclear location. Involved in innate immune signaling promoting the production of type I interferon (IFN-alpha and IFN-beta); proposed to act as viral RNA sensor, signaling intermediate and transcriptional coactivator. Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, plays a role of scaffolding adapter that links IKBKE and IRF3 and coordinates their activation. Also found associated with IFNB promoters; the function is independent of IRF3. Can bind to viral RNAs and via association with MAVS/IPS1 and DDX58/RIG-I is thought to induce signaling in early stages of infection. Involved in regulation of apoptosis. May be required for activation of the intrinsic but inhibit activation of the extrinsic apoptotic pathway. Acts as an antiapoptotic protein through association with GSK3A/B and BIRC2 in an apoptosis antagonizing signaling complex; activation of death receptors promotes caspase-dependent cleavage of BIRC2 and DDX3X and relieves the inhibition. May be involved in mitotic chromosome segregation. Appears to be a prime target for viral manipulations. Hepatitis B virus (HBV) polymerase and possibly vaccinia virus (VACV) protein K7 inhibit IFNB induction probably by dissociating DDX3X from TBK1 or IKBKE. Is involved in hepatitis C virus (HCV) replication; the function may involve the association with HCV core protein. HCV core protein inhibits the IPS1-dependent function in viral RNA sensing and may switch the function from a INFB inducing to a HCV replication mode. Involved in HIV-1 replication. Acts as a cofactor for XPO1-mediated nuclear export of incompletely spliced HIV-1 Rev RNAs. {ECO:0000269|PubMed:10329544, ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:16301996, ECO:0000269|PubMed:16818630, ECO:0000269|PubMed:17357160, ECO:0000269|PubMed:17667941, ECO:0000269|PubMed:18264132, ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18628297, ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:18846110, ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:20375222, ECO:0000269|PubMed:20657822, ECO:0000269|PubMed:20837705, ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:21589879, ECO:0000269|PubMed:21730191, ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:22323517, ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:23478265}.; . . . . 0.75981 0.33817 -0.119252484 44.53880632 2.33675 0.07955 DDX3Y 0.773099529750687 0.219203822810655 0.00769664743865812 DEAD-box helicase 3, Y-linked FUNCTION: Probable ATP-dependent RNA helicase. May play a role in spermatogenesis.; . TISSUE SPECIFICITY: Testis-specific. Expressed predominantly in spermatogonia. {ECO:0000269|PubMed:15294876}.; medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;frontal lobe;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;artery;tonsil;unclassifiable (Anatomical System);trophoblast;heart;cartilage;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach;aorta; testis - interstitial;testis;trigeminal ganglion; 0.40886 . . . 8.11899 0.29800 DDX4 0.998516038315595 0.0014839616379786 4.64268163008862e-11 DEAD-box helicase 4 FUNCTION: May play a role in germ cell development. May play a role in sperm motility. {ECO:0000269|PubMed:10920202, ECO:0000269|PubMed:21034600}.; . TISSUE SPECIFICITY: Expressed only in ovary and testis. Expressed in migratory primordial germ cells in the region of the gonadal ridge in both sexes. {ECO:0000269|PubMed:10920202}.; unclassifiable (Anatomical System);testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;cerebellum peduncles;testis;ciliary ganglion;skeletal muscle; 0.68619 0.10786 -0.310388054 32.14791224 861.19729 5.72325 DDX5 0.99745409892001 0.00254588017961783 2.09003723082169e-08 DEAD-box helicase 5 FUNCTION: Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for estrogen receptor ESR1 and androgen receptor AR. Increases ESR1 AF-1 domain-mediated transactivation and ESR1 AF-1 and AF-2 domains transcriptional synergistic activity. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specicic manner; the function probbaly involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms. {ECO:0000269|PubMed:10409727, ECO:0000269|PubMed:11250900, ECO:0000269|PubMed:12527917, ECO:0000269|PubMed:15298701, ECO:0000269|PubMed:15660129, ECO:0000269|PubMed:17011493, ECO:0000269|PubMed:17960593, ECO:0000269|PubMed:18829551, ECO:0000269|PubMed:19718048, ECO:0000269|PubMed:21343338}.; . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;cochlea;endometrium;gum;bone;testis;germinal center;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; adrenal cortex;white blood cells;ciliary ganglion; 0.99513 0.25991 -0.712684326 14.49634348 217.31003 3.18659 DDX6 0.998985995919041 0.00101399313499006 1.09459686175165e-08 DEAD-box helicase 6 FUNCTION: In the process of mRNA degradation, may play a role in mRNA decapping.; . TISSUE SPECIFICITY: Abundantly expressed in most tissues.; unclassifiable (Anatomical System);lymph node;heart;hypothalamus;developmental;colon;blood;skin;skeletal muscle;bone marrow;breast;uterus;prostate;lung;frontal lobe;nasopharynx;thyroid;placenta;hippocampus;liver;testis;head and neck;spleen;germinal center;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.57067 0.10408 -0.205617011 38.57631517 51.00128 1.40660 DDX6P1 . . . DEAD-box helicase 6 pseudogene 1 . . . . . . . . . . . DDX6P2 . . . DEAD-box helicase 6 pseudogene 2 . . . . . . . . . . . DDX10 5.41642779880176e-11 0.810476188958052 0.189523810987784 DEAD-box helicase 10 FUNCTION: Putative ATP-dependent RNA helicase.; . TISSUE SPECIFICITY: High in testis but widely expressed.; unclassifiable (Anatomical System);smooth muscle;lymph node;ovary;muscle;adrenal cortex;colon;blood;skeletal muscle;breast;uterus;prostate;whole body;lung;endometrium;nasopharynx;bone;thyroid;placenta;visual apparatus;liver;testis;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;testis - interstitial;pons;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion; 0.40748 0.09833 -0.483123186 22.78249587 110.0097 2.27841 DDX10P1 . . . DEAD-box helicase 10 pseudogene 1 . . . . . . . . . . . DDX10P2 . . . DEAD-box helicase 10 pseudogene 2 . . . . . . . . . . . DDX11 . . . DEAD/H-box helicase 11 FUNCTION: DNA helicase involved in cellular proliferation. Possesses DNA-dependent ATPase and helicase activities. This helicase translocates on single-stranded DNA in the 5' to 3' direction in the presence of ATP and, to a lesser extent, dATP. Its unwinding activity requires a 5'-single-stranded region for helicase loading, since flush-ended duplex structures do not support unwinding. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended to 500 bp by RPA or the cohesion establishment factor, the Ctf18-RFC (replication factor C) complex activities. Stimulates the flap endonuclease activity of FEN1. Required for normal sister chromatid cohesion. Required for recruitment of bovine papillomavirus type 1 regulatory protein E2 to mitotic chrmosomes and for viral genome maintenance. Required for maintaining the chromosome segregation and is essential for embryonic development and the prevention of aneuploidy. May function during either S, G2, or M phase of the cell cycle. Binds to both single- and double-stranded DNA. {ECO:0000269|PubMed:10648783, ECO:0000269|PubMed:17105772, ECO:0000269|PubMed:17189189, ECO:0000269|PubMed:18499658, ECO:0000269|PubMed:9013641}.; . TISSUE SPECIFICITY: Highly expressed in spleen, B-cells, thymus, testis, ovary, small intestine, and pancreas. Very low expression seen in the brain. Expressed in dividing cells and/or cells undergoing high levels of recombination. No expression is seen in cells signaled to terminally differentiate. Expressed in keratinocyte growth factor-stimulated cells but not in serum, EGF and IL1-beta-treated keratinocytes. {ECO:0000269|PubMed:8798685, ECO:0000269|PubMed:9013641}.; lymphoreticular;smooth muscle;ovary;colon;skin;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;skeletal muscle;pancreas;lung;epididymis;nasopharynx;placenta;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis;atrioventricular node; 0.18559 0.13755 1.030617021 91.10639302 2109.31265 8.45409 DDX11-AS1 . . . DDX11 antisense RNA 1 . . . . . . . . . . . DDX11L1 . . . DEAD/H-box helicase 11 like 1 . . . . . . . . . . . DDX11L2 . . . DEAD/H-box helicase 11 like 2 . . . . . . . . . . . DDX11L3 . . . DEAD/H-box helicase 11 like 3 . . . . . . . . . . . DDX11L4 . . . DEAD/H-box helicase 11 like 4 . . . . . . . . . . . DDX11L5 . . . DEAD/H-box helicase 11 like 5 . . . . . . . . . . . DDX11L6 . . . DEAD/H-box helicase 11 like 6 . . . . . . . . . . . DDX11L7 . . . DEAD/H-box helicase 11 like 7 . . . . . . . . . . . DDX11L8 . . . DEAD/H-box helicase 11 like 8 FUNCTION: Putative DNA helicase. {ECO:0000250}.; . . . . . . . . . . DDX11L9 . . . DEAD/H-box helicase 11 like 9 . . . . . . . . . . . DDX11L10 . . . DEAD/H-box helicase 11 like 10 . . . . . . . . . . . DDX11L11 . . . DEAD/H-box helicase 11 like 11 . . . . . . . . . . . DDX11L13 . . . DEAD/H-box helicase 11 like 13 . . . . . . . . . . . DDX11L15 . . . DEAD/H-box helicase 11 like 15 . . . . . . . . . . . DDX11L16 . . . DEAD/H-box helicase 11 like 16 . . . . . . . . . . . DDX12P . . . DEAD/H-box helicase 12, pseudogene FUNCTION: DNA helicase involved in cellular proliferation. Probably required for maintaining the chromosome segregation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Only expressed in proliferating tissues. {ECO:0000269|PubMed:9013641}.; lymphoreticular;smooth muscle;ovary;colon;skin;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);heart;cartilage;blood;skeletal muscle;pancreas;lung;epididymis;nasopharynx;placenta;liver;cervix;kidney;stomach;thymus; . . 0.11668 . . . . DDX17 . . . DEAD-box helicase 17 FUNCTION: RNA-dependent ATPase activity. Involved in transcriptional regulation. Transcriptional coactivator for estrogen receptor ESR1. Increases ESR1 AF-1 domain-mediated transactivation. Synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and probably involved in skeletal muscle differentiation. Required for zinc-finger antiviral protein ZC3HAV1-mediated mRNA degradation. {ECO:0000269|PubMed:11250900, ECO:0000269|PubMed:15298701, ECO:0000269|PubMed:17011493, ECO:0000269|PubMed:17226766, ECO:0000269|PubMed:18334637, ECO:0000269|PubMed:19718048}.; . TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;cochlea;endometrium;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; . 0.95209 0.27727 -0.516085732 21.20193442 42.19846 1.22768 DDX18 0.839996435028735 0.159998245619693 5.31935157221361e-06 DEAD-box helicase 18 FUNCTION: Probable RNA-dependent helicase.; . . smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;placenta;head and neck;kidney;stomach;aorta; subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;white blood cells;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.82639 0.11156 0.99945266 90.6935598 3948.76824 12.42883 DDX18P1 . . . DEAD-box helicase 18 pseudogene 1 . . . . . . . . . . . DDX18P2 . . . DEAD-box helicase 18 pseudogene 2 . . . . . . . . . . . DDX18P3 . . . DEAD-box helicase 18 pseudogene 3 . . . . . . . . . . . DDX18P4 . . . DEAD-box helicase 18 pseudogene 4 . . . . . . . . . . . DDX18P5 . . . DEAD-box helicase 18 pseudogene 5 . . . . . . . . . . . DDX18P6 . . . DEAD-box helicase 18 pseudogene 6 . . . . . . . . . . . DDX19A 0.92306130907744 0.0769348326657447 3.85825681516408e-06 DEAD-box helicase 19A FUNCTION: ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19 functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;endometrium;bone;testis;amniotic fluid;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;skeletal muscle; 0.24809 0.11676 -0.139478553 43.29440906 14.42148 0.52000 DDX19B 0.0357117798271904 0.962682615629402 0.00160560454340718 DEAD-box helicase 19B FUNCTION: ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19B functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins.; . . lymphoreticular;medulla oblongata;ovary;colon;skin;retina;bone marrow;uterus;prostate;endometrium;gum;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;muscle;blood;lens;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.19860 0.61718 0.038710339 56.92380278 185.18047 2.95514 DDX20 4.187651178714e-07 0.819148759173008 0.180850822061874 DEAD-box helicase 20 FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs). {ECO:0000269|PubMed:18984161}.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.18370 0.27351 1.734373503 96.61476763 3458.89491 11.30256 DDX20P1 . . . DEAD-box helicase 20 pseudogene 1 . . . . . . . . . . . DDX21 0.998039215836896 0.00196078371049027 4.52613831743852e-10 DEAD-box helicase 21 FUNCTION: RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) (PubMed:25470060). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs (PubMed:25470060). In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification. Required for rRNA 2'- O-methylation, possibly by promoting the recruitment of late- acting snoRNAs SNORD56 and SNORD58 with pre-ribosomal complexes (PubMed:25470060, PubMed:25477391). In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes (PubMed:25470060). Functions as cofactor for JUN-activated transcription: required for phosphorylation of JUN at 'Ser-77' (PubMed:11823437, PubMed:25260534). Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase) (PubMed:9461305). Involved in rRNA processing (PubMed:14559904, PubMed:18180292). {ECO:0000269|PubMed:11823437, ECO:0000269|PubMed:14559904, ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:25260534, ECO:0000269|PubMed:25470060, ECO:0000269|PubMed:25477391, ECO:0000269|PubMed:9461305}.; . . lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; superior cervical ganglion;fetal liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.39141 0.22891 -0.400392389 26.85185185 95.1412 2.10446 DDX23 0.999558303316101 0.000441696683409468 4.90045594761989e-13 DEAD-box helicase 23 FUNCTION: Involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. {ECO:0000269|PubMed:18425142}.; . . lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;thymus;cerebellum; placenta;white blood cells;thymus; 0.42523 0.13467 -0.979072682 8.752064166 16.04533 0.56782 DDX24 0.221392665021272 0.778537613743995 6.97212347333898e-05 DEAD-box helicase 24 FUNCTION: ATP-dependent RNA helicase. {ECO:0000305}.; . TISSUE SPECIFICITY: Ubiquitous. Most abundant in heart and brain, but with lowest levels in thymus and small intestine.; lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;urinary;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; amygdala;whole brain;superior cervical ganglion;thalamus;occipital lobe;testis - interstitial;medulla oblongata;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;adrenal cortex;pons;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.17786 0.15314 1.337468036 94.28520878 365.64888 4.04721 DDX25 4.23433637836541e-09 0.194323761465986 0.805676234299677 DEAD-box helicase 25 FUNCTION: ATP-dependent RNA helicase. Required for mRNA export and translation regulation during spermatid development (By similarity). {ECO:0000250, ECO:0000269|PubMed:10608860}.; . TISSUE SPECIFICITY: Highly expressed in the Leydig and germ cells of the testis and weakly expressed in the pituitary and hypothalamus. {ECO:0000269|PubMed:10608860, ECO:0000269|Ref.2}.; unclassifiable (Anatomical System);uterus;medulla oblongata;lung;frontal lobe;adrenal gland;visual apparatus;testis;brain;retina; amygdala;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis; 0.56905 0.10553 -0.448125345 24.19202642 21.62223 0.72710 DDX27 0.250170092340815 0.749829465385797 4.42273388661246e-07 DEAD-box helicase 27 FUNCTION: Probable ATP-dependent RNA helicase. Component of the nucleolar ribosomal RNA (rRNA) processing machinery that regulates 3' end formation of ribosomal 47S rRNA (PubMed:25825154). {ECO:0000269|PubMed:25825154}.; . . . . 0.17829 0.10926 -0.062423436 48.86765747 4157.56288 12.79754 DDX28 0.0348937305744781 0.957019844781937 0.00808642464358476 DEAD-box helicase 28 FUNCTION: Plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function (PubMed:25683708, PubMed:25683715). May be involved in RNA processing or transport. Has RNA and Mg(2+)-dependent ATPase activity (PubMed:11350955). {ECO:0000269|PubMed:11350955, ECO:0000269|PubMed:25683708, ECO:0000269|PubMed:25683715}.; . TISSUE SPECIFICITY: Expressed in all tissues tested, including brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, leukocytes, colon, small intestine, ovary and prostate. {ECO:0000269|PubMed:11350955}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;alveolus;spleen;kidney;mammary gland;stomach;thymus; placenta;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex; 0.07529 0.08396 0.308721233 72.59966973 103.76005 2.20032 DDX31 2.75575676923568e-06 0.999194111289686 0.000803132953544579 DEAD-box helicase 31 FUNCTION: Probable ATP-dependent RNA helicase (By similarity). Plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1 (PubMed:23019224). {ECO:0000250, ECO:0000269|PubMed:23019224}.; . TISSUE SPECIFICITY: Weakly or undetectably expressed in normal organs. Up-regulated in renal cell carcinoma. {ECO:0000269|PubMed:23019224}.; unclassifiable (Anatomical System);uterus;lung;placenta;iris;testis;stomach; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.24736 0.07666 1.004917985 90.78792168 604.47797 4.97674 DDX39A 0.843485807212333 0.156392019896649 0.000122172891017904 DEAD-box helicase 39A FUNCTION: Isoform 1: Involved in pre-mRNA splicing. Required for the export of mRNA out of the nucleus. {ECO:0000269|PubMed:15047853, ECO:0000269|PubMed:17548965}.; . TISSUE SPECIFICITY: Detected in testis, and at lower levels in brain, kidney, lung, thymus, spleen and salivary gland. {ECO:0000269|PubMed:15047853}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;tumor;trigeminal ganglion;skeletal muscle;thymus;cerebellum;bone marrow; 0.19290 0.12971 -0.580403979 18.58928993 124.14286 2.42456 DDX39AP1 . . . DEAD-box helicase 39A pseudogene 1 . . . . . . . . . . . DDX39B 0.997728044454765 0.0022718773046267 7.82406078456496e-08 DEAD-box helicase 39B FUNCTION: Involved in nuclear export of spliced and unspliced mRNA. Assembling component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription- independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. May undergo several rounds of ATP hydrolysis during assembly of TREX to drive subsequent loading of components such as ALYREF/THOC and CHTOP onto mRNA. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Also associates with pre-mRNA independent of ALYREF/THOC4 and the THO complex. Involved in the nuclear export of intronless mRNA; the ATP-bound form is proposed to recruit export adapter ALYREF/THOC4 to intronless mRNA; its ATPase activity is cooperatively stimulated by RNA and ALYREF/THOC4 and ATP hydrolysis is thought to trigger the dissociation from RNA to allow the association of ALYREF/THOC4 and the NXF1-NXT1 heterodimer. Involved in transcription elongation and genome stability.; . . . . 0.60041 . -0.119252484 44.53880632 52.2488 1.42845 DDX39B-AS1 . . . DDX39B antisense RNA 1 . . . . . . . . . . . DDX39BP1 . . . DEAD-box helicase 39B pseudogene 1 . . . . . . . . . . . DDX39BP2 . . . DEAD-box helicase 39B pseudogene 2 . . . . . . . . . . . DDX41 0.000984379620636701 0.998505065554851 0.000510554824512249 DEAD-box helicase 41 FUNCTION: Probable ATP-dependent RNA helicase. Is required during post-transcriptional gene expression. May be involved in pre-mRNA splicing.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; whole brain;temporal lobe;prefrontal cortex;pons; 0.22452 0.25806 -1.089312628 7.047652748 219.21549 3.20188 DDX42 0.999995783745318 4.21625467837612e-06 3.50544738783894e-15 DEAD-box helicase 42 FUNCTION: ATP-dependent RNA helicase. Binds to partially double- stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single-strand binding proteins. Mediates also RNA duplex formation thereby displacing the single-strand RNA binding protein. ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands. Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis-stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm. {ECO:0000269|PubMed:16397294, ECO:0000269|PubMed:19377511}.; . TISSUE SPECIFICITY: Expressed in several cell lines (at protein level). Expressed in liver, lung, tonsil, thymus, muscle and pancreatic islets. {ECO:0000269|PubMed:10727850, ECO:0000269|PubMed:16397294}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;cerebral cortex;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;medulla oblongata;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.32154 0.11852 -0.997481928 8.47487615 58.4695 1.54889 DDX43 6.82016832652361e-05 0.998964934139212 0.000966864177523239 DEAD-box helicase 43 . . TISSUE SPECIFICITY: Expressed in testis. Expressed in many tumors of various histological types at a level that is 100-fold higher than the level observed in normal tissues except testis. {ECO:0000269|PubMed:10919659}.; . . 0.24998 0.09700 0.711016566 85.72776598 3031.70851 10.45812 DDX43P1 . . . DEAD-box helicase 43 pseudogene 1 . . . . . . . . . . . DDX43P2 . . . DEAD-box helicase 43 pseudogene 2 . . . . . . . . . . . DDX43P3 . . . DEAD-box helicase 43 pseudogene 3 . . . . . . . . . . . DDX46 0.999997754157555 2.24584244514244e-06 3.09463779972705e-17 DEAD-box helicase 46 FUNCTION: Plays an essential role in splicing, either prior to, or during splicing A complex formation. {ECO:0000269|PubMed:12234937}.; . . ovary;developmental;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;larynx;bone;thyroid;pituitary gland;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion;globus pallidus;white blood cells;ciliary ganglion;atrioventricular node;parietal lobe; 0.71667 0.11044 -1.111360919 6.717386176 12.79601 0.46528 DDX47 1.14178044496829e-08 0.771651387339608 0.228348601242587 DEAD-box helicase 47 FUNCTION: Involved in apoptosis. May have a role in rRNA processing and mRNA splicing. Associates with pre-rRNA precursors. {ECO:0000269|PubMed:15977068, ECO:0000269|PubMed:16963496}.; . . ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;urinary;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;colon;choroid;fovea centralis;vein;uterus;whole body;atrium;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach; testis - interstitial;testis;white blood cells; 0.32686 0.12744 -0.911109353 9.961075725 66.67569 1.68421 DDX49 3.23743409567641e-10 0.290018089279951 0.709981910396305 DEAD-box helicase 49 . . . ovary;salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;tongue;muscle;urinary;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; cerebellum peduncles;pons;trigeminal ganglion;skeletal muscle; 0.11149 0.11691 -0.176292081 40.56381222 365.25289 4.04439 DDX50 0.000758121354986356 0.999211411597423 3.04670475903669e-05 DEAD-box helicase 50 . . . . . 0.78356 0.13377 -0.556537043 19.72753008 134.49024 2.52188 DDX50P1 . . . DEAD-box helicase 50 pseudogene 1 . . . . . . . . . . . DDX50P2 . . . DEAD-box helicase 50 pseudogene 2 . . . . . . . . . . . DDX51 2.27756414069476e-10 0.418488133053364 0.58151186671888 DEAD-box helicase 51 FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. {ECO:0000250}.; . . ovary;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;larynx;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;spinal cord;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;head and neck;cervix;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.12940 0.10964 0.161677043 64.96225525 2903.26584 10.21578 DDX52 1.44174737874652e-10 0.5528929124902 0.447107087365625 DEAD-box helicase 52 . . . ovary;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;skeletal muscle;bile duct;lung;nasopharynx;placenta;liver;amnion;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.18508 0.25158 0.04598748 57.47817882 187.23376 2.97139 DDX53 0.825398952735036 0.173795631158949 0.000805416106015381 DEAD-box helicase 53 . . TISSUE SPECIFICITY: Expressed in testis. Wide expression in various cancer tissues and cancer cell lines. {ECO:0000269|PubMed:11922625}.; . . 0.01993 0.10291 0.42259095 77.22929936 2068.65942 8.38312 DDX54 1.04148957531094e-06 0.99934160948413 0.000657349026294398 DEAD-box helicase 54 FUNCTION: Has RNA-dependent ATPase activity. Represses the transcriptional activity of nuclear receptors. {ECO:0000269|PubMed:12466272}.; . . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;optic nerve;oesophagus;endometrium;thyroid;bone;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; pons;skeletal muscle; 0.16664 0.11639 0.36555769 74.7287096 1623.89906 7.45152 DDX55 6.00815721436613e-06 0.970504582467271 0.0294894093755151 DEAD-box helicase 55 FUNCTION: Probable ATP-binding RNA helicase.; . . sympathetic chain;colon;parathyroid;skin;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;skeletal muscle;pancreas;lung;epididymis;placenta;visual apparatus;liver;cervix;kidney;stomach;aorta; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.12682 0.11357 -0.108334733 45.57088936 2452.48731 9.21367 DDX55P1 . . . DEAD-box helicase 55 pseudogene 1 . . . . . . . . . . . DDX56 3.51574131414912e-06 0.940960768181996 0.0590357160766897 DEAD-box helicase 56 FUNCTION: May play a role in later stages of the processing of the pre-ribosomal particles leading to mature 60S ribosomal subunits. Has intrinsic ATPase activity.; . TISSUE SPECIFICITY: Detected in heart, brain, liver, pancreas, placenta and lung.; myocardium;medulla oblongata;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;medulla oblongata;subthalamic nucleus;ciliary ganglion;pons;trigeminal ganglion;parietal lobe; 0.17022 0.11773 -0.532670911 20.78320359 703.39126 5.27223 DDX58 1.08821627751063e-14 0.250604873548455 0.749395126451534 DEXD/H-box helicase 58 FUNCTION: Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. Its ligands include: 5'- triphosphorylated ssRNA and dsRNA and short dsRNA (<1 kb in length). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential. Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity. A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity. Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK- related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV). It also detects rotavirus and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration. {ECO:0000269|PubMed:15208624, ECO:0000269|PubMed:15708988, ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453, ECO:0000269|PubMed:16153868, ECO:0000269|PubMed:17190814, ECO:0000269|PubMed:18636086, ECO:0000269|PubMed:19122199, ECO:0000269|PubMed:19211564, ECO:0000269|PubMed:19576794, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:21742966}.; DISEASE: Singleton-Merten syndrome 2 (SGMRT2) [MIM:616298]: A form of Singleton-Merten syndrome, an autosomal dominant disorder characterized by marked aortic calcification, dental anomalies, osteopenia, acro-osteolysis, and to a lesser extend glaucoma, psoriasis, muscle weakness, and joint laxity. Additional clinical manifestations include particular facial characteristics and abnormal joint and muscle ligaments. SGMRT2 is an atypical form characterized by variable expression of glaucoma, aortic calcification, and skeletal abnormalities, without dental anomalies. {ECO:0000269|PubMed:25620203}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Present in vascular smooth cells (at protein level). {ECO:0000269|PubMed:15219805}.; . . 0.68732 0.21527 0.051446096 57.53715499 1360.70863 6.92315 DDX59 0.00107791458335624 0.988247924173157 0.0106741612434874 DEAD-box helicase 59 . DISEASE: Orofaciodigital syndrome 5 (OFD5) [MIM:174300]: A form of orofaciodigital syndrome, a group of heterogeneous disorders characterized by malformations of the oral cavity, face and digits, and associated phenotypic abnormalities that lead to the delineation of various subtypes. OFD5 patients show the core features of cleft palate, lobulated tongue, and polydactyly. Additional features include frontal bossing and intellectual disability. {ECO:0000269|PubMed:23972372}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in fibroblasts (at protein level). {ECO:0000269|PubMed:23972372}.; unclassifiable (Anatomical System);smooth muscle;heart;ovary;islets of Langerhans;hypothalamus;adrenal cortex;colon;parathyroid;lens;skin;uterus;prostate;whole body;lung;bone;placenta;visual apparatus;pituitary gland;liver;testis;cervix;spleen;germinal center;kidney;brain;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;adrenal cortex;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex; 0.05633 0.10449 1.067416815 91.66666667 1872.45459 7.95919 DDX60 3.67465810588512e-10 0.999999718637689 2.80994844805097e-07 DEXD/H-box helicase 60 FUNCTION: Positively regulates DDX58/RIG-I- and IFIH1/MDA5- dependent type I interferon and interferon inducible gene expression in response to viral infection. Binds ssRNA, dsRNA and dsDNA and can promote the binding of DDX58/RIG-I to dsRNA. Exhibits antiviral activity against hepatitis C virus and vesicular stomatitis virus (VSV). {ECO:0000269|PubMed:21478870, ECO:0000269|PubMed:21791617}.; . TISSUE SPECIFICITY: Brain, lymph node, prostate, stomach, thyroid, tongue, trachea, uterus, skeletal muscle, spleen, kidney, liver and small intestine. {ECO:0000269|PubMed:21791617}.; . . 0.12481 0.09080 -0.314266677 31.69379571 875.60425 5.75739 DDX60L 8.16952566679389e-30 0.000634233257219368 0.999365766742781 DEAD-box helicase 60-like . . . colon;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cerebellum cortex;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;head and neck;cervix;kidney;stomach;thymus; . 0.07164 0.07270 2.618410593 98.77919321 7052.9357 17.95780 DEAF1 0.000193157379315308 0.975124961835423 0.0246818807852618 DEAF1, transcription factor FUNCTION: Transcription factor that binds to sequence with multiple copies of 5'-TTC[CG]G-3' present in its own promoter and that of the HNRPA2B1 gene. Down-regulates transcription of these genes. Binds to the retinoic acid response element (RARE) 5'- AGGGTTCACCGAAAGTTCA-3'. Activates the proenkephalin gene independently of promoter binding, probably through protein- protein interaction. When secreted, behaves as an inhibitor of cell proliferation, by arresting cells in the G0 or G1 phase. Required for neural tube closure and skeletal patterning. Regulates epithelial cell proliferation and side-branching in the mammary gland. Controls the expression of peripheral tissue antigens in pancreatic lymph nodes. Isoform 1 displays greater transcriptional activity than isoform 4. Isoform 4 may inhibit transcriptional activity of isoform 1 by interacting with isoform 1 and retaining it in the cytoplasm. Transcriptional activator of EIF4G3. {ECO:0000269|PubMed:10521432, ECO:0000269|PubMed:11427895, ECO:0000269|PubMed:11705868, ECO:0000269|PubMed:18826651, ECO:0000269|PubMed:19668219, ECO:0000269|PubMed:24726472}.; DISEASE: Mental retardation, autosomal dominant 24 (MRD24) [MIM:615828]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:21076407, ECO:0000269|PubMed:24726472}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in various tissues and cells such as in peripheral mononuclear cells and hormone-secreting pituitary cells. Expression in pancreatic lymph nodes of patients with type 1 diabetes is 20 times higher than in healthy controls. Highly expressed in fetal and adult brain. {ECO:0000269|PubMed:19668219, ECO:0000269|PubMed:24726472}.; ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;larynx;thyroid;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; amygdala;whole brain;subthalamic nucleus;cerebellum peduncles;temporal lobe;prefrontal cortex;globus pallidus;pons;cingulate cortex;cerebellum; 0.16145 0.10001 -0.887242605 10.43288511 86.78056 1.98955 DEC1 0.000209448507541278 0.293886756081133 0.705903795411326 deleted in esophageal cancer 1 FUNCTION: Candidate tumor suppressor. {ECO:0000269|PubMed:10612805}.; . . . . 0.03485 . 0.435547893 77.45340882 13.82711 0.50177 DECR1 1.66744250187555e-05 0.668478438469521 0.331504887105461 2,4-dienoyl-CoA reductase 1, mitochondrial FUNCTION: Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3- enoyl-CoA.; . TISSUE SPECIFICITY: Heart = liver = pancreas > kidney >> skeletal muscle = lung. {ECO:0000269|PubMed:7818482}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;atrium;whole body;ganglion;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;spinal cord;pharynx;blood;skeletal muscle;breast;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; testis - interstitial;fetal liver;adipose tissue;testis - seminiferous tubule;adrenal gland;liver;testis;kidney; 0.46712 0.93559 -0.0274281 51.65723048 37.40416 1.11371 DECR2 3.46558531082418e-09 0.0497633601714559 0.950236636362959 2,4-dienoyl-CoA reductase 2, peroxisomal FUNCTION: Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19- docosaheptaenoyl-CoA, suggesting that it does not constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid.; . . ovary;colon;skin;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;urinary;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;spleen;cervix;kidney;stomach; testis - seminiferous tubule;liver;kidney;skeletal muscle; 0.30516 0.13063 -0.244249595 36.17008728 109.53122 2.27353 DEDD 0.869503209773923 0.130127430521994 0.00036935970408298 death effector domain containing FUNCTION: A scaffold protein that directs CASP3 to certain substrates and facilitates their ordered degradation during apoptosis. May also play a role in mediating CASP3 cleavage of KRT18. Regulates degradation of intermediate filaments during apoptosis. May play a role in the general transcription machinery in the nucleus and might be an important regulator of the activity of GTF3C3. Inhibits DNA transcription in vitro (By similarity). {ECO:0000250, ECO:0000269|PubMed:12235123}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in testis. {ECO:0000269|PubMed:9832420}.; . . 0.48110 0.13398 -0.05129383 49.75819769 50.2724 1.39373 DEDD2 0.284523203677244 0.693582716001562 0.0218940803211938 death effector domain containing 2 FUNCTION: May play a critical role in death receptor-induced apoptosis and may target CASP8 and CASP10 to the nucleus. May regulate degradation of intermediate filaments during apoptosis. May play a role in the general transcription machinery in the nucleus and might be an important regulator of the activity of GTF3C3.; . TISSUE SPECIFICITY: Expressed in most tissues. High levels were found in liver, kidney, heart, ovary, spleen, testes, skeletal muscle and peripheral blood leukocytes. Expression was absent or low in colon and small intestine. Expression is relatively high in the tumor cell lines chronic myologenous leukemia K-562 and the colorectal adenocarcinoma SW480. Expression is moderate in the cervical carcinoma HeLa, the Burkitt's lymphoma Raji, the lung carcinoma A-549, and the melanoma G-361. In contrast, two leukemia cell lines, HL-60 (promyelocytic leukemia) and MOLT-4 (lymphoblastic leukemia), show relatively low levels. {ECO:0000269|PubMed:11741985, ECO:0000269|PubMed:11965497}.; ovary;salivary gland;colon;skin;bone marrow;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;alveolus;spleen;cervix;stomach; cerebellum; 0.13208 . -0.205617011 38.57631517 28.84673 0.92173 DEF6 0.976824149100722 0.0231749053676814 9.45531596541017e-07 DEF6, guanine nucleotide exchange factor FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which plays a role in the activation of Rho GTPases RAC1, RhoA and CDC42. Can regulate cell morphology in cooperation with activated RAC1. Plays a role in Th2 (T helper cells) development and/or activation, perhaps by interfering with ZAP70 signaling (By similarity). {ECO:0000250, ECO:0000269|PubMed:12651066, ECO:0000269|PubMed:15023524}.; . TISSUE SPECIFICITY: Broadly expressed in the immune system and can be detected in T and B-cells. {ECO:0000269|PubMed:12651066}.; ovary;colon;substantia nigra;skin;bone marrow;retina;uterus;prostate;optic nerve;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;nervous;blood;pancreas;lung;nasopharynx;placenta;head and neck;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;white blood cells; 0.55197 0.11305 0.240763792 69.36777542 500.14117 4.59071 DEF8 0.389991487866254 0.609924177090884 8.43350428619118e-05 differentially expressed in FDCP 8 homolog (mouse) . . . lymphoreticular;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;lacrimal gland;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;aorta;peripheral nerve; superior cervical ganglion; 0.16968 0.10329 -0.021969881 52.14673272 223.67964 3.23402 DEFA1 . . . defensin alpha 1 FUNCTION: Defensin 1 and defensin 2 have antibacterial, fungicide and antiviral activities. Has antimicrobial activity against Gram- negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. {ECO:0000269|PubMed:15616305, ECO:0000269|PubMed:17452329}.; . . . . . 0.04893 . . . . DEFA1A3 . . . defensin alpha 1 and alpha 3, variable copy number locus FUNCTION: Defensin 1 and defensin 2 have antibacterial, fungicide and antiviral activities. Has antimicrobial activity against Gram- negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. {ECO:0000269|PubMed:15616305, ECO:0000269|PubMed:17452329}.; . . . . 0.01910 0.04893 . . . . DEFA1B . . . defensin alpha 1B FUNCTION: Defensin 1 and defensin 2 have antibacterial, fungicide and antiviral activities. Has antimicrobial activity against Gram- negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. {ECO:0000269|PubMed:15616305, ECO:0000269|PubMed:17452329}.; . . . . . . . . . . DEFA3 0.489152996997351 0.432923060935593 0.0779239420670562 defensin alpha 3 FUNCTION: Defensin 2 and defensin 3 have antibiotic, fungicide and antiviral activities. Has antimicrobial activity against Gram- negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. {ECO:0000269|PubMed:15616305, ECO:0000269|PubMed:15894545, ECO:0000269|PubMed:17452329, ECO:0000269|PubMed:2006422}.; . . unclassifiable (Anatomical System);cartilage;heart;umbilical cord;blood;skin;skeletal muscle;bone marrow;uterus;lung;bone;placenta;liver;testis;spleen;kidney;thymus; . 0.01910 0.04893 . . 10.33361 0.37696 DEFA4 0.271968353462833 0.634937792548525 0.0930938539886421 defensin alpha 4 FUNCTION: Has antimicrobial activity against Gram-negative bacteria, and to a lesser extent also against Gram-positive bacteria and fungi. Protects blood cells against infection with HIV-1 (in vitro). Inhibits corticotropin (ACTH)-stimulated corticosterone production. {ECO:0000269|PubMed:15616305, ECO:0000269|PubMed:15620707}.; . . uterus;heart;bone;blood;skin;bone marrow; superior cervical ganglion;appendix;pons;trigeminal ganglion;skeletal muscle;bone marrow; 0.11993 . 0.481458261 79.03986789 443.96292 4.38235 DEFA5 0.000100681038440857 0.200800243834708 0.799099075126851 defensin alpha 5 FUNCTION: Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. All DEFA5 peptides exert antimicrobial activities, but their potency is affected by peptide processing. {ECO:0000269|PubMed:12021776, ECO:0000269|PubMed:15616305, ECO:0000269|PubMed:17088326}.; . TISSUE SPECIFICITY: Paneth cells of the small intestine (at protein level). {ECO:0000269|PubMed:12021776}.; optic nerve;small intestine;macula lutea;fovea centralis;choroid;lens;stomach;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.10730 0.03412 -0.005381972 53.50908233 9.08816 0.33262 DEFA6 0.00438946005151902 0.433275333044151 0.56233520690433 defensin alpha 6 FUNCTION: Has very low antimicrobial activity against Gram- negative and Gram-positive bacteria. May protect cells against infection with HIV-1. {ECO:0000269|PubMed:15616305, ECO:0000269|PubMed:17088326}.; . TISSUE SPECIFICITY: Paneth cells of the small intestine.; unclassifiable (Anatomical System);small intestine;stomach; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.55197 0.11305 0.747842143 86.47676339 140.11248 2.58223 DEFA7P . . . defensin alpha 7, pseudogene . . . . . . . . . . . DEFA8P . . . defensin alpha 8, pseudogene . . . . . . . . . . . DEFA9P . . . defensin alpha 9, pseudogene . . . . . . . . . . . DEFA10P . . . defensin alpha 10, pseudogene . . . . . . . . . . . DEFA11P . . . defensin alpha 11, pseudogene . . . . . . . . . . . DEFB1 5.06986674339156e-05 0.138224734122617 0.861724567209949 defensin beta 1 FUNCTION: Has bactericidal activity. {ECO:0000250}.; . TISSUE SPECIFICITY: Blood plasma (at protein level). {ECO:0000269|PubMed:7628632}.; unclassifiable (Anatomical System);uterus;optic nerve;heart;islets of Langerhans;thyroid;colon;kidney;skin;skeletal muscle;stomach; superior cervical ganglion;pancreas;tongue;salivary gland;beta cell islets;liver;ciliary ganglion;kidney;skin; 0.14602 0.25463 -0.073340031 48.11866006 115.80462 2.34077 DEFB4A 0.399812614148335 0.471821032230792 0.128366353620874 defensin beta 4A FUNCTION: Has antibacterial activity. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in the skin and respiratory tract.; hypopharynx;head and neck;stomach; . 0.02791 0.08540 . . 2.11236 0.06961 DEFB4B . . . defensin beta 4B FUNCTION: Has antibacterial activity. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in the skin and respiratory tract.; hypopharynx;head and neck;stomach; . . . . . 40.90308 1.19832 DEFB103A . . . defensin beta 103A FUNCTION: Exhibits antimicrobial activity against Gram-positive bacteria S.aureus and S.pyogenes, Gram-negative bacteria P.aeruginosa and E.coli and the yeast C.albicans. Kills multiresistant S.aureus and vancomycin-resistant E.faecium. No significant hemolytic activity was observed. {ECO:0000269|PubMed:11085990}.; . TISSUE SPECIFICITY: Highly expressed in skin and tonsils, and to a lesser extent in trachea, uterus, kidney, thymus, adenoid, pharynx and tongue. Low expression in salivary gland, bone marrow, colon, stomach, polyp and larynx. No expression in small intestine. {ECO:0000269|PubMed:11085990}.; . . 0.17923 0.31462 . . . . DEFB103B . . . defensin beta 103B FUNCTION: Exhibits antimicrobial activity against Gram-positive bacteria S.aureus and S.pyogenes, Gram-negative bacteria P.aeruginosa and E.coli and the yeast C.albicans. Kills multiresistant S.aureus and vancomycin-resistant E.faecium. No significant hemolytic activity was observed. {ECO:0000269|PubMed:11085990}.; . TISSUE SPECIFICITY: Highly expressed in skin and tonsils, and to a lesser extent in trachea, uterus, kidney, thymus, adenoid, pharynx and tongue. Low expression in salivary gland, bone marrow, colon, stomach, polyp and larynx. No expression in small intestine. {ECO:0000269|PubMed:11085990}.; . . 0.21099 0.22085 . . . . DEFB104A 0.519473453237245 0.415757233087639 0.064769313675116 defensin beta 104A FUNCTION: Has antimicrobial activity. Synergistic effects with lysozyme and DEFB103. {ECO:0000269|PubMed:11481241}.; . TISSUE SPECIFICITY: High expression in the testis. Gastric antrum exhibited relatively high levels. A lower expression is observed in uterus and neutrophils thyroid gland, lung, and kidney. No detectable expression in other tissues tested. {ECO:0000269|PubMed:11481241}.; . . 0.15037 0.13240 0.61192669 82.99716914 0.80248 0.01535 DEFB104B . . . defensin beta 104B FUNCTION: Has antimicrobial activity. Synergistic effects with lysozyme and DEFB103. {ECO:0000269|PubMed:11481241}.; . TISSUE SPECIFICITY: High expression in the testis. Gastric antrum exhibited relatively high levels. A lower expression is observed in uterus and neutrophils thyroid gland, lung, and kidney. No detectable expression in other tissues tested. {ECO:0000269|PubMed:11481241}.; . . 0.11632 0.09963 . . 0.00011 0.00000 DEFB105A 0.436248234904372 0.458260487617288 0.10549127747834 defensin beta 105A FUNCTION: Has antibacterial activity. {ECO:0000305}.; . TISSUE SPECIFICITY: Specifically expressed in testis.; . . 0.05342 0.06800 . . 1.46217 0.05025 DEFB105B . . . defensin beta 105B FUNCTION: Has antibacterial activity. {ECO:0000305}.; . TISSUE SPECIFICITY: Specifically expressed in testis.; . . 0.06924 . . . . . DEFB106A 0.409307651822525 0.468620602323296 0.122071745854179 defensin beta 106A FUNCTION: Has antibacterial activity. {ECO:0000269|PubMed:12600824}.; . TISSUE SPECIFICITY: Expressed specifically in epididymis and lung. {ECO:0000269|PubMed:12600824}.; lung;testis; . 0.03230 . . . 0.99212 0.02539 DEFB106B . . . defensin beta 106B FUNCTION: Has antibacterial activity. {ECO:0000269|PubMed:12600824}.; . TISSUE SPECIFICITY: Expressed specifically in epididymis and lung. {ECO:0000269|PubMed:12600824}.; lung;testis; . 0.00769 0.03441 . . 0.10915 0.00155 DEFB107A . . . defensin beta 107A FUNCTION: Has antibacterial activity. {ECO:0000305}.; . TISSUE SPECIFICITY: Specifically expressed in testis.; . . 0.02704 0.04953 . . 1.84695 0.05835 DEFB107B . . . defensin beta 107B FUNCTION: Has antibacterial activity. {ECO:0000305}.; . TISSUE SPECIFICITY: Specifically expressed in testis.; . . 0.01665 0.05482 . . 514.069 4.64084 DEFB108B 0.0235485404628086 0.543593617933776 0.432857841603415 defensin beta 108B FUNCTION: Has antibacterial activity. {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in testis. Low expression is detected also in liver. {ECO:0000269|PubMed:12600824}.; . . 0.02481 0.05260 1.368844567 94.46803491 2689.92955 9.76404 DEFB108P1 . . . defensin beta 108 pseudogene 1 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . . . . . . . . . . DEFB108P2 . . . defensin beta 108 pseudogene 2 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . . . . . . . . . . DEFB108P3 . . . defensin beta 108 pseudogene 3 . . . . . . . . . . . DEFB108P4 . . . defensin beta 108 pseudogene 4 . . . . . . . . . . . DEFB109P1 . . . defensin beta 109 pseudogene 1 FUNCTION: Has antibacterial activity. {ECO:0000250}.; . . . . . . . . . . DEFB109P1B . . . defensin beta 109 pseudogene 1B FUNCTION: Has antibacterial activity. {ECO:0000250}.; . . . . . . . . . . DEFB109P2 . . . defensin beta 109 pseudogene 2 . . . . . . . . . . . DEFB109P3 . . . defensin beta 109 pseudogene 3 . . . . . . . . . . . DEFB110 0.0332221914618416 0.612957321999274 0.353820486538884 defensin beta 110 FUNCTION: Has antibacterial activity. {ECO:0000250}.; . . . . . . -0.163345027 41.24793583 4.94873 0.18416 DEFB112 4.67296856823663e-05 0.240967016398685 0.758986253915633 defensin beta 112 FUNCTION: Has antibacterial activity. {ECO:0000250}.; . . . . 0.05981 . 0.014844891 54.94810097 10.78375 0.39176 DEFB113 0.000538841057144388 0.269837502531853 0.729623656411003 defensin beta 113 FUNCTION: Has antibacterial activity. {ECO:0000250}.; . . . . 0.04897 . -0.141298762 42.87567823 2.87291 0.10177 DEFB114 0.162703129468739 0.639333426252074 0.197963444279187 defensin beta 114 FUNCTION: Has a salt-sensitive antimicrobial activity against Gram-negative bacteria, including E.coli, Gram-positive, including S.aureus, and fungi, including C.albicans. Binds to and neutralizes bacterial lipopolysaccharides (LPS), abolishing TNF production by macrophages challenged with LPS. Rescues the LPS- induced reduction of sperm motility in vitro and may protect from LPS-induced lethality. {ECO:0000269|PubMed:23482568}.; . TISSUE SPECIFICITY: Expressed in epididymis, predominantly in the caput (at protein level). {ECO:0000269|PubMed:23482568}.; . . 0.01872 0.04453 -0.009020804 52.8544468 3.01781 0.10928 DEFB115 0.0337152856700566 0.615860426984962 0.350424287344981 defensin beta 115 FUNCTION: Has antibacterial activity. {ECO:0000250}.; . . . . . . 0.21326276 67.71644256 11.60987 0.42053 DEFB116 0.00162884060058742 0.457912447378793 0.540458712020619 defensin beta 116 FUNCTION: Has antibacterial activity. {ECO:0000250}.; . . . . 0.00823 . 0.347360312 73.97381458 218.77062 3.19724 DEFB117 . . . defensin beta 117 (pseudogene) . . . . . 0.08991 . . . . . DEFB118 0.0891188757776611 0.764109655042359 0.14677146917998 defensin beta 118 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . TISSUE SPECIFICITY: High-level and epididymis-specific expression. Most abundant in the epithelium of the caput and is also present in the lumen and bound to sperm. Expressed also in pancreas. {ECO:0000269|PubMed:12600824}.; medulla oblongata;lung;epididymis;testis; superior cervical ganglion;testis; 0.07474 0.07271 0.3032669 72.009908 28.42795 0.91021 DEFB119 0.0586265124896855 0.714209077271413 0.227164410238901 defensin beta 119 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . TISSUE SPECIFICITY: Abundant expression in the male reproductive tract only. Abundant expressed in testis and the caput region of epididymis, but low in the corpus region. {ECO:0000269|PubMed:15772680}.; unclassifiable (Anatomical System);medulla oblongata;testis;skeletal muscle; . 0.00629 0.02641 0.461228372 78.46190139 472.36162 4.49840 DEFB121 0.0315382968992368 0.602642949876438 0.365818753224325 defensin beta 121 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . TISSUE SPECIFICITY: Abundant expression in the male reproductive tract only. {ECO:0000269|PubMed:15772680}.; . . 0.03953 0.05763 -0.075159878 47.78839349 4.4497 0.16151 DEFB122 . . . defensin beta 122 (pseudogene) . . . . . . . . . . . DEFB123 0.00636985353515393 0.50806553513838 0.485564611326466 defensin beta 123 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . TISSUE SPECIFICITY: Abundant expression in the male reproductive tract only. Abundant expressed in testis and the caput region of epididymis, but low in the corpus region. {ECO:0000269|PubMed:15772680}.; . . 0.10432 6.59E-3 -0.009020804 52.8544468 0.80248 0.01513 DEFB124 0.18733564893744 0.646516154460666 0.166148196601894 defensin beta 124 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . . . . 0.01024 . 0.768075923 86.8895966 156.30745 2.73290 DEFB125 0.000941817347898508 0.577131591327562 0.421926591324539 defensin beta 125 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . . . . . 0.04674 0.325313577 73.11276244 22.51624 0.75317 DEFB126 0.000723030120606571 0.312945164343282 0.686331805536111 defensin beta 126 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . TISSUE SPECIFICITY: High-level and epididymis-specific expression.; . . 0.01271 . 0.25917371 70.05779665 16.64627 0.58659 DEFB127 7.41963201429962e-06 0.0878274828166775 0.912165097551308 defensin beta 127 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . . . . 0.14052 0.06441 0.657836546 84.27105449 3614.22997 11.64220 DEFB128 0.560121291818518 0.390103257209 0.0497754509724817 defensin beta 128 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . . . . 0.00108 0.02246 1.080382899 91.76102854 63.46985 1.63151 DEFB129 0.0087103445415641 0.574086126700584 0.417203528757852 defensin beta 129 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed specifically in testis. {ECO:0000269|PubMed:12600824}.; lung;testis; testis;atrioventricular node;trigeminal ganglion;skin; 0.28436 0.08761 0.393270925 76.04977589 1335.47977 6.86451 DEFB130 . . . defensin beta 130 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . . . . . . . . . . DEFB131 0.15739801203891 0.636904366206824 0.205697621754266 defensin beta 131 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . TISSUE SPECIFICITY: Highly expressed in testis. Is moderately expressed in the prostate and small intestine. {ECO:0000269|PubMed:12600824}.; . . 0.04816 . 0.591694063 82.45458835 8.97171 0.32951 DEFB132 0.00647477436924981 0.511460670439641 0.482064555191109 defensin beta 132 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . . . . 0.10486 0.08083 1.170393003 92.68105685 24.35412 0.80070 DEFB133 . . . defensin beta 133 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . . . . 0.10611 . . . 96.09507 2.11890 DEFB134 0.0322373411768572 0.607001815206542 0.360760843616601 defensin beta 134 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . . . . . . -0.141298762 42.87567823 5.91894 0.22279 DEFB135 1.31655071986469e-06 0.0617835955249481 0.938215087924332 defensin beta 135 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . . . . . . 0.147123112 64.11299835 371.7432 4.06869 DEFB136 0.0340000990200746 0.617514012146879 0.348485888833046 defensin beta 136 FUNCTION: Has antibacterial activity. {ECO:0000305}.; . . . . . . -0.185391282 39.67916962 2.6816 0.09746 DEFT1P . . . defensin, theta 1 pseudogene . . . . . . . . . . . DEFT1P2 . . . defensin, theta 1 pseudogene 2 . . . . . . . . . . . DEGS1 0.859651068829934 0.138200418653805 0.0021485125162608 delta(4)-desaturase, sphingolipid 1 FUNCTION: Has sphingolipid-delta-4-desaturase activity. Converts D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine). {ECO:0000269|PubMed:11937514}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9188692}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;pituitary gland;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;mesenchyma;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;whole brain;prostate;thyroid;placenta;trigeminal ganglion;skeletal muscle;skin; 0.11956 0.32370 -0.117432389 44.89266336 36.32886 1.08853 DEGS2 0.00586427408044219 0.728224261373734 0.265911464545824 delta(4)-desaturase, sphingolipid 2 FUNCTION: Bifunctional enzyme which acts as both a sphingolipid delta(4)-desaturase and a sphingolipid C4-monooxygenase. {ECO:0000269|PubMed:15063729}.; . TISSUE SPECIFICITY: Highly expressed in skin, intestine and kidney. {ECO:0000269|PubMed:15063729}.; unclassifiable (Anatomical System);heart;islets of Langerhans;colon;blood;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;optic nerve;lung;macula lutea;germinal center;stomach; . 0.07873 0.13991 0.396906589 76.30927105 1118.58419 6.38498 DEK 0.102359186951826 0.890489818662751 0.00715099438542254 DEK proto-oncogene FUNCTION: Involved in chromatin organization. {ECO:0000269|PubMed:17524367}.; DISEASE: Note=A chromosomal aberration involving DEK is found in a subset of acute myeloid leukemia (AML); also known as acute non- lymphocytic leukemia (PubMed:1549122). Translocation t(6;9)(p23;q34) with NUP214/CAN (PubMed:1549122). It results in the formation of a DEK-NUP214 fusion gene (PubMed:1549122). {ECO:0000269|PubMed:1549122}.; TISSUE SPECIFICITY: Ubiquitous. Expressed at relatively high levels.; myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;bile duct;pancreas;lung;pia mater;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; thyroid;tumor;white blood cells; 0.89842 . -0.381986487 27.68931352 22.40799 0.75211 DENND1A 0.904475401385969 0.0955245428573144 5.5756716785144e-08 DENN domain containing 1A FUNCTION: Guanine nucleotide exchange factor (GEF) regulating clathrin-mediated endocytosis through RAB35 activation. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB35 into its active GTP-bound form. Regulates clathrin-mediated endocytosis of synaptic vesicles. {ECO:0000269|PubMed:20154091, ECO:0000269|PubMed:20937701}.; . . . . 0.11907 0.08380 -1.456898556 3.862939372 223.58404 3.23355 DENND1B 0.636578248354416 0.363133538308913 0.000288213336671119 DENN domain containing 1B FUNCTION: Guanine nucleotide exchange factor (GEF) for RAB35. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB35 into its active GTP-bound form. May play a role in clathrin- mediated endocytosis. {ECO:0000269|PubMed:20154091, ECO:0000269|PubMed:20937701}.; . TISSUE SPECIFICITY: Highly expressed in dendritic and natural killer cells and at lower levels in other myeloid lineage cells and in pituitary. Significantly up-regulated in effector memory T- cells as compared with naive T-cells. {ECO:0000269|PubMed:20032318}.; unclassifiable (Anatomical System);lymph node;ovary;colon;blood;bone marrow;breast;bile duct;pancreas;lung;nasopharynx;thyroid;placenta;liver;testis;germinal center;kidney;brain;artery;aorta;stomach; superior cervical ganglion; 0.04511 0.09045 -0.427900189 25.14744043 57.41583 1.52674 DENND1C 0.0360059989669383 0.963928827184334 6.51738487276034e-05 DENN domain containing 1C FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB8A, RAB13 and RAB35. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. {ECO:0000269|PubMed:20154091, ECO:0000269|PubMed:20937701}.; . . . . 0.12173 . 1.249272484 93.46543996 1257.08513 6.68696 DENND2A 0.972231280413339 0.02776870733505 1.22516114986237e-08 DENN domain containing 2A FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP- bound form. May play a role in late endosomes back to trans-Golgi network/TGN transport. {ECO:0000269|PubMed:20937701}.; . . ovary;adrenal medulla;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;skeletal muscle;breast;lung;placenta;hippocampus;visual apparatus;liver;spleen;kidney;stomach;cerebellum; ciliary ganglion;pons; 0.09707 . -0.812021021 12.07242274 3762.56226 11.99657 DENND2C 1.70408687930238e-07 0.998215437229738 0.00178439236157372 DENN domain containing 2C FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP- bound form. {ECO:0000269|PubMed:20937701}.; . . . . 0.62273 0.10215 1.004917985 90.78792168 2159.38676 8.54844 DENND2D 1.02695227272951e-05 0.937883885823626 0.0621058446536467 DENN domain containing 2D FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP- bound form. {ECO:0000269|PubMed:20937701}.; . TISSUE SPECIFICITY: In bronchial mucosa, mainly expressed in ciliated and basal epithelial cells and weakly in alveolar cells (at protein level). Tends to be down-regulated in lung cancers, immortalized bronchial epithelial cell lines and precancerous lesions. {ECO:0000269|PubMed:23182661}.; unclassifiable (Anatomical System);nasopharynx;placenta;hypopharynx;blood;head and neck;skeletal muscle;stomach;bone marrow; lymph node;white blood cells;tonsil;thymus; 0.08627 0.10027 -0.290161348 33.33923095 77.48048 1.85134 DENND3 0.0171730327867355 0.982825328346388 1.63886687613821e-06 DENN domain containing 3 FUNCTION: Guanine nucleotide exchange factor (GEF) activating RAB12. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB12 into its active GTP-bound form. Thereby, may play a role in protein transport from recycling endosomes to lysosomes regulating, for instance, the degradation of the transferrin receptor. {ECO:0000269|PubMed:20937701}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;alveolus;amnion;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;skeletal muscle; 0.09826 0.08644 -0.564052047 19.0552017 1817.59938 7.86039 DENND4A 0.00135462134565384 0.998645269117007 1.09537339629208e-07 DENN domain containing 4A FUNCTION: Probable guanine nucleotide exchange factor (GEF) which may activate RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP- bound form. According to PubMed:8056341, it may bind to ISRE-like element (interferon-stimulated response element) of MYC P2 promoter. {ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:8056341}.; . TISSUE SPECIFICITY: Expressed ubiquitously. Highest expression in bone marrow, medium in peripheral blood lymphocytes and lowest in spleen. In brain, breast, and prostate, higher expression was seen in normal cells than in tumor cells. Expression is regulated in a growth- and cell cycle-dependent manner. {ECO:0000269|PubMed:12906859}.; . . 0.70803 0.10819 -0.92407637 9.766454352 347.16472 3.95019 DENND4B 0.999987069079939 1.29309200589591e-05 2.20016745846499e-15 DENN domain containing 4B FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. {ECO:0000269|PubMed:20937701}.; . . smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;amnion;hypopharynx;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; thalamus;subthalamic nucleus;prefrontal cortex;globus pallidus;skeletal muscle;parietal lobe;cingulate cortex;cerebellum; 0.38773 0.10021 -2.456612937 0.996697334 2406.58842 9.11113 DENND4C 0.406967594357299 0.593032404613816 1.02888499429931e-09 DENN domain containing 4C FUNCTION: Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin. {ECO:0000269|PubMed:20937701}.; . . ovary;skin;retina;bone marrow;uterus;prostate;endometrium;thyroid;pituitary gland;testis;bladder;brain;unclassifiable (Anatomical System);islets of Langerhans;blood;skeletal muscle;pancreas;lung;placenta;liver;head and neck;cervix;kidney;mammary gland;stomach; ciliary ganglion; 0.38649 . -0.957327604 9.017456947 1816.18274 7.85903 DENND5A 0.991775356411996 0.00822464356284012 2.51639600555597e-11 DENN domain containing 5A FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB6A and RAB39A and/or RAB39B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. {ECO:0000269|PubMed:20937701}.; . . smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; whole brain;medulla oblongata;occipital lobe;hypothalamus;spinal cord;prefrontal cortex;caudate nucleus;parietal lobe;cerebellum; 0.30398 0.10749 -1.370504439 4.452701109 2936.75498 10.27925 DENND5B 0.999945504401691 5.44955979477285e-05 3.61518543775632e-13 DENN domain containing 5B FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB39A and/or RAB39B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. {ECO:0000269|PubMed:20937701}.; . . unclassifiable (Anatomical System);lymph node;islets of Langerhans;colon;blood;bone marrow;uterus;prostate;whole body;lung;frontal lobe;thyroid;liver;testis;head and neck;spleen;cervix;amniotic fluid;germinal center;brain; appendix;skeletal muscle; . . -0.440847477 24.59896202 5379.04327 15.12450 DENND5B-AS1 . . . DENND5B antisense RNA 1 . . . . . . . . . . . DENND6A 0.852272523176061 0.147727301200785 1.75623153661848e-07 DENN domain containing 6A FUNCTION: Guanine nucleotide exchange factor (GEF) for RAB14. Component of an endocytic recycling pathway that is required for the control of ADAM10 transport, shedding of N-cadherin/CDH2 by ADAM9 or ADAM10 and regulation of cell-cell junctions. Required for RAB14 recruitment to recycling endosomes. {ECO:0000269|PubMed:22595670}.; . . . . 0.26434 . -0.0274281 51.65723048 40.37373 1.18488 DENND6A-AS1 . . . DENND6A antisense RNA 1 . . . . . . . . . . . DENND6B 0.0310203476755261 0.966992704340567 0.00198694798390729 DENN domain containing 6B FUNCTION: Guanine nucleotide exchange factor (GEF) for RAB14. Also has some, lesser GEF activity towards RAB35. {ECO:0000269|PubMed:22595670}.; . . . . 0.18579 . -0.951568548 9.271054494 2114.67479 8.46343 DENR 0.846252782580504 0.151019674809551 0.00272754260994491 density-regulated protein FUNCTION: May be involved in the translation of target mRNAs by scanning and recognition of the initiation codon. Involved in translation initiation; promotes recruitmnet of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. Plays a role in the modulation of the translational profile of a subset of cancer-related mRNAs when recruited to the translational initiation complex by the oncogene MCTS1. {ECO:0000269|PubMed:16982740, ECO:0000269|PubMed:17878526, ECO:0000269|PubMed:20713520}.; . TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle and moderately expressed in the brain, placenta, liver and pancreas. Weakly expressed in the lung and kidney. {ECO:0000269|PubMed:9628587}.; unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;developmental;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;frontal lobe;endometrium;bone;placenta;macula lutea;visual apparatus;liver;testis;spleen;germinal center;stomach; superior cervical ganglion;prefrontal cortex;white blood cells; 0.09903 0.09101 0.235309407 68.71903751 4.88397 0.18092 DEPDC1 3.29623878527281e-07 0.98369171974125 0.0163079506348717 DEP domain containing 1 FUNCTION: May be involved in transcriptional regulation as a transcriptional corepressor. The DEPDC1A-ZNF224 complex may play a critical role in bladder carcinogenesis by repressing the transcription of the A20 gene, leading to transport of NF-KB protein into the nucleus, resulting in suppression of apoptosis of bladder cancer cells. {ECO:0000269|PubMed:20587513}.; . TISSUE SPECIFICITY: Expressed in testis. Up-regulated in bladder cancer cells (at protein level). {ECO:0000269|PubMed:17452976}.; . . 0.08697 0.08467 -0.134019284 43.90776126 413.61173 4.25924 DEPDC1-AS1 . . . DEPDC1 antisense RNA 1 . . . . . . . . . . . DEPDC1B 2.28513658245294e-05 0.978157022960747 0.0218201256734286 DEP domain containing 1B . . . unclassifiable (Anatomical System);lymph node;ovary;colon;parathyroid;skin;skeletal muscle;bone marrow;uterus;pancreas;prostate;whole body;lung;placenta;visual apparatus;testis;germinal center;kidney;brain;stomach; . 0.78536 0.12709 -0.602450568 17.91106393 45.94992 1.30436 DEPDC1P1 . . . DEP domain containing 1 pseudogene 1 . . . . . . . . . . . DEPDC1P2 . . . DEP domain containing 1 pseudogene 2 . . . . . . . . . . . DEPDC4 4.10418498875559e-09 0.0287887484482775 0.971211247447538 DEP domain containing 4 . . . unclassifiable (Anatomical System);uterus;lung;testis;blood;kidney;bone marrow; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09749 . -0.181750739 40.15687662 343.84113 3.93093 DEPDC5 0.99999993402596 6.59740399847371e-08 9.62207546324156e-24 DEP domain containing 5 FUNCTION: As a component of the GATOR1 complex, inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC- containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. {ECO:0000269|PubMed:23723238}.; DISEASE: Note=Inactivating mutations and truncating deletions in the genes encoding GATOR1 proteins, including DEPDC5, are detected in glioblastoma and ovarian tumors and are associated with loss of heterozygosity events. Inactivation of GATOR1 proteins promotes constitutive localization of mTORC1 to the lysosomal membrane and blocks mTORC1 inactivation following amino acid withdrawal (PubMed:23723238). {ECO:0000269|PubMed:23723238}.; TISSUE SPECIFICITY: Expressed in developing and adult brain. {ECO:0000269|PubMed:23542701}.; unclassifiable (Anatomical System);lymph node;ovary;muscle;colon;blood;skeletal muscle;bone marrow;breast;uterus;pancreas;lung;frontal lobe;nasopharynx;bone;liver;head and neck;germinal center;spinal ganglion;thymus; subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.19403 0.09278 -1.115293937 6.623024298 895.81677 5.83244 DEPDC7 1.25056837709977e-05 0.951509448221312 0.0484780460949167 DEP domain containing 7 . . TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:10568747}.; unclassifiable (Anatomical System);medulla oblongata;islets of Langerhans;skin;retina;bone marrow;pancreas;lung;liver;testis;spleen;germinal center;kidney;brain; testis - interstitial;testis - seminiferous tubule;testis; 0.07468 . -0.069700724 48.54328851 431.22089 4.33209 DEPTOR 0.000777355950659311 0.927038665893268 0.0721839781560722 DEP domain containing MTOR-interacting protein FUNCTION: Negative regulator of the mTORC1 and mTORC2 signaling pathways. Inhibits the kinase activity of both complexes. {ECO:0000269|PubMed:19446321}.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;thyroid;bone;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;liver;cervix;kidney;mammary gland;stomach;aorta; occipital lobe;superior cervical ganglion;adrenal gland;thyroid;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.23138 . 0.066214104 58.95848077 2720.36668 9.82547 DERA 0.0340764800521968 0.927604166795199 0.0383193531526039 deoxyribose-phosphate aldolase FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy- D-ribose 5-phosphate. Participates in stress granule (SG) assembly. May allow ATP production from extracellular deoxyinosine in conditions of energy deprivation. {ECO:0000269|PubMed:25229427}.; . TISSUE SPECIFICITY: Mainly expressed in liver, lung and colon. {ECO:0000269|PubMed:25229427}.; . . 0.13571 0.18036 -0.426079032 25.36565228 60.26579 1.57754 DERL1 0.0115886691978839 0.979972717313267 0.00843861348884956 derlin 1 FUNCTION: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the degradation substrate. In case of infection by cytomegaloviruses, it plays a central role in the export from the ER and subsequent degradation of MHC class I heavy chains via its interaction with US11 viral protein, which recognizes and associates with MHC class I heavy chains. Also participates in the degradation process of misfolded cytomegalovirus US2 protein. {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:15215856}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:16449189}.; myocardium;lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;cerebral cortex;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; testis - interstitial;liver;testis;atrioventricular node;trigeminal ganglion; 0.22250 0.18208 -0.05129383 49.75819769 355.10674 3.98507 DERL2 0.932959932073288 0.0669738649959455 6.62029307663077e-05 derlin 2 FUNCTION: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the degradation substrate. In contrast to DERL1, it is not involved in the degradation of MHC class I heavy chains following infection by cytomegaloviruses. May play a role in cell proliferation. {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:16186509, ECO:0000269|PubMed:16449189}.; . TISSUE SPECIFICITY: Ubiquitous. Overexpressed in various hepatocarcinomas. {ECO:0000269|PubMed:11500051, ECO:0000269|PubMed:16449189}.; ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;iris;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;epididymis;nasopharynx;placenta;macula lutea;liver;spleen;kidney; testis - interstitial;testis - seminiferous tubule;placenta;testis;white blood cells; 0.60196 0.13588 -0.141298762 42.87567823 650.6157 5.11656 DERL3 0.000238218108055327 0.520950390453634 0.47881139143831 derlin 3 FUNCTION: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the degradation substrate. {ECO:0000269|PubMed:16449189, ECO:0000269|PubMed:22607976}.; . TISSUE SPECIFICITY: Unlike DERL1 and DERL2, restricted to several tissues. Expressed at high levels in placenta, pancreas, spleen and small intestine. {ECO:0000269|PubMed:16449189}.; unclassifiable (Anatomical System);islets of Langerhans;colon;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;bone;macula lutea;liver;testis;spleen;kidney;germinal center;mammary gland;stomach; . 0.23259 0.12763 0.595326758 82.66100495 1232.36532 6.63447 DES 0.00308243386387878 0.985331559419 0.0115860067171213 desmin FUNCTION: Desmin are class-III intermediate filaments found in muscle cells. In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures. {ECO:0000269|PubMed:25394388}.; DISEASE: Myopathy, myofibrillar, 1 (MFM1) [MIM:601419]: A neuromuscular disorder characterized by skeletal muscle weakness associated with cardiac conduction blocks, arrhythmias, restrictive heart failure, and by myofibrillar destruction with intracytoplasmic accumulation of desmin-reactive deposits in cardiac and skeletal muscle cells. {ECO:0000269|PubMed:10545598, ECO:0000269|PubMed:10717012, ECO:0000269|PubMed:10905661, ECO:0000269|PubMed:11061256, ECO:0000269|PubMed:11668632, ECO:0000269|PubMed:12620971, ECO:0000269|PubMed:12766977, ECO:0000269|PubMed:14648196, ECO:0000269|PubMed:14711882, ECO:0000269|PubMed:15800015, ECO:0000269|PubMed:16009553, ECO:0000269|PubMed:16865695, ECO:0000269|PubMed:17221859, ECO:0000269|PubMed:18061454, ECO:0000269|PubMed:19879535, ECO:0000269|PubMed:20829228, ECO:0000269|PubMed:22106715, ECO:0000269|PubMed:22395865, ECO:0000269|PubMed:25394388, ECO:0000269|PubMed:9697706, ECO:0000269|PubMed:9736733}. Note=The disease is caused by mutations affecting the gene represented in this entry. Mutations in the DES gene are associated with a variable clinical phenotype which encompasses isolated myopathies, pure cardiac phenotypes (including dilated cardiomyopathy, restrictive cardiomyopathy and arrhythmogenic right ventricular cardiomyopathy), cardiac conduction disease, and combinations of these disorders. If both cardiologic and neurologic features occur, they can manifest in any order, as cardiologic features can precede, occur simultaneously with, or follow manifestation of generalized neuromuscular disease (PubMed:19879535). {ECO:0000269|PubMed:19879535}.; DISEASE: Cardiomyopathy, dilated 1I (CMD1I) [MIM:604765]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:10430757}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Neurogenic scapuloperoneal syndrome Kaeser type (Kaeser syndrome) [MIM:181400]: Autosomal dominant disorder with a peculiar scapuloperoneal distribution of weakness and atrophy. A large clinical variability is observed ranging from scapuloperoneal, limb grindle and distal phenotypes with variable cardiac or respiratory involvement. Facial weakness, dysphagia and gynaecomastia are frequent additional symptoms. Affected men seemingly bear a higher risk of sudden, cardiac death as compared to affected women. Histological and immunohistochemical examination of muscle biopsy specimens reveal a wide spectrum of findings ranging from near normal or unspecific pathology to typical, myofibrillar changes with accumulation of desmin. {ECO:0000269|PubMed:17439987, ECO:0000269|PubMed:25394388}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Limb-girdle muscular dystrophy 2R (LGMD2R) [MIM:615325]: A form of limb-girdle muscular dystrophy, a disease characterized by proximal weakness, weakness of the hip and shoulder girdles and prominent asymmetrical quadriceps femoris and biceps brachii atrophy. {ECO:0000269|PubMed:23687351}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.78691 0.12202 -0.512444034 21.55579146 152.44729 2.69928 DESI1 0.0937224778463612 0.868534703584057 0.0377428185695822 desumoylating isopeptidase 1 FUNCTION: Protease which deconjugates SUMO1, SUMO2 and SUMO3 from some substrate proteins. Has isopeptidase but not SUMO-processing activity. Desumoylates ZBTB46 (By similarity). {ECO:0000250}.; . . . . 0.64236 . -0.119252484 44.53880632 4.99568 0.18555 DESI2 0.915084441052073 0.0843259441027454 0.000589614845181482 desumoylating isopeptidase 2 FUNCTION: Protease which may deconjugate SUMO from some substrate proteins. {ECO:0000250}.; . . . . 0.11628 0.07259 0.21326276 67.71644256 11.70962 0.42542 DET1 0.542030761589873 0.457332499419874 0.000636738990252651 de-etiolated homolog 1 (Arabidopsis) FUNCTION: Component of the E3 ubiquitin ligase DCX DET1-COP1 complex, which is required for ubiquitination and subsequent degradation of target proteins. The complex is involved in JUN ubiquitination and degradation. {ECO:0000269|PubMed:14739464}.; . TISSUE SPECIFICITY: Highly expressed in the ovary, some lymphoid organs and resting leukocytes. {ECO:0000269|PubMed:14739464}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;parathyroid;retina;uterus;pancreas;prostate;lung;larynx;thyroid;placenta;head and neck;spleen;germinal center;kidney;brain;pineal gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons; 0.21616 0.16040 -0.955204708 9.170794999 62.50488 1.61506 DEXI 0.45368757225915 0.450603984665308 0.0957084430755417 Dexi homolog (mouse) . . TISSUE SPECIFICITY: Highest levels in heart. Also expressed in brain, liver, pancreas, placenta and lung. Up-regulated in emphysematous lung compared to normal lung. {ECO:0000269|PubMed:11472984}.; myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;breast;bile duct;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; whole brain;thalamus;adrenal gland;liver;prefrontal cortex;cingulate cortex; . . 0.079165051 59.43029016 3.59417 0.13074 DFFA 0.00021837065189826 0.740902211652935 0.258879417695167 DNA fragmentation factor subunit alpha FUNCTION: Inhibitor of the caspase-activated DNase (DFF40).; . . . . 0.25697 0.12724 0.507139401 80.10143902 180.29756 2.91715 DFFB 5.08618071063922e-05 0.668989030858828 0.330960107334066 DNA fragmentation factor subunit beta FUNCTION: Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology.; . . unclassifiable (Anatomical System);lung;spleen;skeletal muscle; dorsal root ganglion;superior cervical ganglion;globus pallidus;white blood cells;cingulate cortex; 0.13818 0.14884 -0.071520315 48.34866714 515.42292 4.64343 DFFBP1 . . . DNA fragmentation factor subunit beta pseudogene 1 . . . . . . . . . . . DFN5 . . . deafness, X-linked 5 . . . . . . . . . . . DFN8 . . . deafness, X-linked 8 . . . . . . . . . . . DFNA5 1.21683174137448e-05 0.824314523407211 0.175673308275375 deafness, autosomal dominant 5 FUNCTION: Involved in apoptosis and cell survival. Plays a role in the TP53-regulated cellular response to DNA damage probably by cooperating with TP53. {ECO:0000269|PubMed:16897187, ECO:0000269|PubMed:18223688, ECO:0000269|PubMed:21522185}.; DISEASE: Note=Is a tumor suppressor gene with an important role in colorectal cancer (CRC). {ECO:0000303|PubMed:18223688}.; TISSUE SPECIFICITY: Expressed in cochlea. Low level of expression in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas, with highest expression in placenta.; ovary;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;muscle;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney; trigeminal ganglion; 0.10609 0.11513 -0.130380821 44.03161123 1208.59464 6.58361 DFNA7 . . . deafness, autosomal dominant 7 . . . . . . . . . . . DFNA16 . . . deafness, autosomal dominant 16 . . . . . . . . . . . DFNA18 . . . deafness, autosomal dominant 18 . . . . . . . . . . . DFNA19 . . . deafness, autosomal dominant 19 . . . . . . . . . . . DFNA21 . . . deafness, autosomal dominant 21 . . . . . . . . . . . DFNA24 . . . deafness, autosomal dominant 24 . . . . . . . . . . . DFNA27 . . . deafness, autosomal dominant 27 . . . . . . . . . . . DFNA29 . . . deafness, autosomal dominant 29 . . . . . . . . . . . DFNA30 . . . deafness, autosomal dominant 30 . . . . . . . . . . . DFNA31 . . . deafness, autosomal dominant 31 . . . . . . . . . . . DFNA32 . . . deafness, autosomal dominant 32 . . . . . . . . . . . DFNA33 . . . deafness, autosomal dominant 33 . . . . . . . . . . . DFNA34 . . . deafness, autosomal dominant 34 . . . . . . . . . . . DFNA35 . . . deafness, autosomal dominant 35 . . . . . . . . . . . DFNA37 . . . deafness, autosomal dominant 37 . . . . . . . . . . . DFNA40 . . . deafness, autosomal dominant 40 . . . . . . . . . . . DFNA42 . . . deafness, autosomal dominant 42 . . . . . . . . . . . DFNA43 . . . deafness, autosomal dominant 43 . . . . . . . . . . . DFNA45 . . . deafness, autosomal dominant 45 . . . . . . . . . . . DFNA46 . . . deafness, autosomal dominant 46 . . . . . . . . . . . DFNA47 . . . deafness, autosomal dominant 47 . . . . . . . . . . . DFNA48 . . . deafness, autosomal dominant 48 . . . . . . . . . . . DFNA49 . . . deafness, autosomal dominant 49 . . . . . . . . . . . DFNA52 . . . deafness, autosomal dominant 52 . . . . . . . . . . . DFNA53 . . . deafness, autosomal dominant 53 . . . . . . . . . . . DFNA54 . . . deafness, autosomal dominant 54 . . . . . . . . . . . DFNA55 . . . deafness, autosomal dominant 55 . . . . . . . . . . . DFNA57 . . . deafness, autosomal dominant 57 . . . . . . . . . . . DFNA58 . . . deafness, autosomal dominant 58 . . . . . . . . . . . DFNA59 . . . deafness, autosomal dominant 59 . . . . . . . . . . . DFNA60 . . . deafness, autosomal dominant 60 . . . . . . . . . . . DFNA61 . . . deafness, autosomal dominant 61 . . . . . . . . . . . DFNA62 . . . deafness, autosomal dominant 62 . . . . . . . . . . . DFNA63 . . . deafness, autosomal dominant 63 . . . . . . . . . . . DFNB5 . . . deafness, autosomal recessive 5 . . . . . . . . . . . DFNB13 . . . deafness, autosomal recessive 13 . . . . . . . . . . . DFNB14 . . . deafness, autosomal recessive 14 . . . . . . . . . . . DFNB17 . . . deafness, autosomal recessive 17 . . . . . . . . . . . DFNB19 . . . deafness, autosomal recessive 19 . . . . . . . . . . . DFNB20 . . . deafness, autosomal recessive 20 . . . . . . . . . . . DFNB26 . . . deafness, autosomal recessive 26 . . . . . . . . . . . DFNB27 . . . deafness, autosomal recessive 27 . . . . . . . . . . . DFNB31 0.0110884966572566 0.98706011557098 0.00185138777176348 deafness, autosomal recessive 31 FUNCTION: Necessary for elongation and maintenance of inner and outer hair cell stereocilia in the organ of Corti in the inner ear. {ECO:0000250}.; DISEASE: Deafness, autosomal recessive, 31 (DFNB31) [MIM:607084]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:11973626, ECO:0000269|PubMed:12833159, ECO:0000269|PubMed:15841483}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Usher syndrome 2D (USH2D) [MIM:611383]: USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa and sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). USH2 is characterized by congenital mild hearing impairment with normal vestibular responses. {ECO:0000269|PubMed:17171570}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;endometrium;synovium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);adrenal cortex;blood;lens;breast;lung;macula lutea;visual apparatus;cervix;spleen;kidney;mammary gland;stomach; medulla oblongata;testis - interstitial;superior cervical ganglion;thalamus;testis - seminiferous tubule;adrenal gland;spinal cord;prefrontal cortex;adrenal cortex;testis;caudate nucleus;cingulate cortex;parietal lobe; 0.30697 0.16487 0.637419773 83.64590705 3091.97485 10.56807 DFNB32 . . . deafness, autosomal recessive 32 . . . . . . . . . . . DFNB33 . . . deafness, autosomal recessive 33 . . . . . . . . . . . DFNB34 . . . deafness, autosomal recessive 34 . . . . . . . . . . . DFNB38 . . . deafness, autosomal recessive 38 . . . . . . . . . . . DFNB40 . . . deafness, autosomal recessive 40 . . . . . . . . . . . DFNB43 . . . deafness, autosomal recessive 43 . . . . . . . . . . . DFNB44 . . . deafness, autosomal recessive 44 . . . . . . . . . . . DFNB45 . . . deafness, autosomal recessive 45 . . . . . . . . . . . DFNB46 . . . deafness, autosomal recessive 46 . . . . . . . . . . . DFNB47 . . . deafness, autosomal recessive 47 . . . . . . . . . . . DFNB50 . . . deafness, autosomal recessive 50 . . . . . . . . . . . DFNB51 . . . deafness, autosomal recessive 51 . . . . . . . . . . . DFNB54 . . . deafness, autosomal recessive 54 . . . . . . . . . . . DFNB55 . . . deafness, autosomal recessive 55 . . . . . . . . . . . DFNB56 . . . deafness, autosomal recessive 56 . . . . . . . . . . . DFNB57 . . . deafness, autosomal recessive 57 . . . . . . . . . . . DFNB58 . . . deafness, autosomal recessive 58 . . . . . . . . . . . DFNB59 1.07044413650742e-05 0.80229595103298 0.197693344525655 deafness, autosomal recessive 59 FUNCTION: Essential in the activity of auditory pathway neurons.; . . . . 0.37738 . -0.137658575 43.57159707 383.66914 4.13032 DFNB60 . . . deafness, autosomal recessive 60 . . . . . . . . . . . DFNB62 . . . deafness, autosomal recessive 62 . . . . . . . . . . . DFNB65 . . . deafness, autosomal recessive 65 . . . . . . . . . . . DFNB66 . . . deafness, autosomal recessive 66 . . . . . . . . . . . DFNB68 . . . deafness, autosomal recessive 68 . . . . . . . . . . . DFNB69 . . . deafness, autosomal recessive 69 . . . . . . . . . . . DFNB71 . . . deafness, autosomal recessive 71 . . . . . . . . . . . DFNB75 . . . deafness, autosomal recessive 75 . . . . . . . . . . . DFNB78 . . . deafness, autosomal recessive 78 . . . . . . . . . . . DFNB80 . . . deafness, autosomal recessive 80 . . . . . . . . . . . DFNB81 . . . deafness, autosomal recessive 81 . . . . . . . . . . . DFNB83 . . . deafness, autosomal recessive 83 . . . . . . . . . . . DFNB85 . . . deafness, autosomal recessive 85 . . . . . . . . . . . DFNB87 . . . deafness, autosomal recessive 87 . . . . . . . . . . . DFNB90 . . . deafness, autosomal recessive 90 . . . . . . . . . . . DFNB92 . . . deafness, autosomal recessive 92 . . . . . . . . . . . DFNB93 . . . deafness, autosomal recessive 93 . . . . . . . . . . . DFNB96 . . . deafness, autosomal recessive 96 . . . . . . . . . . . DFNB100 . . . deafness, autosomal recessive 100 . . . . . . . . . . . DFNM1 . . . deafness (recessive, non-syndromic) modifier 1 . . . . . . . . . . . DFNM2 . . . deafness (mitochondrial) modifier 2 . . . . . . . . . . . DFNX3 . . . deafness, X-linked 3 . . . . . . . . . . . DFNY1 . . . deafness, Y-linked 1 . . . . . . . . . . . DGAT1 2.90054760621977e-10 0.274285643919623 0.725714355790323 diacylglycerol O-acyltransferase 1 FUNCTION: Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly. In liver, plays a role in esterifying exogenous fatty acids to glycerol. Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders. {ECO:0000269|PubMed:16214399, ECO:0000269|PubMed:9756920}.; DISEASE: Diarrhea 7 (DIAR7) [MIM:615863]: A life-threatening disease characterized by severe, intractable, watery diarrhea. {ECO:0000269|PubMed:23114594}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;endometrium;thyroid;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;heart;adrenal gland;liver;adrenal cortex;testis; 0.21291 0.34238 -0.841329384 11.36470866 296.55679 3.67459 DGAT2 7.51042690362332e-08 0.464501216249789 0.535498708645942 diacylglycerol O-acyltransferase 2 FUNCTION: Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides (By similarity). Functions also as an acyl-CoA retinol acyltransferase (ARAT). {ECO:0000250}.; . TISSUE SPECIFICITY: Predominantly expressed in liver and white adipose tissue. Expressed at lower level in mammary gland, testis and peripheral blood leukocytes. Expressed in sebaceous glands of normal skin but decreased psoriatic skin. {ECO:0000269|PubMed:11481335, ECO:0000269|PubMed:14521909}.; lymphoreticular;medulla oblongata;ovary;colon;choroid;skin;uterus;prostate;whole body;cerebral cortex;thyroid;bone;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;urinary;skeletal muscle;breast;pancreas;lung;liver;spleen;kidney;mammary gland;stomach; fetal liver;adipose tissue;ciliary ganglion; 0.13912 0.13760 0.350995466 74.37485256 327.81893 3.84936 DGAT2L6 3.36553042993953e-08 0.0966015196320519 0.903398446712644 diacylglycerol O-acyltransferase 2 like 6 FUNCTION: Probable acyltransferase uses fatty acyl-CoA as substrate (By similarity). Has no wax synthase activity to produce wax esters. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in all tissues tested except pancreas. {ECO:0000269|PubMed:15671038}.; skin; dorsal root ganglion;superior cervical ganglion;medulla oblongata;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;skin; 0.20527 0.10053 -0.648365105 16.35999056 38.52298 1.14250 DGAT2L7P . . . diacylglycerol O-acyltransferase 2 like 7, pseudogene FUNCTION: Probable acyltransferase uses fatty acyl-CoA as substrate. {ECO:0000250}.; . . . . . . . . . . DGCR . . . DiGeorge syndrome chromosome region . . . . . . . . . . . DGCR2 0.00109593805086936 0.951887960332042 0.0470161016170889 DiGeorge syndrome critical region gene 2 FUNCTION: Putative adhesion receptor, that could be involved in cell-cell or cell-matrix interactions required for normal cell differentiation and migration.; . TISSUE SPECIFICITY: Predominantly expressed in brain, heart, lung and fetal kidney. Low levels in liver and adult kidney.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus;cerebellum; amygdala;superior cervical ganglion;medulla oblongata;thalamus;fetal liver;thyroid;globus pallidus;pons;trigeminal ganglion;cerebellum; 0.26003 0.26731 -1.172055164 6.027364945 892.52157 5.82309 DGCR5 . . . DiGeorge syndrome critical region gene 5 (non-protein coding) . . . . . . . . . . . DGCR6 7.62101542352864e-07 0.158922351851112 0.841076886047346 DiGeorge syndrome critical region gene 6 FUNCTION: May play a role in neural crest cell migration into the third and fourth pharyngeal pouches.; . TISSUE SPECIFICITY: Found in all tissues examined with highest expression in liver, heart and skeletal muscle. Lower levels in pancreas and placenta. Weak expression in brain. {ECO:0000269|PubMed:11157784, ECO:0000269|PubMed:15821931}.; myocardium;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;iris;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;spinal cord;muscle;adrenal cortex;blood;lens;skeletal muscle;lung;epididymis;placenta;visual apparatus;hippocampus;liver;alveolus;spleen;cervix;kidney;mammary gland;aorta; . . 0.14019 0.507139401 80.10143902 193.8624 3.02053 DGCR6L 0.128574000583518 0.848762800899022 0.0226631985174598 DiGeorge syndrome critical region gene 6-like FUNCTION: May play a role in neural crest cell migration into the third and fourth pharyngeal pouches.; . TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues. Highest expression in liver, heart and skeletal muscle. Lower levels in pancreas and placenta. Weak expression in brain. {ECO:0000269|PubMed:11157784, ECO:0000269|PubMed:15821931}.; myocardium;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;bone;thyroid;iris;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;spinal cord;muscle;adrenal cortex;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; . 0.14603 0.10101 0.038710339 56.92380278 272.1353 3.53456 DGCR8 0.999895838044823 0.000104161912391768 4.27851784613724e-11 DGCR8 microprocessor complex subunit FUNCTION: Component of the microprocessor complex that acts as a RNA- and heme-binding protein that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DGCR8 function as a molecular anchor necessary for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs DROSHA to cleave 11 bp away form the junction to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. The heme-bound DGCR8 dimer binds pri-miRNAs as a cooperative trimer (of dimers) and is active in triggering pri- miRNA cleavage, whereas the heme-free DGCR8 monomer binds pri- miRNAs as a dimer and is much less active. Both double-stranded and single-stranded regions of a pri-miRNA are required for its binding (PubMed:15531877, PubMed:15574589, PubMed:15589161, PubMed:16751099, PubMed:16906129, PubMed:16963499, PubMed:17159994). Specifically recognizes and binds N6- methyladenosine (m6A)-containing pri-miRNAs, a modification required for pri-miRNAs processing (PubMed:25799998). Involved in the silencing of embryonic stem cells self-renewal (By similarity). {ECO:0000250|UniProtKB:Q9EQM6, ECO:0000269|PubMed:15531877, ECO:0000269|PubMed:15574589, ECO:0000269|PubMed:15589161, ECO:0000269|PubMed:16751099, ECO:0000269|PubMed:16906129, ECO:0000269|PubMed:16963499, ECO:0000269|PubMed:17159994, ECO:0000269|PubMed:25799998}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12705904}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;lens;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; cerebellum peduncles;testis;parietal lobe;cerebellum; 0.25806 0.13995 -0.997481928 8.47487615 255.13351 3.43548 DGCR9 . . . DiGeorge syndrome critical region gene 9 (non-protein coding) . . . . . . . . . . . DGCR10 . . . DiGeorge syndrome critical region gene 10 (non-protein coding) . . . . . . . . . . . DGCR11 . . . DiGeorge syndrome critical region gene 11 (non-protein coding) . . . . . . . . . . . DGCR12 . . . DiGeorge syndrome critical region gene 12 (non-protein coding) . . . . . . . . . . . DGCR14 9.97852446509117e-06 0.789634589474075 0.21035543200146 DiGeorge syndrome critical region gene 14 FUNCTION: May be involved in pre-mRNA splicing.; . TISSUE SPECIFICITY: Highly expressed in heart, brain and skeletal muscle. Detected at low levels in placenta. {ECO:0000269|PubMed:8776594}.; ovary;salivary gland;colon;skin;retina;uterus;frontal lobe;cerebral cortex;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.20466 0.21785 0.466683681 78.73908941 1245.23515 6.66527 DGKA 0.999250949298834 0.000749050692393915 8.77171680206767e-12 diacylglycerol kinase alpha FUNCTION: Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity.; . TISSUE SPECIFICITY: Lymphocytes and oligodendroglial cells.; lymphoreticular;ovary;colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.34464 0.14016 0.154398214 64.73814579 48.43832 1.35776 DGKB 0.669214093853988 0.33078554788184 3.58264171963669e-07 diacylglycerol kinase beta FUNCTION: Exhibits high phosphorylation activity for long-chain diacylglycerols. {ECO:0000250}.; . . unclassifiable (Anatomical System);frontal lobe;sympathetic chain;blood; medulla oblongata;pons;caudate nucleus; 0.17814 0.12712 -0.93133804 9.613116301 366.37055 4.04890 DGKD 0.97707055456914 0.0229294454180697 1.27906808173812e-11 diacylglycerol kinase delta FUNCTION: May function as signaling molecule. {ECO:0000269|PubMed:17880279}.; . TISSUE SPECIFICITY: Isoform 2 is ubiquitously expressed also in tumor tissues. Isoform 1 is expressed in ovary, spleen and some tumor-derived cells. {ECO:0000269|PubMed:12200442}.; salivary gland;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;duodenum;amnion;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; testis - interstitial;testis - seminiferous tubule;fetal brain;cerebellum peduncles;testis;white blood cells;skeletal muscle;cerebellum; 0.13096 0.13727 -2.34451481 1.155933003 88.47472 2.01631 DGKE 0.000684088440351919 0.995096355056644 0.00421955650300453 diacylglycerol kinase epsilon FUNCTION: Highly selective for arachidonate-containing species of diacylglycerol (DAG). May terminate signals transmitted through arachidonoyl-DAG or may contribute to the synthesis of phospholipids with defined fatty acid composition.; DISEASE: Hemolytic uremic syndrome atypical 7 (AHUS7) [MIM:615008]: An atypical form of hemolytic uremic syndrome characterized by acute onset in the first year of life of microangiopathic hemolytic anemia, thrombocytopenia, and renal failure. After the acute episode, most patients develop chronic renal insufficiency. Unlike other genetic forms of aHUS, AHUS7 is not related to abnormal activation of the complement system. {ECO:0000269|PubMed:23542698}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly in testis. Expressed in endothelium, platelets and podocytes (at protein level). {ECO:0000269|PubMed:23542698}.; unclassifiable (Anatomical System);breast;prostate;lung;ovary;cervix;germinal center;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.17572 0.22972 -0.378346116 28.01368247 112.24732 2.30438 DGKG 5.43821441070651e-06 0.99850147958706 0.00149308219852894 diacylglycerol kinase gamma FUNCTION: Reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid.; . TISSUE SPECIFICITY: Predominantly expressed in retina and in a much lesser extent in the brain. Other tissues contain extremely low levels of DGK-gamma.; unclassifiable (Anatomical System);lung;frontal lobe;ovary;placenta;parathyroid;blood;germinal center;brain;skeletal muscle;retina;bone marrow; superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;pons;trigeminal ganglion;cerebellum; 0.45176 0.18992 -1.524862616 3.42061807 110.98235 2.29646 DGKH 0.818123800274802 0.181876199620357 1.04840726996419e-10 diacylglycerol kinase eta FUNCTION: Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA). Plays a key role in promoting cell growth. Activates the Ras/B-Raf/C-Raf/MEK/ERK signaling pathway induced by EGF. Regulates the recruitment of RAF1 and BRAF from cytoplasm to membranes and their heterodimerization. {ECO:0000269|PubMed:12810723, ECO:0000269|PubMed:19710016}.; . TISSUE SPECIFICITY: Isoform 2 is ubiquitously expressed. Isoform 1 is expressed only in testis, kidney and colon. {ECO:0000269|PubMed:12810723}.; unclassifiable (Anatomical System);heart;ovary;blood;skin;uterus;breast;prostate;lung;hypopharynx;head and neck;brain;pineal gland; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.20308 0.13239 -1.304353358 4.91861288 1799.65958 7.82525 DGKI 0.738016171796638 0.261983826741952 1.46140997557688e-09 diacylglycerol kinase iota . . . unclassifiable (Anatomical System);lung;heart;placenta;testis;brain;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons; 0.09948 0.12778 -1.041578376 7.773059684 340.01459 3.91285 DGKK . . . diacylglycerol kinase kappa FUNCTION: Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA). {ECO:0000269|PubMed:16210324}.; . TISSUE SPECIFICITY: Expressed in testis, and to a lesser extent in placenta. {ECO:0000269|PubMed:16210324}.; . . 0.24434 0.09038 . . . . DGKQ 0.0011940236557909 0.998419113863445 0.000386862480763892 diacylglycerol kinase theta FUNCTION: Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA). May regulate the activity of protein kinase C by controlling the balance between these two signaling lipids. Activated in the nucleus in response to alpha-thrombin and nerve growth factor (By similarity). May be involved in cAMP- induced activation of NR5A1 and subsequent steroidogenic gene transcription by delivering PA as ligand for NR5A1. Acts synergistically with NR5A1 on CYP17 transcriptional activity. {ECO:0000250, ECO:0000269|PubMed:17664281}.; . . ovary;colon;parathyroid;skin;bone marrow;uterus;frontal lobe;endometrium;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;muscle;blood;pancreas;lung;epididymis;placenta;liver;alveolus;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;testis - interstitial;trigeminal ganglion;parietal lobe;skeletal muscle; 0.08498 0.13903 -2.675433159 0.73720217 787.21391 5.54052 DGKZ 0.998142633966722 0.00185736603261309 6.64826109634418e-13 diacylglycerol kinase zeta FUNCTION: Displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. Isoform 2 but not isoform 1 regulates RASGRP1 activity. {ECO:0000269|PubMed:11257115}.; . TISSUE SPECIFICITY: Highest levels in brain, and substantial levels in skeletal muscle, heart, and pancreas. Isoform 1 is predominantly expressed in muscle.; unclassifiable (Anatomical System);lymph node;ovary;heart;colon;blood;choroid;skin;bone marrow;uterus;lung;endometrium;bone;placenta;visual apparatus;hippocampus;testis;cervix;spleen;germinal center;kidney;brain;mammary gland;bladder;stomach;thymus; . 0.12998 0.23787 0.270087468 70.69473933 3430.85138 11.24598 DGKZP1 . . . diacylglycerol kinase zeta pseudogene 1 . . . . . . . . . . . DGUOK 0.368434604695276 0.629154813457802 0.00241058184692144 deoxyguanosine kinase FUNCTION: Required for the phosphorylation of several deoxyribonucleosides and certain nucleoside analogs widely employed as antiviral and chemotherapeutic agents. {ECO:0000269|PubMed:8706825}.; . TISSUE SPECIFICITY: Ubiquitous. Highest expression in muscle, brain, liver and lymphoid tissues. {ECO:0000269|PubMed:8706825}.; lymphoreticular;smooth muscle;ovary;skin;bone marrow;prostate;endometrium;thyroid;germinal center;brain;bladder;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;kidney;aorta;stomach;thymus; whole brain;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;parietal lobe; 0.06877 0.17777 -0.247889024 35.98726115 90.67924 2.04929 DGUOK-AS1 . . . DGUOK antisense RNA 1 . . . . . . . . . . . DHCR7 5.04266438763907e-08 0.222172274910119 0.777827674663237 7-dehydrocholesterol reductase FUNCTION: Production of cholesterol by reduction of C7-C8 double bond of 7-dehydrocholesterol (7-DHC).; . TISSUE SPECIFICITY: Most abundant in adrenal gland, liver, testis, and brain. {ECO:0000269|PubMed:9878250}.; ovary;sympathetic chain;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;pineal body;adrenal cortex;blood;lens;breast;pancreas;lung;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;fetal liver;adrenal gland;adrenal cortex;liver; 0.10133 0.32155 -0.861560326 10.89289927 117.70382 2.35908 DHCR24 0.969136893394347 0.0308611852543166 1.92135133651564e-06 24-dehydrocholesterol reductase FUNCTION: Catalyzes the reduction of the delta-24 double bond of sterol intermediates. Protects cells from oxidative stress by reducing caspase 3 activity during apoptosis induced by oxidative stress. Also protects against amyloid-beta peptide-induced apoptosis. {ECO:0000269|PubMed:11007892, ECO:0000269|PubMed:11519011, ECO:0000269|PubMed:22010141}.; . TISSUE SPECIFICITY: Highly expressed in brain and adrenal gland with moderate expression in liver, lung, spleen, prostate and spinal cord. Low expression in heart, uterus and prostate. Undetectable in blood cells. In the brain, strongly expressed in cortical regions, substantia nigra, caudate nucleus, hippocampus, medulla oblongata and pons. In brains affected by Alzheimer disease, expression in the inferior temporal lobe is substantially lower than in the frontal cortex. {ECO:0000269|PubMed:11007892, ECO:0000269|PubMed:11519011}.; . . 0.19237 0.23658 -0.822919685 11.76574664 93.19943 2.07714 DHDDS 0.704700922518414 0.295148752429204 0.000150325052382678 dehydrodolichyl diphosphate synthase subunit FUNCTION: With DHDDS, forms the dehydrodolichyl diphosphate syntase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precusrosor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol. {ECO:0000269|PubMed:25066056, ECO:0000303|PubMed:21572394}.; . TISSUE SPECIFICITY: Expressed at high levels in testis and kidney. Expressed in epididymis (at protein level). Slightly expressed in heart, spleen and thymus. {ECO:0000269|PubMed:20736409}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;thyroid;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;urinary;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;epididymis;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach; cerebellum peduncles;trigeminal ganglion;skeletal muscle; 0.13611 0.82506 -0.093566408 46.7386176 3214.14466 10.80738 DHDH 3.48849486684174e-06 0.350383738044402 0.649612773460731 dihydrodiol dehydrogenase . . TISSUE SPECIFICITY: Small intestine. {ECO:0000269|PubMed:10477285}.; unclassifiable (Anatomical System);uterus;lung;bone;testis;kidney; . 0.26966 0.19437 1.756425229 96.70912951 6394.82578 16.70148 DHFR 0.276594317743087 0.700080993107319 0.0233246891495935 dihydrofolate reductase FUNCTION: Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFRL1. {ECO:0000269|PubMed:12096917, ECO:0000269|PubMed:21876188}.; . TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues, including throughout the fetal and adult brains and whole blood. Expression is higher in the adult brain than in the fetal brain. {ECO:0000269|PubMed:21310276}.; . . 0.59131 0.66216 0.147123112 64.11299835 10.61889 0.38617 DHFRL1 0.102597562557193 0.773775380837356 0.123627056605451 dihydrofolate reductase like 1 FUNCTION: Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Required to prevent uracil accumulation in mtDNA. Binds its own mRNA and that of DHFR. {ECO:0000269|PubMed:21876184, ECO:0000269|PubMed:21876188}.; . TISSUE SPECIFICITY: Expressed in numerous cell lines. {ECO:0000269|PubMed:21876184}.; unclassifiable (Anatomical System);heart;colon;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;optic nerve;lung;frontal lobe;bone;macula lutea;hippocampus;testis;germinal center;kidney;brain; . 0.44546 . 0.193034296 66.82000472 1099.19969 6.34556 DHFRP1 . . . dihydrofolate reductase pseudogene 1 . . . . . 0.59131 . . . . . DHFRP2 . . . dihydrofolate reductase pseudogene 2 . . . . . . . . . . . DHH 0.259714235022627 0.713541604560793 0.02674416041658 desert hedgehog FUNCTION: Intercellular signal essential for a variety of patterning events during development. May function as a spermatocyte survival factor in the testes. Essential for testes development.; DISEASE: Partial gonadal dysgenesis with minifascicular neuropathy 46,XY (PGD) [MIM:607080]: Characterized by the presence of a testis on one side and a streak or an absent gonad at the other, persistence of Muellerian duct structures, and a variable degree of genital ambiguity. {ECO:0000269|PubMed:11017805}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: 46,XY sex reversal 7 (SRXY7) [MIM:233420]: A disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females. SRXY7 patients have no functional gonads. {ECO:0000269|PubMed:15356051}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);medulla oblongata;pancreas;testis;spinal ganglion; ciliary ganglion;atrioventricular node; 0.61011 0.39166 . . 27.8283 0.89354 DHODH 0.0128239089226836 0.953447806064904 0.0337282850124122 dihydroorotate dehydrogenase (quinone) FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.; DISEASE: Postaxial acrofacial dysostosis (POADS) [MIM:263750]: POADS is characterized by severe micrognathia, cleft lip and/or palate, hypoplasia or aplasia of the posterior elements of the limbs, coloboma of the eyelids and supernumerary nipples. POADS is a very rare disorder: only 2 multiplex families, each consisting of 2 affected siblings born to unaffected, nonconsanguineous parents, have been described among a total of around 30 reported cases. {ECO:0000269|PubMed:19915526}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;islets of Langerhans;bone marrow;prostate;optic nerve;lung;endometrium;larynx;placenta;visual apparatus;liver;testis;head and neck;spleen;cervix;spinal ganglion;brain;stomach;gall bladder; superior cervical ganglion;liver;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.28914 0.43947 0.042348793 57.31304553 571.39979 4.84941 DHPS 0.0034521520485461 0.951817908818991 0.0447299391324631 deoxyhypusine synthase FUNCTION: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.; . . medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;kidney;stomach;cerebellum; whole brain;subthalamic nucleus;heart;cerebellum peduncles;liver;prefrontal cortex;tumor;white blood cells;skeletal muscle;parietal lobe;cerebellum; 0.26731 0.16415 -0.534490515 20.70063694 317.48292 3.78306 DHRS1 2.40813512310606e-10 0.0385565488416832 0.961443450917503 dehydrogenase/reductase (SDR family) member 1 . . TISSUE SPECIFICITY: Detected in heart and liver, and at low levels in skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:12153138}.; lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;thyroid;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;breast;pancreas;pia mater;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;tongue;liver;trigeminal ganglion; 0.26842 0.09683 -0.492218069 22.35786742 729.91529 5.36441 DHRS2 4.75351023968218e-06 0.405466890899858 0.594528355589902 dehydrogenase/reductase (SDR family) member 2 FUNCTION: Displays NADPH-dependent dicarbonyl reductase activity in vitro with 3,4-Hexanedione, 2,3-Heptanedione and 1-Phenyl-1,2- propanedione as substrates. No reductase activity is displayed in vitro with steroids, retinoids and sugars as substrates. Attenuates MDM2-mediated p53/TP53 degradation, leading to p53/TP53 stabilization and increased transcription activity, resulting in the accumulation of MDM2 and CDKN1A/p21. {ECO:0000269|PubMed:16685466, ECO:0000269|PubMed:20547751}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in liver and kidney, followed by heart, spleen, skeletal muscle and placenta. In hemopoietic cells, expressed in dendritic cells, but not in monocytes, macrophages, granulocytes, nor in B and T lymphocytes. {ECO:0000269|PubMed:11944995}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;endometrium;bone;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;urinary;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;kidney;mammary gland; testis - interstitial;superior cervical ganglion;placenta;globus pallidus;atrioventricular node;skeletal muscle; 0.30040 . 0.712836712 85.76315169 144.88041 2.62184 DHRS3 0.661359704005279 0.333234968665235 0.00540532732948569 dehydrogenase/reductase (SDR family) member 3 FUNCTION: Catalyzes the reduction of all-trans-retinal to all- trans-retinol in the presence of NADPH. {ECO:0000269|PubMed:9705317}.; . TISSUE SPECIFICITY: Widely expressed with highest levels found in heart, placenta, lung, liver, kidney, pancreas, thyroid, testis, stomach, trachea and spinal cord. Lower levels found in skeletal muscle, intestine and lymph node. No expression detected in brain. In the retina, expressed in cone but not rod outer segments. {ECO:0000269|PubMed:11861404, ECO:0000269|PubMed:9705317}.; . . 0.23544 0.16906 -0.337894035 30.37272942 209.35526 3.12368 DHRS4 0.121200513498066 0.853774364397515 0.0250251221044182 dehydrogenase/reductase (SDR family) member 4 FUNCTION: Reduces all-trans-retinal and 9-cis retinal. Can also catalyze the oxidation of all-trans-retinol with NADP as co- factor, but with much lower efficiency. Reduces alkyl phenyl ketones and alpha-dicarbonyl compounds with aromatic rings, such as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine, menadione and 4-hexanoylpyridine. Has no activity towards aliphatic aldehydes and ketones (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in normal cervix (at protein level). Isoform 4 is expressed in some neoplastic cervical tissues, but not in normal cervix (at protein level). Isoform 5 and isoform 6 are expressed in a few neoplastic cervical tissues.; lymphoreticular;ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;bile duct;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; ciliary ganglion;kidney;trigeminal ganglion; . 0.13249 0.485092724 79.37603208 978.06562 6.04152 DHRS4-AS1 . . . DHRS4 antisense RNA 1 . . . . . 0.08602 . . . 202.38423 3.06932 DHRS4L1 . . . dehydrogenase/reductase (SDR family) member 4 like 1 FUNCTION: Putative oxidoreductase. {ECO:0000250}.; . . . . . . . . . . DHRS4L2 0.357376761988657 0.630130112960092 0.0124931250512512 dehydrogenase/reductase (SDR family) member 4 like 2 FUNCTION: Probable oxidoreductase. {ECO:0000250}.; . . lymphoreticular;ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;lens;bile duct;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; ciliary ganglion;kidney;trigeminal ganglion; 0.03505 0.09070 2.465816951 98.61405992 3973.73722 12.46785 DHRS7 1.22281963443987e-05 0.600876033371822 0.399111738431833 dehydrogenase/reductase (SDR family) member 7 . . . lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; fetal liver;prostate;thyroid;whole blood;skeletal muscle; 0.12314 0.09317 0.240763792 69.36777542 . . DHRS7B 4.75875090057093e-08 0.117359365895303 0.882640586517188 dehydrogenase/reductase (SDR family) member 7B FUNCTION: Putative oxidoreductase. {ECO:0000305}.; . . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;liver;duodenum;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; testis - interstitial;testis - seminiferous tubule;testis; 0.18780 0.08946 -0.049474214 50.01179523 36.48054 1.09338 DHRS7C 1.11557777202949e-06 0.195360449080527 0.804638435341701 dehydrogenase/reductase (SDR family) member 7C FUNCTION: Putative oxidoreductase. {ECO:0000305}.; . . . . 0.12540 0.11202 0.196671391 67.19155461 854.22881 5.70669 DHRS9 2.60804336160151e-07 0.0873445535743717 0.912655185621292 dehydrogenase/reductase (SDR family) member 9 FUNCTION: 3-alpha-hydroxysteroid dehydrogenase that converts 3- alpha-tetrahydroprogesterone (allopregnanolone) to dihydroxyprogesterone and 3-alpha-androstanediol to dihydroxyprogesterone. May play a role in the biosynthesis of retinoic acid from retinaldehyde, but seems to have low activity with retinoids. Can utilize both NADH and NADPH. {ECO:0000269|PubMed:11294878, ECO:0000269|PubMed:11304534, ECO:0000269|PubMed:12618084}.; . TISSUE SPECIFICITY: Highly expressed in trachea and epidermis. Detected at lower levels in spinal cord, bone marrow, brain, tongue, esophagus, heart, colon, testis, placenta, lung, skeletal muscle and lymph node. {ECO:0000269|PubMed:11294878, ECO:0000269|PubMed:11304534, ECO:0000269|PubMed:12618084}.; unclassifiable (Anatomical System);lymphoreticular;medulla oblongata;cartilage;islets of Langerhans;colon;blood;skin;uterus;pancreas;lung;endometrium;adrenal gland;nasopharynx;bone;testis;cervix;kidney;germinal center;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.16471 0.13847 0.663285274 84.55414013 257.34805 3.45020 DHRS11 0.0315613338859281 0.925855824799966 0.042582841314106 dehydrogenase/reductase (SDR family) member 11 . . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion; . 0.11372 -0.183570861 39.95046001 2776.61224 9.95098 DHRS12 0.00725776436102893 0.922301763613723 0.0704404720252483 dehydrogenase/reductase (SDR family) member 12 FUNCTION: Putative oxidoreductase. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;pancreas;lung;epididymis;placenta;macula lutea;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;trigeminal ganglion;skeletal muscle; 0.04597 . 0.619191319 83.36282142 168.91394 2.83619 DHRS13 0.000234050386511642 0.517209932675996 0.482556016937492 dehydrogenase/reductase (SDR family) member 13 FUNCTION: Putative oxidoreductase. {ECO:0000305}.; . . . . 0.19627 0.09325 -0.26993514 34.59542345 75.56081 1.81915 DHRSX 0.00645955012200972 0.912427630712452 0.0811128191655384 dehydrogenase/reductase (SDR family) X-linked . . TISSUE SPECIFICITY: Widely expressed.; pancreas;placenta; . 0.18443 . 0.464864541 78.69190847 2632.59577 9.62334 DHRSX-IT1 . . . DHRSX intronic transcript 1 . . . . . . . . . . . DHTKD1 1.97824193673953e-16 0.0947350788807705 0.905264921119229 dehydrogenase E1 and transketolase domain containing 1 FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.; DISEASE: Charcot-Marie-Tooth disease 2Q (CMT2Q) [MIM:615025]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. {ECO:0000269|PubMed:23141294}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: 2-aminoadipic 2-oxoadipic aciduria (AMOXAD) [MIM:204750]: A metabolic disorder characterized by increased levels of 2- oxoadipate and 2-hydroxyadipate in the urine, and elevated 2- aminoadipate in the plasma. Patients can have mild to severe intellectual disability, muscular hypotonia, developmental delay, ataxia, and epilepsy. Most cases are asymptomatic. {ECO:0000269|PubMed:23141293}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;skin;bone marrow;uterus;prostate;oesophagus;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; kidney;trigeminal ganglion; 0.13449 . 0.986521626 90.48124558 3727.11408 11.93027 DHX8 0.934509015310341 0.0654909846540979 3.5561403305839e-11 DEAH-box helicase 8 FUNCTION: Facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. {ECO:0000269|PubMed:8608946}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;synovium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);amygdala;trophoblast;cartilage;small intestine;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;white blood cells;whole blood;skeletal muscle; 0.32459 0.09593 -1.063626766 7.484076433 50.49145 1.39801 DHX9 0.999999986154664 1.3845335871776e-08 6.32631325614564e-22 DEAH-box helicase 9 FUNCTION: Unwinds double-stranded DNA and RNA in a 3' to 5' direction. Alteration of secondary structure may subsequently influence interactions with proteins or other nucleic acids. Functions as a transcriptional activator. Component of the CRD- mediated complex that promotes MYC mRNA stability. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms. Positively regulates HIV-1 LTR-directed gene expression. {ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:22190748}.; . . . . 0.90888 0.13318 -1.155457828 6.168907761 30.04953 0.95923 DHX9P1 . . . DEAH-box helicase 9 pseudogene 1 . . . . . . . . . . . DHX15 0.999997156110677 2.84388931616858e-06 6.63880770251447e-15 DEAH-box helicase 15 FUNCTION: Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. In cooperation with TFIP11 seem to be involved in the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns. {ECO:0000269|PubMed:19103666}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;muscle;pancreas;pia mater;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;tumor;white blood cells; 0.98442 0.44966 -0.824740496 11.67728238 20.5721 0.69910 DHX16 2.0110821119233e-07 0.999997430510378 2.3683814105227e-06 DEAH-box helicase 16 FUNCTION: Probable ATP-binding RNA helicase involved in pre-mRNA splicing.; . . . . 0.43046 0.11126 -0.020150552 52.25288983 501.85245 4.59583 DHX29 0.00352731615478607 0.996472656271851 2.75733629144799e-08 DEAH-box helicase 29 FUNCTION: ATP-binding RNA helicase involved in translation initiation. Part of the 43S preinitiation complex that is required for efficient initiation on mammalian mRNAs with structured 5'- UTRs by promoting efficient NTPase-dependent 48S complex formation. Specifically binds to the 40S ribosome near the mRNA entrance. Does not possess a processive helicase activity. {ECO:0000269|PubMed:19109895, ECO:0000269|PubMed:23706745}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; amygdala;dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.68652 0.10202 -0.992035476 8.604623732 544.90078 4.74818 DHX30 0.999999462569762 5.3743023751252e-07 1.14695344843148e-16 DEAH-box helicase 30 FUNCTION: Plays an important role in the assembly of the mitochondrial large ribosomal subunit (PubMed:25683715). Required for optimal function of the zinc-finger antiviral protein ZC3HAV1 (By similarity). Associates with mitochondrial DNA (PubMed:18063578). {ECO:0000250|UniProtKB:Q5BJS0, ECO:0000269|PubMed:18063578, ECO:0000269|PubMed:25683715}.; . . myocardium;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;spleen;cervix;kidney;stomach;peripheral nerve;cerebellum;thymus; . 0.56050 0.13398 -1.506435464 3.544468035 29.26995 0.93686 DHX32 6.96915711971685e-07 0.892687616343949 0.107311686740339 DEAH-box helicase 32 (putative) . . TISSUE SPECIFICITY: Expressed in lymphoid tissues (at protein level). Expressed in brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung, lymphoid tissues and blood leukocytes. {ECO:0000269|PubMed:12163057, ECO:0000269|PubMed:16181624}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; medulla oblongata;testis - interstitial;superior cervical ganglion;globus pallidus;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;cingulate cortex;skeletal muscle; 0.27890 0.09350 -0.50880549 21.72682236 236.88833 3.32379 DHX33 0.0083822781334698 0.991052359190516 0.000565362676014235 DEAH-box helicase 33 FUNCTION: Stimulates RNA polymerase I transcription of the 47S precursor rRNA. Associates with ribosomal DNA (rDNA) loci where it is involved in POLR1A recruitment. Important element of nucleolar organization. {ECO:0000269|PubMed:21930779}.; . . unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;colon;skin;uterus;lung;placenta;thyroid;visual apparatus;liver;testis;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12221 . -0.172654315 40.63458363 2125.04472 8.48845 DHX34 2.87824570211658e-08 0.995391392956775 0.00460857826076829 DEAH-box helicase 34 FUNCTION: Probable ATP-binding RNA helicase.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach; superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;temporal lobe;testis;trigeminal ganglion;skin;skeletal muscle; 0.49294 0.10569 -1.019881385 8.003066761 1159.03008 6.48069 DHX35 9.69273790916275e-11 0.973981761071891 0.026018238831181 DEAH-box helicase 35 FUNCTION: May be involved in pre-mRNA splicing.; . . lymphoreticular;smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;larynx;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lung;placenta;visual apparatus;duodenum;liver;amnion;spleen;head and neck;cervix;kidney;stomach;thymus; superior cervical ganglion; 0.27324 0.09942 -0.328796968 30.86223166 2233.3121 8.70874 DHX36 0.99055580055265 0.00944419944020669 7.14339010472901e-12 DEAH-box helicase 36 FUNCTION: Proposed to have a global role in regulating mRNA expression including transcriptional regulation and mRNA stability. Binds with high affinity to and resolves tetramolecular RNA and DNA quadruplex structures. Unwinds intramolecular quadruplexes derived from the ZIC1 and the MYC promoters. Binds to quadruplex structures in the promoters of YY1 and ALPL genes and regulates their expression. Binds to telomerase RNA template component (TERC) 5'-end (nucleotides 1-43) and unwinds an internal quadruplex formation in TERC 5'-end to promote P1 helix formation; the P1 helix acts as a template boundary ensuring accurate reverse transcription and is disrupted by quadruplex formation. May be involved in regulation of telomere length. Plays a role in degradation and deadenylation of mRNAs containing in their 3'-UTR the consensus ARE sequence element. May function in sex development and spermatogenesis. May play a role in ossification. {ECO:0000269|PubMed:12198572, ECO:0000269|PubMed:14731398, ECO:0000269|PubMed:16150737, ECO:0000269|PubMed:18842585, ECO:0000269|PubMed:20472641, ECO:0000269|PubMed:21149580, ECO:0000269|PubMed:21586581, ECO:0000269|PubMed:21993297, ECO:0000269|PubMed:22238380}.; . TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:12198572, ECO:0000269|PubMed:14731398}.; lymphoreticular;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; testis - interstitial;testis; 0.41559 0.13076 -1.063626766 7.484076433 4572.91937 13.56321 DHX37 0.978475417629788 0.0215245821029543 2.672576198097e-10 DEAH-box helicase 37 . . . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;muscle;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.23320 0.09926 -1.0455342 7.637414485 4588.20578 13.59867 DHX38 1.03801324416004e-06 0.999993481177933 5.48080882262213e-06 DEAH-box helicase 38 FUNCTION: Probable ATP-binding RNA helicase involved in pre-mRNA splicing.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;whole body;endometrium;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;blood;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; . 0.10249 0.13990 -1.144569759 6.363529134 154.29475 2.71461 DHX40 0.996354246510063 0.00364575143456766 2.05536957897776e-09 DEAH-box helicase 40 FUNCTION: Probable ATP-dependent RNA helicase. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12522690}.; medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;ciliary body;heart;cartilage;pineal body;urinary;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;lung;cornea;placenta;kidney;stomach;aorta;thymus; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.29370 0.13300 -0.80269335 12.23755603 18.00486 0.62873 DHX40P1 . . . DEAH-box helicase 40 pseudogene 1 . . . . . . . . . . . DHX57 4.41862619399682e-08 0.999995733784608 4.22202913053087e-06 DEAH-box helicase 57 FUNCTION: Probable ATP-binding RNA helicase.; . . unclassifiable (Anatomical System);cartilage;ovary;heart;epidermis;adrenal cortex;colon;parathyroid;vein;skin;breast;uterus;bile duct;pancreas;lung;frontal lobe;placenta;visual apparatus;pituitary gland;hypopharynx;liver;testis;amniotic fluid;head and neck;spleen;kidney;brain;stomach;gall bladder; testis - seminiferous tubule; 0.18434 . -1.13554371 6.404812456 568.16791 4.83789 DHX58 7.28555219955648e-08 0.696434590007963 0.303565337136515 DEXH-box helicase 58 FUNCTION: Acts as a regulator of DDX58/RIG-I and IFIH1/MDA5 mediated antiviral signaling. Cannot initiate antiviral signaling as it lacks the CARD domain required for activating MAVS/IPS1- dependent signaling events. Can have both negative and positive regulatory functions related to DDX58/RIG-I and IFIH1/MDA5 signaling and this role in regulating signaling may be complex and could probably depend on characteristics of the infecting virus or target cells, or both. Its inhibitory action on DDX58/RIG-I signaling may involve the following mechanisms: competition with DDX58/RIG-I for binding to the viral RNA, binding to DDX58/RIG-I and inhibiting its dimerization and interaction with MAVS/IPS1, competing with IKBKE in its binding to MAVS/IPS1 thereby inhibiting activation of interferon regulatory factor 3 (IRF3). Its positive regulatory role may involve unwinding or stripping nucleoproteins of viral RNA thereby facilitating their recognition by DDX58/RIG-I and IFIH1/MDA5. Involved in the innate immune response to various RNA viruses and some DNA viruses such as poxviruses, and also to the bacterial pathogen Listeria monocytogenes. Can bind both ssRNA and dsRNA, with a higher affinity for dsRNA. Shows a preference to 5'-triphosphorylated RNA, although it can recognize RNA lacking a 5'-triphosphate. {ECO:0000269|PubMed:16116171, ECO:0000269|PubMed:17020950, ECO:0000269|PubMed:17190814, ECO:0000269|PubMed:18411269, ECO:0000269|PubMed:19208642, ECO:0000269|PubMed:19211564, ECO:0000269|PubMed:19278996, ECO:0000269|PubMed:19380577, ECO:0000269|PubMed:21187438, ECO:0000269|PubMed:21525357}.; . . ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;unclassifiable (Anatomical System);heart;cartilage;blood;lens;pancreas;lung;macula lutea;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.08087 0.11805 -0.28106828 33.55744279 1079.87607 6.29985 DIABLO 0.000889964950590053 0.796275600676406 0.202834434373004 diablo IAP-binding mitochondrial protein FUNCTION: Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases. Isoform 3 attenuates the stability and apoptosis- inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-proteasome pathway. Isoform 3 also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. Isoform 1 is defective in the capacity to down-regulate the XIAP/BIRC4 abundance. {ECO:0000269|PubMed:10929711, ECO:0000269|PubMed:14523016, ECO:0000269|PubMed:15200957}.; DISEASE: Deafness, autosomal dominant, 64 (DFNA64) [MIM:614152]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:21722859}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed with highest expression in testis. Expression is also high in heart, liver, kidney, spleen, prostate and ovary. Low in brain, lung, thymus and peripheral blood leukocytes. Isoform 3 is ubiquitously expressed. {ECO:0000269|PubMed:10929711, ECO:0000269|PubMed:14523016}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;salivary gland;sympathetic chain;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;cochlea;bone;pituitary gland;iris;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;duodenum;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;cerebellum; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion; 0.09995 . -0.205617011 38.57631517 31.18086 0.98367 DIANPH . . . diabetic nephropathy . . . . . . . . . . . DIAPH1 0.267109674008721 0.732890310401282 1.55899968489512e-08 diaphanous related formin 1 FUNCTION: Acts in a Rho-dependent manner to recruit PFY1 to the membrane. Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization. Required for cytokinesis, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics. Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration (By similarity). Has neurite outgrowth promoting activity (By similarity). In hear cells, it may play a role in the regulation of actin polymerization in hair cells. The MEMO1-RHOA- DIAPH1 signaling pathway plays an important role in ERBB2- dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape (PubMed:20937854, PubMed:21834987). Plays a role in brain development (PubMed:24781755). {ECO:0000250|UniProtKB:O08808, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:24781755}.; DISEASE: Deafness, autosomal dominant, 1 (DFNA1) [MIM:124900]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:9360932}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Seizures, cortical blindness, microcephaly syndrome (SCBMS) [MIM:616632]: A severe autosomal recessive neurodevelopmental disorder characterized by microcephaly, early- onset seizures, severely delayed psychomotor development, short stature, and cortical blindness. {ECO:0000269|PubMed:24781755, ECO:0000269|PubMed:26463574}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, heart, placenta, lung, kidney, pancreas, liver, skeletal muscle and cochlea.; lymphoreticular;colon;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;thyroid;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);tongue;islets of Langerhans;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.49753 0.16376 -1.240018202 5.461193678 140.54727 2.58545 DIAPH2 0.999119100290442 0.000880899645201355 6.43568847124018e-11 diaphanous related formin 2 FUNCTION: Could be involved in oogenesis. Involved in the regulation of endosome dynamics. Implicated in a novel signal transduction pathway, in which isoform 3 and CSK are sequentially activated by RHOD to regulate the motility of early endosomes through interactions with the actin cytoskeleton. {ECO:0000269|PubMed:12577064}.; DISEASE: Premature ovarian failure 2A (POF2A) [MIM:300511]: An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol. {ECO:0000269|PubMed:9497258}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in testis, ovary, small intestine, prostate, lung, liver, kidney and leukocytes.; unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;colon;skeletal muscle;skin;uterus;prostate;oesophagus;placenta;thyroid;head and neck;cervix;brain;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.56881 0.27299 -0.999300439 8.368719038 38.85136 1.15117 DIAPH2-AS1 . . . DIAPH2 antisense RNA 1 FUNCTION: May function as an early signal that helps mediate the activation of T-cells. {ECO:0000269|PubMed:8133036}.; . . . . . . . . . . DIAPH3 1.2254557817215e-12 0.976666900805318 0.0233330991934563 diaphanous related formin 3 FUNCTION: Binds to GTP-bound form of Rho and to profilin. Acts in a Rho-dependent manner to recruit profilin to the membrane, where it promotes actin polymerization. It is required for cytokinesis, stress fiber formation, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics (By similarity). {ECO:0000250}.; DISEASE: Auditory neuropathy, autosomal dominant, 1 (AUNA1) [MIM:609129]: A form of sensorineural hearing loss with absent or severely abnormal auditory brainstem response, in the presence of normal cochlear outer hair cell function and normal otoacoustic emissions. Auditory neuropathies result from a lesion in the area including the inner hair cells, connections between the inner hair cells and the cochlear branch of the auditory nerve, the auditory nerve itself and auditory pathways of the brainstem. {ECO:0000269|PubMed:20624953}. Note=The disease is caused by mutations affecting the gene represented in this entry. A disease- causing mutation in the conserved 5'-UTR leads to increased protein expression (PubMed:20624953). {ECO:0000269|PubMed:20624953}.; . unclassifiable (Anatomical System);breast;testis;blood;germinal center;mammary gland;skin;skeletal muscle; superior cervical ganglion;pons;skin; 0.12782 0.08502 0.185543665 66.2715263 1035.20492 6.17751 DIAPH3-AS1 . . . DIAPH3 antisense RNA 1 . . . . . . . . . . . DIAPH3-AS2 . . . DIAPH3 antisense RNA 2 . . . . . . . . . . . DICER1 0.9999945509466 5.44905339955331e-06 2.22094630940701e-18 dicer 1 ribonuclease III FUNCTION: Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA- induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, also called RNA interference, controls the elimination of transcripts from mobile and repetitive DNA elements of the genome but also the degradation of exogenous RNA of viral origin for instance. The miRNA pathway on the other side is a mean to specifically regulate the expression of target genes. {ECO:0000269|PubMed:15242644, ECO:0000269|PubMed:15973356, ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387, ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:18178619, ECO:0000269|PubMed:19219043}.; DISEASE: Pleuropulmonary blastoma (PPB) [MIM:601200]: A rare pediatric intrathoracic neoplasm. The tumor arises from the lung, pleura, or both, and appears to be purely mesenchymal in phenotype. It lacks malignant epithelial elements, a feature that distinguishes it from the classic adult-type pulmonary blastoma. It arises during fetal lung development and is often part of an inherited cancer syndrome. The tumor contain both epithelial and mesenchymal cells. Early in tumorigenesis, cysts form in lung airspaces, and these cysts are lined with benign-appearing epithelium. Mesenchymal cells susceptible to malignant transformation reside within the cyst walls and form a dense layer beneath the epithelial lining. In a subset of patients, overgrowth of the mesenchymal cells produces a sarcoma, a transition that is associated with a poorer prognosis. Some patients have multilocular cystic nephroma, a benign kidney tumor. {ECO:0000269|PubMed:19556464}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Goiter multinodular 1, with or without Sertoli-Leydig cell tumors (MNG1) [MIM:138800]: A common disorder characterized by nodular overgrowth of the thyroid gland. Some individuals may also develop Sertoli-Leydig cell tumors, usually of the ovary. {ECO:0000269|PubMed:21205968}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Rhabdomyosarcoma, embryonal, 2 (RMSE2) [MIM:180295]: A form of rhabdomyosarcoma, a highly malignant tumor of striated muscle derived from primitive mesenchymal cells and exhibiting differentiation along rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most frequently occurring soft tissue sarcomas and the most common in children. It occurs in four forms: alveolar, pleomorphic, embryonal and botryoidal rhabdomyosarcomas. {ECO:0000269|PubMed:21882293}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=DICER1 mutations have been found in uterine cervix embryonal rhabdomyosarcoma, primitive neuroectodermal tumor, Wilms tumor, pulmonary sequestration and juvenile intestinal polyp (PubMed:21882293). Somatic missense mutations affecting the RNase IIIb domain of DICER1 are common in non-epithelial ovarian tumors. These mutations do not abolish DICER1 function but alter it in specific cell types, a novel mechanism through which perturbation of microRNA processing may be oncogenic (PubMed:22187960). {ECO:0000269|PubMed:21882293, ECO:0000269|PubMed:22187960}.; . smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;pituitary gland;testis;amniotic fluid;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; amygdala;dorsal root ganglion;superior cervical ganglion;occipital lobe;spinal cord;prefrontal cortex;appendix;trigeminal ganglion;skeletal muscle;parietal lobe; 0.41655 0.49485 -1.521247944 3.44420854 150.94725 2.68525 DICER1-AS1 . . . DICER1 antisense RNA 1 . . . . . . . . . . . DIDO1 0.99999076875449 9.23124550969987e-06 8.02042208147514e-18 death inducer-obliterator 1 FUNCTION: Putative transcription factor, weakly pro-apoptotic when overexpressed (By similarity). Tumor suppressor. Required for early embryonic stem cell development. {ECO:0000250, ECO:0000269|PubMed:16127461}.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;placenta;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.59140 0.14648 -1.407954242 4.151922623 412.69422 4.25392 DIEXF 0.0492348597469146 0.950566490112206 0.000198650140879806 digestive organ expansion factor homolog (zebrafish) FUNCTION: Regulates the p53 pathway to control the expansion growth of digestive organs. {ECO:0000250}.; . . . . 0.39061 0.23111 1.025142459 91.07100731 341.99855 3.92161 DIH1 . . . diaphragmatic hernia 1 . . . . . . . . . . . DIMT1 1.47117897450072e-05 0.854128005052381 0.145857283157874 DIM1 dimethyladenosine transferase 1 homolog FUNCTION: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;cochlea;oesophagus;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;adipose tissue;salivary gland;tumor;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.24528 0.37575 -0.163345027 41.24793583 30.45427 0.97032 DIO1 0.271104148641763 0.704517701028533 0.0243781503297039 deiodinase, iodothyronine, type I FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'- tetraiodothyronine) into T3 (3,5,3'-triiodothyronine) and of T3 into T2 (3,3'-diiodothyronine). Plays a role in providing a source of plasma T3 by deiodination of T4 in peripheral tissues such as liver and kidney.; . . unclassifiable (Anatomical System);thyroid;liver;spleen;kidney; superior cervical ganglion;fetal liver;thyroid;liver;kidney;pons;fetal thyroid;trigeminal ganglion; 0.22979 . -0.249709319 35.74545883 58.24117 1.54477 DIO2 0.217796806901725 0.744069584291628 0.0381336088066468 deiodinase, iodothyronine, type II FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'- tetraiodothyronine) into T3 (3,5,3'-triiodothyronine). Essential for providing the brain with appropriate levels of T3 during the critical period of development.; . TISSUE SPECIFICITY: Heart, skeletal muscle, placenta, fetal brain and several regions of the adult brain.; . . 0.12534 . 0.03689118 56.64071715 164.63001 2.80177 DIO2-AS1 . . . DIO2 antisense RNA 1 . . . . . . . . . . . DIO3 0.768046570846978 0.223782706536682 0.00817072261634102 deiodinase, iodothyronine, type III FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'- tetraiodothyronine) into RT3 (3,3',5'-triiodothyronine) and of T3 (3,5,3'-triiodothyronine) into T2 (3,3'-diiodothyronine). RT3 and T2 are inactive metabolites. May play a role in preventing premature exposure of developing fetal tissues to adult levels of thyroid hormones. Can regulate circulating fetal thyroid hormone concentrations throughout gestation. Essential role for regulation of thyroid hormone inactivation during embryological development. {ECO:0000269|PubMed:7593630}.; . TISSUE SPECIFICITY: Expressed in placenta and several fetal tissues.; . . 0.29932 . -0.293801652 32.93819297 26.09417 0.84714 DIO3OS . . . DIO3 opposite strand/antisense RNA (head to head) . . . . . . . . . . . DIP2A 0.726099073608303 0.273900924724522 1.6671750069127e-09 disco interacting protein 2 homolog A FUNCTION: May provide positional cues for axon pathfinding and patterning in the central nervous system.; . TISSUE SPECIFICITY: Low expression in all tissues tested.; smooth muscle;sympathetic chain;colon;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;oral cavity;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;adrenal cortex;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.20513 0.09801 -2.776863601 0.678225997 1074.58254 6.28283 DIP2A-IT1 . . . DIP2A intronic transcript 1 . . . . . . . . . . . DIP2B 0.999668381879693 0.000331618120306863 8.26795431783405e-17 disco interacting protein 2 homolog B . . TISSUE SPECIFICITY: Moderately expressed in adult brain, placenta, skeletal muscle, heart, kidney, pancreas, lung, spleen and colon. Expression was weaker in adult liver, kidney, spleen, and ovary, and in fetal brain and liver. In the brain, it is expressed in the cerebral cortex; the frontal, parietal, occipital and temporal lobes; the paracentral gyrus; the pons; the corpus callosum and the hippocampus. Highest expression levels in the brain were found in the cerebral cortex and the frontal and parietal lobes. {ECO:0000269|PubMed:10819331, ECO:0000269|PubMed:17236128}.; ovary;salivary gland;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;whole brain;thalamus;superior cervical ganglion;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;atrioventricular node;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.30490 0.09843 -1.809748265 2.193913659 364.30858 4.04045 DIP2C 0.999999838277401 1.61722598949221e-07 2.08733517764299e-21 disco interacting protein 2 homolog C . . . ovary;colon;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;pituitary gland;testis;dura mater;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;meninges;lymph node;heart;blood;lens;skeletal muscle;pancreas;pia mater;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; amygdala;dorsal root ganglion;whole brain;medulla oblongata;occipital lobe;superior cervical ganglion;prefrontal cortex;caudate nucleus;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle;cerebellum; 0.19810 0.10061 -3.62272315 0.294880868 69.01323 1.72102 DIRAS1 0.62334167137764 0.345008073986866 0.031650254635494 DIRAS family GTP binding RAS like 1 FUNCTION: Displays low GTPase activity and exist predominantly in the GTP-bound form.; . TISSUE SPECIFICITY: Highly expressed in heart and brain. {ECO:0000269|PubMed:12107278, ECO:0000269|PubMed:12194967}.; lymphoreticular;myocardium;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;bone;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;lung;macula lutea;hippocampus;visual apparatus;liver;duodenum;hypopharynx;head and neck;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;kidney;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.15842 0.12940 -0.119252484 44.53880632 5.43659 0.20180 DIRAS2 0.327172252454951 0.608465295663069 0.0643624518819801 DIRAS family GTP binding RAS like 2 FUNCTION: Displays low GTPase activity and exist predominantly in the GTP-bound form.; . TISSUE SPECIFICITY: Highly expressed in brain. {ECO:0000269|PubMed:12194967}.; . . 0.18683 0.14229 -0.141298762 42.87567823 5.62871 0.21088 DIRAS3 0.0372391763198298 0.635192759159983 0.327568064520188 DIRAS family GTP binding RAS like 3 . . TISSUE SPECIFICITY: Expressed in normal ovarian and breast epithelial cells but not in ovarian and breast cancers.; . . 0.07750 0.15446 -0.05129383 49.75819769 38.92233 1.15291 DIRC1 0.0222588439435162 0.532142118412193 0.44559903764429 disrupted in renal carcinoma 1 . . TISSUE SPECIFICITY: Expressed at low steady-state level in adult placenta, testis, ovary, prostate, fetal kidney, spleen and skeletal muscle. {ECO:0000269|PubMed:11587072}.; unclassifiable (Anatomical System);uterus;heart;skin; superior cervical ganglion;globus pallidus;ciliary ganglion;pons;trigeminal ganglion; 0.09074 . 0.635788962 83.63411182 48.51691 1.35897 DIRC2 6.7997685830619e-06 0.714248826788268 0.285744373443149 disrupted in renal carcinoma 2 FUNCTION: Electrogenic metabolite transporter. {ECO:0000269|PubMed:21692750}.; DISEASE: Note=A chromosomal aberration involving DIRC2 has been found in a family with renal carcinoma. Translocation t(2;3)(q35;q21) (PubMed:11912179). {ECO:0000269|PubMed:11912179}.; TISSUE SPECIFICITY: Ubiquitous. Expressed in proximal tubular cells of the kidney. {ECO:0000269|PubMed:11912179}.; unclassifiable (Anatomical System);lymph node;ovary;heart;islets of Langerhans;hypothalamus;colon;parathyroid;blood;skin;bone marrow;breast;uterus;prostate;lung;cerebral cortex;placenta;hippocampus;hypopharynx;liver;testis;cervix;head and neck;spleen;kidney;brain;mammary gland;stomach; superior cervical ganglion;placenta; 0.10586 0.08291 -0.293801652 32.93819297 24.77583 0.81354 DIRC3 . . . disrupted in renal carcinoma 3 . . . . . . . . . 1079.12143 6.29796 DIRC3-AS1 . . . DIRC3 antisense RNA 1 . . . . . . . . . . . DIS3 2.04523468343561e-11 0.953344005089227 0.0466559948903208 DIS3 homolog, exosome endoribonuclease and 3'-5' exoribonuclease FUNCTION: Putative catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. DIS3 has both 3'-5' exonuclease and endonuclease activities. {ECO:0000269|PubMed:19056938, ECO:0000269|PubMed:20531386}.; . TISSUE SPECIFICITY: Widely expressed.; . . 0.42672 0.11422 -0.016511957 52.31776362 2458.67493 9.23038 DIS3L 1.29328456685495e-10 0.982437431535476 0.0175625683351954 DIS3 like exosome 3'-5' exoribonuclease FUNCTION: Putative cytoplasm-specific catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. {ECO:0000269|PubMed:20531386, ECO:0000269|PubMed:20531389}.; . . colon;parathyroid;skin;retina;larynx;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;blood;breast;lung;adrenal gland;placenta;visual apparatus;liver;alveolus;cervix;head and neck;stomach;thymus; superior cervical ganglion; 0.06265 0.10069 -0.25902169 34.96697334 2222.56237 8.68242 DIS3L2 0.863517182071107 0.136482675808421 1.4212047270836e-07 DIS3 like 3'-5' exoribonuclease 2 FUNCTION: 3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of both mRNAs and miRNAs that have been polyuridylated by a terminal uridylyltransferase, such as ZCCHC11/TUT4. Mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'. Mediates degradation of uridylated pre-let-7 miRNAs, contributing to the maintenance of embryonic stem (ES) cells. Essential for correct mitosis, and negatively regulates cell proliferation. {ECO:0000255|HAMAP-Rule:MF_03045, ECO:0000269|PubMed:23756462, ECO:0000269|PubMed:24141620}.; DISEASE: Perlman syndrome (PRLMNS) [MIM:267000]: An autosomal recessive congenital overgrowth syndrome. Affected children are large at birth, are hypotonic, and show organomegaly, characteristic facial dysmorphisms (inverted V-shaped upper lip, prominent forehead, deep-set eyes, broad and flat nasal bridge, and low-set ears), renal anomalies (nephromegaly and hydronephrosis), frequent neurodevelopmental delay, and high neonatal mortality. Perlman syndrome is associated with a high risk of Wilms tumor. Histologic examination of the kidneys in affected children shows frequent nephroblastomatosis, which is a precursor lesion for Wilms tumor. {ECO:0000269|PubMed:22306653, ECO:0000269|PubMed:23486540, ECO:0000269|PubMed:23576526}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;heart;ovary;islets of Langerhans;hypothalamus;colon;blood;parathyroid;lens;skeletal muscle;bone marrow;pancreas;whole body;lung;nasopharynx;placenta;bone;visual apparatus;testis;kidney;mammary gland;brain; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.06945 0.09055 -0.282886048 33.53385232 511.74911 4.63116 DIS3L2P1 . . . DIS3 like 3'-5' exoribonuclease 2 pseudogene 1 . . . . . . . . . . . DISC1 0.0197098835616187 0.976388716381253 0.00390140005712806 disrupted in schizophrenia 1 FUNCTION: Involved in the regulation of multiple aspects of embryonic and adult neurogenesis. Required for neural progenitor proliferation in the ventrical/subventrical zone during embryonic brain development and in the adult dentate gyrus of the hippocampus. Participates in the Wnt-mediated neural progenitor proliferation as a positive regulator by modulating GSK3B activity and CTNNB1 abundance. Plays a role as a modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including neuron positioning, dendritic development and synapse formation. Inhibits the activation of AKT-mTOR signaling upon interaction with CCDC88A. Regulates the migration of early-born granule cell precursors toward the dentate gyrus during the hippocampal development. Plays a role, together with PCNT, in the microtubule network formation. {ECO:0000269|PubMed:18955030, ECO:0000269|PubMed:19303846, ECO:0000269|PubMed:19502360}.; DISEASE: Note=A chromosomal aberration involving DISC1 segregates with schizophrenia and related psychiatric disorders in a large Scottish family. Translocation t(1;11)(q42.1;q14.3). The truncated DISC1 protein produced by this translocation is unable to interact with ATF4, ATF5 and NDEL1.; DISEASE: Schizophrenia 9 (SCZD9) [MIM:604906]: A complex, multifactorial psychotic disorder or group of disorders characterized by disturbances in the form and content of thought (e.g. delusions, hallucinations), in mood (e.g. inappropriate affect), in sense of self and relationship to the external world (e.g. loss of ego boundaries, withdrawal), and in behavior (e.g bizarre or apparently purposeless behavior). Although it affects emotions, it is distinguished from mood disorders in which such disturbances are primary. Similarly, there may be mild impairment of cognitive function, and it is distinguished from the dementias in which disturbed cognitive function is considered primary. Some patients manifest schizophrenic as well as bipolar disorder symptoms and are often given the diagnosis of schizoaffective disorder. {ECO:0000269|PubMed:11468279, ECO:0000269|PubMed:14532331, ECO:0000269|PubMed:15939883}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Highly expressed in the dentate gyrus of the hippocampus. Also expressed in the temporal and parahippocampal cortices and cells of the white matter. {ECO:0000269|PubMed:16510495}.; unclassifiable (Anatomical System); superior cervical ganglion;atrioventricular node;pons; 0.08914 0.26891 0.20394914 67.45694739 3238.0087 10.83421 DISC1-IT1 . . . DISC1 intronic transcript 1 . . . . . . . . . . . DISC1FP1 . . . DISC1 fusion partner 1 (non-protein coding) . . . . . . . . . . . DISC2 . . . disrupted in schizophrenia 2 (non-protein coding) . . . . . . . . . . . DISP1 4.23342758464293e-06 0.997859917504751 0.00213584906766469 dispatched RND transporter family member 1 FUNCTION: Functions in hedgehog (Hh) signaling. Regulates the release and extracellular accumulation of cholesterol-modified hedgehog proteins and is hence required for effective production of the Hh signal (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;heart;muscle;colon;blood;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;lung;endometrium;bone;macula lutea;liver;testis;spleen;kidney;brain;bladder;mammary gland; superior cervical ganglion;testis;trigeminal ganglion; 0.16068 0.11183 0.369203982 74.77589054 4506.07665 13.48325 DISP2 0.0162511640768809 0.983534330297595 0.00021450562552355 dispatched RND transporter family member 2 . . . unclassifiable (Anatomical System);heart;blood;lens;skin;retina;bone marrow;uterus;pancreas;whole body;lung;frontal lobe;hippocampus;brain;stomach; dorsal root ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.37491 0.10902 0.481263226 78.95730125 1049.95108 6.22287 DISP3 . . . dispatched RND transporter family member 3 . . TISSUE SPECIFICITY: Expressed in brain and testis. {ECO:0000269|PubMed:15645143}.; . . 0.14945 0.11858 -0.251753628 35.00235905 . . DIXDC1 4.26871314762917e-06 0.997885056696332 0.00211067459052053 DIX domain containing 1 FUNCTION: Positive effector of the Wnt signaling pathway; activates WNT3A signaling via DVL2. Regulates JNK activation by AXIN1 and DVL2. {ECO:0000269|PubMed:15262978, ECO:0000269|PubMed:21189423}.; . TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in cardiac and skeletal muscles. {ECO:0000269|PubMed:16814745}.; smooth muscle;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;frontal lobe;thyroid;bone;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;breast;lung;placenta;hippocampus;visual apparatus;macula lutea;liver;spleen;stomach; amygdala;whole brain;occipital lobe;thalamus;adipose tissue;hypothalamus;spinal cord;caudate nucleus;uterus;fetal brain;thyroid;prefrontal cortex;parietal lobe;cerebellum; 0.28623 0.10690 . . 168.08416 2.83065 DKC1 0.9989001727892 0.00109981386778464 1.3343015451071e-08 dyskerin pseudouridine synthase 1 FUNCTION: Isoform 1: Required for ribosome biogenesis and telomere maintenance. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. Also required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme.; DISEASE: Hoyeraal-Hreidarsson syndrome (HHS) [MIM:305000]: A clinically severe variant of dyskeratosis congenita that is characterized by multisystem involvement, early onset in utero, and often results in death in childhood. Affected individuals show intrauterine growth retardation, microcephaly, cerebellar hypoplasia, delayed development, and bone marrow failure resulting in immunodeficiency. {ECO:0000269|PubMed:10583221, ECO:0000269|PubMed:12437656, ECO:0000269|PubMed:19734544, ECO:0000269|PubMed:24914498}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10903840}.; . . 0.96016 0.24988 0.104848986 61.49445624 70.37291 1.74518 DKK1 0.075574375488613 0.872450160971675 0.0519754635397121 dickkopf WNT signaling pathway inhibitor 1 FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero- posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease. {ECO:0000269|PubMed:22000856}.; . TISSUE SPECIFICITY: Placenta.; . . 0.24823 0.59197 0.415317661 76.81056853 38.85123 1.15088 DKK2 0.864037651771095 0.135550653285884 0.000411694943021127 dickkopf WNT signaling pathway inhibitor 2 FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero- posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in heart, brain, skeletal muscle and lung.; unclassifiable (Anatomical System);heart;skin;retina;uterus;whole body;cochlea;nasopharynx;placenta;bone;testis;brain;aorta; dorsal root ganglion;superior cervical ganglion;appendix;pons;atrioventricular node; 0.44953 0.14403 0.082802743 60.09082331 2261.45499 8.78864 DKK3 1.88888907624104e-05 0.695129650855814 0.304851460253423 dickkopf WNT signaling pathway inhibitor 3 FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero- posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highest expression in heart, brain, and spinal cord. {ECO:0000269|PubMed:10570958, ECO:0000269|Ref.4}.; smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;iris;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;larynx;bone;testis;spinal ganglion;artery;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; amygdala;whole brain;medulla oblongata;thalamus;occipital lobe;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.30876 0.28825 0.729426781 86.17008728 247.33215 3.39259 DKK4 0.0213797596918408 0.907646768228221 0.0709734720799379 dickkopf WNT signaling pathway inhibitor 4 FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero- posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in cerebellum, T-cells, esophagus and lung.; unclassifiable (Anatomical System);breast;hypothalamus;colon;stomach; superior cervical ganglion;pancreas;atrioventricular node; 0.06897 0.12956 -0.405853867 26.23260203 20.21262 0.69207 DKKL1 0.000105207763605655 0.584790086125637 0.415104706110757 dickkopf like acrosomal protein 1 . . . unclassifiable (Anatomical System);optic nerve;whole body;frontal lobe;macula lutea;testis;fovea centralis;choroid;lens;retina; testis - interstitial;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;testis;cingulate cortex;parietal lobe;skeletal muscle; 0.37280 0.12586 1.638895725 96.11347016 6845.74883 17.63695 DKKL1P1 . . . dickkopf-like 1 pseudogene 1 . . . . . . . . . . . DLAT 6.67603193149511e-06 0.974397294278349 0.0255960296897199 dihydrolipoamide S-acetyltransferase FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.; DISEASE: Note=Primary biliary cirrhosis is a chronic, progressive cholestatic liver disease characterized by the presence of antimitochondrial autoantibodies in patients' serum. It manifests with inflammatory obliteration of intra-hepatic bile duct, leading to liver cell damage and cirrhosis. Patients with primary biliary cirrhosis show autoantibodies against the E2 component of pyruvate dehydrogenase complex.; DISEASE: Pyruvate dehydrogenase E2 deficiency (PDHE2 deficiency) [MIM:245348]: Pyruvate dehydrogenase (PDH) deficiency is a major cause of primary lactic acidosis and neurological dysfunction in infancy and early childhood. In this form of PDH deficiency episodic dystonia is the major neurological manifestation, with other more common features of pyruvate dehydrogenase deficiency, such as hypotonia and ataxia, being less prominent. {ECO:0000269|PubMed:16049940}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;iris;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;spinal cord;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;adipose tissue;heart;ciliary ganglion;skeletal muscle; 0.80314 0.42344 0.356452144 74.62845011 6667.69783 17.30223 DLC1 0.992807272978016 0.00719272700385759 1.81262518547771e-11 DLC1 Rho GTPase activating protein FUNCTION: Functions as a GTPase-activating protein for the small GTPases RHOA, RHOB, RHOC and CDC42, terminating their downstream signaling. This induces morphological changes and detachment through cytoskeletal reorganization, playing a critical role in biological processes such as cell migration and proliferation. Also functions in vivo as an activator of the phospholipase PLCD1. Active DLC1 increases cell migration velocity but reduces directionality. {ECO:0000269|PubMed:18786931, ECO:0000269|PubMed:19170769, ECO:0000269|PubMed:19710422}.; . TISSUE SPECIFICITY: Highest level of expression in the spleen, with rather lower levels in prostate, testis, ovary, small intestine and colon, but none in the thymus.; myocardium;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;brain;heart;cartilage;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;islets of Langerhans;bile duct;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;head and neck;kidney;aorta;stomach;thymus; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.21331 0.09513 -0.437506654 24.64024534 762.817 5.47345 DLD 0.371053212777847 0.628849204207725 9.75830144270376e-05 dihydrolipoamide dehydrogenase FUNCTION: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction.; DISEASE: Dihydrolipoamide dehydrogenase deficiency (DLDD) [MIM:246900]: An autosomal recessive metabolic disorder characterized biochemically by a combined deficiency of the branched-chain alpha-keto acid dehydrogenase complex (BCKDC), pyruvate dehydrogenase complex (PDC), and alpha-ketoglutarate dehydrogenase complex (KGDC). Clinically, affected individuals have lactic acidosis and neurologic deterioration due to sensitivity of the central nervous system to defects in oxidative metabolism. {ECO:0000269|PubMed:8506365, ECO:0000269|PubMed:8968745, ECO:0000269|PubMed:9934985}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;spinal cord;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;colon;parathyroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;muscle;bile duct;pancreas;pia mater;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; skeletal muscle; 0.23887 0.88655 -0.113792788 45.25831564 97.39591 2.13230 DLEC1 6.45016367111782e-18 0.995627230372842 0.00437276962715849 deleted in lung and esophageal cancer 1 FUNCTION: May act as a tumor suppressor by inhibiting cell proliferation. {ECO:0000269|PubMed:10213508}.; DISEASE: Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis. Note=The gene represented in this entry may be involved in disease pathogenesis. DLEC1 silencing due to promoter methylation and aberrant transcription are implicated in the development of lung cancer.; DISEASE: Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the esophagus. The most common types are esophageal squamous cell carcinoma and adenocarcinoma. Cancer of the esophagus remains a devastating disease because it is usually not detected until it has progressed to an advanced incurable stage. {ECO:0000269|PubMed:10213508}. Note=The gene represented in this entry may be involved in disease pathogenesis. DLEC1 silencing due to promoter methylation and aberrant transcription may be implicated in the development of esophageal cancer.; TISSUE SPECIFICITY: Expressed in all tissues examined. Expression is highest in prostate and testis. {ECO:0000269|PubMed:10213508}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;pancreas;lung;cornea;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;uterus corpus;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.98238 0.10873 0.161491526 64.92686954 3130.50362 10.64467 DLEC1P1 . . . deleted in lung and esophageal cancer 1 pseudogene 1 . . . . . . . . . . . DLEU1 . . . deleted in lymphocytic leukemia 1 (non-protein coding) FUNCTION: May act as a tumor suppressor.; . . . . 0.02957 . . . 640.06835 5.08709 DLEU1-AS1 . . . DLEU1 antisense RNA 1 . . . . . . . . . . . DLEU2 . . . deleted in lymphocytic leukemia 2 (non-protein coding) . . . brain; . 0.03989 0.08185 . . . . DLEU2L . . . deleted in lymphocytic leukemia 2-like . . . ovary;islets of Langerhans;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;lung;thyroid;macula lutea;visual apparatus;liver;pituitary gland;testis; . 0.03989 0.08185 . . 0.63842 0.00934 DLEU7 0.0310204749254743 0.59934102064686 0.369638504427665 deleted in lymphocytic leukemia, 7 . . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:14706829}.; lung;testis;brain; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.10449 0.07903 . . 765.51721 5.48128 DLEU7-AS1 . . . DLEU7 antisense RNA 1 . . . . . . . . . . . DLG1 0.998742049204796 0.00125795079494742 2.57104109505953e-13 discs large homolog 1, scribble cell polarity complex component FUNCTION: Essential multidomain scaffolding protein required for normal development (By similarity). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel. {ECO:0000250, ECO:0000269|PubMed:10656683, ECO:0000269|PubMed:12445884, ECO:0000269|PubMed:14699157, ECO:0000269|PubMed:15263016, ECO:0000269|PubMed:19213956, ECO:0000269|PubMed:20605917}.; . TISSUE SPECIFICITY: Abundantly expressed in atrial myocardium (at protein level). Expressed in lung fibroblasts, cervical epithelial and B-cells (at protein level). Widely expressed, with isoforms displaying different expression profiles. {ECO:0000269|PubMed:12445884, ECO:0000269|PubMed:19213956, ECO:0000269|PubMed:7937897}.; ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;larynx;thyroid;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; amygdala;dorsal root ganglion;superior cervical ganglion;occipital lobe;medulla oblongata;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;atrioventricular node;skeletal muscle;skin;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.99058 0.18443 0.400544645 76.40953055 1887.1995 7.98983 DLG1-AS1 . . . DLG1 antisense RNA 1 . . . . . . . . . . . DLG2 0.673545370161857 0.326454626990323 2.84781972675477e-09 discs large homolog 2 FUNCTION: Required for perception of chronic pain through NMDA receptor signaling. Regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord. Interacts with the cytoplasmic tail of NMDA receptor subunits as well as inward rectifying potassium channels. Involved in regulation of synaptic stability at cholinergic synapses. Part of the postsynaptic protein scaffold of excitatory synapses (By similarity). {ECO:0000250}.; . . prostate;lung;whole body;frontal lobe;ovary;placenta;visual apparatus;testis;colon;parathyroid;kidney;brain;skeletal muscle; superior cervical ganglion;globus pallidus;ciliary ganglion;parietal lobe; 0.98599 0.11658 -1.596455314 3.037272942 110.44489 2.28742 DLG2-AS1 . . . DLG2 antisense RNA 1 . . . . . . . . . . . DLG3 0.999544464508013 0.000455533934514725 1.55747246994448e-09 discs large homolog 3 FUNCTION: Required for learning most likely through its role in synaptic plasticity following NMDA receptor signaling.; DISEASE: Mental retardation, X-linked 90 (MRX90) [MIM:300850]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non- syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. {ECO:0000269|PubMed:15185169}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;atrioventricular node;pons;skeletal muscle;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;cerebellum; 0.99914 0.34195 -0.247889024 35.98726115 26.23007 0.84957 DLG3-AS1 . . . DLG3 antisense RNA 1 . . . . . . . . . . . DLG4 0.996592666400884 0.00340733324651338 3.52602826809443e-10 discs large homolog 4 FUNCTION: Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Brain.; unclassifiable (Anatomical System);amygdala;cartilage;ovary;colon;skeletal muscle;retina;breast;pancreas;prostate;lung;frontal lobe;trabecular meshwork;hippocampus;hypopharynx;testis;head and neck;kidney;mammary gland;brain;cerebellum; amygdala;medulla oblongata;superior cervical ganglion;temporal lobe;prefrontal cortex;ciliary ganglion;pons;caudate nucleus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.98317 0.61145 -0.66859065 15.76433121 53.37804 1.45165 DLG5 0.999998542279994 1.45772000618587e-06 2.18515863181878e-18 discs large homolog 5 FUNCTION: May play a role at the plasma membrane in the maintenance of the structure of epithelial cells and in the transmission of extracellular signals to the membrane and cytoskeleton. {ECO:0000269|PubMed:11876824}.; . TISSUE SPECIFICITY: Highly expressed in the placenta and prostate. Expressed at a lower level in the thyroid, spinal cord, trachea, adrenal gland, skeletal muscle, pancreas, heart, brain, liver and kidney. A short splice product shows more limited expression, being absent from at least the brain. {ECO:0000269|PubMed:11876824, ECO:0000269|PubMed:12657639, ECO:0000269|PubMed:9738934}.; . . 0.27889 0.16537 -2.369063868 1.126444916 774.17189 5.50725 DLG5-AS1 . . . DLG5 antisense RNA 1 . . . . . . . . . . . DLGAP1 0.993045514283556 0.00695447575874536 9.95769830937997e-09 discs large homolog associated protein 1 FUNCTION: Part of the postsynaptic scaffold in neuronal cells.; . TISSUE SPECIFICITY: Expressed in brain.; unclassifiable (Anatomical System);optic nerve;lung;frontal lobe;ovary;macula lutea;testis;fovea centralis;choroid;lens;brain;skin;retina; amygdala;subthalamic nucleus;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.79189 0.12527 -1.594640695 3.054965794 104.85869 2.21324 DLGAP1-AS1 . . . DLGAP1 antisense RNA 1 . . . . . . . . . . . DLGAP1-AS2 . . . DLGAP1 antisense RNA 2 . . . . . . . . . . . DLGAP1-AS3 . . . DLGAP1 antisense RNA 3 . . . . . . . . . . . DLGAP1-AS4 . . . DLGAP1 antisense RNA 4 . . . . . . . . . . . DLGAP1-AS5 . . . DLGAP1 antisense RNA 5 . . . . . . . . . . . DLGAP2 0.950397325917595 0.0496014039389906 1.27014341393871e-06 discs large homolog associated protein 2 FUNCTION: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane.; . TISSUE SPECIFICITY: Expressed in brain and kidney.; unclassifiable (Anatomical System);uterus;lung;frontal lobe;larynx;testis;head and neck;kidney;brain; amygdala;medulla oblongata;superior cervical ganglion;occipital lobe;temporal lobe;caudate nucleus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.18261 0.10991 -1.609459583 3.001887238 . . DLGAP2-AS1 . . . DLGAP2 antisense RNA 1 . . . . . . . . . . . DLGAP3 0.999638515813562 0.000361483299843293 8.86595109478199e-10 discs large homolog associated protein 3 FUNCTION: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane.; . . unclassifiable (Anatomical System);medulla oblongata;lung;testis;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.34205 0.11195 -0.865195027 10.79853739 200.13226 3.05673 DLGAP4 0.991952626284089 0.00804730338411752 7.03317932226947e-08 discs large homolog associated protein 4 FUNCTION: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane.; . . medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;synovium;bone;thyroid;testis;brain;pineal gland;amygdala;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;skeletal muscle; 0.16345 0.11716 -0.723828344 14.26043878 431.55028 4.33630 DLGAP4-AS1 . . . DLGAP4 antisense RNA 1 . . . . . . . . . . . DLGAP5 1.74110377765691e-05 0.99970092500981 0.000281663952413531 discs large homolog associated protein 5 FUNCTION: Potential cell cycle regulator that may play a role in carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the ubiquitin-proteasome pathway. Key regulator of adherens junction integrity and differentiation that may be involved in CDH1-mediated adhesion and signaling in epithelial cells. {ECO:0000269|PubMed:12527899, ECO:0000269|PubMed:14699157, ECO:0000269|PubMed:15145941}.; . TISSUE SPECIFICITY: Abundantly expressed in fetal liver. Expressed at lower levels in bone marrow, testis, colon, and placenta. {ECO:0000269|PubMed:12527899}.; unclassifiable (Anatomical System);lymph node;ovary;heart;colon;blood;skin;skeletal muscle;breast;uterus;whole body;lung;endometrium;bone;placenta;visual apparatus;liver;testis;head and neck;germinal center;kidney;brain;mammary gland;stomach; superior cervical ganglion;fetal liver;tumor;atrioventricular node;skeletal muscle; 0.21009 0.08968 -0.21856543 37.66218448 4389.95882 13.22375 DLGAP5P1 . . . discs large homolog associated protein 5 pseudogene 1 . . . . . . . . . . . DLK1 0.400971249953363 0.590006829421268 0.00902192062536917 delta-like 1 homolog (Drosophila) FUNCTION: May have a role in neuroendocrine differentiation.; . TISSUE SPECIFICITY: Found within the stromal cells in close contact to the vascular structure of placental villi, yolk sac, fetal liver, adrenal cortex and pancreas and in the beta cells of the islets of Langerhans in the adult pancreas. Found also in some forms of neuroendocrine lung tumor tissue.; unclassifiable (Anatomical System);medulla oblongata;heart;ovary;islets of Langerhans;adrenal cortex;choroid;breast;lung;whole body;adrenal gland;placenta;liver;pituitary gland;spleen;head and neck;brain;peripheral nerve; fetal liver;ovary;testis - seminiferous tubule;adrenal gland;placenta;adrenal cortex;testis;fetal lung;pituitary; 0.89119 0.35587 0.554869705 81.59943383 603.54115 4.97325 DLK2 0.685774157956481 0.309925480809687 0.00430036123383221 delta-like 2 homolog (Drosophila) FUNCTION: Regulates adipogenesis. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;whole body;lung;endometrium;placenta;macula lutea;hypopharynx;head and neck;cervix;kidney;brain; prostate;superior cervical ganglion; 0.24395 0.10908 -0.157884861 42.05590941 195.83844 3.02899 DLL1 0.999053067436918 0.000946923298646302 9.26443592691992e-09 delta-like 1 (Drosophila) FUNCTION: Transmembrane ligand protein of NOTCH1, NOTCH2 and NOTCH3 receptors that binds the extracellular domain (ECD) of Notch receptor in a cis and trans fashion manner (PubMed:11006133). Following transinteraction, ligand cells produce mechanical force that depends of a clathrin-mediated endocytosis, requiring ligand ubiquitination, EPN1 interaction, and actin polymerisation; these events promote Notch receptor extracellular domain (NECD) transendocytosis and triggers Notch signaling through induction of cleavage, hyperphosphorylation, and nuclear accumulation of the intracellular domain of Notch receptors (NICD) (By similarity). Is required for embryonic development and maintenance of adult stem cells in many different tissues and immune systeme; the DLL1-induced Notch signaling is mediated through an intercellular communication that regulates cell lineage, cell specification, cell patterning and morphogenesis through effects on differentiation and proliferation (PubMed:11581320). Plays a role in brain development at different level, namely by regulating neuronal differentiation of neural precursor cells via cell-cell interaction, most likely through the lateral inhibitory system in an endogenous level dependent-manner. During neocortex development, Dll1-Notch signaling transmission is mediated by dynamic interactions between intermediate neurogenic progenitors and radial glia; the cell-cell interactions are mediated via dynamic and transient elongation processes, likely to reactivate/maintain Notch activity in neighboring progenitors, and coordinate progenitor cell division and differentiation across radial and zonal boundaries. During cerebellar development, regulates Bergmann glial monolayer formation and its morphological maturation through a Notch signaling pathway. At the retina and spinal cord level, regulates neurogenesis by preventing the premature differentiation of neural progenitors and also by maintaining progenitors in spinal cord through Notch signaling pathway. Also controls neurogenesis of the neural tube in a progenitor domain-specific fashion along the dorsoventral axis. Maintains quiescence of neural stem cells and plays a role as a fate determinant that segregates asymmetrically to one daughter cell during neural stem cells mitosis, resulting in neuronal differentiation in Dll1-inheriting cell. Plays a role in immune systeme development, namely the development of all T cells and marginal zone (MZ) B cells (By similarity). Blocks the differentiation of progenitor cells into the B-cell lineage while promoting the emergence of a population of cells with the characteristics of a T-cell/NK-cell precursor (PubMed:11581320). Also plays a role during muscle development. During early development, inhibits myoblasts differentiation from the medial dermomyotomal lip and later regulates progenitor cell differentiation. Directly modulates cell adhesion and basal lamina formation in satellite cells through Notch signaling. Maintains myogenic progenitors pool by suppressing differentiation through down-regulation of MYOD1 and is required for satellite cell homing and PAX7 expression. During craniofacial and trunk myogenesis suppresses differentiation of cranial mesoderm-derived and somite- derived muscle via MYOD1 regulation but in cranial mesoderm- derived progenitors, is neither required for satellite cell homing nor for PAX7 expression. Also plays a role during pancreatic cell development. During type B pancreatic cell development, may be involved in the initiation of proximodistal patterning in the early pancreatic epithelium. Stimulates multipotent pancreatic progenitor cells proliferation and pancreatic growth by maintaining HES1 expression and PTF1A protein levels. During fetal stages of development, is required to maintain arterial identity and the responsiveness of arterial endothelial cells for VEGFA through regulation of KDR activation and NRP1 expression. Controls sprouting angiogenesis and subsequent vertical branch formation througth regulation on tip cell differentiation. Negatively regulates goblet cell differentiation in intestine and controls secretory fat commitment through lateral inhibition in small intestine. Plays a role during inner ear development; negatively regulates auditory hair cell differentiation. Plays a role during nephron development through Notch signaling pathway. Regulates growth, blood pressure and energy homeostasis (By similarity). {ECO:0000250|UniProtKB:P97677, ECO:0000250|UniProtKB:Q61483, ECO:0000269|PubMed:11006133, ECO:0000269|PubMed:11581320}.; . TISSUE SPECIFICITY: Expressed in heart and pancreas, with lower expression in brain and muscle and almost no expression in placenta, lung, liver and kidney.; . . 0.74623 0.59852 -1.104093597 6.894314697 154.6003 2.71834 DLL3 1.65028093606891e-05 0.666246920206884 0.333736576983755 delta-like 3 (Drosophila) FUNCTION: Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity). {ECO:0000250}.; DISEASE: Spondylocostal dysostosis 1, autosomal recessive (SCDO1) [MIM:277300]: A condition of variable severity associated with vertebral and rib segmentation defects. The main skeletal malformations include fusion of vertebrae, hemivertebrae, fusion of certain ribs, and other rib malformations. Deformity of the chest and spine (severe scoliosis, kyphoscoliosis and lordosis) is a natural consequence of the malformation and leads to a dwarf- like appearance. As the thorax is small, infants frequently have respiratory insufficiency and repeated respiratory infections resulting in life-threatening complications in the first year of life. {ECO:0000269|PubMed:10742114}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;ovary;hypothalamus;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;lung;frontal lobe;placenta;macula lutea;visual apparatus;pituitary gland;cervix;brain; superior cervical ganglion;cerebellum; 0.51078 0.14012 . . 1551.90885 7.30223 DLL4 0.982859473655879 0.0171400768449608 4.49499160645531e-07 delta-like 4 (Drosophila) FUNCTION: Involved in the Notch signaling pathway as Notch ligand. Activates NOTCH1 and NOTCH4. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Essential for retinal progenitor proliferation is required for suppressing rod fates in late retinal progenitors as well as for proper generation of other retinal cell types. During spinal cord neurogenesis, inhibits V2a interneuron fate. {ECO:0000269|PubMed:17728344, ECO:0000269|PubMed:20616313}.; . TISSUE SPECIFICITY: Expressed in vascular endothelium.; unclassifiable (Anatomical System);heart;colon;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;cerebral cortex;placenta;macula lutea;testis;spleen;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.96704 0.20571 -1.353899809 4.558858221 43.0836 1.24658 DLST 0.95039365180288 0.049600071438322 6.27675879808501e-06 dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex) FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;blood;lens;breast;lung;placenta;macula lutea;liver;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; . 0.46572 -0.710864321 14.5730125 218.89249 3.19817 DLSTP1 . . . dihydrolipoamide S-succinyltransferase pseudogene 1 . . . . . . 0.45242 . . . . DLX1 0.926719407831698 0.0728748054836132 0.000405786684688472 distal-less homeobox 1 FUNCTION: Likely to play a regulatory role in the development of the ventral forebrain. May play a role in craniofacial patterning and morphogenesis and may be involved in the early development of diencephalic subdivisions (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;ovary;hypothalamus;bone;placenta;testis;parathyroid;brain;mammary gland;peripheral nerve; amygdala;whole brain;dorsal root ganglion;fetal brain;pons;cingulate cortex; 0.15127 0.20297 -0.207437529 38.2814343 2.45008 0.08952 DLX2 0.887610614037221 0.111181434585839 0.00120795137694089 distal-less homeobox 2 FUNCTION: Likely to play a regulatory role in the development of the ventral forebrain. May play a role in craniofacial patterning and morphogenesis.; . . unclassifiable (Anatomical System);pancreas;lung;duodenum;pharynx;brain;stomach; dorsal root ganglion;superior cervical ganglion;fetal brain;globus pallidus;ciliary ganglion;pons;atrioventricular node;caudate nucleus;parietal lobe;cingulate cortex;skeletal muscle; 0.89493 0.11911 -0.163345027 41.24793583 328.98155 3.85636 DLX2-AS1 . . . DLX2 antisense RNA 1 (head to head) . . . . . . . . . . . DLX3 0.0113653471173306 0.842127956348687 0.146506696533982 distal-less homeobox 3 FUNCTION: Likely to play a regulatory role in the development of the ventral forebrain. May play a role in craniofacial patterning and morphogenesis.; DISEASE: Trichodentoosseous syndrome (TDO) [MIM:190320]: An autosomal dominant disease characterized by curly kinky hair at birth, enamel hypoplasia, taurodontism, thickening of cortical bones and variable expression of craniofacial morphology. {ECO:0000269|PubMed:9467018}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Amelogenesis imperfecta 4 (AI4) [MIM:104510]: An autosomal dominant defect of enamel formation associated with enlarged pulp chambers. Enamel is thin, teeth are small and widely spaced. {ECO:0000269|PubMed:15666299}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.52412 0.21177 -0.315847836 31.68789809 44.07393 1.26496 DLX4 0.00519723009622915 0.703783582380299 0.291019187523472 distal-less homeobox 4 FUNCTION: May play a role in determining the production of hemoglobin S. May act as a repressor. {ECO:0000269|PubMed:11909945}.; . TISSUE SPECIFICITY: Expressed in leukemia cells and placenta. Also expressed in kidney and fetal liver. {ECO:0000269|PubMed:11069021, ECO:0000269|PubMed:11909945}.; unclassifiable (Anatomical System);uterus;ovary;heart;bone;placenta;liver;parathyroid;spleen;skin; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.77847 0.10751 0.349177632 74.18023119 237.42518 3.32665 DLX5 0.675979516490967 0.319299868682678 0.004720614826355 distal-less homeobox 5 FUNCTION: Transcriptional factor involved in bone development. Acts as an immediate early BMP-responsive transcriptional activator essential for osteoblast differentiation. Stimulates ALPL promoter activity in a RUNX2-independent manner during osteoblast differentiation. Stimulates SP7 promoter activity during osteoblast differentiation. Promotes cell proliferation by up-regulating MYC promoter activity. Involved as a positive regulator of both chondrogenesis and chondrocyte hypertrophy in the endochondral skeleton. Binds to the homeodomain-response element of the ALPL and SP7 promoter. Binds to the MYC promoter. Requires the 5'-TAATTA-3' consensus sequence for DNA-binding. {ECO:0000269|PubMed:19497851}.; DISEASE: Split-hand/foot malformation 1 with sensorineural hearing loss, autosomal recessive (SHFM1D) [MIM:220600]: A disease characterized by the association of split-hand/foot malformation with deafness. Split-hand/foot malformation is a limb malformation involving the central rays of the autopod and presenting with syndactyly, median clefts of the hands and feet, and aplasia and/or hypoplasia of the phalanges, metacarpals, and metatarsals. Some patients have been found to have mental retardation, ectodermal and craniofacial findings, and orofacial clefting. {ECO:0000269|PubMed:22121204}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);smooth muscle;heart;ovary;parathyroid;skin;uterus;prostate;lung;endometrium;larynx;bone;placenta;head and neck;kidney;brain;stomach; superior cervical ganglion;pons; 0.91921 0.32331 -0.249709319 35.74545883 21.7021 0.73078 DLX6 0.842830433475103 0.154279613389766 0.00288995313513163 distal-less homeobox 6 . . . unclassifiable (Anatomical System);uterus;heart;endometrium;tongue;bone;placenta;head and neck;brain; superior cervical ganglion;trigeminal ganglion; 0.64931 0.18289 -0.163345027 41.24793583 1210.09882 6.58665 DLX6-AS1 . . . DLX6 antisense RNA 1 . . . . . . . . . . . DLX6-AS2 . . . DLX6 antisense RNA 2 . . . . . . . . . . . DMAP1 0.336141633295794 0.663225658265179 0.000632708439026643 DNA methyltransferase 1 associated protein 1 FUNCTION: Involved in transcription repression and activation. Its interaction with HDAC2 may provide a mechanism for histone deacetylation in heterochromatin following replication of DNA at late firing origins. Can also repress transcription independently of histone deacetylase activity. May specifically potentiate DAXX- mediated repression of glucocorticoid receptor-dependent transcription. Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Participates in the nuclear localization of URI1 and increases its transcriptional corepressor activity. {ECO:0000269|PubMed:14665632, ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:14978102, ECO:0000269|PubMed:15367675}.; . . medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.21214 0.16306 -0.756778259 13.44656759 48.7075 1.36140 DMBT1 7.35516622313886e-32 0.326788430990087 0.673211569009913 deleted in malignant brain tumors 1 FUNCTION: May be considered as a candidate tumor suppressor gene for brain, lung, esophageal, gastric, and colorectal cancers. May play roles in mucosal defense system, cellular immune defense and epithelial differentiation. May play a role as an opsonin receptor for SFTPD and SPAR in macrophage tissues throughout the body, including epithelial cells lining the gastrointestinal tract. May play a role in liver regeneration. May be an important factor in fate decision and differentiation of transit-amplifying ductular (oval) cells within the hepatic lineage. Required for terminal differentiation of columnar epithelial cells during early embryogenesis. May function as a binding protein in saliva for the regulation of taste sensation. Binds to HIV-1 envelope protein and has been shown to both inhibit and facilitate viral transmission. Displays a broad calcium-dependent binding spectrum against both Gram-positive and Gram-negative bacteria, suggesting a role in defense against bacterial pathogens. Binds to a range of poly- sulfated and poly-phosphorylated ligands which may explain its broad bacterial-binding specificity. Inhibits cytoinvasion of S.enterica. Associates with the actin cytoskeleton and is involved in its remodeling during regulated exocytosis. Interacts with pancreatic zymogens in a pH-dependent manner and may act as a Golgi cargo receptor in the regulated secretory pathway of the pancreatic acinar cell. {ECO:0000269|PubMed:10485905, ECO:0000269|PubMed:11007786, ECO:0000269|PubMed:11751412, ECO:0000269|PubMed:16796526, ECO:0000269|PubMed:17548659, ECO:0000269|PubMed:17709527, ECO:0000269|PubMed:19189310, ECO:0000269|PubMed:9288095}.; DISEASE: Glioma (GLM) [MIM:137800]: Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes. Note=The gene represented in this entry is involved in disease pathogenesis. Homozygous deletions may be the predominant mechanism of DMBT1 inactivation playing a role in carcinogenesis. DMBT1 is deleted in medulloblastoma and glioblastoma cell lines; point mutations have also been reported in patients with glioma. A loss or reduction of DMBT1 expression has been seen in esophageal, gastric, lung and colorectal carcinomas as well.; TISSUE SPECIFICITY: Highly expressed in alveolar and macrophage tissues. In some macrophages, expression is seen on the membrane, and in other macrophages, strongly expressed in the phagosome/phagolysosome compartments. Expressed in lung, trachea, salivary gland, small intestine and stomach. In pancreas, expressed in certain cells of the islets of Langerhans. In digestive tract, confined to tissues with large epithelial surfaces. In intestinal tissue, moderately expressed in epithelial cells of the midcrypts and the crypt base. Expression is significantly elevated in intestinal tissue from patients with inflammatory bowel disease (IBD), particularly in surface epithelial and Paneth cells, but not in IBD patients with mutant NOD2. Present in crypt bases of the duodenum, in crypt tops of the colon, and in collecting ducts of the cortical kidney. Expressed in stratified squamous epithelium of vagina and in outer luminar surface and basilar region of columnar epithelial cells in cervix (at protein level). Isoform 1 is secreted to the lumen of the respiratory tract. {ECO:0000269|PubMed:10485905, ECO:0000269|PubMed:10749143, ECO:0000269|PubMed:11751412, ECO:0000269|PubMed:16796526, ECO:0000269|PubMed:17548659, ECO:0000269|PubMed:17983803, ECO:0000269|PubMed:9288095}.; unclassifiable (Anatomical System);heart;small intestine;ovary;lacrimal gland;urinary;colon;blood;skin;skeletal muscle;uterus;pancreas;prostate;lung;nasopharynx;kidney;stomach; trachea;trigeminal ganglion;skeletal muscle; 0.25445 . 4.221416241 99.71691437 3210.34948 10.79937 DMBT1P1 . . . deleted in malignant brain tumors 1 pseudogene 1 . . . . . . . . . . . DMBX1 0.915995646935682 0.0834306901094656 0.000573662954852149 diencephalon/mesencephalon homeobox 1 FUNCTION: Functions as a transcriptional repressor. May repress OTX2-mediated transactivation by forming a heterodimer with OTX2 on the P3C (5'-TAATCCGATTA-3') sequence. Required for brain development (By similarity). {ECO:0000250}.; . . . . 0.19749 0.11482 -0.246069119 36.06982779 354.48832 3.98340 DMC1 0.180759800545053 0.818719064023205 0.00052113543174153 DNA meiotic recombinase 1 FUNCTION: May participate in meiotic recombination, specifically in homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks. {ECO:0000250}.; . . lymph node; dorsal root ganglion;superior cervical ganglion;temporal lobe;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.53615 0.12378 -0.139478553 43.29440906 368.97169 4.05850 DMD 0.999999999803525 1.96474599012663e-10 2.2943472160496e-33 dystrophin FUNCTION: Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin- associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission. {ECO:0000250|UniProtKB:P11531, ECO:0000269|PubMed:16710609}.; DISEASE: Duchenne muscular dystrophy (DMD) [MIM:310200]: Most common form of muscular dystrophy; a sex-linked recessive disorder. It typically presents in boys aged 3 to 7 year as proximal muscle weakness causing waddling gait, toe-walking, lordosis, frequent falls, and difficulty in standing up and climbing up stairs. The pelvic girdle is affected first, then the shoulder girdle. Progression is steady and most patients are confined to a wheelchair by age of 10 or 12. Flexion contractures and scoliosis ultimately occur. About 50% of patients have a lower IQ than their genetic expectations would suggest. There is no treatment. {ECO:0000269|PubMed:12632325, ECO:0000269|PubMed:7981690, ECO:0000269|PubMed:8401582, ECO:0000269|PubMed:8817332, ECO:0000269|PubMed:9851445}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Becker muscular dystrophy (BMD) [MIM:300376]: A neuromuscular disorder characterized by dystrophin deficiency. It appears between the age of 5 and 15 years with a proximal motor deficiency of variable progression. Heart involvement can be the initial sign. Becker muscular dystrophy has a more benign course than Duchenne muscular dystrophy. {ECO:0000269|PubMed:10573008}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated, X-linked 3B (CMD3B) [MIM:302045]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:12354438, ECO:0000269|PubMed:12359139, ECO:0000269|PubMed:25340340, ECO:0000269|PubMed:9170407}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in muscle fibers accumulating in the costameres of myoplasm at the sarcolemma. Expressed in brain, muscle, kidney, lung and testis. Isoform 5 is expressed in heart, brain, liver, testis and hepatoma cells. Most tissues contain transcripts of multiple isoforms, however only isoform 5 is detected in heart and liver. {ECO:0000269|PubMed:1319059, ECO:0000269|PubMed:16000376, ECO:0000269|PubMed:8541829}.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;thyroid;bone;testis;germinal center;brain;artery;unclassifiable (Anatomical System);amygdala;heart;tongue;islets of Langerhans;hypothalamus;spinal cord;lens;skeletal muscle;lung;adrenal gland;nasopharynx;placenta;hippocampus;macula lutea;liver;spleen;head and neck;cervix;stomach;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;olfactory bulb;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin; 0.34010 0.76370 -0.842180844 11.28214201 7684.36218 18.86491 DMD-AS3 . . . DMD antisense RNA 3 . . . . . . . . . . . DMGDH 8.90328276029772e-17 0.0315701712524405 0.968429828747559 dimethylglycine dehydrogenase . DISEASE: DMGDH deficiency (DMGDHD) [MIM:605850]: Disorder characterized by fish odor, muscle fatigue with increased serum creatine kinase. Biochemically it is characterized by an increase of N,N-dimethylglycine (DMG) in serum and urine. {ECO:0000269|PubMed:11231903}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);liver;colon;spleen;kidney;stomach;retina; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.08977 . 0.159856957 64.91507431 4655.58952 13.74870 DMKN 3.47258381606507e-09 0.519307607519924 0.480692389007492 dermokine FUNCTION: May act as a soluble regulator of keratinocyte differentiation. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in epidermis; in the spinous and granular layers and in placenta. Also found in the epithelia of the small intestine, macrophages of the lung and endothelial cells of the lung. Isoform 15 is expressed in epidermis and placenta. Isoform 1 is expressed in epidermis. {ECO:0000269|PubMed:16374476, ECO:0000269|PubMed:17380110}.; ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;pituitary gland;testis;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland; superior cervical ganglion;tongue;skin; 0.37135 0.07165 0.446457185 77.97829677 3765.88099 12.00009 DMP1 0.000223014124025285 0.745111583096339 0.254665402779635 dentin matrix acidic phosphoprotein 1 FUNCTION: May have a dual function during osteoblast differentiation. In the nucleus of undifferentiated osteoblasts, unphosphorylated form acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the osteoblast to osteocyte transition phase it is phosphorylated and exported into the extracellular matrix, where it regulates nucleation of hydroxyapatite. {ECO:0000269|PubMed:12615915}.; DISEASE: Hypophosphatemic rickets, autosomal recessive, 1 (ARHR1) [MIM:241520]: A hereditary form of hypophosphatemic rickets, a disorder of proximal renal tubule function that causes phosphate loss, hypophosphatemia and skeletal deformities, including rickets and osteomalacia unresponsive to vitamin D. Symptoms are bone pain, fractures and growth abnormalities. {ECO:0000269|PubMed:17033621, ECO:0000269|PubMed:17033625}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in tooth particularly in odontoblast, ameloblast and cementoblast.; whole body; superior cervical ganglion;testis - seminiferous tubule;temporal lobe;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.59270 0.10850 0.512596355 80.29606039 1525.209 7.25595 DMPK 0.0330811788641306 0.965115711150776 0.0018031099850938 dystrophia myotonica protein kinase FUNCTION: Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity. {ECO:0000269|PubMed:10811636, ECO:0000269|PubMed:10913253, ECO:0000269|PubMed:11287000, ECO:0000269|PubMed:15598648, ECO:0000269|PubMed:21457715, ECO:0000269|PubMed:21949239}.; DISEASE: Dystrophia myotonica 1 (DM1) [MIM:160900]: A muscular disorder characterized by myotonia, muscle wasting in the distal extremities, cataract, hypogonadism, defective endocrine functions, male baldness and cardiac arrhythmias. {ECO:0000269|PubMed:1302022, ECO:0000269|PubMed:1310900, ECO:0000269|PubMed:1546326, ECO:0000269|PubMed:19514047}. Note=The disease is caused by mutations affecting the gene represented in this entry. The causative mutation is a CTG expansion in the 3'- UTR of the DMPK gene. A length exceeding 50 CTG repeats is pathogenic, while normal individuals have 5 to 37 repeats. Intermediate alleles with 35-49 triplets are not disease-causing but show instability in intergenerational transmissions. Disease severity varies with the number of repeats: mildly affected persons have 50 to 150 repeats, patients with classic DM have 100 to 1,000 repeats, and those with congenital onset can have more than 2,000 repeats. {ECO:0000269|PubMed:1310900, ECO:0000269|PubMed:19514047}.; TISSUE SPECIFICITY: Most isoforms are expressed in many tissues including heart, skeletal muscle, liver and brain, except for isoform 2 which is only found in the heart and skeletal muscle, and isoform 14 which is only found in the brain, with high levels in the striatum, cerebellar cortex and pons. {ECO:0000269|PubMed:7488138}.; ovary;colon;skin;retina;uterus;prostate;frontal lobe;larynx;thyroid;iris;testis;germinal center;brain;spinal ganglion;tonsil;unclassifiable (Anatomical System);muscle;lens;lung;mesenchyma;placenta;liver;head and neck;cervix;kidney;stomach; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.19672 0.28050 -0.771553417 13.15168672 1526.99605 7.25949 DMRT1 0.683592810352089 0.312015794705435 0.00439139494247575 doublesex and mab-3 related transcription factor 1 FUNCTION: Transcription factor that plays a key role in male sex determination and differentiation by controlling testis development and male germ cell proliferation. Plays a central role in spermatogonia by inhibiting meiosis in undifferentiated spermatogonia and promoting mitosis, leading to spermatogonial development and allowing abundant and continuous production of sperm. Acts both as a transcription repressor and activator: prevents meiosis by restricting retinoic acid (RA)-dependent transcription and repressing STRA8 expression and promotes spermatogonial development by activating spermatogonial differentiation genes, such as SOHLH1. Also plays a key role in postnatal sex maintenance by maintaining testis determination and preventing feminization: represses transcription of female promoting genes such as FOXL2 and activates male-specific genes. May act as a tumor suppressor. May also play a minor role in oogenesis (By similarity). {ECO:0000250}.; DISEASE: Testicular germ cell tumor (TGCT) [MIM:273300]: A common malignancy in males representing 95% of all testicular neoplasms. TGCTs have various pathologic subtypes including: unclassified intratubular germ cell neoplasia, seminoma (including cases with syncytiotrophoblastic cells), spermatocytic seminoma, embryonal carcinoma, yolk sac tumor, choriocarcinoma, and teratoma. {ECO:0000269|PubMed:20543847}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: 46,XY sex reversal 4 (SRXY4) [MIM:154230]: A condition characterized by male-to-female sex reversal in the presence of a normal 46,XY karyotype. Patients display complete or partial gonadal dysgenesis and a chromosome 9p deletion. {ECO:0000269|PubMed:21048976, ECO:0000269|PubMed:9490411, ECO:0000269|PubMed:9718346}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Testis-specific. Expressed in prostate cancer (at protein level). {ECO:0000269|PubMed:10857744, ECO:0000269|PubMed:23436708}.; . . 0.45161 . -0.424258538 25.56027365 686.09902 5.22982 DMRT2 0.46093942790113 0.533286746845832 0.00577382525303861 doublesex and mab-3 related transcription factor 2 FUNCTION: Transcriptional activator that directly regulates early activation of the myogenic determination gene MYF5 by binding in a sequence-specific manner to the early epaxial enhancer element of it. Involved in somitogenesis during embryogenesis and somite development and differentiation into sclerotome and dermomyotome. Required for the initiation and/or maintenance of proper organization of the sclerotome, dermomyotome and myotome (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis, kidney and skeletal muscle.; unclassifiable (Anatomical System);heart;colon;parathyroid;skin;skeletal muscle;uterus;lung;placenta;hypopharynx;testis;head and neck;spleen;kidney; medulla oblongata;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.28432 0.10271 . . 2506.77548 9.33199 DMRT3 0.00137345213214081 0.865389710912052 0.133236836955807 doublesex and mab-3 related transcription factor 3 FUNCTION: Probable transcription factor that plays a role in configuring the spinal circuits controlling stride in vertebrates. Involved in neuronal specification within specific subdivision of spinal cord neurons and in the development of a coordinated locomotor network controlling limb movements. May regulate transcription during sexual development (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:10729223}.; unclassifiable (Anatomical System);lung;testis;colon;parathyroid; testis - interstitial; 0.17729 0.11564 0.644875971 84.10002359 1261.05455 6.69629 DMRTA1 8.38884762019811e-05 0.535736981188543 0.464179130335255 DMRT like family A1 . . TISSUE SPECIFICITY: Expressed in liver, kidney, pancreas, prostate and weakly detected in testis and ovary. {ECO:0000269|PubMed:11863363}.; unclassifiable (Anatomical System);lung;liver;testis;kidney; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.12240 0.11899 . . 158.15062 2.74667 DMRTA2 . . . DMRT like family A2 FUNCTION: May be involved in sexual development.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:11863363}.; . . . 0.11745 . . 72.11214 1.76880 DMRTB1 0.589036510844938 0.400946827184466 0.0100166619705957 DMRT like family B with proline rich C-terminal 1 . . TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:11863363}.; . . 0.41891 0.09833 . . 1259.2225 6.69214 DMRTC1 0.43895356043987 0.457120088386407 0.103926351173723 DMRT like family C1 . . TISSUE SPECIFICITY: Predominantly expressed in kidney, pancreas, ovary and testis. Detected in brain and in many other tissues. {ECO:0000269|PubMed:11863363}.; unclassifiable (Anatomical System);optic nerve;lung;frontal lobe;macula lutea;fovea centralis;choroid;kidney;lens;brain;retina; . 0.04427 0.05294 . . 261.14093 3.46940 DMRTC1B . . . DMRT like family C1B . . TISSUE SPECIFICITY: Predominantly expressed in kidney, pancreas, ovary and testis. Detected in brain and in many other tissues. {ECO:0000269|PubMed:11863363}.; unclassifiable (Anatomical System);optic nerve;lung;frontal lobe;thyroid;macula lutea;spleen;fovea centralis;choroid;kidney;lens;brain;retina; . 0.04684 0.05294 . . . . DMRTC2 0.726527694192844 0.272884882433523 0.000587423373632305 DMRT like family C2 FUNCTION: May be involved in sexual development. {ECO:0000269|PubMed:11863363}.; . TISSUE SPECIFICITY: Expressed in testis and pancreas. {ECO:0000269|PubMed:11863363}.; unclassifiable (Anatomical System);testis; dorsal root ganglion;globus pallidus;trigeminal ganglion; . 0.08510 -0.514264485 21.41424864 37.06083 1.10740 DMTF1 0.956216302595223 0.0437836593638388 3.80409385888204e-08 cyclin D binding myb like transcription factor 1 FUNCTION: Transcriptional activator which activates the CDKN2A/ARF locus in response to Ras-Raf signaling, thereby promoting p53/TP53-dependent growth arrest (By similarity). Binds to the consensus sequence 5'-CCCG[GT]ATGT-3' (By similarity). Isoform 1 may cooperate with MYB to activate transcription of the ANPEP gene. Isoform 2 may antagonize transcriptional activation by isoform 1. {ECO:0000250, ECO:0000269|PubMed:12917399}.; . TISSUE SPECIFICITY: Expressed at relatively low levels in colonic mucosa, ovary, peripheral leukocytes, prostate and small intestine, and at higher levels in spleen, testis and thymus. Expressed in multiple regions of the brain and CNS including amygdala, caudate, corpus callosum, hippocampus, substantia nigra and subthalamic nucleus. Isoform 1 is the predominant isoform in monocytes, macrophages and neutrophils, isoform 2 is most strongly expressed in peripheral blood leukocytes and quiescent CD34 positive cells, and isoform 3 is expressed at low levels in all hematopoietic cell types. Expression is frequently reduced in non- small-cell lung carcinomas (NSCLC) due to hemizygous gene deletion, strongly suggesting that this locus is haploinsufficient for tumor suppression. Loss of this locus frequently occurs in tumors which retain wild-type CDKN2A/ARF and p53/TP53 loci. Hemizygous gene deletion has also been observed in leukemic blasts from patients with abnormalities of the long arm of chromosome 7. {ECO:0000269|PubMed:10095122, ECO:0000269|PubMed:12917399, ECO:0000269|PubMed:17936562}.; ovary;developmental;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;muscle;urinary;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;medulla oblongata;prefrontal cortex;globus pallidus;atrioventricular node;pons;trigeminal ganglion;cingulate cortex; 0.56131 0.12154 -0.111973265 45.35857514 283.65163 3.60477 DMTN 0.961762589977884 0.0382341366445303 3.27337758520153e-06 dematin actin binding protein FUNCTION: Membrane-cytoskeleton-associated protein with F-actin- binding activity that induces F-actin bundles formation and stabilization. Its F-actin-bundling activity is reversibly regulated upon its phosphorylation by the cAMP-dependent protein kinase A (PKA). Binds to the erythrocyte membrane glucose transporter-1 SLC2A1/GLUT1, and hence stabilizes and attaches the spectrin-actin network to the erythrocytic plasma membrane. Plays a role in maintaining the functional integrity of PKA-activated erythrocyte shape and the membrane mechanical properties. Plays also a role as a modulator of actin dynamics in fibroblasts; acts as a negative regulator of the RhoA activation pathway. In platelets, functions as a regulator of internal calcium mobilization across the dense tubular system that affects platelet granule secretion pathways and aggregation. Also required for the formation of a diverse set of cell protrusions, such as filopodia and lamellipodia, necessary for platelet cell spreading, motility and migration. Acts as a tumor suppressor and inhibits malignant cell transformation. {ECO:0000269|PubMed:10565303, ECO:0000269|PubMed:11856323, ECO:0000269|PubMed:18347014, ECO:0000269|PubMed:19241372, ECO:0000269|PubMed:22927433, ECO:0000269|PubMed:23355471}.; . TISSUE SPECIFICITY: Expressed in platelets (at protein level). Expressed in heart, brain, lung, skeletal muscle, and kidney. {ECO:0000269|PubMed:23060452}.; . . 0.14304 0.24243 -0.358119787 29.16371786 209.65906 3.12551 DMWD 0.00790211300454926 0.928697400346482 0.0634004866489689 dystrophia myotonica, WD repeat containing FUNCTION: Could have a regulatory function in meiosis. {ECO:0000269|PubMed:8499920}.; . . unclassifiable (Anatomical System);heart;pineal body;colon;fovea centralis;choroid;lens;skin;retina;pancreas;prostate;optic nerve;lung;placenta;bone;macula lutea;visual apparatus;cervix;kidney;brain;tonsil;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.39365 0.17550 -0.558357437 19.54470394 54.93113 1.48497 DMXL1 0.999998843167901 1.15683209865886e-06 3.49660717260196e-24 Dmx like 1 . . TISSUE SPECIFICITY: Expressed in bone, breast, eye, foreskin, heart, parathyroid, small intestine, testis, tonsils, placenta and uterus. {ECO:0000269|PubMed:10708522}.; sympathetic chain;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;heart;urinary;adrenal cortex;blood;skeletal muscle;pancreas;lung;adrenal gland;placenta;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; amygdala;medulla oblongata;prostate;hypothalamus;thyroid;spinal cord;prefrontal cortex;caudate nucleus; 0.71329 0.11984 -0.820119436 11.8895966 2325.86474 8.93384 DMXL2 0.999999999395933 6.04067034890624e-10 8.64215442828467e-31 Dmx like 2 FUNCTION: May serve as a scaffold protein for MADD and RAB3GA on synaptic vesicles (PubMed:11809763). Plays a role in the brain as a key controller of neuronal and endocrine homeostatic processes (By similarity). {ECO:0000250|UniProtKB:Q8BPN8, ECO:0000269|PubMed:11809763}.; DISEASE: Polyendocrine-polyneuropathy syndrome (PEPNS) [MIM:616113]: A progressive endocrine and neurodevelopmental disorder manifesting early in childhood with growth retardation and recurrent episodes of profound asymptomatic hypoglycemia. PEPNS is characterized by central hypothyroidism, hypogonadotropic hypogonadism, incomplete puberty, progressive non-autoimmune insulin-dependent diabetes mellitus, peripheral demyelinating sensorimotor polyneuropathy, and cerebellar and pyramidal signs. {ECO:0000269|PubMed:25248098}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;bone marrow;breast;uterus;prostate;lung;frontal lobe;endometrium;larynx;placenta;pituitary gland;liver;testis;head and neck;germinal center;kidney;brain;aorta;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.29917 0.10305 -1.876572788 1.999292286 2585.78027 9.51277 DNA2 1.94885128663318e-08 0.991999565481716 0.00800041502977097 DNA replication helicase/nuclease 2 FUNCTION: Key enzyme involved in DNA replication and DNA repair in nucleus and mitochondrion. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double- strand break (DSB) repair: recruited by BLM and mediates the cleavage of 5'-ssDNA, while the 3'-ssDNA cleavage is prevented by the presence of RPA. Also involved in DNA replication checkpoint independently of Okazaki fragments processing. Possesses different enzymatic activities, such as single-stranded DNA (ssDNA)- dependent ATPase, 5'-3' helicase and endonuclease activities. While the ATPase and endonuclease activities are well-defined and play a key role in Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase activity is subject to debate. According to various reports, the helicase activity is weak and its function remains largely unclear. Helicase activity may promote the motion of DNA2 on the flap, helping the nuclease function. {ECO:0000269|PubMed:16595799, ECO:0000269|PubMed:16595800, ECO:0000269|PubMed:18995831, ECO:0000269|PubMed:19487465, ECO:0000269|PubMed:21325134, ECO:0000269|PubMed:21572043, ECO:0000269|PubMed:22570407, ECO:0000269|PubMed:22570476}.; DISEASE: Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal dominant, 6 (PEOA6) [MIM:615156]: A disorder characterized by muscle weakness, mainly affecting the lower limbs, external ophthalmoplegia, exercise intolerance, and mitochondrial DNA deletions on muscle biopsy. Symptoms may appear in childhood or adulthood and show slow progression. {ECO:0000269|PubMed:23352259}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Seckel syndrome 8 (SCKL8) [MIM:615807]: A rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and mental retardation. {ECO:0000269|PubMed:24389050}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);urinary;colon;blood;skin;breast;prostate;lung;larynx;thyroid;placenta;testis;head and neck;germinal center;bladder;stomach;thymus; trigeminal ganglion;skeletal muscle; 0.62197 . . . 1134.53366 6.42769 DNAAF1 5.41468353704791e-06 0.966130360612423 0.0338642247040402 dynein (axonemal) assembly factor 1 FUNCTION: Cilium-specific protein required for the stability of the ciliary architecture. Plays a role in cytoplasmic preassembly of dynein arms. Involved in regulation of microtubule-based cilia and actin-based brush border microvilli. {ECO:0000269|PubMed:18385425, ECO:0000269|PubMed:19944400, ECO:0000269|PubMed:19944405}.; . TISSUE SPECIFICITY: Mainly expressed in trachea and testis. {ECO:0000269|PubMed:19944405}.; unclassifiable (Anatomical System);medulla oblongata;lymph node;cartilage;ovary;islets of Langerhans;colon;blood;retina;uterus;prostate;whole body;lung;frontal lobe;endometrium;bone;visual apparatus;liver;testis;spleen;kidney;brain;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;hypothalamus;testis;fetal lung;trigeminal ganglion;skeletal muscle; 0.06057 0.06574 2.745190925 98.97381458 2743.80748 9.87481 DNAAF2 4.78818341115889e-06 0.406825399506219 0.59316981231037 dynein (axonemal) assembly factor 2 FUNCTION: Required for cytoplasmic pre-assembly of axonemal dyneins, thereby playing a central role in motility in cilia and flagella. Involved in pre-assembly of dynein arm complexes in the cytoplasm before intraflagellar transport loads them for the ciliary compartment.; DISEASE: Ciliary dyskinesia, primary, 10 (CILD10) [MIM:612518]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:19052621, ECO:0000269|PubMed:25186273}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;testis;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;hypothalamus;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;aorta; testis - interstitial;temporal lobe; 0.42666 . . . 5058.3547 14.56268 DNAAF3 3.21577634646308e-06 0.934084409327109 0.0659123748965449 dynein (axonemal) assembly factor 3 FUNCTION: Required for the assembly of axonemal inner and outer dynein arms. Involved in preassembly of dyneins into complexes before their transport into cilia. {ECO:0000269|PubMed:22387996}.; DISEASE: Ciliary dyskinesia, primary, 2 (CILD2) [MIM:606763]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:22387996}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.11936 . 0.665103516 84.6131163 2734.55934 9.85329 DNAAF5 . . . dynein (axonemal) assembly factor 5 FUNCTION: Cytoplasmic protein involved in the delivery of the dynein machinery to the motile cilium. It is required for the assembly of the axonemal dynein inner and outer arms, two structures attached to the peripheral outer doublet A microtubule of the axoneme, that play a crucial role in cilium motility. {ECO:0000269|PubMed:23040496, ECO:0000269|PubMed:25232951}.; DISEASE: Ciliary dyskinesia, primary, 18 (CILD18) [MIM:614874]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:23040496, ECO:0000269|PubMed:25232951}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in nasal epithelium and lung epithelium by ciliated cells (at protein level). {ECO:0000269|PubMed:23040496}.; . . 0.15548 0.10096 -0.569494998 19.04340646 . . DNAH1 4.42227332517076e-20 0.999999999998172 1.82836286627503e-12 dynein axonemal heavy chain 1 FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed primarily in trachea and testis, 2 tissues containing axonemal structures. Also expressed in brain. {ECO:0000269|PubMed:11175280, ECO:0000269|PubMed:9256245}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;blood;skin;breast;bile duct;prostate;pancreas;optic nerve;whole body;lung;frontal lobe;thyroid;placenta;liver;testis;germinal center;kidney;brain;bladder;stomach; superior cervical ganglion;occipital lobe;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10314 0.12173 -0.361375728 28.63882991 4201.19407 12.89158 DNAH2 2.48851849978906e-21 1 2.65111723481861e-18 dynein axonemal heavy chain 2 FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed primarily in trachea and testis, 2 tissues containing axonemal structures. Also expressed in lung. {ECO:0000269|PubMed:9256245}.; ovary;salivary gland;pharynx;colon;blood;breast;prostate;lung;endometrium;larynx;placenta;visual apparatus;liver;testis;head and neck;kidney;brain;bladder; superior cervical ganglion;uterus corpus;testis;appendix;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10385 0.09775 -2.390798793 1.085161595 6709.34711 17.36230 DNAH3 9.63057947571572e-51 0.0137199585080936 0.986280041491906 dynein axonemal heavy chain 3 FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed primarily in trachea and testis, 2 tissues containing axonemal structures. Also expressed in lung. {ECO:0000269|PubMed:9256245}.; unclassifiable (Anatomical System);pancreas;lung;ovary;testis;blood; dorsal root ganglion;testis - interstitial;superior cervical ganglion;tongue;adrenal cortex;atrioventricular node;pons;skeletal muscle;skin;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.19721 0.12485 -1.472892299 3.733191791 9793.07417 21.54604 DNAH5 5.78867795702671e-37 0.999999999801309 1.98691071889824e-10 dynein axonemal heavy chain 5 FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required for structural and functional integrity of the cilia of ependymal cells lining the brain ventricles.; DISEASE: Ciliary dyskinesia, primary, 3 (CILD3) [MIM:608644]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:11062149, ECO:0000269|PubMed:16627867, ECO:0000269|PubMed:25186273}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Kartagener syndrome (KTGS) [MIM:244400]: An autosomal recessive disorder characterized by the association of primary ciliary dyskinesia with situs inversus. Clinical features include recurrent respiratory infections, bronchiectasis, infertility, and lateral transposition of the viscera of the thorax and abdomen. The situs inversus is most often total, although it can be partial in some cases (isolated dextrocardia or isolated transposition of abdominal viscera). {ECO:0000269|PubMed:11788826}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);endometrium;islets of Langerhans;bone;amnion;blood;kidney;mammary gland;corpus callosum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.10168 . -0.181093951 40.16277424 17941.81819 28.59961 DNAH6 0.000223494727431832 0.915044779219374 0.0847317260531943 dynein axonemal heavy chain 6 FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in brain, testis and trachea. {ECO:0000269|PubMed:11175280}.; uterus;meninges;pia mater;lung;endometrium;bone;pituitary gland;dura mater;skin; superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node;caudate nucleus;trigeminal ganglion;parietal lobe; 0.38274 0.10174 2.022922571 97.71762208 2649.61757 9.66425 DNAH7 1.0373966005542e-47 0.815068071870201 0.184931928129799 dynein axonemal heavy chain 7 FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in brain, testis and trachea. Detected in bronchial cells (at protein level). {ECO:0000269|PubMed:11175280, ECO:0000269|PubMed:11877439}.; unclassifiable (Anatomical System);lung;ovary;endometrium;thyroid;placenta;pituitary gland;testis;kidney;germinal center;brain;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.23862 0.10363 5.09315636 99.81717386 6415.17778 16.77483 DNAH8 2.09466493164173e-37 0.999999999144842 8.55157874037014e-10 dynein axonemal heavy chain 8 FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). {ECO:0000250}.; . . prostate;lung;hypothalamus;testis;germinal center; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.33816 0.09678 . . 14314.45201 26.19227 DNAH9 1.36586328854305e-35 0.999999244383913 7.55616087445322e-07 dynein axonemal heavy chain 9 FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.; . . unclassifiable (Anatomical System);uterus;lung;heart;hypothalamus;placenta;testis;brain;skin; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.20972 0.11901 0.45554211 78.06086341 11534.8129 23.18197 DNAH10 4.14031534574386e-37 0.999995316132189 4.6838678109361e-06 dynein axonemal heavy chain 10 FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). Probable inner arm dynein heavy chain. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed primarily in trachea and testis, 2 tissues containing axonemal structures. Also expressed in brain but not in adult heart.; . . 0.13173 . 1.325829575 94.09648502 4889.92858 14.22093 DNAH10OS 0.0133663892213768 0.431255198069895 0.555378412708728 dynein axonemal heavy chain 10 opposite strand . . . . . . . . . 458.23563 4.44493 DNAH11 . . . dynein axonemal heavy chain 11 FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.; DISEASE: Kartagener syndrome (KTGS) [MIM:244400]: An autosomal recessive disorder characterized by the association of primary ciliary dyskinesia with situs inversus. Clinical features include recurrent respiratory infections, bronchiectasis, infertility, and lateral transposition of the viscera of the thorax and abdomen. The situs inversus is most often total, although it can be partial in some cases (isolated dextrocardia or isolated transposition of abdominal viscera). {ECO:0000269|PubMed:12142464, ECO:0000269|PubMed:18022865, ECO:0000269|PubMed:25186273}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ciliary dyskinesia, primary, 7 (CILD7) [MIM:611884]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:12142464, ECO:0000269|PubMed:18022865}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;vein;skin;uterus;prostate;cochlea;endometrium;gum;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.12513 0.12171 . . 20704.35568 30.36052 DNAH12 0.000394165957730919 0.957685660024892 0.0419201740173774 dynein axonemal heavy chain 12 FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);pancreas;lung;nasopharynx;testis; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.40937 0.09978 0.841481379 88.35810333 7404.50475 18.48845 DNAH14 8.77000190556253e-06 0.3191763133612 0.680814916636895 dynein axonemal heavy chain 14 FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;testis;colon;brain;skeletal muscle; dorsal root ganglion;testis - interstitial;superior cervical ganglion;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.32231 0.10036 1.394519284 94.6685539 7454.49367 18.56756 DNAH17 . . . dynein axonemal heavy chain 17 FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:9545504}.; . . 0.10041 . . . 8793.71322 20.21811 DNAH17-AS1 0.446203082126616 0.453977726787194 0.0998191910861907 DNAH17 antisense RNA 1 . . . . . . . . . 10615.75068 22.42106 DNAI1 0.0001273439173132 0.997928177528922 0.00194447855376425 dynein axonemal intermediate chain 1 FUNCTION: Part of the dynein complex of respiratory cilia.; DISEASE: Ciliary dyskinesia, primary, 1 (CILD1) [MIM:244400]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:25186273}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Kartagener syndrome (KTGS) [MIM:244400]: An autosomal recessive disorder characterized by the association of primary ciliary dyskinesia with situs inversus. Clinical features include recurrent respiratory infections, bronchiectasis, infertility, and lateral transposition of the viscera of the thorax and abdomen. The situs inversus is most often total, although it can be partial in some cases (isolated dextrocardia or isolated transposition of abdominal viscera). {ECO:0000269|PubMed:11231901}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);medulla oblongata;optic nerve;lung;endometrium;islets of Langerhans;nasopharynx;macula lutea;testis;fovea centralis;choroid;lens;retina; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.31394 0.15171 -0.306750577 32.23047889 2255.22848 8.77187 DNAI2 4.56806643361888e-11 0.331271928954035 0.668728071000285 dynein axonemal intermediate chain 2 FUNCTION: Part of the dynein complex of respiratory cilia.; . TISSUE SPECIFICITY: Highly expressed in trachea and testis.; medulla oblongata;lung;endometrium;testis;spleen; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.12601 0.10505 0.007353605 54.12243454 4492.04811 13.45364 DNAJA1 0.260111368523282 0.738699814938131 0.00118881653858638 DnaJ heat shock protein family (Hsp40) member A1 FUNCTION: Co-chaperone for HSPA8/Hsc70 (PubMed:10816573). Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (PubMed:24318877). Plays a role in protein transport into mitochondria via its role as co- chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis (PubMed:14752510). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (PubMed:24512202). {ECO:0000269|PubMed:10816573, ECO:0000269|PubMed:14752510, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24512202, ECO:0000269|PubMed:9192730}.; . TISSUE SPECIFICITY: Ubiquitous. Isoform 2 is highly expressed in testis and lung, but detected at low levels in thymus, prostate, colon and liver. {ECO:0000269|PubMed:10816573, ECO:0000269|PubMed:15595953}.; . . 0.49896 0.36254 -0.560178693 19.30879925 6.16298 0.23238 DNAJA1P1 . . . DnaJ heat shock protein family (Hsp40) member A1 pseudogene 1 . . . . . . . . . . . DNAJA1P2 . . . DnaJ heat shock protein family (Hsp40) member A1 pseudogene 2 . . . . . . . . . . . DNAJA1P3 . . . DnaJ heat shock protein family (Hsp40) member A1 pseudogene 3 . . . . . . . . . . . DNAJA1P4 . . . DnaJ heat shock protein family (Hsp40) member A1 pseudogene 4 . . . . . . . . . . . DNAJA1P5 . . . DnaJ heat shock protein family (Hsp40) member A1 pseudogene 5 . . . . . . . . . . . DNAJA1P6 . . . DnaJ heat shock protein family (Hsp40) member A1 pseudogene 6 . . . . . . . . . . . DNAJA2 0.985455360988873 0.0145431558566137 1.48315451346589e-06 DnaJ heat shock protein family (Hsp40) member A2 FUNCTION: Co-chaperone of Hsc70.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;hypothalamus;pineal body;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach;thymus; amygdala;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;cingulate cortex;skeletal muscle;parietal lobe; 0.44030 0.42262 -0.317668748 31.45789101 11.9428 0.43302 DNAJA3 0.3856771260961 0.613892630436674 0.000430243467226495 DnaJ heat shock protein family (Hsp40) member A3 FUNCTION: Modulates apoptotic signal transduction or effector structures within the mitochondrial matrix. Affect cytochrome C release from the mitochondria and caspase 3 activation, but not caspase 8 activation. Isoform 1 increases apoptosis triggered by both TNF and the DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses apoptosis. Can modulate IFN-gamma- mediated transcriptional activity. Isoform 2 may play a role in neuromuscular junction development as an effector of the MUSK signaling pathway.; . TISSUE SPECIFICITY: Widely expressed with highest levels in heart, liver, lung and skeletal muscles. Also expressed in keratinocytes. {ECO:0000269|PubMed:9683573}.; ovary;salivary gland;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;adrenal gland;liver;testis;kidney;cerebellum; 0.55527 . -0.644723694 16.52512385 78.73451 1.87281 DNAJA4 3.56777071333241e-05 0.818075428236024 0.181888894056843 DnaJ heat shock protein family (Hsp40) member A4 . . . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;pons;skeletal muscle; 0.16281 0.13378 0.64123826 83.97617363 128.72728 2.47255 DNAJB1 0.372156950000017 0.616660454826792 0.0111825951731902 DnaJ heat shock protein family (Hsp40) member B1 FUNCTION: Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP.; . . ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;kidney;stomach;aorta;thymus; testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node; 0.58197 0.56967 -1.06726444 7.372021703 26.58877 0.86093 DNAJB1P1 . . . DnaJ heat shock protein family (Hsp40) member B1 pseudogene 1 . . . . . . . . . . . DNAJB2 5.19696073671681e-06 0.657023107413548 0.342971695625715 DnaJ heat shock protein family (Hsp40) member B2 . DISEASE: Charcot-Marie-Tooth disease 2T (CMT2T) [MIM:616233]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. {ECO:0000269|PubMed:24627108, ECO:0000269|PubMed:25274842}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Brain (neuronal layers). Weakly, in skeletal muscle and spleen.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; whole brain;amygdala;hypothalamus;spinal cord;prefrontal cortex;parietal lobe; 0.17121 0.08355 -0.137658575 43.57159707 126.33722 2.44829 DNAJB3 . . . DnaJ heat shock protein family (Hsp40) member B3 FUNCTION: May operate as a co-chaperone of the male germ cell- and haploid stage-specific Hsp70 proteins. {ECO:0000305}.; . . . . . . . . . . DNAJB4 0.840407621121713 0.15896084272727 0.000631536151016861 DnaJ heat shock protein family (Hsp40) member B4 FUNCTION: Probable chaperone.; . TISSUE SPECIFICITY: Expressed in heart, pancreas and skeletal muscle, and to a lesser extent in brain, placenta and liver. {ECO:0000269|PubMed:9546042}.; . . 0.62010 . -0.317668748 31.45789101 11.79709 0.42763 DNAJB5 0.491267707346988 0.504137508930085 0.00459478372292749 DnaJ heat shock protein family (Hsp40) member B5 . . . myocardium;ovary;colon;parathyroid;choroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;bone;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;skeletal muscle;bile duct;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; uterus corpus;superior cervical ganglion;heart;cerebellum peduncles;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.75765 0.12918 -0.427900189 25.14744043 48.2466 1.35321 DNAJB5-AS1 . . . DNAJB5 antisense RNA 1 (head to head) . . . . . . . . . . . DNAJB5P1 . . . DnaJ heat shock protein family (Hsp40) member B5 pseudogene 1 . . . . . . . . . . . DNAJB6 0.963595740652646 0.0363899565582552 1.43027890983652e-05 DnaJ heat shock protein family (Hsp40) member B6 FUNCTION: Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Isoform B but not isoform A inhibits huntingtin aggregation. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity. {ECO:0000269|PubMed:10954706, ECO:0000269|PubMed:11896048, ECO:0000269|PubMed:20159555, ECO:0000269|PubMed:22366786}.; DISEASE: Limb-girdle muscular dystrophy 1E (LGMD1E) [MIM:603511]: An autosomal dominant myopathy characterized by adult onset of proximal muscle weakness, beginning in the hip girdle region and later progressing to the shoulder girdle region. {ECO:0000269|PubMed:22334415, ECO:0000269|PubMed:22366786}. Note=The disease is caused by mutations affecting the gene represented in this entry. There is evidence that LGMD1E is caused by dysfunction of isoform B (PubMed:22366786). {ECO:0000269|PubMed:22366786}.; TISSUE SPECIFICITY: Widely expressed. Highest levels in testis and brain, and lower levels in heart, spleen, intestine, ovary, placenta, lung, kidney, pancreas, thymus, prostate, skeletal muscle, liver and leukocytes. In testis, expressed in germ cells in the earlier stages of differentiation pathway as well as in spermatids. In brain, expressed at a higher level in hippocampus and thalamus and a lower level in amygdala, substantia nigra, corpus callosum and caudate nucleus. {ECO:0000269|PubMed:10319584, ECO:0000269|PubMed:11896048, ECO:0000269|PubMed:22366786, ECO:0000269|PubMed:9915854}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;bone;thyroid;pituitary gland;testis;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; amygdala;thalamus;testis - interstitial;testis;pons;trigeminal ganglion;cingulate cortex;skeletal muscle;parietal lobe; 0.34214 0.21906 -0.139478553 43.29440906 27.41429 0.88400 DNAJB7 2.09351234250952e-11 0.0024980808794855 0.997501919099579 DnaJ heat shock protein family (Hsp40) member B7 FUNCTION: Probably acts as a co-chaperone. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;visual apparatus;iris;pituitary gland;testis;mammary gland; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;appendix;testis;ciliary ganglion;pons; 0.12629 0.17682 0.685332364 85.09672092 482.69457 4.52412 DNAJB8 0.0475406871720836 0.680058130216826 0.27240118261109 DnaJ heat shock protein family (Hsp40) member B8 FUNCTION: Efficient suppressor of aggregation and toxicity of disease-associated polyglutamine proteins. {ECO:0000269|PubMed:20159555}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion; 0.12855 0.11010 -0.380166007 27.88393489 66.41036 1.67832 DNAJB8-AS1 . . . DNAJB8 antisense RNA 1 . . . . . . . . . . . DNAJB9 0.224582946037773 0.739473542412384 0.0359435115498421 DnaJ heat shock protein family (Hsp40) member B9 FUNCTION: Involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Acts as a co-chaperone with an Hsp70 protein. {ECO:0000269|PubMed:18400946}.; . . myocardium;umbilical cord;ovary;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;duodenum;liver;cervix;kidney;stomach;aorta; superior cervical ganglion;placenta;trigeminal ganglion;pituitary; 0.08805 0.09981 0.193034296 66.82000472 221.86399 3.22002 DNAJB11 0.909930974034799 0.0900404739509765 2.85520142246885e-05 DnaJ heat shock protein family (Hsp40) member B11 FUNCTION: Serves as a co-chaperone for HSPA5. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. {ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:15525676}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:11584023, ECO:0000269|PubMed:15525676}.; lymphoreticular;smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta;cerebellum;thymus; . 0.38216 . -0.05129383 49.75819769 2096.197 8.43237 DNAJB12 0.0399386738756349 0.95346034245418 0.00660098367018487 DnaJ heat shock protein family (Hsp40) member B12 . . . myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;amygdala;testis - interstitial;superior cervical ganglion;subthalamic nucleus;medulla oblongata;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.30963 0.12793 -0.111973265 45.35857514 123.27828 2.41796 DNAJB13 0.121954826569755 0.872750328214636 0.00529484521560875 DnaJ heat shock protein family (Hsp40) member B13 FUNCTION: May be involved in inhibiting testis spermatogenesis apoptosis.; . TISSUE SPECIFICITY: Specifically expressed in testis.; prostate;lung;cartilage;ovary;endometrium;placenta;urinary;liver;testis;parathyroid; superior cervical ganglion;testis - seminiferous tubule;atrioventricular node;cerebellum; 0.13751 0.13274 0.396906589 76.30927105 2202.42808 8.64001 DNAJB14 0.956254969811075 0.0437404497451248 4.58044380030472e-06 DnaJ heat shock protein family (Hsp40) member B14 FUNCTION: Acts as a co-chaperone with HSPA8 and promotes the degradation of misfolded transmembrane proteins in the ER- associated degradation (ERAD) pathway. {ECO:0000269|PubMed:23018488}.; . . unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;pineal body;colon;fovea centralis;lens;skin;skeletal muscle;uterus;prostate;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;testis;head and neck;spleen;germinal center;kidney;brain;stomach;thymus; prefrontal cortex; 0.20812 0.10778 -0.293801652 32.93819297 305.48604 3.72246 DNAJC1 1.42208526512983e-08 0.811595355552354 0.188404630226793 DnaJ heat shock protein family (Hsp40) member C1 FUNCTION: May modulate protein synthesis. {ECO:0000250}.; . . . . 0.12424 0.09575 -0.558357437 19.54470394 54.54446 1.47779 DNAJC2 0.984694417551266 0.0153055685173253 1.39314088129071e-08 DnaJ heat shock protein family (Hsp40) member C2 FUNCTION: Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb- repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3'. {ECO:0000269|PubMed:15802566, ECO:0000269|PubMed:16002468, ECO:0000269|PubMed:21179169}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11034098}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;breast;bile duct;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; testis - interstitial;testis - seminiferous tubule;tumor;testis;white blood cells; 0.61343 0.11838 -0.071520315 48.34866714 96.05754 2.11818 DNAJC3 0.951080561997675 0.0489182113184231 1.22668390174675e-06 DnaJ heat shock protein family (Hsp40) member C3 FUNCTION: Involved in the unfolded protein response (UPR) during endoplasmic reticulum (ER) stress. Acts as a negative regulator of the EIF2AK4/GCN2 kinase activity by preventing the phosphorylation of eIF-2-alpha at 'Ser-52' and hence attenuating general protein synthesis under ER stress, hypothermic and amino acid starving stress conditions (By similarity). Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activity. {ECO:0000250|UniProtKB:Q27968, ECO:0000250|UniProtKB:Q91YW3, ECO:0000269|PubMed:12601012, ECO:0000269|PubMed:8576172, ECO:0000269|PubMed:9447982, ECO:0000269|PubMed:9920933}.; DISEASE: Ataxia, combined cerebellar and peripheral, with hearing loss and diabetes mellitus (ACPHD) [MIM:616192]: A disease characterized by juvenile-onset diabetes and neurodegeneration, resulting in ataxia, upper-motor-neuron damage, peripheral neuropathy, hearing loss, and cerebral atrophy. {ECO:0000269|PubMed:25466870}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed with high level in the pancreas and testis. Also expressed in cell lines with different levels. {ECO:0000269|PubMed:8666242}.; . . 0.17383 0.15780 -0.47017169 23.25430526 89.70123 2.03720 DNAJC3-AS1 . . . DNAJC3 antisense RNA 1 (head to head) . . . . . . . . . . . DNAJC4 6.43771101373159e-06 0.464473143795735 0.535520418493251 DnaJ heat shock protein family (Hsp40) member C4 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;lung;placenta;visual apparatus;hippocampus;macula lutea;head and neck;kidney;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;testis; 0.07428 0.07645 0.060756528 58.52795471 36.66268 1.09995 DNAJC5 0.858492458762531 0.139312428651262 0.00219511258620651 DnaJ heat shock protein family (Hsp40) member C5 FUNCTION: May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity). {ECO:0000250}.; DISEASE: Ceroid lipofuscinosis, neuronal, 4B (CLN4B) [MIM:162350]: An adult-onset neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. CLN4B has no visual involvement and is characterized by seizures and other neurologic symptoms. {ECO:0000269|PubMed:21820099, ECO:0000269|PubMed:22073189, ECO:0000269|PubMed:22235333, ECO:0000269|PubMed:22978711}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in pancreas, kidney, skeletal muscle, liver, lung, placenta, brain and heart. {ECO:0000269|PubMed:8764987}.; ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;thyroid;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;blood;lens;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;mammary gland;stomach;cerebellum; whole brain;subthalamic nucleus;occipital lobe;cerebellum peduncles;globus pallidus;pons;atrioventricular node;parietal lobe;cingulate cortex;skeletal muscle;cerebellum; 0.17855 0.11262 -0.339715008 30.06605331 3.7021 0.13784 DNAJC5B 0.0096775847127486 0.818260190514274 0.172062224772978 DnaJ heat shock protein family (Hsp40) member C5 beta . . TISSUE SPECIFICITY: Testis specific.; unclassifiable (Anatomical System);breast;medulla oblongata;lung;placenta;hippocampus;testis;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.14279 0.10409 0.082802743 60.09082331 81.44212 1.91057 DNAJC5G 0.00397478941010456 0.647248072340885 0.348777138249011 DnaJ heat shock protein family (Hsp40) member C5 gamma . . TISSUE SPECIFICITY: Testis specific.; medulla oblongata;testis; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;skeletal muscle; 0.03631 0.06726 0.349177632 74.18023119 266.1821 3.49962 DNAJC6 0.99918835079312 0.000811649154164987 5.27155036536954e-11 DnaJ heat shock protein family (Hsp40) member C6 FUNCTION: Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles. Plays a role in clathrin-mediated endocytosis in neurons (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in various brain regions, including cerebellum, corpus callosum, cortex, striatum, brainstem, pons, putamen, spinal cord and substantia nigra. Very low expression in non-neural tissues such as leukocytes, liver, adipose tissue, skeletal muscle and bone marrow. {ECO:0000269|PubMed:23211418}.; sympathetic chain;colon;skin;bone marrow;retina;uterus;subthalamic nucleus;whole body;frontal lobe;ganglion;pituitary gland;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;hypothalamus;spinal cord;skeletal muscle;placenta;visual apparatus;liver;spleen;mammary gland;cerebellum; whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.58486 0.12050 -0.659500046 16.07100731 161.88436 2.77982 DNAJC7 0.999727953382784 0.000272046173630329 4.43585300447261e-10 DnaJ heat shock protein family (Hsp40) member C7 FUNCTION: Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone- substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity). {ECO:0000250, ECO:0000269|PubMed:12853476, ECO:0000269|PubMed:18620420}.; . . myocardium;lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; medulla oblongata;pons;caudate nucleus;parietal lobe; 0.46633 0.24415 -0.427900189 25.14744043 24.74494 0.81220 DNAJC8 0.582006641588927 0.417532813098522 0.000460545312551521 DnaJ heat shock protein family (Hsp40) member C8 . . . myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;synovium;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach;thymus; . 0.11419 0.11616 -0.053113545 49.38664779 1242.65868 6.65601 DNAJC8P1 . . . DnaJ heat shock protein family (Hsp40) member C8 pseudogene 1 . . . . . . . . . . . DNAJC9 0.547006457229025 0.450007532473748 0.00298601029722716 DnaJ heat shock protein family (Hsp40) member C9 FUNCTION: May play a role as co-chaperone of the Hsp70 family proteins HSPA1A, HSPA1B and HSPA8. {ECO:0000269|PubMed:17182002}.; . TISSUE SPECIFICITY: Expressed in heart, placenta, liver, skeletal muscle, kidney, pancreas, thymus, ovary, colon and peripheral blood. {ECO:0000269|PubMed:17182002}.; . . 0.11690 0.12515 0.281220278 71.07808445 57.66511 1.53433 DNAJC9-AS1 . . . DNAJC9 antisense RNA 1 . . . . . 0.11113 . . . . . DNAJC10 8.94919335579899e-05 0.999883647893308 2.6860173133964e-05 DnaJ heat shock protein family (Hsp40) member C10 FUNCTION: Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, but to facilitate the release of DNAJC10 from its substrate. Promotes apoptotic signaling pathway in response to endoplasmic reticulum stress. {ECO:0000269|PubMed:12411443, ECO:0000269|PubMed:18400946, ECO:0000269|PubMed:19122239, ECO:0000269|PubMed:23769672}.; . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;liver;kidney;mammary gland;stomach; testis - interstitial;smooth muscle;testis - seminiferous tubule;testis;white blood cells; 0.53896 0.12506 0.711016566 85.72776598 5535.22519 15.37741 DNAJC11 0.999970790294974 2.92097030932467e-05 1.9329749552448e-12 DnaJ heat shock protein family (Hsp40) member C11 . . . lymphoreticular;myocardium;ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;endometrium;synovium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;skeletal muscle;bile duct;pancreas;lung;cornea;mesenchyma;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; amygdala;whole brain;prefrontal cortex;globus pallidus;caudate nucleus; 0.17653 0.10958 -0.156065314 42.16206653 1499.67492 7.20665 DNAJC12 0.000104073988925761 0.582424720076634 0.41747120593444 DnaJ heat shock protein family (Hsp40) member C12 . . TISSUE SPECIFICITY: Expressed at high levels in brain, heart, and testis, and at reduced levels in kidney and stomach.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;bone;testis;brain;bladder;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; amygdala;adrenal gland;cerebellum peduncles;beta cell islets;caudate nucleus;parietal lobe;cerebellum; 0.16862 0.09541 0.305084559 72.22811984 151.04304 2.68690 DNAJC13 0.999999999681765 3.18235048237197e-10 4.43055145132242e-30 DnaJ heat shock protein family (Hsp40) member C13 FUNCTION: Involved in membrane trafficking through early endosomes, such as the early endosome to recycling endosome transport implicated in the recycling of transferrin and the early endosome to late endosome transport implicated in degradation of EGF and EGFR (PubMed:18256511, PubMed:18307993). Involved in the regulation of endosomal membrane tubulation and regulates th dynamics of SNX1 on the endosomal membrane; via association with FAM21 may link the WASH complex to the retromer SNX-BAR subcomplex (PubMed:24643499). {ECO:0000269|PubMed:18256511, ECO:0000269|PubMed:18307993, ECO:0000269|PubMed:24643499}.; DISEASE: Parkinson disease 21 (PARK21) [MIM:616361]: An autosomal dominant form of adult-onset Parkinson disease, a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. {ECO:0000269|PubMed:24218364}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;urinary;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.41777 0.13911 0.17442557 65.77022883 851.5822 5.70174 DNAJC14 0.999707754511218 0.00029224496063541 5.28146934319398e-10 DnaJ heat shock protein family (Hsp40) member C14 FUNCTION: Regulates the export of target proteins, such as DRD1, from the endoplasmic reticulum to the cell surface. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in pancreas and selectively expressed in brain, lung, liver, skeletal muscle and kidney. {ECO:0000269|PubMed:12768437}.; lymphoreticular;ovary;colon;skin;retina;bone marrow;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);hypothalamus;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;cervix;spleen;mammary gland;stomach; . 0.57454 0.14465 -0.336073593 30.55555556 63.50033 1.63248 DNAJC15 2.92123814107371e-07 0.0931391920470958 0.90686051582909 DnaJ heat shock protein family (Hsp40) member C15 FUNCTION: Negative regulator of the mitochondrial respiratory chain. Prevents mitochondrial hyperpolarization state and restricts mitochondrial generation of ATP (By similarity). Acts as an import component of the TIM23 translocase complex. Stimulates the ATPase activity of HSPA9. {ECO:0000250, ECO:0000269|PubMed:23263864}.; . TISSUE SPECIFICITY: Expressed at highest levels in heart, followed by liver and kidney. {ECO:0000269|PubMed:11358853, ECO:0000269|PubMed:23530063}.; . . 0.06115 0.10528 0.170987912 65.5579146 822.54052 5.62889 DNAJC16 3.79285066744292e-05 0.999507164967027 0.000454906526298807 DnaJ heat shock protein family (Hsp40) member C16 . . . . . 0.12031 . -1.263883952 5.260674687 72.69635 1.77916 DNAJC17 0.0285392981407643 0.960570696906046 0.01089000495319 DnaJ heat shock protein family (Hsp40) member C17 . . . unclassifiable (Anatomical System);medulla oblongata;lymph node;trophoblast;colon;fovea centralis;choroid;lens;skeletal muscle;retina;breast;optic nerve;lung;larynx;thyroid;placenta;macula lutea;head and neck;cervix;germinal center;kidney;brain;mammary gland;bladder;stomach; . 0.16529 . 0.373041938 75.29488087 340.46908 3.91559 DNAJC18 0.00546933470257871 0.989393706101372 0.00513695919604917 DnaJ heat shock protein family (Hsp40) member C18 . . . unclassifiable (Anatomical System);medulla oblongata;cartilage;hypothalamus;muscle;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;optic nerve;lung;frontal lobe;macula lutea;visual apparatus;hippocampus;alveolus;pituitary gland;testis;kidney;brain;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion; 0.21997 0.09590 -0.714505427 14.4019816 35.75998 1.07542 DNAJC19 0.0144036901582712 0.872072687395186 0.113523622446543 DnaJ heat shock protein family (Hsp40) member C19 FUNCTION: Probable component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. May act as a co-chaperone that stimulate the ATP-dependent activity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; . . 0.24673 0.14229 -0.075159878 47.78839349 12.52066 0.45614 DNAJC19P1 . . . DnaJ heat shock protein family (Hsp40) member C19 pseudogene 1 . . . . . . . . . . . DNAJC19P2 . . . DnaJ heat shock protein family (Hsp40) member C19 pseudogene 2 . . . . . . . . . . . DNAJC19P3 . . . DnaJ heat shock protein family (Hsp40) member C19 pseudogene 3 . . . . . . . . . . . DNAJC19P4 . . . DnaJ heat shock protein family (Hsp40) member C19 pseudogene 4 . . . . . . . . . . . DNAJC19P5 . . . DnaJ heat shock protein family (Hsp40) member C19 pseudogene 5 . . . . . . . . . . . DNAJC19P6 . . . DnaJ heat shock protein family (Hsp40) member C19 pseudogene 6 . . . . . . . . . . . DNAJC19P7 . . . DnaJ heat shock protein family (Hsp40) member C19 pseudogene 7 . . . . . . . . . . . DNAJC19P8 . . . DnaJ heat shock protein family (Hsp40) member C19 pseudogene 8 . . . . . . . . . . . DNAJC19P9 . . . DnaJ heat shock protein family (Hsp40) member C19 pseudogene 9 . . . . . . . . . . . DNAJC21 1.4512199767017e-05 0.99123339306773 0.00875209473250283 DnaJ heat shock protein family (Hsp40) member C21 FUNCTION: May act as a co-chaperone for HSP70.; . TISSUE SPECIFICITY: Brain, placenta, kidney and pancreas.; ovary;colon;skin;bone marrow;uterus;whole body;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;skeletal muscle;bile duct;breast;lung;epididymis;placenta;liver;head and neck;cervix;kidney;stomach;aorta; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;white blood cells; 0.13651 0.10368 -0.154246007 42.22694032 118.51193 2.36941 DNAJC22 1.10777165570409e-05 0.202809823110493 0.79717909917295 DnaJ heat shock protein family (Hsp40) member C22 FUNCTION: May function as a co-chaperone.; . . . . . 0.10996 -0.381986487 27.68931352 157.20728 2.73999 DNAJC24 7.24727295119377e-07 0.0829571002670014 0.917042175005703 DnaJ heat shock protein family (Hsp40) member C24 FUNCTION: Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) which can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A (Eta). {ECO:0000269|PubMed:22367199, ECO:0000269|PubMed:22509046}.; . . . . 0.03877 0.12532 0.391453969 75.87284737 19.09788 0.65860 DNAJC25 0.00562063467846135 0.898877819112946 0.095501546208593 DnaJ heat shock protein family (Hsp40) member C25 . . . smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;testis;germinal center;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;bile duct;breast;lung;adrenal gland;trabecular meshwork;placenta;liver;head and neck;kidney;mammary gland; . 0.22370 0.10299 . . 770.17917 5.49149 DNAJC25-GNG10 0.00277817399396608 0.350438669283322 0.646783156722712 DNAJC25-GNG10 readthrough . . . . . . . . . 0.65084 0.00978 DNAJC27 0.0482582333406014 0.928439777985251 0.0233019886741479 DnaJ heat shock protein family (Hsp40) member C27 FUNCTION: GTPase which can activate the MEK/ERK pathway and induce cell transformation when overexpressed. May act as a nuclear scaffold for MAPK1, probably by association with MAPK1 nuclear export signal leading to enhanced ERK1/ERK2 signaling. {ECO:0000250|UniProtKB:Q8CFP6}.; . TISSUE SPECIFICITY: Overexpressed in gastrointestinal cancers; expression correlates with later tumor-node-metastasis stages of colorectal cancers. {ECO:0000269|PubMed:24746703}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;urinary;lens;skeletal muscle;lung;trabecular meshwork;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.48871 . -0.117432389 44.89266336 37.28644 1.11199 DNAJC27-AS1 . . . DNAJC27 antisense RNA 1 . . . . . . . . . . . DNAJC28 2.51142673645981e-07 0.286674009715548 0.713325739141778 DnaJ heat shock protein family (Hsp40) member C28 FUNCTION: May have a role in protein folding or as a chaperone.; . . unclassifiable (Anatomical System);ovary;heart;salivary gland;intestine;pharynx;colon;blood;skin;breast;uterus;prostate;lung;bone;liver;testis;kidney;brain;bladder; dorsal root ganglion;ciliary ganglion;skeletal muscle; 0.10024 . 0.284856336 71.40835103 1385.56304 6.96711 DNAJC30 0.00479827795416004 0.687217962066204 0.307983759979636 DnaJ heat shock protein family (Hsp40) member C30 . . TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, spleen, stomach and testis. {ECO:0000269|PubMed:12073013}.; . . 0.15659 0.09146 0.41713504 76.95800896 1636.86057 7.48002 DNAL1 0.00640146907989069 0.745417862397987 0.248180668522122 dynein axonemal light chain 1 . . TISSUE SPECIFICITY: Expressed in tissues carrying motile cilia such as testis. {ECO:0000269|PubMed:15845866}.; unclassifiable (Anatomical System);amygdala;ovary;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;skin;retina;breast;prostate;whole body;lung;bone;liver;testis;kidney;brain;bladder;aorta;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.36783 0.11901 0.257356108 69.83368719 24.54661 0.80738 DNAL4 0.32342202050456 0.610584670431043 0.0659933090643967 dynein axonemal light chain 4 FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity (By similarity). {ECO:0000250}.; DISEASE: Mirror movements 3 (MRMV3) [MIM:616059]: A disorder characterized by contralateral involuntary movements that mirror voluntary ones. While mirror movements are occasionally found in young children, persistence beyond the age of 10 is abnormal. Mirror movements occur more commonly in the upper extremities. {ECO:0000269|PubMed:25098561}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;colon;skin;retina;bone marrow;whole body;frontal lobe;synovium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;skeletal muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;alveolus;spleen;kidney;stomach; . 0.26861 0.12378 -0.09720619 46.20193442 7.12898 0.26648 DNALI1 6.82031949142269e-08 0.143328666162226 0.85667126563458 dynein axonemal light intermediate chain 1 FUNCTION: May play a dynamic role in flagellar motility.; . TISSUE SPECIFICITY: Expressed in many tissues. A smaller 0.9 kb and a larger 2.5 kb transcripts were detected at the highest level in the testis, at medium levels in the prostate, heart, liver, lung and pancreas, at low levels in the ovary, skeletal muscle and small intestine. Not detected in spleen, colon epithelium, thymus or peripheral blood leukocytes. The 0.9 kb transcript is expressed at a 20-fold higher level than the 2.5 kb transcript in the testis.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;epidermis;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; . 0.17199 0.10586 0.374860183 75.43052607 2071.89484 8.38465 DNASE1 1.00614589458506e-11 0.0115619465169384 0.988438053473 deoxyribonuclease I FUNCTION: Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization (By similarity). {ECO:0000250}.; DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:11479590}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Principally in tissues of the digestive system. Highest levels found in urine, but also relatively abundant in semen and saliva.; lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;iris;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.14362 0.35590 0.380318343 75.63104506 2650.94195 9.67042 DNASE1L1 0.0612658007905369 0.869128049859128 0.0696061493503354 deoxyribonuclease I-like 1 . . TISSUE SPECIFICITY: Highest levels in skeletal and cardiac muscles. Detectable in all other tissues tested except brain. {ECO:0000269|PubMed:8541839}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;aorta;peripheral nerve; . 0.19047 0.28561 -0.0274281 51.65723048 48.03027 1.34745 DNASE1L2 2.27540813731848e-07 0.150778273927148 0.849221498532038 deoxyribonuclease I-like 2 FUNCTION: Divalent cation-dependent acid DNA endonuclease involved in the breakdown of the nucleus during corneocyte formation of epidermal keratinocytes. May play an immune role by eliminating harmful DNA released into the extracellular environment by damaged epidermal cells. {ECO:0000269|PubMed:16902420}.; . TISSUE SPECIFICITY: Preferentially expressed in the skin and up- regulated during keratinocytes differentiation. Highly abundant (at protein level) in the stratum granulosum. {ECO:0000269|PubMed:16902420}.; unclassifiable (Anatomical System);optic nerve;ovary;macula lutea;fovea centralis;choroid;lens;brain;skin;retina; superior cervical ganglion; 0.02997 0.18130 -0.093566408 46.7386176 43.79426 1.26021 DNASE1L3 0.155489629437521 0.828257675251996 0.0162526953104831 deoxyribonuclease I-like 3 FUNCTION: Has DNA hydrolytic activity. Does not bind to actin. Cleaves chromatin DNA to nucleosomal units.; . TISSUE SPECIFICITY: Liver and spleen.; unclassifiable (Anatomical System);cartilage;heart;adrenal cortex;colon;skin;skeletal muscle;uterus;pancreas;lung;nasopharynx;placenta;liver;testis;spleen;germinal center;kidney;brain; superior cervical ganglion;liver;trigeminal ganglion; 0.15489 0.09901 0.308721233 72.59966973 301.75378 3.70002 DNASE2 0.0537334042909933 0.92640310830645 0.0198634874025569 deoxyribonuclease II, lysosomal FUNCTION: Hydrolyzes DNA under acidic conditions with a preference for double-stranded DNA. Plays a major role in the degradation of nuclear DNA in cellular apoptosis during development. Necessary for proper fetal development and for definitive erythropoiesis in fetal liver, where it degrades nuclear DNA expelled from erythroid precursor cells.; . . lymphoreticular;ovary;salivary gland;colon;vein;skin;prostate;endometrium;bone;thyroid;pituitary gland;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;islets of Langerhans;spinal cord;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;duodenum;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.07523 0.13067 0.393270925 76.04977589 43.67777 1.25724 DNASE2B 3.78798985155026e-14 0.00309154011436729 0.996908459885595 deoxyribonuclease II beta FUNCTION: Hydrolyzes DNA under acidic conditions. Does not require divalent cations for activity. Participates in the degradation of nuclear DNA during lens cell differentiation. {ECO:0000269|PubMed:11700027, ECO:0000269|PubMed:12944971}.; . TISSUE SPECIFICITY: Highly expressed in the eye lens and in salivary gland. Detected at lower levels in lung, prostate and lymph node. Isoform 2 is lung specific. {ECO:0000269|PubMed:11376952, ECO:0000269|PubMed:11700027, ECO:0000269|PubMed:12944971}.; . . 0.20864 0.10705 0.883760026 89.07171503 3581.36449 11.57147 DND1 0.709666236197164 0.286940377548949 0.0033933862538869 DND microRNA-mediated repression inhibitor 1 FUNCTION: RNA-binding factor that positively regulates gene expression by prohibiting miRNA-mediated gene suppression. Relieves miRNA repression in germline cells (By similarity). Prohibits the function of several miRNAs by blocking the accessibility of target mRNAs. Sequence-specific RNA-binding factor that binds specifically to U-rich regions (URRs) in the 3' untranslated region (3'-UTR) of several mRNAs. Does not bind to miRNAs. May play a role during primordial germ cell (PGC) survival (By similarity). However, does not seem to be essential for PGC migration (By similarity). {ECO:0000250, ECO:0000269|PubMed:18155131}.; . . . . 0.38489 0.14624 . . 150.19546 2.67373 DND1P1 . . . DND microRNA-mediated repression inhibitor 1 pseudogene 1 . . . . . . . . . . . DND1P2 . . . DND microRNA-mediated repression inhibitor 1 pseudogene 2 . . . . . . . . . . . DNER 0.785502089513872 0.214485950637814 1.19598483140103e-05 delta/notch like EGF repeat containing FUNCTION: Activator of the NOTCH1 pathway. May mediate neuron-glia interaction during astrocytogenesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, spinal cord and adrenal gland. {ECO:0000269|PubMed:11997712}.; fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;larynx;bone;pituitary gland;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;lacrimal gland;hypothalamus;lens;skeletal muscle;breast;pia mater;lung;adrenal gland;placenta;macula lutea;hippocampus;liver;cervix;head and neck;kidney;cerebellum; whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;adrenal cortex;pons;caudate nucleus;subthalamic nucleus;fetal brain;adrenal gland;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.26323 0.23990 -1.017713296 8.103326256 318.26859 3.78890 DNHD1 1.33457888519476e-18 0.411356391786314 0.588643608213686 dynein heavy chain domain 1 . . . unclassifiable (Anatomical System);prostate;lung;epididymis;spinal cord;liver;testis;spleen; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.08316 . 6.676327134 99.88204765 15349.22988 26.78541 DNLZ 0.00894156460568737 0.579670541913603 0.41138789348071 DNL-type zinc finger FUNCTION: May function as a co-chaperone towards HSPA9/mortalin which, by itself, is prone to self-aggregation. {ECO:0000269|PubMed:23462535}.; . . . . 0.14720 0.09976 . . 621.18542 5.02661 DNM1 0.999863839316264 0.000136160680371301 3.36424024630027e-12 dynamin 1 FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis.; DISEASE: Epileptic encephalopathy, early infantile, 31 (EIEE31) [MIM:616346]: A form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. {ECO:0000269|PubMed:25262651, ECO:0000269|PubMed:25533962}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;bone marrow;retina;optic nerve;whole body;frontal lobe;testis;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;islets of Langerhans;hypothalamus;lens;lung;placenta;hippocampus;visual apparatus;macula lutea;kidney;stomach;cerebellum; whole brain;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.21825 0.67914 -0.558357437 19.54470394 214.81838 3.16122 DNM1L 0.176947821562628 0.823047669297185 4.5091401876996e-06 dynamin 1-like FUNCTION: Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into membrane- associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage. Required for normal brain development, including that of cerebellum. Facilitates developmentally regulated apoptosis during neural tube formation. Required for a normal rate of cytochrome c release and caspase activation during apoptosis; this requirement may depend upon the cell type and the physiological apoptotic cues. Also required for mitochondrial fission during mitosis. Required for formation of endocytic vesicles. Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in synaptic vesicles; the function may require its recruitment by MFF to clathrin-containing vesicles. Required for programmed necrosis execution.; DISEASE: Note=May be associated with Alzheimer disease through beta-amyloid-induced increased S-nitrosylation of DNM1L, which triggers, directly or indirectly, excessive mitochondrial fission, synaptic loss and neuronal damage. {ECO:0000269|PubMed:19342591}.; DISEASE: Encephalopathy, lethal, due to defective mitochondrial and peroxisomal fission (EMPF) [MIM:614388]: A rare autosomal dominant systemic disorder resulting in lack of neurologic development and death in infancy. After birth, infants present in the first week of life with poor feeding and neurologic impairment, including hypotonia, little spontaneous movement, no tendon reflexes, no response to light stimulation, and poor visual fixation. Other features include mildly elevated plasma concentration of very-long-chain fatty acids, lactic acidosis, microcephaly, deep-set eyes, optic atrophy and hypoplasia, and an abnormal gyral pattern in both frontal lobes associated with dysmyelination. {ECO:0000269|PubMed:17460227}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed with highest levels found in skeletal muscles, heart, kidney and brain. Isoform 1 is brain-specific. Isoform 2 and isoform 3 are predominantly expressed in testis and skeletal muscles respectively. Isoform 4 is weakly expressed in brain, heart and kidney. Isoform 5 is dominantly expressed in liver, heart and kidney. Isoform 6 is expressed in neurons. {ECO:0000269|PubMed:10749171, ECO:0000269|PubMed:9422767, ECO:0000269|PubMed:9570752, ECO:0000269|PubMed:9731200, ECO:0000269|PubMed:9786947}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;uterus;prostate;frontal lobe;endometrium;cochlea;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;hypothalamus;pineal body;pharynx;blood;skeletal muscle;bile duct;breast;lung;epididymis;mesenchyma;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;subthalamic nucleus;occipital lobe;medulla oblongata;thalamus;globus pallidus;caudate nucleus;pons;parietal lobe;cingulate cortex; 0.40663 0.24974 -0.979072682 8.752064166 26.57798 0.85958 DNM1P5 . . . dynamin 1 pseudogene 5 . . . . . . . . . . . DNM1P9 . . . dynamin 1 pseudogene 9 . . . . . . . . . . . DNM1P17 . . . dynamin 1 pseudogene 17 . . . . . . . . . . . DNM1P18 . . . dynamin 1 pseudogene 18 . . . . . . . . . . . DNM1P19 . . . dynamin 1 pseudogene 19 . . . . . . . . . . . DNM1P24 . . . dynamin 1 pseudogene 24 . . . . . . . . . . . DNM1P25 . . . dynamin 1 pseudogene 25 . . . . . . . . . . . DNM1P26 . . . dynamin 1 pseudogene 26 . . . . . . . . . . . DNM1P27 . . . dynamin 1 pseudogene 27 . . . . . . . . . . . DNM1P28 . . . dynamin 1 pseudogene 28 . . . . . . . . . . . DNM1P29 . . . dynamin 1 pseudogene 29 . . . . . . . . . . . DNM1P30 . . . dynamin 1 pseudogene 30 . . . . . . . . . . . DNM1P31 . . . dynamin 1 pseudogene 31 . . . . . . . . . . . DNM1P32 . . . dynamin 1 pseudogene 32 . . . . . . . . . . . DNM1P33 . . . dynamin 1 pseudogene 33 . . . . . . . . . . . DNM1P34 . . . dynamin 1 pseudogene 34 . . . . . . . . . . . DNM1P35 . . . dynamin 1 pseudogene 35 . . . . . . . . . . . DNM1P36 . . . dynamin 1 pseudogene 36 . . . . . . . . . . . DNM1P37 . . . dynamin 1 pseudogene 37 . . . . . . . . . . . DNM1P38 . . . dynamin 1 pseudogene 38 . . . . . . . . . . . DNM1P39 . . . dynamin 1 pseudogene 39 . . . . . . . . . . . DNM1P40 . . . dynamin 1 pseudogene 40 . . . . . . . . . . . DNM1P41 . . . dynamin 1 pseudogene 41 . . . . . . . . . . . DNM1P43 . . . dynamin 1 pseudogene 43 . . . . . . . . . . . DNM1P44 . . . dynamin 1 pseudogene 44 . . . . . . . . . . . DNM1P45 . . . dynamin 1 pseudogene 45 . . . . . . . . . . . DNM1P46 . . . dynamin 1 pseudogene 46 . . . unclassifiable (Anatomical System);thyroid;kidney; . . . . . . . DNM1P47 . . . dynamin 1 pseudogene 47 . . . . . . . . . . . DNM1P48 . . . dynamin 1 pseudogene 48 . . . . . . . . . . . DNM1P49 . . . dynamin 1 pseudogene 49 . . . . . . . . . . . DNM1P50 . . . dynamin 1 pseudogene 50 . . . . . . . . . . . DNM1P51 . . . dynamin 1 pseudogene 51 . . . . . . . . . . . DNM2 0.999968599089655 3.14009098783304e-05 4.66488228227116e-13 dynamin 2 FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Plays an important role in vesicular trafficking processes, in particular endocytosis. Involved in cytokinesis. {ECO:0000250|UniProtKB:P39052, ECO:0000269|PubMed:12498685}.; DISEASE: Myopathy, centronuclear, 1 (CNM1) [MIM:160150]: A congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers. {ECO:0000269|PubMed:16227997, ECO:0000269|PubMed:17825552, ECO:0000269|PubMed:17932957, ECO:0000269|PubMed:19122038, ECO:0000269|PubMed:19623537, ECO:0000269|PubMed:19932619, ECO:0000269|PubMed:19932620, ECO:0000269|PubMed:20227276, ECO:0000269|PubMed:22396310}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Lethal congenital contracture syndrome 5 (LCCS5) [MIM:615368]: A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy and congenital non-progressive joint contractures. The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth. {ECO:0000269|PubMed:23092955}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease, dominant, intermediate type, B (CMTDIB) [MIM:606482]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. The dominant intermediate type B is characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. {ECO:0000269|PubMed:15731758}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease 2M (CMT2M) [MIM:606482]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. {ECO:0000269|PubMed:17636067, ECO:0000269|PubMed:18560793}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;amnion;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; . 0.13329 0.67364 -1.328217086 4.712196273 50.91122 1.40599 DNM3 0.028276990644479 0.971703983613098 1.90257424232593e-05 dynamin 3 FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis (By similarity). {ECO:0000250}.; . . medulla oblongata;sympathetic chain;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;hypothalamus;adrenal cortex;lens;skeletal muscle;lung;hippocampus;visual apparatus;macula lutea;kidney;mammary gland;cerebellum; amygdala;whole brain;superior cervical ganglion;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.25528 0.24339 -1.111360919 6.717386176 102.17679 2.18523 DNM3-IT1 . . . DNM3 intronic transcript 1 . . . . . . . . . . . DNM3OS . . . DNM3 opposite strand/antisense RNA . . . . . . . . . . . DNMBP 1.15012174102811e-09 0.999839089953007 0.000160908896871288 dynamin binding protein FUNCTION: Scaffold protein that links dynamin with actin- regulating proteins. May play a role in membrane trafficking between the cell surface and the Golgi (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in heart, brain, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:14506234}.; ovary;salivary gland;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;cerebral cortex;bone;thyroid;testis;germinal center;brain;spinal ganglion;unclassifiable (Anatomical System);cartilage;heart;tongue;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16068 0.14332 -0.468608479 23.26020288 1197.04737 6.56444 DNMBP-AS1 . . . DNMBP antisense RNA 1 . . . . . . . . . . . DNMT1 0.999999999466791 5.33209206062012e-10 2.26934254447258e-25 DNA (cytosine-5-)-methyltransferase 1 FUNCTION: Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. {ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:18413740, ECO:0000269|PubMed:18754681}.; DISEASE: Neuropathy, hereditary sensory, 1E (HSN1E) [MIM:614116]: A neurodegenerative disorder characterized by adult onset of progressive peripheral sensory loss associated with progressive hearing impairment and early-onset dementia. {ECO:0000269|PubMed:21532572}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cerebellar ataxia, deafness, and narcolepsy, autosomal dominant (ADCADN) [MIM:604121]: An autosomal dominant neurologic disorder characterized by adult onset of progressive cerebellar ataxia, narcolepsy, cataplexy, sensorineural deafness, and dementia. More variable features include optic atrophy, sensory neuropathy, psychosis, and depression. {ECO:0000269|PubMed:22328086}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous; highly expressed in fetal tissues, heart, kidney, placenta, peripheral blood mononuclear cells, and expressed at lower levels in spleen, lung, brain, small intestine, colon, liver, and skeletal muscle. Isoform 2 is less expressed than isoform 1. {ECO:0000269|PubMed:10325416}.; ovary;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach;cerebellum; testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;placenta;tumor;testis;bone marrow;thymus;cerebellum; 0.75008 0.70645 -1.541497103 3.326256192 224.68683 3.24198 DNMT3A 7.7278751608327e-45 8.71631773323096e-11 0.999999999912837 DNA (cytosine-5-)-methyltransferase 3 alpha FUNCTION: Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZBTB18. Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. Can actively repress transcription through the recruitment of HDAC activity. {ECO:0000269|PubMed:16357870}.; DISEASE: Tatton-Brown-Rahman syndrome (TBRS) [MIM:615879]: An overgrowth syndrome characterized by a distinctive facial appearance, tall stature and intellectual disability. Facial gestalt is characterized by a round face, heavy horizontal eyebrows and narrow palpebral fissures. Less common features include atrial septal defects, seizures, umbilical hernia, and scoliosis. {ECO:0000269|PubMed:24614070}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in fetal tissues, skeletal muscle, heart, peripheral blood mononuclear cells, kidney, and at lower levels in placenta, brain, liver, colon, spleen, small intestine and lung. {ECO:0000269|PubMed:10325416}.; unclassifiable (Anatomical System);cartilage;ovary;heart;tongue;islets of Langerhans;pineal body;colon;parathyroid;blood;skin;skeletal muscle;retina;uterus;pancreas;whole body;lung;endometrium;larynx;nasopharynx;placenta;visual apparatus;liver;testis;cervix;head and neck;spleen;brain; superior cervical ganglion;skeletal muscle; 0.88689 0.41514 -1.131590109 6.481481481 41.83604 1.21826 DNMT3AP1 . . . DNA methyltransferase 3A pseudogene 1 . . . . . . . . . . . DNMT3B 0.999774600266445 0.000225399733459755 9.51532533872796e-14 DNA (cytosine-5-)-methyltransferase 3 beta FUNCTION: Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. May preferentially methylates nucleosomal DNA within the nucleosome core region. May function as transcriptional co- repressor by associating with CBX4 and independently of DNA methylation. Seems to be involved in gene silencing (By similarity). In association with DNMT1 and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Isoforms 4 and 5 are probably not functional due to the deletion of two conserved methyltransferase motifs. Function as transcriptional corepressor by associating with ZHX1. {ECO:0000250, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:17303076, ECO:0000269|PubMed:18413740, ECO:0000269|PubMed:18567530}.; DISEASE: Immunodeficiency-centromeric instability-facial anomalies syndrome 1 (ICF1) [MIM:242860]: A rare disorder characterized by a variable immunodeficiency resulting in recurrent infections, facial anomalies, and branching of chromosomes 1, 9, and 16. Other variable symptoms include growth retardation, failure to thrive, and psychomotor retardation. Laboratory studies show limited hypomethylation of DNA in a small fraction of the genome in some, but not all, patients. {ECO:0000269|PubMed:10555141, ECO:0000269|PubMed:10588719, ECO:0000269|PubMed:10647011, ECO:0000269|PubMed:11102980, ECO:0000269|PubMed:15580563}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous; highly expressed in fetal liver, heart, kidney, placenta, and at lower levels in spleen, colon, brain, liver, small intestine, lung, peripheral blood mononuclear cells, and skeletal muscle. Isoform 1 is expressed in all tissues except brain, skeletal muscle and PBMC, 3 is ubiquitous, 4 is expressed in all tissues except brain, skeletal muscle, lung and prostate and 5 is detectable only in testis and at very low level in brain and prostate.; ovary;colon;parathyroid;skin;bone marrow;uterus;thyroid;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;breast;lung;placenta;visual apparatus;hypopharynx;liver;cervix;head and neck;kidney; superior cervical ganglion;testis;atrioventricular node; 0.64188 0.09494 -1.703090605 2.535975466 197.4701 3.03837 DNMT3L 1.25678875267047e-06 0.81681097764307 0.183187765568177 DNA (cytosine-5-)-methyltransferase 3-like FUNCTION: Catalytically inactive regulatory factor of DNA methyltransferases. It is essential for the function of DNMT3A and DNMT3B. Activates DNMT3A and DNMT3B by binding to their catalytic domain. Accelerates the binding of DNA and AdoMet to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases. Recognizes unmethylated histone H3 lysine 4 (H3K4) and induces de novo DNA methylation by recruitment or activation of DNMT3. {ECO:0000269|PubMed:17687327}.; . TISSUE SPECIFICITY: Expressed at low levels in several tissues including testis, ovary, and thymus.; unclassifiable (Anatomical System);lung;placenta;testis; superior cervical ganglion;testis - seminiferous tubule;liver;pons; 0.11433 0.17888 -0.488577883 22.64685067 631.44216 5.06208 DNPEP 0.000202595534805018 0.976661043674132 0.023136360791063 aspartyl aminopeptidase FUNCTION: Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism. {ECO:0000269|PubMed:9632644}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9632644}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;gum;bone;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;adipose tissue;heart;tumor;atrioventricular node;skeletal muscle;testis - seminiferous tubule;placenta;liver;testis;ciliary ganglion;trigeminal ganglion; 0.35948 0.10835 0.240763792 69.36777542 357.16949 4.00568 DNPH1 0.000716569937593186 0.51836332137231 0.480920108690097 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5- phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'- monophosphates containing purine bases are preferred to those containing pyrimidine bases. {ECO:0000255|HAMAP-Rule:MF_03036, ECO:0000269|PubMed:24260472, ECO:0000269|PubMed:25108359}.; . TISSUE SPECIFICITY: Expressed at low levels in brain, colon, lung, peripheral blood leukocytes, placenta, small intestine, and thymus. Expressed at high levels in heart, kidney, liver, skeletal muscle and spleen. Overexpressed in a significant proportion of breast cancers. {ECO:0000269|PubMed:18726892}.; . . 0.07277 0.15165 . . 8.3349 0.30514 DNTT 8.53802251177926e-05 0.983450369808469 0.0164642499664137 DNA nucleotidylexotransferase FUNCTION: Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells. {ECO:0000250|UniProtKB:P09838}.; . . . . 0.13258 0.92580 -0.288341872 33.41589998 134.78939 2.52426 DNTTIP1 0.431436687799906 0.568259861428034 0.000303450772060806 deoxynucleotidyltransferase, terminal, interacting protein 1 FUNCTION: Increases DNTT terminal deoxynucleotidyltransferase activity (in vitro) (PubMed:11473582). Also acts as a transcriptional regulator, binding to the consensus sequence 5'- GNTGCATG-3' following an AT-tract. Associates with RAB20 promoter and positively regulates its transcription. Binds DNA and nucleosomes; may recruit HDAC1 complexes to nucleosomes or naked DNA. {ECO:0000269|PubMed:11473582, ECO:0000269|PubMed:23874396, ECO:0000305|PubMed:25653165}.; . . . . 0.30429 0.11484 0.014844891 54.94810097 278.74725 3.57888 DNTTIP2 0.000217903722961202 0.978830360970323 0.0209517353067156 deoxynucleotidyltransferase, terminal, interacting protein 2 FUNCTION: Regulates the transcriptional activity of DNTT and ESR1. May function as a chromatin remodeling protein. {ECO:0000269|PubMed:12786946, ECO:0000269|PubMed:15047147}.; . TISSUE SPECIFICITY: Widely expressed with higher levels in testis. {ECO:0000269|PubMed:12786946, ECO:0000269|PubMed:15047147}.; unclassifiable (Anatomical System); superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.41626 0.08192 -0.132199953 43.97853267 996.15945 6.08277 DOC2A 0.0185536457979363 0.961204690801942 0.0202416634001217 double C2-like domains, alpha FUNCTION: Calcium sensor which most probably regulates fusion of vesicles with membranes. Binds calcium and phospholipids. May be involved in calcium dependent neurotransmitter release through the interaction with UNC13A. May be involved in calcium-dependent spontaneous release of neurotransmitter in absence of action potentials in neuronal cells. Regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells. {ECO:0000269|PubMed:18354201, ECO:0000269|PubMed:9736751, ECO:0000269|PubMed:9804756}.; . TISSUE SPECIFICITY: Predominantly expressed in brain. Also expressed in testis. {ECO:0000269|PubMed:7826360, ECO:0000269|PubMed:8554557}.; unclassifiable (Anatomical System);uterus;optic nerve;whole body;frontal lobe;bone;thyroid;testis;kidney;brain;cerebellum; amygdala;superior cervical ganglion;globus pallidus;ciliary ganglion; 0.29685 0.10952 -0.556537043 19.72753008 1428.98715 7.05864 DOC2B 0.382719811977725 0.476953141588302 0.140327046433973 double C2-like domains, beta FUNCTION: Calcium sensor which positively regulates SNARE- dependent fusion of vesicles with membranes. Binds phospholipids in a calcium-dependent manner and may act at the priming stage of fusion by modifying membrane curvature to stimulate fusion. Involved in calcium-triggered exocytosis in chromaffin cells and calcium-dependent spontaneous release of neurotransmitter in absence of action potentials in neuronal cells. Involved both in glucose-stimulated insulin secretion in pancreatic cells and insulin-dependent GLUT4 transport to the plasma membrane in adipocytes (By similarity). {ECO:0000250, ECO:0000269|PubMed:9804756}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in brain and kidney. Expressed in pancreatic islet cells (at protein level). {ECO:0000269|PubMed:17548353, ECO:0000269|PubMed:8554557}.; optic nerve;ovary;placenta;macula lutea;fovea centralis;choroid;lens;brain;retina; . 0.22422 0.11084 . . 58.48664 1.54921 DOC2GP . . . double C2-like domains, gamma, pseudogene . . . . . . . . . . . DOCK1 0.36842317046063 0.631576829539275 9.49676081056938e-14 dedicator of cytokinesis 1 FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Functions as a guanine nucleotide exchange factor (GEF), which activates Rac Rho small GTPases by exchanging bound GDP for free GTP. Its GEF activity may be enhanced by ELMO1. {ECO:0000269|PubMed:8657152}.; . TISSUE SPECIFICITY: Highly expressed in placenta, lung, kidney, pancreas and ovary. Expressed at intermediate level in thymus, testes and colon.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;dura mater;brain;unclassifiable (Anatomical System);amygdala;meninges;cartilage;small intestine;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;medulla oblongata;caudate nucleus;trigeminal ganglion;parietal lobe; 0.11584 0.19704 . . 350.01956 3.96565 DOCK2 0.999999892553994 1.07446005463636e-07 6.38720031627346e-24 dedicator of cytokinesis 2 FUNCTION: Involved in cytoskeletal rearrangements required for lymphocyte migration in response of chemokines. Activates RAC1 and RAC2, but not CDC42, by functioning as a guanine nucleotide exchange factor (GEF), which exchanges bound GDP for free GTP. May also participate in IL2 transcriptional activation via the activation of RAC2. {ECO:0000269|PubMed:21613211}.; DISEASE: Immunodeficiency 40 (IMD40) [MIM:616433]: A form of combined immunodeficiency characterized by lymphopenia, and defective T-cell, B-cell, and NK-cell responses. Patients suffer from severe invasive bacterial and viral infections in early childhood and may die without bone marrow transplantation. {ECO:0000269|PubMed:26083206}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Specifically expressed in hematopoietic cells. Highly expressed in peripheral blood leukocytes, and expressed at intermediate level in thymus and spleen. Expressed at very low level in the small intestine and colon. {ECO:0000269|PubMed:10559471}.; lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;stomach;thymus; lymph node;tumor;white blood cells;whole blood;tonsil;bone marrow;thymus; 0.50359 0.10971 -1.155796362 6.10403397 368.53431 4.05624 DOCK3 0.999999698562023 3.01437976982967e-07 7.88098918406588e-23 dedicator of cytokinesis 3 FUNCTION: Potential guanine nucleotide exchange factor (GEF). GEF proteins activate some small GTPases by exchanging bound GDP for free GTP. Its interaction with presenilin proteins as well as its ability to stimulate Tau/MAPT phosphorylation suggest that it may be involved in Alzheimer disease. Ectopic expression in nerve cells decreases the secretion of beta-amyloid APBA1 protein and lowers the rate of cell-substratum adhesion, suggesting that it may affect the function of some small GTPase involved in the regulation of actin cytoskeleton or cell adhesion receptors (By similarity). {ECO:0000250}.; DISEASE: Note=A chromosomal aberration involving DOCK3 has been found in a family with early-onset behavioral/developmental disorder with features of attention deficit-hyperactivity disorder and intellectual disability. Inversion inv(3)(p14:q21). The inversion disrupts DOCK3 and SLC9A9. {ECO:0000269|PubMed:14569117}.; TISSUE SPECIFICITY: In normal brains, it is localized in the neuropil, and occasionally in the pyramidal cells, while in Alzheimer disease brains, it is associated with neurofibrillary tangles. {ECO:0000269|PubMed:11696419}.; unclassifiable (Anatomical System);frontal lobe;testis;lens; dorsal root ganglion;amygdala;whole brain;testis - interstitial;medulla oblongata;superior cervical ganglion;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;atrioventricular node;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.26912 0.13159 -1.875913477 2.005189903 126.70308 2.45415 DOCK4 0.998535732717338 0.00146426728266177 2.55531807044135e-17 dedicator of cytokinesis 4 FUNCTION: Involved in regulation of adherens junction between cells. Plays a role in cell migration. Functions as a guanine nucleotide exchange factor (GEF), which activates Rap1 small GTPase by exchanging bound GDP for free GTP. {ECO:0000269|PubMed:12628187, ECO:0000269|PubMed:20679435}.; . TISSUE SPECIFICITY: Widely expressed at low level. Highly expressed in skeletal muscle, prostate and ovary. {ECO:0000269|PubMed:12628187}.; colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;tongue;islets of Langerhans;pineal body;adrenal cortex;lens;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;head and neck;kidney; amygdala;whole brain;medulla oblongata;occipital lobe;superior cervical ganglion;prefrontal cortex;appendix;ciliary ganglion;caudate nucleus;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.35780 0.09967 -0.830447013 11.52984194 . . DOCK4-AS1 . . . DOCK4 antisense RNA 1 . . . . . . . . . . . DOCK5 0.00134268610814527 0.998657313854223 3.76313675273481e-11 dedicator of cytokinesis 5 FUNCTION: Guanine nucleotide exchange factor (GEF) for Rho and Rac. GEF proteins activate small GTPases by exchanging bound GDP for free GTP.; . . unclassifiable (Anatomical System);cartilage;ovary;heart;tongue;colon;blood;skeletal muscle;bone marrow;breast;prostate;lung;bone;placenta;liver;testis;amniotic fluid;cervix;head and neck;spleen;spinal ganglion;brain;mammary gland;bladder;stomach; superior cervical ganglion;temporal lobe;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; . 0.14957 -2.350524415 1.150035386 3159.36883 10.70955 DOCK6 2.83089712599404e-19 0.984497717774324 0.0155022822256758 dedicator of cytokinesis 6 FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for CDC42 and RAC1 small GTPases. Through its activation of CDC42 and RAC1, may regulate neurite outgrowth (By similarity). {ECO:0000250, ECO:0000269|PubMed:17196961}.; DISEASE: Adams-Oliver syndrome 2 (AOS2) [MIM:614219]: A disorder characterized by the congenital absence of skin (aplasia cutis congenita) in combination with transverse limb defects. Aplasia cutis congenita can be located anywhere on the body, but in the vast majority of the cases, it is present on the posterior parietal region where it is often associated with an underlying defect of the parietal bones. Limb abnormalities are typically limb truncation defects affecting the distal phalanges or entire digits (true ectrodactyly). Only rarely, metatarsals/metacarpals or more proximal limb structures are also affected. Apart from transverse limb defects, syndactyly, most commonly of second and third toes, can also be observed. The clinical features are highly variable and can also include cardiovascular malformations, brain abnormalities and vascular defects such as cutis marmorata and dilated scalp veins. {ECO:0000269|PubMed:21820096}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Expressed at low level in spleen, cerebellum, hippocampus and in substantia nigra. {ECO:0000269|PubMed:10718198}.; medulla oblongata;ovary;colon;parathyroid;vein;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;nervous;tongue;islets of Langerhans;hypothalamus;blood;skeletal muscle;pancreas;lung;epididymis;nasopharynx;placenta;liver;head and neck;spleen;kidney;mammary gland;aorta;stomach;thymus; dorsal root ganglion;superior cervical ganglion;heart;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.15719 0.10035 -0.941152229 9.418494928 1944.2298 8.11461 DOCK7 0.771361085896655 0.228638914103345 1.13269301939624e-16 dedicator of cytokinesis 7 FUNCTION: Functions as a guanine nucleotide exchange factor (GEF), which activates Rac1 and Rac3 Rho small GTPases by exchanging bound GDP for free GTP. Does not have a GEF activity for CDC42. Required for STMN1 'Ser-15' phosphorylation during axon formation and consequently for neuronal polarization (PubMed:16982419). Has a role in pigmentation (By similarity). Involved in the regulation of cortical neurogenesis through the control of radial glial cells (RGCs) proliferation versus differentiation; negatively regulates the basal-to-apical interkinetic nuclear migration of RGCs by antagonizing the microtubule growth-promoting function of TACC3 (By similarity). {ECO:0000250|UniProtKB:Q8R1A4, ECO:0000269|PubMed:16982419}.; DISEASE: Epileptic encephalopathy, early infantile, 23 (EIEE23) [MIM:615859]: A severe disease characterized by early-onset intractable epilepsy, dysmorphic features, intellectual disability, and cortical blindness. Brain imaging shows an abnormally marked pontobulbar sulcus with mild pontine hypoplasia, white matter abnormalities, and atrophy in the occipital lobe. {ECO:0000269|PubMed:24814191}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11214970}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;larynx;bone;pituitary gland;testis;amniotic fluid;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.10496 0.13670 -2.535908408 0.884642604 451.1915 4.41537 DOCK8 0.00013543398043996 0.999864565977926 4.16342439173150e-11 dedicator of cytokinesis 8 FUNCTION: Potential guanine nucleotide exchange factor (GEF). GEF proteins activate some small GTPases by exchanging bound GDP for free GTP (By similarity). {ECO:0000250}.; DISEASE: Hyperimmunoglobulin E recurrent infection syndrome, autosomal recessive (AR-HIES) [MIM:243700]: A rare disorder characterized by immunodeficiency, recurrent infections, eczema, increased serum IgE, eosinophilia and lack of connective tissue and skeletal involvement. {ECO:0000269|PubMed:19776401}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mental retardation, autosomal dominant 2 (MRD2) [MIM:614113]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:18060736}. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration disrupting DOCK8 has been found in a patient with mental retardation and ectodermal dysplasia. A balanced translocation, t(X;9) (q13.1;p24). A genomic deletion of approximately 230 kb in subtelomeric 9p has been detected in a patient with mental retardation.; . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;pituitary gland;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;aorta;thymus; . 0.49276 0.10648 -1.937487856 1.899032791 7212.15102 18.28926 DOCK9 0.999999306507167 6.93492832773746e-07 2.96401060799086e-21 dedicator of cytokinesis 9 FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. Overexpression induces filopodia formation. {ECO:0000269|PubMed:12172552, ECO:0000269|PubMed:19745154}.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in heart and placenta. Expressed at intermediate level in kidney, brain, lung and skeletal muscle. {ECO:0000269|PubMed:12172552}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;amygdala;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;spinal cord;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; amygdala;dorsal root ganglion;superior cervical ganglion;fetal brain;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.35485 0.10142 -2.778633322 0.672328379 918.16821 5.89066 DOCK9-AS1 . . . DOCK9 antisense RNA 1 . . . . . . . . . . . DOCK9-AS2 . . . DOCK9 antisense RNA 2 (head to head) . . . . . . . . . . . DOCK10 0.0291925300959096 0.970807469902004 2.08645242772845e-12 dedicator of cytokinesis 10 FUNCTION: Potential guanine nucleotide exchange factor (GEF). GEF proteins activate some small GTPases by exchanging bound GDP for free GTP.; . TISSUE SPECIFICITY: Expressed at low level in brain and lung. Isoform 1 is enriched in normal T-cells, isoform 3 is enriched in normal B-cells and chronic lymphocytic leukemia (CLL) B-cells. {ECO:0000269|PubMed:21514340, ECO:0000269|PubMed:9734811}.; ovary;salivary gland;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;breast;pancreas;lung;visual apparatus;alveolus;liver;spleen;head and neck;kidney; dorsal root ganglion;amygdala;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;lymph node;olfactory bulb;hypothalamus;temporal lobe;spinal cord;white blood cells;atrioventricular node;pons;caudate nucleus;skeletal muscle;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.22785 0.12287 -1.065786145 7.377919321 3131.37113 10.65498 DOCK11 0.998084519073803 0.00191548092619063 5.93759418985278e-15 dedicator of cytokinesis 11 FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. {ECO:0000250}.; . . colon;skin;bone marrow;uterus;prostate;whole body;endometrium;cochlea;thyroid;testis;germinal center;dura mater;brain;spinal ganglion;unclassifiable (Anatomical System);meninges;heart;blood;skeletal muscle;lung;pia mater;placenta;alveolus;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;adipose tissue;ciliary ganglion;atrioventricular node;trigeminal ganglion;whole blood; 0.40264 . -0.079012906 47.25760793 409.41373 4.24093 DOCK11P1 . . . dedicator of cytokinesis 11 pseudogene 1 . . . . . . . . . . . DOHH 0.0201020241741167 0.743880885399026 0.236017090426857 deoxyhypusine hydroxylase/monooxygenase FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)- L-lysine intermediate to form hypusine, an essential post- translational modification only found in mature eIF-5A factor. {ECO:0000255|HAMAP-Rule:MF_03101, ECO:0000269|PubMed:16371467, ECO:0000269|PubMed:19706422}.; . . unclassifiable (Anatomical System);lymphoreticular;lymph node;ovary;islets of Langerhans;hypothalamus;colon;parathyroid;blood;prostate;whole body;lung;frontal lobe;bone;placenta;hippocampus;testis;germinal center;kidney;brain;tonsil;thymus; parietal lobe; 0.31912 0.14859 . . 25.09665 0.82131 DOK1 0.0169928839616036 0.960107294431644 0.0228998216067523 docking protein 1 FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3. {ECO:0000269|PubMed:18156175}.; . TISSUE SPECIFICITY: Expressed in pancreas, heart, leukocyte and spleen. Expressed in both resting and activated peripheral blood T-cells. Expressed in breast cancer. {ECO:0000269|PubMed:12595900}.; unclassifiable (Anatomical System);medulla oblongata;lymph node;cartilage;tongue;islets of Langerhans;colon;blood;skin;skeletal muscle;retina;bone marrow;uterus;pancreas;prostate;lung;endometrium;placenta;testis;head and neck;spleen;germinal center;kidney;brain;mammary gland; subthalamic nucleus;superior cervical ganglion;heart;trigeminal ganglion; 0.43563 0.22365 -0.690637458 15.12149092 78.44422 1.86906 DOK2 2.33626639170304e-06 0.287355718447453 0.712641945286155 docking protein 2 FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK2 may modulate the cellular proliferation induced by IL-4, as well as IL-2 and IL-3. May be involved in modulating Bcr-Abl signaling. Attenuates EGF-stimulated MAP kinase activation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in peripheral blood leukocytes, lymph nodes and spleen. Lower expression in thymus, bone marrow and fetal liver. {ECO:0000269|PubMed:9478921}.; unclassifiable (Anatomical System);cartilage;heart;blood;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;lung;larynx;bone;placenta;macula lutea;alveolus;testis;head and neck;spleen;kidney;brain;stomach; . 0.07960 0.15433 -0.420619508 25.72540694 241.71921 3.35685 DOK3 7.27877709275655e-05 0.743816689195886 0.256110523033187 docking protein 3 FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK3 is a negative regulator of JNK signaling in B-cells through interaction with INPP5D/SHIP1. May modulate ABL1 function (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in spleen. {ECO:0000269|PubMed:12595900}.; unclassifiable (Anatomical System);lymph node;cartilage;colon;blood;bone marrow;uterus;endometrium;placenta;thyroid;testis;germinal center;mammary gland;brain;stomach;tonsil; . 0.16443 0.09799 -0.08265057 47.20452937 503.42172 4.60415 DOK4 0.197602909551512 0.792064708729878 0.0103323817186097 docking protein 4 FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK4 functions in RET-mediated neurite outgrowth and plays a positive role in activation of the MAP kinase pathway (By similarity). Putative link with downstream effectors of RET in neuronal differentiation. May be involved in the regulation of the immune response induced by T-cells. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. High expression in skeletal muscle, heart, kidney and liver. Weaker expression in spleen, lung and small intestine, brain, heart and. Expressed in both resting and activated peripheral blood T-cells. {ECO:0000269|PubMed:12595900, ECO:0000269|PubMed:12730241}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;hypopharynx;head and neck;cervix;kidney;stomach;cerebellum; uterus corpus;subthalamic nucleus;superior cervical ganglion;fetal brain;trigeminal ganglion;skeletal muscle; 0.55569 0.13588 -0.66859065 15.76433121 109.57389 2.27428 DOK5 0.0439811915489279 0.950317261899106 0.00570154655196666 docking protein 5 FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK5 functions in RET-mediated neurite outgrowth and plays a positive role in activation of the MAP kinase pathway. Putative link with downstream effectors of RET in neuronal differentiation.; . TISSUE SPECIFICITY: Highest expression in skeletal muscle, lower in brain, heart and kidney. Also detected in activated peripheral blood T-lymphocytes. {ECO:0000269|PubMed:12595900, ECO:0000269|PubMed:12730241}.; unclassifiable (Anatomical System);ovary;cartilage;spinal cord;parathyroid;fovea centralis;skin;lung;endometrium;placenta;bone;macula lutea;iris;testis;brain;thymus; dorsal root ganglion;amygdala;whole brain;superior cervical ganglion;occipital lobe;fetal brain;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.48741 0.11878 -0.582225231 18.44184949 47.86079 1.34382 DOK6 0.458839966900032 0.539947947045582 0.00121208605438539 docking protein 6 FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK6 promotes Ret- mediated neurite growth. May have a role in brain development and/or maintenance. {ECO:0000269|PubMed:15286081}.; . TISSUE SPECIFICITY: Highly expressed in fetal and adult brain. Highly expressed in the cerebellum. Weak expression in kidney, spinal cord and testis. {ECO:0000269|PubMed:15286081}.; . . 0.17804 0.12378 0.283038099 71.26680821 36.77199 1.10196 DOK7 0.00480838202293031 0.881308684844347 0.113882933132723 docking protein 7 FUNCTION: Probable muscle-intrinsic activator of MUSK that plays an essential role in neuromuscular synaptogenesis. Acts in aneural activation of MUSK and subsequent acetylcholine receptor (AchR) clustering in myotubes. Induces autophosphorylation of MUSK. {ECO:0000269|PubMed:20603078}.; DISEASE: Myasthenic syndrome, congenital, 10 (CMS10) [MIM:254300]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS10 is an autosomal recessive, post-synaptic form characterized by a typical 'limb girdle' pattern of muscle weakness with small, simplified neuromuscular junctions but normal acetylcholine receptor and acetylcholinesterase function. {ECO:0000269|PubMed:16917026, ECO:0000269|PubMed:17439981, ECO:0000269|PubMed:20012313, ECO:0000269|PubMed:22661499}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Preferentially expressed in skeletal muscle and heart. Present in thigh muscle, diaphragm and heart but not in the liver or spleen (at protein level). {ECO:0000269|PubMed:16794080}.; ovary;islets of Langerhans;parathyroid;choroid;fovea centralis;lens;retina;uterus;optic nerve;whole body;placenta;macula lutea;testis; pancreas;temporal lobe;ciliary ganglion; 0.17120 . . . 2606.59203 9.55466 DOLK 0.0576024421193242 0.924510652300583 0.0178869055800931 dolichol kinase FUNCTION: Involved in the synthesis of the sugar donor Dol-P-Man which is required in the synthesis of N-linked and O-linked oligosaccharides and for that of GPI anchors. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.21531 0.13958 -0.844966979 11.1759849 81.64791 1.91402 DOLPP1 0.604058624199982 0.394067235690615 0.00187414010940278 dolichyldiphosphatase 1 FUNCTION: Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate (By similarity). {ECO:0000250|UniProtKB:Q9JMF7}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.57121 0.12309 -0.361761279 28.6329323 16.44077 0.58201 DONSON 4.37159572043293e-05 0.959424354035422 0.0405319300073734 downstream neighbor of SON FUNCTION: Essential for DNA amplification in the ovary and required for cell proliferation during development. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;skin;uterus;whole body;cochlea;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;tongue;breast;lung;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;mammary gland;stomach;aorta; . 0.08203 . 0.306902668 72.38145789 126.67146 2.45337 DOPEY1 0.999995778425231 4.22157476871109e-06 4.04567096434759e-22 dopey family member 1 FUNCTION: May be involved in protein traffic between late Golgi and early endosomes. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;liver;spleen;kidney;stomach;thymus; subthalamic nucleus;medulla oblongata;testis - seminiferous tubule;prefrontal cortex;globus pallidus;pons; 0.32920 0.09427 -1.052752328 7.619721632 1415.32398 7.03165 DOPEY2 9.61164900781145e-08 0.999999892423314 1.14601957952762e-08 dopey family member 2 FUNCTION: May be involved in protein traffic between late Golgi and early endosomes. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Overexpressed in lymphoblasts from Down syndrome patients. {ECO:0000269|PubMed:10950924, ECO:0000269|PubMed:12767918}.; unclassifiable (Anatomical System);lymph node;spinal cord;muscle;colon;blood;skeletal muscle;bone marrow;prostate;pancreas;lung;frontal lobe;oesophagus;larynx;thyroid;placenta;liver;testis;head and neck;germinal center;brain;aorta;stomach;cerebellum; superior cervical ganglion;uterus corpus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.29781 0.10131 -3.64623945 0.277188016 3301.99985 10.96533 DOT1L 0.999988961757209 1.10382427895687e-05 1.49637792774902e-15 DOT1 like histone H3K79 methyltransferase FUNCTION: Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;blood;parathyroid;choroid;bone marrow;breast;lung;placenta;testis;germinal center;brain; superior cervical ganglion;adrenal cortex;trigeminal ganglion;skeletal muscle; 0.18824 0.14133 -3.179435477 0.44821892 1608.73768 7.42567 DPAGT1 0.00018751828847891 0.896187989209092 0.103624492502429 dolichyl-phosphate N-acetylglucosaminephosphotransferase 1 FUNCTION: Catalyzes the initial step in the synthesis of dolichol- P-P-oligosaccharides.; DISEASE: Congenital disorder of glycosylation 1J (CDG1J) [MIM:608093]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:12872255}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myasthenic syndrome, congenital, 13 (CMS13) [MIM:614750]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness. CMS13 is characterized by muscle weakness mostly affecting proximal limb muscles, minimal involvement of facial, ocular and bulbar muscles, and tubular aggregates present on muscle biopsy. Symptoms include difficulty walking and frequent falls. Younger patients show hypotonia and poor head control. Neurophysiological features indicate a disorder of neuromuscular transmission on electromyography. {ECO:0000269|PubMed:22742743}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.18765 0.21836 0.060756528 58.52795471 503.86292 4.60672 DPCD 0.0027034038456891 0.794849358417712 0.202447237736599 deleted in primary ciliary dyskinesia homolog (mouse) FUNCTION: May play a role in the formation or function of ciliated cells. {ECO:0000269|PubMed:14630615}.; . TISSUE SPECIFICITY: Highly expressed in the testis. Weakly expressed in pancreas, skeletal muscle and heart. Expression increases during ciliated cell differentiation. {ECO:0000269|PubMed:14630615}.; . . . . 0.349177632 74.18023119 33.15909 1.02565 DPCR1 0.140380580992053 0.8401331782522 0.0194862407557472 diffuse panbronchiolitis critical region 1 . . TISSUE SPECIFICITY: Detected in lung, esophagus, stomach, rectum, skin, cervix, testis, kidney, uterus and small intestine. {ECO:0000269|PubMed:12185533}.; pancreas;brain;stomach; . 0.02486 0.04424 2.820592219 99.06227884 2074.37466 8.39231 DPEP1 0.000136492958599163 0.854342419897604 0.145521087143797 dipeptidase 1 (renal) FUNCTION: Hydrolyzes a wide range of dipeptides. Implicated in the renal metabolism of glutathione and its conjugates. Converts leukotriene D4 to leukotriene E4; it may play an important role in the regulation of leukotriene activity.; . . unclassifiable (Anatomical System);medulla oblongata;lymph node;lung;islets of Langerhans;placenta;testis;colon;kidney;stomach; testis - interstitial;pancreas;testis - seminiferous tubule;testis;kidney;atrioventricular node; 0.14863 0.26780 -0.773369631 13.10450578 499.50349 4.58879 DPEP2 4.01062336318903e-05 0.837265383616595 0.162694510149773 dipeptidase 2 FUNCTION: Probable metalloprotease which hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4). {ECO:0000250}.; . . unclassifiable (Anatomical System);umbilical cord;heart;islets of Langerhans;colon;blood;skin;bone marrow;uterus;pancreas;prostate;lung;bone;placenta;alveolus;spleen;germinal center;kidney;brain;mammary gland; white blood cells;whole blood;skeletal muscle; 0.10287 0.11548 -0.178111357 40.44585987 172.96744 2.86359 DPEP3 9.13571963954139e-07 0.521108009215973 0.478891077212064 dipeptidase 3 FUNCTION: Probable metalloprotease which hydrolyzes cystinyl-bis- glycine. May be involved in meiosis (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;medulla oblongata;testis;kidney; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.05011 0.10755 0.15257911 64.60839821 929.8668 5.91573 DPF1 0.988986049504721 0.0110132008740806 7.49621198031407e-07 double PHD fingers 1 FUNCTION: May have an important role in developing neurons by participating in regulation of cell survival, possibly as a neurospecific transcription factor. Belongs to the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);visual apparatus;head and neck;brain;bone marrow; subthalamic nucleus;superior cervical ganglion;medulla oblongata;fetal brain;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.28964 0.10376 -0.315847836 31.68789809 13.71775 0.49728 DPF2 0.999787288487276 0.000212711269129612 2.43594035590972e-10 double PHD fingers 2 FUNCTION: May be a transcription factor required for the apoptosis response following survival factor withdrawal from myeloid cells. Might also have a role in the development and maturation of lymphoid cells.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;uterus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus;cerebellum; testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis; 0.41308 0.13535 -0.449946534 24.00330267 4.43065 0.16082 DPF3 0.828481786371688 0.171486464741366 3.1748886946457e-05 double PHD fingers 3 FUNCTION: Belongs to the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Muscle-specific component of the BAF complex, a multiprotein complex involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Specifically binds acetylated lysines on histone 3 and 4 (H3K14ac, H3K9ac, H4K5ac, H4K8ac, H4K12ac, H4K16ac). In the complex, it acts as a tissue-specific anchor between histone acetylations and methylations and chromatin remodeling. It thereby probably plays an essential role in heart and skeletal muscle development. {ECO:0000250, ECO:0000269|PubMed:18765789}.; . . . . 0.48007 0.11809 -0.53631094 20.53550366 136.59831 2.54057 DPH1 2.34177044084966e-08 0.453945917676163 0.546054058906132 diphthamide biosynthesis 1 FUNCTION: Required for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2). When overexpressed, suppresses colony formation ability and growth rate of ovarian cancer cells. Acts also as a tumor suppressor in lung and breast cancers (By similarity). Plays a role in embryonic growth, organogenesis and postnatal survival (By similarity). {ECO:0000250, ECO:0000269|PubMed:10519411}.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, mammary gland, colon, small intestine, testis and ovary. Reduced expression in primary breast and ovarian tumors. {ECO:0000269|PubMed:10519411, ECO:0000269|PubMed:8616839}.; medulla oblongata;ovary;salivary gland;sympathetic chain;colon;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;oesophagus;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.60203 0.13269 0.398725314 76.35645199 1069.64157 6.27059 DPH2 0.00684674768380938 0.989432058672414 0.00372119364377703 DPH2 homolog FUNCTION: Required for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2). {ECO:0000250}.; . TISSUE SPECIFICITY: Strongly expressed in skeletal muscle. Moderately expressed in heart, small intestine, liver, pancreas, testis and colon. Weakly expressed in brain, placenta, kidney, spleen, thymus, prostate, ovary and lymphocytes. {ECO:0000269|PubMed:9782084}.; medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.06913 0.09017 -0.135838822 43.77211607 48.08951 1.34957 DPH3 0.0446708183979692 0.669055677704183 0.286273503897848 diphthamide biosynthesis 3 FUNCTION: Essential for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in elongation factor 2 (EEF2) and which can be ADP- ribosylated by diphtheria toxin and by Pseudomonas exotoxin A (Eta). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in small intestine, spleen, thymus, heart, liver and lung. {ECO:0000269|PubMed:14527407, ECO:0000269|PubMed:14980502}.; myocardium;ovary;salivary gland;intestine;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;aorta; . 0.40465 0.12971 0.101211609 60.95777306 7.22072 0.27215 DPH3P1 . . . diphthamide biosynthesis 3 pseudogene 1 . . . . . . . . . . . DPH3P2 . . . diphthamide biosynthesis 3 pseudogene 2 . . . . . . . . . . . DPH5 0.00189943547170022 0.904856553709231 0.0932440108190687 diphthamide biosynthesis 5 FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis. {ECO:0000250|UniProtKB:P32469, ECO:0000269|PubMed:23486472}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;appendix;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin;cingulate cortex; 0.54810 0.10207 0.3032669 72.009908 87.8002 2.00115 DPH6 0.00246862782790718 0.929247668220681 0.0682837039514116 diphthamine biosynthesis 6 FUNCTION: Amidase that catalyzes the last step of diphthamide biosynthesis using ammonium and ATP. Diphthamide biosynthesis consists in the conversion of an L-histidine residue in the translation elongation factor (EEF2) to diphthamide (By similarity). {ECO:0000250, ECO:0000269|PubMed:23169644}.; . . . . 0.29600 . 0.681699246 84.93158764 278.48188 3.57635 DPH6-AS1 . . . DPH6 antisense RNA 1 (head to head) . . . . . . . . . . . DPH7 4.37594731994362e-05 0.850719446124892 0.149236794401909 diphthamide biosynthesis 7 FUNCTION: Catalyzes the demethylation of diphthine methyl ester to form diphthine, an intermediate diphthamide biosynthesis, a post- translational modification of histidine which occurs in translation elongation factor 2 (EEF2) which can be ADP- ribosylated by diphtheria toxin and by Pseudomonas exotoxin A (Eta). {ECO:0000250|UniProtKB:P38332, ECO:0000269|PubMed:19965467, ECO:0000269|PubMed:23486472}.; . . . . 0.09077 . 0.242582624 69.45623968 157.31543 2.74124 DPM1 0.536747471706315 0.462588543845081 0.00066398444860427 dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit FUNCTION: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O- mannosylation of proteins; catalytic subunit of the dolichol- phosphate mannose (DPM) synthase complex.; DISEASE: Congenital disorder of glycosylation 1E (CDG1E) [MIM:608799]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. Some CDG1E patients have features consistent with a dystroglycanopathy and congenital muscular dystrophy, including O-mannosylation defect, camptodactyly, elevated creatine kinase, motor delay and dystrophic changes on muscel biopsy. {ECO:0000269|PubMed:10642597, ECO:0000269|PubMed:10642602, ECO:0000269|PubMed:15669674, ECO:0000269|PubMed:23856421}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.48144 0.46642 0.03689118 56.64071715 . . DPM2 0.0198009574006693 0.741157528259661 0.23904151433967 dolichyl-phosphate mannosyltransferase polypeptide 2, regulatory subunit FUNCTION: Regulates the biosynthesis of dolichol phosphate- mannose. Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization and stable expression of DPM1. When associated with the GPI-GlcNAc transferase (GPI-GnT) complex enhances but is not essential for its activity. {ECO:0000269|PubMed:10944123}.; DISEASE: Congenital disorder of glycosylation 1U (CDG1U) [MIM:615042]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. Some CDG1U patients have dystrophic changes seen on muscle biopsy and reduced O-mannosyl glycans on alpha-dystroglycan. {ECO:0000269|PubMed:23109149}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; atrioventricular node; 0.02699 0.07780 0.457594962 78.16112291 14.63837 0.52751 DPM3 0.233470170067034 0.645756523463157 0.120773306469808 dolichyl-phosphate mannosyltransferase subunit 3 FUNCTION: Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit DPM1 to the ER. {ECO:0000269|PubMed:10835346}.; DISEASE: Congenital disorder of glycosylation 1O (CDG1O) [MIM:612937]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. CDG1O patients have increased serum creatine kinase, dystrophic changes on muscle biopsy, and reduced O-mannosylation of alpha-dystroglycan. {ECO:0000269|PubMed:19576565}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);pancreas;smooth muscle;lung;bone;placenta;colon;cervix;blood;brain;skin;stomach;retina; prostate;adrenal gland;thyroid;liver; 0.04771 0.06274 -0.009020804 52.8544468 4.45494 0.16174 DPP3 4.36332090330589e-09 0.939852020912517 0.0601479747241623 dipeptidyl peptidase 3 FUNCTION: Cleaves and degrades of the opioid peptide enkephalin. Also cleaves Arg-Arg-beta-naphthylamide. {ECO:0000269|PubMed:22493238}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;pharynx;blood;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;liver;prefrontal cortex;ciliary ganglion;pons;atrioventricular node;kidney;caudate nucleus;trigeminal ganglion;cingulate cortex;cerebellum; . 0.29988 0.874458024 88.88888889 4443.48457 13.35156 DPP3P1 . . . dipeptidyl peptidase 3 pseudogene 1 . . . . . . . . . . . DPP3P2 . . . dipeptidyl peptidase 3 pseudogene 2 . . . . . . . . . . . DPP4 4.05740539448844e-10 0.98316128842061 0.0168387111736494 dipeptidyl peptidase 4 FUNCTION: Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF- kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. {ECO:0000269|PubMed:10570924, ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:10900005, ECO:0000269|PubMed:10951221, ECO:0000269|PubMed:11772392, ECO:0000269|PubMed:14691230, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17287217, ECO:0000269|PubMed:17549790, ECO:0000269|PubMed:18708048}.; . TISSUE SPECIFICITY: Expressed specifically in lymphatic vessels but not in blood vessels in the skin, small intestine, esophagus, ovary, breast and prostate glands. Not detected in lymphatic vessels in the lung, kidney, uterus, liver and stomach (at protein level). Expressed in the poorly differentiated crypt cells of the small intestine as well as in the mature villous cells. Expressed at very low levels in the colon. {ECO:0000269|PubMed:1677636, ECO:0000269|PubMed:18708048}.; smooth muscle;ovary;colon;parathyroid;vein;skin;uterus;prostate;whole body;endometrium;thyroid;bone;testis;amniotic fluid;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;skeletal muscle;lung;adrenal gland;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;smooth muscle;skeletal muscle; 0.31053 0.64989 -0.973616687 8.8995046 165.27236 2.81237 DPP6 0.96769110706309 0.032308875100511 1.7836398758489e-08 dipeptidyl peptidase like 6 FUNCTION: Promotes cell surface expression of the potassium channel KCND2 (PubMed:15454437, PubMed:19441798). Modulates the activity and gating characteristics of the potassium channel KCND2 (PubMed:18364354). Has no dipeptidyl aminopeptidase activity (PubMed:8103397, PubMed:15476821). {ECO:0000269|PubMed:15454437, ECO:0000269|PubMed:18364354, ECO:0000269|PubMed:8103397, ECO:0000305|PubMed:15476821}.; DISEASE: Familial paroxysmal ventricular fibrillation 2 (VF2) [MIM:612956]: A cardiac arrhythmia marked by fibrillary contractions of the ventricular muscle due to rapid repetitive excitation of myocardial fibers without coordinated contraction of the ventricle and by absence of atrial activity. {ECO:0000269|PubMed:19285295}. Note=The disease is caused by mutations affecting the gene represented in this entry. A genetic variation 340 bases upstream from the ATG start site of the DPP6 gene is the cause of familial paroxysmal ventricular fibrillation type 2.; DISEASE: Mental retardation, autosomal dominant 33 (MRD33) [MIM:616311]: A form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD33 patients manifest microcephaly and intellectual disability. {ECO:0000269|PubMed:23832105}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly in brain.; unclassifiable (Anatomical System);uterus;heart;visual apparatus;brain;skin; amygdala;whole brain;dorsal root ganglion;occipital lobe;medulla oblongata;thalamus;superior cervical ganglion;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.12322 0.12460 . . 1053.66513 6.23311 DPP7 2.02498204002921e-15 0.00393425904212887 0.996065740957869 dipeptidyl peptidase 7 FUNCTION: Plays an important role in the degradation of some oligopeptides. {ECO:0000269|PubMed:15487984}.; . TISSUE SPECIFICITY: Detected in seminal plasma (at protein level). {ECO:0000269|PubMed:15487984}.; . . 0.12150 . 0.246221394 69.56829441 352.55256 3.97729 DPP8 0.999271312821212 0.000728687138254098 4.05343723797431e-11 dipeptidyl peptidase 8 FUNCTION: Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. May play a role in T-cell activation and immune function. {ECO:0000269|PubMed:11012666}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in testis, placenta, prostate, muscle and brain. {ECO:0000269|PubMed:11012666, ECO:0000269|PubMed:12662155}.; ovary;salivary gland;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;head and neck;cervix;kidney;stomach; amygdala;dorsal root ganglion;occipital lobe;medulla oblongata;superior cervical ganglion;testis - interstitial;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.25827 0.21386 -0.775187015 13.05142722 73.66646 1.79357 DPP9 0.999114700689224 0.000885298988834889 3.21941114709575e-10 dipeptidyl peptidase 9 FUNCTION: Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in liver, heart and muscle, and lowest levels in brain. {ECO:0000269|PubMed:12459266, ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:15245913}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.38871 0.17929 -0.795417163 12.5324369 212.24455 3.14241 DPP9-AS1 . . . DPP9 antisense RNA 1 . . . . . . . . . . . DPP10 0.99998928551057 1.07144893960554e-05 3.39912349980731e-14 dipeptidyl peptidase like 10 FUNCTION: Promotes cell surface expression of the potassium channel KCND2 (PubMed:15454437). Modulates the activity and gating characteristics of the potassium channel KCND2 (PubMed:15454437). Has no dipeptidyl aminopeptidase activity (PubMed:12662155). {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:15454437, ECO:0000269|PubMed:15671030}.; DISEASE: Asthma (ASTHMA) [MIM:600807]: The most common chronic disease affecting children and young adults. It is a complex genetic disorder with a heterogeneous phenotype, largely attributed to the interactions among many genes and between these genes and the environment. It is characterized by recurrent attacks of paroxysmal dyspnea, with wheezing due to spasmodic contraction of the bronchi. {ECO:0000269|PubMed:14566338, ECO:0000269|PubMed:19237393}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in serum, T-cells and brain (at protein level). Expressed in brain, pancreas, spinal cord and adrenal glands. {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:14566338}.; unclassifiable (Anatomical System);uterus;lung;frontal lobe;hypothalamus;visual apparatus;testis;colon;kidney;brain; globus pallidus;ciliary ganglion; 0.36675 0.14962 0.382138899 75.65463553 784.31527 5.53417 DPP10-AS1 . . . DPP10 antisense RNA 1 . . . . . . . . . . . DPP10-AS2 . . . DPP10 antisense RNA 2 . . . . . . . . . . . DPP10-AS3 . . . DPP10 antisense RNA 3 . . . . . . . . . . . DPPA2 7.75895224134516e-08 0.153863569752368 0.84613635265811 developmental pluripotency associated 2 FUNCTION: Binds to target gene promoters, including NKX2-5 and SYCE1, but not GATA4, and may be involved in the maintenance of the active epigenetic status of these genes. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in embryonic stem cells. No expression is seen in 5 months embryo, mesenchymal stem cells, embryonic fibrocytes and adult tissues. {ECO:0000269|PubMed:15583978}.; . . 0.06840 0.08803 0.305084559 72.22811984 134.6296 2.52228 DPPA2P1 . . . developmental pluripotency associated 2 pseudogene 1 . . . . . . . . . . . DPPA2P2 . . . developmental pluripotency associated 2 pseudogene 2 . . . . . . . . . . . DPPA2P3 . . . developmental pluripotency associated 2 pseudogene 3 . . . . . . . . . . . DPPA2P4 . . . developmental pluripotency associated 2 pseudogene 4 . . . . . . . . . . . DPPA3 0.165194336334944 0.772640391263547 0.0621652724015096 developmental pluripotency associated 3 FUNCTION: Primordial germ cell (PGCs)-specific protein involved in epigenetic chromatin reprogramming in the zygote following fertilization. In zygotes, DNA demethylation occurs selectively in the paternal pronucleus before the first cell division, while the adjacent maternal pronucleus and certain paternally-imprinted loci are protected from this process. Participates in protection of DNA methylation in the maternal pronucleus by preventing conversion of 5mC to 5hmC: specifically recognizes and binds histone H3 dimethylated at 'Lys-9' (H3K9me2) on maternal genome, and protects maternal genome from TET3-mediated conversion to 5hmC and subsequent DNA demethylation. Does not bind paternal chromatin, which is mainly packed into protamine and does not contain much H3K9me2 mark. Also protects imprinted loci that are marked with H3K9me2 in mature sperm from DNA demethylation in early embryogenesis. May be important for the totipotent/pluripotent states continuing through preimplantation development. Also involved in chromatin condensation in oocytogenesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Low expression in testis, ovary and thymus. Expressed in embryonic stem and carcinoma cells. Highly expressed in testicular germ cell tumors. {ECO:0000269|PubMed:14654002, ECO:0000269|PubMed:14684992, ECO:0000269|PubMed:14990856}.; unclassifiable (Anatomical System);testis; . 0.02429 0.07229 0.591694063 82.45458835 39.72884 1.17090 DPPA3P1 . . . developmental pluripotency associated 3 pseudogene 1 . . . . . . . . . . . DPPA3P2 . . . developmental pluripotency associated 3 pseudogene 2 . . . . . . . . . . . DPPA3P3 . . . developmental pluripotency associated 3 pseudogene 3 . . . . . . . . . . . DPPA4 0.0016014612995864 0.885407957852632 0.112990580847781 developmental pluripotency associated 4 FUNCTION: May be involved in the maintenance of active epigenetic status of target genes. May inhibit differentiation of embryonic cells into a primitive ectoderm lineage. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;skin;uterus;lung;epididymis;placenta;liver;testis;spleen;brain;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.36315 0.06198 0.104848986 61.49445624 122.76044 2.41332 DPPA4P1 . . . developmental pluripotency associated 4 pseudogene 1 . . . . . . . . . . . DPPA5 0.000949315393546459 0.578856816311265 0.420193868295189 developmental pluripotency associated 5 FUNCTION: Involved in the maintenance of embryonic stem (ES) cell pluripotency. Dispensable for self-renewal of pluripotent ES cells and establishment of germ cells. Associates with specific target mRNAs (By similarity). {ECO:0000250}.; . . . . 0.12265 0.10351 0.257356108 69.83368719 6.81457 0.25210 DPPA5P1 . . . developmental pluripotency associated 5 pseudogene 1 . . . . . . . . . . . DPPA5P2 . . . developmental pluripotency associated 5 pseudogene 2 . . . . . . . . . . . DPPA5P3 . . . developmental pluripotency associated 5 pseudogene 3 . . . . . . . . . . . DPPA5P4 . . . developmental pluripotency associated 5 pseudogene 4 . . . . . . . . . . . DPRX 1.14132203135122e-06 0.19776259994515 0.802236258732819 divergent-paired related homeobox FUNCTION: Putative transcription factor. {ECO:0000250}.; . . . . 0.03378 . 0.016664174 55.21939137 178.24736 2.90240 DPRXP1 . . . divergent-paired related homeobox pseudogene 1 . . . . . . . . . . . DPRXP2 . . . divergent-paired related homeobox pseudogene 2 . . . . . . . . . . . DPRXP3 . . . divergent-paired related homeobox pseudogene 3 . . . . . . . . . . . DPRXP4 . . . divergent-paired related homeobox pseudogene 4 . . . . . . . . . . . DPRXP5 . . . divergent-paired related homeobox pseudogene 5 . . . . . . . . . . . DPRXP6 . . . divergent-paired related homeobox pseudogene 6 . . . . . . . . . . . DPRXP7 . . . divergent-paired related homeobox pseudogene 7 . . . . . . . . . . . DPT 9.10510156884477e-05 0.553372302316068 0.446536646668243 dermatopontin FUNCTION: Seems to mediate adhesion by cell surface integrin binding. May serve as a communication link between the dermal fibroblast cell surface and its extracellular matrix environment. Enhances TGFB1 activity. Inhibits cell proliferation. Accelerates collagen fibril formation, and stabilizes collagen fibrils against low-temperature dissociation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in fibroblasts, heart, skeletal muscle, brain and pancreas. Expressed at an intermediate level in lung and kidney, and at a low level in liver and placenta. Expressed at a lower level in fibroblasts from hypertrophic scar lesional skin and in fibroblasts from patients with systemic sclerosis than in normal skin fibroblasts. {ECO:0000269|PubMed:10233760, ECO:0000269|PubMed:8104875}.; . . 0.13571 0.20005 0.68351529 85.03774475 284.24232 3.60936 DPY19L1 0.142871737069563 0.857094822690348 3.34402400880943e-05 dpy-19 like 1 (C. elegans) FUNCTION: Probable C-mannosyltransferase that mediates C- mannosylation of tryptophan residues on target proteins. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16526957}.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;stomach;thymus; subthalamic nucleus;superior cervical ganglion;globus pallidus;parietal lobe; 0.22929 . -0.404032746 26.53338051 2009.33576 8.25199 DPY19L1P1 . . . DPY19L1 pseudogene 1 . . . . . . . . . . . DPY19L1P2 . . . DPY19L1 pseudogene 2 . . . . . . . . . . . DPY19L2 7.02940400276182e-05 0.99900380686087 0.000925899099102138 dpy-19 like 2 (C. elegans) FUNCTION: Probable C-mannosyltransferase that mediates C- mannosylation of tryptophan residues on target proteins (By similarity). Required during spermatogenesis for sperm head elongation and acrosome formation. {ECO:0000250, ECO:0000269|PubMed:21397063, ECO:0000269|PubMed:21397064}.; . TISSUE SPECIFICITY: Widely expressed with high expression in testis. Not detectable in ejaculated sperm (at protein level). {ECO:0000269|PubMed:16526957, ECO:0000269|PubMed:21397064}.; unclassifiable (Anatomical System);myocardium;medulla oblongata;smooth muscle;heart;ovary;islets of Langerhans;parathyroid;skin;skeletal muscle;uterus;whole body;lung;cochlea;endometrium;bone;placenta;liver;testis;spleen;kidney;brain;peripheral nerve; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;cingulate cortex; 0.10850 . 1.354051915 94.39726351 4007.99241 12.53898 DPY19L2P1 . . . DPY19L2 pseudogene 1 FUNCTION: Probable C-mannosyltransferase that mediates C- mannosylation of tryptophan residues on target proteins. {ECO:0000250}.; . TISSUE SPECIFICITY: Brain, heart, placenta and testis. {ECO:0000269|PubMed:16526957}.; . . 0.01555 . . . . . DPY19L2P2 . . . DPY19L2 pseudogene 2 FUNCTION: Probable C-mannosyltransferase that mediates C- mannosylation of tryptophan residues on target proteins. {ECO:0000250}.; . TISSUE SPECIFICITY: Fibroblast, lung, lymphoblast, spleen and testis. {ECO:0000269|PubMed:16526957}.; unclassifiable (Anatomical System);myocardium;smooth muscle;ovary;islets of Langerhans;skeletal muscle;skin;uterus;liver;testis;spleen;brain;peripheral nerve; . 0.13982 . . . . . DPY19L2P3 . . . DPY19L2 pseudogene 3 . . . . . . . . . . . DPY19L2P4 . . . DPY19L2 pseudogene 4 . . . . . . . . . . . DPY19L2P5 . . . DPY19L2 pseudogene 5 . . . . . . . . . . . DPY19L3 0.0800404724813009 0.919941055103366 1.84724153332331e-05 dpy-19 like 3 (C. elegans) FUNCTION: Probable C-mannosyltransferase that mediates C- mannosylation of tryptophan residues on target proteins. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16526957}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;urinary;adrenal cortex;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.09022 0.06578 -0.664951379 15.91177164 69.40023 1.72795 DPY19L4 1.51116557898014e-15 0.15819441935715 0.841805580642849 dpy-19 like 4 (C. elegans) FUNCTION: Probable C-mannosyltransferase that mediates C- mannosylation of tryptophan residues on target proteins. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16526957}.; . . 0.17373 0.08478 0.312359769 72.71172446 304.07084 3.71567 DPY30 0.451358336289617 0.52087302406641 0.0277686396439727 dpy-30, histone methyltransferase complex regulatory subunit FUNCTION: As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport. {ECO:0000269|PubMed:19556245, ECO:0000269|PubMed:19651892, ECO:0000269|PubMed:21335234}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;bone;testis;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;heart;islets of Langerhans;hypothalamus;spinal cord;muscle;pharynx;blood;skeletal muscle;bile duct;breast;pia mater;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;medulla oblongata;pons;trigeminal ganglion;cingulate cortex; 0.45630 0.12971 0.057118534 57.99716914 1.11171 0.02986 DPYD 4.18972244079049e-09 0.996985954159169 0.00301404165110853 dihydropyrimidine dehydrogenase FUNCTION: Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil.; . TISSUE SPECIFICITY: Found in most tissues with greatest activity found in liver and peripheral blood mononuclear cells.; unclassifiable (Anatomical System);uterus;lymph node;larynx;bone;placenta;liver;duodenum;head and neck;brain;bone marrow; fetal liver; 0.29965 0.38628 1.431149089 95.02241095 1997.46528 8.23273 DPYD-AS1 . . . DPYD antisense RNA 1 . . . . . . . . . . . DPYD-AS2 . . . DPYD antisense RNA 2 . . . . . . . . . . . DPYD-IT1 . . . DPYD intronic transcript 1 . . . . . . . . . . . DPYS 9.89625849678714e-08 0.521739109867602 0.478260791169813 dihydropyrimidinase FUNCTION: Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyze the ring opening of 5,6- dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate.; DISEASE: Dihydropyrimidinase deficiency (DPYSD) [MIM:222748]: An autosomal recessive disorder of pyrimidine metabolism characterized by dihydropyrimidinuria. It is associated with a variable clinical phenotype characterized by epileptic or convulsive attacks, dysmorphic features and severe developmental delay, and congenital microvillous atrophy. Most patients are, however, asymptomatic. {ECO:0000269|PubMed:9718352}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver and kidney.; unclassifiable (Anatomical System);lung;liver;spleen;kidney; fetal liver;superior cervical ganglion;liver;kidney; 0.14479 0.30292 -1.043396569 7.71408351 332.05523 3.87475 DPYSL2 0.995558288769102 0.00444162993082648 8.13000713854268e-08 dihydropyrimidinase like 2 FUNCTION: Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis. {ECO:0000269|PubMed:11477421, ECO:0000269|PubMed:15466863, ECO:0000269|PubMed:20801876}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;spinal cord;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.54792 0.54626 -0.756778259 13.44656759 125.03577 2.43271 DPYSL3 0.996483173643699 0.00351659917110604 2.27185195380906e-07 dihydropyrimidinase like 3 FUNCTION: Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Mainly expressed in heart and skeletal muscle. Also strongly expressed in fetal brain and spinal cord.; lymphoreticular;myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;tongue;islets of Langerhans;urinary;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;amygdala;superior cervical ganglion;fetal brain;hypothalamus;spinal cord;ciliary ganglion;caudate nucleus;trigeminal ganglion; 0.89066 0.14682 -0.358119787 29.16371786 99.15207 2.15522 DPYSL4 5.85788198919438e-06 0.969490270920616 0.0305038711973945 dihydropyrimidinase like 4 FUNCTION: Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity). {ECO:0000250}.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;adrenal cortex;lens;lung;placenta;visual apparatus;macula lutea;liver;spleen;mammary gland; whole brain;amygdala;medulla oblongata;superior cervical ganglion;fetal brain;temporal lobe;prefrontal cortex;pons;parietal lobe;cingulate cortex;skeletal muscle; 0.23393 0.12567 -1.50462206 3.568058504 305.19911 3.71985 DPYSL5 0.998332100766402 0.00166786241167032 3.68219272991883e-08 dihydropyrimidinase like 5 FUNCTION: May have a function in neuronal differentiation and/or axon growth.; . . unclassifiable (Anatomical System);lung;frontal lobe;visual apparatus;colon;blood;brain;retina;bone marrow; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.70946 0.11809 -0.490397599 22.50530786 155.45494 2.72458 DQX1 7.46878481629986e-15 0.11170530393139 0.888294696068602 DEAQ-box RNA dependent ATPase 1 . . . . . 0.22563 0.08530 -0.178111357 40.44585987 310.98066 3.75345 DR1 0.835491729483673 0.161249260194996 0.00325901032133149 down-regulator of transcription 1 FUNCTION: The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. {ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:8670811}.; . . . . 0.35009 0.17821 0.3455435 73.78509082 53.62913 1.45848 DRAIC . . . downregulated RNA in cancer, inhibitor of cell invasion and migration . . . . . . . . . . . DRAM1 0.0807000769340284 0.872050796368938 0.0472491266970341 DNA damage regulated autophagy modulator 1 FUNCTION: Lysosomal modulator of autophagy that plays a central role in p53/TP53-mediated apoptosis. Not involved in p73/TP73- mediated autophagy. {ECO:0000269|PubMed:16839881, ECO:0000269|PubMed:17304243}.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; . . -0.229483771 36.86010852 8.7844 0.32424 DRAM2 0.00139586626243694 0.867612463906653 0.13099166983091 DNA damage regulated autophagy modulator 2 FUNCTION: Plays a role in the initiation of autophagy. In the retina, might be involved in the process of photoreceptor cells renewal and recycling to preserve visual function. Induces apoptotic cell death when coexpressed with DRAM1. {ECO:0000269|PubMed:19895784, ECO:0000269|PubMed:25983245}.; . TISSUE SPECIFICITY: Expression is down-regulated in ovarian tumors (at protein level). Widely expressed with highest levels in placenta and heart. Expressed in the retina. Not detected in brain or thymus. {ECO:0000269|PubMed:19556885, ECO:0000269|PubMed:19895784, ECO:0000269|PubMed:25983245}.; lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; atrioventricular node;trigeminal ganglion; 0.10562 0.09329 -0.183570861 39.95046001 44.80454 1.28253 DRAP1 0.215306249804435 0.745715912806949 0.0389778373886165 DR1 associated protein 1 FUNCTION: The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own. {ECO:0000269|PubMed:8608938, ECO:0000269|PubMed:8670811}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in adult testis, heart, skeletal muscle, pancreas and brain, and in fetal brain, liver and kidney. {ECO:0000269|PubMed:8608938, ECO:0000269|PubMed:8670811}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;thyroid;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;oesophagus;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach;cerebellum; whole brain;testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;temporal lobe;testis; 0.26498 0.11070 -0.383807564 27.41802312 31.39483 0.98952 DRAXIN 6.64368474068458e-10 0.0364258429675605 0.963574156368071 dorsal inhibitory axon guidance protein FUNCTION: Chemorepulsive axon guidance protein required for the development of spinal cord and forebrain commissures. Acts as a chemorepulsive guidance protein for commissural axons during development. Able to inhibit or repel neurite outgrowth from dorsal spinal cord. Inhibits the stabilization of cytosolic beta- catenin (CTNNB1) via its interaction with LRP6, thereby acting as an antagonist of Wnt signaling pathway. {ECO:0000255|HAMAP- Rule:MF_03060}.; . . . . 0.15303 0.10234 1.219937511 93.19414956 1036.5412 6.18211 DRAXINP1 . . . dorsal inhibitory axon guidance protein pseudogene 1 . . . . . . . . . . . DRC1 1.30453003302834e-10 0.767685318083452 0.232314681786095 dynein regulatory complex subunit 1 FUNCTION: Key component of the nexin-dynein regulatory complex (N- DRC), essential for N-DRC integrity. Required for the assembly and regulation of specific classes of inner dynein arm motors. May also function to restrict dynein-driven microtubule sliding, thus aiding in the generation of ciliary bending. {ECO:0000269|PubMed:23354437}.; DISEASE: Ciliary dyskinesia, primary, 21 (CILD21) [MIM:615294]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia. Patients may exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:23354437, ECO:0000269|PubMed:25186273}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.08328 . 0.896505334 89.30761972 4608.92048 13.62929 DRC3 . . . dynein regulatory complex subunit 3 FUNCTION: Key component of the nexin-dynein regulatory complex (N- DRC), a key regulator of ciliary motility. {ECO:0000250|UniProtKB:A8IVX2}.; . . . . 0.10823 . 0.556689353 81.63481953 . . DRC7 . . . dynein regulatory complex subunit 7 FUNCTION: Key component of the nexin-dynein regulatory complex (N- DRC), essential for N-DRC integrity. Involved in the regulation of flagellar motility. {ECO:0000250|UniProtKB:A8JAM0}.; . . . . 0.23416 0.10344 0.723780906 85.87520642 . . DRD1 0.896431549924012 0.102589410586154 0.000979039489833952 dopamine receptor D1 FUNCTION: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.; . TISSUE SPECIFICITY: Detected in caudate, nucleus accumbens and in the olfactory tubercle. {ECO:0000269|PubMed:2144334}.; islets of Langerhans;macula lutea;fovea centralis; superior cervical ganglion;prefrontal cortex;globus pallidus;atrioventricular node;caudate nucleus;skin; 0.22847 0.30148 -0.404032746 26.53338051 30.11978 0.96089 DRD2 0.733263888671177 0.266190452794248 0.000545658534574978 dopamine receptor D2 FUNCTION: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. {ECO:0000269|PubMed:21645528}.; . . unclassifiable (Anatomical System);sympathetic chain;muscle;colon;choroid;fovea centralis;lens;retina;pancreas;lung;optic nerve;macula lutea;pituitary gland;brain; dorsal root ganglion;medulla oblongata;superior cervical ganglion;spinal cord;ciliary ganglion;caudate nucleus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.18972 0.72427 -0.600630256 18.06440198 247.18312 3.39065 DRD3 0.0102953433153304 0.944520016879353 0.0451846398053162 dopamine receptor D3 FUNCTION: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Promotes cell proliferation. {ECO:0000269|PubMed:19520868}.; DISEASE: Tremor, hereditary essential 1 (ETM1) [MIM:190300]: A common movement disorder mainly characterized by postural tremor of the arms. Head, legs, trunk, voice, jaw, and facial muscles also may be involved. The condition can be aggravated by emotions, hunger, fatigue and temperature extremes, and may cause a functional disability or even incapacitation. Inheritance is autosomal dominant. {ECO:0000269|PubMed:16650084, ECO:0000269|PubMed:16809426}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Brain.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;uterus corpus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21922 0.36101 -0.358119787 29.16371786 55.45707 1.49561 DRD4 7.58378913666363e-06 0.165303717100163 0.834688699110701 dopamine receptor D4 FUNCTION: Dopamine receptor responsible for neuronal signaling in the mesolimbic system of the brain, an area of the brain that regulates emotion and complex behavior. Its activity is mediated by G proteins which inhibit adenylyl cyclase. Modulates the circadian rhythm of contrast sensitivity by regulating the rhythmic expression of NPAS2 in the retinal ganglion cells (By similarity). {ECO:0000250}.; . . optic nerve;ovary;macula lutea;fovea centralis;choroid;kidney;lens;retina; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12431 0.39932 . . 1176.96356 6.51838 DRD5 2.52172129080646e-14 0.000655682425695765 0.999344317574279 dopamine receptor D5 FUNCTION: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase. {ECO:0000269|PubMed:1834671}.; . TISSUE SPECIFICITY: Neuron-specific, localized primarily within limbic regions of the brain. {ECO:0000269|PubMed:1834671}.; unclassifiable (Anatomical System);optic nerve;ovary;macula lutea;fovea centralis;choroid;lens;retina; dorsal root ganglion;superior cervical ganglion;medulla oblongata;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.08041 0.21802 0.374860183 75.43052607 215.45171 3.16721 DRD5P1 . . . dopamine receptor D5 pseudogene 1 . . . . . 0.13040 . . . . . DRD5P2 . . . dopamine receptor D5 pseudogene 2 . . . . . 0.14181 . . . . . DRG1 0.953443602675955 0.0465299700059471 2.64273180975346e-05 developmentally regulated GTP binding protein 1 FUNCTION: Critical regulator of cell growth under specific conditions. Implicated in differentiation and cell cycle arrest.; . TISSUE SPECIFICITY: High levels in skeletal muscle, heart, and kidney. Intermediate levels in liver, placenta and brain. Low levels in colon, thymus, spleen, small intestine, lung and leukocytes. {ECO:0000269|PubMed:10760581}.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;bladder;brain;heart;nervous;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;bile duct;lung;nasopharynx;placenta;hippocampus;kidney;stomach;cerebellum; testis - interstitial;testis - seminiferous tubule;testis;cingulate cortex;skeletal muscle; 0.72657 0.11262 -0.185391282 39.67916962 4.83001 0.17791 DRG2 0.148077281811429 0.851159901275145 0.000762816913425935 developmentally regulated GTP binding protein 2 FUNCTION: May play a role in cell proliferation, differentiation and death.; . TISSUE SPECIFICITY: Highest levels in skeletal muscle, heart and kidney. Low levels in colon, thymus, spleen, small intestine, lung and Leukocytes.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; . 0.20284 0.12287 0.194852702 67.03231894 107.35174 2.24849 DRGX 0.252322869969299 0.719254217135676 0.0284229128950257 dorsal root ganglia homeobox FUNCTION: Transcription factor required for the formation of correct projections from nociceptive sensory neurons to the dorsal horn of the spinal cord and normal perception of pain. {ECO:0000250}.; . . . . 0.95664 . -0.0274281 51.65723048 57.22958 1.52359 DRICH1 . . . aspartate-rich 1 . . . . . . . 1.282454727 93.71313989 . . DROSHA 0.99639964840206 0.0036003515979127 2.76850027797028e-14 drosha ribonuclease III FUNCTION: Ribonuclease III double-stranded (ds) RNA-specific endoribonuclease that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DROSHA cleaves the 3' and 5' strands of a stem-loop in pri-miRNAs (processing center 11 bp from the dsRNA- ssRNA junction) to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. Involved also in pre-rRNA processing. Cleaves double- strand RNA and does not cleave single-strand RNA. Involved in the formation of GW bodies. {ECO:0000269|PubMed:10948199, ECO:0000269|PubMed:14508493, ECO:0000269|PubMed:15531877, ECO:0000269|PubMed:15565168, ECO:0000269|PubMed:15574589, ECO:0000269|PubMed:15589161, ECO:0000269|PubMed:16751099, ECO:0000269|PubMed:16906129, ECO:0000269|PubMed:17159994}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10948199}.; lymphoreticular;ovary;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pineal body;urinary;blood;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.60911 0.25509 -0.461076406 23.66124086 2101.94263 8.44322 DRP2 0.00940021508163857 0.990502876315032 9.69086033298469e-05 dystrophin related protein 2 FUNCTION: Required for normal myelination and for normal organization of the cytoplasm and the formation of Cajal bands in myelinating Schwann cells. Required for normal PRX location at appositions between the abaxonal surface of the myelin sheath and the Schwann cell plasma membrane. Possibly involved in membrane- cytoskeleton interactions of the central nervous system. {ECO:0000250, ECO:0000250|UniProtKB:Q05AA6}.; . TISSUE SPECIFICITY: Detected in fetal brain. {ECO:0000269|PubMed:8640231}.; . . 0.57194 0.11419 -0.464712395 23.5727766 523.76759 4.66808 DSC1 4.38539889001518e-08 0.987788201526495 0.0122117546195166 desmocollin 1 FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms. Linked to the keratinization of epithelial tissues.; . TISSUE SPECIFICITY: Strongly expressed in epidermis, less in lymph node and tongue.; unclassifiable (Anatomical System);heart;hypothalamus;colon;skin;retina; dorsal root ganglion;superior cervical ganglion;skin; 0.35051 0.11664 0.762397607 86.8542109 2118.91351 8.47436 DSC2 0.000683301516097171 0.998454435502736 0.000862262981166764 desmocollin 2 FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms.; DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 11 (ARVD11) [MIM:610476]: A congenital heart disease characterized by infiltration of adipose and fibrous tissue into the right ventricle and loss of myocardial cells, resulting in ventricular and supraventricular arrhythmias. {ECO:0000269|PubMed:17033975, ECO:0000269|PubMed:19863551, ECO:0000269|PubMed:21062920}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in epithelia, myocardium and lymph nodes.; ovary;colon;parathyroid;uterus;prostate;endometrium;thyroid;brain;bladder;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;oral cavity;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;duodenum;hypopharynx;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;prostate;superior cervical ganglion;tongue;testis;trigeminal ganglion;skeletal muscle; 0.50770 0.14810 -1.216154 5.667610285 1478.45895 7.16137 DSC3 5.45072408048126e-20 0.000786563147811693 0.999213436852188 desmocollin 3 FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms.; DISEASE: Hypotrichosis and recurrent skin vesicles (HRSV) [MIM:613102]: A disorder characterized by hypotrichosis and the appearance of recurrent skin vesicle formation. Affected individuals show sparse and fragile hair on scalp, as well as absent eyebrows and eyelashes. Vesicles filled with thin, watery fluid are observed on the scalp and skin of most of the body. Mucosal vesicles are absent. {ECO:0000269|PubMed:19765682}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Epidermis, buccal mucosa, esophagus and cervix.; unclassifiable (Anatomical System);breast;heart;larynx;thyroid;placenta;duodenum;cervix;head and neck;skin; superior cervical ganglion;tongue;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.18504 0.08220 0.297596326 71.67964142 2012.65614 8.25942 DSCAM 0.99999999983846 1.61539536423789e-10 1.23775129409144e-26 Down syndrome cell adhesion molecule FUNCTION: Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Mediates within retinal amacrine and ganglion cell subtypes both isoneuronal self-avoidance for creating an orderly dendritic arborization and heteroneuronal self-avoidance to maintain the mosaic spacing between amacrine and ganglion cell bodies (PubMed:10925149). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC. In spinal chord development plays a role in guiding commissural axons projection and pathfinding across the ventral midline to reach the floor plate upon ligand binding (PubMed:18585357, PubMed:19196994). Enhances netrin-induced phosphorylation of PAK1 and FYN (PubMed:15169762). Mediates intracellular signaling by stimulating the activation of MAPK8 and MAP kinase p38 (PubMed:18585357, PubMed:19196994). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity). {ECO:0000250|UniProtKB:F1NY98, ECO:0000269|PubMed:10925149, ECO:0000269|PubMed:15169762, ECO:0000269|PubMed:18585357, ECO:0000269|PubMed:19196994}.; . TISSUE SPECIFICITY: Primarily expressed in brain.; . . 0.15662 0.10818 -3.289804051 0.430526067 213.32232 3.15158 DSCAM-AS1 . . . DSCAM antisense RNA 1 . . . . . . . . . . . DSCAM-IT1 . . . DSCAM intronic transcript 1 . . . . . . . . . . . DSCAML1 0.999999092176902 9.07823098512181e-07 1.39505068135052e-19 Down syndrome cell adhesion molecule like 1 FUNCTION: Cell adhesion molecule that plays a role in neuronal self-avoidance (PubMed:11453658). Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Promotes both isoneuronal self-avoidance for creating an orderly neurite arborization in retinal rod bipolar cells and heteroneuronal self-avoidance to maintain mosaic spacing between AII amacrine cells (By similarity). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity). {ECO:0000250|UniProtKB:E1C8P7, ECO:0000250|UniProtKB:Q4VA61, ECO:0000269|PubMed:11453658}.; . TISSUE SPECIFICITY: Detected in heart, liver, pancreas, skeletal muscle, kidney and in brain, in particular in the amygdala, caudate nucleus, corpus callosum, hippocampus, substantia nigra, thalamus and subthalamus. {ECO:0000269|PubMed:11453658, ECO:0000269|PubMed:12051741}.; unclassifiable (Anatomical System);islets of Langerhans;fovea centralis;choroid;lens;retina;optic nerve;lung;frontal lobe;macula lutea;visual apparatus;liver;pituitary gland;kidney;mammary gland;brain; subthalamic nucleus;medulla oblongata;superior cervical ganglion;caudate nucleus;skeletal muscle;cingulate cortex;parietal lobe; 0.37119 0.10468 -4.215605034 0.147440434 3718.21654 11.90265 DSCAS . . . DSC1/DSC2 antisense RNA . . . . . . . . . . . DSCC1 0.0227186261604573 0.962112287615065 0.0151690862244777 DNA replication and sister chromatid cohesion 1 FUNCTION: Loads PCNA onto primed templates regulating velocity, spacing and restart activity of replication forks. May couple DNA replication to sister chromatid cohesion through regulation of the acetylation of the cohesin subunit SMC3. {ECO:0000269|PubMed:12766176, ECO:0000269|PubMed:19907496}.; . . unclassifiable (Anatomical System);ovary;colon;retina;bone marrow;uterus;pancreas;prostate;lung;endometrium;placenta;visual apparatus;liver;testis;cervix;spleen;germinal center;kidney;brain;mammary gland;stomach;cerebellum; superior cervical ganglion; 0.79771 0.12766 -0.0274281 51.65723048 70.03356 1.73656 DSCR3 0.50591897208566 0.489971529122825 0.00410949879151493 DSCR3 arrestin fold containing . . TISSUE SPECIFICITY: Ubiquitously expressed.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;lung;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; superior cervical ganglion;white blood cells;trigeminal ganglion; 0.14303 0.12016 -0.26993514 34.59542345 28.95913 0.92530 DSCR4 0.00131700519306661 0.416518143563007 0.582164851243927 Down syndrome critical region 4 . . TISSUE SPECIFICITY: Mainly expressed in placenta.; . . 0.04709 . . . 38.01909 1.12894 DSCR4-IT1 . . . DSCR4 intronic transcript 1 . . . . . . . . . . . DSCR8 . . . Down syndrome critical region 8 . . TISSUE SPECIFICITY: Expressed in numerous tissues; not found in breast, heart, small intestine and liver.; unclassifiable (Anatomical System); superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; 0.17221 0.11691 . . 302.72063 3.70575 DSCR9 . . . Down syndrome critical region 9 (non-protein coding) . . TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12168953}.; . . . . . . . . DSCR10 . . . Down syndrome critical region 10 (non-protein coding) . . TISSUE SPECIFICITY: Expressed in placenta and testis. {ECO:0000269|PubMed:12168953}.; . . . . . . . . DSE 0.385415297078461 0.614497351370299 8.73515512403393e-05 dermatan sulfate epimerase FUNCTION: Converts D-glucuronic acid to L-iduronic acid (IdoUA) residues. {ECO:0000269|PubMed:16505484}.; . TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in kidney and ovary and lower expression in brain, colon and thymus. Also expressed in renal cell carcinomas, brain tumors, and in a part of melanomas and adenocarcinomas from organs other than the breast. Expressed in squamous cell carcinomas (SCC), glioma, and some adenocarcinoma cell lines, but not in breast cancer cell lines or any normal tissues (at protein level). {ECO:0000269|PubMed:10679095}.; ovary;developmental;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;thyroid;testis;amniotic fluid;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;urinary;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;duodenum;liver;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.16791 0.15011 -0.350843407 29.54116537 2165.69773 8.56436 DSEL 5.16087410257055e-06 0.992162421463415 0.007832417662482 dermatan sulfate epimerase-like . . TISSUE SPECIFICITY: Expressed in different brain areas as well as in multiple other peripheral tissues. {ECO:0000269|PubMed:12556911}.; unclassifiable (Anatomical System);lung;ovary;heart;cerebral cortex;head and neck;brain; ciliary ganglion;trigeminal ganglion; 0.23775 . -0.191064116 39.27813163 3154.04309 10.68868 DSG1 0.979103460229869 0.020896533702468 6.06766275706549e-09 desmoglein 1 FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.; DISEASE: Palmoplantar keratoderma 1, striate, focal, or diffuse (PPKS1) [MIM:148700]: A dermatological disorder characterized by thickening of the skin on the palms and soles, and longitudinal hyperkeratotic lesions on the palms, running the length of each finger. {ECO:0000269|PubMed:10332028}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Erythroderma, congenital, with palmoplantar keratoderma, hypotrichosis, and hyper IgE (EPKHE) [MIM:615508]: A syndrome characterized by severe dermatitis, multiple allergies and metabolic wasting. Clinical features include erythroderma, yellowish papules and plaques arranged at the periphery of the palms, along the fingers and over weight-bearing areas of the feet, skin erosions and scaling, and hypotrichosis. Additionally, patients manifest severe food allergies, elevated immunoglobulin E (IgE) levels and recurrent infections with marked metabolic wasting. {ECO:0000269|PubMed:23974871}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Epidermis, tongue, tonsil and esophagus.; unclassifiable (Anatomical System);optic nerve;heart;oral cavity;visual apparatus;liver;duodenum;hypopharynx;testis;spleen;head and neck;skin;skeletal muscle; dorsal root ganglion;tongue;ciliary ganglion;atrioventricular node;skeletal muscle;skin; 0.78331 0.21050 1.6369421 96.09577731 3496.97426 11.38730 DSG1-AS1 . . . DSG1 antisense RNA 1 . . . . . . . . . . . DSG2 0.000747066619496092 0.998494272026896 0.000758661353607778 desmoglein 2 FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.; DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 10 (ARVD10) [MIM:610193]: A congenital heart disease characterized by infiltration of adipose and fibrous tissue into the right ventricle and loss of myocardial cells, resulting in ventricular and supraventricular arrhythmias. {ECO:0000269|PubMed:16773573, ECO:0000269|PubMed:19863551, ECO:0000269|PubMed:20031617, ECO:0000269|PubMed:21062920}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1BB (CMD1BB) [MIM:612877]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:18678517}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: All of the tissues tested and carcinomas.; unclassifiable (Anatomical System);islets of Langerhans;colon;skeletal muscle;breast;uterus;pancreas;prostate;lung;endometrium;larynx;thyroid;placenta;visual apparatus;amnion;duodenum;liver;testis;cervix;head and neck;kidney;brain;mammary gland;stomach; thyroid; 0.43502 0.14712 2.296680326 98.31917905 2306.73684 8.89924 DSG2-AS1 . . . DSG2 antisense RNA 1 . . . . . . . . . . . DSG3 3.35935663514832e-13 0.44914595949395 0.550854040505714 desmoglein 3 FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.; . TISSUE SPECIFICITY: Epidermis, tongue, tonsil, esophagus and carcinomas.; unclassifiable (Anatomical System);smooth muscle;heart;tongue;colon;skin;skeletal muscle;uterus;pancreas;lung;oesophagus;adrenal gland;larynx;gum;nasopharynx;hypopharynx;liver;head and neck; superior cervical ganglion;tongue;atrioventricular node;trigeminal ganglion;tonsil; 0.32733 0.16869 -0.701780438 14.81481481 750.20081 5.43292 DSG4 6.32076861880848e-05 0.999718180977419 0.000218611336392827 desmoglein 4 FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. Coordinates the transition from proliferation to differentiation in hair follicle keratinocytes (By similarity). {ECO:0000250}.; DISEASE: Hypotrichosis 6 (HYPT6) [MIM:607903]: A condition characterized by the presence of less than the normal amount of hair and abnormal hair follicles and shafts, which are thin and atrophic. The disorder affects the trunk and extremities as well as the scalp, and the eyebrows and eyelashes may also be involved, whereas beard, pubic, and axillary hairs are largely spared. In addition, patients can develop hyperkeratotic follicular papules, erythema, and pruritus in affected areas. In some patients with congenital hypotrichosis, monilethrix-like hairs showing elliptical nodes have been observed. {ECO:0000269|PubMed:15191570}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Autoantibodies against DSG4 are found in patients with pemphigus vulgaris. Pemphigus vulgaris is a potentially lethal skin disease in which epidermal blisters occur as the result of the loss of cell-cell adhesion.; TISSUE SPECIFICITY: Highly expressed in skin, testis and prostate; less in salivary gland. In scalp follicles, present in the inner root sheath (IRS) and all layers of the matrix and precortex. {ECO:0000269|PubMed:12648213, ECO:0000269|PubMed:12705872}.; testis; . 0.30616 0.16550 1.833561474 97.05119132 578.83724 4.87526 DSN1 1.72357694081058e-06 0.659001624014821 0.340996652408238 DSN1 homolog, MIS12 kinetochore complex component FUNCTION: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. {ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}.; . . . . 0.08232 0.07785 -0.139478553 43.29440906 80.07637 1.89200 DSP 0.999901542789998 9.84572100025319e-05 7.19423015500153e-21 desmoplakin FUNCTION: Major high molecular weight protein of desmosomes. Involved in the organization of the desmosomal cadherin- plakoglobin complexes into discrete plasma membrane domains and in the anchoring of intermediate filaments to the desmosomes.; DISEASE: Keratoderma, palmoplantar, striate 2 (SPPK2) [MIM:612908]: A dermatological disorder characterized by thickening of the skin on the palms (linear pattern) and the soles (island-like pattern) and flexor aspect of the fingers. Abnormalities of the nails, the teeth and the hair are rarely present. {ECO:0000269|PubMed:9887343}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated, with woolly hair and keratoderma (DCWHK) [MIM:605676]: An autosomal recessive cardiocutaneous syndrome characterized by a generalized striate keratoderma particularly affecting the palmoplantar epidermis, woolly hair, and dilated left ventricular cardiomyopathy. {ECO:0000269|PubMed:11063735}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 8 (ARVD8) [MIM:607450]: A congenital heart disease characterized by infiltration of adipose and fibrous tissue into the right ventricle and loss of myocardial cells, resulting in ventricular and supraventricular arrhythmias. {ECO:0000269|PubMed:12373648, ECO:0000269|PubMed:15941723, ECO:0000269|PubMed:20031617}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Skin fragility-woolly hair syndrome (SFWHS) [MIM:607655]: An autosomal recessive genodermatosis characterized by skin fragility with blistering, focal and diffuse palmoplantar keratoderma, hyperkeratotic plaques on the trunk and limbs, and woolly hair with varying degrees of alopecia. {ECO:0000269|PubMed:11841538}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa, lethal acantholytic (EBLA) [MIM:609638]: A form of epidermolysis bullosa characterized by severe fragility of skin and mucous membranes. The phenotype is lethal in the neonatal period because of immense transcutaneous fluid loss. Typical features include universal alopecia, neonatal teeth, and nail loss. Histopathology of the skin shows suprabasal clefting and acantholysis throughout the spinous layer, mimicking pemphigus. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated, with woolly hair, keratoderma, and tooth agenesis (DCWHKTA) [MIM:615821]: A cardiocutaneous syndrome characterized by biventricular dilated cardiomyopathy, hyperkeratosis, woolly hair, palmoplantar keratoderma, and hypo/oligodontia. {ECO:0000269|PubMed:16628197, ECO:0000269|PubMed:20940358, ECO:0000269|PubMed:22795705}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform DPI is apparently an obligate constituent of all desmosomes. Isoform DPII resides predominantly in tissues and cells of stratified origin.; . . 0.67242 0.36963 -2.227884388 1.321066289 4755.60752 13.95902 DSPP 0.000618023464984046 0.725993736256164 0.273388240278852 dentin sialophosphoprotein FUNCTION: DSP may be an important factor in dentinogenesis. DPP may bind high amount of calcium and facilitate initial mineralization of dentin matrix collagen as well as regulate the size and shape of the crystals.; DISEASE: Deafness, autosomal dominant, 39, with dentinogenesis imperfecta 1 (DFNA39/DGI1) [MIM:605594]: A disorder characterized by the association of progressive sensorineural high-frequency hearing loss with dentinogenesis imperfecta. {ECO:0000269|PubMed:11175790}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dentinogenesis imperfecta, Shields type 2 (DGI2) [MIM:125490]: A form of dentinogenesis imperfecta, an autosomal dominant dentin disorder characterized by amber-brown, opalescent teeth that fracture and shed their enamel during mastication, thereby exposing the dentin to rapid wear. Radiographically, the crown appears bulbous and pulpal obliteration is common. The pulp chambers are initially larger than normal prior and immediately after tooth eruption, and then progressively close down to become almost obliterated by abnormal dentin formation. Roots are short and thin. Both primary and permanent teeth are affected. DGI2 is not associated with osteogenesis imperfecta. {ECO:0000269|PubMed:11175779, ECO:0000269|PubMed:14758537, ECO:0000269|PubMed:17627120, ECO:0000269|PubMed:21029264}. Note=The disease is caused by mutations affecting the gene represented in this entry. DSPP defects causing dentin abnormalities act in a dominant negative manner and include missense, splice-site, frameshift mutations. 5' frameshift mutations cause dentin dysplasia while frameshift mutations at the 3' end cause the more severe dentinogenesis imperfecta phenotype (PubMed:18521831 and PubMed:22392858).; DISEASE: Dentinogenesis imperfecta, Shields type 3 (DGI3) [MIM:125500]: A form of dentinogenesis imperfecta, an autosomal dominant dentin disorder characterized by amber-brown, opalescent teeth that fracture and shed their enamel during mastication, thereby exposing the dentin to rapid wear. Radiographically, the crown appears bulbous and pulpal obliteration is common. The pulp chambers are initially larger than normal prior and immediately after tooth eruption, and then progressively close down to become almost obliterated by abnormal dentin formation. Roots are short and thin. Both primary and permanent teeth are affected. DGI3 teeth typically manifest multiple periapical radiolucencies. DGI3 is not associated with osteogenesis imperfecta. {ECO:0000269|PubMed:15592686, ECO:0000269|PubMed:18521831, ECO:0000269|PubMed:23509818}. Note=The disease is caused by mutations affecting the gene represented in this entry. DSPP defects causing dentin abnormalities act in a dominant negative manner and include missense, splice-site, frameshift mutations. 5' frameshift mutations cause dentin dysplasia while frameshift mutations at the 3' end cause the more severe dentinogenesis imperfecta phenotype (PubMed:18521831 and PubMed:22392858).; DISEASE: Dentin dysplasia 2 (DTDP2) [MIM:125420]: A dental defect in which the deciduous teeth are opalescent. The permanent teeth are of normal shape, form, and color in most cases. The root length is normal. On radiographs, the pulp chambers of permanent teeth are obliterated, have a thistle-tube deformity and contain pulp stones. {ECO:0000269|PubMed:12354781, ECO:0000269|PubMed:18521831}. Note=The disease is caused by mutations affecting the gene represented in this entry. DSPP defects causing dentin abnormalities act in a dominant negative manner and include missense, splice-site, frameshift mutations. 5' frameshift mutations cause dentin dysplasia while frameshift mutations at the 3' end cause the more severe dentinogenesis imperfecta phenotype (PubMed:18521831, PubMed:22392858). {ECO:0000269|PubMed:18521831, ECO:0000269|PubMed:22392858}.; TISSUE SPECIFICITY: Expressed in teeth. DPP is synthesized by odontoblast and transiently expressed by pre-ameloblasts.; kidney; skeletal muscle; 0.79857 . 4.036181747 99.66383581 13973.59023 25.50962 DST 0.99999999999999 9.56233768805028e-15 4.07735602188469e-50 dystonin FUNCTION: Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin- containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two- dimensional mesh.; FUNCTION: Isoform 6: required for bundling actin filaments around the nucleus. {ECO:0000250, ECO:0000269|PubMed:10428034, ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:19403692}.; DISEASE: Neuropathy, hereditary sensory and autonomic, 6 (HSAN6) [MIM:614653]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by sensory and/or autonomic abnormalities. HSAN6 is a severe autosomal recessive disorder characterized by neonatal hypotonia, respiratory and feeding difficulties, lack of psychomotor development, and autonomic abnormalities including labile cardiovascular function, lack of corneal reflexes leading to corneal scarring, areflexia, and absent axonal flare response after intradermal histamine injection. {ECO:0000269|PubMed:22522446}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa simplex, autosomal recessive 2 (EBSB2) [MIM:615425]: A form of epidermolysis bullosa, a dermatologic disorder characterized by localized blistering on the dorsal, lateral and plantar surfaces of the feet. EBSB2 is characterized by trauma-induced blistering mainly occurring on the feet and ankles. Ultrastructural analysis of skin biopsy shows abnormal hemidesmosomes with poorly formed inner plaques. {ECO:0000269|PubMed:20164846, ECO:0000269|PubMed:22113475}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is expressed in myoblasts (at protein level). Isoform 3 is expressed in the skin. Isoform 6 is expressed in the brain. Highly expressed in skeletal muscle and cultured keratinocytes. {ECO:0000269|PubMed:11751855, ECO:0000269|PubMed:19932097, ECO:0000269|PubMed:8752219}.; myocardium;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;bladder;brain;heart;cartilage;tongue;urinary;blood;lens;skeletal muscle;breast;macula lutea;liver;spleen;cervix;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; amygdala;dorsal root ganglion;occipital lobe;medulla oblongata;thalamus;superior cervical ganglion;tongue;hypothalamus;spinal cord;pons;atrioventricular node;caudate nucleus;skin;skeletal muscle;uterus;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.87634 0.40727 -0.532709792 20.70653456 9099.85464 20.71216 DSTN 0.759201434624303 0.231751677713556 0.00904688766214077 destrin (actin depolymerizing factor) FUNCTION: Actin-depolymerizing protein. Severs actin filaments (F- actin) and binds to actin monomers (G-actin). Acts in a pH- independent manner.; . TISSUE SPECIFICITY: Widely distributed in various tissues.; myocardium;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;trophoblast;small intestine;islets of Langerhans;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach; uterus;amygdala;heart; 0.14182 0.23021 0.057118534 57.99716914 2.50944 0.09269 DSTNP1 . . . destrin (actin depolymerizing factor) pseudogene 1 . . . . . . . . . . . DSTNP2 . . . destrin (actin depolymerizing factor) pseudogene 2 . . . . . . . . . . . DSTNP3 . . . destrin (actin depolymerizing factor) pseudogene 3 . . . . . . . . . . . DSTNP4 . . . destrin (actin depolymerizing factor) pseudogene 4 . . . . . . . . . . . DSTNP5 . . . destrin (actin depolymerizing factor) pseudogene 5 . . . . . . . . . . . DSTYK 0.147285745754517 0.85270785750713 6.39673835317042e-06 dual serine/threonine and tyrosine protein kinase FUNCTION: Acts as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. May induce both caspase-dependent apoptosis and caspase-independent cell death. {ECO:0000269|PubMed:15178406, ECO:0000269|PubMed:23862974}.; . TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and testis. Expressed in basolateral and apical membranes of all tubular epithelia. Expressed in thin ascending limb of the loop of Henle and the distal convoluted tubule. Expressed in all layers of transitional ureteric epithelium and in the ureteric smooth-muscle cells. Weakly expressed in heart, brain, placenta, kidney, pancreas, spleen, thymus, prostate, uterus, small intestine, white blood cells, stomach, spinal cord and adrenal gland. Is widely distributed in the CNS. Also detected in several tumor cell lines. {ECO:0000269|PubMed:15178406, ECO:0000269|PubMed:17123648, ECO:0000269|PubMed:23862974}.; . . 0.20448 0.10172 0.091899012 60.68058504 447.37017 4.40005 DTD1 0.290212859228027 0.688858099760753 0.0209290410112198 D-tyrosyl-tRNA deacylase 1 FUNCTION: ATPase involved in DNA replication, may facilitate loading of CDC45 onto pre-replication complexes. May hydrolyze D- tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr), a possible defense mechanism against a harmful effect of D-tyrosine. {ECO:0000269|PubMed:15653697, ECO:0000269|PubMed:20065034}.; . TISSUE SPECIFICITY: Expressed in many adult and fetal tissues. Highest levels in testis, ovary, spleen and in adult and fetal brain. {ECO:0000269|PubMed:12392168}.; . . . 0.14645 -0.207437529 38.2814343 250.36944 3.40862 DTD2 0.00170814911545887 0.467463367968197 0.530828482916344 D-tyrosyl-tRNA deacylase 2 (putative) FUNCTION: Hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr). Could be a defense mechanism against a harmful effect of D-tyrosine (Potential). {ECO:0000305}.; . . . . 0.25961 0.07098 -0.053113545 49.38664779 6.20561 0.23402 DTHD1 . . . death domain containing 1 . . . lung;nasopharynx;testis; . . . 1.594792159 95.83628214 3165.84845 10.72526 DTL 0.0070133816764049 0.992838193757878 0.000148424565717024 denticleless E3 ubiquitin protein ligase homolog FUNCTION: Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), FBXO18/FBH1 and SETD8 (PubMed:16861906, PubMed:16949367, PubMed:16964240, PubMed:17085480, PubMed:18703516, PubMed:18794347, PubMed:18794348, PubMed:19332548, PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613). CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication (PubMed:16861906, PubMed:16949367, PubMed:17085480). CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing (PubMed:18794348, PubMed:19332548). SETD8 degradation is also important for a proper regulation of mechanisms such as TGF- beta signaling, cell cycle progression, DNA repair and cell migration (PubMed:23478445). Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA-dependent translesion DNA synthesis (PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613). {ECO:0000269|PubMed:16861906, ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240, ECO:0000269|PubMed:17085480, ECO:0000269|PubMed:18703516, ECO:0000269|PubMed:18794347, ECO:0000269|PubMed:18794348, ECO:0000269|PubMed:19332548, ECO:0000269|PubMed:20129063, ECO:0000269|PubMed:23478441, ECO:0000269|PubMed:23478445, ECO:0000269|PubMed:23677613}.; . TISSUE SPECIFICITY: Expressed in placenta and testis, very low expression seen in skeletal muscle. Detected in all hematopoietic tissues examined, with highest expression in thymus and bone marrow. A low level detected in the spleen and lymph node, and barely detectable level in the peripheral leukocytes. RA treatment down-regulated the expression in NT2 cell. {ECO:0000269|PubMed:11278750, ECO:0000269|PubMed:17106265}.; . . 0.77262 0.17795 0.044168103 57.40740741 126.25129 2.44634 DTNA 0.921398185265569 0.0786016478666321 1.66867799264866e-07 dystrobrevin alpha FUNCTION: May be involved in the formation and stability of synapses as well as being involved in the clustering of nicotinic acetylcholine receptors.; DISEASE: Left ventricular non-compaction 1 (LVNC1) [MIM:604169]: A disease due to an arrest of myocardial morphogenesis. It is characterized by a hypertrophic left ventricle with deep trabeculations and with poor systolic function, with or without associated left ventricular dilation. In some cases, it is associated with other congenital heart anomalies such as ventricular septal defects, pulmonic stenosis and atrial septal defects. The right ventricle may also be affected. {ECO:0000269|PubMed:11238270}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in brain, skeletal and cardiac muscles, and expressed at lower levels in lung, liver and pancreas. Isoform 2 is not expressed in cardiac muscle. Isoform 7 and isoform 8 are only expressed in muscle.; myocardium;smooth muscle;colon;skin;retina;uterus;prostate;whole body;frontal lobe;larynx;thyroid;testis;brain;amygdala;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;muscle;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;hippocampus;liver;head and neck;spleen;stomach;cerebellum; whole brain;dorsal root ganglion;amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.92328 0.20424 -0.510624372 21.65015334 94.31832 2.09114 DTNB 0.000530412146332964 0.999218121720225 0.000251466133441806 dystrobrevin beta . . TISSUE SPECIFICITY: Highly expressed in brain, kidney and pancreas.; sympathetic chain;colon;parathyroid;skin;retina;uterus;prostate;thyroid;bone;testis;germinal center;brain;spinal ganglion;unclassifiable (Anatomical System);blood;breast;pancreas;lung;placenta;cervix;head and neck;kidney;mammary gland;stomach;cerebellum; whole brain;amygdala;superior cervical ganglion;hypothalamus;temporal lobe;spinal cord;prefrontal cortex;caudate nucleus;cingulate cortex;skeletal muscle;skin; 0.59206 0.49987 -0.799052816 12.45576787 225.44054 3.24713 DTNBP1 1.33929654176623e-06 0.603943095007221 0.396055565696237 dystrobrevin binding protein 1 FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Associates with the BLOC-2 complex to facilitate the transport of TYRP1 independent of AP-3 function. Plays a role in synaptic vesicle trafficking and in neurotransmitter release. Plays a role in the regulation of cell surface exposure of DRD2. May play a role in actin cytoskeleton reorganization and neurite outgrowth. May modulate MAPK8 phosphorylation. Appears to promote neuronal transmission and viability through regulating the expression of SNAP25 and SYN1, modulating PI3-kinase-Akt signaling and influencing glutamatergic release. Regulates the expression of SYN1 through binding to its promoter. Modulates prefrontal cortical activity via the dopamine/D2 pathway. {ECO:0000269|PubMed:15345706, ECO:0000269|PubMed:16837549, ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:17989303, ECO:0000269|PubMed:19094965, ECO:0000269|PubMed:20180862, ECO:0000269|PubMed:20921223}.; DISEASE: Hermansky-Pudlak syndrome 7 (HPS7) [MIM:614076]: A form of Hermansky-Pudlak syndrome, a genetically heterogeneous autosomal recessive disorder characterized by oculocutaneous albinism, bleeding due to platelet storage pool deficiency, and lysosomal storage defects. This syndrome results from defects of diverse cytoplasmic organelles including melanosomes, platelet dense granules and lysosomes. Ceroid storage in the lungs is associated with pulmonary fibrosis, a common cause of premature death in individuals with HPS. {ECO:0000269|PubMed:12923531}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in DTNBP1 are associated with susceptibility to schizophrenia, a mental disorder characterized by a breakdown of thought processes and by poor emotional responsiveness. Genetic mutations lead to alterations in the glutamatergic transmisssion in the brain and modified Akt signaling (PubMed:15345706). Protein levels and expression are reduced in nerve terminals of the hippocampus and there is an increased release of glutamate in schizophrenic patients (PubMed:15124027). Levels of isoform 1 are reduced in the pSTG, but not in HF, by about 48% in 92% of schizophrenic patients. In the HF, there is an average of 33% reduction in synaptic expression of isoform 2 in 67% of cases, and of isoform 3, an average reduction of 35% in 80% of cases. In the dorsolateral prefrontal cortex (DLPFC), significant reductions in levels of isoform 3 are observed about 71% of schizophrenic patients showed an average reduction of this isoform of about 60% (PubMed:19617633). {ECO:0000269|PubMed:15124027, ECO:0000269|PubMed:15345706, ECO:0000269|PubMed:19617633}.; TISSUE SPECIFICITY: Detected in brain, in neurons and in neuropil. Isoform 1 is expressed in the cerebral cortex, and hippocampal frontal (HF). Specific expression in the posterior half of the superior temporal gyrus (pSTG). Higher expression of isoform 2 and 3 in the HF than in the pSTG while isoform 1 shows no difference in expression in these areas. In the HF, detected in dentate gyrus (DG) and in pyramidal cells of hippocampus CA2 and CA3 (at protein level). Expressed in all principal neuronal populations of the HF, namely pyramidal neurons in the subiculum and CA1-3, granule cells in the dense cell layer of the DG (DGg), and polymorph cells in the hilus of the DG (DGh). Maximal levels in CA2, CA3, and DGh. Isoform 2 not expressed in the cerebral cortex. {ECO:0000269|PubMed:16980328}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;tongue;islets of Langerhans;muscle;pharynx;blood;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; . 0.10981 0.28878 0.665103516 84.6131163 517.45762 4.65055 DTWD1 1.4054382775955e-05 0.400120075765011 0.599865869852213 DTW domain containing 1 . . . unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;skin;skeletal muscle;uterus;prostate;whole body;lung;endometrium;nasopharynx;trabecular meshwork;bone;placenta;hippocampus;testis;cervix;kidney;brain;mammary gland; . 0.08638 . 0.12689526 63.00424628 108.59043 2.26156 DTWD2 2.16048560607966e-05 0.484452633133217 0.515525762010723 DTW domain containing 2 . . . unclassifiable (Anatomical System);ovary;salivary gland;pharynx;colon;blood;skeletal muscle;retina;breast;prostate;lung;visual apparatus;liver;testis;kidney;brain;bladder;stomach; . 0.17158 0.11490 -0.448125345 24.19202642 92.81718 2.06998 DTX1 0.00125591757009814 0.959340865638321 0.0394032167915805 deltex 1 FUNCTION: Functions as a ubiquitin ligase protein in vivo, mediating ubiquitination and promoting degradation of MEKK1, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity (By similarity). Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Mainly acts as a positive regulator of Notch, but it also acts as a negative regulator, depending on the developmental and cell context. Mediates the antineural activity of Notch, possibly by inhibiting the transcriptional activation mediated by MATCH1. Involved in neurogenesis, lymphogenesis and myogenesis, and may also be involved in MZB (Marginal zone B) cell differentiation. Promotes B-cell development at the expense of T- cell development, suggesting that it can antagonize NOTCH1. {ECO:0000250, ECO:0000269|PubMed:11564735, ECO:0000269|PubMed:11869684, ECO:0000269|PubMed:9590294}.; . TISSUE SPECIFICITY: Widely expressed. Strongly expressed in blood vessel. Also expressed in embryonic nervous system, pancreas, lung, adrenal gland, digestive tube and muscles. Expressed in MZB cells and developing B- and T-cells. {ECO:0000269|PubMed:12753744, ECO:0000269|PubMed:9590294}.; unclassifiable (Anatomical System);lymphoreticular;smooth muscle;lymph node;parathyroid;fovea centralis;pancreas;lung;endometrium;larynx;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;germinal center;kidney;brain;tonsil; dorsal root ganglion; 0.48222 0.14238 -0.88906181 10.36801132 104.41372 2.20954 DTX2 0.106757915614529 0.886582046961913 0.00666003742355764 deltex 2, E3 ubiquitin ligase FUNCTION: Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Probably acts both as a positive and negative regulator of Notch, depending on the developmental and cell context. Mediates the antineural activity of Notch, possibly by inhibiting the transcriptional activation mediated by MATCH1. Functions as a ubiquitin ligase protein in vitro, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity.; . . . . 0.25831 0.10988 -0.683363435 15.36329323 137.65609 2.55415 DTX2P1 . . . DTX2 pseudogene 1 . . . . . . . . . . . DTX2P1-UPK3BP1-PMS2P11 . . . DTX2P1-UPK3BP1-PMS2P11 readthrough, transcribed pseudogene . . . . . . . . . . . DTX3 0.921137255195518 0.0783740640981225 0.000488680706358951 deltex 3, E3 ubiquitin ligase FUNCTION: Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Probably acts both as a positive and negative regulator of Notch, depending on the developmental and cell context (By similarity). Functions as an ubiquitin ligase protein in vitro, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity. {ECO:0000250}.; . . myocardium;ovary;adrenal medulla;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;pancreas;lung;placenta;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; amygdala;dorsal root ganglion;occipital lobe;superior cervical ganglion;prefrontal cortex;caudate nucleus;pons; 0.26487 0.11557 -0.494039303 22.09247464 12.09498 0.43818 DTX3L 2.44159143785208e-05 0.91633704522149 0.0836385388641314 deltex 3 like, E3 ubiquitin ligase FUNCTION: Ubiquitin ligase that mediates monoubiquitination of 'Lys-91' of histone H4 (H4K91ub1), in response to DNA damage. Protects cells exposed to DNA-damaging agents. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post- translational modifications such as H4 'Lys-20' methylation (H4K20me). Involved in the recruitment of 53BP1/TP53BP1 to sites of DNA damage by mediating H4K91ub1 formation. In concert with PARP9, plays a role in PARP1-dependent DNA damage repair. PARP1- dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. {ECO:0000269|PubMed:12670957, ECO:0000269|PubMed:19818714, ECO:0000269|PubMed:23230272}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; ciliary ganglion;atrioventricular node; 0.03369 0.06049 -0.354480518 29.42911064 265.46071 3.49515 DTX4 0.594144205008104 0.405439587719877 0.000416207272019095 deltex 4, E3 ubiquitin ligase FUNCTION: Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations (By similarity). Functions as a ubiquitin ligase protein in vivo, mediating 'Lys48'-linked polyubiquitination and promoting degradation of TBK1, targeting to TBK1 requires interaction with NLRP4. {ECO:0000250, ECO:0000269|PubMed:22388039}.; . . lymphoreticular;smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pineal body;blood;lens;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;alveolus;liver;cervix;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;fetal brain;spinal cord;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe; 0.26219 0.10412 -0.288341872 33.41589998 60.73464 1.58425 DTYMK 0.54609142720961 0.439911411674413 0.0139971611159773 deoxythymidylate kinase FUNCTION: Catalyzes the conversion of dTMP to dTDP.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion; . 0.27220 -0.538132194 20.26421326 24.53091 0.80631 DUBR . . . DPPA2 upstream binding RNA . . . . . . . . . . . DUOX1 1.97275277824694e-13 0.999430300265189 0.000569699734613539 dual oxidase 1 FUNCTION: Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain. {ECO:0000269|PubMed:11514595, ECO:0000269|PubMed:12824283}.; . TISSUE SPECIFICITY: Expressed in thyrocytes and tracheal surface epithelial cells (at protein level). Expressed in thyroid, trachea, bronchium, and to a lower extent, in placenta, testis, prostate, pancreas and heart. {ECO:0000269|PubMed:10806195, ECO:0000269|PubMed:11514595, ECO:0000269|PubMed:12824283, ECO:0000269|PubMed:15210697}.; unclassifiable (Anatomical System);heart;tongue;skin;skeletal muscle;uterus;optic nerve;whole body;lung;larynx;thyroid;hypopharynx;testis;head and neck;bladder;cerebellum; superior cervical ganglion;tongue;thyroid;ciliary ganglion;atrioventricular node;fetal thyroid;skeletal muscle; 0.35019 0.22041 -2.42025884 1.037980656 3614.85122 11.64544 DUOX2 1.8967607743652e-37 3.81333784492947e-06 0.999996186662155 dual oxidase 2 FUNCTION: Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain. {ECO:0000269|PubMed:12824283}.; DISEASE: Thyroid dyshormonogenesis 6 (TDH6) [MIM:607200]: A disorder due to a defective conversion of accumulated iodide to organically bound iodine. The iodide organification defect can be partial or complete. {ECO:0000269|PubMed:12110737, ECO:0000269|PubMed:16134168, ECO:0000269|PubMed:16322276, ECO:0000269|PubMed:20187165}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in colon, small intestine, duodenum and tracheal surface epithelial cells (at protein level). Expressed in thyrocytes. Also detected in kidney, liver, lung, pancreas, prostate, salivary glands, rectum and testis. {ECO:0000269|PubMed:10806195, ECO:0000269|PubMed:11514595, ECO:0000269|PubMed:12824283, ECO:0000269|PubMed:15210697, ECO:0000269|PubMed:15591162}.; . . 0.15059 0.21524 0.227640447 68.52441614 1216.76018 6.60084 DUOXA1 0.000109720453384831 0.947987111799934 0.051903167746681 dual oxidase maturation factor 1 FUNCTION: May be required for the maturation and the transport from the endoplasmic reticulum to the plasma membrane of functional DUOX1. {ECO:0000305|PubMed:16651268}.; . TISSUE SPECIFICITY: Specifically expressed in thyroid gland. Also detected in esophagus. {ECO:0000269|PubMed:16651268}.; unclassifiable (Anatomical System);meninges;cartilage;colon;skin;uterus;lung;pia mater;endometrium;larynx;thyroid;head and neck;dura mater; . 0.04745 0.18038 0.264628794 70.5178108 350.37954 3.96898 DUOXA2 1.49970920077282e-07 0.119681603541219 0.880318246487861 dual oxidase maturation factor 2 FUNCTION: Required for the maturation and the transport from the endoplasmic reticulum to the plasma membrane of functional DUOX2. May play a role in thyroid hormone synthesis. {ECO:0000269|PubMed:16651268}.; DISEASE: Thyroid dyshormonogenesis 5 (TDH5) [MIM:274900]: A disorder due to thyroid dyshormonogenesis, causing hypothyroidism, goiter, and variable mental deficits derived from unrecognized and untreated hypothyroidism. {ECO:0000269|PubMed:18042646, ECO:0000269|PubMed:25675383}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Specifically expressed in thyroid. Also detected in salivary glands. {ECO:0000269|PubMed:16651268}.; unclassifiable (Anatomical System);uterus;prostate;lung;cartilage;endometrium;thyroid;colon;skeletal muscle; . 0.03739 0.10844 -0.426079032 25.36565228 54.46162 1.47498 DUPD1 1.17861404790217e-07 0.0554659359752876 0.944533946163308 dual specificity phosphatase and pro isomerase domain containing 1 . . TISSUE SPECIFICITY: Skeletal muscle, liver and adipose tissue. {ECO:0000269|PubMed:17498703}.; . . 0.12588 0.10963 0.617373774 83.25076669 1268.11055 6.70980 DURS1 . . . Duane retraction syndrome 1 . . . . . . . . . . . DUS1L 1.5346357409002e-06 0.958876534105775 0.0411219312584838 dihydrouridine synthase 1 like FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. {ECO:0000250}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;larynx;bone;thyroid;testis;germinal center;bladder;brain;artery;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;alveolus;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach;aorta; testis - seminiferous tubule;liver;testis;atrioventricular node; 0.17768 0.10832 -0.865195027 10.79853739 216.85677 3.18381 DUS2 0.000272032398658379 0.999072267641516 0.000655699959825474 dihydrouridine synthase 2 FUNCTION: Dihydrouridine synthase. Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Negatively regulates the activation of EIF2AK2/PKR. {ECO:0000269|PubMed:15994936, ECO:0000269|PubMed:18096616}.; . TISSUE SPECIFICITY: Weak expression in heart, placenta and skeletal muscle. Up-regulated in most lung cancer cells (at protein level). {ECO:0000269|PubMed:15994936}.; . . 0.08346 0.11249 -0.400392389 26.85185185 261.28866 3.47039 DUS3L 2.44680259980273e-09 0.447364589128752 0.552635408424445 dihydrouridine synthase 3 like FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. {ECO:0000250}.; . . lymphoreticular;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;blood;lens;bile duct;pancreas;lung;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve;thymus; superior cervical ganglion;testis - interstitial;subthalamic nucleus;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16355 . -0.685180376 15.32200991 3219.59367 10.81274 DUS4L 0.000141354055808242 0.649322981223746 0.350535664720445 dihydrouridine synthase 4 like FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;vein;skin;skeletal muscle;uterus;lung;frontal lobe;placenta;bone;liver;testis;spleen;kidney;brain;aorta;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.50741 0.17915 0.016664174 55.21939137 245.99238 3.38387 DUSP1 0.0205002018825111 0.904706908939658 0.0747928891778311 dual specificity phosphatase 1 FUNCTION: Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at high levels in the lung, liver placenta and pancreas. Moderate levels seen in the heart and skeletal muscle. Lower levels found in the brain and kidney. {ECO:0000269|PubMed:8106404}.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;brain;tonsil;cartilage;urinary;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;cervix;spleen;mammary gland;colon;parathyroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;placenta;head and neck;kidney;aorta;stomach; white blood cells; 0.45721 0.29763 . . 218.27707 3.19307 DUSP2 0.791321031693344 0.202539477906902 0.006139490399754 dual specificity phosphatase 2 FUNCTION: Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2.; . TISSUE SPECIFICITY: Expressed in hematopoietic tissues.; unclassifiable (Anatomical System);lymph node;ovary;heart;islets of Langerhans;hypothalamus;colon;parathyroid;blood;skin;uterus;pancreas;prostate;lung;endometrium;epididymis;placenta;testis;cervix;spleen;germinal center;kidney;brain; white blood cells; 0.29136 0.35283 . . 43.27797 1.24894 DUSP3 0.736744916251957 0.251704815133165 0.011550268614878 dual specificity phosphatase 3 FUNCTION: Shows activity both for tyrosine-protein phosphate and serine-protein phosphate, but displays a strong preference toward phosphotyrosines. Specifically dephosphorylates and inactivates ERK1 and ERK2. {ECO:0000269|PubMed:10224087, ECO:0000269|PubMed:11863439}.; . . lymphoreticular;smooth muscle;ovary;substantia nigra;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;amniotic fluid;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach; subthalamic nucleus;globus pallidus;skeletal muscle; 0.32920 0.21177 -0.317668748 31.45789101 17.73708 0.62001 DUSP4 0.53906924159124 0.4461716999455 0.0147590584632606 dual specificity phosphatase 4 FUNCTION: Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;liver;alveolus;spleen;mammary gland;stomach; superior cervical ganglion;adipose tissue;trachea;placenta;trigeminal ganglion;skeletal muscle; 0.21102 0.31213 -0.448125345 24.19202642 28.01967 0.89955 DUSP5 0.0255938782141754 0.91804717849403 0.0563589432917944 dual specificity phosphatase 5 FUNCTION: Displays phosphatase activity toward several substrates. The highest relative activity is toward ERK1.; . . . . 0.38324 0.25193 1.374284246 94.51521585 292.05416 3.65600 DUSP5P1 . . . dual specificity phosphatase 5 pseudogene 1 . . . . . 0.18886 . . . . . DUSP5P2 . . . dual specificity phosphatase 5 pseudogene 2 . . . . . . . . . . . DUSP6 0.911205141065287 0.0881342487896103 0.000660610145103103 dual specificity phosphatase 6 FUNCTION: Inactivates MAP kinases. Has a specificity for the ERK family.; DISEASE: Hypogonadotropic hypogonadism 19 with or without anosmia (HH19) [MIM:615269]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:23643382}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. Some patients carrying mutations in DUSP6 also have a heterozygous mutation in another HH-associated gene including FGFR1 and SPRY4 (PubMed:23643382). {ECO:0000269|PubMed:23643382}.; . lymphoreticular;ovary;sympathetic chain;developmental;colon;parathyroid;choroid;vein;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;alveolus;duodenum;liver;head and neck;spleen;kidney;mammary gland;aorta;stomach; lung;whole blood; 0.38346 0.37312 0.104848986 61.49445624 5632.29639 15.53337 DUSP7 0.228528646563016 0.736731347447801 0.034740005989183 dual specificity phosphatase 7 FUNCTION: Regulates the activity of the MAP kinase family in response to changes in the cellular environment. PYST2-S may act as a negative regulator of PYST2-L although it is unclear whether this is by competing for transcription, translation or activation factors. {ECO:0000269|PubMed:14603440}.; . TISSUE SPECIFICITY: Expressed at significantly higher levels in malignant hematopoietic cells than in corresponding non-malignant cells. {ECO:0000269|PubMed:14576828}.; unclassifiable (Anatomical System);amygdala;lymph node;tongue;testis;cervix;head and neck;brain;stomach; whole brain;medulla oblongata;temporal lobe;atrioventricular node;cingulate cortex;parietal lobe; 0.63246 0.14048 -0.449946534 24.00330267 61.31805 1.59545 DUSP8 0.6844729650101 0.311172545061669 0.00435448992823164 dual specificity phosphatase 8 FUNCTION: This protein shows both activity toward tyrosine-protein phosphate as well as with serine/threonine-protein phosphate. {ECO:0000250}.; . TISSUE SPECIFICITY: Abundant in brain, heart and skeletal muscle. {ECO:0000269|PubMed:7561881}.; uterus;lung;heart;endometrium;islets of Langerhans;liver;colon;spleen;brain;skin;stomach; amygdala;subthalamic nucleus;occipital lobe;superior cervical ganglion;temporal lobe;prefrontal cortex;globus pallidus;pons;parietal lobe;cingulate cortex; 0.12453 0.12894 . . 35.08836 1.06434 DUSP8P1 . . . dual specificity phosphatase 8 pseudogene 1 . . . . . . . . . . . DUSP8P2 . . . dual specificity phosphatase 8 pseudogene 2 . . . . . . . . . . . DUSP8P3 . . . dual specificity phosphatase 8 pseudogene 3 . . . . . . . . . . . DUSP8P4 . . . dual specificity phosphatase 8 pseudogene 4 . . . . . . . . . . . DUSP8P5 . . . dual specificity phosphatase 8 pseudogene 5 . . . . . . . . . . . DUSP9 0.648808512961975 0.325298657590022 0.0258928294480028 dual specificity phosphatase 9 FUNCTION: Inactivates MAP kinases. Has a specificity for the ERK family.; . . unclassifiable (Anatomical System);lung;ovary;endometrium;placenta;liver;testis;parathyroid;spleen;head and neck;kidney;brain; fetal liver;superior cervical ganglion;placenta;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.58545 0.14414 . . 44.5503 1.27775 DUSP10 0.499521469849817 0.496163251867368 0.00431527828281461 dual specificity phosphatase 10 FUNCTION: Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. It preferably dephosphorylates p38. {ECO:0000269|PubMed:10391943, ECO:0000269|PubMed:10597297, ECO:0000269|PubMed:22375048}.; . TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:16806267}.; lymphoreticular;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;gum;thyroid;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;lung;placenta;macula lutea;liver;spleen;kidney;stomach;peripheral nerve; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.71559 0.15250 -0.490397599 22.50530786 37.8217 1.12434 DUSP11 9.06000699119451e-05 0.93400983428852 0.0658995656415684 dual specificity phosphatase 11 FUNCTION: Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. In addition, has phosphatase activity with ATP, ADP and O-methylfluorescein phosphate (in vitro). Binds to RNA. May participate in nuclear mRNA metabolism. {ECO:0000269|PubMed:10347225, ECO:0000269|PubMed:24447265, ECO:0000269|PubMed:9685386}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;spinal cord;muscle;adrenal cortex;pharynx;blood;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion; 0.17953 0.09680 0.215080721 67.91696155 20.14995 0.68920 DUSP12 0.00353533720698026 0.953096538258875 0.0433681245341444 dual specificity phosphatase 12 . . TISSUE SPECIFICITY: Ubiquitous, highest expression in spleen, testis, ovary, and peripheral blood leukocytes and lower expression in liver and lung.; . . 0.14009 0.17197 -0.137658575 43.57159707 58.88449 1.55715 DUSP12P1 . . . dual specificity phosphatase 12 pseudogene 1 . . . . . . . . . . . DUSP13 9.99450179596282e-08 0.176639151383948 0.823360748671034 dual specificity phosphatase 13 FUNCTION: Probable protein tyrosine phosphatase. Has a phosphatase activity-independent regulatory role in MAP3K5/ASK1-mediated apoptosis, preventing MAP3K5/ASK1 inhibition by AKT1. Shows no phosphatase activity on MAPK1/ERK2, MAPK8/JNK, MAPK14/p38 and MAP3K5/ASK1. {ECO:0000269|PubMed:20358250}.; . TISSUE SPECIFICITY: Skeletal muscle specific. {ECO:0000269|PubMed:15252030}.; unclassifiable (Anatomical System);greater omentum;prostate;pancreas;whole body;heart;muscle;testis;skeletal muscle;retina; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.24878 0.09203 1.423841958 94.96933239 5121.96842 14.71123 DUSP14 0.773652009392439 0.218702035368053 0.00764595523950802 dual specificity phosphatase 14 FUNCTION: Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases.; . . . . 0.52392 0.13910 -0.295622497 32.61972163 33.1602 1.02593 DUSP15 0.000219668008201055 0.503853760398491 0.495926571593308 dual specificity phosphatase 15 . . TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:15138252}.; unclassifiable (Anatomical System);medulla oblongata;pancreas;lung;ovary;colon;testis;kidney;germinal center;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; . . . . 269.71288 3.52355 DUSP16 0.112697836437734 0.886057140900844 0.00124502266142171 dual specificity phosphatase 16 FUNCTION: Dual specificity protein phosphatase involved in the inactivation of MAP kinases. Dephosphorylates MAPK10 bound to ARRB2. {ECO:0000269|PubMed:11489891, ECO:0000269|PubMed:15888437}.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;endometrium;testis;brain;gall bladder;unclassifiable (Anatomical System);blood;lens;skeletal muscle;breast;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;mammary gland;stomach; superior cervical ganglion;atrioventricular node; 0.81610 0.12143 -0.775187015 13.05142722 1698.00555 7.59718 DUSP18 0.0618037276513494 0.721982949310874 0.216213323037777 dual specificity phosphatase 18 FUNCTION: Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine. In vitro, dephosphorylates p-nitrophenyl phosphate (pNPP).; . TISSUE SPECIFICITY: Widely expressed with highest levels in liver, brain, ovary and testis. {ECO:0000269|PubMed:12408986, ECO:0000269|PubMed:12591617}.; unclassifiable (Anatomical System);umbilical cord;ovary;tongue;colon;parathyroid;blood;lens;skeletal muscle;bone marrow;breast;pancreas;prostate;lung;bone;placenta;pituitary gland;testis;head and neck;kidney;brain;stomach; . 0.21984 0.11923 -0.183570861 39.95046001 27.51871 0.88673 DUSP19 0.00439399968226496 0.668667923753985 0.32693807656375 dual specificity phosphatase 19 FUNCTION: Has a dual specificity toward Ser/Thr and Tyr-containing proteins. {ECO:0000269|PubMed:12479873}.; . TISSUE SPECIFICITY: Expressed in the heart, lung, liver, and pancreas. The expression level in the pancreas is the highest. {ECO:0000269|PubMed:12479873}.; unclassifiable (Anatomical System);lung;testis;parathyroid;blood; dorsal root ganglion;medulla oblongata;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10285 0.11721 0.082802743 60.09082331 77.58469 1.85440 DUSP21 0.00358650089236117 0.395305247919196 0.601108251188443 dual specificity phosphatase 21 FUNCTION: Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:12408986}.; liver;testis;spleen; superior cervical ganglion;testis;atrioventricular node; 0.04568 0.08746 0.215080721 67.91696155 13.93927 0.50501 DUSP22 0.00430707145380812 0.867381637996829 0.128311290549363 dual specificity phosphatase 22 FUNCTION: Activates the Jnk signaling pathway. Dephosphorylates and deactivates p38 and stress-activated protein kinase/c-Jun N- terminal kinase (SAPK/JNK) (By similarity). {ECO:0000250, ECO:0000269|PubMed:11717427}.; . TISSUE SPECIFICITY: Ubiquitous. Highest expression seen in heart, placenta, lung, liver, kidney and pancreas. {ECO:0000269|PubMed:11717427}.; myocardium;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;bone;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pancreas;lung;nasopharynx;placenta;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland; testis - seminiferous tubule;testis; 0.19715 0.15782 0.284856336 71.40835103 805.07854 5.59092 DUSP23 0.0411468265638501 0.844060057786226 0.114793115649924 dual specificity phosphatase 23 FUNCTION: Protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. Able to enhance activation of JNK and p38 (MAPK14). {ECO:0000269|PubMed:15147733, ECO:0000269|PubMed:15201283}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in spleen, prostate, colon, adrenal gland, mammary gland, thyroid and trachea. Expressed at lower level in uterus, small intestine, bladder, bone marrow, brain, spinal cord and stomach. {ECO:0000269|PubMed:15147733, ECO:0000269|PubMed:15201283}.; . . 0.18842 0.12378 . . 810.92229 5.60058 DUSP26 0.003914765174449 0.85427423995989 0.141810994865661 dual specificity phosphatase 26 (putative) FUNCTION: Inactivates MAPK1 and MAPK3 which leads to dephosphorylation of heat shock factor protein 4 and a reduction in its DNA-binding activity. Inhibits MAP kinase p38 by dephosphorylating it and inhibits p38-mediated apoptosis in anaplastic thyroid cancer cells. Can also induce activation of MAP kinase p38 and c-Jun N-terminal kinase (JNK). {ECO:0000269|PubMed:15796912, ECO:0000269|PubMed:16581800, ECO:0000269|PubMed:16924234, ECO:0000269|PubMed:17001450}.; . TISSUE SPECIFICITY: Brain. In the brain it is expressed ubiquitously except in the hippocampus. Expressed in embryonal cancers (retinoblastoma, neuroepithilioma and neuroblastoma) and in anaplatic thyroid cancer. {ECO:0000269|PubMed:15796912, ECO:0000269|PubMed:16581800, ECO:0000269|PubMed:16924234, ECO:0000269|PubMed:17001450}.; unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;fovea centralis;choroid;lens;skeletal muscle;retina;pancreas;prostate;optic nerve;whole body;lung;bone;macula lutea;visual apparatus;hippocampus;liver;testis;spleen;brain;cerebellum; subthalamic nucleus;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;globus pallidus;pons;skeletal muscle;cingulate cortex;parietal lobe;cerebellum; 0.20217 0.12218 -0.293801652 32.93819297 33.74643 1.03945 DUSP27 2.04584346521462e-15 0.00761556984387641 0.992384430156122 dual specificity phosphatase 27 (putative) . . . unclassifiable (Anatomical System);lung;ovary;heart;larynx;thyroid;placenta;muscle;colon;head and neck;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.17012 . 0.973628696 90.27482897 2123.65841 8.48218 DUSP28 0.23221694539441 0.645973264244093 0.121809790361497 dual specificity phosphatase 28 . . . unclassifiable (Anatomical System);ovary;islets of Langerhans;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;whole body;lung;placenta;macula lutea;liver;testis;spleen;kidney;mammary gland; superior cervical ganglion;trigeminal ganglion; 0.21695 0.12783 -0.293801652 32.93819297 189.5586 2.98903 DUT 0.339206865298345 0.64646207523173 0.0143310594699254 deoxyuridine triphosphatase FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000269|PubMed:8805593}.; . TISSUE SPECIFICITY: Found in a variety of tissues. Isoform 3 expression is constitutive, while isoform 2 expression correlates with the onset of DNA replication (at protein level). Isoform 2 degradation coincides with the cessation of nuclear DNA replication (at protein level). {ECO:0000269|PubMed:9228092}.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;lung;pia mater;nasopharynx;placenta;head and neck;kidney;stomach;aorta; amygdala;whole brain;dorsal root ganglion;superior cervical ganglion;tumor;atrioventricular node;bone marrow;uterus;prostate;thyroid;prefrontal cortex;ciliary ganglion;trigeminal ganglion;thymus; 0.89615 0.49535 . . 20.06802 0.68582 DUTP1 . . . deoxyuridine triphosphatase pseudogene 1 . . . . . . . . . . . DUTP2 . . . deoxyuridine triphosphatase pseudogene 2 . . . . . . . . . . . DUTP3 . . . deoxyuridine triphosphatase pseudogene 3 . . . . . . . . . . . DUTP4 . . . deoxyuridine triphosphatase pseudogene 4 . . . . . . . . . . . DUTP5 . . . deoxyuridine triphosphatase pseudogene 5 . . . . . . . . . . . DUTP6 . . . deoxyuridine triphosphatase pseudogene 6 . . . . . . . . . . . DUTP7 . . . deoxyuridine triphosphatase pseudogene 7 . . . . . . . . . . . DUTP8 . . . deoxyuridine triphosphatase pseudogene 8 . . . . . . . . . . . DUX1 . . . double homeobox 1 FUNCTION: Probable transcription activator. Binds the P5 DNA element sequence 5'-GATCTGAGTCTAATTGAGAATTACTGTAC-3'. {ECO:0000269|PubMed:9736770}.; . TISSUE SPECIFICITY: Expressed in rhabdomyosarcoma TE671 cells as well as in several other normal and cancer cells. {ECO:0000269|PubMed:9736770}.; . . . . . . . . DUX3 . . . double homeobox 3 . . TISSUE SPECIFICITY: Expressed in hepatoma Hep3B cells. {ECO:0000269|PubMed:11245978}.; . . . . . . . . DUX4 . . . double homeobox 4 FUNCTION: Involved in transcriptional regulation. May regulate microRNA (miRNA) expression. {ECO:0000269|PubMed:10433963, ECO:0000269|PubMed:24145033}.; DISEASE: Facioscapulohumeral muscular dystrophy 1 (FSHD1) [MIM:158900]: A degenerative muscle disease characterized by slowly progressive weakness of the muscles of the face, upper-arm, and shoulder girdle. The onset of symptoms usually occurs in the first or second decade of life. Affected individuals usually present with impairment of upper extremity elevation. This tends to be followed by facial weakness, primarily involving the orbicularis oris and orbicularis oculi muscles. {ECO:0000269|PubMed:10433963, ECO:0000269|PubMed:19320656}. Note=The gene represented in this entry is involved in disease pathogenesis. The disease is caused by deletion of an integral number of units of a 3.3-kb tandem repeats, termed D4Z4 macrosatellite, located on chromosome 4q35. In unaffected subjects, the D4Z4 array consists of 11-150 repeats, while in FSHD1 patients, the array is reduced to 1-10 repeats (PubMed:19320656). DUX4 is located in D4Z4 macrosatellite which is epigenetically repressed in somatic tissues. D4Z4 chromatin relaxation in FSHD1 results in inefficient epigenetic repression of DUX4 and a variegated pattern of DUX4 protein expression in a subset of skeletal muscle nuclei. Ectopic expression of DUX4 in skeletal muscle activates the expression of stem cell and germline genes, and, when overexpressed in somatic cells, DUX4 can ultimately lead to cell death. {ECO:0000269|PubMed:19320656}.; TISSUE SPECIFICITY: Does not seem to be expressed in normal muscle, but is detected in muscle of individuals with FSHD, and also in testis (at protein level) (PubMed:21060811). Does not seem to be expressed in normal muscle, but in muscle of individuals with FSHD, where it may be toxic to cells. {ECO:0000269|PubMed:10433963, ECO:0000269|PubMed:21060811}.; . . . . . . . . DUX4L1 . . . double homeobox 4 like 1 FUNCTION: Involved in transcriptional regulation. May regulate microRNA (miRNA) expression. {ECO:0000269|PubMed:10433963, ECO:0000269|PubMed:24145033}.; DISEASE: Facioscapulohumeral muscular dystrophy 1 (FSHD1) [MIM:158900]: A degenerative muscle disease characterized by slowly progressive weakness of the muscles of the face, upper-arm, and shoulder girdle. The onset of symptoms usually occurs in the first or second decade of life. Affected individuals usually present with impairment of upper extremity elevation. This tends to be followed by facial weakness, primarily involving the orbicularis oris and orbicularis oculi muscles. {ECO:0000269|PubMed:10433963, ECO:0000269|PubMed:19320656}. Note=The gene represented in this entry is involved in disease pathogenesis. The disease is caused by deletion of an integral number of units of a 3.3-kb tandem repeats, termed D4Z4 macrosatellite, located on chromosome 4q35. In unaffected subjects, the D4Z4 array consists of 11-150 repeats, while in FSHD1 patients, the array is reduced to 1-10 repeats (PubMed:19320656). DUX4 is located in D4Z4 macrosatellite which is epigenetically repressed in somatic tissues. D4Z4 chromatin relaxation in FSHD1 results in inefficient epigenetic repression of DUX4 and a variegated pattern of DUX4 protein expression in a subset of skeletal muscle nuclei. Ectopic expression of DUX4 in skeletal muscle activates the expression of stem cell and germline genes, and, when overexpressed in somatic cells, DUX4 can ultimately lead to cell death. {ECO:0000269|PubMed:19320656}.; TISSUE SPECIFICITY: Does not seem to be expressed in normal muscle, but is detected in muscle of individuals with FSHD, and also in testis (at protein level) (PubMed:21060811). Does not seem to be expressed in normal muscle, but in muscle of individuals with FSHD, where it may be toxic to cells. {ECO:0000269|PubMed:10433963, ECO:0000269|PubMed:21060811}.; . . . . . . . . DUX4L2 . . . double homeobox 4 like 2 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . . . DUX4L3 . . . double homeobox 4 like 3 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . . . DUX4L4 . . . double homeobox 4 like 4 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . 3.40274 0.12434 DUX4L5 . . . double homeobox 4 like 5 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . . . DUX4L6 . . . double homeobox 4 like 6 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . . . DUX4L7 . . . double homeobox 4 like 7 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . . . DUX4L8 . . . double homeobox 4 like 8 . . . . . . . . . . . DUX4L9 . . . double homeobox 4 like 9 FUNCTION: May be involved in transcriptional regulation (By similarity). Down-regulates MYOD1 expression and may up-regulate MYF5 expression. May regulate microRNA (miRNA) transcription, upregulating the expression of some myogenic miRNAs, including MIR1-1, MIR133A2, MIR133B and MIR206. Impairs the differentiation of myoblasts and may be involved in muscle regeneration. {ECO:0000250, ECO:0000269|PubMed:18723017, ECO:0000269|PubMed:19829708, ECO:0000269|PubMed:24145033}.; DISEASE: Note=Up-regulated in myoblasts of facioscapulohumeral muscular dystrophy (FSHD) patients (at protein level). {ECO:0000269|PubMed:19829708}.; TISSUE SPECIFICITY: Expressed in muscles, as well as in primary myoblasts and myotubes (at protein level). {ECO:0000269|PubMed:19829708}.; . . . . . . . . DUX4L10 . . . double homeobox 4 like 10 . . . . . . . . . . . DUX4L11 . . . double homeobox 4 like 11 . . . . . . . . . . . DUX4L12 . . . double homeobox 4 like 12 . . . . . . . . . . . DUX4L13 . . . double homeobox 4 like 13 . . . . . . . . . . . DUX4L14 . . . double homeobox 4 like 14 . . . . . . . . . . . DUX4L15 . . . double homeobox 4 like 15 . . . . . . . . . . . DUX4L16 . . . double homeobox 4 like 16 . . . . . . . . . . . DUX4L17 . . . double homeobox 4 like 17 . . . . . . . . . . . DUX4L18 . . . double homeobox 4 like 18 . . . . . . . . . . . DUX4L19 . . . double homeobox 4 like 19 . . . . . . . . . . . DUX4L20 . . . double homeobox 4 like 20 . . . . . . . . . . . DUX4L21 . . . double homeobox 4 like 21 . . . . . . . . . . . DUX4L22 . . . double homeobox 4 like 22 . . . . . . . . . . . DUX4L23 . . . double homeobox 4 like 23 . . . . . . . . . . . DUX4L24 . . . double homeobox 4 like 24 . . . . . . . . . . . DUX4L25 . . . double homeobox 4 like 25 . . . . . . . . . . . DUX4L26 . . . double homeobox 4 like 26 . . . . . . . . . . . DUX4L27 . . . double homeobox 4 like 27 . . . . . . . . . . . DUX4L28 . . . double homeobox 4 like 28 . . . . . . . . . . . DUX4L29 . . . double homeobox 4 like 29 . . . . . . . . . . . DUX4L31 . . . double homeobox 4 like 31 (pseudogene) . . . . . . . . . . . DUX4L32 . . . double homeobox 4 like 32 (pseudogene) . . . . . . . . . . . DUX4L33 . . . double homeobox 4 like 33 (pseudogene) . . . . . . . . . . . DUX4L34 . . . double homeobox 4 like 34 (pseudogene) . . . . . . . . . . . DUX4L35 . . . double homeobox 4 like 35 (pseudogene) . . . . . . . . . . . DUX4L36 . . . double homeobox 4 like 36 (pseudogene) . . . . . . . . . . . DUX4L37 . . . double homeobox 4 like 37 (pseudogene) . . . . . . . . . . . DUX4L38 . . . double homeobox 4 like 38 (pseudogene) . . . . . . . . . . . DUX4L39 . . . double homeobox 4 like 39 (pseudogene) . . . . . . . . . . . DUX4L40 . . . double homeobox 4 like 40 (pseudogene) . . . . . . . . . . . DUX4L41 . . . double homeobox 4 like 41 (pseudogene) . . . . . . . . . . . DUX4L42 . . . double homeobox 4 like 42 (pseudogene) . . . . . . . . . . . DUX4L43 . . . double homeobox 4 like 43 (pseudogene) . . . . . . . . . . . DUX4L44 . . . double homeobox 4 like 44 (pseudogene) . . . . . . . . . . . DUX4L45 . . . double homeobox 4 like 45 (pseudogene) . . . . . . . . . . . DUX4L46 . . . double homeobox 4 like 46 (pseudogene) . . . . . . . . . . . DUX4L47 . . . double homeobox 4 like 47 (pseudogene) . . . . . . . . . . . DUX4L48 . . . double homeobox 4 like 48 (pseudogene) . . . . . . . . . . . DUX4L49 . . . double homeobox 4 like 49 (pseudogene) . . . . . . . . . . . DUX4L50 . . . double homeobox 4 like 50 (pseudogene) . . . . . . . . . . . DUX4L51 . . . double homeobox 4 like 51 (pseudogene) . . . . . . . . . . . DUX4L52 . . . double homeobox 4 like 52 (pseudogene) . . . . . . . . . . . DUX5 . . . double homeobox 5 . . TISSUE SPECIFICITY: Expressed in hepatoma Hep3B cells. {ECO:0000269|PubMed:11245978}.; . . . . . . . . DUXA 3.05558525416354e-05 0.557922776527085 0.442046667620373 double homeobox A FUNCTION: Putative transcription factor. {ECO:0000250}.; . . . . 0.11265 0.08793 0.237127192 68.98443029 20.69426 0.70223 DUXAP1 . . . double homeobox A pseudogene 1 . . . . . . . . . . . DUXAP2 . . . double homeobox A pseudogene 2 . . . . . . . . . . . DUXAP3 . . . double homeobox A pseudogene 3 . . . . . . . . . . . DUXAP4 . . . double homeobox A pseudogene 4 . . . . . . . . . . . DUXAP5 . . . double homeobox A pseudogene 5 . . . . . . . . . . . DUXAP6 . . . double homeobox A pseudogene 6 . . . . . . . . . . . DUXAP7 . . . double homeobox A pseudogene 7 . . . . . . . . . . . DUXAP8 . . . double homeobox A pseudogene 8 . . . . . . . . . . . DUXAP9 . . . double homeobox A pseudogene 9 . . . . . . . . . . . DUXAP10 . . . double homeobox A pseudogene 10 . . . . . . . . . . . DUXAP11 . . . double homeobox A pseudogene 11 . . . . . . . . . . . DUXAP12 . . . double homeobox A pseudogene 12 . . . . . . . . . . . DUXB . . . double homeobox B . . . . . . . . . . . DVL1 0.157164971605877 0.842152650553916 0.000682377840206944 dishevelled segment polarity protein 1 FUNCTION: Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ).; DISEASE: Robinow syndrome, autosomal dominant 2 (DRS2) [MIM:616331]: A rare skeletal dysplasia syndrome characterized by dysmorphic features resembling a fetal face, mesomelic limb shortening, hypoplastic external genitalia in males, costovertebral segmentation defects, and renal anomalies. {ECO:0000269|PubMed:25817014, ECO:0000269|PubMed:25817016}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;kidney;stomach; prefrontal cortex;skeletal muscle; . . -1.168429872 6.062750649 128.03318 2.46667 DVL1P1 . . . dishevelled segment polarity protein 1 pseudogene 1 FUNCTION: May play a role in the signal transduction pathway mediated by multiple Wnt genes.; . TISSUE SPECIFICITY: Expressed in thymus, heart, liver, kidney, brain, skeletal muscle, and pancreas. {ECO:0000269|PubMed:8644734}.; . . . . . . . . DVL2 0.011361463937534 0.988275687015362 0.000362849047104128 dishevelled segment polarity protein 2 FUNCTION: Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes (By similarity). {ECO:0000250, ECO:0000269|PubMed:19252499}.; . . lymphoreticular;medulla oblongata;ovary;adrenal medulla;colon;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lung;epididymis;placenta;visual apparatus;hippocampus;duodenum;cervix;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis;globus pallidus;ciliary ganglion;atrioventricular node;cingulate cortex;cerebellum; 0.91956 0.21432 -1.212529868 5.691200755 215.16746 3.16537 DVL3 0.995402942345558 0.00459703976236269 1.78920794847031e-08 dishevelled segment polarity protein 3 FUNCTION: May play a role in the signal transduction pathway mediated by multiple Wnt genes.; . . lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;breast;lung;epididymis;placenta;macula lutea;visual apparatus;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;placenta;ciliary ganglion;trigeminal ganglion; 0.63158 0.17697 -0.955204708 9.170794999 109.50412 2.27316 DWS . . . dandy-walker syndrome . . . . . . . . . . . DXO 4.98479742091705e-10 0.0586914681153949 0.941308531386125 decapping exoribonuclease FUNCTION: Ribonuclease that specifically degrades pre-mRNAs with a defective 5' end cap and is part of a pre-mRNA capping quality control. Has decapping, pyrophosphohydrolase and 5'-3' exonuclease activities. Has decapping activity toward incomplete 5' end cap mRNAs such as unmethylated 5' end-capped RNA to release GpppN and 5' end monophosphate RNA. The 5' end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs. Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5' end triphosphate to release pyrophosphates (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9799600}.; . . 0.36515 . 0.174625237 65.9648502 1139.50418 6.43746 DYDC1 0.00206579247169306 0.74419376812796 0.253740439400347 DPY30 domain containing 1 FUNCTION: Plays a crucial role during acrosome biogenesis. {ECO:0000269|PubMed:19545932}.; . TISSUE SPECIFICITY: Brain and testis. Accumulates during late stage of spermiogenesis. {ECO:0000269|PubMed:19545932}.; . . 0.14943 0.07339 -0.029247611 51.40363293 8.72381 0.32065 DYDC2 0.0233122399240471 0.769496689908513 0.20719107016744 DPY30 domain containing 2 . . . optic nerve;lung;macula lutea;testis;fovea centralis;choroid;lens;brain;skin;retina; trachea;atrioventricular node;trigeminal ganglion; 0.04717 0.06217 0.880130671 88.9596603 209.76007 3.12596 DYM 5.18111501130597e-09 0.951560786386507 0.0484392084323782 dymeclin FUNCTION: Necessary for correct organization of Golgi apparatus. Involved in bone development. {ECO:0000269|PubMed:21280149}.; DISEASE: Dyggve-Melchior-Clausen syndrome (DMC) [MIM:223800]: A rare autosomal recessive disorder belonging to the group of spondyloepimetaphyseal dysplasias. DMC is characterized by progressive short stature with short trunk dwarfism, microcephaly, protruding sternum, and psychomotor retardation. Radiological features include a platyspondyly with double vertebral humps, an epiphyso-metaphyseal dysplasia and lacy pelvis iliac crests. {ECO:0000269|PubMed:12491225, ECO:0000269|PubMed:12554689}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Smith-McCort dysplasia 1 (SMC1) [MIM:607326]: A rare autosomal recessive osteochondrodysplasia with skeletal features identical to those of Dyggve-Melchior-Clausen syndrome, but with normal intelligence and no microcephaly. It is characterized by short limbs and trunk with barrel-shaped chest. The radiographic phenotype includes platyspondyly, generalized abnormalities of the epiphyses and metaphyses, and a distinctive lacy appearance of the iliac crest. {ECO:0000269|PubMed:12491225, ECO:0000269|PubMed:19005420}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in most embryo-fetal and adult tissues. Abundant in primary chondrocytes, osteoblasts, cerebellum, kidney, lung, stomach, heart, pancreas and fetal brain. Very low or no expression in the spleen, thymus, esophagus, bladder and thyroid gland. {ECO:0000269|PubMed:12554689, ECO:0000269|PubMed:18996921}.; ovary;colon;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;muscle;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach; superior cervical ganglion;trigeminal ganglion; 0.17392 0.16362 -0.753139731 13.67067705 143.40049 2.61130 DYNAP 0.409402930300484 0.553549683748271 0.0370473859512452 dynactin associated protein FUNCTION: Plays a role in the regulation of cell proliferation. Promotes activation of the AKT1 signaling pathway. Promotes phosphorylation of AKT1 at 'Ser-473'. {ECO:0000269|PubMed:20978158}.; . TISSUE SPECIFICITY: Expressed in fibroblast and numerous cancer cell lines (at protein level). {ECO:0000269|PubMed:20978158}.; . . 0.09111 . 0.681699246 84.93158764 55.04137 1.48653 DYNC1H1 1 5.9534498588438e-24 9.61798541804241e-61 dynein cytoplasmic 1 heavy chain 1 FUNCTION: Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.; DISEASE: Charcot-Marie-Tooth disease 2O (CMT2O) [MIM:614228]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. {ECO:0000269|PubMed:21820100, ECO:0000269|PubMed:24307404, ECO:0000269|PubMed:25512093}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mental retardation, autosomal dominant 13 (MRD13) [MIM:614563]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD13 is associated with variable neuronal migration defects and mild dysmorphic features. Some patients may also show signs of peripheral neuropathy, such as abnormal gait and hyporeflexia. {ECO:0000269|PubMed:21076407, ECO:0000269|PubMed:22368300, ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:23603762}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spinal muscular atrophy, lower extremity-predominant 1, autosomal dominant (SMALED1) [MIM:158600]: A form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. SMALED1 is characterized by muscle weakness predominantly affecting the proximal lower extremities. {ECO:0000269|PubMed:22459677, ECO:0000269|PubMed:22847149, ECO:0000269|PubMed:25512093}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; dorsal root ganglion;whole brain;amygdala;medulla oblongata;thalamus;occipital lobe;superior cervical ganglion;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.46830 0.37481 -6.0104656 0.041283322 935.72699 5.93050 DYNC1I1 0.0116377037964894 0.988291362265978 7.09339375331077e-05 dynein cytoplasmic 1 intermediate chain 1 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150- glued) DCNT1. May play a role in mediating the interaction of cytoplasmic dynein with membranous organelles and kinetochores.; . . ovary;salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;iris;testis;bladder;pineal gland;brain;amygdala;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;lung;trabecular meshwork;hippocampus;macula lutea;visual apparatus;liver;kidney; dorsal root ganglion;whole brain;amygdala;thalamus;superior cervical ganglion;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;atrioventricular node;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.27887 0.19826 -0.578583623 18.71903751 149.80256 2.66880 DYNC1I2 5.18719626749822e-07 0.960355696907867 0.0396437843725061 dynein cytoplasmic 1 intermediate chain 2 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150- glued) DCNT1. Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes.; . . smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;gall bladder;heart;tongue;spinal cord;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; . 0.21410 0.19929 -0.582225231 18.44184949 26.9112 0.86987 DYNC1I2P1 . . . dynein cytoplasmic 1 intermediate chain 2 pseudogene 1 . . . . . . . . . . . DYNC1LI1 0.977918890005446 0.0220802709362754 8.39058278808122e-07 dynein cytoplasmic 1 light intermediate chain 1 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress throuh the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores. {ECO:0000269|PubMed:19229290}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;cerebellum;thymus; amygdala;subthalamic nucleus;testis; 0.81000 . 0.50895761 80.20169851 609.20306 4.99003 DYNC1LI2 0.798419344341552 0.201531047007338 4.9608651109385e-05 dynein cytoplasmic 1 light intermediate chain 2 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes.; . . lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;placenta;head and neck;kidney;stomach; subthalamic nucleus;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.34546 0.09320 -0.692458599 14.96815287 29.20904 0.93355 DYNC2H1 2.1785373082787e-21 0.999999999999998 1.91434385965646e-15 dynein cytoplasmic 2 heavy chain 1 FUNCTION: May function as a motor for intraflagellar retrograde transport. Functions in cilia biogenesis. May play a role in transport between endoplasmic reticulum and Golgi or organization of the Golgi in cells (By similarity). {ECO:0000250}.; DISEASE: Short-rib thoracic dysplasia 3 with or without polydactyly (SRTD3) [MIM:613091]: A form of short-rib thoracic dysplasia, a group of autosomal recessive ciliopathies that are characterized by a constricted thoracic cage, short ribs, shortened tubular bones, and a 'trident' appearance of the acetabular roof. Polydactyly is variably present. Non-skeletal involvement can include cleft lip/palate as well as anomalies of major organs such as the brain, eye, heart, kidneys, liver, pancreas, intestines, and genitalia. Some forms of the disease are lethal in the neonatal period due to respiratory insufficiency secondary to a severely restricted thoracic cage, whereas others are compatible with life. Disease spectrum encompasses Ellis-van Creveld syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-Saldino syndrome, and short rib-polydactyly syndrome. {ECO:0000269|PubMed:19361615, ECO:0000269|PubMed:19442771, ECO:0000269|PubMed:22499340, ECO:0000269|PubMed:23456818}. Note=The disease is caused by mutations affecting the gene represented in this entry. In some cases DYNC2H1 mutations result in disease phenotype in the presence of mutations in NEK1 indicating digenic inheritance (digenic short rib-polydactyly syndrome 3/6 with polydactyly) (PubMed:21211617). {ECO:0000269|PubMed:21211617}.; . unclassifiable (Anatomical System);heart;endometrium;skeletal muscle; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12011 0.10624 -0.347849649 29.56475584 5392.75345 15.15350 DYNC2LI1 8.37968944079953e-05 0.927454684065915 0.0724615190396766 dynein cytoplasmic 2 light intermediate chain 1 FUNCTION: May function as a motor for intraflagellar retrograde transport. Functions in cilia biogenesis (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;cerebellum; testis - interstitial;globus pallidus;atrioventricular node; 0.05380 0.08230 1.596607091 95.87166785 1692.77547 7.58315 DYNLL1 0.696580483081237 0.28628993224683 0.017129584671933 dynein light chain LC8-type 1 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.; FUNCTION: Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8628263}.; myocardium;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;germinal center;bladder;brain;amygdala;spinal cord;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;vein;uterus;cerebral cortex;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;kidney;stomach;aorta; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;olfactory bulb;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;testis;cingulate cortex;parietal lobe;cerebellum; 0.09560 0.09513 0.12325821 62.38499646 . . DYNLL1P1 . . . dynein light chain LC8-type 1 pseudogene 1 . . . . . . . . . . . DYNLL1P2 . . . dynein light chain LC8-type 1 pseudogene 2 . . . . . . . . . . . DYNLL1P3 . . . dynein light chain LC8-type 1 pseudogene 3 . . . . . . . . . . . DYNLL1P4 . . . dynein light chain LC8-type 1 pseudogene 4 . . . . . . . . . . . DYNLL1P5 . . . dynein light chain LC8-type 1 pseudogene 5 . . . . . . . . . . . DYNLL1P6 . . . dynein light chain LC8-type 1 pseudogene 6 . . . . . . . . . . . DYNLL1P7 . . . dynein light chain LC8-type 1 pseudogene 7 . . . . . . . . . . . DYNLL2 0.687802227346452 0.293642017582155 0.0185557550713934 dynein light chain LC8-type 2 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;colon;choroid;uterus;prostate;lung;frontal lobe;trabecular meshwork;visual apparatus;testis;kidney;brain;aorta; testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.44131 . 0.057118534 57.99716914 . . DYNLRB1 0.842802760335196 0.15430594846779 0.00289129119701372 dynein light chain roadblock-type 1 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.; . TISSUE SPECIFICITY: High expression in heart, liver, brain and pancreas; moderate in placenta, skeletal muscle and kidney; low in lung, prostate, testis, small intestine and colon. Isoform 1 expression is up-regulated in 64% hepatocellular carcinoma (HCC) patients. {ECO:0000269|PubMed:11750132}.; lymphoreticular;smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;kidney;stomach;aorta; dorsal root ganglion;whole brain;amygdala;medulla oblongata;superior cervical ganglion;thalamus;occipital lobe;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.08178 0.16827 -0.009020804 52.8544468 5.11603 0.18972 DYNLRB2 0.390767288946825 0.567200733016393 0.0420319780367825 dynein light chain roadblock-type 2 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.; . TISSUE SPECIFICITY: High expression in heart, brain, placenta, skeletal muscle, prostate and small intestine; moderate in kidney, pancreas, spleen, testis, ovary and colon; low in lung, liver, thymus and leukocyte.; unclassifiable (Anatomical System);lung;nasopharynx;placenta;macula lutea;testis;fovea centralis;kidney; testis - interstitial;trachea;testis - seminiferous tubule;testis;caudate nucleus; 0.17004 0.12971 0.080983847 59.76055674 66.91731 1.69010 DYNLT1 0.0392109729198064 0.839414506414042 0.121374520666151 dynein light chain Tctex-type 1 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Binds to transport cargos and is involved in apical cargo transport such as rhodopsin-bearing vesicles in polarized epithelia. Is involved in intracellular targeting of D-type retrovirus gag polyproteins to the cytoplasmic assembly site. May also be a accessory component of axonemal dynein. {ECO:0000269|PubMed:18647839}.; . TISSUE SPECIFICITY: Expressed in heart, placenta, skeletal muscle kidney, pancreas, spleen, prostate, testis, ovary, ileum and colon. Expressed in lung endothelial and smooth muscle cells (at protein level). {ECO:0000269|PubMed:14583445}.; . . 0.37148 0.23984 -0.119252484 44.53880632 8.35132 0.30562 DYNLT3 0.650718442302593 0.323788392156481 0.0254931655409251 dynein light chain Tctex-type 3 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Probably binds BUB3 as part of transport cargo. Required for the efficient progression through mitosis (By similarity). {ECO:0000250}.; . . . . 0.07994 0.11010 -0.009020804 52.8544468 273.84756 3.54509 DYNLT3P1 . . . dynein light chain Tctex-type 3 pseudogene 1 . . . . . . . . . . . DYNLT3P2 . . . dynein light chain Tctex-type 3 pseudogene 2 . . . . . . . . . . . DYRK1A 0.999584541726647 0.000415458021545489 2.51807787327076e-10 dual specificity tyrosine phosphorylation regulated kinase 1A FUNCTION: May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Modulates alternative splicing by phosphorylating the splice factor SRSF6 (By similarity). Phosphorylates serine, threonine and tyrosine residues in its sequence and in exogenous substrates such as CRY2, FOXO1, SRSF6 and SIRT1. Exhibits a sugstrate preference for proline at position P+1 and arginine at position P-3. {ECO:0000250, ECO:0000269|PubMed:20981014, ECO:0000269|PubMed:21127067, ECO:0000269|PubMed:23665168, ECO:0000269|PubMed:8769099}.; DISEASE: Mental retardation, autosomal dominant 7 (MRD7) [MIM:614104]: A disease characterized by primary microcephaly, severe mental retardation without speech, anxious autistic behavior, and dysmorphic features, including bitemporal narrowing, deep-set eyes, large simple ears, and a pointed nasal tip. Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:21294719}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Highest levels in skeletal muscle, testis, fetal lung and fetal kidney. {ECO:0000269|PubMed:10329007, ECO:0000269|PubMed:8769099, ECO:0000269|PubMed:8872470, ECO:0000269|PubMed:8975710}.; myocardium;medulla oblongata;smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;cerebellum peduncles;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex; 0.65395 0.31640 -0.422438699 25.64284029 45.78305 1.30076 DYRK1AIP1 . . . DYRK1A interacting protein 1 . . . . . . . . . . . DYRK1AIP2 . . . DYRK1A interacting protein 2 . . . . . . . . . . . DYRK1B 0.915927122253969 0.0840489613023407 2.39164436900913e-05 dual specificity tyrosine phosphorylation regulated kinase 1B FUNCTION: Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. Enhances the transcriptional activity of TCF1/HNF1A and FOXO1. Inhibits epithelial cell migration. Mediates colon carcinoma cell survival in mitogen-poor environments. Inhibits the SHH and WNT1 pathways, thereby enhancing adipogenesis. In addition, promotes expression of the gluconeogenic enzyme glucose-6-phosphatase (G6PC). {ECO:0000269|PubMed:10910078, ECO:0000269|PubMed:11980910, ECO:0000269|PubMed:14500717, ECO:0000269|PubMed:24827035}.; DISEASE: Abdominal obesity-metabolic syndrome 3 (AOMS3) [MIM:615812]: A form of abdominal obesity-metabolic syndrome, a disorder characterized by abdominal obesity, high triglycerides, low levels of high density lipoprotein cholesterol, high blood pressure, and elevated fasting glucose levels. AOMS3 is characterized by early-onset coronary artery disease, central obesity, hypertension, and diabetes. {ECO:0000269|PubMed:24827035}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest expression in skeletal muscle, testis, heart and brain with little expression in colon or lung. Expressed in a variety of tumor cell lines. {ECO:0000269|PubMed:10910078}.; medulla oblongata;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;pancreas;lung;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; thalamus;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;atrioventricular node; 0.65474 0.16753 -0.844966979 11.1759849 75.91525 1.82590 DYRK2 0.979337328880354 0.0206453082770054 1.73628426402399e-05 dual specificity tyrosine phosphorylation regulated kinase 2 FUNCTION: Serine/threonine-protein kinase involved in the regulation of the mitotic cell cycle, cell proliferation, apoptosis, organization of the cytoskeleton and neurite outgrowth. Functions in part via its role in ubiquitin-dependent proteasomal protein degradation. Functions downstream of ATM and phosphorylates p53/TP53 at 'Ser-46', and thereby contributes to the induction of apoptosis in response to DNA damage. Phosphorylates NFATC1, and thereby inhibits its accumulation in the nucleus and its transcription factor activity. Phosphorylates EIF2B5 at 'Ser-544', enabling its subsequent phosphorylation and inhibition by GSK3B. Likewise, phosphorylation of NFATC1, CRMP2/DPYSL2 and CRMP4/DPYSL3 promotes their subsequent phosphorylation by GSK3B. May play a general role in the priming of GSK3 substrates. Inactivates GYS1 by phosphorylation at 'Ser- 641', and potentially also a second phosphorylation site, thus regulating glycogen synthesis. Mediates EDVP E3 ligase complex formation and is required for the phosphorylation and subsequent degradation of KATNA1. Phosphorylates TERT at 'Ser-457', promoting TERT ubiquitination by the EDVP complex. Phosphorylates SIAH2, and thereby increases its ubiquitin ligase activity. Promotes the proteasomal degradation of MYC and JUN, and thereby regulates progress through the mitotic cell cycle and cell proliferation. Promotes proteasomal degradation of GLI2 and GLI3, and thereby plays a role in smoothened and sonic hedgehog signaling. Plays a role in cytoskeleton organization and neurite outgrowth via its phosphorylation of DCX and DPYSL2. Phosphorylates CRMP2/DPYSL2, CRMP4/DPYSL3, DCX, EIF2B5, EIF4EBP1, GLI2, GLI3, GYS1, JUN, MDM2, MYC, NFATC1, p53/TP53, TAU/MAPT and KATNA1. Can phosphorylate histone H1, histone H3 and histone H2B (in vitro). Can phosphorylate CARHSP1 (in vitro). {ECO:0000269|PubMed:11311121, ECO:0000269|PubMed:12588975, ECO:0000269|PubMed:14593110, ECO:0000269|PubMed:15910284, ECO:0000269|PubMed:16511445, ECO:0000269|PubMed:16611631, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:18455992, ECO:0000269|PubMed:18599021, ECO:0000269|PubMed:19287380, ECO:0000269|PubMed:22307329, ECO:0000269|PubMed:22878263, ECO:0000269|PubMed:23362280, ECO:0000269|PubMed:9748265}.; . TISSUE SPECIFICITY: Testis, after the onset of spermatogenesis. {ECO:0000269|PubMed:9748265}.; unclassifiable (Anatomical System);ovary;colon;blood;skeletal muscle;retina;bone marrow;uterus;bile duct;pancreas;whole body;lung;larynx;bone;placenta;pituitary gland;duodenum;liver;testis;head and neck;kidney;germinal center;brain;stomach;thymus; superior cervical ganglion;fetal brain;appendix;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.64278 0.25662 -0.578583623 18.71903751 58.22856 1.54445 DYRK3 0.000220921842662409 0.743229160329982 0.256549917827355 dual specificity tyrosine phosphorylation regulated kinase 3 FUNCTION: Negative regulator of EPO-dependent erythropoiesis, may place an upper limit on red cell production during stress erythropoiesis. Inhibits cell death due to cytokine withdrawal in hematopoietic progenitor cells. May act by regulating CREB/CRE signaling. {ECO:0000269|PubMed:10779429}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed in testis and in hematopoietic tissue such as fetal liver, and bone marrow. Isoform 2 is the predominant form in testis. Isoform 1 is the predominant form in fetal liver and bone marrow. Isoform 1 and isoform 2 are present at low levels in heart, pancreas, lymph node, and thymus. {ECO:0000269|PubMed:10779429}.; . . 0.18710 0.10907 0.174625237 65.9648502 210.86296 3.13235 DYRK4 3.79608758155986e-10 0.175755298082675 0.824244701537716 dual specificity tyrosine phosphorylation regulated kinase 4 FUNCTION: Possible non-essential role in spermiogenesis. {ECO:0000250}.; . . medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;cerebellum cortex;tongue;blood;lens;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;spinal cord;testis; 0.06395 0.07590 7.61E-05 53.98089172 818.07757 5.61998 DYSF 1.00255104624413e-15 0.999999362011487 6.37988511916368e-07 dysferlin FUNCTION: Key calcium ion sensor involved in the Ca(2+)-triggered synaptic vesicle-plasma membrane fusion. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress (By similarity). {ECO:0000250}.; DISEASE: Limb-girdle muscular dystrophy 2B (LGMD2B) [MIM:253601]: An autosomal recessive degenerative myopathy characterized by weakness and atrophy starting in the proximal pelvifemoral muscles, with onset in the late teens or later, massive elevation of serum creatine kinase levels and slow progression. Scapular muscle involvement is minor and not present at onset. Upper limb girdle involvement follows some years after the onset in lower limbs. {ECO:0000269|PubMed:10196377, ECO:0000269|PubMed:11134403, ECO:0000269|PubMed:14678801, ECO:0000269|PubMed:15469449, ECO:0000269|PubMed:16010686, ECO:0000269|PubMed:16100712, ECO:0000269|PubMed:16705711, ECO:0000269|PubMed:16996541, ECO:0000269|PubMed:17287450, ECO:0000269|PubMed:18306167, ECO:0000269|PubMed:18853459, ECO:0000269|PubMed:9731526}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Miyoshi muscular dystrophy 1 (MMD1) [MIM:254130]: A late- onset muscular dystrophy involving the distal lower limb musculature. It is characterized by weakness that initially affects the gastrocnemius muscle during early adulthood. {ECO:0000269|PubMed:10196377, ECO:0000269|PubMed:11134403, ECO:0000269|PubMed:11468312, ECO:0000269|PubMed:12796534, ECO:0000269|PubMed:15116377, ECO:0000269|PubMed:15469449, ECO:0000269|PubMed:15477515, ECO:0000269|PubMed:15515206, ECO:0000269|PubMed:16010686, ECO:0000269|PubMed:16100712, ECO:0000269|PubMed:17287450, ECO:0000269|PubMed:18306167, ECO:0000269|PubMed:18853459, ECO:0000269|PubMed:9731526, ECO:0000269|Ref.26}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Distal myopathy with anterior tibial onset (DMAT) [MIM:606768]: Onset of the disorder is between 14 and 28 years of age and the anterior tibial muscles are the first muscle group to be involved. Inheritance is autosomal recessive. {ECO:0000269|PubMed:11198284}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in skeletal muscle, myoblast, myotube and in the syncytiotrophoblast (STB) of the placenta (at protein level). Ubiquitous. Highly expressed in skeletal muscle. Also found in heart, brain, spleen, intestine, placenta and at lower levels in liver, lung, kidney and pancreas. {ECO:0000269|PubMed:10196375, ECO:0000269|PubMed:11532985, ECO:0000269|PubMed:11959863, ECO:0000269|PubMed:15318348, ECO:0000269|PubMed:16896923, ECO:0000269|PubMed:17185750, ECO:0000269|PubMed:17363620, ECO:0000269|PubMed:17554076, ECO:0000269|PubMed:24239457}.; colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;thyroid;iris;testis;brain;unclassifiable (Anatomical System);amygdala;tongue;muscle;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland; placenta; 0.18661 0.30664 -1.309065031 4.853739089 1760.18248 7.74393 DYT2 . . . dystonia 2, torsion (autosomal recessive) . . . . . . . . . . . DYT7 . . . dystonia 7, torsion (autosomal dominant) . . . . . . . . . . . DYT13 . . . dystonia 13, torsion . . . . . . . . . . . DYT15 . . . dystonia 15, myoclonic . . . . . . . . . . . DYT17 . . . dystonia 17 . . . . . . . . . . . DYT21 . . . dystonia 21, torsion (autosomal dominant) . . . . . . . . . . . DYT22 . . . dystonia 22 . . . . . . . . . . . DYTN 2.804133893579e-15 0.00916508912409923 0.990834910875898 dystrotelin . . . . . . . 2.645930833 98.82637414 1193.19407 6.55238 DYX1 . . . dyslexia susceptibility 1 . . . . . . . . . . . DYX1C1 4.61254731939258e-07 0.614200833510026 0.385798705235242 dyslexia susceptibility 1 candidate 1 FUNCTION: Involved in neuronal migration during development of the cerebral neocortex. May regulate the stability and proteasomal degradation of the estrogen receptors that play an important role in neuronal differentiation, survival and plasticity. Axonemal dynein assembly factor required for ciliary motility. {ECO:0000269|PubMed:19423554, ECO:0000269|PubMed:23872636}.; DISEASE: Ciliary dyskinesia, primary, 25 (CILD25) [MIM:615482]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia. Patients may exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:23872636, ECO:0000269|PubMed:25186273}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in several tissues, including brain, lung, kidney and testis. In brain localizes to a fraction of cortical neurons and white matter glial cells. {ECO:0000269|PubMed:12954984}.; . . 0.09828 0.08410 1.087645262 91.8494928 2741.31251 9.87265 DYX1C1-CCPG1 . . . DYX1C1-CCPG1 readthrough (NMD candidate) . . . unclassifiable (Anatomical System);bile duct;pancreas;lung;bone;testis;kidney;brain;skin;stomach; . . . . . . . DYX2 . . . dyslexia susceptibility 2 . . . . . . . . . . . DYX3 . . . dyslexia susceptibility 3 . . . . . . . . . . . DYX4 . . . dyslexia susceptibility 4 . . . . . . . . . . . DYX5 . . . dyslexia susceptibility 5 . . . . . . . . . . . DYX6 . . . dyslexia susceptibility 6 . . . . . . . . . . . DYX7 . . . dyslexia susceptibility 7 . . . . . . . . . . . DYX8 . . . dyslexia susceptibility 8 . . . . . . . . . . . DYX9 . . . dyslexia susceptibility 9 . . . . . . . . . . . DZANK1 4.59513480508911e-15 0.0448525755380905 0.955147424461905 double zinc ribbon and ankyrin repeat domains 1 . . . parathyroid;choroid;fovea centralis;skin;retina;uterus;whole body;optic nerve;frontal lobe;endometrium;bone;iris;testis;brain;unclassifiable (Anatomical System);hypothalamus;lens;skeletal muscle;lung;mesenchyma;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;macula lutea;liver;kidney; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04900 0.07349 0.53464283 81.00967209 3603.71823 11.61957 DZIP1 3.32705692527064e-12 0.700868375154268 0.299131624842405 DAZ interacting zinc finger protein 1 FUNCTION: May participate in spermatogenesis via its interaction with DAZ (PubMed:15081113). Has a role in primary cilium formation (PubMed:19852954). {ECO:0000269|PubMed:15081113, ECO:0000269|PubMed:19852954}.; . TISSUE SPECIFICITY: Predominantly expressed in testis. Also expressed in fetal brain, adult oocytes and ovary. Expressed in undifferentiated ES cells. In testis, it is probably specifically expressed in germ cells. Expressed in mature germ cells and secondary spermatocytes, while it is weakly or not expressed in primary spermatocytes. {ECO:0000269|PubMed:15081113}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;oesophagus;bone;testis;bladder;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;kidney; amygdala;occipital lobe;superior cervical ganglion;testis - interstitial;medulla oblongata;hypothalamus;temporal lobe;atrioventricular node;pons;skeletal muscle;fetal brain;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion; 0.25522 0.09891 -0.685180376 15.32200991 1904.19832 8.02915 DZIP1L 6.92918542273119e-20 0.000906046993159829 0.99909395300684 DAZ interacting zinc finger protein 1 like FUNCTION: Has a role in primary cilium formation. {ECO:0000269|PubMed:19852954}.; . . unclassifiable (Anatomical System);pancreas;lung;ovary;nasopharynx;placenta;parathyroid;kidney;brain;skin;bone marrow; dorsal root ganglion;testis - interstitial;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.13926 0.08833 0.007353605 54.12243454 177.86229 2.89807 DZIP3 3.74220282201281e-10 0.999836768583973 0.000163231041806959 DAZ interacting zinc finger protein 3 FUNCTION: E3 Ubiquitin ligase proteins mediate ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Able to specifically bind RNA. {ECO:0000269|PubMed:12538761}.; . TISSUE SPECIFICITY: Widely expressed at low level. Highly expressed in skeletal muscle, kidney and heart. Expressed at low level in placenta, lung, brain, liver and pancreas. {ECO:0000269|PubMed:12538761}.; ovary;sympathetic chain;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;lens;skeletal muscle;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach; amygdala;dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;hypothalamus;prefrontal cortex;testis;globus pallidus;atrioventricular node;skeletal muscle;parietal lobe; 0.08364 0.09530 -1.102280959 6.912007549 427.18655 4.31766 E2F1 0.95553054498313 0.0443535976703024 0.000115857346567997 E2F transcription factor 1 FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC- 3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can mediate both cell proliferation and TP53/p53-dependent apoptosis. Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters (PubMed:20176812). {ECO:0000250|UniProtKB:Q61501, ECO:0000269|PubMed:10675335, ECO:0000269|PubMed:12717439, ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:20176812, ECO:0000269|PubMed:8170954}.; . . lymphoreticular;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;cervix;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.99293 0.79067 0.306902668 72.38145789 145.79444 2.63160 E2F2 0.914702778499156 0.0851748960893124 0.000122325411531943 E2F transcription factor 2 FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC- 3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from g1 to s phase. E2F2 binds specifically to RB1 in a cell-cycle dependent manner.; . TISSUE SPECIFICITY: Highest level of expression is found in placenta, low levels are found in lung. Found as well in many immortalized cell lines derived from tumor samples.; ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;skeletal muscle;bile duct;breast;lung;placenta;visual apparatus;liver;spleen;kidney;stomach;thymus; skeletal muscle; 0.35536 0.19467 1.218120595 93.15876386 3750.11789 11.98253 E2F3 0.84245784569691 0.157417802750749 0.00012435155234081 E2F transcription factor 3 FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC- 3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F3 binds specifically to RB1 in a cell-cycle dependent manner. Inhibits adipogenesis, probably through the repression of CEBPA binding to its target gene promoters (By similarity). {ECO:0000250|UniProtKB:O35261}.; . . ovary;salivary gland;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;temporal lobe;prefrontal cortex;pons;whole blood;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.86757 0.09637 0.349177632 74.18023119 122.01208 2.40597 E2F3-IT1 . . . E2F3 intronic transcript 1 . . . . . . . . . . . E2F3P1 . . . E2F transcription factor 3 pseudogene 1 . . . . . . . . . . . E2F3P2 . . . E2F transcription factor 3 pseudogene 2 . . . . . . . . . . . E2F4 0.320999401239657 0.675507064993334 0.00349353376700854 E2F transcription factor 4 FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC- 3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F4 binds with high affinity to RBL1 and RBL2. In some instances can also bind RB1. Specifically required for multiciliate cell differentiation: together with MCIDAS and E2F5, binds and activate genes required for centriole biogenesis. {ECO:0000250|UniProtKB:Q6DE14, ECO:0000269|PubMed:7958924, ECO:0000269|PubMed:7958925}.; . TISSUE SPECIFICITY: Found in all tissue examined including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; . . 0.87542 0.29794 -0.736552314 13.93606983 30.36322 0.96838 E2F4P1 . . . E2F transcription factor 4 pseudogene 1 . . . . . . . . . . . E2F5 0.0263290981712336 0.919367982004903 0.0543029198238636 E2F transcription factor 5 FUNCTION: Transcriptional activator that binds to E2F sites, these sites are present in the promoter of many genes whose products are involved in cell proliferation. May mediate growth factor- initiated signal transduction. It is likely involved in the early responses of resting cells to growth factor stimulation. Specifically required for multiciliate cell differentiation: together with MCIDAS and E2F5, binds and activate genes required for centriole biogenesis. {ECO:0000250|UniProtKB:Q6DE14}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;lens;breast;bile duct;lung;cornea;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; tumor; 0.82126 0.17937 0.191216164 66.57230479 151.0009 2.68649 E2F6 0.55450901223844 0.442677636924132 0.00281335083742833 E2F transcription factor 6 FUNCTION: Inhibitor of E2F-dependent transcription. Binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3'. Has a preference for the 5'-TTTCCCGC-3' E2F recognition site. E2F6 lacks the transcriptional activation and pocket protein binding domains. Appears to regulate a subset of E2F-dependent genes whose products are required for entry into the cell cycle but not for normal cell cycle progression. May silence expression via the recruitment of a chromatin remodeling complex containing histone H3-K9 methyltransferase activity. Overexpression delays the exit of cells from the S-phase.; . TISSUE SPECIFICITY: Expressed in all tissues examined. Highest levels in placenta, skeletal muscle, heart, ovary, kidney, small intestine and spleen.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;bile duct;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;kidney;mammary gland;stomach; . 0.14447 0.13079 0.03689118 56.64071715 12.99441 0.47320 E2F6P1 . . . E2F transcription factor 6 pseudogene 1 . . . . . . . . . . . E2F6P2 . . . E2F transcription factor 6 pseudogene 2 . . . . . . . . . . . E2F6P3 . . . E2F transcription factor 6 pseudogene 3 . . . . . . . . . . . E2F6P4 . . . E2F transcription factor 6 pseudogene 4 . . . . . . . . . . . E2F7 0.423130675694931 0.576856072478697 1.32518263723208e-05 E2F transcription factor 7 FUNCTION: Atypical E2F transcription factor that participates in various processes such as angiogenesis, polyploidization of specialized cells and DNA damage response. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'- TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1. Acts as a regulator of S-phase by recognizing and binding the E2-related site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Also involved in DNA damage response: up-regulated by p53/TP53 following genotoxic stress and acts as a downstream effector of p53/TP53-dependent repression by mediating repression of indirect p53/TP53 target genes involved in DNA replication. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene. Acts as a negative regulator of keratinocyte differentiation. {ECO:0000269|PubMed:14633988, ECO:0000269|PubMed:15133492, ECO:0000269|PubMed:18202719, ECO:0000269|PubMed:19223542, ECO:0000269|PubMed:21248772, ECO:0000269|PubMed:22802528, ECO:0000269|PubMed:22802529, ECO:0000269|PubMed:22903062}.; . . unclassifiable (Anatomical System);medulla oblongata;adrenal cortex;colon;blood;skin;bone marrow;breast;lung;endometrium;larynx;bone;placenta;visual apparatus;alveolus;liver;testis;cervix;head and neck;spleen;germinal center;brain;stomach; superior cervical ganglion;ciliary ganglion;cerebellum; 0.12836 0.09736 0.093718683 60.71007313 193.44742 3.01697 E2F8 0.995041279088296 0.00495871655562556 4.35607795742843e-09 E2F transcription factor 8 FUNCTION: Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1: component of a feedback loop in S phase by repressing the expression of E2F1, thereby preventing p53/TP53-dependent apoptosis. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene. {ECO:0000269|PubMed:15897886, ECO:0000269|PubMed:16179649, ECO:0000269|PubMed:18202719, ECO:0000269|PubMed:22903062}.; . . unclassifiable (Anatomical System);ovary;parathyroid;skeletal muscle;breast;whole body;lung;placenta;liver;testis;spleen;germinal center;kidney;mammary gland; testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.39192 0.09135 -0.773369631 13.10450578 260.40561 3.46644 E4F1 0.434844067114666 0.56486024395203 0.000295688933304511 E4F transcription factor 1 FUNCTION: May function as a transcriptional repressor. May also function as a ubiquitin ligase mediating ubiquitination of chromatin-associated TP53. Functions in cell survival and proliferation through control of the cell cycle. Functions in the p53 and pRB tumor suppressor pathways and regulates the cyclin CCNA2 transcription.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9530632}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;tongue;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; heart;skeletal muscle; 0.78462 0.12258 -0.725642751 14.24274593 156.51441 2.73457 E11S . . . ECHO virus (serotypes 4, 6, 11, 19) sensitivity . . . . . . . . . . . EAF1 0.070565049762035 0.872131820088246 0.0573031301497195 ELL associated factor 1 FUNCTION: Acts as a transcriptional transactivator of ELL and ELL2 elongation activities. {ECO:0000269|PubMed:11418481, ECO:0000269|PubMed:16006523}.; . TISSUE SPECIFICITY: Strongly expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, prostate, testis, small intestine and colon. Poorly expressed in thymus. {ECO:0000269|PubMed:11418481}.; . . 0.14659 0.11262 0.61555716 83.13871196 38.43741 1.14048 EAF1-AS1 . . . EAF1 antisense RNA 1 . . . . . . . . . . . EAF2 0.000680757757036257 0.745494808971303 0.25382443327166 ELL associated factor 2 FUNCTION: Acts as a transcriptional transactivator of TCEA1 elongation activity (By similarity). Acts as a transcriptional transactivator of ELL and ELL2 elongation activities. Potent inducer of apoptosis in prostatic and non-prostatic cell lines. Inhibits prostate tumor growth in vivo. {ECO:0000250, ECO:0000269|PubMed:12446457, ECO:0000269|PubMed:12907652, ECO:0000269|PubMed:16006523}.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, skeletal muscle, kidney, pancreas, spleen, prostate, testis, small intestine, colon, adrenal, bone marrow, lymph node, spinal gland, stomach, thyroid, trachea, thymus, liver and leukocytes. {ECO:0000269|PubMed:12446457, ECO:0000269|PubMed:12907652}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;bone marrow;breast;prostate;lung;endometrium;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland;bladder;tonsil; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12883 0.11720 0.128714042 63.19886766 81.30921 1.90954 EAPP 2.71832573208649e-05 0.532738305171013 0.467234511571666 E2F associated phosphoprotein FUNCTION: May play an important role in the fine-tuning of both major E2F1 activities, the regulation of the cell-cycle and the induction of apoptosis. Promotes S-phase entry, and inhibits p14(ARP) expression. {ECO:0000269|PubMed:15716352}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highest levels in heart, placenta, skeletal muscle and pancreas. Lower levels in brain, lung and kidney. In the brain, expressed in all regions with high levels in the cerebellum and cerebral cortex. Expressed in COS1 and transformed skin fibroblasts. {ECO:0000269|PubMed:15716352, ECO:0000269|PubMed:15820313}.; medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;testis;germinal center;brain;artery;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; . 0.17724 0.11651 0.41713504 76.95800896 285.36442 3.61650 EARS2 2.07046774730899e-07 0.444791804560188 0.555207988393037 glutamyl-tRNA synthetase 2, mitochondrial FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). {ECO:0000250}.; DISEASE: Combined oxidative phosphorylation deficiency 12 (COXPD12) [MIM:614924]: An autosomal recessive, mitochondrial, neurologic disorder characterized by onset in infancy of hypotonia and delayed psychomotor development, or early developmental regression, associated with T2-weighted hyperintensities in the deep cerebral white matter, brainstem, and cerebellar white matter. Serum lactate is increased due to a defect in mitochondrial respiration. There are 2 main phenotypic groups: those with a milder disease course and some recovery of skills after age 2 years, and those with a severe disease course resulting in marked disability. {ECO:0000269|PubMed:22492562, ECO:0000269|PubMed:23008233}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;frontal lobe;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;cartilage;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;cervix;kidney; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.08986 0.38627 0.042348793 57.31304553 349.13506 3.95902 EBAG9 0.717057362958321 0.2797984459115 0.0031441911301791 estrogen receptor binding site associated, antigen, 9 FUNCTION: May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1- beta converting enzyme (ICE)-like proteases. {ECO:0000269|PubMed:12054692, ECO:0000269|PubMed:12138241, ECO:0000269|PubMed:12672804}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in ovary, testis, prostate, thymus, muscle and heart, but not in small intestine, colon, lymph nodes, or peripherical blood lymphocytes. The protein is not detected in any of the above organs.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;uterus;prostate;frontal lobe;endometrium;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; amygdala;subthalamic nucleus;superior cervical ganglion;occipital lobe;thyroid;temporal lobe;spinal cord; 0.21283 0.13584 -0.09720619 46.20193442 13.13583 0.47840 EBAG9P1 . . . estrogen receptor binding site associated, antigen, 9 pseudogene 1 . . . . . . . . . . . EBF1 0.996264496901181 0.00373544982967388 5.32691446121056e-08 early B-cell factor 1 FUNCTION: Transcriptional activator which recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3'. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;ovary;heart;parathyroid;blood;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;placenta;thyroid;macula lutea;visual apparatus;testis;head and neck;kidney;germinal center;mammary gland; superior cervical ganglion;cerebellum peduncles;cerebellum; 0.98970 0.28911 -0.47017169 23.25430526 46.86767 1.32389 EBF2 0.971965790083313 0.0280339035540616 3.06362625598298e-07 early B-cell factor 2 FUNCTION: Transcription factor that, in osteoblasts, activates the decoy receptor for RANKL, TNFRSF11B, which in turn regulates osteoclast differentiation. Acts in synergy with the Wnt- responsive LEF1/CTNNB1 pathway. Recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3' (By similarity). {ECO:0000250}.; . . . . . . -0.624497208 17.16206653 336.08683 3.89430 EBF3 0.998590013761644 0.00140998129125642 4.94709964493925e-09 early B-cell factor 3 FUNCTION: Transcriptional activator which recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3'. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:12355068}.; unclassifiable (Anatomical System);heart;ovary;parathyroid;blood;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;whole body;lung;endometrium;placenta;macula lutea;visual apparatus;liver;testis;spleen;kidney;mammary gland; . 0.13556 0.10822 -0.646543901 16.44255721 30.75664 0.97699 EBF4 0.0780569989244377 0.751474041191287 0.170468959884275 early B-cell factor 4 FUNCTION: Transcriptional factor which recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3'. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;endometrium;placenta;macula lutea;visual apparatus;testis;brain;stomach;gall bladder; superior cervical ganglion; 0.19920 0.09318 . . 46.6956 1.31968 EBI3 0.0195996499684184 0.901344485006813 0.0790558650247685 Epstein-Barr virus induced 3 FUNCTION: Associates with IL27 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. IL-27 has pro- and anti-inflammatory properties, that can regulate T- helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells, and that has diverse effects on innate immune cells. Among its target cells are CD4 T-helper cells which can differentiate in type 1 effector cells (TH1), type 2 effector cells (TH2) and IL17 producing helper T-cells (TH17). It drives rapid clonal expansion of naive but not memory CD4 T-cells. It also strongly synergizes with IL-12 to trigger interferon-gamma/IFN-gamma production of naive CD4 T-cells, binds to the cytokine receptor WSX-1/TCCR. Another important role of IL-27 is its antitumor activity as well as its antiangiogenic activity with activation of production of antiangiogenic chemokines. {ECO:0000269|PubMed:12121660}.; . . unclassifiable (Anatomical System);heart;ovary;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;placenta;macula lutea;liver;spleen;cervix;germinal center;tonsil; placenta; 0.08419 0.18579 -0.492218069 22.35786742 17.05573 0.60084 EBLN1 6.91019370514168e-05 0.163861145919072 0.836069752143876 endogenous Bornavirus-like nucleoprotein 1 FUNCTION: May act as an RNA-binding protein. Highly homologous to the bornavirus nucleocapsid N protein that binds viral RNA and oligomerizes (By similarity). {ECO:0000250}.; . . . . . . . . 8391.4152 19.77457 EBLN2 0.0865230043591697 0.761575808017695 0.151901187623135 endogenous Bornavirus-like nucleoprotein 2 FUNCTION: May act as an RNA-binding protein. The C-terminal region is highly homologous to the bornavirus nucleocapsid N protein that binds viral RNA and oligomerizes. The viral protein also possesses a nuclear import and a nuclear export signal. These 2 signals seem absent in EBLN-2 supporting an unrelated function in Human.; . . . . . . 0.905808022 89.4373673 1890.42342 7.99543 EBLN3 . . . endogenous Bornavirus-like nucleoprotein 3 . . . . . . . . . . . EBM . . . epidermolysis bullosa, macular type . . . . . . . . . . . EBNA1BP2 2.3767005478956e-06 0.905637200049021 0.0943604232504311 EBNA1 binding protein 2 FUNCTION: Required for the processing of the 27S pre-rRNA. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11327720}.; ovary;salivary gland;intestine;colon;parathyroid;vein;skin;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; globus pallidus; 0.29292 0.12704 0.41713504 76.95800896 643.22607 5.09641 EBP 0.858629818405411 0.139180627245459 0.00218955434912991 emopamil binding protein (sterol isomerase) FUNCTION: Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers.; DISEASE: Chondrodysplasia punctata 2, X-linked dominant (CDPX2) [MIM:302960]: A clinically and genetically heterogeneous disorder characterized by punctiform calcification of the bones. The key clinical features of CDPX2 are chondrodysplasia punctata, linear ichthyosis, cataracts and short stature. CDPX2 is a rare disorder of defective cholesterol biosynthesis, biochemically characterized by an increased amount of 8-dehydrocholesterol and cholest-8(9)- en-3-beta-ol in the plasma and tissues. {ECO:0000269|PubMed:10391218, ECO:0000269|PubMed:10391219, ECO:0000269|PubMed:10942423, ECO:0000269|PubMed:11493318, ECO:0000269|PubMed:18176751, ECO:0000269|PubMed:25814754}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: MEND syndrome (MEND) [MIM:300960]: An X-linked recessive disorder associated with a defect in sterol biosynthesis. Disease manifestations and severity are highly variable. Clinical features include intellectual disability, short stature, scoliosis, digital abnormalities, cataracts, and dermatologic abnormalities. {ECO:0000269|PubMed:12503101, ECO:0000269|PubMed:20949533, ECO:0000269|PubMed:24459067, ECO:0000269|PubMed:24700572}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;blood;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;stomach; . 0.25395 0.09869 -0.141298762 42.87567823 15.38266 0.55216 EBPL 0.0388533331243391 0.838493275488185 0.122653391387476 emopamil binding protein like FUNCTION: Does not possess sterol isomerase activity and does not bind sigma ligands. {ECO:0000269|PubMed:12760743}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in liver, lung and kidney. {ECO:0000269|PubMed:12760743}.; ovary;colon;skin;retina;bone marrow;uterus;prostate;cochlea;endometrium;larynx;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;skeletal muscle;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; liver; 0.05028 0.07010 -0.141298762 42.87567823 28.87736 0.92255 EBR3 . . . epidermolysis bullosa 3, progressiva . . . . . . . . . . . EBR4 . . . epidermolysis bullosa 4, pseudojunctional (intraepidermal) . . . . . . . . . . . EBVM1 . . . Epstein Barr virus modification site 1 . . . . . . . . . . . EBVS1 . . . Epstein Barr virus integration site 1 . . . . . . . . . . . ECA1 . . . epilepsy, childhood absence 1 . . . . . . . . . . . ECD 1.14934390390028e-09 0.758064251051079 0.241935747799577 ecdysoneless cell cycle regulator FUNCTION: Novel regulator of p53 stability and function. May also be a transcriptional activator required for the expression of glycolytic genes. {ECO:0000269|PubMed:16849563, ECO:0000269|PubMed:9928932}.; . TISSUE SPECIFICITY: Highly expressed in muscle and heart.; . . 0.18941 0.13143 0.047806932 57.51946214 6128.58348 16.34269 ECE1 0.999768645958376 0.000231353981139093 6.04845435976919e-11 endothelin converting enzyme 1 FUNCTION: Converts big endothelin-1 to endothelin-1. {ECO:0000269|PubMed:9396733}.; . TISSUE SPECIFICITY: All isoforms are expressed in umbilical vein endothelial cells, polynuclear neutrophils, fibroblasts, atrium cardiomyocytes and ventricles. Isoforms A, B and C are also expressed in placenta, lung, heart, adrenal gland and phaeochromocytoma; isoforms A and C in liver, testis and small intestine; isoform B, C and D in endothelial cells and umbilical vein smooth muscle cells; isoforms C and D in saphenous vein cells, and isoform C in kidney. {ECO:0000269|PubMed:10491078, ECO:0000269|PubMed:9396733}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;larynx;bone;thyroid;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;amnion;hypopharynx;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; adrenal gland;adrenal cortex;ciliary ganglion;pons;skeletal muscle; 0.31635 0.38954 -0.685180376 15.32200991 308.51135 3.73871 ECE2 1.65047866122531e-17 0.0431941048063052 0.956805895193695 endothelin converting enzyme 2 FUNCTION: Converts big endothelin-1 to endothelin-1. Also involved in the processing of various neuroendocrine peptides, including neurotensin, angiotensin I, substance P, proenkephalin-derived peptides, and prodynorphin-derived peptides. May limit beta- amyloid peptide accumulation in brain. May also have methyltransferase activity. {ECO:0000269|PubMed:12560336}.; . TISSUE SPECIFICITY: Expressed in brain. Strongly down-regulated in inferior parietal lobe from Alzheimer disease patients (at protein level). {ECO:0000269|PubMed:17188679}.; ovary;colon;choroid;fovea centralis;skin;retina;uterus;prostate;whole body;optic nerve;pituitary gland;testis;germinal center;brain;amygdala;unclassifiable (Anatomical System);islets of Langerhans;blood;lens;bile duct;lung;adrenal gland;visual apparatus;macula lutea;liver;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.15170 0.09790 -0.874545591 10.58622317 423.29385 4.29671 ECEL1 9.10967319793021e-05 0.999779536028043 0.000129367239977244 endothelin converting enzyme-like 1 FUNCTION: May contribute to the degradation of peptide hormones and be involved in the inactivation of neuronal peptides.; DISEASE: Arthrogryposis, distal, 5D (DA5D) [MIM:615065]: An autosomal recessive form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA5D is characterized by severe camptodactyly of the hands, mild camptodactyly of the toes, clubfoot and/or a calcaneovalgus deformity, extension contractures of the knee, unilateral ptosis or ptosis that is more severe on one side, a round-shaped face, arched eyebrows, a bulbous upturned nose, and micrognathia. Patients do not have ophthalmoplegia. {ECO:0000269|PubMed:23236030, ECO:0000269|PubMed:23261301, ECO:0000269|PubMed:23808592, ECO:0000269|PubMed:23829171}. Note=The disease is caused by mutations affecting the gene represented in this entry. ECEL1 mutations have also been found in patients with arthrogryposis, significant ophthalmoplegia, and refractive errors (PubMed:23808592). {ECO:0000269|PubMed:23808592}.; TISSUE SPECIFICITY: Highly expressed in the CNS, in particular in putamen, spinal cord, medulla and subthalamic nucleus. A strong signal was also detected in uterine subepithelial cells and around renal blood vessels. Detected at lower levels in amygdala, caudate, thalamus, pancreas and skeletal muscle. Detected at very low levels in substantia nigra, cerebellum, cortex, corpus callosum and hippocampus.; unclassifiable (Anatomical System);cartilage;tongue;fovea centralis;choroid;lung;endometrium;macula lutea;visual apparatus;duodenum;pituitary gland;head and neck;brain;tonsil;stomach; ovary;hypothalamus;temporal lobe;atrioventricular node;skeletal muscle; 0.12989 0.20455 0.003714825 54.06935598 432.34761 4.33992 ECEL1P1 . . . endothelin converting enzyme-like 1, pseudogene 1 . . . . . . . . . . . ECEL1P2 . . . endothelin converting enzyme-like 1, pseudogene 2 . . . . . . . . . . . ECEL1P3 . . . endothelin converting enzyme-like 1, pseudogene 3 . . . . . . . . . . . ECH1 0.00416642683428467 0.960890261368259 0.0349433117974563 enoyl-CoA hydratase 1, peroxisomal FUNCTION: Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4- trans-dienoyl-CoA. {ECO:0000250}.; . . myocardium;smooth muscle;ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach; . 0.09522 0.20323 0.196671391 67.19155461 2653.07243 9.67866 ECHDC1 6.03175404565904e-05 0.466856359346134 0.533083323113409 ethylmalonyl-CoA decarboxylase 1 FUNCTION: Decarboxylases ethylmalonyl-CoA decarboxylase, a potentially toxic metabolite, to form butyryl-CoA, suggesting it might be involved in metabolite proofreading. Also has methylmalonyl-CoA decarboxylase activity at lower level. {ECO:0000269|PubMed:22016388}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;liver;alveolus;spleen;kidney;stomach;peripheral nerve; superior cervical ganglion;adipose tissue; 0.08478 0.09737 -0.205617011 38.57631517 26.76863 0.86662 ECHDC2 1.18082144336839e-07 0.55967683815826 0.440323043759596 enoyl-CoA hydratase domain containing 2 . . . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;retina;uterus;prostate;optic nerve;cerebral cortex;oesophagus;endometrium;thyroid;testis;germinal center;spinal ganglion;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);lacrimal gland;tongue;islets of Langerhans;oral cavity;blood;skeletal muscle;lung;epididymis;placenta;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;liver;atrioventricular node;skeletal muscle; 0.08337 0.18096 0.062575634 58.74026893 116.86465 2.35220 ECHDC3 0.000536785623378491 0.45874964919374 0.540713565182882 enoyl-CoA hydratase domain containing 3 . . . . . 0.12334 0.16358 0.420771676 77.15852795 961.97162 6.00420 ECHS1 0.519800839729468 0.476505736814252 0.00369342345628061 enoyl-CoA hydratase, short chain, 1, mitochondrial FUNCTION: Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.; . TISSUE SPECIFICITY: Liver, fibroblast, muscle. Barely detectable in spleen and kidney.; . . 0.09269 . -0.071520315 48.34866714 11.5292 0.41686 ECI1 4.20005738223802e-10 0.0278988841123013 0.972101115467693 enoyl-CoA delta isomerase 1 FUNCTION: Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species.; . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;pineal body;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; prostate;heart;thyroid;liver;kidney;fetal thyroid; 0.07768 0.23871 0.064394823 58.84642604 126.52267 2.45024 ECI2 3.83619595564471e-09 0.0995847832842634 0.900415212879541 enoyl-CoA delta isomerase 2 FUNCTION: Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Abundant in heart, skeletal muscle and liver. Expressed in CD34(+) T-cells and CD34(+) bone marrow cells. {ECO:0000269|PubMed:15217832}.; myocardium;ovary;skin;prostate;cochlea;endometrium;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;spinal cord;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;vein;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; fetal liver;kidney; 0.08286 0.10164 0.308721233 72.59966973 3840.65595 12.19442 ECM1 7.32850722654138e-08 0.889468621246304 0.110531305468624 extracellular matrix protein 1 FUNCTION: Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity. {ECO:0000269|PubMed:11165938, ECO:0000269|PubMed:11292659, ECO:0000269|PubMed:16512877}.; . TISSUE SPECIFICITY: Expressed in breast cancer tissues. Little or no expression observed in normal breast tissues. Expressed in skin; wide expression is observed throughout the dermis with minimal expression in the epidermis. {ECO:0000269|PubMed:11292659, ECO:0000269|PubMed:12604605}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;oral cavity;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;tongue;placenta; 0.14850 0.30134 -0.26629572 34.81953291 2116.73281 8.46967 ECM1P1 . . . extracellular matrix protein 1 pseudogene 1 . . . . . . . . . . . ECM1P2 . . . extracellular matrix protein 1 pseudogene 2 . . . . . . . . . . . ECM2 1.56333125806507e-06 0.851722410099954 0.148276026568788 extracellular matrix protein 2, female organ and adipocyte specific FUNCTION: Promotes matrix assembly and cell adhesiveness. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed predominantly in adipose tissue as well as female-specific organs such as mammary gland, ovary, and uterus.; unclassifiable (Anatomical System);lung;ovary;nasopharynx;liver;testis;spleen;head and neck;kidney;mammary gland;skeletal muscle; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.08752 . 0.424410872 77.25878745 175.72328 2.88468 ECSCR . . . endothelial cell surface expressed chemotaxis and apoptosis regulator FUNCTION: Regulates endothelial chemotaxis and tube formation. Has a role in angiogenesis and apoptosis via modulation of the actin cytoskeleton and facilitation of proteasomal degradation of the apoptosis inhibitors BIRC3/IAP1 and BIRC2/IAP2. {ECO:0000269|PubMed:18556573, ECO:0000269|PubMed:19416853}.; . TISSUE SPECIFICITY: Highest expression in endothelial cells. Also detected in vascular smooth muscle, macrophages, lymphocytes, and mast cells. {ECO:0000269|PubMed:18556573, ECO:0000269|PubMed:19416853}.; . . . . . . 2.96298 0.10723 ECSIT 0.0156465744672347 0.958666354685652 0.025687070847113 ECSIT signalling integrator FUNCTION: Adapter protein of the Toll-like and IL-1 receptor signaling pathway that is involved in the activation of NF-kappa-B via MAP3K1. Promotes proteolytic activation of MAP3K1. Involved in the BMP signaling pathway. Required for normal embryonic development (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;pancreas;lung;nasopharynx;placenta;visual apparatus;duodenum;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve;cerebellum;thymus; heart; 0.16183 0.10428 -0.446304853 24.33356924 383.85954 4.13090 ECT2 2.55528752962742e-05 0.999941573590007 3.28735346967807e-05 epithelial cell transforming 2 FUNCTION: Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)- induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells, thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death. {ECO:0000269|PubMed:10579713, ECO:0000269|PubMed:14645260, ECO:0000269|PubMed:15254234, ECO:0000269|PubMed:15545273, ECO:0000269|PubMed:15642749, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16170345, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:16495035, ECO:0000269|PubMed:19129481, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19617897, ECO:0000269|PubMed:21189248, ECO:0000269|PubMed:21373644}.; . TISSUE SPECIFICITY: Expressed in lung epithelial cells (at protein level). Expressed in squamous cell carcinoma, primary non-small cell lung cancer tumors and lung adenocarcinoma. {ECO:0000269|PubMed:19617897}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.50680 0.12276 -0.865195027 10.79853739 372.8648 4.07379 ECT2L 7.34277312291911e-32 2.86167579029623e-06 0.99999713832421 epithelial cell transforming 2 like FUNCTION: May act as a guanine nucleotide exchange factor (GEF). {ECO:0000250}.; . . . . 0.13791 . 2.853641583 99.12125501 1954.13419 8.13625 EDA 0.922511722867168 0.077020895867089 0.000467381265743437 ectodysplasin A FUNCTION: Seems to be involved in epithelial-mesenchymal signaling during morphogenesis of ectodermal organs. Isoform 1 binds only to the receptor EDAR, while isoform 3 binds exclusively to the receptor XEDAR.; DISEASE: Ectodermal dysplasia 1, hypohidrotic, X-linked (XHED) [MIM:305100]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by sparse hair (atrichosis or hypotrichosis), abnormal or missing teeth and the inability to sweat due to the absence of sweat glands. It is the most common form of over 150 clinically distinct ectodermal dysplasias. {ECO:0000269|PubMed:10469321, ECO:0000269|PubMed:10951256, ECO:0000269|PubMed:11279189, ECO:0000269|PubMed:11295832, ECO:0000269|PubMed:11343303, ECO:0000269|PubMed:11378824, ECO:0000269|PubMed:12225002, ECO:0000269|PubMed:12932274, ECO:0000269|PubMed:17256800, ECO:0000269|PubMed:18231121, ECO:0000269|PubMed:19127222, ECO:0000269|PubMed:19438931, ECO:0000269|PubMed:20486090, ECO:0000269|PubMed:20979233, ECO:0000269|PubMed:22008666, ECO:0000269|PubMed:22350046, ECO:0000269|PubMed:8696334, ECO:0000269|PubMed:9507389, ECO:0000269|PubMed:9630076, ECO:0000269|PubMed:9683615, ECO:0000269|PubMed:9736768}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Tooth agenesis selective X-linked 1 (STHAGX1) [MIM:313500]: A form of selective tooth agenesis, a common anomaly characterized by the congenital absence of one or more teeth. Selective tooth agenesis without associated systemic disorders has sometimes been divided into 2 types: oligodontia, defined as agenesis of 6 or more permanent teeth, and hypodontia, defined as agenesis of less than 6 teeth. The number in both cases does not include absence of third molars (wisdom teeth). {ECO:0000269|PubMed:16583127, ECO:0000269|PubMed:18657636, ECO:0000269|PubMed:19278982, ECO:0000269|PubMed:23603338, ECO:0000269|PubMed:23625373, ECO:0000269|PubMed:24487376}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Not abundant; expressed in specific cell types of ectodermal (but not mesodermal) origin of keratinocytes, hair follicles, sweat glands. Also in adult heart, liver, muscle, pancreas, prostate, fetal liver, uterus, small intestine and umbilical chord. {ECO:0000269|Ref.6}.; . . 0.37117 0.09946 0.25917371 70.05779665 74.95239 1.81206 EDA2R 0.136305948867017 0.779886038882049 0.0838080122509341 ectodysplasin A2 receptor FUNCTION: Receptor for EDA isoform A2, but not for EDA isoform A1. Mediates the activation of the NF-kappa-B and JNK pathways. Activation seems to be mediated by binding to TRAF3 and TRAF6. {ECO:0000269|PubMed:12270937}.; . . unclassifiable (Anatomical System);liver;mammary gland; superior cervical ganglion; 0.01967 0.09742 0.483275131 79.25218212 36.62146 1.09938 EDAR 8.30571010658446e-05 0.926676769869595 0.0732401730293392 ectodysplasin A receptor FUNCTION: Receptor for EDA isoform A1, but not for EDA isoform A2. Mediates the activation of NF-kappa-B and JNK. May promote caspase-independent cell death.; DISEASE: Ectodermal dysplasia 10A, hypohidrotic/hair/nail type, autosomal dominant (ECTD10A) [MIM:129490]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. It is an autosomal dominant condition characterized by hypotrichosis, abnormal or missing teeth, and hypohidrosis due to the absence of sweat glands. {ECO:0000269|PubMed:10431241, ECO:0000269|PubMed:18231121}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ectodermal dysplasia 10B, hypohidrotic/hair/tooth type, autosomal recessive (ECTD10B) [MIM:224900]: A disorder due to abnormal development of two or more ectodermal structures, and characterized by sparse hair (atrichosis or hypotrichosis), abnormal or missing teeth and the inability to sweat due to the absence of sweat glands. {ECO:0000269|PubMed:10431241, ECO:0000269|PubMed:15373768, ECO:0000269|PubMed:16029325, ECO:0000269|PubMed:16435307, ECO:0000269|PubMed:18231121, ECO:0000269|PubMed:19438931, ECO:0000269|PubMed:20979233}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in fetal kidney, lung, skin and cultured neonatal epidermal keratinocytes. Not detected in lymphoblast and fibroblast cell lines.; uterus;lymphoreticular;prostate;whole body;heart;endometrium;colon;kidney;skin; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.19297 0.44715 -0.44448505 24.46331682 2615.65726 9.57676 EDARADD 0.103567654975129 0.864134435161007 0.032297909863864 EDAR-associated death domain FUNCTION: Adapter protein that interacts with EDAR DEATH domain and couples the receptor to EDA signaling pathway during morphogenesis of ectodermal organs. Mediates the activation of NF- kappa-B. {ECO:0000269|PubMed:11882293}.; DISEASE: Ectodermal dysplasia 11B, hypohidrotic/hair/tooth type, autosomal recessive (ECTD11B) [MIM:614941]: A disorder due to abnormal development of two or more ectodermal structures, and characterized by sparse hair (atrichosis or hypotrichosis), abnormal or missing teeth and the inability to sweat due to the absence of sweat glands. {ECO:0000269|PubMed:11780064, ECO:0000269|PubMed:20222921}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in adult pancreas, placenta and fetal skin, and at lower levels in lung, thymus, prostate and testis.; unclassifiable (Anatomical System);lymphoreticular;heart;islets of Langerhans;muscle;colon;skin;bile duct;pancreas;prostate;lung;endometrium;larynx;thyroid;liver;head and neck;cervix;bladder; . 0.12325 0.09383 0.193034296 66.82000472 94.90963 2.10085 EDC3 0.635930663137711 0.362647529795199 0.0014218070670892 enhancer of mRNA decapping 3 FUNCTION: Binds single-stranded RNA. Involved in the process of mRNA degradation and in the positive regulation of mRNA decapping. May play a role in spermiogenesis and oogenesis. {ECO:0000269|PubMed:16364915, ECO:0000269|PubMed:17533573, ECO:0000269|PubMed:18678652, ECO:0000269|PubMed:25701870}.; DISEASE: Mental retardation, autosomal recessive 50 (MRT50) [MIM:616460]: A form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT50 patients show mild intellectual disability and microcephaly. {ECO:0000269|PubMed:25701870}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in theca and granulosa cells in ovary, and in spermatids of the meiotic division part II and apical membrane of Sertoli cells in testis (at protein level). Also expressed in brain and mammary gland. {ECO:0000269|PubMed:17533573}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;muscle;blood;lens;breast;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; testis - interstitial;testis;pons;parietal lobe; 0.62984 0.12354 -0.071520315 48.34866714 44.6206 1.28133 EDC4 0.995195899401119 0.00480410059751381 1.36755609706201e-12 enhancer of mRNA decapping 4 FUNCTION: In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro). {ECO:0000269|PubMed:16364915}.; . . lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;peripheral nerve;cerebellum;thymus; testis - seminiferous tubule;prefrontal cortex;testis; 0.30148 0.16198 -1.434847051 3.998584572 87.70239 1.99974 EDDM3A 2.78870436637145e-09 0.0119806410659307 0.988019356145365 epididymal protein 3A FUNCTION: Possible function in sperm maturation.; . TISSUE SPECIFICITY: Epididymis, with predominant expression in the corpus region. Moderately expressed in the vas deferens; only low levels are detectable in the caput and cauda regions.; unclassifiable (Anatomical System);prostate;testis; superior cervical ganglion;temporal lobe;globus pallidus;testis;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.09268 . 0.881944684 89.02453409 1128.10842 6.40628 EDDM3B 0.0185127670928452 0.728783992385733 0.252703240521421 epididymal protein 3B FUNCTION: Possible function in sperm maturation.; . TISSUE SPECIFICITY: Epididymis.; testis; superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06898 0.11659 0.481458261 79.03986789 38.02005 1.12923 EDDM3CP . . . epididymal protein 3C, pseudogene . . . . . . . . . . . EDDM3DP . . . epididymal protein 3D, pseudogene . . . . . . . . . . . EDEM1 5.59576418489089e-11 0.365416395582507 0.634583604361535 ER degradation enhancer, mannosidase alpha-like 1 FUNCTION: Extracts misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. It is directly involved in endoplasmic reticulum-associated degradation (ERAD) and targets misfolded glycoproteins for degradation in an N-glycan-independent manner, probably by forming a complex with SEL1L. It has low mannosidase activity, catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2. {ECO:0000269|PubMed:12610306, ECO:0000269|PubMed:19524542, ECO:0000269|PubMed:19934218, ECO:0000269|PubMed:25092655}.; . . colon;parathyroid;vein;skin;bone marrow;uterus;prostate;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;lung;epididymis;placenta;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;placenta;skeletal muscle;thymus; 0.38273 0.14838 -0.955204708 9.170794999 194.45921 3.02231 EDEM2 0.000137533138342907 0.991394781252954 0.00846768560870323 ER degradation enhancer, mannosidase alpha-like 2 FUNCTION: Initiates the endoplasmic reticulum-associated degradation (ERAD) that targets misfolded glycoproteins for degradation in an N-glycan-dependent manner. Catalyzes the first mannose trimming step, from Man9GlcNAc2 to Man8GlcNAc2 (PubMed:25092655). Extracts misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. {ECO:0000269|PubMed:15537790, ECO:0000269|PubMed:15579471, ECO:0000269|PubMed:25092655}.; . TISSUE SPECIFICITY: Expressed ubiquitously in all tissues tested with slightly higher levels detected in small intestine and peripheral blood leukocytes and weakest levels in brain and skeletal muscle. {ECO:0000269|PubMed:15537790}.; . . 0.26467 0.11909 -0.089927255 46.99221515 349.6484 3.96234 EDEM3 0.122702493142942 0.877295703865225 1.80299183335777e-06 ER degradation enhancer, mannosidase alpha-like 3 FUNCTION: Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes, by catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2 in the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:25092655}.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;urinary;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.86373 0.11969 -0.663133267 15.94715735 464.80578 4.46599 EDF1 0.908576775721659 0.0907116196620351 0.000711604616306287 endothelial differentiation-related factor 1 FUNCTION: Transcriptional coactivator stimulating NR5A1 and ligand-dependent NR1H3/LXRA and PPARG transcriptional activities. Enhances the DNA-binding activity of ATF1, ATF2, CREB1 and NR5A1. Regulates nitric oxid synthase activity probably by sequestering calmodulin in the cytoplasm. May function in endothelial cells differentiation, hormone-induced cardiomyocytes hypertrophy and lipid metabolism. {ECO:0000269|PubMed:10567391, ECO:0000269|PubMed:12040021, ECO:0000269|PubMed:15112053, ECO:0000269|PubMed:9813014}.; . TISSUE SPECIFICITY: Expressed in brain, liver, lung, kidney and heart (at protein level). Ubiquitously expressed. More abundant in heart, pancreas, liver, intestine and adipose tissues. {ECO:0000269|PubMed:10567391, ECO:0000269|PubMed:12040021, ECO:0000269|PubMed:9813014}.; myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;vein;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;oral cavity;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; whole brain;subthalamic nucleus;cerebellum peduncles;skeletal muscle; 0.56285 0.18619 0.103030231 61.2762444 2.12304 0.07029 EDIL3 4.08771487713601e-05 0.990205566896933 0.00975355595429531 EGF like repeats and discoidin domains 3 FUNCTION: Promotes adhesion of endothelial cells through interaction with the alpha-v/beta-3 integrin receptor. Inhibits formation of vascular-like structures. May be involved in regulation of vascular morphogenesis of remodeling in embryonic development.; . . unclassifiable (Anatomical System);amygdala;heart;ovary;cartilage;hypothalamus;parathyroid;skin;skeletal muscle;retina;uterus;prostate;whole body;lung;frontal lobe;placenta;thyroid;bone;visual apparatus;hippocampus;testis;brain; whole brain;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.47277 0.13726 -0.426079032 25.36565228 65.31372 1.66299 EDN1 0.0810200671130622 0.872004581730739 0.0469753511561987 endothelin 1 FUNCTION: Endothelins are endothelium-derived vasoconstrictor peptides.; DISEASE: Auriculocondylar syndrome 3 (ARCND3) [MIM:615706]: A craniofacial malformation syndrome characterized by variable mandibular anomalies, including mild to severe micrognathia, temporomandibular joint ankylosis, cleft palate, and a characteristic ear malformation that consists of separation of the lobule from the external ear, giving the appearance of a question mark (question-mark ear). Other frequently described features include prominent cheeks, cupped and posteriorly rotated ears, preauricular tags, and microstomia. {ECO:0000269|PubMed:24268655}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in lung, placental stem villi vessels and in cultured placental vascular smooth muscle cells. {ECO:0000269|PubMed:9284755}.; . . 0.17971 0.75140 -0.205617011 38.57631517 747.20557 5.42362 EDN2 0.0110864412384733 0.838621290249539 0.150292268511988 endothelin 2 FUNCTION: Endothelins are endothelium-derived vasoconstrictor peptides.; . TISSUE SPECIFICITY: Expressed in lung, but not in placental stem villi vessels or cultured placental villi smooth muscle cells. {ECO:0000269|PubMed:9284755}.; . . 0.21013 0.23218 -0.095386216 46.48502005 827.07834 5.63702 EDN3 0.0723949084714923 0.872338251693349 0.055266839835159 endothelin 3 FUNCTION: Endothelins are endothelium-derived vasoconstrictor peptides.; DISEASE: Congenital central hypoventilation syndrome (CCHS) [MIM:209880]: Rare disorder characterized by abnormal control of respiration in the absence of neuromuscular or lung disease, or an identifiable brain stem lesion. A deficiency in autonomic control of respiration results in inadequate or negligible ventilatory and arousal responses to hypercapnia and hypoxemia. {ECO:0000269|PubMed:8696331}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Waardenburg syndrome 4B (WS4B) [MIM:613265]: A disorder characterized by the association of Waardenburg features (depigmentation and deafness) with the absence of enteric ganglia in the distal part of the intestine (Hirschsprung disease). {ECO:0000269|PubMed:11303518, ECO:0000269|PubMed:12189494, ECO:0000269|PubMed:8630503}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in trophoblasts and placental stem villi vessels, but not in cultured placental smooth muscle cells. {ECO:0000269|PubMed:9284755}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;hypothalamus;colon;choroid;skeletal muscle;pancreas;prostate;optic nerve;cochlea;endometrium;gum;thyroid;placenta;pituitary gland;liver;head and neck;spleen;brain;mammary gland;stomach;peripheral nerve; globus pallidus;atrioventricular node;skeletal muscle;pituitary;cingulate cortex; 0.37232 0.36965 -0.359940251 28.93371078 48.41222 1.35654 EDNRA 0.986016088385212 0.0139772626332455 6.64898154269879e-06 endothelin receptor type A FUNCTION: Receptor for endothelin-1. Mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. The rank order of binding affinities for ET-A is: ET1 > ET2 >> ET3.; . TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 4 are expressed in a variety of tissues, with highest levels in the aorta and cerebellum, followed by lung, atrium and cerebral cortex, lower levels in the placenta, kidney, adrenal gland, duodenum, colon, ventricle and liver but no expression in umbilical vein endothelial cells. Within the placenta, isoform 1, isoform 2, isoform 3 and isoform 4 are expressed in the villi and stem villi vessels. {ECO:0000269|PubMed:8611157, ECO:0000269|PubMed:9284755}.; ovary;colon;parathyroid;skin;uterus;prostate;whole body;cochlea;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;spinal cord;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;duodenum;amnion;spleen;head and neck;kidney;mammary gland;stomach;aorta; dorsal root ganglion;uterus;superior cervical ganglion;uterus corpus;prostate;ciliary ganglion;fetal lung;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.36973 0.41480 -0.383807564 27.41802312 6.56136 0.24247 EDNRB 0.0193615215886145 0.976633450998883 0.00400502741250214 endothelin receptor type B FUNCTION: Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. {ECO:0000269|PubMed:7536888}.; DISEASE: Waardenburg syndrome 4A (WS4A) [MIM:277580]: A disorder characterized by the association of Waardenburg features (depigmentation and deafness) with the absence of enteric ganglia in the distal part of the intestine (Hirschsprung disease). {ECO:0000269|PubMed:12189494, ECO:0000269|PubMed:8634719}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hirschsprung disease 2 (HSCR2) [MIM:600155]: A disorder of neural crest development characterized by absence of enteric ganglia along a variable length of the intestine. It is the most common cause of congenital intestinal obstruction. Early symptoms range from complete acute neonatal obstruction, characterized by vomiting, abdominal distention and failure to pass stool, to chronic constipation in the older child. {ECO:0000269|PubMed:8001158, ECO:0000269|PubMed:8630503, ECO:0000269|PubMed:8852659, ECO:0000269|PubMed:8852660}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: ABCD syndrome (ABCDS) [MIM:600501]: An autosomal recessive syndrome characterized by albinism, black lock at temporal occipital region, bilateral deafness, aganglionosis of the large intestine and total absence of neurocytes and nerve fibers in the small intestine. {ECO:0000269|PubMed:11891690}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in placental stem villi vessels, but not in cultured placental villi smooth muscle cells. {ECO:0000269|PubMed:9284755}.; medulla oblongata;ovary;sympathetic chain;substantia nigra;parathyroid;choroid;skin;retina;prostate;optic nerve;whole body;cochlea;bone;testis;amniotic fluid;artery;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;spinal cord;adrenal cortex;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; amygdala;dorsal root ganglion;superior cervical ganglion;hypothalamus;placenta;spinal cord;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.80070 0.72937 0.308721233 72.59966973 99.96482 2.16801 EDNRB-AS1 . . . EDNRB antisense RNA 1 . . . . . . . . . . . EDRF1 . . . erythroid differentiation regulatory factor 1 FUNCTION: Transcription factor involved in erythroid differentiation. Involved in transcriptional activation of the globin gene. {ECO:0000269|PubMed:12609092}.; . . . . 0.35494 0.10872 -0.771553417 13.15168672 855.81962 5.71248 EDRF1-AS1 . . . EDRF1 antisense RNA 1 . . . . . . . . . . . EEA1 0.6973588149443 0.302641184963463 9.22365737231111e-11 early endosome antigen 1 FUNCTION: Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking.; . . smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;whole body;frontal lobe;bone;thyroid;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;spinal cord;adrenal cortex;blood;skeletal muscle;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve; superior cervical ganglion;adrenal cortex;appendix;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.64608 0.35524 -0.547447733 19.99882048 354.71592 3.98395 EEC1 . . . ectrodactyly, ectodermal dysplasia and cleft lip/palate syndrome 1 . . . . . . . . . . . EEC2 . . . ectrodactyly, ectodermal dysplasia and cleft lip/palate syndrome 2 . . . . . . . . . . . EED 0.997671033484958 0.00232894969582419 1.68192175859177e-08 embryonic ectoderm development FUNCTION: Polycomb group (PcG) protein. Component of the PRC2/EED- EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A. {ECO:0000269|PubMed:10581039, ECO:0000269|PubMed:14532106, ECO:0000269|PubMed:15225548, ECO:0000269|PubMed:15231737, ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:20974918, ECO:0000269|PubMed:9584199}.; . TISSUE SPECIFICITY: Expressed in brain, colon, heart, kidney, liver, lung, muscle, ovary, peripheral blood leukocytes, pancreas, placenta, prostate, spleen, small intestine, testis, thymus and uterus. Appears to be overexpressed in breast and colon cancer. {ECO:0000269|PubMed:15684044, ECO:0000269|PubMed:9584199, ECO:0000269|PubMed:9765275, ECO:0000269|PubMed:9806832, ECO:0000269|PubMed:9880543}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;pharynx;blood;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;white blood cells;trigeminal ganglion;skeletal muscle; 0.92247 0.14896 -0.427900189 25.14744043 11.81975 0.42836 EEF1A1 0.984461027263021 0.0155303588071478 8.61392983076049e-06 eukaryotic translation elongation factor 1 alpha 1 FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. With PARP1 and TXK, forms a complex that acts as a T helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. {ECO:0000269|PubMed:17177976}.; . TISSUE SPECIFICITY: Brain, placenta, lung, liver, kidney, pancreas but barely detectable in heart and skeletal muscle.; ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;brain;heart;tongue;urinary;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; . 0.98787 0.69630 -0.273576253 33.97027601 10.98489 0.39784 EEF1A1P1 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 1 . . . . . . . . . . . EEF1A1P2 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 2 . . . . . . . . . . . EEF1A1P3 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 3 . . . . . . . . . . . EEF1A1P4 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 4 . . . . . . . . . . . EEF1A1P5 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 5 FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. {ECO:0000250}.; . . . . . 0.64919 . . . . EEF1A1P6 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 6 . . . . . . . . . . . EEF1A1P7 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 7 . . . . . . . . . . . EEF1A1P8 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 8 . . . . . . . . . . . EEF1A1P9 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 9 . . . . . . . . . . . EEF1A1P10 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 10 . . . . . . . . . . . EEF1A1P11 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 11 . . . . . . . . . . . EEF1A1P12 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 12 . . . . . . . . . . . EEF1A1P13 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 13 . . . . . . . . . . . EEF1A1P14 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 14 . . . . . . . . . . . EEF1A1P15 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 15 . . . . . . . . . . . EEF1A1P16 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 16 . . . . . . . . . . . EEF1A1P17 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 17 . . . . . . . . . . . EEF1A1P18 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 18 . . . . . . . . . . . EEF1A1P19 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 19 . . . . . . . . . . . EEF1A1P20 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 20 . . . . . . . . . . . EEF1A1P21 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 21 . . . . . . . . . . . EEF1A1P22 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 22 . . . . . . . . . . . EEF1A1P23 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 23 . . . . . . . . . . . EEF1A1P24 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 24 . . . . . . . . . . . EEF1A1P25 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 25 . . . . . . . . . . . EEF1A1P26 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 26 . . . . . . . . . . . EEF1A1P27 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 27 . . . . . . . . . . . EEF1A1P28 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 28 . . . . . . . . . . . EEF1A1P29 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 29 . . . . . . . . . . . EEF1A1P30 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 30 . . . . . . . . . . . EEF1A1P31 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 31 . . . . . . . . . . . EEF1A1P32 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 32 . . . . . . . . . . . EEF1A1P33 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 33 . . . . . . . . . . . EEF1A1P34 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 34 . . . . . . . . . . . EEF1A1P35 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 35 . . . . . . . . . . . EEF1A1P36 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 36 . . . . . . . . . . . EEF1A1P37 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 37 . . . . . . . . . . . EEF1A1P38 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 38 . . . . . . . . . . . EEF1A1P39 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 39 . . . . . . . . . . . EEF1A1P40 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 40 . . . . . . . . . . . EEF1A1P41 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 41 . . . . . . . . . . . EEF1A1P42 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 42 . . . . . . . . . . . EEF1A1P43 . . . eukaryotic translation elongation factor 1 alpha 1 pseudogene 43 . . . . . . . . . . . EEF1A2 0.96413145424868 0.0358006704304085 6.78753209114381e-05 eukaryotic translation elongation factor 1 alpha 2 FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.; DISEASE: Mental retardation, autosomal dominant 38 (MRD38) [MIM:616393]: A form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD38 common features are severe intellectual disability, autistic behavior, absent speech, neonatal hypotonia, epilepsy and progressive microcephaly. {ECO:0000269|PubMed:24697219}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Brain, heart, and skeletal muscle.; sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;pituitary gland;amniotic fluid;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;epididymis;macula lutea;visual apparatus;hippocampus;duodenum;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;temporal lobe;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.50184 0.47586 -0.670411825 15.61689078 2.10901 0.06894 EEF1AKMT1 . . . eukaryotic translation elongation factor 1 alpha lysine methyltransferase 1 FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that methylates elongation factor 1-alpha. {ECO:0000255|HAMAP-Rule:MF_03187}.; . . . . 0.11639 0.09343 0.038710339 56.92380278 . . EEF1B2 0.333347471841196 0.651668469061992 0.0149840590968127 eukaryotic translation elongation factor 1 beta 2 FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP.; . . myocardium;lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;frontal lobe;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach; . 0.27915 0.27706 -0.029247611 51.40363293 147.98282 2.65036 EEF1B2P1 . . . eukaryotic translation elongation factor 1 beta 2 pseudogene 1 . . . . . . . . . . . EEF1B2P2 . . . eukaryotic translation elongation factor 1 beta 2 pseudogene 2 . . . . . . . . . . . EEF1B2P3 . . . eukaryotic translation elongation factor 1 beta 2 pseudogene 3 . . . . . . . . . . . EEF1B2P4 . . . eukaryotic translation elongation factor 1 beta 2 pseudogene 4 . . . . . . . . . . . EEF1B2P5 . . . eukaryotic translation elongation factor 1 beta 2 pseudogene 5 . . . . . . . . . . . EEF1B2P6 . . . eukaryotic translation elongation factor 1 beta 2 pseudogene 6 . . . . . . . . . . . EEF1B2P7 . . . eukaryotic translation elongation factor 1 beta 2 pseudogene 7 . . . . . . . . . . . EEF1B2P8 . . . eukaryotic translation elongation factor 1 beta 2 pseudogene 8 . . . . . . . . . . . EEF1D 0.394239744215719 0.60535734382441 0.000402911959870776 eukaryotic translation elongation factor 1 delta FUNCTION: Isoform 1: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1- alpha for another round of transfer of aminoacyl-tRNAs to the ribosome.; . TISSUE SPECIFICITY: Isoform 2 is specifically expressed in brain, cerebellum and testis.; lymphoreticular;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;muscle;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;amnion;duodenum;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; pancreas;liver;adrenal cortex;white blood cells;skeletal muscle; 0.60061 . 0.34168906 73.72611465 589.16998 4.92122 EEF1DP1 . . . eukaryotic translation elongation factor 1 delta pseudogene 1 . . . . . . . . . . . EEF1DP2 . . . eukaryotic translation elongation factor 1 delta pseudogene 2 . . . . . . . . . . . EEF1DP3 . . . eukaryotic translation elongation factor 1 delta pseudogene 3 . . . . . . . . . . . EEF1DP4 . . . eukaryotic translation elongation factor 1 delta pseudogene 4 . . . . . . . . . . . EEF1DP5 . . . eukaryotic translation elongation factor 1 delta pseudogene 5 . . . . . . . . . . . EEF1DP6 . . . eukaryotic translation elongation factor 1 delta pseudogene 6 . . . . . . . . . . . EEF1DP7 . . . eukaryotic translation elongation factor 1 delta pseudogene 7 . . . . . . . . . . . EEF1DP8 . . . eukaryotic translation elongation factor 1 delta pseudogene 8 . . . . . . . . . . . EEF1E1 0.553269942523892 0.433477199295187 0.0132528581809216 eukaryotic translation elongation factor 1 epsilon 1 FUNCTION: Positive modulator of ATM response to DNA damage.; . TISSUE SPECIFICITY: Down-regulated in various cancer tissues. {ECO:0000269|PubMed:15680327}.; . . 0.88414 0.13991 -0.141298762 42.87567823 10.98126 0.39735 EEF1E1-BLOC1S5 . . . EEF1E1-BLOC1S5 readthrough (NMD candidate) . . . . . . . . . . . EEF1E1P1 . . . eukaryotic translation elongation factor 1 epsilon 1 pseudogene 1 . . . . . . . . . . . EEF1G 0.998058440819428 0.00194150584833994 5.33322324218227e-08 eukaryotic translation elongation factor 1 gamma FUNCTION: Probably plays a role in anchoring the complex to other cellular components.; . TISSUE SPECIFICITY: Highly expressed in pancreatic tumor tissue and to a lesser extent in normal kidney, intestine, pancreas, stomach, lung, brain, spleen and liver.; ovary;salivary gland;sympathetic chain;colon;vein;skin;uterus;prostate;whole body;frontal lobe;endometrium;oesophagus;gum;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;muscle;urinary;adrenal cortex;pharynx;blood;skeletal muscle;greater omentum;pancreas;lung;adrenal gland;placenta;liver;cervix;spleen;kidney;mammary gland;aorta;stomach;peripheral nerve; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.55420 0.39334 -0.449946534 24.00330267 12.73981 0.46355 EEF1GP1 . . . eukaryotic translation elongation factor 1 gamma pseudogene 1 . . . . . 0.55420 . . . . . EEF1GP2 . . . eukaryotic translation elongation factor 1 gamma pseudogene 2 . . . . . . . . . . . EEF1GP3 . . . eukaryotic translation elongation factor 1 gamma pseudogene 3 . . . . . . . . . . . EEF1GP4 . . . eukaryotic translation elongation factor 1 gamma pseudogene 4 . . . . . . . . . . . EEF1GP5 . . . eukaryotic translation elongation factor 1 gamma pseudogene 5 . . . . . . . . . . . EEF1GP6 . . . eukaryotic translation elongation factor 1 gamma pseudogene 6 . . . . . . . . . . . EEF1GP7 . . . eukaryotic translation elongation factor 1 gamma pseudogene 7 . . . . . . . . . . . EEF1GP8 . . . eukaryotic translation elongation factor 1 gamma pseudogene 8 . . . . . . . . . . . EEF2 0.994520586206042 0.00547938631788365 2.74760746010633e-08 eukaryotic translation elongation factor 2 FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.; DISEASE: Spinocerebellar ataxia 26 (SCA26) [MIM:609306]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. {ECO:0000269|PubMed:23001565}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; prostate;lung;adipose tissue;heart;thyroid;liver;kidney;cerebellum; 0.93627 0.50591 -2.280141674 1.238499646 10.26606 0.37454 EEF2K 8.33829176238637e-11 0.876537980454968 0.123462019461649 eukaryotic elongation factor 2 kinase FUNCTION: Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced. {ECO:0000269|PubMed:14709557, ECO:0000269|PubMed:9144159}.; . . ovary;developmental;colon;parathyroid;skin;retina;uterus;prostate;frontal lobe;endometrium;thyroid;bone;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;skeletal muscle;breast;pancreas;lung;placenta;liver;head and neck;cervix;kidney;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.10910 0.17393 -1.478950235 3.703703704 1351.44727 6.90569 EEF2KMT . . . eukaryotic elongation factor 2 lysine methyltransferase FUNCTION: Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on 'Lys-525'. {ECO:0000269|PubMed:25231979}.; . . . . . 0.10249 1.620475625 96.01321066 . . EEFSEC 0.0131152875630723 0.954167066754137 0.0327176456827911 eukaryotic elongation factor, selenocysteine-tRNA-specific FUNCTION: Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP.; . . lymphoreticular;ovary;colon;parathyroid;optic nerve;endometrium;thyroid;bone;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;muscle;adrenal cortex;pancreas;lung;placenta;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;kidney;trigeminal ganglion;cerebellum; 0.26555 0.26974 -0.376526807 28.10804435 263.47872 3.48275 EEGV1 . . . electro-encephalographic variant pattern 1 . . . . . . . . . . . EEPD1 0.00265719814434564 0.983083917217239 0.0142588846384155 endonuclease/exonuclease/phosphatase family domain containing 1 . . . lymphoreticular;umbilical cord;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;lens;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.24062 . -0.310388054 32.14791224 177.93918 2.89937 EFCAB1 0.000635897890174213 0.731800073279523 0.267564028830303 EF-hand calcium binding domain 1 . . . unclassifiable (Anatomical System);lung;heart;endometrium;alveolus;testis;spleen;head and neck;brain; ciliary ganglion; 0.10005 0.09904 -0.05129383 49.75819769 55.42984 1.49499 EFCAB2 7.50630911796469e-05 0.512099014158517 0.487825922750303 EF-hand calcium binding domain 2 . . . . . 0.15887 . -0.007201372 53.19061099 2225.85026 8.69721 EFCAB3 0.000159092434528578 0.967821674053753 0.0320192335117179 EF-hand calcium binding domain 3 . . . lung;cochlea;testis; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skin; . . 0.663285274 84.55414013 1537.30339 7.28318 EFCAB5 7.41783951945302e-16 0.798035783743655 0.201964216256344 EF-hand calcium binding domain 5 . . . unclassifiable (Anatomical System);lung;testis; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion; 0.13961 . 2.234196929 98.17763623 1355.8784 6.91005 EFCAB6 4.56556650101554e-19 0.653193486945154 0.346806513054846 EF-hand calcium binding domain 6 FUNCTION: Negatively regulates the androgen receptor by recruiting histone deacetylase complex, and protein DJ-1 antagonizes this inhibition by abrogation of this complex. {ECO:0000269|PubMed:12612053}.; . TISSUE SPECIFICITY: Specifically expressed in the testis. {ECO:0000269|PubMed:12612053}.; unclassifiable (Anatomical System);lung;testis;skeletal muscle;retina; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08485 0.08528 2.227005808 98.165841 2252.2218 8.76518 EFCAB6-AS1 . . . EFCAB6 antisense RNA 1 . . . . . . . . . . . EFCAB7 1.67071925383672e-12 0.189361538980885 0.810638461017444 EF-hand calcium binding domain 7 . . . . . 0.03745 . 1.622295219 96.0250059 3616.53403 11.65518 EFCAB8 . . . EF-hand calcium binding domain 8 . . . . . . . . . 1790.38994 7.81048 EFCAB9 . . . EF-hand calcium binding domain 9 . . . . . . . -0.053113545 49.38664779 177.32492 2.89375 EFCAB10 0.100686560719915 0.583579506306325 0.31573393297376 EF-hand calcium binding domain 10 . . . . . . . . . 17.61965 0.61719 EFCAB11 0.0202622727133803 0.903854941321241 0.0758827859653788 EF-hand calcium binding domain 11 . . . unclassifiable (Anatomical System);uterus;bile duct;lung;islets of Langerhans;visual apparatus;testis;colon;spleen;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.28532 0.10663 0.703746784 85.42108988 381.13617 4.11426 EFCAB12 2.17729967150611e-06 0.70883145949987 0.291166363200459 EF-hand calcium binding domain 12 . . . . . 0.11157 . 2.269130367 98.23071479 1905.18922 8.03479 EFCAB13 8.2199210022743e-19 0.0143771764972519 0.985622823502748 EF-hand calcium binding domain 13 . . . . . 0.04216 . 0.894680455 89.3017221 2438.67192 9.18228 EFCAB14 0.000132862974740103 0.959280685099068 0.0405864519261916 EF-hand calcium binding domain 14 . . . . . 0.34001 . -0.268115223 34.70747818 225.08115 3.24385 EFCAB14-AS1 . . . EFCAB14 antisense RNA 1 . . . . . . . . . . . EFCAB14P1 . . . EF-hand calcium binding domain 14 pseudogene 1 . . . . . . . . . . . EFCC1 0.000466919773276265 0.431262269570119 0.568270810656604 EF-hand and coiled-coil domain containing 1 . . . . . 0.17322 0.09470 . . 4007.19538 12.53500 EFEMP1 0.999786492859359 0.000213506894821474 2.45819659676097e-10 EGF containing fibulin-like extracellular matrix protein 1 FUNCTION: Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth. {ECO:0000269|PubMed:19804359, ECO:0000269|PubMed:19887559, ECO:0000269|PubMed:20005202}.; . TISSUE SPECIFICITY: In the eye, associated with photoreceptor outer and inner segment regions, the nerve fiber layer, outer nuclear layer and inner and outer plexiform layers of the retina. {ECO:0000269|PubMed:12242346, ECO:0000269|PubMed:20005202}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;gum;thyroid;iris;bladder;brain;gall bladder;heart;cartilage;tongue;nervous;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;atrium;larynx;bone;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;cornea;nasopharynx;placenta;head and neck;kidney;stomach;aorta; superior cervical ganglion;smooth muscle;adipose tissue;heart;placenta;atrioventricular node;trigeminal ganglion; 0.17515 0.23532 -0.756778259 13.44656759 46.1235 1.30886 EFEMP2 0.0283881635333074 0.960636654724935 0.010975181741758 EGF containing fibulin-like extracellular matrix protein 2 . DISEASE: Cutis laxa, autosomal recessive, 1B (ARCL1B) [MIM:614437]: A connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. The clinical spectrum of autosomal recessive cutis laxa is highly heterogeneous with respect to organ involvement and severity. ARCL1B features include emphysema, lethal pulmonary artery occlusion, aortic aneurysm, cardiopulmonary insufficiency, birth fractures, arachnodactyly, and fragility of blood vessels. {ECO:0000269|PubMed:16685658, ECO:0000269|PubMed:17937443, ECO:0000269|PubMed:19664000}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;endometrium;synovium;bone;iris;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; superior cervical ganglion;heart;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17343 0.12122 -0.600630256 18.06440198 39.99621 1.17614 EFHB 6.02556402227351e-17 0.0251484121065134 0.974851587893487 EF-hand domain family member B . . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;lung;nasopharynx;liver;testis;spleen;kidney;brain;bladder; . 0.07272 . 1.96037261 97.55248879 3938.96656 12.40558 EFHC1 5.05957542028851e-12 0.18887654969037 0.811123450304571 EF-hand domain (C-terminal) containing 1 FUNCTION: Necessary for radial and tangential cell migration during brain development, possibly acting as a regulator of cell morphology and process formation during migration (PubMed:22926142). May enhance calcium influx through CACNA1E and stimulate programmed cell death (PubMed:15258581). {ECO:0000269|PubMed:15258581, ECO:0000269|PubMed:22926142}.; DISEASE: Juvenile absence epilepsy 1 (JAE1) [MIM:607631]: A subtype of idiopathic generalized epilepsy characterized by onset occurring around puberty, absence seizures, generalized tonic- clonic seizures (GTCS), GTCS on awakening, and myoclonic seizures. {ECO:0000305|PubMed:17159113}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=Mutation Leu-229 may be a cause of intractable epilepsy of infancy. Affected individuals have seizures of multiple type, manifested as tonic, clonic, and myoclonic seizures in the neonatal period, and as tonic seizures activated frequently by sleep, and repeated frequent myoclonic seizures in later infancy. The seizures are unresponsive to numerous antiepileptic drugs, and infants die in the first years of life. Although heterozygosity for Leu-229 has been associated with relatively benign forms of epilepsy in adolescence, homozygosity for the same mutation has much more severe consequences. {ECO:0000269|PubMed:22690745}.; TISSUE SPECIFICITY: Widely expressed. Not detected in lymphocytes. {ECO:0000269|PubMed:15258581}.; . . 0.35867 0.15462 1.269496963 93.63057325 1124.37017 6.39756 EFHC2 0.941723124383347 0.0582304179374893 4.64576791640045e-05 EF-hand domain (C-terminal) containing 2 . . . unclassifiable (Anatomical System);lung;nasopharynx;pituitary gland; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10684 0.09536 0.598963042 82.7789573 385.16328 4.13550 EFHD1 0.77000556440612 0.222009755608688 0.00798467998519179 EF-hand domain family member D1 . . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;tongue;islets of Langerhans;hypothalamus;muscle;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;head and neck;kidney;mammary gland;stomach;aorta;cerebellum; whole brain;thalamus;medulla oblongata;occipital lobe;hypothalamus;spinal cord;pons;caudate nucleus;placenta;prefrontal cortex;globus pallidus;kidney;cingulate cortex;parietal lobe; 0.32874 0.12025 -0.139478553 43.29440906 1981.10324 8.20179 EFHD2 0.378995543892118 0.575502975857703 0.045501480250179 EF-hand domain family member D2 FUNCTION: May regulate B-cell receptor (BCR)-induced immature and primary B-cell apoptosis. Plays a role as negative regulator of the canonical NF-kappa-B-activating branch. Controls spontaneous apoptosis through the regulation of BCL2L1 abundance. {ECO:0000250}.; . TISSUE SPECIFICITY: Found in lymphocytes; preferentially expressed in CD8+ cells. {ECO:0000269|PubMed:11788997, ECO:0000269|PubMed:15274114}.; . . 0.25549 0.12378 -0.161524709 41.6430762 97.27988 2.13121 EFL1 . . . elongation factor like GTPase 1 FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes. Together with SBDS, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Has low intrinsic GTPase activity. GTPase activity is increased by contact with 60S ribosome subunits. {ECO:0000269|PubMed:21536732}.; . . . . 0.29718 0.11472 0.826715241 88.09271054 . . EFNA1 0.872063427950098 0.126248045799289 0.00168852625061355 ephrin-A1 FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. Plays an important role in angiogenesis and tumor neovascularization. The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. Exerts anti-oncogenic effects in tumor cells through activation and down-regulation of EPHA2. Activates EPHA2 by inducing tyrosine phosphorylation which leads to its internalization and degradation. Acts as a negative regulator in the tumorigenesis of gliomas by down-regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal growth cone and regulates dendritic spine morphogenesis. {ECO:0000269|PubMed:17332925, ECO:0000269|PubMed:18794797}.; . TISSUE SPECIFICITY: Brain. Down-regulated in primary glioma tissues compared to the normal tissues. The soluble monomeric form is expressed in the glioblastoma multiforme (GBM) and breast cancer cells (at protein level). {ECO:0000269|PubMed:17332925}.; . . 0.11427 0.20761 0.25917371 70.05779665 2215.21898 8.66769 EFNA2 0.376749730846869 0.577056500042446 0.0461937691106851 ephrin-A2 FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. With the EPHA2 receptor may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System); superior cervical ganglion;pons;trigeminal ganglion; 0.18047 0.23560 . . 4.72277 0.17120 EFNA3 0.18056410470307 0.765883296511033 0.0535525987858974 ephrin-A3 FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, skeletal muscle, spleen, thymus, prostate, testis, ovary, small intestine, and peripheral blood leukocytes.; . . 0.43564 0.13588 0.193034296 66.82000472 606.48242 4.98163 EFNA4 0.000252891317706202 0.533686273759329 0.466060834922965 ephrin-A4 FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. May play a role in the interaction between activated B-lymphocytes and dendritic cells in tonsils.; . TISSUE SPECIFICITY: Expressed in the adult spleen, lymph node, prostate, ovary, small intestine, and colon, and in fetal heart, lung, liver and kidney. Also detected in hematopoietic cell lines.; . . 0.21845 0.11756 -0.161524709 41.6430762 15.40065 0.55266 EFNA5 0.889436552296034 0.109405383000763 0.00115806470320301 ephrin-A5 FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion. {ECO:0000269|PubMed:10601038, ECO:0000269|PubMed:11870224}.; . . breast;pituitary gland; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.35594 0.35747 -0.163345027 41.24793583 19.98197 0.68062 EFNB1 0.781251723198181 0.211777215428357 0.00697106137346191 ephrin-B1 FUNCTION: Binds to the receptor tyrosine kinases EPHB1 and EPHA1. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons (By similarity). {ECO:0000250}.; DISEASE: Craniofrontonasal syndrome (CFNS) [MIM:304110]: X-linked inherited syndrome characterized by hypertelorism, coronal synostosis with brachycephaly, downslanting palpebral fissures, clefting of the nasal tip, joint anomalies, longitudinally grooved fingernails and other digital anomalies. {ECO:0000269|PubMed:15124102, ECO:0000269|PubMed:15166289, ECO:0000269|PubMed:15959873}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Heart, placenta, lung, liver, skeletal muscle, kidney, pancreas.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;synovium;testis;brain;bladder;unclassifiable (Anatomical System);amygdala;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;ciliary ganglion;trigeminal ganglion; 0.26774 0.37081 0.21689899 68.12927577 55.46506 1.49624 EFNB2 0.938926864720003 0.0608168086785361 0.000256326601460579 ephrin-B2 FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds to receptor tyrosine kinase including EPHA4, EPHA3 and EPHB4. Together with EPHB4 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells. May play a role in constraining the orientation of longitudinally projecting axons. {ECO:0000269|PubMed:12734395}.; . TISSUE SPECIFICITY: Lung and kidney.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;artery;unclassifiable (Anatomical System);cartilage;heart;muscle;lens;skeletal muscle;bile duct;breast;pancreas;lung;mesenchyma;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;amnion;spleen;kidney;mammary gland;stomach;aorta; globus pallidus;ciliary ganglion;trigeminal ganglion; 0.45742 0.19361 -0.516085732 21.20193442 13.29196 0.48262 EFNB3 0.456670731318802 0.537368110677708 0.00596115800349022 ephrin-B3 FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in brain; expressed in embryonic floor plate, roof plate and hindbrain segments.; unclassifiable (Anatomical System);amygdala;ovary;heart;salivary gland;intestine;pharynx;colon;parathyroid;blood;skin;uterus;lung;frontal lobe;cornea;visual apparatus;hippocampus;duodenum;liver;testis;head and neck;kidney;brain;mammary gland; whole brain;amygdala;occipital lobe;superior cervical ganglion;hypothalamus;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.38853 0.12462 0.104848986 61.49445624 86.61997 1.98814 EFR3A 0.00926619083230622 0.990713781356399 2.00278112945463e-05 EFR3 homolog A FUNCTION: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane (PubMed:23229899, PubMed:25608530, PubMed:26571211). The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis (Probable). In the complex, EFR3A probably acts as the membrane-anchoring component (PubMed:23229899). Also involved in responsiveness to G-protein-coupled receptors; it is however unclear whether this role is direct or indirect (PubMed:25380825). {ECO:0000269|PubMed:23229899, ECO:0000269|PubMed:25380825, ECO:0000269|PubMed:25608530, ECO:0000305}.; DISEASE: Note=Genetic variations in EFR3A may be associated with susceptibility to autism. {ECO:0000305|PubMed:24860643}.; . myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;urinary;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;developmental;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus;cerebellum; whole brain;amygdala;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;pons;subthalamic nucleus;thyroid;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.08097 0.08792 -0.306750577 32.23047889 480.62032 4.52224 EFR3B . . . EFR3 homolog B FUNCTION: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane (PubMed:23229899, PubMed:25608530, PubMed:26571211). The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis (Probable). In the complex, EFR3B probably acts as the membrane-anchoring component (PubMed:23229899). Also involved in responsiveness to G-protein-coupled receptors; it is however unclear whether this role is direct or indirect (PubMed:25380825). {ECO:0000269|PubMed:23229899, ECO:0000269|PubMed:25380825, ECO:0000269|PubMed:25608530, ECO:0000269|PubMed:26571211, ECO:0000305}.; . . lung;frontal lobe;testis;brain;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;kidney;pons;trigeminal ganglion; 0.13482 . -0.404032746 26.53338051 68.85195 1.71937 EFS 2.44587050452523e-06 0.494202307747298 0.505795246382198 embryonal Fyn-associated substrate FUNCTION: Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. May serve as an activator of SRC and a downstream effector. Interacts with the SH3 domain of FYN and with CRK, SRC, and YES (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: The protein has been detected in lung and placenta.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;thyroid;bone;testis;amniotic fluid;brain;unclassifiable (Anatomical System);heart;cartilage;lens;pancreas;lung;placenta;macula lutea;hippocampus;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;hypothalamus;placenta;spinal cord;caudate nucleus;trigeminal ganglion; 0.41116 0.14682 1.734373503 96.61476763 5246.98871 14.94057 EFTUD1P1 . . . elongation factor Tu GTP binding domain containing 1 pseudogene 1 . . . . . . . . . . . EFTUD1P2 . . . elongation factor Tu GTP binding domain containing 1 pseudogene 2 . . . . . . . . . . . EFTUD2 0.999991435314757 8.56468522354969e-06 1.96995682641502e-14 elongation factor Tu GTP binding domain containing 2 FUNCTION: Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex required for pre-mRNA splicing. Binds GTP.; DISEASE: Mandibulofacial dysostosis with microcephaly (MFDM) [MIM:610536]: A rare syndrome characterized by progressive microcephaly, midface and malar hypoplasia, micrognathia, microtia, dysplastic ears, preauricular skin tags, significant developmental delay, and speech delay. Many patients have major sequelae, including choanal atresia that results in respiratory difficulties, conductive hearing loss, and cleft palate. {ECO:0000269|PubMed:22305528}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;bone;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;muscle;pancreas;lung;placenta;duodenum;hypopharynx;head and neck;kidney;stomach; . 0.23692 0.33699 -1.153638777 6.233781552 20.07609 0.68608 EGF 7.013329027337e-12 0.999591882080802 0.000408117912184162 epidermal growth factor FUNCTION: EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6. Can induce neurite outgrowth in motoneurons of the pond snail Lymnaea stagnalis in vitro (PubMed:10964941). {ECO:0000269|PubMed:10964941, ECO:0000269|PubMed:17671655}.; DISEASE: Hypomagnesemia 4 (HOMG4) [MIM:611718]: A disorder characterized by massive renal hypomagnesemia and normal levels of serum calcium and calcium excretion. Clinical features include seizures, mild-to moderate psychomotor retardation, and brisk tendon reflexes. {ECO:0000269|PubMed:17671655}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in kidney, salivary gland, cerebrum and prostate. {ECO:0000269|PubMed:17671655}.; unclassifiable (Anatomical System);spinal cord;colon;skeletal muscle;retina;pancreas;lung;larynx;trabecular meshwork;placenta;pituitary gland;testis;head and neck;kidney;brain; superior cervical ganglion;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion; 0.39648 0.97288 1.298854499 93.91365888 1258.40063 6.68903 EGFEM1P . . . EGF like and EMI domain containing 1, pseudogene . . . . . . . . . . . EGFL6 2.66228154128096e-08 0.479907784943782 0.520092188433403 EGF like domain multiple 6 FUNCTION: May bind integrin alpha-8/beta-1 and play a role in hair follicle morphogenesis. Promotes matrix assembly (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;cochlea;larynx;placenta;macula lutea;visual apparatus;liver;testis;head and neck;spleen;kidney;brain;aorta; dorsal root ganglion;superior cervical ganglion;placenta;fetal lung;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.10208 0.09271 1.10969368 92.05590941 951.37974 5.96983 EGFL7 9.26440008429184e-13 0.00284449979109325 0.99715550020798 EGF like domain multiple 7 FUNCTION: Regulates vascular tubulogenesis in vivo. Inhibits platelet-derived growth factor (PDGF)-BB-induced smooth muscle cell migration and promotes endothelial cell adhesion to the extracellular matrix and angiogenesis. {ECO:0000269|PubMed:23386126, ECO:0000269|PubMed:23639441}.; . . ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.14150 0.13815 0.174625237 65.9648502 1242.79734 6.65703 EGFL8 3.51576835152093e-06 0.571678550659358 0.428317933572291 EGF like domain multiple 8 . . . ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;hypothalamus;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . . . 0.040529541 57.15380986 1136.2114 6.42964 EGFLAM 9.38438550961537e-10 0.994801331626989 0.0051986674345722 EGF like, fibronectin type III and laminin G domains FUNCTION: Involved in both the retinal photoreceptor ribbon synapse formation and physiological functions of visual perception. Necessary for proper bipolar dendritic tip apposition to the photoreceptor ribbon synapse. Promotes matrix assembly and cell adhesiveness (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;sympathetic chain;colon;parathyroid;choroid;skin;skeletal muscle;retina;uterus;pancreas;prostate;whole body;lung;adrenal gland;nasopharynx;bone;placenta;visual apparatus;liver;testis;spleen;brain; dorsal root ganglion;superior cervical ganglion;occipital lobe;olfactory bulb;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21901 0.73839 1.058154044 91.38947865 3829.87111 12.17606 EGFLAM-AS1 . . . EGFLAM antisense RNA 1 . . . . . . . . . . . EGFLAM-AS2 . . . EGFLAM antisense RNA 2 . . . . . . . . . . . EGFLAM-AS3 . . . EGFLAM antisense RNA 3 . . . . . . . . . . . EGFLAM-AS4 . . . EGFLAM antisense RNA 4 . . . . . . . . . . . EGFR 0.998664530178053 0.00133546982164989 2.97452025087101e-13 epidermal growth factor receptor FUNCTION: Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS- RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin.; DISEASE: Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis. {ECO:0000269|PubMed:15118125, ECO:0000269|PubMed:16533793, ECO:0000269|PubMed:16672372}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Inflammatory skin and bowel disease, neonatal, 2 (NISBD2) [MIM:616069]: A disorder characterized by inflammatory features with neonatal onset, involving the skin, hair, and gut. The skin lesions involve perioral and perianal erythema, psoriasiform erythroderma, with flares of erythema, scaling, and widespread pustules. Gastrointestinal symptoms include malabsorptive diarrhea that is exacerbated by intercurrent gastrointestinal infections. The hair is short or broken, and the eyelashes and eyebrows are wiry and disorganized. {ECO:0000269|PubMed:24691054}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers. {ECO:0000269|PubMed:17671655}.; ovary;sympathetic chain;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;lens;skeletal muscle;breast;bile duct;lung;placenta;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;placenta;liver;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.99968 0.98895 -2.160861741 1.439018636 119.9504 2.38669 EGFR-AS1 . . . EGFR antisense RNA 1 . . . . . . . . . . . EGI . . . epilepsy, generalized, idiopathic . . . . . . . . . . . EGLN1 0.925890293932093 0.074024297135037 8.54089328703851e-05 egl-9 family hypoxia-inducible factor 1 FUNCTION: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif. {ECO:0000269|PubMed:11595184, ECO:0000269|PubMed:12181324, ECO:0000269|PubMed:12351678, ECO:0000269|PubMed:15897452, ECO:0000269|PubMed:19339211, ECO:0000269|PubMed:21792862, ECO:0000269|PubMed:25129147}.; DISEASE: Erythrocytosis, familial, 3 (ECYT3) [MIM:609820]: An autosomal dominant disorder characterized by increased serum red blood cell mass, elevated serum hemoglobin and hematocrit, and normal serum erythropoietin levels. {ECO:0000269|PubMed:16407130, ECO:0000269|PubMed:17579185}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: According to PubMed:11056053, widely expressed with highest levels in skeletal muscle and heart, moderate levels in pancreas, brain (dopaminergic neurons of adult and fetal substantia nigra) and kidney, and lower levels in lung and liver. According to PubMed:12351678 widely expressed with highest levels in brain, kidney and adrenal gland. Expressed in cardiac myocytes, aortic endothelial cells and coronary artery smooth muscle. According to PubMed:12788921; expressed in adult and fetal heart, brain, liver, lung, skeletal muscle and kidney. Also expressed in placenta. Highest levels in adult heart, brain, lung and liver and fetal brain, heart spleen and skeletal muscle. {ECO:0000269|PubMed:11056053, ECO:0000269|PubMed:12163023, ECO:0000269|PubMed:12351678, ECO:0000269|PubMed:12670503, ECO:0000269|PubMed:12788921}.; . . 0.77234 0.09555 . . 1049.62982 6.22194 EGLN1P1 . . . egl-9 family hypoxia-inducible factor 1 pseudogene 1 . . . . . . . . . . . EGLN2 0.286988738826209 0.708404391722654 0.00460686945113711 egl-9 family hypoxia-inducible factor 2 FUNCTION: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle. Also regulates susceptibility to normoxic oxidative neuronal death. Links oxygen sensing to cell cycle and primary cilia formation by hydroxylating the critical centrosome component CEP192 which promotes its ubiquitination and subsequent proteasomal degradation. Hydroxylates IKBKB, mediating NF-kappaB activation in hypoxic conditions. Target proteins are preferentially recognized via a LXXLAP motif. {ECO:0000269|PubMed:11595184, ECO:0000269|PubMed:12181324, ECO:0000269|PubMed:16509823, ECO:0000269|PubMed:17114296, ECO:0000269|PubMed:19339211, ECO:0000269|PubMed:23932902}.; . TISSUE SPECIFICITY: Expressed in adult and fetal heart, brain, liver, lung, skeletal muscle, and kidney. Also expressed in testis and placenta. Highest levels in adult brain, placenta, lung, kidney, and testis. Expressed in hormone responsive tissues, including normal and cancerous mammary, ovarian and prostate epithelium. {ECO:0000269|PubMed:12163023}.; smooth muscle;ovary;skin;retina;prostate;optic nerve;endometrium;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus; testis - interstitial;testis - seminiferous tubule;testis; 0.42712 0.17320 -0.778825328 12.88039632 87.13981 1.99376 EGLN3 0.00264133555777407 0.790698520597503 0.206660143844723 egl-9 family hypoxia-inducible factor 3 FUNCTION: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Also hydroxylates PKM in hypoxia, limiting glycolysis. Under normoxia, hydroxylates and regulates the stability of ADRB2. Regulator of cardiomyocyte and neuronal apoptosis. In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex. In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity. Also essential for hypoxic regulation of neutrophilic inflammation. Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway. Target proteins are preferentially recognized via a LXXLAP motif. {ECO:0000269|PubMed:11595184, ECO:0000269|PubMed:12181324, ECO:0000269|PubMed:16098468, ECO:0000269|PubMed:19584355, ECO:0000269|PubMed:20849813, ECO:0000269|PubMed:20978507, ECO:0000269|PubMed:21317538, ECO:0000269|PubMed:21483450, ECO:0000269|PubMed:21575608, ECO:0000269|PubMed:21620138, ECO:0000269|PubMed:22797300}.; . TISSUE SPECIFICITY: Widely expressed at low levels. Expressed at higher levels in adult heart (cardiac myocytes, aortic endothelial cells and coronary artery smooth muscle), lung and placenta, and in fetal spleen, heart and skeletal muscle. Also expressed in pancreas. Localized to pancreatic acini and islet cells. {ECO:0000269|PubMed:12163023, ECO:0000269|PubMed:12670503, ECO:0000269|PubMed:21575608}.; unclassifiable (Anatomical System);heart;ovary;hypothalamus;colon;lens;skin;retina;uterus;prostate;lung;frontal lobe;endometrium;trabecular meshwork;placenta;visual apparatus;iris;liver;testis;cervix;spleen;kidney;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.80367 0.21485 -0.073340031 48.11866006 27.38988 0.88319 EGLN3-AS1 . . . EGLN3 antisense RNA 1 . . . . . . . . . . . EGLN3P1 . . . egl-9 family hypoxia-inducible factor 3 pseudogene 1 . . . . . . . . . . . EGOT . . . eosinophil granule ontogeny transcript (non-protein coding) . . . . . . . . . . . EGR1 0.674344947164404 0.320861373024958 0.00479367981063715 early growth response 1 FUNCTION: Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-CGCCCCCGC-3'(EGR-site). Activates the transcription of target genes whose products are required for mitogenesis and differentiation.; . . myocardium;ovary;sympathetic chain;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;oesophagus;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;urinary;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;epididymis;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.98853 0.88685 -0.846787714 11.05803255 55.14984 1.48872 EGR2 0.619543204134511 0.372661298434547 0.00779549743094242 early growth response 2 FUNCTION: Sequence-specific DNA-binding transcription factor. Binds to two specific DNA sites located in the promoter region of HOXA4. {ECO:0000269|PubMed:21836637}.; DISEASE: Neuropathy, congenital hypomyelinating or amyelinating (CHN) [MIM:605253]: A severe degenerating neuropathy that results from a congenital impairment in myelin formation. It is clinically characterized by early onset of hypotonia, areflexia, distal muscle weakness, and very slow nerve conduction velocities (as low as 3m/s). Some patients manifest nearly complete absence of spontaneous limb movements, respiratory distress at birth, and complete absence of myelin shown by electron microscopy of peripheral nerves. Inheritance can be autosomal dominant or recessive. {ECO:0000269|PubMed:22522483, ECO:0000269|PubMed:9537424}. Note=The disease is caused by mutations affecting the gene represented in this entry. Patients affected by the amyelinating form carry a causative, homozygous deletion encompassing a myelin-specific enhancer of EGR2 (PubMed:22522483). {ECO:0000269|PubMed:22522483}.; DISEASE: Charcot-Marie-Tooth disease 1D (CMT1D) [MIM:607678]: A dominant demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot- Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. {ECO:0000269|PubMed:10502832, ECO:0000269|PubMed:10762521, ECO:0000269|PubMed:11239949, ECO:0000269|PubMed:12736090, ECO:0000269|PubMed:15241803, ECO:0000269|PubMed:15947997, ECO:0000269|PubMed:9537424, ECO:0000269|Ref.15}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dejerine-Sottas syndrome (DSS) [MIM:145900]: A severe degenerating neuropathy of the demyelinating Charcot-Marie-Tooth disease category, with onset by age 2 years. Characterized by motor and sensory neuropathy with very slow nerve conduction velocities, increased cerebrospinal fluid protein concentrations, hypertrophic nerve changes, delayed age of walking as well as areflexia. There are both autosomal dominant and autosomal recessive forms of Dejerine-Sottas syndrome. {ECO:0000269|PubMed:10371530}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;colon;parathyroid;skin;retina;uterus;endometrium;larynx;thyroid;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;blood;breast;pancreas;lung;adrenal gland;placenta;spleen;head and neck;kidney;stomach; . 0.96995 0.66487 -0.227663163 37.11370606 35.98532 1.08083 EGR3 0.81109794446274 0.184199524764321 0.00470253077293932 early growth response 3 FUNCTION: Probable transcription factor involved in muscle spindle development.; . . unclassifiable (Anatomical System);cartilage;sympathetic chain;spinal cord;blood;skin;retina;lung;cochlea;thyroid;liver;mammary gland;brain;aorta; whole brain;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;temporal lobe;pons;caudate nucleus;trigeminal ganglion;parietal lobe; 0.95365 . -0.427900189 25.14744043 10.47491 0.38108 EGR4 0.0062667783643699 0.741293115488045 0.252440106147585 early growth response 4 FUNCTION: Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-GCGGGGGCG-3' (GSG). Activates the transcription of target genes whose products are required for mitogenesis and differentiation (By similarity). {ECO:0000250}.; . . . . 0.49816 0.15084 . . 55.61488 1.49875 EHBP1 0.999748961950681 0.000251038049293964 2.50319111524304e-14 EH domain binding protein 1 FUNCTION: May play a role in actin reorganization. Links clathrin- mediated endocytosis to the actin cytoskeleton. {ECO:0000269|PubMed:14676205}.; DISEASE: Prostate cancer, hereditary, 12 (HPC12) [MIM:611868]: A condition associated with familial predisposition to cancer of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma. {ECO:0000269|PubMed:18264098}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;bone;thyroid;iris;testis;dura mater;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;blood;pancreas;pia mater;lung;placenta;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;thalamus;testis - interstitial;occipital lobe;olfactory bulb;hypothalamus;skin;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.24287 0.11626 -0.080831688 47.22222222 564.36096 4.82304 EHBP1L1 8.081316771713e-07 0.999807515004489 0.000191676863833957 EH domain binding protein 1 like 1 . . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;lymph node;tongue;ciliary ganglion;pons;atrioventricular node;whole blood;trigeminal ganglion;skin;skeletal muscle;bone marrow; 0.16998 0.08888 0.077132183 59.19438547 4618.64715 13.65497 EHD1 0.894832021981373 0.104958010709684 0.000209967308942714 EH domain containing 1 FUNCTION: ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes (PubMed:15020713, PubMed:17233914, PubMed:20801876). Recruited to endosomal membranes upon nerve growth factor stimulation, indirectly regulates neurite outgrowth (By similarity). Plays a role in myoblast fusion (By similarity). Also plays a role in the formation of the ciliary vesicle, an early step in cilium biogenesis (PubMed:25686250). {ECO:0000250|UniProtKB:Q641Z6, ECO:0000250|UniProtKB:Q9WVK4, ECO:0000269|PubMed:15020713, ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:20801876, ECO:0000269|PubMed:25686250}.; . TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:10395801}.; lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;thyroid;iris;amniotic fluid;germinal center;brain;gall bladder;tonsil;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;mesenchyma;placenta;head and neck;kidney;stomach;thymus;cerebellum; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;placenta;testis;white blood cells;ciliary ganglion;whole blood;trigeminal ganglion;skeletal muscle;cerebellum; 0.19133 0.16306 -1.375949569 4.393724935 34.3386 1.05018 EHD2 0.531641412437229 0.464989567658867 0.00336901990390407 EH domain containing 2 FUNCTION: ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis (By similarity). Plays a role in membrane trafficking between the plasma membrane and endosomes (PubMed:17233914). Important for the internalization of GLUT4. Required for fusion of myoblasts to skeletal muscle myotubes. Required for normal translocation of FER1L5 to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q8BH64, ECO:0000269|PubMed:17233914}.; . TISSUE SPECIFICITY: Highly expressed in heart and moderately expressed in placenta, lung, and skeletal muscle. {ECO:0000269|PubMed:10673336}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;smooth muscle;adipose tissue;heart;fetal thyroid;skeletal muscle;uterus;lung;adrenal gland;placenta;appendix;fetal lung;trigeminal ganglion; 0.14909 0.13604 -1.041578376 7.773059684 254.81204 3.43303 EHD3 0.0885343960081059 0.902369320555585 0.0090962834363094 EH domain containing 3 FUNCTION: ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis (PubMed:25686250). Plays a role in endocytic transport (PubMed:16251358, PubMed:17233914). Also plays a role in the formation of the ciliary vesicle, an early step in cilium biogenesis (PubMed:25686250). {ECO:0000269|PubMed:16251358, ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:25686250}.; . TISSUE SPECIFICITY: Highly expressed in heart and brain and moderately expressed in kidney, liver, and placenta. {ECO:0000269|PubMed:10673336}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;oesophagus;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.15844 0.10909 -1.131590109 6.481481481 46.83363 1.32269 EHD4 0.00149680577068074 0.967256231872781 0.0312469623565387 EH domain containing 4 FUNCTION: ATP- and membrane-binding protein that probably controls membrane reorganization/tubulation upon ATP hydrolysis. Plays a role in early endosomal transport. {ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:18331452}.; . TISSUE SPECIFICITY: Highly expressed in pancreas and heart. {ECO:0000269|PubMed:10673336}.; lymphoreticular;smooth muscle;ovary;colon;choroid;skin;uterus;prostate;optic nerve;cerebral cortex;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons; 0.18697 0.12232 -0.754958418 13.57631517 609.04347 4.98933 EHD4-AS1 . . . EHD4 antisense RNA 1 . . . . . . . . . . . EHF 0.978731448718073 0.02126477231981 3.77896211663096e-06 ETS homologous factor FUNCTION: Transcriptional activator that may play a role in regulating epithelial cell differentiation and proliferation. May act as a repressor for a specific subset of ETS/AP-1-responsive genes and as a modulator of the nuclear response to mitogen- activated protein kinase signaling cascades. Binds to DNA sequences containing the consensus nucleotide core sequence GGAA. Involved in regulation of TNFRSF10B/DR5 expression through Ets- binding sequences on the TNFRSF10B/DR5 promoter. May contribute to development and carcinogenesis by acting as a tumor suppressor gene or anti-oncogene. {ECO:0000269|PubMed:10527851, ECO:0000269|PubMed:10644770, ECO:0000269|PubMed:11259407, ECO:0000269|PubMed:12444029, ECO:0000269|PubMed:17027647}.; . TISSUE SPECIFICITY: Expressed exclusively in tissues with a high content of epithelial cells. Highly expressed in salivary gland, mammary gland, prostate, and lung. Weakly expressed in kidney and colon. Not detected in heart, brain, placenta, liver, skeletal muscle, spleen, thymus, testis, ovary, small intestine or peripheral blood leukocytes. {ECO:0000269|PubMed:10527851, ECO:0000269|PubMed:10644770, ECO:0000269|PubMed:11259407, ECO:0000269|PubMed:12444029}.; meninges;lacrimal gland;islets of Langerhans;colon;skin;skeletal muscle;breast;pancreas;prostate;pia mater;lung;endometrium;thyroid;liver;head and neck;dura mater;kidney;bladder;stomach; superior cervical ganglion;trachea; 0.49064 0.12294 -0.293801652 32.93819297 311.21572 3.75503 EHHADH 8.50410911635847e-11 0.142513409403244 0.857486590511715 enoyl-CoA, hydratase/3-hydroxyacyl CoA dehydrogenase . DISEASE: Fanconi renotubular syndrome 3 (FRTS3) [MIM:615605]: A disease due to a generalized dysfunction of the proximal kidney tubule resulting in decreased solute and water reabsorption. Patients have polydipsia and polyuria with phosphaturia, glycosuria and aminoaciduria. They may develop hypophosphatemic rickets or osteomalacia, acidosis and a tendency toward dehydration. Some eventually develop renal insufficiency. {ECO:0000269|PubMed:24401050}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver and kidney. Strongly expressed in the terminal segments of the proximal tubule. Lower amounts seen in the brain. {ECO:0000269|PubMed:24401050, ECO:0000269|PubMed:8188243}.; unclassifiable (Anatomical System);lymph node;ovary;heart;colon;parathyroid;lens;skin;skeletal muscle;uterus;prostate;lung;frontal lobe;endometrium;larynx;thyroid;placenta;liver;testis;cervix;head and neck;spleen;kidney;mammary gland;stomach; superior cervical ganglion; 0.06270 0.40821 2.27279014 98.24251003 2942.72265 10.28873 EHHADH-AS1 . . . EHHADH antisense RNA 1 . . . . . . . . . . . EHMT1 0.99999990401202 9.59879795724989e-08 3.4944631440694e-19 euchromatic histone-lysine N-methyltransferase 1 FUNCTION: Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non- histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. {ECO:0000269|PubMed:12004135, ECO:0000269|PubMed:20118233}.; DISEASE: Kleefstra syndrome (KLESTS) [MIM:610253]: A syndrome characterized by severe mental retardation, hypotonia, brachy(micro)cephaly, and facial dysmorphisms. Additionally, congenital heart defects, urogenital defects, epilepsy and behavioral problems are frequently observed. {ECO:0000269|PubMed:16826528, ECO:0000269|PubMed:19264732}. Note=The disease is caused by mutations affecting the gene represented in this entry (PubMed:16826528). The syndrome can be either caused by intragenic EHMT1 mutations leading to haploinsufficiency of the EHMT1 gene or by a submicroscopic 9q34.3 deletion. Although it is not known if and to what extent other genes in the 9q34.3 region contribute to the syndrome observed in deletion cases, EHMT1 seems to be the major determinant of the core disease phenotype (PubMed:19264732). {ECO:0000269|PubMed:16826528, ECO:0000269|PubMed:19264732}.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11347906}.; unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;salivary gland;colon;parathyroid;blood;skin;bone marrow;uterus;prostate;lung;frontal lobe;epididymis;placenta;liver;testis;spleen;germinal center;kidney;brain;mammary gland; subthalamic nucleus;globus pallidus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.19698 0.14590 -1.582005788 3.13163482 397.32742 4.18760 EHMT1-IT1 . . . EHMT1 intronic transcript 1 . . . . . . . . . . . EHMT2 0.0644714712842996 0.935528484706048 4.40096523141543e-08 euchromatic histone-lysine N-methyltransferase 2 FUNCTION: Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys- 373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself. {ECO:0000269|PubMed:11316813, ECO:0000269|PubMed:18438403, ECO:0000269|PubMed:20084102, ECO:0000269|PubMed:20118233, ECO:0000269|PubMed:22387026, ECO:0000269|PubMed:8457211}.; . TISSUE SPECIFICITY: Expressed in all tissues examined, with high levels in fetal liver, thymus, lymph node, spleen and peripheral blood leukocytes and lower level in bone marrow. {ECO:0000269|PubMed:11707778}.; . . 0.29937 0.12008 -0.883608246 10.50365652 954.38937 5.98037 EHMT2-AS1 . . . EHMT2 antisense RNA 1 . . . . . . . . . . . EI24 0.965168318705079 0.0348188663546146 1.28149403065889e-05 EI24, autophagy associated transmembrane protein FUNCTION: Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy (By similarity). {ECO:0000250}.; DISEASE: Note=EI24 is on a chromosomal region frequently deleted in solid tumors, and it is thought to play a role in breast and cervical cancer. Particularly, expression analysis of EI24 in cancerous tissues shows that EI24 loss is associated with tumor invasiveness.; . smooth muscle;ovary;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;gum;bone;thyroid;iris;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;epidermis;islets of Langerhans;muscle;urinary;blood;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;aorta;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion; 0.74136 0.10490 . . 26.27733 0.85200 EI24P1 . . . EI24, autophagy associated transmembrane protein pseudogene 1 . . . . . . . . . . . EI24P2 . . . EI24, autophagy associated transmembrane protein pseudogene 2 . . . . . . . . . . . EI24P3 . . . EI24, autophagy associated transmembrane protein pseudogene 3 . . . . . . . . . . . EI24P4 . . . EI24, autophagy associated transmembrane protein pseudogene 4 . . . . . . . . . . . EI24P5 . . . EI24, autophagy associated transmembrane protein pseudogene 5 . . . . . . . . . . . EID1 0.64535520974644 0.328018253378392 0.0266265368751677 EP300 interacting inhibitor of differentiation 1 FUNCTION: Interacts with RB1 and EP300 and acts as a repressor of MYOD1 transactivation. Inhibits EP300 and CBP histone acetyltransferase activity. May be involved in coupling cell cycle exit to the transcriptional activation of genes required for cellular differentiation. May act as a candidate coinhibitory factor for NR0B2 that can be directly linked to transcription inhibitory mechanisms. {ECO:0000269|PubMed:11073989, ECO:0000269|PubMed:11073990}.; . TISSUE SPECIFICITY: Widely expressed. Most abundantly expressed in heart, skeletal muscle, pancreas, brain and testis. Expressed at much lower levels in placenta and peripheral blood leukocyte. Barely detectable in lung. Also weakly expressed in lung carcinoma A-549 and various leukemia cell lines. {ECO:0000269|PubMed:11073990, ECO:0000269|PubMed:11223246}.; . . 0.07008 . -0.075159878 47.78839349 10.19536 0.37139 EID2 0.750053234702107 0.239929604635796 0.0100171606620979 EP300 interacting inhibitor of differentiation 2 FUNCTION: Interacts with EP300 and acts as a repressor of MYOD- dependent transcription and muscle differentiation. Inhibits EP300 histone acetyltransferase activity. Acts as a repressor of TGFB/SMAD transcriptional responses. May act as a repressor of the TGFB/SMAD3-dependent signaling by selectively blocking formation of TGFB-induced SMAD3-SMAD4 complex. {ECO:0000269|PubMed:12586827, ECO:0000269|PubMed:14585496, ECO:0000269|PubMed:14612439}.; . TISSUE SPECIFICITY: Most abundantly expressed in placenta. Highly expressed in liver, brain, heart, skeletal muscle, and kidney. {ECO:0000269|PubMed:14585496}.; . . 0.15271 0.09734 0.457594962 78.16112291 1987.72319 8.21502 EID2B 0.126192494543355 0.614699695333925 0.259107810122719 EP300 interacting inhibitor of differentiation 2B FUNCTION: Acts as a repressor of MYOD-dependent transcription, glucocorticoid receptor-dependent transcription, and muscle differentiation. {ECO:0000269|PubMed:15970276}.; . . unclassifiable (Anatomical System);lung;bone;brain; cerebellum peduncles; 0.06505 0.08604 0.191216164 66.57230479 15.13461 0.54460 EID3 0.237610982131272 0.730240176872432 0.0321488409962961 EP300 interacting inhibitor of differentiation 3 FUNCTION: Tissue-specific component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination and mediates sumoylation of shelterin complex (telosome) components. {ECO:0000269|PubMed:15987788}.; . TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:15987788}.; . . . . 0.260991686 70.25831564 91.29644 2.05499 EIF1 0.764131765089407 0.22731709125612 0.00855114365447321 eukaryotic translation initiation factor 1 FUNCTION: Necessary for scanning and involved in initiation site selection. Promotes the assembly of 48S ribosomal complexes at the authentic initiation codon of a conventional capped mRNA.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;iris;bladder;brain;heart;cartilage;urinary;spinal cord;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;peripheral nerve;salivary gland;intestine;colon;choroid;uterus;cerebral cortex;bone;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; . 0.76332 . 0.12325821 62.38499646 294.36299 3.66425 EIF1AD 0.181571133840477 0.765386169485757 0.053042696673766 eukaryotic translation initiation factor 1A domain containing FUNCTION: Plays a role into cellular response to oxidative stress. Decreases cell proliferation. {ECO:0000269|PubMed:20644585, ECO:0000269|PubMed:22095125}.; . TISSUE SPECIFICITY: Expressed in the glioblastoma cell line U- 87MG, the embryonic kidney cell line HEK293, the pancreatic carcinoma cell line PANC-1, the breast carcinoma cell line MCF-7, the lung cancer cell line NCI-H460, and the chronic myelogenous leukemia cell line K-562. {ECO:0000269|PubMed:20644585}.; unclassifiable (Anatomical System);cartilage;ovary;heart;islets of Langerhans;colon;blood;skin;bone marrow;uterus;prostate;lung;bone;thyroid;placenta;liver;testis;spleen;germinal center;kidney;brain;stomach; . 0.16708 0.11594 0.525552348 80.57914603 448.36483 4.40372 EIF1AX 0.881572170128827 0.117045289278308 0.00138254059286494 eukaryotic translation initiation factor 1A, X-linked FUNCTION: Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.; . . . . . 0.13638 0.057118534 57.99716914 . . EIF1AX-AS1 . . . EIF1AX antisense RNA 1 . . . . . . . . . . . EIF1AXP1 . . . eukaryotic translation initiation factor 1A, X-linked pseudogene 1 . . . . . . . . . . . EIF1AXP2 . . . eukaryotic translation initiation factor 1A, X-linked pseudogene 2 . . . . . . . . . . . EIF1AY 0.424064592561161 0.463173783034068 0.112761624404771 eukaryotic translation initiation factor 1A, Y-linked FUNCTION: Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;cochlea;bone;thyroid;testis;germinal center;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;hippocampus;liver;alveolus;kidney;stomach; . 0.26510 . . . . . EIF1B 0.394740519246042 0.564340605871749 0.0409188748822093 eukaryotic translation initiation factor 1B FUNCTION: Probably involved in translation.; . . myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;atrium;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;kidney;stomach;aorta;thymus;cerebellum; whole brain;amygdala;fetal brain;cerebellum; 0.36503 0.11809 0.057118534 57.99716914 1.20885 0.03791 EIF1B-AS1 . . . EIF1B antisense RNA 1 . . . . . . . . . . . EIF1P1 . . . eukaryotic translation initiation factor 1 pseudogene 1 . . . . . . . . . . . EIF1P2 . . . eukaryotic translation initiation factor 1 pseudogene 2 . . . . . . . . . . . EIF1P3 . . . eukaryotic translation initiation factor 1 pseudogene 3 . . . . . . . . . . . EIF1P4 . . . eukaryotic translation initiation factor 1 pseudogene 4 . . . . . . . . . . . EIF1P5 . . . eukaryotic translation initiation factor 1 pseudogene 5 . . . . . . . . . . . EIF1P6 . . . eukaryotic translation initiation factor 1 pseudogene 6 . . . . . . . . . . . EIF1P7 . . . eukaryotic translation initiation factor 1 pseudogene 7 . . . . . . . . . . . EIF2A 0.00015893869213679 0.967780657243117 0.0320604040647459 eukaryotic translation initiation factor 2A FUNCTION: Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF- 2 complex, it binds methionyl-tRNAi to 40 S subunits in a codon- dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40 S subunits in a GTP-dependent manner. May act by impiging the expression of specific proteins. {ECO:0000269|PubMed:12133843}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in pancreas, heart, brain and placenta. {ECO:0000269|PubMed:12133843}.; myocardium;medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;bladder;heart;cartilage;tongue;pineal body;spinal cord;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum;thymus; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.76857 0.11166 -0.203796826 38.81811748 3443.82688 11.27269 EIF2AK1 0.000121058308025956 0.99778858755231 0.00209035413966366 eukaryotic translation initiation factor 2 alpha kinase 1 FUNCTION: Inhibits protein synthesis at the translation initiation level, in response to various stress conditions, including oxidative stress, heme deficiency, osmotic shock and heat shock. Exerts its function through the phosphorylation of EIF2S1 at 'Ser- 48' and 'Ser-51', thus preventing its recycling. Binds hemin forming a 1:1 complex through a cysteine thiolate and histidine nitrogenous coordination. This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell. Thanks to this unique heme-sensing capacity, plays a crucial role to shut off protein synthesis during acute heme-deficient conditions. In red blood cells (RBCs), controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of its heme and globin moieties. Thus plays an essential protective role for RBC survival in anemias of iron deficiency. Similarly, in hepatocytes, involved in heme-mediated translational control of CYP2B and CYP3A and possibly other hepatic P450 cytochromes. May also contain ER stress during acute heme-deficient conditions (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed predominantly in erythroid cells. At much lower levels, expressed in hepatocytes (at protein level). {ECO:0000269|PubMed:20071449}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach; superior cervical ganglion;occipital lobe;subthalamic nucleus;fetal liver;cerebellum;bone marrow; 0.13551 0.29413 0.356452144 74.62845011 1369.09001 6.94068 EIF2AK2 0.0515534226933567 0.94826172448566 0.000184852820983555 eukaryotic translation initiation factor 2 alpha kinase 2 FUNCTION: IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1). Inhibits viral replication via phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (EIF2S1), this phosphorylation impairs the recycling of EIF2S1 between successive rounds of initiation leading to inhibition of translation which eventually results in shutdown of cellular and viral protein synthesis. Also phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11. In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteosomal degradation. Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding proinflammatory cytokines and IFNs. Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6. Can act as both a positive and negative regulator of the insulin signaling pathway (ISP). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser- 312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes. Can trigger apoptosis via FADD-mediated activation of CASP8. Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin. {ECO:0000269|PubMed:10848580, ECO:0000269|PubMed:11836380, ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15229216, ECO:0000269|PubMed:18835251, ECO:0000269|PubMed:19189853, ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:19507191, ECO:0000269|PubMed:19840259, ECO:0000269|PubMed:20171114, ECO:0000269|PubMed:20395957, ECO:0000269|PubMed:20685959, ECO:0000269|PubMed:21072047, ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:21710204, ECO:0000269|PubMed:22214662, ECO:0000269|PubMed:22381929, ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:22948139, ECO:0000269|PubMed:23084476, ECO:0000269|PubMed:23115276, ECO:0000269|PubMed:23229543, ECO:0000269|PubMed:23372823, ECO:0000269|PubMed:23399035}.; . TISSUE SPECIFICITY: Highly expressed in thymus, spleen and bone marrow compared to non-hematopoietic tissues such as small intestine, liver, or kidney tissues. Colocalizes with GSK3B and TAU in the Alzheimer disease (AD) brain. Elevated levels seen in breast and colon carcinomas,and which correlates with tumor progression and invasiveness or risk of progression. {ECO:0000269|PubMed:21029237, ECO:0000269|PubMed:23403623}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;islets of Langerhans;colon;blood;skin;uterus;prostate;lung;frontal lobe;endometrium;bone;placenta;liver;testis;amniotic fluid;cervix;head and neck;kidney;brain;mammary gland;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;prefrontal cortex;atrioventricular node;pons;trigeminal ganglion; 0.46059 0.29413 -0.670411825 15.61689078 8.14754 0.30014 EIF2AK3 0.0114235489498432 0.988573466214862 2.98483529481389e-06 eukaryotic translation initiation factor 2 alpha kinase 3 FUNCTION: Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) on 'Ser-52' during the unfolded protein response (UPR) and in response to low amino acid availability. Converts phosphorylated eIF-2-alpha/EIF2S1 either in a global protein synthesis inhibitor, leading to a reduced overall utilization of amino acids, or to a translation initiation activator of specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion. Serves as a critical effector of unfolded protein response (UPR)- induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function. {ECO:0000250|UniProtKB:Q9Z2B5}.; DISEASE: Wolcott-Rallison syndrome (WRS) [MIM:226980]: A rare autosomal recessive disorder, characterized by permanent neonatal or early infancy insulin-dependent diabetes and, at a later age, epiphyseal dysplasia, osteoporosis, growth retardation and other multisystem manifestations, such as hepatic and renal dysfunctions, mental retardation and cardiovascular abnormalities. {ECO:0000269|PubMed:10932183}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. A high level expression is seen in secretory tissues.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; amygdala;thyroid; 0.26099 0.58678 0.090079492 60.64519934 2881.36573 10.17167 EIF2AK4 8.32742943473465e-10 0.999999912359779 8.68074780055899e-08 eukaryotic translation initiation factor 2 alpha kinase 4 FUNCTION: Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) on 'Ser-52' in response to low amino acid availability (PubMed:25329545). Plays a role as an activator of the integrated stress response (ISR) required for adapatation to amino acid starvation. Converts phosphorylated eIF- 2-alpha/EIF2S1 either to a competitive inhibitor of the translation initiation factor eIF-2B, leading to a global protein synthesis repression, and thus to a reduced overall utilization of amino acids, or to a translational initiation activation of specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion. Binds uncharged tRNAs (By similarity). Involved in cell cycle arrest by promoting cyclin D1 mRNA translation repression after the unfolded protein response pathway (UPR) activation or cell cycle inhibitor CDKN1A/p21 mRNA translation activation in response to amino acid deprivation (PubMed:26102367). Plays a role in the consolidation of synaptic plasticity, learning as well as formation of long-term memory. Plays a role in neurite outgrowth inhibition. Plays a proapoptotic role in response to glucose deprivation. Promotes global cellular protein synthesis repression in response to UV irradiation independently of the stress- activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) and p38 MAPK signaling pathways (By similarity). {ECO:0000250|UniProtKB:P15442, ECO:0000250|UniProtKB:Q9QZ05, ECO:0000269|PubMed:25329545, ECO:0000269|PubMed:26102367}.; DISEASE: Pulmonary venoocclusive disease 2, autosomal recessive (PVOD2) [MIM:234810]: A disease characterized by widespread fibrous obstruction and intimal thickening of septal veins and preseptal venules, a low diffusing capacity for carbon monoxide, occult alveolar hemorrhage, and nodular ground-glass opacities, septal lines and lymph node enlargement showed by high-resolution computed tomography of the chest. It is frequently associated with pulmonary capillary dilatation and proliferation, and is a rare and devastating cause of pulmonary hypertension. {ECO:0000269|PubMed:24135949, ECO:0000269|PubMed:24292273}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed (PubMed:10504407). Expressed in lung, smooth muscle cells and macrophages (PubMed:24292273). {ECO:0000269|PubMed:10504407, ECO:0000269|PubMed:24292273}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve; . 0.17808 . -0.722015017 14.27223402 2847.71785 10.09156 EIF2AP1 . . . eukaryotic translation initiation factor 2A pseudogene 1 . . . . . . . . . . . EIF2AP2 . . . eukaryotic translation initiation factor 2A pseudogene 2 . . . . . . . . . . . EIF2AP3 . . . eukaryotic translation initiation factor 2A pseudogene 3 . . . . . . . . . . . EIF2AP4 . . . eukaryotic translation initiation factor 2A pseudogene 4 . . . . . . . . . . . EIF2B1 0.104796388339037 0.888330945781824 0.00687266587913879 eukaryotic translation initiation factor 2B subunit alpha FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.; DISEASE: Leukodystrophy with vanishing white matter (VWM) [MIM:603896]: A leukodystrophy that occurs mainly in children. Neurological signs include progressive cerebellar ataxia, spasticity, inconstant optic atrophy and relatively preserved mental abilities. The disease is chronic-progressive with, in most individuals, additional episodes of rapid deterioration following febrile infections or minor head trauma. While childhood onset is the most common form of the disorder, some severe forms are apparent at birth. A severe, early-onset form seen among the Cree and Chippewayan populations of Quebec and Manitoba is called Cree leukoencephalopathy. Milder forms may not become evident until adolescence or adulthood. Some females with milder forms of the disease who survive to adolescence exhibit ovarian dysfunction. This variant of the disorder is called ovarioleukodystrophy. {ECO:0000269|PubMed:11835386, ECO:0000269|PubMed:15776425}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;skin;retina;bone marrow;uterus;prostate;larynx;synovium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;bile duct;breast;lung;placenta;liver;spleen;head and neck;mammary gland;stomach; medulla oblongata;testis;parietal lobe; 0.43453 0.12528 -0.383807564 27.41802312 25.93892 0.84283 EIF2B2 0.000428255871835589 0.858614234583202 0.140957509544963 eukaryotic translation initiation factor 2B subunit beta FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.; DISEASE: Leukodystrophy with vanishing white matter (VWM) [MIM:603896]: A leukodystrophy that occurs mainly in children. Neurological signs include progressive cerebellar ataxia, spasticity, inconstant optic atrophy and relatively preserved mental abilities. The disease is chronic-progressive with, in most individuals, additional episodes of rapid deterioration following febrile infections or minor head trauma. While childhood onset is the most common form of the disorder, some severe forms are apparent at birth. A severe, early-onset form seen among the Cree and Chippewayan populations of Quebec and Manitoba is called Cree leukoencephalopathy. Milder forms may not become evident until adolescence or adulthood. Some females with milder forms of the disease who survive to adolescence exhibit ovarian dysfunction. This variant of the disorder is called ovarioleukodystrophy. {ECO:0000269|PubMed:11704758, ECO:0000269|PubMed:12707859, ECO:0000269|PubMed:15776425, ECO:0000269|PubMed:21484434, ECO:0000269|PubMed:22285377, ECO:0000269|PubMed:22729508}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;liver;head and neck;spleen;cervix;kidney;aorta;stomach; superior cervical ganglion;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.22259 0.17757 -0.271755481 34.31823543 46.00949 1.30646 EIF2B3 0.393440242907713 0.606154371864943 0.000405385227343499 eukaryotic translation initiation factor 2B subunit gamma FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.; DISEASE: Leukodystrophy with vanishing white matter (VWM) [MIM:603896]: A leukodystrophy that occurs mainly in children. Neurological signs include progressive cerebellar ataxia, spasticity, inconstant optic atrophy and relatively preserved mental abilities. The disease is chronic-progressive with, in most individuals, additional episodes of rapid deterioration following febrile infections or minor head trauma. While childhood onset is the most common form of the disorder, some severe forms are apparent at birth. A severe, early-onset form seen among the Cree and Chippewayan populations of Quebec and Manitoba is called Cree leukoencephalopathy. Milder forms may not become evident until adolescence or adulthood. Some females with milder forms of the disease who survive to adolescence exhibit ovarian dysfunction. This variant of the disorder is called ovarioleukodystrophy. {ECO:0000269|PubMed:11835386, ECO:0000269|PubMed:19158808, ECO:0000269|PubMed:21484434}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;sympathetic chain;intestine;colon;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;nervous;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;cerebellum;thymus; testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.52579 0.16783 -0.115612493 45.12856806 47.17108 1.32992 EIF2B4 0.832609528731968 0.167384458026396 6.01324163540441e-06 eukaryotic translation initiation factor 2B subunit delta FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.; DISEASE: Leukodystrophy with vanishing white matter (VWM) [MIM:603896]: A leukodystrophy that occurs mainly in children. Neurological signs include progressive cerebellar ataxia, spasticity, inconstant optic atrophy and relatively preserved mental abilities. The disease is chronic-progressive with, in most individuals, additional episodes of rapid deterioration following febrile infections or minor head trauma. While childhood onset is the most common form of the disorder, some severe forms are apparent at birth. A severe, early-onset form seen among the Cree and Chippewayan populations of Quebec and Manitoba is called Cree leukoencephalopathy. Milder forms may not become evident until adolescence or adulthood. Some females with milder forms of the disease who survive to adolescence exhibit ovarian dysfunction. This variant of the disorder is called ovarioleukodystrophy. {ECO:0000269|PubMed:11835386, ECO:0000269|PubMed:12707859, ECO:0000269|PubMed:15776425}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;endometrium;gum;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;cerebellum; testis - interstitial;testis;skeletal muscle; 0.71502 0.13179 -0.756778259 13.44656759 58.26509 1.54540 EIF2B5 0.996711860525997 0.00328813787646591 1.59753655465205e-09 eukaryotic translation initiation factor 2B subunit epsilon FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.; DISEASE: Leukodystrophy with vanishing white matter (VWM) [MIM:603896]: A leukodystrophy that occurs mainly in children. Neurological signs include progressive cerebellar ataxia, spasticity, inconstant optic atrophy and relatively preserved mental abilities. The disease is chronic-progressive with, in most individuals, additional episodes of rapid deterioration following febrile infections or minor head trauma. While childhood onset is the most common form of the disorder, some severe forms are apparent at birth. A severe, early-onset form seen among the Cree and Chippewayan populations of Quebec and Manitoba is called Cree leukoencephalopathy. Milder forms may not become evident until adolescence or adulthood. Some females with milder forms of the disease who survive to adolescence exhibit ovarian dysfunction. This variant of the disorder is called ovarioleukodystrophy. {ECO:0000269|PubMed:11704758, ECO:0000269|PubMed:12325082, ECO:0000269|PubMed:12707859, ECO:0000269|PubMed:15776425, ECO:0000269|PubMed:19158808, ECO:0000269|PubMed:21484434}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;parietal lobe;skeletal muscle; 0.51279 0.15904 -0.887242605 10.43288511 3888.77026 12.30249 EIF2B5-AS1 . . . EIF2B5 antisense RNA 1 . . . . . . . . . . . EIF2B5-IT1 . . . EIF2B5 intronic transcript 1 . . . . . . . . . . . EIF2D 6.59630829154375e-06 0.994455937269421 0.00553746642228758 eukaryotic translation initiation factor 2D FUNCTION: Translation initiation factor that is able to deliver tRNA to the P-site of the eukaryotic ribosome in a GTP-independent manner. The binding of Met-tRNA(I) occurs after the AUG codon finds its position in the P-site of 40S ribosomes, the situation that takes place during initiation complex formation on some specific RNAs. Its activity in tRNA binding with 40S subunits does not require the presence of the aminoacyl moiety. Possesses the unique ability to deliver non-Met (elongator) tRNAs into the P- site of the 40S subunit. In addition to its role in initiation, can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. {ECO:0000269|PubMed:20566627, ECO:0000269|PubMed:20713520}.; . . lymphoreticular;umbilical cord;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;gum;bone;iris;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;bile duct;pancreas;lung;mesenchyma;placenta;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; superior cervical ganglion;skeletal muscle; 0.24884 0.13449 -0.402212257 26.7338995 277.94888 3.57230 EIF2S1 0.916802002902544 0.083083238644944 0.000114758452511775 eukaryotic translation initiation factor 2 subunit alpha FUNCTION: Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach; dorsal root ganglion;testis - interstitial;occipital lobe;superior cervical ganglion;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.88990 0.49283 -0.207437529 38.2814343 8.52186 0.31301 EIF2S2 0.863603165264989 0.136312324734672 8.45100003388537e-05 eukaryotic translation initiation factor 2 subunit beta FUNCTION: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.; . . . . 0.91716 0.18980 0.103030231 61.2762444 54.089 1.46657 EIF2S2P1 . . . eukaryotic translation initiation factor 2 subunit 2 beta pseudogene 1 . . . . . . . . . . . EIF2S2P2 . . . eukaryotic translation initiation factor 2 subunit 2 beta pseudogene 2 . . . . . . . . . . . EIF2S2P3 . . . eukaryotic translation initiation factor 2 subunit 2 beta pseudogene 3 . . . . . . . . . . . EIF2S2P4 . . . eukaryotic translation initiation factor 2 subunit 2 beta pseudogene 4 . . . . . . . . . . . EIF2S2P5 . . . eukaryotic translation initiation factor 2 subunit 2 beta pseudogene 5 . . . . . . . . . . . EIF2S2P6 . . . eukaryotic translation initiation factor 2 subunit 2 beta pseudogene 6 . . . . . . . . . . . EIF2S2P7 . . . eukaryotic translation initiation factor 2 subunit 2 beta pseudogene 7 . . . . . . . . . . . EIF2S3 0.916323958431386 0.0835595866727955 0.000116454895818104 eukaryotic translation initiation factor 2 subunit gamma FUNCTION: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.; . . ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;amygdala;heart;cartilage;tongue;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;hypothalamus;pancreas;lung;cornea;mesenchyma;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; . 0.86209 0.21829 0.125076652 62.7388535 525.56681 4.67785 EIF3A 0.999999999560078 4.3992222697918e-10 5.81618253731632e-27 eukaryotic translation initiation factor 3 subunit A FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre- initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Essential for the initiation of translation on type-1 viral ribosomal entry sites (IRESs), like for HCV, PV, EV71 or BEV translation (PubMed:23766293, PubMed:24357634). In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000255|HAMAP-Rule:MF_03000, ECO:0000269|PubMed:11169732, ECO:0000269|PubMed:18056426, ECO:0000269|PubMed:23766293, ECO:0000269|PubMed:24357634}.; . . . . 0.95541 . -0.879979233 10.5626327 389.53412 4.15742 EIF3B 0.999970669114633 2.93308834149615e-05 1.95256691286675e-12 eukaryotic translation initiation factor 3 subunit B FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre- initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426, ECO:0000269|PubMed:9388245}.; . . myocardium;lymphoreticular;ovary;skin;retina;prostate;frontal lobe;endometrium;gum;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;nervous;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;vein;uterus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;testis - seminiferous tubule;testis;skeletal muscle; 0.97682 0.13736 -0.622676946 17.30950696 275.48249 3.55465 EIF3C 0.34330310885051 0.598904816921278 0.0577920742282124 eukaryotic translation initiation factor 3 subunit C FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.; . . lymphoreticular;ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;trophoblast;heart;islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;pancreas;lung;mesenchyma;epididymis;placenta;visual apparatus;duodenum;cervix;kidney;mammary gland;stomach;peripheral nerve; . 0.93105 0.16254 . . 8.28548 0.30395 EIF3CL . . . eukaryotic translation initiation factor 3 subunit C-like FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (By similarity). {ECO:0000250}.; . . . . 0.25453 0.11770 . . 550.20273 4.77077 EIF3D 0.994221961457999 0.00577800726115687 3.12808440327664e-08 eukaryotic translation initiation factor 3 subunit D FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre- initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}.; . . lymphoreticular;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;gum;bone;thyroid;testis;germinal center;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;aorta;stomach; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;tumor;testis;white blood cells; 0.42006 0.12971 -0.560178693 19.30879925 9.92337 0.36342 EIF3E 0.734231961664271 0.265658372110639 0.000109666225090206 eukaryotic translation initiation factor 3 subunit E FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Required for nonsense- mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway. May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins. {ECO:0000255|HAMAP-Rule:MF_03004, ECO:0000269|PubMed:17310990, ECO:0000269|PubMed:17324924, ECO:0000269|PubMed:17468741}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at highest levels in appendix, lymph, pancreas, skeletal muscle, spleen and thymus. {ECO:0000269|PubMed:8688078, ECO:0000269|PubMed:9295280}.; smooth muscle;ovary;salivary gland;intestine;colon;substantia nigra;parathyroid;vein;skin;retina;uterus;prostate;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve;thymus; tumor;white blood cells; 0.98740 0.15588 -0.273576253 33.97027601 13.34485 0.48535 EIF3EP1 . . . eukaryotic translation initiation factor 3 subunit E pseudogene 1 . . . . . . . . . . . EIF3EP2 . . . eukaryotic translation initiation factor 3 subunit E pseudogene 2 . . . . . . . . . . . EIF3EP3 . . . eukaryotic translation initiation factor 3 subunit E pseudogene 3 . . . . . . . . . . . EIF3EP4 . . . eukaryotic translation initiation factor 3 subunit E pseudogene 4 . . . . . . . . . . . EIF3F 0.669067337550454 0.329883135292594 0.00104952715695203 eukaryotic translation initiation factor 3 subunit F FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. {ECO:0000255|HAMAP- Rule:MF_03005, ECO:0000269|PubMed:21124883}.; . . lymphoreticular;ovary;salivary gland;colon;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;hypothalamus;spinal cord;muscle;blood;lens;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion; 0.20443 0.11208 -0.291981272 33.20358575 455.62295 4.43443 EIF3FP1 . . . eukaryotic translation initiation factor 3 subunit F pseudogene 1 . . . . . . . . . . . EIF3FP2 . . . eukaryotic translation initiation factor 3 subunit F pseudogene 2 . . . . . . . . . . . EIF3FP3 . . . eukaryotic translation initiation factor 3 subunit F pseudogene 3 . . . . . . . . . . . EIF3G 0.983422491559563 0.0165674103126343 1.00981278031589e-05 eukaryotic translation initiation factor 3 subunit G FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre- initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. This subunit can bind 18S rRNA. In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}.; . . lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;iris;bladder;brain;amygdala;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; testis - interstitial;liver;testis; 0.38539 0.11809 -0.846787714 11.05803255 15.29088 0.55064 EIF3H 0.465051249825806 0.533792584799043 0.00115616537515159 eukaryotic translation initiation factor 3 subunit H FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.; . . myocardium;lymphoreticular;smooth muscle;ovary;substantia nigra;skin;bone marrow;retina;prostate;optic nerve;endometrium;gum;germinal center;brain;tonsil;heart;cartilage;blood;lens;skeletal muscle;greater omentum;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;vein;uterus;whole body;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;aorta; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;tumor;ciliary ganglion;white blood cells;pons;trigeminal ganglion; 0.96842 0.23432 -0.383807564 27.41802312 20.00044 0.68192 EIF3I 0.417329824985689 0.581009824495841 0.00166035051847015 eukaryotic translation initiation factor 3 subunit I FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;optic nerve;bone;testis;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;islets of Langerhans;pineal body;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; superior cervical ganglion;skeletal muscle; 0.81933 0.38767 -0.163345027 41.24793583 10.71668 0.38860 EIF3IP1 . . . eukaryotic translation initiation factor 3 subunit I pseudogene 1 . . . . . . . . . . . EIF3J 0.859084260110388 0.140463030401696 0.000452709487916176 eukaryotic translation initiation factor 3 subunit J FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. This subunit binds directly within the mRNA entry channel of the 40S ribosome to the aminoacyl (A) site. It may regulate the interaction between the 43S PIC and mRNA.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;duodenum;liver;cervix;head and neck;kidney;mammary gland;stomach;peripheral nerve; amygdala;dorsal root ganglion;medulla oblongata;superior cervical ganglion;ciliary ganglion;atrioventricular node;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.59194 0.14047 0.147123112 64.11299835 1108.12894 6.36378 EIF3J-AS1 . . . EIF3J antisense RNA 1 (head to head) . . . . . . . . . . . EIF3K 0.00233163486953566 0.92447505921497 0.0731933059154947 eukaryotic translation initiation factor 3 subunit K FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.; . TISSUE SPECIFICITY: Ubiquitous, with the highest levels of expression in brain, testis and kidney. {ECO:0000269|PubMed:14519125}.; myocardium;lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;endometrium;gum;thyroid;brain;bladder;gall bladder;tonsil;heart;tongue;pineal body;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;pia mater;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; whole brain;heart;white blood cells;kidney;skeletal muscle;cerebellum; 0.43691 0.20297 0.349177632 74.18023119 59.17651 1.55969 EIF3KP1 . . . eukaryotic translation initiation factor 3 subunit K pseudogene 1 . . . . . . . . . . . EIF3KP2 . . . eukaryotic translation initiation factor 3 subunit K pseudogene 2 . . . . . . . . . . . EIF3KP3 . . . eukaryotic translation initiation factor 3 subunit K pseudogene 3 . . . . . . . . . . . EIF3L 0.93881361379477 0.0611842308708074 2.15533442312302e-06 eukaryotic translation initiation factor 3 subunit L FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre- initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;frontal lobe;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;islets of Langerhans;muscle;urinary;pharynx;blood;breast;bile duct;lung;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach; fetal brain;thyroid;white blood cells; 0.10378 0.12326 -0.758599262 13.32861524 8.36913 0.30609 EIF3LP1 . . . eukaryotic translation initiation factor 3 subunit L pseudogene 1 . . . . . . . . . . . EIF3LP2 . . . eukaryotic translation initiation factor 3 subunit L pseudogene 2 . . . . . . . . . . . EIF3LP3 . . . eukaryotic translation initiation factor 3 subunit L pseudogene 3 . . . . . . . . . . . EIF3M 0.981660594170631 0.018336782856932 2.62297243668643e-06 eukaryotic translation initiation factor 3 subunit M FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. May favor virus entry in case of infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2). {ECO:0000255|HAMAP-Rule:MF_03012, ECO:0000269|PubMed:15919898, ECO:0000269|PubMed:17403899}.; . TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:15919898}.; medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;bone;pituitary gland;testis;dura mater;spinal ganglion;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;muscle;bile duct;pancreas;pia mater;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;kidney;stomach;aorta;thymus; tumor;white blood cells; 0.54053 0.12038 -0.183570861 39.95046001 23.02701 0.76851 EIF4A1 0.999614421273252 0.00038557768921707 1.03753127636823e-09 eukaryotic translation initiation factor 4A1 FUNCTION: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon. {ECO:0000269|PubMed:19153607, ECO:0000269|PubMed:19204291}.; . . lymphoreticular;ovary;colon;skin;bone marrow;prostate;frontal lobe;testis;brain;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach; . 0.99419 0.42641 -0.361761279 28.6329323 4.86778 0.17953 EIF4A1P1 . . . eukaryotic translation initiation factor 4A1 pseudogene 1 . . . . . . . . . . . EIF4A1P2 . . . eukaryotic translation initiation factor 4A1 pseudogene 2 . . . . . . . . . . . EIF4A1P3 . . . eukaryotic translation initiation factor 4A1 pseudogene 3 . . . . . . . . . . . EIF4A1P4 . . . eukaryotic translation initiation factor 4A1 pseudogene 4 . . . . . . . . . . . EIF4A1P5 . . . eukaryotic translation initiation factor 4A1 pseudogene 5 . . . . . . . . . . . EIF4A1P6 . . . eukaryotic translation initiation factor 4A1 pseudogene 6 . . . . . . . . . . . EIF4A1P7 . . . eukaryotic translation initiation factor 4A1 pseudogene 7 . . . . . . . . . . . EIF4A1P8 . . . eukaryotic translation initiation factor 4A1 pseudogene 8 . . . . . . . . . . . EIF4A1P9 . . . eukaryotic translation initiation factor 4A1 pseudogene 9 . . . . . . . . . . . EIF4A1P10 . . . eukaryotic translation initiation factor 4A1 pseudogene 10 . . . . . . . . . . . EIF4A1P11 . . . eukaryotic translation initiation factor 4A1 pseudogene 11 . . . . . . . . . . . EIF4A1P12 . . . eukaryotic translation initiation factor 4A1 pseudogene 12 . . . . . . . . . . . EIF4A1P13 . . . eukaryotic translation initiation factor 4A1 pseudogene 13 . . . . . . . . . . . EIF4A2 0.997112604533517 0.002887255059909 1.40406574223878e-07 eukaryotic translation initiation factor 4A2 FUNCTION: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;small intestine;cerebellum cortex;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;cerebellum; whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;pituitary;parietal lobe;cerebellum; 0.98068 0.14229 -0.207437529 38.2814343 4.79763 0.17467 EIF4A2P1 . . . eukaryotic translation initiation factor 4A2 pseudogene 1 . . . . . . . . . . . EIF4A2P2 . . . eukaryotic translation initiation factor 4A2 pseudogene 2 . . . . . . . . . . . EIF4A2P3 . . . eukaryotic translation initiation factor 4A2 pseudogene 3 . . . . . . . . . . . EIF4A2P4 . . . eukaryotic translation initiation factor 4A2 pseudogene 4 . . . . . . . . . . . EIF4A2P5 . . . eukaryotic translation initiation factor 4A2 pseudogene 5 . . . . . . . . . . . EIF4A3 0.998989654876332 0.00101033427371516 1.08499524958631e-08 eukaryotic translation initiation factor 4A3 FUNCTION: ATP-dependent RNA helicase. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly. Involved in craniofacial development. {ECO:0000269|PubMed:15034551, ECO:0000269|PubMed:16170325, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:17375189, ECO:0000269|PubMed:19409878, ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:24360810}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10623621}.; smooth muscle;ovary;skin;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;aorta; testis - interstitial;adrenal cortex;testis; 0.18593 0.20297 -0.626318434 17.03231894 9.44537 0.34823 EIF4A3P1 . . . eukaryotic translation initiation factor 4A3 pseudogene 1 . . . . . . . . . . . EIF4B 0.99998652408939 1.34759103166617e-05 2.93665784768038e-13 eukaryotic translation initiation factor 4B FUNCTION: Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'- terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F.; . . lymphoreticular;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;larynx;thyroid;testis;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;lung;adrenal gland;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;globus pallidus;white blood cells;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.66882 0.27989 -0.53631094 20.53550366 187.16747 2.97007 EIF4BP1 . . . eukaryotic translation initiation factor 4B pseudogene 1 . . . . . . . . . . . EIF4BP2 . . . eukaryotic translation initiation factor 4B pseudogene 2 . . . . . . . . . . . EIF4BP3 . . . eukaryotic translation initiation factor 4B pseudogene 3 . . . . . . . . . . . EIF4BP4 . . . eukaryotic translation initiation factor 4B pseudogene 4 . . . . . . . . . . . EIF4BP5 . . . eukaryotic translation initiation factor 4B pseudogene 5 . . . . . . . . . . . EIF4BP6 . . . eukaryotic translation initiation factor 4B pseudogene 6 . . . . . . . . . . . EIF4BP7 . . . eukaryotic translation initiation factor 4B pseudogene 7 . . . . . . . . . . . EIF4BP8 . . . eukaryotic translation initiation factor 4B pseudogene 8 . . . . . . . . . . . EIF4BP9 . . . eukaryotic translation initiation factor 4B pseudogene 9 . . . . . . . . . . . EIF4E 0.983573342194326 0.0164167840267913 9.87377888252887e-06 eukaryotic translation initiation factor 4E FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates the binding to the mRNA cap. {ECO:0000269|PubMed:16271312, ECO:0000269|PubMed:22578813}.; DISEASE: Autism 19 (AUTS19) [MIM:615091]: A complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation. {ECO:0000269|PubMed:19556253}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. A heterozygous single-nucleotide insertion has been found in families affected by autism. The variant results in increased promoter activity and is involved in disease pathogenesis through EIF4E deregulation (PubMed:19556253). {ECO:0000269|PubMed:19556253}.; DISEASE: Note=A chromosomal aberration involving EIF4E has been found in a patient with classic autism. Translocation t(45)(q23q31.3). The breakpoint on chromosome 4 is located 56 kb downstream of EIF4E (PubMed:19556253). {ECO:0000269|PubMed:19556253}.; . medulla oblongata;smooth muscle;ovary;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;pituitary gland;testis;dura mater;germinal center;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);meninges;heart;hypothalamus;blood;lens;skeletal muscle;bile duct;pancreas;pia mater;lung;adrenal gland;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;stomach;aorta;thymus; amygdala;dorsal root ganglion;medulla oblongata;superior cervical ganglion;occipital lobe;temporal lobe;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.93654 0.38765 -0.031067188 51.03798066 0.16068 0.00333 EIF4E1B 0.111053691650741 0.860062191598093 0.0288841167511657 eukaryotic translation initiation factor 4E family member 1B FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structure. {ECO:0000250}.; . . . . . 0.10553 0.571462851 81.99457419 51.62786 1.41859 EIF4E2 0.91955877975189 0.0803359414915663 0.000105278756543224 eukaryotic translation initiation factor 4E family member 2 FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures.; . . ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;uterus;prostate;whole body;endometrium;synovium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);heart;cerebellum cortex;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;lung;placenta;liver;trigeminal ganglion;skeletal muscle; 0.17819 0.09139 -0.339715008 30.06605331 15.40745 0.55342 EIF4E2P1 . . . eukaryotic translation initiation factor 4E family member 2 pseudogene 1 . . . . . . . . . . . EIF4E2P2 . . . eukaryotic translation initiation factor 4E family member 2 pseudogene 2 . . . . . . . . . . . EIF4E3 0.00423250331377467 0.865055705768148 0.130711790918077 eukaryotic translation initiation factor 4E family member 3 FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis. May act as an inhibitor of EIF4E1 activity (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);amygdala;cartilage;heart;ovary;islets of Langerhans;colon;skin;skeletal muscle;retina;bone marrow;uterus;whole body;lung;endometrium;trabecular meshwork;thyroid;placenta;hippocampus;iris;testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.46792 0.11262 -0.09720619 46.20193442 12.95683 0.47196 EIF4EBP1 0.184082876876197 0.645919868880287 0.169997254243516 eukaryotic translation initiation factor 4E binding protein 1 FUNCTION: Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. {ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:7935836}.; . . ovary;salivary gland;developmental;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);trophoblast;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; lung;heart;liver; 0.61974 0.29145 . . 3.04371 0.11042 EIF4EBP1P1 . . . eukaryotic translation initiation factor 4E binding protein 1 pseudogene 1 . . . . . . . . . . . EIF4EBP1P2 . . . eukaryotic translation initiation factor 4E binding protein 1 pseudogene 2 . . . . . . . . . . . EIF4EBP2 0.694677115504761 0.287890709283753 0.0174321752114853 eukaryotic translation initiation factor 4E binding protein 2 FUNCTION: Repressor of translation initiation involved in synaptic plasticity, learning and memory formation (By similarity). Regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form of EIF4EBP2 competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation (PubMed:25533957). EIF4EBP2 is enriched in brain and acts as a regulator of synapse activity and neuronal stem cell renewal via its ability to repress translation initiation (By similarity). Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways (By similarity). {ECO:0000250|UniProtKB:P70445, ECO:0000269|PubMed:25533957}.; . . . . 0.29913 0.11262 -0.163345027 41.24793583 8.60496 0.31587 EIF4EBP2P1 . . . eukaryotic translation initiation factor 4E binding protein 2 pseudogene 1 . . . . . . . . . . . EIF4EBP2P2 . . . eukaryotic translation initiation factor 4E binding protein 2 pseudogene 2 . . . . . . . . . . . EIF4EBP2P3 . . . eukaryotic translation initiation factor 4E binding protein 2 pseudogene 3 . . . . . . . . . . . EIF4EBP3 0.0542430246091404 0.702120832337414 0.243636143053445 eukaryotic translation initiation factor 4E binding protein 3 FUNCTION: Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. {ECO:0000250|UniProtKB:Q13541}.; . TISSUE SPECIFICITY: Expression is highest in skeletal muscle, heart, kidney, and pancreas, whereas there is very little expression in brain and thymus. {ECO:0000269|PubMed:9593750}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;muscle;blood;lens;skeletal muscle;lung;placenta;macula lutea;liver;spleen;mammary gland;stomach;peripheral nerve; . . 0.11167 0.013025609 54.62962963 5.73826 0.21485 EIF4ENIF1 0.999689053765957 0.000310946233013003 1.02979004628938e-12 eukaryotic translation initiation factor 4E nuclear import factor 1 FUNCTION: Nucleoplasmic shuttling protein. Mediates the nuclear import of EIF4E by a piggy-back mechanism.; . TISSUE SPECIFICITY: Widely expressed.; smooth muscle;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;adrenal cortex;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach; . 0.37607 0.23099 -0.973616687 8.8995046 113.80534 2.32557 EIF4EP1 . . . eukaryotic translation initiation factor 4E pseudogene 1 . . . . . . . . . . . EIF4EP2 . . . eukaryotic translation initiation factor 4E pseudogene 2 . . . . . . . . . . . EIF4EP3 . . . eukaryotic translation initiation factor 4E pseudogene 3 . . . . . . . . . . . EIF4EP4 . . . eukaryotic translation initiation factor 4E pseudogene 4 . . . . . . . . . . . EIF4EP5 . . . eukaryotic translation initiation factor 4E pseudogene 5 . . . . . . . . . . . EIF4G1 0.999999999936491 6.35087555662035e-11 6.29429189596712e-27 eukaryotic translation initiation factor 4 gamma 1 FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome.; DISEASE: Parkinson disease 18 (PARK18) [MIM:614251]: An autosomal dominant, late-onset form of Parkinson disease. Parkinson disease is a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. {ECO:0000269|PubMed:21907011}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;muscle;adrenal cortex;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;duodenum;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;prostate;thyroid;liver;trigeminal ganglion;parietal lobe;skeletal muscle; 0.87963 0.17117 -1.271459448 5.207596131 356.57929 3.99843 EIF4G2 . . . eukaryotic translation initiation factor 4 gamma 2 FUNCTION: Appears to play a role in the switch from cap-dependent to IRES-mediated translation during mitosis, apoptosis and viral infection. Cleaved by some caspases and viral proteases. {ECO:0000269|PubMed:11511540, ECO:0000269|PubMed:11943866, ECO:0000269|PubMed:9032289, ECO:0000269|PubMed:9049310}.; . TISSUE SPECIFICITY: Ubiquitously expressed in all adult tissues examined, with high levels in skeletal muscle and heart. Also expressed in fetal brain, lung, liver and kidney. {ECO:0000269|PubMed:9030685, ECO:0000269|PubMed:9032289, ECO:0000269|PubMed:9049310}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;oesophagus;gum;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;kidney;mammary gland;aorta;stomach;thymus; occipital lobe;fetal brain;testis;ciliary ganglion;parietal lobe;skeletal muscle; 0.81317 0.15304 -1.087493118 7.106628922 18.07447 0.63052 EIF4G3 0.999999906532496 9.34675036344982e-08 1.34095481705077e-20 eukaryotic translation initiation factor 4 gamma 3 FUNCTION: Probable component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Thought to be a functional homolog of EIF4G1. {ECO:0000269|PubMed:9418880}.; . . myocardium;ovary;sympathetic chain;skin;bone marrow;retina;prostate;frontal lobe;endometrium;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;medulla oblongata;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.66507 . 0.299418187 71.70323189 263.5748 3.48374 EIF4H 0.922544880243499 0.0773595366435847 9.55831129158644e-05 eukaryotic translation initiation factor 4H FUNCTION: Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA. {ECO:0000269|PubMed:10585411, ECO:0000269|PubMed:11418588}.; . TISSUE SPECIFICITY: The short isoform is the predominant isoform and is expressed alone in liver and skeletal muscle. Both isoforms are expressed in fibroblast, spleen, testis and bone marrow. Levels are high in lung and pancreas and low in heart, frontal cortex and kidney. {ECO:0000269|PubMed:11003705, ECO:0000269|PubMed:8812460}.; lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;heart;tongue;blood;lens;breast;visual apparatus;macula lutea;liver;cervix;mammary gland;peripheral nerve;colon;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;aorta;stomach;thymus;cerebellum; whole brain;subthalamic nucleus;thalamus;cerebellum peduncles;placenta;prefrontal cortex;globus pallidus;caudate nucleus;cingulate cortex;parietal lobe;cerebellum; 0.52550 0.15968 -0.029247611 51.40363293 10.30437 0.37575 EIF4HP1 . . . eukaryotic translation initiation factor 4H pseudogene 1 . . . . . . . . . . . EIF4HP2 . . . eukaryotic translation initiation factor 4H pseudogene 2 . . . . . . . . . . . EIF5 0.907859809790479 0.0921099143858646 3.02758236569108e-05 eukaryotic translation initiation factor 5 FUNCTION: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]).; . . ovary;skin;retina;bone marrow;subthalamic nucleus;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach; amygdala;occipital lobe;testis - interstitial;superior cervical ganglion;medulla oblongata;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal liver;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex; 0.79326 0.13538 -0.692458599 14.96815287 22.15109 0.74315 EIF5A 0.890876903696708 0.108003450628589 0.00111964567470253 eukaryotic translation initiation factor 5A FUNCTION: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. With syntenin SDCBP, functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis. Regulates also TNF- alpha-mediated apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation. Also described as a cellular cofactor of human T-cell leukemia virus type I (HTLV-1) Rex protein and of human immunodeficiency virus type 1 (HIV-1) Rev protein, essential for mRNA export of retroviral transcripts. {ECO:0000269|PubMed:15371445, ECO:0000269|PubMed:15452064, ECO:0000269|PubMed:16987817, ECO:0000269|PubMed:17187778, ECO:0000269|PubMed:17360499}.; . TISSUE SPECIFICITY: Expressed in umbilical vein endothelial cells and several cancer cell lines (at protein level). {ECO:0000269|PubMed:16519677}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; . 0.29774 -0.053113545 49.38664779 4.08635 0.14955 EIF5A2 0.167390171566573 0.771777839223557 0.0608319892098705 eukaryotic translation initiation factor 5A2 FUNCTION: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:14622290}.; . TISSUE SPECIFICITY: Expressed in ovarian and colorectal cancer cell lines (at protein level). Highly expressed in testis. Overexpressed in some cancer cells. {ECO:0000269|PubMed:11161802, ECO:0000269|PubMed:16519677}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;brain;unclassifiable (Anatomical System);amygdala;islets of Langerhans;hypothalamus;lens;lung;nasopharynx;placenta;macula lutea;hippocampus;visual apparatus;liver;spleen;kidney;stomach;aorta; superior cervical ganglion;ciliary ganglion; 0.49170 0.13588 0.079165051 59.43029016 5.53805 0.20646 EIF5A2P1 . . . eukaryotic translation initiation factor 5A2 pseudogene 1 . . . . . . . . . . . EIF5AL1 . . . eukaryotic translation initiation factor 5A-like 1 FUNCTION: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation (By similarity). {ECO:0000250}.; . . . . . 0.29774 . . 18.72537 0.64596 EIF5AP2 . . . eukaryotic translation initiation factor 5A pseudogene 2 . . . . . . . . . . . EIF5AP3 . . . eukaryotic translation initiation factor 5A pseudogene 3 . . . . . . . . . . . EIF5AP4 . . . eukaryotic translation initiation factor 5A pseudogene 4 . . . . . . . . . . . EIF5B 0.895387512560445 0.104612486854755 5.84799424114745e-10 eukaryotic translation initiation factor 5B FUNCTION: Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;salivary gland;foreskin;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;cerebral cortex;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;cervix;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;medulla oblongata;olfactory bulb;testis - seminiferous tubule;ciliary ganglion;trigeminal ganglion;cingulate cortex;skeletal muscle;parietal lobe; 0.97150 0.21066 -0.196519234 39.20736023 107.37591 2.24999 EIF5P1 . . . eukaryotic translation initiation factor 5 pseudogene 1 . . . . . . . . . . . EIF5P2 . . . eukaryotic translation initiation factor 5 pseudogene 2 . . . . . . . . . . . EIF6 0.781942924365479 0.216569394748479 0.00148768088604182 eukaryotic translation initiation factor 6 FUNCTION: Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. May behave as a stimulatory translation initiation factor downstream insulin/growth factors. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export. Cytoplasmic release of TIF6 from 60S subunits and nuclear relocalization is promoted by a RACK1 (GNB2L1)-dependent protein kinase C activity. {ECO:0000255|HAMAP-Rule:MF_03132, ECO:0000269|PubMed:10085284, ECO:0000269|PubMed:14654845, ECO:0000269|PubMed:21536732}.; . TISSUE SPECIFICITY: Expressed at very high levels in colon carcinoma with lower levels in normal colon and ileum and lowest levels in kidney and muscle (at protein level). {ECO:0000269|PubMed:11290417}.; . . 0.43993 0.13443 0.038710339 56.92380278 44.89079 1.28641 EJM2 . . . epilepsy, juvenile myoclonic 2 . . . . . . . . . . . ELAC1 0.895039746012204 0.10394709574849 0.00101315823930582 elaC ribonuclease Z 1 FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'- processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.; . TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:11401430}.; ovary;colon;substantia nigra;parathyroid;skin;uterus;prostate;whole body;frontal lobe;cochlea;cerebral cortex;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;skeletal muscle;lung;placenta;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.15243 0.16396 0.016664174 55.21939137 62.94617 1.62312 ELAC2 4.06301820140536e-11 0.920902554841294 0.0790974451180756 elaC ribonuclease Z 2 FUNCTION: Zinc phosphodiesterase, which displays mitochondrial tRNA 3'-processing endonuclease activity. Involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. {ECO:0000269|PubMed:21593607}.; DISEASE: Combined oxidative phosphorylation deficiency 17 (COXPD17) [MIM:615440]: An autosomal recessive disorder of mitochondrial dysfunction characterized by onset of severe hypertrophic cardiomyopathy in the first year of life. Other features include hypotonia, poor growth, lactic acidosis, and failure to thrive. The disorder may be fatal in early childhood. {ECO:0000269|PubMed:23849775}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart, placenta, liver, skeletal muscle, kidney, pancreas, testis and ovary. Weakly expressed in brain, lung, spleen, thymus, prostate, small intestine, colon and leukocytes. {ECO:0000269|PubMed:11175785}.; lymphoreticular;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;tongue;pineal body;pharynx;blood;lens;skeletal muscle;greater omentum;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;mesenchyma;placenta;hippocampus;hypopharynx;amnion;head and neck;kidney;stomach; prefrontal cortex;white blood cells;skeletal muscle; 0.04345 0.09787 -0.905656269 10.12031139 1342.48638 6.87747 ELANE 0.767207228111322 0.231003692811876 0.00178907907680186 elastase, neutrophil expressed FUNCTION: Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis. {ECO:0000269|PubMed:15140022}.; DISEASE: Neutropenia, severe congenital 1, autosomal dominant (SCN1) [MIM:202700]: A disorder of hematopoiesis characterized by maturation arrest of granulopoiesis at the level of promyelocytes with peripheral blood absolute neutrophil counts below 0.5 x 10(9)/l and early onset of severe bacterial infections. {ECO:0000269|PubMed:11001877, ECO:0000269|PubMed:11675333, ECO:0000269|PubMed:12091371, ECO:0000269|PubMed:14962902, ECO:0000269|PubMed:17436313, ECO:0000269|PubMed:18946670, ECO:0000269|PubMed:19036076, ECO:0000269|PubMed:19415009, ECO:0000269|PubMed:19927291, ECO:0000269|PubMed:20220065, ECO:0000269|PubMed:20803142, ECO:0000269|PubMed:21425445, ECO:0000269|PubMed:23463630}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Bone marrow cells.; unclassifiable (Anatomical System);optic nerve;lung;macula lutea;liver;cervix;spleen;blood;fovea centralis;choroid;lens;retina;bone marrow; bone marrow; 0.60870 0.91567 0.194852702 67.03231894 67.22126 1.69633 ELAVL1 0.959986603851889 0.0399243272074458 8.9068940664928e-05 ELAV like RNA binding protein 1 FUNCTION: RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability. Involved in embryonic stem cells (ESCs) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESCs differentiation. Binds to poly-U elements and AU- rich elements (AREs) in the 3'-UTR of target mRNAs. Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, binds to a core element of 27 nucleotides that contain AUUUA, AUUUUA, and AUUUUUA motifs. Binds preferentially to the 5'-UUUU[AG]UUU-3' motif in vitro. With ZNF385A, binds the 3'-UTR of p53/TP53 mRNA to control their nuclear export induced by CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the CDKN2A anti-proliferative activity. May also bind with ZNF385A the CCNB1 mRNA. {ECO:0000269|PubMed:19029303}.; . TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;muscle;bile duct;pancreas;lung;cornea;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; . 0.41503 0.49283 -0.317668748 31.45789101 12.81067 0.46627 ELAVL2 0.972927704179956 0.0270384815974611 3.38142225829353e-05 ELAV like neuron-specific RNA binding protein 2 FUNCTION: Binds RNA. Seems to recognize a GAAA motif. Can bind to its own 3'-UTR, the FOS 3'-UTR and the ID 3'-UTR.; . TISSUE SPECIFICITY: Brain; neural-specific.; unclassifiable (Anatomical System);medulla oblongata;ovary;lacrimal gland;hypothalamus;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;frontal lobe;placenta;bone;macula lutea;hippocampus;testis;brain; dorsal root ganglion;testis - interstitial;occipital lobe;superior cervical ganglion;subthalamic nucleus;temporal lobe;testis;globus pallidus;trigeminal ganglion;parietal lobe; 0.61357 0.27035 -0.405853867 26.23260203 13.64166 0.49554 ELAVL3 0.822602583621291 0.176556391686242 0.000841024692466664 ELAV like neuron-specific RNA binding protein 3 FUNCTION: Binds to AU-rich sequences (AREs) of target mRNAs, including VEGF mRNA. May also bind poly-A tracts via RRM 3 (By similarity). May be involved in neuronal differentiation and maintenance. {ECO:0000250, ECO:0000269|PubMed:10710437}.; . TISSUE SPECIFICITY: Brain specific.; unclassifiable (Anatomical System);ovary;nervous;hypothalamus;blood;parathyroid;fovea centralis;choroid;lens;retina;bone marrow;optic nerve;lung;frontal lobe;placenta;macula lutea;visual apparatus;brain;aorta;cerebellum; subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.39015 0.23372 -0.780646273 12.77423921 9.21155 0.33694 ELAVL4 0.976912761697479 0.0230644148561025 2.28234464182909e-05 ELAV like neuron-specific RNA binding protein 4 FUNCTION: May play a role in neuron-specific RNA processing. Protects CDKN1A mRNA from decay by binding to its 3'-UTR (By similarity). Binds to AU-rich sequences (AREs) of target mRNAs, including VEGF and FOS mRNA. {ECO:0000250, ECO:0000269|PubMed:10710437, ECO:0000269|PubMed:7898713}.; . TISSUE SPECIFICITY: Brain.; unclassifiable (Anatomical System);lung;whole body;islets of Langerhans;placenta;sympathetic chain;hippocampus;testis;brain; whole brain;amygdala;dorsal root ganglion;medulla oblongata;occipital lobe;temporal lobe;pons;atrioventricular node;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.68875 0.15149 -0.095386216 46.48502005 19.6708 0.67387 ELDR . . . EGFR long non-coding downstream RNA . . . . . . . . . . . ELF1 0.547779993268523 0.452096613216507 0.000123393514969588 E74 like ETS transcription factor 1 FUNCTION: Transcription factor that activates the LYN and BLK promoters. Appears to be required for the T-cell-receptor-mediated trans activation of HIV-2 gene expression. Binds specifically to two purine-rich motifs in the HIV-2 enhancer. {ECO:0000269|PubMed:8756667}.; . TISSUE SPECIFICITY: In fetal tissues, it is highly expressed in heart, lung liver and kidney, and weakly expressed in brain. In adult, it is highly expressed in pancreas, spleen, thymus and peripheral blood leukocytes, expressed at moderate levels in heart, placenta, lung, liver, skeletal muscle, kidney, prostate, ovary, small intestine and colon, and weakly expressed in brain and testis. {ECO:0000269|PubMed:8756667, ECO:0000269|PubMed:9524226}.; myocardium;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;brain;tonsil;amygdala;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;pancreas;lung;cornea;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;thymus; prostate;trachea;thyroid;placenta;white blood cells;whole blood;tonsil;thymus;bone marrow; 0.76801 0.11538 0.312359769 72.71172446 5928.95524 16.00243 ELF2 0.985385386978225 0.0146131122761113 1.50074566399378e-06 E74 like ETS transcription factor 2 FUNCTION: Isoform 1 transcriptionally activates the LYN and BLK promoters and acts synergistically with RUNX1 to transactivate the BLK promoter.; . TISSUE SPECIFICITY: Expressed in all fetal and adult tissues examined. Among fetal tissues, highest levels of expression detected in heart, lung, liver and kidney, and lower levels in brain. Among adult tissues, highest levels of expression detected in heart, placenta, lung, skeletal muscle, spleen, thymus, testis and ovary. Moderate expression in prostate, small intestine, kidney, liver and pancreas, and weak expression in colon, brain and peripheral blood lymphocytes. {ECO:0000269|PubMed:8756667}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;thyroid;bone;testis;germinal center;brain;artery;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;spleen;head and neck;kidney;stomach;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.19471 0.14089 0.52918614 80.81505072 355.52103 3.99118 ELF2P1 . . . E74-like factor 2 pseudogene 1 . . . . . . . . . . . ELF2P2 . . . E74-like factor 2 pseudogene 2 . . . . . . . . . . . ELF2P3 . . . E74-like factor 2 pseudogene 3 . . . . . . . . . . . ELF2P4 . . . E74-like factor 2 pseudogene 4 . . . . . . . . . . . ELF3 0.986666748385297 0.0133320536624106 1.19795229199535e-06 E74 like ETS transcription factor 3 FUNCTION: Transcriptional activator that binds and transactivates ETS sequences containing the consensus nucleotide core sequence GGA[AT]. Acts synergistically with POU2F3 to transactivate the SPRR2A promoter and with RUNX1 to transactivate the ANGPT1 promoter. Also transactivates collagenase, CCL20, CLND7, FLG, KRT8, NOS2, PTGS2, SPRR2B, TGFBR2 and TGM3 promoters. Represses KRT4 promoter activity. Involved in mediating vascular inflammation. May play an important role in epithelial cell differentiation and tumorigenesis. May be a critical downstream effector of the ERBB2 signaling pathway. May be associated with mammary gland development and involution. Plays an important role in the regulation of transcription with TATA-less promoters in preimplantation embryos, which is essential in preimplantation development (By similarity). {ECO:0000250, ECO:0000269|PubMed:10391676, ECO:0000269|PubMed:10644990, ECO:0000269|PubMed:10773884, ECO:0000269|PubMed:11036073, ECO:0000269|PubMed:11313868, ECO:0000269|PubMed:12414801, ECO:0000269|PubMed:12624109, ECO:0000269|PubMed:12682075, ECO:0000269|PubMed:12713734, ECO:0000269|PubMed:14715662, ECO:0000269|PubMed:14767472, ECO:0000269|PubMed:15075319, ECO:0000269|PubMed:15169914, ECO:0000269|PubMed:15794755, ECO:0000269|PubMed:16307850, ECO:0000269|PubMed:17060315, ECO:0000269|PubMed:9129154, ECO:0000269|PubMed:9234700, ECO:0000269|PubMed:9336459, ECO:0000269|PubMed:9395241, ECO:0000269|PubMed:9417054}.; . TISSUE SPECIFICITY: Expressed exclusively in tissues containing a high content of terminally differentiated epithelial cells including mammary gland, colon, trachea, kidney, prostate, uterus, stomach and skin. {ECO:0000269|PubMed:9129154, ECO:0000269|PubMed:9234700, ECO:0000269|PubMed:9336459, ECO:0000269|PubMed:9395241}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;endometrium;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.13920 0.31362 0.042348793 57.31304553 572.83419 4.85960 ELF4 0.611464084402785 0.386776178505737 0.00175973709147734 E74 like ETS transcription factor 4 FUNCTION: Transcriptional activator that binds to DNA sequences containing the consensus 5'-WGGA-3'. Transactivates promoters of the hematopoietic growth factor genes CSF2, IL3, IL8, and of the bovine lysozyme gene. Acts synergistically with RUNX1 to transactivate the IL3 promoter (By similarity). Also transactivates the PRF1 promoter in natural killer (NK) cells. Plays a role in the development and function of NK and NK T-cells and in innate immunity. Controls the proliferation and homing of CD8+ T-cells via the Kruppel-like factors KLF4 and KLF2 (By similarity). Controls cell senescence in a p53-dependent manner. Can also promote cellular transformation through inhibition of the p16 pathway. {ECO:0000250, ECO:0000269|PubMed:10207087, ECO:0000269|PubMed:14625302, ECO:0000269|PubMed:14976184, ECO:0000269|PubMed:19380490, ECO:0000269|PubMed:8895518, ECO:0000269|PubMed:9524226}.; DISEASE: Note=A chromosomal aberration involving ELF4 has been found in a case of acute myeloid leukemia (AML). Translocation t(X;21)(q25-26;q22) with ERG. {ECO:0000269|PubMed:16303180}.; TISSUE SPECIFICITY: Abundantly expressed in the placenta and in a variety of myeloid leukemia cell lines. Moderate levels of expression in heart, lung, spleen, thymus, peripheral blood lymphocytes, ovary and colon. Lower levels of expression in Jurkat T-cells and other T-cell lines and no expression in brain. {ECO:0000269|PubMed:8895518, ECO:0000269|PubMed:9524226}.; lymphoreticular;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;larynx;thyroid;testis;amniotic fluid;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;blood;breast;pancreas;lung;placenta;alveolus;liver;head and neck;spleen;kidney;mammary gland;stomach;cerebellum; lung;placenta;globus pallidus;white blood cells;atrioventricular node;whole blood;skeletal muscle;bone marrow; 0.49512 0.08696 -0.113792788 45.25831564 47.87953 1.34442 ELF5 0.0190865143588019 0.961465428974853 0.0194480566663452 E74 like ETS transcription factor 5 FUNCTION: Transcriptionally activator that may play a role in regulating the later stages of keratinocytes terminal differentiation. {ECO:0000269|PubMed:10506207}.; . TISSUE SPECIFICITY: Expressed exclusively in tissues with a high content of epithelial cells. Highly expressed in salivary gland, mammary gland, kidney and prostate. Weakly expressed in placenta and lung. Isoform 1 and isoform 2 are differentially expressed in different tissues. In the kidney, only isoform 1 was expressed, while prostate expressed both isoforms, with levels of isoform 2 being higher. Expression is up-regulated during keratinocyte differentiation. Several epithelial carcinoma cell lines showed lack of expression. {ECO:0000269|PubMed:10506207, ECO:0000269|PubMed:9840936}.; unclassifiable (Anatomical System);uterus;prostate;lung;heart;lacrimal gland;testis;colon;kidney;skin;skeletal muscle;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;medulla oblongata;trachea;salivary gland;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.30942 0.13105 -0.538132194 20.26421326 35.76631 1.07571 ELFN1 0.699066032235909 0.284194067812413 0.0167398999516772 extracellular leucine-rich repeat and fibronectin type III domain containing 1 FUNCTION: Postsynaptic protein that regulates circuit dynamics in the central nervous system by modulating the temporal dynamics of interneuron recruitment. Specifically present in excitatory synapses onto oriens-lacunosum molecular (OLM) interneurons and acts as a regulator of presynaptic release probability to direct the formation of highly facilitating pyramidal-OLM synapses (By similarity). Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. {ECO:0000250, ECO:0000269|PubMed:19389623}.; . . . . . . . . 295.30698 3.66787 ELFN1-AS1 . . . ELFN1 antisense RNA 1 . . . . . . . . . . . ELFN2 0.84901528665725 0.150440504250459 0.000544209092291015 extracellular leucine-rich repeat and fibronectin type III domain containing 2 FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. {ECO:0000269|PubMed:19389623}.; . . lymph node;brain; uterus corpus;medulla oblongata;superior cervical ganglion;occipital lobe;globus pallidus;atrioventricular node;trigeminal ganglion; 0.18208 . -1.835411529 2.081858929 137.02578 2.54496 ELK1 0.756057873787214 0.234569302136053 0.00937282407673343 ELK1, ETS transcription factor FUNCTION: Transcription factor that binds to purine-rich DNA sequences. Forms a ternary complex with SRF and the ETS and SRF motifs of the serum response element (SRE) on the promoter region of immediate early genes such as FOS and IER2. Induces target gene transcription upon JNK-signaling pathway stimulation (By similarity). {ECO:0000250|UniProtKB:A4GTP4, ECO:0000269|PubMed:1630903, ECO:0000269|PubMed:7889942}.; . TISSUE SPECIFICITY: Lung and testis.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;cerebellum; 0.99996 0.15613 0.327131069 73.27199811 572.0593 4.85348 ELK1P1 . . . ELK1, member of ETS oncogene family pseudogene 1 . . . . . . . . . . . ELK2AP . . . ELK2A, member of ETS oncogene family, pseudogene . . . . . . . . . . . ELK2BP . . . ELK2B, member of ETS oncogene family, pseudogene . . . . . . . . . . . ELK3 0.101741246004499 0.865040429099787 0.033218324895714 ELK3, ETS transcription factor FUNCTION: May be a negative regulator of transcription, but can activate transcription when coexpressed with Ras, Src or Mos. Forms a ternary complex with the serum response factor and the ETS and SRF motifs of the Fos serum response element.; . . unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;colon;skin;skeletal muscle;uterus;whole body;lung;nasopharynx;thyroid;placenta;liver;testis;spleen;germinal center;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.99665 0.12884 -0.222203495 37.54423213 177.97683 2.89980 ELK4 0.0845886750240457 0.871337360818669 0.0440739641572857 ELK4, ETS transcription factor FUNCTION: Involved in both transcriptional activation and repression. Interaction with SIRT7 leads to recruitment and stabilization of SIRT7 at promoters, followed by deacetylation of histone H3 at 'Lys-18' (H3K18Ac) and subsequent transcription repression. Forms a ternary complex with the serum response factor (SRF). Requires DNA-bound SRF for ternary complex formation and makes extensive DNA contacts to the 5'side of SRF, but does not bind DNA autonomously. {ECO:0000269|PubMed:22722849}.; . . medulla oblongata;ovary;colon;prostate;endometrium;thyroid;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);tongue;islets of Langerhans;blood;breast;lung;placenta;hippocampus;visual apparatus;liver;hypopharynx;cervix;spleen;head and neck;kidney;stomach; superior cervical ganglion;testis - seminiferous tubule;appendix;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.97352 0.09592 -0.404032746 26.53338051 34.43157 1.05188 ELL 0.940941238331597 0.0590567907656279 1.9709027750227e-06 elongation factor for RNA polymerase II FUNCTION: Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Elongation factor component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968, PubMed:23932780). Specifically required for stimulating the elongation step of RNA polymerase II- and III-dependent snRNA gene transcription (PubMed:23932780). ELL also plays an early role before its assembly into in the SEC complex by stabilizing RNA polymerase II recruitment/initiation and entry into the pause site. Required to stabilize the pre-initiation complex and early elongation. {ECO:0000269|PubMed:16006523, ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948, ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:22252557, ECO:0000269|PubMed:23932780, ECO:0000269|PubMed:8596958}.; . TISSUE SPECIFICITY: Expressed in all tissues tested. Highest levels found in placenta, skeletal muscle, testis and peripheral blood leukocytes.; lymphoreticular;medulla oblongata;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;tongue;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;placenta;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.48397 0.16855 -0.596992387 18.18825195 117.93921 2.36099 ELL2 0.99828854499778 0.00171144706781751 7.93440264337483e-09 elongation factor for RNA polymerase II 2 FUNCTION: Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968). Plays a role in immunoglobulin secretion in plasma cells: directs efficient alternative mRNA processing, influencing both proximal poly(A) site choice and exon skipping, as well as immunoglobulin heavy chain (IgH) alternative processing. Probably acts by regulating histone modifications accompanying transition from membrane- specific to secretory IgH mRNA expression. {ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948, ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:23251033}.; . . lymphoreticular;ovary;colon;parathyroid;skin;uterus;prostate;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;skeletal muscle;breast;pancreas;lung;epididymis;placenta;liver;hypopharynx;spleen;head and neck;cervix;kidney;stomach;peripheral nerve; . 0.44435 0.12744 0.108486928 61.90728946 2777.8585 9.95538 ELL2P1 . . . elongation factor for RNA polymerase II 2 pseudogene 1 . . . . . . . . . . . ELL2P2 . . . elongation factor for RNA polymerase II 2 pseudogene 2 . . . . . . . . . . . ELL2P3 . . . elongation factor for RNA polymerase II 2 pseudogene 3 . . . . . . . . . . . ELL2P4 . . . elongation factor for RNA polymerase II 2 pseudogene 4 . . . . . . . . . . . ELL3 3.17480785408243e-06 0.783663594228779 0.216333230963367 elongation factor for RNA polymerase II 3 FUNCTION: Enhancer-binding elongation factor that specifically binds enhancers in embryonic stem cells (ES cells), marks them, and is required for their future activation during stem cell specification. Does not only bind to enhancer regions of active genes, but also marks the enhancers that are in a poised or inactive state in ES cells and is required for establishing proper RNA polymerase II occupancy at developmentally regulated genes in a cohesin-dependent manner. Probably required for priming developmentally regulated genes for later recruitment of the super elongation complex (SEC), for transcriptional activation during differentiation. Required for recruitment of P-TEFb within SEC during differentiation. Probably preloaded on germ cell chromatin, suggesting that it may prime gene activation by marking enhancers as early as in the germ cells. Promoting epithelial-mesenchymal transition (EMT) (By similarity). Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968). {ECO:0000250, ECO:0000269|PubMed:10882741, ECO:0000269|PubMed:22195968}.; . TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:10882741}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;heart;islets of Langerhans;colon;blood;skin;skeletal muscle;uterus;prostate;pancreas;lung;endometrium;nasopharynx;bone;placenta;liver;testis;spleen;kidney;germinal center;brain;tonsil;stomach; . 0.09252 0.08312 0.485092724 79.37603208 884.77548 5.79433 ELMO1 0.993000631915938 0.00699936766989453 4.14167938233584e-10 engulfment and cell motility 1 FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in assocation with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1. {ECO:0000269|PubMed:11595183, ECO:0000269|PubMed:12134158}.; . TISSUE SPECIFICITY: Widely expressed, with a higher expression in the spleen and placenta.; ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cerebellum cortex;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;cerebellum; whole brain;amygdala;medulla oblongata;occipital lobe;thalamus;subthalamic nucleus;cerebellum peduncles;temporal lobe;prefrontal cortex;globus pallidus;pons;cingulate cortex;parietal lobe;cerebellum; 0.37805 0.16577 -0.534490515 20.70063694 43.0263 1.24480 ELMO1-AS1 . . . ELMO1 antisense RNA 1 . . . . . . . . . . . ELMO2 0.000350882321256971 0.999630464153957 1.86535247865218e-05 engulfment and cell motility 2 FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in assocation with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1. {ECO:0000269|PubMed:11595183, ECO:0000269|PubMed:11703939, ECO:0000269|PubMed:20679435}.; . TISSUE SPECIFICITY: Widely expressed, with a higher expression in skeletal muscle, kidney and placenta. {ECO:0000269|PubMed:11595183}.; smooth muscle;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;mammary gland;stomach;peripheral nerve; amygdala;whole brain;occipital lobe;superior cervical ganglion;cerebellum peduncles;prefrontal cortex;testis;globus pallidus;cingulate cortex;skeletal muscle;cerebellum; 0.27932 0.14131 -0.822919685 11.76574664 130.35074 2.48631 ELMO2P1 . . . engulfment and cell motility 2 pseudogene 1 . . . . . . . . . . . ELMO3 1.20206324348469e-07 0.985878913505631 0.0141209662880447 engulfment and cell motility 3 FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in assocation with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1 (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);islets of Langerhans;colon;blood;prostate;lung;endometrium;larynx;thyroid;placenta;liver;testis;head and neck;spleen;cervix;kidney;brain;mammary gland;stomach; testis; 0.18130 0.10790 0.562153464 81.71148856 1809.19268 7.84819 ELMOD1 0.536337679434055 0.460414739552087 0.00324758101385845 ELMO domain containing 1 FUNCTION: Acts as a GTPase-activating protein (GAP) toward guanine nucleotide exchange factors like ARL2, ARL3, ARF1 and ARF6, but not for GTPases outside the Arf family. {ECO:0000269|PubMed:17452337}.; . . unclassifiable (Anatomical System);cartilage;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;frontal lobe;cochlea;larynx;macula lutea;hippocampus;visual apparatus;head and neck;mammary gland;brain; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.10236 0.09622 -0.471992905 23.03609342 31.91015 1.00377 ELMOD2 0.804445977851897 0.19532926608285 0.000224756065252982 ELMO domain containing 2 FUNCTION: Acts as a GTPase-activating protein (GAP) toward guanine nucleotide exchange factors like ARL2, ARL3, ARF1 and ARF6, but not for GTPases outside the Arf family. Regulates IFN-related antiviral responses. {ECO:0000269|PubMed:17452337, ECO:0000269|PubMed:19966137}.; . . ovary;colon;parathyroid;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);cartilage;lacrimal gland;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.35237 0.11956 0.193034296 66.82000472 54.66599 1.47966 ELMOD3 4.56408780285543e-11 0.0533699707377029 0.946630029216656 ELMO domain containing 3 FUNCTION: Acts as a GTPase-activating protein (GAP) for ARL2 with low specific activity. {ECO:0000269|PubMed:24039609}.; . TISSUE SPECIFICITY: Both isoform 1 and isoform 6 are widely expressed. {ECO:0000269|PubMed:24039609}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;heart;cartilage;muscle;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.16716 . 0.665103516 84.6131163 711.58397 5.30149 ELMSAN1 0.999772779607384 0.000227220380903269 1.17128167271926e-11 ELM2 and Myb/SANT-like domain containing 1 . . . . . 0.57946 0.09931 -0.079012906 47.25760793 1091.15207 6.32169 ELN 1.51996287413625e-05 0.999915497445724 6.9302925534003e-05 elastin FUNCTION: Major structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly and recover completely. Molecular determinant of the late arterial morphogenesis, stabilizing arterial structure by regulating proliferation and organization of vascular smooth muscle (By similarity). {ECO:0000250|UniProtKB:P54320}.; DISEASE: Cutis laxa, autosomal dominant, 1 (ADCL1) [MIM:123700]: A connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. Additional variable clinical features are gastrointestinal diverticula, hernia, and genital prolapse. Rare manifestations are pulmonary artery stenosis, aortic aneurysm, bronchiectasis, and emphysema. {ECO:0000269|PubMed:9873040}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Supravalvular aortic stenosis (SVAS) [MIM:185500]: Congenital narrowing of the ascending aorta which can occur sporadically, as an autosomal dominant condition, or as one component of Williams-Beuren syndrome. {ECO:0000269|PubMed:10942104}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=ELN is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of ELN may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease (PubMed:8812460). {ECO:0000269|PubMed:8812460}.; TISSUE SPECIFICITY: Expressed within the outer myometrial smooth muscle and throughout the arteriolar tree of uterus (at protein level). Also expressed in the large arteries, lung and skin. {ECO:0000269|PubMed:8812460}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;hypothalamus;muscle;skin;skeletal muscle;uterus;prostate;pancreas;whole body;lung;endometrium;placenta;bone;thyroid;testis;spleen;kidney;spinal ganglion;brain;stomach;aorta; superior cervical ganglion;adipose tissue;fetal lung;atrioventricular node;fetal thyroid;trigeminal ganglion;skeletal muscle; 0.93105 . -0.08265057 47.20452937 888.18423 5.80530 ELOF1 0.403135808004397 0.558206247186818 0.038657944808785 elongation factor 1 homolog FUNCTION: Transcription elongation factor implicated in the maintenance of proper chromatin structure in actively transcribed regions. {ECO:0000250}.; . . smooth muscle;ovary;salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;synovium;thyroid;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;trophoblast;heart;muscle;lens;skeletal muscle;lung;macula lutea;visual apparatus;liver;amnion;cervix;kidney;stomach;thymus; testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;trigeminal ganglion; 0.26833 0.11262 0.013025609 54.62962963 433.33205 4.34414 ELOVL1 0.223414530247304 0.768536418836924 0.00804905091577214 ELOVL fatty acid elongase 1 FUNCTION: Catalyzes the first and rate-limiting reaction of the four that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. Condensing enzyme that exhibits activity toward saturated C18 to C26 acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. May participate to the production of both saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Important for saturated C24:0 and monounsaturated C24:1 sphingolipid synthesis. Indirectly inhibits RPE65 via production of VLCFAs. {ECO:0000255|HAMAP-Rule:MF_03201, ECO:0000269|PubMed:20166112, ECO:0000269|PubMed:20937905}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:20937905}.; . . 0.49800 0.10153 0.03689118 56.64071715 26.98906 0.87177 ELOVL2 0.000198697181598092 0.902737542792624 0.0970637600257779 ELOVL fatty acid elongase 2 FUNCTION: Catalyzes the first and rate-limiting reaction of the four that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. Acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C20:4(n- 6) acyl-CoA. Condensing enzyme that catalyzes the synthesis of polyunsaturated very long chain fatty acid (C20- and C22-PUFA). May participate to the production of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP-Rule:MF_03202, ECO:0000269|PubMed:12371743, ECO:0000269|PubMed:20937905}.; . TISSUE SPECIFICITY: Liver and testis. {ECO:0000269|PubMed:20937905}.; unclassifiable (Anatomical System);heart;ovary;hypothalamus;parathyroid;skin;skeletal muscle;uterus;prostate;whole body;lung;frontal lobe;cochlea;placenta;visual apparatus;liver;testis;spleen;kidney;spinal ganglion;brain;mammary gland;peripheral nerve; fetal liver;occipital lobe;superior cervical ganglion;fetal brain;spinal cord;testis;parietal lobe; 0.87008 0.17956 -0.181750739 40.15687662 60.95094 1.58745 ELOVL2-AS1 . . . ELOVL2 antisense RNA 1 . . . . . . . . . . . ELOVL3 0.0100893512709736 0.824710911864718 0.165199736864309 ELOVL fatty acid elongase 3 FUNCTION: Catalyzes the first and rate-limiting reaction of the four that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:0 acyl-CoAs. May participate to the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:20937905}.; . TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:20937905}.; . . 0.06708 0.09234 0.170987912 65.5579146 21.76205 0.73209 ELOVL4 0.74105115457534 0.258448683411332 0.00050016201332877 ELOVL fatty acid elongase 4 FUNCTION: Catalyzes the first and rate-limiting reaction of the four that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. Condensing enzyme that specifically elongates C24:0 and C26:0 acyl-CoAs. May participate to the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May play a critical role in early brain and skin development. {ECO:0000255|HAMAP-Rule:MF_03204, ECO:0000269|PubMed:20937905}.; DISEASE: Stargardt disease 3 (STGD3) [MIM:600110]: A common hereditary macular degeneration. It is characterized by decreased central vision, atrophy of the macula and underlying retinal pigment epithelium, and frequent presence of prominent flecks in the posterior pole of the retina. {ECO:0000269|PubMed:11138005, ECO:0000269|PubMed:11581213}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ichthyosis, spastic quadriplegia, and mental retardation (ISQMR) [MIM:614457]: A severe autosomal recessive disorder characterized by ichthyosis apparent from birth, profound psychomotor retardation with essentially no development, spastic quadriplegia, and seizures. {ECO:0000269|PubMed:22100072}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spinocerebellar ataxia 34 (SCA34) [MIM:133190]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA34 is an autosomal dominant form characterized by the association of progressive cerebellar ataxia with erythrokeratodermia variabilis. {ECO:0000269|PubMed:24566826}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the retina and at much lower level in the brain. Ubiquitous, highest expression in thymus, followed by testis, small intestine, ovary, and prostate. Little or no expression in heart, lung, liver, or leukocates. {ECO:0000269|PubMed:20937905}.; . . 0.69400 0.09974 0.393270925 76.04977589 1023.81814 6.15180 ELOVL5 0.924260371630133 0.075649351997974 9.0276371892825e-05 ELOVL fatty acid elongase 5 FUNCTION: Catalyzes the first and rate-limiting reaction of the four that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. Condensing enzyme that acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate to the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:10970790, ECO:0000269|PubMed:20937905}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in the adrenal gland and testis. Weakly expressed in prostate, lung and brain. Expressed in the cerebellum. {ECO:0000269|PubMed:10970790, ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:25065913}.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;amygdala;cartilage;pharynx;blood;breast;trabecular meshwork;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;vein;uterus;whole body;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus;cerebellum; dorsal root ganglion;superior cervical ganglion;prostate;adipose tissue;adrenal gland;spinal cord;adrenal cortex;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;whole blood;cingulate cortex; 0.66708 . 0.080983847 59.76055674 25.28024 0.82695 ELOVL6 0.97107445684069 0.0288857142333782 3.98289259320318e-05 ELOVL fatty acid elongase 6 FUNCTION: Catalyzes the first and rate-limiting reaction of the four that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. Condensing enzyme that elongates fatty acids with 12, 14 and 16 carbons with higher activity toward C16:0 acyl-CoAs. Catalyzes the synthesis of unsaturated C16 long chain fatty acids and, to a lesser extent, C18:0 and those with low desaturation degree. May participate to the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP- Rule:MF_03206, ECO:0000269|PubMed:20937905}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:20937905}.; ovary;colon;parathyroid;skin;retina;uterus;optic nerve;whole body;larynx;bone;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;adrenal cortex;blood;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; fetal liver;superior cervical ganglion;adipose tissue;ciliary ganglion;trigeminal ganglion; 0.04544 0.03306 -0.207437529 38.2814343 . . ELOVL7 0.00156092226554038 0.882232714496789 0.116206363237671 ELOVL fatty acid elongase 7 FUNCTION: Catalyzes the first and rate-limiting reaction of the four that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate to the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP-Rule:MF_03207, ECO:0000269|PubMed:19826053, ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040}.; . TISSUE SPECIFICITY: Expressed in most tissues except heart and skeletal muscle. {ECO:0000269|PubMed:20937905}.; . . 0.12796 0.10172 0.060756528 58.52795471 71.64347 1.76147 ELP2 1.30720183321891e-07 0.999469907379679 0.000529961900137788 elongator acetyltransferase complex subunit 2 FUNCTION: Regulates the ligand-dependent activation of STAT3. {ECO:0000250}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;oral cavity;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;cerebellum;thymus; . 0.47073 0.14455 1.20517535 93.01722104 4260.20726 12.97448 ELP3 3.92611121629076e-07 0.987202103757385 0.0127975036314935 elongator acetyltransferase complex subunit 3 FUNCTION: Catalytic histone acetyltransferase subunit of the RNA polymerase II elongator complex, which is a component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. Involved in acetylation of alpha-tubulin (PubMed:19185337). May also have a methyltransferase activity. Involved in cell migration. Involved in neurogenesis. Regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha- tubulin acetylation (By similarity). {ECO:0000250|UniProtKB:Q9CZX0, ECO:0000269|PubMed:11714725, ECO:0000269|PubMed:11818576, ECO:0000269|PubMed:15902492, ECO:0000269|PubMed:16713582, ECO:0000269|PubMed:19185337}.; . TISSUE SPECIFICITY: Expressed in the cerebellum and spinal motor neurons. {ECO:0000269|PubMed:18996918}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;cerebellum cortex;pharynx;blood;lens;skeletal muscle;breast;lung;mesenchyma;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; testis - seminiferous tubule;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.17235 0.15918 -1.06726444 7.372021703 39.86292 1.17352 ELP4 0.0125582812097109 0.979923544108105 0.00751817468218417 elongator acetyltransferase complex subunit 4 FUNCTION: Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. {ECO:0000269|PubMed:11714725, ECO:0000269|PubMed:11818576, ECO:0000269|PubMed:16713582}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11889558}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;blood;lens;breast;bile duct;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;testis;pons;atrioventricular node;parietal lobe;cerebellum; 0.12042 0.11067 0.863528995 88.74144845 89.77807 2.03791 ELP5 6.47714386783623e-06 0.465706882730219 0.534286640125913 elongator acetyltransferase complex subunit 5 FUNCTION: Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. Involved in cell migration (By similarity). May be involved in TP53-mediated transcriptional regulation. {ECO:0000250, ECO:0000269|PubMed:16850183}.; . TISSUE SPECIFICITY: Ubiquitously expressed with high levels in heart, brain, liver, skeletal muscle and testis.; . . 0.24558 0.08824 -0.047654689 50.22410946 149.28012 2.66387 ELP6 0.00350789886566748 0.838053770219057 0.158438330915275 elongator acetyltransferase complex subunit 6 FUNCTION: Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. Involved in cell migration.; . . . . 0.05881 . 0.148941568 64.31941496 81.03032 1.90540 ELSPBP1 0.000181420081969443 0.702779959107818 0.297038620810213 epididymal sperm binding protein 1 FUNCTION: Binds to spermatozoa upon ejaculation and may play a role in sperm capacitation. Has phosphorylcholine-binding activity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in cauda epididymidal fluid and on sperm membrane (at protein level). {ECO:0000269|PubMed:11144225, ECO:0000269|PubMed:17307309}.; unclassifiable (Anatomical System);lung;epididymis;placenta;macula lutea;testis;fovea centralis; superior cervical ganglion;testis;trigeminal ganglion;skeletal muscle; 0.11014 0.14681 1.839182427 97.06298655 4867.60793 14.18004 EMB 6.39337047960594e-05 0.71740727228163 0.282528794013574 embigin FUNCTION: Plays a role in the outgrowth of motoneurons and in the formation of neuromuscular junctions. Following muscle denervation, promotes nerve terminal sprouting and the formation of additional acetylcholine receptor clusters at synaptic sites without affecting terminal Schwann cell number or morphology. Delays the retraction of terminal sprouts following re-innervation of denervated endplates. May play a role in targeting the monocarboxylate transporters SLC16A1 and SLC16A7 to the cell membrane (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;colon;skin;skeletal muscle;bone marrow;uterus;lung;nasopharynx;bone;thyroid;placenta;pituitary gland;testis;germinal center; dorsal root ganglion;superior cervical ganglion;white blood cells;atrioventricular node; 0.03594 0.13545 0.17280645 65.75843359 64.86866 1.65453 EMBP1 . . . embigin pseudogene 1 . . . . . . . . . . . EMC1 6.03747917977484e-14 0.93520673962781 0.0647932603721292 ER membrane protein complex subunit 1 . . . . . 0.49773 0.11263 . . 1605.4443 7.41586 EMC2 8.61007227016537e-05 0.929791462997725 0.0701224362795733 ER membrane protein complex subunit 2 . . . . . 0.30770 0.11065 -0.09720619 46.20193442 9.46573 0.34895 EMC3 0.801934562245368 0.19783255762596 0.000232880128672142 ER membrane protein complex subunit 3 . . . . . 0.15255 0.07902 0.103030231 61.2762444 21.92945 0.73762 EMC3-AS1 . . . EMC3 antisense RNA 1 . . . . . . . . . . . EMC4 0.912468200149828 0.0868948582706029 0.000636941579569038 ER membrane protein complex subunit 4 FUNCTION: May mediate anti-apoptotic activity.; . TISSUE SPECIFICITY: Isoform 1 is expressed in brain and heart. Isoform 2 is expressed in heart. {ECO:0000269|PubMed:18586032}.; . . 0.03499 0.12971 0.103030231 61.2762444 27.14266 0.87530 EMC6 0.491983958076831 0.431396987295716 0.076619054627453 ER membrane protein complex subunit 6 . . . . . 0.11447 0.12378 -0.009020804 52.8544468 3.50189 0.12731 EMC7 0.935651560043946 0.0640561129858116 0.000292326970242066 ER membrane protein complex subunit 7 . . . . . 0.40557 0.11865 0.435547893 77.45340882 32.41768 1.01217 EMC8 0.25900842753047 0.714092214626605 0.0268993578429253 ER membrane protein complex subunit 8 . . TISSUE SPECIFICITY: Expressed in liver, pancreas, heart, lung, kidney, brain, skeletal muscle, and placenta. Expression levels are highest in pancreas and moderate in heart, skeletal muscle, and placenta.; . . 0.14679 0.11262 -0.317668748 31.45789101 3.91042 0.14541 EMC9 0.00035382769828854 0.606584552242219 0.393061620059492 ER membrane protein complex subunit 9 . . . . . 0.19996 0.09543 0.283038099 71.26680821 78.56922 1.87008 EMC10 1.56498022796748e-07 0.224495180881637 0.77550466262034 ER membrane protein complex subunit 10 . . TISSUE SPECIFICITY: Present in serum (at protein level). Expressed in the pituitary gland; very low levels in other brain regions. {ECO:0000269|PubMed:19570817, ECO:0000269|PubMed:20680400}.; . . 0.13156 0.10621 -0.247889024 35.98726115 176.91631 2.89029 EMCN 1.65285025326724e-05 0.666582651371326 0.333400820126142 endomucin FUNCTION: Endothelial sialomucin, also called endomucin or mucin- like sialoglycoprotein, which interferes with the assembly of focal adhesion complexes and inhibits interaction between cells and the extracellular matrix.; . TISSUE SPECIFICITY: Expressed in heart, kidney and lung. {ECO:0000269|PubMed:11418125, ECO:0000269|PubMed:12485444}.; unclassifiable (Anatomical System);heart;colon;parathyroid;vein;skin;skeletal muscle;whole body;lung;nasopharynx;trabecular meshwork;bone;iris;pituitary gland;testis;kidney;brain;stomach;gall bladder; dorsal root ganglion;superior cervical ganglion;appendix;globus pallidus;atrioventricular node;trigeminal ganglion;fetal thyroid;skin; 0.31171 . 0.060756528 58.52795471 2740.85611 9.87049 EMD 0.84440846047199 0.152777227117484 0.00281431241052601 emerin FUNCTION: Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta- catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. Required for proper localization of non-farnesylated prelamin-A/C. {ECO:0000269|PubMed:15328537, ECO:0000269|PubMed:16680152, ECO:0000269|PubMed:16858403, ECO:0000269|PubMed:17785515, ECO:0000269|PubMed:19323649}.; DISEASE: Emery-Dreifuss muscular dystrophy 1, X-linked (EDMD1) [MIM:310300]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:10323252, ECO:0000269|PubMed:11587540}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Skeletal muscle, heart, colon, testis, ovary and pancreas.; . . 0.06261 0.53733 -0.05129383 49.75819769 19.04046 0.65783 EME1 7.06666940107235e-11 0.0685995008069808 0.931400499122353 essential meiotic structure-specific endonuclease 1 FUNCTION: Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'- flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks. {ECO:0000269|PubMed:12686547, ECO:0000269|PubMed:12721304, ECO:0000269|PubMed:14617801, ECO:0000269|PubMed:17289582}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.07791 0.09742 1.003094668 90.77022883 6068.55092 16.26682 EME2 9.50138363079845e-14 0.00275915920701435 0.997240840792891 essential meiotic structure-specific endonuclease subunit 2 FUNCTION: Interacts with MUS81 to form a DNA structure-specific endonuclease which cleaves substrates such as 3'-flap structures. {ECO:0000269|PubMed:17289582}.; . . ovary;developmental;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;gum;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;tongue;islets of Langerhans;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; . 0.08789 0.09565 . . 277.72803 3.57028 EMG1 0.0106038960648901 0.945929626593384 0.0434664773417259 EMG1 N1-specific pseudouridine methyltransferase FUNCTION: S-adenosyl-L-methionine-dependent pseudouridine N(1)- methyltransferase that methylates pseudouridine at position 1248 (Psi1248) in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Is not able to methylate uridine at this position (PubMed:20047967). Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 during the formation of pre-ribosomes (By similarity). {ECO:0000250|UniProtKB:Q06287, ECO:0000269|PubMed:20047967}.; DISEASE: Bowen-Conradi syndrome (BWCNS) [MIM:211180]: A combination of malformations characterized in newborns by low birth weight, microcephaly, mild joint restriction, a prominent nose, micrognathia, fifth finger clinodactyly, and 'rocker-bottom' feet. The syndrome is transmitted as an autosomal recessive trait. The prognosis is poor, with all infants dying within the first few months of life. {ECO:0000269|PubMed:19463982}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;pharynx;blood;lens;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion; 0.33153 0.15110 . . 134.41471 2.52109 EMID1 0.0397077266512435 0.953633155806475 0.00665911754228154 EMI domain containing 1 . . . unclassifiable (Anatomical System);cartilage;heart;colon;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;breast;prostate;optic nerve;lung;endometrium;placenta;thyroid;macula lutea;spleen;kidney;brain;stomach; thalamus;superior cervical ganglion;kidney;trigeminal ganglion;cerebellum; 0.28625 0.07814 0.885576705 89.14248644 2331.25441 8.94428 EMILIN1 0.00521656081419512 0.993659209776448 0.0011242294093567 elastin microfibril interfacer 1 FUNCTION: May be responsible for anchoring smooth muscle cells to elastic fibers, and may be involved not only in the formation of the elastic fiber, but also in the processes that regulate vessel assembly. Has cell adhesive capacity.; . TISSUE SPECIFICITY: Distributed in tissues where resilience and elastic recoil are prominent. Highest levels in the adult small intestine, aorta, lung, uterus, and appendix and in the fetal spleen, kidney, lung, and heart; intermediate expression was detected in adult liver, ovary, colon, stomach, lymph node and spleen; adult heart, bladder, prostate, adrenal gland, mammary gland, placenta and kidney showed low expression whereas a series of other adult tissues, including skeletal muscle and different regions of adult brain show no expression. {ECO:0000269|PubMed:11278945}.; . . 0.30295 0.14760 -0.108334733 45.57088936 261.91178 3.47286 EMILIN2 1.59772922427617e-09 0.367748617562554 0.632251380839717 elastin microfibril interfacer 2 FUNCTION: May be responsible for anchoring smooth muscle cells to elastic fibers, and may be involved not only in the formation of the elastic fiber, but also in the processes that regulate vessel assembly. Has cell adhesive capacity.; . TISSUE SPECIFICITY: Highest levels are present in fetal heart and adult lung. Intermediate levels in peripheral leukocytes, placenta, and spinal cord and low expression in fetal brain, spleen, thymus, and lung and in adult heart, aorta, testis, bone marrow, small intestine, thymus, lymph node, and appendix.; myocardium;smooth muscle;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;larynx;thyroid;brain;unclassifiable (Anatomical System);heart;cartilage;pineal body;blood;lens;lung;placenta;visual apparatus;macula lutea;head and neck;kidney; . 0.26506 0.10129 -0.497908112 21.86246756 1036.3099 6.18119 EMILIN3 0.00139809720973059 0.964387676810098 0.0342142259801715 elastin microfibril interfacer 3 . . . ovary;rectum;colon;parathyroid;fovea centralis;choroid;skin;retina;optic nerve;whole body;synovium;bone;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;lung;epididymis;placenta;visual apparatus;macula lutea;liver;mammary gland;stomach; . 0.15060 0.09871 -0.589727438 18.25902335 2353.45664 8.99155 EML1 0.999446460294898 0.0005535397009042 4.19745640744173e-12 echinoderm microtubule associated protein like 1 FUNCTION: Modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. Required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. Does not affect neuron migration per se (By similarity). {ECO:0000250}.; DISEASE: Note=Mutations in this gene are associated with atypical heterotopia, epilepsy and mental retardation. Patients present giant bilateral periventricular and ribbon-like subcortical heterotopia with polymicrogyria and agenesis of the corpus callosum.; TISSUE SPECIFICITY: Ubiquitous; expressed in most tissues with the exception of thymus and peripheral blood lymphocytes. {ECO:0000269|PubMed:10521658}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;bone;testis;brain;ciliary body;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;caudate nucleus;trigeminal ganglion; 0.29081 0.16371 -0.420619508 25.72540694 2161.08861 8.55162 EML2 7.57699496433696e-10 0.671944659499472 0.328055339742829 echinoderm microtubule associated protein like 2 FUNCTION: Tubulin binding protein that inhibits microtubule nucleation and growth, resulting in shorter microtubules. {ECO:0000269|PubMed:11694528}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10521658}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;medulla oblongata;placenta;trigeminal ganglion;cingulate cortex; 0.17207 0.11401 0.224175308 68.48903043 3227.53207 10.82078 EML2-AS1 . . . EML2 antisense RNA 1 . . . . . . . . . . . EML3 0.394340909405705 0.605658414602527 6.75991767913931e-07 echinoderm microtubule associated protein like 3 FUNCTION: May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. {ECO:0000250}.; . . ovary;colon;fovea centralis;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;olfactory bulb;trigeminal ganglion;fetal thyroid; 0.25723 0.09936 -0.843147538 11.2762444 758.07118 5.45547 EML4 0.391138665343134 0.608861306291527 2.83653391180616e-08 echinoderm microtubule associated protein like 4 FUNCTION: May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. {ECO:0000250}.; . . lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.20914 0.12830 -1.346642726 4.62962963 2437.31101 9.17493 EML5 0.158418534732481 0.841581465264346 3.17284590353364e-12 echinoderm microtubule associated protein like 5 FUNCTION: May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;sympathetic chain;parathyroid;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;cerebral cortex;placenta;macula lutea;visual apparatus;kidney;mammary gland;brain;thymus; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.28613 0.11219 -1.433039328 4.010379807 2332.61573 8.94776 EML6 0.44303244895019 0.455367431512181 0.101600119537629 echinoderm microtubule associated protein like 6 FUNCTION: May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. {ECO:0000250}.; . . unclassifiable (Anatomical System);optic nerve;lung;islets of Langerhans;macula lutea;testis;fovea centralis;choroid;germinal center;lens;brain;peripheral nerve;retina; ciliary ganglion; . . -0.613589782 17.49823071 281.49654 3.59206 EMP1 0.411003665812915 0.55235010848728 0.0366462256998054 epithelial membrane protein 1 . . . lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;ciliary body;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;synovium;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;oral cavity;pancreas;lung;pia mater;mesenchyma;placenta;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;tongue;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07248 0.15375 0.391453969 75.87284737 30.34305 0.96727 EMP2 5.89781732945459e-05 0.271748243059306 0.728192778767399 epithelial membrane protein 2 FUNCTION: Functions as a key regulator of cell membrane composition by regulating proteins surface expression. Also, plays a role in regulation of processes including cell migration, cell proliferation, cell contraction and cell adhesion. Negatively regulates caveolae formation by reducing CAV1 expression and CAV1 amount by increasing lysosomal degradation (PubMed:24814193). Facilitates surface trafficking and formation of lipid rafts bearing GPI-anchor proteins (By similarity). Regulates surface expression of MHC1 and ICAM1 proteins increasing susceptibility to T cell mediated cytotoxicity (By similarity). Regulates the plasma membrane expression of the integrin heterodimers ITGA6-ITGB1, ITGA5-ITGB3 and ITGA5-ITGB1 resulting in modulation of cell-matrix adhesion (PubMed:16216233). Also regulates many processes through PTK2. Regulates blood vessel endothelial cell migration and angiogenesis by regulating VEGF protein expression through PTK2 activation (PubMed:23439602). Regulates cell migration and cell contraction through PTK2 and SRC activation (PubMed:21637765, PubMed:22728127). Regulates focal adhesion density, F-actin conformation and cell adhesion capacity through interaction with PTK2 (PubMed:19494199). Positively regulates cell proliferation (PubMed:24814193). Plays a role during cell death and cell blebbing (PubMed:12107182). Promotes angiogenesis and vasculogenesis through induction of VEGFA via a HIF1A-dependent pathway (PubMed:23334331). Also plays a role in embryo implantation by regulating surface trafficking of integrin heterodimer ITGA5-ITGB3 (PubMed:16487956). May play a role in glomerular filtration (By similarity). {ECO:0000250|UniProtKB:F1QIK8, ECO:0000250|UniProtKB:O88662, ECO:0000269|PubMed:12107182, ECO:0000269|PubMed:16216233, ECO:0000269|PubMed:16487956, ECO:0000269|PubMed:19494199, ECO:0000269|PubMed:21637765, ECO:0000269|PubMed:22728127, ECO:0000269|PubMed:23334331, ECO:0000269|PubMed:23439602, ECO:0000269|PubMed:24814193}.; DISEASE: Nephrotic syndrome 10 (NPHS10) [MIM:615861]: A form of nephrotic syndrome, a renal disease clinically characterized by focal segmental glomerulosclerosis, progressive renal failure, severe proteinuria, hypoalbuminemia, hyperlipidemia and edema. NPHS10 is a steroid-sensitive form characterized by onset in childhood and remission without end-stage kidney disease. {ECO:0000269|PubMed:24814193}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in ciliary body epithelia, sclera, cornea, and retinal pigment epithelium (at protein level) (PubMed:12710941). {ECO:0000269|PubMed:12710941}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.08675 . -0.359940251 28.93371078 8.21106 0.30276 EMP3 0.000573648342962621 0.710622247608108 0.288804104048929 epithelial membrane protein 3 FUNCTION: Probably involved in cell proliferation and cell-cell interactions.; . . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;mammary gland;stomach;thymus; lung;heart;white blood cells;whole blood; 0.28856 0.15440 0.103030231 61.2762444 133.39566 2.50920 EMSY . . . EMSY, BRCA2 interacting transcriptional repressor FUNCTION: Regulator which is able to repress transcription, possibly via its interaction with a multiprotein chromatin remodeling complex that modifies the chromatin. Its interaction with BRCA2 suggests that it may play a central role in the DNA repair function of BRCA2. As part of a histone H3-specific methyltransferase complex may mediate ligand-dependent transcriptional activation by nuclear hormone receptors. {ECO:0000269|PubMed:14651845, ECO:0000269|PubMed:19131338}.; . . . . 0.59367 0.11683 -1.947491103 1.875442321 . . EMWX . . . episodic muscle weakness, X-linked . . . . . . . . . . . EMX1 0.710215196701832 0.274718292512403 0.0150665107857647 empty spiracles homeobox 1 FUNCTION: Transcription factor, which in cooperation with EMX2, acts to generate the boundary between the roof and archipallium in the developing brain. May function in combinations with OTX1/2 to specify cell fates in the developing central nervous system.; . TISSUE SPECIFICITY: Cerebral cortex.; unclassifiable (Anatomical System);hippocampus;colon;kidney;brain;mammary gland; superior cervical ganglion;prefrontal cortex;kidney;skeletal muscle; 0.33836 0.16654 . . 5.42472 0.20134 EMX2 0.941755033342245 0.0580174210384328 0.000227545619322529 empty spiracles homeobox 2 FUNCTION: Transcription factor, which in cooperation with EMX2, acts to generate the boundary between the roof and archipallium in the developing brain. May function in combinations with OTX1/2 to specify cell fates in the developing central nervous system.; . TISSUE SPECIFICITY: Cerebral cortex.; . . 0.93765 0.31462 -0.09720619 46.20193442 14.66972 0.52877 EMX2OS . . . EMX2 opposite strand/antisense RNA . . . . . . . . . . . EN1 0.751931859883325 0.238255669085437 0.00981247103123836 engrailed homeobox 1 . . . whole body;bone;placenta; superior cervical ganglion; 0.60781 0.26527 . . 13.35248 0.48584 EN2 0.433107378953652 0.535388331869819 0.0315042891765291 engrailed homeobox 2 . DISEASE: Note=Genetic variations in EN2 may be associated with susceptibility to autism.; . endometrium;colon;brain;mammary gland; superior cervical ganglion;cerebellum peduncles;cerebellum; 0.19517 0.41480 . . 1467.46629 7.13833 ENAH 0.995700037438515 0.00429994736305026 1.51984346768424e-08 enabled homolog (Drosophila) FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation (By similarity). {ECO:0000250, ECO:0000269|PubMed:11696321, ECO:0000269|PubMed:18158903}.; . TISSUE SPECIFICITY: Expressed in myoepithelia of parotid, breast, bronchial glands and sweat glands. Expressed in colon-rectum muscolaris mucosae epithelium, pancreas acinar ductal epithelium, endometrium epithelium, prostate fibromuscolar stroma and placenta vascular media. Overexpressed in a majority of breast cancer cell lines and primary breast tumor lesions. {ECO:0000269|PubMed:15027125}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;pharynx;blood;breast;lung;adrenal gland;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; superior cervical ganglion;testis;trigeminal ganglion; 0.97655 . -0.624497208 17.16206653 91.725 2.06034 ENAM 5.67050431084391e-07 0.964727512754342 0.0352719201952274 enamelin FUNCTION: Involved in the mineralization and structural organization of enamel. Involved in the extension of enamel during the secretory stage of dental enamel formation. {ECO:0000250|UniProtKB:O97939}.; DISEASE: Amelogenesis imperfecta 1B (AI1B) [MIM:104500]: An autosomal dominant defect of enamel formation. Clinical manifestations may be variable. Some cases present with generalized enamel hypoplasia resulting in small, smooth, yellow and widely spaced teeth (smooth hypoplastic AI). Others show horizontal rows of pits, grooves or a hypoplastic area in the enamel (local hypoplastic AI). {ECO:0000269|PubMed:11487571, ECO:0000269|PubMed:11978766, ECO:0000269|PubMed:20439930, ECO:0000269|PubMed:25789606}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Amelogenesis imperfecta 1C (AI1C) [MIM:204650]: An autosomal recessive defect of dental enamel formation. Teeth show local hypoplastic and unmineralized enamel, and a yellow-brown discoloration. Enamel defects can be associated with facial and oral features including vertical dysgnathia and anterior openbite malocclusion. {ECO:0000269|PubMed:14684688, ECO:0000269|PubMed:20439930}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in tooth particularly in odontoblast, ameloblast and cementoblast. {ECO:0000269|PubMed:11487571}.; . . 0.09364 0.11786 -0.079012906 47.25760793 1343.42987 6.88072 ENC1 0.879896897082265 0.119806196951807 0.000296905965928298 ectodermal-neural cortex 1 FUNCTION: Actin-binding protein involved in the regulation of neuronal process formation and in differentiation of neural crest cells. Down-regulates transcription factor NF2L2/NRF2 by decreasing the rate of protein synthesis and not via a ubiquitin- mediated proteasomal degradation mechanism. {ECO:0000269|PubMed:19424503}.; . TISSUE SPECIFICITY: Detected in fetal brain tissue, moderate expression in fetal heart, lung and kidney. Highly expressed in adult brain, particularly high in the hippocampus and amygdala, and spinal chord. Detectable in adult pancreas. May be down- regulated in neuroblastoma tumors.; smooth muscle;ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;pineal gland;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;muscle;adrenal cortex;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; whole brain;amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.82409 0.11108 -0.648365105 16.35999056 9.15273 0.33382 ENDOD1 1.42162447825975e-06 0.222248280160735 0.777750298214787 endonuclease domain containing 1 FUNCTION: May act as a DNase and a RNase. {ECO:0000305}.; . . sympathetic chain;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;urinary;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;olfactory bulb;hypothalamus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.23376 0.10380 0.995816767 90.62278839 2505.4149 9.32819 ENDOG 0.00624335330071762 0.503907606066843 0.489849040632439 endonuclease G FUNCTION: Cleaves DNA at double-stranded (DG)n.(DC)n and at single-stranded (DC)n tracts. In addition to deoxyribonuclease activities, also has ribonuclease (RNase) and RNase H activities. Capable of generating the RNA primers required by DNA polymerase gamma to initiate replication of mitochondrial DNA (By similarity). {ECO:0000250}.; . . . . 0.21004 0.20079 . . 85.13297 1.96679 ENDOU 6.22319085378802e-12 0.0167486080304933 0.983251391963283 endonuclease, poly(U) specific FUNCTION: Endoribonuclease that cleaves single-stranded RNAs at uridylates and releases products that have 2'-3'-cyclic phosphate termini. {ECO:0000269|PubMed:18936097}.; . TISSUE SPECIFICITY: Placental-specific, but also associated with various malignant neoplasms.; uterus;lung;frontal lobe;heart;placenta;spinal cord;adrenal cortex;testis;blood;kidney;brain;skin; tongue;placenta; . . -0.179930907 40.35739561 207.83067 3.11321 ENDOV 2.6283345911486e-06 0.509256446704064 0.490740924961345 endonuclease V FUNCTION: Endoribonuclease that specifically cleaves inosine- containing RNAs: cleaves RNA at the second phosphodiester bond 3' to inosine. Has strong preference for single-stranded RNAs (ssRNAs) toward double-stranded RNAs (dsRNAs). Cleaves mRNAs and tRNAs containing inosine. Also able to cleave structure-specific dsRNA substrates containing the specific sites 5'-IIUI-3' and 5'- UIUU-3'. Inosine is present in a number of RNAs following editing; the function of inosine-specific endoribonuclease is still unclear: it could either play a regulatory role in edited RNAs, or be involved in antiviral response by removing the hyperedited long viral dsRNA genome that has undergone A-to-I editing. Binds branched DNA structures. {ECO:0000269|PubMed:23139746, ECO:0000269|PubMed:23912683, ECO:0000269|PubMed:23912718}.; . . unclassifiable (Anatomical System);islets of Langerhans;skin;uterus;pancreas;lung;frontal lobe;placenta;bone;visual apparatus;liver;testis;mammary gland; . . . -0.023789244 52.09365416 1106.26933 6.35610 ENG 0.989617028317184 0.0103828404070345 1.31275781729863e-07 endoglin FUNCTION: Major glycoprotein of vascular endothelium. Involved in the regulation of angiogenesis. May play a critical role in the binding of endothelial cells to integrins and/or other RGD receptors. Acts as TGF-beta coreceptor and is involved in the TGF- beta/BMP signaling cascade. Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGF-beta1 signaling through SMAD3. {ECO:0000269|PubMed:21737454, ECO:0000269|PubMed:23300529}.; . TISSUE SPECIFICITY: Endoglin is restricted to endothelial cells in all tissues except bone marrow.; lymphoreticular;myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;synovium;larynx;bone;thyroid;iris;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;urinary;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; heart;placenta;testis;trigeminal ganglion; 0.15044 0.76645 -0.394936437 27.02878037 285.23723 3.61548 ENGASE 8.06055418663565e-21 0.00094656497022446 0.999053435029776 endo-beta-N-acetylglucosaminidase FUNCTION: Endoglycosidase that releases N-glycans from glycoproteins by cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose core. Involved in the processing of free oligosaccharides in the cytosol. {ECO:0000269|PubMed:12114544}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in thymus and spleen. {ECO:0000269|PubMed:12114544}.; ovary;sympathetic chain;adrenal medulla;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;optic nerve;endometrium;oesophagus;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;pancreas;lung;placenta;macula lutea;liver;hypopharynx;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; . . -0.632009432 16.78461901 2375.52075 9.04291 ENHO 0.113449545869116 0.600898218719171 0.285652235411713 energy homeostasis associated FUNCTION: Involved in the regulation of glucose homeostasis and lipid metabolism. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in liver and brain. {ECO:0000269|PubMed:19041763}.; unclassifiable (Anatomical System);optic nerve;whole body;heart;hypothalamus;liver;spleen;brain; . 0.79457 . 0.079165051 59.43029016 1.86131 0.05857 ENKD1 2.15383278184853e-05 0.4838173179187 0.516161143753482 enkurin domain containing 1 . . . . . 0.25697 0.09867 0.729426781 86.17008728 239.88217 3.34724 ENKUR 9.60808494268811e-06 0.333823752727977 0.66616663918708 enkurin, TRPC channel interacting protein FUNCTION: Adapter that functions to localize a calcium-sensitive signal transduction machinery in sperm to a calcium-permeable ion channel. {ECO:0000250}.; . . unclassifiable (Anatomical System);optic nerve;lung;endometrium;nasopharynx;macula lutea;testis;fovea centralis;choroid;lens;brain;retina; . 0.17201 . 0.77170517 87.00754895 90.41146 2.04573 ENO1 0.0103734127326719 0.979738802047778 0.00988778521955011 enolase 1, (alpha) FUNCTION: Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production.; . TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.; ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;gum;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; whole brain;lung;smooth muscle;heart;liver;tumor; 0.35486 0.12263 -0.181750739 40.15687662 29.45013 0.94209 ENO1-AS1 . . . ENO1 antisense RNA 1 . . . . . . . . . . . ENO1-IT1 . . . ENO1 intronic transcript 1 . . . . . . . . . . . ENO1P1 . . . enolase 1, (alpha) pseudogene 1 . . . . . 0.06432 . . . . . ENO1P2 . . . enolase 1, (alpha) pseudogene 2 . . . . . . . . . . . ENO1P3 . . . enolase 1, (alpha) pseudogene 3 . . . . . . . . . . . ENO1P4 . . . enolase 1, (alpha) pseudogene 4 . . . . . . . . . . . ENO2 0.0185777100017329 0.977166773509804 0.00425551648846334 enolase 2 (gamma, neuronal) FUNCTION: Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.; ovary;sympathetic chain;substantia nigra;skin;bone marrow;retina;optic nerve;frontal lobe;endometrium;thyroid;brain;amygdala;heart;cartilage;pineal body;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;mesenchyma;adrenal gland;placenta;hippocampus;head and neck;kidney;cerebellum; whole brain;amygdala;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.85446 0.85833 -0.405853867 26.23260203 15.72045 0.55973 ENO3 6.90899000171878e-11 0.0677193085189577 0.932280691411952 enolase 3 (beta, muscle) FUNCTION: Appears to have a function in striated muscle development and regeneration.; DISEASE: Glycogen storage disease 13 (GSD13) [MIM:612932]: A metabolic disorder that results in exercise-induced myalgias, generalized muscle weakness and fatigability. It is characterized by increased serum creatine kinase and decreased enolase 3 activity. Dramatically reduced protein levels with focal sarcoplasmic accumulation of glycogen-beta particles are detected on ultrastructural analysis. {ECO:0000269|PubMed:11506403}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.; myocardium;ovary;salivary gland;developmental;intestine;colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;bone;thyroid;testis;amniotic fluid;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;cerebellum cortex;tongue;muscle;pharynx;blood;lens;skeletal muscle;greater omentum;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;stomach; heart;tongue;thyroid;liver;skeletal muscle; 0.88864 0.37745 -0.488577883 22.64685067 3157.89688 10.70432 ENO4 . . . enolase family member 4 . . . unclassifiable (Anatomical System);heart;ovary;parathyroid;skin;uterus;prostate;lung;endometrium;placenta;testis;germinal center;brain;stomach; . . . . . 139.77329 2.57780 ENOPH1 0.00175784115061139 0.896387389565341 0.101854769284047 enolase-phosphatase 1 FUNCTION: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK- MTPene). {ECO:0000255|HAMAP-Rule:MF_03117, ECO:0000269|PubMed:15843022}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; amygdala;whole brain;superior cervical ganglion;thalamus;medulla oblongata;occipital lobe;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.05836 . -0.141298762 42.87567823 11.59579 0.41930 ENOSF1 1.26226997891008e-10 0.176876518056968 0.823123481816806 enolase superfamily member 1 FUNCTION: Plays a role in the catabolism of L-fucose, a sugar that is part of the carbohydrates that are attached to cellular glycoproteins. Catalyzes the dehydration of L-fuconate to 2-keto- 3-deoxy-L-fuconate by the abstraction of the 2-proton to generate an enediolate intermediate that is stabilized by the magnesium ion (PubMed:24697329). {ECO:0000269|PubMed:24697329}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.31397 0.23467 0.576916344 82.25406936 1103.22771 6.35035 ENOX1 0.0364014174663741 0.963534486706737 6.40958268887357e-05 ecto-NOX disulfide-thiol exchanger 1 FUNCTION: Probably acts as a terminal oxidase of plasma electron transport from cytosolic NAD(P)H via hydroquinones to acceptors at the cell surface. Hydroquinone oxidase activity alternates with a protein disulfide-thiol interchange/oxidoreductase activity which may control physical membrane displacements associated with vesicle budding or cell enlargement. The activities oscillate with a period length of 24 minutes and play a role in control of the ultradian cellular biological clock. {ECO:0000269|PubMed:11360993, ECO:0000269|PubMed:12565167, ECO:0000269|PubMed:17027975, ECO:0000269|PubMed:19055324}.; . TISSUE SPECIFICITY: Expressed in lymphocyte cells, breast and breast cancer (at protein level). Found in the sera of cancer patients with a wide variety of cancers including breast, prostate, lung and ovarian cancers, leukemias, and lymphomas. Found also in the serum of healthy volunteers or patients with disorders other than cancer. Probably shed into serum by cancer cells.; unclassifiable (Anatomical System);lymph node;ovary;heart;parathyroid;blood;skin;uterus;prostate;pancreas;whole body;lung;placenta;visual apparatus;hippocampus;liver;testis;head and neck;spleen;kidney;brain;aorta;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.47836 0.11392 -0.44448505 24.46331682 355.37885 3.98952 ENOX1-AS1 . . . ENOX1 antisense RNA 1 . . . . . . . . . . . ENOX1-AS2 . . . ENOX1 antisense RNA 2 . . . . . . . . . . . ENOX2 0.00314555069570329 0.985593488156742 0.0112609611475543 ecto-NOX disulfide-thiol exchanger 2 FUNCTION: May be involved in cell growth. Probably acts as a terminal oxidase of plasma electron transport from cytosolic NAD(P)H via hydroquinones to acceptors at the cell surface. Hydroquinone oxidase activity alternates with a protein disulfide- thiol interchange/oxidoreductase activity which may control physical membrane displacements associated with vesicle budding or cell enlargement. The activities oscillate with a period length of 22 minutes and play a role in control of the ultradian cellular biological clock. {ECO:0000269|PubMed:12356293, ECO:0000269|PubMed:9932650}.; . TISSUE SPECIFICITY: Found in the sera of cancer patients with a wide variety of cancers including breast, prostate, lung and ovarian cancers, leukemias, and lymphomas. Not found in the serum of healthy volunteers or patients with disorders other than cancer. Probably shed into serum by cancer cells. Found on the cell borders of renal, kidney and ovarian carcinomas but not on the borders of surrounding non-cancerous stromal cells.; smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;whole body;endometrium;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;adrenal cortex;pancreas;lung;adrenal gland;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;spinal cord;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.12779 0.10711 -0.426079032 25.36565228 48.90233 1.36505 ENPEP 3.57621192360691e-19 0.0169444161266028 0.983055583873397 glutamyl aminopeptidase FUNCTION: Appears to have a role in the catabolic pathway of the renin-angiotensin system. Probably plays a role in regulating growth and differentiation of early B-lineage cells.; . TISSUE SPECIFICITY: Expressed by epithelial cells of the proximal tubule cells and the glomerulus of the nephron. Also found in a variety of other tissues.; unclassifiable (Anatomical System);heart;ovary;parathyroid;skin;skeletal muscle;uterus;pancreas;lung;endometrium;placenta;liver;testis;kidney;brain;stomach; superior cervical ganglion;kidney;trigeminal ganglion; 0.21927 0.47886 0.385781814 75.678226 422.73046 4.29372 ENPP1 2.30987361236777e-05 0.999938899224151 3.80020397247421e-05 ectonucleotide pyrophosphatase/phosphodiesterase 1 FUNCTION: By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity and function. {ECO:0000269|PubMed:10615944, ECO:0000269|PubMed:8001561}.; DISEASE: Ossification of the posterior longitudinal ligament of the spine (OPLL) [MIM:602475]: A calcification of the posterior longitudinal ligament of the spinal column, usually at the level of the cervical spine. Patients with OPLL frequently present with a severe myelopathy that can lead to tetraparesis. {ECO:0000269|PubMed:10453738}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Arterial calcification of infancy, generalized, 1 (GACI1) [MIM:208000]: A severe autosomal recessive disorder characterized by calcification of the internal elastic lamina of muscular arteries and stenosis due to myointimal proliferation. The disorder is often fatal within the first 6 months of life because of myocardial ischemia resulting in refractory heart failure. {ECO:0000269|PubMed:12881724, ECO:0000269|PubMed:15605415, ECO:0000269|PubMed:15940697, ECO:0000269|PubMed:22209248}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:16186408}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Hypophosphatemic rickets, autosomal recessive, 2 (ARHR2) [MIM:613312]: A hereditary form of hypophosphatemic rickets, a disorder of proximal renal tubule function that causes phosphate loss, hypophosphatemia and skeletal deformities, including rickets and osteomalacia unresponsive to vitamin D. Symptoms are bone pain, fractures and growth abnormalities. {ECO:0000269|PubMed:20137772, ECO:0000269|PubMed:20137773}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cole disease (COLED) [MIM:615522]: A rare autosomal dominant genodermatosis characterized by punctate keratoderma associated with irregularly shaped hypopigmented macules, which are typically found over the arms and legs but not the trunk or acral regions. Skin biopsies of palmoplantar lesions show hyperorthokeratosis, hypergranulosis, and acanthosis. Hypopigmented areas of skin, however, reveal a reduction in melanin content in keratinocytes but not in melanocytes, as well as hyperkeratosis and a normal number of melanocytes. Ultrastructurally, melanocytes show a disproportionately large number of melanosomes in the cytoplasm and dendrites, whereas keratinocytes show a paucity of these organelles, suggestive of impaired melanosome transfer. Some patients also exhibit calcinosis cutis or calcific tendinopathy. {ECO:0000269|PubMed:24075184}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in plasma cells and also in a number of non-lymphoid tissues, including the distal convoluted tubule of the kidney, chondrocytes and epididymis. {ECO:0000269|PubMed:9344668}.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;blood;skin;skeletal muscle;breast;uterus;whole body;lung;bone;placenta;liver;testis;spleen;kidney;brain; dorsal root ganglion;thyroid;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.54099 0.47148 -0.396754488 26.97570182 2168.46072 8.57235 ENPP2 0.00682819825531218 0.993170522893436 1.27885125214713e-06 ectonucleotide pyrophosphatase/phosphodiesterase 2 FUNCTION: Hydrolyzes lysophospholipids to produce lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine. Also can act on sphingosylphosphphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP. Involved in several motility- related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. May have a role in induction of parturition. Possible involvement in cell proliferation and adipose tissue development. Tumor cell motility-stimulating factor. {ECO:0000269|PubMed:11559573, ECO:0000269|PubMed:1733949, ECO:0000269|PubMed:21240271}.; . TISSUE SPECIFICITY: Predominantly expressed in brain, placenta, ovary, and small intestine. Expressed in a number of carcinomas such as hepatocellular and prostate carcinoma, neuroblastoma and non-small-cell lung cancer. Expressed in body fluids such as plasma, cerebral spinal fluid (CSF), saliva, follicular and amniotic fluids. Not detected in leukocytes. Isoform 1 is more highly expressed in peripheral tissues than in the central nervous system (CNS). Adipocytes only express isoform 1. Isoform 3 is more highly expressed in the brain than in peripheral tissues. {ECO:0000269|PubMed:18175805, ECO:0000269|PubMed:8579579, ECO:0000269|PubMed:8586446}.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;tonsil;amygdala;heart;cartilage;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; amygdala;whole brain;thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;hypothalamus;spinal cord;caudate nucleus;pons;uterus corpus;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.46033 0.19601 0.161677043 64.96225525 485.27426 4.53673 ENPP3 6.43746414984857e-17 0.174729562034544 0.825270437965456 ectonucleotide pyrophosphatase/phosphodiesterase 3 FUNCTION: Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in bile ducts, prostate, uterus and colon. Exclusively expressed on basophils, mast cells and their progenitors. {ECO:0000269|PubMed:15072822, ECO:0000269|PubMed:9344668}.; unclassifiable (Anatomical System);cartilage;ovary;heart;islets of Langerhans;colon;parathyroid;blood;skin;skeletal muscle;breast;uterus;prostate;whole body;lung;endometrium;placenta;bone;liver;testis;spleen;kidney;brain;stomach; dorsal root ganglion;thyroid;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.13014 0.42297 0.385781814 75.678226 943.91985 5.95230 ENPP4 0.414683930724528 0.577167970245 0.00814809903047188 ectonucleotide pyrophosphatase/phosphodiesterase 4 (putative) FUNCTION: Hydrolyzes extracellular Ap3A into AMP and ADP, and Ap4A into AMP and ATP. Ap3A and Ap4A are diadenosine polyphosphates thought to induce proliferation of vascular smooth muscle cells. Acts as a procoagulant, mediating platelet aggregation at the site of nascent thrombus via release of ADP from Ap3A and activation of ADP receptors. {ECO:0000269|PubMed:22995898, ECO:0000269|PubMed:24338010}.; . TISSUE SPECIFICITY: Expressed on the surface of vascular endothelia. {ECO:0000269|PubMed:22995898}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;hypothalamus;spinal cord;adrenal cortex;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;hippocampus;liver;kidney;stomach;aorta;thymus; amygdala;superior cervical ganglion;occipital lobe;caudate nucleus;parietal lobe; 0.06637 0.10147 0.373041938 75.29488087 3077.64338 10.54535 ENPP5 1.91660634387746e-05 0.4600736700562 0.539907163880361 ectonucleotide pyrophosphatase/phosphodiesterase 5 (putative) FUNCTION: May play a role in neuronal cell communication. Lacks nucleotide pyrophosphatase and lysopholipase D activity (By similarity). {ECO:0000250|UniProtKB:P84039}.; . . unclassifiable (Anatomical System);cartilage;heart;colon;parathyroid;fovea centralis;skin;skeletal muscle;pancreas;prostate;optic nerve;lung;endometrium;macula lutea;hippocampus;liver;pituitary gland;testis;kidney;brain;mammary gland;aorta; . 0.09518 0.08781 0.176444282 66.07100731 6521.86997 16.95828 ENPP6 6.11082610084163e-07 0.438795273740325 0.561204115177065 ectonucleotide pyrophosphatase/phosphodiesterase 6 FUNCTION: Choline-specific glycerophosphodiester phosphodiesterase. The preferred substrate may be lysosphingomyelin (By similarity). Hydrolyzes lysophosphatidylcholine (LPC) to form monoacylglycerol and phosphorylcholine but not lysophosphatidic acid, showing it has a lysophospholipase C activity. Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty acids. Also hydrolyzes glycerophosphorylcholine and sphingosylphosphorylcholine efficiently. Hydrolyzes the classical substrate for phospholipase C, p-nitrophenyl phosphorylcholine in vitro, while it does not hydrolyze the classical nucleotide phosphodiesterase substrate, p-nitrophenyl thymidine 5'- monophosphate. Does not hydrolyze diacyl phospholipids such as phosphatidylethanolamine, phosphatidylinositol, phosphatidylserine, phosphatidylglycerol and phosphatidic acid. {ECO:0000250, ECO:0000269|PubMed:15788404}.; . TISSUE SPECIFICITY: Predominantly expressed in kidney and brain. In the kidney, expressed specifically in the proximal tubules and thin descending limbs of Henle (at protein level). {ECO:0000269|PubMed:15788404}.; unclassifiable (Anatomical System);heart;ovary;parathyroid;breast;prostate;lung;cerebral cortex;placenta;bone;hippocampus;testis;head and neck;kidney;brain;stomach; . 0.14539 . -0.352661697 29.48808681 79.1324 1.87829 ENPP7 2.20917341359956e-10 0.0191736626605458 0.980826337118537 ectonucleotide pyrophosphatase/phosphodiesterase 7 FUNCTION: Converts sphingomyelin to ceramide. Also has phospholipase C activity toward palmitoyl lyso-phosphocholine. Does not appear to have nucleotide pyrophosphatase activity. {ECO:0000269|PubMed:12885774}.; . TISSUE SPECIFICITY: Detected in the colon (at protein level). Expressed in the duodenum, jejunum and liver and at low levels in the ileum. Expression was very low in the esophagus, stomach and colon. {ECO:0000269|PubMed:12671034, ECO:0000269|PubMed:12885774}.; liver;colon;spleen;kidney;stomach; . 0.09443 0.14256 0.518060413 80.35503657 712.55949 5.30299 ENPP7P1 . . . ectonucleotide pyrophosphatase/phosphodiesterase 7 pseudogene 1 . . . . . . . . . . . ENPP7P2 . . . ectonucleotide pyrophosphatase/phosphodiesterase 7 pseudogene 2 . . . . . . . . . . . ENPP7P3 . . . ectonucleotide pyrophosphatase/phosphodiesterase 7 pseudogene 3 . . . . . . . . . . . ENPP7P4 . . . ectonucleotide pyrophosphatase/phosphodiesterase 7 pseudogene 4 . . . . . . . . . . . ENPP7P5 . . . ectonucleotide pyrophosphatase/phosphodiesterase 7 pseudogene 5 . . . . . . . . . . . ENPP7P6 . . . ectonucleotide pyrophosphatase/phosphodiesterase 7 pseudogene 6 . . . . . . . . . . . ENPP7P7 . . . ectonucleotide pyrophosphatase/phosphodiesterase 7 pseudogene 7 . . . . . . . . . . . ENPP7P8 . . . ectonucleotide pyrophosphatase/phosphodiesterase 7 pseudogene 8 . . . . . . . . . . . ENPP7P9 . . . ectonucleotide pyrophosphatase/phosphodiesterase 7 pseudogene 9 . . . . . . . . . . . ENPP7P10 . . . ectonucleotide pyrophosphatase/phosphodiesterase 7 pseudogene 10 . . . . . . . . . . . ENPP7P11 . . . ectonucleotide pyrophosphatase/phosphodiesterase 7 pseudogene 11 . . . . . . . . . . . ENPP7P12 . . . ectonucleotide pyrophosphatase/phosphodiesterase 7 pseudogene 12 . . . . . . . . . . . ENPP7P13 . . . ectonucleotide pyrophosphatase/phosphodiesterase 7 pseudogene 13 . . . . . . . . . . . ENPP7P14 . . . ectonucleotide pyrophosphatase/phosphodiesterase 7 pseudogene 14 . . . . . . . . . . . ENSA 0.162369766475176 0.773694403514811 0.063935830010013 endosulfine alpha FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-67 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase (By similarity). Also acts as a stimulator of insulin secretion by interacting with sulfonylurea receptor (ABCC8), thereby preventing sulfonylurea from binding to its receptor and reducing K(ATP) channel currents. {ECO:0000250, ECO:0000269|PubMed:9653196}.; . TISSUE SPECIFICITY: Widely expressed with high levels in skeletal muscle and brain and lower levels in the pancreas. {ECO:0000269|PubMed:14728987, ECO:0000269|PubMed:9653196}.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;iris;germinal center;bladder;brain;tonsil;gall bladder;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; dorsal root ganglion;amygdala;whole brain;superior cervical ganglion;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;temporal lobe;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.16235 . 0.413500896 76.67492333 9.50386 0.35040 ENSAP1 . . . endosulfine alpha pseudogene 1 . . . . . . . . . . . ENSAP2 . . . endosulfine alpha pseudogene 2 . . . . . . . . . . . ENSAP3 . . . endosulfine alpha pseudogene 3 . . . . . . . . . . . ENTHD1 3.66824019270564e-06 0.580932538494391 0.419063793265416 ENTH domain containing 1 . . . unclassifiable (Anatomical System);lung;testis;skin; ciliary ganglion; 0.09862 0.07647 -0.156065314 42.16206653 519.77845 4.65769 ENTHD2 0.000515475663107338 0.883637157432014 0.115847366904878 ENTH domain containing 2 . . . . . 0.09160 0.08903 0.624649618 83.53385232 268.51912 3.51406 ENTPD1 0.519393999413089 0.479844980528228 0.000761020058682951 ectonucleoside triphosphate diphosphohydrolase 1 FUNCTION: In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well. {ECO:0000269|PubMed:8955160}.; DISEASE: Spastic paraplegia 64, autosomal recessive (SPG64) [MIM:615683]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. {ECO:0000269|PubMed:24482476}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed primarily on activated lymphoid cells. Also expressed in endothelial tissues. Isoform 1 and isoform 3 are present in both placenta and umbilical vein, whereas isoform 2 is present in placenta only.; . . 0.17364 0.23859 -0.336073593 30.55555556 66.52934 1.68061 ENTPD1-AS1 . . . ENTPD1 antisense RNA 1 . . . . . . . . . . . ENTPD2 9.49154003624772e-07 0.529242473966343 0.470756576879653 ectonucleoside triphosphate diphosphohydrolase 2 FUNCTION: In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent. The order of activity with different substrates is ATP > GTP > CTP = ITP > UTP >> ADP = UDP.; . TISSUE SPECIFICITY: Brain, placenta, skeletal muscle, kidney, pancreas, heart, ovary, testis, colon, small intestine, prostate and pancreas. No expression in adult thymus, spleen, lung, liver and peripheral blood leukocytes.; unclassifiable (Anatomical System);prostate;lung;ovary;islets of Langerhans;sympathetic chain;colon;kidney;stomach; globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.26192 0.15452 0.198490371 67.30360934 423.42211 4.29730 ENTPD3 2.55562814397697e-19 0.000141873120806751 0.999858126879193 ectonucleoside triphosphate diphosphohydrolase 3 FUNCTION: Has a threefold preference for the hydrolysis of ATP over ADP.; . TISSUE SPECIFICITY: Expressed in adult brain, pancreas, spleen and prostate. Moderate or low expression is seen in most tissues. Not expressed in liver and peripheral blood leukocytes.; unclassifiable (Anatomical System);heart;islets of Langerhans;sympathetic chain;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;lung;endometrium;larynx;macula lutea;hippocampus;testis;head and neck;germinal center;brain; dorsal root ganglion;superior cervical ganglion;pons;caudate nucleus; 0.16865 0.16922 -0.26629572 34.81953291 1007.34812 6.11352 ENTPD3-AS1 . . . ENTPD3 antisense RNA 1 . . . . . . . . . . . ENTPD4 2.06793054504749e-11 0.835451906864523 0.164548093114797 ectonucleoside triphosphate diphosphohydrolase 4 FUNCTION: Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent. The order of activity with different substrates is UDP >> GDP = CDP = TDP, AMP, ADP, ATP and UMP are not substrates. Preferred substrates for isoform 2 are CTP, UDP, CDP, GTP and GDP, while isoform 1 utilizes UTP and TTP.; . TISSUE SPECIFICITY: Ubiquitous. Highest expression in testis and lowest in bladder.; unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;skeletal muscle;bone marrow;uterus;prostate;lung;bone;placenta;thyroid;hippocampus;testis;mammary gland;stomach; dorsal root ganglion;amygdala;subthalamic nucleus;superior cervical ganglion;medulla oblongata;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.47883 0.15656 -0.663133267 15.94715735 1302.58974 6.78964 ENTPD5 0.000105198200581121 0.987569317943187 0.0123254838562322 ectonucleoside triphosphate diphosphohydrolase 5 FUNCTION: Uridine diphosphatase (UDPase) that promotes protein N- glycosylation and ATP level regulation. UDP hydrolysis promotes protein N-glycosylation and folding in the endoplasmic reticulum, as well as elevated ATP consumption in the cytosol via an ATP hydrolysis cycle. Together with CMPK1 and AK1, constitutes an ATP hydrolysis cycle that converts ATP to AMP and results in a compensatory increase in aerobic glycolysis. The nucleotide hydrolyzing preference is GDP > IDP > UDP, but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. Plays a key role in the AKT1-PTEN signaling pathway by promoting glycolysis in proliferating cells in response to phosphoinositide 3-kinase (PI3K) signaling. {ECO:0000269|PubMed:10400613}.; . TISSUE SPECIFICITY: Expressed in adult liver, kidney, prostate, testis and colon. Much weaker expression in other tissues. {ECO:0000269|PubMed:9676430}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;lens;breast;lung;placenta;macula lutea;hippocampus;visual apparatus;liver;kidney;stomach; superior cervical ganglion;liver;testis;ciliary ganglion;atrioventricular node; 0.12021 0.17656 0.41713504 76.95800896 118.81379 2.37133 ENTPD6 4.98993289171908e-05 0.965878343827056 0.0340717568440269 ectonucleoside triphosphate diphosphohydrolase 6 (putative) FUNCTION: Might support glycosylation reactions in the Golgi apparatus and, when released from cells, might catalyze the hydrolysis of extracellular nucleotides. Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent, there is no hydrolysis of nucleoside 5'-monophosphates. The order of activity with different substrates is GDP > IDP >> UDP = CDP >> ADP (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in most tissues, but predominantly in heart. {ECO:0000269|PubMed:11041856}.; myocardium;smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lacrimal gland;muscle;pancreas;lung;cornea;placenta;head and neck;kidney;stomach;thymus;cerebellum; whole brain;prostate;prefrontal cortex;caudate nucleus;cingulate cortex; 0.17609 0.11941 0.935129812 89.86199575 1414.90137 7.03053 ENTPD7 2.56620119878035e-08 0.974496986080331 0.0255029882576573 ectonucleoside triphosphate diphosphohydrolase 7 FUNCTION: Preferentially hydrolyzes nucleoside 5'-triphosphates. The order of activity with respect to possible substrates is UTP > GTP > CTP.; . . . . 0.30652 0.14392 0.110306132 62.00165133 1308.95673 6.80558 ENTPD8 1.72250124679312e-07 0.409343869871568 0.590655957878307 ectonucleoside triphosphate diphosphohydrolase 8 FUNCTION: Canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside NTPDases catalyze the hydrolysis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides. Has activity toward ATP, ADP, UTP and UDP, but not toward AMP. {ECO:0000269|PubMed:16752921, ECO:0000269|PubMed:17095758}.; . . unclassifiable (Anatomical System);lymphoreticular;endometrium;islets of Langerhans;testis;colon;kidney;mammary gland;stomach;retina; . 0.13589 0.14168 -1.063626766 7.484076433 379.58904 4.10854 ENUR1 . . . enuresis, nocturnal 1 . . . . . . . . . . . ENUR2 . . . enuresis, nocturnal 2 . . . . . . . . . . . ENY2 0.797810081751442 0.196549855774476 0.0056400624740822 enhancer of yellow 2 homolog (Drosophila) FUNCTION: Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B. The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. {ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:21746879}.; . . lymphoreticular;ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; white blood cells; 0.92577 . 0.145304857 63.81221986 1.27901 0.04509 EOGT 9.78550475841108e-06 0.934081868496479 0.0659083459987624 EGF domain-specific O-linked N-acetylglucosamine (GlcNAc) transferase FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins resulting in their modification with a beta-linked N- acetylglucosamine (O-GlcNAc). Specifically glycosylates the Thr residue located between the fifth and sixth conserved cysteines of folded EGF-like domains. {ECO:0000269|PubMed:23671640}.; DISEASE: Adams-Oliver syndrome 4 (AOS4) [MIM:615297]: A form of Adams-Oliver syndrome, a disorder characterized by the congenital absence of skin (aplasia cutis congenita) in combination with transverse limb defects. Aplasia cutis congenita can be located anywhere on the body, but in the vast majority of the cases, it is present on the posterior parietal region where it is often associated with an underlying defect of the parietal bones. Limb abnormalities are typically limb truncation defects affecting the distal phalanges or entire digits (true ectrodactyly). Only rarely, metatarsals/metacarpals or more proximal limb structures are also affected. Apart from transverse limb defects, syndactyly, most commonly of second and third toes, can also be observed. The clinical features are highly variable and can also include cardiovascular malformations, brain abnormalities and vascular defects such as cutis marmorata and dilated scalp veins. {ECO:0000269|PubMed:23522784}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.51752 0.09534 0.174625237 65.9648502 406.4022 4.22680 EOMES 0.71187838114463 0.287982075662636 0.000139543192733166 eomesodermin FUNCTION: Functions as a transcriptional activator playing a crucial role during development. Functions in trophoblast differentiation and later in gastrulation, regulating both mesoderm delamination and endoderm specification. Plays a role in brain development being required for the specification and the proliferation of the intermediate progenitor cells and their progeny in the cerebral cortex. Also involved in the differentiation of CD8+ T-cells during immune response regulating the expression of lytic effector genes. {ECO:0000269|PubMed:17353897, ECO:0000269|PubMed:17566017}.; DISEASE: Note=A translocation t(3;10)(p24;q23) located 215 kb 3' to the EOMES gene but leading to loss of its expression was identified in a large consanguineous family. Homozygous silencing produces microcephaly associated with corpus callosum agenesis, bilateral polymicrogyria, ventricular dilatation and a small cerebellum.; TISSUE SPECIFICITY: Expressed in CD8+ T-cells. {ECO:0000269|PubMed:17566017}.; unclassifiable (Anatomical System);uterus;pancreas;whole body;cartilage;nasopharynx;spleen;cerebellum; ciliary ganglion; 0.48495 0.33032 . . 149.31934 2.66428 EP300 0.999999999999484 5.15637503646322e-13 1.03030180470722e-32 E1A binding protein p300 FUNCTION: Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. Mediates acetylation of histone H3 at 'Lys-27' (H3K27ac). Also functions as acetyltransferase for nonhistone targets. Acetylates 'Lys-131' of ALX1 and acts as its coactivator. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Acetylates FOXO1 and enhances its transcriptional activity. Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity. Participates in CLOCK or NPAS2-regulated rhythmic gene transcription; exhibits a circadian association with CLOCK or NPAS2, correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter. Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity (PubMed:10733570, PubMed:11430825, PubMed:11701890, PubMed:12402037, PubMed:12586840, PubMed:12929931, PubMed:14645221, PubMed:15186775, PubMed:15890677, PubMed:16617102, PubMed:16762839, PubMed:18722353, PubMed:18995842, PubMed:23415232, PubMed:23911289, PubMed:23934153, PubMed:8945521). Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity (PubMed:20955178). Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902). Acetylates MEF2D. {ECO:0000269|PubMed:10733570, ECO:0000269|PubMed:11430825, ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:12402037, ECO:0000269|PubMed:12586840, ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15890677, ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:16762839, ECO:0000269|PubMed:18722353, ECO:0000269|PubMed:18995842, ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:23415232, ECO:0000269|PubMed:23911289, ECO:0000269|PubMed:23934153, ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:8945521, ECO:0000305|PubMed:20955178}.; DISEASE: Note=Defects in EP300 may play a role in epithelial cancer.; DISEASE: Note=Chromosomal aberrations involving EP300 may be a cause of acute myeloid leukemias. Translocation t(8;22)(p11;q13) with KAT6A.; DISEASE: Rubinstein-Taybi syndrome 2 (RSTS2) [MIM:613684]: A disorder characterized by craniofacial abnormalities, postnatal growth deficiency, broad thumbs, broad big toes, mental retardation and a propensity for development of malignancies. Some individuals with RSTS2 have less severe mental impairment, more severe microcephaly, and a greater degree of changes in facial bone structure than RSTS1 patients. {ECO:0000269|PubMed:15706485}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;atrium;whole body;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;testis;amniotic fluid;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;pharynx;blood;breast;lung;epididymis;nasopharynx;placenta;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; testis - interstitial;superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.99999 0.91015 -3.681999375 0.259495164 1174.22905 6.51042 EP300-AS1 . . . EP300 antisense RNA 1 . . . . . . . . . . . EP400 0.999999999883201 1.16799188576848e-10 1.57871656963504e-32 E1A binding protein p400 FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. May be required for transcriptional activation of E2F1 and MYC target genes during cellular proliferation. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. May regulate ZNF42 transcription activity. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. {ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:24463511}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11509179}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;bile duct;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;stomach;thymus; superior cervical ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.18578 0.27854 -3.863869047 0.218211842 4549.61959 13.54811 EP400NL 0.0912207592458008 0.765987765061308 0.142791475692891 EP400 N-terminal like . . . unclassifiable (Anatomical System);prostate;lung;ovary;placenta;visual apparatus;liver;testis;colon;spleen;blood;germinal center;brain; . 0.11553 . . . 506.16871 4.61699 EPAS1 0.997628292931524 0.00237170351079056 3.55768560308448e-09 endothelial PAS domain protein 1 FUNCTION: Transcription factor involved in the induction of oxygen regulated genes. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation seems to require recruitment of transcriptional coactivators such as CREBPB and probably EP300. Interaction with redox regulatory protein APEX seems to activate CTAD.; DISEASE: Erythrocytosis, familial, 4 (ECYT4) [MIM:611783]: An autosomal dominant disorder characterized by increased serum red blood cell mass, elevated serum hemoglobin and hematocrit, and normal platelet and leukocyte counts. {ECO:0000269|PubMed:18184961, ECO:0000269|PubMed:18378852, ECO:0000269|PubMed:19208626, ECO:0000269|PubMed:22367913}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in most tissues, with highest levels in placenta, lung and heart. Selectively expressed in endothelial cells.; smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;thyroid;brain;gall bladder;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;atrium;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;bile duct;pancreas;lung;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; lung;placenta;fetal lung;skeletal muscle; 0.24536 0.38555 -0.881793075 10.53904223 461.40716 4.45544 EPB41 0.0621098709716946 0.937884489988455 5.63903985092626e-06 erythrocyte membrane protein band 4.1 FUNCTION: Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes.; DISEASE: Elliptocytosis 1 (EL1) [MIM:611804]: A Rhesus-linked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape. {ECO:0000269|PubMed:3467321}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.75657 0.35913 -0.596992387 18.18825195 250.99535 3.41349 EPB41L1 0.645386132721516 0.354611657759902 2.20951858260536e-06 erythrocyte membrane protein band 4.1-like 1 FUNCTION: May function to confer stability and plasticity to neuronal membrane via multiple interactions, including the spectrin-actin-based cytoskeleton, integral membrane channels and membrane-associated guanylate kinases.; . TISSUE SPECIFICITY: Highest expression in brain, lower in heart, kidney, pancreas, placenta, lung and skeletal muscle.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;ganglion;frontal lobe;cochlea;larynx;bone;testis;amniotic fluid;brain;amygdala;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;pineal body;adrenal cortex;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;hippocampus;macula lutea;visual apparatus;hypopharynx;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; amygdala;dorsal root ganglion;whole brain;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;adrenal gland;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.11337 0.09363 -0.729274834 14.15428167 152.04173 2.69722 EPB41L2 0.993883457586741 0.00611654094126471 1.47199430671655e-09 erythrocyte membrane protein band 4.1-like 2 . . TISSUE SPECIFICITY: Widely expressed.; myocardium;lymphoreticular;ovary;skin;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;amygdala;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;olfactory bulb;testis;pons;trigeminal ganglion; 0.51043 0.13219 -0.990222991 8.634111819 306.66673 3.72665 EPB41L3 0.0292783880452307 0.970720872771158 7.39183610974376e-07 erythrocyte membrane protein band 4.1-like 3 FUNCTION: Tumor suppressor that inhibits cell proliferation and promotes apoptosis. Modulates the activity of protein arginine N- methyltransferases, including PRMT3 and PRMT5. {ECO:0000269|PubMed:15334060, ECO:0000269|PubMed:15737618, ECO:0000269|PubMed:16420693, ECO:0000269|PubMed:9892180}.; . TISSUE SPECIFICITY: Expressed at high levels in brain, with lower levels in kidney, intestine, and testis. Detected in lung. {ECO:0000269|PubMed:9892180}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;larynx;testis;dura mater;spinal ganglion;pineal gland;brain;unclassifiable (Anatomical System);meninges;lymph node;heart;cartilage;islets of Langerhans;hypothalamus;spinal cord;lens;breast;pancreas;pia mater;lung;adrenal gland;placenta;macula lutea;head and neck;kidney;stomach;aorta;cerebellum; whole brain;amygdala;superior cervical ganglion;thalamus;medulla oblongata;occipital lobe;hypothalamus;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.49060 0.20412 0.900159287 89.32531257 770.96799 5.49464 EPB41L4A 1.98631994116418e-11 0.951565139984968 0.0484348599951689 erythrocyte membrane protein band 4.1 like 4A . . TISSUE SPECIFICITY: Expressed in many tissues. High levels of expression in brain, liver, thymus and peripheral blood leukocytes and low levels of expression in heart, kidney, testis and colon.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;blood;skeletal muscle;prostate;lung;placenta;testis;kidney;brain;spinal ganglion;stomach;thymus; dorsal root ganglion;superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.12696 0.10578 1.605718424 95.91295117 1187.73182 6.53635 EPB41L4A-AS1 . . . EPB41L4A antisense RNA 1 . . . . . . . . . . . EPB41L4A-AS2 . . . EPB41L4A antisense RNA 2 (head to head) . . . . . . . . . 1355.56838 6.90896 EPB41L4B 0.999700026887568 0.00029997310776913 4.66277382680854e-12 erythrocyte membrane protein band 4.1 like 4B FUNCTION: Up-regulates the activity of the Rho guanine nucleotide exchange factor ARHGEF18 (By similarity). Involved in the regulation of the circumferential actomyosin belt in epithelial cells (PubMed:22006950). Promotes cellular adhesion, migration and motility in vitro and may play a role in wound healing (PubMed:23664528). May have a role in mediating cytoskeletal changes associated with steroid-induced cell differentiation (PubMed:14521927). {ECO:0000250|UniProtKB:Q9JMC8, ECO:0000269|PubMed:14521927, ECO:0000269|PubMed:22006950, ECO:0000269|PubMed:23664528}.; . TISSUE SPECIFICITY: Expressed at higher levels in acute wounds than chronic wounds with increased expression in healing wounds, especially at the leading wound edge (PubMed:23664528). Isoform 1 is highly expressed in brain. Isoform 2 is highly expressed in testis with lower levels in prostate and breast (PubMed:14521927). {ECO:0000269|PubMed:14521927, ECO:0000269|PubMed:23664528}.; ovary;colon;parathyroid;fovea centralis;choroid;retina;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;lens;skeletal muscle;bile duct;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum; dorsal root ganglion;pancreas;superior cervical ganglion;thyroid;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.56535 0.10659 -0.707227564 14.71455532 652.77838 5.12595 EPB41L5 0.0229338405829811 0.97706509296208 1.06645493878883e-06 erythrocyte membrane protein band 4.1 like 5 FUNCTION: May contribute to the correct positioning of tight junctions during the establishment of polarity in epithelial cells. {ECO:0000269|PubMed:17920587}.; . . colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;islets of Langerhans;adrenal cortex;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;liver;duodenum;alveolus;head and neck;spleen;kidney;stomach;cerebellum; dorsal root ganglion;medulla oblongata;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe; 0.19351 0.09111 0.04598748 57.47817882 253.06645 3.42227 EPB42 1.56180488450141e-07 0.955587190547662 0.04441265327185 erythrocyte membrane protein band 4.2 FUNCTION: Probably plays an important role in the regulation of erythrocyte shape and mechanical properties.; DISEASE: Spherocytosis 5 (SPH5) [MIM:612690]: Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Absence of band 4.2 associated with spur or target erythrocytes has also been reported. {ECO:0000269|PubMed:10406914, ECO:0000269|PubMed:1558976, ECO:0000269|PubMed:7772513, ECO:0000269|PubMed:7819064, ECO:0000269|PubMed:8547071, ECO:0000269|PubMed:8547605}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);whole body;cartilage;bone;visual apparatus;liver;testis;colon;spleen;choroid; superior cervical ganglion;fetal liver;ciliary ganglion;fetal lung;atrioventricular node;skeletal muscle;bone marrow; 0.41009 0.12721 -0.194700582 39.24274593 150.84156 2.68319 EPC1 0.999993177292492 6.82270749652117e-06 1.13215577287487e-14 enhancer of polycomb homolog 1 FUNCTION: Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. {ECO:0000269|PubMed:14966270}.; . . sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;cochlea;larynx;thyroid;testis;amniotic fluid;germinal center;brain;artery;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;hypopharynx;liver;spleen;head and neck;kidney;aorta;stomach;peripheral nerve;thymus; . 0.34209 0.09515 -0.619039275 17.39797122 594.10458 4.93849 EPC2 0.999952360459163 4.76395344736943e-05 6.36364726847593e-12 enhancer of polycomb homolog 2 FUNCTION: May play a role in transcription or DNA repair. {ECO:0000250}.; . . ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;cerebral cortex;larynx;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;mammary gland;stomach; skeletal muscle; 0.17117 0.16034 -0.291981272 33.20358575 99.22432 2.15595 EPCAM 7.50009447417055e-07 0.479893423209315 0.520105826781238 epithelial cell adhesion molecule FUNCTION: May act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E. {ECO:0000269|PubMed:15195135, ECO:0000269|PubMed:15922867, ECO:0000269|PubMed:19785009, ECO:0000269|PubMed:20064925}.; DISEASE: Diarrhea 5, with tufting enteropathy, congenital (DIAR5) [MIM:613217]: An intractable diarrhea of infancy characterized by villous atrophy and absence of inflammation, with intestinal epithelial cell dysplasia manifesting as focal epithelial tufts in the duodenum and jejunum. {ECO:0000269|PubMed:18572020}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hereditary non-polyposis colorectal cancer 8 (HNPCC8) [MIM:613244]: An autosomal dominant disease associated with marked increase in cancer susceptibility. It is characterized by a familial predisposition to early-onset colorectal carcinoma (CRC) and extra-colonic tumors of the gastrointestinal, urological and female reproductive tracts. HNPCC is reported to be the most common form of inherited colorectal cancer in the Western world. Clinically, HNPCC is often divided into two subgroups. Type I is characterized by hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon. Type II is characterized by increased risk for cancers in certain tissues such as the uterus, ovary, breast, stomach, small intestine, skin, and larynx in addition to the colon. Diagnosis of classical HNPCC is based on the Amsterdam criteria: 3 or more relatives affected by colorectal cancer, one a first degree relative of the other two; 2 or more generation affected; 1 or more colorectal cancers presenting before 50 years of age; exclusion of hereditary polyposis syndromes. The term 'suspected HNPCC' or 'incomplete HNPCC' can be used to describe families who do not or only partially fulfill the Amsterdam criteria, but in whom a genetic basis for colon cancer is strongly suspected. {ECO:0000269|PubMed:19098912}. Note=The disease is caused by mutations affecting the gene represented in this entry. HNPCC8 results from heterozygous deletion of 3-prime exons of EPCAM and intergenic regions directly upstream of MSH2, resulting in transcriptional read-through and epigenetic silencing of MSH2 in tissues expressing EPCAM.; TISSUE SPECIFICITY: Highly and selectively expressed by undifferentiated rather than differentiated embryonic stem cells (ESC). Levels rapidly diminish as soon as ESC's differentiate (at protein levels). Expressed in almost all epithelial cell membranes but not on mesodermal or neural cell membranes. Found on the surface of adenocarcinoma. {ECO:0000269|PubMed:20064925}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;pituitary gland;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; pancreas;thyroid;beta cell islets; 0.61487 0.29457 0.373041938 75.29488087 2850.98345 10.10064 EPDR1 0.029388013814021 0.804855059313927 0.165756926872052 ependymin related 1 . . . myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;spinal cord;muscle;adrenal cortex;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach;cerebellum; . 0.14857 0.10928 0.483275131 79.25218212 1445.4096 7.09147 EPG5 6.93636539718872e-07 0.999999306362335 1.12495677841537e-12 ectopic P-granules autophagy protein 5 homolog (C. elegans) FUNCTION: Involved in autophagy. May play a role in a late step of autophagy, such as clearance of autophagosomal cargo. {ECO:0000269|PubMed:20550938, ECO:0000269|PubMed:23222957}.; DISEASE: Vici syndrome (VICIS) [MIM:242840]: A rare congenital multisystem disorder characterized by agenesis of the corpus callosum, cataracts, pigmentary defects, progressive cardiomyopathy, and variable immunodeficiency. Affected individuals also have profound psychomotor retardation and hypotonia due to a myopathy. {ECO:0000269|PubMed:23222957}. Note=The disease is caused by mutations affecting the gene represented in this entry. Affected individuals show homozygosity or compound heterozygosity for truncating mutations, aberrant splicing and/or missense mutations. Parental studies suggest recessive inheritance with no carrier manifestation (PubMed:23222957). {ECO:0000269|PubMed:23222957}.; . unclassifiable (Anatomical System);breast;lung;placenta;alveolus;colon;blood;germinal center;bone marrow; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.22772 0.09992 -0.364112929 28.31446096 6235.40864 16.50843 EPGN 0.00349254550043154 0.619325485984178 0.377181968515391 epithelial mitogen FUNCTION: Promotes the growth of epithelial cells. May stimulate the phosphorylation of EGFR and mitogen-activated protein kinases. {ECO:0000269|PubMed:15611079}.; . . . . 0.33459 0.33018 -0.229483771 36.86010852 8.92956 0.32831 EPHA1 5.30365074340992e-11 0.94286155798998 0.0571384419569839 EPH receptor A1 FUNCTION: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds with a low affinity EFNA3 and EFNA4 and with a high affinity to EFNA1 which most probably constitutes its cognate/functional ligand. Upon activation by EFNA1 induces cell attachment to the extracellular matrix inhibiting cell spreading and motility through regulation of ILK and downstream RHOA and RAC. Plays also a role in angiogenesis and regulates cell proliferation. May play a role in apoptosis. {ECO:0000269|PubMed:17634955, ECO:0000269|PubMed:19118217, ECO:0000269|PubMed:20043122}.; . TISSUE SPECIFICITY: Overexpressed in several carcinomas.; unclassifiable (Anatomical System);cartilage;ovary;urinary;colon;parathyroid;blood;bone marrow;breast;prostate;optic nerve;lung;thyroid;liver;testis;spleen;germinal center;brain;stomach;cerebellum; superior cervical ganglion; 0.66064 0.17893 -0.898404627 10.16749233 981.68133 6.04867 EPHA1-AS1 . . . EPHA1 antisense RNA 1 . . . . . . . . . . . EPHA2 0.738294173427745 0.261704957521137 8.69051117714366e-07 EPH receptor A2 FUNCTION: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand- independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis. {ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:16236711, ECO:0000269|PubMed:18339848, ECO:0000269|PubMed:19573808, ECO:0000269|PubMed:20679435, ECO:0000269|PubMed:20861311, ECO:0000269|PubMed:23358419}.; DISEASE: Cataract 6, multiple types (CTRCT6) [MIM:116600]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT6 includes posterior polar and age- related cortical cataracts, among others. Posterior polar cataract is a subcapsular opacity, usually disk-shaped, located at the back of the lens. Age-related cortical cataract is a developmental punctate opacity restricted to the cortex. The cataract is white or cerulean, increases in number with age, but rarely affects vision. {ECO:0000269|PubMed:19005574, ECO:0000269|PubMed:19306328, ECO:0000269|PubMed:19649315}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Overexpressed in several cancer types and promotes malignancy. {ECO:0000269|PubMed:19573808}.; TISSUE SPECIFICITY: Expressed in brain and glioma tissue and glioma cell lines (at protein level). Expressed most highly in tissues that contain a high proportion of epithelial cells, e.g. skin, intestine, lung, and ovary. {ECO:0000269|PubMed:17332925}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;testis;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;urinary;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;duodenum;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion; 0.54830 0.28861 -0.628385276 16.82000472 391.87029 4.16611 EPHA3 0.0156859621990761 0.98431216443612 1.87336480404369e-06 EPH receptor A3 FUNCTION: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development. {ECO:0000269|PubMed:11870224}.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:12738854}. Note=The gene represented in this entry may be involved in disease pathogenesis.; TISSUE SPECIFICITY: Widely expressed. Highest level in placenta.; unclassifiable (Anatomical System);ovary;cartilage;hypothalamus;developmental;colon;parathyroid;skin;skeletal muscle;prostate;whole body;placenta;bone;testis;spleen;kidney;brain; subthalamic nucleus;superior cervical ganglion;fetal brain;adrenal cortex;testis;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.29873 0.21233 -0.903841325 10.14390186 4421.59874 13.31806 EPHA4 0.99989132522117 0.000108674778437245 3.9304079059375e-13 EPH receptor A4 FUNCTION: Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections. May also control the segregation of motor and sensory axons during neuromuscular circuit development. In addition to its role in axonal guidance plays a role in synaptic plasticity. Activated by EFNA1 phosphorylates CDK5 at 'Tyr-15' which in turn phosphorylates NGEF regulating RHOA and dendritic spine morphogenesis. In the nervous system, plays also a role in repair after injury preventing axonal regeneration and in angiogenesis playing a role in central nervous system vascular formation. Additionally, its promiscuity makes it available to participate in a variety of cell-cell signaling regulating for instance the development of the thymic epithelium. {ECO:0000269|PubMed:17143272}.; . TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;developmental;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;atrium;whole body;frontal lobe;endometrium;thyroid;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;lens;skeletal muscle;pancreas;lung;trabecular meshwork;macula lutea;visual apparatus;hippocampus;spleen;head and neck;kidney;mammary gland;stomach;aorta; whole brain;amygdala;medulla oblongata;occipital lobe;subthalamic nucleus;fetal brain;cerebellum peduncles;temporal lobe;prefrontal cortex;globus pallidus;testis;pons;parietal lobe;cingulate cortex; 0.77201 0.21939 -1.39618256 4.222694032 66.61755 1.68323 EPHA5 0.000390070112904698 0.999530763110319 7.9166776776703e-05 EPH receptor A5 FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI- anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Among GPI-anchored ephrin-A ligands, EFNA5 most probably constitutes the cognate/functional ligand for EPHA5. Functions as an axon guidance molecule during development and may be involved in the development of the retinotectal, entorhino- hippocampal and hippocamposeptal pathways. Together with EFNA5 plays also a role in synaptic plasticity in adult brain through regulation of synaptogenesis. In addition to its function in the nervous system, the interaction of EPHA5 with EFNA5 mediates communication between pancreatic islet cells to regulate glucose- stimulated insulin secretion (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Almost exclusively expressed in the nervous system in cortical neurons, cerebellar Purkinje cells and pyramidal neurons within the cortex and hippocampus. Display an increasing gradient of expression from the forebrain to hindbrain and spinal cord. {ECO:0000269|PubMed:10375373, ECO:0000269|PubMed:9191074}.; unclassifiable (Anatomical System);lung;hypothalamus;brain;skeletal muscle; globus pallidus;atrioventricular node;parietal lobe; 0.29288 0.13579 -1.238203625 5.490681765 548.86151 4.76544 EPHA5-AS1 . . . EPHA5 antisense RNA 1 . . . . . . . . . . . EPHA6 0.954513146757851 0.0454868113885373 4.18536118755321e-08 EPH receptor A6 FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI- anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain and testis. {ECO:0000269|PubMed:14726470}.; . . 0.34698 . -0.771553417 13.15168672 252.47147 3.41934 EPHA7 0.987759366731359 0.0122406316402381 1.62840292162679e-09 EPH receptor A7 FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI- anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Among GPI-anchored ephrin-A ligands, EFNA5 is a cognate/functional ligand for EPHA7 and their interaction regulates brain development modulating cell-cell adhesion and repulsion. Has a repellent activity on axons and is for instance involved in the guidance of corticothalamic axons and in the proper topographic mapping of retinal axons to the colliculus. May also regulate brain development through a caspase(CASP3)-dependent proapoptotic activity. Forward signaling may result in activation of components of the ERK signaling pathway including MAP2K1, MAP2K2, MAPK1 AND MAPK3 which are phosphorylated upon activation of EPHA7. {ECO:0000269|PubMed:17726105}.; . TISSUE SPECIFICITY: Widely expressed.; . . 0.89790 0.16935 -0.863377021 10.84571833 969.55706 6.01927 EPHA8 1.13671356316739e-08 0.983030390753397 0.016969597879468 EPH receptor A8 FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI- anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. The GPI-anchored ephrin-A EFNA2, EFNA3, and EFNA5 are able to activate EPHA8 through phosphorylation. With EFNA5 may regulate integrin-mediated cell adhesion and migration on fibronectin substrate but also neurite outgrowth. During development of the nervous system plays also a role in axon guidance. Downstream effectors of the EPHA8 signaling pathway include FYN which promotes cell adhesion upon activation by EPHA8 and the MAP kinases in the stimulation of neurite outgrowth (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);pancreas;optic nerve;lung;islets of Langerhans;macula lutea;fovea centralis;choroid;lens;retina; . 0.32535 0.12252 0.130330208 63.21066289 1372.14313 6.94837 EPHA10 3.15992066275912e-18 0.00858399368055652 0.991416006319443 EPH receptor A10 FUNCTION: Receptor for members of the ephrin-A family. Binds to EFNA3, EFNA4 and EFNA5. {ECO:0000269|PubMed:15777695}.; . TISSUE SPECIFICITY: Mainly expressed in testis. {ECO:0000269|PubMed:15777695}.; lung;islets of Langerhans;macula lutea;hippocampus;testis;colon;fovea centralis;kidney; superior cervical ganglion;testis - interstitial;testis;ciliary ganglion; 0.12012 0.10146 1.078370636 91.75513093 4746.47085 13.92599 EPHB1 0.998398641021365 0.0016013576134173 1.36521758746319e-09 EPH receptor B1 FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Cognate/functional ephrin ligands for this receptor include EFNB1, EFNB2 and EFNB3. During nervous system development, regulates retinal axon guidance redirecting ipsilaterally ventrotemporal retinal ganglion cells axons at the optic chiasm midline. This probably requires repulsive interaction with EFNB2. In the adult nervous system together with EFNB3, regulates chemotaxis, proliferation and polarity of the hippocampus neural progenitors. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and synapse formation. May also regulate angiogenesis. More generally, may play a role in targeted cell migration and adhesion. Upon activation by EFNB1 and probably other ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively. {ECO:0000269|PubMed:12223469, ECO:0000269|PubMed:12925710, ECO:0000269|PubMed:18034775, ECO:0000269|PubMed:9430661, ECO:0000269|PubMed:9499402}.; . TISSUE SPECIFICITY: Preferentially expressed in brain.; . . 0.81976 0.22741 -1.326403565 4.71809389 94.20968 2.08790 EPHB2 0.999948635231362 5.13647609935642e-05 7.64459666502637e-12 EPH receptor B2 FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Functions in axon guidance during development. Involved in the guidance of commissural axons, that form a major interhemispheric connection between the 2 temporal lobes of the cerebral cortex. Also involved in guidance of contralateral inner ear efferent growth cones at the midline and of retinal ganglion cell axons to the optic disk. In addition to axon guidance, also regulates dendritic spines development and maturation and stimulates the formation of excitatory synapses. Upon activation by EFNB1, abolishes the ARHGEF15-mediated negative regulation on excitatory synapse formation. Controls other aspects of development including angiogenesis, palate development and in inner ear development through regulation of endolymph production. Forward and reverse signaling through the EFNB2/EPHB2 complex regulate movement and adhesion of cells that tubularize the urethra and septate the cloaca. May function as a tumor suppressor. {ECO:0000269|PubMed:15300251}.; . TISSUE SPECIFICITY: Brain, heart, lung, kidney, placenta, pancreas, liver and skeletal muscle. Preferentially expressed in fetal brain.; . . 0.22176 0.58013 -1.456898556 3.862939372 184.17467 2.94594 EPHB3 0.956539592127129 0.0434603705306278 3.73422427877128e-08 EPH receptor B3 FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Generally has an overlapping and redundant function with EPHB2. Like EPHB2, functions in axon guidance during development regulating for instance the neurons forming the corpus callosum and the anterior commissure, 2 major interhemispheric connections between the temporal lobes of the cerebral cortex. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and the formation of excitatory synapses. Controls other aspects of development through regulation of cell migration and positioning. This includes angiogenesis, palate development and thymic epithelium development for instance. Forward and reverse signaling through the EFNB2/EPHB3 complex also regulate migration and adhesion of cells that tubularize the urethra and septate the cloaca. Finally, plays an important role in intestinal epithelium differentiation segregating progenitor from differentiated cells in the crypt. {ECO:0000269|PubMed:15536074}.; . TISSUE SPECIFICITY: Ubiquitous.; unclassifiable (Anatomical System);smooth muscle;ovary;heart;colon;skin;breast;uterus;prostate;pancreas;whole body;lung;larynx;bone;placenta;hypopharynx;testis;head and neck;kidney;brain;mammary gland;bladder;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.42115 0.22788 -2.677226852 0.731304553 89.15737 2.02905 EPHB4 0.989869332436591 0.0101306665394343 1.02397516390408e-09 EPH receptor B4 FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with its cognate ligand/functional ligand EFNB2 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4- mediated forward signaling controls cellular repulsion and segregation form EFNB2-expressing cells. Plays also a role in postnatal blood vessel remodeling, morphogenesis and permeability and is thus important in the context of tumor angiogenesis. {ECO:0000269|PubMed:12734395, ECO:0000269|PubMed:16424904}.; . TISSUE SPECIFICITY: Abundantly expressed in placenta but also detected in kidney, liver, lung, pancreas, skeletal muscle and heart. Expressed in primitive and myeloid, but not lymphoid, hematopoietic cells. Also observed in cell lines derived from liver, breast, colon, lung, melanocyte and cervix. {ECO:0000269|PubMed:8188704}.; myocardium;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;iris;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;duodenum;liver;hypopharynx;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; subthalamic nucleus;superior cervical ganglion;adrenal gland;placenta;globus pallidus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.46877 0.25774 -1.501002093 3.597546591 175.15701 2.87821 EPHB6 0.253348704299398 0.746649171330968 2.12436963398061e-06 EPH receptor B6 FUNCTION: Kinase-defective receptor for members of the ephrin-B family. Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion and migration by exerting both positive and negative effects upon stimulation with ephrin-B2. Inhibits JNK activation, T-cell receptor-induced IL-2 secretion and CD25 expression upon stimulation with ephrin-B2. {ECO:0000269|PubMed:12517763, ECO:0000269|PubMed:15955811}.; . TISSUE SPECIFICITY: Expressed in brain. Expressed in non invasive breast carcinoma cell lines (at protein level). Strong expression in brain and pancreas, and weak expression in other tissues, such as heart, placenta, lung, liver, skeletal muscle and kidney. Expressed in breast non invasive tumors but not in metastatic lesions. Isoform 3 is expressed in cell lines of glioblastomas, anaplastic astrocytomas, gliosarcomas and astrocytomas. Isoform 3 is not detected in normal tissues. {ECO:0000269|PubMed:18754880, ECO:0000269|PubMed:19234485, ECO:0000269|PubMed:9207182}.; . . 0.36674 0.22955 -1.434847051 3.998584572 2582.66198 9.50484 EPHX1 1.6189441694091e-07 0.397801202451498 0.602198635654085 epoxide hydrolase 1 FUNCTION: Biotransformation enzyme that catalyzes the hydrolysis of arene and aliphatic epoxides to less reactive and more water soluble dihydrodiols by the trans addition of water.; DISEASE: Familial hypercholanemia (FHCA) [MIM:607748]: A disorder characterized by elevated serum bile acid concentrations, itching, and fat malabsorption. {ECO:0000269|PubMed:12878321}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in liver. {ECO:0000269|PubMed:12878321}.; medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;colon;fovea centralis;choroid;uterus;whole body;cerebral cortex;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;placenta;hippocampus;hypopharynx;kidney;stomach;cerebellum; adipose tissue;adrenal gland;liver;adrenal cortex; 0.13476 0.66493 0.712836712 85.76315169 5182.02528 14.81092 EPHX2 4.92248524715445e-13 0.0963431123703321 0.903656887629176 epoxide hydrolase 2 FUNCTION: Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo- 9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro- 9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy- octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate. {ECO:0000269|PubMed:12574508, ECO:0000269|PubMed:12574510}.; . . . . 0.09483 0.39073 0.692611128 85.26185421 2236.75889 8.72195 EPHX3 5.04640148477413e-07 0.402263767141354 0.597735728218497 epoxide hydrolase 3 . . . unclassifiable (Anatomical System);pancreas;lymph node;lung;placenta;blood;kidney;skin;bone marrow; superior cervical ganglion;globus pallidus;trigeminal ganglion;skeletal muscle; 0.60283 0.11290 -0.115612493 45.12856806 40.12731 1.17934 EPHX4 0.033543926869158 0.957879628717333 0.00857644441350924 epoxide hydrolase 4 . . . . . 0.16360 0.10274 -0.494039303 22.09247464 26.72369 0.86499 EPM2A 3.58971451329325e-05 0.368559658109774 0.631404444745093 epilepsy, progressive myoclonus type 2A, Lafora disease (laforin) . . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;blood;fovea centralis;skin;skeletal muscle;retina;uterus;prostate;lung;endometrium;epididymis;placenta;macula lutea;pituitary gland;cervix;germinal center;kidney;brain; superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.54907 0.32511 . . 120.1533 2.38861 EPM2AIP1 0.164415268467168 0.832511254047911 0.00307347748492114 EPM2A (laforin) interacting protein 1 . . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, liver, pancreas, kidney and skeletal muscle. {ECO:0000269|PubMed:12782127}.; . . . . -0.005381972 53.50908233 25.37407 0.82883 EPN1 0.430317762502804 0.568177492479064 0.00150474501813175 epsin 1 FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis. {ECO:0000250, ECO:0000269|PubMed:10557078}.; . . unclassifiable (Anatomical System);prostate;lung;bone;placenta;visual apparatus;liver;testis;colon;cervix;brain;mammary gland;skin;skeletal muscle; subthalamic nucleus;globus pallidus;skeletal muscle;cingulate cortex; 0.29364 0.17391 -0.262657925 34.93158764 163.13888 2.78909 EPN2 0.177426616638577 0.82203284114896 0.00054054221246301 epsin 2 FUNCTION: Plays a role in the formation of clathrin-coated invaginations and endocytosis. {ECO:0000269|PubMed:10567358}.; . TISSUE SPECIFICITY: Highest expression is found in brain. Detected at lower levels in lung and liver. {ECO:0000269|PubMed:10567358}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;hippocampus;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; amygdala;whole brain;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;caudate nucleus;pons;parietal lobe;skeletal muscle; 0.21802 0.10187 -0.376526807 28.10804435 83.96156 1.95145 EPN2-AS1 . . . EPN2 antisense RNA 1 . . . . . . . . . . . EPN2-IT1 . . . EPN2 intronic transcript 1 . . . . . . . . . . . EPN3 1.33458182552155e-09 0.190008941203008 0.80999105746241 epsin 3 . . TISSUE SPECIFICITY: Detected in migrating keratinocytes from wounded skin, but not in differentiating keratinocytes or in normal skin. Detected in chronic wounds, basal cell carcinoma and ulcerative colitis. {ECO:0000269|PubMed:11359770}.; unclassifiable (Anatomical System);uterus;prostate;lymph node;lung;placenta;testis;colon;kidney; dorsal root ganglion;thalamus;prostate;subthalamic nucleus;superior cervical ganglion;tongue;ciliary ganglion;atrioventricular node;cingulate cortex;skeletal muscle; 0.28302 0.09290 1.140856814 92.36848313 3548.81195 11.50502 EPO 0.116862381941263 0.856558017463752 0.0265796005949852 erythropoietin FUNCTION: Erythropoietin is the principal hormone involved in the regulation of erythrocyte differentiation and the maintenance of a physiological level of circulating erythrocyte mass.; . TISSUE SPECIFICITY: Produced by kidney or liver of adult mammals and by liver of fetal or neonatal mammals.; prostate;optic nerve;macula lutea;liver;spleen;fovea centralis;choroid;lens;brain;retina; dorsal root ganglion;subthalamic nucleus;medulla oblongata;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle;skin;parietal lobe; 0.39663 0.80190 0.637604436 83.77565464 40.18285 1.18109 EPOR 0.058450671852552 0.924054964571437 0.0174943635760109 erythropoietin receptor FUNCTION: Receptor for erythropoietin. Mediates erythropoietin- induced erythroblast proliferation and differentiation. Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade. In some cell types, can also activate STAT1 and STAT3. May also activate the LYN tyrosine kinase.; DISEASE: Erythrocytosis, familial, 1 (ECYT1) [MIM:133100]: An autosomal dominant disorder characterized by increased serum red blood cell mass, elevated hemoglobin and hematocrit, hypersensitivity of erythroid progenitors to erythropoietin, erythropoietin low serum levels, and no increase in platelets nor leukocytes. It has a relatively benign course and does not progress to leukemia. {ECO:0000269|PubMed:8174675, ECO:0000269|PubMed:8506290, ECO:0000269|PubMed:8608241}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Erythroid cells and erythroid progenitor cells. Isoform EPOR-F is the most abundant form in EPO-dependent erythroleukemia cells and in late-stage erythroid progenitors. Isoform EPOR-S and isoform EPOR-T are the predominant forms in bone marrow. Isoform EPOR-T is the most abundant from in early- stage erythroid progenitor cells.; unclassifiable (Anatomical System);cartilage;heart;colon;uterus;optic nerve;whole body;lung;endometrium;bone;thyroid;placenta;liver;testis;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;fetal liver;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.59339 . 0.775339069 87.13729653 324.33322 3.82732 EPPIN 0.000111214074168112 0.596925697238306 0.402963088687526 epididymal peptidase inhibitor FUNCTION: Serine protease inhibitor that plays an essential role in male reproduction and fertility. Modulates the hydrolysis of SEMG1 by KLK3/PSA (a serine protease), provides antimicrobial protection for spermatozoa in the ejaculate coagulum, and binds SEMG1 thereby inhibiting sperm motility. {ECO:0000269|PubMed:15229136, ECO:0000269|PubMed:17644992}.; . TISSUE SPECIFICITY: In testis, expressed and secreted by Sertoli cells, appearing on the surface of testicular and ejaculate spermatozoa. Expressed in the spermatogonia and the earliest preleptotene spermatocytes. In the epididymis, is expressed and secreted by epithelial cells and covers the surface of epididymal spermatozoa and ciliated epithelial cells (at protein level). Expressed specifically in epididymis and testis. Isoform 2 is expressed only in the epididymis. Weak expression is detected in myoid cells as well as spermatogenic cells. {ECO:0000269|PubMed:11404006, ECO:0000269|PubMed:21461566}.; . . . 0.09006 0.435547893 77.45340882 229.94095 3.27678 EPPIN-WFDC6 0.000111214074168112 0.596925697238306 0.402963088687526 EPPIN-WFDC6 readthrough FUNCTION: Serine protease inhibitor that plays an essential role in male reproduction and fertility. Modulates the hydrolysis of SEMG1 by KLK3/PSA (a serine protease), provides antimicrobial protection for spermatozoa in the ejaculate coagulum, and binds SEMG1 thereby inhibiting sperm motility. {ECO:0000269|PubMed:15229136, ECO:0000269|PubMed:17644992}.; . TISSUE SPECIFICITY: In testis, expressed and secreted by Sertoli cells, appearing on the surface of testicular and ejaculate spermatozoa. Expressed in the spermatogonia and the earliest preleptotene spermatocytes. In the epididymis, is expressed and secreted by epithelial cells and covers the surface of epididymal spermatozoa and ciliated epithelial cells (at protein level). Expressed specifically in epididymis and testis. Isoform 2 is expressed only in the epididymis. Weak expression is detected in myoid cells as well as spermatogenic cells. {ECO:0000269|PubMed:11404006, ECO:0000269|PubMed:21461566}.; . . . . 0.215080721 67.91696155 . . EPPK1 4.95287341529358e-21 0.00136859556079458 0.998631404439205 epiplakin 1 . . TISSUE SPECIFICITY: Widely expressed with highest levels in liver, small intestine, colon, salivary glands, stomach and appendix.; . . . . . . 5706.98129 15.64597 EPRS 3.847395094191e-07 0.999999426453109 1.88807381925044e-07 glutamyl-prolyl-tRNA synthetase FUNCTION: Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop- containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. {ECO:0000269|PubMed:15479637, ECO:0000269|PubMed:1756734, ECO:0000269|PubMed:23071094}.; . . . . 0.82595 0.52905 -0.123106115 44.10828025 875.37524 5.75488 EPS8 0.947393284119214 0.0526067036816457 1.21991406459943e-08 epidermal growth factor receptor pathway substrate 8 FUNCTION: Signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture. Depending on its association with other signal transducers, can regulate different processes. Together with SOS1 and ABI1, forms a trimeric complex that participates in transduction of signals from Ras to Rac by activating the Rac- specific guanine nucleotide exchange factor (GEF) activity. Acts as a direct regulator of actin dynamics by binding actin filaments and has both barbed-end actin filament capping and actin bundling activities depending on the context. Displays barbed-end actin capping activity when associated with ABI1, thereby regulating actin-based motility process: capping activity is auto-inhibited and inhibition is relieved upon ABI1 interaction. Also shows actin bundling activity when associated with BAIAP2, enhancing BAIAP2- dependent membrane extensions and promoting filopodial protrusions. Involved in the regulation of processes such as axonal filopodia growth, stereocilia length, dendritic cell migration and cancer cell migration and invasion. Acts as a regulator of axonal filopodia formation in neurons: in the absence of neurotrophic factors, negatively regulates axonal filopodia formation via actin-capping activity. In contrast, it is phosphorylated in the presence of BDNF leading to inhibition of its actin-capping activity and stimulation of filopodia formation. Component of a complex with DFNB31 and MYO15A that localizes at stereocilia tips and is required for elongation of the stereocilia actin core. Indirectly involved in cell cycle progression; its degradation following ubiquitination being required during G2 phase to promote cell shape changes. {ECO:0000269|PubMed:15558031, ECO:0000269|PubMed:17115031}.; DISEASE: Deafness, autosomal recessive, 102 (DFNB102) [MIM:615974]: A form of non-syndromic deafness characterized by profound hearing loss affecting all frequencies. Vestibular function is unaffected. {ECO:0000269|PubMed:24741995}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in EPS8 are associated with some cancers, such as pancreatic, oral squamous cell carcinomas or pituitary cancers. Contributes to cell transformation in response to growth factor treatment and is overexpressed in a number of tumors, indicating that EPS8 levels must be tightly regulated. {ECO:0000269|PubMed:11244499, ECO:0000269|PubMed:18566210, ECO:0000269|PubMed:19008210, ECO:0000269|PubMed:19116338, ECO:0000269|PubMed:19448673}.; TISSUE SPECIFICITY: Expressed in all tissues analyzed, including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Expressed in all epithelial and fibroblastic lines examined and in some, but not all, hematopoietic cells.; smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;iris;testis;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;aorta;stomach; uterus;superior cervical ganglion;adipose tissue; 0.17322 0.29870 -0.304932527 32.24817174 284.10077 3.60783 EPS8L1 2.74517829340862e-08 0.904569390202506 0.0954305823457115 EPS8 like 1 FUNCTION: Stimulates guanine exchange activity of SOS1. May play a role in membrane ruffling and remodeling of the actin cytoskeleton. {ECO:0000269|PubMed:14565974}.; . TISSUE SPECIFICITY: Detected in placenta. {ECO:0000269|PubMed:14565974}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;testis;brain;unclassifiable (Anatomical System);islets of Langerhans;muscle;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;tongue;placenta;thyroid;ciliary ganglion;pons;trigeminal ganglion;skin;skeletal muscle; 0.14351 0.10672 7.61E-05 53.98089172 6300.10769 16.58867 EPS8L2 0.00182700802996643 0.997138159400746 0.00103483256928805 EPS8 like 2 FUNCTION: Stimulates guanine exchange activity of SOS1. May play a role in membrane ruffling and remodeling of the actin cytoskeleton. {ECO:0000269|PubMed:14565974}.; . TISSUE SPECIFICITY: Detected in fibroblasts and placenta. {ECO:0000269|PubMed:14565974}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;epidermis;tongue;islets of Langerhans;muscle;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;kidney; 0.20869 0.13493 -1.262067713 5.284265157 298.71169 3.68547 EPS8L3 0.000100217168096749 0.999342890677421 0.000556892154482446 EPS8 like 3 . . . breast;unclassifiable (Anatomical System);bile duct;ovary;liver;testis;colon;kidney;skeletal muscle;stomach; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.07946 0.08886 0.868987491 88.84760557 7291.82629 18.38006 EPS15 0.241707066029501 0.758290573874726 2.36009577328865e-06 epidermal growth factor receptor pathway substrate 15 FUNCTION: Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta- 1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269|PubMed:16903783, ECO:0000269|PubMed:18362181, ECO:0000269|PubMed:19458185, ECO:0000269|PubMed:22648170}.; DISEASE: Note=A chromosomal aberration involving EPS15 is found in acute leukemias. Translocation t(1;11)(p32;q23) with KMT2A/MLL1. The result is a rogue activator protein.; TISSUE SPECIFICITY: Ubiquitously expressed.; . . 0.59794 0.43407 0.470324112 78.82755367 2560.45416 9.44971 EPS15L1 0.970002535208416 0.0299974617897538 3.00183059132308e-09 epidermal growth factor receptor pathway substrate 15-like 1 FUNCTION: Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269|PubMed:22648170, ECO:0000269|PubMed:9407958}.; . . unclassifiable (Anatomical System);islets of Langerhans;urinary;adrenal cortex;colon;skeletal muscle;breast;uterus;pancreas;prostate;lung;frontal lobe;endometrium;larynx;nasopharynx;placenta;visual apparatus;testis;cervix;head and neck;spleen;germinal center;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;medulla oblongata;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.14632 0.12662 -2.125742609 1.509790045 75.39978 1.81746 EPS15P1 . . . epidermal growth factor receptor pathway substrate 15 pseudogene 1 . . . . . . . . . . . EPSTI1 1.3509232083864e-18 0.000378544928644078 0.999621455071356 epithelial stromal interaction 1 (breast) . . TISSUE SPECIFICITY: Highly expressed in placenta, small intestine, spleen, kidney, thymus, liver, salivary gland and testes. Weakly expressed in breast, skeletal muscle and colon. Highly expressed in breast cancer upon interaction between tumor cells and stromal cells in vitro. Expressed in blood mononuclear cells from patients with systemic lupus erythematosus (SLE). {ECO:0000269|PubMed:11991720, ECO:0000269|PubMed:16769699}.; unclassifiable (Anatomical System);smooth muscle;lymph node;cartilage;heart;ovary;colon;parathyroid;skin;bile duct;uterus;pancreas;prostate;lung;endometrium;larynx;nasopharynx;thyroid;placenta;liver;alveolus;testis;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12257 0.07438 0.374860183 75.43052607 2836.67793 10.06668 EPT1 0.347461749547272 0.649702516062555 0.00283573439017278 ethanolaminephosphotransferase 1 FUNCTION: Catalyzes phosphatidylethanolamine biosynthesis from CDP-ethanolamine. It thereby plays a central role in the formation and maintenance of vesicular membranes. Involved in the formation of phosphatidylethanolamine via 'Kennedy' pathway.; . TISSUE SPECIFICITY: Widely expressed. Abundant in brain, placenta, liver and pancreas, followed by heart, skeletal muscle, lung and kidney. In brain it is strongly expressed in cerebellum, followed by the occipital pole and the frontal lobe. {ECO:0000269|PubMed:17132865}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;gum;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; . . . -0.205617011 38.57631517 22.92337 0.76401 EPX 6.21196893270215e-10 0.84549436451461 0.154505634864193 eosinophil peroxidase FUNCTION: Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils. Shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv by inducing bacterial fragmentation and lysis. {ECO:0000269|PubMed:12540536, ECO:0000269|PubMed:18694936}.; DISEASE: Eosinophil peroxidase deficiency (EPXD) [MIM:261500]: A rare abnormality without clinical symptoms characterized by decreased or absent peroxidase activity and decreased volume of the granule matrix in eosinophils. {ECO:0000269|PubMed:7809065}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);blood;thymus;bone marrow; bone marrow; 0.11697 0.27934 1.144514984 92.38617598 3507.58993 11.42105 EPYC 5.0529732963996e-05 0.667576988569896 0.33237248169714 epiphycan FUNCTION: May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization.; . TISSUE SPECIFICITY: Cartilage, ligament, and placenta. {ECO:0000269|PubMed:8975717}.; unclassifiable (Anatomical System);uterus;whole body;cartilage;heart;cochlea;endometrium;bone;placenta;colon;head and neck;skin; dorsal root ganglion;superior cervical ganglion; 0.07211 0.12934 0.507139401 80.10143902 339.71978 3.90903 EQTN 1.33350036518987e-07 0.112070549633681 0.887929317016283 equatorin FUNCTION: Acrosomal membrane-anchored protein involved in the process of fertilization and in acrosome biogenesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is highly expressed in testis. Isoform 2 is expressed at low levels in skin and blood. {ECO:0000269|PubMed:11118625}.; . . 0.03615 0.06376 0.084621747 60.31493277 292.78473 3.65806 ERAL1 1.04173456681738e-06 0.783374197548636 0.216624760716797 Era-like 12S mitochondrial rRNA chaperone 1 FUNCTION: Probable GTPase that plays a role in the mitochondrial ribosomal small subunit assembly. Specifically binds the 12S mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating the 3' terminal stem-loop region. May act as a chaperone that protects the 12S mt-rRNA on the 28S mitoribosomal subunit during ribosomal small subunit assembly. {ECO:0000269|PubMed:20430825, ECO:0000269|PubMed:20604745}.; . . lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex;cerebellum; 0.14956 0.10585 -0.003562597 53.72729417 63.6629 1.63540 ERAP1 9.99009541070118e-18 0.0322790265108296 0.967720973489171 endoplasmic reticulum aminopeptidase 1 FUNCTION: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney. {ECO:0000269|PubMed:15908954, ECO:0000269|PubMed:16286653, ECO:0000269|PubMed:21478864}.; . TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;whole body;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;appendix;pons;trigeminal ganglion; 0.10680 0.11578 1.076540831 91.72564284 6533.99861 17.01375 ERAP2 3.18437372981209e-22 0.00100820887142091 0.998991791128579 endoplasmic reticulum aminopeptidase 2 FUNCTION: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Preferentially hydrolyzes the basic residues Arg and Lys. {ECO:0000269|PubMed:12799365, ECO:0000269|PubMed:15908954, ECO:0000269|PubMed:16286653}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in spleen and leukocytes. {ECO:0000269|PubMed:12799365}.; . . 0.38511 0.14234 0.387604191 75.69591885 909.93603 5.86316 ERAS 0.51999564841992 0.415446201777044 0.0645581498030353 ES cell expressed Ras FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays an important role in the tumor-like growth properties of embryonic stem cells (By similarity). {ECO:0000250}.; . . . . 0.30096 0.17203 -0.075159878 47.78839349 3.31005 0.12091 ERBB2 0.998894657455293 0.00110534254451983 1.87586296395678e-13 erb-b2 receptor tyrosine kinase 2 FUNCTION: Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization.; DISEASE: Hereditary diffuse gastric cancer (HDGC) [MIM:137215]: A cancer predisposition syndrome with increased susceptibility to diffuse gastric cancer. Diffuse gastric cancer is a malignant disease characterized by poorly differentiated infiltrating lesions resulting in thickening of the stomach. Malignant tumors start in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Glioma (GLM) [MIM:137800]: Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Note=Chromosomal aberrations involving ERBB2 may be a cause gastric cancer. Deletions within 17q12 region producing fusion transcripts with CDK12, leading to CDK12-ERBB2 fusion leading to truncated CDK12 protein not in-frame with ERBB2.; TISSUE SPECIFICITY: Expressed in a variety of tumor tissues including primary breast tumors and tumors from small bowel, esophagus, kidney and mouth. {ECO:0000269|PubMed:15380516}.; ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;spinal ganglion;ciliary body;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;muscle;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;placenta;globus pallidus;kidney;trigeminal ganglion; 0.99949 0.89401 -0.5879134 18.28261382 5901.30986 15.94968 ERBB3 4.35825057327711e-06 0.999995500411156 1.41338270817751e-07 erb-b2 receptor tyrosine kinase 3 FUNCTION: Binds and is activated by neuregulins and NTAK. May also be activated by CSPG5. {ECO:0000269|PubMed:15358134}.; DISEASE: Lethal congenital contracture syndrome 2 (LCCS2) [MIM:607598]: A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy, and congenital non-progressive joint contractures (arthrogryposis). The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth. LCCS2 patients manifest craniofacial/ocular findings, lack of hydrops, multiple pterygia, and fractures, as well as a normal duration of pregnancy and a unique feature of a markedly distended urinary bladder (neurogenic bladder defect). The phenotype suggests a spinal cord neuropathic etiology. {ECO:0000269|PubMed:17701904}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Epithelial tissues and brain.; ovary;sympathetic chain;colon;parathyroid;skin;uterus;prostate;optic nerve;endometrium;larynx;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;spinal cord;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;hippocampus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;occipital lobe;olfactory bulb;atrioventricular node;kidney;caudate nucleus;trigeminal ganglion;parietal lobe; 0.98417 0.53106 -0.655870776 16.12408587 704.71886 5.27522 ERBB4 0.999900653614005 9.9346385992574e-05 2.61676785192033e-15 erb-b2 receptor tyrosine kinase 4 FUNCTION: Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins and EGF family members and regulates development of the heart, the central nervous system and the mammary gland, gene transcription, cell proliferation, differentiation, migration and apoptosis. Required for normal cardiac muscle differentiation during embryonic development, and for postnatal cardiomyocyte proliferation. Required for normal development of the embryonic central nervous system, especially for normal neural crest cell migration and normal axon guidance. Required for mammary gland differentiation, induction of milk proteins and lactation. Acts as cell-surface receptor for the neuregulins NRG1, NRG2, NRG3 and NRG4 and the EGF family members BTC, EREG and HBEGF. Ligand binding triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Ligand specificity and signaling is modulated by alternative splicing, proteolytic processing, and by the formation of heterodimers with other ERBB family members, thereby creating multiple combinations of intracellular phosphotyrosines that trigger ligand- and context-specific cellular responses. Mediates phosphorylation of SHC1 and activation of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Isoform JM-A CYT-1 and isoform JM-B CYT-1 phosphorylate PIK3R1, leading to the activation of phosphatidylinositol 3-kinase and AKT1 and protect cells against apoptosis. Isoform JM-A CYT-1 and isoform JM-B CYT-1 mediate reorganization of the actin cytoskeleton and promote cell migration in response to NRG1. Isoform JM-A CYT-2 and isoform JM-B CYT-2 lack the phosphotyrosine that mediates interaction with PIK3R1, and hence do not phosphorylate PIK3R1, do not protect cells against apoptosis, and do not promote reorganization of the actin cytoskeleton and cell migration. Proteolytic processing of isoform JM-A CYT-1 and isoform JM-A CYT-2 gives rise to the corresponding soluble intracellular domains (4ICD) that translocate to the nucleus, promote nuclear import of STAT5A, activation of STAT5A, mammary epithelium differentiation, cell proliferation and activation of gene expression. The ERBB4 soluble intracellular domains (4ICD) colocalize with STAT5A at the CSN2 promoter to regulate transcription of milk proteins during lactation. The ERBB4 soluble intracellular domains can also translocate to mitochondria and promote apoptosis. {ECO:0000269|PubMed:10348342, ECO:0000269|PubMed:10353604, ECO:0000269|PubMed:10358079, ECO:0000269|PubMed:10722704, ECO:0000269|PubMed:10867024, ECO:0000269|PubMed:11178955, ECO:0000269|PubMed:11390655, ECO:0000269|PubMed:12807903, ECO:0000269|PubMed:15534001, ECO:0000269|PubMed:15746097, ECO:0000269|PubMed:16251361, ECO:0000269|PubMed:16778220, ECO:0000269|PubMed:16837552, ECO:0000269|PubMed:17486069, ECO:0000269|PubMed:17638867, ECO:0000269|PubMed:19098003, ECO:0000269|PubMed:20858735, ECO:0000269|PubMed:8383326, ECO:0000269|PubMed:8617750, ECO:0000269|PubMed:9135143, ECO:0000269|PubMed:9168115, ECO:0000269|PubMed:9334263}.; DISEASE: Amyotrophic lateral sclerosis 19 (ALS19) [MIM:615515]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. {ECO:0000269|PubMed:24119685}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at highest levels in brain, heart, kidney, in addition to skeletal muscle, parathyroid, cerebellum, pituitary, spleen, testis and breast. Lower levels in thymus, lung, salivary gland, and pancreas. Isoform JM-A CYT-1 and isoform JM-B CYT-1 are expressed in cerebellum, but only the isoform JM-B is expressed in the heart. {ECO:0000269|PubMed:10353604, ECO:0000269|PubMed:8383326, ECO:0000269|PubMed:9334263}.; unclassifiable (Anatomical System);amygdala;breast;uterus;myocardium;frontal lobe;thyroid;testis;brain;skeletal muscle; amygdala;dorsal root ganglion;medulla oblongata;occipital lobe;superior cervical ganglion;ciliary ganglion;pons;caudate nucleus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.99493 0.40209 -1.969545983 1.786978061 97.59344 2.13593 ERBIN . . . erbb2 interacting protein FUNCTION: Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state (PubMed:16203728). Inhibits NOD2-dependent NF-kappa-B signaling and proinflammatory cytokine secretion (PubMed:16203728). {ECO:0000269|PubMed:10878805, ECO:0000269|PubMed:16203728}.; . TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney, muscle and stomach, followed by liver, spleen and intestine. {ECO:0000269|PubMed:10878805}.; . . 0.44557 0.10863 1.387050485 94.63906582 . . ERC1 0.00412388322590132 0.99587557945178 5.37322318866941e-07 ELKS/RAB6-interacting/CAST family member 1 FUNCTION: Regulatory subunit of the IKK complex. Probably recruits IkappaBalpha/NFKBIA to the complex. May be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. May be involved in vesicle trafficking at the CAZ. May be involved in Rab-6 regulated endosomes to Golgi transport. {ECO:0000269|PubMed:15218148}.; . TISSUE SPECIFICITY: Widely expressed. Isoform 2 and isoform 4 are abundantly expressed in brain. Isoform 1 and isoform 3 are predominantly expressed in testis and thyroid, and isoform 1 predominates in other tissues tested. {ECO:0000269|PubMed:12203787}.; medulla oblongata;colon;choroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;optic nerve;thyroid;testis;amniotic fluid;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;oral cavity;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;macula lutea;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.23552 0.23338 -0.881793075 10.53904223 2042.24706 8.33140 ERC2 0.9968564624658 0.00314353747559091 5.86094808095434e-11 ELKS/RAB6-interacting/CAST family member 2 FUNCTION: Thought to be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. Seems to act together with BSN. May recruit liprin-alpha proteins to the CAZ.; . . unclassifiable (Anatomical System);amygdala;ovary;parathyroid;pancreas;whole body;lung;frontal lobe;placenta;hypopharynx;liver;pituitary gland;testis;head and neck;spleen;brain; whole brain;amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.79983 0.11050 -0.328796968 30.86223166 667.89389 5.16807 ERC2-IT1 . . . ERC2 intronic transcript 1 . . TISSUE SPECIFICITY: Widely expressed.; . . . . . . . . ERCC1 0.000286883321902936 0.793158680717787 0.20655443596031 excision repair cross-complementation group 1 FUNCTION: Isoform 1: Non-catalytic component of a structure- specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. Also required for homology-directed repair (HDR) of DNA double-strand breaks, in conjunction with SLX4.; DISEASE: Cerebro-oculo-facio-skeletal syndrome 4 (COFS4) [MIM:610758]: A disorder of prenatal onset characterized by microcephaly, congenital cataracts, facial dysmorphism, neurogenic arthrogryposis, growth failure and severe psychomotor retardation. COFS is considered to be part of the nucleotide-excision repair disorders spectrum that include also xeroderma pigmentosum, trichothiodystrophy and Cockayne syndrome. {ECO:0000269|PubMed:17273966, ECO:0000269|PubMed:23623389}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;thyroid;bone;iris;testis;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; whole brain;superior cervical ganglion;lung;heart;ciliary ganglion;skeletal muscle; 0.82893 0.70750 -0.358119787 29.16371786 21.98733 0.73946 ERCC2 3.14163491830693e-13 0.25379132024469 0.746208679754995 excision repair cross-complementation group 2 FUNCTION: ATP-dependent 5'-3' DNA helicase, component of the core- TFIIH basal transcription factor. Involved in nucleotide excision repair (NER) of DNA by opening DNA around the damage, and in RNA transcription by RNA polymerase II by anchoring the CDK-activating kinase (CAK) complex, composed of CDK7, cyclin H and MAT1, to the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers. {ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:15494306, ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:8413672}.; DISEASE: Xeroderma pigmentosum complementation group D (XP-D) [MIM:278730]: An autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. The skin develops marked freckling and other pigmentation abnormalities. Some XP-D patients present features of Cockayne syndrome, including cachectic dwarfism, pigmentary retinopathy, ataxia, decreased nerve conduction velocities. The phenotype combining xeroderma pigmentosum and Cockayne syndrome traits is referred to as XP-CS complex. {ECO:0000269|PubMed:11709541, ECO:0000269|PubMed:7585650, ECO:0000269|PubMed:7825573, ECO:0000269|PubMed:7849702, ECO:0000269|PubMed:9101292}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Trichothiodystrophy 1, photosensitive (TTD1) [MIM:601675]: A form of trichothiodystrophy, an autosomal recessive disease characterized by sulfur-deficient brittle hair and multisystem variable abnormalities. The spectrum of clinical features varies from mild disease with only hair involvement to severe disease with cutaneous, neurologic and profound developmental defects. Ichthyosis, intellectual and developmental disabilities, decreased fertility, abnormal characteristics at birth, ocular abnormalities, short stature, and infections are common manifestations. There are both photosensitive and non- photosensitive forms of the disorder. TTD1 patients manifest cutaneous photosensitivity. {ECO:0000269|PubMed:11242112, ECO:0000269|PubMed:7920640, ECO:0000269|PubMed:8571952, ECO:0000269|PubMed:9195225, ECO:0000269|PubMed:9238033, ECO:0000269|PubMed:9758621}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cerebro-oculo-facio-skeletal syndrome 2 (COFS2) [MIM:610756]: A disorder of prenatal onset characterized by microcephaly, congenital cataracts, facial dysmorphism, neurogenic arthrogryposis, growth failure and severe psychomotor retardation. COFS is considered to be part of the nucleotide-excision repair disorders spectrum that include also xeroderma pigmentosum, trichothiodystrophy and Cockayne syndrome. {ECO:0000269|PubMed:11443545}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;myocardium;ovary;colon;parathyroid;choroid;skin;endometrium;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;skeletal muscle;breast;pancreas;lung;placenta;liver;cervix;spleen;stomach; . 0.40797 0.77072 -1.945684699 1.887237556 3745.39177 11.96853 ERCC3 2.05509479327392e-05 0.999757424483124 0.000222024568942779 excision repair cross-complementation group 3 FUNCTION: ATP-dependent 3'-5' DNA helicase, component of the core- TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. Acts by opening DNA either around the RNA transcription start site or the DNA damage. {ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:8157004}.; DISEASE: Xeroderma pigmentosum complementation group B (XP-B) [MIM:610651]: An autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. The skin develops marked freckling and other pigmentation abnormalities. Some XP-B patients present features of Cockayne syndrome, including cachectic dwarfism, pigmentary retinopathy, ataxia, decreased nerve conduction velocities. The phenotype combining xeroderma pigmentosum and Cockayne syndrome traits is referred to as XP-CS complex. {ECO:0000269|PubMed:16947863, ECO:0000269|PubMed:8304337}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Trichothiodystrophy 2, photosensitive (TTD2) [MIM:616390]: A form of trichothiodystrophy, an autosomal recessive disease characterized by sulfur-deficient brittle hair and multisystem variable abnormalities. The spectrum of clinical features varies from mild disease with only hair involvement to severe disease with cutaneous, neurologic and profound developmental defects. Ichthyosis, intellectual and developmental disabilities, decreased fertility, abnormal characteristics at birth, ocular abnormalities, short stature, and infections are common manifestations. There are both photosensitive and non- photosensitive forms of the disorder. {ECO:0000269|PubMed:9012405}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;oesophagus;synovium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis;ciliary ganglion;atrioventricular node;cingulate cortex; 0.72446 0.26840 -1.284117362 5.113234253 87.85755 2.00291 ERCC4 3.33157717442271e-10 0.733032262337526 0.266967737329316 excision repair cross-complementation group 4 FUNCTION: Catalytic component of a structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link. {ECO:0000269|PubMed:19596235}.; DISEASE: Xeroderma pigmentosum complementation group F (XP-F) [MIM:278760]: An autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. The skin develops marked freckling and other pigmentation abnormalities. XP-F patients show a mild phenotype. {ECO:0000269|PubMed:8797827, ECO:0000269|PubMed:9579555, ECO:0000269|PubMed:9580660}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: XFE progeroid syndrome (XFEPS) [MIM:610965]: A syndrome characterized by aged bird-like facies, lack of subcutaneous fat, dwarfism, cachexia and microcephaly. Additional features include sun-sensitivity from birth, learning disabilities, hearing loss, and visual impairment. {ECO:0000269|PubMed:17183314}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Xeroderma pigmentosum type F/Cockayne syndrome (XPF/CS) [MIM:278760]: A variant form of Cockayne syndrome, a disorder characterized by growth retardation, microcephaly, impairment of nervous system development, pigmentary retinopathy, peculiar facies, and progeria together with abnormal skin photosensitivity. Cockayne syndrome dermatological features are milder than those in xeroderma pigmentosum and skin cancers are not found in affected individuals. XPF/CS patients, however, present with severe skin phenotypes, including severe photosensitivity, abnormal skin pigmentation, and skin cancer predisposition. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Fanconi anemia complementation group Q (FANCQ) [MIM:615272]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:23623386, ECO:0000269|PubMed:24027083}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;ovary;adrenal cortex;colon;parathyroid;lens;skin;skeletal muscle;breast;uterus;prostate;optic nerve;whole body;adrenal gland;bone;thyroid;placenta;liver;testis;spleen;germinal center;kidney;brain;pineal gland; superior cervical ganglion; 0.84260 0.47836 -0.367438677 28.29087049 549.8051 4.76877 ERCC5 4.64770040217028e-06 0.999615771202756 0.000379581096842021 excision repair cross-complementation group 5 FUNCTION: Single-stranded structure-specific DNA endonuclease involved in DNA excision repair. Makes the 3'incision in DNA nucleotide excision repair (NER). Acts as a cofactor for a DNA glycosylase that removes oxidized pyrimidines from DNA. May also be involved in transcription-coupled repair of this kind of damage, in transcription by RNA polymerase II, and perhaps in other processes too.; DISEASE: Xeroderma pigmentosum complementation group G (XP-G) [MIM:278780]: An autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. The skin develops marked freckling and other pigmentation abnormalities. Some XP-G patients present features of Cockayne syndrome, cachectic dwarfism, pigmentary retinopathy, ataxia, decreased nerve conduction velocities. The phenotype combining xeroderma pigmentosum and Cockayne syndrome traits is referred to as XP-CS complex. {ECO:0000269|PubMed:11228268, ECO:0000269|PubMed:11841555, ECO:0000269|PubMed:12060391, ECO:0000269|PubMed:7951246, ECO:0000269|PubMed:9096355}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;synovium;bone;thyroid;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; pancreas;trigeminal ganglion;cingulate cortex; 0.08139 0.49343 0.547404288 81.13352206 2484.51011 9.30163 ERCC6 5.00691675988158e-13 0.9992610992513 0.000738900748198946 excision repair cross-complementation group 6 FUNCTION: Essential factor involved in transcription-coupled nucleotide excision repair which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. It is required for transcription-coupled repair complex formation. It recruits the CSA complex (DCX(ERCC8) complex), nucleotide excision repair proteins and EP300 to the at sites of RNA polymerase II- blocking lesions. {ECO:0000269|PubMed:15548521, ECO:0000269|PubMed:16916636, ECO:0000269|PubMed:20541997}.; DISEASE: Cockayne syndrome B (CSB) [MIM:133540]: A rare disorder characterized by cutaneous sensitivity to sunlight, abnormal and slow growth, cachectic dwarfism, progeroid appearance, progressive pigmentary retinopathy and sensorineural deafness. There is delayed neural development and severe progressive neurologic degeneration resulting in mental retardation. Two clinical forms are recognized: in the classical form or Cockayne syndrome type 1, the symptoms are progressive and typically become apparent within the first few years or life; the less common Cockayne syndrome type 2 is characterized by more severe symptoms that manifest prenatally. Cockayne syndrome shows some overlap with certain forms of xeroderma pigmentosum. Unlike xeroderma pigmentosum, patients with Cockayne syndrome do not manifest increased freckling and other pigmentation abnormalities in the skin and have no significant increase in skin cancer. {ECO:0000269|PubMed:19894250, ECO:0000269|PubMed:9443879}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cerebro-oculo-facio-skeletal syndrome 1 (COFS1) [MIM:214150]: A disorder of prenatal onset characterized by microcephaly, congenital cataracts, facial dysmorphism, neurogenic arthrogryposis, growth failure and severe psychomotor retardation. COFS is considered to be part of the nucleotide-excision repair disorders spectrum that include also xeroderma pigmentosum, trichothiodystrophy and Cockayne syndrome. {ECO:0000269|PubMed:19894250}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: De Sanctis-Cacchione syndrome (DSC) [MIM:278800]: An autosomal recessive syndrome consisting of xeroderma pigmentosum associated with severe neurological and developmental involvement. In addition to the clinical signs of xeroderma pigmentosum, patients present with mental retardation, dwarfism, gonadal hypoplasia, microcephaly and various neurologic complications of early onset. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Macular degeneration, age-related, 5 (ARMD5) [MIM:613761]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. {ECO:0000269|PubMed:16754848}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: UV-sensitive syndrome 1 (UVSS1) [MIM:600630]: An autosomal recessive disorder characterized by cutaneous photosensitivity and mild freckling in the absence of neurological abnormalities or skin tumors. {ECO:0000269|PubMed:15486090}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymphoreticular;lung;testis;colon;blood;skeletal muscle;bone marrow; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle;skin; . 0.46867 1.486276519 95.32318943 3542.12652 11.48622 ERCC6-PGBD3 2.07309895414368e-06 0.994098820471301 0.00589910642974454 ERCC6-PGBD3 readthrough . . . . . . . . . 54.30276 1.47186 ERCC6L 0.986827393517475 0.0131714436515484 1.16283097661227e-06 excision repair cross-complementation group 6 like FUNCTION: DNA helicase that acts as an essential component of the spindle assembly checkpoint. Contributes to the mitotic checkpoint by recruiting MAD2 to kinetochores and monitoring tension on centromeric chromatin. Acts as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. {ECO:0000269|PubMed:17218258}.; . . unclassifiable (Anatomical System);ovary;fovea centralis;choroid;lens;skin;skeletal muscle;retina;bone marrow;uterus;breast;optic nerve;whole body;lung;epididymis;bone;macula lutea;liver;germinal center;kidney; superior cervical ganglion;testis - interstitial;atrioventricular node;skeletal muscle; 0.33669 0.09735 -0.176292081 40.56381222 110.04424 2.27878 ERCC6L2 0.00155590713206106 0.99817971528977 0.000264377578169412 excision repair cross-complementation group 6 like 2 FUNCTION: May be involved in early DNA damage response. {ECO:0000269|PubMed:24507776}.; DISEASE: Bone marrow failure syndrome 2 (BMFS2) [MIM:615715]: An autosomal recessive disorder characterized by trilineage bone marrow failure, bone marrow hypocellularity, learning difficulties, and microcephaly. Insufficient hematopoiesis results in peripheral blood cytopenias, affecting myeloid, erythroid and megakaryocyte lines. Cutaneous features and increased chromosome breakage are not features. {ECO:0000269|PubMed:24507776}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in bone marrow (at protein level). {ECO:0000269|PubMed:24507776}.; . . 0.06219 0.08403 . . 3928.7793 12.38630 ERCC8 8.5728345941739e-09 0.281056490796018 0.718943500631148 excision repair cross-complementation group 8 FUNCTION: Substrate-recognition component of the CSA complex, a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, involved in transcription-coupled nucleotide excision repair. The CSA complex (DCX(ERCC8) complex) promotes the ubiquitination and subsequent proteasomal degradation of ERCC6 in a UV-dependent manner; ERCC6 degradation is essential for the recovery of RNA synthesis after transcription-coupled repair. It is required for the recruitment of XAB2, HMGN1 and TCEA1/TFIIS to a transcription- coupled repair complex which removes RNA polymerase II-blocking lesions from the transcribed strand of active genes. {ECO:0000269|PubMed:16751180, ECO:0000269|PubMed:16916636, ECO:0000269|PubMed:16964240}.; DISEASE: Cockayne syndrome A (CSA) [MIM:216400]: A rare disorder characterized by cutaneous sensitivity to sunlight, abnormal and slow growth, cachectic dwarfism, progeroid appearance, progressive pigmentary retinopathy and sensorineural deafness. There is delayed neural development and severe progressive neurologic degeneration resulting in mental retardation. Two clinical forms are recognized: in the classical form or Cockayne syndrome type 1, the symptoms are progressive and typically become apparent within the first few years or life; the less common Cockayne syndrome type 2 is characterized by more severe symptoms that manifest prenatally. Cockayne syndrome shows some overlap with certain forms of xeroderma pigmentosum. Unlike xeroderma pigmentosum, patients with Cockayne syndrome do not manifest increased freckling and other pigmentation abnormalities in the skin and have no significant increase in skin cancer. {ECO:0000269|PubMed:14661080, ECO:0000269|PubMed:15744458, ECO:0000269|PubMed:19894250}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: UV-sensitive syndrome 2 (UVSS2) [MIM:614621]: An autosomal recessive disorder characterized by cutaneous photosensitivity and mild freckling in the absence of neurological abnormalities or skin tumors. {ECO:0000269|PubMed:19329487}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;muscle;colon;parathyroid;skin;skeletal muscle;bone marrow;bile duct;pancreas;whole body;lung;nasopharynx;placenta;testis;kidney;brain;pineal gland;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion; 0.47975 0.18568 -0.534490515 20.70063694 1298.26823 6.78011 ERCM1 . . . excision repair complementing defective repair in mouse cells . . . . . . . . . . . ERDA1 . . . expanded repeat domain, CAG/CTG 1 . . . . . . . . . . . EREG 0.00040011069339593 0.633453519906714 0.36614636939989 epiregulin FUNCTION: Ligand of the EGF receptor/EGFR and ERBB4. Stimulates EGFR and ERBB4 tyrosine phosphorylation (PubMed:9419975). Contributes to inflammation, wound healing, tissue repair, and oocyte maturation by regulating angiogenesis and vascular remodeling and by stimulating cell proliferation (PubMed:24631357). {ECO:0000269|PubMed:9419975, ECO:0000303|PubMed:24631357}.; . TISSUE SPECIFICITY: In normal adults, expressed predominantly in the placenta and peripheral blood leukocytes. High levels were detected in carcinomas of the bladder, lung, kidney and colon. {ECO:0000269|PubMed:9337852}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;heart;colon;blood;skeletal muscle;skin;uterus;lung;liver;brain;stomach; superior cervical ganglion; 0.35931 0.43067 0.104848986 61.49445624 46.83269 1.32239 ERF 0.807144401200279 0.19263934990826 0.000216248891461343 ETS2 repressor factor FUNCTION: Potent transcriptional repressor that binds to the H1 element of the Ets2 promoter. May regulate other genes involved in cellular proliferation. Required for extraembryonic ectoderm differentiation, ectoplacental cone cavity closure, and chorioallantoic attachment (By similarity). May be important for regulating trophoblast stem cell differentiation (By similarity). {ECO:0000250}.; DISEASE: Craniosynostosis 4 (CRS4) [MIM:600775]: A primary abnormality of skull growth involving premature fusion of one or more cranial sutures. The growth velocity of the skull often cannot match that of the developing brain resulting in an abnormal head shape and, in some cases, increased intracranial pressure, which must be treated promptly to avoid permanent neurodevelopmental disability. {ECO:0000269|PubMed:23354439}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest levels in testis, ovary, pancreas, and heart. {ECO:0000269|PubMed:9192842}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;ciliary ganglion; 0.63786 0.13887 -0.424258538 25.56027365 41.74458 1.21591 ERG 0.968344473919641 0.0316454202533152 1.01058270439903e-05 v-ets avian erythroblastosis virus E26 oncogene homolog FUNCTION: Transcriptional regulator. May participate in transcriptional regulation through the recruitment of SETDB1 histone methyltransferase and subsequent modification of local chromatin structure.; DISEASE: Ewing sarcoma (ES) [MIM:612219]: A highly malignant, metastatic, primitive small round cell tumor of bone and soft tissue that affects children and adolescents. It belongs to the Ewing sarcoma family of tumors, a group of morphologically heterogeneous neoplasms that share the same cytogenetic features. They are considered neural tumors derived from cells of the neural crest. Ewing sarcoma represents the less differentiated form of the tumors. {ECO:0000269|PubMed:8076344}. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving ERG has been found in patients with Erwing sarcoma. Translocation t(21;22)(q22;q12) with EWSR1. {ECO:0000269|PubMed:8076344}.; DISEASE: Note=Chromosomal aberrations involving ERG have been found in acute myeloid leukemia (AML). Translocation t(16;21)(p11;q22) with FUS (PubMed:8187069). Translocation t(X;21)(q25-26;q22) with ELF4 (PubMed:16303180). {ECO:0000269|PubMed:16303180, ECO:0000269|PubMed:8187069}.; . ovary;salivary gland;intestine;colon;vein;skin;bone marrow;uterus;prostate;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pharynx;blood;skeletal muscle;lung;cornea;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.23165 0.30312 -0.602450568 17.91106393 22.18834 0.74473 ERGIC1 0.714836766400926 0.284497724642849 0.000665508956224928 endoplasmic reticulum-golgi intermediate compartment 1 FUNCTION: Possible role in transport between endoplasmic reticulum and Golgi. {ECO:0000303|PubMed:15308636}.; . . unclassifiable (Anatomical System);ovary;adrenal cortex;colon;parathyroid;uterus;bile duct;pancreas;prostate;lung;larynx;thyroid;placenta;visual apparatus;liver;testis;head and neck;kidney;spinal ganglion;brain;pineal gland;mammary gland;tonsil; dorsal root ganglion;prostate;superior cervical ganglion;liver;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cerebellum; 0.29044 0.12142 -0.359940251 28.93371078 23.12846 0.77117 ERGIC2 0.320357206097489 0.678925091693622 0.000717702208889601 ERGIC and golgi 2 FUNCTION: Possible role in transport between endoplasmic reticulum and Golgi. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11445006}.; smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;artery;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;skeletal muscle;breast;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;liver;cervix;kidney;mammary gland;stomach;aorta;thymus; testis - interstitial;cingulate cortex; 0.84052 0.08503 -0.339715008 30.06605331 9.56131 0.35232 ERGIC3 0.0038590767192969 0.994404724007987 0.00173619927271599 ERGIC and golgi 3 FUNCTION: Possible role in transport between endoplasmic reticulum and Golgi. {ECO:0000250}.; . . myocardium;medulla oblongata;smooth muscle;ovary;rectum;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;iris;germinal center;brain;heart;nervous;pineal body;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;duodenum;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;adrenal gland;testis;atrioventricular node;kidney;pons;trigeminal ganglion;skeletal muscle; 0.29981 0.10239 -0.404032746 26.53338051 12.39957 0.44974 ERH 0.846059923578033 0.151203542420548 0.00273653400141921 enhancer of rudimentary homolog (Drosophila) FUNCTION: May have a role in the cell cycle.; . TISSUE SPECIFICITY: Expressed in all tissues examined. {ECO:0000269|PubMed:8786099}.; myocardium;lymphoreticular;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; prefrontal cortex;testis;tumor; 0.74643 0.18619 0.101211609 60.95777306 . . ERHP1 . . . enhancer of rudimentary homolog (Drosophila) pseudogene 1 . . . . . . . . . . . ERHP2 . . . enhancer of rudimentary homolog (Drosophila) pseudogene 2 . . . . . . . . . . . ERI1 0.000454685197816091 0.867074884872607 0.132470429929576 exoribonuclease 1 FUNCTION: RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA. Binds with high affinity to the stem-loop structure of replication- dependent histone pre-mRNAs. {ECO:0000269|PubMed:14536070, ECO:0000269|PubMed:16912046}.; . . colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;lens;skeletal muscle;lung;adrenal gland;placenta;visual apparatus;macula lutea;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;thalamus;testis - seminiferous tubule;ciliary ganglion;caudate nucleus;atrioventricular node;trigeminal ganglion; 0.16343 0.08222 -0.159704656 41.90846898 74.0924 1.79860 ERI2 6.38834089545038e-05 0.717244337365027 0.282691779226019 ERI1 exoribonuclease family member 2 . . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;whole body;cochlea;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;skeletal muscle;breast;lung;placenta;liver;spleen;cervix;kidney;mammary gland;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.22979 0.07048 1.596607091 95.87166785 1931.68541 8.08737 ERI3 0.129756091189771 0.865497552890986 0.00474635591924324 ERI1 exoribonuclease family member 3 . . . . . 0.29101 0.10507 -0.339715008 30.06605331 7.02644 0.26389 ERI3-IT1 . . . ERI3 intronic transcript 1 . . . . . . . . . . . ERICD . . . E2F1-regulated inhibitor of cell death (non-protein coding) . . . . . . . . . . . ERICH1 1.38646429216599e-10 0.0279713726206213 0.972028627240732 glutamate rich 1 . . . myocardium;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;skeletal muscle;lung;cornea;placenta;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;testis;atrioventricular node; 0.06769 0.07517 0.07167258 59.15899976 140.672 2.58786 ERICH1-AS1 . . . ERICH1 antisense RNA 1 . . . . . . . . . . . ERICH2 . . . glutamate rich 2 . . . . . . . . . 42.70427 1.23948 ERICH3 . . . glutamate rich 3 . . . . . 0.15022 . 2.043117123 97.75300778 . . ERICH3-AS1 . . . ERICH3 antisense RNA 1 . . . . . . . . . . . ERICH4 . . . glutamate rich 4 . . . . . . . . . . . ERICH5 . . . glutamate rich 5 . . . . . 0.03155 . 0.817616644 87.95116773 . . ERICH6 . . . glutamate rich 6 . . . . . 0.11078 . 1.822581424 97.02170323 . . ERICH6-AS1 . . . ERICH6 antisense RNA 1 . . . . . . . . . . . ERICH6B . . . glutamate rich 6B . . . . . . . 2.710287147 98.93842887 . . ERLEC1 0.000679063416474332 0.995056886922254 0.00426404966127196 endoplasmic reticulum lectin 1 FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. {ECO:0000269|PubMed:16531414, ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18502753}.; . . medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;kidney;stomach;cerebellum; superior cervical ganglion;testis - interstitial;testis;globus pallidus;ciliary ganglion;skeletal muscle; 0.39225 0.10625 -0.690637458 15.12149092 592.52283 4.93296 ERLEC1P1 . . . endoplasmic reticulum lectin 1 pseudogene 1 . . . . . . . . . . . ERLIN1 0.931709473902675 0.0682211462343103 6.93798630143403e-05 ER lipid raft associated 1 FUNCTION: Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. Binds cholesterol and may promote ER retention of the SCAP-SREBF complex (PubMed:24217618). {ECO:0000269|PubMed:19240031, ECO:0000269|PubMed:24217618}.; . TISSUE SPECIFICITY: Expressed in heart, placenta, liver, kidney, pancreas, prostate, testis, ovary and small intestine. {ECO:0000269|PubMed:11118313}.; . . 0.35424 0.10225 -0.139478553 43.29440906 1529.31629 7.26540 ERLIN2 0.111582004871944 0.882241733342704 0.00617626178535191 ER lipid raft associated 2 FUNCTION: Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs) such as ITPR1 (PubMed:19240031, PubMed:17502376). Promotes sterol-accelerated ERAD of HMGCR probably implicating an AMFR/gp78-containing ubiquitin ligase complex (PubMed:21343306). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. May promote ER retention of the SCAP-SREBF complex (PubMed:24217618). {ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:19240031, ECO:0000269|PubMed:21343306, ECO:0000269|PubMed:24217618}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10449903}.; unclassifiable (Anatomical System);smooth muscle;heart;ovary;islets of Langerhans;adrenal cortex;colon;blood;retina;bone marrow;breast;pancreas;prostate;lung;endometrium;bone;placenta;duodenum;liver;testis;spleen;kidney;brain;spinal ganglion; dorsal root ganglion;superior cervical ganglion;thyroid;trigeminal ganglion;skeletal muscle; 0.32262 0.11600 -0.494039303 22.09247464 11.05451 0.40051 ERMAP 5.8055284133168e-05 0.889182912080922 0.110759032634945 erythroblast membrane associated protein (Scianna blood group) FUNCTION: Possible role as a cell-adhesion or receptor molecule of erythroid cells.; . TISSUE SPECIFICITY: Expressed in erythroid-enriched bone marrow (at protein level). Highly expressed in bone marrow and to a lower extent in leukocytes, thymus, lymph node and spleen. {ECO:0000269|PubMed:11549310, ECO:0000269|PubMed:11783959}.; unclassifiable (Anatomical System);heart;cartilage;pineal body;adrenal cortex;colon;skin;uterus;breast;lung;placenta;bone;liver;testis;kidney;brain; fetal liver;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.36694 . 0.666922772 84.64260439 543.71214 4.74487 ERMARD 5.17462949024395e-10 0.815863864295328 0.184136135187209 ER membrane-associated RNA degradation FUNCTION: May play a role in neuronal migration during embryonic development. {ECO:0000269|PubMed:24056535}.; DISEASE: Periventricular nodular heterotopia 6 (PVNH6) [MIM:615544]: A form of periventricular nodular heterotopia, a disorder resulting from a defect in the pattern of neuronal migration in which ectopic collections of neurons lie along the lateral ventricles of the brain or just beneath, contiguously or in isolated patches. PVNH6 results in delayed psychomotor development, delayed speech, strabismus, and onset of seizures with hypsarrhythmia in early infancy. {ECO:0000269|PubMed:24056535}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.15772 0.09330 1.42749112 94.99292286 732.7048 5.37282 ERMN 0.00310152547649555 0.81842746184519 0.178471012678315 ermin FUNCTION: Plays a role in cytoskeletal rearrangements during the late wrapping and/or compaction phases of myelinogenesis as well as in maintenance and stability of myelin sheath in the adult. May play an important role in late-stage oligodendroglia maturation, myelin/Ranvier node formation during CNS development, and in the maintenance and plasticity of related structures in the mature CNS (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in adult and fetal brain. Expressed at intermediate levels in the lung and liver. {ECO:0000269|PubMed:10574461}.; . . 0.09303 0.08320 0.637604436 83.77565464 28.41309 0.90939 ERMP1 4.54996963090227e-05 0.998228721896326 0.00172577840736499 endoplasmic reticulum metallopeptidase 1 FUNCTION: Within the ovary, required for the organization of somatic cells and oocytes into discrete follicular structures. {ECO:0000250|UniProtKB:Q6UPR8}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;thyroid;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion; 0.17248 0.09494 -1.03976177 7.802547771 243.10681 3.36551 ERN1 0.91361398180331 0.0863858055991904 2.1259749930798e-07 endoplasmic reticulum to nucleus signaling 1 FUNCTION: Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices XBP1 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator and triggering growth arrest and apoptosis. {ECO:0000250|UniProtKB:Q9EQY0, ECO:0000269|PubMed:11175748, ECO:0000269|PubMed:12637535, ECO:0000269|PubMed:9637683}.; . TISSUE SPECIFICITY: Ubiquitously expressed. High levels observed in pancreatic tissue. {ECO:0000269|PubMed:9637683}.; . . 0.17946 0.31077 -0.43902969 24.63434772 364.03468 4.03820 ERN2 1.79313065351506e-15 0.517166147833857 0.482833852166141 endoplasmic reticulum to nucleus signaling 2 FUNCTION: Induces translational repression through 28S ribosomal RNA cleavage in response to ER stress. Pro-apoptotic. Appears to play no role in the unfolded-protein response, unlike closely related proteins. {ECO:0000269|PubMed:11175748}.; . . unclassifiable (Anatomical System);pancreas;lung;colon;stomach; superior cervical ganglion;trachea;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.37292 0.11979 -1.697674421 2.583156405 1512.87602 7.22771 ERO1A . . . endoplasmic reticulum oxidoreductase alpha FUNCTION: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. {ECO:0000269|PubMed:10671517, ECO:0000269|PubMed:10970843, ECO:0000269|PubMed:11707400, ECO:0000269|PubMed:12403808, ECO:0000269|PubMed:18833192, ECO:0000269|PubMed:18971943, ECO:0000269|PubMed:23027870}.; . TISSUE SPECIFICITY: Widely expressed at low level. Expressed at high level in upper digestive tract. Highly expressed in esophagus. Weakly expressed in stomach and duodenum. {ECO:0000269|PubMed:10818100}.; . . 0.24339 0.12942 -0.404032746 26.53338051 . . ERO1B . . . endoplasmic reticulum oxidoreductase beta FUNCTION: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Other protein disulfide isomerase family members can also be reoxidized, but at lower rates compared to P4HB, including PDIA2 (50% of P4HB reoxidation rate), as well as PDIA3, PDIA4, PDIA6 and NXNDC12 (<10%). Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. May be involved in oxidative proinsulin folding in pancreatic cells, hence may play a role in glucose homeostasis. {ECO:0000269|PubMed:11707400, ECO:0000269|PubMed:21091435}.; . TISSUE SPECIFICITY: Highly expressed in the digestive tract, including the duodenum and lower digestive tract. In the stomach, highly expressed in enzyme-producing chief cells (at protein level). In the pancreas, expressed in islets of Langerhans and, at lower levels, in enzyme-secreting cells (at protein level). Detected at low level in many other tissues. {ECO:0000269|PubMed:10818100, ECO:0000269|PubMed:16012172}.; . . 0.15697 . 0.751474114 86.64779429 . . ERP27 1.10529479333454e-07 0.100851006843075 0.899148882627446 endoplasmic reticulum protein 27 . . . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;blood;uterus;pancreas;lung;endometrium;bone;thyroid;placenta;liver;spleen;cervix;germinal center;kidney;stomach; pancreas;atrioventricular node;skeletal muscle; 0.08713 0.07858 -0.049474214 50.01179523 141.86947 2.59956 ERP29 0.470649236214131 0.505089877334398 0.024260886451471 endoplasmic reticulum protein 29 FUNCTION: Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER.; . TISSUE SPECIFICITY: Ubiquitous. Mostly expressed in secretory tissues.; ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;amniotic fluid;bladder;brain;tonsil;heart;cartilage;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;liver;white blood cells; 0.09406 0.19858 -0.137658575 43.57159707 123.78234 2.42145 ERP29P1 . . . endoplasmic reticulum lumenal protein 29 pseudogene 1 . . . . . . . . . . . ERP44 0.956751213284096 0.0432443351080704 4.45160783389168e-06 endoplasmic reticulum protein 44 FUNCTION: Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1A and ERO1B in the endoplasmic reticulum. {ECO:0000269|PubMed:11847130, ECO:0000269|PubMed:14517240}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.13873 0.13430 -0.073340031 48.11866006 28.07485 0.90091 ERRFI1 0.046551582399882 0.928881632248865 0.0245667853512532 ERBB receptor feedback inhibitor 1 FUNCTION: Negative regulator of EGFR signaling in skin morphogenesis. Acts as a negative regulator for several EGFR family members, including ERBB2, ERBB3 and ERBB4. Inhibits EGFR catalytic activity by interfering with its dimerization. Inhibits autophosphorylation of EGFR, ERBB2 and ERBB4. Important for normal keratinocyte proliferation and differentiation. Plays a role in modulating the response to steroid hormones in the uterus. Required for normal response to progesterone in the uterus and for fertility. Mediates epithelial estrogen responses in the uterus by regulating ESR1 levels and activation. Important for regulation of endometrium cell proliferation. Important for normal prenatal and perinatal lung development (By similarity). {ECO:0000250}.; . . . . 0.34109 0.21670 0.352813824 74.49280491 351.33398 3.97230 ERV3-1 4.31444689510584e-07 0.373833950922049 0.626165617633262 endogenous retrovirus group 3 member 1 FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its fusogenic properties. It can inhibit cell growth through decrease expression of cyclin B1 and increased expression of p21 in vitro. {ECO:0000269|PubMed:10692254, ECO:0000269|PubMed:14557543, ECO:0000269|PubMed:7645262}.; FUNCTION: TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at higher level in adrenal, sebaceous glands and placenta. Expressed at lower level in bone marrow, brain, breast, colon, heart, kidney, liver, lung, ovary, PBL, prostate, skin, spleen, testis, thymus, thyroid, trachea. {ECO:0000269|PubMed:12970426}.; . . . . 1.940150696 97.52300071 2816.57142 10.01067 ERV3-2 . . . endogenous retrovirus group 3 member 2 . . . . . . . . . . . ERV9-1 . . . endogenous retrovirus group 9 member 1 . . . . . . . . . . . ERV18-1 . . . endogenous retrovirus group 18 member 1 . . . . . . . . . . . ERVE-1 . . . endogenous retrovirus group E member 1 . . . . . . . . . . . ERVE-2 . . . endogenous retrovirus group E member 2 . . . . . . . . . . . ERVE-3 . . . endogenous retrovirus group E member 3 . . . . . . . . . . . ERVE-4 . . . endogenous retrovirus group E member 4 . . . . . . . . . . . ERVFC1-1 . . . endogenous retrovirus group FC1 member 1 FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties. {ECO:0000269|PubMed:14557543}.; . TISSUE SPECIFICITY: Low expression in skin and testis. {ECO:0000269|PubMed:12970426}.; . . . . . . . . ERVFH21-1 . . . endogenous retrovirus group FH21 member 1 . . . . . . . . . . . ERVFRD-1 0.00242834562362554 0.927902061030775 0.0696695933455998 endogenous retrovirus group FRD member 1 FUNCTION: This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. The interaction with MFSD2A is apparently important for this process (PubMed:18988732). {ECO:0000269|PubMed:18988732}.; . TISSUE SPECIFICITY: Expressed at higher level in placenta. Expressed at lower level in adrenal, bone marrow, brain, breast, colon, kidney, lung, ovary, peripheral blood lymphocytes, prostate, skin, spleen, testis, thymus, thyroid, trachea. {ECO:0000269|PubMed:12970426}.; . . . . -0.203796826 38.81811748 28.45838 0.91131 ERVFRD-2 . . . endogenous retrovirus group FRD member 2 . . . . . . . . . . . ERVFRD-3 . . . endogenous retrovirus group FRD member 3 . . . . . . . . . . . ERVH-1 . . . endogenous retrovirus group H member 1 . . . . . . . . . . . ERVH-2 . . . endogenous retrovirus group H member 2 . . . . . . . . . . . ERVH-3 . . . endogenous retrovirus group H member 3 . . . . . . . . . . . ERVH-4 . . . endogenous retrovirus group H member 4 . . . . . . . . . . . ERVH-5 . . . endogenous retrovirus group H member 5 . . . . . . . . . . . ERVH-6 . . . endogenous retrovirus group H member 6 . . . . . . . . . . . ERVH-7 . . . endogenous retrovirus group H member 7 . . . . . . . . . . . ERVH48-1 . . . endogenous retrovirus group 48 member 1 FUNCTION: May play a role in trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development. May negatively regulate cell-cell fusion by interacting with SLC1A5, the probable receptor on the cell surface of the fusogenic syncytin-1/ERVW-1. {ECO:0000269|PubMed:23492904}.; . TISSUE SPECIFICITY: Specifically expressed in placenta by extravillous trophoblasts and syncytiotrophoblasts (at protein level). {ECO:0000269|PubMed:23492904}.; . . . . . . . . ERVI-1 . . . endogenous retrovirus group I member 1 . . . . . . . . . . . ERVK-1 . . . endogenous retrovirus group K member 1 . . . . . . . . . . . ERVK-2 . . . endogenous retrovirus group K member 2 . . . . . . . . . . . ERVK-3 . . . endogenous retrovirus group K member 3 . . . . . . . . . . . ERVK-4 . . . endogenous retrovirus group K member 4 . . . . . . . . . . . ERVK-5 . . . endogenous retrovirus group K member 5 FUNCTION: May possess a function in tumorigenesis. {ECO:0000250}.; . . . . 0.26846 . . . . . ERVK-6 . . . endogenous retrovirus group K member 6 FUNCTION: Retroviral replication requires the nuclear export and translation of unspliced, singly-spliced and multiply-spliced derivatives of the initial genomic transcript. Rec interacts with a highly structured RNA element (RcRE) present in the viral 3'LTR and recruits the cellular nuclear export machinery. This permits export to the cytoplasm of unspliced genomic or incompletely spliced subgenomic viral transcripts. {ECO:0000269|PubMed:10516058, ECO:0000269|PubMed:10557333, ECO:0000269|PubMed:10980608, ECO:0000269|PubMed:11000203, ECO:0000269|PubMed:11105755, ECO:0000269|PubMed:11581404}.; . TISSUE SPECIFICITY: Expressed at higher level in placenta, expressed at lower level in several organs and cell lines. {ECO:0000269|PubMed:12083821}.; . . . . . . . . ERVK-7 . . . endogenous retrovirus group K member 7 FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution.; FUNCTION: TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in lung, placenta, testis and peripheral blood lymphocytes. {ECO:0000269|PubMed:11401426}.; . . . . . . . . ERVK-8 . . . endogenous retrovirus group K member 8 FUNCTION: Retroviral replication requires the nuclear export and translation of unspliced, singly-spliced and multiply-spliced derivatives of the initial genomic transcript. Rec interacts with a highly structured RNA element (RcRE) present in the viral 3'LTR and recruits the cellular nuclear export machinery. This permits export to the cytoplasm of unspliced genomic or incompletely spliced subgenomic viral transcripts (By similarity). {ECO:0000250}.; . . . . . . . . . . ERVK-9 . . . endogenous retrovirus group K member 9 FUNCTION: Retroviral replication requires the nuclear export and translation of unspliced, singly-spliced and multiply-spliced derivatives of the initial genomic transcript. Rec interacts with a highly structured RNA element (RcRE) present in the viral 3'LTR and recruits the cellular nuclear export machinery. This permits export to the cytoplasm of unspliced genomic or incompletely spliced subgenomic viral transcripts (By similarity). {ECO:0000250}.; . . . . . . . . . . ERVK-10 . . . endogenous retrovirus group K member 10 FUNCTION: Retroviral proteases have roles in processing of the primary translation products and the maturation of the viral particle. Endogenous Pro proteins may have kept, lost or modified their original function during evolution. This endogenous protein has retained most of the characteristics of retroviral proteases.; . . . . . . . . . . ERVK-11 . . . endogenous retrovirus group K member 11 FUNCTION: Early post-infection, the reverse transcriptase converts the viral RNA genome into double-stranded viral DNA. The RNase H domain of the reverse transcriptase performs two functions. It degrades the RNA template and specifically removes the RNA primer from the RNA/DNA hybrid. Following nuclear import, the integrase catalyzes the insertion of the linear, double-stranded viral DNA into the host cell chromosome. Endogenous Pol proteins may have kept, lost or modified their original function during evolution (By similarity). {ECO:0000250}.; . . . . . . . . . . ERVK-12 . . . endogenous retrovirus group K member 12 . . . . . . . . . . . ERVK-13 . . . endogenous retrovirus group K member 13 . . . . . . . . . . . ERVK-14 . . . endogenous retrovirus group K member 14 . . . . . . . . . . . ERVK-15 . . . endogenous retrovirus group K member 15 . . . . . . . . . . . ERVK-16 . . . endogenous retrovirus group K member 16 FUNCTION: Retroviral replication requires the nuclear export and translation of unspliced, singly-spliced and multiply-spliced derivatives of the initial genomic transcript. Rec interacts with a highly structured RNA element (RcRE) present in the viral 3'LTR and recruits the cellular nuclear export machinery. This permits export to the cytoplasm of unspliced genomic or incompletely spliced subgenomic viral transcripts (By similarity). {ECO:0000250}.; . . . . . . . . . . ERVK-17 . . . endogenous retrovirus group K member 17 . . . . . . . . . . . ERVK-18 . . . endogenous retrovirus group K member 18 FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This envelope protein has superantigenic properties.; FUNCTION: TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at higher level in the thymus. Expressed at lower level in peripheral blood lymphocytes.; . . . . . . . . ERVK-19 . . . endogenous retrovirus group K member 19 FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties. {ECO:0000269|PubMed:14557543}.; FUNCTION: TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (By similarity). {ECO:0000250}.; . . . . . . . . . . ERVK-20 . . . endogenous retrovirus group K member 20 . . . . . . . . . . . ERVK-21 . . . endogenous retrovirus group K member 21 FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties. {ECO:0000269|PubMed:14557543}.; FUNCTION: TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (By similarity). {ECO:0000250}.; . . . . . . . . . . ERVK-22 . . . endogenous retrovirus group K member 22 . . . . . . . . . . . ERVK-23 . . . endogenous retrovirus group K member 23 . . . . . . . . . . . ERVK-24 . . . endogenous retrovirus group K member 24 FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution.; FUNCTION: TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in teratocarcinoma cell line. {ECO:0000269|PubMed:11401426}.; . . . . . . . . ERVK-25 . . . endogenous retrovirus group K member 25 FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution (By similarity). {ECO:0000250}.; FUNCTION: TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (By similarity). {ECO:0000250}.; . . . . . . . . . . ERVK-26 . . . endogenous retrovirus group K member 26 . . . . . . . . . . . ERVK-27 . . . endogenous retrovirus group K member 27 . . . . . . . . . . . ERVK-28 . . . endogenous retrovirus group K member 28 . . . . . . . . . . . ERVK-29 . . . endogenous retrovirus group K member 29 . . . . . . . . . . . ERVK-30 . . . endogenous retrovirus group K member 30 . . . . . . . . . . . ERVK-31 . . . endogenous retrovirus group K member 31 . . . . . . . . . . . ERVK3-1 . . . endogenous retrovirus group K3 member 1 . . . . . . . . . . . ERVK3-2 . . . endogenous retrovirus group K3 member 2 . . . . . . . . . . . ERVK3-3 . . . endogenous retrovirus group K3 member 3 . . . . . . . . . . . ERVK3-4 . . . endogenous retrovirus group K3 member 4 . . . . . . . . . . . ERVK3-5 . . . endogenous retrovirus group K3 member 5 . . . . . . . . . . . ERVK3-6 . . . endogenous retrovirus group K3 member 6 . . . . . . . . . . . ERVK3-7 . . . endogenous retrovirus group K3 member 7 . . . . . . . . . . . ERVK3-8 . . . endogenous retrovirus group K3 member 8 . . . . . . . . . . . ERVK11-1 . . . endogenous retrovirus group K11 member 1 FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Cerebellum and testis.; . . . . . . . . ERVK13-1 . . . endogenous retrovirus group K13 member 1 FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution (By similarity). {ECO:0000250}.; FUNCTION: TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Primary culture of CD34+, lung, thymus, ileal mucosa, small intestine, and testis.; . . . . . . . . ERVMER34-1 . . . endogenous retrovirus group MER34 member 1 FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution (By similarity). {ECO:0000250}.; . . . . . . . . 1781.76914 7.79307 ERVMER61-1 . . . endogenous retrovirus group MER61 member 1 . . . . . . . . . . . ERVPABLB-1 . . . endogenous retrovirus group PABLB member 1 FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties. {ECO:0000269|PubMed:14557543}.; . TISSUE SPECIFICITY: Low expression in placenta and testis. {ECO:0000269|PubMed:12970426}.; . . . . . . . . ERVS71-1 . . . endogenous retrovirus group S71 member 1 FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties. {ECO:0000269|PubMed:14557543}.; . TISSUE SPECIFICITY: Expressed at higher level in thyroid. Expressed at lower level in adrenal, bone marrow, brain, breast, kidney, ovary, placenta, prostate, skin, testis and trachea. {ECO:0000269|PubMed:12970426}.; . . . . . . . . ERVS71-2 . . . endogenous retrovirus group S71 member 2 . . . . . . . . . . . ERVV-1 . . . endogenous retrovirus group V member 1 . . TISSUE SPECIFICITY: Expressed in placenta. {ECO:0000269|PubMed:18826608}.; . . . . . . 741.13732 5.40431 ERVV-2 . . . endogenous retrovirus group V member 2 . . TISSUE SPECIFICITY: Expressed in placenta. {ECO:0000269|PubMed:18826608}.; . . . . . . 1560.40535 7.31777 ERVW-1 0.0135671717993117 0.955187201618077 0.0312456265826109 endogenous retrovirus group W member 1 FUNCTION: This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. May induce fusion through binding of SLC1A4 and SLC1A5 (PubMed:10708449, PubMed:12050356, PubMed:23492904). {ECO:0000269|PubMed:10708449, ECO:0000269|PubMed:12050356, ECO:0000269|PubMed:23492904}.; . TISSUE SPECIFICITY: Expressed at higher level in placental syncytiotrophoblast. Expressed at intermediate level in testis. Seems also to be found at low level in adrenal tissue, bone marrow, breast, colon, kidney, ovary, prostate, skin, spleen, thymus, thyroid, brain and trachea. Both mRNA and protein levels are significantly increased in the brain of individuals with multiple sclerosis, particularly in astrocytes and microglia. {ECO:0000269|PubMed:10693809, ECO:0000269|PubMed:10708449, ECO:0000269|PubMed:12970426, ECO:0000269|PubMed:15452578}.; . . 0.11765 . 0.973768544 90.33970276 387.50636 4.14587 ERVW-2 . . . endogenous retrovirus group W member 2 . . . . . . . . . . . ERVW-3 . . . endogenous retrovirus group W member 3 . . . . . . . . . . . ERVW-4 . . . endogenous retrovirus group W member 4 . . . . . . . . . . . ERVW-5 . . . endogenous retrovirus group W member 5 . . . . . . . . . . . ERVW-6 . . . endogenous retrovirus group W member 6 . . . . . . . . . . . ERVW-7 . . . endogenous retrovirus group W member 7 . . . . . . . . . . . ERVW-8 . . . endogenous retrovirus group W member 8 . . . . . . . . . . . ERVW-9 . . . endogenous retrovirus group W member 9 . . . . . . . . . . . ERVW-10 . . . endogenous retrovirus group W member 10 . . . . . . . . . . . ERVW-11 . . . endogenous retrovirus group W member 11 . . . . . . . . . . . ERVW-12 . . . endogenous retrovirus group W member 12 . . . . . . . . . . . ERVW-13 . . . endogenous retrovirus group W member 13 . . . . . . . . . . . ERVW-14 . . . endogenous retrovirus group W member 14 . . . . . . . . . . . ERVW-15 . . . endogenous retrovirus group W member 15 . . . . . . . . . . . ERVW-16 . . . endogenous retrovirus group W member 16 . . . . . . . . . . . ERVW-17 . . . endogenous retrovirus group W member 17 . . . . . . . . . . . ERVW-18 . . . endogenous retrovirus group W member 18 . . . . . . . . . . . ERVW-19 . . . endogenous retrovirus group W member 19 . . . . . . . . . . . ERVW-20 . . . endogenous retrovirus group W member 20 . . . . . . . . . . . ERVW-21 . . . endogenous retrovirus group W member 21 . . . . . . . . . . . ERVW-22 . . . endogenous retrovirus group W member 22 . . . . . . . . . . . ERVW-23 . . . endogenous retrovirus group W member 23 . . . . . . . . . . . ERVW-24 . . . endogenous retrovirus group W member 24 . . . . . . . . . . . ERVW-25 . . . endogenous retrovirus group W member 25 . . . . . . . . . . . ERVW-26 . . . endogenous retrovirus group W member 26 . . . . . . . . . . . ERVW-27 . . . endogenous retrovirus group W member 27 . . . . . . . . . . . ERVW-28 . . . endogenous retrovirus group W member 28 . . . . . . . . . . . ERVW-29 . . . endogenous retrovirus group W member 29 . . . . . . . . . . . ESA4 . . . esterase A4 . . . . . . . . . . . ESAM 0.191978713582815 0.797084510697894 0.0109367757192913 endothelial cell adhesion molecule FUNCTION: Can mediate aggregation most likely through a homophilic molecular interaction. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in endothelial cells. {ECO:0000269|PubMed:11279107}.; ovary;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;stomach; thyroid;placenta;fetal lung; 0.13146 0.16638 0.196671391 67.19155461 411.75477 4.24978 ESAT . . . esterase activator . . . . . . . . . . . ESB3 . . . esterase B3 . . . . . . . . . . . ESCO1 0.998809460698957 0.00119053602574102 3.27530178650755e-09 establishment of sister chromatid cohesion N-acetyltransferase 1 FUNCTION: Acetyltransferase required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase. Acts by mediating the acetylation of cohesin component SMC3. {ECO:0000269|PubMed:14576321, ECO:0000269|PubMed:15958495, ECO:0000269|PubMed:18614053, ECO:0000269|PubMed:19907496}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, liver, placenta, lung, kidney and pancreas. Highly expressed in muscle. {ECO:0000269|PubMed:14576321}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;oesophagus;endometrium;bone;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;cervix;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion;skin; 0.87705 0.10278 -0.242430445 36.22906346 103.25615 2.19516 ESCO2 0.178963923075095 0.820504603615161 0.000531473309743903 establishment of sister chromatid cohesion N-acetyltransferase 2 FUNCTION: Acetyltransferase required for the establishment of sister chromatid cohesion. Couples the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during the S phase. Acetylates the cohesin component SMC3. {ECO:0000269|PubMed:15821733, ECO:0000269|PubMed:19907496, ECO:0000269|PubMed:21111234}.; DISEASE: SC phocomelia syndrome (SCPS) [MIM:269000]: Has a milder phenotype than RBS, with a lesser degree of symmetric limb reduction and additionally includes flexion contractures of various joints, midfacial hemangioma, hypoplastic cartilage of ears and nose, scant silvery-blond hair, and cloudy corneae. Although microcephaly is present, mental retardation may be mild and survival into adulthood is common. {ECO:0000269|PubMed:16380922}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed in fetal tissues. In adult, it is expressed in thymus, placenta and small intestine. {ECO:0000269|PubMed:15821733}.; unclassifiable (Anatomical System);lymph node;ovary;tongue;blood;skeletal muscle;uterus;pancreas;whole body;lung;cochlea;bone;placenta;liver;testis;spleen;germinal center;brain;mammary gland;bladder; superior cervical ganglion;appendix;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.06900 0.20781 0.733063566 86.27034678 519.31576 4.65639 ESD 0.00061169243619552 0.903689580483765 0.0956987270800399 esterase D FUNCTION: Serine hydrolase involved in the detoxification of formaldehyde. {ECO:0000269|PubMed:3770744, ECO:0000269|PubMed:4768551}.; . . . . 0.40836 0.54052 0.104848986 61.49445624 2176.67282 8.59157 ESF1 0.0844452787570408 0.915471185141424 8.35361015352641e-05 ESF1 nucleolar pre-rRNA processing protein homolog FUNCTION: May constitute a novel regulatory system for basal transcription. Negatively regulates ABT1 (By similarity). {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;cornea;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.65708 0.09360 -0.686998355 15.26893135 717.45503 5.31732 ESM1 0.0261762175615844 0.787958926496667 0.185864855941749 endothelial cell specific molecule 1 FUNCTION: Involved in angiogenesis; promotes angiogenic sprouting. May have potent implications in lung endothelial cell-leukocyte interactions. {ECO:0000269|PubMed:20616313}.; . TISSUE SPECIFICITY: Expressed in lung, on the vascular capillary network within alveolar walls, and also at lower level in kidney.; . . 0.13126 0.11684 0.03689118 56.64071715 26.51672 0.85768 ESPL1 0.999999917627418 8.23725822330336e-08 8.1661010051455e-23 extra spindle pole bodies like 1, separase FUNCTION: Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the SCC1/RAD21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by different mechanisms. {ECO:0000269|PubMed:10411507, ECO:0000269|PubMed:11509732}.; . . unclassifiable (Anatomical System);lymphoreticular;lymph node;cartilage;heart;ovary;colon;parathyroid;skin;skeletal muscle;breast;uterus;prostate;lung;placenta;liver;cervix;spleen;germinal center;brain;tonsil;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;tongue;testis;tumor;atrioventricular node;skin;skeletal muscle; 0.20062 0.10572 1.796834896 96.89195565 1610.44431 7.42812 ESPN 0.00255384128821556 0.982377837309084 0.0150683214027005 espin FUNCTION: Multifunctional actin-bundling protein. Plays a major role in regulating the organization, dimensions, dynamics and signaling capacities of the actin filament-rich, microvillus-type specializations that mediate sensory transduction in variouS mechanosensory and chemosensory cells (By similarity). {ECO:0000250}.; DISEASE: Deafness, autosomal recessive, 36, with or without vestibular involvement (DFNB36) [MIM:609006]: A form of non- syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNB36 is characterized by prelingual, profound hearing loss, and vestibular areflexia in some patients. {ECO:0000269|PubMed:15286153, ECO:0000269|PubMed:15930085}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.09981 0.12971 . . 1569.90563 7.33096 ESPNL 3.87784946442822e-10 0.0959331547690705 0.904066844843145 espin-like . . . unclassifiable (Anatomical System);lung;pituitary gland;testis; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.15159 . . . 879.16727 5.77414 ESPNP . . . espin pseudogene . . . unclassifiable (Anatomical System);optic nerve;ovary;macula lutea;testis;fovea centralis;choroid;lens;mammary gland;stomach;retina; . . . . . . . ESR1 0.987167021325736 0.0128318880557621 1.09061850149614e-06 estrogen receptor 1 FUNCTION: Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA- binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF- kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA- binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Isoform 3 is involved in activation of NOS3 and endothelial nitric oxide production. Isoforms lacking one or several functional domains are thought to modulate transcriptional activity by competitive ligand or DNA binding and/or heterodimerization with the full length receptor. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3. Isoform 3 can bind to ERE and inhibit isoform 1. {ECO:0000269|PubMed:10681512, ECO:0000269|PubMed:10816575, ECO:0000269|PubMed:11477071, ECO:0000269|PubMed:11682626, ECO:0000269|PubMed:14764652, ECO:0000269|PubMed:15078875, ECO:0000269|PubMed:15891768, ECO:0000269|PubMed:16043358, ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:16684779, ECO:0000269|PubMed:17922032, ECO:0000269|PubMed:17932106, ECO:0000269|PubMed:18247370, ECO:0000269|PubMed:19350539, ECO:0000269|PubMed:20074560, ECO:0000269|PubMed:20705611, ECO:0000269|PubMed:21330404, ECO:0000269|PubMed:22083956, ECO:0000269|PubMed:7651415, ECO:0000269|PubMed:9328340}.; DISEASE: Estrogen resistance (ESTRR) [MIM:615363]: A disorder characterized by partial or complete resistance to estrogens, in the presence of elevated estrogen serum levels. Clinical features include absence of the pubertal growth spurt, delayed bone maturation, unfused epiphyses, reduced bone mineral density, osteoporosis, continued growth into adulthood and very tall adult stature. Glucose intolerance, hyperinsulinemia and lipid abnormalities may also be present. {ECO:0000269|PubMed:23841731, ECO:0000269|PubMed:8961262}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Isoform 3 is not expressed in the pituitary gland. {ECO:0000269|PubMed:10970861}.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;skeletal muscle;uterus;breast;pancreas;prostate;whole body;lung;endometrium;adrenal gland;pituitary gland;testis;kidney;mammary gland; uterus;dorsal root ganglion;superior cervical ganglion;uterus corpus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;pituitary;cingulate cortex; 0.99765 0.95064 0.242582624 69.45623968 148.46269 2.65650 ESR2 5.15440712040043e-08 0.391979443153873 0.608020505302056 estrogen receptor 2 (ER beta) FUNCTION: Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner (PubMed:20074560). Isoform beta-cx lacks ligand binding ability and has no or only very low ere binding activity resulting in the loss of ligand-dependent transactivation ability. DNA-binding by ESR1 and ESR2 is rapidly lost at 37 degrees Celsius in the absence of ligand while in the presence of 17 beta-estradiol and 4-hydroxy-tamoxifen loss in DNA-binding at elevated temperature is more gradual. {ECO:0000269|PubMed:20074560}.; . TISSUE SPECIFICITY: Isoform beta-1 is expressed in testis and ovary, and at a lower level in heart, brain, placenta, liver, skeletal muscle, spleen, thymus, prostate, colon, bone marrow, mammary gland and uterus. Also found in uterine bone, breast, and ovarian tumor cell lines, but not in colon and liver tumors. Isoform beta-2 is expressed in spleen, thymus, testis and ovary and at a lower level in skeletal muscle, prostate, colon, small intestine, leukocytes, bone marrow, mammary gland and uterus. Isoform beta-3 is found in testis. Isoform beta-4 is expressed in testis, and at a lower level in spleen, thymus, ovary, mammary gland and uterus. Isoform beta-5 is expressed in testis, placenta, skeletal muscle, spleen and leukocytes, and at a lower level in heart, lung, liver, kidney, pancreas, thymus, prostate, colon, small intestine, bone marrow, mammary gland and uterus. Not expressed in brain.; unclassifiable (Anatomical System);placenta;testis; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.29296 0.74862 -0.951568548 9.271054494 97.48684 2.13375 ESRG . . . embryonic stem cell related (non-protein coding) . . TISSUE SPECIFICITY: Expressed only in fetal ovary and in undifferentiated ES cells. {ECO:0000269|PubMed:17803967, ECO:0000269|PubMed:23628413}.; . . . . . . . . ESRP1 0.999134056583357 0.000865943111587433 3.05055548739505e-10 epithelial splicing regulatory protein 1 FUNCTION: mRNA splicing factor that regulates the formation of epithelial cell-specific isoforms. Specifically regulates the expression of FGFR2-IIIb, an epithelial cell-specific isoform of FGFR2. Also regulates the splicing of CD44, CTNND1, ENAH, 3 transcripts that undergo changes in splicing during the epithelial-to-mesenchymal transition (EMT). Acts by directly binding specific sequences in mRNAs. Binds the GU-rich sequence motifs in the ISE/ISS-3, a cis-element regulatory region present in the mRNA of FGFR2. {ECO:0000269|PubMed:19285943}.; . TISSUE SPECIFICITY: Epithelial cell-specific. {ECO:0000269|PubMed:19285943}.; ovary;colon;parathyroid;skin;prostate;whole body;endometrium;larynx;thyroid;pituitary gland;testis;dura mater;bladder;unclassifiable (Anatomical System);meninges;islets of Langerhans;urinary;bile duct;breast;pancreas;pia mater;lung;nasopharynx;placenta;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; pancreas;trachea;placenta;skeletal muscle; 0.66402 0.11975 -0.534490515 20.70063694 88.50054 2.01702 ESRP2 0.731424518577173 0.268570845043798 4.63637902919037e-06 epithelial splicing regulatory protein 2 FUNCTION: mRNA splicing factor that regulates the formation of epithelial cell-specific isoforms. Specifically regulates the expression of FGFR2-IIIb, an epithelial cell-specific isoform of FGFR2. Also regulates the splicing of CD44, CTNND1, ENAH, 3 transcripts that undergo changes in splicing during the epithelial-to-mesenchymal transition (EMT). Acts by directly binding specific sequences in mRNAs. Binds the GU-rich sequence motifs in the ISE/ISS-3, a cis-element regulatory region present in the mRNA of FGFR2. {ECO:0000269|PubMed:19285943}.; . TISSUE SPECIFICITY: Epithelial cell-specific. {ECO:0000269|PubMed:19285943}.; lymphoreticular;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;urinary;pharynx;blood;lens;breast;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;amnion;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.87554 . -0.731092527 14.13658882 286.34992 3.62417 ESRRA 0.527244156756672 0.469269460877509 0.00348638236581946 estrogen related receptor alpha FUNCTION: Binds to an ERR-alpha response element (ERRE) containing a single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium-chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and may act as an important regulator of MCAD promoter. Binds to the C1 region of the lactoferrin gene promoter. Requires dimerization and the coactivator, PGC-1A, for full activity. The ERRalpha/PGC1alpha complex is a regulator of energy metabolism. Induces the expression of PERM1 in the skeletal muscle. {ECO:0000269|PubMed:12522104, ECO:0000269|PubMed:16150865, ECO:0000269|PubMed:17676930, ECO:0000269|PubMed:18063693, ECO:0000269|PubMed:23836911, ECO:0000269|PubMed:9271417}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;larynx;bone;iris;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;pons;trigeminal ganglion;skeletal muscle; 0.51994 0.37283 -0.359940251 28.93371078 38.05712 1.13096 ESRRAP1 . . . estrogen-related receptor alpha pseudogene 1 . . . . . . . . . . . ESRRAP2 . . . estrogen-related receptor alpha pseudogene 2 . . . . . . . . . . . ESRRB 0.542080991203377 0.45728252396934 0.000636484827283287 estrogen related receptor beta FUNCTION: Nuclear receptor, may regulate ESR1 transcriptional activity. Induces the expression of PERM1 in the skeletal muscle. {ECO:0000269|PubMed:19755138, ECO:0000269|PubMed:23836911}.; DISEASE: Deafness, autosomal recessive, 35 (DFNB35) [MIM:608565]: A form of non-syndromic deafness characterized by non-progressive, prelingual hearing loss. {ECO:0000269|PubMed:18179891}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);optic nerve;heart;macula lutea;fovea centralis;choroid;lens;skeletal muscle;retina; superior cervical ganglion;ciliary ganglion; 0.18747 0.20256 0.176444282 66.07100731 673.49263 5.18270 ESRRG 0.93661120997453 0.0633313409107383 5.74491147317209e-05 estrogen related receptor gamma FUNCTION: Orphan receptor that acts as transcription activator in the absence of bound ligand. Binds specifically to an estrogen response element and activates reporter genes controlled by estrogen response elements (By similarity). Induces the expression of PERM1 in the skeletal muscle. {ECO:0000250, ECO:0000269|PubMed:11864604, ECO:0000269|PubMed:18063693, ECO:0000269|PubMed:19067653, ECO:0000269|PubMed:23836911}.; . TISSUE SPECIFICITY: Expressed in the heart, kidney, brain, lung, bone marrow, adrenal gland, trachea, spinal cord and thyroid gland. {ECO:0000269|PubMed:14651967, ECO:0000269|PubMed:9676434}.; unclassifiable (Anatomical System);ovary;heart;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;whole body;optic nerve;cochlea;endometrium;placenta;macula lutea;visual apparatus;kidney;brain;pineal gland; atrioventricular node;skeletal muscle; 0.42324 0.19444 -0.560178693 19.30879925 15.97048 0.56554 ESX1 0.635809622081592 0.357406648586188 0.00678372933221937 ESX homeobox 1 FUNCTION: May coordinately regulate cell cycle progression and transcription during spermatogenesis. Inhibits degradation of polyubiquitinated cyclin A and cyclin B1 and thereby arrests the cell cycle at early M phase. ESXR1-N acts as a transcriptional repressor. Binds to the sequence 5'-TAATGTTATTA-3' which is present within the first intron of the KRAS gene and inhibits its expression. ESXR1-C has the ability to inhibit cyclin turnover. {ECO:0000269|PubMed:15235584, ECO:0000269|PubMed:15897875}.; . TISSUE SPECIFICITY: Expressed in placenta and testis. Expressed in testicular germ cell tumors. {ECO:0000269|PubMed:11374906, ECO:0000269|PubMed:15235584}.; . . 0.14806 0.09574 0.040529541 57.15380986 238.93432 3.33765 ESYT1 2.14071709405869e-07 0.99999934780968 4.38118610852483e-07 extended synaptotagmin protein 1 FUNCTION: Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). Binds calcium (via the C2 domains) and translocates to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels. Helps tether the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. {ECO:0000250, ECO:0000269|PubMed:23791178, ECO:0000269|PubMed:24183667}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17360437}.; lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus; lung;adipose tissue;heart;placenta;white blood cells;whole blood;thymus; 0.14917 0.10000 -1.857465733 2.022882755 202.12335 3.06797 ESYT2 0.00844095092621287 0.991536104688721 2.29443850655829e-05 extended synaptotagmin protein 2 FUNCTION: Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid internalization of FGFR1 that has been activated by FGF1 binding; this occurs most likely via the AP-2 complex. {ECO:0000269|PubMed:17360437, ECO:0000269|PubMed:20833364, ECO:0000269|PubMed:23791178, ECO:0000269|PubMed:24847877}.; . TISSUE SPECIFICITY: Widely expressed with high level in cerebellum. {ECO:0000269|PubMed:17360437}.; lymphoreticular;myocardium;ovary;skin;retina;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;amygdala;heart;cartilage;tongue;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;placenta;head and neck;kidney;stomach; . 0.20986 0.10633 -0.106515707 45.60627506 6582.08374 17.11541 ESYT3 2.43267295856475e-11 0.962750697651079 0.0372493023245944 extended synaptotagmin protein 3 FUNCTION: Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. {ECO:0000250, ECO:0000269|PubMed:23791178}.; . TISSUE SPECIFICITY: Widely expressed with high level in cerebellum and skin. {ECO:0000269|PubMed:17360437}.; unclassifiable (Anatomical System);lung;placenta;testis;colon;kidney;brain;skeletal muscle; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.07274 . 1.896046011 97.34017457 5031.67435 14.48715 ETAA1 0.975314596420393 0.0246842985115596 1.1050680473098e-06 Ewing tumor-associated antigen 1 . . TISSUE SPECIFICITY: Expressed at high levels in the brain, liver kidney and Ewing tumor cell lines. {ECO:0000269|PubMed:16003559}.; myocardium;colon;skin;bone marrow;retina;uterus;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;breast;pancreas;lung;placenta;liver;head and neck;kidney;stomach;aorta; superior cervical ganglion;skeletal muscle; 0.05142 0.07884 1.49181482 95.36447275 1000.99228 6.09541 ETF1 0.998925127429319 0.00107485995357489 1.26171060075756e-08 eukaryotic translation termination factor 1 FUNCTION: Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. {ECO:0000269|PubMed:7990965}.; . . ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;pharynx;blood;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; . 0.98811 0.37501 -0.317668748 31.45789101 1.55963 0.05160 ETF1P1 . . . eukaryotic translation termination factor 1 pseudogene 1 . . . . . . . . . . . ETF1P2 . . . eukaryotic translation termination factor 1 pseudogene 2 . . . . . . . . . . . ETF1P3 . . . eukaryotic translation termination factor 1 pseudogene 3 . . . . . . . . . . . ETFA 0.0129272726537226 0.979861854827518 0.00721087251875967 electron transfer flavoprotein alpha subunit FUNCTION: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl- CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).; DISEASE: Glutaric aciduria 2A (GA2A) [MIM:231680]: An autosomal recessively inherited disorder of fatty acid, amino acid, and choline metabolism. It is characterized by multiple acyl-CoA dehydrogenase deficiencies resulting in large excretion not only of glutaric acid, but also of lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids. {ECO:0000269|PubMed:1430199, ECO:0000269|PubMed:1882842}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; adipose tissue;tumor;skeletal muscle; 0.17645 0.72960 0.082802743 60.09082331 378.75818 4.10282 ETFB 0.00371616291629958 0.846731413167692 0.149552423916008 electron transfer flavoprotein beta subunit FUNCTION: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl- CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). {ECO:0000250|UniProtKB:Q9DCW4, ECO:0000269|PubMed:25416781}.; DISEASE: Glutaric aciduria 2B (GA2B) [MIM:231680]: An autosomal recessively inherited disorder of fatty acid, amino acid, and choline metabolism. It is characterized by multiple acyl-CoA dehydrogenase deficiencies resulting in large excretion not only of glutaric acid, but also of lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids. {ECO:0000269|PubMed:12815589, ECO:0000269|PubMed:7912128}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Abundant in liver, heart and skeletal muscle. A weak expression is seen in the brain, placenta, lung, kidney and pancreas. {ECO:0000269|PubMed:8504797}.; myocardium;lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;kidney;stomach;aorta;thymus; thalamus;fetal liver;heart;liver;kidney;cingulate cortex; 0.38126 0.27764 0.64123826 83.97617363 4731.06385 13.90411 ETFBKMT . . . electron transfer flavoprotein beta subunit lysine methyltransferase FUNCTION: Protein-lysine methyltransferase that selectively trimethylates the flavoprotein ETFB in mitochondria (PubMed:25023281, PubMed:25416781). Thereby, may negatively regulate the function of ETFB in electron transfer from Acyl-CoA dehydrogenases to the main respiratory chain (PubMed:25416781). {ECO:0000269|PubMed:25023281, ECO:0000269|PubMed:25416781}.; . . . . . 0.10016 0.749657564 86.56522765 . . ETFDH 1.63440676840321e-07 0.846807838164647 0.153191998394676 electron transfer flavoprotein dehydrogenase FUNCTION: Accepts electrons from ETF and reduces ubiquinone.; DISEASE: Glutaric aciduria 2C (GA2C) [MIM:231680]: An autosomal recessively inherited disorder of fatty acid, amino acid, and choline metabolism. It is characterized by multiple acyl-CoA dehydrogenase deficiencies resulting in large excretion not only of glutaric acid, but also of lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids. {ECO:0000269|PubMed:12815589}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;colon;parathyroid;skin;retina;uterus;whole body;bone;thyroid;pituitary gland;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion; 0.05430 0.31484 -0.558357437 19.54470394 50.78471 1.40384 ETHE1 0.0161751862087467 0.88438027200358 0.0994445417876733 ethylmalonic encephalopathy 1 FUNCTION: Sulfur dioxygenase that plays an essential role in hydrogen sulfide catabolism in the mitochondrial matrix. Hydrogen sulfide (H(2)S) is first oxidized by SQRDL, giving rise to cysteine persulfide residues. ETHE1 consumes molecular oxygen to catalyze the oxidation of the persulfide, once it has been transferred to a thiophilic acceptor, such as glutathione (R-SSH). Plays an important role in metabolic homeostasis in mitochondria by metabolizing hydrogen sulfide and preventing the accumulation of supraphysiological H(2)S levels that have toxic effects, due to the inhibition of cytochrome c oxidase. First described as a protein that can shuttle between the nucleus and the cytoplasm and suppress p53-induced apoptosis by sequestering the transcription factor RELA/NFKB3 in the cytoplasm and preventing its accumulation in the nucleus (PubMed:12398897). {ECO:0000269|PubMed:12398897, ECO:0000269|PubMed:14732903, ECO:0000269|PubMed:19136963, ECO:0000269|PubMed:23144459}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:14732903}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pineal body;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;alveolus;liver;spleen;kidney;stomach; superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.08791 0.16605 -0.317668748 31.45789101 124.64494 2.42727 ETM1 . . . essential tremor 1 . . . . . . . . . . . ETM2 . . . essential tremor 2 . . . . . . . . . . . ETNK1 0.865130479359824 0.134787503233256 8.20174069191458e-05 ethanolamine kinase 1 FUNCTION: Highly specific for ethanolamine phosphorylation. May be a rate-controlling step in phosphatidylethanolamine biosynthesis.; . TISSUE SPECIFICITY: Expressed in kidney, liver, placenta, heart, leukocyte, ovary and testis.; ovary;salivary gland;intestine;colon;parathyroid;skin;whole body;larynx;thyroid;bone;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;pia mater;lung;cornea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.16374 0.10712 0.038710339 56.92380278 215.24648 3.16629 ETNK2 0.00711885369597901 0.92075436640957 0.0721267798944514 ethanolamine kinase 2 FUNCTION: Highly specific for ethanolamine phosphorylation. Does not have choline kinase activity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in kidney, liver, ovary, testis and prostate. {ECO:0000269|PubMed:11044454}.; . . 0.07996 0.08354 0.016664174 55.21939137 1450.59804 7.10742 ETNPPL 0.000225469247160346 0.979777728239731 0.0199968025131091 ethanolamine-phosphate phospho-lyase FUNCTION: Catalyzes the pyridoxal-phosphate-dependent breakdown of phosphoethanolamine, converting it to ammonia, inorganic phosphate and acetaldehyde. {ECO:0000269|PubMed:22241472}.; . . . . 0.09750 0.17016 -0.001743238 53.85114414 1772.05008 7.77574 ETS1 0.795176655680943 0.204771467981711 5.18763373461854e-05 ETS proto-oncogene 1, transcription factor FUNCTION: Transcription factor. Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts. May control the differentiation, survival and proliferation of lymphoid cells. May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion. {ECO:0000269|PubMed:10698492, ECO:0000269|PubMed:11909962, ECO:0000269|PubMed:15247905, ECO:0000269|PubMed:15592518}.; . TISSUE SPECIFICITY: Highly expressed within lymphoid cells. Isoforms c-ETS-1A and Ets-1 p27 are both detected in all fetal tissues tested, but vary with tissue type in adult tissues. None is detected in brain or kidney. {ECO:0000269|PubMed:19377509, ECO:0000269|PubMed:20378371}.; smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;oesophagus;synovium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;muscle;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; . 0.94439 0.72578 -0.203796826 38.81811748 21.67457 0.72999 ETS2 0.993350130351238 0.00664879283026328 1.0768184986953e-06 ETS proto-oncogene 2, transcription factor FUNCTION: Transcription factor activating transcription. Binds specifically the DNA GGAA/T core motif (Ets-binding site or EBS) in gene promoters and stimulates transcription. {ECO:0000269|PubMed:11909962}.; . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;lens;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; skeletal muscle; 0.72780 0.55475 -0.047654689 50.22410946 55.06437 1.48716 ETV1 0.996674203240852 0.00332559852237683 1.98236771238771e-07 ETS variant 1 FUNCTION: Transcriptional activator that binds to DNA sequences containing the consensus pentanucleotide 5'-CGGA[AT]-3'.; DISEASE: Ewing sarcoma (ES) [MIM:612219]: A highly malignant, metastatic, primitive small round cell tumor of bone and soft tissue that affects children and adolescents. It belongs to the Ewing sarcoma family of tumors, a group of morphologically heterogeneous neoplasms that share the same cytogenetic features. They are considered neural tumors derived from cells of the neural crest. Ewing sarcoma represents the less differentiated form of the tumors. {ECO:0000269|PubMed:7700648}. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving ETV1 is found in patients with Erwing sarcoma. Translocation t(7;22)(p22;q12) with EWSR1. {ECO:0000269|PubMed:7700648}.; TISSUE SPECIFICITY: Very highly expressed in brain, highly expressed in testis, lung and heart, moderately in spleen, small intestine, pancreas and colon, weakly in liver, prostate and thymus, very weakly in skeletal muscle, kidney and ovary and not in placenta and peripheral blood leukocytes.; unclassifiable (Anatomical System);lung;frontal lobe;heart;islets of Langerhans;hippocampus;liver;spinal ganglion;brain;skin;skeletal muscle; amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;cerebellum peduncles;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex;cerebellum; 0.80740 . -0.426079032 25.36565228 2627.67174 9.61317 ETV2 0.0328967978548939 0.926872870549323 0.0402303315957836 ETS variant 2 FUNCTION: Binds to DNA sequences containing the consensus pentanucleotide 5'-CGGA[AT]-3'. {ECO:0000250}.; . . . . 0.14248 0.07914 0.527368849 80.73248408 897.23069 5.83584 ETV3 0.783799556047856 0.209446438645531 0.00675400530661293 ETS variant 3 FUNCTION: Transcriptional repressor that contribute to growth arrest during terminal macrophage differentiation by repressing target genes involved in Ras-dependent proliferation. Represses MMP1 promoter activity. {ECO:0000269|PubMed:12007404}.; . . unclassifiable (Anatomical System);thyroid;liver;colon;blood;bone marrow; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;liver;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.14650 0.24163 -0.339715008 30.06605331 22.17717 0.74420 ETV3L 1.20827466358355e-05 0.598257044889535 0.401730872363829 ETS variant 3 like FUNCTION: Transcriptional regulator. {ECO:0000250}.; . . . . 0.14862 . 1.442251694 95.08138712 1778.4488 7.78773 ETV4 0.00270290986689264 0.99440207828221 0.00289501185089696 ETS variant 4 FUNCTION: Transcriptional activator that binds to the enhancer of the adenovirus E1A gene; the core-binding sequence is 5'[AC]GGA[AT]GT-3'. {ECO:0000269|PubMed:19307308}.; . . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;larynx;bone;brain;unclassifiable (Anatomical System);heart;cartilage;muscle;blood;pancreas;lung;placenta;liver;duodenum;spleen;head and neck;kidney;mammary gland;stomach; atrioventricular node;skeletal muscle; 0.56480 0.45988 0.286674996 71.49681529 207.59681 3.11139 ETV5 0.999892475775242 0.000107524178530185 4.62277796677443e-11 ETS variant 5 FUNCTION: Binds to DNA sequences containing the consensus nucleotide core sequence 5'-GGAA.-3'. {ECO:0000269|PubMed:8152800}.; . TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;muscle;pharynx;blood;lens;bile duct;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;placenta;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.70874 0.10902 -0.358119787 29.16371786 128.63466 2.47177 ETV5-AS1 . . . ETV5 antisense RNA 1 . . . . . . . . . . . ETV6 0.99522782011263 0.00477208301229203 9.68750781828605e-08 ETS variant 6 FUNCTION: Transcriptional repressor; binds to the DNA sequence 5'- CCGGAAGT-3'. Plays a role in hematopoiesis and malignant transformation. {ECO:0000269|PubMed:25581430}.; DISEASE: Note=A chromosomal aberration involving ETV6 is found in a form of chronic myelomonocytic leukemia (CMML). Translocation t(5;12)(q33;p13) with PDGFRB. It is characterized by abnormal clonal myeloid proliferation and by progression to acute myelogenous leukemia (AML). {ECO:0000269|PubMed:8168137}.; DISEASE: Note=Chromosomal aberrations involving ETV6 are found in acute myeloid leukemia (AML). Translocation t(12;22)(p13;q11) with MN1 (PubMed:7731705). Translocation t(4;12)(q12;p13) with CHIC2 (PubMed:10477709). {ECO:0000269|PubMed:10477709, ECO:0000269|PubMed:7731705}.; DISEASE: Note=Chromosomal aberrations involving ETV6 are found in childhood acute lymphoblastic leukemia (ALL). Translocations t(12;21)(p12;q22) and t(12;21)(p13;q22) with RUNX1/AML1. {ECO:0000269|PubMed:7761424}.; DISEASE: Note=A chromosomal aberration involving ETV6 is found in a form of pre-B acute lymphoid leukemia. Translocation t(9;12)(p24;p13) with JAK2. {ECO:0000269|PubMed:9326218}.; DISEASE: Note=A chromosomal aberration involving ETV6 and JAK2 is found in an atypical chronic myelogenous leukemia. Translocation t(9;15;12)(p24;q15;p13). {ECO:0000269|PubMed:9326218}.; DISEASE: Note=A chromosomal aberration involving ETV6 is found in myelodysplastic syndrome (MDS) with basophilia. Translocation t(5;12)(q31;p13) with ACSL6. {ECO:0000269|PubMed:10502316}.; DISEASE: Note=A chromosomal aberration involving ETV6 is found in acute eosinophilic leukemia (AEL). Translocation t(5;12)(q31;p13) with ACSL6. {ECO:0000269|PubMed:10502316}.; DISEASE: Note=A chromosomal aberration involving ETV6 is found in myelodysplastic syndrome (MDS). Translocation t(1;12)(p36.1;p13) with MDS2. {ECO:0000269|PubMed:12203785}.; DISEASE: Note=A chromosomal aberration involving ETV6 is found in acute lymphoblastic leukemia. Translocation t(9;12)(p13;p13) with PAX5. {ECO:0000269|PubMed:17344859}.; DISEASE: Myeloproliferative disorder chronic with eosinophilia (MPE) [MIM:131440]: A hematologic disorder characterized by malignant eosinophils proliferation. {ECO:0000269|PubMed:12181402}. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving ETV6 is found in many instances of myeloproliferative disorder chronic with eosinophilia. Translocation t(5;12) with PDGFRB on chromosome 5 creating an ETV6-PDGFRB fusion protein. {ECO:0000269|PubMed:12181402}.; DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. {ECO:0000269|PubMed:15806161}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Thrombocytopenia 5 (THC5) [MIM:616216]: Thrombocytopenia is defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting. THC5 is an autosomal dominant disorder, associated with an increased susceptibility to the development of hematologic and solid malignancies. {ECO:0000269|PubMed:25581430}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; ovary;adrenal medulla;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.91377 0.51420 -0.624497208 17.16206653 77.68821 1.85610 ETV7 2.00672826880885e-08 0.245599352476762 0.754400627455955 ETS variant 7 FUNCTION: Transcriptional repressor; binds to the DNA sequence 5'- CCGGAAGT-3'. Isoform A does not seem to have a repressor activity. Isoform C does not seem to have a repressor activity.; . TISSUE SPECIFICITY: Expressed in hematopoietic tissues.; unclassifiable (Anatomical System);lung;islets of Langerhans;adrenal cortex;colon;blood;germinal center;brain;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.70881 . 1.243805243 93.41825902 433.45398 4.34535 EVA1A 0.0618110308718402 0.721999936152195 0.216189032975965 eva-1 homolog A, regulator of programmed cell death FUNCTION: Acts as a regulator of programmed cell death, mediating both autophagy and apoptosis. {ECO:0000269|PubMed:17492404, ECO:0000269|PubMed:19029833}.; . TISSUE SPECIFICITY: Expressed in lung, kidney, liver, pancreas, placenta, but not in heart and skeletal muscle. {ECO:0000269|PubMed:17492404}.; . . 0.16311 0.10716 0.25917371 70.05779665 651.06467 5.11944 EVA1B 0.656674967875198 0.319050640241911 0.0242743918828919 eva-1 homolog B (C. elegans) . . . . . 0.14155 . . . 37.49298 1.11629 EVA1C 0.325814898143043 0.670822938625029 0.00336216323192887 eva-1 homolog C (C. elegans) FUNCTION: Binds heparin. {ECO:0000269|PubMed:19470522}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:19470522}.; . . 0.15987 . 0.174625237 65.9648502 244.83382 3.37468 EVC 8.01499590160707e-08 0.994773582450156 0.00522633739988531 EvC ciliary complex subunit 1 FUNCTION: Acts as a positive mediator of Hedgehog signaling indispensable for normal endochondral growth and skeletal development. {ECO:0000250}.; DISEASE: Acrofacial dysostosis, Weyers type (WAD) [MIM:193530]: An autosomal dominant condition characterized by dysplastic nails, postaxial polydactyly, dental anomalies, short limbs, short stature and normal intelligence. The phenotype is milder than Ellis-van Creveld syndrome. {ECO:0000269|PubMed:10700184}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in the developing vertebral bodies, ribs, upper and lower limbs, heart, kidney, lung.; unclassifiable (Anatomical System);myocardium;smooth muscle;heart;spinal cord;colon;skin;skeletal muscle;breast;uterus;prostate;lung;bone;thyroid;placenta;hypopharynx;liver;head and neck;kidney;brain;stomach; uterus;dorsal root ganglion;superior cervical ganglion;olfactory bulb;thyroid;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.12742 0.18000 3.727172238 99.58126917 4073.85379 12.66019 EVC2 1.0533170759541e-21 0.0278258399724403 0.97217416002756 EvC ciliary complex subunit 2 FUNCTION: Positive regulator of the hedgehog signaling pathway (By similarity). Plays a critical role in bone formation and skeletal development. {ECO:0000250}.; DISEASE: Acrofacial dysostosis, Weyers type (WAD) [MIM:193530]: An autosomal dominant condition characterized by dysplastic nails, postaxial polydactyly, dental anomalies, short limbs, short stature and normal intelligence. The phenotype is milder than Ellis-van Creveld syndrome. {ECO:0000269|PubMed:16404586}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in the heart, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:12468274}.; unclassifiable (Anatomical System);lymph node;heart;adrenal medulla;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;cerebral cortex;macula lutea;testis;germinal center;kidney;tonsil; superior cervical ganglion;trigeminal ganglion; 0.11712 0.13432 -0.064465206 48.78509082 2881.09884 10.16936 EVI2A 8.68889031084954e-06 0.17798261979517 0.822008691314519 ecotropic viral integration site 2A FUNCTION: May complex with itself or/and other proteins within the membrane, to function as part of a cell-surface receptor.; . . ovary;colon;skin;uterus;optic nerve;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;spinal cord;blood;pancreas;lung;adrenal gland;hippocampus;spleen;head and neck;kidney;stomach;thymus; amygdala;whole brain;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;hypothalamus;spinal cord;caudate nucleus;pons;whole blood;cingulate cortex;parietal lobe; 0.66380 0.08018 0.283038099 71.26680821 41.35352 1.20916 EVI2B 0.177043580614625 0.767571892974377 0.0553845264109981 ecotropic viral integration site 2B . . TISSUE SPECIFICITY: Bone marrow, peripheral blood mononuclear cells, fibroblasts and Epstein-Barr virus-transformed lymphoblastoid cell lines.; ovary;parathyroid;skin;bone marrow;uterus;frontal lobe;endometrium;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);amygdala;meninges;lymph node;cartilage;urinary;blood;skeletal muscle;bile duct;pia mater;lung;nasopharynx;placenta;liver;spleen;kidney;stomach;aorta;thymus; superior cervical ganglion;lymph node;white blood cells;whole blood;bone marrow; 0.08545 0.08637 0.418953042 77.06416608 93.93749 2.08431 EVI5 2.33071549244674e-06 0.998976691925617 0.00102097735889063 ecotropic viral integration site 5 FUNCTION: Functions as a regulator of cell cycle progression by stabilizing the FBXO5 protein and promoting cyclin-A accumulation during interphase. May play a role in cytokinesis. {ECO:0000269|PubMed:16439210}.; DISEASE: Note=A chromosomal aberration involving EVI5 is found is a patient with stage 4S neuroblastoma. Translocation t(1;10)(p22;q21) that forms a EVI5-TRNG10 fusion protein. TRNG10 is a probable structural transcript which is normally not translated. {ECO:0000269|PubMed:9618176}.; TISSUE SPECIFICITY: Expressed in various cell lines (at protein level). Expressed in a wide range of tissues including brain and adrenal. {ECO:0000269|PubMed:16033705, ECO:0000269|PubMed:9618176}.; unclassifiable (Anatomical System);breast;prostate;lung;placenta;skeletal muscle; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;parietal lobe;skeletal muscle; 0.31005 0.10649 0.178263593 66.12998349 2473.07172 9.26773 EVI5L 0.989107012846773 0.0108928395037137 1.47649513678485e-07 ecotropic viral integration site 5 like FUNCTION: Functions as a GTPase-activating protein (GAP) with a broad specificity. {ECO:0000269|PubMed:16923123}.; . . myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;pituitary gland;testis;pineal gland;brain;unclassifiable (Anatomical System);islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;mammary gland;peripheral nerve;cerebellum; caudate nucleus;skeletal muscle; 0.53412 0.10843 -0.824740496 11.67728238 14.85019 0.53429 EVL 0.992615269783271 0.00738444856731403 2.81649414921653e-07 Enah/Vasp-like FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.; . . . . 0.74284 0.16663 -0.359940251 28.93371078 237.51255 3.32761 EVPL 6.48709103471533e-14 0.997202160069246 0.00279783993068899 envoplakin FUNCTION: Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments.; . TISSUE SPECIFICITY: Exclusively expressed in stratified squamous epithelia.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;testis;bladder;unclassifiable (Anatomical System);heart;lens;breast;pancreas;lung;placenta;macula lutea;hypopharynx;head and neck;cervix;kidney; tongue; 0.45755 0.25979 0.769689266 86.89549422 2455.91155 9.22294 EVPLL 2.73060502638625e-08 0.0858182283134477 0.914181744380502 envoplakin-like . . . . . . . 0.858082312 88.55862232 308.50866 3.73819 EVR3 . . . exudative vitreoretinopathy 3 . . . . . . . . . . . EVX1 2.93029181691565e-05 0.334193746037642 0.665776951044189 even-skipped homeobox 1 FUNCTION: May play a role in the specification of neuronal cell types.; . . colon; occipital lobe;superior cervical ganglion;globus pallidus;ciliary ganglion;kidney;atrioventricular node; 0.69401 0.12697 . . 105.81622 2.22953 EVX1-AS . . . EVX1 antisense RNA . . . . . . . . . . . EVX2 . . . even-skipped homeobox 2 . . . unclassifiable (Anatomical System);ovary; dorsal root ganglion;superior cervical ganglion;testis - interstitial;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.34467 0.13076 . . 36.59603 1.09824 EWSAT1 . . . Ewing sarcoma associated transcript 1 . . . . . 0.11458 . . . . . EWSR1 0.998559249387376 0.001440750399128 2.13495811822332e-10 EWS RNA binding protein 1 FUNCTION: Might normally function as a transcriptionnal repressor. EWS-fusion-proteins (EFPS) may play a role in the tumorigenic process. They may disturb gene expression by mimicking, or interfering with the normal function of CTD-POLII within the transcription initiation complex. They may also contribute to an aberrant activation of the fusion protein target genes.; DISEASE: Ewing sarcoma (ES) [MIM:612219]: A highly malignant, metastatic, primitive small round cell tumor of bone and soft tissue that affects children and adolescents. It belongs to the Ewing sarcoma family of tumors, a group of morphologically heterogeneous neoplasms that share the same cytogenetic features. They are considered neural tumors derived from cells of the neural crest. Ewing sarcoma represents the less differentiated form of the tumors. {ECO:0000269|PubMed:15044653, ECO:0000269|PubMed:1522903, ECO:0000269|PubMed:7700648, ECO:0000269|PubMed:9121764}. Note=The protein represented in this entry is involved in disease pathogenesis. Chromosomal aberrations involving EWSR1 are found in patients with Ewing sarcoma. Translocation t(11;22)(q24;q12) with FLI1 (PubMed:1522903, PubMed:15044653). Translocation t(7;22)(p22;q12) with ETV1 (PubMed:7700648). Translocation t(21;22)(q22;q21) with ERG (PubMed:15044653). Translocation t(2;21;22)(q23;q22;q12) that forms a EWSR1-FEV fusion protein with potential oncogenic activity (PubMed:9121764). {ECO:0000269|PubMed:15044653, ECO:0000269|PubMed:1522903, ECO:0000269|PubMed:7700648, ECO:0000269|PubMed:9121764}.; DISEASE: Note=A chromosomal aberration involving EWSR1 has been found in extraskeletal myxoid chondrosarcoma. Translocation t(9;22)(q22-31;q11-12) with NR4A3. {ECO:0000269|PubMed:7539287}.; DISEASE: Note=A chromosomal aberration involving EWSR1 is associated with desmoplastic small round cell tumor (DSRCT). Translocation t(11;22)(p13;q12) with WT1. {ECO:0000269|PubMed:7862627}.; DISEASE: Note=A chromosomal aberration involving EWSR1 is associated with malignant melanoma of soft parts (MMSP). Translocation t(12;22)(q13;q12) with ATF1. Malignant melanoma of soft parts, also known as soft tissue clear cell sarcoma, is a rare tumor developing in tendons and aponeuroses. {ECO:0000269|PubMed:8401579}.; DISEASE: Note=A chromosomal aberration involving EWSR1 is associated with small round cell sarcoma. Translocation t(11;22)(p36.1;q12) with PATZ1. {ECO:0000269|PubMed:10949935}.; DISEASE: Angiomatoid fibrous histiocytoma (AFH) [MIM:612160]: A distinct variant of malignant fibrous histiocytoma that typically occurs in children and adolescents and is manifest by nodular subcutaneous growth. Characteristic microscopic features include lobulated sheets of histiocyte-like cells intimately associated with areas of hemorrhage and cystic pseudovascular spaces, as well as a striking cuffing of inflammatory cells, mimicking a lymph node metastasis. {ECO:0000269|PubMed:15884099, ECO:0000269|PubMed:17724745}. Note=The gene represented in this entry is involved in disease pathogenesis. Chromosomal aberrations involving EWSR1 are found in patients with angiomatoid fibrous histiocytoma. Translocation t(12;22)(q13;q12) with ATF1 generates a chimeric EWSR1/ATF1 protein (PubMed:15884099). Translocation t(2;22)(q33;q12) with CREB1 generates a EWSR1/CREB1 fusion gene that is most common genetic abnormality in this tumor type (PubMed:17724745). {ECO:0000269|PubMed:15884099, ECO:0000269|PubMed:17724745}.; DISEASE: Note=EFPS arise due to chromosomal translocations in which EWSR1 is fused to a variety of cellular transcription factors. EFPS are very potent transcriptional activators dependent on the EAD and a C-terminal DNA-binding domain contributed by the fusion partner. The spectrum of malignancies associated with EFPS are thought to arise via EFP-induced transcriptional deregulation, with the tumor phenotype specified by the EWSR1 fusion partner and cell type. Transcriptional repression of the transforming growth factor beta type II receptor (TGF beta RII) is an important target of the EWS-FLI1, EWS-ERG, or EWS-ETV1 oncogene. {ECO:0000305}.; TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;cartilage;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;mesenchyma;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;thymus;cerebellum; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;testis;globus pallidus;pons;trigeminal ganglion; 0.95588 0.43129 -0.778825328 12.88039632 40.05548 1.17730 EXD1 2.0333200373386e-13 0.0159559474765186 0.984044052523278 exonuclease 3'-5' domain containing 1 . . . unclassifiable (Anatomical System);testis; . 0.15367 . -0.468351206 23.42533616 57.71872 1.53496 EXD2 1.11026481255e-08 0.179351940047373 0.820648048849979 exonuclease 3'-5' domain containing 2 . . . developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;testis;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;tongue;islets of Langerhans;pineal body;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node; 0.16345 . 0.020302773 55.60863411 131.60994 2.49655 EXD3 1.18854775167792e-08 0.779240537970376 0.220759450144147 exonuclease 3'-5' domain containing 3 FUNCTION: Possesses 3'-5' exoribonuclease activity. Required for 3'-end trimming of AGO1-bound miRNAs (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;islets of Langerhans;breast;pancreas;lung;cerebral cortex;endometrium;placenta;bone;liver;testis;spleen;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; . . 2.951159138 99.16843595 1636.4035 7.47753 EXO1 9.25484656376633e-09 0.907319130180496 0.0926808605646575 exonuclease 1 FUNCTION: 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair (MMR) to excise mismatch- containing DNA tracts directed by strand breaks located either 5' or 3' to the mismatch. Also exhibits endonuclease activity against 5'-overhanging flap structures similar to those generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Required for somatic hypermutation (SHM) and class switch recombination (CSR) of immunoglobulin genes. Essential for male and female meiosis. {ECO:0000269|PubMed:10364235, ECO:0000269|PubMed:10608837, ECO:0000269|PubMed:11809771, ECO:0000269|PubMed:11842105, ECO:0000269|PubMed:12414623, ECO:0000269|PubMed:12704184, ECO:0000269|PubMed:14636568, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:15225546, ECO:0000269|PubMed:15886194, ECO:0000269|PubMed:16143102, ECO:0000269|PubMed:9685493}.; . TISSUE SPECIFICITY: Highly expressed in bone marrow, testis and thymus. Expressed at lower levels in colon, lymph nodes, ovary, placenta, prostate, small intestine, spleen and stomach. {ECO:0000269|PubMed:10856833, ECO:0000269|PubMed:9685493, ECO:0000269|PubMed:9788596, ECO:0000269|PubMed:9823303}.; ovary;parathyroid;skin;uterus;cochlea;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;thymus; ciliary ganglion; 0.36257 0.26115 3.144138867 99.29818353 4081.92208 12.67661 EXO5 0.000872651077294589 0.5605794504974 0.438547898425306 exonuclease 5 FUNCTION: Single-stranded DNA (ssDNA) bidirectional exonuclease involved in DNA repair. Probably involved in DNA repair following ultraviolet (UV) irradiation and interstrand cross-links (ICLs) damage. Has both 5'-3' and 3'-5' exonuclease activities with a strong preference for 5'-ends. Acts as a sliding exonuclease that loads at ssDNA ends and then slides along the ssDNA prior to cutting; however the sliding and the 3'-5' exonuclease activities are abolished upon binding to the replication protein A (RPA) complex that enforces 5'-directionality activity. {ECO:0000269|PubMed:23095756}.; . . . . 0.12832 . 0.463046108 78.58575136 1109.13513 6.36571 EXOC1 0.0966642040161599 0.90333306909363 2.72689020959958e-06 exocyst complex component 1 FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.; . . myocardium;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;cochlea;cerebral cortex;endometrium;gum;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;aorta;stomach;peripheral nerve;thymus; dorsal root ganglion;amygdala;thalamus;superior cervical ganglion;occipital lobe;hypothalamus;spinal cord;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.13172 0.10878 -0.644723694 16.52512385 79.41774 1.88308 EXOC2 0.000114966062554538 0.99988124078909 3.7931483551743e-06 exocyst complex component 2 FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.; . TISSUE SPECIFICITY: Widely expressed with highest levels in brain and placenta. {ECO:0000269|PubMed:12459492}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;thymus; dorsal root ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.54231 0.15254 -0.973616687 8.8995046 126.71394 2.45454 EXOC3 0.755230038369907 0.244683765853482 8.61957766114409e-05 exocyst complex component 3 FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.; . TISSUE SPECIFICITY: Expressed in epididymis (at protein level). {ECO:0000269|PubMed:20736409}.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;brain;tonsil;heart;cartilage;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;head and neck;kidney;stomach;thymus;cerebellum; whole brain;superior cervical ganglion;subthalamic nucleus;thalamus;globus pallidus;ciliary ganglion;white blood cells;atrioventricular node;trigeminal ganglion;cerebellum; 0.18544 0.17499 -1.596455314 3.037272942 77.50955 1.85270 EXOC3-AS1 . . . EXOC3 antisense RNA 1 . . . . . . . 0.902179145 89.34890304 . . EXOC3L1 7.64087796717592e-10 0.673750144252059 0.326249854983853 exocyst complex component 3-like 1 FUNCTION: As part of the exocyst, may play a role in regulated exocytosis of insulin granules. {ECO:0000250}.; . . lung;hypothalamus;placenta;liver;spleen;kidney;brain; dorsal root ganglion;liver;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19251 0.09720 1.069238311 91.68435952 1822.68883 7.87534 EXOC3L2 0.925564031557031 0.0743495986846777 8.6369758290786e-05 exocyst complex component 3-like 2 . . . unclassifiable (Anatomical System);islets of Langerhans;thyroid; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.10560 . -0.157884861 42.05590941 776.32764 5.51673 EXOC3L4 3.12925255065406e-07 0.529923455309692 0.470076231765053 exocyst complex component 3 like 4 . . . . . 0.10594 . . . 3467.18598 11.33566 EXOC4 0.000726958108385659 0.999240679874957 3.23620166574731e-05 exocyst complex component 4 FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}.; . . ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.45903 . -1.280491183 5.16631281 159.10541 2.75629 EXOC5 0.996683024892685 0.00331693524976087 3.98575538018413e-08 exocyst complex component 5 FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9119050}.; ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;germinal center;brain;gall bladder;amygdala;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; . 0.78664 0.11725 0.21689899 68.12927577 151.2475 2.68896 EXOC5P1 . . . exocyst complex component 5 pseudogene 1 . . . . . . . . . . . EXOC6 0.0281606351001072 0.971835491009896 3.8738899967418e-06 exocyst complex component 6 FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. Together with RAB11A, RAB3IP, RAB8A, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;sympathetic chain;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;oral cavity;blood;skeletal muscle;breast;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;liver;spleen;head and neck;aorta;stomach; dorsal root ganglion;globus pallidus;trigeminal ganglion;skeletal muscle; 0.46257 0.11456 0.158037129 64.85020052 826.99627 5.63539 EXOC6B 0.666298051678121 0.333701580013825 3.68308054195862e-07 exocyst complex component 6B FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.; . . unclassifiable (Anatomical System);lung;frontal lobe;tongue;thyroid;placenta;testis;head and neck;skeletal muscle;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;cingulate cortex; 0.59778 0.11124 -0.865195027 10.79853739 132.52888 2.50485 EXOC7 0.000651392901677263 0.99842512191136 0.000923485186962418 exocyst complex component 7 FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. In adipocytes, plays a crucial role in targeting SLC2A4 vesicle to the plasma membrane in response to insulin, perhaps directing the vesicle to the precise site of fusion (By similarity). {ECO:0000250}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;cartilage;heart;nervous;urinary;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;larynx;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;aorta;stomach;cerebellum; amygdala;whole brain;dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;atrioventricular node;caudate nucleus;placenta;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.15278 0.17578 -0.93133804 9.613116301 60.9023 1.58649 EXOC7P1 . . . exocyst complex component 7 pseudogene 1 . . . . . . . . . . . EXOC8 0.987113069402522 0.0128858286915649 1.10190591329412e-06 exocyst complex component 8 FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.; . . unclassifiable (Anatomical System);lung;thyroid;testis;germinal center;brain;skin; . 0.32016 0.11638 -0.488577883 22.64685067 289.66539 3.64057 EXOG 2.8645498363351e-08 0.16397594672833 0.836024024626171 endo/exonuclease (5'-3'), endonuclease G-like FUNCTION: Endo/exonuclease with nicking activity towards supercoiled DNA, a preference for single-stranded DNA and 5'-3' exonuclease activity. {ECO:0000269|PubMed:18187503}.; . TISSUE SPECIFICITY: Ubiquitous.; colon;parathyroid;skin;uterus;prostate;whole body;larynx;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;adrenal cortex;blood;skeletal muscle;lung;adrenal gland;placenta;visual apparatus;spleen;head and neck;kidney;stomach;peripheral nerve; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle; 0.10827 0.27260 -0.446304853 24.33356924 81.83051 1.91747 EXOGP1 . . . endo/exonuclease (5'-3'), endonuclease G-like pseudogene 1 . . . . . . . . . . . EXOSC1 1.88218256844532e-07 0.247254023100547 0.752745788681196 exosome component 1 FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC1 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC6 and EXOSC8.; . . . . 0.16187 0.15588 -0.361761279 28.6329323 13.84096 0.50226 EXOSC2 0.0040898062988956 0.960095368921426 0.035814824779678 exosome component 2 FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC2 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC4 and EXOSC7. {ECO:0000269|PubMed:17545563}.; . . . . 0.73339 0.11634 -0.22584292 37.32012267 81.20346 1.90816 EXOSC3 0.701888823414483 0.294440053758721 0.00367112282679674 exosome component 3 FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC3 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC9 and EXOSC5. {ECO:0000269|PubMed:11782436, ECO:0000269|PubMed:17545563, ECO:0000269|PubMed:19056938, ECO:0000269|PubMed:21255825}.; DISEASE: Pontocerebellar hypoplasia 1B (PCH1B) [MIM:614678]: A severe autosomal recessive neurologic disorder characterized by a combination of cerebellar and spinal motor neuron degeneration beginning at birth. There is diffuse muscle weakness, progressive microcephaly, global developmental delay, and brainstem involvement. {ECO:0000269|PubMed:22544365}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;lung;cornea;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach;peripheral nerve; . 0.08047 0.10928 0.617373774 83.25076669 339.95169 3.91231 EXOSC3P1 . . . exosome component 3 pseudogene 1 . . . . . . . . . . . EXOSC3P2 . . . exosome component 3 pseudogene 2 . . . . . . . . . . . EXOSC4 0.0994501752994272 0.866122543236004 0.0344272814645689 exosome component 4 FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC4 binds to ARE-containing RNAs. {ECO:0000269|PubMed:16912217, ECO:0000269|PubMed:17545563, ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:20368444, ECO:0000269|PubMed:21255825}.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;muscle;pharynx;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;heart;temporal lobe;liver;testis;caudate nucleus;trigeminal ganglion; 0.44204 0.11809 -0.315847836 31.68789809 35.67323 1.07315 EXOSC5 0.00119255746638531 0.628610762800424 0.37019667973319 exosome component 5 FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. {ECO:0000269|PubMed:11782436, ECO:0000269|PubMed:21255825}.; . TISSUE SPECIFICITY: Highly expressed in a variety of hematopoietic and epithelial tumor cell lines, but not in normal hematopoietic tissues or other normal tissue, with the exception of testis.; lymphoreticular;myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; liver; 0.40632 0.10940 -0.291981272 33.20358575 27.33486 0.88047 EXOSC6 0.49417393399594 0.43020531564633 0.0756207503577301 exosome component 6 FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. {ECO:0000269|PubMed:21255825}.; . . . . 0.10772 . . . 431.25885 4.33269 EXOSC7 0.0141395293232584 0.956328930793171 0.0295315398835705 exosome component 7 FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;head and neck;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;testis - interstitial;superior cervical ganglion;adrenal gland;tumor;testis;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.63473 0.26851 -0.025608647 51.91672564 488.76108 4.55064 EXOSC8 1.75847936308234e-05 0.679899336370455 0.320083078835914 exosome component 8 FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC8 binds to ARE-containing RNAs. {ECO:0000269|PubMed:16912217, ECO:0000269|PubMed:17545563}.; DISEASE: Pontocerebellar hypoplasia 1C (PCH1C) [MIM:616081]: A severe autosomal recessive neurodegenerative disease characterized by cerebellar and corpus callosum hypoplasia, abnormal myelination of the central nervous system, and spinal motor neuron disease. Affected individuals manifest failure to thrive, severe muscle weakness, spasticity and psychomotor retardation. Vision and hearing are impaired. {ECO:0000269|PubMed:24989451}. Note=The disease is caused by mutations affecting the gene represented in this entry. EXOSC8 dysfunction causes myelin disruption through an imbalanced supply of myelin proteins due to dysregulation of their ARE-containing mRNAs (PubMed:24989451). {ECO:0000269|PubMed:24989451}.; . lymphoreticular;smooth muscle;colon;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;bone;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;aorta;stomach; testis - interstitial;testis;tumor;white blood cells; 0.11004 0.13727 0.104848986 61.49445624 103.34466 2.19590 EXOSC9 1.87139306709704e-06 0.877009959561031 0.122988169045902 exosome component 9 FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC9 binds to ARE-containing RNAs. {ECO:0000269|PubMed:11782436, ECO:0000269|PubMed:16455498, ECO:0000269|PubMed:16912217, ECO:0000269|PubMed:17545563}.; . . medulla oblongata;smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;urinary;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;head and neck;cervix;kidney;mammary gland;aorta;thymus; testis - interstitial;testis - seminiferous tubule;testis;white blood cells;skeletal muscle; 0.21898 0.12274 -0.247889024 35.98726115 1407.55472 7.00928 EXOSC10 1.65795367368417e-07 0.999923521697167 7.63125074654418e-05 exosome component 10 FUNCTION: Putative catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. EXOSC10 has 3'-5' exonuclease activity (By similarity). EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of SKIV2L2, C1D and MPP6 wth the RNA exosome involved in the maturation of 5.8S rRNA. {ECO:0000250, ECO:0000269|PubMed:14527413, ECO:0000269|PubMed:16455498, ECO:0000269|PubMed:17412707, ECO:0000269|PubMed:17545563, ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:19056938, ECO:0000269|PubMed:20368444, ECO:0000269|PubMed:20699273}.; . . medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;developmental;colon;choroid;fovea centralis;uterus;whole body;cerebral cortex;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach; testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;hypothalamus;prefrontal cortex;testis;cingulate cortex; 0.37692 0.30625 -1.238203625 5.490681765 396.49941 4.18353 EXPH5 5.76468072680194e-21 0.0106681859994675 0.989331814000532 exophilin 5 FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking.; . TISSUE SPECIFICITY: Expressed in keratinocytes. {ECO:0000269|PubMed:23176819}.; unclassifiable (Anatomical System);breast;prostate;lung;ovary;epididymis;larynx;placenta;colon;parathyroid;head and neck;kidney; superior cervical ganglion;cerebellum peduncles;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin;cerebellum; 0.09624 0.09179 4.115639618 99.68742628 9943.87558 21.70751 EXT1 0.999320485111258 0.000679514053714648 8.3502718613293e-10 exostosin glycosyltransferase 1 FUNCTION: Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor. {ECO:0000269|PubMed:11518722}.; DISEASE: Tricho-rhino-phalangeal syndrome 2 (TRPS2) [MIM:150230]: A syndrome that combines the clinical features of tricho-rhino- phalangeal syndrome type 1 and multiple exostoses type 1. Affected individuals manifest multiple dysmorphic facial features including large, laterally protruding ears, a bulbous nose, an elongated upper lip, as well as sparse scalp hair, winged scapulae, multiple cartilaginous exostoses, redundant skin, and mental retardation. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration resulting in the loss of functional copies of TRPS1 and EXT1 has been found in TRPS2 patients.; DISEASE: Chondrosarcoma (CHDSA) [MIM:215300]: A malignant neoplasm derived from cartilage cells. Chondrosarcomas range from slow- growing non-metastasizing lesions to highly aggressive metastasizing sarcomas. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; . . 0.73601 0.26791 -1.133409319 6.434300543 42.34323 1.23181 EXT2 2.46055407087129e-07 0.975673722168668 0.0243260317759247 exostosin glycosyltransferase 2 FUNCTION: Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor.; DISEASE: Potocki-Shaffer syndrome (POSHS) [MIM:601224]: A syndrome characterized by foramina parietalia permagna, multiple exostoses, and craniofacial dysostosis and mental retardation in some cases. Note=The gene represented in this entry is involved in disease pathogenesis.; TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;lung;mesenchyma;adrenal gland;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;uterus corpus;superior cervical ganglion;placenta;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.11643 0.12110 -0.484940685 22.75300778 212.82777 3.14929 EXT3 . . . exostoses (multiple) 3 FUNCTION: Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor.; DISEASE: Potocki-Shaffer syndrome (POSHS) [MIM:601224]: A syndrome characterized by foramina parietalia permagna, multiple exostoses, and craniofacial dysostosis and mental retardation in some cases. Note=The gene represented in this entry is involved in disease pathogenesis.; TISSUE SPECIFICITY: Ubiquitous.; . . 0.11643 0.12110 -0.484940685 22.75300778 . . EXTL1 1.17897567862766e-12 0.0232623702457822 0.976737629753039 exostosin-like glycosyltransferase 1 FUNCTION: Probable glycosyltransferase. {ECO:0000250}.; . . . . 0.19886 0.09359 0.714657953 85.81623024 742.09286 5.41048 EXTL2 3.15804988853622e-05 0.565077560704439 0.434890858796676 exostosin-like glycosyltransferase 2 FUNCTION: Glycosyltransferase required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N- acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains. {ECO:0000269|PubMed:10318803}.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.55326 0.12246 -0.315847836 31.68789809 27.37761 0.88183 EXTL2P1 . . . exostoses (multiple)-like 2 pseudogene 1 . . . . . . . . . . . EXTL3 0.0612804860054933 0.938025332461151 0.000694181533355702 exostosin like glycosyltransferase 3 FUNCTION: Probable glycosyltransferase (By similarity). Required for the function of REG3A in regulating keratinocyte proliferation and differentiation. {ECO:0000250, ECO:0000269|PubMed:22727489}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in keratinocytes. {ECO:0000269|PubMed:22727489}.; myocardium;medulla oblongata;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.34888 0.17708 -1.791303746 2.23519698 66.33025 1.67767 EXTL3-AS1 . . . EXTL3 antisense RNA 1 . . . . . . . . . . . EYA1 0.955704570459788 0.0442952359950226 1.93545189733321e-07 EYA transcriptional coactivator and phosphatase 1 FUNCTION: Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5 (By similarity). Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress (PubMed:19234442). Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis (By similarity). Has also phosphatase activity with proteins phosphorylated on Ser and Thr residues (in vitro) (By similarity). Required for normal embryonic development of the craniofacial and trunk skeleton, kidneys and ears (By similarity). Together with SIX1, it plays an important role in hypaxial muscle development; in this it is functionally redundant with EYA2 (By similarity). {ECO:0000250|UniProtKB:P97767, ECO:0000269|PubMed:19234442}.; DISEASE: Branchiootorenal syndrome 1 (BOR1) [MIM:113650]: A syndrome characterized by branchial cleft fistulas or cysts, sensorineural and/or conductive hearing loss, pre-auricular pits, structural defects of the outer, middle or inner ear, and renal malformations. {ECO:0000269|PubMed:10464653, ECO:0000269|PubMed:10655545, ECO:0000269|PubMed:10991693, ECO:0000269|PubMed:11558900, ECO:0000269|PubMed:21280147, ECO:0000269|PubMed:9361030}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Otofaciocervical syndrome 1 (OFC1) [MIM:166780]: A disorder characterized by facial dysmorphism, cup-shaped low-set ears, preauricular fistulas, hearing loss, branchial defects, skeletal anomalies including vertebral defects, low-set clavicles, winged scapulae, sloping shoulders, and mild intellectual disability. {ECO:0000269|PubMed:11409867, ECO:0000269|PubMed:16441263}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Branchiootic syndrome 1 (BOS1) [MIM:602588]: A syndrome characterized by usually bilateral branchial cleft fistulas or cysts, sensorineural and/or conductive hearing loss, pre-auricular pits, and structural defects of the outer, middle or inner ear. Otic defects include malformed and hypoplastic pinnae, a narrowed external ear canal, bulbous internal auditory canal, stapes fixation, malformed and hypoplastic cochlea. Branchial and otic anomalies overlap with those seen in individuals with the branchiootorenal syndrome. However renal anomalies are absent in branchiootic syndrome patients. {ECO:0000269|PubMed:12701758, ECO:0000269|PubMed:16691597, ECO:0000269|PubMed:9359046}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Anterior segment anomalies with or without cataract (ASA) [MIM:602588]: A disease characterized by various types of developmental eye anomalies, in the absence of other abnormalities. The phenotypic spectrum of anterior segment anomalies include central corneal opacity, Peters anomaly, and bilateral persistence of the pupillary membrane. Some patients have cataract. {ECO:0000269|PubMed:10655545}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In the embryo, highly expressed in kidney with lower levels in brain. Weakly expressed in lung. In the adult, highly expressed in heart and skeletal muscle. Weakly expressed in brain and liver. No expression in eye or kidney.; unclassifiable (Anatomical System);meninges;cartilage;developmental;skin;pia mater;lung;cochlea;nasopharynx;placenta;pituitary gland;testis;kidney;dura mater;brain; superior cervical ganglion;caudate nucleus;trigeminal ganglion;skin; 0.82736 0.27632 -0.844966979 11.1759849 582.72096 4.89372 EYA2 0.335504422060954 0.664366664995641 0.000128912943405299 EYA transcriptional coactivator and phosphatase 2 FUNCTION: Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5 (PubMed:12500905, PubMed:23435380). Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress (PubMed:19351884). Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis. Plays an important role in hypaxial muscle development together with SIX1 and DACH2; in this it is functionally redundant with EYA1 (PubMed:12500905). {ECO:0000269|PubMed:12500905, ECO:0000269|PubMed:19351884, ECO:0000269|PubMed:21706047, ECO:0000269|PubMed:23435380}.; . TISSUE SPECIFICITY: Highest expression in muscle with lower levels in kidney, placenta, pancreas, brain and heart. {ECO:0000269|PubMed:9195991}.; ovary;colon;parathyroid;fovea centralis;choroid;bone marrow;retina;prostate;optic nerve;whole body;endometrium;cerebral cortex;thyroid;testis;artery;brain;unclassifiable (Anatomical System);pineal body;lens;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;olfactory bulb;thyroid;ciliary ganglion;atrioventricular node; 0.81212 0.14915 0.090079492 60.64519934 167.12007 2.82511 EYA3 0.995035731060423 0.00496424735283706 2.15867400793495e-08 EYA transcriptional coactivator and phosphatase 3 FUNCTION: Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1 (PubMed:19234442, PubMed:19351884). Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. Coactivates SIX1, and seems to coactivate SIX2, SIX4 and SIX5. The repression of precursor cell proliferation in myoblasts by SIX1 is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex and seems to be dependent on EYA3 phosphatase activity (By similarity). May be involved in development of the eye. {ECO:0000250|UniProtKB:P97480, ECO:0000269|PubMed:19234442, ECO:0000269|PubMed:19351884}.; . . . . 0.88298 0.07831 -0.648365105 16.35999056 30.28063 0.96533 EYA4 0.126429148938264 0.873529106243093 4.17448186428594e-05 EYA transcriptional coactivator and phosphatase 4 FUNCTION: Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1. Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. May be involved in development of the eye (By similarity). {ECO:0000250|UniProtKB:Q99502}.; DISEASE: Cardiomyopathy, dilated 1J (CMD1J) [MIM:605362]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. CMD1J is characterized by the association of sensorineural hearing loss and dilated cardiomyopathy in the absence of other anomalies. {ECO:0000269|PubMed:15735644}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle. {ECO:0000269|PubMed:15735644}.; unclassifiable (Anatomical System);breast;lung;whole body;frontal lobe;bone;liver;brain;skeletal muscle; ciliary ganglion;trigeminal ganglion; 0.74786 0.15999 -0.424258538 25.56027365 4701.77691 13.82839 EYCL1 . . . eye color 1 (green/blue) . . . . . . . . . . . EYS 8.21411418968935e-09 0.2750076762546 0.724992315531286 eyes shut homolog (Drosophila) FUNCTION: Required to maintain the integrity of photoreceptor cells. {ECO:0000269|PubMed:18836446}.; . TISSUE SPECIFICITY: Present in retina. {ECO:0000269|PubMed:18836446, ECO:0000269|PubMed:18976725}.; visual apparatus;skeletal muscle; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.03723 0.08384 7.740745446 99.92922859 9390.99527 20.95425 EZH1 0.000641437785994428 0.999319821857295 3.87403567105647e-05 enhancer of zeste 1 polycomb repressive complex 2 subunit FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Required for embryonic stem cell derivation and self-renewal, suggesting that it is involved in safeguarding embryonic stem cell identity. Compared to EZH2-containing complexes, it is less abundant in embryonic stem cells, has weak methyltransferase activity and plays a less critical role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. {ECO:0000269|PubMed:19026781}.; . . lymphoreticular;myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;lung;epididymis;placenta;macula lutea;liver;spleen;kidney;stomach;aorta;cerebellum;thymus; superior cervical ganglion;olfactory bulb;hypothalamus;prefrontal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.55996 0.11632 -0.448125345 24.19202642 19.92021 0.67829 EZH2 0.999990079045986 9.92095387428438e-06 1.39275423749753e-13 enhancer of zeste 2 polycomb repressive complex 2 subunit FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys- 27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Compared to EZH2-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A and retinoic acid target genes. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA. Regulates the circadian clock via histone methylation at the promoter of the circadian genes. Essential for the CRY1/2-mediated repression of the transcriptional activation of PER1/2 by the CLOCK-ARNTL/BMAL1 heterodimer; involved in the di and trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters which is necessary for the CRY1/2 proteins to inhibit transcription. {ECO:0000269|PubMed:14532106, ECO:0000269|PubMed:15225548, ECO:0000269|PubMed:15231737, ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:16179254, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:16618801, ECO:0000269|PubMed:16717091, ECO:0000269|PubMed:16936726, ECO:0000269|PubMed:17210787, ECO:0000269|PubMed:17344414, ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:19026781, ECO:0000269|PubMed:20935635, ECO:0000269|PubMed:23063525, ECO:0000269|PubMed:24474760}.; DISEASE: Weaver syndrome (WVS) [MIM:277590]: A syndrome of accelerated growth and osseous maturation, unusual craniofacial appearance, hoarse and low-pitched cry, and hypertonia with camptodactyly. Distinguishing features of Weaver syndrome include broad forehead and face, ocular hypertelorism, prominent wide philtrum, micrognathia, deep horizontal chin groove, and deep-set nails. In addition, carpal bone development is advanced over the rest of the hand. {ECO:0000269|PubMed:22177091}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in many tissues. Overexpressed in numerous tumor types including carcinomas of the breast, colon, larynx, lymphoma and testis. {ECO:0000269|PubMed:14532106}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;muscle;pharynx;blood;bile duct;pancreas;lung;placenta;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis - interstitial;fetal liver;testis - seminiferous tubule;testis;tumor;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.97537 0.31462 -0.53631094 20.53550366 732.50896 5.37129 EZH2P1 . . . enhancer of zeste 2 polycomb repressive complex 2 subunit pseudogene 1 . . . . . . . . . . . EZR 0.988110189680017 0.0118896273042728 1.83015710515867e-07 ezrin FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis. {ECO:0000269|PubMed:17881735, ECO:0000269|PubMed:18270268, ECO:0000269|PubMed:19111582}.; . TISSUE SPECIFICITY: Expressed in cerebral cortex, basal ganglia, hippocampus, hypophysis, and optic nerve. Weakly expressed in brain stem and diencephalon. Stronger expression was detected in gray matter of frontal lobe compared to white matter (at protein level). Component of the microvilli of intestinal epithelial cells. Preferentially expressed in astrocytes of hippocampus, frontal cortex, thalamus, parahippocampal cortex, amygdala, insula, and corpus callosum. Not detected in neurons in most tissues studied. {ECO:0000269|PubMed:15797715}.; smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;lung;trachea;adrenal gland;placenta;temporal lobe;adrenal cortex;ciliary ganglion;white blood cells;atrioventricular node;kidney;pons;trigeminal ganglion;parietal lobe;tonsil; 0.64339 0.72105 -1.197736472 5.785562633 62.54234 1.61602 EZR-AS1 . . . EZR antisense RNA 1 . . . . . . . . . . . F2 0.959943187768661 0.0400566617022686 1.50529070705804e-07 coagulation factor II, thrombin FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. {ECO:0000269|PubMed:2856554}.; DISEASE: Factor II deficiency (FA2D) [MIM:613679]: A very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels. {ECO:0000269|PubMed:1349838, ECO:0000269|PubMed:1354985, ECO:0000269|PubMed:1421398, ECO:0000269|PubMed:14962227, ECO:0000269|PubMed:2719946, ECO:0000269|PubMed:3242619, ECO:0000269|PubMed:3567158, ECO:0000269|PubMed:3771562, ECO:0000269|PubMed:3801671, ECO:0000269|PubMed:6405779, ECO:0000269|PubMed:7792730, ECO:0000269|PubMed:7865694}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. {ECO:0000269|PubMed:15534175}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Thrombophilia due to thrombin defect (THPH1) [MIM:188050]: A multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation. {ECO:0000269|PubMed:2825773}. Note=The disease is caused by mutations affecting the gene represented in this entry. A common genetic variation in the 3-prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis.; DISEASE: Pregnancy loss, recurrent, 2 (RPRGL2) [MIM:614390]: A common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions. {ECO:0000269|PubMed:11506076}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; unclassifiable (Anatomical System);whole body;bone;liver;spleen;bone marrow; superior cervical ganglion;fetal liver;liver;fetal lung;atrioventricular node; 0.70915 0.14818 -0.710864321 14.5730125 1350.01732 6.90025 F2R 0.0412384876728322 0.844266417367133 0.114495094960035 coagulation factor II thrombin receptor FUNCTION: High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development. {ECO:0000269|PubMed:10079109}.; . TISSUE SPECIFICITY: Platelets and vascular endothelial cells.; unclassifiable (Anatomical System);cartilage;heart;muscle;urinary;colon;skin;skeletal muscle;bone marrow;breast;uterus;pancreas;lung;endometrium;adrenal gland;bone;thyroid;placenta;visual apparatus;liver;testis;spleen;brain;pineal gland;aorta;stomach; superior cervical ganglion;pons;trigeminal ganglion; 0.07098 0.39918 -0.648365105 16.35999056 25.52168 0.83233 F2RL1 0.00202251710092648 0.739989938659827 0.257987544239246 F2R like trypsin receptor 1 FUNCTION: Receptor for trypsin and trypsin-like enzymes coupled to G proteins. Its function is mediated through the activation of several signaling pathways including phospholipase C (PLC), intracellular calcium, mitogen-activated protein kinase (MAPK), I- kappaB kinase/NF-kappaB and Rho. Can also be transactivated by cleaved F2R/PAR1. Involved in modulation of inflammatory responses and regulation of innate and adaptive immunity, and acts as a sensor for proteolytic enzymes generated during infection. Generally is promoting inflammation. Can signal synergistically with TLR4 and probably TLR2 in inflammatory responses and modulates TLR3 signaling. Has a protective role in establishing the endothelial barrier; the activity involves coagulation factor X. Proposed to have a bronchoprotective role in airway epithelium, but also shown to compromise the airway epithelial barrier by interrupting E-cadherin adhesion. Involved in the regulation of vascular tone; activation results in hypotension presumably mediated by vasodilation. Associates with a subset of G proteins alpha subunits such as G alpha-q, G alpha-11, G alpha-14, G alpha- 12 and G alpha-13, but probably not with G(o) alpha, G(i) subunit alpha-1 and G(i) subunit alpha-2. However, according to PubMed:21627585 can signal through G(i) subunit alpha. Believed to be a class B receptor which internalizes as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptor, for extended periods of time. Mediates inhibition of TNF-alpha stimulated JNK phosphorylation via coupling to G alpha-q/11; the function involves dissociation of RIPK1 and TRADD from TNFR1. Mediates phosphorylation of nuclear factor NF-kappa-B RELA subunit at 'Ser-536'; the function involves IKBKB and is predominantly independent of G proteins. Involved in cellular migration. Involved in cytoskeletal rearrangement and chemotaxis through beta-arrestin-promoted scaffolds; the function is independent of G alpha-q/11 and involves promotion of cofilin dephosphoryltaion and actin filament severing. Induces redistribution of COPS5 from the plasma membrane to the cytosol and activation of the JNK cascade is mediated by COPS5. Involved in the recruitment of leukocytes to the sites of inflammation and is the major PAR receptor capable of modulating eosinophil function such as proinflammatory cytokine secretion, superoxide production and degranulation. During inflammation promotes dendritic cell maturation, trafficking to the lymph nodes and subsequent T-cell activation. Involved in antimicrobial response of innate immnune cells; activation enhances phagocytosis of Gram- positive and killing of Gram-negative bacteria. Acts synergistically with interferon-gamma in enhancing antiviral responses. Implicated in a number of acute and chronic inflammatory diseases such as of the joints, lungs, brain, gastrointestinal tract, periodontium, skin, and vascular systems, and in autoimmune disorders. {ECO:0000269|PubMed:10086357, ECO:0000269|PubMed:10725339, ECO:0000269|PubMed:11413129, ECO:0000269|PubMed:11441110, ECO:0000269|PubMed:11447194, ECO:0000269|PubMed:11714832, ECO:0000269|PubMed:12832443, ECO:0000269|PubMed:15155775, ECO:0000269|PubMed:16359518, ECO:0000269|PubMed:16410250, ECO:0000269|PubMed:16478888, ECO:0000269|PubMed:16714334, ECO:0000269|PubMed:17404307, ECO:0000269|PubMed:17500066, ECO:0000269|PubMed:18424071, ECO:0000269|PubMed:18453611, ECO:0000269|PubMed:18474671, ECO:0000269|PubMed:18622013, ECO:0000269|PubMed:19494303, ECO:0000269|PubMed:19781631, ECO:0000269|PubMed:19864598, ECO:0000269|PubMed:19865078, ECO:0000269|PubMed:20826780, ECO:0000269|PubMed:21501162}.; . TISSUE SPECIFICITY: Widely expressed in tissues with especially high levels in pancreas, liver, kidney, small intestine, and colon. Moderate expression is detected in many organs, but none in brain or skeletal muscle.; unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;urinary;colon;skin;bone marrow;uterus;bile duct;pancreas;prostate;lung;endometrium;adrenal gland;placenta;pituitary gland;liver;kidney;brain;mammary gland;aorta;stomach; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.35247 0.17332 -0.381986487 27.68931352 49.04062 1.36840 F2RL2 7.36707093228916e-07 0.0837335761161487 0.916265687176758 coagulation factor II thrombin receptor like 2 FUNCTION: Receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. {ECO:0000269|PubMed:10079109}.; . TISSUE SPECIFICITY: Highest expression in the megakaryocytes of the bone marrow, lower in mature megakaryocytes, in platelets and in a variety of other tissues such as heart and gut. {ECO:0000269|PubMed:9614115}.; unclassifiable (Anatomical System);heart;cartilage;skeletal muscle;skin;uterus;lung;larynx;thyroid;bone;testis;head and neck;kidney;peripheral nerve; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13366 0.10614 0.773521534 87.06062751 250.22329 3.40668 F2RL3 0.00302235446967585 0.587961870929343 0.409015774600981 F2R like thrombin/trypsin receptor 3 FUNCTION: Receptor for activated thrombin or trypsin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation. {ECO:0000269|PubMed:10079109}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in lung, pancreas, thyroid, testis and small intestine. Not expressed in brain, kidney, spinal cord and peripheral blood leukocytes. Also detected in platelets.; unclassifiable (Anatomical System);islets of Langerhans;skin;retina; . 0.12446 0.13885 . . 1303.21959 6.79177 F3 0.132021360809909 0.846313339934842 0.0216652992552496 coagulation factor III, tissue factor FUNCTION: Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited protolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. {ECO:0000269|PubMed:12652293}.; . TISSUE SPECIFICITY: Lung, placenta and pancreas. {ECO:0000269|PubMed:12652293}.; unclassifiable (Anatomical System);amygdala;meninges;heart;tongue;islets of Langerhans;hypothalamus;skin;skeletal muscle;retina;pancreas;prostate;pia mater;lung;frontal lobe;mesenchyma;larynx;placenta;testis;head and neck;dura mater;kidney;brain;stomach; amygdala;occipital lobe;lung;olfactory bulb;ovary;trachea;placenta;temporal lobe;prefrontal cortex; 0.28537 0.94770 0.881944684 89.02453409 115.77684 2.34039 F5 4.69402330698069e-08 0.999999794568192 1.58491575015974e-07 coagulation factor V FUNCTION: Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.; DISEASE: Factor V deficiency (FA5D) [MIM:227400]: A blood coagulation disorder leading to an hemorrhagic diathesis known as parahemophilia. {ECO:0000269|PubMed:10942390, ECO:0000269|PubMed:12393490}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Thrombophilia due to activated protein C resistance (THPH2) [MIM:188055]: A hemostatic disorder due to defective degradation of factor V by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis. {ECO:0000269|PubMed:11435304, ECO:0000269|PubMed:11858490, ECO:0000269|PubMed:14617013, ECO:0000269|PubMed:9454742}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Budd-Chiari syndrome (BDCHS) [MIM:600880]: A syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera. {ECO:0000269|PubMed:9245936}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. {ECO:0000269|PubMed:15534175}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Pregnancy loss, recurrent, 1 (RPRGL1) [MIM:614389]: A common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions. {ECO:0000269|PubMed:11018168}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma.; . . 0.17357 . 3.230985335 99.38075018 7503.35737 18.61572 F7 1.3314119006302e-05 0.838878390568147 0.161108295312847 coagulation factor VII FUNCTION: Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.; DISEASE: Factor VII deficiency (FA7D) [MIM:227500]: A hemorrhagic disease with variable presentation. The clinical picture can be very severe, with the early occurrence of intracerebral hemorrhages or repeated hemarthroses, or, in contrast, moderate with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a surgical intervention. Finally, numerous subjects are completely asymptomatic despite very low factor VII levels. {ECO:0000269|PubMed:10862079, ECO:0000269|PubMed:11091194, ECO:0000269|PubMed:11129332, ECO:0000269|PubMed:12472587, ECO:0000269|PubMed:14717781, ECO:0000269|PubMed:1634227, ECO:0000269|PubMed:18976247, ECO:0000269|PubMed:19432927, ECO:0000269|PubMed:19751712, ECO:0000269|PubMed:2070047, ECO:0000269|PubMed:21206266, ECO:0000269|PubMed:21372693, ECO:0000269|PubMed:7974346, ECO:0000269|PubMed:7981691, ECO:0000269|PubMed:8043443, ECO:0000269|PubMed:8204879, ECO:0000269|PubMed:8364544, ECO:0000269|PubMed:8652821, ECO:0000269|PubMed:8844208, ECO:0000269|PubMed:8883260, ECO:0000269|PubMed:8940045, ECO:0000269|PubMed:9414278, ECO:0000269|PubMed:9452082, ECO:0000269|PubMed:9576180}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma.; unclassifiable (Anatomical System);hippocampus;liver;colon;spleen; fetal liver;superior cervical ganglion;liver;ciliary ganglion;trigeminal ganglion; 0.10286 0.26819 -0.020150552 52.25288983 194.25954 3.02186 F7R . . . coagulation factor VII regulator . . . . . . . . . . . F8 0.999999811590639 1.88409360555536e-07 1.80634119105655e-18 coagulation factor VIII FUNCTION: Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa.; DISEASE: Hemophilia A (HEMA) [MIM:306700]: A disorder of blood coagulation characterized by a permanent tendency to hemorrhage. About 50% of patients have severe hemophilia resulting in frequent spontaneous bleeding into joints, muscles and internal organs. Less severe forms are characterized by bleeding after trauma or surgery. {ECO:0000269|PubMed:10215414, ECO:0000269|PubMed:10338101, ECO:0000269|PubMed:10404764, ECO:0000269|PubMed:10408784, ECO:0000269|PubMed:10554831, ECO:0000269|PubMed:10612839, ECO:0000269|PubMed:10691849, ECO:0000269|PubMed:10800171, ECO:0000269|PubMed:10886198, ECO:0000269|PubMed:10896236, ECO:0000269|PubMed:10910910, ECO:0000269|PubMed:10910913, ECO:0000269|PubMed:11298607, ECO:0000269|PubMed:11341489, ECO:0000269|PubMed:11410838, ECO:0000269|PubMed:11442643, ECO:0000269|PubMed:11442647, ECO:0000269|PubMed:11554935, ECO:0000269|PubMed:11748850, ECO:0000269|PubMed:11857744, ECO:0000269|PubMed:11858487, ECO:0000269|PubMed:12195713, ECO:0000269|PubMed:12199686, ECO:0000269|PubMed:12203998, ECO:0000269|PubMed:12325022, ECO:0000269|PubMed:12351418, ECO:0000269|PubMed:12406074, ECO:0000269|PubMed:12614369, ECO:0000269|PubMed:12871415, ECO:0000269|PubMed:12930394, ECO:0000269|PubMed:1301194, ECO:0000269|PubMed:1301932, ECO:0000269|PubMed:1301960, ECO:0000269|PubMed:1349567, ECO:0000269|PubMed:1356412, ECO:0000269|PubMed:15682412, ECO:0000269|PubMed:15810915, ECO:0000269|PubMed:1639429, ECO:0000269|PubMed:16805874, ECO:0000269|PubMed:18184865, ECO:0000269|PubMed:1851341, ECO:0000269|PubMed:1908096, ECO:0000269|PubMed:1908817, ECO:0000269|PubMed:1973901, ECO:0000269|PubMed:2104766, ECO:0000269|PubMed:2105106, ECO:0000269|PubMed:2105906, ECO:0000269|PubMed:2106480, ECO:0000269|PubMed:2107542, ECO:0000269|PubMed:21371196, ECO:0000269|PubMed:2495245, ECO:0000269|PubMed:2498882, ECO:0000269|PubMed:2499363, ECO:0000269|PubMed:2506948, ECO:0000269|PubMed:2510835, ECO:0000269|PubMed:25550078, ECO:0000269|PubMed:2833855, ECO:0000269|PubMed:2835904, ECO:0000269|PubMed:3012775, ECO:0000269|PubMed:3122181, ECO:0000269|PubMed:7579394, ECO:0000269|PubMed:7759074, ECO:0000269|PubMed:7794769, ECO:0000269|PubMed:8322269, ECO:0000269|PubMed:8449505, ECO:0000269|PubMed:8639447, ECO:0000269|PubMed:8644728, ECO:0000269|PubMed:8759905, ECO:0000269|PubMed:9029040, ECO:0000269|PubMed:9326186, ECO:0000269|PubMed:9341862, ECO:0000269|PubMed:9450898, ECO:0000269|PubMed:9452104, ECO:0000269|PubMed:9569180, ECO:0000269|PubMed:9569189, ECO:0000269|PubMed:9603440, ECO:0000269|PubMed:9792405, ECO:0000269|PubMed:9829908, ECO:0000269|PubMed:9886318}. Note=The disease is caused by mutations affecting the gene represented in this entry. Of particular interest for the understanding of the function of F8 is the category of CRM (cross-reacting material) positive patients (approximately 5%) that have considerable amount of F8 in their plasma (at least 30% of normal), but the protein is non-functional; i.e. the F8 activity is much less than the plasma protein level. CRM-reduced is another category of patients in which the F8C antigen and activity are reduced to approximately the same level. Most mutations are CRM negative, and probably affect the folding and stability of the protein.; . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;sympathetic chain;parathyroid;skeletal muscle;skin;retina;uterus;prostate;lung;bone;placenta;hippocampus;liver;iris;pituitary gland;testis;cervix;kidney;spinal ganglion;brain; superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.09749 0.82924 -0.745876353 13.76503892 362.2218 4.02864 F8A1 . . . coagulation factor VIII-associated 1 FUNCTION: Not known. Possible housekeeping role.; . . . . 0.19472 0.10599 . . . . F8A2 . . . coagulation factor VIII-associated 2 FUNCTION: Not known. Possible housekeeping role.; . . . . 0.22240 0.10599 . . . . F8A3 . . . coagulation factor VIII-associated 3 FUNCTION: Not known. Possible housekeeping role.; . . . . 0.18659 0.10599 . . . . F9 0.989580625058095 0.0104161433790533 3.23156285159704e-06 coagulation factor IX FUNCTION: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. {ECO:0000269|PubMed:1730085, ECO:0000269|PubMed:19846852, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:8295821}.; DISEASE: Hemophilia B (HEMB) [MIM:306900]: An X-linked blood coagulation disorder characterized by a permanent tendency to hemorrhage, due to factor IX deficiency. It is phenotypically similar to hemophilia A, but patients present with fewer symptoms. Many patients are asymptomatic until the hemostatic system is stressed by surgery or trauma. {ECO:0000269|PubMed:10094553, ECO:0000269|PubMed:10698280, ECO:0000269|PubMed:11122099, ECO:0000269|PubMed:12588353, ECO:0000269|PubMed:12604421, ECO:0000269|PubMed:1346975, ECO:0000269|PubMed:1615485, ECO:0000269|PubMed:1902289, ECO:0000269|PubMed:1958666, ECO:0000269|PubMed:2162822, ECO:0000269|PubMed:2339358, ECO:0000269|PubMed:2372509, ECO:0000269|PubMed:2472424, ECO:0000269|PubMed:25251685, ECO:0000269|PubMed:25470321, ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:2713493, ECO:0000269|PubMed:2714791, ECO:0000269|PubMed:2738071, ECO:0000269|PubMed:2753873, ECO:0000269|PubMed:2773937, ECO:0000269|PubMed:2775660, ECO:0000269|PubMed:3009023, ECO:0000269|PubMed:3243764, ECO:0000269|PubMed:3401602, ECO:0000269|PubMed:3790720, ECO:0000269|PubMed:6603618, ECO:0000269|PubMed:7981722, ECO:0000269|PubMed:8076946, ECO:0000269|PubMed:8199596, ECO:0000269|PubMed:8257988, ECO:0000269|PubMed:8295821, ECO:0000269|PubMed:8680410, ECO:0000269|PubMed:9222764, ECO:0000269|PubMed:9452115, ECO:0000269|PubMed:9590153, ECO:0000269|PubMed:9600455}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide (PubMed:12588353, PubMed:2738071, PubMed:3009023, PubMed:8295821, PubMed:9169594, PubMed:9600455, PubMed:25251685). Mutation in position 93 (Alabama) probably fails to bind to cell membranes (PubMed:3790720). Mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya or Hilo) prevent cleavage of the activation peptide (PubMed:6603618, PubMed:8076946, PubMed:12588353, PubMed:2162822, PubMed:25251685, PubMed:2713493). {ECO:0000269|PubMed:12588353, ECO:0000269|PubMed:2162822, ECO:0000269|PubMed:25251685, ECO:0000269|PubMed:2713493, ECO:0000269|PubMed:2738071, ECO:0000269|PubMed:3009023, ECO:0000269|PubMed:3790720, ECO:0000269|PubMed:6603618, ECO:0000269|PubMed:8076946, ECO:0000269|PubMed:8295821, ECO:0000269|PubMed:9169594, ECO:0000269|PubMed:9600455}.; DISEASE: Thrombophilia, X-linked, due to factor IX defect (THPH8) [MIM:300807]: A hemostatic disorder characterized by a tendency to thrombosis. {ECO:0000269|PubMed:19846852}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in blood plasma (at protein level) (PubMed:3857619, PubMed:8295821, PubMed:2592373, PubMed:9169594, PubMed:19846852). Synthesized primarily in the liver and secreted in plasma. {ECO:0000269|PubMed:19846852, ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:3857619}.; unclassifiable (Anatomical System);liver; fetal liver;superior cervical ganglion;liver;trigeminal ganglion;skin; 0.34741 0.57236 -0.0274281 51.65723048 29.63264 0.94623 F10 0.160510707320587 0.83627277170822 0.00321652097119334 coagulation factor X FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.; DISEASE: Factor X deficiency (FA10D) [MIM:227600]: A hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis. {ECO:0000269|PubMed:10468877, ECO:0000269|PubMed:10746568, ECO:0000269|PubMed:11248282, ECO:0000269|PubMed:11728527, ECO:0000269|PubMed:12574802, ECO:0000269|PubMed:12945883, ECO:0000269|PubMed:15075089, ECO:0000269|PubMed:15650540, ECO:0000269|PubMed:17393015, ECO:0000269|PubMed:19135706, ECO:0000269|PubMed:1973167, ECO:0000269|PubMed:1985698, ECO:0000269|PubMed:25313940, ECO:0000269|PubMed:2790181, ECO:0000269|PubMed:7669671, ECO:0000269|PubMed:7860069, ECO:0000269|PubMed:8529633, ECO:0000269|PubMed:8845463, ECO:0000269|PubMed:8910490}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma; synthesized in the liver. {ECO:0000269|PubMed:6587384}.; . . 0.14421 0.45572 -0.552898813 19.86317528 103.8517 2.20105 F10-AS1 . . . F10 antisense RNA 1 . . . . . . . . . . . F11 1.91287337257915e-22 0.000104379235037357 0.999895620764963 coagulation factor XI FUNCTION: Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX.; DISEASE: Factor XI deficiency (FA11D) [MIM:612416]: A hemorrhagic disease characterized by reduced levels and activity of factor XI resulting in moderate bleeding symptoms, usually occurring after trauma or surgery. Patients usually do not present spontaneous bleeding but women can present with menorrhagia. Hemorrhages are usually moderate. {ECO:0000269|PubMed:10027710, ECO:0000269|PubMed:10606881, ECO:0000269|PubMed:11895778, ECO:0000269|PubMed:15026311, ECO:0000269|PubMed:15180874, ECO:0000269|PubMed:1547342, ECO:0000269|PubMed:15953011, ECO:0000269|PubMed:16607084, ECO:0000269|PubMed:18005151, ECO:0000269|PubMed:21457405, ECO:0000269|PubMed:21668437, ECO:0000269|PubMed:21999818, ECO:0000269|PubMed:22016685, ECO:0000269|PubMed:22159456, ECO:0000269|PubMed:22322133, ECO:0000269|PubMed:2813350, ECO:0000269|PubMed:7669672, ECO:0000269|PubMed:7888672, ECO:0000269|PubMed:9401068, ECO:0000269|PubMed:9787168}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 2 is produced by platelets and megakaryocytes but absent from other blood cells.; unclassifiable (Anatomical System);prostate;small intestine;islets of Langerhans;visual apparatus;liver;spleen;kidney; superior cervical ganglion; 0.04557 0.48270 -0.929520514 9.683887709 197.33532 3.03658 F11-AS1 . . . F11 antisense RNA 1 . . . . . . . . . . . F11R 5.54288059660764e-05 0.883429694429363 0.116514876764671 F11 receptor FUNCTION: Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3. The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly (By similarity). Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier. Involved in platelet activation. {ECO:0000250}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;bladder;brain;heart;tongue;adrenal cortex;blood;lens;breast;epididymis;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;oral cavity;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;lung;trachea;placenta;liver;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.10225 0.06893 -0.137658575 43.57159707 23.15435 0.77223 F12 3.46472901004721e-06 0.939877691511458 0.0601188437595319 coagulation factor XII FUNCTION: Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta- factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa. {ECO:0000269|PubMed:21304106}.; DISEASE: Factor XII deficiency (FA12D) [MIM:234000]: An asymptomatic anomaly of in vitro blood coagulation. Its diagnosis is based on finding a low plasma activity of the factor in coagulating assays. It is usually only accidentally discovered through pre-operative blood tests. Factor XII deficiency is divided into two categories, a cross-reacting material (CRM)- negative group (negative F12 antigen detection) and a CRM-positive group (positive F12 antigen detection). {ECO:0000269|PubMed:10361128, ECO:0000269|PubMed:11776307, ECO:0000269|PubMed:15205584, ECO:0000269|PubMed:15617741, ECO:0000269|PubMed:2510163, ECO:0000269|PubMed:2882793, ECO:0000269|PubMed:8049433, ECO:0000269|PubMed:8528215, ECO:0000269|PubMed:9354665}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hereditary angioedema 3 (HAE3) [MIM:610618]: An hereditary angioedema occurring only in women. Hereditary angioedema is an autosomal dominant disorder characterized by episodic local swelling involving subcutaneous or submucous tissue of the upper respiratory and gastrointestinal tracts, face, extremities, and genitalia. Hereditary angioedema type 3 differs from types 1 and 2 in that both concentration and function of C1 esterase inhibitor are normal. Hereditary angioedema type 3 is precipitated or worsened by high estrogen levels (e.g., during pregnancy or treatment with oral contraceptives). {ECO:0000269|PubMed:16638441, ECO:0000269|PubMed:17186468}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;whole body;cartilage;liver;testis;colon;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;fetal liver;placenta;spinal cord;liver;atrioventricular node;skeletal muscle; 0.28750 0.09552 0.532823122 80.96249115 139.15881 2.57137 F13A1 0.00102736089825156 0.998492486294057 0.000480152807691957 coagulation factor XIII A chain FUNCTION: Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl- epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.; DISEASE: Factor XIII subunit A deficiency (FA13AD) [MIM:613225]: An autosomal recessive hematologic disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women. {ECO:0000269|PubMed:1353995, ECO:0000269|PubMed:24286209, ECO:0000269|PubMed:24329762, ECO:0000269|PubMed:24889649}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;thyroid;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;urinary;breast;pancreas;lung;adrenal gland;placenta;macula lutea;liver;alveolus;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;placenta; 0.33587 0.59246 0.249861693 69.66265629 4254.75217 12.96128 F13B 2.13259736615404e-05 0.976011650763721 0.0239670232626178 coagulation factor XIII B chain FUNCTION: The B chain of factor XIII is not catalytically active, but is thought to stabilize the A subunits and regulate the rate of transglutaminase formation by thrombin. {ECO:0000303|PubMed:21742792, ECO:0000303|PubMed:3021194}.; DISEASE: Factor XIII subunit B deficiency (FA13BD) [MIM:613235]: An autosomal recessive hematologic disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women. {ECO:0000269|PubMed:11313256, ECO:0000269|PubMed:20331752, ECO:0000269|PubMed:26247044, ECO:0000269|PubMed:8324218}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.12787 0.25774 0.731244617 86.21137061 130.2596 2.48552 FA2H 0.726409723584695 0.273002101095238 0.000588175320066303 fatty acid 2-hydroxylase FUNCTION: Required for alpha-hydroxylation of free fatty acids and the formation of alpha-hydroxylated sphingolipids. {ECO:0000269|PubMed:15337768, ECO:0000269|PubMed:17355976}.; DISEASE: Spastic paraplegia 35, autosomal recessive (SPG35) [MIM:612319]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG35 is a complicated form characterized by childhood onset of gait difficulties. It has a rapid progression and many patients become wheelchair-bound as young adults. Patients manifest cognitive decline associated with leukodystrophy. Other variable neurologic features, such as dystonia, optic atrophy, and seizures may also occur. {ECO:0000269|PubMed:19068277, ECO:0000269|PubMed:20104589, ECO:0000269|PubMed:20853438}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in differentiating cultured keratinocytes (at protein level). Detected in epidermis and cultured keratinocytes. Highly expressed in brain and colon. Detected at lower levels in testis, prostate, pancreas and kidney. {ECO:0000269|PubMed:15337768, ECO:0000269|PubMed:17355976}.; unclassifiable (Anatomical System);heart;hypothalamus;colon;blood;skin;skeletal muscle;uterus;pancreas;optic nerve;lung;thyroid;visual apparatus;hippocampus;liver;testis;cervix;kidney;brain;stomach; dorsal root ganglion;amygdala;whole brain;occipital lobe;medulla oblongata;thalamus;superior cervical ganglion;olfactory bulb;hypothalamus;spinal cord;atrioventricular node;pons;caudate nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.26161 0.13138 -0.247889024 35.98726115 32.08247 1.00685 FAAH 5.9295002678292e-07 0.872135462658369 0.127863944391604 fatty acid amide hydrolase FUNCTION: Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates. {ECO:0000269|PubMed:17015445}.; . TISSUE SPECIFICITY: Highly expressed in the brain, small intestine, pancreas, skeletal muscle and testis. Also expressed in the kidney, liver, lung, placenta and prostate. {ECO:0000269|PubMed:17015445}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;testis;brain;heart;lens;skeletal muscle;lung;placenta;macula lutea;hippocampus;head and neck;kidney;mammary gland;peripheral nerve;cerebellum; occipital lobe;medulla oblongata;testis;parietal lobe;skeletal muscle; 0.11182 0.16192 -0.468351206 23.42533616 1643.89831 7.49371 FAAH2 2.45580805455636e-17 0.000292395407237397 0.999707604592763 fatty acid amide hydrolase 2 FUNCTION: Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes monounsaturated substrate anandamide preferentially as compared to polyunsaturated substrates. {ECO:0000269|PubMed:17015445}.; . TISSUE SPECIFICITY: Highly expressed in the brain, small intestine and testis. Also expressed in the heart, kidney, liver, lung and prostate. {ECO:0000269|PubMed:17015445}.; . . 0.17056 0.11018 -0.288341872 33.41589998 68.11458 1.70685 FAAHP1 . . . fatty acid amide hydrolase pseudogene 1 . . . . . . . . . . . FAAP20 . . . Fanconi anemia core complex associated protein 20 FUNCTION: Component of the Fanconi anemia (FA) complex required to recruit the FA complex to DNA interstrand cross-links (ICLs) and promote ICLs repair. Following DNA damage recognizes and binds 'Lys-63'-linked ubiquitin generated by RNF8 at ICLs and recruits other components of the FA complex. Promotes translesion synthesis via interaction with REV1. {ECO:0000269|PubMed:22266823, ECO:0000269|PubMed:22343915, ECO:0000269|PubMed:22396592, ECO:0000269|PubMed:22705371}.; . . . . 0.06450 . 0.371224249 75.12384996 . . FAAP24 . . . Fanconi anemia core complex associated protein 24 FUNCTION: Plays a role in DNA repair through recruitment of the FA core complex to damaged DNA. Regulates FANCD2 monoubiquitination upon DNA damage. Induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents, when repressed. Targets FANCM/FAAP24 complex to the DNA, preferentially to single strand DNA. {ECO:0000269|PubMed:17289582}.; . . . . 0.04342 0.13382 0.994001092 90.5579146 . . FAAP100 . . . Fanconi anemia core complex associated protein 100 FUNCTION: Plays a role in Fanconi anemia-associated DNA damage response network. Regulates FANCD2 monoubiquitination and the stability of the FA core complex. Induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents, when repressed. {ECO:0000269|PubMed:17396147}.; . . . . 0.14739 0.16001 0.363735434 74.71101675 . . FABP1 0.0160619800486128 0.701541378006758 0.282396641944629 fatty acid binding protein 1 FUNCTION: Plays a role in lipoprotein-mediated cholesterol uptake in hepatocytes (PubMed:25732850). Binds cholesterol (PubMed:25732850). Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity). {ECO:0000250|UniProtKB:P82289, ECO:0000269|PubMed:25732850}.; . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;rectum;pharynx;colon;parathyroid;blood;skin;skeletal muscle;breast;prostate;lung;placenta;visual apparatus;liver;testis;spleen;kidney;brain;bladder;stomach;gall bladder; pancreas;superior cervical ganglion;fetal liver;liver;fetal lung;kidney;trigeminal ganglion; 0.91697 . 0.125076652 62.7388535 910.05423 5.86402 FABP2 0.00117790515234333 0.625916937155343 0.372905157692314 fatty acid binding protein 2 FUNCTION: FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long- chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor.; . TISSUE SPECIFICITY: Expressed in the small intestine and at much lower levels in the large intestine. Highest expression levels in the jejunum. {ECO:0000269|PubMed:14563446}.; unclassifiable (Anatomical System);placenta;colon; subthalamic nucleus;globus pallidus; 0.13395 0.29754 0.03689118 56.64071715 11.89638 0.43106 FABP3 0.354913336595959 0.591610018258547 0.0534766451454935 fatty acid binding protein 3 FUNCTION: FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.; . . . . 0.18670 . 0.191216164 66.57230479 91.66803 2.05891 FABP3P2 . . . fatty acid binding protein 3 pseudogene 2 . . . . . . . . . . . FABP4 0.00492564212941202 0.692682432129768 0.30239192574082 fatty acid binding protein 4 FUNCTION: Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus (By similarity). {ECO:0000250}.; . . lymphoreticular;myocardium;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;cerebral cortex;bone;testis;dura mater;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;lens;skeletal muscle;breast;pia mater;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;testis - interstitial;adipose tissue;placenta;appendix;ciliary ganglion;fetal thyroid;skin; 0.36529 0.47982 0.169169615 65.33380514 12.2126 0.44235 FABP5 0.09583820082204 0.769607357558743 0.134554441619217 fatty acid binding protein 5 FUNCTION: High specificity for fatty acids. Highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity. May be involved in keratinocyte differentiation.; . TISSUE SPECIFICITY: Keratinocytes; highly expressed in psoriatic skin.; ovary;salivary gland;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;optic nerve;whole body;larynx;gum;bone;thyroid;testis;amniotic fluid;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;lung;cornea;trabecular meshwork;placenta;visual apparatus;hypopharynx;liver;head and neck;kidney;mammary gland;aorta;stomach;thymus; . . 0.13162 0.235309407 68.71903751 14.12358 0.51150 FABP5P1 . . . fatty acid binding protein 5 pseudogene 1 FUNCTION: High specificity for fatty acids. Highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity. May be involved in keratinocyte differentiation.; . TISSUE SPECIFICITY: Keratinocytes; highly expressed in psoriatic skin.; . . . 0.13162 0.235309407 68.71903751 . . FABP5P2 . . . fatty acid binding protein 5 pseudogene 2 . . . . . . . . . . . FABP5P3 . . . fatty acid binding protein 5 pseudogene 3 FUNCTION: High specificity for fatty acids. {ECO:0000250}.; . . . . . 0.13162 . . . . FABP5P4 . . . fatty acid binding protein 5 pseudogene 4 . . . . . . . . . . . FABP5P5 . . . fatty acid binding protein 5 pseudogene 5 . . . . . . . . . . . FABP5P6 . . . fatty acid binding protein 5 pseudogene 6 . . . . . . . . . . . FABP5P7 . . . fatty acid binding protein 5 pseudogene 7 . . . . . . . . . . . FABP5P8 . . . fatty acid binding protein 5 pseudogene 8 . . . . . . . . . . . FABP5P9 . . . fatty acid binding protein 5 pseudogene 9 . . . . . . . . . . . FABP5P10 . . . fatty acid binding protein 5 pseudogene 10 . . . . . . . . . . . FABP5P11 . . . fatty acid binding protein 5 pseudogene 11 . . . . . . . . . . . FABP5P12 . . . fatty acid binding protein 5 pseudogene 12 . . . . . . . . . . . FABP5P13 . . . fatty acid binding protein 5 pseudogene 13 . . . . . . . . . . . FABP5P14 . . . fatty acid binding protein 5 pseudogene 14 . . . . . . . . . . . FABP5P15 . . . fatty acid binding protein 5 pseudogene 15 . . . . . . . . . . . FABP6 0.000205946389112365 0.490415279127064 0.509378774483824 fatty acid binding protein 6 FUNCTION: Ileal protein which stimulates gastric acid and pepsinogen secretion. Seems to be able to bind to bile salts and bilirubins. Isoform 2 is essential for the survival of colon cancer cells to bile acid-induced apoptosis. {ECO:0000269|PubMed:17909007}.; . TISSUE SPECIFICITY: Isoform 2 is expressed in colorectal adenocarcinomas and their adjacent normal mucosa (at protein level). Isoform 1 is expressed in the jejunum, ileum, cecum and ascending colon intestine. Isoform 2 is expressed in the gallbladder, duodenum, jejunum, ileum, cecum, ascending, transverse and descending colon, sigmoid colon and rectum. {ECO:0000269|PubMed:17909007}.; . . 0.15380 0.16481 0.038710339 56.92380278 4736.24502 13.91504 FABP7 0.0907134613307402 0.765548217526699 0.143738321142561 fatty acid binding protein 7 FUNCTION: B-FABP could be involved in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. It is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain and other neural tissues.; unclassifiable (Anatomical System);heart;cerebellum cortex;hypothalamus;fovea centralis;choroid;skin;uterus;whole body;lung;frontal lobe;bone;macula lutea;visual apparatus;hippocampus;kidney;mammary gland;brain;cerebellum; dorsal root ganglion;whole brain;amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;temporal lobe;pons;atrioventricular node;subthalamic nucleus;uterus corpus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.58851 0.13319 -0.09720619 46.20193442 83.68211 1.94623 FABP7P1 . . . fatty acid binding protein 7 pseudogene 1 . . . . . . . . . . . FABP7P2 . . . fatty acid binding protein 7 pseudogene 2 . . . . . . . . . . . FABP9 0.000340176944486432 0.372584491370267 0.627075331685246 fatty acid binding protein 9 . . . . . 0.09393 0.10492 . . 202.77881 3.07428 FABP12 0.00294556959022277 0.582383894126606 0.414670536283172 fatty acid binding protein 12 FUNCTION: May play a role in lipid transport. {ECO:0000250}.; . . lung;testis; superior cervical ganglion;skeletal muscle; . 0.05254 0.281220278 71.07808445 38.80843 1.14857 FABP12P1 . . . fatty acid binding protein 12 pseudogene 1 . . . . . . . . . . . FADD 0.665952895317945 0.311589332495943 0.0224577721861114 Fas associated via death domain FUNCTION: Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling. {ECO:0000269|PubMed:16762833, ECO:0000269|PubMed:19118384, ECO:0000269|PubMed:20935634, ECO:0000269|PubMed:21109225}.; DISEASE: Infections, recurrent, associated with encephalopathy, hepatic dysfunction and cardiovascular malformations (IEHDCM) [MIM:613759]: A condition with biological features of autoimmune lymphoproliferative syndrome such as high-circulating CD4(-)CD8(-)TCR-alpha-beta(+) T-cell counts, and elevated IL10 and FASL levels. Affected individuals suffer from recurrent, stereotypical episodes of fever, encephalopathy, and mild liver dysfunction sometimes accompanied by generalized seizures. The episodes can be triggered by varicella zoster virus (VZV), measles mumps rubella (MMR) attenuated vaccine, parainfluenza virus, and Epstein-Barr virus (EBV). {ECO:0000269|PubMed:21109225}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in a wide variety of tissues, except for peripheral blood mononuclear leukocytes.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; heart;adrenal gland;atrioventricular node;trigeminal ganglion; 0.06427 0.50068 0.058937498 58.26256192 5.23001 0.19483 FADS1 0.383801126989728 0.615762385384928 0.000436487625343874 fatty acid desaturase 1 FUNCTION: Isoform 2 does not exhibit any catalytic activity toward 20:3n-6, but it may enhance FADS2 activity (By similarity). Isoform 1 is a component of a lipid metabolic pathway that catalyzes biosynthesis of highly unsaturated fatty acids (HUFA) from precursor essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3). Catalyzes the desaturation of dihomo-gamma-linoleic acid (DHGLA) (20:3n-6) and eicosatetraenoic acid (20:4n-3) to generate arachidonic acid (AA) (20:4n-6) and eicosapentaenoic acid (EPA)(20:5n-3), respectively. {ECO:0000250, ECO:0000269|PubMed:10601301, ECO:0000269|PubMed:10769175}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in liver, brain, adrenal gland and heart. Highly expressed in fetal liver and brain. {ECO:0000269|PubMed:10601301, ECO:0000269|PubMed:10769175, ECO:0000269|PubMed:10860662}.; myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;synovium;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;placenta;amnion;kidney;stomach; dorsal root ganglion;superior cervical ganglion;adipose tissue;adrenal gland; 0.10578 0.23947 -0.119252484 44.53880632 20.11123 0.68764 FADS2 0.990052486204972 0.0099469297498039 5.84045223988614e-07 fatty acid desaturase 2 FUNCTION: Component of a lipid metabolic pathway that catalyzes biosynthesis of highly unsaturated fatty acids (HUFA) from precursor essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3). Catalyzes the first and rate limiting step in this pathway which is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma- linoleic acid (GLA) (18:3n-6) and stearidonic acid (18:4n-3) respectively and other desaturation steps. Highly unsaturated fatty acids (HUFA) play pivotal roles in many biological functions. It catalizes as well the introduction of a cis double bond in palmitate to produce the mono-unsaturated fatty acid sapienate, the most abundant fatty acid in sebum. {ECO:0000269|PubMed:12713571, ECO:0000269|PubMed:9867867}.; . TISSUE SPECIFICITY: Expressed in a wide array of tissues, highest expression is found in liver followed by brain, lung, heart, and retina. A lower level is found in breast tumor when compared with normal tissues; lowest levels were found in patients with poor prognostic index. {ECO:0000269|PubMed:10860662, ECO:0000269|PubMed:12851727, ECO:0000269|PubMed:9867867}.; lymphoreticular;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;iris;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; adrenal gland;liver; 0.13043 0.27803 -0.383807564 27.41802312 5.86832 0.22092 FADS2P1 . . . fatty acid desaturase 2 pseudogene 1 . . . . . . . . . . . FADS3 0.0488722447276726 0.946277860316892 0.00484989495543598 fatty acid desaturase 3 . . TISSUE SPECIFICITY: Has been found in heart, liver, lung, uterus, and brainstem. {ECO:0000269|PubMed:10860662}.; medulla oblongata;ovary;sympathetic chain;colon;skin;retina;uterus;prostate;optic nerve;cerebral cortex;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;blood;lung;placenta;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland; dorsal root ganglion;placenta;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; . . -0.60427181 17.74593064 18.56228 0.64338 FADS6 2.48053373843411e-07 0.0848948535000815 0.915104898446545 fatty acid desaturase 6 . . . . . 0.10578 . -0.134019284 43.90776126 817.1966 5.61512 FAF1 0.997397841844743 0.00260215725264376 9.02612661243105e-10 Fas associated factor 1 FUNCTION: Potentiates but cannot initiate FAS-induced apoptosis.; . TISSUE SPECIFICITY: Most abundant in testis, slightly less abundant in skeletal muscle and heart, followed by prostate, thymus, ovary, small intestine, and colon. Not detected in the peripheral blood leukocytes.; . . 0.40020 0.10743 -0.424258538 25.56027365 26.29951 0.85309 FAF2 0.998046615446585 0.00195337360036275 1.09530521347531e-08 Fas associated factor family member 2 FUNCTION: Plays an important role in endoplasmic reticulum- associated degradation (ERAD) that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed:18711132, PubMed:24215460). Involved in inhibition of lipid droplet degradation by binding to phospholipase PNPL2 and inhibiting its activity by promoting dissociation of PNPL2 from its endogenous activator, ABHD5 which inhibits the rate of triacylglycerol hydrolysis (PubMed:23297223). {ECO:0000269|PubMed:18711132, ECO:0000269|PubMed:23297223, ECO:0000269|PubMed:24215460}.; . TISSUE SPECIFICITY: Broadly expressed, with highest levels in brain. {ECO:0000269|PubMed:12372427}.; lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;iris;germinal center;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;small intestine;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; testis; 0.56666 0.11640 -0.427900189 25.14744043 21.63519 0.72815 FAF2P1 . . . Fas associated factor family member 2 pseudogene 1 . . . . . . . . . . . FAH 2.80762381206333e-11 0.142874355849813 0.857125644122111 fumarylacetoacetate hydrolase (fumarylacetoacetase) . . TISSUE SPECIFICITY: Mainly expressed in liver and kidney. Lower levels are also detected in many other tissues.; medulla oblongata;ovary;colon;skin;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;pituitary gland;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; liver; 0.14140 0.24341 -0.909290275 10.03184713 149.7435 2.66839 FAHD1 1.1922677900771e-08 0.0146238038265972 0.985376184250725 fumarylacetoacetate hydrolase domain containing 1 FUNCTION: Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro (PubMed:15551868, PubMed:21878618). Also has oxaloacetate decarboxylase activity (PubMed:25575590). {ECO:0000269|PubMed:15551868, ECO:0000269|PubMed:21878618, ECO:0000269|PubMed:25575590}.; . TISSUE SPECIFICITY: Ubiquitous (at protein level). {ECO:0000269|PubMed:21878618}.; . . 0.12357 0.14417 -0.291981272 33.20358575 1357.87776 6.91551 FAHD2A 0.0540720339307648 0.926250732422308 0.0196772336469275 fumarylacetoacetate hydrolase domain containing 2A FUNCTION: May have hydrolase activity. {ECO:0000250}.; . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;pharynx;blood;lung;trabecular meshwork;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;stomach; testis - interstitial;superior cervical ganglion;liver;testis;trigeminal ganglion;parietal lobe; 0.11150 0.11160 -0.670411825 15.61689078 28.33119 0.90693 FAHD2B 0.0279113840334889 0.921824877455926 0.0502637385105852 fumarylacetoacetate hydrolase domain containing 2B FUNCTION: May have hydrolase activity. {ECO:0000250}.; . . lymphoreticular;myocardium;ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;bone marrow;uterus;prostate;whole body;frontal lobe;oesophagus;larynx;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;pharynx;blood;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach; . 0.12112 0.11353 0.283038099 71.26680821 551.68748 4.77743 FAHD2CP . . . fumarylacetoacetate hydrolase domain containing 2C, pseudogene . . . . . . . . . . . FAHD2P1 . . . fumarylacetoacetate hydrolase domain containing 2 pseudogene 1 . . . . . . . . . . . FAIM 0.0681171937664527 0.871676576352671 0.0602062298808761 Fas apoptotic inhibitory molecule FUNCTION: Plays a role as an inducible effector molecule that mediates Fas resistance produced by surface Ig engagement in B cells. {ECO:0000250}.; . . ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;pancreas;lung;nasopharynx;placenta;trabecular meshwork;visual apparatus;macula lutea;liver;stomach;thymus; ciliary ganglion;trigeminal ganglion; 0.10450 0.11959 0.170987912 65.5579146 4094.91295 12.69722 FAIM2 0.619353001444294 0.38031148160419 0.000335516951516216 Fas apoptotic inhibitory molecule 2 FUNCTION: Antiapoptotic protein which protects cells uniquely from Fas-induced apoptosis. Regulates Fas-mediated apoptosis in neurons by interfering with caspase-8 activation. May play a role in cerebellar development by affecting cerebellar size, internal granular layer (IGL) thickness, and Purkinje cell (PC) development. {ECO:0000269|PubMed:10535980, ECO:0000269|PubMed:17635665}.; . TISSUE SPECIFICITY: Highly expressed in breast carcinoma tissues. Enhanced expression correlates with the grade of the tumor (grade II/grade III) in primary breast tumors (at protein level). Widely expressed. Expressed at high levels in the brain especially in the hippocampus. {ECO:0000269|PubMed:10535980, ECO:0000269|PubMed:20336406}.; ovary;sympathetic chain;colon;parathyroid;choroid;fovea centralis;retina;prostate;optic nerve;frontal lobe;cerebral cortex;testis;brain;unclassifiable (Anatomical System);amygdala;islets of Langerhans;hypothalamus;lens;skeletal muscle;lung;hippocampus;visual apparatus;macula lutea;stomach;thymus;cerebellum; dorsal root ganglion;amygdala;whole brain;occipital lobe;superior cervical ganglion;thalamus;medulla oblongata;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;atrioventricular node;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;testis;cingulate cortex;parietal lobe;cerebellum; 0.12867 0.11159 -0.293801652 32.93819297 34.11332 1.04566 FALEC . . . focally amplified long non-coding RNA in epithelial cancer . . . . . . . . . . . FAM3A 0.844646763701685 0.152550234176105 0.00280300212221053 family with sequence similarity 3 member A FUNCTION: May act as a defensin against invading fungal microorganisms.; . TISSUE SPECIFICITY: In similar amounts in testis, pancreas, adrenal, placenta, brain, fetal brain, liver, kidney, skeletal muscle and heart.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;hippocampus;macula lutea;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;cerebellum; thalamus;globus pallidus;atrioventricular node;trigeminal ganglion;parietal lobe; 0.24143 0.10878 -0.427900189 25.14744043 9.33497 0.34294 FAM3B 1.17773609454313e-06 0.354957330542549 0.645041491721356 family with sequence similarity 3 member B FUNCTION: Induces apoptosis of alpha and beta cells in a dose- and time-dependent manner. {ECO:0000269|PubMed:16114871}.; . TISSUE SPECIFICITY: Highly expressed in the pancreas. Also found in the colon, kidney, prostate, small intestine and testis. {ECO:0000269|PubMed:16114871}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;uterus;prostate;lung;thyroid;placenta;liver;testis;head and neck;spleen;stomach; superior cervical ganglion;atrioventricular node; 0.05893 0.08671 0.238945317 69.20853975 279.42207 3.58293 FAM3C 0.00108107460535983 0.829468686283147 0.169450239111493 family with sequence similarity 3 member C FUNCTION: May be involved in retinal laminar formation. Promotes epithelial to mesenchymal transition.; . TISSUE SPECIFICITY: Present in most secretory epithelia (at protein level). {ECO:0000269|PubMed:16959614}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;cochlea;endometrium;bone;thyroid;pituitary gland;testis;dura mater;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;breast;pancreas;pia mater;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;cervix;spleen;kidney;mammary gland;stomach;aorta;thymus; amygdala;subthalamic nucleus;thyroid;prefrontal cortex;globus pallidus;parietal lobe; 0.14569 0.10378 -0.207437529 38.2814343 7.15758 0.26837 FAM3C2 . . . family with sequence similarity 3 member C2 (pseudogene) . . . unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;colon;skin;uterus;breast;pancreas;lung;mesenchyma;visual apparatus;testis;spleen;germinal center;spinal ganglion;brain;mammary gland; . . . . . . . FAM3D 0.00403090933804102 0.959459475654538 0.0365096150074211 family with sequence similarity 3 member D . . TISSUE SPECIFICITY: Abundantly expressed in placenta and weakly expressed in small intestine. {ECO:0000269|PubMed:12160727}.; unclassifiable (Anatomical System);lung;heart;islets of Langerhans;thyroid;colon;cervix;head and neck;mammary gland;skeletal muscle;stomach; trachea;tongue; 0.05290 0.09521 0.262810045 70.43524416 38.8879 1.15175 FAM3D-AS1 . . . FAM3D antisense RNA 1 . . . . . . . . . . . FAM8A1 0.170367796343802 0.826760626435561 0.00287157722063765 family with sequence similarity 8 member A1 . . TISSUE SPECIFICITY: Ubiquitously expressed, with a higher level of expression in testis. {ECO:0000269|PubMed:11707071}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;thyroid;testis;dura mater;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;lens;skeletal muscle;bile duct;breast;pancreas;pia mater;lung;adrenal gland;placenta;macula lutea;liver;head and neck;kidney;mammary gland;stomach; amygdala;superior cervical ganglion;prefrontal cortex;ciliary ganglion;caudate nucleus;parietal lobe;cingulate cortex; 0.32001 0.09845 . . 13.63508 0.49529 FAM8A2P . . . family with sequence similarity 8 member A2, pseudogene . . . . . . . . . . . FAM8A3P . . . family with sequence similarity 8 member A3, pseudogene . . . . . . . . . . . FAM8A4P . . . family with sequence similarity 8 member A4, pseudogene . . . . . . . . . . . FAM8A5P . . . family with sequence similarity 8 member A5, pseudogene . . . . . . . . . . . FAM8A6P . . . family with sequence similarity 8 member A6, pseudogene . . . . . . . . . . . FAM8A7P . . . family with sequence similarity 8 member A7, pseudogene . . . . . . . . . . . FAM8A9P . . . family with sequence similarity 8 member A9, pseudogene . . . . . . . . . . . FAM8A10P . . . family with sequence similarity 8 member A10, pseudogene . . . . . . . . . . . FAM9A 2.85647915187388e-05 0.330046143363933 0.669925291844548 family with sequence similarity 9 member A . . TISSUE SPECIFICITY: Expressed exclusively in testis. {ECO:0000269|PubMed:12213195}.; . . 0.06388 . 0.283038099 71.26680821 266.1444 3.49912 FAM9B 9.496950290472e-05 0.344602061688842 0.655302968808253 family with sequence similarity 9 member B . . TISSUE SPECIFICITY: Expressed exclusively in testis. {ECO:0000269|PubMed:12213195}.; lung;bone;testis;cervix; . 0.04436 . 0.03689118 56.64071715 14.04643 0.50975 FAM9C 5.54037336232307e-05 0.263177425476651 0.736767170789726 family with sequence similarity 9 member C . . TISSUE SPECIFICITY: Expressed exclusively in testis. {ECO:0000269|PubMed:12213195}.; unclassifiable (Anatomical System);stomach; . 0.00768 . -0.207437529 38.2814343 8.63009 0.31659 FAM13A 2.45411477501299e-14 0.950345244499659 0.049654755500316 family with sequence similarity 13 member A . . TISSUE SPECIFICITY: Isoform 1 is widely expressed, with highest expression in skeletal muscle, thymus, brain and lung. Isoform 3 is less abundant than isoform 1 and predominantly expressed in kidney, pancreas,liver, lung and thymus. {ECO:0000269|PubMed:15234000}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;oesophagus;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;urinary;blood;skeletal muscle;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;aorta;stomach;cerebellum; superior cervical ganglion;thyroid;placenta;prefrontal cortex;globus pallidus;trigeminal ganglion; 0.11030 0.11643 -0.369255208 28.25548478 433.44617 4.34475 FAM13A-AS1 . . . FAM13A antisense RNA 1 . . . . . . . . . . . FAM13B 0.900071909481818 0.0999280278545732 6.26636081968545e-08 family with sequence similarity 13 member B . . . ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;islets of Langerhans;adrenal cortex;blood;breast;lung;adrenal gland;placenta;liver;spleen;cervix;kidney;stomach; amygdala;dorsal root ganglion;medulla oblongata;occipital lobe;hypothalamus;pons;caudate nucleus;atrioventricular node;subthalamic nucleus;fetal brain;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.36494 0.12763 -0.995664936 8.539749941 288.15523 3.63441 FAM13C 0.000441695756137109 0.997947005809164 0.00161129843469854 family with sequence similarity 13 member C . . . smooth muscle;ovary;parathyroid;choroid;fovea centralis;skin;retina;uterus;optic nerve;whole body;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;kidney;stomach;aorta; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.60399 0.07743 0.755110637 86.7539514 188.80308 2.98285 FAM19A1 0.861963100838969 0.135979471726574 0.00205742743445693 family with sequence similarity 19 (chemokine (C-C motif)-like), member A1 . . TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:15028294}.; . . 0.48906 0.11262 -0.075159878 47.78839349 5.97949 0.22442 FAM19A2 0.547457170346071 0.43868992155336 0.0138529081005683 family with sequence similarity 19 (chemokine (C-C motif)-like), member A2 . . TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:15028294}.; . . 0.48543 0.09934 0.21326276 67.71644256 15.92723 0.56478 FAM19A3 0.0271473784019524 0.793450356658405 0.179402264939643 family with sequence similarity 19 (chemokine (C-C motif)-like), member A3 . . TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:15028294}.; lung;heart;bone;testis;choroid;retina; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16333 . 0.903992902 89.39018636 146.42865 2.63649 FAM19A4 0.198148820346351 0.756390433923599 0.0454607457300501 family with sequence similarity 19 (chemokine (C-C motif)-like), member A4 . . TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:15028294}.; unclassifiable (Anatomical System);lung;whole body;hypothalamus;hippocampus;testis;pineal gland; globus pallidus;ciliary ganglion;atrioventricular node;skin; 0.09818 0.09240 0.058937498 58.26256192 31.7283 0.99929 FAM19A5 0.310031381590844 0.617806908774345 0.0721617096348112 family with sequence similarity 19 (chemokine (C-C motif)-like), member A5 . . TISSUE SPECIFICITY: Isoform 2 is brain-specific. {ECO:0000269|PubMed:15028294}.; unclassifiable (Anatomical System);lung;ovary;hypothalamus;placenta;liver;testis;parathyroid;spleen;choroid;brain; amygdala;whole brain;subthalamic nucleus;superior cervical ganglion;medulla oblongata;globus pallidus;cingulate cortex;cerebellum; 0.13152 . 0.347360312 73.97381458 13.36073 0.48609 FAM20A 0.00250112243343209 0.994263791850269 0.00323508571629914 family with sequence similarity 20 member A FUNCTION: Pseudokinase that acts as an allosteric activator of the Golgi serine/threonine protein kinase FAM20C and is involved in biomineralization of teeth. Forms a complex with FAM20C and increases the ability of FAM20C to phosphorylate the proteins that form the 'matrix' that guides the deposition of the enamel minerals. {ECO:0000269|PubMed:25789606}.; DISEASE: Amelogenesis imperfecta 1G (AI1G) [MIM:204690]: A disorder characterized by dental anomalies, gingival overgrowth, and nephrocalcinosis. Dental anomalies include hypoplastic amelogenesis imperfecta, intrapulpal calcifications, delay of tooth eruption, hypodontia/oligodontia, pericoronal radiolucencies and unerupted teeth. {ECO:0000269|PubMed:21549343, ECO:0000269|PubMed:21990045, ECO:0000269|PubMed:23434854, ECO:0000269|PubMed:23468644, ECO:0000269|PubMed:23697977, ECO:0000269|PubMed:24196488, ECO:0000269|PubMed:24259279, ECO:0000269|PubMed:24756937, ECO:0000269|PubMed:25636655, ECO:0000269|PubMed:25789606, ECO:0000269|PubMed:25827751}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in lung and liver. Intermediate levels in thymus and ovary. {ECO:0000269|PubMed:15676076}.; ovary;colon;choroid;fovea centralis;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;brain;unclassifiable (Anatomical System);tongue;lens;lung;epididymis;placenta;visual apparatus;macula lutea;liver;alveolus;spleen;head and neck;kidney;mammary gland; trigeminal ganglion; 0.15812 0.11059 -0.356299879 29.31115829 3377.18408 11.12635 FAM20B 0.285813780362229 0.713232893703707 0.000953325934064074 family with sequence similarity 20 member B FUNCTION: Responsible for the 2-O-phosphorylation of xylose in the glycosaminoglycan-protein linkage region of proteoglycans thereby regulating the amount of mature GAG chains. Sulfated glycosaminoglycans (GAGs), including heparan sulfate and chondroitin sulfate, are synthesized on the so-called common GAG- protein linkage region (GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1- O-Ser) of core proteins, which is formed by the stepwise addition of monosaccharide residues by the respective specific glycosyltransferases. Xylose 2-O-phosphorylation may influence the catalytic activity of B3GAT3 (GlcAT-I) which completes the precursor tetrasaccharide of GAG-protein linkage regions on which the repeating disaccharide region is synthesized. {ECO:0000269|PubMed:19473117, ECO:0000269|PubMed:24425863}.; . TISSUE SPECIFICITY: Widely expressed. Strongly expressed in pancreas, spleen and fetal liver. {ECO:0000269|PubMed:15676076, ECO:0000269|PubMed:24425863}.; myocardium;smooth muscle;ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;uterus;prostate;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;skeletal muscle;bile duct;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; amygdala;superior cervical ganglion;occipital lobe;trigeminal ganglion;parietal lobe;skeletal muscle; 0.44067 0.11201 -0.115612493 45.12856806 46.84331 1.32329 FAM20C 0.587993382102887 0.370943116495888 0.0410635014012255 family with sequence similarity 20 member C FUNCTION: Golgi serine/threonine protein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs and plays a key role in biomineralization of bones and teeth (PubMed:22582013, PubMed:23754375, PubMed:25789606). Constitutes the main protein kinase for extracellular proteins, generating the majority of the extracellular phosphoproteome (PubMed:26091039). Mainly phosphorylates proteins within the Ser- x-Glu/pSer motif, but also displays a broader substrate specificity (PubMed:26091039). Phosphorylates casein as well as a number of proteins involved in biomineralization such as AMELX, AMTN, ENAM and SPP1 (PubMed:22582013, PubMed:25789606). In addition to its role in biomineralization, also plays a role in lipid homeostasis, wound healing and cell migration and adhesion (PubMed:26091039). {ECO:0000269|PubMed:22582013, ECO:0000269|PubMed:23754375, ECO:0000269|PubMed:25789606, ECO:0000269|PubMed:26091039}.; DISEASE: Raine syndrome (RNS) [MIM:259775]: Autosomal recessive osteosclerotic bone dysplasia with neonatal lethal outcome. Clinical features include generalized osteosclerosis, craniofacial dysplasia and microcephaly. {ECO:0000269|PubMed:17924334, ECO:0000269|PubMed:22582013, ECO:0000269|PubMed:25789606}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15676076}.; unclassifiable (Anatomical System);ovary;kidney;brain; kidney; 0.07558 . 1.572740636 95.70653456 380.64486 4.11254 FAM21A . . . family with sequence similarity 21 member A FUNCTION: Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes inhibits WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization and is involved in the fission of tubules that serve as transport intermediates during endosome sorting. Mediates the recruitment of the WASH core complex to endosome membranes via binding to phospholipids and VPS35 of the retromer CSC. Mediates the recruitment of the F-actin-capping protein dimer to the WASH core complex probably promoting localized F-actin polymerization needed for vesicle scission. Via its C-terminus binds various phospholipids, most strongly phosphatidylinositol 4-phosphate (PtdIns-(4)P), phosphatidylinositol 5-phosphate (PtdIns-(5)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. Required for the association of DNAJC13, SDCCAG3, ANKRD50 with retromer CSC subunit VPS35. Required for the endosomal recruitment of CCC complex subunits COMMD1, CCDC93 and C16orf62. Plays a role in fluid-phase endocytosis, a process exploited by vaccinia intracellular mature virus (IMV) to enter cells. As a result, may facilitate the penetration of IMV into cells (By similarity). {ECO:0000250|UniProtKB:Q9Y4E1}.; . . lymphoreticular;ovary;adrenal medulla;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; . . . . . 2734.88168 9.85973 FAM21C . . . family with sequence similarity 21 member C FUNCTION: Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes inhibits WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization and is involved in the fission of tubules that serve as transport intermediates during endosome sorting. Mediates the recruitment of the WASH core complex to endosome membranes via binding to phospholipids and VPS35 of the retromer CSC. Mediates the recruitment of the F-actin-capping protein dimer to the WASH core complex probably promoting localized F-actin polymerization needed for vesicle scission (PubMed:19922874, PubMed:20498093, PubMed:22513087, PubMed:23331060). Via its C-terminus binds various phospholipids, most strongly phosphatidylinositol 4- phosphate (PtdIns-(4)P), phosphatidylinositol 5-phosphate (PtdIns- (5)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1 (PubMed:25278552). Required for the association of DNAJC13, SDCCAG3, ANKRD50 with retromer CSC subunit VPS35 (PubMed:24980502). Required for the endosomal recruitment of CCC complex subunits COMMD1, CCDC93 AND C16orf62 (PubMed:25355947). Plays a role in fluid-phase endocytosis, a process exploited by vaccinia intracellular mature virus (IMV) to enter cells. As a result, may facilitate the penetration of IMV into cells (PubMed:18550675). {ECO:0000269|PubMed:18550675, ECO:0000269|PubMed:19922874, ECO:0000269|PubMed:20498093, ECO:0000269|PubMed:22513087, ECO:0000269|PubMed:23331060, ECO:0000269|PubMed:24980502, ECO:0000269|PubMed:25278552, ECO:0000269|PubMed:25355947}.; . . lymphoreticular;ovary;adrenal medulla;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;urinary;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus;cerebellum; . . 0.08281 . . 2123.81367 8.48531 FAM21D . . . family with sequence similarity 21 member D . . . lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;blood;lens;breast;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . . 0.08281 . . . . FAM21EP . . . family with sequence similarity 21 member E, pseudogene . . . . . . . . . . . FAM21FP . . . family with sequence similarity 21 member F, pseudogene . . . . . . . . . . . FAM24A 0.167839101766311 0.641366927118146 0.190793971115543 family with sequence similarity 24 member A . . . . . 0.04570 . -0.075159878 47.78839349 19.37663 0.66610 FAM24B 0.0336499409548214 0.615478659010646 0.350871400034532 family with sequence similarity 24 member B . . . . . 0.03386 . 0.169169615 65.33380514 2.89239 0.10541 FAM25A . . . family with sequence similarity 25 member A . . . unclassifiable (Anatomical System);lung;placenta;testis;blood;bone marrow; . . . . . 219.44164 3.20466 FAM25BP . . . family with sequence similarity 25 member B, pseudogene . . . . . . . . . . . FAM25C . . . family with sequence similarity 25 member C . . . unclassifiable (Anatomical System);lung;placenta;testis;blood;bone marrow; . . . . . 5.85078 0.22045 FAM25D . . . family with sequence similarity 25 member D . . . . . . . . . . . FAM25E . . . family with sequence similarity 25 member E . . . . . . . . . . . FAM25G . . . family with sequence similarity 25 member G . . . unclassifiable (Anatomical System);lung;placenta;testis;blood;bone marrow; . . . . . . . FAM26D 0.0338388220536114 0.616579732816341 0.349581445130047 family with sequence similarity 26 member D FUNCTION: Pore-forming subunit of a voltage-gated ion channel. {ECO:0000250}.; . . . . 0.04547 . -0.141298762 42.87567823 675.33683 5.18929 FAM26E 0.00110838835995408 0.612647200395886 0.38624441124416 family with sequence similarity 26 member E FUNCTION: Pore-forming subunit of a voltage-gated ion channel. {ECO:0000250}.; . . . . 0.56443 . 0.328949044 73.41354093 64.66715 1.64998 FAM26F 1.79931863021701e-05 0.1442218283755 0.855760178438198 family with sequence similarity 26 member F FUNCTION: Pore-forming subunit of a voltage-gated ion channel. {ECO:0000250}.; . . . . 0.05778 . . . 2565.4477 9.46343 FAM27B . . . family with sequence similarity 27 member B . . . . . 0.05206 . . . . . FAM27C . . . family with sequence similarity 27 member C . . . . . 0.12954 . . . . . FAM27D1 . . . family with sequence similarity 27 member D1 . . . . . . . . . . . FAM27E2 . . . family with sequence similarity 27 member E2 . . . . . . . . . 582.12532 4.89167 FAM27E3 . . . family with sequence similarity 27 member E3 . . . unclassifiable (Anatomical System);cervix; . . . . . 2.25256 0.07571 FAM27E4 . . . family with sequence similarity 27 member E4 . . . . . . . . . . . FAM27E5 . . . family with sequence similarity E5 . . . . . 0.22445 . . . . . FAM32A 0.00905286803934175 0.582308132786717 0.408638999173941 family with sequence similarity 32 member A FUNCTION: Isoform 1, but not isoform 2 or isoform 3, may induce G2 arrest and apoptosis. May also increase cell sensitivity to apoptotic stimuli. {ECO:0000269|PubMed:21339736}.; . TISSUE SPECIFICITY: Expressed in ovary, with isoform 1 being predominant. {ECO:0000269|PubMed:21339736}.; lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;oral cavity;bile duct;pancreas;lung;cornea;placenta;hypopharynx;head and neck;kidney;stomach; skeletal muscle; 0.21065 0.11262 0.079165051 59.43029016 14.39403 0.51950 FAM32BP . . . family with sequence similarity 32 member B, pseudogene . . . . . . . . . . . FAM32CP . . . family with sequence similarity 32 member C, pseudogene . . . . . . . . . . . FAM32DP . . . family with sequence similarity 32 member D, pseudogene . . . . . . . . . . . FAM32EP . . . family with sequence similarity 32 member E, pseudogene . . . . . . . . . . . FAM35A 0.156586368560935 0.840044007491038 0.00336962394802646 family with sequence similarity 35 member A . . . colon;choroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;placenta;visual apparatus;macula lutea;liver;kidney;mammary gland;stomach; . . 0.07931 -0.067881249 48.69072895 4261.11405 12.97888 FAM35BP . . . family with sequence similarity 35 member B, pseudogene . . . . . . . . . . . FAM35CP . . . family with sequence similarity 35 member C, pseudogene . . . . . . . . . . . FAM35DP . . . family with sequence similarity 35 member D, pseudogene . . . . . . 0.08731 . . . . FAM41AY1 . . . family with sequence similarity 41 member A, Y-linked 1 . . . . . . . . . . . FAM41AY2 . . . family with sequence similarity 41 member A, Y-linked 2 . . . . . . . . . . . FAM41C . . . family with sequence similarity 41 member C . . . . . . . . . . . FAM43A . . . family with sequence similarity 43 member A . . . . . 0.45758 0.11009 . . 138.44008 2.56175 FAM43B . . . family with sequence similarity 43 member B . . . unclassifiable (Anatomical System);uterus;lung;bone; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.45014 . . . 14.81864 0.53354 FAM45A 0.000243198672562155 0.923088119197785 0.0766686821296525 family with sequence similarity 45 member A . . . ovary;salivary gland;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;amnion;liver;head and neck;kidney;mammary gland;stomach; . . 0.07038 0.128714042 63.19886766 74.89007 1.81105 FAM45BP . . . family with sequence similarity 45 member B, pseudogene . . . . . . 0.06956 . . . . FAM46A 0.34745796945762 0.639079069233481 0.013462961308899 family with sequence similarity 46 member A . . TISSUE SPECIFICITY: Widely expressed, with preferential expression observed in the retina compared to other ocular tissues. {ECO:0000269|PubMed:12054608}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; uterus;prostate;trachea;salivary gland;placenta;adrenal cortex;ciliary ganglion;pituitary;bone marrow; 0.94550 0.10561 0.238945317 69.20853975 98.13789 2.14211 FAM46B 0.0511898745130631 0.860804368771494 0.0880057567154433 family with sequence similarity 46 member B . . . unclassifiable (Anatomical System);ovary;parathyroid;skin;retina;uterus;prostate;lung;epididymis;placenta;thyroid;bone;visual apparatus;iris;testis;brain; superior cervical ganglion;tongue;ciliary ganglion;trigeminal ganglion; 0.61834 0.10784 -0.468351206 23.42533616 1686.27108 7.56791 FAM46C 0.523539097501889 0.459890812031446 0.0165700904666651 family with sequence similarity 46 member C FUNCTION: Seems to enhance replication of some viruses, including yellow fever virus, in response to type I interferon. {ECO:0000269|PubMed:21478870}.; . . . . 0.56632 0.11049 -0.113792788 45.25831564 50.1058 1.38975 FAM46D 0.67476351159847 0.30441430401743 0.0208221843841001 family with sequence similarity 46 member D . . . unclassifiable (Anatomical System);testis;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.29221 0.07473 -0.0274281 51.65723048 10.15403 0.37018 FAM47A 0.748400418346306 0.249365908622197 0.00223367303149726 family with sequence similarity 47 member A . . . . . 0.02900 . 1.223576934 93.23543289 70.3477 1.74418 FAM47B 0.000117993061079711 0.382239079520397 0.617642927418523 family with sequence similarity 47 member B . . . . . 0.03716 . 1.86668643 97.19863175 109.32312 2.27091 FAM47C 0.0577973111457409 0.86697677999908 0.0752259088551793 family with sequence similarity 47 member C . . . . . 0.03714 . 1.76190403 96.75041283 797.36508 5.56605 FAM47DP . . . family with sequence similarity 47 member D, pseudogene . . . . . . . . . . . FAM47E 0.341134282192102 0.485778602045648 0.17308711576225 family with sequence similarity 47 member E . . . ovary;islets of Langerhans;colon;fovea centralis;choroid;lens;retina;optic nerve;lung;frontal lobe;placenta;macula lutea;liver;testis;spleen;kidney;brain; dorsal root ganglion;testis - interstitial;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;skeletal muscle; . . 1.480910504 95.29959896 37.91552 1.12578 FAM47E-STBD1 1.57859436993511e-07 0.0656001952909573 0.934399646849606 FAM47E-STBD1 readthrough . . . . . . . . . 724.25132 5.34232 FAM49A 0.805360676032756 0.194594334966951 4.49890002935527e-05 family with sequence similarity 49 member A . . . ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;lens;skeletal muscle;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;kidney;mammary gland; amygdala;medulla oblongata;thalamus;superior cervical ganglion;occipital lobe;temporal lobe;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.24628 0.11262 -0.141298762 42.87567823 2.12358 0.07074 FAM49B 0.996856902184787 0.00314292511020005 1.72705013218177e-07 family with sequence similarity 49 member B . . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;oral cavity;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;head and neck;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;occipital lobe;appendix;trigeminal ganglion;whole blood; 0.64302 0.11262 -0.075159878 47.78839349 6.91851 0.25776 FAM50A 0.945400813260401 0.0545597638855868 3.9422854011715e-05 family with sequence similarity 50 member A FUNCTION: May be a DNA-binding protein or transcriptional factor. {ECO:0000269|PubMed:9339379}.; . TISSUE SPECIFICITY: Expressed in all tissues examined. Mostly abundant in fetal brain, liver and kidney; in the adult, high levels were also observed in heart, skeletal muscle, spleen, thymus, prostate and small intestine. {ECO:0000269|PubMed:9339379}.; smooth muscle;ovary;colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;adrenal cortex;blood;lens;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach;aorta; skeletal muscle; 0.09076 0.14095 -0.007201372 53.19061099 4.30709 0.15645 FAM50B 0.195542493403811 0.757898835871355 0.0465586707248346 family with sequence similarity 50 member B . . TISSUE SPECIFICITY: Widely expressed. Mostly abundant in testis and adult and fetal brain.; . . 0.13610 . 0.016664174 55.21939137 32.24195 1.00937 FAM53A 3.00698000612452e-05 0.338433051659038 0.661536878540901 family with sequence similarity 53 member A FUNCTION: May play an important role in neural development; the dorsomedial roof of the third ventricle. {ECO:0000250}.; . . pancreas;stomach; . 0.08649 . . . 1340.12163 6.87098 FAM53B 0.40047960162071 0.590465448851629 0.00905494952766115 family with sequence similarity 53 member B . . TISSUE SPECIFICITY: Detected in skeletal muscle, kidney, spleen, thyroid, testis, ovary, small intestine, colon and peripheral blood. {ECO:0000269|PubMed:8590280}.; lymphoreticular;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;spinal cord;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;bone marrow; 0.25894 0.10449 -0.354480518 29.42911064 34.73119 1.05867 FAM53B-AS1 . . . FAM53B antisense RNA 1 . . . . . . . . . . . FAM53C 0.639249208225445 0.359370432593125 0.00138035918143002 family with sequence similarity 53 member C . . . smooth muscle;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; amygdala;prefrontal cortex;testis;ciliary ganglion;trigeminal ganglion;cerebellum; 0.66065 0.10755 -0.381986487 27.68931352 51.92484 1.42321 FAM57A 0.0207651978444373 0.905626602757646 0.0736081993979166 family with sequence similarity 57 member A . . TISSUE SPECIFICITY: Highly expressed in pancreas. Detected at intermediate levels in heart, placenta and kidney, and at low levels in brain, liver and skeletal muscle. Not detected in normal lung. {ECO:0000269|PubMed:12270127}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;endometrium;synovium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;lens;bile duct;lung;placenta;macula lutea;liver;hypopharynx;spleen;head and neck;stomach;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.10590 0.08656 -0.516085732 21.20193442 22.16868 0.74367 FAM57B 0.285736245520272 0.692579589196252 0.0216841652834764 family with sequence similarity 57 member B FUNCTION: Involved in ceramide synthesis. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;choroid;fovea centralis;skin;retina;optic nerve;whole body;frontal lobe;testis;brain;unclassifiable (Anatomical System);pharynx;blood;lens;pancreas;lung;cornea;visual apparatus;macula lutea;liver;kidney;mammary gland;cerebellum; . 0.32096 . -0.405853867 26.23260203 517.79767 4.65250 FAM58A 0.840139167823986 0.156838866660589 0.00302196551542456 family with sequence similarity 58 member A FUNCTION: Activating cyclin for the cyclin-associated kinase CDK10. {ECO:0000269|PubMed:18297069, ECO:0000269|PubMed:24218572}.; DISEASE: Toe syndactyly, telecanthus, and anogenital and renal malformations (STAR) [MIM:300707]: A syndrome characterized by anal, genital and renal tract anomalies, facial dysmorphism and syndactyly. Features include anal stenosis, a rectovaginal fistula, clitoral hypertrophy, a pelvic right kidney, toe syndactyly, and telecanthus. {ECO:0000269|PubMed:18297069}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);smooth muscle;ovary;salivary gland;urinary;colon;blood;choroid;lens;skeletal muscle;pancreas;optic nerve;whole body;lung;frontal lobe;endometrium;placenta;liver;testis;cervix;kidney;brain;tonsil;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.15774 0.09700 . . 14.6063 0.52626 FAM58BP . . . family with sequence similarity 58 member B, pseudogene . . TISSUE SPECIFICITY: Expressed in normal breast, breast cancer cell lines, healthy retina and retinoblastoma. {ECO:0000269|PubMed:15897902}.; . . . . . . . . FAM58CP . . . family with sequence similarity 58 member C, pseudogene . . . . . . . . . . . FAM58DP . . . family with sequence similarity 58 member D, pseudogene . . . . . . . . . . . FAM60A 0.936959839782085 0.062762562213348 0.000277598004566822 family with sequence similarity 60 member A FUNCTION: Subunit of the Sin3 deacetylase complex (Sin3/HDAC), this subunit is important for the repression of genes encoding components of the TGF-beta signaling pathway. {ECO:0000269|PubMed:22865885, ECO:0000269|PubMed:22984288}.; . . ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;amnion;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;tumor;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.84588 0.14896 0.21326276 67.71644256 26.42559 0.85606 FAM60BP . . . family with sequence similarity 60 member B, pseudogene . . . . . . . . . . . FAM60CP . . . family with sequence similarity 60 member C, pseudogene . . . . . . . . . . . FAM60DP . . . family with sequence similarity 60 member D, pseudogene . . . . . . . . . . . FAM63A 8.24250956861272e-06 0.918956533272664 0.0810352242177676 family with sequence similarity 63 member A . . . unclassifiable (Anatomical System);lymph node;heart;ovary;tongue;islets of Langerhans;parathyroid;skin;skeletal muscle;retina;uterus;prostate;lung;frontal lobe;cochlea;bone;thyroid;placenta;visual apparatus;hippocampus;liver;testis;head and neck;cervix;brain;mammary gland;stomach; atrioventricular node;trigeminal ganglion; 0.06573 0.06370 0.464864541 78.69190847 297.62579 3.68029 FAM63B 0.189061306036796 0.810462013131581 0.000476680831622572 family with sequence similarity 63 member B . . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;muscle;pharynx;blood;lung;placenta;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach;thymus; amygdala;superior cervical ganglion;subthalamic nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12804 . -0.134019284 43.90776126 160.37511 2.76300 FAM64A 0.239012864115994 0.729217345914942 0.0317697899690632 family with sequence similarity 64 member A FUNCTION: During mitosis, may play a role in the control of metaphase-to-anaphase transition. {ECO:0000269|PubMed:18757745}.; . TISSUE SPECIFICITY: Expressed in thymus (at protein level). Detected in spleen, colon, ovary and small intestines. {ECO:0000269|PubMed:16491119, ECO:0000269|PubMed:19383357}.; unclassifiable (Anatomical System);ovary;salivary gland;adrenal cortex;colon;parathyroid;skin;prostate;whole body;lung;endometrium;bone;placenta;visual apparatus;liver;head and neck;brain;stomach; superior cervical ganglion;trigeminal ganglion; 0.16156 0.06450 -0.315847836 31.68789809 346.30271 3.94688 FAM65A 0.895578365834564 0.104421631289025 2.87641127193176e-09 family with sequence similarity 65 member A . . . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;ganglion;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;islets of Langerhans;pancreas;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cerebellum; 0.20827 0.08953 -0.681547523 15.38098608 677.89608 5.20178 FAM65B 0.971310088681335 0.0286883081633201 1.60315534477217e-06 family with sequence similarity 65 member B FUNCTION: Required for hearing (PubMed:24958875). Involved in skeletal muscle development (PubMed:24687993). {ECO:0000269|PubMed:24687993, ECO:0000269|PubMed:24958875}.; DISEASE: Note=FAM65B mutations may be a cause of non-syndromic deafness. A splice site mutation causing in-frame skipping of exon 3 has been found in a large consanguineous kindred with recessive non-syndromic, prelingual, profound hearing loss. The mutation perfectly cosegregates with the phenotype in the family. {ECO:0000269|PubMed:24958875}.; TISSUE SPECIFICITY: Expressed in muscle. Isoform 1 is present in the brain. Isoform 2 is expressed during differentiation of fetal primary myoblasts. Also shows marked expression during cytotrophoblast differentiation. {ECO:0000269|PubMed:17150207, ECO:0000269|PubMed:24687993, ECO:0000269|PubMed:9055809}.; lymphoreticular;ovary;colon;parathyroid;skin;bone marrow;uterus;whole body;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;aorta; amygdala;dorsal root ganglion;superior cervical ganglion;ciliary ganglion;white blood cells;trigeminal ganglion;whole blood; 0.22910 0.09809 2.403294158 98.51969804 2475.38571 9.27337 FAM65C 1.45014435980138e-12 0.521127557387527 0.478872442611023 family with sequence similarity 65 member C . . . unclassifiable (Anatomical System);lung;adrenal gland;liver;testis;blood;bone marrow; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.20745 . -0.716581425 14.29582449 272.21933 3.53556 FAM66A . . . family with sequence similarity 66 member A . . . . . . . . . . . FAM66B . . . family with sequence similarity 66 member B . . . . . . . . . . . FAM66C . . . family with sequence similarity 66 member C . . . . . . . . . . . FAM66D . . . family with sequence similarity 66 member D . . . . . . . . . . . FAM66E . . . family with sequence similarity 66 member E . . . . . . . . . . . FAM69A 0.0908652263134349 0.765680617882664 0.143454155803901 family with sequence similarity 69 member A . . . . . 0.29640 0.10717 0.391453969 75.87284737 47.54737 1.33928 FAM69B 0.00357715901222349 0.841033065138851 0.155389775848926 family with sequence similarity 69 member B . . . . . 0.06938 0.09982 -0.661316159 16.02382637 127.02199 2.45767 FAM69C 0.016640101426451 0.708454567271467 0.274905331302082 family with sequence similarity 69 member C . . . unclassifiable (Anatomical System);medulla oblongata;heart;ovary;hypothalamus;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;whole body;lung;placenta;macula lutea;visual apparatus;testis;brain; . 0.12115 . . . 515.3244 4.64278 FAM71A 2.16426906493996e-10 0.0189447785339238 0.981055221249649 family with sequence similarity 71 member A . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; . 0.15547 . 1.894214943 97.33427695 2843.81408 10.08023 FAM71B 0.00232967390794607 0.924402544434447 0.0732677816576068 family with sequence similarity 71 member B FUNCTION: May be involved in RNA biogenesis. {ECO:0000269|PubMed:17103222}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;hippocampus;testis; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.07340 0.07424 0.490549924 79.54706299 349.51492 3.96178 FAM71BP1 . . . family with sequence similarity 71 member B pseudogene 1 . . . . . . . . . . . FAM71C 0.0299979974622026 0.80768244191844 0.162319560619357 family with sequence similarity 71 member C . . . unclassifiable (Anatomical System);medulla oblongata;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;trigeminal ganglion; 0.05178 0.09345 1.194256079 92.88747346 1515.20965 7.23710 FAM71D . . . family with sequence similarity 71 member D . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; . 0.22408 . -0.157884861 42.05590941 558.78739 4.80085 FAM71E1 0.00613239345260664 0.737056922651469 0.256810683895924 family with sequence similarity 71 member E1 . . . unclassifiable (Anatomical System);ovary;colon;parathyroid;fovea centralis;uterus;prostate;lung;placenta;macula lutea;testis;cervix;kidney; testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.18198 . 0.194852702 67.03231894 119.58351 2.38015 FAM71E2 . . . family with sequence similarity 71 member E2 . . . . . 0.20506 . . . 1495.28202 7.19499 FAM71F1 8.94982212165727e-06 0.533135149281536 0.466855900896343 family with sequence similarity 71 member F1 . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.08451 0.08670 0.350995466 74.37485256 4182.32974 12.85715 FAM71F2 0.0624738918069958 0.869730158731169 0.0677959494618351 family with sequence similarity 71 member F2 . . . . . 0.23028 . 1.284269037 93.76621845 9080.86781 20.58328 FAM72A . . . family with sequence similarity 72 member A FUNCTION: May play a role in the regulation of cellular reactive oxygen species metabolism. May participate in cell growth regulation. {ECO:0000269|PubMed:21317926}.; . TISSUE SPECIFICITY: May be up-regulated in malignant colon cancers, compared to normal colon and colon adenomas. Expression is also elevated in other common cancer types, including breast, lung, uterus, and ovary. {ECO:0000269|PubMed:18676834}.; ovary;colon;skin;uterus;prostate;whole body;larynx;thyroid;bone;testis;germinal center;bladder;unclassifiable (Anatomical System);heart;cartilage;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;duodenum;spleen;head and neck;mammary gland;stomach; . 0.61862 . . . 0.6735 0.01045 FAM72B 0.251829881310335 0.641547537937334 0.106622580752332 family with sequence similarity 72 member B . . . unclassifiable (Anatomical System);cartilage;ovary;colon;blood;skin;skeletal muscle;breast;uterus;prostate;pancreas;whole body;lung;larynx;bone;thyroid;placenta;duodenum;testis;head and neck;germinal center;bladder;stomach; . 0.10172 . . . 454.84337 4.43197 FAM72C . . . family with sequence similarity 72 member C . . . . . . . . . . . FAM72D 0.580818100007918 0.375989552378234 0.0431923476138477 family with sequence similarity 72 member D . . . . . . . . . 644.66701 5.10000 FAM73A 0.000750458579415592 0.998495795919211 0.000753745501373062 family with sequence similarity 73 member A FUNCTION: Regulator of mitochondrial fusion: acts by forming homo- and heterodimers at the mitochondrial outer membrane and facilitating the formation of PLD6/MitoPLD dimers. May act by regulating phospholipid metabolism via PLD6/MitoPLD. {ECO:0000269|PubMed:26711011}.; . . . . 0.34194 . -0.732911333 14.07761264 38.95858 1.15465 FAM73B 0.0035189659568434 0.994498454741951 0.00198257930120575 family with sequence similarity 73 member B FUNCTION: Regulator of mitochondrial fusion: acts by forming homo- and heterodimers at the mitochondrial outer membrane and facilitating the formation of PLD6/MitoPLD dimers. May act by regulating phospholipid metabolism via PLD6/MitoPLD. {ECO:0000269|PubMed:26711011}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;ganglion;frontal lobe;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;muscle;blood;lens;skeletal muscle;breast;lung;epididymis;placenta;macula lutea;alveolus;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; atrioventricular node; 0.12512 0.10354 -0.044015879 50.44821892 1887.73278 7.99123 FAM74A1 . . . family with sequence similarity 74 member A1 . . . . . . . . . . . FAM74A2 . . . family with sequence similarity 74 member A2 . . . . . . . . . . . FAM74A3 . . . family with sequence similarity 74 member A3 . . . lung;testis; . . . . . . . FAM74A4 . . . family with sequence similarity 74 member A4 . . . . . . . . . . . FAM74A6 . . . family with sequence similarity 74 member A6 . . . . . . . . . . . FAM74A7 . . . family with sequence similarity 74 member A7 . . . . . . . . . . . FAM76A 0.000561029444884688 0.893922130277864 0.105516840277251 family with sequence similarity 76 member A . . . unclassifiable (Anatomical System);cartilage;heart;ovary;rectum;parathyroid;skeletal muscle;skin;uterus;prostate;lung;endometrium;adrenal gland;bone;placenta;liver;testis;spleen;mammary gland; superior cervical ganglion;medulla oblongata;testis - interstitial;globus pallidus;pons;atrioventricular node;trigeminal ganglion; 0.34031 . -0.163345027 41.24793583 18.53585 0.64132 FAM76B 0.0224491994808166 0.962119358206831 0.0154314423123523 family with sequence similarity 76 member B . . . unclassifiable (Anatomical System);cartilage;colon;retina;bone marrow;breast;uterus;pancreas;lung;endometrium;adrenal gland;nasopharynx;thyroid;placenta;visual apparatus;alveolus;liver;testis;germinal center;kidney;stomach; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.44457 0.10847 -0.029247611 51.40363293 17.29212 0.60697 FAM78A 0.480800490723991 0.496620200661865 0.0225793086141439 family with sequence similarity 78 member A . . . lymph node;lung;heart;testis;blood;brain;skeletal muscle; . 0.23071 0.12183 -0.427900189 25.14744043 25.56147 0.83340 FAM78B 0.770974373780866 0.221131897617074 0.00789372860205979 family with sequence similarity 78 member B . . . unclassifiable (Anatomical System);whole body;optic nerve;endometrium;macula lutea;fovea centralis;choroid;lens;retina; . 0.76543 . -0.361761279 28.6329323 17.83216 0.62308 FAM81A 0.487072320130673 0.511950502669263 0.000977177200064167 family with sequence similarity 81 member A . . . unclassifiable (Anatomical System);colon;skeletal muscle;uterus;prostate;lung;endometrium;hippocampus;liver;testis;germinal center;brain;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin; 0.18828 . -0.249709319 35.74545883 61.35931 1.59577 FAM81B 5.11790785662586e-06 0.862389633868797 0.137605248223346 family with sequence similarity 81 member B . . . unclassifiable (Anatomical System);medulla oblongata;lung;endometrium;islets of Langerhans;nasopharynx;testis;kidney; superior cervical ganglion;testis - interstitial;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06705 . 0.442818085 77.8544468 421.52117 4.28716 FAM83A 0.00286574578553523 0.805065407649648 0.192068846564817 family with sequence similarity 83 member A FUNCTION: Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both RAS/MAPK and PI3K/AKT/TOR signaling cascades downstream of EGFR. Required for the RAS/MAPK signaling cascade activation upon EGFR stimulation, it also activates both signaling cascades independently of EGFR activation. {ECO:0000269|PubMed:22886303}.; . . unclassifiable (Anatomical System);tongue;urinary;blood;skeletal muscle;uterus;pancreas;prostate;optic nerve;lung;oesophagus;larynx;gum;bone;visual apparatus;cervix;head and neck;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.24165 0.12489 0.839664339 88.29912715 1225.76391 6.61813 FAM83A-AS1 . . . FAM83A antisense RNA 1 . . . . . . . . . . . FAM83B 7.60280952486396e-08 0.973561983425437 0.0264379405464681 family with sequence similarity 83 member B FUNCTION: Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. May activate both the EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling cascades. {ECO:0000269|PubMed:22886302, ECO:0000269|PubMed:23676467, ECO:0000269|PubMed:23912460}.; . . unclassifiable (Anatomical System);testis; atrioventricular node; 0.07919 . -0.479490344 22.81788158 2976.1222 10.34607 FAM83C 3.49242479222024e-05 0.814439448490691 0.185525627261387 family with sequence similarity 83 member C FUNCTION: May play a role in MAPK signaling. {ECO:0000303|PubMed:24736947}.; . . . . 0.07214 0.10851 -0.102878093 45.65935362 2176.91533 8.59318 FAM83C-AS1 . . . FAM83C antisense RNA 1 . . . . . . . . . . . FAM83D 2.57679581643321e-05 0.758545361850981 0.241428870190855 family with sequence similarity 83 member D FUNCTION: Probable proto-oncogene that regulates cell proliferation, growth, migration and epithelial to mesenchymal transition. Through the degradation of FBXW7, may act indirectly on the expression and downstream signaling of MTOR, JUN and MYC (PubMed:24344117). May play also a role in cell proliferation through activation of the ERK1/ERK2 signaling cascade (PubMed:25646692). May also be important for proper chromosome congression and alignment during mitosis through its interaction with KIF22. {ECO:0000269|PubMed:18485706, ECO:0000269|PubMed:24344117, ECO:0000269|PubMed:25646692}.; . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.66298 . 0.374860183 75.43052607 2847.08474 10.08929 FAM83E 6.61984443140011e-06 0.470123090772455 0.529870289383113 family with sequence similarity 83 member E FUNCTION: May play a role in MAPK signaling. {ECO:0000303|PubMed:24736947}.; . . unclassifiable (Anatomical System);prostate;pancreas;lacrimal gland;liver;colon;stomach; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.21444 0.10504 . . 1306.17158 6.79814 FAM83F 0.000400741432694423 0.848815606809672 0.150783651757634 family with sequence similarity 83 member F . . . unclassifiable (Anatomical System);medulla oblongata;lymph node;islets of Langerhans;colon;breast;prostate;lung;placenta;hypopharynx;testis;head and neck;kidney;brain;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.17566 0.12201 0.354632714 74.58126917 2615.96375 9.57877 FAM83G 0.0157267816621613 0.978845051933789 0.00542816640405001 family with sequence similarity 83 member G FUNCTION: May regulate the bone morphogenetic proteins (BMP) pathway. {ECO:0000269|PubMed:24554596}.; . . unclassifiable (Anatomical System);placenta;cervix;germinal center;brain; dorsal root ganglion;ciliary ganglion; 0.06986 . -0.038558137 50.51899033 1649.03079 7.50370 FAM83H 0.884824710028448 0.115121210858674 5.40791128782009e-05 family with sequence similarity 83 member H FUNCTION: May play a major role in the structural organization and calcification of developing enamel (PubMed:18252228). May play a role in keratin cytoskeleton disassembly by recruiting CSNK1A1 to keratin filaments. Thereby, it may regulate epithelial cell migration (PubMed:23902688). {ECO:0000269|PubMed:18252228, ECO:0000269|PubMed:23902688}.; . TISSUE SPECIFICITY: Expressed in the tooth follicle. {ECO:0000269|PubMed:18252228}.; . . 0.27378 0.10604 . . 1586.01963 7.36593 FAM83H-AS1 . . . FAM83H antisense RNA 1 (head to head) . . . . . . . . . . . FAM84A 0.0878163030920847 0.762868639263457 0.149315057644459 family with sequence similarity 84 member A . . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;spinal cord;colon;skin;uterus;lung;cornea;endometrium;placenta;visual apparatus;hippocampus;iris;testis;cervix;kidney;brain;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.15023 0.08134 -0.075159878 47.78839349 16.9347 0.59676 FAM84B 0.0156910063345731 0.696930273052895 0.287378720612532 family with sequence similarity 84 member B . . TISSUE SPECIFICITY: Expressed in esophageal squamous cell carcinomas. {ECO:0000269|PubMed:16490593}.; ovary;colon;parathyroid;skin;retina;uterus;prostate;endometrium;testis;bladder;brain;unclassifiable (Anatomical System);islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;lung;trabecular meshwork;placenta;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.19321 . . . 203.68357 3.07969 FAM85A . . . family with sequence similarity 85 member A . . . . . . . . . . . FAM85B . . . family with sequence similarity 85 member B . . . . . . . . . . . FAM86B1 0.744460341331624 0.244896120983096 0.0106435376852797 family with sequence similarity 86 member B1 . . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;adrenal cortex;colon;parathyroid;skin;uterus;prostate;lung;endometrium;placenta;visual apparatus;duodenum;liver;testis;spleen;kidney;brain;stomach; . . . . . 492.38443 4.56268 FAM86B2 0.674121349080742 0.304940141100216 0.0209385098190423 family with sequence similarity 86 member B2 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;adrenal cortex;pharynx;blood;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;kidney;mammary gland;stomach; . . 0.10249 . . 1835.46297 7.89854 FAM86B3P . . . family with sequence similarity 86 member B3, pseudogene . . . . . . . . . . . FAM86C1 1.47905868931909e-08 0.0317678111351509 0.968232174074262 family with sequence similarity 86 member C1 . . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pineal body;pharynx;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; . 0.09393 . 0.505321956 80.00707714 5743.67103 15.72823 FAM86C2P . . . family with sequence similarity 86 member C2, pseudogene . . . . . . . . . . . FAM86DP . . . family with sequence similarity 86 member D, pseudogene . . . . . 0.06283 . . . . . FAM86EP . . . family with sequence similarity 86 member E, pseudogene . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;pineal body;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;stomach; . . . . . . . FAM86FP . . . family with sequence similarity 86 member F, pseudogene . . . unclassifiable (Anatomical System);liver; . . . . . . . FAM86GP . . . family with sequence similarity 86 member G, pseudogene . . . . . . . . . . . FAM86HP . . . family with sequence similarity 86 member H, pseudogene . . . . . . . . . . . FAM86JP . . . family with sequence similarity 86 member J, pseudogene . . . . . . . . . . . FAM86KP . . . family with sequence similarity 86 member K, pseudogene . . . . . 0.06283 . . . . . FAM86LP . . . family with sequence similarity 86 member L, pseudogene . . . . . . . . . . . FAM86MP . . . family with sequence similarity 86 member M, pseudogene . . . . . . . . . . . FAM87A . . . family with sequence similarity 87 member A . . . unclassifiable (Anatomical System);testis; ciliary ganglion;skeletal muscle; . . . . . . FAM87B . . . family with sequence similarity 87 member B . . . unclassifiable (Anatomical System);bone;testis; . . . . . . . FAM89A 0.0096405423416975 0.595717236988232 0.394642220670071 family with sequence similarity 89 member A . . . . . 0.14111 . . . 32.30404 1.01021 FAM89B 0.0291384645647437 0.586788283653369 0.384073251781887 family with sequence similarity 89 member B FUNCTION: Negatively regulates TGF-beta-induced signaling; in cooperation with SKI prevents the translocation of SMAD2 from the nucleus to the cytoplasm in response to TGF-beta. {ECO:0000250}.; . . ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;blood;skeletal muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;liver;spleen;cervix;kidney;mammary gland;stomach; whole brain;superior cervical ganglion;prefrontal cortex;atrioventricular node;whole blood;skeletal muscle; 0.15431 . . . 14.74223 0.53128 FAM90A1 6.49112967670201e-12 0.00464728669233084 0.995352713301178 family with sequence similarity 90 member A1 . . . unclassifiable (Anatomical System);islets of Langerhans;bone;brain; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.12392 0.07233 1.978773583 97.6232602 5236.32434 14.91295 FAM90A2P . . . family with sequence similarity 90 member A2, pseudogene . . . . . 0.00881 . . . . . FAM90A3P . . . family with sequence similarity 90 member A3, pseudogene . . . . . . . . . . . FAM90A4P . . . family with sequence similarity 90 member A4, pseudogene . . . . . . . . . . . FAM90A5P . . . family with sequence similarity 90 member A5, pseudogene . . . . . . . . . . . FAM90A6P . . . family with sequence similarity 90 member A6, pseudogene . . . . . . . . . . . FAM90A7P . . . family with sequence similarity 90 member A7, pseudogene . . . . . . . . . . . FAM90A8P . . . family with sequence similarity 90 member A8, pseudogene . . . . . . . . . . . FAM90A9P . . . family with sequence similarity 90 member A9, pseudogene . . . . . . . . . . . FAM90A10P . . . family with sequence similarity 90 member A10, pseudogene . . . . . . . . . . . FAM90A11P . . . family with sequence similarity 90 member A11, pseudogene . . . . . . . . . . . FAM90A12P . . . family with sequence similarity 90 member A12, pseudogene . . . . . . . . . . . FAM90A13P . . . family with sequence similarity 90 member A13, pseudogene . . . . . . . . . . . FAM90A14P . . . family with sequence similarity 90 member A14, pseudogene . . . . . . . . . . . FAM90A15P . . . family with sequence similarity 90 member A15, pseudogene . . . . . . . . . . . FAM90A16P . . . family with sequence similarity 90 member A16, pseudogene . . . . . . . . . . . FAM90A17P . . . family with sequence similarity 90 member A17, pseudogene . . . . . . . . . . . FAM90A18P . . . family with sequence similarity 90 member A18, pseudogene . . . . . . . . . . . FAM90A19P . . . family with sequence similarity 90 member A19, pseudogene . . . . . . . . . . . FAM90A20P . . . family with sequence similarity 90 member A20, pseudogene . . . . . . . . . . . FAM90A21P . . . family with sequence similarity 90 member A21, pseudogene . . . . . . . . . . . FAM90A22P . . . family with sequence similarity 90 member A22, pseudogene . . . . . . . . . . . FAM90A23P . . . family with sequence similarity 90 member A23, pseudogene . . . . . . . . . . . FAM90A24P . . . family with sequence similarity 90 member A24, pseudogene . . . . . . . . . . . FAM90A25P . . . family with sequence similarity 90 member A25, pseudogene . . . . . . . . . . . FAM90A26 . . . family with sequence similarity 90 member A26 . . . . . . . . . 2188.92718 8.61895 FAM90A27P . . . family with sequence similarity 90 member A27, pseudogene . . . . . . . . . . . FAM90A28P . . . family with sequence similarity 90 member A28, pseudogene . . . . . . . . . . . FAM91A1 0.515693526571197 0.484306206680873 2.66747929714425e-07 family with sequence similarity 91 member A1 . . . unclassifiable (Anatomical System); superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.30469 . -0.622676946 17.30950696 54.36063 1.47405 FAM91A2P . . . family with sequence similarity 91 member A2, pseudogene . . . . . . . . . . . FAM91A3P . . . family with sequence similarity 91 member A3, pseudogene . . . . . . . . . . . FAM91A4P . . . family with sequence similarity 91 member A4, pseudogene . . . . . . . . . . . FAM92A1 3.68953972008855e-05 0.823709194859705 0.176253909743094 family with sequence similarity 92 member A1 . . . unclassifiable (Anatomical System);heart;skeletal muscle;skin;bone marrow;uterus;endometrium;placenta;thyroid;bone;testis;head and neck;kidney;brain;stomach; . . 0.09004 0.325313577 73.11276244 752.52049 5.44068 FAM92A1P1 . . . family with sequence similarity 92 member A1 pseudogene 1 . . . . . . 0.09004 . . . . FAM92A1P2 . . . family with sequence similarity 92 member A1 pseudogene 2 . . . . . 0.12982 . . . . . FAM92B 3.59457728092944e-11 0.0243597168938082 0.975640283070246 family with sequence similarity 92 member B . . . . . 0.07343 0.09186 0.396906589 76.30927105 291.69998 3.65342 FAM95A . . . family with sequence similarity 95 member A . . . . . . . . . . . FAM95B1 . . . family with sequence similarity 95 member B1 . . . . . . . . . . . FAM95C . . . family with sequence similarity 95 member C . . . . . . . . . . . FAM96A 0.0134508962309797 0.86408084530506 0.122468258463961 family with sequence similarity 96 member A FUNCTION: May play a role in chromosome segregation through establishment of sister chromatid cohesion. {ECO:0000250}.; . TISSUE SPECIFICITY: Substantially enriched in macrophages. {ECO:0000269|PubMed:22683786}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;oesophagus;thyroid;pituitary gland;testis;dura mater;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);meninges;lymph node;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;adrenal cortex;pharynx;blood;lens;breast;bile duct;pancreas;pia mater;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach;thymus; fetal liver; 0.29377 . -0.141298762 42.87567823 5.33243 0.19738 FAM96AP1 . . . family with sequence similarity 96 member A pseudogene 1 . . . . . . . . . . . FAM96AP2 . . . family with sequence similarity 96 member A pseudogene 2 . . . . . . . . . . . FAM96B 0.00210375204791455 0.510385151637808 0.487511096314278 family with sequence similarity 96 member B FUNCTION: Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. {ECO:0000269|PubMed:20797633}.; . . . . 0.24177 0.10692 0.013025609 54.62962963 7.86023 0.28897 FAM98A 0.68941491445387 0.310549554736141 3.55308099880986e-05 family with sequence similarity 98 member A . . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;head and neck;kidney;mammary gland;stomach; amygdala;occipital lobe;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;cingulate cortex;parietal lobe; 0.83067 0.10583 0.132352165 63.48785091 125.01147 2.43232 FAM98B 0.394827182699865 0.60320303156434 0.00196978573579498 family with sequence similarity 98 member B . . . unclassifiable (Anatomical System);uterus;bone;liver;kidney;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.13230 0.08332 -0.361761279 28.6329323 66.65776 1.68388 FAM98C 3.566522831586e-10 0.048395533257487 0.951604466385861 family with sequence similarity 98 member C . . . unclassifiable (Anatomical System);ovary;islets of Langerhans;salivary gland;colon;blood;skeletal muscle;pancreas;whole body;lung;bone;placenta;hippocampus;testis;cervix;kidney;brain;mammary gland;tonsil;stomach; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node; 0.16451 . 0.729426781 86.17008728 1449.69233 7.10399 FAM99A . . . family with sequence similarity 99 member A (non-protein coding) . . . . . . . . . . . FAM99B . . . family with sequence similarity 99 member B (non-protein coding) . . . . . . . . . . . FAM101A 0.212634236356269 0.648047209784885 0.139318553858846 family with sequence similarity 101 member A FUNCTION: Involved in the regulation of the perinuclear actin network and nuclear shape through interaction with filamins. Plays an essential role in actin cytoskeleton formation in developing cartilaginous cells. {ECO:0000250|UniProtKB:Q7TS73}.; . . unclassifiable (Anatomical System);cartilage;muscle;fovea centralis;choroid;lens;retina;bile duct;optic nerve;synovium;macula lutea;visual apparatus;liver;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.18633 0.11097 0.681699246 84.93158764 141.85581 2.59916 FAM101B . . . family with sequence similarity 101 member B FUNCTION: Involved in the regulation of the perinuclear actin network and nuclear shape through interaction with filamins. Plays an essential role in the formation of cartilaginous skeletal elements. {ECO:0000250|UniProtKB:Q5SVD0}.; . . unclassifiable (Anatomical System);lung;salivary gland;placenta;testis;blood;brain;retina;thymus; superior cervical ganglion;bone marrow; 0.26143 0.10024 . . 433.75703 4.34656 FAM102A 0.430347065056518 0.568148523887247 0.00150441105623481 family with sequence similarity 102 member A FUNCTION: May play a role in estrogen action. {ECO:0000269|PubMed:14605097}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.24087 0.12171 -0.580403979 18.58928993 44.26996 1.26912 FAM102B 0.0479307719355573 0.947071769785852 0.0049974582785909 family with sequence similarity 102 member B . . . . . 0.21212 . -0.073340031 48.11866006 16.97459 0.59804 FAM103A1 0.82844521510956 0.167913869112469 0.00364091577797144 family with sequence similarity 103 member A1 FUNCTION: Required for efficient mRNA cap methylation. Regulates RNMT expression by a post-transcriptional stabilizing mechanism. {ECO:0000269|PubMed:22099306}.; . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;thyroid;testis;germinal center;brain;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;bile duct;lung;nasopharynx;placenta;liver;amnion;spleen;kidney;stomach; atrioventricular node; 0.09140 0.10748 0.25917371 70.05779665 177.4953 2.89591 FAM103A2P . . . family with sequence similarity 103 member A2, pseudogene . . . . . . . . . . . FAM104A 0.612044064845623 0.379655368686305 0.00830056646807246 family with sequence similarity 104 member A . . . . . 0.16210 . 0.060756528 58.52795471 44.93114 1.28730 FAM104B 0.00870993932895896 0.574076212934116 0.417213847736925 family with sequence similarity 104 member B . . . breast;prostate;bone;liver;spleen;kidney;skin; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.12752 . 0.413500896 76.67492333 9.21627 0.33742 FAM105A 2.32580771885254e-07 0.275709325726846 0.724290441692383 family with sequence similarity 105 member A . . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;skin;uterus;pancreas;prostate;lung;endometrium;placenta;visual apparatus;iris;pituitary gland;liver;testis;spleen;cervix; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.10280 0.09828 0.106667882 61.73036093 389.06175 4.15395 FAM106A . . . family with sequence similarity 106 member A . . . . . 0.06770 . . . 1.95899 0.06375 FAM106B . . . family with sequence similarity 106 member B . . . . . . . . . . . FAM106CP . . . family with sequence similarity 106 member C, pseudogene . . . . . . . . . . . FAM106DP . . . family with sequence similarity 106 member D, pseudogene . . . . . . . . . . . FAM107A 0.00164508891972831 0.459898287937401 0.53845662314287 family with sequence similarity 107 member A FUNCTION: When transfected into cell lines in which it is not expressed, suppresses cell growth. May play a role in tumor development. {ECO:0000269|PubMed:10564580}.; . TISSUE SPECIFICITY: Widely expressed in normal tissues. Expression is reduced or absent in a number of cancer cell lines. {ECO:0000269|PubMed:10564580}.; smooth muscle;ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;cerebral cortex;thyroid;iris;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;macula lutea;hippocampus;spleen;head and neck;kidney;mammary gland;cerebellum; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.16601 0.14015 0.481458261 79.03986789 1686.63762 7.57171 FAM107B 0.00019611623707521 0.719007881858455 0.28079600190447 family with sequence similarity 107 member B . . . lymphoreticular;smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;prefrontal cortex;parietal lobe; 0.25700 0.08443 -0.025608647 51.91672564 401.93658 4.20511 FAM109A 0.00514982698391651 0.464684894879918 0.530165278136166 family with sequence similarity 109 member A FUNCTION: Plays a role in endocytic trafficking. Required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. {ECO:0000269|PubMed:21233288}.; . . unclassifiable (Anatomical System);ovary;colon;parathyroid;pancreas;prostate;lung;synovium;placenta;visual apparatus;iris;liver;testis;spleen;kidney;brain;peripheral nerve; . 0.13853 . . . 3638.05621 11.71080 FAM109B 0.000109676972120869 0.369261974028399 0.63062834899948 family with sequence similarity 109 member B FUNCTION: Plays a role in endocytic trafficking. Required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. {ECO:0000269|PubMed:21233288}.; . . ovary;colon;parathyroid;skin;bone marrow;uterus;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;mammary gland;stomach;aorta;thymus; globus pallidus;ciliary ganglion; 0.09731 . 0.194852702 67.03231894 153.91357 2.71212 FAM110A 0.74779060333009 0.241941913828315 0.0102674828415948 family with sequence similarity 110 member A . . TISSUE SPECIFICITY: Detected in thyroid, lymph node, trachea, adrenal gland, bone marrow, spleen, thymus, prostate, and peripheral blood leukocyte. Detected at lower levels in stomach, testis and spinal cord. {ECO:0000269|PubMed:17499476}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;bladder;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;tongue;muscle;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; . 0.15136 . . . 131.21573 2.49458 FAM110B 0.172625630799022 0.7695771916741 0.0577971775268781 family with sequence similarity 110 member B FUNCTION: May be involved in tumor progression.; . TISSUE SPECIFICITY: Detected in thyroid, spleen and testis, and at lower levels in stomach, spinal cord, lymph node, trachea, adrenal gland, prostate, ovary and intestine. {ECO:0000269|PubMed:17499476}.; unclassifiable (Anatomical System);ovary;cartilage;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;optic nerve;whole body;lung;frontal lobe;cerebral cortex;endometrium;placenta;bone;macula lutea;liver;testis;kidney;brain; amygdala;whole brain;occipital lobe;fetal brain;cerebellum peduncles;caudate nucleus; 0.16799 0.10844 -0.271755481 34.31823543 18.95041 0.65421 FAM110C 8.70816981585542e-08 0.0465815443868096 0.953418368531492 family with sequence similarity 110 member C FUNCTION: May play a role in microtubule organization. May play a role in cell spreading and cell migration of epithelial cells; the function may involve the AKT1 signaling pathway. {ECO:0000269|PubMed:17499476, ECO:0000269|PubMed:19698782}.; . TISSUE SPECIFICITY: Detected in stomach, thyroid, trachea, adrenal gland and testis, and at low levels in prostate, ovary, intestine, colon, spinal cord and lymph node. {ECO:0000269|PubMed:17499476}.; unclassifiable (Anatomical System);uterus; . 0.10597 0.09932 . . 74.5315 1.80533 FAM110D 0.550404227081523 0.396493198598544 0.0531025743199324 family with sequence similarity 110 member D . . . . . 0.42842 . . . 1309.4018 6.80877 FAM111A 3.22456890783558e-09 0.0477349867982194 0.952265009977212 family with sequence similarity 111 member A FUNCTION: Chromatin-associated protein required for PCNA loading on replication sites. Promotes S-phase entry and DNA synthesis (PubMed:24561620). May directly function at replication forks, explaining why Simian virus 40 (SV40) interacts with FAM111A to overcome host range restriction (PubMed:23093934). {ECO:0000269|PubMed:23093934, ECO:0000269|PubMed:24561620}.; DISEASE: Kenny-Caffey syndrome 2 (KCS2) [MIM:127000]: A disorder characterized by impaired skeletal development with small and dense bones, short stature, and primary hypoparathyroidism with hypocalcemia. Clinical features include cortical thickening and medullary stenosis of the tubular bones, delayed closure of fontanels, defective dentition, small eyes with hypermetropia, and frontal bossing with a triangular face. {ECO:0000269|PubMed:23684011, ECO:0000269|PubMed:23996431, ECO:0000269|PubMed:24635597}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Gracile bone dysplasia (GCLEB) [MIM:602361]: A perinatally lethal condition characterized by narrowing of the medullary cavity of the long bones and of the skull, gracile bones with thin diaphyses, premature closure of basal cranial sutures, and microphthalmia. Most affected individuals who survive beyond the perinatal period develop hypocalcemia with low parathyroid hormone levels. {ECO:0000269|PubMed:23684011}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;white blood cells;trigeminal ganglion; 0.07837 . -0.264476624 34.8844067 206.63586 3.10639 FAM111B 7.17098815107683e-11 0.0691770187995142 0.930822981128776 family with sequence similarity 111 member B . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:24268661}.; unclassifiable (Anatomical System);lung;heart;testis;germinal center; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.06545 . -0.731092527 14.13658882 246.97414 3.38968 FAM114A1 2.38422962541873e-08 0.457538177073708 0.542461799083995 family with sequence similarity 114 member A1 FUNCTION: May play a role in neuronal cell development. {ECO:0000250}.; . . medulla oblongata;ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;larynx;thyroid;bone;testis;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; dorsal root ganglion;superior cervical ganglion;adrenal gland;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11964 . 0.358272123 74.66383581 2541.88338 9.41853 FAM114A2 3.07870322878957e-07 0.763221580198055 0.236778111931622 family with sequence similarity 114 member A2 . . . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;blood;lens;breast;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.10406 0.08373 -0.178111357 40.44585987 244.27833 3.37275 FAM117A 1.21995888453457e-05 0.82474036618659 0.175247434224565 family with sequence similarity 117 member A . . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;optic nerve;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;liver;spleen;kidney;stomach; testis - interstitial;fetal liver;superior cervical ganglion;testis;trigeminal ganglion;skeletal muscle;bone marrow; 0.39399 . -0.181750739 40.15687662 82.49772 1.92819 FAM117B 0.0673870151606627 0.929684121703119 0.00292886313621799 family with sequence similarity 117 member B . . . unclassifiable (Anatomical System);ovary;placenta;parathyroid;blood;kidney;skeletal muscle;bone marrow; superior cervical ganglion;ciliary ganglion;kidney;trigeminal ganglion;cerebellum; 0.40441 0.10989 . . 42.96972 1.24303 FAM118A 0.591868565334658 0.406055483854439 0.00207595081090287 family with sequence similarity 118 member A . . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;synovium;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;lens;skeletal muscle;lung;nasopharynx;placenta;macula lutea;liver;spleen;cervix;kidney;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10583 0.09201 -0.001743238 53.85114414 52.56756 1.43555 FAM118B 0.390427138904487 0.607535918121822 0.002036942973691 family with sequence similarity 118 member B FUNCTION: May play a role in Cajal bodies formation. {ECO:0000269|PubMed:24569877}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;bone;testis;dura mater;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);meninges;cartilage;islets of Langerhans;pharynx;blood;lens;breast;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach; . 0.21181 0.10712 -0.448125345 24.19202642 89.05849 2.02586 FAM120A 0.999907050343555 9.29496498852301e-05 6.55992208311924e-12 family with sequence similarity 120A FUNCTION: May participate in mRNA transport in the cytoplasm (By similarity). Critical component of the oxidative stress-induced survival signaling. Activates src family kinases and acts as a scaffolding protein enabling src family kinases to phosphorylate and activate PI3-kinase. Binds RNA and promotes the secretion of IGF-II. May play a pivotal role in the progression of scirrhous- type gastric cancer by supporting cancer cell survival in environments with various oxidative stresses. {ECO:0000250, ECO:0000269|PubMed:19015244}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in scirrhous-type gastric cancer tissues compared with normal gastric mucosa (at protein level). {ECO:0000269|PubMed:14585507, ECO:0000269|PubMed:19015244}.; lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;bile duct;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;cerebellum; superior cervical ganglion;placenta;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.24853 0.11006 -2.037519759 1.657230479 38.57086 1.14394 FAM120AOS 0.514390706669033 0.467885771290312 0.017723522040655 family with sequence similarity 120A opposite strand . . . . . 0.12217 . 0.970138239 90.23354565 948.12851 5.96368 FAM120B 2.3406676741202e-08 0.971139544863802 0.0288604317295209 family with sequence similarity 120B FUNCTION: Functions as a transactivator of PPARG and ESR1. Functions in adipogenesis through PPARG activation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14585507}.; unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pineal body;colon;blood;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;optic nerve;whole body;lung;frontal lobe;placenta;macula lutea;visual apparatus;testis;kidney;spinal ganglion;brain; amygdala;whole brain;dorsal root ganglion;occipital lobe;medulla oblongata;thalamus;superior cervical ganglion;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.09273 0.08316 1.181302384 92.80490682 1935.1263 8.09595 FAM120C 0.973037034571628 0.026962687243381 2.78184991114711e-07 family with sequence similarity 120C . . TISSUE SPECIFICITY: Expressed at low levels in a number of tissues. {ECO:0000269|PubMed:14585507}.; unclassifiable (Anatomical System);lung;pituitary gland;liver;testis;brain; dorsal root ganglion;superior cervical ganglion;liver;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;cerebellum; 0.53229 0.10318 -0.137658575 43.57159707 68.89853 1.72003 FAM122A 0.800532188149013 0.194028994998109 0.0054388168528784 family with sequence similarity 122A . . . . . 0.57302 . -0.139478553 43.29440906 26.32597 0.85390 FAM122B 0.757591088967366 0.24040130633538 0.00200760469725387 family with sequence similarity 122B . . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;cochlea;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;hypothalamus;urinary;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;stomach;thymus; superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.24481 0.08164 0.347360312 73.97381458 16.09371 0.56984 FAM122C 0.174595943528543 0.768699003360513 0.0567050531109434 family with sequence similarity 122C . . . . . 0.06219 . 0.347360312 73.97381458 55.56403 1.49812 FAM124A 5.43000288891245e-07 0.240489773745443 0.759509683254268 family with sequence similarity 124 member A . . . unclassifiable (Anatomical System);cartilage;heart;ovary;cerebellum cortex;colon;skin;skeletal muscle;retina;uterus;lung;thyroid;placenta;visual apparatus;liver;testis;kidney;brain;stomach;aorta; atrioventricular node;trigeminal ganglion;skin; 0.37251 0.09790 0.154398214 64.73814579 1309.33779 6.80771 FAM124B 0.00229940234451662 0.529159785142823 0.46854081251266 family with sequence similarity 124 member B . . . unclassifiable (Anatomical System);lung;nasopharynx;placenta;testis;spleen;skeletal muscle; superior cervical ganglion;placenta;pons;trigeminal ganglion; 0.07065 0.09019 0.040529541 57.15380986 173.94414 2.87089 FAM126A 0.803307844592117 0.19664583291224 4.63224956431547e-05 family with sequence similarity 126 member A FUNCTION: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane (PubMed:26571211). The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis (PubMed:26571211). FAM126A plays a key role in oligodendrocytes formation, a cell type with expanded plasma membrane that requires generation of PtdIns(4)P (PubMed:26571211). Its role in oligodendrocytes formation probably explains its importance in myelination of the central and peripheral nervous system (PubMed:26571211, PubMed:16951682). May also have a role in the beta-catenin/Lef signaling pathway (Probable). {ECO:0000269|PubMed:16951682, ECO:0000269|PubMed:26571211, ECO:0000305|PubMed:10910037}.; DISEASE: Leukodystrophy, hypomyelinating, 5 (HLD5) [MIM:610532]: A hypomyelinating leukodystrophy associated with congenital cataract. It is clinically characterized by congenital cataract, progressive neurologic impairment, and diffuse myelin deficiency. Affected individuals experience progressive pyramidal and cerebellar dysfunction, muscle weakness and wasting prevailingly in the lower limbs. Mental deficiency ranges from mild to moderate. HLD5 shows clinical variability, but features of hypomyelination combined with increased periventricular white matter water content are consistently observed. {ECO:0000269|PubMed:16951682, ECO:0000269|PubMed:21911699, ECO:0000269|PubMed:23998934}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Highest levels in heart, brain, placenta, spleen and testis. {ECO:0000269|PubMed:10910037}.; . . 0.22734 0.17004 0.264628794 70.5178108 150.95643 2.68566 FAM126B 0.979818816441785 0.0201805114974423 6.72060772594608e-07 family with sequence similarity 126 member B FUNCTION: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. {ECO:0000305|PubMed:26571211}.; . . unclassifiable (Anatomical System);lymph node;islets of Langerhans;colon;parathyroid;blood;skin;skeletal muscle;breast;uterus;pancreas;prostate;lung;bone;placenta;visual apparatus;liver;testis;germinal center;kidney;brain;thymus; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;cerebellum; 0.13455 . -0.426079032 25.36565228 38.41371 1.14019 FAM127A 0.599977362549409 0.362346249657068 0.0376763877935231 family with sequence similarity 127 member A . . . myocardium;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;ganglion;frontal lobe;endometrium;iris;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;uterus;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;head and neck;kidney;aorta;stomach;cerebellum; whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;heart;hypothalamus;temporal lobe;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.04079 0.08874 0.101211609 60.95777306 . . FAM127B 0.0279082981400185 0.578084863461266 0.394006838398716 family with sequence similarity 127 member B . . . . . 0.16386 . 0.479642105 78.95140363 6.08773 0.23027 FAM127C 0.0255981569872327 0.560565943682196 0.413835899330572 family with sequence similarity 127 member C . . . . . 0.10735 . -0.075159878 47.78839349 0.84889 0.01691 FAM129A 1.39592253616035e-13 0.16478000924884 0.83521999075102 family with sequence similarity 129 member A FUNCTION: Regulates phosphorylation of a number of proteins involved in translation regulation including EIF2A, EIF4EBP1 and RPS6KB1. May be involved in the endoplasmic reticulum stress response (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in various types of thyroid tumor such as papillary thyroid carcinomas and oxyphilic thyroid tumors but not in normal thyroid tissue (at protein level). Strongly expressed in heart, skeletal muscle, pancreas, white blood cells and prostate with moderate expression in colon and spleen. Expressed in renal carcinoma cells but not in normal kidney. {ECO:0000269|PubMed:11011112, ECO:0000269|PubMed:16949643}.; . . 0.53295 0.08445 1.208829905 93.05260675 471.32354 4.49277 FAM129B 0.0967032137688596 0.903283319366944 1.34668641968895e-05 family with sequence similarity 129 member B FUNCTION: May play a role in apoptosis suppression. May promote melanoma cell invasion in vitro. {ECO:0000269|PubMed:19362540, ECO:0000269|PubMed:21148485}.; . . . . 0.24632 0.10776 -1.346642726 4.62962963 224.45345 3.23964 FAM129C 1.3407670261693e-10 0.537255646882213 0.46274435298371 family with sequence similarity 129 member C . . TISSUE SPECIFICITY: Specifically expressed in B-lymphocytes. {ECO:0000269|PubMed:12886250}.; unclassifiable (Anatomical System);uterus;lymphoreticular;lymph node;liver;testis;spleen;blood;germinal center; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07921 0.08410 1.581840753 95.7891012 2832.82344 10.04868 FAM131A 0.0313284236342615 0.925656059368452 0.0430155169972863 family with sequence similarity 131 member A . . . ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;lung;placenta;macula lutea;liver;spleen;kidney;stomach;thymus; amygdala;whole brain;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.38029 0.09699 -0.205617011 38.57631517 64.91238 1.65518 FAM131B 0.921928277751244 0.077974185113721 9.75371350347252e-05 family with sequence similarity 131 member B . . . . . 0.53663 . -0.426079032 25.36565228 1759.67089 7.74129 FAM131C 0.276924372627756 0.699812583052299 0.0232630443199451 family with sequence similarity 131 member C . . . . . 0.13051 0.08851 0.839664339 88.29912715 7166.58738 18.22977 FAM132A 4.67625423888147e-05 0.416873507225484 0.583079730232127 family with sequence similarity 132 member A FUNCTION: Insulin-sensitizing adipocyte-secreted protein (adipokine) that regulates glucose metabolism in liver and adipose tissue. Promotes glucose uptake in adipocytes and suppresses de novo glucose production in hepatocytes via the PI3K-Akt signaling pathway. Administration lead to reduction of blood glucose. Able to attenuate inflammation in fat tissue (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Predominantly expressed by adipose tissues. {ECO:0000269|PubMed:22275362}.; adrenal gland;colon;kidney;brain; . . . . . 2036.93326 8.31480 FAM132B . . . family with sequence similarity 132 member B FUNCTION: Iron-regulatory hormone that acts as an erythroid regulator after hemorrhage: produced by erythroblasts following blood loss and mediates suppression of hepcidin (HAMP) expression in the liver, thereby promoting increased iron absorption and mobilization from stores. Promotes lipid uptake into adipocytes and hepatocytes via transcriptional up-regulation of genes involved in fatty acid uptake (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;colon;blood;skin;uterus;pancreas;prostate;lung;frontal lobe;endometrium;iris;testis;spleen;brain;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . . . 334.56431 3.88615 FAM133A 0.659793341226144 0.316553832961199 0.0236528258126565 family with sequence similarity 133 member A . . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;testis;bladder;brain;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;breast;lung;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;stomach; globus pallidus;trigeminal ganglion;skeletal muscle; 0.29797 0.09259 0.545784012 81.11582921 121.96674 2.40481 FAM133B 0.000297398530792941 0.799631177745466 0.200071423723741 family with sequence similarity 133 member B . . . . . 0.10255 . 0.057118534 57.99716914 8.47334 0.31062 FAM133CP . . . family with sequence similarity 133 member C, pseudogene . . . . . 0.10255 . . . . . FAM133DP . . . family with sequence similarity 133 member D, pseudogene . . . . . . . . . . . FAM134A 0.758589563138407 0.24100250237059 0.000407934491003232 family with sequence similarity 134 member A . . . lymphoreticular;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; whole brain;amygdala;medulla oblongata;occipital lobe;testis - interstitial;superior cervical ganglion;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.37654 0.10022 0.50895761 80.20169851 2531.60479 9.38756 FAM134B 0.00565139603237414 0.971198145770552 0.0231504581970743 family with sequence similarity 134 member B FUNCTION: Endoplasmic reticulum-anchored autophagy receptor that mediates ER delivery into lysosomes through sequestration into autophagosomes (PubMed:26040720). Promotes membrane remodeling and ER scission via its membrane bending capacity and targets the fragments into autophagosomes via interaction with ATG8 family proteins (PubMed:26040720). Required for long-term survival of nociceptive and autonomic ganglion neurons (PubMed:19838196, PubMed:26040720). {ECO:0000269|PubMed:19838196, ECO:0000269|PubMed:26040720}.; DISEASE: Neuropathy, hereditary sensory and autonomic, 2B (HSAN2B) [MIM:613115]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by sensory and/or autonomic abnormalities. HSAN2B is an autosomal recessive disorder characterized by impairment of pain, temperature and touch sensation. Onset occurs in the first or second decade, with impaired nociception and progressive mutilating ulceration of the hands and feet with osteomyelitis and acroosteolysis. Amputations of the hands and feet are common. Autonomic dysfunction includes hyperhidrosis, urinary incontinence, and slow pupillary light response. {ECO:0000269|PubMed:19838196}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;testis;spinal ganglion;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;hippocampus;liver;kidney;mammary gland;stomach; subthalamic nucleus;prefrontal cortex;ciliary ganglion;parietal lobe;skeletal muscle; 0.67796 0.10874 0.395088462 76.15003539 212.64281 3.14699 FAM134C 0.145899133690528 0.853316826241047 0.000784040068425045 family with sequence similarity 134 member C FUNCTION: Mediates NRF1-enhanced neurite outgrowth. {ECO:0000269|PubMed:23939472}.; . . colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; 0.37734 . -0.800872469 12.33191791 110.46599 2.28780 FAM135A 0.787125610333894 0.212874385694955 3.971150164976e-09 family with sequence similarity 135 member A . . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16192744}.; myocardium;ovary;colon;parathyroid;uterus;prostate;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);tongue;islets of Langerhans;hypothalamus;adrenal cortex;skeletal muscle;lung;placenta;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; medulla oblongata;testis - interstitial;subthalamic nucleus;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skin; 0.23330 0.08995 -0.501537595 21.83887709 3830.0762 12.17973 FAM135B 0.999998682401374 1.31759862595743e-06 2.06204447169464e-16 family with sequence similarity 135 member B . . . unclassifiable (Anatomical System);lung;testis;brain; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08052 0.09691 -1.425829947 4.051663128 148.31692 2.65323 FAM136A 0.00147861672914258 0.438791519893955 0.559729863376903 family with sequence similarity 136 member A . . . smooth muscle;ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;brain;bladder;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;hypothalamus;adrenal cortex;pharynx;blood;breast;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;aorta;stomach; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.23468 0.10874 -0.007201372 53.19061099 1636.32361 7.47629 FAM136BP . . . family with sequence similarity 136 member B, pseudogene . . . . . . . . . . . FAM138A . . . family with sequence similarity 138 member A . . . . . . . . . . . FAM138B . . . family with sequence similarity 138 member B . . . . . . . . . . . FAM138C . . . family with sequence similarity 138 member C . . . unclassifiable (Anatomical System);cartilage;ovary;parathyroid;skeletal muscle;uterus;prostate;lung;cerebral cortex;larynx;bone;placenta;testis;head and neck;kidney;brain;aorta;stomach; . . . . . . . FAM138D . . . family with sequence similarity 138 member D . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);islets of Langerhans;urinary;lens;pancreas;placenta;macula lutea;hippocampus;liver;hypopharynx;spleen;head and neck;cervix;kidney; testis; . . . . . . FAM138E . . . family with sequence similarity 138 member E . . . . . . . . . . . FAM138F . . . family with sequence similarity 138 member F . . . . . . . . . . . FAM149A 0.00644452968141037 0.989495688589466 0.00405978172912347 family with sequence similarity 149 member A . . . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;blood;retina;uterus;prostate;lung;endometrium;placenta;kidney;spinal ganglion;brain;stomach; whole brain;amygdala;medulla oblongata;superior cervical ganglion;hypothalamus;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;liver;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion;parietal lobe; 0.09547 . 3.116543701 99.26869545 2340.94942 8.95998 FAM149B1 . . . family with sequence similarity 149 member B1 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;endometrium;bone;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;cerebellum; superior cervical ganglion;temporal lobe;globus pallidus;testis;ciliary ganglion;caudate nucleus;skeletal muscle; 0.67394 . 0.725794416 85.98136353 4384.17888 13.21443 FAM149B1P1 . . . family with sequence similarity 149 member B1 pseudogene 1 . . . . . . . . . . . FAM150A 0.00184552053934947 0.483207568596935 0.514946910863715 family with sequence similarity 150 member A . . . . . 0.21613 . . . 14.90183 0.53630 FAM150B 0.384937770733736 0.571344910380227 0.0437173188860366 family with sequence similarity 150 member B . . . unclassifiable (Anatomical System);prostate;lung;ovary;endometrium;islets of Langerhans;testis;kidney;brain;artery;aorta; . 0.00641 . . . 2.26875 0.07639 FAM151A 3.92272933199048e-13 0.0122164577155876 0.98778354228402 family with sequence similarity 151 member A . . . unclassifiable (Anatomical System);lymph node;ovary;colon;fovea centralis;choroid;lens;retina;prostate;optic nerve;placenta;thyroid;macula lutea;liver;pituitary gland;spleen;kidney;mammary gland;stomach; ciliary ganglion;kidney;trigeminal ganglion; 0.16157 . 1.627768939 96.05449398 2291.10675 8.86149 FAM151B 8.20978463368662e-07 0.165513363505595 0.834485815515942 family with sequence similarity 151 member B . . . unclassifiable (Anatomical System);lung;visual apparatus;testis;kidney;brain; . 0.09514 . 0.038710339 56.92380278 64.73791 1.65096 FAM153A 0.276667825081711 0.718309518717874 0.00502265620041544 family with sequence similarity 153 member A . . . unclassifiable (Anatomical System);islets of Langerhans;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;hippocampus;macula lutea;testis;spleen;kidney;brain; amygdala;superior cervical ganglion;testis - interstitial;occipital lobe;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.13798 . . . 1096.63323 6.33886 FAM153B 0.647490029033932 0.352248801830811 0.00026116913525621 family with sequence similarity 153 member B . . . unclassifiable (Anatomical System);testis;brain; . 0.13388 . . . 20.48848 0.69728 FAM153C 0.848853442214669 0.148538405670693 0.00260815211463825 family with sequence similarity 153 member C . . . . . 0.05044 . . . 2.12315 0.07052 FAM155A 0.80041532637658 0.199346780963829 0.000237892659591308 family with sequence similarity 155 member A . . . . . 0.22573 . -0.005381972 53.50908233 761.08845 5.47031 FAM155A-IT1 . . . FAM155A intronic transcript 1 . . . . . . . . . . . FAM155B 0.870611038142857 0.127650233383395 0.00173872847374764 family with sequence similarity 155 member B . . . unclassifiable (Anatomical System);prostate;lung;testis;kidney;brain; atrioventricular node;cerebellum; 0.25498 0.14169 0.461228372 78.46190139 123.56427 2.41990 FAM156A . . . family with sequence similarity 156 member A . . . smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus; . . 0.09673 . . . . FAM156B . . . family with sequence similarity 156 member B . . . . . . 0.09673 . . . . FAM157A . . . family with sequence similarity 157 member A . . . . . . . . . . . FAM157B . . . family with sequence similarity 157 member B . . . . . . . . . . . FAM157C . . . family with sequence similarity 157 member C . . . . . . . . . . . FAM159A 0.000284217822528371 0.341801977667195 0.657913804510276 family with sequence similarity 159 member A . . . . . . . -0.007201372 53.19061099 59.48074 1.56478 FAM159B 0.101184301652243 0.58432846341258 0.314487234935178 family with sequence similarity 159 member B . . . . . . . 0.501689326 79.7888653 1066.66795 6.26401 FAM160A1 . . . family with sequence similarity 160 member A1 . . . . . . . 1.976952171 97.61146497 326.38989 3.84128 FAM160A2 0.999881559428366 0.000118440559796041 1.18383759412736e-11 family with sequence similarity 160 member A2 FUNCTION: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). {ECO:0000269|PubMed:18799622}.; . . colon;fovea centralis;skin;bone marrow;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;blood;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;head and neck;kidney;stomach; . 0.53179 0.09753 -0.944313493 9.394904459 1681.56018 7.55651 FAM160B1 0.999984985147066 1.50148525519254e-05 3.82162476351732e-13 family with sequence similarity 160 member B1 . . . . . 0.15009 . -0.754958418 13.57631517 80.29201 1.89406 FAM160B2 2.05240114095338e-05 0.974736924017089 0.0252425519715014 family with sequence similarity 160 member B2 . . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;ciliary body;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;skeletal muscle; 0.14877 . -0.591542347 18.24722812 2808.87174 10.00178 FAM161A 3.02772896806868e-09 0.729236750813486 0.270763246158785 family with sequence similarity 161 member A FUNCTION: Involved in ciliogenesis. {ECO:0000269|PubMed:22940612}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 3 are widely expressed with highest levels in retina and testis, with isoform 1 being the most abundant in all tissues tested. {ECO:0000269|PubMed:20705278, ECO:0000269|PubMed:20705279}.; unclassifiable (Anatomical System);colon;skin;retina;uterus;whole body;lung;optic nerve;frontal lobe;endometrium;adrenal gland;trabecular meshwork;visual apparatus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;fetal brain;globus pallidus;testis;ciliary ganglion;trigeminal ganglion; . . 1.023320772 91.04741684 2162.95207 8.55480 FAM161B 9.86041048036769e-11 0.279055189560387 0.720944810341009 family with sequence similarity 161 member B . . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:22791751}.; unclassifiable (Anatomical System);colon;retina;uterus;pancreas;lung;liver;testis;cervix;kidney;brain;artery;mammary gland;aorta;stomach; ciliary ganglion;atrioventricular node; 0.09509 0.08229 0.536463361 81.06864827 3600.98595 11.61635 FAM162A 0.000629842253416895 0.72985638185107 0.269513775895513 family with sequence similarity 162 member A FUNCTION: Proposed to be involved in regulation of apoptosis; the exact mechanism may differ between cell types/tissues. May be involved in hypoxia-induced cell death of transformed cells implicating cytochrome C release and caspase activation (such as CASP9) and inducing mitochondrial permeability transition. May be involved in hypoxia-induced cell death of neuronal cells probably by promoting release of AIFM1 from mitochondria to cytoplasm and its translocation to the nucleus; however, the involvement of caspases has been reported conflictingly. {ECO:0000269|PubMed:15082785}.; . . unclassifiable (Anatomical System);cartilage;heart;bone;liver;testis;spleen; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.06311 0.06397 0.703746784 85.42108988 264.18948 3.48771 FAM162B 0.000825834892494331 0.782646415128411 0.216527749979095 family with sequence similarity 162 member B . . . . . . . . . 527.11681 4.68633 FAM163A 0.579850964182797 0.376663838574543 0.0434851972426603 family with sequence similarity 163 member A . . TISSUE SPECIFICITY: Highly expressed in neuroblastoma compared to other tissues, suggesting that it may be used as a marker for metastasis in bone marrow. {ECO:0000269|PubMed:17208556}.; placenta;brain; dorsal root ganglion;superior cervical ganglion;testis;atrioventricular node;skeletal muscle; 0.20314 0.10025 0.193034296 66.82000472 44.1542 1.26734 FAM163B 0.428150995206124 0.461566947770031 0.110282057023845 family with sequence similarity 163 member B . . . placenta;brain; . . . . . 19.90115 0.67751 FAM166A 1.69745841119407e-11 0.0157097961749787 0.984290203808047 family with sequence similarity 166 member A . . . ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;oesophagus;bone;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;urinary;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; . . . -0.328796968 30.86223166 323.4384 3.82036 FAM166B 3.8532046326348e-06 0.209037472400288 0.79095867439508 family with sequence similarity 166 member B . . . . . . . 0.395088462 76.15003539 1190.3356 6.54235 FAM167A 0.000192997889999534 0.281984251110813 0.717822750999187 family with sequence similarity 167 member A . . TISSUE SPECIFICITY: Expressed in skin, including primary keratinocytes, spleen, kidney, leukocytes, testis, lung, small intestine and prostate. {ECO:0000269|PubMed:11896452}.; unclassifiable (Anatomical System);amygdala;smooth muscle;cartilage;heart;islets of Langerhans;salivary gland;skin;prostate;pancreas;whole body;lung;larynx;bone;placenta;liver;testis;head and neck;spleen;kidney;germinal center;brain;aorta;stomach; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.11080 0.08153 0.575097644 82.1656051 148.33677 2.65364 FAM167A-AS1 . . . FAM167A antisense RNA 1 . . . . . 0.08683 . . . . . FAM167B 0.00269115267024858 0.562852585871348 0.434456261458403 family with sequence similarity 167 member B . . . . . 0.44729 . . . 63.4375 1.63087 FAM168A 0.951667905445732 0.0481894694439583 0.000142625110309883 family with sequence similarity 168 member A . . . unclassifiable (Anatomical System);lymphoreticular;lymph node;bone;colon;spleen;skeletal muscle; . 0.33523 0.11215 -0.295622497 32.61972163 13.90232 0.50451 FAM168B 0.0437714936797545 0.849524037702781 0.106704468617465 family with sequence similarity 168 member B FUNCTION: Modulates neuronal axonal outgrowth by acting as a negative regulator of CDC42 and STAT3 and a positive regulator of STMN2. Positive regulator of CDC27 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the brain, within neuronal axonal fibers and associated with myelin sheets (at protein level). Expression tends to be lower in the brain of Alzheimer disease patients compared to healthy individuals (at protein level). {ECO:0000269|PubMed:20716133}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;urinary;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;thymus; amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;cingulate cortex;parietal lobe;cerebellum; . . -0.185391282 39.67916962 20.93895 0.70903 FAM169A 0.998576224772368 0.0014237701617577 5.06587406763732e-09 family with sequence similarity 169 member A . . . . . . . -0.201976964 38.98325077 51.25227 1.41152 FAM169B 0.00135689866124102 0.656623917878415 0.342019183460344 family with sequence similarity 169 member B . . . . . . . 0.749657564 86.56522765 50.63929 1.40077 FAM170A . . . family with sequence similarity 170 member A FUNCTION: Acts as a nuclear transcription factor that positively regulates the expression of heat shock genes. Binds to heat shock promoter elements (HSE). {ECO:0000269|PubMed:20162441}.; . TISSUE SPECIFICITY: Expressed strongly in testis and brain and weakly in prostate, spleen, pancreas and uterus. {ECO:0000269|PubMed:20162441}.; medulla oblongata; . . 0.07670 0.350995466 74.37485256 1445.4921 7.09261 FAM170B . . . family with sequence similarity 170 member B FUNCTION: Plays a role in fertilization through the acrosome reaction. {ECO:0000250|UniProtKB:E9PXT9}.; . TISSUE SPECIFICITY: Exclusively expressed in adult testis. {ECO:0000269|PubMed:26179146}.; medulla oblongata;testis; . 0.14419 . 1.436808095 95.04600142 2513.30848 9.33771 FAM170B-AS1 . . . FAM170B antisense RNA 1 . . . . . . . . . . . FAM171A1 0.987016297989282 0.0129834748762515 2.27134466494003e-07 family with sequence similarity 171 member A1 . . . . . 0.47668 0.12496 -1.324592054 4.729889125 1348.47272 6.89264 FAM171A2 . . . family with sequence similarity 171 member A2 . . . unclassifiable (Anatomical System);heart;ovary;parathyroid;uterus;pancreas;lung;oesophagus;endometrium;placenta;duodenum;testis;spleen;brain; . . . . . 553.79869 4.78277 FAM171B 0.0574213565538764 0.941808995861223 0.000769647584901115 family with sequence similarity 171 member B . . . unclassifiable (Anatomical System);ovary;colon;parathyroid;retina;breast;lung;frontal lobe;cerebral cortex;placenta;hippocampus;pituitary gland;testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion; 0.22405 . -1.085675268 7.147912243 280.39489 3.58851 FAM172A 0.0182871087954041 0.977357868317006 0.00435502288758984 family with sequence similarity 172 member A . . . . . 0.37235 0.11009 -0.071520315 48.34866714 202.3911 3.06977 FAM172BP . . . family with sequence similarity 172 member B, pseudogene . . . . . . . . . . . FAM173A 0.00048241002631383 0.437611208315395 0.561906381658292 family with sequence similarity 173 member A . . . unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;colon;blood;lens;skin;lung;endometrium;placenta;bone;testis;kidney;brain;stomach; testis - interstitial;temporal lobe;testis; 0.14733 0.11217 . . 229.47969 3.27395 FAM173B 2.44499722250718e-07 0.282806723138108 0.71719303236217 family with sequence similarity 173 member B . . . ovary;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;skeletal muscle; . 0.10150 0.418953042 77.06416608 3547.74917 11.49248 FAM174A 0.000618293705839529 0.487516700315557 0.511865005978603 family with sequence similarity 174 member A . . . medulla oblongata;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cerebellum cortex;hypothalamus;urinary;lens;pancreas;lung;placenta;macula lutea;hippocampus;liver;kidney;stomach;thymus; whole brain; 0.10888 . 0.525552348 80.57914603 102.19661 2.18560 FAM174B 0.00994225008853275 0.602281740057338 0.387776009854129 family with sequence similarity 174 member B . . . ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;prostate;thyroid;fetal thyroid; . . . . 75.73807 1.82252 FAM175A 0.314878215342693 0.684371624492695 0.000750160164611791 family with sequence similarity 175 member A FUNCTION: Involved in DNA damage response and double-strand break (DSB) repair. Component of the BRCA1-A complex, acting as a central scaffold protein that assembles the various components of the complex and mediates the recruitment of BRCA1. The BRCA1-A complex specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at DSBs. This complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. {ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:17643122, ECO:0000269|PubMed:18077395, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:22357538}.; DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:22357538}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . . . 0.30324 . 0.949904335 90.00943619 1881.46106 7.97588 FAM175B 0.0868521973405688 0.911210347842391 0.00193745481704044 family with sequence similarity 175 member B FUNCTION: Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates (PubMed:19214193, PubMed:20032457, PubMed:20656690, PubMed:24075985). May act as a central scaffold protein that assembles the various components of the BRISC complex and retains them in the cytoplasm (PubMed:20656690). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys- 63'-linked ubiquitination of target proteins (By similarity). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1 (PubMed:26195665). Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activities by enhancing its stability and cell surface expression (PubMed:24075985, PubMed:26344097). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985). Required for normal induction of p53/TP53 in response to DNA damage (PubMed:25283148). Independent of the BRISC complex, promotes interaction between USP7 and p53/TP53, and thereby promotes deubiquitination of p53/TP53, preventing its degradation and resulting in increased p53/TP53-mediated transcription regulation and p53/TP53-dependent apoptosis in response to DNA damage (PubMed:25283148). {ECO:0000250|UniProtKB:Q3TCJ1, ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:20032457, ECO:0000269|PubMed:20656690, ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:25283148}.; . TISSUE SPECIFICITY: Detected in heart muscle (at protein level). Detected in heart and muscle, and at much lower levels in brain (PubMed:21195082). {ECO:0000269|PubMed:21195082}.; ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;adrenal cortex;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;occipital lobe;medulla oblongata;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.65527 0.10946 -0.670411825 15.61689078 45.54009 1.29657 FAM177A1 0.00206788278490877 0.744393884642755 0.253538232572337 family with sequence similarity 177 member A1 . . . smooth muscle;ovary;colon;substantia nigra;parathyroid;uterus;prostate;whole body;frontal lobe;endometrium;bone;testis;bladder;pineal gland;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;blood;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;liver;kidney;stomach;peripheral nerve; amygdala;whole brain;testis - interstitial;testis - seminiferous tubule;hypothalamus;prefrontal cortex;testis;cingulate cortex; 0.19726 0.09455 0.12689526 63.00424628 41.2709 1.20623 FAM177A1P1 . . . family with sequence similarity 177 member A1 pseudogene 1 . . . . . . . . . . . FAM177B 9.20960342032327e-06 0.326964178796982 0.673026611599597 family with sequence similarity 177 member B . . . . . . . 0.237127192 68.98443029 16.97077 0.59778 FAM178B 8.69889482161504e-05 0.330167527293484 0.6697454837583 family with sequence similarity 178 member B . . . breast;myocardium;ovary;placenta;liver;testis;parathyroid;spleen; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; . . 0.839664339 88.29912715 1005.80053 6.10536 FAM179A 2.53209738989517e-20 0.000500621121329605 0.99949937887867 family with sequence similarity 179 member A . . . . . . . 3.195707687 99.33356924 9668.4641 21.29956 FAM179B 2.88662498531604e-06 0.999996858009446 2.55365568224047e-07 family with sequence similarity 179 member B . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;cochlea;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;cerebellum; amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;prefrontal cortex;globus pallidus;atrioventricular node;caudate nucleus;cingulate cortex;parietal lobe; 0.41096 0.09610 -1.096852975 6.965086105 1813.22409 7.85225 FAM180A 0.337078259629403 0.602676808769463 0.0602449316011343 family with sequence similarity 180 member A . . . unclassifiable (Anatomical System);smooth muscle;lung;cartilage;bone;brain;skin; . . . -0.005381972 53.50908233 215.46862 3.16767 FAM180B 0.315838165150116 0.48833754069695 0.195824294152934 family with sequence similarity 180 member B . . . . . . . . . 37.53286 1.11773 FAM181A 0.0249838634471543 0.780708498461758 0.194307638091088 family with sequence similarity 181 member A . . . unclassifiable (Anatomical System);ovary;placenta;testis;parathyroid; superior cervical ganglion;testis;ciliary ganglion; 0.23785 . 0.286674996 71.49681529 88.77887 2.02126 FAM181A-AS1 . . . FAM181A antisense RNA 1 . . . . . . . . . . . FAM181B 0.216567007712648 0.647838862734545 0.135594129552808 family with sequence similarity 181 member B . . . . . . . . . 3754.95689 11.98955 FAM182A . . . family with sequence similarity 182 member A . . . unclassifiable (Anatomical System);uterus;lung;frontal lobe;heart;macula lutea;testis;blood;fovea centralis;brain;mammary gland;skin; dorsal root ganglion;superior cervical ganglion;fetal liver;atrioventricular node; 0.07076 . . . . . FAM182B . . . family with sequence similarity 182 member B . . . . . . . . . 26.25882 0.85119 FAM183A 0.0293267361122758 0.80456481637476 0.166108447512965 family with sequence similarity 183 member A . . . uterus;lung;ovary;heart;endometrium;placenta;pituitary gland;parathyroid;spleen;skin; . . . 0.25917371 70.05779665 34.56351 1.05527 FAM183BP . . . family with sequence similarity 183 member B, pseudogene . . . . . . . . . . . FAM183CP . . . family with sequence similarity 183 member C, pseudogene . . . . . . . . . . . FAM183DP . . . family with sequence similarity 183 member D, pseudogene . . . . . . . . . . . FAM183EP . . . family with sequence similarity 183 member E, pseudogene . . . . . . . . . . . FAM184A 2.04433944490058e-13 0.943252599844914 0.0567474001548819 family with sequence similarity 184 member A . . . unclassifiable (Anatomical System);heart;islets of Langerhans;sympathetic chain;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;lung;placenta;visual apparatus;liver;testis;spleen;germinal center;kidney;brain; subthalamic nucleus;testis - interstitial;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.39040 0.09585 -0.21856543 37.66218448 717.75614 5.32034 FAM184B . . . family with sequence similarity 184 member B . . . ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.09640 1.774838537 96.82118424 732.69323 5.37206 FAM185A . . . family with sequence similarity 185 member A . . . . . . . . . 1636.94804 7.48126 FAM185BP . . . family with sequence similarity 185 member B, pseudogene . . . . . . . . . . . FAM186A . . . family with sequence similarity 186 member A . . . unclassifiable (Anatomical System);lung;testis; . . . 4.334192819 99.73460722 3006.74044 10.40904 FAM186B 2.40022432048492e-12 0.125511798592957 0.874488201404642 family with sequence similarity 186 member B . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis;germinal center;brain; . 0.06391 . 1.409099734 94.8041991 990.62981 6.06748 FAM187A . . . family with sequence similarity 187 member A . . . unclassifiable (Anatomical System);ovary;cartilage;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;endometrium;placenta;bone;macula lutea;testis;brain; superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;skeletal muscle; . . . . 2840.61241 10.07571 FAM187B 3.6655613907075e-06 0.203552249337369 0.79644408510124 family with sequence similarity 187 member B . . . uterus;medulla oblongata;lung;testis; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.03863 . 1.464302001 95.23472517 4746.74444 13.93148 FAM187B2P . . . family with sequence similarity 187 member B2, pseudogene . . . . . . . . . . . FAM188A 0.629692867941796 0.37024503035369 6.21017045141612e-05 family with sequence similarity 188 member A FUNCTION: May have pro-apoptotic function. Overexpression significantly inhibits cell proliferation in several tumor cell lines.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, and kidney, with weak expression in liver and brain. {ECO:0000269|PubMed:12054670}.; myocardium;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;dura mater;germinal center;brain;pineal gland;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;mesenchyma;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;aorta;stomach; amygdala;subthalamic nucleus; 0.42945 0.11262 -0.912929826 9.902099552 78.0218 1.86325 FAM188B 2.24554390700363e-15 0.0296007633694396 0.970399236630558 family with sequence similarity 188 member B . . . unclassifiable (Anatomical System);medulla oblongata;heart;colon;fovea centralis;choroid;lens;retina;optic nerve;lung;endometrium;placenta;macula lutea;testis;kidney;brain;stomach; . 0.70453 . 2.252570408 98.20712432 896.11188 5.83414 FAM188B2 . . . family with sequence similarity 188 member B2 . . . . . . . . . 67.25444 1.69732 FAM189A1 . . . family with sequence similarity 189 member A1 . . . unclassifiable (Anatomical System);ovary;endometrium;placenta;visual apparatus;parathyroid;kidney;brain;cerebellum; amygdala;medulla oblongata;fetal brain;cerebellum peduncles;temporal lobe;prefrontal cortex;trigeminal ganglion;parietal lobe;cingulate cortex; . . 1.460671256 95.18164661 1223.91052 6.61202 FAM189A2 8.91881745197623e-06 0.926228217208679 0.0737628639738685 family with sequence similarity 189 member A2 . . TISSUE SPECIFICITY: Prominently expressed in muscle.; unclassifiable (Anatomical System);ovary;hypothalamus;colon;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;lung;endometrium;thyroid;macula lutea;testis;mammary gland;brain; dorsal root ganglion;superior cervical ganglion;thyroid;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09306 0.09084 -0.290161348 33.33923095 112.90062 2.31156 FAM189B 0.000482815313135408 0.992600532382348 0.00691665230451691 family with sequence similarity 189 member B . . TISSUE SPECIFICITY: Widely expressed.; lymphoreticular;myocardium;ovary;sympathetic chain;colon;parathyroid;vein;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;muscle;adrenal cortex;breast;pancreas;lung;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; whole brain;adipose tissue; 0.18306 0.11698 0.132352165 63.48785091 556.05948 4.79080 FAM192A 0.944099351189242 0.0558588176958419 4.18311149163811e-05 family with sequence similarity 192 member A . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; amygdala;whole brain;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;hypothalamus;spinal cord;pons;caudate nucleus;prefrontal cortex;cingulate cortex;cerebellum; . . 0.03689118 56.64071715 9.8191 0.36004 FAM192BP . . . family with sequence similarity 192 member B, pseudogene . . . . . . . . . . . FAM193A 0.997818289407157 0.00218171000561206 5.87230710924595e-10 family with sequence similarity 193 member A . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; testis - interstitial;testis - seminiferous tubule;testis; 0.11328 0.08772 0.191006924 66.32460486 709.33249 5.28946 FAM193B 0.923710453002021 0.0762708964073684 1.86505906103064e-05 family with sequence similarity 193 member B . . TISSUE SPECIFICITY: Isoform 1 is up-regulated in both embryonal rhabdomyosarcoma and alveolar rhabdomyosarcoma cell lines. {ECO:0000269|PubMed:21177767}.; colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;stomach;thymus; . . . 0.156217551 64.82071243 220.7484 3.21303 FAM195A 0.0533617873640192 0.699481802330695 0.247156410305286 family with sequence similarity 195 member A . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; liver;kidney; 0.12411 . . . 8.6531 0.31826 FAM195B 0.317596823645591 0.488234136426656 0.194169039927753 family with sequence similarity 195 member B FUNCTION: The phosphorylation status of FAM195B functions as a molecular switch to regulate epithelial-mesenchymal transition. Unphosphorylated FAM195B binds to and inhibits the transcriptional corepressor CTBP(s). When phosphorylated by MAPK/ERK, FAM195B releases CTBP(s) resulting in transcriptional silencing of the E- cadherin gene and induction of epithelial-mesenchymal transition (PubMed:25728771). {ECO:0000269|PubMed:25728771}.; . . . . . . 0.12325821 62.38499646 7.50567 0.27878 FAM195CP . . . family with sequence similarity 195 member C, pseudogene . . . . . . . . . . . FAM195DP . . . family with sequence similarity 195 member D, pseudogene . . . . . . . . . . . FAM196A 0.849026864550399 0.15042903803938 0.000544097410221464 family with sequence similarity 196 member A . . . . . 0.31865 . -0.220384297 37.6032083 562.55427 4.81294 FAM196B . . . family with sequence similarity 196 member B . . . . . . . 0.481458261 79.03986789 1014.26246 6.12988 FAM197Y1P . . . family with sequence similarity 197 Y-linked member 1, pseudogene . . . . . . . . . . . FAM197Y2P . . . family with sequence similarity 197 Y-linked member 2, pseudogene . . . . . . . . . . . FAM197Y3 . . . family with sequence similarity 197 Y-linked member 3 . . . . . . . . . . . FAM197Y4P . . . family with sequence similarity 197 Y-linked member 4, pseudogene . . . . . . . . . . . FAM197Y5P . . . family with sequence similarity 197 Y-linked member 5, pseudogene . . . . . . . . . . . FAM197Y6 . . . family with sequence similarity 197 Y-linked member 6 . . . . . . . . . . . FAM197Y7P . . . family with sequence similarity 197 Y-linked member 7, pseudogene . . . . . . . . . . . FAM197Y8 . . . family with sequence similarity 197 Y-linked member 8 . . . . . . . . . . . FAM197Y9 . . . family with sequence similarity 197 Y-linked member 9 . . . . . . . . . . . FAM197Y10 . . . family with sequence similarity 197 Y-linked member 10 . . . . . . . . . . . FAM198A . . . family with sequence similarity 198 member A . . . unclassifiable (Anatomical System);cartilage;blood;fovea centralis;choroid;lens;retina;bone marrow;breast;pancreas;prostate;optic nerve;lung;placenta;macula lutea;mammary gland;brain; superior cervical ganglion;trigeminal ganglion; 0.06236 . 1.638895725 96.11347016 2400.506 9.09668 FAM198B 2.49581508305481e-06 0.736909785222243 0.263087718962674 family with sequence similarity 198 member B . . . myocardium;medulla oblongata;ovary;colon;parathyroid;vein;skin;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;dura mater;brain;artery;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;lacrimal gland;tongue;hypothalamus;adrenal cortex;skeletal muscle;breast;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node; 0.15675 0.09902 -0.132199953 43.97853267 86.39529 1.98499 FAM199X 0.926151027548092 0.0734351788681815 0.000413793583726235 family with sequence similarity 199, X-linked . . . unclassifiable (Anatomical System);ovary;lacrimal gland;islets of Langerhans;hypothalamus;colon;parathyroid;skin;skeletal muscle;breast;uterus;pancreas;lung;nasopharynx;bone;thyroid;placenta;liver;cervix;germinal center;kidney;brain;mammary gland;stomach; . 0.26839 . 0.013025609 54.62962963 3.17863 0.11429 FAM199YP . . . family with sequence similarity 199, Y-linked, pseudogene . . . . . . . . . . . FAM200A 6.00941061236888e-05 0.274361971227141 0.725577934666736 family with sequence similarity 200 member A . . . . . . . 0.283038099 71.26680821 137.08423 2.54616 FAM200B . . . family with sequence similarity 200 member B . . . . . . . 0.701931997 85.34442085 2850.58717 10.09837 FAM201A . . . family with sequence similarity 201 member A . . . . . 0.16226 . . . . . FAM201B . . . family with sequence similarity 201 member B . . . . . . . . . . . FAM201CP . . . family with sequence similarity 201 member C, pseudogene . . . . . . . . . . . FAM204A 0.0507124221470989 0.927633393841517 0.0216541840113839 family with sequence similarity 204 member A . . . . . 0.11866 . -0.295622497 32.61972163 9.33319 0.34270 FAM204BP . . . family with sequence similarity 204 member B, pseudogene . . . . . . . . . . . FAM204CP . . . family with sequence similarity 204 member C, pseudogene . . . . . . . . . . . FAM204DP . . . family with sequence similarity 204 member D, pseudogene . . . . . . . . . . . FAM205A . . . family with sequence similarity 205 member A . . . . . . . 2.682783088 98.86765747 10907.68954 22.70135 FAM205BP . . . family with sequence similarity 205 member B, pseudogene . . . . . 0.16449 . . . . . FAM205C . . . family with sequence similarity 205 member C . . . . . . . . . . . FAM206A 0.00336234418280111 0.831465363313854 0.165172292503345 family with sequence similarity 206 member A . . . . . 0.06921 0.13187 0.349177632 74.18023119 82.24853 1.92508 FAM206BP . . . family with sequence similarity 206 member B, pseudogene . . . . . . . . . . . FAM207A 0.0395817647359521 0.840348217051301 0.120070018212747 family with sequence similarity 207 member A . . TISSUE SPECIFICITY: Not detected in any tested tissue.; unclassifiable (Anatomical System);lymphoreticular;lymph node;muscle;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;optic nerve;lung;larynx;macula lutea;testis;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13615 0.09244 0.128714042 63.19886766 1574.8486 7.34419 FAM207BP . . . family with sequence similarity 207 member B, pseudogene . . . . . . . . . . . FAM207CP . . . family with sequence similarity 207 member C, pseudogene . . . . . . . . . . . FAM208A 0.999672316077973 0.000327683916244721 5.78270738090263e-12 family with sequence similarity 208 member A FUNCTION: Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. {ECO:0000269|PubMed:26022416}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;lung;adrenal gland;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; superior cervical ganglion;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;atrioventricular node;cingulate cortex; 0.32261 0.08919 -0.235157409 36.32932295 2779.36721 9.95977 FAM208B 0.96506326510446 0.0349367348881919 7.34820575452733e-12 family with sequence similarity 208 member B . . . ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;thymus; superior cervical ganglion;testis - interstitial;testis;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.34489 0.07588 2.833872852 99.09176693 3636.96782 11.70093 FAM209A 0.0316770454966637 0.814916719605943 0.153406234897393 family with sequence similarity 209 member A . . . . . 0.00453 . 0.415317661 76.81056853 27.98372 0.89845 FAM209B 0.0297206395001582 0.806410632414151 0.163868728085691 family with sequence similarity 209 member B . . . . . 0.00817 . 0.903992902 89.39018636 1097.44289 6.34269 FAM210A 0.0151243026401628 0.877442545634647 0.10743315172519 family with sequence similarity 210 member A . . . unclassifiable (Anatomical System);heart;ovary;adrenal cortex;colon;parathyroid;fovea centralis;skin;retina;uterus;pancreas;adrenal gland;bone;thyroid;macula lutea;visual apparatus;liver;testis;spleen;germinal center;kidney;brain;pineal gland;stomach; superior cervical ganglion; 0.11096 0.10074 -0.227663163 37.11370606 12.23715 0.44334 FAM210B 0.0723304939713369 0.742797205119476 0.184872300909187 family with sequence similarity 210 member B . . . . . 0.22323 0.10255 . . 1868.32668 7.95503 FAM210CP . . . family with sequence similarity 210 member C, pseudogene . . . . . . . . . . . FAM212A 0.000589161385315042 0.477600689590392 0.521810149024293 family with sequence similarity 212 member A . . . unclassifiable (Anatomical System);heart;ovary;cartilage;urinary;parathyroid;skin;uterus;pancreas;whole body;lung;placenta;germinal center;brain; . 0.12379 . 0.128714042 63.19886766 30.64073 0.97449 FAM212B 0.00359051662635945 0.841596659753954 0.154812823619687 family with sequence similarity 212 member B . . . unclassifiable (Anatomical System);cartilage;muscle;colon;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;uterus;prostate;optic nerve;macula lutea;liver;cervix;brain; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.09827 . -0.60427181 17.74593064 22.74555 0.76057 FAM212B-AS1 . . . FAM212B antisense RNA 1 . . . . . . . . . . . FAM213A 0.000157315082288998 0.672458848895318 0.327383836022393 family with sequence similarity 213 member A FUNCTION: Involved in redox regulation of the cell. Acts as an antioxidant. Inhibits TNFSF11-induced NFKB1 and JUN activation and osteoclast differentiation. May affect bone resorption and help to maintain bone mass. {ECO:0000269|PubMed:19951071}.; . TISSUE SPECIFICITY: Expressed in CSF1 and TNFSF11-stimulated CD14(+) peripheral blood mononuclear cells (PBMCs). {ECO:0000269|PubMed:19951071}.; . . . 0.11003 -0.005381972 53.50908233 36.37219 1.08995 FAM213B 0.000166699570192146 0.447562930819138 0.55227036961067 family with sequence similarity 213 member B FUNCTION: Catalyzes the reduction of prostaglandin-ethanolamide H(2) (prostamide H(2)) to prostamide F(2alpha) with NADPH as proton donor. Also able to reduce prostaglandin H(2) to prostaglandin F(2alpha) (By similarity). {ECO:0000250}.; . . . . 0.12582 . -0.007201372 53.19061099 29.5158 0.94320 FAM214A 0.96699856876149 0.0330014274341551 3.80435518861838e-09 family with sequence similarity 214 member A . . . ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;lung;trabecular meshwork;placenta;visual apparatus;liver;hypopharynx;head and neck;kidney;aorta;cerebellum; dorsal root ganglion;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.37711 . 0.604424343 82.90280727 912.11977 5.87174 FAM214B 0.387716111489972 0.610204382539193 0.00207950597083559 family with sequence similarity 214 member B . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion;bone marrow; 0.64887 0.09296 -0.135838822 43.77211607 261.20024 3.46990 FAM215A . . . family with sequence similarity 215 member A (non-protein coding) . . . . . . . . . 13.12567 0.47741 FAM215B . . . family with sequence similarity 215 member B (non-protein coding) . . . . . . . . . . . FAM216A 0.0011162985137716 0.834605539227425 0.164278162258804 family with sequence similarity 216 member A . . . . . 0.04692 . 0.170987912 65.5579146 62.01365 1.60508 FAM216B 9.4200190421495e-05 0.343245325694347 0.656660474115232 family with sequence similarity 216 member B . . . . . 0.25651 . 0.103030231 61.2762444 48.70291 1.36110 FAM217A 1.67423776229135e-06 0.65270212062675 0.347296205135488 family with sequence similarity 217 member A . . . . . 0.07530 . 2.397825098 98.50790281 1907.6107 8.04186 FAM217AP1 . . . family with sequence similarity 217 member A pseudogene 1 . . . . . . . . . . . FAM217B 0.0010813237416719 0.829505952403819 0.169412723854509 family with sequence similarity 217 member B . . . . . 0.07776 . -0.580403979 18.58928993 30.6159 0.97338 FAM218A 0.00182632450339697 0.481065140965548 0.517108534531055 family with sequence similarity 218 member A . . . . . . . 0.547599505 81.2160887 569.96992 4.84263 FAM218BP . . . family with sequence similarity 218 member B, pseudogene . . . . . . . . . . . FAM219A 0.2726030357487 0.703311762034402 0.024085202216898 family with sequence similarity 219 member A . . . . . 0.38041 0.10115 -0.009020804 52.8544468 1.20345 0.03590 FAM219B 0.00122765065389532 0.634924531338269 0.363847818007836 family with sequence similarity 219 member B . . . . . 0.11960 . 0.148941568 64.31941496 34.12026 1.04594 FAM220A 1.23121895874442e-05 0.214533293691874 0.785454394118538 family with sequence similarity 220 member A FUNCTION: May negatively regulate STAT3. {ECO:0000250}.; . . . . . . 0.885576705 89.14248644 2000.02674 8.23864 FAM220BP . . . family with sequence similarity 220 member B, pseudogene . . . . . 0.07310 . . . . . FAM220CP . . . family with sequence similarity 220 member C, pseudogene . . . . . . . . . . . FAM221A 5.09767784280586e-09 0.0621389298223292 0.937861065079993 family with sequence similarity 221 member A . . . . . 0.42342 . 0.973768544 90.33970276 1011.39471 6.12351 FAM221B 4.05317460075816e-06 0.214728197143675 0.785267749681724 family with sequence similarity 221 member B . . . . . 0.00881 . 1.306318795 93.99622552 1696.25859 7.59335 FAM222A 0.400389071715135 0.560226567416437 0.0393843608684281 family with sequence similarity 222 member A . . . . . 0.15954 . . . 164.93994 2.80855 FAM222A-AS1 . . . FAM222A antisense RNA 1 . . . . . . . . . . . FAM222B 0.549446554284703 0.44762458192866 0.00292886378663681 family with sequence similarity 222 member B . . . . . 0.82131 . -0.534490515 20.70063694 96.48425 2.12179 FAM223A . . . family with sequence similarity 223 member A (non-protein coding) . . . . . 0.11883 . . . . . FAM223B . . . family with sequence similarity 223 member B (non-protein coding) . . . . . . . . . . . FAM224A . . . family with sequence similarity 224 member A (non-protein coding) . . . . . . . . . . . FAM224B . . . family with sequence similarity 224 member B (non-protein coding) . . . . . . . . . . . FAM225A . . . family with sequence similarity 225 member A (non-protein coding) . . . . . . . . . . . FAM225B . . . family with sequence similarity 225 member B (non-protein coding) . . . . . . . . . . . FAM226A . . . family with sequence similarity 226 member A (non-protein coding) . . . . . . . . . . . FAM226B . . . family with sequence similarity 226 member B (non-protein coding) . . . . . . . . . . . FAM227A . . . family with sequence similarity 227 member A . . . . . . . . . 358.7527 4.01183 FAM227B 2.74008557766254e-16 0.00864182084129015 0.99135817915871 family with sequence similarity 227 member B . . . . . 0.33011 . -0.334253673 30.70299599 66.26675 1.67669 FAM228A 0.000409739893538017 0.638638547428711 0.360951712677751 family with sequence similarity 228 member A . . . . . . . 0.193034296 66.82000472 . . FAM228B . . . family with sequence similarity 228 member B . . . . . . . . . 954.7073 5.98213 FAM229A . . . family with sequence similarity 229 member A . . . . . . . . . 364.6141 4.04157 FAM229B 0.549545407306745 0.397050439747001 0.0534041529462536 family with sequence similarity 229 member B . . . . . . . 0.768075923 86.8895966 216.45119 3.17919 FAM230A . . . family with sequence similarity 230 member A . . . . . . . . . 37410.40377 38.14203 FAM230B . . . family with sequence similarity 230 member B (non-protein coding) . . . . . . . . . . . FAM230C . . . family with sequence similarity 230 member C . . . . . . . . . . . FAM231A . . . family with sequence similarity 231 member A . . . . . . . . . . . FAM231B . . . family with sequence similarity 231 member B . . . . . . . . . 41.68314 1.21474 FAM231C . . . family with sequence similarity 231 member C . . . . . . . . . . . FAM231D . . . family with sequence similarity 231 member D . . . . . . . . . 41.92699 1.22120 FAM231EP . . . family with sequence similarity 231 member E, pseudogene . . . . . . . . . . . FAM234A . . . family with sequence similarity 234 member A . . . . . 0.13582 0.11265 -0.573127851 18.96083982 . . FAM234B . . . family with sequence similarity 234 member B . . . . . 0.16392 . -0.440847477 24.59896202 . . FAN1 1.46792582485245e-15 0.155699392946095 0.844300607053904 FANCD2/FANCI-associated nuclease 1 FUNCTION: Nuclease required for the repair of DNA interstrand cross-links (ICL) recruited at sites of DNA damage by monoubiquitinated FANCD2. Specifically involved in repair of ICL- induced DNA breaks by being required for efficient homologous recombination, probably in the resolution of homologous recombination intermediates (PubMed:20603015, PubMed:20603016, PubMed:20603073, PubMed:20671156, PubMed:24981866, PubMed:25430771). Not involved in DNA double-strand breaks resection (PubMed:20603015, PubMed:20603016). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions. Probably keeps excising with 3'-flap annealing until it reaches and unhooks the ICL (PubMed:25430771). Acts at sites that have a 5'-terminal phosphate anchor at a nick or a 1- or 2-nucleotide flap and is augmented by a 3' flap (PubMed:25430771). Also has endonuclease activity toward 5'-flaps (PubMed:20603015, PubMed:20603016, PubMed:24981866). {ECO:0000269|PubMed:20603015, ECO:0000269|PubMed:20603016, ECO:0000269|PubMed:20603073, ECO:0000269|PubMed:20671156, ECO:0000269|PubMed:24981866, ECO:0000269|PubMed:25135477, ECO:0000269|PubMed:25430771}.; DISEASE: Interstitial nephritis, karyomegalic (KMIN) [MIM:614817]: A rare kidney disease characterized by chronic tubulointerstitial nephritis associated with massively enlarged tubular epithelial cell nuclei. The clinical picture is associated with recurrent upper respiratory tract infections in addition to chronic kidney disease beginning in the third decade of life. {ECO:0000269|PubMed:22772369}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Schizophrenia and autism. Schizophrenia is a severe psychiatric disorder characterized by positive, negative, and cognitive symptoms, and it is associated with increased mortality and severely reduced fecundity. Autim is a complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation.Disease susceptibility may be associated with variations affecting the gene represented in this entry. {ECO:0000269|PubMed:24344280}.; . ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);heart;cerebellum cortex;islets of Langerhans;urinary;adrenal cortex;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;ciliary ganglion; 0.10351 0.08667 0.277371677 70.75961312 337.65639 3.90248 FANCA 2.08124711168363e-34 0.000122618656540907 0.999877381343459 Fanconi anemia complementation group A FUNCTION: DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be involved in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability.; DISEASE: Fanconi anemia, complementation group A (FANCA) [MIM:227650]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:10094191, ECO:0000269|PubMed:10210316, ECO:0000269|PubMed:10521298, ECO:0000269|PubMed:10807541, ECO:0000269|PubMed:11091222, ECO:0000269|PubMed:17924555, ECO:0000269|PubMed:9371798, ECO:0000269|PubMed:9399890, ECO:0000269|PubMed:9929978}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;urinary;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;temporal lobe;tumor;testis;trigeminal ganglion;parietal lobe; 0.23385 0.24341 -0.101294944 45.66525124 1788.01434 7.80511 FANCB 0.988393525012567 0.0116022653451297 4.20964230352489e-06 Fanconi anemia complementation group B FUNCTION: DNA repair protein required for FANCD2 ubiquitination. {ECO:0000269|PubMed:15502827}.; DISEASE: Fanconi anemia complementation group B (FANCB) [MIM:300514]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. Some severe FANCB cases manifest features of VACTERL syndrome with hydrocephalus. {ECO:0000269|PubMed:16679491}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);whole body;colon;germinal center; globus pallidus;ciliary ganglion;pons; 0.10977 0.31695 -0.400392389 26.85185185 279.99623 3.58445 FANCC 5.87975059285447e-10 0.61677378114316 0.383226218268865 Fanconi anemia complementation group C FUNCTION: DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. Upon IFNG induction, may facilitate STAT1 activation by recruiting STAT1 to IFNGR1. {ECO:0000269|PubMed:11520787}.; DISEASE: Fanconi anemia complementation group C (FANCC) [MIM:227645]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:11520787, ECO:0000269|PubMed:15299030, ECO:0000269|PubMed:1574115, ECO:0000269|PubMed:8128956, ECO:0000269|PubMed:8499901, ECO:0000269|PubMed:8844212, ECO:0000269|PubMed:9242535}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;frontal lobe;endometrium;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.07462 0.51811 0.354632714 74.58126917 244.22212 3.37227 FANCD2 2.47937339463725e-14 0.999907163284518 9.28367154577e-05 Fanconi anemia complementation group D2 FUNCTION: Required for maintenance of chromosomal stability. Promotes accurate and efficient pairing of homologs during meiosis. Involved in the repair of DNA double-strand breaks, both by homologous recombination and single-strand annealing. May participate in S phase and G2 phase checkpoint activation upon DNA damage. Plays a role in preventing breakage and loss of missegregating chromatin at the end of cell division, particularly after replication stress. Required for the targeting, or stabilization, of BLM to non-centromeric abnormal structures induced by replicative stress. Promotes BRCA2/FANCD1 loading onto damaged chromatin. May also be involved in B-cell immunoglobulin isotype switching. {ECO:0000269|PubMed:11239453, ECO:0000269|PubMed:11239454, ECO:0000269|PubMed:12086603, ECO:0000269|PubMed:12239151, ECO:0000269|PubMed:14517836, ECO:0000269|PubMed:15115758, ECO:0000269|PubMed:15314022, ECO:0000269|PubMed:15377654, ECO:0000269|PubMed:15454491, ECO:0000269|PubMed:15650050, ECO:0000269|PubMed:15661754, ECO:0000269|PubMed:15671039, ECO:0000269|PubMed:19465921}.; DISEASE: Fanconi anemia complementation group D2 (FANCD2) [MIM:227646]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:11239453}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in germinal center cells of the spleen, tonsil, and reactive lymph nodes, and in the proliferating basal layer of squamous epithelium of tonsil, esophagus, oropharynx, larynx and cervix. Expressed in cytotrophoblastic cells of the placenta and exocrine cells of the pancreas (at protein level). Highly expressed in testis, where expression is restricted to maturing spermatocytes. {ECO:0000269|PubMed:11239453, ECO:0000269|PubMed:14517836, ECO:0000269|PubMed:15454491}.; unclassifiable (Anatomical System);pancreas;lymph node;lung;ovary;bone;liver;testis;colon;spleen;blood;brain;stomach;bone marrow; dorsal root ganglion;atrioventricular node;trigeminal ganglion; 0.25008 . -0.920453886 9.790044822 710.41171 5.29622 FANCD2OS 0.0484543148164917 0.683351411456788 0.268194273726721 FANCD2 opposite strand . . . . . 0.36373 . 0.238945317 69.20853975 294.02338 3.66219 FANCD2P1 . . . Fanconi anemia complementation group D2 pseudogene 1 . . . . . . . . . . . FANCD2P2 . . . Fanconi anemia complementation group D2 pseudogene 2 . . . . . . . . . . . FANCE 0.00313889923167915 0.985566611642033 0.0112944891262883 Fanconi anemia complementation group E FUNCTION: As part of the Fanconi anemia (FA) complex functions in DNA cross-links repair. Required for the nuclear accumulation of FANCC and provides a critical bridge between the FA complex and FANCD2. {ECO:0000269|PubMed:12093742, ECO:0000269|PubMed:17296736}.; DISEASE: Fanconi anemia complementation group E (FANCE) [MIM:600901]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:11001585, ECO:0000269|PubMed:17924555}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);colon;fovea centralis;choroid;lens;retina;uterus;prostate;optic nerve;larynx;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;brain;stomach; subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.02889 0.47640 -0.312207497 32.05944798 1627.89945 7.46141 FANCF 0.00381453403362032 0.638390858946806 0.357794607019573 Fanconi anemia complementation group F FUNCTION: DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability (By similarity). {ECO:0000250}.; DISEASE: Fanconi anemia complementation group F (FANCF) [MIM:603467]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:10615118}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;intestine;colon;skin;prostate;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;visual apparatus;liver;spleen;cervix;kidney;stomach; trigeminal ganglion; 0.08224 0.29179 -0.023789244 52.09365416 112.88235 2.31118 FANCG 9.75294817310612e-09 0.740774929814062 0.259225060432989 Fanconi anemia complementation group G FUNCTION: DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. Candidate tumor suppressor gene.; . TISSUE SPECIFICITY: Highly expressed in testis and thymus. Found in lymphoblasts.; . . . 0.40608 0.775339069 87.13729653 737.81275 5.39122 FANCI 5.16501380164005e-19 0.679808795017253 0.320191204982747 Fanconi anemia complementation group I FUNCTION: Plays an essential role in the repair of DNA double- strand breaks by homologous recombination and in the repair of interstrand DNA cross-links (ICLs) by promoting FANCD2 monoubiquitination by FANCL and participating in recruitment to DNA repair sites. Required for maintenance of chromosomal stability. Specifically binds branched DNA: binds both single- stranded DNA (ssDNA) and double-stranded DNA (dsDNA). Participates in S phase and G2 phase checkpoint activation upon DNA damage. {ECO:0000269|PubMed:17412408, ECO:0000269|PubMed:17452773, ECO:0000269|PubMed:17460694, ECO:0000269|PubMed:19111657}.; DISEASE: Fanconi anemia complementation group I (FANCI) [MIM:609053]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:17452773}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;head and neck;kidney;mammary gland;stomach;thymus;peripheral nerve; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;tumor; 0.35148 0.20284 -0.117651763 44.54470394 6752.04504 17.44782 FANCL 2.09960326026736e-08 0.432455785172077 0.56754419383189 Fanconi anemia complementation group L FUNCTION: Ubiquitin ligase protein that mediates monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCI. May stimulate the ubiquitin release from UBE2W. May be required for proper primordial germ cell proliferation in the embryonic stage, whereas it is probably not needed for spermatogonial proliferation after birth. {ECO:0000269|PubMed:12973351, ECO:0000269|PubMed:16916645, ECO:0000269|PubMed:17938197, ECO:0000269|PubMed:19111657, ECO:0000269|PubMed:19589784}.; DISEASE: Fanconi anemia complementation group L (FANCL) [MIM:614083]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:12973351}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; amygdala;trigeminal ganglion; 0.32406 0.28376 -0.291981272 33.20358575 143.50228 2.61211 FANCM 6.24486171840289e-12 0.99998024181229 1.97581814647238e-05 Fanconi anemia complementation group M FUNCTION: ATPase required for FANCD2 ubiquitination, a key reaction in DNA repair. Binds to ssDNA but not to dsDNA. Recruited to forks stalled by DNA interstrand cross-links, and required for cellular resistance to such lesions. {ECO:0000269|PubMed:16116422, ECO:0000269|PubMed:16116434, ECO:0000269|Ref.8, ECO:0000269|Ref.9}.; . . unclassifiable (Anatomical System);heart;ovary;colon;skin;uterus;breast;prostate;lung;endometrium;testis;germinal center;kidney;brain; dorsal root ganglion;medulla oblongata;superior cervical ganglion;testis - interstitial;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.06764 0.16264 1.11512027 92.07949988 6367.90206 16.68075 FANK1 0.000115654248643306 0.951345270880267 0.0485390748710898 fibronectin type III and ankyrin repeat domains 1 . . TISSUE SPECIFICITY: Mostly restricted to testis. {ECO:0000269|PubMed:17604233}.; . . 0.24852 0.09413 1.642526957 96.14885586 280.30409 3.58800 FANK1-AS1 . . . FANK1 antisense RNA 1 . . . . . . . . . . . FAP 3.27312070401378e-11 0.974918303457656 0.0250816965096129 fibroblast activation protein alpha FUNCTION: Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2 (PubMed:14751930, PubMed:16223769, PubMed:16480718, PubMed:16410248, PubMed:17381073, PubMed:18095711, PubMed:21288888, PubMed:24371721). Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein (PubMed:9065413, PubMed:2172980, PubMed:7923219, PubMed:10347120, PubMed:10455171, PubMed:12376466, PubMed:16223769, PubMed:16651416, PubMed:18095711). Have also dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro (PubMed:10347120, PubMed:10593948, PubMed:16175601, PubMed:16223769, PubMed:16651416, PubMed:16410248, PubMed:17381073, PubMed:21314817, PubMed:24371721, PubMed:24717288). Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner. {ECO:0000250|UniProtKB:P97321, ECO:0000269|PubMed:10347120, ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:16223769, ECO:0000269|PubMed:16410248, ECO:0000269|PubMed:16480718, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17105646, ECO:0000269|PubMed:17381073, ECO:0000269|PubMed:18095711, ECO:0000269|PubMed:20707604, ECO:0000269|PubMed:21288888, ECO:0000269|PubMed:21314817, ECO:0000269|PubMed:2172980, ECO:0000269|PubMed:24371721, ECO:0000269|PubMed:24717288, ECO:0000269|PubMed:7923219, ECO:0000269|PubMed:9065413}.; . TISSUE SPECIFICITY: Expressed in adipose tissue. Expressed in the dermal fibroblasts in the fetal skin. Expressed in the granulation tissue of healing wounds and on reactive stromal fibroblast in epithelial cancers. Expressed in activated fibroblast-like synoviocytes from inflamed synovial tissues. Expressed in activated hepatic stellate cells (HSC) and myofibroblasts from cirrhotic liver, but not detected in normal liver. Expressed in glioma cells (at protein level). Expressed in glioblastomas and glioma cells. Isoform 1 and isoform 2 are expressed in melanoma, carcinoma and fibroblast cell lines. {ECO:0000269|PubMed:10347120, ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:10644713, ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:17105646, ECO:0000269|PubMed:20707604, ECO:0000269|PubMed:24371721, ECO:0000269|PubMed:7911242}.; unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;skin;skeletal muscle;uterus;pancreas;prostate;whole body;lung;cochlea;mesenchyma;bone;placenta;amnion;liver;testis;amniotic fluid;mammary gland;stomach; superior cervical ganglion;uterus corpus;smooth muscle;adipose tissue;appendix;atrioventricular node;trigeminal ganglion;skin; 0.37525 0.24378 -1.105907904 6.86482661 161.12606 2.77308 FAR1 0.87956746195825 0.120420222799763 1.23152419869164e-05 fatty acyl-CoA reductase 1 FUNCTION: Catalyzes the reduction of saturated fatty acyl-CoA with chain length C16 or C18 to fatty alcohols. {ECO:0000269|PubMed:15220348}.; DISEASE: Peroxisomal fatty acyl-CoA reductase 1 disorder (PFCRD) [MIM:616154]: An autosomal recessive metabolic disorder clinically characterized by severe intellectual disability, early-onset epilepsy, microcephaly, congenital cataracts, growth retardation, and spasticity. {ECO:0000269|PubMed:25439727}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;testis - interstitial;ciliary ganglion;atrioventricular node; 0.42982 0.10748 -0.205617011 38.57631517 20.01938 0.68322 FAR1-IT1 . . . FAR1 intronic transcript 1 . . . . . . . . . . . FAR1P1 . . . fatty acyl-CoA reductase 1 pseudogene 1 . . . . . . . . . . . FAR2 0.922173887824306 0.0778064868167035 1.96253589902748e-05 fatty acyl-CoA reductase 2 FUNCTION: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. The preferred substrates are C16, C18, C18:1 and C18:2 but low activity can be observed with C10-C14 substrates. {ECO:0000269|PubMed:15220348}.; . . unclassifiable (Anatomical System);heart;hypothalamus;colon;blood;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;optic nerve;lung;placenta;macula lutea;testis;bladder;brain; superior cervical ganglion;testis - interstitial;skeletal muscle;bone marrow; 0.11607 0.13485 -0.844966979 11.1759849 59.26666 1.56096 FAR2P1 . . . fatty acyl-CoA reductase 2 pseudogene 1 . . . . . . . . . . . FAR2P2 . . . fatty acyl-CoA reductase 2 pseudogene 2 . . . . . . . . . . . FAR2P3 . . . fatty acyl-CoA reductase 2 pseudogene 3 . . . . . . . . . . . FAR2P4 . . . fatty acyl-CoA reductase 2 pseudogene 4 . . . . . . . . . . . FARP1 0.0452630742628719 0.954736545955762 3.79781365538282e-07 FERM, ARH/RhoGEF and pleckstrin domain protein 1 FUNCTION: Functions as guanine nucleotide exchange factor for RAC1. May play a role in semaphorin signaling. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in cAMP-treated chondrocytes, but not in untreated chondrocytes. Detected in fetal brain, heart and spleen, and in adult testis, kidney and lung. {ECO:0000269|PubMed:9425278}.; smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;amniotic fluid;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;placenta;duodenum;amnion;head and neck;kidney;stomach; fetal brain;prefrontal cortex;kidney; 0.20246 0.11058 0.102819578 60.96956829 825.14469 5.63133 FARP1-AS1 . . . FARP1 antisense RNA 1 . . . . . . . . . . . FARP2 1.9753652138302e-20 0.0419303359786851 0.958069664021315 FERM, ARH/RhoGEF and pleckstrin domain protein 2 FUNCTION: Functions as guanine nucleotide exchange factor that activates RAC1. May have relatively low activity. Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton. Plays a role in TNFSF11-mediated osteoclast differentiation, especially in podosome rearrangement and reorganization of the actin cytoskeleton. Regulates the activation of ITGB3, integrin signaling and cell adhesion (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;skin;retina;uterus;prostate;endometrium;thyroid;iris;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;placenta;cervix;kidney;mammary gland;stomach; trigeminal ganglion;skeletal muscle; 0.07766 0.19172 0.374677996 75.3066761 2229.31594 8.70050 FARS2 4.54145794820807e-06 0.627649016891973 0.372346441650078 phenylalanyl-tRNA synthetase 2, mitochondrial FUNCTION: Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation. To a lesser extent, also catalyzes direct attachment of m-Tyr (an oxidized version of Phe) to tRNA(Phe), thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins. {ECO:0000269|PubMed:19549855, ECO:0000269|PubMed:22833457}.; DISEASE: Combined oxidative phosphorylation deficiency 14 (COXPD14) [MIM:614946]: A severe multisystemic autosomal recessive disorder characterized by neonatal onset of global developmental delay, refractory seizures, and lactic acidosis. Biochemical studies show deficiencies of multiple mitochondrial respiratory enzymes. {ECO:0000269|PubMed:22499341, ECO:0000269|PubMed:22833457}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;uterus;prostate;whole body;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;bile duct;breast;lung;nasopharynx;placenta;liver;cervix;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.08287 0.13859 -0.067881249 48.69072895 108.99828 2.26679 FARSA 0.00405072098603709 0.994330090082268 0.00161918893169473 phenylalanyl-tRNA synthetase alpha subunit . . . medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;hypothalamus;muscle;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;aorta; whole brain;occipital lobe;thalamus;subthalamic nucleus;hypothalamus;prefrontal cortex;liver;tumor;globus pallidus;parietal lobe;cerebellum; 0.30699 0.19969 0.066214104 58.95848077 151.78294 2.69474 FARSA-AS1 . . . FARSA antisense RNA 1 . . . . . . . . . . . FARSB 0.900979753771666 0.0990187515965624 1.49463177152284e-06 phenylalanyl-tRNA synthetase beta subunit . . . smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;germinal center;bladder;brain;gall bladder;amygdala;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;atrium;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; superior cervical ganglion; 0.65130 0.15254 -0.380166007 27.88393489 80.99373 1.90403 FARSBP1 . . . phenylalanyl-tRNA synthetase beta subunit pseudogene 1 . . . . . . . . . . . FAS 0.726173343974111 0.273236971861571 0.000589684164317641 Fas cell surface death receptor FUNCTION: Receptor for TNFSF6/FASLG. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death- inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS- mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both. The secreted isoforms 2 to 6 block apoptosis (in vitro). {ECO:0000269|PubMed:19118384, ECO:0000269|PubMed:7533181}.; DISEASE: Autoimmune lymphoproliferative syndrome 1A (ALPS1A) [MIM:601859]: A disorder of apoptosis that manifests in early childhood and results in the accumulation of autoreactive lymphocytes. It is characterized by non-malignant lymphadenopathy with hepatosplenomegaly, and autoimmune hemolytic anemia, thrombocytopenia and neutropenia. {ECO:0000269|PubMed:10090885, ECO:0000269|PubMed:10340403, ECO:0000269|PubMed:10515860, ECO:0000269|PubMed:11418480, ECO:0000269|PubMed:17336828, ECO:0000269|PubMed:7540117, ECO:0000269|PubMed:8929361, ECO:0000269|PubMed:9028321, ECO:0000269|PubMed:9028957, ECO:0000269|PubMed:9322534, ECO:0000269|PubMed:9821419, ECO:0000269|PubMed:9927496}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 and isoform 6 are expressed at equal levels in resting peripheral blood mononuclear cells. After activation there is an increase in isoform 1 and decrease in the levels of isoform 6. {ECO:0000269|PubMed:7575433}.; smooth muscle;ovary;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;blood;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.09094 0.87160 0.461228372 78.46190139 115.58745 2.33810 FAS-AS1 . . . FAS antisense RNA 1 . . . . . . . . . . . FASLG 0.611670213878948 0.380003372696377 0.00832641342467479 Fas ligand FUNCTION: Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells. May be involved in cytotoxic T-cell mediated apoptosis and in T-cell development. TNFRSF6/FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both. Binding to the decoy receptor TNFRSF6B/DcR3 modulates its effects. {ECO:0000269|PubMed:17557115}.; DISEASE: Autoimmune lymphoproliferative syndrome 1B (ALPS1B) [MIM:601859]: A disorder of apoptosis that manifests in early childhood and results in the accumulation of autoreactive lymphocytes. It is characterized by non-malignant lymphadenopathy with hepatosplenomegaly, and autoimmune hemolytic anemia, thrombocytopenia and neutropenia. {ECO:0000269|PubMed:8787672}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.69145 0.84779 -0.405853867 26.23260203 29.04738 0.92915 FASN 0.99999995015986 4.98401399489786e-08 5.86578165724555e-22 fatty acid synthase FUNCTION: Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.; . TISSUE SPECIFICITY: Ubiquitous. Prominent expression in brain, lung, and liver. {ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:7595075}.; lymphoreticular;medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;adipose tissue;liver;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.56688 0.17024 -3.393118793 0.377447511 929.78531 5.91487 FASTK 0.0305313518323476 0.96743359000434 0.0020350581633121 Fas activated serine/threonine kinase FUNCTION: Phosphorylates the splicing regulator TIA1, thereby promoting the inclusion of FAS exon 6, which leads to an mRNA encoding a pro-apoptotic form of the receptor. {ECO:0000269|PubMed:17135269, ECO:0000269|PubMed:7544399}.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; myocardium;medulla oblongata;ovary;salivary gland;colon;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; whole brain;superior cervical ganglion;heart;white blood cells;skeletal muscle; 0.12282 0.20838 -0.247889024 35.98726115 524.233 4.67068 FASTKD1 1.65436401216165e-12 0.334550118411732 0.665449881586613 FAST kinase domains 1 . . TISSUE SPECIFICITY: Expression detected in spleen, thymus, testis, ovary, colon, heart, smooth muscle, kidney, brain, lung, liver and white adipose tissue with highest expression in heart. {ECO:0000269|PubMed:20869947}.; . . 0.21212 . -0.12856188 44.04930408 452.27241 4.42397 FASTKD2 4.03134120797395e-06 0.950309504182795 0.0496864644759972 FAST kinase domains 2 FUNCTION: Plays an important role in assembly of the mitochondrial large ribosomal subunit (PubMed:25683715). {ECO:0000269|PubMed:25683715}.; . TISSUE SPECIFICITY: Expression detected in spleen, thymus, testis, ovary, colon, heart, smooth muscle, kidney, brain, lung, liver and white adipose tissue with highest expression in heart, smooth muscle and thyroid. {ECO:0000269|PubMed:20869947}.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;nasopharynx;placenta;hypopharynx;amnion;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04917 . 0.86534717 88.80042463 954.8755 5.98389 FASTKD3 2.49269112263401e-10 0.0746427739276539 0.925357225823077 FAST kinase domains 3 FUNCTION: Required for normal mitochondrial respiration. {ECO:0000269|PubMed:20869947}.; . TISSUE SPECIFICITY: Expression detected in spleen, thymus, testis, ovary, colon, heart, smooth muscle, kidney, brain, lung, liver and white adipose tissue with highest expression in liver and thyroid. {ECO:0000269|PubMed:20869947}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;parathyroid;skin;skeletal muscle;uterus;prostate;optic nerve;lung;larynx;bone;placenta;liver;testis;cervix;head and neck;germinal center;kidney;bladder;brain;stomach; superior cervical ganglion;parietal lobe;skeletal muscle; 0.03664 0.06179 0.290313621 71.56758669 465.44079 4.46909 FASTKD5 3.4250816581256e-06 0.797527432125259 0.202469142793083 FAST kinase domains 5 FUNCTION: Plays an important role in the processing of non- canonical mitochondrial mRNA precursors (PubMed:25683715). {ECO:0000269|PubMed:25683715}.; . TISSUE SPECIFICITY: Expression detected in spleen, thymus, testis, ovary, colon, heart, smooth muscle, kidney, brain, lung, liver and white adipose tissue with highest expression in heart, smooth muscle, liver and thyroid. {ECO:0000269|PubMed:20869947}.; . . 0.12051 0.08503 -0.727458245 14.19556499 581.4268 4.88688 FAT1 1.77905878379738e-10 0.999999999767447 5.46475717706945e-11 FAT atypical cadherin 1 FUNCTION: Plays an essential role for cellular polarization, directed cell migration and modulating cell-cell contact. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in many epithelial and some endothelial and smooth muscle cells.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;amniotic fluid;bladder;brain;heart;cartilage;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;amnion;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;kidney; 0.43649 0.17117 -0.392997457 27.05826846 12587.77428 24.10511 FAT1P1 . . . FAT atypical cadherin 1 pseudogene 1 . . . . . . . . . . . FAT2 7.35015824204342e-11 0.999999998965583 9.60915250083777e-10 FAT atypical cadherin 2 FUNCTION: Plays a role in the migration of epidermal cells. May modulate the extracellular space surronding parallel fibers of cerebellar during development (By similarity). {ECO:0000250, ECO:0000269|PubMed:18534823}.; . TISSUE SPECIFICITY: Expressed in epidermal keratinocytes, infant brain, cerebellum, and also in a variety of tumors, such as pancreatic cancer, diffuse type gastric cancer, ovarian cancer, esophageal cancer, skin squamous cell carcinoma, head and neck cancer. Not expressed in melanoma cell line A375 cells, normal epidermal melanocytes or normal dermal fibroblasts. Expressed in epidermal keratinocytes and squamous cell carcinoma (at protein level). {ECO:0000269|PubMed:16865240, ECO:0000269|PubMed:17900869}.; ovary;tongue;parathyroid;lens;skin;skeletal muscle;uterus;breast;lung;bone;thyroid;liver;pituitary gland;testis;head and neck;spleen;kidney;brain;stomach; cerebellum peduncles;cerebellum; 0.15430 0.09701 1.951664999 97.53479594 17917.39848 28.44166 FAT3 0.999999813687366 1.86312633536772e-07 4.93959948605759e-24 FAT atypical cadherin 3 FUNCTION: May play a role in the interactions between neurites derived from specific subsets of neurons during development. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in ES cells, primitive neuroectoderm, fetal brain, infant brain, adult neural tissues and prostate. {ECO:0000269|PubMed:16865240}.; unclassifiable (Anatomical System);prostate;whole body;frontal lobe;bone;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; . . . . 2077.88707 8.39691 FAT4 0.999999998364028 1.63597210043659e-09 5.83737259752425e-27 FAT atypical cadherin 4 FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. FAT4 plays a role in the maintenance of planar cell polarity as well as in inhibition of YAP1-mediated neuroprogenitor cell proliferation and differentiation (By similarity). {ECO:0000250}.; DISEASE: Van Maldergem syndrome 2 (VMLDS2) [MIM:615546]: An autosomal recessive disorder characterized by intellectual disability, typical craniofacial features, auditory malformations resulting in hearing loss, and skeletal and limb malformations. Some patients have renal hypoplasia. Brain MRI typically shows periventricular nodular heterotopia. {ECO:0000269|PubMed:24056717}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hennekam lymphangiectasia-lymphedema syndrome 2 (HKLLS2) [MIM:616006]: A form of Hennekam lymphangiectasia-lymphedema syndrome, a generalized lymph-vessels dysplasia characterized by intestinal lymphangiectasia with severe lymphedema of the limbs, genitalia and face. In addition, affected individuals have unusual facies and severe mental retardation. HKLLS2 individuals have lymphangiectasia variably affecting the gut, pericardium, lungs, kidneys, and genitalia. Other features include camptodactyly and rare syndactyly. {ECO:0000269|PubMed:24913602}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Expressed in fetal brain, infant brain, brain tumor and colorectal cancer. {ECO:0000269|PubMed:15003449, ECO:0000269|PubMed:16865240}.; unclassifiable (Anatomical System);choroid;fovea centralis;lens;skeletal muscle;retina;bile duct;whole body;optic nerve;visual apparatus;macula lutea;brain;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;fetal brain;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.20940 0.10056 -0.502828893 21.81528662 13346.97344 24.85144 FATE1 0.0344637295961143 0.825345732292395 0.140190538111491 fetal and adult testis expressed 1 . . TISSUE SPECIFICITY: Testis-specific in fetus (aged from 6 to 11 weeks). In adult, expressed predominantly in testis, with some expression in lung, heart, kidney, adrenal gland and whole brain.; . . 0.08440 0.10370 -0.161524709 41.6430762 578.71272 4.87390 FAU 0.768145175266772 0.223693534937075 0.00816128979615259 Finkel-Biskis-Reilly murine sarcoma virus (FBR-MuSV) ubiquitously expressed . . . myocardium;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;epidermis;islets of Langerhans;muscle;pancreas;lung;pia mater;cornea;placenta;head and neck;kidney;stomach;aorta; . 0.79372 0.14919 0.235309407 68.71903751 15.91712 0.56453 FAUP1 . . . FBR-MuSV-associated ubiquitously expressed (fox derived) pseudogene 1 . . . . . . . . . . . FAUP2 . . . FBR-MuSV-associated ubiquitously expressed (fox derived) pseudogene 2 . . . . . . . . . . . FAUP3 . . . FBR-MuSV-associated ubiquitously expressed (fox derived) pseudogene 3 . . . . . . . . . . . FAXC 0.872413322160328 0.127238647493218 0.000348030346453539 failed axon connections homolog FUNCTION: May play a role in axonal development. {ECO:0000250}.; . . . . 0.16364 . -0.071520315 48.34866714 34.389 1.05131 FAXDC2 1.47672397769909e-06 0.395048675788001 0.604949847488021 fatty acid hydroxylase domain containing 2 . . . . . 0.12780 0.09555 0.639420866 83.8995046 374.34014 4.08004 FBF1 1.13971483330464e-19 0.00866520942456154 0.991334790575438 Fas (TNFRSF6) binding factor 1 FUNCTION: Keratin-binding protein required for epithelial cell polarization. Involved in apical junction complex (AJC) assembly via its interaction with PARD3. Required for ciliogenesis. {ECO:0000269|PubMed:18838552, ECO:0000269|PubMed:23348840}.; . TISSUE SPECIFICITY: Present in various epithelial cells (at protein level).; ovary;salivary gland;intestine;colon;skin;uterus;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;urinary;muscle;pharynx;blood;skeletal muscle;lung;cornea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;ciliary ganglion; 0.10085 0.10300 -0.694532205 14.83840528 . . FBL 0.984496356217353 0.0155019086584158 1.73512423101811e-06 fibrillarin FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ104me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (PubMed:24352239). {ECO:0000269|PubMed:24352239}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;iris;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;adrenal gland;epididymis;nasopharynx;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;tumor;testis;white blood cells; 0.95160 . -0.0274281 51.65723048 20.52599 0.69806 FBLIM1 0.000789060297699282 0.928321056546903 0.0708898831553974 filamin binding LIM protein 1 FUNCTION: Serves as an anchoring site for cell-ECM adhesion proteins and filamin-containing actin filaments. Is implicated in cell shape modulation (spreading) and motility. May participate in the regulation of filamin-mediated cross-linking and stabilization of actin filaments. May also regulate the assembly of filamin- containing signaling complexes that control actin assembly. Promotes dissociation of FLNA from ITGB3 and ITGB7. Promotes activation of integrins and regulates integrin-mediated cell-cell adhesion. {ECO:0000269|PubMed:12496242, ECO:0000269|PubMed:12679033, ECO:0000269|PubMed:18829455, ECO:0000269|PubMed:19074766}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 3 are expressed in heart, kidney, lung, pancreas, placenta and platelets. Isoform 2 is expressed in brain, heart, kidney, lung, pancreas, placenta, skeletal muscle and platelets. {ECO:0000269|PubMed:12496242}.; . . 0.30445 0.10649 0.510776592 80.23708422 197.45136 3.03792 FBLL1 . . . fibrillarin-like 1 FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Also acts as a protein methyltransferase by mediating methylation of glutamine residues (By similarity). {ECO:0000250}.; . . islets of Langerhans;testis;brain; amygdala;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; . . . . 2877.45353 10.15553 FBLN1 0.852457932605284 0.147541202384306 8.65010410414805e-07 fibulin 1 FUNCTION: Incorporated into fibronectin-containing matrix fibers. May play a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Could be important for certain developmental processes and contribute to the supramolecular organization of ECM architecture, in particular to those of basement membranes. Has been implicated in a role in cellular transformation and tumor invasion, it appears to be a tumor suppressor. May play a role in haemostasis and thrombosis owing to its ability to bind fibrinogen and incorporate into clots. Could play a significant role in modulating the neurotrophic activities of APP, particularly soluble APP. {ECO:0000269|PubMed:11792823, ECO:0000269|PubMed:9393974, ECO:0000269|PubMed:9466671}.; DISEASE: Note=A chromosomal aberration involving FBLN1 is found in a complex type of synpolydactyly referred to as 3/3-prime/4 synpolydactyly associated with metacarpal and metatarsal synostoses. Reciprocal translocation t(12;22)(p11.2;q13.3) with RASSF8. Fibroblasts derived from a patient with synpolydactyly displayed alterations in the level of isoform D splice variant incorporated into the ECM and secreted into the conditioned culture medium. By contrast, the expression of isoform C was not perturbed in the patients fibroblasts. Furthermore, no aberrant polypeptides were detected in extracts of cultured patients fibroblasts. The translocation t(12;22) may result in haploinsufficiency of the isoform D splice variant, which could lead to the observed limb malformation. {ECO:0000269|PubMed:11836357}.; DISEASE: Note=Elevated expression and altered processing of FBLN1 protein is associated with human breast cancer. {ECO:0000269|PubMed:12644824}.; TISSUE SPECIFICITY: Isoform A and isoform B are only expressed in placenta. Isoform C and isoform D are expressed in a variety of tissues and cultured cells. {ECO:0000269|PubMed:9106159}.; ovary;salivary gland;colon;choroid;skin;retina;uterus;prostate;frontal lobe;endometrium;larynx;synovium;bone;iris;pituitary gland;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);heart;muscle;urinary;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;thalamus;adipose tissue;atrioventricular node;pons;uterus;prostate;uterus corpus;trachea;placenta;appendix;globus pallidus;ciliary ganglion;fetal lung;trigeminal ganglion; 0.67327 0.23543 -0.345391639 29.61193678 160.09965 2.76174 FBLN2 0.62982515300036 0.370172306334954 2.54066468637704e-06 fibulin 2 FUNCTION: Its binding to fibronectin and some other ligands is calcium dependent.; . TISSUE SPECIFICITY: Component of both basement membranes and other connective tissues. Expressed in heart, placenta and ovary.; myocardium;ovary;colon;parathyroid;choroid;skin;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;cerebral cortex;synovium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;skeletal muscle;breast;lung;placenta;visual apparatus;hippocampus;cervix;kidney;stomach;peripheral nerve; testis - interstitial;olfactory bulb;adipose tissue;heart;fetal thyroid;skin;skeletal muscle;testis - seminiferous tubule;placenta;thyroid;appendix;testis;trigeminal ganglion; 0.76637 0.22472 -1.091439713 6.988676575 754.76604 5.44846 FBLN5 0.995790692927138 0.00420923577191787 7.13009436667891e-08 fibulin 5 FUNCTION: Essential for elastic fiber formation, is involved in the assembly of continuous elastin (ELN) polymer and promotes the interaction of microfibrils and ELN (PubMed:18185537). Stabilizes and organizes elastic fibers in the skin, lung and vasculature (By similarity). Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Vascular ligand for integrin receptors which may play a role in vascular development and remodeling (PubMed:10428823). {ECO:0000250|UniProtKB:Q9WVH9, ECO:0000269|PubMed:10428823, ECO:0000269|PubMed:18185537}.; DISEASE: Cutis laxa, autosomal dominant, 2 (ADCL2) [MIM:614434]: A connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. Additional variable clinical features are gastrointestinal diverticula, hernia, and genital prolapse. Rare manifestations are pulmonary artery stenosis, aortic aneurysm, bronchiectasis, and emphysema. {ECO:0000269|PubMed:12618961}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cutis laxa, autosomal recessive, 1A (ARCL1A) [MIM:219100]: A connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. The clinical spectrum of autosomal recessive cutis laxa is highly heterogeneous with respect to organ involvement and severity. Type I autosomal recessive cutis laxa is a specific, life-threatening disorder with organ involvement, lung atelectasis and emphysema, diverticula of the gastrointestinal and genitourinary systems, and vascular anomalies. Associated cranial anomalies, late closure of the fontanel, joint laxity, hip dislocation, and inguinal hernia have been observed but are uncommon. {ECO:0000269|PubMed:12189163, ECO:0000269|PubMed:16652333, ECO:0000269|PubMed:16691202, ECO:0000269|PubMed:17035250, ECO:0000269|PubMed:18185537}. Note=The disease is caused by mutations affecting the gene represented in this entry. Mutations affecting this gene can modify the phenotype of diseases caused by ELN mutations. {ECO:0000269|PubMed:19194475}.; DISEASE: Macular degeneration, age-related, 3 (ARMD3) [MIM:608895]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. {ECO:0000269|PubMed:15269314, ECO:0000269|PubMed:16652333}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in skin fibroblasts (at protein level)(PubMed:17035250). Expressed predominantly in heart, ovary, and colon but also in kidney, pancreas, testis, lung and placenta. Not detectable in brain, liver, thymus, prostate, or peripheral blood leukocytes (PubMed:10428823). {ECO:0000269|PubMed:10428823, ECO:0000269|PubMed:17035250}.; smooth muscle;ovary;sympathetic chain;colon;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;bone;thyroid;testis;spinal ganglion;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach;aorta; adipose tissue; 0.33795 0.17455 -0.580403979 18.58928993 28.43292 0.91103 FBLN7 1.57848110307796e-05 0.656623583995634 0.343360631193335 fibulin 7 FUNCTION: An adhesion molecule that interacts with extracellular matrix molecules in developing teeth and may play important roles in differentiation and maintenance of odontoblasts as well as in dentin formation. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;parathyroid;choroid;fovea centralis;lens;retina;prostate;optic nerve;lung;placenta;visual apparatus;macula lutea;kidney; globus pallidus;ciliary ganglion;atrioventricular node; 0.26972 0.10055 -0.642904474 16.62538335 403.7545 4.21506 FBN1 1 1.04665187289805e-17 7.74151344572488e-45 fibrillin 1 FUNCTION: Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-1- containing microfibrils provide long-term force bearing structural support. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively. {ECO:0000269|PubMed:15062093}.; DISEASE: Marfan syndrome (MFS) [MIM:154700]: A hereditary disorder of connective tissue that affects the skeletal, ocular, and cardiovascular systems. A wide variety of skeletal abnormalities occurs with Marfan syndrome, including scoliosis, chest wall deformity, tall stature, abnormal joint mobility. Ectopia lentis occurs in most of the patients and is almost always bilateral. The leading cause of premature death is progressive dilation of the aortic root and ascending aorta, causing aortic incompetence and dissection. Neonatal Marfan syndrome is the most severe form resulting in death from cardiorespiratory failure in the first few years of life. {ECO:0000269|PubMed:10425041, ECO:0000269|PubMed:10441597, ECO:0000269|PubMed:10694921, ECO:0000269|PubMed:11700157, ECO:0000269|PubMed:11826022, ECO:0000269|PubMed:12203992, ECO:0000269|PubMed:1301946, ECO:0000269|PubMed:14695540, ECO:0000269|PubMed:15221638, ECO:0000269|PubMed:1569206, ECO:0000269|PubMed:16220557, ECO:0000269|PubMed:16222657, ECO:0000269|PubMed:1852208, ECO:0000269|PubMed:20803651, ECO:0000269|PubMed:21542060, ECO:0000269|PubMed:7611299, ECO:0000269|PubMed:7738200, ECO:0000269|PubMed:7870075, ECO:0000269|PubMed:7977366, ECO:0000269|PubMed:8004112, ECO:0000269|PubMed:8040326, ECO:0000269|PubMed:8071963, ECO:0000269|PubMed:8136837, ECO:0000269|PubMed:8281141, ECO:0000269|PubMed:8406497, ECO:0000269|PubMed:8504310, ECO:0000269|PubMed:8863159, ECO:0000269|PubMed:8882780, ECO:0000269|PubMed:9254848, ECO:0000269|PubMed:9338581, ECO:0000269|PubMed:9452085, ECO:0000269|PubMed:9837823, ECO:0000269|Ref.43}. Note=The disease is caused by mutations affecting the gene represented in this entry. The majority of the more than 600 mutations in FBN1 currently known are point mutations, the rest are frameshifts and splice site mutations. Marfan syndrome has been suggested in at least 2 historical figures, Abraham Lincoln and Paganini.; DISEASE: Ectopia lentis 1, isolated, autosomal dominant (ECTOL1) [MIM:129600]: An ocular abnormality characterized by partial or complete displacement of the lens from its space resulting from defective zonule formation. {ECO:0000269|PubMed:11700157, ECO:0000269|PubMed:11826022, ECO:0000269|PubMed:12203992, ECO:0000269|PubMed:8188302}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Weill-Marchesani syndrome 2 (WMS2) [MIM:608328]: A rare connective tissue disorder characterized by short stature, brachydactyly, joint stiffness, and eye abnormalities including microspherophakia, ectopia lentis, severe myopia and glaucoma. {ECO:0000269|PubMed:12525539}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Overlap connective tissue disease (OCTD) [MIM:604308]: Heritable disorder of connective tissue characterized by involvement of the mitral valve, aorta, skeleton, and skin. MASS syndrome is closely resembling both the Marfan syndrome and the Barlow syndrome. However, no dislocation of the lenses or aneurysmal changes occur in the aorta, and the mitral valve prolapse is by no means invariable. {ECO:0000269|PubMed:2739055}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Stiff skin syndrome (SSKS) [MIM:184900]: A syndrome characterized by hard, thick skin, usually over the entire body, which limits joint mobility and causes flexion contractures. Other occasional findings include lipodystrophy and muscle weakness. {ECO:0000269|PubMed:20375004}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Geleophysic dysplasia 2 (GPHYSD2) [MIM:614185]: An autosomal dominant disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening. Radiologic features include delayed bone age, cone-shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies. Affected individuals have characteristic facial features including a 'happy' face with full cheeks, shortened nose, hypertelorism, long and flat philtrum, and thin upper lip. Other distinctive features include progressive cardiac valvular thickening often leading to an early death, toe walking, tracheal stenosis, respiratory insufficiency, and lysosomal-like storage vacuoles in various tissues. {ECO:0000269|PubMed:21683322}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Acromicric dysplasia (ACMICD) [MIM:102370]: An autosomal dominant disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening. Radiologic features include delayed bone age, cone-shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies. Affected individuals have distinct facial features, including round face, well-defined eyebrows, long eyelashes, bulbous nose with anteverted nostrils, long and prominent philtrum, and thick lips with a small mouth. Other characteristic features include hoarse voice and pseudomuscular build, and there are distinct skeletal features as well, including an internal notch of the femoral head, internal notch of the second metacarpal, and external notch of the fifth metacarpal. {ECO:0000269|PubMed:21683322}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;bone;thyroid;iris;testis;amniotic fluid;spinal ganglion;brain;pineal gland;artery;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;mesenchyma;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;smooth muscle;adipose tissue;heart;placenta;testis;ciliary ganglion;trigeminal ganglion; 0.83380 0.11376 -2.813971075 0.642840293 915.46367 5.88549 FBN2 0.999999991794472 8.20552780336503e-09 4.11852941699783e-30 fibrillin 2 FUNCTION: Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-2- containing microfibrils regulate the early process of elastic fiber assembly. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (By similarity). {ECO:0000250|UniProtKB:Q61555}.; DISEASE: Macular degeneration, early-onset (EOMD) [MIM:616118]: An ocular disorder characterized by macular changes resulting in progressive loss of visual acuity. {ECO:0000269|PubMed:24899048}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in fetal eye (18 weeks)in the retinal pigment epithelium (RPE), the choroid, Bruch's membrane and in the sclera. Not expressed in the neural retina. {ECO:0000269|PubMed:24899048}.; smooth muscle;ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;stomach; superior cervical ganglion;adipose tissue;placenta;testis;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.65403 0.22936 -1.867776262 2.016985138 3419.53483 11.21650 FBN3 1.35475416104555e-27 0.999811748657587 0.000188251342413204 fibrillin 3 FUNCTION: Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin- containing microfibrils provide long-term force bearing structural support. {ECO:0000269|PubMed:14962672}.; . TISSUE SPECIFICITY: Predominantly expressed in connective tissues such as skeletal muscle, tendon, skin, perichondrium and periosteum. Highly expressed in fetal lung, brain, kidney. Expressed at low level in prostate, testis, mammary gland, uterus, ovary, placenta, bladder, adrenal gland, thyroid, fetal thymus, fetal liver, liver, fetal heart and heart. {ECO:0000269|PubMed:14962672}.; unclassifiable (Anatomical System);uterus;lung;whole body;adrenal medulla;brain;stomach; superior cervical ganglion;ciliary ganglion; 0.09923 0.13532 7.067302466 99.89384289 18901.16442 29.48902 FBP1 0.0985907926556028 0.866512033387524 0.0348971739568735 fructose-bisphosphatase 1 FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain. {ECO:0000269|PubMed:16497803, ECO:0000269|PubMed:18375435, ECO:0000269|PubMed:22517657}.; DISEASE: Fructose-1,6-bisphosphatase deficiency (FBP1D) [MIM:229700]: An autosomal recessive metabolic disorder characterized by impaired gluconeogenesis, and episodes of hypoglycemia and metabolic acidosis that can be lethal in newborn infants or young children. {ECO:0000269|PubMed:12126934, ECO:0000269|PubMed:9382095}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in pancreatic islets. {ECO:0000269|PubMed:18375435}.; . . 0.37365 0.50695 -0.005381972 53.50908233 143.00069 2.60725 FBP2 0.00139312366455047 0.867343828288974 0.131263048046475 fructose-bisphosphatase 2 FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations and probably participates in glycogen synthesis from carbohydrate precursors, such as lactate. {ECO:0000269|PubMed:17350621, ECO:0000269|PubMed:18214967}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level). {ECO:0000269|PubMed:12507293}.; . . 0.16578 0.23270 0.486911049 79.46449634 177.28797 2.89288 FBP2P1 . . . fructose-1,6-bisphosphatase 2 pseudogene 1 . . . . . . . . . . . FBRS 0.981524681800076 0.0184621357575703 1.3182442353781e-05 fibrosin . . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;thyroid;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; 0.32662 . . . 201.82278 3.06617 FBRSL1 . . . fibrosin like 1 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;subthalamic nucleus;globus pallidus;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; . . . . 1039.6602 6.19134 FBXL2 0.216479060538488 0.783506142191214 1.47972702978028e-05 F-box and leucine-rich repeat protein 2 FUNCTION: Calcium-activated substrate recognition component of the SCF (SKP1-cullin-F-box protein) E3 ubiquitin-protein ligase complex, SCF(FBXL2), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Unlike many F-box proteins, FBXL2 does not seem to target phosphodegron within its substrates but rather calmodulin-binding motifs and is thereby antagonized by calmodulin. This is the case for the cyclins CCND2 and CCND3 which polyubiquitination and subsequent degradation are inhibited by calmodulin. Through CCND2 and CCND3 degradation induces cell-cycle arrest in G(0) (PubMed:22020328, PubMed:22323446). SCF(FBXL2) also mediates PIK3R2 ubiquitination and proteasomal degradation thereby regulating phosphatidylinositol 3-kinase signaling and autophagy (PubMed:23604317). PCYT1A monoubiquitination by SCF(FBXL2) and subsequent degradation regulates synthesis of phosphatidylcholine, which is utilized for formation of membranes and of pulmonary surfactant (By similarity). {ECO:0000250|UniProtKB:Q8BH16, ECO:0000269|PubMed:22020328, ECO:0000269|PubMed:22323446, ECO:0000269|PubMed:23604317}.; . TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, pancreas and placenta. {ECO:0000269|PubMed:10531037}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;lens;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;head and neck;kidney;mammary gland;stomach;aorta; . 0.59915 . -0.205617011 38.57631517 30.86122 0.97810 FBXL3 0.251434579423949 0.742322965730349 0.00624245484570197 F-box and leucine-rich repeat protein 3 FUNCTION: Substrate-recognition component of the SCF(FBXL3) E3 ubiquitin ligase complex involved in circadian rhythm function. Plays a key role in the maintenance of both the speed and the robustness of the circadian clock oscillation. The SCF(FBXL3) complex mainly acts in the nucleus and mediates ubiquitination and subsequent degradation of CRY1 and CRY2. Activity of the SCF(FBXL3) complex is counteracted by the SCF(FBXL21) complex. {ECO:0000269|PubMed:17463251, ECO:0000269|PubMed:23452855}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10531035}.; lymphoreticular;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;larynx;bone;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;placenta;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;parietal lobe; 0.39724 0.11058 -0.317668748 31.45789101 3.93416 0.14587 FBXL4 0.0079087988593491 0.989068653586563 0.00302254755408758 F-box and leucine-rich repeat protein 4 . . TISSUE SPECIFICITY: Expressed in heart, kidney, liver, lung, pancreas, and placenta, but not in skeletal muscle. {ECO:0000269|PubMed:10531037}.; smooth muscle;ovary;parathyroid;skin;retina;bone marrow;uterus;prostate;thyroid;bone;germinal center;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;urinary;blood;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach; superior cervical ganglion; 0.42917 0.09922 -0.933156985 9.54824251 139.80195 2.57820 FBXL5 0.977580081625291 0.0224190471789746 8.71195734881384e-07 F-box and leucine-rich repeat protein 5 FUNCTION: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued. {ECO:0000269|PubMed:17532294, ECO:0000269|PubMed:19762596, ECO:0000269|PubMed:19762597}.; . . ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;bone;pituitary gland;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;kidney;stomach;aorta; amygdala;dorsal root ganglion;hypothalamus;thyroid;prefrontal cortex;testis;whole blood; 0.15411 0.10259 -0.957024976 9.088228356 161.83747 2.77939 FBXL6 3.69520806815842e-06 0.810919382971005 0.189076921820927 F-box and leucine-rich repeat protein 6 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;synovium;bone;pituitary gland;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;blood;lens;lung;placenta;macula lutea;alveolus;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.09239 0.10079 -0.442665927 24.53408823 363.5906 4.03651 FBXL7 0.200106851536876 0.789815928618607 0.0100772198445173 F-box and leucine-rich repeat protein 7 FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of AURKA during mitosis, causing mitotic arrest. {ECO:0000250}.; . . unclassifiable (Anatomical System);optic nerve;lung;macula lutea;fovea centralis;choroid;lens;retina; dorsal root ganglion;superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.54228 0.11262 -0.66859065 15.76433121 66.49829 1.67963 FBXL8 0.0144390750003526 0.680271738386945 0.305289186612702 F-box and leucine-rich repeat protein 8 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;endometrium;bone;placenta;hippocampus;kidney;brain; . 0.16708 0.10297 . . 229.24162 3.27301 FBXL12 0.0145183376555761 0.872963515009791 0.112518147334633 F-box and leucine-rich repeat protein 12 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. Mediates the polyubiquitination and proteasomal degradation of CAMK1 leading to disruption of cyclin D1/CDK4 complex assembly which results in G1 cell cycle arrest in lung epithelia. {ECO:0000269|PubMed:23707388}.; . . ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;uterus;prostate;endometrium;bone;iris;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.17931 0.11169 -0.179930907 40.35739561 175.94288 2.88597 FBXL13 1.66151922936947e-11 0.56695894865527 0.433041051328114 F-box and leucine-rich repeat protein 13 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . unclassifiable (Anatomical System);breast;lung;heart;bone;kidney;brain; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.10383 0.08853 0.492370491 79.60603916 1213.65219 6.59374 FBXL14 0.40527008579802 0.585991643495625 0.00873827070635501 F-box and leucine-rich repeat protein 14 FUNCTION: Substrate-recognition component of some SCF (SKP1-CUL1- F-box protein)-type E3 ubiquitin-protein ligase complexes. The SCF(FBXL14) complex acts by mediating ubiquitination and subsequent degradation of SNAI1. {ECO:0000269|PubMed:19955572}.; . . unclassifiable (Anatomical System);lung;ovary;islets of Langerhans;placenta;sympathetic chain;testis;spleen;blood;germinal center;lens;brain;bone marrow; amygdala;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;atrioventricular node;trigeminal ganglion; 0.12142 0.11262 -0.580403979 18.58928993 13.39968 0.48733 FBXL15 0.00210111721413477 0.510122269801997 0.487776612983868 F-box and leucine-rich repeat protein 15 FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SMURF1, thereby acting as a positive regulator of the BMP signaling pathway. Required for dorsal/ventral pattern formation and bone mass maintenance. Also mediates ubiquitination of SMURF2 and WWP2. {ECO:0000269|PubMed:21572392}.; . . ovary;sympathetic chain;colon;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;pituitary gland;testis;ciliary body;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;pineal body;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; whole brain;amygdala;thalamus;cerebellum peduncles;thyroid;temporal lobe;prefrontal cortex;caudate nucleus;cingulate cortex;parietal lobe;cerebellum; 0.20541 0.10468 . . 47.46542 1.33717 FBXL16 0.95155737500943 0.0482991837084133 0.000143441282157119 F-box and leucine-rich repeat protein 16 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;oesophagus;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;pineal body;lens;pancreas;lung;placenta;hippocampus;visual apparatus;macula lutea;kidney;stomach;cerebellum; whole brain;amygdala;superior cervical ganglion;medulla oblongata;temporal lobe;prefrontal cortex;globus pallidus;ciliary ganglion;pons;atrioventricular node;caudate nucleus; 0.51575 0.10838 -0.317668748 31.45789101 7.62155 0.28186 FBXL17 0.977900472361054 0.0220790366880718 2.04909508739532e-05 F-box and leucine-rich repeat protein 17 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;cartilage;islets of Langerhans;urinary;adrenal cortex;skin;skeletal muscle;uterus;prostate;cochlea;visual apparatus;liver;spleen;germinal center;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.62107 . . . 251.54404 3.41593 FBXL18 2.5658113917006e-07 0.161035519513549 0.838964223905312 F-box and leucine-rich repeat protein 18 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . lymphoreticular;unclassifiable (Anatomical System);pancreas;prostate;lung;liver;testis;spleen;head and neck;germinal center;stomach;skin; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;pons;parietal lobe;bone marrow; 0.20557 0.10131 -0.797234383 12.48525596 510.82237 4.62793 FBXL19 0.982522202972825 0.017477325447157 4.7158001784573e-07 F-box and leucine-rich repeat protein 19 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;islets of Langerhans;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;whole body;lung;adrenal gland;placenta;bone;macula lutea;visual apparatus;testis;spleen;brain;mammary gland;stomach;thymus; whole brain;superior cervical ganglion;medulla oblongata;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.37396 0.11262 -0.071520315 48.34866714 2594.94168 9.53466 FBXL19-AS1 . . . FBXL19 antisense RNA 1 (head to head) . . . . . . . . . . . FBXL20 0.998874815002399 0.00112518214339868 2.8542019794133e-09 F-box and leucine-rich repeat protein 20 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. Role in neural transmission (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;colon;blood;skin;bone marrow;uterus;lung;larynx;thyroid;placenta;visual apparatus;testis;head and neck;germinal center;kidney;brain;mammary gland;stomach; superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.85874 0.08027 -0.095386216 46.48502005 13.67512 0.49604 FBXL21 . . . F-box and leucine-rich repeat protein 21 (gene/pseudogene) FUNCTION: Substrate-recognition component of the SCF(FBXL21) E3 ubiquitin ligase complex involved in circadian rhythm function. Plays a key role in the maintenance of both the speed and the robustness of the circadian clock oscillation. The SCF(FBXL21) complex mainly acts in the cytosol and mediates ubiquitination of CRY proteins (CRY1 and CRY2), leading to CRY proteins stabilization. The SCF(FBXL21) complex counteracts the activity of the SCF(FBXL3) complex and protects CRY proteins from degradation. Involved in the hypothalamic suprachiasmatic nucleus (SCN) clock regulating temporal organization of the daily activities (By similarity). {ECO:0000250}.; . . liver;colon;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node; 0.05964 0.06344 . . . . FBXL22 0.000439659300268727 0.419701360367865 0.579858980331866 F-box and leucine-rich repeat protein 22 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. Promotes ubiquitination of sarcomeric proteins alpha-actinin-2 (ACTN2) and filamin-C (FLNC). {ECO:0000269|PubMed:22972877}.; . TISSUE SPECIFICITY: Enriched in cardiac muscle. {ECO:0000269|PubMed:22972877}.; unclassifiable (Anatomical System);uterus;prostate;heart;brain;skin; uterus;ciliary ganglion; 0.36227 0.08576 . . 450.94121 4.41230 FBXO2 0.273382985936642 0.702682642354057 0.0239343717093014 F-box protein 2 FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Involved in the endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranslocated into the cytosol and promoting their ubiquitination and subsequent degradation. Prevents formation of cytosolic aggregates of unfolded glycoproteins that have been retrotranslocated into the cytosol. Able to recognize and bind denatured glycoproteins, preferentially those of the high-mannose type (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;choroid;skin;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;hypothalamus;blood;lens;pancreas;lung;epididymis;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach; amygdala;whole brain;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;cingulate cortex;parietal lobe; 0.17151 . . . 2428.3402 9.15113 FBXO3 0.969760026410035 0.0302396039549736 3.6963499118754e-07 F-box protein 3 FUNCTION: Substrate recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. Mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. In the presence of PML, HIPK2 ubiquitination still occurs, but degradation is prevented. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53- dependent transactivation. {ECO:0000269|PubMed:18809579}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;prostate;whole body;frontal lobe;endometrium;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;prefrontal cortex; 0.31348 0.19093 -0.359940251 28.93371078 256.5808 3.44627 FBXO3-AS1 . . . FBXO3 antisense RNA 1 (head to head) . . . . . . . . . . . FBXO4 7.10839893911415e-05 0.739063821692363 0.260865094318246 F-box protein 4 FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes ubiquitination of CCND1 and its subsequent proteasomal degradation. Recognizes TERF1 and promotes its ubiquitination together with UBE2D1. {ECO:0000269|PubMed:10531035, ECO:0000269|PubMed:16275645, ECO:0000269|PubMed:18598945, ECO:0000269|PubMed:20159592, ECO:0000269|PubMed:20181953}.; . . ovary;parathyroid;vein;skin;uterus;prostate;whole body;cochlea;endometrium;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;aorta; . 0.11077 0.10076 0.016664174 55.21939137 143.35179 2.61049 FBXO5 0.982078346510874 0.0179191751676522 2.47832147406462e-06 F-box protein 5 FUNCTION: Regulates progression through early mitosis by inhibiting the anaphase promoting complex/cyclosome (APC). Binds to the APC activators CDC20 and FZR1/CDH1 to prevent APC activation. Can also bind directly to the APC to inhibit substrate-binding. {ECO:0000269|PubMed:11988738, ECO:0000269|PubMed:16921029}.; . . lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;testis;germinal center;bladder;brain;tonsil;unclassifiable (Anatomical System);pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland; dorsal root ganglion;testis - interstitial;superior cervical ganglion;fetal liver;globus pallidus;appendix;atrioventricular node;trigeminal ganglion; 0.65486 0.10924 0.439181676 77.69521113 411.83527 4.25096 FBXO6 0.00048573148176465 0.875989883943966 0.123524384574269 F-box protein 6 FUNCTION: Substrate-recognition component of some SCF (SKP1-CUL1- F-box protein)-type E3 ubiquitin ligase complexes. Involved in endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranlocated into the cytosol and promoting their ubiquitination and subsequent degradation. Able to recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex- type oligosaccharides. Also recognizes sulfated glycans. Also involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. Ubiquitination of CHEK1 is required to insure that activated CHEK1 does not accumulate as cells progress through S phase, or when replication forks encounter transient impediments during normal DNA replication. {ECO:0000269|PubMed:18203720, ECO:0000269|PubMed:19716789}.; . . . . 0.13994 0.11181 0.352813824 74.49280491 438.70808 4.36654 FBXO7 0.0987224228672443 0.899714722662918 0.00156285446983808 F-box protein 7 FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes BIRC2 and DLGAP5. Plays a role downstream of PINK1 in the clearance of damaged mitochondria via selective autophagy (mitophagy) by targeting PARK2 to dysfunctional depolarized mitochondria. Promotes MFN1 ubiquitination. {ECO:0000269|PubMed:15145941, ECO:0000269|PubMed:16510124, ECO:0000269|PubMed:23933751}.; DISEASE: Parkinson disease 15 (PARK15) [MIM:260300]: A neurodegenerative disorder characterized by parkinsonian and pyramidal signs. Clinical manifestations include tremor, bradykinesia, rigidity, postural instability, spasticity, mainly in the lower limbs, and hyperreflexia. {ECO:0000269|PubMed:18513678}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;submandibular gland;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;vein;uterus;whole body;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;hypothalamus;muscle;lung;pia mater;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; superior cervical ganglion;fetal liver;testis - interstitial;testis - seminiferous tubule;testis;parietal lobe;bone marrow; 0.06845 0.13843 0.088260113 60.56853031 65.67131 1.66951 FBXO8 0.836833761720097 0.162495855284271 0.000670382995632026 F-box protein 8 FUNCTION: May promote guanine-nucleotide exchange on an ARF. Promotes the activation of ARF through replacement of GDP with GTP (Potential). {ECO:0000305}.; . . medulla oblongata;ovary;developmental;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;lens;skeletal muscle;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;cervix;kidney;stomach;aorta; ciliary ganglion; 0.11487 0.14376 -0.183570861 39.95046001 26.90092 0.86960 FBXO9 0.734879394524417 0.265011726215458 0.000108879260125361 F-box protein 9 FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, the SCF(FBXO9) does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTORC1 is inactivated to restrain cell growth and protein translation, while mTORC2 is activated due to the relief of feedback inhibition by mTORC1. {ECO:0000269|PubMed:23263282}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;cerebellum; amygdala;whole brain;superior cervical ganglion;medulla oblongata;thalamus;occipital lobe;hypothalamus;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.07606 0.13403 -0.337894035 30.37272942 47.43335 1.33626 FBXO10 0.00149253162516481 0.997124076536353 0.00138339183848226 F-box protein 10 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. The SCF(FBXO10) complex mediates ubiquitination and degradation of BCL2, an antiapoptotic protein, thereby playing a role in apoptosis by controlling the stability of BCL2. {ECO:0000269|PubMed:23431138}.; DISEASE: Note=Defects in FBXO10 may be a cause of diffuse large B- cell lymphoma by allowing the accumulation of BCL2, an oncoprotein that has a critical role in lymphomas. {ECO:0000269|PubMed:23431138}.; . unclassifiable (Anatomical System);lung;ovary;liver;testis;blood;germinal center;thymus; dorsal root ganglion;medulla oblongata;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.34931 . -1.991601082 1.763387591 169.89282 2.84473 FBXO11 0.999979628316394 2.03716834434339e-05 1.62593906016623e-13 F-box protein 11 FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. The SCF(FBXO11) complex mediates ubiquitination and degradation of BCL6, thereby playing a role in the germinal center B-cells terminal differentiation toward memory B-cells and plasma cells. The SCF(FBXO11) complex also mediates ubiquitination and degradation of DTL, an important step for the regulation of TGF- beta signaling, cell migration and the timing of the cell-cycle progression and exit. Binds to and neddylates phosphorylated p53/TP53, inhibiting its transcriptional activity. SCF(FBXO11) does not seem to direct ubiquitination of p53/TP53. {ECO:0000269|PubMed:17098746, ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:23478441, ECO:0000269|PubMed:23478445, ECO:0000269|PubMed:23892434, ECO:0000269|PubMed:24613396}.; DISEASE: Note=Defects in FBXO11 may be a cause of diffuse large B- cell lymphoma by allowing the accumulation of BCL6, an oncoprotein that has a critical role in lymphomas. {ECO:0000269|PubMed:22113614}.; TISSUE SPECIFICITY: Isoform 5 is expressed in keratinocytes, fibroblasts and melanocytes. {ECO:0000269|PubMed:11775060}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;nasopharynx;placenta;kidney;stomach;aorta;thymus; dorsal root ganglion;amygdala;occipital lobe;testis - interstitial;superior cervical ganglion;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;appendix;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.56684 0.12641 -0.690637458 15.12149092 113.87494 2.32633 FBXO15 0.0274701773773479 0.961013230505491 0.0115165921171606 F-box protein 15 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;hypothalamus;macula lutea;testis;fovea centralis;kidney;brain;retina; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09595 0.10715 -0.402212257 26.7338995 267.77208 3.51057 FBXO16 6.61703415087813e-07 0.454532249196479 0.545467089100105 F-box protein 16 FUNCTION: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation.; . TISSUE SPECIFICITY: Expressed in heart, spleen and colon. {ECO:0000269|PubMed:12243353}.; unclassifiable (Anatomical System);smooth muscle;islets of Langerhans;colon;parathyroid;skin;skeletal muscle;retina;bone marrow;prostate;lung;nasopharynx;liver;testis;kidney;brain; . 0.04035 . 0.262810045 70.43524416 4498.3269 13.47336 FBXO17 1.22848221120316e-07 0.197402838449792 0.802597038701987 F-box protein 17 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. Able to recognize and bind denatured glycoproteins, which are modified with complex- type oligosaccharides. Also recognizes sulfated glycans. Does not bind high-mannose glycoproteins.; . TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, liver and kidney. Expressed at lower levels in spleen and brain. {ECO:0000269|PubMed:12383498}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;head and neck;spleen;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.16613 . . . 74.44966 1.80365 FBXO18 0.755821847790508 0.24417812315149 2.90580012635309e-08 F-box protein, helicase, 18 FUNCTION: 3'-5' DNA helicase and substrate-recognition component of the SCF(FBXO18) E3 ubiquitin ligase complex that plays a key role in response to stalled/damaged replication forks (PubMed:11956208, PubMed:23393192). Involved in genome maintenance by acting as an anti-recombinogenic helicase and preventing extensive strand exchange during homologous recombination: promotes RAD51 filament dissolution from stalled forks, thereby inhibiting homologous recombination and preventing excessive recombination (PubMed:17724085, PubMed:19736316). Also promotes cell death and DNA double-strand breakage in response to replication stress: together with MUS81, promotes the endonucleolytic DNA cleavage following prolonged replication stress via its helicase activity, possibly to eliminate cells with excessive replication stress (PubMed:23319600, PubMed:23361013). Plays a major role in remodeling of stalled DNA forks by catalyzing fork regression, in which the fork reverses and the two nascent DNA strands anneal (PubMed:25772361). In addition to the helicase activity, also acts as the substrate-recognition component of the SCF(FBXO18) E3 ubiquitin ligase complex, a complex that mediates ubiquitination of RAD51, leading to regulate RAD51 subcellular location (PubMed:25585578). {ECO:0000269|PubMed:11956208, ECO:0000269|PubMed:17724085, ECO:0000269|PubMed:19736316, ECO:0000269|PubMed:23319600, ECO:0000269|PubMed:23361013, ECO:0000269|PubMed:25585578, ECO:0000269|PubMed:25772361}.; DISEASE: Note=Defects in FBXO18 are frequently observed in melanomas, resulting in increased survival in response to replicative stress. Its inactivation may play a role in oncogenic transformation. {ECO:0000269|PubMed:23466708}.; . . . 0.15096 0.09809 -2.033907235 1.680820948 83.31056 1.94067 FBXO21 0.990625618968859 0.00937427883101342 1.02200127147342e-07 F-box protein 21 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . ovary;rectum;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;heart;cartilage;spinal cord;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach; amygdala;whole brain;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;cerebellum peduncles;caudate nucleus;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;adrenal gland;prefrontal cortex;globus pallidus;testis;kidney;trigeminal ganglion;parietal lobe;cerebellum; 0.28705 0.11072 -0.780646273 12.77423921 18.8244 0.65034 FBXO22 0.893814403062287 0.105970311196969 0.000215285740743699 F-box protein 22 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. Promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function. {ECO:0000269|PubMed:22972877}.; . TISSUE SPECIFICITY: Predominantly expressed in liver, also enriched in cardiac muscle. {ECO:0000269|PubMed:22972877}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;temporal lobe;appendix;testis;atrioventricular node;trigeminal ganglion; 0.10004 . -0.0274281 51.65723048 31.16585 0.98339 FBXO22-AS1 . . . FBXO22 antisense RNA 1 . . . . . . . . . . . FBXO24 0.141279967523548 0.857888169369723 0.000831863106729019 F-box protein 24 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . uterus;lymph node;islets of Langerhans;testis;blood;germinal center; testis - interstitial;testis - seminiferous tubule;testis;pons; 0.24815 0.10734 -0.576764155 18.7839113 1924.25503 8.07452 FBXO25 0.310315222130944 0.688906306136593 0.000778471732463113 F-box protein 25 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. May play a role in accumulation of expanded polyglutamine (polyQ) protein huntingtin (HTT) (By similarity). {ECO:0000250}.; DISEASE: Note=A chromosomal aberration involving FBXO25 is a cause of X-linked mental retardation (XLMR). Translocation t(X;8)(p11.22;p23.3) with SHROOM4.; TISSUE SPECIFICITY: Expressed in all brain tissue observed. {ECO:0000269|PubMed:16278047}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;uterus;prostate;cerebral cortex;bone;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);heart;cartilage;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.25545 0.11096 -0.157884861 42.05590941 1337.76087 6.86882 FBXO27 2.08184662248635e-10 0.0354326458808131 0.964567353911002 F-box protein 27 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. Able to recognize and bind denatured glycoproteins, which are modified with complex- type oligosaccharides. {ECO:0000269|PubMed:18203720}.; . TISSUE SPECIFICITY: Predominantly expressed in brain, heart and kidney. Expressed at lower levels in liver and lung. {ECO:0000269|PubMed:12383498}.; unclassifiable (Anatomical System);prostate;pancreas;lung;hypothalamus;placenta;liver;spleen;kidney;skeletal muscle; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18224 0.10419 . . 46.98347 1.32540 FBXO28 0.930139055201687 0.0697874429197644 7.35018785487944e-05 F-box protein 28 FUNCTION: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. {ECO:0000250}.; . . . . 0.56307 0.10536 0.058937498 58.26256192 29.03574 0.92860 FBXO30 0.987340441468601 0.0126585037268633 1.05480453599357e-06 F-box protein 30 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. Required for muscle atrophy following denervation. {ECO:0000250}.; . . ovary;colon;parathyroid;vein;skin;retina;uterus;prostate;endometrium;bone;testis;germinal center;ciliary body;brain;unclassifiable (Anatomical System);lymph node;cartilage;urinary;lens;skeletal muscle;bile duct;lung;placenta;hippocampus;visual apparatus;liver;kidney;aorta; . 0.36496 0.10474 -0.26629572 34.81953291 2099.17271 8.44011 FBXO31 0.911167117005807 0.0888053293979215 2.75535962713794e-05 F-box protein 31 FUNCTION: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in G1 arrest following DNA damage. Specifically recognizes phosphorylated cyclin-D1 (CCND1), promoting its ubiquitination and degradation by the proteasome, resulting in G1 arrest. May act as a tumor suppressor. {ECO:0000269|PubMed:16357137, ECO:0000269|PubMed:19412162}.; DISEASE: Mental retardation, autosomal recessive 45 (MRT45) [MIM:615979]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT45 manifestations include mild to moderate intellectual disability and dysmorphic features, including coarse facies, broad nasal bridge, fleshy nares, and thick, prominent lips. {ECO:0000269|PubMed:24623383}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in brain. Expressed at moderate levels in most tissues, except bone marrow. {ECO:0000269|PubMed:16357137}.; myocardium;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;mammary gland;stomach; atrioventricular node; 0.10830 . -0.822919685 11.76574664 24.17342 0.79350 FBXO32 0.972568188048745 0.027424725547911 7.08640334382677e-06 F-box protein 32 FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins during skeletal muscle atrophy. Recognizes TERF1. {ECO:0000269|PubMed:15531760}.; . TISSUE SPECIFICITY: Specifically expressed in cardiac and skeletal muscle.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;brain;gall bladder;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;tongue;islets of Langerhans;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;liver;kidney;mammary gland;stomach; superior cervical ganglion;skeletal muscle; 0.50082 0.22697 -0.049474214 50.01179523 503.32869 4.60351 FBXO33 0.986077142306714 0.0139215254579886 1.33223529733356e-06 F-box protein 33 FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins. Recognizes YBX1 (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;gum;thyroid;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;lens;breast;lung;placenta;macula lutea;liver;kidney;mammary gland;stomach;aorta; temporal lobe;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.56928 0.09949 -0.337894035 30.37272942 164.97193 2.80940 FBXO34 0.00459847722302636 0.964774418584277 0.0306271041926966 F-box protein 34 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;bone;testis;germinal center;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; amygdala;whole brain;occipital lobe;medulla oblongata;superior cervical ganglion;subthalamic nucleus;globus pallidus;pons;trigeminal ganglion; 0.26264 0.09132 0.312359769 72.71172446 686.72416 5.23353 FBXO36 3.22841418359222e-06 0.190168131670241 0.809828639915575 F-box protein 36 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;colon;skin;skeletal muscle;pancreas;optic nerve;lung;cochlea;endometrium;nasopharynx;placenta;bone;testis;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.18276 0.08157 0.12689526 63.00424628 1851.54095 7.93152 FBXO36-IT1 . . . FBXO36 intronic transcript 1 . . . . . . . . . . . FBXO36P1 . . . F-box protein 36 pseudogene 1 . . . . . . . . . . . FBXO38 0.999962180270506 3.78197294881352e-05 6.07960822415577e-15 F-box protein 38 FUNCTION: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. May coactivate KLF7, but does not seem to promote KLF7 ubiquitination (By similarity). {ECO:0000250}.; DISEASE: Neuronopathy, distal hereditary motor, 2D (HMN2D) [MIM:615575]: A disorder characterized by onset of slowly progressive distal lower limb weakness and atrophy between the second and fourth decades of life. Weakness usually begins in the calf muscles and later involves more proximal muscles. The severity is variable, and some patients have difficulty walking or running. Most also have upper limb involvement, particularly of the triceps and intrinsic hand muscles. Some patients may lose independent ambulation later in the disease course. Sensory impairment is typically not present, and cognition and bulbar function are normal. {ECO:0000269|PubMed:24207122}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;hypothalamus;spinal cord;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;amygdala;superior cervical ganglion;appendix;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.28234 0.10767 -0.883608246 10.50365652 2999.5379 10.39443 FBXO39 0.0250184337777255 0.916925250667204 0.0580563155550701 F-box protein 39 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;testis; . 0.12595 0.07997 1.354051915 94.39726351 4714.51122 13.86068 FBXO40 3.6419894887019e-08 0.331990200981867 0.668009762598239 F-box protein 40 FUNCTION: Probable substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that may function in myogenesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed only in heart and skeletal muscle. {ECO:0000269|PubMed:17928169}.; unclassifiable (Anatomical System);prostate;heart;bone;liver;blood;skin;skeletal muscle;bone marrow; superior cervical ganglion;skeletal muscle; 0.19390 0.10260 -0.793601146 12.57372022 3905.35622 12.34801 FBXO41 0.95177320105102 0.0482209510414936 5.84790748650861e-06 F-box protein 41 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . unclassifiable (Anatomical System);smooth muscle;lymph node;heart;ovary;islets of Langerhans;blood;skeletal muscle;bone marrow;prostate;lung;frontal lobe;visual apparatus;testis;germinal center;brain;mammary gland; dorsal root ganglion;amygdala;whole brain;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.30259 0.11150 . . 1132.93967 6.42282 FBXO42 0.975946026927229 0.0240537633220292 2.09750741338292e-07 F-box protein 42 FUNCTION: Substrate-recognition component of some SCF (SKP1-CUL1- F-box protein)-type E3 ubiquitin ligase complex. Specifically recognizes p53/TP53, promoting its ubiquitination and degradation. {ECO:0000269|PubMed:19509332}.; . . . . 0.12896 0.11149 -0.620857637 17.3566879 1007.65744 6.11533 FBXO43 0.000150255023791678 0.868061365788439 0.13178837918777 F-box protein 43 FUNCTION: Required to establish and maintain the arrest of oocytes at the second meiotic metaphase until fertilization. Probably acts by inhibiting the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase. Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation (Probable). {ECO:0000305}.; . . . . 0.40234 0.10353 0.044168103 57.40740741 766.41956 5.48364 FBXO44 3.59578966017025e-05 0.593385345354657 0.406578696748741 F-box protein 44 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex.; . TISSUE SPECIFICITY: Abundantly expressed in brain and kidney. Expressed at lower levels in heart, spleen and liver. {ECO:0000269|PubMed:12383498}.; ovary;colon;choroid;fovea centralis;skin;retina;uterus;optic nerve;frontal lobe;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;hippocampus;visual apparatus;macula lutea;duodenum;spleen;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;subthalamic nucleus;occipital lobe;temporal lobe;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;parietal lobe;cerebellum; 0.16492 . 0.220536484 68.38287332 494.28537 4.57095 FBXO45 0.857972569151264 0.139811199046568 0.00221623180216798 F-box protein 45 FUNCTION: Component of E3 ubiquitin ligase complexes. Required for normal neuromuscular synaptogenesis, axon pathfinding and neuronal migration (By similarity). Plays a role in the regulation of neurotransmission at mature neurons (By similarity). May controls synaptic activity by controlling UNC13A via ubiquitin dependent pathway (By similarity). Specifically recognizes TP73, promoting its ubiquitination and degradation. {ECO:0000250, ECO:0000269|PubMed:19581926}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;pons;cingulate cortex;parietal lobe; 0.26727 . -0.031067188 51.03798066 22.92623 0.76428 FBXO46 0.876437042044124 0.123243071710423 0.000319886245452971 F-box protein 46 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . . . . . -0.448125345 24.19202642 9.22634 0.33766 FBXO47 0.0140525574075023 0.979555824919097 0.00639161767340124 F-box protein 47 FUNCTION: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in kidney, liver and pancreas. Down-regulated in tumors. {ECO:0000269|PubMed:15723337}.; . . 0.34702 0.09302 0.284856336 71.40835103 197.8752 3.04060 FBXO48 0.0166653080454206 0.7087486957227 0.27458599623188 F-box protein 48 . . . . . 0.10683 . -0.053113545 49.38664779 6.26552 0.23637 FBXW2 0.976204028260448 0.0237713809599114 2.45907796405511e-05 F-box and WD repeat domain containing 2 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;gum;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;urinary;blood;lens;skeletal muscle;lung;placenta;macula lutea;hippocampus;alveolus;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.14719 0.09352 -0.381986487 27.68931352 12.47814 0.45392 FBXW4 0.000691009777576757 0.979529351455477 0.0197796387669461 F-box and WD repeat domain containing 4 FUNCTION: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. Likely to be involved in key signaling pathways crucial for normal limb development. May participate in Wnt signaling.; . TISSUE SPECIFICITY: Expressed in brain, kidney, lung and liver.; . . 0.17374 0.11558 -0.626318434 17.03231894 183.37204 2.93851 FBXW4P1 . . . F-box and WD repeat domain containing 4 pseudogene 1 . . . . . . . . . . . FBXW5 1.16272334357727e-08 0.0993645288954423 0.900635459477324 F-box and WD repeat domain containing 5 FUNCTION: Substrate recognition component of both SCF (SKP1-CUL1- F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. Substrate recognition component of the SCF(FBXW5) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SASS6 during S phase, leading to prevent centriole reduplication. The SCF(FBXW5) complex also mediates ubiquitination and degradation of actin-regulator EPS8 during G2 phase, leading to the transient degradation of EPS8 and subsequent cell shape changes required to allow mitotic progression. Substrate-specific adapter of the DCX(FBXW5) E3 ubiquitin-protein ligase complex which mediates the polyubiquitination and subsequent degradation of TSC2. May also act as a negative regulator of MAP3K7/TAK1 signaling in the interleukin-1B (IL1B) signaling pathway. {ECO:0000269|PubMed:18381890, ECO:0000269|PubMed:19232515, ECO:0000269|PubMed:21725316}.; . . medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; testis - interstitial;testis - seminiferous tubule;liver;testis; 0.14087 0.12028 -1.275066404 5.189903279 259.79365 3.46349 FBXW7 0.999977858674741 2.21413242744332e-05 9.84315313227968e-13 F-box and WD repeat domain containing 7 FUNCTION: Substrate recognition component of an SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter bring them to the SCF complex for ubiquitination (PubMed:17434132). Identified substrates include cyclin-E (CCNE1 or CCNE2), JUN, MYC, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1 (PubMed:11565034, PubMed:12354302, PubMed:11585921, PubMed:15103331, PubMed:14739463, PubMed:17558397, PubMed:17873522, PubMed:22608923). Acts as a negative regulator of JNK signaling by binding to phosphorylated JUN and promoting its ubiquitination and subsequent degradation (PubMed:14739463). {ECO:0000269|PubMed:11565034, ECO:0000269|PubMed:11585921, ECO:0000269|PubMed:14739463, ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:17434132, ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:17873522, ECO:0000269|PubMed:22608923, ECO:0000305|PubMed:12354302}.; . TISSUE SPECIFICITY: Isoform 1 is widely expressed. Isoform 3 is expressed in brain. {ECO:0000269|PubMed:12354302}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;placenta;hippocampus;macula lutea;liver;kidney;stomach; amygdala;medulla oblongata;subthalamic nucleus;occipital lobe;temporal lobe;prefrontal cortex;globus pallidus;pons;trigeminal ganglion;cingulate cortex;parietal lobe; 0.98577 0.62169 -0.111973265 45.35857514 117.50249 2.35679 FBXW8 8.69106598857506e-13 0.0372304325616035 0.962769567437527 F-box and WD repeat domain containing 8 FUNCTION: Substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The Cul7-RING(FBXW8) complex mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain (PubMed:21572988). Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2) (PubMed:18498745). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradatation, thereby affecting cell proliferation and differentiation (PubMed:24362026). Associated component of the 3M complex, suggesting that it mediates some of 3M complex functions (PubMed:24793695). {ECO:0000269|PubMed:18498745, ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24362026, ECO:0000269|PubMed:24793695}.; . . unclassifiable (Anatomical System);lymph node;ovary;heart;islets of Langerhans;colon;skin;bone marrow;uterus;pancreas;whole body;lung;endometrium;placenta;visual apparatus;liver;germinal center;kidney;brain;pineal gland;mammary gland;bladder;stomach; ciliary ganglion;atrioventricular node;skeletal muscle; 0.19894 0.27411 -0.28470423 33.48667138 330.90072 3.86825 FBXW9 1.9961927856908e-09 0.235283100092443 0.764716897911364 F-box and WD repeat domain containing 9 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . . . . 0.13654 0.08056 0.597144447 82.7435716 1381.90423 6.96490 FBXW10 . . . F-box and WD repeat domain containing 10 FUNCTION: Probable substrate-recognition component of a SCF (SKP1- CUL1-F-box protein)-type E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Overexpression is leading to degradation of CBX5 and CBX1. {ECO:0000269|PubMed:20498703}.; . . unclassifiable (Anatomical System);breast;lung;bone;testis;kidney;brain; . 0.34021 0.08511 1.271321208 93.65416372 5966.82868 16.06479 FBXW11 0.997161483868132 0.00283851061709708 5.51477059714903e-09 F-box and WD repeat domain containing 11 FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins. SCF(FBXW11) mediates the ubiquitination of phosphorylated CTNNB1 and participates in Wnt signaling. SCF(FBXW11) mediates the ubiquitination of phosphorylated NFKBIA, which degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. SCF(FBXW11) mediates the ubiquitination of IFNAR1. SCF(FBXW11) mediates the ubiquitination of CEP68; this is required for centriole separation during mitosis (PubMed:25503564). Involved in the oxidative stress-induced a ubiquitin-mediated decrease in RCAN1. Mediates the degradation of CDC25A induced by ionizing radiation in cells progressing through S phase and thus may function in the intra-S- phase checkpoint. Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and phosphorylated PER2. Is target of human immunodeficiency virus type 1 (HIV-1) protein VPU to polyubiquitinate and deplete BST2 from cells and antagonize its antiviral action. {ECO:0000269|PubMed:10321728, ECO:0000269|PubMed:10437795, ECO:0000269|PubMed:10644755, ECO:0000269|PubMed:10648623, ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:14603323, ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:18575781, ECO:0000269|PubMed:19730691, ECO:0000269|PubMed:19966869, ECO:0000269|PubMed:20347421, ECO:0000269|PubMed:25503564}.; . . ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;nervous;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach;peripheral nerve; whole brain;dorsal root ganglion;amygdala;testis - interstitial;occipital lobe;superior cervical ganglion;hypothalamus;atrioventricular node;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.63280 0.16023 -0.471992905 23.03609342 11.11765 0.40246 FBXW11P1 . . . F-box and WD repeat domain containing 11 pseudogene 1 . . . . . . . . . . . FBXW12 1.97457661872321e-07 0.671732731204732 0.328267071337606 F-box and WD repeat domain containing 12 FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15040455}.; . . 0.04217 0.06211 0.777157784 87.17857985 310.28271 3.74713 FCAMR 8.00343370771682e-06 0.509407430485307 0.490584566080986 Fc fragment of IgA and IgM receptor FUNCTION: Functions as a receptor for the Fc fragment of IgA and IgM. Binds IgA and IgM with high affinity and mediates their endocytosis. May function in the immune response to microbes mediated by IgA and IgM. {ECO:0000269|PubMed:11779189}.; . TISSUE SPECIFICITY: Expressed by mesangial cells. {ECO:0000269|PubMed:11779189}.; unclassifiable (Anatomical System);ovary;colon;kidney;stomach; dorsal root ganglion;superior cervical ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.04742 0.36294 1.532271902 95.54140127 465.81874 4.47034 FCAR 0.000228786600561729 0.750187300232957 0.249583913166481 Fc fragment of IgA receptor FUNCTION: Binds to the Fc region of immunoglobulins alpha. Mediates several functions including cytokine production. {ECO:0000269|PubMed:12768205}.; . TISSUE SPECIFICITY: Isoform A.1, isoform A.2 and isoform A.3 are differentially expressed between blood and mucosal myeloid cells. Isoform A.1, isoform A.2 and isoform A.3 are expressed in monocytes. Isoform A.1 and isoform A.2 are expressed in alveolar macrophages; however only one isoform is expressed at alveolar macrophages surfaces. {ECO:0000269|PubMed:8666819, ECO:0000269|PubMed:8836118}.; unclassifiable (Anatomical System);blood;bone marrow; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin;bone marrow; 0.05137 0.10575 0.396906589 76.30927105 445.22601 4.39150 FCER1A 0.0025580283628798 0.784897097013871 0.212544874623249 Fc fragment of IgE receptor Ia FUNCTION: Binds to the Fc region of immunoglobulins epsilon. High affinity receptor. Responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The same receptor also induces the secretion of important lymphokines.; . . . . 0.02724 0.73135 0.12689526 63.00424628 165.88815 2.81789 FCER1G 0.635845638352269 0.35737275098388 0.00678161066385073 Fc fragment of IgE receptor Ig FUNCTION: Associates with a variety of FcR alpha chains to form a functional signaling complex. Regulates several aspects of the immune response. The gamma subunit has a critical role in allowing the IgE Fc receptor to reach the cell surface. Also involved in collagen-mediated platelet activation and in neutrophil activation mediated by integrin. {ECO:0000269|PubMed:8611682}.; . . myocardium;umbilical cord;colon;choroid;skin;bone marrow;uterus;whole body;frontal lobe;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; whole blood; 0.11372 0.14394 0.3455435 73.78509082 28.27342 0.90665 FCER2 1.50208228042754e-09 0.109896050935813 0.890103947562105 Fc fragment of IgE receptor II FUNCTION: Low-affinity receptor for immunoglobulin E (IgE) and CR2/CD21. Has essential roles in the regulation of IgE production and in the differentiation of B-cells (it is a B-cell-specific antigen).; . . unclassifiable (Anatomical System);lung;testis;blood;germinal center;tonsil;aorta;bone marrow; superior cervical ganglion; 0.07031 . 0.310540264 72.65864591 2245.71524 8.74684 FCF1 0.934256694936662 0.0656802994801493 6.30055831884291e-05 FCF1 rRNA-processing protein FUNCTION: Essential protein involved in pre-rRNA processing and 40S ribosomal subunit assembly. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;heart;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;bone marrow;breast;uterus;prostate;whole body;lung;cornea;placenta;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland; dorsal root ganglion;thyroid;globus pallidus;skeletal muscle; 0.20531 0.13588 -0.05129383 49.75819769 72.49327 1.77481 FCF1P1 . . . FCF1 pseudogene 1 . . . . . . . . . . . FCF1P2 . . . FCF1 pseudogene 2 . . . . . . . . . . . FCF1P3 . . . FCF1 pseudogene 3 . . . . . . . . . . . FCF1P4 . . . FCF1 pseudogene 4 . . . . . . . . . . . FCF1P5 . . . FCF1 pseudogene 5 . . . . . . . . . . . FCF1P6 . . . FCF1 pseudogene 6 . . . . . . . . . . . FCF1P7 . . . FCF1 pseudogene 7 . . . . . . . . . . . FCF1P8 . . . FCF1 pseudogene 8 . . . . . . . . . . . FCF1P9 . . . FCF1 pseudogene 9 . . . . . . . . . . . FCF1P10 . . . FCF1 pseudogene 10 . . . . . . . . . . . FCF1P11 . . . FCF1 pseudogene 11 . . . . . . . . . . . FCGBP . . . Fc fragment of IgG binding protein FUNCTION: May be involved in the maintenance of the mucosal structure as a gel-like component of the mucosa. {ECO:0000269|PubMed:9182547}.; . TISSUE SPECIFICITY: Mainly expressed in placenta and colon epithelium. Expressed in thyroid, and down-regulated in thyroid carcinomas. Present in serum, with higher levels in patients with various autoimmune diseases (at protein level). {ECO:0000269|PubMed:11600203, ECO:0000269|PubMed:12208673, ECO:0000269|PubMed:9182547}.; lymphoreticular;myocardium;ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);tongue;islets of Langerhans;muscle;blood;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;trachea;thyroid;fetal thyroid; 0.54275 . . . 18359.5916 28.93384 FCGR1A 0.97163343240963 0.0283286152914141 3.79522989562642e-05 Fc fragment of IgG receptor Ia FUNCTION: High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses. {ECO:0000269|PubMed:10397749, ECO:0000269|PubMed:10514529, ECO:0000269|PubMed:21965667, ECO:0000269|PubMed:8611682, ECO:0000269|PubMed:9881690}.; . TISSUE SPECIFICITY: Monocyte/macrophage specific.; . . 0.10110 0.26466 . . 63.31925 1.62893 FCGR1B 0.676508623032471 0.318794230303266 0.00469714666426312 Fc fragment of IgG receptor Ib FUNCTION: May bind to the Fc region of immunoglobulins gamma with a low affinity compared to FCGR1A. May function in the humoral immune response. {ECO:0000269|PubMed:1430234, ECO:0000269|PubMed:9881690}.; . . . . . 0.07223 . . 1164.44041 6.49256 FCGR1CP . . . Fc fragment of IgG receptor Ic, pseudogene FUNCTION: May bind to the Fc region of immunoglobulins gamma. May function in the humoral immune response (By similarity). {ECO:0000250}.; . . . . . 0.26466 . . . . FCGR2A 0.000150862363564485 0.663432186668333 0.336416950968103 Fc fragment of IgG receptor IIa FUNCTION: Binds to the Fc region of immunoglobulins gamma. Low affinity receptor. By binding to IgG it initiates cellular responses against pathogens and soluble antigens. Promotes phagocytosis of opsonized antigens. {ECO:0000269|PubMed:19011614}.; . TISSUE SPECIFICITY: Found on monocytes, neutrophils and eosinophil platelets.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;bone;testis;brain;unclassifiable (Anatomical System);amygdala;cartilage;tongue;pharynx;blood;lens;breast;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; . 0.15715 . 0.841481379 88.35810333 565.82336 4.83249 FCGR2B 0.0474026079439954 0.855728325274511 0.0968690667814938 Fc fragment of IgG receptor IIb FUNCTION: Receptor for the Fc region of complexed or aggregated immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of immune complexes and modulation of antibody production by B- cells. Binding to this receptor results in down-modulation of previous state of cell activation triggered via antigen receptors on B-cells (BCR), T-cells (TCR) or via another Fc receptor. Isoform IIB1 fails to mediate endocytosis or phagocytosis. Isoform IIB2 does not trigger phagocytosis.; DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:12115230, ECO:0000269|PubMed:20385827}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Is the most broadly distributed Fc-gamma- receptor. Expressed in monocyte, neutrophils, macrophages, basophils, eosinophils, Langerhans cells, B-cells, platelets cells and placenta (endothelial cells). Not detected in natural killer cells.; unclassifiable (Anatomical System);smooth muscle;lymph node;ovary;islets of Langerhans;colon;blood;choroid;skin;retina;uterus;pancreas;lung;nasopharynx;bone;placenta;liver;testis;spleen;germinal center;kidney;brain;mammary gland; placenta; . 0.12522 0.060756528 58.52795471 1693.68129 7.58570 FCGR2C . . . Fc fragment of IgG receptor IIc (gene/pseudogene) FUNCTION: Receptor for the Fc region of complexed immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of immune complexes and modulation of antibody production by B-cells.; . TISSUE SPECIFICITY: Isoform IIC1 is detected in monocytes, macrophages, polymorphonuclear cells and natural killer cells.; . . . 0.12522 . . . . FCGR3A 1.22273626907589e-05 0.37487787713909 0.625109895498219 Fc fragment of IgG receptor IIIa FUNCTION: Receptor for the Fc region of IgG. Binds complexed or aggregated IgG and also monomeric IgG. Mediates antibody-dependent cellular cytotoxicity (ADCC) and other antibody-dependent responses, such as phagocytosis. {ECO:0000269|PubMed:21768335, ECO:0000269|PubMed:22023369}.; DISEASE: Immunodeficiency 20 (IMD20) [MIM:615707]: A rare autosomal recessive primary immunodeficiency characterized by functional deficiency of NK cells. Affected individuals typically present with severe herpes viral infections, particularly Epstein Barr virus (EBV), and human papillomavirus (HPV). {ECO:0000269|PubMed:23006327, ECO:0000269|PubMed:8608639, ECO:0000269|PubMed:8609432, ECO:0000269|PubMed:8874200}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed on natural killer cells, macrophages, subpopulation of T-cells, immature thymocytes and placental trophoblasts.; . . 0.01788 0.14705 0.440999548 77.79547063 98.19478 2.14247 FCGR3B 3.30211049830827e-05 0.354127220295679 0.645839758599338 Fc fragment of IgG receptor IIIb FUNCTION: Receptor for the Fc region of immunoglobulins gamma. Low affinity receptor. Binds complexed or aggregated IgG and also monomeric IgG. Contrary to III-A, is not capable to mediate antibody-dependent cytotoxicity and phagocytosis. May serve as a trap for immune complexes in the peripheral circulation which does not activate neutrophils.; . TISSUE SPECIFICITY: Expressed specifically by polymorphonuclear leukocytes (neutrophils). Also expressed by stimulated eosinophils.; smooth muscle;ovary;colon;parathyroid;bone marrow;uterus;prostate;ganglion;frontal lobe;cerebral cortex;endometrium;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;blood;breast;pancreas;lung;nasopharynx;placenta;liver;alveolus;spleen;kidney;stomach; superior cervical ganglion;whole blood;bone marrow; 0.00848 0.09063 -0.115612493 45.12856806 161.44959 2.77603 FCGRT 0.825587179671645 0.173609763697004 0.000803056631351571 Fc fragment of IgG receptor and transporter FUNCTION: Binds to the Fc region of monomeric immunoglobulins gamma. Mediates the uptake of IgG from milk. Possible role in transfer of immunoglobulin G from mother to fetus.; . . myocardium;lymphoreticular;medulla oblongata;ovary;sympathetic chain;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;epididymis;macula lutea;visual apparatus;liver;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;placenta;hippocampus;kidney;aorta;stomach;thymus; liver;whole blood; 0.39576 0.41470 -0.137658575 43.57159707 99.2347 2.15632 FCHO1 0.998992547558912 0.0010074524230263 1.80621538113599e-11 FCH domain only 1 FUNCTION: Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. May regulate Bmp signaling by regulating clathrin-mediated endocytosis of Bmp receptors. {ECO:0000269|PubMed:20448150}.; . . unclassifiable (Anatomical System);lymph node;ovary;muscle;colon;lens;bone marrow;uterus;lung;visual apparatus;testis;head and neck;cervix;germinal center;brain;stomach; superior cervical ganglion;medulla oblongata;cerebellum peduncles;prefrontal cortex;pons;trigeminal ganglion; 0.54261 0.09810 -1.102280959 6.912007549 126.48054 2.44985 FCHO2 0.999038489396249 0.000961508657990929 1.94576054288681e-09 FCH domain only 2 FUNCTION: Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP- 2-dependent endocytosis of the transferin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor. {ECO:0000269|PubMed:17540576, ECO:0000269|PubMed:20448150, ECO:0000269|PubMed:21762413, ECO:0000269|PubMed:22323290}.; . . ovary;colon;parathyroid;skin;uterus;whole body;endometrium;larynx;thyroid;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;lacrimal gland;oral cavity;adrenal cortex;breast;pia mater;lung;placenta;visual apparatus;liver;head and neck;spleen;kidney;stomach;cerebellum; superior cervical ganglion; 0.70872 0.09884 0.064394823 58.84642604 1018.65668 6.14083 FCHSD1 1.92350768763502e-16 0.0493374125939209 0.950662587406079 FCH and double SH3 domains 1 . . . . . 0.10818 0.08823 0.227815529 68.53621137 837.75243 5.66885 FCHSD2 0.994752587131223 0.00524740786683739 5.00193900470488e-09 FCH and double SH3 domains 2 . . TISSUE SPECIFICITY: Liver, brain, heart, placenta, skeletal muscle, pancreas, lung and kidney. {ECO:0000269|PubMed:14627983}.; medulla oblongata;ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;adrenal cortex;pancreas;lung;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; amygdala;subthalamic nucleus;white blood cells; 0.39961 0.11323 -0.88906181 10.36801132 103.87407 2.20142 FCMR . . . Fc fragment of IgM receptor FUNCTION: May play a role in the immune system processes. Protects cells from FAS-, TNF alpha- and FADD-induced apoptosis without increasing expression of the inhibitors of apoptosis BCL2 and BCLXL. Seems to activate an inhibitory pathway that prevents CASP8 activation following FAS stimulation, rather than blocking apoptotic signals downstream. May inhibit FAS-induced apoptosis by preventing CASP8 processing through CFLAR up-regulation. {ECO:0000269|PubMed:9586636}.; . TISSUE SPECIFICITY: Expressed in lymph nodes, peripheral blood leukocytes, lung, thymus and kidneys. Very weak expression detected in spleen, liver, heart, and salivary gland. Expressed in lymphoid cell lines such as Jurkat, CEM-T4, MOLT-4, HB11;19 and Reh. No expression detected in nonhematopoietic cell lines including Hep-G2, HEK293 and HeLa. Detected at high levels in chronic lymphocytic leukemia cells. {ECO:0000269|PubMed:21908424, ECO:0000269|PubMed:9586636}.; . . 0.09171 0.09949 0.016664174 55.21939137 . . FCMTE1 . . . familial cortical myoclonic tremor with epilepsy 1 . . . . . . . . . . . FCMTE2 . . . familial cortical myoclonic tremor with epilepsy 2 . . . . . . . . . . . FCMTE3 . . . familial cortical myoclonic tremor with epilepsy 3 . . . . . . . . . . . FCN1 1.2564580969204e-11 0.0252519862939865 0.974748013693449 ficolin 1 FUNCTION: Extracellular lectin functioning as a pattern- recognition receptor in innate immunity. Binds the sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes and activates the lectin pathway of the complement system. May also activate monocytes through a G protein-coupled receptor, FFAR2, inducing the secretion of interleukin-8/IL-8 (PubMed:21037097). Binds preferentially to 9-O-acetylated 2-6- linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage. {ECO:0000269|PubMed:20032467, ECO:0000269|PubMed:21037097}.; . TISSUE SPECIFICITY: Peripheral blood leukocytes, monocytes and granulocytes. Also detected in spleen, lung, and thymus, may be due to the presence of tissue macrophages or trapped blood in these tissues. Not detected on lymphocytes. {ECO:0000269|PubMed:20400674}.; unclassifiable (Anatomical System);blood;fovea centralis;choroid;lens;bone marrow;retina;optic nerve;lung;placenta;bone;macula lutea;liver;spleen;mammary gland; whole blood;bone marrow; 0.26534 . -0.264476624 34.8844067 141.94751 2.60118 FCN2 1.93230355683024e-09 0.126502910314143 0.873497087753553 ficolin 2 FUNCTION: May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc- binding lectin. Enhances phagocytosis of S.typhimurium by neutrophils, suggesting an opsonic effect via the collagen region. {ECO:0000269|PubMed:10679061, ECO:0000269|PubMed:17215869}.; . TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; liver;spleen;blood;bone marrow; liver;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09798 0.09630 0.578735925 82.29535268 4032.47143 12.58303 FCN3 0.0172513382815348 0.960327318053166 0.022421343665299 ficolin 3 FUNCTION: May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc- binding lectin. Has affinity with GalNAc, GlcNAc, D-fucose, as mono/oligosaccharide and lipopolysaccharides from S.typhimurium and S.minnesota. {ECO:0000269|PubMed:11907111, ECO:0000269|PubMed:17215869}.; DISEASE: Ficolin 3 deficiency (FCN3D) [MIM:613860]: A disorder characterized by immunodeficiency, recurrent infections, brain abscesses and recurrent warts on the fingers. Affected individuals have normal levels of lymphocytes, normal T-cell responses, and normal antibodies, but a selective deficient antibody response to pneumococcal polysaccharide vaccine. {ECO:0000269|PubMed:19535802}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver and lung. In liver it is produced by bile duct epithelial cells and hepatocytes. In lung it is produced by both ciliated bronchial epithelial cells and type II alveolar epithelial cells. {ECO:0000269|PubMed:10330454}.; unclassifiable (Anatomical System);islets of Langerhans;colon;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;adrenal gland;placenta;macula lutea;liver;testis;spleen;kidney;brain;gall bladder; fetal liver;liver;fetal lung; 0.09658 0.11286 0.308721233 72.59966973 193.54891 3.01786 FCP1 . . . F-cell production 1 . . . . . . . . . . . FCRL1 0.00159526703104064 0.969712500688868 0.0286922322800916 Fc receptor like 1 FUNCTION: May function as an activating coreceptor in B-cells. May function in B-cells activation and differentiation. {ECO:0000269|PubMed:15479727}.; . TISSUE SPECIFICITY: Primarily expressed in secondary lymphoid tissues by mature subsets of B-cells. Detected in spleen, lymph node, heart, skeletal muscle, kidney, liver and placenta. Specifically expressed by mature B lineage cells with higher expression in naive versus memory B-cells (at protein level). {ECO:0000269|PubMed:11493702, ECO:0000269|PubMed:11929751, ECO:0000269|PubMed:15479727, ECO:0000269|PubMed:16849395}.; unclassifiable (Anatomical System);pancreas;lymph node;lung;nasopharynx;placenta;liver;testis;spleen;germinal center; superior cervical ganglion;skeletal muscle; 0.07901 0.08898 0.644875971 84.10002359 530.37396 4.70073 FCRL2 0.000160040383245631 0.968072631773163 0.0317673278435917 Fc receptor like 2 FUNCTION: May have an regulatory role in normal and neoplastic B cell development. {ECO:0000269|PubMed:11493702}.; . TISSUE SPECIFICITY: Expressed in the secondary lymphoid organs, spleen and lymph node. Expression is limited to the mature B-cell lines. Highly expressed in CD19 and within the mantle zones of the tonsil tissue. Isoform 2 is expressed in the spleen, peripheral blood and bone marrow. Isoform 2 and isoform 4 are expressed in B- cell lines. Preferentially expressed in memory B-cells (at protein level). {ECO:0000269|PubMed:11162587, ECO:0000269|PubMed:11493702, ECO:0000269|PubMed:11929751, ECO:0000269|PubMed:16849395}.; lymphoreticular;endometrium;tongue;spleen;head and neck;germinal center; dorsal root ganglion;superior cervical ganglion; 0.15420 0.07766 -0.198338176 39.17197452 237.32527 3.32617 FCRL3 4.5604025041299e-18 0.00287659349909668 0.997123406500903 Fc receptor like 3 . DISEASE: Rheumatoid arthritis (RA) [MIM:180300]: An inflammatory disease with autoimmune features and a complex genetic component. It primarily affects the joints and is characterized by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures. {ECO:0000269|PubMed:15838509, ECO:0000269|PubMed:16176992, ECO:0000269|PubMed:16476711, ECO:0000269|PubMed:16859508, ECO:0000269|PubMed:17133579, ECO:0000269|PubMed:17179172, ECO:0000269|PubMed:17763442}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=Genetic variation in FCRL3 may influence susceptibility to autoimmune disorders, including Graves disease. Graves disease is an autoimmune disorder associated with overactivity of the thyroid gland and hyperthyroidism. {ECO:0000269|PubMed:15838509, ECO:0000269|PubMed:16384851, ECO:0000269|PubMed:17952073}.; TISSUE SPECIFICITY: Primarily expressed in secondary lymphoid tissues by mature subsets of B-cells. Detected in spleen, lymph node, peripheral blood lymphocytes, thymus, bone marrow, kidney, salivary gland, adrenal gland and uterus. Expressed a low levels in naive, germinal center and memory B-cells but also expressed in NK cells (at protein level). {ECO:0000269|PubMed:11493702, ECO:0000269|PubMed:11929751, ECO:0000269|PubMed:12051764, ECO:0000269|PubMed:15838509, ECO:0000269|PubMed:16849395}.; nasopharynx;germinal center; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11005 . 1.252926935 93.48313281 356.99736 4.00289 FCRL4 1.59511072407105e-07 0.843063415820287 0.156936424668641 Fc receptor like 4 FUNCTION: May function as an inhibitor of the B-cell receptor signaling. May function in the B-cell-mediated immune response. {ECO:0000269|PubMed:14597715}.; DISEASE: Note=A chromosomal aberration involving FCRL4 is found in non-Hodgkin lymphoma (NHG). Translocation t(1;1)(p36.3; q21.1-2). {ECO:0000269|PubMed:12619161}.; DISEASE: Note=A chromosomal aberration involving FCRL4 is found in multiple myeloma (MM). Translocation t(1;14)(q21;q32) that forms a FCRL4-IGHA1 fusion protein. {ECO:0000269|PubMed:11290337}.; TISSUE SPECIFICITY: Specifically expressed by memory and monocytoid B-cells which populate spleen and lymph nodes. Preferentially expressed in memory B-cells associated with mucosal tissue (at protein level). {ECO:0000269|PubMed:11290337, ECO:0000269|PubMed:11929751, ECO:0000269|PubMed:12881317, ECO:0000269|PubMed:16079106, ECO:0000269|PubMed:16157685, ECO:0000269|PubMed:16849395}.; unclassifiable (Anatomical System);lung;testis;germinal center; ciliary ganglion;atrioventricular node; 0.04926 0.08563 0.512596355 80.29606039 105.58892 2.22693 FCRL5 7.49244691962338e-14 0.062143889385888 0.937856110614037 Fc receptor like 5 FUNCTION: May be involved in B-cell development and differentiation in peripheral lymphoid organs and may be useful markers of B-cell stages. May have an immunoregulatory role in marginal zone B-cells. {ECO:0000269|PubMed:11453668}.; DISEASE: Note=A chromosomal aberration involving FCRL5 has been found in cell lines with 1q21 abnormalities derived from Burkitt lymphoma. Duplication dup(1)(q21q32). {ECO:0000269|PubMed:11290337}.; TISSUE SPECIFICITY: Expressed in marginal zone B-cells, immunoblasts, tonsillar germinal center centrocytes and in the intraepithelial and interfollicular regions of the tonsil. Expressed in many lymphoma cell lines and on hairy cell leukemia cells. Isoform 1, isoform 3, isoform 4 and isoform 5 are detected in lymph node, spleen, bone marrow, and small intestine with preponderance of isoform 3. Expressed in mature and memory B-cells and down-regulated in germinal center cells (at protein level). {ECO:0000269|PubMed:11290337, ECO:0000269|PubMed:11929751, ECO:0000269|PubMed:16849395}.; unclassifiable (Anatomical System);lymph node;tongue;adrenal cortex;colon;parathyroid;blood;skeletal muscle;uterus;pancreas;lung;adrenal gland;thyroid;testis;head and neck;germinal center;pineal gland; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.04519 . 2.274625269 98.25430526 998.13105 6.08728 FCRL6 5.08221240608822e-14 0.00707259130406633 0.992927408695883 Fc receptor like 6 . . TISSUE SPECIFICITY: Expressed by cytolytic cells including NK cells, effector and effector-memory CD8+ T-cells. Expression among T-cells is greatly expanded in HIV-1 infected individuals, and includes not only effector and effector-memory CD8+ T-cells but also populations of CD4+ T-cells. {ECO:0000269|PubMed:17213291}.; uterus;pancreas;colon; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.04934 0.07352 0.270087468 70.69473933 1480.88076 7.16599 FCRL6P1 . . . Fc receptor like 6 pseudogene 1 . . . . . . . . . . . FCRLA 0.000166358002713443 0.684428385049454 0.315405256947833 Fc receptor like A FUNCTION: May be implicated in B-cell differentiation and lymphomagenesis. {ECO:0000269|PubMed:11754007, ECO:0000269|PubMed:11891275}.; . TISSUE SPECIFICITY: Expressed specifically in primary and secondary lymphoid tissues like lymph node, spleen and tonsil. Specifically expressed in B-cells with a high level in normal germinal center B-cells, centroblasts and in a subset of diffuse large B-cell lymphomas. Highly expressed in bone marrow B-cells and weakly in earlier B lineage cells. Expressed in pre-germinal and germinal center B-cells in secondary lymphoid tissues. Also expressed in melanoma and melanocytes. {ECO:0000269|PubMed:11754007, ECO:0000269|PubMed:11891275, ECO:0000269|PubMed:12202404, ECO:0000269|PubMed:15551350}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;cartilage;heart;tongue;blood;skin;bone marrow;uterus;pancreas;nasopharynx;head and neck;spleen;germinal center;tonsil; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.10014 0.10516 0.486911049 79.46449634 496.23442 4.57922 FCRLB 1.19992605936002e-08 0.101144300387823 0.898855687612917 Fc receptor like B . . TISSUE SPECIFICITY: Expressed at low levels. Expressed in B- lymphocytes. Detected in tonsil, lung, kidney, spleen and placenta. Expressed by a small subset of germinal center B-cells in tonsils and by melanocytes (at protein level). {ECO:0000269|PubMed:15551350, ECO:0000269|PubMed:15676285, ECO:0000269|PubMed:15815692, ECO:0000269|PubMed:16263223}.; unclassifiable (Anatomical System);breast;lymph node;cartilage;placenta;muscle;skin; atrioventricular node; 0.17548 0.11384 0.751474114 86.64779429 1860.22338 7.94948 FDCSP 0.358744941994043 0.589132193848472 0.0521228641574852 follicular dendritic cell secreted protein FUNCTION: Can bind to the surface of B-lymphoma cells, but not T- lymphoma cells, consistent with a function as a secreted mediator acting upon B-cells.; . TISSUE SPECIFICITY: Abundantly expressed in tonsil, lymph node, and trachea; strong expression in prostate; lower expression in thyroid, stomach, and colon. {ECO:0000269|PubMed:12193705}.; unclassifiable (Anatomical System);lymph node;adrenal cortex;colon;parathyroid;blood;prostate;lung;adrenal gland;nasopharynx;thyroid;liver;head and neck;mammary gland;pineal gland;aorta; . 0.01019 0.03189 -0.031067188 51.03798066 4.74355 0.17328 FDFT1 . . . farnesyl-diphosphate farnesyltransferase 1 . . . lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;ciliary body;heart;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach; whole brain;lung;hypothalamus;spinal cord;prefrontal cortex;testis; 0.18108 0.26710 -1.131590109 6.481481481 295.40734 3.66942 FDPS 0.00175127849063184 0.972949491066754 0.0252992304426147 farnesyl diphosphate synthase FUNCTION: Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.; DISEASE: Porokeratosis 9, multiple types (POROK9) [MIM:616631]: A form of porokeratosis, a disorder of faulty keratinization characterized by one or more atrophic patches surrounded by a distinctive hyperkeratotic ridgelike border called the cornoid lamella. The keratotic lesions can progress to overt cutaneous neoplasms, typically squamous cell carcinomas. Multiple clinical variants of porokeratosis are recognized, including porokeratosis of Mibelli, linear porokeratosis, disseminated superficial actinic porokeratosis, palmoplantar porokeratosis, and punctate porokeratosis. Different clinical presentations can be observed among members of the same family. Individuals expressing more than one variant have also been reported. {ECO:0000269|PubMed:26202976}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;skin;bone marrow;prostate;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;larynx;bone;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;amnion;head and neck;kidney;stomach;thymus; . 0.17645 0.35141 0.571462851 81.99457419 126.3179 2.44712 FDPSP1 . . . farnesyl diphosphate synthase pseudogene 1 . . . . . . . . . . . FDPSP2 . . . farnesyl diphosphate synthase pseudogene 2 . . . . . . . . . . . FDPSP3 . . . farnesyl diphosphate synthase pseudogene 3 . . . . . . . . . . . FDPSP4 . . . farnesyl diphosphate synthase pseudogene 4 . . . . . . . . . . . FDPSP5 . . . farnesyl diphosphate synthase pseudogene 5 . . . . . . . . . . . FDPSP6 . . . farnesyl diphosphate synthase pseudogene 6 . . . . . . . . . . . FDPSP7 . . . farnesyl diphosphate synthase pseudogene 7 . . . . . . . . . . . FDPSP8 . . . farnesyl diphosphate synthase pseudogene 8 . . . . . . . . . . . FDPSP9 . . . farnesyl diphosphate synthase pseudogene 9 . . . . . . . . . . . FDPSP10 . . . farnesyl diphosphate synthase pseudogene 10 . . . . . . . . . . . FDX1 0.0839816283786201 0.75885167258279 0.15716669903859 ferredoxin 1 FUNCTION: Participates in the synthesis of thyroid hormones. Essential for the synthesis of various steroid hormones, participates in the reduction of mitochondrial cytochrome P450 for steroidogenesis. Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain cleavage. {ECO:0000269|PubMed:20547883, ECO:0000269|PubMed:21636783}.; . TISSUE SPECIFICITY: Highest levels in the adrenal gland (at protein level). Also detected in kidney and testis (at protein level). {ECO:0000269|PubMed:20547883}.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;hippocampus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; adrenal gland;placenta;adrenal cortex;trigeminal ganglion; 0.18193 0.30744 . . 20.08686 0.68660 FDX1L 0.00318935064209165 0.599628833804476 0.397181815553432 ferredoxin 1-like FUNCTION: Essential for heme A and Fe/S protein biosynthesis. {ECO:0000269|PubMed:20547883}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in testis, kidney and brain (at protein level). {ECO:0000269|PubMed:20547883}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;vein;skin;uterus;prostate;lung;placenta;thyroid;visual apparatus;testis;kidney;brain; superior cervical ganglion;occipital lobe;subthalamic nucleus;globus pallidus;trigeminal ganglion;parietal lobe; 0.11643 0.10474 0.349177632 74.18023119 81.69702 1.91540 FDX1P1 . . . ferredoxin 1 pseudogene 1 . . . . . . . . . . . FDX1P2 . . . ferredoxin 1 pseudogene 2 . . . . . . . . . . . FDXACB1 3.14671300310384e-07 0.320888710756768 0.679110974571931 ferredoxin-fold anticodon binding domain containing 1 . . . colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;lens;pancreas;lung;nasopharynx;macula lutea;liver;spleen;kidney;stomach; dorsal root ganglion;testis;skeletal muscle; . . 0.42623145 77.29417315 221.00441 3.21582 FDXR 0.000894955007086674 0.985265334660726 0.0138397103321877 ferredoxin reductase FUNCTION: Serves as the first electron transfer protein in all the mitochondrial P450 systems. Including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver.; . . ovary;colon;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;synovium;bone;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;adrenal cortex;skeletal muscle;bile duct;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; testis - seminiferous tubule;adrenal gland;adrenal cortex;testis; 0.11072 0.38259 0.536463361 81.06864827 1785.73974 7.80110 FEB1 . . . febrile convulsions 1 . . . . . . . . . . . FEB2 . . . febrile convulsions 2 . . . . . . . . . . . FEB4 . . . febrile convulsions 4 . . . . . . . . . . . FEB5 . . . febrile convulsions 5 . . . . . . . . . . . FEB6 . . . febrile convulsions 6 . . . . . . . . . . . FEB7 . . . febrile convulsions 7 . . . . . . . . . . . FECH 0.138946552569902 0.860195859326802 0.000857588103295649 ferrochelatase FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.; DISEASE: Erythropoietic protoporphyria (EPP) [MIM:177000]: A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. Erythropoietic protoporphyria is marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals. {ECO:0000269|PubMed:10942404, ECO:0000269|PubMed:11375302, ECO:0000269|PubMed:12063482, ECO:0000269|PubMed:12601550, ECO:0000269|PubMed:1376018, ECO:0000269|PubMed:15286165, ECO:0000269|PubMed:17196862, ECO:0000269|PubMed:1755842, ECO:0000269|PubMed:7910885, ECO:0000269|PubMed:8757534, ECO:0000269|PubMed:9585598, ECO:0000269|PubMed:9740232}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;larynx;testis;unclassifiable (Anatomical System);islets of Langerhans;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach; dorsal root ganglion;fetal liver;superior cervical ganglion;ciliary ganglion;atrioventricular node;bone marrow; 0.43819 0.30344 0.042348793 57.31304553 497.02805 4.58177 FECHP1 . . . ferrochelatase pseudogene 1 . . . . . . . . . . . FEM1A . . . fem-1 homolog a (C. elegans) FUNCTION: Probable component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit (By similarity). May participate in antiinflammatory signaling via its interaction with PTGER4. {ECO:0000250}.; . TISSUE SPECIFICITY: Present in macrophages derived from peripheral blood monocytes. Also present in atheromata (at protein level). {ECO:0000269|PubMed:16424369}.; lymphoreticular;myocardium;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;testis;germinal center;spinal ganglion;ciliary body;brain;unclassifiable (Anatomical System);heart;cartilage;blood;skeletal muscle;pancreas;lung;placenta;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;thalamus;superior cervical ganglion;temporal lobe;atrioventricular node;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;parietal lobe;cerebellum; 0.22328 0.11703 -0.003562597 53.72729417 33.87624 1.04170 FEM1AP1 . . . fem-1 homolog a (C. elegans) pseudogene 1 . . . . . . . . . . . FEM1AP2 . . . fem-1 homolog a (C. elegans) pseudogene 2 . . . . . . . . . . . FEM1AP3 . . . fem-1 homolog a (C. elegans) pseudogene 3 . . . . . . . . . . . FEM1AP4 . . . fem-1 homolog a (C. elegans) pseudogene 4 . . . . . . . . . . . FEM1B 0.540948666821381 0.45591918695115 0.00313214622746941 fem-1 homolog b (C. elegans) FUNCTION: Component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit. Involved in apoptosis by acting as a death receptor-associated protein that mediates apoptosis. Also involved in glucose homeostasis in pancreatic islet. Functions as an adapter/mediator in replication stress-induced signaling that leads to the activation of CHEK1. {ECO:0000269|PubMed:10542291, ECO:0000269|PubMed:19330022}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis. Weakly expressed in other tissues. {ECO:0000269|PubMed:10542291}.; medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;placenta;hippocampus;head and neck;kidney;stomach; amygdala;medulla oblongata;occipital lobe;testis - interstitial;superior cervical ganglion;cerebellum peduncles;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;fetal brain;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.25236 0.11809 -0.381986487 27.68931352 34.24977 1.04820 FEM1C 0.624676084568469 0.373753959920523 0.00156995551100737 fem-1 homolog c (C. elegans) FUNCTION: Probable component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney, cardiac tissue, skeletal muscle and testis. Expressed at lower levels in other tissues, including cartilage. {ECO:0000269|PubMed:11733146, ECO:0000269|PubMed:14527725}.; smooth muscle;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;urinary;blood;breast;lung;placenta;hippocampus;liver;cervix;kidney;stomach;thymus; testis;cerebellum; 0.62830 0.11262 -0.626318434 17.03231894 19.14031 0.65963 FEN1 3.47774227503768e-05 0.363035259805493 0.636929962771757 flap structure-specific endonuclease 1 FUNCTION: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double- stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA. {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:10744741, ECO:0000269|PubMed:11986308, ECO:0000269|PubMed:18443037, ECO:0000269|PubMed:20729856, ECO:0000269|PubMed:7961795, ECO:0000269|PubMed:8621570}.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach; superior cervical ganglion;tumor;skeletal muscle; 0.97376 0.54258 -0.117432389 44.89266336 106.44506 2.23882 FEN1P1 . . . flap structure-specific endonuclease 1 pseudogene 1 . . . . . . . . . . . FENDRR . . . FOXF1 adjacent non-coding developmental regulatory RNA . . . . . . . . . . . FER 0.968420467139565 0.031579516007219 1.68532157760407e-08 FER tyrosine kinase FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Plays a role in synapse organization, trafficking of synaptic vesicles, the generation of excitatory postsynaptic currents and neuron-neuron synaptic transmission. Plays a role in neuronal cell death after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3, but the biological relevance of this depends on cell type and stimulus. {ECO:0000269|PubMed:12972546, ECO:0000269|PubMed:14517306, ECO:0000269|PubMed:19147545, ECO:0000269|PubMed:19339212, ECO:0000269|PubMed:19738202, ECO:0000269|PubMed:20111072, ECO:0000269|PubMed:21518868, ECO:0000269|PubMed:22223638, ECO:0000269|PubMed:7623846, ECO:0000269|PubMed:9722593}.; . TISSUE SPECIFICITY: Isoform 1 is detected in normal colon and in fibroblasts (at protein level). Isoform 3 is detected in normal testis, in colon carcinoma-derived metastases in lung, liver and ovary, and in colon carcinoma and hepato carcinoma cell lines (at protein level). Isoform 3 is not detected in normal colon or in normal fibroblasts (at protein level). Widely expressed. {ECO:0000269|PubMed:18985748, ECO:0000269|PubMed:2156206, ECO:0000269|PubMed:22223638}.; unclassifiable (Anatomical System);uterus;prostate;lung;ovary;placenta;testis;cervix;stomach; testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;atrioventricular node;skeletal muscle; 0.10446 0.14420 -0.440847477 24.59896202 528.33339 4.69026 FER1L4 . . . fer-1 like family member 4, pseudogene . . . unclassifiable (Anatomical System);medulla oblongata;ovary;placenta;colon;parathyroid;brain;bladder;stomach; . 0.06122 . . . . . FER1L5 . . . fer-1 like family member 5 FUNCTION: Plays a role in myoblast fusion; probable mediator of endocytic recycling for membrane trafficking events during myotube formation. {ECO:0000250}.; . . . . 0.16074 . . . . . FER1L6 7.9960324128331e-30 0.031650992138852 0.968349007861148 fer-1 like family member 6 . . . . . 0.41964 . -0.126979582 44.0552017 989.85095 6.06569 FER1L6-AS1 . . . FER1L6 antisense RNA 1 . . . . . 0.03957 . . . . . FER1L6-AS2 . . . FER1L6 antisense RNA 2 . . . . . . . . . . . FERD3L 0.258156359245349 0.639680503223444 0.102163137531206 Fer3-like bHLH transcription factor FUNCTION: Transcription factor that binds to the E-box and functions as inhibitor of transcription. DNA binding requires dimerization with an E protein. Inhibits transcription activation by ASCL1/MASH1 by sequestering E proteins (By similarity). {ECO:0000250}.; . . . . 0.06899 0.10459 -0.185391282 39.67916962 1899.17663 8.01366 FERMT1 7.56849863577804e-07 0.976026841773364 0.0239724013767728 fermitin family member 1 FUNCTION: Involved in cell adhesion. Contributes to integrin activation. When coexpressed with talin, potentiates activation of ITGA2B. Required for normal keratinocyte proliferation. Required for normal polarization of basal keratinocytes in skin, and for normal cell shape. Required for normal adhesion of keratinocytes to fibronectin and laminin, and for normal keratinocyte migration to wound sites. May mediate TGF-beta 1 signaling in tumor progression. {ECO:0000269|PubMed:14634021, ECO:0000269|PubMed:17012746, ECO:0000269|PubMed:19804783}.; DISEASE: Kindler syndrome (KINDS) [MIM:173650]: Autosomal recessive skin disorder characterized by skin blistering, photosensitivity, progressive poikiloderma, and extensive skin atrophy. Additional clinical features include gingival erosions, ocular, esophageal, gastrointestinal and urogenital involvement, and an increased risk of mucocutaneous malignancy. {ECO:0000269|PubMed:12668616, ECO:0000269|PubMed:12789646, ECO:0000269|PubMed:21936020}. Note=The disease is caused by mutations affecting the gene represented in this entry. Although most FERMT1 mutations are predicted to lead to premature termination of translation, and to loss of FERMT1 function, significant clinical variability is observed among patients. There is an association of FERMT1 missense and in-frame deletion mutations with milder disease phenotypes, and later onset of complications (PubMed:21936020). {ECO:0000269|PubMed:21936020}.; TISSUE SPECIFICITY: Expressed in brain, skeletal muscle, kidney, colon, adrenal gland, prostate, and placenta. Weakly or not expressed in heart, thymus, spleen, liver, small intestine, bone marrow, lung and peripheral blood leukocytes. Overexpressed in some colon and lung tumors. In skin, it is localized within the epidermis and particularly in basal keratocytes. Not detected in epidermal melanocytes and dermal fibroblasts. {ECO:0000269|PubMed:12668616, ECO:0000269|PubMed:12697302, ECO:0000269|PubMed:12789646, ECO:0000269|PubMed:14634021, ECO:0000269|PubMed:17012746}.; unclassifiable (Anatomical System);lymph node;ovary;heart;islets of Langerhans;oral cavity;colon;parathyroid;blood;skin;prostate;pancreas;lung;cerebral cortex;placenta;hippocampus;hypopharynx;liver;cervix;head and neck;kidney;brain;stomach; superior cervical ganglion;adrenal gland;trigeminal ganglion; 0.07514 0.14458 -0.418800956 25.79028073 5797.87588 15.77834 FERMT2 0.999827199539689 0.00017280031348011 1.46831086213408e-10 fermitin family member 2 FUNCTION: Scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. Binds to membranes enriched in phosphoinositides. Enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Required for the assembly of focal adhesions. Participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits FBLIM1 to focal adhesions. Plays a role in the TGFB1 and integrin signaling pathways. Stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling. {ECO:0000269|PubMed:12679033, ECO:0000269|PubMed:18458155, ECO:0000269|PubMed:21325030, ECO:0000269|PubMed:22030399, ECO:0000269|PubMed:22078565, ECO:0000269|PubMed:22699938}.; . TISSUE SPECIFICITY: Ubiquitous. Found in numerous tumor tissues.; ovary;colon;substantia nigra;parathyroid;skin;bone marrow;uterus;prostate;whole body;atrium;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;testis;dura mater;artery;brain;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;spinal cord;breast;pancreas;pia mater;lung;adrenal gland;placenta;visual apparatus;liver;cervix;head and neck;spleen;kidney;mammary gland;stomach;aorta; uterus;adipose tissue;ciliary ganglion;trigeminal ganglion; 0.86422 0.13433 -0.688817379 15.20405756 51.45434 1.41582 FERMT3 0.257005091081095 0.742944691937914 5.02169809906173e-05 fermitin family member 3 FUNCTION: Plays a central role in cell adhesion in hematopoietic cells (PubMed:19234463, PubMed:26359933). Acts by activating the integrin beta-1-3 (ITGB1, ITGB2 and ITGB3) (By similarity). Required for integrin-mediated platelet adhesion and leukocyte adhesion to endothelial cells (PubMed:19234460). Required for activation of integrin beta-2 (ITGB2) in polymorphonuclear granulocytes (PMNs) (By similarity). {ECO:0000250|UniProtKB:Q8K1B8, ECO:0000269|PubMed:19234460, ECO:0000269|PubMed:19234463, ECO:0000269|PubMed:26359933}.; DISEASE: Leukocyte adhesion deficiency 3 (LAD3) [MIM:612840]: A disorder characterized by recurrent bacterial infections without pus formation, leukocytosis and major bleeding disorders. {ECO:0000269|PubMed:18779414, ECO:0000269|PubMed:19064721, ECO:0000269|PubMed:19234460, ECO:0000269|PubMed:19234463, ECO:0000269|PubMed:19617577, ECO:0000269|PubMed:26359933}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in lymph node. Expressed in thymus, spleen and leukocytes. Weakly expressed in placenta, small intestine, stomach, testis and lung. Overexpressed in B-cell malignancies. {ECO:0000269|PubMed:12697302, ECO:0000269|PubMed:12886250}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;alveolus;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach;thymus; skeletal muscle; 0.17064 0.12600 -0.194700582 39.24274593 133.43862 2.50959 FERP1 . . . FER tyrosine kinase pseudogene 1 . . . . . . . . . . . FES 2.77390387287312e-05 0.999827901522206 0.000144359439064942 FES proto-oncogene, tyrosine kinase FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down- stream of the activated FCER1 receptor and the mast/stem cell growth factor receptor KIT. Plays a role in the regulation of mast cell degranulation. Plays a role in the regulation of cell differentiation and promotes neurite outgrowth in response to NGF signaling. Plays a role in cell scattering and cell migration in response to HGF-induced activation of EZR. Phosphorylates BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1, PECAM1, STAT3 and TRIM28. {ECO:0000269|PubMed:11509660, ECO:0000269|PubMed:15302586, ECO:0000269|PubMed:15485904, ECO:0000269|PubMed:16455651, ECO:0000269|PubMed:17595334, ECO:0000269|PubMed:18046454, ECO:0000269|PubMed:19001085, ECO:0000269|PubMed:19051325, ECO:0000269|PubMed:20111072, ECO:0000269|PubMed:2656706, ECO:0000269|PubMed:8955135}.; DISEASE: Note=Has been shown to act as proto-oncogene in some types of cancer, possibly due to abnormal activation of the kinase. Has been shown to act as tumor suppressor in other types of cancer. Expressed and present as activated kinase in a subset of acute myeloid leukemia patients; promotes survival of leukemia cells (PubMed:20111072). Expression is absent in K562 leukemia cells; ectopic expression of FSP/FES restores myeloid differentiation (PubMed:2656706). May function as tumor suppressor in colorectal cancer; expression is reduced or absent in samples from some colon cancer patients (PubMed:16455651). Ectopic expression of FSP/FES suppresses anchorage-independent growth in colon cancer cell lines (PubMed:16455651). Up-regulated in prostate cancer, and might be a predictor of recurrence after radical surgery (PubMed:21563194). May promote growth of renal carcinoma cells (PubMed:19082481). {ECO:0000269|PubMed:16455651, ECO:0000269|PubMed:19082481, ECO:0000269|PubMed:20111072, ECO:0000269|PubMed:21563194, ECO:0000269|PubMed:2656706}.; TISSUE SPECIFICITY: Widely expressed. Detected in adult colon epithelium. {ECO:0000269|PubMed:16455651, ECO:0000269|PubMed:19051325}.; colon;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;endometrium;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;spleen;kidney;mammary gland;stomach; . 0.33656 0.39964 -0.92407637 9.766454352 107.00427 2.24477 FETUB 6.8836490746529e-05 0.732564853124392 0.267366310384862 fetuin B FUNCTION: Protease inhibitor required for egg fertilization. Required to prevent premature zona pellucida hardening before fertilization, probably by inhibiting the protease activity of ASTL, a protease that mediates the cleavage of ZP2 and triggers zona pellucida hardening (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Liver and testis.; unclassifiable (Anatomical System);liver;testis;spleen;brain; superior cervical ganglion;fetal liver;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.02716 . 0.621009802 83.41589998 583.45117 4.89852 FEV . . . FEV, ETS transcription factor FUNCTION: Functions as a transcriptional regulator. According to PubMed:12761502, it functions as a transcriptional repressor. Functions in the differentiation and the maintenance of the central serotonergic neurons. May play a role in cell growth. {ECO:0000269|PubMed:12761502}.; DISEASE: Note=A chromosomal aberration involving FEV is found in Ewing tumors. Translocation t(2;21;22)(q23;q22;q12) that forms a EWSR1-FEV fusion protein with a potential oncogenic activity. {ECO:0000269|PubMed:9121764}.; TISSUE SPECIFICITY: In brain, exclusively expressed in the major serotonergic neurons of the dorsal and median raphe nuclei located in the midbrain and pons. Also detected in prostate and small intestine. {ECO:0000269|PubMed:15003288, ECO:0000269|PubMed:15986391, ECO:0000269|PubMed:9121764}.; unclassifiable (Anatomical System);prostate;islets of Langerhans; dorsal root ganglion;prostate;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.19482 0.19231 . . 6.8667 0.25493 FEZ1 0.540112166448388 0.459241318364625 0.000646515186986555 fasciculation and elongation protein zeta 1 FUNCTION: May be involved in axonal outgrowth as component of the network of molecules that regulate cellular morphology and axon guidance machinery. Able to restore partial locomotion and axonal fasciculation to C.elegans unc-76 mutants in germline transformation experiments. May participate in the transport of mitochondria and other cargos along microtubules. {ECO:0000269|PubMed:20812761, ECO:0000269|PubMed:22354037}.; . TISSUE SPECIFICITY: Mainly expressed in brain.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;gum;testis;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;hypothalamus;pineal body;spinal cord;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;cerebellum;thymus; whole brain;amygdala;dorsal root ganglion;superior cervical ganglion;thalamus;occipital lobe;medulla oblongata;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.55708 0.13366 -0.005381972 53.50908233 1017.81531 6.13809 FEZ2 3.59160198779228e-05 0.59313048799359 0.406833595986532 fasciculation and elongation protein zeta 2 FUNCTION: Involved in axonal outgrowth and fasciculation. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in nonneural tissues, such as heart, lung, spleen, muscle, testis, placenta and melanocytes.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;brain;gall bladder;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);small intestine;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach; whole brain;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;olfactory bulb;spinal cord;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.07682 0.09729 -0.071520315 48.34866714 97.78971 2.13848 FEZF1 0.298172189886215 0.697626836403747 0.00420097371003876 FEZ family zinc finger 1 FUNCTION: Transcription repressor. Involved in the axonal projection and proper termination of olfactory sensory neurons (OSN). Plays a role in rostro-caudal patterning of the diencephalon and in prethalamic formation. Expression is required in OSN to cell-autonomously regulate OSN axon projections. Regulates non-cell-autonomously the layer formation of the olfactory bulb development and the interneurons. May be required for correct rostral migration of the interneuron progenitors (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain. Little or no expression in other tissues. Overexpressed specifically in gastric cancers. A 2- to 20-fold increase is found in over 50% of gastric cancer tissues. {ECO:0000269|PubMed:19318583}.; unclassifiable (Anatomical System);stomach; . 0.35376 0.09478 -0.007201372 53.19061099 35.86211 1.07741 FEZF1-AS1 . . . FEZF1 antisense RNA 1 . . . . . . . . . . . FEZF2 0.902033503582519 0.0971174527939089 0.000849043623571907 FEZ family zinc finger 2 FUNCTION: Transcription repressor. Required for the specification of corticospinal motor neurons and other subcerebral projection neurons. May play a role in layer and neuronal subtype-specific patterning of subcortical projections and axonal fasciculation. Controls the development of dendritic arborization and spines of large layer V pyramidal neurons. May be involved in innate immunity (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);optic nerve;hypothalamus;macula lutea;visual apparatus;head and neck;fovea centralis;choroid;lens;brain;retina; amygdala;superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.53205 0.14896 -0.185391282 39.67916962 12.16514 0.44039 FFAR1 0.00137025456396348 0.424069059892158 0.574560685543879 free fatty acid receptor 1 FUNCTION: G-protein coupled receptor for medium and long chain saturated and unsaturated fatty acids that plays an important role in glucose homeostasis. Fatty acid binding increases glucose- stimulated insulin secretion, and may also enhance the secretion of glucagon-like peptide 1 (GLP-1). May also play a role in bone homeostasis; receptor signaling activates pathways that inhibit osteoclast differentiation (By similarity). Ligand binding leads to a conformation change that triggers signaling via G-proteins that activate phospholipase C, leading to an increase of the intracellular calcium concentration. Seems to act through a G(q) and G(i)-mediated pathway. {ECO:0000250|UniProtKB:Q76JU9, ECO:0000269|PubMed:12496284, ECO:0000269|PubMed:17699519, ECO:0000269|PubMed:24130766}.; . TISSUE SPECIFICITY: Detected in brain and pancreas. Detected in pancreatic beta cells. {ECO:0000269|PubMed:12496284, ECO:0000269|PubMed:16289108}.; unclassifiable (Anatomical System);islets of Langerhans; . 0.14218 0.12937 0.238945317 69.20853975 61.22306 1.59289 FFAR2 0.000643946787473112 0.495939903941847 0.503416149270679 free fatty acid receptor 2 FUNCTION: G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins but also to the Gq family (PubMed:12496283, PubMed:12711604, PubMed:23589301). Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation. May play a role in glucose homeostasis by regulating the secretion of GLP-1, in response to short-chain fatty acids accumulating in the intestine. May also regulate the production of LEP/Leptin, a hormone acting on the central nervous system to inhibit food intake. Finally, may also regulate whole-body energy homeostasis through adipogenesis regulating both differentiation and lipid storage of adipocytes. In parallel to its role in energy homeostasis, may also mediate the activation of the inflammatory and immune responses by SCFA in the intestine, regulating the rapid production of chemokines and cytokines. May also play a role in the resolution of the inflammatory response and control chemotaxis in neutrophils. In addition to SCFAs, may also be activated by the extracellular lectin FCN1 in a process leading to activation of monocytes and inducing the secretion of interleukin- 8/IL-8 in response to the presence of microbes (PubMed:21037097). Among SCFAs, the fatty acids containing less than 6 carbons, the most potent activators are probably acetate, propionate and butyrate (PubMed:12496283, PubMed:12711604). Exhibits a SCFA- independent constitutive G protein-coupled receptor activity (PubMed:23066016). {ECO:0000269|PubMed:12496283, ECO:0000269|PubMed:12684041, ECO:0000269|PubMed:12711604, ECO:0000269|PubMed:18801738, ECO:0000269|PubMed:21037097, ECO:0000269|PubMed:23066016, ECO:0000269|PubMed:23589301}.; . TISSUE SPECIFICITY: Expressed at relatively high levels in peripheral blood leukocytes and, to lesser extent, in spleen. {ECO:0000269|PubMed:12496283, ECO:0000269|PubMed:12684041}.; unclassifiable (Anatomical System);lung;islets of Langerhans; superior cervical ganglion;whole blood; 0.13126 0.11628 0.463046108 78.58575136 440.09435 4.37140 FFAR3 . . . free fatty acid receptor 3 FUNCTION: G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins. Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation (PubMed:12711604). Activated by SCFAs and by beta-hydroxybutyrate, a ketone body produced by the liver upon starvation, it inhibits N-type calcium channels and modulates the activity of sympathetic neurons through a signaling cascade involving the beta and gamma subunits of its coupled G protein, phospholipase C and MAP kinases. Thereby, it may regulate energy expenditure through the control of the sympathetic nervous system that controls for instance heart rate. Upon activation by SCFAs accumulating in the intestine, it may also signal to the brain via neural circuits which in turn would regulate intestinal gluconeogenesis. May also control the production of hormones involved in whole-body energy homeostasis. May for instance, regulate blood pressure through renin secretion. May also regulate secretion of the PYY peptide by enteroendocrine cells and control gut motility, intestinal transit rate, and the harvesting of energy from SCFAs produced by gut microbiota. May also indirectly regulate the production of LEP/Leptin, a hormone acting on the CNS to inhibit food intake, in response to the presence of short-chain fatty acids in the intestine. Finally, may also play a role in glucose homeostasis. Besides its role in energy homeostasis, may play a role in intestinal immunity. May mediate the activation of the inflammatory and immune response by SCFAs in the gut, regulating the rapid production of chemokines and cytokines by intestinal epithelial cells. Among SCFAs, the fatty acids containing less than 6 carbons, the most potent activators are probably propionate, butyrate and pentanoate while acetate is a poor activator (PubMed:12496283, PubMed:12711604). {ECO:0000269|PubMed:12496283, ECO:0000269|PubMed:12711604, ECO:0000269|PubMed:18801738, ECO:0000269|PubMed:23066016}.; . TISSUE SPECIFICITY: Highest level in adipose tissue, and lower expression across all tissues tested. Expressed in sympathetic ganglia. {ECO:0000269|PubMed:12496283, ECO:0000269|PubMed:21518883}.; unclassifiable (Anatomical System); . 0.10472 0.10014 0.154398214 64.73814579 44.5476 1.27746 FFAR4 0.0055724932654211 0.897975383210862 0.0964521235237165 free fatty acid receptor 4 FUNCTION: Receptor for medium and long-chain free fatty acids (FFAs). Signals via a G(q)/G(11)-coupled pathway. Acts as a receptor for omega-3 fatty acids and mediates robust anti- inflammatory effects, particularly in macrophages and fat cells. The anti-inflammatory effects involve inhibition of TAK1 through a beta-arrestin 2 (ARRB2)/TAB1-dependent effect, but independent of the G(q)/G(11)-coupled pathway. Mediates potent insulin sensitizing and antidiabetic effects by repressing macrophage- induced tissue inflammation. May mediate the taste of fatty acids. Mediates FFA-induced inhibition of apoptosis in enteroendocrine cells. May play a role in the regulation of adipocyte development and differentiation. {ECO:0000269|PubMed:15619630}.; . TISSUE SPECIFICITY: Abundant expression in the intestinal tract. Highly expressed in adipose tissue, small intestine and pancreas. {ECO:0000269|PubMed:15619630, ECO:0000269|PubMed:17250804}.; . . 0.40257 0.11747 -0.26993514 34.59542345 1561.1598 7.31897 FGA 6.34645634966279e-10 0.401936682920703 0.598063316444651 fibrinogen alpha chain FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3- dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways. {ECO:0000250|UniProtKB:E9PV24}.; DISEASE: Congenital afibrinogenemia (CAFBN) [MIM:202400]: Rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. {ECO:0000269|PubMed:25427968}. Note=The disease is caused by mutations affecting the gene represented in this entry. The majority of cases of afibrinogenemia are due to truncating mutations. Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias.; DISEASE: Amyloidosis 8 (AMYL8) [MIM:105200]: A hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash. {ECO:0000269|PubMed:8097946}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dysfibrinogenemia, congenital (DYSFIBRIN) [MIM:616004]: A disorder characterized by qualitative abnormalities (dysfibrinogenemia) of the circulating fibrinogen. Affected individuals are frequently asymptomatic, but some patients have bleeding diathesis, thromboembolic complications, or both. In some cases, dysfibrinogenemia is associated with low circulating fibrinogen levels (hypodysfibrinogenemia). {ECO:0000269|PubMed:16846481, ECO:0000269|PubMed:8473507}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in blood plasma (at protein level). {ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.; unclassifiable (Anatomical System);lymphoreticular;cartilage;heart;colon;skin;uterus;pancreas;lung;liver;testis;spleen;kidney;stomach;gall bladder; fetal liver;superior cervical ganglion;liver;fetal lung;trigeminal ganglion;skeletal muscle; 0.22383 0.41722 -0.751322189 13.71196037 387.58071 4.14645 FGB 0.19539017557497 0.802416765598764 0.00219305882626594 fibrinogen beta chain FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways. {ECO:0000250|UniProtKB:E9PV24}.; DISEASE: Congenital afibrinogenemia (CAFBN) [MIM:202400]: Rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. {ECO:0000269|PubMed:10666208, ECO:0000269|PubMed:11468164, ECO:0000269|PubMed:25427968}. Note=The disease is caused by mutations affecting the gene represented in this entry. Patients with congenital fibrinogen abnormalities can manifest different clinical pictures. Some cases are clinically silent, some show a tendency toward bleeding and some show a predisposition for thrombosis with or without bleeding.; DISEASE: Dysfibrinogenemia, congenital (DYSFIBRIN) [MIM:616004]: A disorder characterized by qualitative abnormalities (dysfibrinogenemia) of the circulating fibrinogen. Affected individuals are frequently asymptomatic, but some patients have bleeding diathesis, thromboembolic complications, or both. In some cases, dysfibrinogenemia is associated with low circulating fibrinogen levels (hypodysfibrinogenemia). {ECO:0000269|PubMed:1634610}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in blood plasma (at protein level). {ECO:0000269|PubMed:10074346, ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.; unclassifiable (Anatomical System);pancreas;lung;bone;visual apparatus;liver;spleen;brain;skeletal muscle;gall bladder; dorsal root ganglion;fetal liver;superior cervical ganglion;liver;fetal lung;trigeminal ganglion; 0.72928 0.41068 0.308721233 72.59966973 122.60149 2.41177 FGD1 0.972835312099674 0.0271632876264429 1.40027388339493e-06 FYVE, RhoGEF and PH domain containing 1 FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape. {ECO:0000269|PubMed:8969170}.; DISEASE: Aarskog-Scott syndrome (AAS) [MIM:305400]: A rare multisystemic disorder characterized by disproportionately short stature, and by facial, skeletal and urogenital anomalies. Some patients manifest mental retardation, attention deficit disorder and hyperactivity. {ECO:0000269|PubMed:10930571, ECO:0000269|PubMed:11093277, ECO:0000269|PubMed:14560308}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in FGD1 are found in a patient with non- syndromal X-linked mental retardation. {ECO:0000269|PubMed:11940089}.; TISSUE SPECIFICITY: Expressed in fetal heart, brain, lung, kidney and placenta. Less expressed in liver; adult heart, brain, lung, pancreas and skeletal muscle.; . . 0.32307 0.28713 -0.512444034 21.55579146 122.42363 2.40983 FGD2 4.70751448593272e-05 0.991954624671129 0.00799830018401189 FYVE, RhoGEF and PH domain containing 2 FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Activates JNK1 via CDC42 but not RAC1. Binds to phosphatidylinositol 4,5- bisphosphate, phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4- monophosphate and phosphatidylinositol 3-monophosphate (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;larynx;placenta;spleen;blood;head and neck;germinal center;brain;tonsil;retina; dorsal root ganglion;superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.10967 0.10287 0.450099045 78.01958009 140.18637 2.58343 FGD3 8.70335327222514e-06 0.98215912976505 0.0178321668816778 FYVE, RhoGEF and PH domain containing 3 FUNCTION: Promotes the formation of filopodia. May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape (By similarity). {ECO:0000250}.; . . lymphoreticular;colon;choroid;fovea centralis;bone marrow;retina;uterus;prostate;optic nerve;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;blood;lens;lung;placenta;macula lutea;spleen;kidney;mammary gland;stomach; lymph node;white blood cells;whole blood;thymus;bone marrow; 0.15586 0.14877 -1.083859071 7.195093182 82.61084 1.93131 FGD4 0.335778541836355 0.664216189138809 5.26902483585315e-06 FYVE, RhoGEF and PH domain containing 4 FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape. Activates MAPK8 (By similarity). {ECO:0000250, ECO:0000269|PubMed:15133042}.; DISEASE: Charcot-Marie-Tooth disease 4H (CMT4H) [MIM:609311]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot- Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie-Tooth disease are designated CMT4. {ECO:0000269|PubMed:17564959, ECO:0000269|PubMed:17564972}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in different tissues, including brain, cerebellum, peripheral nerve, skeletal muscle, heart, uterus, placenta and testis. {ECO:0000269|PubMed:17564959}.; unclassifiable (Anatomical System);heart;ovary;colon;skin;uterus;breast;pancreas;prostate;lung;frontal lobe;visual apparatus;liver;testis;brain;pineal gland;stomach; . 0.11096 0.12967 -0.156065314 42.16206653 4418.91881 13.30854 FGD5 0.994386979064628 0.00561301974217773 1.19319433641995e-09 FYVE, RhoGEF and PH domain containing 5 FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Mediates VEGF-induced CDC42 activation. May regulate proangiogenic action of VEGF in vascular endothelial cells, including network formation, directional movement and proliferation. May play a role in regulating the actin cytoskeleton and cell shape. {ECO:0000269|PubMed:22328776}.; . TISSUE SPECIFICITY: Expressed in endothelial cells (at protein level). {ECO:0000269|PubMed:22328776}.; unclassifiable (Anatomical System);cartilage;heart;ovary;adrenal medulla;choroid;skin;skeletal muscle;uterus;breast;lung;iris;alveolus;duodenum;liver;testis;spleen;kidney;brain;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.18319 . 1.01772518 90.87048832 1520.71867 7.24887 FGD5-AS1 . . . FGD5 antisense RNA 1 . . . . . . . . . . . FGD5P1 . . . FYVE, RhoGEF and PH domain containing 5 pseudogene 1 . . . . . . . . . . . FGD6 0.995227689206774 0.00477231076036185 3.2863907116088e-11 FYVE, RhoGEF and PH domain containing 6 FUNCTION: May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. May play a role in regulating the actin cytoskeleton and cell shape (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;frontal lobe;heart;kidney;germinal center;skeletal muscle; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.18424 0.09130 -1.076610636 7.324840764 1000.15705 6.09179 FGF1 0.320471735942387 0.612223006879397 0.0673052571782161 fibroblast growth factor 1 FUNCTION: Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. {ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:20145243, ECO:0000269|PubMed:8663044}.; . TISSUE SPECIFICITY: Predominantly expressed in kidney and brain. Detected at much lower levels in heart and skeletal muscle. {ECO:0000269|PubMed:11964394, ECO:0000269|PubMed:7504343}.; amygdala;unclassifiable (Anatomical System);heart;cartilage;ovary;hypothalamus;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;frontal lobe;placenta;thyroid;macula lutea;hippocampus;liver;kidney;brain;peripheral nerve; dorsal root ganglion;amygdala;whole brain;occipital lobe;medulla oblongata;thalamus;superior cervical ganglion;olfactory bulb;hypothalamus;temporal lobe;spinal cord;caudate nucleus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.90797 0.95238 0.014844891 54.94810097 20.31977 0.69363 FGF2 . . . fibroblast growth factor 2 FUNCTION: Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. {ECO:0000269|PubMed:1721615, ECO:0000269|PubMed:8663044}.; . TISSUE SPECIFICITY: Expressed in granulosa and cumulus cells. Expressed in hepatocellular carcinoma cells, but not in non- cancerous liver tissue. {ECO:0000269|PubMed:1417798, ECO:0000269|PubMed:1721615}.; ovary;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;thyroid;bone;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;skeletal muscle;breast;pia mater;lung;trabecular meshwork;placenta;visual apparatus;liver;kidney;mammary gland;stomach; smooth muscle;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.96797 0.89410 . . 48.49255 1.35837 FGF3 0.0330372169885067 0.820236048316638 0.146726734694855 fibroblast growth factor 3 FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Required for normal ear development. {ECO:0000269|PubMed:8663044}.; DISEASE: Deafness with labyrinthine aplasia, microtia and microdontia (LAMM) [MIM:610706]: Unique autosomal recessive syndrome characterized by type I microtia, microdontia, and profound congenital deafness associated with a complete absence of inner ear structures (Michel aplasia). {ECO:0000269|PubMed:17236138, ECO:0000269|PubMed:18435799}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . brain; skeletal muscle; 0.81859 0.41514 . . 47.44932 1.33686 FGF4 0.750215677974647 0.23978497316598 0.00999934885937313 fibroblast growth factor 4 FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Required for normal limb and cardiac valve development during embryogenesis. {ECO:0000269|PubMed:8663044}.; . . unclassifiable (Anatomical System);lung;testis; . 0.38823 0.60875 . . 7.05213 0.26412 FGF5 4.31893230685642e-05 0.401942731133061 0.598014079543871 fibroblast growth factor 5 FUNCTION: Plays an important role in the regulation of cell proliferation and cell differentiation. Required for normal regulation of the hair growth cycle. Functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen the apoptosis-induced regression phase (By similarity). {ECO:0000250|UniProtKB:Q20FD0, ECO:0000269|PubMed:8663044}.; DISEASE: Trichomegaly (TCMGLY) [MIM:190330]: A morphologic trait characterized by unusually long eyelashes and mild hypertrichosis of eyebrows. It can be observed in association with corneal irritation, cataracts, and hereditary spherocytosis. {ECO:0000269|PubMed:24989505}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in neonatal brain.; unclassifiable (Anatomical System);lung;whole body;cartilage;bone;blood;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;medulla oblongata;uterus corpus;globus pallidus;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.94136 0.22107 -0.025608647 51.91672564 265.4958 3.49565 FGF6 0.000705757813368273 0.515149768506955 0.484144473679677 fibroblast growth factor 6 FUNCTION: Plays an important role in the regulation of cell proliferation, cell differentiation, angiogenesis and myogenesis, and is required for normal muscle regeneration. {ECO:0000269|PubMed:8663044}.; . TISSUE SPECIFICITY: Leukemia cell lines with platelet/ megakaryocytic differentiation potential.; . . 0.69677 0.19827 0.218717575 68.27081859 939.23735 5.94008 FGF7 0.874992687904998 0.123417205011628 0.00159010708337395 fibroblast growth factor 7 FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. Required for normal branching morphogenesis. Growth factor active on keratinocytes. Possible major paracrine effector of normal epithelial cell proliferation. {ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:8663044}.; . TISSUE SPECIFICITY: Epithelial cell.; unclassifiable (Anatomical System);smooth muscle;cartilage;heart;islets of Langerhans;choroid;skeletal muscle;bone marrow;lung;cochlea;mesenchyma;nasopharynx;trabecular meshwork;bone;placenta;cervix;kidney;artery;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin; 0.98066 0.58572 0.057118534 57.99716914 0.89584 0.01869 FGF7P1 . . . fibroblast growth factor 7 pseudogene 1 . . . . . . . . . . . FGF7P2 . . . fibroblast growth factor 7 pseudogene 2 . . . . . . 0.58572 . . . . FGF8 0.927194848734189 0.0724059880481627 0.000399163217648434 fibroblast growth factor 8 FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. Required for normal brain, eye, ear and limb development during embryogenesis. Required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system (PubMed:16384934, PubMed:16597617, PubMed:8663044). Plays a role in neurite outgrowth in hippocampal cells (PubMed:21576111). {ECO:0000269|PubMed:16384934, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:21576111, ECO:0000269|PubMed:8663044}.; DISEASE: Hypogonadotropic hypogonadism 6 with or without anosmia (HH6) [MIM:612702]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:18596921, ECO:0000269|PubMed:23643382}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. The genetics of hypogonadotropic hypogonadism involves various modes of transmission. Oligogenic inheritance has been reported in some patients carrying mutations in FGF8 as well as in other HH- associated genes including FGFR1 (PubMed:23643382). {ECO:0000269|PubMed:23643382}.; . duodenum; temporal lobe;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.53552 0.58572 -0.317668748 31.45789101 10.22234 0.37284 FGF9 0.910715910113492 0.0886141668494015 0.00066992303710623 fibroblast growth factor 9 FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. May have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors. {ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:8663044}.; DISEASE: Multiple synostoses syndrome 3 (SYNS3) [MIM:612961]: A bone disease characterized by multiple progressive joint fusions that commonly involve proximal interphalangeal, tarsal-carpal, humeroradial and cervical spine joints. Additional features can include progressive conductive deafness and facial dysmorphism. {ECO:0000269|PubMed:19589401}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Glial cells.; . . 0.90259 0.31502 0.169169615 65.33380514 24.43081 0.80364 FGF10 0.858814551551722 0.13900335504837 0.00218209339990832 fibroblast growth factor 10 FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. Required for normal branching morphogenesis. May play a role in wound healing. {ECO:0000269|PubMed:16597617}.; DISEASE: Aplasia of lacrimal and salivary glands (ALSG) [MIM:180920]: A rare condition characterized by dry conjunctival mucosae, irritable eyes, epiphora (constant tearing), and xerostomia (dryness of the mouth), which increases risk of dental erosion, dental caries, periodontal disease, and oral infections. ALSG has variable expressivity, and affected individuals may have aplasia or hypoplasia of the lacrimal, parotid, submandibular, and sublingual glands and absence of the lacrimal puncta. {ECO:0000269|PubMed:15654336}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Lacrimo-auriculo-dento-digital syndrome (LADDS) [MIM:149730]: An autosomal dominant ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Lacrimo-auriculo-dento-digital syndrome is characterized by aplastic/hypoplastic lacrimal and salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia and enamel hypoplasia, and distal limb segments anomalies. In addition to these cardinal features, facial dysmorphism, malformations of the kidney and respiratory system and abnormal genitalia have been reported. Craniosynostosis and severe syndactyly are not observed. {ECO:0000269|PubMed:16501574, ECO:0000269|PubMed:16630169}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . duodenum;skeletal muscle; . 0.60971 0.45158 0.413500896 76.67492333 17.92009 0.62667 FGF10-AS1 . . . FGF10 antisense RNA 1 . . . . . . . . . . . FGF11 0.0681958357641297 0.871694573861473 0.0601095903743977 fibroblast growth factor 11 FUNCTION: Probably involved in nervous system development and function.; . . unclassifiable (Anatomical System);heart;ovary;spinal cord;adrenal cortex;colon;parathyroid;fovea centralis;lens;skin;retina;uterus;whole body;lung;cerebral cortex;bone;placenta;thyroid;macula lutea;visual apparatus;kidney;brain;bladder;mammary gland;stomach; . 0.21502 0.13667 -0.383807564 27.41802312 28.02661 0.89982 FGF12 0.114210585344935 0.858191468747534 0.0275979459075307 fibroblast growth factor 12 FUNCTION: Probably involved in nervous system development and function.; . TISSUE SPECIFICITY: Brain, eye and testis; highly expressed in embryonic retina, olfactory epithelium, olfactory bulb, and in a segmental pattern of the body wall; in adult olfactory bulb, less in cerebellum, deep cerebellar nuclei, cortex and multiple midbrain structures.; unclassifiable (Anatomical System);ovary;islets of Langerhans;hypothalamus;fovea centralis;retina;whole body;atrium;lung;ganglion;macula lutea;hippocampus;pituitary gland;testis;kidney;brain; amygdala;subthalamic nucleus;superior cervical ganglion;occipital lobe;globus pallidus;trigeminal ganglion;parietal lobe;cerebellum; 0.90811 0.17448 -0.163345027 41.24793583 12.24987 0.44383 FGF12-AS1 . . . FGF12 antisense RNA 1 . . . . . . . . . . . FGF12-AS2 . . . FGF12 antisense RNA 2 . . . . . . . . . . . FGF12-AS3 . . . FGF12 antisense RNA 3 . . . . . . . . . . . FGF13 0.964223639772387 0.0357089171166589 6.74431109536615e-05 fibroblast growth factor 13 FUNCTION: Microtubule-binding protein which directly binds tubulin and is involved in both polymerization and stabilization of microtubules. Through its action on microtubules, may participate to the refinement of axons by negatively regulating axonal and leading processes branching. Plays a crucial role in neuron polarization and migration in the cerebral cortex and the hippocampus. {ECO:0000269|PubMed:15282281}.; FUNCTION: May also play a role in MAPK signaling. {ECO:0000269|PubMed:15282281}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Predominantly expressed in the nervous system. {ECO:0000269|PubMed:9232594}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;hypothalamus;salivary gland;colon;substantia nigra;parathyroid;skin;skeletal muscle;uterus;prostate;whole body;lung;bone;placenta;visual apparatus;hippocampus;alveolus;liver;head and neck;kidney;brain; dorsal root ganglion;whole brain;amygdala;occipital lobe;fetal brain;ciliary ganglion;caudate nucleus; 0.89726 0.10286 -0.207437529 38.2814343 1.05559 0.02673 FGF13-AS1 . . . FGF13 antisense RNA 1 . . . . . . . . . . . FGF14 0.724525962590089 0.2725676738245 0.00290636358541117 fibroblast growth factor 14 FUNCTION: Probably involved in nervous system development and function.; . TISSUE SPECIFICITY: Nervous system.; . . 0.79785 0.17050 -0.005381972 53.50908233 23.4147 0.78046 FGF14-AS1 . . . FGF14 antisense RNA 1 . . . . . . . . . . . FGF14-AS2 . . . FGF14 antisense RNA 2 . . . . . . . . . . . FGF14-IT1 . . . FGF14 intronic transcript 1 . . . . . . . . . . . FGF16 . . . fibroblast growth factor 16 FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation, and is required for normal cardiomyocyte proliferation and heart development. {ECO:0000269|PubMed:16597617}.; DISEASE: Metacarpal 4-5 fusion (MF4) [MIM:309630]: A rare congenital malformation of the hand characterized by the partial or complete fusion of the fourth and fifth metacarpals. The anomaly occurs as an isolated trait or part of a syndrome. {ECO:0000269|PubMed:23709756, ECO:0000269|PubMed:25333065}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.91430 0.13588 . . . . FGF17 0.865331559549294 0.132739230821453 0.00192920962925221 fibroblast growth factor 17 FUNCTION: Plays an important role in the regulation of embryonic development and as signaling molecule in the induction and patterning of the embryonic brain. Required for normal brain development. {ECO:0000269|PubMed:16597617}.; DISEASE: Hypogonadotropic hypogonadism 20 with or without anosmia (HH20) [MIM:615270]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:23643382}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. Some patients carrying mutations in FGF17 also have a mutation in another HH-associated gene including FGFR1, HS6ST1 and FLRT3 (PubMed:23643382). {ECO:0000269|PubMed:23643382}.; TISSUE SPECIFICITY: Preferentially expressed in the embryonic brain.; unclassifiable (Anatomical System);optic nerve;macula lutea;fovea centralis;choroid;lens;retina; superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.97990 0.11262 -0.229483771 36.86010852 5.5877 0.20855 FGF18 0.175827312241956 0.768136897525061 0.0560357902329829 fibroblast growth factor 18 FUNCTION: Plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. Required for normal ossification and bone development. Stimulates hepatic and intestinal proliferation. {ECO:0000269|PubMed:16597617}.; . . unclassifiable (Anatomical System);uterus;lung;ovary;heart;placenta;colon;parathyroid;skin; dorsal root ganglion;superior cervical ganglion;uterus corpus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.55384 0.26913 -0.317668748 31.45789101 7.53265 0.27949 FGF19 0.294076907366963 0.625646243256635 0.0802768493764021 fibroblast growth factor 19 FUNCTION: Involved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression, following positive regulation of the JNK and ERK1/2 cascades. Stimulates glucose uptake in adipocytes. Activity requires the presence of KLB and FGFR4. {ECO:0000269|PubMed:12815072, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:19085950}.; . TISSUE SPECIFICITY: Expressed in fetal brain, cartilage, retina, and adult gall bladder. {ECO:0000269|PubMed:10525310}.; unclassifiable (Anatomical System);breast;uterus;whole body;colon;parathyroid;brain; dorsal root ganglion;ciliary ganglion;cerebellum; 0.32840 0.15837 . . 13.85831 0.50276 FGF20 0.702854984376326 0.280987374702364 0.01615764092131 fibroblast growth factor 20 FUNCTION: Neurotrophic factor that regulates central nervous development and function. {ECO:0000269|PubMed:16597617}.; . TISSUE SPECIFICITY: Predominantly expressed in the cerebellum. {ECO:0000269|PubMed:11306498}.; uterus;optic nerve;lung;heart;macula lutea;colon;fovea centralis;choroid;lens;skin;retina; uterus corpus;skeletal muscle; 0.72897 0.23041 . . 355.28801 3.98673 FGF21 0.213002020207769 0.747218697899747 0.0397792818924841 fibroblast growth factor 21 FUNCTION: Stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression (but not SLC2A4/GLUT4 expression). Activity requires the presence of KLB. {ECO:0000269|PubMed:15902306, ECO:0000269|PubMed:17623664}.; . . unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;atrioventricular node;skeletal muscle; 0.07904 0.13530 -0.336073593 30.55555556 17.09083 0.60135 FGF22 0.000103153895712467 0.203418421009917 0.79647842509437 fibroblast growth factor 22 FUNCTION: Plays a role in the fasting response, glucose homeostasis, lipolysis and lipogenesis. Can stimulate cell proliferation (in vitro). May be involved in hair development. {ECO:0000269|PubMed:16597617}.; . . ovary;hippocampus; . 0.35325 0.12614 . . 180.74457 2.92194 FGF23 0.0279896645640281 0.797935042919904 0.174075292516068 fibroblast growth factor 23 FUNCTION: Regulator of phosphate homeostasis. Inhibits renal tubular phosphate transport by reducing SLC34A1 levels. Upregulates EGR1 expression in the presence of KL (By similarity). Acts directly on the parathyroid to decrease PTH secretion (By similarity). Regulator of vitamin-D metabolism. Negatively regulates osteoblast differentiation and matrix mineralization. {ECO:0000250, ECO:0000269|PubMed:11062477, ECO:0000269|PubMed:11409890, ECO:0000269|PubMed:15040831, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:18282132}.; DISEASE: Hypophosphatemic rickets, autosomal dominant (ADHR) [MIM:193100]: A disease characterized by isolated renal phosphate wasting, hypophosphatemia, and inappropriately normal 1,25- dihydroxyvitamin D3 (calcitriol) levels. Patients frequently present with bone pain, rickets, and tooth abscesses. {ECO:0000269|PubMed:11062477}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Tumoral calcinosis, hyperphosphatemic, familial (HFTC) [MIM:211900]: A severe metabolic disorder that manifests with hyperphosphatemia and massive calcium deposits in the skin and subcutaneous tissues. Some patients manifest recurrent, transient, painful swellings of the long bones associated with the radiographic findings of periosteal reaction and cortical hyperostosis and absence of skin involvement. {ECO:0000269|PubMed:15590700, ECO:0000269|PubMed:16030159, ECO:0000269|PubMed:16151858, ECO:0000269|PubMed:24680727}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in osteogenic cells particularly during phases of active bone remodeling. In adult trabecular bone, expressed in osteocytes and flattened bone-lining cells (inactive osteoblasts). {ECO:0000269|PubMed:12952917}.; . . 0.49415 0.34710 0.082802743 60.09082331 23.20742 0.77515 FGFBP1 0.00103703132793641 0.37277546497605 0.626187503696014 fibroblast growth factor binding protein 1 FUNCTION: Acts as a carrier protein that release fibroblast- binding factors (FGFs) from the extracellular matrix (EM) storage and thus enhance the mitogenic activity of FGFs. Enhances FGF2 signaling during tissue repair, angiogenesis and in tumor growth. {ECO:0000269|PubMed:11509569, ECO:0000269|PubMed:15806171, ECO:0000269|PubMed:1885605, ECO:0000269|PubMed:9334727}.; . TISSUE SPECIFICITY: Expressed in the suprabasal region of the epidermis, in hair follicles, the basement membrane at the dermo- epidermal junction (occasionally extending into the basement membrane of dermal blood vessels), wounded skin and several invasive squamous cell carcinomas (at protein level). Expressed in normal and wounded skin and various squamous cell carcinomas. {ECO:0000269|PubMed:11148217, ECO:0000269|PubMed:15806171, ECO:0000269|PubMed:1885605}.; unclassifiable (Anatomical System);lymph node;ovary;heart;tongue;colon;parathyroid;skin;bone marrow;uterus;bile duct;prostate;pancreas;lung;endometrium;adrenal gland;gum;placenta;visual apparatus;hypopharynx;head and neck;brain;stomach; superior cervical ganglion;lung;trachea;tongue;ciliary ganglion;trigeminal ganglion; 0.06841 0.10927 0.551232944 81.48148148 123.07908 2.41641 FGFBP2 1.14165900472648e-07 0.0544579374833951 0.945541948350704 fibroblast growth factor binding protein 2 . . TISSUE SPECIFICITY: Expressed in serum, peripheral leukocytes and cytotoxic T-lymphocytes, but not in granulocytes and monocytes (at protein level). {ECO:0000269|PubMed:11342666}.; unclassifiable (Anatomical System);pancreas;lung;whole body;cartilage;bone;adrenal cortex;testis;spleen;kidney;retina;bone marrow; . 0.11298 . 0.595326758 82.66100495 1450.01478 7.10513 FGFBP3 0.00171216825220463 0.46793805359812 0.530349778149675 fibroblast growth factor binding protein 3 FUNCTION: Heparin-binding protein which binds to FGF2, prevents binding of FGF2 to heparin and probably inhibits immobilization of FGF2 on extracellular matrix glycosaminoglycans, allowing its release and subsequent activation of FGFR signaling which leads to increased vascular permeability. {ECO:0000269|PubMed:18669637}.; . . unclassifiable (Anatomical System);heart;colon;skin;uterus;breast;pancreas;lung;frontal lobe;bone;liver;testis;spleen;kidney;spinal ganglion;brain;mammary gland; dorsal root ganglion;ciliary ganglion;trigeminal ganglion;parietal lobe;skeletal muscle; 0.11953 0.09295 . . 849.06742 5.69514 FGFR1 0.988744284614171 0.0112557088348007 6.551028094229e-09 fibroblast growth factor receptor 1 FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation. {ECO:0000250|UniProtKB:P16092, ECO:0000269|PubMed:10830168, ECO:0000269|PubMed:11353842, ECO:0000269|PubMed:12181353, ECO:0000269|PubMed:1379697, ECO:0000269|PubMed:1379698, ECO:0000269|PubMed:15117958, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17311277, ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:18480409, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19261810, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:20133753, ECO:0000269|PubMed:20139426, ECO:0000269|PubMed:21765395, ECO:0000269|PubMed:8622701, ECO:0000269|PubMed:8663044}.; DISEASE: Pfeiffer syndrome (PS) [MIM:101600]: A syndrome characterized by the association of craniosynostosis, broad and deviated thumbs and big toes, and partial syndactyly of the fingers and toes. Three subtypes are known: mild autosomal dominant form (type 1); cloverleaf skull, elbow ankylosis, early death, sporadic (type 2); craniosynostosis, early demise, sporadic (type 3). {ECO:0000269|PubMed:7874169}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hypogonadotropic hypogonadism 2 with or without anosmia (HH2) [MIM:147950]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:12627230, ECO:0000269|PubMed:15001591, ECO:0000269|PubMed:15605412, ECO:0000269|PubMed:15845591, ECO:0000269|PubMed:16606836, ECO:0000269|PubMed:16757108, ECO:0000269|PubMed:16764984, ECO:0000269|PubMed:16882753, ECO:0000269|PubMed:17154279, ECO:0000269|PubMed:19820032, ECO:0000269|PubMed:21700882, ECO:0000269|PubMed:22927827, ECO:0000269|PubMed:23643382, ECO:0000269|PubMed:25077900, ECO:0000269|PubMed:26277103}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. Some patients carrying mutations in FGFR1 also have a mutation other HH-associated genes including DUSP6, FGF8, FGF17, FLRT3, GNRH1, GNRHR, HS6ST1, IL17RD, ANOS1, KISS1R, NSMF, PROKR2, SPRY4 and TACR3 (PubMed:23643382). {ECO:0000269|PubMed:23643382}.; DISEASE: Osteoglophonic dysplasia (OGD) [MIM:166250]: Characterized by craniosynostosis, prominent supraorbital ridge, and depressed nasal bridge, as well as by rhizomelic dwarfism and nonossifying bone lesions. Inheritance is autosomal dominant. {ECO:0000269|PubMed:15625620, ECO:0000269|PubMed:16470795}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hartsfield syndrome (HRTFDS) [MIM:615465]: A syndrome characterized by the triad of holoprosencephaly, ectrodactyly, and cleft/lip palate. Profound mental retardation is also present. Multiple other congenital anomalies usually occur. {ECO:0000269|PubMed:23812909, ECO:0000269|PubMed:24888332}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Trigonocephaly 1 (TRIGNO1) [MIM:190440]: A keel-shaped deformation of the forehead, caused by premature fusion of the metopic sutures. It results in a triangular shape of the head. {ECO:0000269|PubMed:11173846}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving FGFR1 may be a cause of stem cell leukemia lymphoma syndrome (SCLL). Translocation t(8;13)(p11;q12) with ZMYM2. SCLL usually presents as lymphoblastic lymphoma in association with a myeloproliferative disorder, often accompanied by pronounced peripheral eosinophilia and/or prominent eosinophilic infiltrates in the affected bone marrow. {ECO:0000269|PubMed:9716603}.; DISEASE: Note=A chromosomal aberration involving FGFR1 may be a cause of stem cell myeloproliferative disorder (MPD). Translocation t(6;8)(q27;p11) with FGFR1OP. Insertion ins(12;8)(p11;p11p22) with FGFR1OP2. MPD is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. The fusion proteins FGFR1OP2-FGFR1, FGFR1OP-FGFR1 or FGFR1-FGFR1OP may exhibit constitutive kinase activity and be responsible for the transforming activity. {ECO:0000269|PubMed:10688839, ECO:0000269|PubMed:15034873, ECO:0000269|PubMed:16946300, ECO:0000269|PubMed:17389761, ECO:0000269|PubMed:9949182}.; DISEASE: Note=A chromosomal aberration involving FGFR1 may be a cause of stem cell myeloproliferative disorder (MPD). Translocation t(8;9)(p12;q33) with CNTRL. MPD is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. The fusion protein CNTRL-FGFR1 is found in the cytoplasm, exhibits constitutive kinase activity and may be responsible for the transforming activity.; TISSUE SPECIFICITY: Detected in astrocytoma, neuroblastoma and adrenal cortex cell lines. Some isoforms are detected in foreskin fibroblast cell lines, however isoform 17, isoform 18 and isoform 19 are not detected in these cells. {ECO:0000269|PubMed:1652059}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;iris;germinal center;bladder;brain;amygdala;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;choroid;fovea centralis;vein;uterus;whole body;synovium;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;pancreas;lung;placenta;hippocampus;head and neck;kidney;aorta;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex;cerebellum; 0.99630 0.78607 -1.352082458 4.582448691 135.04043 2.52823 FGFR1OP 0.710817709841688 0.28904119183769 0.000141098320622086 FGFR1 oncogene partner FUNCTION: Required for anchoring microtubules to the centrosomes. {ECO:0000269|PubMed:16314388}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, liver, muscle, kidney, intestine, colon, adrenal gland, prostate, testis, and pancreas. {ECO:0000269|PubMed:9949182}.; unclassifiable (Anatomical System);lymph node;ovary;heart;hypothalamus;muscle;colon;parathyroid;skin;skeletal muscle;uterus;bile duct;whole body;lung;larynx;bone;placenta;pituitary gland;testis;head and neck;germinal center;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skin; 0.62808 0.25222 1.063778722 91.58410002 895.94414 5.83329 FGFR1OP2 0.42972800313106 0.568760514559844 0.00151148230909622 FGFR1 oncogene partner 2 FUNCTION: May be involved in wound healing pathway. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in bone marrow, spleen and thymus.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;lens;skeletal muscle;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;hippocampus;liver;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;appendix;trigeminal ganglion;cingulate cortex;parietal lobe; 0.16605 0.12716 -0.361761279 28.6329323 26.47953 0.85687 FGFR1OP2P1 . . . FGFR1 oncogene partner 2 pseudogene 1 . . . . . . . . . . . FGFR2 0.999752493022751 0.000247506962823288 1.4425836982295e-11 fibroblast growth factor receptor 2 FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1. {ECO:0000269|PubMed:12529371, ECO:0000269|PubMed:15190072, ECO:0000269|PubMed:15629145, ECO:0000269|PubMed:16384934, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17311277, ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:18374639, ECO:0000269|PubMed:19103595, ECO:0000269|PubMed:19387476, ECO:0000269|PubMed:19410646, ECO:0000269|PubMed:21596750, ECO:0000269|PubMed:8663044}.; DISEASE: Crouzon syndrome (CS) [MIM:123500]: An autosomal dominant syndrome characterized by craniosynostosis, hypertelorism, exophthalmos and external strabismus, parrot-beaked nose, short upper lip, hypoplastic maxilla, and a relative mandibular prognathism. {ECO:0000269|PubMed:10574673, ECO:0000269|PubMed:11173845, ECO:0000269|PubMed:11380921, ECO:0000269|PubMed:11781872, ECO:0000269|PubMed:7581378, ECO:0000269|PubMed:7655462, ECO:0000269|PubMed:7874170, ECO:0000269|PubMed:7987400, ECO:0000269|PubMed:8528214, ECO:0000269|PubMed:8644708, ECO:0000269|PubMed:8946174, ECO:0000269|PubMed:8956050, ECO:0000269|PubMed:9002682, ECO:0000269|PubMed:9152842, ECO:0000269|PubMed:9521581, ECO:0000269|PubMed:9677057, ECO:0000269|Ref.10}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Jackson-Weiss syndrome (JWS) [MIM:123150]: An autosomal dominant craniosynostosis syndrome characterized by craniofacial abnormalities and abnormality of the feet: broad great toes with medial deviation and tarsal-metatarsal coalescence. {ECO:0000269|PubMed:7874170, ECO:0000269|PubMed:8528214, ECO:0000269|PubMed:8644708, ECO:0000269|PubMed:9385368, ECO:0000269|PubMed:9677057}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Apert syndrome (APRS) [MIM:101200]: A syndrome characterized by facio-cranio-synostosis, osseous and membranous syndactyly of the four extremities, and midface hypoplasia. The craniosynostosis is bicoronal and results in acrocephaly of brachysphenocephalic type. Syndactyly of the fingers and toes may be total (mitten hands and sock feet) or partial affecting the second, third, and fourth digits. Intellectual deficit is frequent and often severe, usually being associated with cerebral malformations. {ECO:0000269|PubMed:11781872, ECO:0000269|PubMed:7668257, ECO:0000269|PubMed:7719344, ECO:0000269|PubMed:9002682, ECO:0000269|PubMed:9452027, ECO:0000269|PubMed:9677057}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pfeiffer syndrome (PS) [MIM:101600]: A syndrome characterized by the association of craniosynostosis, broad and deviated thumbs and big toes, and partial syndactyly of the fingers and toes. Three subtypes are known: mild autosomal dominant form (type 1); cloverleaf skull, elbow ankylosis, early death, sporadic (type 2); craniosynostosis, early demise, sporadic (type 3). {ECO:0000269|PubMed:10394936, ECO:0000269|PubMed:10945669, ECO:0000269|PubMed:11173845, ECO:0000269|PubMed:11781872, ECO:0000269|PubMed:7719333, ECO:0000269|PubMed:7719345, ECO:0000269|PubMed:8644708, ECO:0000269|PubMed:9002682, ECO:0000269|PubMed:9150725, ECO:0000269|PubMed:9693549, ECO:0000269|PubMed:9719378}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Beare-Stevenson cutis gyrata syndrome (BSTVS) [MIM:123790]: An autosomal dominant disease characterized by craniofacial anomalies, particularly craniosynostosis, and ear defects, cutis gyrata, acanthosis nigricans, anogenital anomalies, skin tags, and prominent umbilical stump. The skin furrows have a corrugated appearance and are widespread. Cutis gyrata variably affects the scalp, forehead, face, preauricular area, neck, trunk, hands, and feet. {ECO:0000269|PubMed:12000365, ECO:0000269|PubMed:8696350}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Familial scaphocephaly syndrome (FSPC) [MIM:609579]: An autosomal dominant craniosynostosis syndrome characterized by scaphocephaly, macrocephaly, hypertelorism, maxillary retrusion, and mild intellectual disability. Scaphocephaly is the most common of the craniosynostosis conditions and is characterized by a long, narrow head. It is due to premature fusion of the sagittal suture or from external deformation. {ECO:0000269|PubMed:16061565}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Lacrimo-auriculo-dento-digital syndrome (LADDS) [MIM:149730]: An autosomal dominant ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Lacrimo-auriculo-dento-digital syndrome is characterized by aplastic/hypoplastic lacrimal and salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia and enamel hypoplasia, and distal limb segments anomalies. In addition to these cardinal features, facial dysmorphism, malformations of the kidney and respiratory system and abnormal genitalia have been reported. Craniosynostosis and severe syndactyly are not observed. {ECO:0000269|PubMed:16501574}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Antley-Bixler syndrome, without genital anomalies or disordered steroidogenesis (ABS2) [MIM:207410]: A rare syndrome characterized by craniosynostosis, radiohumeral synostosis present from the perinatal period, midface hypoplasia, choanal stenosis or atresia, femoral bowing and multiple joint contractures. Arachnodactyly and/or camptodactyly have also been reported. {ECO:0000269|PubMed:10633130}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bent bone dysplasia syndrome (BBDS) [MIM:614592]: A perinatal lethal skeletal dysplasia characterized by poor mineralization of the calvarium, craniosynostosis, dysmorphic facial features, prenatal teeth, hypoplastic pubis and clavicles, osteopenia, and bent long bones. Dysmorphic facial features included low-set ears, hypertelorism, midface hypoplasia, prematurely erupted fetal teeth, and micrognathia. {ECO:0000269|PubMed:22387015}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;developmental;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;urinary;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;epididymis;nasopharynx;trabecular meshwork;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; whole brain;medulla oblongata;thalamus;superior cervical ganglion;occipital lobe;cerebellum peduncles;caudate nucleus;pons;fetal thyroid;uterus;subthalamic nucleus;thyroid;globus pallidus;ciliary ganglion;fetal lung;trigeminal ganglion;cingulate cortex;amygdala;hypothalamus;temporal lobe;spinal cord;atrioventricular node;skeletal muscle;fetal liver;trachea;prefrontal cortex;appendix;parietal lobe;cerebellum; 0.96396 0.76280 -1.50462206 3.568058504 593.43974 4.93642 FGFR3 0.00290912236409275 0.996560983354136 0.000529894281771077 fibroblast growth factor receptor 3 FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but can also promote cancer cell proliferation. Required for normal development of the inner ear. Phosphorylates PLCG1, CBL and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Plays a role in the regulation of vitamin D metabolism. Mutations that lead to constitutive kinase activation or impair normal FGFR3 maturation, internalization and degradation lead to aberrant signaling. Over-expressed or constitutively activated FGFR3 promotes activation of PTPN11/SHP2, STAT1, STAT5A and STAT5B. Secreted isoform 3 retains its capacity to bind FGF1 and FGF2 and hence may interfere with FGF signaling. {ECO:0000269|PubMed:10611230, ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:11703096, ECO:0000269|PubMed:14534538, ECO:0000269|PubMed:16410555, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17145761, ECO:0000269|PubMed:17311277, ECO:0000269|PubMed:17509076, ECO:0000269|PubMed:17561467, ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:19286672, ECO:0000269|PubMed:8663044}.; DISEASE: Achondroplasia (ACH) [MIM:100800]: A frequent form of short-limb dwarfism. It is characterized by a long, narrow trunk, short extremities, particularly in the proximal (rhizomelic) segments, a large head with frontal bossing, hypoplasia of the midface and a trident configuration of the hands. {ECO:0000269|PubMed:7758520, ECO:0000269|PubMed:7847369, ECO:0000269|PubMed:8078586}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Crouzon syndrome with acanthosis nigricans (CAN) [MIM:612247]: Classic Crouzon disease which is caused by mutations in the FGFR2 gene is characterized by craniosynostosis (premature fusion of the skull sutures), and facial hypoplasia. Crouzon syndrome with acanthosis nigricans (a skin disorder characterized by pigmentation anomalies), CAN, is considered to be an independent disorder from classic Crouzon syndrome. CAN is characterized by additional more severe physical manifestation, such as Chiari malformation, hydrocephalus, and atresia or stenosis of the choanas, and is caused by a specific mutation (Ala-391 to Glu) in the transmembrane domain of FGFR3. It is proposed to have an autosomal dominant mode of inheritance. {ECO:0000269|PubMed:17935505, ECO:0000269|PubMed:7493034}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Thanatophoric dysplasia 1 (TD1) [MIM:187600]: A neonatal lethal skeletal dysplasia. Affected individuals manifest severe shortening of the limbs with macrocephaly, narrow thorax, short ribs, and curved femurs. {ECO:0000269|PubMed:10360402, ECO:0000269|PubMed:10671061, ECO:0000269|PubMed:7773297, ECO:0000269|PubMed:8589699, ECO:0000269|PubMed:8845844, ECO:0000269|PubMed:9790257}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Thanatophoric dysplasia 2 (TD2) [MIM:187601]: A neonatal lethal skeletal dysplasia causing severe shortening of the limbs, narrow thorax and short ribs. Patients with thanatophoric dysplasia type 2 have straight femurs and cloverleaf skull. {ECO:0000269|PubMed:7773297}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hypochondroplasia (HCH) [MIM:146000]: Autosomal dominant disease and is characterized by disproportionate short stature. It resembles achondroplasia, but with a less severe phenotype. {ECO:0000269|PubMed:10215410, ECO:0000269|PubMed:10777366, ECO:0000269|PubMed:11055896, ECO:0000269|PubMed:12707965, ECO:0000269|PubMed:7670477, ECO:0000269|PubMed:9452043}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bladder cancer (BLC) [MIM:109800]: A malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas that begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences. {ECO:0000269|PubMed:10471491, ECO:0000269|PubMed:11314002}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Somatic mutations can constitutively activate FGFR3.; DISEASE: Cervical cancer (CERCA) [MIM:603956]: A malignant neoplasm of the cervix, typically originating from a dysplastic or premalignant lesion previously present at the active squamocolumnar junction. The transformation from mild dysplastic to invasive carcinoma generally occurs slowly within several years, although the rate of this process varies widely. Carcinoma in situ is particularly known to precede invasive cervical cancer in most cases. Cervical cancer is strongly associated with infection by oncogenic types of human papillomavirus. {ECO:0000269|PubMed:10471491}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Camptodactyly tall stature and hearing loss syndrome (CATSHL syndrome) [MIM:610474]: Autosomal dominant syndrome characterized by permanent and irreducible flexion of one or more fingers of the hand and/or feet, tall stature, scoliosis and/or a pectus excavatum, and hearing loss. Affected individuals have developmental delay and/or mental retardation, and several of these have microcephaly. Radiographic findings included tall vertebral bodies with irregular borders and broad femoral metaphyses with long tubular shafts. On audiological exam, each tested member have bilateral sensorineural hearing loss and absent otoacoustic emissions. The hearing loss was congenital or developed in early infancy, progressed variably in early childhood, and range from mild to severe. Computed tomography and magnetic resonance imaging reveal that the brain, middle ear, and inner ear are structurally normal. {ECO:0000269|PubMed:17033969}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multiple myeloma (MM) [MIM:254500]: A malignant tumor of plasma cells usually arising in the bone marrow and characterized by diffuse involvement of the skeletal system, hyperglobulinemia, Bence-Jones proteinuria and anemia. Complications of multiple myeloma are bone pain, hypercalcemia, renal failure and spinal cord compression. The aberrant antibodies that are produced lead to impaired humoral immunity and patients have a high prevalence of infection. Amyloidosis may develop in some patients. Multiple myeloma is part of a spectrum of diseases ranging from monoclonal gammopathy of unknown significance (MGUS) to plasma cell leukemia. {ECO:0000269|PubMed:11529856, ECO:0000269|PubMed:9207791}. Note=The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving FGFR3 is found in multiple myeloma. Translocation t(4;14)(p16.3;q32.3) with the IgH locus.; DISEASE: Lacrimo-auriculo-dento-digital syndrome (LADDS) [MIM:149730]: An autosomal dominant ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Lacrimo-auriculo-dento-digital syndrome is characterized by aplastic/hypoplastic lacrimal and salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia and enamel hypoplasia, and distal limb segments anomalies. In addition to these cardinal features, facial dysmorphism, malformations of the kidney and respiratory system and abnormal genitalia have been reported. Craniosynostosis and severe syndactyly are not observed. {ECO:0000269|PubMed:16501574}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Keratinocytic non-epidermolytic nevus (KNEN) [MIM:162900]: Epidermal nevi of the common, non-organoid and non- epidermolytic type are benign skin lesions and may vary in their extent from a single (usually linear) lesion to widespread and systematized involvement. They may be present at birth or develop early during childhood. {ECO:0000269|PubMed:16841094}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Muenke syndrome (MNKS) [MIM:602849]: A condition characterized by premature closure of coronal suture of skull during development (coronal craniosynostosis), which affects the shape of the head and face. It may be uni- or bilateral. When bilateral, it is characterized by a skull with a small antero- posterior diameter (brachycephaly), often with a decrease in the depth of the orbits and hypoplasia of the maxillae. Unilateral closure of the coronal sutures leads to flattening of the orbit on the involved side (plagiocephaly). The intellect is normal. In addition to coronal craniosynostosis some affected individuals show skeletal abnormalities of hands and feet, sensorineural hearing loss, mental retardation and respiratory insufficiency. {ECO:0000269|PubMed:11746040, ECO:0000269|PubMed:9042914, ECO:0000269|PubMed:9950359}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Keratosis, seborrheic (KERSEB) [MIM:182000]: A common benign skin tumor. Seborrheic keratoses usually begin with the appearance of one or more sharply defined, light brown, flat macules. The lesions may be sparse or numerous. As they initially grow, they develop a velvety to finely verrucous surface, followed by an uneven warty surface with multiple plugged follicles and a dull or lackluster appearance. {ECO:0000269|PubMed:15772091}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Testicular germ cell tumor (TGCT) [MIM:273300]: A common malignancy in males representing 95% of all testicular neoplasms. TGCTs have various pathologic subtypes including: unclassified intratubular germ cell neoplasia, seminoma (including cases with syncytiotrophoblastic cells), spermatocytic seminoma, embryonal carcinoma, yolk sac tumor, choriocarcinoma, and teratoma. {ECO:0000269|PubMed:19855393}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Achondroplasia, severe, with developmental delay and acanthosis nigricans (SADDAN) [MIM:616482]: A severe form of achondroplasia associated with developmental delay and acanthosis nigricans. Patients manifest short-limb dwarfism, with a long, narrow trunk, short extremities, particularly in the proximal (rhizomelic) segments, a large head with frontal bossing, hypoplasia of the midface and a trident configuration of the hands. Acanthosis nigricans is a skin condition characterized by brown-pigmented, velvety verrucosities in body folds and creases. {ECO:0000269|PubMed:10053006}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, kidney and testis. Very low or no expression in spleen, heart, and muscle. In 20- to 22- week old fetuses it is expressed at high level in kidney, lung, small intestine and brain, and to a lower degree in spleen, liver, and muscle. Isoform 2 is detected in epithelial cells. Isoform 1 is not detected in epithelial cells. Isoform 1 and isoform 2 are detected in fibroblastic cells. {ECO:0000269|PubMed:1664411}.; unclassifiable (Anatomical System);amygdala;cartilage;heart;ovary;urinary;colon;parathyroid;lens;skin;uterus;prostate;lung;frontal lobe;larynx;bone;placenta;iris;liver;testis;spleen;kidney;brain;bladder;stomach; whole brain;dorsal root ganglion;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;cerebellum peduncles;pons;caudate nucleus;skin;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;amygdala;tongue;hypothalamus;temporal lobe;spinal cord;atrioventricular node;skeletal muscle;prefrontal cortex;kidney;parietal lobe;cerebellum; 0.84572 0.78546 -2.054162281 1.639537627 129.20225 2.47726 FGFR3P1 . . . fibroblast growth factor receptor 3 pseudogene 1 . . . . . . . . . . . FGFR3P2 . . . fibroblast growth factor receptor 3 pseudogene 2 . . . . . . . . . . . FGFR3P3 . . . fibroblast growth factor receptor 3 pseudogene 3 . . . . . . . . . . . FGFR3P4 . . . fibroblast growth factor receptor 3 pseudogene 4 . . . . . . . . . . . FGFR3P5 . . . fibroblast growth factor receptor 3 pseudogene 5 . . . . . . . . . . . FGFR3P6 . . . fibroblast growth factor receptor 3 pseudogene 6 . . . . . . . . . . . FGFR4 1.30017490282e-06 0.997645977567797 0.00235272225730068 fibroblast growth factor receptor 4 FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays a role in the regulation of cell proliferation, differentiation and migration, and in regulation of lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism and phosphate homeostasis. Required for normal down-regulation of the expression of CYP7A1, the rate-limiting enzyme in bile acid synthesis, in response to FGF19. Phosphorylates PLCG1 and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes SRC-dependent phosphorylation of the matrix protease MMP14 and its lysosomal degradation. FGFR4 signaling is down-regulated by receptor internalization and degradation; MMP14 promotes internalization and degradation of FGFR4. Mutations that lead to constitutive kinase activation or impair normal FGFR4 inactivation lead to aberrant signaling. {ECO:0000269|PubMed:11433297, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17311277, ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:18480409, ECO:0000269|PubMed:18670643, ECO:0000269|PubMed:20018895, ECO:0000269|PubMed:20683963, ECO:0000269|PubMed:20798051, ECO:0000269|PubMed:20876804, ECO:0000269|PubMed:21653700, ECO:0000269|PubMed:7518429, ECO:0000269|PubMed:7680645, ECO:0000269|PubMed:8663044}.; . TISSUE SPECIFICITY: Expressed in gastrointestinal epithelial cells, pancreas, and gastric and pancreatic cancer cell lines. {ECO:0000269|PubMed:10631118}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;heart;tongue;muscle;adrenal cortex;colon;skin;retina;uterus;pancreas;whole body;lung;placenta;iris;liver;testis;spleen;kidney;brain;stomach;peripheral nerve; liver;pons;trigeminal ganglion;skeletal muscle; 0.93925 0.31636 -1.16661987 6.074545883 3921.42674 12.37862 FGFRL1 0.582186675448565 0.415564326836932 0.00224899771450375 fibroblast growth factor receptor-like 1 FUNCTION: Has a negative effect on cell proliferation. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed preferentially in cartilaginous tissues and pancreas. Highly expressed in the liver, kidney, heart, brain and skeletal muscle. Weakly expressed in the lung, small intestine and spleen. {ECO:0000269|PubMed:11031111, ECO:0000269|PubMed:11267671, ECO:0000269|PubMed:11418238}.; ovary;colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;tongue;muscle;lens;pancreas;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;head and neck;kidney;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.28351 0.19079 -0.773369631 13.10450578 1602.42506 7.40485 FGG 0.0792944198109911 0.918454564363406 0.00225101582560299 fibrinogen gamma chain FUNCTION: Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re- epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3- dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways. {ECO:0000250|UniProtKB:E9PV24}.; DISEASE: Congenital afibrinogenemia (CAFBN) [MIM:202400]: Rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. {ECO:0000269|PubMed:25427968}. Note=The disease is caused by mutations affecting the gene represented in this entry. Patients with congenital fibrinogen abnormalities can manifest different clinical pictures. Some cases are clinically silent, some show a tendency toward bleeding and some show a predisposition for thrombosis with or without bleeding.; DISEASE: Dysfibrinogenemia, congenital (DYSFIBRIN) [MIM:616004]: A disorder characterized by qualitative abnormalities (dysfibrinogenemia) of the circulating fibrinogen. Affected individuals are frequently asymptomatic, but some patients have bleeding diathesis, thromboembolic complications, or both. In some cases, dysfibrinogenemia is associated with low circulating fibrinogen levels (hypodysfibrinogenemia). {ECO:0000269|PubMed:15632207, ECO:0000269|PubMed:2257302, ECO:0000269|PubMed:2976995, ECO:0000269|PubMed:3708159}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in blood plasma (at protein level). {ECO:0000269|PubMed:10074346, ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;bone;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;urinary;pharynx;blood;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland; fetal liver;superior cervical ganglion;liver;fetal lung;atrioventricular node;trigeminal ganglion; 0.41926 0.35159 -0.025608647 51.91672564 178.16892 2.90197 FGGY 1.20951730816233e-11 0.165739878636241 0.834260121351664 FGGY carbohydrate kinase domain containing . DISEASE: Amyotrophic lateral sclerosis (ALS) [MIM:105400]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. {ECO:0000269|PubMed:17671248}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in kidney, lung and small intestine and to a lower extent in liver and detected in cerebrospinal fluid (at protein level). {ECO:0000269|PubMed:17671248}.; unclassifiable (Anatomical System);pancreas;optic nerve;cartilage;bone;placenta;macula lutea;colon;fovea centralis;choroid;germinal center;lens;stomach;retina; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.10533 0.14102 0.338046437 73.70252418 2727.68735 9.84042 FGL1 1.873536127279e-16 0.000502618554616534 0.999497381445383 fibrinogen like 1 FUNCTION: Has hepatocyte mitogenic activity.; . TISSUE SPECIFICITY: Liver specific.; unclassifiable (Anatomical System);heart;islets of Langerhans;skeletal muscle;skin;uterus;pancreas;lung;liver;testis;spleen;cervix;brain;gall bladder; superior cervical ganglion;fetal liver;pancreas;liver;fetal lung;pons; 0.41553 . 1.291545885 93.87827318 2773.25166 9.94002 FGL2 0.0949976759625154 0.868036518323295 0.0369658057141898 fibrinogen like 2 FUNCTION: May play a role in physiologic lymphocyte functions at mucosal sites.; . TISSUE SPECIFICITY: Constitutively expressed in cytotoxic T-cells.; colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;cerebral cortex;thyroid;iris;testis;germinal center;brain;artery;pineal gland;unclassifiable (Anatomical System);heart;adrenal cortex;blood;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach;aorta; superior cervical ganglion;ciliary ganglion;whole blood;trigeminal ganglion; 0.17333 0.32083 -0.071520315 48.34866714 835.01222 5.65658 FGR 0.177174438745081 0.822283511602123 0.000542049652795049 FGR proto-oncogene, Src family tyrosine kinase FUNCTION: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors devoid of kinase activity and contributes to the regulation of immune responses, including neutrophil, monocyte, macrophage and mast cell functions, cytoskeleton remodeling in response to extracellular stimuli, phagocytosis, cell adhesion and migration. Promotes mast cell degranulation, release of inflammatory cytokines and IgE-mediated anaphylaxis. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as MS4A2/FCER1B, FCGR2A and/or FCGR2B. Acts downstream of ITGB1 and ITGB2, and regulates actin cytoskeleton reorganization, cell spreading and adhesion. Depending on the context, activates or inhibits cellular responses. Functions as negative regulator of ITGB2 signaling, phagocytosis and SYK activity in monocytes. Required for normal ITGB1 and ITGB2 signaling, normal cell spreading and adhesion in neutrophils and macrophages. Functions as positive regulator of cell migration and regulates cytoskeleton reorganization via RAC1 activation. Phosphorylates SYK (in vitro) and promotes SYK- dependent activation of AKT1 and MAP kinase signaling. Phosphorylates PLD2 in antigen-stimulated mast cells, leading to PLD2 activation and the production of the signaling molecules lysophosphatidic acid and diacylglycerol. Promotes activation of PIK3R1. Phosphorylates FASLG, and thereby regulates its ubiquitination and subsequent internalization. Phosphorylates ABL1. Promotes phosphorylation of CBL, CTTN, PIK3R1, PTK2/FAK1, PTK2B/PYK2 and VAV2. Phosphorylates HCLS1 that has already been phosphorylated by SYK, but not unphosphorylated HCLS1. {ECO:0000269|PubMed:10739672, ECO:0000269|PubMed:17164290, ECO:0000269|PubMed:1737799, ECO:0000269|PubMed:7519620}.; DISEASE: Note=Mutations that cause aberrant kinase activation can confer oncogene activity and promote aberrant cell proliferation.; TISSUE SPECIFICITY: Detected in neutrophils, monocytes and natural killer cells (at protein level). Detected in monocytes and large lymphocytes. {ECO:0000269|PubMed:11078731, ECO:0000269|PubMed:2181286, ECO:0000269|PubMed:8327512}.; . . 0.51380 0.60658 -0.890882376 10.30313753 36.77665 1.10224 FGS2 . . . FG syndrome 2 . . . . . . . . . . . FGS3 . . . FG syndrome 3 . . . . . . . . . . . FGS5 . . . FG syndrome 5 . . . . . . . . . . . FH 0.148694445276004 0.847596211626511 0.00370934309748547 fumarate hydratase FUNCTION: Also acts as a tumor suppressor.; DISEASE: Hereditary leiomyomatosis and renal cell cancer (HLRCC) [MIM:150800]: A disorder characterized by predisposition to cutaneous and uterine leiomyomas, and papillary type 2 renal cancer which occurs in about 20% of patients. {ECO:0000269|PubMed:11865300}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in red blood cells; underexpressed in red blood cells (cytoplasm) of patients with hereditary non- spherocytic hemolytic anemia of unknown etiology. {ECO:0000269|PubMed:22509282}.; . . 0.16989 0.62965 -0.47017169 23.25430526 46.01019 1.30676 FHAD1 . . . forkhead-associated (FHA) phosphopeptide binding domain 1 . . . unclassifiable (Anatomical System);lung;cartilage;ovary;endometrium;testis;colon;cervix;brain;skin;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.15161 . . . 7171.08749 18.24457 FHDC1 0.024454126798477 0.975428957891545 0.000116915309977695 FH2 domain containing 1 . . . unclassifiable (Anatomical System);heart;ovary;lacrimal gland;colon;parathyroid;skin;skeletal muscle;retina;bone marrow;breast;uterus;prostate;whole body;lung;placenta;visual apparatus;liver;testis;spleen;brain;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.39667 0.08948 0.969962249 90.20995518 6091.11428 16.31408 FHIT 0.00139183900459992 0.662104570551977 0.336503590443423 fragile histidine triad FUNCTION: Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'- adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low- affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor. {ECO:0000269|PubMed:12574506, ECO:0000269|PubMed:15313915, ECO:0000269|PubMed:16407838, ECO:0000269|PubMed:18077326, ECO:0000269|PubMed:19622739, ECO:0000269|PubMed:8794732, ECO:0000269|PubMed:9323207}.; DISEASE: Note=A chromosomal aberration involving FHIT has been found in a lymphoblastoid cell line established from a family with renal cell carcinoma and thyroid carcinoma. Translocation t(3;8)(p14.2;q24.1) with RNF139. Although the 3p14.2 breakpoint has been shown to interrupt FHIT in its 5-prime non-coding region, it is unlikely that FHIT is causally related to renal or other malignancies. {ECO:0000269|PubMed:15007172}.; DISEASE: Note=Associated with digestive tract cancers. Numerous tumor types are found to have aberrant forms of FHIT protein due to deletions in a coding region of chromosome 3p14.2 including the fragile site locus FRA3B. {ECO:0000269|PubMed:15007172}.; TISSUE SPECIFICITY: Low levels expressed in all tissues tested. Phospho-FHIT observed in liver and kidney, but not in brain and lung. Phospho-FHIT undetected in all tested human tumor cell lines.; unclassifiable (Anatomical System);liver; superior cervical ganglion;testis;globus pallidus;trigeminal ganglion; 0.25475 . -0.560178693 19.30879925 49.36677 1.37510 FHL1 0.918480756354643 0.0809877123835607 0.000531531261796771 four and a half LIM domains 1 FUNCTION: May have an involvement in muscle development or hypertrophy.; DISEASE: Scapuloperoneal myopathy, X-linked dominant (SPM) [MIM:300695]: A disease characterized by progressive muscle weakness and wasting, upper and lower limbs weakness, foot drop, scapular winging, and myopathic changes on muscle biopsy. Most affected individuals become wheelchair-bound. {ECO:0000269|PubMed:18179901}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myopathy, X-linked, with postural muscle atrophy (XMPMA) [MIM:300696]: A progressive muscular dystrophy with onset in adulthood. Affected individuals develop a proximal myopathy characterized by specific atrophy of postural muscles, limited neck flexion, bent spine, contractures of the Achilles tendon, respiratory problems, and cardiomyopathy. Patients may show muscle hypertrophy in the early stages of the disorder. {ECO:0000269|PubMed:18179888}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Reducing body myopathy, X-linked 1A, severe, with infantile or early childhood onset (RBMX1A) [MIM:300717]: A rare myopathy clinically characterized by rapidly progressive muscular weakness, and pathologically by the presence of intracytoplasmic inclusion bodies strongly stained by menadione-linked alpha- glycerophosphate dehydrogenase in the absence of substrate, alpha- glycerophosphate. The term 'reducing body' refers to the reducing activity of the inclusions to nitroblue tetrazolium in the absence of substrate. This condition is also commonly associated with rimmed vacuoles and cytoplasmic bodies. Death in childhood is frequent in the severe form of the disease, due to respiratory failure. {ECO:0000269|PubMed:18274675}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Reducing body myopathy, X-linked 1B, with late childhood or adult onset (RBMX1B) [MIM:300718]: A rare myopathy clinically characterized by rapidly progressive muscular weakness, and pathologically by the presence of intracytoplasmic inclusion bodies strongly stained by menadione-linked alpha-glycerophosphate dehydrogenase in the absence of substrate, alpha-glycerophosphate. The term 'reducing body' refers to the reducing activity of the inclusions to nitroblue tetrazolium in the absence of substrate. This condition is also commonly associated with rimmed vacuoles and cytoplasmic bodies. {ECO:0000269|PubMed:18274675}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is highly expressed in skeletal muscle and to a lesser extent in heart, placenta, ovary, prostate, testis, small intestine, colon and spleen. Expression is barely detectable in brain, lung, liver, kidney, pancreas, thymus and peripheral blood leukocytes. Isoform 2 is expressed in brain, skeletal muscle and to a lesser extent in heart, colon, prostate and small intestine. Isoform 3 is expressed in testis, heart and skeletal muscle. {ECO:0000269|PubMed:10352231, ECO:0000269|PubMed:10480922, ECO:0000269|PubMed:10524257, ECO:0000269|PubMed:11400158, ECO:0000269|PubMed:9714789}.; lymphoreticular;myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;larynx;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;stomach;peripheral nerve;thymus; uterus;superior cervical ganglion;tongue;thyroid;testis;ciliary ganglion;atrioventricular node;fetal thyroid;trigeminal ganglion;skeletal muscle; 0.45850 0.13588 -0.029247611 51.40363293 11.75791 0.42591 FHL2 0.00288060194827599 0.805956694483372 0.191162703568352 four and a half LIM domains 2 FUNCTION: May function as a molecular transmitter linking various signaling pathways to transcriptional regulation. Negatively regulates the transcriptional repressor E4F1 and may function in cell growth. Inhibits the transcriptional activity of FOXO1 and its apoptotic function by enhancing the interaction of FOXO1 with SIRT1 and FOXO1 deacetylation. {ECO:0000269|PubMed:15692560, ECO:0000269|PubMed:16652157, ECO:0000269|PubMed:18853468}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle and heart. {ECO:0000269|PubMed:11813260}.; myocardium;smooth muscle;ovary;salivary gland;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;oesophagus;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; heart;testis; 0.43632 0.43471 0.305084559 72.22811984 179.31638 2.90890 FHL3 0.534417265883107 0.462285973038152 0.00329676107874104 four and a half LIM domains 3 . . TISSUE SPECIFICITY: Expressed only in skeletal muscle.; . . 0.29794 0.11106 0.284856336 71.40835103 213.429 3.15204 FHL5 1.6770876188147e-08 0.0649839781428217 0.935016005086302 four and a half LIM domains 5 FUNCTION: May be involved in the regulation of spermatogenesis. Stimulates CREM transcriptional activity in a phosphorylation- independent manner. {ECO:0000269|PubMed:11327716}.; . TISSUE SPECIFICITY: Testis-specific (at protein level). {ECO:0000269|PubMed:11327716}.; unclassifiable (Anatomical System);uterus;medulla oblongata;prostate;lung;hippocampus;testis;kidney;brain;aorta;peripheral nerve; superior cervical ganglion; 0.50220 0.10754 0.551232944 81.48148148 7073.32393 18.05603 FHOD1 9.46042582987411e-11 0.973117690619692 0.0268823092857035 formin homology 2 domain containing 1 FUNCTION: Required for the assembly of F-actin structures, such as stress fibers. Depends on the Rho-ROCK cascade for its activity. Contributes to the coordination of microtubules with actin fibers and plays a role in cell elongation. Acts synergistically with ROCK1 to promote SRC-dependent non-apoptotic plasma membrane blebbing. {ECO:0000269|PubMed:14576350, ECO:0000269|PubMed:15878344, ECO:0000269|PubMed:18694941}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in spleen.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; ciliary ganglion;skeletal muscle; 0.07189 0.11325 -1.210720546 5.708893607 299.32026 3.68910 FHOD3 0.997517122779082 0.00248287721956847 1.34944150052697e-12 formin homology 2 domain containing 3 FUNCTION: Actin-organizing protein that may cause stress fiber formation together with cell elongation (By similarity). Isoform 4 may play a role in actin filament polymerization in cardiomyocytes. {ECO:0000250, ECO:0000269|PubMed:21149568}.; . TISSUE SPECIFICITY: Expressed in the heart, kidney and brain. May be down-regulated in various types of heart diseases, including idiopathic dilated, ventricular dilated, familial dilated and perinatal dilated cardiomyopathies, as well as ischemic heart disease (at protein level). {ECO:0000269|PubMed:15966898, ECO:0000269|PubMed:21149568}.; myocardium;ovary;sympathetic chain;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;gum;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;liver;kidney;peripheral nerve; . 0.22803 0.10389 -0.514518236 21.21962727 7901.72753 19.20257 FHP1 . . . fumarate hydratase pseudogene 1 . . . . . . . . . . . FIBCD1 7.56460038005606e-06 0.497591280316804 0.502401155082815 fibrinogen C domain containing 1 FUNCTION: Acetyl group-binding receptor which shows a high- affinity and calcium-dependent binding to acetylated structures such as chitin, some N-acetylated carbohydrates, and amino acids, but not to their non-acetylated counterparts. Can facilitate the endocytosis of acetylated components. {ECO:0000269|PubMed:19710473, ECO:0000269|PubMed:19892701}.; . TISSUE SPECIFICITY: Expressed in the small and large intestinal epithelial cells with a highly polarized localization to the apical surface corresponding to the brush border and in the ducts of the salivary gland. {ECO:0000269|PubMed:19710473}.; unclassifiable (Anatomical System);lung;hippocampus;adrenal cortex;cervix; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; 0.11187 0.10744 . . 113.48525 2.31913 FIBIN 0.308532918780581 0.618579950060675 0.072887131158744 fin bud initiation factor homolog (zebrafish) . . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;cerebral cortex;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;stomach;aorta; dorsal root ganglion;kidney; . 0.10479 -0.073340031 48.11866006 90.00872 2.04253 FIBP 0.0147227845892947 0.957339109782707 0.0279381056279981 fibroblast growth factor (acidic) intracellular binding protein FUNCTION: May be involved in mitogenic function of FGF1. May mediate with IER2 FGF-signaling in the establishment of laterality in the embryo (By similarity). {ECO:0000250|UniProtKB:Q6T938, ECO:0000269|PubMed:9806903}.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and pancreas. Expressed at lower levels in brain. Also found in placenta, liver and kidney.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;blood;bile duct;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus;cerebellum; whole brain;occipital lobe;testis;globus pallidus;cingulate cortex;parietal lobe; 0.06689 0.11018 -0.734731259 14.01863647 126.71963 2.45493 FICD 0.00638582212011792 0.74494475973827 0.248669418141612 FIC domain containing FUNCTION: Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. Able to inactivate Rho GTPases in vitro by adding AMP to RhoA, Rac and Cdc42. It is however unclear whether it inactivates GTPases in vivo and physiological substrates probably remain to be identified. {ECO:0000269|PubMed:19362538, ECO:0000269|PubMed:22266942}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:19362538}.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;adrenal cortex;colon;skeletal muscle;lung;frontal lobe;endometrium;placenta;thyroid;bone;testis;cervix;germinal center;kidney; superior cervical ganglion;pons;trigeminal ganglion;parietal lobe; 0.16362 0.11879 -0.841329384 11.36470866 77.87832 1.86121 FIG4 6.58630936583289e-27 0.000172410793897148 0.999827589206103 FIG4 phosphoinositide 5-phosphatase FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). In vitro, hydrolyzes all three D5-phosphorylated polyphosphoinositide substrates in the order PtdIns(4,5)P2 > PtdIns(3,5)P2 > PtdIns(3,4,5)P3. Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes. {ECO:0000269|PubMed:17556371}.; DISEASE: Charcot-Marie-Tooth disease 4J (CMT4J) [MIM:611228]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot- Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie-Tooth disease are designated CMT4. {ECO:0000269|PubMed:17572665, ECO:0000269|PubMed:21705420}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Amyotrophic lateral sclerosis 11 (ALS11) [MIM:612577]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. {ECO:0000269|PubMed:19118816}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Yunis-Varon syndrome (YVS) [MIM:216340]: A severe autosomal recessive disorder characterized by skeletal defects, including cleidocranial dysplasia and digital anomalies, and severe neurologic involvement with neuronal loss. Enlarged cytoplasmic vacuoles are found in neurons, muscle, and cartilage. The disorder is usually lethal in infancy. {ECO:0000269|PubMed:23623387}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Polymicrogyria, bilateral temporooccipital (BTOP) [MIM:612691]: A disease characterized by temporo-occipital polymicrogyria, psychiatric manifestations, and epilepsy. {ECO:0000269|PubMed:24598713}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;liver;head and neck;kidney;mammary gland;stomach;aorta; dorsal root ganglion;medulla oblongata;subthalamic nucleus;superior cervical ganglion;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;caudate nucleus;pons;cingulate cortex;parietal lobe; 0.10577 0.13228 -0.308569083 32.17150271 2517.20331 9.35490 FIGF 0.0109063275472999 0.947209588622675 0.0418840838300256 c-fos induced growth factor (vascular endothelial growth factor D) FUNCTION: Growth factor active in angiogenesis, lymphangiogenesis and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in the formation of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates VEGFR-2 (KDR/FLK1) and VEGFR-3 (FLT4) receptors. {ECO:0000269|PubMed:21148085}.; . TISSUE SPECIFICITY: Highly expressed in lung, heart, small intestine and fetal lung, and at lower levels in skeletal muscle, colon, and pancreas.; unclassifiable (Anatomical System);uterus;lung;cartilage;heart;testis;kidney;mammary gland;skin; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.12987 0.18163 -0.427900189 25.14744043 117.16289 2.35335 FIGLA 0.731738228189441 0.256095983466897 0.0121657883436626 folliculogenesis specific bHLH transcription factor FUNCTION: Germline specific transcription factor implicated in postnatal oocyte-specific gene expression. Plays a key regulatory role in the expression of multiple oocyte-specific genes, including those that initiate folliculogenesis and those that encode the zona pellucida (ZP1, ZP2 and ZP3) required for fertilization and early embryonic survival. Essential for oocytes to survive and form primordial follicles. The persistence of FIGLA in adult females suggests that it may regulate additional pathways that are essential for normal ovarian development. Binds to the E- box (5'-CANNTG-3') of the ZPs (ZP1, ZP2, ZP3) promoters. {ECO:0000269|PubMed:15044608}.; DISEASE: Premature ovarian failure 6 (POF6) [MIM:612310]: An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol. {ECO:0000269|PubMed:18499083}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Germ cells. Expressed in the fetal ovary, but not by a range of other tissues. Expression increases across mid- gestation, rising some 40-fold by the time of primordial follicle formation. {ECO:0000269|PubMed:12468641, ECO:0000269|PubMed:15044608}.; . . 0.16674 0.09641 . . 11.44199 0.41368 FIGN 0.741736097596996 0.257767603659159 0.000496298743845078 fidgetin FUNCTION: ATP-dependent microtubule severing protein. Severs microtubules along their length and depolymerizes their ends, primarily the minus-end, that may lead to the suppression of microtubule growth from and attachment to centrosomes. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. {ECO:0000269|PubMed:22672901}.; . . unclassifiable (Anatomical System);prostate;islets of Langerhans;thyroid;liver;spleen;brain;skin; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.54402 0.11798 -1.021348453 7.997169144 349.42142 3.96068 FIGNL1 0.000108679232933473 0.818210839213463 0.181680481553603 fidgetin like 1 FUNCTION: Involved in DNA double-strand break (DBS) repair via homologous recombination (HR). Recruited at DSB sites independently of BRCA2, RAD51 and RAD51 paralogs in a H2AX- dependent manner. May regulate osteoblast proliferation and differentiation. {ECO:0000269|PubMed:23754376}.; . . ovary;colon;skin;retina;bone marrow;prostate;whole body;frontal lobe;larynx;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;muscle;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.47322 0.11118 0.093718683 60.71007313 480.09442 4.52035 FIGNL2 . . . fidgetin like 2 . . . . . . . . . . . FILIP1 1.85337719894375e-07 0.998417340484233 0.00158247417804711 filamin A interacting protein 1 FUNCTION: By acting through a filamin-A/F-actin axis, it controls the start of neocortical cell migration from the ventricular zone. May be able to induce the degradation of filamin-A. {ECO:0000250|UniProtKB:Q8K4T4}.; . TISSUE SPECIFICITY: Moderately expressed in adult heart and brain. Weakly expressed in lung, skeletal muscle, ovary, testis, kidney, and fetal brain, and hardly detectable in liver, pancreas, spleen, and fetal liver. Within brain, moderate expression is found in amygdala and caudate nucleus. {ECO:0000269|PubMed:10574462}.; unclassifiable (Anatomical System);myocardium;heart;spinal cord;skin;retina;uterus;whole body;lung;frontal lobe;nasopharynx;placenta;iris;hypopharynx;liver;head and neck;kidney;brain;aorta; . 0.47544 0.10259 -0.459259448 23.69072895 469.74844 4.48528 FILIP1L 0.000245912456600934 0.998996257957046 0.00075782958635314 filamin A interacting protein 1-like FUNCTION: Acts as a regulator of the antiangiogenic activity on endothelial cells. When overexpressed in endothelial cells, leads to inhibition of cell proliferation and migration and an increase in apoptosis. Inhibits melanoma growth When expressed in tumor- associated vasculature. {ECO:0000269|PubMed:18794120}.; . TISSUE SPECIFICITY: Expressed in endothelial cells, colon and colon cancers. In the colon, expressed in the vasculature and muscularis mucosa. In colon cancer, strongly expressed in tumor stroma and the vasculature (at protein level). Expressed in ovarian epithelial cells. Down-regulated in ovarian cancer. {ECO:0000269|PubMed:18794120, ECO:0000269|PubMed:8314147}.; medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;aorta; uterus;testis - interstitial;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.48690 0.09442 -1.190479796 5.874026893 2080.08329 8.40306 FIP1L1 0.600789667366506 0.399209671395459 6.61238034724868e-07 factor interacting with PAPOLA and CPSF1 FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre- mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. FIP1L1 contributes to poly(A) site recognition and stimulates poly(A) addition. Binds to U-rich RNA sequence elements surrounding the poly(A) site. May act to tether poly(A) polymerase to the CPSF complex. {ECO:0000269|PubMed:14749727}.; DISEASE: Note=A chromosomal aberration involving FIP1L1 is found in some cases of hypereosinophilic syndrome. Interstitial chromosomal deletion del(4)(q12q12) causes the fusion of FIP1L1 and PDGFRA (FIP1L1-PDGFRA). {ECO:0000269|PubMed:12660384, ECO:0000269|PubMed:12808148}.; . medulla oblongata;ovary;foreskin;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus; testis - interstitial;testis - seminiferous tubule;testis;white blood cells; 0.65360 0.14098 -0.582225231 18.44184949 70.2485 1.74153 FIRRE . . . firre intergenic repeating RNA element . . . . . . . . . . . FIS1 0.0401785771611955 0.841806543972658 0.118014878866147 fission, mitochondrial 1 FUNCTION: Involved in the fragmentation of the mitochondrial network and its perinuclear clustering. Plays a minor role in the recruitment and association of the fission mediator dynamin- related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis. Also mediates peroxisomal fission. {ECO:0000269|PubMed:12783892, ECO:0000269|PubMed:12861026, ECO:0000269|PubMed:14996942, ECO:0000269|PubMed:16107562, ECO:0000269|PubMed:16118244, ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:23530241}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;iris;testis;amniotic fluid;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;hypothalamus;pineal body;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; whole brain;thalamus;heart;liver;parietal lobe; 0.15008 0.11262 0.169169615 65.33380514 445.95856 4.39577 FITM1 0.072113818994595 0.872313595280136 0.0555725857252694 fat storage-inducing transmembrane protein 1 FUNCTION: Plays an important role in lipid droplet accumulation. {ECO:0000269|PubMed:18160536}.; . TISSUE SPECIFICITY: Primarily expressed in heart and skeletal muscle. {ECO:0000269|PubMed:18160536}.; heart;ovary;muscle;parathyroid;skin;skeletal muscle;uterus;pancreas;whole body;lung;bone;placenta;pituitary gland;testis;spleen;cervix; heart;skeletal muscle; . . -0.336073593 30.55555556 81.11464 1.90644 FITM2 0.000110416566392742 0.370442505339718 0.629447078093889 fat storage-inducing transmembrane protein 2 FUNCTION: Plays an important role in lipid droplet accumulation. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:18160536, ECO:0000269|PubMed:21834987}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18160536}.; . . 0.15955 . 0.016664174 55.21939137 99.56974 2.15960 FIZ1 0.450714683779002 0.521392124199136 0.0278931920218618 FLT3 interacting zinc finger 1 FUNCTION: May be a transcriptional repressor of NRL function in photoreceptors. Does not repress CRX-mediated transactivation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12566383}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;muscle;urinary;pharynx;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.19240 0.12929 . . 105.13819 2.21878 FJX1 0.823951146531355 0.172149809347554 0.00389904412109132 four jointed box 1 FUNCTION: Acts as an inhibitor of dendrite extension and branching. {ECO:0000250}.; . . . . . . . . 573.0294 4.86028 FKBP1A 0.678638213250307 0.301232015687691 0.0201297710620027 FK506 binding protein 1A FUNCTION: Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. {ECO:0000269|PubMed:16720724, ECO:0000269|PubMed:9233797}.; . . . . 0.42043 0.33817 0.101211609 60.95777306 . . FKBP1A-SDCBP2 . . . FKBP1A-SDCBP2 readthrough (NMD candidate) . . . . . . . . . . . FKBP1AP1 . . . FK506 binding protein 1A pseudogene 1 . . . . . . . . . . . FKBP1AP2 . . . FK506 binding protein 1A pseudogene 2 . . . . . . . . . . . FKBP1AP3 . . . FK506 binding protein 1A pseudogene 3 . . . . . . . . . . . FKBP1AP4 . . . FK506 binding protein 1A pseudogene 4 . . . . . . . . . . . FKBP1B 0.00888532712656979 0.578325486171245 0.412789186702185 FK506 binding protein 1B FUNCTION: Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.; . TISSUE SPECIFICITY: Detected in heart muscle (at protein level). Isoform 1 and isoform 2 are ubiquitous with highest levels in brain and thymus. {ECO:0000269|PubMed:10830164}.; . . 0.73676 0.13588 -0.053113545 49.38664779 . . FKBP1C 0.000605467062300138 0.286322494200957 0.713072038736743 FK506 binding protein 1C . . . unclassifiable (Anatomical System);ovary;colon;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;prostate;optic nerve;lung;endometrium;placenta;macula lutea;hippocampus;liver;germinal center;brain;stomach; . 0.08683 . . . 15.57562 0.55569 FKBP2 0.307159555574364 0.674513163239108 0.0183272811865275 FK506 binding protein 2 FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.; . TISSUE SPECIFICITY: T-cells and thymus.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;bone;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;hypothalamus;pineal body;blood;lens;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; whole brain;thalamus;hypothalamus;placenta;thyroid;liver;caudate nucleus;pituitary; 0.19241 0.15665 0.058937498 58.26256192 203.88388 3.08240 FKBP3 0.812901762488181 0.186125399136339 0.000972838375480004 FK506 binding protein 3 FUNCTION: FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins.; . . medulla oblongata;ovary;salivary gland;intestine;colon;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;alveolus;hypopharynx;liver;head and neck;kidney;mammary gland;aorta;stomach; amygdala;subthalamic nucleus;superior cervical ganglion;thalamus;temporal lobe;prefrontal cortex;globus pallidus;caudate nucleus;pons;skeletal muscle;cingulate cortex;parietal lobe; 0.60725 0.13947 -0.229483771 36.86010852 2040.66315 8.32536 FKBP4 0.927473130653813 0.0725104758531231 1.63934930637242e-05 FK506 binding protein 4 FUNCTION: Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria. {ECO:0000269|PubMed:1279700, ECO:0000269|PubMed:1376003, ECO:0000269|PubMed:19945390, ECO:0000269|PubMed:21730050, ECO:0000269|PubMed:2378870}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:1279700}.; myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;duodenum;head and neck;kidney;stomach;thymus;cerebellum; whole brain;medulla oblongata;superior cervical ganglion;olfactory bulb;cerebellum peduncles;temporal lobe;liver;testis;globus pallidus;skeletal muscle;cerebellum; 0.21776 0.18689 0.040529541 57.15380986 145.4406 2.62631 FKBP4P1 . . . FK506 binding protein 4 pseudogene 1 . . . . . . . . . . . FKBP4P2 . . . FK506 binding protein 4 pseudogene 2 . . . . . . . . . . . FKBP4P5 . . . FK506 binding protein 4 pseudogene 5 . . . . . . . . . . . FKBP4P6 . . . FK506 binding protein 4 pseudogene 6 . . . . . . . . . . . FKBP4P7 . . . FK506 binding protein 4 pseudogene 7 . . . . . . . . . . . FKBP4P8 . . . FK506 binding protein 4 pseudogene 8 . . . . . . . . . . . FKBP5 0.498849476622916 0.500257970282122 0.000892553094961795 FK506 binding protein 5 FUNCTION: Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded.; . TISSUE SPECIFICITY: Widely expressed, enriched in testis compared to other tissues.; lymphoreticular;ovary;substantia nigra;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;ciliary body;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;uterus;whole body;cerebral cortex;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta; adipose tissue;white blood cells;atrioventricular node;skeletal muscle; 0.56735 0.09512 -0.025608647 51.91672564 44.99636 1.28850 FKBP6 0.13060063873413 0.864707462357507 0.00469189890836331 FK506 binding protein 6 FUNCTION: Co-chaperone required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Acts as a co-chaperone via its interaction with HSP90 and is required for the piRNA amplification process, the secondary piRNA biogenesis. May be required together with HSP90 in removal of 16 nucleotide ping-pong by-products from Piwi complexes, possibly facilitating turnover of Piwi complexes (By similarity). {ECO:0000250}.; DISEASE: Note=Defects in FKBP6 may be a cause of azoospermia. A study based on 323 patients with azoospermia or severe oligozoospermia suggested an association between FKBP6 variants and azoospermia (PubMed:17307919). However, other studies suggest that defects in FKBP6 are not a common cause of non-obstructive azoospermia (PubMed:16227348). {ECO:0000269|PubMed:16227348, ECO:0000269|PubMed:17307919}.; TISSUE SPECIFICITY: Detected in all tissues examined, with higher expression in testis, heart, skeletal muscle, liver, and kidney.; unclassifiable (Anatomical System);medulla oblongata;lung;ovary;placenta;testis;cervix;brain; testis - interstitial;testis - seminiferous tubule;testis; 0.10589 0.13002 0.238945317 69.20853975 68.82594 1.71871 FKBP7 3.15602385489856e-05 0.346477747724784 0.653490692036667 FK506 binding protein 7 FUNCTION: PPIases accelerate the folding of proteins during protein synthesis.; . . unclassifiable (Anatomical System);meninges;heart;cartilage;colon;skeletal muscle;skin;bone marrow;uterus;prostate;pia mater;lung;frontal lobe;bone;placenta;pituitary gland;liver;testis;dura mater; . 0.06749 0.09204 -0.449946534 24.00330267 18.91851 0.65344 FKBP8 0.9787380986207 0.0212432716370972 1.86297422025165e-05 FK506 binding protein 8 FUNCTION: Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis. {ECO:0000269|PubMed:12510191, ECO:0000269|PubMed:15757646, ECO:0000269|PubMed:16176796}.; . TISSUE SPECIFICITY: Widely expressed. Highest levels seen in the brain. Highly abundant in the retina. {ECO:0000269|PubMed:18385096}.; myocardium;lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;bladder;brain;tonsil;heart;cartilage;tongue;blood;lens;skeletal muscle;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus;cerebellum; whole brain;amygdala;medulla oblongata;superior cervical ganglion;temporal lobe;caudate nucleus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.14814 0.16202 -0.578583623 18.71903751 316.31545 3.77722 FKBP9 0.072366214136072 0.925022056712653 0.00261172915127463 FK506 binding protein 9 FUNCTION: PPIases accelerate the folding of proteins during protein synthesis.; . . smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;brain;heart;cartilage;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;duodenum;amnion;head and neck;kidney;stomach;aorta; . 0.47569 0.11062 0.130533008 63.35810333 148.62583 2.65937 FKBP9P1 . . . FK506 binding protein 9 pseudogene 1 . . . . . 0.23971 . . . . . FKBP10 0.000807424942436765 0.983229411361435 0.0159631636961284 FK506 binding protein 10 FUNCTION: PPIases accelerate the folding of proteins during protein synthesis.; DISEASE: Osteogenesis imperfecta 11 (OI11) [MIM:610968]: A form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI11 is an autosomal recessive form. {ECO:0000269|PubMed:20362275, ECO:0000269|PubMed:20839288, ECO:0000269|PubMed:22949511}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bruck syndrome 1 (BRKS1) [MIM:259450]: A disease characterized by generalized osteopenia, congenital joint contractures, fragile bones with onset of fractures in infancy or early childhood, short stature, severe limb deformity, progressive scoliosis, and pterygia. {ECO:0000269|PubMed:20839288, ECO:0000269|PubMed:22949511}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;adrenal medulla;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;thyroid;pituitary gland;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pineal body;urinary;blood;lens;breast;bile duct;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;duodenum;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;smooth muscle;heart;trigeminal ganglion; 0.44644 0.10813 -0.751322189 13.71196037 103.41854 2.19663 FKBP11 2.22757446059631e-05 0.490772658169189 0.509205066086205 FK506 binding protein 11 FUNCTION: PPIases accelerate the folding of proteins during protein synthesis.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;urinary;adrenal cortex;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach; pancreas;prostate;trachea;white blood cells; 0.36875 0.12101 -0.339715008 30.06605331 8.52455 0.31325 FKBP14 4.19320787675072e-05 0.396481259087196 0.603476808834036 FK506 binding protein 14 FUNCTION: PPIases accelerate the folding of proteins during protein synthesis.; DISEASE: Ehlers-Danlos syndrome, with progressive kyphoscoliosis, myopathy, and hearing loss (EDSKMH) [MIM:614557]: A syndrome with features of Ehlers-Danlos syndrome types VIA and VIB on the one hand, and the collagen VI-related congenital myopathies Ullrich congenital muscular dystrophy and Bethlem myopathy on the other hand. Clinically, this disorder is characterized by the following features: severe generalized hypotonia at birth with marked muscle weakness that improve in infancy; early-onset progressive kyphoscoliosis; joint hypermobility without contractures; hyperelastic skin with follicular hyperkeratosis, easy bruising, and occasional abnormal scarring; myopathy; hearing impairment, which is predominantly sensorineural; normal ratio of lysyl pyridinoline to hydroxylysyl pyridinoline (LP/HP) in urine. {ECO:0000269|PubMed:22265013}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;colon;skin;bone marrow;prostate;whole body;cerebral cortex;endometrium;larynx;thyroid;bone;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;pharynx;blood;breast;lung;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.17135 0.11614 -0.161524709 41.6430762 37.3396 1.11342 FKBP15 1.84755802385896e-07 0.999934489182673 6.53260615248033e-05 FK506 binding protein 15 FUNCTION: May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule- based movement. {ECO:0000250, ECO:0000269|PubMed:19121306}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.62404 0.09599 0.211232079 67.53951404 4394.82714 13.24713 FKBPL 5.3549944756646e-05 0.680050583135255 0.319895866919988 FK506 binding protein like FUNCTION: May be involved in response to X-ray. Regulates p21 protein stability by binding to Hsp90 and p21. {ECO:0000269|PubMed:15664193}.; . TISSUE SPECIFICITY: Ubiquitously expressed with higher levels in testis. {ECO:0000269|PubMed:15664193}.; . . 0.20032 . 0.21689899 68.12927577 1055.64821 6.23778 FKRP 0.000382800164368902 0.393814367980436 0.605802831855195 fukutin related protein FUNCTION: Transferase involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine- beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. {ECO:0000269|PubMed:25279699}.; DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A5 (MDDGA5) [MIM:613153]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with cobblestone lissencephaly and other brain anomalies, eye malformations, profound mental retardation, and death usually in the first years of life. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease. {ECO:0000269|PubMed:15121789}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Muscular dystrophy-dystroglycanopathy congenital with or without mental retardation B5 (MDDGB5) [MIM:606612]: A congenital muscular dystrophy characterized by a severe phenotype with inability to walk, muscle hypertrophy, marked elevation of serum creatine kinase, secondary deficiency of laminin alpha2, and a marked reduction in alpha-dystroglycan expression. Only a subset of affected individuals have brain involvements. {ECO:0000269|PubMed:11592034, ECO:0000269|PubMed:12654965, ECO:0000269|PubMed:12666124, ECO:0000269|PubMed:14652796, ECO:0000269|PubMed:17336067}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C5 (MDDGC5) [MIM:607155]: An autosomal recessive degenerative myopathy with age of onset ranging from childhood to adult life, and variable severity. Clinical features include proximal muscle weakness, waddling gait, calf hypertrophy, cardiomyopathy and respiratory insufficiency. A reduction of alpha-dystroglycan and laminin alpha-2 expression can be observed on skeletal muscle biopsy from MDDGC5 patients. {ECO:0000269|PubMed:11741828, ECO:0000269|PubMed:12666124, ECO:0000269|PubMed:14523375, ECO:0000269|PubMed:14647208, ECO:0000269|PubMed:23800702}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly in skeletal muscle, placenta, and heart and relatively weakly in brain, lung, liver kidney and pancreas.; unclassifiable (Anatomical System);islets of Langerhans;skeletal muscle;retina;prostate;whole body;lung;endometrium;epididymis;bone;placenta;duodenum;testis;germinal center;kidney;brain;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle; 0.16424 0.28737 . . 139.62484 2.57619 FKTN 0.000192375264435551 0.974989911177295 0.024817713558269 fukutin FUNCTION: Glycosyltransferase involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine- beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. May interact with and reinforce a large complex encompassing the outside and inside of muscle membranes. Could be involved in brain development. {ECO:0000269|PubMed:25279699}.; DISEASE: Muscular dystrophy-dystroglycanopathy congenital without mental retardation B4 (MDDGB4) [MIM:613152]: An autosomal recessive disorder characterized by congenital muscular dystrophy and evidence of dystroglycanopathy. Features included increased serum creatine kinase, generalized weakness, mild white matter changes on brain MRI, and absence of mental retardation. {ECO:0000269|PubMed:14627679, ECO:0000269|PubMed:18177472, ECO:0000269|PubMed:19179078, ECO:0000269|PubMed:19299310}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C4 (MDDGC4) [MIM:611588]: An autosomal recessive degenerative myopathy characterized by progressive weakness of the pelvic and shoulder girdle muscles, and elevated serum creatine kinase. MDDGC4 has no brain involvement and a remarkable clinical response to corticosteroids. {ECO:0000269|PubMed:17044012, ECO:0000269|PubMed:19342235}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1X (CMD1X) [MIM:611615]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:17036286}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed with highest expression in brain, heart, pancreas and skeletal muscle. Expressed at similar levels in control fetal and adult brain, but is much reduced in Fukuyama-type congenital dystrophy (FCMD) brains. Expressed in migrating neurons, including Cajar-Retzius cells and adult cortical neurons, as well as hippocampal pyramidal cells and cerebellar Purkinje cells. No expression observed in the glia limitans, the subpial astrocytes (which contribute to basement membrane formation) or other glial cells. In the FCMD brain, neurons in regions with no dysplasia show fair expression, whereas transcripts are nearly undetectable in the overmigrated dysplastic region. {ECO:0000269|PubMed:11115853}.; unclassifiable (Anatomical System);smooth muscle;cartilage;heart;lacrimal gland;islets of Langerhans;parathyroid;skin;uterus;pancreas;whole body;lung;visual apparatus;liver;testis;amniotic fluid;germinal center;kidney;brain;bladder; amygdala;medulla oblongata;prefrontal cortex;caudate nucleus;pons;parietal lobe;cingulate cortex; 0.09504 0.38939 0.576916344 82.25406936 2081.26605 8.40460 FLAD1 0.0917935111458052 0.906439743472951 0.00176674538124356 flavin adenine dinucleotide synthetase 1 FUNCTION: Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;larynx;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;liver;pons;trigeminal ganglion;skeletal muscle; 0.11392 0.23178 -1.043396569 7.71408351 87.62766 1.99904 FLCN 0.958489798196264 0.041506184015502 4.01778823409988e-06 folliculin FUNCTION: May be a tumor suppressor. May be involved in energy and/or nutrient sensing through the AMPK and mTOR signaling pathways. May regulate phosphorylation of RPS6KB1. {ECO:0000269|PubMed:12204536, ECO:0000269|PubMed:17028174, ECO:0000269|PubMed:18663353}.; DISEASE: Birt-Hogg-Dube syndrome (BHD) [MIM:135150]: A rare autosomal dominant genodermatosis characterized by hair follicle hamartomas (fibrofolliculomas), kidney tumors, and spontaneous pneumothorax. Fibrofolliculomas are part of the triad of Birt- Hogg-Dube syndrome skin lesions that also includes trichodiscomas and acrochordons. Onset of this dermatologic condition is invariably in adulthood. Birt-Hogg-Dube syndrome is associated with a variety of histologic types of renal tumors, including chromophobe renal cell carcinoma (RCC), benign renal oncocytoma, clear-cell RCC and papillary type I RCC. Multiple lipomas, angiolipomas, and parathyroid adenomas are also seen in Birt-Hogg- Dube syndrome patients. {ECO:0000269|PubMed:12204536, ECO:0000269|PubMed:15852235, ECO:0000269|PubMed:18234728, ECO:0000269|PubMed:19785621}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Primary spontaneous pneumothorax (PSP) [MIM:173600]: Condition in which air is present in the pleural space in the absence of a precipitating event, such as trauma or lung disease. This results in secondary collapse of the lung, either partially or completely, and some degree of hypoxia. PSP is relatively common, with an incidence between 7.4-18/100'000 for men and 1.2- 6/100'000 for women and a dose-dependent, increased risk among smokers. Most cases are sporadic, typically occurring in tall, thin men aged 10-30 years and generally while at rest. Familial PSP is rarer and usually is inherited as an autosomal dominant condition with reduced penetrance, although X-linked recessive and autosomal recessive inheritance have also been suggested. {ECO:0000269|PubMed:15657874, ECO:0000269|PubMed:18505456, ECO:0000269|PubMed:18579543}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Renal cell carcinoma (RCC) [MIM:144700]: Renal cell carcinoma is a heterogeneous group of sporadic or hereditary carcinoma derived from cells of the proximal renal tubular epithelium. It is subclassified into clear cell renal carcinoma (non-papillary carcinoma), papillary renal cell carcinoma, chromophobe renal cell carcinoma, collecting duct carcinoma with medullary carcinoma of the kidney, and unclassified renal cell carcinoma. Clear cell renal cell carcinoma is the most common subtype. {ECO:0000269|PubMed:18794106}. Note=The gene represented in this entry may be involved in disease pathogenesis.; TISSUE SPECIFICITY: Expressed in most tissues tested, including skin, lung, kidney, heart, testis and stomach. {ECO:0000269|PubMed:12204536}.; unclassifiable (Anatomical System);islets of Langerhans;colon;blood;skin;skeletal muscle;bone marrow;breast;pancreas;prostate;lung;frontal lobe;synovium;placenta;bone;testis;kidney;brain; skeletal muscle; 0.21576 0.17241 -0.198338176 39.17197452 30.47814 0.97088 FLG . . . filaggrin FUNCTION: Aggregates keratin intermediate filaments and promotes disulfide-bond formation among the intermediate filaments during terminal differentiation of mammalian epidermis.; DISEASE: Ichthyosis vulgaris (VI) [MIM:146700]: The most common form of ichthyosis inherited as an autosomal dominant trait. It is characterized by palmar hyperlinearity, keratosis pilaris and a fine scale that is most prominent over the lower abdomen, arms, and legs. Ichthyosis vulgaris is characterized histologically by absent or reduced keratohyalin granules in the epidermis and mild hyperkeratosis. The disease can be associated with frequent asthma, eczema or hay fever. {ECO:0000269|PubMed:16444271}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dermatitis atopic 2 (ATOD2) [MIM:605803]: Atopic dermatitis is a complex, inflammatory disease with multiple alleles at several loci thought to be involved in the pathogenesis. It commonly begins in infancy or early childhood and is characterized by a chronic relapsing form of skin inflammation, a disturbance of epidermal barrier function that culminates in dry skin, and IgE-mediated sensitization to food and environmental allergens. It is manifested by lichenification, excoriation, and crusting, mainly on the flexural surfaces of the elbow and knee. {ECO:0000269|PubMed:16550169, ECO:0000269|PubMed:16815158, ECO:0000269|PubMed:17030239, ECO:0000269|PubMed:17291859}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in skin, thymus, stomach, tonsils, testis, placenta, kidney, pancreas, mammary gland, bladder, thyroid, salivary gland and trachea, but not detected in heart, brain, liver, lung, bone marrow, small intestine, spleen, prostate, colon, or adrenal gland (PubMed:19384417). In the skin, mainly expressed in stratum granulosum of the epidermis (PubMed:1429717) (PubMed:19384417). {ECO:0000269|PubMed:1429717, ECO:0000269|PubMed:19384417}.; unclassifiable (Anatomical System);endometrium;oral cavity; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.08975 . 24.30246465 99.98820477 16458.42079 27.35022 FLG-AS1 . . . FLG antisense RNA 1 . . . . . . . . . . . FLG2 4.64992449263283e-41 1.05381705529679e-07 0.999999894618294 filaggrin family member 2 . . TISSUE SPECIFICITY: Expressed in skin, thymus, stomach and placenta, but not detected in heart, brain, liver, lung, bone marrow, small intestine, spleen, prostate, colon, adrenal gland, kidney, pancreas, mammary gland, bladder, thyroid, salivary gland and trachea. Weakly expressed in esophagus, tonsils and testis (at protein level). In the skin, strongly expressed in the upper stratum granulosum and lower stratum corneum, but not detected in the upper stratum corneum (at protein level) (PubMed:19384417) (PubMed:21531719). In scalp hair follicles, mainly restricted within the granular and cornified cells surrounding the infundibular outer root sheath, with weak expression in central and proximal outer root sheath (at protein level). Tends to be down-regulated in sporiatic lesions compared to non-lesional skin inthe same patients (PubMed:19384417). {ECO:0000269|PubMed:19384417, ECO:0000269|PubMed:21531719}.; . . 0.10445 . 2.276748373 98.2661005 6513.79854 16.94727 FLI1 0.819814084378667 0.180006652530668 0.000179263090664846 Fli-1 proto-oncogene, ETS transcription factor FUNCTION: Sequence-specific transcriptional activator. Recognizes the DNA sequence 5'-C[CA]GGAAGT-3'.; DISEASE: Ewing sarcoma (ES) [MIM:612219]: A highly malignant, metastatic, primitive small round cell tumor of bone and soft tissue that affects children and adolescents. It belongs to the Ewing sarcoma family of tumors, a group of morphologically heterogeneous neoplasms that share the same cytogenetic features. They are considered neural tumors derived from cells of the neural crest. Ewing sarcoma represents the less differentiated form of the tumors. {ECO:0000269|PubMed:1522903, ECO:0000269|PubMed:1765382}. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving FLI1 is found in patients with Erwing sarcoma. Translocation t(11;22)(q24;q12) with EWSR1. {ECO:0000269|PubMed:1522903, ECO:0000269|PubMed:1765382}.; . unclassifiable (Anatomical System);amygdala;lymphoreticular;lymph node;blood;skeletal muscle;bone marrow;pancreas;prostate;lung;adrenal gland;thyroid;placenta;liver;testis;head and neck;spleen;brain; dorsal root ganglion;superior cervical ganglion;white blood cells;ciliary ganglion;atrioventricular node;whole blood;trigeminal ganglion;skeletal muscle; 0.61450 . -0.890882376 10.30313753 37.50769 1.11686 FLII 3.31006863649052e-06 0.999991565815696 5.12411566728952e-06 flightless I actin binding protein FUNCTION: May play a role as coactivator in transcriptional activation by hormone-activated nuclear receptors (NR) and acts in cooperation with NCOA2 and CARM1. Involved in estrogen hormone signaling. Involved in early embryonic development (By similarity). May play a role in regulation of cytoskeletal rearrangements involved in cytokinesis and cell migration, by inhibiting Rac1-dependent paxillin phosphorylation. {ECO:0000250, ECO:0000269|PubMed:14966289}.; . TISSUE SPECIFICITY: Strongest expression in skeletal muscle with high expression also in the heart and lung. {ECO:0000269|PubMed:9525888}.; myocardium;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;germinal center;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;head and neck;kidney;stomach;aorta;cerebellum; testis - interstitial;lung;heart;testis;trigeminal ganglion;skeletal muscle; 0.32333 0.23356 -2.936657799 0.554376032 332.27693 3.87529 FLNA 0.999999987607637 1.2392363207874e-08 2.38657877180705e-21 filamin A FUNCTION: Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface- localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis. {ECO:0000250, ECO:0000269|PubMed:22121117}.; DISEASE: Periventricular nodular heterotopia 1 (PVNH1) [MIM:300049]: A developmental disorder characterized by the presence of periventricular nodules of cerebral gray matter, resulting from a failure of neurons to migrate normally from the lateral ventricular proliferative zone, where they are formed, to the cerebral cortex. PVNH1 is an X-linked dominant form. Heterozygous females have normal intelligence but suffer from seizures and various manifestations outside the central nervous system, especially related to the vascular system. Hemizygous affected males die in the prenatal or perinatal period. {ECO:0000269|PubMed:11532987, ECO:0000269|PubMed:11914408, ECO:0000269|PubMed:12410386, ECO:0000269|PubMed:15249610, ECO:0000269|PubMed:15668422, ECO:0000269|PubMed:15994863, ECO:0000269|PubMed:16299064}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Otopalatodigital syndrome 1 (OPD1) [MIM:311300]: X-linked dominant multiple congenital anomalies disease mainly characterized by a generalized skeletal dysplasia, mild mental retardation, hearing loss, cleft palate, and typical facial anomalies. OPD1 belongs to a group of X-linked skeletal dysplasias known as oto-palato-digital syndrome spectrum disorders that also include OPD2, Melnick-Needles syndrome (MNS), and frontometaphyseal dysplasia (FMD). Remodeling of the cytoskeleton is central to the modulation of cell shape and migration. FLNA is a widely expressed protein that regulates re-organization of the actin cytoskeleton by interacting with integrins, transmembrane receptor complexes and second messengers. Males with OPD1 have cleft palate, malformations of the ossicles causing deafness and milder bone and limb defects than those associated with OPD2. Obligate female carriers of mutations causing both OPD1 and OPD2 have variable (often milder) expression of a similar phenotypic spectrum. {ECO:0000269|PubMed:12612583, ECO:0000269|PubMed:15940695}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Otopalatodigital syndrome 2 (OPD2) [MIM:304120]: Congenital bone disorder that is characterized by abnormally modeled, bowed bones, small or absent first digits and, more variably, cleft palate, posterior fossa brain anomalies, omphalocele and cardiac defects. {ECO:0000269|PubMed:12612583, ECO:0000269|PubMed:17431908}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Frontometaphyseal dysplasia (FMD) [MIM:305620]: Congenital bone disease characterized by supraorbital hyperostosis, deafness and digital anomalies. {ECO:0000269|PubMed:12612583, ECO:0000269|PubMed:16596676}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Melnick-Needles syndrome (MNS) [MIM:309350]: Severe congenital bone disorder characterized by typical facies (exophthalmos, full cheeks, micrognathia and malalignment of teeth), flaring of the metaphyses of long bones, s-like curvature of bones of legs, irregular constrictions in the ribs, and sclerosis of base of skull. {ECO:0000269|PubMed:12612583}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Intestinal pseudoobstruction, neuronal, chronic idiopathic, X-linked (IPOX) [MIM:300048]: A disease characterized by a severe abnormality of gastrointestinal motility due to primary qualitative defects of enteric ganglia and nerve fibers. Affected individuals manifest recurrent signs of intestinal obstruction in the absence of any mechanical lesion. {ECO:0000269|PubMed:17357080}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: FG syndrome 2 (FGS2) [MIM:300321]: FG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation. {ECO:0000269|PubMed:17632775}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Terminal osseous dysplasia (TOD) [MIM:300244]: A rare X- linked dominant male-lethal disease characterized by skeletal dysplasia of the limbs, pigmentary defects of the skin and recurrent digital fibroma during infancy. A significant phenotypic variability is observed in affected females. {ECO:0000269|PubMed:20598277}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiac valvular dysplasia X-linked (CVDX) [MIM:314400]: A rare X-linked heart disease characterized by mitral and/or aortic valve regurgitation. The histologic features include fragmentation of collagenous bundles within the valve fibrosa and accumulation of proteoglycans, which produces excessive valve tissue leading to billowing of the valve leaflets. {ECO:0000269|PubMed:17190868}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in FLNA may be a cause of macrothrombocytopenia, a disorder characterized by subnormal levels of blood platelets. Blood platelets are abnormally enlarged (PubMed:21960593). {ECO:0000269|PubMed:21960593}.; DISEASE: Congenital short bowel syndrome, X-linked (CSBSX) [MIM:300048]: A disease characterized by a shortened small intestine, and malabsorption. The mean length of the small intestine in affected individuals is approximately 50 cm, compared with a normal length at birth of 190-280 cm. It is associated with significant mortality and morbidity. Infants usually present with failure to thrive, recurrent vomiting, and diarrhea. {ECO:0000269|PubMed:23037936}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;stomach;thymus; uterus;prostate;adipose tissue;lung;heart;appendix;white blood cells;whole blood; 0.74137 0.64395 -3.240384062 0.442321302 815.2172 5.61188 FLNB 0.00243124047488239 0.99756875952188 3.23783118333372e-12 filamin B FUNCTION: Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro.; DISEASE: Note=Interaction with FLNA may compensate for dysfunctional FLNA homodimer in the periventricular nodular heterotopia (PVNH) disorder.; DISEASE: Atelosteogenesis 1 (AO1) [MIM:108720]: A lethal chondrodysplasia characterized by distal hypoplasia of the humeri and femurs, hypoplasia of the mid-thoracic spine, occasionally complete lack of ossification of single hand bones, and the finding in cartilage of multiple degenerated chondrocytes which are encapsulated in fibrous tissue. {ECO:0000269|PubMed:14991055}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Atelosteogenesis 3 (AO3) [MIM:108721]: A short-limb lethal skeletal dysplasia with vertebral abnormalities, disharmonious skeletal maturation, poorly modeled long bones and joint dislocations. Recurrent respiratory insufficiency and/or infections usually result in early death. {ECO:0000269|PubMed:14991055}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Boomerang dysplasia (BOOMD) [MIM:112310]: A perinatal lethal osteochondrodysplasia characterized by absence or underossification of the limb bones and vertebrae. Patients manifest dwarfism with short, bowed, rigid limbs and characteristic facies. Boomerang dysplasia is distinguished from atelosteogenesis on the basis of a more severe defect in mineralization, with complete absence of ossification in some limb elements and vertebral segments. {ECO:0000269|PubMed:15994868}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Larsen syndrome (LRS) [MIM:150250]: An osteochondrodysplasia characterized by large-joint dislocations and characteristic craniofacial abnormalities. The cardinal features of the condition are dislocations of the hip, knee and elbow joints, with equinovarus or equinovalgus foot deformities. Spatula-shaped fingers, most marked in the thumb, are also present. Craniofacial anomalies include hypertelorism, prominence of the forehead, a depressed nasal bridge, and a flattened midface. Cleft palate and short stature are often associated features. Spinal anomalies include scoliosis and cervical kyphosis. Hearing loss is a well-recognized complication. {ECO:0000269|PubMed:14991055, ECO:0000269|PubMed:16801345}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spondylocarpotarsal synostosis syndrome (SCT) [MIM:272460]: Disorder characterized by short stature and vertebral, carpal and tarsal fusions. {ECO:0000269|PubMed:14991055}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Isoform 1 and isoform 2 are expressed in placenta, bone marrow, brain, umbilical vein endothelial cells (HUVEC), retina and skeletal muscle. Isoform 1 is predominantly expressed in prostate, uterus, liver, thyroid, stomach, lymph node, small intestine, spleen, skeletal muscle, kidney, placenta, pancreas, heart, lung, platelets, endothelial cells, megakaryocytic and erythroleukemic cell lines. Isoform 2 is predominantly expressed in spinal cord, platelet and Daudi cells. Also expressed in thyroid adenoma, neurofibrillary tangles (NFT), senile plaques in the hippocampus and cerebral cortex in Alzheimer disease (AD). Isoform 3 and isoform 6 are expressed predominantly in lung, heart, skeletal muscle, testis, spleen, thymus and leukocytes. Isoform 4 and isoform 5 are expressed in heart. {ECO:0000269|PubMed:11807098, ECO:0000269|PubMed:8327473, ECO:0000269|PubMed:9651345, ECO:0000269|PubMed:9694715}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;ciliary body;bladder;brain;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;greater omentum;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;oral cavity;bile duct;pancreas;lung;nasopharynx;placenta;hypopharynx;amnion;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;lung;placenta;skeletal muscle; 0.45177 0.21590 -1.444990676 3.939608398 1028.35714 6.16096 FLNB-AS1 . . . FLNB antisense RNA 1 . . . . . . . . . . . FLNC 0.999503524836351 0.000496475163648908 9.04867806423254e-18 filamin C FUNCTION: Muscle-specific filamin, which plays a central role in muscle cells, probably by functioning as a large actin-cross- linking protein. May be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. Critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers.; DISEASE: Myopathy, myofibrillar, 5 (MFM5) [MIM:609524]: A neuromuscular disorder, usually with an adult onset, characterized by focal myofibrillar destruction, pathological cytoplasmic protein aggregations, and clinical features of a limb-girdle myopathy. {ECO:0000269|PubMed:15929027}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myopathy, distal, 4 (MPD4) [MIM:614065]: A slowly progressive muscular disorder characterized by distal muscle weakness and atrophy affecting the upper and lower limbs. Onset occurs around the third to fourth decades of life, and patients remain ambulatory even after long disease duration. Muscle biopsy shows non-specific changes with no evidence of rods, necrosis, or inflammation. {ECO:0000269|PubMed:21620354}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in striated muscles. Weakly expressed in thyroid, fetal brain, fetal lung, retina, spinal cord and bone marrow. Not expressed in testis, pancreas, adrenal gland, placenta, liver and kidney. {ECO:0000269|PubMed:11038172, ECO:0000269|PubMed:7689010, ECO:0000269|PubMed:9791010}.; myocardium;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;testis;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;tongue;spinal cord;muscle;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;epididymis;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;peripheral nerve; heart;tongue;fetal thyroid;trigeminal ganglion;skeletal muscle; 0.30916 0.28051 -3.641201716 0.288983251 941.7091 5.94968 FLOT1 0.0152734382576229 0.983567583267384 0.00115897847499287 flotillin 1 FUNCTION: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.; . . . . 0.12551 0.19349 -0.516085732 21.20193442 25.27793 0.82668 FLOT2 0.0172343470815513 0.97801585329628 0.00474979962216862 flotillin 2 FUNCTION: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles. May be involved in epidermal cell adhesion and epidermal structure and function.; . TISSUE SPECIFICITY: In skin, expressed in epidermis and epidermal appendages but not in dermis. Expressed in all layers of the epidermis except the basal layer. In hair follicles, expressed in the suprabasal layer but not the basal layer. Also expressed in melanoma and carcinoma cell lines, fibroblasts and foreskin melanocytes.; . . 0.59010 0.19444 -0.181750739 40.15687662 133.59956 2.51118 FLRT1 0.546319766734407 0.439707277682029 0.0139729555835647 fibronectin leucine rich transmembrane protein 1 FUNCTION: Plays a role in fibroblast growth factor-mediated signaling cascades that lead to the activation of MAP kinases. Promotes neurite outgrowth via FGFR1-mediated activation of downstream MAP kinases. Promotes an increase both in neurite number and in neurite length. May play a role in cell-cell adhesion and cell guidance via its interaction with ADGRL1/LPHN1 and ADGRL3. {ECO:0000250|UniProtKB:Q6RKD8}.; . TISSUE SPECIFICITY: Expressed in kidney and brain. {ECO:0000269|PubMed:10644439}.; unclassifiable (Anatomical System);prostate;optic nerve;larynx;macula lutea;visual apparatus;head and neck;fovea centralis;choroid;lens;brain;mammary gland;retina; superior cervical ganglion;pons;trigeminal ganglion;parietal lobe; 0.06239 0.11168 -0.705410796 14.77942911 67.31626 1.69830 FLRT2 0.894038333573428 0.105747558350016 0.000214108076556408 fibronectin leucine rich transmembrane protein 2 FUNCTION: Functions in cell-cell adhesion, cell migration and axon guidance. Mediates cell-cell adhesion via its interactions with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells. May play a role in the migration of cortical neurons during brain development via its interaction with UNC5D. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5D, and possibly also other UNC-5 family members. Plays a role in fibroblast growth factor-mediated signaling cascades. Required for normal organization of the cardiac basement membrane during embryogenesis, and for normal embryonic epicardium and heart morphogenesis. {ECO:0000250|UniProtKB:Q8BLU0}.; . TISSUE SPECIFICITY: Expressed in pancreas, skeletal muscle, brain, and heart. {ECO:0000269|PubMed:10644439}.; ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;optic nerve;whole body;cochlea;bone;testis;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;spinal cord;lens;skeletal muscle;lung;placenta;macula lutea;liver;spleen;head and neck; occipital lobe;subthalamic nucleus;superior cervical ganglion;fetal brain;prefrontal cortex;globus pallidus;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe; 0.22410 0.11009 -0.044015879 50.44821892 1227.80506 6.62629 FLRT3 0.988394618338844 0.0116011729908838 4.20867027233278e-06 fibronectin leucine rich transmembrane protein 3 FUNCTION: Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners. Plays a role in the spatial organization of brain neurons. Plays a role in vascular development in the retina (By similarity). Plays a role in cell-cell adhesion via its interaction with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells (PubMed:26235030). Interaction with the intracellular domain of ROBO1 mediates axon attraction towards cells expressing NTN1. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5B, and possibly also other UNC-5 family members (By similarity). Promotes neurite outgrowth (in vitro) (PubMed:14706654). Mediates cell-cell contacts that promote an increase both in neurite number and in neurite length. Plays a role in the regulation of the density of glutamaergic synapses. Plays a role in fibroblast growth factor-mediated signaling cascades. Required for normal morphogenesis during embryonic development, but not for normal embryonic patterning. Required for normal ventral closure, headfold fusion and definitive endoderm migration during embryonic development. Required for the formation of a normal basement membrane and the maintenance of a normal anterior visceral endoderm during embryonic development (By similarity). {ECO:0000250|UniProtKB:B1H234, ECO:0000250|UniProtKB:Q8BGT1, ECO:0000269|PubMed:14706654, ECO:0000269|PubMed:26235030}.; DISEASE: Hypogonadotropic hypogonadism 21 with or without anosmia (HH21) [MIM:615271]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:23643382}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. Some patients carrying mutations in FLRT3 also have a mutation in another HH-associated gene including FGFR1, HS6ST1 and FGF17 (PubMed:23643382). {ECO:0000269|PubMed:23643382}.; TISSUE SPECIFICITY: Expressed in kidney, brain, pancreas, skeletal muscle, lung, liver, placenta, and heart. {ECO:0000269|PubMed:10644439}.; unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;parathyroid;skin;skeletal muscle;uterus;prostate;lung;frontal lobe;cochlea;larynx;liver;testis;head and neck;spleen;kidney;brain;bladder;stomach; superior cervical ganglion; 0.43584 0.12222 -0.089927255 46.99221515 2304.67459 8.89235 FLT1 0.997806027350573 0.00219397264842896 9.97954938585104e-13 fms related tyrosine kinase 1 FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro). Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Likewise, isoforms lacking a transmembrane domain, such as isoform 2, isoform 3 and isoform 4, may function as decoy receptors for VEGFA. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC and YES1, and may also phosphorylate CBL. Isoform 1 phosphorylates PLCG. Promotes phosphorylation of AKT1 at 'Ser-473'. Promotes phosphorylation of PTK2/FAK1. Isoform 7 has a truncated kinase domain; it increases phosphorylation of SRC at 'Tyr-418' by unknown means and promotes tumor cell invasion. {ECO:0000269|PubMed:11141500, ECO:0000269|PubMed:11312102, ECO:0000269|PubMed:11811792, ECO:0000269|PubMed:12796773, ECO:0000269|PubMed:14633857, ECO:0000269|PubMed:15735759, ECO:0000269|PubMed:16685275, ECO:0000269|PubMed:18079407, ECO:0000269|PubMed:18515749, ECO:0000269|PubMed:18583712, ECO:0000269|PubMed:18593464, ECO:0000269|PubMed:20512933, ECO:0000269|PubMed:20551949, ECO:0000269|PubMed:21752276, ECO:0000269|PubMed:7824266, ECO:0000269|PubMed:8248162, ECO:0000269|PubMed:8605350, ECO:0000269|PubMed:9299537}.; DISEASE: Note=Can contribute to cancer cell survival, proliferation, migration, and invasion, and tumor angiogenesis and metastasis. May contribute to cancer pathogenesis by promoting inflammatory responses and recruitment of tumor-infiltrating macrophages.; DISEASE: Note=Abnormally high expression of soluble isoforms (isoform 2, isoform 3 or isoform 4) may be a cause of preeclampsia.; TISSUE SPECIFICITY: Detected in normal lung, but also in placenta, liver, kidney, heart and brain tissues. Specifically expressed in most of the vascular endothelial cells, and also expressed in peripheral blood monocytes. Isoform 2 is strongly expressed in placenta. Isoform 3 is expressed in corneal epithelial cells (at protein level). Isoform 3 is expressed in vascular smooth muscle cells (VSMC). {ECO:0000269|PubMed:18515749, ECO:0000269|PubMed:20512933}.; unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;parathyroid;blood;fovea centralis;skeletal muscle;retina;uterus;prostate;whole body;lung;thyroid;placenta;macula lutea;liver;testis;spleen;kidney;brain; superior cervical ganglion;placenta;atrioventricular node;cingulate cortex;skeletal muscle; 0.24106 0.64822 -1.521247944 3.44420854 121.53409 2.40056 FLT1P1 . . . fms related tyrosine kinase 1 pseudogene 1 . . . . . . . . . . . FLT3 0.609047700982651 0.390952174329172 1.24688176891552e-07 fms related tyrosine kinase 3 FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine FLT3LG and regulates differentiation, proliferation and survival of hematopoietic progenitor cells and of dendritic cells. Promotes phosphorylation of SHC1 and AKT1, and activation of the downstream effector MTOR. Promotes activation of RAS signaling and phosphorylation of downstream kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation of FES, FER, PTPN6/SHP, PTPN11/SHP-2, PLCG1, and STAT5A and/or STAT5B. Activation of wild-type FLT3 causes only marginal activation of STAT5A or STAT5B. Mutations that cause constitutive kinase activity promote cell proliferation and resistance to apoptosis via the activation of multiple signaling pathways. {ECO:0000269|PubMed:10080542, ECO:0000269|PubMed:11090077, ECO:0000269|PubMed:14504097, ECO:0000269|PubMed:16266983, ECO:0000269|PubMed:16627759, ECO:0000269|PubMed:18490735, ECO:0000269|PubMed:20111072, ECO:0000269|PubMed:21067588, ECO:0000269|PubMed:21262971, ECO:0000269|PubMed:21516120, ECO:0000269|PubMed:7507245}.; DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. {ECO:0000269|PubMed:11090077, ECO:0000269|PubMed:11290608, ECO:0000269|PubMed:11442493, ECO:0000269|PubMed:14504097, ECO:0000269|PubMed:16266983, ECO:0000269|PubMed:18305215, ECO:0000269|PubMed:8946930, ECO:0000269|PubMed:9737679}. Note=The gene represented in this entry may be involved in disease pathogenesis. Somatic mutations that lead to constitutive activation of FLT3 are frequent in AML patients. These mutations fall into two classes, the most common being in-frame internal tandem duplications of variable length in the juxtamembrane region that disrupt the normal regulation of the kinase activity. Likewise, point mutations in the activation loop of the kinase domain can result in a constitutively activated kinase.; TISSUE SPECIFICITY: Detected in bone marrow, in hematopoietic stem cells, in myeloid progenitor cells and in granulocyte/macrophage progenitor cells (at protein level). Detected in bone marrow, liver, thymus, spleen and lymph node, and at low levels in kidney and pancreas. Highly expressed in T-cell leukemia. {ECO:0000269|PubMed:18490735, ECO:0000269|PubMed:7507245, ECO:0000269|PubMed:8394751, ECO:0000269|PubMed:8637232}.; unclassifiable (Anatomical System);lung;testis;kidney;stomach;bone marrow; superior cervical ganglion;atrioventricular node; 0.33642 0.35136 0.097358507 60.71597075 3420.34408 11.21944 FLT3LG 0.950828697992112 0.049022408835691 0.000148893172196815 fms related tyrosine kinase 3 ligand FUNCTION: Stimulates the proliferation of early hematopoietic cells by activating FLT3. Synergizes well with a number of other colony stimulating factors and interleukins.; . . unclassifiable (Anatomical System);pancreas;optic nerve;lymph node;macula lutea;visual apparatus;fovea centralis;choroid;kidney;lens;retina; whole blood; 0.24328 0.14299 -0.560178693 19.30879925 10.2966 0.37550 FLT4 0.999936678740361 6.33212596345212e-05 4.31714994113817e-15 fms related tyrosine kinase 4 FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFC and VEGFD, and plays an essential role in adult lymphangiogenesis and in the development of the vascular network and the cardiovascular system during embryonic development. Promotes proliferation, survival and migration of endothelial cells, and regulates angiogenic sprouting. Signaling by activated FLT4 leads to enhanced production of VEGFC, and to a lesser degree VEGFA, thereby creating a positive feedback loop that enhances FLT4 signaling. Modulates KDR signaling by forming heterodimers. The secreted isoform 3 may function as a decoy receptor for VEGFC and/or VEGFD and play an important role as a negative regulator of VEGFC-mediated lymphangiogenesis and angiogenesis. Binding of vascular growth factors to isoform 1 or isoform 2 leads to the activation of several signaling cascades; isoform 2 seems to be less efficient in signal transduction, because it has a truncated C-terminus and therefore lacks several phosphorylation sites. Mediates activation of the MAPK1/ERK2, MAPK3/ERK1 signaling pathway, of MAPK8 and the JUN signaling pathway, and of the AKT1 signaling pathway. Phosphorylates SHC1. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3- kinase. Promotes phosphorylation of MAPK8 at 'Thr-183' and 'Tyr- 185', and of AKT1 at 'Ser-473'. {ECO:0000269|PubMed:11532940, ECO:0000269|PubMed:15102829, ECO:0000269|PubMed:15474514, ECO:0000269|PubMed:16076871, ECO:0000269|PubMed:16452200, ECO:0000269|PubMed:17210781, ECO:0000269|PubMed:19610651, ECO:0000269|PubMed:19779139, ECO:0000269|PubMed:20224550, ECO:0000269|PubMed:20431062, ECO:0000269|PubMed:20445537, ECO:0000269|PubMed:21273538, ECO:0000269|PubMed:7675451, ECO:0000269|PubMed:8700872, ECO:0000269|PubMed:9435229}.; DISEASE: Lymphedema, hereditary, 1A (LMPH1A) [MIM:153100]: A chronic disabling condition which results in swelling of the extremities due to altered lymphatic flow. Patients with lymphedema suffer from recurrent local infections and physical impairment. {ECO:0000269|PubMed:10835628, ECO:0000269|PubMed:10856194, ECO:0000269|PubMed:16924388, ECO:0000269|PubMed:16965327, ECO:0000269|PubMed:17458866, ECO:0000269|PubMed:19289394, ECO:0000269|PubMed:26091405, ECO:0000269|PubMed:9817924}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hemangioma, capillary infantile (HCI) [MIM:602089]: A condition characterized by dull red, firm, dome-shaped hemangiomas, sharply demarcated from surrounding skin, usually presenting at birth or occurring within the first two or three months of life. They result from highly proliferative, localized growth of capillary endothelium and generally undergo regression and involution without scarring. {ECO:0000269|PubMed:11807987}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=Plays an important role in tumor lymphangiogenesis, in cancer cell survival, migration, and formation of metastases.; TISSUE SPECIFICITY: Detected in endothelial cells (at protein level). Widely expressed. Detected in fetal spleen, lung and brain. Detected in adult liver, muscle, thymus, placenta, lung, testis, ovary, prostate, heart, and kidney. {ECO:0000269|PubMed:1327515, ECO:0000269|PubMed:20224550, ECO:0000269|PubMed:7675451}.; unclassifiable (Anatomical System);lymph node;placenta;visual apparatus;testis;colon;brain;skeletal muscle; placenta; 0.19958 0.23555 0.707220641 85.53314461 835.41804 5.65903 FLVCR1 0.00037308554680706 0.954617557282145 0.0450093571710476 feline leukemia virus subgroup C cellular receptor 1 FUNCTION: Isoform 1: Heme transporter that exports cytoplasmic heme. It can also export coproporphyrin and protoporphyrin IX, which are both intermediate products in the heme biosynthetic pathway. Does not export bilirubin. Heme export depends on the presence of HPX and may be required to protect developing erythroid cells from heme toxicity. Heme export also provides protection from heme or ferrous iron toxicities in liver and brain. Causes susceptibility to FeLV-C in vitro. Required during erythtopoiesis to maintain intracellular free heme balance since in proerythroblasts, heme synthesis intensifies and it's accumulation is toxic for cells.; DISEASE: Posterior column ataxia with retinitis pigmentosa (PCARP) [MIM:609033]: A neurodegenerative syndrome beginning in infancy with areflexia and retinitis pigmentosa. Nyctalopia (night blindness) and peripheral visual field loss are usually evident during late childhood or teenage years, with subsequent progressive constriction of the visual fields and loss of central retinal function over time. A sensory ataxia caused by degeneration of the posterior columns of the spinal cord results in a loss of proprioceptive sensation that is clinically evident in the second decade of life and gradually progresses. Scoliosis, camptodactyly, achalasia, gastrointestinal dysmotility, and a sensory peripheral neuropathy are variable features of the disease. Affected individuals have no clinical or radiological evidence of cerebral or cerebellar involvement. {ECO:0000269|PubMed:21070897, ECO:0000269|PubMed:21267618}. Note=The disease is caused by mutations affecting the gene represented in this entry. Defective neuronal heme transmembrane export due to FLVCR1 mutations may abrogate the neuroprotective effects of neuroglobin and initiate an apoptotic cascade that results in the selective degeneration of photoreceptors in the neurosensory retina and sensory neurons in the posterior spinal cord.; TISSUE SPECIFICITY: Found all hematopoietic tissues including peripheral blood lymphocytes. Some expression is found in pancreas and kidney. {ECO:0000269|PubMed:10400745}.; . . 0.09758 0.11226 0.018483465 55.44939844 2854.4394 10.10746 FLVCR1-AS1 . . . FLVCR1 antisense RNA 1 (head to head) . . TISSUE SPECIFICITY: Expressed in a wide variety of tissues. {ECO:0000269|PubMed:11943475}.; unclassifiable (Anatomical System);skeletal muscle; . . . . . . . FLVCR2 0.000368276215601782 0.953864127588797 0.045767596195601 feline leukemia virus subgroup C cellular receptor family member 2 FUNCTION: Acts as an importer of heme. Also acts as a transporter for a calcium-chelator complex, important for growth and calcium metabolism. {ECO:0000269|PubMed:20823265}.; . TISSUE SPECIFICITY: Expressed in non-hematopoietic tissues, with relative abundant expression in brain, placenta, lung, liver and kidney. Also expressed in hematopoietic tissues (fetal liver, spleen, lymph node, thymus, leukocytes and bone marrow). Found in acidophil cells of the pituitary that secrete growth hormone and prolactin.; . . 0.23375 0.14729 0.352813824 74.49280491 939.09039 5.93921 FLYWCH1 . . . FLYWCH-type zinc finger 1 . . . myocardium;ovary;salivary gland;intestine;colon;fovea centralis;skin;retina;bone marrow;uterus;prostate;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;pineal body;muscle;urinary;adrenal cortex;pharynx;blood;lens;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;atrioventricular node; . 0.10918 -0.365622677 28.30856334 355.33706 3.98840 FLYWCH1P1 . . . FLYWCH-type zinc finger 1 pseudogene 1 . . . . . . . . . . . FLYWCH2 0.580537079882413 0.376185625225785 0.0432772948918026 FLYWCH family member 2 . . . ovary;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;stomach; whole brain; 0.06392 . 0.393270925 76.04977589 118.75585 2.37095 FMN1 1.72654491663651e-13 0.328979991025955 0.671020008973872 formin 1 FUNCTION: Plays a role in the formation of adherens junction and the polymerization of linear actin cables. {ECO:0000250}.; . . uterus;unclassifiable (Anatomical System);breast;lung;heart;endometrium;bone;liver;testis;brain;skin;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;subthalamic nucleus;occipital lobe;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.27195 0.10473 0.861555086 88.63529134 6822.84749 17.56030 FMN2 0.994502609230201 0.00549739072336863 4.64303005065204e-11 formin 2 FUNCTION: Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis (By similarity). Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization. Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress- induced cell cycle arrest. Protects cells against apoptosis by protecting CDKN1A against degradation. {ECO:0000250, ECO:0000269|PubMed:22330775, ECO:0000269|PubMed:23375502}.; DISEASE: Mental retardation, autosomal recessive 47 (MRT47) [MIM:616193]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT47 patients show delayed development, with cognition and speech more affected than motor skills. {ECO:0000269|PubMed:25480035}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed almost exclusively in the developing and mature central nervous system. {ECO:0000269|PubMed:10781961}.; unclassifiable (Anatomical System);ovary;hypothalamus;placenta;parathyroid;germinal center;brain; whole brain;amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;olfactory bulb;hypothalamus;pons;atrioventricular node;subthalamic nucleus;prefrontal cortex;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.10939 0.10224 0.411473843 76.55697098 3664.1256 11.76047 FMNL1 0.999687036181592 0.000312963813238273 5.17011796859924e-12 formin like 1 FUNCTION: May play a role in the control of cell motility and survival of macrophages (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. {ECO:0000250, ECO:0000269|PubMed:21834987}.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;bone;pituitary gland;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;kidney;stomach;thymus; white blood cells;whole blood; 0.38561 0.13099 -1.063626766 7.484076433 3176.17327 10.74104 FMNL2 0.996999397171698 0.00300060277598355 5.23178680141251e-11 formin like 2 FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics. {ECO:0000269|PubMed:21834987}.; . . ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;hypothalamus;adrenal cortex;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;olfactory bulb;hypothalamus;spinal cord;pons;atrioventricular node;caudate nucleus;prefrontal cortex;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.37448 . 0.135991087 63.61759849 191.04411 2.99833 FMNL3 0.356499503624211 0.643500313121553 1.83254235739549e-07 formin like 3 FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. Required for developmental angiogenesis (By similarity). In this process, required for microtubule reorganization and for efficient endothelial cell elongation. In quiescent endothelial cells, triggers rearrangement of the actin cytoskeleton, but does not alter microtubule alignement. {ECO:0000250|UniProtKB:Q6NXC0, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:22275430}.; . TISSUE SPECIFICITY: Expressed in endothelial cells. {ECO:0000269|PubMed:22275430}.; smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion;testis - interstitial;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.12501 0.10847 -1.017713296 8.103326256 188.83904 2.98373 FMO1 5.09733210470965e-07 0.850540322743909 0.14945916752288 flavin containing monooxygenase 1 FUNCTION: This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. Form I catalyzes the N-oxygenation of secondary and tertiary amines.; . TISSUE SPECIFICITY: Expressed mainly in fetal liver, adult kidney and, to a lesser extent, the intestine.; unclassifiable (Anatomical System);heart;colon;skin;skeletal muscle;uterus;whole body;lung;nasopharynx;placenta;liver;testis;spleen;germinal center;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;fetal liver;tongue;kidney;trigeminal ganglion;skeletal muscle; 0.50134 0.15488 1.087645262 91.8494928 396.22444 4.18178 FMO2 0.00129017983136937 0.960672054381535 0.0380377657870955 flavin containing monooxygenase 2 FUNCTION: Catalyzes the N-oxidation of certain primary alkylamines to their oximes via an N-hydroxylamine intermediate. Inactive toward certain tertiary amines, such as imipramine or chloropromazine. Can catalyze the S-oxidation of methimazole. The truncated form is catalytically inactive. {ECO:0000269|PubMed:9804831}.; . TISSUE SPECIFICITY: Expressed in lung (at protein level). Expressed predominantly in lung, and at a much lesser extent in kidney. Also expressed in fetal lung, but not in liver, kidney and brain. {ECO:0000269|PubMed:11042094, ECO:0000269|PubMed:9804831}.; ovary;sympathetic chain;parathyroid;skin;retina;prostate;thyroid;dura mater;spinal ganglion;artery;ciliary body;unclassifiable (Anatomical System);meninges;cartilage;pancreas;lung;pia mater;nasopharynx;placenta;trabecular meshwork;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11569 . 2.465816951 98.61405992 13453.86804 25.27896 FMO3 2.82794197226029e-09 0.156115313655022 0.843884683517036 flavin containing monooxygenase 3 FUNCTION: Involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. It N-oxygenates primary aliphatic alkylamines as well as secondary and tertiary amines. Plays an important role in the metabolism of trimethylamine (TMA), via the production of TMA N-oxide (TMAO). Is also able to perform S-oxidation when acting on sulfide compounds (PubMed:9224773). {ECO:0000250|UniProtKB:P97501, ECO:0000269|PubMed:9224773}.; . TISSUE SPECIFICITY: Liver.; . . 0.08168 0.11814 1.043548753 91.30691201 4771.19044 13.99230 FMO4 2.40849026007635e-09 0.259386150850907 0.740613846740603 flavin containing monooxygenase 4 FUNCTION: This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides.; . TISSUE SPECIFICITY: Liver.; . . 0.09522 0.11163 0.554869705 81.59943383 99.90833 2.16654 FMO5 3.69166290202894e-15 0.00291006455380284 0.997089935446194 flavin containing monooxygenase 5 FUNCTION: In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme.; . TISSUE SPECIFICITY: Expressed in fetal and adult liver.; unclassifiable (Anatomical System);prostate;ovary;lacrimal gland;placenta;liver;testis;colon;parathyroid;spleen;kidney;brain;mammary gland; fetal liver;superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.04411 0.09026 0.066214104 58.95848077 91.52075 2.05713 FMO6P 0.376800998137273 0.478534501513713 0.144664500349013 flavin containing monooxygenase 6 pseudogene FUNCTION: It is probable that this protein is only produced in very small quantity or not at all as the gene coding for it seems to be unable to produce full length transcripts.; . . lung;mammary gland; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . . . . 580.33047 4.88346 FMO7P . . . flavin containing monooxygenase 7 pseudogene . . . . . . . . . . . FMO8P . . . flavin containing monooxygenase 8 pseudogene . . . . . . . . . . . FMO9P . . . flavin containing monooxygenase 9 pseudogene . . . . . 0.14677 . . . . . FMO10P . . . flavin containing monooxygenase 10, pseudogene . . . . . . . . . . . FMO11P . . . flavin containing monooxygenase 11, pseudogene . . . . . . . . . . . FMOD 0.0495813811462611 0.858805082156007 0.0916135366977321 fibromodulin FUNCTION: Affects the rate of fibrils formation. May have a primary role in collagen fibrillogenesis (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;endometrium;bone;testis;middle ear;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;blood;lens;skeletal muscle;pancreas;lung;internal ear;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;trachea;thyroid;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.30724 0.10833 -0.424258538 25.56027365 82.11546 1.92197 FMR1 0.127197887114845 0.871796248916094 0.00100586396906128 fragile X mental retardation 1 FUNCTION: Translation repressor. Component of the CYFIP1-EIF4E- FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates translation repression (By similarity). RNA- binding protein that plays a role in intracellular RNA transport and in the regulation of translation of target mRNAs. Associated with polysomes. May play a role in the transport of mRNA from the nucleus to the cytoplasm. Binds strongly to poly(G), binds moderately to poly(U) but shows very little binding to poly(A) or poly(C). {ECO:0000250}.; DISEASE: Fragile X syndrome (FRAX) [MIM:300624]: Common genetic disease (has a prevalence of one in every 2000 children) which is characterized by moderate to severe mental retardation, macroorchidism (enlargement of the testicles), large ears, prominent jaw, and high-pitched, jocular speech. The defect in most fragile X syndrome patients results from an amplification of a CGG repeat region which is directly in front of the coding region. {ECO:0000269|PubMed:7688265, ECO:0000269|PubMed:8401578, ECO:0000269|PubMed:8490650}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Fragile X tremor/ataxia syndrome (FXTAS) [MIM:300623]: In FXTAS, the expanded repeats range in size from 55 to 200 repeats and are referred to as 'premutations'. Full repeat expansions with greater than 200 repeats results in fragile X mental retardation syndrome [MIM:300624]. Carriers of the premutation typically do not show the full fragile X syndrome phenotype, but comprise a subgroup that may have some physical features of fragile X syndrome or mild cognitive and emotional problems. {ECO:0000269|PubMed:11445641}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Premature ovarian failure 1 (POF1) [MIM:311360]: An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol. {ECO:0000269|PubMed:9719368}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest levels found in neurons, brain, testis, placenta and lymphocytes. Also expressed in epithelial tissues and at very low levels in glial cells. {ECO:0000269|PubMed:8401578, ECO:0000269|PubMed:8504300}.; unclassifiable (Anatomical System);amygdala;lymph node;islets of Langerhans;colon;blood;skin;skeletal muscle;uterus;breast;whole body;lung;endometrium;placenta;visual apparatus;liver;testis;head and neck;germinal center;brain;stomach; amygdala;superior cervical ganglion;occipital lobe;prefrontal cortex;globus pallidus;trigeminal ganglion;cerebellum; 0.57959 0.51740 0.260991686 70.25831564 96.23707 2.12071 FMR1-AS1 . . . FMR1 antisense RNA 1 . . . . . . . . . . . FMR1-IT1 . . . FMR1 intronic transcript 1 . . . . . . . . . . . FMR1NB 0.180154210181597 0.76608387498595 0.0537619148324533 fragile X mental retardation 1 neighbor . . TISSUE SPECIFICITY: Testis-specific. Expressed in melanoma, sarcoma, lung, breast, bladder, esophageal and ovarian cancers. {ECO:0000269|PubMed:12601173}.; . . 0.06690 . -0.161524709 41.6430762 324.6393 3.83054 FMR3 . . . fragile X mental retardation associated 3 . . . . . . . . . . . FN1 0.0644415382988527 0.935558461701147 2.07475663084699e-16 fibronectin 1 FUNCTION: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts.; DISEASE: Glomerulopathy with fibronectin deposits 2 (GFND2) [MIM:601894]: Genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life. {ECO:0000269|PubMed:18268355}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms), made by fibroblasts, epithelial and other cell types, is deposited as fibrils in the extracellular matrix. Ugl-Y1, Ugl-Y2 and Ugl-Y3 are found in urine. {ECO:0000269|PubMed:17614963, ECO:0000269|PubMed:3584091}.; ovary;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;thyroid;bone;amniotic fluid;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;spinal cord;lens;skeletal muscle;breast;pancreas;lung;cornea;epididymis;placenta;trabecular meshwork;macula lutea;visual apparatus;amnion;liver;alveolus;head and neck;mammary gland;aorta; dorsal root ganglion;superior cervical ganglion;adipose tissue;olfactory bulb;smooth muscle;heart;fetal liver;lung;trachea;placenta;liver;ciliary ganglion;fetal lung;trigeminal ganglion; 0.92203 0.99216 -2.323170444 1.18542109 825.54252 5.63214 FN3K 1.64310323001164e-05 0.665305922359269 0.33467764660843 fructosamine 3 kinase FUNCTION: May initiate a process leading to the deglycation of fructoselysine and of glycated proteins. May play a role in the phosphorylation of 1-deoxy-1-morpholinofructose (DMF), fructoselysine, fructoseglycine, fructose and glycated lysozyme.; . TISSUE SPECIFICITY: Expressed in erythrocytes.; unclassifiable (Anatomical System);ovary;cartilage;colon;fovea centralis;choroid;lens;skin;retina;uterus;breast;pancreas;optic nerve;lung;thyroid;macula lutea;iris;testis;kidney;brain;stomach; trigeminal ganglion; 0.21413 0.13148 -0.137658575 43.57159707 1203.46839 6.57250 FN3KRP 3.65777484277493e-07 0.19511904805601 0.804880586166506 fructosamine 3 kinase related protein FUNCTION: Phosphorylates psicosamines and ribulosamines, but not fructosamines, on the third carbon of the sugar moiety. Protein- bound psicosamine 3-phosphates and ribulosamine 3-phosphates are unstable and decompose under physiological conditions. Thus phosphorylation leads to deglycation. {ECO:0000269|PubMed:14633848, ECO:0000269|PubMed:15137908}.; . . lymphoreticular;ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;larynx;bone;testis;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; amygdala;whole brain;superior cervical ganglion;occipital lobe;pons;parietal lobe;cerebellum; . . 0.020302773 55.60863411 297.84245 3.68184 FNBP1 0.846297745604282 0.153697482434704 4.7719610147507e-06 formin binding protein 1 FUNCTION: May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL. {ECO:0000250, ECO:0000269|PubMed:15252009, ECO:0000269|PubMed:16318909, ECO:0000269|PubMed:16326391, ECO:0000269|PubMed:16418535, ECO:0000269|PubMed:17512409}.; DISEASE: Note=A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with KMT2A/MLL1. The relatively low incidence of the KMT2A/MLL1-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.; TISSUE SPECIFICITY: Very highly expressed in the epithelial cells of the gastrointestinal tract, respiratory, reproductive and urinary systems. Also highly expressed in brown adipose tissue, cardiomyocytes, enteric ganglia and glucagon producing cells of the pancreas. Expressed in germ cells of the testis and all regions of the brain. {ECO:0000269|PubMed:11438682, ECO:0000269|PubMed:15252009}.; unclassifiable (Anatomical System);breast;uterus;placenta;testis;head and neck;brain; amygdala;occipital lobe;spinal cord;white blood cells;cerebellum;thymus; 0.30172 0.16385 -0.157884861 42.05590941 211.92001 3.14012 FNBP1L 0.965504529201717 0.0344929377602116 2.53303807137263e-06 formin binding protein 1 like FUNCTION: Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by activating the WASL/N-WASP-WASPIP/WIP complex, the predominant form of WASL/N-WASP in cells. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Essential for autophagy of intracellular bacterial pathogens. {ECO:0000269|PubMed:15260990, ECO:0000269|PubMed:16326391, ECO:0000269|PubMed:19342671}.; . . unclassifiable (Anatomical System);colon;vein;skeletal muscle;retina;breast;duodenum;liver;pituitary gland;spleen;germinal center;brain;spinal ganglion; superior cervical ganglion;fetal brain;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.84238 0.12559 -0.780646273 12.77423921 22.94851 0.76481 FNBP1P1 . . . formin binding protein 1 pseudogene 1 . . . . . . . . . . . FNBP1P2 . . . formin binding protein 1 pseudogene 2 . . . . . . . . . . . FNBP4 0.999993422916695 6.57708329489717e-06 1.03542662639004e-14 formin binding protein 4 . . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;hypothalamus;urinary;pharynx;blood;skeletal muscle;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;cerebellum;thymus; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.52555 0.08820 0.510776592 80.23708422 3100.85744 10.59345 FNDC1 3.07460719768204e-07 0.999968249177555 3.14433617248477e-05 fibronectin type III domain containing 1 FUNCTION: May be an activator of G protein signaling. {ECO:0000250}.; . TISSUE SPECIFICITY: Almost absent from healthy skin; especially in epidermal keratinocytes, skin fibroblasts or endothelial cells and is barely detectable in benign melanocytic naevi. Expressed in the stroma close to skin tumors, in the tumor cells themselves and in the epidermis of psoriasis.; colon;skin;uterus;whole body;endometrium;cochlea;synovium;bone;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;blood;skeletal muscle;breast;pancreas;lung;trabecular meshwork;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;thyroid;temporal lobe;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13240 0.09503 2.671889479 98.84996461 6512.79761 16.93629 FNDC1-IT1 . . . FNDC1 intronic transcript 1 . . . . . . . . . . . FNDC3A 0.999884367658408 0.000115632341573092 1.87185210706884e-14 fibronectin type III domain containing 3A FUNCTION: Mediates spermatid-Sertoli adhesion during spermatogenesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the odontoblast and nerves in the dental pulp. Also expressed in trachea and to a lesser extent in the brain, liver, lung and kidney. {ECO:0000269|PubMed:18218838}.; smooth muscle;ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;heart;lacrimal gland;tongue;islets of Langerhans;hypothalamus;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;aorta;stomach;cerebellum; superior cervical ganglion;testis - interstitial;trigeminal ganglion;skeletal muscle;pituitary; 0.44936 0.49287 -1.54691447 3.284972871 365.09768 4.04270 FNDC3B 0.999999985029909 1.49700908355058e-08 1.86893274849544e-20 fibronectin type III domain containing 3B FUNCTION: May be a positive regulator of adipogenesis. {ECO:0000269|PubMed:15564382}.; . TISSUE SPECIFICITY: Predominantly expressed in white adipose tissue (WAT) especially in the stromal vascular cells. Expressed in adipocyte differentiable 3T3-L1 cells but not in the non- adipogenic cell line NIH-3T3. Expression increased in the early stage of adipogenesis. {ECO:0000269|PubMed:15564382}.; myocardium;ovary;skin;bone marrow;retina;prostate;endometrium;cochlea;thyroid;amniotic fluid;germinal center;brain;gall bladder;heart;cartilage;adrenal cortex;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;developmental;colon;parathyroid;uterus;oesophagus;larynx;bone;testis;dura mater;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;pancreas;lung;pia mater;adrenal gland;placenta;head and neck;kidney;stomach;aorta;thymus; placenta;trigeminal ganglion; 0.41387 0.10529 -0.6338229 16.76692616 163.76466 2.79500 FNDC3CP . . . fibronectin type III domain containing 3C, pseudogene . . . . . . . . . . . FNDC4 0.759219015798597 0.238811641623656 0.00196934257774686 fibronectin type III domain containing 4 . . . unclassifiable (Anatomical System);ovary;heart;hypothalamus;sympathetic chain;adrenal cortex;colon;parathyroid;blood;skin;skeletal muscle;uterus;pancreas;prostate;whole body;lung;frontal lobe;bone;thyroid;placenta;hippocampus;liver;testis;spleen;kidney;brain;stomach;cerebellum; whole brain;thalamus;occipital lobe;superior cervical ganglion;adipose tissue;fetal brain;temporal lobe;adrenal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.32272 0.11109 -0.185391282 39.67916962 41.95696 1.22238 FNDC5 0.406509132252723 0.555707807659499 0.0377830600877785 fibronectin type III domain containing 5 FUNCTION: Irisin: Contrary to mouse, may not be involved in the beneficial effects of muscular exercise, nor in the induction of browning of human white adipose tissue. {ECO:0000269|PubMed:24040023}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in heart. Very low expression, if any, in colon, pancreas and spleen. {ECO:0000269|PubMed:24040023}.; . . 0.74032 0.15416 -0.251530012 35.42108988 37.09426 1.10826 FNDC7 0.000318365257387006 0.944595541105238 0.0550860936373753 fibronectin type III domain containing 7 . . . unclassifiable (Anatomical System);testis;mammary gland; . 0.34946 . 1.379742765 94.60368011 1673.11244 7.54892 FNDC8 1.90285973893222e-05 0.269203465176812 0.730777506225799 fibronectin type III domain containing 8 . . . unclassifiable (Anatomical System);medulla oblongata;lung;amnion;testis;kidney;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node;skeletal muscle; 0.17045 . -0.224023033 37.4321774 72.97365 1.78284 FNDC9 0.00399382359916547 0.648274140723814 0.347732035677021 fibronectin type III domain containing 9 . . . unclassifiable (Anatomical System);hypothalamus;brain;retina;cerebellum; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.22519 . 0.328949044 73.41354093 1317.46667 6.82585 FNIP1 0.99981944509088 0.000180554908845711 2.73921817377501e-13 folliculin interacting protein 1 FUNCTION: May be involved in energy and/or nutrient sensing through the AMPK and mTOR signaling pathways. May regulate phosphorylation of RPS6KB1. {ECO:0000269|PubMed:17028174, ECO:0000269|PubMed:18663353}.; . TISSUE SPECIFICITY: Strong expression is found in the heart, liver placenta, muscle, nasal mucosa, salivary gland and uvula and moderate expression in kidney and lung. Higher levels detected in clear cell renal cell carcinoma (RCC) and chromophobe RCC than in normal kidney tissue. {ECO:0000269|PubMed:17028174, ECO:0000269|PubMed:18403135}.; unclassifiable (Anatomical System);heart;islets of Langerhans;colon;parathyroid;blood;skin;uterus;lung;frontal lobe;placenta;liver;testis;spleen;germinal center;kidney;brain;stomach; . 0.56317 . -0.571310997 19.01391838 387.17012 4.14356 FNIP2 0.997777001640614 0.0022229977446802 6.14705471124547e-10 folliculin interacting protein 2 FUNCTION: May play a role in the signal transduction pathway of apoptosis induced by O6-methylguanine-mispaired lesions (By similarity). May be involved in energy and/or nutrient sensing through the AMPK and mTOR signaling pathways. May regulate phosphorylation of RPS6KB1. {ECO:0000250, ECO:0000269|PubMed:18403135, ECO:0000269|PubMed:18663353}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in muscle, nasal mucosa, salivary gland, uvula, fat, liver, heart, placenta and pancreas. Moderately expressed in the lung, small intestine, kidney and brain. Lower levels detected in renal cell carcinoma than in normal kidney tissue. Higher levels detected in oncocytoma than in normal kidney. {ECO:0000269|PubMed:18403135, ECO:0000269|PubMed:18663353}.; lymphoreticular;ovary;colon;parathyroid;skin;uterus;thyroid;bone;testis;amniotic fluid;brain;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;lung;placenta;liver;hypopharynx;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.11511 0.08281 -0.10469683 45.64755839 731.02841 5.36823 FNTA 0.988212601847893 0.01178651279615 8.85355957351412e-07 farnesyltransferase, CAAX box, alpha FUNCTION: Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1 prenylation and activation. {ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937, ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:8419339, ECO:0000269|PubMed:8494894}.; . . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;urinary;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta; dorsal root ganglion;amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;olfactory bulb;hypothalamus;spinal cord;prefrontal cortex;pons;caudate nucleus;trigeminal ganglion;parietal lobe; 0.46996 0.10423 -0.071520315 48.34866714 53.56528 1.45538 FNTAP1 . . . farnesyltransferase, CAAX box, alpha pseudogene 1 . . . . . . . . . . . FNTAP2 . . . farnesyltransferase, CAAX box, alpha pseudogene 2 . . . . . . . . . . . FNTB 0.17200103905538 0.827424696774128 0.000574264170492466 farnesyltransferase, CAAX box, beta FUNCTION: Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C- terminus of several proteins having the C-terminal sequence Cys- aliphatic-aliphatic-X. {ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937, ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:8494894}.; . . myocardium;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;bone;iris;testis;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;cerebellum cortex;hypothalamus;pharynx;blood;lens;breast;pancreas;lung;epididymis;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;spinal cord;testis;ciliary ganglion;atrioventricular node;skeletal muscle;cerebellum; 0.22283 0.11360 -0.426079032 25.36565228 9.65839 0.35473 FOCAD 5.37298120474939e-16 0.999961845662663 3.81543373361336e-05 focadhesin FUNCTION: Potential tumor suppressor in gliomas. {ECO:0000250, ECO:0000269|PubMed:22427331}.; . TISSUE SPECIFICITY: Ubiquitous. High expression in brain followed by testis, muscle, pancreas, heart, ovary, small intestine, placenta, prostate, thymus, kidney, colon, liver, lung, spleen and leukocytes. Expression is reduced in most glioblastomas and all glioblastoma cell lines. {ECO:0000269|PubMed:16877819, ECO:0000269|PubMed:22427331}.; . . 0.07009 0.07997 -0.191316565 39.26043878 5977.84024 16.10083 FOCAD-AS1 . . . FOCAD antisense RNA 1 . . . . . . . . . . . FOLH1 0.253396884638148 0.746592621385707 1.04939761456324e-05 folate hydrolase (prostate-specific membrane antigen) 1 FUNCTION: Has both folate hydrolase and N-acetylated-alpha-linked- acidic dipeptidase (NAALADase) activity. Has a preference for tri- alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N- aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression.; . TISSUE SPECIFICITY: Highly expressed in prostate epithelium. Detected in urinary bladder, kidney, testis, ovary, fallopian tube, breast, adrenal gland, liver, esophagus, stomach, small intestine, colon and brain (at protein level). Detected in the small intestine, brain, kidney, liver, spleen, colon, trachea, spinal cord and the capillary endothelium of a variety of tumors. Expressed specifically in jejunum brush border membranes. In the brain, highly expressed in the ventral striatum and brain stem. Also expressed in fetal liver and kidney. Isoform PSMA' is the most abundant form in normal prostate. Isoform PSMA-1 is the most abundant form in primary prostate tumors. Isoform PSMA-2 is also found in normal prostate as well as in brain and liver. Isoform PSMA-9 is specifically expressed in prostate cancer. {ECO:0000269|PubMed:14716746, ECO:0000269|PubMed:16555021, ECO:0000269|PubMed:17150306, ECO:0000269|PubMed:9375657}.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;prostate;lung;frontal lobe;cornea;endometrium;visual apparatus;liver;testis;spleen;kidney;spinal ganglion;brain;mammary gland;peripheral nerve; amygdala;dorsal root ganglion;whole brain;thalamus;occipital lobe;medulla oblongata;olfactory bulb;salivary gland;hypothalamus;spinal cord;caudate nucleus;prostate;subthalamic nucleus;prefrontal cortex;ciliary ganglion;parietal lobe;cingulate cortex; 0.15752 0.43198 1.332002318 94.20853975 2268.34509 8.81053 FOLH1B . . . folate hydrolase 1B FUNCTION: Has both folate hydrolase and N-acetylated-alpha-linked- acidic dipeptidase (NAALADase) activity. {ECO:0000250}.; . TISSUE SPECIFICITY: Kidney and liver. Not expressed in the prostate. {ECO:0000269|PubMed:14716746}.; . . . . . . . . FOLR1 0.00741067522640952 0.923931695254235 0.0686576295193553 folate receptor 1 (adult) FUNCTION: Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells. Has high affinity for folate and folic acid analogs at neutral pH. Exposure to slightly acidic pH after receptor endocytosis triggers a conformation change that strongly reduces its affinity for folates and mediates their release. Required for normal embryonic development and normal cell proliferation. {ECO:0000269|PubMed:23851396, ECO:0000269|PubMed:23934049, ECO:0000269|PubMed:2527252, ECO:0000269|PubMed:8033114, ECO:0000269|PubMed:8567728}.; DISEASE: Neurodegeneration due to cerebral folate transport deficiency (NCFTD) [MIM:613068]: A neurodegenerative disorder resulting from brain-specific folate deficiency early in life. Onset is apparent in late infancy with severe developmental regression, movement disturbances, epilepsy and leukodystrophy. {ECO:0000269|PubMed:19732866}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Primarily expressed in tissues of epithelial origin. Expression is increased in malignant tissues. Expressed in kidney, lung and cerebellum. Detected in placenta and thymus epithelium. {ECO:0000269|PubMed:2527252, ECO:0000269|PubMed:2768245, ECO:0000269|PubMed:9063895}.; unclassifiable (Anatomical System);cartilage;ovary;colon;parathyroid;choroid;uterus;prostate;lung;endometrium;nasopharynx;placenta;liver;cervix;kidney;brain;mammary gland;stomach; superior cervical ganglion;trachea;kidney;trigeminal ganglion; 0.40687 0.26385 0.459411326 78.28497287 31.20225 0.98450 FOLR1P1 . . . folate receptor 1 (adult) pseudogene 1 . . . . . . . . . . . FOLR2 6.16825536172656e-07 0.141482210688922 0.858517172485541 folate receptor 2 (fetal) FUNCTION: Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells. Has high affinity for folate and folic acid analogs at neutral pH. Exposure to slightly acidic pH after receptor endocytosis triggers a conformation change that strongly reduces its affinity for folates and mediates their release. {ECO:0000269|PubMed:23934049, ECO:0000269|PubMed:2605182, ECO:0000269|PubMed:4066659}.; . TISSUE SPECIFICITY: Expressed in placenta and hematopoietic cells. Expression is increased in malignant tissues. {ECO:0000269|PubMed:2605182, ECO:0000269|PubMed:8445646}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;iris;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;lens;skeletal muscle;pancreas;pia mater;lung;nasopharynx;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;placenta;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skin; 0.05794 0.14661 0.060756528 58.52795471 66.56597 1.68159 FOLR3 0.0108674399648362 0.835756389152169 0.153376170882995 folate receptor 3 (gamma) FUNCTION: Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate to the interior of cells. Isoform Short does not bind folate.; . TISSUE SPECIFICITY: Spleen, thymus, bone marrow, ovarian carcinoma, and uterine carcinoma.; larynx;blood;head and neck;kidney;bone marrow; superior cervical ganglion;whole blood;trigeminal ganglion;skeletal muscle;bone marrow; 0.09866 0.10400 . . 1068.47557 6.26588 FOLR3P1 . . . folate receptor 3 (gamma) pseudogene 1 . . . . . . . . . . . FOPNL 9.46709362306996e-06 0.331417657193178 0.668572875713199 FGFR1OP N-terminal like FUNCTION: Involved in the biogenesis of cilia. {ECO:0000269|PubMed:20551181}.; . TISSUE SPECIFICITY: Widely expressed. Detected in brain, heart, kidney, liver, lung, skeletal muscle, placenta and intestine. {ECO:0000269|PubMed:20551181}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;aorta;stomach; testis - interstitial;subthalamic nucleus;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.18822 . -0.073340031 48.11866006 2560.2307 9.44776 FOS 0.435710740653144 0.557319878376936 0.00696938096992051 FBJ murine osteosarcoma viral oncogene homolog FUNCTION: Nuclear phosphoprotein which forms a tight but non- covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD- binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum. {ECO:0000269|PubMed:16055710, ECO:0000269|PubMed:17160021, ECO:0000269|PubMed:22105363, ECO:0000269|PubMed:7588633, ECO:0000269|PubMed:9732876}.; . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;synovium;larynx;bone;thyroid;iris;pituitary gland;testis;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;pancreas;lung;adrenal gland;epididymis;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.95410 0.96732 -0.049474214 50.01179523 37.9377 1.12664 FOSB 0.852916176747718 0.146576388091855 0.000507435160426595 FBJ murine osteosarcoma viral oncogene homolog B FUNCTION: FosB interacts with Jun proteins enhancing their DNA binding activity.; . . smooth muscle;ovary;umbilical cord;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;thyroid;iris;testis;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; ciliary ganglion; 0.56755 0.43030 -0.117432389 44.89266336 34.12794 1.04651 FOSL1 0.28979602655229 0.689205893910146 0.0209980795375643 FOS like antigen 1 . . . ovary;salivary gland;intestine;colon;skin;bone marrow;prostate;bone;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;pharynx;blood;bile duct;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;amnion;head and neck;cervix;kidney;stomach; ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.31244 0.46150 0.016664174 55.21939137 29.14509 0.93162 FOSL1P1 . . . FOS like antigen 1 pseudogene 1 . . . . . . . . . . . FOSL2 0.925334261981773 0.0742402684662243 0.000425469552002478 FOS like antigen 2 FUNCTION: Controls osteoclast survival and size. As a dimer with JUN, activates LIF transcription. Activates CEBPB transcription in PGE2-activated osteoblasts. {ECO:0000250}.; . . ovary;salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;hypopharynx;liver;amnion;head and neck;cervix;kidney;mammary gland;stomach; olfactory bulb;adrenal gland;adrenal cortex;ciliary ganglion;trigeminal ganglion;skin;skeletal muscle; 0.89377 0.28962 -0.692458599 14.96815287 25.82937 0.84094 FOXA1 . . . forkhead box A1 FUNCTION: Transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3' (By similarity). Proposed to play a role in translating the epigenetic signatures into cell type-specific enhancer-driven transcriptional programs. Its differential recruitment to chromatin is dependent on distribution of histone H3 methylated at 'Lys-5' (H3K4me2) in estrogen-regulated genes. Involved in the development of multiple endoderm-derived organ systems such as liver, pancreas, lung and prostate; FOXA1 and FOXA2 seem to have at least in part redundant roles (By similarity). Modulates the transcriptional activity of nuclear hormone receptors. Is involved in ESR1-mediated transcription; required for ESR1 binding to the NKX2-1 promoter in breast cancer cells; binds to the RPRM promter and is required for the estrogen-induced repression of RPRM. Involved in regulation of apoptosis by inhibiting the expression of BCL2. Involved in cell cycle regulation by activating expression of CDKN1B, alone or in conjunction with BRCA1. Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis- acting regulatory regions of these genes. Involved in glucose homeostasis. {ECO:0000250, ECO:0000269|PubMed:16087863, ECO:0000269|PubMed:16331276, ECO:0000269|PubMed:18358809, ECO:0000269|PubMed:19127412, ECO:0000269|PubMed:19917725}.; . TISSUE SPECIFICITY: Highly expressed in prostate and ESR1-positive breast tumors. Overexpressed in esophageal and lung adenocarcinomas. {ECO:0000269|PubMed:12234996, ECO:0000269|PubMed:15987773, ECO:0000269|PubMed:16331276}.; unclassifiable (Anatomical System);colon;blood;breast;prostate;lung;larynx;nasopharynx;liver;testis;head and neck;spleen;kidney;brain;mammary gland;bladder;stomach;peripheral nerve; . 0.81174 0.43217 0.61555716 83.13871196 355.894 3.99230 FOXA2 . . . forkhead box A2 FUNCTION: Transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3' (By similarity). In embryonic development is required for notochord formation. Involved in the development of multiple endoderm-derived organ systems such as the liver, pancreas and lungs; FOXA1 and FOXA2 seem to have at least in part redundant roles. Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis; regulates the expression of genes important for glucose sensing in pancreatic beta-cells and glucose homeostasis. Involved in regulation of fat metabolism. Binds to fibrinogen beta promoter and is involved in IL6-induced fibrinogen beta transcriptional activation. {ECO:0000250}.; . . unclassifiable (Anatomical System);pancreas;lung;cartilage;ovary;endometrium;islets of Langerhans;placenta;liver;testis;colon;parathyroid;choroid;mammary gland; dorsal root ganglion;pancreas;superior cervical ganglion;lung;beta cell islets;liver;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.53135 0.65868 0.038710339 56.92380278 181.27451 2.92760 FOXA3 0.395510308295114 0.563783218183445 0.0407064735214409 forkhead box A3 FUNCTION: Transcription factor that is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites (By similarity). Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis; binds to and activates transcription from the G6PC promoter. Binds to the CYP3A4 promoter and activates its transcription in cooperation with CEBPA. Binds to the CYP3A7 promoter together with members of the CTF/NF-I family. Involved in regulation of neuronal-specific transcription. May be involved in regulation of spermatogenesis. {ECO:0000250, ECO:0000269|PubMed:12695546}.; . TISSUE SPECIFICITY: Expressed in erythroleukemia and hepatoma cell lines and in liver and pancreas. Not expressed in any other cell lines or tissues examined. {ECO:0000269|PubMed:8499623}.; unclassifiable (Anatomical System);prostate;cartilage;islets of Langerhans;bone;liver;colon;spleen;stomach; dorsal root ganglion;superior cervical ganglion;temporal lobe;ciliary ganglion;atrioventricular node; 0.96935 0.24480 -0.494039303 22.09247464 34.86418 1.06122 FOXB1 0.702812387833519 0.281023503714348 0.0161641084521329 forkhead box B1 . . . . . 0.76924 0.15588 -0.185391282 39.67916962 38.21286 1.13442 FOXB2 2.39247928093334e-06 0.0868861065483093 0.91311150097241 forkhead box B2 FUNCTION: Transcription factor. {ECO:0000305}.; . . . . 0.57849 0.10915 . . 70.49669 1.74683 FOXC1 . . . forkhead box C1 FUNCTION: Binding of FREAC-3 and FREAC-4 to their cognate sites results in bending of the DNA at an angle of 80-90 degrees. Regulates FOXO1 through binding to a conserved element, 5'- GTAAACAAA-3' in its promoter region, implicating FOXC1 as an important regulator of cell viability and resistance to oxidative stress in the eye. {ECO:0000269|PubMed:17993506}.; DISEASE: Iridogoniodysgenesis anomaly (IGDA) [MIM:601631]: Autosomal dominant phenotype characterized by iris hypoplasia, goniodysgenesis, and juvenile glaucoma. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peters anomaly (PETAN) [MIM:604229]: Consists of a central corneal leukoma, absence of the posterior corneal stroma and Descemet membrane, and a variable degree of iris and lenticular attachments to the central aspect of the posterior cornea. {ECO:0000269|PubMed:12614756}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues and cell lines examined. {ECO:0000269|PubMed:8499623}.; . . 0.71308 0.29904 . . 1711.71278 7.62793 FOXC2 . . . forkhead box C2 FUNCTION: Transcriptional activator. Might be involved in the formation of special mesenchymal tissues. {ECO:0000269|PubMed:9169153}.; DISEASE: Lymphedema-distichiasis (LYD) [MIM:153400]: A disorder characterized by primary limb lymphedema associated with distichiasis (double rows of eyelashes, with extra eyelashes growing from the Meibomian gland orifices). Swelling of the extremities, due to altered lymphatic flow, usually appears in late childhood or puberty. Most affected individuals have ocular findings including corneal irritation, recurrent conjunctivitis, and photophobia. Drooping of the upper eyelid (ptosis) is a variable feature of the lymphedema-distichiasis syndrome, occurring in about 30% of patients. {ECO:0000269|PubMed:11078474, ECO:0000269|PubMed:11371511, ECO:0000269|PubMed:11499682}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . uterus;optic nerve;lung;cerebral cortex;macula lutea;head and neck;fovea centralis;choroid;kidney;lens;retina; superior cervical ganglion; 0.38597 0.23829 . . 50.82093 1.40445 FOXC2-AS1 . . . FOXC2 antisense RNA 1 . . . . . . . . . . . FOXCUT . . . FOXC1 upstream transcript (non-protein coding) . . . . . . . . . . . FOXD1 . . . forkhead box D1 FUNCTION: Transcription factor required for formation of positional identity in the developing retina, regionalization of the optic chiasm and morphogenesis of the kidney. Can neuralize ectodermal cells directly (By similarity). {ECO:0000250}.; . . . . . . . . 3852.25413 12.23510 FOXD1-AS1 . . . FOXD1 antisense RNA 1 . . . . . . . . . . . FOXD2 . . . forkhead box D2 FUNCTION: Probable transcription factor involved in embryogenesis and somatogenesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Kidney specific. {ECO:0000269|PubMed:9403061}.; unclassifiable (Anatomical System);optic nerve;lung; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.49407 . . . 682.33346 5.22095 FOXD2-AS1 . . . FOXD2 antisense RNA 1 (head to head) . . . . . . . . . . . FOXD3 . . . forkhead box D3 FUNCTION: Binds to the consensus sequence 5'-A[AT]T[AG]TTTGTTT-3' and acts as a transcriptional repressor. Also acts as a transcriptional activator. Promotes development of neural crest cells from neural tube progenitors. Restricts neural progenitor cells to the neural crest lineage while suppressing interneuron differentiation. Required for maintenance of pluripotent cells in the pre-implantation and peri-implantation stages of embryogenesis. {ECO:0000269|PubMed:11891324}.; . TISSUE SPECIFICITY: Expressed in chronic myeloid leukemia, Jurkat T-cell leukemia and teratocarcinoma cell lines, but not in any other cell lines or normal tissues examined. {ECO:0000269|PubMed:8499623}.; . . 0.60815 0.22434 . . 413.93622 4.26161 FOXD3-AS1 . . . FOXD3 antisense RNA 1 (head to head) . . . . . . . . . . . FOXD4 . . . forkhead box D4 . . . . . 0.15599 . 0.885576705 89.14248644 2757.82566 9.90294 FOXD4L1 . . . forkhead box D4-like 1 . . . unclassifiable (Anatomical System);uterus;lung;whole body;ovary;placenta;developmental;colon;parathyroid; . 0.05795 0.07954 1.616843854 95.96013211 3262.81752 10.89654 FOXD4L3 . . . forkhead box D4-like 3 . . . unclassifiable (Anatomical System);uterus;prostate;lung;whole body;ovary;placenta;colon;parathyroid; . . . . . 336.15283 3.89485 FOXD4L4 . . . forkhead box D4-like 4 . . . . . . . . . . . FOXD4L5 . . . forkhead box D4-like 5 . . . . . . . . . 79.92726 1.89028 FOXD4L6 . . . forkhead box D4-like 6 . . . . . . . . . 8.05022 0.29515 FOXE1 . . . forkhead box E1 FUNCTION: Probable transcription factor. Could be involved in thyroid gland organogenesis.; DISEASE: Bamforth-Lazarus syndrome (BLS) [MIM:241850]: A disease characterized by thyroid agenesis, cleft palate and choanal atresia. {ECO:0000269|PubMed:12165566, ECO:0000269|PubMed:9697705}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in adult brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, heart, colon, small intestine testis and thymus. Expression was strongest in heart and pancreas.; . . . 0.10592 . . 82.34677 1.92681 FOXE3 . . . forkhead box E3 FUNCTION: Transcription factor that controls lens epithelial cell growth through regulation of proliferation, apoptosis and cell cycle (PubMed:22527307, PubMed:25504734). During lens development, controls the ratio of the lens fiber cells to the cells of the anterior lens epithelium by regulating the rate of proliferation and differentiation (By similarity). Controls lens vesicle closure and subsequent separation of the lens vesicle from ectoderm (By similarity). Is required for morphogenesis and differentiation of the anterior segment of the eye (By similarity). {ECO:0000250|UniProtKB:Q9QY14, ECO:0000269|PubMed:22527307, ECO:0000269|PubMed:25504734}.; DISEASE: Anterior segment mesenchymal dysgenesis (ASMD) [MIM:107250]: A range of developmental defects in structures at the front of the eye, resulting from abnormal migration or differentiation of the neural crest derived mesenchymal cells that give rise to the cornea, iris, and other components of the anterior chamber during eye development. Different mature anterior segment anomalies may exist alone or in combination, and are associated with an increased risk of glaucoma and corneal opacity. Conditions falling within the phenotypic spectrum of anterior segment anomalies include aniridia, posterior embryotoxon, Axenfeld anomaly, Reiger anomaly/syndrome, Peters anomaly, and iridogoniodysgenesis. {ECO:0000269|PubMed:11159941, ECO:0000269|PubMed:11980846}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Congenital primary aphakia (CPA) [MIM:610256]: Aphakia is a rare congenital eye disorder in which the lens is missing. It has been histologically subdivided into primary and secondary forms, in accordance with the severity of defects of the ocular tissues, whose development requires the initial presence of a lens. CPA results from an early developmental arrest, around the 4th-5th week of gestation in humans, that prevents the formation of any lens structure and leads to severe secondary ocular defects, including a complete aplasia of the anterior segment of the eye. In contrast, in secondary aphakic eyes, lens induction has occurred, and the lens vesicle has developed to some degree but finally has progressively resorbed perinatally, leading, therefore, to less-severe ocular defects. {ECO:0000269|PubMed:16826526, ECO:0000269|PubMed:25504734}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . prostate;testis;lens; superior cervical ganglion;prefrontal cortex;trigeminal ganglion;skeletal muscle; 0.07488 . . . 94.84396 2.09941 FOXF1 0.909443996784091 0.0898614860958734 0.000694517120035773 forkhead box F1 FUNCTION: Probable transcription activator for a number of lung- specific genes.; DISEASE: Alveolar capillary dysplasia with misalignment of pulmonary veins (ACDMPV) [MIM:265380]: A rare developmental disorder characterized by abnormal development of the capillary vascular system in the lungs. Histological features include failure of formation and ingrowth of alveolar capillaries, medial muscular thickening of small pulmonary arterioles with muscularization of the intraacinar arterioles, thickened alveolar walls, and anomalously situated pulmonary veins running alongside pulmonary arterioles and sharing the same adventitial sheath. Less common features include a reduced number of alveoli and a patchy distribution of the histopathologic changes. Affected infants present with respiratory distress and the disease is fatal within the newborn period. Additional features include multiple congenital anomalies affecting the cardiovascular, gastrointestinal, genitourinary, and musculoskeletal systems, as well as disruption of the normal right-left asymmetry of intrathoracic or intraabdominal organs. ACDMPV is a rare cause of persistent pulmonary hypertension of the newborn, an abnormal physiologic state caused by failure of transition of the pulmonary circulation from the high pulmonary vascular resistance of the fetus to the low pulmonary vascular resistance of the newborn. {ECO:0000269|PubMed:19500772, ECO:0000269|PubMed:23505205}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in lung and placenta. {ECO:0000269|PubMed:7957066}.; unclassifiable (Anatomical System);prostate;smooth muscle;lung;cartilage;placenta;testis;colon;cervix;spleen;stomach; superior cervical ganglion; 0.35916 0.20256 . . 87.48564 1.99763 FOXF2 . . . forkhead box F2 FUNCTION: Probable transcription activator for a number of lung- specific genes.; . TISSUE SPECIFICITY: Lung and placenta.; cartilage;developmental;skin;retina;pancreas;prostate;lung;trabecular meshwork;liver;testis;cervix;kidney;spinal ganglion;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.12698 . . . 4302.7333 13.06347 FOXG1 . . . forkhead box G1 FUNCTION: Transcription repression factor which plays an important role in the establishment of the regional subdivision of the developing brain and in the development of the telencephalon. {ECO:0000269|PubMed:12657635}.; . TISSUE SPECIFICITY: Expression is restricted to the neurons of the developing telencephalon. {ECO:0000269|PubMed:7959731}.; unclassifiable (Anatomical System);ovary;cochlea;testis;brain;stomach; whole brain;amygdala;medulla oblongata;superior cervical ganglion;occipital lobe;testis - interstitial;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;cingulate cortex;parietal lobe; 0.40390 0.69601 -0.251530012 35.42108988 15.2583 0.54838 FOXG1-AS1 . . . FOXG1 antisense RNA 1 (head to head) . . . . . . . . . . . FOXH1 0.0132911961348389 0.862630826345821 0.12407797751934 forkhead box H1 FUNCTION: Transcriptional activator. Recognizes and binds to the DNA sequence 5'-TGT[GT][GT]ATT-3'. Required for induction of the goosecoid (GSC) promoter by TGF-beta or activin signaling. Forms a transcriptionally active complex containing FOXH1/SMAD2/SMAD4 on a site on the GSC promoter called TARE (TGF-beta/activin response element). {ECO:0000269|PubMed:9702198}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9702198}.; unclassifiable (Anatomical System);trophoblast;ovary; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.71587 0.24185 -0.001743238 53.85114414 246.30123 3.38726 FOXI1 0.109581473399305 0.776852731272463 0.113565795328232 forkhead box I1 FUNCTION: Transcriptional activator required for the development of normal hearing, sense of balance and kidney function. Required for the expression of SLC26A4/PDS, JAG1 and COCH in a subset of epithelial cells and the development of the endolymphatic system in the inner ear. Also required for the expression of SLC4A1/AE1, SLC4A9/AE4, ATP6V1B1 and the differentiation of intercalated cells in the epithelium of distal renal tubules (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in kidney.; lung;colon;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.20973 0.19960 -0.446304853 24.33356924 38.96229 1.15494 FOXI2 1.59663014247231e-05 0.135003915649439 0.864980118049136 forkhead box I2 FUNCTION: Possible transcriptional activator. {ECO:0000250}.; . . . . 0.05959 . . . 146.02366 2.63323 FOXI3 . . . forkhead box I3 FUNCTION: Possible transcriptional factor. {ECO:0000250}.; . . . . . . . . . . FOXJ1 0.826867383152592 0.169402385069852 0.00373023177755665 forkhead box J1 FUNCTION: Transcription factor required for motile ciliogenesis. {ECO:0000250|UniProtKB:Q61660}.; DISEASE: Allergic rhinitis (ALRH) [MIM:607154]: A common disease with complex inheritance characterized by mucosal inflammation caused by allergen exposure. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Testis, oviduct, lung and brain cortex.; unclassifiable (Anatomical System);ovary;cartilage;islets of Langerhans;colon;uterus;pancreas;lung;endometrium;testis;spleen;kidney;brain;stomach; subthalamic nucleus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18626 0.25683 . . 94.31479 2.09078 FOXJ2 0.998394611630928 0.00160538158066298 6.7884090383002e-09 forkhead box J2 FUNCTION: Transcriptional activator. Able to bind to two different type of DNA binding sites. Isoform FOXJ2.L behaves as a more potent transactivator than FOXJ2.S.; . TISSUE SPECIFICITY: Widely expressed.; ovary;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;thyroid;iris;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;liver;spleen;kidney;mammary gland;cerebellum; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.81015 0.13622 -0.600630256 18.06440198 91.09698 2.05356 FOXJ3 0.977575009123256 0.0224248144833204 1.76393423759192e-07 forkhead box J3 FUNCTION: Transcriptional activator of MEF2C involved in the regulation pf adult muscle fiber type identity and skeletal muscle regeneration. {ECO:0000250|UniProtKB:Q8BUR3}.; . . colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;duodenum;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;cerebellum; amygdala;superior cervical ganglion;prefrontal cortex;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.75216 0.14428 0.286674996 71.49681529 467.55831 4.48092 FOXK1 0.962670920746712 0.0373138547820163 1.52244712711955e-05 forkhead box K1 FUNCTION: Transcriptional regulator that binds to the upstream enhancer region (CCAC box) of myoglobin gene. Has a role in myogenic differentiation and in remodeling processes of adult muscles that occur in response to physiological stimuli (By similarity). {ECO:0000250|UniProtKB:P42128}.; . TISSUE SPECIFICITY: Expressed both developing and adult tissues. In adults, significant expression is seen in tumors of the brain, colon and lymph node. {ECO:0000269|PubMed:15289879}.; unclassifiable (Anatomical System);uterus;lung;ovary;heart;islets of Langerhans;testis;colon;brain;skin;thymus; superior cervical ganglion;subthalamic nucleus;testis;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.15597 0.12005 -1.107723888 6.829440906 888.10645 5.80361 FOXK2 0.918748433171859 0.081229654663201 2.19121649402805e-05 forkhead box K2 FUNCTION: Recognizes the core sequence 5'-TAAACA-3'. Binds to NFAT-like motifs (purine-rich) in the IL2 promoter. Also binds to HIV-1 long terminal repeat. May be involved in both positive and negative regulation of important viral and cellular promoter elements. {ECO:0000269|PubMed:1339390, ECO:0000269|PubMed:1909027}.; . TISSUE SPECIFICITY: Expressed in both lymphoid and non-lymphoid cells. {ECO:0000269|PubMed:1339390}.; myocardium;ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;synovium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;nervous;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;thymus; adrenal gland;adrenal cortex;testis;trigeminal ganglion;skeletal muscle; 0.52179 0.20433 -0.415165735 25.83746167 357.93334 4.00848 FOXL1 0.0639302371886436 0.726767173550347 0.209302589261009 forkhead box L1 FUNCTION: Transcription factor required for proper proliferation and differentiation in the gastrointestinal epithelium. Target gene of the hedgehog (Hh) signaling pathway via GLI2 AND GLI3 transcription factors (By similarity). {ECO:0000250}.; . . lung; superior cervical ganglion;subthalamic nucleus;trigeminal ganglion;skeletal muscle;parietal lobe; 0.73079 . . . 70.601 1.74883 FOXL2 . . . forkhead box L2 FUNCTION: Transcriptional regulator. Critical factor essential for ovary differentiation and maintenance, and repression of the genetic program for somatic testis determination. Prevents trans- differentiation of ovary to testis through transcriptional repression of the Sertoli cell-promoting gene SOX9 (By similarity). Has apoptotic activity in ovarian cells. Suppresses ESR1-mediated transcription of PTGS2/COX2 stimulated by tamoxifen (By similarity). Is a regulator of CYP19 expression (By similarity). Participates in SMAD3-dependent transcription of FST via the intronic SMAD-binding element (By similarity). Is a transcriptional repressor of STAR. Activates SIRT1 transcription under cellular stress conditions. Activates transcription of OSR2. {ECO:0000250, ECO:0000269|PubMed:16153597, ECO:0000269|PubMed:19010791, ECO:0000269|PubMed:19429596, ECO:0000269|PubMed:19744555}.; DISEASE: Blepharophimosis, ptosis, and epicanthus inversus syndrome (BPES) [MIM:110100]: A disorder characterized by eyelid dysplasia, small palpebral fissures, drooping eyelids and a skin fold curving in the mediolateral direction, inferior to the inner canthus. In type I BPSE (BPES1) eyelid abnormalities are associated with female infertility. Affected females show an ovarian deficit due to primary amenorrhea or to premature ovarian failure (POF). In type II BPSE (BPES2) affected individuals show only the eyelid defects. {ECO:0000269|PubMed:11175783, ECO:0000269|PubMed:11468277, ECO:0000269|PubMed:12400065, ECO:0000269|PubMed:12529855, ECO:0000269|PubMed:12630957, ECO:0000269|PubMed:12938087, ECO:0000269|PubMed:15257268, ECO:0000269|PubMed:16454982, ECO:0000269|PubMed:17089161, ECO:0000269|PubMed:18484667, ECO:0000269|PubMed:18642388, ECO:0000269|Ref.2}. Note=The disease is caused by mutations affecting the gene represented in this entry. There is a mutational hotspot in the region coding for the poly-Ala domain, since 30% of all mutations in the ORF lead to poly-Ala expansions, resulting mainly in BPES type II.; DISEASE: Premature ovarian failure 3 (POF3) [MIM:608996]: An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol. {ECO:0000269|PubMed:12149404, ECO:0000269|PubMed:19429596}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In addition to its expression in the developing eyelid, it is transcribed very early in somatic cells of the developing gonad (before sex determination) and its expression persists in the follicular cells of the adult ovary.; unclassifiable (Anatomical System);uterus;ovary;placenta;parathyroid;cervix; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.16474 0.41578 . . 1425.70829 7.05187 FOXL2NB . . . FOXL2 neighbor . . . . . . . 0.679884223 84.81363529 . . FOXM1 0.802589769159313 0.197400757693072 9.4731476144222e-06 forkhead box M1 FUNCTION: Transcriptional factor regulating the expression of cell cycle genes essential for DNA replication and mitosis. Plays a role in the control of cell proliferation. Plays also a role in DNA breaks repair participating in the DNA damage checkpoint response. {ECO:0000269|PubMed:17101782, ECO:0000269|PubMed:19160488, ECO:0000269|PubMed:20360045}.; . TISSUE SPECIFICITY: Expressed in thymus, testis, small intestine, colon followed by ovary. Appears to be expressed only in adult organs containing proliferating/cycling cells or in response to growth factors. Also expressed in epithelial cell lines derived from tumors. Not expressed in resting cells. Isoform 2 is highly expressed in testis.; medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;muscle;urinary;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;testis;tumor; 0.75033 0.64204 0.361913759 74.69922151 1962.3687 8.16089 FOXN1 0.969497551741561 0.0304932311468119 9.21711162709766e-06 forkhead box N1 FUNCTION: Transcriptional regulator which regulates the development, differentiation, and function of thymic epithelial cells (TECs) both in the prenatal and postnatal thymus. Acts as a master regulator of the TECs lineage development and is required from the onset of differentiation in progenitor TECs in the developing fetus to the final differentiation steps through which TECs mature to acquire their full functionality. Regulates, either directly or indirectly the expression of a variety of genes that mediate diverse aspects of thymus development and function, including MHC Class II, DLL4, CCL25, CTSL, CD40 and PAX1. Regulates the differentiation of the immature TECs into functional cortical TECs (cTECs) and medullary TECs (mTECs). Essential for maintenance of mTECs population in the postnatal thymus. Involved in the morphogenesis and maintenance of the three-dimensional thymic microstructure which is necessary for a fully functional thymus. Plays an important role in the maintenance of hematopoiesis and particularly T lineage progenitors within the bone marrow niche with age. Essential for the vascularization of the thymus anlage. Promotes the terminal differentiation of epithelial cells in the epidermis and hair follicles, partly by negatively regulating the activity of protein kinase C (By similarity). Plays a crucial role in the early prenatal stages of T cell ontogeny (PubMed:21507891). {ECO:0000250|UniProtKB:Q61575, ECO:0000269|PubMed:21507891}.; . TISSUE SPECIFICITY: Expressed in thymus.; larynx;head and neck; superior cervical ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.48685 0.24513 -0.216746887 37.69757018 2393.45251 9.08407 FOXN2 0.392770620749062 0.605228496102159 0.00200088314877944 forkhead box N2 FUNCTION: Binds to the purine-rich region in HTLV-I LTR.; . . unclassifiable (Anatomical System);ovary;colon;parathyroid;blood;skin;skeletal muscle;uterus;bile duct;prostate;pancreas;whole body;lung;frontal lobe;larynx;thyroid;placenta;liver;testis;head and neck;germinal center;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.61165 0.16462 -0.736552314 13.93606983 20.06643 0.68556 FOXN3 0.907799359973324 0.0920512326597177 0.000149407366958792 forkhead box N3 FUNCTION: Acts as a transcriptional repressor. May be involved in DNA damage-inducible cell cycle arrests (checkpoints). {ECO:0000269|PubMed:16102918}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;thymus;cerebellum; dorsal root ganglion;superior cervical ganglion;medulla oblongata;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.74209 0.17554 -0.356299879 29.31115829 47.54211 1.33837 FOXN3-AS1 . . . FOXN3 antisense RNA 1 . . . . . . . . . . . FOXN3-AS2 . . . FOXN3 antisense RNA 2 . . . . . . . . . . . FOXN3P1 . . . forkhead box N3 pseudogene 1 . . . . . . . . . . . FOXN4 0.133060550432118 0.780118037540766 0.0868214120271157 forkhead box N4 FUNCTION: Transcription factor essential for neural and some non- neural tissues development, such as retina and lung respectively. Binds to an 11-bp consensus sequence containing the invariant tetranucleotide 5'-ACGC-3'. During development of the central nervous system, is required to specify the amacrine and horizontal cell fates from multipotent retinal progenitors while suppressing the alternative photoreceptor cell fates through activating DLL4- NOTCH signaling. Also acts synergistically with ASCL1/MASH1 to activate DLL4-NOTCH signaling and drive commitment of p2 progenitors to the V2b interneuron fates during spinal cord neurogenesis. In development of non-neural tissues, plays an essential role in the specification of the atrioventricular canal and is indirectly required for patterning the distal airway during lung development (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;lung;testis; . 0.16734 0.15176 -0.135838822 43.77211607 157.5309 2.74249 FOXO1 0.966380393739249 0.0335618040937296 5.78021670210881e-05 forkhead box O1 FUNCTION: Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'- TT[G/A]TTTAC-3'. Activity suppressed by insulin. Main regulator of redox balance and osteoblast numbers and controls bone mass. Orchestrates the endocrine function of the skeleton in regulating glucose metabolism. Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity. Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP. In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC and PCK1. Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and SKT4/MST1. Promotes neural cell death. Mediates insulin action on adipose tissue. Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake. Regulates the transcriptional activity of GADD45A and repair of nitric oxide- damaged DNA in beta-cells. Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner. {ECO:0000250|UniProtKB:Q9R1E0, ECO:0000269|PubMed:10358076, ECO:0000269|PubMed:12228231, ECO:0000269|PubMed:15220471, ECO:0000269|PubMed:15890677, ECO:0000269|PubMed:18356527, ECO:0000269|PubMed:19221179, ECO:0000269|PubMed:20543840, ECO:0000269|PubMed:21245099}.; DISEASE: Rhabdomyosarcoma 2 (RMS2) [MIM:268220]: A form of rhabdomyosarcoma, a highly malignant tumor of striated muscle derived from primitive mesenchymal cells and exhibiting differentiation along rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most frequently occurring soft tissue sarcomas and the most common in children. It occurs in four forms: alveolar, pleomorphic, embryonal and botryoidal rhabdomyosarcomas. Note=The gene represented in this entry may be involved in disease pathogenesis. Chromosomal aberrations involving FOXO1 are found in rhabdomyosarcoma. Translocation (2;13)(q35;q14) with PAX3 and translocation t(1;13)(p36;q14) with PAX7. The resulting protein is a transcriptional activator.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9479491}.; . . 0.97621 0.82936 -0.468351206 23.42533616 329.3803 3.85852 FOXO1B . . . forkhead box O1B pseudogene . . . . . . . . . . . FOXO3 . . . forkhead box O3 FUNCTION: Transcriptional activator which triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress. Recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3'. Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post- transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation. {ECO:0000269|PubMed:10102273, ECO:0000269|PubMed:16751106, ECO:0000269|PubMed:21329882}.; DISEASE: Note=A chromosomal aberration involving FOXO3 is found in secondary acute leukemias. Translocation t(6;11)(q21;q23) with KMT2A/MLL1.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9479491}.; ovary;colon;fovea centralis;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);islets of Langerhans;muscle;adrenal cortex;blood;skeletal muscle;bile duct;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;amnion;spleen;cervix;kidney;stomach;thymus; cerebellum peduncles;prefrontal cortex;atrioventricular node;skeletal muscle; . 0.59462 -0.492218069 22.35786742 267.4981 3.50708 FOXO3B . . . forkhead box O3B pseudogene . . . . . . . . . . . FOXO4 0.861869126511084 0.136069793031167 0.00206108045774861 forkhead box O4 FUNCTION: Transcription factor involved in the regulation of the insulin signaling pathway. Binds to insulin-response elements (IREs) and can activate transcription of IGFBP1. Down-regulates expression of HIF1A and suppresses hypoxia-induced transcriptional activation of HIF1A-modulated genes. Also involved in negative regulation of the cell cycle. Involved in increased proteasome activity in embryonic stem cells (ESCs) by activating expression of PSMD11 in ESCs, leading to enhanced assembly of the 26S proteasome, followed by higher proteasome activity. {ECO:0000269|PubMed:10217147, ECO:0000269|PubMed:10783894, ECO:0000269|PubMed:12761217, ECO:0000269|PubMed:15126506, ECO:0000269|PubMed:16054032, ECO:0000269|PubMed:16964248, ECO:0000269|PubMed:20874444, ECO:0000269|PubMed:22972301}.; DISEASE: Note=A chromosomal aberration involving FOXO4 is found in acute leukemias. Translocation t(X;11)(q13;q23) with KMT2A/MLL1. The result is a rogue activator protein.; TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Isoform zeta is most abundant in the liver, kidney, and pancreas.; unclassifiable (Anatomical System);ovary;larynx;placenta;liver;parathyroid;blood;head and neck;brain;bone marrow; superior cervical ganglion;placenta;atrioventricular node;trigeminal ganglion; 0.83176 0.23122 -0.229483771 36.86010852 14.66357 0.52852 FOXO6 0.437580050850403 0.457701286822953 0.104718662326644 forkhead box O6 FUNCTION: Transcriptional activator. {ECO:0000250}.; . . . . . . . . 2056.27016 8.35718 FOXP1 0.999750735055125 0.00024926493019828 1.46767288016392e-11 forkhead box P1 FUNCTION: Transcriptional repressor (PubMed:18347093). Can act with CTBP1 to synergistically repress transcription but CTPBP1 is not essential (By similarity). Plays an important role in the specification and differentiation of lung epithelium. Acts cooperatively with FOXP4 to regulate lung secretory epithelial cell fate and regeneration by restricting the goblet cell lineage program; the function may involve regulation of AGR2. Essential transcriptional regulator of B-cell development. Involved in regulation of cardiac muscle cell proliferation. Involved in the columnar organization of spinal motor neurons. Promotes the formation of the lateral motor neuron column (LMC) and the preganglionic motor column (PGC) and is required for respective appropriate motor axon projections. The segment-appropriate generation of spinal chord motor columns requires cooperation with other Hox proteins. Can regulate PITX3 promoter activity; may promote midbrain identity in embryonic stem cell-derived dopamine neurons by regulating PITX3. Negatively regulates the differentiation of T follicular helper cells T(FH)s. Involved in maintainance of hair follicle stem cell quiescence; the function probably involves regulation of FGF18 (By similarity). Represses transcription of various pro-apoptotic genes and cooperates with NF-kappa B-signaling in promoting B-cell expansion by inhibition of caspase-dependent apoptosis (PubMed:25267198). Binds to CSF1R promoter elements and is involved in regulation of monocyte differentiation and macrophage functions; repression of CSF1R in monocytes seems to involve NCOR2 as corepressor (PubMed:15286807, PubMed:18799727, PubMed:18347093). Involved in endothelial cell proliferation, tube formation and migration indicative for a role in angiogenesis; the role in neovascularization seems to implicate suppression of SEMA5B (PubMed:24023716). Can negatively regulate androgen receptor signaling (PubMed:18640093). {ECO:0000250|UniProtKB:P58462, ECO:0000269|PubMed:15286807, ECO:0000269|PubMed:18640093, ECO:0000269|PubMed:18799727, ECO:0000269|PubMed:24023716, ECO:0000269|PubMed:25267198, ECO:0000305|PubMed:18347093, ECO:0000305|PubMed:24023716}.; DISEASE: Note=A chromosomal aberration involving FOXP1 is found in acute lymphoblastic leukemia. Translocation t(9;3)(p13;p14.1) with PAX5.; DISEASE: Mental retardation with language impairment and autistic features (MRLIAF) [MIM:613670]: A developmental disorder characterized by mild to moderate mental retardation, language impairment, and autistic features. Patients show global delay, delayed walking, severely delayed speech development, and behavioral abnormalities, including irritability, hyperactivity, aggression, and stereotypical rigid behaviors. {ECO:0000269|PubMed:20950788}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 8 is specifically expressed in embryonic stem cells. {ECO:0000269|PubMed:21924763}.; ovary;umbilical cord;rectum;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.57291 0.32628 -0.378346116 28.01368247 60.34446 1.57849 FOXP1-AS1 . . . FOXP1 antisense RNA 1 . . . . . . . . . . . FOXP1-IT1 . . . FOXP1 intronic transcript 1 . . . . . . . . . . . FOXP2 0.996178831092855 0.00382116881276149 9.43833931347474e-11 forkhead box P2 FUNCTION: Transcriptional repressor that may play a role in the specification and differentiation of lung epithelium. May also play a role in developing neural, gastrointestinal and cardiovascular tissues. Can act with CTBP1 to synergistically repress transcription but CTPBP1 is not essential. Plays a role in synapse formation by regulating SRPX2 levels. Involved in neural mechanisms mediating the development of speech and language.; DISEASE: Speech-language disorder 1 (SPCH1) [MIM:602081]: A disorder characterized by severe orofacial dyspraxia resulting in largely incomprehensible speech. Affected individuals have severe impairment in the selection and sequencing of fine orofacial movements which are necessary for articulation, and deficits in several facets of grammatical skills and language processing, such as the ability to break up words into their constituent phonemes. {ECO:0000269|PubMed:11586359}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving FOXP2 is a cause of severe speech and language impairment. Translocation t(5;7)(q22;q31.2).; TISSUE SPECIFICITY: Isoform 1 and isoform 6 are expressed in adult and fetal brain, caudate nucleus and lung. {ECO:0000269|PubMed:12189486}.; unclassifiable (Anatomical System);uterus;optic nerve;macula lutea;fovea centralis;choroid;kidney;lens;skin;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.91139 0.65138 -0.824740496 11.67728238 219.19563 3.20141 FOXP3 0.948721767538971 0.0511128713514846 0.000165361109544365 forkhead box P3 FUNCTION: Transcriptional regulator which is crucial for the development and inhibitory function of regulatory T-cells (Treg). Plays an essential role in maintaining homeostasis of the immune system by allowing the acquisition of full suppressive function and stability of the Treg lineage, and by directly modulating the expansion and function of conventional T-cells. Can act either as a transcriptional repressor or a transcriptional activator depending on its interactions with other transcription factors, histone acetylases and deacetylases. The suppressive activity of Treg involves the coordinate activation of many genes, including CTLA4 and TNFRSF18 by FOXP3 along with repression of genes encoding cytokines such as interleukin-2 (IL2) and interferon- gamma (IFNG). Inhibits cytokine production and T-cell effector function by repressing the activity of two key transcription factors, RELA and NFATC2 (PubMed:15790681). Mediates transcriptional repression of IL2 via its association with histone acetylase KAT5 and histone deacetylase HDAC7 (PubMed:17360565). Can activate the expression of TNFRSF18, IL2RA and CTLA4 and repress the expression of IL2 and IFNG via its association with transcription factor RUNX1 (PubMed:17377532). Inhibits the differentiation of IL17 producing helper T-cells (Th17) by antagonizing RORC function, leading to down-regulation of IL17 expression, favoring Treg development (PubMed:18368049). Inhibits the transcriptional activator activity of RORA (PubMed:18354202). Can repress the expression of IL2 and IFNG via its association with transcription factor IKZF4 (By similarity). {ECO:0000250|UniProtKB:Q99JB6, ECO:0000269|PubMed:15790681, ECO:0000269|PubMed:17360565, ECO:0000269|PubMed:17377532, ECO:0000269|PubMed:18354202, ECO:0000269|PubMed:18368049, ECO:0000269|PubMed:23169781}.; DISEASE: Immunodeficiency polyendocrinopathy, enteropathy, X- linked syndrome (IPEX) [MIM:304790]: Characterized by neonatal onset insulin-dependent diabetes mellitus, infections, secretory diarrhea, thrombocytopenia, anemia and eczema. It is usually lethal in infancy. {ECO:0000269|PubMed:11120765, ECO:0000269|PubMed:11137992, ECO:0000269|PubMed:11137993, ECO:0000269|PubMed:11768393}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.38658 0.53010 -0.249709319 35.74545883 42.16868 1.22709 FOXP4 0.671770825297787 0.328186984802943 4.21898992701699e-05 forkhead box P4 FUNCTION: Transcriptional repressor that represses lung-specific expression. {ECO:0000250}.; . . colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.55342 0.15286 -0.951568548 9.271054494 131.44683 2.49577 FOXP4-AS1 . . . FOXP4 antisense RNA 1 . . . . . . . . . . . FOXQ1 . . . forkhead box Q1 FUNCTION: Plays a role in hair follicle differentiation. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed predominantly in the stomach, trachea, bladder and salivary gland. {ECO:0000269|PubMed:11747606}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;endometrium;testis;bladder;brain;unclassifiable (Anatomical System);islets of Langerhans;oral cavity;urinary;pharynx;blood;lens;breast;lung;macula lutea;liver;head and neck;cervix;kidney;stomach;peripheral nerve; . 0.08176 . . . 1694.04107 7.58825 FOXR1 0.00292657754004723 0.941813283241781 0.0552601392181716 forkhead box R1 . . . unclassifiable (Anatomical System);medulla oblongata;testis; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09967 0.15417 0.150760231 64.51403633 122.94463 2.41448 FOXR2 0.00256624410589497 0.552621714370202 0.444812041523903 forkhead box R2 . . TISSUE SPECIFICITY: Expressed in breast cancer cell lines and primary cancer. {ECO:0000269|PubMed:15202009}.; . . . 0.09268 0.12689526 63.00424628 8.51821 0.31277 FOXRED1 4.09171835158384e-11 0.175564849822612 0.824435150136471 FAD-dependent oxidoreductase domain containing 1 FUNCTION: Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) (PubMed:20858599, PubMed:25678554). Involved in mid-late stages of complex I assembly (PubMed:25678554). {ECO:0000269|PubMed:20858599, ECO:0000269|PubMed:25678554}.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:20818383, ECO:0000269|PubMed:20858599}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;salivary gland;intestine;colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;pharynx;blood;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;alveolus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.02675 0.08568 -0.400392389 26.85185185 2969.42193 10.33406 FOXRED2 0.00691546683994862 0.989416458695432 0.003668074464619 FAD dependent oxidoreductase domain containing 2 FUNCTION: Probable flavoprotein which may function in endoplasmic reticulum associated degradation (ERAD). May bind non-native proteins in the endoplasmic reticulum and target them to the ubiquitination machinery for subsequent degradation. {ECO:0000269|PubMed:19706418}.; . . unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;temporal lobe;colon;fovea centralis;choroid;lens;skin;retina;bile duct;pancreas;optic nerve;frontal lobe;endometrium;thyroid;macula lutea;liver;testis;cervix;kidney;brain;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skeletal muscle; 0.11152 . 0.586023223 82.34843123 888.12063 5.80446 FOXS1 0.0996331503834563 0.772102357199547 0.128264492416996 forkhead box S1 FUNCTION: Transcriptional repressor that suppresses transcription from the FASLG, FOXO3 and FOXO4 promoters. May have a role in the organization of the testicular vasculature (By similarity). {ECO:0000250}.; . . . . 0.08878 0.09740 0.132352165 63.48785091 168.08155 2.83022 FPGS 0.000112877619093231 0.988716023195936 0.0111710991849712 folylpolyglutamate synthase FUNCTION: Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis. Unsubstituted reduced folates are the preferred substrates. Metabolizes methotrexate (MTX) to polyglutamates. {ECO:0000269|PubMed:8408018, ECO:0000269|PubMed:8408019, ECO:0000269|PubMed:8408021, ECO:0000269|PubMed:8662720}.; . . . . 0.08683 0.26961 -0.534490515 20.70063694 105.84338 2.22990 FPGT 5.97096312971038e-08 0.242753725300415 0.757246214989954 fucose-1-phosphate guanylyltransferase FUNCTION: Catalyzes the formation of GDP-L-fucose from GTP and L- fucose-1-phosphate. Functions as a salvage pathway to reutilize L- fucose arising from the turnover of glycoproteins and glycolipids.; . TISSUE SPECIFICITY: Expressed in many tissues.; . . . 0.10778 0.398725314 76.35645199 82.23723 1.92473 FPGT-TNNI3K 1.84157554257575e-38 1.3479002055496e-07 0.999999865209979 FPGT-TNNI3K readthrough FUNCTION: May play a role in cardiac physiology. {ECO:0000303|PubMed:12721663}.; DISEASE: Cardiac conduction disease with or without dilated cardiomyopathy (CCDD) [MIM:616117]: A cardiac disorder characterized by atrial tachyarrhythmia and conduction system disease. Some patients have dilated cardiomyopathy. {ECO:0000269|PubMed:24925317}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in both adult and fetal heart. {ECO:0000269|PubMed:12721663}.; unclassifiable (Anatomical System);uterus;lung;heart;liver;testis;kidney;skin; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . -0.389485787 27.07596131 415.57781 4.26754 FPR1 0.0638058133694423 0.726496015715005 0.209698170915552 formyl peptide receptor 1 FUNCTION: High affinity receptor for N-formyl-methionyl peptides (fMLP), which are powerful neutrophil chemotactic factors (PubMed:2161213, PubMed:2176894, PubMed:10514456, PubMed:15153520). Binding of fMLP to the receptor stimulates intracellular calcium mobilization and superoxide anion release (PubMed:2161213, PubMed:1712023, PubMed:15153520). This response is mediated via a G-protein that activates a phosphatidylinositol- calcium second messenger system (PubMed:1712023, PubMed:10514456). {ECO:0000269|PubMed:10514456, ECO:0000269|PubMed:15153520, ECO:0000269|PubMed:2161213, ECO:0000269|PubMed:2176894, ECO:0000303|PubMed:10514456, ECO:0000303|PubMed:1712023, ECO:0000303|PubMed:2161213, ECO:0000303|PubMed:2176894}.; . TISSUE SPECIFICITY: Neutrophils.; ovary;colon;fovea centralis;choroid;retina;bone marrow;uterus;optic nerve;whole body;endometrium;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;hippocampus;liver;alveolus;spleen;kidney;mammary gland;stomach; whole blood;bone marrow; 0.05324 0.19446 1.131742211 92.26232602 1727.75864 7.66928 FPR2 0.0191752897136947 0.735298153217378 0.245526557068927 formyl peptide receptor 2 FUNCTION: Low affinity receptor for N-formyl-methionyl peptides, which are powerful neutrophils chemotactic factors. Binding of FMLP to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. The activation of LXA4R could result in an anti-inflammatory outcome counteracting the actions of proinflammatory signals such as LTB4 (leukotriene B4).; . TISSUE SPECIFICITY: Expressed abundantly in the lung and neutrophils. Also found in the spleen and testis. {ECO:0000269|PubMed:9151906}.; unclassifiable (Anatomical System);lung;placenta; superior cervical ganglion;whole blood;bone marrow; 0.06779 0.22129 -0.314027422 31.9297004 45.66154 1.29807 FPR3 0.113913457642539 0.778211705753505 0.107874836603956 formyl peptide receptor 3 FUNCTION: Low affinity receptor for N-formyl-methionyl peptides, which are powerful neutrophils chemotactic factors. Binding of FMLP to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system.; . . unclassifiable (Anatomical System);pancreas;lung;islets of Langerhans;nasopharynx;placenta;brain;skeletal muscle;stomach;thymus; superior cervical ganglion;skeletal muscle; 0.03991 0.08342 -0.271755481 34.31823543 10.87508 0.39346 FRA1A . . . fragile site, aphidicolin type, common, fra(1)(p36) . . . . . . . . . . . FRA1B . . . fragile site, aphidicolin type, common, fra(1)(p32) . . . . . . . . . . . FRA1C . . . fragile site, aphidicolin type, common, fra(1)(p31.2) . . . . . . . . . . . FRA1D . . . fragile site, aphidicolin type, common, fra(1)(p22) . . . . . . . . . . . FRA1E . . . fragile site, aphidicolin type, common, fra(1)(p21.2) . . . . . . . . . . . FRA1F . . . fragile site, aphidicolin type, common, fra(1)(q21) . . . . . . . . . . . FRA1G . . . fragile site, aphidicolin type, common, fra(1)(q25.1) . . . . . . . . . . . FRA1H . . . fragile site, 5-azacytidine type, common, fra(1)(q42) . . . . . . . . . . . FRA1I . . . fragile site, aphidicolin type, common, fra(1)(q44) . . . . . . . . . . . FRA1J . . . fragile site, 5-azacytidine type, common, fra(1)(q12) . . . . . . . . . . . FRA1K . . . fragile site, aphidicolin type, common, fra(1)(q31) . . . . . . . . . . . FRA1L . . . fragile site, aphidicolin type, common, fra(1)(p31) . . . . . . . . . . . FRA1M . . . fragile site, folic acid type, rare, fra(1)(p21.3) . . . . . . . . . . . FRA2A . . . fragile site, folic acid type, rare, fra(2)(q11.2) . . . . . . . . . . . FRA2B . . . fragile site, folic acid type, rare, fra(2)(q13) . . . . . . . . . . . FRA2C . . . fragile site, aphidicolin type, common, fra(2)(p24.2) . . . . . . . . . . . FRA2D . . . fragile site, aphidicolin type, common, fra(2)(p16.2) . . . . . . . . . . . FRA2E . . . fragile site, aphidicolin type, common, fra(2)(p13) . . . . . . . . . . . FRA2F . . . fragile site, aphidicolin type, common, fra(2)(q21.3) . . . . . . . . . . . FRA2G . . . fragile site, aphidicolin type, common, fra(2)(q31) . . . . . . . . . . . FRA2H . . . fragile site, aphidicolin type, common, fra(2)(q32.1) . . . . . . . . . . . FRA2I . . . fragile site, aphidicolin type, common, fra(2)(q33) . . . . . . . . . . . FRA2J . . . fragile site, aphidicolin type, common, fra(2)(q37.3) . . . . . . . . . . . FRA2K . . . fragile site, folic acid type, rare, fra(2)(q22.3) . . . . . . . . . . . FRA3A . . . fragile site, aphidicolin type, common, fra(3)(p24.2) . . . . . . . . . . . FRA3B . . . fragile site, aphidicolin type, common, fra(3)(p14.2) . . . . . . . . . . . FRA3C . . . fragile site, aphidicolin type, common, fra(3)(q27) . . . . . . . . . . . FRA3D . . . fragile site, aphidicolin type, common, fra(3)(q25) . . . . . . . . . . . FRA4A . . . fragile site, aphidicolin type, common, fra(4)(p16.1) . . . . . . . . . . . FRA4B . . . fragile site, BrdU type, common, fra(4)(q12) . . . . . . . . . . . FRA4C . . . fragile site, aphidicolin type, common, fra(4)(q31.1) . . . . . . . . . . . FRA4D . . . fragile site, aphidicolin type, common, fra(4)(p15) . . . . . . . . . . . FRA5A . . . fragile site, BrdU type, common, fra(5)(p13) . . . . . . . . . . . FRA5B . . . fragile site, BrdU type, common, fra(5)(q15) . . . . . . . . . . . FRA5C . . . fragile site, aphidicolin type, common, fra(5)(q31.1) . . . . . . . . . . . FRA5D . . . fragile site, aphidicolin type, common, fra(5)(q15) . . . . . . . . . . . FRA5E . . . fragile site, aphidicolin type, common, fra(5)(p14) . . . . . . . . . . . FRA5F . . . fragile site, aphidicolin type, common, fra(5)(q21) . . . . . . . . . . . FRA5G . . . fragile site, folic acid type, rare, fra(5)(q35) . . . . . . . . . . . FRA6A . . . fragile site, folic acid type, rare, fra(6)(p23) . . . . . . . . . . . FRA6B . . . fragile site, aphidicolin type, common, fra(6)(p25.1) . . . . . . . . . . . FRA6C . . . fragile site, aphidicolin type, common, fra(6)(p22.2) . . . . . . . . . . . FRA6D . . . fragile site, BrdU type, common, fra(6)(q13) . . . . . . . . . . . FRA6E . . . fragile site, aphidicolin type, common, fra(6)(q26) . . . . . . . . . . . FRA6F . . . fragile site, aphidicolin type, common, fra(6)(q21) . . . . . . . . . . . FRA6G . . . fragile site, aphidicolin type, common, fra(6)(q15) . . . . . . . . . . . FRA7A . . . fragile site, folic acid type, rare, fra(7)(p11.2) . . . . . . . . . . . FRA7B . . . fragile site, aphidicolin type, common, fra(7)(p22) . . . . . . . . . . . FRA7C . . . fragile site, aphidicolin type, common, fra(7)(p14.2) . . . . . . . . . . . FRA7D . . . fragile site, aphidicolin type, common, fra(7)(p13) . . . . . . . . . . . FRA7E . . . fragile site, aphidicolin type, common, fra(7)(q21.2) . . . . . . . . . . . FRA7F . . . fragile site, aphidicolin type, common, fra(7)(q22) . . . . . . . . . . . FRA7G . . . fragile site, aphidicolin type, common, fra(7)(q31.2) . . . . . . . . . . . FRA7H . . . fragile site, aphidicolin type, common, fra(7)(q32.3) . . . . . . . . . . . FRA7I . . . fragile site, aphidicolin type, common, fra(7)(q36) . . . . . . . . . . . FRA7J . . . fragile site, aphidicolin type, common, fra(7)(q11) . . . . . . . . . . . FRA8A . . . fragile site, folic acid type, rare, fra(8)(q22.3) . . . . . . . . . . . FRA8B . . . fragile site, aphidicolin type, common, fra(8)(q22.1) . . . . . . . . . . . FRA8C . . . fragile site, aphidicolin type, common, fra(8)(q24.1) . . . . . . . . . . . FRA8D . . . fragile site, aphidicolin type, common, fra(8)(q24.3) . . . . . . . . . . . FRA8E . . . fragile site, distamycin A type, rare, fra(8)(q24.1) . . . . . . . . . . . FRA9A . . . fragile site, folic acid type, rare, fra(9)(p21) . . . . . . . . . . . FRA9B . . . fragile site, folic acid type, rare, fra(9)(q32) . . . . . . . . . . . FRA9C . . . fragile site, BrdU type, common, fra(9)(p21) . . . . . . . . . . . FRA9D . . . fragile site, aphidicolin type, common, fra(9)(q22.1) . . . . . . . . . . . FRA9E . . . fragile site, aphidicolin type, common, fra(9)(q32) . . . . . . . . . . . FRA9F . . . fragile site, 5-azacytidine type, common, fra(9)(q12) . . . . . . . . . . . FRA10A . . . fragile site, folic acid type, rare, fra(10)(q23.3) or fra(10)(q24.2) . . . . . . . . . . . FRA10AC1 9.71537508229325e-10 0.159952787245073 0.840047211783389 fragile site, folic acid type, rare, fra(10)(q23.3) or fra(10)(q24.2) candidate 1 . . TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in brain, heart, skeletal muscle, kidney and liver. {ECO:0000269|PubMed:15203205}.; . . 0.12222 0.08299 0.749657564 86.56522765 3720.54582 11.91644 FRA10B . . . fragile site, BrdU type, rare, fra(10)(q25.2) . . . . . . . . . . . FRA10C . . . fragile site, BrdU type, common, fra(10)(q21) . . . . . . . . . . . FRA10D . . . fragile site, aphidicolin type, common, fra(10)(q22.1) . . . . . . . . . . . FRA10E . . . fragile site, aphidicolin type, common, fra(10)(q25.2) . . . . . . . . . . . FRA10F . . . fragile site, aphidicolin type, common, fra(10)(q26.1) . . . . . . . . . . . FRA10G . . . fragile site, aphidicolin type, common, fra(10)(q11.2) . . . . . . . . . . . FRA11A . . . fragile site, folic acid type, rare, fra(11)(q13.3) . . . . . . . . . . . FRA11B . . . fragile site, folic acid type, rare, fra(11)(q23.3) . . . . . . . . . . . FRA11C . . . fragile site, aphidicolin type, common, fra(11)(p15.1) . . . . . . . . . . . FRA11D . . . fragile site, aphidicolin type, common, fra(11)(p14.2) . . . . . . . . . . . FRA11E . . . fragile site, aphidicolin type, common, fra(11)(p13) . . . . . . . . . . . FRA11F . . . fragile site, aphidicolin type, common, fra(11)(q14.2) . . . . . . . . . . . FRA11G . . . fragile site, aphidicolin type, common, fra(11)(q23.3) . . . . . . . . . . . FRA11H . . . fragile site, aphidicolin type, common, fra(11)(q13) . . . . . . . . . . . FRA11I . . . fragile site, distamycin A type, rare, fra(11)(p15.1) . . . . . . . . . . . FRA12A . . . fragile site, folic acid type, rare, fra(12)(q13.1) . . . . . . . . . . . FRA12B . . . fragile site, aphidicolin type, common, fra(12)(q21.3) . . . . . . . . . . . FRA12C . . . fragile site, BrdU type, rare, fra(12)(q24.2) . . . . . . . . . . . FRA12D . . . fragile site, folic acid type, rare, fra(12)(q24.13) . . . . . . . . . . . FRA12E . . . fragile site, aphidicolin type, common, fra(12)(q24) . . . . . . . . . . . FRA13A . . . fragile site, aphidicolin type, common, fra(13)(q13.2) . . . . . . . . . . . FRA13B . . . fragile site, BrdU type, common, fra(13)(q21) . . . . . . . . . . . FRA13C . . . fragile site, aphidicolin type, common, fra(13)(q21.2) . . . . . . . . . . . FRA13D . . . fragile site, aphidicolin type, common, fra(13)(q32) . . . . . . . . . . . FRA14B . . . fragile site, aphidicolin type, common, fra(14)(q23) . . . . . . . . . . . FRA14C . . . fragile site, aphidicolin type, common, fra(14)(q24.1) . . . . . . . . . . . FRA15A . . . fragile site, aphidicolin type, common, fra(15)(q22) . . . . . . . . . . . FRA16A . . . fragile site, folic acid type, rare, fra(16)(p13.11) . . . . . . . . . . . FRA16B . . . fragile site, distamycin A type, rare, fra(16)(q22.1) . . . . . . . . . . . FRA16C . . . fragile site, aphidicolin type, common, fra(16)(q22.1) . . . . . . . . . . . FRA16D . . . fragile site, aphidicolin type, common, fra(16)(q23.2) . . . . . . . . . . . FRA16E . . . fragile site, distamycin A type, rare, fra(16)(p12.1) . . . . . . . . . . . FRA17A . . . fragile site, distamycin A type, rare, fra(17)(p12) . . . . . . . . . . . FRA17B . . . fragile site, aphidicolin type, common, fra(17)(q23.1) . . . . . . . . . . . FRA18A . . . fragile site, aphidicolin type, common, fra(18)(q12.2) . . . . . . . . . . . FRA18B . . . fragile site, aphidicolin type, common, fra(18)(q21.3) . . . . . . . . . . . FRA18C . . . fragile site, aphidicolin type, common, fra(18)(q22.2) . . . . . . . . . . . FRA19A . . . fragile site, 5-azacytidine type, common, fra(19)(q13) . . . . . . . . . . . FRA19B . . . fragile site, folic acid type, rare, fra(19)(p13) . . . . . . . . . . . FRA20A . . . fragile site, folic acid type, rare, fra(20)(p11.23) . . . . . . . . . . . FRA20B . . . fragile site, aphidicolin type, common, fra(20)(p12.2) . . . . . . . . . . . FRA22A . . . fragile site, folic acid type, rare, fra(22)(q13) . . . . . . . . . . . FRA22B . . . fragile site, aphidicolin type, common, fra(22)(q12.2) . . . . . . . . . . . FRAS1 2.28997696302965e-23 0.999999999208951 7.91049436331022e-10 Fraser extracellular matrix complex subunit 1 . DISEASE: Fraser syndrome (FRASS) [MIM:219000]: Multisystem malformation usually comprising cryptophthalmos, cutaneous syndactyly, ear abnormalities, renal agenesis and congenital heart defects. {ECO:0000269|PubMed:23473829}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in many adult tissues, with highest levels in kidney, pancreas and thalamus. Relatively high expression was also detected in fetal kidney and heart. {ECO:0000269|PubMed:12766769}.; unclassifiable (Anatomical System);cartilage;heart;muscle;colon;skin;skeletal muscle;lung;frontal lobe;endometrium;adrenal gland;larynx;bone;placenta;thyroid;visual apparatus;liver;testis;head and neck;spleen;kidney;brain;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;pancreas;globus pallidus;ciliary ganglion;atrioventricular node;caudate nucleus;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.59318 0.10946 4.646228703 99.76999292 7813.79024 19.03935 FRAT1 0.271480885095774 0.635119927567285 0.0933991873369409 frequently rearranged in advanced T-cell lymphomas 1 FUNCTION: Positively regulates the Wnt signaling pathway by stabilizing beta-catenin through the association with GSK-3. May play a role in tumor progression and collaborate with PIM1 and MYC in lymphomagenesis. {ECO:0000269|PubMed:12556519}.; . . . . 0.22939 0.16985 . . 15.02957 0.53957 FRAT2 0.630848044064571 0.339283492093716 0.029868463841713 frequently rearranged in advanced T-cell lymphomas 2 FUNCTION: Positively regulates the Wnt signaling pathway by stabilizing beta-catenin through the association with GSK-3.; . . . . 0.74070 0.13782 . . 736.11623 5.38355 FRAXA . . . fragile site, folic acid type, rare, fra(X)(q27.3) A (macroorchidism, mental retardation) . . . . . . . . . . . FRAXB . . . fragile site, aphidicolin type, common, fra(X)(p22.31) B . . . . . . . . . . . FRAXC . . . fragile site, aphidicolin type, common, fra(X)(q22.1) C . . . . . . . . . . . FRAXD . . . fragile site, aphidicolin type, common, fra(X)(q27.2) D . . . . . . . . . . . FRAXE . . . fragile site, folic acid type, rare, fra(X)(q28) E . . . . . . . . . . . FRAXF . . . fragile site, folic acid type, rare, fra(X)(q28) F . . . . . . . . . . . FRDA2 . . . Friedreich ataxia 2 . . . . . . . . . . . FREM1 . . . FRAS1 related extracellular matrix 1 FUNCTION: Extracellular matrix protein that plays a role in epidermal differentiation and is required for epidermal adhesion during embryonic development. {ECO:0000250}.; DISEASE: Bifid nose, with or without anorectal and renal anomalies (BNAR) [MIM:608980]: A disease characterized by the presence of a bifid nose usually associated with renal agenesis and anorectal malformations. A bifid nose is a congenital deformity due to failure of the paired nasal processes to fuse to a single midline organ during early gestation. {ECO:0000269|PubMed:19732862}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Manitoba oculotrichoanal syndrome (MOTA) [MIM:248450]: A rare condition defined by eyelid colobomas, cryptophthalmos, and anophthalmia/microphthalmia, an aberrant hairline, a bifid or broad nasal tip, and gastrointestinal anomalies such as omphalocele and anal stenosis. {ECO:0000269|PubMed:21507892}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Trigonocephaly 2 (TRIGNO2) [MIM:614485]: A keel-shaped deformation of the forehead, caused by premature fusion of the metopic sutures. It results in a triangular shape of the head. {ECO:0000269|PubMed:21931569}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.10036 0.10225 -0.625172172 17.03821656 4944.55241 14.32186 FREM2 1.25164781172615e-07 0.999999873248075 1.58714419144731e-09 FRAS1 related extracellular matrix protein 2 FUNCTION: Extracellular matrix protein required for maintenance of the integrity of the skin epithelium and for maintenance of renal epithelia. May be required for epidermal adhesion. {ECO:0000269|PubMed:15838507}.; DISEASE: Fraser syndrome (FRASS) [MIM:219000]: Multisystem malformation usually comprising cryptophthalmos, cutaneous syndactyly, ear abnormalities, renal agenesis and congenital heart defects. {ECO:0000269|PubMed:15838507}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;lung;whole body;endometrium;adrenal gland;sympathetic chain;testis;colon;kidney;mammary gland;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.41290 0.11172 -0.632876892 16.77282378 10803.546 22.53898 FREM2-AS1 . . . FREM2 antisense RNA 1 . . . . . . . . . . . FREM3 . . . FRAS1 related extracellular matrix 3 FUNCTION: Extracellular matrix protein which may play a role in cell adhesion. {ECO:0000250}.; . . . . 0.14428 0.09865 4.072907685 99.67563105 2763.73618 9.92253 FRG1 3.6739295210831e-06 0.359220085781862 0.640776240288617 FSHD region gene 1 FUNCTION: Binds to mRNA in a sequence-independent manner. May play a role in regulation of pre-mRNA splicing or in the assembly of rRNA into ribosomal subunits. May be involved in mRNA transport. May be involved in epigenetic regulation of muscle differentiation through regulation of activity of the histone-lysine N- methyltransferase SUV420H1. {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:15060122, ECO:0000269|PubMed:20970242, ECO:0000269|PubMed:21699900, ECO:0000269|PubMed:23720823}.; . TISSUE SPECIFICITY: Expressed in adult muscle, lymphocytes, fetal brain, muscle, and placenta. Also expressed in the smooth muscle of arteries and veins, the sweat glands and the epidermis. {ECO:0000269|PubMed:20970242}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;pharynx;blood;lens;bile duct;breast;pancreas;lung;nasopharynx;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; . . 0.13913 -0.251530012 35.42108988 86.27493 1.98323 FRG1BP . . . FSHD region gene 1 family member B, pseudogene . . . . . 0.12824 . . . . . FRG1CP . . . FSHD region gene 1 family member C, pseudogene . . . . . . . . . . . FRG1DP . . . FSHD region gene 1 family member D, pseudogene . . . . . . . . . . . FRG1EP . . . FSHD region gene 1 family member E, pseudogene . . . . . . . . . . . FRG1HP . . . FSHD region gene 1 family member H, pseudogene . . . . . . . . . . . FRG1JP . . . FSHD region gene 1 family member J, pseudogene . . . . . . . . . . . FRG1KP . . . FSHD region gene 1 family member K, pseudogene . . . . . . . . . . . FRG2 0.431237852770668 0.460325500334308 0.108436646895025 FSHD region gene 2 . . TISSUE SPECIFICITY: Expression is undetectable in all tissues tested except for differentiating myoblasts of FSHD patients, which display low, yet distinct levels of expression, partly from FRG2, but predominantly originating from its homolog on chromosome 10. {ECO:0000269|PubMed:15520407}.; . . . . . . . . FRG2B 0.152494211914454 0.776845825435888 0.0706599626496584 FSHD region gene 2 family member B . . . . . . . . . 690.57498 5.23946 FRG2C . . . FSHD region gene 2 family member C . . . . . . . . . . . FRG2DP . . . FSHD region gene 2 family member D, pseudogene . . . . . . . . . . . FRG2EP . . . FSHD region gene 2 family member E, pseudogene . . . . . . . . . . . FRG2FP . . . FSHD region gene 2 family member F, pseudogene . . . . . . . . . . . FRG2GP . . . FSHD region gene 2 family member G, pseudogene . . . . . . . . . . . FRG2HP . . . FSHD region gene 2 family member H, pseudogene . . . . . . . . . . . FRG2IP . . . FSHD region gene 2 family member I, pseudogene . . . . . . . . . . . FRG2JP . . . FSHD region gene 2 family member J, pseudogene . . . . . . . . . . . FRG2KP . . . FSHD region gene 2 family member K, pseudogene . . . . . . . . . . . FRG2LP . . . FSHD region gene 2 family member L, pseudogene . . . . . . . . . . . FRG2MP . . . FSHD region gene 2 family member M, pseudogene . . . . . . . . . . . FRGCA . . . FOXM1-regulated, gastric cancer associated . . . . . . . . . . . FRK 6.59374622255819e-10 0.409074597743169 0.590925401597456 fyn related Src family tyrosine kinase FUNCTION: Non-receptor tyrosine-protein kinase that negatively regulates cell proliferation. Positively regulates PTEN protein stability through phosphorylation of PTEN on 'Tyr-336', which in turn prevents its ubiquitination and degradation, possibly by reducing its binding to NEDD4. May function as a tumor suppressor. {ECO:0000269|PubMed:19345329}.; . TISSUE SPECIFICITY: Predominantly expressed in epithelial derived cell lines and tissues, especially normal liver, kidney, breast and colon. {ECO:0000269|PubMed:7696183}.; . . 0.65267 0.16997 -0.332434268 30.74427931 3263.17261 10.89927 FRMD1 5.14902401948958e-13 0.0143284991671232 0.985671500832362 FERM domain containing 1 . . . unclassifiable (Anatomical System);kidney;spinal ganglion; superior cervical ganglion;atrioventricular node; 0.15715 . 1.120636874 92.10309035 503.02609 4.60159 FRMD3 0.195215061672292 0.80433801753169 0.000446920796018704 FERM domain containing 3 FUNCTION: Putative tumor suppressor gene that may be implicated in the origin and progression of lung cancer. {ECO:0000269|PubMed:17260017}.; . TISSUE SPECIFICITY: Ovary-specific. {ECO:0000269|PubMed:12601556}.; unclassifiable (Anatomical System);medulla oblongata;heart;hypothalamus;colon;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;frontal lobe;endometrium;placenta;thyroid;bone;macula lutea;alveolus;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17112 0.11121 0.643056625 84.05284265 440.25802 4.37201 FRMD4A 0.999986541343185 1.34586568031028e-05 1.19861769302975e-14 FERM domain containing 4A . . . smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;brain;bladder;cartilage;heart;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;internal ear;placenta;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.37226 0.10977 -1.570776628 3.172918141 406.77829 4.22856 FRMD4B 0.807013707732818 0.192986277356203 1.49109789645514e-08 FERM domain containing 4B FUNCTION: Member of GRP1 signaling complexes that are acutely recruited to plasma membrane ruffles in response to insulin receptor signaling. May function as a scaffolding protein (By similarity). {ECO:0000250}.; . . . . 0.22435 0.10026 0.85606445 88.52323661 2651.86818 9.67454 FRMD5 0.991843164486017 0.00815676281762829 7.26963544868761e-08 FERM domain containing 5 . . . . . 0.49661 0.10982 0.130533008 63.35810333 105.20777 2.21989 FRMD6 0.438403934830725 0.561537774157949 5.82910113259917e-05 FERM domain containing 6 . . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;atrium;whole body;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;testis - interstitial;medulla oblongata;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.36584 0.15515 -0.909290275 10.03184713 67.82195 1.70422 FRMD6-AS1 . . . FRMD6 antisense RNA 1 . . . . . . . . . . . FRMD6-AS2 . . . FRMD6 antisense RNA 2 . . . . . . . . . . . FRMD7 0.910660048623758 0.0893119909549348 2.79604213073176e-05 FERM domain containing 7 FUNCTION: Plays a role in neurite development, may be through the activation of the GTPase RAC1. Plays a role in the control of eye movement and gaze stability. {ECO:0000250|UniProtKB:A2AD83, ECO:0000269|PubMed:17013395, ECO:0000269|PubMed:23946638}.; DISEASE: Nystagmus congenital X-linked 1 (NYS1) [MIM:310700]: A condition defined as conjugated, spontaneous and involuntary ocular oscillations that appear at birth or during the first three months of life. Other associated features may include mildly decreased visual acuity, strabismus, astigmatism, and occasionally head nodding. {ECO:0000269|PubMed:17013395, ECO:0000269|PubMed:17397053, ECO:0000269|PubMed:17768376, ECO:0000269|PubMed:17893669, ECO:0000269|PubMed:17962394, ECO:0000269|PubMed:18087240, ECO:0000269|PubMed:18246032, ECO:0000269|PubMed:18431453, ECO:0000269|PubMed:21303855, ECO:0000269|PubMed:21365021, ECO:0000269|PubMed:22490987, ECO:0000269|PubMed:23946638}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in liver, kidney, pancreas and at low levels in brain and heart. Expressed in embryonic brain and developing neural retina. {ECO:0000269|PubMed:17013395}.; kidney; superior cervical ganglion;appendix;ciliary ganglion;trigeminal ganglion; 0.15350 0.12382 0.306902668 72.38145789 790.14837 5.54450 FRMD8 0.0842909431231267 0.913673175046831 0.00203588183004193 FERM domain containing 8 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pharynx;blood;skeletal muscle;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.11775 0.10812 -0.154246007 42.22694032 164.96748 2.80897 FRMD8P1 . . . FERM domain containing 8 pseudogene 1 . . . . . . . . . . . FRMPD1 3.5321087486031e-10 0.995711786868788 0.00428821277800116 FERM and PDZ domain containing 1 FUNCTION: Stabilizes membrane-bound GPSM1, and thereby promotes its interaction with GNAI1. {ECO:0000269|PubMed:18566450}.; . . . . 0.15661 0.09359 1.70862952 96.44373673 4200.93656 12.88726 FRMPD2 1.17402718335837e-15 0.250462770592058 0.749537229407941 FERM and PDZ domain containing 2 FUNCTION: May play a role in the regulation of tight junction formation. Binds phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2). {ECO:0000269|PubMed:19706687}.; . TISSUE SPECIFICITY: Expressed in epithelial cells. {ECO:0000269|PubMed:19706687}.; unclassifiable (Anatomical System);choroid;fovea centralis;lens;skeletal muscle;retina;optic nerve;lung;frontal lobe;macula lutea;testis;brain;pineal gland; superior cervical ganglion;olfactory bulb;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.01607 0.09100 -0.65224539 16.15357396 2152.63806 8.53732 FRMPD2B . . . FERM and PDZ domain containing 2B, pseudogene . . . . . 0.02812 . . . . . FRMPD3 0.910767889845881 0.0892320633926677 4.67614515820078e-08 FERM and PDZ domain containing 3 . . . unclassifiable (Anatomical System);amygdala;thyroid;testis;germinal center;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.15593 . . . 207.91833 3.11367 FRMPD3-AS1 . . . FRMPD3 antisense RNA 1 . . . . . . . . . . . FRMPD4 0.997190828986364 0.00280916563693654 5.37669965256383e-09 FERM and PDZ domain containing 4 FUNCTION: Positive regulator of dendritic spine morphogenesis and density. Required for the maintenance of excitatory synaptic transmission. Binds phosphatidylinositol 4,5-bisphosphate. {ECO:0000269|PubMed:19118189}.; . . mammary gland; amygdala;subthalamic nucleus;occipital lobe;prefrontal cortex;globus pallidus;atrioventricular node;parietal lobe; 0.24477 0.09751 -1.837219906 2.070063694 64.79719 1.65323 FRMPD4-AS1 . . . FRMPD4 antisense RNA 1 . . . . . . . . . . . FRRS1 5.4989943969967e-08 0.850368316498901 0.149631628511155 ferric chelate reductase 1 FUNCTION: Ferric-chelate reductases reduce Fe(3+) to Fe(2+) before its transport from the endosome to the cytoplasm. {ECO:0000250}.; . . placenta;bladder; . 0.17562 0.12535 -0.110153916 45.48832272 1265.75071 6.70460 FRRS1L 0.00842827995041548 0.795607569748745 0.195964150300839 ferric chelate reductase 1 like . . TISSUE SPECIFICITY: Expressed in adult and fetal brain. Very weak expression in medulla, spinal cord and in adult ovary. {ECO:0000269|PubMed:10603000}.; . . 0.20283 0.12030 . . 48.36325 1.35594 FRS2 0.979070203401274 0.0209261643437508 3.63225497491172e-06 fibroblast growth factor receptor substrate 2 FUNCTION: Adapter protein that links activated FGR and NGF receptors to downstream signaling pathways. Plays an important role in the activation of MAP kinases and in the phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3- kinase, in response to ligand-mediated activation of FGFR1. Modulates signaling via SHC1 by competing for a common binding site on NTRK1. {ECO:0000269|PubMed:12974390, ECO:0000269|PubMed:21765395}.; . TISSUE SPECIFICITY: Highly expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:10092678}.; unclassifiable (Anatomical System);hypothalamus;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.93947 . -0.26993514 34.59542345 57.86658 1.53780 FRS3 0.808550861208179 0.191237234153598 0.000211904638223001 fibroblast growth factor receptor substrate 3 FUNCTION: Adapter protein that links FGF and NGF receptors to downstream signaling pathways. Involved in the activation of MAP kinases. Down-regulates ERK2 signaling by interfering with the phosphorylation and nuclear translocation of ERK2. {ECO:0000269|PubMed:15094036}.; . . unclassifiable (Anatomical System);lung;frontal lobe;bone;visual apparatus;testis;colon;blood;brain;stomach;bone marrow; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.95809 0.13806 0.290313621 71.56758669 526.0408 4.68111 FRY 0.999999999958023 4.19771806202542e-11 5.34490196356081e-35 FRY microtubule binding protein FUNCTION: Plays a crucial role in the structural integrity of mitotic centrosomes and in the maintenance of spindle bipolarity by promoting PLK1 activity at the spindle poles in early mitosis. May function as a scaffold promoting the interaction between AURKA and PLK1, thereby enhancing AURKA-mediated PLK1 phosphorylation. {ECO:0000269|PubMed:22753416}.; . . brain; superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.81429 . -2.659471462 0.748997405 2413.95265 9.12382 FRY-AS1 . . . FRY antisense RNA 1 . . . . . . . . . . . FRYL 0.999999992503124 7.49687622718013e-09 6.6878299295692e-31 FRY like transcription coactivator FUNCTION: Plays a key role in maintaining the integrity of polarized cell extensions during morphogenesis, regulates the actin cytoskeleton and plays a key role in patterning sensory neuron dendritic fields by promoting avoidance between homologous dendrites as well as by limiting dendritic branching (By similarity). May function as a transcriptional activator. {ECO:0000250, ECO:0000269|PubMed:16061630}.; . TISSUE SPECIFICITY: Widely expressed with higher expression in colon, placenta, brain and cells of lymphoid origin. {ECO:0000269|PubMed:16061630}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; amygdala;dorsal root ganglion;medulla oblongata;occipital lobe;thalamus;superior cervical ganglion;olfactory bulb;hypothalamus;spinal cord;caudate nucleus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.21972 . -2.418488491 1.049775891 551.87429 4.77944 FRZB 0.125665908311615 0.850778375983442 0.0235557157049429 frizzled-related protein FUNCTION: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP3/FRZB appears to be involved in limb skeletogenesis. Antagonist of Wnt8 signaling. Regulates chondrocyte maturation and long bone development.; DISEASE: Osteoarthritis 1 (OS1) [MIM:165720]: A degenerative disease of the joints characterized by degradation of the hyaline articular cartilage and remodeling of the subchondral bone with sclerosis. Clinical symptoms include pain and joint stiffness often leading to significant disability and joint replacement. {ECO:0000269|PubMed:15210948}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed primarily in the cartilaginous cores of the long bone during embryonic and fetal development and in the appendicular skeleton (6-13 weeks). At 13 weeks of gestation, transcripts were present in early chondroblasts of the tarsal bones of the foot, the carpal bones of the hands and the epiphysis of long bones. Highly expressed in placenta and heart, followed by brain, skeletal muscle, kidney and pancreas. Weakly expressed in lung and liver.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;whole body;frontal lobe;cochlea;bone;thyroid;iris;pituitary gland;testis;dura mater;spinal ganglion;ciliary body;brain;unclassifiable (Anatomical System);meninges;cartilage;heart;tongue;islets of Langerhans;hypothalamus;lens;bile duct;pancreas;pia mater;lung;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;trachea;placenta;ciliary ganglion;trigeminal ganglion; 0.24654 0.22445 0.440999548 77.79547063 1944.35537 8.11605 FSBP . . . fibrinogen silencer binding protein FUNCTION: Transcriptional repressor that down-regulates the expression of the fibrinogen gamma chain. Represses transcription of GSK3B gene promoter via its interaction with APBA1. {ECO:0000269|PubMed:20531236}.; . TISSUE SPECIFICITY: Expressed in multiple tissues including brain. {ECO:0000269|PubMed:20531236}.; . . . . . . 34.64327 1.05669 FSCB 4.81479388500392e-13 0.00372542340785937 0.996274576591659 fibrous sheath CABYR binding protein FUNCTION: May be involved in the later stages of fibrous sheath biogenesis. Binds calcium (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;testis;skeletal muscle; testis - interstitial;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; . 0.06726 1.982425511 97.62915782 1274.65222 6.72231 FSCN1 0.776273596220643 0.222127384528239 0.00159901925111739 fascin actin-bundling protein 1 FUNCTION: Organizes filamentous actin into bundles with a minimum of 4.1:1 actin/fascin ratio. Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration. {ECO:0000269|PubMed:20137952, ECO:0000269|PubMed:20393565, ECO:0000269|PubMed:9362073, ECO:0000269|PubMed:9571235}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;skin;uterus;prostate;whole body;frontal lobe;larynx;thyroid;testis;amniotic fluid;brain;unclassifiable (Anatomical System);amygdala;hypothalamus;muscle;bile duct;pancreas;lung;epididymis;placenta;visual apparatus;hippocampus;liver;duodenum;spleen;head and neck;cervix;kidney;stomach; amygdala;dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;kidney;pons;trigeminal ganglion; 0.21283 0.42167 -0.047654689 50.22410946 57.09514 1.52138 FSCN1P1 . . . fascin actin-bundling protein 1 pseudogene 1 . . . . . . . . . . . FSCN2 9.45740737766919e-09 0.0467309709478343 0.953269019594758 fascin actin-bundling protein 2, retinal FUNCTION: Acts as an actin bundling protein. May play a pivotal role in photoreceptor cell-specific events, such as disk morphogenesis.; . TISSUE SPECIFICITY: Localized specifically in the outer and inner segments of the photoreceptor cells in the retina.; optic nerve;ovary;macula lutea;fovea centralis;choroid;lens;retina; testis - interstitial;appendix;pons;trigeminal ganglion;skeletal muscle; 0.09186 0.14299 . . 204.25837 3.08691 FSCN3 7.76329851727915e-12 0.0692708452026741 0.930729154789563 fascin actin-bundling protein 3 FUNCTION: Acts as an actin bundling protein. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis.; unclassifiable (Anatomical System);medulla oblongata;hippocampus;testis;kidney; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.18021 . 0.490549924 79.54706299 1567.61429 7.32976 FSD1 0.732578210899087 0.267310093550352 0.000111695550561082 fibronectin type III and SPRY domain containing 1 FUNCTION: May be involved in microtubule organization and stabilization. {ECO:0000269|PubMed:12154070, ECO:0000269|PubMed:12445389}.; . TISSUE SPECIFICITY: Highly expressed in brain tissues, including cerebellum, cerebral cortex, medulla, occipital pole, frontal lobe, temporal lobe and putamen. Lower expression in spinal chord. {ECO:0000269|PubMed:11267680, ECO:0000269|PubMed:12154070}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;larynx;bone;brain;unclassifiable (Anatomical System);muscle;pharynx;blood;lens;lung;cornea;placenta;macula lutea;visual apparatus;liver;duodenum;head and neck;kidney;mammary gland;stomach; amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.57517 0.10873 -0.887242605 10.43288511 137.96052 2.55695 FSD1L . . . fibronectin type III and SPRY domain containing 1-like . . . . . 0.19237 0.10665 1.058333711 91.42486435 149.46024 2.66511 FSD2 2.36468713050695e-12 0.0663234129599549 0.933676587037681 fibronectin type III and SPRY domain containing 2 . . . ovary;parathyroid;choroid;fovea centralis;skin;retina;uterus;optic nerve;whole body;endometrium;testis;germinal center;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;blood;lens;skeletal muscle;lung;placenta;visual apparatus;macula lutea;liver;stomach;aorta; dorsal root ganglion;superior cervical ganglion;fetal liver;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06498 0.09268 -0.817464788 11.97806086 1591.87667 7.38048 FSHB 0.0128991685953233 0.657148411246663 0.329952420158014 follicle stimulating hormone beta subunit FUNCTION: Stimulates development of follicle and spermatogenesis in the reproductive organs.; DISEASE: Hypogonadotropic hypogonadism 24 without anosmia (HH24) [MIM:229070]: A form of hypogonadotropic hypogonadism, a group of disorders characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic-pituitary axis. HH24 is characterized by primary amenorrhea in women, oligo or azoospermia with low to normal testosterone levels in men, and infertility. {ECO:0000269|PubMed:8220432, ECO:0000269|PubMed:9271483, ECO:0000269|PubMed:9280841}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . frontal lobe;pituitary gland;testis; cerebellum peduncles;temporal lobe;pituitary; 0.36716 0.81783 0.03689118 56.64071715 19.89022 0.67725 FSHMD1A . . . facioscapulohumeral muscular dystrophy 1A . . . . . . . . . . . FSHMD1B . . . facioscapulohumeral muscular dystrophy 1B . . . . . . . . . . . FSHR 3.74938916692834e-10 0.0941241461110122 0.905875853514049 follicle stimulating hormone receptor FUNCTION: Receptor for follicle-stimulating hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Induces cAMP production through the activation of PI3K-AKT and SRC-ERK1/2 signaling pathways. {ECO:0000269|PubMed:24058690}.; DISEASE: Ovarian dysgenesis 1 (ODG1) [MIM:233300]: An autosomal recessive disease characterized by primary amenorrhea, variable development of secondary sex characteristics, poorly developed streak ovaries, and high serum levels of follicle-stimulating hormone (FSH) and luteinizing hormone (LH). {ECO:0000269|PubMed:10551778, ECO:0000269|PubMed:11889179, ECO:0000269|PubMed:12571157, ECO:0000269|PubMed:12915623, ECO:0000269|PubMed:7553856, ECO:0000269|PubMed:9769327, ECO:0000269|PubMed:9851774}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ovarian hyperstimulation syndrome (OHSS) [MIM:608115]: Disorder which occurs either spontaneously or most often as an iatrogenic complication of ovarian stimulation treatments for in vitro fertilization. The clinical manifestations vary from abdominal distention and discomfort to potentially life- threatening, massive ovarian enlargement and capillary leak with fluid sequestration. Pathologic features of this syndrome include the presence of multiple serous and hemorrhagic follicular cysts lined by luteinized cells, a condition called hyperreactio luteinalis. {ECO:0000269|PubMed:12930927, ECO:0000269|PubMed:12930928, ECO:0000269|PubMed:15080154, ECO:0000269|PubMed:16278261, ECO:0000269|PubMed:17721928, ECO:0000269|PubMed:24058690, ECO:0000269|PubMed:25581598}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Sertoli cells and ovarian granulosa cells.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08250 0.40004 -0.110153916 45.48832272 2768.0636 9.92690 FSIP1 4.51252744804813e-07 0.609400584034773 0.390598964712482 fibrous sheath interacting protein 1 . . . unclassifiable (Anatomical System);testis;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.09176 0.07645 1.556142814 95.65935362 3550.99356 11.51445 FSIP2 3.21632919900929e-08 0.999967049429988 3.29184067200601e-05 fibrous sheath interacting protein 2 . . . uterus;lung;heart;nasopharynx;testis;skin; . 0.05212 0.07622 . . 5663.99441 15.56525 FSIP2-AS1 . . . FSIP2 antisense RNA 1 . . . . . . . . . . . FST 0.963797331589925 0.0361332125488419 6.94558612332951e-05 follistatin FUNCTION: Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH).; . TISSUE SPECIFICITY: Isoform 1 is the predominant isoform in serum but is undetectable in follicular fluid. {ECO:0000269|PubMed:15472207}.; unclassifiable (Anatomical System);cartilage;heart;ovary;hypothalamus;skin;uterus;pancreas;prostate;whole body;lung;cochlea;larynx;bone;thyroid;visual apparatus;liver;testis;head and neck;spleen;kidney;brain;mammary gland; superior cervical ganglion;fetal liver;lung;smooth muscle;heart;atrioventricular node;skeletal muscle; 0.88912 0.48610 0.591694063 82.45458835 44.28611 1.27001 FSTL1 0.959341928524645 0.0406392344790319 1.88369963229796e-05 follistatin like 1 FUNCTION: May modulate the action of some growth factors on cell proliferation and differentiation. Binds heparin (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Overexpressed in synovial tissues from rheumatoid arthritis. {ECO:0000269|PubMed:15638044}.; myocardium;smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;cochlea;endometrium;bone;thyroid;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;hypopharynx;alveolus;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;adipose tissue;smooth muscle;placenta;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;fetal thyroid; 0.52355 0.17050 -0.315847836 31.68789809 41.84684 1.21885 FSTL3 0.418831972518919 0.546425894652553 0.0347421328285287 follistatin like 3 FUNCTION: Isoform 1 or the secreted form is a binding and antagonizing protein for members of the TGF-beta family, such us activin, BMP2 and MSTN. Inhibits activin A-, activin B-, BMP2- and MSDT-induced cellular signaling; more effective on activin A than on activin B. Involved in bone formation; inhibits osteoclast differentiationc. Involved in hematopoiesis; involved in differentiation of hemopoietic progenitor cells, increases hematopoietic cell adhesion to fibronectin and seems to contribute to the adhesion of hematopoietic precursor cells to the bone marrow stroma. Isoform 2 or the nuclear form is probably involved in transcriptional regulation via interaction with MLLT10. {ECO:0000269|PubMed:11948405, ECO:0000269|PubMed:15451575, ECO:0000269|PubMed:15574124, ECO:0000269|PubMed:16336961, ECO:0000269|PubMed:17868029, ECO:0000269|PubMed:17878677}.; . TISSUE SPECIFICITY: Expressed in a wide range of tissues. {ECO:0000269|PubMed:11459787}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;adrenal gland;placenta;adrenal cortex;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.18233 0.14781 . . 14.98402 0.53881 FSTL4 0.981626121203096 0.0183738743779593 4.41894462086476e-09 follistatin like 4 . . . unclassifiable (Anatomical System);islets of Langerhans;urinary;fovea centralis;choroid;lens;retina;breast;pancreas;optic nerve;lung;placenta;macula lutea;testis;kidney;brain;stomach; superior cervical ganglion;medulla oblongata;temporal lobe;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.09890 0.10056 -0.479490344 22.81788158 416.3819 4.27051 FSTL5 0.0025626068189185 0.997308520980881 0.000128872200200942 follistatin like 5 . . . unclassifiable (Anatomical System);hypothalamus;fovea centralis;choroid;lens;skeletal muscle;skin;retina;optic nerve;lung;cochlea;macula lutea;pituitary gland;cervix;mammary gland;brain; subthalamic nucleus;ciliary ganglion;atrioventricular node; 0.18465 0.09747 0.536463361 81.06864827 1669.41879 7.54135 FTCD 4.30129998812761e-08 0.359852363009066 0.640147593977935 formimidoyltransferase cyclodeaminase FUNCTION: Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool.; DISEASE: Glutamate formiminotransferase deficiency (FIGLU-URIA) [MIM:229100]: Autosomal recessive disorder. Features of a severe phenotype, include elevated levels of formiminoglutamate (FIGLU) in the urine in response to histidine administration, megaloblastic anemia, and mental retardation. Features of a mild phenotype include high urinary excretion of FIGLU in the absence of histidine administration, mild developmental delay, and no hematological abnormalities. {ECO:0000269|PubMed:12815595}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;optic nerve;lung;islets of Langerhans;placenta;liver;testis;spleen;kidney; fetal liver;superior cervical ganglion;testis - seminiferous tubule;liver;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13129 . -0.749505784 13.74144845 813.27557 5.60784 FTCD-AS1 . . . FTCD antisense RNA 1 . . . . . . . . . . . FTCDNL1 . . . formiminotransferase cyclodeaminase N-terminal like . . TISSUE SPECIFICITY: Widely expressed with highest levels in liver and skeletal muscle, and moderate levels in kidney, bone and pancreas. {ECO:0000269|PubMed:21573128}.; . . . . . . 70.89144 1.75348 FTH1 0.918437494529701 0.081030257799496 0.000532247670802989 ferritin, heavy polypeptide 1 FUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the liver. {ECO:0000269|PubMed:11389486}.; myocardium;ovary;colon;substantia nigra;choroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;synovium;larynx;bone;thyroid;iris;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;small intestine;islets of Langerhans;arterial adventitia;pineal body;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;epididymis;trabecular meshwork;placenta;visual apparatus;hippocampus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; olfactory bulb;spinal cord; . 0.48545 0.103030231 61.2762444 8.70049 0.31993 FTH1P1 . . . ferritin, heavy polypeptide 1 pseudogene . . . . . . . . . . . FTH1P2 . . . ferritin, heavy polypeptide 1 pseudogene 2 . . . . . . . . . . . FTH1P3 . . . ferritin, heavy polypeptide 1 pseudogene 3 . . . . . . . . . . . FTH1P4 . . . ferritin, heavy polypeptide 1 pseudogene 4 . . . . . . . . . . . FTH1P5 . . . ferritin, heavy polypeptide 1 pseudogene 5 . . . . . . . . . . . FTH1P6 . . . ferritin, heavy polypeptide 1 pseudogene 6 . . . . . . . . . . . FTH1P7 . . . ferritin, heavy polypeptide 1 pseudogene 7 . . . . . . . . . . . FTH1P8 . . . ferritin, heavy polypeptide 1 pseudogene 8 . . . . . . . . . . . FTH1P9 . . . ferritin, heavy polypeptide 1 pseudogene 9 . . . . . . . . . . . FTH1P10 . . . ferritin, heavy polypeptide 1 pseudogene 10 . . . . . . . . . . . FTH1P11 . . . ferritin, heavy polypeptide 1 pseudogene 11 . . . . . . . . . . . FTH1P12 . . . ferritin, heavy polypeptide 1 pseudogene 12 . . . . . . . . . . . FTH1P13 . . . ferritin, heavy polypeptide 1 pseudogene 13 . . . . . . . . . . . FTH1P14 . . . ferritin, heavy polypeptide 1 pseudogene 14 . . . . . . . . . . . FTH1P15 . . . ferritin, heavy polypeptide 1 pseudogene 15 . . . . . . . . . . . FTH1P16 . . . ferritin, heavy polypeptide 1 pseudogene 16 . . . . . . . . . . . FTH1P18 . . . ferritin, heavy polypeptide 1 pseudogene 18 . . . . . . . . . . . FTH1P19 . . . ferritin, heavy polypeptide 1 pseudogene 19 . . . . . . . . . . . FTH1P20 . . . ferritin, heavy polypeptide 1 pseudogene 20 . . . . . . . . . . . FTH1P21 . . . ferritin, heavy polypeptide 1 pseudogene 21 . . . . . . . . . . . FTH1P22 . . . ferritin, heavy polypeptide 1 pseudogene 22 . . . . . . . . . . . FTH1P23 . . . ferritin, heavy polypeptide 1 pseudogene 23 . . . . . . . . . . . FTH1P24 . . . ferritin, heavy polypeptide 1 pseudogene 24 . . . . . . . . . . . FTH1P25 . . . ferritin, heavy polypeptide 1 pseudogene 25 . . . . . . . . . . . FTH1P26 . . . ferritin, heavy polypeptide 1 pseudogene 26 . . . . . . . . . . . FTH1P27 . . . ferritin, heavy polypeptide 1 pseudogene 27 . . . . . . . . . . . FTHL17 0.000467382833595725 0.250781009649819 0.748751607516585 ferritin, heavy polypeptide-like 17 . . TISSUE SPECIFICITY: Testis specific. Also expressed in several cancers. {ECO:0000269|PubMed:12704671}.; . . 0.05515 0.10585 1.23654218 93.29440906 1050.37389 6.22380 FTL 0.000458652707063046 0.427809813333335 0.571731533959602 ferritin, light polypeptide FUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity). {ECO:0000250, ECO:0000269|PubMed:19923220, ECO:0000269|PubMed:20159981}.; DISEASE: Hereditary hyperferritinemia-cataract syndrome (HHCS) [MIM:600886]: An autosomal dominant disease characterized by elevated level of ferritin in serum and tissues, and early-onset bilateral cataract. {ECO:0000269|PubMed:19176363}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Neurodegeneration with brain iron accumulation 3 (NBIA3) [MIM:606159]: A neurodegenerative disorder associated with iron accumulation in the brain, primarily in the basal ganglia. It is characterized by a variety of neurological signs including parkinsonism, ataxia, corticospinal signs, mild non-progressive cognitive deficit and episodic psychosis. It is linked with decreased serum ferritin levels. {ECO:0000269|PubMed:16116125}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: L-ferritin deficiency (LFTD) [MIM:615604]: A condition characterized by low levels of ferritin in serum and tissues in the absence of other hematological symptoms. Seizures and mild neuropsychologic impairment may manifest in individuals with complete ferritin deficiency. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.08288 0.64843 -0.163345027 41.24793583 10.88019 0.39394 FTLP1 . . . ferritin, light polypeptide pseudogene 1 . . . . . . . . . . . FTLP2 . . . ferritin, light polypeptide pseudogene 2 . . . . . . . . . . . FTLP3 . . . ferritin, light polypeptide pseudogene 3 . . . . . . . . . . . FTLP4 . . . ferritin, light polypeptide pseudogene 4 . . . . . . . . . . . FTLP5 . . . ferritin, light polypeptide pseudogene 5 . . . . . . . . . . . FTLP6 . . . ferritin, light polypeptide pseudogene 6 . . . . . . . . . . . FTLP7 . . . ferritin, light polypeptide pseudogene 7 . . . . . . . . . . . FTLP8 . . . ferritin, light polypeptide pseudogene 8 . . . . . . . . . . . FTLP9 . . . ferritin, light polypeptide pseudogene 9 . . . . . . . . . . . FTLP10 . . . ferritin, light polypeptide pseudogene 10 . . . . . . . . . . . FTLP11 . . . ferritin, light polypeptide pseudogene 11 . . . . . . . . . . . FTLP12 . . . ferritin, light polypeptide pseudogene 12 . . . . . . . . . . . FTLP13 . . . ferritin, light polypeptide pseudogene 13 . . . . . . . . . . . FTLP14 . . . ferritin, light polypeptide pseudogene 14 . . . . . . . . . . . FTLP15 . . . ferritin, light polypeptide pseudogene 15 . . . . . . . . . . . FTLP16 . . . ferritin, light polypeptide pseudogene 16 . . . . . . . . . . . FTLP17 . . . ferritin, light polypeptide pseudogene 17 . . . . . . . . . . . FTLP18 . . . ferritin, light polypeptide pseudogene 18 . . . . . . . . . . . FTLP19 . . . ferritin, light polypeptide pseudogene 19 . . . . . . . . . . . FTMT 0.0816239867421276 0.75609522519524 0.162280788062632 ferritin mitochondrial FUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. {ECO:0000269|PubMed:11323407, ECO:0000269|PubMed:15201052}.; . TISSUE SPECIFICITY: Detected in testis and erythroleukemia. Expression is very low or not detectable in brain, colon, heart, kidney, liver, lung, muscle, placental, spleen and small intestine. {ECO:0000269|PubMed:11323407}.; testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06302 0.20458 0.371224249 75.12384996 105.36958 2.22323 FTO 0.0113445756239307 0.986864609239865 0.00179081513620422 fat mass and obesity associated FUNCTION: Dioxygenase that repairs alkylated DNA and RNA by oxidative demethylation. Has highest activity towards single- stranded RNA containing 3-methyluracil, followed by single- stranded DNA containing 3-methylthymine. Has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3-methylcytosine (PubMed:18775698, PubMed:20376003). Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (PubMed:22002720, PubMed:26458103). Has no activity towards 1- methylguanine. Has no detectable activity towards double-stranded DNA. Requires molecular oxygen, alpha-ketoglutarate and iron. Contributes to the regulation of the global metabolic rate, energy expenditure and energy homeostasis. Contributes to the regulation of body size and body fat accumulation (PubMed:18775698, PubMed:20376003). In particular, it is involved in the regulation of thermogenesis and the control of adipocyte differentiation into brown or white fat cells (PubMed:26287746). {ECO:0000269|PubMed:18775698, ECO:0000269|PubMed:20376003, ECO:0000269|PubMed:22002720, ECO:0000269|PubMed:26287746, ECO:0000269|PubMed:26458103}.; DISEASE: Growth retardation, developmental delay, and facial dysmorphism (GDFD) [MIM:612938]: A severe polymalformation syndrome characterized by postnatal growth retardation, microcephaly, severe psychomotor delay, functional brain deficits and characteristic facial dysmorphism. In some patients, structural brain malformations, cardiac defects, genital anomalies, and cleft palate are observed. Early death occurs by the age of 3 years. {ECO:0000269|PubMed:19559399}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Obesity (OBESITY) [MIM:601665]: A condition characterized by an increase of body weight beyond the limitation of skeletal and physical requirements, as the result of excessive accumulation of body fat. {ECO:0000269|PubMed:26287746}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. A pathogenic intronic FTO variation (rs1421085) disrupts an evolutionarily conserved motif for ARID5B binding. Loss of ARID5B binding results in overexpression of two genes distal to FTO, IRX3 and IRX5. IRX3 and IRX5 overexpression shifts pre-adipocytes differentiation from brown to white fat cells, resulting in increased lipid storage and loss of mitochondrial thermogenesis. {ECO:0000269|PubMed:26287746}.; TISSUE SPECIFICITY: Ubiquitously expressed, with relatively high expression in adrenal glands and brain; especially in hypothalamus and pituitary. {ECO:0000269|PubMed:17434869, ECO:0000269|PubMed:17496892}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;frontal lobe;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach; amygdala;dorsal root ganglion;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;subthalamic nucleus;adrenal gland;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.42596 0.28005 -0.288341872 33.41589998 98.07425 2.14102 FTO-IT1 . . . FTO intronic transcript 1 . . . . . . . . . . . FTOP1 . . . fat mass and obesity associated pseudogene 1 . . . . . . . . . . . FTSJ1 0.96163278031456 0.0382869856064354 8.02340790046344e-05 FtsJ RNA methyltransferase homolog 1 (E. coli) FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs. {ECO:0000255|HAMAP-Rule:MF_03162}.; . TISSUE SPECIFICITY: Found in fetal brain, lung, liver and kidney. In the adult brain, expressed in amygdala, caudate nucleus, corpus callosum, hippocampus and thalamus. {ECO:0000269|PubMed:15162322}.; ovary;salivary gland;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.06441 0.17687 -0.005381972 53.50908233 42.30218 1.23122 FTSJ2 1.97487905738454e-05 0.274364019447349 0.725616231762077 FtsJ RNA methyltransferase homolog 2 (E. coli) FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O- methyluridine at position 1369 (Um1369) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA. {ECO:0000269|PubMed:25009282, ECO:0000269|PubMed:25074936}.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in muscle, placenta, and heart. {ECO:0000269|PubMed:11827451}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;muscle;pharynx;blood;skeletal muscle;bile duct;lung;cornea;nasopharynx;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.15151 0.14343 -0.22584292 37.32012267 64.20932 1.64382 FTSJ3 0.484157751981298 0.515842179109866 6.89088358442307e-08 FtsJ homolog 3 (E. coli) FUNCTION: Probable methyltransferase involved in the processing of the 34S pre-rRNA to 18S rRNA and in 40S ribosomal subunit formation. {ECO:0000255|HAMAP-Rule:MF_03163, ECO:0000269|PubMed:22195017}.; . . . . 0.12533 0.10053 0.07167258 59.15899976 570.78462 4.84670 FTX . . . FTX transcript, XIST regulator (non-protein coding) . . . . . . . . . . . FUBP1 0.999972830983476 2.71690149033464e-05 1.62035516806659e-12 far upstream element binding protein 1 FUNCTION: Regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. May act both as activator and repressor of transcription. {ECO:0000269|PubMed:8125259}.; . . skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;skeletal muscle;breast;lung;epididymis;nasopharynx;placenta;visual apparatus;kidney;mammary gland;stomach;peripheral nerve;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;lymph node;testis - seminiferous tubule;fetal brain;globus pallidus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.60917 0.16996 -0.291981272 33.20358575 48.41037 1.35624 FUBP3 0.86267942485269 0.13731986124344 7.139038704667e-07 far upstream element (FUSE) binding protein 3 FUNCTION: May interact with single-stranded DNA from the far- upstream element (FUSE). May activate gene expression.; . TISSUE SPECIFICITY: Detected in a number of cell lines.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;endometrium;larynx;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);heart;lacrimal gland;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;alveolus;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; . 0.33681 0.10802 -0.512444034 21.55579146 37.67364 1.12204 FUCA1 3.3905830953051e-08 0.320516512565617 0.679483453528552 fucosidase, alpha-L- 1, tissue FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N- acetylglucosamine of the carbohydrate moieties of glycoproteins.; DISEASE: Fucosidosis (FUCA1D) [MIM:230000]: An autosomal recessive lysosomal storage disease characterized by accumulation of fucose- containing glycolipids and glycoproteins in various tissues. Clinical signs include facial dysmorphism, dysostosis multiplex, moderate hepatomegaly, severe intellectual deficit, deafness, and according to age, angiokeratomas. {ECO:0000269|PubMed:7874128, ECO:0000269|PubMed:8504303, ECO:0000269|PubMed:9762612}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.08865 0.29252 0.663285274 84.55414013 2719.65674 9.82333 FUCA1P1 . . . fucosidase, alpha-L- 1, tissue pseudogene 1 . . . . . . . . . . . FUCA2 0.000365583505701958 0.953432936370397 0.046201480123901 fucosidase, alpha-L- 2, plasma FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N- acetylglucosamine of the carbohydrate moieties of glycoproteins.; . . myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;oesophagus;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; . 0.17282 0.41419 0.597144447 82.7435716 4017.78712 12.55895 FUK 8.47562895767482e-16 0.114843567459153 0.885156432540846 fucokinase FUNCTION: Takes part in the salvage pathway for reutilization of fucose from the degradation of oligosaccharides.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;adrenal cortex;pancreas;lung;epididymis;placenta;macula lutea;liver;duodenum;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19333 0.13669 -0.916836882 9.831328143 572.35277 4.85756 FUNDC1 0.440692340205304 0.529408335786876 0.0298993240078206 FUN14 domain containing 1 FUNCTION: Acts as an activator of hypoxia-induced mitophagy, an important mechanism for mitochondrial quality control. {ECO:0000269|PubMed:22267086}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:22267086}.; . . 0.18670 0.09080 0.013025609 54.62962963 13.30923 0.48336 FUNDC2 0.841264939337729 0.15576878095872 0.00296627970355182 FUN14 domain containing 2 . . . . . 0.03109 0.06604 -0.031067188 51.03798066 6.64559 0.24552 FUNDC2P1 . . . FUN14 domain containing 2 pseudogene 1 . . . . . . . . . . . FUNDC2P2 . . . FUN14 domain containing 2 pseudogene 2 . . . medulla oblongata;lung;small intestine;testis; . . . . . . . FUNDC2P3 . . . FUN14 domain containing 2 pseudogene 3 . . . breast;uterus;islets of Langerhans;larynx;nasopharynx;bone;liver;spleen;head and neck;germinal center; . . . . . . . FUNDC2P4 . . . FUN14 domain containing 2 pseudogene 4 . . . . . . . . . . . FUOM 0.00160107219629907 0.454482829499067 0.543916098304634 fucose mutarotase FUNCTION: Involved in the interconversion between alpha- and beta- L-fucoses. L-Fucose (6-deoxy-L-galactose) exists as alpha-L-fucose (29.5%) and beta-L-fucose (70.5%), the beta-form is metabolized through the salvage pathway. GDP-L-fucose formed either by the de novo or salvage pathways is transported into the endoplasmic reticulum, where it serves as a substrate for N- and O- glycosylations by fucosyltransferases. Fucosylated structures expressed on cell surfaces or secreted in biological fluids are believed to play a critical role in cell-cell adhesion and recognition processes. {ECO:0000269|PubMed:17602138}.; . . . . 0.07483 0.09585 0.391453969 75.87284737 22.28332 0.74736 FURIN 0.999933300929352 6.66990562032405e-05 1.44450711215262e-11 furin, paired basic amino acid cleaving enzyme FUNCTION: Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif. {ECO:0000269|PubMed:7690548}.; . TISSUE SPECIFICITY: Seems to be expressed ubiquitously.; smooth muscle;ovary;salivary gland;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;blood;breast;pancreas;lung;epididymis;placenta;alveolus;duodenum;liver;cervix;spleen;head and neck;kidney;aorta;stomach;cerebellum;thymus; superior cervical ganglion;placenta;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.56554 0.76978 -0.793601146 12.57372022 202.72489 3.07338 FUS 0.999963786341319 3.62136554179506e-05 3.26289863888912e-12 FUS RNA binding protein FUNCTION: Binds both single-stranded and double-stranded DNA and promotes ATP-independent annealing of complementary single- stranded DNAs and D-loop formation in superhelical double-stranded DNA. May play a role in maintenance of genomic integrity.; DISEASE: Note=A chromosomal aberration involving FUS is found in a patient with malignant myxoid liposarcoma. Translocation t(12;16)(q13;p11) with DDIT3. {ECO:0000269|PubMed:7503811}.; DISEASE: Note=A chromosomal aberration involving FUS is a cause of acute myeloid leukemia (AML). Translocation t(16;21)(p11;q22) with ERG. {ECO:0000269|PubMed:8187069}.; DISEASE: Angiomatoid fibrous histiocytoma (AFH) [MIM:612160]: A distinct variant of malignant fibrous histiocytoma that typically occurs in children and adolescents and is manifest by nodular subcutaneous growth. Characteristic microscopic features include lobulated sheets of histiocyte-like cells intimately associated with areas of hemorrhage and cystic pseudovascular spaces, as well as a striking cuffing of inflammatory cells, mimicking a lymph node metastasis. {ECO:0000269|PubMed:11063792}. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving FUS is found in a patient with angiomatoid fibrous histiocytoma. Translocation t(12;16)(q13;p11.2) with ATF1 generates a chimeric FUS/ATF1 protein. {ECO:0000269|PubMed:11063792}.; DISEASE: Amyotrophic lateral sclerosis 6, with or without frontotemporal dementia (ALS6) [MIM:608030]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. {ECO:0000269|PubMed:19251627, ECO:0000269|PubMed:19251628, ECO:0000269|PubMed:19861302, ECO:0000269|PubMed:20124201}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Tremor, hereditary essential 4 (ETM4) [MIM:614782]: A common movement disorder mainly characterized by postural tremor of the arms. Head, legs, trunk, voice, jaw, and facial muscles also may be involved. The condition can be aggravated by emotions, hunger, fatigue and temperature extremes, and may cause a functional disability or even incapacitation. Inheritance is autosomal dominant. {ECO:0000269|PubMed:22863194}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;globus pallidus;testis;pons;trigeminal ganglion;cerebellum; 0.42621 0.49093 -1.001120478 8.321538099 78.86065 1.87589 FUSE . . . polykaryocytosis promoter . . . . . . . . . . . FUT1 0.000508774873537715 0.448074831421771 0.551416393704691 fucosyltransferase 1 (H blood group) FUNCTION: Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble A and B antigen synthesis pathway. H and Se enzymes fucosylate the same acceptor substrates but exhibit different Km values.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;skin;skeletal muscle;uterus;lung;frontal lobe;bone;placenta;liver;testis;spleen;cervix;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10946 0.26216 -0.161524709 41.6430762 690.0301 5.23872 FUT2 5.46581459214613e-12 0.0042001724083725 0.995799827586162 fucosyltransferase 2 FUNCTION: Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble A and B antigen synthesis pathway. H and Se enzymes fucosylate the same acceptor substrates but exhibit different Km values.; . TISSUE SPECIFICITY: Small intestine, colon and lung.; . . 0.05184 . 0.823072022 88.03963199 10077.22821 21.87521 FUT3 0.373828733490639 0.615127561949185 0.0110437045601754 fucosyltransferase 3 (Lewis blood group) FUNCTION: May catalyze alpha-1,3 and alpha-1,4 glycosidic linkages involved in the expression of Vim-2, Lewis A, Lewis B, sialyl Lewis X and Lewis X/SSEA-1 antigens. May be involved in blood group Lewis determination; Lewis-positive (Le(+)) individuals have an active enzyme while Lewis-negative (Le(-)) individuals have an inactive enzyme. Also acts on the corresponding 1,4-galactosyl derivative, forming 1,3-L-fucosyl links.; . TISSUE SPECIFICITY: Highly expressed in stomach, colon, small intestine, lung and kidney and to a lesser extent in salivary gland, bladder, uterus and liver.; islets of Langerhans;urinary;colon;skeletal muscle;retina;breast;pancreas;optic nerve;lung;endometrium;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skeletal muscle; 0.13415 0.18780 2.601812899 98.76739797 3247.52981 10.85579 FUT4 0.055379992152633 0.925637263358273 0.0189827444890943 fucosyltransferase 4 FUNCTION: May catalyze alpha-1,3 glycosidic linkages involved in the expression of Lewis X/SSEA-1 and VIM-2 antigens.; . . ovary;colon;fovea centralis;choroid;retina;bone marrow;uterus;optic nerve;whole body;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;urinary;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;medulla oblongata;appendix; 0.05714 0.35785 . . 502.31886 4.59839 FUT5 0.00235788381432205 0.76977721823782 0.227864897947858 fucosyltransferase 5 FUNCTION: May catalyze alpha-1,3 glycosidic linkages involved in the expression of VIM-2, Lewis X/SSEA-1 and sialyl Lewis X antigens.; . TISSUE SPECIFICITY: Liver, colon and testis and trace amounts in T-cells and brain.; colon;stomach; superior cervical ganglion;subthalamic nucleus;heart;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10256 0.12025 0.112125503 62.09601321 4259.93143 12.97007 FUT6 0.0221299532408796 0.909913769648779 0.0679562771103408 fucosyltransferase 6 FUNCTION: Enzyme involved in the biosynthesis of the E-Selectin ligand, sialyl-Lewis X. Catalyzes the transfer of fucose from GDP- beta-fucose to alpha-2,3 sialylated substrates.; . TISSUE SPECIFICITY: Kidney, liver, colon, small intestine, bladder, uterus and salivary gland.; unclassifiable (Anatomical System);cartilage;ovary;colon;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;pancreas;prostate;optic nerve;lung;endometrium;placenta;macula lutea;hypopharynx;cervix;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;thalamus;salivary gland;pons;atrioventricular node;caudate nucleus;skeletal muscle;uterus corpus;trachea;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion;parietal lobe;cingulate cortex; 0.09020 0.12285 0.178263593 66.12998349 2059.85399 8.36480 FUT7 0.905391611564477 0.0944487168361814 0.000159671599341858 fucosyltransferase 7 (alpha (1,3) fucosyltransferase) FUNCTION: May catalyze alpha-1,3 glycosidic linkages involved in the expression of sialyl Lewis X antigens.; . TISSUE SPECIFICITY: Leukocytic/myeloid lineage cells.; unclassifiable (Anatomical System);lung;testis;germinal center;stomach; ciliary ganglion;whole blood;skeletal muscle; 0.08408 . 0.576916344 82.25406936 180.33556 2.91759 FUT8 0.997566109877212 0.00243388633326219 3.78952605680299e-09 fucosyltransferase 8 (alpha (1,6) fucosyltransferase) FUNCTION: Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans. {ECO:0000269|PubMed:17172260, ECO:0000269|PubMed:9133635}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; medulla oblongata;occipital lobe;olfactory bulb;hypothalamus;placenta;spinal cord;prefrontal cortex; 0.11849 0.20101 -0.468351206 23.42533616 1542.85964 7.28794 FUT8-AS1 . . . FUT8 antisense RNA 1 . . . . . . . . . . . FUT9 0.0813711620521245 0.871951197019538 0.0466776409283379 fucosyltransferase 9 (alpha (1,3) fucosyltransferase) FUNCTION: Transfers a fucose to lacto-N-neotetraose but not to either alpha2,3-sialyl lacto-N-neotetraose or lacto-N-tetraose. Can catalyze the last step in the biosynthesis of Lewis antigen, the addition of a fucose to precursor polysaccharides. {ECO:0000269|PubMed:10386598}.; . TISSUE SPECIFICITY: Strongly expressed in forebrain and stomach, lower expression in spleen and peripheral blood leukocytes, and no expression in small intestine, colon, liver, lung, kidney, adrenal cortex or uterus. {ECO:0000269|PubMed:10386598}.; unclassifiable (Anatomical System);islets of Langerhans; dorsal root ganglion;superior cervical ganglion;temporal lobe;trigeminal ganglion;skin;skeletal muscle; 0.63762 0.12971 0.12689526 63.00424628 12.10453 0.43867 FUT10 3.07918840008664e-07 0.526483135559184 0.473516556521976 fucosyltransferase 10 (alpha (1,3) fucosyltransferase) FUNCTION: Probable fucosyltransferase. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;tongue;colon;fovea centralis;choroid;lens;skin;skeletal muscle;retina;breast;uterus;optic nerve;lung;epididymis;placenta;macula lutea;liver;head and neck;spleen;cervix;kidney;brain;peripheral nerve; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.06224 0.09649 0.446457185 77.97829677 3746.81614 11.97903 FUT11 1.25546506236405e-05 0.379581674558346 0.620405770791031 fucosyltransferase 11 (alpha (1,3) fucosyltransferase) FUNCTION: Probable fucosyltransferase. {ECO:0000250}.; . . . . 0.13856 0.11338 0.086440867 60.47416844 114.46877 2.33088 FUZ 0.00208816398655203 0.914415470795178 0.0834963652182702 fuzzy planar cell polarity protein FUNCTION: Probable planar cell polarity effector involved in cilium biogenesis. May regulate protein and membrane transport to the cilium. May regulate the morphogenesis of hair follicles which depends on functional primary cilia (By similarity). {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.36339 0.24864 0.018483465 55.44939844 625.91831 5.04573 FXN 0.81775377252312 0.177972052602335 0.00427417487454558 frataxin FUNCTION: Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. Modulates the RNA-binding activity of ACO1. {ECO:0000269|PubMed:12785837, ECO:0000269|PubMed:15247478, ECO:0000269|PubMed:15641778, ECO:0000269|PubMed:16239244, ECO:0000269|PubMed:16608849, ECO:0000269|PubMed:20053667}.; DISEASE: Friedreich ataxia (FRDA) [MIM:229300]: Autosomal recessive, progressive degenerative disease characterized by neurodegeneration and cardiomyopathy it is the most common inherited ataxia. The disorder is usually manifest before adolescence and is generally characterized by incoordination of limb movements, dysarthria, nystagmus, diminished or absent tendon reflexes, Babinski sign, impairment of position and vibratory senses, scoliosis, pes cavus, and hammer toe. In most patients, FRDA is due to GAA triplet repeat expansions in the first intron of the frataxin gene. But in some cases the disease is due to mutations in the coding region. {ECO:0000269|PubMed:10732799, ECO:0000269|PubMed:10874325, ECO:0000269|PubMed:9150176, ECO:0000269|PubMed:9779809, ECO:0000269|PubMed:9989622, ECO:0000269|Ref.35, ECO:0000269|Ref.7, ECO:0000269|Ref.8}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the heart, peripheral blood lymphocytes and dermal fibroblasts. {ECO:0000269|PubMed:17468497}.; . . 0.33107 0.39012 0.413500896 76.67492333 28.22067 0.90447 FXNP1 . . . frataxin pseudogene 1 . . . . . . . . . . . FXNP2 . . . frataxin pseuodgene 2 . . . . . . . . . . . FXR1 0.999992197639482 7.80236044010123e-06 7.7579936909787e-14 FMR1 autosomal homolog 1 FUNCTION: RNA-binding protein required for embryonic and postnatal development of muscle tissue. May regulate intracellular transport and local translation of certain mRNAs (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in all tissues examined including heart, brain, kidney and testis. {ECO:0000269|PubMed:7781595}.; lymphoreticular;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;uterus;atrium;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;cerebellum; testis - interstitial;superior cervical ganglion;olfactory bulb;testis - seminiferous tubule;temporal lobe;prefrontal cortex;testis;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.83345 0.19444 -0.648365105 16.35999056 32.43007 1.01245 FXR2 0.999770109253338 0.000229890734610926 1.20509936764329e-11 FMR1 autosomal homolog 2 FUNCTION: RNA-binding protein.; . . myocardium;ovary;salivary gland;colon;choroid;skin;bone marrow;uterus;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;lung;mesenchyma;placenta;visual apparatus;hippocampus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach; whole brain;subthalamic nucleus;medulla oblongata;cerebellum peduncles;temporal lobe;prefrontal cortex;globus pallidus;cingulate cortex;skeletal muscle;parietal lobe;cerebellum; 0.41144 0.14925 -0.534490515 20.70063694 43.34685 1.25161 FXYD1 0.233039911970241 0.73353721439025 0.0334228736395092 FXYD domain containing ion transport regulator 1 FUNCTION: May have a functional role in muscle contraction. Induces a hyperpolarization-activated chloride current when exogenously expressed.; . TISSUE SPECIFICITY: Highest expression in skeletal muscle and heart. Moderate levels in brain, placenta, lung, liver, pancreas, uterus, bladder, prostate, small intestine and colon with mucosal lining. Very low levels in kidney, colon and small intestine without mucosa, prostate without endothelial lining, spleen, and testis.; myocardium;ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;testis;brain;unclassifiable (Anatomical System);heart;pineal body;muscle;skeletal muscle;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;olfactory bulb;liver;skeletal muscle; . . 0.523736627 80.45529606 . . FXYD2 0.698943754498667 0.284297318653487 0.016758926847846 FXYD domain containing ion transport regulator 2 FUNCTION: May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase.; . TISSUE SPECIFICITY: Expressed in the distal convoluted tubule in the kidney. Found on basolateral membranes of nephron epithelial cells.; unclassifiable (Anatomical System);heart;islets of Langerhans;colon;blood;skeletal muscle;pancreas;whole body;lung;liver;testis;spleen;kidney;stomach; fetal liver;beta cell islets;kidney; 0.19855 . 0.193034296 66.82000472 22.06592 0.74077 FXYD3 0.00343233596536991 0.834690567782353 0.161877096252277 FXYD domain containing ion transport regulator 3 FUNCTION: Induces a hyperpolarization-activated chloride current when expressed in Xenopus oocytes. May be a modulator capable of activating endogenous oocyte channels.; . TISSUE SPECIFICITY: Expressed in a subset of human breast tumors.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;oral cavity;urinary;pharynx;blood;lens;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;olfactory bulb;tongue;salivary gland;beta cell islets;atrioventricular node;pons;skin;skeletal muscle;prostate;pancreas;lung;trachea;placenta;fetal lung;ciliary ganglion;kidney;trigeminal ganglion;parietal lobe;tonsil;cerebellum; 0.12271 0.09495 0.72761005 86.08162302 238.10522 3.33286 FXYD4 0.0524503210084792 0.862223003004584 0.0853266759869371 FXYD domain containing ion transport regulator 4 . . . . . 0.10957 . 0.347360312 73.97381458 254.12131 3.42863 FXYD5 0.464175278334183 0.530189139111228 0.00563558255458893 FXYD domain containing ion transport regulator 5 FUNCTION: Involved in down-regulation of E-cadherin which results in reduced cell adhesion. Promotes metastasis. {ECO:0000269|PubMed:11756660}.; . . smooth muscle;ovary;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;breast;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;alveolus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;heart;placenta;ciliary ganglion;white blood cells;trigeminal ganglion;whole blood;bone marrow; 0.06179 0.11841 0.661468037 84.4420854 703.46761 5.27298 FXYD6 0.829814383552752 0.166621066841455 0.00356454960579353 FXYD domain containing ion transport regulator 6 . DISEASE: Schizophrenia 2 (SCZD2) [MIM:603342]: A complex, multifactorial psychotic disorder or group of disorders characterized by disturbances in the form and content of thought (e.g. delusions, hallucinations), in mood (e.g. inappropriate affect), in sense of self and relationship to the external world (e.g. loss of ego boundaries, withdrawal), and in behavior (e.g bizarre or apparently purposeless behavior). Although it affects emotions, it is distinguished from mood disorders in which such disturbances are primary. Similarly, there may be mild impairment of cognitive function, and it is distinguished from the dementias in which disturbed cognitive function is considered primary. Some patients manifest schizophrenic as well as bipolar disorder symptoms and are often given the diagnosis of schizoaffective disorder. {ECO:0000269|PubMed:17357072}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;thyroid;bone;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;cerebellum cortex;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; amygdala;whole brain;occipital lobe;globus pallidus;parietal lobe; 0.31291 0.12971 0.235309407 68.71903751 1.61538 0.05272 FXYD6-FXYD2 0.637758562604967 0.355571610076315 0.00666982731871779 FXYD6-FXYD2 readthrough . . . . . . . . . 33.58013 1.03663 FXYD6P1 . . . FXYD domain containing ion transport regulator 6 pseudogene 1 . . . . . . . . . . . FXYD6P2 . . . FXYD domain containing ion transport regulator 6 pseudogene 2 . . . . . . . . . . . FXYD6P3 . . . FXYD domain containing ion transport regulator 6 pseudogene 3 . . . . . 0.16715 . . . . . FXYD7 0.122293436649701 0.779799774896313 0.0979067884539856 FXYD domain containing ion transport regulator 7 . . . unclassifiable (Anatomical System);frontal lobe;cartilage;ovary;endometrium;hypothalamus;placenta;parathyroid;brain; amygdala;dorsal root ganglion;whole brain;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; . 0.11262 0.057118534 57.99716914 1031.4616 6.16923 FYB 0.792005858585418 0.207983176246404 1.09651681787723e-05 FYN binding protein FUNCTION: Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells. Modulates the expression of interleukin-2 (IL-2). Involved in platelet activation. Prevents the degradation of SKAP1 and SKAP2. May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton. {ECO:0000269|PubMed:10747096, ECO:0000269|PubMed:15849195, ECO:0000269|PubMed:16980616}.; . TISSUE SPECIFICITY: Expressed in hematopoietic tissues such as myeloid and T-cells, spleen and thymus. Not expressed in B-cells, nor in non-lymphoid tissues.; unclassifiable (Anatomical System);medulla oblongata;lymph node;tongue;bone marrow;breast;uterus;epididymis;nasopharynx;thyroid;placenta;liver;spleen;germinal center;kidney;tonsil;thymus; superior cervical ganglion;white blood cells;atrioventricular node;whole blood;parietal lobe;skeletal muscle; 0.07439 0.19683 -0.176292081 40.56381222 438.57455 4.36533 FYCO1 9.66912529361977e-13 0.993090186028509 0.00690981397052423 FYVE and coiled-coil domain containing 1 FUNCTION: May mediate microtubule plus end-directed vesicle transport. {ECO:0000269|PubMed:20100911}.; . TISSUE SPECIFICITY: Expressed in heart and skeletal muscle. {ECO:0000269|PubMed:11896456}.; ovary;sympathetic chain;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;artery;unclassifiable (Anatomical System);cartilage;heart;pineal body;spinal cord;muscle;blood;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;tongue;globus pallidus;atrioventricular node;skeletal muscle; 0.07842 0.09492 3.045022694 99.23920736 6643.52317 17.25477 FYN 0.99563570991725 0.00436427432306385 1.57596863424065e-08 FYN proto-oncogene, Src family tyrosine kinase FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta- catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1. {ECO:0000269|PubMed:11005864, ECO:0000269|PubMed:11162638, ECO:0000269|PubMed:11536198, ECO:0000269|PubMed:12788081, ECO:0000269|PubMed:14707117, ECO:0000269|PubMed:14761972, ECO:0000269|PubMed:15536091, ECO:0000269|PubMed:15557120, ECO:0000269|PubMed:16387660, ECO:0000269|PubMed:16841086, ECO:0000269|PubMed:17194753, ECO:0000269|PubMed:18056706, ECO:0000269|PubMed:18258597, ECO:0000269|PubMed:19179337, ECO:0000269|PubMed:19652227, ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:22080863, ECO:0000269|PubMed:7568038, ECO:0000269|PubMed:7822789}.; . TISSUE SPECIFICITY: Isoform 1 is highly expressed in the brain. Isoform 2 is expressed in cells of hemopoietic lineages, especially T-lymphocytes. {ECO:0000269|PubMed:10196263}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; amygdala;superior cervical ganglion;spinal cord;prefrontal cortex;white blood cells;skeletal muscle;cingulate cortex; 0.99540 0.83848 -0.53631094 20.53550366 33.47213 1.03240 FYTTD1 0.829001566647634 0.170843098172685 0.000155335179681369 forty-two-three domain containing 1 FUNCTION: Required for mRNA export from the nucleus to the cytoplasm. Acts as an adapter that uses the DDX39B/UAP56-NFX1 pathway to ensure efficient mRNA export and delivering to the nuclear pore. Associates with spliced and unspliced mRNAs simultaneously with ALYREF/THOC4. {ECO:0000269|PubMed:19836239}.; . TISSUE SPECIFICITY: Expressed in a wide variety of cancer types. {ECO:0000269|PubMed:25662211}.; lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;amygdala;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;lung;mesenchyma;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;cerebellum; testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.15810 0.10356 0.038710339 56.92380278 35.69383 1.07400 FYTTD1P1 . . . forty-two-three domain containing 1 pseudogene 1 . . . . . . . . . . . FZD1 0.344486647877948 0.65261098129921 0.0029023708228426 frizzled class receptor 1 FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK- 3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Activated by Wnt3A, Wnt3, Wnt1 and to a lesser extent Wnt2, but not by Wnt4, Wnt5A, Wnt5B, Wnt6, Wnt7A or Wnt7B.; . TISSUE SPECIFICITY: Expressed in adult heart, placenta, lung, kidney, pancreas, prostate, and ovary and in fetal lung and kidney.; smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;synovium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;thyroid;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.94576 0.22819 -0.912929826 9.902099552 3999.71723 12.51910 FZD2 . . . frizzled class receptor 2 FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK- 3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues.; . TISSUE SPECIFICITY: Widely expressed. In the adult, mainly found in heart, placenta, skeletal muscle, lung, kidney, pancreas, prostate, testis, ovary and colon. In the fetus, expressed in brain, lung and kidney. Low levels in fetal liver.; unclassifiable (Anatomical System);lymphoreticular;lung;whole body;cartilage;endometrium;bone;visual apparatus;testis;kidney;brain; superior cervical ganglion; 0.81707 0.22085 0.483275131 79.25218212 62.74872 1.62086 FZD3 0.275435382319683 0.724353383734043 0.000211233946274137 frizzled class receptor 3 FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK- 3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Activation by Wnt5A stimulates PKC activity via a G-protein-dependent mechanism. Involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Plays a role in controlling early axon growth and guidance processes necessary for the formation of a subset of central and peripheral major fiber tracts. Required for the development of major fiber tracts in the central nervous system, including: the anterior commissure, the corpus callosum, the thalamocortical, corticothalamic and nigrostriatal tracts, the corticospinal tract, the fasciculus retroflexus, the mammillothalamic tract, the medial lemniscus, and ascending fiber tracts from the spinal cord to the brain. In the peripheral nervous system, controls axon growth in distinct populations of cranial and spinal motor neurons, including the facial branchimotor nerve, the hypoglossal nerve, the phrenic nerve, and motor nerves innervating dorsal limbs. Involved in the migration of cranial neural crest cells. May also be implicated in the transmission of sensory information from the trunk and limbs to the brain. Controls commissural sensory axons guidance after midline crossing along the anterior-posterior axis in the developing spinal cord in a Wnt-dependent signaling pathway. Together with FZD6, is involved in the neural tube closure and plays a role in the regulation of the establishment of planar cell polarity (PCP), particularly in the orientation of asymmetric bundles of stereocilia on the apical faces of a subset of auditory and vestibular sensory cells located in the inner ear. Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle in a beta-catenin-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q61086}.; . TISSUE SPECIFICITY: Widely expressed. Relatively high expression in the CNS, including regions of the limbic system, in kidney, pancreas, skeletal muscle, uterus and testis.; unclassifiable (Anatomical System);ovary;heart;colon;skin;retina;uterus;prostate;lung;cerebral cortex;larynx;visual apparatus;duodenum;testis;head and neck;germinal center;kidney;brain;aorta;stomach; superior cervical ganglion;trigeminal ganglion; 0.48316 0.14212 -0.890882376 10.30313753 20.93006 0.70850 FZD4 0.920786850569231 0.0787189442283831 0.000494205202385426 frizzled class receptor 4 FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin (CTNNB1) canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin (CTNNB1) and activation of Wnt target genes. Plays a critical role in retinal vascularization by acting as a receptor for Wnt proteins and norrin (NDP). In retina, it can be both activated by Wnt protein-binding, but also by a Wnt-independent signaling via binding of norrin (NDP), promoting in both cases beta-catenin (CTNNB1) accumulation and stimulation of LEF/TCF-mediated transcriptional programs. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues.; DISEASE: Vitreoretinopathy, exudative 1 (EVR1) [MIM:133780]: A disorder of the retinal vasculature characterized by an abrupt cessation of growth of peripheral capillaries, leading to an avascular peripheral retina. This may lead to compensatory retinal neovascularization, which is thought to be induced by hypoxia from the initial avascular insult. New vessels are prone to leakage and rupture causing exudates and bleeding, followed by scarring, retinal detachment and blindness. Clinical features can be highly variable, even within the same family. Patients with mild forms of the disease are asymptomatic, and their only disease related abnormality is an arc of avascular retina in the extreme temporal periphery. In many ways the disease resembles retinopathy of prematurity but there is no evidence of prematurity or small birth weight in the patient history. {ECO:0000269|PubMed:12172548, ECO:0000269|PubMed:14507768, ECO:0000269|PubMed:15035989, ECO:0000269|PubMed:15223780, ECO:0000269|PubMed:15370539, ECO:0000269|PubMed:15488808, ECO:0000269|PubMed:15733276, ECO:0000269|PubMed:15981244, ECO:0000269|PubMed:17093393, ECO:0000269|PubMed:19172507, ECO:0000269|PubMed:19324841, ECO:0000269|PubMed:20340138}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Almost ubiquitous. Largely expressed in adult heart, skeletal muscle, ovary, and fetal kidney. Moderate amounts in adult liver, kidney, pancreas, spleen, and fetal lung, and small amounts in placenta, adult lung, prostate, testis, colon, fetal brain and liver.; . . 0.34940 0.20970 -0.334253673 30.70299599 215.98465 3.17366 FZD5 0.898345425581581 0.100721257807842 0.000933316610577375 frizzled class receptor 5 FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK- 3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Interacts specifically with Wnt5A to induce the beta- catenin pathway. {ECO:0000269|PubMed:10097073}.; . . unclassifiable (Anatomical System);prostate;cartilage;ovary;bone;placenta;amnion;liver;colon;spleen;kidney;skeletal muscle;stomach; superior cervical ganglion;fetal liver;trigeminal ganglion;skeletal muscle; 0.71406 0.20120 -0.205617011 38.57631517 180.92805 2.92412 FZD6 8.02772643839484e-08 0.716747382496496 0.283252537226239 frizzled class receptor 6 FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK- 3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Together with FZD3, is involved in the neural tube closure and plays a role in the regulation of the establishment of planar cell polarity (PCP), particularly in the orientation of asymmetric bundles of stereocilia on the apical faces of a subset of auditory and vestibular sensory cells located in the inner ear (By similarity). {ECO:0000250|UniProtKB:Q61089}.; DISEASE: Nail disorder, non-syndromic congenital, 10 (NDNC10) [MIM:614157]: A nail disorder characterized by a variable degree of onychauxis (thick nails), hyponychia, and onycholysis of all nails, with claw-shaped fingernails in some individuals. No other anomalies of ectodermal tissues, including hair, teeth, sweat glands, or skin, are noted, and individuals with dysplastic nails have normal hearing and normal psychomotor development. {ECO:0000269|PubMed:21665003}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Rare non-synonymous variants in FZD6 may contribute to neural tube defects, congenital malformations of the central nervous system and adjacent structures related to defective neural tube closure during the first trimester of pregnancy.; TISSUE SPECIFICITY: Detected in adult heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, thymus, prostate, testis, ovary, small intestine and colon. In the fetus, expressed in brain, lung, liver and kidney.; ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;gum;bone;thyroid;pituitary gland;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;urinary;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;placenta;hypopharynx;liver;spleen;head and neck;kidney;aorta;stomach; superior cervical ganglion;appendix;atrioventricular node;trigeminal ganglion; 0.34946 0.19092 1.001272896 90.72304789 5226.90716 14.88551 FZD7 0.73019872989797 0.267066520315932 0.00273474978609707 frizzled class receptor 7 FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK- 3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues.; . TISSUE SPECIFICITY: High expression in adult skeletal muscle and fetal kidney, followed by fetal lung, adult heart, brain, and placenta. Specifically expressed in squamous cell esophageal carcinomas.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;duodenum;alveolus;spleen;head and neck;kidney;mammary gland;aorta;cerebellum; superior cervical ganglion;cerebellum peduncles;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.84885 0.20046 -0.468351206 23.42533616 58.65393 1.55143 FZD8 . . . frizzled class receptor 8 FUNCTION: Receptor for Wnt proteins. Component of the Wnt-Fzd- LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome- sized signalosomes. The beta-catenin canonical signaling pathway leads to the activation of disheveled proteins, inhibition of GSK- 3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Coreceptor along with RYK of Wnt proteins, such as WNT1. {ECO:0000269|PubMed:11448771}.; . TISSUE SPECIFICITY: Most abundant in fetal kidney, followed by brain and lung. In adult tissues, expressed in kidney, heart, pancreas and skeletal muscle.; . . 0.27396 0.22085 -0.714505427 14.4019816 38.10857 1.13240 FZD9 . . . frizzled class receptor 9 FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK- 3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues.; . TISSUE SPECIFICITY: Expressed predominantly in adult and fetal brain, testis, eye, skeletal muscle and kidney. Moderately expressed in pancreas, thyroid, adrenal cortex, small intestine and stomach. Detected in fetal liver and kidney.; unclassifiable (Anatomical System);lung;cartilage;hypothalamus;spleen;brain;skin; dorsal root ganglion;thalamus;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11300 0.14212 -0.337894035 30.37272942 59.1934 1.56065 FZD10 . . . frizzled class receptor 10 FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK- 3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues.; . TISSUE SPECIFICITY: Highest levels in the placenta and fetal kidney, followed by fetal lung and brain. In adult brain, abundantly expressed in the cerebellum, followed by cerebral cortex, medulla and spinal cord; very low levels in total brain, frontal lobe, temporal lobe and putamen. Weak expression detected in adult brain, heart, lung, skeletal muscle, pancreas, spleen and prostate.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;spinal cord;colon;skin;uterus;lung;cochlea;endometrium;cervix;kidney;brain;stomach; superior cervical ganglion; 0.38719 0.15548 -0.912929826 9.902099552 46.18818 1.30976 FZD10-AS1 . . . FZD10 antisense RNA 1 (head to head) . . . . . . . . . . . FZR1 0.99794752523794 0.00205241369227964 6.106978071536e-08 fizzy/cell division cycle 20 related 1 FUNCTION: Key regulator of ligase activity of the anaphase promoting complex/cyclosome (APC/C), which confers substrate specificity upon the complex. Associates with the APC/C in late mitosis, in replacement of CDC20, and activates the APC/C during anaphase and telophase. The APC/C remains active in degrading substrates to ensure that positive regulators of the cell cycle do not accumulate prematurely. At the G1/S transition FZR1 is phosphorylated, leading to its dissociation from the APC/C. Following DNA damage, it is required for the G2 DNA damage checkpoint: its dephosphorylation and reassociation with the APC/C leads to the ubiquitination of PLK1, preventing entry into mitosis. {ECO:0000269|PubMed:18662541, ECO:0000269|PubMed:21596315, ECO:0000269|PubMed:9734353}.; . TISSUE SPECIFICITY: Isoform 2 is expressed at high levels in heart, liver, spleen and some cancer cell lines whereas isoform 3 is expressed only at low levels in these tissues. {ECO:0000269|PubMed:12797865}.; salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;larynx;synovium;bone;iris;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;oral cavity;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;cingulate cortex; 0.90616 0.13588 -0.80269335 12.23755603 10.58122 0.38471 G2E3 0.751141211279106 0.248858038757634 7.49963259732346e-07 G2/M-phase specific E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Essential in early embryonic development to prevent apoptotic death. {ECO:0000269|PubMed:18511420}.; . TISSUE SPECIFICITY: Predominantly expressed in brain, liver, kidney, testes and ovary. {ECO:0000269|PubMed:10718198}.; ovary;salivary gland;colon;parathyroid;vein;skin;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.13015 0.09390 0.373041938 75.29488087 239.73907 3.34628 G3BP1 0.98839076401586 0.011609063380795 1.72603345243806e-07 G3BP stress granule assembly factor 1 FUNCTION: May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium- dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA. {ECO:0000269|PubMed:11604510, ECO:0000269|PubMed:9889278}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - interstitial;trigeminal ganglion;skeletal muscle; 0.91724 0.16278 -0.361761279 28.6329323 35.68074 1.07372 G3BP2 0.983145417305228 0.0168541514223992 4.31272372810046e-07 G3BP stress granule assembly factor 2 FUNCTION: Probable scaffold protein that may be involved in mRNA transport. {ECO:0000305}.; . . ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;amygdala;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;uterus;whole body;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; whole brain;amygdala;occipital lobe;testis - interstitial;medulla oblongata;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.96341 0.18404 -0.317668748 31.45789101 27.08786 0.87395 G6PC 0.00181135620983483 0.899736377134395 0.0984522666557705 glucose-6-phosphatase catalytic subunit FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production through glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels.; DISEASE: Glycogen storage disease 1A (GSD1A) [MIM:232200]: A metabolic disorder characterized by impairment of terminal steps of glycogenolysis and gluconeogenesis. Patients manifest a wide range of clinical symptoms and biochemical abnormalities, including hypoglycemia, severe hepatomegaly due to excessive accumulation of glycogen, kidney enlargement, growth retardation, lactic acidemia, hyperlipidemia, and hyperuricemia. {ECO:0000269|PubMed:10070617, ECO:0000269|PubMed:10094563, ECO:0000269|PubMed:10447271, ECO:0000269|PubMed:10612834, ECO:0000269|PubMed:10738005, ECO:0000269|PubMed:10748407, ECO:0000269|PubMed:10874313, ECO:0000269|PubMed:10960498, ECO:0000269|PubMed:11058903, ECO:0000269|PubMed:11058910, ECO:0000269|PubMed:12373566, ECO:0000269|PubMed:15151508, ECO:0000269|PubMed:15316959, ECO:0000269|PubMed:15542400, ECO:0000269|PubMed:7573034, ECO:0000269|PubMed:7623438, ECO:0000269|PubMed:7655466, ECO:0000269|PubMed:8182131, ECO:0000269|PubMed:8733042, ECO:0000269|PubMed:9001800, ECO:0000269|PubMed:9332655, ECO:0000269|PubMed:9506659, ECO:0000269|PubMed:9700612, ECO:0000269|PubMed:9700613}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . liver;spleen;kidney; superior cervical ganglion;fetal liver;liver;appendix;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;parietal lobe; 0.89328 0.79464 -0.736552314 13.93606983 18.80998 0.64957 G6PC2 1.91255841634904e-09 0.0670405037604778 0.932959494326964 glucose-6-phosphatase catalytic subunit 2 FUNCTION: May hydrolyze glucose-6-phosphate to glucose in the endoplasmic reticulum. May be responsible for glucose production through glycogenolysis and gluconeogenesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in pancreas and also detected to a lower extent in testis. Expressed by most islet cells in the pancreas (at protein level). {ECO:0000269|PubMed:11297555}.; islets of Langerhans; superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13013 0.15428 0.687150476 85.17928757 4473.63161 13.41934 G6PC3 1.07483483664146e-05 0.572699007388306 0.427290244263327 glucose 6 phosphatase catalytic subunit 3 FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. May form with the glucose-6-phosphate transporter (SLC37A4/G6PT) a ubiquitously expressed complex responsible for glucose production through glycogenolysis and gluconeogenesis. Probably required for normal neutrophil function. {ECO:0000269|PubMed:12370122, ECO:0000269|PubMed:12965222, ECO:0000269|PubMed:13129915}.; DISEASE: Dursun syndrome (DURSS) [MIM:612541]: A disease characterized by pulmonary arterial hypertension, cardiac abnormalities including secundum-type atrial septal defect, intermittent neutropenia, lymphopenia, monocytosis and anemia. {ECO:0000269|PubMed:20799326}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in skeletal muscle, at intermediate levels in heart, brain, placenta, kidney, colon, thymus, spleen and pancreas. Also detected in testis, prostate, ovary, liver, lung, small intestine and peripheral blood lymphocytes. {ECO:0000269|PubMed:12370122, ECO:0000269|PubMed:12965222, ECO:0000269|PubMed:14765991}.; medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;choroid;vein;skin;retina;bone marrow;uterus;prostate;endometrium;bone;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;hippocampus;duodenum;liver;amnion;spleen;cervix;kidney;mammary gland;stomach; whole brain;superior cervical ganglion;thyroid;testis;kidney; 0.19416 0.16745 0.21689899 68.12927577 213.57014 3.15387 G6PD 0.966391447459592 0.0335968270329679 1.17255074395504e-05 glucose-6-phosphate dehydrogenase FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. {ECO:0000269|PubMed:15858258, ECO:0000269|PubMed:24769394}.; DISEASE: Anemia, non-spherocytic hemolytic, due to G6PD deficiency (NSHA) [MIM:300908]: A disease characterized by G6PD deficiency, acute hemolytic anemia, fatigue, back pain, and jaundice. In most patients, the disease is triggered by an exogenous agent, such as some drugs, food, or infection. Increased unconjugated bilirubin, lactate dehydrogenase, and reticulocytosis are markers of the disorder. Although G6PD deficiency can be life-threatening, most patients are asymptomatic throughout their life. {ECO:0000269|PubMed:1611091}. Note=The disease is caused by mutations affecting the gene represented in this entry. Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of NSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class- IV have near normal activity.; TISSUE SPECIFICITY: Isoform Long is found in lymphoblasts, granulocytes and sperm.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum;thymus; adipose tissue;testis - seminiferous tubule;testis;whole blood; 0.37858 0.98951 -0.135838822 43.77211607 506.24881 4.61763 G6PR . . . glucose-6-phosphatase regulator . . . . . . . . . . . GAA 4.62006515849408e-11 0.781839837847216 0.218160162106584 glucosidase, alpha; acid FUNCTION: Essential for the degradation of glygogen to glucose in lysosomes.; DISEASE: Glycogen storage disease 2 (GSD2) [MIM:232300]: A metabolic disorder with a broad clinical spectrum. The severe infantile form, or Pompe disease, presents at birth with massive accumulation of glycogen in muscle, heart and liver. Cardiomyopathy and muscular hypotonia are the cardinal features of this form whose life expectancy is less than two years. The juvenile and adult forms present as limb-girdle muscular dystrophy beginning in the lower limbs. Final outcome depends on respiratory muscle failure. Patients with the adult form can be free of clinical symptoms for most of their life but finally develop a slowly progressive myopathy. {ECO:0000269|PubMed:10189220, ECO:0000269|PubMed:10206684, ECO:0000269|PubMed:10338092, ECO:0000269|PubMed:10737124, ECO:0000269|PubMed:11071489, ECO:0000269|PubMed:11738358, ECO:0000269|PubMed:12601120, ECO:0000269|PubMed:12923862, ECO:0000269|PubMed:14643388, ECO:0000269|PubMed:14695532, ECO:0000269|PubMed:14972326, ECO:0000269|PubMed:15145338, ECO:0000269|PubMed:15668445, ECO:0000269|PubMed:16433701, ECO:0000269|PubMed:1652892, ECO:0000269|PubMed:16782080, ECO:0000269|PubMed:1684505, ECO:0000269|PubMed:16917947, ECO:0000269|PubMed:17643989, ECO:0000269|PubMed:18425781, ECO:0000269|PubMed:18429042, ECO:0000269|PubMed:1898413, ECO:0000269|PubMed:19588081, ECO:0000269|PubMed:20080426, ECO:0000269|PubMed:20350966, ECO:0000269|PubMed:21109266, ECO:0000269|PubMed:22644586, ECO:0000269|PubMed:22676651, ECO:0000269|PubMed:25681614, ECO:0000269|PubMed:7695647, ECO:0000269|PubMed:7717400, ECO:0000269|PubMed:7866409, ECO:0000269|PubMed:7881422, ECO:0000269|PubMed:7981676, ECO:0000269|PubMed:8094613, ECO:0000269|PubMed:8401535, ECO:0000269|PubMed:8834250, ECO:0000269|PubMed:9521422, ECO:0000269|PubMed:9535769, ECO:0000269|PubMed:9660056, ECO:0000269|Ref.5}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;uterus;prostate;oesophagus;thyroid;bone;iris;testis;brain;bladder;pineal gland;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;urinary;muscle;pancreas;lung;placenta;visual apparatus;alveolus;spleen;cervix;kidney;mammary gland;stomach; placenta;testis; 0.11717 0.93517 -1.159397299 6.098136353 1841.49194 7.91500 GAB1 0.686084015452251 0.313908552691924 7.4318558244337e-06 GRB2 associated binding protein 1 FUNCTION: Adapter protein that plays a role in intracellular signaling cascades triggered by activated receptor-type kinases. Plays a role in FGFR1 signaling. Probably involved in signaling by the epidermal growth factor receptor (EGFR) and the insulin receptor (INSR).; . . unclassifiable (Anatomical System);heart;colon;skin;bone marrow;breast;uterus;prostate;whole body;lung;ganglion;frontal lobe;bone;placenta;pituitary gland;liver;testis;spleen;kidney;brain; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.56132 0.13791 -0.003562597 53.72729417 88.08154 2.00855 GAB2 0.998921870889081 0.00107812653896496 2.57195380671025e-09 GRB2 associated binding protein 2 FUNCTION: Adapter protein which acts downstream of several membrane receptors including cytokine, antigen, hormone, cell matrix and growth factor receptors to regulate multiple signaling pathways. Regulates osteoclast differentiation mediating the TNFRSF11A/RANK signaling. In allergic response, it plays a role in mast cells activation and degranulation through PI-3-kinase regulation. Also involved in the regulation of cell proliferation and hematopoiesis. {ECO:0000269|PubMed:15750601, ECO:0000269|PubMed:19172738}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; subthalamic nucleus;globus pallidus; 0.33753 0.45406 -1.041578376 7.773059684 308.9105 3.74187 GAB3 0.990602402777157 0.00939508748109694 2.50974174584155e-06 GRB2 associated binding protein 3 . . . . . 0.23691 0.10150 -0.049474214 50.01179523 56.46274 1.51162 GAB4 6.04411095952199e-06 0.689473192905826 0.310520762983215 GRB2 associated binding protein family member 4 . . . . . 0.07436 0.06872 1.025142459 91.07100731 4763.03429 13.97563 GABARAP 0.670186209633902 0.324830321569822 0.00498346879627505 GABA(A) receptor-associated protein FUNCTION: Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in apoptosis. Involved in autophagy. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. {ECO:0000269|PubMed:15977068}.; . TISSUE SPECIFICITY: Heart, brain, placenta, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:11146101, ECO:0000269|PubMed:9892355}.; myocardium;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;artery;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;islets of Langerhans;hypothalamus;oral cavity;muscle;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; testis; 0.35309 0.19444 0.101211609 60.95777306 . . GABARAPL1 0.782335274522732 0.210786532043507 0.00687819343376167 GABA(A) receptor-associated protein like 1 FUNCTION: Ubiquitin-like modifier that increases cell-surface expression of kappa-type opioid receptor through facilitating anterograde intracellular trafficking of the receptor. Involved in formation of autophagosomal vacuoles. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. {ECO:0000269|PubMed:16431922, ECO:0000269|PubMed:20404487}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed at very high levels in the brain, heart, peripheral blood leukocytes, liver, kidney, placenta and skeletal muscle. Expressed at very low levels in thymus and small intestine. In the brain, expression is particularly intense in motoneurons in the embryo and in neurons involved in somatomotor and neuroendocrine functions in the adult, particularly in the substantia nigra pars compacta. {ECO:0000269|PubMed:11374880, ECO:0000269|PubMed:11414770, ECO:0000269|PubMed:23690988}.; ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;gall bladder;heart;cartilage;tongue;urinary;spinal cord;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;vein;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;small intestine;cerebellum cortex;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;head and neck;kidney;stomach;cerebellum; whole brain;subthalamic nucleus; . 0.14229 0.057118534 57.99716914 1.37955 0.04890 GABARAPL2 0.000743181272649561 0.526099312336043 0.473157506391308 GABA(A) receptor-associated protein like 2 FUNCTION: Ubiquitin-like modifier involved in intra-Golgi traffic. Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation. It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1 (By similarity). Involved in autophagy. Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. {ECO:0000250, ECO:0000269|PubMed:20418806, ECO:0000269|PubMed:23209295}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the brain, heart, prostate, ovary, spleen and skeletal muscle. Expressed at very low levels in lung, thymus and small intestine. {ECO:0000269|PubMed:11146101, ECO:0000269|PubMed:11414770}.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;spinal cord;pharynx;blood;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;peripheral nerve;salivary gland;developmental;intestine;colon;fovea centralis;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;kidney;stomach;aorta; whole brain;amygdala;occipital lobe;subthalamic nucleus;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;globus pallidus;caudate nucleus;parietal lobe;cerebellum; 0.36793 0.15588 -0.053113545 49.38664779 2.40691 0.08498 GABARAPL3 0.01940596500072 0.504383523752435 0.476210511246845 GABA(A) receptors associated protein like 3, pseudogene FUNCTION: Ubiquitin-like modifier involved in autophagosome formation. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed at very high levels in the brain, heart, peripheral blood leukocytes, liver, kidney, placenta and skeletal muscle. Expressed at very low levels in thymus and small intestine. {ECO:0000269|PubMed:11414770}.; . . . 0.13588 . . 475.10373 4.50403 GABBR1 0.999969901472702 3.00985272128555e-05 8.51371829336864e-14 gamma-aminobutyric acid type B receptor subunit 1 FUNCTION: Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Calcium is required for high affinity binding to GABA. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception. Activated by (-)-baclofen, cgp27492 and blocked by phaclofen.; . TISSUE SPECIFICITY: Highly expressed in brain and weakly in heart, small intestine and uterus. Isoform 1A is mostly expressed in granular cell and molecular layer. Isoform 1B is mostly expressed in Purkinje cells. Isoform 1E is predominantly expressed in peripheral tissues as kidney, lung, trachea, colon, small intestine, stomach, bone marrow, thymus and mammary gland. {ECO:0000269|PubMed:9844003}.; ovary;sympathetic chain;colon;substantia nigra;fovea centralis;choroid;retina;uterus;optic nerve;frontal lobe;endometrium;larynx;testis;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;tongue;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; . 0.06622 . -0.426079032 25.36565228 1567.59549 7.32856 GABBR2 0.999790262521872 0.000209737468490762 9.63726054104311e-12 gamma-aminobutyric acid type B receptor subunit 2 FUNCTION: Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception. {ECO:0000269|PubMed:10328880, ECO:0000269|PubMed:18165688, ECO:0000269|PubMed:22660477, ECO:0000269|PubMed:24305054, ECO:0000269|PubMed:9872316}.; . TISSUE SPECIFICITY: Highly expressed in brain, especially in cerebral cortex, thalamus, hippocampus, frontal, occipital and temporal lobe, occipital pole and cerebellum, followed by corpus callosum, caudate nucleus, spinal cord, amygdala and medulla. Weakly expressed in heart, testis and skeletal muscle. {ECO:0000269|PubMed:10087195, ECO:0000269|PubMed:10328880, ECO:0000269|PubMed:10727622}.; unclassifiable (Anatomical System);amygdala;ovary;hypothalamus;adrenal cortex;parathyroid;fovea centralis;skeletal muscle;optic nerve;whole body;lung;frontal lobe;placenta;macula lutea;visual apparatus;liver;spleen;pineal gland;brain;cerebellum; amygdala;whole brain;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;pons;atrioventricular node;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.72097 0.15588 -1.285933373 5.083746167 1340.48679 6.87315 GABPA 0.973789161166602 0.0262095571186937 1.28171470473864e-06 GA binding protein transcription factor alpha subunit FUNCTION: Transcription factor capable of interacting with purine rich repeats (GA repeats). Necessary for the expression of the Adenovirus E4 gene.; . . myocardium;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;small intestine;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; . 0.15204 0.19130 -0.405853867 26.23260203 13.41069 0.48783 GABPAP . . . GA binding protein transcription factor alpha subunit pseudogene FUNCTION: Transcription factor capable of interacting with purine rich repeats (GA repeats). Necessary for the expression of the Adenovirus E4 gene. {ECO:0000269|PubMed:10675337, ECO:0000269|PubMed:8816484}.; . . . . . 0.19444 0.347360312 73.97381458 . . GABPB1 0.929888310247904 0.0700966502099665 1.5039542129485e-05 GA binding protein transcription factor beta subunit 1 FUNCTION: Transcription factor capable of interacting with purine rich repeats (GA repeats). Necessary for the expression of the Adenovirus E4 gene. {ECO:0000269|PubMed:10675337, ECO:0000269|PubMed:8816484}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; . 0.19444 0.347360312 73.97381458 25.43283 0.83017 GABPB1-AS1 . . . GABPB1 antisense RNA 1 . . . . . . . . . . . GABPB2 0.00262905195509113 0.982899001962967 0.0144719460819422 GA binding protein transcription factor beta subunit 2 FUNCTION: May function as transcription factor capable of interacting with purine rich repeats (GA repeats). {ECO:0000250}.; . . . . . 0.09759 0.262810045 70.43524416 2570.24909 9.47325 GABRA1 0.963866034985763 0.0361199250282176 1.40399860194151e-05 gamma-aminobutyric acid type A receptor alpha1 subunit FUNCTION: Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand- gated chloride channel (By similarity). {ECO:0000250}.; DISEASE: Epilepsy, childhood absence 4 (ECA4) [MIM:611136]: A subtype of idiopathic generalized epilepsy characterized by an onset at age 6-7 years, frequent absence seizures (several per day) and bilateral, synchronous, symmetric 3-Hz spike waves on EEG. Tonic-clonic seizures often develop in adolescence. Absence seizures may either remit or persist into adulthood. {ECO:0000269|PubMed:16718694}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Epilepsy, idiopathic generalized 13 (EIG13) [MIM:611136]: A disorder characterized by recurring generalized seizures in the absence of detectable brain lesions and/or metabolic abnormalities. Generalized seizures arise diffusely and simultaneously from both hemispheres of the brain. Seizure types include juvenile myoclonic seizures, absence seizures, and generalized tonic-clonic seizures. {ECO:0000269|PubMed:21714819}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Juvenile myoclonic epilepsy 5 (EJM5) [MIM:611136]: A subtype of idiopathic generalized epilepsy. Patients have afebrile seizures only, with onset in adolescence (rather than in childhood) and myoclonic jerks which usually occur after awakening and are triggered by sleep deprivation and fatigue. {ECO:0000269|PubMed:11992121}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Epileptic encephalopathy, early infantile, 19 (EIEE19) [MIM:615744]: A severe neurologic disorder characterized by onset of seizures in the first months of life and usually associated with EEG abnormalities. Affected infants have convulsive seizures (hemiclonic or generalized) that are often prolonged and triggered by fever. Other seizure types include focal, myoclonic, absence seizures, and drop attacks. Development is normal in the first year of life with later slowing and intellectual disability. {ECO:0000269|PubMed:24623842}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . amygdala;frontal lobe;cerebellum cortex;adrenal gland;hypothalamus;macula lutea;fovea centralis;brain;cerebellum; amygdala;whole brain;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.56574 0.26790 -0.449946534 24.00330267 14.94107 0.53856 GABRA2 0.976963701382334 0.0230316967056161 4.60191204986479e-06 gamma-aminobutyric acid type A receptor alpha2 subunit FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.; . . unclassifiable (Anatomical System);lung;ovary;hypothalamus;placenta;hippocampus;parathyroid;brain; amygdala;occipital lobe;superior cervical ganglion;subthalamic nucleus;medulla oblongata;temporal lobe;prefrontal cortex;globus pallidus;pons;parietal lobe; 0.31694 0.13475 -0.273576253 33.97027601 19.24152 0.66325 GABRA3 0.273213945815421 0.721614475448021 0.00517157873655736 gamma-aminobutyric acid type A receptor alpha3 subunit FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.; . . . . 0.04073 0.21583 -0.05129383 49.75819769 7.92122 0.29087 GABRA4 0.981416568659062 0.0185807215921206 2.70974881729007e-06 gamma-aminobutyric acid type A receptor alpha4 subunit FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.; . . unclassifiable (Anatomical System);frontal lobe;hypothalamus;placenta;hippocampus;liver;spleen;brain;skeletal muscle;aorta; superior cervical ganglion;medulla oblongata;ciliary ganglion;pons;caudate nucleus;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex;skeletal muscle; 0.15547 0.13425 0.260991686 70.25831564 2958.52439 10.30300 GABRA5 0.951529195038544 0.0484415703076528 2.92346538030347e-05 gamma-aminobutyric acid type A receptor alpha5 subunit FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.; . . unclassifiable (Anatomical System);amygdala;hypothalamus;choroid;fovea centralis;lens;skeletal muscle;skin;retina;optic nerve;lung;hippocampus;macula lutea;testis;brain; dorsal root ganglion;whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;pons;caudate nucleus;atrioventricular node;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.40940 0.19440 -0.358119787 29.16371786 61.82121 1.60284 GABRA6 9.41937064600856e-08 0.306354827729993 0.6936450780763 gamma-aminobutyric acid type A receptor alpha6 subunit FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.; . . unclassifiable (Anatomical System);cerebellum cortex;brain;skeletal muscle;cerebellum; cerebellum peduncles;skeletal muscle;cerebellum; 0.79098 0.16037 0.222355725 68.44184949 678.61776 5.20841 GABRB1 0.977782832819184 0.0222163153040257 8.51876790702126e-07 gamma-aminobutyric acid type A receptor beta1 subunit FUNCTION: Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand- gated chloride channel (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);frontal lobe;hypothalamus;bone;placenta;kidney;brain; amygdala;subthalamic nucleus;medulla oblongata;superior cervical ganglion;occipital lobe;temporal lobe;prefrontal cortex;globus pallidus;pons;trigeminal ganglion;cingulate cortex;parietal lobe; 0.31766 0.11156 -0.359940251 28.93371078 31.23713 0.98534 GABRB2 0.940299230468594 0.059690762733396 1.0006798009612e-05 gamma-aminobutyric acid type A receptor beta2 subunit FUNCTION: Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand- gated chloride channel. {ECO:0000269|PubMed:19763268, ECO:0000269|PubMed:8264558}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 show reduced expression in schizophrenic brain. Isoform 3 shows increased expression in schizophrenic and bipolar disorder brains while isoform 4 shows reduced expression. {ECO:0000269|PubMed:16983389, ECO:0000269|PubMed:19763268}.; unclassifiable (Anatomical System);amygdala;colon; superior cervical ganglion;pons; 0.31714 0.15588 -0.692458599 14.96815287 15.77729 0.56225 GABRB3 0.997073960271659 0.00292589469262432 1.45035717051528e-07 gamma-aminobutyric acid type A receptor beta3 subunit FUNCTION: Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand- gated chloride channel. {ECO:0000269|PubMed:18281286, ECO:0000269|PubMed:18514161, ECO:0000269|PubMed:22243422, ECO:0000269|PubMed:22303015, ECO:0000269|PubMed:24909990}.; DISEASE: Epilepsy, childhood absence 5 (ECA5) [MIM:612269]: A subtype of idiopathic generalized epilepsy characterized by an onset at age 6-7 years, frequent absence seizures (several per day) and bilateral, synchronous, symmetric 3-Hz spike waves on EEG. Tonic-clonic seizures often develop in adolescence. Absence seizures may either remit or persist into adulthood. {ECO:0000269|PubMed:18514161}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;whole body;larynx;visual apparatus;pituitary gland;testis;head and neck;kidney;brain;retina; dorsal root ganglion;subthalamic nucleus;globus pallidus;skeletal muscle;cingulate cortex; 0.87387 0.29110 -0.492218069 22.35786742 2410.54465 9.11838 GABRD 0.923498878454823 0.0764085129864542 9.26085587228242e-05 gamma-aminobutyric acid type A receptor delta subunit FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.; DISEASE: Generalized epilepsy with febrile seizures plus 5 (GEFS+5) [MIM:613060]: A rare autosomal dominant, familial condition with incomplete penetrance and large intrafamilial variability. Patients display febrile seizures persisting sometimes beyond the age of 6 years and/or a variety of afebrile seizure types. This disease combines febrile seizures, generalized seizures often precipitated by fever at age 6 years or more, and partial seizures, with a variable degree of severity. {ECO:0000269|PubMed:15115768}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Epilepsy, idiopathic generalized 10 (EIG10) [MIM:613060]: A disorder characterized by recurring generalized seizures in the absence of detectable brain lesions and/or metabolic abnormalities. Generalized seizures arise diffusely and simultaneously from both hemispheres of the brain. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Juvenile myoclonic epilepsy 7 (EJM7) [MIM:613060]: A subtype of idiopathic generalized epilepsy. Patients have afebrile seizures only, with onset in adolescence (rather than in childhood) and myoclonic jerks which usually occur after awakening and are triggered by sleep deprivation and fatigue. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . . . 0.14846 0.16992 -0.510624372 21.65015334 60.3441 1.57817 GABRE 0.000183719411945096 0.705422161666386 0.294394118921669 gamma-aminobutyric acid type A receptor epsilon subunit FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.; . TISSUE SPECIFICITY: Expressed in many tissues. Highest levels of expression in adult heart and placenta.; . . 0.41565 0.13483 1.820761234 97.009908 93.05133 2.07285 GABRG1 0.00847448373058956 0.978352684086311 0.0131728321830989 gamma-aminobutyric acid type A receptor gamma1 subunit FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.; . . unclassifiable (Anatomical System);amygdala;optic nerve;frontal lobe;hypothalamus;macula lutea;fovea centralis;choroid;lens;brain;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09734 0.08962 -0.80269335 12.23755603 45.46745 1.29537 GABRG2 0.958543398155425 0.0414525970013531 4.00484322195471e-06 gamma-aminobutyric acid type A receptor gamma2 subunit FUNCTION: Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand- gated chloride channel. {ECO:0000269|PubMed:2538761}.; DISEASE: Epilepsy, childhood absence 2 (ECA2) [MIM:607681]: A subtype of idiopathic generalized epilepsy characterized by an onset at age 6-7 years, frequent absence seizures (several per day) and bilateral, synchronous, symmetric 3-Hz spike waves on EEG. Tonic-clonic seizures often develop in adolescence. Some individuals manifest febrile seizures. Absence seizures may either remit or persist into adulthood. {ECO:0000269|PubMed:11326275}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Febrile seizures, familial, 8 (FEB8) [MIM:611277]: Seizures associated with febrile episodes in childhood without any evidence of intracranial infection or defined pathologic or traumatic cause. It is a common condition, affecting 2-5% of children aged 3 months to 5 years. The majority are simple febrile seizures (generally defined as generalized onset, single seizures with a duration of less than 30 minutes). Complex febrile seizures are characterized by focal onset, duration greater than 30 minutes, and/or more than one seizure in a 24 hour period. The likelihood of developing epilepsy following simple febrile seizures is low. Complex febrile seizures are associated with a moderately increased incidence of epilepsy. {ECO:0000269|PubMed:16924025}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Generalized epilepsy with febrile seizures plus 3 (GEFS+3) [MIM:611277]: A rare autosomal dominant, familial condition with incomplete penetrance and large intrafamilial variability. Patients display febrile seizures persisting sometimes beyond the age of 6 years and/or a variety of afebrile seizure types. This disease combines febrile seizures, generalized seizures often precipitated by fever at age 6 years or more, and partial seizures, with a variable degree of severity. {ECO:0000269|PubMed:11326274}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cerebellum cortex;hypothalamus;pineal body;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;adrenal gland;thyroid;macula lutea;hippocampus;visual apparatus;pituitary gland;head and neck;pineal gland;brain; subthalamic nucleus;occipital lobe;superior cervical ganglion;globus pallidus;parietal lobe; 0.19140 0.20783 -0.427900189 25.14744043 16.67966 0.58760 GABRG3 0.993679844208636 0.00631920485474683 9.50936617041e-07 gamma-aminobutyric acid type A receptor gamma3 subunit FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.; . . . . 0.08854 0.10206 -0.093566408 46.7386176 47.84861 1.34351 GABRG3-AS1 . . . GABRG3 antisense RNA 1 . . . . . . . . . . . GABRP 9.63031365626368e-06 0.783078633244096 0.216911736442248 gamma-aminobutyric acid type A receptor pi subunit FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. In the uterus, the function of the receptor appears to be related to tissue contractility. The binding of this pI subunit with other GABA(A) receptor subunits alters the sensitivity of recombinant receptors to modulatory agents such as pregnanolone.; . TISSUE SPECIFICITY: Most abundant in the uterus, also expressed in lung, thymus and prostate.; unclassifiable (Anatomical System);ovary;parathyroid;skeletal muscle;uterus;breast;pancreas;prostate;lung;endometrium;nasopharynx;placenta;testis;brain;mammary gland;tonsil;stomach; uterus;medulla oblongata;superior cervical ganglion;trachea;tongue;temporal lobe;appendix;trigeminal ganglion;skeletal muscle;tonsil; 0.12490 0.16969 0.266447942 70.5826846 2449.21042 9.20811 GABRQ 0.0100883396988473 0.979623196443375 0.010288463857778 gamma-aminobutyric acid type A receptor theta subunit FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.; . . brain; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12937 0.23004 -0.758599262 13.32861524 174.95873 2.87605 GABRR1 2.12253958201951e-07 0.687205420728094 0.312794367017948 gamma-aminobutyric acid type A receptor rho1 subunit FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Rho-1 GABA receptor could play a role in retinal neurotransmission.; . TISSUE SPECIFICITY: Highly expressed in the retina and in a lesser extent in brain, lung and thymus.; . . 0.16436 0.12099 0.020302773 55.60863411 2268.00024 8.80716 GABRR2 4.52031672010083e-07 0.382145797809108 0.61785375015922 gamma-aminobutyric acid type A receptor rho2 subunit FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Rho-2 GABA receptor could play a role in retinal neurotransmission.; . . . . 0.13732 0.13026 0.069852974 59.10592121 2213.04585 8.65953 GABRR3 . . . gamma-aminobutyric acid type A receptor rho3 subunit (gene/pseudogene) FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. {ECO:0000250}.; . . . . . . -0.023789244 52.09365416 . . GACAT1 . . . gastric cancer associated transcript 1 (non-protein coding) . . . . . . . . . . . GACAT2 . . . gastric cancer associated transcript 2 (non-protein coding) . . . . . . . . . . . GACAT3 . . . gastric cancer associated transcript 3 (non-protein coding) . . . . . . . . . . . GAD1 0.82254015260978 0.177452792547152 7.05484306804972e-06 glutamate decarboxylase 1 FUNCTION: Catalyzes the production of GABA.; . TISSUE SPECIFICITY: Isoform 3 is expressed in pancreatic islets, testis, adrenal cortex, and perhaps other endocrine tissues, but not in brain. {ECO:0000269|PubMed:10671565}.; ovary;colon;parathyroid;choroid;retina;frontal lobe;endometrium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);cerebellum cortex;hypothalamus;blood;lens;skeletal muscle;bile duct;lung;placenta;hippocampus;head and neck;kidney;mammary gland;cerebellum; whole brain;amygdala;superior cervical ganglion;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.96836 0.78686 -0.512444034 21.55579146 542.12172 4.74024 GAD2 0.898626707693029 0.101371703728611 1.58857836027205e-06 glutamate decarboxylase 2 FUNCTION: Catalyzes the production of GABA.; . . unclassifiable (Anatomical System);pancreas;lung;islets of Langerhans;hypothalamus;brain; dorsal root ganglion;amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;atrioventricular node;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.46051 0.86241 -0.111973265 45.35857514 169.77404 2.84260 GADD45A 0.109847669303976 0.776947753905408 0.113204576790615 growth arrest and DNA damage inducible alpha FUNCTION: In T-cells, functions as a regulator of p38 MAPKs by inhibiting p88 phosphorylation and activity (By similarity). Might affect PCNA interaction with some CDK (cell division protein kinase) complexes; stimulates DNA excision repair in vitro and inhibits entry of cells into S phase. {ECO:0000250}.; . . . . 0.63560 0.83799 -0.031067188 51.03798066 2.12736 0.07097 GADD45AP1 . . . growth arrest and DNA damage inducible alpha pseudogene 1 . . . . . . . . . . . GADD45B 0.185427441870799 0.763426871868814 0.0511456862603868 growth arrest and DNA damage inducible beta FUNCTION: Involved in the regulation of growth and apoptosis. Mediates activation of stress-responsive MTK1/MEKK4 MAPKKK.; . . choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;spinal cord;urinary;muscle;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;hippocampus;liver;mammary gland;stomach; superior cervical ganglion;olfactory bulb;appendix;ciliary ganglion;atrioventricular node;fetal thyroid;trigeminal ganglion;skeletal muscle; 0.43236 0.38305 -0.031067188 51.03798066 5224.38363 14.87867 GADD45G 0.72098224781391 0.265455096038499 0.0135626561475913 growth arrest and DNA damage inducible gamma FUNCTION: Involved in the regulation of growth and apoptosis. Mediates activation of stress-responsive MTK1/MEKK4 MAPKKK.; . . ovary;colon;parathyroid;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;lens;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;thymus; uterus corpus;prostate;placenta;testis; 0.40592 0.22108 0.21326276 67.71644256 71.39747 1.75880 GADD45GIP1 0.000318097001528209 0.583320009385633 0.416361893612839 GADD45G interacting protein 1 FUNCTION: Acts as a negative regulator of G1 to S cell cycle phase progression by inhibiting cyclin-dependent kinases. Inhibitory effects are additive with GADD45 proteins but occurs also in the absence of GADD45 proteins. Acts as a repressor of the orphan nuclear receptor NR4A1 by inhibiting AB domain-mediated transcriptional activity. May be involved in the hormone-mediated regulation of NR4A1 transcriptional activity. May play a role in mitochondrial protein synthesis.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in the thyroid gland, heart, lymph nodes, trachea and adrenal tissues. Expressed at lower level in liver skeletal muscle, kidney, pancreas, testis, ovary and stomach. Barely detectable in adrenal adenoma and papillary thyroid cancer. {ECO:0000269|PubMed:12716909}.; ovary;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);trophoblast;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; whole brain;thalamus;lung;heart;thyroid;prefrontal cortex;liver;tumor;caudate nucleus;cingulate cortex; 0.10172 . 0.547599505 81.2160887 150.86841 2.68401 GADL1 5.39098728033269e-09 0.120531248222808 0.879468746386205 glutamate decarboxylase like 1 FUNCTION: May catalyze the decarboxylation of aspartate, cysteine sulfinic acid, and cysteic acid to beta-alanine, hypotaurine and taurine, respectively. Does not exhibit any decarboxylation activity toward glutamate. {ECO:0000269|PubMed:23038267}.; . . . . 0.14446 0.12327 0.554869705 81.59943383 339.26926 3.90684 GAGE1 0.438832810615359 0.457171365809977 0.103995823574663 G antigen 1 FUNCTION: Antigen, recognized on melanoma by autologous cytolytic T-lymphocytes. Completely silent in normal adult tissues, except testis.; . TISSUE SPECIFICITY: Expressed in a variety of tumor tissues but not in normal tissues, except testis.; . . . . . . 134.89566 2.52545 GAGE2A . . . G antigen 2A . . . . . . . . . . . GAGE2B . . . G antigen 2B FUNCTION: Antigen, recognized on melanoma by autologous cytolytic T-lymphocytes.; . . . . . . . . 0.22223 0.00489 GAGE2C . . . G antigen 2C FUNCTION: Antigen, recognized on melanoma by autologous cytolytic T-lymphocytes.; . . . . . . . . . . GAGE2D 0.402977937434793 0.470781220641568 0.126240841923639 G antigen 2D . . TISSUE SPECIFICITY: Not expressed in normal tissues, except in testis, but expressed by a large proportion of tumors of various histological origins.; . . . . . . 839.43668 5.67458 GAGE2E . . . G antigen 2E . . . . . . . . . . . GAGE3 . . . G antigen 3 . . TISSUE SPECIFICITY: Expressed in a variety of tumor tissues but not in normal tissues, except testis.; . . . . . . . . GAGE4 . . . G antigen 4 . . TISSUE SPECIFICITY: Expressed in a variety of tumor tissues but not in normal tissues, except testis.; . . . . . . . . GAGE5 . . . G antigen 5 . . TISSUE SPECIFICITY: Expressed in a variety of tumor tissues but not in normal tissues, except testis.; . . . . . . . . GAGE6 . . . G antigen 6 . . TISSUE SPECIFICITY: Expressed in a variety of tumor tissues but not in normal tissues, except testis.; . . . . . . . . GAGE7 . . . G antigen 7 . . TISSUE SPECIFICITY: Expressed in some prostate cancer tissues but not in normal prostate tissue.; . . . . . . . . GAGE8 . . . G antigen 8 . . TISSUE SPECIFICITY: Not expressed in normal tissues, except in testis, but expressed by a large proportion of tumors of various histological origins.; . . . . . . . . GAGE10 0.00111994818700601 0.386509923659708 0.612370128153286 G antigen 10 . . . . . . . 0.191216164 66.57230479 2.20684 0.07390 GAGE12B . . . G antigen 12B . . . unclassifiable (Anatomical System);lung;liver;testis; . . . . . . . GAGE12C . . . G antigen 12C . . . . . . . . . . . GAGE12D . . . G antigen 12D . . . . . . . . . . . GAGE12E . . . G antigen 12E . . . . . . . . . . . GAGE12F . . . G antigen 12F . . . . . . . . . . . GAGE12G . . . G antigen 12G . . . . . . . . . . . GAGE12H . . . G antigen 12H . . . . . . . . . . . GAGE12I . . . G antigen 12I . . . . . . . . . . . GAGE12J 0.0235889056454509 0.543941999510255 0.432469094844294 G antigen 12J . . . . . . . . . 536.04533 4.72044 GAGE13 . . . G antigen 13 . . . . . . . . . . . GAK 0.973134951387495 0.0268650481503384 4.62166459332498e-10 cyclin G associated kinase FUNCTION: Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin- coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1. {ECO:0000269|PubMed:10625686}.; . TISSUE SPECIFICITY: Ubiquitous. Highest in testis.; lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;skeletal muscle;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach;cerebellum; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.22857 0.21456 -1.350697123 4.588346308 1354.12903 6.90678 GAL 0.000289003407059731 0.562450001282782 0.437260995310159 galanin/GMAP prepropeptide FUNCTION: Endocrine hormone of the central and peripheral nervous systems that binds and activates the G protein-coupled receptors GALR1, GALR2, and GALR3. This small neuropeptide may regulate diverse physiologic functions including contraction of smooth muscle of the gastrointestinal and genitourinary tract, growth hormone and insulin release and adrenal secretion. {ECO:0000269|PubMed:1370155, ECO:0000269|PubMed:1722333, ECO:0000269|PubMed:25691535}.; DISEASE: Epilepsy, familial temporal lobe, 8 (ETL8) [MIM:616461]: A focal form of epilepsy characterized by recurrent seizures that arise from foci within the temporal lobe. Seizures are usually accompanied by sensory symptoms, most often auditory in nature. {ECO:0000269|PubMed:25691535}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;blood;skin;bone marrow;pancreas;lung;liver;pituitary gland;spleen;cervix;stomach; superior cervical ganglion;ciliary ganglion;pituitary; 0.61129 0.42521 0.813985927 87.81552253 94.99581 2.10121 GAL3ST1 0.379107293050681 0.610275883533425 0.0106168234158936 galactose-3-O-sulfotransferase 1 FUNCTION: Catalyzes the sulfation of membrane glycolipids. Seems to prefer beta-glycosides at the non-reducing termini of sugar chains attached to a lipid moiety. Catalyzes the synthesis of galactosylceramide sulfate (sulfatide), a major lipid component of the myelin sheath and of monogalactosylalkylacylglycerol sulfate (seminolipid), present in spermatocytes (By similarity). Also acts on lactosylceramide, galactosyl 1-alkyl-2-sn-glycerol and galactosyl diacylglycerol (in vitro). {ECO:0000250, ECO:0000269|PubMed:8830034}.; . TISSUE SPECIFICITY: Expressed in kidney proximal tubule, gastric mucosa and adenocarcinoma. Highly expressed in renal cell carcinoma cell lines.; unclassifiable (Anatomical System);lung;whole body;frontal lobe;liver;testis;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;olfactory bulb;hypothalamus;spinal cord;kidney;trigeminal ganglion;skeletal muscle; 0.22863 0.18171 0.688969636 85.20877565 2447.68495 9.20257 GAL3ST2 4.41529604975779e-05 0.406053404025812 0.59390244301369 galactose-3-O-sulfotransferase 2 FUNCTION: Transfers a sulfate group to the hydroxyl group at C3 of non-reducing beta-galactosyl residues. Acts both on type 1 (Gal- beta-1,3-GlcNAc) and type 2 (Gal-beta-1,4-GlcNAc) chains with similar efficiency.; . TISSUE SPECIFICITY: Ubiquitous. Detected in heart, stomach, colon, liver and spleen, in epithelial cells lining the lower to middle layer of the crypts in colonic mucosa, hepatocytes surrounding the central vein of the liver, extravillous cytotrophoblasts in the basal plate of the septum of the placenta, renal tubules of the kidney, and neuronal cells of the cerebral cortex. {ECO:0000269|PubMed:11029462}.; optic nerve;lung;macula lutea;fovea centralis;choroid;lens;brain;retina; dorsal root ganglion;superior cervical ganglion; 0.06361 0.10897 . . 866.72212 5.73404 GAL3ST3 1.24668822518249e-06 0.112679869257986 0.887318884053789 galactose-3-O-sulfotransferase 3 FUNCTION: Transfers a sulfate to position 3 of non-reducing beta- galactosyl residues in N-glycans and core2-branched O-glycans. Has high activity towards Gal-beta-1,4-GlcNAc, Gal-beta-1,4(Fuc-alpha- 1,3)GlcNAc and lower activity towards Gal-beta-1,3(Fuc-alpha- 1,4)GlcNAc. {ECO:0000269|PubMed:11323440, ECO:0000269|PubMed:11356829}.; . TISSUE SPECIFICITY: Highly expressed in thyroid, brain, kidney, heart and spinal cord. {ECO:0000269|PubMed:11323440, ECO:0000269|PubMed:11356829}.; unclassifiable (Anatomical System);medulla oblongata;optic nerve;lung;macula lutea;hippocampus;testis;fovea centralis;choroid;kidney;lens;brain;retina; amygdala;dorsal root ganglion;superior cervical ganglion;pons;cerebellum; 0.15643 0.11032 . . 1051.62866 6.22659 GAL3ST4 3.81535057360793e-10 0.0950565365087819 0.904943463109683 galactose-3-O-sulfotransferase 4 FUNCTION: Catalyzes the transfer of sulfate to beta-1,3-linked galactose residues in O-linked glycoproteins. Good substrates include asialofetuin, Gal-beta-1,3-GalNAc and Gal-beta-1,3 (GlcNAc-beta-1,6)GalNAc. {ECO:0000269|PubMed:11333265}.; . TISSUE SPECIFICITY: Expressed mainly in placenta, thymus, testis, ovary, spinal cord, trachea and adrenal gland and at low levels in brain, lung, spleen, prostate, small intestine, colon, stomach thyroid and lymph node. {ECO:0000269|PubMed:11333265}.; unclassifiable (Anatomical System);cartilage;tongue;skeletal muscle;skin;placenta;thyroid;bone;hippocampus;visual apparatus;spinal ganglion;mammary gland;brain;stomach; superior cervical ganglion;trigeminal ganglion; 0.10060 0.09344 1.067416815 91.66666667 270.62468 3.52805 GALC 6.28347214969704e-07 0.993385120505396 0.00661425114738869 galactosylceramidase FUNCTION: Hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon. {ECO:0000269|PubMed:8281145, ECO:0000269|PubMed:8399327}.; DISEASE: Leukodystrophy, globoid cell (GLD) [MIM:245200]: An autosomal recessive disorder characterized by insufficient catabolism of several galactolipids that are important for normal myelin production. Four clinical forms are recognized. The infantile form accounts for 90% of cases. It manifests before six months of age with irritability, spasticity, arrest of motor and mental development, and bouts of temperature elevation without infection. This is followed by myoclonic jerks of arms and legs, oposthotonus, hypertonic fits, and mental regression, which progresses to a severe decerebrate condition with no voluntary movements and death from respiratory infections or cerebral hyperpyrexia before 2 years of age. Cases with later onset present with unexplained blindness, weakness and sensorimotor peripheral neuropathy, mental deterioration and death. {ECO:0000269|PubMed:10234611, ECO:0000269|PubMed:10477434, ECO:0000269|PubMed:17579360, ECO:0000269|PubMed:20886637, ECO:0000269|PubMed:23462331, ECO:0000269|PubMed:8595408, ECO:0000269|PubMed:8786069, ECO:0000269|PubMed:8940268, ECO:0000269|PubMed:9272171}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in urine. Detected in testis, brain and placenta (at protein level). Detected in kidney and liver. {ECO:0000269|PubMed:8399327}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;pituitary gland;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;amnion;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;olfactory bulb;hypothalamus;spinal cord;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.06866 0.44905 0.846940207 88.47605567 6435.96683 16.82798 GALE 3.26698555553297e-08 0.17612576433918 0.823874202990964 UDP-galactose-4-epimerase FUNCTION: Catalyzes two distinct but analogous reactions: the reversible epimerization of UDP-glucose to UDP-galactose and the reversible epimerization of UDP-N-acetylglucosamine to UDP-N- acetylgalactosamine. The reaction with UDP-Gal plays a critical role in the Leloir pathway of galactose catabolism in which galactose is converted to the glycolytic intermediate glucose 6- phosphate. It contributes to the catabolism of dietary galactose and enables the endogenous biosynthesis of both UDP-Gal and UDP- GalNAc when exogenous sources are limited. Both UDP-sugar interconversions are important in the synthesis of glycoproteins and glycolipids. {ECO:0000269|PubMed:22654673, ECO:0000303|PubMed:23732289}.; DISEASE: Epimerase-deficiency galactosemia (EDG) [MIM:230350]: Clinical features include early-onset cataracts, liver damage, deafness and mental retardation. There are two clinically distinct forms of EDG. (1) A benign, or 'peripheral' form with no detectable GALE activity in red blood cells and characterized by mild symptoms. Some patients may suffer no symptoms beyond raised levels of galactose-1-phosphate in the blood. (2) A much rarer 'generalized' form with undetectable levels of GALE activity in all tissues and resulting in severe features such as restricted growth and mental development. {ECO:0000269|PubMed:11903335, ECO:0000269|PubMed:16301867, ECO:0000269|PubMed:9326324, ECO:0000269|PubMed:9538513, ECO:0000269|PubMed:9973283}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.43492 0.56947 -0.556537043 19.72753008 97.5207 2.13484 GALK1 0.000940520588108951 0.806045460475044 0.193014018936847 galactokinase 1 FUNCTION: Major enzyme for galactose metabolism.; DISEASE: Galactosemia II (GALCT2) [MIM:230200]: Autosomal recessive deficiency characterized by congenital cataracts during infancy and presenile cataracts in the adult population. The cataracts are secondary to accumulation of galactitol in the lenses. {ECO:0000269|PubMed:10521295, ECO:0000269|PubMed:10790206, ECO:0000269|PubMed:11139256, ECO:0000269|PubMed:11231902, ECO:0000269|PubMed:15024738}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;liver;skeletal muscle; 0.08075 . -0.844966979 11.1759849 72.99527 1.78318 GALK2 8.74120031890395e-06 0.924426155559252 0.0755651032404287 galactokinase 2 FUNCTION: Acts on GalNAc. Also acts as a galactokinase when galactose is present at high concentrations. May be involved in a salvage pathway for the reutilization of free GalNAc derived from the degradation of complex carbohydrates. {ECO:0000269|PubMed:16006554}.; . . medulla oblongata;ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; appendix;skeletal muscle; 0.20809 0.14099 -0.179930907 40.35739561 96.73851 2.12614 GALM 8.92598000417204e-09 0.0855581708228325 0.914441820251187 galactose mutarotase (aldose 1-epimerase) FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose (By similarity). {ECO:0000250, ECO:0000269|PubMed:12753898, ECO:0000269|PubMed:15026423}.; . . colon;parathyroid;skin;uterus;prostate;endometrium;thyroid;bone;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14669 0.18874 -0.069700724 48.54328851 1754.52673 7.72942 GALNS 0.000862039524473656 0.984558724590707 0.0145792358848191 galactosamine (N-acetyl)-6-sulfatase . DISEASE: Mucopolysaccharidosis 4A (MPS4A) [MIM:253000]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. {ECO:0000269|PubMed:1522213, ECO:0000269|PubMed:16287098, ECO:0000269|PubMed:24726177, ECO:0000269|PubMed:7581409, ECO:0000269|PubMed:7633425, ECO:0000269|PubMed:7668283, ECO:0000269|PubMed:7795586, ECO:0000269|PubMed:8651279, ECO:0000269|PubMed:8826435, ECO:0000269|PubMed:9298823, ECO:0000269|PubMed:9375852, ECO:0000269|PubMed:9521421}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;blood;lens;breast;pancreas;lung;mesenchyma;placenta;macula lutea;hippocampus;alveolus;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;trigeminal ganglion; 0.12338 . 0.472145421 78.85114414 1713.43108 7.63179 GALNT1 0.742968960381217 0.25701091256501 2.01270537728159e-05 polypeptide N-acetylgalactosaminyltransferase 1 FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. {ECO:0000269|PubMed:9295285}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in all tissues tested. {ECO:0000269|PubMed:7592619}.; lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;pineal body;urinary;pharynx;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;oral cavity;pancreas;pia mater;lung;cornea;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;skin;cingulate cortex; 0.45435 0.11809 -0.405853867 26.23260203 29.49125 0.94237 GALNT2 0.881985612838068 0.118013909015926 4.78146005764041e-07 polypeptide N-acetylgalactosaminyltransferase 2 FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. {ECO:0000269|PubMed:12438318, ECO:0000269|PubMed:16434399, ECO:0000269|PubMed:7592619, ECO:0000269|PubMed:9295285}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:7592619}.; . . 0.22673 0.13430 -0.556537043 19.72753008 893.81757 5.82734 GALNT3 2.0116310885668e-05 0.974044470882333 0.0259354128067815 polypeptide N-acetylgalactosaminyltransferase 3 FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Probably glycosylates fibronectin in vivo. Glycosylates FGF23. Plays a central role in phosphate homeostasis. {ECO:0000269|PubMed:16638743, ECO:0000269|PubMed:9295285}.; DISEASE: Tumoral calcinosis, hyperphosphatemic, familial (HFTC) [MIM:211900]: A severe metabolic disorder that manifests with hyperphosphatemia and massive calcium deposits in the skin and subcutaneous tissues. Some patients manifest recurrent, transient, painful swellings of the long bones associated with the radiographic findings of periosteal reaction and cortical hyperostosis and absence of skin involvement. {ECO:0000269|PubMed:15133511, ECO:0000269|PubMed:15599692}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in organs that contain secretory epithelial glands. Highly expressed in pancreas, skin, kidney and testis. Weakly expressed in prostate, ovary, intestine and colon. Also expressed in placenta and lung and fetal lung and fetal kidney. {ECO:0000269|PubMed:12708471, ECO:0000269|PubMed:8663203}.; . . 0.22774 . -0.376526807 28.10804435 206.5604 3.10594 GALNT4 0.112929757253281 0.881019997364159 0.00605024538255948 polypeptide N-acetylgalactosaminyltransferase 4 FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of SELPLG.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in mucous cells. {ECO:0000269|PubMed:9804815}.; . . . . 0.42259095 77.22929936 1883.07913 7.98145 GALNT5 1.33613590422636e-12 0.167789717002705 0.832210282995959 polypeptide N-acetylgalactosaminyltransferase 5 FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;cartilage;colon;parathyroid;skin;bile duct;uterus;lung;bone;liver;spleen;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.40721 0.07992 -0.326979057 30.90351498 1982.32949 8.20767 GALNT6 1.65843390047223e-06 0.962839716321056 0.037158625245044 polypeptide N-acetylgalactosaminyltransferase 6 FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. May participate in synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2, EA2 and fibronectin peptides.; . TISSUE SPECIFICITY: Expressed in placenta and trachea. Weakly expressed in brain and pancreas. Expressed in fibroblast. Weakly or not expressed in lung, liver, muscle, kidney, spleen, thymus, prostate, testis, ovary, intestine, colon, leukocyte, stomach, thyroid, spinal cord, lymph node, trachea, adrenal gland and bone marrow. {ECO:0000269|PubMed:10464263}.; unclassifiable (Anatomical System);amygdala;uterus;lung;liver;colon;spleen;germinal center;mammary gland;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;trachea;pons;trigeminal ganglion;skeletal muscle; 0.12421 0.10440 -0.551080959 19.93394669 380.61274 4.11197 GALNT7 0.000181549323194455 0.998647807602936 0.00117064307386909 polypeptide N-acetylgalactosaminyltransferase 7 FUNCTION: Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.; . TISSUE SPECIFICITY: Widely expressed. Expressed in uterus, retina, kidney, small intestine, omentum, stomach and CNS. {ECO:0000269|PubMed:10544240}.; ovary;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;oesophagus;larynx;bone;thyroid;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;heart;small intestine;islets of Langerhans;blood;skeletal muscle;breast;greater omentum;pancreas;lung;trabecular meshwork;placenta;alveolus;liver;cervix;head and neck;kidney;aorta;stomach;cerebellum;thymus; trachea;spinal cord; 0.24197 0.10967 0.442818085 77.8544468 113.12755 2.31496 GALNT8 1.87452420046286e-10 0.218590446354465 0.781409553458083 polypeptide N-acetylgalactosaminyltransferase 8 FUNCTION: Probably catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in heart, skeletal muscle, kidney, liver, small intestine and placenta. Weakly expressed in colon, thymus, spleen, lung and leukocyte. {ECO:0000269|PubMed:10767557}.; unclassifiable (Anatomical System);lacrimal gland; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05047 0.07267 1.625941868 96.04269875 1254.16781 6.67972 GALNT9 0.594228592829193 0.396165056549276 0.00960635062153087 polypeptide N-acetylgalactosaminyltransferase 9 FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Does not glycosylate apomucin or SDC3.; . TISSUE SPECIFICITY: Specifically expressed in brain. Not expressed in heart, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocyte. In brain, it is expressed in cerebellum, frontal lobe, temporal lobe, putamen and spinal cord, weakly expressed in cerebral cortex. Not expressed in medulla and occipital pole. {ECO:0000269|PubMed:10978536}.; unclassifiable (Anatomical System);prostate;optic nerve;lung;bone;hippocampus;testis;kidney;brain; ciliary ganglion;atrioventricular node; . 0.10575 -0.66859065 15.76433121 356.88776 4.00122 GALNT10 0.000449260379215831 0.99797813373219 0.00157260588859393 polypeptide N-acetylgalactosaminyltransferase 10 FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward Muc5Ac and EA2 peptide substrates.; . TISSUE SPECIFICITY: Widely expressed. Expressed at high level in small intestine, and at intermediate levels in stomach, pancreas, ovary, thyroid gland and spleen. Weakly expressed in other tissues. {ECO:0000269|PubMed:12417297}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;thyroid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;thyroid; 0.65879 0.11161 -1.197736472 5.785562633 85.35691 1.96853 GALNT11 0.00404741904705645 0.995623522889047 0.000329058063896239 polypeptide N-acetylgalactosaminyltransferase 11 FUNCTION: Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N- acetylgalactosaminyltransferases catalyze the transfer of an N- acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward MUC1, MUC4, and EA2 than GALNT1. Not involved in glycosylation of erythropoietin (EPO). {ECO:0000269|PubMed:11925450, ECO:0000269|PubMed:24226769}.; DISEASE: Note=Defects in GALNT11 may be a cause of heterotaxy, a congenital heart disease resulting from abnormalities in left- right (LR) body patterning. {ECO:0000269|PubMed:21282601}.; TISSUE SPECIFICITY: Highly expressed in kidney. Expressed at intermediate level in brain, heart and skeletal muscle. Weakly expressed other tissues. In kidney, it is strongly expressed in tubules but not expressed in glomeruli. {ECO:0000269|PubMed:11925450}.; myocardium;ovary;salivary gland;intestine;colon;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;synovium;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;cerebellum cortex;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;kidney;stomach;thymus; kidney; 0.13704 0.10054 -0.43902969 24.63434772 485.66524 4.53862 GALNT12 0.0028256589510292 0.984087514632742 0.0130868264162289 polypeptide N-acetylgalactosaminyltransferase 12 FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with Muc2 and Muc7. Displays enzymatic activity toward the Gal-NAc- Muc5AC glycopeptide, but no detectable activity to mono-GalNAc- glycosylated Muc1a, Muc2, Muc7 and EA2. May play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs.; DISEASE: Colorectal cancer 1 (CRCS1) [MIM:608812]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:19617566, ECO:0000269|PubMed:22461326, ECO:0000269|PubMed:24115450}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. The role of GALNT12 in colon cancer susceptibility is however subject to discussion: studies on 103 probants with colorectal cancer 1 (CRCS1) suggest that it does not act as a major contributor of CRCS1 (PubMed:24115450). {ECO:0000269|PubMed:24115450}.; TISSUE SPECIFICITY: Widely expressed at different levels of expression. Highly expressed in digestive organs such as small intestine, stomach, pancreas and colon. Expressed at intermediate level in testis, thyroid gland and spleen. Weakly expressed in whole brain, cerebral cortex, cerebellum, fetal brain, bone marrow, thymus, leukocytes, heart, skeletal muscle, liver, lung, esophagus, kidney, adrenal gland, mammary gland, uterus, placenta, ovary and prostate. {ECO:0000269|PubMed:12135769}.; . . 0.53016 0.10373 -0.732911333 14.07761264 529.70382 4.69680 GALNT13 0.853952804016347 0.146026645090227 2.05508934263512e-05 polypeptide N-acetylgalactosaminyltransferase 13 FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. Able to glycosylate SDC3. May be responsible for the synthesis of Tn antigen in neuronal cells.; . TISSUE SPECIFICITY: Specifically expressed in neuronal cells. Expressed in fetal brain, whole adult brain, cerebral cortex and cerebellum. Not expressed in other tissues tested. {ECO:0000269|PubMed:12407114}.; . . 0.31847 0.07912 -0.181750739 40.15687662 77.7295 1.85780 GALNT14 3.03253774344532e-09 0.729560652226631 0.270439344740831 polypeptide N-acetylgalactosaminyltransferase 14 FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). May be involved in O-glycosylation in kidney.; . TISSUE SPECIFICITY: Detected in renal tubules (at protein level). Highly expressed in fetal and adult kidney. Widely expressed at low level. Weakly expressed in whole brain, cerebellum, thymus, lung, mammary gland, liver, stomach, small intestine, colon, pancreas, spleen, bladder, uterus, placenta, testis, ovary, skeletal muscle, leukocyte, B-cell, bone marrow, fetal brain, fetal thymus, fetal lung, fetal liver, fetal small intestine, fetal spleen, fetal skeletal and fetus. Detected in renal tubules (at protein level). {ECO:0000269|PubMed:12507512, ECO:0000269|PubMed:20179215}.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;urinary;adrenal cortex;lens;pancreas;lung;placenta;macula lutea;hippocampus;visual apparatus;liver;spleen;kidney; superior cervical ganglion;thalamus;ciliary ganglion;kidney; 0.06647 0.09129 -0.21856543 37.66218448 2206.0062 8.64813 GALNT15 5.51634648613177e-10 0.376453241356124 0.623546758092241 polypeptide N-acetylgalactosaminyltransferase 15 FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, it is able to transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. Prefers Muc1a as substrate.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in small intestine, placenta, spleen, cerebral cortex and ovary. Expressed at intermediate level in uterus, mammary gland, stomach, cerebellum and whole brain. Weakly expressed in fetal brain, bone marrow, thyroid gland, thymus, heart, skeletal muscle, lung, liver, colon, pancreas, kidney and testis. Not expressed in leukocyte. Expressed in both normal and osteoarthritic cartilage. Expressed at low level in chondrocytes in all zones of both normal and osteoarthritic cartilage. {ECO:0000269|PubMed:11597177, ECO:0000269|PubMed:15147861}.; . . 0.30314 0.09703 -0.661316159 16.02382637 2902.69931 10.21345 GALNT16 0.0168277172834296 0.982968536076429 0.00020374664014144 polypeptide N-acetylgalactosaminyltransferase 16 FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. {ECO:0000269|PubMed:22186971}.; . . . . 0.53484 0.10872 -0.50880549 21.72682236 1976.95492 8.19007 GALNT18 0.0476851755722948 0.95128505587176 0.00102976855594484 polypeptide N-acetylgalactosaminyltransferase 18 FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. {ECO:0000269|PubMed:22186971}.; . . . . 0.20546 0.09952 -0.775187015 13.05142722 69.4345 1.72927 GALNTL5 6.05278672454337e-13 0.0157521987160198 0.984247801283375 polypeptide N-acetylgalactosaminyltransferase-like 5 FUNCTION: Probable inactive glycosyltransferase required during spermatid development. May participate to protein loading into the acrosomes and accumulation of ubiquitin-proteasome systems around the head-tail coupling apparatus region.; DISEASE: Note=Defects in GALNTL5 have been found in a patient with primary infertility due to asthenozoospermia. {ECO:0000269|PubMed:24398516}.; TISSUE SPECIFICITY: Mainly expressed in testis. Weakly or not expressed in other tissues. {ECO:0000269|PubMed:24398516}.; . . 0.03378 0.07001 1.420201535 94.92215145 2517.22991 9.35681 GALNTL6 0.00165568126276253 0.997152290706873 0.00119202803036428 polypeptide N-acetylgalactosaminyltransferase-like 6 FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. {ECO:0000250}.; . . . . . 0.10877 -0.824740496 11.67728238 48.92451 1.36627 GALP 0.00121511522532655 0.632691224573629 0.366093660201044 galanin like peptide FUNCTION: Isoform 1: Hypothalamic neuropeptide which binds to the G-protein-coupled galanin receptors (GALR1, GALR2 and GALR3). Involved in a large number of putative physiological functions in CNS homeostatic processes, including the regulation of gonadotropin-releasing hormone secretion.; . TISSUE SPECIFICITY: Isoform 2 is found in ganglia of ganglioneuroma and ganglioneuroblastoma, as well as in differentiated tumor cells of neuroblastoma tissues. Not found in undifferentiated neuroblasts. Isoform 2 is found in the skin, in pericytes covering microvascular arterioles and venules on their abluminal surfaces. In larger vessels, isoform 2 is expressed in layers of smooth muscle cells. Isoform 2 is not detected in endothelial cells.; unclassifiable (Anatomical System); subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;parietal lobe;skeletal muscle; 0.19910 0.15102 0.481458261 79.03986789 1796.64496 7.81987 GALR1 0.000193369133207075 0.477441936387544 0.522364694479249 galanin receptor 1 FUNCTION: Receptor for the hormone galanin. The activity of this receptor is mediated by G proteins that inhibit adenylate cyclase activity. {ECO:0000269|PubMed:25691535, ECO:0000269|PubMed:7524088}.; . . unclassifiable (Anatomical System);sympathetic chain; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.09235 0.18135 0.262810045 70.43524416 421.27663 4.28478 GALR2 0.00797093656746506 0.785946320209039 0.206082743223496 galanin receptor 2 FUNCTION: Receptor for the hormone galanin and GALP. Receptor for the hormone spexin-1 (PubMed:24517231). The activity of this receptor is mediated by G proteins that activate the phospholipase C/protein kinase C pathway (via G(q)) and that inhibit adenylyl cyclase (via G(i)). {ECO:0000269|PubMed:24517231, ECO:0000269|PubMed:25691535, ECO:0000269|PubMed:9480833, ECO:0000269|PubMed:9685625, ECO:0000269|PubMed:9832121, ECO:0000269|PubMed:9880084}.; . TISSUE SPECIFICITY: Expressed abundantly within the central nervous system in both hypothalamus and hippocampus. In peripheral tissues, the strongest expression was observed in heart, kidney, liver, and small intestine.; unclassifiable (Anatomical System);bone; . 0.13007 0.15927 1.172206761 92.69874971 381.76733 4.11884 GALR3 0.0231534228966913 0.768362369723608 0.208484207379701 galanin receptor 3 FUNCTION: Receptor for the hormone galanin (PubMed:25691535). Receptor for the hormone spexin-1 (PubMed:24517231). {ECO:0000269|PubMed:24517231, ECO:0000269|PubMed:25691535, ECO:0000269|PubMed:9722565, ECO:0000269|PubMed:9832121}.; . . unclassifiable (Anatomical System);optic nerve;ovary;macula lutea;fovea centralis;choroid;lens;retina; dorsal root ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.58078 0.13785 . . 221.3043 3.21815 GALT 0.00119073949704641 0.989527544138032 0.00928171636492168 galactose-1-phosphate uridylyltransferase . DISEASE: Galactosemia (GALCT) [MIM:230400]: Inherited disorder of galactose metabolism that causes jaundice, cataracts, and mental retardation. {ECO:0000269|PubMed:10220154, ECO:0000269|PubMed:11754113, ECO:0000269|PubMed:11919338, ECO:0000269|PubMed:1373122, ECO:0000269|PubMed:1427861, ECO:0000269|PubMed:15841485, ECO:0000269|PubMed:1610789, ECO:0000269|PubMed:17041746, ECO:0000269|PubMed:17876724, ECO:0000269|PubMed:18956253, ECO:0000269|PubMed:1897530, ECO:0000269|PubMed:2011574, ECO:0000269|PubMed:22461411, ECO:0000269|PubMed:23022339, ECO:0000269|PubMed:25592817, ECO:0000269|PubMed:25614870, ECO:0000269|PubMed:7550229, ECO:0000269|PubMed:7887416, ECO:0000269|PubMed:7887417, ECO:0000269|PubMed:8499924, ECO:0000269|PubMed:8598637, ECO:0000269|PubMed:8741038, ECO:0000269|PubMed:8869397, ECO:0000269|PubMed:8956044, ECO:0000269|PubMed:9222760}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.10313 0.09557 -0.135838822 43.77211607 526.58141 4.68372 GAMT 2.64994350917261e-05 0.31806907016621 0.681904430398698 guanidinoacetate N-methyltransferase . . TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:8651275}.; lymphoreticular;ovary;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; liver;skeletal muscle; 0.09690 0.18907 -0.093566408 46.7386176 61.87248 1.60348 GAMTP1 . . . guanidinoacetate N-methyltransferase pseudogene 1 . . . . . . . . . . . GAMTP2 . . . guanidinoacetate N-methyltransferase pseudogene 2 . . . . . . . . . . . GAN 0.036349933633412 0.963332817870557 0.000317248496030672 gigaxonin FUNCTION: Probable cytoskeletal component that directly or indirectly plays an important role in neurofilament architecture. May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Controls degradation of TBCB. Controls degradation of MAP1B and MAP1S, and is critical for neuronal maintenance and survival. {ECO:0000269|PubMed:12147674, ECO:0000269|PubMed:15983046, ECO:0000269|PubMed:16227972, ECO:0000269|PubMed:16303566}.; DISEASE: Giant axonal neuropathy 1, autosomal recessive (GAN1) [MIM:256850]: A severe autosomal recessive sensorimotor neuropathy affecting both the peripheral nerves and the central nervous system. Axonal loss and the presence of giant axonal swellings filled with neurofilaments on nerve biopsies are the hallmarks of this neurodegenerative disorder. {ECO:0000269|PubMed:11062483, ECO:0000269|PubMed:11971098, ECO:0000269|PubMed:12655563, ECO:0000269|PubMed:17578852, ECO:0000269|PubMed:17587580}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, heart and muscle. {ECO:0000269|PubMed:12147674}.; unclassifiable (Anatomical System);breast;prostate;lung;trabecular meshwork;placenta;urinary;iris;colon;kidney;skeletal muscle; skin; 0.24569 0.28104 -0.598810865 18.13517339 50.51575 1.39863 GANAB 0.99994841038629 5.15896137070492e-05 2.62078899026907e-15 glucosidase II alpha subunit FUNCTION: Cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins. {ECO:0000269|PubMed:10929008}.; . TISSUE SPECIFICITY: Detected in placenta. {ECO:0000269|PubMed:3881423}.; myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;pineal body;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; adrenal gland;placenta;kidney;trigeminal ganglion; 0.37415 0.22864 -0.661316159 16.02382637 409.59625 4.24270 GANC 2.37915434464825e-21 0.0121935437207295 0.987806456279271 glucosidase, alpha; neutral C FUNCTION: Has alpha-glucosidase activity. {ECO:0000269|PubMed:12370436}.; . . ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;cochlea;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach;cerebellum; . 0.08474 0.73647 0.389427191 75.7136117 5154.47458 14.75083 GAP43 0.0123799221019638 0.64860165936902 0.339018418529016 growth associated protein 43 FUNCTION: This protein is associated with nerve growth. It is a major component of the motile "growth cones" that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction. {ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:21152083}.; . . ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;prostate;whole body;frontal lobe;bone;iris;testis;brain;artery;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;hypothalamus;pharynx;blood;breast;lung;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;aorta;cerebellum; amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.53571 0.35432 -0.449946534 24.00330267 30.11581 0.96061 GAPDH 0.180460004147139 0.807213729067538 0.0123262667853223 glyceraldehyde-3-phosphate dehydrogenase FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D- glyceroyl phosphate. Component of the GAIT (gamma interferon- activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. {ECO:0000250, ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:3170585}.; . . ovary;salivary gland;sympathetic chain;developmental;colon;skin;retina;bone marrow;uterus;prostate;pituitary gland;testis;brain;artery;unclassifiable (Anatomical System);lymph node;trophoblast;heart;islets of Langerhans;hypothalamus;bile duct;lung;placenta;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve;cerebellum; subthalamic nucleus;thalamus;medulla oblongata;smooth muscle;heart;tongue;temporal lobe;globus pallidus;pons;cingulate cortex;parietal lobe;skeletal muscle; . 0.99142 -0.404032746 26.53338051 25.5685 0.83367 GAPDHP1 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 1 . . . . . . . . . . . GAPDHP2 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 2 . . . . . . . . . . . GAPDHP14 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 14 . . . . . . . . . . . GAPDHP15 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 15 . . . . . . . . . . . GAPDHP16 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 16 . . . . . . . . . . . GAPDHP17 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 17 . . . . . . . . . . . GAPDHP19 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 19 . . . . . . . . . . . GAPDHP20 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 20 . . . . . . . . . . . GAPDHP21 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 21 . . . . . . . . . . . GAPDHP22 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 22 . . . . . . . . . . . GAPDHP23 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 23 . . . . . . . . . . . GAPDHP24 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 24 . . . . . . . . . . . GAPDHP25 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 25 . . . . . . . . . . . GAPDHP26 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 26 . . . . . . . . . . . GAPDHP27 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 27 . . . . . . . . . . . GAPDHP28 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 28 . . . . . . . . . . . GAPDHP29 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 29 . . . . . . . . . . . GAPDHP30 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 30 . . . . . . . . . . . GAPDHP31 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 31 . . . . . . . . . . . GAPDHP32 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 32 . . . . . . . . . . . GAPDHP33 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 33 . . . . . . . . . . . GAPDHP34 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 34 . . . . . . . . . . . GAPDHP35 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 35 . . . . . . . . . . . GAPDHP36 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 36 . . . . . . . . . . . GAPDHP37 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 37 . . . . . . . . . . . GAPDHP38 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 38 . . . . . . . . . . . GAPDHP39 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 39 . . . . . . . . . . . GAPDHP40 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 40 . . . . . . . . . . . GAPDHP41 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 41 . . . . . . . . . . . GAPDHP42 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 42 . . . . . . . . . . . GAPDHP43 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 43 . . . . . . . . . . . GAPDHP44 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 44 . . . . . . . . . . . GAPDHP45 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 45 . . . . . . . . . . . GAPDHP46 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 46 . . . . . . . . . . . GAPDHP47 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 47 . . . . . . . . . . . GAPDHP48 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 48 . . . . . . . . . . . GAPDHP49 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 49 . . . . . . . . . . . GAPDHP50 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 50 . . . . . . . . . . . GAPDHP51 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 51 . . . . . . . . . . . GAPDHP52 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 52 . . . . . . . . . . . GAPDHP53 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 53 . . . . . . . . . . . GAPDHP54 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 54 . . . . . . . . . . . GAPDHP55 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 55 . . . . . . . . . . . GAPDHP56 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 56 . . . . . . . . . . . GAPDHP57 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 57 . . . . . . . . . . . GAPDHP58 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 58 . . . . . . . . . . . GAPDHP59 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 59 . . . . . . . . . . . GAPDHP60 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 60 . . . . . . . . . . . GAPDHP61 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 61 . . . . . . . . . . . GAPDHP62 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 62 . . . . . . . . . . . GAPDHP63 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 63 . . . . . . . . . . . GAPDHP64 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 64 . . . . . . . . . . . GAPDHP65 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 65 . . . . . . . . . . . GAPDHP66 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 66 . . . . . . . . . . . GAPDHP67 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 67 . . . . . . . . . . . GAPDHP68 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 68 . . . . . . . . . . . GAPDHP69 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 69 . . . . . . . . . . . GAPDHP70 . . . glyceraldehyde 3 phosphate dehydrogenase pseudogene 70 . . . . . . . . . . . GAPDHP71 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 71 . . . . . . . . . . . GAPDHP72 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 72 . . . . . . . . . . . GAPDHP73 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 73 . . . . . . . . . . . GAPDHP74 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 74 . . . . . . . . . . . GAPDHP75 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 75 . . . . . . . . . . . GAPDHP76 . . . glyceraldehyde-3-phosphate dehydrogenase pseudogene 76 . . . . . . . . . . . GAPDHS 0.135772125697306 0.863333453326509 0.000894420976185317 glyceraldehyde-3-phosphate dehydrogenase, spermatogenic FUNCTION: May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis specific.; unclassifiable (Anatomical System);medulla oblongata;thyroid;testis;choroid;ciliary body;skin; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node; 0.07551 0.27102 -0.134019284 43.90776126 154.41391 2.71585 GAPLINC . . . gastric adenocarcinoma associated, positive CD44 regulator, long intergenic non-coding RNA . . . . . . . . . . . GAPT 0.00163093337057768 0.458169082331663 0.540199984297759 GRB2-binding adaptor protein, transmembrane FUNCTION: Negatively regulates B-cell proliferation following stimulation through the B-cell receptor. May play an important role in maintenance of marginal zone (MZ) B-cells (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in spleen and PBL, detected at lower levels in thymus, and undetectable in all other tissues tested. Also expressed in various B-cell lines, monocytic cell line THP-1 and NK-like cell line YT, but not in T-cell line Jurkat or HeLa cells. {ECO:0000269|PubMed:18559951}.; unclassifiable (Anatomical System);lymphoreticular;prostate;lung;cartilage;nasopharynx;testis;germinal center;brain;bone marrow; . 0.00638 0.03086 0.193034296 66.82000472 11.63344 0.42199 GAPVD1 0.999999871594819 1.28405180617197e-07 1.43640532770659e-19 GTPase activating protein and VPS9 domains 1 FUNCTION: Acts both as a GTPase-activating protein (GAP) and a guanine nucleotide exchange factor (GEF), and participates in various processes such as endocytosis, insulin receptor internalization or LC2A4/GLUT4 trafficking. Acts as a GEF for the Ras-related protein RAB31 by exchanging bound GDP for free GTP, leading to regulate LC2A4/GLUT4 trafficking. In the absence of insulin, it maintains RAB31 in an active state and promotes a futile cycle between LC2A4/GLUT4 storage vesicles and early endosomes, retaining LC2A4/GLUT4 inside the cells. Upon insulin stimulation, it is translocated to the plasma membrane, releasing LC2A4/GLUT4 from intracellular storage vesicles. Also involved in EGFR trafficking and degradation, possibly by promoting EGFR ubiquitination and subsequent degradation by the proteasome. Has GEF activity for Rab5 and GAP activity for Ras. {ECO:0000269|PubMed:16410077}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;cochlea;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;tongue;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;amnion;spleen;head and neck;cervix;kidney;stomach;aorta;peripheral nerve;cerebellum; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.65564 0.11468 -0.857930839 10.95187544 177.04932 2.89115 GAR1 0.812564980288159 0.187235181167102 0.000199838544738264 GAR1 ribonucleoprotein FUNCTION: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ("psi") residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme. {ECO:0000269|PubMed:10757788, ECO:0000269|PubMed:15044956}.; . . unclassifiable (Anatomical System);uterus;lung;placenta;testis;lens;skin;skeletal muscle;stomach; tumor;testis; 0.15921 0.12543 0.347360312 73.97381458 48.13207 1.35139 GAREM1 . . . GRB2 associated regulator of MAPK1 subtype 1 FUNCTION: Isoform 1: Acts as an adapter protein that plays a role in intracellular signaling cascades triggered either by the cell surface activated epidermal growth factor receptor and/or cytoplasmic protein tyrosine kinases. Promotes activation of the MAPK/ERK signaling pathway. Plays a role in the regulation of cell proliferation. {ECO:0000269|PubMed:19509291}.; . TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed. {ECO:0000269|PubMed:19509291}.; . . 0.55267 . -0.727458245 14.19556499 . . GAREM2 . . . GRB2 associated regulator of MAPK1 subtype 2 FUNCTION: Probable adapter protein that may provide a link between cell surface epidermal growth factor receptor and the MAPK/ERK signaling pathway. {ECO:0000250}.; . . . . . . . . . . GARNL3 0.0210868407044144 0.978912914732752 2.44562833397913e-07 GTPase activating Rap/RanGAP domain-like 3 . . . frontal lobe;heart;sympathetic chain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.32581 0.10019 -1.082044518 7.242274121 72.16886 1.76980 GARS 0.788927209872354 0.211072322151864 4.67975782228012e-07 glycyl-tRNA synthetase FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly). Is also able produce diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. {ECO:0000269|PubMed:17544401, ECO:0000269|PubMed:19710017}.; DISEASE: Neuronopathy, distal hereditary motor, 5A (HMN5A) [MIM:600794]: A disorder characterized by distal muscular atrophy mainly affecting the upper extremities, in contrast to other distal motor neuronopathies. These constitute a heterogeneous group of neuromuscular diseases caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. {ECO:0000269|PubMed:12690580, ECO:0000269|PubMed:24627108}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, including brain and spinal cord. {ECO:0000269|PubMed:12690580}.; . . 0.32729 0.09418 -0.710864321 14.5730125 146.27493 2.63526 GARSP1 . . . glycyl-tRNA synthetase pseudogene 1 . . . . . . . . . . . GART 0.0630561344999445 0.936938361115377 5.50438467845889e-06 phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;cervix;kidney;stomach;aorta; dorsal root ganglion;subthalamic nucleus;testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;bone marrow; 0.93269 0.45609 0.738527175 86.34111819 1828.99248 7.88351 GAS1 0.616849184793069 0.34990011273545 0.0332507024714807 growth arrest specific 1 FUNCTION: Specific growth arrest protein involved in growth suppression. Blocks entry to S phase. Prevents cycling of normal and transformed cells. {ECO:0000269|PubMed:8127893}.; . . hippocampus;brain; uterus;uterus corpus;prostate;superior cervical ganglion;adipose tissue;trachea;ovary;placenta;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.47753 . . . 10.18598 0.37115 GAS1RR . . . GAS1 adjacent regulatory RNA . . . . . . . . . . . GAS2 0.0262897655046356 0.96143098505522 0.0122792494401442 growth arrest specific 2 FUNCTION: May play a role in apoptosis by acting as a cell death substrate for caspases. Is cleaved during apoptosis and the cleaved form induces dramatic rearrangements of the actin cytoskeleton and potent changes in the shape of the affected cells. May be involved in the membrane ruffling process (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in liver, lung, and kidney. Not found in spleen.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;whole body;lung;thyroid;placenta;macula lutea;liver;head and neck;spleen;kidney;brain;stomach; fetal liver;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.53592 0.11293 0.193034296 66.82000472 133.74823 2.51395 GAS2L1 0.700430403558868 0.295844563709895 0.00372503273123664 growth arrest specific 2 like 1 FUNCTION: Seems to be involved in the cross-linking of microtubules and microfilaments. {ECO:0000269|PubMed:12584248}.; . . myocardium;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;oesophagus;endometrium;testis;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;lens;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; whole brain;amygdala;superior cervical ganglion;prefrontal cortex;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.31736 0.11947 0.373041938 75.29488087 1065.39448 6.25931 GAS2L1P1 . . . growth arrest specific 2 like 1 pseudogene 1 . . . . . . . . . . . GAS2L1P2 . . . growth arrest specific 2 like 1 pseudogene 2 . . . . . . . . . . . GAS2L2 0.000457988892081333 0.992090064823698 0.00745194628422069 growth arrest specific 2 like 2 FUNCTION: Seems to be involved in the cross-linking of microtubules and microfilaments. {ECO:0000269|PubMed:12584248}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle. {ECO:0000269|PubMed:12584248}.; lung; ciliary ganglion;atrioventricular node; 0.06691 0.07053 0.192828665 66.58410002 3098.11603 10.58582 GAS2L3 0.000258593475911662 0.983177979228799 0.0165634272952897 growth arrest specific 2 like 3 FUNCTION: Cytoskeletal linker protein. May promote and stabilize the formation of the actin and microtubule network. {ECO:0000269|PubMed:21561867}.; . TISSUE SPECIFICITY: Expressed in the pancreas, heart, liver, placenta, brain, skeletal muscle, kidney and lung. {ECO:0000269|PubMed:21561867}.; unclassifiable (Anatomical System);skin;breast;prostate;lung;placenta;visual apparatus;liver;testis;spleen;cervix;spinal ganglion;brain;peripheral nerve; . 0.11868 0.08968 0.891034851 89.2663364 163.59839 2.79289 GAS5 . . . growth arrest specific 5 (non-protein coding) . . . . . . . . . . . GAS5-AS1 . . . GAS5 antisense RNA 1 . . . . . . . . . . . GAS6 0.333438602414211 0.666430350052204 0.000131047533585049 growth arrest specific 6 FUNCTION: Ligand for tyrosine-protein kinase receptors AXL, TYRO3 and MER whose signaling is implicated in cell growth and survival, cell adhesion and cell migration. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. {ECO:0000269|PubMed:12364394, ECO:0000269|PubMed:18840707}.; . TISSUE SPECIFICITY: Plasma. Isoform 1 and isoform 2 are widely expressed. Isoform 1 is the predominant form in spleen. {ECO:0000269|PubMed:8336730, ECO:0000269|PubMed:9326368}.; ovary;colon;parathyroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;adipose tissue;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.18220 0.26643 -0.437212558 24.67563105 267.9424 3.51157 GAS6-AS1 . . . GAS6 antisense RNA 1 . . . . . . . . . . . GAS6-AS2 . . . GAS6 antisense RNA 2 (head to head) . . . . . . . . . . . GAS7 0.0255296444534551 0.973929211431346 0.000541144115198987 growth arrest specific 7 FUNCTION: May play a role in promoting maturation and morphological differentiation of cerebellar neurons.; DISEASE: Note=A chromosomal aberration involving GAS7 is found in acute myeloid leukemia. Translocation t(11;17)(q23;p13) with KMT2A/MLL1. {ECO:0000269|PubMed:10706619}.; . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;thyroid;iris;germinal center;brain;amygdala;heart;cartilage;nervous;urinary;adrenal cortex;blood;lens;breast;epididymis;visual apparatus;macula lutea;spleen;mammary gland;peripheral nerve;colon;choroid;fovea centralis;uterus;whole body;cerebral cortex;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;amygdala;whole brain;medulla oblongata;superior cervical ganglion;occipital lobe;olfactory bulb;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.97597 0.12766 -0.53631094 20.53550366 26.29294 0.85282 GAS8 8.03531596883606e-08 0.47824060940234 0.5217593102445 growth arrest specific 8 FUNCTION: Cytoskeletal linker which binds microtubules and probably functions in axonemal and non-axonemal dynein regulation. May play a role in the spermatozoa motility (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the heart, skeletal muscle, pancreas and liver. Weakly or not expressed in brain, placenta, lung and kidney. {ECO:0000269|PubMed:9790751}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;iris;testis;brain;unclassifiable (Anatomical System);cartilage;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;cervix;head and neck;kidney;mammary gland;stomach; testis - interstitial;parietal lobe; 0.10285 0.10886 0.205769367 67.49823071 638.93703 5.08494 GAS8-AS1 . . . GAS8 antisense RNA 1 . . . . . . . 0.325313577 73.11276244 . . GAST 0.00317378388720094 0.598567143640383 0.398259072472416 gastrin FUNCTION: Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine.; . . stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06712 0.37189 0.391453969 75.87284737 17.04946 0.60033 GATA1 0.837375784159948 0.159462701799493 0.0031615140405591 GATA binding protein 1 FUNCTION: Transcriptional activator or repressor which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory regions of globin genes and of other genes expressed in erythroid cells. Activates the transcription of genes involved in erythroid differentiation of K562 erythroleukemia cells, including HBB, HBG1/2, ALAS2 and HMBS (PubMed:24245781). {ECO:0000269|PubMed:22235304, ECO:0000269|PubMed:24245781}.; DISEASE: X-linked dyserythropoietic anemia and thrombocytopenia (XDAT) [MIM:300367]: Disorder characterized by erythrocytes with abnormal size and shape, and paucity of platelets in peripheral blood. The bone marrow contains abundant and abnormally small megakaryocytes. {ECO:0000269|PubMed:10700180, ECO:0000269|PubMed:11418466, ECO:0000269|PubMed:11675338, ECO:0000269|PubMed:11809723}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Thrombocytopenia with beta-thalassemia, X-linked (XLTT) [MIM:314050]: An unusual form of thrombocytopenia associated with beta-thalassemia. Patients have splenomegaly and petechiae, moderate thrombocytopenia, prolonged bleeding time due to platelet dysfunction, reticulocytosis and unbalanced (hemo)globin chain synthesis resembling that of beta-thalassemia minor. {ECO:0000269|PubMed:12200364}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Anemia without thrombocytopenia, X-linked (XLAWT) [MIM:300835]: A form of anemia characterized by abnormal morphology of erythrocytes and granulocytes in peripheral blood, bone marrow dysplasia with hypocellularity of erythroid and granulocytic lineages, and normal or increased number of megakaryocytes. Neutropenia of a variable degree is present in affected individuals. {ECO:0000269|PubMed:16783379}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Erythrocytes. {ECO:0000269|PubMed:8524811}.; . . 0.33731 0.70879 -0.60427181 17.74593064 13.74199 0.49878 GATA2 0.979762089854754 0.0202214131848697 1.64969603759823e-05 GATA binding protein 2 FUNCTION: Transcriptional activator which regulates endothelin-1 gene expression in endothelial cells. Binds to the consensus sequence 5'-AGATAG-3'.; DISEASE: Lymphedema, primary, with myelodysplasia (LMPM) [MIM:614038]: A chronic disabling condition characterized by swelling of the extremities due to altered lymphatic flow, associated with myelodysplasia. Patients with lymphedema suffer from recurrent local infections, and physical impairment. {ECO:0000269|PubMed:21892158}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myelodysplastic syndrome (MDS) [MIM:614286]: A heterogeneous group of closely related clonal hematopoietic disorders. All are characterized by a hypercellular or hypocellular bone marrow with impaired morphology and maturation, dysplasia of the myeloid, megakaryocytic and/or erythroid lineages, and peripheral blood cytopenias resulting from ineffective blood cell production. Included diseases are: refractory anemia (RA), refractory anemia with ringed sideroblasts (RARS), refractory anemia with excess blasts (RAEB), refractory cytopenia with multilineage dysplasia and ringed sideroblasts (RCMD-RS); chronic myelomonocytic leukemia (CMML) is a myelodysplastic/myeloproliferative disease. MDS is considered a premalignant condition in a subgroup of patients that often progresses to acute myeloid leukemia (AML). {ECO:0000269|PubMed:21892162}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Endothelial cells.; unclassifiable (Anatomical System);ovary;parathyroid;blood;choroid;bone marrow;uterus;pancreas;prostate;lung;cochlea;endometrium;placenta;iris;liver;spleen;cervix;kidney;brain;stomach; prostate;superior cervical ganglion;placenta;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.36437 0.63508 -0.424258538 25.56027365 2249.29606 8.75850 GATA2-AS1 . . . GATA2 antisense RNA 1 . . . . . . . . . . . GATA3 0.882718840964597 0.117002181675328 0.000278977360074611 GATA binding protein 3 FUNCTION: Transcriptional activator which binds to the enhancer of the T-cell receptor alpha and delta genes. Binds to the consensus sequence 5'-AGATAG-3'. Required for the T-helper 2 (Th2) differentiation process following immune and inflammatory responses. {ECO:0000269|PubMed:23824597}.; DISEASE: Hypoparathyroidism, sensorineural deafness, and renal disease (HDR) [MIM:146255]: A disease characterized by steroid- resistant nephrosis with progressive renal failure, hypoparathyroidism, sensorineural deafness, and renal dysplasia. {ECO:0000269|PubMed:10935639, ECO:0000269|PubMed:11389161}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: T-cells and endothelial cells.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;thyroid;brain;bladder;unclassifiable (Anatomical System);heart;tongue;urinary;pharynx;blood;lens;breast;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;thymus; superior cervical ganglion;prostate;placenta;kidney;trigeminal ganglion;skin;thymus; 0.68970 0.82566 -0.648365105 16.35999056 21.7772 0.73288 GATA3-AS1 . . . GATA3 antisense RNA 1 . . . . . . . . . . . GATA4 0.802155487205778 0.196709896364293 0.00113461642992872 GATA binding protein 4 FUNCTION: Transcriptional activator that binds to the consensus sequence 5'-AGATAG-3' and plays a key role in cardiac development. Involved in bone morphogenetic protein (BMP)-mediated induction of cardiac-specific gene expression. Binds to BMP response element (BMPRE) DNA sequences within cardiac activating regions. Acts as a transcriptional activator of ANF in cooperation with NKX2-5. Promotes cardiac myocyte enlargement. Required during testicular development. {ECO:0000269|PubMed:20081228, ECO:0000269|PubMed:21220346, ECO:0000269|PubMed:24000169}.; DISEASE: Atrial septal defect 2 (ASD2) [MIM:607941]: A congenital heart malformation characterized by incomplete closure of the wall between the atria resulting in blood flow from the left to the right atria. Patients show other heart abnormalities including ventricular and atrioventricular septal defects, pulmonary valve thickening or insufficiency of the cardiac valves. The disease is not associated with defects in the cardiac conduction system or non-cardiac abnormalities. {ECO:0000269|PubMed:12845333, ECO:0000269|PubMed:15810002, ECO:0000269|PubMed:17643447, ECO:0000269|PubMed:18055909, ECO:0000269|PubMed:20347099, ECO:0000269|PubMed:20659440}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ventricular septal defect 1 (VSD1) [MIM:614429]: A common form of congenital cardiovascular anomaly that may occur alone or in combination with other cardiac malformations. It can affect any portion of the ventricular septum, resulting in abnormal communications between the two lower chambers of the heart. Classification is based on location of the communication, such as perimembranous, inlet, outlet (infundibular), central muscular, marginal muscular, or apical muscular defect. Large defects that go unrepaired may give rise to cardiac enlargement, congestive heart failure, pulmonary hypertension, Eisenmenger's syndrome, delayed fetal brain development, arrhythmias, and even sudden cardiac death. {ECO:0000269|PubMed:18055909, ECO:0000269|PubMed:18672102, ECO:0000269|PubMed:21110066, ECO:0000269|PubMed:21637914, ECO:0000269|PubMed:22101736}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Tetralogy of Fallot (TOF) [MIM:187500]: A congenital heart anomaly which consists of pulmonary stenosis, ventricular septal defect, dextroposition of the aorta (aorta is on the right side instead of the left) and hypertrophy of the right ventricle. In this condition, blood from both ventricles (oxygen-rich and oxygen-poor) is pumped into the body often causing cyanosis. {ECO:0000269|PubMed:18672102, ECO:0000269|PubMed:21110066, ECO:0000269|PubMed:24000169}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Atrioventricular septal defect 4 (AVSD4) [MIM:614430]: A congenital heart malformation characterized by a common atrioventricular junction coexisting with deficient atrioventricular septation. The complete form involves underdevelopment of the lower part of the atrial septum and the upper part of the ventricular septum; the valve itself is also shared. A less severe form, known as ostium primum atrial septal defect, is characterized by separate atrioventricular valvar orifices despite a common junction. {ECO:0000269|PubMed:17643447}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Testicular anomalies with or without congenital heart disease (TACHD) [MIM:615542]: A 46,XY disorder of sex development with variable clinical presentation and defects in testicular differentiation and function. Clinical features include ambiguous genitalia, fused labioscrotal folds, hypospadias, microphallus, and bilateral inguinal hernia containing gonads. {ECO:0000269|PubMed:21220346}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=GATA4 mutations can predispose to dilated cardiomyopathy (CMD), a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:24041700, ECO:0000269|PubMed:25017055}.; . unclassifiable (Anatomical System);medulla oblongata;heart;ovary;islets of Langerhans;colon;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;lung;placenta;macula lutea;liver;testis;spleen;brain;stomach;thymus; heart;testis - seminiferous tubule;testis; 0.95416 0.71185 . . 448.35115 4.40311 GATA5 0.250742908677773 0.72045946830414 0.0287976230180864 GATA binding protein 5 FUNCTION: Transcription factor required during cardiovascular development (PubMed:23289003). Plays an important role in the transcriptional program(s) that underlies smooth muscle cell diversity (By similarity). Binds to the functionally important CEF-1 nuclear protein binding site in the cardiac-specific slow/cardiac troponin C transcriptional enhancer (PubMed:25543888). {ECO:0000250|UniProtKB:P97489, ECO:0000269|PubMed:23289003, ECO:0000269|PubMed:25543888}.; DISEASE: Note=Rare variants in GATA5 may be a cause of susceptibility to atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:22483626, ECO:0000269|PubMed:23175127, ECO:0000269|PubMed:23295592}.; DISEASE: Note=Rare variants in GATA5 may be a cause of susceptibility to Tetraology of Fallot (TOF) [MIM:187500]. TOF is a congenital heart anomaly which consists of pulmonary stenosis, ventricular septal defect, dextroposition of the aorta (aorta is on the right side instead of the left) and hypertrophy of the right ventricle. In this condition, blood from both ventricles (oxygen-rich and oxygen-poor) is pumped into the body often causing cyanosis. {ECO:0000269|PubMed:23289003, ECO:0000269|PubMed:24573614}.; DISEASE: Note=Rare variants in GATA5 may be a cause of susceptibility to ventriculoseptal defect (VSD). VSD is a congenital heart disease which may lead to cardiac enlargement, ventricular dysfunction or heart failure, poor quality of life, pulmonary hypertension, Eisenmenger's syndrome, delayed fetal brain development, arrhythmias, and even sudden cardiac death in the absence of surgical treatment or transcatheter repair. {ECO:0000269|PubMed:22961344}.; DISEASE: Note=Rare variants in GATA5 may be a cause of susceptibility to aortic valve disease (AOVD). AOVD is a common defect in the aortic valve in which two rather than three leaflets are present. It is often associated with aortic valve calcification, stenosis and insufficiency. In extreme cases, the blood flow may be so restricted that the left ventricle fails to grow, resulting in hypoplastic left heart syndrome. {ECO:0000269|PubMed:24638895}.; DISEASE: Note=Rare variants in GATA5 may be a cause of susceptibility to dilated cardiomyopathy (CMD). CMD is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:22641149, ECO:0000269|PubMed:25543888}.; . unclassifiable (Anatomical System);uterus;prostate;lung;cartilage;liver;testis;spleen;kidney; dorsal root ganglion;superior cervical ganglion;adrenal gland;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.53172 0.30287 . . 873.58675 5.75154 GATA6 . . . GATA binding protein 6 FUNCTION: Transcriptional activator that regulates SEMA3C and PLXNA2. Thought to be important for regulating terminal differentiation and/or proliferation. Involved in gene regulation specifically in the gastric epithelium. Involved in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to BMP response element (BMPRE) DNA sequences within cardiac activating regions (By similarity). {ECO:0000250, ECO:0000269|PubMed:19666519}.; DISEASE: Conotruncal heart malformations (CTHM) [MIM:217095]: A group of congenital heart defects involving the outflow tracts. Examples include truncus arteriosus communis, double-outlet right ventricle and transposition of great arteries. Truncus arteriosus communis is characterized by a single outflow tract instead of a separate aorta and pulmonary artery. In transposition of the great arteries, the aorta arises from the right ventricle and the pulmonary artery from the left ventricle. In double outlet of the right ventricle, both the pulmonary artery and aorta arise from the right ventricle. {ECO:0000269|PubMed:19666519}. Note=The disease is caused by mutations affecting the gene represented in this entry. GATA6 mutations have been found in patients with non- syndromic persistent truncus arteriosus (PubMed:19666519). {ECO:0000269|PubMed:19666519}.; DISEASE: Atrial septal defect 9 (ASD9) [MIM:614475]: A congenital heart malformation characterized by incomplete closure of the wall between the atria resulting in blood flow from the left to the right atria. Some patients manifest tricuspid valve disease, pulmonary valve disease, and pulmonary artery hypertension. {ECO:0000269|PubMed:20631719}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Tetralogy of Fallot (TOF) [MIM:187500]: A congenital heart anomaly which consists of pulmonary stenosis, ventricular septal defect, dextroposition of the aorta (aorta is on the right side instead of the left) and hypertrophy of the right ventricle. In this condition, blood from both ventricles (oxygen-rich and oxygen-poor) is pumped into the body often causing cyanosis. {ECO:0000269|PubMed:20581743, ECO:0000269|PubMed:20631719}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Atrioventricular septal defect 5 (AVSD5) [MIM:614474]: A congenital heart malformation characterized by a common atrioventricular junction coexisting with deficient atrioventricular septation. The complete form involves underdevelopment of the lower part of the atrial septum and the upper part of the ventricular septum; the valve itself is also shared. A less severe form, known as ostium primum atrial septal defect, is characterized by separate atrioventricular valvar orifices despite a common junction. {ECO:0000269|PubMed:20581743}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pancreatic agenesis and congenital heart defects (PACHD) [MIM:600001]: An autosomal dominant disease characterized by pancreatic severe hypoplasia or agenesis, diabetes mellitus, and congenital heart abnormalities including ventricular septal defect, patent ductus arteriosus, pulmonary artery stenosis, truncus arteriosus and tetralogy of Fallot. {ECO:0000269|PubMed:22158542}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in heart, gut and gut-derived tissues.; unclassifiable (Anatomical System);myocardium;smooth muscle;cartilage;ovary;heart;islets of Langerhans;colon;parathyroid;blood;whole body;lung;placenta;liver;testis;cervix;spleen;kidney;aorta;stomach; uterus;uterus corpus;heart;adrenal gland;adrenal cortex;testis; 0.63517 0.40862 . . 110.3852 2.28630 GATA6-AS1 . . . GATA6 antisense RNA 1 (head to head) . . . . . . . . . . . GATAD1 0.507483499064787 0.473876778509361 0.0186397224258525 GATA zinc finger domain containing 1 FUNCTION: Component of some chromatin complex recruited to chromatin sites methylated 'Lys-4' of histone H3 (H3K4me). {ECO:0000269|PubMed:20850016}.; . TISSUE SPECIFICITY: Ubiquitously expressed among various tissue types. Expressed in left ventricular myocytes. {ECO:0000269|PubMed:21965549}.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;spinal ganglion;brain;artery;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; amygdala;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.65734 0.10130 -0.007201372 53.19061099 340.57978 3.91668 GATAD2A 0.995362828250654 0.00463715347352683 1.82758187232231e-08 GATA zinc finger domain containing 2A FUNCTION: Transcriptional repressor. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2B. {ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:16415179}.; . TISSUE SPECIFICITY: Ubiquitous, both in fetal and adult tissues. {ECO:0000269|PubMed:12183469}.; lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;amnion;liver;spleen;head and neck;cervix;kidney;stomach; testis - seminiferous tubule;testis; 0.34093 . -0.951568548 9.271054494 163.14317 2.78951 GATAD2B 0.998594716203308 0.00140527888971798 4.90697395918439e-09 GATA zinc finger domain containing 2B FUNCTION: Transcriptional repressor. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2A. Targets MBD3 to discrete loci in the nucleus. May play a role in synapse development. {ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:16415179}.; DISEASE: Mental retardation, autosomal dominant 18 (MRD18) [MIM:615074]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD18 patients have severe intellectual disability and dysmorphic features. {ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:23644463}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12183469}.; . . 0.76491 0.10651 -0.069700724 48.54328851 66.82128 1.68781 GATB . . . glutamyl-tRNA(Gln) amidotransferase, subunit B FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_03147, ECO:0000269|PubMed:19805282}.; . TISSUE SPECIFICITY: Predominantly expressed in tissues characterized by high rates of oxidative phosphorylation (OxPhos), including muscle and heart. {ECO:0000269|PubMed:9878253}.; . . 0.05276 0.13335 0.358272123 74.66383581 . . GATC 7.79020409773576e-05 0.312672744742528 0.687249353216495 glutamyl-tRNA(Gln) amidotransferase, subunit C FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_03149, ECO:0000269|PubMed:19805282}.; . . . . 0.22892 0.10495 -0.095386216 46.48502005 241.12139 3.35348 GATM 0.866491076784892 0.133492749620755 1.61735943536133e-05 glycine amidinotransferase FUNCTION: Catalyzes the biosynthesis of guanidinoacetate, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues. May play a role in embryonic and central nervous system development. May be involved in the response to heart failure by elevating local creatine synthesis. {ECO:0000269|PubMed:16125225, ECO:0000269|PubMed:16614068, ECO:0000269|PubMed:16820567}.; DISEASE: Cerebral creatine deficiency syndrome 3 (CCDS3) [MIM:612718]: An autosomal recessive disorder characterized by developmental delay/regression, mental retardation, severe disturbance of expressive and cognitive speech, and severe depletion of creatine/phosphocreatine in the brain. Most patients develop a myopathy characterized by muscle weakness and atrophy later in life. {ECO:0000269|PubMed:11555793, ECO:0000269|PubMed:20682460, ECO:0000269|PubMed:22386973, ECO:0000269|PubMed:23660394, ECO:0000269|PubMed:23770102}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, salivary gland and skeletal muscle tissue, with the highest expression in kidney. Biallelically expressed in placenta and fetal tissues. {ECO:0000269|PubMed:16125225, ECO:0000269|PubMed:16614068, ECO:0000269|PubMed:16820567}.; . . 0.20421 0.20718 -0.139478553 43.29440906 9.84943 0.36076 GATS 0.000965025102116515 0.582429823263089 0.416605151634794 GATS, stromal antigen 3 opposite strand . . . . . . . -0.251530012 35.42108988 16.48448 0.58354 GATSL2 . . . GATS protein-like 2 . . . brain; . . . . . 5.41824 0.20064 GATSL3 0.453126498226772 0.540752387388585 0.00612111438464263 GATS protein-like 3 . . . . . . . -0.205617011 38.57631517 389.27369 4.15511 GBA 0.0340405400496017 0.964232717995036 0.00172674195536255 glucosidase, beta, acid . DISEASE: Gaucher disease (GD) [MIM:230800]: A lysosomal storage disease due to deficient activity of beta-glucocerebrosidase and characterized by accumulation of glucosylceramide in the reticulo- endothelial system. Different clinical forms are recognized depending on the presence (neuronopathic forms) or absence of central nervous system involvement, severity and age of onset. {ECO:0000269|PubMed:10352942, ECO:0000269|PubMed:10360404, ECO:0000269|PubMed:10447266, ECO:0000269|PubMed:10744424, ECO:0000269|PubMed:10796875, ECO:0000269|PubMed:11933202, ECO:0000269|PubMed:11992489, ECO:0000269|PubMed:12204005, ECO:0000269|PubMed:15292921, ECO:0000269|PubMed:1972019, ECO:0000269|PubMed:1974409, ECO:0000269|PubMed:7627184, ECO:0000269|PubMed:7627192, ECO:0000269|PubMed:7916532, ECO:0000269|PubMed:8076951, ECO:0000269|PubMed:8112750, ECO:0000269|PubMed:8294033, ECO:0000269|PubMed:8432537, ECO:0000269|PubMed:8790604, ECO:0000269|PubMed:8829654, ECO:0000269|PubMed:8829663, ECO:0000269|PubMed:8937765, ECO:0000269|PubMed:9061570, ECO:0000269|PubMed:9153297, ECO:0000269|PubMed:9182788, ECO:0000269|PubMed:9217217, ECO:0000269|PubMed:9279145, ECO:0000269|PubMed:9516376, ECO:0000269|PubMed:9554454, ECO:0000269|PubMed:9554746, ECO:0000269|PubMed:9650766, ECO:0000269|PubMed:9683600}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Gaucher disease 1 (GD1) [MIM:230800]: A form of Gaucher disease characterized by hepatosplenomegaly with consequent anemia and thrombopenia, and bone involvement. The central nervous system is not involved. {ECO:0000269|PubMed:10206680, ECO:0000269|PubMed:10340647, ECO:0000269|PubMed:15605411, ECO:0000269|PubMed:8889591, ECO:0000269|Ref.14}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Gaucher disease 2 (GD2) [MIM:230900]: The most severe form of Gaucher disease. It manifests soon after birth, with death generally occurring before patients reach two years of age. {ECO:0000269|PubMed:9637431, ECO:0000269|PubMed:9851895}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Gaucher disease 3 (GD3) [MIM:231000]: A subacute form of neuronopathic Gaucher disease. It has later onset and slower progression compared to the acute form of neuronopathic Gaucher disease 2. {ECO:0000269|PubMed:8780099}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Gaucher disease 3C (GD3C) [MIM:231005]: A variant of subacute neuronopathic Gaucher disease 3 associated with cardiovascular calcifications. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Gaucher disease perinatal lethal (GDPL) [MIM:608013]: Distinct form of Gaucher disease type 2, characterized by fetal onset. Hydrops fetalis, in utero fetal death and neonatal distress are prominent features. When hydrops is absent, neurologic involvement begins in the first week and leads to death within 3 months. Hepatosplenomegaly is a major sign, and is associated with ichthyosis, arthrogryposis, and facial dysmorphism. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Perinatal lethal Gaucher disease is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.; DISEASE: Parkinson disease (PARK) [MIM:168600]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features. {ECO:0000269|PubMed:12847165, ECO:0000269|PubMed:16148263, ECO:0000269|PubMed:19286695}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;mesenchyma;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; . 0.08789 0.63610 0.178263593 66.12998349 149.04466 2.66182 GBA2 4.79266614474154e-09 0.997511903647946 0.00248809155938822 glucosidase, beta (bile acid) 2 FUNCTION: Non-lysosomal glucosylceramidase that catalyzes the conversion of glucosylceramide (GlcCer) to free glucose and ceramide. Involved in sphingomyelin generation and prevention of glycolipid accumulation. May also catalyze the hydrolysis of bile acid 3-O-glucosides, however, the relevance of such activity is unclear in vivo. Plays a role in central nevous system development. Required for proper formation of motor neuron axons. {ECO:0000269|PubMed:17105727, ECO:0000269|PubMed:23332916}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain, heart, skeletal muscle, kidney and placenta and expressed at lower level in liver. {ECO:0000269|PubMed:11489889}.; . . 0.11563 0.19384 -0.150608082 42.28001887 730.63358 5.36594 GBA3 . . . glucosidase, beta, acid 3 (gene/pseudogene) FUNCTION: Glycosidase probably involved in the intestinal absorption and metabolism of dietary flavonoid glycosides. Able to hydrolyze a broad variety of glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens. Possesses beta- glycosylceramidase activity and may be involved in a nonlysosomal catabolic pathway of glycosylceramide. {ECO:0000269|PubMed:11784319, ECO:0000269|PubMed:12594539, ECO:0000269|PubMed:17595169}.; . TISSUE SPECIFICITY: Present in small intestine (at protein level). Expressed in liver, small intestine, colon, spleen and kidney. Down-regulated in renal cell carcinomas and hepatocellular carcinomas. {ECO:0000269|PubMed:11043382, ECO:0000269|PubMed:12594539}.; . . 0.09146 0.47755 0.775339069 87.13729653 . . GBAP1 . . . glucosidase, beta, acid pseudogene 1 . . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node; . . . . . . GBAS 4.14826721847044e-05 0.842560252987086 0.15739826434073 glioblastoma amplified sequence . . TISSUE SPECIFICITY: Widely expressed. Most abundant in heart and skeletal muscle.; lymphoreticular;myocardium;smooth muscle;ovary;salivary gland;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;atrium;whole body;cochlea;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;superior cervical ganglion;subthalamic nucleus;occipital lobe;hypothalamus;thyroid;prefrontal cortex;skeletal muscle; 0.12465 0.10558 0.080983847 59.76055674 119.86171 2.38400 GBD2 . . . gallbladder disease 2 . . . . . . . . . . . GBD3 . . . gallbladder disease 3 . . . . . . . . . . . GBE1 1.17856543699791e-13 0.042480254367404 0.957519745632478 glucan (1,4-alpha-), branching enzyme 1 FUNCTION: Required for sufficient glycogen accumulation. The alpha 1-6 branches of glycogen play an important role in increasing the solubility of the molecule and, consequently, in reducing the osmotic pressure within cells.; DISEASE: Note=Neuromuscular perinatal glycogen storage disease type 4 is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders. {ECO:0000269|PubMed:15452297}.; DISEASE: Polyglucosan body neuropathy, adult form (APBN) [MIM:263570]: A late-onset, slowly progressive disorder affecting the central and peripheral nervous systems. Patients typically present after age 40 years with a variable combination of cognitive impairment, pyramidal tetraparesis, peripheral neuropathy, and neurogenic bladder. Other manifestations include cerebellar dysfunction and extrapyramidal signs. The pathologic hallmark of APBN is the widespread accumulation of round, intracellular polyglucosan bodies throughout the nervous system, which are confined to neuronal and astrocytic processes. {ECO:0000269|PubMed:10762170}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest levels found in liver and muscle.; ovary;colon;parathyroid;skin;retina;uterus;prostate;endometrium;larynx;bone;iris;pituitary gland;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;skeletal muscle;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; adipose tissue;smooth muscle; 0.33563 0.45525 0.624649618 83.53385232 3530.8208 11.46128 GBF1 4.12350724274109e-07 0.999999587362748 2.8652727931814e-10 golgi brefeldin A resistant guanine nucleotide exchange factor 1 FUNCTION: Guanine-nucleotide exchange factor (GEF) for members of the Arf family of small GTPases involved in trafficking in the early secretory pathway; its GEF activity initiates the coating of nascent vesicles via the localized generation of activated ARFs through replacement of GDP with GTP. Recruitment to cis-Golgi membranes requires membrane association of Arf-GDP and can be regulated by ARF1, ARF3, ARF4 and ARF5. Involved in the recruitment of the COPI coat complex to the endoplasmic reticulum exit sites (ERES), and the endoplasmic reticulum-Golgi intermediate (ERGIC) and cis-Golgi compartments which implicates ARF1 activation. Involved in COPI vesicle-dependent retrograde transport from the ERGIC and cis-Golgi compartments to the endoplasmatic reticulum (ER) (PubMed:16926190, PubMed:17956946, PubMed:18003980, PubMed:12047556, PubMed:12808027, PubMed:19039328, PubMed:24213530). Involved in the trans-Golgi network recruitment of GGA1, GGA2, GGA3, BIG1, BIG2, and the AP-1 adaptor protein complex related to chlathrin-dependent transport; the function requires its GEF activity (probably at least in part on ARF4 and ARF5) (PubMed:23386609). Has GEF activity towards ARF1 (PubMed:15616190). Has in vitro GEF activity towards ARF5 (By similarity). Involved in the processing of PSAP (PubMed:17666033). Required for the assembly of the Golgi apparatus (PubMed:12808027, PubMed:18003980). The AMPK-phosphorylated form is involved in Golgi disassembly during mitotis and under stress conditions (PubMed:18063581, PubMed:23418352). May be involved in the COPI vesicle-dependent recruitment of PNPLA2 to lipid droplets; however, this function is under debate (PubMed:19461073, PubMed:22185782). In neutrophils, involved in G protein-coupled receptor (GPCR)-mediated chemotaxis und superoxide production. Proposed to be recruited by phosphatidylinositol-phosphates generated upon GPCR stimulation to the leading edge where it recruits and activates ARF1, and is involved in recruitment of GIT2 and the NADPH oxidase complex (PubMed:22573891). {ECO:0000250|UniProtKB:Q9R1D7, ECO:0000269|PubMed:12047556, ECO:0000269|PubMed:12808027, ECO:0000269|PubMed:15616190, ECO:0000269|PubMed:16926190, ECO:0000269|PubMed:17666033, ECO:0000269|PubMed:17956946, ECO:0000269|PubMed:18003980, ECO:0000269|PubMed:18063581, ECO:0000269|PubMed:19461073, ECO:0000269|PubMed:22185782, ECO:0000269|PubMed:22573891, ECO:0000269|PubMed:23386609, ECO:0000269|PubMed:23418352, ECO:0000269|PubMed:24213530, ECO:0000305|PubMed:19039328, ECO:0000305|PubMed:22573891}.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.65170 0.10544 -3.002865511 0.53668318 218.46616 3.19539 GBGT1 0.000100077199027406 0.573886649519179 0.426013273281793 globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 FUNCTION: Catalyzes the formation of some glycolipid via the addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to some substrate. Glycolipids probably serve for adherence of some pathogens.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in placenta, ovary and peripheral blood leukocyte, whereas it is weakly expressed in liver, thymus, and testis. {ECO:0000269|PubMed:10506200}.; . . 0.09616 0.16256 1.668219306 96.30219391 646.47154 5.10503 GBP1 1.80843358162521e-12 0.107131980239492 0.892868019758699 guanylate binding protein 1 FUNCTION: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions. Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes. {ECO:0000269|PubMed:22106366}.; . . . . 0.51402 0.17326 -0.08265057 47.20452937 1596.87131 7.39752 GBP1P1 . . . guanylate binding protein 1 pseudogene 1 . . . . . . . . . . . GBP2 1.96948500969075e-05 0.973294418037154 0.0266858871127493 guanylate binding protein 2 FUNCTION: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions, but the major reaction product is GDP (PubMed:8706832). Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes (By similarity). {ECO:0000250|UniProtKB:P32455, ECO:0000269|PubMed:8706832}.; . . . . 0.15461 . 0.957177419 90.14508139 53.19341 1.44886 GBP3 5.83109623121067e-18 0.00172636088016635 0.998273639119834 guanylate binding protein 3 FUNCTION: Exhibits antiviral activity against influenza virus. {ECO:0000269|PubMed:22106366}.; . . unclassifiable (Anatomical System);cartilage;ovary;colon;parathyroid;skeletal muscle;bone marrow;uterus;bile duct;pancreas;whole body;lung;endometrium;adrenal gland;nasopharynx;bone;placenta;liver;kidney;brain;bladder;stomach; . 0.06010 0.08192 3.02462456 99.22741213 9983.77449 21.77381 GBP4 1.42218697793758e-09 0.347776876663484 0.652223121914329 guanylate binding protein 4 FUNCTION: Binds GTP, GDP and GMP. Hydrolyzes GTP very efficiently; GDP rather than GMP is the major reaction product. Plays a role in erythroid differentiation (By similarity). {ECO:0000250}.; . . . . 0.06048 . 1.758248793 96.72682236 364.12153 4.03932 GBP5 7.95482106405718e-06 0.915496036041413 0.084496009137523 guanylate binding protein 5 FUNCTION: As an activator of NLRP3 inflammasome assembly, plays a role in innate immunity and inflammation. Promotes selective NLRP3 inflammasome assembly in response to microbial and soluble, but not crystalline, agents (PubMed:22461501). Hydrolyzes GTP, but in contrast to other family members, does not produce GMP (PubMed:20180847). {ECO:0000269|PubMed:20180847, ECO:0000269|PubMed:22461501}.; . TISSUE SPECIFICITY: Expressed in peripheral blood monocytes (at protein level). {ECO:0000269|PubMed:15175044}.; unclassifiable (Anatomical System);lymph node;ovary;parathyroid;blood;skeletal muscle;uterus;lung;endometrium;placenta;alveolus;liver;germinal center;kidney;mammary gland; white blood cells;whole blood; 0.05604 . 0.53464283 81.00967209 334.13832 3.88397 GBP6 2.45413567039759e-10 0.251700065778585 0.748299933976002 guanylate binding protein family member 6 FUNCTION: Binds GTP, GDP and GMP. {ECO:0000250}.; . . . . 0.06049 0.08911 1.291545885 93.87827318 312.72771 3.76400 GBP7 5.50946977464199e-11 0.206010593328775 0.79398940661613 guanylate binding protein 7 FUNCTION: Hydrolyzes GTP to GMP in two consecutive cleavage reactions. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes (By similarity). {ECO:0000250}.; . . visual apparatus; . 0.02980 0.12513 0.936951807 89.86789337 505.52099 4.61442 GBX1 0.269607760761063 0.705717520382989 0.024674718855948 gastrulation brain homeobox 1 . . . unclassifiable (Anatomical System); superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.41174 . . . 183.386 2.93938 GBX2 0.567961292707506 0.42020625868964 0.0118324486028538 gastrulation brain homeobox 2 FUNCTION: May act as a transcription factor for cell pluripotency and differentiation in the embryo.; . . unclassifiable (Anatomical System);colon;brain;stomach; superior cervical ganglion;adrenal cortex; 0.79886 0.23775 -0.229483771 36.86010852 119.9659 2.38746 GC 5.77520038554047e-06 0.878852319305628 0.121141905493987 group-specific component (vitamin D binding protein) FUNCTION: Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation. {ECO:0000305|PubMed:16302727}.; . TISSUE SPECIFICITY: Expressed in the liver. Found in plasma, ascites, cerebrospinal fluid and urine. {ECO:0000269|PubMed:20079467, ECO:0000269|PubMed:2416779, ECO:0000305|PubMed:16302727}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;parathyroid;skin;skeletal muscle;uterus;pancreas;whole body;lung;bone;placenta;liver;testis;spleen;kidney;gall bladder; fetal liver;superior cervical ganglion;beta cell islets;liver;fetal lung; 0.15304 0.43038 0.042348793 57.31304553 110.27767 2.28479 GCA 0.000445654786146001 0.864280583917146 0.135273761296708 grancalcin FUNCTION: Calcium-binding protein that may play a role in the adhesion of neutrophils to fibronectin. May play a role in the formation of focal adhesions.; . TISSUE SPECIFICITY: Detected in neutrophils and macrophages (at protein level). Highly expressed in bone marrow. {ECO:0000269|PubMed:1737748}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;hippocampus;alveolus;liver;spleen;kidney;aorta;stomach; superior cervical ganglion;whole blood;bone marrow; 0.09315 0.18330 0.525552348 80.57914603 485.21462 4.53610 GCAT 7.76096763410133e-06 0.502947203012461 0.497045036019905 glycine C-acetyltransferase . . TISSUE SPECIFICITY: Strongly expressed in heart, brain, liver and pancreas. Also found in lung. {ECO:0000269|PubMed:10712613}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;pharynx;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;liver;skeletal muscle;parietal lobe; 0.07508 0.15012 0.845119304 88.4170795 867.59334 5.73571 GCATP1 . . . glycine C-acetyltransferase pseudogene 1 . . . . . . . . . . . GCC1 6.6895203134617e-08 0.441440477812731 0.558559455292066 GRIP and coiled-coil domain containing 1 FUNCTION: Probably involved in maintaining Golgi structure.; . . ovary;colon;parathyroid;fovea centralis;skin;bone marrow;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;blood;bile duct;breast;lung;placenta;macula lutea;liver;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;caudate nucleus;trigeminal ganglion; 0.20327 0.11174 0.246221394 69.56829441 458.08135 4.44307 GCC2 0.0134657614610954 0.986534234607569 3.93133566128148e-09 GRIP and coiled-coil domain containing 2 FUNCTION: Golgin which probably tethers transport vesicles to the trans-Golgi network (TGN) and regulates vesicular transport between the endosomes and the Golgi. As a RAB9A effector it is involved in recycling of the mannose 6-phosphate receptor from the late endosomes to the TGN. May also play a role in transport between the recycling endosomes and the Golgi. Required for maintenance of the Golgi structure, it is involved in the biogenesis of noncentrosomal, Golgi-associated microtubules through recruitment of CLASP1 and CLASP2. {ECO:0000269|PubMed:16885419, ECO:0000269|PubMed:17488291, ECO:0000269|PubMed:17543864}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11149944}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;colon;parathyroid;choroid;fovea centralis;uterus;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;small intestine;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;amnion;head and neck;kidney;stomach; superior cervical ganglion;medulla oblongata;occipital lobe;subthalamic nucleus;prefrontal cortex;globus pallidus;caudate nucleus;pons;cingulate cortex;parietal lobe; 0.13750 0.11200 -1.627912093 2.860344421 302.85096 3.70836 GCC2-AS1 . . . GCC2 antisense RNA 1 . . . . . . . . . . . GCDH 0.335283401044871 0.664079570397029 0.000637028558099355 glutaryl-CoA dehydrogenase FUNCTION: Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive. {ECO:0000269|PubMed:17176108, ECO:0000269|PubMed:6423663, ECO:0000269|PubMed:8541831}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in fibroblasts and liver.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;cerebellum;thymus; liver;ciliary ganglion;atrioventricular node; 0.08086 0.68440 -0.510624372 21.65015334 70.65549 1.74949 GCFC2 6.26945536555853e-12 0.597110715844345 0.402889284149386 GC-rich sequence DNA-binding factor 2 FUNCTION: Factor that represses transcription. It binds to the GC- rich sequences (5'-GCGGGGC-3') present in the epidermal growth factor receptor, beta-actin, and calcium-dependent protease promoters. Involved in pre-mRNA splicing through regulating spliceosome C complex formation. May play a role during late-stage splicing events and turnover of excised inrons. {ECO:0000269|PubMed:24304693}.; . TISSUE SPECIFICITY: Widely expressed in tissues and cell lines.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;kidney;stomach; subthalamic nucleus;superior cervical ganglion;testis - interstitial;ciliary ganglion;skeletal muscle; 0.08010 0.18863 1.512041961 95.47062987 2091.71134 8.42618 GCG 0.0772034616847316 0.872396144601012 0.0504003937142559 glucagon FUNCTION: Glucagon plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes.; FUNCTION: GLP-2 stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. The gastrointestinal tract, from the stomach to the colon is the principal target for GLP-2 action. Plays a key role in nutrient homeostasis, enhancing nutrient assimilation through enhanced gastrointestinal function, as well as increasing nutrient disposal. Stimulates intestinal glucose transport and decreases mucosal permeability.; FUNCTION: Glicentin may modulate gastric acid secretion and the gastro-pyloro-duodenal activity. May play an important role in intestinal mucosal growth in the early period of life.; . TISSUE SPECIFICITY: Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract. GLP-1 and GLP-2 are also secreted in selected neurons in the brain.; . . 0.24832 0.84371 0.03689118 56.64071715 11.36425 0.40978 GCGR 0.452713871338603 0.451050229081489 0.0962358995799088 glucagon receptor FUNCTION: G-protein coupled receptor for glucagon that plays a central role in the regulation of blood glucose levels and glucose homeostasis. Regulates the rate of hepatic glucose production by promoting glycogen hydrolysis and gluconeogenesis. Plays an important role in mediating the responses to fasting. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Promotes activation of adenylate cyclase. Besides, plays a role in signaling via a phosphatidylinositol-calcium second messenger system. {ECO:0000269|PubMed:19657311, ECO:0000269|PubMed:22908259, ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:7507321, ECO:0000269|PubMed:9287038}.; . . . . 0.31375 . 0.194852702 67.03231894 88.80044 2.02268 GCH1 0.942485932944866 0.0572936200565306 0.000220446998603702 GTP cyclohydrolase 1 FUNCTION: Positively regulates nitric oxide synthesis in umbilical vein endothelial cells (HUVECs). May be involved in dopamine synthesis. May modify pain sensitivity and persistence. Isoform GCH-1 is the functional enzyme, the potential function of the enzymatically inactive isoforms remains unknown. {ECO:0000269|PubMed:12176133, ECO:0000269|PubMed:16338639, ECO:0000269|PubMed:17057711, ECO:0000269|PubMed:8068008, ECO:0000269|PubMed:9445252}.; DISEASE: Hyperphenylalaninemia, BH4-deficient, B (HPABH4B) [MIM:233910]: A disease characterized by malignant hyperphenylalaninemia due to tetrahydrobiopterin deficiency, and defective neurotransmission due to depletion of the neurotransmitters dopamine and serotonin. The principal symptoms include: psychomotor retardation, tonicity disorders, convulsions, drowsiness, irritability, abnormal movements, hyperthermia, hypersalivation, and difficulty swallowing. Some patients may present a phenotype of intermediate severity between severe hyperphenylalaninemia and mild dystonia. In this intermediate phenotype, there is marked motor delay, but no mental retardation and only minimal, if any, hyperphenylalaninemia. {ECO:0000269|PubMed:7501255, ECO:0000269|PubMed:9667588}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dystonia, dopa-responsive (DRD) [MIM:128230]: A form of dystonia that responds to L-DOPA treatment without side effects. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. DRD typically presents in childhood with walking problems due to dystonia of the lower limbs and worsening of the dystonia towards the evening. It is characterized by postural and motor disturbances showing marked diurnal fluctuation. Torsion of the trunk is unusual. Symptoms are alleviated after sleep and aggravated by fatigue and exercise. {ECO:0000269|PubMed:10076897, ECO:0000269|PubMed:10208576, ECO:0000269|PubMed:10582612, ECO:0000269|PubMed:10825351, ECO:0000269|PubMed:10987649, ECO:0000269|PubMed:11113234, ECO:0000269|PubMed:12391354, ECO:0000269|PubMed:17101830, ECO:0000269|PubMed:7501255, ECO:0000269|PubMed:7874165, ECO:0000269|PubMed:8852666, ECO:0000269|PubMed:8957022, ECO:0000269|PubMed:9120469, ECO:0000269|PubMed:9328244, ECO:0000269|PubMed:9778264}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In epidermis, expressed predominantly in basal undifferentiated keratinocytes and in some but not all melanocytes (at protein level). {ECO:0000269|PubMed:16778797}.; lymphoreticular;colon;skin;retina;bone marrow;uterus;whole body;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;skeletal muscle;bile duct;breast;lung;adrenal gland;nasopharynx;placenta;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; . 0.29184 0.75661 -0.09720619 46.20193442 11.31874 0.40734 GCHFR 0.0418968845933878 0.65739075852251 0.300712356884102 GTP cyclohydrolase I feedback regulator FUNCTION: Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine. {ECO:0000269|PubMed:16778797}.; . TISSUE SPECIFICITY: In epidermis, expressed predominantly in basal undifferentiated keratinocytes and in some but not all melanocytes (at protein level). {ECO:0000269|PubMed:16778797}.; lymphoreticular;ovary;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;bone;germinal center;brain;tonsil;unclassifiable (Anatomical System);pineal body;muscle;lens;breast;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;stomach; superior cervical ganglion;liver;kidney; 0.16698 0.10138 -0.053113545 49.38664779 2.4231 0.08612 GCK 0.204306172514215 0.793690928856395 0.0020028986293902 glucokinase FUNCTION: Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage.; DISEASE: Familial hyperinsulinemic hypoglycemia 3 (HHF3) [MIM:602485]: Most common cause of persistent hypoglycemia in infancy. Unless early and aggressive intervention is undertaken, brain damage from recurrent episodes of hypoglycemia may occur. {ECO:0000269|PubMed:9435328}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is expressed in pancreas. Isoform 2 and isoform 3 is expressed in liver.; unclassifiable (Anatomical System);lung;whole body;islets of Langerhans;placenta;pituitary gland;testis;germinal center;brain; superior cervical ganglion;prefrontal cortex;skeletal muscle;parietal lobe;cingulate cortex; 0.81260 0.74195 -0.359940251 28.93371078 9.29304 0.34078 GCKR 3.58392509874806e-16 0.0371435948178218 0.962856405182178 glucokinase (hexokinase 4) regulator FUNCTION: Inhibits glucokinase (GCK) by forming an inactive complex with this enzyme. The affinity of GCKR for GCK is modulated by fructose metabolites: GCKR with bound fructose 6- phosphate has increased affinity for GCK, while GCKR with bound fructose 1-phosphate has strongly decreased affinity for GCK and does not inhibit GCK activity. {ECO:0000269|PubMed:23621087, ECO:0000269|PubMed:23733961}.; . TISSUE SPECIFICITY: Found in liver and pancreas. Not detected in muscle, brain, heart, thymus, intestine, uterus, adipose tissue, kidney, adrenal, lung or spleen. {ECO:0000269|PubMed:19643913, ECO:0000269|PubMed:9570959}.; unclassifiable (Anatomical System);lung;liver;testis;spleen;skeletal muscle; superior cervical ganglion;liver;atrioventricular node;skeletal muscle; 0.29708 0.18718 -0.727458245 14.19556499 151.76469 2.69433 GCLC 0.815078354570402 0.184920046366986 1.59906261202927e-06 glutamate-cysteine ligase catalytic subunit . DISEASE: Hemolytic anemia due to gamma-glutamylcysteine synthetase deficiency (HAGGSD) [MIM:230450]: A disease characterized by hemolytic anemia, glutathione deficiency, myopathy, late-onset spinocerebellar degeneration, and peripheral neuropathy. {ECO:0000269|PubMed:10515893, ECO:0000269|PubMed:10733484, ECO:0000269|PubMed:12663448}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;oesophagus;larynx;gum;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; amygdala;occipital lobe;fetal liver;superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.68568 0.65219 -0.468351206 23.42533616 93.14803 2.07607 GCLM 0.414918212155138 0.576947854949899 0.00813393289496279 glutamate-cysteine ligase modifier subunit . . TISSUE SPECIFICITY: In all tissues examined. Highest levels in skeletal muscle.; . . 0.19946 0.34757 -0.163345027 41.24793583 8.69887 0.31970 GCM1 0.988333939596922 0.0116617975838278 4.26281925064158e-06 glial cells missing homolog 1 FUNCTION: Transcription factor that is necessary for placental development. Binds to the trophoblast-specific element 2 (TSE2) of the aromatase gene enhancer.; . TISSUE SPECIFICITY: Placenta specific.; uterus;whole body;ovary;heart;tongue;placenta;parathyroid;head and neck;kidney;skin; dorsal root ganglion;placenta;ciliary ganglion;trigeminal ganglion; 0.17303 0.18733 -0.091746757 46.91554612 45.12276 1.28999 GCM2 0.00140119057160784 0.964484631912937 0.0341141775154555 glial cells missing homolog 2 FUNCTION: Probable transcriptional regulator.; DISEASE: Hypoparathyroidism, familial isolated (FIH) [MIM:146200]: A disorder characterized by hypocalcemia and hyperphosphatemia due to inadequate secretion of parathyroid hormone. Clinical features include seizures, tetany and cramps. {ECO:0000269|PubMed:15728199, ECO:0000269|PubMed:15863676, ECO:0000269|PubMed:20190276, ECO:0000269|PubMed:20463099, ECO:0000269|Ref.3}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.26903 0.14879 1.155610133 92.59259259 242.64121 3.36214 GCN1 . . . GCN1, eIF2 alpha kinase activator homolog FUNCTION: Acts as a positive activator of the EIF2AK4/GCN2 protein kinase activity in response to amino acid starvation. Forms a complex with EIF2AK4/GCN2 on translating ribosomes; during this process, GCN1 seems to act as a chaperone to facilitate delivery of uncharged tRNAs that enter the A site of ribosomes to the tRNA- binding domain of EIF2AK4/GCN2, and hence stimulating EIF2AK4/GCN2 kinase activity. Participates in the repression of global protein synthesis and in gene-specific mRNA translation activation, such as the transcriptional activator ATF4, by promoting the EIF2AK4/GCN2-mediated phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) on 'Ser-52', and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion. {ECO:0000250|UniProtKB:E9PVA8, ECO:0000250|UniProtKB:P33892}.; . TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:9039502). Expressed in skeletal muscules, ovary and testis (PubMed:9234705). {ECO:0000269|PubMed:9039502, ECO:0000269|PubMed:9234705}.; . . 0.20989 0.39107 -3.766903034 0.235904695 . . GCNT1 0.0665766367898709 0.871276331127133 0.0621470320829958 glucosaminyl (N-acetyl) transferase 1, core 2 FUNCTION: Glycosyltransferase that catalyzes the transfer of an N- acetylglucosamine moiety onto mucin-type core 1 O-glycan to form the branched mucin-type core 2 O-glycan. Mucin-type core 2 O- glycans play an important role in leukocyte extravasation as they serve as scaffolds for the display of the selectin ligand sialyl Lewis X by leukocytes. {ECO:0000269|PubMed:23027862}.; . TISSUE SPECIFICITY: Highly expressed in activated T-lymphocytes and myeloid cells.; . . 0.09236 0.15899 0.374860183 75.43052607 1448.65204 7.10058 GCNT1P1 . . . glucosaminyl (N-acetyl) transferase 1, core 2 pseudogene 1 . . . . . . . . . . . GCNT1P2 . . . glucosaminyl (N-acetyl) transferase 1, core 2 pseudogene 2 . . . . . . . . . . . GCNT1P3 . . . glucosaminyl (N-acetyl) transferase 1, core 2 pseudogene 3 . . . . . . . . . . . GCNT1P4 . . . glucosaminyl (N-acetyl) transferase 1, core 2 pseudogene 4 . . . . . . . . . . . GCNT1P5 . . . glucosaminyl (N-acetyl) transferase 1, core 2 pseudogene 5 . . . . . . . . . . . GCNT2 0.0193977222149499 0.90053707550264 0.0800652022824106 glucosaminyl (N-acetyl) transferase 2, I-branching enzyme (I blood group) FUNCTION: Branching enzyme that converts linear into branched poly-N-acetyllactosaminoglycans. Introduces the blood group I antigen during embryonic development. It is closely associated with the development and maturation of erythroid cells. The expression of the blood group I antigen in erythrocytes is determined by isoform C.; DISEASE: Cataract 13, with adult i phenotype (CTRCT13) [MIM:116700]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT13 is associated with the rare adult i phenotype, in which adult red blood cells are rich in i antigen and contain low levels of I antigen. {ECO:0000269|PubMed:11739194}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In the adult, highly expressed in prostate and to a lesser extent in small intestine and colon. Barely detected in heart, brain, kidney and pancreas. No expression in placenta, lung, liver, skeletal muscle, spleen, thymus, testis, ovary and peripheral blood leukocytes. In fetus, highly expressed in brain and to a lesser extent in lung and kidney. Barely detected in liver. {ECO:0000269|PubMed:12424189, ECO:0000269|PubMed:9405606}.; unclassifiable (Anatomical System);ovary;blood;parathyroid;skeletal muscle;prostate;lung;placenta;bone;liver;spleen;germinal center;kidney;brain;mammary gland; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.21275 0.15862 -1.300731691 4.948100967 83.70152 1.94658 GCNT3 4.04466927083348e-09 0.0543994349703735 0.945600560984957 glucosaminyl (N-acetyl) transferase 3, mucin type FUNCTION: Glycosyltransferase that can synthesize all known mucin beta 6 N-acetylglucosaminides. Mediates core 2 and core 4 O-glycan branching, 2 important steps in mucin-type biosynthesis. Has also I-branching enzyme activity by converting linear into branched poly-N-acetyllactosaminoglycans, leading to introduce the blood group I antigen during embryonic development. {ECO:0000269|PubMed:9915862}.; . TISSUE SPECIFICITY: Primarily expressed in mucus-secreting tissues. Expressed in colon, kidney, small intestine, trachea, and stomach, where mucin is produced. {ECO:0000269|PubMed:17303715, ECO:0000269|PubMed:9915862}.; . . 0.11221 0.09788 0.446457185 77.97829677 58.26865 1.54572 GCNT4 0.0212350420721519 0.907184787359645 0.071580170568203 glucosaminyl (N-acetyl) transferase 4, core 2 FUNCTION: Glycosyltransferase that mediates core 2 O-glycan branching, an important step in mucin-type biosynthesis. Does not have core 4 O-glycan or I-branching enzyme activity. {ECO:0000269|PubMed:10753916}.; . TISSUE SPECIFICITY: Predominantly expressed in thymus. Weakly expressed in pancreas, peripheral blood leukocytes, placenta, small intestine and stomach. Barely detectable in liver, spleen, lung and lymph node. {ECO:0000269|PubMed:10753916}.; placenta; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.18493 . 0.328949044 73.41354093 3641.88978 11.71739 GCNT6 . . . glucosaminyl (N-acetyl) transferase 6 FUNCTION: Glycosyltransferase. {ECO:0000250}.; . . . . 0.03395 . . . 400.8076 4.19985 GCNT7 . . . glucosaminyl (N-acetyl) transferase family member 7 FUNCTION: Glycosyltransferase. {ECO:0000250}.; . . unclassifiable (Anatomical System);testis;kidney; superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion; 0.03282 . . . 752.86612 5.44146 GCOM1 3.95491169061382e-09 0.781567100660043 0.218432895385046 GRINL1A complex locus 1 FUNCTION: Plays a role in cellular signaling via Rho-related GTP- binding proteins and subsequent activation of transcription factor SRF (By similarity). Targets TJP1 to cell junctions. In cortical neurons, may play a role in glutaminergic signal transduction through interaction with the NMDA receptor subunit GRIN1 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in heart, liver, skeletal muscle, placenta, small intestine, lung, prostate and testis. {ECO:0000269|PubMed:15233991, ECO:0000269|PubMed:20093627}.; myocardium;colon;skin;uterus;prostate;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;skeletal muscle;pancreas;lung;epididymis;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;stomach;aorta; amygdala;uterus;occipital lobe;subthalamic nucleus;superior cervical ganglion;prefrontal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; . 0.10192 0.622829232 83.47487615 194.4878 3.02275 GCOM2 . . . GRINL1B complex locus 2 (pseudogene) . . . . . . 0.10192 . . . . GCSAM 0.0985013069335167 0.866552058214434 0.0349466348520496 germinal center-associated, signaling and motility FUNCTION: Involved in the negative regulation of lymphocyte motility. It mediates the migration-inhibitory effects of IL6. Serves as a positive regulator of the RhoA signaling pathway. Enhancement of RhoA activation results in inhibition of lymphocyte and lymphoma cell motility by activation of its downstream effector ROCK. Is a regulator of B-cell receptor signaling, that acts through SYK kinase activation. {ECO:0000269|PubMed:17823310, ECO:0000269|PubMed:20844236, ECO:0000269|PubMed:23299888}.; . TISSUE SPECIFICITY: Expressed in diffuse large B-cell lymphoma (DLBCL) and several germinal center (GC)-like lymphoma cell lines (at protein level). Highly expressed in normal GC lymphocytes and GC-derived malignancies. Expressed in thymus and spleen. {ECO:0000269|PubMed:12509382, ECO:0000269|PubMed:12819018, ECO:0000269|PubMed:15677569}.; . . 0.03022 0.07327 -0.449946534 24.00330267 16.47287 0.58303 GCSAML 0.0357958598740132 0.829722090439499 0.134482049686488 germinal center-associated, signaling and motility-like . . . . . 0.08205 . 0.325313577 73.11276244 334.62249 3.88723 GCSAML-AS1 . . . GCSAML antisense RNA 1 . . . . . . . . . . . GCSH 0.0197283428790772 0.740491496085807 0.239780161035116 glycine cleavage system protein H (aminomethyl carrier) FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The H protein (GCSH) shuttles the methylamine group of glycine from the P protein (GLDC) to the T protein (GCST).; DISEASE: Non-ketotic hyperglycinemia (NKH) [MIM:605899]: Autosomal recessive disease characterized by accumulation of a large amount of glycine in body fluid and by severe neurological symptoms. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;larynx;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cerebellum cortex;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.74905 0.16387 0.191216164 66.57230479 356.43965 3.99620 GCSHP1 . . . glycine cleavage system protein H (aminomethyl carrier) pseudogene 1 . . . . . . . . . . . GCSHP2 . . . glycine cleavage system protein H (aminomethyl carrier) pseudogene 2 . . . . . . . . . . . GCSHP3 . . . glycine cleavage system protein H (aminomethyl carrier) pseudogene 3 . . . . . . . . . . . GCSHP4 . . . glycine cleavage system protein H (aminomethyl carrier) pseudogene 4 . . . . . . . . . . . GCSHP5 . . . glycine cleavage system protein H pseudogene 5 . . . . . . . . . . . GCY . . . growth control, Y chromosome influenced . . . . . . . . . . . GDA 0.998845432686572 0.00115456427413287 3.039294897943e-09 guanine deaminase FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia. {ECO:0000250}.; . . unclassifiable (Anatomical System);amygdala;small intestine;tongue;islets of Langerhans;hypothalamus;oral cavity;colon;breast;lung;frontal lobe;endometrium;bone;placenta;liver;head and neck;cervix;kidney;brain;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.44628 0.28214 0.018483465 55.44939844 101.51403 2.18156 GDAP1 0.000184528849113524 0.894311985244708 0.105503485906178 ganglioside induced differentiation associated protein 1 FUNCTION: Regulates the mitochondrial network by promoting mitochondrial fission. {ECO:0000269|PubMed:16172208}.; DISEASE: Charcot-Marie-Tooth disease 4A (CMT4A) [MIM:214400]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot- Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie-Tooth disease are designated CMT4. CMT4A is a severe form characterized by early age of onset and rapid progression leading to inability to walk in late childhood or adolescence. {ECO:0000269|PubMed:11743579, ECO:0000269|PubMed:12601710, ECO:0000269|PubMed:15772096, ECO:0000269|PubMed:16172208}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease, axonal, with vocal cord paresis, autosomal recessive (CMT2RV) [MIM:607706]: A form of Charcot-Marie-Tooth disease characterized by the association of axonal neuropathy with vocal cord paresis. Charcot-Marie-Tooth disease is a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. {ECO:0000269|PubMed:12868504}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease 2K (CMT2K) [MIM:607831]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. Charcot-Marie-Tooth disease type 2K onset is in early childhood (younger than 3 years). This phenotype is characterized by foot deformities, kyphoscoliosis, distal limb muscle weakness and atrophy, areflexia, and diminished sensation in the lower limbs. Weakness in the upper limbs is observed in the first decade, with clawing of the fingers. Inheritance can be autosomal dominant or recessive. {ECO:0000269|PubMed:22206013}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease, recessive, intermediate type, A (CMTRIA) [MIM:608340]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Recessive intermediate forms of Charcot-Marie-Tooth disease are characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. {ECO:0000269|PubMed:12499475, ECO:0000269|PubMed:12566285, ECO:0000269|PubMed:15772096, ECO:0000269|PubMed:16172208}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in whole brain and spinal cord. Predominant expression in central tissues of the nervous system not only in neurons but also in Schwann cells. {ECO:0000269|PubMed:11743580, ECO:0000269|PubMed:16172208}.; unclassifiable (Anatomical System);lung;frontal lobe;ovary;islets of Langerhans;hypothalamus;hippocampus;colon;brain;bladder;skeletal muscle;bone marrow; amygdala;subthalamic nucleus;occipital lobe;cerebellum peduncles;ciliary ganglion;trigeminal ganglion; 0.17410 0.16319 -0.692458599 14.96815287 24.90016 0.81756 GDAP1L1 0.353968502367603 0.633213776614276 0.0128177210181204 ganglioside induced differentiation associated protein 1-like 1 . . . unclassifiable (Anatomical System);heart;ovary;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;lung;frontal lobe;placenta;macula lutea;hippocampus;visual apparatus;testis;brain;aorta; superior cervical ganglion;fetal brain;temporal lobe;skeletal muscle; 0.78590 0.11210 -0.157884861 42.05590941 114.53628 2.33164 GDAP2 8.51357562104278e-05 0.996460847012528 0.00345401723126165 ganglioside induced differentiation associated protein 2 . . . . . 0.18506 . -0.602450568 17.91106393 37.23143 1.10998 GDE1 4.09186346553975e-05 0.621672719734795 0.378286361630549 glycerophosphodiester phosphodiesterase 1 FUNCTION: Has glycerophosphoinositol phosphodiesterase activity. Has little or no activity towards glycerophosphocholine. GDE1 activity can be modulated by G-protein signaling pathways (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10760272}.; lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;brain;heart;cartilage;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;amnion;head and neck;kidney;stomach; whole brain;amygdala;occipital lobe;thalamus;caudate nucleus;parietal lobe; 0.15410 0.10770 -0.249709319 35.74545883 49.51969 1.37692 GDF1 0.544923744446604 0.400027863976694 0.0550483915767017 growth differentiation factor 1 FUNCTION: May mediate cell differentiation events during embryonic development.; DISEASE: Transposition of the great arteries dextro-looped 3 (DTGA3) [MIM:613854]: A congenital heart defect consisting of complete inversion of the great vessels, so that the aorta incorrectly arises from the right ventricle and the pulmonary artery incorrectly arises from the left ventricle. This creates completely separate pulmonary and systemic circulatory systems, an arrangement that is incompatible with life. The presence or absence of associated cardiac anomalies defines the clinical presentation and surgical management of patients with transposition of the great arteries. {ECO:0000269|PubMed:17924340}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Tetralogy of Fallot (TOF) [MIM:187500]: A congenital heart anomaly which consists of pulmonary stenosis, ventricular septal defect, dextroposition of the aorta (aorta is on the right side instead of the left) and hypertrophy of the right ventricle. In this condition, blood from both ventricles (oxygen-rich and oxygen-poor) is pumped into the body often causing cyanosis. {ECO:0000269|PubMed:17924340}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Right atrial isomerism (RAI) [MIM:208530]: A severe complex congenital heart defect resulting from embryonic disruption of proper left-right axis determination. RAI is usually characterized by complete atrioventricular septal defect with a common atrium and univentricular AV connection, total anomalous pulmonary drainage, and transposition or malposition of the great arteries. Affected individuals present at birth with severe cardiac failure. Other associated abnormalities include bilateral trilobed lungs, midline liver, and asplenia, as well as situs inversus affecting other organs. {ECO:0000269|PubMed:20413652}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the brain.; unclassifiable (Anatomical System);amygdala;medulla oblongata;frontal lobe;nervous;islets of Langerhans;hypothalamus;colon;brain;stomach;retina; whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;testis;cingulate cortex;parietal lobe;cerebellum; 0.13118 0.12149 . . 947.71674 5.96281 GDF2 0.0860071410894876 0.870999455908717 0.0429934030017957 growth differentiation factor 2 FUNCTION: Potent circulating inhibitor of angiogenesis. Could be involved in bone formation. Signals through the type I activin receptor ACVRL1 but not other Alks. Signaling through SMAD1 in endothelial cells requires TGF-beta coreceptor endoglin/ENG. {ECO:0000269|PubMed:18309101, ECO:0000269|PubMed:22799562, ECO:0000269|PubMed:23300529}.; DISEASE: Telangiectasia, hereditary hemorrhagic, 5 (HHT5) [MIM:615506]: A multisystemic vascular dysplasia leading to dilation of permanent blood vessels and arteriovenous malformations of skin, mucosa, and viscera. The disease is characterized by recurrent epistaxis and gastro-intestinal hemorrhage. Visceral involvement includes arteriovenous malformations of the lung, liver, and brain. {ECO:0000269|PubMed:23972370}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . liver; . 0.05516 0.22144 -0.380166007 27.88393489 58.06389 1.54129 GDF3 0.0812132152427739 0.871975557728448 0.046811227028778 growth differentiation factor 3 . DISEASE: Klippel-Feil syndrome 3, autosomal dominant (KFS3) [MIM:613702]: A skeletal disorder characterized by congenital fusion of cervical vertebrae. It is due to a failure in the normal segmentation of vertebrae during the early weeks of fetal development. The clinical triad consists of short neck, low posterior hairline, and limited neck movement. {ECO:0000269|PubMed:19864492}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Microphthalmia, isolated, with coloboma, 6 (MCOPCB6) [MIM:613703]: A disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues. Ocular abnormalities like opacities of the cornea and lens, scaring of the retina and choroid, and other abnormalities may also be present. Ocular colobomas are a set of malformations resulting from abnormal morphogenesis of the optic cup and stalk, and the fusion of the fetal fissure (optic fissure). {ECO:0000269|PubMed:19864492}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Microphthalmia, isolated, 7 (MCOP7) [MIM:613704]: A disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues. Ocular abnormalities like opacities of the cornea and lens, scaring of the retina and choroid, and other abnormalities may also be present. {ECO:0000269|PubMed:19864492}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);epididymis;kidney;brain; superior cervical ganglion;pons; 0.32466 0.11410 0.41713504 76.95800896 1188.69549 6.53835 GDF5 0.923194898928876 0.0767115511028565 9.35499682675929e-05 growth differentiation factor 5 FUNCTION: Growth factor involved in bone and cartilage formation. During cartilage development regulates differentiation of chondrogenic tissue through two pathways. Firstly, positively regulates differentiation of chondrogenic tissue through its binding of high affinity with BMPR1B and of less affinity with BMPR1A, leading to induction of SMAD1-SMAD5-SMAD8 complex phosphorylation and then SMAD protein signaling transduction (PubMed:24098149, PubMed:21976273, PubMed:15530414, PubMed:25092592). Secondly, negatively regulates chondrogenic differentiation through its interaction with NOG (PubMed:21976273). Required to prevent excessive muscle loss upon denervation. This function requires SMAD4 and is mediated by phosphorylated SMAD1/5/8 (By similarity). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). {ECO:0000250|UniProtKB:P43027, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:15530414, ECO:0000269|PubMed:19229295, ECO:0000269|PubMed:19956691, ECO:0000269|PubMed:21976273, ECO:0000269|PubMed:24098149, ECO:0000269|PubMed:25092592}.; DISEASE: Acromesomelic chondrodysplasia, Hunter-Thompson type (AMDH) [MIM:201250]: An autosomal recessive form of dwarfism. Patients have limb abnormalities, with the middle and distal segments being most affected and the lower limbs more affected than the upper. AMDH is characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet. {ECO:0000269|PubMed:8589725}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Brachydactyly C (BDC) [MIM:113100]: A form of brachydactyly. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. Brachydactyly type C is characterized by deformity of the middle and proximal phalanges of the second and third fingers, sometimes with hypersegmentation of the proximal phalanx. The ring finger may be essentially normal and project beyond the others. {ECO:0000269|PubMed:14735582, ECO:0000269|PubMed:22828468, ECO:0000269|PubMed:25092592, ECO:0000269|PubMed:25820810}. Note=The disease is caused by mutations affecting the gene represented in this entry. Some BDC patients with GDF5 mutations also manifest clinical features of ASPED angel-shaped phalango- epiphyseal dysplasia (ASPED), an autosomal dominant skeletal abnormality characterized by a typical angel-shaped phalanx, brachydactyly, specific radiological findings, abnormal dentition, hip dysplasia, and delayed bone age. This suggests that BDC and ASPED are part of the same clinical spectrum (PubMed:22828468). {ECO:0000269|PubMed:22828468}.; DISEASE: Du Pan syndrome (DPS) [MIM:228900]: Rare autosomal recessive condition characterized by absence of the fibulae and severe acromesomelic limb shortening with small, non-functional toes. Although milder, the phenotype resembles the autosomal recessive Hunter-Thompson and Grebe types of acromesomelic chondrodysplasia. {ECO:0000269|PubMed:12121354, ECO:0000269|PubMed:16222676, ECO:0000269|PubMed:18629880}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Symphalangism, proximal 1B (SYM1B) [MIM:615298]: A disease characterized by the hereditary absence of the proximal interphalangeal joints. Distal interphalangeal joints are less frequently involved and metacarpophalangeal joints are rarely affected whereas carpal bone malformation and fusion are common. In the lower extremities, tarsal bone coalition is common. Conductive hearing loss is seen and is due to fusion of the stapes to the petrous part of the temporal bone. {ECO:0000269|PubMed:16127465, ECO:0000269|PubMed:16892395, ECO:0000269|PubMed:18283415}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multiple synostoses syndrome 2 (SYNS2) [MIM:610017]: A bone disease characterized by multiple progressive joint fusions that commonly involve proximal interphalangeal, tarsal-carpal, humeroradial and cervical spine joints. Additional features can include progressive conductive deafness and facial dysmorphism. {ECO:0000269|PubMed:16532400, ECO:0000269|PubMed:19956691, ECO:0000269|PubMed:21976273, ECO:0000269|PubMed:24098149, ECO:0000269|Ref.16}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Brachydactyly A2 (BDA2) [MIM:112600]: A form of brachydactyly. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. In brachydactyly type A2 shortening of the middle phalanges is confined to the index finger and the second toe, all other digits being more or less normal. Because of a rhomboid or triangular shape of the affected middle phalanx, the end of the second finger usually deviates radially. {ECO:0000269|PubMed:16127465, ECO:0000269|PubMed:18203755, ECO:0000269|PubMed:21976273}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteoarthritis 5 (OS5) [MIM:612400]: A degenerative disease of the joints characterized by degradation of the hyaline articular cartilage and remodeling of the subchondral bone with sclerosis. Clinical symptoms include pain and joint stiffness often leading to significant disability and joint replacement. {ECO:0000269|PubMed:17384641}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Brachydactyly A1, C (BDA1C) [MIM:615072]: A form of brachydactyly type A1. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. Brachydactyly type A1 is characterized by middle phalanges of all the digits rudimentary or fused with the terminal phalanges. The proximal phalanges of the thumbs and big toes are short. {ECO:0000269|PubMed:20683927, ECO:0000269|PubMed:24098149}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in long bones during embryonic development. Expressed in monocytes (at protein level). {ECO:0000269|PubMed:11276205}.; . . 0.49057 0.32768 -0.067881249 48.69072895 256.70735 3.44774 GDF5OS 0.0423623916485043 0.846702761048564 0.110934847302932 growth differentiation factor 5 opposite strand . . . . . 0.07541 . . . 2684.12599 9.73888 GDF6 0.910386172281508 0.0889375818968724 0.000676245821619169 growth differentiation factor 6 FUNCTION: Growth factor that controls proliferation and cellular differentiation in the retina and bone formation. Plays a key role in regulating apoptosis during retinal development. Establishes dorsal-ventral positional information in the retina and controls the formation of the retinotectal map. Required for normal formation of bones and joints in the limbs, skull, and axial skeleton. Plays a key role in establishing boundaries between skeletal elements during development. May signal through the growth factor receptors subunits BMPR1A, BMPR1B, BMPR2 and ACVR2A. {ECO:0000269|PubMed:23307924}.; DISEASE: Klippel-Feil syndrome 1, autosomal dominant (KFS1) [MIM:118100]: A skeletal disorder characterized by congenital fusion of cervical vertebrae. It is due to a failure in the normal segmentation of vertebrae during the early weeks of fetal development. The clinical triad consists of short neck, low posterior hairline, and limited neck movement. Deafness is a feature in some cases and may be of sensorineural, conductive, or mixed type. {ECO:0000269|PubMed:18425797, ECO:0000269|PubMed:19129173}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving GDF6 has been found in a patient with Klippel-Feil syndrome (KFS). Paracentric inv(8)(q22;2q23.3). {ECO:0000269|PubMed:18425797}.; DISEASE: Microphthalmia, isolated, 4 (MCOP4) [MIM:613094]: A disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues. Ocular abnormalities like opacities of the cornea and lens, scaring of the retina and choroid, and other abnormalities may also be present. {ECO:0000269|PubMed:19129173}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leber congenital amaurosis 17 (LCA17) [MIM:615360]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or almost absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:23307924}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);bone;placenta;liver;testis;spleen; . 0.53569 0.21387 . . 56.37434 1.50848 GDF7 0.778067351749562 0.214683846723988 0.00724880152645024 growth differentiation factor 7 FUNCTION: May play an active role in the motor area of the primate neocortex. {ECO:0000250}.; . . blood;kidney; . 0.07912 0.10303 . . 405.95773 4.22445 GDF9 1.19472233006091e-05 0.370783547694731 0.629204505081968 growth differentiation factor 9 FUNCTION: Required for ovarian folliculogenesis. Promotes primordial follicle development. Stimulates granulosa cell proliferation. Promotes cell transition from G0/G1 to S and G2/M phases, through an increase of CCND1 and CCNE1 expression, and RB1 phosphorylation. It regulates STAR expression and cAMP-dependent progesterone release in granulosa and thecal cells. Attenuates the suppressive effects of activin A on STAR expression and progesterone production by increasing the expression of inhibin B. It suppresses FST and FSTL3 production in granulosa-lutein cells. {ECO:0000269|PubMed:12050262, ECO:0000269|PubMed:19366876, ECO:0000269|PubMed:20660033, ECO:0000269|PubMed:21632818, ECO:0000269|PubMed:21829661}.; DISEASE: Note=Altered GDF9 function may be involved in ovarian disorders. Rare variants in GDF9 have been found in patients with premature ovarian failure and mothers of dizygotic twins. {ECO:0000269|PubMed:16954162}.; TISSUE SPECIFICITY: Expressed in ovarian granulosa cells. Present in oocytes of primary follicles (at protein level). {ECO:0000269|PubMed:10443672, ECO:0000269|PubMed:12050262}.; unclassifiable (Anatomical System);lung;adrenal cortex;testis;brain; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.12610 . -0.023789244 52.09365416 93.11522 2.07499 GDF10 0.308234424584061 0.673590677905821 0.018174897510118 growth differentiation factor 10 FUNCTION: Growth factor involved in osteogenesis and adipogenesis. Plays an inhibitory role in the process of osteoblast differentiation via SMAD2/3 pathway. Plays an inhibitory role in the process of adipogenesis. {ECO:0000250|UniProtKB:P97737}.; . TISSUE SPECIFICITY: Expressed in femur, brain, lung, skeletal muscle, pancreas and testis. {ECO:0000269|PubMed:8670277}.; prostate;lung;whole body;cartilage;cochlea;thyroid;testis;spleen;head and neck;brain;pineal gland;retina; superior cervical ganglion; 0.72718 0.17481 0.084621747 60.31493277 102.79492 2.19148 GDF11 0.963838119160384 0.0360926191000265 6.92617395895424e-05 growth differentiation factor 11 FUNCTION: Secreted signal that acts globally to specify positional identity along the anterior/posterior axis during development. Play critical roles in patterning both mesodermal and neural tissues and in establishing the skeletal pattern.; . . unclassifiable (Anatomical System);cartilage;colon;blood;parathyroid;choroid;bone marrow;uterus;larynx;liver;testis;head and neck;spleen;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.59882 0.18619 -0.05129383 49.75819769 12.40367 0.44998 GDF15 0.000282486503125805 0.557508407624453 0.442209105872421 growth differentiation factor 15 . . TISSUE SPECIFICITY: Highly expressed in placenta, with lower levels in prostate and colon and some expression in kidney.; unclassifiable (Anatomical System);ovary;islets of Langerhans;muscle;colon;parathyroid;choroid;skin;uterus;pancreas;prostate;lung;endometrium;trabecular meshwork;placenta;visual apparatus;amnion;liver;testis;spleen;kidney;brain;mammary gland;stomach; prostate;lung;placenta;kidney;trigeminal ganglion; 0.32866 0.36016 0.72761005 86.08162302 2898.22579 10.20180 GDI1 0.987884008546527 0.0121113141965237 4.67725694904445e-06 GDP dissociation inhibitor 1 FUNCTION: Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Promotes the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Promotes the dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes. {ECO:0000269|PubMed:23815289}.; . TISSUE SPECIFICITY: Brain; predominant in neural and sensory tissues. {ECO:0000269|PubMed:7543319}.; . . 0.27741 0.18356 -0.427900189 25.14744043 4.70588 0.16936 GDI2 0.98715482475951 0.01284408207637 1.09316412014177e-06 GDP dissociation inhibitor 2 FUNCTION: Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7543319}.; . . 0.34910 0.20873 -0.115612493 45.12856806 59.51686 1.56510 GDI2P1 . . . GDP dissociation inhibitor 2 pseudogene 1 . . . . . . . . . . . GDI2P2 . . . GDP dissociation inhibitor 2 pseudogene 2 . . . . . . . . . . . GDNF 0.698672292120293 0.284526487364373 0.0168012205153341 glial cell derived neurotrophic factor FUNCTION: Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake. {ECO:0000269|PubMed:8493557}.; DISEASE: Hirschsprung disease 3 (HSCR3) [MIM:613711]: A disorder of neural crest development characterized by absence of enteric ganglia along a variable length of the intestine. It is the most common cause of congenital intestinal obstruction. Early symptoms range from complete acute neonatal obstruction, characterized by vomiting, abdominal distention and failure to pass stool, to chronic constipation in the older child. {ECO:0000269|PubMed:10917288, ECO:0000269|PubMed:8896568, ECO:0000269|PubMed:8896569, ECO:0000269|PubMed:8968758}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Congenital central hypoventilation syndrome (CCHS) [MIM:209880]: Rare disorder characterized by abnormal control of respiration in the absence of neuromuscular or lung disease, or an identifiable brain stem lesion. A deficiency in autonomic control of respiration results in inadequate or negligible ventilatory and arousal responses to hypercapnia and hypoxemia. {ECO:0000269|PubMed:9497256}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In the brain, predominantly expressed in the striatum with highest levels in the caudate and lowest in the putamen. Isoform 2 is absent from most tissues except for low levels in intestine and kidney. Highest expression of isoform 3 is found in pancreatic islets. Isoform 5 is expressed at very low levels in putamen, nucleus accumbens, prefrontal cortex, amygdala, hypothalamus and intestine. Isoform 3 is up-regulated in the middle temporal gyrus of Alzheimer disease patients while isoform 2 shows no change. {ECO:0000269|PubMed:22081608, ECO:0000269|PubMed:7867768}.; . . 0.70999 0.71389 0.193034296 66.82000472 25.41025 0.82937 GDNF-AS1 . . . GDNF antisense RNA 1 (head to head) . . . . . . . . . . . GDPD1 0.00337916957867071 0.986439380697331 0.010181449723998 glycerophosphodiester phosphodiesterase domain containing 1 . . TISSUE SPECIFICITY: Detected in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocytes. {ECO:0000269|PubMed:16147865}.; unclassifiable (Anatomical System);medulla oblongata;testis;colon;brain;artery;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.28757 . -0.185391282 39.67916962 16.98489 0.59880 GDPD2 0.116236323908697 0.882584049052226 0.00117962703907737 glycerophosphodiester phosphodiesterase domain containing 2 FUNCTION: Has glycerophosphoinositol inositolphosphodiesterase activity and specifically hydrolyzes glycerophosphoinositol, with no activity for other substrates such as glycerophosphoinositol 4- phosphate, glycerophosphocholine, glycerophosphoethanolamine, and glycerophosphoserine. Accelerates the program of osteoblast differentiation and growth. May play a role in remodeling of the actin cytoskeleton (By similarity). {ECO:0000250}.; . . . . 0.22680 0.09391 0.062575634 58.74026893 33.31252 1.02902 GDPD3 1.05164952856676e-07 0.534705474293935 0.465294420541112 glycerophosphodiester phosphodiesterase domain containing 3 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;tongue;colon;retina;pancreas;prostate;optic nerve;lung;placenta;hypopharynx;liver;head and neck;spleen;kidney;mammary gland; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.11934 . 0.040529541 57.15380986 159.35257 2.75755 GDPD4 9.33225882341034e-09 0.493225777741361 0.506774212926381 glycerophosphodiester phosphodiesterase domain containing 4 . . . unclassifiable (Anatomical System);lung;testis; . 0.01594 0.03924 1.730733976 96.56758669 6153.15866 16.39078 GDPD5 0.0699851235479039 0.929453908006848 0.00056096844524816 glycerophosphodiester phosphodiesterase domain containing 5 FUNCTION: Promotes neurite formation. Cooperates with PRDX1 to drive postmitotic motor neuron differentiation. The glycerophosphodiester phosphodiesterase activity may be required for its role in neuronal differentiation. May contribute to the osmotic regulation of cellular glycerophosphocholine.; . . unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;blood;choroid;skin;retina;bone marrow;uterus;prostate;bone;placenta;liver;testis;spleen;kidney;brain;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;thalamus;placenta;testis;trigeminal ganglion;cingulate cortex;cerebellum; 0.17042 0.10895 -1.284117362 5.113234253 86.65899 1.98885 GDPGP1 8.68771623153128e-06 0.177969600294333 0.822021711989436 GDP-D-glucose phosphorylase 1 FUNCTION: Specific and highly efficient GDP-D-glucose phosphorylase regulating the levels of GDP-D-glucose in cells. {ECO:0000269|PubMed:21507950}.; . . . . . . 0.843299698 88.37579618 1766.17882 7.76777 GEM 6.12905425295423e-06 0.692436912267599 0.307556958678148 GTP binding protein overexpressed in skeletal muscle FUNCTION: Could be a regulatory protein, possibly participating in receptor-mediated signal transduction at the plasma membrane. Has guanine nucleotide-binding activity but undetectable intrinsic GTPase activity.; . TISSUE SPECIFICITY: Most abundant in thymus, spleen, kidney, lung, and testis. Less abundant in heart, brain, liver and skeletal muscle.; colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;bone;testis;spinal ganglion;artery;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;kidney;mammary gland;stomach;aorta; uterus;superior cervical ganglion;uterus corpus;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.41720 0.11643 -0.005381972 53.50908233 136.3647 2.53818 GEMIN2 0.00660919664980099 0.974736440425215 0.0186543629249839 gem nuclear organelle associated protein 2 FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. {ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:9323129}.; . . unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;colon;parathyroid;skin;uterus;whole body;lung;cochlea;epididymis;placenta;visual apparatus;pituitary gland;liver;testis;spleen;germinal center;kidney; dorsal root ganglion;medulla oblongata;testis - interstitial;superior cervical ganglion;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;appendix;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.13020 0.14380 0.016664174 55.21939137 6043.31497 16.22939 GEMIN2P1 . . . gem nuclear organelle associated protein 2 pseudogene 1 . . . . . . . . . . . GEMIN2P2 . . . gem nuclear organelle associated protein 2 pseudogene 2 . . . . . . . . . . . GEMIN4 1.88601867514957e-07 0.661831928783828 0.338167882614305 gem nuclear organelle associated protein 4 FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. {ECO:0000269|PubMed:18984161}.; . . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;cochlea;endometrium;bone;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;lens;skeletal muscle;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.40154 0.14505 3.398035863 99.45152159 2013.5496 8.26239 GEMIN5 3.13420201203131e-14 0.998386454749945 0.00161354525002356 gem nuclear organelle associated protein 5 FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. GEMIN5 acts as the snRNA-binding protein of the SMN complex. {ECO:0000269|PubMed:11714716, ECO:0000269|PubMed:16857593, ECO:0000269|PubMed:18984161}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach;thymus; superior cervical ganglion;tongue;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin; 0.40307 0.12127 0.218520745 68.13517339 680.51029 5.21504 GEMIN6 0.00259514571092877 0.555029087248596 0.442375767040475 gem nuclear organelle associated protein 6 FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. {ECO:0000269|PubMed:11748230, ECO:0000269|PubMed:18984161}.; . . ovary;salivary gland;intestine;colon;fovea centralis;skin;uterus;prostate;bone;germinal center;bladder;brain;tonsil;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pharynx;blood;lung;epididymis;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.12259 0.11866 -0.073340031 48.11866006 1124.75882 6.39949 GEMIN7 0.347103990823881 0.59655299792132 0.0563430112547986 gem nuclear organelle associated protein 7 FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. {ECO:0000269|PubMed:12065586, ECO:0000269|PubMed:18984161}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;macula lutea;visual apparatus;liver;spleen;kidney;stomach; ciliary ganglion; 0.13525 0.10082 -0.053113545 49.38664779 11.78683 0.42665 GEMIN8 0.906251194519291 0.0929900883745775 0.000758717106131423 gem nuclear organelle associated protein 8 FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. {ECO:0000269|PubMed:17023415, ECO:0000269|PubMed:18984161}.; . . . . 0.09583 0.09376 0.12689526 63.00424628 199.52361 3.05225 GEMIN8P1 . . . gem nuclear organelle associated protein 8 pseudogene 1 . . . . . . . . . . . GEMIN8P2 . . . gem nuclear organelle associated protein 8 pseudogene 2 . . . . . . . . . . . GEMIN8P3 . . . gem nuclear organelle associated protein 8 pseudogene 3 . . . . . . . . . . . GEMIN8P4 . . . gem nuclear organelle associated protein 8 pseudogene 4 . . . . . . . . . . . GEN1 2.85815324965099e-10 0.701305470840361 0.298694528873824 GEN1, Holliday junction 5' flap endonuclease FUNCTION: Endonuclease which resolves Holliday junctions by the introduction of symmetrically related cuts across the junction point, to produce nicked duplex products in which the nicks can be readily ligated. Four-way DNA intermediates, also known as Holliday junctions, are formed during homologous recombination and DNA repair, and their resolution is necessary for proper chromosome segregation. {ECO:0000269|PubMed:19020614}.; . . unclassifiable (Anatomical System);pancreas;lung;frontal lobe;cartilage;ovary;testis;colon;spleen;kidney;germinal center;skeletal muscle;thymus; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.09983 0.09830 2.202964732 98.1304553 1735.74111 7.68619 GET4 0.972149418653344 0.0278143132199995 3.6268126656526e-05 golgi to ER traffic protein 4 FUNCTION: Component of the BAT3 complex, a multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. The complex acts by facilitating TA proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins, and transfers them to ASNA1/TRC40 for targeting. {ECO:0000269|PubMed:20676083}.; . . lymphoreticular;ovary;salivary gland;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pineal body;blood;lens;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.18748 0.09537 -1.265702118 5.237084218 16.67728 0.58735 GFAP 2.22936756487388e-05 0.729609157986731 0.27036854833762 glial fibrillary acidic protein FUNCTION: GFAP, a class-III intermediate filament, is a cell- specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells.; DISEASE: Alexander disease (ALXDRD) [MIM:203450]: A rare disorder of the central nervous system. The most common form affects infants and young children, and is characterized by progressive failure of central myelination, usually leading to death within the first decade. Infants with Alexander disease develop a leukodystrophy with macrocephaly, seizures, and psychomotor retardation. Patients with juvenile or adult forms typically experience ataxia, bulbar signs and spasticity, and a more slowly progressive course. Histologically, Alexander disease is characterized by Rosenthal fibers, homogeneous eosinophilic inclusions in astrocytes. {ECO:0000269|PubMed:11138011, ECO:0000269|PubMed:11567214, ECO:0000269|PubMed:11595337, ECO:0000269|PubMed:12034785, ECO:0000269|PubMed:12034796, ECO:0000269|PubMed:12581808, ECO:0000269|PubMed:12944715, ECO:0000269|PubMed:12975300, ECO:0000269|PubMed:15030911, ECO:0000269|PubMed:15732097, ECO:0000269|PubMed:17043438, ECO:0000269|PubMed:17805552, ECO:0000269|PubMed:17894839, ECO:0000269|PubMed:17934883, ECO:0000269|PubMed:17960815, ECO:0000269|PubMed:18004641, ECO:0000269|PubMed:18079314, ECO:0000269|PubMed:19412928, ECO:0000269|PubMed:20359319, ECO:0000269|PubMed:21917775, ECO:0000269|PubMed:23364391, ECO:0000269|PubMed:23743246, ECO:0000269|PubMed:24742911}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in cells lacking fibronectin. {ECO:0000269|PubMed:1847665}.; unclassifiable (Anatomical System);cerebellum cortex;hypothalamus;pineal body;spinal cord;blood;retina;bone marrow;optic nerve;lung;ganglion;frontal lobe;larynx;visual apparatus;testis;head and neck;dura mater;kidney;mammary gland;pineal gland;brain;cerebellum; amygdala;whole brain;dorsal root ganglion;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.61775 0.95538 0.622829232 83.47487615 423.1212 4.29611 GFER 1.85054644807578e-06 0.075073848062476 0.924924301391076 growth factor, augmenter of liver regeneration FUNCTION: Isoform 1: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re- oxidized by donating electrons to cytochrome c or molecular oxygen.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highest expression in the testis and liver and low expression in the muscle. {ECO:0000269|PubMed:19409522}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;lung;placenta;macula lutea;kidney;stomach;thymus;cerebellum; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex; 0.07200 0.30380 . . 149.48152 2.66593 GFI1 0.029628557114147 0.923974536320879 0.0463969065649736 growth factor independent 1 transcription repressor FUNCTION: Transcription repressor essential for hematopoiesis. Functions in a cell-context and development-specific manner. Binds to 5'-TAAATCAC[AT]GCA-3' in the promoter region of a large number of genes. Component of several complexes, including the EHMT2- GFI1-HDAC1, AJUBA-GFI1-HDAC1 and RCOR-GFI-KDM1A-HDAC complexes, that suppress, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Regulates neutrophil differentiation, promotes proliferation of lymphoid cells, and is required for granulocyte development. Mediates, together with U2AF1L4, the alternative splicing of CD45 and controls T-cell receptor signaling. Regulates the endotoxin- mediated Toll-like receptor (TLR) inflammatory response by antagonizing RELA. Cooperates with CBFA2T2 to regulate ITGB1- dependent neurite growth. Controls cell-cycle progression by repressing CDKNIA/p21 transcription in response to TGFB1 via recruitment of GFI1 by ZBTB17 to the CDKNIA/p21 and CDKNIB promoters. Required for the maintenance of inner ear hair cells. {ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:12778173, ECO:0000269|PubMed:16287849, ECO:0000269|PubMed:17197705, ECO:0000269|PubMed:17646546, ECO:0000269|PubMed:18805794, ECO:0000269|PubMed:19026687, ECO:0000269|PubMed:19164764, ECO:0000269|PubMed:20190815, ECO:0000269|PubMed:20547752, ECO:0000269|PubMed:8754800}.; DISEASE: Neutropenia, severe congenital 2, autosomal dominant (SCN2) [MIM:613107]: A disorder of hematopoiesis characterized by maturation arrest of granulopoiesis at the level of promyelocytes with peripheral blood absolute neutrophil counts below 0.5 x 10(9)/l and early onset of severe bacterial infections. {ECO:0000269|PubMed:12778173}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dominant nonimmune chronic idiopathic neutropenia of adults (NI-CINA) [MIM:607847]: Relatively mild form of neutropenia diagnosed in adults, but predisposing to leukemia in a subset of patients. {ECO:0000269|PubMed:12778173}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . uterus;pancreas;lymph node;lung;heart;nasopharynx;spleen;blood;germinal center;skin;thymus;bone marrow; superior cervical ganglion;globus pallidus;bone marrow; 0.36337 0.28825 0.327131069 73.27199811 206.38015 3.10367 GFI1B 0.0128387744473726 0.953485736343471 0.0336754892091563 growth factor independent 1B transcription repressor FUNCTION: Essential proto-oncogenic transcriptional regulator necessary for development and differentiation of erythroid and megakaryocytic lineages. Component of a RCOR-GFI-KDM1A-HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation. Transcriptional repressor or activator depending on both promoter and cell type context; represses promoter activity of SOCS1 and SOCS3 and thus, may regulate cytokine signaling pathways. Cooperates with GATA1 to repress target gene transcription, such as the apoptosis regulator BCL2L1; GFI1B silencing in leukemic cell lines markedly increase apoptosis rate. Inhibits down- regulation of MYC and MYB as well as the cyclin-dependent kinase inhibitor CDKN1A/P21WAF1 in IL6-treated myelomonocytic cells. Represses expression of GATA3 in T-cell lymphomas and inhibits GATA1-mediated transcription; as GATA1 also mediates erythroid GFI1B transcription, both GATA1 and GFI1B participate in a feedback regulatory pathway controlling the expression of GFI1B gene in erythroid cells. Suppresses GATA1-mediated stimulation of GFI1B promoter through protein interaction. Binds to gamma- satellite DNA and to its own promoter, auto-repressing its own expression. Alters histone methylation by recruiting histone methyltransferase to target genes promoters. Plays a role in heterochromatin formation. {ECO:0000269|PubMed:12351384, ECO:0000269|PubMed:16177182, ECO:0000269|PubMed:16688220, ECO:0000269|PubMed:16782810, ECO:0000269|PubMed:17156408, ECO:0000269|PubMed:17272506, ECO:0000269|PubMed:17420275}.; DISEASE: Bleeding disorder, platelet-type 17 (BDPLT17) [MIM:187900]: An autosomal dominant disorder characterized by increased bleeding tendency due to platelet dysfunction, and associated with macrothrombocytopenia and red cell anisopoikilocytosis. Platelets appear abnormal on light microscopy, while electron microscopy shows a heterogeneous decrease of alpha granules within platelets. Bone marrow biopsy shows increased numbers of abnormal megakaryocytes, suggesting a defect in megakaryopoiesis and platelet production. The severity of bleeding is variable with some affected individuals experiencing spontaneous bleeding while other exhibit only abnormal bleeding with surgery. {ECO:0000269|PubMed:23927492, ECO:0000269|PubMed:24325358}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in bone marrow and fetal liver, but also detectable in fetal spleen, fetal thymus, and testes. Detected in hematopoietic stem cells, erythroblasts, and megakaryocytes. Overexpressed in bone marrow of patients with erythroleukemia and megakaryocytic leukemia as well as in their corresponding leukemic cell lines, and markedly repressed in severe aplastic anemia (SAA). {ECO:0000269|PubMed:12351384, ECO:0000269|PubMed:17156408, ECO:0000269|PubMed:9878267}.; unclassifiable (Anatomical System);lymphoreticular;medulla oblongata;lung;heart;liver;spleen;bone marrow; . 0.45628 0.15819 0.220536484 68.38287332 206.46454 3.10458 GFM1 1.66398179768796e-06 0.999662634160704 0.000335701857498621 G elongation factor, mitochondrial 1 FUNCTION: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A- site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03061, ECO:0000269|PubMed:19716793}.; DISEASE: Combined oxidative phosphorylation deficiency 1 (COXPD1) [MIM:609060]: A mitochondrial disease resulting in early rapidly progressive hepatoencephalopathy. {ECO:0000269|PubMed:15537906, ECO:0000269|PubMed:17160893}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;oesophagus;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;mesenchyma;placenta;macula lutea;duodenum;liver;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;globus pallidus;ciliary ganglion;skeletal muscle; 0.09685 0.16154 0.622829232 83.47487615 654.74789 5.13318 GFM2 1.22849095804363e-08 0.98475563345386 0.01524435426123 G elongation factor, mitochondrial 2 FUNCTION: Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation. {ECO:0000255|HAMAP-Rule:MF_03059, ECO:0000269|PubMed:19716793}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11735030}.; medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;pineal body;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13615 . 1.155610133 92.59259259 7010.51659 17.84819 GFOD1 0.0496190699820879 0.858854470917614 0.0915264591002979 glucose-fructose oxidoreductase domain containing 1 . . . . . 0.10170 0.11809 -0.560178693 19.30879925 23.72415 0.78445 GFOD1-AS1 . . . GFOD1 antisense RNA 1 . . . . . . . . . . . GFOD2 0.0605374338437669 0.868729803954543 0.0707327622016898 glucose-fructose oxidoreductase domain containing 2 FUNCTION: Promotes matrix assembly. {ECO:0000250}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;cartilage;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.22169 0.11262 -0.66859065 15.76433121 34.89686 1.06151 GFPT1 0.974567999344653 0.0254319907991867 9.85616060609691e-09 glutamine--fructose-6-phosphate transaminase 1 FUNCTION: Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes ARNTL/BMAL1 and CRY1.; . TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in skeletal muscle. Not expressed in brain. Seems to be selectively expressed in striated muscle. {ECO:0000269|PubMed:11679416}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;spinal ganglion;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;head and neck;kidney;mammary gland;stomach;aorta; testis - interstitial;testis - seminiferous tubule;testis; 0.70055 0.50919 -0.494039303 22.09247464 28.51548 0.91350 GFPT2 6.62530503452039e-07 0.993862341832059 0.00613699563743707 glutamine-fructose-6-phosphate transaminase 2 FUNCTION: Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.; . TISSUE SPECIFICITY: Highest levels of expression in heart, placenta, and spinal cord.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;heart;cartilage;islets of Langerhans;urinary;adrenal cortex;skeletal muscle;pancreas;lung;placenta;duodenum;mammary gland; dorsal root ganglion;superior cervical ganglion;smooth muscle;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.72946 0.28603 -0.819281839 11.93677754 1696.47592 7.59462 GFRA1 0.119577142602515 0.874942801780411 0.00548005561707404 GDNF family receptor alpha 1 FUNCTION: Receptor for GDNF. Mediates the GDNF-induced autophosphorylation and activation of the RET receptor (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymphoreticular;ovary;salivary gland;pharynx;colon;blood;skin;breast;prostate;lung;visual apparatus;liver;kidney;brain;mammary gland;bladder;stomach; superior cervical ganglion;trigeminal ganglion; 0.28553 0.18412 -0.290161348 33.33923095 1065.87095 6.26119 GFRA2 0.337127994516478 0.648312856854087 0.0145591486294347 GDNF family receptor alpha 2 FUNCTION: Receptor for neurturin. Mediates the NRTN-induced autophosphorylation and activation of the RET receptor. Also able to mediate GDNF signaling through the RET tyrosine kinase receptor.; . TISSUE SPECIFICITY: Isoform 1 is found in both brain and placenta.; unclassifiable (Anatomical System);heart;colon;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;synovium;placenta;bone;macula lutea;visual apparatus;liver;testis;spleen;kidney;brain; whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;subthalamic nucleus;thyroid;prefrontal cortex;ciliary ganglion;trigeminal ganglion;cingulate cortex;skeletal muscle;parietal lobe; 0.31812 0.14483 . . 4026.41733 12.57097 GFRA3 0.0290609621761813 0.960334953148261 0.0106040846755576 GDNF family receptor alpha 3 FUNCTION: Receptor for the glial cell line-derived neurotrophic factor, ARTN (artemin). Mediates the artemin-induced autophosphorylation and activation of the RET receptor tyrosine kinase. {ECO:0000269|PubMed:9883723}.; . TISSUE SPECIFICITY: Widely expressed in adult and fetus which exhibit a similar pattern. Essentially not expressed in the central nervous system, but highly expressed in several sensory and sympathetic ganglia of the peripheral nervous system. Moderate expression in many non-neuronal tissues, particularly those of the digestive and urogenital systems, but high expression in stomach and appendix. Several types of glandular tissues show low expression. Very low or no expression detected in the hematopoietic system. {ECO:0000269|PubMed:9576965}.; unclassifiable (Anatomical System);medulla oblongata;heart;ovary;sympathetic chain;parathyroid;retina;pancreas;prostate;lung;cochlea;endometrium;placenta;liver;iris;spleen; dorsal root ganglion;testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.46091 0.13852 -0.337894035 30.37272942 24.01119 0.79004 GFRA4 0.00834571960566959 0.564979056394245 0.426675224000085 GDNF family receptor alpha 4 FUNCTION: Receptor for persephin. Mediates the GDNF-induced autophosphorylation and activation of the RET receptor. May be important in C-cell development and, in the postnatal development of the adrenal medulla.; . TISSUE SPECIFICITY: Predominantly expressed in the adult thyroid gland. Low levels also found in fetal adrenal and thyroid glands.; . . 0.07295 0.11154 . . 103.68907 2.19995 GFRAL 0.000114819883521722 0.827374461464404 0.172510718652074 GDNF family receptor alpha like . . . . . 0.12290 0.06893 0.951720429 90.06251474 2734.70659 9.85758 GFY . . . golgi associated olfactory signaling regulator FUNCTION: Required for proper function of the olfactory system. May be involved in establishing the acuity of olfactory sensory signaling (By similarity). {ECO:0000250}.; . . . . . . . . 2324.4405 8.92864 GGA1 0.999441827375042 0.000558170069692227 2.555265936311e-09 golgi-associated, gamma adaptin ear containing, ARF binding protein 1 FUNCTION: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF- dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (AC-LL) motif. {ECO:0000269|PubMed:11301005}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;tonsil;heart;cartilage;tongue;nervous;urinary;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.24989 0.14460 -1.107723888 6.829440906 83.21214 1.93928 GGA2 5.0464979295437e-05 0.992697992775674 0.00725154224503047 golgi-associated, gamma adaptin ear containing, ARF binding protein 2 FUNCTION: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF- dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (AC-LL) motif.; . TISSUE SPECIFICITY: Ubiquitously expressed.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;bladder;tonsil;heart;cartilage;spinal cord;urinary;adrenal cortex;pharynx;blood;lens;breast;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;pancreas;lung;nasopharynx;placenta;duodenum;hypopharynx;amnion;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.07789 0.10492 -0.975433863 8.852323661 35.99433 1.08140 GGA3 0.505243695718199 0.494721382098468 3.49221833326312e-05 golgi-associated, gamma adaptin ear containing, ARF binding protein 3 FUNCTION: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF- dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (AC-LL) motif. {ECO:0000269|PubMed:11301005}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;uterus;prostate;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;epididymis;placenta;hippocampus;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.13535 0.13562 -0.639268965 16.70794999 355.14585 3.98562 GGACT . . . gamma-glutamylamine cyclotransferase FUNCTION: Contributes to degradation of proteins cross-linked by transglutaminases. Degrades the cross-link between a lysine and a glutamic acid residue from two proteins that have been cross- linked by transglutaminases. Catalyzes the formation of 5- oxoproline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L-gamma-glutamyl-alpha-amino acid substrates such as L-gamma- glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine. {ECO:0000269|PubMed:20110353}.; . . . . . 0.10482 0.189398298 66.31870724 135.39261 2.53181 GGCT 0.000385990598175728 0.625609338054993 0.374004671346831 gamma-glutamylcyclotransferase FUNCTION: Catalyzes the formation of 5-oxoproline from gamma- glutamyl dipeptides and may play a significant role in glutathione homeostasis. Induces release of cytochrome c from mitochondria with resultant induction of apoptosis. {ECO:0000269|PubMed:16765912, ECO:0000269|PubMed:18515354}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;synovium;thyroid;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; . 0.11261 0.14664 0.103030231 61.2762444 11.24177 0.40539 GGCX 1.19797696730827e-08 0.984216115259621 0.0157838727606091 gamma-glutamyl carboxylase FUNCTION: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide. {ECO:0000269|PubMed:17073445}.; DISEASE: Combined deficiency of vitamin K-dependent clotting factors 1 (VKCFD1) [MIM:277450]: VKCFD leads to a bleeding tendency that is usually reversed by oral administration of vitamin K. {ECO:0000269|PubMed:11071668, ECO:0000269|PubMed:15287948, ECO:0000269|PubMed:9845520}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pseudoxanthoma elasticum-like disorder with multiple coagulation factor deficiency (PXEL-MCFD) [MIM:610842]: Characterized by hyperlaxity of the skin involving the entire body. Important phenotypic differences with classical PXE include much more severe skin laxity with spreading toward the trunk and limbs with thick, leathery skin folds rather than confinement to flexural areas, and no decrease in visual acuity. Moreover, detailed electron microscopic analyzes revealed that alterations of elastic fibers as well as their mineralization are slightly different from those in classic PXE. {ECO:0000269|PubMed:17110937}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;ovary;heart;islets of Langerhans;colon;parathyroid;choroid;skin;skeletal muscle;uterus;prostate;whole body;lung;endometrium;mesenchyma;nasopharynx;bone;placenta;visual apparatus;hypopharynx;liver;cervix;head and neck;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;fetal liver;liver;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.14175 0.13982 -0.705410796 14.77942911 1092.95806 6.32645 GGH 0.578462954904656 0.419218309483568 0.00231873561177647 gamma-glutamyl hydrolase FUNCTION: Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha- glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;gum;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;bile duct;breast;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; fetal liver;superior cervical ganglion;trigeminal ganglion; 0.22475 0.23669 0.305084559 72.22811984 2683.33357 9.73679 GGN 0.134074173944406 0.844825831994218 0.0210999940613754 gametogenetin FUNCTION: May be involved in spermatogenesis. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;testis; . 0.05529 0.11413 . . 2472.2856 9.26586 GGNBP1 . . . gametogenetin binding protein 1 (pseudogene) FUNCTION: May be involved in spermatogenesis. {ECO:0000250}.; . . . . 0.07374 0.08696 . . 24.37073 0.80177 GGNBP2 0.99992911200978 7.08879868298858e-05 3.39038078995991e-12 gametogenetin binding protein 2 FUNCTION: May be involved in spermatogenesis.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Expressed more abundantly in heart, pancreas and skeletal muscle. {ECO:0000269|PubMed:15145523}.; smooth muscle;ovary;sympathetic chain;rectum;skin;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;cornea;placenta;hippocampus;head and neck;kidney;aorta;stomach; amygdala;testis - interstitial;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;testis; 0.39344 . -0.934977358 9.465675867 50.12009 1.39036 GGPS1 0.666629559092989 0.328220145018193 0.00515029588881812 geranylgeranyl diphosphate synthase 1 FUNCTION: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins.; . TISSUE SPECIFICITY: Abundantly expressed in testis. Found in other tissues to a lower extent.; smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.22133 0.17306 -0.317668748 31.45789101 27.92768 0.89682 GGT1 0.676974716705773 0.322827182586394 0.000198100707832817 gamma-glutamyltransferase 1 FUNCTION: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive. {ECO:0000269|PubMed:20622017, ECO:0000269|PubMed:24047895, ECO:0000269|PubMed:7673200, ECO:0000269|PubMed:7759490, ECO:0000269|PubMed:8095045, ECO:0000269|PubMed:8827453}.; DISEASE: Glutathionuria (GLUTH) [MIM:231950]: Autosomal recessive disease. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in fetal and adult kidney and liver, adult pancreas, stomach, intestine, placenta and lung. Isoform 3 is lung-specific. There are several other tissue-specific forms that arise from alternative promoter usage but that produce the same protein.; unclassifiable (Anatomical System);cartilage;heart;tongue;colon;fovea centralis;choroid;lens;retina;breast;uterus;pancreas;prostate;optic nerve;lung;frontal lobe;macula lutea;liver;testis;head and neck;spleen;kidney;mammary gland;stomach; . . 0.82835 -0.091746757 46.91554612 108.30452 2.25857 GGT2 0.804816509817502 0.19005173101808 0.00513175916441775 gamma-glutamyltransferase 2 FUNCTION: Isoform 1, isoform 2 and isoform 3 lack catalytic activity due to its inability to undergo the autocatalytic cleavage needed to produce a mature, enzymatically active heterodimer. {ECO:0000269|PubMed:23682772}.; . TISSUE SPECIFICITY: Highly expressed in fetal and adult kidney and liver.; . . . 0.11718 . . 1425.85016 7.05300 GGT3P . . . gamma-glutamyltransferase 3 pseudogene FUNCTION: Initiates extracellular glutathione (GSH) breakdown; catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. {ECO:0000250}.; . . . . . 0.09978 . . . . GGT4P . . . gamma-glutamyltransferase 4 pseudogene . . . . . . . . . . . GGT5 1.39303239383364e-05 0.957793620176963 0.0421924494990991 gamma-glutamyltransferase 5 FUNCTION: Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4).; . . ovary;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;optic nerve;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;temporal lobe;lens;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;kidney;mammary gland;stomach; uterus corpus;adipose tissue;kidney;atrioventricular node;parietal lobe; 0.05038 . -0.372889896 28.20240623 353.63063 3.98062 GGT6 2.45819064940681e-06 0.164065498132247 0.835932043677103 gamma-glutamyltransferase 6 FUNCTION: Cleaves glutathione conjugates. {ECO:0000250}.; . . prostate;optic nerve;lung;heart;macula lutea;testis;colon;fovea centralis;choroid;kidney;lens;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle;cerebellum; 0.10281 . 0.510776592 80.23708422 974.18175 6.03617 GGT7 0.998200259468736 0.00179973156155669 8.96970721157501e-09 gamma-glutamyltransferase 7 FUNCTION: Cleaves glutathione conjugates. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed, but at low level, except in the airway epithelial cells. Detected in brain, heart, kidney, liver, lung, spleen, testis and trachea.; myocardium;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;cerebellum; ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.33903 0.34383 -0.644723694 16.52512385 71.78454 1.76380 GGT8P . . . gamma-glutamyltransferase 8 pseudogene . . . . . . . . . . . GGTA1P . . . glycoprotein, alpha-galactosyltransferase 1 pseudogene . . . . . 0.10828 . . . . . GGTA2P . . . glycoprotein, alpha-galactosyltransferase 2, pseudogene . . . . . . . . . . . GGTLC1 0.000145547384937393 0.421162142431476 0.578692310183587 gamma-glutamyltransferase light chain 1 . . . unclassifiable (Anatomical System);medulla oblongata;heart;cartilage;colon;fovea centralis;choroid;lens;retina;uterus;breast;prostate;optic nerve;lung;macula lutea;liver;testis;spleen;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;kidney;trigeminal ganglion;skeletal muscle; 0.20602 . 0.885576705 89.14248644 150.88184 2.68484 GGTLC2 0.000421521541315101 0.411717193472767 0.587861284985918 gamma-glutamyltransferase light chain 2 . . TISSUE SPECIFICITY: Placenta and sigmoid tissues.; . . 0.17087 . . . 1959.81555 8.15073 GGTLC3 . . . gamma-glutamyltransferase light chain 3 . . . . . . . . . 25.47088 0.83152 GGTLC4P . . . gamma-glutamyltransferase light chain 4 pseudogene . . . . . . . . . . . GGTLC5P . . . gamma-glutamyltransferase light chain 5 pseudogene . . . . . . . . . . . GH1 0.0174315619078563 0.891491677845688 0.0910767602464554 growth hormone 1 FUNCTION: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.; DISEASE: Growth hormone deficiency, isolated, 1A (IGHD1A) [MIM:262400]: An autosomal recessive, severe deficiency of growth hormone leading to dwarfism. Patients often develop antibodies to administered growth hormone. {ECO:0000269|PubMed:8364549}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Growth hormone deficiency, isolated, 1B (IGHD1B) [MIM:612781]: An autosomal recessive deficiency of growth hormone leading to short stature. Patients have low but detectable levels of growth hormone, significantly retarded bone age, and a positive response and immunologic tolerance to growth hormone therapy. {ECO:0000269|PubMed:12655557}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Kowarski syndrome (KWKS) [MIM:262650]: A syndrome clinically characterized by short stature associated with bioinactive growth hormone, normal or slightly increased growth hormone secretion, pathologically low insulin-like growth factor 1 levels, and normal catch-up growth on growth hormone replacement therapy. {ECO:0000269|PubMed:8552145, ECO:0000269|PubMed:9276733}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Growth hormone deficiency, isolated, 2 (IGHD2) [MIM:173100]: An autosomal dominant deficiency of growth hormone leading to short stature. Clinical severity is variable. Patients have a positive response and immunologic tolerance to growth hormone therapy. {ECO:0000269|PubMed:11502836, ECO:0000269|PubMed:9152628}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;umbilical cord;cerebral cortex;epididymis;placenta;pituitary gland;blood;brain; dorsal root ganglion;superior cervical ganglion;tongue;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;pituitary;skeletal muscle; 0.10625 0.25130 0.308721233 72.59966973 112.31173 2.30513 GH2 3.38589979948727e-05 0.35841504396121 0.641551097040795 growth hormone 2 FUNCTION: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.; . TISSUE SPECIFICITY: Expressed in the placenta.; lung;cerebral cortex;epididymis;placenta;pituitary gland;brain;aorta; superior cervical ganglion;tongue;placenta;adrenal cortex;appendix;pituitary; 0.07440 . 0.707379532 85.62750649 51.66822 1.41951 GHDC 2.1212473947494e-05 0.901589924767775 0.0983888627582771 GH3 domain containing . . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; . 0.05978 0.10176 0.198490371 67.30360934 168.48553 2.83321 GHET1 . . . gastric carcinoma proliferation enhancing transcript 1 . . . . . . . . . . . GHITM 0.129493357758818 0.865743162041709 0.00476348019947298 growth hormone inducible transmembrane protein FUNCTION: Required for the mitochondrial tubular network and cristae organization. Involved in apoptotic release of cytochrome c. {ECO:0000269|PubMed:18417609}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;pia mater;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach;thymus; whole brain;dorsal root ganglion;amygdala;thalamus;medulla oblongata;testis - interstitial;occipital lobe;hypothalamus;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;adrenal gland;prefrontal cortex;globus pallidus;testis;kidney;parietal lobe;cingulate cortex; 0.13857 0.11797 -0.115612493 45.12856806 174.8105 2.87519 GHR 0.000232177140704853 0.980558078408474 0.0192097444508216 growth hormone receptor FUNCTION: Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to the JAK2/STAT5 pathway (By similarity). {ECO:0000250}.; FUNCTION: Isoform 2 up-regulates the production of GHBP and acts as a negative inhibitor of GH signaling.; DISEASE: Laron syndrome (LARS) [MIM:262500]: A severe form of growth hormone insensitivity characterized by growth impairment, short stature, dysfunctional growth hormone receptor, and failure to generate insulin-like growth factor I in response to growth hormone. {ECO:0000269|PubMed:10870033, ECO:0000269|PubMed:14678285, ECO:0000269|PubMed:2779634, ECO:0000269|PubMed:8137822, ECO:0000269|PubMed:8421103, ECO:0000269|PubMed:8504296, ECO:0000269|PubMed:9024232, ECO:0000269|PubMed:9661642, ECO:0000269|PubMed:9851797}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Growth hormone insensitivity, partial (GHIP) [MIM:604271]: A disease characterized by partial resistance to growth hormone resulting in short stature. Short stature is defined by a standing height more than 2 standard deviations below the mean (or below the 2.5 percentile) for sex and chronological age, compared with a well-nourished, healthy, genetically relevant population. {ECO:0000269|PubMed:7565946}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in various tissues with high expression in liver and skeletal muscle. Isoform 4 is predominantly expressed in kidney, bladder, adrenal gland and brain stem. Isoform 1 expression in placenta is predominant in chorion and decidua. Isoform 4 is highly expressed in placental villi. Isoform 2 is expressed in lung, stomach and muscle. Low levels in liver.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;uterus;prostate;whole body;cochlea;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;pharynx;blood;skeletal muscle;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;adipose tissue;liver;trigeminal ganglion; 0.38194 0.52767 0.756930627 86.79523473 4777.95984 14.00903 GHRH 0.455312663756291 0.517672896614367 0.0270144396293419 growth hormone releasing hormone FUNCTION: GRF is released by the hypothalamus and acts on the adenohypophyse to stimulate the secretion of growth hormone.; . . unclassifiable (Anatomical System);lung; superior cervical ganglion;globus pallidus; 0.11024 0.34400 0.169169615 65.33380514 41.86877 1.22003 GHRHR 0.00267945937720418 0.983226465302438 0.0140940753203575 growth hormone releasing hormone receptor FUNCTION: Receptor for GRF, coupled to G proteins which activate adenylyl cyclase. Stimulates somatotroph cell growth, growth hormone gene transcription and growth hormone secretion.; . TISSUE SPECIFICITY: Pituitary gland.; pituitary gland;brain; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;pituitary; 0.14838 0.22267 -0.288341872 33.41589998 610.73855 4.99493 GHRL 8.36902634828911e-05 0.323955125481469 0.675961184255048 ghrelin/obestatin prepropeptide FUNCTION: Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation.; . TISSUE SPECIFICITY: Highest level in stomach. All forms are found in serum as well. Other tissues compensate for the loss of ghrelin synthesis in the stomach following gastrectomy. {ECO:0000269|PubMed:12414809}.; unclassifiable (Anatomical System);lung;cartilage;testis;brain;stomach; . 0.07833 0.35915 0.61555716 83.13871196 932.46692 5.92354 GHRLOS . . . ghrelin opposite strand/antisense RNA . . . . . . . . . . . GHSR 0.0433453469862917 0.848697099777407 0.107957553236302 growth hormone secretagogue receptor FUNCTION: Receptor for ghrelin, coupled to G-alpha-11 proteins. Stimulates growth hormone secretion. Binds also other growth hormone releasing peptides (GHRP) (e.g. Met-enkephalin and GHRP-6) as well as non-peptide, low molecular weight secretagogues (e.g. L-692,429, MK-0677, adenosine). {ECO:0000269|PubMed:10604470, ECO:0000269|PubMed:11322507}.; . TISSUE SPECIFICITY: Pituitary and hypothalamus.; unclassifiable (Anatomical System); medulla oblongata;superior cervical ganglion;liver;globus pallidus;kidney;skeletal muscle;cingulate cortex; 0.58942 0.22438 -0.091746757 46.91554612 69.10886 1.72267 GID4 0.937456357393192 0.0622715123966461 0.000272130210161855 GID complex subunit 4 homolog . . . . . 0.48689 . . . 37.49301 1.11658 GID8 0.961707185864695 0.0382129662359572 7.98478993478833e-05 GID complex subunit 8 . . . . . 0.29868 0.11262 -0.09720619 46.20193442 3.59477 0.13097 GIF 0.434202069663625 0.564336815522819 0.00146111481355561 gastric intrinsic factor FUNCTION: Promotes absorption of the essential vitamin cobalamin (Cbl) in the ileum. After interaction with CUBN, the GIF-cobalamin complex is internalized via receptor-mediated endocytosis.; . TISSUE SPECIFICITY: Gastric mucosa.; unclassifiable (Anatomical System);colon;kidney;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.08359 0.32009 0.687150476 85.17928757 116.32414 2.34572 GIGYF1 0.978704811680111 0.0212951882672218 5.26672603486132e-11 GRB10 interacting GYF protein 1 FUNCTION: May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling. May increase IGF1 receptor phosphorylation under IGF1 stimulation as well as phosphorylation of IRS1 and SHC1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:12771153}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;blood;bone marrow;uterus;prostate;lung;frontal lobe;thyroid;placenta;visual apparatus;testis;cervix;germinal center;brain;stomach;cerebellum; . 0.17963 0.14866 -1.655370293 2.754187308 1759.42516 7.73997 GIGYF2 0.99999999997935 2.06501034539141e-11 4.07829157222728e-28 GRB10 interacting GYF protein 2 FUNCTION: May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling, including IGF1 and insulin receptors. {ECO:0000269|PubMed:12771153}.; DISEASE: Parkinson disease 11 (PARK11) [MIM:607688]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. {ECO:0000269|PubMed:18358451}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . . . 0.69759 0.11014 -1.146380093 6.334041047 981.73564 6.04956 GIMAP1 0.839321399910499 0.157615762694693 0.00306283739480788 GTPase, IMAP family member 1 FUNCTION: May regulate lymphocyte survival. Required for normal levels of mature T-lymphocytes and mature B-cells (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Predominantly expressed in the spleen and to a lesser extent in the lymph nodes. Detected in T-cells. {ECO:0000269|PubMed:11814688, ECO:0000269|PubMed:23454188}.; unclassifiable (Anatomical System);smooth muscle;lung;cartilage;ovary;placenta;kidney; . 0.10763 . 0.283038099 71.26680821 33.99796 1.04340 GIMAP1-GIMAP5 . . . GIMAP1-GIMAP5 readthrough . . . . . . . . . . . GIMAP2 0.00122833357888369 0.635045509932237 0.363726156488879 GTPase, IMAP family member 2 FUNCTION: The heterodimer formed by GIMAP2 and GIMAP7 has GTPase activity. In contrast, GIMAP2 has no GTPase activity by itself. {ECO:0000269|PubMed:23454188}.; . TISSUE SPECIFICITY: Detected in T-cells. {ECO:0000269|PubMed:23454188}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;pharynx;blood;lens;bile duct;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;stomach; superior cervical ganglion; 0.05760 0.06700 0.973768544 90.33970276 317.47381 3.78253 GIMAP3P . . . GTPase, IMAP family member 3 pseudogene . . . . . . . . . . . GIMAP4 7.68887548397492e-05 0.31064471072685 0.68927840051831 GTPase, IMAP family member 4 FUNCTION: May play a role in regulating lymphocyte apoptosis (By similarity). Exhibits intrisinic GTPase activity. Shows a higher affinity for GDP over GTP (about 12-fold higher), and binding shows an absolute requirement for magnesium. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in spleen and peripheral blood leukocytes that contain mostly T- and B-lymphocytes. Expressed specifically in resting T- and B-lymphocytes and expression significantly decreases during B- or T-lymphocyte activation. Expressed at lower levels in thymus, ovary, colon and small intestine. {ECO:0000269|PubMed:23454188}.; lymphoreticular;ovary;parathyroid;vein;skin;uterus;prostate;thyroid;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;skeletal muscle;pancreas;lung;nasopharynx;placenta;spleen;kidney;mammary gland;aorta;thymus; whole blood; 0.03461 0.06465 0.306902668 72.38145789 688.54331 5.23575 GIMAP5 0.189192166314945 0.761432673875469 0.0493751598095865 GTPase, IMAP family member 5 FUNCTION: Required for mitochondrial integrity and T-cell survival. May contribute to T-cell quiescence (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed with high levels in lymph node and spleen. High expression found in CD4 and CD8-positive T- cells and monocytes with very low levels in B-lymphocytes. Highly expressed in B-lymphocyte-derived neoplasms. {ECO:0000269|PubMed:14724691}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;bone marrow;uterus;prostate;frontal lobe;endometrium;cerebral cortex;testis;brain;tonsil;unclassifiable (Anatomical System);cartilage;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;kidney;stomach;aorta;peripheral nerve; dorsal root ganglion;medulla oblongata;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.08488 0.11148 0.106667882 61.73036093 42.68067 1.23830 GIMAP6 0.0973436196255574 0.867060619089796 0.0355957612846466 GTPase, IMAP family member 6 . . TISSUE SPECIFICITY: Highly expressed in spleen, lymph nodes, lung and placenta. Expressed at moderate level in thymus, kidney, heart and digestive tract. Weakly expressed in other lymphoid tissues. Detected in T-cells. {ECO:0000269|PubMed:15474311, ECO:0000269|PubMed:23454188}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;parathyroid;choroid;skin;uterus;pancreas;whole body;lung;nasopharynx;bone;placenta;alveolus;testis;spleen;kidney;stomach; white blood cells;whole blood; 0.05482 0.07910 1.063778722 91.58410002 1915.22577 8.05319 GIMAP7 0.00184489304608896 0.483137820709756 0.515017286244155 GTPase, IMAP family member 7 FUNCTION: The dimer has GTPase activity; the active site contains residues from both subunits. {ECO:0000269|PubMed:23454188}.; . TISSUE SPECIFICITY: Detected in T-cells. {ECO:0000269|PubMed:23454188}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;islets of Langerhans;adrenal cortex;parathyroid;skin;skeletal muscle;uterus;pancreas;lung;adrenal gland;nasopharynx;bone;thyroid;placenta;testis;spleen;kidney;brain;pineal gland;mammary gland;aorta; . 0.01635 . 0.128714042 63.19886766 1328.14795 6.84943 GIMAP8 6.85022595051609e-06 0.715783729037417 0.284209420736632 GTPase, IMAP family member 8 FUNCTION: Exerts an anti-apoptotic effect in the immune system and is involved in responses to infections. {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in T-cells. {ECO:0000269|PubMed:23454188}.; unclassifiable (Anatomical System);amygdala;smooth muscle;cartilage;uterus;pancreas;prostate;lung;nasopharynx;placenta;thyroid;germinal center;kidney;spinal ganglion; trigeminal ganglion; 0.03828 0.05667 -0.020150552 52.25288983 134.24352 2.51910 GIMD1 . . . GIMAP family P-loop NTPase domain containing 1 . . . . . . . . . . . GIN1 0.00667768191022757 0.974933007469218 0.0183893106205547 gypsy retrotransposon integrase 1 . . TISSUE SPECIFICITY: Widely expressed. Also found in tumors originating from parathyroid gland, colon, stomach, bladder, uterus and prostate. {ECO:0000269|PubMed:11470852}.; . . 0.14682 0.13594 0.595326758 82.66100495 269.7708 3.52405 GINGF2 . . . gingival fibromatosis, hereditary, 2 . . . . . . . . . . . GINGF3 . . . gingival fibromatosis, hereditary, 3 . . . . . . . . . . . GINGF4 . . . gingival fibromatosis, hereditary, 4 . . . . . . . . . . . GINM1 7.70683279294107e-05 0.755141444417351 0.244781487254719 glycoprotein integral membrane 1 . . . . . 0.17281 . 0.371224249 75.12384996 190.0777 2.99257 GINS1 0.0500369772330311 0.945286354695983 0.00467666807098593 GINS complex subunit 1 (Psf1 homolog) FUNCTION: The GINS complex plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single- stranded DNA. GINS1 is essential for function. {ECO:0000269|PubMed:17417653}.; . . unclassifiable (Anatomical System);lymph node;placenta;visual apparatus;testis;colon;cervix;blood;germinal center;brain;bone marrow; dorsal root ganglion;superior cervical ganglion;tumor; 0.09197 0.14744 0.3032669 72.009908 129.73418 2.48159 GINS2 6.07718456409909e-09 0.0361702382996778 0.963829755623138 GINS complex subunit 2 (Psf2 homolog) FUNCTION: The GINS complex plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single- stranded DNA. {ECO:0000269|PubMed:17417653}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;skin;uterus;prostate;optic nerve;gum;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;muscle;pharynx;blood;breast;bile duct;pancreas;lung;cornea;nasopharynx;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; fetal liver;testis;tumor; 0.57106 0.13609 -0.736552314 13.93606983 29.98936 0.95840 GINS3 0.236040219115464 0.73137979753705 0.0325799833474867 GINS complex subunit 3 (Psf3 homolog) FUNCTION: The GINS complex plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single- stranded DNA. {ECO:0000269|PubMed:17417653}.; . . sympathetic chain;colon;vein;skin;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach;thymus; ciliary ganglion;trigeminal ganglion; 0.23879 . -0.117432389 44.89266336 41.4762 1.21092 GINS4 0.0504728646441056 0.927720256354825 0.0218068790010698 GINS complex subunit 4 (Sld5 homolog) FUNCTION: The GINS complex plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS4 is important for GINS complex assembly. GINS complex seems to bind preferentially to single-stranded DNA. {ECO:0000269|PubMed:17417653}.; . . unclassifiable (Anatomical System);ovary;heart;salivary gland;intestine;pharynx;colon;blood;skin;bone marrow;breast;uterus;bile duct;prostate;nasopharynx;bone;placenta;visual apparatus;liver;testis;kidney;brain;bladder; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.31888 0.14665 -0.273576253 33.97027601 33.02354 1.02227 GIP 0.162839345434596 0.773523614342377 0.063637040223027 gastric inhibitory polypeptide FUNCTION: Potent stimulator of insulin secretion and relatively poor inhibitor of gastric acid secretion.; . . stomach; thalamus;ciliary ganglion;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.09377 0.28525 0.527368849 80.73248408 415.38531 4.26695 GIPC1 0.020370586194085 0.904245915645819 0.075383498160096 GIPC PDZ domain containing family member 1 FUNCTION: May be involved in G protein-linked signaling.; . TISSUE SPECIFICITY: Widely expressed.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;urinary;pharynx;blood;lens;breast;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;cerebellum; subthalamic nucleus;superior cervical ganglion;cingulate cortex; 0.42070 0.19852 0.106667882 61.73036093 627.61682 5.04928 GIPC2 3.41555177810974e-08 0.0974095002793782 0.902590465565104 GIPC PDZ domain containing family member 2 . . TISSUE SPECIFICITY: Expressed at highest levels in ascending colon and at moderate levels in adult kidney. Expressed at low levels in adult pancreas and at very low levels in adult liver. Expression is down-regulated in several primary tumors, such as kidney, colon and rectal tumors. {ECO:0000269|PubMed:11836570}.; . . 0.12531 0.10725 -0.337894035 30.37272942 798.82852 5.57165 GIPC3 0.0542521307918308 0.864042108440264 0.0817057607679051 GIPC PDZ domain containing family member 3 FUNCTION: Required for postnatal maturation of the hair bundle and long-term survival of hair cells and spiral ganglion. {ECO:0000250}.; DISEASE: Deafness, autosomal recessive, 15 (DFNB15) [MIM:601869]: A form of non-syndromic sensorineural hearing loss with prelingual onset. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:21326233, ECO:0000269|PubMed:21660509}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.24274 0.13034 -0.139478553 43.29440906 47.34091 1.33475 GIPR 2.5408335570195e-22 3.32315033542334e-05 0.999966768496646 gastric inhibitory polypeptide receptor FUNCTION: This is a receptor for GIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.; . . unclassifiable (Anatomical System);islets of Langerhans;pituitary gland; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;pituitary; 0.41791 0.16686 0.687150476 85.17928757 1766.09386 7.76644 GIT1 0.999303229612392 0.000696770207997679 1.79610459309251e-10 GIT ArfGAP 1 FUNCTION: GTPase-activating protein for the ADP ribosylation factor family. May serve as a scaffold to bring together molecules to form signaling modules controlling vesicle trafficking, adhesion and cytoskeletal organization. Increases the speed of cell migration, as well as the size and rate of formation of protrusions, possibly by targeting PAK1 to adhesions and the leading edge of lamellipodia. Sequesters inactive non-tyrosine- phosphorylated paxillin in cytoplasmic complexes. Involved in the regulation of cytokinesis; the function may involve SDCCAG3 and PTPN13 (By similarity). {ECO:0000250|UniProtKB:Q68FF6, ECO:0000269|PubMed:11896197}.; . . lymphoreticular;medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;bone;iris;testis;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; testis - interstitial;subthalamic nucleus;testis;globus pallidus;pons;cingulate cortex; 0.45144 0.17620 -1.397999468 4.193205945 21.48868 0.72421 GIT2 0.970632700807013 0.0293672851185887 1.40743978333036e-08 GIT ArfGAP 2 FUNCTION: GTPase-activating protein for the ADP ribosylation factor family.; . . smooth muscle;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;globus pallidus;white blood cells;atrioventricular node;whole blood;skeletal muscle; 0.15762 0.11158 -0.50880549 21.72682236 632.82145 5.06778 GJA1 0.215546849622465 0.775782971111432 0.00867017926610283 gap junction protein alpha 1 FUNCTION: Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a critical role in the physiology of hearing by participating in the recycling of potassium to the cochlear endolymph. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract (By similarity). May play a role in cell growth inhibition through the regulation of NOV expression and localization. Plays an essential role in gap junction communication in the ventricles (By similarity). {ECO:0000250|UniProtKB:P08050, ECO:0000250|UniProtKB:P23242}.; DISEASE: Oculodentodigital dysplasia (ODDD) [MIM:164200]: A disease characterized by a typical facial appearance and variable involvement of the eyes, dentition, and fingers. Characteristic facial features include a narrow, pinched nose with hypoplastic alae nasi, prominent columella and thin anteverted nares together with a narrow nasal bridge, and prominent epicanthic folds giving the impression of hypertelorism. The teeth are usually small and carious. Typical eye findings include microphthalmia and microcornea. The characteristic digital malformation is complete syndactyly of the fourth and fifth fingers (syndactyly type III) but the third finger may be involved and associated camptodactyly is a common finding. Cardiac abnormalities are observed in rare instances. {ECO:0000269|PubMed:12457340, ECO:0000269|PubMed:14729836, ECO:0000269|PubMed:15108203, ECO:0000269|PubMed:15637728, ECO:0000269|PubMed:16219735, ECO:0000269|PubMed:16222672, ECO:0000269|PubMed:16378922, ECO:0000269|PubMed:16709485, ECO:0000269|PubMed:16813608, ECO:0000269|PubMed:16816024, ECO:0000269|PubMed:17509830, ECO:0000269|PubMed:18161618, ECO:0000269|PubMed:19338053, ECO:0000269|PubMed:21670345, ECO:0000269|PubMed:23550541, ECO:0000269|PubMed:24508941}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Oculodentodigital dysplasia, autosomal recessive (ODDD- AR) [MIM:257850]: A disease characterized by a typical facial appearance and variable involvement of the eyes, dentition, and fingers. Characteristic facial features include a narrow, pinched nose with hypoplastic alae nasi, prominent columella and thin anteverted nares together with a narrow nasal bridge, and prominent epicanthic folds giving the impression of hypertelorism. The teeth are usually small and carious. Typical eye findings include microphthalmia and microcornea. The characteristic digital malformation is complete syndactyly of the fourth and fifth fingers (syndactyly type III) but the third finger may be involved and associated camptodactyly is a common finding. Cardiac abnormalities are observed in rare instances. {ECO:0000269|PubMed:16816024}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Syndactyly 3 (SDTY3) [MIM:186100]: A form of syndactyly, a congenital anomaly of the hand or foot marked by persistence of the webbing between adjacent digits that are more or less completely attached. In SDTY3, there is usually complete and bilateral syndactyly between the fourth and fifth fingers. Usually it is soft tissue syndactyly but occasionally the distal phalanges are fused. The fifth finger is short with absent or rudimentary middle phalanx. The feet are not affected. {ECO:0000269|PubMed:14729836}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Hypoplastic left heart syndrome 1 (HLHS1) [MIM:241550]: A syndrome due to defective development of the aorta proximal to the entrance of the ductus arteriosus, and hypoplasia of the left ventricle and mitral valve. As a result of the abnormal circulation, the ductus arteriosus and foramen ovale are patent and the right atrium, right ventricle, and pulmonary artery are enlarged. {ECO:0000269|PubMed:11470490}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hallermann-Streiff syndrome (HSS) [MIM:234100]: A disorder characterized by a typical skull shape (brachycephaly with frontal bossing), hypotrichosis, microphthalmia, cataracts, beaked nose, micrognathia, skin atrophy, dental anomalies and proportionate short stature. Mental retardation is present in a minority of cases. {ECO:0000269|PubMed:14974090}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Atrioventricular septal defect 3 (AVSD3) [MIM:600309]: A congenital heart malformation characterized by a common atrioventricular junction coexisting with deficient atrioventricular septation. The complete form involves underdevelopment of the lower part of the atrial septum and the upper part of the ventricular septum; the valve itself is also shared. A less severe form, known as ostium primum atrial septal defect, is characterized by separate atrioventricular valvar orifices despite a common junction. {ECO:0000269|PubMed:11470490}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Craniometaphyseal dysplasia, autosomal recessive (CMDR) [MIM:218400]: An osteochondrodysplasia characterized by hyperostosis and sclerosis of the craniofacial bones associated with abnormal modeling of the metaphyses. Sclerosis of the skull may lead to asymmetry of the mandible, as well as to cranial nerve compression, that may finally result in hearing loss and facial palsy. {ECO:0000269|PubMed:23951358}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the heart and fetal cochlea. {ECO:0000269|PubMed:11741837}.; smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;larynx;bone;thyroid;testis;dura mater;spinal ganglion;brain;artery;unclassifiable (Anatomical System);amygdala;meninges;heart;islets of Langerhans;hypothalamus;adrenal cortex;lens;skeletal muscle;breast;pia mater;lung;adrenal gland;mesenchyma;trabecular meshwork;placenta;visual apparatus;hippocampus;hypopharynx;liver;amnion;head and neck;mammary gland;stomach;aorta; amygdala;adrenal gland;hypothalamus;spinal cord;prefrontal cortex;caudate nucleus; 0.95221 0.36533 -0.271755481 34.31823543 29.87324 0.95342 GJA1P1 . . . gap junction protein alpha 1 pseudogene 1 . . . . . . . . . . . GJA3 0.000279889069012082 0.339261061901884 0.660459049029104 gap junction protein alpha 3 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.; DISEASE: Cataract 14, multiple types (CTRCT14) [MIM:601885]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT14 includes zonular pulverulent cataract, among others. Zonular or lamellar cataracts are opacities, broad or narrow, usually consisting of powdery white dots affecting only certain layers or zones between the cortex and nucleus of an otherwise clear lens. The opacity may be so dense as to render the entire central region of the lens completely opaque, or so translucent that vision is hardly if at all impeded. Usually sharply separated from a clear cortex outside them, they may have projections from their outer edges known as riders or spokes. {ECO:0000269|PubMed:10205266, ECO:0000269|PubMed:10746562, ECO:0000269|PubMed:14627959, ECO:0000269|PubMed:15208569, ECO:0000269|PubMed:15286166, ECO:0000269|PubMed:15448617, ECO:0000269|PubMed:16234473, ECO:0000269|PubMed:16254549, ECO:0000269|PubMed:16885921, ECO:0000269|PubMed:16971895, ECO:0000269|PubMed:17615540, ECO:0000269|PubMed:17893674, ECO:0000269|PubMed:20431721, ECO:0000269|PubMed:21552498, ECO:0000269|PubMed:21647269, ECO:0000269|PubMed:21681855, ECO:0000269|PubMed:21897748, ECO:0000269|PubMed:22312188, ECO:0000269|PubMed:24772942, ECO:0000269|PubMed:25635993}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.22516 0.12787 . . 17.88913 0.62488 GJA4 0.239138208939641 0.729125632642975 0.031736158417384 gap junction protein alpha 4 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.; . TISSUE SPECIFICITY: Expressed in multiple organs and tissues, including heart, uterus, ovary, and blood vessel endothelium.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;sympathetic chain;colon;choroid;lens;skin;uterus;pancreas;prostate;optic nerve;whole body;lung;endometrium;bone;placenta;hippocampus;testis;spleen;kidney;brain;mammary gland;stomach; heart;placenta;thyroid;liver;trigeminal ganglion; 0.16392 . 0.396906589 76.30927105 1645.66054 7.49496 GJA5 0.09799649643541 0.866775939940298 0.0352275636242918 gap junction protein alpha 5 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.; DISEASE: Atrial standstill 1 (ATRST1) [MIM:108770]: A rare arrhythmia characterized by the absence of electrical and mechanical activity in the atria. Electrocardiographically, it is characterized by bradycardia, the absence of P waves, and a junctional narrow complex escape rhythm. {ECO:0000269|PubMed:16790700}. Note=The disease may be caused by mutations affecting distinct genetic loci, including the gene represented in this entry. A rare GJA5 genotype has been detected in combination with a mutation in SCN5A in a large family with atrial standstill.; DISEASE: Atrial fibrillation, familial, 11 (ATFB11) [MIM:614049]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:20650941}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;heart;ovary;cartilage;islets of Langerhans;skin;uterus;lung;placenta;liver;testis;spleen;kidney; superior cervical ganglion;placenta; 0.10083 0.17511 -0.626318434 17.03231894 13.74549 0.49952 GJA6P . . . gap junction protein alpha 6 pseudogene . . . . . . . . . . . GJA8 2.67760459251749e-05 0.31970627035212 0.680266953601955 gap junction protein alpha 8 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.; . TISSUE SPECIFICITY: Eye lens.; uterus;optic nerve;macula lutea;testis;fovea centralis;choroid;lens;retina; dorsal root ganglion;superior cervical ganglion;testis - interstitial;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.33054 0.24051 -0.179930907 40.35739561 34.49315 1.05329 GJA9 3.07324197077134e-06 0.329427686736176 0.670569240021853 gap junction protein alpha 9 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly abundant in skeletal muscle. Also detected in testis. {ECO:0000269|PubMed:12881038}.; unclassifiable (Anatomical System);ovary;cartilage;colon;fovea centralis;choroid;lens;skeletal muscle;retina;bile duct;optic nerve;lung;placenta;thyroid;macula lutea;visual apparatus;liver;testis;spleen;kidney;brain;stomach; . 0.59650 0.12386 0.951720429 90.06251474 638.87219 5.08422 GJA10 4.55274700970182e-13 0.00360471426170468 0.99639528573784 gap junction protein alpha 10 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Involved in tracer coupling between horizontal cells of the retina. May play a role in the regulation of horizontal cell patterning (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle and heart. {ECO:0000269|PubMed:12881038}.; . . 0.32861 0.09592 -0.200157416 39.11299835 84.41578 1.95632 GJB1 0.65980172421035 0.316547105799048 0.0236511699906016 gap junction protein beta 1 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.; DISEASE: Charcot-Marie-Tooth disease, X-linked dominant, 1 (CMTX1) [MIM:302800]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies characterized by severely reduced motor nerve conduction velocities (NCVs) (less than 38m/s) and segmental demyelination and remyelination, and primary peripheral axonal neuropathies characterized by normal or mildly reduced NCVs and chronic axonal degeneration and regeneration on nerve biopsy. CMTX1 has both demyelinating and axonal features. Central nervous system involvement may occur. {ECO:0000269|PubMed:10071100, ECO:0000269|PubMed:10220155, ECO:0000269|PubMed:10234007, ECO:0000269|PubMed:10586284, ECO:0000269|PubMed:10732813, ECO:0000269|PubMed:10737979, ECO:0000269|PubMed:10873293, ECO:0000269|PubMed:10894999, ECO:0000269|PubMed:10923043, ECO:0000269|PubMed:10938190, ECO:0000269|PubMed:11030070, ECO:0000269|PubMed:11140841, ECO:0000269|PubMed:11180613, ECO:0000269|PubMed:11437164, ECO:0000269|PubMed:11438991, ECO:0000269|PubMed:11562788, ECO:0000269|PubMed:11571214, ECO:0000269|PubMed:11723288, ECO:0000269|PubMed:11835375, ECO:0000269|PubMed:12185164, ECO:0000269|PubMed:12207932, ECO:0000269|PubMed:12325071, ECO:0000269|PubMed:12402337, ECO:0000269|PubMed:12477701, ECO:0000269|PubMed:12497641, ECO:0000269|PubMed:12536289, ECO:0000269|PubMed:12707076, ECO:0000269|PubMed:14627639, ECO:0000269|PubMed:15241803, ECO:0000269|PubMed:15468313, ECO:0000269|PubMed:15852376, ECO:0000269|PubMed:7477983, ECO:0000269|PubMed:7833935, ECO:0000269|PubMed:8004109, ECO:0000269|PubMed:8162049, ECO:0000269|PubMed:8266101, ECO:0000269|PubMed:8628473, ECO:0000269|PubMed:8698335, ECO:0000269|PubMed:8733054, ECO:0000269|PubMed:8737658, ECO:0000269|PubMed:8807343, ECO:0000269|PubMed:8829637, ECO:0000269|PubMed:8889588, ECO:0000269|PubMed:8956046, ECO:0000269|PubMed:8990008, ECO:0000269|PubMed:9018031, ECO:0000269|PubMed:9099841, ECO:0000269|PubMed:9187667, ECO:0000269|PubMed:9272161, ECO:0000269|PubMed:9361298, ECO:0000269|PubMed:9452025, ECO:0000269|PubMed:9452099, ECO:0000269|PubMed:9469569, ECO:0000269|PubMed:9633821, ECO:0000269|PubMed:9818870, ECO:0000269|PubMed:9856562, ECO:0000269|Ref.12}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dejerine-Sottas syndrome (DSS) [MIM:145900]: A severe degenerating neuropathy of the demyelinating Charcot-Marie-Tooth disease category, with onset by age 2 years. Characterized by motor and sensory neuropathy with very slow nerve conduction velocities, increased cerebrospinal fluid protein concentrations, hypertrophic nerve changes, delayed age of walking as well as areflexia. There are both autosomal dominant and autosomal recessive forms of Dejerine-Sottas syndrome. {ECO:0000269|PubMed:15947997}. Note=The gene represented in this entry may act as a disease modifier.; . unclassifiable (Anatomical System);heart;nervous;islets of Langerhans;hypothalamus;colon;skin;uterus;pancreas;lung;frontal lobe;endometrium;placenta;liver;testis;spleen;kidney;brain;mammary gland;stomach; liver; 0.82351 0.43956 0.21326276 67.71644256 13.74274 0.49927 GJB2 1.02863295453376e-11 0.00164377442881105 0.998356225560903 gap junction protein beta 2 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.; DISEASE: Deafness, autosomal recessive, 1A (DFNB1A) [MIM:220290]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:10830906, ECO:0000269|PubMed:11313763, ECO:0000269|PubMed:11439000, ECO:0000269|PubMed:12121355, ECO:0000269|PubMed:12239718, ECO:0000269|PubMed:12786758, ECO:0000269|PubMed:14722929, ECO:0000269|PubMed:15666300, ECO:0000269|PubMed:15994881, ECO:0000269|PubMed:17660464, ECO:0000269|PubMed:17666888, ECO:0000269|PubMed:19384972, ECO:0000269|PubMed:23680645, ECO:0000269|PubMed:9328482, ECO:0000269|PubMed:9336442, ECO:0000269|PubMed:9471561, ECO:0000269|PubMed:9529365}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal dominant, 3A (DFNA3A) [MIM:601544]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:10807696, ECO:0000269|PubMed:11313763, ECO:0000269|PubMed:11439000, ECO:0000269|PubMed:12786758, ECO:0000269|PubMed:19384972, ECO:0000269|PubMed:9620796}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Vohwinkel syndrome (VS) [MIM:124500]: VS is an autosomal dominant disease characterized by hyperkeratosis, constriction on fingers and toes and congenital deafness. {ECO:0000269|PubMed:10369869, ECO:0000269|PubMed:15954104, ECO:0000269|PubMed:18688874}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Keratoderma, palmoplantar, with deafness (PPKDFN) [MIM:148350]: An autosomal dominant disorder characterized by the association of palmoplantar hyperkeratosis with progressive, bilateral, high-frequency, sensorineural deafness. {ECO:0000269|PubMed:10633135, ECO:0000269|PubMed:10757647, ECO:0000269|PubMed:12372058, ECO:0000269|PubMed:15996214, ECO:0000269|PubMed:17993581, ECO:0000269|PubMed:9856479}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Keratitis-ichthyosis-deafness syndrome (KID syndrome) [MIM:148210]: An autosomal dominant form of ectodermal dysplasia. Ectodermal dysplasia defines a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Keratitis-ichthyosis-deafness syndrome is characterized by the association of hyperkeratotic skin lesions with vascularizing keratitis and profound sensorineural hearing loss. Clinical features include deafness, ichthyosis, photophobia, absent or decreased eyebrows, sparse or absent scalp hair, decreased sweating and dysplastic finger and toenails. {ECO:0000269|PubMed:11912510, ECO:0000269|PubMed:12548749, ECO:0000269|PubMed:12752120}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bart-Pumphrey syndrome (BPS) [MIM:149200]: An autosomal dominant disorder characterized by sensorineural hearing loss, palmoplantar keratoderma, knuckle pads, and leukonychia, It shows considerable phenotypic variability. {ECO:0000269|PubMed:15482471, ECO:0000269|PubMed:15952212}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ichthyosis hystrix-like with deafness syndrome (HID syndrome) [MIM:602540]: An autosomal dominant keratinizing disorder characterized by sensorineural deafness and spiky hyperkeratosis affecting the entire skin. HID syndrome is considered to differ from the similar KID syndrome in the extent and time of occurrence of skin symptoms and the severity of the associated keratitis. {ECO:0000269|PubMed:12072059}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.42941 0.50569 0.663285274 84.55414013 794.09383 5.55726 GJB3 0.00273307067844208 0.796783882458591 0.200483046862967 gap junction protein beta 3 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.; DISEASE: Erythrokeratodermia variabilis (EKV) [MIM:133200]: A genodermatosis characterized by the appearance of two independent skin lesions: transient figurate erythematous patches and hyperkeratosis that is usually localized but occasionally occurs in its generalized form. Clinical presentation varies significantly within a family and from one family to another. Palmoplantar keratoderma is present in around 50% of cases. {ECO:0000269|PubMed:10594760, ECO:0000269|PubMed:10798362, ECO:0000269|PubMed:9843209}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal dominant, 2B (DFNA2B) [MIM:612644]: A form of non-syndromic sensorineural deafness characterized by progressive high frequency hearing loss in adulthood, with milder expression in females. {ECO:0000269|PubMed:9843210}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.12965 0.16401 0.198490371 67.30360934 303.93192 3.71358 GJB4 1.96484561379576e-06 0.0776833075675531 0.922314727586833 gap junction protein beta 4 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.; DISEASE: Erythrokeratodermia variabilis (EKV) [MIM:133200]: A genodermatosis characterized by the appearance of two independent skin lesions: transient figurate erythematous patches and hyperkeratosis that is usually localized but occasionally occurs in its generalized form. Clinical presentation varies significantly within a family and from one family to another. Palmoplantar keratoderma is present in around 50% of cases. {ECO:0000269|PubMed:11017804}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);skin; fetal liver;subthalamic nucleus;superior cervical ganglion;adrenal gland;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe;cerebellum; 0.18667 0.11084 0.644875971 84.10002359 1814.33582 7.85361 GJB5 7.70660156496684e-05 0.31100067130371 0.68892226268064 gap junction protein beta 5 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.; . . unclassifiable (Anatomical System);heart;pharynx;colon;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;macula lutea;hypopharynx;head and neck;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18241 0.13265 -0.047654689 50.22410946 106.01558 2.23287 GJB6 0.000189819676898347 0.473658801853174 0.526151378469928 gap junction protein beta 6 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.; DISEASE: Ectodermal dysplasia 2, Clouston type (ECTD2) [MIM:129500]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures such as hair, teeth, nails and sweat glands, with or without any additional clinical sign. Each combination of clinical features represents a different type of ectodermal dysplasia. ECTD2 is an autosomal dominant condition characterized by atrichosis, nail hypoplasia and deformities, hyperpigmentation of the skin, normal teeth, normal sweat and sebaceous gland function. Palmoplantar hyperkeratosis is a frequent feature. Hearing impairment has been detected in few cases. {ECO:0000269|PubMed:11017065, ECO:0000269|PubMed:11874494}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal recessive, 1B (DFNB1B) [MIM:612645]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:11807148, ECO:0000269|PubMed:15994881}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal dominant, 3B (DFNA3B) [MIM:612643]: A form of non-syndromic sensorineural hearing loss characterized by a variable phenotype, ranging from bilateral middle to high frequency hearing loss to profound sensorineural deafness. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:10471490}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;prostate;pancreas;cochlea;larynx;hypopharynx;colon;head and neck;brain;skin;stomach; . 0.05323 0.32175 0.260991686 70.25831564 38.94364 1.15378 GJB7 1.49897888141327e-06 0.0665556349732633 0.933442866047855 gap junction protein beta 7 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. {ECO:0000250, ECO:0000269|PubMed:12064583}.; . TISSUE SPECIFICITY: Weakly expressed in placenta. {ECO:0000269|PubMed:12881038}.; lung;placenta;testis;germinal center; dorsal root ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10882 . 1.150157577 92.46874263 555.71508 4.78879 GJC1 0.944105282209013 0.0556895104176745 0.000205207373312465 gap junction protein gamma 1 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.; . . unclassifiable (Anatomical System);smooth muscle;cartilage;heart;ovary;skin;uterus;breast;prostate;lung;frontal lobe;placenta;bone;visual apparatus;liver;testis;spleen;kidney; superior cervical ganglion;pons;trigeminal ganglion; 0.42755 0.17458 -0.117432389 44.89266336 27.01888 0.87313 GJC2 0.483282478985978 0.49453325451006 0.0221842665039618 gap junction protein gamma 2 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a role in myelination in central and peripheral nervous systems. {ECO:0000269|PubMed:15192806}.; DISEASE: Spastic paraplegia 44, autosomal recessive (SPG44) [MIM:613206]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. {ECO:0000269|PubMed:19056803}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Lymphedema, hereditary, 1C (LMPH1C) [MIM:613480]: A chronic disabling condition which results in swelling of the extremities due to altered lymphatic flow. Patients with lymphedema suffer from recurrent local infections and physical impairment. {ECO:0000269|PubMed:20537300}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in central nervous system, in sciatic nerve and sural nerve. Also detected in skeletal muscles. {ECO:0000269|PubMed:15192806}.; . . 0.11954 0.13829 . . 27.09817 0.87449 GJC3 0.00578882239787705 0.725642581392211 0.268568596209912 gap junction protein gamma 3 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. {ECO:0000250}.; . TISSUE SPECIFICITY: CNS specific. Expression is restricted to brain, spinal cord, and sciatic nerve. According to PubMed:12881038, expression is abundant in skeletal muscle, liver, and heart, and to a minor degree in pancreas and kidney. {ECO:0000269|PubMed:12151525, ECO:0000269|PubMed:12881038}.; mammary gland; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.15085 0.10686 0.194852702 67.03231894 191.62609 3.00187 GJD2 0.1177216002599 0.856017325084344 0.0262610746557563 gap junction protein delta 2 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.; . TISSUE SPECIFICITY: Highly expressed in neurons.; visual apparatus; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.33289 0.19444 -0.271755481 34.31823543 43.42131 1.25398 GJD3 0.00490136828897798 0.454842732135977 0.540255899575045 gap junction protein delta 3 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in vascular smooth muscle cells. Found in heart, colon, and artery (at protein level). Found in cerebral cortex, heart, liver, lung, kidney, spleen and testis. {ECO:0000269|PubMed:12154091, ECO:0000269|PubMed:12176752}.; unclassifiable (Anatomical System);lung;cartilage;visual apparatus;liver;colon;spleen;brain;skin; . 0.42755 0.09484 -0.117432389 44.89266336 50.22778 1.39220 GJD4 2.7835442829258e-05 0.325880695549367 0.674091469007803 gap junction protein delta 4 FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in pancreas, kidney, skeletal muscle, liver, placenta, and heart. {ECO:0000269|PubMed:12881038}.; brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.10619 0.09939 . . 168.49996 2.83363 GJE1 . . . gap junction protein epsilon 1 . . . . . 0.40858 . . . 1322.76603 6.84084 GK 0.9032586495572 0.096734397369059 6.95307374075428e-06 glycerol kinase FUNCTION: Key enzyme in the regulation of glycerol uptake and metabolism.; . TISSUE SPECIFICITY: Highly expressed in the liver, kidney and testis. Isoform 2 and isoform 3 are expressed specifically in testis and fetal liver, but not in the adult liver.; . . . 0.44410 -0.273576253 33.97027601 4.23799 0.15391 GK-AS1 . . . GK antisense RNA 1 . . . . . . . . . . . GK-IT1 . . . GK intronic transcript 1 . . . . . . . . . . . GK2 2.89758110627621e-08 0.0887564597393632 0.911243511284826 glycerol kinase 2 FUNCTION: Key enzyme in the regulation of glycerol uptake and metabolism. {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.10571 . -0.088107893 47.06298655 81.69796 1.91575 GK3P . . . glycerol kinase 3 pseudogene FUNCTION: Key enzyme in the regulation of glycerol uptake and metabolism.; . . . . . 0.44410 . . . . GK4P . . . glycerol kinase 4 pseudogene . . . . . . . . . . . GK5 0.519887601252046 0.480081245226539 3.11535214146593e-05 glycerol kinase 5 (putative) . . . . . 0.11834 0.10568 -0.582225231 18.44184949 25.18144 0.82292 GK6P . . . glycerol kinase 6 pseudogene . . . . . . . . . . . GKAP1 0.122828409976511 0.876101186406195 0.00107040361729421 G kinase anchoring protein 1 . . . . . 0.32406 0.10985 -0.383807564 27.41802312 33.37021 1.03043 GKN1 0.00026487819662883 0.543620055148877 0.456115066654494 gastrokine 1 FUNCTION: Has mitogenic activity and may be involved in maintaining the integrity of the gastric mucosal epithelium. {ECO:0000269|PubMed:12851218}.; . TISSUE SPECIFICITY: Expressed in stomach. No expression is detected in cancer tissue or gastric cancer cell lines. {ECO:0000269|PubMed:10835488, ECO:0000269|PubMed:12851218}.; . . 0.11358 0.11276 -0.183570861 39.95046001 19.98855 0.68088 GKN2 0.000143060405510152 0.651929788894844 0.347927150699646 gastrokine 2 . . TISSUE SPECIFICITY: Expressed in gastric mucosa. {ECO:0000269|PubMed:15924415}.; unclassifiable (Anatomical System);lung;cartilage;heart;placenta;colon;kidney;skeletal muscle;stomach; . 0.08859 0.08459 0.549415813 81.38122199 443.53341 4.38174 GKN3P . . . gastrokine 3, pseudogene FUNCTION: May inhibit gastric epithelial cell proliferation. {ECO:0000250}.; . . . . . . . . . . GLA 0.985045990572971 0.0149461702485405 7.83917848836595e-06 galactosidase alpha . DISEASE: Fabry disease (FD) [MIM:301500]: Rare X-linked sphingolipidosis disease where glycolipid accumulates in many tissues. The disease consists of an inborn error of glycosphingolipid catabolism. FD patients show systemic accumulation of globotriaosylceramide (Gb3) and related glycosphingolipids in the plasma and cellular lysosomes throughout the body. Clinical recognition in males results from characteristic skin lesions (angiokeratomas) over the lower trunk. Patients may show ocular deposits, febrile episodes, and burning pain in the extremities. Death results from renal failure, cardiac or cerebral complications of hypertension or other vascular disease. Heterozygous females may exhibit the disorder in an attenuated form, they are more likely to show corneal opacities. {ECO:0000269|PubMed:10090526, ECO:0000269|PubMed:10208848, ECO:0000269|PubMed:10666480, ECO:0000269|PubMed:10916280, ECO:0000269|PubMed:11076046, ECO:0000269|PubMed:11295840, ECO:0000269|PubMed:11668641, ECO:0000269|PubMed:11889412, ECO:0000269|PubMed:12694230, ECO:0000269|PubMed:1315715, ECO:0000269|PubMed:15162124, ECO:0000269|PubMed:15712228, ECO:0000269|PubMed:16533976, ECO:0000269|PubMed:1846223, ECO:0000269|PubMed:19621417, ECO:0000269|PubMed:2152885, ECO:0000269|PubMed:2171331, ECO:0000269|PubMed:2539398, ECO:0000269|PubMed:7504405, ECO:0000269|PubMed:7531540, ECO:0000269|PubMed:7575533, ECO:0000269|PubMed:7596372, ECO:0000269|PubMed:7599642, ECO:0000269|PubMed:7759078, ECO:0000269|PubMed:8069316, ECO:0000269|PubMed:8395937, ECO:0000269|PubMed:8738659, ECO:0000269|PubMed:8807334, ECO:0000269|PubMed:8834244, ECO:0000269|PubMed:8863162, ECO:0000269|PubMed:8875188, ECO:0000269|PubMed:8931708, ECO:0000269|PubMed:9100224, ECO:0000269|PubMed:9105656, ECO:0000269|PubMed:9452068, ECO:0000269|PubMed:9452090, ECO:0000269|PubMed:9452111, ECO:0000269|PubMed:9554750}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;ciliary body;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;cervix;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.09385 0.74184 0.038710339 56.92380278 286.62877 3.62570 GLB1 4.86457143252396e-08 0.952417326877713 0.0475826244765725 galactosidase beta 1 FUNCTION: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.; DISEASE: GM1-gangliosidosis 1 (GM1G1) [MIM:230500]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. {ECO:0000269|PubMed:10338095, ECO:0000269|PubMed:10737981, ECO:0000269|PubMed:10839995, ECO:0000269|PubMed:1487238, ECO:0000269|PubMed:15365997, ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:15791924, ECO:0000269|PubMed:16538002, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:1907800, ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:1928092, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8213816, ECO:0000269|Ref.24, ECO:0000269|Ref.27}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: GM1-gangliosidosis 2 (GM1G2) [MIM:230600]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose- terminal oligosaccharides. Inheritance is autosomal recessive. {ECO:0000269|PubMed:10737981, ECO:0000269|PubMed:12644936, ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:1907800, ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8213816}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: GM1-gangliosidosis 3 (GM1G3) [MIM:230650]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. {ECO:0000269|PubMed:11511921, ECO:0000269|PubMed:15986423, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:1907800, ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8198123, ECO:0000269|Ref.24, ECO:0000269|Ref.26}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mucopolysaccharidosis 4B (MPS4B) [MIM:253010]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. {ECO:0000269|PubMed:11511921, ECO:0000269|PubMed:12393180, ECO:0000269|PubMed:16538002, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:1928092, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:7586649}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;spinal cord;lens;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; superior cervical ganglion; 0.13760 0.09869 0.576916344 82.25406936 1991.79429 8.22239 GLB1L 2.51566098661046e-10 0.674140946414511 0.325859053333923 galactosidase beta 1 like FUNCTION: Probable glycosyl hydrolase. {ECO:0000305}.; . . ovary;colon;skin;retina;uterus;prostate;whole body;endometrium;gum;thyroid;bone;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.29758 0.12181 -0.400392389 26.85185185 99.39769 2.15850 GLB1L2 1.44692099840466e-16 0.0219021462789147 0.978097853721085 galactosidase beta 1 like 2 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;frontal lobe;thyroid;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;lung;placenta;hippocampus;visual apparatus;macula lutea;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21002 . -0.883608246 10.50365652 362.34844 4.03033 GLB1L3 1.88655110815495e-13 0.105062431079256 0.894937568920555 galactosidase beta 1 like 3 . . . . . 0.05812 . -0.861560326 10.89289927 104.9553 2.21434 GLC1B . . . glaucoma 1, open angle, B (adult-onset) . . . . . . . . . . . GLC1C . . . glaucoma 1, open angle, C . . . . . . . . . . . GLC1D . . . glaucoma 1, open angle, D (adult-onset) . . . . . . . . . . . GLC1H . . . glaucoma 1, open angle, H (adult-onset) . . . . . . . . . . . GLC1I . . . glaucoma 1, open angle, I . . . . . . . . . . . GLC1J . . . glaucoma 1, open angle, J (juvenile-onset) . . . . . . . . . . . GLC1K . . . glaucoma 1, open angle, K (juvenile-onset) . . . . . . . . . . . GLC1L . . . glaucoma 1, open angle, L (adult-onset) . . . . . . . . . . . GLC1M . . . glaucoma 1, open angle, M (juvenile-onset) . . . . . . . . . . . GLC1N . . . glaucoma 1, open angle, N (juvenile-onset) . . . . . . . . . . . GLC1P . . . glaucoma 1, open angle, P . . . . . . . . . . . GLC1Q . . . glaucoma 1, open angle, Q . . . . . . . . . . . GLC2A . . . glaucoma 2, angle closure . . . . . . . . . . . GLC3B . . . glaucoma 3, primary infantile, B . . . . . . . . . . . GLC3C . . . glaucoma 3, primary congenital, C . . . . . . . . . . . GLCCI1 0.24528207975459 0.753361140011309 0.00135678023410023 glucocorticoid induced 1 . . TISSUE SPECIFICITY: Predominantly expressed in lung, spleen, thymus and testis and, at lower levels, in brain, bone marrow, peripheral leukocytes, skin and trachea. {ECO:0000269|PubMed:12557054, ECO:0000269|PubMed:21991891}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;cochlea;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;lens;lung;nasopharynx;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;aorta; superior cervical ganglion; 0.27158 . -0.538132194 20.26421326 73.8512 1.79592 GLCE 0.327374271928511 0.669304911741976 0.00332081632951348 glucuronic acid epimerase FUNCTION: Converts D-glucuronic acid residues adjacent to N- sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains. This is important for further modifications that determine the specificity of interactions between these glycosaminoglycans and proteins. {ECO:0000269|PubMed:20118238}.; . . unclassifiable (Anatomical System);heart;ovary;tongue;islets of Langerhans;colon;parathyroid;skin;skeletal muscle;retina;uterus;whole body;lung;endometrium;bone;thyroid;placenta;liver;testis;head and neck;spleen;brain;stomach;gall bladder; superior cervical ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.32693 0.23355 0.086440867 60.47416844 110.70948 2.29194 GLDC 4.8794486364637e-14 0.747827753800922 0.252172246199029 glycine dehydrogenase (decarboxylating) FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The P protein (GLDC) binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (GCSH).; DISEASE: Non-ketotic hyperglycinemia (NKH) [MIM:605899]: Autosomal recessive disease characterized by accumulation of a large amount of glycine in body fluid and by severe neurological symptoms. {ECO:0000269|PubMed:11286506, ECO:0000269|PubMed:11592811, ECO:0000269|PubMed:1634607, ECO:0000269|PubMed:1996985}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.55085 0.31242 -0.674294 15.41047417 1105.53255 6.35322 GLDCP1 . . . glycine dehydrogenase (decarboxylase) pseudogene 1 . . . . . . . . . . . GLDN 1.79271352388512e-11 0.0591363115696326 0.94086368841244 gliomedin FUNCTION: Ligand for NRCAM and NFASC/neurofascin that plays a role in the formation and maintenance of the nodes of Ranvier on myelinated axons. Mediates interaction between Schwann cell microvilli and axons via its interactions with NRCAM and NFASC. Nodes of Ranvier contain clustered sodium channels that are crucial for the saltatory propagation of action potentials along myelinated axons. During development, nodes of Ranvier are formed by the fusion of two heminodes. Required for normal clustering of sodium channels at heminodes; not required for the formation of mature nodes with normal sodium channel clusters. Required, together with NRCAM, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier. {ECO:0000250|UniProtKB:Q8BMF8}.; . TISSUE SPECIFICITY: Specifically expressed in spinal cord, brain, placenta and sciatic nerve. More abundant in peripheral than central nervous system. {ECO:0000269|PubMed:16039564}.; unclassifiable (Anatomical System);uterus;lung;placenta;testis;spinal ganglion;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.22242 0.10145 1.420201535 94.92215145 2856.68957 10.11429 GLE1 1.53824816142355e-05 0.998327205835792 0.00165741168259424 GLE1, RNA export mediator FUNCTION: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC). {ECO:0000269|PubMed:12668658, ECO:0000269|PubMed:16000379, ECO:0000269|PubMed:9618489}.; DISEASE: Lethal congenital contracture syndrome 1 (LCCS1) [MIM:253310]: A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy, and congenital non-progressive joint contractures (arthrogryposis). The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth. LCCS1 patients manifest early fetal hydrops and akinesia, micrognathia, pulmonary hypoplasia, pterygia, and multiple joint contractures. It leads to prenatal death. {ECO:0000269|PubMed:18204449}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Lethal arthrogryposis with anterior horn cell disease (LAAHD) [MIM:611890]: A disorder characterized by fetal akinesia, arthrogryposis and motor neuron loss. The fetus often survives delivery, but dies early as a result of respiratory failure. Neuropathological findings resemble those of lethal congenital contracture syndrome type 1, but are less severe. {ECO:0000269|PubMed:18204449}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;pharynx;blood;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.33736 0.10182 -0.088107893 47.06298655 1002.42975 6.09812 GLG1 0.997711423693009 0.00228857630694538 4.52909704490388e-14 golgi glycoprotein 1 FUNCTION: Binds fibroblast growth factor and E-selectin (cell- adhesion lectin on endothelial cells mediating the binding of neutrophils).; . TISSUE SPECIFICITY: Widely expressed. Highest levels in pancreas, skeletal muscle, placenta, heart, testis and ovary. Also found in the kidney, liver, lung and brain. {ECO:0000269|PubMed:9182700}.; lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;adrenal cortex;blood;lens;breast;visual apparatus;liver;spleen;mammary gland;developmental;colon;uterus;whole body;cerebral cortex;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;nasopharynx;placenta;duodenum;amnion;head and neck;kidney;stomach;aorta;thymus; testis - interstitial;superior cervical ganglion;placenta;testis;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe; 0.17994 0.15913 -1.682848699 2.653927813 89.984 2.04218 GLI1 1.94829927539368e-06 0.993557453700709 0.00644059800001568 GLI family zinc finger 1 FUNCTION: Acts as a transcriptional activator (PubMed:19706761, PubMed:10806483, PubMed:19878745, PubMed:24311597, PubMed:24217340). Binds to the DNA consensus sequence 5'- GACCACCCA-3' (PubMed:2105456, PubMed:8378770, PubMed:24217340). May regulate the transcription of specific genes during normal development (PubMed:19706761). May play a role in craniofacial development and digital development, as well as development of the central nervous system and gastrointestinal tract. Mediates SHH signaling (PubMed:19706761). Plays a role in cell proliferation and differentiation via its role in SHH signaling (Probable). {ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:19706761, ECO:0000269|PubMed:19878745, ECO:0000269|PubMed:2105456, ECO:0000269|PubMed:24217340, ECO:0000269|PubMed:24311597, ECO:0000269|PubMed:8378770, ECO:0000305}.; . TISSUE SPECIFICITY: Detected in testis (at protein level) (PubMed:2105456). Testis, myometrium and fallopian tube. Also expressed in the brain with highest expression in the cerebellum, optic nerve and olfactory tract (PubMed:19878745). Isoform 1 is detected in brain, spleen, pancreas, liver, kidney and placenta; isoform 2 is not detectable in these tissues (PubMed:19706761). {ECO:0000269|PubMed:19706761, ECO:0000269|PubMed:19878745, ECO:0000269|PubMed:2105456}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;cartilage;heart;ovary;muscle;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;placenta;bone;macula lutea;alveolus;cervix;germinal center;kidney;aorta; superior cervical ganglion;testis - interstitial; 0.98302 0.56403 -0.879979233 10.5626327 3015.45702 10.42861 GLI2 0.998939595969048 0.00106040392981731 1.01134803139008e-10 GLI family zinc finger 2 FUNCTION: Functions as transcription regulator in the hedgehog (Hh) pathway (PubMed:18455992). Functions as transcriptional activator (PubMed:9557682, PubMed:19878745, PubMed:24311597). May also function as transcriptional repressor (By similarity). Requires STK36 for full transcriptional activator activity. Required for normal embryonic development (PubMed:15994174, PubMed:20685856). {ECO:0000250|UniProtKB:Q0VGT2, ECO:0000269|PubMed:15994174, ECO:0000269|PubMed:18455992, ECO:0000269|PubMed:19878745, ECO:0000269|PubMed:24311597, ECO:0000269|PubMed:9557682, ECO:0000305|PubMed:20685856}.; FUNCTION: Isoform 5: Acts as a transcriptional repressor. {ECO:0000269|PubMed:15994174}.; DISEASE: Holoprosencephaly 9 (HPE9) [MIM:610829]: A structural anomaly of the brain, in which the developing forebrain fails to correctly separate into right and left hemispheres. Holoprosencephaly is genetically heterogeneous and associated with several distinct facies and phenotypic variability. Holoprosencephaly type 9 is characterized by defective anterior pituitary formation and pan-hypopituitarism, with or without overt forebrain cleavage abnormalities, and holoprosencephaly-like midfacial hypoplasia. {ECO:0000269|PubMed:14581620, ECO:0000269|PubMed:17096318, ECO:0000269|PubMed:20685856}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Culler-Jones syndrome (CJS) [MIM:615849]: An autosomal dominant disorder characterized by a wide range of clinical manifestations. Clinical features include hypothalamic hamartoma, pituitary dysfunction, central or postaxial polydactyly, and syndactyly. Malformations are frequent in the viscera, e.g. anal atresia, bifid uvula, congenital heart malformations, pulmonary or renal dysplasia. {ECO:0000269|PubMed:15994174, ECO:0000269|PubMed:20685856}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 and isoform 4 are expressed in HTLV- 1-infected T-cell lines (at protein level). Isoform 1 and isoform 2 are strongly expressed in HTLV-1-infected T-cell lines. Isoform 3 and isoform 4 are weakly expressed in HTLV-1-infected T-cell lines. {ECO:0000269|PubMed:9557682}.; unclassifiable (Anatomical System);lung;synovium;brain;stomach;bone marrow; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.97757 0.34098 -1.242213846 5.378627035 484.45133 4.53105 GLI3 0.999994739435503 5.26056449062654e-06 6.00953250163151e-15 GLI family zinc finger 3 FUNCTION: Has a dual function as a transcriptional activator and a repressor of the sonic hedgehog (Shh) pathway, and plays a role in limb development. The full-length GLI3 form (GLI3FL) after phosphorylation and nuclear translocation, acts as an activator (GLI3A) while GLI3R, its C-terminally truncated form, acts as a repressor. A proper balance between the GLI3 activator and the repressor GLI3R, rather than the repressor gradient itself or the activator/repressor ratio gradient, specifies limb digit number and identity. In concert with TRPS1, plays a role in regulating the size of the zone of distal chondrocytes, in restricting the zone of PTHLH expression in distal cells and in activating chondrocyte proliferation. Binds to the minimal GLI-consensus sequence 5'-GGGTGGTC-3'. {ECO:0000269|PubMed:10693759, ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:17764085}.; DISEASE: Greig cephalo-poly-syndactyly syndrome (GCPS) [MIM:175700]: Autosomal dominant disorder affecting limb and craniofacial development. It is characterized by pre- and postaxial polydactyly, syndactyly of fingers and toes, macrocephaly and hypertelorism. {ECO:0000269|PubMed:10441342, ECO:0000269|PubMed:12414818, ECO:0000269|PubMed:12794692, ECO:0000269|PubMed:9302279}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pallister-Hall syndrome (PHS) [MIM:146510]: An autosomal dominant disorder characterized by a wide range of clinical manifestations. Clinical features include hypothalamic hamartoma, pituitary dysfunction, central or postaxial polydactyly, and syndactyly. Malformations are frequent in the viscera, e.g. anal atresia, bifid uvula, congenital heart malformations, pulmonary or renal dysplasia. {ECO:0000269|PubMed:10441570}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Polydactyly, postaxial A1 (PAPA1) [MIM:174200]: A condition characterized by the occurrence of supernumerary digits in the upper and/or lower extremities. In postaxial polydactyly type A, the extra digit is well-formed and articulates with the fifth or a sixth metacarpal/metatarsal. {ECO:0000269|PubMed:10441570}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Polydactyly, postaxial B (PAPB) [MIM:174200]: A condition characterized by an extra digit in the occurrence of supernumerary digits in the upper and/or lower extremities. In postaxial polydactyly type B the extra digit is not well formed and is frequently in the form of a skin. {ECO:0000269|PubMed:10441570}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Polydactyly preaxial 4 (POP4) [MIM:174700]: Preaxial polydactyly (i.e., polydactyly on the radial/tibial side of the hand/foot) covers a heterogeneous group of entities. In preaxial polydactyly type IV, the thumb shows only the mildest degree of duplication, and syndactyly of various degrees affects fingers 3 and 4. {ECO:0000269|PubMed:10441570}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Is expressed in a wide variety of normal adult tissues, including lung, colon, spleen, placenta, testis, and myometrium.; . . 0.99640 0.10708 -1.310171316 4.83014862 2831.41391 10.04419 GLI4 0.00102128735288296 0.594782801349434 0.404195911297683 GLI family zinc finger 4 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;pharynx;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;kidney;thymus; amygdala;superior cervical ganglion;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; . . . . 2699.91143 9.77879 GLIDR . . . glioblastoma down-regulated RNA . . . . . . . . . . . GLIPR1 1.05178857542352e-09 0.0898910792068283 0.910108919741383 GLI pathogenesis related 1 . . TISSUE SPECIFICITY: According to PubMed:8973356, it is ubiquitously expressed with high levels in lung and kidney and low levels in heart and liver. Highly expressed in cell lines derived from nervous system tumors arising from glia, low or absent in non-glial-derived nervous system tumor cell lines. Also found in fetal kidney. According to PubMed:7607567 it is expressed only in brain tumor glioblastoma multiforme/astrocytoma and not in other nervous system tumors or normal fetal or adult tissues.; ovary;salivary gland;intestine;colon;vein;skin;bone marrow;uterus;prostate;optic nerve;bone;testis;amniotic fluid;germinal center;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;kidney;aorta;stomach; superior cervical ganglion;smooth muscle;white blood cells;whole blood;skeletal muscle; 0.04945 0.08267 -0.426079032 25.36565228 20.42182 0.69597 GLIPR1L1 0.00366338494663925 0.844610581777894 0.151726033275467 GLI pathogenesis related 1 like 1 . . TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:16714093}.; unclassifiable (Anatomical System);breast;uterus;testis; dorsal root ganglion;superior cervical ganglion;testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.04642 0.06434 -0.139478553 43.29440906 89.10762 2.02692 GLIPR1L2 0.00310862434597101 0.818805201244282 0.178086174409747 GLI pathogenesis-related 1 like 2 . . TISSUE SPECIFICITY: Highly expressed in testis. Detected in prostate, kidney, bladder, lung and bone marrow. {ECO:0000269|PubMed:16714093}.; unclassifiable (Anatomical System);larynx;hippocampus;testis;head and neck;skin; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.02820 0.07439 0.238945317 69.20853975 52.37853 1.43123 GLIPR2 0.000501676858537022 0.445298801078909 0.554199522062554 GLI pathogenesis-related 2 . . TISSUE SPECIFICITY: Highest expression in lung and peripheral leukocytes, and minor expression in liver and kidney. {ECO:0000269|PubMed:12137952}.; . . 0.10762 0.12028 -0.383807564 27.41802312 19.58638 0.67206 GLIS1 0.0999809478306639 0.892580198374259 0.00743885379507714 GLIS family zinc finger 1 FUNCTION: Acts as both a repressor and activator of transcription. Binds to the consensus sequence 5'-GACCACCCAC-3' (By similarity). {ECO:0000250|UniProtKB:Q8K1M4}.; . . unclassifiable (Anatomical System);cartilage;visual apparatus;kidney;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.17132 0.09750 0.696256907 85.2913423 1474.73624 7.15329 GLIS2 0.953068391479354 0.0467990804508141 0.00013252806983152 GLIS family zinc finger 2 FUNCTION: Can act either as a transcriptional repressor or as a transcriptional activator, depending on the cell context. Acts as a repressor of the Hedgehog signaling pathway (By similarity). Represses the Hedgehog-dependent expression of Wnt4 (By similarity). Necessary to maintain the differentiated epithelial phenotype in renal cells through the inhibition of SNAI1, which itself induces the epithelial-to-mesenchymal transition (By similarity). Represses transcriptional activation mediated by CTNNB1 in the Wnt signaling pathway. May act by recruiting the corepressors CTBP1 and HDAC3. May be involved in neuron differentiation (By similarity). {ECO:0000250}.; DISEASE: Nephronophthisis 7 (NPHP7) [MIM:611498]: An autosomal recessive disorder resulting in end-stage renal disease during childhood or adolescence. It is a progressive tubulo-interstitial kidney disorder histologically characterized by modifications of the tubules with thickening of the basement membrane, interstitial fibrosis and, in the advanced stages, medullary cysts. {ECO:0000269|PubMed:17618285}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at high levels in kidney and at low levels in heart, lung and placenta. Expressed in colon. {ECO:0000269|PubMed:11738817, ECO:0000269|PubMed:17289029}.; unclassifiable (Anatomical System);amygdala;smooth muscle;cartilage;ovary;islets of Langerhans;colon;lens;skeletal muscle;retina;uterus;pancreas;whole body;lung;endometrium;bone;placenta;duodenum;liver;testis;spleen;kidney;brain;mammary gland; superior cervical ganglion; 0.22932 0.07981 -0.179930907 40.35739561 614.21234 5.00828 GLIS2-AS1 . . . GLIS2 antisense RNA 1 . . . . . . . . . . . GLIS3 0.000100596771327456 0.997176535370395 0.00272286785827785 GLIS family zinc finger 3 FUNCTION: Acts as both a repressor and activator of transcription. Binds to the consensus sequence 5'-GACCACCCAC-3' (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: In the adult, expressed at high levels in the kidney and at lower levels in the brain, skeletal muscle, pancreas, liver, lung, thymus and ovary. {ECO:0000269|PubMed:14500813}.; unclassifiable (Anatomical System);amygdala;ovary;cartilage;fovea centralis;choroid;lens;retina;breast;pancreas;optic nerve;lung;endometrium;placenta;macula lutea;visual apparatus;liver;testis;spleen;cervix;brain;stomach; . 0.59622 . -0.007415459 52.86034442 744.78269 5.41665 GLIS3-AS1 . . . GLIS3 antisense RNA 1 . . . . . . . . . . . GLMN 4.16913776813199e-06 0.989426605545151 0.0105692253170811 glomulin, FKBP associated protein FUNCTION: Essential for normal development of the vasculature. May represent a naturally occurring ligand of the immunophilins FKBP59 and FKBP12. May function as an membrane anchoring protein. Isoform 1 may stimulate the p70S6K pathway. Isoform 2 may inhibit cell proliferation and increase IL2 production. {ECO:0000269|PubMed:11571281, ECO:0000269|PubMed:12604780}.; DISEASE: Glomuvenous malformations (GVMs) [MIM:138000]: Characterized by the presence of smooth-muscle-like glomus cells in the media surrounding distended vascular lumens. {ECO:0000269|PubMed:11845407}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; . . 0.27629 0.11166 1.2860853 93.80160415 261.44458 3.47138 GLMP . . . glycosylated lysosomal membrane protein . . . . . 0.07356 0.09409 0.020302773 55.60863411 . . GLO1 0.000220688734065718 0.74301799431605 0.256761316949884 glyoxalase I FUNCTION: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF- kappa-B. Required for normal osteoclastogenesis. {ECO:0000269|PubMed:19199007, ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9705294}.; . . . . 0.35016 0.90621 -0.05129383 49.75819769 2572.91849 9.48113 GLOD4 8.10949511197997e-05 0.765054321687701 0.234864583361179 glyoxalase domain containing 4 . . TISSUE SPECIFICITY: Expressed in heart, brain, liver, kidney, pancreas and placenta. Not expressed in skeletal muscle and lung. {ECO:0000269|PubMed:11642406}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;blood;lens;skeletal muscle;breast;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;synovium;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;small intestine;islets of Langerhans;pancreas;lung;pia mater;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion; 0.10371 0.08655 -0.135838822 43.77211607 237.64347 3.32856 GLOD5 0.0460777312018374 0.674577832764732 0.279344436033431 glyoxalase domain containing 5 . . . unclassifiable (Anatomical System);lung;cartilage;testis;kidney; . 0.19902 0.11026 0.836034065 88.17527719 222.01723 3.22235 GLP1R 0.0640780487665267 0.935275507344299 0.000646443889174809 glucagon like peptide 1 receptor FUNCTION: This is a receptor for glucagon-like peptide 1. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.; . . . . 0.12670 0.25668 0.134171522 63.57041755 2392.4607 9.07868 GLP2R 1.03528817609606e-07 0.925801050503668 0.0741988459675149 glucagon-like peptide 2 receptor FUNCTION: This is a receptor for glucagon-like peptide 2. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.; . . lung;cervix; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05999 0.14665 1.023320772 91.04741684 675.48654 5.19149 GLRA1 0.0764924553316808 0.921120403986622 0.00238714068169755 glycine receptor alpha 1 FUNCTION: The glycine receptor is a neurotransmitter-gated ion channel. Binding of glycine to its receptor increases the chloride conductance and thus produces hyperpolarization (inhibition of neuronal firing).; DISEASE: Hyperekplexia 1 (HKPX1) [MIM:149400]: A neurologic disorder characterized by muscular rigidity of central nervous system origin, particularly in the neonatal period, and by an exaggerated startle response to unexpected acoustic or tactile stimuli. {ECO:0000269|PubMed:10514101, ECO:0000269|PubMed:7611730, ECO:0000269|PubMed:7881416, ECO:0000269|PubMed:7981700, ECO:0000269|PubMed:8298642, ECO:0000269|PubMed:8571969, ECO:0000269|PubMed:8733061, ECO:0000269|PubMed:9067762, ECO:0000269|PubMed:9920650, ECO:0000269|Ref.10}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.31125 0.20061 -0.512444034 21.55579146 149.47271 2.66552 GLRA2 0.908587632299454 0.0912662271677071 0.00014614053283916 glycine receptor alpha 2 FUNCTION: The glycine receptor is a neurotransmitter-gated ion channel. Binding of glycine to its receptor increases the chloride conductance and thus produces hyperpolarization (inhibition of neuronal firing).; . . unclassifiable (Anatomical System);whole body;hypothalamus;hippocampus;retina; superior cervical ganglion;trigeminal ganglion; 0.66711 0.31094 -0.095386216 46.48502005 12.68155 0.46281 GLRA3 0.0437525585382368 0.956008802077829 0.000238639383934058 glycine receptor alpha 3 FUNCTION: The glycine receptor is a neurotransmitter-gated ion channel. Binding of glycine to its receptor increases the chloride conductance and thus produces hyperpolarization (inhibition of neuronal firing).; . TISSUE SPECIFICITY: Widely distributed throughout the central nervous system.; unclassifiable (Anatomical System);ovary;placenta;parathyroid;blood;germinal center;bone marrow; dorsal root ganglion;superior cervical ganglion;uterus corpus;temporal lobe;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.45993 0.16306 -0.66859065 15.76433121 37.91689 1.12606 GLRA4 4.1690448487125e-05 0.625760410127138 0.374197899424375 glycine receptor alpha 4 FUNCTION: The glycine receptor is a neurotransmitter-gated ion channel. Binding of glycine to its receptor increases the chloride conductance and thus produces hyperpolarization (inhibition of neuronal firing).; . . . . 0.48437 0.09986 1.174022298 92.72823779 1295.84706 6.77588 GLRB 0.0269281197941717 0.970615134657015 0.00245674554881286 glycine receptor beta FUNCTION: The glycine receptor is a neurotransmitter-gated ion channel. Binding of glycine to its receptor increases the chloride conductance and thus produces hyperpolarization (inhibition of neuronal firing).; DISEASE: Hyperekplexia 2 (HKPX2) [MIM:614619]: A neurologic disorder characterized by muscular rigidity of central nervous system origin, particularly in the neonatal period, and by an exaggerated startle response to unexpected acoustic or tactile stimuli. {ECO:0000269|PubMed:11929858, ECO:0000269|PubMed:21391991}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;hypothalamus;colon;parathyroid;fovea centralis;uterus;lung;frontal lobe;endometrium;thyroid;placenta;macula lutea;hippocampus;pituitary gland;liver;kidney;brain;pineal gland;mammary gland;stomach;cerebellum; amygdala;whole brain;occipital lobe;medulla oblongata;thalamus;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.72074 0.14782 -1.001120478 8.321538099 40.74042 1.19393 GLRX 0.000187398851916141 0.277796477278761 0.722016123869323 glutaredoxin FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;bone;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;cerebellum cortex;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;liver;cervix;spleen;kidney;mammary gland;stomach;thymus; superior cervical ganglion;placenta;kidney;whole blood;skeletal muscle; 0.08971 0.34230 -0.207437529 38.2814343 7.01678 0.26341 GLRX2 6.50645483475157e-05 0.285670735680128 0.714264199771524 glutaredoxin 2 FUNCTION: Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release. {ECO:0000269|PubMed:11297543, ECO:0000269|PubMed:14676218, ECO:0000269|PubMed:15328416, ECO:0000269|PubMed:15649413}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta and lung. Not expressed in peripheral blood leukocytes. {ECO:0000269|PubMed:11297543, ECO:0000269|PubMed:15184054, ECO:0000269|PubMed:15297967}.; . . 0.30018 0.11278 0.391453969 75.87284737 9.4597 0.34847 GLRX3 0.629710154906928 0.369983474198136 0.000306370894935863 glutaredoxin 3 FUNCTION: Critical negative regulator of cardiac hypertrophy and a positive inotropic regulator (By similarity). Crucial regulator of cellular iron homeostasis and hemoglobin maturation. May play a role in regulating the function of the thioredoxin system. Does not posses any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity. {ECO:0000250, ECO:0000269|PubMed:23615448}.; . TISSUE SPECIFICITY: Expressed in heart, spleen, testis and, to a lower extent, in thymus and peripheral blood leukocytes. Weakly expressed in lung, placenta, colon and small intestine.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;optic nerve;endometrium;bone;testis;germinal center;brain;lymph node;islets of Langerhans;lens;lung;placenta;visual apparatus;macula lutea;liver;alveolus;spleen; dorsal root ganglion;testis - interstitial;superior cervical ganglion;tongue;atrioventricular node;pons;skin;skeletal muscle;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.47187 0.14227 -0.071520315 48.34866714 2511.66261 9.33390 GLRX3P1 . . . glutaredoxin 3 pseudogene 1 . . . . . . . . . . . GLRX3P2 . . . glutaredoxin 3 pseudogene 2 . . . . . . . . . . . GLRX5 0.626214086667008 0.342826078930465 0.0309598344025278 glutaredoxin 5 FUNCTION: Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (PubMed:20364084). Required for normal iron homeostasis. Required for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1 (PubMed:20364084). May protect cells against apoptosis due to reactive oxygen species and oxidative stress (By similarity). {ECO:0000250|UniProtKB:P30153, ECO:0000269|PubMed:20364084}.; DISEASE: Anemia, sideroblastic, pyridoxine-refractory, autosomal recessive (PRARSA) [MIM:205950]: A form of sideroblastic anemia not responsive to pyridoxine. Sideroblastic anemia is characterized by anemia of varying severity, hypochromic peripheral erythrocytes, systemic iron overload secondary to chronic ineffective erythropoiesis, and the presence of bone marrow ringed sideroblasts. Sideroblasts are characterized by iron-loaded mitochondria clustered around the nucleus. {ECO:0000269|PubMed:17485548, ECO:0000269|PubMed:20364084, ECO:0000269|PubMed:25342667, ECO:0000269|PubMed:26100117}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;epididymis;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;thymus; amygdala;whole brain;fetal liver;testis - interstitial;placenta;liver;tumor;kidney;bone marrow; 0.11222 0.19900 . . 728.75601 5.35907 GLRXP1 . . . glutaredoxin (thioltransferase) pseudogene 1 . . . . . . . . . . . GLRXP2 . . . glutaredoxin (thioltransferase) pseudogene 2 . . . . . . . . . . . GLRXP3 . . . glutaredoxin (thioltransferase) pseudogene 3 . . . . . 0.08782 0.07814 . . . . GLS 0.999302599696976 0.000697400123017496 1.80006401100286e-10 glutaminase FUNCTION: Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate in the brain. Isoform 2 lacks catalytic activity.; . TISSUE SPECIFICITY: Isoform 1 and isoform 3 are detected in brain cortex. Isoform 3 is highly expressed in astrocytoma, ganglioglioma and ependymoma. Isoform 1 is highly expressed in brain and kidney, but not detected in liver. Isoform 3 is highly expressed in heart and pancreas, detected at lower levels in placenta, lung, pancreas and kidney, but is not detected in liver. Isoform 2 is expressed in cardiac and skeletal muscle. {ECO:0000269|PubMed:11015561}.; umbilical cord;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;kidney;stomach;aorta;thymus; amygdala;dorsal root ganglion;whole brain;superior cervical ganglion;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;atrioventricular node;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.13416 . 0.148941568 64.31941496 124.96269 2.43077 GLS2 0.0009871223239844 0.998909879984021 0.000102997691994184 glutaminase 2 FUNCTION: Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha-ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production. May play a role in preventing tumor proliferation. {ECO:0000269|PubMed:20378837}.; . TISSUE SPECIFICITY: Highly expressed in liver. Expressed in brain and pancreas. Not observed in heart, placenta, lung, skeletal muscle and kidney. Expression is significantly reduced in hepatocellular carcinomas. {ECO:0000269|PubMed:10620514, ECO:0000269|PubMed:20378837}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;testis;bladder;brain;unclassifiable (Anatomical System);heart;pharynx;blood;skeletal muscle;bile duct;breast;lung;placenta;visual apparatus;hippocampus;liver;spleen;kidney;stomach; medulla oblongata;subthalamic nucleus;liver;globus pallidus;pons;parietal lobe; 0.67720 0.28130 -0.53631094 20.53550366 556.03172 4.79013 GLT1D1 9.15081325034839e-05 0.787823530771055 0.212084961096441 glycosyltransferase 1 domain containing 1 . . . unclassifiable (Anatomical System);prostate;smooth muscle;ovary;hypothalamus;macula lutea;visual apparatus;liver;testis;spleen;blood;fovea centralis;brain;bone marrow; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;pons;trigeminal ganglion; 0.14436 . 0.15257911 64.60839821 172.50596 2.86144 GLT6D1 0.00318828821641753 0.822952939172666 0.173858772610917 glycosyltransferase 6 domain containing 1 . . TISSUE SPECIFICITY: Expressed in both healthy and inflamed gingival tissue samples at similar levels, with higher expression in the gingival connective tissue compared to gingival epithelium. Strongest expression in testis, followed by leukocytes. {ECO:0000269|PubMed:19897590}.; . . 0.04797 0.08893 1.330184494 94.17315405 3212.14932 10.80471 GLT8D1 0.00348977535071494 0.986780692655875 0.00972953199341029 glycosyltransferase 8 domain containing 1 . . . ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;gall bladder;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;placenta;duodenum;kidney;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;thyroid;testis;trigeminal ganglion; 0.08875 . -0.071520315 48.34866714 240.47267 3.34964 GLT8D2 3.34398984119123e-07 0.544155092739301 0.455844572861715 glycosyltransferase 8 domain containing 2 . . . unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;colon;blood;skin;skeletal muscle;retina;uterus;pancreas;prostate;whole body;lung;trabecular meshwork;bone;placenta;pituitary gland;amnion;testis;kidney;brain;mammary gland;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.12150 . -0.113792788 45.25831564 78.91487 1.87658 GLTP 0.22708870640821 0.737737795369964 0.0351734982218257 glycolipid transfer protein FUNCTION: Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides. {ECO:0000269|PubMed:15329726, ECO:0000269|PubMed:15504043, ECO:0000269|PubMed:17980653, ECO:0000269|PubMed:18261224}.; . TISSUE SPECIFICITY: Detected in fibroblasts (at protein level). Detected in fibroblasts and in various cancer cell lines. {ECO:0000269|PubMed:17980653, ECO:0000269|PubMed:18261224}.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;urinary;colon;skin;skeletal muscle;pancreas;lung;larynx;nasopharynx;visual apparatus;hippocampus;iris;hypopharynx;liver;testis;head and neck;germinal center;mammary gland; dorsal root ganglion;skeletal muscle;parietal lobe; . 0.15588 -0.139478553 43.29440906 22.60764 0.75634 GLTPD2 0.0259777981808854 0.786792453287109 0.187229748532006 glycolipid transfer protein domain containing 2 . . . unclassifiable (Anatomical System);islets of Langerhans;visual apparatus;liver;colon;kidney; . 0.12003 . . . 836.46884 5.66475 GLTPP1 . . . glycolipid transfer protein pseudogene 1 . . . . . . . . . . . GLTSCR1 0.997123313976457 0.002876546884163 1.39139379639844e-07 glioma tumor suppressor candidate region gene 1 . . TISSUE SPECIFICITY: Expressed at moderate levels in heart, brain, placenta, skeletal muscle, and pancreas, and at lower levels in lung, liver and kidney. {ECO:0000269|PubMed:10708517}.; . . 0.16010 0.12546 . . 3165.7821 10.72264 GLTSCR1-AS1 . . . GLTSCR1 antisense RNA 1 . . . . . . . . . . . GLTSCR1L 0.999918135203136 8.18647730707571e-05 2.37937447431562e-11 GLTSCR1 like . . . . . 0.40714 0.08685 -0.573127851 18.96083982 233.74152 3.30473 GLTSCR2 0.253946323601522 0.744798311314433 0.00125536508404471 glioma tumor suppressor candidate region gene 2 . . TISSUE SPECIFICITY: Expressed at high levels in heart and pancreas, moderate levels in placenta, liver, skeletal muscle, and kidney, and low levels in brain and lung. {ECO:0000269|PubMed:10708517}.; lymphoreticular;medulla oblongata;ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;synovium;bone;iris;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;islets of Langerhans;muscle;urinary;blood;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; . 0.62172 0.18135 0.400544645 76.40953055 729.54176 5.36136 GLTSCR2-AS1 . . . GLTSCR2 antisense RNA 1 . . . . . . . . . . . GLUD1 0.0139354648468801 0.979595033893377 0.00646950125974286 glutamate dehydrogenase 1 FUNCTION: Mitochondrial glutamate dehydrogenase that converts L- glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity). {ECO:0000250}.; DISEASE: Familial hyperinsulinemic hypoglycemia 6 (HHF6) [MIM:606762]: Familial hyperinsulinemic hypoglycemia [MIM:256450], also referred to as congenital hyperinsulinism, nesidioblastosis, or persistent hyperinsulinemic hypoglycemia of infancy (PPHI), is the most common cause of persistent hypoglycemia in infancy and is due to defective negative feedback regulation of insulin secretion by low glucose levels. In HHF6 elevated oxidation rate of glutamate to alpha-ketoglutarate stimulates insulin secretion in the pancreatic beta cells, while they impair detoxification of ammonium in the liver. {ECO:0000269|PubMed:10636977, ECO:0000269|PubMed:11214910, ECO:0000269|PubMed:11297618, ECO:0000269|PubMed:9571255}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;spinal cord;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;larynx;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; whole brain;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;thalamus;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;fetal liver;subthalamic nucleus;liver;prefrontal cortex;globus pallidus;kidney;cingulate cortex;parietal lobe; 0.45386 0.70938 -0.029247611 51.40363293 74.75678 1.80903 GLUD1P2 . . . glutamate dehydrogenase 1 pseudogene 2 . . . . . . . . . . . GLUD1P3 . . . glutamate dehydrogenase 1 pseudogene 3 . . . . . . . . . . . GLUD1P4 . . . glutamate dehydrogenase 1 pseudogene 4 . . . . . . . . . . . GLUD1P5 . . . glutamate dehydrogenase 1 pseudogene 5 . . . . . . . . . . . GLUD1P6 . . . glutamate dehydrogenase 1 pseudogene 6 . . . . . . . . . . . GLUD1P7 . . . glutamate dehydrogenase 1 pseudogene 7 . . . . . . . . . . . GLUD1P8 . . . glutamate dehydrogenase 1 pseudogene 8 . . . . . . . . . . . GLUD1P9 . . . glutamate dehydrogenase 1 pseudogene 9 . . . . . . . . . . . GLUD2 0.0713078915604148 0.741068911909808 0.187623196529777 glutamate dehydrogenase 2 FUNCTION: Important for recycling the chief excitatory neurotransmitter, glutamate, during neurotransmission.; . TISSUE SPECIFICITY: Expressed in retina, testis and, at a lower level, brain.; unclassifiable (Anatomical System);lymph node;colon;blood;skin;bone marrow;breast;lung;endometrium;thyroid;placenta;hippocampus;liver;testis;head and neck;spleen;kidney;brain;stomach; amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;pons;caudate nucleus;fetal liver;globus pallidus;testis;ciliary ganglion;kidney;trigeminal ganglion;parietal lobe;cingulate cortex; 0.12079 0.62023 0.150760231 64.51403633 183.33854 2.93763 GLUL 0.977842592811399 0.0221367836954847 2.06234931168032e-05 glutamate-ammonia ligase FUNCTION: This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner (By similarity). Essential for proliferation of fetal skin fibroblasts. {ECO:0000250, ECO:0000269|PubMed:18662667}.; DISEASE: Congenital systemic glutamine deficiency (CSGD) [MIM:610015]: Rare developmental disorder with severe brain malformation resulting in multi-organ failure and neonatal death. Glutamine is largely absent from affected patients serum, urine and cerebrospinal fluid. {ECO:0000269|PubMed:16267323}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;oesophagus;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;blood;cerebrum;lens;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;alveolus;liver;spleen;kidney;mammary gland;stomach;thymus; adipose tissue; 0.28656 0.78759 -0.427900189 25.14744043 14.61592 0.52701 GLULP1 . . . glutamate-ammonia ligase (glutamine synthetase) pseudogene 1 . . . . . . . . . . . GLULP2 . . . glutamate-ammonia ligase (glutamine synthetase) pseudogene 2 . . . . . . . . . . . GLULP3 . . . glutamate-ammonia ligase (glutamine synthetase) pseudogene 3 . . . . . . . . . . . GLULP4 . . . glutamate-ammonia ligase (glutamine synthetase) pseudogene 4 . . . . . . . . . . . GLULP5 . . . glutamate-ammonia ligase (glutamine synthetase) pseudogene 5 . . . . . . . . . . . GLULP6 . . . glutamate-ammonia ligase (glutamine synthetase) pseudogene 6 . . . . . . . . . . . GLYAT 8.03824153928287e-05 0.526615154377704 0.473304463206903 glycine-N-acyltransferase FUNCTION: Mitochondrial acyltransferase which transfers an acyl group to the N-terminus of glycine and glutamine, although much less efficiently. Can conjugate numerous substrates to form a variety of N-acylglycines, with a preference for benzoyl-CoA over phenylacetyl-CoA as acyl donors. Thereby detoxify xenobiotics, such as benzoic acid or salicylic acid, and endogenous organic acids, such as isovaleric acid. {ECO:0000269|PubMed:22475485, ECO:0000269|PubMed:7802672}.; . TISSUE SPECIFICITY: Predominantly expressed in liver (at protein level) and kidney. Down-regulated in hepatocellular carcinoma and other liver cancers. {ECO:0000269|PubMed:22475485}.; unclassifiable (Anatomical System);liver;spleen;kidney; dorsal root ganglion;superior cervical ganglion;liver;appendix;ciliary ganglion;atrioventricular node;kidney;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.09105 0.27434 0.238945317 69.20853975 153.69996 2.71087 GLYATL1 6.26859114623908e-05 0.898251587721717 0.10168572636682 glycine-N-acyltransferase like 1 FUNCTION: Acyltransferase which transfers an acyl group to the N- terminus of glutamine. Can use phenylacetyl-CoA as an acyl donor. {ECO:0000269|PubMed:22475485}.; . TISSUE SPECIFICITY: Expressed in liver and kidney and, at lower levels, in pancreas, testis, ovary and stomach. {ECO:0000269|Ref.1}.; unclassifiable (Anatomical System);prostate;lung;pineal body;liver;colon;parathyroid;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.05663 . -1.155457828 6.168907761 6.92195 0.25823 GLYATL1P1 . . . glycine-N-acyltransferase like 1 pseudogene 1 . . . . . . . . . . . GLYATL1P2 . . . glycine-N-acyltransferase like 1 pseudogene 2 . . . . . . . . . . . GLYATL1P3 . . . glycine-N-acyltransferase like 1 pseudogene 3 . . . . . . . . . . . GLYATL1P4 . . . glycine-N-acyltransferase like 1 pseudogene 4 . . . . . . . . . . . GLYATL2 9.09624563195602e-11 0.0114012575444402 0.988598742364597 glycine-N-acyltransferase like 2 FUNCTION: Mitochondrial acyltransferase which transfers the acyl group to the N-terminus of glycine. Conjugates numerous substrates, such as arachidonoyl-CoA and saturated medium and long-chain acyl-CoAs ranging from chain-length C8:0-CoA to C18:0- CoA, to form a variety of N-acylglycines. Shows a preference for monounsaturated fatty acid oleoyl-CoA (C18:1-CoA) as an acyl donor. Does not exhibit any activity toward C22:6-CoA and chenodeoxycholoyl-CoA, nor toward serine or alanine. {ECO:0000269|PubMed:20305126}.; . TISSUE SPECIFICITY: Expressed at highest levels in salivary gland and trachea. Also detected in thyroid gland, spinal cord, prostate, lung and fetal brain. {ECO:0000269|PubMed:20305126}.; unclassifiable (Anatomical System);brain; superior cervical ganglion;trigeminal ganglion; 0.08561 . 0.949904335 90.00943619 133.78349 2.51554 GLYATL3 . . . glycine-N-acyltransferase like 3 FUNCTION: Acyltransferase which transfers the acyl group to the N- terminus of glycine. {ECO:0000250}.; . . . . . . 0.459411326 78.28497287 9266.94585 20.87204 GLYB . . . glycine B complementing . . . . . . . . . . . GLYCAM1 . . . glycosylation dependent cell adhesion molecule 1 (pseudogene) . . TISSUE SPECIFICITY: Expressed in cells harvested from milk of lactating women. Not found in other tissues. {ECO:0000269|PubMed:12057858}.; . . . . . . . . GLYCTK 1.36482731873284e-06 0.217511979436582 0.7824866557361 glycerate kinase . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16753811}.; unclassifiable (Anatomical System);colon;skin;pancreas;prostate;lung;bone;placenta;liver;testis;spleen;germinal center;kidney;brain;mammary gland;stomach;thymus; . 0.03971 0.18636 0.242582624 69.45623968 309.95494 3.74502 GLYCTK-AS1 . . . GLYCTK antisense RNA 1 . . . . . . . . . . . GLYR1 0.999877719491225 0.00012228044553991 6.32346940432907e-11 glyoxylate reductase 1 homolog (Arabidopsis) FUNCTION: May have oxidoreductase activity. Regulates p38 MAP kinase activity by mediating stress activation of p38alpha/MAPK14 and specifically regulating MAPK14 signaling. Indirectly promotes phosphorylation of MAPK14 and activation of ATF2. The phosphorylation of MAPK14 requires upstream activity of MAP2K4 and MAP2K6. Recruited on chromatin, recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). {ECO:0000269|PubMed:16352664, ECO:0000269|PubMed:20850016}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;endometrium;synovium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;spinal cord;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; amygdala;medulla oblongata;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex;cerebellum; . . -0.890882376 10.30313753 24.61709 0.80872 GLYS1 . . . glycosuria 1, renal . . . . . . . . . . . GM2A 0.111186454530615 0.777402352408525 0.11141119306086 GM2 ganglioside activator FUNCTION: The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity (By similarity). Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta- hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3. {ECO:0000250}.; DISEASE: GM2-gangliosidosis AB (GM2GAB) [MIM:272750]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. It is characterized by GM2 gangliosides accumulation in the presence of both normal hexosaminidase A and B. {ECO:0000269|PubMed:1915858, ECO:0000269|PubMed:8244332, ECO:0000269|PubMed:8900233}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;pharynx;blood;skeletal muscle;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;hypopharynx;duodenum;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;lung;placenta;trigeminal ganglion; 0.26723 0.19354 0.681699246 84.93158764 326.06898 3.83913 GM2AP1 . . . GM2 ganglioside activator pseudogene 1 . . . . . . . . . . . GM2AP2 . . . GM2 ganglioside activator pseudogene 2 . . . . . . . . . . . GMCL1 9.6231886938057e-06 0.984465205579307 0.0155251712319993 germ cell-less, spermatogenesis associated 1 FUNCTION: Possible function in spermatogenesis. Enhances the degradation of MDM2 and increases the amount of p53 probably by modulating the nucleocytoplasmic transport (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;colon;skin;bone marrow;uterus;prostate;testis;germinal center;brain;unclassifiable (Anatomical System);small intestine;cartilage;cerebellum cortex;islets of Langerhans;blood;skeletal muscle;breast;lung;adrenal gland;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; . 0.11371 -0.448125345 24.19202642 77.54664 1.85338 GMCL1P1 . . . germ cell-less, spermatogenesis associated 1 pseudogene 1 FUNCTION: Possible function in spermatogenesis. Enhances the degradation of MDM2 and increases the amount of p53 probably by modulating the nucleocytoplasmic transport (By similarity). Probable substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250, ECO:0000269|PubMed:14528312}.; . . . . . 0.11371 . . . . GMCL1P2 . . . germ cell-less, spermatogenesis associated 1 pseudogene 2 . . . . . . . . . . . GMDS 0.997690128557445 0.00230978997893162 8.14636237801715e-08 GDP-mannose 4,6-dehydratase FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4- dehydro-6-deoxy-D-mannose.; . . . . 0.20350 0.22881 -0.295622497 32.61972163 12.57528 0.45910 GMDS-AS1 . . . GMDS antisense RNA 1 (head to head) . . . . . . . . . . . GMEB1 0.960593932192331 0.0393886443935074 1.74234141612071e-05 glucocorticoid modulatory element binding protein 1 FUNCTION: Trans-acting factor that binds to glucocorticoid modulatory elements (GME) present in the TAT (tyrosine aminotransferase) promoter and increases sensitivity to low concentrations of glucocorticoids. Binds also to the transferrin receptor promoter. Essential auxiliary factor for the replication of parvoviruses.; . . ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;muscle;pharynx;blood;lens;breast;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.22159 . -0.47017169 23.25430526 29.05249 0.92942 GMEB2 0.990659130636514 0.00933839655370025 2.47280978561433e-06 glucocorticoid modulatory element binding protein 2 FUNCTION: Trans-acting factor that binds to glucocorticoid modulatory elements (GME) present in the TAT (tyrosine aminotransferase) promoter and increases sensitivity to low concentrations of glucocorticoids. Binds also to the transferrin receptor promoter. Essential auxiliary factor for the replication of parvoviruses.; . TISSUE SPECIFICITY: Expressed in peripheral blood lymphocytes and fetal liver. Expressed preferentially in reproductive and/or developmentally important cells, such as testis, placenta, bone marrow and fetal tissues.; lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;thymus; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.29677 0.10651 -0.732911333 14.07761264 28.70202 0.91871 GMFA . . . glia maturation factor alpha . . . . . . . . . . . GMFB 0.323144112210257 0.660656266296019 0.0161996214937231 glia maturation factor beta FUNCTION: This protein causes differentiation of brain cells, stimulation of neural regeneration, and inhibition of proliferation of tumor cells.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;head and neck;cervix;kidney;stomach; dorsal root ganglion;amygdala;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;olfactory bulb;hypothalamus;temporal lobe;spinal cord;atrioventricular node;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.77300 0.19194 -0.009020804 52.8544468 5.74474 0.21578 GMFBP1 . . . glia maturation factor beta pseudogene 1 . . . . . . . . . . . GMFG 1.91273633031565e-05 0.459667684107355 0.540313188529341 glia maturation factor gamma . . TISSUE SPECIFICITY: Expressed predominantly in lung, heart and placenta.; umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;thyroid;testis;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;aorta;stomach; white blood cells;whole blood;thymus;bone marrow; 0.54387 0.13479 -0.029247611 51.40363293 98.83545 2.14902 GMIP 7.29298933296636e-05 0.999749041774764 0.000178028331906577 GEM interacting protein FUNCTION: Stimulates, in vitro and in vivo, the GTPase activity of RhoA. {ECO:0000269|PubMed:12093360}.; . . colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;blood;lens;pancreas;lung;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;thyroid;white blood cells;whole blood;trigeminal ganglion; 0.42947 0.12719 0.319642692 72.82967681 407.18097 4.23092 GML 0.439134841904715 0.530642518663555 0.0302226394317294 glycosylphosphatidylinositol anchored molecule like FUNCTION: May play a role in the apoptotic pathway or cell-cycle regulation induced by p53/TP53 after DNA damage.; . . . . 0.04983 0.08759 0.549415813 81.38122199 2327.47979 8.94080 GMNC . . . geminin coiled-coil domain containing FUNCTION: Regulator of DNA replication. Promotes initiation of chromosomal DNA replication by mediating TOPBP1- and CDK2- dependent recruitment of CDC45L onto replication origins (By similarity). {ECO:0000250}.; . . . . . . 1.414757139 94.83958481 4297.05431 13.03212 GMNN 0.607453614744368 0.383923952097351 0.00862243315828106 geminin, DNA replication inhibitor FUNCTION: Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC). It is degraded during the mitotic phase of the cell cycle. Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle.; . . medulla oblongata;ovary;colon;parathyroid;skin;uterus;prostate;frontal lobe;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; testis - interstitial;fetal liver;superior cervical ganglion;testis; 0.42797 0.17974 0.99218692 90.51663128 1758.98161 7.73865 GMPPA 2.35237377979873e-06 0.904520375705181 0.0954772719210394 GDP-mannose pyrophosphorylase A FUNCTION: May serve as a regulatory subunit and allow allosteric feedback inhibition of GMPPB by GDP-mannose. {ECO:0000269|PubMed:24035193}.; . TISSUE SPECIFICITY: Expressed in fibroblasts (at protein level). {ECO:0000269|PubMed:24035193}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;synovium;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;liver;pons;skeletal muscle; 0.36841 0.11533 -0.290161348 33.33923095 53.14173 1.44700 GMPPB 8.24535896597197e-05 0.768249593922664 0.231667952487676 GDP-mannose pyrophosphorylase B . DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A14 (MDDGA14) [MIM:615350]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with brain anomalies, eye malformations, and profound mental retardation. The disorder includes a severe form designated as Walker-Warburg syndrome and a less severe phenotype known as muscle-eye-brain disease. MDDGA14 features include increased muscle tone, microcephaly, cleft palate, feeding difficulties, severe muscle weakness, sensorineural hearing loss, cerebellar hypoplasia, ataxia, and retinal dysfunction. {ECO:0000269|PubMed:23768512}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Muscular dystrophy-dystroglycanopathy congenital with mental retardation B14 (MDDGB14) [MIM:615351]: A congenital muscular dystrophy characterized by severe muscle weakness apparent in infancy and mental retardation. Some patients may have additional features, such as microcephaly, cardiac dysfunction, seizures, or cerebellar hypoplasia. {ECO:0000269|PubMed:23768512}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C14 (MDDGC14) [MIM:615352]: An autosomal recessive form of muscular dystrophy characterized by mild proximal muscle weakness with onset in early childhood. Some patients may have additional features, such as mild intellectual disability or seizures. {ECO:0000269|PubMed:23768512}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;hypothalamus;blood;lens;skeletal muscle;bile duct;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; . 0.82507 0.19615 -0.336073593 30.55555556 48.18496 1.35260 GMPR 0.00252568644042527 0.931077240580624 0.0663970729789504 guanosine monophosphate reductase FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. {ECO:0000255|HAMAP-Rule:MF_03195}.; . . ovary;colon;parathyroid;skin;uterus;prostate;frontal lobe;endometrium;larynx;thyroid;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;testis - seminiferous tubule;testis;skeletal muscle; 0.17422 0.21865 -0.314027422 31.9297004 85.22384 1.96783 GMPR2 0.000987612921603035 0.945330015412194 0.0536823716662034 guanosine monophosphate reductase 2 FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides (PubMed:12009299, PubMed:12669231, PubMed:16359702, PubMed:22037469). Plays a role in modulating cellular differentiation (PubMed:12669231). {ECO:0000255|HAMAP- Rule:MF_03195, ECO:0000269|PubMed:12009299, ECO:0000269|PubMed:12669231, ECO:0000269|PubMed:16359702, ECO:0000269|PubMed:22037469}.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, kidney, brain, liver, prostate, spleen, placenta, testis and ovary. Low expression in colon, thymus and peripheral blood leukocytes. {ECO:0000269|PubMed:12009299, ECO:0000269|PubMed:12669231}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;cerebellum;thymus; occipital lobe;thalamus;caudate nucleus;kidney;pons; 0.08646 0.24855 -0.181750739 40.15687662 135.26118 2.53022 GMPS 0.993904305716876 0.00609565863040834 3.56527153912458e-08 guanine monophosphate synthase FUNCTION: Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division.; DISEASE: Note=A chromosomal aberration involving GMPS is found in acute myeloid leukemias. Translocation t(3,11)(q25,q23) with KMT2A/MLL1.; . ovary;salivary gland;intestine;colon;skin;uterus;prostate;frontal lobe;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;spinal cord;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;tumor;testis;atrioventricular node; 0.83069 0.53341 -0.247889024 35.98726115 62.16037 1.60798 GMPSP1 . . . guanine monophosphate synthase pseudogene 1 . . . . . . . . . . . GNA11 0.966183014336431 0.0337583383420937 5.86473214752704e-05 G protein subunit alpha 11 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C.; DISEASE: Hypocalciuric hypercalcemia, familial 2 (HHC2) [MIM:145981]: A form of hypocalciuric hypercalcemia, a disorder of mineral homeostasis that is transmitted as an autosomal dominant trait with a high degree of penetrance. It is characterized biochemically by lifelong elevation of serum calcium concentrations and is associated with inappropriately low urinary calcium excretion and a normal or mildly elevated circulating parathyroid hormone level. Hypermagnesemia is typically present. Affected individuals are usually asymptomatic and the disorder is considered benign. However, chondrocalcinosis and pancreatitis occur in some adults. {ECO:0000269|PubMed:23802516}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hypocalcemia, autosomal dominant 2 (HYPOC2) [MIM:615361]: A form of hypocalcemia, a disorder of mineral homeostasis characterized by blood calcium levels below normal, and low or normal serum parathyroid hormone concentrations. Disease manifestations include hypocalcemia, paresthesias, carpopedal spasm, seizures, hypercalciuria with nephrocalcinosis or kidney stones, and ectopic and basal ganglia calcifications. {ECO:0000269|PubMed:23782177, ECO:0000269|PubMed:23802516}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:18703424}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;synovium;bone;thyroid;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;bile duct;lung;cornea;placenta;visual apparatus;liver;kidney;mammary gland;stomach;cerebellum;thymus; amygdala;medulla oblongata;testis - interstitial;occipital lobe;superior cervical ganglion;cerebellum peduncles;pons;skeletal muscle;prostate;testis - seminiferous tubule;adrenal gland;thyroid;prefrontal cortex;globus pallidus;testis;cingulate cortex;cerebellum; 0.47544 0.17658 -0.137658575 43.57159707 30.42276 0.96949 GNA12 0.908269982155965 0.0910123059953378 0.000717711848697389 G protein subunit alpha 12 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. May play a role in the control of cell migration through the TOR signaling cascade. {ECO:0000269|PubMed:22609986}.; . . smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;bone;pituitary gland;testis;amniotic fluid;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;hypothalamus;muscle;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion; 0.13269 0.21177 -0.471992905 23.03609342 14.33823 0.51800 GNA13 0.533516375005495 0.463163565467446 0.00332005952705895 G protein subunit alpha 13 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.; . TISSUE SPECIFICITY: Expressed in testis, including in Leydig cells and in the seminiferous epithelium, in differentiating cells from the spermatogonia to mature spermatozoa stages and round spermatids (at protein level). Expressed in 99.2% of spermatozoa from healthy individuals, but only in 28.6% of macrocephalic spermatozoa from infertile patients (at protein level). {ECO:0000269|PubMed:18703424}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;trabecular meshwork;placenta;visual apparatus;alveolus;liver;cervix;head and neck;kidney;mammary gland;aorta;stomach;thymus; . 0.22564 0.12009 0.082802743 60.09082331 89.77367 2.03756 GNA14 6.82392732529186e-10 0.0702689355571555 0.929731063760452 G protein subunit alpha 14 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.; . . . . 0.31433 0.13990 -0.134019284 43.90776126 89.27799 2.03082 GNA14-AS1 . . . GNA14 antisense RNA 1 . . . . . . . . . . . GNA15 0.306963811881902 0.689125445691136 0.00391074242696207 G protein subunit alpha 15 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.; . TISSUE SPECIFICITY: Specifically expressed in hematopoietic cells. Expressed in epididymis (at protein level). {ECO:0000269|PubMed:20736409}.; unclassifiable (Anatomical System);smooth muscle;cartilage;heart;ovary;colon;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;larynx;placenta;macula lutea;liver;testis;head and neck;spleen;bladder;stomach;thymus; . 0.06813 . -0.490397599 22.50530786 101.86504 2.18376 GNAI1 0.917528243665787 0.0823595451770563 0.000112211157156691 G protein subunit alpha i1 FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:8774883, PubMed:18434541). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (By similarity). The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. Required for normal cytokinesis during mitosis (PubMed:17635935). {ECO:0000250|UniProtKB:P10824, ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:8774883}.; . . colon;fovea centralis;choroid;skin;retina;uterus;subthalamic nucleus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;amniotic fluid;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;aorta; amygdala; 0.45411 0.08286 -0.161524709 41.6430762 25.65134 0.83582 GNAI2 0.861160290278213 0.138404502167127 0.000435207554659622 G protein subunit alpha i2 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. May play a role in cell division. {ECO:0000269|PubMed:17635935}.; . . lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;adrenal cortex;pharynx;blood;greater omentum;breast;visual apparatus;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;choroid;vein;uterus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; parietal lobe; 0.79857 0.25991 -0.337894035 30.37272942 19.39378 0.66714 GNAI2P1 . . . G protein subunit alpha i2 pseudogene 1 . . . . . . . . . . . GNAI2P2 . . . G protein subunit alpha i2 pseudogene 2 . . . . . . . . . . . GNAI3 0.038811277618943 0.954295997368132 0.00689272501292476 G protein subunit alpha i3 FUNCTION: Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:8774883, PubMed:18434541, PubMed:19478087). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (PubMed:19478087). Stimulates the activity of receptor-regulated K(+) channels (PubMed:2535845). The active GTP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division (PubMed:17635935). {ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:2535845, ECO:0000269|PubMed:8774883}.; DISEASE: Auriculocondylar syndrome 1 (ARCND1) [MIM:602483]: An autosomal dominant craniofacial malformation syndrome characterized by variable mandibular anomalies, including mild to severe micrognathia, temporomandibular joint ankylosis, cleft palate, and a characteristic ear malformation that consists of separation of the lobule from the external ear, giving the appearance of a question mark (question-mark ear). Other frequently described features include prominent cheeks, cupped and posteriorly rotated ears, preauricular tags, and microstomia. {ECO:0000269|PubMed:22560091}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.63150 0.15588 -0.251530012 35.42108988 23.17555 0.77382 GNAL 0.987372719895044 0.0126262318879234 1.04821703248664e-06 G protein subunit alpha L FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G(olf) alpha mediates signal transduction within the olfactory neuroepithelium and the basal ganglia. May be involved in some aspect of visual transduction, and in mediating the effect of one or more hormones/neurotransmitters.; . TISSUE SPECIFICITY: Detected in olfactory neuroepithelium, brain, testis, and to a lower extent in retina, lung alveoli, spleen. Trace amounts where seen in kidney, adrenal gland and liver. Found to be expressed in all the insulinomas examined.; uterus;unclassifiable (Anatomical System);lung;frontal lobe;placenta;pituitary gland;testis;brain; amygdala;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;hypothalamus;caudate nucleus;pons;skeletal muscle;fetal brain;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.37028 0.18893 -0.295622497 32.61972163 136.08803 2.53460 GNAO1 0.98428817684836 0.0157029719203003 8.85123133930705e-06 G protein subunit alpha o1 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(o) protein function is not clear. Stimulated by RGS14.; DISEASE: Epileptic encephalopathy, early infantile, 17 (EIEE17) [MIM:615473]: A severe neurologic disorder characterized by onset of intractable seizures in the first weeks or months of life and usually associated with EEG abnormalities. Affected infants have very poor psychomotor development and may have brain abnormalities, such as cerebral atrophy or thin corpus callosum. Some patients may show involuntary movements. {ECO:0000269|PubMed:23993195}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;fovea centralis;choroid;lens;retina;prostate;optic nerve;whole body;lung;frontal lobe;endometrium;adrenal gland;thyroid;macula lutea;testis;brain; whole brain;dorsal root ganglion;amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;atrioventricular node;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.24762 0.17859 -0.736552314 13.93606983 11.79169 0.42714 GNAQ 0.984390020772814 0.0156082147030256 1.76452416021474e-06 G protein subunit alpha q FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity). {ECO:0000250}.; DISEASE: Capillary malformations, congenital (CMC) [MIM:163000]: A form of vascular malformations that are present from birth, tend to grow with the individual, do not regress spontaneously, and show normal rates of endothelial cell turnover. Capillary malformations are distinct from capillary hemangiomas, which are highly proliferative lesions that appear shortly after birth and show rapid growth, slow involution, and endothelial hypercellularity. {ECO:0000269|PubMed:23656586}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Sturge-Weber syndrome (SWS) [MIM:185300]: A syndrome characterized by an intracranial vascular anomaly, leptomeningeal angiomatosis, most often involving the occipital and posterior parietal lobes. The most common features are facial cutaneous vascular malformations (port-wine stains), seizures, and glaucoma. Stasis results in ischemia underlying the leptomeningeal angiomatosis, leading to calcification and laminar cortical necrosis. The clinical course is highly variable and some children experience intractable seizures, mental retardation, and recurrent stroke-like episodes. {ECO:0000269|PubMed:23656586}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in ovary, prostate, testis and colon. Down-regulated in the peripheral blood lymphocytes (PBLs) of rheumatoid arthritis patients (at protein level). {ECO:0000269|PubMed:21923740, ECO:0000269|PubMed:8664309}.; lymphoreticular;colon;skin;uterus;prostate;frontal lobe;cerebral cortex;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;skeletal muscle;breast;lung;nasopharynx;placenta;hippocampus;liver;duodenum;hypopharynx;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;occipital lobe;prefrontal cortex;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.49774 0.43956 -0.251530012 35.42108988 4.88397 0.18068 GNAQP1 . . . G protein subunit alpha q pseudogene 1 . . . . . . . . . . . GNAS 0.9995400816303 0.000459918047113187 3.22586941834638e-10 GNAS complex locus . DISEASE: ACTH-independent macronodular adrenal hyperplasia 1 (AIMAH1) [MIM:219080]: A rare adrenal defect characterized by multiple, bilateral, non-pigmented, benign, adrenocortical nodules. It results in excessive production of cortisol leading to ACTH-independent Cushing syndrome. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes. {ECO:0000269|PubMed:12727968}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pseudohypoparathyroidism 1B (PHP1B) [MIM:603233]: A disorder characterized by end-organ resistance to parathyroid hormone, hypocalcemia and hyperphosphatemia. Patients affected with PHP1B lack developmental defects characteristic of Albright hereditary osteodystrophy, and typically show no other endocrine abnormalities besides resistance to PTH. {ECO:0000269|PubMed:11029463, ECO:0000269|PubMed:11067869, ECO:0000269|PubMed:11294659, ECO:0000269|PubMed:12858292, ECO:0000269|PubMed:14561710, ECO:0000269|PubMed:15592469, ECO:0000269|PubMed:15800843}. Note=The disease is caused by mutations affecting the gene represented in this entry. Most affected individuals have defects in methylation of the gene. In some cases microdeletions involving the STX16 appear to cause loss of methylation at exon A/B of GNAS, resulting in PHP1B. Paternal uniparental isodisomy have also been observed.; DISEASE: GNAS hyperfunction (GNASHYP) [MIM:139320]: This condition is characterized by increased trauma-related bleeding tendency, prolonged bleeding time, brachydactyly and mental retardation. Both the XLas isoforms and the ALEX protein are mutated which strongly reduces the interaction between them and this may allow unimpeded activation of the XLas isoforms. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;amniotic fluid;germinal center;ciliary body;bladder;brain;gall bladder;cartilage;heart;tongue;pineal body;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;greater omentum;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta;cerebellum; amygdala;whole brain;occipital lobe;testis - interstitial;thalamus;medulla oblongata;superior cervical ganglion;cerebellum peduncles;hypothalamus;beta cell islets;temporal lobe;spinal cord;pons;fetal thyroid;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;trigeminal ganglion;cingulate cortex;pituitary;parietal lobe;cerebellum; 0.48401 0.79966 -0.016511957 52.31776362 290.01884 3.64365 GNAS-AS1 . . . GNAS antisense RNA 1 . . . . . . . . . . . GNAT1 2.50523154178956e-06 0.499198865849963 0.500798628918495 G protein subunit alpha transducin 1 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase.; DISEASE: Night blindness, congenital stationary, autosomal dominant 3 (CSNBAD3) [MIM:610444]: A non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia. {ECO:0000269|PubMed:17584859, ECO:0000269|PubMed:8673138}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Night blindness, congenital stationary, 1G (CSNB1G) [MIM:616389]: An autosomal recessive form of congenital stationary night blindness, a non-progressive retinal disorder characterized by impaired night vision or in dim light, with good vision only on bright days. {ECO:0000269|PubMed:22190596}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Rod. Predominantly expressed in the retina followed by the ciliary body, iris and retinal pigment epithelium. {ECO:0000269|PubMed:22190596}.; unclassifiable (Anatomical System);medulla oblongata;optic nerve;lung;macula lutea;visual apparatus;testis;fovea centralis;choroid;lens;brain;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;thalamus;uterus corpus;temporal lobe;globus pallidus;ciliary ganglion;caudate nucleus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.78050 0.18619 -0.60427181 17.74593064 23.3189 0.77807 GNAT2 0.00815865202254078 0.977944340124814 0.0138970078526454 G protein subunit alpha transducin 2 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase.; . TISSUE SPECIFICITY: Retinal rod outer segment.; unclassifiable (Anatomical System);visual apparatus;blood; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.44167 0.16824 0.016664174 55.21939137 763.95788 5.47736 GNAT3 0.000297548170729583 0.799720860049773 0.199981591779497 G protein subunit alpha transducin 3 FUNCTION: Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction. Transduction by this alpha subunit involves coupling of specific cell-surface receptors with a cGMP-phosphodiesterase; Activation of phosphodiesterase lowers intracellular levels of cAMP and cGMP which may open a cyclic nucleotide-suppressible cation channel leading to influx of calcium, ultimately leading to release of neurotransmitter. Indeed, denatonium and strychnine induce transient reduction in cAMP and cGMP in taste tissue, whereas this decrease is inhibited by GNAT3 antibody. Gustducin heterotrimer transduces response to bitter and sweet compounds via regulation of phosphodiesterase for alpha subunit, as well as via activation of phospholipase C for beta and gamma subunits, with ultimate increase inositol trisphosphate and increase of intracellular Calcium. GNAT3 can functionally couple to taste receptors to transmit intracellular signal: receptor heterodimer TAS1R2/TAS1R3 senses sweetness and TAS1R1/TAS1R3 transduces umami taste, whereas the T2R family GPCRs act as bitter sensors. Functions also as lumenal sugar sensors in the gut to control the expression of the Na+-glucose transporter SGLT1 in response to dietaty sugar, as well as the secretion of Glucagon-like peptide- 1, GLP-1 and glucose-dependent insulinotropic polypeptide, GIP. Thus, may modulate the gut capacity to absorb sugars, with implications in malabsorption syndromes and diet-related disorders including diabetes and obesity. {ECO:0000269|PubMed:11917125, ECO:0000269|PubMed:17724330}.; . TISSUE SPECIFICITY: Expressed in taste buds (sensory organs of clustered epithelial cells) of the circumvallate and foliate papillae of the tongue at protein level. Expressed in enteroendocrine L cells of the gut. Detected also in spermatozoa. {ECO:0000269|PubMed:16728727, ECO:0000269|PubMed:17021831, ECO:0000269|PubMed:17724332, ECO:0000269|PubMed:8015379}.; . . 0.29635 . 0.483275131 79.25218212 95.44529 2.10878 GNAZ 0.886293663993377 0.112461574917917 0.00124476108870634 G protein subunit alpha z FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.; . . choroid;fovea centralis;skin;retina;uterus;optic nerve;whole body;frontal lobe;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;breast;lung;epididymis;hippocampus;visual apparatus;macula lutea;liver;spleen;kidney;mammary gland; amygdala;whole brain;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;cerebellum peduncles;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.31906 0.17050 -0.846787714 11.05803255 7.7129 0.28470 GNB1 0.995187833121982 0.00481167835276296 4.8852525544842e-07 G protein subunit beta 1 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction.; . . . . 0.86155 0.25991 -0.317668748 31.45789101 0.82137 0.01624 GNB1L 0.00126345233746083 0.853507343226865 0.145229204435674 G protein subunit beta 1 like . . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, liver, skeletal muscle, kidney, spleen, thymus and pancreas. Detected at low levels in lung, placenta and brain.; unclassifiable (Anatomical System);cartilage;ovary;colon;parathyroid;lens;skin;skeletal muscle;prostate;lung;frontal lobe;bone;placenta;thyroid;testis;head and neck;spleen;germinal center;kidney;brain; skeletal muscle; 0.10188 . 0.687150476 85.17928757 1650.07221 7.50745 GNB2 0.989239434673184 0.0107570683115816 3.49701523393963e-06 G protein subunit beta 2 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction.; . . lymphoreticular;smooth muscle;ovary;skin;bone marrow;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;heart;tongue;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus;cerebellum; . 0.37986 0.14229 -0.492218069 22.35786742 28.35841 0.90830 GNB3 6.50125510048293e-09 0.133763321200304 0.866236672298441 G protein subunit beta 3 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction.; . . unclassifiable (Anatomical System);cartilage;fovea centralis;choroid;lens;skeletal muscle;retina;pancreas;optic nerve;lung;placenta;thyroid;macula lutea;visual apparatus;pituitary gland;pineal gland;brain;stomach; cingulate cortex; 0.15058 0.28104 -0.402212257 26.7338995 185.15549 2.95426 GNB4 0.629775083415026 0.369918721613448 0.00030619497152557 G protein subunit beta 4 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction.; . TISSUE SPECIFICITY: Strongly expressed in lung and placenta, whereas it is weakly expressed in brain and heart. Abundantly expressed in the axons and Schwann cells of peripheral nerves. {ECO:0000269|PubMed:11842130, ECO:0000269|PubMed:23434117}.; unclassifiable (Anatomical System);cartilage;ovary;heart;muscle;colon;parathyroid;breast;uterus;whole body;lung;mesenchyma;larynx;bone;thyroid;placenta;hippocampus;alveolus;liver;testis;head and neck;germinal center;brain;artery;aorta; . 0.45415 0.12971 -0.029247611 51.40363293 17.25958 0.60544 GNB5 0.00144292854144753 0.991478854217979 0.00707821724057374 G protein subunit beta 5 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction.; . TISSUE SPECIFICITY: Expressed in multiple tissues.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;bone;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach;cerebellum; amygdala;whole brain;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;cerebellum peduncles;pons;subthalamic nucleus;globus pallidus;kidney;cingulate cortex;cerebellum; 0.10623 0.15963 -0.578583623 18.71903751 98.54299 2.14466 GNE 4.85673826932321e-07 0.956816155756041 0.0431833585701326 glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase FUNCTION: Regulates and initiates biosynthesis of N- acetylneuraminic acid (NeuAc), a precursor of sialic acids. Plays an essential role in early development (By similarity). Required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. {ECO:0000250, ECO:0000269|PubMed:10334995}.; DISEASE: Sialuria (SIALURIA) [MIM:269921]: In sialuria, free sialic acid accumulates in the cytoplasm and gram quantities of neuraminic acid are secreted in the urine. The metabolic defect involves lack of feedback inhibition of UDP-GlcNAc 2-epimerase by CMP-Neu5Ac, resulting in constitutive overproduction of free Neu5Ac. Clinical features include variable degrees of developmental delay, coarse facial features and hepatomegaly. Sialuria inheritance is autosomal dominant. {ECO:0000269|PubMed:10330343, ECO:0000269|PubMed:10356312, ECO:0000269|PubMed:2808337}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Inclusion body myopathy 2 (IBM2) [MIM:600737]: Hereditary inclusion body myopathies are a group of neuromuscular disorders characterized by adult onset, slowly progressive distal and proximal weakness and a typical muscle pathology including rimmed vacuoles and filamentous inclusions. IBM2 is an autosomal recessive disorder affecting mainly leg muscles, but with an unusual distribution that spares the quadriceps as also observed in Nonaka myopathy. {ECO:0000269|PubMed:11528398, ECO:0000269|PubMed:12409274, ECO:0000269|PubMed:12473769, ECO:0000269|PubMed:12473780, ECO:0000269|PubMed:12497639, ECO:0000269|PubMed:12811782, ECO:0000269|PubMed:15146476}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Nonaka myopathy (NM) [MIM:605820]: Autosomal recessive muscular disorder, allelic to inclusion body myopathy 2. It is characterized by weakness of the anterior compartment of the lower limbs with onset in early adulthood, and sparing of the quadriceps muscles. As the inclusion body myopathy, NM is histologically characterized by the presence of numerous rimmed vacuoles without inflammatory changes in muscle specimens. {ECO:0000269|PubMed:11916006, ECO:0000269|PubMed:12177386, ECO:0000269|PubMed:12325084, ECO:0000269|PubMed:12473753, ECO:0000269|PubMed:12913203}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest expression in liver and placenta. Also found in heart, brain, lung, kidney, skeletal muscle and pancreas. Isoform 1 is expressed in heart, brain, kidney, liver, placenta, lung, spleen, pancreas, skeletal muscle and colon. Isoform 2 is expressed mainly in placenta, but also in brain, kidney, liver, lung, pancreas and colon. Isoform 3 is expressed at low level in kidney, liver, placenta and colon. {ECO:0000269|PubMed:10330343, ECO:0000269|PubMed:10431835, ECO:0000269|PubMed:17597614}.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;skin;skeletal muscle;breast;uterus;prostate;lung;larynx;placenta;liver;testis;cervix;head and neck;spleen;germinal center;brain;stomach; superior cervical ganglion;trachea;placenta;liver;pons;trigeminal ganglion;cerebellum; 0.43615 0.25685 -0.025608647 51.91672564 46.34235 1.31216 GNG2 0.52377049107399 0.413182893832688 0.063046615093322 G protein subunit gamma 2 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in fetal tissues, including testis, adrenal gland, brain, white blood cells and brain. {ECO:0000269|PubMed:10833460}.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;retina;uterus;prostate;whole body;lung;cornea;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland; . 0.20474 0.14229 0.057118534 57.99716914 30.28316 0.96560 GNG3 0.5272272299072 0.411087504175409 0.0616852659173911 G protein subunit gamma 3 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction.; . . unclassifiable (Anatomical System);cerebellum cortex;hypothalamus;sympathetic chain;blood;fovea centralis;retina;lung;optic nerve;frontal lobe;hippocampus;macula lutea;testis;brain; whole brain;dorsal root ganglion;amygdala;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.48726 . 0.167351552 65.04482189 1.16568 0.03232 GNG4 0.158455672191453 0.637416191696643 0.204128136111904 G protein subunit gamma 4 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. {ECO:0000305}.; . TISSUE SPECIFICITY: Brain, kidney, pancreas, skeletal muscle and faintly in cardiac muscle.; . . 0.67478 0.11016 0.057118534 57.99716914 2.42849 0.08680 GNG5 0.524989345213255 0.412446529939574 0.0625641248471713 G protein subunit gamma 5 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction.; . . . . 0.45223 0.13588 0.145304857 63.81221986 14.03615 0.50925 GNG5P1 . . . G protein subunit gamma 5 pseudogene 1 . . . unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;optic nerve;whole body;lung;placenta;macula lutea;testis;kidney; . . . . . . . GNG5P2 0.38481704945863 0.47636822817413 0.13881472236724 G protein subunit gamma 5 pseudogene 2 . . . . . 0.30587 . . . 23.97445 0.78924 GNG5P3 . . . G protein subunit gamma 5 pseudogene 3 . . . . . . . . . . . GNG5P4 . . . G protein subunit gamma 5 pseudogene 4 . . . . . . . . . . . GNG5P5 . . . G protein subunit gamma 5 pseudogene 5 . . . . . . . . . . . GNG7 0.475557140257132 0.440021407779758 0.0844214519631104 G protein subunit gamma 7 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Plays a role in the regulation of adenylyl cyclase signaling in certain regions of the brain. Plays a role in the formation or stabilzation of a G protein heterotrimer (G(olf) subunit alpha-beta-gamma-7) that is required for adenylyl cyclase activity in the striatum (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in a variety of tissues. Down- regulated in pancreatic and esophageal cancer. {ECO:0000269|PubMed:18219292}.; . . 0.46138 0.11262 0.079165051 59.43029016 3.26659 0.11840 GNG8 0.147000773638907 0.63109907143993 0.221900154921163 G protein subunit gamma 8 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction.; . . unclassifiable (Anatomical System); superior cervical ganglion;fetal brain;globus pallidus; 0.36029 0.12378 0.145304857 63.81221986 14.28776 0.51650 GNG10 0.000310150416814466 0.202104559832518 0.797585289750667 G protein subunit gamma 10 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Interacts with beta-1 and beta-2, but not with beta-3.; . TISSUE SPECIFICITY: Abundantly and ubiquitously expressed.; . . 0.22370 0.10299 . . 85.39974 1.96993 GNG10P1 . . . G protein subunit gamma 10 pseudogene 1 . . . . . . . . . . . GNG11 0.163792461884714 0.639790285787115 0.196417252328172 G protein subunit gamma 11 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction.; . TISSUE SPECIFICITY: Abundantly expressed in all tissues tested except for brain.; myocardium;ovary;salivary gland;intestine;colon;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;testis;dura mater;spinal ganglion;brain;unclassifiable (Anatomical System);meninges;lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;pancreas;pia mater;lung;cornea;epididymis;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;aorta;stomach;thymus; smooth muscle;heart;placenta; 0.36044 . 0.057118534 57.99716914 5.56773 0.20715 GNG12 0.553351817862124 0.394571311427446 0.0520768707104297 G protein subunit gamma 12 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction.; . . . . 0.27104 0.14896 -0.009020804 52.8544468 9.47113 0.34919 GNG12-AS1 . . . GNG12 antisense RNA 1 . . . . . . . . . . . GNG13 0.00489277449013945 0.454495353247449 0.540611872262412 G protein subunit gamma 13 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction.; . . unclassifiable (Anatomical System);islets of Langerhans;urinary;colon;blood;fovea centralis;choroid;lens;retina;optic nerve;endometrium;placenta;thyroid;bone;macula lutea;testis;mammary gland;brain;stomach; subthalamic nucleus;thalamus;superior cervical ganglion;cerebellum peduncles;temporal lobe;prefrontal cortex;ciliary ganglion;atrioventricular node;parietal lobe;skeletal muscle;cingulate cortex;cerebellum; 0.16114 0.13588 -0.075159878 47.78839349 16.22258 0.57592 GNGT1 0.276892736896177 0.633040351863086 0.0900669112407366 G protein subunit gamma transducin 1 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction.; . TISSUE SPECIFICITY: Retinal rod outer segment.; unclassifiable (Anatomical System);pineal body;adrenal cortex;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;adrenal gland;placenta;thyroid;macula lutea;pineal gland; superior cervical ganglion;subthalamic nucleus;temporal lobe;appendix;trigeminal ganglion;skeletal muscle; 0.74854 0.17821 0.191216164 66.57230479 3.21371 0.11566 GNGT2 0.173047625856269 0.643126693021893 0.183825681121838 G protein subunit gamma transducin 2 FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction.; . TISSUE SPECIFICITY: Retinal cones.; unclassifiable (Anatomical System);uterus;lung;visual apparatus;colon;blood;kidney;germinal center;skin;retina; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.18249 0.12971 0.501689326 79.7888653 165.03072 2.81024 GNL1 0.999930615118599 6.93848654976359e-05 1.59031734886289e-11 G protein nucleolar 1 (putative) FUNCTION: Possible regulatory or functional link with the histocompatibility cluster.; . . . . 0.55180 . -0.446304853 24.33356924 102.84229 2.19222 GNL2 0.453032469584323 0.546965394905718 2.13550995891285e-06 G protein nucleolar 2 FUNCTION: GTPase that associates with pre-60S ribosomal subunits in the nucleolus and is required for their nuclear export and maturation. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed at relatively low levels in all human tissues tested, with the highest level of expression in the testes.; . . 0.89972 0.10766 -0.995664936 8.539749941 121.77165 2.40365 GNL2P1 . . . G protein nucleolar 2 pseudogene 1 . . . . . . . . . . . GNL3 1.53959646341731e-09 0.58390746247596 0.416092535984443 G protein nucleolar 3 FUNCTION: May be required to maintain the proliferative capacity of stem cells. Stabilizes MDM2 by preventing its ubiquitination, and hence proteasomal degradation (By similarity). {ECO:0000250, ECO:0000269|PubMed:12464630, ECO:0000269|PubMed:16012751}.; . TISSUE SPECIFICITY: Increased levels in lung tissue in cancer patients. {ECO:0000269|PubMed:16012751}.; . . 0.94475 0.17418 0.799205007 87.58551545 6200.21239 16.45902 GNL3L 0.991954332117903 0.00804395184243412 1.7160396632294e-06 G protein nucleolar 3 like FUNCTION: Stabilizes TERF1 telomeric association by preventing TERF1 recruitment by PML. Stabilizes TERF1 protein by preventing its ubiquitination and hence proteasomal degradation. Does so by interfering with TERF1-binding to FBXO4 E3 ubiquitin-protein ligase. Required for cell proliferation. By stabilizing TRF1 protein during mitosis, promotes metaphase-to-anaphase transition. Stabilizes MDM2 protein by preventing its ubiquitination, and hence proteasomal degradation. By acting on MDM2, may affect TP53 activity. Required for normal processing of ribosomal pre-rRNA. Binds GTP. {ECO:0000269|PubMed:16251348, ECO:0000269|PubMed:17034816, ECO:0000269|PubMed:19487455, ECO:0000269|PubMed:21132010}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;thyroid;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;mesenchyma;nasopharynx;placenta;visual apparatus;duodenum;liver;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;medulla oblongata;globus pallidus;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;cingulate cortex;skeletal muscle; 0.12299 0.10778 -0.312207497 32.05944798 58.89631 1.55747 GNL3LP1 . . . G protein nucleolar 3 like pseudogene 1 . . . . . . . . . . . GNLY 0.00154995699769898 0.685106929196547 0.313343113805754 granulysin FUNCTION: Antimicrobial protein that kills intracellular pathogens. Active against a broad range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis.; . TISSUE SPECIFICITY: Expressed in natural killer and T-cells.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;germinal center;tonsil;unclassifiable (Anatomical System);heart;tongue;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;aorta;stomach;thymus; placenta;whole blood;bone marrow; 0.35845 . 1.104245073 91.95564992 . . GNMT 0.667933555724909 0.326977802478053 0.00508864179703854 glycine N-methyltransferase FUNCTION: Catalyzes the methylation of glycine by using S- adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue concentration of AdoMet and of metabolism of methionine. {ECO:0000269|PubMed:15340920, ECO:0000269|PubMed:17660255}.; . TISSUE SPECIFICITY: Abundant in liver.; . . 0.75363 0.31829 0.060756528 58.52795471 49.85197 1.38486 GNPAT 0.291272732702187 0.708689867733941 3.73995638716371e-05 glyceronephosphate O-acyltransferase . DISEASE: Rhizomelic chondrodysplasia punctata 2 (RCDP2) [MIM:222765]: A disease characterized by rhizomelic shortening of femur and humerus, vertebral disorders, cataract, cutaneous lesions and severe mental retardation. {ECO:0000269|PubMed:11152660, ECO:0000269|PubMed:21990100, ECO:0000269|PubMed:9536089}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.52109 0.26501 -0.200157416 39.11299835 1060.52275 6.24900 GNPATP . . . glyceronephosphate O-acyltransferase pseudogene . . . . . . . . . . . GNPDA1 0.00342635564065799 0.834419200960058 0.162154443399284 glucosamine-6-phosphate deaminase 1 FUNCTION: Seems to trigger calcium oscillations in mammalian eggs. These oscillations serve as the essential trigger for egg activation and early development of the embryo (By similarity). {ECO:0000250}.; . . myocardium;medulla oblongata;ovary;skin;bone marrow;prostate;endometrium;cochlea;thyroid;iris;bladder;brain;heart;cartilage;urinary;adrenal cortex;blood;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;vein;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; . 0.25539 0.16395 -0.471992905 23.03609342 12.07805 0.43768 GNPDA2 0.0126461807896128 0.856415728970233 0.130938090240154 glucosamine-6-phosphate deaminase 2 . . . myocardium;ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;cerebral cortex;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;skeletal muscle;bile duct;pancreas;lung;trabecular meshwork;placenta;liver;spleen;cervix;kidney;stomach;aorta; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.35632 0.13986 -0.207437529 38.2814343 16.82634 0.59193 GNPNAT1 0.00556740862247386 0.7178081215283 0.276624469849226 glucosamine-phosphate N-acetyltransferase 1 . . . ovary;salivary gland;intestine;colon;fovea centralis;skin;uterus;prostate;whole body;endometrium;bone;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;cornea;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; globus pallidus;skeletal muscle; 0.17873 0.12378 -0.053113545 49.38664779 9.96006 0.36486 GNPTAB 4.22557947344879e-06 0.999977940591976 1.78338285510433e-05 N-acetylglucosamine-1-phosphate transferase alpha and beta subunits FUNCTION: Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment. {ECO:0000269|PubMed:19955174, ECO:0000269|PubMed:23733939}.; DISEASE: Mucolipidosis type II (MLII) [MIM:252500]: Fatal, autosomal recessive, lysosomal storage disorder characterized by severe clinical and radiologic features, peculiar fibroblast inclusions, and no excessive mucopolysacchariduria. Congenital dislocation of the hip, thoracic deformities, hernia, and hyperplastic gums are evident soon after birth. {ECO:0000269|PubMed:16200072, ECO:0000269|PubMed:16835905, ECO:0000269|PubMed:19197337, ECO:0000269|PubMed:19617216, ECO:0000269|PubMed:19634183, ECO:0000269|PubMed:19938078, ECO:0000269|PubMed:22495880, ECO:0000269|PubMed:23566849, ECO:0000269|PubMed:23733939, ECO:0000269|PubMed:23773965, ECO:0000269|PubMed:24375680, ECO:0000269|PubMed:24798265, ECO:0000269|PubMed:25505245, ECO:0000269|PubMed:25788519}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mucolipidosis type III complementation group A (MLIIIA) [MIM:252600]: Autosomal recessive disease of lysosomal enzyme targeting. Clinically MLIII is characterized by restricted joint mobility, skeletal dysplasia, and short stature. Mildly coarsened facial features and thickening of the skin have been described. Cardiac valvular disease and corneal clouding may also occur. Half of the reported patients show learning disabilities or mental retardation. {ECO:0000269|PubMed:16094673, ECO:0000269|PubMed:16465621, ECO:0000269|PubMed:16630736, ECO:0000269|PubMed:17034777, ECO:0000269|PubMed:19197337, ECO:0000269|PubMed:19617216, ECO:0000269|PubMed:19634183, ECO:0000269|PubMed:19938078, ECO:0000269|PubMed:23566849, ECO:0000269|PubMed:24045841, ECO:0000269|PubMed:24375680, ECO:0000269|PubMed:24550498, ECO:0000269|PubMed:25505245, ECO:0000269|PubMed:25788519}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in GNPTAB have been suggested to play a role in susceptibility to persistent stuttering. Stuttering is a common speech disorder characterized by repetitions, prolongations, and interruptions in the flow of speech. {ECO:0000269|PubMed:20147709}.; TISSUE SPECIFICITY: Expressed in the heart, whole brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:16120602}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;spinal cord;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;superior cervical ganglion;occipital lobe;fetal brain;prefrontal cortex;ciliary ganglion;pons;caudate nucleus;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.70519 0.14868 -1.366884746 4.505779665 437.11196 4.35866 GNPTG 5.99621775569544e-08 0.243287932286244 0.756712007751579 N-acetylglucosamine-1-phosphate transferase gamma subunit FUNCTION: Non-catalytic subunit of the N-acetylglucosamine-1- phosphotransferase complex, an enzyme that catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. Binds and presents the high mannose glycans of the acceptor to the catalytic alpha and beta subunits (GNPTAB). Enhances the rate of N-acetylglucosamine- 1-phosphate transfer to the oligosaccharides of acid hydrolase acceptors. {ECO:0000269|PubMed:10712439, ECO:0000269|PubMed:19955174}.; DISEASE: Mucolipidosis type III complementation group C (MLIIIC) [MIM:252605]: Autosomal recessive disease of lysosomal hydrolase trafficking. Unlike the related diseases, mucolipidosis II and IIIA, the enzyme affected in mucolipidosis IIIC (GlcNAc- phosphotransferase) retains full transferase activity on synthetic substrates but lacks activity on lysosomal hydrolases. Typical clinical findings include stiffness of the hands and shoulders, claw-hand deformity, scoliosis, short stature, coarse facies, and mild mental retardation. Radiographically, severe dysostosis multiplex of the hip is characteristic and frequently disabling. The clinical diagnosis can be confirmed by finding elevated serum lysosomal enzyme levels and/or decreased lysosomal enzyme levels in cultured fibroblasts. {ECO:0000269|PubMed:10712439, ECO:0000269|PubMed:15532026, ECO:0000269|PubMed:24316125}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in GNPTG have been suggested to play a role in susceptibility to persistent stuttering. Stuttering is a common speech disorder characterized by repetitions, prolongations, and interruptions in the flow of speech. {ECO:0000269|PubMed:20147709}.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10712439}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;bone;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;amnion;head and neck;kidney;stomach; amygdala;adrenal gland;globus pallidus;pons; 0.11006 0.14352 -0.334253673 30.70299599 52.40877 1.43216 GNRH1 0.0986916060732056 0.771521432360107 0.129786961566688 gonadotropin releasing hormone 1 FUNCTION: Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones.; DISEASE: Hypogonadotropic hypogonadism 12 with or without anosmia (HH12) [MIM:614841]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:19535795, ECO:0000269|PubMed:23643382}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. The genetics of hypogonadotropic hypogonadism involves various modes of transmission. Oligogenic inheritance has been reported in some patients carrying mutations in GNRH1 as well as in other HH- associated genes including PROKR2 and FGFR1 (PubMed:23643382). {ECO:0000269|PubMed:23643382}.; . unclassifiable (Anatomical System);heart;blood;skeletal muscle;skin;retina;bone marrow;uterus;prostate;lung;germinal center;mammary gland;brain;stomach; subthalamic nucleus;skeletal muscle; 0.03094 0.64241 0.679884223 84.81363529 441.6412 4.37565 GNRH2 0.000228749333342023 0.512369653267543 0.487401597399115 gonadotropin releasing hormone 2 FUNCTION: Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones.; . TISSUE SPECIFICITY: Midbrain; expressed at significantly higher levels outside the brain (up to 30-fold), particularly in the kidney, bone marrow and prostate.; unclassifiable (Anatomical System);testis; pons;skeletal muscle; 0.02963 0.23480 0.237127192 68.98443029 1967.33811 8.17254 GNRHR 0.0139680451262733 0.86855315024995 0.117478804623776 gonadotropin releasing hormone receptor FUNCTION: Receptor for gonadotropin releasing hormone (GnRH) that mediates the action of GnRH to stimulate the secretion of the gonadotropic hormones luteinizing hormone (LH) and follicle- stimulating hormone (FSH). This receptor mediates its action by association with G-proteins that activate a phosphatidylinositol- calcium second messenger system. Isoform 2 may act as an inhibitor of GnRH-R signaling.; . TISSUE SPECIFICITY: Pituitary, ovary, testis, breast and prostate but not in liver and spleen.; unclassifiable (Anatomical System); dorsal root ganglion;uterus corpus;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;pituitary;skeletal muscle; 0.44100 0.23622 -0.115612493 45.12856806 24.68684 0.81033 GNRHR2 . . . gonadotropin releasing hormone receptor 2 (pseudogene) FUNCTION: Putative receptor for gonadotropin releasing hormone II (GnRH II) which is most probably non-functional. {ECO:0000269|PubMed:12538601, ECO:0000269|PubMed:19657181}.; . TISSUE SPECIFICITY: Expressed in many tissues. {ECO:0000269|PubMed:11861490}.; ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;urinary;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach;aorta; . 0.03438 . . . . . GNRHR2P1 . . . GNRHR2 pseudogene 1 . . . . . . . . . . . GNS 0.0829052963160252 0.916669454626573 0.000425249057402338 glucosamine (N-acetyl)-6-sulfatase . DISEASE: Mucopolysaccharidosis 3D (MPS3D) [MIM:252940]: A form of mucopolysaccharidosis type 3, an autosomal recessive lysosomal storage disease due to impaired degradation of heparan sulfate. MPS3 is characterized by severe central nervous system degeneration, but only mild somatic disease. Onset of clinical features usually occurs between 2 and 6 years; severe neurologic degeneration occurs in most patients between 6 and 10 years of age, and death occurs typically during the second or third decade of life. {ECO:0000269|PubMed:12573255, ECO:0000269|PubMed:20232353}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;amnion;head and neck;kidney;stomach;aorta; adrenal gland;placenta;kidney;trigeminal ganglion; 0.41887 0.32506 -0.314027422 31.9297004 384.936 4.13377 GOLGA1 0.00610739448233049 0.993885174371972 7.43114569755067e-06 golgin A1 FUNCTION: Probably involved in maintaining Golgi structure. {ECO:0000269|PubMed:9324025}.; . . . . 0.64237 0.11337 0.025760883 55.78556263 1183.82096 6.52835 GOLGA2 0.994925568732598 0.00507443122922103 3.81807488920858e-11 golgin A2 FUNCTION: Peripheral membrane component of the cis-Golgi stack that acts as a membrane skeleton that maintains the structure of the Golgi apparatus, and as a vesicle thether that facilitates vesicle fusion to the Golgi membrane. Together with p115/USO1 and STX5, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus. Plays a central role in mitotic Golgi disassembly: phosphorylation at Ser-37 by CDK1 at the onset of mitosis inhibits the interaction with p115/USO1, preventing tethering of COPI vesicles and thereby inhibiting transport through the Golgi apparatus during mitosis (By similarity). Also plays a key role in spindle pole assembly and centrosome organization (PubMed:26165940). Promotes the mitotic spindle pole assembly by activating the spindle assembly factor TPX2 to nucleate microtubules around the Golgi and capture them to couple mitotic membranes to the spindle: upon phosphorylation at the onset of mitosis, GOLGA2 interacts with importin-alpha via the nuclear localization signal region, leading to recruit importin- alpha to the Golgi membranes and liberate the spindle assembly factor TPX2 from importin-alpha. TPX2 then activates AURKA kinase and stimulates local microtubule nucleation. Upon filament assembly, nascent microtubules are further captured by GOLGA2, thus linking Golgi membranes to the spindle (PubMed:19242490, PubMed:26165940). Regulates the meiotic spindle pole assembly, probably via the same mechanism (By similarity). Also regulates the centrosome organization (PubMed:18045989, PubMed:19109421). Also required for the Golgi ribbon formation and glycosylation of membrane and secretory proteins (PubMed:16489344, PubMed:17314401). {ECO:0000250|UniProtKB:Q62839, ECO:0000250|UniProtKB:Q921M4, ECO:0000269|PubMed:16489344, ECO:0000269|PubMed:17314401, ECO:0000269|PubMed:18045989, ECO:0000269|PubMed:19109421, ECO:0000269|PubMed:19242490, ECO:0000269|PubMed:26165940}.; . . . . 0.13521 0.10126 0.361913759 74.69922151 3976.0248 12.47569 GOLGA2P1 . . . golgin A2 pseudogene 1 . . . . . . . . . . . GOLGA2P2Y . . . golgin A2 pseudogene 2, Y-linked . . . . . . . . . . . GOLGA2P3Y . . . golgin A2 pseudogene 3, Y-linked . . . . . . . . . . . GOLGA2P4 . . . golgin A2 pseudogene 4 . . . . . . . . . . . GOLGA2P5 . . . golgin A2 pseudogene 5 . . . . . 0.09852 . . . . . GOLGA2P6 . . . golgin A2 pseudogene 6 . . . . . . . . . . . GOLGA2P7 . . . golgin A2 pseudogene 7 . . . . . . . . . . . GOLGA2P8 . . . golgin A2 pseudogene 8 . . . . . . . . . . . GOLGA2P9 . . . golgin A2 pseudogene 9 . . . . . . . . . . . GOLGA2P10 . . . golgin A2 pseudogene 10 . . . . . . . . . . . GOLGA2P11 . . . golgin A2 pseudogene 11 . . . . . . . . . . . GOLGA3 0.991564255599712 0.0084357443948699 5.41767026702645e-12 golgin A3 FUNCTION: Golgi auto-antigen; probably involved in maintaining Golgi structure.; . TISSUE SPECIFICITY: Expressed in all tissues tested. Expressed in liver, testis, lung, heart, salivary gland and kidney. {ECO:0000269|PubMed:15951434}.; ovary;salivary gland;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; . 0.42503 0.13258 -0.571624906 18.96673744 4390.25176 13.22841 GOLGA4 2.26164990605558e-09 0.999999977059311 2.06790392004724e-08 golgin A4 FUNCTION: May play a role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with MACF1. {ECO:0000269|PubMed:15265687}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;atrium;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;tongue;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; testis - interstitial;superior cervical ganglion;thyroid;testis;trigeminal ganglion; 0.31004 0.19068 0.069649268 59.04694503 2466.17662 9.25088 GOLGA4P1 . . . golgin A4 pseudogene 1 . . . . . . . . . . . GOLGA4P2 . . . golgin A4 pseudogene 2 . . . . . . . . . . . GOLGA4P3 . . . golgin A4 pseudogene 3 . . . . . . . . . . . GOLGA5 0.363133884753824 0.636865255241833 8.60004342741971e-07 golgin A5 FUNCTION: Involved in maintaining Golgi structure. Stimulates the formation of Golgi stacks and ribbons. Involved in intra-Golgi retrograde transport. {ECO:0000269|PubMed:12538640, ECO:0000269|PubMed:15718469}.; DISEASE: Note=A chromosomal aberration involving GOLGA5 is found in papillary thyroid carcinomas (PTCs). Translocation t(10;14)(q11;q32) with RET. The translocation generates the RET/GOLGA5 (PTC5) oncogene. {ECO:0000269|PubMed:2734021, ECO:0000269|PubMed:9443391}.; TISSUE SPECIFICITY: Ubiquitous. Highly expressed in seminiferous tubules and Leydig cells in testis, and detected at much lower levels in the other tissues tested. Expression is very low or not detectable in spermatozoa. {ECO:0000269|PubMed:9915833}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19423 0.14002 0.270087468 70.69473933 1496.7136 7.19849 GOLGA5P1 . . . golgin A5 pseudogene 1 . . . . . . . . . . . GOLGA6A 0.224411353907766 0.739591663948979 0.035996982143255 golgin A6 family member A . . TISSUE SPECIFICITY: Highly expressed in seminiferous tubes in testis. Highly expressed in spermatids, barely detectable in late pachytene spermatocytes, and not detectable in spermatogonia. Detected at intermediate levels in pancreas and lymph nodes, and at much lower levels in spleen, peripheral blood leukocytes, skeletal muscle, liver, lung, placenta, brain and heart.; unclassifiable (Anatomical System);testis; . . 0.07726 . . 525.23752 4.67589 GOLGA6B 0.302338863626375 0.693600691654435 0.00406044471918907 golgin A6 family member B . . . . . 0.06962 . . . 919.78048 5.89498 GOLGA6C 0.0400514301413968 0.841500384896894 0.118448184961709 golgin A6 family member C . . . testis; . . . . . 64.94994 1.65583 GOLGA6D 0.318585416071094 0.61325685422551 0.0681577297033963 golgin A6 family member D . . . . . 0.06962 . . . 269.62979 3.52255 GOLGA6L1 . . . golgin A6 family-like 1 . . . . . . . . . 3.72822 0.13876 GOLGA6L2 8.97094503942648e-06 0.322765802087888 0.677225226967072 golgin A6 family-like 2 . . . lung;testis; . . . . . 13588.28081 25.35450 GOLGA6L3 . . . golgin A6 family-like 3 . . . . . . . . . . . GOLGA6L4 0.389324704197603 0.475068149278961 0.135607146523436 golgin A6 family-like 4 . . . . . . . . . 12.32264 0.44678 GOLGA6L5P . . . golgin A6 family-like 5, pseudogene . . . . . . . . . . . GOLGA6L6 0.0868643024684935 0.560054824892067 0.35308087263944 golgin A6 family-like 6 . . . . . . . . . 1388.57903 6.97595 GOLGA6L7P . . . golgin A6 family-like 7, pseudogene . . . . . . . . . . . GOLGA6L9 . . . golgin A6 family-like 9 . . . unclassifiable (Anatomical System);optic nerve;oesophagus;larynx;thyroid;macula lutea;head and neck;fovea centralis;choroid;kidney;lens;retina; . . . . . . . GOLGA6L10 0.368958940189802 0.480468939609581 0.150572120200616 golgin A6 family-like 10 . . . . . . . . . 738.28141 5.39276 GOLGA6L11P . . . golgin A6 family-like 11, pseudogene . . . . . . . . . . . GOLGA6L12P . . . golgin A6 family-like 12, pseudogene . . . . . . . . . . . GOLGA6L13P . . . golgin A6 family-like 13, pseudogene . . . . . . . . . . . GOLGA6L14P . . . golgin A6 family-like 14, pseudogene . . . . . . . . . . . GOLGA6L16P . . . golgin A6 family-like 16, pseudogene . . . . . . . . . . . GOLGA6L17P . . . golgin A6 family-like 17, pseudogene . . . . . . . . . . . GOLGA6L19 . . . golgin A6 family-like 19 . . . . . . . . . 86.90239 1.99060 GOLGA6L22 . . . golgin A6 family-like 22 . . . . . . . . . . . GOLGA7 0.691723360705822 0.304217318477596 0.00405932081658231 golgin A7 FUNCTION: May be involved in protein transport from Golgi to cell surface. The ZDHHC9-GOLGA7 complex is a palmitoyltransferase specific for HRAS and NRAS. {ECO:0000269|PubMed:14522980, ECO:0000269|PubMed:16000296}.; . TISSUE SPECIFICITY: Expressed in all tissues except colon and thymus. {ECO:0000269|PubMed:14522980, ECO:0000269|PubMed:16000296}.; ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;amygdala;heart;adrenal cortex;pharynx;blood;breast;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach; amygdala;whole brain;thalamus;medulla oblongata;occipital lobe;hypothalamus;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.37257 0.11262 -0.009020804 52.8544468 5.92607 0.22325 GOLGA7B 0.0104883753574862 0.830551489623629 0.158960135018885 golgin A7 family member B FUNCTION: May be involved in protein transport from Golgi to cell surface. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, but not in lung, nor chondrocytes. {ECO:0000269|PubMed:17074475}.; . . 0.15384 . 0.125076652 62.7388535 1279.0742 6.73486 GOLGA8A 0.693302517089581 0.289044507601442 0.0176529753089771 golgin A8 family member A FUNCTION: May be involved in maintaining Golgi structure. {ECO:0000250}.; . . ovary;sympathetic chain;colon;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;blood;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;cerebellum; globus pallidus;ciliary ganglion; 0.42751 . . . 2044.76566 8.33897 GOLGA8B 0.280132444754512 0.631736256047476 0.0881312991980117 golgin A8 family member B FUNCTION: May be involved in maintaining Golgi structure. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in brain, heart and kidney. Detected at lower levels in liver, thymus, spleen, lung and peripheral blood leukocytes. {ECO:0000269|PubMed:10660574}.; ovary;sympathetic chain;colon;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;cerebellum; . 0.16071 . . . 2341.597 8.96698 GOLGA8CP . . . golgin A8 family member C, pseudogene . . . . . . . . . . . GOLGA8DP . . . golgin A8 family member D, pseudogene . . . medulla oblongata;lung;islets of Langerhans;testis;colon;retina; . . . . . . . GOLGA8EP . . . golgin A8 family member E, pseudogene . . . . . 0.09256 . . . . . GOLGA8F 0.559396882573985 0.390584963080198 0.0500181543458167 golgin A8 family member F . . . ovary;sympathetic chain;colon;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;blood;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;cerebellum; . . . . . 381.64468 4.11770 GOLGA8G 0.447085283334208 0.453586842344391 0.0993278743214014 golgin A8 family member G . . . medulla oblongata;testis; . . . . . 66.72374 1.68552 GOLGA8H 3.19984019621833e-05 0.567934430778572 0.432033570819466 golgin A8 family member H . . . . . . . . . 1721.62757 7.65373 GOLGA8IP . . . golgin A8 family member I, pseudogene FUNCTION: May be involved in maintaining Golgi structure. {ECO:0000250}.; . . fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;frontal lobe;oesophagus;endometrium;larynx;thyroid;macula lutea;liver;head and neck;kidney;brain; . . . . . . . GOLGA8J 0.355056850110703 0.591517823091405 0.0534253267978919 golgin A8 family member J . . . unclassifiable (Anatomical System);skeletal muscle; . . . . . 717.36954 5.31657 GOLGA8K 0.337642789863851 0.602338901000817 0.0600183091353319 golgin A8 family member K . . . . . . . . . 1766.81182 7.76910 GOLGA8M 0.920983506421717 0.0785253936064475 0.000491099971835606 golgin A8 family member M . . . . . . . . . 10942.81507 22.78487 GOLGA8N . . . golgin A8 family member N . . . . . . . . . 0.87685 0.01758 GOLGA8O . . . golgin A8 family member O . . . . . . . . . 598.00901 4.94958 GOLGA8Q 0.480898386722338 0.437278858345088 0.081822754932574 golgin A8 family member Q . . . . . . . . . 55.46059 1.49593 GOLGA8R 0.175047823831853 0.643724944715452 0.181227231452694 golgin A8 family member R . . . . . . . . . 3.15781 0.11293 GOLGA8S 0.00466261611098299 0.877542934697521 0.117794449191496 golgin A8 family member S . . . . . . . . . 7996.64766 19.29597 GOLGA8T 0.76143467128854 0.229745312752647 0.00882001595881354 golgin A8 family member T . . . . . . . . . 256.37604 3.44528 GOLGA8UP . . . golgin A8 family member U, pseudogene . . . . . . . . . . . GOLGA8VP . . . golgin A8 family member V, pseudogene . . . . . . . . . . . GOLGB1 4.23236652462592e-06 0.999995767631428 2.04727319374544e-12 golgin B1 FUNCTION: May participate in forming intercisternal cross-bridges of the Golgi complex.; . . lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);oral cavity;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; medulla oblongata;testis - interstitial;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex; 0.12855 0.11656 -0.209740065 37.76834159 4766.46932 13.98118 GOLIM4 5.53788033369551e-11 0.94587964519921 0.0541203547454116 golgi integral membrane protein 4 FUNCTION: Plays a role in endosome to Golgi protein trafficking; mediates protein transport along the late endosome-bypass pathway from the early endosome to the Golgi. {ECO:0000269|PubMed:15331763}.; . . ovary;colon;parathyroid;fovea centralis;choroid;retina;prostate;optic nerve;whole body;frontal lobe;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;tongue;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;liver;hypopharynx;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;uterus corpus;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.10082 0.09393 -0.33061537 30.82094834 857.93003 5.71496 GOLM1 0.00261253568459098 0.982787989822921 0.0145994744924875 golgi membrane protein 1 FUNCTION: Unknown. Cellular response protein to viral infection.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in colon, prostate, trachea and stomach. Expressed at lower level in testis, muscle, lymphoid tissues, white blood cells and spleen. Predominantly expressed by cells of the epithelial lineage. Expressed at low level in normal liver. Expression significantly increases in virus (HBV, HCV) infected liver. Expression does not increase in liver disease due to non-viral causes (alcohol-induced liver disease, autoimmune hepatitis). Increased expression in hepatocytes appears to be a general feature of advanced liver disease. In liver tissue from patients with adult giant-cell hepatitis (GCH), it is strongly expressed in hepatocytes-derived syncytial giant cells. Constitutively expressed by biliary epithelial cells but not by hepatocytes. {ECO:0000269|PubMed:10831838, ECO:0000269|PubMed:12029628}.; lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;brain;gall bladder;heart;cartilage;tongue;urinary;spinal cord;adrenal cortex;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;parathyroid;fovea centralis;vein;uterus;whole body;oesophagus;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;pia mater;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus; . 0.39576 0.10761 0.643056625 84.05284265 489.5122 4.55380 GOLPH3 0.0143654910992665 0.871772673911863 0.113861834988871 golgi phosphoprotein 3 FUNCTION: Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Has also been involved in the control of the localization of Golgi enzymes through interaction with their cytoplasmic part. May play an indirect role in cell migration. Has also been involved in the modulation of mTOR signaling. May also be involved in the regulation of mitochondrial lipids biosynthesis. {ECO:0000269|PubMed:16263763, ECO:0000269|PubMed:19553991, ECO:0000269|PubMed:19837035, ECO:0000269|PubMed:22745132, ECO:0000269|PubMed:23027862, ECO:0000269|PubMed:23345592, ECO:0000269|PubMed:23500462}.; . TISSUE SPECIFICITY: Detected in muscle fibers of patients with mitochondrial diseases; not detected in normal muscle fibers.; medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;cerebellum; superior cervical ganglion;prostate;placenta; 0.79262 0.10184 -0.361761279 28.6329323 11.79185 0.42738 GOLPH3L 0.0221067463015886 0.962117500050466 0.0157757536479457 golgi phosphoprotein 3 like FUNCTION: Phosphatidylinositol-4-phosphate-binding protein that may antagonize the action of GOLPH3 which is required for the process of vesicle budding at the Golgi and anterograde transport to the plasma membrane. {ECO:0000269|PubMed:23345592}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;blood;lens;skeletal muscle;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; adrenal gland;beta cell islets; 0.21720 0.11050 0.038710339 56.92380278 54.0768 1.46626 GOLT1A 0.0387578834234533 0.838243925973991 0.122998190602555 golgi transport 1A FUNCTION: May be involved in fusion of ER-derived transport vesicles with the Golgi complex. {ECO:0000269|PubMed:10406798}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;salivary gland;intestine;pharynx;colon;parathyroid;blood;prostate;pancreas;lung;visual apparatus;liver;testis;spleen;kidney;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.11431 0.59876 -0.339715008 30.06605331 18.54855 0.64184 GOLT1B 0.798383719617006 0.196019028591186 0.00559725179180853 golgi transport 1B FUNCTION: May be involved in fusion of ER-derived transport vesicles with the Golgi complex.; . TISSUE SPECIFICITY: Widely expressed. Tends to be up-regulated in seminomas compared to normal testis. {ECO:0000269|PubMed:12414650}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion; 0.20274 0.11262 0.501689326 79.7888653 47.70445 1.34200 GON4L 0.999998891638014 1.10836198559455e-06 2.26844741215484e-19 gon-4 like FUNCTION: Has transcriptional repressor activity, probably as part of a complex with YY1, SIN3A AND HDAC1. Required for B cell lymphopoiesis. {ECO:0000250|UniProtKB:Q9DB00}.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;iris;amniotic fluid;germinal center;bladder;brain;ciliary body;tonsil;heart;cartilage;tongue;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;colon;fovea centralis;choroid;uterus;oesophagus;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;thymus;cerebellum; superior cervical ganglion;testis - seminiferous tubule;globus pallidus;pons;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.14902 0.08718 -1.357871407 4.535267752 369.16949 4.06020 GOPC 0.0219840797762706 0.974694754944139 0.00332116527959024 golgi-associated PDZ and coiled-coil motif containing FUNCTION: Plays a role in intracellular protein trafficking and degradation. May regulate CFTR chloride currents and acid-induced ASIC3 currents by modulating cell surface expression of both channels. May also regulate the intracellular trafficking of the ADR1B receptor. May play a role in autophagy. Overexpression results in CFTR intracellular retention and degradation in the lysosomes. {ECO:0000269|PubMed:11707463, ECO:0000269|PubMed:14570915, ECO:0000269|PubMed:15358775}.; DISEASE: Note=A chromosomal aberration involving GOPC is found in a glioblastoma multiforme sample. An intra-chromosomal deletion del(6)(q21q21) is responsible for the formation of GOPC-ROS1 chimeric protein which has a constitutive receptor tyrosine kinase activity. {ECO:0000269|PubMed:12661006}.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11162552, ECO:0000269|PubMed:11384996, ECO:0000269|PubMed:11707463}.; smooth muscle;ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;oesophagus;endometrium;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;epidermis;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;aorta;stomach; . 0.58095 0.13069 -0.626318434 17.03231894 74.93482 1.81139 GORAB 6.82629373307261e-06 0.715057451311503 0.284935722394763 golgin, RAB6-interacting . DISEASE: Geroderma osteodysplasticum (GO) [MIM:231070]: A rare autosomal recessive disorder characterized by lax, wrinkled skin, joint laxity and a typical face with a prematurely aged appearance. Skeletal signs include severe osteoporosis leading to frequent fractures, malar and mandibular hypoplasia and a variable degree of growth retardation. {ECO:0000269|PubMed:18997784}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.10544 0.08948 -0.468351206 23.42533616 48.46487 1.35806 GORASP1 0.698377750425013 0.300833855749465 0.000788393825522541 golgi reassembly stacking protein 1 FUNCTION: Stacking factor involved in the postmitotic assembly of Golgi stacks from mitotic Golgi fragments. Key structural protein required for the maintenance of the Golgi apparatus integrity: its caspase-mediated cleavage is required for fragmentation of the Golgi during apoptosis (By similarity). Also mediates, via its interaction with GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes (PubMed:16489344). {ECO:0000250|UniProtKB:O35254, ECO:0000269|PubMed:16489344}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;cerebellum;thymus; caudate nucleus;skeletal muscle;cerebellum; 0.28227 0.10211 1.352234299 94.36777542 239.43549 3.34388 GORASP2 0.891064439802649 0.108888811607109 4.67485902418441e-05 golgi reassembly stacking protein 2 FUNCTION: Plays a role in the assembly and membrane stacking of the Golgi cisternae, and in the process by which Golgi stacks reform after mitotic breakdown. May regulate the intracellular transport and presentation of a defined set of transmembrane proteins, such as transmembrane TGFA. {ECO:0000269|PubMed:10487747, ECO:0000269|PubMed:21515684}.; . . ovary;umbilical cord;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;pineal body;spinal cord;blood;lens;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;hippocampus;amnion;duodenum;head and neck;kidney;stomach;thymus;cerebellum; amygdala;superior cervical ganglion;testis - interstitial;placenta;testis; 0.30609 0.14799 -0.26993514 34.59542345 529.4287 4.69614 GOSR1 0.450937720669574 0.547775241018542 0.00128703831188464 golgi SNAP receptor complex member 1 FUNCTION: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide- sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi. {ECO:0000269|PubMed:15215310, ECO:0000269|PubMed:21860593}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;aorta; subthalamic nucleus;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;cerebellum; 0.54685 0.14936 -0.029247611 51.40363293 . . GOSR2 0.00028919421780916 0.794610519599903 0.205100286182288 golgi SNAP receptor complex member 2 FUNCTION: Involved in transport of proteins from the cis/medial- Golgi to the trans-Golgi network.; DISEASE: Epilepsy, progressive myoclonic 6 (EPM6) [MIM:614018]: A neurologic disorder characterized by onset of ataxia in the first years of life, followed by action myoclonus and seizures later in childhood, and loss of independent ambulation in the second decade. Cognition is not usually affected, although mild memory difficulties may occur in the third decade. {ECO:0000269|PubMed:21549339}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;lens;bile duct;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; testis - interstitial;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16926 0.11871 0.349177632 74.18023119 3077.20985 10.54284 GOT1 0.129221467229635 0.869800681712995 0.000977851057369666 glutamic-oxaloacetic transaminase 1, soluble FUNCTION: Biosynthesis of L-glutamate from L-aspartate or L- cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3- mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain. {ECO:0000269|PubMed:16039064}.; . . . . 0.21578 0.59876 -0.582225231 18.44184949 76.27807 1.83064 GOT1L1 2.11851720642321e-10 0.0357937232754938 0.964206276512655 glutamic-oxaloacetic transaminase 1-like 1 . . . testis; superior cervical ganglion; 0.05135 . -0.200157416 39.11299835 507.731 4.62149 GOT2 0.896491160129866 0.103467917416485 4.09224536495769e-05 glutamic-oxaloacetic transaminase 2 FUNCTION: Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids. {ECO:0000269|PubMed:9537447}.; . . myocardium;ovary;foreskin;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;oesophagus;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; whole brain;thalamus;subthalamic nucleus;liver;skeletal muscle;cingulate cortex;cerebellum; 0.23122 0.97542 0.308721233 72.59966973 996.67916 6.08458 GOT2P1 . . . glutamic-oxaloacetic transaminase 2 pseudogene 1 . . . . . . . . . . . GOT2P2 . . . glutamic-oxaloacetic transaminase 2 pseudogene 2 . . . . . . . . . . . GOT2P3 . . . glutamic-oxaloacetic transaminase 2 pseudogene 3 . . . . . . . . . . . GOT2P4 . . . glutamic-oxaloacetic transaminase 2 pseudogene 4 . . . . . . . . . . . GOT2P5 . . . glutamic-oxaloacetic transaminase 2 pseudogene 5 . . . . . . . . . . . GP1BA 0.0131577164310646 0.861392686440575 0.125449597128361 glycoprotein Ib platelet alpha subunit FUNCTION: GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium.; DISEASE: Non-arteritic anterior ischemic optic neuropathy (NAION) [MIM:258660]: An ocular disease due to ischemic injury to the optic nerve. It usually affects the optic disk and leads to visual loss and optic disk swelling of a pallid nature. Visual loss is usually sudden, or over a few days at most and is usually permanent, with some recovery possibly occurring within the first weeks or months. Patients with small disks having smaller or non- existent cups have an anatomical predisposition for non-arteritic anterior ischemic optic neuropathy. As an ischemic episode evolves, the swelling compromises circulation, with a spiral of ischemia resulting in further neuronal damage. {ECO:0000269|PubMed:14711733}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Bernard-Soulier syndrome (BSS) [MIM:231200]: A coagulation disorder characterized by a prolonged bleeding time, unusually large platelets, thrombocytopenia, and impaired prothrombin consumption. {ECO:0000269|PubMed:10089893, ECO:0000269|PubMed:1730088, ECO:0000269|PubMed:7690774, ECO:0000269|PubMed:7819107, ECO:0000269|PubMed:7873390, ECO:0000269|PubMed:9639514}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bernard-Soulier syndrome A2, autosomal dominant (BSSA2) [MIM:153670]: A coagulation disorder characterized by mild to moderate bleeding tendency, thrombocytopenia, and an increased mean platelet volume. Some individuals have no symptoms. Mild bleeding tendencies manifest as epistaxis, gingival bleeding, menorrhagia, easy bruising, or prolonged bleeding after dental surgery. {ECO:0000269|PubMed:11222377}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pseudo-von Willebrand disease (VWDP) [MIM:177820]: A bleeding disorder characterized by abnormally enhanced binding of von Willebrand factor by the platelet glycoprotein Ib (GP Ib) receptor complex. Hemostatic function is impaired due to the removal of VWF multimers from the circulation. {ECO:0000269|PubMed:14521605, ECO:0000269|PubMed:2052556, ECO:0000269|PubMed:8384898, ECO:0000269|PubMed:8486780}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;whole body;spleen;blood;bone marrow; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skin;skeletal muscle; 0.10914 0.54988 0.135991087 63.61759849 587.99997 4.91777 GP1BB 0.101120792076755 0.584233252261321 0.314645955661924 glycoprotein Ib platelet beta subunit FUNCTION: Gp-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to von Willebrand factor, which is already bound to the subendothelium.; . TISSUE SPECIFICITY: Expressed in heart and brain. {ECO:0000269|PubMed:8200976}.; . . 0.16068 . . . 33.41099 1.03099 GP2 1.13365800269189e-12 0.0434285951773897 0.956571404821477 glycoprotein 2 . . TISSUE SPECIFICITY: Pancreatic secretory (zymogen) granule.; unclassifiable (Anatomical System);prostate;pancreas;islets of Langerhans;nasopharynx;liver;spleen;skeletal muscle;stomach; pancreas;superior cervical ganglion;beta cell islets;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.37065 0.17461 -0.400392389 26.85185185 170.14124 2.84645 GP5 4.00900429038836e-06 0.213484397720296 0.786511593275413 glycoprotein V platelet FUNCTION: The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis.; . TISSUE SPECIFICITY: Platelets and megakaryocytes.; bone marrow; superior cervical ganglion;appendix;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09675 0.16811 -0.025608647 51.91672564 273.14874 3.54359 GP6 1.19709008860195e-14 0.00581488954461905 0.994185110455369 glycoprotein VI platelet FUNCTION: Collagen receptor involved in collagen-induced platelet adhesion and activation. Plays a key role in platelet procoagulant activity and subsequent thrombin and fibrin formation. This procoagulant function may contribute to arterial and venous thrombus formation. The signaling pathway involves the FcR gamma- chain, the Src kinases (likely Fyn/Lyn), the adapter protein LAT and leads to the activation of phospholipase C gamma2. {ECO:0000269|PubMed:10961879}.; DISEASE: Bleeding disorder, platelet-type 11 (BDPLT11) [MIM:614201]: A mild to moderate bleeding disorder caused by defective platelet activation and aggregation in response to collagen. {ECO:0000269|PubMed:19549989, ECO:0000269|PubMed:19552682}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Megakaryocytes and platelets. {ECO:0000269|PubMed:10961879}.; breast;tongue;epididymis;muscle;hypopharynx;colon;head and neck;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.04935 . 2.133152036 97.93583392 2178.85823 8.60122 GP9 0.570607601028968 0.383036099429935 0.0463562995410978 glycoprotein IX platelet FUNCTION: The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis. GP-IX may provide for membrane insertion and orientation of GP-Ib.; DISEASE: Bernard-Soulier syndrome (BSS) [MIM:231200]: A coagulation disorder characterized by a prolonged bleeding time, unusually large platelets, thrombocytopenia, and impaired prothrombin consumption. {ECO:0000269|PubMed:10583255, ECO:0000269|PubMed:11167791, ECO:0000269|PubMed:11758225, ECO:0000269|PubMed:12100158, ECO:0000269|PubMed:8481514, ECO:0000269|PubMed:9163595, ECO:0000269|PubMed:9886312}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;pancreas;lung;heart;liver;spleen;choroid;skin; skeletal muscle; 0.23572 0.22665 . . 370.65958 4.06642 GPA33 1.49713378108759e-06 0.628328022828167 0.371670480038052 glycoprotein A33 FUNCTION: May play a role in cell-cell recognition and signaling.; . TISSUE SPECIFICITY: Expressed in normal gastrointestinal epithelium and in 95% of colon cancers.; . . 0.10740 0.09823 0.132352165 63.48785091 190.04131 2.99213 GPAA1 2.89309136314948e-07 0.751050313471447 0.248949397219417 glycosylphosphatidylinositol anchor attachment 1 FUNCTION: Essential for GPI-anchoring of precursor proteins but not for GPI synthesis. Acts before or during formation of the carbonyl intermediate. {ECO:0000269|PubMed:9468317}.; . TISSUE SPECIFICITY: Ubiquitously expressed in fetal and adult tissues. Expressed at higher levels in fetal tissues than adult tissues. {ECO:0000269|PubMed:9468317}.; medulla oblongata;smooth muscle;ovary;salivary gland;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;synovium;bone;thyroid;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; prostate;heart;thyroid;liver; 0.09437 0.11978 0.224175308 68.48903043 269.44203 3.52155 GPAA1P1 . . . glycosylphosphatidylinositol anchor attachment 1 pseudogene 1 . . . . . . . . . . . GPAA1P2 . . . glycosylphosphatidylinositol anchor attachment 1 pseudogene 2 . . . . . . . . . . . GPALPP1 0.000396088218762865 0.847047277211305 0.152556634569932 GPALPP motifs containing 1 . . . . . 0.06253 0.10394 0.238945317 69.20853975 95.18227 2.10518 GPAM 0.000580579250988833 0.999410373591293 9.04715771798068e-06 glycerol-3-phosphate acyltransferase, mitochondrial FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. {ECO:0000250|UniProtKB:P97564, ECO:0000269|PubMed:18238778}.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;endometrium;thyroid;bone;testis;dura mater;germinal center;spinal ganglion;brain;artery;unclassifiable (Anatomical System);meninges;heart;spinal cord;blood;skeletal muscle;bile duct;pia mater;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;adipose tissue;skeletal muscle; 0.22152 0.37514 -0.242430445 36.22906346 242.46149 3.36070 GPANK1 0.000931901014120056 0.804435665045993 0.194632433939887 G-patch domain and ankyrin repeats 1 . . . . . 0.08422 . 0.41713504 76.95800896 1461.93567 7.13259 GPAT2 0.0016122998449236 0.992339400687431 0.00604829946764563 glycerol-3-phosphate acyltransferase 2, mitochondrial FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. {ECO:0000250}.; . . medulla oblongata;placenta;testis; . . . . . 151.08322 2.68731 GPAT3 . . . glycerol-3-phosphate acyltransferase 3 FUNCTION: May transfer the acyl-group from acyl-coA to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Also transfers the acyl-group from acyl-coA to the sn-2 position of 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid, or LPA), forming 1,2-diacyl-sn-glycerol-3- phosphate (phosphatidic acid, or PA). {ECO:0000269|PubMed:17002884, ECO:0000269|PubMed:17170135, ECO:0000269|PubMed:19318427}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in liver, kidney, testis, brain, heart, skeletal muscle, thyroid, prostate, thymus and placenta. Also expressed lung and adipose tissue. {ECO:0000269|PubMed:17002884, ECO:0000269|PubMed:17170135}.; . . 0.13125 0.11511 -0.089927255 46.99221515 . . GPAT4 . . . glycerol-3-phosphate acyltransferase 4 FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Active against both saturated and unsaturated long- chain fatty acyl-CoAs. {ECO:0000269|PubMed:18238778}.; . TISSUE SPECIFICITY: Ubiquitous. Relatively high level of expression in skeletal muscle, heart and testis. Relatively low level of expression in lung. {ECO:0000269|PubMed:12938015, ECO:0000269|PubMed:18238778}.; . . 0.17788 0.13340 -0.405853867 26.23260203 . . GPATCH1 3.44131002476153e-05 0.999944147165831 2.14397339212731e-05 G-patch domain containing 1 . . . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;muscle;colon;skeletal muscle;uterus;pancreas;lung;frontal lobe;larynx;nasopharynx;bone;thyroid;placenta;visual apparatus;pituitary gland;testis;head and neck;germinal center;kidney;brain;stomach; testis;white blood cells;trigeminal ganglion; 0.12487 . -0.211293113 37.76244397 310.91302 3.75292 GPATCH2 9.6600306030973e-05 0.986025694727082 0.0138777049668869 G-patch domain containing 2 FUNCTION: Enhances the ATPase activity of DHX15 in vitro. {ECO:0000269|PubMed:19432882}.; . TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:19432882}.; . . 0.35805 . 0.108486928 61.90728946 309.35921 3.74450 GPATCH2L 0.539068808366984 0.46090441283142 2.67788015962707e-05 G-patch domain containing 2 like . . . . . 0.17685 . 0.084621747 60.31493277 38.10571 1.13211 GPATCH3 6.05252012288109e-07 0.673308122059031 0.326691272688957 G-patch domain containing 3 . . . ovary;colon;skin;retina;uterus;whole body;frontal lobe;thyroid;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;kidney;mammary gland;stomach;thymus; . 0.05396 . -0.554717505 19.79830149 82.09693 1.92127 GPATCH4 1.68775621140413e-07 0.405527236548468 0.594472594675911 G-patch domain containing 4 . . . unclassifiable (Anatomical System);breast;uterus;pancreas;heart;nasopharynx;hippocampus;blood;brain;mammary gland;skin;stomach; . 0.05745 0.07896 0.685332364 85.09672092 171.79987 2.85887 GPATCH8 0.99949548967494 0.000504510321711166 3.34844784091655e-12 G-patch domain containing 8 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;nervous;blood;lens;skeletal muscle;bile duct;breast;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;testis - interstitial;subthalamic nucleus;prefrontal cortex;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex;skeletal muscle; 0.45714 0.10442 -0.742251371 13.78862939 262.93252 3.47830 GPATCH11 1.26665642095237e-05 0.381170947665872 0.618816385769919 G-patch domain containing 11 . . . . . 0.05413 0.09433 -0.073340031 48.11866006 143.65077 2.61292 GPBAR1 1.86484038880538e-06 0.0754040718503482 0.924594063309263 G protein-coupled bile acid receptor 1 FUNCTION: Receptor for bile acid. Bile acid-binding induces its internalization, activation of extracellular signal-regulated kinase and intracellular cAMP production. May be involved in the suppression of macrophage functions by bile acids. {ECO:0000269|PubMed:12419312, ECO:0000269|PubMed:12524422}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at higher level in spleen and placenta. Expressed at lower level in other tissues. In digestive tissues, it is expressed in stomach, duodenum, ileocecum, ileum, jejunum, ascending colon, transverse colon, descending colon, cecum and liver, but not in esophagus and rectum. {ECO:0000269|PubMed:12044878, ECO:0000269|PubMed:12419312, ECO:0000269|PubMed:12524422}.; . . . . 0.062575634 58.74026893 75.49312 1.81813 GPBP1 0.975851112431475 0.0241478409167017 1.04665182318739e-06 GC-rich promoter binding protein 1 FUNCTION: Functions as a GC-rich promoter-specific transactivating transcription factor. {ECO:0000250|UniProtKB:Q6NXH3}.; . TISSUE SPECIFICITY: Widely expressed. Some isoforms may be specifically expressed in veins and arteries (at protein level). Isoform 4 is widely expressed. Isoform 1, isoform 2 and isoform 3 may be specifically expressed in vascular smooth muscle cells. {ECO:0000269|PubMed:12842993, ECO:0000269|PubMed:14612417}.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;cochlea;thyroid;germinal center;bladder;brain;heart;pineal body;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;kidney;aorta;stomach;cerebellum;thymus; amygdala;subthalamic nucleus;testis - interstitial;occipital lobe;medulla oblongata;testis - seminiferous tubule;globus pallidus;testis;atrioventricular node;parietal lobe; 0.84318 0.11313 0.042348793 57.31304553 66.67652 1.68454 GPBP1L1 0.435324050435863 0.564381337942621 0.000294611621515938 GC-rich promoter binding protein 1 like 1 FUNCTION: Possible transcription factor. {ECO:0000305}.; . . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;bone;pituitary gland;testis;amniotic fluid;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;blood;lens;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.56585 0.10266 -0.977252525 8.799245105 188.2901 2.97932 GPC1 0.109569938244377 0.884058457158115 0.00637160459750771 glypican 1 FUNCTION: Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling. {ECO:0000250, ECO:0000269|PubMed:19936054, ECO:0000269|PubMed:21642435}.; DISEASE: Note=Associates (via the heparan sulfate side chains) with fibrillar APP-beta amyloid peptides in primitive and classic amyloid plaques and may be involved in the deposition of these senile plaques in the Alzheimer disease (AD) brain (PubMed:15084524). {ECO:0000269|PubMed:15084524}.; DISEASE: Note=Misprocessing of GPC1 is found in fibroblasts of patients with Niemann-Pick Type C1 disease. This is due to the defective deaminative degradation of heparan sulfate chains (PubMed:16645004). {ECO:0000269|PubMed:16645004}.; . myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;iris;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;muscle;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;alveolus;head and neck;cervix;kidney;mammary gland;stomach;thymus; amygdala;heart;prefrontal cortex;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.18428 0.26249 -1.015898037 8.144609578 . . GPC2 0.307395086157098 0.691807682227599 0.000797231615302419 glypican 2 FUNCTION: Cell surface proteoglycan that bears heparan sulfate. May fulfill a function related to the motile behaviors of developing neurons (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;frontal lobe;brain; . 0.11100 . -0.868835007 10.65109696 35.7743 1.07628 GPC3 0.987985908845658 0.0120095097651898 4.58138915265795e-06 glypican 3 FUNCTION: Cell surface proteoglycan that bears heparan sulfate. Inhibits the dipeptidyl peptidase activity of DPP4. May be involved in the suppression/modulation of growth in the predominantly mesodermal tissues and organs. May play a role in the modulation of IGF2 interactions with its receptor and thereby modulate its function. May regulate growth and tumor predisposition. {ECO:0000269|PubMed:17549790}.; . TISSUE SPECIFICITY: Highly expressed in lung, liver and kidney.; . . 0.78059 0.36196 -0.448125345 24.19202642 61.55096 1.59866 GPC4 0.948476974816376 0.0514889498050591 3.40753785649734e-05 glypican 4 FUNCTION: Cell surface proteoglycan that bears heparan sulfate. May be involved in the development of kidney tubules and of the central nervous system (By similarity). {ECO:0000250}.; . . . . 0.87492 0.15966 -0.071520315 48.34866714 5960.27493 16.04688 GPC5 1.99113939736555e-05 0.894331187850491 0.105648900755535 glypican 5 FUNCTION: Cell surface proteoglycan that bears heparan sulfate. {ECO:0000250}.; . TISSUE SPECIFICITY: In adult, primarily expressed in the brain. Also detected in fetal brain, lung and liver. {ECO:0000269|PubMed:9070915, ECO:0000269|PubMed:9331333}.; . . 0.67301 0.15304 -0.819281839 11.93677754 2274.18788 8.81899 GPC5-AS1 . . . GPC5 antisense RNA 1 . . . . . . . . . . . GPC5-AS2 . . . GPC5 antisense RNA 2 . . . . . . . . . . . GPC5-IT1 . . . GPC5 intronic transcript 1 . . . . . . . . . . . GPC6 0.338854613354057 0.660526121878298 0.000619264767644976 glypican 6 FUNCTION: Cell surface proteoglycan that bears heparan sulfate. Putative cell surface coreceptor for growth factors, extracellular matrix proteins, proteases and anti-proteases (By similarity). Enhances migration and invasion of cancer cells through WNT5A signaling. {ECO:0000250, ECO:0000269|PubMed:21871017}.; DISEASE: Omodysplasia 1 (OMOD1) [MIM:258315]: A rare autosomal recessive skeletal dysplasia characterized by facial dysmorphism and severe congenital micromelia with shortening and distal tapering of the humeri and femora, to give a club-like appearance. Typical facial features include a prominent forehead, frontal bossing, short nose with a depressed broad bridge, short columella, anteverted nostrils, long philtrum, and small chin. {ECO:0000269|PubMed:19481194}. Note=The disease is caused by mutations affecting the gene represented in this entry. Point mutations leading to protein truncation, as well as larger genomic rearrangements resulting in exon deletions, have been found in family segregating omodysplasia type 1. All mutations identified in individuals affected by omodysplasia could lead to the absence of a functional protein, the mutant RNAs being suspected to be nonsense-mediated mRNA decay (NMD) targets. Even if the mRNA escapes NMD and is translated, all mutations are expected to disrupt the three-dimensional protein structure and often to abolish multiple highly conserved cysteine residues.; TISSUE SPECIFICITY: Widely expressed. High expression in fetal kidney and lung and lower expressions in fetal liver and brain. In adult tissues, very abundant in ovary, high levels also observed in liver, kidney, small intestine and colon. Not detected in peripheral blood leukocytes. Detected in breast cancer cells (at protein level). {ECO:0000269|PubMed:10480909, ECO:0000269|PubMed:21871017}.; . . 0.68500 . 0.020302773 55.60863411 2044.39602 8.33745 GPC6-AS1 . . . GPC6 antisense RNA 1 . . . . . . . . . . . GPC6-AS2 . . . GPC6 antisense RNA 2 . . . . . . . . . . . GPCPD1 0.125571598748616 0.874386145680133 4.22555712515332e-05 glycerophosphocholine phosphodiesterase 1 FUNCTION: May be involved in the negative regulation of skeletal muscle differentiation, independently of its glycerophosphocholine phosphodiesterase activity. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in spinal chord.; . . . . -0.201976964 38.98325077 1192.76751 6.54937 GPD1 0.147319093451793 0.834779708437735 0.0179011981104714 glycerol-3-phosphate dehydrogenase 1 . DISEASE: Hypertriglyceridemia, transient infantile (HTGTI) [MIM:614480]: An autosomal recessive disorder characterized by onset of moderate to severe transient hypertriglyceridemia in infancy that normalizes with age. The hypertriglyceridemia is associated with hepatomegaly, moderately elevated transaminases, persistent fatty liver, and the development of hepatic fibrosis. {ECO:0000269|PubMed:22226083, ECO:0000269|PubMed:24549054}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;cerebral cortex;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;macula lutea;hippocampus;visual apparatus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;adipose tissue;spinal cord;liver;pons;kidney;trigeminal ganglion;skeletal muscle; 0.79940 0.52323 0.15257911 64.60839821 153.40117 2.70922 GPD1L 0.00953782790179044 0.940551460776925 0.0499107113212847 glycerol-3-phosphate dehydrogenase 1-like FUNCTION: Plays a role in regulating cardiac sodium current; decreased enzymatic activity with resulting increased levels of glycerol 3-phosphate activating the DPD1L-dependent SCN5A phosphorylation pathway, may ultimately lead to decreased sodium current; cardiac sodium current may also be reduced due to alterations of NAD(H) balance induced by DPD1L. {ECO:0000269|PubMed:19666841, ECO:0000269|PubMed:19745168}.; DISEASE: Sudden infant death syndrome (SIDS) [MIM:272120]: SIDS is the sudden death of an infant younger than 1 year that remains unexplained after a thorough case investigation, including performance of a complete autopsy, examination of the death scene, and review of clinical history. Pathophysiologic mechanisms for SIDS may include respiratory dysfunction, cardiac dysrhythmias, cardiorespiratory instability, and inborn errors of metabolism, but definitive pathogenic mechanisms precipitating an infant sudden death remain elusive. {ECO:0000269|PubMed:17967976}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Most highly expressed in heart tissue, with lower levels in the skeletal muscle, kidney, lung and other organs. {ECO:0000269|PubMed:17967977}.; myocardium;lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;urinary;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;amnion;head and neck;kidney;stomach;aorta;cerebellum; skeletal muscle; 0.57173 0.17371 -0.492218069 22.35786742 25.53397 0.83259 GPD2 0.000100774785789542 0.997183216468283 0.00271600874592729 glycerol-3-phosphate dehydrogenase 2 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;skin;skeletal muscle;retina;uterus;breast;lung;hypopharynx;liver;testis;head and neck;spleen;germinal center;brain;stomach; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.43617 0.51354 0.224175308 68.48903043 295.46766 3.67045 GPDS1 . . . glaucoma-related pigment dispersion syndrome 1 . . . . . . . . . . . GPER1 0.725420978638944 0.261605333573653 0.0129736877874037 G protein-coupled estrogen receptor 1 FUNCTION: G-protein coupled estrogen receptor that binds to 17- beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth factor (HB-EGF) and subsequent transactivation of the epidermal growth factor receptor (EGFR), activating downstream signaling pathways such as PI3K/Akt and ERK/MAPK. Mediates pleiotropic functions among others in the cardiovascular, endocrine, reproductive, immune and central nervous systems. Has a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a RAMP3-dependent manner. Regulates arterial blood pressure by stimulating vasodilation and reducing vascular smooth muscle and microvascular endothelial cell proliferation. Plays a role in blood glucose homeostasis contributing to the insulin secretion response by pancreatic beta cells. Triggers mitochondrial apoptosis during pachytene spermatocyte differentiation. Stimulates uterine epithelial cell proliferation. Enhances uterine contractility in response to oxytocin. Contributes to thymic atrophy by inducing apoptosis. Attenuates TNF-mediated endothelial expression of leukocyte adhesion molecules. Promotes neuritogenesis in developing hippocampal neurons. Plays a role in acute neuroprotection against NMDA- induced excitotoxic neuronal death. Increases firing activity and intracellular calcium oscillations in luteinizing hormone- releasing hormone (LHRH) neurons. Inhibits early osteoblast proliferation at growth plate during skeletal development. Inhibits mature adipocyte differentiation and lipid accumulation. Involved in the recruitment of beta-arrestin 2 ARRB2 at the plasma membrane in epithelial cells. Functions also as a receptor for aldosterone mediating rapid regulation of vascular contractibility through the PI3K/ERK signaling pathway. Involved in cancer progression regulation. Stimulates cancer-associated fibroblast (CAF) proliferation by a rapid genomic response through the EGFR/ERK transduction pathway. Associated with EGFR, may act as a transcription factor activating growth regulatory genes (c-fos, cyclin D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN) matrix assembly in breast cancer cells. {ECO:0000269|PubMed:11043579, ECO:0000269|PubMed:15539556, ECO:0000269|PubMed:15705806, ECO:0000269|PubMed:19179659, ECO:0000269|PubMed:19342448, ECO:0000269|PubMed:20203690, ECO:0000269|PubMed:20551055, ECO:0000269|PubMed:21149639, ECO:0000269|PubMed:21242460, ECO:0000269|PubMed:21427217, ECO:0000269|PubMed:23135268, ECO:0000269|PubMed:23283935, ECO:0000269|PubMed:23285008, ECO:0000269|PubMed:23674134}.; . TISSUE SPECIFICITY: Expressed in placenta, endothelial and epithelial cells, non laboring and laboring term myometrium, fibroblasts and cancer-associated fibroblasts (CAF), prostate cancer cells and invasive adenocarcinoma (at protein level). Ubiquitously expressed, but is most abundant in placenta. In brain regions, expressed as a 2.8 kb transcript in basal forebrain, frontal cortex, thalamus, hippocampus, caudate and putamen. {ECO:0000269|PubMed:20203690, ECO:0000269|PubMed:20551055, ECO:0000269|PubMed:21149639, ECO:0000269|PubMed:21354433, ECO:0000269|PubMed:21427217, ECO:0000269|PubMed:23285008}.; . . 0.07814 0.13437 -0.288341872 33.41589998 417.97863 4.27645 GPHA2 2.06936557406623e-05 0.280970277581512 0.719009028762747 glycoprotein hormone alpha 2 FUNCTION: Stimulates the thyroid. Binds and activates THSR, leads to increased cAMP production. {ECO:0000269|PubMed:12045258}.; . TISSUE SPECIFICITY: Found in a variety of tissues. {ECO:0000269|PubMed:12089349}.; unclassifiable (Anatomical System);cartilage;heart;adrenal cortex;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;endometrium;adrenal gland;thyroid;macula lutea;alveolus;testis;kidney;brain;pineal gland; . 0.27609 0.11395 -0.251530012 35.42108988 12.08689 0.43793 GPHB5 . . . glycoprotein hormone beta 5 FUNCTION: Stimulates the thyroid. Binds and activates THSR, leading to increased cAMP production. {ECO:0000269|PubMed:12045258, ECO:0000269|PubMed:16210345}.; . TISSUE SPECIFICITY: Highly expressed in brain and at low levels in pituitary. Also found in retina, testis and skin but not in pancreas, parotid, kidney, stomach, liver, colon, small intestine, thyroid, brain or adrenal gland. In pituitary, colocalizes with ACTH, suggesting that it is located in corticotrophs. {ECO:0000269|PubMed:12089349, ECO:0000269|PubMed:16210345}.; . . 0.22919 0.08540 . . . . GPHN 0.999981472805078 1.8527194792572e-05 1.29034232501701e-13 gephyrin FUNCTION: Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules (By similarity). Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. {ECO:0000250}.; DISEASE: Molybdenum cofactor deficiency, complementation group C (MOCODC) [MIM:615501]: A form of molybdenum cofactor deficiency, an autosomal recessive metabolic disorder leading to the pleiotropic loss of molybdoenzyme activities. It is clinically characterized by onset in infancy of poor feeding, intractable seizures, severe psychomotor retardation, and death in early childhood in most patients. {ECO:0000269|PubMed:11095995, ECO:0000269|PubMed:22040219}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;cerebellum; superior cervical ganglion;ciliary ganglion; 0.13794 0.40936 0.062575634 58.74026893 27.01369 0.87259 GPI 0.0015814519272106 0.997145391194375 0.00127315687841401 glucose-6-phosphate isomerase FUNCTION: Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons. {ECO:0000269|PubMed:11004567, ECO:0000269|PubMed:11437381}.; DISEASE: Hemolytic anemia, non-spherocytic, due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:613470]: A form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; whole brain;thalamus;occipital lobe;heart;cerebellum peduncles;temporal lobe;prefrontal cortex;liver;caudate nucleus;parietal lobe;cerebellum; 0.36660 0.85936 -0.909290275 10.03184713 131.65784 2.49774 GPIHBP1 0.023780962945537 0.772772146614099 0.203446890440364 glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1 FUNCTION: Plays a key role in the lipolytic processing of chylomicrons. Required for the transport of lipoprotein lipase LPL into the capillary lumen (By similarity). {ECO:0000250}.; DISEASE: Hyperlipoproteinemia 1D (HLPP1D) [MIM:615947]: An autosomal recessive disorder characterized by hyperlipoproteinemia, decreased plasma LPL levels in some patients, high plasma triglyceride levels, and refractory fasting chylomicronemia. {ECO:0000269|PubMed:19304573, ECO:0000269|PubMed:20026666, ECO:0000269|PubMed:21816778}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);optic nerve;lung;cartilage;heart;endometrium;pineal body;testis;spinal ganglion;brain;skeletal muscle; subthalamic nucleus;occipital lobe;temporal lobe;globus pallidus;ciliary ganglion;pons;atrioventricular node;caudate nucleus;trigeminal ganglion;parietal lobe; 0.09775 0.08547 0.283038099 71.26680821 1903.93816 8.02633 GPKOW 0.979573126517589 0.0204099945887753 1.68788936355326e-05 G-patch domain and KOW motifs . . . medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;pituitary gland;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.07384 0.08716 -0.381986487 27.68931352 35.20025 1.06605 GPLD1 5.63947612847098e-09 0.99802777437441 0.00197221998611406 glycosylphosphatidylinositol specific phospholipase D1 FUNCTION: This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane.; . . unclassifiable (Anatomical System);lymphoreticular;heart;sympathetic chain;blood;skin;retina;uterus;prostate;lung;visual apparatus;liver;testis;spleen;germinal center; superior cervical ganglion;testis - seminiferous tubule;temporal lobe;liver;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.29457 0.11794 0.279193852 70.77730597 885.76891 5.79686 GPM6A 0.952961852044875 0.0469048675991595 0.000133280355965938 glycoprotein M6A FUNCTION: Involved in neuronal differentiation, including differentiation and migration of neuronal stem cells. Plays a role in neuronal plasticity and is involved in neurite and filopodia outgrowth, filopodia motility and probably synapse formation. GPM6A-induced filopodia formation involves mitogen-activated protein kinase (MAPK) and Src signaling pathways. May be involved in neuronal NGF-dependent Ca(2+) influx. May be involved in regulation of endocytosis and intracellular trafficking of G- protein-coupled receptors (GPCRs); enhances internalization and recycling of mu-type opioid receptor. {ECO:0000269|PubMed:19298174}.; . . ovary;parathyroid;choroid;fovea centralis;retina;uterus;optic nerve;whole body;frontal lobe;cerebral cortex;iris;brain;unclassifiable (Anatomical System);amygdala;lymph node;islets of Langerhans;hypothalamus;spinal cord;lens;skeletal muscle;lung;placenta;hippocampus;visual apparatus;macula lutea;kidney; whole brain;amygdala;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.80608 0.11262 -0.163345027 41.24793583 5.49379 0.20459 GPM6B 0.494053306674971 0.501448058980174 0.00449863434485549 glycoprotein M6B FUNCTION: May be involved in neural development. Involved in regulation of osteoblast function and bone formation. Involved in matrix vesicle release by osteoblasts; this function seems to involve maintenance of the actin cytoskeleton. May be involved in cellular trafficking of SERT and thereby in regulation of serotonin uptake. {ECO:0000269|PubMed:21638316}.; . TISSUE SPECIFICITY: Neurons and glia; cerebellar Bergmann glia, in glia within white matter tracts of the cerebellum and cerebrum, and in embryonic dorsal root ganglia.; ovary;salivary gland;sympathetic chain;colon;parathyroid;choroid;skin;bone marrow;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;testis;spinal ganglion;bladder;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;nervous;hypothalamus;spinal cord;pharynx;blood;breast;lung;adrenal gland;internal ear;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;cerebellum; whole brain;dorsal root ganglion;amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;atrioventricular node;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.92659 0.13588 -0.05129383 49.75819769 12.17701 0.44088 GPM6BP1 . . . glycoprotein M6B pseudogene 1 . . . . . . . . . . . GPM6BP2 . . . glycoprotein M6B pseudogene 2 . . . . . . . . . . . GPM6BP3 . . . glycoprotein M6B pseudogene 3 . . . . . . . . . . . GPN1 0.0049035919998219 0.989091992642152 0.0060044153580257 GPN-loop GTPase 1 FUNCTION: Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII) (PubMed:20855544, PubMed:21768307). May act at an RNAP assembly step prior to nuclear import (PubMed:21768307). Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding proteins, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation (PubMed:17643375). May be involved in nuclear localization of XPA (PubMed:11058119). {ECO:0000269|PubMed:17643375, ECO:0000269|PubMed:20855544, ECO:0000269|PubMed:21768307, ECO:0000305|PubMed:11058119}.; . TISSUE SPECIFICITY: Expressed ubiquitously.; ovary;sympathetic chain;colon;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;small intestine;tongue;islets of Langerhans;muscle;adrenal cortex;lung;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis;ciliary ganglion;atrioventricular node; 0.08087 0.09383 -0.001743238 53.85114414 1208.68215 6.58462 GPN2 0.0369234540989058 0.92881818466289 0.0342583612382041 GPN-loop GTPase 2 FUNCTION: Small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import. {ECO:0000250|UniProtKB:Q08726}.; . . . . 0.14055 0.11191 0.040529541 57.15380986 126.21801 2.44517 GPN3 0.000100471691467198 0.804648764548428 0.195250763760104 GPN-loop GTPase 3 FUNCTION: Small GTPase required for proper localization of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import. {ECO:0000269|PubMed:21768307}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; . 0.51050 0.10747 -0.381986487 27.68931352 60.55868 1.58137 GPN3P1 . . . GPN-loop GTPase 3 pseudogene 1 . . . . . . . . . . . GPNMB 1.12477120855255e-12 0.0819062119410753 0.9180937880578 glycoprotein nmb FUNCTION: Could be a melanogenic enzyme. {ECO:0000250}.; . TISSUE SPECIFICITY: Up-regulated in various cancer cells, including in glioblastoma multiforme. Expressed in many melanoma cells, as well as in tissue macrophages, including liver Kuppfer cells and lung alveolar macrophages, in podocytes and in some cells of the ciliary body of the eye (at protein level). Hardly detectable in healthy brain. {ECO:0000269|PubMed:16489096, ECO:0000269|PubMed:16609006, ECO:0000269|PubMed:7814155}.; myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;cochlea;endometrium;thyroid;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;mesenchyma;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;uterus corpus;lymph node;adipose tissue;tongue;salivary gland;placenta;ciliary ganglion;skin; 0.70223 0.13545 0.892856963 89.28992687 437.62024 4.36108 GPR1 1.8355531462035e-05 0.264277150233622 0.735704494234916 G protein-coupled receptor 1 FUNCTION: Receptor for the inflammation-associated leukocyte chemoattractant chemerin/RARRES2 suggesting a role for this receptor in the regulation of inflammation. Can act as a coreceptor for HIV-1. {ECO:0000269|PubMed:18165312}.; . TISSUE SPECIFICITY: Expressed in hippocampus.; . . 0.42235 0.12474 0.573279816 82.08303845 3005.9513 10.40661 GPR1-AS . . . GPR1 antisense RNA . . . . . . . . . . . GPR3 0.0209357972702136 0.751114612977536 0.22794958975225 G protein-coupled receptor 3 FUNCTION: Orphan receptor with constitutive G(s) signaling activity that activate cyclic AMP. Has a potential role in modulating a number of brain functions, including behavioral responses to stress (By similarity), amyloid-beta peptide generation in neurons and neurite outgrowth (By similarity). Maintains also meiotic arrest in oocytes (By similarity). {ECO:0000250, ECO:0000269|PubMed:19213921}.; . TISSUE SPECIFICITY: Expressed predominantly in the central nervous system, and at low levels in the lung, kidney, testis, ovary and eye. Highly expressed in regions of the brain implicated in the Alzheimer disease.; . . 0.64069 0.11438 0.060756528 58.52795471 114.40031 2.33012 GPR4 0.165986421627129 0.772333517328805 0.0616800610440659 G protein-coupled receptor 4 FUNCTION: Proton-sensing receptor coupled to several G-proteins, including G(s), G(13) and G(q)/G(11) proteins, leading to cAMP production. {ECO:0000269|PubMed:12955148, ECO:0000269|PubMed:17462861}.; . . unclassifiable (Anatomical System);heart;colon;skin;uterus;lung;thyroid;liver;testis;spleen;kidney;brain;stomach;cerebellum; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.17528 0.14766 -0.405853867 26.23260203 3.50108 0.12685 GPR6 0.746040034732595 0.243495944591874 0.0104640206755314 G protein-coupled receptor 6 FUNCTION: Orphan receptor with constitutive G(s) signaling activity that activate cyclic AMP. Promotes neurite outgrowth and blocks myelin inhibition in neurons (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);hypothalamus; superior cervical ganglion;medulla oblongata;caudate nucleus;pons; 0.32471 0.11399 0.082802743 60.09082331 69.96255 1.73589 GPR12 0.852043161669527 0.145490451077995 0.00246638725247726 G protein-coupled receptor 12 FUNCTION: Promotes neurite outgrowth and blocks myelin inhibition in neurons (By similarity). Receptor with constitutive G(s) signaling activity that stimulates cyclic AMP production. {ECO:0000250}.; . . . . 0.14509 . 0.170987912 65.5579146 23.77511 0.78578 GPR15 0.00326499920869601 0.604715554106753 0.392019446684551 G protein-coupled receptor 15 FUNCTION: Probable chemokine receptor. Alternative coreceptor with CD4 for HIV-1 infection.; . . hypothalamus;liver;blood;kidney; trigeminal ganglion;skeletal muscle; 0.09210 0.11997 0.485092724 79.37603208 1411.49836 7.01710 GPR17 1.06559378636528e-05 0.198646253324262 0.801343090737875 G protein-coupled receptor 17 FUNCTION: Dual specificity receptor for uracil nucleotides and cysteinyl leukotrienes (CysLTs). Signals through G(i) and inhibition of adenylyl cyclase. May mediate brain damage by nucleotides and CysLTs following ischemia. {ECO:0000269|PubMed:16990797}.; . TISSUE SPECIFICITY: Expressed in brain, kidney, heart and umbilical vein endothelial cells. Highest level in brain. {ECO:0000269|PubMed:16990797}.; unclassifiable (Anatomical System);uterus;lung;heart;hypothalamus;placenta;colon;kidney;brain;skeletal muscle;skin;stomach; whole brain;amygdala;dorsal root ganglion;superior cervical ganglion;olfactory bulb;hypothalamus;spinal cord;pons;atrioventricular node;skeletal muscle;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.21346 0.13022 -0.352661697 29.48808681 95.63056 2.11167 GPR18 9.91795601258391e-07 0.183384425005779 0.81661458319862 G protein-coupled receptor 18 FUNCTION: Receptor for N-arachidonyl glycine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. May contribute to regulation of the immune system. {ECO:0000269|PubMed:16844083}.; . TISSUE SPECIFICITY: Most abundant in testis and spleen. Highly expressed in CD4 and CD8-positive T-cells as well as CD19-positive B-cells. {ECO:0000269|PubMed:16844083}.; unclassifiable (Anatomical System);medulla oblongata;nasopharynx;liver;testis;spleen;germinal center;bone marrow; testis - interstitial;superior cervical ganglion;testis;white blood cells;trigeminal ganglion;tonsil; 0.07084 0.10178 -0.47017169 23.25430526 28.62864 0.91652 GPR19 0.348589813892755 0.638061840230636 0.0133483458766091 G protein-coupled receptor 19 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Abundant expression in the brain.; unclassifiable (Anatomical System);placenta;brain; superior cervical ganglion;trigeminal ganglion;cerebellum; 0.38476 0.10046 0.373041938 75.29488087 35.08917 1.06463 GPR20 0.315068599677581 0.615155302773598 0.0697760975488216 G protein-coupled receptor 20 FUNCTION: Orphan receptor with constitutive G(i) signaling activity that activate cyclic AMP. {ECO:0000269|PubMed:18347022}.; . TISSUE SPECIFICITY: Ubiquitous with highest levels in intestinal tissues. In the brain detected in thalamus, putamen, and caudate, but not in frontal cortex, pons and hypothalamus. {ECO:0000269|PubMed:18347022}.; . . 0.25166 0.10874 -0.310388054 32.14791224 693.68114 5.25284 GPR21 0.0246511140506383 0.778578241369907 0.196770644579454 G protein-coupled receptor 21 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Not detected in the brain regions thalamus, putamen, caudate, frontal cortex, pons, hypothalamus, hippocampus.; . . 0.44821 . -0.404032746 26.53338051 103.008 2.19332 GPR22 0.427181284606709 0.571277791271145 0.00154092412214588 G protein-coupled receptor 22 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: In the brain regions frontal cortex, caudate, putamen and thalamus; not in pons, hypothalamus and hippocampus.; unclassifiable (Anatomical System);lung;atrium;frontal lobe;heart;testis;brain; subthalamic nucleus;superior cervical ganglion;fetal brain;globus pallidus;trigeminal ganglion;parietal lobe;skeletal muscle; 0.97891 0.11262 -0.361761279 28.6329323 12.01943 0.43621 GPR25 0.00563545142572482 0.720257784569597 0.274106764004678 G protein-coupled receptor 25 FUNCTION: Orphan receptor.; . . unclassifiable (Anatomical System); globus pallidus;ciliary ganglion;trigeminal ganglion; 0.46411 0.11621 . . 69.25611 1.72399 GPR26 0.627337376565242 0.365365814953039 0.00729680848171806 G protein-coupled receptor 26 FUNCTION: Orphan receptor. Displays a significant level of constitutive activity. Its effect is mediated by G(s)-alpha protein that stimulate adenylate cyclase, resulting in an elevation of intracellular cAMP. {ECO:0000269|PubMed:17363172}.; . TISSUE SPECIFICITY: Highly expressed in the CNS, the highest expression is seen in the amygdala, hippocampus and thalamus. Weak expression is detected in testis. Down-regulated in glioblastoma. {ECO:0000269|PubMed:17363172, ECO:0000269|PubMed:18037267}.; unclassifiable (Anatomical System);brain; dorsal root ganglion;superior cervical ganglion;testis - interstitial;temporal lobe;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16795 0.11125 . . 15.615 0.55670 GPR27 0.598851196353134 0.36316290890944 0.0379858947374261 G protein-coupled receptor 27 FUNCTION: Orphan receptor. Possible candidate for amine-like G- protein coupled receptor.; . TISSUE SPECIFICITY: Highly expressed as a 3.0 kb transcript in brain, ovary, testis, heart, prostate and peripheral Leukocytes. Lower levels in pancreas and small intestine. A 2.3 kb transcript was also found in peripheral Leukocytes. In brain regions, detected as a 3.0 kb transcript in all regions tested. Highest levels in the caudate nucleus, putamen, hippocampus and subthalamic nucleus. Lowest level in the cerebellum.; unclassifiable (Anatomical System);pancreas;ovary;placenta;visual apparatus;parathyroid;blood;brain; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.07426 . . . 12.51484 0.45565 GPR31 0.000351018338141658 0.378149617868468 0.62149936379339 G protein-coupled receptor 31 FUNCTION: High-affinity receptor for 12-(S)-hydroxy-5,8,10,14- eicosatetraenoic acid (12-S-HETE). 12-(S)-HETE is an arachidonic acid metabolite secreted by platelets and tumor cells, and known to induce endothelial cells retraction allowing invasive cell access to the subendothelial matrix, which is a critical step for extravasation or metastasis. Ligand-binding lead to activation of ERK1/2 (MAPK3/MAPK1), MEK, and NF-kappa-B. {ECO:0000269|PubMed:21712392}.; . . . . 0.09399 0.11901 0.485092724 79.37603208 70.1629 1.73954 GPR32 7.90945665733303e-05 0.31503876570359 0.684882139729836 G protein-coupled receptor 32 FUNCTION: Orphan receptor.; . . unclassifiable (Anatomical System);placenta; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.08930 . 0.108486928 61.90728946 99.68741 2.16289 GPR32P1 . . . G protein-coupled receptor 32, pseudogene 1 FUNCTION: Orphan receptor.; . . . . . . . . . . GPR33 . . . G protein-coupled receptor 33 (gene/pseudogene) FUNCTION: Orphan receptor; could be a chemoattractant receptor.; . TISSUE SPECIFICITY: Expressed in spleen, lung, heart, liver, kidney, pancreas, thymus, gonads and leukocytes. {ECO:0000269|PubMed:15987686}.; . . . . . . . . GPR34 0.457038660900044 0.516270244756416 0.0266910943435402 G protein-coupled receptor 34 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Broadly expressed.; . . 0.32139 0.10446 0.03689118 56.64071715 41.07152 1.20330 GPR35 0.00363558120757164 0.628014565849745 0.368349852942684 G protein-coupled receptor 35 FUNCTION: Acts as a receptor for kynurenic acid, an intermediate in the tryptophan metabolic pathway. The activity of this receptor is mediated by G-proteins that elicit calcium mobilization and inositol phosphate production through G(qi/o) proteins. {ECO:0000269|PubMed:16754668}.; . TISSUE SPECIFICITY: Predominantly expressed in immune and gastrointestinal tissues. {ECO:0000269|PubMed:16754668}.; unclassifiable (Anatomical System);breast;lung;testis;colon;blood;stomach; dorsal root ganglion;superior cervical ganglion;pons;atrioventricular node;skeletal muscle;parietal lobe; 0.10566 0.11148 1.467941683 95.26421326 475.95713 4.50591 GPR36 . . . G protein-coupled receptor 36 . . . . . . . . . . . GPR37 0.799390711133167 0.200367973439842 0.00024131542699102 G protein-coupled receptor 37 FUNCTION: Receptor for the neuroprotective and glioprotective factor prosaposin. Ligand binding induces endocytosis, followed by an ERK phosphorylation cascade. {ECO:0000269|PubMed:11439185, ECO:0000269|PubMed:23690594, ECO:0000269|PubMed:9526070}.; . TISSUE SPECIFICITY: Expressed in brain and spinal cord, and at lower levels in testis, placenta and liver, but no detectable expression observed in any other tissue. When overexpressed in cells, tends to become insoluble and unfolded. Accumulation of the unfolded protein may lead to dopaminergic neuronal death in juvenile Parkinson disease (PDJ). {ECO:0000269|PubMed:9526070}.; unclassifiable (Anatomical System);cartilage;cerebellum cortex;hypothalamus;fovea centralis;skin;whole body;lung;frontal lobe;placenta;macula lutea;hippocampus;duodenum;liver;testis;kidney;brain; amygdala;whole brain;medulla oblongata;superior cervical ganglion;occipital lobe;thalamus;hypothalamus;spinal cord;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;testis;cingulate cortex;parietal lobe;cerebellum; 0.85075 0.16646 -0.422438699 25.64284029 106.05545 2.23398 GPR37L1 2.88015901916168e-07 0.17150211398622 0.828497597997878 G protein-coupled receptor 37 like 1 FUNCTION: Receptor for the neuroprotective and glioprotective factor prosaposin. Ligand binding induces endocytosis, followed by an ERK phosphorylation cascade. {ECO:0000269|PubMed:23690594}.; . TISSUE SPECIFICITY: Expressed in the central nervous system.; . . 0.21248 0.11578 -0.420619508 25.72540694 700.47828 5.26476 GPR39 1.54608229502499e-12 0.00199704096836732 0.998002959030087 G protein-coupled receptor 39 FUNCTION: Zn(2+) acts as a agonist. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated mainly through G(q)-alpha and G(12)/G(13) proteins. Involved in regulation of body weight, gastrointestinal mobility, hormone secretion and cell death (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in many tissues, including the stomach, intestine and hypothalamus. {ECO:0000269|PubMed:9441746}.; ovary;parathyroid;vein;skin;retina;uterus;optic nerve;whole body;endometrium;bone;iris;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;adrenal cortex;lens;pancreas;lung;placenta;hippocampus;visual apparatus;kidney;mammary gland;stomach; superior cervical ganglion;skeletal muscle; 0.09776 0.14424 -0.088107893 47.06298655 3269.39412 10.91569 GPR42 0.659177796443367 0.317047573564271 0.0237746299923619 G protein-coupled receptor 42 (gene/pseudogene) FUNCTION: Probable G protein-coupled receptor that may be activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that may play a role in the regulation of whole-body energy homeostasis and/or in intestinal immunity. {ECO:0000269|PubMed:19630535}.; . . . . 0.05833 0.09432 . . 638.82366 5.08350 GPR45 0.864764500756331 0.133285073728977 0.00195042551469267 G protein-coupled receptor 45 FUNCTION: Orphan receptor. May play a role in brain function.; . TISSUE SPECIFICITY: Expressed in brain; detected in the basal forebrain, frontal cortex, and caudate, but not in thalamus, hippocampus, or putamen.; unclassifiable (Anatomical System);lung; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.07961 0.11474 -0.26993514 34.59542345 739.53882 5.39968 GPR50 0.445210115354658 0.525810593078184 0.0289792915671583 G protein-coupled receptor 50 FUNCTION: Does not bind melatonin.; . TISSUE SPECIFICITY: Hypothalamus and pituitary.; unclassifiable (Anatomical System); superior cervical ganglion;cingulate cortex;skeletal muscle; 0.08612 0.10006 -0.378346116 28.01368247 1098.54685 6.34364 GPR50-AS1 . . . GPR50 antisense RNA 1 . . . . . . . . . . . GPR52 0.0654585923633591 0.870926816906899 0.0636145907297418 G protein-coupled receptor 52 FUNCTION: Orphan receptor.; . . . . 0.42322 . -0.295622497 32.61972163 47.47437 1.33747 GPR53P . . . G protein-coupled receptor 53, pseudogene . . . . . . . . . . . GPR55 0.000388569399865933 0.396560337174937 0.603051093425196 G protein-coupled receptor 55 FUNCTION: May be involved in hyperalgesia associated with inflammatory and neuropathic pain (By similarity). Receptor for L- alpha-lysophosphatidylinositol (LPI). LPI induces Ca(2+) release from intracellular stores via the heterotrimeric G protein GNA13 and RHOA. Putative cannabinoid receptor. May play a role in bone physiology by regulating osteoclast number and function. {ECO:0000250, ECO:0000269|PubMed:19805329}.; . TISSUE SPECIFICITY: Expressed in the caudate nucleus and putamen, but not detected in the hippocampus, thalamus, pons cerebellum, frontal cortex of the brain or in the liver. Expressed in osteoclasts and osteoblasts. {ECO:0000269|PubMed:19805329, ECO:0000269|PubMed:9931487}.; . . 0.16275 . -0.003562597 53.72729417 1566.19521 7.32376 GPR61 0.801488898268086 0.197365880594203 0.00114522113771068 G protein-coupled receptor 61 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Expressed in brain; detected in frontal and temporal lobes, occipital pole, amygdala and hippocampus. Also expressed in testis. Low expression in many other tissues.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.80901 0.12077 -0.471992905 23.03609342 24.64009 0.80926 GPR62 0.229621630878426 0.646391570601315 0.123986798520258 G protein-coupled receptor 62 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Expressed in brain; detected in the basal forebrain, frontal cortex, caudate, putamen, thalamus and hippocampus.; ovary;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;oesophagus;bone;pituitary gland;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;lens;skeletal muscle;lung;placenta;macula lutea;hippocampus;visual apparatus;kidney;stomach; . 0.39796 . . . 469.7716 4.48590 GPR63 0.646359079516381 0.347455962334308 0.00618495814931009 G protein-coupled receptor 63 FUNCTION: Orphan receptor. May play a role in brain function.; . TISSUE SPECIFICITY: Expressed in brain; detected in the frontal cortex, with lower levels in the thalamus, caudate, hypothalamus and midbrain.; unclassifiable (Anatomical System);frontal lobe;testis; ciliary ganglion; 0.45590 0.10983 -0.093566408 46.7386176 69.34097 1.72696 GPR65 0.505440551202977 0.475640986432739 0.0189184623642834 G protein-coupled receptor 65 FUNCTION: Receptor for the glycosphingolipid psychosine (PSY) and several related glycosphingolipids. May have a role in activation- induced cell death or differentiation of T-cells. {ECO:0000269|PubMed:11309421}.; . TISSUE SPECIFICITY: Predominantly expressed in thymus, spleen, lymph nodes, small intestine, lung, placenta and peripheral blood leukocytes. {ECO:0000269|PubMed:11309421, ECO:0000269|PubMed:9655242}.; unclassifiable (Anatomical System);pancreas;lung;whole body;nasopharynx;thyroid;liver;testis;colon;spleen;kidney;brain;stomach;aorta; dorsal root ganglion;superior cervical ganglion;white blood cells;atrioventricular node;whole blood; 0.17356 0.10446 -0.05129383 49.75819769 1188.28165 6.53735 GPR68 0.000219036510559383 0.300566804301724 0.699214159187716 G protein-coupled receptor 68 FUNCTION: Proton-sensing receptor involved in pH homeostasis. May represents an osteoblastic pH sensor regulating cell-mediated responses to acidosis in bone. Mediates its action by association with G proteins that stimulates inositol phosphate (IP) production or Ca(2+) mobilization. The receptor is almost silent at pH 7.8 but fully activated at pH 6.8. Function also as a metastasis suppressor gene in prostate cancer (By similarity). {ECO:0000250, ECO:0000269|PubMed:12955148}.; . TISSUE SPECIFICITY: Found at low level in a wide range of tissues, but significantly expressed in lung, kidney, bone and nervous system. {ECO:0000269|PubMed:12955148}.; unclassifiable (Anatomical System);uterus;optic nerve;macula lutea;blood;fovea centralis;choroid;lens;retina; superior cervical ganglion;uterus corpus;atrioventricular node;skeletal muscle; 0.23859 0.12020 -0.602450568 17.91106393 55.75726 1.50000 GPR75 0.00319480233774598 0.823284843900208 0.173520353762047 G protein-coupled receptor 75 FUNCTION: G protein-coupled receptor that is activated by the chemokine CCL5/RANTES. Probably coupled to heterotrimeric Gq proteins, it stimulates inositol trisphosphate production and calcium mobilization upon activation. Together with CCL5/RANTES, may play a role in neuron survival through activation of a downstream signaling pathway involving the PI3, Akt and MAP kinases. CCL5/RANTES may also regulate insulin secretion by pancreatic islet cells through activation of this receptor. {ECO:0000250|UniProtKB:Q6X632, ECO:0000303|PubMed:23979485}.; . TISSUE SPECIFICITY: Expressed at high levels in brain and spinal cord and at detectable levels in retinal pigment epithelium. In situ hybridization of adult eye sections localized transcripts only to the perivascular cells, surrounding retinal arterioles, in the ganglion cell/nerve fiber layer. Also expressed by islet cells (at protein level). {ECO:0000269|PubMed:10381362, ECO:0000269|PubMed:11466257, ECO:0000269|PubMed:23979485}.; . . 0.25312 0.10813 -0.354480518 29.42911064 211.85738 3.13875 GPR75-ASB3 0.247642059161546 0.751029752425599 0.00132818841285466 GPR75-ASB3 readthrough FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes TNFRSF1B. {ECO:0000269|PubMed:15899873}.; . . . . . . 0.132352165 63.48785091 . . GPR78 1.28260435114209e-05 0.219226647416157 0.780760526540331 G protein-coupled receptor 78 FUNCTION: Orphan receptor. Displays a significant level of constitutive activity. Its effect is mediated by G(s)-alpha protein that stimulate adenylate cyclase, resulting in an elevation of intracellular cAMP. {ECO:0000269|PubMed:17363172}.; . TISSUE SPECIFICITY: High level of expression in placenta. Expressed throughout the brain at low level. No expression detected in skeletal muscle, lung, heart, liver, pancreas, or kidney. {ECO:0000269|PubMed:17363172}.; . . 0.10686 0.11450 0.023941474 55.75607455 647.17018 5.10647 GPR79 . . . G protein-coupled receptor 79, pseudogene . . . . . . . . . . . GPR82 0.00101851085267785 0.369606317077508 0.629375172069814 G protein-coupled receptor 82 FUNCTION: Orphan receptor.; . . unclassifiable (Anatomical System);adrenal gland;thyroid;placenta;adrenal cortex;colon;parathyroid;pineal gland; . 0.31322 . 0.103030231 61.2762444 24.4195 0.80337 GPR83 0.0324677129064709 0.92656909075491 0.0409631963386192 G protein-coupled receptor 83 FUNCTION: Orphan receptor. Could be a neuropeptide Y receptor.; . TISSUE SPECIFICITY: Brain specific.; unclassifiable (Anatomical System);lung;cartilage;sympathetic chain;spinal cord;brain;cerebellum; . 0.12505 0.25074 -0.26629572 34.81953291 105.42668 2.22471 GPR84 2.72207266045491e-07 0.166314702956684 0.83368502483605 G protein-coupled receptor 84 FUNCTION: Receptor for medium-chain free fatty acid (FFA) with carbon chain lengths of C9 to C14. Capric acid (C10:0), undecanoic acid (C11:0) and lauric acid (C12:0) are the most potent agonists. Not activated by short-chain and long-chain saturated and unsaturated FFAs. Activation by medium-chain free fatty acid is coupled to a pertussis toxin sensitive G(i/o) protein pathway. May have important roles in processes from fatty acid metabolism to regulation of the immune system. {ECO:0000269|PubMed:16966319}.; . TISSUE SPECIFICITY: Expressed predominantly in hematopoietic tissues. High levels detected in the bone marrow and lower levels in the peripheral leukocytes and lung. Also expressed in brain, heart, muscle, colon, thymus, spleen, kidney, liver, placenta and intestine. Within the leukocyte population expression is higher in neutrophils and eosinophils relative to T- or B-lymphocytes. {ECO:0000269|PubMed:11273702, ECO:0000269|PubMed:11404393, ECO:0000269|PubMed:16966319}.; unclassifiable (Anatomical System);optic nerve;lung;macula lutea;colon;blood;fovea centralis;choroid;lens;brain;retina;bone marrow; . 0.09441 0.08635 0.086440867 60.47416844 175.47159 2.88122 GPR85 0.810447100376797 0.18480703406084 0.00474586556236315 G protein-coupled receptor 85 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Highly expressed in brain and testis. Lower levels in small intestine, placenta and spleen. In brain regions, detected in all regions tested, but somewhat lower levels in the corpus callosum, medulla and spinal cord. {ECO:0000269|PubMed:10833454, ECO:0000269|PubMed:10978537}.; unclassifiable (Anatomical System);lung;whole body;bone;testis;colon;brain; superior cervical ganglion;skeletal muscle; 0.26443 0.44692 -0.207437529 38.2814343 10.71236 0.38811 GPR87 0.290536848999693 0.688587593792448 0.0208755572078588 G protein-coupled receptor 87 FUNCTION: Receptor for lysophosphatidic acid (LPA). Necessary for p53/TP53-dependent survival in response to DNA damage. {ECO:0000269|PubMed:17905198, ECO:0000269|PubMed:19602589}.; . TISSUE SPECIFICITY: Expressed in placenta and prostate. Weaker expression in thymus. Not expressed in thalamus, hippocampus, pons or cerebellum. Overexpressed in squamous cell carcinoma of the lung. {ECO:0000269|PubMed:17905198}.; unclassifiable (Anatomical System);prostate;pancreas;optic nerve;lung;heart;adrenal gland;nasopharynx;testis;spleen;bladder;skin; superior cervical ganglion;appendix;atrioventricular node; 0.22830 0.11116 0.350995466 74.37485256 52.35596 1.43030 GPR88 0.754055177236605 0.236360293245059 0.00958452951833583 G protein-coupled receptor 88 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Expressed almost exclusively in striatum. {ECO:0000269|PubMed:11056049}.; myocardium;ovary;salivary gland;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;amnion;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; amygdala;medulla oblongata;pons;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.85046 0.11105 . . 1969.98687 8.18130 GPR89A 0.847988631121754 0.151898437627327 0.000112931250919031 G protein-coupled receptor 89A FUNCTION: Voltage dependent anion channel required for acidification and functions of the Golgi apparatus that may function in counter-ion conductance. {ECO:0000250, ECO:0000269|PubMed:12761501, ECO:0000269|PubMed:18794847}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:18794847}.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;cochlea;endometrium;larynx;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;lens;pancreas;lung;adrenal gland;placenta;liver;spleen;head and neck;kidney;stomach; . . . . . 24.14895 0.79297 GPR89B 0.791699861953137 0.206991183179123 0.00130895486773982 G protein-coupled receptor 89B FUNCTION: Voltage dependent anion channel required for acidification and functions of the Golgi apparatus that may function in counter-ion conductance. {ECO:0000250, ECO:0000269|PubMed:18794847}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:18794847}.; . . 0.21111 . . . 43.35196 1.25220 GPR89P . . . G protein-coupled receptor 89 pseudogene . . . . . . . . . . . GPR101 0.403512441739383 0.557928230883097 0.03855932737752 G protein-coupled receptor 101 FUNCTION: Orphan receptor.; DISEASE: Pituitary adenoma, growth hormone-secreting, 2 (PAGH2) [MIM:300943]: A growth hormone-secreting, benign neoplasm of the anterior pituitary gland, also known as somatotropinoma. It clinically results in acromegaly, a condition characterized by coarse facial features, protruding jaw, and enlarged extremities. Excessive production of growth hormone in children or adolescents before the closure of epiphyses causes gigantism, a condition characterized by abnormally tall stature. {ECO:0000269|PubMed:25470569}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.27350 0.09927 0.663285274 84.55414013 3489.39734 11.37510 GPR107 0.839149575740717 0.160845028263222 5.39599606151261e-06 G protein-coupled receptor 107 FUNCTION: Involved in Golgi-to-ER retrograde transport. Functions as a host factor required for infection by Pseudomonas aeruginosa exotoxin A and Campylobacter jejuni CDT toxins. {ECO:0000269|PubMed:25031321}.; . . unclassifiable (Anatomical System);colon;blood;skin;bone marrow;breast;uterus;whole body;lung;larynx;bone;thyroid;placenta;visual apparatus;liver;amniotic fluid;cervix;head and neck;spleen;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;thalamus;occipital lobe;hypothalamus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cingulate cortex; 0.07500 0.08557 -0.44448505 24.46331682 153.55593 2.71005 GPR108 1.69455789377898e-08 0.840489879220035 0.159510103834386 G protein-coupled receptor 108 . . . ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;urinary;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach; ciliary ganglion; 0.14980 0.10366 0.268267497 70.64166077 318.67096 3.79102 GPR119 0.0972559050997455 0.77058774718485 0.132156347715405 G protein-coupled receptor 119 FUNCTION: Receptor for the endogenous fatty-acid ethanolamide oleoylethanolamide (OEA) and lysophosphatidylcholine (LPC). Functions as a glucose-dependent insulinotropic receptor. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Seems to act through a G(s) mediated pathway. {ECO:0000269|PubMed:16517404}.; . TISSUE SPECIFICITY: Predominantly expressed in the pancreas, especially in the islets. {ECO:0000269|PubMed:15607732}.; unclassifiable (Anatomical System);islets of Langerhans; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.47443 0.11062 0.260991686 70.25831564 18.65114 0.64441 GPR132 0.0347124102896783 0.826190614482098 0.139096975228223 G protein-coupled receptor 132 FUNCTION: May be a receptor for oxidized free fatty acids derived from linoleic and arachidonic acids such as 9- hydroxyoctadecadienoic acid (9-HODE). Activates a G alpha protein, most likely G alpha(q). May be involved in apoptosis. Functions at the G2/M checkpoint to delay mitosis. May function as a sensor that monitors the oxidative states and mediates appropriate cellular responses such as secretion of paracrine signals and attenuation of proliferation. May mediate ths accumulation of intracellular inositol phosphates at acidic pH through proton- sensing activity. {ECO:0000269|PubMed:12586833, ECO:0000269|PubMed:19855098, ECO:0000269|PubMed:9770487}.; . TISSUE SPECIFICITY: Highly expressed in macrophages and hematopoietic tissues rich in lymphocytes, like spleen and thymus. Weakly expressed in heart and lung. In atherosclerotic plaques, expression is observed around the lipid core and at the shoulder region. {ECO:0000269|PubMed:12482833}.; unclassifiable (Anatomical System);uterus;lung;heart;colon;blood;skin;bone marrow; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12048 0.23810 -0.666770504 15.86459071 22.46387 0.75291 GPR135 0.00393204052879483 0.644923881038713 0.351144078432493 G protein-coupled receptor 135 FUNCTION: Orphan receptor.; . . . . 0.05073 . . . 520.54112 4.65898 GPR137 0.484398269659545 0.514604315712261 0.00099741462819381 G protein-coupled receptor 137 . . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;adrenal cortex;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis;ciliary ganglion;caudate nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21956 0.10323 -0.424258538 25.56027365 102.5892 2.19001 GPR137B 0.000253029828140192 0.926638513760741 0.073108456411119 G protein-coupled receptor 137B . . TISSUE SPECIFICITY: Expressed in kidney, heart, brain and placenta. {ECO:0000269|PubMed:9521871}.; . . 0.31949 0.11644 -0.404032746 26.53338051 44.24582 1.26823 GPR137C 0.695444477253459 0.303743533305157 0.000811989441384611 G protein-coupled receptor 137C . . . unclassifiable (Anatomical System);amygdala;lymph node;lung;ovary;cochlea;hypothalamus;kidney;brain; . 0.18845 . -0.315847836 31.68789809 2850.01654 10.09383 GPR139 0.144423629277907 0.778727153434761 0.0768492172873319 G protein-coupled receptor 139 FUNCTION: Orphan receptor. Seems to act through a G(q/11)-mediated pathway.; . TISSUE SPECIFICITY: Expressed almost exclusively in the brain. Detected at very low levels in the peripheral tissues. {ECO:0000269|PubMed:15845401}.; . . 0.27849 0.13588 -0.293801652 32.93819297 48.82937 1.36323 GPR141 1.53229743185974e-05 0.131960568104646 0.868024108921036 G protein-coupled receptor 141 FUNCTION: Orphan receptor.; . . unclassifiable (Anatomical System);nasopharynx; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13720 0.08690 -0.53631094 20.53550366 36.95374 1.10597 GPR142 5.59549133508041e-05 0.689421966639887 0.310522078446762 G protein-coupled receptor 142 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Exclusively expressed in the central nervous system, most abundantly in the ventrolateral region of caudate putamen, the habenular nucleus, the zona incerta, and the medial mammillary nucleus. {ECO:0000269|PubMed:15845401}.; . . . . -0.214928658 37.7388535 583.16278 4.89646 GPR143 0.672222023530739 0.32288811803786 0.00488985843140061 G protein-coupled receptor 143 FUNCTION: Receptor for tyrosine, L-DOPA and dopamine. After binding to L-DOPA, stimulates Ca(2+) influx into the cytoplasm, increases secretion of the neurotrophic factor SERPINF1 and relocalizes beta arrestin at the plasma membrane; this ligand- dependent signaling occurs through a G(q)-mediated pathway in melanocytic cells. Its activity is mediated by G proteins which activate the phosphoinositide signaling pathway. Plays also a role as an intracellular G protein-coupled receptor involved in melanosome biogenesis, organization and transport. {ECO:0000269|PubMed:10471510, ECO:0000269|PubMed:16524428, ECO:0000269|PubMed:18697795, ECO:0000269|PubMed:18828673, ECO:0000269|PubMed:19717472}.; DISEASE: Albinism ocular 1 (OA1) [MIM:300500]: Form of albinism affecting only the eye. Pigment of the hair and skin is normal or only slightly diluted. Eyes may be severely affected with photophobia and reduced visual acuity. Nystagmus or strabismus are often associated. The irides and fundus are depigmented. {ECO:0000269|PubMed:11214907, ECO:0000269|PubMed:16646960, ECO:0000269|PubMed:17822861, ECO:0000269|PubMed:17960122, ECO:0000269|PubMed:18978956, ECO:0000269|PubMed:8634705, ECO:0000269|PubMed:9529334, ECO:0000269|PubMed:9887374}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Nystagmus congenital X-linked 6 (NYS6) [MIM:300814]: A condition defined as conjugated, spontaneous and involuntary ocular oscillations that appear at birth or during the first three months of life. Other associated features may include mildly decreased visual acuity, strabismus, astigmatism, and occasionally head nodding. {ECO:0000269|PubMed:17516023}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at high levels in the retina, including the retinal pigment epithelium (RPE), and in melanocytes. Weak expression is observed in brain and adrenal gland. {ECO:0000269|PubMed:18828673, ECO:0000269|PubMed:7647783}.; . . 0.10363 0.22673 0.018483465 55.44939844 49.01054 1.36779 GPR143P . . . G protein-coupled receptor 143 pseudogene . . . . . . . . . . . GPR146 0.00279412642316597 0.570960083416592 0.426245790160242 G protein-coupled receptor 146 FUNCTION: Orphan receptor.; . . unclassifiable (Anatomical System);meninges;ovary;parathyroid;skin;skeletal muscle;retina;uterus;pancreas;prostate;optic nerve;pia mater;lung;endometrium;bone;placenta;liver;testis;spleen;dura mater;kidney;brain; . 0.15219 0.11370 -0.064242613 48.844067 159.85173 2.76007 GPR148 0.00480951704813308 0.687707115599248 0.307483367352619 G protein-coupled receptor 148 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Expression restricted to nervous system and testis. Is also detected in several tumors types, most notably prostate cancer. {ECO:0000269|PubMed:15688318}.; . . 0.07493 0.14930 1.019682101 90.97664544 440.82205 4.37383 GPR149 2.6464400182055e-05 0.763728348073471 0.236245187526347 G protein-coupled receptor 149 FUNCTION: Orphan receptor.; . . . . 0.15312 0.09679 -0.554717505 19.79830149 121.73084 2.40326 GPR150 0.00224716234978038 0.524286126316422 0.473466711333798 G protein-coupled receptor 150 FUNCTION: Orphan receptor.; . . . . 0.27177 0.10161 . . 263.35907 3.48176 GPR151 1.05612992862494e-05 0.349525992478378 0.650463446222335 G protein-coupled receptor 151 FUNCTION: Orphan receptor.; . . . . 0.22570 0.09843 0.464864541 78.69190847 707.11601 5.28196 GPR152 1.00978862123821e-05 0.342011538841809 0.657978363271978 G protein-coupled receptor 152 FUNCTION: Orphan receptor.; . . lung;liver;spleen; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.09859 0.09818 0.536463361 81.06864827 424.39381 4.30448 GPR153 0.000377954117161823 0.621011134065295 0.378610911817544 G protein-coupled receptor 153 FUNCTION: Orphan receptor.; . . . . 0.19561 0.11293 . . 700.3385 5.26401 GPR155 8.12952100257327e-11 0.670522098632914 0.329477901285791 G protein-coupled receptor 155 . . . unclassifiable (Anatomical System);ovary;cartilage;sympathetic chain;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;lung;frontal lobe;larynx;thyroid;bone;macula lutea;visual apparatus;duodenum;liver;pituitary gland;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11958 0.08323 -0.997481928 8.47487615 90.25481 2.04431 GPR156 3.67917855529623e-07 0.796552693098485 0.20344693898366 G protein-coupled receptor 156 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Ubiquitous expression both in the CNS and in peripheral tissues. Very high expression in fetal brain and testis relative to expression in other tissues. {ECO:0000269|PubMed:12591167}.; unclassifiable (Anatomical System);testis; testis;cerebellum; 0.05667 0.07670 1.403615907 94.76291578 382.75192 4.12458 GPR157 2.63491769393547e-05 0.317175264895151 0.682798385927909 G protein-coupled receptor 157 FUNCTION: Orphan receptor.; . . . . 0.10208 0.10380 -0.268115223 34.70747818 2122.36684 8.48061 GPR158 0.678504824963118 0.321495108729682 6.63072000476043e-08 G protein-coupled receptor 158 FUNCTION: Orphan receptor.; . . . . 0.20324 0.10856 -0.411532969 25.8492569 5259.95266 14.97534 GPR158-AS1 . . . GPR158 antisense RNA 1 . . . . . . . . . . . GPR160 0.00375671992599514 0.635096406550431 0.361146873523574 G protein-coupled receptor 160 FUNCTION: Orphan receptor.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;small intestine;lens;skeletal muscle;bile duct;breast;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;stomach; . 0.32439 0.08271 0.371224249 75.12384996 84.75876 1.96120 GPR161 0.0295792897121091 0.960088859455923 0.0103318508319677 G protein-coupled receptor 161 FUNCTION: Key negative regulator of Shh signaling, which promotes the processing of GLI3 into GLI3R during neural tube development. Recruited by TULP3 and the IFT-A complex to primary cilia and acts as a regulator of the PKA-dependent basal repression machinery in Shh signaling by increasing cAMP levels, leading to promote the PKA-dependent processing of GLI3 into GLI3R and repress the Shh signaling. In presence of SHH, it is removed from primary cilia and is internalized into recycling endosomes, preventing its activity and allowing activation of the Shh signaling. Its ligand is unknown (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;frontal lobe;endometrium;bone;placenta;macula lutea;spleen;brain;mammary gland; uterus;dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.15614 0.15387 -0.800872469 12.33191791 94.16225 2.08754 GPR162 0.0171343880053493 0.960229807583519 0.0226358044111321 G protein-coupled receptor 162 FUNCTION: Orphan receptor.; . . unclassifiable (Anatomical System);heart;cartilage;nervous;hypothalamus;fovea centralis;lens;skeletal muscle;skin;retina;uterus;lung;bone;macula lutea;visual apparatus;hippocampus;testis;pineal gland;brain;cerebellum; whole brain;occipital lobe;superior cervical ganglion;subthalamic nucleus;cerebellum peduncles;temporal lobe;prefrontal cortex;globus pallidus;ciliary ganglion;pons;cingulate cortex;cerebellum; . . -0.971800989 8.946685539 802.1892 5.58047 GPR165P . . . G protein-coupled receptor 165 pseudogene . . . . . . . . . . . GPR166P . . . G protein-coupled receptor 166 pseudogene . . . . . . . . . . . GPR171 0.00167512127492569 0.701463475704847 0.296861403020227 G protein-coupled receptor 171 FUNCTION: Orphan receptor.; . . unclassifiable (Anatomical System);pancreas;endometrium;nasopharynx;liver;spleen;head and neck; . 0.26218 . -0.205617011 38.57631517 272.28231 3.53656 GPR173 0.678239841602563 0.301559943833062 0.020200214564375 G protein-coupled receptor 173 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Expressed at high levels in brain and ovary. Lower levels in small intestine. In brain regions, detected in all regions tested. Highest levels in the cerebellum and cerebral cortex.; unclassifiable (Anatomical System);lung;hypothalamus;visual apparatus;brain;cerebellum; superior cervical ganglion;heart;trigeminal ganglion; 0.18443 0.11809 -0.494039303 22.09247464 11.95575 0.43351 GPR174 0.888101966399909 0.110703637362607 0.00119439623748407 G protein-coupled receptor 174 FUNCTION: Putative receptor for purines coupled to G-proteins. {ECO:0000250}.; . . lymph node;germinal center; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13960 . 0.371224249 75.12384996 15.20516 0.54712 GPR176 0.413262635237383 0.578502794623624 0.00823457013899334 G protein-coupled receptor 176 FUNCTION: Orphan receptor.; . . unclassifiable (Anatomical System);pancreas;bone;visual apparatus;cervix;kidney;brain;cerebellum; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.07701 0.19824 -0.712684326 14.49634348 52.6543 1.43741 GPR179 2.67654454919677e-20 0.313048070465942 0.686951929534058 G protein-coupled receptor 179 FUNCTION: Orphan receptor, involved in vision. Required for signal transduction through retinal depolarizing bipolar cells. {ECO:0000269|PubMed:22325362}.; . TISSUE SPECIFICITY: Expressed in the retina. {ECO:0000269|PubMed:22325361}.; unclassifiable (Anatomical System);brain;retina; . 0.08115 0.08448 2.769596314 99.00330267 2584.33645 9.50880 GPR180 6.5915409717463e-11 0.0346741423171868 0.965325857616898 G protein-coupled receptor 180 . . . . . 0.16696 0.19106 -0.005381972 53.50908233 105.61338 2.22730 GPR182 0.000859696118417304 0.557344581505817 0.441795722375765 G protein-coupled receptor 182 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, immune system, adrenal gland and liver. {ECO:0000269|PubMed:9367907}.; unclassifiable (Anatomical System);medulla oblongata;pancreas;lung;testis;colon;kidney;stomach; . 0.11085 0.28827 -0.268115223 34.70747818 271.96548 3.53355 GPR183 0.0255456321889338 0.784197295075932 0.190257072735134 G protein-coupled receptor 183 FUNCTION: Receptor for oxysterol 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) and other related oxysterols. Binding of 7- alpha,25-OHC mediates the correct localization of B-cells during humoral immune responses. Promotes activated B-cell localization in the outer follicle and interfollicular regions. Its specific expression during B-cell maturation helps position B-cells appropriately for mounting T-dependent antibody responses (By similarity). Signals constitutively through G(i)-alpha, but not through G(s)-alpha or G(q)-alpha. Signals constitutively also via MAPK1/3 (ERK1/2). {ECO:0000250, ECO:0000269|PubMed:16540462, ECO:0000269|PubMed:21673108}.; . TISSUE SPECIFICITY: Expressed abundantly in lymphoid tissues such as spleen and lymph node, and in B- and T-lymphocytes. Also highly expressed in lung, heart and gastrointestinal tract, and weakly expressed in the urogenital system and brain. {ECO:0000269|PubMed:16540462, ECO:0000269|PubMed:8383238}.; . . 0.12099 0.11502 0.060756528 58.52795471 37.4109 1.11428 GPRASP1 0.501518109194796 0.498304365956169 0.00017752484903525 G protein-coupled receptor associated sorting protein 1 FUNCTION: Modulates lysosomal sorting and functional down- regulation of a variety of G-protein coupled receptors. Targets receptors for degradation in lysosomes via its interaction with BECN2. {ECO:0000269|PubMed:12142540, ECO:0000269|PubMed:15452121, ECO:0000269|PubMed:23954414}.; . TISSUE SPECIFICITY: Expressed in the brain, with lower expression in medulla, spinal cord and substantia nigra. {ECO:0000269|PubMed:12142540, ECO:0000269|PubMed:15086532}.; fovea centralis;choroid;bone marrow;retina;uterus;prostate;optic nerve;frontal lobe;thyroid;pituitary gland;iris;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;lung;adrenal gland;trabecular meshwork;macula lutea;liver;cervix;spleen;kidney;peripheral nerve;cerebellum; amygdala;medulla oblongata;subthalamic nucleus;occipital lobe;thalamus;hypothalamus;prefrontal cortex;globus pallidus;cingulate cortex; 0.23815 . -0.24061166 36.28214201 775.22244 5.51120 GPRASP2 0.498014765173916 0.497620134894299 0.00436509993178438 G protein-coupled receptor associated sorting protein 2 FUNCTION: May play a role in regulation of a variety of G-protein coupled receptors. {ECO:0000269|PubMed:15086532}.; . TISSUE SPECIFICITY: Expressed in the brain. {ECO:0000269|PubMed:15086532}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;head and neck;kidney; . 0.05886 0.08503 0.286674996 71.49681529 81.63519 1.91368 GPRC5A 8.02764467699413e-06 0.305454470284472 0.694537502070851 G protein-coupled receptor class C group 5 member A FUNCTION: Orphan receptor. Could be involved in modulating differentiation and maintaining homeostasis of epithelial cells. This retinoic acid-inducible GPCR provide evidence for a possible interaction between retinoid and G-protein signaling pathways. Functions as a negative modulator of EGFR signaling (By similarity). May act as a lung tumor suppressor (PubMed:18000218). {ECO:0000250|UniProtKB:Q8BHL4, ECO:0000269|PubMed:18000218}.; . TISSUE SPECIFICITY: Expressed at high level in fetal and adult lung tissues but repressed in most human lung cancers (PubMed:9857033, PubMed:18000218). Constitutively expressed in fetal kidney and adult placenta, kidney, prostate, testis, ovary, small intestine, colon, stomach, and spinal chord at low to moderate levels. Not detectable in fetal heart, brain, and liver and adult heart, brain, liver, skeletal muscle, pancreas, spleen, thymus, and peripheral leukocytes. According to PubMed:10783259, expressed at low but detectable level in pancreas and heart. {ECO:0000269|PubMed:10783259, ECO:0000269|PubMed:10945465, ECO:0000269|PubMed:18000218, ECO:0000269|PubMed:9857033}.; ovary;colon;skin;bone marrow;uterus;prostate;endometrium;bone;thyroid;iris;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;cartilage;skeletal muscle;bile duct;greater omentum;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;lung;trachea;thyroid;fetal lung;atrioventricular node;fetal thyroid; 0.11338 0.11845 -0.066061882 48.77919321 431.49031 4.33570 GPRC5B 0.527206905590426 0.469305702382432 0.00348739202714222 G protein-coupled receptor class C group 5 member B FUNCTION: Unknown. This retinoic acid-inducible G-protein coupled receptor provide evidence for a possible interaction between retinoid and G-protein signaling pathways.; . TISSUE SPECIFICITY: Expression is high in kidney, pancreas, and testis, medium in brain, heart, prostate, small intestine, and spleen, low in liver, placenta, skeletal muscle, colon, ovary, and thymus, and not detectable in lung and peripheral leukocyte. According to PubMed:10945465, highly expressed in most brain areas examined, with the highest levels observed in corpus callosum, caudate nucleus, putamen, substantia nigra, thalamus, hippocampus, and spinal chord as well as in dorsal root ganglia (DRG). In the periphery, expression levels are relatively low, compared to the CNS, with the strongest expression detected in pancreas, testis, uterus, and stomach. {ECO:0000269|PubMed:10783259, ECO:0000269|PubMed:10945465}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);amygdala;cartilage;heart;tongue;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach;aorta;thymus; whole brain;amygdala;medulla oblongata;thalamus;occipital lobe;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;testis;cingulate cortex;parietal lobe;cerebellum; 0.72847 0.13456 -0.821100135 11.88369899 145.32089 2.62509 GPRC5C 0.0055136074174967 0.896850360380922 0.0976360322015811 G protein-coupled receptor class C group 5 member C FUNCTION: This retinoic acid-inducible G-protein coupled receptor provide evidence for a possible interaction between retinoid and G-protein signaling pathways. {ECO:0000250}.; . TISSUE SPECIFICITY: Expression is highest in the periphery, particularly in the stomach, but also in the kidney, liver, pancreas, and prostate. In brain, levels of expression are generally lower than in the periphery, with the exception of cerebellum, spinal cord, and dorsal root ganglia (DRG). {ECO:0000269|PubMed:10945465, ECO:0000269|PubMed:11311935}.; ovary;colon;choroid;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;urinary;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach;cerebellum; cerebellum peduncles;thyroid;liver;kidney;cerebellum; 0.20606 0.11470 -0.992035476 8.604623732 218.77947 3.19770 GPRC5D 2.97022164147864e-05 0.55179298162175 0.448177316161835 G protein-coupled receptor class C group 5 member D . . TISSUE SPECIFICITY: Widely expressed in the peripheral system. Expression pattern is high in pancreas, medium in kidney, small intestine, spleen and testis, low in lung, colon, leukocyte, prostate and thymus and not detectable in brain, heart, liver, placenta, skeletal muscle and ovary. {ECO:0000269|PubMed:11311935}.; unclassifiable (Anatomical System);prostate;brain;bone marrow; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion; 0.11752 0.10615 0.086440867 60.47416844 107.32361 2.24738 GPRC6A 4.63567516085775e-14 0.0128785139310454 0.987121486068908 G protein-coupled receptor class C group 6 member A FUNCTION: Receptor activated by amino acids with a preference for basic amino acids such as L-Lys, L-Arg and L-ornithine but also by small and polar amino acids. The L-alpha amino acids respond is augmented by divalent cations Ca(2+) and Mg(2+). Activated by extracellular calcium and osteocalin. Seems to act through a G(q)/G(11) and G(i)-coupled pathway. Mediates the non-genomic effects of androgens in multiple tissue. May coordinates nutritional and hormonal anabolic signals through the sensing of extracellular amino acids, osteocalcin, divalents ions and its responsiveness to anabolic steroids. {ECO:0000269|PubMed:15576628, ECO:0000269|PubMed:20947496}.; . TISSUE SPECIFICITY: Isoform 1 is expressed at high level in brain, skeletal muscle, testis, bone, calvaria, osteoblasts and leukocytes. Expressed at intermediate level in liver, heart, kidney and spleen. Expressed at low level in lung, pancreas, placenta and ovary. Not detected in thymus, prostate, small intestine, tongue and colon. Isoform 1 and isoform 2 are expressed in kidney at the same level. Isoform 2 is expressed at lower level than isoform 1 in the other tissues. {ECO:0000269|PubMed:15194188}.; unclassifiable (Anatomical System);kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.10422 0.09940 1.629598519 96.0603916 5803.3068 15.79517 GPRIN1 0.787287341879441 0.21242825806323 0.000284400057328623 G protein regulated inducer of neurite outgrowth 1 FUNCTION: May be involved in neurite outgrowth. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed in the central nervous system, with highest levels in spinal cord. {ECO:0000269|PubMed:10480904}.; colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;pancreas;lung;placenta;hippocampus;visual apparatus;macula lutea;duodenum;kidney;mammary gland; . 0.09709 0.08002 0.159856957 64.91507431 2314.51425 8.90786 GPRIN2 0.00029629113351708 0.567856072743045 0.431847636123438 G protein regulated inducer of neurite outgrowth 2 FUNCTION: May be involved in neurite outgrowth. {ECO:0000269|PubMed:10480904}.; . TISSUE SPECIFICITY: Expressed specifically in the cerebellum. {ECO:0000269|PubMed:10480904}.; . . 0.10901 0.09180 1.091286379 91.89667374 5810.0309 15.81207 GPRIN3 0.000266284255273368 0.779428481455553 0.220305234289174 GPRIN family member 3 FUNCTION: May be involved in neurite outgrowth. {ECO:0000250}.; . . unclassifiable (Anatomical System);breast;lung; . 0.10468 0.07744 2.45475012 98.57867422 1050.66369 6.22566 GPS1 0.98465745647653 0.0153408523802197 1.69114325013499e-06 G protein pathway suppressor 1 FUNCTION: Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN- dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Suppresses G-protein- and mitogen-activated protein kinase-mediated signal transduction. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:9535219}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8943324}.; lymphoreticular;myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;synovium;larynx;bone;pituitary gland;testis;pineal gland;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; globus pallidus;parietal lobe; 0.24457 0.08968 -0.887242605 10.43288511 39.06599 1.15842 GPS2 0.590137501711014 0.409432075507529 0.000430422781457097 G protein pathway suppressor 2 FUNCTION: Suppresses G-protein- and mitogen-activated protein kinase-mediated signal transduction.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8943324}.; medulla oblongata;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;blood;lens;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;testis; 0.09680 0.07046 -0.494039303 22.09247464 40.43591 1.18663 GPS2P1 . . . G protein pathway suppressor 2 pseudogene 1 . . . . . . . . . . . GPS2P2 . . . G protein pathway suppressor 2 pseudogene 2 . . . . . . . . . . . GPSM1 0.00214952675934529 0.978725625665293 0.0191248475753615 G-protein signaling modulator 1 FUNCTION: Guanine nucleotide dissociation inhibitor (GDI) which functions as a receptor-independent activator of heterotrimeric G- protein signaling. Keeps G(i/o) alpha subunit in its GDP-bound form thus uncoupling heterotrimeric G-proteins signaling from G protein-coupled receptors. Controls spindle orientation and asymmetric cell fate of cerebral cortical progenitors. May also be involved in macroautophagy in intestinal cells. May play a role in drug addiction. {ECO:0000269|PubMed:11024022, ECO:0000269|PubMed:12642577}.; . TISSUE SPECIFICITY: Expressed in intestinal cells. {ECO:0000269|PubMed:12642577}.; ovary;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;whole body;synovium;larynx;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;lens;lung;placenta;visual apparatus;macula lutea;hypopharynx;liver;head and neck;spleen;kidney;mammary gland;stomach;cerebellum; . 0.17026 0.12903 -1.324592054 4.729889125 1235.6164 6.64163 GPSM2 2.9412972070079e-10 0.707324343746965 0.292675655958906 G-protein signaling modulator 2 FUNCTION: Plays an important role in mitotic spindle pole organization via its interaction with NUMA1 (PubMed:15632202, PubMed:21816348). Plays an important role in asymmetric cell divisions (PubMed:21816348). Has guanine nucleotide dissociation inhibitor (GDI) activity towards G(i) alpha proteins, such as GNAI1 and GNAI3, and thereby regulates their activity (By similarity). {ECO:0000250|UniProtKB:Q8VDU0, ECO:0000269|PubMed:15632202, ECO:0000269|PubMed:21816348}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;urinary;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; hypothalamus; 0.56526 . 0.022122107 55.69120075 906.41324 5.85974 GPSM3 0.609591627820476 0.381937072138269 0.00847130004125496 G-protein signaling modulator 3 FUNCTION: Interacts with subunit of G(i) alpha proteins and regulates the activation of G(i) alpha proteins. {ECO:0000269|PubMed:14656218, ECO:0000269|PubMed:15096500}.; . TISSUE SPECIFICITY: Expressed in heart, placenta, lung and liver. {ECO:0000269|PubMed:15096500}.; . . 0.31812 . 0.191216164 66.57230479 41.76394 1.21679 GPT 2.84324204580575e-15 0.00129558361150448 0.998704416388493 glutamic-pyruvate transaminase (alanine aminotransferase) FUNCTION: Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Liver, kidney, heart, and skeletal muscles. Expressed at moderate levels in the adipose tissue. {ECO:0000269|PubMed:11863375}.; unclassifiable (Anatomical System);pancreas;lung;testis;colon;kidney;brain;skin; superior cervical ganglion;liver;kidney;skeletal muscle; 0.13708 0.81545 0.292133603 71.59707478 2186.3535 8.61249 GPT2 0.00368564013628491 0.987306854555435 0.00900750530827968 glutamic pyruvate transaminase (alanine aminotransferase) 2 FUNCTION: Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. {ECO:0000269|PubMed:11863375}.; . TISSUE SPECIFICITY: Expressed at high levels in muscle, adipose tissue, kidney and brain and at lower levels in the liver and breast. {ECO:0000269|PubMed:11863375}.; myocardium;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;gum;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.18767 0.75735 -0.426079032 25.36565228 46.30617 1.31126 GPX1 0.00693165111693131 0.525707784386783 0.467360564496286 glutathione peroxidase 1 FUNCTION: Protects the hemoglobin in erythrocytes from oxidative breakdown.; . . . . 0.33604 . 0.237127192 68.98443029 1198.35095 6.56847 GPX1P1 . . . glutathione peroxidase pseudogene 1 . . . . . 0.33604 . . . . . GPX1P2 . . . glutathione peroxidase pseudogene 2 . . . . . . . . . . . GPX2 0.00231703379463956 0.530782848750632 0.466900117454728 glutathione peroxidase 2 FUNCTION: Could play a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. Tert-butyl hydroperoxide, cumene hydroperoxide and linoleic acid hydroperoxide but not phosphatidycholine hydroperoxide, can act as acceptors.; . TISSUE SPECIFICITY: Mostly in liver and gastrointestinal tract, not found in heart or kidney.; . . 0.21400 . 0.43736446 77.56546355 120.19686 2.38900 GPX3 0.0155826368713898 0.880590374554031 0.103826988574579 glutathione peroxidase 3 FUNCTION: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione.; . TISSUE SPECIFICITY: Secreted in plasma.; . . 0.37997 . -0.427900189 25.14744043 11.94387 0.43327 GPX4 0.0173298887825943 0.890958813947099 0.091711297270307 glutathione peroxidase 4 FUNCTION: Protects cells against membrane lipid peroxidation and cell death. Required for normal sperm development and male fertility. Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage. {ECO:0000250|UniProtKB:O70325}.; . TISSUE SPECIFICITY: Present primarily in testis.; myocardium;medulla oblongata;ovary;sympathetic chain;skin;retina;prostate;optic nerve;endometrium;germinal center;bladder;brain;tonsil;cartilage;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus;cerebellum; testis - interstitial;testis - seminiferous tubule;liver;testis; 0.14175 . -0.117432389 44.89266336 . . GPX5 0.00888467745572368 0.80447170699167 0.186643615552606 glutathione peroxidase 5 FUNCTION: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids.; . TISSUE SPECIFICITY: Epididymis.; . . 0.12640 0.19448 0.926041233 89.65557915 126.88311 2.45610 GPX6 3.13757952195529e-05 0.345495692978221 0.654472931226559 glutathione peroxidase 6 . . TISSUE SPECIFICITY: Expressed in olfactory epithelium and embryos. {ECO:0000269|PubMed:12775843}.; . . 0.05631 . 1.771210783 96.79169615 596.27463 4.94195 GPX7 0.000179755480234412 0.700841963972439 0.298978280547327 glutathione peroxidase 7 FUNCTION: It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks. {ECO:0000269|PubMed:22157330}.; . TISSUE SPECIFICITY: Expressed in esophageal epithelial cells; expression is up-regulated after exposure to acidic bile acids. {ECO:0000269|PubMed:22157330}.; ovary;parathyroid;skin;bone marrow;uterus;whole body;endometrium;synovium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;heart;cartilage;tongue;blood;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;trigeminal ganglion; 0.13313 0.19112 -0.05129383 49.75819769 55.37298 1.49311 GPX8 0.0190662288898625 0.734248254529008 0.24668551658113 glutathione peroxidase 8 (putative) . . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;cochlea;larynx;thyroid;bone;testis;dura mater;brain;unclassifiable (Anatomical System);heart;cartilage;lens;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; smooth muscle;adipose tissue;heart;ciliary ganglion;atrioventricular node; . 0.10503 -0.007201372 53.19061099 3.57258 0.12960 GRAMD1A 0.568380698661449 0.431615021677215 4.27966133611184e-06 GRAM domain containing 1A . . . myocardium;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;bone;thyroid;germinal center;brain;pineal gland;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;liver;spleen;head and neck;cervix;kidney;stomach;peripheral nerve; . 0.11858 0.11551 -1.017713296 8.103326256 1134.30997 6.42672 GRAMD1B 0.984850768297199 0.0151491645693425 6.71334580466348e-08 GRAM domain containing 1B . . . amygdala;ovary;colon;skin;bile duct;uterus;frontal lobe;cerebral cortex;placenta;thyroid;bone;visual apparatus;hippocampus;hypopharynx;head and neck;cervix;kidney;brain;mammary gland;cerebellum; . 0.39325 . -0.466531444 23.51380042 88.61285 2.01949 GRAMD1C 8.13050191922526e-10 0.970293694543742 0.0297063046432078 GRAM domain containing 1C . . . unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;skin;uterus;lung;endometrium;placenta;visual apparatus;hippocampus;liver;testis;cervix;germinal center;kidney;brain;gall bladder; amygdala;superior cervical ganglion;prefrontal cortex;testis;appendix;ciliary ganglion; 0.10537 . 0.134171522 63.57041755 129.86305 2.48277 GRAMD2 2.95954761695704e-08 0.299545467785445 0.700454502619079 GRAM domain containing 2 . . . heart;ovary;fovea centralis;skin;uterus;lung;endometrium;placenta;thyroid;macula lutea;liver;testis;head and neck;spleen;kidney;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.04746 . 0.350995466 74.37485256 103.31631 2.19553 GRAMD3 1.53546581217794e-07 0.6170140083997 0.382985838053718 GRAM domain containing 3 . . . smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;dura mater;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);meninges;cartilage;heart;tongue;islets of Langerhans;hypothalamus;skeletal muscle;bile duct;breast;pancreas;pia mater;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; amygdala;placenta;spinal cord;prefrontal cortex;globus pallidus; 0.11843 0.09781 -0.047654689 50.22410946 152.70618 2.70301 GRAMD4 0.999791413435688 0.000208586517318381 4.699378800934e-11 GRAM domain containing 4 FUNCTION: Plays a role as a mediator of E2F1-induced apoptosis in the absence of p53/TP53. {ECO:0000269|PubMed:15565177}.; . TISSUE SPECIFICITY: Expressed in lung and in primary lung squamous cell carcinoma (LSCC). {ECO:0000269|PubMed:18302964}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;adrenal cortex;ciliary ganglion; 0.11928 0.11475 -1.065444789 7.425100259 21.90891 0.73656 GRAMD4P1 . . . GRAM domain containing 4 pseudogene 1 . . . . . . . . . . . GRAMD4P2 . . . GRAM domain containing 4 pseudogene 2 . . . . . . . . . . . GRAMD4P3 . . . GRAM domain containing 4 pseudogene 3 . . . . . . . . . . . GRAMD4P4 . . . GRAM domain containing 4 pseudogene 4 . . . . . . . . . . . GRAMD4P5 . . . GRAM domain containing 4 pseudogene 5 . . . . . . . . . . . GRAMD4P6 . . . GRAM domain containing 4 pseudogene 6 . . . . . . . . . . . GRAMD4P7 . . . GRAM domain containing 4 pseudogene 7 . . . . . . . . . . . GRAMD4P8 . . . GRAM domain containing 4 pseudogene 8 . . . . . . . . . . . GRAP 0.21706363500994 0.64780477309064 0.13513159189942 GRB2-related adaptor protein FUNCTION: Couples signals from receptor and cytoplasmic tyrosine kinases to the Ras signaling pathway.; . . unclassifiable (Anatomical System);lymphoreticular;lymph node;heart;retina;pancreas;lung;endometrium;placenta;liver;testis;spleen;germinal center;kidney;brain;mammary gland;tonsil;thymus; ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.52773 0.14689 . . 12.18996 0.44137 GRAP2 0.101871595396695 0.896646827113422 0.00148157748988278 GRB2-related adaptor protein 2 FUNCTION: Interacts with SLP-76 to regulate NF-AT activation. Binds to tyrosine-phosphorylated shc.; . . unclassifiable (Anatomical System);lung;nasopharynx;placenta;liver;testis;spleen;thymus; pons;trigeminal ganglion;skeletal muscle;thymus; 0.87215 0.37468 0.283038099 71.26680821 81.93324 1.91955 GRAPL . . . GRB2-related adaptor protein-like . . . . . . . . . . . GRASP 0.930936502160189 0.0689921076058431 7.13902339682528e-05 GRP1 (general receptor for phosphoinositides 1)-associated scaffold protein FUNCTION: Plays a role in intracellular trafficking and contributes to the macromolecular organization of group 1 metabotropic glutamate receptors (mGluRs) at synapses. {ECO:0000250}.; . . unclassifiable (Anatomical System);smooth muscle;cartilage;heart;ovary;tongue;islets of Langerhans;sympathetic chain;colon;fovea centralis;choroid;lens;skin;retina;prostate;optic nerve;lung;frontal lobe;cerebral cortex;larynx;macula lutea;testis;head and neck;spleen;brain;stomach; . 0.64717 0.15222 . . 95.16207 2.10482 GRASPOS . . . GRP1-associated scaffold protein opposite strand . . . . . . . . . . . GRB2 0.549680745843086 0.447395824250563 0.00292342990635075 growth factor receptor bound protein 2 FUNCTION: Adapter protein that provides a critical link between cell surface growth factor receptors and the Ras signaling pathway.; . . ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;choroid;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;internal ear;placenta;hippocampus;duodenum;kidney;stomach; dorsal root ganglion;superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe; 0.99989 0.90497 -0.119252484 44.53880632 1.21964 0.04105 GRB7 0.000820005745088645 0.995920604563532 0.00325938969137882 growth factor receptor bound protein 7 FUNCTION: Adapter protein that interacts with the cytoplasmic domain of numerous receptor kinases and modulates down-stream signaling. Promotes activation of down-stream protein kinases, including STAT3, AKT1, MAPK1 and/or MAPK3. Promotes activation of HRAS. Plays a role in signal transduction in response to EGF. Plays a role in the regulation of cell proliferation and cell migration. Plays a role in the assembly and stability of RNA stress granules. Binds to the 5'UTR of target mRNA molecules and represses translation of target mRNA species, when not phosphorylated. Phosphorylation impairs RNA binding and promotes stress granule disassembly during recovery after cellular stress (By similarity). {ECO:0000250, ECO:0000269|PubMed:10893408, ECO:0000269|PubMed:12021278, ECO:0000269|PubMed:12223469, ECO:0000269|PubMed:20622016}.; . . ovary;colon;parathyroid;choroid;uterus;endometrium;larynx;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;oral cavity;urinary;blood;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.70460 0.27733 0.07167258 59.15899976 281.56375 3.59409 GRB10 0.367423738728048 0.632555946481429 2.03147905230319e-05 growth factor receptor bound protein 10 FUNCTION: Adapter protein which modulates coupling of a number of cell surface receptor kinases with specific signaling pathways. Binds to, and suppress signals from, activated receptors tyrosine kinases, including the insulin (INSR) and insulin-like growth factor (IGF1R) receptors. The inhibitory effect can be achieved by 2 mechanisms: interference with the signaling pathway and increased receptor degradation. Delays and reduces AKT1 phosphorylation in response to insulin stimulation. Blocks association between INSR and IRS1 and IRS2 and prevents insulin- stimulated IRS1 and IRS2 tyrosine phosphorylation. Recruits NEDD4 to IGF1R, leading to IGF1R ubiquitination, increased internalization and degradation by both the proteasomal and lysosomal pathways. May play a role in mediating insulin- stimulated ubiquitination of INSR, leading to proteasomal degradation. Negatively regulates Wnt signaling by interacting with LRP6 intracellular portion and interfering with the binding of AXIN1 to LRP6. Positive regulator of the KDR/VEGFR-2 signaling pathway. May inhibit NEDD4-mediated degradation of KDR/VEGFR-2. {ECO:0000269|PubMed:12493740, ECO:0000269|PubMed:15060076, ECO:0000269|PubMed:16434550, ECO:0000269|PubMed:17376403}.; . TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues, including fetal and postnatal liver, lung, kidney, skeletal muscle, heart, spleen, skin and brain. {ECO:0000269|PubMed:11527390}.; ovary;salivary gland;intestine;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;spinal cord;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;stomach;aorta;peripheral nerve; superior cervical ganglion;medulla oblongata;testis - interstitial;trigeminal ganglion;skeletal muscle; 0.41987 0.67373 -0.134019284 43.90776126 129.04538 2.47569 GRB14 0.0966012167550771 0.903069559204665 0.000329224040257746 growth factor receptor bound protein 14 FUNCTION: Adapter protein which modulates coupling of cell surface receptor kinases with specific signaling pathways. Binds to, and suppresses signals from, the activated insulin receptor (INSR). Potent inhibitor of insulin-stimulated MAPK3 phosphorylation. Plays a critical role regulating PDPK1 membrane translocation in response to insulin stimulation and serves as an adapter protein to recruit PDPK1 to activated insulin receptor, thus promoting PKB/AKT1 phosphorylation and transduction of the insulin signal. {ECO:0000269|PubMed:15210700, ECO:0000269|PubMed:19648926}.; . TISSUE SPECIFICITY: Expressed at high levels in the liver, kidney, pancreas, testis, ovary, heart and skeletal muscle.; unclassifiable (Anatomical System);ovary;islets of Langerhans;parathyroid;fovea centralis;skin;whole body;lung;endometrium;placenta;macula lutea;liver;testis;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis; 0.81570 0.16430 -0.178111357 40.44585987 4317.13537 13.08149 GREB1 0.0254855377300684 0.974514460743219 1.52671225838867e-09 growth regulation by estrogen in breast cancer 1 FUNCTION: May play a role in estrogen-stimulated cell proliferation. Acts as a regulator of hormone-dependent cancer growth in breast and prostate cancers.; . TISSUE SPECIFICITY: Expressed in proliferating prostatic tissue and prostate cancer. {ECO:0000269|PubMed:16496412}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;skin;skeletal muscle;breast;uterus;prostate;endometrium;hippocampus;liver;spleen;mammary gland;brain;stomach;peripheral nerve; amygdala;uterus;prostate;uterus corpus;superior cervical ganglion;ovary;testis;ciliary ganglion;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; . . -0.053555672 48.93253126 8947.74529 20.48286 GREB1L . . . growth regulation by estrogen in breast cancer-like . . . unclassifiable (Anatomical System);ovary;tongue;blood;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;whole body;epididymis;placenta;macula lutea;visual apparatus;liver;head and neck;spleen; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skin; 0.24849 0.10248 0.86534717 88.80042463 315.39267 3.77352 GREM1 0.711099436104345 0.273961646048147 0.014938917847508 gremlin 1, DAN family BMP antagonist FUNCTION: Cytokine that may play an important role during carcinogenesis and metanephric kidney organogenesis, as a BMP antagonist required for early limb outgrowth and patterning in maintaining the FGF4-SHH feedback loop. Down-regulates the BMP4 signaling in a dose-dependent manner. Acts as inhibitor of monocyte chemotaxis (By similarity). {ECO:0000250, ECO:0000269|PubMed:10894942}.; DISEASE: Polyposis syndrome, mixed hereditary 1 (HMPS1) [MIM:601228]: A disease characterized by apparent autosomal dominant inheritance of multiple types of colorectal polyp, with colorectal carcinoma occurring in a high proportion of affected individuals. Patients can develop polyps of multiple and mixed morphologies, including serrated lesions, Peutz-Jeghers polyps, juvenile polyps, conventional adenomas and colorectal carcinoma in the absence of any identifiable extra-colonic features. {ECO:0000269|PubMed:22561515}. Note=The disease is caused by mutations affecting the gene represented in this entry. HMPS1 is caused by a duplication spanning the 3' end of the SCG5 gene and a region upstream of the GREM1 locus. This duplication is associated with increased allele-specific GREM1 expression that may cause reduced bone morphogenetic protein (BMP) pathway activity. This mechanism also underlies tumorigenesis in juvenile polyposis of the large bowel (PubMed:22561515). {ECO:0000269|PubMed:22561515}.; TISSUE SPECIFICITY: Highly expressed in small intestine, fetal brain and colon. Expression is restricted to intestinal subepithelial myofibroblasts (ISEMFs) at the crypt base. In subjects with HMPS1, by contrast, GREM1 is expressed, not only in basal ISEMFs, but also at very high levels in epithelial cells (predominantly colonocytes), with expression extending most of the way up the sides of the crypt. Weakly expressed in brain, ovary, prostate, pancreas and skeletal muscle. In brain found in the region localized around the internal capsule in the large subcortical nuclei, including caudate, putamen, substantia nigra, thalamus and subthalamus. Predominantly expressed in normal cells including neurons, astrocytes and fibroblasts. {ECO:0000269|PubMed:10894942, ECO:0000269|PubMed:22561515}.; ovary;colon;parathyroid;skin;bone marrow;uterus;whole body;endometrium;larynx;thyroid;bone;testis;brain;gall bladder;unclassifiable (Anatomical System);cartilage;tongue;spinal cord;urinary;skeletal muscle;bile duct;breast;pancreas;lung;mesenchyma;placenta;liver;alveolus;head and neck;stomach; superior cervical ganglion;uterus corpus;smooth muscle;appendix;pons;trigeminal ganglion; 0.80979 0.55950 0.125076652 62.7388535 14.2143 0.51400 GREM2 0.081742843165364 0.756239684499432 0.162017472335204 gremlin 2, DAN family BMP antagonist FUNCTION: Cytokine that inhibits the activity of BMP2 and BMP4 in a dose-dependent manner, and thereby modulates signaling by BMP family members. Contributes to the regulation of embryonic morphogenesis via BMP family members. Antagonizes BMP4-induced suppression of progesterone production in granulosa cells (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;cartilage;heart;bone;placenta;testis;brain;stomach; liver;skeletal muscle;cingulate cortex;cerebellum; 0.19273 0.14896 0.125076652 62.7388535 11.78198 0.42616 GRHL1 0.983150778709021 0.0168491340893525 8.72016264443748e-08 grainyhead like transcription factor 1 FUNCTION: Transcription factor involved in epithelial development. Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' (PubMed:12175488, PubMed:18288204). Important regulator of DSG1 in the context of hair anchorage and epidermal differentiation, participates in the maintenance of the skin barrier. There is no genetic interaction with GRHL3, no functional cooperativity due to diverse target gene selectivity during epithelia development (By similarity). Isoform 1 may function as an activator and isoform 2 as a repressor in tissues where both forms are expressed (PubMed:12175488). {ECO:0000250|UniProtKB:Q921D9, ECO:0000269|PubMed:12175488, ECO:0000269|PubMed:18288204}.; . TISSUE SPECIFICITY: Isoform 1 is highly expressed in brain, pancreas, tonsil, placenta and kidney. Isoform 2 is highly expressed in brain and liver. Expressed at very low levels in non- steroidogenic cells. {ECO:0000269|PubMed:10644752, ECO:0000269|PubMed:12175488}.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;blood;skin;skeletal muscle;breast;uterus;prostate;whole body;lung;endometrium;thyroid;placenta;liver;testis;amniotic fluid;head and neck;brain;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.18056 0.20109 -0.113792788 45.25831564 1942.58495 8.11174 GRHL2 0.999880613176069 0.000119386811860728 1.20700955182549e-11 grainyhead like transcription factor 2 FUNCTION: Transcription factor playing an important role in primary neurulation and in epithelial development (PubMed:25152456). Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' acting as an activator and repressor on distinct target genes (By similarity). During embryogenesis, plays unique and cooperative roles with GRHL3 in establishing distinct zones of primary neurulation. Essential for closure 3 (rostral end of the forebrain), functions cooperatively with GRHL3 in closure 2 (forebrain/midbrain boundary) and posterior neuropore closure (By similarity). Regulates epithelial morphogenesis acting as a target gene-associated transcriptional activator of apical junctional complex components. Up-regulates of CLDN3 and CLDN4, as well as of RAB25, which increases the CLDN4 protein and its localization at tight junctions (By similarity). Comprises an essential component of the transcriptional machinery that establishes appropriate expression levels of CLDN4 and CDH1 in different types of epithelia. Exhibits functional redundancy with GRHL3 in epidermal morphogenetic events and epidermal wound repair (By similarity). In lung, forms a regulatory loop with NKX2-1 that coordinates lung epithelial cell morphogenesis and differentiation (By similarity). In keratinocytes, plays a role in telomerase activation during cellular proliferation, regulates TERT expression by binding to TERT promoter region and inhibiting DNA methylation at the 5'-CpG island, possibly by interfering with DNMT1 enzyme activity (PubMed:19015635, PubMed:20938050). In addition, impairs keratinocyte differentiation and epidermal function by inhibiting the expression of genes clustered at the epidermal differentiation complex (EDC) as well as GRHL1 and GRHL3 through epigenetic mechanisms (PubMed:23254293). {ECO:0000250|UniProtKB:Q8K5C0, ECO:0000269|PubMed:19015635, ECO:0000269|PubMed:20938050, ECO:0000269|PubMed:20978075, ECO:0000269|PubMed:23254293, ECO:0000269|PubMed:25152456, ECO:0000305|PubMed:12175488}.; DISEASE: Deafness, autosomal dominant, 28 (DFNA28) [MIM:608641]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA28 is characterized by mild to moderate hearing loss across most frequencies that progresses to severe loss in the higher frequencies by the fifth decade. {ECO:0000269|PubMed:12393799}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ectodermal dysplasia/short stature syndrome (ECTDS) [MIM:616029]: An autosomal recessive ectodermal dysplasia syndrome characterized by nail dystrophy and/or loss, oral mucosa and/or tongue pigmentation, abnormal dentition, keratoderma affecting the margins of the palms and soles, focal hyperkeratosis of the dorsal aspects of the hands and feet, and short stature. {ECO:0000269|PubMed:25152456}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in keratinocytes (at protein level). Highly expressed in placenta, prostate, brain and kidney. Lower- level expression in a variety of epithelial tissues such as thymus, lung, salivary gland, mammary gland and digestive tract. Expressed in the cochlear. {ECO:0000269|PubMed:12175488, ECO:0000269|PubMed:12393799, ECO:0000269|PubMed:20978075, ECO:0000269|PubMed:25152456}.; unclassifiable (Anatomical System);cartilage;heart;ovary;colon;blood;skin;skeletal muscle;breast;uterus;prostate;lung;endometrium;larynx;placenta;head and neck;stomach; . 0.94042 0.15234 -0.402212257 26.7338995 378.61795 4.10168 GRHL3 0.99558395801223 0.0044159618303512 8.01574183462199e-08 grainyhead like transcription factor 3 FUNCTION: Transcription factor playing important roles in primary neurulation and in the differentiation of stratified epithelia of both ectodermal and endodermal origin (By similarity). Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' acting as an activator and repressor on distinct target genes (PubMed:21081122, PubMed:25347468). xhibits functional redundancy with GRHL2 in epidermal morphogenetic events and epidermal wound repair (By similarity). Exhibits functional redundancy with GRHL2 in epidermal morphogenetic events and epidermal wound repair but is essential to form the epidermal barrier with TGM3 as critical direct target gene among others. Despite being dispensable during normal epidermal homeostasis in the adulthood, is again required for barrier repair after immune-mediated epidermal damage, regulates distinct gene batteries in embryonic epidermal differentiation and adult epidermal barrier reformation after injury. Plays unique and cooperative roles with GRHL2 in establishing distinct zones of primary neurulation. Essential for spinal closure, functions cooperatively with GRHL2 in closure 2 (forebrain/midbrain boundary) and posterior neuropore closure (By similarity). Also required for proper development of the oral periderm (PubMed:24360809). No genetic interaction with GRHL3, no functional cooperativity due to diverse target gene selectivity (PubMed:21081122). {ECO:0000250|UniProtKB:Q5FWH3, ECO:0000269|PubMed:12549979, ECO:0000269|PubMed:21081122, ECO:0000269|PubMed:24360809, ECO:0000269|PubMed:25347468}.; . TISSUE SPECIFICITY: Expressed in brain, colon, pancreas, placenta and kidney. Isoform 1 is expressed in lung and tonsil. Isoform 2 is prostate-specific. {ECO:0000269|PubMed:12549979}.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;skin;uterus;breast;lung;endometrium;larynx;placenta;testis;head and neck;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.16947 0.22965 0.538284722 81.08634112 3383.66644 11.13788 GRHPR 0.00013344009925403 0.850978985765411 0.148887574135335 glyoxylate reductase/hydroxypyruvate reductase FUNCTION: Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate.; . TISSUE SPECIFICITY: Ubiquitous. Most abundantly expressed in the liver. {ECO:0000269|PubMed:10679197}.; myocardium;lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;gum;thyroid;iris;germinal center;brain;tonsil;heart;adrenal cortex;blood;lens;breast;epididymis;macula lutea;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;duodenum;amnion;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;heart;liver;ciliary ganglion;atrioventricular node;kidney;skeletal muscle; 0.11316 . -0.111973265 45.35857514 206.49934 3.10503 GRIA1 0.999436340840325 0.000563659052529541 1.07145585613702e-10 glutamate ionotropic receptor AMPA type subunit 1 FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L- glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. {ECO:0000269|PubMed:20805473, ECO:0000269|PubMed:21172611}.; . TISSUE SPECIFICITY: Widely expressed in brain.; unclassifiable (Anatomical System);frontal lobe;placenta;brain;skeletal muscle; amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;cerebellum peduncles;temporal lobe;pons;caudate nucleus;atrioventricular node;subthalamic nucleus;fetal brain;globus pallidus;trigeminal ganglion;parietal lobe;cerebellum; 0.39857 0.29337 -1.197736472 5.785562633 947.1656 5.96106 GRIA2 0.99550949045347 0.00449050612766888 3.41886082988809e-09 glutamate ionotropic receptor AMPA type subunit 2 FUNCTION: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L- glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. {ECO:0000269|PubMed:20614889}.; . . unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;retina;uterus;breast;pancreas;lung;frontal lobe;endometrium;hippocampus;pituitary gland;testis;brain; whole brain;dorsal root ganglion;amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.30570 0.25829 -0.778825328 12.88039632 32.84712 1.01918 GRIA3 0.998653777646266 0.0013462179344122 4.41932159254472e-09 glutamate ionotropic receptor AMPA type subunit 3 FUNCTION: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L- glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. {ECO:0000269|PubMed:21172611}.; DISEASE: Mental retardation, X-linked 94 (MRX94) [MIM:300699]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non- syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. MRX94 patients have moderate mental retardation. Other variable features are macrocephaly, seizures, myoclonic jerks, autistic behavior, asthenic body habitus, distal muscle weakness and hyporeflexia. {ECO:0000269|PubMed:17989220}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;islets of Langerhans;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;breast;optic nerve;lung;frontal lobe;adrenal gland;placenta;macula lutea;liver;kidney; amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;pons;atrioventricular node;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.40491 0.17596 -0.115612493 45.12856806 18.51356 0.64055 GRIA4 0.988749209826684 0.0112507888491724 1.32414383326382e-09 glutamate ionotropic receptor AMPA type subunit 4 FUNCTION: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L- glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. {ECO:0000269|PubMed:21172611}.; . . unclassifiable (Anatomical System);optic nerve;frontal lobe;sympathetic chain;macula lutea;hippocampus;fovea centralis;choroid;lens;brain;retina; superior cervical ganglion;ciliary ganglion;parietal lobe; 0.25025 0.18924 -1.089312628 7.047652748 39.34342 1.16364 GRID1 0.950796125986905 0.0492036221499444 2.51863150524501e-07 glutamate ionotropic receptor delta type subunit 1 FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists.; . . unclassifiable (Anatomical System);heart;ovary;cartilage;skin;uterus;lung;frontal lobe;thyroid;hippocampus;testis;spleen;kidney;brain;pineal gland;stomach; subthalamic nucleus;superior cervical ganglion;temporal lobe;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.40271 0.11711 -2.100076584 1.545175749 701.32829 5.26849 GRID1-AS1 . . . GRID1 antisense RNA 1 . . . . . . . . . . . GRID2 0.999998446555818 1.55344418154788e-06 3.07957251237632e-16 glutamate ionotropic receptor delta type subunit 2 FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists.; DISEASE: Spinocerebellar ataxia, autosomal recessive, 18 (SCAR18) [MIM:616204]: Spinocerebellar ataxia defines a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR18 features include progressive cerebellar atrophy, delayed psychomotor development, severely impaired gait, ocular movement abnormalities, and intellectual disability. {ECO:0000269|PubMed:23611888, ECO:0000269|PubMed:24078737, ECO:0000269|PubMed:25841024}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;testis; superior cervical ganglion;globus pallidus;skeletal muscle; 0.34658 0.16148 -0.839512508 11.40009436 1421.60468 7.04400 GRID2IP 0.314734427863365 0.488396554797204 0.196869017339431 Grid2 interacting protein FUNCTION: Postsynaptic scaffolding protein at the parallel fiber- Purkinje cell synapse, where it may serve to link GRID2 with actin cytoskeleton and various signaling molecules. {ECO:0000250}.; . . . . 0.17067 . . . 4147.16671 12.78487 GRIFIN . . . galectin-related inter-fiber protein . . TISSUE SPECIFICITY: Not detected in lens. {ECO:0000269|PubMed:18087242}.; . . . . . . . . GRIK1 3.20558900258698e-05 0.999388921315192 0.000579022794782239 glutamate ionotropic receptor kainate type subunit 1 FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L- glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. May be involved in the transmission of light information from the retina to the hypothalamus.; . TISSUE SPECIFICITY: Most abundant in the cerebellum and the suprachiasmatic nuclei (SCN) of the hypothalamus.; unclassifiable (Anatomical System);uterus;prostate;whole body;ovary;placenta;parathyroid;germinal center;kidney;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;cingulate cortex; 0.17737 0.54971 -1.635123713 2.836753951 70.21802 1.74053 GRIK1-AS1 . . . GRIK1 antisense RNA 1 . . . heart; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.29471 . . . . . GRIK1-AS2 0.395414271289592 0.473220172850382 0.131365555860025 GRIK1 antisense RNA 2 . . . . . 0.07597 . . . 10.98282 0.39759 GRIK2 0.994567954112697 0.0054320447859458 1.10135670037754e-09 glutamate ionotropic receptor kainate type subunit 2 FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L- glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. May be involved in the transmission of light information from the retina to the hypothalamus. Modulates cell surface expression of NETO2 (By similarity). {ECO:0000250}.; DISEASE: Mental retardation, autosomal recessive 6 (MRT6) [MIM:611092]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. In contrast to syndromic or specific mental retardation which also present with associated physical, neurological and/or psychiatric manifestations, intellectual deficiency is the only primary symptom of non-syndromic mental retardation. MRT6 patients display mild to severe mental retardation and psychomotor development delay in early childhood. Patients do not have neurologic problems, congenital malformations, or facial dysmorphism. Body height, weight, and head circumference are normal. {ECO:0000269|PubMed:17847003}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expression is higher in cerebellum than in cerebral cortex.; unclassifiable (Anatomical System);ovary;placenta;parathyroid;brain;skeletal muscle;cerebellum; amygdala;dorsal root ganglion;whole brain;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;cerebellum peduncles;hypothalamus;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.53627 . -1.131590109 6.481481481 129.48869 2.48041 GRIK3 0.999980170163858 1.98298359892781e-05 1.52259968927211e-13 glutamate ionotropic receptor kainate type subunit 3 FUNCTION: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA.; . . . . 0.20191 0.13449 -1.679229468 2.677518283 63.24558 1.62764 GRIK4 0.630846158157366 0.36915132407563 2.51776700393243e-06 glutamate ionotropic receptor kainate type subunit 4 FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists.; . . . . 0.25904 0.16134 -0.547447733 19.99882048 476.06358 4.50654 GRIK5 0.917779687927041 0.0822201248159323 1.87257026961289e-07 glutamate ionotropic receptor kainate type subunit 5 FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds kainate > quisqualate > domoate > L- glutamate >> AMPA >> NMDA = 1S,3R-ACPD.; . . unclassifiable (Anatomical System);lymph node;islets of Langerhans;retina;prostate;optic nerve;frontal lobe;bone;hippocampus;visual apparatus;testis;kidney;mammary gland;brain;peripheral nerve; amygdala;superior cervical ganglion;thalamus;occipital lobe;cerebellum peduncles;temporal lobe;atrioventricular node;caudate nucleus;pons;subthalamic nucleus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.24988 0.16105 -1.127956862 6.522764803 136.49056 2.53978 GRIN1 0.972708946068042 0.0272909959305508 5.80014069022555e-08 glutamate ionotropic receptor NMDA type subunit 1 FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. This protein plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors (By similarity). {ECO:0000250}.; DISEASE: Mental retardation, autosomal dominant 8 (MRD8) [MIM:614254]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:21376300}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);amygdala;optic nerve;frontal lobe;islets of Langerhans;macula lutea;visual apparatus;fovea centralis;choroid;lens;brain;retina; whole brain;amygdala;medulla oblongata;superior cervical ganglion;thalamus;temporal lobe;caudate nucleus;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.29795 0.23773 -1.111360919 6.717386176 4.30815 0.15668 GRIN2A 0.99804480805101 0.00195519149951803 4.49472318599573e-10 glutamate ionotropic receptor NMDA type subunit 2A FUNCTION: NMDA receptor subtype of glutamate-gated ion channels possesses high calcium permeability and voltage-dependent sensitivity to magnesium. Activation requires binding of agonist to both types of subunits.; DISEASE: Epilepsy, focal, with speech disorder and with or without mental retardation (FESD) [MIM:245570]: A highly variable neurologic disorder with features ranging from severe early-onset seizures associated with delayed psychomotor development, persistent speech difficulties, and mental retardation to a more benign entity characterized by childhood onset of mild or asymptomatic seizures associated with transient speech difficulties followed by remission of seizures in adolescence and normal psychomotor development. The disorder encompasses several clinical entities, including Landau-Kleffner syndrome, epileptic encephalopathy with continuous spike and wave during slow-wave sleep, autosomal dominant rolandic epilepsy, mental retardation and speech dyspraxia, and benign epilepsy with centrotemporal spikes. {ECO:0000269|PubMed:20890276, ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:23933818, ECO:0000269|PubMed:23933819, ECO:0000269|PubMed:23933820, ECO:0000269|PubMed:24504326, ECO:0000269|PubMed:24903190}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving GRIN2A has been found in a family with epilepsy and neurodevelopmental defects. Translocation t(16;17)(p13.2;q11.2).; DISEASE: Note=GRIN2A somatic mutations have been frequently found in cutaneous malignant melanoma, suggesting that the glutamate signaling pathway may play a role in the pathogenesis of melanoma. {ECO:0000269|PubMed:21499247, ECO:0000269|PubMed:24455489}.; . medulla oblongata;frontal lobe;nasopharynx;head and neck;kidney;lens;brain;skeletal muscle; subthalamic nucleus;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;globus pallidus;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.37855 0.47307 -1.455091209 3.886529842 119.73741 2.38246 GRIN2B 0.999994895762786 5.10423718653419e-06 2.75953725792621e-14 glutamate ionotropic receptor NMDA type subunit 2B FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death (By similarity). {ECO:0000250}.; DISEASE: Mental retardation, autosomal dominant 6 (MRD6) [MIM:613970]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:20890276, ECO:0000269|PubMed:23033978}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epileptic encephalopathy, early infantile, 27 (EIEE27) [MIM:616139]: A form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberrations involving GRIN2B has been found in patients with mental retardation. Translocations t(9;12)(p23;p13.1) and t(10;12)(q21.1;p13.1) with a common breakpoint in 12p13.1.; TISSUE SPECIFICITY: Primarily found in the fronto-parieto-temporal cortex and hippocampus pyramidal cells, lower expression in the basal ganglia. {ECO:0000269|PubMed:9547169}.; lung;testis;colon;brain; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.44258 0.47751 -2.412493531 1.067468743 41.83799 1.21856 GRIN2C 0.00393764821854446 0.994375797722345 0.00168655405911031 glutamate ionotropic receptor NMDA type subunit 2C FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine.; . TISSUE SPECIFICITY: Mainly expressed in brain with predominant expression is in the cerebellum, also present in the hippocampus, amygdala, caudate nucleus, corpus callosum, subthalamic nuclei and thalamus. Detected in the heart, skeletal muscle and pancreas.; unclassifiable (Anatomical System);optic nerve;hypothalamus;thyroid;macula lutea;iris;colon;fovea centralis;choroid;lens;brain;retina; amygdala;superior cervical ganglion;occipital lobe;thalamus;cerebellum peduncles;temporal lobe;pons;caudate nucleus;skeletal muscle;thyroid;prefrontal cortex;ciliary ganglion;trigeminal ganglion;cerebellum; 0.11618 0.20784 . . 2384.65773 9.06255 GRIN2D 0.998648757458714 0.00135123808168232 4.45960371921106e-09 glutamate ionotropic receptor NMDA type subunit 2D FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine.; . . unclassifiable (Anatomical System);lung;frontal lobe;ovary;testis; dorsal root ganglion;superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.31918 0.14626 . . 114.71527 2.33202 GRIN3A 0.123333065136569 0.876623303008957 4.36318544734111e-05 glutamate ionotropic receptor NMDA type subunit 3A FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with reduced single-channel conductance, low calcium permeability and low voltage-dependent sensitivity to magnesium. Mediated by glycine. May play a role in the development of dendritic spines. May play a role in PPP2CB-NMDAR mediated signaling mechanism (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);brain;peripheral nerve; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.42957 0.11045 0.209410829 67.5277188 9121.93484 20.73840 GRIN3B 0.00111371164374087 0.952832627879133 0.0460536604771257 glutamate ionotropic receptor NMDA type subunit 3B FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with reduced single-channel conductance, low calcium permeability and low voltage-dependent sensitivity to magnesium. Mediated by glycine.; . . lung; . 0.05632 . . . 14513.3031 26.28567 GRINA 0.757342473317658 0.242243479701761 0.000414046980580848 glutamate ionotropic receptor NMDA type subunit associated protein 1 FUNCTION: Potential apoptotic regulator.; . . medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;placenta;hippocampus;duodenum;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;liver;prefrontal cortex;globus pallidus;atrioventricular node;skeletal muscle; 0.19477 0.13845 -0.494039303 22.09247464 14.93909 0.53831 GRIP1 0.916894968096624 0.0831050303088267 1.59454973209467e-09 glutamate receptor interacting protein 1 FUNCTION: May play a role as a localized scaffold for the assembly of a multiprotein signaling complex and as mediator of the trafficking of its binding partners at specific subcellular location in neurons. {ECO:0000269|PubMed:10197531}.; DISEASE: Fraser syndrome (FRASS) [MIM:219000]: Multisystem malformation usually comprising cryptophthalmos, cutaneous syndactyly, ear abnormalities, renal agenesis and congenital heart defects. {ECO:0000269|PubMed:22510445}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;lung;ovary;heart;placenta;testis;parathyroid;kidney;brain;skin;retina; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.48210 0.27614 -0.529034136 20.85987261 260.84427 3.46842 GRIP2 . . . glutamate receptor interacting protein 2 FUNCTION: May play a role as a localized scaffold for the assembly of a multiprotein signaling complex and as mediator of the trafficking of its binding partners at specific subcellular location in neurons. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;colon;parathyroid;fovea centralis;choroid;lens;retina;bone marrow;breast;pancreas;prostate;optic nerve;lung;endometrium;bone;placenta;macula lutea;testis;germinal center;kidney;brain;stomach; . 0.38331 0.12505 . . . . GRIPAP1 0.996933311471836 0.00306668186836813 6.65979575081835e-09 GRIP1 associated protein 1 . . . . . 0.17879 0.08356 -0.290161348 33.33923095 49.34047 1.37418 GRK1 0.00915421207464947 0.8093753960402 0.18147039188515 G protein-coupled receptor kinase 1 FUNCTION: Retina-specific kinase involved in the signal turnoff via phosphorylation of rhodopsin (RHO), the G protein- coupled receptor that initiates the phototransduction cascade. This rapid desensitization is essential for scotopic vision and permits rapid adaptation to changes in illumination. {ECO:0000269|PubMed:15946941}.; DISEASE: Night blindness, congenital stationary, Oguchi type 2 (CSNBO2) [MIM:613411]: A non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia. Congenital stationary night blindness Oguchi type is associated with fundus discoloration and abnormally slow dark adaptation. {ECO:0000269|PubMed:17070587, ECO:0000269|PubMed:9020843}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Retinal-specific. Expressed in rods and cones cells. {ECO:0000269|PubMed:11717351}.; . . 0.17845 0.18043 . . 241.91658 3.35925 GRK4 5.6904219834531e-07 0.964890222158263 0.0351092087995383 G protein-coupled receptor kinase 4 FUNCTION: Specifically phosphorylates the activated forms of G protein-coupled receptors. GRK4-alpha can phosphorylate rhodopsin and its activity is inhibited by calmodulin; the other three isoforms do not phosphorylate rhodopsin and do not interact with calmodulin. GRK4-alpha and GRK4-gamma phosphorylate DRD3. Phosphorylates ADRB2. {ECO:0000269|PubMed:19520868, ECO:0000269|PubMed:8626439}.; . TISSUE SPECIFICITY: Isoform 1, isoform 2, isoform 3, and isoform 4 are expressed in testis. Isoform 4 is expressed in myometrium. {ECO:0000269|PubMed:16636192, ECO:0000269|PubMed:8626439}.; optic nerve;lung;nasopharynx;placenta;macula lutea;iris;testis;fovea centralis;choroid;lens;brain;retina; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;pons; 0.46645 . 0.602602982 82.87331918 5893.84025 15.91487 GRK5 0.984107718022279 0.0158922064573729 7.55203483704489e-08 G protein-coupled receptor kinase 5 FUNCTION: Serine/threonine kinase that phosphorylates preferentially the activated forms of a variety of G-protein- coupled receptors (GPCRs). Such receptor phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events leading to their down-regulation. Phosphorylates a variety of GPCRs, including adrenergic receptors, muscarinic acetylcholine receptors (more specifically Gi-coupled M2/M4 subtypes), dopamine receptors and opioid receptors. In addition to GPCRs, also phosphorylates various substrates: Hsc70- interacting protein/ST13, TP53/p53, HDAC5, and arrestin-1/ARRB1. Phosphorylation of ARRB1 by GRK5 inhibits G-protein independent MAPK1/MAPK3 signaling downstream of 5HT4-receptors. Phosphorylation of HDAC5, a repressor of myocyte enhancer factor 2 (MEF2) leading to nuclear export of HDAC5 and allowing MEF2- mediated transcription. Phosphorylation of TP53/p53, a crucial tumor suppressor, inhibits TP53/p53-mediated apoptosis. Phosphorylation of ST13 regulates internalization of the chemokine receptor. Phosphorylates rhodopsin (RHO) (in vitro) and a non G- protein-coupled receptor, LRP6 during Wnt signaling (in vitro). {ECO:0000269|PubMed:19661922, ECO:0000269|PubMed:19801552, ECO:0000269|PubMed:20038610, ECO:0000269|PubMed:20124405, ECO:0000269|PubMed:21728385}.; . TISSUE SPECIFICITY: Highest levels in heart, placenta, lung > skeletal muscle > brain, liver, pancreas > kidney. {ECO:0000269|PubMed:7685906}.; . . 0.30883 0.17184 0.04598748 57.47817882 2649.7747 9.66631 GRK5-IT1 . . . GRK5 intronic transcript 1 . . . . . . . . . . . GRK6 0.248841091131392 0.751104891152422 5.40177161860498e-05 G protein-coupled receptor kinase 6 FUNCTION: Specifically phosphorylates the activated forms of G protein-coupled receptors. Such receptor phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events leading to their desensitization. Seems to be involved in the desensitization of D2-like dopamine receptors in striatum and chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis (By similarity). Phosphorylates rhodopsin (RHO) (in vitro) and a non G-protein-coupled receptor: LRP6 during Wnt signaling (in vitro). {ECO:0000250, ECO:0000269|PubMed:19801552, ECO:0000269|PubMed:20048153}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8415712}.; lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;optic nerve;endometrium;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;heart;white blood cells;whole blood; 0.50650 0.20697 -0.244249595 36.17008728 119.55567 2.37977 GRK6P1 . . . G protein-coupled receptor kinase 6 pseudogene 1 . . . . . . . . . . . GRK7 1.19306241308231e-07 0.194332168830884 0.805667711862874 G protein-coupled receptor kinase 7 FUNCTION: Retina-specific kinase involved in the shutoff of the photoresponse and adaptation to changing light conditions via cone opsin phosphorylation, including rhodopsin (RHO). {ECO:0000269|PubMed:15946941}.; . TISSUE SPECIFICITY: Retinal cones, outer and inner segments. {ECO:0000269|PubMed:11754336, ECO:0000269|PubMed:18803695}.; . . 0.10201 0.11568 0.712836712 85.76315169 958.17218 5.99095 GRM1 0.989964591707789 0.0100353838550882 2.44371229842454e-08 glutamate receptor, metabotropic 1 FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum. {ECO:0000269|PubMed:24603153, ECO:0000269|PubMed:7476890}.; . TISSUE SPECIFICITY: Detected in brain.; lymphoreticular;skin;uterus;prostate;larynx;pituitary gland;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;hypothalamus;blood;skeletal muscle;pancreas;lung;placenta;hippocampus;liver;head and neck;spleen;kidney;thymus;cerebellum; superior cervical ganglion;cerebellum peduncles;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle;cerebellum; 0.35028 0.18579 -0.145152788 42.33899505 369.26185 4.06076 GRM2 0.983083426226356 0.0169144235880976 2.15018554681022e-06 glutamate receptor, metabotropic 2 FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. May mediate suppression of neurotransmission or may be involved in synaptogenesis or synaptic stabilization. {ECO:0000269|PubMed:18297054, ECO:0000269|PubMed:22300836, ECO:0000269|PubMed:23129762, ECO:0000269|PubMed:7620613}.; . TISSUE SPECIFICITY: Detected in brain cortex (at protein level). Widely expressed in different regions of the adult brain as well as in fetal brain. {ECO:0000269|PubMed:18297054}.; unclassifiable (Anatomical System);optic nerve;macula lutea;testis;fovea centralis;choroid;lens;brain;skeletal muscle;retina; amygdala;whole brain;superior cervical ganglion;heart;prefrontal cortex;skeletal muscle; 0.87398 0.18223 -0.350843407 29.54116537 367.28065 4.05059 GRM3 0.984710456532565 0.0152892040996612 3.39367773702995e-07 glutamate receptor, metabotropic 3 FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity. {ECO:0000269|PubMed:8840013}.; . TISSUE SPECIFICITY: Detected in brain cortex, thalamus, subthalamic nucleus, substantia nigra, hypothalamus, hippocampus, corpus callosum, caudate nucleus and amygdala. {ECO:0000269|PubMed:8840013}.; unclassifiable (Anatomical System);lung;frontal lobe;hypothalamus;placenta;hippocampus;testis;brain;aorta; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.49425 0.25538 -1.285933373 5.083746167 78.36031 1.86769 GRM4 0.979350085369263 0.020649770712684 1.4391805272608e-07 glutamate receptor, metabotropic 4 FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity. {ECO:0000269|PubMed:7617140, ECO:0000269|PubMed:8738157, ECO:0000269|PubMed:9473604}.; . TISSUE SPECIFICITY: Strongly expressed in the cerebellum. Expressed at low levels in hippocampus, hypothalamus and thalamus. No expression detected in liver. {ECO:0000269|PubMed:7617140, ECO:0000269|PubMed:8738157}.; . . 0.27001 0.19777 -2.478673049 0.96131163 76.44854 1.83436 GRM5 0.985984068270878 0.0140158762706693 5.54584531757082e-08 glutamate receptor, metabotropic 5 FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system and generates a calcium-activated chloride current. Plays an important role in the regulation of synaptic plasticity and the modulation of the neural network activity. {ECO:0000269|PubMed:7908515, ECO:0000269|Ref.7}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;whole body;brain; whole brain;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.34314 0.18668 -1.263883952 5.260674687 220.27519 3.20838 GRM5-AS1 . . . GRM5 antisense RNA 1 . . . . . . . . . . . GRM6 2.41818920529745e-09 0.445039690245563 0.554960307336247 glutamate receptor, metabotropic 6 FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity (By similarity). Signaling stimulates TRPM1 channel activity and Ca(2+) uptake. Required for normal vision. {ECO:0000250, ECO:0000269|PubMed:23452348}.; . TISSUE SPECIFICITY: Detected in melanocytes. {ECO:0000269|PubMed:23452348}.; breast;optic nerve;whole body;macula lutea;fovea centralis;choroid;lens;brain;stomach;retina; dorsal root ganglion;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.28520 . -1.31556435 4.794762916 962.94902 6.00597 GRM7 0.999169068679813 0.000830929956848364 1.36333839654473e-09 glutamate receptor, metabotropic 7 FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. {ECO:0000269|PubMed:9473604}.; . TISSUE SPECIFICITY: Expressed in many areas of the brain, especially in the cerebral cortex, hippocampus, and cerebellum. Expression of GRM7 isoforms in non-neuronal tissues appears to be restricted to isoform 3 and isoform 4. {ECO:0000269|PubMed:12052533, ECO:0000269|PubMed:8840028}.; medulla oblongata; dorsal root ganglion;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.68439 0.09371 -1.616692429 2.937013447 1262.73334 6.70044 GRM7-AS1 . . . GRM7 antisense RNA 1 . . . . . . . . . . . GRM7-AS2 . . . GRM7 antisense RNA 2 . . . . . . . . . . . GRM7-AS3 . . . GRM7 antisense RNA 3 . . . . . . . . . . . GRM8 0.0040386229885192 0.99589454132281 6.68356886704179e-05 glutamate receptor, metabotropic 8 FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. {ECO:0000269|PubMed:9473604}.; . . unclassifiable (Anatomical System);lung;colon;mammary gland;brain; dorsal root ganglion;testis - interstitial;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.52674 0.18704 -0.569494998 19.04340646 1608.26119 7.42199 GRN 0.0602784288448183 0.939577162259816 0.000144408895365817 granulin FUNCTION: Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling.; DISEASE: Ubiquitin-positive frontotemporal dementia (UP-FTD) [MIM:607485]: Frontotemporal dementia (FTD) is the second most common cause of dementia in people under the age of 65 years. It is an autosomal dominant neurodegenerative disease. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ceroid lipofuscinosis, neuronal, 11 (CLN11) [MIM:614706]: A form of neuronal ceroid lipofuscinosis characterized by rapidly progressive visual loss due to retinal dystrophy, seizures, cerebellar ataxia, and cerebellar atrophy. Cognitive decline may also occur. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material. {ECO:0000269|PubMed:22608501}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In myelogenous leukemic cell lines of promonocytic, promyelocytic, and proerythroid lineage, in fibroblasts, and very strongly in epithelial cell lines. Present in inflammatory cells and bone marrow. Highest levels in kidney.; medulla oblongata;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;prostate;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;urinary;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; lung;placenta; 0.11811 0.43018 -0.461076406 23.66124086 118.35089 2.36635 GRP 2.14419491039997e-06 0.0816436076811639 0.918354248123926 gastrin releasing peptide FUNCTION: GRP stimulates gastrin release as well as other gastrointestinal hormones. Operates as a negative feedback regulating fear and established a causal relationship between GRP- receptor gene expression, long-term potentiation, and amygdala- dependent memory for fear (By similarity). {ECO:0000250}.; . . uterus;prostate;lung;ovary;heart;placenta;testis;parathyroid;pineal gland;skin; whole brain;superior cervical ganglion;fetal brain;ciliary ganglion;fetal lung; 0.15047 0.12256 . . 108.79814 2.26455 GRPEL1 0.896268185523963 0.102748808318231 0.000983006157805838 GrpE like 1, mitochondrial FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins.; . . medulla oblongata;ovary;salivary gland;intestine;colon;vein;skin;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;iris;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;adrenal gland;adrenal cortex;prefrontal cortex;liver;testis;kidney;skeletal muscle; 0.19622 0.11034 0.170987912 65.5579146 184.97165 2.95207 GRPEL2 0.00575467231542279 0.901311364374467 0.0929339633101107 GrpE like 2, mitochondrial FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins. Stimulates ATPase activity of mt-HSP70. May also serve to modulate the interconversion of oligomeric (inactive) and monomeric (active) forms of mt-HSP70 (By similarity). {ECO:0000250}.; . . ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;frontal lobe;cochlea;cerebral cortex;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.02850 0.08104 -0.383807564 27.41802312 18.50199 0.64003 GRPEL2-AS1 . . . GRPEL2 antisense RNA 1 . . . . . . . . . . . GRPEL2P1 . . . GrpE like 2, mitochondrial pseudogene 1 . . . . . . . . . . . GRPEL2P2 . . . GrpE like 2, mitochondrial pseudogene 2 . . . . . . . . . . . GRPEL2P3 . . . GrpE like 2, mitochondrial pseudogene 3 . . . . . . . . . . . GRPR 0.138137201690617 0.779694565478721 0.0821682328306629 gastrin releasing peptide receptor FUNCTION: Receptor for gastrin releasing peptide (GRP). This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.; . TISSUE SPECIFICITY: Highly expressed in pancreas. Also expressed in stomach, adrenal cortex and brain. {ECO:0000269|PubMed:11245983}.; . . 0.44732 0.21795 0.106667882 61.73036093 42.61477 1.23623 GRSF1 7.98241685263603e-07 0.731401567091525 0.26859763466679 G-rich RNA sequence binding factor 1 FUNCTION: Regulator of post-transcriptional mitochondrial gene expression, required for assembly of the mitochondrial ribosome and for recruitment of mRNA and lncRNA. Binds RNAs containing the 14 base G-rich element. Preferentially binds RNAs transcribed from three contiguous genes on the light strand of mtDNA, the ND6 mRNA, and the long non-coding RNAs for MT-CYB and MT-ND5, each of which contains multiple consensus binding sequences. {ECO:0000269|PubMed:23473033, ECO:0000269|PubMed:23473034}.; . . ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;pineal body;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;atrium;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;placenta;hippocampus;kidney;stomach;aorta;thymus; dorsal root ganglion;amygdala;whole brain;occipital lobe;medulla oblongata;hypothalamus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.35977 . -0.514264485 21.41424864 50.68004 1.40200 GRTP1 4.78830161751861e-06 0.406830018914622 0.59316519278376 growth hormone regulated TBC protein 1 FUNCTION: May act as a GTPase-activating protein for Rab family protein(s).; . . unclassifiable (Anatomical System);ovary;colon;fovea centralis;choroid;lens;retina;uterus;prostate;optic nerve;lung;placenta;macula lutea;liver;spleen;kidney;bladder;mammary gland;stomach; superior cervical ganglion;temporal lobe;liver; 0.39539 . 0.132352165 63.48785091 1686.15264 7.56664 GRTP1-AS1 . . . GRTP1 antisense RNA 1 . . . . . . . . . . . GRWD1 0.337778593629583 0.659162388646251 0.00305901772416609 glutamate-rich WD repeat containing 1 . . . lymphoreticular;medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;cornea;adrenal gland;mesenchyma;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;thalamus;adrenal cortex;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.23957 0.12398 -0.378346116 28.01368247 2363.82526 9.02158 GRXCR1 1.27110683991337e-07 0.201037024133287 0.798962848756029 glutaredoxin and cysteine rich domain containing 1 FUNCTION: May play a role in actin filament architecture in developing stereocilia of sensory cells. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at low levels in adult lung, brain and duodenum with moderate levels in testis. Highly expressed in fetal cochlea. {ECO:0000269|PubMed:20137778}.; . . . . 0.527368849 80.73248408 2061.22005 8.36632 GRXCR2 1.74530955295463e-05 0.44146921279336 0.55851333411111 glutaredoxin and cysteine rich domain containing 2 FUNCTION: Could play a role in maintaining cochlear stereocilia bundles that are involved in sound detection. {ECO:0000269|PubMed:24619944}.; DISEASE: Deafness, autosomal recessive, 101 (DFNB101) [MIM:615837]: A form of non-syndromic deafness characterized by bilateral, moderate to severe hearing loss. Vestibular function is unaffected. {ECO:0000269|PubMed:24619944}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . . 0.705562627 85.52724699 1177.71732 6.52037 G0S2 0.153689954137791 0.634997968669883 0.211312077192326 G0/G1 switch 2 FUNCTION: Promotes apoptosis by binding to BCL2, hence preventing the formation of protective BCL2-BAX heterodimers. {ECO:0000269|PubMed:19706769}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in peripheral blood, skeletal muscle and heart, followed by kidney and liver. {ECO:0000269|PubMed:19706769}.; . . 0.07249 . 0.125076652 62.7388535 25.9802 0.84445 GSAP 3.59525944818388e-16 0.241435266914275 0.758564733085724 gamma-secretase activating protein FUNCTION: Regulator of gamma-secretase activity, which specifically activates the production of beta-amyloid protein (beta-amyloid protein 40 and beta-amyloid protein 42), without affecting the cleavage of other gamma-secretase targets such has Notch. The gamma-secretase complex is an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Specifically promotes the gamma-cleavage of APP CTF-alpha (also named APP-CTF) by the gamma-secretase complex to generate beta- amyloid, while it reduces the epsilon-cleavage of APP CTF-alpha, leading to a low production of AICD. {ECO:0000269|PubMed:20811458}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:20811458}.; . . . . 0.268267497 70.64166077 2346.20682 8.97223 GSC 0.0697083404726596 0.73824825316222 0.19204340636512 goosecoid homeobox FUNCTION: Regulates chordin (CHRD). May play a role in spatial programing within discrete embryonic fields or lineage compartments during organogenesis. In concert with NKX3-2, plays a role in defining the structural components of the middle ear; required for the development of the entire tympanic ring (By similarity). Probably involved in the regulatory networks that define neural crest cell fate specification and determine mesoderm cell lineages in mammals. {ECO:0000250, ECO:0000269|PubMed:24290375}.; DISEASE: Short stature, auditory canal atresia, mandibular hypoplasia, skeletal abnormalities (SAMS) [MIM:602471]: An autosomal recessive developmental disorder with features of a first and second branchial arch syndrome, and with unique rhizomelic skeletal anomalies. Craniofacial abnormalities can lead to conductive hearing loss, respiratory insufficiency, and feeding difficulties. Skeletal features include bilateral humeral hypoplasia, humeroscapular synostosis, pelvic abnormalities, and proximal defects of the femora. Affected individuals may also have some features of a neurocristopathy or abnormal mesoderm development, such as urogenital anomalies, that are distinct from other branchial arch syndromes. {ECO:0000269|PubMed:24290375}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;endometrium;bone; superior cervical ganglion;skeletal muscle; 0.20428 0.21922 . . 144.95997 2.62265 GSC2 0.0371862070942536 0.63491946301857 0.327894329887176 goosecoid homeobox 2 FUNCTION: May have a role in development. May regulate its own transcription. May bind the bicoid consensus sequence TAATCC.; . TISSUE SPECIFICITY: Detected in adult testis and pituitary, and in 9-10 week fetal tissue (thorax). Probably expressed in other tissues at low levels.; . . 0.11474 0.11375 . . 611.77755 4.99844 GSDMA 7.61359631115565e-13 0.0180161236519517 0.981983876347287 gasdermin A FUNCTION: Induces apoptosis. {ECO:0000269|PubMed:17471240}.; . TISSUE SPECIFICITY: Expressed predominantly in the gastrointestinal tract and in the skin at a lower level. Also detected in mammary gland. Detected in mucus-secreting pit cells of the gastric epithelium. Not expressed in gastric cancer cells. {ECO:0000269|PubMed:10967128, ECO:0000269|PubMed:17471240}.; tongue;thyroid;head and neck; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.21118 0.10074 0.400544645 76.40953055 11249.16215 23.09053 GSDMB 1.73303703920524e-07 0.41049035032097 0.589509476375326 gasdermin B FUNCTION: May play a role as secretory or metabolic product involved in secretory pathway. May also play a role in achieving and maintaining the final differentiation state of epithelial cells. {ECO:0000269|PubMed:15010812, ECO:0000269|PubMed:18038310}.; . TISSUE SPECIFICITY: Expressed in gastric, liver and colon cell lines, carcinomas and non-lesional tissues. {ECO:0000269|PubMed:18038310}.; unclassifiable (Anatomical System);cartilage;urinary;colon;skeletal muscle;breast;uterus;pancreas;whole body;lung;endometrium;larynx;bone;thyroid;placenta;liver;testis;head and neck;spleen;brain;stomach; ciliary ganglion; 0.12898 0.04721 1.17583962 92.75182826 3707.09331 11.87179 GSDMC 9.34939571735548e-12 0.0770282057555979 0.922971794235053 gasdermin C . . TISSUE SPECIFICITY: Expressed primarily in trachea and spleen. {ECO:0000269|PubMed:11223543}.; pancreas;lung;whole body;larynx;head and neck;skin;skeletal muscle; superior cervical ganglion; 0.02470 0.07503 0.692611128 85.26185421 337.42356 3.90030 GSDMD 4.80694673198233e-07 0.393297033314205 0.606702485991122 gasdermin D . . . ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;liver;white blood cells; 0.06547 0.09123 -0.086288664 47.11606511 230.01248 3.27773 GSE1 . . . Gse1 coiled-coil protein . . . . . 0.17211 0.10783 -2.812224078 0.64873791 1324.65098 6.84299 GSG1 0.00134933358137472 0.862926653688022 0.135724012730603 germ cell associated 1 FUNCTION: May cause the redistribution of PAPOLB from the cytosol to the endoplasmic reticulum. {ECO:0000250}.; . . medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;bladder;pineal gland;brain;unclassifiable (Anatomical System);heart;pineal body;pharynx;blood;lens;breast;lung;macula lutea;visual apparatus;liver;kidney; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.05521 . 1.063778722 91.58410002 653.74481 5.13028 GSG1L 0.541032304996425 0.455837608635666 0.00313008636790887 GSG1-like FUNCTION: As a component of the inner core of AMPAR complex, modifies AMPA receptor (AMPAR) gating. {ECO:0000250}.; . . . . 0.14757 . . . 57.52801 1.53022 GSG1L2 . . . GSG1-like 2 . . . . . . . . . . . GSG2 0.0511317633316248 0.944345649816811 0.00452258685156416 germ cell associated 2 (haspin) FUNCTION: Serine/threonine-protein kinase that phosphorylates histone H3 at 'Ser-3' (H3T3ph) during mitosis. This positions and activates AURKB and other components of the chromosomal passenger complex (CPC) at centromeres to ensure proper chromatid cohesion, metaphase alignment and normal progression through the cell cycle. {ECO:0000269|PubMed:11228240, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:17084365, ECO:0000269|PubMed:20705812, ECO:0000269|PubMed:20929775}.; . TISSUE SPECIFICITY: Strongly expressed in testis. Also present in thymus and bone marrow and low levels observed in prostate, intestine, lung, spleen and lymph node. Expressed in fetal skin, liver, kidney and small intestine and also in proliferating but not non-proliferating cell lines. {ECO:0000269|PubMed:11228240, ECO:0000269|PubMed:11311556}.; unclassifiable (Anatomical System);lymph node;liver;hypopharynx;testis;colon;head and neck;germinal center;mammary gland;stomach;thymus; . 0.44479 0.20004 0.159856957 64.91507431 1190.27323 6.54135 GSK3A 0.997436755748489 0.00256313924388052 1.05007630698942e-07 glycogen synthase kinase 3 alpha FUNCTION: Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), CTNNB1/beta-catenin, APC and AXIN1. Requires primed phosphorylation of the majority of its substrates. Contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. Regulates glycogen metabolism in liver, but not in muscle. May also mediate the development of insulin resistance by regulating activation of transcription factors. In Wnt signaling, regulates the level and transcriptional activity of nuclear CTNNB1/beta-catenin. Facilitates amyloid precursor protein (APP) processing and the generation of APP-derived amyloid plaques found in Alzheimer disease. May be involved in the regulation of replication in pancreatic beta-cells. Is necessary for the establishment of neuronal polarity and axon outgrowth. Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation. {ECO:0000269|PubMed:12761548, ECO:0000269|PubMed:17229088}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;temporal lobe;globus pallidus;ciliary ganglion;pons;atrioventricular node;skeletal muscle;cerebellum; 0.45002 0.81977 -0.317668748 31.45789101 4.65623 0.16705 GSK3B 0.998731142420546 0.00126885375387401 3.82557952729253e-09 glycogen synthase kinase 3 beta FUNCTION: Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1. Requires primed phosphorylation of the majority of its substrates. In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. May also mediate the development of insulin resistance by regulating activation of transcription factors. Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase. In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin. Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules. MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair. Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA). Negatively regulates replication in pancreatic beta-cells, resulting in apoptosis, loss of beta-cells and diabetes. Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation. Phosphorylates MUC1 in breast cancer cells, decreasing the interaction of MUC1 with CTNNB1/beta-catenin. Is necessary for the establishment of neuronal polarity and axon outgrowth. Phosphorylates MARK2, leading to inhibit its activity. Phosphorylates SIK1 at 'Thr-182', leading to sustain its activity. Phosphorylates ZC3HAV1 which enhances its antiviral activity. Phosphorylates SNAI1, leading to its BTRC-triggered ubiquitination and proteasomal degradation. Phosphorylates SFPQ at 'Thr-687' upon T-cell activation. Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and stabilizes it by protecting it from proteasomal degradation. Regulates the circadian clock via phosphorylation of the major clock components including ARNTL/BMAL1, CLOCK and PER2. Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal degradation. Phosphorylates ARNTL/BMAL1 at 'Ser-17' and 'Ser-21' and primes it for ubiquitination and proteasomal degradation. Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regulates its activity. Phosphorylates MYCN in neuroblastoma cells which may promote its degradation (PubMed:24391509). {ECO:0000269|PubMed:11430833, ECO:0000269|PubMed:12554650, ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:15448698, ECO:0000269|PubMed:15647282, ECO:0000269|PubMed:16484495, ECO:0000269|PubMed:18348280, ECO:0000269|PubMed:1846781, ECO:0000269|PubMed:19946213, ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:22514281, ECO:0000269|PubMed:24391509, ECO:0000269|PubMed:8397507, ECO:0000269|PubMed:9072970, ECO:0000269|PubMed:9819408}.; . TISSUE SPECIFICITY: Expressed in testis, thymus, prostate and ovary and weakly expressed in lung, brain and kidney. Colocalizes with EIF2AK2/PKR and TAU in the Alzheimer disease (AD) brain. {ECO:0000269|PubMed:21029237}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;hypothalamus;colon;blood;skin;retina;breast;uterus;pancreas;lung;bone;placenta;visual apparatus;testis;germinal center;brain;bladder;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;testis;pons;atrioventricular node; 0.97945 0.98572 -0.293801652 32.93819297 17.42742 0.61080 GSKIP 0.718816129437916 0.267327299410232 0.0138565711518516 GSK3B interacting protein . . TISSUE SPECIFICITY: Detected in heart, brain, placenta, liver, skeletal muscle, kidney, testis, lung and pancreas. {ECO:0000269|PubMed:16981698}.; . . 0.21483 0.11262 -0.031067188 51.03798066 2.864 0.10155 GSM1 . . . geniospasm 1 . . . . . . . . . . . GSN 3.18617651517055e-06 0.984630361052357 0.0153664527711276 gelsolin FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis. {ECO:0000269|PubMed:20393563}.; DISEASE: Amyloidosis 5 (AMYL5) [MIM:105120]: A hereditary generalized amyloidosis due to gelsolin amyloid deposition. It is typically characterized by cranial neuropathy and lattice corneal dystrophy. Most patients have modest involvement of internal organs, but severe systemic disease can develop in some individuals causing peripheral polyneuropathy, amyloid cardiomyopathy, and nephrotic syndrome leading to renal failure. {ECO:0000269|PubMed:1338910, ECO:0000269|PubMed:2176481}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Phagocytic cells, platelets, fibroblasts, nonmuscle cells, smooth and skeletal muscle cells.; myocardium;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;tongue;urinary;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;amnion;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;olfactory bulb;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.23446 0.75221 0.608069891 82.94409059 2029.53758 8.28926 GSN-AS1 . . . GSN antisense RNA 1 . . . . . . . . . . . GSPT1 0.951655491719969 0.0483386245060238 5.88377400723063e-06 G1 to S phase transition 1 FUNCTION: Involved in translation termination in response to the termination codons UAA, UAG and UGA. Stimulates the activity of ERF1. Involved in regulation of mammalian cell growth. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons.; . . . . 0.61675 0.14776 -0.029247611 51.40363293 3023.13945 10.43842 GSPT2 0.904748870176252 0.0944609673516125 0.00079016247213573 G1 to S phase transition 2 FUNCTION: Involved in translation termination in response to the termination codons UAA, UAG and UGA. May play a role as a potent stimulator of the release factor activity of ETF1. Exhibits GTPase activity, which is ribosome- and ETF1-dependent. May play a role in cell cycle progression. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. {ECO:0000269|PubMed:11524954, ECO:0000269|PubMed:15987998, ECO:0000269|PubMed:17562865}.; . TISSUE SPECIFICITY: Highly expressed in IUCC stage II colorectal cancer (CRC). {ECO:0000269|PubMed:16721809}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;oesophagus;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;spinal cord;muscle;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; superior cervical ganglion;medulla oblongata;testis;pons; 0.46371 0.11637 -0.073340031 48.11866006 39.09239 1.15900 GSR 0.012481213675682 0.979933676480082 0.00758510984423643 glutathione reductase FUNCTION: Maintains high levels of reduced glutathione in the cytosol.; . . salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;pituitary gland;brain;unclassifiable (Anatomical System);small intestine;cartilage;islets of Langerhans;urinary;breast;lung;placenta;liver;hypopharynx;spleen;head and neck;cervix;mammary gland;stomach; superior cervical ganglion;atrioventricular node; 0.15973 . -0.356299879 29.31115829 560.27629 4.80756 GSS 0.0225186832470012 0.976828618013099 0.000652698739899645 glutathione synthetase . DISEASE: Glutathione synthetase deficiency (GSS deficiency) [MIM:266130]: Severe form characterized by an increased rate of hemolysis and defective function of the central nervous system. {ECO:0000269|PubMed:8896573, ECO:0000269|PubMed:9215686}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Glutathione synthetase deficiency of erythrocytes (GLUSYNDE) [MIM:231900]: Mild form causing hemolytic anemia. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;synovium;larynx;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pineal body;muscle;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; superior cervical ganglion;tumor;testis;kidney;pons;trigeminal ganglion;skeletal muscle; 0.26630 0.32806 -0.556537043 19.72753008 71.54191 1.76080 GSTA1 0.0590105424594988 0.867804346960665 0.0731851105798358 glutathione S-transferase alpha 1 FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. {ECO:0000269|PubMed:20606271}.; . TISSUE SPECIFICITY: Liver.; unclassifiable (Anatomical System);medulla oblongata;cartilage;heart;ovary;islets of Langerhans;hypothalamus;adrenal cortex;colon;parathyroid;skin;uterus;prostate;whole body;lung;adrenal gland;nasopharynx;thyroid;placenta;liver;testis;spleen;kidney;pineal gland;mammary gland;stomach; testis - interstitial;superior cervical ganglion;fetal liver;testis - seminiferous tubule;trachea;adrenal gland;adrenal cortex;liver;testis;kidney; 0.05662 . -0.181750739 40.15687662 74.35516 1.80096 GSTA2 4.24100248085288e-08 0.0584354870514434 0.941564470538532 glutathione S-transferase alpha 2 FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.; . TISSUE SPECIFICITY: Liver.; . . 0.05834 . 0.951720429 90.06251474 230.94855 3.28576 GSTA3 0.0868631567505918 0.870776858576273 0.0423599846731354 glutathione S-transferase alpha 3 FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)- pregnene-3,20-dione, precursors to testosterone and progesterone, respectively. {ECO:0000269|PubMed:15595823, ECO:0000269|PubMed:20083122}.; . . placenta;testis;parathyroid; superior cervical ganglion;adrenal gland;placenta;adrenal cortex;pons;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.05888 . 0.595326758 82.66100495 489.16433 4.55254 GSTA4 0.0213022543085222 0.907400375906659 0.0712973697848188 glutathione S-transferase alpha 4 FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. This isozyme has a high catalytic efficiency with 4-hydroxyalkenals such as 4- hydroxynonenal (4-HNE). {ECO:0000269|PubMed:10329152, ECO:0000269|PubMed:20085333}.; . TISSUE SPECIFICITY: Expressed at a high level in brain, placenta, and skeletal muscle and much lower in lung and liver.; . . 0.15499 0.20866 -0.295622497 32.61972163 24.28731 0.79830 GSTA5 3.9842196790073e-09 0.0282955975417266 0.971704398474054 glutathione S-transferase alpha 5 . . TISSUE SPECIFICITY: Expression not detected.; liver; . 0.04631 0.09860 0.61555716 83.13871196 72.17726 1.77014 GSTA6P . . . glutathione S-transferase alpha 6, pseudogene . . . . . . . . . . . GSTA7P . . . glutathione S-transferase alpha 7, pseudogene . . . . . . . . . . . GSTA8P . . . glutathione S-transferase alpha 8, pseudogene . . . . . . . . . . . GSTA9P . . . glutathione S-transferase alpha 9, pseudogene . . . . . . . . . . . GSTA10P . . . glutathione S-transferase alpha 10, pseudogene . . . . . . . . . . . GSTA11P . . . glutathione S-transferase alpha 11, pseudogene . . . . . . . . . . . GSTA12P . . . glutathione S-transferase alpha 12, pseudogene . . . . . . . . . . . GSTCD 1.33356519642071e-07 0.81378722422979 0.18621264241369 glutathione S-transferase C-terminal domain containing . . TISSUE SPECIFICITY: Widely expressed in cell types relevant to airway function, including airway smooth muscle cells and epithelial cells. {ECO:0000269|PubMed:24058608}.; unclassifiable (Anatomical System);breast;uterus;ovary;islets of Langerhans;placenta;testis;colon;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.24599 0.94934 -0.314027422 31.9297004 89.32087 2.03117 GSTK1 1.10372350730423e-09 0.0256136214142914 0.974386377481985 glutathione S-transferase kappa 1 FUNCTION: Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB).; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:14742434}.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; testis - interstitial;liver;testis;kidney;whole blood; 0.11172 0.10034 0.305084559 72.22811984 34.76555 1.05952 GSTM1 0.345713720441091 0.640644622618512 0.0136416569403973 glutathione S-transferase mu 1 FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. {ECO:0000269|PubMed:16548513}.; . TISSUE SPECIFICITY: Liver (at protein level). {ECO:0000269|PubMed:7822249}.; unclassifiable (Anatomical System);cartilage;heart;ovary;tongue;hypothalamus;colon;blood;lens;skin;skeletal muscle;retina;breast;uterus;prostate;lung;endometrium;epididymis;thyroid;visual apparatus;iris;liver;testis;head and neck;brain;stomach; . 0.03081 0.48885 1.414757139 94.83958481 640.41901 5.08780 GSTM2 0.00890200357706731 0.936558283389817 0.0545397130331159 glutathione S-transferase mu 2 (muscle) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. {ECO:0000269|PubMed:16549767}.; . TISSUE SPECIFICITY: Muscle.; medulla oblongata;ovary;sympathetic chain;colon;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;lung;epididymis;placenta;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; . 0.17927 . -0.183570861 39.95046001 36.78516 1.10282 GSTM2P1 . . . glutathione S-transferase mu 2 (muscle) pseudogene 1 . . . . . . . . . . . GSTM3 0.00057258920556302 0.896292573024296 0.103134837770141 glutathione S-transferase mu 3 (brain) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers. {ECO:0000269|PubMed:10587441}.; . TISSUE SPECIFICITY: Testis and brain.; medulla oblongata;ovary;sympathetic chain;skin;retina;prostate;optic nerve;endometrium;thyroid;iris;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;breast;visual apparatus;macula lutea;alveolus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;atrium;cerebral cortex;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;placenta;hippocampus;kidney;stomach; subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;pons;kidney; 0.34422 0.34630 0.459411326 78.28497287 372.71249 4.07323 GSTM3P1 . . . glutathione S-transferase mu 3 pseudogene 1 . . . . . . . . . . . GSTM3P2 . . . glutathione S-transferase mu 3 pseudogene 2 . . . . . . . . . . . GSTM4 0.000917344712640999 0.801666001838896 0.197416653448463 glutathione S-transferase mu 4 FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Active on 1- chloro-2,4-dinitrobenzene.; . TISSUE SPECIFICITY: Expressed in a wide variety of tissues.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;bone;pituitary gland;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach; whole brain;dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13696 0.09566 1.282454727 93.71313989 57.80607 1.53622 GSTM5 0.000214167029024381 0.736990280528081 0.262795552442894 glutathione S-transferase mu 5 FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. {ECO:0000269|PubMed:10587441}.; . . unclassifiable (Anatomical System);heart;cartilage;sympathetic chain;lens;skin;uterus;prostate;lung;frontal lobe;thyroid;hippocampus;testis;brain;cerebellum; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04393 . 0.905808022 89.4373673 506.91274 4.62021 GSTM5P1 . . . glutathione S-transferase mu 5 pseudogene 1 . . . . . . . . . . . GSTO1 0.0150378430797143 0.876826240677468 0.108135916242818 glutathione S-transferase omega 1 FUNCTION: Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid. {ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:11511179, ECO:0000269|PubMed:17226937, ECO:0000269|PubMed:18028863, ECO:0000269|PubMed:21106529}.; . TISSUE SPECIFICITY: Ubiquitous. Highest expression in liver, pancreas, skeletal muscle, spleen, thymus, colon, blood leukocyte and heart. Lowest expression in brain, placenta and lung. {ECO:0000269|PubMed:10783391}.; . . 0.10921 0.34026 0.77170517 87.00754895 2228.72518 8.69885 GSTO2 1.66971146764309e-07 0.127061951497841 0.872937881531012 glutathione S-transferase omega 2 FUNCTION: Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA). {ECO:0000269|PubMed:15970797}.; . TISSUE SPECIFICITY: Expressed in a range of tissues, including the liver, kidney, skeletal muscle and prostate. Strongest expression in the testis. {ECO:0000269|PubMed:12618591}.; medulla oblongata;heart;islets of Langerhans;colon;parathyroid;skin;uterus;breast;pancreas;prostate;lung;trachea;bone;visual apparatus;liver;testis;spleen;brain; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; 0.08017 0.25921 -0.005381972 53.50908233 1186.2911 6.53235 GSTO3P . . . glutathione S-transferase omega 3, pseudogene . . . . . . . . . . . GSTP1 0.115024062658021 0.857696189815521 0.0272797475264577 glutathione S-transferase pi 1 FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration. {ECO:0000269|PubMed:21668448}.; . . . . 0.20152 0.75268 -0.093566408 46.7386176 940.3042 5.94531 GSTP1P1 . . . glutathione S-transferase pi 1 pseudogene 1 . . . . . . . . . . . GSTT1 0.00166897825306788 0.700695115502823 0.297635906244109 glutathione S-transferase theta 1 FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Acts on 1,2- epoxy-3-(4-nitrophenoxy)propane, phenethylisothiocyanate 4- nitrobenzyl chloride and 4-nitrophenethyl bromide. Displays glutathione peroxidase activity with cumene hydroperoxide. {ECO:0000269|PubMed:16298388, ECO:0000269|PubMed:20097269}.; . TISSUE SPECIFICITY: Found in erythrocyte. Expressed at low levels in liver. In lung, expressed at low levels in Clara cells and ciliated cells at the alveolar/bronchiolar junction. Absent from epithelial cells of larger bronchioles. {ECO:0000269|PubMed:8761485}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;optic nerve;synovium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;cartilage;tongue;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;greater omentum;breast;lung;cornea;epididymis;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.23736 0.55232 0.725794416 85.98136353 406.29444 4.22562 GSTT1-AS1 . . . GSTT1 antisense RNA 1 . . . . . . . . . . . GSTT2 0.2267348291534 0.646807501125444 0.126457669721157 glutathione S-transferase theta 2 (gene/pseudogene) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a sulfatase activity.; . TISSUE SPECIFICITY: Expressed at low levels in liver. In lung, expressed at low levels in ciliated bronchiolar cells, alveolar macrophages and alveolar type II cells. {ECO:0000269|PubMed:8761485}.; unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;colon;parathyroid;skin;retina;uterus;prostate;whole body;lung;endometrium;adrenal gland;placenta;hippocampus;liver;spleen;cervix;kidney;brain;stomach;thymus; . 0.10039 0.08341 . . 1784.90752 7.79976 GSTT2B 0.520153497085797 0.415352084362014 0.0644944185521892 glutathione S-transferase theta 2B (gene/pseudogene) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a sulfatase activity.; . TISSUE SPECIFICITY: Expressed at low levels in liver. In lung, expressed at low levels in ciliated bronchiolar cells, alveolar macrophages and alveolar type II cells. {ECO:0000269|PubMed:8761485}.; unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;colon;parathyroid;skin;retina;uterus;prostate;whole body;lung;endometrium;adrenal gland;placenta;hippocampus;liver;spleen;cervix;kidney;brain;stomach;thymus; . 0.14155 0.10575 . . 483.93189 4.52853 GSTTP1 . . . glutathione S-transferase theta pseudogene 1 . . . . . . 0.10546 . . . . GSTTP2 . . . glutathione S-transferase theta pseudogene 2 . . . . . . . . . . . GSTZ1 1.06852258414363e-05 0.571416641396212 0.428572673377947 glutathione S-transferase zeta 1 FUNCTION: Bifunctional enzyme showing minimal glutathione- conjugating activity with ethacrynic acid and 7-chloro-4- nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. Has also low glutathione peroxidase activity with T- butyl and cumene hydroperoxides. Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid. {ECO:0000269|PubMed:10739172}.; . TISSUE SPECIFICITY: Mostly expressed in liver followed by kidney, skeletal muscle and brain. Also expressed in melanocytes, synovium, placenta, breast and fetal liver and heart.; lymphoreticular;ovary;salivary gland;colon;parathyroid;choroid;skin;uterus;prostate;endometrium;synovium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;placenta;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;liver;testis; 0.17491 0.30537 0.949904335 90.00943619 3700.05099 11.85814 GSX1 0.0795564103198462 0.753485272534219 0.166958317145935 GS homeobox 1 FUNCTION: Probable transcription factor that binds to the DNA sequence 5'-GC[TA][AC]ATTA[GA]-3'. Activates the transcription of the GHRH gene. Plays an important role in pituitary development.; . . . . 0.22044 0.15473 . . 62.32946 1.61184 GSX2 0.14870134534922 0.777813987177756 0.0734846674730232 GS homeobox 2 FUNCTION: During telencephalic development, causes ventralization of pallial progenitors and, depending on the developmental stage, specifies different neuronal fates. At early stages, necessary and sufficient to correctly specify the ventral lateral ganglionic eminence (LGE) and its major derivatives, the striatal projection neurons. At later stages, may specify LGE progenitors toward dorsal LGE fates, including olfactory bulb interneurons (By similarity). Transcription factor that binds 5'-CNAATTAG-3' DNA sequence. {ECO:0000250|UniProtKB:P31316}.; . . unclassifiable (Anatomical System);lung;testis;germinal center;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.39555 0.13685 . . 43.48507 1.25516 GTDC1 2.40902542593717e-10 0.073202360258519 0.926797639500578 glycosyltransferase like domain containing 1 . . TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the lung, brain, spleen, testis, placenta. ovary, pancreas, spleen and peripheral blood leukocytes. Expressed at low level in the colon, small intestine, kidney, skeletal muscle and thymus. Expressed at high level in colon adenocarcinoma. {ECO:0000269|PubMed:15068588, ECO:0000269|PubMed:21821951}.; ovary;umbilical cord;parathyroid;skin;bone marrow;uterus;whole body;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;liver;spleen;head and neck;mammary gland;aorta; dorsal root ganglion;amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.15283 0.07494 -0.176292081 40.56381222 263.31779 3.48127 GTF2A1 0.956765261830397 0.0432127775712127 2.19605983898954e-05 general transcription factor IIA 1 FUNCTION: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity. {ECO:0000269|PubMed:11030333, ECO:0000269|PubMed:16537915}.; . . unclassifiable (Anatomical System);breast;lung;frontal lobe;placenta;visual apparatus;testis;blood;germinal center;brain;skeletal muscle;thymus; dorsal root ganglion;uterus corpus;testis - interstitial;superior cervical ganglion;heart;skeletal muscle; 0.81592 0.17821 -0.185391282 39.67916962 12.41878 0.45047 GTF2A1L 5.65246891903056e-07 0.423681770815733 0.576317663937375 general transcription factor IIA 1 like FUNCTION: May function as a testis specific transcription factor. Binds DNA in conjunction with GTF2A2 and TBP (the TATA-binding protein) and together with GTF2A2, allows mRNA transcription. {ECO:0000269|PubMed:10364255}.; . TISSUE SPECIFICITY: Testis specific. Detected in adult testis mostly in round and elongating spermatids (at protein level). Detected in testis. {ECO:0000269|PubMed:10364255, ECO:0000269|PubMed:16525715}.; . . . 0.10362 -0.044015879 50.44821892 0.74258 0.01290 GTF2A2 0.386341515138839 0.570352779089421 0.0433057057717403 general transcription factor IIA 2 FUNCTION: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity. {ECO:0000269|PubMed:11030333}.; . . medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;spinal cord;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;hypothalamus;oral cavity;muscle;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; . 0.32479 0.16574 0.057118534 57.99716914 29.96889 0.95701 GTF2B 0.489078694212667 0.509959058025759 0.000962247761574412 general transcription factor IIB FUNCTION: General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II.; . . . . 0.92672 0.35026 0.103030231 61.2762444 13.6013 0.49429 GTF2E1 0.902579885844598 0.0972479020388318 0.000172212116569775 general transcription factor IIE subunit 1 FUNCTION: Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase.; . . unclassifiable (Anatomical System);heart;tongue;skeletal muscle;skin;retina;uterus;whole body;thyroid;hippocampus;testis;head and neck;germinal center;kidney;brain; superior cervical ganglion;testis;ciliary ganglion;parietal lobe; 0.75331 0.18434 1.306318795 93.99622552 1675.73581 7.55145 GTF2E2 0.00866855235922082 0.978572984500916 0.0127584631398631 general transcription factor IIE subunit 2 FUNCTION: Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node; 0.63363 0.14795 0.060756528 58.52795471 29.09445 0.93052 GTF2F1 0.0287352714286824 0.969035607942689 0.0022291206286283 general transcription factor IIF subunit 1 FUNCTION: TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. {ECO:0000269|PubMed:10428810}.; . . . . 0.31407 0.12174 -1.195919584 5.832743572 81.00123 1.90437 GTF2F2 0.0252302317679079 0.961733409885725 0.0130363583463675 general transcription factor IIF subunit 2 FUNCTION: TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. This subunit shows ATP-dependent DNA- helicase activity. {ECO:0000269|PubMed:2477704}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;islets of Langerhans;pharynx;blood;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;skeletal muscle; 0.15957 0.11833 -0.163345027 41.24793583 12.47447 0.45368 GTF2F2P1 . . . general transcription factor IIF subunit 2 pseudogene 1 . . . . . . . . . . . GTF2F2P2 . . . general transcription factor IIF subunit 2 pseudogene 2 . . . . . . . . . . . GTF2H1 0.995912255857913 0.00408773071059165 1.34314949544005e-08 general transcription factor IIH subunit 1 FUNCTION: Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II.; . . lymphoreticular;smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;atrium;whole body;cochlea;endometrium;bone;testis;amniotic fluid;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;mesenchyma;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;testis - interstitial;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;testis;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.90623 0.15878 -0.381986487 27.68931352 65.62646 1.66885 GTF2H2 0.724561788823269 0.262351904641985 0.0130863065347458 general transcription factor IIH subunit 2 FUNCTION: Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. The N-terminus interacts with and regulates XPD whereas an intact C- terminus is required for a successful escape of RNAP II form the promoter.; . TISSUE SPECIFICITY: Widely expressed, with higher expression in skeletal muscle.; ovary;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;pons;trigeminal ganglion; . 0.17563 . . 20.14031 0.68894 GTF2H2B . . . general transcription factor IIH subunit 2B (pseudogene) . . . . . . 0.10903 . . . . GTF2H2C 0.89190553150668 0.10700176093631 0.00109270755701008 GTF2H2 family member C FUNCTION: Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. {ECO:0000250}.; . . . . . 0.10903 . . 29.88171 0.95369 GTF2H2C_2 . . . GTF2H2 family member C, copy 2 FUNCTION: Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. {ECO:0000250}.; . . . . . 0.10903 . . . . GTF2H3 1.59171384172212e-05 0.865467582327924 0.134516500533659 general transcription factor IIH subunit 3 FUNCTION: Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. Anchors XPB.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;heart;small intestine;hypothalamus;pharynx;blood;skeletal muscle;breast;lung;mesenchyma;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach; superior cervical ganglion;subthalamic nucleus;temporal lobe;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.29679 . -0.205617011 38.57631517 31.3121 0.98757 GTF2H4 0.25803488725879 0.741719348047253 0.000245764693957563 general transcription factor IIH subunit 4 FUNCTION: Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II.; . . lymphoreticular;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;duodenum;alveolus;liver;spleen;head and neck;kidney;stomach; . 0.26675 0.12378 -0.492218069 22.35786742 49.60165 1.37906 GTF2H5 0.0468099786233029 0.677353349051733 0.275836672324964 general transcription factor IIH subunit 5 FUNCTION: Component of the TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. Necessary for the stability of the TFIIH complex and for the presence of normal levels of TFIIH in the cell. {ECO:0000269|PubMed:15220921}.; DISEASE: Trichothiodystrophy 3, photosensitive (TTD3) [MIM:616395]: A form of trichothiodystrophy, an autosomal recessive disease characterized by sulfur-deficient brittle hair and multisystem variable abnormalities. The spectrum of clinical features varies from mild disease with only hair involvement to severe disease with cutaneous, neurologic and profound developmental defects. Ichthyosis, intellectual and developmental disabilities, decreased fertility, abnormal characteristics at birth, ocular abnormalities, short stature, and infections are common manifestations. There are both photosensitive and non- photosensitive forms of the disorder. {ECO:0000269|PubMed:15220921}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.07711 0.18619 -0.075159878 47.78839349 4.78359 0.17398 GTF2I 0.999348689931056 0.000651309315872212 7.53072167677302e-10 general transcription factor IIi FUNCTION: Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C- FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box. Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation. {ECO:0000269|PubMed:10373551, ECO:0000269|PubMed:11373296, ECO:0000269|PubMed:16738337}.; DISEASE: Note=GTF2I is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of GTF2I may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease.; TISSUE SPECIFICITY: Ubiquitous. Isoform 1 is strongly expressed in fetal brain, weakly in adult brain, muscle, and lymphoblasts and is almost undetectable in other adult tissues, while the other isoforms are equally expressed in all adult tissues.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;bile duct;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;hypothalamus;spinal cord;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.44744 0.43572 . . 71.71526 1.76313 GTF2IP1 . . . general transcription factor IIi pseudogene 1 . . . . . . . . . . . GTF2IP2 . . . general transcription factor IIi pseudogene 2 . . . . . . . . . . . GTF2IP3 . . . general transcription factor IIi pseudogene 3 . . . . . . . . . . . GTF2IP4 . . . general transcription factor IIi pseudogene 4 . . . . . . . . . . . GTF2IP5 . . . general transcription factor IIi pseudogene 5 . . . . . . . . . . . GTF2IP6 . . . general transcription factor IIi pseudogene 6 . . . . . . . . . . . GTF2IP7 . . . general transcription factor IIi pseudogene 7 . . . . . . . . . . . GTF2IP8 . . . general transcription factor IIi pseudogene 8 . . . . . . . . . . . GTF2IP9 . . . general transcription factor IIi pseudogene 9 . . . . . . . . . . . GTF2IP10 . . . general transcription factor IIi pseudogene 10 . . . . . . . . . . . GTF2IP11 . . . general transcription factor IIi pseudogene 11 . . . . . . . . . . . GTF2IP12 . . . general transcription factor IIi pseudogene 12 . . . . . . . . . . . GTF2IP13 . . . general transcription factor IIi pseudogene 13 . . . . . . . . . . . GTF2IP14 . . . general transcription factor IIi pseudogene 14 . . . . . . . . . . . GTF2IP15 . . . general transcription factor IIi pseudogene 15 . . . . . . . . . . . GTF2IP16 . . . general transcription factor IIi pseudogene 16 . . . . . . . . . . . GTF2IP17 . . . general transcription factor IIi pseudogene 17 . . . . . . . . . . . GTF2IP18 . . . general transcription factor IIi pseudogene 18 . . . . . . . . . . . GTF2IP19 . . . general transcription factor IIi pseudogene 19 . . . . . . . . . . . GTF2IP20 . . . general transcription factor IIi pseudogene 20 . . . . . . . . . . . GTF2IP21 . . . general transcription factor IIi pseudogene 21 . . . . . . . . . . . GTF2IP22 . . . general transcription factor IIi pseudogene 22 . . . . . . . . . . . GTF2IP23 . . . general transcription factor IIi pseudogene 23 . . . . . . . . . . . GTF2IRD1 0.996434356913921 0.00356564300636788 7.97110670447281e-11 GTF2I repeat domain containing 1 FUNCTION: May be a transcription regulator involved in cell-cycle progression and skeletal muscle differentiation. May repress GTF2I transcriptional functions, by preventing its nuclear residency, or by inhibiting its transcriptional activation. May contribute to slow-twitch fiber type specificity during myogenesis and in regenerating muscles. Binds troponin I slow-muscle fiber enhancer (USE B1). Binds specifically and with high affinity to the EFG sequences derived from the early enhancer of HOXC8 (By similarity). {ECO:0000250, ECO:0000269|PubMed:11438732}.; DISEASE: Note=GTF2IRD1 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of GTF2IRD1 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease.; TISSUE SPECIFICITY: Highly expressed in adult skeletal muscle, heart, fibroblast, bone and fetal tissues. Expressed at lower levels in all other tissues tested.; ovary;salivary gland;colon;parathyroid;skin;retina;uterus;prostate;endometrium;synovium;larynx;thyroid;bone;testis;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;tongue;muscle;skeletal muscle;breast;pancreas;lung;visual apparatus;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;kidney;atrioventricular node;skeletal muscle; 0.34165 0.16024 -1.390744555 4.305260675 101.42808 2.18046 GTF2IRD1P1 . . . GTF2I repeat domain containing 1 pseudogene 1 . . . . . . . . . . . GTF2IRD2 . . . GTF2I repeat domain containing 2 . . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15100712}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;colon;skin;breast;prostate;pancreas;whole body;lung;placenta;alveolus;liver;testis;head and neck;kidney;brain; . . 0.12054 . . 846.3466 5.69102 GTF2IRD2B . . . GTF2I repeat domain containing 2B . . TISSUE SPECIFICITY: Ubiquitous.; unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;colon;skin;bone marrow;pancreas;prostate;lung;thyroid;bone;placenta;alveolus;liver;testis;head and neck;kidney;brain; . 0.16608 0.08600 . . 102.51624 2.18891 GTF2IRD2P1 . . . GTF2I repeat domain containing 2 pseudogene 1 . . . . . 0.11287 0.08600 . . . . GTF3A . . . general transcription factor IIIA FUNCTION: Interacts with the internal control region (ICR) of approximately 50 bases within the 5S RNA genes, is required for correct transcription of these genes by RNA polymerase III. Also binds the transcribed 5S RNA's. May initiate transcription of the 5S ribosomal RNA gene and maintain the stability of transcription of other genes.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.03343 0.11761 0.43736446 77.56546355 812.31719 5.60623 GTF3AP1 . . . general transcription factor IIIA pseudogene 1 . . . . . . . . . . . GTF3AP2 . . . general transcription factor IIIA pseudogene 2 . . . . . . . . . . . GTF3AP3 . . . general transcription factor IIIA pseudogene 3 . . . . . . . . . . . GTF3AP4 . . . general transcription factor IIIA pseudogene 4 . . . . . . . . . . . GTF3AP5 . . . general transcription factor IIIA pseudogene 5 . . . . . . . . . . . GTF3AP6 . . . general transcription factor IIIA pseudogene 6 . . . . . . . . . . . GTF3C1 0.999995618775871 4.38122412925123e-06 1.08162320352085e-20 general transcription factor IIIC subunit 1 FUNCTION: Required for RNA polymerase III-mediated transcription. Component of TFIIIC that initiates transcription complex assembly on tRNA and is required for transcription of 5S rRNA and other stable nuclear and cytoplasmic RNAs. Binds to the box B promoter element.; . . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;pineal body;spinal cord;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; prostate;testis - seminiferous tubule;thyroid;prefrontal cortex;testis;cingulate cortex;skeletal muscle; 0.48876 0.28603 -1.710755469 2.506487379 930.46672 5.91834 GTF3C2 0.999786435918561 0.000213564081355315 8.34365839210673e-14 general transcription factor IIIC subunit 2 FUNCTION: Required for RNA polymerase III-mediated transcription. Component of TFIIIC that initiates transcription complex assembly on tRNA and is required for transcription of 5S rRNA and other stable nuclear and cytoplasmic RNAs. May play a direct role in stabilizing interactions of TFIIIC2 with TFIIIC1.; . . myocardium;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach; atrioventricular node;trigeminal ganglion;skeletal muscle; 0.55936 0.23478 -1.39618256 4.222694032 130.42898 2.48710 GTF3C2-AS1 . . . GTF3C2 antisense RNA 1 . . . . . . . . . . . GTF3C3 5.35810483574069e-06 0.999685126399782 0.000309515495382427 general transcription factor IIIC subunit 3 FUNCTION: Involved in RNA polymerase III-mediated transcription. Integral, tightly associated component of the DNA-binding TFIIIC2 subcomplex that directly binds tRNA and virus-associated RNA promoters.; . . smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;gum;thyroid;germinal center;bladder;brain;gall bladder;amygdala;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;aorta;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.34288 0.24605 -0.422438699 25.64284029 26.74564 0.86554 GTF3C4 0.0149762555569875 0.979195682393008 0.00582806205000438 general transcription factor IIIC subunit 4 FUNCTION: Essential for RNA polymerase III to make a number of small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin. Has histone acetyltransferase activity (HAT) with unique specificity for free and nucleosomal H3. May cooperate with GTF3C5 in facilitating the recruitment of TFIIIB and RNA polymerase through direct interactions with BRF1, POLR3C and POLR3F. May be localized close to the A box.; . . . . 0.15360 0.24522 -0.201976964 38.98325077 70.80891 1.75149 GTF3C5 0.00274002234197739 0.994420969191169 0.0028390084668534 general transcription factor IIIC subunit 5 FUNCTION: Involved in RNA polymerase III-mediated transcription. Integral, tightly associated component of the DNA-binding TFIIIC2 subcomplex that directly binds tRNA and virus-associated RNA promoters.; . . colon;fovea centralis;choroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; trigeminal ganglion;skeletal muscle; 0.12598 0.10871 -1.107723888 6.829440906 86.1619 1.98218 GTF3C6 0.0117194903947077 0.846364330767219 0.141916178838074 general transcription factor IIIC subunit 6 FUNCTION: Involved in RNA polymerase III-mediated transcription. Integral, tightly associated component of the DNA-binding TFIIIC2 subcomplex that directly binds tRNA and virus-associated RNA promoters. {ECO:0000269|PubMed:17409385}.; . . . . 0.08301 0.09249 0.169169615 65.33380514 211.15735 3.13418 GTPBP1 0.996188561880383 0.00381138216815993 5.59514568261658e-08 GTP binding protein 1 FUNCTION: Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity (By similarity). {ECO:0000250}.; . . ovary;sympathetic chain;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;muscle;blood;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;kidney;cerebellum; superior cervical ganglion;adrenal cortex;ciliary ganglion;trigeminal ganglion; 0.30257 0.17298 -0.778825328 12.88039632 38.04609 1.13038 GTPBP2 0.884778920255619 0.115218860825659 2.21891872213269e-06 GTP binding protein 2 . . TISSUE SPECIFICITY: Predominantly expressed in thymus, spleen, and testis. Expressed at lower levels in brain, lung, kidney, and ovary. {ECO:0000269|PubMed:11054535}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; testis; 0.35793 0.13486 -0.426079032 25.36565228 137.66196 2.55455 GTPBP3 0.0447520916377848 0.949695706004744 0.00555220235747137 GTP binding protein 3 (mitochondrial) FUNCTION: GTPase involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs. {ECO:0000305}.; DISEASE: Combined oxidative phosphorylation deficiency 23 (COXPD23) [MIM:616198]: An autosomal recessive mitochondrial disorder characterized by hypertrophic cardiomyopathy and/or neurologic symptoms with onset in early childhood. Disease features include hypertrophic cardiomyopathy, hypotonia, delayed psychomotor development, lactic acidosis, impaired activities of respiratory complexes I and IV, and defective translation of mitochondrial proteins. Disease severity is variable, ranging from death in early infancy to survival into the second decade of life. {ECO:0000269|PubMed:25434004}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12370316}.; ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;whole body;frontal lobe;endometrium;bone;testis;germinal center;artery;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;spinal cord;blood;breast;bile duct;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;macula lutea;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;aorta; amygdala;dorsal root ganglion;superior cervical ganglion;tumor;white blood cells;atrioventricular node;pons;skin;skeletal muscle;subthalamic nucleus;prefrontal cortex;appendix;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.14469 0.16683 0.222355725 68.44184949 670.17891 5.17538 GTPBP4 0.999865566823629 0.000134433160253795 1.61171110804036e-11 GTP binding protein 4 FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;pharynx;blood;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;testis;ciliary ganglion;skeletal muscle; 0.91550 0.10297 0.20394914 67.45694739 585.95145 4.91020 GTPBP6 . . . GTP binding protein 6 (putative) . . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9466997}.; lymphoreticular;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;thyroid;bone;testis;brain;pineal gland;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;skeletal muscle;pancreas;lung;placenta;alveolus;cervix;kidney;mammary gland;stomach; superior cervical ganglion;heart;liver;pons;trigeminal ganglion;skeletal muscle; 0.12869 . . . 708.06292 5.28421 GTPBP8 2.88123347250605e-06 0.319126287704591 0.680870831061936 GTP-binding protein 8 (putative) . . . unclassifiable (Anatomical System);lung;whole body;ovary;islets of Langerhans;trabecular meshwork;bone;testis;kidney; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;trigeminal ganglion; 0.07867 0.09921 0.571462851 81.99457419 473.80032 4.50028 GTPBP10 0.13073148451219 0.864584974173262 0.00468354131454829 GTP-binding protein 10 (putative) FUNCTION: May be involved in the ribosome maturation process. Complements an ObgE(CgtA) function in E.coli ribosome maturation. Plays a role of GTPase in vitro. When missing, disorganization of the nuceleolar architecture is observed. {ECO:0000269|PubMed:17054726}.; . . ovary;salivary gland;intestine;colon;choroid;fovea centralis;skin;retina;uterus;prostate;whole body;optic nerve;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;visual apparatus;macula lutea;liver;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.13590 0.09790 1.084010791 91.8141071 723.95938 5.34080 GTS . . . Gilles de la Tourette syndrome . . . . . . . . . . . GTSCR1 . . . Gilles de la Tourette syndrome chromosome region, candidate 1 (non-protein coding) . . . . . . . . . 263.8848 3.48523 GTSE1 6.90346708786844e-06 0.900506170993661 0.099486925539251 G2 and S-phase expressed 1 FUNCTION: May be involved in p53-induced cell cycle arrest in G2/M phase by interfering with microtubule rearrangements that are required to enter mitosis. Overexpression delays G2/M phase progression.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);muscle;adrenal cortex;pharynx;blood;bile duct;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;bone marrow; 0.10167 0.06860 0.854236942 88.51144138 773.1469 5.50331 GTSE1-AS1 . . . GTSE1 antisense RNA 1 (head to head) . . . . . . . . . . . GTSF1 0.513379498300112 0.482739622194702 0.00388087950518642 gametocyte specific factor 1 FUNCTION: Required for spermatogenesis and is involved in the suppression of retrotransposon transcription in male germ cells. {ECO:0000250|UniProtKB:Q9DAN6}.; . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;uterus;prostate;lung;nasopharynx;bone;thyroid;placenta;visual apparatus;liver;testis;head and neck;spleen;germinal center;kidney;brain;bladder; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion; 0.47837 0.11262 -0.119252484 44.53880632 20.3661 0.69467 GTSF1L 0.0573625002264625 0.710893216103402 0.231744283670135 gametocyte specific factor 1-like . . . . . 0.13580 . 0.881944684 89.02453409 163.0868 2.78825 GUCA1A 0.00991832803266624 0.822086106634332 0.167995565333002 guanylate cyclase activator 1A FUNCTION: Stimulates guanylyl cyclase 1 (GC1) when free calcium ions concentration is low and inhibits GC1 when free calcium ions concentration is elevated. This Ca(2+)-sensitive regulation of GC is a key event in recovery of the dark state of rod photoreceptors following light exposure.; . TISSUE SPECIFICITY: Retina; cone outer and inner segments, in particular, in disk membrane regions, and to a lesser extent rod inner and outer segments.; unclassifiable (Anatomical System);medulla oblongata;pineal body;choroid;fovea centralis;lens;retina;optic nerve;lung;placenta;visual apparatus;macula lutea;testis;pineal gland; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;temporal lobe;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.31117 0.18332 -0.05129383 49.75819769 50.44741 1.39740 GUCA1B 0.00199506191376467 0.737261345896465 0.26074359218977 guanylate cyclase activator 1B FUNCTION: Stimulates guanylyl cyclase 1 (GC1) and GC2 when free calcium ions concentration is low, and GC1 and GC2 when free calcium ions concentration is elevated. This Ca(2+)-sensitive regulation of GC is a key event in recovery of the dark state of rod photoreceptors following light exposure.; . TISSUE SPECIFICITY: Retina. Cones and rod.; unclassifiable (Anatomical System);prostate;optic nerve;lung;whole body;cartilage;synovium;macula lutea;fovea centralis;skeletal muscle;retina;thymus; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.09416 0.17821 0.038710339 56.92380278 86.07498 1.98078 GUCA1C 0.000632586350938465 0.492244137942482 0.507123275706579 guanylate cyclase activator 1C FUNCTION: Stimulates guanylyl cyclase 1 (GC1) and GC2 when free calcium ions concentration is low and inhibits guanylyl cyclases when free calcium ions concentration is elevated. This Ca(2+)- sensitive regulation of guanylyl cyclase (GC) is a key event in recovery of the dark state of rod photoreceptors following light exposure.; . TISSUE SPECIFICITY: Retina.; unclassifiable (Anatomical System);hypothalamus;pineal body;macula lutea;testis;blood;fovea centralis;retina; . 0.04671 0.10392 0.994001092 90.5579146 3904.99392 12.34420 GUCA2A 0.00607225846311219 0.498168118696098 0.49575962284079 guanylate cyclase activator 2A FUNCTION: Endogenous activator of intestinal guanylate cyclase. It stimulates this enzyme through the same receptor binding region as the heat-stable enterotoxins.; . TISSUE SPECIFICITY: Highly expressed in ileum and colon. Found in plasma.; unclassifiable (Anatomical System);colon;skeletal muscle; dorsal root ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.07925 0.17531 0.193034296 66.82000472 2662.47848 9.70348 GUCA2B 0.707935696188502 0.276665435618812 0.0153988681926863 guanylate cyclase activator 2B FUNCTION: Endogenous activator of intestinal guanylate cyclase. It stimulates this enzyme through the same receptor binding region as the heat-stable enterotoxins. May be a potent physiological regulator of intestinal fluid and electrolyte transport. May be an autocrine/paracrine regulator of intestinal salt and water transport.; . TISSUE SPECIFICITY: Stomach and intestine.; . . 0.52902 0.15937 0.237127192 68.98443029 23.08443 0.77037 GUCD1 0.0166878645052519 0.887425217476971 0.0958869180177775 guanylyl cyclase domain containing 1 . . . . . 0.22702 . -0.494039303 22.09247464 17.29726 0.60773 GUCY1A2 0.377257492585874 0.622649492459099 9.30149550265124e-05 guanylate cyclase 1, soluble, alpha 2 FUNCTION: Has guanylyl cyclase on binding to the beta-1 subunit.; . TISSUE SPECIFICITY: Isoform 1 is expressed in fetal brain, liver, colon, endothelium and testis. Isoform 2 is expressed only in liver, colon and endothelium.; uterus;lung;frontal lobe;ovary;heart;skin;skeletal muscle; superior cervical ganglion; 0.32989 0.13525 -1.045216355 7.661004954 25.81831 0.84013 GUCY1A3 1.41368686812155e-06 0.954271727389239 0.0457268589238933 guanylate cyclase 1, soluble, alpha 3 . . TISSUE SPECIFICITY: Detected in brain cortex and lung (at protein level). {ECO:0000269|PubMed:1352257}.; smooth muscle;ovary;colon;fovea centralis;skin;bone marrow;retina;uterus;prostate;thyroid;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;breast;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;spleen;kidney;mammary gland;aorta;peripheral nerve; medulla oblongata;superior cervical ganglion;appendix;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.13292 0.14167 -0.997481928 8.47487615 199.89032 3.05449 GUCY1B2 . . . guanylate cyclase 1, soluble, beta 2 (pseudogene) . . . . . 0.13600 . . . . . GUCY1B3 0.000916633852893547 0.996303149830097 0.00278021631700976 guanylate cyclase 1, soluble, beta 3 FUNCTION: Mediates responses to nitric oxide (NO) by catalyzing the biosynthesis of the signaling molecule cGMP. {ECO:0000250|UniProtKB:P16068, ECO:0000269|PubMed:1352257}.; . TISSUE SPECIFICITY: Detected in brain cortex and cerebellum (at protein level). {ECO:0000269|PubMed:1352257}.; islets of Langerhans;colon;fovea centralis;choroid;lens;skeletal muscle;retina;pancreas;optic nerve;placenta;hippocampus;macula lutea;spleen;germinal center; amygdala;dorsal root ganglion;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.27150 0.13780 -0.558357437 19.54470394 41.67691 1.21444 GUCY2C 1.77521150622888e-18 0.275107033977408 0.724892966022592 guanylate cyclase 2C FUNCTION: Receptor for the E.coli heat-stable enterotoxin (E.coli enterotoxin markedly stimulates the accumulation of cGMP in mammalian cells expressing GC-C). Also activated by the endogenous peptides guanylin and uroguanylin.; DISEASE: Diarrhea 6 (DIAR6) [MIM:614616]: A relatively mild, early-onset chronic diarrhea that may be associated with increased susceptibility to inflammatory bowel disease, small bowel obstruction, and esophagitis. {ECO:0000269|PubMed:22436048}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Meconium ileus (MECIL) [MIM:614665]: A condition characterized by a intestinal obstruction due to inspissated meconium in the distal ileum and cecum, which develops in utero and presents shortly after birth as a failure to pass meconium. Meconium ileus is a known clinical manifestation of cystic fibrosis. {ECO:0000269|PubMed:22521417}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);endometrium;islets of Langerhans;colon;kidney;skin;skeletal muscle;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle;skin; 0.43821 0.15328 -1.104093597 6.894314697 93.29327 2.07929 GUCY2D 0.000772456643664516 0.999081015572227 0.000146527784108289 guanylate cyclase 2D, membrane (retina-specific) FUNCTION: Probably plays a specific functional role in the rods and/or cones of photoreceptors. It may be the enzyme involved in the resynthesis of cGMP required for recovery of the dark state after phototransduction.; DISEASE: Cone-rod dystrophy 6 (CORD6) [MIM:601777]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. {ECO:0000269|PubMed:12552567, ECO:0000269|PubMed:15111605, ECO:0000269|PubMed:18332321, ECO:0000269|PubMed:18487367, ECO:0000269|PubMed:20517349, ECO:0000269|PubMed:21552474, ECO:0000269|PubMed:22194653, ECO:0000269|PubMed:23734073, ECO:0000269|PubMed:24480840, ECO:0000269|PubMed:9618177, ECO:0000269|PubMed:9683616}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Retina. Localized exclusively in the nuclei and inner segments of the rod and cone photoreceptor cells.; optic nerve;lung;macula lutea;fovea centralis;choroid;lens;retina; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.31296 0.10453 -1.366884746 4.505779665 3787.88145 12.06391 GUCY2EP . . . guanylate cyclase 2E, pseudogene . . . . . 0.37667 0.09522 . . . . GUCY2F 1.51652106018158e-05 0.99829336196557 0.00169147282382806 guanylate cyclase 2F, retinal FUNCTION: Probably plays a specific functional role in the rods and/or cones of photoreceptors. It may be the enzyme involved in the resynthesis of cGMP required for recovery of the dark state after phototransduction.; . TISSUE SPECIFICITY: Retina. Localized exclusively in the outer nuclear layer and inner segments of the rod and cone photoreceptor cells.; unclassifiable (Anatomical System);retina; superior cervical ganglion;fetal liver;trigeminal ganglion;skeletal muscle; 0.18122 0.16895 1.561617801 95.67114886 2443.21089 9.19149 GUCY2GP . . . guanylate cyclase 2G, pseudogene . . . . . . . . . . . GUF1 2.3678005877753e-11 0.644357600825359 0.355642399150963 GUF1 homolog, GTPase FUNCTION: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one- codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner. {ECO:0000255|HAMAP-Rule:MF_03137}.; . . ovary;developmental;colon;skin;retina;bone marrow;uterus;endometrium;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;blood;breast;lung;nasopharynx;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11190 0.24875 0.244401822 69.50931824 3123.60655 10.62924 GUK1 0.000100020035077034 0.573762217570585 0.426137762394338 guanylate kinase 1 FUNCTION: Essential for recycling GMP and indirectly, cGMP.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;gum;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;whole brain;occipital lobe;lung;temporal lobe;prefrontal cortex;caudate nucleus; 0.61935 0.39826 -0.957024976 9.088228356 85.40721 1.97028 GUK2 . . . guanylate kinase 2 . . . . . . . . . . . GULOP . . . gulonolactone (L-) oxidase, pseudogene . . . . . . . . . . . GULP1 0.677557750178314 0.321474382952885 0.000967866868801797 GULP, engulfment adaptor PTB domain containing 1 FUNCTION: May function as an adapter protein. Required for efficient phagocytosis of apoptotic cells. Modulates cellular glycosphingolipid and cholesterol transport. May play a role in the internalization and endosomal trafficking of various LRP1 ligands, such as PSAP. Increases cellular levels of GTP-bound ARF6. {ECO:0000269|PubMed:10574763, ECO:0000269|PubMed:10574771, ECO:0000269|PubMed:16497666, ECO:0000269|PubMed:17398097}.; . TISSUE SPECIFICITY: Widely expressed. Detected in macrophages, pancreas, kidney, skeletal muscle, heart, colon, intestine, lung, placenta and ovary. {ECO:0000269|PubMed:10574763}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;prostate;whole body;endometrium;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;spinal cord;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;placenta;testis;globus pallidus;atrioventricular node;skeletal muscle; 0.49297 0.14271 -0.229483771 36.86010852 19.84674 0.67647 GUSB 4.07005874224264e-05 0.997935443769257 0.00202385564332109 glucuronidase beta FUNCTION: Plays an important role in the degradation of dermatan and keratan sulfates.; DISEASE: Mucopolysaccharidosis 7 (MPS7) [MIM:253220]: An autosomal recessive lysosomal storage disease characterized by inability to degrade glucuronic acid-containing glycosaminoglycans. The phenotype is highly variable, ranging from severe lethal hydrops fetalis to mild forms with survival into adulthood. Most patients with the intermediate phenotype show hepatomegaly, skeletal anomalies, coarse facies, and variable degrees of mental impairment. {ECO:0000269|PubMed:12522561, ECO:0000269|PubMed:12859417, ECO:0000269|PubMed:1702266, ECO:0000269|PubMed:7573038, ECO:0000269|PubMed:7633414, ECO:0000269|PubMed:7680524, ECO:0000269|PubMed:8089138, ECO:0000269|PubMed:8111412, ECO:0000269|PubMed:8111413, ECO:0000269|PubMed:8644704, ECO:0000269|PubMed:8707294, ECO:0000269|PubMed:9099834, ECO:0000269|PubMed:9490302}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; placenta;liver;testis; 0.17330 . -0.821100135 11.88369899 22.67372 0.75898 GUSBP1 . . . glucuronidase, beta pseudogene 1 . . TISSUE SPECIFICITY: Ubiquitous.; . . 0.27254 . . . . . GUSBP2 . . . glucuronidase, beta pseudogene 2 . . . . . 0.09983 . . . . . GUSBP3 . . . glucuronidase, beta pseudogene 3 . . . . . . . . . . . GUSBP4 . . . glucuronidase, beta pseudogene 4 . . . . . . . . . . . GUSBP5 . . . glucuronidase, beta pseudogene 5 . . . . . . . . . . . GUSBP6 . . . glucuronidase, beta pseudogene 6 . . . . . . . . . . . GUSBP7 . . . glucuronidase, beta pseudogene 7 . . . . . . . . . . . GUSBP8 . . . glucuronidase, beta pseudogene 8 . . . . . . . . . . . GUSBP9 . . . glucuronidase, beta pseudogene 9 . . . . . . . . . . . GUSBP10 . . . glucuronidase, beta pseudogene 10 . . . . . . . . . . . GUSBP11 . . . glucuronidase, beta pseudogene 11 . . . . . . . . . . . GUSBP12 . . . glucuronidase, beta pseudogene 12 . . . . . . . . . . . GVINP1 . . . GTPase, very large interferon inducible pseudogene 1 . . . . . 0.48483 . . . . . GVINP2 . . . GTPase, very large interferon inducible pseudogene 2 . . . . . . . . . . . GVQW1 . . . GVQW motif containing 1 . . . . . . . . . 31.48689 0.99175 GVQW2 . . . GVQW motif containing 2 . . . . . . . . . . . GXYLT1 0.987483160840119 0.0125158132964534 1.02586342736548e-06 glucoside xylosyltransferase 1 FUNCTION: Glycosyltransferase which elongates the O-linked glucose attached to EGF-like repeats in the extracellular domain of Notch proteins by catalyzing the addition of xylose. {ECO:0000269|PubMed:19940119}.; . . unclassifiable (Anatomical System);placenta;testis; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skin; 0.21612 0.09174 -0.251530012 35.42108988 74.72132 1.80836 GXYLT1P1 . . . glucoside xylosyltransferase 1 pseudogene 1 . . . . . . . . . . . GXYLT1P2 . . . glucoside xylosyltransferase 1 pseudogene 2 . . . . . . . . . . . GXYLT1P3 . . . glucoside xylosyltransferase 1 pseudogene 3 . . . . . . . . . . . GXYLT1P4 . . . glucoside xylosyltransferase 1 pseudogene 4 . . . . . . . . . . . GXYLT1P5 . . . glucoside xylosyltransferase 1 pseudogene 5 . . . . . . . . . . . GXYLT1P6 . . . glucoside xylosyltransferase 1 pseudogene 6 . . . . . . . . . . . GXYLT2 1.76182494127584e-06 0.428309793424854 0.571688444750204 glucoside xylosyltransferase 2 FUNCTION: Glycosyltransferase which elongates the O-linked glucose attached to EGF-like repeats in the extracellular domain of Notch proteins by catalyzing the addition of xylose. {ECO:0000269|PubMed:19940119}.; . . . . 0.19686 . 0.062575634 58.74026893 339.44608 3.90793 GYG1 6.90635734321028e-07 0.463117900376276 0.53688140898799 glycogenin 1 FUNCTION: Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.; DISEASE: Glycogen storage disease 15 (GSD15) [MIM:613507]: A metabolic disorder resulting in muscle weakness, associated with the glycogen depletion in skeletal muscle, and cardiac arrhythmia, associated with the accumulation of abnormal storage material in the heart. The skeletal muscle shows a marked predominance of slow-twitch, oxidative muscle fibers and mitochondrial proliferation. {ECO:0000269|PubMed:20357282}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Polyglucosan body myopathy 2 (PGBM2) [MIM:616199]: A glycogen storage disease characterized by polyglucosan accumulation in muscle, and skeletal myopathy without cardiac involvement. Most patients manifest slowly progressive, hip girdle, shoulder girdle, and/or hand and leg muscle weakness. Polyglucosan contains abnormally long and poorly branched glucosyl chains and is variably resistant to digestion by alpha-amylase. {ECO:0000269|PubMed:25272951}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;atrium;oesophagus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle;bone marrow; 0.17298 0.16384 -0.069700724 48.54328851 98.90905 2.15121 GYG1P1 . . . glycogenin 1 pseudogene 1 . . . . . . . . . . . GYG1P2 . . . glycogenin 1 pseudogene 2 . . . . . . . . . . . GYG1P3 . . . glycogenin 1 pseudogene 3 . . . . . . . . . . . GYG2 1.70507761922303e-05 0.436900721057361 0.563082228166447 glycogenin 2 FUNCTION: Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.; . TISSUE SPECIFICITY: Expressed preferentially in liver, heart, and pancreas.; unclassifiable (Anatomical System);lymph node;heart;muscle;developmental;colon;fovea centralis;choroid;lens;skeletal muscle;skin;retina;lung;whole body;optic nerve;bone;macula lutea;liver;testis;spleen;kidney;mammary gland;brain;stomach; dorsal root ganglion;fetal liver;superior cervical ganglion;adipose tissue;spinal cord;atrioventricular node;skeletal muscle; 0.50173 . 0.198490371 67.30360934 468.74281 4.48403 GYG2-AS1 . . . GYG2 antisense RNA 1 . . . . . . . . . . . GYG2P1 . . . glycogenin 2 pseudogene 1 . . . breast;frontal lobe; . . . . . . . GYG2P2 . . . glycogenin 2 pseudogene 2 . . . . . . . . . . . GYLTL1B 8.27410616426457e-12 0.134518112428313 0.865481887563413 glycosyltransferase-like 1B FUNCTION: Bifunctional glycosyltransferase with both xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine- beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1). Phosphorylated O-mannosyl trisaccharid is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide. Has a higher activity toward alpha-dystroglycan than LARGE. {ECO:0000269|PubMed:15661757, ECO:0000269|PubMed:15752776, ECO:0000269|PubMed:25138275}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at high level in placenta, pancreas and kidney compared to LARGE. Not expressed in brain. {ECO:0000269|PubMed:15752776, ECO:0000269|PubMed:15958417}.; unclassifiable (Anatomical System);lymph node;ovary;tongue;urinary;colon;parathyroid;blood;skin;breast;uterus;prostate;pancreas;lung;endometrium;epididymis;larynx;bone;placenta;testis;head and neck;germinal center;kidney;stomach; . 0.26582 0.13929 -1.236390924 5.520169851 171.79216 2.85844 GYPA 0.0153129822194926 0.878762331941337 0.10592468583917 glycophorin A (MNS blood group) FUNCTION: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). {ECO:0000269|PubMed:10926825, ECO:0000269|PubMed:12813056, ECO:0000269|PubMed:14604989, ECO:0000269|PubMed:15331714, ECO:0000269|PubMed:19438409, ECO:0000269|PubMed:8009226}.; . . uterus;lung;heart;visual apparatus;liver;testis;spleen;blood;skin; fetal liver;superior cervical ganglion;subthalamic nucleus;temporal lobe;fetal lung;ciliary ganglion;trigeminal ganglion;skeletal muscle;bone marrow; 0.07262 . 0.393270925 76.04977589 304.01951 3.71514 GYPB 0.442245534937964 0.528174410380687 0.029580054681349 glycophorin B (MNS blood group) FUNCTION: This protein is a minor sialoglycoprotein in erythrocyte membranes.; . . liver;spleen;blood; fetal liver;superior cervical ganglion;subthalamic nucleus;temporal lobe;fetal lung;ciliary ganglion;trigeminal ganglion;skeletal muscle;bone marrow; 8.74545 . 1.683000003 96.35527247 334.29603 3.88506 GYPC 0.0138697690065761 0.672086617411939 0.314043613581485 glycophorin C (Gerbich blood group) FUNCTION: This protein is a minor sialoglycoprotein in human erythrocyte membranes. The blood group Gerbich antigens and receptors for Plasmodium falciparum merozoites are most likely located within the extracellular domain. Glycophorin-C plays an important role in regulating the stability of red cells.; . TISSUE SPECIFICITY: Glycophorin-C is expressed in erythrocytes. Glycophorin-D and IsoGPC are ubiquitously expressed. {ECO:0000269|PubMed:2349119}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;prostate;endometrium;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;blood;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;kidney;mammary gland;stomach; fetal liver;skeletal muscle;bone marrow; 0.03488 . 0.637604436 83.77565464 89.11228 2.02728 GYPE 0.00163909694496274 0.459167739973119 0.539193163081918 glycophorin E (MNS blood group) FUNCTION: This protein is a minor sialoglycoprotein in human erythrocyte membranes.; . TISSUE SPECIFICITY: Erythrocytes.; uterus;lung;heart;liver;testis;spleen;blood;skin; fetal liver;superior cervical ganglion;trigeminal ganglion;skin;parietal lobe; 0.35082 . -0.009020804 52.8544468 3.69628 0.13738 GYS1 0.00832267410134216 0.991561605006237 0.000115720892421095 glycogen synthase 1 FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan.; DISEASE: Muscle glycogen storage disease 0 (GSD0b) [MIM:611556]: Metabolic disorder characterized by fasting hypoglycemia presenting in infancy or early childhood. The role of muscle glycogen is to provide critical energy during bursts of activity and sustained muscle work. {ECO:0000269|PubMed:17928598}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pineal body;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;muscle;bile duct;pancreas;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus; superior cervical ganglion;heart;ciliary ganglion;atrioventricular node;skeletal muscle;cerebellum; 0.32455 0.72413 -1.175687564 5.974286388 259.39967 3.46151 GYS2 1.21631815172674e-14 0.146486871159475 0.853513128840512 glycogen synthase 2 FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan.; DISEASE: Glycogen storage disease 0 (GSD0) [MIM:240600]: A metabolic disorder characterized by fasting hypoglycemia presenting in infancy or early childhood, high blood ketones and low alanine and lactate concentrations. Although feeding relieves symptoms, it often results in postprandial hyperglycemia and hyperlactatemia. {ECO:0000269|PubMed:9691087}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);whole body;liver;spleen;kidney; superior cervical ganglion;fetal liver;liver; 0.13195 0.57267 0.316000233 72.80018872 423.9852 4.29969 GZF1 0.00788572311664667 0.977536311458363 0.0145779654249908 GDNF inducible zinc finger protein 1 FUNCTION: Transcriptional repressor. Binds the GZF1 responsive element (GRE) (consensus: 5'-TGCGCN[TG][CA]TATA-3'). May be regulating VSX2/HOX10 expression. {ECO:0000269|PubMed:14522971, ECO:0000269|PubMed:16049025}.; . TISSUE SPECIFICITY: Expressed in adult brain, heart, skeletal muscle, kidney and liver. Also detected in fetal brain and kidney, and at lower levels in fetal lung and liver. {ECO:0000269|PubMed:14522971}.; ovary;colon;parathyroid;skin;prostate;frontal lobe;cochlea;oesophagus;endometrium;testis;brain;gall bladder;tonsil;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;pineal body;lens;bile duct;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.14700 0.10999 -0.574945567 18.90186365 158.42232 2.74918 GZMA 3.24372441390747e-07 0.182907071475289 0.817092604152269 granzyme A FUNCTION: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent cell death with morphological features of apoptosis when delivered into the target cell through the immunological synapse. It cleaves after Lys or Arg. Cleaves APEX1 after 'Lys-31' and destroys its oxidative repair activity. Cleaves the nucleosome assembly protein SET after 'Lys-189', which disrupts its nucleosome assembly activity and allows the SET complex to translocate into the nucleus to nick and degrade the DNA. {ECO:0000269|PubMed:11555662, ECO:0000269|PubMed:12524539, ECO:0000269|PubMed:12628186, ECO:0000269|PubMed:16818237}.; . . unclassifiable (Anatomical System);cartilage;colon;blood;uterus;whole body;lung;endometrium;nasopharynx;placenta;testis;germinal center;kidney; superior cervical ganglion; 0.10463 0.06730 -0.22584292 37.32012267 183.49661 2.94025 GZMAP1 . . . granzyme A pseudogene 1 . . . . . . . . . . . GZMB 1.78750946382579e-06 0.431109670948733 0.568888541541804 granzyme B FUNCTION: This enzyme is necessary for target cell lysis in cell- mediated immune responses. It cleaves after Asp. Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. Cleaves caspase-3, -7, -9 and 10 to give rise to active enzymes mediating apoptosis.; . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;pancreas;lung;cornea;endometrium;thyroid;placenta;visual apparatus;alveolus;liver;spleen;kidney;brain;mammary gland;bladder;stomach; whole blood; 0.04747 0.52613 0.305084559 72.22811984 2042.02554 8.32989 GZMH 0.000213178163607732 0.497586565263182 0.502200256573211 granzyme H FUNCTION: Cytotoxic chymotrypsin-like serine protease with preference for bulky and aromatic residues at the P1 position and acidic residues at the P3' and P4' sites. Probably necessary for target cell lysis in cell-mediated immune responses. Participates in the antiviral response via direct cleavage of several proteins essential for viral replication. {ECO:0000269|PubMed:22156497, ECO:0000269|PubMed:23269243}.; . TISSUE SPECIFICITY: Constituvely expressed in NK cells. {ECO:0000269|PubMed:23269243}.; unclassifiable (Anatomical System);uterus;optic nerve;lung;nasopharynx;testis;colon;blood;kidney;brain; whole blood; 0.28899 0.13546 0.305084559 72.22811984 62.71334 1.61957 GZMK 0.000569041450124066 0.708942831957089 0.290488126592787 granzyme K . . TISSUE SPECIFICITY: Expressed in lung, spleen, thymus and peripheral blood leukocytes.; unclassifiable (Anatomical System);lymphoreticular;adrenal cortex;colon;parathyroid;pancreas;lung;adrenal gland;nasopharynx;thyroid;liver;testis;spleen;germinal center;kidney;pineal gland; . 0.10384 . -0.26993514 34.59542345 42.21234 1.22856 GZMM 0.00121003300542887 0.63177886796472 0.367011099029851 granzyme M FUNCTION: Cleaves peptide substrates after methionine, leucine, and norleucine. Physiological substrates include EZR, alpha- tubulins and the apoptosis inhibitor BIRC5/Survivin. Promotes caspase activation and subsequent apoptosis of target cells. {ECO:0000269|PubMed:18523284, ECO:0000269|PubMed:20406824}.; . TISSUE SPECIFICITY: Highly and constitutively expressed in activated natural killer (NK) cells. {ECO:0000269|PubMed:18523284}.; unclassifiable (Anatomical System);pancreas;colon;spleen;aorta; whole blood; 0.05690 . 0.97558591 90.37508846 160.5953 2.76678 H1F0 0.154802582065257 0.635588541354863 0.20960887657988 H1 histone family member 0 FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. The H1F0 histones are found in cells that are in terminal stages of differentiation or that have low rates of cell division.; . . ovary;colon;parathyroid;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;synovium;larynx;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;bile duct;pancreas;lung;cornea;mesenchyma;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.85024 0.20751 -0.053113545 49.38664779 8.17863 0.30157 H1FNT 0.00506623310388001 0.698519843031113 0.296413923865007 H1 histone family member N, testis specific FUNCTION: Essential for normal spermatogenesis and male fertility. Required for proper cell restructuring and DNA condensation during the elongation phase of spermiogenesis. Involved in the histone- protamine transition of sperm chromatin and the subsequent production of functional sperm. Binds both double-stranded and single-stranded DNA, ATP and protamine-1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:16533358}.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:16533358}.; unclassifiable (Anatomical System);medulla oblongata;lung;placenta;testis;kidney; . 0.04377 0.11120 0.461228372 78.46190139 1893.16801 7.99963 H1FOO 0.398598145711215 0.561536947150976 0.0398649071378087 H1 histone family member O, oocyte specific FUNCTION: May play a key role in the control of gene expression during oogenesis and early embryogenesis, presumably through the perturbation of chromatin structure. Essential for meiotic maturation of germinal vesicle-stage oocytes. The somatic type linker histone H1c is rapidly replaced by H1oo in a donor nucleus transplanted into an oocyte. The greater mobility of H1oo as compared to H1c may contribute to this rapid replacement and increased instability of the embryonic chromatin structure. The rapid replacement of H1c with H1oo may play an important role in nuclear remodeling (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Oocyte-specific. {ECO:0000269|PubMed:12711322}.; testis; globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.03563 0.10455 0.661468037 84.4420854 124.29836 2.42572 H1FX 0.496856075371417 0.428732714533446 0.0744112100951374 H1 histone family member X FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures.; . TISSUE SPECIFICITY: Expressed ubiquitously.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;blood;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;prostate;optic nerve;lung;bone;placenta;macula lutea;visual apparatus;alveolus;kidney;brain;peripheral nerve; thymus; 0.07274 0.18511 -0.119252484 44.53880632 14.69093 0.53002 H1FX-AS1 . . . H1FX antisense RNA 1 . . . . . 0.11103 . . . . . H2AFB1 . . . H2A histone family member B1 FUNCTION: Atypical histone H2A which can replace conventional H2A in some nucleosomes and is associated with active transcription and mRNA processing. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Nucleosomes containing this histone are less rigid and organize less DNA than canonical nucleosomes in vivo. They are enriched in actively transcribed genes and associate with the elongating form of RNA polymerase. They associate with spliceosome components and are required for mRNA splicing. May participate in spermatogenesis. {ECO:0000269|PubMed:15257289, ECO:0000269|PubMed:16287874, ECO:0000269|PubMed:16957777, ECO:0000269|PubMed:17591702, ECO:0000269|PubMed:17726088, ECO:0000269|PubMed:18329190, ECO:0000269|PubMed:22795134}.; . TISSUE SPECIFICITY: Present in mature sperm. {ECO:0000269|PubMed:20008104}.; unclassifiable (Anatomical System);lung;visual apparatus;liver;testis;spleen; . 0.10800 . . . . . H2AFB2 . . . H2A histone family member B2 FUNCTION: Atypical histone H2A which can replace conventional H2A in some nucleosomes and is associated with active transcription and mRNA processing. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Nucleosomes containing this histone are less rigid and organize less DNA than canonical nucleosomes in vivo. They are enriched in actively transcribed genes and associate with the elongating form of RNA polymerase. They associate with spliceosome components and are required for mRNA splicing. May participate in spermatogenesis. {ECO:0000269|PubMed:15257289, ECO:0000269|PubMed:16287874, ECO:0000269|PubMed:16957777, ECO:0000269|PubMed:17591702, ECO:0000269|PubMed:17726088, ECO:0000269|PubMed:18329190, ECO:0000269|PubMed:22795134}.; . TISSUE SPECIFICITY: Present in mature sperm. {ECO:0000269|PubMed:20008104}.; unclassifiable (Anatomical System);lung;visual apparatus;liver;testis;spleen; . 0.13216 . . . . . H2AFB3 . . . H2A histone family member B3 FUNCTION: Atypical histone H2A which can replace conventional H2A in some nucleosomes and is associated with active transcription and mRNA processing. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Nucleosomes containing this histone are less rigid and organize less DNA than canonical nucleosomes in vivo. They are enriched in actively transcribed genes and associate with the elongating form of RNA polymerase. They associate with spliceosome components and are required for mRNA splicing. May participate in spermatogenesis. {ECO:0000269|PubMed:15257289, ECO:0000269|PubMed:16287874, ECO:0000269|PubMed:16957777, ECO:0000269|PubMed:17591702, ECO:0000269|PubMed:17726088, ECO:0000269|PubMed:18329190, ECO:0000269|PubMed:22795134}.; . TISSUE SPECIFICITY: Present in mature sperm. {ECO:0000269|PubMed:20008104}.; . . 0.14605 0.16270 . . . . H2AFJ 0.765927441730416 0.225697347288167 0.00837521098141735 H2A histone family member J FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; . 0.87835 0.13522 0.147123112 64.11299835 3.65353 0.13509 H2AFV 0.412114349708015 0.551515381286724 0.0363702690052604 H2A histone family member V FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division (By similarity). {ECO:0000250}.; . . lymphoreticular;myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;germinal center;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;placenta;head and neck;kidney;stomach;aorta;thymus; amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;hypothalamus;spinal cord;atrioventricular node;caudate nucleus;bone marrow;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum;thymus; 0.77017 0.20297 0.101211609 60.95777306 1.33297 0.04733 H2AFVP1 . . . H2A histone family member V pseudogene 1 . . . . . . . . . . . H2AFX 0.620410500240712 0.347223585163417 0.0323659145958712 H2A histone family member X FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C- terminal phosphorylation. {ECO:0000269|PubMed:10959836, ECO:0000269|PubMed:12419185, ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:15201865}.; . . . . 0.99939 0.86367 -0.075159878 47.78839349 2.11117 0.06939 H2AFY 0.795089570241366 0.2036598919217 0.00125053783693425 H2A histone family member Y FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post- translational modifications of histones, also called histone code, and nucleosome remodeling. Involved in stable X chromosome inactivation. Inhibits the binding of transcription factors and interferes with the activity of remodeling SWI/SNF complexes. Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin. In addition, isoform 1, but not isoform 2, binds ADP-ribose and O-acetyl-ADP- ribose, and may be involved in ADP-ribose-mediated chromatin modulation. {ECO:0000269|PubMed:12718888, ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16107708, ECO:0000269|PubMed:16428466}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9714746}.; lymphoreticular;myocardium;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;bone;pituitary gland;testis;artery;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;oral cavity;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum;thymus; amygdala;medulla oblongata;occipital lobe;parietal lobe;bone marrow;cerebellum; 0.30780 0.21177 -0.405853867 26.23260203 1.46789 0.05048 H2AFY2 0.975641110489864 0.0243328383370053 2.60511731309658e-05 H2A histone family member Y2 FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post- translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in stable X chromosome inactivation. {ECO:0000269|PubMed:15621527}.; . . . . 0.17144 0.18311 -0.53631094 20.53550366 26.5668 0.85876 H2AFZ 0.855327138804775 0.142347144179023 0.00232571701620167 H2A histone family member Z FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division. {ECO:0000269|PubMed:15878876}.; . . medulla oblongata;ovary;umbilical cord;foreskin;skin;bone marrow;retina;prostate;frontal lobe;endometrium;bladder;brain;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;placenta;hippocampus;duodenum;kidney;stomach;aorta; tumor;testis;bone marrow;thymus; 0.98581 0.27035 0.057118534 57.99716914 . . H2AFZP1 . . . H2A histone family member Z pseudogene 1 . . . . . . . . . . . H2AFZP2 . . . H2A histone family member Z pseudogene 2 . . . . . . . . . . . H2AFZP3 . . . H2A histone family member Z pseudogene 3 . . . . . . . . . . . H2AFZP4 . . . H2A histone family member Z pseudogene 4 . . . . . . . . . . . H2AFZP5 . . . H2A histone family member Z pseudogene 5 . . . . . . . . . . . H2AFZP6 . . . H2A histone family member Z pseudogene 6 . . . . . . . . . . . H2BFM 0.186492116512072 0.646371011869418 0.16713687161851 H2B histone family member M FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System);liver;germinal center;brain;stomach; . . . 0.61192669 82.99716914 2411.23931 9.12019 H2BFS . . . H2B histone family member S (pseudogene) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . . . . . . . H2BFWT 0.000863657976086968 0.341474475412133 0.65766186661178 H2B histone family member W, testis specific FUNCTION: Atypical histone H2B. Nucleosomes containing it are structurally and dynamically indistinguishable from those containing conventional H2B. However, unlike conventional H2B, does not recruit chromosome condensation factors and does not participate in the assembly of mitotic chromosomes. May be important for telomere function. {ECO:0000269|PubMed:16449661}.; . TISSUE SPECIFICITY: Testis-specific. Present in sperm cells (at protein level). {ECO:0000269|PubMed:15475252}.; . . . 0.09294 0.238945317 69.20853975 22.25555 0.74631 H2BFXP . . . H2B histone family member X, pseudogene . . . . . . . . . . . H3F3A 0.692334633697484 0.28985577197658 0.0178095943259361 H3 histone, family 3A FUNCTION: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:15776021, ECO:0000269|PubMed:16258499}.; . . . . 0.81411 0.17375 0.145304857 63.81221986 1.21964 0.04083 H3F3AP1 . . . H3 histone, family 3A pseudogene 1 . . . . . . . . . . . H3F3AP2 . . . H3 histone, family 3A pseudogene 2 . . . . . . . . . . . H3F3AP3 . . . H3 histone, family 3A pseudogene 3 . . . . . . . . . . . H3F3AP4 . . . H3 histone, family 3A, pseudogene 4 . . . . . . . . . . . H3F3AP5 . . . H3 histone, family 3A, pseudogene 5 . . . . . . . . . . . H3F3AP6 . . . H3 histone, family 3A, pseudogene 6 . . . unclassifiable (Anatomical System);kidney; superior cervical ganglion;trigeminal ganglion; 0.29148 . . . . . H3F3B 0.809724779677426 0.185480954968376 0.00479426535419747 H3 histone, family 3B (H3.3B) FUNCTION: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:15776021, ECO:0000269|PubMed:16258499}.; . . smooth muscle;ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;caudate nucleus; 0.29831 . -0.207437529 38.2814343 2211.25884 8.65790 H3F3BP1 . . . H3 histone, family 3B (H3.3B) pseudogene 1 . . . . . . . . . . . H3F3BP2 . . . H3 histone, family 3B (H3.3B) pseudogene 2 . . . . . . . . . . . H3F3C 0.297369301956225 0.624101295195883 0.0785294028478917 H3 histone, family 3C FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Hominid-specific H3.5/H3F3C preferentially colocalizes with euchromatin, and it is associated with actively transcribed genes. {ECO:0000269|PubMed:21274551}.; . TISSUE SPECIFICITY: Specifically expressed in the seminiferous tubules of testis. {ECO:0000269|PubMed:21274551}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;islets of Langerhans;hypothalamus;blood;lens;skin;uterus;prostate;lung;nasopharynx;bone;thyroid;visual apparatus;testis;brain;stomach; . . . 0.881944684 89.02453409 866.25712 5.73238 H6PD 0.000111404418020294 0.94897871542963 0.0509098801523499 hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase) FUNCTION: Oxidizes glucose-6-phosphate and glucose, as well as other hexose-6-phosphates.; . TISSUE SPECIFICITY: Present in most tissues examined, strongest in liver.; . . 0.15410 . -0.891174372 10.18518519 2649.42707 9.66219 H19 . . . H19, imprinted maternally expressed transcript (non-protein coding) . . . . . . . . . . . HAAO 7.80091656962148e-06 0.742306975555867 0.257685223527563 3-hydroxyanthranilate 3,4-dioxygenase FUNCTION: Catalyzes the oxidative ring opening of 3- hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate. {ECO:0000255|HAMAP- Rule:MF_03019, ECO:0000269|PubMed:7514594}.; . . unclassifiable (Anatomical System);lung;whole body;hypothalamus;placenta;sympathetic chain;urinary;liver;spleen;kidney;lens; superior cervical ganglion;liver;atrioventricular node;trigeminal ganglion; 0.22234 0.09474 0.52918614 80.81505072 2164.69331 8.56117 HABP2 1.17394512031747e-14 0.0110529278050514 0.988947072194937 hyaluronan binding protein 2 FUNCTION: Cleaves the alpha-chain at multiple sites and the beta- chain between 'Lys-53' and 'Lys-54' but not the gamma-chain of fibrinogen and therefore does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave (activate) prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator (pro- urokinase) to the active two chain form. Activates coagulation factor VII. {ECO:0000269|PubMed:10754382, ECO:0000269|PubMed:11217080, ECO:0000269|PubMed:8827452}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:8827452}.; unclassifiable (Anatomical System);myocardium;heart;spinal cord;muscle;colon;skeletal muscle;pancreas;prostate;lung;endometrium;liver;spleen;kidney;stomach;peripheral nerve; fetal liver;superior cervical ganglion;liver;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.45405 0.10896 -0.06060434 48.88535032 157.81255 2.74375 HABP4 0.00493250468368015 0.967203697796494 0.0278637975198255 hyaluronan binding protein 4 FUNCTION: May be involved in nuclear functions such as the remodeling of chromatin and the regulation of transcription. {ECO:0000269|PubMed:14699138, ECO:0000269|PubMed:16455055}.; . TISSUE SPECIFICITY: Highly expressed in brain, heart, and kidney, and moderately expressed in skeletal muscle. Also expressed in a variety of tumor cell lines and in activated but not resting leukocytes. {ECO:0000269|PubMed:12505151, ECO:0000269|PubMed:9523163}.; . . 0.18355 0.11001 -0.560178693 19.30879925 16.2504 0.57669 HACD1 . . . 3-hydroxyacyl-CoA dehydratase 1 FUNCTION: Isoform 1: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000269|PubMed:18554506}.; DISEASE: Myopathy, congenital, with fiber-type disproportion (CFTD) [MIM:255310]: A genetically heterogeneous disorder in which there is relative hypotrophy of type 1 muscle fibers compared to type 2 fibers on skeletal muscle biopsy. However, these findings are not specific and can be found in many different myopathic and neuropathic conditions. {ECO:0000269|PubMed:23933735}. Note=The gene represented in this entry may be involved in disease pathogenesis. A loss-of-function mutation that segregates with the disease was found in four members of a consanguineous family and not identified in unaffected controls. The mutation affects the expression of the mRNA and the produced protein is catalytically inactive. {ECO:0000269|PubMed:23933735}.; TISSUE SPECIFICITY: Isoform 1 is highly expressed in the myocardium, and to a lesser extent in skeletal and smooth muscular tissues including those from stomach, jejunum, and bladder. Also detected in gingival fibroblasts, periodontal ligament cells, osteoblasts and cementoblasts (PubMed:11054553, PubMed:22067203). Isoform 2 is specifically expressed by cementoblasts but also detected in periodontal ligament cells, heart, liver and kidney (at protein level) (PubMed:22067203). {ECO:0000269|PubMed:11054553, ECO:0000269|PubMed:22067203}.; . . 0.19708 0.11229 0.170987912 65.5579146 . . HACD2 . . . 3-hydroxyacyl-CoA dehydratase 2 FUNCTION: Catalyzes the third of the four reactions of the long- chain fatty acids elongation cycle. This endoplasmic reticulum- bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000269|PubMed:18554506}.; . TISSUE SPECIFICITY: Highly expressed in testis, spleen, prostate, colon and heart, followed by moderate expression in thymus, ovary, small intestine, peripheral blood leukocytes, liver, skeletal muscle and pancreas. Weakly detected in kidney, placenta, brain and lung. {ECO:0000269|PubMed:15024066}.; . . 0.22532 0.08820 0.013025609 54.62962963 . . HACD3 . . . 3-hydroxyacyl-CoA dehydratase 3 FUNCTION: Catalyzes the third of the four reactions of the long- chain fatty acids elongation cycle. This endoplasmic reticulum- bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May be involved in Rac1-signaling pathways leading to the modulation of gene expression. Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (PubMed:25687571). {ECO:0000269|PubMed:10747961, ECO:0000269|PubMed:18554506, ECO:0000269|PubMed:25687571}.; . TISSUE SPECIFICITY: Highly expressed in testis, kidney, brain, liver and weakly in skeletal muscle, spleen and heart. No expression detected in leukocytes. {ECO:0000269|PubMed:10747961, ECO:0000269|PubMed:18554506}.; . . 0.17892 0.11511 0.283038099 71.26680821 . . HACD4 . . . 3-hydroxyacyl-CoA dehydratase 4 FUNCTION: Catalyzes the third of the four reactions of the long- chain fatty acids elongation cycle. This endoplasmic reticulum- bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000269|PubMed:18554506}.; . TISSUE SPECIFICITY: Highly expressed in leukocytes, and low expression in heart, spleen, kidney, and placenta. {ECO:0000269|PubMed:18554506}.; . . 0.14669 0.11079 0.371224249 75.12384996 . . HACE1 0.00159566252447192 0.99839389264758 1.04448279483369e-05 HECT domain and ankyrin repeat containing E3 ubiquitin protein ligase 1 FUNCTION: E3 ubiquitin-protein ligase involved in Golgi membrane fusion and regulation of small GTPases. Acts as a regulator of Golgi membrane dynamics during the cell cycle: recruited to Golgi membrane by Rab proteins and regulates postmitotic Golgi membrane fusion. Acts by mediating ubiquitination during mitotic Golgi disassembly, ubiquitination serving as a signal for Golgi reassembly later, after cell division. Specifically interacts with GTP-bound RAC1, mediating ubiquitination and subsequent degradation of active RAC1, thereby playing a role in host defense against pathogens. May also act as a transcription regulator via its interaction with RARB. {ECO:0000269|PubMed:15254018, ECO:0000269|PubMed:21988917, ECO:0000269|PubMed:22036506}.; DISEASE: Note=Defects in HACE1 are a cause of Wilms tumor (WT). WT is a pediatric malignancy of kidney and one of the most common solid cancers in childhood. HACE1 is epigenetically down-regulated in sporadic Wilms tumor. Moreover, a t(5;6)(q21;q21) translocation that truncates HACE1 has been found in a child with bilateral, young-onset Wilms tumor (PubMed:19948536). {ECO:0000269|PubMed:17694067, ECO:0000269|PubMed:19948536}.; TISSUE SPECIFICITY: Expressed in multiple tissues including heart, brain and kidney. {ECO:0000269|PubMed:15254018}.; unclassifiable (Anatomical System);lymph node;heart;ovary;islets of Langerhans;hypothalamus;colon;parathyroid;skin;lung;ganglion;frontal lobe;endometrium;bone;placenta;pituitary gland;hypopharynx;liver;testis;head and neck;brain;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.20587 0.10335 -0.911109353 9.961075725 45.70885 1.29926 HACL1 4.18066326371778e-10 0.329389403558953 0.670610596022981 2-hydroxyacyl-CoA lyase 1 FUNCTION: Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde.; . TISSUE SPECIFICITY: Expressed in high levels in liver, also expressed in kidney, heart and skeletal muscle. {ECO:0000269|PubMed:10468558}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.09220 0.07873 -0.420619508 25.72540694 226.89898 3.25558 HADH 0.000613689575050013 0.904043531181633 0.0953427792433166 hydroxyacyl-CoA dehydrogenase FUNCTION: Plays an essential role in the mitochondrial beta- oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA.; DISEASE: 3-alpha-hydroxyacyl-CoA dehydrogenase deficiency (HADH deficiency) [MIM:231530]: A metabolic disorder with various clinical presentations including hypoglycemia, hepatoencephalopathy, myopathy or cardiomyopathy, and in some cases sudden death. {ECO:0000269|Ref.13}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Familial hyperinsulinemic hypoglycemia 4 (HHF4) [MIM:609975]: Most common cause of persistent hypoglycemia in infancy. Unless early and aggressive intervention is undertaken, brain damage from recurrent episodes of hypoglycemia may occur. HHF4 should be easily recognizable by analysis of acylcarnitine species and that this disorder responds well to treatment with diazoxide. It provides the first 'experiment of nature' that links impaired fatty acid oxidation to hyperinsulinism and that provides support for the concept that a lipid signaling pathway is implicated in the control of insulin secretion. {ECO:0000269|PubMed:11489939}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in liver, kidney, pancreas, heart and skeletal muscle.; lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;spinal cord;adrenal cortex;pharynx;lens;skeletal muscle;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;kidney;stomach;aorta; superior cervical ganglion;testis - interstitial;adipose tissue;liver;testis;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07665 0.31408 0.817616644 87.95116773 1437.95027 7.07446 HADHA 0.0151113309974031 0.984840331993952 4.83370086448278e-05 hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit FUNCTION: Bifunctional subunit.; DISEASE: Mitochondrial trifunctional protein deficiency (MTPD) [MIM:609015]: A disease biochemically characterized by loss of all enzyme activities of the mitochondrial trifunctional protein complex. Variable clinical manifestations include hypoglycemia, cardiomyopathy, delayed psychomotor development, sensorimotor axonopathy, generalized weakness, hepatic dysfunction, respiratory failure. Sudden infant death may occur. Most patients die from heart failure. {ECO:0000269|PubMed:9739053}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Long-chain 3-hydroxyl-CoA dehydrogenase deficiency (LCHAD deficiency) [MIM:609016]: The clinical features are very similar to TFP deficiency. Biochemically, LCHAD deficiency is characterized by reduced long-chain 3-hydroxyl-CoA dehydrogenase activity, while the other enzyme activities of the TFP complex are normal or only slightly reduced. {ECO:0000269|PubMed:7811722, ECO:0000269|PubMed:9266371}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Maternal acute fatty liver of pregnancy (AFLP) [MIM:609016]: Severe maternal illness occurring during pregnancies with affected fetuses. This disease is associated with LCHAD deficiency and characterized by sudden unexplained infant death or hypoglycemia and abnormal liver enzymes (Reye-like syndrome). {ECO:0000269|PubMed:7846063}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.06142 0.51611 -0.642904474 16.62538335 330.14198 3.86230 HADHAP1 . . . hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit pseudogene 1 . . . . . . . . . . . HADHAP2 . . . hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit pseudogene 2 . . . . . . . . . . . HADHB 1.04714648529854e-07 0.926810509104057 0.0731893861812944 hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), beta subunit . DISEASE: Mitochondrial trifunctional protein deficiency (MTPD) [MIM:609015]: A disease biochemically characterized by loss of all enzyme activities of the mitochondrial trifunctional protein complex. Variable clinical manifestations include hypoglycemia, cardiomyopathy, delayed psychomotor development, sensorimotor axonopathy, generalized weakness, hepatic dysfunction, respiratory failure. Sudden infant death may occur. Most patients die from heart failure. {ECO:0000269|PubMed:12754706, ECO:0000269|PubMed:8651282, ECO:0000269|PubMed:9259266}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;iris;bladder;brain;heart;cartilage;tongue;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;amnion;head and neck;kidney;stomach;aorta; hypothalamus;spinal cord;kidney;skeletal muscle;parietal lobe; 0.09577 0.24360 -0.53631094 20.53550366 84.59855 1.95806 HAGH 0.000143398287880002 0.65244198298171 0.34741461873041 hydroxyacylglutathione hydrolase FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D- lactoyl-glutathione to form glutathione and D-lactic acid.; . TISSUE SPECIFICITY: Expressed in liver and kidney. {ECO:0000269|PubMed:15117945}.; . . 0.32361 0.30121 -0.111973265 45.35857514 243.61664 3.36889 HAGHL 0.000148930109473316 0.425566792046185 0.574284277844341 hydroxyacylglutathione hydrolase-like FUNCTION: Hydrolase acting on ester bonds. {ECO:0000305}.; . . unclassifiable (Anatomical System);ovary;colon;blood;parathyroid;skin;prostate;lung;bone;placenta;thyroid;cervix;kidney;brain;stomach;thymus; . 0.06518 0.09645 . . 52.77485 1.43926 HAGLR . . . HOXD antisense growth-associated long non-coding RNA . . . . . . . . . . . HAGLROS . . . HAGLR opposite strand (non-protein coding) . . . . . . . . . . . HAL 5.90868534733458e-17 0.0129668485976917 0.987033151402308 histidine ammonia-lyase . DISEASE: Histidinemia (HISTID) [MIM:235800]: Autosomal recessive disease characterized by increased histidine and histamine as well as decreased urocanic acid in body fluids. {ECO:0000269|PubMed:15806399}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;pituitary gland;liver;spleen;blood;bone marrow; fetal liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.51979 . -0.659500046 16.07100731 149.14468 2.66223 HAMP 0.0425051340417533 0.847000084032949 0.110494781925298 hepcidin antimicrobial peptide FUNCTION: Liver-produced hormone that constitutes the main circulating regulator of iron absorption and distribution across tissues. Acts by promoting endocytosis and degradation of ferroportin, leading to the retention of iron in iron-exporting cells and decreased flow of iron into plasma. Controls the major flows of iron into plasma: absorption of dietary iron in the intestine, recycling of iron by macrophages, which phagocytose old erythrocytes and other cells, and mobilization of stored iron from hepatocytes (PubMed:22306005). {ECO:0000269|PubMed:22306005}.; DISEASE: Hemochromatosis 2B (HFE2B) [MIM:613313]: A juvenile form of hemochromatosis, a disorder of iron metabolism with excess deposition of iron in a variety of organs leading to their failure, bronze skin pigmentation, hepatic cirrhosis, arthropathy and diabetes. The most common symptoms of juvenile hemochromatosis at presentation are hypogonadism and cardiomyopathy. {ECO:0000269|PubMed:12915468, ECO:0000269|PubMed:14630809, ECO:0000269|PubMed:14633868, ECO:0000269|PubMed:14670915, ECO:0000269|PubMed:15099344}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest expression in liver and to a lesser extent in heart and brain. Low levels in lung, tonsils, salivary gland, trachea, prostate gland, adrenal gland and thyroid gland. Secreted into the urine. {ECO:0000269|PubMed:11034317}.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;fovea centralis;choroid;lens;skin;retina;optic nerve;lung;cornea;macula lutea;visual apparatus;liver;testis;spleen;kidney;brain;mammary gland; fetal liver;liver;atrioventricular node;trigeminal ganglion; 0.31367 0.54192 0.457594962 78.16112291 6.0157 0.22653 HAND1 0.0695994741559291 0.738050943104054 0.192349582740017 heart and neural crest derivatives expressed 1 FUNCTION: Transcription factor that plays an essential role in both trophoblast-giant cells differentiation and in cardiac morphogenesis. In the adult, could be required for ongoing expression of cardiac-specific genes. Binds the DNA sequence 5'- NRTCTG-3' (non-canonical E-box) (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Heart.; unclassifiable (Anatomical System);optic nerve;macula lutea;fovea centralis;choroid;lens;brain;peripheral nerve;retina; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.32450 0.22992 0.03689118 56.64071715 34.31596 1.04990 HAND2 0.351297751553542 0.593916721479608 0.0547855269668502 heart and neural crest derivatives expressed 2 FUNCTION: Essential for cardiac morphogenesis, particularly for the formation of the right ventricle and of the aortic arch arteries. Required for vascular development and regulation of angiogenesis, possibly through a VEGF signaling pathway. Plays also an important role in limb development, particularly in the establishment of anterior-posterior polarization, acting as an upstream regulator of sonic hedgehog (SHH) induction in the limb bud. Is involved in the development of branchial arches, which give rise to unique structures in the head and neck. Binds DNA on E-box consensus sequence 5'-CANNTG-3' (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Heart.; unclassifiable (Anatomical System);heart;ovary;tongue;islets of Langerhans;colon;skin;uterus;pancreas;lung;endometrium;bone;thyroid;placenta;liver;head and neck;spleen;brain;peripheral nerve; . 0.65035 0.29199 . . 30.35159 0.96782 HAND2-AS1 . . . HAND2 antisense RNA 1 (head to head) . . . . . . . . . . . HAO1 0.000672388585939552 0.913547079449021 0.0857805319650395 hydroxyacid oxidase (glycolate oxidase) 1 FUNCTION: Has 2-hydroxyacid oxidase activity. Most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids, with high activity towards 2-hydroxy palmitate and 2- hydroxy octanoate. {ECO:0000269|PubMed:18215067}.; . TISSUE SPECIFICITY: Liver.; . . 0.15595 0.30205 0.306902668 72.38145789 125.15 2.43505 HAO2 4.4763295317251e-08 0.36677287410365 0.633227081133055 hydroxyacid oxidase 2 (long chain) FUNCTION: Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids.; . TISSUE SPECIFICITY: Liver and kidney.; unclassifiable (Anatomical System);cartilage;thyroid;liver;colon;spleen;head and neck;kidney;skin;stomach; superior cervical ganglion;liver;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion; 0.05887 0.10046 -0.201976964 38.98325077 43.06465 1.24598 HAO2-IT1 . . . HAO2 intronic transcript 1 . . . . . . . . . . . HAP1 1.58556445592013e-19 0.000397559834814778 0.999602440165185 huntingtin-associated protein 1 FUNCTION: Originally identified as neuronal protein that specifically associates with HTT/huntingtin and the binding is enhanced by an expanded polyglutamine repeat within HTT possibly affecting HAP1 interaction properties. Both HTT and HAP1 are involved in intracellular trafficking and HAP1 is proposed to link HTT to motor proteins and/or transport cargos. Seems to play a role in vesicular transport within neurons and axons such as from early endosomes to late endocytic compartments and to promote neurite outgrowth. The vesicular transport function via association with microtubule-dependent transporters can be attenuated by association with mutant HTT. Involved in the axonal transport of BDNF and its activity-dependent secretion; the function seems to involve HTT, DCTN1 and a complex with SORT1. Involved in APP trafficking and seems to faciltate APP anterograde transport and membrane insertion thereby possibly reducing processing into amyloid beta. Involved in delivery of gamma- aminobutyric acid (GABA(A)) receptors to synapses; the function is dependent on kinesin motor protein KIF5 and is disrupted by HTT with expanded polyglutamine repeat. Involved in regulation of autophagosome motility by promoting efficient retrograde axonal transport. Seems to be involved in regulation of membrane receptor recycling and degradation, and respective signal transduction, including GABA(A) receptors, tyrosine kinase receptors, EGFR, IP3 receptor and androgen receptor. Among others suggested to be involved in control of feeding behavior (involving hypothalamic GABA(A) receptors), cerebellar and brainstem development (involving AHI1 and NTRK1/TrkA), postnatal neurogenesis (involving hypothalamic NTRK2/TrkB), and ITPR1/InsP3R1-mediated Ca(2+) release (involving HTT and possibly the effect of mutant HTT). Via association with DCTN1/dynactin p150-glued and HTT/huntingtin involved in cytoplasmic retention of REST in neurons. May be involved in ciliogenesis. Involved in regulation of exocytosis. Seems to be involved in formation of cytoplasmic inclusion bodies (STBs). In case of anomalous expression of TBP, can sequester a subset of TBP into STBs; sequestration is enhanced by an expanded polyglutamine repeat within TBP. HAP1-containing STBs have been proposed to play a protective role against neurodegeneration in Huntigton disease (HD) and spinocerebellar ataxia 17 (SCA17). {ECO:0000269|PubMed:18922795}.; . TISSUE SPECIFICITY: Predominantly expressed in brain. Selectively expressed in neurons.; unclassifiable (Anatomical System);islets of Langerhans;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;breast;lung;optic nerve;larynx;bone;macula lutea;hypopharynx;liver;spleen;head and neck;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skin;skeletal muscle;cingulate cortex; 0.11435 . 1.870334421 97.21042699 3938.80877 12.40172 HAPLN1 0.260833364813835 0.733416191266102 0.00575044392006368 hyaluronan and proteoglycan link protein 1 FUNCTION: Stabilizes the aggregates of proteoglycan monomers with hyaluronic acid in the extracellular cartilage matrix.; . TISSUE SPECIFICITY: Widely expressed. Weakly expressed in the brain. {ECO:0000269|PubMed:11027579, ECO:0000269|PubMed:12663660}.; unclassifiable (Anatomical System);cartilage;heart;ovary;parathyroid;bone marrow;bile duct;prostate;whole body;lung;cochlea;bone;placenta;visual apparatus;liver;testis;head and neck;kidney;brain; superior cervical ganglion;heart;atrioventricular node;trigeminal ganglion; 0.21811 0.18489 -0.53631094 20.53550366 33.08596 1.02480 HAPLN2 1.05244127720139e-05 0.348935789959836 0.651053685627392 hyaluronan and proteoglycan link protein 2 FUNCTION: Mediates a firm binding of versican V2 to hyaluronic acid. May play a pivotal role in the formation of the hyaluronan- associated matrix in the central nervous system (CNS) which facilitates neuronal conduction and general structural stabilization. Binds to hyaluronic acid (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed only in adult brain. {ECO:0000269|PubMed:11027579}.; unclassifiable (Anatomical System);prostate;lung;testis;brain; thalamus;hypothalamus;spinal cord;skeletal muscle;cingulate cortex; 0.46946 0.10764 . . 106.78825 2.24254 HAPLN3 3.91721530857888e-06 0.370376544243149 0.629619538541543 hyaluronan and proteoglycan link protein 3 FUNCTION: May function in hyaluronic acid binding. {ECO:0000303|PubMed:12663660}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in spleen and placenta. {ECO:0000269|PubMed:12663660}.; unclassifiable (Anatomical System);lymphoreticular;heart;ovary;colon;parathyroid;skeletal muscle;retina;pancreas;lung;frontal lobe;endometrium;placenta;mammary gland;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14360 0.10628 -0.354480518 29.42911064 4444.58352 13.35637 HAPLN4 0.0326847848265823 0.926725398791703 0.0405898163817147 hyaluronan and proteoglycan link protein 4 FUNCTION: Binds to hyaluronic acid and may be involved in formation of the extracellular matrix. {ECO:0000250|UniProtKB:Q80WM4}.; . TISSUE SPECIFICITY: Expressed predominantly in brain. {ECO:0000269|PubMed:12663660}.; unclassifiable (Anatomical System);heart;tongue;fovea centralis;choroid;lens;retina;optic nerve;lung;frontal lobe;larynx;macula lutea;testis;head and neck;brain;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;pancreas;liver;globus pallidus;ciliary ganglion;atrioventricular node;skin;parietal lobe; 0.16701 0.11410 . . 40.8701 1.19715 HAR1A . . . highly accelerated region 1A (non-protein coding) . . . . . . . . . . . HAR1B . . . highly accelerated region 1B (non-protein coding) . . . . . . . . . . . HARBI1 0.00570134099999797 0.900356759230341 0.0939418997696613 harbinger transposase derived 1 FUNCTION: Transposase-derived protein that may have nuclease activity (Potential). Does not have transposase activity. {ECO:0000269|PubMed:15169610, ECO:0000269|PubMed:18339812, ECO:0000305}.; . TISSUE SPECIFICITY: Detected in brain, eye, nerve tissue, kidney and lung. {ECO:0000269|PubMed:15169610}.; medulla oblongata;fovea centralis;choroid;lens;skin;retina;pancreas;optic nerve;lung;frontal lobe;endometrium;bone;macula lutea;pituitary gland;testis;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node; 0.34196 0.11703 -0.626318434 17.03231894 34.93143 1.06179 HARS 0.000736050889038717 0.995462033655921 0.00380191545504074 histidyl-tRNA synthetase FUNCTION: Cytoplasmic histidine--tRNA ligase (Probable). Plays a role in axon guidance. {ECO:0000269|PubMed:26072516, ECO:0000305}.; DISEASE: Charcot-Marie-Tooth disease 2W (CMT2W) [MIM:616625]: An autosomal dominant, axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot- Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. CMT2W patients manifest a peripheral neuropathy mainly affecting the lower limbs and resulting in gait difficulties and distal sensory impairment. Most patients also have upper limb involvement. {ECO:0000269|PubMed:22930593, ECO:0000269|PubMed:26072516}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Brain, heart, liver and kidney.; ovary;skin;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;placenta;duodenum;head and neck;kidney;stomach;cerebellum; whole brain;subthalamic nucleus;thalamus;medulla oblongata;occipital lobe;hypothalamus;prefrontal cortex;globus pallidus;pons;cingulate cortex;parietal lobe; 0.24759 . 0.264628794 70.5178108 160.6993 2.76846 HARS2 8.12767561165649e-05 0.982298324756155 0.0176203984877288 histidyl-tRNA synthetase 2, mitochondrial . . TISSUE SPECIFICITY: A high level expression is seen in the heart, kidney and skeletal muscle while a lower level expression is seen in the brain and liver.; lymphoreticular;myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;pharynx;blood;lens;breast;pancreas;lung;epididymis;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; . 0.14645 -0.404032746 26.53338051 49.63991 1.38089 HAS1 6.04485755172797e-11 0.0172250179081521 0.982774982031399 hyaluronan synthase 1 FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of the isozymes catalyzing that reaction. Also able to catalyze the synthesis of chito- oligosaccharide depending on the substrate (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in ovary followed by spleen, thymus, prostate, testes and large intestine. Weakly expressed in small intestine. {ECO:0000269|PubMed:8651928}.; pancreas;cartilage;ovary;hypothalamus;bone;placenta;colon;parathyroid;brain; superior cervical ganglion;trigeminal ganglion; 0.21654 0.24468 . . 3167.35591 10.73052 HAS2 0.994245615539079 0.0057536283106059 7.561503152833e-07 hyaluronan synthase 2 FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of the isozymes catalyzing that reaction and it is particularly responsible for the synthesis of high molecular mass hyaluronan. Required for the transition of endocardial cushion cells into mesenchymal cells, a process crucial for heart development. May also play a role in vasculogenesis. High molecular mass hyaluronan also play a role in early contact inhibition a process which stops cell growth when cells come into contact with each other or the extracellular matrix (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in fibroblasts.; unclassifiable (Anatomical System);whole body;mesenchyma;bone;muscle;liver;cervix;skin;bone marrow; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.48285 0.33817 -0.251530012 35.42108988 30.33807 0.96699 HAS2-AS1 . . . HAS2 antisense RNA 1 . . . . . . . . . . . HAS3 0.26938711218293 0.729516330467862 0.00109655734920831 hyaluronan synthase 3 FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of the isozymes catalyzing that reaction (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;thyroid;bone;iris;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;lens;pancreas;lung;placenta;visual apparatus;macula lutea;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach; . 0.66420 0.22757 -0.552898813 19.86317528 188.46987 2.98241 HAT1 0.839884792256617 0.16008887783586 2.63299075228507e-05 histone acetyltransferase 1 FUNCTION: Acetylates soluble but not nucleosomal histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, acetylates histone H2A at 'Lys-5' (H2AK5ac). Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. May be involved in nucleosome assembly during DNA replication and repair as part of the histone H3.1 and H3.3 complexes. May play a role in DNA repair in response to free radical damage. {ECO:0000269|PubMed:11585814, ECO:0000269|PubMed:20953179, ECO:0000269|PubMed:22615379, ECO:0000269|PubMed:9427644}.; . . ovary;colon;retina;uterus;prostate;cochlea;endometrium;bone;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; tumor;skeletal muscle; 0.95898 0.13385 0.128714042 63.19886766 200.4494 3.05988 HAUS1 0.000296742662155892 0.799237317237491 0.200465940100353 HAUS augmin like complex subunit 1 FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269|PubMed:15082789, ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in pancreas, kidney, skeletal muscle, liver and heart. Weakly expressed in lung, brain and placenta. {ECO:0000269|PubMed:15082789}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;small intestine;islets of Langerhans;pharynx;blood;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;stomach;peripheral nerve;thymus; . 0.75978 0.11423 0.549415813 81.38122199 139.20452 2.57298 HAUS1P1 . . . HAUS augmin like complex subunit 1 pseudogene 1 . . . . . . . . . . . HAUS1P2 . . . HAUS augmin like complex subunit 1 pseudogene 2 . . . . . . . . . . . HAUS1P3 . . . HAUS augmin like complex subunit 1 pseudogene 3 . . . . . . . . . . . HAUS2 0.00140043242000112 0.663429135110192 0.335170432469807 HAUS augmin like complex subunit 2 FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}.; . . unclassifiable (Anatomical System);lung;placenta;liver;testis;spleen;kidney;germinal center;brain;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;parietal lobe; 0.13793 0.11088 0.703746784 85.42108988 106.97024 2.24440 HAUS3 8.89916619400129e-07 0.515548619168805 0.484450490914575 HAUS augmin like complex subunit 3 FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}.; . . unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;colon;parathyroid;skin;skeletal muscle;lung;endometrium;placenta;visual apparatus;alveolus;liver;spleen;brain;mammary gland;pineal gland; superior cervical ganglion;pons; 0.09518 0.09228 -0.023789244 52.09365416 610.32432 4.99283 HAUS4 0.036809880472709 0.955725811759243 0.00746430776804799 HAUS augmin like complex subunit 4 FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;cerebral cortex;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis;atrioventricular node; 0.41351 . -0.315847836 31.68789809 87.11944 1.99341 HAUS4P1 . . . HAUS augmin like complex subunit 4 pseudogene 1 . . . . . . . . . . . HAUS5 0.000826136639407559 0.999040823084452 0.000133040276140855 HAUS augmin like complex subunit 5 FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);muscle;blood;lens;pancreas;lung;placenta;macula lutea;liver;hypopharynx;head and neck;cervix;kidney;cerebellum; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; 0.12457 . 0.135991087 63.61759849 792.04822 5.55167 HAUS6 6.60892812829788e-10 0.854816357735651 0.145183641603456 HAUS augmin like complex subunit 6 FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. Promotes the nucleation of microtubules from the spindle through recruitment of NEDD1 and gamma-tubulin. {ECO:0000269|PubMed:19029337, ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}.; . . . . 0.37338 0.07679 1.032445072 91.12408587 1600.47359 7.40118 HAUS6P1 . . . HAUS augmin like complex subunit 6 pseudogene 1 . . . . . . . . . . . HAUS6P2 . . . HAUS augmin like complex subunit 6 pseudogene 2 . . . . . . . . . . . HAUS6P3 . . . HAUS augmin like complex subunit 6 pseudogene 3 . . . . . . . . . . . HAUS7 0.959453959935133 0.0404539920315623 9.20480333045315e-05 HAUS augmin like complex subunit 7 FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}.; . TISSUE SPECIFICITY: Detected in spleen, thymus, testis, ovary, small intestine and colon, with highest levels of expression in testis and ovary. {ECO:0000269|PubMed:11163772}.; . . 0.08206 . -0.047654689 50.22410946 61.22675 1.59321 HAUS8 0.000726405158492587 0.980804538159796 0.018469056681711 HAUS augmin like complex subunit 8 FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269|PubMed:18362163, ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}.; . . unclassifiable (Anatomical System);medulla oblongata;cartilage;muscle;urinary;colon;blood;skin;retina;breast;uterus;whole body;lung;endometrium;bone;placenta;visual apparatus;liver;testis;spleen;cervix;germinal center;kidney;brain;mammary gland; testis - interstitial;globus pallidus;tumor; . . -0.200157416 39.11299835 1991.75853 8.22092 HAUS8P1 . . . HAUS augmin like complex subunit 8 pseudogene 1 . . . . . . . . . . . HAVCR1 0.00305433633416917 0.944598690977843 0.0523469726879883 hepatitis A virus cellular receptor 1 FUNCTION: May play a role in T-helper cell development and the regulation of asthma and allergic diseases. Receptor for TIMD4 (By similarity). May play a role in kidney injury and repair. {ECO:0000250, ECO:0000269|PubMed:17471468}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in kidney and testis. Expressed by activated CD4+ T-cells during the development of helper T-cells responses. {ECO:0000269|PubMed:9658108}.; uterus;lung;visual apparatus;testis;colon;kidney; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.02654 . 0.797386419 87.53833451 2662.53334 9.70555 HAVCR1P1 . . . hepatitis A virus cellular receptor 1 pseudogene 1 . . . . . . . . . . . HAVCR1P2 . . . hepatitis A virus cellular receptor 1 pseudogene 2 . . . . . . . . . . . HAVCR2 0.111384118892431 0.859870340639784 0.0287455404677855 hepatitis A virus cellular receptor 2 FUNCTION: Cell surface receptor implicated in modulating innate and adaptive immune responses. Generally accepted to have an inhibiting function. Reports on stimulating functions suggest that the activity may be influenced by the cellular context and/or the respective ligand (PubMed:24825777). Regulates macrophage activation (PubMed:11823861). Inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance (PubMed:14556005). In CD8+ cells attenuates TCR-induced signaling, specifically by blocking NF- kappaB and NFAT promoter activities resulting in the loss of IL-2 secretion. The function may implicate its association with LCK proposed to impair phosphorylation of TCR subunits, and/or LGALS9- dependent recruitment of PTPRC to the immunological synapse (PubMed:24337741, PubMed:26492563). In contrast, shown to activate TCR-induced signaling in T cells probably implicating ZAP70, LCP2, LCK and FYN (By similarity). Expressed on Treg cells can inhibit Th17 cell responses (PubMed:24838857). Receptor for LGALS9 (PubMed:16286920, PubMed:24337741). Binding to LGALS9 is believed to result in suppression of T cell responses; the resulting apoptosis of antigen-specific cells may implicate HAVCR2 phosphorylation and disruption of its association with BAG6. Binding to LGALS9 is proposed to be involved in innate immune response to intracellular pathogens. Expressed on Th1 cells interacts with LGALS9 expressed on Mycobacterium tuberculosis- infected macrophages to stimulate antibactericidal activity including IL-1 beta secretion and to restrict intracellular bacterial growth (By similarity). However, the function as receptor for LGALS9 has been challenged (PubMed:23555261). Also reported to enhance CD8+ T cell responses to an acute infection such as by Listeria monocytogenes (By similarity). Receptor for phosphatidylserine (PtSer); PtSer-binding is calcium-dependent. May recognize PtSer on apoptotic cells leading to their phagocytosis. Mediates the engulfment of apoptotic cells by dendritic cells. Expressed on T cells, promotes conjugation but not engulfment of apoptotic cells. Expressed on dendritic cells (DCs) positively regulates innate immune response and in synergy with Toll-like receptors promotes secretion of TNF-alpha. In tumor-imfiltrating DCs suppresses nucleic acid-mediated innate immune repsonse by interaction with HMGB1 and interfering with nucleic acid-sensing and trafficking of nucleid acids to endosomes (By similarity). Expressed on natural killer (NK) cells acts as a coreceptor to enhance IFN-gamma production in response to LGALS9 (PubMed:22323453). In contrast, shown to suppress NK cell-mediated cytotoxicity (PubMed:22383801). Negatively regulates NK cell function in LPS-induced endotoxic shock (By similarity). {ECO:0000250|UniProtKB:Q8VIM0, ECO:0000269|PubMed:11823861, ECO:0000269|PubMed:14556005, ECO:0000269|PubMed:16286920, ECO:0000269|PubMed:22323453, ECO:0000269|PubMed:23555261, ECO:0000269|PubMed:24838857, ECO:0000269|PubMed:26492563, ECO:0000305|PubMed:24825777}.; DISEASE: Note=May be involved in T cell exhaustion associated with chronic viral infections such as with human immunodeficiency virus (HIV) and hepatitic C virus (HCV). {ECO:0000269|PubMed:19001139, ECO:0000269|PubMed:19587053}.; TISSUE SPECIFICITY: Expressed in T-helper type 1 (Th1) lymphocytes. Expressed on regulatory T (Treg) cells after TCR stimulation. Expressed in dendritic cells and natural killer (NK) cells. Expressed in epithelial tissues. Expression is increased on CD4+ and CD8+ T cells in chronic hepatitis C virus (HCV) infection. In progressive HIV-1 infection, expression is up- regulated on HIV-1-specific CD8 T cells. {ECO:0000269|PubMed:11823861, ECO:0000269|PubMed:17069754, ECO:0000269|PubMed:18006747, ECO:0000269|PubMed:19001139, ECO:0000269|PubMed:19587053, ECO:0000269|PubMed:22323453, ECO:0000269|PubMed:22383801, ECO:0000269|PubMed:24838857}.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;blood;skeletal muscle;bone marrow;uterus;pancreas;lung;nasopharynx;placenta;liver;testis;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;trigeminal ganglion; 0.06821 . 0.973768544 90.33970276 88.27515 2.01313 HAX1 1.10582340278236e-05 0.578893749131909 0.421095192634063 HCLS1 associated protein X-1 FUNCTION: Promotes cell survival. Potentiates GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. May regulate intracellular calcium pools. {ECO:0000269|PubMed:15339924, ECO:0000269|PubMed:16857965, ECO:0000269|PubMed:17545607, ECO:0000269|PubMed:18319618, ECO:0000269|PubMed:18971376, ECO:0000269|PubMed:9058808}.; DISEASE: Neutropenia, severe congenital 3, autosomal recessive (SCN3) [MIM:610738]: A disorder of hematopoiesis characterized by maturation arrest of granulopoiesis at the level of promyelocytes with peripheral blood absolute neutrophil counts below 0.5 x 10(9)/l and early onset of severe bacterial infections. Some patients affected by severe congenital neutropenia type 3 have neurological manifestations such as psychomotor retardation and seizures. {ECO:0000269|PubMed:17187068, ECO:0000269|PubMed:18337561, ECO:0000269|PubMed:19796188, ECO:0000269|PubMed:20220065}. Note=The disease is caused by mutations affecting the gene represented in this entry. The clinical phenotype due to HAX1 deficiency appears to depend on the localization of the mutations and their influence on the transcript variants. Mutations affecting exclusively isoform 1 are associated with isolated congenital neutropenia, whereas mutations affecting both isoform 1 and isoform 5 are associated with additional neurologic symptoms (PubMed:18337561). {ECO:0000269|PubMed:18337561}.; TISSUE SPECIFICITY: Ubiquitous. Up-regulated in oral cancers. {ECO:0000269|PubMed:17545607, ECO:0000269|PubMed:9058808}.; lymphoreticular;synovium;colon;brain;skeletal muscle; dorsal root ganglion;thalamus;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;caudate nucleus;skeletal muscle; 0.13278 0.20513 -0.560178693 19.30879925 27.58424 0.88754 HBA1 0.511601563401791 0.420384296003805 0.068014140594404 hemoglobin subunit alpha 1 FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.; DISEASE: Heinz body anemias (HEIBAN) [MIM:140700]: Form of non- spherocytic hemolytic anemia of Dacie type 1. After splenectomy, which has little benefit, basophilic inclusions called Heinz bodies are demonstrable in the erythrocytes. Before splenectomy, diffuse or punctate basophilia may be evident. Most of these cases are probably instances of hemoglobinopathy. The hemoglobin demonstrates heat lability. Heinz bodies are observed also with the Ivemark syndrome (asplenia with cardiovascular anomalies) and with glutathione peroxidase deficiency. {ECO:0000269|PubMed:2833478}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Alpha-thalassemia (A-THAL) [MIM:604131]: A form of thalassemia. Thalassemias are common monogenic diseases occurring mostly in Mediterranean and Southeast Asian populations. The hallmark of alpha-thalassemia is an imbalance in globin-chain production in the adult HbA molecule. The level of alpha chain production can range from none to very nearly normal levels. Deletion of both copies of each of the two alpha-globin genes causes alpha(0)-thalassemia, also known as homozygous alpha thalassemia. Due to the complete absence of alpha chains, the predominant fetal hemoglobin is a tetramer of gamma-chains (Bart hemoglobin) that has essentially no oxygen carrying capacity. This causes oxygen starvation in the fetal tissues leading to prenatal lethality or early neonatal death. The loss of two alpha genes results in mild alpha-thalassemia, also known as heterozygous alpha-thalassemia. Affected individuals have small red cells and a mild anemia (microcytosis). If three of the four alpha-globin genes are functional, individuals are completely asymptomatic. Some rare forms of alpha-thalassemia are due to point mutations (non-deletional alpha-thalassemia). Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Alpha(0)-thalassemia is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non- immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.; DISEASE: Hemoglobin H disease (HBH) [MIM:613978]: A form of alpha- thalassemia due to the loss of three alpha genes. This results in high levels of a tetramer of four beta chains (hemoglobin H), causing a severe and life-threatening anemia. Untreated, most patients die in childhood or early adolescence. {ECO:0000269|PubMed:10569720}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Red blood cells.; lymphoreticular;myocardium;colon;skin;retina;bone marrow;whole body;frontal lobe;bone;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;skeletal muscle;lung;placenta;liver;spleen;head and neck;kidney;stomach;thymus; . 0.12890 0.14878 . . 2.80809 0.09996 HBA2 0.448693557225498 0.452869562367643 0.0984368804068594 hemoglobin subunit alpha 2 FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.; DISEASE: Heinz body anemias (HEIBAN) [MIM:140700]: Form of non- spherocytic hemolytic anemia of Dacie type 1. After splenectomy, which has little benefit, basophilic inclusions called Heinz bodies are demonstrable in the erythrocytes. Before splenectomy, diffuse or punctate basophilia may be evident. Most of these cases are probably instances of hemoglobinopathy. The hemoglobin demonstrates heat lability. Heinz bodies are observed also with the Ivemark syndrome (asplenia with cardiovascular anomalies) and with glutathione peroxidase deficiency. {ECO:0000269|PubMed:2833478}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Alpha-thalassemia (A-THAL) [MIM:604131]: A form of thalassemia. Thalassemias are common monogenic diseases occurring mostly in Mediterranean and Southeast Asian populations. The hallmark of alpha-thalassemia is an imbalance in globin-chain production in the adult HbA molecule. The level of alpha chain production can range from none to very nearly normal levels. Deletion of both copies of each of the two alpha-globin genes causes alpha(0)-thalassemia, also known as homozygous alpha thalassemia. Due to the complete absence of alpha chains, the predominant fetal hemoglobin is a tetramer of gamma-chains (Bart hemoglobin) that has essentially no oxygen carrying capacity. This causes oxygen starvation in the fetal tissues leading to prenatal lethality or early neonatal death. The loss of two alpha genes results in mild alpha-thalassemia, also known as heterozygous alpha-thalassemia. Affected individuals have small red cells and a mild anemia (microcytosis). If three of the four alpha-globin genes are functional, individuals are completely asymptomatic. Some rare forms of alpha-thalassemia are due to point mutations (non-deletional alpha-thalassemia). Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Alpha(0)-thalassemia is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non- immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.; DISEASE: Hemoglobin H disease (HBH) [MIM:613978]: A form of alpha- thalassemia due to the loss of three alpha genes. This results in high levels of a tetramer of four beta chains (hemoglobin H), causing a severe and life-threatening anemia. Untreated, most patients die in childhood or early adolescence. {ECO:0000269|PubMed:10569720}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Red blood cells.; lymphoreticular;myocardium;colon;skin;bone marrow;whole body;frontal lobe;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;blood;skeletal muscle;pancreas;lung;placenta;liver;spleen;head and neck;kidney;stomach;thymus; . 0.08099 0.20275 . . 4.67458 0.16774 HBAP1 . . . hemoglobin subunit alpha pseudogene 1 . . . . . . . . . . . HBB 1.02493118765881e-08 0.0133834873012062 0.986616502449482 hemoglobin subunit beta FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.; FUNCTION: Spinorphin: functions as an endogenous inhibitor of enkephalin-degrading enzymes such as DPP3, and as a selective antagonist of the P2RX3 receptor which is involved in pain signaling, these properties implicate it as a regulator of pain and inflammation.; DISEASE: Heinz body anemias (HEIBAN) [MIM:140700]: Form of non- spherocytic hemolytic anemia of Dacie type 1. After splenectomy, which has little benefit, basophilic inclusions called Heinz bodies are demonstrable in the erythrocytes. Before splenectomy, diffuse or punctate basophilia may be evident. Most of these cases are probably instances of hemoglobinopathy. The hemoglobin demonstrates heat lability. Heinz bodies are observed also with the Ivemark syndrome (asplenia with cardiovascular anomalies) and with glutathione peroxidase deficiency. {ECO:0000269|PubMed:186485, ECO:0000269|PubMed:2599881, ECO:0000269|PubMed:6259091, ECO:0000269|PubMed:8704193}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Beta-thalassemia (B-THAL) [MIM:613985]: A form of thalassemia. Thalassemias are common monogenic diseases occurring mostly in Mediterranean and Southeast Asian populations. The hallmark of beta-thalassemia is an imbalance in globin-chain production in the adult HbA molecule. Absence of beta chain causes beta(0)-thalassemia, while reduced amounts of detectable beta globin causes beta(+)-thalassemia. In the severe forms of beta- thalassemia, the excess alpha globin chains accumulate in the developing erythroid precursors in the marrow. Their deposition leads to a vast increase in erythroid apoptosis that in turn causes ineffective erythropoiesis and severe microcytic hypochromic anemia. Clinically, beta-thalassemia is divided into thalassemia major which is transfusion dependent, thalassemia intermedia (of intermediate severity), and thalassemia minor that is asymptomatic. {ECO:0000269|PubMed:15481886, ECO:0000269|PubMed:2399911, ECO:0000269|PubMed:6166632, ECO:0000269|PubMed:7693620}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Sickle cell anemia (SKCA) [MIM:603903]: Characterized by abnormally shaped red cells resulting in chronic anemia and periodic episodes of pain, serious infections and damage to vital organs. Normal red blood cells are round and flexible and flow easily through blood vessels, but in sickle cell anemia, the abnormal hemoglobin (called Hb S) causes red blood cells to become stiff. They are C-shaped and resembles a sickle. These stiffer red blood cells can led to microvascular occlusion thus cutting off the blood supply to nearby tissues. {ECO:0000269|PubMed:13464827, ECO:0000269|Ref.10}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Beta-thalassemia, dominant, inclusion body type (B- THALIB) [MIM:603902]: An autosomal dominant form of beta thalassemia characterized by moderate anemia, lifelong jaundice, cholelithiasis and splenomegaly, marked morphologic changes in the red cells, erythroid hyperplasia of the bone marrow with increased numbers of multinucleate red cell precursors, and the presence of large inclusion bodies in the normoblasts, both in the marrow and in the peripheral blood after splenectomy. {ECO:0000269|PubMed:1971109}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Red blood cells. {ECO:0000269|PubMed:6539334}.; myocardium;ovary;choroid;skin;retina;bone marrow;uterus;prostate;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;adrenal cortex;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;kidney; . . 0.08201 -0.005381972 53.50908233 113.2496 2.31723 HBBP1 . . . hemoglobin subunit beta pseudogene 1 . . . . . . . . . . . HBD 0.000155107643467577 0.252090840044314 0.747754052312218 hemoglobin subunit delta FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.; . TISSUE SPECIFICITY: Red blood cells.; ovary;umbilical cord;colon;parathyroid;choroid;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;liver;spleen;kidney;aorta; atrioventricular node;bone marrow; . . 0.481458261 79.03986789 20.28992 0.69337 HBE1 0.0108144244545265 0.620147952057578 0.369037623487895 hemoglobin subunit epsilon 1 FUNCTION: The epsilon chain is a beta-type chain of early mammalian embryonic hemoglobin.; . TISSUE SPECIFICITY: Red blood cells.; unclassifiable (Anatomical System);myocardium;heart;pharynx;blood;bone marrow;breast;whole body;lung;cochlea;bone;liver;spleen;brain;thymus; fetal liver;prostate;fetal brain;placenta;fetal lung;fetal thyroid;bone marrow; 0.32278 0.08735 -0.007201372 53.19061099 16.33304 0.57871 HBEGF 0.830814322298121 0.165676236595189 0.00350944110668997 heparin binding EGF like growth factor FUNCTION: Growth factor that mediates its effects via EGFR, ERBB2 and ERBB4. Required for normal cardiac valve formation and normal heart function. Promotes smooth muscle cell proliferation. May be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts, but not endothelial cells. It is able to bind EGF receptor/EGFR with higher affinity than EGF itself and is a far more potent mitogen for smooth muscle cells than EGF. Also acts as a diphtheria toxin receptor.; . . myocardium;ovary;sympathetic chain;colon;parathyroid;vein;skin;retina;uterus;prostate;whole body;bone;testis;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;bile duct;breast;pancreas;lung;mesenchyma;placenta;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;olfactory bulb;lung;spinal cord; 0.55105 0.43208 -0.007201372 53.19061099 24.22839 0.79590 HBG1 0.0297794697176572 0.591163869673478 0.379056660608865 hemoglobin subunit gamma 1 FUNCTION: Gamma chains make up the fetal hemoglobin F, in combination with alpha chains.; . TISSUE SPECIFICITY: Red blood cells.; unclassifiable (Anatomical System);heart;cartilage;skin;retina;bone marrow;pancreas;lung;frontal lobe;cochlea;placenta;visual apparatus;liver;pituitary gland;testis;spleen;kidney;brain;thymus; fetal liver;prostate;fetal brain;placenta;fetal lung;fetal thyroid;bone marrow; 0.51338 0.78327 . . 4.73605 0.17282 HBG2 0.241303510098989 0.644191317093571 0.11450517280744 hemoglobin subunit gamma 2 FUNCTION: Gamma chains make up the fetal hemoglobin F, in combination with alpha chains.; DISEASE: Cyanosis transient neonatal (TNCY) [MIM:613977]: A disorder characterized by cyanosis in the fetus and neonate, due to a defect in the fetal hemoglobin chain which has reduced affinity for oxygen. Some patients develop anemia resulting from increased destruction of red cells containing abnormal or unstable hemoglobin. The cyanosis resolves spontaneously by 5 to 6 months of age or earlier, as the adult beta-globin chain is produced and replaces the fetal gamma-globin chain. {ECO:0000269|PubMed:19065339, ECO:0000269|PubMed:21561349, ECO:0000269|PubMed:24502349, ECO:0000269|PubMed:2470017, ECO:0000269|PubMed:2483933, ECO:0000269|PubMed:7741137}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Red blood cells.; unclassifiable (Anatomical System);heart;cartilage;skin;retina;bone marrow;pancreas;lung;frontal lobe;cochlea;placenta;visual apparatus;liver;pituitary gland;testis;spleen;kidney;brain;thymus; fetal liver;prostate;fetal brain;placenta;fetal lung;fetal thyroid;bone marrow; 0.44272 0.09558 -0.009020804 52.8544468 11.65671 0.42248 HBM 0.00684674520290924 0.52312386577811 0.470029389018981 hemoglobin subunit mu . . TISSUE SPECIFICITY: Expressed in erythroid tissues. {ECO:0000269|PubMed:15855277}.; liver;spleen; . 0.16742 0.10750 . . 72.49158 1.77448 HBP1 0.770302411913946 0.22962581316835 7.17749177039252e-05 HMG-box transcription factor 1 FUNCTION: Transcriptional repressor that binds to the promoter region of target genes. Plays a role in the regulation of the cell cycle and of the Wnt pathway. Binds preferentially to the sequence 5'-TTCATTCATTCA-3'. Binding to the H1F0 promoter is enhanced by interaction with RB1. Disrupts the interaction between DNA and TCF4. {ECO:0000269|PubMed:10562551, ECO:0000269|PubMed:10958660, ECO:0000269|PubMed:11500377}.; . . myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;gall bladder;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;placenta;hippocampus;amnion;head and neck;kidney;stomach;thymus; superior cervical ganglion;pons;atrioventricular node; 0.55717 0.16564 -0.315847836 31.68789809 56.25857 1.50596 HBQ1 0.00582839332902991 0.489747193743501 0.504424412927469 hemoglobin subunit theta 1 . . . ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;lung;visual apparatus;liver;kidney;brain;bladder; fetal liver;superior cervical ganglion;appendix;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;bone marrow; 0.06438 0.20684 . . 92.48712 2.06748 HBS1L 0.924522220570616 0.0754776289910087 1.50438375464264e-07 HBS1 like translational GTPase . . TISSUE SPECIFICITY: Detected in heart, brain, placenta, liver, muscle, kidney and pancreas. {ECO:0000269|PubMed:9872408}.; unclassifiable (Anatomical System);prostate;lung;placenta;testis;germinal center; superior cervical ganglion;medulla oblongata;occipital lobe;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;cingulate cortex; 0.41898 0.25241 1.225399457 93.24722812 375.67317 4.08629 HBZ 0.0166772462869549 0.474138049776373 0.509184703936672 hemoglobin subunit zeta FUNCTION: The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin.; . TISSUE SPECIFICITY: Detected in fetal erythrocytes (at protein level). {ECO:0000269|PubMed:6171809, ECO:0000269|PubMed:6539334}.; unclassifiable (Anatomical System);myocardium;pancreas;liver;spleen;blood;brain;thymus; . 0.34225 . . . 8.27243 0.30323 HBZP1 . . . hemoglobin subunit zeta pseudogene 1 . . . unclassifiable (Anatomical System);liver;spleen;brain; . . . . . . . HCAR1 0.140999390466245 0.779311972055743 0.079688637478012 hydroxycarboxylic acid receptor 1 FUNCTION: Acts as a receptor for L-lactate and mediates its anti- lipolytic effect through a G(i)-protein-mediated pathway. {ECO:0000269|PubMed:19047060}.; . TISSUE SPECIFICITY: Expressed abundantly in brown and white fat. It also detectable at lower levels in liver, kidney, skeletal muscle, brain and pituitary. Not detected in frontal, temporal and occipital lobes of the cortex, basal forebrain, caudate nucleus, nucleus accumbens and hippocampus. {ECO:0000269|PubMed:11574155, ECO:0000269|PubMed:19047060}.; unclassifiable (Anatomical System);uterus;colon;mammary gland;bladder; globus pallidus; 0.13233 0.08739 -0.356299879 29.31115829 238.79328 3.33717 HCAR2 0.0201092731074374 0.743945709711527 0.235945017181035 hydroxycarboxylic acid receptor 2 FUNCTION: Acts as a high affinity receptor for both nicotinic acid (also known as niacin) and (D)-beta-hydroxybutyrate and mediates increased adiponectin secretion and decreased lipolysis through G(i)-protein-mediated inhibition of adenylyl cyclase. This pharmacological effect requires nicotinic acid doses that are much higher than those provided by a normal diet. Mediates nicotinic acid-induced apoptosis in mature neutrophils. Receptor activation by nicotinic acid results in reduced cAMP levels which may affect activity of cAMP-dependent protein kinase A and phosphorylation of target proteins, leading to neutrophil apoptosis. The rank order of potency for the displacement of nicotinic acid binding is 5- methyl pyrazole-3-carboxylic acid = pyridine-3-acetic acid > acifran > 5-methyl nicotinic acid = acipimox >> nicotinuric acid = nicotinamide. {ECO:0000269|PubMed:17932499}.; . TISSUE SPECIFICITY: Expression largely restricted to adipose tissue and spleen. Expressed on mature neutrophils but not on immature neutrophils or eosinophils. {ECO:0000269|PubMed:12522134, ECO:0000269|PubMed:17932499}.; unclassifiable (Anatomical System);tongue;blood;skin;skeletal muscle;uterus;pancreas;lung;nasopharynx;placenta;hypopharynx;testis;head and neck;spleen;brain; . . . -0.069700724 48.54328851 51.73079 1.42044 HCAR3 6.93117983208457e-06 0.157373990956954 0.842619077863214 hydroxycarboxylic acid receptor 3 FUNCTION: Receptor for 3-OH-octanoid acid mediates a negative feedback regulation of adipocyte lipolysis to counteract prolipolytic influences under conditions of physiological or pathological increases in beta-oxidation rates. Acts as a low affinity receptor for nicotinic acid. This pharmacological effect requires nicotinic acid doses that are much higher than those provided by a normal diet. {ECO:0000269|PubMed:12522134, ECO:0000269|PubMed:19561068}.; . TISSUE SPECIFICITY: Expression largely restricted to adipose tissue and spleen. {ECO:0000269|PubMed:12522134}.; . . . . 0.643056625 84.05284265 4388.50195 13.21909 HCCAT5 . . . hepatocellular carcinoma associated transcript 5 (non-protein coding) . . . . . . . . . . . HCCS 0.950550391243934 0.0492986005275317 0.000151008228534698 holocytochrome c synthase FUNCTION: Links covalently the heme group to the apoprotein of cytochrome c. {ECO:0000250}.; DISEASE: Linear skin defects with multiple congenital anomalies 1 (LSDMCA1) [MIM:309801]: A disorder characterized by dermal, ocular, neurological and cardiac abnormalities. LSDMCA1 main features are unilateral or bilateral microphthalmia, linear skin defects in affected females, and in utero lethality for males. Skin defects are limited to the face and neck, consisting of areas of aplastic skin that heal with age to form hyperpigmented areas. Additional features in female patients include agenesis of the corpus callosum, sclerocornea, chorioretinal abnormalities, infantile seizures, congenital heart defect, mental retardation, and diaphragmatic hernia. Microphthalmia is a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. {ECO:0000269|PubMed:17033964}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;bone marrow;uterus;prostate;atrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pharynx;blood;breast;bile duct;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach; whole brain;superior cervical ganglion;ciliary ganglion;pons; 0.11391 0.19434 0.325313577 73.11276244 16.98395 0.59855 HCFC1 0.999995934499134 4.06550085064359e-06 1.58538527956109e-14 host cell factor C1 FUNCTION: Involved in control of the cell cycle. Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300. Coactivator for EGR2 and GABP2. Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC) complexes (involved in the activation and repression of transcription, respectively) together. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. In case of human herpes simplex virus (HSV) infection, HCFC1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and POU2F1 thereby enabling the transcription of the viral immediate early genes. {ECO:0000269|PubMed:10629049, ECO:0000269|PubMed:10675337, ECO:0000269|PubMed:10779346, ECO:0000269|PubMed:10920196, ECO:0000269|PubMed:12244100, ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:14532282, ECO:0000269|PubMed:15190068, ECO:0000269|PubMed:16624878, ECO:0000269|PubMed:17578910, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:20200153, ECO:0000269|PubMed:9990006}.; DISEASE: Mental retardation, X-linked 3 (MRX3) [MIM:309541]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non- syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. {ECO:0000269|PubMed:23000143}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in fetal tissues and the adult kidney. Present in all tissues tested. {ECO:0000269|PubMed:9389645}.; lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;choroid;skin;bone marrow;uterus;prostate;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.35843 0.15758 -1.456898556 3.862939372 70.30656 1.74352 HCFC1-AS1 . . . HCFC1 antisense RNA 1 . . . . . . . . . . . HCFC1R1 0.000463237063043746 0.429729927030164 0.569806835906792 host cell factor C1 regulator 1 (XPO1 dependent) FUNCTION: Regulates HCFC1 activity by modulating its subcellular localization. Overexpression of HCFC1R1 leads to accumulation of HCFC1 in the cytoplasm. HCFC1R1-mediated export may provide the pool of cytoplasmic HCFC1 required for import of virion-derived VP16 into the nucleus. {ECO:0000269|PubMed:12235138}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12235138}.; ovary;salivary gland;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;larynx;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;muscle;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; whole brain;subthalamic nucleus;thalamus;medulla oblongata;superior cervical ganglion;temporal lobe;prefrontal cortex;globus pallidus;caudate nucleus;skeletal muscle;cingulate cortex; 0.18009 0.10182 0.457594962 78.16112291 1311.04878 6.81197 HCFC2 0.994468276315441 0.0055317179942717 5.69028698406869e-09 host cell factor C2 . . TISSUE SPECIFICITY: Highly expressed in testis. Detected at lower levels in spleen, thymus, prostate, ovary, small intestine and colon. {ECO:0000269|PubMed:10196288}.; unclassifiable (Anatomical System);medulla oblongata;lymph node;ovary;salivary gland;intestine;pharynx;colon;parathyroid;blood;skeletal muscle;bone marrow;prostate;lung;endometrium;bone;thyroid;placenta;visual apparatus;liver;testis;cervix;germinal center;kidney;brain;mammary gland;bladder; testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;skeletal muscle; 0.54137 0.20015 0.084621747 60.31493277 202.17732 3.06842 HCFC2P1 . . . host cell factor C2 pseudogene 1 . . . . . . . . . . . HCG4 . . . HLA complex group 4 (non-protein coding) . . . . . . . . . . . HCG4B . . . HLA complex group 4B (non-protein coding) . . . . . . . . . . . HCG4P1 . . . HLA complex group 4 pseudogene 1 . . . . . . . . . . . HCG4P2 . . . HLA complex group 4 pseudogene 2 . . . . . . . . . . . HCG4P3 . . . HLA complex group 4 pseudogene 3 . . . . . . . . . . . HCG4P4 . . . HLA complex group 4 pseudogene 4 . . . . . . . . . . . HCG4P5 . . . HLA complex group 4 pseudogene 5 . . . . . . . . . . . HCG4P7 . . . HLA complex group 4 pseudogene 7 . . . . . . . . . . . HCG4P8 . . . HLA complex group 4 pseudogene 8 . . . . . . . . . . . HCG4P9 . . . HLA complex group 4 pseudogene 9 . . . . . . . . . . . HCG4P11 . . . HLA complex group 4 pseudogene 11 . . . . . . . . . . . HCG8 . . . HLA complex group 8 . . . . . . . . . . . HCG9 . . . HLA complex group 9 (non-protein coding) . . . . . . . . . . . HCG9P1 . . . HLA complex group 9 pseudogene 1 . . . . . . . . . . . HCG9P2 . . . HLA complex group 9 pseudogene 2 . . . . . . . . . . . HCG9P3 . . . HLA complex group 9 pseudogene 3 . . . . . . . . . . . HCG9P5 . . . HLA complex group 9 pseudogene 5 . . . . . . . . . . . HCG11 . . . HLA complex group 11 (non-protein coding) . . . . . . . . . . . HCG13P . . . HLA complex group 13 pseudogene . . . . . . . . . . . HCG14 . . . HLA complex group 14 (non-protein coding) . . . . . . . . . . . HCG15 . . . HLA complex group 15 (non-protein coding) . . . . . . . . . . . HCG16 . . . HLA complex group 16 (non-protein coding) . . . . . . . . . . . HCG17 . . . HLA complex group 17 (non-protein coding) . . . . . . . . . . . HCG18 . . . HLA complex group 18 (non-protein coding) . . . . . . . . . . . HCG19P . . . HLA complex group 19 pseudogene . . . . . . . . . . . HCG20 . . . HLA complex group 20 (non-protein coding) . . . . . . . . . . . HCG21 . . . HLA complex group 21 (non-protein coding) . . . . . . . . . . . HCG22 . . . HLA complex group 22 . . TISSUE SPECIFICITY: Detected in the brain, lung, spleen, thymus and prostate. {ECO:0000269|PubMed:20981447}.; . . . . . . . . HCG23 . . . HLA complex group 23 (non-protein coding) . . . . . . . . . . . HCG24 . . . HLA complex group 24 (non-protein coding) . . . . . . . . . . . HCG25 . . . HLA complex group 25 (non-protein coding) . . . . . . . . . . . HCG26 . . . HLA complex group 26 (non-protein coding) . . . . . . . . . . . HCG27 . . . HLA complex group 27 (non-protein coding) . . . . . . . . . . . HCHOLA4 . . . hypercholesterolemia, autosomal dominant 4 . . . . . . . . . . . HCK . . . HCK proto-oncogene, Src family tyrosine kinase FUNCTION: Non-receptor tyrosine-protein kinase found in hematopoietic cells that transmits signals from cell surface receptors and plays an important role in the regulation of innate immune responses, including neutrophil, monocyte, macrophage and mast cell functions, phagocytosis, cell survival and proliferation, cell adhesion and migration. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as FCGR1A and FCGR2A, but also CSF3R, PLAUR, the receptors for IFNG, IL2, IL6 and IL8, and integrins, such as ITGB1 and ITGB2. During the phagocytic process, mediates mobilization of secretory lysosomes, degranulation, and activation of NADPH oxidase to bring about the respiratory burst. Plays a role in the release of inflammatory molecules. Promotes reorganization of the actin cytoskeleton and actin polymerization, formation of podosomes and cell protrusions. Inhibits TP73-mediated transcription activation and TP73-mediated apoptosis. Phosphorylates CBL in response to activation of immunoglobulin gamma Fc region receptors. Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, GAB2, RAPGEF1, STAT5B, TP73, VAV1 and WAS. {ECO:0000269|PubMed:10092522, ECO:0000269|PubMed:10779760, ECO:0000269|PubMed:10973280, ECO:0000269|PubMed:11741929, ECO:0000269|PubMed:11896602, ECO:0000269|PubMed:12411494, ECO:0000269|PubMed:15010462, ECO:0000269|PubMed:15952790, ECO:0000269|PubMed:15998323, ECO:0000269|PubMed:17310994, ECO:0000269|PubMed:17535448, ECO:0000269|PubMed:19114024, ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:20452982, ECO:0000269|PubMed:21338576, ECO:0000269|PubMed:7535819, ECO:0000269|PubMed:8132624, ECO:0000269|PubMed:9406996, ECO:0000269|PubMed:9407116}.; DISEASE: Note=Aberrant activation of HCK by HIV-1 protein Nef enhances HIV-1 replication and contributes to HIV-1 pathogenicity.; DISEASE: Note=Aberrant activation of HCK, e.g. by the BCR-ABL fusion protein, promotes cancer cell proliferation.; TISSUE SPECIFICITY: Detected in monocytes and neutrophils (at protein level). Expressed predominantly in cells of the myeloid and B-lymphoid lineages. Highly expressed in granulocytes. Detected in tonsil. {ECO:0000269|PubMed:3453117, ECO:0000269|PubMed:8064233, ECO:0000269|PubMed:8995234}.; lymphoreticular;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;iris;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;urinary;blood;lens;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland; whole blood;bone marrow; 0.64241 0.53209 -0.023789244 52.09365416 180.49053 2.92020 HCL1 . . . hair color 1 (brown) . . . . . . . . . . . HCL2 . . . hair color 2 (red) . . . . . . . . . . . HCL3 . . . hair color 3 (brown) . . . . . . . . . . . HCLS1 5.08798891518146e-05 0.992780875577451 0.00716824453339724 hematopoietic cell-specific Lyn substrate 1 FUNCTION: Substrate of the antigen receptor-coupled tyrosine kinase. Plays a role in antigen receptor signaling for both clonal expansion and deletion in lymphoid cells. May also be involved in the regulation of gene expression.; . TISSUE SPECIFICITY: Expressed only in tissues and cells of hematopoietic origin.; lymphoreticular;myocardium;ovary;umbilical cord;sympathetic chain;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;endometrium;larynx;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney; superior cervical ganglion;lymph node;white blood cells;ciliary ganglion;atrioventricular node;whole blood;trigeminal ganglion;tonsil;bone marrow; 0.51692 0.13272 0.536463361 81.06864827 3623.93429 11.67799 HCN1 0.953138502832124 0.0468612743078507 2.22860024976317e-07 hyperpolarization activated cyclic nucleotide gated potassium channel 1 FUNCTION: Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). May mediate responses to sour stimuli. {ECO:0000269|PubMed:15351778}.; DISEASE: Epileptic encephalopathy, early infantile, 24 (EIEE24) [MIM:615871]: A disease characterized by early-onset seizures, intellectual disability of varying degrees, and behavioral disturbances or autistic features in most individuals. {ECO:0000269|PubMed:24747641}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in brain, in particular in amygdala and hippocampus, while expression in caudate nucleus, corpus callosum, substantia nigra, subthalamic nucleus and thalamus is very low or not detectable. Detected at very low levels in muscle and pancreas. {ECO:0000269|PubMed:9630217}.; unclassifiable (Anatomical System);optic nerve;macula lutea;fovea centralis;choroid;lens;brain;skeletal muscle;retina; superior cervical ganglion;adrenal gland;atrioventricular node;cerebellum; 0.58066 0.16306 -0.758599262 13.32861524 214.69878 3.16077 HCN2 0.832343161848257 0.167509635247704 0.000147202904039401 hyperpolarization activated cyclic nucleotide gated potassium channel 2 FUNCTION: Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron. Produces a large instantaneous current. Modulated by intracellular chloride ions and pH; acidic pH shifts the activation to more negative voltages (By similarity). {ECO:0000250, ECO:0000269|PubMed:10228147, ECO:0000269|PubMed:10524219}.; . TISSUE SPECIFICITY: Highly expressed throughout the brain. Detected at low levels in heart. {ECO:0000269|PubMed:10228147, ECO:0000269|PubMed:9630217}.; unclassifiable (Anatomical System);islets of Langerhans;colon;blood;choroid;fovea centralis;lens;retina;optic nerve;lung;frontal lobe;macula lutea;testis;brain; amygdala;occipital lobe;heart;prefrontal cortex;atrioventricular node;caudate nucleus;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.16077 . . . 2164.49201 8.55958 HCN3 0.0150933826344395 0.979144122306231 0.00576249505932915 hyperpolarization activated cyclic nucleotide gated potassium channel 3 FUNCTION: Hyperpolarization-activated potassium channel. May also facilitate the permeation of sodium ions. {ECO:0000269|PubMed:16043489}.; . TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:16043489}.; . . 0.13001 0.13176 0.069852974 59.10592121 364.06739 4.03876 HCN4 0.234597783260834 0.765098319511583 0.000303897227583155 hyperpolarization activated cyclic nucleotide gated potassium channel 4 FUNCTION: Hyperpolarization-activated ion channel with very slow activation and inactivation exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) that regulate the rhythm of heart beat. May contribute to the native pacemaker currents in neurons (Ih). May mediate responses to sour stimuli. {ECO:0000269|PubMed:10228147, ECO:0000269|PubMed:10430953, ECO:0000269|PubMed:16407510, ECO:0000269|PubMed:19165230, ECO:0000269|PubMed:20829353}.; DISEASE: Sick sinus syndrome 2 (SSS2) [MIM:163800]: The term 'sick sinus syndrome' encompasses a variety of conditions caused by sinus node dysfunction. The most common clinical manifestations are syncope, presyncope, dizziness, and fatigue. Electrocardiogram typically shows sinus bradycardia, sinus arrest, and/or sinoatrial block. Episodes of atrial tachycardias coexisting with sinus bradycardia ('tachycardia-bradycardia syndrome') are also common in this disorder. SSS occurs most often in the elderly associated with underlying heart disease or previous cardiac surgery, but can also occur in the fetus, infant, or child without heart disease or other contributing factors. SSS2 onset is in utero or at birth. {ECO:0000269|PubMed:15123648, ECO:0000269|PubMed:16407510, ECO:0000269|PubMed:20662977}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Brugada syndrome 8 (BRGDA8) [MIM:613123]: A tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs, the individual will faint and may die in a few minutes if the heart is not reset. {ECO:0000269|PubMed:19165230}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in thalamus, testis and in heart, both in ventricle and atrium. Detected at much lower levels in amygdala, substantia nigra, cerebellum and hippocampus. {ECO:0000269|PubMed:10228147, ECO:0000269|PubMed:10430953}.; unclassifiable (Anatomical System);frontal lobe;heart;brain; superior cervical ganglion;testis;ciliary ganglion;trigeminal ganglion; 0.25692 0.13980 . . 277.28874 3.56675 HCP5 . . . HLA complex P5 (non-protein coding) . . TISSUE SPECIFICITY: Expressed in lymphoid tissues; Detected in spleen as well as in B-cell lines, NK cell lines and activated lymphocytes. {ECO:0000269|PubMed:8462994}.; . . . . . . . . HCP5B . . . HLA complex P5B (non-protein coding) . . . . . . . . . . . HCRT 0.502440434384708 0.425620861320929 0.0719387042943624 hypocretin (orexin) neuropeptide precursor FUNCTION: Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested. Orexin-A binds to both OX1R and OX2R with a high affinity, whereas orexin-B binds only to OX2R with a similar high affinity.; DISEASE: Narcolepsy 1 (NRCLP1) [MIM:161400]: Neurological disabling sleep disorder, characterized by excessive daytime sleepiness, sleep fragmentation, symptoms of abnormal rapid-eye- movement (REM) sleep, cataplexy, hypnagogic hallucinations, and sleep paralysis. Cataplexy is a sudden loss of muscle tone triggered by emotions, which is the most valuable clinical feature used to diagnose narcolepsy. Human narcolepsy is primarily a sporadically occurring disorder but familial clustering has been observed. {ECO:0000269|PubMed:10973318}. Note=The disease is caused by mutations affecting the gene represented in this entry. Human narcolepsy is associated with a deficient orexin system. Orexins are absent and/or greatly diminished in the brain and cerebrospinal fluid (CSF) of most narcoleptic patients.; TISSUE SPECIFICITY: Abundantly expressed in subthalamic nucleus but undetectable in other brain regions tested (hypothalamus was not tested) and in heart, placenta, lung, liver, skeletal muscle, kidney and pancreas.; unclassifiable (Anatomical System);frontal lobe; superior cervical ganglion;hypothalamus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14911 0.34337 -0.247889024 35.98726115 21.78034 0.73314 HCRTR1 0.261800018351598 0.732497437624627 0.00570254402377455 hypocretin receptor 1 FUNCTION: Moderately selective excitatory receptor for orexin-A and, with a lower affinity, for orexin-B neuropeptide. Seems to be exclusively coupled to the G(q) subclass of heteromeric G proteins, which activates the phospholipase C mediated signaling cascade (By similarity). {ECO:0000250}.; . . . . 0.15533 0.15015 0.154398214 64.73814579 4030.26984 12.57499 HCRTR2 0.0636440358462457 0.933147715412349 0.00320824874140512 hypocretin receptor 2 FUNCTION: Nonselective, high-affinity receptor for both orexin-A and orexin-B neuropeptides.; . . . . 0.16728 0.11868 0.707379532 85.62750649 106.09434 2.23510 HCST 0.0119335980806641 0.640918781493266 0.34714762042607 hematopoietic cell signal transducer FUNCTION: Transmembrane adapter protein which associates with KLRK1 to form an activation receptor KLRK1-HCST in lymphoid and myeloid cells; this receptor plays a major role in triggering cytotoxicity against target cells expressing cell surface ligands such as MHC class I chain-related MICA and MICB, and UL16-binding proteins (ULBPs); these ligands are up-regulated by stress conditions and pathological state such as viral infection and tumor transformation. Functions as docking site for PI3-kinase PIK3R1 and GRB2. Interaction of ULBPs with KLRK1-HCST triggers calcium mobilization and activation of the PIK3R1, MAP2K/ERK, and JAK2/STAT5 signaling pathways. Both PIK3R1 and GRB2 are required for full KLRK1-HCST-mediated activation and ultimate killing of target cells. In NK cells, KLRK1-HCST signaling directly induces cytotoxicity and enhances cytokine production initiated via DAP12/TYROBP-associated receptors. In T-cells, it provides primarily costimulation for TCR-induced signals. KLRK1-HCST receptor plays a role in immune surveillance against tumors and is required for cytolysis of tumors cells; indeed, melanoma cells that do not express KLRK1 ligands escape from immune surveillance mediated by NK cells. {ECO:0000269|PubMed:10426994, ECO:0000269|PubMed:10528161, ECO:0000269|PubMed:11015446, ECO:0000269|PubMed:11777960, ECO:0000269|PubMed:12740575, ECO:0000269|PubMed:12740576, ECO:0000269|PubMed:16002667, ECO:0000269|PubMed:16339517, ECO:0000269|PubMed:16582911, ECO:0000269|PubMed:18097042}.; . TISSUE SPECIFICITY: Predominantly expressed in hemopoietic cells such as NK cells, subset of T-cells and monocytes. Detected in leukocytes, spleen, and thymus. {ECO:0000269|PubMed:10528161}.; unclassifiable (Anatomical System);pancreas;lung;liver;spleen;blood;kidney;germinal center;brain;stomach;bone marrow; . 0.24247 0.19222 0.635788962 83.63411182 18.78205 0.64931 HCVS . . . human coronavirus sensitivity . . . . . . . . . . . HDAC1 0.937916989643132 0.0620807742161009 2.23614076676165e-06 histone deacetylase 1 FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST- mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation. {ECO:0000269|PubMed:12837748, ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:17996965, ECO:0000269|PubMed:19081374, ECO:0000269|PubMed:19343227}.; . TISSUE SPECIFICITY: Ubiquitous, with higher levels in heart, pancreas and testis, and lower levels in kidney and brain.; . . 0.99856 0.91877 -0.692458599 14.96815287 496.44795 4.57986 HDAC1P1 . . . histone deacetylase 1 pseudogene 1 . . . . . . . . . . . HDAC1P2 . . . histone deacetylase 1 pseudogene 2 . . . . . . . . . . . HDAC2 0.999390588066461 0.000609408768523133 3.16501545758175e-09 histone deacetylase 2 FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation. Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A. {ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:21965678}.; . TISSUE SPECIFICITY: Widely expressed; lower levels in brain and lung.; . . 0.95245 0.84052 -0.119252484 44.53880632 722.29744 5.33473 HDAC3 0.955038023763879 0.044960983331965 9.92904155755059e-07 histone deacetylase 3 FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys- 27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression. Probably participates in the regulation of transcription through its binding to the zinc-finger transcription factor YY1; increases YY1 repression activity. Required to repress transcription of the POU1F1 transcription factor. Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation (PubMed:21444723, PubMed:23911289). Contributes, together with XBP1 isoform 1, to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI(3)K/mTORC2/Akt-dependent signaling pathway leading to endothelial cell (EC) survival under disturbed flow/oxidative stress (PubMed:25190803). {ECO:0000269|PubMed:21444723, ECO:0000269|PubMed:23911289, ECO:0000269|PubMed:25190803}.; . TISSUE SPECIFICITY: Widely expressed.; ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;skeletal muscle;pancreas;lung;epididymis;placenta;visual apparatus;duodenum;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;trigeminal ganglion;parietal lobe;cerebellum; 0.96555 0.64888 -0.029247611 51.40363293 98.72035 2.14866 HDAC4 0.999989726820827 1.02731791418582e-05 3.06811979822235e-14 histone deacetylase 4 FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. {ECO:0000269|PubMed:10523670, ECO:0000269|PubMed:24413532}.; DISEASE: Brachydactyly-mental retardation syndrome (BDMR) [MIM:600430]: A syndrome resembling the physical anomalies found in Albright hereditary osteodystrophy. Common features are mild facial dysmorphism, congenital heart defects, distinct brachydactyly type E, mental retardation, developmental delay, seizures, autism spectrum disorder, and stocky build. Soft tissue ossification is absent, and there are no abnormalities in parathyroid hormone or calcium metabolism. {ECO:0000269|PubMed:20691407, ECO:0000269|PubMed:23188045, ECO:0000269|PubMed:24715439}. Note=The gene represented in this entry is involved in disease pathogenesis. HDAC4 point mutations and chromosomal microdeletions encompassing this gene have been found in BDMR patients (PubMed:20691407, PubMed:24715439, PubMed:23188045). However, HDAC4 haploinsufficiency is not fully penetrant and multiple genes may contribute to manifestation of the full phenotypic spectrum (PubMed:24715439, PubMed:23188045). {ECO:0000269|PubMed:20691407, ECO:0000269|PubMed:23188045, ECO:0000269|PubMed:24715439}.; TISSUE SPECIFICITY: Ubiquitous.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;thyroid;bone;testis;amniotic fluid;brain;unclassifiable (Anatomical System);amygdala;heart;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;head and neck;kidney;mammary gland;stomach; . 0.46692 0.30959 -2.848385772 0.607454588 143.07556 2.60765 HDAC5 0.999808248473516 0.000191751524916634 1.56743431230296e-12 histone deacetylase 5 FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. {ECO:0000269|PubMed:24413532}.; . TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;cervix;kidney;mammary gland;stomach;thymus; . 0.42557 0.28748 -1.280491183 5.16631281 171.08527 2.85329 HDAC6 0.99992079805848 7.92019195677164e-05 2.1952264899771e-11 histone deacetylase 6 FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. {ECO:0000250, ECO:0000269|PubMed:12024216, ECO:0000269|PubMed:17846173, ECO:0000269|PubMed:24413532}.; DISEASE: Chondrodysplasia with platyspondyly, distinctive brachydactyly, hydrocephaly, and microphthalmia (CDP-PBHM) [MIM:300863]: A disease characterized by chondrodysplasia, severe platyspondyly, hydrocephaly, and facial features with microphthalmia. Bone abnormalities include a distinctive metaphyseal cupping of the metacarpals, metatarsals, and phalanges. Affected females show a milder phenotype with small stature, sometimes associated with body asymmetry and mild mental retardation. {ECO:0000269|PubMed:20181727}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;umbilical cord;skin;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;urinary;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);cerebellum cortex;hypothalamus;lung;mesenchyma;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;cerebellum peduncles;adrenal cortex;pons;kidney;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;cerebellum; 0.14620 0.18896 0.069852974 59.10592121 228.99662 3.26923 HDAC7 0.998019873410435 0.0019801261259853 4.63579522769778e-10 histone deacetylase 7 FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity). May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene. Positively regulates the transcriptional repressor activity of FOXP3 (PubMed:17360565). {ECO:0000250|UniProtKB:Q8C2B3, ECO:0000269|PubMed:12239305, ECO:0000269|PubMed:17360565}.; . . smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;oesophagus;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;placenta;amnion;head and neck;kidney;stomach; . 0.11030 . -0.038558137 50.51899033 940.4494 5.94619 HDAC8 0.922707724679457 0.0771972041302312 9.50711903119025e-05 histone deacetylase 8 FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility. {ECO:0000269|PubMed:10748112, ECO:0000269|PubMed:10922473, ECO:0000269|PubMed:10926844, ECO:0000269|PubMed:14701748, ECO:0000269|PubMed:22885700}.; DISEASE: Cornelia de Lange syndrome 5 (CDLS5) [MIM:300882]: A form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. It is characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies. {ECO:0000269|PubMed:22885700}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Wilson-Turner X-linked mental retardation syndrome (WTS) [MIM:309585]: A neurologic disorder characterized by severe intellectual disability, dysmorphic facial features, hypogonadism, short stature, and truncal obesity. Affected females have a milder phenotype than affected males. {ECO:0000269|PubMed:22889856}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Weakly expressed in most tissues. Expressed at higher level in heart, brain, kidney and pancreas and also in liver, lung, placenta, prostate and kidney. {ECO:0000269|PubMed:10926844, ECO:0000269|PubMed:14701748, ECO:0000269|PubMed:15772115, ECO:0000269|PubMed:16538051}.; . . 0.18055 0.12564 -0.273576253 33.97027601 9.87212 0.36173 HDAC9 0.998375125074442 0.0016248749138385 1.17196112074122e-11 histone deacetylase 9 FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Represses MEF2-dependent transcription.; DISEASE: Note=A chromosomal aberration involving HDAC9 is found in a family with Peters anomaly. Translocation t(1;7)(q41;p21) with TGFB2 resulting in lack of HDAC9 protein. {ECO:0000269|PubMed:12706107}.; TISSUE SPECIFICITY: Broadly expressed, with highest levels in brain, heart, muscle and testis. Isoform 3 is present in human bladder carcinoma cells (at protein level). {ECO:0000269|PubMed:10655483, ECO:0000269|PubMed:11535832, ECO:0000269|PubMed:12590135, ECO:0000269|PubMed:12706107}.; unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;optic nerve;lung;cerebral cortex;larynx;placenta;macula lutea;visual apparatus;liver;pituitary gland;testis;head and neck;germinal center;brain; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;medulla oblongata;temporal lobe;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.93284 0.71489 -1.061810361 7.519462137 78.75617 1.87350 HDAC10 3.2788087078515e-12 0.149158505614695 0.850841494382026 histone deacetylase 10 FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.; . TISSUE SPECIFICITY: Ubiquitous. High expression in liver, spleen, pancreas and kidney.; ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;spinal ganglion;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; . 0.10737 0.15425 -0.172654315 40.63458363 807.74818 5.59736 HDAC11 0.0447802083550292 0.949672918303024 0.00554687334194642 histone deacetylase 11 FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. {ECO:0000269|PubMed:11948178}.; . TISSUE SPECIFICITY: Weakly expressed in most tissues. Strongly expressed in brain, heart, skeletal muscle, kidney and testis.; myocardium;medulla oblongata;ovary;sympathetic chain;colon;choroid;fovea centralis;retina;uterus;prostate;optic nerve;frontal lobe;testis;brain;spinal ganglion;gall bladder;unclassifiable (Anatomical System);muscle;lens;lung;placenta;hippocampus;visual apparatus;macula lutea;kidney; superior cervical ganglion;testis - interstitial;temporal lobe;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14826 0.14319 -0.670411825 15.61689078 10.99153 0.39808 HDAC11-AS1 . . . HDAC11 antisense RNA 1 . . . . . . . . . . . HDC 0.514822964237295 0.485144623417719 3.24123449851232e-05 histidine decarboxylase FUNCTION: Catalyzes the biosynthesis of histamine from histidine. {ECO:0000269|PubMed:22767596}.; . . unclassifiable (Anatomical System);nasopharynx;testis; superior cervical ganglion;hypothalamus; 0.19079 0.25621 -0.244249595 36.17008728 832.23192 5.65250 HDDC2 0.00127336194428677 0.854649077562963 0.14407756049275 HD domain containing 2 . . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;pineal body;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;amygdala;thalamus;superior cervical ganglion;occipital lobe;medulla oblongata;hypothalamus;temporal lobe;spinal cord;pons;atrioventricular node;caudate nucleus;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.08930 0.11207 -0.229483771 36.86010852 33.61139 1.03747 HDDC3 0.0718306276352796 0.741959546508552 0.186209825856168 HD domain containing 3 FUNCTION: ppGpp hydrolyzing enzyme involved in starvation response. {ECO:0000269|PubMed:20818390}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);heart;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney; whole brain; 0.13691 0.11058 -0.031067188 51.03798066 57.05049 1.52044 HDGF 0.269699273955011 0.705644263336704 0.024656462708285 hepatoma-derived growth factor FUNCTION: Heparin-binding protein, with mitogenic activity for fibroblasts. Acts as a transcriptional repressor. {ECO:0000269|PubMed:17974029}.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;tonsil;heart;tongue;adrenal cortex;pharynx;blood;skeletal muscle;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;pia mater;cornea;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus; fetal liver;kidney;trigeminal ganglion;cerebellum;bone marrow; 0.66799 . 0.17280645 65.75843359 1546.08712 7.29032 HDGFL1 0.313343421346475 0.6160725220761 0.070584056577425 hepatoma derived growth factor-like 1 . . . medulla oblongata; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.11613 . . . 1396.82078 6.98926 HDGFP1 . . . hepatoma-derived growth factor pseudogene 1 . . . . . . . . . . . HDHD2 0.000427885483918572 0.648067114333069 0.351505000183013 haloacid dehalogenase like hydrolase domain containing 2 . . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;larynx;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;lens;pancreas;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;whole brain;amygdala;thalamus;superior cervical ganglion;occipital lobe;medulla oblongata;hypothalamus;caudate nucleus;subthalamic nucleus;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.08068 0.08621 -0.071520315 48.34866714 305.46157 3.72194 HDHD3 0.005551021155164 0.717212424052774 0.277236554792062 haloacid dehalogenase like hydrolase domain containing 3 . . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pineal body;muscle;blood;lens;skeletal muscle;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;aorta;stomach;thymus; superior cervical ganglion;adrenal gland;thyroid;liver;atrioventricular node; 0.07781 0.09884 -0.115612493 45.12856806 59.57083 1.56606 HDLBP 0.999998382970679 1.61702932066634e-06 6.87099110909431e-17 high density lipoprotein binding protein FUNCTION: Appears to play a role in cell sterol metabolism. It may function to protect cells from over-accumulation of cholesterol.; . . ovary;salivary gland;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;oesophagus;larynx;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; testis - interstitial;prostate;smooth muscle;testis - seminiferous tubule;placenta;thyroid;liver;testis;skeletal muscle; 0.83358 0.17552 -1.368693559 4.482189196 124.99167 2.43155 HDLCQ1 . . . high density lipoprotein cholesterol level QTL 1 . . . . . . . . . . . HDX 0.517074458559921 0.482150619475215 0.000774921964863686 highly divergent homeobox . . . unclassifiable (Anatomical System);bile duct;lung;cochlea;tongue;islets of Langerhans;visual apparatus;head and neck;kidney;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.39060 0.10362 -0.025608647 51.91672564 692.43533 5.24837 HEATR1 0.999999993216506 6.78349365199169e-09 9.21897994303394e-25 HEAT repeat containing 1 FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. Involved in ribosome biosynthesis (By similarity). {ECO:0000250}.; . . . . 0.09748 0.08985 2.322745612 98.36635999 19763.61088 30.12571 HEATR3 0.000127664947241789 0.990470629254393 0.00940170579836534 HEAT repeat containing 3 . . . unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;colon;skeletal muscle;skin;uterus;breast;pancreas;lung;bone;placenta;liver;pituitary gland;testis;spleen;cervix;kidney;brain;stomach; amygdala;superior cervical ganglion;white blood cells;atrioventricular node; 0.10176 . 0.110306132 62.00165133 346.43566 3.94743 HEATR4 6.23228339805708e-17 0.0924982325592827 0.907501767440717 HEAT repeat containing 4 . . . colon;choroid;fovea centralis;skin;retina;uterus;optic nerve;whole body;testis;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lens;lung;placenta;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;kidney;stomach; . 0.07879 0.07513 -0.009234793 52.3767398 905.99964 5.85717 HEATR5A . . . HEAT repeat containing 5A . . . . . 0.22930 . . . 4462.98132 13.39987 HEATR5B 8.10479286093348e-10 0.999999998441817 7.47703642034084e-10 HEAT repeat containing 5B . . . ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;cochlea;cerebral cortex;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;hypopharynx;spleen;head and neck;kidney;stomach; dorsal root ganglion;occipital lobe;superior cervical ganglion;subthalamic nucleus;medulla oblongata;fetal brain;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe; 0.25312 . -2.513844451 0.914130691 1161.22267 6.48464 HEATR6 4.94357747313783e-10 0.997343151916292 0.00265684758935036 HEAT repeat containing 6 FUNCTION: Amplification-dependent oncogene.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;gum;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;muscle;urinary;adrenal cortex;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.29209 0.09791 -0.990222991 8.634111819 1456.38452 7.11769 HEATR9 . . . HEAT repeat containing 9 . . . . . 0.05583 . 0.979225112 90.42816702 . . HEBP1 8.07251624878692e-05 0.318238435431312 0.681680839406201 heme binding protein 1 FUNCTION: May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N- methylprotoporphyrin with similar affinities. {ECO:0000269|PubMed:12413491}.; . . lymphoreticular;ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;cochlea;endometrium;gum;bone;pituitary gland;testis;amniotic fluid;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pineal body;urinary;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;alveolus;spleen;kidney;mammary gland;stomach;aorta;cerebellum; . 0.14187 0.13530 -0.183570861 39.95046001 142.53467 2.60361 HEBP2 0.000947405784931283 0.578418665091517 0.420633929123552 heme binding protein 2 FUNCTION: Can promote mitochondrial permeability transition and facilitate necrotic cell death under different types of stress conditions. Does not bind hemin. {ECO:0000269|PubMed:17098234}.; . TISSUE SPECIFICITY: Detected in placenta. {ECO:0000269|PubMed:2018407}.; lymphoreticular;myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;alveolus;kidney;mammary gland;stomach;aorta;thymus; prostate;adipose tissue;skeletal muscle; 0.10072 0.10769 0.104848986 61.49445624 44.44389 1.27448 HECA 0.347342389373824 0.639182886128926 0.0134747244972503 hdc homolog, cell cycle regulator FUNCTION: May play an important role in some human cancers. May be part of the regulatory mechanism in the development of epithelial tube networks such as the circulatory system and lungs. {ECO:0000303|PubMed:11696983}.; . . . . 0.23021 0.15297 -0.670411825 15.61689078 12.19968 0.44186 HECTD1 0.999999999999764 2.35638401796607e-13 1.26711730883596e-35 HECT domain E3 ubiquitin protein ligase 1 FUNCTION: Probable E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. May be required for development of the head mesenchyme and neural tube closure (By similarity). {ECO:0000250}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;cingulate cortex;skeletal muscle; 0.71166 0.10385 -2.227040428 1.332861524 686.62409 5.23205 HECTD2 0.994416490072573 0.00558350874950637 1.17792100697812e-09 HECT domain E3 ubiquitin protein ligase 2 FUNCTION: Probable E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;tongue;islets of Langerhans;parathyroid;retina;uterus;prostate;whole body;lung;cochlea;endometrium;bone;thyroid;placenta;hippocampus;testis;head and neck;germinal center;kidney;brain;artery;aorta; superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion;cerebellum; 0.19567 0.09606 -0.091746757 46.91554612 41.29743 1.20711 HECTD2-AS1 . . . HECTD2 antisense RNA 1 . . . . . . . . . . . HECTD3 0.0170427799161936 0.982949029154797 8.19092900975493e-06 HECT domain E3 ubiquitin protein ligase 3 FUNCTION: E3 ubiquitin ligases accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of TRIOBP and its subsequent proteasomal degradation, thus faciliting cell cycle progression by regulating the turn-over of TRIOBP. Mediates also ubiquitination of STX8 (By similarity). {ECO:0000250, ECO:0000269|PubMed:18194665}.; . . . . 0.16671 0.11719 -0.907472583 10.07313046 819.47471 5.62322 HECTD4 0.99999999999996 4.0137220455537e-14 5.76573544380311e-41 HECT domain E3 ubiquitin protein ligase 4 FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000250}.; . . . . 0.39833 0.11010 . . 278.35608 3.57584 HECW1 0.999999893537852 1.06462147576184e-07 3.72575270305492e-21 HECT, C2 and WW domain containing E3 ubiquitin protein ligase 1 FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent degradation of DVL1. Also targets the mutant SOD1 protein involved in familial amyotrophic lateral sclerosis (FALS). Forms cytotoxic aggregates with DVL1, SSR3 and mutant SOD1 that lead to motor neuron death in FALS. {ECO:0000269|PubMed:14684739}.; . TISSUE SPECIFICITY: Predominantly expressed in neurons of adult and fetal brain. Weakly expressed in the kidney. {ECO:0000269|PubMed:14684739}.; unclassifiable (Anatomical System);hypothalamus;testis;kidney;brain;skin; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.33439 0.17385 -0.42995042 24.72281198 490.10632 4.55570 HECW1-IT1 . . . HECW1 intronic transcript 1 . . . lung;testis; . . . . . . . HECW2 0.99999585183338 4.14816661955249e-06 1.14281805642054e-18 HECT, C2 and WW domain containing E3 ubiquitin protein ligase 2 FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of TP73. Acts to stabilize TP73 and enhance activation of transcription by TP73. {ECO:0000269|PubMed:12890487}.; . TISSUE SPECIFICITY: Predominantly expressed in adult brain, lung and heart. {ECO:0000269|PubMed:12890487}.; unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;colon;skin;skeletal muscle;uterus;lung;larynx;liver;testis;cervix;head and neck;spleen;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.46115 0.10644 -2.471501108 0.979004482 280.44408 3.58901 HEG1 6.98959647837495e-06 0.998950548736638 0.00104246166688373 heart development protein with EGF like domains 1 FUNCTION: Receptor component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity May act through the stabilization of endothelial cell junctions. {ECO:0000250}.; . . myocardium;umbilical cord;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;ganglion;endometrium;larynx;bone;thyroid;iris;testis;amniotic fluid;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;spinal cord;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;heart;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.35779 . 0.992010122 90.49893843 5583.21586 15.45469 HEIH . . . hepatocellular carcinoma up-regulated EZH2-associated long non-coding RNA . . . . . . . . . . . HELB 2.01687819135373e-13 0.201004527849826 0.798995472149972 helicase (DNA) B FUNCTION: Unwinds duplex DNA with 5'-3' polarity. Has single- strand DNA-dependent ATPase and DNA helicase activities. Prefers ATP and dATP as substrates. During S phase, may facilitate cellular recovery from replication stress. {ECO:0000269|PubMed:12181327, ECO:0000269|PubMed:22194613}.; . TISSUE SPECIFICITY: Highly expressed in testis and thymus and weakly in liver, spleen, kidney and brain. {ECO:0000269|PubMed:12181327}.; unclassifiable (Anatomical System);lymph node;heart;choroid;fovea centralis;lens;skeletal muscle;skin;retina;uterus;optic nerve;macula lutea;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skin; 0.03646 0.09863 1.076540831 91.72564284 4335.69084 13.10867 HELLPAR . . . HELLP associated long non-coding RNA . . . . . . . . . . . HELLS 0.999418431126719 0.000581568872322923 9.57964285891944e-13 helicase, lymphoid-specific FUNCTION: Plays an essential role in normal development and survival. Involved in regulation of the expansion or survival of lymphoid cells. Required for de novo or maintenance DNA methylation. May control silencing of the imprinted CDKN1C gene through DNA methylation. May play a role in formation and organization of heterochromatin, implying a functional role in the regulation of transcription and mitosis (By similarity). {ECO:0000250|UniProtKB:Q60848}.; . TISSUE SPECIFICITY: Highly expressed in proliferative tissues such as adult thymus and testis, and expressed at lower levels in uterus, small intestine, colon, and peripheral blood mononuclear cells. Also expressed in neoplastic cell lines including those derived from myeloid and lymphoid leukemias. {ECO:0000269|PubMed:10910076}.; ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;cochlea;endometrium;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);urinary;pharynx;blood;skeletal muscle;breast;lung;visual apparatus;liver;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;pons; 0.63819 0.32258 0.020302773 55.60863411 64.90459 1.65485 HELQ 4.80499059166513e-11 0.789098827052868 0.210901172899082 helicase, POLQ-like FUNCTION: DNA-dependent ATPase and 5' to 3' DNA helicase. {ECO:0000269|PubMed:11751861}.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;spinal cord;blood;skin;skeletal muscle;retina;bone marrow;uterus;prostate;lung;cochlea;endometrium;thyroid;liver;testis;spleen;cervix;germinal center;kidney;brain;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;appendix;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; . . 1.783955458 96.85656995 1460.39054 7.12685 HELT 0.0473977091398056 0.855720896906832 0.096881393953363 helt bHLH transcription factor FUNCTION: Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGCG-3'. {ECO:0000250}.; . . . . 0.39188 0.19120 -0.492218069 22.35786742 956.04697 5.98478 HELZ 0.999999999965185 3.48149380378462e-11 7.19347355540406e-27 helicase with zinc finger FUNCTION: May act as a helicase that plays a role in RNA metabolism in multiple tissues and organs within the developing embryo.; . TISSUE SPECIFICITY: Expressed predominantly in thymus and brain. Expression is down-regulated in 28 of 95 tested cancer cell lines. {ECO:0000269|PubMed:12691822}.; lymphoreticular;ovary;colon;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;bone;thyroid;iris;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;bile duct;lung;epididymis;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;medulla oblongata;testis - seminiferous tubule;prefrontal cortex;testis;atrioventricular node;trigeminal ganglion; 0.33626 0.09834 -1.210720546 5.708893607 2913.40807 10.24388 HELZ2 1.25628851402837e-09 0.999300380812385 0.000699617931326302 helicase with zinc finger 2, transcriptional coactivator FUNCTION: Helicase that acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. {ECO:0000269|PubMed:16239304, ECO:0000269|PubMed:23525231}.; . TISSUE SPECIFICITY: Expressed in various tissues including heart, pancreas, skeletal muscle, colon, spleen, liver, kidney, lung, peripheral blood and placenta. {ECO:0000269|PubMed:16239304}.; . . . . -0.147490202 42.30360934 4463.72358 13.40473 HEMGN 3.18514258889817e-07 0.322816104272371 0.67718357721337 hemogen FUNCTION: Regulates the proliferation and differentiation of hematopoietic cells. Overexpression block the TPA-induced megakaryocytic differentiation in the K562 cell model. May also prevent cell apoptosis through the activation of the nuclear factor-kappa B (NF-kB). {ECO:0000269|PubMed:14730214, ECO:0000269|PubMed:15332117, ECO:0000269|PubMed:15920494}.; . TISSUE SPECIFICITY: Expressed in hematopoietic precursor cells, thyroid and spermatids (at protein level). Expressed in bone marrow, testis, thymus. Expressed in prostate cancer and ovarian cancer. Also expressed in thymus and thyroid tumors, non-Hodgkin lymphoma, various leukemia cell lines, peripheral blood mononuclear cells (PBMCs) and bone marrow mononuclear cells (BMMCs) of patients with leukemia. {ECO:0000269|PubMed:11404085, ECO:0000269|PubMed:14648837, ECO:0000269|PubMed:14730214, ECO:0000269|PubMed:15332117, ECO:0000269|PubMed:15920494, ECO:0000269|PubMed:23436708}.; unclassifiable (Anatomical System);medulla oblongata;lung;heart;placenta;liver;testis;spleen;blood;bone marrow; fetal liver;fetal lung;skeletal muscle;bone marrow; 0.12418 0.08957 -0.758599262 13.32861524 44.81354 1.28282 HEMK1 8.23152653057192e-05 0.925882694377163 0.0740349903575312 HemK methyltransferase family member 1 FUNCTION: N5-glutamine methyltransferase responsible for the methylation of the GGQ triplet of the mitochondrial translation release factor MTRF1L. {ECO:0000269|PubMed:18541145}.; . . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;blood;lens;skeletal muscle;lung;epididymis;placenta;macula lutea;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland; dorsal root ganglion;testis - interstitial;superior cervical ganglion;heart;testis - seminiferous tubule;testis;appendix;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.04440 0.17390 0.040529541 57.15380986 241.6513 3.35541 HENMT1 1.41529040753691e-06 0.387296154639841 0.612702430069751 HEN1 methyltransferase homolog 1 (Arabidopsis) FUNCTION: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. This probably protects the 3'-end of piRNAs from uridylation activity and subsequent degradation. Stabilization of piRNAs is essential for gametogenesis (By similarity). {ECO:0000250}.; . . . . 0.10276 0.09717 0.795569043 87.49115357 149.5592 2.66675 HEPACAM 0.630644860946896 0.367865238228753 0.00148990082435081 hepatic and glial cell adhesion molecule FUNCTION: Involved in regulating cell motility and cell-matrix interactions. May inhibit cell growth through suppression of cell proliferation. {ECO:0000269|PubMed:15885354, ECO:0000269|PubMed:15917256}.; DISEASE: Leukoencephalopathy, megalencephalic, with subcortical cysts, 2A (MLC2A) [MIM:613925]: A neurodegenerative disorder characterized by infantile-onset macrocephaly and later onset of motor deterioration, with ataxia and spasticity, seizures, and cognitive decline of variable severity. The brain appears swollen on magnetic resonance imaging with white-matter abnormalities and subcortical cysts, in all stages of the disease. {ECO:0000269|PubMed:21419380}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leukoencephalopathy, megalencephalic, with subcortical cysts, 2B (MLC2B) [MIM:613926]: A neurodegenerative disorder characterized by infantile-onset of macrocephaly and mildly delayed motor development associated with white-matter abnormalities on brain magnetic resonance imaging. The phenotype is milder that MLC2A, with better preserved cerebellar white matter and no subcortical cysts outside the temporal region. On follow-up, patients show normal or almost normal motor function. Some patients have normal intelligence, whereas others have a significant cognitive deficiency. {ECO:0000269|PubMed:21419380}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);frontal lobe;hypothalamus;spinal cord;liver;choroid;brain;mammary gland;skeletal muscle; globus pallidus; 0.46854 0.11472 -0.159704656 41.90846898 425.56161 4.31106 HEPACAM2 8.70715988746485e-09 0.157127629002976 0.842872362289865 HEPACAM family member 2 FUNCTION: Required during prometaphase for centrosome maturation. Following poly-ADP-ribosylation (PARsylation) by TNKS, translocates from the Golgi apparatus to mitotic centrosomes and plays a key role in the formation of robust microtubules for prompt movement of chromosomes: anchors AKAP9/CG-NAP, a scaffold protein of the gamma-tubulin ring complex and promotes centrosome maturation. {ECO:0000269|PubMed:22864114}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19358830}.; unclassifiable (Anatomical System);islets of Langerhans;pituitary gland;liver;testis;colon;spleen;blood;kidney;skeletal muscle;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; . 0.09316 0.639420866 83.8995046 181.19055 2.92629 HEPH 0.0095892677408694 0.990316598193242 9.41340658886565e-05 hephaestin FUNCTION: May function as a ferroxidase for ferrous (II) to ferric ion (III) conversion and may be involved in copper transport and homeostasis. Implicated in iron homeostasis and may mediate iron efflux associated to ferroportin 1.; . TISSUE SPECIFICITY: Detected in breast, colon, bone trabecular cells and fibroblasts.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;synovium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;temporal lobe;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22053 0.37532 0.382138899 75.65463553 173.08353 2.86444 HEPHL1 7.16328140545691e-28 8.98442850537333e-05 0.999910155714946 hephaestin like 1 FUNCTION: May function as a ferroxidase and may be involved in copper transport and homeostasis. {ECO:0000250}.; . . lung;gum;colon;skeletal muscle; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.28294 . -0.275617382 33.58693088 455.63895 4.43505 HEPN1 0.0262294918736351 0.565514343249057 0.408256164877308 hepatocellular carcinoma, down-regulated 1 . . TISSUE SPECIFICITY: Expressed in liver. Expression is either down- regulated or lost in hepatocellular carcinomas (HCC). {ECO:0000269|PubMed:12971969}.; . . . . 0.679884223 84.81363529 13.11329 0.47691 HERC1 0.999999999998371 1.62950732273949e-12 5.49313862627333e-44 HECT and RLD domain containing E3 ubiquitin protein ligase family member 1 FUNCTION: Involved in membrane trafficking via some guanine nucleotide exchange factor (GEF) activity and its ability to bind clathrin. Acts as a GEF for Arf and Rab, by exchanging bound GDP for free GTP. Binds phosphatidylinositol 4,5-bisphosphate, which is required for GEF activity. May also act as a E3 ubiquitin- protein ligase which accepts ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000269|PubMed:15642342, ECO:0000269|PubMed:8861955, ECO:0000269|PubMed:9233772}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8861955}.; . . 0.23691 0.11976 -3.879373239 0.212314225 3717.15902 11.89921 HERC2 1 3.99148696809968e-17 4.69739089143488e-51 HECT and RLD domain containing E3 ubiquitin protein ligase 2 FUNCTION: E3 ubiquitin-protein ligase that regulates ubiquitin- dependent retention of repair proteins on damaged chromosomes. Recruited to sites of DNA damage in response to ionizing radiation (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA damage-induced formation of 'Lys-63'-linked ubiquitin chains. Acts as a mediator of binding specificity between UBE2N and RNF8. Involved in the maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of XPA which influences the circadian oscillation of DNA excision repair activity. {ECO:0000269|PubMed:20023648, ECO:0000269|PubMed:20304803, ECO:0000269|PubMed:22508508}.; DISEASE: Mental retardation, autosomal recessive 38 (MRT38) [MIM:615516]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT38 is characterized by global developmental delay affecting motor, speech, adaptive, and social development. Patients manifest autistic features, aggression, self-injury, impulsivity, and distractibility. {ECO:0000269|PubMed:23065719}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;nervous;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;epididymis;nasopharynx;placenta;macula lutea;hippocampus;duodenum;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; whole brain;amygdala;medulla oblongata;thalamus;superior cervical ganglion;prefrontal cortex;caudate nucleus;pons;trigeminal ganglion;cingulate cortex; 0.24532 0.21556 -5.985628431 0.047180939 2166.06955 8.56756 HERC2P1 . . . hect domain and RLD 2 pseudogene 1 . . . . . . . . . . . HERC2P2 . . . hect domain and RLD 2 pseudogene 2 . . . . . . . . . . . HERC2P3 . . . hect domain and RLD 2 pseudogene 3 . . . . . . . . . . . HERC2P4 . . . hect domain and RLD 2 pseudogene 4 . . . . . . . . . . . HERC2P5 . . . hect domain and RLD 2 pseudogene 5 . . . . . . . . . . . HERC2P6 . . . hect domain and RLD 2 pseudogene 6 . . . . . . . . . . . HERC2P7 . . . hect domain and RLD 2 pseudogene 7 . . . . . . . . . . . HERC2P8 . . . hect domain and RLD 2 pseudogene 8 . . . . . . . . . . . HERC2P9 . . . hect domain and RLD 2 pseudogene 9 . . . . . . . . . . . HERC2P10 . . . hect domain and RLD 2 pseudogene 10 . . . . . . . . . . . HERC2P11 . . . hect domain and RLD 2 pseudogene 11 . . . . . . . . . . . HERC3 0.719742122657536 0.280257833735768 4.36066958670361e-08 HECT and RLD domain containing E3 ubiquitin protein ligase 3 FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000250}.; . . smooth muscle;ovary;parathyroid;skin;retina;bone marrow;uterus;endometrium;larynx;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;breast;lung;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;trigeminal ganglion; 0.23812 0.12055 -0.376526807 28.10804435 2027.02267 8.28328 HERC4 0.99270709607873 0.0072929034633176 4.57952104649761e-10 HECT and RLD domain containing E3 ubiquitin protein ligase 4 FUNCTION: Probable E3 ubiquitin-protein ligase involved in either protein trafficking or in the distribution of cellular structures. Required for spermatozoon maturation and fertility, and for the removal of the cytoplasmic droplet of the spermatozoon. E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfer it to targeted substrates (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain and testis and detected in heart and placenta. {ECO:0000269|PubMed:15676274}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;atrium;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;stomach; dorsal root ganglion;subthalamic nucleus;testis - interstitial;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.32963 0.10350 -1.087493118 7.106628922 51.14307 1.40906 HERC5 5.20637325902102e-05 0.99965916319981 0.00028877306759994 HECT and RLD domain containing E3 ubiquitin protein ligase 5 FUNCTION: Major E3 ligase for ISG15 conjugation. Acts as a positive regulator of innate antiviral response in cells induced by interferon. Functions as part of the ISGylation machinery that recognizes target proteins in a broad and relatively non-specific manner. Catalyzes ISGylation of IRF3 which results in sustained activation, it attenuates IRF3-PIN1 interaction, which antagonizes IRF3 ubiquitination and degradation, and boosts the antiviral response. Catalyzes ISGylation of influenza A viral NS1 which attenuates virulence; ISGylated NS1 fails to form homodimers and thus to interact with its RNA targets. Catalyzes ISGylation of papillomavirus type 16 L1 protein which results in dominant- negative effect on virus infectivity. Physically associated with polyribosomes, broadly modifies newly synthesized proteins in a cotranslational manner. In an interferon-stimulated cell, newly translated viral proteins are primary targets of ISG15. {ECO:0000269|PubMed:16407192, ECO:0000269|PubMed:16815975, ECO:0000269|PubMed:16884686, ECO:0000269|PubMed:20133869, ECO:0000269|PubMed:20308324, ECO:0000269|PubMed:20385878, ECO:0000269|PubMed:20542004}.; . TISSUE SPECIFICITY: Expressed in testis and to a lesser degree in brain, ovary and placenta. Found in most tissues at low levels. {ECO:0000269|PubMed:10581175, ECO:0000269|PubMed:15331633}.; unclassifiable (Anatomical System);medulla oblongata;cartilage;ovary;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;retina;bile duct;uterus;optic nerve;lung;larynx;nasopharynx;placenta;macula lutea;liver;testis;head and neck;cervix;brain;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.26416 0.07870 -0.817464788 11.97806086 426.35259 4.31346 HERC6 3.19039189946829e-09 0.912303230027373 0.0876967667822353 HECT and RLD domain containing E3 ubiquitin protein ligase family member 6 FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in brain, heart, placenta and testis. {ECO:0000269|PubMed:15676274}.; unclassifiable (Anatomical System);islets of Langerhans;pineal body;colon;uterus;breast;prostate;optic nerve;whole body;lung;liver;testis;spleen;cervix; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.09058 0.08047 1.938319883 97.51120547 1555.21394 7.30701 HERPUD1 0.82104286595303 0.178781207819706 0.000175926227264076 homocysteine-inducible, endoplasmic reticulum stress-inducible, ubiquitin-like domain member 1 FUNCTION: Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Could enhance presenilin-mediated beta-amyloid protein 40 generation. Binds to ubiquilins and this interaction is required for efficient degradation of CD3D via the ERAD pathway (PubMed:18307982). {ECO:0000269|PubMed:16289116, ECO:0000269|PubMed:18307982}.; . TISSUE SPECIFICITY: Widely expressed; in the brain, expression seems to be restricted to neurons and vascular smooth muscle cells. Present in activated microglia in senile plaques in the brain of patients with Alzheimer disease.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;ciliary body;gall bladder;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;pituitary gland;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;pia mater;lung;mesenchyma;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;aorta;stomach; prostate;olfactory bulb;trachea;thyroid;liver; 0.06471 0.28463 -0.137658575 43.57159707 1037.76371 6.18765 HERPUD2 0.906200797865081 0.0937674988448221 3.17032900970029e-05 HERPUD family member 2 FUNCTION: Could be involved in the unfolded protein response (UPR) pathway. {ECO:0000250}.; . . medulla oblongata;colon;skin;uterus;prostate;whole body;cochlea;cerebral cortex;oesophagus;endometrium;larynx;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;skeletal muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;cingulate cortex; 0.30423 . 0.17280645 65.75843359 3038.96213 10.47543 HES1 0.644078951582769 0.349610322346674 0.00631072607055641 hes family bHLH transcription factor 1 FUNCTION: Transcriptional repressor of genes that require a bHLH protein for their transcription. May act as a negative regulator of myogenesis by inhibiting the functions of MYOD1 and ASH1. Binds DNA on N-box motifs: 5'-CACNAG-3' with high affinity and on E-box motifs: 5'-CANNTG-3' with low affinity (By similarity). May play a role in a functional FA core complex response to DNA cross-link damage, being required for the stability and nuclear localization of FA core complex proteins, as well as for FANCD2 monoubiquitination in response to DNA damage. {ECO:0000250, ECO:0000269|PubMed:18550849}.; . . medulla oblongata;ovary;sympathetic chain;skin;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;testis - interstitial;thyroid;adrenal cortex;appendix;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.93844 . -0.163345027 41.24793583 13.19158 0.48038 HES2 0.0670466550651167 0.733221260580489 0.199732084354395 hes family bHLH transcription factor 2 FUNCTION: Transcriptional repressor of genes that require a bHLH protein for their transcription. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in placenta, pancreatic cancer, colon cancer with RER, cervical cancer, and in head and neck tumors. {ECO:0000269|PubMed:15254753}.; . . 0.51030 0.10923 . . 242.73824 3.36407 HES3 0.268868568223653 0.636078121859468 0.0950533099168787 hes family bHLH transcription factor 3 FUNCTION: Transcriptional repressor of genes that require a bHLH protein for their transcription. {ECO:0000250}.; . . . . 0.40239 . . . 325.01069 3.83269 HES4 0.00014794288110518 0.245981533859779 0.753870523259116 hes family bHLH transcription factor 4 FUNCTION: Transcriptional repressor. Binds DNA on N-box motifs: 5'-CACNAG-3' (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);endometrium; superior cervical ganglion;atrioventricular node; 0.20655 0.11867 . . 1800.58057 7.82660 HES5 0.532717161921776 0.407715442244432 0.0595673958337923 hes family bHLH transcription factor 5 FUNCTION: Transcriptional repressor of genes that require a bHLH protein for their transcription. Plays an important role as neurogenesis negative regulator (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in fetal heart and brain tumors. {ECO:0000269|PubMed:15254753}.; . . 0.13204 0.42345 . . 76.66448 1.83809 HES6 0.00886156439200741 0.577754617292807 0.413383818315185 hes family bHLH transcription factor 6 FUNCTION: Does not bind DNA itself but suppresses both HES1- mediated N box-dependent transcriptional repression and binding of HES1 to E box sequences. Also suppresses HES1-mediated inhibition of the heterodimer formed by ASCL1/MASH1 and TCF3/E47, allowing ASCL1 and TCF3 to up-regulate transcription in its presence. Promotes cell differentiation (By similarity). {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;lung;cornea;placenta;macula lutea;visual apparatus;liver;alveolus;kidney;mammary gland;stomach; medulla oblongata;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node; 0.16965 . . . 141.65667 2.59674 HES7 0.7828835695289 0.210284914901363 0.00683151556973717 hes family bHLH transcription factor 7 FUNCTION: Transcriptional repressor. Represses transcription from both N box- and E box-containing promoters. May with HES1, cooperatively regulate somite formation in the presomitic mesoderm (PSM). May function as a segmentation clock, which is essential for coordinated somite segmentation (By similarity). {ECO:0000250}.; DISEASE: Spondylocostal dysostosis 4, autosomal recessive (SCDO4) [MIM:613686]: A rare condition of variable severity characterized by vertebral and costal anomalies. The main feature include dwarfism, vertebral fusion, hemivertebrae, posterior rib fusion, reduced rib number, and other rib malformations. {ECO:0000269|PubMed:18775957, ECO:0000269|PubMed:20087400}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . bone; . 0.27407 0.11360 . . 14.20939 0.51375 HESX1 0.00816309859692874 0.790106390916927 0.201730510486144 HESX homeobox 1 FUNCTION: Required for the normal development of the forebrain, eyes and other anterior structures such as the olfactory placodes and pituitary gland. Possible transcriptional repressor. Binds to the palindromic PIII sequence, 5'-AGCTTGAGTCTAATTGAATTAACTGTAC-3'. HESX1 and PROP1 bind as heterodimers on this palindromic site, and, in vitro, HESX1 can antagonize PROP1 activation (By similarity). {ECO:0000250}.; DISEASE: Septooptic dysplasia (SOD) [MIM:182230]: A clinically heterogeneous disorder defined by any combination of optic nerve hypoplasia, pituitary gland hypoplasia with panhypopopituitarism, and midline abnormalities of the brain, including absence of the corpus callosum and septum pellucidum. {ECO:0000269|PubMed:11136712, ECO:0000269|PubMed:9620767}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Growth hormone deficiency with pituitary anomalies (GHDPA) [MIM:182230]: A disease characterized by low or absent growth hormone levels, in the presence of a hypoplastic anterior pituitary lobe and ectopic or absent posterior pituitary lobe. {ECO:0000269|PubMed:11136712, ECO:0000269|PubMed:17148560}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pituitary hormone deficiency, combined, 5 (CPHD5) [MIM:182230]: Combined pituitary hormone deficiency is defined as the impaired production of growth hormone and one or more of the other five anterior pituitary hormones. CPHD5 is characterized by complete or partial deficiencies of growth hormone, thyroid- stimulating hormone, luteinizing hormone, follicle stimulating hormone and adrenocorticotropic hormone. {ECO:0000269|PubMed:11136712, ECO:0000269|PubMed:14561704}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;ovary; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;appendix;pons;trigeminal ganglion;skeletal muscle; 0.59812 0.19387 0.193034296 66.82000472 421.69703 4.28895 HEXA 5.04679454539172e-07 0.958913301368433 0.0410861939521127 hexosaminidase subunit alpha FUNCTION: Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues. The form B is active against certain oligosaccharides. The form S has no measurable activity.; DISEASE: GM2-gangliosidosis 1 (GM2G1) [MIM:272800]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. It is characterized by GM2 gangliosides accumulation in the absence of HEXA activity, leading to neurodegeneration and, in the infantile form, death in early childhood. It exists in several forms: infantile (most common and most severe), juvenile and adult (late-onset). {ECO:0000269|PubMed:1301189, ECO:0000269|PubMed:1301190, ECO:0000269|PubMed:1302612, ECO:0000269|PubMed:14566483, ECO:0000269|PubMed:1532289, ECO:0000269|PubMed:1837283, ECO:0000269|PubMed:2144098, ECO:0000269|PubMed:2522679, ECO:0000269|PubMed:2970528, ECO:0000269|PubMed:7717398, ECO:0000269|PubMed:7837766, ECO:0000269|PubMed:7898712, ECO:0000269|PubMed:7951261, ECO:0000269|PubMed:8445615, ECO:0000269|PubMed:8490625, ECO:0000269|PubMed:8581357, ECO:0000269|PubMed:8757036, ECO:0000269|PubMed:9150157, ECO:0000269|PubMed:9338583, ECO:0000269|PubMed:9375850, ECO:0000269|PubMed:9401008, ECO:0000269|PubMed:9603435}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;synovium;bone;thyroid;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;adrenal cortex;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum; superior cervical ganglion;thyroid;placenta;kidney; 0.11138 0.59493 -0.334253673 30.70299599 142.96503 2.60684 HEXA-AS1 . . . HEXA antisense RNA 1 . . . . . . . . . . . HEXB 1.49158509655983e-05 0.991564205559349 0.00842087858968593 hexosaminidase subunit beta FUNCTION: Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues.; DISEASE: GM2-gangliosidosis 2 (GM2G2) [MIM:268800]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. Clinically indistinguishable from GM2-gangliosidosis type 1, presenting startle reactions, early blindness, progressive motor and mental deterioration, macrocephaly and cherry-red spots on the macula. {ECO:0000269|PubMed:1531140, ECO:0000269|PubMed:1720305, ECO:0000269|PubMed:7557963, ECO:0000269|PubMed:7626071, ECO:0000269|PubMed:7633435, ECO:0000269|PubMed:8357844, ECO:0000269|PubMed:8950198, ECO:0000269|PubMed:9401004, ECO:0000269|PubMed:9694901, ECO:0000269|PubMed:9856491}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;endometrium;larynx;bone;thyroid;amniotic fluid;spinal ganglion;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;breast;pancreas;lung;mesenchyma;trabecular meshwork;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;placenta; 0.20473 0.08046 0.951720429 90.06251474 1282.40292 6.74324 HEXDC 1.58767542915452e-06 0.854020781070575 0.145977631253996 hexosaminidase (glycosyl hydrolase family 20, catalytic domain) containing FUNCTION: Has hexosaminidase activity. {ECO:0000269|PubMed:19040401}.; . . medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;lung;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; . 0.14030 . 0.560331224 81.70559094 113.59821 2.32178 HEXDC-IT1 . . . HEXDC intronic transcript 1 . . . . . . . . . . . HEXIM1 0.944400234927573 0.0553972617920334 0.000202503280394089 hexamethylene bis-acetamide inducible 1 FUNCTION: Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor. In cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. May also regulate NF-kappa-B, ESR1, NR3C1 and CIITA-dependent transcriptional activity. {ECO:0000269|PubMed:12581153, ECO:0000269|PubMed:12832472, ECO:0000269|PubMed:12941847, ECO:0000269|PubMed:14580347, ECO:0000269|PubMed:15201869, ECO:0000269|PubMed:15713661, ECO:0000269|PubMed:15940264, ECO:0000269|PubMed:15941832, ECO:0000269|PubMed:17088550}.; . TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in placenta. HEXIM1 and HEXIM2 are differentially expressed. Expressed in endocrine tissues. {ECO:0000269|PubMed:12941847, ECO:0000269|PubMed:15713661}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;thyroid;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; placenta;parietal lobe; 0.09217 0.14068 -0.117432389 44.89266336 31.97836 1.00517 HEXIM2 0.368236513275247 0.62024798456257 0.0115155021621831 hexamethylene bis-acetamide inducible 2 FUNCTION: Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor. In cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. {ECO:0000269|PubMed:15713661, ECO:0000269|PubMed:15713662}.; . TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in testis. HEXIM1 and HEXIM2 are differentially expressed. {ECO:0000269|PubMed:15713661}.; unclassifiable (Anatomical System);lymphoreticular;ovary;islets of Langerhans;colon;parathyroid;fovea centralis;choroid;lens;lung;bone;placenta;macula lutea;visual apparatus;hippocampus;testis;germinal center;kidney;brain;pineal gland;stomach; testis - interstitial;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.13139 0.11068 -0.005381972 53.50908233 99.6053 2.16106 HEY1 0.916104730437935 0.0837780314365038 0.00011723812556166 hes related family bHLH transcription factor with YRPW motif 1 FUNCTION: Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGTG-3' (PubMed:11095750). Downstream effector of Notch signaling required for cardiovascular development. Specifically required for the Notch-induced endocardial epithelial to mesenchymal transition, which is itself criticial for cardiac valve and septum development. May be required in conjunction with HEY2 to specify arterial cell fate or identity. Promotes maintenance of neuronal precursor cells and glial versus neuronal fate specification. Represses transcription by the cardiac transcriptional activators GATA4 and GATA6 and by the neuronal bHLH factors ASCL1/MASH1 and NEUROD4/MATH3 (PubMed:15485867). Involved in the regulation of liver cancer cells self-renewal (PubMed:25985737). {ECO:0000250|UniProtKB:Q9WV93, ECO:0000269|PubMed:11095750, ECO:0000269|PubMed:15485867, ECO:0000269|PubMed:25985737}.; . TISSUE SPECIFICITY: Expressed in the somitic mesoderm, the central nervous system, the kidney, the heart, nasal epithelium, and limbs.; ovary;salivary gland;sympathetic chain;intestine;colon;skin;cochlea;oesophagus;endometrium;larynx;bone;testis;brain;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland; whole brain;dorsal root ganglion;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;olfactory bulb;hypothalamus;spinal cord;pons;caudate nucleus;atrioventricular node;fetal brain;placenta;prefrontal cortex;fetal lung;trigeminal ganglion;cingulate cortex;cerebellum; 0.48579 0.23362 -0.071520315 48.34866714 21.23101 0.71766 HEY2 0.444357733397612 0.54910741369535 0.00653485290703815 hes related family bHLH transcription factor with YRPW motif 2 FUNCTION: Downstream effector of Notch signaling which may be required for cardiovascular development. Transcriptional repressor which binds preferentially to the canonical E box sequence 5'- CACGTG-3'. Represses transcription by the cardiac transcriptional activators GATA4 and GATA6. {ECO:0000269|PubMed:10692439, ECO:0000269|PubMed:11095750, ECO:0000269|PubMed:15485867, ECO:0000269|PubMed:16293227}.; . . . . 0.37195 0.17951 -0.404032746 26.53338051 218.50627 3.19585 HEYL 6.80881163426979e-07 0.270320938476197 0.72967838064264 hes related family bHLH transcription factor with YRPW motif-like FUNCTION: Downstream effector of Notch signaling which may be required for cardiovascular development (By similarity). Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGTG-3' (By similarity). Represses transcription by the cardiac transcriptional activators GATA4 and GATA6. {ECO:0000250, ECO:0000269|PubMed:15485867}.; . . . . 0.14354 0.11836 -0.137658575 43.57159707 64.20269 1.64349 HFE 8.4969700310781e-07 0.505802901039445 0.494196249263552 hemochromatosis FUNCTION: Binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin. {ECO:0000269|PubMed:9465039}.; DISEASE: Hemochromatosis 1 (HFE1) [MIM:235200]: A disorder of iron metabolism characterized by iron overload. Excess iron is deposited in a variety of organs leading to their failure, and resulting in serious illnesses including cirrhosis, hepatomas, diabetes, cardiomyopathy, arthritis, and hypogonadotropic hypogonadism. Severe effects of the disease usually do not appear until after decades of progressive iron loading. {ECO:0000269|PubMed:10094552, ECO:0000269|PubMed:10194428, ECO:0000269|PubMed:10401000, ECO:0000269|PubMed:10575540, ECO:0000269|PubMed:11423500, ECO:0000269|PubMed:11446670, ECO:0000269|PubMed:12542741, ECO:0000269|PubMed:12584229, ECO:0000269|PubMed:12737937, ECO:0000269|PubMed:14633868, ECO:0000269|PubMed:15046077, ECO:0000269|PubMed:18157833, ECO:0000269|PubMed:8696333, ECO:0000269|PubMed:9024376, ECO:0000269|PubMed:9106528, ECO:0000269|PubMed:9620340, ECO:0000269|Ref.25}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Variegate porphyria (VP) [MIM:176200]: A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. Variegate porphyria is the most common form of porphyria in South Africa. It is characterized by skin hyperpigmentation and hypertrichosis, abdominal pain, tachycardia, hypertension and neuromuscular disturbances. High fecal levels of protoporphyrin and coproporphyrin, increased urine uroporphyrins and iron overload are typical markers of the disease. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Iron overload due to HFE variants is a precipitating or exacerbating factor in variegate porphyria.; DISEASE: Microvascular complications of diabetes 7 (MVCD7) [MIM:612635]: Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end- stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues tested except brain.; unclassifiable (Anatomical System);cartilage;ovary;colon;parathyroid;skin;uterus;prostate;lung;frontal lobe;adrenal gland;placenta;visual apparatus;alveolus;liver;spleen;kidney;bladder;stomach; dorsal root ganglion;superior cervical ganglion;thyroid;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.10665 0.73042 0.084621747 60.31493277 796.87118 5.56445 HFE2 0.0123303974512737 0.952108248831909 0.0355613537168177 hemochromatosis type 2 (juvenile) FUNCTION: Acts as a bone morphogenetic protein (BMP) coreceptor. Through enhancement of BMP signaling regulates hepcidin (HAMP) expression and regulates iron homeostasis. {ECO:0000250|UniProtKB:Q7TQ32}.; DISEASE: Hemochromatosis 2A (HFE2A) [MIM:602390]: A juvenile form of hemochromatosis, a disorder of iron metabolism with excess deposition of iron in a variety of organs leading to their failure, bronze skin pigmentation, hepatic cirrhosis, arthropathy and diabetes. The most common symptoms of juvenile hemochromatosis at presentation are hypogonadism and cardiomyopathy. {ECO:0000269|PubMed:14647275, ECO:0000269|PubMed:14982867, ECO:0000269|PubMed:14982873, ECO:0000269|PubMed:15461631}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Adult and fetal liver, heart, and skeletal muscle. {ECO:0000269|PubMed:14647275}.; unclassifiable (Anatomical System);myocardium;heart;ovary;parathyroid;skin;skeletal muscle;uterus;prostate;whole body;larynx;placenta;liver;head and neck;spleen;peripheral nerve; dorsal root ganglion;subthalamic nucleus;fetal liver;superior cervical ganglion;tongue;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.82615 0.23869 -0.336073593 30.55555556 301.48557 3.69898 HFM1 1.44957889668382e-23 0.202359022429858 0.797640977570142 HFM1, ATP-dependent DNA helicase homolog FUNCTION: Required for crossover formation and complete synapsis of homologous chromosomes during meiosis. {ECO:0000250|UniProtKB:D3Z4R1}.; . TISSUE SPECIFICITY: Preferentially expressed in testis and ovary. {ECO:0000269|PubMed:17286053}.; lung;whole body;testis;brain; . 0.07282 . -0.722015017 14.27223402 900.90192 5.84436 HGD 6.42452291651269e-05 0.975643951409981 0.0242918033608536 homogentisate 1,2-dioxygenase . . TISSUE SPECIFICITY: Highest expression in the prostate, small intestine, colon, kidney and liver.; unclassifiable (Anatomical System);ovary;islets of Langerhans;adrenal cortex;colon;parathyroid;fovea centralis;choroid;lens;retina;breast;prostate;optic nerve;lung;endometrium;adrenal gland;thyroid;placenta;macula lutea;iris;liver;spleen;kidney;pineal gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;fetal thyroid;skeletal muscle;prostate;fetal liver;thyroid;liver;fetal lung;ciliary ganglion;kidney;trigeminal ganglion; 0.59080 0.23529 -0.378346116 28.01368247 210.818 3.13190 HGF 0.994701028645709 0.00529897131184924 4.24413310681965e-11 hepatocyte growth factor FUNCTION: Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types. Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization. {ECO:0000269|PubMed:15167892, ECO:0000269|PubMed:20624990}.; DISEASE: Deafness, autosomal recessive, 39 (DFNB39) [MIM:608265]: A form of profound prelingual sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:19576567}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;heart;bone;placenta;visual apparatus;liver;kidney;brain;skeletal muscle;bone marrow; dorsal root ganglion;superior cervical ganglion;uterus corpus;adrenal cortex;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.39794 0.75896 -0.422438699 25.64284029 196.39487 3.03122 HGFAC 5.20820571636199e-07 0.640751849155977 0.359247630023452 HGF activator FUNCTION: Activates hepatocyte growth factor (HGF) by converting it from a single chain to a heterodimeric form.; . TISSUE SPECIFICITY: Liver.; . . 0.13559 0.10506 0.499660491 79.67091295 2517.30927 9.35873 HGH1 . . . HGH1 homolog . . . . . 0.15973 0.10429 . . . . HGS 0.131424768706374 0.868567351716087 7.87957753885906e-06 hepatocyte growth factor-regulated tyrosine kinase substrate FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down- regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes. May contribute to the efficient recruitment of SMADs to the activin receptor complex. Involved in receptor recycling via its association with the CART complex, a multiprotein complex required for efficient transferrin receptor recycling but not for EGFR degradation.; . TISSUE SPECIFICITY: Ubiquitous expression in adult and fetal tissues with higher expression in testis and peripheral blood leukocytes. {ECO:0000269|PubMed:9407053, ECO:0000269|PubMed:9630564}.; medulla oblongata;ovary;salivary gland;colon;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum; amygdala;superior cervical ganglion;testis;trigeminal ganglion; 0.44040 0.38303 -1.501002093 3.597546591 224.72604 3.24245 HGSNAT 1.43961491298178e-06 0.990136695455246 0.00986186492984086 heparan-alpha-glucosaminide N-acetyltransferase FUNCTION: Lysosomal acetyltransferase that acetylates the non- reducing terminal alpha-glucosamine residue of intralysosomal heparin or heparan sulfate, converting it into a substrate for luminal alpha-N-acetyl glucosaminidase. {ECO:0000269|PubMed:16960811, ECO:0000269|PubMed:17033958, ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20650889}.; DISEASE: Mucopolysaccharidosis 3C (MPS3C) [MIM:252930]: A form of mucopolysaccharidosis type 3, an autosomal recessive lysosomal storage disease due to impaired degradation of heparan sulfate. MPS3 is characterized by severe central nervous system degeneration, but only mild somatic disease. Onset of clinical features usually occurs between 2 and 6 years; severe neurologic degeneration occurs in most patients between 6 and 10 years of age, and death occurs typically during the second or third decade of life. {ECO:0000269|PubMed:16960811, ECO:0000269|PubMed:17033958, ECO:0000269|PubMed:17397050, ECO:0000269|PubMed:18024218, ECO:0000269|PubMed:19479962}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, with highest level in leukocytes, heart, liver, skeletal muscle, lung, placenta and liver. {ECO:0000269|PubMed:16960811, ECO:0000269|PubMed:17033958}.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;cerebral cortex;larynx;thyroid;bone;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;cervix;head and neck;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;trachea;adrenal gland;kidney;trigeminal ganglion;skeletal muscle; 0.12890 . 0.156217551 64.82071243 334.82887 3.88886 HHAT 0.000341683761055846 0.988411707995218 0.0112466082437262 hedgehog acyltransferase FUNCTION: Catalyzes N-terminal palmitoylation of SHH; which is required for SHH signaling. May bind GTP. {ECO:0000250, ECO:0000269|PubMed:11486055}.; . TISSUE SPECIFICITY: Ubiquitously expressed in normal tissues and cancer cell lines. {ECO:0000269|PubMed:11160356}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;parathyroid;skeletal muscle;breast;prostate;lung;cochlea;endometrium;placenta;thyroid;hippocampus;testis;brain;mammary gland; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10126 . -0.020150552 52.25288983 2686.0728 9.74725 HHATL 1.48700262097741e-05 0.961231001045094 0.0387541289286958 hedgehog acyltransferase-like FUNCTION: Negatively regulates N-terminal palmitoylation of SHH by HHAT/SKN. {ECO:0000250}.; . TISSUE SPECIFICITY: Heart-specific. {ECO:0000269|PubMed:11374908}.; myocardium;ovary;parathyroid;fovea centralis;choroid;skin;retina;optic nerve;frontal lobe;thyroid;pituitary gland;iris;testis;brain;unclassifiable (Anatomical System);amygdala;heart;tongue;hypothalamus;muscle;spinal cord;skeletal muscle;pancreas;lung;macula lutea;hippocampus;visual apparatus;spleen;head and neck; . 0.15730 0.10609 0.112125503 62.09601321 127.59248 2.46275 HHATL-AS1 . . . HHATL antisense RNA 1 . . . . . . . . . . . HHEX 0.216268139022434 0.745082748530258 0.0386491124473079 hematopoietically expressed homeobox FUNCTION: Recognizes the DNA sequence 5'-ATTAA-3'. Transcriptional repressor. May play a role in hematopoietic differentiation. Establishes anterior identity at two levels; acts early to enhance canonical WNT-signaling by repressing expression of TLE4, and acts later to inhibit NODAL-signaling by directly targeting NODAL (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Liver and promyelocytic leukemia cell line HL- 60. {ECO:0000269|PubMed:1360645, ECO:0000269|PubMed:8096636, ECO:0000269|PubMed:8103988}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;cochlea;larynx;thyroid;iris;pituitary gland;testis;dura mater;germinal center;unclassifiable (Anatomical System);meninges;lymph node;heart;blood;lens;skeletal muscle;pancreas;pia mater;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach;aorta; superior cervical ganglion;thyroid;ciliary ganglion;trigeminal ganglion; 0.56966 0.68625 . . 13.95035 0.50551 HHIP 0.984617793727221 0.0153818618269231 3.44445855553521e-07 hedgehog interacting protein FUNCTION: Modulates hedgehog signaling in several cell types including brain and lung through direct interaction with members of the hedgehog family. {ECO:0000269|PubMed:11472839, ECO:0000269|PubMed:19561609}.; . TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues. Highest expression in adult heart, liver and pancreas, and in fetal kidney. {ECO:0000269|PubMed:11435703, ECO:0000269|Ref.1}.; unclassifiable (Anatomical System);prostate;lymph node;lung;cartilage;hypothalamus;muscle;testis;spleen;brain;vein;skeletal muscle;aorta; superior cervical ganglion;heart;ciliary ganglion;skeletal muscle;cingulate cortex; 0.22874 0.13202 0.023941474 55.75607455 361.49865 4.02415 HHIP-AS1 . . . HHIP antisense RNA 1 . . . . . . . . . . . HHIPL1 0.00214437023105914 0.916941660503521 0.0809139692654199 HHIP like 1 . . . unclassifiable (Anatomical System);heart;ovary;parathyroid;fovea centralis;choroid;lens;retina;prostate;optic nerve;placenta;bone;visual apparatus;macula lutea;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;trigeminal ganglion;skeletal muscle; 0.11131 . . . 68.16919 1.70849 HHIPL2 1.14241085217888e-17 0.00256535295242012 0.99743464704758 HHIP like 2 . . . unclassifiable (Anatomical System);pancreas;lung;thyroid;muscle;testis;mammary gland; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.11441 0.08653 1.403615907 94.76291578 1440.85409 7.08126 HHLA1 . . . HERV-H LTR-associating 1 . . . . . 0.04900 . . . 614.22764 5.00899 HHLA2 8.08523957370927e-05 0.764476182058601 0.235442965545662 HERV-H LTR-associating 2 FUNCTION: Through interaction with TMIGD2, costimulates T-cells in the context of TCR-mediated activation. Enhances T-cell proliferation and cytokine production via an AKT-dependent signaling cascade. {ECO:0000269|PubMed:23784006}.; . TISSUE SPECIFICITY: Expressed at high levels in colon, kidney, testis, lung and pancreas, and at lower levels in small intestine, liver and skeletal muscle. In immune cells, highly expressed in B- cells, dendritic cells and macrophages. Not detected in T-cells. {ECO:0000269|PubMed:10444326, ECO:0000269|PubMed:23784006}.; colon;skeletal muscle; dorsal root ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.04717 0.07085 1.818943827 96.98631753 717.3309 5.31430 HHLA3 0.00618097014298229 0.501830574228187 0.49198845562883 HERV-H LTR-associating 3 . . TISSUE SPECIFICITY: Expressed in kidney and liver. {ECO:0000269|PubMed:10444326}.; uterus;ovary;heart;skin;retina; thalamus;liver; 0.06287 . 0.325313577 73.11276244 154.86249 2.71959 HIBADH 0.25072009941523 0.742997994845106 0.0062819057396645 3-hydroxyisobutyrate dehydrogenase . . TISSUE SPECIFICITY: Detected in skin fibroblasts. {ECO:0000269|PubMed:16466957}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;bile duct;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;adrenal gland;kidney;trigeminal ganglion; 0.36731 0.28982 -0.427900189 25.14744043 24.46519 0.80444 HIBCH 4.18223751191075e-08 0.575949269259159 0.424050688918466 3-hydroxyisobutyryl-CoA hydrolase FUNCTION: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA. {ECO:0000269|PubMed:8824301}.; . TISSUE SPECIFICITY: Highly expressed in liver and kidney, also detected in heart, muscle and brain (at protein level). Not detected in lung. {ECO:0000269|PubMed:8824301}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; amygdala;testis - interstitial;fetal liver;superior cervical ganglion;kidney; 0.09489 0.17960 0.749657564 86.56522765 2485.32619 9.30542 HIC1 . . . hypermethylated in cancer 1 FUNCTION: Transcriptional repressor. Recognizes and binds to the consensus sequence '5-[CG]NG[CG]GGGCA[CA]CC-3'. May act as a tumor suppressor. May be involved in development of head, face, limbs and ventral body wall. Involved in down-regulation of SIRT1 and thereby is involved in regulation of p53/TP53-dependent apoptotic DNA-damage responses. The specific target gene promoter association seems to be depend on corepressors, such as CTBP1 or CTBP2 and MTA1. The regulation of SIRT1 transcription in response to nutrient deprivation seems to involve CTBP1. In cooperation with MTA1 (indicative for an association with the NuRD complex) represses transcription from CCND1/cyclin-D1 and CDKN1C/p57Kip2 specifically in quiescent cells. Involved in regulation of the Wnt signaling pathway probably by association with TCF7L2 and preventing TCF7L2 and CTNNB1 association with promoters of TCF- responsive genes. Seems to repress transcription from E2F1 and ATOH1 which involves ARID1A, indicative for the participation of a distinct SWI/SNF-type chromatin-remodeling complex. Probably represses transcription from ACKR3, FGFBP1 and EFNA1. {ECO:0000269|PubMed:12052894, ECO:0000269|PubMed:15231840, ECO:0000269|PubMed:16269335, ECO:0000269|PubMed:16690027, ECO:0000269|PubMed:16724116, ECO:0000269|PubMed:17213307, ECO:0000269|PubMed:18347096, ECO:0000269|PubMed:19486893, ECO:0000269|PubMed:19525223, ECO:0000269|PubMed:20154726, ECO:0000269|PubMed:20547755}.; . TISSUE SPECIFICITY: Ubiquitously expressed with highest levels found in lung, colon, prostate, thymus, testis and ovary. Expression is absent or decreased in many tumor cells.; lung;whole body;ovary;bone;testis;cervix;blood;kidney;brain;aorta; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.78805 0.19765 . . 274.8491 3.55112 HIC2 0.947187316266396 0.0526346595664317 0.000178024167172311 hypermethylated in cancer 2 FUNCTION: Transcriptional repressor.; . TISSUE SPECIFICITY: Highest levels in cerebellum.; . . 0.66020 0.12515 -0.400392389 26.85185185 184.09017 2.94506 HID1 0.465505319637047 0.534447268099928 4.74122630244831e-05 HID1 domain containing FUNCTION: May play an important role in the development of cancers in a broad range of tissues. {ECO:0000269|PubMed:11281419}.; . TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, colon, spleen, kidney, liver, small intestine and lung. Highest expression is seen in brain and placenta. Loss of expression is seen in some breast, cervical, hepatocellular, lung, thyroid, gastric and renal cell-cancer lines. Highly expressed in secretory cell lines. {ECO:0000269|PubMed:11281419, ECO:0000269|PubMed:21337012}.; . . 0.15824 0.09962 -1.172055164 6.027364945 387.7479 4.14760 HID1-AS1 . . . HID1 antisense RNA 1 . . . . . . . . . . . HIF1A 0.980689532418508 0.0193104428974842 2.4684007697282e-08 hypoxia inducible factor 1 alpha subunit FUNCTION: Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia. {ECO:0000269|PubMed:11292861, ECO:0000269|PubMed:11566883, ECO:0000269|PubMed:15465032, ECO:0000269|PubMed:16543236, ECO:0000269|PubMed:16973622, ECO:0000269|PubMed:17610843, ECO:0000269|PubMed:19528298, ECO:0000269|PubMed:20624928, ECO:0000269|PubMed:22009797, ECO:0000269|PubMed:9887100}.; . TISSUE SPECIFICITY: Expressed in most tissues with highest levels in kidney and heart. Overexpressed in the majority of common human cancers and their metastases, due to the presence of intratumoral hypoxia and as a result of mutations in genes encoding oncoproteins and tumor suppressors. A higher level expression seen in pituitary tumors as compared to the pituitary gland. {ECO:0000269|PubMed:22009797}.; smooth muscle;ovary;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;urinary;blood;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;mammary gland;colon;parathyroid;fovea centralis;vein;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;pia mater;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach; smooth muscle;adrenal cortex;fetal lung; 0.98578 0.91075 -0.198338176 39.17197452 711.15824 5.29923 HIF1A-AS1 . . . HIF1A antisense RNA 1 . . . . . . . . . . . HIF1A-AS2 . . . HIF1A antisense RNA 2 . . . . . . . . . . . HIF1AN 0.867690854822548 0.132231196696118 7.79484813340241e-05 hypoxia inducible factor 1 alpha subunit inhibitor FUNCTION: Hydroxylates HIF-1 alpha at 'Asp-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300- interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation. {ECO:0000269|PubMed:12042299, ECO:0000269|PubMed:12080085, ECO:0000269|PubMed:17003112, ECO:0000269|PubMed:17573339, ECO:0000269|PubMed:18299578, ECO:0000269|PubMed:19245366, ECO:0000269|PubMed:21177872, ECO:0000269|PubMed:21251231}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.53978 0.14896 0.25917371 70.05779665 1388.57335 6.97485 HIF1AP1 . . . hypoxia inducible factor 1 alpha subunit pseudogene 1 . . . . . . . . . . . HIF3A 0.218113050468269 0.781531612396233 0.000355337135498287 hypoxia inducible factor 3 alpha subunit FUNCTION: Acts as a transcriptional regulator in adaptive response to low oxygen tension. Acts as a regulator of hypoxia-inducible gene expression (PubMed:11573933, PubMed:16126907, PubMed:19694616, PubMed:20416395, PubMed:21069422). Functions as an inhibitor of angiogenesis in hypoxic cells of the cornea. Plays a role in the development of the cardiorespiratory system. May also be involved in apoptosis (By similarity). {ECO:0000250|UniProtKB:Q0VBL6, ECO:0000269|PubMed:11573933, ECO:0000269|PubMed:16126907, ECO:0000269|PubMed:19694616, ECO:0000269|PubMed:20416395, ECO:0000269|PubMed:21069422}.; FUNCTION: Isoform 3: Attenuates the ability of transcription factor HIF1A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation. {ECO:0000269|PubMed:19694616, ECO:0000269|PubMed:20416395, ECO:0000269|PubMed:21069422}.; FUNCTION: Isoform 5: Attenuates the ability of transcription factor HIF1A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation. {ECO:0000269|PubMed:21069422}.; . TISSUE SPECIFICITY: Expressed in vascular cells (at protein level) (PubMed:21069422). Expressed in kidney (PubMed:11573933, PubMed:19694616). Expressed in lung epithelial cells (PubMed:16775626). Expressed in endothelial cells (venous and arterial cells from umbilical cord and aortic endothelial cells) and in vascular smooth muscle cells (aorta) (PubMed:21069422). Strongly expressed in the heart, placenta, and skeletal muscle, whereas a weak expression profile was found in the lung, liver, and kidney (PubMed:12538644). Expressed weakly in cell renal cell carcinoma (CC-RCC) compared to normal renal cells (PubMed:16126907). Expression is down-regulated in numerous kidney tumor cells compared to non tumor kidney tissues (PubMed:16126907). Isoform 2 is expressed in heart, placenta, lung, liver, skeletal muscle and pancreas and in numerous cancer cell lines (PubMed:20416395). Isoform 3 and isoform 4 are weakly expressed in heart, placenta, lung, liver, skeletal muscle and pancreas (PubMed:20416395). Isoform 4 is expressed in fetal tissues, such as heart, brain, thymus, lung, liver, skeletal kidney and spleen (PubMed:20416395). Isoform 3 is weakly expressed in fetal tissues, such as liver and kidney (PubMed:20416395). {ECO:0000269|PubMed:11573933, ECO:0000269|PubMed:12538644, ECO:0000269|PubMed:16126907, ECO:0000269|PubMed:16775626, ECO:0000269|PubMed:19694616, ECO:0000269|PubMed:20416395, ECO:0000269|PubMed:21069422}.; ovary;sympathetic chain;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;pituitary gland;brain;unclassifiable (Anatomical System);heart;cartilage;muscle;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;head and neck;spleen;kidney; dorsal root ganglion;amygdala;superior cervical ganglion;placenta;temporal lobe;prefrontal cortex;globus pallidus;fetal lung;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.91764 0.15402 -0.326979057 30.90351498 1871.98223 7.95641 HIGD1A 0.450480881720745 0.521580558151632 0.0279385601276231 HIG1 hypoxia inducible domain family member 1A FUNCTION: Proposed subunit of cytochrome c oxidase (COX, complex IV), which is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. May play a role in the assembly of respiratory supercomplexes. {ECO:0000269|PubMed:22342701}.; . . ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;endometrium;gum;thyroid;bladder;brain;amygdala;heart;spinal cord;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;larynx;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;thalamus;medulla oblongata;occipital lobe;hypothalamus;spinal cord;prefrontal cortex;parietal lobe; 0.23506 0.24555 -0.031067188 51.03798066 13.409 0.48758 HIGD1AP1 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 1 . . . . . . . . . . . HIGD1AP2 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 2 . . . . . . . . . . . HIGD1AP3 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 3 . . . . . . . . . . . HIGD1AP4 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 4 . . . . . . . . . . . HIGD1AP5 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 5 . . . . . . . . . . . HIGD1AP6 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 6 . . . . . . . . . . . HIGD1AP7 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 7 . . . . . . . . . . . HIGD1AP8 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 8 . . . . . . . . . . . HIGD1AP9 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 9 . . . . . . . . . . . HIGD1AP10 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 10 . . . . . . . . . . . HIGD1AP11 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 11 . . . . . . . . . . . HIGD1AP12 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 12 . . . . . . . . . . . HIGD1AP13 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 13 . . . . . . . . . . . HIGD1AP14 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 14 . . . . . . . . . . . HIGD1AP15 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 15 . . . . . . . . . . . HIGD1AP16 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 16 . . . . . . . . . . . HIGD1AP17 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 17 . . . . . . . . . . . HIGD1AP18 . . . HIG1 hypoxia inducible domain family member 1A pseudogene 18 . . . . . . . . . . . HIGD1B 0.00234558353981055 0.533388118782772 0.464266297677417 HIG1 hypoxia inducible domain family member 1B . . . myocardium;ovary;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;testis;amniotic fluid;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;lung;adrenal gland;placenta;macula lutea;liver;spleen;kidney; placenta;temporal lobe; 0.13872 0.07513 0.415317661 76.81056853 1089.4486 6.31884 HIGD1C 2.42000601499889e-05 0.169637870115432 0.830337929824418 HIG1 hypoxia inducible domain family member 1C . . . . . . . 0.391453969 75.87284737 72.51339 1.77515 HIGD2A 0.238671224285494 0.644757016050603 0.116571759663903 HIG1 hypoxia inducible domain family member 2A FUNCTION: Proposed subunit of cytochrome c oxidase (COX, complex IV), which is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. May be involved in cytochrome c oxidase activity. May play a role in the assembly of respiratory supercomplexes. {ECO:0000269|PubMed:22342701}.; . . myocardium;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;stomach;cerebellum; superior cervical ganglion;testis - interstitial;liver;skeletal muscle; 0.03795 0.07677 0.013025609 54.62962963 2.02536 0.06601 HIGD2B 0.0943807874236842 0.573523562664733 0.332095649911583 HIG1 hypoxia inducible domain family member 2B . . . . . 0.14943 . . . 435.02942 4.35019 HILPDA 0.422104597498185 0.46392953416922 0.113965868332595 hypoxia inducible lipid droplet associated FUNCTION: Increases intracellular lipid accumulation. Stimulates expression of cytokines including IL6, MIF and VEGFA. Enhances cell growth and proliferation. {ECO:0000269|PubMed:15930302, ECO:0000269|PubMed:20624928}.; . TISSUE SPECIFICITY: Highly expressed in renal cell carcinoma cells but barely detectable in adjacent normal kidney tissue. Detected in some cervical and endometrial cancers. Expression also detected in fetal kidney with little or no expression observed in normal adult heart, liver, lung, pancreas, prostate or spinal cord (at protein level). {ECO:0000269|PubMed:15930302, ECO:0000269|PubMed:20624928, ECO:0000269|PubMed:21614900}.; medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);tongue;islets of Langerhans;spinal cord;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;duodenum;head and neck;cervix;kidney;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . . 0.457594962 78.16112291 17.14115 0.60237 HILS1 . . . histone linker H1 domain, spermatid-specific 1 (pseudogene) FUNCTION: DNA-binding protein that may be implicated in chromatin remodeling and/or transcriptional regulation during spermiogenesis, the process of spermatid maturation into spermatozoa.; . TISSUE SPECIFICITY: Expressed exclusively in the testis.; lung;testis;brain; superior cervical ganglion;testis; 0.06044 . . . . . HINFP 0.979628977326725 0.0203703349187519 6.87754522655416e-07 histone H4 transcription factor FUNCTION: Transcriptional repressor that binds to the consensus sequence 5'-CGGACGTT-3' and to the RB1 promoter. Transcriptional activator that promotes histone H4 gene transcription at the G1/S phase transition in conjunction with NPAT. Also activates transcription of the ATM and PRKDC genes. Autoregulates its expression by associating with its own promoter. {ECO:0000269|PubMed:11553631, ECO:0000269|PubMed:14585971, ECO:0000269|PubMed:14752047, ECO:0000269|PubMed:15988025, ECO:0000269|PubMed:17163457, ECO:0000269|PubMed:17974976, ECO:0000269|PubMed:18850719}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, heart, skeletal muscle, spleen, kidney, small intestine, placenta and liver. {ECO:0000269|PubMed:11553631}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lacrimal gland;cerebellum cortex;islets of Langerhans;urinary;blood;lens;skeletal muscle;lung;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;stomach; testis; 0.15278 0.16565 0.176444282 66.07100731 1319.98792 6.83226 HINT1 0.0842644971048886 0.759167283549613 0.156568219345498 histidine triad nucleotide binding protein 1 FUNCTION: Hydrolyzes purine nucleotide phosphoramidates with a single phosphate group, including adenosine 5'monophosphoramidate (AMP-NH2), adenosine 5'monophosphomorpholidate (AMP-morpholidate) and guanosine 5'monophosphomorpholidate (GMP-morpholidate). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase, as well as Met-AMP, His- AMP and Asp-AMP, lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) and AMP-N-alanine methyl ester. Can also convert adenosine 5'-O-phosphorothioate and guanosine 5'-O- phosphorothioate to the corresponding nucleoside 5'-O-phosphates with concomitant release of hydrogen sulfide. In addition, functions as scaffolding protein that modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex and by the complex formed with MITF and CTNNB1. Modulates p53/TP53 levels and p53/TP53-mediated apoptosis. Modulates proteasomal degradation of target proteins by the SCF (SKP2-CUL1-F-box protein) E3 ubiquitin- protein ligase complex. {ECO:0000269|PubMed:15703176, ECO:0000269|PubMed:16014379, ECO:0000269|PubMed:16835243, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:22329685, ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:9323207}.; . TISSUE SPECIFICITY: Widely expressed.; ovary;umbilical cord;substantia nigra;skin;retina;corpus callosum;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;oesophagus;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; whole brain;amygdala;occipital lobe;thalamus;subthalamic nucleus;cerebellum peduncles;hypothalamus;temporal lobe;globus pallidus;pons;cingulate cortex;parietal lobe;cerebellum; 0.30498 0.21608 -0.141298762 42.87567823 6.034 0.22840 HINT1P1 . . . histidine triad nucleotide binding protein 1 pseudogene 1 . . . . . . . . . . . HINT1P2 . . . histidine triad nucleotide binding protein 1 pseudogene 2 . . . . . . . . . . . HINT2 0.000235168176378488 0.518218668687011 0.48154616313661 histidine triad nucleotide binding protein 2 FUNCTION: Hydrolase probably involved in steroid biosynthesis. May play a role in apoptosis. Has adenosine phosphoramidase activity. {ECO:0000269|PubMed:16762638, ECO:0000269|PubMed:18653718}.; . TISSUE SPECIFICITY: High expression in liver and pancreas. Expression is significantly down-regulated in hepatocellular carcinoma (HCC) patients. {ECO:0000269|PubMed:16762638}.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;iris;pituitary gland;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);heart;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;liver;kidney;trigeminal ganglion; 0.09753 0.08365 -0.075159878 47.78839349 29.71444 0.94789 HINT2P1 . . . histidine triad nucleotide binding protein 2 pseudogene 1 . . . . . . . . . . . HINT3 0.0967127481995421 0.770219099199622 0.133068152600836 histidine triad nucleotide binding protein 3 FUNCTION: Hydrolyzes phosphoramidate and acyl-adenylate substrates. {ECO:0000269|PubMed:17870088}.; . . colon;skin;retina;uterus;prostate;whole body;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;cartilage;hypothalamus;adrenal cortex;lens;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;hypopharynx;amnion;spleen;head and neck;cervix;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; 0.04425 0.07782 0.21326276 67.71644256 22.25513 0.74604 HIP1 0.999681016475132 0.000318983524822786 4.48675653614689e-14 huntingtin interacting protein 1 FUNCTION: Plays a role in clathrin-mediated endocytosis and trafficking. Involved in regulating AMPA receptor trafficking in the central nervous system in an NMDA-dependent manner. Enhances androgen receptor (AR)-mediated transcription. May act as a proapoptotic protein that induces cell death by acting through the intrinsic apoptosis pathway. Binds 3-phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis. May play a functional role in the cell filament networks. May be required for differentiation, proliferation, and/or survival of somatic and germline progenitors. {ECO:0000269|PubMed:11007801, ECO:0000269|PubMed:11532990, ECO:0000269|PubMed:11577110, ECO:0000269|PubMed:11889126, ECO:0000269|PubMed:12163454, ECO:0000269|PubMed:14732715, ECO:0000269|PubMed:16027218, ECO:0000269|PubMed:9147654}.; DISEASE: Note=A chromosomal aberration involving HIP1 is found in a form of chronic myelomonocytic leukemia (CMML). Translocation t(5;7)(q33;q11.2) with PDGFRB (PubMed:9616134). The chimeric HIP1- PDGFRB transcript results from an in-frame fusion of the two genes (PubMed:9616134). The reciprocal PDGFRB-HIP1 transcript is not expressed (PubMed:9616134). {ECO:0000269|PubMed:9616134}.; TISSUE SPECIFICITY: Ubiquitously expressed with the highest level in brain. Expression is up-regulated in prostate and colon cancer. {ECO:0000269|PubMed:12163454, ECO:0000269|PubMed:9140394, ECO:0000269|PubMed:9147654}.; unclassifiable (Anatomical System);medulla oblongata;smooth muscle;ovary;islets of Langerhans;muscle;skin;skeletal muscle;breast;pancreas;lung;frontal lobe;endometrium;bone;thyroid;placenta;visual apparatus;testis;head and neck;spleen;cervix;brain;stomach; superior cervical ganglion;ciliary ganglion; 0.65870 0.30421 -0.992035476 8.604623732 556.37533 4.79214 HIP1R 1.442966534484e-06 0.999915154543802 8.34024896637301e-05 huntingtin interacting protein 1 related FUNCTION: Component of clathrin-coated pits and vesicles, that may link the endocytic machinery to the actin cytoskeleton. Binds 3- phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis. {ECO:0000269|PubMed:11889126, ECO:0000269|PubMed:14732715}.; . TISSUE SPECIFICITY: Brain, heart, kidney, pancreas, and liver, but not in lung or placenta.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;oesophagus;endometrium;larynx;bone;thyroid;iris;pituitary gland;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; amygdala;whole brain;thalamus;superior cervical ganglion;occipital lobe;hypothalamus;spinal cord;atrioventricular node;caudate nucleus;skeletal muscle;prefrontal cortex;trigeminal ganglion;parietal lobe;cingulate cortex; 0.26127 0.10468 -1.054560763 7.60202878 723.1398 5.33777 HIPK1 0.999942914529477 5.70854701180028e-05 4.04807580569439e-13 homeodomain interacting protein kinase 1 FUNCTION: Serine/threonine-protein kinase involved in transcription regulation and TNF-mediated cellular apoptosis. Plays a role as a corepressor for homeodomain transcription factors. Phosphorylates DAXX and MYB. Phosphorylates DAXX in response to stress, and mediates its translocation from the nucleus to the cytoplasm. Inactivates MYB transcription factor activity by phosphorylation. Prevents MAP3K5-JNK activation in the absence of TNF. TNF triggers its translocation to the cytoplasm in response to stress stimuli, thus activating nuclear MAP3K5-JNK by derepression and promoting apoptosis. May be involved in anti- oxidative stress responses. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. Promotes angiogenesis and to be involved in erythroid differentiation. May be involved in malignant squamous cell tumor formation. {ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:12968034, ECO:0000269|PubMed:15701637, ECO:0000269|PubMed:16390825, ECO:0000269|PubMed:19646965}.; . TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in skeletal muscle and heart. Overexpressed in breast cancer cell lines. Isoform 2 is highly expressed in testis. {ECO:0000269|PubMed:12529400, ECO:0000269|PubMed:12702766}.; lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;nasopharynx;placenta;hippocampus;kidney;stomach;thymus;cerebellum; superior cervical ganglion;testis - interstitial;cerebellum peduncles;thymus;cerebellum; 0.99417 0.13501 -1.638744339 2.801368247 2454.72448 9.21923 HIPK1-AS1 . . . HIPK1 antisense RNA 1 . . . . . . . . . . . HIPK2 0.998346420156677 0.00165357954459643 2.98726239207249e-10 homeodomain interacting protein kinase 2 FUNCTION: Serine/threonine-protein kinase involved in transcription regulation, p53/TP53-mediated cellular apoptosis and regulation of the cell cycle. Acts as a corepressor of several transcription factors, including SMAD1 and POU4F1/Brn3a and probably NK homeodomain transcription factors. Phosphorylates PDX1, ATF1, PML, p53/TP53, CREB1, CTBP1, CBX4, RUNX1, EP300, CTNNB1, HMGA1 and ZBTB4. Inhibits cell growth and promotes apoptosis through the activation of p53/TP53 both at the transcription level and at the protein level (by phosphorylation and indirect acetylation). The phosphorylation of p53/TP53 may be mediated by a p53/TP53-HIPK2-AXIN1 complex. Involved in the response to hypoxia by acting as a transcriptional co-suppressor of HIF1A. Mediates transcriptional activation of TP73. In response to TGFB, cooperates with DAXX to activate JNK. Negative regulator through phosphorylation and subsequent proteasomal degradation of CTNNB1 and the antiapoptotic factor CTBP1. In the Wnt/beta-catenin signaling pathway acts as an intermediate kinase between MAP3K7/TAK1 and NLK to promote the proteasomal degradation of MYB. Phosphorylates CBX4 upon DNA damage and promotes its E3 SUMO- protein ligase activity. Activates CREB1 and ATF1 transcription factors by phosphorylation in response to genotoxic stress. In response to DNA damage, stabilizes PML by phosphorylation. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53- dependent transactivation. Promotes angiogenesis, and is involved in erythroid differentiation, especially during fetal liver erythropoiesis. Phosphorylation of RUNX1 and EP300 stimulates EP300 transcription regulation activity. Triggers ZBTB4 protein degradation in response to DNA damage. Modulates HMGA1 DNA-binding affinity. In response to high glucose, triggers phosphorylation- mediated subnuclear localization shifting of PDX1. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. {ECO:0000269|PubMed:11740489, ECO:0000269|PubMed:11925430, ECO:0000269|PubMed:12851404, ECO:0000269|PubMed:12874272, ECO:0000269|PubMed:14678985, ECO:0000269|PubMed:17018294, ECO:0000269|PubMed:17960875, ECO:0000269|PubMed:18695000, ECO:0000269|PubMed:18809579, ECO:0000269|PubMed:19015637, ECO:0000269|PubMed:19046997, ECO:0000269|PubMed:19448668, ECO:0000269|PubMed:20307497, ECO:0000269|PubMed:20573984, ECO:0000269|PubMed:20637728, ECO:0000269|PubMed:20980392, ECO:0000269|PubMed:21192925, ECO:0000269|PubMed:22825850}.; . TISSUE SPECIFICITY: Highly expressed in heart, muscle and kidney. Weakly expressed in a ubiquitous way. Down-regulated in several thyroid and breast tumors. {ECO:0000269|PubMed:11267674, ECO:0000269|PubMed:11798164}.; colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;amniotic fluid;bladder;brain;unclassifiable (Anatomical System);islets of Langerhans;muscle;blood;lens;placenta;macula lutea;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;occipital lobe;medulla oblongata;superior cervical ganglion;temporal lobe;pons;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.50793 0.23342 . . 89.58874 2.03614 HIPK3 0.893187377239476 0.106812607681409 1.50791155502138e-08 homeodomain interacting protein kinase 3 FUNCTION: Serine/threonine-protein kinase involved in transcription regulation, apoptosis and steroidogenic gene expression. Phosphorylates JUN and RUNX2. Seems to negatively regulate apoptosis by promoting FADD phosphorylation. Enhances androgen receptor-mediated transcription. May act as a transcriptional corepressor for NK homeodomain transcription factors. The phosphorylation of NR5A1 activates SF1 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. In osteoblasts, supports transcription activation: phosphorylates RUNX2 that synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF- responsive element (OCFRE). {ECO:0000269|PubMed:14766760, ECO:0000269|PubMed:17210646}.; . TISSUE SPECIFICITY: Overexpressed in multidrug resistant cells. Highly expressed in heart and skeletal muscle, and at lower levels in placenta, pancreas, brain, spleen, prostate, thymus, testis, small intestine, colon and leukocytes. Not found in liver and lung. {ECO:0000269|PubMed:11034606, ECO:0000269|PubMed:9373137, ECO:0000269|PubMed:9725910}.; unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;spinal cord;colon;parathyroid;blood;skin;skeletal muscle;retina;breast;uterus;lung;frontal lobe;larynx;placenta;hippocampus;hypopharynx;liver;testis;cervix;head and neck;germinal center;kidney;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.99893 0.11172 -0.725642751 14.24274593 336.31364 3.89539 HIPK4 0.00392487635427892 0.95825673786983 0.0378183857758916 homeodomain interacting protein kinase 4 FUNCTION: Protein kinase that phosphorylates human TP53 at Ser-9, and thus induces TP53 repression of BIRC5 promoter (By similarity). May act as a corepressor of transcription factors (Potential). {ECO:0000250, ECO:0000305}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;frontal lobe;adrenal cortex;testis; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.14796 0.10821 -0.08446956 47.15145081 563.27864 4.81899 HIRA 0.999998171154956 1.82884504315275e-06 4.58295104736758e-16 histone cell cycle regulator FUNCTION: Cooperates with ASF1A to promote replication-independent chromatin assembly. Required for the periodic repression of histone gene transcription during the cell cycle. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit. {ECO:0000269|PubMed:12370293, ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:15621527}.; . TISSUE SPECIFICITY: Expressed at high levels in kidney, pancreas and skeletal muscle and at lower levels in brain, heart, liver, lung, and placenta. {ECO:0000269|PubMed:9063745}.; colon;skin;retina;bone marrow;uterus;prostate;whole body;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;duodenum;liver;spleen;head and neck;kidney;stomach; amygdala;whole brain;fetal liver;thyroid; 0.94243 0.23230 -1.374132436 4.429110639 37.48735 1.11600 HIRAP1 . . . histone cell cycle regulator pseudogene 1 . . . . . . . . . . . HIRIP3 0.0190027818505393 0.976880648633126 0.00411656951633434 HIRA interacting protein 3 FUNCTION: May play a role in chromatin function and histone metabolism via its interaction with HIRA and histones. {ECO:0000269|PubMed:9710638}.; . TISSUE SPECIFICITY: Widely expressed. Isoform 1 is predominant in skeletal muscle. Isoform 2 is predominant in liver and heart. {ECO:0000269|PubMed:9710638}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis; 0.24361 0.09072 0.488730112 79.52347252 259.51396 3.46201 HIST1H1A 0.00353079926543669 0.392451757479103 0.604017443255461 histone cluster 1, H1a FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}.; . . colon; dorsal root ganglion;superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.18502 0.21329 -0.088107893 47.06298655 378.07848 4.10054 HIST1H1B 0.509138756022723 0.421807908998682 0.0690533349785954 histone cluster 1, H1b FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in the majority of the cell lines tested and in testis. {ECO:0000269|PubMed:9031620}.; bladder; superior cervical ganglion;trigeminal ganglion;parietal lobe; 0.27585 0.20571 0.575097644 82.1656051 458.1171 4.44431 HIST1H1C . . . histone cluster 1, H1c FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}.; . . myocardium;medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; placenta;fetal thyroid;skeletal muscle; 0.45051 0.29431 -0.216746887 37.69757018 927.43057 5.91227 HIST1H1D . . . histone cluster 1, H1d FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}.; . . oral cavity;blood;head and neck;germinal center; . 0.23935 0.18936 -0.376526807 28.10804435 771.47117 5.49779 HIST1H1E . . . histone cluster 1, H1e FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}.; . . . . 0.49661 0.22787 -1.195919584 5.832743572 110.44404 2.28705 HIST1H1PS1 . . . histone cluster 1, H1, pseudogene 1 . . . . . . . . . . . HIST1H1PS2 . . . histone cluster 1, H1, pseudogene 2 . . . . . . . . . . . HIST1H1T . . . histone cluster 1, H1t FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures.; . . . . 0.03489 0.16249 0.602602982 82.87331918 1368.53569 6.93739 HIST1H2AA 0.00086097937187989 0.340959839551857 0.658179181076263 histone cluster 1, H2aa FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . testis; superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion; 0.91890 0.11169 -0.670411825 15.61689078 9.21128 0.33670 HIST1H2AB 0.00531944331445787 0.471189491174036 0.523491065511506 histone cluster 1, H2ab FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System); testis - interstitial; 0.27024 . -0.670411825 15.61689078 29.43172 0.94099 HIST1H2AC 0.599175549394101 0.362927883164291 0.0378965674416072 histone cluster 1, H2ac FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;whole blood; 0.93332 0.11262 -0.163345027 41.24793583 4.32056 0.15737 HIST1H2AD 3.99677268819075e-05 0.221996466497677 0.777963565775441 histone cluster 1, H2ad FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System);breast;endometrium;kidney;skin;stomach; . 0.36930 . -0.582225231 18.44184949 7.01457 0.26294 HIST1H2AE 0.62412365369502 0.344415114388404 0.0314612319165761 histone cluster 1, H2ae FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System);breast;whole body;placenta;liver;testis;spleen;mammary gland;stomach; prostate; 0.16428 . -0.405853867 26.23260203 0.95683 0.02048 HIST1H2AG 0.000610464103704842 0.287514681618108 0.711874854278187 histone cluster 1, H2ag FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . cartilage;cervix;blood;stomach; temporal lobe;testis;trigeminal ganglion;skeletal muscle; . 0.14896 -0.383807564 27.41802312 10.74064 0.39030 HIST1H2AH 6.2950794420684e-05 0.155717960388121 0.844219088817458 histone cluster 1, H2ah FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.97210 . -0.514264485 21.41424864 37.30912 1.11256 HIST1H2AI 0.581587114173739 0.375452387475716 0.0429604983505453 histone cluster 1, H2ai FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . blood;brain; . 0.12146 . -0.141298762 42.87567823 13.01221 0.47394 HIST1H2AJ 0.19119768143705 0.647097758711335 0.161704559851615 histone cluster 1, H2aj FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System);optic nerve;macula lutea;fovea centralis;choroid;lens;retina; . 0.97697 0.11262 -0.141298762 42.87567823 5.10146 0.18926 HIST1H2AK 0.0684285015781424 0.73588449648503 0.195687001936827 histone cluster 1, H2ak FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . lymph node;ovary;testis; . 0.35065 . 0.060756528 58.52795471 175.04946 2.87692 HIST1H2AL 0.0624869158210738 0.723555170516095 0.213957913662832 histone cluster 1, H2al FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . placenta; superior cervical ganglion;skeletal muscle; 0.02661 . -0.229483771 36.86010852 13.50243 0.49081 HIST1H2AM 0.000856482029037302 0.340093445156317 0.659050072814646 histone cluster 1, H2am FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . bone;placenta;visual apparatus;brain; . 0.36930 . -0.273576253 33.97027601 6.36805 0.23895 HIST1H2APS1 . . . histone cluster 1, H2a, pseudogene 1 . . . . . . . . . . . HIST1H2APS2 . . . histone cluster 1, H2a, pseudogene 2 . . . . . . . . . . . HIST1H2APS3 . . . histone cluster 1, H2a, pseudogene 3 . . . . . . . . . . . HIST1H2APS4 . . . histone cluster 1, H2a, pseudogene 4 . . . liver;kidney; . . . . . . . HIST1H2APS5 . . . histone cluster 1, H2a, pseudogene 5 . . . . . . . . . . . HIST1H2APS6 . . . histone cluster 1, H2a, pseudogene 6 . . . . . . . . . . . HIST1H2BA 0.132823726172591 0.62068683532991 0.2464894384975 histone cluster 1, H2ba FUNCTION: Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization (By similarity). Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear. Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000250, ECO:0000269|PubMed:21249133}.; . TISSUE SPECIFICITY: Mainly expressed in testis, and the corresponding protein is also present in mature sperm (at protein level). Also found in some fat cells. {ECO:0000269|PubMed:12213818, ECO:0000269|PubMed:21249133}.; unclassifiable (Anatomical System);lung;testis; . 0.72959 0.20059 -0.780646273 12.77423921 11.90297 0.43155 HIST1H2BB 0.130327871216174 0.618522669218852 0.251149459564973 histone cluster 1, H2bb FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.97508 . -0.031067188 51.03798066 14.52983 0.52275 HIST1H2BC 0.00287801155749555 0.356422638233369 0.640699350209135 histone cluster 1, H2bc FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;fovea centralis;choroid;lens;retina;bone marrow;uterus;pancreas;prostate;optic nerve;placenta;macula lutea;alveolus;liver;spleen;pineal gland;bladder;mammary gland;peripheral nerve; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;whole blood; 0.56417 . -0.251530012 35.42108988 8.62709 0.31635 HIST1H2BD 0.000277979441009119 0.190591618997324 0.809130401561667 histone cluster 1, H2bd FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System);lymph node;ovary;colon;fovea centralis;choroid;lens;retina;uterus;prostate;optic nerve;whole body;lung;endometrium;adrenal gland;bone;placenta;macula lutea;liver;spleen;germinal center;kidney;brain;mammary gland;thymus; superior cervical ganglion;prostate;appendix;atrioventricular node;trigeminal ganglion;fetal thyroid; . 0.11262 -0.05129383 49.75819769 65.06961 1.66006 HIST1H2BE 0.000307871828087192 0.201310460854869 0.798381667317044 histone cluster 1, H2be FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . pancreas;lung;frontal lobe;thyroid;placenta;colon;spleen;head and neck;kidney;stomach; prostate;thymus; 0.06718 . 0.193034296 66.82000472 2710.32625 9.79782 HIST1H2BF 0.000300020472922898 0.198550161998267 0.80114981752881 histone cluster 1, H2bf FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System);liver;spleen;kidney; . 0.22419 . -0.427900189 25.14744043 7.11981 0.26530 HIST1H2BG 2.94452400546665e-06 0.0517553662490425 0.948241689226952 histone cluster 1, H2bg FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System);endometrium;epididymis;placenta;liver;duodenum;spleen;kidney; . 0.73765 . -0.161524709 41.6430762 18.22838 0.63361 HIST1H2BH 0.000295729876724394 0.197025605832447 0.802678664290829 histone cluster 1, H2bh FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . stomach; prostate;placenta;thymus; 0.92926 . -0.383807564 27.41802312 8.15434 0.30085 HIST1H2BI 0.138012141980387 0.624857185303571 0.237130672716042 histone cluster 1, H2bi FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.31655 . -0.031067188 51.03798066 15.11819 0.54384 HIST1H2BJ 0.47884211441258 0.438341825980345 0.0828160596070753 histone cluster 1, H2bj FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . umbilical cord;ovary;iris;blood;retina;bone marrow; dorsal root ganglion;prostate;bone marrow; 0.97050 0.11809 -0.383807564 27.41802312 26.91604 0.87042 HIST1H2BK 0.490754148427297 0.43206193607246 0.0771839155002425 histone cluster 1, H2bk FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System);heart;colon;skin;uterus;prostate;lung;placenta;thyroid;liver;cervix;germinal center;stomach;gall bladder; prostate;placenta; 0.95090 0.12181 -0.405853867 26.23260203 12.92013 0.47122 HIST1H2BL 0.00286755404850941 0.355802358809361 0.641330087142129 histone cluster 1, H2bl FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.78869 . -0.117432389 44.89266336 803.68126 5.58448 HIST1H2BM 0.00275346435077864 0.348935793831758 0.648310741817464 histone cluster 1, H2bm FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System);stomach; superior cervical ganglion; 0.89104 . -0.117432389 44.89266336 26.19347 0.84903 HIST1H2BN 0.139774615254902 0.626176640441021 0.234048744304077 histone cluster 1, H2bn FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.05916 . -0.09720619 46.20193442 11.81004 0.42812 HIST1H2BO 3.07277582735277e-05 0.104529941378546 0.895439330863181 histone cluster 1, H2bo FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . bone marrow; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.92596 . -0.163345027 41.24793583 11.65158 0.42224 HIST1H2BPS1 . . . histone cluster 1, H2b, pseudogene 1 . . . . . . . . . . . HIST1H2BPS2 . . . histone cluster 1, H2b, pseudogene 2 . . . . . . . . . . . HIST1H2BPS3 . . . histone cluster 1, H2b, pseudogene 3 . . . . . . . . . . . HIST1H3A 3.98008178767139e-05 0.120835595319755 0.879124603862368 histone cluster 1, H3a FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System);uterus;iris; superior cervical ganglion;subthalamic nucleus;uterus corpus;trigeminal ganglion;skeletal muscle; 0.15183 . -1.089312628 7.047652748 21.81436 0.73446 HIST1H3B 0.307282993148648 0.619219138269179 0.0734978685821734 histone cluster 1, H3b FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.36256 . -0.185391282 39.67916962 3.42202 0.12502 HIST1H3C 0.215540519058334 0.647903842463723 0.136555638477943 histone cluster 1, H3c FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.09650 . -0.251530012 35.42108988 6.73287 0.24811 HIST1H3D 0.011195071454157 0.627467716656287 0.361337211889556 histone cluster 1, H3d FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . . . -0.141298762 42.87567823 5.36373 0.19901 HIST1H3E 0.000813428842528686 0.331647651750985 0.667538919406486 histone cluster 1, H3e FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System);breast;lung;testis;brain; . 0.20314 . -0.60427181 17.74593064 15.33925 0.55140 HIST1H3F 0.042215361750485 0.658785096752254 0.298999541497261 histone cluster 1, H3f FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.24831 . -0.031067188 51.03798066 7.96978 0.29229 HIST1H3G 1.71005632806188e-05 0.140228263618707 0.859754635818013 histone cluster 1, H3g FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.29148 . -0.273576253 33.97027601 5.51052 0.20552 HIST1H3H 0.02493915563981 0.555264195756552 0.419796648603638 histone cluster 1, H3h FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.21975 . -0.119252484 44.53880632 5.79924 0.21882 HIST1H3I 0.360879945054601 0.587736995743344 0.0513830592020545 histone cluster 1, H3i FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System);germinal center;brain; . 0.31574 . -0.09720619 46.20193442 6.59255 0.24364 HIST1H3J 0.695883936820569 0.286876166441171 0.0172398967382597 histone cluster 1, H3j FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.29705 . 0.057118534 57.99716914 . . HIST1H3PS1 . . . histone cluster 1, H3, pseudogene 1 . . . . . . . . . . . HIST1H4A 0.00228540295756206 0.318648485418162 0.679066111624276 histone cluster 1, H4a FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.; . unclassifiable (Anatomical System); superior cervical ganglion;atrioventricular node; 0.29478 . -0.075159878 47.78839349 6.98543 0.26035 HIST1H4B 0.00854182671998013 0.569923962525089 0.421534210754931 histone cluster 1, H4b FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.; . . . 0.06894 . -0.648365105 16.35999056 14.51754 0.52175 HIST1H4C 8.85616839210981e-05 0.18745056149179 0.812460876824289 histone cluster 1, H4c FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.; . . . 0.34325 . -0.339715008 30.06605331 5.65515 0.21228 HIST1H4D 0.00226430020608533 0.31719344187476 0.680542257919154 histone cluster 1, H4d FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.; . unclassifiable (Anatomical System); . 0.34778 . -0.361761279 28.6329323 23.84646 0.78658 HIST1H4E 0.000642250549090646 0.294964991128732 0.704392758322177 histone cluster 1, H4e FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.; . unclassifiable (Anatomical System);pancreas;endometrium;placenta;testis;spleen;blood;brain;skin;thymus;bone marrow; atrioventricular node;trigeminal ganglion; 0.10242 . -0.383807564 27.41802312 6.74798 0.24905 HIST1H4F 0.181985150966619 0.6454821218455 0.17253272718788 histone cluster 1, H4f FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.; . . . 0.05585 . 0.014844891 54.94810097 8.1986 0.30252 HIST1H4G 0.00262999657981332 0.341290845157288 0.656079158262898 histone cluster 1, H4g FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity). {ECO:0000250}.; . . . . 0.22457 . 0.147123112 64.11299835 335.75297 3.89267 HIST1H4H 0.00879032933359599 0.576034218017051 0.415175452649353 histone cluster 1, H4h FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.; . unclassifiable (Anatomical System);breast;uterus;prostate;trophoblast;lung;placenta;liver;blood;kidney;stomach; dorsal root ganglion;superior cervical ganglion;appendix;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14757 . -0.405853867 26.23260203 6.83594 0.25399 HIST1H4I 0.446296012965993 0.453936637204161 0.0997673498298457 histone cluster 1, H4i FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.; . unclassifiable (Anatomical System);pancreas;colon;spleen; dorsal root ganglion;trigeminal ganglion;parietal lobe;skeletal muscle; . . -0.09720619 46.20193442 4.4177 0.16036 HIST1H4J 0.423753830207411 0.463294259009398 0.112951910783191 histone cluster 1, H4j FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.; . unclassifiable (Anatomical System);trophoblast;ovary;salivary gland;intestine;pharynx;colon;blood;prostate;visual apparatus;liver;spleen;kidney;brain;bladder; . 0.53052 . -0.053113545 49.38664779 4.36427 0.15875 HIST1H4K 0.429118935200097 0.461180216061355 0.109700848738548 histone cluster 1, H4k FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.; . unclassifiable (Anatomical System);trophoblast;ovary;salivary gland;intestine;pharynx;colon;blood;prostate;visual apparatus;liver;spleen;kidney;brain;bladder; . 0.61668 . . . 14.39166 0.51925 HIST1H4L 0.191234624133278 0.647102674975899 0.161662700890823 histone cluster 1, H4l FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.; . . . 0.23637 . 0.080983847 59.76055674 24.99407 0.81943 HIST1H4PS1 . . . histone cluster 1, H4, pseudogene 1 . . . . . . . . . . . HIST2H2AA3 . . . histone cluster 2, H2aa3 FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.14118 . . . . . HIST2H2AA4 . . . histone cluster 2, H2aa4 FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.11334 . . . . . HIST2H2AB 0.216215034165356 0.647861978081185 0.135922987753459 histone cluster 2, H2ab FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . lung;blood;bone marrow; . 0.94267 0.17050 -0.119252484 44.53880632 2.43929 0.08861 HIST2H2AC 0.209670054818694 0.648130298006004 0.142199647175302 histone cluster 2, H2ac FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . unclassifiable (Anatomical System);smooth muscle;lung;nasopharynx;bone marrow; . 0.94662 0.11262 -0.053113545 49.38664779 1.67782 0.05430 HIST2H2BA . . . histone cluster 2, H2ba (pseudogene) . . . . . . . . . . . HIST2H2BB . . . histone cluster 2, H2bb (pseudogene) . . . . . . . . . . . HIST2H2BC . . . histone cluster 2, H2bc (pseudogene) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . . . . . . . HIST2H2BD . . . histone cluster 2, H2bd (pseudogene) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.05916 . . . . . HIST2H2BE 0.487682589452728 0.433709259197203 0.0786081513500692 histone cluster 2, H2be FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.94829 . 0.147123112 64.11299835 6.01727 0.22723 HIST2H2BF 0.0259999814401532 0.563729938984829 0.410270079575018 histone cluster 2, H2bf FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.10021 0.11050 0.169169615 65.33380514 32.00975 1.00601 HIST2H3A . . . histone cluster 2, H3a FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.12120 0.11809 . . . . HIST2H3C . . . histone cluster 2, H3c FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.36821 . . . . . HIST2H3D 0.498937279946072 0.427580174103902 0.0734825459500255 histone cluster 2, H3d FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . pancreas;spleen; . . . 0.035072054 56.2514744 6.52563 0.24176 HIST2H3DP1 . . . histone cluster 2, H3d pseudogene 1 . . . . . . . . . . . HIST2H3PS2 0.135983520424883 0.623278241451814 0.240738238123303 histone cluster 2, H3, pseudogene 2 . . . . . . . . . 173.12826 2.86487 HIST2H4A . . . histone cluster 2, H4a FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.; . . . 0.11436 . . . . . HIST2H4B . . . histone cluster 2, H4b FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.; . . . 0.24760 . . . . . HIST3H2A 0.484381729433831 0.435457976081068 0.0801602944851015 histone cluster 3, H2a FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.95998 0.11262 -0.185391282 39.67916962 6.30329 0.23730 HIST3H2BA . . . histone cluster 3, H2ba (pseudogene) . . . . . . . . . . . HIST3H2BB 0.0228263871923496 0.53725929059171 0.43991432221594 histone cluster 3, H2bb FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . . . . 0.82656 0.11262 -0.317668748 31.45789101 8.72423 0.32089 HIST3H3 0.000822080676547451 0.333367439103685 0.665810480219767 histone cluster 3, H3 FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; . TISSUE SPECIFICITY: Expressed in testicular cells.; . . 0.60152 0.12166 -0.514264485 21.41424864 156.552 2.73498 HIST4H4 0.260791362702686 0.638844553082587 0.100364084214727 histone cluster 4, H4 FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.; . lymph node;testis; . 0.18251 . -0.075159878 47.78839349 55.03237 1.48591 HIVEP1 0.999986917229393 1.30827706070713e-05 9.26806003781935e-17 human immunodeficiency virus type I enhancer binding protein 1 FUNCTION: This protein specifically binds to the DNA sequence 5'- GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV-1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, and interferon-beta genes. It may act in T-cell activation. Involved in activating HIV-1 gene expression. Isoform 2 and isoform 3 also bind to the IPCS (IRF1 and p53 common sequence) DNA sequence in the promoter region of interferon regulatory factor 1 and p53 genes and are involved in transcription regulation of these genes. Isoform 2 does not activate HIV-1 gene expression. Isoform 2 and isoform 3 may be involved in apoptosis.; . . . . 0.18367 . 1.216289636 93.09389007 3060.83267 10.52275 HIVEP2 0.999999664252267 3.35747733176297e-07 7.37862086254662e-18 human immunodeficiency virus type I enhancer binding protein 2 FUNCTION: This protein specifically binds to the DNA sequence 5'- GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, somatostatin receptor II, and interferon- beta genes. It may act in T-cell activation.; . TISSUE SPECIFICITY: Expressed in brain and skeletal muscle. {ECO:0000269|PubMed:10207097}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;lacrimal gland;hypothalamus;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;liver;alveolus;spleen;head and neck;kidney;mammary gland; amygdala;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;pons;caudate nucleus;atrioventricular node;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.57854 0.15610 -2.196075097 1.374144845 466.73466 4.47593 HIVEP3 0.0308106016636644 0.969189259863282 1.38473053519261e-07 human immunodeficiency virus type I enhancer binding protein 3 FUNCTION: Plays a role of transcription factor; binds to recognition signal sequences (Rss heptamer) for somatic recombination of immunoglobulin and T-cell receptor gene segments; Binds also to the kappa-B motif of gene such as S100A4, involved in cell progression and differentiation. Kappa-B motif is a gene regulatory element found in promoters and enhancers of genes involved in immunity, inflammation, and growth and that responds to viral antigens, mitogens, and cytokines. Involvement of HIVEP3 in cell growth is strengthened by the fact that its down- regulation promotes cell cycle progression with ultimate formation of multinucleated giant cells. Strongly inhibits TNF-alpha-induced NF-kappa-B activation; Interferes with nuclear factor NF-kappa-B by several mechanisms: as transcription factor, by competing for Kappa-B motif and by repressing transcription in the nucleus; through a non transcriptional process, by inhibiting nuclear translocation of RELA by association with TRAF2, an adapter molecule in the tumor necrosis factor signaling, which blocks the formation of IKK complex. Interaction with TRAF proteins inhibits both NF-Kappa-B-mediated and c-Jun N-terminal kinase/JNK-mediated responses that include apoptosis and proinflammatory cytokine gene expression. Positively regulates the expression of IL2 in T-cell. Essential regulator of adult bone formation. {ECO:0000269|PubMed:11161801}.; . . unclassifiable (Anatomical System);uterus;lymphoreticular;lymph node;lung;frontal lobe;colon;cervix;kidney;germinal center;brain;stomach; superior cervical ganglion; 0.28273 0.18943 -0.514887152 21.20783204 2707.92091 9.79359 HJURP 1.26222310392964e-05 0.952080752251829 0.0479066255171322 Holliday junction recognition protein FUNCTION: Centromeric protein that plays a central role in the incorporation and maintenance of histone H3-like variant CENPA at centromeres. Acts as a specific chaperone for CENPA and is required for the incorporation of newly synthesized CENPA molecules into nucleosomes at replicated centromeres. Prevents CENPA-H4 tetramerization and prevents premature DNA binding by the CENPA-H4 tetramer. Directly binds Holliday junctions. {ECO:0000269|PubMed:19410544, ECO:0000269|PubMed:19410545}.; . TISSUE SPECIFICITY: According to PubMed:17256767, highly expressed in the thymus with lower levels in the placenta, small intestine, liver, skeletal muscle, and colon. According to PubMed:17823411, highly expressed in testis, and at a relatively lower level in thymus and bone marrow. Significantly overexpressed in many lung cancer samples, compared with normal lung. {ECO:0000269|PubMed:17256767, ECO:0000269|PubMed:17823411}.; . . 0.53936 0.06636 1.381566496 94.62137297 2382.87075 9.06076 HK1 0.555733310453426 0.444265729939447 9.59607127385369e-07 hexokinase 1 . DISEASE: Hexokinase deficiency (HK deficiency) [MIM:235700]: Rare autosomal recessive disease with nonspherocytic hemolytic anemia as the predominant clinical feature. {ECO:0000269|PubMed:12393545, ECO:0000269|PubMed:7655856}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Neuropathy, hereditary motor and sensory, Russe type (HMSNR) [MIM:605285]: An autosomal recessive progressive complex peripheral neuropathy characterized by onset in the first decade of distal lower limb weakness and muscle atrophy resulting in walking difficulties. Distal impairment of the upper limbs usually occurs later, as does proximal lower limb weakness. There is distal sensory impairment, with pes cavus and areflexia. Laboratory studies suggest that it is a myelinopathy resulting in reduced nerve conduction velocities in the demyelinating range as well as a length-dependent axonopathy. {ECO:0000269|PubMed:19536174}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 2 is erythrocyte specific. Isoform 3 and isoform 4 are testis-specific.; myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;tonsil;heart;cartilage;tongue;pineal body;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;mammary gland;colon;parathyroid;choroid;uterus;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta;thymus;cerebellum; amygdala;whole brain;subthalamic nucleus;occipital lobe;cerebellum peduncles;cingulate cortex;cerebellum; 0.85793 0.80177 -1.217968826 5.638122199 351.47887 3.97341 HK2 0.0209328439585101 0.979037314476686 2.98415648044265e-05 hexokinase 2 . . TISSUE SPECIFICITY: Predominant hexokinase isozyme expressed in insulin-responsive tissues such as skeletal muscle.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;muscle;adrenal cortex;blood;lens;skeletal muscle;bile duct;breast;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;adipose tissue;testis - seminiferous tubule;testis;skeletal muscle; 0.54380 0.45841 -0.946125119 9.377211607 2100.17144 8.44166 HK2P1 . . . hexokinase 2 pseudogene 1 . . . . . . . . . . . HK3 1.15547608704236e-14 0.0761898713555853 0.923810128644403 hexokinase 3 . . . unclassifiable (Anatomical System);ovary;cartilage;tongue;colon;blood;fovea centralis;choroid;lens;skin;skeletal muscle;retina;bone marrow;uterus;prostate;optic nerve;lung;placenta;macula lutea;alveolus;head and neck;brain; whole blood;bone marrow; 0.81290 0.18777 -0.556806243 19.55060156 675.11075 5.18856 HKDC1 1.84795215291941e-12 0.803550177078468 0.196449822919684 hexokinase domain containing 1 . . . unclassifiable (Anatomical System);heart;colon;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;pancreas;optic nerve;lung;thyroid;bone;macula lutea;visual apparatus;liver;spleen;kidney;brain;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;kidney;caudate nucleus;trigeminal ganglion;skeletal muscle;parietal lobe;skin; 0.58579 0.11499 0.281016493 70.87756546 2378.97896 9.05182 HKR1 2.71836692118079e-10 0.146437229210252 0.853562770517911 HKR1, GLI-Kruppel zinc finger family member FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);smooth muscle;cartilage;ovary;hypothalamus;colon;parathyroid;skin;skeletal muscle;retina;breast;uterus;prostate;whole body;lung;endometrium;larynx;epididymis;bone;thyroid;placenta;visual apparatus;iris;testis;head and neck;germinal center;kidney;brain;stomach; superior cervical ganglion;testis - seminiferous tubule;globus pallidus;atrioventricular node; 0.06617 . 0.271907863 70.73012503 2989.12061 10.37502 HLA-A 0.132779664827761 0.862664913079238 0.00455542209300079 major histocompatibility complex, class I, A FUNCTION: Involved in the presentation of foreign antigens to the immune system.; . . unclassifiable (Anatomical System);lymph node;endometrium;islets of Langerhans;bone;testis;colon;cervix; . 0.19139 . 8.928758265 99.95871668 31164.80389 34.46226 HLA-B 0.00266463463685607 0.93518903102164 0.0621463343415036 major histocompatibility complex, class I, B FUNCTION: Involved in the presentation of foreign antigens to the immune system.; . . . . . . 8.952805914 99.9646143 16291.10418 27.23123 HLA-C 9.94564281082044e-10 0.0870851514429539 0.912914847562482 major histocompatibility complex, class I, C FUNCTION: Involved in the presentation of foreign antigens to the immune system.; . . . . . 0.79928 7.653485912 99.91743336 21803.44637 30.60876 HLA-DMA 0.687977633420569 0.307812506757939 0.00420985982149156 major histocompatibility complex, class II, DM alpha FUNCTION: Plays a critical role in catalyzing the release of class II-associated invariant chain peptide (CLIP) from newly synthesized MHC class II molecules and freeing the peptide binding site for acquisition of antigenic peptides. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. {ECO:0000269|PubMed:16547258, ECO:0000269|PubMed:8849454, ECO:0000269|PubMed:9768757}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;blood;skeletal muscle;bile duct;pancreas;lung;epididymis;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.15692 0.09496 0.749657564 86.56522765 931.80661 5.92181 HLA-DMB 0.00490510636506002 0.883692011621669 0.111402882013271 major histocompatibility complex, class II, DM beta FUNCTION: Plays a critical role in catalyzing the release of class II-associated invariant chain peptide (CLIP) from newly synthesized MHC class II molecules and freeing the peptide binding site for acquisition of antigenic peptides. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. {ECO:0000269|PubMed:16547258, ECO:0000269|PubMed:8849454, ECO:0000269|PubMed:9768757}.; . . . . 0.04445 0.06902 1.038098315 91.20665251 277.70231 3.56978 HLA-DOA 1.88487379125175e-05 0.267897036073586 0.732084115188502 major histocompatibility complex, class II, DO alpha FUNCTION: Important modulator in the HLA class II restricted antigen presentation pathway by interaction with the HLA-DM molecule in B-cells. Modifies peptide exchange activity of HLA-DM.; . . unclassifiable (Anatomical System);prostate;smooth muscle;lymph node;lung;ovary;testis;germinal center;brain;tonsil;bone marrow; . 0.18533 0.09317 0.661468037 84.4420854 211.90493 3.13967 HLA-DOB 9.08751665004379e-05 0.552954446504831 0.446954678328669 major histocompatibility complex, class II, DO beta FUNCTION: Important modulator in the HLA class II restricted antigen presentation pathway by interaction with the HLA-DM molecule in B-cells. Modifies peptide exchange activity of HLA-DM.; . . . . 0.11913 0.12310 0.72761005 86.08162302 1166.25764 6.49652 HLA-DPA1 0.000185717032888532 0.469215738907011 0.530598544060101 major histocompatibility complex, class II, DP alpha 1 FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.; . . . . 0.12228 . 3.285765937 99.40434065 7603.77264 18.69721 HLA-DPA2 . . . major histocompatibility complex, class II, DP alpha 2 (pseudogene) . . . . . . . . . . . HLA-DPA3 . . . major histocompatibility complex, class II, DP alpha 3 (pseudogene) . . . . . . . . . . . HLA-DPB1 7.18465788950328e-09 0.075619220558398 0.924380772256944 major histocompatibility complex, class II, DP beta 1 FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.; . . . . 0.05183 0.18779 3.396108778 99.44562397 17883.2969 28.14203 HLA-DPB2 . . . major histocompatibility complex, class II, DP beta 2 (pseudogene) . . . . . . . . . . . HLA-DQA1 0.166625329932453 0.772082464636609 0.0612922054309378 major histocompatibility complex, class II, DQ alpha 1 FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.; . . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;brain;artery;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;lens;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; ciliary ganglion; 0.08030 . 5.110977474 99.82307148 16622.23863 27.59846 HLA-DQA2 0.00504406368032515 0.697612525457181 0.297343410862494 major histocompatibility complex, class II, DQ alpha 2 FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading. {ECO:0000269|PubMed:22407913}.; . TISSUE SPECIFICITY: Restricted to skin Langerhans cells, although some expression at low levels may occur at the surface of B lymphoblastoid cells. {ECO:0000269|PubMed:22407913, ECO:0000269|PubMed:9036956}.; . . 0.16449 . 1.216305531 93.13517339 883.96094 5.79012 HLA-DQB1 0.353015151654053 0.634074738576959 0.0129101097689875 major histocompatibility complex, class II, DQ beta 1 FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.; . . . . 0.12207 . 7.699638782 99.92333097 28568.90925 33.37082 HLA-DQB1-AS1 . . . HLA-DQB1 antisense RNA 1 . . . . . . . . . . . HLA-DQB2 0.00935592869459469 0.812895752209809 0.177748319095596 major histocompatibility complex, class II, DQ beta 2 FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading. {ECO:0000269|PubMed:22407913}.; . TISSUE SPECIFICITY: Restricted to skin Langerhans cells (at protein level). {ECO:0000269|PubMed:22407913}.; . . 0.13783 . . . 221.62626 3.21955 HLA-DQB3 . . . major histocompatibility complex, class II, DQ beta 3 . . . . . . . . . . . HLA-DRA 0.700164889675938 0.296100199700572 0.00373491062348963 major histocompatibility complex, class II, DR alpha FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.; . . . . 0.14747 0.08778 0.3032669 72.009908 116.32725 2.34610 HLA-DRB1 5.62352879494898e-05 0.690484032840629 0.309459731871422 major histocompatibility complex, class II, DR beta 1 FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;oesophagus;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;epididymis;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . . . 2.971408917 99.1861288 6731.06694 17.41096 HLA-DRB2 . . . major histocompatibility complex, class II, DR beta 2 (pseudogene) . . . . . . . . . . . HLA-DRB3 . . . major histocompatibility complex, class II, DR beta 3 FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.; . . . . 0.20620 . . . . . HLA-DRB4 . . . major histocompatibility complex, class II, DR beta 4 FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.; . . . . . 0.07973 . . . . HLA-DRB5 0.0032272662883476 0.824923014710233 0.171849719001419 major histocompatibility complex, class II, DR beta 5 FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.; . . . . 0.04311 0.13590 4.551415577 99.75230007 16958.17858 27.72811 HLA-DRB6 . . . major histocompatibility complex, class II, DR beta 6 (pseudogene) . . . . . . . . . . . HLA-DRB7 . . . major histocompatibility complex, class II, DR beta 7 (pseudogene) . . . . . . . . . . . HLA-DRB8 . . . major histocompatibility complex, class II, DR beta 8 (pseudogene) . . . . . . . . . . . HLA-DRB9 . . . major histocompatibility complex, class II, DR beta 9 (pseudogene) . . . . . 0.10502 . . . . . HLA-E 0.347084032103792 0.650071866941134 0.0028441009550735 major histocompatibility complex, class I, E FUNCTION: Preferably binds to a peptide derived from the signal sequence of most HLA-A, -B, -C and -G molecules.; . . . . 0.16157 . 0.705562627 85.52724699 73.71608 1.79424 HLA-F 4.40041067524121e-05 0.851554694220994 0.148401301672254 major histocompatibility complex, class I, F FUNCTION: Involved in the presentation of foreign antigens to the immune system.; . . lymphoreticular;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cerebral cortex;endometrium;bone;iris;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;small intestine;heart;tongue;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;macula lutea;liver;spleen;head and neck;cervix;kidney;stomach; . 0.09799 . 1.394519284 94.6685539 1783.18039 7.79708 HLA-F-AS1 . . . HLA-F antisense RNA 1 . . . . . . . . . . . HLA-G 9.54870629366445e-08 0.172321091050293 0.827678813462644 major histocompatibility complex, class I, G FUNCTION: Involved in the presentation of foreign antigens to the immune system. Plays a role in maternal tolerance of the fetus by mediating protection from the deleterious effects of natural killer cells, cytotoxic T-lymphocytes, macrophages and mononuclear cells.; . TISSUE SPECIFICITY: Expressed in trophoblasts.; unclassifiable (Anatomical System);ovary;placenta;testis;parathyroid;blood; . 0.10600 . 0.086440867 60.47416844 1614.20809 7.43550 HLA-H . . . major histocompatibility complex, class I, H (pseudogene) FUNCTION: Involved in the presentation of foreign antigens to the immune system.; . . . . . . . . . . HLA-J . . . major histocompatibility complex, class I, J (pseudogene) . . . . . . . . . . . HLA-K . . . major histocompatibility complex, class I, K (pseudogene) . . . . . . . . . . . HLA-L . . . major histocompatibility complex, class I, L (pseudogene) . . . . . . . . . . . HLA-N . . . major histocompatibility complex, class I, N (pseudogene) . . . . . . . . . . . HLA-P . . . major histocompatibility complex, class I, P (pseudogene) . . . . . . . . . . . HLA-S . . . major histocompatibility complex, class I, S (pseudogene) . . . . . . . . . . . HLA-T . . . major histocompatibility complex, class I, T (pseudogene) . . . . . . . . . . . HLA-U . . . major histocompatibility complex, class I, U (pseudogene) . . . . . . . . . . . HLA-V . . . major histocompatibility complex, class I, V (pseudogene) . . . . . . . . . . . HLA-W . . . major histocompatibility complex, class I, W (pseudogene) . . . . . . . . . . . HLA-X . . . major histocompatibility complex, class I, X (pseudogene) . . . . . . . . . . . HLA-Y . . . major histocompatibility complex, class I, Y (pseudogene) . . . . . . . . . . . HLA-Z . . . major histocompatibility complex, class I, Z (pseudogene) . . . . . . . . . . . HLCS 0.486548323659441 0.513252415191493 0.000199261149065693 holocarboxylase synthetase FUNCTION: Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl- CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase.; . TISSUE SPECIFICITY: Mostly expressed in muscle, placenta, in lesser extent in the brain, kidney, pancreas, liver and lung.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;adrenal cortex;lens;skeletal muscle;lung;placenta;macula lutea;liver;alveolus;amnion;spleen;head and neck;cervix;kidney;mammary gland; uterus corpus;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cingulate cortex; 0.07149 0.25106 -0.591542347 18.24722812 151.46286 2.69061 HLCS-IT1 . . . HLCS intronic transcript 1 . . . . . . . . . . . HLF 0.87786179819329 0.12064087689146 0.00149732491524981 hepatic leukemia factor . DISEASE: Note=A chromosomal aberration involving HLF is a cause of pre-B-cell acute lymphoblastic leukemia (B-ALL). Translocation t(17;19)(q22;p13.3) with TCF3.; TISSUE SPECIFICITY: Highly expressed in liver; lower levels in lung and kidney.; unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;lung;frontal lobe;placenta;macula lutea;visual apparatus;liver;testis;head and neck;spleen;kidney;brain;mammary gland; whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;atrioventricular node;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.47087 0.13588 -0.317668748 31.45789101 7.36104 0.27404 HLFP1 . . . hepatic leukemia factor pseudogene 1 . . . . . . . . . . . HLTF 6.80799092701924e-20 0.0236002122135326 0.976399787786467 helicase-like transcription factor FUNCTION: Has both helicase and E3 ubiquitin ligase activities. Possesses intrinsic ATP-dependent nucleosome-remodeling activity; This activity may be required for transcriptional activation or repression of specific target promoters (By similarity). These may include the SERPINE1 and HIV-1 promoters and the SV40 enhancer, to which this protein can bind directly. Plays a role in error-free postreplication repair (PRR) of damaged DNA and maintains genomic stability through acting as a ubiquitin ligase for 'Lys-63'-linked polyubiquitination of chromatin-bound PCNA. {ECO:0000250, ECO:0000269|PubMed:10391891, ECO:0000269|PubMed:18316726, ECO:0000269|PubMed:18719106, ECO:0000269|PubMed:7876228, ECO:0000269|PubMed:8672239, ECO:0000269|PubMed:9126292}.; . TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. {ECO:0000269|PubMed:8672239, ECO:0000269|PubMed:9126292}.; myocardium;medulla oblongata;smooth muscle;ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;macula lutea;visual apparatus;liver;cervix;kidney;peripheral nerve; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.49829 0.15627 0.960822749 90.18636471 889.98091 5.81292 HLTF-AS1 . . . HLTF antisense RNA 1 . . . . . . . . . . . HLX 0.561219969045613 0.4361136694995 0.00266636145488703 H2.0-like homeobox FUNCTION: Transcription factor required for TBX21/T-bet-dependent maturation of Th1 cells as well as maintenance of Th1-specific gene expression. Involved in embryogenesis and hematopoiesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Low level in normal B and T-cells, high level in activated lymphocytes and monocytes. Also found in thymus, tonsil, bone marrow, developing vessels, and fetal brain.; . . 0.24235 0.15740 0.619191319 83.36282142 4095.05049 12.70135 HLX-AS1 . . . HLX antisense RNA 1 . . . . . . . . . . . HM13 0.882288325132847 0.117654415673903 5.72591932495301e-05 histocompatibility (minor) 13 FUNCTION: Catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein, resulting in the release of the fragment from the ER membrane into the cytoplasm. Required to generate lymphocyte cell surface (HLA-E) epitopes derived from MHC class I signal peptides (PubMed:11714810). May be necessary for the removal of the signal peptide that remains attached to the hepatitis C virus core protein after the initial proteolytic processing of the polyprotein (PubMed:12145199). Involved in the intramembrane cleavage of the integral membrane protein PSEN1 (PubMed:12077416, PubMed:11714810, PubMed:14741365). Cleaves the integral membrane protein XBP1 isoform 1 in a DERL1/RNF139-dependent manner (PubMed:25239945). May play a role in graft rejection (By similarity). {ECO:0000250|UniProtKB:Q9D8V0, ECO:0000269|PubMed:11714810, ECO:0000269|PubMed:12077416, ECO:0000269|PubMed:12145199, ECO:0000269|PubMed:14741365, ECO:0000269|PubMed:25239945}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in kidney, liver, placenta, lung, leukocytes and small intestine and reduced expression in heart and skeletal muscle. Expressed abundantly in the CNS with highest levels in thalamus and medulla. {ECO:0000269|PubMed:12139484, ECO:0000269|PubMed:12972007}.; ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; . 0.29362 0.22177 -0.427900189 25.14744043 28.97209 0.92612 HM13-AS1 . . . HM13 antisense RNA 1 . . . . . . . . . . . HM13-IT1 . . . HM13 intronic transcript 1 . . . . . . . . . . . HMBOX1 0.997096381434551 0.00290358976117465 2.88042742931643e-08 homeobox containing 1 FUNCTION: Transcription factor. Isoform 1 acts as a transcriptional repressor. Isoform 4 has very low activity as a transcriptional repressor. {ECO:0000269|PubMed:16825764, ECO:0000269|PubMed:19757162}.; . TISSUE SPECIFICITY: Ubiquitous. Detected in pancreas, brain, spleen, placenta, prostate, thymus, liver, heart, bone marrow, skeletal muscle, stomach, uterus, testis, kidney, ovary, and colon. {ECO:0000269|PubMed:16825764, ECO:0000269|PubMed:19757162}.; ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;breast;lung;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion; 0.48328 0.09421 -0.339715008 30.06605331 30.16957 0.96283 HMBOX1-IT1 . . . HMBOX1 intronic transcript 1 . . . . . . . . . . . HMBS 0.944813615556974 0.0551781780960097 8.20634701622723e-06 hydroxymethylbilane synthase FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.; . TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed. Isoform 2 is found only in erythroid cells. {ECO:0000269|PubMed:3422427}.; medulla oblongata;ovary;sympathetic chain;colon;parathyroid;skin;uterus;prostate;whole body;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;muscle;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;fetal liver;superior cervical ganglion;trigeminal ganglion;skeletal muscle;bone marrow; 0.38026 0.69128 -0.337894035 30.37272942 24.11657 0.79217 HMCES 4.51657466936959e-05 0.855418047809758 0.144536786443548 5-hydroxymethylcytosine (hmC) binding, ES cell-specific FUNCTION: Specifically binds 5-hydroxymethylcytosine (5hmC)- containing DNA in stem cells, suggesting that it acts as a specific reader of 5hmC in stem cells (By similarity). May act as a peptidase; experimental evidences are however required to confirm this prediction (PubMed:23945014). {ECO:0000250, ECO:0000269|PubMed:23945014}.; . . . . 0.10176 . -0.53631094 20.53550366 420.57757 4.28299 HMCN1 2.19206065668674e-18 1 6.41537883948367e-24 hemicentin 1 . . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in skin fibroblasts and retinal pigment epithelium (RPE) cells. {ECO:0000269|PubMed:14570714}.; unclassifiable (Anatomical System);cartilage;skin;skeletal muscle;breast;uterus;whole body;lung;larynx;bone;thyroid;placenta;duodenum;liver;head and neck;kidney;spinal ganglion;mammary gland;artery;aorta;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin;cerebellum; 0.11657 0.21661 -3.689691478 0.247699929 8270.20936 19.62945 HMCN2 . . . hemicentin 2 . . . unclassifiable (Anatomical System);heart;ovary;cartilage;colon;parathyroid;skin;uterus;prostate;lung;placenta;testis;cervix;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12716 . . . 2669.68768 9.71594 HMG20A 0.932476251384682 0.0675100798967252 1.36687185929244e-05 high mobility group 20A FUNCTION: Plays a role in neuronal differentiation as chromatin- associated protein. Acts as inhibitor of HMG20B. Overcomes the repressive effects of the neuronal silencer REST and induces the activation of neuronal-specific genes. Involved in the recruitment of the histone methyltransferase KMT2A/MLL1 and consequent increased methylation of histone H3 lysine 4 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10773667}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;cerebellum; amygdala;superior cervical ganglion;prefrontal cortex;testis;caudate nucleus; 0.56924 0.10992 -0.161524709 41.6430762 16.35078 0.57973 HMG20B 0.342236180884619 0.643758262690189 0.0140055564251922 high mobility group 20B FUNCTION: Required for correct progression through G2 phase of the cell cycle and entry into mitosis. Required for RCOR1/CoREST mediated repression of neuronal specific gene promoters.; . TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues. {ECO:0000269|PubMed:10773667, ECO:0000269|PubMed:11997092}.; lymphoreticular;smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;medulla oblongata;prostate;placenta;kidney; 0.54724 . -0.207437529 38.2814343 23.95513 0.78870 HMGA1 0.724299774339856 0.262579443651955 0.0131207820081894 high mobility group AT-hook 1 FUNCTION: HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions.; DISEASE: Note=A chromosomal aberration involving HMGA1 is found in pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23-24) with RAD51B. {ECO:0000269|PubMed:11978964}.; . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;endometrium;larynx;bone;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;duodenum;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach;aorta; fetal liver;testis;tumor; 0.99432 0.53499 -0.053113545 49.38664779 74.66102 1.80667 HMGA1P1 . . . high mobility group AT-hook 1 pseudogene 1 . . . . . . . . . . . HMGA1P2 . . . high mobility group AT-hook 1 pseudogene 2 . . . . . . . . . . . HMGA1P3 . . . high mobility group AT-hook 1 pseudogene 3 . . . . . . . . . . . HMGA1P4 . . . high mobility group AT-hook 1 pseudogene 4 . . . . . . . . . . . HMGA1P5 . . . high mobility group AT-hook 1 pseudogene 5 . . . . . . . . . . . HMGA1P6 . . . high mobility group AT-hook 1 pseudogene 6 . . . . . . . . . . . HMGA1P7 . . . high mobility group AT-hook 1 pseudogene 7 . . . . . . . . . . . HMGA1P8 . . . high mobility group AT-hook 1 pseudogene 8 . . . . . . . . . . . HMGA2 0.733852103838821 0.254244628463731 0.0119032676974485 high mobility group AT-hook 2 FUNCTION: Functions as a transcriptional regulator. Functions in cell cycle regulation through CCNA2. Plays an important role in chromosome condensation during the meiotic G2/M transition of spermatocytes. {ECO:0000269|PubMed:14645522}.; DISEASE: Note=A chromosomal aberration involving HMGA2 is associated with a subclass of benign mesenchymal tumors known as lipomas. Translocation t(3;12)(q27-q28;q13-q15) with LPP is shown in lipomas. HMGA2 is also fused with a number of other genes in lipomas. {ECO:0000269|PubMed:8824803}.; DISEASE: Note=A chromosomal aberration involving HMGA2 is associated with pulmonary chondroid hamartomas. Translocation t(3;12)(q27-q28;q14-q15) with LPP is detected in pulmonary chondroid hamartomas. {ECO:0000269|PubMed:11066083}.; DISEASE: Note=A chromosomal aberration involving HMGA2 is associated with parosteal lipomas. Translocation t(3;12)(q28;q14) with LPP is also shown in one parosteal lipoma. {ECO:0000269|PubMed:9772904}.; DISEASE: Note=A chromosomal aberration involving HMGA2 is found in uterine leiomyoma. Translocation t(12;14)(q15;q23-24) with RAD51B. Chromosomal rearrangements involving HMGA2 do not seem to be the principle pathobiological mechanism in uterine leiomyoma. {ECO:0000269|PubMed:12649198, ECO:0000269|PubMed:9892177}.; . unclassifiable (Anatomical System);bile duct;prostate;bone;testis;colon; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.55673 0.47945 0.191216164 66.57230479 44.48147 1.27567 HMGB1 0.633893930973864 0.359208895852383 0.00689717317375289 high mobility group box 1 FUNCTION: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance (PubMed:23519706, PubMed:23446148, PubMed:23994764, PubMed:25048472). Has proangiogdenic activity (By similarity). May be involved in platelet activation (By similarity). Binds to phosphatidylserine and phosphatidylethanolamide (By similarity). Bound to RAGE mediates signaling for neuronal outgrowth (By similarity). May play a role in accumulation of expanded polyglutamine (polyQ) proteins such as huntingtin (HTT) or TBP (PubMed:23303669, PubMed:25549101). {ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P12682, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:23303669, ECO:0000269|PubMed:25549101, ECO:0000305|PubMed:23446148, ECO:0000305|PubMed:23519706, ECO:0000305|PubMed:23994764, ECO:0000305|PubMed:25048472}.; FUNCTION: In the cytoplasm proposed to dissociate the BECN1:BCL2 complex via competitive interaction with BECN1 leading to autophagy activation (PubMed:20819940). Involved in oxidative stress-mediated autophagy (PubMed:21395369). Can protect BECN1 and ATG5 from calpain-mediated cleavage and thus proposed to control their proautophagic and proapoptotic functions and to regulate the extent and severity of inflammation-associated cellular injury (By similarity). In myeloid cells has a protective role against endotoxemia and bacterial infection by promoting autophagy (By similarity). Involved in endosomal translocation and activation of TLR9 in response to CpG-DNA in macrophages (By similarity). {ECO:0000250|UniProtKB:P63158, ECO:0000269|PubMed:20819940, ECO:0000269|PubMed:21395369}.; . TISSUE SPECIFICITY: Ubiquituous. Expressed in platelets (PubMed:11154118). {ECO:0000269|PubMed:11154118}.; ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;oral cavity;muscle;bile duct;pancreas;lung;pia mater;cornea;placenta;duodenum;head and neck;kidney;stomach;aorta; . . . -0.207437529 38.2814343 32.26454 1.00993 HMGB1P1 . . . high mobility group box 1 pseudogene 1 FUNCTION: Binds preferentially single-stranded DNA and unwinds double-stranded DNA. {ECO:0000250}.; . . . . 0.23982 . . . . . HMGB1P3 . . . high mobility group box 1 pseudogene 3 . . . . . . . . . . . HMGB1P4 . . . high mobility group box 1 pseudogene 4 . . . . . . . . . . . HMGB1P5 . . . high mobility group box 1 pseudogene 5 . . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;prostate;thyroid;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach; . . 0.21093 . . . . HMGB1P6 . . . high mobility group box 1 pseudogene 6 . . . . . . . . . . . HMGB1P7 . . . high mobility group box 1 pseudogene 7 . . . . . . . . . . . HMGB1P8 . . . high mobility group box 1 pseudogene 8 . . . . . . . . . . . HMGB1P9 . . . high mobility group box 1 pseudogene 9 . . . . . . . . . . . HMGB1P10 . . . high mobility group box 1 pseudogene 10 . . . . . . . . . . . HMGB1P11 . . . high mobility group box 1 pseudogene 11 . . . . . . . . . . . HMGB1P12 . . . high mobility group box 1 pseudogene 12 . . . . . . . . . . . HMGB1P13 . . . high mobility group box 1 pseudogene 13 . . . . . . . . . . . HMGB1P14 . . . high mobility group box 1 pseudogene 14 . . . . . . . . . . . HMGB1P15 . . . high mobility group box 1 pseudogene 15 . . . . . . . . . . . HMGB1P16 . . . high mobility group box 1 pseudogene 16 . . . . . . . . . . . HMGB1P17 . . . high mobility group box 1 pseudogene 17 . . . . . . . . . . . HMGB1P18 . . . high mobility group box 1 pseudogene 18 . . . . . . . . . . . HMGB1P19 . . . high mobility group box 1 pseudogene 19 . . . . . . . . . . . HMGB1P20 . . . high mobility group box 1 pseudogene 20 . . . . . . . . . . . HMGB1P21 . . . high mobility group box 1 pseudogene 21 . . . . . . . . . . . HMGB1P22 . . . high mobility group box 1 pseudogene 22 . . . . . . . . . . . HMGB1P23 . . . high mobility group box 1 pseudogene 23 . . . . . . . . . . . HMGB1P24 . . . high mobility group box 1 pseudogene 24 . . . . . . . . . . . HMGB1P25 . . . high mobility group box 1 pseudogene 25 . . . . . . . . . . . HMGB1P26 . . . high mobility group box 1 pseudogene 26 . . . . . . . . . . . HMGB1P27 . . . high mobility group box 1 pseudogene 27 . . . . . . . . . . . HMGB1P28 . . . high mobility group box 1 pseudogene 28 . . . . . . . . . . . HMGB1P29 . . . high mobility group box 1 pseudogene 29 . . . . . . . . . . . HMGB1P30 . . . high mobility group box 1 pseudogene 30 . . . . . . . . . . . HMGB1P31 . . . high mobility group box 1 pseudogene 31 . . . . . . . . . . . HMGB1P32 . . . high mobility group box 1 pseudogene 32 . . . . . . . . . . . HMGB1P33 . . . high mobility group box 1 pseudogene 33 . . . . . . . . . . . HMGB1P34 . . . high mobility group box 1 pseudogene 34 . . . . . . . . . . . HMGB1P35 . . . high mobility group box 1 pseudogene 35 . . . . . . . . . . . HMGB1P36 . . . high mobility group box 1 pseudogene 36 . . . . . . . . . . . HMGB1P37 . . . high mobility group box 1 pseudogene 37 . . . . . . . . . . . HMGB1P38 . . . high mobility group box 1 pseudogene 38 . . . . . . . . . . . HMGB1P39 . . . high mobility group box 1 pseudogene 39 . . . . . . . . . . . HMGB1P40 . . . high mobility group box 1 pseudogene 40 . . . . . . . . . . . HMGB1P41 . . . high mobility group box 1 pseudogene 41 . . . . . . . . . . . HMGB1P42 . . . high mobility group box 1 pseudogene 42 . . . . . . . . . . . HMGB1P43 . . . high mobility group box 1 pseudogene 43 . . . . . . . . . . . HMGB1P44 . . . high mobility group box 1 pseudogene 44 . . . . . . . . . . . HMGB1P45 . . . high mobility group box 1 pseudogene 45 . . . . . . . . . . . HMGB1P46 . . . high mobility group box 1 pseudogene 46 . . . . . . . . . . . HMGB1P47 . . . high mobility group box 1 pseudogene 47 . . . . . . . . . . . HMGB1P48 . . . high mobility group box 1 pseudogene 48 . . . . . . . . . . . HMGB1P49 . . . high mobility group box 1 pseudogene 49 . . . . . . . . . . . HMGB2 0.907849743135355 0.0914241264464482 0.000726130418197312 high mobility group box 2 FUNCTION: Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. In the nucleus is an abundant chromatin-associated non-histone protein involved in transcription, chromatin remodeling and V(D)J recombination and probably other processes. Binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity (PubMed:7797075, PubMed:11909973, PubMed:19522541, PubMed:18413230, PubMed:19965638, PubMed:20123072). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS) (By similarity). Proposed to be involved in the innate immune response to nucleic acids by acting as a promiscuous immunogenic DNA/RNA sensor which cooperates with subsequent discriminative sensing by specific pattern recognition receptors (By similarity). In the extracellular compartment acts as a chemokine. Promotes proliferation and migration of endothelial cells implicating AGER/RAGE (PubMed:19811285). Has antimicrobial activity in gastrointestinal epithelial tissues (PubMed:23877675). Involved in inflammatory response to antigenic stimulus coupled with proinflammatory activity (By similarity). Involved in modulation of neurogenesis probably by regulation of neural stem proliferation (By similarity). Involved in articular cartilage surface maintenance implicating LEF1 and the Wnt/beta-catenin pathway (By similarity). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P30681, ECO:0000269|PubMed:11909973, ECO:0000269|PubMed:18413230, ECO:0000269|PubMed:19522541, ECO:0000269|PubMed:19811285, ECO:0000269|PubMed:19965638, ECO:0000269|PubMed:23877675, ECO:0000269|PubMed:7797075, ECO:0000305|PubMed:20123072}.; . TISSUE SPECIFICITY: Expressed in gastric and intestinal tissues (at protein level). {ECO:0000269|PubMed:23877675}.; smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;bile duct;pancreas;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; testis - interstitial;fetal liver;testis - seminiferous tubule;tumor;testis;white blood cells;whole blood;tonsil;bone marrow;thymus; 0.93997 0.22063 -0.031067188 51.03798066 28.58852 0.91569 HMGB2P1 . . . high mobility group box 2 pseudogene 1 . . . . . . . . . . . HMGB3 0.770459764489854 0.221598282249246 0.00794195326090004 high mobility group box 3 FUNCTION: Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. Associates with chromatin and binds DNA with a preference to non- canonical DNA structures such as single-stranded DNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters (By similarity). Proposed to be involved in the innate immune response to nucleic acids by acting as a cytoplasmic promiscuous immunogenic DNA/RNA sensor (By similarity). Negatively regulates B-cell and myeloid cell differentiation. In hematopoietic stem cells may regulate the balance between self-renewal and differentiation. Involved in negative regulation of canonical Wnt signaling (By similarity). {ECO:0000250|UniProtKB:O54879, ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P40618}.; DISEASE: Microphthalmia, syndromic, 13 (MCOPS13) [MIM:300915]: A form of microphthalmia, a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. MCOPS13 patients exhibit colobomatous microphthalmia with microcephaly, short stature, and psychomotor retardation. {ECO:0000269|PubMed:24993872}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly in placenta.; . . 0.93520 0.14229 -0.031067188 51.03798066 2.88181 0.10223 HMGB3P1 . . . high mobility group box 3 pseudogene 1 . . . . . . . . . . . HMGB3P2 . . . high mobility group box 3 pseudogene 2 . . . . . . . . . . . HMGB3P3 . . . high mobility group box 3 pseudogene 3 . . . . . . . . . . . HMGB3P4 . . . high mobility group box 3 pseudogene 4 . . . . . . . . . . . HMGB3P5 . . . high mobility group box 3 pseudogene 5 . . . . . . . . . . . HMGB3P6 . . . high mobility group box 3 pseudogene 6 . . . . . . . . . . . HMGB3P7 . . . high mobility group box 3 pseudogene 7 . . . . . . . . . . . HMGB3P8 . . . high mobility group box 3 pseudogene 8 . . . . . . . . . . . HMGB3P9 . . . high mobility group box 3 pseudogene 9 . . . . . . . . . . . HMGB3P10 . . . high mobility group box 3 pseudogene 10 . . . . . . . . . . . HMGB3P11 . . . high mobility group box 3 pseudogene 11 . . . . . . . . . . . HMGB3P12 . . . high mobility group box 3 pseudogene 12 . . . . . . . . . . . HMGB3P13 . . . high mobility group box 3 pseudogene 13 . . . . . . . . . . . HMGB3P14 . . . high mobility group box 3 pseudogene 14 . . . . . . . . . . . HMGB3P15 . . . high mobility group box 3 pseudogene 15 . . . . . . . . . . . HMGB3P16 . . . high mobility group box 3 pseudogene 16 . . . . . . . . . . . HMGB3P17 . . . high mobility group box 3 pseudogene 17 . . . . . . . . . . . HMGB3P18 . . . high mobility group box 3 pseudogene 18 . . . . . . . . . . . HMGB3P19 . . . high mobility group box 3 pseudogene 19 . . . . . . . . . . . HMGB3P20 . . . high mobility group box 3 pseudogene 20 . . . . . . . . . . . HMGB3P21 . . . high mobility group box 3 pseudogene 21 . . . . . . . . . . . HMGB3P22 . . . high mobility group box 3 pseudogene 22 . . . . . . . . . . . HMGB3P23 . . . high mobility group box 3 pseudogene 23 . . . . . . . . . . . HMGB3P24 . . . high mobility group box 3 pseudogene 24 . . . . . . . . . . . HMGB3P25 . . . high mobility group box 3 pseudogene 25 . . . . . . . . . . . HMGB3P26 . . . high mobility group box 3 pseudogene 26 . . . . . . . . . . . HMGB3P27 . . . high mobility group box 3 pseudogene 27 . . . . . . . . . . . HMGB3P28 . . . high mobility group box 3 pseudogene 28 . . . . . . . . . . . HMGB3P29 . . . high mobility group box 3 pseudogene 29 . . . . . . . . . . . HMGB3P30 . . . high mobility group box 3 pseudogene 30 . . . . . . . . . . . HMGB3P31 . . . high mobility group box 3 pseudogene 31 . . . . . . . . . . . HMGB3P32 . . . high mobility group box 3 pseudogene 32 . . . . . . . . . . . HMGB4 9.96360941849729e-06 0.191619450918095 0.808370585472487 high mobility group box 4 . . . . . 0.03889 0.07350 0.68351529 85.03774475 92.42199 2.06677 HMGCL 0.00256252926835471 0.932213320581801 0.0652241501498445 3-hydroxymethyl-3-methylglutaryl-CoA lyase FUNCTION: Key enzyme in ketogenesis (ketone body formation). Terminal step in leucine catabolism. Ketone bodies (beta- hydroxybutyrate, acetoacetate and acetone) are essential as an alternative source of energy to glucose, as lipid precursors and as regulators of metabolism. {ECO:0000269|PubMed:22847177, ECO:0000269|PubMed:22865860, ECO:0000269|PubMed:8566388}.; . TISSUE SPECIFICITY: Highest expression in liver. Expressed in pancreas, kidey, intestine, testis, fibroblasts and lymphoblasts. Very low expression in brain and skeletal muscle. The relative expression of isoform 2 (at mRNA level) is highest in heart (30%), skeletal muscle (22%), and brain (14%). {ECO:0000269|PubMed:21952825}.; lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; liver;kidney;skeletal muscle; 0.08547 0.24601 -0.60427181 17.74593064 31.95009 1.00489 HMGCLL1 8.77269111699165e-07 0.512524617652996 0.487474505077893 3-hydroxymethyl-3-methylglutaryl-CoA lyase-like 1 FUNCTION: Non-mitochondrial 3-hydroxymethyl-3-methylglutaryl-CoA lyase that catalyzes a cation-dependent cleavage of (S)-3-hydroxy- 3-methylglutaryl-CoA into acetyl-CoA and acetoacetate, a key step in ketogenesis, the products of which support energy production in nonhepatic animal tissues. {ECO:0000269|PubMed:22847177, ECO:0000269|PubMed:22865860}.; . . unclassifiable (Anatomical System);lung;whole body;islets of Langerhans;hippocampus;testis;brain; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.11966 0.16464 0.106667882 61.73036093 48.27497 1.35412 HMGCR 0.999836644997739 0.000163354997018844 5.24241070920194e-12 3-hydroxy-3-methylglutaryl-CoA reductase FUNCTION: Transmembrane glycoprotein that is the rate-limiting enzyme in cholesterol biosynthesis as well as in the biosynthesis of nonsterol isoprenoids that are essential for normal cell function including ubiquinone and geranylgeranyl proteins.; . . lymphoreticular;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; amygdala;fetal liver;occipital lobe;fetal brain;adrenal gland;adrenal cortex; 0.89376 0.61671 -0.492218069 22.35786742 48.92052 1.36596 HMGCS1 0.972848684238687 0.0271444073599248 6.90840138789878e-06 3-hydroxy-3-methylglutaryl-CoA synthase 1 FUNCTION: This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);lymph node;hypothalamus;urinary;adrenal cortex;pharynx;blood;skeletal muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; fetal liver;occipital lobe;superior cervical ganglion;fetal brain;hypothalamus;prefrontal cortex;globus pallidus;atrioventricular node;parietal lobe; 0.37751 0.40200 -0.405853867 26.23260203 38.55982 1.14337 HMGCS2 1.06116787483877e-08 0.520211434993224 0.479788554395097 3-hydroxy-3-methylglutaryl-CoA synthase 2 FUNCTION: This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase.; DISEASE: 3-hydroxy-3-methylglutaryl-CoA synthase-2 deficiency (HMGCS2D) [MIM:605911]: A metabolic disorder characterized by severe hypoketotic hypoglycemia, encephalopathy, and hepatomegaly. {ECO:0000269|PubMed:11228257, ECO:0000269|PubMed:11479731, ECO:0000269|PubMed:12647205}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expression in liver is 200-fold higher than in any other tissue. Low expression in colon, kidney, testis, and pancreas. Very low expression in heart and skeletal muscle. Not detected in brain. The relative expression of isoform 3 (at mRNA level) is highest in heart (70%) and skeletal muscle (60%). {ECO:0000269|PubMed:16940161, ECO:0000269|PubMed:21952825, ECO:0000269|PubMed:7893153}.; . . 0.20011 0.27949 -0.867014353 10.72776598 66.95673 1.69109 HMGN1 0.425365462309957 0.541410677129897 0.0332238605601455 high mobility group nucleosome binding domain 1 FUNCTION: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation. Inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2 (By similarity). {ECO:0000250}.; . . ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;brain;bladder;tonsil;heart;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;choroid;vein;uterus;oesophagus;larynx;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;aorta;stomach; . 0.46691 0.07886 0.3032669 72.009908 414.2321 4.26339 HMGN1P1 . . . high mobility group nucleosome binding domain 1 pseudogene 1 . . . . . . . . . . . HMGN1P2 . . . high mobility group nucleosome binding domain 1 pseudogene 2 . . . . . . . . . . . HMGN1P3 . . . high mobility group nucleosome binding domain 1 pseudogene 3 . . . . . . . . . . . HMGN1P4 . . . high mobility group nucleosome binding domain 1 pseudogene 4 . . . . . . . . . . . HMGN1P5 . . . high mobility group nucleosome binding domain 1 pseudogene 5 . . . . . . . . . . . HMGN1P6 . . . high mobility group nucleosome binding domain 1 pseudogene 6 . . . . . . . . . . . HMGN1P7 . . . high mobility group nucleosome binding domain 1 pseudogene 7 . . . . . . . . . . . HMGN1P8 . . . high mobility group nucleosome binding domain 1 pseudogene 8 . . . . . . . . . . . HMGN1P9 . . . high mobility group nucleosome binding domain 1 pseudogene . . . . . . . . . . . HMGN1P10 . . . high mobility group nucleosome binding domain 1 pseudogene 10 . . . . . . . . . . . HMGN1P11 . . . high mobility group nucleosome binding domain 1 pseudogene 11 . . . . . . . . . . . HMGN1P12 . . . high mobility group nucleosome binding domain 1 pseudogene 12 . . . . . . . . . . . HMGN1P13 . . . high mobility group nucleosome binding domain 1 pseudogene 13 . . . . . . . . . . . HMGN1P14 . . . high mobility group nucleosome binding domain 1 pseudogene 14 . . . . . . . . . . . HMGN1P15 . . . high mobility group nucleosome binding domain 1 pseudogene 15 . . . . . . . . . . . HMGN1P16 . . . high mobility group nucleosome binding domain 1 pseudogene 16 . . . . . . . . . . . HMGN1P17 . . . high mobility group nucleosome binding domain 1 pseudogene 17 . . . . . . . . . . . HMGN1P18 . . . high mobility group nucleosome binding domain 1 pseudogene 18 . . . . . . . . . . . HMGN1P19 . . . high mobility group nucleosome binding domain 1 pseudogene 19 . . . . . . . . . . . HMGN1P20 . . . high mobility group nucleosome binding domain 1 pseudogene 20 . . . . . . . . . . . HMGN1P21 . . . high mobility group nucleosome binding domain 1 pseudogene 21 . . . . . . . . . . . HMGN1P22 . . . high mobility group nucleosome binding domain 1 pseudogene 22 . . . . . . . . . . . HMGN1P23 . . . high mobility group nucleosome binding domain 1 pseudogene 23 . . . . . . . . . . . HMGN1P24 . . . high mobility group nucleosome binding domain 1 pseudogene 24 . . . . . . . . . . . HMGN1P25 . . . high mobility group nucleosome binding domain 1 pseudogene 25 . . . . . . . . . . . HMGN1P26 . . . high mobility group nucleosome binding domain 1 pseudogene 26 . . . . . . . . . . . HMGN1P27 . . . high mobility group nucleosome binding domain 1 pseudogene 27 . . . . . . . . . . . HMGN1P28 . . . high mobility group nucleosome binding domain 1 pseudogene 28 . . . . . . . . . . . HMGN1P29 . . . high mobility group nucleosome binding domain 1 pseudogene 29 . . . . . . . . . . . HMGN1P30 . . . high mobility group nucleosome binding domain 1 pseudogene 30 . . . . . . . . . . . HMGN1P31 . . . high mobility group nucleosome binding domain 1 pseudogene 31 . . . . . . . . . . . HMGN1P32 . . . high mobility group nucleosome binding domain 1 pseudogene 32 . . . . . . . . . . . HMGN1P33 . . . high mobility group nucleosome binding domain 1 pseudogene 33 . . . . . . . . . . . HMGN1P34 . . . high mobility group nucleosome binding domain 1 pseudogene 34 . . . . . . . . . . . HMGN1P35 . . . high mobility group nucleosome binding domain 1 pseudogene 35 . . . testis; . . . . . . . HMGN1P36 . . . high mobility group nucleosome binding domain 1 pseudogene 36 . . . . . . . . . . . HMGN1P37 . . . high mobility group nucleosome binding domain 1 pseudogene 37 . . . . . . . . . . . HMGN1P38 . . . high mobility group nucleosome binding domain 1 pseudogene 38 . . . . . . . . . . . HMGN2 0.79667455877069 0.197599998301451 0.00572544292785892 high mobility group nucleosomal binding domain 2 FUNCTION: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation (By similarity). {ECO:0000250}.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.91320 0.15588 0.057118534 57.99716914 1.14949 0.03142 HMGN2P1 . . . high mobility group nucleosomal binding domain 2 pseudogene 1 . . . . . . . . . . . HMGN2P2 . . . high mobility group nucleosomal binding domain 2 pseudogene 2 . . . . . . . . . . . HMGN2P3 . . . high mobility group nucleosomal binding domain 2 pseudogene 3 . . . . . . . . . . . HMGN2P4 . . . high mobility group nucleosomal binding domain 2 pseudogene 4 . . . . . . . . . . . HMGN2P5 . . . high mobility group nucleosomal binding domain 2 pseudogene 5 . . . . . . . . . . . HMGN2P6 . . . high mobility group nucleosomal binding domain 2 pseudogene 6 . . . . . . . . . . . HMGN2P7 . . . high mobility group nucleosomal binding domain 2 pseudogene 7 . . . . . . . . . . . HMGN2P8 . . . high mobility group nucleosomal binding domain 2 pseudogene 8 . . . . . . . . . . . HMGN2P9 . . . high mobility group nucleosomal binding domain 2 pseudogene 9 . . . . . . . . . . . HMGN2P10 . . . high mobility group nucleosomal binding domain 2 pseudogene10 . . . . . . . . . . . HMGN2P11 . . . high mobility group nucleosomal binding domain 2 pseudogene 11 . . . . . . . . . . . HMGN2P12 . . . high mobility group nucleosomal binding domain 2 pseudogene 12 . . . . . . . . . . . HMGN2P13 . . . high mobility group nucleosomal binding domain 2 pseudogene 13 . . . . . . . . . . . HMGN2P14 . . . high mobility group nucleosomal binding domain 2 pseudogene14 . . . . . . . . . . . HMGN2P15 . . . high mobility group nucleosomal binding domain 2 pseudogene 15 . . . . . . . . . . . HMGN2P16 . . . high mobility group nucleosomal binding domain 2 pseudogene 16 . . . . . . . . . . . HMGN2P17 . . . high mobility group nucleosomal binding domain 2 pseudogene 17 . . . . . . . . . . . HMGN2P18 . . . high mobility group nucleosomal binding domain 2 pseudogene 18 . . . . . . . . . . . HMGN2P19 . . . high mobility group nucleosomal binding domain 2 pseudogene 19 . . . . . . . . . . . HMGN2P20 . . . high mobility group nucleosomal binding domain 2 pseudogene 20 . . . . . . . . . . . HMGN2P21 . . . high mobility group nucleosomal binding domain 2 pseudogene 21 . . . . . . . . . . . HMGN2P22 . . . high mobility group nucleosomal binding domain 2 pseudogene 22 . . . . . . . . . . . HMGN2P23 . . . high mobility group nucleosomal binding domain 2 pseudogene 23 . . . . . . . . . . . HMGN2P24 . . . high mobility group nucleosomal binding domain 2 pseudogene 24 . . . . . . . . . . . HMGN2P25 . . . high mobility group nucleosomal binding domain 2 pseudogene 25 . . . . . . . . . . . HMGN2P26 . . . high mobility group nucleosomal binding domain 2 pseudogene 26 . . . . . . . . . . . HMGN2P27 . . . high mobility group nucleosomal binding domain 2 pseudogene 27 . . . . . . . . . . . HMGN2P28 . . . high mobility group nucleosomal binding domain 2 pseudogene 28 . . . . . . . . . . . HMGN2P29 . . . high mobility group nucleosomal binding domain 2 pseudogene 29 . . . . . . . . . . . HMGN2P30 . . . high mobility group nucleosomal binding domain 2 pseudogene 30 . . . . . . . . . . . HMGN2P31 . . . high mobility group nucleosomal binding domain 2 pseudogene 31 . . . . . . . . . . . HMGN2P32 . . . high mobility group nucleosomal binding domain 2 pseudogene 32 . . . . . . . . . . . HMGN2P33 . . . high mobility group nucleosomal binding domain 2 pseudogene 33 . . . . . . . . . . . HMGN2P34 . . . high mobility group nucleosomal binding domain 2 pseudogene 34 . . . . . . . . . . . HMGN2P35 . . . high mobility group nucleosomal binding domain 2 pseudogene 35 . . . . . . . . . . . HMGN2P36 . . . high mobility group nucleosomal binding domain 2 pseudogene 36 . . . . . . . . . . . HMGN2P37 . . . high mobility group nucleosomal binding domain 2 pseudogene 37 . . . . . . . . . . . HMGN2P38 . . . high mobility group nucleosomal binding domain 2 pseudogene 38 . . . . . . . . . . . HMGN2P39 . . . high mobility group nucleosomal binding domain 2 pseudogene 39 . . . . . . . . . . . HMGN2P40 . . . high mobility group nucleosomal binding domain 2 pseudogene 40 . . . . . . . . . . . HMGN2P41 . . . high mobility group nucleosomal binding domain 2 pseudogene 41 . . . . . . . . . . . HMGN2P42 . . . high mobility group nucleosomal binding domain 2 pseudogene 42 . . . . . . . . . . . HMGN2P43 . . . high mobility group nucleosomal binding domain 2 pseudogene 43 . . . . . . . . . . . HMGN2P44 . . . high mobility group nucleosomal binding domain 2 pseudogene 44 . . . . . . . . . . . HMGN2P45 . . . high mobility group nucleosomal binding domain 2 pseudogene 45 . . . . . . . . . . . HMGN2P46 . . . high mobility group nucleosomal binding domain 2 pseudogene 46 . . TISSUE SPECIFICITY: Very high expression in prostate and prostate cancer. Faint expression in other tissues. {ECO:0000269|PubMed:15027122}.; unclassifiable (Anatomical System); . 0.62873 0.12926 . . . . HMGN2P47 . . . high mobility group nucleosomal binding domain 2 pseudogene 47 . . . . . . . . . . . HMGN3 0.175434355125753 0.7683173707938 0.0562482740804472 high mobility group nucleosomal binding domain 3 FUNCTION: Binds to nucleosomes, regulating chromatin structure and consequently, chromatin-dependent processes such as transcription, DNA replication and DNA repair. Affects both insulin and glucagon levels and modulates the expression of pancreatic genes involved in insulin secretion. Regulates the expression of the glucose transporter SLC2A2 by binding specifically to its promoter region and recruiting PDX1 and additional transcription factors. Regulates the expression of SLC6A9, a glycine transporter which regulates the glycine concentration in synaptic junctions in the central nervous system, by binding to its transcription start site. May play a role in ocular development and astrocyte function (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in kidney, lung, pancreas, testis, skeletal muscle, heart, thyroid gland, pituitary gland, prostate and uterus. Low expression in liver, spleen, placenta and ovaries. {ECO:0000269|PubMed:11356838, ECO:0000269|PubMed:7776974}.; lymphoreticular;smooth muscle;ovary;umbilical cord;substantia nigra;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; . 0.35023 0.16306 0.079165051 59.43029016 12.67719 0.46256 HMGN3-AS1 . . . HMGN3 antisense RNA 1 . . . . . . . . . . . HMGN3P1 . . . high mobility group nucleosomal binding domain 3 pseudogene 1 . . . . . . . . . . . HMGN4 0.557082341510099 0.392118331592725 0.0507993268971755 high mobility group nucleosomal binding domain 4 . . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;thyroid;ciliary ganglion;kidney;pons;trigeminal ganglion;whole blood; 0.14168 0.17050 0.3032669 72.009908 122.53964 2.41061 HMGN5 0.326715650017622 0.608725505677787 0.0645588443045913 high mobility group nucleosome binding domain 5 FUNCTION: Preferentially binds to euchromatin and modulates cellular transcription by counteracting linker histone-mediated chromatin compaction. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11161810}.; unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;bone marrow;lung;frontal lobe;cochlea;cornea;adrenal gland;thyroid;visual apparatus;liver;testis;cervix;kidney;brain;mammary gland; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;skeletal muscle; 0.45306 0.08754 0.880130671 88.9596603 127.24661 2.46080 HMGXB3 . . . HMG-box containing 3 . . . . . . 0.08438 1.666397606 96.29039868 1157.42277 6.47773 HMGXB4 0.218813415259936 0.780833648439574 0.000352936300489587 HMG-box containing 4 FUNCTION: Negatively regulates Wnt/beta-catenin signaling during development. {ECO:0000250}.; . . colon;skin;uterus;prostate;whole body;cochlea;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;pharynx;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;alveolus;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;skeletal muscle; 0.88512 0.11014 -0.492218069 22.35786742 1952.80292 8.13335 HMHA1 0.453633762319863 0.546364111936219 2.12574391850203e-06 histocompatibility (minor) HA-1 FUNCTION: GTPase activator for the Rho-type GTPases. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed on cells of the hematopoietic lineage. Detected in dendritic cells and epidermal Langerhans cells. Expressed in peripheral blood mononuclear cells, in all leukemia/lymphoma cell lines. Detected also in some solid tumors and tissues such as cancerous and non-cancerous tissue. {ECO:0000269|PubMed:11965046, ECO:0000269|PubMed:8843592}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;urinary;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;kidney;stomach; lymph node;tumor;white blood cells;whole blood;tonsil;bone marrow;thymus; 0.39366 0.12838 0.010992521 54.17551309 1699.51637 7.60229 HMHB1 . . . histocompatibility (minor) HB-1 FUNCTION: Precursor of the histocomplatibility antigen HB-1. More generally, minor histocomplatibility antigens (mHags) refer to immunogenic peptide which, when complexed with MHC, can generate an immune response after recognition by specific T-cells. The peptides are derived from polymorphic intracellular proteins, which are cleaved by normal pathways of antigen processing. The binding of these peptides to MHC class I or class II molecules and its expression on the cell surface can stimulate T-cell responses and thereby trigger graft rejection or graft-versus-host disease (GVHD) after hematopoietic stem cell transplantation from HLA- identical sibling donor. GVHD is a frequent complication after bone marrow transplantation (BMT), due to mismatch of minor histocomplatibility antigen in HLA-matched sibling marrow transplants. HB-1 is presented on the cell surface by MHC class I HLA-B44. This complex specifically elicits donor-cytotoxic T lymphocyte (CTL) reactivity in B-cell acute lymphoblastic leukemia (B-ALL) after treatment by HLA-identical allogenic bone marrow transplantation (BMT). It induces cell recognition and lysis by CTL. However, HB-1 restricted expression in B-ALL cells and not in normal tissues may allow a specific CTL reactivity against B-ALL without the risk of evoking graft-versus-host disease. {ECO:0000269|PubMed:15102363, ECO:0000269|PubMed:8992968, ECO:0000269|PubMed:9892612}.; . TISSUE SPECIFICITY: Expressed in acute lymphoblastic leukemia B- cells and Epstein-Barr virus-transformed B-cells. {ECO:0000269|PubMed:8992968, ECO:0000269|PubMed:9892612}.; unclassifiable (Anatomical System); superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04294 . 0.191216164 66.57230479 687.96623 5.23427 HMMR 1.03956948492903e-14 0.0717291022111027 0.928270897788887 hyaluronan mediated motility receptor FUNCTION: Involved in cell motility. When hyaluronan binds to HMMR, the phosphorylation of a number of proteins, including PTK2/FAK1 occurs. May also be involved in cellular transformation and metastasis formation, and in regulating extracellular- regulated kinase (ERK) activity.; . TISSUE SPECIFICITY: Expressed in breast cancer cell lines and in normal breast tissue.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;lens;breast;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;fetal liver;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;tumor;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.40906 0.27584 2.289361599 98.30738382 2640.61112 9.64170 HMMR-AS1 . . . HMMR antisense RNA 1 . . . . . . . . . . . HMOX1 0.000641360507953024 0.733533292216658 0.265825347275389 heme oxygenase 1 FUNCTION: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.; DISEASE: Heme oxygenase 1 deficiency (HMOX1D) [MIM:614034]: A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly. {ECO:0000269|PubMed:9884342}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at higher levels in renal cancer tissue than in normal tissue (at protein level). {ECO:0000269|PubMed:20855888}.; myocardium;medulla oblongata;ovary;salivary gland;intestine;colon;choroid;vein;skin;bone marrow;uterus;prostate;bone;iris;testis;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;heart;ciliary ganglion;trigeminal ganglion; 0.11014 0.86226 -0.602450568 17.91106393 251.56278 3.41691 HMOX2 0.0011006560316462 0.832356719768214 0.16654262420014 heme oxygenase 2 FUNCTION: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.; . . lymphoreticular;myocardium;ovary;salivary gland;intestine;colon;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; testis - interstitial;thalamus;testis - seminiferous tubule;testis;trigeminal ganglion;parietal lobe; 0.09048 0.62605 -0.756778259 13.44656759 29.62046 0.94596 HMSD 0.0023239519442082 0.531416738489302 0.46625930956649 histocompatibility (minor) serpin domain containing FUNCTION: Putative serine protease inhibitor. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in dendritic cells and primary leukemia cells, especially those of myeloid lineage. {ECO:0000269|PubMed:17409267}.; . . . . -0.075159878 47.78839349 31.77068 1.00013 HMX1 0.125284952216653 0.613819869583131 0.260895178200217 H6 family homeobox 1 FUNCTION: DNA-binding protein that binds to the 5'-CAAG-3' core sequence. May function as a transcriptional repressor. Seems to act as a transcriptional antagonist of NKX2-5. May play an important role in the development of craniofacial structures such as the eye and ear. {ECO:0000269|PubMed:10206974}.; DISEASE: Oculoauricular syndrome (OCACS) [MIM:612109]: A syndrome characterized by microphthalmia, microcornea, anterior segment dysgenesis, cataract, ocular coloboma, retinal pigment epithelium abnormalities, rod-cone dystrophy, and anomalies of the external ear. {ECO:0000269|PubMed:18423520}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.09566 . . . 870.80003 5.74653 HMX2 0.000305119293834059 0.353730675466876 0.64596420523929 H6 family homeobox 2 FUNCTION: Transcription factor involved in specification of neuronal cell types and which is required for inner ear and hypothalamus development. {ECO:0000250}.; . . lung;brain;retina; . 0.70789 0.10801 0.170987912 65.5579146 136.82403 2.54217 HMX3 0.772661528331209 0.219601476940973 0.00773699472781845 H6 family homeobox 3 FUNCTION: Transcription factor involved in specification of neuronal cell types and which is required for inner ear and hypothalamus development. Binds to the 5'-CAAGTG-3' core sequence. Controls semicircular canal formation in the inner ear. Also required for hypothalamic/pituitary axis of the CNS (By similarity). {ECO:0000250}.; . . . . 0.32793 0.13428 . . 185.69332 2.95865 HN1 0.0193134506649175 0.736615830728663 0.24407071860642 hematological and neurological expressed 1 . . TISSUE SPECIFICITY: Expressed in testis, skeletal muscle, thymus, prostate, colon, peripheral blood cells, brain and placenta. {ECO:0000269|PubMed:15094197}.; ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;uterus;prostate;whole body;ganglion;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;skeletal muscle;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;duodenum;liver;head and neck;kidney;mammary gland;stomach;aorta; amygdala;whole brain;superior cervical ganglion;testis - interstitial;lung;testis - seminiferous tubule;fetal brain;cerebellum peduncles;testis;tumor;whole blood;cerebellum; 0.39762 0.11394 0.525552348 80.57914603 52.6163 1.43679 HN1L 0.516099964468604 0.466397124511726 0.0175029110196694 hematological and neurological expressed 1-like . . TISSUE SPECIFICITY: Expressed in liver, kidney, prostate, testis and uterus. {ECO:0000269|PubMed:15094197}.; lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;gum;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; prostate;fetal liver;superior cervical ganglion;trachea;hypothalamus;placenta;spinal cord;tumor;ciliary ganglion;atrioventricular node; 0.26768 0.10014 0.080983847 59.76055674 8.76946 0.32280 HNB1 . . . hereditary neuroblastoma 1 . . . . . . . . . . . HNF1A 0.969659467322862 0.0303386910270896 1.84165004877094e-06 HNF1 homeobox A FUNCTION: Transcriptional activator that regulates the tissue specific expression of multiple genes, especially in pancreatic islet cells and in liver. Required for the expression of several liver specific genes. Binds to the inverted palindrome 5'- GTTAATNATTAAC-3'. {ECO:0000269|PubMed:10966642, ECO:0000269|PubMed:12453420}.; DISEASE: Hepatic adenomas familial (HEPAF) [MIM:142330]: Rare benign liver tumors of presumable epithelial origin that develop in an otherwise normal liver. Hepatic adenomas may be single or multiple. They consist of sheets of well-differentiated hepatocytes that contain fat and glycogen and can produce bile. Bile ducts or portal areas are absent. Kupffer cells, if present, are reduced in number and are non-functional. Conditions associated with adenomas are insulin-dependent diabetes mellitus and glycogen storage diseases (types 1 and 3). Note=The disease is caused by mutations affecting the gene represented in this entry. Bi-allelic inactivation of HNF1A, whether sporadic or associated with MODY3, may be an early step in the development of some hepatocellular carcinomas.; DISEASE: Maturity-onset diabetes of the young 3 (MODY3) [MIM:600496]: A form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease. {ECO:0000269|PubMed:10078571, ECO:0000269|PubMed:10102714, ECO:0000269|PubMed:10482964, ECO:0000269|PubMed:10588527, ECO:0000269|PubMed:8945470, ECO:0000269|PubMed:9032114, ECO:0000269|PubMed:9075818, ECO:0000269|PubMed:9075819, ECO:0000269|PubMed:9097962, ECO:0000269|PubMed:9166684, ECO:0000269|PubMed:9287053, ECO:0000269|PubMed:9392505, ECO:0000269|PubMed:9626139, ECO:0000269|PubMed:9754819}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, insulin-dependent, 20 (IDDM20) [MIM:612520]: A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:10333057, ECO:0000269|PubMed:9313763, ECO:0000269|PubMed:9867222}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver.; unclassifiable (Anatomical System);colon;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;macula lutea;visual apparatus;liver;testis;kidney;pineal gland;brain;stomach; superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.86603 . -0.440847477 24.59896202 5494.65453 15.28646 HNF1A-AS1 . . . HNF1A antisense RNA 1 . . . . . . . . . . . HNF1B 0.999286182382324 0.000713812964779848 4.65289568727915e-09 HNF1 homeobox B FUNCTION: Transcription factor, probably binds to the inverted palindrome 5'-GTTAATNATTAAC-3'.; DISEASE: Renal cysts and diabetes syndrome (RCAD) [MIM:137920]: An autosomal dominant disorder comprising non-diabetic renal disease resulting from abnormal renal development, and diabetes, which in some cases occurs earlier than age 25 years and is thus consistent with a diagnosis of maturity-onset diabetes of the young (MODY5). The renal disease is highly variable and includes renal cysts, glomerular tufts, aberrant nephrogenesis, primitive tubules, irregular collecting systems, oligomeganephronia, enlarged renal pelves, abnormal calyces, small kidney, single kidney, horseshoe kidney, and hyperuricemic nephropathy. Affected individuals may also have abnormalities of the genital tract. {ECO:0000269|PubMed:10484768, ECO:0000269|PubMed:10672455, ECO:0000269|PubMed:11845238, ECO:0000269|PubMed:11918730, ECO:0000269|PubMed:14583183, ECO:0000269|PubMed:15001636, ECO:0000269|PubMed:15068978, ECO:0000269|PubMed:15181075, ECO:0000269|PubMed:15930087, ECO:0000269|PubMed:16249435}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:12161522}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; DISEASE: Prostate cancer, hereditary, 11 (HPC11) [MIM:611955]: A condition associated with familial predisposition to cancer of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma. {ECO:0000269|PubMed:18264097}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;pancreas;prostate;lung;frontal lobe;endometrium;placenta;liver;testis;spleen;kidney;brain;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;atrioventricular node;kidney;skeletal muscle;cingulate cortex; 0.39307 0.70810 -0.538132194 20.26421326 88.79768 2.02232 HNF4A 0.919225678145736 0.0807527378416198 2.15840126440406e-05 hepatocyte nuclear factor 4 alpha FUNCTION: Transcriptionally controlled transcription factor. Binds to DNA sites required for the transcription of alpha 1- antitrypsin, apolipoprotein CIII, transthyretin genes and HNF1- alpha. May be essential for development of the liver, kidney and intestine.; DISEASE: Maturity-onset diabetes of the young 1 (MODY1) [MIM:125850]: A form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease. {ECO:0000269|PubMed:17407387, ECO:0000269|PubMed:9243109, ECO:0000269|PubMed:9313765}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:9449683}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; DISEASE: Fanconi renotubular syndrome 4 with maturity-onset diabetes of the young (FRTS4) [MIM:616026]: A disease characterized by Fanconi syndrome associated with a beta cell phenotype of neonatal hyperinsulinism with macrosomia and young onset diabetes. Fanconi syndrome is a proximal tubulopathy resulting in generalised aminoaciduria, low molecular weight proteinuria, glycosuria, hyperphosphaturia and hypouricemia. Some FRTS4 patients have nephrocalcinosis, renal impairment, hypercalciuria with relative hypocalcemia, and hypermagnesemia. {ECO:0000269|PubMed:22802087, ECO:0000269|PubMed:24285859}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);liver;colon;spleen;kidney;stomach; superior cervical ganglion;liver;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;fetal thyroid;cingulate cortex;skeletal muscle;parietal lobe; 0.94499 0.93785 -0.955204708 9.170794999 238.98386 3.33861 HNF4A-AS1 . . . HNF4A antisense RNA 1 . . . . . . . . . . . HNF4G 0.544634189825221 0.454742126117176 0.000623684057602613 hepatocyte nuclear factor 4 gamma FUNCTION: Transcription factor. Has a lower transcription activation potential than HNF4-alpha.; . TISSUE SPECIFICITY: Expressed in pancreas, kidney, small intestine and testis. Weakly expressed in colon. Not expressed in liver, skeletal muscle, lung, placenta, brain, heart, peripheral blood, ovary, prostate, thymus and spleen.; liver;brain;stomach; superior cervical ganglion;atrioventricular node; 0.61144 0.22824 -0.025608647 51.91672564 31.63046 0.99538 HNF4GP1 . . . hepatocyte nuclear factor 4 gamma pseudogene 1 . . . . . . . . . . . HNMT 0.0967293826850996 0.867323342130545 0.0359472751843555 histamine N-methyltransferase FUNCTION: Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;bone;thyroid;testis;dura mater;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;spinal cord;adrenal cortex;pharynx;blood;breast;pia mater;lung;cornea;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;aorta;stomach; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09265 0.23774 -0.293801652 32.93819297 615.50798 5.00969 HNRNPA0 0.863701458346368 0.134307942659843 0.00199059899378935 heterogeneous nuclear ribonucleoprotein A0 FUNCTION: mRNA-binding component of ribonucleosomes. Specifically binds AU-rich element (ARE)-containing mRNAs. Involved in post- transcriptional regulation of cytokines mRNAs. {ECO:0000269|PubMed:12456657}.; . . ovary;colon;skin;retina;uterus;whole body;cerebral cortex;thyroid;bone;testis;spinal ganglion;ciliary body;brain;gall bladder;tonsil;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;islets of Langerhans;muscle;pancreas;lung;placenta;visual apparatus;spleen;kidney;mammary gland;stomach; superior cervical ganglion;fetal brain;cerebellum peduncles;placenta;globus pallidus;testis;cerebellum; 0.16379 0.31462 0.103030231 61.2762444 50.4127 1.39618 HNRNPA1 0.966614388412206 0.0333740783633851 1.15332244085573e-05 heterogeneous nuclear ribonucleoprotein A1 FUNCTION: Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. May play a role in HCV RNA replication. {ECO:0000269|PubMed:17229681}.; DISEASE: Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 3 (IBMPFD3) [MIM:615424]: An autosomal dominant disease characterized by disabling muscle weakness clinically resembling to limb girdle muscular dystrophy, osteolytic bone lesions consistent with Paget disease, and premature frontotemporal dementia. Clinical features show incomplete penetrance. {ECO:0000269|PubMed:23455423}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Amyotrophic lateral sclerosis 20 (ALS20) [MIM:615426]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. {ECO:0000269|PubMed:23455423}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;spinal cord;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; fetal brain;hypothalamus;tumor;white blood cells; 0.80629 . -0.185391282 39.67916962 44.85595 1.28432 HNRNPA1L2 6.70372795331927e-05 0.290017031748343 0.709915930972124 heterogeneous nuclear ribonucleoprotein A1-like 2 FUNCTION: Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. {ECO:0000250}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;muscle;pharynx;blood;breast;bile duct;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;head and neck;kidney;mammary gland;stomach; ciliary ganglion;atrioventricular node;trigeminal ganglion; . 0.07305 1.306318795 93.99622552 1629.3303 7.46389 HNRNPA1P1 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 1 . . . . . . . . . . . HNRNPA1P2 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 2 . . . . . . . . . . . HNRNPA1P3 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 3 . . . . . . . . . . . HNRNPA1P4 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 4 . . . . . . 0.08180 . . . . HNRNPA1P5 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 5 . . . . . . . . . . . HNRNPA1P6 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 6 . . . . . . . . . . . HNRNPA1P7 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 7 . . . . . . . . . . . HNRNPA1P8 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 8 . . . . . . . . . . . HNRNPA1P9 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 9 . . . . . . . . . . . HNRNPA1P10 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 10 . . . . . . . . . . . HNRNPA1P11 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 11 . . . . . . . . . . . HNRNPA1P12 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 12 . . . . . . . . . . . HNRNPA1P13 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 13 . . . . . . . . . . . HNRNPA1P14 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 14 . . . . . . . . . . . HNRNPA1P15 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 15 . . . . . . . . . . . HNRNPA1P16 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 16 . . . . . . . . . . . HNRNPA1P17 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 17 . . . . . . . . . . . HNRNPA1P18 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 18 . . . . . . . . . . . HNRNPA1P19 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 19 . . . . . . . . . . . HNRNPA1P20 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 20 . . . . . . . . . . . HNRNPA1P21 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 21 . . . . . . . . . . . HNRNPA1P22 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 22 . . . . . . . . . . . HNRNPA1P23 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 23 . . . . . . . . . . . HNRNPA1P24 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 24 . . . . . . . . . . . HNRNPA1P25 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 25 . . . . . . . . . . . HNRNPA1P26 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 26 . . . . . . . . . . . HNRNPA1P27 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 27 . . . . . . . . . . . HNRNPA1P28 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 28 . . . . . . . . . . . HNRNPA1P29 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 29 . . . . . . . . . . . HNRNPA1P30 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 30 . . . . . . . . . . . HNRNPA1P31 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 31 . . . . . . . . . . . HNRNPA1P32 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 32 . . . . . . . . . . . HNRNPA1P33 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 33 . . . . . . . . . . . HNRNPA1P34 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 34 . . . . . . . . . . . HNRNPA1P35 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 35 . . . . . . . . . . . HNRNPA1P36 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 36 . . . . . . . . . . . HNRNPA1P37 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 37 . . . . . . . . . . . HNRNPA1P38 . . . heterogeneous nuclear ribonucleoprotein A1pseudogene 38 . . . . . . . . . . . HNRNPA1P39 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 39 . . . . . . . . . . . HNRNPA1P40 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 40 . . . . . . . . . . . HNRNPA1P41 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 41 . . . . . . . . . . . HNRNPA1P42 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 42 . . . . . . . . . . . HNRNPA1P43 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 43 . . . . . . . . . . . HNRNPA1P44 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 44 . . . . . . . . . . . HNRNPA1P45 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 45 . . . . . . . . . . . HNRNPA1P46 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 46 . . . . . . . . . . . HNRNPA1P47 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 47 . . . . . . . . . . . HNRNPA1P48 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 48 . . . . . . . . . . . HNRNPA1P49 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 49 . . . . . . . . . . . HNRNPA1P50 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 50 . . . . . . . . . . . HNRNPA1P51 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 51 . . . . . . . . . . . HNRNPA1P52 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 52 . . . . . . . . . . . HNRNPA1P53 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 53 . . . . . . . . . . . HNRNPA1P54 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 54 . . . . . . . . . . . HNRNPA1P55 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 55 . . . . . . . . . . . HNRNPA1P56 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 56 . . . . . . . . . . . HNRNPA1P57 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 57 . . . . . . . . . . . HNRNPA1P58 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 58 . . . . . . . . . . . HNRNPA1P59 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 59 . . . . . . . . . . . HNRNPA1P60 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 60 . . . . . . . . . . . HNRNPA1P61 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 61 . . . . . . . . . . . HNRNPA1P62 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 62 . . . . . . . . . . . HNRNPA1P63 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 63 . . . . . . . . . . . HNRNPA1P64 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 64 . . . . . . . . . . . HNRNPA1P65 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 65 . . . . . . . . . . . HNRNPA1P66 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 66 . . . . . . . . . . . HNRNPA1P67 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 67 . . . . . . . . . . . HNRNPA1P68 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 68 . . . . . . . . . . . HNRNPA1P69 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 69 . . . . . . . . . . . HNRNPA1P70 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 70 . . . . . . . . . . . HNRNPA1P71 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 71 . . . . . . . . . . . HNRNPA1P72 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 72 . . . . . . . . . . . HNRNPA1P73 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 73 . . . . . . . . . . . HNRNPA1P74 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 74 . . . . . . . . . . . HNRNPA1P75 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 75 . . . . . . . . . . . HNRNPA1P76 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 76 . . . . . . . . . . . HNRNPA1P77 . . . heterogeneous nuclear ribonucleoprotein A1 pseudogene 77 . . . . . . . . . . . HNRNPA2B1 0.970043353092889 0.0299478333388736 8.81356823720325e-06 heterogeneous nuclear ribonucleoprotein A2/B1 FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non- random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs (PubMed:19099192). Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (PubMed:10567417). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri- miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts (PubMed:26321680). Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs (PubMed:24356509). Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A- containing pre-mRNAs (PubMed:26321680). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000269|PubMed:10567417, ECO:0000269|PubMed:24356509, ECO:0000269|PubMed:26321680, ECO:0000303|PubMed:19099192}.; DISEASE: Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 2 (IBMPFD2) [MIM:615422]: An autosomal dominant disease characterized by disabling muscle weakness clinically resembling to limb girdle muscular dystrophy, osteolytic bone lesions consistent with Paget disease, and premature frontotemporal dementia. Clinical features show incomplete penetrance. {ECO:0000269|PubMed:23455423}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;smooth muscle;ovary;umbilical cord;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;alveolus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; testis - interstitial;testis - seminiferous tubule;testis; 0.79465 0.22978 -0.229483771 36.86010852 7.18025 0.27003 HNRNPA3 0.992644939735303 0.00735368247711416 1.37778758315287e-06 heterogeneous nuclear ribonucleoprotein A3 FUNCTION: Plays a role in cytoplasmic trafficking of RNA. Binds to the cis-acting response element, A2RE. May be involved in pre-mRNA splicing. {ECO:0000269|PubMed:11886857}.; . . . . 0.36128 0.09250 -0.273576253 33.97027601 10.21749 0.37260 HNRNPA3P1 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 1 . . . . . . . . . . . HNRNPA3P2 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 2 . . . . . . . . . . . HNRNPA3P3 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 3 . . . . . . . . . . . HNRNPA3P4 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 4 . . . . . . . . . . . HNRNPA3P5 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 5 . . . . . . . . . . . HNRNPA3P6 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 6 . . . . . . . . . . . HNRNPA3P7 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 7 . . . . . . . . . . . HNRNPA3P8 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 8 . . . . . . . . . . . HNRNPA3P9 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 9 . . . . . . . . . . . HNRNPA3P10 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 10 . . . . . . . . . . . HNRNPA3P11 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 11 . . . . . . . . . . . HNRNPA3P12 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 12 . . . . . . . . . . . HNRNPA3P13 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 13 . . . . . . . . . . . HNRNPA3P14 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 14 . . . . . . . . . . . HNRNPA3P15 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 15 . . . . . . . . . . . HNRNPA3P16 . . . heterogeneous nuclear ribonucleoprotein A3 pseudogene 16 . . . . . . . . . . . HNRNPAB 0.960162611643984 0.0398194855272338 1.79028287817438e-05 heterogeneous nuclear ribonucleoprotein A/B FUNCTION: Binds single-stranded RNA. Has a high affinity for G- rich and U-rich regions of hnRNA. Also binds to APOB mRNA transcripts around the RNA editing site.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;subthalamic nucleus;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; lung;adrenal gland;tumor;bone marrow; 0.41717 0.13056 -0.383807564 27.41802312 22.99318 0.76692 HNRNPABP1 . . . heterogeneous nuclear ribonucleoprotein A/B pseudogene 1 . . . . . . . . . . . HNRNPC 0.985848437293407 0.0141447163493978 6.84635719567576e-06 heterogeneous nuclear ribonucleoprotein C (C1/C2) FUNCTION: Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). Specifically recognizes and binds N6- methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs that affects mRNA splicing, processing and stability. M6A alters the local structure in mRNAs and long non- coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch' to facilitate binding of HNRNPC, leading to regulation of mRNA splicing (PubMed:25719671). Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre- mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'- UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules (PubMed:12509468, PubMed:16010978, PubMed:7567451, PubMed:8264621). {ECO:0000269|PubMed:12509468, ECO:0000269|PubMed:16010978, ECO:0000269|PubMed:25719671, ECO:0000269|PubMed:7567451, ECO:0000269|PubMed:8264621}.; . . ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;oral cavity;muscle;pancreas;lung;adrenal gland;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus; . 0.16171 0.28104 -0.075159878 47.78839349 6.88559 0.25634 HNRNPCL1 0.0107232661654143 0.833814449680548 0.155462284154037 heterogeneous nuclear ribonucleoprotein C-like 1 FUNCTION: May play a role in nucleosome assembly by neutralizing basic proteins such as A and B core hnRNPs. {ECO:0000250}.; . . . . 0.25159 . 1.194256079 92.88747346 2213.53889 8.66280 HNRNPCL2 . . . heterogeneous nuclear ribonucleoprotein C-like 2 FUNCTION: May play a role in nucleosome assembly by neutralizing basic proteins such as A and B core hnRNPs. {ECO:0000250}.; . . . . . . . . . . HNRNPCL3 . . . heterogeneous nuclear ribonucleoprotein C-like 3 . . . . . . . . . . . HNRNPCL4 . . . heterogeneous nuclear ribonucleoprotein C-like 4 . . . . . . . . . . . HNRNPCP1 . . . heterogeneous nuclear ribonucleoprotein C pseudogene 1 . . . . . . . . . . . HNRNPCP2 . . . heterogeneous nuclear ribonucleoprotein C pseudogene 2 . . . . . . . . . . . HNRNPCP3 . . . heterogeneous nuclear ribonucleoprotein C pseudogene 3 . . . . . . . . . . . HNRNPCP4 . . . heterogeneous nuclear ribonucleoprotein C pseudogene 4 . . . . . . . . . . . HNRNPCP6 . . . heterogeneous nuclear ribonucleoprotein C pseudogene 6 . . . . . . . . . . . HNRNPCP7 . . . heterogeneous nuclear ribonucleoprotein C pseudogene 7 . . . . . . . . . . . HNRNPCP8 . . . heterogeneous nuclear ribonucleoprotein C pseudogene 8 . . . . . . . . . . . HNRNPCP9 . . . heterogeneous nuclear ribonucleoprotein C pseudogene 9 . . . . . . . . . . . HNRNPCP10 . . . heterogeneous nuclear ribonucleoprotein C pseudogene 10 . . . . . . . . . . . HNRNPD 0.957344185404364 0.0426345813231368 2.12332724989423e-05 heterogeneous nuclear ribonucleoprotein D FUNCTION: Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto- oncogenes and cytokine mRNAs. Also binds to double- and single- stranded DNA sequences in a specific manner and functions a transcription factor. Each of the RNA-binding domains specifically can bind solely to a single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'- TTAGGG-3' repeats. Binding of RRM1 to DNA inhibits the formation of DNA quadruplex structure which may play a role in telomere elongation. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. May play a role in the regulation of the rhythmic expression of circadian clock core genes. Directly binds to the 3'UTR of CRY1 mRNA and induces CRY1 rhythmic translation. May also be involved in the regulation of PER2 translation. {ECO:0000269|PubMed:10080887, ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:24423872}.; . . smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;duodenum;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;salivary gland;globus pallidus;white blood cells;ciliary ganglion;skin; 0.21152 0.42641 -0.009020804 52.8544468 2.46627 0.09065 HNRNPDL 0.916051062720941 0.0839251112174094 2.38260616495801e-05 heterogeneous nuclear ribonucleoprotein D like FUNCTION: Acts as a transcriptional regulator. Promotes transcription repression. Promotes transcription activation in differentiated myotubes (By similarity). Binds to double- and single-stranded DNA sequences. Binds to the transcription suppressor CATR sequence of the COX5B promoter (By similarity). Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Binds both to nuclear and cytoplasmic poly(A) mRNAs. Binds to poly(G) and poly(A), but not to poly(U) or poly(C) RNA homopolymers. Binds to the 5'-ACUAGC-3' RNA consensus sequence. {ECO:0000250, ECO:0000269|PubMed:9538234}.; DISEASE: Limb-girdle muscular dystrophy 1G (LGMD1G) [MIM:609115]: An autosomal dominant degenerative myopathy characterized by slowly progressive wasting and weakness of the proximal muscles of arms and legs around the pelvic or shoulder girdles, elevated creatine kinase levels and dystrophic features on muscle biopsy. LGMD1G is characterized by a mild late-onset and is associated with progressive fingers and toes flexion limitation. Affected individuals may also develop cataracts before age 50. {ECO:0000269|PubMed:24647604}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocytes. Expressed in myeloid leukemia, gastric adenocarcinoma, cervical carcinoma, hepatoma, fibrosarcoma, colon adenocarcinoma, epidermoid carcinoma, osteosarcoma and urinary bladder carcinoma cells. {ECO:0000269|PubMed:10072754, ECO:0000269|PubMed:9538234}.; . . 0.36874 0.13169 -0.249709319 35.74545883 143.6778 2.61332 HNRNPDLP1 . . . heterogeneous nuclear ribonucleoprotein D-like pseudogene 1 . . . . . . . . . . . HNRNPDLP2 . . . heterogeneous nuclear ribonucleoprotein D-like pseudogene 2 . . . . . . . . . . . HNRNPDLP3 . . . heterogeneous nuclear ribonucleoprotein D-like pseudogene 3 . . . . . . . . . . . HNRNPDLP4 . . . heterogeneous nuclear ribonucleoprotein D-like pseudogene 4 . . . . . . . . . . . HNRNPDLP5 . . . heterogeneous nuclear ribonucleoprotein D-like pseudogene 5 . . . . . . . . . . . HNRNPDP1 . . . heterogeneous nuclear ribonucleoprotein D pseudogene 1 . . . . . . . . . . . HNRNPDP2 . . . heterogeneous nuclear ribonucleoprotein D pseudogene 2 . . . . . . . . . . . HNRNPF 0.864039577145677 0.133982658572984 0.00197776428133983 heterogeneous nuclear ribonucleoprotein F FUNCTION: Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Plays a role in the regulation of alternative splicing events. Binds G-rich sequences in pre-mRNAs and keeps target RNA in an unfolded state. {ECO:0000269|PubMed:20526337}.; . TISSUE SPECIFICITY: Expressed ubiquitously.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;duodenum;head and neck;kidney;aorta;stomach;thymus; testis - interstitial;superior cervical ganglion;testis;tumor;appendix;trigeminal ganglion;skeletal muscle; 0.13118 0.47945 -0.602450568 17.91106393 33.80359 1.04086 HNRNPFP1 . . . heterogeneous nuclear ribonucleoprotein F pseudogene 1 . . . . . . . . . . . HNRNPH1 0.99914829403982 0.000851698804657036 7.15552253773744e-09 heterogeneous nuclear ribonucleoprotein H1 (H) FUNCTION: This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Mediates pre-mRNA alternative splicing regulation. Inhibits, together with CUGBP1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Binds to the IR RNA. Binds poly(RG). {ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:16946708}.; . TISSUE SPECIFICITY: Expressed ubiquitously.; lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;thymus; amygdala;thyroid;testis;atrioventricular node; 0.83563 . -0.273576253 33.97027601 18.26126 0.63463 HNRNPH1P1 . . . heterogeneous nuclear ribonucleoprotein H1 pseudogene 1 . . . . . . . . . . . HNRNPH1P2 . . . heterogeneous nuclear ribonucleoprotein H1 pseudogene 2 . . . . . . . . . . . HNRNPH1P3 . . . heterogeneous nuclear ribonucleoprotein H1 pseudogene 3 . . . . . . . . . . . HNRNPH2 0.868284240433363 0.129894638412921 0.00182112115371607 heterogeneous nuclear ribonucleoprotein H2 (H') FUNCTION: This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Binds poly(RG).; . TISSUE SPECIFICITY: Expressed ubiquitously.; . . 0.91289 0.22085 -0.141298762 42.87567823 4.99946 0.18578 HNRNPH3 0.996456324079282 0.00354362908381022 4.6836908053289e-08 heterogeneous nuclear ribonucleoprotein H3 FUNCTION: Involved in the splicing process and participates in early heat shock-induced splicing arrest. Due to their great structural variations the different isoforms may possess different functions in the splicing reaction.; . . smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;heart;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;head and neck;kidney;stomach; thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;white blood cells;atrioventricular node;pons;caudate nucleus;skeletal muscle;fetal brain;testis - seminiferous tubule;prefrontal cortex;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.29214 0.11262 0.03689118 56.64071715 255.83946 3.44038 HNRNPH3P1 . . . heterogeneous nuclear ribonucleoprotein H3 pseudogene 1 . . . . . . . . . . . HNRNPK 0.999782388949029 0.000217610793480853 2.57489718500518e-10 heterogeneous nuclear ribonucleoprotein K FUNCTION: One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single- stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction (By similarity). As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest. {ECO:0000250, ECO:0000269|PubMed:16360036, ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:22825850}.; . . lymphoreticular;myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus; . 0.88640 0.67288 -0.207437529 38.2814343 5.95251 0.22372 HNRNPKP1 . . . heterogeneous nuclear ribonucleoprotein K pseudogene 1 . . . . . . . . . . . HNRNPKP2 . . . heterogeneous nuclear ribonucleoprotein K pseudogene 2 . . . . . . . . . . . HNRNPKP3 . . . heterogeneous nuclear ribonucleoprotein K pseudogene 3 . . . . . . . . . . . HNRNPKP4 . . . heterogeneous nuclear ribonucleoprotein K pseudogene 4 . . . . . . . . . . . HNRNPKP5 . . . heterogeneous nuclear ribonucleoprotein K pseudogene 5 . . . . . . . . . . . HNRNPL 0.945068590001273 0.0549232988233087 8.11117541791397e-06 heterogeneous nuclear ribonucleoprotein L FUNCTION: Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter. {ECO:0000269|PubMed:11809897}.; . . ovary;salivary gland;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;oesophagus;bone;thyroid;iris;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;pharynx;blood;breast;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;amnion;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;adrenal cortex;testis;kidney;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle;cerebellum; 0.89270 . -0.626318434 17.03231894 12.63054 0.46083 HNRNPLL 0.00539438758557714 0.993534538129982 0.00107107428444049 heterogeneous nuclear ribonucleoprotein L like FUNCTION: RNA-binding protein that functions as regulator of alternative splicing for multiple target mRNAs, including PTPRC/CD45 and STAT5A. Required for alternative splicing of PTPRC. {ECO:0000269|PubMed:18669861}.; . TISSUE SPECIFICITY: Widely expressed. Detected in bone marrow stroma cells, skeletal muscle, heart, placenta, pancreas, kidney and lung. {ECO:0000269|PubMed:15256261}.; . . 0.57310 0.10892 -0.337894035 30.37272942 190.96145 2.99700 HNRNPLP1 . . . heterogeneous nuclear ribonucleoprotein L pseudogene 1 . . . . . . . . . . . HNRNPLP2 . . . heterogeneous nuclear ribonucleoprotein L pseudogene 2 . . . . . . . . . . . HNRNPM 0.999948048705257 5.19512868843426e-05 7.85897863036523e-12 heterogeneous nuclear ribonucleoprotein M FUNCTION: Pre-mRNA binding protein in vivo, binds avidly to poly(G) and poly(U) RNA homopolymers in vitro. Involved in splicing. Acts as a receptor for carcinoembryonic antigen in Kupffer cells, may initiate a series of signaling events leading to tyrosine phosphorylation of proteins and induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines.; . . ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;urinary;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;cornea;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus; white blood cells; 0.10353 0.17489 -1.39618256 4.222694032 52.82684 1.44081 HNRNPMP1 . . . heterogeneous nuclear ribonucleoprotein M pseudogene 1 . . . . . . . . . . . HNRNPMP2 . . . heterogeneous nuclear ribonucleoprotein M pseudogene 2 . . . . . . . . . . . HNRNPR 0.999079074304417 0.000920917039067008 8.65651567109856e-09 heterogeneous nuclear ribonucleoprotein R FUNCTION: Component of ribonucleosomes, which are complexes of at least 20 other different heterogenious nuclear ribonucleoproteins (hnRNP). hnRNP play an important role in processing of precursor mRNA in the nucleus.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;gall bladder;heart;cartilage;tongue;urinary;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;placenta;head and neck;kidney;aorta;stomach;thymus; amygdala; 0.99138 0.27614 -0.449946534 24.00330267 21.63195 0.72789 HNRNPRP1 . . . heterogeneous nuclear ribonucleoprotein R pseudogene 1 . . . . . . . . . . . HNRNPRP2 . . . heterogeneous nuclear ribonucleoprotein R pseudogene 2 . . . . . . . . . . . HNRNPRP3 . . . heterogeneous nuclear ribonucleoprotein R pseudogene 3 . . . . . . . . . . . HNRNPU 0.999903322582432 9.66774103489884e-05 7.21935279496976e-12 heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A) FUNCTION: Component of the CRD-mediated complex that promotes MYC mRNA stabilization. Binds to pre-mRNA. Has high affinity for scaffold-attached region (SAR) DNA. Binds to double- and single- stranded DNA and RNA. Plays a role in the circadian regulation of the core clock component ARNTL/BMAL1 transcription (By similarity). {ECO:0000250|UniProtKB:Q8VEK3, ECO:0000269|PubMed:19029303}.; . . ovary;sympathetic chain;rectum;skin;retina;bone marrow;prostate;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;oesophagus;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;adrenal gland;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; testis - interstitial;testis - seminiferous tubule;testis;white blood cells; 0.51398 0.38821 -0.60427181 17.74593064 41.32875 1.20799 HNRNPUL1 0.99984751233348 0.000152487665622562 8.9699469812296e-13 heterogeneous nuclear ribonucleoprotein U-like 1 FUNCTION: Acts as a basic transcriptional regulator. Represses basic transcription driven by several virus and cellular promoters. When associated with BRD7, activates transcription of glucocorticoid-responsive promoter in the absence of ligand- stimulation. Plays also a role in mRNA processing and transport. Binds avidly to poly(G) and poly(C) RNA homopolymers in vitro. {ECO:0000269|PubMed:12489984, ECO:0000269|PubMed:9733834}.; . . lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pineal body;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;hippocampus;amnion;duodenum;head and neck;kidney;stomach;aorta; superior cervical ganglion;testis - interstitial;thyroid;prefrontal cortex;testis;atrioventricular node; 0.45377 0.15922 -0.732911333 14.07761264 45.16441 1.29059 HNRNPUL2 0.999925394683505 7.46053157177133e-05 7.76981214125202e-13 heterogeneous nuclear ribonucleoprotein U-like 2 . . . colon;choroid;fovea centralis;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;thyroid;iris;testis;bladder;brain;unclassifiable (Anatomical System);blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;macula lutea;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.35408 0.13466 -0.378346116 28.01368247 161.94024 2.78066 HNRNPUL2-BSCL2 . . . HNRNPUL2-BSCL2 readthrough (NMD candidate) . . . . . . . . . . . HNRNPUP1 . . . heterogeneous nuclear ribonucleoprotein U pseudogene 1 . . . . . . . . . . . HOAC . . . hypoacusis 2 (autosomal recessive) . . . . . . . . . . . HOGA1 7.32776904772909e-06 0.490977588009671 0.509015084221281 4-hydroxy-2-oxoglutarate aldolase 1 FUNCTION: Catalyzes the final step in the metabolic pathway of hydroxyproline. {ECO:0000269|PubMed:20797690, ECO:0000269|PubMed:21998747}.; DISEASE: Hyperoxaluria primary 3 (HP3) [MIM:613616]: A disorder phenotypically similar to hyperoxaluria type 1 and type 2. It is characterized by increase in urinary oxalate excretion and mild glycolic aciduria. Clinical manifestations include calcium oxalate urolithiasis, hematuria, pain, and/or urinary tract infection. {ECO:0000269|PubMed:20797690}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.09183 0.14613 -1.001120478 8.321538099 46.84769 1.32359 HOMER1 0.995922024391312 0.00407764952920563 3.26079482711533e-07 homer scaffolding protein 1 FUNCTION: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Isoform 1 regulates the trafficking and surface expression of GRM5. Isoform 3 acts as a natural dominant negative, in dynamic competition with constitutively expressed isoform 1 to regulate synaptic metabotropic glutamate function. Isoform 3, may be involved in the structural changes that occur at synapses during long-lasting neuronal plasticity and development.; . . smooth muscle;ovary;umbilical cord;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;atrium;frontal lobe;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);amygdala;trophoblast;hypothalamus;urinary;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;peripheral nerve; whole brain;amygdala;subthalamic nucleus;medulla oblongata;occipital lobe;temporal lobe;prefrontal cortex;globus pallidus;pons;cingulate cortex;parietal lobe; 0.78134 0.16844 -0.251530012 35.42108988 . . HOMER2 0.0545468794795003 0.941363116646163 0.00409000387433625 homer scaffolding protein 2 FUNCTION: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;lacrimal gland;islets of Langerhans;hypothalamus;blood;choroid;skin;breast;uterus;bile duct;pancreas;prostate;lung;endometrium;epididymis;bone;thyroid;visual apparatus;liver;testis;spleen;kidney;brain; . 0.45032 0.21299 0.130533008 63.35810333 352.41599 3.97618 HOMER2P1 . . . homer scaffolding protein 2 pseudogene 1 . . . . . . . . . . . HOMER2P2 . . . homer scaffolding protein 2 pseudogene 2 . . . . . . . . . . . HOMER3 0.222332288001803 0.76953662659556 0.00813108540263721 homer scaffolding protein 3 FUNCTION: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses.; . . ovary;parathyroid;choroid;fovea centralis;vein;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;oesophagus;bone;thyroid;iris;brain;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;pharynx;lens;pancreas;lung;placenta;visual apparatus;macula lutea;liver;spleen;cervix;head and neck;kidney;stomach; subthalamic nucleus;superior cervical ganglion;heart;cerebellum peduncles;thyroid;globus pallidus;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.44732 0.13823 -0.181750739 40.15687662 145.24326 2.62428 HOMEZ 0.342229011643787 0.65481690510079 0.00295408325542312 homeobox and leucine zipper encoding FUNCTION: May function as a transcriptional regulator.; . TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in adult testis and kidney as well as fetal lung and kidney. {ECO:0000269|PubMed:12925734}.; unclassifiable (Anatomical System);medulla oblongata;lymph node;heart;tongue;islets of Langerhans;colon;fovea centralis;choroid;lens;skin;retina;uterus;breast;optic nerve;lung;placenta;macula lutea;liver;testis;head and neck; . 0.12857 0.09376 0.286674996 71.49681529 4926.41666 14.30388 HOOK1 4.15670073195207e-05 0.999559540374661 0.000398892618019945 hook microtubule-tethering protein 1 FUNCTION: Required for spermatid differentiation. Probably involved in the positioning of the microtubules of the manchette and the flagellum in relation to the membrane skeleton (By similarity). Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). {ECO:0000250}.; . . . . 0.45946 0.11182 -0.620857637 17.3566879 137.27061 2.54855 HOOK2 6.32320511450437e-09 0.991854052219961 0.00814594145683423 hook microtubule-tethering protein 2 FUNCTION: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Contributes to the establishment and maintenance of centrosome function. May function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. {ECO:0000269|PubMed:17140400, ECO:0000269|PubMed:17540036, ECO:0000269|PubMed:18799622}.; . . medulla oblongata;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;cerebral cortex;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;lacrimal gland;islets of Langerhans;hypothalamus;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland; superior cervical ganglion;thyroid;trigeminal ganglion; 0.10119 0.10697 0.314179756 72.75300778 2046.86585 8.34200 HOOK3 0.99999800538276 1.99461723706597e-06 2.79796654074941e-15 hook microtubule-tethering protein 3 FUNCTION: Probably serves as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking (By similarity). Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). May regulate clearance of endocytosed receptors such as MSR1. Participates in defining the architecture and localization of the Golgi complex. {ECO:0000250, ECO:0000269|PubMed:11238449, ECO:0000269|PubMed:17237231, ECO:0000269|PubMed:18799622}.; . . unclassifiable (Anatomical System);lymph node;heart;ovary;blood;skin;skeletal muscle;bone marrow;breast;prostate;lung;cochlea;placenta;visual apparatus;amnion;testis;germinal center;gall bladder; . 0.18115 0.12073 -0.670411825 15.61689078 29.82218 0.95148 HOPX 0.146965694076451 0.631077003486743 0.221957302436806 HOP homeobox FUNCTION: Atypical homeodomain protein which does not bind DNA and is required to modulate cardiac growth and development. Acts via its interaction with SRF, thereby modulating the expression of SRF-dependent cardiac-specific genes and cardiac development. Prevents SRF-dependent transcription either by inhibiting SRF binding to DNA or by recruiting histone deacetylase (HDAC) proteins that prevent transcription by SRF. Overexpression causes cardiac hypertrophy (By similarity). May act as a tumor suppressor. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in the heart, brain, placenta, lung, skeletal and smooth muscles, uterus, urinary bladder, kidney and spleen. Down-regulated in some types of cancer such as lung cancer, choriocarcinoma, head and neck squamous cell carcinoma and oral squamous cell carcinoma. {ECO:0000269|PubMed:12573257, ECO:0000269|PubMed:12759545}.; medulla oblongata;smooth muscle;ovary;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;whole body;optic nerve;frontal lobe;endometrium;thyroid;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;epidermis;islets of Langerhans;hypothalamus;blood;lens;pancreas;lung;nasopharynx;placenta;hippocampus;macula lutea;visual apparatus;stomach;cerebellum; whole brain;tongue;placenta; 0.17364 0.18111 0.169169615 65.33380514 205.91743 3.10186 HORMAD1 0.00312691335861907 0.985517755157866 0.0113553314835146 HORMA domain containing 1 FUNCTION: Plays a key role in meiotic progression. Regulates 3 different functions during meiosis: ensures that sufficient numbers of processed DNA double-strand breaks (DSBs) are available for successful homology search by increasing the steady-state numbers of single-stranded DSB ends. Promotes synaptonemal-complex formation independently of its role in homology search. Plays a key role in the male mid-pachytene checkpoint and the female meiotic prophase checkpoint: required for efficient build-up of ATR activity on unsynapsed chromosome regions, a process believed to form the basis of meiotic silencing of unsynapsed chromatin (MSUC) and meiotic prophase quality control in both sexes (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis-specific. Over-expressed in carcinomas. {ECO:0000269|PubMed:15999985}.; unclassifiable (Anatomical System);medulla oblongata;testis;mammary gland; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.34431 0.09942 0.104848986 61.49445624 1498.42733 7.20315 HORMAD2 3.44849609468045e-05 0.584244147461912 0.415721367577141 HORMA domain containing 2 FUNCTION: Essential for synapsis surveillance during meiotic prophase via the recruitment of ATR activity. Plays a key role in the male mid-pachytene checkpoint and the female meiotic prophase checkpoint: required for efficient build-up of ATR activity on unsynapsed chromosome regions, a process believed to form the basis of meiotic silencing of unsynapsed chromatin (MSUC) and meiotic prophase quality control in both sexes. Required for the DNA double-strand break-independent, BRCA1-dependent activation of ATR on the sex chromosomes that is essential for normal sex body formation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in testis (at protein level). Expressed in lung adenocarcinoma and squamous cell carcinoma (at protein level). Expressed at lower levels in the liver, brain and kidney. {ECO:0000269|PubMed:15999985, ECO:0000269|PubMed:22893617}.; unclassifiable (Anatomical System);medulla oblongata;lung;liver;testis;kidney; superior cervical ganglion;testis - interstitial;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.14701 0.09455 0.927856124 89.70276008 116.45113 2.34686 HORMAD2-AS1 . . . HORMAD2 antisense RNA 1 . . . . . . . . . . . HOTAIR . . . HOX transcript antisense RNA . . . . . . . . . . . HOTAIRM1 . . . HOXA transcript antisense RNA, myeloid-specific 1 . . . . . . . . . . . HOTTIP . . . HOXA distal transcript antisense RNA . . . . . . . . . . . HOXA-AS2 . . . HOXA cluster antisense RNA 2 . . . . . . . . . . . HOXA-AS3 . . . HOXA cluster antisense RNA 3 . . . . . . . . . . . HOXA1 0.0849873631655924 0.871246371609187 0.0437662652252202 homeobox A1 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures. Seems to act in the maintenance and/or generation of hindbrain segments.; DISEASE: Athabaskan brainstem dysgenesis syndrome (ABDS) [MIM:601536]: Characterized by horizontal gaze palsy, sensorineural deafness, central hypoventilation, and developmental delay. Some patients had swallowing dysfunction, vocal cord paralysis, facial paresis, seizures, and cardiac outflow tract anomalies. {ECO:0000269|PubMed:16155570}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bosley-Salih-Alorainy syndrome (BSAS) [MIM:601536]: A disease characterized by horizontal gaze abnormalities, deafness, facial weakness, vascular malformations of the internal carotid arteries and cardiac outflow trac. Some patients manifest mental retardation and autism spectrum disorder. Affected individuals do not suffer from central hypoventilation. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);bone;brain;bladder;stomach; superior cervical ganglion;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.80315 0.22881 0.062575634 58.74026893 138.6209 2.56455 HOXA2 0.278337993967382 0.698660880694486 0.0230011253381319 homeobox A2 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; DISEASE: Microtia, hearing impairment, and cleft palate (MHICP) [MIM:612290]: A disease characterized by microtia, mixed symmetric severe to profound hearing impairment, and partial cleft palate. Microtia is a congenital deformity of the outer ear that is small and abnormally shaped. In classic microtia, the pinna is essentially absent, except for a vertical sausage-shaped skin remnant. The superior aspect of this sausage-shaped skin remnant consists of underlying unorganized cartilage, and the inferior aspect of this remnant consists of a relatively well-formed lobule. Syndromic forms of microtia occur in conjunction with other abnormalities including cleft palate, a congenital fissure of the soft and/or hard palate due to faulty fusion. {ECO:0000269|PubMed:18394579}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Microtia with or without hearing impairment (MCRT) [MIM:612290]: Microtia is a congenital deformity of the outer ear that is small and abnormally shaped. In classic microtia, the pinna is essentially absent, except for a vertical sausage-shaped skin remnant. The superior aspect of this sausage-shaped skin remnant consists of underlying unorganized cartilage, and the inferior aspect of this remnant consists of a relatively well- formed lobule. {ECO:0000269|PubMed:23775976}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);smooth muscle;lung;ovary;heart;thyroid;liver;testis;colon;head and neck;kidney; superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;trigeminal ganglion;skeletal muscle; 0.42384 0.13878 -0.339715008 30.06605331 36.16556 1.08453 HOXA3 0.931754220622883 0.0679067589368127 0.000339020440304683 homeobox A3 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;urinary;colon;parathyroid;prostate;lung;larynx;placenta;pituitary gland;testis;cervix;head and neck;kidney;mammary gland;aorta;stomach; subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node; 0.56281 0.12883 -0.005381972 53.50908233 83.09844 1.93755 HOXA4 0.00942667003682843 0.814101264899771 0.176472065063401 homeobox A4 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds to sites in the 5'-flanking sequence of its coding region with various affinities. The consensus sequences of the high and low affinity binding sites are 5'-TAATGA[CG]-3' and 5'-CTAATTTT- 3'.; . TISSUE SPECIFICITY: Embryonic nervous system.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;skin;uterus;whole body;lung;endometrium;placenta;liver;testis;amniotic fluid;spleen;kidney;brain; . 0.43874 . . . 1446.47473 7.09489 HOXA5 0.79621299361995 0.198026615710537 0.00576039066951374 homeobox A5 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Also binds to its own promoter. Binds specifically to the motif 5'-CYYNATTA[TG]Y-3'.; . . unclassifiable (Anatomical System);pancreas;lung;whole body;ovary;placenta;testis;colon;parathyroid;germinal center;brain; . 0.99243 0.21481 -0.273576253 33.97027601 24.97328 0.81917 HOXA6 1.80043020270311e-05 0.261665000061784 0.738316995636189 homeobox A6 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);lung;visual apparatus;amniotic fluid;brain; . 0.39553 0.11991 -0.317668748 31.45789101 9.21209 0.33718 HOXA7 0.00316907031376716 0.598244643517389 0.398586286168844 homeobox A7 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);uterus;lung;bone;placenta;testis;colon;kidney;vein; . 0.77607 0.11023 0.21689899 68.12927577 159.92209 2.76090 HOXA9 0.000100012594431347 0.353323917405884 0.646576069999684 homeobox A9 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. {ECO:0000269|PubMed:22269951}.; DISEASE: Note=A chromosomal aberration involving HOXA9 is found in a form of acute myeloid leukemia. Translocation t(7;11)(p15;p15) with NUP98.; DISEASE: Note=A chromosomal aberration involving HOXA9 may contribute to disease progression in chronic myeloid leukemia. Translocation t(7;17)(p15;q23) with MSI2.; . unclassifiable (Anatomical System);ovary;cartilage;colon;blood;skin;uterus;prostate;endometrium;placenta;bone;testis;cervix;kidney; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.94111 0.40610 -0.005381972 53.50908233 85.51718 1.97203 HOXA10 0.678435260569461 0.316952297792256 0.00461244163828279 homeobox A10 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds to the DNA sequence 5'-AA[AT]TTTTATTAC-3'.; . . unclassifiable (Anatomical System);lymph node;cartilage;heart;colon;blood;skin;bone marrow;bile duct;uterus;prostate;lung;endometrium;synovium;bone;placenta;visual apparatus;liver;testis;kidney;brain;peripheral nerve; . 0.99786 . . . 118.73422 2.37018 HOXA10-AS . . . HOXA10 antisense RNA . . . . . . . . . . . HOXA11 0.863825169181447 0.134188933950083 0.00198589686846927 homeobox A11 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; DISEASE: Radioulnar synostosis with amegakaryocytic thrombocytopenia (RSAT) [MIM:605432]: The syndrome consists of an unusual association of bone marrow failure and skeletal defects. Patients have the same skeletal defects, the proximal fusion of the radius and ulna, resulting in extremely limited pronation and supination of the forearm. Some patients have also symptomatic thrombocytopenia, with bruising and bleeding problems since birth, necessitating correction by bone marrow or umbilical-cord stem- cell transplantation. {ECO:0000269|PubMed:11101832}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymphoreticular;smooth muscle;cartilage;ovary;colon;parathyroid;skin;uterus;prostate;endometrium;bone;placenta;liver;spleen;cervix;kidney;brain;stomach; uterus;amygdala;superior cervical ganglion;uterus corpus;testis;atrioventricular node; 0.37463 0.23021 -0.361761279 28.6329323 37.83874 1.12463 HOXA11-AS . . . HOXA11 antisense RNA . . . . . . . . . . . HOXA13 . . . homeobox A13 FUNCTION: Sequence-specific, AT-rich binding transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior- posterior axis.; DISEASE: Hand-foot-genital syndrome (HFG) [MIM:140000]: A disorder characterized by limb and genitourinary anomalies. Clinical features include small feet with unusually short great toes and abnormal thumbs. Females with the disorder have duplication of the genital tract. {ECO:0000269|PubMed:10839976, ECO:0000269|PubMed:12073020}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Guttmacher syndrome (GUTTS) [MIM:176305]: Dominantly inherited combination of distal limb and genital tract abnormalities. It has several features in common with hand-foot- genital syndrome, including hypoplastic first digits and hypospadias. Typical features not seen in hand-foot-genital syndrome include postaxial polydactyly of the hands and uniphalangeal second toes with absent nails. {ECO:0000269|PubMed:11968094}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;prostate;pancreas;heart;placenta;liver;colon;bladder;skin; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle;parietal lobe; 0.68929 . . . 122.9053 2.41409 HOXA@ . . . homeobox A cluster . . . . . . . . . . . HOXB-AS1 . . . HOXB cluster antisense RNA 1 . . . . . . . . . . . HOXB-AS2 . . . HOXB cluster antisense RNA 2 . . . . . . . . . . . HOXB-AS3 . . . HOXB cluster antisense RNA 3 . . . . . . . . . . . HOXB-AS4 . . . HOXB cluster antisense RNA 4 . . . . . . . . . . . HOXB1 0.115199709546097 0.857588563935988 0.0272117265179145 homeobox B1 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures.; DISEASE: Facial paresis, hereditary congenital, 3 (HCFP3) [MIM:614744]: A form of facial paresis, a disease characterized by isolated dysfunction of the facial nerve (CN VII). HCFP3 patients are affected by bilateral facial palsy, facial muscle weakness of muscles innervated by CN VII, hearing loss, and strabismus. {ECO:0000269|PubMed:22770981}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System); superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.78216 0.16646 0.194852702 67.03231894 1079.64503 6.29890 HOXB2 0.00183830846418713 0.720699042332429 0.277462649203384 homeobox B2 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. {ECO:0000269|PubMed:10595394}.; . . unclassifiable (Anatomical System);heart;ovary;sympathetic chain;adrenal cortex;colon;parathyroid;skin;uterus;pancreas;whole body;lung;cerebral cortex;endometrium;bone;placenta;liver;testis;brain;stomach;peripheral nerve; adrenal gland;spinal cord; 0.38232 . -0.091746757 46.91554612 148.37143 2.65404 HOXB3 0.610993265044198 0.380633355162578 0.00837337979322368 homeobox B3 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);uterus;cerebral cortex;endometrium;blood; dorsal root ganglion;atrioventricular node;cingulate cortex;skeletal muscle; 0.45029 . -0.22584292 37.32012267 58.11765 1.54255 HOXB4 0.119746209572469 0.779452332575787 0.100801457851745 homeobox B4 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);uterus;myocardium;pancreas;lung;cartilage;endometrium;testis;blood;kidney;mammary gland;skeletal muscle; . 0.35821 0.25237 0.3032669 72.009908 44.84119 1.28372 HOXB5 0.481440388121452 0.496082743452521 0.0224768684260268 homeobox B5 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . TISSUE SPECIFICITY: Spinal cord.; unclassifiable (Anatomical System);cartilage;ovary;colon;parathyroid;uterus;pancreas;prostate;whole body;lung;endometrium;placenta;testis;spleen;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.98125 0.16686 -0.273576253 33.97027601 20.91465 0.70772 HOXB6 0.00958340713523565 0.81672021386098 0.173696379003785 homeobox B6 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);cartilage;ovary;colon;parathyroid;blood;breast;uterus;prostate;whole body;lung;endometrium;bone;placenta;duodenum;testis;cervix;kidney;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.44539 0.32894 . . 43.68844 1.25783 HOXB7 0.00759639061323712 0.777387724557811 0.215015884828952 homeobox B7 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;endometrium;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;muscle;pharynx;blood;bile duct;pancreas;lung;visual apparatus;liver;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.71697 0.19162 . . 735.07067 5.37818 HOXB8 0.444768417534794 0.548716697178651 0.00651488528655478 homeobox B8 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);prostate;whole body;ovary;placenta;testis;colon;parathyroid;cervix;blood;kidney; . 0.70662 0.17050 0.347360312 73.97381458 275.34627 3.55414 HOXB9 0.101637476227325 0.773258893477158 0.125103630295517 homeobox B9 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);ovary;muscle;colon;breast;pancreas;prostate;whole body;lung;bone;amniotic fluid;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;kidney;skeletal muscle;cerebellum; 0.94566 0.13197 0.014844891 54.94810097 153.95584 2.71253 HOXB13 0.00987475094591023 0.821405115827386 0.168720133226704 homeobox B13 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; DISEASE: Prostate cancer (PC) [MIM:176807]: A malignancy originating in tissues of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma. {ECO:0000269|PubMed:22236224, ECO:0000269|PubMed:22714738, ECO:0000269|PubMed:23064873, ECO:0000269|PubMed:23292082, ECO:0000269|PubMed:25629170}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;colon;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;prostate;optic nerve;lung;bone;macula lutea;visual apparatus;testis;brain;stomach; dorsal root ganglion;uterus corpus;prostate;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.23838 0.14726 -0.073340031 48.11866006 31.93126 1.00461 HOXB@ . . . homeobox B cluster . . . . . . . . . . . HOXC-AS1 . . . HOXC cluster antisense RNA 1 . . . . . . . . . . . HOXC-AS2 . . . HOXC cluster antisense RNA 2 . . . . . . . . . . . HOXC-AS3 . . . HOXC cluster antisense RNA 3 . . . . . . . . . . . HOXC4 0.311491215792623 0.670787072252532 0.0177217119548454 homeobox C4 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);lung;bone;sympathetic chain;colon;kidney;spinal ganglion;brain;skin; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.24592 0.15588 0.393270925 76.04977589 1227.25694 6.62119 HOXC5 0.039073775712826 0.839063526186414 0.121862698100759 homeobox C5 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);lung;whole body;ovary;visual apparatus;testis;kidney;stomach; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion; 0.88105 . 0.080983847 59.76055674 94.27743 2.08934 HOXC6 0.907689925205709 0.0915807266509614 0.000729348143329381 homeobox C6 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);heart;ovary;colon;blood;parathyroid;skin;uterus;pancreas;lung;placenta;testis;kidney;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;olfactory bulb;adipose tissue;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.89509 0.12378 -0.073340031 48.11866006 36.57663 1.09681 HOXC8 0.392360835996751 0.598020665266465 0.00961849873678434 homeobox C8 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);breast;lung;cartilage;bone;kidney; dorsal root ganglion;skeletal muscle; 0.42841 0.17984 -0.251530012 35.42108988 45.93106 1.30406 HOXC9 0.128099662221138 0.780190128294889 0.0917102094839735 homeobox C9 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);cartilage;heart;colon;skin;uterus;breast;larynx;bone;liver;testis;head and neck;cervix;kidney;brain;stomach; superior cervical ganglion;skeletal muscle; 0.57833 0.12841 . . 173.55995 2.86917 HOXC10 0.648346217700278 0.345576829368353 0.00607695293136917 homeobox C10 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;skin;breast;uterus;pancreas;prostate;whole body;lung;endometrium;bone;placenta;liver;testis;cervix;kidney;stomach; superior cervical ganglion;adipose tissue;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion; 0.65041 0.12450 -0.47017169 23.25430526 82.76994 1.93235 HOXC11 0.0786952810694774 0.872285611631581 0.049019107298941 homeobox C11 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds to a promoter element of the lactase-phlorizin hydrolase gene.; . . unclassifiable (Anatomical System);lung;bone;testis;cervix;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.73855 0.13576 -0.427900189 25.14744043 739.58494 5.40045 HOXC12 1.8910234355918e-09 0.00953838158922963 0.990461616519747 homeobox C12 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . . . 0.48129 0.11137 . . 147.24409 2.64383 HOXC13 0.379358816453153 0.575250746119503 0.0453904374273445 homeobox C13 FUNCTION: Transcription factor which plays a role in hair follicle differentiation. Regulates FOXQ1 expression and that of other hair-specific genes (By similarity). {ECO:0000250}.; DISEASE: Ectodermal dysplasia 9, hair/nail type (ECTD9) [MIM:614931]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures such as hair, teeth, nails and sweat glands, with or without any additional clinical sign. Each combination of clinical features represents a different type of ectodermal dysplasia. ECTD9 is characterized by hypotrichosis and nail dystrophy without non-ectodermal or other ectodermal manifestations. Hypotrichosis usually occurs after birth with varying degrees of severity, ranging from mild hair loss to complete atrichia, including the loss of scalp hair, beard, eyebrows, eyelashes, axillary hair, and pubic hair. Nail dystrophy affects all 20 digits by causing short fragile nails or spoon nails (koilonychia). {ECO:0000269|PubMed:23063621}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;ovary;parathyroid;skin;uterus;breast;pancreas;larynx;placenta;bone;visual apparatus;head and neck;cervix;stomach; superior cervical ganglion;trigeminal ganglion;cingulate cortex; 0.43866 0.12121 . . 208.85373 3.11867 HOXC13-AS . . . HOXC13 antisense RNA . . . . . . . . . . . HOXC@ . . . homeobox C cluster . . . . . . . . . . . HOXD-AS2 . . . HOXD cluster antisense RNA 2 . . . . . . . . . . . HOXD1 0.0105884596930334 0.831957114636209 0.157454425670757 homeobox D1 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures.; . . unclassifiable (Anatomical System);heart;ovary;urinary;colon;parathyroid;skin;uterus;pancreas;whole body;lung;placenta;liver;testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;cerebellum; 0.22711 0.11232 . . 1842.48447 7.91637 HOXD3 0.407559214082803 0.583849866032942 0.00859091988425493 homeobox D3 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);lung;ovary;endometrium;visual apparatus;kidney;mammary gland; superior cervical ganglion;testis;appendix;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.30676 0.20527 0.106667882 61.73036093 82.0261 1.92024 HOXD4 0.167399010627391 0.771774292910368 0.0608266964622417 homeobox D4 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . uterus;heart;endometrium;kidney;skin;skeletal muscle; . 0.56855 0.12666 -0.205617011 38.57631517 1547.41349 7.29746 HOXD8 0.617630962362728 0.37444714710939 0.00792189052788207 homeobox D8 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);uterus;lung;heart;sympathetic chain;testis;kidney;brain;mammary gland;bladder; testis - interstitial;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;testis;ciliary ganglion;caudate nucleus; 0.20417 0.10681 . . 432.7737 4.34173 HOXD9 0.422099307773999 0.543925697679505 0.033974994546496 homeobox D9 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;blood;skin;skeletal muscle;uterus;prostate;optic nerve;lung;endometrium;placenta;testis;cervix;kidney;brain;stomach; dorsal root ganglion;skeletal muscle; 0.48119 . . . 142.62847 2.60441 HOXD10 0.132556118191002 0.845927856923414 0.021516024885584 homeobox D10 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; DISEASE: Vertical talus, congenital (CVT) [MIM:192950]: A rare malformation characterized by vertical orientation of the talus with a rigid dorsal dislocation of the navicular, equinus deformity of the calcaneus, abduction deformity of the forefoot, and contracture of the soft tissues of the hind- and mid-foot. This condition is usually associated with multiple other congenital deformities and only rarely is an isolated deformity with familial occurrence. {ECO:0000269|PubMed:15146389}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Strongly expressed in the adult male and female urogenital tracts.; unclassifiable (Anatomical System);uterus;heart;kidney;skin; superior cervical ganglion;uterus corpus;temporal lobe;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle;parietal lobe; 0.61794 0.11868 -0.049474214 50.01179523 44.97885 1.28820 HOXD11 0.0131898476206074 0.661759099481592 0.3250510528978 homeobox D11 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . unclassifiable (Anatomical System);uterus;prostate;whole body;heart;bone;placenta;urinary;cervix;kidney;brain;skin; superior cervical ganglion;atrioventricular node; 0.23968 . . . 52.05051 1.42475 HOXD12 0.00334591723055039 0.610026817212266 0.386627265557184 homeobox D12 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; . . . . 0.88860 0.19255 0.395088462 76.15003539 604.16052 4.97604 HOXD13 0.33206948542304 0.652799793274805 0.0151307213021551 homeobox D13 FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; DISEASE: Synpolydactyly 1 (SPD1) [MIM:186000]: Limb malformation that shows a characteristic manifestation in both hands and feet. This condition is inherited as an autosomal dominant trait with reduced penetrance. {ECO:0000269|PubMed:12414828, ECO:0000269|PubMed:8817328}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Brachydactyly D (BDD) [MIM:113200]: A form of brachydactyly. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. Brachydactyly type D is characterized by short and broad terminal phalanges of the thumbs and big toes. {ECO:0000269|PubMed:12649808}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Syndactyly 5 (SDTY5) [MIM:186300]: A form of syndactyly, a congenital anomaly of the hand or foot marked by persistence of the webbing between adjacent digits that are more or less completely attached. The characteristic finding in SDTY5 is the presence of an associated metacarpal and metatarsal fusion. The metacarpals and metatarsals most commonly fused are the 4th and 5th or the 3rd and 4th. Soft tissue syndactyly usually affects the 3rd and 4th fingers and the 2nd and 3rd toes. {ECO:0000269|PubMed:17236141}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Brachydactyly-syndactyly syndrome (BDSD) [MIM:610713]: A disease characterized by generalized shortening of the hands and feet, broad and short distal phalanges of the thumbs, and cutaneous syndactyly of toes 2 and 3. The limb phenotypes observed in this syndrome overlap those of brachydactyly types A4, D, E and syndactyly type 1. {ECO:0000269|PubMed:17236141}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Brachydactyly E1 (BDE1) [MIM:113300]: A form of brachydactyly. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. Brachydactyly type E is characterized by shortening of the fingers mainly in the metacarpals and metatarsals. Wide variability in the number of digits affected occurs from person to person, even in the same family. Some individuals are moderately short of stature. Brachydactyly type E1 is characterized by shortening limited to fourth metacarpals and/or metatarsals. {ECO:0000269|PubMed:12649808}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: VACTERL association (VACTERL) [MIM:192350]: VACTERL is an acronym for vertebral anomalies, anal atresia, congenital cardiac disease, tracheoesophageal fistula, renal anomalies, radial dysplasia, and other limb defects. {ECO:0000269|PubMed:19006232}. Note=The gene represented in this entry may be involved in disease pathogenesis.; . . . 0.83205 0.40904 -0.095386216 46.48502005 95.62533 2.11131 HOXD@ . . . homeobox D cluster . . . . . . . . . . . HP 0.0293907467277115 0.923705635180552 0.0469036180917364 haptoglobin FUNCTION: As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an Antimicrobial; Antioxidant, has antibacterial activity and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidely cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pathway. {ECO:0000269|PubMed:21248165}.; DISEASE: Anhaptoglobinemia (AHP) [MIM:614081]: A condition characterized by the absence of the serum glycoprotein haptoglobin. Serum levels of haptoglobin vary among normal persons: levels are low in the neonatal period and in the elderly, differ by population, and can be influenced by environmental factors, such as infection. Secondary hypohaptoglobinemia can occur as a consequence of hemolysis, during which haptoglobin binds to free hemoglobin. Congenital haptoglobin deficiency is a risk factor for anaphylactic non-hemolytic transfusion reactions. {ECO:0000269|PubMed:14999562}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; unclassifiable (Anatomical System);cartilage;ovary;blood;skeletal muscle;bone marrow;uterus;lung;endometrium;nasopharynx;alveolus;liver;spleen;stomach;gall bladder; fetal liver;superior cervical ganglion;adipose tissue;liver;fetal lung;atrioventricular node;trigeminal ganglion;bone marrow; . 0.84093 -0.80269335 12.23755603 392.89017 4.17017 HP1BP3 0.991643467677446 0.00835615117339761 3.81149156081669e-07 heterochromatin protein 1 binding protein 3 FUNCTION: Component of heterochromatin that maintains heterochromatin integrity during G1/S progression and regulates the duration of G1 phase to critically influence cell proliferative capacity (PubMed:24830416). Mediates chromatin condensation during hypoxia, leading to increased tumor cell viability, radio-resistance, chemo-resistance and self- renewal(PubMed:25100860). {ECO:0000269|PubMed:24830416, ECO:0000269|PubMed:25100860}.; . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;cochlea;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;stomach;peripheral nerve;thymus; superior cervical ganglion;skeletal muscle; 0.51974 0.16149 -0.26993514 34.59542345 60.34656 1.57913 HPC1 . . . hereditary prostate cancer 1 . . . . . . . . . . . HPCA 0.433846185685315 0.534809260960759 0.0313445533539255 hippocalcin FUNCTION: May be involved in the calcium-dependent regulation of rhodopsin phosphorylation. Binds two calcium ions.; DISEASE: Dystonia 2, torsion, autosomal recessive (DYT2) [MIM:224500]: A form of torsion dystonia, a disease defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. 'Torsion' refers to the twisting nature of body movements, often affecting the trunk. DYT2 is a slowly progressive form that first affects distal limbs and later involves the neck, orofacial, and craniocervical regions. {ECO:0000269|PubMed:25799108}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.44847 0.16306 -0.09720619 46.20193442 3.85861 0.14403 HPCAL1 0.779954229263187 0.21296241309511 0.0070833576417029 hippocalcin like 1 FUNCTION: May be involved in the calcium-dependent regulation of rhodopsin phosphorylation.; . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;greater omentum;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum; whole brain;amygdala;occipital lobe;cerebellum peduncles;temporal lobe;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.22820 0.13477 -0.073340031 48.11866006 9.80626 0.35955 HPCAL4 0.0184227514017707 0.727873214800875 0.253704033797355 hippocalcin like 4 FUNCTION: May be involved in the calcium-dependent regulation of rhodopsin phosphorylation. {ECO:0000250}.; . . . . 0.17416 0.12921 -0.207437529 38.2814343 5.19266 0.19344 HPCX . . . hereditary prostate cancer, X-linked . . . . . . . . . . . HPD 0.00776520567552076 0.989131194375298 0.00310359994918092 4-hydroxyphenylpyruvate dioxygenase FUNCTION: Key enzyme in the degradation of tyrosine.; DISEASE: Tyrosinemia 3 (TYRSN3) [MIM:276710]: An inborn error of metabolism characterized by elevations of tyrosine in the blood and urine, seizures and mild mental retardation. {ECO:0000269|PubMed:10942115, ECO:0000269|PubMed:11073718}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hawkinsinuria (HAWK) [MIM:140350]: An inborn error of tyrosine metabolism characterized by failure to thrive, persistent metabolic acidosis, fine and sparse hair, and excretion of the unusual cyclic amino acid metabolite, hawkinsin, in the urine. {ECO:0000269|PubMed:11073718}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);colon;fovea centralis;choroid;lens;retina;optic nerve;lung;macula lutea;hippocampus;visual apparatus;liver;iris;spleen;cervix;kidney;stomach; superior cervical ganglion;fetal liver;liver;kidney;trigeminal ganglion;skeletal muscle; 0.09532 0.35459 0.464864541 78.69190847 445.11138 4.39027 HPDL 0.0139648272169788 0.868526334921881 0.11750883786114 4-hydroxyphenylpyruvate dioxygenase-like FUNCTION: May have dioxygenase activity. {ECO:0000305}.; . . unclassifiable (Anatomical System);lung;placenta;testis;colon;cervix;blood;brain;mammary gland;stomach;retina; . 0.05977 0.15732 -0.071520315 48.34866714 19.88683 0.67699 HPE1 . . . holoprosencephaly 1, alobar . . . . . . . . . . . HPFH2 . . . hereditary persistence of fetal hemoglobin, heterocellular, Indian type . . . . . . . . . . . HPGD 0.00328250843894793 0.827650929991925 0.169066561569127 hydroxyprostaglandin dehydrogenase 15-(NAD) FUNCTION: Prostaglandin inactivation. Contributes to the regulation of events that are under the control of prostaglandin levels. Catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4. Inhibits in vivo proliferation of colon cancer cells. {ECO:0000269|PubMed:10837478, ECO:0000269|PubMed:15574495, ECO:0000269|PubMed:16828555}.; DISEASE: Hypertrophic osteoarthropathy, primary, autosomal recessive, 1 (PHOAR1) [MIM:259100]: A disease characterized by digital clubbing, periostosis, acroosteolysis, painful joint enlargement, and variable features of pachydermia that include thickened facial skin and a thickened scalp. Other developmental anomalies include delayed closure of the cranial sutures and congenital heart disease. {ECO:0000269|PubMed:18500342}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cranioosteoarthropathy (COA) [MIM:259100]: A form of osteoarthropathy characterized by swelling of the joints, digital clubbing, hyperhidrosis, delayed closure of the fontanels, periostosis, and variable patent ductus arteriosus. Pachydermia is not a prominent feature. {ECO:0000269|PubMed:18500342}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Isolated congenital nail clubbing (ICNC) [MIM:119900]: A rare genodermatosis characterized by enlargement of the nail plate and terminal segments of the fingers and toes, resulting from proliferation of the connective tissues between the nail matrix and the distal phalanx. It is usually symmetrical and bilateral (in some cases unilateral). In nail clubbing usually the distal end of the nail matrix is relatively high compared to the proximal end, while the nail plate is complete but its dimensions and diameter more or less vary in comparison to normal. There may be different fingers and toes involved to varying degrees. Some fingers or toes are spared, but the thumbs are almost always involved. {ECO:0000269|PubMed:18805827}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in colon epithelium (at protein level). {ECO:0000269|PubMed:15574495}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;iris;testis;bladder;unclassifiable (Anatomical System);heart;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;uterus;superior cervical ganglion;placenta;fetal lung;trigeminal ganglion; 0.57438 0.23162 -0.205617011 38.57631517 62.58814 1.61796 HPGDS 8.21760977553245e-07 0.16559933365894 0.834399844580083 hematopoietic prostaglandin D synthase FUNCTION: Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides and organic isothiocyanates. Also exhibits low glutathione-peroxidase activity towards cumene hydroperoxide. {ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:19939518, ECO:0000269|PubMed:9353279, ECO:0000269|PubMed:9425264}.; . TISSUE SPECIFICITY: Expressed in a number of megakaryocytic cell lines but not in platelets. Highly expressed in adipose tissue, macrophages and placenta. Also expressed at lower levels in lung, heart, lymph nodes, appendix, bone marrow and fetal liver. {ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:9353279, ECO:0000269|PubMed:9425264}.; unclassifiable (Anatomical System);myocardium;umbilical cord;adrenal cortex;blood;parathyroid;lung;adrenal gland;nasopharynx;placenta;thyroid;testis;kidney;pineal gland; superior cervical ganglion;pons;trigeminal ganglion; . . 0.194852702 67.03231894 206.65965 3.10685 HPLH1 . . . hemophagocytic lymphohistiocytosis 1 FUNCTION: May have an involvement in muscle development or hypertrophy.; DISEASE: Scapuloperoneal myopathy, X-linked dominant (SPM) [MIM:300695]: A disease characterized by progressive muscle weakness and wasting, upper and lower limbs weakness, foot drop, scapular winging, and myopathic changes on muscle biopsy. Most affected individuals become wheelchair-bound. {ECO:0000269|PubMed:18179901}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myopathy, X-linked, with postural muscle atrophy (XMPMA) [MIM:300696]: A progressive muscular dystrophy with onset in adulthood. Affected individuals develop a proximal myopathy characterized by specific atrophy of postural muscles, limited neck flexion, bent spine, contractures of the Achilles tendon, respiratory problems, and cardiomyopathy. Patients may show muscle hypertrophy in the early stages of the disorder. {ECO:0000269|PubMed:18179888}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Reducing body myopathy, X-linked 1A, severe, with infantile or early childhood onset (RBMX1A) [MIM:300717]: A rare myopathy clinically characterized by rapidly progressive muscular weakness, and pathologically by the presence of intracytoplasmic inclusion bodies strongly stained by menadione-linked alpha- glycerophosphate dehydrogenase in the absence of substrate, alpha- glycerophosphate. The term 'reducing body' refers to the reducing activity of the inclusions to nitroblue tetrazolium in the absence of substrate. This condition is also commonly associated with rimmed vacuoles and cytoplasmic bodies. Death in childhood is frequent in the severe form of the disease, due to respiratory failure. {ECO:0000269|PubMed:18274675}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Reducing body myopathy, X-linked 1B, with late childhood or adult onset (RBMX1B) [MIM:300718]: A rare myopathy clinically characterized by rapidly progressive muscular weakness, and pathologically by the presence of intracytoplasmic inclusion bodies strongly stained by menadione-linked alpha-glycerophosphate dehydrogenase in the absence of substrate, alpha-glycerophosphate. The term 'reducing body' refers to the reducing activity of the inclusions to nitroblue tetrazolium in the absence of substrate. This condition is also commonly associated with rimmed vacuoles and cytoplasmic bodies. {ECO:0000269|PubMed:18274675}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is highly expressed in skeletal muscle and to a lesser extent in heart, placenta, ovary, prostate, testis, small intestine, colon and spleen. Expression is barely detectable in brain, lung, liver, kidney, pancreas, thymus and peripheral blood leukocytes. Isoform 2 is expressed in brain, skeletal muscle and to a lesser extent in heart, colon, prostate and small intestine. Isoform 3 is expressed in testis, heart and skeletal muscle. {ECO:0000269|PubMed:10352231, ECO:0000269|PubMed:10480922, ECO:0000269|PubMed:10524257, ECO:0000269|PubMed:11400158, ECO:0000269|PubMed:9714789}.; . . 0.45850 0.13588 -0.029247611 51.40363293 . . HPN 0.997916181778818 0.00208375485203099 6.33691514275082e-08 hepsin FUNCTION: Plays an essential role in cell growth and maintenance of cell morphology. May mediate the activating cleavage of HGF and MST1/HGFL. Plays a role in the proteolytic processing of ACE2. {ECO:0000269|PubMed:15839837, ECO:0000269|PubMed:21875933, ECO:0000269|PubMed:24227843}.; . TISSUE SPECIFICITY: Present in most tissues, with the highest level in liver.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;skeletal muscle;uterus;pancreas;prostate;whole body;lung;endometrium;epididymis;thyroid;liver;spleen;kidney;brain;stomach; fetal liver;liver;kidney; 0.28168 0.26172 -0.47017169 23.25430526 57.2172 1.52327 HPN-AS1 . . . HPN antisense RNA 1 . . . . . . . . . . . HPP1 . . . hyperpigmentation, progressive, 1 . . . . . . . . . . . HPR 2.94872175113387e-07 0.17370690981753 0.826292795310295 haptoglobin-related protein FUNCTION: Primate-specific plasma protein associated with apolipoprotein L-I (apoL-I)-containing high-density lipoprotein (HDL). This HDL particle, termed trypanosome lytic factor-1 (TLF- 1), mediates human innate immune protection against many species of African trypanosomes. Binds hemoglobin with high affinity and may contribute to the clearance of cell-free hemoglobin to allow hepatic recycling of heme iron. {ECO:0000269|PubMed:16778136}.; . TISSUE SPECIFICITY: In adult liver the amount of HPR mRNA is at the lower limit of detection, therefore the extent of its expression is at most less than 1000-fold that of the HP1F gene. No HPR mRNA can be detected in fetal liver. Expressed in Hep-G2 and leukemia MOLT-4 cell lines. {ECO:0000269|PubMed:8945641}.; unclassifiable (Anatomical System);heart;cartilage;ovary;hypothalamus;blood;skeletal muscle;bone marrow;uterus;lung;endometrium;nasopharynx;alveolus;liver;spleen;brain;stomach;gall bladder; fetal liver;superior cervical ganglion;adipose tissue;liver;fetal lung;atrioventricular node;trigeminal ganglion;bone marrow; . 0.84093 0.376678994 75.50719509 536.91867 4.72373 HPRT1 0.916893576419955 0.0825482146179769 0.000558208962068263 hypoxanthine phosphoribosyltransferase 1 FUNCTION: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5- phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway.; DISEASE: Lesch-Nyhan syndrome (LNS) [MIM:300322]: Characterized by complete lack of enzymatic activity that results in hyperuricemia, choreoathetosis, mental retardation, and compulsive self- mutilation. {ECO:0000269|PubMed:15571223, ECO:0000269|PubMed:17027311, ECO:0000269|PubMed:2071157, ECO:0000269|PubMed:2246854, ECO:0000269|PubMed:2347587, ECO:0000269|PubMed:2358296, ECO:0000269|PubMed:24940672, ECO:0000269|PubMed:2910902, ECO:0000269|PubMed:3265398, ECO:0000269|PubMed:3384338, ECO:0000269|PubMed:6853716, ECO:0000269|PubMed:7627191, ECO:0000269|PubMed:9452051}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Gout HPRT-related (GOUT-HPRT) [MIM:300323]: Characterized by partial enzyme activity and hyperuricemia. {ECO:0000269|PubMed:15571223, ECO:0000269|PubMed:17027311, ECO:0000269|PubMed:20544509, ECO:0000269|PubMed:24940672, ECO:0000269|PubMed:2909537, ECO:0000269|PubMed:3198771, ECO:0000269|PubMed:3358423, ECO:0000269|PubMed:6572373, ECO:0000269|PubMed:6706936, ECO:0000269|PubMed:6853490, ECO:0000269|PubMed:7987318}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;substantia nigra;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;bile duct;breast;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; amygdala;whole brain;testis - interstitial;medulla oblongata;occipital lobe;superior cervical ganglion;hypothalamus;temporal lobe;pons;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;cingulate cortex;parietal lobe; 0.65494 0.94051 -0.009020804 52.8544468 3.61036 0.13211 HPRT1P1 . . . hypoxanthine phosphoribosyltransferase 1 pseudogene 1 . . . . . . . . . . . HPRT1P2 . . . hypoxanthine phosphoribosyltransferase 1 pseudogene 2 . . . . . . . . . . . HPRT1P3 . . . hypoxanthine phosphoribosyltransferase 1 pseudogene 3 . . . . . . . . . . . HPS1 5.9907099496673e-07 0.96719882033045 0.0328005805985547 HPS1, biogenesis of lysosomal organelles complex 3 subunit 1 FUNCTION: Component of multiple cytoplasmic organelles. Apparently crucial for their normal development and function. May be involved in intracellular protein sorting.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;medulla oblongata;ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;small intestine;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;liver;cervix;spleen;kidney;mammary gland;stomach;peripheral nerve;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle;skin;bone marrow; 0.56605 0.15893 0.850585932 88.49374853 2245.61435 8.74351 HPS3 3.52030440679389e-15 0.136562010146379 0.863437989853617 HPS3, biogenesis of lysosomal organelles complex 2 subunit 1 FUNCTION: Involved in early stages of melanosome biogenesis and maturation. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Higher levels of expression are observed in kidney, liver and placenta.; smooth muscle;ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;tongue;pharynx;blood;lens;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;adrenal gland;placenta;head and neck;kidney;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.55069 0.16394 -1.282303301 5.130927105 227.78064 3.25888 HPS4 1.40159466155322e-05 0.958127596803329 0.0418583872500551 HPS4, biogenesis of lysosomal organelles complex 3 subunit 2 FUNCTION: May function in the pathway of organelle biogenesis.; DISEASE: Hermansky-Pudlak syndrome 4 (HPS4) [MIM:614073]: A form of Hermansky-Pudlak syndrome, a genetically heterogeneous autosomal recessive disorder characterized by oculocutaneous albinism, bleeding due to platelet storage pool deficiency, and lysosomal storage defects. This syndrome results from defects of diverse cytoplasmic organelles including melanosomes, platelet dense granules and lysosomes. Ceroid storage in the lungs is associated with pulmonary fibrosis, a common cause of premature death in individuals with HPS. {ECO:0000269|PubMed:11836498}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;pia mater;lung;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; trigeminal ganglion;skeletal muscle; 0.10351 0.22400 1.76373572 96.76220807 676.45649 5.19590 HPS5 9.07535902902917e-06 0.999845626840371 0.000145297800600081 HPS5, biogenesis of lysosomal organelles complex 2 subunit 2 FUNCTION: May regulate the synthesis and function of lysosomes and of highly specialized organelles, such as melanosomes and platelet dense granules. Regulates intracellular vesicular trafficking in fibroblasts. May be involved in the regulation of general functions of integrins. {ECO:0000269|PubMed:15296495, ECO:0000269|PubMed:17301833}.; . TISSUE SPECIFICITY: Widely expressed. Isoform 1:Highly expressed in lungs and testis. Isoform 2:Highly expressed in placenta, kidney, testis ovary, lung and thymus. {ECO:0000269|PubMed:15296495}.; ovary;salivary gland;colon;parathyroid;skin;uterus;prostate;optic nerve;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;testis;trigeminal ganglion;skeletal muscle; 0.11105 0.18651 0.185543665 66.2715263 1900.67032 8.01647 HPS6 0.301742441643438 0.698088198773101 0.000169359583460206 HPS6, biogenesis of lysosomal organelles complex 2 subunit 3 FUNCTION: May regulate the synthesis and function of lysosomes and of highly specialized organelles, such as melanosomes and platelet dense granules. {ECO:0000269|PubMed:17041891}.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;optic nerve;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node; 0.10132 0.14852 -1.043396569 7.71408351 80.48507 1.89577 HPSE 1.81464251749446e-08 0.636706160685246 0.363293821168329 heparanase FUNCTION: Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix (ECM) degradation and remodeling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. It is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans, and increases endothelial invasion and angiogenesis in myelomas. Acts as procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extacellular matrix (ECM), independent of its enzymatic activity. Induces AKT1/PKB phosphorylation via lipid rafts increasing cell mobility and invasion. Heparin increases this AKT1/PKB activation. Regulates osteogenesis. Enhances angiogenesis through up- regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis. {ECO:0000269|PubMed:12213822, ECO:0000269|PubMed:12773484, ECO:0000269|PubMed:15044433, ECO:0000269|PubMed:16452201, ECO:0000269|PubMed:18557927, ECO:0000269|PubMed:18798279, ECO:0000269|PubMed:19244131, ECO:0000269|PubMed:20097882, ECO:0000269|PubMed:20181948, ECO:0000269|PubMed:20309870, ECO:0000269|PubMed:20561914, ECO:0000269|PubMed:21131364}.; . TISSUE SPECIFICITY: Highly expressed in placenta and spleen and weakly expressed in lymph node, thymus, peripheral blood leukocytes, bone marrow, endothelial cells, fetal liver and tumor tissues. Also expressed in hair follicles, specifically in both Henle's and Huxley's layers of inner the root sheath (IRS) at anagen phase. {ECO:0000269|PubMed:10395326, ECO:0000269|PubMed:10405343, ECO:0000269|PubMed:10764835, ECO:0000269|PubMed:18557927, ECO:0000269|PubMed:20309870}.; unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;adrenal cortex;colon;parathyroid;uterus;pancreas;lung;nasopharynx;bone;placenta;pituitary gland;liver;testis;spleen;germinal center;kidney;brain; placenta; 0.07488 0.32465 0.022122107 55.69120075 170.93256 2.85201 HPSE2 1.85176194871334e-06 0.875616336385948 0.124381811852103 heparanase 2 (inactive) FUNCTION: Binds heparin and heparan sulfate with high affinity, but lacks heparanase activity. Inhibits HPSE, possibly by competing for its substrates (in vitro). {ECO:0000269|PubMed:20576607}.; DISEASE: Urofacial syndrome 1 (UFS1) [MIM:236730]: A rare autosomal recessive disorder characterized by facial grimacing when attempting to smile and failure of the urinary bladder to void completely despite a lack of anatomical bladder outflow obstruction or overt neurological damage. Affected individuals often have reflux of infected urine from the bladder to the upper renal tract, with a risk of kidney damage and renal failure. {ECO:0000269|PubMed:20560209, ECO:0000269|PubMed:20560210}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, with the highest expression in brain, mammary gland, prostate, small intestine, testis and uterus. In the central nervous system, expressed in the spinal chord, caudate nucleus, thalamus, substantia nigra, medulla oblongata, putamen and pons. In the urinary bladder, expressed in longitudinal and circular layers of detrusor muscle. Found both in normal and cancer tissues. {ECO:0000269|PubMed:11027606, ECO:0000269|PubMed:20560210}.; . . 0.29661 0.18462 0.088260113 60.56853031 215.03157 3.16398 HPT . . . hypoparathyroidism . . . . . . . . . . . HPV6AI1 . . . human papillomavirus (type 6a) integration site 1 . . . . . . . . . . . HPV18I1 . . . human papilloma virus (type 18) integration site 1 . . . . . . . . . . . HPV18I2 . . . human papillomavirus (type 18) integration site 2 . . . . . . . . . . . HPVC1 . . . human papillomavirus (type 18) E5 central sequence-like 1 . . . . . . . . . . . HPX 0.00412144745614206 0.988189736186449 0.00768881635740911 hemopexin FUNCTION: Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation.; . TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; unclassifiable (Anatomical System);lung;whole body;heart;bone;liver;testis;spleen;brain;mammary gland;gall bladder; fetal liver;subthalamic nucleus;adrenal cortex;liver;fetal lung;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.27843 0.54325 0.112125503 62.09601321 344.00549 3.93368 HPYR1 . . . Helicobacter pylori responsive 1 (non-protein coding) . . . . . . . . . . . HR 2.12734947334705e-05 0.999767443687523 0.000211282817743024 hair growth associated FUNCTION: Histone demethylase that specifically demethylates both mono- and dimethylated 'Lys-9' of histone H3. May act as a transcription regulator controlling hair biology (via targeting of collagens), neural activity, and cell cycle. {ECO:0000269|PubMed:24334705}.; DISEASE: Alopecia universalis congenita (ALUNC) [MIM:203655]: A rare disorder characterized by loss of hair from the entire body. No hair are present in hair follicles on skin biopsy. {ECO:0000269|PubMed:12406339, ECO:0000269|PubMed:9445480, ECO:0000269|PubMed:9736769}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Atrichia with papular lesions (APL) [MIM:209500]: An autosomal recessive disease characterized by papillary lesions over most of the body and almost complete absence of hair. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hypotrichosis 4 (HYPT4) [MIM:146550]: An autosomal dominant condition characterized by reduced amount of hair, alopecia, little or no eyebrows, eyelashes or body hair, and coarse, wiry, twisted hair in early childhood. {ECO:0000269|PubMed:19122663, ECO:0000269|PubMed:24961381}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Strongest expression of isoforms 1 and 2 is seen in the small intestine, weaker expression in brain and colon, and trace expression is found in liver, pancreas, spleen, thymus, stomach, salivary gland, appendix and trachea. Isoform 1 is always the most abundant. Isoform 1 is exclusively expressed at low levels in kidney and testis. Isoform 2 is exclusively expressed at high levels in the skin. {ECO:0000269|PubMed:10051399, ECO:0000269|PubMed:9736769}.; unclassifiable (Anatomical System);heart;pineal body;colon;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;frontal lobe;larynx;placenta;macula lutea;testis;head and neck;cervix;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.20146 0.12424 1.238210393 93.30620429 2359.44163 9.01450 HRAS 0.00794104930284198 0.785285637637198 0.20677331305996 Harvey rat sarcoma viral oncogene homolog FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. {ECO:0000269|PubMed:12740440, ECO:0000269|PubMed:14500341, ECO:0000269|PubMed:9020151}.; DISEASE: Costello syndrome (CSTLO) [MIM:218040]: A rare condition characterized by prenatally increased growth, postnatal growth deficiency, mental retardation, distinctive facial appearance, cardiovascular abnormalities (typically pulmonic stenosis, hypertrophic cardiomyopathy and/or atrial tachycardia), tumor predisposition, skin and musculoskeletal abnormalities. {ECO:0000269|PubMed:16170316, ECO:0000269|PubMed:16329078, ECO:0000269|PubMed:16443854, ECO:0000269|PubMed:17054105, ECO:0000269|PubMed:18039947, ECO:0000269|PubMed:18247425, ECO:0000269|PubMed:19995790}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Congenital myopathy with excess of muscle spindles (CMEMS) [MIM:218040]: Variant of Costello syndrome. {ECO:0000269|PubMed:17412879}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hurthle cell thyroid carcinoma (HCTC) [MIM:607464]: A rare type of thyroid cancer accounting for only about 3-10% of all differentiated thyroid cancers. These neoplasms are considered a variant of follicular carcinoma of the thyroid and are referred to as follicular carcinoma, oxyphilic type. {ECO:0000269|PubMed:12727991}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=Mutations which change positions 12, 13 or 61 activate the potential of HRAS to transform cultured cells and are implicated in a variety of human tumors. {ECO:0000269|PubMed:3670300}.; DISEASE: Bladder cancer (BLC) [MIM:109800]: A malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas that begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences. {ECO:0000269|PubMed:6298635, ECO:0000269|PubMed:6844927}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Schimmelpenning-Feuerstein-Mims syndrome (SFM) [MIM:163200]: A disease characterized by sebaceous nevi, often on the face, associated with variable ipsilateral abnormalities of the central nervous system, ocular anomalies, and skeletal defects. Many oral manifestations have been reported, not only including hypoplastic and malformed teeth, and mucosal papillomatosis, but also ankyloglossia, hemihyperplastic tongue, intraoral nevus, giant cell granuloma, ameloblastoma, bone cysts, follicular cysts, oligodontia, and odontodysplasia. Sebaceous nevi follow the lines of Blaschko and these can continue as linear intraoral lesions, as in mucosal papillomatosis. {ECO:0000269|PubMed:22683711}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14500341}.; ovary;developmental;colon;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;oesophagus;endometrium;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;lung;placenta;visual apparatus;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; whole brain;medulla oblongata;trigeminal ganglion; 0.99944 0.99980 -0.339715008 30.06605331 4.91473 0.18207 HRASLS 0.000717831128354625 0.518735472244493 0.480546696627153 HRAS like suppressor FUNCTION: Exhibits calcium-independent phospholipase activity towards phosphatidylcholine (PC) and phosphatidylethanolamine (PE). Also shows acyltransferase activities, transferring an acyl group of PCs to the amino group of PEs and the hydroxyl group of lyso PCs. {ECO:0000269|PubMed:21880860}.; . TISSUE SPECIFICITY: Abundantly expressed in testis, skeletal muscle, brain, and heart. {ECO:0000269|PubMed:21880860}.; unclassifiable (Anatomical System);uterus;lung;whole body;ovary;macula lutea;testis;cervix;fovea centralis;brain;pineal gland;skeletal muscle; testis - interstitial;testis - seminiferous tubule;testis; 0.07267 0.11276 -0.117432389 44.89266336 83.42496 1.94171 HRASLS2 0.0182738037126763 0.726352244252976 0.255373952034348 HRAS like suppressor 2 FUNCTION: Exhibits PLA1/2 activity, catalyzing the calcium- independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. Catalyzes N-acylation of PE using both sn-1 and sn-2 palmitoyl groups of PC as acyl donor. Also catalyzes O-acylation converting lyso-PC into PC. {ECO:0000269|PubMed:19615464}.; . TISSUE SPECIFICITY: Expressed in liver, kidney, small intestine testis and colon (PubMed:19615464). Undetectable in testis, placenta, salivary gland and fetal brain (PubMed:18163183). {ECO:0000269|PubMed:18163183, ECO:0000269|PubMed:19615464}.; unclassifiable (Anatomical System);lung;thyroid;testis;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;skin;skeletal muscle; 0.01021 0.04717 0.082802743 60.09082331 55.32699 1.49279 HRASLS5 0.000123369757946174 0.619627423180986 0.380249207061068 HRAS like suppressor family member 5 FUNCTION: catalyzes N-acylation of phosphatidylethanolamine (PE) to generate N-Acylphosphatidylethanolamine (NAPE) a precursor of bioactive N-acylethanolamines, including the endocannabinoid anandamide. {ECO:0000269|PubMed:19000777}.; . TISSUE SPECIFICITY: Highest expression level in testis and pancreas.; unclassifiable (Anatomical System);medulla oblongata;lung;ovary;testis; testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.04664 0.06022 1.484536216 95.31729181 289.40446 3.63903 HRC 3.13676309509999e-05 0.938156955407487 0.0618116769615621 histidine rich calcium binding protein FUNCTION: May play a role in the regulation of calcium sequestration or release in the SR of skeletal and cardiac muscle.; . . unclassifiable (Anatomical System);myocardium;prostate;heart;liver;choroid;skeletal muscle; superior cervical ganglion;heart;skeletal muscle; 0.09082 0.10821 1.890561548 97.3165841 3253.38154 10.86120 HRCT1 0.158290620361276 0.637337237458589 0.204372142180135 histidine rich carboxyl terminus 1 . . . . . . . 0.971952656 90.26893135 3373.78484 11.12060 HRES1 . . . HTLV-1 related endogenous sequence . . . . . . . . . . . HRG 1.70020586338944e-12 0.0150313119474337 0.984968688050866 histidine rich glycoprotein FUNCTION: Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such as immune complex and pathogen clearance, cell chemotaxis, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2. Acts as a regulator of the vascular endothelial growth factor (VEGF) signaling pathway; inhibits endothelial cell motility by reducing VEGF-induced complex formation between PXN/paxillin and ILK/integrin-linked protein kinase and by promoting inhibition of VEGF-induced tyrosine phosphorylation of focal adhesion kinases and alpha-actinins in endothelial cells. Also plays a role in the regulation of tumor angiogenesis and tumor immune surveillance. Normalizes tumor vessels and promotes antitumor immunity by polarizing tumor-associated macrophages, leading to decreased tumor growth and metastasis. {ECO:0000269|PubMed:11134179, ECO:0000269|PubMed:12235005, ECO:0000269|PubMed:14744774, ECO:0000269|PubMed:15220341, ECO:0000269|PubMed:15313924, ECO:0000269|PubMed:16436387, ECO:0000269|PubMed:16489009, ECO:0000269|PubMed:19285951, ECO:0000269|PubMed:19535045, ECO:0000269|PubMed:19712047, ECO:0000269|PubMed:19903770, ECO:0000269|PubMed:20573803, ECO:0000269|PubMed:21215706, ECO:0000269|PubMed:21304106}.; DISEASE: Thrombophilia due to histidine-rich glycoprotein deficiency (THPH11) [MIM:613116]: A hemostatic disorder characterized by a tendency to thrombosis. {ECO:0000269|PubMed:11057869, ECO:0000269|PubMed:9414276}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in macrophages and in malignant cells. Expressed by the liver and secreted in plasma (at protein level). {ECO:0000269|PubMed:14744774, ECO:0000269|PubMed:19903770, ECO:0000269|PubMed:21215706}.; unclassifiable (Anatomical System);uterus;lung;heart;liver;testis;colon;spleen;kidney;skin;stomach; dorsal root ganglion;superior cervical ganglion;fetal liver;liver;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.08365 0.23013 3.668232708 99.55178108 6246.61359 16.54837 HRH1 0.00156116787120129 0.882252402170328 0.116186429958471 histamine receptor H1 FUNCTION: In peripheral tissues, the H1 subclass of histamine receptors mediates the contraction of smooth muscles, increase in capillary permeability due to contraction of terminal venules, and catecholamine release from adrenal medulla, as well as mediating neurotransmission in the central nervous system.; . . . . 0.12992 0.14371 0.374860183 75.43052607 91.19342 2.05392 HRH2 0.83527325871176 0.16145630101233 0.00327044027590981 histamine receptor H2 FUNCTION: The H2 subclass of histamine receptors mediates gastric acid secretion. Also appears to regulate gastrointestinal motility and intestinal secretion. Possible role in regulating cell growth and differentiation. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase and, through a separate G protein-dependent mechanism, the phosphoinositide/protein kinase (PKC) signaling pathway (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);kidney; superior cervical ganglion; 0.13225 0.15038 -0.516085732 21.20193442 5.58713 0.20832 HRH3 0.366881477706972 0.621485558375915 0.0116329639171125 histamine receptor H3 FUNCTION: The H3 subclass of histamine receptors could mediate the histamine signals in CNS and peripheral nervous system. Signals through the inhibition of adenylate cyclase and displays high constitutive activity (spontaneous activity in the absence of agonist). Agonist stimulation of isoform 3 neither modified adenylate cyclase activity nor induced intracellular calcium mobilization.; . TISSUE SPECIFICITY: Expressed predominantly in the CNS, with the greatest expression in the thalamus and caudate nucleus. The various isoforms are mainly coexpressed in brain, but their relative expression level varies in a region-specific manner. Isoform 3 and isoform 7 are highly expressed in the thalamus, caudate nucleus and cerebellum while isoform 5 and isoform 6 show a poor expression. Isoform 5 and isoform 6 show a high expression in the amygdala, substantia nigra, cerebral cortex and hypothalamus. Isoform 7 is not found in hypothalamus or substantia nigra.; unclassifiable (Anatomical System);frontal lobe;brain; medulla oblongata;superior cervical ganglion;globus pallidus;ciliary ganglion;caudate nucleus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.13091 0.14017 -0.381986487 27.68931352 29.11072 0.93080 HRH4 1.67289121238146e-07 0.127196481098851 0.872803351612028 histamine receptor H4 FUNCTION: The H4 subclass of histamine receptors could mediate the histamine signals in peripheral tissues. Displays a significant level of constitutive activity (spontaneous activity in the absence of agonist). {ECO:0000269|PubMed:12503632}.; . TISSUE SPECIFICITY: Expressed primarily in the bone marrow and eosinophils. Shows preferential distribution in cells of immunological relevance such as T-cells, dendritic cells, monocytes, mast cells, neutrophils. Also expressed in a wide variety of peripheral tissues, including the heart, kidney, liver, lung, pancreas, skeletal muscle, prostate, small intestine, spleen, testis, colon, fetal liver and lymph node. {ECO:0000269|PubMed:12503632}.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.14531 0.12217 0.68351529 85.03774475 775.35427 5.51278 HRK . . . harakiri, BCL2 interacting protein FUNCTION: Promotes apoptosis. {ECO:0000269|PubMed:15031724, ECO:0000269|PubMed:9130713}.; . . unclassifiable (Anatomical System);uterus;lymph node;heart;skin; superior cervical ganglion;trigeminal ganglion; 0.31112 . . . 7.87563 0.28921 HRNR 5.01202544702428e-29 0.999822617360506 0.000177382639494222 hornerin FUNCTION: Component of the epidermal cornified cell envelopes. {ECO:0000269|PubMed:21282207}.; . TISSUE SPECIFICITY: Expressed in cornified epidermis, psoriatic and regenerating skin after wounding. Found in the upper granular layer and in the entire cornified layer of epidermis. {ECO:0000269|PubMed:15507446, ECO:0000269|PubMed:21282207}.; . . 0.18527 0.10879 -0.141298762 42.87567823 4521.01702 13.50310 HS1BP3 0.000353324886507251 0.829054118425793 0.170592556687699 HCLS1 binding protein 3 FUNCTION: May be a modulator of IL-2 signaling. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lung;cornea;placenta;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12276 0.09924 0.711016566 85.72776598 769.75452 5.48992 HS1BP3-IT1 . . . HS1BP3 intronic transcript 1 . . . . . . . . . . . HS2ST1 0.535866622243903 0.463464750714515 0.000668627041582084 heparan sulfate 2-O-sulfotransferase 1 FUNCTION: Catalyzes the transfer of sulfate to the C2-position of selected hexuronic acid residues within the maturing heparan sulfate (HS). 2-O-sulfation within HS, particularly of iduronate residues, is essential for HS to participate in a variety of high- affinity ligand-binding interactions and signaling processes. Mediates 2-O-sulfation of both L-iduronyl and D-glucuronyl residues (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;frontal lobe;cartilage;endometrium;islets of Langerhans;placenta;visual apparatus;hippocampus;testis;brain;skeletal muscle;stomach; amygdala;superior cervical ganglion;prefrontal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.85379 0.14176 -0.005381972 53.50908233 45.88283 1.30316 HS3ST1 0.00617541021258819 0.73842636403027 0.255398225757141 heparan sulfate-glucosamine 3-sulfotransferase 1 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site. {ECO:0000269|PubMed:9346953}.; . TISSUE SPECIFICITY: Highly expressed in the brain and kidney and weakly expressed in the heart, lung and placenta. {ECO:0000269|PubMed:9988767}.; unclassifiable (Anatomical System);ovary;hypothalamus;colon;parathyroid;blood;fovea centralis;retina;whole body;lung;bone;placenta;macula lutea;hippocampus;hypopharynx;testis;head and neck;spleen;germinal center;kidney;brain;mammary gland;bladder;stomach; cerebellum peduncles;atrioventricular node;skeletal muscle;cerebellum; 0.07246 0.13175 -0.426079032 25.36565228 285.43597 3.61701 HS3ST2 0.212162588155993 0.778881433490758 0.00895597835324936 heparan sulfate-glucosamine 3-sulfotransferase 2 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N- unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in GlcA2S-GlcNS. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate.; . TISSUE SPECIFICITY: Highly expressed in the brain and weakly expressed in the heart, placenta, lung and skeletal muscle. {ECO:0000269|PubMed:9988767}.; unclassifiable (Anatomical System);optic nerve;lung;cartilage;islets of Langerhans;placenta;choroid;kidney;brain; whole brain;dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex;parietal lobe; 0.40391 0.13431 -0.161524709 41.6430762 110.89084 2.29570 HS3ST3A1 . . . heparan sulfate-glucosamine 3-sulfotransferase 3A1 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N- unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry. Unlike 3-OST-1, does not convert non- anticoagulant heparan sulfate to anticoagulant heparan sulfate. {ECO:0000269|PubMed:10520990}.; . TISSUE SPECIFICITY: Ubiquitous. Most abundant in heart and placenta, followed by liver and kidney. {ECO:0000269|PubMed:9988767}.; unclassifiable (Anatomical System);uterus;lung;whole body;heart;bone;placenta;muscle;colon;brain;skin; superior cervical ganglion;trigeminal ganglion; 0.04246 0.14226 . . 387.81432 4.14876 HS3ST3B1 0.085454926854491 0.760461162325554 0.154083910819955 heparan sulfate-glucosamine 3-sulfotransferase 3B1 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N- unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry. Unlike 3-OST-1, does not convert non- anticoagulant heparan sulfate to anticoagulant heparan sulfate. {ECO:0000269|PubMed:10520990}.; . TISSUE SPECIFICITY: Ubiquitous. Most abundant in liver and placenta, followed by heart and kidney. {ECO:0000269|PubMed:9988767}.; ovary;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;larynx;testis;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;tongue;lacrimal gland;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.18243 0.11102 . . 248.66731 3.39841 HS3ST4 0.581015604864414 0.408305835375856 0.01067855975973 heparan sulfate-glucosamine 3-sulfotransferase 4 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N- unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Unlike 3-OST-1, does not convert non- anticoagulant heparan sulfate to anticoagulant heparan sulfate (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:9988767}.; brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.16398 . . . 370.50242 4.06472 HS3ST5 0.569245912900789 0.419039564727221 0.0117145223719901 heparan sulfate-glucosamine 3-sulfotransferase 5 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site. Also generates GlcUA- GlcNS or IdoUA-GlcNS and IdoUA2S-GlcNH2. The substrate-specific O- sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry. {ECO:0000269|PubMed:12138164}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle and fetal brain, and also found in adult brain, spinal cord, cerebellum and colon. {ECO:0000269|PubMed:12138164, ECO:0000269|PubMed:12740361}.; unclassifiable (Anatomical System);lung;larynx;head and neck;brain;stomach; . 0.48732 0.11432 0.106667882 61.73036093 39.78823 1.17236 HS3ST6 0.00322375385292522 0.601956982280684 0.39481926386639 heparan sulfate-glucosamine 3-sulfotransferase 6 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to heparan sulfate. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes Simplex Virus-1 (HSV-1) and permits its entry. Unlike 3- OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate. {ECO:0000269|PubMed:15303968}.; . . unclassifiable (Anatomical System);prostate;optic nerve;heart;macula lutea;fovea centralis;choroid;lens;retina; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle;skin; 0.05734 0.11432 0.106667882 61.73036093 7934.87321 19.23969 HS6ST1 0.906059214439201 0.0931780945801464 0.000762690980652594 heparan sulfate 6-O-sulfotransferase 1 FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate. Critical for normal neuronal development where it may play a role in neuron branching. May also play a role in limb development. May prefer iduronic acid. {ECO:0000269|PubMed:21700882}.; DISEASE: Hypogonadotropic hypogonadism 15 with or without anosmia (HH15) [MIM:614880]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:21700882, ECO:0000269|PubMed:25077900}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in fetal brain. {ECO:0000269|PubMed:9535912}.; unclassifiable (Anatomical System);uterus;ovary;heart;endometrium;visual apparatus;germinal center;brain;skin; . 0.46499 0.15578 . . 219.6517 3.20652 HS6ST1P1 . . . heparan sulfate 6-O-sulfotransferase 1 pseudogene 1 . . . . . . . . . . . HS6ST2 0.119199983371802 0.855074480341609 0.0257255362865892 heparan sulfate 6-O-sulfotransferase 2 FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate.; . . unclassifiable (Anatomical System);thyroid;colon;bone marrow; globus pallidus; 0.44508 0.10349 0.238945317 69.20853975 110.26687 2.28442 HS6ST2-AS1 . . . HS6ST2 antisense RNA 1 . . . . . . . . . . . HS6ST3 0.747377572908153 0.250362513546854 0.00225991354499291 heparan sulfate 6-O-sulfotransferase 3 FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate.; . . . . 0.59827 0.11479 -0.113792788 45.25831564 369.2782 4.06133 HSBP1 0.530903532161435 0.408835375403252 0.0602610924353132 heat shock factor binding protein 1 FUNCTION: Negative regulator of the heat shock response. Negatively affects HSF1 DNA-binding activity. May have a role in the suppression of the activation of the stress response during the aging process.; . . . . 0.14212 0.09145 0.079165051 59.43029016 7.21533 0.27192 HSBP1L1 . . . heat shock factor binding protein 1-like 1 . . . . . . . 0.61192669 82.99716914 5.30066 0.19599 HSBP1P1 . . . heat shock factor binding protein 1 pseudogene 1 . . . . . . . . . . . HSBP1P2 . . . heat shock factor binding protein 1 pseudogene 2 . . . unclassifiable (Anatomical System);umbilical cord;ovary;heart;salivary gland;intestine;pharynx;colon;blood;lens;skin;skeletal muscle;retina;uterus;prostate;atrium;lung;cochlea;visual apparatus;alveolus;liver;testis;spleen;kidney;germinal center;brain;mammary gland;bladder; . 0.14212 . . . . . HSCB 0.000141919775298349 0.650190987757107 0.349667092467595 HscB mitochondrial iron-sulfur cluster co-chaperone FUNCTION: Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria. {ECO:0000269|PubMed:20668094}.; . TISSUE SPECIFICITY: Expressed in lung, brain, stomach, spleen, ovary, testis, liver, muscle and heart. {ECO:0000269|PubMed:12938016, ECO:0000269|PubMed:20668094}.; unclassifiable (Anatomical System);lung;heart;thyroid;placenta;visual apparatus;liver;testis;colon;spleen;kidney;germinal center;brain; superior cervical ganglion;ciliary ganglion; 0.10187 0.12339 0.215080721 67.91696155 166.01119 2.81916 HSD3B1 8.51173207421434e-05 0.774308986699933 0.225605895979325 hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1 FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. Efficiently catalyzes the transformation of pregnenolone to progesterone, 17-alpha-hydroxypregnenolone to 17- alpha-hydroxyprogesterone, DHEA to 4-androstenedione, dihydrotestosterone to 5-alpha-androstane-3 beta,17 beta-diol, dehydroepiandrosterone to androstenedione and 5-alpha-androstan-3 beta,17 beta-diol to 5-alpha-dihydrotestosterone. {ECO:0000269|PubMed:1401999, ECO:0000269|PubMed:2139411}.; . TISSUE SPECIFICITY: Placenta and skin. Predominantly expressed in mammary gland tissue.; unclassifiable (Anatomical System);ovary;colon;blood;parathyroid;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;optic nerve;adrenal gland;placenta;macula lutea;liver;spleen; placenta;adrenal cortex; 0.14489 0.32692 0.154398214 64.73814579 53.24055 1.44917 HSD3B2 1.21147217431287e-06 0.204166868625763 0.795831919902063 hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 2 FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids.; DISEASE: Note=Mild HSD3B2 deficiency in hyperandrogenic females is associated with characteristic traits of polycystic ovary syndrome, such as insulin resistance and luteinizing hormone hypersecretion. {ECO:0000269|PubMed:14764797}.; TISSUE SPECIFICITY: Expressed in adrenal gland, testis and ovary.; . . 0.13279 0.27298 0.086440867 60.47416844 94.24227 2.08826 HSD3B7 4.6418471440819e-06 0.401043650057428 0.598951708095428 hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 7 FUNCTION: The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. HSD VII is active against four 7-alpha-hydroxylated sterols. Does not metabolize several different C(19/21) steroids as substrates. Involved in bile acid synthesis.; DISEASE: Congenital bile acid synthesis defect 1 (CBAS1) [MIM:607765]: A primary defect in bile synthesis leading to progressive liver disease. Clinical features include neonatal jaundice, severe intrahepatic cholestasis, cirrhosis. {ECO:0000269|PubMed:11067870, ECO:0000269|PubMed:12679481}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;endometrium;pituitary gland;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;lens;breast;pancreas;lung;placenta;visual apparatus;macula lutea;liver;cervix;spleen;kidney;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.20431 0.17304 -0.200157416 39.11299835 2910.85435 10.23683 HSD3BP1 . . . hydroxy-delta-5-steroid dehydrogenase, 3 beta, pseudogene 1 . . . . . . . . . . . HSD3BP2 . . . hydroxy-delta-5-steroid dehydrogenase, 3 beta, pseudogene 2 . . . . . . . . . . . HSD3BP3 . . . hydroxy-delta-5-steroid dehydrogenase, 3 beta, pseudogene 3 . . . . . . . . . . . HSD3BP4 . . . hydroxy-delta-5-steroid dehydrogenase, 3 beta, pseudogene 4 . . . . . . . . . . . HSD3BP5 . . . hydroxy-delta-5-steroid dehydrogenase, 3 beta, pseudogene 5 . . . . . . . . . . . HSD11B1 0.691555250680053 0.304378760488008 0.00406598883193896 hydroxysteroid (11-beta) dehydrogenase 1 FUNCTION: Catalyzes reversibly the conversion of cortisol to the inactive metabolite cortisone. Catalyzes reversibly the conversion of 7-ketocholesterol to 7-beta-hydroxycholesterol. In intact cells, the reaction runs only in one direction, from 7- ketocholesterol to 7-beta-hydroxycholesterol (By similarity). {ECO:0000250}.; DISEASE: Cortisone reductase deficiency (CRD) [MIM:604931]: In CRD, activation of cortisone to cortisol does not occur, resulting in adrenocorticotropin-mediated androgen excess and a phenotype resembling polycystic ovary syndrome (PCOS). {ECO:0000269|PubMed:12858176}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Highest expression in liver.; unclassifiable (Anatomical System);medulla oblongata;cartilage;ovary;colon;blood;skin;uterus;pancreas;prostate;lung;cerebral cortex;placenta;pituitary gland;alveolus;liver;spleen;kidney;brain; dorsal root ganglion;superior cervical ganglion;placenta;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.38141 0.63224 -0.427900189 25.14744043 4.46983 0.16220 HSD11B1L 0.00169630641794967 0.704087430660645 0.294216262921405 hydroxysteroid (11-beta) dehydrogenase 1-like . . . ovary;salivary gland;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;muscle;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;kidney;stomach; . 0.13258 . 0.058937498 58.26256192 75.61656 1.82083 HSD11B2 0.244955464937436 0.724823671685825 0.0302208633767394 hydroxysteroid (11-beta) dehydrogenase 2 FUNCTION: Catalyzes the conversion of cortisol to the inactive metabolite cortisone. Modulates intracellular glucocorticoid levels, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids.; . TISSUE SPECIFICITY: Expressed in kidney, pancreas, prostate, ovary, small intestine and colon. At midgestation, expressed at high levels in placenta and in fetal kidney and, at much lower levels, in fetal lung and testis (PubMed:8530071). {ECO:0000269|PubMed:8530071}.; unclassifiable (Anatomical System);medulla oblongata;heart;lacrimal gland;colon;skin;bile duct;uterus;prostate;lung;frontal lobe;endometrium;thyroid;placenta;liver;testis;spleen;kidney;brain;mammary gland;bladder;stomach; subthalamic nucleus;salivary gland;placenta;kidney;trigeminal ganglion;skin; 0.72570 0.64394 -0.47017169 23.25430526 28.64779 0.91706 HSD17B1 0.0560175126865773 0.865604261359475 0.0783782259539478 hydroxysteroid (17-beta) dehydrogenase 1 FUNCTION: Favors the reduction of estrogens and androgens. Also has 20-alpha-HSD activity. Uses preferentially NADH.; . . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;colon;parathyroid;blood;fovea centralis;choroid;lens;skin;retina;pancreas;optic nerve;whole body;lung;endometrium;bone;placenta;macula lutea;visual apparatus;liver;brain;mammary gland;aorta; placenta;atrioventricular node;skeletal muscle; 0.27098 0.28524 -0.137658575 43.57159707 36.9477 1.10568 HSD17B1P1 . . . hydroxysteroid (17-beta) dehydrogenase 1 pseudogene 1 . . . . . . . . . . . HSD17B2 3.82582400367301e-10 0.0264220467508261 0.973577952866592 hydroxysteroid (17-beta) dehydrogenase 2 FUNCTION: Capable of catalyzing the interconversion of testosterone and androstenedione, as well as estradiol and estrone. Also has 20-alpha-HSD activity. Uses NADH while EDH17B3 uses NADPH.; . . ovary;colon;retina;bone marrow;prostate;larynx;bone;iris;brain;unclassifiable (Anatomical System);small intestine;heart;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; fetal liver;superior cervical ganglion;placenta;liver; 0.20302 . 0.20030965 67.3566879 164.9854 2.80982 HSD17B3 2.48712329277216e-05 0.751588150997587 0.248386977769485 hydroxysteroid (17-beta) dehydrogenase 3 FUNCTION: Favors the reduction of androstenedione to testosterone. Uses NADPH while the two other EDH17B enzymes use NADH.; . TISSUE SPECIFICITY: Testis.; . . 0.12200 0.21916 -0.157884861 42.05590941 269.99321 3.52555 HSD17B4 1.82463226929793e-05 0.998683550324624 0.00129820335268338 hydroxysteroid (17-beta) dehydrogenase 4 FUNCTION: Bifunctional enzyme acting on the peroxisomal beta- oxidation pathway for fatty acids. Catalyzes the formation of 3- ketoacyl-CoA intermediates from both straight-chain and 2-methyl- branched-chain fatty acids. {ECO:0000269|PubMed:8902629, ECO:0000269|PubMed:9089413}.; DISEASE: Perrault syndrome 1 (PRLTS1) [MIM:233400]: A sex- influenced disorder characterized by sensorineural deafness in both males and females and ovarian dysgenesis in females. Some patients also have neurologic manifestations, including mild mental retardation and cerebellar and peripheral nervous system involvement. {ECO:0000269|PubMed:20673864}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Present in many tissues with highest concentrations in liver, heart, prostate and testis.; ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; thalamus;fetal liver;occipital lobe;adipose tissue;hypothalamus;prefrontal cortex;caudate nucleus;parietal lobe;cingulate cortex; 0.65952 0.49708 0.270087468 70.69473933 11180.56296 23.00098 HSD17B6 0.381986470871383 0.615840973313996 0.00217255581462144 hydroxysteroid (17-beta) dehydrogenase 6 FUNCTION: NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (in vitro). Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (in vitro). Converts 5-alpha-androstan-3- alpha,17-beta-diol to androsterone and estradiol to estrone (in vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards androsterone (in vitro). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro). Can convert androsterone to epi-androsterone. Androsterone is first oxidized to 5-alpha- androstane-3,17-dione and then reduced to epi-andosterone. Can act on both C-19 and C-21 3-alpha-hydroxysteroids. {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992, ECO:0000269|PubMed:11513953}.; . TISSUE SPECIFICITY: Detected in liver and prostate (at protein level). Detected in adult liver, lung, brain, placenta, prostate, adrenal gland, testis, mammary gland, spleen, spinal cord and uterus. Detected in caudate nucleus, and at lower levels in amygdala, corpus callosum, hippocampus, substantia nigra and thalamus. Detected in fetal lung, liver and brain. {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:9188497}.; unclassifiable (Anatomical System);medulla oblongata;heart;ovary;parathyroid;skin;uterus;prostate;lung;trabecular meshwork;placenta;liver;testis;germinal center;brain; occipital lobe;uterus corpus;thyroid;liver;testis;caudate nucleus;fetal thyroid; 0.12846 0.26652 -0.0274281 51.65723048 53.53801 1.45445 HSD17B7 0.00175450778717878 0.896172410879783 0.102073081333038 hydroxysteroid (17-beta) dehydrogenase 7 FUNCTION: Responsible for the reduction of the keto group on the C-3 of sterols. {ECO:0000269|PubMed:12829805}.; . TISSUE SPECIFICITY: Highly expressed in adrenal gland, liver, lung and thymus. Expressed in breast, ovaries, pituitary gland, pregnant uterus, prostate, kidney, lymph node, small intestine, spinal cord and trachea. Weakly expressed in all other tissues tested. Isoform 3 is expressed in eye ciliary epithelial cells and neuroendocrine cells.; ovary;salivary gland;colon;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bladder;brain;unclassifiable (Anatomical System);tongue;islets of Langerhans;pharynx;blood;breast;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; . . . 0.016664174 55.21939137 643.08042 5.09426 HSD17B7P1 . . . hydroxysteroid (17-beta) dehydrogenase 7 pseudogene 1 . . . . . . . . . . . HSD17B7P2 . . . hydroxysteroid (17-beta) dehydrogenase 7 pseudogene 2 FUNCTION: Responsible for the reduction of the keto group on the C-3 of sterols. {ECO:0000269|PubMed:12829805}.; . TISSUE SPECIFICITY: Highly expressed in adrenal gland, liver, lung and thymus. Expressed in breast, ovaries, pituitary gland, pregnant uterus, prostate, kidney, lymph node, small intestine, spinal cord and trachea. Weakly expressed in all other tissues tested. Isoform 3 is expressed in eye ciliary epithelial cells and neuroendocrine cells.; ovary;salivary gland;colon;bone marrow;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;pituitary gland;bladder;brain;unclassifiable (Anatomical System);tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; . . 0.06435 0.016664174 55.21939137 . . HSD17B8 0.744497984421353 0.255021072737254 0.000480942841393109 hydroxysteroid (17-beta) dehydrogenase 8 FUNCTION: NAD-dependent 17-beta-hydroxysteroid dehydrogenase with highest activity towards estradiol. Has very low activity towards testosterone. The heteroteramer with CBR4 has NADH-dependent 3- ketoacyl-acyl carrier protein reductase activity. May play a role in biosynthesis of fatty acids in mitochondria. {ECO:0000269|PubMed:17978863, ECO:0000269|PubMed:19571038}.; . TISSUE SPECIFICITY: Highly expressed in placenta, liver and pancreas, lower in the skeletal muscle and kidney. Widely expressed. {ECO:0000269|PubMed:17978863}.; . . 0.18096 . 0.569646743 81.88841708 256.25067 3.44381 HSD17B10 0.886870267829669 0.111901173578175 0.00122855859215596 hydroxysteroid (17-beta) dehydrogenase 10 FUNCTION: Functions in mitochondrial tRNA maturation. Part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/TRMT10C, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends. Catalyzes the beta-oxidation at position 17 of androgens and estrogens and has 3-alpha-hydroxysteroid dehydrogenase activity with androsterone. Catalyzes the third step in the beta-oxidation of fatty acids. Carries out oxidative conversions of 7-alpha-OH and 7-beta-OH bile acids. Also exhibits 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids. By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD). {ECO:0000269|PubMed:12917011, ECO:0000269|PubMed:18984158, ECO:0000269|PubMed:9338779}.; DISEASE: Mental retardation, X-linked, syndromic, 10 (MRXS10) [MIM:300220]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXS10 patients manifest mild mental retardation, choreoathetosis and abnormal behavior. {ECO:0000269|PubMed:17236142}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mental retardation, X-linked 17 (MRX17) [MIM:300705]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non- syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. {ECO:0000269|PubMed:18252223}. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal microduplication involving HSD17B10 and HUWE1 has been found in patients with mental retardation.; TISSUE SPECIFICITY: Ubiquitously expressed in normal tissues but is overexpressed in neurons affected in AD. {ECO:0000269|PubMed:9338779}.; lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;nasopharynx;placenta;duodenum;kidney;stomach; . 0.40037 0.22329 0.013025609 54.62962963 5.13761 0.19065 HSD17B11 0.000142446252538164 0.650995432583061 0.348862121164401 hydroxysteroid (17-beta) dehydrogenase 11 FUNCTION: Can convert androstan-3-alpha,17-beta-diol (3-alpha- diol) to androsterone in vitro, suggesting that it may participate in androgen metabolism during steroidogenesis. May act by metabolizing compounds that stimulate steroid synthesis and/or by generating metabolites that inhibit it. Has no activity toward DHEA (dehydroepiandrosterone), or A-dione (4-androste-3,17-dione), and only a slight activity toward testosterone to A-dione. Tumor- associated antigen in cutaneous T-cell lymphoma.; . TISSUE SPECIFICITY: Present at high level in steroidogenic cells such as syncytiotrophoblasts, sebaceous gland, Leydig cells, and granulosa cells of the dominant follicle and corpus luteum. In lung, it is detected in the ciliated epithelium and in acini of adult trachea, in bronchioles, but not in alveoli. In the eye, it is detected in the nonpigmented epithelium of the ciliary body and, at lower level, in the inner nuclear layer of the retina (at protein level). Widely expressed. Highly expressed in retina, pancreas, kidney, liver, lung, adrenal, small intestine, ovary and heart. {ECO:0000269|PubMed:10800688, ECO:0000269|PubMed:11165019, ECO:0000269|PubMed:12697717, ECO:0000269|PubMed:9888557}.; lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;endometrium;cochlea;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;hypothalamus;pancreas;lung;cornea;nasopharynx;placenta;kidney;stomach;aorta;thymus; fetal liver;whole blood; 0.16342 0.10655 0.170987912 65.5579146 8.11144 0.29752 HSD17B12 0.00555447777759886 0.97074012400701 0.0237053982153913 hydroxysteroid (17-beta) dehydrogenase 12 FUNCTION: Catalyzes the second of the four reactions of the long- chain fatty acids elongation cycle. This endoplasmic reticulum- bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3- ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May also catalyze the transformation of estrone (E1) into estradiol (E2) and play a role in estrogen formation. {ECO:0000269|PubMed:12482854, ECO:0000269|PubMed:16166196}.; . TISSUE SPECIFICITY: Expressed in most tissues tested. Highly expressed in the ovary and mammary. Expressed in platelets. {ECO:0000269|PubMed:12482854, ECO:0000269|PubMed:16113833, ECO:0000269|PubMed:16166196}.; ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;gum;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;occipital lobe;adipose tissue;hypothalamus;spinal cord;parietal lobe; 0.11055 0.19829 0.060756528 58.52795471 416.42358 4.27110 HSD17B13 0.00195742553870655 0.907985180875317 0.090057393585976 hydroxysteroid (17-beta) dehydrogenase 13 . . TISSUE SPECIFICITY: Highly expressed in the liver. Also detected in ovary, bone marrow, kidney, brain, lung, skeletal muscle, bladder and testis. {ECO:0000269|PubMed:17311113}.; unclassifiable (Anatomical System);lung;ovary;islets of Langerhans;placenta;liver;testis;parathyroid;brain; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.16350 0.10834 0.396906589 76.30927105 2759.97613 9.90946 HSD17B14 0.00137252498082087 0.963567036020717 0.0350604389984621 hydroxysteroid (17-beta) dehydrogenase 14 FUNCTION: Has NAD-dependent 17-beta-hydroxysteroid dehydrogenase activity. Converts oestradiol to oestrone. The physiological substrate is not known. Acts on oestradiol and 5-androstene-3- beta,17-beta-diol (in vitro). {ECO:0000269|PubMed:17067289}.; . TISSUE SPECIFICITY: Highly expressed in brain, placenta, liver and kidney. {ECO:0000269|PubMed:10800688, ECO:0000269|PubMed:17067289}.; unclassifiable (Anatomical System);medulla oblongata;heart;ovary;hypothalamus;colon;parathyroid;choroid;skin;retina;uterus;bile duct;lung;endometrium;adrenal gland;epididymis;thyroid;placenta;iris;duodenum;liver;testis;spleen;kidney;brain;mammary gland;stomach; . 0.21207 . 0.927856124 89.70276008 1316.53203 6.82371 HSDL1 0.000929031159036312 0.803894736779607 0.195176232061357 hydroxysteroid dehydrogenase like 1 . . TISSUE SPECIFICITY: Highly expressed in testis and ovary. Also detected in thyroid, spinal cord, adrenal gland, heart, placenta, skeletal muscle, small intestine, colon, spleen, prostate and pancreas. {ECO:0000269|PubMed:12153137, ECO:0000269|PubMed:19026618}.; ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;muscle;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;stomach;peripheral nerve; . 0.21383 0.11171 -0.514264485 21.41424864 1653.96914 7.51747 HSDL2 3.95214567435055e-05 0.834926673509719 0.165033805033537 hydroxysteroid dehydrogenase like 2 FUNCTION: Has apparently no steroid dehydrogenase activity. {ECO:0000269|PubMed:19703561}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12834046}.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;colon;skin;bone marrow;uterus;prostate;endometrium;larynx;bone;pituitary gland;testis;dura mater;germinal center;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;pineal body;spinal cord;urinary;adrenal cortex;blood;lens;skeletal muscle;pancreas;pia mater;lung;nasopharynx;placenta;hippocampus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;fetal liver;tongue;hypothalamus;prefrontal cortex;caudate nucleus; 0.33732 0.11787 0.016664174 55.21939137 450.73811 4.41107 HSF1 0.586374294516982 0.413181557182807 0.000444148300211381 heat shock transcription factor 1 FUNCTION: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. {ECO:0000269|PubMed:11447121, ECO:0000269|PubMed:11583998, ECO:0000269|PubMed:12659875, ECO:0000269|PubMed:12665592, ECO:0000269|PubMed:16278218, ECO:0000269|PubMed:8946918, ECO:0000269|PubMed:9121459, ECO:0000269|PubMed:9535852}.; . . . . 0.11458 0.16496 -0.865195027 10.79853739 350.11867 3.96676 HSF2 0.919340110510229 0.0806555356569034 4.35383286716833e-06 heat shock transcription factor 2 FUNCTION: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.; . . . . 0.48052 0.17427 -0.758599262 13.32861524 24.89099 0.81702 HSF2BP 6.3650365720359e-10 0.0355309115547799 0.964469087808717 heat shock transcription factor 2 binding protein FUNCTION: May be involved in modulating HSF2 activation in testis.; . TISSUE SPECIFICITY: Testis specific.; unclassifiable (Anatomical System);uterus;medulla oblongata;lung;heart;bone;testis;cervix;skin; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.14341 0.10134 -0.358119787 29.16371786 45.29789 1.29238 HSF4 2.50047825950513e-10 0.0747757274204006 0.925224272329552 heat shock transcription factor 4 FUNCTION: DNA-binding protein that specifically binds heat shock promoter elements (HSE). Isoform HSF4A represses transcription while the isoform HSF4B activates transcription. {ECO:0000269|PubMed:16371476}.; DISEASE: Cataract 5, multiple types (CTRCT5) [MIM:116800]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT5 includes infantile, lamellar, zonular, nuclear, anterior polar, stellate, and Marner-type cataracts, among others. Finger malformation is observed in some kindreds. {ECO:0000269|PubMed:12089525, ECO:0000269|PubMed:16876512}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, eye and brain, and at much lower levels in some other tissues. {ECO:0000269|PubMed:12089525}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;lens;uterus;prostate;optic nerve;lung;endometrium;bone;thyroid;placenta;hippocampus;testis;kidney;brain;pineal gland;mammary gland;stomach;peripheral nerve; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.26972 0.12484 -0.26993514 34.59542345 33.20248 1.02677 HSF5 0.741540032327461 0.257962565313985 0.00049740235855384 heat shock transcription factor family member 5 FUNCTION: May act as a transcriptional factor. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;testis; . 0.21248 . 0.018483465 55.44939844 1423.22371 7.04737 HSFX1 . . . heat shock transcription factor family, X-linked 1 . . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:15044259}.; . . . 0.07076 . . . . HSFX2 . . . heat shock transcription factor family, X-linked 2 . . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:15044259}.; . . . 0.07076 . . . . HSFY1 . . . heat shock transcription factor, Y-linked 1 . . TISSUE SPECIFICITY: Testis-specific. Present in Sertoli cells and spermatogenic cells (at protein level). {ECO:0000269|PubMed:12815422, ECO:0000269|PubMed:15044259}.; unclassifiable (Anatomical System);lung;testis;kidney; . 0.08420 . . . . . HSFY1P1 . . . heat shock transcription factor, Y-linked 1 pseudogene 1 . . . . . . . . . . . HSFY2 . . . heat shock transcription factor, Y-linked 2 . . TISSUE SPECIFICITY: Testis-specific. Present in Sertoli cells and spermatogenic cells (at protein level). {ECO:0000269|PubMed:12815422, ECO:0000269|PubMed:15044259}.; unclassifiable (Anatomical System);lung;testis;kidney; . . . . . . . HSFY3P . . . heat shock transcription factor, Y-linked 3, pseudogene . . . . . . . . . . . HSFY4P . . . heat shock transcription factor, Y-linked 4, pseudogene . . . . . . . . . . . HSFY5P . . . heat shock transcription factor, Y-linked 5, pseudogene . . . . . . . . . . . HSFY6P . . . heat shock transcription factor, Y-linked 6, pseudogene . . . . . . . . . . . HSFY7P . . . heat shock transcription factor, Y-linked 7, pseudogene . . . . . . . . . . . HSFY8P . . . heat shock transcription factor, Y-linked 8, pseudogene . . . . . . . . . . . HSH2D . . . hematopoietic SH2 domain containing FUNCTION: May be a modulator of the apoptotic response through its ability to affect mitochondrial stability (By similarity). Adapter protein involved in tyrosine kinase and CD28 signaling. Seems to affect CD28-mediated activation of the RE/AP element of the interleukin-2 promoter. {ECO:0000250, ECO:0000269|PubMed:11700021, ECO:0000269|PubMed:12960172, ECO:0000269|PubMed:15284240}.; . TISSUE SPECIFICITY: Predominantly expressed in spleen and hematopoietic cells such as peripheral blood leukocytes and weakly expressed in prostate, thymus, heart, small intestine and placenta. {ECO:0000269|PubMed:11700021, ECO:0000269|PubMed:12960172}.; unclassifiable (Anatomical System);lymph node;umbilical cord;colon;blood;bone marrow;uterus;pancreas;prostate;placenta;spleen;germinal center;stomach; ciliary ganglion;white blood cells; 0.08615 0.12976 . . 39.37363 1.16422 HSP90AA1 0.676747646700996 0.323244212940672 8.14035833203779e-06 heat shock protein 90kDa alpha family class A member 1 FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. {ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:15937123}.; . . lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;bladder;brain;heart;cartilage;tongue;pineal body;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;placenta;kidney;stomach;aorta; amygdala;medulla oblongata;thalamus;occipital lobe;testis - interstitial;olfactory bulb;hypothalamus;pons;caudate nucleus;atrioventricular node;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; . . -1.015898037 8.144609578 90.4171 2.04609 HSP90AA2P . . . heat shock protein 90kDa alpha family class A member 2, pseudogene FUNCTION: Putative molecular chaperone that may promote the maturation, structural maintenance and proper regulation of specific target proteins. {ECO:0000250}.; . . . . . . . . . . HSP90AA3P . . . heat shock protein 90kDa alpha family class A member 3, pseudogene . . . . . . . . . . . HSP90AA4P . . . heat shock protein 90kDa alpha family class A member 4, pseudogene FUNCTION: Putative molecular chaperone that may promote the maturation, structural maintenance and proper regulation of specific target proteins. {ECO:0000250}.; . . . . . . . . . . HSP90AA5P . . . heat shock protein 90kDa alpha family class A member 5, pseudogene FUNCTION: Putative molecular chaperone that may promote the maturation, structural maintenance and proper regulation of specific target proteins. {ECO:0000250}.; . . . . . . . . . . HSP90AA6P . . . heat shock protein 90kDa alpha family class A member 6, pseudogene . . . . . 0.12837 . . . . . HSP90AB1 0.99529931563779 0.00470059099397846 9.33682314406571e-08 heat shock protein 90kDa alpha family class B member 1 FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. {ECO:0000269|PubMed:16478993, ECO:0000269|PubMed:19696785}.; . . lymphoreticular;ovary;salivary gland;colon;skin;retina;uterus;prostate;frontal lobe;endometrium;larynx;bone;iris;testis;brain;artery;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;tongue;spinal cord;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; medulla oblongata;thalamus;subthalamic nucleus;occipital lobe;cerebellum peduncles;temporal lobe;globus pallidus;pons;parietal lobe;skeletal muscle;cingulate cortex;cerebellum; 0.17451 0.26816 -1.265702118 5.237084218 20.0367 0.68400 HSP90AB2P . . . heat shock protein 90kDa alpha family class B member 2, pseudogene FUNCTION: Putative molecular chaperone that may promote the maturation, structural maintenance and proper regulation of specific target proteins. {ECO:0000250}.; . . . . . . . . . . HSP90AB3P . . . heat shock protein 90kDa alpha family class B member 3, pseudogene FUNCTION: Putative molecular chaperone that may promote the maturation, structural maintenance and proper regulation of specific target proteins. {ECO:0000250}.; . . . . 0.13318 . . . . . HSP90AB4P . . . heat shock protein 90kDa alpha family class B member 4, pseudogene FUNCTION: Putative molecular chaperone that may promote the maturation, structural maintenance and proper regulation of specific target proteins. {ECO:0000250}.; . . . . 0.20153 . . . . . HSP90AB5P . . . heat shock protein 90kDa alpha family class B member 5, pseudogene . . . . . . . . . . . HSP90AB6P . . . heat shock protein 90kDa alpha family class B member 6, pseudogene . . . . . . . . . . . HSP90AB7P . . . heat shock protein 90kDa alpha family class B member 7, pseudogene . . . . . . . . . . . HSP90B1 0.987843128807057 0.0121568632797216 7.91322146686302e-09 heat shock protein 90kDa beta family member 1 FUNCTION: Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. {ECO:0000250, ECO:0000269|PubMed:18264092}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;bile duct;breast;lung;adrenal gland;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; smooth muscle;thyroid;white blood cells; 0.85829 0.42920 -0.356299879 29.31115829 1011.50807 6.12533 HSP90B2P . . . heat shock protein 90kDa beta family member 2, pseudogene FUNCTION: Putative molecular chaperone. {ECO:0000250}.; . . . . 0.23028 0.12579 -0.338129542 30.07784855 . . HSP90B3P . . . heat shock protein 90kDa beta family member 3, pseudogene . . . . . . . . . . . HSPA1A . . . heat shock protein family A (Hsp70) member 1A FUNCTION: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). {ECO:0000269|PubMed:16537599, ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23973223}.; . . . . 0.50161 . . . 1907.06868 8.03903 HSPA1B . . . heat shock protein family A (Hsp70) member 1B FUNCTION: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). {ECO:0000269|PubMed:16537599, ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23973223}.; . TISSUE SPECIFICITY: HSPA1B is testis-specific.; . . 0.61105 . . . 619.532 5.02167 HSPA1L 2.19040919542089e-06 0.27810907648359 0.721888733107215 heat shock protein family A (Hsp70) member 1 like FUNCTION: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity). Positive regulator of PARK2 translocation to damaged mitochondria. {ECO:0000250, ECO:0000269|PubMed:24270810}.; . TISSUE SPECIFICITY: Expressed in spermatids. {ECO:0000269|PubMed:9685725}.; . . 0.52721 . -0.110153916 45.48832272 2435.22546 9.16759 HSPA2 . . . heat shock protein family A (Hsp70) member 2 FUNCTION: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage.; . . ovary;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;pituitary gland;testis;ciliary body;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;adrenal cortex;blood;lens;bile duct;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;hypopharynx;amnion;spleen;head and neck;kidney;mammary gland;stomach; whole brain;amygdala;occipital lobe;medulla oblongata;testis - interstitial;superior cervical ganglion;thalamus;olfactory bulb;hypothalamus;spinal cord;caudate nucleus;pons;testis - seminiferous tubule;prefrontal cortex;testis;kidney;cingulate cortex;parietal lobe; 0.63859 . 0.130533008 63.35810333 148.46704 2.65691 HSPA4 0.999958225713848 4.1774285963053e-05 1.89190963125037e-13 heat shock protein family A (Hsp70) member 4 . . . lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach;thymus; testis - interstitial;testis - seminiferous tubule;testis;cingulate cortex; 0.98265 0.95217 -0.154246007 42.22694032 307.12317 3.72927 HSPA4L 0.0300111206441728 0.969971487776037 1.73915797902492e-05 heat shock protein family A (Hsp70) member 4 like FUNCTION: Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase. {ECO:0000250}.; . . unclassifiable (Anatomical System);pineal body;fovea centralis;skeletal muscle;uterus;whole body;lung;frontal lobe;thyroid;macula lutea;visual apparatus;liver;testis;cervix;kidney;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.63233 0.16248 0.244401822 69.50931824 741.29995 5.40585 HSPA5 0.885688897994033 0.114258079592226 5.30224137407905e-05 heat shock protein family A (Hsp70) member 5 FUNCTION: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate. {ECO:0000269|PubMed:2294010, ECO:0000269|PubMed:23769672, ECO:0000269|PubMed:23990668}.; DISEASE: Note=Autoantigen in rheumatoid arthritis. {ECO:0000269|PubMed:11160188}.; . myocardium;smooth muscle;ovary;colon;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;oesophagus;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;blood;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; fetal liver;olfactory bulb;placenta;thyroid;testis;pituitary; 0.80324 0.96597 -0.249709319 35.74545883 36.2231 1.08539 HSPA6 0.461296068531822 0.512795530548354 0.0259084009198241 heat shock protein family A (Hsp70) member 6 FUNCTION: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;colon;fovea centralis;choroid;lens;skin;retina;uterus;breast;prostate;optic nerve;lung;endometrium;bone;placenta;macula lutea;alveolus;kidney;brain;bladder;thymus; . 0.19157 . -0.020150552 52.25288983 2672.98543 9.72218 HSPA7 . . . heat shock protein family A (Hsp70) member 7 . . . . . . . . . . . HSPA8 0.997882601177929 0.00211733293356035 6.5888510104962e-08 heat shock protein family A (Hsp70) member 8 FUNCTION: Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19- CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase CHIP. {ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:23990462}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11276205}.; ovary;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;cerebellum cortex;islets of Langerhans;pineal body;urinary;adrenal cortex;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;alveolus;liver;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; . 0.99996 0.92706 -0.824740496 11.67728238 5.99029 0.22489 HSPA8P1 . . . heat shock protein family A (Hsp70) member 8 pseudogene 1 . . . . . . . . . . . HSPA8P2 . . . heat shock protein family A (Hsp70) member 8 pseudogene 2 . . . . . . . . . . . HSPA8P3 . . . heat shock protein family A (Hsp70) member 8 pseudogene 3 . . . . . . . . . . . HSPA8P4 . . . heat shock protein family A (Hsp70) member 8 pseudogene 4 . . . . . . . . . . . HSPA8P5 . . . heat shock protein family A (Hsp70) member 8 pseudogene 5 . . . . . . . . . . . HSPA8P6 . . . heat shock protein family A (Hsp70) member 8 pseudogene 6 . . . . . . . . . . . HSPA8P7 . . . heat shock protein family A (Hsp70) member 8 pseudogene 7 . . . . . . . . . . . HSPA8P8 . . . heat shock protein family A (Hsp70) member 8 pseudogene 8 . . . . . . . . . . . HSPA8P9 . . . heat shock protein family A (Hsp70) member 8 pseudogene 9 . . . . . . . . . . . HSPA8P10 . . . heat shock protein family A (Hsp70) member 8 pseudogene 10 . . . . . . . . . . . HSPA8P11 . . . heat shock protein family A (Hsp70) member 8 pseudogene 11 . . . . . . . . . . . HSPA8P12 . . . heat shock protein family A (Hsp70) member 8 pseudogene 12 . . . . . . . . . . . HSPA8P13 . . . heat shock protein family A (Hsp70) member 8 pseudogene 13 . . . . . . . . . . . HSPA8P14 . . . heat shock protein family A (Hsp70) member 8 pseudogene 14 . . . . . . . . . . . HSPA8P15 . . . heat shock protein family A (Hsp70) member 8 pseudogene 15 . . . . . . . . . . . HSPA8P16 . . . heat shock protein family A (Hsp70) member 8 pseudogene 16 . . . . . . . . . . . HSPA8P17 . . . heat shock protein family A (Hsp70) member 8 pseudogene 17 . . . . . . . . . . . HSPA8P18 . . . heat shock protein family A (Hsp70) member 8 pseudogene 18 . . . . . . . . . . . HSPA8P19 . . . heat shock protein family A (Hsp70) member pseudogene 19 . . . . . . . . . . . HSPA8P20 . . . heat shock protein family A (Hsp70) member 8 pseudogene 20 . . . . . . . . . . . HSPA9 0.981119322463888 0.0188806541837 2.33524119712582e-08 heat shock protein family A (Hsp70) member 9 FUNCTION: Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone. {ECO:0000269|PubMed:23501103}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;muscle;pancreas;lung;cornea;placenta;duodenum;head and neck;kidney;stomach; thalamus;occipital lobe;superior cervical ganglion;hypothalamus;pons;parietal lobe;cingulate cortex;skeletal muscle; 0.62414 0.73410 -0.846787714 11.05803255 21.59412 0.72579 HSPA9P1 . . . heat shock protein family A (Hsp70) member 9 pseudogene 1 . . . . . . . . . . . HSPA9P2 . . . heat shock protein family A (Hsp70) member 9 pseudogene 2 . . . . . . . . . . . HSPA12A 0.980307172080411 0.0196921952377186 6.32681870100134e-07 heat shock protein family A (Hsp70) member 12A . . TISSUE SPECIFICITY: Widely expressed with highest levels in brain, kidney and muscle. {ECO:0000269|PubMed:12552099}.; . . 0.17546 0.15354 -0.663133267 15.94715735 103.51783 2.19811 HSPA12B 0.0105082037359554 0.987489741322837 0.00200205494120735 heat shock protein family A (Hsp70) member 12B . . TISSUE SPECIFICITY: Highest expression in muscle and heart. Lower levels in liver and kidney. {ECO:0000269|PubMed:12552099}.; unclassifiable (Anatomical System);lung;ovary;heart;cerebral cortex;bone;placenta;urinary;kidney; . 0.13074 0.12119 . . 622.34303 5.03015 HSPA13 0.00188636989282119 0.904126003605997 0.0939876265011814 heat shock protein family A (Hsp70) member 13 FUNCTION: Has peptide-independent ATPase activity.; . TISSUE SPECIFICITY: Constitutively expressed in all tissues.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;cervix;kidney;mammary gland;aorta;stomach; amygdala;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.24388 0.14306 -0.159704656 41.90846898 38.77166 1.14770 HSPA14 0.991685161782873 0.00831476202549471 7.61916324292553e-08 heat shock protein family A (Hsp70) member 14 FUNCTION: Component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity. {ECO:0000269|PubMed:16002468}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;whole body;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);tongue;pharynx;blood;breast;lung;cornea;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;hypothalamus;prefrontal cortex;testis;tumor;white blood cells;trigeminal ganglion; 0.34695 0.13081 -0.448125345 24.19202642 125.6653 2.44089 HSPB1 6.92483241362485e-06 0.157295070270267 0.842698004897319 heat shock protein family B (small) member 1 FUNCTION: Involved in stress resistance and actin organization.; DISEASE: Charcot-Marie-Tooth disease 2F (CMT2F) [MIM:606595]: A dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. Onset of Charcot-Marie-Tooth disease type 2F is between 15 and 25 years with muscle weakness and atrophy usually beginning in feet and legs (peroneal distribution). Upper limb involvement occurs later. {ECO:0000269|PubMed:15122254, ECO:0000269|PubMed:22206013}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Neuronopathy, distal hereditary motor, 2B (HMN2B) [MIM:608634]: A neuromuscular disorder. Distal hereditary motor neuronopathies constitute a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. {ECO:0000269|PubMed:15122254}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in all tissues tested: skeletal muscle, heart, aorta, large intestine, small intestine, stomach, esophagus, bladder, adrenal gland, thyroid, pancreas, testis, adipose tissue, kidney, liver, spleen, cerebral cortex, blood serum and cerebrospinal fluid. Highest levels are found in the heart and in tissues composed of striated and smooth muscle. {ECO:0000269|PubMed:1560006}.; ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;uterus;prostate;endometrium;bone;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach; prostate;heart;tongue;placenta;skeletal muscle; 0.49765 0.79641 . . 15.14355 0.54485 HSPB1P1 . . . heat shock protein family B (small) member 1 pseudogene 1 . . . . . . . . . . . HSPB1P2 . . . heat shock protein family B (small) member 1 pseudogene 2 . . . . . . . . . . . HSPB2 0.211781189194987 0.748006748875643 0.0402120619293699 heat shock protein family B (small) member 2 FUNCTION: May regulate the kinase DMPK. {ECO:0000269|PubMed:9490724}.; . TISSUE SPECIFICITY: Expressed preferentially in skeletal muscle and heart but not in the lens.; . . 0.55740 . 0.014844891 54.94810097 40.23425 1.18255 HSPB2-C11orf52 . . . HSPB2-C11orf52 readthrough (NMD candidate) . . . . . . . . . . . HSPB3 0.000440374165595957 0.420011123317178 0.579548502517226 heat shock protein family B (small) member 3 FUNCTION: Inhibitor of actin polymerization.; DISEASE: Neuronopathy, distal hereditary motor, 2C (HMN2C) [MIM:613376]: A neuromuscular disorder. Distal hereditary motor neuronopathies constitute a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. {ECO:0000269|PubMed:20142617}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . heart;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;optic nerve;whole body;lung;synovium;macula lutea;alveolus; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.17853 0.10255 -0.117432389 44.89266336 33.16744 1.02621 HSPB6 0.391248531059943 0.474495630720869 0.134255838219188 heat shock protein family B (small) member 6 . . . myocardium;smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;larynx;thyroid;bone;testis;brain;pineal gland;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;epididymis;trabecular meshwork;placenta;macula lutea;visual apparatus;spleen;head and neck;kidney;mammary gland;stomach; heart;atrioventricular node;skeletal muscle; 0.20112 0.17491 . . 48.79034 1.36262 HSPB7 0.013149236960213 0.661122194446331 0.325728568593456 heat shock protein family B (small) member 7 . . TISSUE SPECIFICITY: Isoform 1 is highly expressed in adult and fetal heart, skeletal muscle, and at a much lower levels in adipose tissue and in aorta. Undetectable in other tissues. Isoform 2 and isoform 3 are poorly detected in heart.; myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;thyroid;bone;iris;testis;unclassifiable (Anatomical System);heart;cartilage;tongue;muscle;adrenal cortex;skeletal muscle;greater omentum;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;head and neck;kidney;mammary gland; heart;ciliary ganglion;skeletal muscle; 0.16053 0.15049 -0.183570861 39.95046001 531.27716 4.70270 HSPB8 0.0277554701284337 0.796712969802447 0.175531560069119 heat shock protein family B (small) member 8 FUNCTION: Displays temperature-dependent chaperone activity.; DISEASE: Neuronopathy, distal hereditary motor, 2A (HMN2A) [MIM:158590]: A neuromuscular disorder. Distal hereditary motor neuronopathies constitute a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. {ECO:0000269|PubMed:15122253}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease 2L (CMT2L) [MIM:608673]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. {ECO:0000269|PubMed:15565283}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and heart. {ECO:0000269|PubMed:11470154}.; myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;nervous;tongue;islets of Langerhans;hypothalamus;pineal body;spinal cord;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;aorta; amygdala;whole brain;thalamus;hypothalamus;placenta;spinal cord;prefrontal cortex;caudate nucleus;skeletal muscle; 0.55644 0.22085 0.215080721 67.91696155 44.12462 1.26645 HSPB9 5.41472479924188e-05 0.14334088265776 0.856604970094247 heat shock protein family B (small) member 9 . . TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:11470154}.; unclassifiable (Anatomical System);lung;islets of Langerhans;testis; . 0.12376 . 0.571462851 81.99457419 1997.96313 8.23568 HSPB11 0.00497874000170344 0.694910565027313 0.300110694970984 heat shock protein family B (small) member 11 FUNCTION: Component of the IFT complex B required for sonic hedgehog/SHH signaling. May mediate transport of SHH components: required for the export of SMO and PTCH1 receptors out of the cilium and the accumulation of GLI2 at the ciliary tip in response to activation of the SHH pathway, suggesting it is involved in the dynamic transport of SHH signaling molecules within the cilium. Not required for ciliary assembly (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in placenta. {ECO:0000269|PubMed:2018407}.; unclassifiable (Anatomical System);heart;tongue;hypothalamus;parathyroid;uterus;pancreas;prostate;lung;placenta;liver;testis;kidney;brain;aorta;stomach; amygdala;superior cervical ganglion;thyroid;testis;tumor; 0.11958 0.13601 0.169169615 65.33380514 4983.07578 14.40678 HSPBAP1 9.97537509364561e-07 0.77524523976688 0.22475376269561 HSPB1 associated protein 1 FUNCTION: May play a role in cellular stress response. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11978969}.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;lung;endometrium;bone;thyroid;placenta;visual apparatus;testis;cervix;spleen;germinal center;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;testis; 0.07229 0.08631 0.50895761 80.20169851 1771.10273 7.77441 HSPBP1 0.00948086162359598 0.94022041985099 0.0502987185254143 HSPA (heat shock 70kDa) binding protein, cytoplasmic cochaperone 1 FUNCTION: Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR. {ECO:0000269|PubMed:10786638, ECO:0000269|PubMed:12651857, ECO:0000269|PubMed:15215316, ECO:0000269|PubMed:9830037}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9830037}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;muscle;lens;bile duct;pancreas;lung;placenta;macula lutea;hippocampus;liver;hypopharynx;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;whole brain;prefrontal cortex;caudate nucleus;atrioventricular node; . 0.13057 -0.181750739 40.15687662 90.81976 2.05036 HSPD1 0.985208243840261 0.01479021032679 1.54583294922653e-06 heat shock protein family D (Hsp60) member 1 FUNCTION: Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix.; DISEASE: Spastic paraplegia 13, autosomal dominant (SPG13) [MIM:605280]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. {ECO:0000269|PubMed:11898127}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leukodystrophy, hypomyelinating, 4 (HLD4) [MIM:612233]: A severe autosomal recessive hypomyelinating leukodystrophy. Clinically characterized by infantile-onset rotary nystagmus, progressive spastic paraplegia, neurologic regression, motor impairment, profound mental retardation. Death usually occurs within the first two decades of life. {ECO:0000269|PubMed:18571143}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;oesophagus;endometrium;larynx;bone;thyroid;testis;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;pia mater;lung;cornea;adrenal gland;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; . 0.97860 0.98090 -0.203796826 38.81811748 89.54005 2.03508 HSPD1P1 . . . heat shock protein family D (Hsp60) member 1 pseudogene 1 . . . . . . . . . . . HSPD1P2 . . . heat shock protein family D (Hsp60) member 1 pseudogene 2 . . . . . . . . . . . HSPD1P3 . . . heat shock protein family D (Hsp60) member 1 pseudogene 3 . . . . . . . . . . . HSPD1P4 . . . heat shock protein family D (Hsp60) member 1 pseudogene 4 . . . . . . . . . . . HSPD1P5 . . . heat shock protein family D (Hsp60) member 1 pseudogene 5 . . . . . . . . . . . HSPD1P6 . . . heat shock protein family D (Hsp60) member 1 pseudogene 6 . . . . . . . . . . . HSPD1P7 . . . heat shock protein family D (Hsp60) member 1 pseudogene 7 . . . . . . . . . . . HSPD1P8 . . . heat shock protein family D (Hsp60) member 1 pseudogene 8 . . . . . . . . . . . HSPD1P9 . . . heat shock protein family D (Hsp60) member 1 pseudogene 9 . . . . . . . . . . . HSPD1P10 . . . heat shock protein family D (Hsp60) member 1 pseudogene 10 . . . . . . . . . . . HSPD1P11 . . . heat shock protein family D (Hsp60) member 1 pseudogene 11 . . . . . . . . . . . HSPD1P12 . . . heat shock protein family D (Hsp60) member 1 pseudogene 12 . . . . . . . . . . . HSPD1P13 . . . heat shock protein family D (Hsp60) member 1 pseudogene 13 . . . . . . . . . . . HSPD1P14 . . . heat shock protein family D (Hsp60) member 1 pseudogene 14 . . . . . . . . . . . HSPD1P15 . . . heat shock protein family D (Hsp60) member 1 pseudogene 15 . . . . . . . . . . . HSPD1P16 . . . heat shock protein family D (Hsp60) member 1 pseudogene 16 . . . . . . . . . . . HSPD1P17 . . . heat shock protein family D (Hsp60) member 1 pseudogene 17 . . . . . . . . . . . HSPD1P18 . . . heat shock protein family D (Hsp60) member 1 pseudogene 18 . . . . . . . . . . . HSPD1P19 . . . heat shock protein family D (Hsp60) member 1 pseudogene 19 . . . . . . . . . . . HSPD1P20 . . . heat shock protein family D (Hsp60) member 1 pseudogene 20 . . . . . . . . . . . HSPD1P21 . . . heat shock protein family D (Hsp60) member 1 pseudogene 21 . . . . . . . . . . . HSPD1P22 . . . heat shock protein family D (Hsp60) member 1 pseudogene 22 . . . . . . . . . . . HSPE1 0.787528047849985 0.206027426379775 0.00644452577024023 heat shock protein family E (Hsp10) member 1 FUNCTION: Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.; . . lymphoreticular;ovary;rectum;skin;bone marrow;retina;prostate;cochlea;endometrium;amniotic fluid;bladder;brain;heart;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;placenta;duodenum;kidney;stomach; adrenal gland;adrenal cortex;globus pallidus; 0.65407 0.50749 0.035072054 56.2514744 1.20885 0.03769 HSPE1-MOB4 0.889798357973135 0.109964524728057 0.000237117298807801 HSPE1-MOB4 readthrough . . . . . . . . . 1.21425 0.03926 HSPE1P1 . . . heat shock protein family E (Hsp10) member 1 pseudogene 1 . . . . . . . . . . . HSPE1P2 . . . heat shock protein family E (Hsp10) member 1 pseudogene 2 . . . . . . . . . . . HSPE1P3 . . . heat shock protein family E (Hsp10) member 1 pseudogene 3 . . . . . . . . . . . HSPE1P4 . . . heat shock protein family E (Hsp10) member 1 pseudogene 4 . . . . . . . . . . . HSPE1P5 . . . heat shock protein family E (Hsp10) member 1 pseudogene 5 . . . . . . . . . . . HSPE1P6 . . . heat shock protein family E (Hsp10) member 1 pseudogene 6 . . . . . . . . . . . HSPE1P7 . . . heat shock protein family E (Hsp10) member 1 pseudogene 7 . . . . . . . . . . . HSPE1P8 . . . heat shock protein family E (Hsp10) member 1 pseudogene 8 . . . . . . . . . . . HSPE1P9 . . . heat shock protein family E (Hsp10) member 1 pseudogene 9 . . . . . . . . . . . HSPE1P10 . . . heat shock protein family E (Hsp10) member 1 pseudogene 10 . . . . . . . . . . . HSPE1P11 . . . heat shock protein family E (Hsp10) member 1 pseudogene 11 . . . . . . . . . . . HSPE1P12 . . . heat shock protein family E (Hsp10) member 1 pseudogene 12 . . . . . . . . . . . HSPE1P13 . . . heat shock protein family E (Hsp10) member 1 pseudogene 13 . . . . . . . . . . . HSPE1P14 . . . heat shock protein family E (Hsp10) member 1 pseudogene 14 . . . . . . . . . . . HSPE1P15 . . . heat shock protein family E (Hsp10) member 1 pseudogene 15 . . . . . . . . . . . HSPE1P16 . . . heat shock protein family E (Hsp10) member 1 pseudogene 16 . . . . . . . . . . . HSPE1P17 . . . heat shock protein family E (Hsp10) member 1 pseudogene 17 . . . . . . . . . . . HSPE1P18 . . . heat shock protein family E (Hsp10) member 1 pseudogene 18 . . . . . . . . . . . HSPE1P19 . . . heat shock protein family E (Hsp10) member 1 pseudogene 19 . . . . . . . . . . . HSPE1P20 . . . heat shock protein family E (Hsp10) member 1 pseudogene 20 . . . . . . . . . . . HSPE1P21 . . . heat shock protein family E (Hsp10) member 1 pseudogene 21 . . . . . . . . . . . HSPE1P22 . . . heat shock protein family E (Hsp10) member 1 pseudogene 22 . . . . . . . . . . . HSPE1P23 . . . heat shock protein family E (Hsp10) member 1 pseudogene 23 . . . . . . . . . . . HSPE1P24 . . . heat shock protein family E (Hsp10) member 1 pseudogene 24 . . . . . . . . . . . HSPE1P25 . . . heat shock protein family E (Hsp10) member 1 pseudogene 25 . . . . . . . . . . . HSPE1P26 . . . heat shock protein family E (Hsp10) member 1 pseudogene 26 . . . . . . . . . . . HSPE1P27 . . . heat shock protein family E (Hsp10) member 1 pseudogene 27 . . . . . . . . . . . HSPE1P28 . . . heat shock protein family E (Hsp10) member 1 pseudogene 28 . . . . . . . . . . . HSPG2 6.94653656591348e-06 0.999993053463434 3.92259702663149e-23 heparan sulfate proteoglycan 2 FUNCTION: Integral component of basement membranes. Component of the glomerular basement membrane (GBM), responsible for the fixed negative electrostatic membrane charge, and which provides a barrier which is both size- and charge-selective. It serves as an attachment substrate for cells. Plays essential roles in vascularization. Critical for normal heart development and for regulating the vascular response to injury. Also required for avascular cartilage development.; FUNCTION: The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity.; DISEASE: Schwartz-Jampel syndrome (SJS1) [MIM:255800]: Rare autosomal recessive disorder characterized by permanent myotonia (prolonged failure of muscle relaxation) and skeletal dysplasia, resulting in reduced stature, kyphoscoliosis, bowing of the diaphyses and irregular epiphyses. {ECO:0000269|PubMed:11101850}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dyssegmental dysplasia Silverman-Handmaker type (DDSH) [MIM:224410]: The dyssegmental dysplasias are rare, autosomal recessive skeletal dysplasias with anisospondyly and micromelia. There are two recognized types: the severe, lethal DDSH and the milder Rolland-Desbuquois form. Individuals with DDSH also have a flat face, micrognathia, cleft palate and reduced joint mobility, and frequently have an encephalocoele. The endochondral growth plate is short, the calcospherites (which are spherical calcium- phosphorus crystals produced by hypertrophic chondrocytes) are unfused, and there is mucoid degeneration of the resting cartilage. {ECO:0000269|PubMed:11279527}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in the basement membranes.; . . 0.82995 0.69487 -0.310545309 32.0653456 6624.11904 17.19616 HSPH1 0.983009121355496 0.0169908749998278 3.64467656799966e-09 heat shock protein family H (Hsp110) member 1 FUNCTION: Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in testis. Present at lower levels in most brain regions, except cerebellum. Overexpressed in cancer cells. {ECO:0000269|PubMed:10865058, ECO:0000269|PubMed:16232202}.; lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;ganglion;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;spinal cord;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;oral cavity;pancreas;pia mater;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; amygdala;testis - interstitial;occipital lobe;thalamus;medulla oblongata;hypothalamus;pons;atrioventricular node;caudate nucleus;subthalamic nucleus;testis - seminiferous tubule;fetal brain;prefrontal cortex;globus pallidus;testis;ciliary ganglion;cingulate cortex;parietal lobe; 0.83318 0.34606 -0.573127851 18.96083982 114.40364 2.33050 HTATIP2 3.64419690390924e-12 0.00330864413719737 0.996691355859158 HIV-1 Tat interactive protein 2 FUNCTION: Oxidoreductase required for tumor suppression. NAPDH- bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import. Isoform 1 is a metastasis suppressor with proapoptotic as well as antiangiogenic properties. Isoform 2 has an antiapoptotic effect. {ECO:0000269|PubMed:10611237, ECO:0000269|PubMed:11313954, ECO:0000269|PubMed:15282309, ECO:0000269|PubMed:9174052}.; . TISSUE SPECIFICITY: Ubiquitous. Highest level in liver. High levels in lung, skeletal muscle, pancreas and placenta. Moderate levels in heart and kidney. Low levels in brain. Not expressed or low levels in variant small cell lung carcinomas, 33% of hepatocellular carcinomas and neuroblastomas. {ECO:0000269|PubMed:14695192, ECO:0000269|PubMed:9174052}.; . . 0.19697 0.17580 -0.161524709 41.6430762 95.40073 2.10806 HTATSF1 0.973206628172388 0.0267866866266527 6.68520095942759e-06 HIV-1 Tat specific factor 1 FUNCTION: Functions as a general transcription factor playing a role in the process of transcriptional elongation. May mediate the reciprocal stimulatory effect of splicing on transcriptional elongation. In case of infection by HIV-1, it is up-regulated by the HIV-1 proteins NEF and gp120, acts as a cofactor required for the Tat-enhanced transcription of the virus. {ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:10913173, ECO:0000269|PubMed:11420046, ECO:0000269|PubMed:11780068, ECO:0000269|PubMed:15905670, ECO:0000269|PubMed:8849451, ECO:0000269|PubMed:9765201}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8849451}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;adrenal cortex;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; amygdala;hypothalamus;prefrontal cortex;testis;pons;caudate nucleus;skeletal muscle;pituitary;parietal lobe; 0.48424 0.13421 -0.025608647 51.91672564 23.70635 0.78391 HTATSF1P1 . . . HIV-1 Tat specific factor 1 pseudogene 1 . . . . . . . . . . . HTATSF1P2 . . . HIV-1 Tat specific factor 1 pseudogene 2 . . . . . . . . . . . HTC1 . . . hypertrichosis 1 (universalis, congenital) . . . . . . . . . . . HTC2 . . . hypertrichosis 2 (generalized, congenital) . . . . . . . . . . . HTL . . . high L-leucine transport . . . . . . . . . . . HTN1 0.00180851969959408 0.479061699762907 0.519129780537499 histatin 1 FUNCTION: Histatins are salivary proteins that are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). In addition, histatins exhibit antibacterial and antifungal activities.; . TISSUE SPECIFICITY: Submandibular and parotid glands. {ECO:0000269|PubMed:17503797}.; unclassifiable (Anatomical System);adrenal gland;salivary gland;thyroid;adrenal cortex;liver;parotid gland;testis;parathyroid;pineal gland;skeletal muscle; thalamus;prostate;superior cervical ganglion;trachea;salivary gland;thyroid;trigeminal ganglion; 0.02874 . 0.501689326 79.7888653 88.03901 2.00714 HTN3 0.000271792557384507 0.334440019107591 0.665288188335025 histatin 3 FUNCTION: Histatins are salivary proteins that are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). In addition, histatins exhibit antibacterial and antifungal activities. His3-(20-43)-peptide (histatin-5) is especially effective against C.albicans and C.neoformans, and inhibits Lys-gingipain and Arg-gingipain (rgpB) from P.gingivalis. In addition, His3-(20-43)-peptide is a potent inhibitor of metalloproteinases MMP2 and MMP9. {ECO:0000269|PubMed:11179305, ECO:0000269|PubMed:8945538}.; . . . . 0.05055 . 0.946276448 89.90917669 563.86704 4.82102 HTOR . . . 5-hydroxytryptamine (serotonin) oxygenase regulator . . . . . . . . . . . HTR1A 0.926694462856279 0.0728994010827003 0.000406136061021046 5-hydroxytryptamine receptor 1A FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling inhibits adenylate cyclase activity and activates a phosphatidylinositol-calcium second messenger system that regulates the release of Ca(2+) ions from intracellular stores. Plays a role in the regulation of 5- hydroxytryptamine release and in the regulation of dopamine and 5- hydroxytryptamine metabolism. Plays a role in the regulation of dopamine and 5-hydroxytryptamine levels in the brain, and thereby affects neural activity, mood and behavior. Plays a role in the response to anxiogenic stimuli. {ECO:0000269|PubMed:22957663, ECO:0000269|PubMed:3138543, ECO:0000269|PubMed:8138923, ECO:0000269|PubMed:8393041}.; . TISSUE SPECIFICITY: Detected in lymph nodes, thymus and spleen. Detected in activated T-cells, but not in resting T-cells. {ECO:0000269|PubMed:3041227, ECO:0000269|PubMed:8393041}.; unclassifiable (Anatomical System); superior cervical ganglion;liver;atrioventricular node; 0.49665 0.20425 -0.203796826 38.81811748 80.44881 1.89474 HTR1B 0.645559516982246 0.348211647205362 0.00622883581239247 5-hydroxytryptamine receptor 1B FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for ergot alkaloid derivatives, various anxiolytic and antidepressant drugs and other psychoactive substances, such as lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries. {ECO:0000269|PubMed:10452531, ECO:0000269|PubMed:1315531, ECO:0000269|PubMed:1328844, ECO:0000269|PubMed:1348246, ECO:0000269|PubMed:1351684, ECO:0000269|PubMed:1559993, ECO:0000269|PubMed:1565658, ECO:0000269|PubMed:15853772, ECO:0000269|PubMed:1610347, ECO:0000269|PubMed:23519210, ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:8218242}.; . TISSUE SPECIFICITY: Detected in cerebral artery smooth muscle cells (at protein level). Detected in brain cortex, striatum, amygdala, medulla, hippocampus, caudate nucleus and putamen. {ECO:0000269|PubMed:1348246, ECO:0000269|PubMed:1351684, ECO:0000269|PubMed:15853772}.; . . 0.72163 0.10596 -0.404032746 26.53338051 42.10973 1.22680 HTR1D 0.813006424567561 0.182416617433166 0.0045769579992724 5-hydroxytryptamine receptor 1D FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for ergot alkaloid derivatives, various anxiolytic and antidepressant drugs and other psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction. {ECO:0000269|PubMed:10452531, ECO:0000269|PubMed:1565658, ECO:0000269|PubMed:1652050}.; . TISSUE SPECIFICITY: Detected in brain neocortex and caudate nucleus (at protein level). {ECO:0000269|PubMed:1828434}.; unclassifiable (Anatomical System);brain; uterus corpus;superior cervical ganglion;heart;skeletal muscle; 0.51288 0.20991 -0.53631094 20.53550366 120.59949 2.39323 HTR1DP1 . . . 5-hydroxytryptamine receptor 1D pseudogene 1 . . . . . . . . . . . HTR1E 0.0237097657740907 0.772281465608859 0.204008768617051 5-hydroxytryptamine receptor 1E FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. {ECO:0000269|PubMed:14744596, ECO:0000269|PubMed:1513320, ECO:0000269|PubMed:1608964, ECO:0000269|PubMed:1733778, ECO:0000269|PubMed:21422162}.; . TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:14744596}.; unclassifiable (Anatomical System); superior cervical ganglion; 0.24770 0.11928 -0.47017169 23.25430526 42.67993 1.23800 HTR1F 0.00161477471674346 0.693765065016272 0.304620160266985 5-hydroxytryptamine receptor 1F FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. {ECO:0000269|PubMed:21422162, ECO:0000269|PubMed:8380639, ECO:0000269|PubMed:8384716}.; . . unclassifiable (Anatomical System);placenta; superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.44877 0.12230 -0.161524709 41.6430762 26.56929 0.85904 HTR2A 0.772773609936333 0.225555782848426 0.00167060721524143 5-hydroxytryptamine receptor 2A FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including mescaline, psilocybin, 1-(2,5- dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates phospholipase C and a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and promotes the release of Ca(2+) ions from intracellular stores. Affects neural activity, perception, cognition and mood. Plays a role in the regulation of behavior, including responses to anxiogenic situations and psychoactive substances. Plays a role in intestinal smooth muscle contraction, and may play a role in arterial vasoconstriction. {ECO:0000269|PubMed:1330647, ECO:0000269|PubMed:18297054, ECO:0000269|PubMed:18703043, ECO:0000269|PubMed:19057895, ECO:0000269|PubMed:21645528, ECO:0000269|PubMed:22300836}.; . TISSUE SPECIFICITY: Detected in brain cortex (at protein level). Detected in blood platelets. {ECO:0000269|PubMed:18297054}.; . . 0.41435 0.34232 0.440999548 77.79547063 379.02745 4.10511 HTR2A-AS1 . . . HTR2A antisense RNA 1 . . . . . . . . . . . HTR2B 3.66015293333563e-09 0.0969799783202878 0.903020018019559 5-hydroxytryptamine receptor 2B FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various ergot alkaloid derivatives and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and down- stream signaling cascades and promotes the release of Ca(2+) ions from intracellular stores. Plays a role in the regulation of dopamine and 5-hydroxytryptamine release, 5-hydroxytryptamine uptake and in the regulation of extracellular dopamine and 5- hydroxytryptamine levels, and thereby affects neural activity. May play a role in the perception of pain. Plays a role in the regulation of behavior, including impulsive behavior. Required for normal proliferation of embryonic cardiac myocytes and normal heart development. Protects cardiomyocytes against apoptosis. Plays a role in the adaptation of pulmonary arteries to chronic hypoxia. Plays a role in vasoconstriction. Required for normal osteoblast function and proliferation, and for maintaining normal bone density. Required for normal proliferation of the interstitial cells of Cajal in the intestine. {ECO:0000269|PubMed:12970106, ECO:0000269|PubMed:18703043, ECO:0000269|PubMed:23519210, ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:7926008, ECO:0000269|PubMed:8078486, ECO:0000269|PubMed:8143856, ECO:0000269|PubMed:8882600}.; . TISSUE SPECIFICITY: Ubiquitous. Detected in liver, kidney, heart, pulmonary artery, and intestine. Detected at lower levels in blood, placenta and brain, especially in cerebellum, occipital cortex and frontal cortex. {ECO:0000269|PubMed:21179162, ECO:0000269|PubMed:7926008, ECO:0000269|PubMed:8078486, ECO:0000269|PubMed:8143856, ECO:0000269|PubMed:8882600}.; unclassifiable (Anatomical System);meninges;heart;cartilage;colon;skeletal muscle;skin;uterus;prostate;pia mater;thyroid;bone;testis;dura mater;kidney; uterus;uterus corpus;superior cervical ganglion;appendix;trigeminal ganglion;skeletal muscle; 0.14690 0.13643 0.110306132 62.00165133 566.44526 4.83316 HTR2C 0.0689152859314493 0.87184859680699 0.0592361172615606 5-hydroxytryptamine receptor 2C FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including ergot alkaloid derivatives, 1- 2,5,-dimethoxy-4-iodophenyl-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and down-stream signaling cascades and promotes the release of Ca(2+) ions from intracellular stores. Regulates neuronal activity via the activation of short transient receptor potential calcium channels in the brain, and thereby modulates the activation of pro-opiomelacortin neurons and the release of CRH that then regulates the release of corticosterone. Plays a role in the regulation of appetite and eating behavior, responses to anxiogenic stimuli and stress. Plays a role in insulin sensitivity and glucose homeostasis. {ECO:0000269|PubMed:12970106, ECO:0000269|PubMed:18703043, ECO:0000269|PubMed:19057895, ECO:0000269|PubMed:7895773}.; . TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:8812491}.; unclassifiable (Anatomical System);meninges;pia mater;dura mater;brain;skin;skeletal muscle; amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;hypothalamus;atrioventricular node;pons;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.36129 0.22382 -0.271755481 34.31823543 746.64389 5.42129 HTR3A 1.02839422335736e-09 0.164997592118733 0.835002406852873 5-hydroxytryptamine receptor 3A FUNCTION: This is one of the several different receptors for 5- hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses in neurons. It is a cation-specific, but otherwise relatively nonselective, ion channel. {ECO:0000269|PubMed:12867984, ECO:0000269|PubMed:9950429}.; . TISSUE SPECIFICITY: Expressed in cerebral cortex, amygdala, hippocampus, and testis. Detected in monocytes of the spleen and tonsil, in small and large intestine, uterus, prostate, ovary and placenta. {ECO:0000269|PubMed:10521471}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;parathyroid;lung;larynx;placenta;visual apparatus;liver;testis;head and neck;spleen;germinal center;kidney;brain;tonsil; dorsal root ganglion;uterus corpus;superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.27135 0.24090 -1.105907904 6.86482661 468.18677 4.48279 HTR3B 6.14952696572758e-07 0.676722930712049 0.323276454335254 5-hydroxytryptamine receptor 3B FUNCTION: This is one of the several different receptors for 5- hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel. {ECO:0000269|PubMed:12867984}.; . TISSUE SPECIFICITY: Expressed in the brain cortex, in the caudate nucleus, the hyppocampus, the thalamus and the amygdala. Detected in the kidney and testis as well as in monocytes of the spleen, small and large intestine, uterus, prostate, ovary and placenta. {ECO:0000269|PubMed:10521471, ECO:0000269|PubMed:9950429}.; . . 0.10673 0.09165 0.997633954 90.65227648 2305.77485 8.89752 HTR3C 2.33900863158536e-08 0.265830737109043 0.734169239500871 5-hydroxytryptamine receptor 3C FUNCTION: This is one of the several different receptors for 5- hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel.; . TISSUE SPECIFICITY: Expressed in many tissues including adult brain, colon, intestine, lung, muscle and stomach as well as fetal colon and kidney. {ECO:0000269|PubMed:12801637}.; unclassifiable (Anatomical System); . 0.12832 0.07113 0.913082291 89.54352442 4083.83082 12.68484 HTR3D 2.59130296079301e-06 0.168847484971448 0.831149923725591 5-hydroxytryptamine receptor 3D FUNCTION: This is one of the several different receptors for 5- hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel.; . TISSUE SPECIFICITY: Expressed in liver, as well as fetal and adult colon and kidney. {ECO:0000269|PubMed:12801637}.; . . 0.15779 . 2.50993317 98.66124086 1802.49556 7.83334 HTR3E 0.00133646646478871 0.861581341647191 0.13708219188802 5-hydroxytryptamine receptor 3E FUNCTION: This is one of the several different receptors for 5- hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel.; . TISSUE SPECIFICITY: Expressed in adult colon and intestine. {ECO:0000269|PubMed:12801637, ECO:0000269|PubMed:14597179}.; . . 0.08483 . 0.023941474 55.75607455 490.52097 4.55824 HTR3E-AS1 . . . HTR3E antisense RNA 1 . . . . . . . . . . . HTR4 0.648787512759024 0.349945875757313 0.0012666114836633 5-hydroxytryptamine receptor 4 FUNCTION: This is one of the several different receptors for 5- hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase.; . TISSUE SPECIFICITY: Isoform 5-HT4(A) is expressed in ileum, brain, and atrium, but not in the ventricle. {ECO:0000269|PubMed:15118808}.; unclassifiable (Anatomical System);stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;medulla oblongata;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin;parietal lobe; 0.09018 0.16175 -0.045835247 50.34206181 168.09506 2.83108 HTR5A 0.00578863422656513 0.725636088195404 0.268575277578031 5-hydroxytryptamine receptor 5A FUNCTION: This is one of the several different receptors for 5- hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins.; . . unclassifiable (Anatomical System);lung;hypothalamus;testis;brain; occipital lobe;skeletal muscle; 0.17368 0.13655 -0.468351206 23.42533616 145.62708 2.63038 HTR5A-AS1 0.632521887487388 0.337997121160919 0.0294809913516923 HTR5A antisense RNA 1 . . . . . . . . . 13.85041 0.50251 HTR5BP . . . 5-hydroxytryptamine receptor 5B, pseudogene . . . . . . . . . . . HTR6 0.00106725360649504 0.604391445179635 0.39454130121387 5-hydroxytryptamine receptor 6 FUNCTION: This is one of the several different receptors for 5- hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase. It has a high affinity for tricyclic psychotropic drugs (By similarity). Controls pyramidal neurons migration during corticogenesis, through the regulation of CDK5 activity (By similarity). Is an activator of TOR signaling (PubMed:23027611). {ECO:0000250|UniProtKB:P31388, ECO:0000250|UniProtKB:Q9R1C8, ECO:0000269|PubMed:23027611}.; . TISSUE SPECIFICITY: Expressed in several human brain regions, most prominently in the caudate nucleus.; unclassifiable (Anatomical System);ovary;brain;mammary gland; . 0.20720 0.15087 -0.648365105 16.35999056 53.40321 1.45227 HTR7 0.0340176985624909 0.927571168253742 0.0384111331837673 5-hydroxytryptamine receptor 7 FUNCTION: This is one of the several different receptors for 5- hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase.; . TISSUE SPECIFICITY: Isoform A is the predominant isoform in spleen, caudate and hippocampus. Isoform B is expressed at lower levels. Isoform D is a minor isoform in term of expression. {ECO:0000269|PubMed:9084407}.; unclassifiable (Anatomical System);bone;testis;brain; superior cervical ganglion;testis - interstitial;globus pallidus;trigeminal ganglion;skin;skeletal muscle;cingulate cortex;pituitary; 0.58795 0.15269 0.104848986 61.49445624 35.97418 1.07998 HTR7P1 . . . 5-hydroxytryptamine receptor 7 pseudogene 1 . . . unclassifiable (Anatomical System);uterus;heart;skin; fetal liver;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . . . . . . HTRA1 0.0169475465900735 0.978184770274447 0.00486768313547939 HtrA serine peptidase 1 FUNCTION: Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, although it is unclear whether TGF-beta proteins are themselves degraded. By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets. {ECO:0000269|PubMed:16377621, ECO:0000269|PubMed:20671064, ECO:0000269|PubMed:9852107}.; DISEASE: Macular degeneration, age-related, 7 (ARMD7) [MIM:610149]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. {ECO:0000269|PubMed:17053108, ECO:0000269|PubMed:17053109}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Cerebral arteriopathy, autosomal recessive, with subcortical infarcts and leukoencephalopathy (CARASIL) [MIM:600142]: A cerebrovascular disease characterized by non- hypertensive arteriopathy of cerebral small vessels with subcortical infarcts, alopecia, and spondylosis. Small cerebral arteries show arteriosclerotic changes, fibrous intimal proliferation, and hyaline degeneration with splitting of the intima and/or the internal elastic membrane. Neurologic features include progressive dementia, gait disturbances, extrapyramidal and pyramidal signs, and demyelination of the cerebral white matter with sparing of U fibers. {ECO:0000269|PubMed:19387015}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, with strongest expression in placenta (at protein level). Secreted by synovial fibroblasts. Up- regulated in osteoarthritis and rheumatoid arthritis synovial fluids and cartilage as compared with non-arthritic (at protein level). {ECO:0000269|PubMed:15208355, ECO:0000269|PubMed:16377621, ECO:0000269|PubMed:9852107}.; . . 0.32992 0.33227 . . 409.08973 4.23916 HTRA2 0.00230127577366885 0.98029065446702 0.0174080697593111 HtrA serine peptidase 2 FUNCTION: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 seems to be proteolytically inactive. {ECO:0000269|PubMed:15200957, ECO:0000269|PubMed:19502560}.; DISEASE: Parkinson disease 13 (PARK13) [MIM:610297]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. {ECO:0000269|PubMed:15961413}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is ubiquitous. Isoform 2 is expressed predominantly in the kidney, colon and thyroid.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; whole brain;thalamus; 0.80315 0.37852 0.283038099 71.26680821 88.78352 2.02161 HTRA3 1.71991707578293e-05 0.675145167307777 0.324837633521465 HtrA serine peptidase 3 FUNCTION: Serine protease that cleaves beta-casein/CSN2 as well as several extracellular matrix (ECM) proteoglycans such as decorin/DCN, biglycan/BGN and fibronectin/FN1. Inhibits signaling mediated by TGF-beta family proteins possibly indirectly by degradation of these ECM proteoglycans (By similarity). May act as a tumor suppressor. Negatively regulates, in vitro, trophoblast invasion during placental development and may be involved in the development of the placenta in vivo. May also have a role in ovarian development, granulosa cell differentiation and luteinization (PubMed:21321049, PubMed:22229724). {ECO:0000250|UniProtKB:Q9D236, ECO:0000269|PubMed:21321049, ECO:0000269|PubMed:22229724}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in both adult and fetal heart, ovary, uterus placenta, and bladder. In the endometrium, expressed in epithelial glands and the stroma. Also present in leukocytes. Isoform 1 is predominant in heart and skeletal muscle, whereas isoform 2 is predominant in placenta and kidney. {ECO:0000269|PubMed:12513693, ECO:0000269|PubMed:16650464, ECO:0000269|PubMed:21321049}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;colon;skin;skeletal muscle;uterus;pancreas;optic nerve;whole body;lung;placenta;testis;kidney;stomach;thymus; . 0.16158 0.11489 -0.822919685 11.76574664 170.60666 2.84944 HTRA4 2.53128845476791e-07 0.485367107506994 0.514632639364161 HtrA serine peptidase 4 FUNCTION: Serine protease. {ECO:0000305}.; . . unclassifiable (Anatomical System);placenta; dorsal root ganglion;superior cervical ganglion;trachea;placenta;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.03793 0.07188 0.595326758 82.66100495 96.47695 2.12143 HTT 0.999999999968547 3.14533008702999e-11 6.46298559033531e-34 huntingtin FUNCTION: May play a role in microtubule-mediated transport or vesicle function.; DISEASE: Huntington disease (HD) [MIM:143100]: A neurodegenerative disorder characterized by involuntary movements (chorea), general motor impairment, psychiatric disorders and dementia. Onset of the disease occurs usually in the third or fourth decade of life. Onset and clinical course depend on the degree of poly-Gln repeat expansion, longer expansions resulting in earlier onset and more severe clinical manifestations. Neuropathology of Huntington disease displays a distinctive pattern with loss of neurons, especially in the caudate and putamen. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the brain cortex (at protein level). Widely expressed with the highest level of expression in the brain (nerve fibers, varicosities, and nerve endings). In the brain, the regions where it can be mainly found are the cerebellar cortex, the neocortex, the striatum, and the hippocampal formation. {ECO:0000269|PubMed:16391387}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;subthalamic nucleus;medulla oblongata;cerebellum peduncles;temporal lobe;prefrontal cortex;ciliary ganglion;pons;skeletal muscle;parietal lobe;cingulate cortex; 0.77816 0.10595 -2.029268562 1.692616183 10242.03379 22.04965 HTT-AS . . . HTT antisense RNA (head to head) . . . . . . . . . . . HULC . . . hepatocellular carcinoma up-regulated long non-coding RNA . . . . . . . . . . . HUNK 0.997271074532227 0.00272890071019611 2.47575773341589e-08 hormonally up-regulated Neu-associated kinase . . . unclassifiable (Anatomical System);heart;ovary;cartilage;muscle;colon;parathyroid;skin;uterus;cochlea;endometrium;placenta;visual apparatus;liver;spleen;brain; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.18502 0.10874 -0.152426933 42.25053079 2500.14919 9.31679 HUNK-AS1 . . . HUNK antisense RNA 1 . . . . . . . . . . . HUS1 0.000609572433043018 0.903311452845822 0.0960789747211348 HUS1 checkpoint clamp component FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. {ECO:0000269|PubMed:21659603}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10777662}.; unclassifiable (Anatomical System);meninges;lymph node;ovary;islets of Langerhans;parathyroid;skin;skeletal muscle;bone marrow;uterus;prostate;pia mater;lung;trabecular meshwork;bone;placenta;visual apparatus;liver;testis;spleen;dura mater;germinal center;stomach; superior cervical ganglion;appendix;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; . 0.08275 0.461228372 78.46190139 96.58027 2.12288 HUS1B 0.00831323325620067 0.564149124443798 0.427537642300001 HUS1 checkpoint clamp component B . . TISSUE SPECIFICITY: Expressed strongly in testis, less in spleen, thymus, prostate, colon and leukocytes. {ECO:0000269|PubMed:11944979}.; . . . 0.08275 0.330767508 73.53739089 238.10375 3.33239 HUWE1 0.999999999999995 5.07218760208827e-15 5.44596856030304e-39 HECT, UBA and WWE domain containing 1, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1. Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair. Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4. Binds to an upstream initiator-like sequence in the preprodynorphin gene. Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN. May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation. Mediates polyubiquitination of isoform 2 of PA2G4. {ECO:0000269|PubMed:15567145, ECO:0000269|PubMed:15767685, ECO:0000269|PubMed:15989956, ECO:0000269|PubMed:15989957, ECO:0000269|PubMed:17567951, ECO:0000269|PubMed:18488021, ECO:0000269|PubMed:19037095, ECO:0000269|PubMed:19713937}.; DISEASE: Mental retardation, X-linked, syndromic, Turner type (MRXST) [MIM:300706]: A syndrome characterized by the association of mental retardation with macrocephaly and variable contractures. {ECO:0000269|PubMed:18252223}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mental retardation, X-linked 17 (MRX17) [MIM:300705]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non- syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. {ECO:0000269|PubMed:18252223}. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal microduplication involving HSD17B10 and HUWE1 has been found in patients with mental retardation.; TISSUE SPECIFICITY: Weakly expressed in heart, brain and placenta but not in other tissues. Expressed in a number of cell lines, predominantly in those from colorectal carcinomas. {ECO:0000269|PubMed:15567145}.; lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;iris;germinal center;bladder;brain;cartilage;heart;pineal body;urinary;adrenal cortex;blood;lens;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;hypopharynx;amnion;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;testis - interstitial;testis;ciliary ganglion;pons;caudate nucleus;atrioventricular node;trigeminal ganglion;skin;parietal lobe;skeletal muscle;cerebellum; 0.84682 0.35105 -3.359560776 0.395140363 451.51768 4.41721 HVBS7 . . . hepatitis B virus integration site 7 . . . . . . . . . . . HVBS8 . . . hepatitis B virus integration site 8 . . . . . . . . . . . HVCN1 0.750490678392491 0.24732859038721 0.00218073122029885 hydrogen voltage gated channel 1 FUNCTION: Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagocytosis. {ECO:0000269|PubMed:16554753, ECO:0000269|PubMed:20037153, ECO:0000269|PubMed:22020278}.; . TISSUE SPECIFICITY: Enriched in immune tissues, such as lymph nodes, B-lymphocytes, monocytes and spleen. {ECO:0000269|PubMed:16554753}.; lymphoreticular;ovary;salivary gland;developmental;intestine;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;thyroid;iris;testis;germinal center;bladder;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;visual apparatus;alveolus;liver;head and neck;spleen;kidney;mammary gland;stomach; superior cervical ganglion;testis;ciliary ganglion; 0.06271 0.08538 0.305084559 72.22811984 27.34873 0.88101 HYAL1 0.0055367061124395 0.897294478368243 0.0971688155193174 hyaluronoglucosaminidase 1 FUNCTION: May have a role in promoting tumor progression. May block the TGFB1-enhanced cell growth. {ECO:0000269|PubMed:12084718}.; . TISSUE SPECIFICITY: Highly expressed in the liver, kidney and heart. Weakly expressed in lung, placenta and skeletal muscle. No expression detected in adult brain. Isoform 1 is expressed only in bladder and prostate cancer cells, G2/G3 bladder tumor tissues and lymph node specimens showing tumor invasive tumors cells. Isoform 3, isoform 4, isoform 5 and isoform 6 are expressed in normal bladder and bladder tumor tissues. {ECO:0000269|PubMed:10339581, ECO:0000269|PubMed:12084718, ECO:0000269|PubMed:9223416}.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;skin;uterus;pancreas;lung;liver;testis;spleen;cervix;kidney;brain;mammary gland;stomach; . 0.10841 0.07765 0.110306132 62.00165133 324.88649 3.83161 HYAL2 0.0206315124398338 0.961955323457671 0.0174131641024949 hyaluronoglucosaminidase 2 FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product which is further hydrolyzed by sperm hyaluronidase to give small oligosaccharides. Displays very low levels of activity. Associates with and negatively regulates MST1R. {ECO:0000269|PubMed:11296287, ECO:0000269|PubMed:12676986, ECO:0000269|PubMed:9712871}.; . TISSUE SPECIFICITY: Widely expressed. No expression detected in adult brain. {ECO:0000269|PubMed:9712871}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;pituitary gland;testis;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach; lung;heart; 0.24038 0.15296 -0.424258538 25.56027365 1720.68028 7.64856 HYAL3 1.52465574848001e-05 0.649089718544838 0.350895034897678 hyaluronoglucosaminidase 3 . . TISSUE SPECIFICITY: Bone marrow, testis and kidney. Isoform 4 is detected in all bladder tumor and prostate tumor cells. {ECO:0000269|PubMed:10493834, ECO:0000269|PubMed:12084718}.; unclassifiable (Anatomical System);medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;lung;placenta;thyroid;macula lutea;liver;testis;cervix;kidney;brain;stomach; . 0.06110 . 0.264628794 70.5178108 870.51929 5.74570 HYAL4 2.05182329925812e-15 0.00106904134124099 0.998930958658757 hyaluronoglucosaminidase 4 FUNCTION: Endo-hyaluronidase that degrades hyaluronan to smaller oligosaccharide fragments. Has also chondroitin sulfate hydrolase activity, The best substrate being the galactosaminidic linkage in the sequence of a trisulfated tetrasaccharide. {ECO:0000269|PubMed:16104017, ECO:0000269|PubMed:19889881}.; . TISSUE SPECIFICITY: Detected in placenta and skeletal muscle. {ECO:0000269|PubMed:10493834}.; unclassifiable (Anatomical System);uterus;heart;placenta;liver;spleen;skin; superior cervical ganglion;testis - interstitial;globus pallidus;appendix;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11712 0.10683 0.731244617 86.21137061 1314.20961 6.81410 HYALP1 . . . hyaluronoglucosaminidase pseudogene 1 . . . . . . . . . . . HYD2 . . . hypodontia 2 (autosomal recessive) . . . . . . . . . . . HYDIN . . . HYDIN, axonemal central pair apparatus protein FUNCTION: Required for ciliary motility. {ECO:0000250}.; DISEASE: Ciliary dyskinesia, primary, 5 (CILD5) [MIM:608647]: An autosomal recessive form of primary dyskinesia, a disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. CILD5 is characterized by early onset of a progressive decline in lung function due to an inability to clear mucus and particles from the airways. Affected individuals have recurrent infections of the sinuses, ears, airways, and lungs. Sperm motility is also decreased. Individuals with CILD5 do not have situs inversus. {ECO:0000269|PubMed:23022101, ECO:0000269|PubMed:25186273}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;ovary;islets of Langerhans;thyroid;muscle;testis;kidney;brain;skeletal muscle;retina; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; . . . . 14038.48997 25.58931 HYDIN2 . . . HYDIN2, axonemal central pair apparatus protein (pseudogene) . . . . . . . . . . . HYI 3.15819250162145e-08 0.172919964825085 0.82708000359299 hydroxypyruvate isomerase (putative) FUNCTION: Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde). {ECO:0000250}.; . . . . 0.15662 0.11509 0.839664339 88.29912715 204.51807 3.09008 HYI-AS1 . . . HYI antisense RNA 1 . . . . . . . . . . . HYKK 0.000214856084289355 0.737638273114386 0.262146870801325 hydroxylysine kinase FUNCTION: Catalyzes the GTP-dependent phosphorylation of 5- hydroxy-L-lysine. {ECO:0000269|PubMed:22241472}.; . . . . . . 0.52918614 80.81505072 586.99186 4.91433 HYLS1 5.8228427856488e-05 0.697859454359706 0.302082317212437 hydrolethalus syndrome 1 . DISEASE: Hydrolethalus syndrome 1 (HLS1) [MIM:236680]: A lethal syndrome characterized by polydactyly, central nervous system malformation, and hydrocephalus. The polydactyly is postaxial in the hands and preaxial in the feet. A highly characteristic hallux duplex is seen in almost no other situation. In half of the cases, a large atrioventricular communis defect of the heart is found. The pregnancy is characterized by hydramnios, which is often massive, and by preterm delivery. {ECO:0000269|PubMed:15843405}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;whole body;cartilage;endometrium;bone;placenta;testis;colon;kidney;germinal center;mammary gland; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.11549 0.16710 -0.0274281 51.65723048 2684.80378 9.74306 HYMAI . . . hydatidiform mole associated and imprinted (non-protein coding) . . . . . . . . . . . HYOU1 0.9997793595111 0.000220640488453976 4.46430277771273e-13 hypoxia up-regulated 1 FUNCTION: Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding. {ECO:0000269|PubMed:10037731}.; . TISSUE SPECIFICITY: Highly expressed in tissues that contain well- developed endoplasmic reticulum and synthesize large amounts of secretory proteins. Highly expressed in liver and pancreas and lower expression in brain and kidney. Also expressed in macrophages within aortic atherosclerotic plaques, and in breast cancers.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;brain;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;thymus;cerebellum; whole brain;testis - interstitial;placenta;prefrontal cortex;testis;cingulate cortex; 0.55670 0.18042 -1.835411529 2.081858929 85.0696 1.96574 HYPK 0.021030750002461 0.751910761804074 0.227058488193465 huntingtin interacting protein K FUNCTION: Has a chaperone-like activity preventing polyglutamine (polyQ) aggregation of HTT. Protects against HTT polyQ-mediated apoptosis in Neuro2a neuronal cells. Required for optimal NAA10- NAA15 complex-mediated N-terminal acetylation. {ECO:0000269|PubMed:17947297, ECO:0000269|PubMed:20154145}.; . . . . . . 0.371224249 75.12384996 . . HYPM . . . huntingtin interacting protein M . . . . . 0.02815 0.06915 0.836034065 88.17527719 . . IAH1 0.000119134559107643 0.611982438141157 0.387898427299735 isoamyl acetate-hydrolyzing esterase 1 homolog FUNCTION: Probable lipase. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;breast;bile duct;lung;cornea;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; . 0.16033 0.10293 0.170987912 65.5579146 74.74465 1.80869 IAPP 0.166030146477273 0.640685320377671 0.193284533145055 islet amyloid polypeptide FUNCTION: Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.; . . unclassifiable (Anatomical System);islets of Langerhans; superior cervical ganglion;pancreas;beta cell islets;trigeminal ganglion; 0.24780 0.25622 -0.141298762 42.87567823 12.46247 0.45269 IARS 4.34508835544123e-09 0.999995165096029 4.83055888264987e-06 isoleucyl-tRNA synthetase . . . . . 0.71817 0.19154 -1.074802575 7.336635999 1316.65812 6.82478 IARS2 0.472741795319536 0.527258129464453 7.52160107726284e-08 isoleucyl-tRNA synthetase 2, mitochondrial . DISEASE: Cataracts, growth hormone deficiency, sensory neuropathy, sensorineural hearing loss, and skeletal dysplasia (CAGSSS) [MIM:616007]: An autosomal recessive disorder characterized by cataracts, short-stature secondary to growth hormone deficiency, sensorineural hearing deficit, peripheral sensory neuropathy, skeletal dysplasia, scoliosis, and facial dysmorphism. {ECO:0000269|PubMed:25130867}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;dura mater;germinal center;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;tongue;hypothalamus;blood;lens;skeletal muscle;breast;bile duct;pia mater;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;adipose tissue;testis;parietal lobe; 0.49745 0.12590 -0.929520514 9.683887709 591.48905 4.92950 IARS2P1 . . . isoleucyl-tRNA synthetase 2, mitochondrial pseudogene 1 . . . . . . . . . . . IBA57 0.0830210148136165 0.871663842544641 0.045315142641742 IBA57 homolog, iron-sulfur cluster assembly FUNCTION: Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway. {ECO:0000269|PubMed:23462291}.; DISEASE: Spastic paraplegia 74, autosomal recessive (SPG74) [MIM:616451]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG74 is characterized by a combination of spastic paraplegia, optic atrophy, and peripheral neuropathy with childhood-onset and slow progression into late adulthood. {ECO:0000269|PubMed:25609768}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in skin fibroblasts and skeletal muscle (at protein level). {ECO:0000269|PubMed:23462291}.; . . 0.17510 0.09805 . . 1061.6846 6.25275 IBA57-AS1 . . . IBA57 antisense RNA 1 (head to head) . . . . . 0.11507 . . . 150.4243 2.67743 IBD2 . . . inflammatory bowel disease 2 . . . . . . . . . . . IBD3 . . . inflammatory bowel disease 3 . . . . . . . . . . . IBD4 . . . inflammatory bowel disease 4 . . . . . . . . . . . IBD5 . . . inflammatory bowel disease 5 . . . . . . . . . . . IBD6 . . . inflammatory bowel disease 6 . . . . . . . . . . . IBD7 . . . inflammatory bowel disease 7 . . . . . . . . . . . IBD8 . . . inflammatory bowel disease 8 . . . . . . . . . . . IBD9 . . . inflammatory bowel disease 9 . . . . . . . . . . . IBGC1 . . . idiopathic basal ganglia calcification 1 . . . . . . . . . . . IBSP 7.12926740123526e-08 0.266060798452033 0.733939130255293 integrin binding sialoprotein FUNCTION: Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment.; . . unclassifiable (Anatomical System);whole body;cartilage;cochlea;bone;brain; temporal lobe;trigeminal ganglion;skin;skeletal muscle; 0.20379 0.35591 1.350418743 94.35008257 6442.27833 16.86019 IBTK 0.901146102319855 0.0988538971753528 5.04792577477677e-10 inhibitor of Bruton tyrosine kinase FUNCTION: Acts as an inhibitor of BTK tyrosine kinase activity, thereby playing a role in B-cell development. Down-regulates BTK kinase activity, leading to interference with BTK-mediated calcium mobilization and NF-kappa-B-driven transcription. {ECO:0000269|PubMed:11577348}.; . TISSUE SPECIFICITY: Expressed in DeFew, HEK293T, HeLa and in Jurkat, MC3 and NB4 lymphoid cells (at protein level). Isoform 1 is the predominant isoform expressed in all examined tissues and cell lines. Highly expressed in hemopoietic tissues (fetal liver, spleen, lymph node, thymus, peripheral blood leukocytes and bone marrow). Weakly or not expressed in other tissues. {ECO:0000269|PubMed:11577348, ECO:0000269|PubMed:18596081}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;urinary;blood;lens;skeletal muscle;bile duct;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.36510 0.08876 -0.659500046 16.07100731 1718.28989 7.64339 IBTKP1 . . . inhibitor of Bruton tyrosine kinase pseudogene 1 . . . . . . . . . . . ICA1 0.00495036829251652 0.993837067521844 0.001212564185639 islet cell autoantigen 1 FUNCTION: May play a role in neurotransmitter secretion. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed abundantly in pancreas, heart and brain with low levels of expression in lung, kidney, liver and thyroid.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;breast;lung;nasopharynx;placenta;hippocampus;liver;spleen;kidney;stomach; dorsal root ganglion;testis - interstitial;subthalamic nucleus;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16856 0.19221 -0.712684326 14.49634348 31.41264 0.99064 ICA1L 0.442027586412226 0.557692445678738 0.000279967909035354 islet cell autoantigen 1 like . . . unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;skeletal muscle;retina;prostate;atrium;lung;cochlea;endometrium;nasopharynx;placenta;testis;kidney;brain;cerebellum; superior cervical ganglion;globus pallidus;ciliary ganglion; 0.12377 . 0.373041938 75.29488087 125.08262 2.43349 ICAM1 0.11779732116171 0.8765778257428 0.00562485309549064 intercellular adhesion molecule 1 FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans- endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation. {ECO:0000269|PubMed:11173916, ECO:0000269|PubMed:17875742}.; . . ovary;colon;choroid;skin;bone marrow;uterus;prostate;whole body;endometrium;gum;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;spinal cord;urinary;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;alveolus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;ciliary ganglion;fetal lung;caudate nucleus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.05846 . 0.249861693 69.66265629 980.7979 6.04688 ICAM2 0.0232669387159647 0.912974290849697 0.0637587704343382 intercellular adhesion molecule 2 FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). ICAM2 may play a role in lymphocyte recirculation by blocking LFA-1-dependent cell adhesion. It mediates adhesive interactions important for antigen- specific immune response, NK-cell mediated clearance, lymphocyte recirculation, and other cellular interactions important for immune response and surveillance.; . . . . 0.10405 0.22830 -0.227663163 37.11370606 70.4297 1.74584 ICAM3 2.07707792396741e-22 1.53138942206606e-05 0.999984686105779 intercellular adhesion molecule 3 FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). ICAM3 is also a ligand for integrin alpha-D/beta-2.; . . colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;urinary;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;mammary gland;stomach;aorta; lymph node;heart;liver;white blood cells;whole blood;tonsil;bone marrow;thymus; 0.02658 0.18737 -0.042196577 50.49539986 1207.94912 6.58159 ICAM4 1.53444721877808e-05 0.416589694370778 0.583394961157034 intercellular adhesion molecule 4 (Landsteiner-Wiener blood group) FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). ICAM4 is also a ligand for alpha-4/beta-1 and alpha-V integrins. {ECO:0000269|PubMed:11435317}.; . TISSUE SPECIFICITY: Erythrocytes.; unclassifiable (Anatomical System);lung;colon;brain; superior cervical ganglion;skeletal muscle; 0.07439 . 0.305084559 72.22811984 36.56984 1.09624 ICAM5 . . . intercellular adhesion molecule 5 FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2).; . TISSUE SPECIFICITY: Expressed on neurons in the most rostral segment of the mammalian brain, the telencephalon.; unclassifiable (Anatomical System);lung;ovary;thyroid;placenta;hippocampus;testis;parathyroid;brain; amygdala;subthalamic nucleus;cingulate cortex; 0.25611 . -0.200157416 39.11299835 4945.57388 14.33389 ICE1 . . . interactor of little elongation complex ELL subunit 1 FUNCTION: Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968, PubMed:23932780). Specifically acts as a scaffold protein that promotes the LEC complex formation and recruitment and RNA polymerase II occupancy at snRNA genes in subnuclear bodies (PubMed:23932780). {ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:23932780}.; . . . . . . -0.174712176 40.57560745 . . ICE2 . . . interactor of little elongation complex ELL subunit 2 FUNCTION: Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III. {ECO:0000269|PubMed:23932780}.; . TISSUE SPECIFICITY: Expressed at low levels in lung and testis. {ECO:0000269|PubMed:15606750}.; . . 0.71056 0.16808 -0.815648973 12.01344657 . . ICE2P1 . . . interactor of little elongation complex ELL subunit 2 pseudogene 1 . . . . . . . . . . . ICE2P2 . . . interactor of little elongation complex ELL subunit 2 pseudogene 2 . . . . . . . . . . . ICK 0.10744982933628 0.892538927269114 1.12433946064193e-05 intestinal cell (MAK-like) kinase FUNCTION: Required for ciliogenesis (PubMed:24797473). Phosphorylates KIF3A (By similarity). Involved in the control of ciliary length (PubMed:24853502). Regulates the ciliary localization of SHH pathway components as well as the localization of IFT components at ciliary tips (By similarity). May play a key role in the development of multiple organ systems and particularly in cardiac development (By similarity). {ECO:0000250|UniProtKB:Q62726, ECO:0000250|UniProtKB:Q9JKV2, ECO:0000269|PubMed:24797473, ECO:0000269|PubMed:24853502}.; DISEASE: Endocrine-cerebroosteodysplasia (ECO) [MIM:612651]: Previously unidentified neonatal lethal recessive disorder with multiple anomalies involving the endocrine, cerebral, and skeletal systems. {ECO:0000269|PubMed:19185282}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in heart, brain, placenta, pancreas, thymus, prostate, testis, ovary, small intestine and colon, with highest levels in placenta and testis. Not detected in spleen. Also expressed in many cancer cell lines. {ECO:0000269|PubMed:10699974, ECO:0000269|PubMed:12103360}.; medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;aorta; . 0.22450 0.08611 -0.200157416 39.11299835 413.29784 4.25688 ICMT 0.95914542813838 0.0407607709551166 9.38009065037675e-05 isoprenylcysteine carboxyl methyltransferase FUNCTION: Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues.; . TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at higher levels in the cerebellum and putamen than in other brain regions. Abundant expression seen in the Purkinje cells and pontine neurons. {ECO:0000269|PubMed:10649571}.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;placenta;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;medulla oblongata;testis - interstitial;superior cervical ganglion;cerebellum peduncles;placenta;ciliary ganglion;kidney;trigeminal ganglion;skeletal muscle;cerebellum; 0.66227 0.11002 0.3032669 72.009908 81.9495 1.91989 ICOS 0.0520092290924777 0.861740748087512 0.08625002282001 inducible T-cell co-stimulator FUNCTION: Enhances all basic T-cell responses to a foreign antigen, namely proliferation, secretion of lymphokines, up- regulation of molecules that mediate cell-cell interaction, and effective help for antibody secretion by B-cells. Essential both for efficient interaction between T and B-cells and for normal antibody responses to T-cell dependent antigens. Does not up- regulate the production of interleukin-2, but superinduces the synthesis of interleukin-10. Prevents the apoptosis of pre- activated T-cells. Plays a critical role in CD40-mediated class switching of immunoglobin isotypes (By similarity). {ECO:0000250, ECO:0000269|PubMed:11169414, ECO:0000269|PubMed:9930702}.; DISEASE: Immunodeficiency, common variable, 1 (CVID1) [MIM:607594]: A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low. {ECO:0000269|PubMed:12577056}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Activated T-cells. Highly expressed on tonsillar T-cells, which are closely associated with B-cells in the apical light zone of germinal centers, the site of terminal B- cell maturation. Expressed at lower levels in thymus, lung, lymph node and peripheral blood leukocytes. Expressed in the medulla of fetal and newborn thymus. {ECO:0000269|PubMed:11006126, ECO:0000269|PubMed:11169414, ECO:0000269|PubMed:9930702}.; unclassifiable (Anatomical System);lung;heart;endometrium;nasopharynx;thyroid;alveolus;testis;brain; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.07138 0.26809 0.25917371 70.05779665 56.57789 1.51225 ICOSLG 0.0425484518847542 0.929456998059827 0.0279945500554185 inducible T-cell co-stimulator ligand FUNCTION: Ligand for the T-cell-specific cell surface receptor ICOS. Acts as a costimulatory signal for T-cell proliferation and cytokine secretion; induces also B-cell proliferation and differentiation into plasma cells. Could play an important role in mediating local tissue responses to inflammatory conditions, as well as in modulating the secondary immune response by co- stimulating memory T-cell function (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is widely expressed (brain, heart, kidney, liver, lung, pancreas, placenta, skeletal muscle, bone marrow, colon, ovary, prostate, testis, lymph nodes, leukocytes, spleen, thymus and tonsil), while isoform 2 is detected only in lymph nodes, leukocytes and spleen. Expressed on activated monocytes and dendritic cells. {ECO:0000269|PubMed:10779774}.; unclassifiable (Anatomical System);heart;ovary;colon;blood;parathyroid;fovea centralis;choroid;lens;skin;retina;optic nerve;lung;placenta;macula lutea;testis;germinal center;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;thalamus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12282 0.20617 0.839664339 88.29912715 2097.36585 8.43701 ICR1 . . . ichthyosis congenita I, erythromatous lamellar ichthyosis, ichthyosiform erythroderma . . . . . . . . . . . ICR3 . . . ichthyosis congenita III, vulgaris-like recessive ichthyosis . . . . . . . . . . . ICR4 . . . ichthyosis congenita IV, ichthyosis-prematurity syndrome . . . . . . . . . . . ICR5 . . . ichthyosis congenita V, Sjogren-Larsson-like . . . . . . . . . . . ICS1 . . . immotile cilia syndrome 1 . . . . . . . . . . . ICT1 0.0193427333396564 0.900313626254605 0.0803436404057391 immature colon carcinoma transcript 1 FUNCTION: Essential peptidyl-tRNA hydrolase component of the mitochondrial large ribosomal subunit. Acts as a codon-independent translation release factor that has lost all stop codon specificity and directs the termination of translation in mitochondrion, possibly in case of abortive elongation. May be involved in the hydrolysis of peptidyl-tRNAs that have been prematurely terminated and thus in the recycling of stalled mitochondrial ribosomes. {ECO:0000269|PubMed:20186120}.; . TISSUE SPECIFICITY: Down-regulated during the in vitro differentiation of HT29-D4 colon carcinoma cells. {ECO:0000269|PubMed:8575443}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;cerebral cortex;oesophagus;bone;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);spinal cord;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; heart;liver;tumor;pons; 0.10843 0.11552 0.637604436 83.77565464 239.13828 3.34148 ID1 0.00765557463426437 0.546651605642352 0.445692819723384 inhibitor of DNA binding 1, HLH protein FUNCTION: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer (By similarity). {ECO:0000250}.; . . . . 0.51011 0.65602 -0.271755481 34.31823543 159.0431 2.75546 ID2 0.583638221851485 0.374015313342935 0.0423464648055802 inhibitor of DNA binding 2, HLH protein FUNCTION: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Restricts the CLOCK and ARNTL/BMAL1 localization to the cytoplasm. Plays a role in both the input and output pathways of the circadian clock: in the input component, is involved in modulating the magnitude of photic entrainment and in the output component, contributes to the regulation of a variety of liver clock-controlled genes involved in lipid metabolism. {ECO:0000269|PubMed:20861012}.; . TISSUE SPECIFICITY: Highly expressed in early fetal tissues, including those of the central nervous system.; myocardium;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;adrenal gland;placenta;hippocampus;duodenum;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.73906 0.49283 -0.185391282 39.67916962 8.59687 0.31492 ID2-AS1 . . . ID2 antisense RNA 1 (head to head) . . . . . . . . . . . ID2B . . . inhibitor of DNA binding 2B, HLH protein (pseudogene) . . . . . . . . . . . ID3 0.68879433753555 0.292815042329922 0.0183906201345276 inhibitor of DNA binding 3, HLH protein FUNCTION: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Involved in myogenesis by inhibiting skeletal muscle and cardiac myocyte differentiation and promoting muscle precursor cells proliferation. Inhibits the binding of E2A-containing protein complexes to muscle creatine kinase E-box enhancer. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. {ECO:0000269|PubMed:8437843}.; . TISSUE SPECIFICITY: Expressed abundantly in lung, kidney and adrenal gland, but not in adult brain.; . . 0.91585 0.30770 0.527368849 80.73248408 382.92744 4.12745 ID4 0.149454865643541 0.632600244735631 0.217944889620829 inhibitor of DNA binding 4, HLH protein FUNCTION: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation (By similarity). {ECO:0000250}.; . . . . 0.27698 0.19444 . . 23.5696 0.78258 IDDM3 . . . insulin-dependent diabetes mellitus 3 . . . . . . . . . . . IDDM4 . . . insulin-dependent diabetes mellitus 4 . . . . . . . . . . . IDDM6 . . . insulin-dependent diabetes mellitus 6 . . . . . . . . . . . IDDM7 . . . insulin-dependent diabetes mellitus 7 . . . . . . . . . . . IDDM8 . . . insulin-dependent diabetes mellitus 8 . . . . . . . . . . . IDDM9 . . . insulin-dependent diabetes mellitus 9 . . . . . . . . . . . IDDM11 . . . insulin-dependent diabetes mellitus 11 . . . . . . . . . . . IDDM13 . . . insulin-dependent diabetes mellitus 13 . . . . . . . . . . . IDDM14 . . . insulin-dependent diabetes mellitus 14 . . . . . . . . . . . IDDM15 . . . insulin-dependent diabetes mellitus 15 . . . . . . . . . . . IDDM16 . . . insulin-dependent diabetes mellitus 16 . . . . . . . . . . . IDDM17 . . . insulin-dependent diabetes mellitus 17 . . . . . . . . . . . IDDM18 . . . insulin-dependent diabetes mellitus 18 . . . . . . . . . . . IDE 0.426771018104833 0.573228875104064 1.06791102824021e-07 insulin degrading enzyme FUNCTION: Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia. {ECO:0000269|PubMed:10684867, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;ciliary body;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.83774 0.44335 -1.528486521 3.385232366 70.38074 1.74551 IDH1 0.00145370762541468 0.966058831799573 0.0324874605750121 isocitrate dehydrogenase 1 (NADP+) . DISEASE: Glioma (GLM) [MIM:137800]: Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes. {ECO:0000269|PubMed:19117336, ECO:0000269|PubMed:19935646}. Note=The gene represented in this entry is involved in disease pathogenesis. Mutations affecting Arg-132 are tissue-specific, and suggest that this residue plays a unique role in the development of high-grade gliomas. Mutations of Arg-132 to Cys, His, Leu or Ser abolish magnesium binding and abolish the conversion of isocitrate to alpha-ketoglutarate. Instead, alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate. Elevated levels of R(-)-2- hydroxyglutarate are correlated with an elevated risk of malignant brain tumors. {ECO:0000269|PubMed:19935646}.; . ovary;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;urinary;adrenal cortex;blood;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;alveolus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; prostate;adipose tissue;adrenal gland;adrenal cortex;testis;kidney; 0.86358 0.41617 0.018483465 55.44939844 537.58389 4.72637 IDH1-AS1 . . . IDH1 antisense RNA 1 . . . . . . . . . . . IDH2 0.376558105362484 0.621177131521352 0.00226476311616341 isocitrate dehydrogenase 2 (NADP+), mitochondrial FUNCTION: Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex.; DISEASE: D-2-hydroxyglutaric aciduria 2 (D2HGA2) [MIM:613657]: A neurometabolic disorder causing developmental delay, epilepsy, hypotonia, and dysmorphic features. Both a mild and a severe phenotype exist. The severe phenotype is homogeneous and is characterized by early infantile-onset epileptic encephalopathy and cardiomyopathy. The mild phenotype has a more variable clinical presentation. Diagnosis is based on the presence of an excess of D-2-hydroxyglutaric acid in the urine. {ECO:0000269|PubMed:20847235}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Glioma (GLM) [MIM:137800]: Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes. {ECO:0000269|PubMed:19228619, ECO:0000269|PubMed:25495392}. Note=The gene represented in this entry is involved in disease pathogenesis.; . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;greater omentum;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;placenta;hippocampus;head and neck;kidney;stomach;thymus; amygdala;prostate;heart;tongue;liver;kidney;skeletal muscle;thymus; 0.33255 0.81129 -0.380166007 27.88393489 40.46933 1.18692 IDH3A 0.230948359529529 0.767503776764612 0.00154786370585898 isocitrate dehydrogenase 3 (NAD+) alpha . . . lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;tongue;spinal cord;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;caudate nucleus;atrioventricular node;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.20990 0.44792 -0.005381972 53.50908233 36.85596 1.10396 IDH3B 3.06237188855065e-05 0.9362986505312 0.0636707257499143 isocitrate dehydrogenase 3 (NAD+) beta . DISEASE: Retinitis pigmentosa 46 (RP46) [MIM:612572]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:18806796}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;heart;umbilical cord;islets of Langerhans;colon;blood;skin;bone marrow;bile duct;breast;placenta;visual apparatus;liver;cervix;brain;stomach;cerebellum; dorsal root ganglion;whole brain;superior cervical ganglion;thalamus;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;cerebellum; 0.37949 0.23589 -0.402212257 26.7338995 43.26592 1.24865 IDH3G 0.968084888689833 0.0318643024439203 5.08088662471637e-05 isocitrate dehydrogenase 3 (NAD+) gamma . . . myocardium;lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;tonsil;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;amnion;head and neck;kidney;stomach;aorta;thymus;cerebellum; superior cervical ganglion;subthalamic nucleus;heart;globus pallidus;caudate nucleus;kidney;skeletal muscle; 0.08412 0.28307 0.060756528 58.52795471 199.97272 3.05494 IDI1 0.00205000884385519 0.912622232533407 0.0853277586227379 isopentenyl-diphosphate delta isomerase 1 FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000269|PubMed:8806705}.; . . . . 0.43575 0.13757 -0.251530012 35.42108988 92.82105 2.07034 IDI2 6.34065398267436e-09 0.0370722696932113 0.962927723966135 isopentenyl-diphosphate delta isomerase 2 FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000269|PubMed:17202134}.; . TISSUE SPECIFICITY: Detected in skeletal muscle. {ECO:0000269|PubMed:17202134}.; unclassifiable (Anatomical System);heart;ovary;urinary;colon;fovea centralis;choroid;lens;skeletal muscle;retina;breast;uterus;prostate;optic nerve;lung;bone;placenta;macula lutea;liver;testis;spleen;kidney;brain;aorta;stomach; . 0.14954 . -0.047654689 50.22410946 322.30406 3.81127 IDI2-AS1 . . . IDI2 antisense RNA 1 . . . . . . . . . . . IDNK 0.484632918227252 0.493395174688349 0.0219719070843987 idnK, gluconokinase homolog (E. coli) . . . . . 0.11598 0.13913 0.637604436 83.77565464 452.81398 4.42704 IDO1 1.41760011324181e-05 0.633219628410187 0.36676619558868 indoleamine 2,3-dioxygenase 1 FUNCTION: Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway (PubMed:17671174). Involved in the peripheral immune tolerance, contributing to maintain homeostasis by preventing autoimmunity or immunopathology that would result from uncontrolled and overreacting immune responses (PubMed:25691885). Tryptophan shortage inhibits T lymphocytes division and accumulation of tryptophan catabolites induces T-cell apoptosis and differentiation of regulatory T-cells (PubMed:25691885). Acts as a suppressor of anti-tumor immunity (PubMed:23103127, PubMed:25157255, PubMed:14502282, PubMed:25691885). Limits the growth of intracellular pathogens by depriving tryptophan (PubMed:25691885). Protects the fetus from maternal immune rejection (PubMed:25691885). {ECO:0000269|PubMed:14502282, ECO:0000269|PubMed:17671174, ECO:0000303|PubMed:23103127, ECO:0000303|PubMed:25157255, ECO:0000303|PubMed:25691885}.; . TISSUE SPECIFICITY: Expressed in mature dendritic cells located in lymphoid organs (including lymph nodes, spleen, tonsils, Peyers's patches, the gut lamina propria, and the thymic medulla), in some epithelial cells of the female genital tract, as well as in endothelial cells of term placenta and in lung parenchyma (PubMed:25691885). Weakly or not expressed in most normal tissues, but mostly inducible in most tissues (PubMed:25691885). Expressed in more than 50% of tumors, either by tumoral, stromal, or endothelial cells (expression in tumor is associated with a worse clinical outcome) (PubMed:18418598). Not overexpressed in tumor- draining lymph nodes (PubMed:26155395, PubMed:25691885). {ECO:0000269|PubMed:18418598, ECO:0000269|PubMed:25691885, ECO:0000269|PubMed:26155395}.; unclassifiable (Anatomical System);cartilage;ovary;colon;parathyroid;skeletal muscle;uterus;lung;endometrium;larynx;nasopharynx;bone;thyroid;placenta;alveolus;head and neck;kidney;stomach; placenta; 0.49311 0.43558 0.350995466 74.37485256 89.4479 2.03295 IDO2 9.40310162872685e-06 0.543737508587189 0.456253088311183 indoleamine 2,3-dioxygenase 2 FUNCTION: Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway (PubMed:17671174). Involved in immune regulation. May not play a significant role in tryptophan-related tumoral resistance (PubMed:25691885). {ECO:0000269|PubMed:17671174, ECO:0000303|PubMed:25691885}.; . TISSUE SPECIFICITY: Detected in liver, small intestine, spleen, placenta, thymus, lung, brain, kidney, and colon (PubMed:17671174). Also expressed at low level in testis and thyroid. Not expressed in the majority of human tumor samples (>99%) (PubMed:25691885). {ECO:0000269|PubMed:17671174, ECO:0000303|PubMed:25691885}.; . . 0.12033 . . . 12134.60935 23.61906 IDS 0.97925991869458 0.0207225577993061 1.75235061138504e-05 iduronate 2-sulfatase FUNCTION: Required for the lysosomal degradation of heparan sulfate and dermatan sulfate.; DISEASE: Mucopolysaccharidosis 2 (MPS2) [MIM:309900]: An X-linked lysosomal storage disease characterized by intracellular accumulation of heparan sulfate and dermatan sulfate and their excretion in urine. Most children with MPS2 have a severe form with early somatic abnormalities including skeletal deformities, hepatosplenomegaly, and progressive cardiopulmonary deterioration. A prominent feature is neurological damage that presents as developmental delay and hyperactivity but progresses to mental retardation and dementia. They die before 15 years of age, usually as a result of obstructive airway disease or cardiac failure. In contrast, those with a mild form of MPS2 may survive into adulthood, with attenuated somatic complications and often without mental retardation. {ECO:0000269|PubMed:10215411, ECO:0000269|PubMed:10220152, ECO:0000269|PubMed:10447264, ECO:0000269|PubMed:10671065, ECO:0000269|PubMed:11015461, ECO:0000269|PubMed:11683780, ECO:0000269|PubMed:11731225, ECO:0000269|PubMed:12655569, ECO:0000269|PubMed:12794697, ECO:0000269|PubMed:1284597, ECO:0000269|PubMed:1303211, ECO:0000269|PubMed:16699754, ECO:0000269|PubMed:7581397, ECO:0000269|PubMed:7599640, ECO:0000269|PubMed:7728156, ECO:0000269|PubMed:7866405, ECO:0000269|PubMed:7887413, ECO:0000269|PubMed:7981716, ECO:0000269|PubMed:8281149, ECO:0000269|PubMed:8566953, ECO:0000269|PubMed:8664909, ECO:0000269|PubMed:8830188, ECO:0000269|PubMed:8940265, ECO:0000269|PubMed:9222763, ECO:0000269|PubMed:9266380, ECO:0000269|PubMed:9375851, ECO:0000269|PubMed:9452044, ECO:0000269|PubMed:9501270, ECO:0000269|PubMed:9660053, ECO:0000269|PubMed:9762601, ECO:0000269|PubMed:9875019, ECO:0000269|PubMed:9921913, ECO:0000269|PubMed:9950361}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver, kidney, lung, and placenta.; smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;amygdala;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;fovea centralis;uterus;cerebral cortex;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; whole brain;amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.21576 0.25353 0.376678994 75.50719509 154.43873 2.71627 IDSP1 . . . iduronate 2-sulfatase pseudogene 1 . . . unclassifiable (Anatomical System);smooth muscle;frontal lobe;islets of Langerhans;trabecular meshwork;parathyroid;skeletal muscle; . . . . . . . IDUA 2.64182167327825e-08 0.478326206416257 0.521673767165526 iduronidase, alpha-L- . DISEASE: Mucopolysaccharidosis 1H (MPS1H) [MIM:607014]: A severe form of mucopolysaccharidosis type 1, a rare lysosomal storage disease characterized by progressive physical deterioration with urinary excretion of dermatan sulfate and heparan sulfate. Patients with MPS1H usually present, within the first year of life, a combination of hepatosplenomegaly, skeletal deformities, corneal clouding and severe mental retardation. Obstructive airways disease, respiratory infection and cardiac complications usually result in death before 10 years of age. {ECO:0000269|PubMed:10466419, ECO:0000269|PubMed:10735634, ECO:0000269|PubMed:12559846, ECO:0000269|PubMed:1301941, ECO:0000269|PubMed:15300847, ECO:0000269|PubMed:21394825, ECO:0000269|PubMed:7550232, ECO:0000269|PubMed:7550242, ECO:0000269|PubMed:7951228, ECO:0000269|PubMed:8019563, ECO:0000269|PubMed:8328452, ECO:0000269|PubMed:8401515, ECO:0000269|Ref.20}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mucopolysaccharidosis 1H/S (MPS1H/S) [MIM:607015]: A form of mucopolysaccharidosis type 1, a rare lysosomal storage disease characterized by progressive physical deterioration with urinary excretion of dermatan sulfate and heparan sulfate. MPS1H/S represents an intermediate phenotype of the MPS1 clinical spectrum. It is characterized by relatively little neurological involvement, but most of the somatic symptoms described for severe MPS1 develop in the early to mid-teens, causing considerable loss of mobility. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mucopolysaccharidosis 1S (MPS1S) [MIM:607016]: A mild form of mucopolysaccharidosis type 1, a rare lysosomal storage disease characterized by progressive physical deterioration with urinary excretion of dermatan sulfate and heparan sulfate. Patients with MPS1S may have little or no neurological involvement, normal stature and life span, but present development of joints stiffness, mild hepatosplenomegaly, aortic valve disease and corneal clouding. {ECO:0000269|PubMed:12559846, ECO:0000269|PubMed:15300847, ECO:0000269|PubMed:19396826, ECO:0000269|PubMed:21394825, ECO:0000269|PubMed:25256405, ECO:0000269|PubMed:7550232, ECO:0000269|PubMed:7550242, ECO:0000269|PubMed:8213840}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;pancreas;lung;trabecular meshwork;placenta;macula lutea;alveolus;spleen;head and neck;cervix;kidney;mammary gland; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.08409 0.09876 . . 2688.19258 9.75774 IER2 0.681051567438311 0.299241784918809 0.0197066476428798 immediate early response 2 FUNCTION: DNA-binding protein that seems to act as a transcription factor (PubMed:19584537). Involved in the regulation of neuronal differentiation, acts upon JNK-signaling pathway activation and plays a role in neurite outgrowth in hippocampal cells (By similarity). May mediate with FIBP FGF-signaling in the establishment of laterality in the embryo (By similarity). Promotes cell motility, seems to stimulate tumor metastasis (PubMed:22120713). {ECO:0000250|UniProtKB:B7SXM5, ECO:0000250|UniProtKB:Q6P7D3, ECO:0000269|PubMed:19584537, ECO:0000269|PubMed:22120713}.; . TISSUE SPECIFICITY: Expressed in activated T cells (at protein level) (PubMed:22120713). Expression increases in metastatic tumor cells (at protein level) (PubMed:22120713). {ECO:0000269|PubMed:22120713}.; umbilical cord;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;oral cavity;muscle;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; white blood cells; 0.07606 0.13082 . . 409.12002 4.23975 IER3 0.671461598838892 0.30711329036134 0.0214251107997684 immediate early response 3 FUNCTION: May play a role in the ERK signaling pathway by inhibiting the dephosphorylation of ERK by phosphatase PP2A- PPP2R5C holoenzyme. Acts also as an ERK downstream effector mediating survival. As a member of the NUPR1/RELB/IER3 survival pathway, may provide pancreatic ductal adenocarcinoma with remarkable resistance to cell stress, such as starvation or gemcitabine treatment. {ECO:0000269|PubMed:12356731, ECO:0000269|PubMed:16456541, ECO:0000269|PubMed:22565310}.; . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;amniotic fluid;bladder;unclassifiable (Anatomical System);trophoblast;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; . 0.04261 . . . 20.74499 0.70380 IER3IP1 0.0184346889412637 0.727994361214273 0.253570949844463 immediate early response 3 interacting protein 1 FUNCTION: May be implicated in the regulation of apoptosis. May be involved in protein transport between endoplasmic reticulum and Golgi apparatus (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highest levels in heart, skeletal muscle, and kidney. {ECO:0000269|PubMed:15276200}.; myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.30843 . 0.257356108 69.83368719 21.24503 0.71871 IER5 0.666267931394036 0.311334265188066 0.0223978034178981 immediate early response 5 . . . . . 0.07907 0.10373 . . 2285.7254 8.84614 IER5L 0.829266816302918 0.167138219576968 0.00359496412011383 immediate early response 5-like . . . . . 0.44323 . . . 1784.49436 7.79842 IFFO1 0.0207323486767856 0.975646234177527 0.00362141714568687 intermediate filament family orphan 1 . . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12032826}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;amniotic fluid;germinal center;brain;gall bladder;unclassifiable (Anatomical System);cartilage;blood;lens;skeletal muscle;lung;placenta;visual apparatus;liver;alveolus;spleen;kidney;stomach;thymus; dorsal root ganglion;ciliary ganglion;atrioventricular node;parietal lobe;cingulate cortex; 0.06679 0.09890 -0.424258538 25.56027365 119.73586 2.38208 IFFO2 0.382583916452741 0.57300016541486 0.0444159181323984 intermediate filament family orphan 2 . . . ovary;adrenal medulla;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;tongue;blood;lens;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach; cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;cerebellum; . . . . 254.06335 3.42814 IFI6 0.230931224633812 0.646185680661934 0.122883094704254 interferon, alpha-inducible protein 6 . . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;iris;testis;brain;pineal gland;unclassifiable (Anatomical System);trophoblast;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;liver;cervix;kidney;mammary gland;stomach; placenta; 0.16469 0.16042 . . 0.6571 0.01000 IFI16 0.00295604093058718 0.994497548161134 0.00254641090827843 interferon, gamma-inducible protein 16 FUNCTION: Binds double-stranded DNA. Binds preferentially to supercoiled DNA and cruciform DNA structures. Seems to be involved in transcriptional regulation. May function as a transcriptional repressor. Could have a role in the regulation of hematopoietic differentiation through activation of unknown target genes. Controls cellular proliferation by modulating the functions of cell cycle regulatory factors including p53/TP53 and the retinoblastoma protein. May be involved in TP53-mediated transcriptional activation by enhancing TP53 sequence-specific DNA binding and modulating TP53 phosphorylation status. Seems to be involved in energy-level-dependent activation of the ATM/ AMPK/TP53 pathway coupled to regulation of autophagy. May be involved in regulation of TP53-mediated cell death also involving BRCA1. May be involved in the senescence of prostate epithelial cells. Involved in innate immune response by recognizing viral dsDNA in the cytosol and probably in the nucleus. After binding to viral DNA in the cytoplasm recruits TMEM173/STING and mediates the induction of IFN-beta. Has anti-inflammatory activity and inhibits the activation of the AIM2 inflammasome, probably via association with AIM2. Proposed to bind viral DNA in the nucleus, such as of Kaposi's sarcoma-associated herpesvirus, and to induce the formation of nuclear caspase-1-activating inflammasome formation via association with PYCARD. Inhibits replication of herpesviruses such as human cytomegalovirus (HCMV) probably by interfering with promoter recruitment of members of the Sp1 family of transcription factors. Necessary to activate the IRF3 signaling cascade during human herpes simplex virus 1 (HHV-1) infection and promotes the assembly of heterochromatin on herpesviral DNA and inhibition of viral immediate-early gene expression and replication. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. {ECO:0000269|PubMed:11146555, ECO:0000269|PubMed:12894224, ECO:0000269|PubMed:14654789, ECO:0000269|PubMed:20890285, ECO:0000269|PubMed:21573174, ECO:0000269|PubMed:21575908, ECO:0000269|PubMed:22046441, ECO:0000269|PubMed:22291595, ECO:0000269|PubMed:23027953, ECO:0000269|PubMed:24198334, ECO:0000269|PubMed:24413532, ECO:0000269|PubMed:9642285}.; . TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes, fibroblasts and lymphoid cells. Present in myeloid precursors (CD34+) and throughout monocyte development, but its expression is down-regulated in erythroid and polymorphonuclear precursor cells. Present in prostate, ovary and breast (at protein level). {ECO:0000269|PubMed:12894224}.; lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; superior cervical ganglion;white blood cells;ciliary ganglion;whole blood;trigeminal ganglion; 0.12757 0.10480 1.401792296 94.75112055 802.10147 5.57967 IFI27 0.0561856088767235 0.707684750802045 0.236129640321231 interferon, alpha-inducible protein 27 FUNCTION: Promotes cell death. Mediates IFN-induced apoptosis characterized by a rapid and robust release of cytochrome C from the mitochondria and activation of BAX and caspases 2, 3, 6, 8 and 9. {ECO:0000269|PubMed:18330707}.; . . myocardium;ovary;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;synovium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);heart;tongue;pharynx;skeletal muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; . 0.03920 0.06470 0.369407109 74.95281906 515.79903 4.64537 IFI27L1 0.076473377797993 0.749236719913244 0.174289902288763 interferon, alpha-inducible protein 27-like 1 . . . . . 0.01638 0.04895 0.080983847 59.76055674 76.97751 1.84182 IFI27L2 0.00150740100387573 0.442566185834925 0.555926413161199 interferon, alpha-inducible protein 27-like 2 . . . myocardium;ovary;salivary gland;intestine;colon;skin;uterus;prostate;oesophagus;larynx;bone;iris;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland; . 0.02306 . -0.075159878 47.78839349 20.98106 0.71007 IFI30 2.60170027654508e-05 0.315188047062933 0.684785935934301 interferon, gamma-inducible protein 30 FUNCTION: Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing. Facilitates the generation of MHC class II- restricted epitodes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds (By similarity). Facilitates also MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation (By similarity). {ECO:0000250}.; . . . . 0.37595 . -0.093566408 46.7386176 897.47181 5.83669 IFI35 5.69697011611625e-08 0.129737829255606 0.870262113774693 interferon induced protein 35 FUNCTION: Not yet known.; . TISSUE SPECIFICITY: In a wide range of cell types, including fibroblasts, macrophages, and epithelial cells.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;blood;lens;pancreas;lung;placenta;macula lutea;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.05827 0.09824 0.308721233 72.59966973 303.98626 3.71410 IFI44 4.72292352590193e-14 0.00677427042044323 0.993225729579509 interferon induced protein 44 FUNCTION: This protein aggregates to form microtubular structures. {ECO:0000250}.; . . . . 0.04109 0.07673 -0.843147538 11.2762444 247.60339 3.39404 IFI44L 2.21842256623261e-10 0.0367640910140099 0.963235908764148 interferon induced protein 44 like FUNCTION: Exhibits a low antiviral activity against hepatitis C virus. {ECO:0000269|PubMed:21478870}.; . . lymphoreticular;colon;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cerebellum cortex;tongue;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach; . 0.07603 0.07964 1.734373503 96.61476763 2286.09816 8.84784 IFIH1 6.00238931195841e-26 4.60023510099727e-05 0.99995399764899 interferon induced, with helicase C domain 1 FUNCTION: Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. Its ligands include mRNA lacking 2'-O- methylation at their 5' cap and long-dsRNA (>1 kb in length). Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Responsible for detecting the Picornaviridae family members such as encephalomyocarditis virus (EMCV) and mengo encephalomyocarditis virus (ENMG). Can also detect other viruses such as dengue virus (DENV), west Nile virus (WNV), and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome, such as vaccinia virus. Plays an important role in amplifying innate immune signaling through recognition of RNA metabolites that are produced during virus infection by ribonuclease L (RNase L). May play an important role in enhancing natural killer cell function and may be involved in growth inhibition and apoptosis in several tumor cell lines. {ECO:0000269|PubMed:14645903, ECO:0000269|PubMed:19211564, ECO:0000269|PubMed:19656871, ECO:0000269|PubMed:21217758, ECO:0000269|PubMed:21742966}.; DISEASE: Diabetes mellitus, insulin-dependent, 19 (IDDM19) [MIM:610155]: A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:16699517}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; DISEASE: Note=IFIH1 is the CADM-140 autoantigen, involved in clinically amyopathic dermatomyositis (CADM). This is a chronic inflammatory disorder that shows typical skin manifestations of dermatomyositis but has no or little evidence of clinical myositis. Anti-CADM-140 antibodies appear to be specific to dermatomyositis, especially CADM. Patients with anti-CADM-140 antibodies frequently develop life-threatening acute progressive interstitial lung disease (ILD). {ECO:0000269|PubMed:19565506, ECO:0000269|PubMed:20015976}.; DISEASE: Aicardi-Goutieres syndrome 7 (AGS7) [MIM:615846]: A form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood. {ECO:0000269|PubMed:24686847, ECO:0000269|PubMed:24995871}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Singleton-Merten syndrome 1 (SGMRT1) [MIM:182250]: An autosomal dominant disorder with variable expression. Core features are marked aortic calcification, dental anomalies, osteopenia, acro-osteolysis, and to a lesser extend glaucoma, psoriasis, muscle weakness, and joint laxity. Dental anomalies include delayed eruption and immature root formation of anterior permanent teeth, early loss of permanent teeth due to short roots, acute root resorption, high caries, and aggressive alveolar bone loss. Additional clinical manifestations include particular facial characteristics and abnormal joint and muscle ligaments. {ECO:0000269|PubMed:25620204}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, at a low level. Expression is detected at slightly highest levels in placenta, pancreas and spleen and at barely levels in detectable brain, testis and lung. {ECO:0000269|PubMed:11805321, ECO:0000269|PubMed:12015121, ECO:0000269|PubMed:14645903}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;colon;skeletal muscle;breast;uterus;pancreas;lung;endometrium;bone;thyroid;placenta;duodenum;testis;cervix;germinal center;kidney;brain;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.57579 0.25181 0.96630192 90.19815994 4469.67513 13.40960 IFIT1 0.00534820018141597 0.893560115036222 0.101091684782362 interferon induced protein with tetratricopeptide repeats 1 FUNCTION: Interferon-induced antiviral RNA-binding protein that specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single- stranded RNAs and inhibiting expression of viral messenger RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Exhibits antiviral activity against several viruses including human papilloma and hepatitis C viruses. {ECO:0000269|PubMed:19008854, ECO:0000269|PubMed:19416887, ECO:0000269|PubMed:21976647, ECO:0000269|PubMed:23334420}.; . . . . 0.12073 0.10969 -0.514264485 21.41424864 33.96624 1.04283 IFIT1B 7.25641577038389e-09 0.0760489882872932 0.923951004456291 interferon induced protein with tetratricopeptide repeats 1B . . . . . 0.07276 . 0.420771676 77.15852795 264.85487 3.49217 IFIT1P1 . . . interferon induced protein with tetratricopeptide repeats 1 pseudogene 1 . . . . . . . . . . . IFIT2 0.00148220080965614 0.875620861128731 0.122896938061613 interferon induced protein with tetratricopeptide repeats 2 FUNCTION: IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O- methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5' triphosphorylation, RNA-binding is required for antiviral activity. Can promote apoptosis. {ECO:0000269|PubMed:21190939}.; . . . . 0.08534 0.14909 0.619191319 83.36282142 867.68549 5.73654 IFIT3 0.00442653331666044 0.870961044508861 0.124612422174478 interferon induced protein with tetratricopeptide repeats 3 FUNCTION: IFN-induced antiviral protein which acts as an inhibitor of cellular as well as viral processes, cell migration, proliferation, signaling, and viral replication. Enhances MAVS- mediated host antiviral responses by serving as an adapter bridging TBK1 to MAVS which leads to the activation of TBK1 and phosphorylation of IRF3 and phosphorylated IRF3 translocates into nucleus to promote antiviral gene transcription. Exihibits an antiproliferative activity via the up-regulation of cell cycle negative regulators CDKN1A/p21 and CDKN1B/p27. Normally, CDKN1B/p27 turnover is regulated by COPS5, which binds CDKN1B/p27 in the nucleus and exports it to the cytoplasm for ubiquitin- dependent degradation. IFIT3 sequesters COPS5 in the cytoplasm, thereby increasing nuclear CDKN1B/p27 protein levels. Upregulates CDKN1A/p21 by downregulating MYC, a repressor of CDKN1A/p21. Can negatively regulate the apoptotic effects of IFIT2. {ECO:0000269|PubMed:17050680, ECO:0000269|PubMed:20686046, ECO:0000269|PubMed:21190939, ECO:0000269|PubMed:21642987, ECO:0000269|PubMed:21813773}.; . TISSUE SPECIFICITY: Expression significantly higher in peripheral blood mononuclear cells (PBMCs) and monocytes from systemic lupus erythematosus (SLE) patients than in those from healthy individuals (at protein level). Spleen, lung, leukocytes, lymph nodes, placenta, bone marrow and fetal liver. {ECO:0000269|PubMed:18706081}.; . . 0.02396 0.12703 0.108486928 61.90728946 205.99955 3.10276 IFIT5 0.0581423496290215 0.924222160208213 0.0176354901627652 interferon induced protein with tetratricopeptide repeats 5 FUNCTION: Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP- RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs. {ECO:0000269|PubMed:23317505, ECO:0000269|PubMed:23334420}.; . . . . 0.11264 0.11163 -0.003562597 53.72729417 290.57209 3.64725 IFIT6P . . . interferon induced protein with tetratricopeptide repeats 6, pseudogene . . . . . . . . . . . IFITM1 0.221686062595446 0.647406042897099 0.130907894507454 interferon induced transmembrane protein 1 FUNCTION: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1) and hepatitis C virus (HCV). Can inhibit: influenza virus hemagglutinin protein- mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S protein-mediated viral entry. Also implicated in cell adhesion and control of cell growth and migration. Plays a key role in the antiproliferative action of IFN-gamma either by inhibiting the ERK activation or by arresting cell growth in G1 phase in a p53-dependent manner. Acts as a positive regulator of osteoblast differentiation. {ECO:0000269|PubMed:16847454, ECO:0000269|PubMed:20064371, ECO:0000269|PubMed:20838853, ECO:0000269|PubMed:21177806, ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:21976647, ECO:0000269|PubMed:22479637, ECO:0000269|PubMed:22634173}.; . TISSUE SPECIFICITY: Bone (at protein level). Levels greatly elevated in colon cancer, cervical cancer, esophageal cancer and ovarian cancer. Expressed in glioma cell lines. {ECO:0000269|PubMed:20838853, ECO:0000269|PubMed:22634173}.; lymphoreticular;smooth muscle;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;epididymis;nasopharynx;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; . 0.53827 0.09041 -0.361761279 28.6329323 3.82348 0.14128 IFITM2 0.299375900397776 0.623140630100005 0.0774834695022185 interferon induced transmembrane protein 2 FUNCTION: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1) and vesicular stomatitis virus (VSV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry, SARS-CoV S protein-mediated viral entry and VSV G protein- mediated viral entry. Induces cell cycle arrest and mediates apoptosis by caspase activation and in p53-independent manner. {ECO:0000269|PubMed:19544527, ECO:0000269|PubMed:20064371, ECO:0000269|PubMed:20534863, ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:21177806, ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:22479637}.; . . myocardium;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;iris;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;trophoblast;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;placenta;hypopharynx;head and neck;kidney;stomach;aorta; liver;atrioventricular node;trigeminal ganglion;whole blood; 0.23271 . 0.305084559 72.22811984 8.09946 0.29681 IFITM3 0.199202473288833 0.647887178150543 0.152910348560625 interferon induced transmembrane protein 3 FUNCTION: IFN-induced antiviral protein which disrupts intracellular cholesterol homeostasis. Inhibits the entry of viruses to the host cell cytoplasm by preventing viral fusion with cholesterol depleted endosomes. May inactivate new enveloped viruses which buds out of the infected cell, by letting them go out with a cholesterol depleted membrane. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV) and Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1) and vesicular stomatitis virus (VSV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2- mediated viral entry, SARS-CoV S protein-mediated viral entry and VSV G protein-mediated viral entry. Plays a critical role in the structural stability and function of vacuolar ATPase (v-ATPase). Establishes physical contact with the v-ATPase of endosomes which is critical for proper clathrin localization and is also required for the function of the v-ATPase to lower the pH in phagocytic endosomes thus establishing an antiviral state. {ECO:0000269|PubMed:20064371, ECO:0000269|PubMed:20534863, ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:21177806, ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:22046135, ECO:0000269|PubMed:22479637, ECO:0000269|PubMed:23601107}.; . . . . . . 0.125076652 62.7388535 123.10673 2.41680 IFITM4P . . . interferon induced transmembrane protein 4 pseudogene . . . . . . . . . . . IFITM5 0.000115704605462658 0.216218274285868 0.783666021108669 interferon induced transmembrane protein 5 FUNCTION: Required for normal bone mineralization. {ECO:0000269|PubMed:24519609}.; DISEASE: Osteogenesis imperfecta 5 (OI5) [MIM:610967]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI5 patients manifest moderate to severe bone fragility, calcification of the forearm interosseous membrane, radial head dislocation, a subphyseal metaphyseal radiodense line, and hyperplastic callus formation. {ECO:0000269|PubMed:22863190}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in bone (PubMed:24058703). Detected in osteoblasts and fibroblasts (at protein level) (PubMed:24519609). Detected in bone (PubMed:24058703). Detected in osteoblasts and fibroblasts (PubMed:24519609). {ECO:0000269|PubMed:24058703, ECO:0000269|PubMed:24519609}.; . . 0.16716 0.10951 0.150760231 64.51403633 49.76081 1.38303 IFITM8P . . . interferon induced transmembrane protein 8 pseudogene . . . . . . . . . . . IFITM9P . . . interferon induced transmembrane protein 9 pseudogene . . . . . . . . . . . IFITM10 . . . interferon induced transmembrane protein 10 . . . unclassifiable (Anatomical System);cartilage;ovary;tongue;hypothalamus;salivary gland;parathyroid;fovea centralis;choroid;lens;retina;pancreas;optic nerve;lung;larynx;bone;placenta;macula lutea;liver;head and neck;spleen;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;adrenal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; . . . . 93.13184 2.07535 IFNA1 0.711485383815355 0.273631157098527 0.0148834590861176 interferon, alpha 1 FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. {ECO:0000269|PubMed:1634550}.; . . . . 0.03504 0.07606 0.281220278 71.07808445 798.7805 5.57085 IFNA2 0.0445894041680805 0.668728285101939 0.28668231072998 interferon, alpha 2 FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities.; . . . . 0.03870 0.06599 0.461228372 78.46190139 62.55796 1.61667 IFNA4 0.240444347478374 0.644380291242427 0.115175361279199 interferon, alpha 4 FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.; . . . . 0.05206 . 1.060147109 91.46614768 294.68336 3.66580 IFNA5 0.00683606087118389 0.522796704704948 0.470367234423868 interferon, alpha 5 FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.; . . . . 0.01857 . 0.681699246 84.93158764 126.14211 2.44400 IFNA6 0.000913991156173349 0.350958271901695 0.648127736942132 interferon, alpha 6 FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.; . . . . 0.05022 . 0.148941568 64.31941496 13.95116 0.50576 IFNA7 9.01848744740703e-05 0.189291661751114 0.810618153374412 interferon, alpha 7 FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.; . . . . 0.03655 . 1.038098315 91.20665251 30.6513 0.97504 IFNA8 2.11513003983028e-06 0.0810122822394563 0.918985602630504 interferon, alpha 8 FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.; . . . . 0.00971 0.07910 -0.007201372 53.19061099 135.38375 2.53142 IFNA10 0.00187253447928596 0.486192194492717 0.511935271027997 interferon, alpha 10 FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.; . . . . 0.01351 . 1.728918179 96.55579146 888.2318 5.80615 IFNA11P . . . interferon, alpha 11, pseudogene . . . . . . . . . . . IFNA12P . . . interferon, alpha 12, pseudogene . . . . . . . . . . . IFNA13 0.711459503244693 0.273653323168301 0.0148871735870057 interferon, alpha 13 FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. {ECO:0000269|PubMed:1634550}.; . . . . 0.03721 0.13119 0.147123112 64.11299835 9.90896 0.36293 IFNA14 . . . interferon, alpha 14 FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. {ECO:0000269|PubMed:1634550}.; . . . . 0.07087 0.12159 -0.380166007 27.88393489 59.38996 1.56287 IFNA16 0.00656986926455156 0.514496975336133 0.478933155399316 interferon, alpha 16 FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.; . . . . 0.02358 0.07478 1.26221942 93.55980184 148.8458 2.66019 IFNA17 0.00702582209296288 0.528540961721766 0.464433216185271 interferon, alpha 17 FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. {ECO:0000269|PubMed:1634550}.; . . . . 0.03731 0.59320 0.461228372 78.46190139 360.76195 4.02023 IFNA20P . . . interferon, alpha 20, pseudogene . . . . . . . . . . . IFNA21 8.62552167583039e-08 0.0242673088880292 0.975732604856754 interferon, alpha 21 FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. {ECO:0000269|PubMed:1634550}.; . . . . 0.04610 0.08169 1.172206761 92.69874971 77.2088 1.84522 IFNA22P . . . interferon, alpha 22, pseudogene . . . . . . . . . . . IFNAR1 0.000620329691645639 0.976461236217923 0.0229184340904316 interferon alpha and beta receptor subunit 1 FUNCTION: Component of the receptor for type I interferons, including interferons alpha, IFNB1 and IFNW1 (PubMed:2153461, PubMed:7665574, PubMed:10049744, PubMed:14532120, PubMed:15337770, PubMed:21854986). Functions in general as heterodimer with IFNAR2 (PubMed:7665574, PubMed:10049744, PubMed:21854986). Type I interferon binding activates the JAK-STAT signaling cascade, and triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and the IFNR alpha- and beta- subunits themselves (PubMed:7665574, PubMed:21854986). Can form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway (By similarity). {ECO:0000250|UniProtKB:P33896, ECO:0000269|PubMed:10049744, ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:15337770, ECO:0000269|PubMed:19561067, ECO:0000269|PubMed:2153461, ECO:0000269|PubMed:7665574, ECO:0000305|PubMed:21854986}.; . TISSUE SPECIFICITY: IFN receptors are present in all tissues and even on the surface of most IFN-resistant cells. Isoform 1, isoform 2 and isoform 3 are expressed in the IFN-alpha sensitive myeloma cell line U266B1. Isoform 2 and isoform 3 are expressed in the IFN-alpha resistant myeloma cell line U266R. Isoform 1 is not expressed in IFN-alpha resistant myeloma cell line U266R. {ECO:0000269|PubMed:8307198}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;gum;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;spinal cord;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;amnion;spleen;head and neck;kidney;stomach; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.09415 0.07419 0.042348793 57.31304553 1195.3526 6.56142 IFNAR2 0.00506602558328155 0.968060630018663 0.0268733443980551 interferon alpha and beta receptor subunit 2 FUNCTION: Associates with IFNAR1 to form the type I interferon receptor. Receptor for interferons alpha and beta. Involved in IFN-mediated STAT1, STAT2 and STAT3 activation. Isoform 1 and isoform 2 are directly involved in signal transduction due to their association with the TYR kinase, JAK1 (PubMed:8181059, PubMed:7665574, PubMed:7759950). Isoform 3 is a potent inhibitor of type I IFN receptor activity (PubMed:7759950). {ECO:0000269|PubMed:10049744, ECO:0000269|PubMed:11682488, ECO:0000269|PubMed:12105218, ECO:0000269|PubMed:7665574, ECO:0000269|PubMed:7759950, ECO:0000269|PubMed:8181059}.; . TISSUE SPECIFICITY: Isoform 3 is detected in the urine (at protein level) (PubMed:8181059, PubMed:7759950). Expressed in blood cells. Expressed in lymphoblastoid and fibrosarcoma cell lines. {ECO:0000269|PubMed:7588638, ECO:0000269|PubMed:7759950, ECO:0000269|PubMed:8181059}.; unclassifiable (Anatomical System);lymph node;ovary;heart;lacrimal gland;islets of Langerhans;colon;parathyroid;blood;skin;bone marrow;breast;bile duct;prostate;pancreas;whole body;lung;thyroid;placenta;visual apparatus;duodenum;liver;testis;spleen;kidney;brain; dorsal root ganglion;superior cervical ganglion;temporal lobe;ciliary ganglion;white blood cells;atrioventricular node;skin; 0.07382 0.31770 0.156217551 64.82071243 425.03001 4.30687 IFNB1 0.0136944375935193 0.66948273081327 0.316822831593211 interferon, beta 1, fibroblast FUNCTION: Has antiviral, antibacterial and anticancer activities.; . . . . 0.07684 0.09138 0.415317661 76.81056853 35.51631 1.07116 IFNE 8.78738642634286e-07 0.0925359704741728 0.907463150787185 interferon, epsilon FUNCTION: Type I interferon required for maintaining basal levels of IFN-regulated genes, including 2'-5'-oligoadenylate synthetase, IRF7 and ISG15, in the female reproductive tract. Directly mediates protection against viral and bacterial genital infections (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Endometrium-specific. {ECO:0000269|PubMed:23449591}.; . . . . 0.637604436 83.77565464 308.88585 3.74134 IFNG 0.0204465656775392 0.904517046515695 0.0750363878067654 interferon, gamma FUNCTION: Produced by lymphocytes activated by specific antigens or mitogens. IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions. It is a potent activator of macrophages, it has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.; DISEASE: Aplastic anemia (AA) [MIM:609135]: A form of anemia in which the bone marrow fails to produce adequate numbers of peripheral blood elements. It is characterized by peripheral pancytopenia and marrow hypoplasia. {ECO:0000269|PubMed:15327519}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Released primarily from activated T lymphocytes.; unclassifiable (Anatomical System);lymph node;lung;testis;blood;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.13345 0.99877 -0.031067188 51.03798066 2.1884 0.07277 IFNG-AS1 . . . IFNG antisense RNA 1 . . . . . . . . . . . IFNGR1 0.327969027338138 0.668725776304575 0.00330519635728746 interferon gamma receptor 1 FUNCTION: Receptor for interferon gamma. Two receptors bind one interferon gamma dimer.; DISEASE: Immunodeficiency 27A (IMD27A) [MIM:209950]: A form of Mendelian susceptibility to mycobacterial disease, a rare condition caused by impairment of interferon-gamma mediated immunity. It is characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. Clinical outcome severity depends on the degree of impairment of interferon-gamma mediated immunity. Some patients die of overwhelming mycobacterial disease with lepromatous-like lesions in early childhood, whereas others develop, later in life, disseminated but curable infections with tuberculoid granulomas. {ECO:0000269|PubMed:10811850, ECO:0000269|PubMed:9389728}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Immunodeficiency 27B (IMD27B) [MIM:615978]: A form of Mendelian susceptibility to mycobacterial disease, a rare condition caused by impairment of interferon-gamma mediated immunity. It is characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. Clinical outcome severity depends on the degree of impairment of interferon-gamma mediated immunity. Some patients die of overwhelming mycobacterial disease with lepromatous-like lesions in early childhood, whereas others develop, later in life, disseminated but curable infections with tuberculoid granulomas. IMD27B commonly presents with recurrent, moderately severe infections with environmental mycobacteria or BCG. Salmonellosis is present in about 5% of patients. {ECO:0000269|PubMed:10192386}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.50087 0.51837 -0.200157416 39.11299835 429.70695 4.32908 IFNGR2 0.881281108961234 0.118430869750543 0.000288021288222903 interferon gamma receptor 2 (interferon gamma transducer 1) FUNCTION: Part of the receptor for interferon gamma. Required for signal transduction. This accessory factor is an integral part of the IFN-gamma signal transduction pathway and is likely to interact with GAF, JAK1, and/or JAK2.; DISEASE: Immunodeficiency 28 (IMD28) [MIM:614889]: A form of Mendelian susceptibility to mycobacterial disease, a rare condition caused by impairment of interferon-gamma mediated immunity. It is characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. Clinical outcome severity depends on the degree of impairment of interferon-gamma mediated immunity. Some patients die of overwhelming mycobacterial disease with lepromatous-like lesions in early childhood, whereas others develop, later in life, disseminated but curable infections with tuberculoid granulomas. IMD28 manifests early in life, with severe, often fatal, infection. {ECO:0000269|PubMed:15924140}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;pancreas;lung;placenta;head and neck;kidney;stomach;aorta; whole blood; 0.10337 0.16292 0.663285274 84.55414013 349.45734 3.96123 IFNK 9.61085354448357e-09 0.0247127231491458 0.97528726724 interferon, kappa FUNCTION: May play a role in the regulation of immune cell function. Cytokine that imparts cellular protection against viral infection in a species-specific manner. Activates the interferon- stimulated response element signaling pathway. It is able to directly modulate cytokine release from monocytes and dendritic cells. Binds heparin. {ECO:0000269|PubMed:11514542, ECO:0000269|PubMed:12391192}.; . TISSUE SPECIFICITY: Expressed in keratinocytes, monocytes and in resting dendritic cells. {ECO:0000269|PubMed:11514542, ECO:0000269|PubMed:12391192}.; uterus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16671 0.18311 0.459411326 78.28497287 356.76057 4.00010 IFNL1 2.82388297192014e-05 0.328192910002823 0.671778851167458 interferon, lambda 1 FUNCTION: Cytokine with antiviral, antitumour and immunomodulatory activities. Plays a critical role in the antiviral host defense, predominantly in the epithelial tissues. Acts as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1, and receptor engagement leads to the activation of the JAK/STAT signaling pathway resulting in the expression of IFN- stimulated genes (ISG), which mediate the antiviral state. Has a restricted receptor distribution and therefore restricted targets: is primarily active in epithelial cells and this cell type- selective action is because of the epithelial cell-specific expression of its receptor IFNLR1. Exerts an immunomodulatory effect by up-regulating MHC class I antigen expression.; . . . . 0.06822 . 0.082802743 60.09082331 17.80532 0.62206 IFNL2 1.95487204221475e-05 0.272941566445678 0.7270388848339 interferon, lambda 2 FUNCTION: Cytokine with antiviral, antitumour and immunomodulatory activities. Plays a critical role in the antiviral host defense, predominantly in the epithelial tissues. Acts as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1, and receptor engagement leads to the activation of the JAK/STAT signaling pathway resulting in the expression of IFN- stimulated genes (ISG), which mediate the antiviral state. Has a restricted receptor distribution and therefore restricted targets: is primarily active in epithelial cells and this cell type- selective action is because of the epithelial cell-specific expression of its receptor IFNLR1. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium. Exerts an immunomodulatory effect by up-regulating MHC class I antigen expression. {ECO:0000269|PubMed:12469119, ECO:0000269|PubMed:12483210, ECO:0000269|PubMed:16539846}.; . . . . 0.07551 0.10417 1.128108522 92.19155461 1357.08469 6.91223 IFNL3 1.15936762956742e-05 0.207790472369262 0.792197933954443 interferon, lambda 3 FUNCTION: Cytokine with antiviral, antitumour and immunomodulatory activities. Plays a critical role in the antiviral host defense, predominantly in the epithelial tissues. Acts as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1, and receptor engagement leads to the activation of the JAK/STAT signaling pathway resulting in the expression of IFN- stimulated genes (ISG), which mediate the antiviral state. Has a restricted receptor distribution and therefore restricted targets: is primarily active in epithelial cells and this cell type- selective action is because of the epithelial cell-specific expression of its receptor IFNLR1. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium. Exerts an immunomodulatory effect by up-regulating MHC class I antigen expression. {ECO:0000269|PubMed:12469119, ECO:0000269|PubMed:12483210}.; . . . . 0.03985 0.10111 1.284269037 93.76621845 958.54254 5.99271 IFNL3P1 . . . interferon, lambda 3 pseudogene 1 . . . . . . . . . . . IFNL4 . . . interferon, lambda 4 (gene/pseudogene) FUNCTION: Cytokine that may trigger an antiviral response activating the JAK-STAT pathway and up-regulating specifically some interferon-stimulated genes. {ECO:0000269|PubMed:23291588}.; . . . . . . . . . . IFNL4P1 . . . interferon, lambda 4 pseudogene 1 . . . . . . . . . . . IFNLR1 0.308615221609601 0.6875259516287 0.00385882676169887 interferon, lambda receptor 1 FUNCTION: The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state. Determines the cell type specificity of the lambda interferon action. Shows a more restricted pattern of expression in the epithelial tissues thereby limiting responses to lambda interferons primarily to epithelial cells of the respiratory, gastrointestinal, and reproductive tracts. Seems not to be essential for early virus- activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium. {ECO:0000269|PubMed:12469119, ECO:0000269|PubMed:12483210, ECO:0000269|PubMed:12521379}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12469119, ECO:0000269|PubMed:12483210}.; . . 0.14311 0.11073 -0.089927255 46.99221515 84.33903 1.95528 IFNNP1 . . . interferon, nu 1, pseudogene . . . . . . . . . . . IFNR . . . interferon production regulator . . . . . . . . . . . IFNW1 0.00616591505034941 0.501326648020954 0.492507436928697 interferon, omega 1 . . . . . 0.05188 0.08230 -0.137658575 43.57159707 158.29096 2.74834 IFNWP2 . . . interferon, omega 1 pseudogene 2 . . . . . . . . . . . IFNWP4 . . . interferon, omega 1 pseudogene 4 . . . . . . . . . . . IFNWP5 . . . interferon, omega 1 pseudogene 5 . . . . . . . . . . . IFNWP9 . . . interferon, omega 1 pseudogene 9 . . . . . . . . . . . IFNWP15 . . . interferon, omega 1 pseudogene 15 . . . . . . . . . . . IFNWP18 . . . interferon, omega 1 pseudogene 18 . . . . . . . . . . . IFNWP19 . . . interferon, omega 1 pseudogene 19 . . . . . . . . . . . IFRD1 0.105462456846984 0.893141243467555 0.0013962996854606 interferon related developmental regulator 1 FUNCTION: Could play a role in regulating gene activity in the proliferative and/or differentiative pathways induced by NGF. May be an autocrine factor that attenuates or amplifies the initial ligand-induced signal (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in a variety of tissues.; ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;oral cavity;urinary;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;visual apparatus;liver;spleen;head and neck;cervix;mammary gland;stomach;peripheral nerve;cerebellum; . 0.62527 0.12486 -0.381986487 27.68931352 36.72611 1.10139 IFRD2 5.52609563426163e-06 0.670293634262521 0.329700839641845 interferon-related developmental regulator 2 . . TISSUE SPECIFICITY: Expressed in a variety of tissues.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;gum;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;liver;skeletal muscle; 0.21662 0.13992 0.20030965 67.3566879 745.62592 5.41897 IFT20 0.482557826616381 0.495143206519978 0.0222989668636412 intraflagellar transport 20 FUNCTION: Part of intraflagellar transport (IFT) particles involved in ciliary process assembly. May play a role in the trafficking of ciliary membrane proteins from the Golgi complex to the cilium. Also involved in autophagy since it is required for trafficking of ATG16L and the expansion of the autophagic compartment. {ECO:0000269|PubMed:16775004}.; . TISSUE SPECIFICITY: Expressed in almost all tissues. {ECO:0000269|PubMed:14672413}.; lymphoreticular;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;muscle;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;head and neck;spleen;kidney;mammary gland;aorta;stomach; testis - interstitial;testis - seminiferous tubule;testis;globus pallidus; 0.19220 0.10501 -0.09720619 46.20193442 65.03627 1.65811 IFT22 . . . intraflagellar transport 22 FUNCTION: Small GTPase-like component of the intraflagellar transport (IFT) complex B. {ECO:0000250}.; . . . . 0.16294 0.10657 -0.207437529 38.2814343 . . IFT27 0.000880890777082489 0.79443497102137 0.204684138201547 intraflagellar transport 27 FUNCTION: Small GTPase-like component of the intraflagellar transport (IFT) complex B that promotes the exit of the BBSome complex from cilia via its interaction with ARL6 (PubMed:25443296). Not involved in entry of the BBSome complex into cilium. Prevents aggregation of GTP-free ARL6 (PubMed:25443296). Required for hedgehog signaling. Forms a subcomplex within the IFT complex B with IFT25 (By similarity). {ECO:0000250|UniProtKB:A8HN58, ECO:0000269|PubMed:25443296}.; DISEASE: Bardet-Biedl syndrome 19 (BBS19) [MIM:615996]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:24488770}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;adrenal cortex;lens;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.03165 0.08118 0.393270925 76.04977589 167.91204 2.82937 IFT43 4.37841580307519e-07 0.376444964987201 0.623554597171219 intraflagellar transport 43 FUNCTION: Component of IFT complex A (IFT-A) involved in retrograde ciliary transport along microtubules from the ciliary tip to the base. {ECO:0000269|PubMed:21378380}.; DISEASE: Cranioectodermal dysplasia 3 (CED3) [MIM:614099]: A disorder primarily characterized by craniofacial, skeletal and ectodermal abnormalities. Clinical features include craniosynostosis, narrow rib cage, short limbs, brachydactyly, hypoplastic and widely spaced teeth, sparse hair, skin laxity and abnormal nails. Nephronophthisis leading to progressive renal failure, hepatic fibrosis, heart defects, and retinitis pigmentosa have also been described. {ECO:0000269|PubMed:21378380}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;oesophagus;endometrium;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;alveolus;spleen;kidney;mammary gland;stomach;aorta; testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;parietal lobe; 0.24823 . -0.249709319 35.74545883 1030.15105 6.16463 IFT46 0.950870755108113 0.0490990043132432 3.02405786439858e-05 intraflagellar transport 46 FUNCTION: Forms part of a complex involved in intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia. May play a role in chondrocyte maturation and skeletogenesis (By similarity). {ECO:0000250}.; . . ovary;choroid;skin;retina;bone marrow;uterus;prostate;cerebral cortex;endometrium;bone;thyroid;iris;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;bile duct;breast;pancreas;pia mater;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;globus pallidus;atrioventricular node;pons;trigeminal ganglion;cingulate cortex; 0.09445 0.08875 0.218717575 68.27081859 2672.94319 9.72010 IFT52 0.00016303013234085 0.968842778389026 0.0309941914786329 intraflagellar transport 52 FUNCTION: Forms part of a complex involved in intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia. {ECO:0000250}.; . . . . 0.35584 0.10874 -0.558357437 19.54470394 70.28495 1.74252 IFT57 4.07945731178608e-06 0.827609780057467 0.172386140485221 intraflagellar transport 57 FUNCTION: Required for the formation of cilia. Plays an indirect role in sonic hedgehog signaling, cilia being required for all activity of the hedgehog pathway (By similarity). Has pro- apoptotic function via its interaction with HIP1, leading to recruit caspase-8 (CASP8) and trigger apoptosis. Has the ability to bind DNA sequence motif 5'-AAAGACATG-3' present in the promoter of caspase genes such as CASP1, CASP8 and CASP10, suggesting that it may act as a transcription regulator; however the relevance of such function remains unclear. {ECO:0000250, ECO:0000269|PubMed:11788820, ECO:0000269|PubMed:17107665, ECO:0000269|PubMed:17623017}.; . TISSUE SPECIFICITY: Present in many tissues such as brain, thymus, lymph node, lung, liver, skin and kidney (at protein level). {ECO:0000269|PubMed:11788820}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;spinal ganglion;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;amnion;alveolus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; testis - interstitial;testis - seminiferous tubule;thyroid;testis; 0.15055 0.22097 -0.135838822 43.77211607 83.15321 1.93824 IFT74 9.26889343173298e-06 0.999295023149647 0.000695707956921699 intraflagellar transport 74 FUNCTION: Component of the intraflagellar transport (IFT) complex B: together with IFT81, forms a tubulin-binding module that specifically mediates transport of tubulin within the cilium. Binds beta-tubulin via its basic region. Required for ciliogenesis. {ECO:0000269|PubMed:23990561}.; . TISSUE SPECIFICITY: Highly expressed in adult and fetal kidney and expressed at lower level in adult heart, placenta, lung, liver and pancreas, and in fetal heart, lung and liver. Little to no expression was detected in adult brain and skeletal muscle or in fetal brain, thymus and spleen. {ECO:0000269|PubMed:11683410}.; . . 0.28662 0.08508 1.199707453 92.98183534 3982.59417 12.48355 IFT74-AS1 . . . IFT74 antisense RNA 1 . . . . . . . . . . . IFT80 1.44402047985056e-10 0.934424063949528 0.0655759359060694 intraflagellar transport 80 FUNCTION: Component of the intraflagellar transport (IFT) complex B, which is essential for the development and maintenance of motile and sensory cilia. {ECO:0000269|PubMed:17468754}.; . TISSUE SPECIFICITY: Isoform IFT80-L is widely expressed. {ECO:0000269|PubMed:18601909}.; unclassifiable (Anatomical System);lymph node;heart;ovary;tongue;islets of Langerhans;hypothalamus;parathyroid;skin;skeletal muscle;retina;uterus;whole body;lung;frontal lobe;endometrium;bone;placenta;hippocampus;pituitary gland;liver;testis;head and neck;germinal center;kidney;brain;stomach;peripheral nerve; medulla oblongata;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;parietal lobe; 0.32627 0.10188 -0.286522835 33.47487615 1595.47681 7.38778 IFT81 5.76030312431944e-07 0.998464185788439 0.00153523818124865 intraflagellar transport 81 FUNCTION: Component of the intraflagellar transport (IFT) complex B: together with IFT74, forms a tubulin-binding module that specifically mediates transport of tubulin within the cilium. Binds tubulin via its CH (calponin-homology)-like region. Required for ciliogenesis. {ECO:0000269|PubMed:23990561}.; . TISSUE SPECIFICITY: Highly expressed in testis, moderately in ovary, heart, liver, skeletal muscle, kidney and pancreas, low in prostate, brain, placenta and lung and not detected in spleen, thymus, small intestine and colon. Isoform CDV-1R is abundantly expressed in testis. {ECO:0000269|PubMed:12549821}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;islets of Langerhans;urinary;colon;skeletal muscle;skin;retina;uterus;whole body;lung;frontal lobe;endometrium;bone;placenta;liver;testis;head and neck;spleen;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22031 0.10526 -0.312207497 32.05944798 370.57932 4.06529 IFT88 1.97189619737225e-08 0.998383169937842 0.0016168103431962 intraflagellar transport 88 FUNCTION: Involved in primary cilium biogenesis. Also involved in autophagy since it is required for trafficking of ATG16L and the expansion of the autophagic compartment (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the heart, brain, liver, lung, kidney, skeletal muscle and pancreas. {ECO:0000269|PubMed:7633404}.; ovary;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;thyroid;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);heart;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;kidney; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.39620 0.10523 -0.262657925 34.93158764 1694.62273 7.59080 IFT122 2.16271033723115e-11 0.99959961686367 0.000400383114702787 intraflagellar transport 122 FUNCTION: Required for cilia formation during neuronal patterning. Acts as a negative regulator of Shh signaling. Required to recruit TULP3 to primary cilia (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in many tissues. Predominant expression in testis and pituitary. {ECO:0000269|PubMed:11242542}.; smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;thyroid;bone;iris;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pineal body;muscle;blood;lens;lung;placenta;visual apparatus;hippocampus;liver;cervix;spleen;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; 0.37127 0.14087 -1.271459448 5.207596131 277.35114 3.56725 IFT140 9.13769895125714e-18 0.807693230967578 0.192306769032422 intraflagellar transport 140 FUNCTION: Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport. Plays a pivotal role in proper development and function of ciliated cells. Involved in ciliogenesis and cilia maintenance. {ECO:0000269|PubMed:22503633}.; DISEASE: Short-rib thoracic dysplasia 9 with or without polydactyly (SRTD9) [MIM:266920]: A form of short-rib thoracic dysplasia, a group of autosomal recessive ciliopathies that are characterized by a constricted thoracic cage, short ribs, shortened tubular bones, and a 'trident' appearance of the acetabular roof. Polydactyly is variably present. Non-skeletal involvement can include cleft lip/palate as well as anomalies of major organs such as the brain, eye, heart, kidneys, liver, pancreas, intestines, and genitalia. Some forms of the disease are lethal in the neonatal period due to respiratory insufficiency secondary to a severely restricted thoracic cage, whereas others are compatible with life. Disease spectrum encompasses Ellis-van Creveld syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-Saldino syndrome, and short rib-polydactyly syndrome. SRTD9 is characterized by phalangeal cone-shaped epiphyses, chronic renal disease, nearly constant retinal dystrophy, and mild radiographic abnormality of the proximal femur. Occasional features include short stature, cerebellar ataxia, and hepatic fibrosis. {ECO:0000269|PubMed:22503633, ECO:0000269|PubMed:23418020}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;thyroid;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;duodenum;kidney;mammary gland;stomach;thymus; superior cervical ganglion;skeletal muscle; 0.29672 0.10485 -0.477995801 22.82377919 1498.31247 7.20198 IFT172 2.29011817971014e-18 0.999993369400762 6.63059923773973e-06 intraflagellar transport 172 FUNCTION: Required for the maintenance and formation of cilia. Plays an indirect role in hedgehog (Hh) signaling, cilia being required for all activity of the hedgehog pathway (By similarity). {ECO:0000250}.; DISEASE: Short-rib thoracic dysplasia 10 with or without polydactyly (SRTD10) [MIM:615630]: A form of short-rib thoracic dysplasia, a group of autosomal recessive ciliopathies that are characterized by a constricted thoracic cage, short ribs, shortened tubular bones, and a 'trident' appearance of the acetabular roof. Polydactyly is variably present. Non-skeletal involvement can include cleft lip/palate as well as anomalies of major organs such as the brain, eye, heart, kidneys, liver, pancreas, intestines, and genitalia. Some forms of the disease are lethal in the neonatal period due to respiratory insufficiency secondary to a severely restricted thoracic cage, whereas others are compatible with life. Disease spectrum encompasses Ellis-van Creveld syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-Saldino syndrome, and short rib-polydactyly syndrome. {ECO:0000269|PubMed:24140113}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa 71 (RP71) [MIM:616394]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:25168386}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;testis;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;nasopharynx;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; . 0.25302 0.16159 -1.955181094 1.857749469 367.466 4.05229 IGAD1 . . . immunoglobulin A (IgA) deficiency susceptibility 1 . . . . . . . . . . . IGBP1 0.933825157525953 0.0658611638854107 0.000313678588636704 immunoglobulin (CD79A) binding protein 1 FUNCTION: Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits. {ECO:0000269|PubMed:19818709, ECO:0000269|PubMed:23591866}.; DISEASE: Mental retardation, X-linked, syndromic, 28 (MRXS28) [MIM:300472]: A mental retardation syndrome characterized by agenesis of the corpus callosum, coloboma of the iris and optic nerve, severe retrognathia, and intellectual deficit. Mental retardation is defined by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:14556245}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in heart, skeletal muscle and pancreas.; myocardium;lymphoreticular;smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;amniotic fluid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;kidney;stomach; fetal brain;cerebellum peduncles; 0.13553 0.10700 0.260991686 70.25831564 109.93343 2.27803 IGBP1-AS1 . . . IGBP1 antisense RNA 1 . . . . . . . . . . . IGBP1-AS2 . . . IGBP1 antisense RNA 2 . . . . . . . . . . . IGBP1P1 . . . immunoglobulin (CD79A) binding protein 1 pseudogene 1 . . . . . . . . . . . IGBP1P2 . . . immunoglobulin (CD79A) binding protein 1 pseudogene 2 . . . . . . . . . . . IGBP1P3 . . . immunoglobulin (CD79A) binding protein 1 pseudogene 3 . . . . . . . . . . . IGBP1P4 . . . immunoglobulin (CD79A) binding protein 1 pseudogene 4 . . . . . . . . . . . IGBP1P5 . . . immunoglobulin (CD79A) binding protein 1 pseudogene 5 . . . . . . . . . . . IGDCC3 0.000233060205949579 0.99575353043994 0.00401340935411072 immunoglobulin superfamily, DCC subclass, member 3 . . . unclassifiable (Anatomical System);lung;ovary;visual apparatus;liver;testis;brain; trigeminal ganglion;skeletal muscle; 0.61106 0.11678 -1.456898556 3.862939372 119.80527 2.38361 IGDCC4 0.0148854979044506 0.985104501077913 1.00010176363654e-05 immunoglobulin superfamily, DCC subclass, member 4 . . . unclassifiable (Anatomical System);amygdala;heart;ovary;parathyroid;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;optic nerve;whole body;lung;placenta;thyroid;macula lutea;liver;testis;spleen;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle;parietal lobe; . 0.12313 0.85606445 88.52323661 4828.87634 14.09369 IGES . . . immunoglobulin E concentration, serum . . . . . . . . . . . IGF1 0.469523496452965 0.506022424818536 0.0244540787284994 insulin like growth factor 1 FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. May play a role in synapse maturation. {ECO:0000269|PubMed:21076856, ECO:0000269|PubMed:24132240}.; DISEASE: Insulin-like growth factor I deficiency (IGF1 deficiency) [MIM:608747]: Autosomal recessive disorder characterized by growth retardation, sensorineural deafness and mental retardation. {ECO:0000269|PubMed:8857020}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;cochlea;endometrium;bone;testis;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;internal ear;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;uterus;superior cervical ganglion;testis - interstitial;uterus corpus;adipose tissue;liver;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.66422 0.99377 0.237127192 68.98443029 98.37812 2.14393 IGF1R 0.552974259646112 0.447025700181167 4.01727210206272e-08 insulin like growth factor 1 receptor FUNCTION: Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphorylation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K- driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R.; DISEASE: Insulin-like growth factor 1 resistance (IGF1RES) [MIM:270450]: A disorder characterized by intrauterine growth retardation, poor postnatal growth and increased plasma IGF1 levels. {ECO:0000269|PubMed:14657428, ECO:0000269|PubMed:15928254}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found as a hybrid receptor with INSR in muscle, heart, kidney, adipose tissue, skeletal muscle, hepatoma, fibroblasts, spleen and placenta (at protein level). Expressed in a variety of tissues. Overexpressed in tumors, including melanomas, cancers of the colon, pancreas prostate and kidney. {ECO:0000269|PubMed:12019176, ECO:0000269|PubMed:8247543, ECO:0000269|PubMed:9202395, ECO:0000269|PubMed:9355755}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;lens;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;adrenal gland;placenta;macula lutea;liver;head and neck;kidney;mammary gland; superior cervical ganglion;prostate;prefrontal cortex; 0.99531 0.86203 -1.71613166 2.494692144 156.15124 2.73123 IGF2 0.0253027183278788 0.782705005553932 0.19199227611819 insulin like growth factor 2 FUNCTION: The insulin-like growth factors possess growth-promoting activity. In vitro, they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play a role in fetal development.; DISEASE: Silver-Russell syndrome (SRS) [MIM:180860]: A clinically heterogeneous condition characterized by severe intrauterine growth retardation, poor postnatal growth, craniofacial features such as a triangular shaped face and a broad forehead, body asymmetry, and a variety of minor malformations. The phenotypic expression changes during childhood and adolescence, with the facial features and asymmetry usually becoming more subtle with age. {ECO:0000269|PubMed:19066168}. Note=The gene represented in this entry is involved in disease pathogenesis. Most of the cases of Silver-Russell syndrome are caused by the epigenetic changes of DNA hypomethylation at the telomeric imprinting control region (ICR1) on chromosome 11p15, involving the H19 and IGF2 genes.; DISEASE: Growth restriction, severe, with distinctive facies (GRDF) [MIM:616489]: A disease characterized by severe prenatal and postnatal growth restriction, facial dysmorphism, and short stature in the presence of normal or slightly elevated growth hormone levels. {ECO:0000269|PubMed:26154720}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;colon;fovea centralis;choroid;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;muscle;lens;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;aorta;peripheral nerve; . 0.96370 . -0.271755481 34.31823543 228.9007 3.26829 IGF2-AS . . . IGF2 antisense RNA . . . . . 0.09348 . . . . . IGF2BP1 0.998573996721702 0.00142600224932412 1.02897362875678e-09 insulin like growth factor 2 mRNA binding protein 1 FUNCTION: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to and stabilizes ABCB1/MDR-1 mRNA (By similarity). During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing (By similarity). Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence prevents MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD. Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to the oncofetal H19 transcript and to the neuron-specific TAU mRNA and regulates their localizations. Binds to and stabilizes BTRC/FBW1A mRNA. Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2. Promotes the directed movement of tumor-derived cells by fine-tuning intracellular signaling networks. Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN transcript open reading frame (ORF) and prevents mRNA decay. This combined action on MAPK4 (down-regulation) and PTEN (up-regulation) antagonizes HSPB1 phosphorylation, consequently it prevents G-actin sequestration by phosphorylated HSPB1, allowing F-actin polymerization. Hence enhances the velocity of cell migration and stimulates directed cell migration by PTEN-modulated polarization. Interacts with Hepatitis C virus (HCV) 5'-UTR and 3'-UTR and specifically enhances translation at the HCV IRES, but not 5'-cap- dependent translation, possibly by recruiting eIF3. Interacts with HIV-1 GAG protein and blocks the formation of infectious HIV-1 particles. Reduces HIV-1 assembly by inhibiting viral RNA packaging, as well as assembly and processing of GAG protein on cellular membranes. During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts. {ECO:0000250, ECO:0000269|PubMed:10875929, ECO:0000269|PubMed:16356927, ECO:0000269|PubMed:16541107, ECO:0000269|PubMed:16778892, ECO:0000269|PubMed:17101699, ECO:0000269|PubMed:17255263, ECO:0000269|PubMed:17893325, ECO:0000269|PubMed:18385235, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19541769, ECO:0000269|PubMed:19647520, ECO:0000269|PubMed:20080952, ECO:0000269|PubMed:22279049, ECO:0000269|PubMed:8132663, ECO:0000269|PubMed:9891060}.; . TISSUE SPECIFICITY: Mainly expressed in the embryo, including in fetal liver, fetal lung, fetal kidney, fetal thymus (at protein level). Also expressed follicles of ovary, as well as in gonocytes of testis, spermatogonia, semen, oocytes and placenta (at protein level). Expressed in various cancers, including testis and lung cancers (at protein level), as well as kidney, prostate and trachea cancers. {ECO:0000269|PubMed:12921532, ECO:0000269|PubMed:16049158, ECO:0000269|PubMed:17255263, ECO:0000269|PubMed:9891060}.; unclassifiable (Anatomical System);pancreas;lung;placenta;liver;testis;kidney;germinal center;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.92265 0.48799 -0.381986487 27.68931352 33.32025 1.02987 IGF2BP2 0.942124149210594 0.0578754718254093 3.78963996263379e-07 insulin like growth factor 2 mRNA binding protein 2 FUNCTION: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation (By similarity). Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. Binding is isoform-specific. Binds to beta- actin/ACTB and MYC transcripts. {ECO:0000250, ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:9891060}.; . TISSUE SPECIFICITY: Expressed in oocytes, granulosa cells of small and growing follicles, Leydig cells, spermatogonia and semen (at protein level). Expressed in testicular cancer (at protein level). Expressed weakly in heart, placenta, skeletal muscle, bone marrow, colon, kidney, salivary glands, testis and pancreas. Detected in fetal liver, fetal ovary, gonocytes and interstitial cells of the testis. {ECO:0000269|PubMed:10190901, ECO:0000269|PubMed:16049158}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; placenta;trigeminal ganglion;parietal lobe; 0.80885 0.21615 -0.758599262 13.32861524 26.44571 0.85633 IGF2BP2-AS1 . . . IGF2BP2 antisense RNA 1 . . . . . 0.34166 . . . . . IGF2BP3 0.999726189174336 0.000273810375037966 4.5062605190233e-10 insulin like growth factor 2 mRNA binding protein 3 FUNCTION: RNA-binding factor that may recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to beta- actin/ACTB and MYC transcripts. Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. {ECO:0000269|PubMed:16541107, ECO:0000269|PubMed:23640942}.; . TISSUE SPECIFICITY: Expressed in fetal liver, fetal lung, fetal kidney, fetal thymus, fetal placenta, fetal follicles of ovary and gonocytes of testis, growing oocytes, spermatogonia and semen (at protein level). Expressed in cervix adenocarcinoma, in testicular, pancreatic and renal-cell carcinomas (at protein level). Expressed ubiquitously during fetal development at 8 and 14 weeks of gestation. Expressed in ovary, testis, brain, placenta, pancreatic cancer tissues and pancreatic cancer cell lines. {ECO:0000269|PubMed:10525192, ECO:0000269|PubMed:12161597, ECO:0000269|PubMed:15644775, ECO:0000269|PubMed:16049158, ECO:0000269|PubMed:16814207, ECO:0000269|PubMed:17192788, ECO:0000269|PubMed:9178771, ECO:0000269|PubMed:9891060}.; lymphoreticular;ovary;salivary gland;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;visual apparatus;amnion;liver;cervix;spleen;head and neck;kidney;aorta; superior cervical ganglion;placenta;tumor;atrioventricular node;trigeminal ganglion; 0.81169 0.11096 -0.468351206 23.42533616 23.06422 0.76931 IGF2R 0.999999196216303 8.03783697431275e-07 3.51790096912114e-23 insulin like growth factor 2 receptor FUNCTION: Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6- phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. This receptor also binds IGF2. Acts as a positive regulator of T-cell coactivation, by binding DPP4. {ECO:0000269|PubMed:10900005}.; . . myocardium;lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;urinary;spinal cord;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;adrenal gland;placenta;duodenum;hypopharynx;head and neck;kidney;stomach; whole blood;skeletal muscle; 0.14522 0.70508 -1.928748556 1.904930408 3396.75143 11.16393 IGFALS 2.79990921598618e-05 0.326821262433018 0.673150738474822 insulin like growth factor binding protein acid labile subunit FUNCTION: Involved in protein-protein interactions that result in protein complexes, receptor-ligand binding or cell adhesion.; . TISSUE SPECIFICITY: Plasma.; uterus;iris;liver; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12949 0.44208 -0.883608246 10.50365652 490.6224 4.55888 IGFBP1 0.00178327971594811 0.714456012613973 0.283760707670079 insulin like growth factor binding protein 1 FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Promotes cell migration. {ECO:0000269|PubMed:15972819}.; . . unclassifiable (Anatomical System);uterus;whole body;ovary;placenta;liver;parathyroid;skin; fetal liver;placenta;liver; 0.60048 0.74702 . . 90.72922 2.04965 IGFBP2 0.84435378457342 0.152829303851052 0.00281691157552764 insulin like growth factor binding protein 2 FUNCTION: Inhibits IGF-mediated growth and developmental rates. IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. {ECO:0000269|PubMed:19081843}.; . . myocardium;ovary;colon;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;muscle;adrenal cortex;skeletal muscle;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; prostate;liver; 0.87518 0.43416 . . 17.14107 0.60212 IGFBP3 0.362251902433295 0.58683504376315 0.0509130538035548 insulin like growth factor binding protein 3 FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R. {ECO:0000269|PubMed:20353938}.; . TISSUE SPECIFICITY: Expressed by most tissues. Present in plasma.; myocardium;smooth muscle;ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;cochlea;oesophagus;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;peripheral nerve;cerebellum; uterus corpus;placenta; 0.28872 0.82225 . . 2102.84042 8.44477 IGFBP4 0.236669010399168 0.730924420144852 0.0324065694559798 insulin like growth factor binding protein 4 FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;choroid;vein;skin;retina;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; uterus corpus;adipose tissue;smooth muscle;ovary;liver;atrioventricular node;kidney; 0.57469 0.35026 . . 10.68915 0.38787 IGFBP5 0.859978350463281 0.137886184530129 0.0021354650065906 insulin like growth factor binding protein 5 FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.; . TISSUE SPECIFICITY: Osteosarcoma, and at lower levels in liver, kidney and brain.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; uterus;uterus corpus;superior cervical ganglion;adipose tissue;ovary;adrenal gland;placenta;adrenal cortex;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;fetal thyroid;skeletal muscle; 0.65909 0.31908 . . 128.68174 2.47216 IGFBP6 0.0923313370768109 0.869050824525182 0.0386178383980072 insulin like growth factor binding protein 6 FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.; . . medulla oblongata;ovary;salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;thyroid;bone;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;breast;pancreas;lung;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;hypopharynx;amnion;head and neck;kidney;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;olfactory bulb;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.33818 . . . 109.39728 2.27241 IGFBP7 0.00596320863879663 0.731544377581106 0.262492413780098 insulin like growth factor binding protein 7 FUNCTION: Binds IGF-I and IGF-II with a relatively low affinity. Stimulates prostacyclin (PGI2) production. Stimulates cell adhesion. {ECO:0000269|PubMed:8117260, ECO:0000269|PubMed:8939990}.; DISEASE: Retinal arterial macroaneurysm with supravalvular pulmonic stenosis (RAMSVPS) [MIM:614224]: An autosomal recessive condition characterized by the bilateral appearance of 'beading' along the major retinal arterial trunks, with the subsequent formation of macroaneurysms. Affected individuals also have supravalvular pulmonic stenosis, often requiring surgical correction. {ECO:0000269|PubMed:21835307}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;dura mater;germinal center;brain;tonsil;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;urinary;lens;pancreas;pia mater;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus; heart; 0.50687 0.11283 . . 339.65766 3.90848 IGFBP7-AS1 . . . IGFBP7 antisense RNA 1 . . . . . . . . . . . IGFBPL1 0.0085039334958594 0.797128255788127 0.194367810716014 insulin like growth factor binding protein-like 1 FUNCTION: IGF-binding proteins prolong the half-life of IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs in cell culture. They alter the interaction of IGFs with their cell surface receptors (By similarity). May be a putative tumor suppressor protein. {ECO:0000250, ECO:0000269|PubMed:15845387}.; . TISSUE SPECIFICITY: Expressed at the highest level in both brain and testis, with lower levels in the prostate, bladder and lung. {ECO:0000269|PubMed:15845387}.; . . 0.18270 . . . 211.50895 3.13555 IGFL1 5.92602172870775e-06 0.14439408380836 0.855599990169911 IGF like family member 1 FUNCTION: Probable ligand of the IGFLR1 cell membrane receptor. {ECO:0000269|PubMed:21454693}.; . TISSUE SPECIFICITY: Detected in ovary and spinal cord. {ECO:0000269|PubMed:16890402}.; . . . 0.09357 0.681699246 84.93158764 196.91241 3.03435 IGFL1P1 . . . IGF like family member 1 pseudogene 1 . . . . . . . . . . . IGFL1P2 . . . IGF like family member 1 pseudogene 2 . . . . . . . . . . . IGFL2 0.000244160956618864 0.317265960772951 0.68248987827043 IGF like family member 2 FUNCTION: Potential ligand of the IGFLR1 cell membrane receptor. {ECO:0000269|PubMed:21454693}.; . TISSUE SPECIFICITY: Detected in cerebellum, heart, placenta, spleen, stomach, testis and thymus. {ECO:0000269|PubMed:16890402}.; . . 0.18922 . -0.229483771 36.86010852 5.49399 0.20483 IGFL3 0.00109378557531111 0.609752185423115 0.389154029001574 IGF like family member 3 FUNCTION: Potential ligand of the IGFLR1 cell membrane receptor. {ECO:0000269|PubMed:21454693}.; . TISSUE SPECIFICITY: Detected in the cerebellum. {ECO:0000269|PubMed:16890402}.; heart;bone;skin; . 0.08101 . 0.369407109 74.95281906 27.96458 0.89709 IGFL4 0.00312950335672231 0.595518555228494 0.401351941414783 IGF like family member 4 . . TISSUE SPECIFICITY: Detected in the cerebellum. {ECO:0000269|PubMed:16890402}.; . . 0.11137 . 0.347360312 73.97381458 224.2709 3.23823 IGFLR1 0.00016488397901589 0.68252883069201 0.317306285328974 IGF like family receptor 1 FUNCTION: Probable cell membrane receptor for the IGF-like family proteins. Binds IGFL1 and IGFL3 with a higher affinity. May also bind IGFL2. {ECO:0000269|PubMed:21454693}.; . . unclassifiable (Anatomical System);ovary;heart;colon;blood;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;lung;bone;placenta;macula lutea;liver;testis;spleen;germinal center;kidney;brain;aorta;thymus; superior cervical ganglion;liver;white blood cells; 0.08836 0.09110 0.442818085 77.8544468 212.66787 3.14745 IGFN1 2.50313046386532e-18 0.00748578791750363 0.992514212082496 immunoglobulin-like and fibronectin type III domain containing 1 . . TISSUE SPECIFICITY: Expressed in skeletal muscle. {ECO:0000269|PubMed:15385448}.; unclassifiable (Anatomical System);fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;whole body;larynx;thyroid;macula lutea;alveolus;liver;head and neck;spleen;kidney; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12425 0.10243 6.487063031 99.87615004 12297.47943 23.82839 IGH . . . immunoglobulin heavy locus . . . . . . . . . . . IGHA1 . . . immunoglobulin heavy constant alpha 1 FUNCTION: Ig alpha is the major immunoglobulin class in body secretions. It may serve both to defend against local infection and to prevent access of foreign antigens to the general immunologic system.; DISEASE: Note=A chromosomal aberration involving IGHA1 is found in multiple myeloma (MM) cell lines. Translocation t(1;14)(q21;q32) that forms a FCRL4-IGHA1 fusion protein. {ECO:0000269|PubMed:11290337}.; . . . . . . . . . IGHA2 . . . immunoglobulin heavy constant alpha 2 (A2m marker) FUNCTION: Ig alpha is the major immunoglobulin class in body secretions. It may serve both to defend against local infection and to prevent access of foreign antigens to the general immunologic system.; . . . . . . . . . . IGHD . . . immunoglobulin heavy constant delta FUNCTION: IgD is the major antigen receptor isotype on the surface of most peripheral B-cells, where it is coexpressed with IgM. The membrane-bound IgD (mIgD) induces the phosphorylation of CD79A and CD79B by the Src family of protein tyrosine kinases. Soluble IgD (sIgD) concentration in serum below those of IgG, IgA, and IgM but much higher than that of IgE. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites. After the antigen binds to the B-cell receptor, the secreted form sIgD is shut off. IgD is a potent inducer of TNF, IL1B, and IL1RN. IgD also induces release of IL6, IL10, and LIF from peripheral blood mononuclear cells. Monocytes seem to be the main producers of cytokines in vitro in the presence of IgD. {ECO:0000269|PubMed:8774350}.; . . . . . . . . . . IGHD1-1 . . . immunoglobulin heavy diversity 1-1 . . . . . . . . . . . IGHD1-7 . . . immunoglobulin heavy diversity 1-7 . . . . . . . . . . . IGHD1-14 . . . immunoglobulin heavy diversity 1-14 (non-functional) . . . . . . . . . . . IGHD1-20 . . . immunoglobulin heavy diversity 1-20 . . . . . . . . . . . IGHD1-26 . . . immunoglobulin heavy diversity 1-26 . . . . . . . . . . . IGHD1OR15-1A . . . immunoglobulin heavy diversity 1/OR15-1A (non-functional) . . . . . . . . . . . IGHD1OR15-1B . . . immunoglobulin heavy diversity 1/OR15-1B (non-functional) . . . . . . . . . . . IGHD2-2 . . . immunoglobulin heavy diversity 2-2 . . . . . . . . . . . IGHD2-8 . . . immunoglobulin heavy diversity 2-8 . . . . . . . . . . . IGHD2-15 . . . immunoglobulin heavy diversity 2-15 . . . . . . . . . . . IGHD2-21 . . . immunoglobulin heavy diversity 2-21 . . . . . . . . . . . IGHD2OR15-2A . . . immunoglobulin heavy diversity 2/OR15-2A (non-functional) . . . . . . . . . . . IGHD2OR15-2B . . . immunoglobulin heavy diversity 2/OR15-2B (non-functional) . . . . . . . . . . . IGHD3-3 . . . immunoglobulin heavy diversity 3-3 . . . . . . . . . . . IGHD3-9 . . . immunoglobulin heavy diversity 3-9 . . . . . . . . . . . IGHD3-10 . . . immunoglobulin heavy diversity 3-10 . . . . . . . . . . . IGHD3-16 . . . immunoglobulin heavy diversity 3-16 . . . . . . . . . . . IGHD3-22 . . . immunoglobulin heavy diversity 3-22 . . . . . . . . . . . IGHD3OR15-3A . . . immunoglobulin heavy diversity 3/OR15-3A (non-functional) . . . . . . . . . . . IGHD3OR15-3B . . . immunoglobulin heavy diversity 3/OR15-3B (non-functional) . . . . . . . . . . . IGHD4-4 . . . immunoglobulin heavy diversity 4-4 . . . . . . . . . . . IGHD4-11 . . . immunoglobulin heavy diversity 4-11 (non-functional) . . . . . . . . . . . IGHD4-17 . . . immunoglobulin heavy diversity 4-17 . . . . . . . . . . . IGHD4-23 . . . immunoglobulin heavy diversity 4-23 (non-functional) . . . . . . . . . . . IGHD4OR15-4A . . . immunoglobulin heavy diversity 4/OR15-4A (non-functional) . . . . . . . . . . . IGHD4OR15-4B . . . immunoglobulin heavy diversity 4/OR15-4B (non-functional) . . . . . . . . . . . IGHD5-5 . . . immunoglobulin heavy diversity 5-5 . . . . . . . . . . . IGHD5-12 . . . immunoglobulin heavy diversity 5-12 . . . . . . . . . . . IGHD5-18 . . . immunoglobulin heavy diversity 5-18 . . . . . . . . . . . IGHD5-24 . . . immunoglobulin heavy diversity 5-24 (non-functional) . . . . . . . . . . . IGHD5OR15-5A . . . immunoglobulin heavy diversity 5/OR15-5A (non-functional) . . . . . . . . . . . IGHD5OR15-5B . . . immunoglobulin heavy diversity 5/OR15-5B (non-functional) . . . . . . . . . . . IGHD6-6 . . . immunoglobulin heavy diversity 6-6 . . . . . . . . . . . IGHD6-13 . . . immunoglobulin heavy diversity 6-13 . . . . . . . . . . . IGHD6-19 . . . immunoglobulin heavy diversity 6-19 . . . . . . . . . . . IGHD6-25 . . . immunoglobulin heavy diversity 6-25 . . . . . . . . . . . IGHD7-27 . . . immunoglobulin heavy diversity 7-27 . . . . . . . . . . . IGHE . . . immunoglobulin heavy constant epsilon . . . . . . . . . . . IGHEP1 . . . immunoglobulin heavy constant epsilon P1 (pseudogene) . . . . . . . . . . . IGHEP2 . . . immunoglobulin heavy constant epsilon P2 (pseudogene) . . . . . . . . . . . IGHG1 . . . immunoglobulin heavy constant gamma 1 (G1m marker) . DISEASE: Multiple myeloma (MM) [MIM:254500]: A malignant tumor of plasma cells usually arising in the bone marrow and characterized by diffuse involvement of the skeletal system, hyperglobulinemia, Bence-Jones proteinuria and anemia. Complications of multiple myeloma are bone pain, hypercalcemia, renal failure and spinal cord compression. The aberrant antibodies that are produced lead to impaired humoral immunity and patients have a high prevalence of infection. Amyloidosis may develop in some patients. Multiple myeloma is part of a spectrum of diseases ranging from monoclonal gammopathy of unknown significance (MGUS) to plasma cell leukemia. {ECO:0000269|PubMed:11972529, ECO:0000269|PubMed:8943038}. Note=The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving IGHG1 is found in multiple myeloma. Translocation t(11;14)(q13;q32) with the IgH locus. Translocation t(11;14)(q13;q32) with CCND1; translocation t(4;14)(p16.3;q32.3) with FGFR3; translocation t(6;14)(p25;q32) with IRF4.; . . . . . . . . . IGHG2 . . . immunoglobulin heavy constant gamma 2 (G2m marker) . . . . . . . . . . . IGHG3 . . . immunoglobulin heavy constant gamma 3 (G3m marker) . . . . . . . . . . . IGHG4 . . . immunoglobulin heavy constant gamma 4 (G4m marker) . . . . . . . . . . . IGHGP . . . immunoglobulin heavy constant gamma P (non-functional) . . . . . . . . . . . IGHJ1 . . . immunoglobulin heavy joining 1 . . . . . . . . . . . IGHJ1P . . . immunoglobulin heavy joining 1P (pseudogene) . . . . . . . . . . . IGHJ2 . . . immunoglobulin heavy joining 2 . . . . . . . . . . . IGHJ2P . . . immunoglobulin heavy joining 2P (pseudogene) . . . . . . . . . . . IGHJ3 . . . immunoglobulin heavy joining 3 . . . . . . . . . . . IGHJ3P . . . immunoglobulin heavy joining 3P (pseudogene) . . . . . . . . . . . IGHJ4 . . . immunoglobulin heavy joining 4 . . . . . . . . . . . IGHJ5 . . . immunoglobulin heavy joining 5 . . . . . . . . . . . IGHJ6 . . . immunoglobulin heavy joining 6 . . . . . . . . . . . IGHM . . . immunoglobulin heavy constant mu FUNCTION: IgM antibodies play an important role in primary defense mechanisms. They have been shown to be involved in early recognition of external invaders like bacteria and viruses, cellular waste and modified self, as well as in recognition and elimination of precancerous and cancerous lesions. The membrane- bound form is found in the majority of normal B-cells alongside with IgD. Membrane-bound IgM induces the phosphorylation of CD79A and CD79B by the Src family of protein tyrosine kinases. It may cause death of cells by apoptosis. It is also found in soluble form, which represents about 30% of the total serum immunoglobulins where it is found almost exclusively as a homopentamer. After the antigen binds to the B-cell receptor, the secreted form is secreted in large amounts. {ECO:0000269|PubMed:3137579}.; DISEASE: Agammaglobulinemia 1, autosomal recessive (AGM1) [MIM:601495]: A primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life. {ECO:0000269|PubMed:8890099}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . . . . . . IGHMBP2 1.5094399423583e-08 0.988551377830809 0.011448607074791 immunoglobulin mu binding protein 2 FUNCTION: 5' to 3' helicase that unwinds RNA and DNA duplices in an ATP-dependent reaction. Acts as a transcription regulator. Required for the transcriptional activation of the flounder liver- type antifreeze protein gene. Exhibits strong binding specificity to the enhancer element B of the flounder antifreeze protein gene intron. Binds to the insulin II gene RIPE3B enhancer region. May be involved in translation (By similarity). DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence related to the immunoglobulin mu chain switch region. Preferentially binds to the 5'-GGGCT-3' motif. Interacts with tRNA-Tyr. Stimulates the transcription of the human neurotropic virus JCV. {ECO:0000250, ECO:0000269|PubMed:19158098, ECO:0000269|PubMed:19299493}.; DISEASE: Charcot-Marie-Tooth disease 2S (CMT2S) [MIM:616155]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. {ECO:0000269|PubMed:25439726}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues examined. Expressed in the developing and adult human brain, with highest expression in the cerebellum. Moderately expressed in fibroblasts. {ECO:0000269|PubMed:25439726}.; lymphoreticular;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;urinary;muscle;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10164 0.19917 0.859723513 88.57041755 2057.92719 8.36023 IGHV1-2 . . . immunoglobulin heavy variable 1-2 . . . . . . . . . . . IGHV1-3 . . . immunoglobulin heavy variable 1-3 . . . . . . . . . . . IGHV1-8 . . . immunoglobulin heavy variable 1-8 . . . . . . . . . . . IGHV1-12 . . . immunoglobulin heavy variable 1-12 (pseudogene) . . . . . . . . . . . IGHV1-14 . . . immunoglobulin heavy variable 1-14 (pseudogene) . . . . . . . . . . . IGHV1-17 . . . immunoglobulin heavy variable 1-17 (pseudogene) . . . . . . . . . . . IGHV1-18 . . . immunoglobulin heavy variable 1-18 . . . . . . . . . . . IGHV1-24 . . . immunoglobulin heavy variable 1-24 . . . . . . . . . . . IGHV1-38-4 . . . immunoglobulin heavy variable 1-38-4 (non-functional) . . . . . . . . . . . IGHV1-45 . . . immunoglobulin heavy variable 1-45 . . . . . . . . . . . IGHV1-46 . . . immunoglobulin heavy variable 1-46 . . . . . . . . . . . IGHV1-58 . . . immunoglobulin heavy variable 1-58 . . . . . . . . . . . IGHV1-67 . . . immunoglobulin heavy variable 1-67 (pseudogene) . . . . . . . . . . . IGHV1-68 . . . immunoglobulin heavy variable 1-68 (pseudogene) . . . . . . . . . . . IGHV1-69 . . . immunoglobulin heavy variable 1-69 . . . . . . . . . . . IGHV1-69-2 . . . immunoglobulin heavy variable 1-69-2 . . . . . . . . . . . IGHV1-69D . . . immunoglobulin heavy variable 1-69D . . . . . . . . . . . IGHV1OR15-1 . . . immunoglobulin heavy variable 1/OR15-1 (non-functional) . . . . . . . . . . . IGHV1OR15-2 . . . immunoglobulin heavy variable 1/OR15-2 (pseudogene) . . . . . . . . . . . IGHV1OR15-3 . . . immunoglobulin heavy variable 1/OR15-3 (pseudogene) . . . . . . . . . . . IGHV1OR15-4 . . . immunoglobulin heavy variable 1/OR15-4 (pseudogene) . . . . . . . . . . . IGHV1OR15-5 . . . immunoglobulin heavy variable 1/OR15-5 (non-functional) . . . . . . . . . . . IGHV1OR15-6 . . . immunoglobulin heavy variable 1/OR15-6 (pseudogene) . . . . . . . . . . . IGHV1OR15-9 . . . immunoglobulin heavy variable 1/OR15-9 (non-functional) . . . . . . . . . . . IGHV1OR16-1 . . . immunoglobulin heavy variable 1/OR16-1 (pseudogene) . . . . . . . . . . . IGHV1OR16-2 . . . immunoglobulin heavy variable 1/OR16-2 (pseudogene) . . . . . . . . . . . IGHV1OR16-3 . . . immunoglobulin heavy variable 1/OR16-3 (pseudogene) . . . . . . . . . . . IGHV1OR16-4 . . . immunoglobulin heavy variable 1/OR16-4 (pseudogene) . . . . . . . . . . . IGHV1OR21-1 . . . immunoglobulin heavy variable 1/OR21-1 (non-functional) . . . . . . . . . . . IGHV2-5 . . . immunoglobulin heavy variable 2-5 . . . . . . . . . . . IGHV2-10 . . . immunoglobulin heavy variable 2-10 (pseudogene) . . . . . . . . . . . IGHV2-26 . . . immunoglobulin heavy variable 2-26 . . . . . . . . . . . IGHV2-70 . . . immunoglobulin heavy variable 2-70 . . . . . . . . . . . IGHV2-70D . . . immunoglobulin heavy variable 2-70D . . . . . . . . . . . IGHV2OR16-5 . . . immunoglobulin heavy variable 2/OR16-5 (non-functional) . . . . . . . . . . . IGHV3-6 . . . immunoglobulin heavy variable 3-6 (pseudogene) . . . . . . . . . . . IGHV3-7 . . . immunoglobulin heavy variable 3-7 . . . . . . . . . . . IGHV3-9 . . . immunoglobulin heavy variable 3-9 . . . . . . . . . . . IGHV3-11 . . . immunoglobulin heavy variable 3-11 (gene/pseudogene) . . . . . . . . . . . IGHV3-13 . . . immunoglobulin heavy variable 3-13 . . . . . . . . . . . IGHV3-15 . . . immunoglobulin heavy variable 3-15 . . . . . . . . . . . IGHV3-16 . . . immunoglobulin heavy variable 3-16 (non-functional) . . . . . . . . . . . IGHV3-19 . . . immunoglobulin heavy variable 3-19 (pseudogene) . . . . . . . . . . . IGHV3-20 . . . immunoglobulin heavy variable 3-20 . . . . . . . . . . . IGHV3-21 . . . immunoglobulin heavy variable 3-21 . . . . . . . . . . . IGHV3-22 . . . immunoglobulin heavy variable 3-22 (pseudogene) . . . . . . . . . . . IGHV3-23 . . . immunoglobulin heavy variable 3-23 . . . . . . . . . . . IGHV3-25 . . . immunoglobulin heavy variable 3-25 (pseudogene) . . . . . . . . . . . IGHV3-29 . . . immunoglobulin heavy variable 3-29 (pseudogene) . . . . . . . . . . . IGHV3-30 . . . immunoglobulin heavy variable 3-30 . . . . . . . . . . . IGHV3-30-2 . . . immunoglobulin heavy variable 3-30-2 (pseudogene) . . . . . . . . . . . IGHV3-30-3 . . . immunoglobulin heavy variable 3-30-3 . . . . . . . . . . . IGHV3-30-5 . . . immunoglobulin heavy variable 3-30-5 . . . . . . . . . . . IGHV3-32 . . . immunoglobulin heavy variable 3-32 (pseudogene) . . . . . . . . . . . IGHV3-33 . . . immunoglobulin heavy variable 3-33 . . . . . . . . . . . IGHV3-33-2 . . . immunoglobulin heavy variable 3-33-2 (pseudogene) . . . . . . . . . . . IGHV3-35 . . . immunoglobulin heavy variable 3-35 (non-functional) . . . . . . . . . . . IGHV3-36 . . . immunoglobulin heavy variable 3-36 (pseudogene) . . . . . . . . . . . IGHV3-37 . . . immunoglobulin heavy variable 3-37 (pseudogene) . . . . . . . . . . . IGHV3-38 . . . immunoglobulin heavy variable 3-38 (non-functional) . . . . . . . . . . . IGHV3-38-3 . . . immunoglobulin heavy variable 3-38-3 (non-functional) . . . . . . . . . . . IGHV3-41 . . . immunoglobulin heavy variable 3-41 (pseudogene) . . . . . . . . . . . IGHV3-42 . . . immunoglobulin heavy variable 3-42 (pseudogene) . . . . . . . . . . . IGHV3-43 . . . immunoglobulin heavy variable 3-43 . . . . . . . . . . . IGHV3-43D . . . immunoglobulin heavy variable 3-43D . . . . . . . . . . . IGHV3-47 . . . immunoglobulin heavy variable 3-47 (pseudogene) . . . . . . . . . . . IGHV3-48 . . . immunoglobulin heavy variable 3-48 . . . . . . . . . . . IGHV3-49 . . . immunoglobulin heavy variable 3-49 . . . . . . . . . . . IGHV3-50 . . . immunoglobulin heavy variable 3-50 (pseudogene) . . . . . . . . . . . IGHV3-52 . . . immunoglobulin heavy variable 3-52 (pseudogene) . . . . . . . . . . . IGHV3-53 . . . immunoglobulin heavy variable 3-53 . . . . . . . . . . . IGHV3-54 . . . immunoglobulin heavy variable 3-54 (pseudogene) . . . . . . . . . . . IGHV3-57 . . . immunoglobulin heavy variable 3-57 (pseudogene) . . . . . . . . . . . IGHV3-60 . . . immunoglobulin heavy variable 3-60 (pseudogene) . . . . . . . . . . . IGHV3-62 . . . immunoglobulin heavy variable 3-62 (pseudogene) . . . . . . . . . . . IGHV3-63 . . . immunoglobulin heavy variable 3-63 (pseudogene) . . . . . . . . . . . IGHV3-64 . . . immunoglobulin heavy variable 3-64 . . . . . . . . . . . IGHV3-64D . . . immunoglobulin heavy variable 3-64D . . . . . . . . . . . IGHV3-65 . . . immunoglobulin heavy variable 3-65 (pseudogene) . . . . . . . . . . . IGHV3-66 . . . immunoglobulin heavy variable 3-66 . . . . . . . . . . . IGHV3-69-1 . . . immunoglobulin heavy variable 3-69-1 (pseudogene) . . . . . . . . . . . IGHV3-71 . . . immunoglobulin heavy variable 3-71 (pseudogene) . . . . . . . . . . . IGHV3-72 . . . immunoglobulin heavy variable 3-72 . . . . . . . . . . . IGHV3-73 . . . immunoglobulin heavy variable 3-73 . . . . . . . . . . . IGHV3-74 . . . immunoglobulin heavy variable 3-74 . . . . . . . . . . . IGHV3-75 . . . immunoglobulin heavy variable 3-75 (pseudogene) . . . . . . . . . . . IGHV3-76 . . . immunoglobulin heavy variable 3-76 (pseudogene) . . . . . . . . . . . IGHV3-79 . . . immunoglobulin heavy variable 3-79 (pseudogene) . . . . . . . . . . . IGHV3OR15-7 . . . immunoglobulin heavy variable 3/OR15-7 (pseudogene) . . . . . . . . . . . IGHV3OR16-6 . . . immunoglobulin heavy variable 3/OR16-6 (pseudogene) . . . . . . . . . . . IGHV3OR16-7 . . . immunoglobulin heavy variable 3/OR16-7 (pseudogene) . . . . . . . . . . . IGHV3OR16-8 . . . immunoglobulin heavy variable 3/OR16-8 (non-functional) . . . . . . . . . . . IGHV3OR16-9 . . . immunoglobulin heavy variable 3/OR16-9 (non-functional) . . . . . . . . . . . IGHV3OR16-10 . . . immunoglobulin heavy variable 3/OR16-10 (non-functional) . . . . . . . . . . . IGHV3OR16-11 . . . immunoglobulin heavy variable 3/OR16-11 (pseudogene) . . . . . . . . . . . IGHV3OR16-12 . . . immunoglobulin heavy variable 3/OR16-12 (non-functional) . . . . . . . . . . . IGHV3OR16-13 . . . immunoglobulin heavy variable 3/OR16-13 (non-functional) . . . . . . . . . . . IGHV3OR16-14 . . . immunoglobulin heavy variable 3/OR16-14 (pseudogene) . . . . . . . . . . . IGHV3OR16-15 . . . immunoglobulin heavy variable 3/OR16-15 (pseudogene) . . . . . . . . . . . IGHV3OR16-16 . . . immunoglobulin heavy variable 3/OR16-16 (pseudogene) . . . . . . . . . . . IGHV4-4 . . . immunoglobulin heavy variable 4-4 . . . . . . . . . . . IGHV4-28 . . . immunoglobulin heavy variable 4-28 . . . . . . . . . . . IGHV4-30-1 . . . immunoglobulin heavy variable 4-30-1 . . . . . . . . . . . IGHV4-30-2 . . . immunoglobulin heavy variable 4-30-2 . . . . . . . . . . . IGHV4-30-4 . . . immunoglobulin heavy variable 4-30-4 . . . . . . . . . . . IGHV4-31 . . . immunoglobulin heavy variable 4-31 . . . . . . . . . . . IGHV4-34 . . . immunoglobulin heavy variable 4-34 . . . . . . . . . . . IGHV4-38-2 . . . immunoglobulin heavy variable 4-38-2 . . . . . . . . . . . IGHV4-39 . . . immunoglobulin heavy variable 4-39 . . . . . . . . . . . IGHV4-55 . . . immunoglobulin heavy variable 4-55 (pseudogene) . . . . . . . . . . . IGHV4-59 . . . immunoglobulin heavy variable 4-59 . . . . . . . . . . . IGHV4-61 . . . immunoglobulin heavy variable 4-61 . . . . . . . . . . . IGHV4-80 . . . immunoglobulin heavy variable 4-80 (pseudogene) . . . . . . . . . . . IGHV4OR15-8 . . . immunoglobulin heavy variable 4/OR15-8 (non-functional) . . . . . . . . . . . IGHV5-10-1 . . . immunoglobulin heavy variable 5-10-1 . . . . . . . . . . . IGHV5-51 . . . immunoglobulin heavy variable 5-51 . . . . . . . . . . . IGHV5-78 . . . immunoglobulin heavy variable 5-78 (pseudogene) . . . . . . . . . . . IGHV6-1 . . . immunoglobulin heavy variable 6-1 . . . . . . . . . . . IGHV7-4-1 . . . immunoglobulin heavy variable 7-4-1 . . . . . . . . . . . IGHV7-27 . . . immunoglobulin heavy variable 7-27 (pseudogene) . . . . . . . . . . . IGHV7-34-1 . . . immunoglobulin heavy variable 7-34-1 (pseudogene) . . . . . . . . . . . IGHV7-40 . . . immunoglobulin heavy variable 7-40 (pseudogene) . . . . . . . . . . . IGHV7-56 . . . immunoglobulin heavy variable 7-56 (pseudogene) . . . . . . . . . . . IGHV7-81 . . . immunoglobulin heavy variable 7-81 (non-functional) . . . . . . . . . . . IGHVII-1-1 . . . immunoglobulin heavy variable (II)-1-1 (pseudogene) . . . . . . . . . . . IGHVII-15-1 . . . immunoglobulin heavy variable (II)-15-1 (pseudogene) . . . . . . . . . . . IGHVII-20-1 . . . immunoglobulin heavy variable (II)-20-1 (pseudogene) . . . . . . . . . . . IGHVII-22-1 . . . immunoglobulin heavy variable (II)-22-1 (pseudogene) . . . . . . . . . . . IGHVII-26-2 . . . immunoglobulin heavy variable (II)-26-2 (pseudogene) . . . . . . . . . . . IGHVII-28-1 . . . immunoglobulin heavy variable (II)-28-1 (pseudogene) . . . . . . . . . . . IGHVII-30-1 . . . immunoglobulin heavy variable (II)-30-1 (pseudogene) . . . . . . . . . . . IGHVII-31-1 . . . immunoglobulin heavy variable (II)-31-1 (pseudogene) . . . . . . . . . . . IGHVII-33-1 . . . immunoglobulin heavy variable (II)-33-1 (pseudogene) . . . . . . . . . . . IGHVII-40-1 . . . immunoglobulin heavy variable (II)-40-1 (pseudogene) . . . . . . . . . . . IGHVII-43-1 . . . immunoglobulin heavy variable (II)-43-1 (pseudogene) . . . . . . . . . . . IGHVII-44-2 . . . immunoglobulin heavy variable (II)-44-2 (pseudogene) . . . . . . . . . . . IGHVII-46-1 . . . immunoglobulin heavy variable (II)-46-1 (pseudogene) . . . . . . . . . . . IGHVII-49-1 . . . immunoglobulin heavy variable (II)-49-1 (pseudogene) . . . . . . . . . . . IGHVII-51-2 . . . immunoglobulin heavy variable (II)-51-2 (pseudogene) . . . . . . . . . . . IGHVII-53-1 . . . immunoglobulin heavy variable (II)-53-1 (pseudogene) . . . . . . . . . . . IGHVII-60-1 . . . immunoglobulin heavy variable (II)-60-1 (pseudogene) . . . . . . . . . . . IGHVII-62-1 . . . immunoglobulin heavy variable (II)-62-1 (pseudogene) . . . . . . . . . . . IGHVII-65-1 . . . immunoglobulin heavy variable (II)-65-1 (pseudogene) . . . . . . . . . . . IGHVII-67-1 . . . immunoglobulin heavy variable (II)-67-1 (pseudogene) . . . . . . . . . . . IGHVII-74-1 . . . immunoglobulin heavy variable (II)-74-1 (pseudogene) . . . . . . . . . . . IGHVII-78-1 . . . immunoglobulin heavy variable (II)-78-1 (pseudogene) . . . . . . . . . . . IGHVIII-2-1 . . . immunoglobulin heavy variable (III)-2-1 (pseudogene) . . . . . . . . . . . IGHVIII-5-1 . . . immunoglobulin heavy variable (III)-5-1 (pseudogene) . . . . . . . . . . . IGHVIII-5-2 . . . immunoglobulin heavy variable (III)-5-2 (pseudogene) . . . . . . . . . . . IGHVIII-11-1 . . . immunoglobulin heavy variable (III)-11-1 (pseudogene) . . . . . . . . . . . IGHVIII-13-1 . . . immunoglobulin heavy variable (III)-13-1 (pseudogene) . . . . . . . . . . . IGHVIII-16-1 . . . immunoglobulin heavy variable (III)-16-1 (pseudogene) . . . . . . . . . . . IGHVIII-22-2 . . . immunoglobulin heavy variable (III)-22-2 (pseudogene) . . . . . . . . . . . IGHVIII-25-1 . . . immunoglobulin heavy variable (III)-25-1 (pseudogene) . . . . . . . . . . . IGHVIII-26-1 . . . immunoglobulin heavy variable (III)-26-1 (pseudogene) . . . . . . . . . . . IGHVIII-38-1 . . . immunoglobulin heavy variable (III)-38-1 (pseudogene) . . . . . . . . . . . IGHVIII-44 . . . immunoglobulin heavy variable (III)-44 (pseudogene) . . . . . . . . . . . IGHVIII-47-1 . . . immunoglobulin heavy variable (III)-47-1 (pseudogene) . . . . . . . . . . . IGHVIII-51-1 . . . immunoglobulin heavy variable (III)-51-1 (pseudogene) . . . . . . . . . . . IGHVIII-67-2 . . . immunoglobulin heavy variable (III)-67-2 (pseudogene) . . . . . . . . . . . IGHVIII-67-3 . . . immunoglobulin heavy variable (III)-67-3 (pseudogene) . . . . . . . . . . . IGHVIII-67-4 . . . immunoglobulin heavy variable (III)-67-4 (pseudogene) . . . . . . . . . . . IGHVIII-76-1 . . . immunoglobulin heavy variable (III)-76-1 (pseudogene) . . . . . . . . . . . IGHVIII-82 . . . immunoglobulin heavy variable (III)-82 (pseudogene) . . . . . . . . . . . IGHVIV-44-1 . . . immunoglobulin heavy variable (IV)-44-1 (pseudogene) . . . . . . . . . . . IGIP 0.41991884415955 0.464760799613531 0.115320356226919 IgA-inducing protein FUNCTION: Enhances IgA secretion from B-cells stimulated via CD40. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;cerebral cortex;endometrium;larynx;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;duodenum;liver;spleen;head and neck;kidney;stomach;aorta; . . . 0.746027844 86.40599198 76.02383 1.82726 IGJP1 . . . immunoglobulin J polypeptide pseudogene 1 . . . . . . . . . . . IGK . . . immunoglobulin kappa locus . . . . . . . . . . . IGKC . . . immunoglobulin kappa constant . DISEASE: Immunoglobulin kappa light chain deficiency (IGKCD) [MIM:614102]: A disease characterized by the complete absence of immunoglobulin kappa chains. {ECO:0000269|PubMed:3931219}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . . . . . . IGKDEL . . . immunoglobulin kappa deleting element or like . . . . . . . . . . . IGKJ1 . . . immunoglobulin kappa joining 1 . . . . . . . . . . . IGKJ2 . . . immunoglobulin kappa joining 2 . . . . . . . . . . . IGKJ3 . . . immunoglobulin kappa joining 3 . . . . . . . . . . . IGKJ4 . . . immunoglobulin kappa joining 4 . . . . . . . . . . . IGKJ5 . . . immunoglobulin kappa joining 5 . . . . . . . . . . . IGKV1-5 . . . immunoglobulin kappa variable 1-5 . . . . . . . . . . . IGKV1-6 . . . immunoglobulin kappa variable 1-6 . . . . . . . . . . . IGKV1-8 . . . immunoglobulin kappa variable 1-8 . . . . . . . . . . . IGKV1-9 . . . immunoglobulin kappa variable 1-9 . . . . . . . . . . . IGKV1-12 . . . immunoglobulin kappa variable 1-12 . . . . . . . . . . . IGKV1-13 . . . immunoglobulin kappa variable 1-13 (gene/pseudogene) . . . . . . . . . . . IGKV1-16 . . . immunoglobulin kappa variable 1-16 . . . . . . . . . . . IGKV1-17 . . . immunoglobulin kappa variable 1-17 . . . . . . . . . . . IGKV1-22 . . . immunoglobulin kappa variable 1-22 (pseudogene) . . . . . . . . . . . IGKV1-27 . . . immunoglobulin kappa variable 1-27 . . . . . . . . . . . IGKV1-32 . . . immunoglobulin kappa variable 1-32 (pseudogene) . . . . . . . . . . . IGKV1-33 . . . immunoglobulin kappa variable 1-33 . . . . . . . . . . . IGKV1-35 . . . immunoglobulin kappa variable 1-35 (pseudogene) . . . . . . . . . . . IGKV1-37 . . . immunoglobulin kappa variable 1-37 (non-functional) . . . . . . . . . . . IGKV1-39 . . . immunoglobulin kappa variable 1-39 (gene/pseudogene) . . . . . . . . . . . IGKV1D-8 . . . immunoglobulin kappa variable 1D-8 . . . . . . . . . . . IGKV1D-12 . . . immunoglobulin kappa variable 1D-12 . . . . . . . . . . . IGKV1D-13 . . . immunoglobulin kappa variable 1D-13 . . . . . . . . . . . IGKV1D-16 . . . immunoglobulin kappa variable 1D-16 . . . . . . . . . . . IGKV1D-17 . . . immunoglobulin kappa variable 1D-17 . . . . . . . . . . . IGKV1D-22 . . . immunoglobulin kappa variable 1D-22 (pseudogene) . . . . . . . . . . . IGKV1D-27 . . . immunoglobulin kappa variable 1D-27 (pseudogene) . . . . . . . . . . . IGKV1D-32 . . . immunoglobulin kappa variable 1D-32 (pseudogene) . . . . . . . . . . . IGKV1D-33 . . . immunoglobulin kappa variable 1D-33 . . . . . . . . . . . IGKV1D-35 . . . immunoglobulin kappa variable 1D-35 (pseudogene) . . . . . . . . . . . IGKV1D-37 . . . immunoglobulin kappa variable 1D-37 (non-functional) . . . . . . . . . . . IGKV1D-39 . . . immunoglobulin kappa variable 1D-39 . . . . . . . . . . . IGKV1D-42 . . . immunoglobulin kappa variable 1D-42 (non-functional) . . . . . . . . . . . IGKV1D-43 . . . immunoglobulin kappa variable 1D-43 . . . . . . . . . . . IGKV1OR-2 . . . immunoglobulin kappa variable 1/OR-2 (pseudogene) . . . . . . . . . . . IGKV1OR-3 . . . immunoglobulin kappa variable 1/OR-3 (pseudogene) . . . . . . . . . . . IGKV1OR-4 . . . immunoglobulin kappa variable 1/OR-4 (pseudogene) . . . . . . . . . . . IGKV1OR1-1 . . . immunoglobulin kappa variable 1/OR1-1 (pseudogene) . . . . . . . . . . . IGKV1OR2-0 . . . immunoglobulin kappa variable 1/OR2-0 (non-functional) . . . . . . . . . . . IGKV1OR2-1 . . . immunoglobulin kappa variable 1/OR2-1 (pseudogene) . . . . . . . . . . . IGKV1OR2-2 . . . immunoglobulin kappa variable 1/OR2-2 (pseudogene) . . . . . . . . . . . IGKV1OR2-3 . . . immunoglobulin kappa variable 1/OR2-3 (pseudogene) . . . . . . . . . . . IGKV1OR2-6 . . . immunoglobulin kappa variable 1/OR2-6 (pseudogene) . . . . . . . . . . . IGKV1OR2-9 . . . immunoglobulin kappa variable 1/OR2-9 (pseudogene) . . . . . . . . . . . IGKV1OR2-11 . . . immunoglobulin kappa variable 1/OR2-11 (pseudogene) . . . . . . . . . . . IGKV1OR2-108 . . . immunoglobulin kappa variable 1/OR2-108 (non-functional) . . . . . . . . . . . IGKV1OR2-118 . . . immunoglobulin kappa variable 1/OR2-118 (pseudogene) . . . . . . . . . . . IGKV1OR9-1 . . . immunoglobulin kappa variable 1/OR9-1 (pseudogene) . . . . . . . . . . . IGKV1OR9-2 . . . immunoglobulin kappa variable 1/OR9-2 (pseudogene) . . . . . . . . . . . IGKV1OR10-1 . . . immunoglobulin kappa variable 1/OR10-1 (pseudogene) . . . . . . . . . . . IGKV1OR15-118 . . . immunoglobulin kappa variable 1/OR15-118 (pseudogene) . . . . . . . . . . . IGKV1OR22-1 . . . immunoglobulin kappa variable 1/OR22-1 (pseudogene) . . . . . . . . . . . IGKV1OR22-5 . . . immunoglobulin kappa variable 1/OR22-5 (pseudogene) . . . . . . . . . . . IGKV1ORY-1 . . . immunoglobulin kappa variable 1/ORY-1 (pseudogene) . . . . . . . . . . . IGKV2-4 . . . immunoglobulin kappa variable 2-4 (pseudogene) . . . . . . . . . . . IGKV2-10 . . . immunoglobulin kappa variable 2-10 (pseudogene) . . . . . . . . . . . IGKV2-14 . . . immunoglobulin kappa variable 2-14 (pseudogene) . . . . . . . . . . . IGKV2-18 . . . immunoglobulin kappa variable 2-18 (pseudogene) . . . . . . . . . . . IGKV2-19 . . . immunoglobulin kappa variable 2-19 (pseudogene) . . . . . . . . . . . IGKV2-23 . . . immunoglobulin kappa variable 2-23 (pseudogene) . . . . . . . . . . . IGKV2-24 . . . immunoglobulin kappa variable 2-24 . . . . . . . . . . . IGKV2-26 . . . immunoglobulin kappa variable 2-26 (pseudogene) . . . . . . . . . . . IGKV2-28 . . . immunoglobulin kappa variable 2-28 . . . . . . . . . . . IGKV2-29 . . . immunoglobulin kappa variable 2-29 (gene/pseudogene) . . . . . . . . . . . IGKV2-30 . . . immunoglobulin kappa variable 2-30 . . . . . . . . . . . IGKV2-36 . . . immunoglobulin kappa variable 2-36 (pseudogene) . . . . . . . . . . . IGKV2-38 . . . immunoglobulin kappa variable 2-38 (pseudogene) . . . . . . . . . . . IGKV2-40 . . . immunoglobulin kappa variable 2-40 . . . . . . . . . . . IGKV2D-10 . . . immunoglobulin kappa variable 2D-10 (pseudogene) . . . . . . . . . . . IGKV2D-14 . . . immunoglobulin kappa variable 2D-14 (pseudogene) . . . . . . . . . . . IGKV2D-18 . . . immunoglobulin kappa variable 2D-18 (pseudogene) . . . . . . . . . . . IGKV2D-19 . . . immunoglobulin kappa variable 2D-19 (pseudogene) . . . . . . . . . . . IGKV2D-23 . . . immunoglobulin kappa variable 2D-23 (pseudogene) . . . . . . . . . . . IGKV2D-24 . . . immunoglobulin kappa variable 2D-24 (non-functional) . . . . . . . . . . . IGKV2D-26 . . . immunoglobulin kappa variable 2D-26 . . . . . . . . . . . IGKV2D-28 . . . immunoglobulin kappa variable 2D-28 . . . . . . . . . . . IGKV2D-29 . . . immunoglobulin kappa variable 2D-29 . . . . . . . . . . . IGKV2D-30 . . . immunoglobulin kappa variable 2D-30 . . . . . . . . . . . IGKV2D-36 . . . immunoglobulin kappa variable 2D-36 (pseudogene) . . . . . . . . . . . IGKV2D-38 . . . immunoglobulin kappa variable 2D-38 (pseudogene) . . . . . . . . . . . IGKV2D-40 . . . immunoglobulin kappa variable 2D-40 . . . . . . . . . . . IGKV2OR2-1 . . . immunoglobulin kappa variable 2/OR2-1 (pseudogene) . . . . . . . . . . . IGKV2OR2-2 . . . immunoglobulin kappa variable 2/OR2-2 (pseudogene) . . . . . . . . . . . IGKV2OR2-4 . . . immunoglobulin kappa variable 2/OR2-4 (pseudogene) . . . . . . . . . . . IGKV2OR2-7 . . . immunoglobulin kappa variable 2/OR2-7 (pseudogene) . . . . . . . . . . . IGKV2OR2-7D . . . immunoglobulin kappa variable 2/OR2-7D (pseudogene) . . . . . . . . . . . IGKV2OR2-8 . . . immunoglobulin kappa variable 2/OR2-8 (pseudogene) . . . . . . . . . . . IGKV2OR2-10 . . . immunoglobulin kappa variable 2/OR2-10 (pseudogene) . . . . . . . . . . . IGKV2OR22-3 . . . immunoglobulin kappa variable 2/OR22-3 (pseudogene) . . . . . . . . . . . IGKV2OR22-4 . . . immunoglobulin kappa variable 2/OR22-4 (pseudogene) . . . . . . . . . . . IGKV3-7 . . . immunoglobulin kappa variable 3-7 (non-functional) . . . . . . . . . . . IGKV3-11 . . . immunoglobulin kappa variable 3-11 . . . . . . . . . . . IGKV3-15 . . . immunoglobulin kappa variable 3-15 . . . . . . . . . . . IGKV3-20 . . . immunoglobulin kappa variable 3-20 . . . . . . . . . . . IGKV3-25 . . . immunoglobulin kappa variable 3-25 (pseudogene) . . . . . . . . . . . IGKV3-31 . . . immunoglobulin kappa variable 3-31 (pseudogene) . . . . . . . . . . . IGKV3-34 . . . immunoglobulin kappa variable 3-34 (pseudogene) . . . . . . . . . . . IGKV3D-7 . . . immunoglobulin kappa variable 3D-7 . . . . . . . . . . . IGKV3D-11 . . . immunoglobulin kappa variable 3D-11 . . . . . . . . . . . IGKV3D-15 . . . immunoglobulin kappa variable 3D-15 (gene/pseudogene) . . . . . . . . . . . IGKV3D-20 . . . immunoglobulin kappa variable 3D-20 . . . . . . . . . . . IGKV3D-25 . . . immunoglobulin kappa variable 3D-25 (pseudogene) . . . . . . . . . . . IGKV3D-31 . . . immunoglobulin kappa variable 3D-31 (pseudogene) . . . . . . . . . . . IGKV3D-34 . . . immunoglobulin kappa variable 3D-34 (pseudogene) . . . . . . . . . . . IGKV3OR2-5 . . . immunoglobulin kappa variable 3/OR2-5 (pseudogene) . . . . . . . . . . . IGKV3OR2-268 . . . immunoglobulin kappa variable 3/OR2-268 (non-functional) . . . . . . . . . . . IGKV3OR22-2 . . . immunoglobulin kappa variable 3/OR22-2 (pseudogene) . . . . . . . . . . . IGKV4-1 . . . immunoglobulin kappa variable 4-1 . . . . . . . . . . . IGKV5-2 . . . immunoglobulin kappa variable 5-2 . . . . . . . . . . . IGKV6-21 . . . immunoglobulin kappa variable 6-21 (non-functional) . . . . . . . . . . . IGKV6D-21 . . . immunoglobulin kappa variable 6D-21 (non-functional) . . . . . . . . . . . IGKV6D-41 . . . immunoglobulin kappa variable 6D-41 (non-functional) . . . . . . . . . . . IGKV7-3 . . . immunoglobulin kappa variable 7-3 (pseudogene) . . . . . . . . . . . IGL . . . immunoglobulin lambda locus . . . . . . . . . . . IGLC1 . . . immunoglobulin lambda constant 1 (Mcg marker) . . . . . . . . . . . IGLC2 . . . immunoglobulin lambda constant 2 (Kern-Oz- marker) . . . . . . . . . . . IGLC3 . . . immunoglobulin lambda constant 3 (Kern-Oz+ marker) . . . . . . . . . . . IGLC4 . . . immunoglobulin lambda constant 4 (pseudogene) . . . . . . . . . . . IGLC5 . . . immunoglobulin lambda constant 5 (pseudogene) . . . . . . . . . . . IGLC6 . . . immunoglobulin lambda constant 6 (Kern+Oz- marker, gene/pseudogene) . . . . . . . . . . . IGLC7 . . . immunoglobulin lambda constant 7 . . . . . . . . . . . IGLCOR22-1 . . . immunoglobulin lambda constant/OR22-1 (pseudogene) . . . . . . . . . . . IGLCOR22-2 . . . immunoglobulin lambda constant/OR22-2 (pseudogene) . . . . . . . . . . . IGLJ1 . . . immunoglobulin lambda joining 1 . . . . . . . . . . . IGLJ2 . . . immunoglobulin lambda joining 2 . . . . . . . . . . . IGLJ3 . . . immunoglobulin lambda joining 3 . . . . . . . . . . . IGLJ4 . . . immunoglobulin lambda joining 4 (non-functional) . . . . . . . . . . . IGLJ5 . . . immunoglobulin lambda joining 5 (non-functional) . . . . . . . . . . . IGLJ6 . . . immunoglobulin lambda joining 6 . . . . . . . . . . . IGLJ7 . . . immunoglobulin lambda joining 7 . . . . . . . . . . . IGLJCOR18 . . . immunoglobulin lambda joining-constant/OR18 (pseudogene) . . . . . . . . . . . IGLL1 0.0171677422605345 0.714489286512513 0.268342971226952 immunoglobulin lambda like polypeptide 1 FUNCTION: Critical for B-cell development. {ECO:0000269|PubMed:9419212}.; . TISSUE SPECIFICITY: Expressed only in pre-B-cells and a special B- cell line (which is surface Ig negative). {ECO:0000269|PubMed:2128466}.; unclassifiable (Anatomical System);lymph node;heart;epidermis;blood;bone marrow;uterus;frontal lobe;placenta;liver;testis;spleen;kidney;brain;parietal lobe;thymus; superior cervical ganglion;testis - interstitial;atrioventricular node;skeletal muscle;bone marrow; 0.06657 0.28478 . . 566.97931 4.83519 IGLL2P . . . immunoglobulin lambda like polypeptide 2, pseudogene . . . . . . . . . . . IGLL3P . . . immunoglobulin lambda like polypeptide 3, pseudogene . . . . . 0.05956 0.07001 . . . . IGLL4P . . . immunoglobulin lambda like polypeptide 4, pseudogene . . . . . . . . . . . IGLL5 . . . immunoglobulin lambda like polypeptide 5 . . TISSUE SPECIFICITY: Contrary to IGLL1, not expressed in pre-B- cells. {ECO:0000269|PubMed:1703205, ECO:0000269|PubMed:1900243}.; . . . . . . 130.94307 2.49261 IGLON5 0.822062298227498 0.177089676311471 0.000848025461031377 IgLON family member 5 . . . whole body;frontal lobe;retina; superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;cerebellum; . 0.09574 -0.273576253 33.97027601 48.05169 1.34836 IGLP1 . . . immune response to synthetic polypeptides 1 . . . . . . . . . . . IGLP2 . . . immune response to synthetic polypeptides 2 . . . . . . . . . . . IGLV1-36 . . . immunoglobulin lambda variable 1-36 . . . . . . . . . . . IGLV1-40 . . . immunoglobulin lambda variable 1-40 . . . . . . . . . . . IGLV1-41 . . . immunoglobulin lambda variable 1-41 (pseudogene) . . . . . . . . . . . IGLV1-44 . . . immunoglobulin lambda variable 1-44 . . . . . . . . . . . IGLV1-47 . . . immunoglobulin lambda variable 1-47 . . . . . . . . . . . IGLV1-50 . . . immunoglobulin lambda variable 1-50 (non-functional) . . . . . . . . . . . IGLV1-51 . . . immunoglobulin lambda variable 1-51 . . . . . . . . . . . IGLV1-62 . . . immunoglobulin lambda variable 1-62 (pseudogene) . . . . . . . . . . . IGLV2-5 . . . immunoglobulin lambda variable 2-5 (pseudogene) . . . . . . . . . . . IGLV2-8 . . . immunoglobulin lambda variable 2-8 . . . . . . . . . . . IGLV2-11 . . . immunoglobulin lambda variable 2-11 . . . . . . . . . . . IGLV2-14 . . . immunoglobulin lambda variable 2-14 . . . . . . . . . . . IGLV2-18 . . . immunoglobulin lambda variable 2-18 . . . . . . . . . . . IGLV2-23 . . . immunoglobulin lambda variable 2-23 . . . . . . . . . . . IGLV2-28 . . . immunoglobulin lambda variable 2-28 (pseudogene) . . . . . . . . . . . IGLV2-33 . . . immunoglobulin lambda variable 2-33 (non-functional) . . . . . . . . . . . IGLV2-34 . . . immunoglobulin lambda variable 2-34 (pseudogene) . . . . . . . . . . . IGLV3-1 . . . immunoglobulin lambda variable 3-1 . . . . . . . . . . . IGLV3-2 . . . immunoglobulin lambda variable 3-2 (pseudogene) . . . . . . . . . . . IGLV3-4 . . . immunoglobulin lambda variable 3-4 (pseudogene) . . . . . . . . . . . IGLV3-6 . . . immunoglobulin lambda variable 3-6 (pseudogene) . . . . . . . . . . . IGLV3-7 . . . immunoglobulin lambda variable 3-7 (pseudogene) . . . . . . . . . . . IGLV3-9 . . . immunoglobulin lambda variable 3-9 (gene/pseudogene) . . . . . . . . . . . IGLV3-10 . . . immunoglobulin lambda variable 3-10 . . . . . . . . . . . IGLV3-12 . . . immunoglobulin lambda variable 3-12 . . . . . . . . . . . IGLV3-13 . . . immunoglobulin lambda variable 3-13 (pseudogene) . . . . . . . . . . . IGLV3-15 . . . immunoglobulin lambda variable 3-15 (pseudogene) . . . . . . . . . . . IGLV3-16 . . . immunoglobulin lambda variable 3-16 . . . . . . . . . . . IGLV3-17 . . . immunoglobulin lambda variable 3-17 (pseudogene) . . . . . . . . . . . IGLV3-19 . . . immunoglobulin lambda variable 3-19 . . . . . . . . . . . IGLV3-21 . . . immunoglobulin lambda variable 3-21 . . . . . . . . . . . IGLV3-22 . . . immunoglobulin lambda variable 3-22 (gene/pseudogene) . . . . . . . . . . . IGLV3-24 . . . immunoglobulin lambda variable 3-24 (pseudogene) . . . . . . . . . . . IGLV3-25 . . . immunoglobulin lambda variable 3-25 . . . . . . . . . . . IGLV3-26 . . . immunoglobulin lambda variable 3-26 (pseudogene) . . . . . . . . . . . IGLV3-27 . . . immunoglobulin lambda variable 3-27 . . . . . . . . . . . IGLV3-29 . . . immunoglobulin lambda variable 3-29 (pseudogene) . . . . . . . . . . . IGLV3-30 . . . immunoglobulin lambda variable 3-30 (pseudogene) . . . . . . . . . . . IGLV3-31 . . . immunoglobulin lambda variable 3-31 (pseudogene) . . . . . . . . . . . IGLV3-32 . . . immunoglobulin lambda variable 3-32 (non-functional) . . . . . . . . . . . IGLV4-3 . . . immunoglobulin lambda variable 4-3 . . . . . . . . . . . IGLV4-60 . . . immunoglobulin lambda variable 4-60 . . . . . . . . . . . IGLV4-69 . . . immunoglobulin lambda variable 4-69 . . . . . . . . . . . IGLV5-37 . . . immunoglobulin lambda variable 5-37 . . . . . . . . . . . IGLV5-39 . . . immunoglobulin lambda variable 5-39 . . . . . . . . . . . IGLV5-45 . . . immunoglobulin lambda variable 5-45 . . . . . . . . . . . IGLV5-48 . . . immunoglobulin lambda variable 5-48 (non-functional) . . . . . . . . . . . IGLV5-52 . . . immunoglobulin lambda variable 5-52 . . . . . . . . . . . IGLV6-57 . . . immunoglobulin lambda variable 6-57 . . . . . . . . . . . IGLV7-35 . . . immunoglobulin lambda variable 7-35 (pseudogene) . . . . . . . . . . . IGLV7-43 . . . immunoglobulin lambda variable 7-43 . . . . . . . . . . . IGLV7-46 . . . immunoglobulin lambda variable 7-46 (gene/pseudogene) . . . . . . . . . . . IGLV8-61 . . . immunoglobulin lambda variable 8-61 . . . . . . . . . . . IGLV8OR8-1 . . . immunoglobulin lambda variable 8/OR8-1 (pseudogene) . . . . . . . . . . . IGLV9-49 . . . immunoglobulin lambda variable 9-49 . . . . . . . . . . . IGLV10-54 . . . immunoglobulin lambda variable 10-54 . . . . . . . . . . . IGLV10-67 . . . immunoglobulin lambda variable 10-67 (pseudogene) . . . . . . . . . . . IGLV11-55 . . . immunoglobulin lambda variable 11-55 (non-functional) . . . . . . . . . . . IGLVI-20 . . . immunoglobulin lambda variable (I)-20 (pseudogene) . . . . . . . . . . . IGLVI-38 . . . immunoglobulin lambda variable (I)-38 (pseudogene) . . . . . . . . . . . IGLVI-42 . . . immunoglobulin lambda variable (I)-42 (pseudogene) . . . . . . . . . . . IGLVI-56 . . . immunoglobulin lambda variable (I)-56 (pseudogene) . . . . . . . . . . . IGLVI-63 . . . immunoglobulin lambda variable (I)-63 (pseudogene) . . . . . . . . . . . IGLVI-68 . . . immunoglobulin lambda variable (I)-68 (pseudogene) . . . . . . . . . . . IGLVI-70 . . . immunoglobulin lambda variable (I)-70 (pseudogene) . . . . . . . . . . . IGLVIV-53 . . . immunoglobulin lambda variable (IV)-53 (pseudogene) . . . . . . . . . . . IGLVIV-59 . . . immunoglobulin lambda variable (IV)-59 (pseudogene) . . . . . . . . . . . IGLVIV-64 . . . immunoglobulin lambda variable (IV)-64 (pseudogene) . . . . . . . . . . . IGLVIV-65 . . . immunoglobulin lambda variable (IV)-65 (pseudogene) . . . . . . . . . . . IGLVIV-66-1 . . . immunoglobulin lambda variable (IV)-66-1 (pseudogene) . . . . . . . . . . . IGLVIVOR22-1 . . . immunoglobulin lambda variable (IV)/OR22-1 (pseudogene) . . . . . . . . . . . IGLVIVOR22-2 . . . immunoglobulin lambda variable (IV)/OR22-2 (pseudogene) . . . . . . . . . . . IGLVV-58 . . . immunoglobulin lambda variable (V)-58 (pseudogene) . . . . . . . . . . . IGLVV-66 . . . immunoglobulin lambda variable (V)-66 (pseudogene) . . . . . . . . . . . IGLVVI-22-1 . . . immunoglobulin lambda variable (VI)-22-1 (pseudogene) . . . . . . . . . . . IGLVVI-25-1 . . . immunoglobulin lambda variable (VI)-25-1 (pseudogene) . . . . . . . . . . . IGLVVII-41-1 . . . immunoglobulin lambda variable (VII)-41-1 (pseudogene) . . . . . . . . . . . IGSF1 0.996859546493677 0.00314045321736412 2.88958986275564e-10 immunoglobulin superfamily member 1 FUNCTION: Seems to be a coreceptor in inhibin signaling, but seems not to be a high-affinity inhibin receptor. Antagonizes activin A signaling in the presence or absence of inhibin B (By similarity). Necessary to mediate a specific antagonistic effect of inhibin B on activin-stimulated transcription. {ECO:0000250, ECO:0000269|PubMed:11266516}.; DISEASE: Hypothyroidism, central, and testicular enlargement (CHTE) [MIM:300888]: A disorder characterized by insufficient thyroid gland stimulation by thyroid stimulating hormone (TSH), resulting from hypothalamic and/or pituitary dysfunction. CHTE patients have delayed testosterone increase at puberty with normal testosterone levels in adulthood, normal testicular volume in childhood and enlarged testicles in adulthood. {ECO:0000269|PubMed:23143598}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in pancreas, testis and fetal liver. Moderately expressed in heart, prostate and small intestine. Expressed at very low levels in brain, thymus, ovary, colon, fetal lung and fetal kidney. Expressed in muscle. Isoform 3 is expressed in pituitary gland. {ECO:0000269|PubMed:11854097, ECO:0000269|PubMed:23143598, ECO:0000269|PubMed:9521868}.; unclassifiable (Anatomical System);smooth muscle;ovary;islets of Langerhans;optic nerve;whole body;lung;thyroid;liver;pituitary gland;testis;head and neck;spleen;brain;mammary gland; dorsal root ganglion;fetal liver;hypothalamus;spinal cord;atrioventricular node;pituitary; 0.60334 0.10920 -0.615405356 17.47464025 254.36126 3.43107 IGSF3 0.987084919325614 0.0129150788168979 1.8574884601247e-09 immunoglobulin superfamily member 3 . . TISSUE SPECIFICITY: Expressed in a wide range of tissues with High expression in Placenta, kidney and lung. {ECO:0000269|PubMed:9790749}.; unclassifiable (Anatomical System);skeletal muscle;skin;retina;whole body;lung;placenta;thyroid;bone;hypopharynx;head and neck;kidney;brain;mammary gland;stomach; superior cervical ganglion;fetal brain;placenta;ciliary ganglion;skeletal muscle; 0.55784 0.12462 -1.339418191 4.653220099 2964.58158 10.31731 IGSF5 2.32102326951294e-11 0.00982773376358613 0.990172266213204 immunoglobulin superfamily member 5 FUNCTION: Provides, together with MAGI1, an adhesion machinery at tight junctions, which may regulate the permeability of kidney glomerulus and small intestinal epithelial cells. Mediates calcium-independent homophilic cell adhesion. In testis, it may function as a cell adhesion molecule rather than a tight-junction protein. It may participate in the adhesion between spermatogonia- spermatogonia, spermatogonia-Sertoli cells, and Sertoli cells- Sertoli cells (By similarity). {ECO:0000250}.; . . . . 0.10684 0.08769 1.690270544 96.40835103 1603.80281 7.40729 IGSF6 0.0725547810761045 0.872351162813259 0.0550940561106366 immunoglobulin superfamily member 6 . . TISSUE SPECIFICITY: Expressed in peripheral blood lymphocytes, spleen and lymph node, with low levels in thymus, bone marrow and fetal liver. No expression in non-immune tissues. {ECO:0000269|PubMed:9809579}.; unclassifiable (Anatomical System);smooth muscle;lung;ovary;endometrium;nasopharynx;thyroid;placenta;liver;parathyroid;spleen;brain;mammary gland; superior cervical ganglion;whole blood;trigeminal ganglion; 0.10952 0.12308 0.104848986 61.49445624 53.37534 1.45134 IGSF8 2.27585228881138e-06 0.900861226950215 0.0991364971974966 immunoglobulin superfamily member 8 FUNCTION: May play a key role in diverse functions ascribed to CD81 and CD9 such as oocytes fertilization or hepatitis C virus function. May regulate proliferation and differentiation of keratinocytes. May be a negative regulator of cell motility: suppresses T-cell mobility coordinately with CD81, associates with CD82 to suppress prostate cancer cell migration, regulates epidermoid cell reaggregation and motility on laminin-5 with CD9 and CD81 as key linkers. May also play a role on integrin- dependent morphology and motility functions. May participate in the regulation of neurite outgrowth and maintenance of the neural network in the adult brain. {ECO:0000269|PubMed:11504738, ECO:0000269|PubMed:12750295, ECO:0000269|PubMed:12752121, ECO:0000269|PubMed:14662754, ECO:0000269|PubMed:15070678}.; . TISSUE SPECIFICITY: Expressed in brain, kidney, testis, liver and placenta with moderate expression in all other tissues. Detected on a majority of B-cells, T-cells, and natural killer cells but not on monocytes, polynuclear cells and platelets. {ECO:0000269|PubMed:11504738, ECO:0000269|PubMed:12708969, ECO:0000269|PubMed:12750295}.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;cervix;kidney;mammary gland;stomach;aorta;cerebellum;thymus; . 0.20547 0.12178 -1.374132436 4.429110639 144.07906 2.61454 IGSF9 0.568910879897229 0.43108908479973 3.53030408952838e-08 immunoglobulin superfamily member 9 FUNCTION: Functions in dendrite outgrowth and synapse maturation. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;colon;parathyroid;fovea centralis;choroid;lens;retina;uterus;breast;optic nerve;lung;endometrium;placenta;thyroid;macula lutea;visual apparatus;liver;testis;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.25590 0.10848 0.143271594 63.67067705 1923.17488 8.07309 IGSF9B 0.99987339409272 0.000126605906709361 5.70171697261147e-13 immunoglobulin superfamily member 9B . . . unclassifiable (Anatomical System);prostate;adrenal gland;brain;cerebellum; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.13310 . . . 323.26411 3.81929 IGSF10 2.98760657394284e-36 7.28947515131525e-07 0.999999271052485 immunoglobulin superfamily member 10 FUNCTION: May be involved in the maintenance of osteochondroprogenitor cells pool. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;cartilage;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;whole body;lung;thyroid;macula lutea;testis;head and neck; . 0.19772 0.09261 0.003288954 54.03986789 945.99005 5.95755 IGSF11 0.175167238322195 0.822111121552594 0.00272164012521033 immunoglobulin superfamily member 11 FUNCTION: Functions as a cell adhesion molecule through homophilic interaction. Stimulates cell growth. {ECO:0000269|PubMed:15795899, ECO:0000269|PubMed:16108831}.; . TISSUE SPECIFICITY: Abundantly expressed in testis and ovary and to a lower extent in brain, kidney and skeletal muscle. {ECO:0000269|PubMed:16108831}.; unclassifiable (Anatomical System);medulla oblongata;optic nerve;lung;frontal lobe;testis;brain;skin; superior cervical ganglion;testis;trigeminal ganglion; 0.28733 0.11313 0.108486928 61.90728946 2049.56865 8.34351 IGSF11-AS1 . . . IGSF11 antisense RNA 1 . . . . . . . . . . . IGSF21 0.547298802614659 0.452090627993744 0.000610569391597476 immunoglobin superfamily member 21 . . . unclassifiable (Anatomical System);ovary;pineal body;parathyroid;fovea centralis;choroid;retina;pancreas;prostate;optic nerve;lung;frontal lobe;placenta;macula lutea;hippocampus;brain;aorta; subthalamic nucleus;superior cervical ganglion;fetal brain;cerebellum peduncles;globus pallidus;parietal lobe;cerebellum; 0.24458 0.11097 -0.596992387 18.18825195 624.00017 5.03935 IGSF22 1.19691570710455e-20 0.0044308696259673 0.995569130374033 immunoglobulin superfamily member 22 . . . unclassifiable (Anatomical System);prostate;lung;ovary;sympathetic chain;testis;kidney;germinal center;brain;skeletal muscle;retina; . 0.16772 . 3.993906162 99.65793819 7024.76421 17.86174 IGSF23 . . . immunoglobulin superfamily member 23 . . . . . . . . . . . IHG1 . . . iris hypoplasia with glaucoma 1 . . . . . . . . . . . IHH 0.349924208747533 0.636861235089398 0.0132145561630695 indian hedgehog FUNCTION: Intercellular signal essential for a variety of patterning events during development. Binds to the patched (PTC) receptor, which functions in association with smoothened (SMO), to activate the transcription of target genes. Implicated in endochondral ossification: may regulate the balance between growth and ossification of the developing bones. Induces the expression of parathyroid hormone-related protein (PTHRP) (By similarity). {ECO:0000250, ECO:0000269|PubMed:21537345}.; DISEASE: Brachydactyly A1 (BDA1) [MIM:112500]: A form of brachydactyly. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. Brachydactyly type A1 is characterized by middle phalanges of all the digits rudimentary or fused with the terminal phalanges. The proximal phalanges of the thumbs and big toes are short. {ECO:0000269|PubMed:11455389, ECO:0000269|PubMed:12384778}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Acrocapitofemoral dysplasia (ACFD) [MIM:607778]: A disorder characterized by short stature of variable severity with postnatal onset. The most constant radiographic abnormalities are observed in the tubular bones of the hands and in the proximal part of the femur. Cone-shaped epiphyses or a similar epiphyseal configuration with premature epimetaphyseal fusion result in shortening of the skeletal components involved. Cone-shaped epiphyses are also present to a variable extent at the shoulders, knees and ankles. {ECO:0000269|PubMed:12632327}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in embryonic lung, and in adult kidney and liver.; unclassifiable (Anatomical System);colon;blood;fovea centralis;choroid;lens;retina;prostate;optic nerve;whole body;endometrium;macula lutea;liver;spleen;kidney;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.68460 0.59447 -0.22584292 37.32012267 131.75567 2.49813 IK 3.47058187314951e-06 0.999419482166242 0.000577047251885154 IK cytokine, down-regulator of HLA II FUNCTION: May bind to chromatin.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;smooth muscle;ovary;skin;retina;prostate;ganglion;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;gall bladder;heart;cartilage;pharynx;blood;lens;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;oral cavity;muscle;pancreas;lung;cornea;adrenal gland;placenta;head and neck;kidney;stomach;aorta; testis - interstitial;thalamus;testis - seminiferous tubule;testis;atrioventricular node;cingulate cortex; . . 0.12689526 63.00424628 46.99547 1.32600 IKBIP 9.59326123111629e-05 0.564688284490869 0.435215782896819 IKBKB interacting protein FUNCTION: Target of p53/TP53 with pro-apoptotic function. {ECO:0000269|PubMed:15389287}.; . TISSUE SPECIFICITY: Expressed in vein endothelial cells. Isoform 4 is expressed in lung, kidney, spleen, thymus and skeletal muscle. {ECO:0000269|PubMed:15389287}.; smooth muscle;ovary;colon;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;blood;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; ciliary ganglion;atrioventricular node; . . 0.178263593 66.12998349 299.21117 3.68807 IKBKAP 1.20456829864128e-08 0.999998870655977 1.11729834006819e-06 inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase complex-associated protein FUNCTION: May act as a scaffold protein that may assemble active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK).; DISEASE: Neuropathy, hereditary sensory and autonomic, 3 (HSAN3) [MIM:223900]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by sensory and/or autonomic abnormalities. HSAN3 patients manifest a variety of symptoms such as alacrima, decreased taste, decreased sensitivity to pain and temperature, vasomotor instability, hypoactive or absent deep tendon reflexes, vomiting crises, and gastrointestinal dysfunction. {ECO:0000269|PubMed:11179008, ECO:0000269|PubMed:11179021}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.61725 0.55289 0.837675873 88.18117481 8968.13307 20.53278 IKBKB 0.998786698708708 0.00121330128554223 5.75000460544719e-12 inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase beta FUNCTION: Serine kinase that plays an essential role in the NF- kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Phosphorylates FOXO3, mediating the TNF- dependent inactivation of this pro-apoptotic transcription factor. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation. {ECO:0000269|PubMed:11297557, ECO:0000269|PubMed:15084260, ECO:0000269|PubMed:17213322, ECO:0000269|PubMed:19716809, ECO:0000269|PubMed:20410276, ECO:0000269|PubMed:20434986, ECO:0000269|PubMed:20797629, ECO:0000269|PubMed:21138416}.; DISEASE: Immunodeficiency 15 (IMD15) [MIM:615592]: An autosomal recessive primary immunodeficiency disorder characterized by onset in infancy of life-threatening bacterial, fungal, and viral infections and failure to thrive. Laboratory studies show hypo- or agammaglobulinemia with relatively normal numbers of B and T- cells, and impaired differentiation and activation of immune cells. {ECO:0000269|PubMed:24369075}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in heart, placenta, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis and peripheral blood.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; dorsal root ganglion;uterus corpus;superior cervical ganglion;appendix;ciliary ganglion;white blood cells;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.43187 0.81149 -0.754958418 13.57631517 247.23048 3.39162 IKBKE 0.804391777009201 0.195607844873679 3.78117119570632e-07 inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase epsilon FUNCTION: Serine/threonine kinase that plays an essential role in regulating inflammatory responses to viral infection, through the activation of the type I IFN, NF-kappa-B and STAT signaling. Also involved in TNFA and inflammatory cytokines, like Interleukin-1, signaling. Following activation of viral RNA sensors, such as RIG- I-like receptors, associates with DDX3X and phosphorylates interferon regulatory factors (IRFs), IRF3 and IRF7, as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRF3 leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNB. In order to establish such an antiviral state, IKBKE forms several different complexes whose composition depends on the type of cell and cellular stimuli. Thus, several scaffolding molecules including IPS1/MAVS, TANK, AZI2/NAP1 or TBKBP1/SINTBAD can be recruited to the IKBKE-containing-complexes. Activated by polyubiquitination in response to TNFA and interleukin-1, regulates the NF-kappa-B signaling pathway through, at least, the phosphorylation of CYLD. Phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. In addition, is also required for the induction of a subset of ISGs which displays antiviral activity, may be through the phosphorylation of STAT1 at 'Ser-708'. Phosphorylation of STAT1 at 'Ser-708' seems also to promote the assembly and DNA binding of ISGF3 (STAT1:STAT2:IRF9) complexes compared to GAF (STAT1:STAT1) complexes, in this way regulating the balance between type I and type II IFN responses. Protects cells against DNA damage-induced cell death. Also plays an important role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity. Phosphorylates AKT1. {ECO:0000269|PubMed:17568778, ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:19153231, ECO:0000269|PubMed:20188669, ECO:0000269|PubMed:21138416, ECO:0000269|PubMed:21464307, ECO:0000269|PubMed:22532683, ECO:0000269|PubMed:23453969, ECO:0000269|PubMed:23478265}.; . TISSUE SPECIFICITY: Highly expressed in spleen followed by thymus, peripheral blood leukocytes, pancreas, placenta. Weakly expressed in lung, kidney, prostate, ovary and colon.; . . 0.44931 0.19128 -0.150608082 42.28001887 2297.49177 8.87689 IKBKG 0.628614516375526 0.340994428848876 0.0303910547755975 inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma FUNCTION: Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. However, the specific type of polyubiquitin recognized upon cell stimulation (either 'Lys-63'- linked or linear polyubiquitin) and its functional importance is reported conflictingly. Also considered to be a mediator for TAX activation of NF-kappa-B. Could be implicated in NF-kappa-B- mediated protection from cytokine toxicity. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination. {ECO:0000269|PubMed:14695475, ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20724660}.; DISEASE: Ectodermal dysplasia, anhidrotic, with immunodeficiency X-linked (EDAID) [MIM:300291]: A form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by absence of sweat glands, sparse scalp hair, rare conical teeth and immunological abnormalities resulting in severe infectious diseases. {ECO:0000269|PubMed:11047757, ECO:0000269|PubMed:11224521, ECO:0000269|PubMed:11242109, ECO:0000269|PubMed:12045264, ECO:0000269|PubMed:15100680}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ectodermal dysplasia, anhidrotic, with immunodeficiency, osteopetrosis and lymphedema (OLEDAID) [MIM:300301]: A form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by the association of anhidrotic ectodermal dysplasia with severe immunodeficiency, osteopetrosis and lymphedema. {ECO:0000269|PubMed:11242109}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Immunodeficiency, NEMO-related, without anhidrotic ectodermal dysplasia (NEMOID) [MIM:300584]: Patients manifest immunodeficiency not associated with other abnormalities, and resulting in increased susceptibility to infections. Patients suffer from multiple episodes of infectious diseases. {ECO:0000269|PubMed:15100680, ECO:0000269|PubMed:15356572}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Immunodeficiency 33 (IMD33) [MIM:300636]: A X-linked recessive form of Mendelian susceptibility to mycobacterial disease, a rare condition characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non- tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. {ECO:0000269|PubMed:16818673}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Recurrent isolated invasive pneumococcal disease 2 (IPD2) [MIM:300640]: Recurrent invasive pneumococcal disease (IPD) is defined as two episodes of IPD occurring at least 1 month apart, whether caused by the same or different serotypes or strains. Recurrent IPD occurs in at least 2% of patients in most series, making IPD the most important known risk factor for subsequent IPD. {ECO:0000269|PubMed:16950813}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Incontinentia pigmenti (IP) [MIM:308300]: A genodermatosis usually prenatally lethal in males. In affected females, it causes abnormalities of the skin, hair, eyes, nails, teeth, skeleton, heart, and central nervous system. The prominent skin signs occur in four classic cutaneous stages: perinatal inflammatory vesicles, verrucous patches, a distinctive pattern of hyperpigmentation and dermal scarring. {ECO:0000269|PubMed:10839543, ECO:0000269|PubMed:11590134, ECO:0000269|PubMed:15229184, ECO:0000269|PubMed:17728323, ECO:0000269|PubMed:20434027, ECO:0000269|PubMed:24339369}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; ovary;umbilical cord;salivary gland;colon;choroid;skin;bone marrow;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;tongue;islets of Langerhans;blood;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;stomach; . 0.36770 0.62771 . . 2.5256 0.09337 IKBKGP1 . . . inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma pseudogene 1 . . . . . . . . . . . IKZF1 0.985751324145976 0.0142417135892557 6.9622647680162e-06 IKAROS family zinc finger 1 FUNCTION: Transcription regulator of hematopoietic cell differentiation (PubMed:17934067). Binds gamma-satellite DNA (PubMed:17135265, PubMed:19141594). Plays a role in the development of lymphocytes, B- and T-cells. Binds and activates the enhancer (delta-A element) of the CD3-delta gene. Repressor of the TDT (fikzfterminal deoxynucleotidyltransferase) gene during thymocyte differentiation. Regulates transcription through association with both HDAC-dependent and HDAC-independent complexes. Targets the 2 chromatin-remodeling complexes, NuRD and BAF (SWI/SNF), in a single complex (PYR complex), to the beta- globin locus in adult erythrocytes. Increases normal apoptosis in adult erythroid cells. Confers early temporal competence to retinal progenitor cells (RPCs) (By similarity). Function is isoform-specific and is modulated by dominant-negative inactive isoforms (PubMed:17135265, PubMed:17934067). {ECO:0000250|UniProtKB:Q03267, ECO:0000269|PubMed:10204490, ECO:0000269|PubMed:17135265, ECO:0000269|PubMed:17934067, ECO:0000269|PubMed:19141594}.; DISEASE: Note=Defects in IKZF1 are frequent occurrences (28.6%) in acute lymphoblasic leukemia (ALL). Such alterations or deletions lead to poor prognosis for ALL.; DISEASE: Note=Chromosomal aberrations involving IKZF1 are a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;7)(q27;p12), with BCL6.; TISSUE SPECIFICITY: Abundantly expressed in thymus, spleen and peripheral blood Leukocytes and lymph nodes. Lower expression in bone marrow and small intestine. {ECO:0000269|PubMed:8543809, ECO:0000269|PubMed:8964602}.; lymphoreticular;ovary;salivary gland;colon;parathyroid;bone marrow;prostate;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;stomach;thymus; superior cervical ganglion;appendix;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.62256 0.46610 . . 20.85855 0.70589 IKZF2 0.922956763628976 0.0770241115518539 1.91248191695813e-05 IKAROS family zinc finger 2 FUNCTION: Associates with Ikaros at centromeric heterochromatin.; . . nasopharynx;thyroid;testis;head and neck; . 0.91208 0.17129 0.020302773 55.60863411 105.57661 2.22656 IKZF3 0.994921787627197 0.00507765522447376 5.5714832920275e-07 IKAROS family zinc finger 3 FUNCTION: Transcription factor that plays an important role in the regulation of lymphocyte differentiation. Plays an essential role in regulation of B-cell differentiation, proliferation and maturation to an effector state. Involved in regulating BCL2 expression and controlling apoptosis in T-cells in an IL2- dependent manner. {ECO:0000269|PubMed:10369681}.; . TISSUE SPECIFICITY: Expressed most strongly in peripheral blood leukocytes, the spleen, and the thymus. {ECO:0000269|PubMed:17646674}.; unclassifiable (Anatomical System);breast;lymph node;nasopharynx;blood;thymus; superior cervical ganglion;appendix; 0.78577 0.21092 -0.336073593 30.55555556 47.30933 1.33384 IKZF4 0.953608121096321 0.0463656847820255 2.61941216537142e-05 IKAROS family zinc finger 4 FUNCTION: DNA-binding protein that binds to the 5'GGGAATRCC-3' Ikaros-binding sequence. Transcriptional repressor. Interacts with SPI1 and MITF to repress transcription of the CTSK and ACP5 promoters via recruitment of corepressors SIN3A and CTBP2. May be involved in the development of central and peripheral nervous systems. Essential for the inhibitory function of regulatory T- cells (Treg). Mediates FOXP3-mediated gene silencing in regulatory T-cells (Treg) via recruitment of corepressor CTBP1 (By similarity). {ECO:0000250|UniProtKB:Q8C208, ECO:0000269|PubMed:10978333, ECO:0000269|PubMed:12015313, ECO:0000269|PubMed:12444977}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle, low levels of expression in heart, thymus, kidney, liver, and spleen. Expressed in the hematopoietic cell lines MOLT-4, NALM-6 and K- 562. Highly expressed in THP-1 and M-07e cell lines, which have characteristics of myeloid and early megakaryocytic cells respectively. {ECO:0000269|PubMed:10978333}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lacrimal gland;tongue;islets of Langerhans;blood;lens;skeletal muscle;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.85540 0.26738 -0.490397599 22.50530786 61.86299 1.60316 IKZF5 0.422736840290601 0.569588162381453 0.00767499732794545 IKAROS family zinc finger 5 FUNCTION: DNA-binding protein that binds to the 5'GNNTGTNG-3' core sequence. Transcriptional repressor. {ECO:0000269|PubMed:10978333}.; . TISSUE SPECIFICITY: Expressed in brain, heart, skeletal muscle, kidney, and liver. Expressed in the hematopoietic cell lines MOLT- 4, NALM-6 and K-562. Highly expressed in THP-1 and M-07e cell lines, which have characteristics of myeloid and early megakaryocytic cells respectively. {ECO:0000269|PubMed:10978333}.; . . 0.47442 0.11873 -0.295622497 32.61972163 27.45935 0.88455 IL1A 1.1235918506998e-05 0.360090126484535 0.639898637596958 interleukin 1 alpha FUNCTION: Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.; . . unclassifiable (Anatomical System);lung;ovary;tongue;placenta;testis;colon;pharynx;parathyroid;cervix;germinal center;skin; testis - interstitial;superior cervical ganglion;smooth muscle;testis - seminiferous tubule;testis;ciliary ganglion; 0.04484 0.95426 0.617373774 83.25076669 924.97942 5.90707 IL1B 0.925868311820487 0.0740462147216012 8.54734579118533e-05 interleukin 1 beta FUNCTION: Potent proinflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. {ECO:0000269|PubMed:3920526}.; . TISSUE SPECIFICITY: Expressed in activated monocytes/macrophages (at protein level). {ECO:0000269|PubMed:15192144}.; unclassifiable (Anatomical System);lymphoreticular;cartilage;islets of Langerhans;colon;blood;skin;skeletal muscle;bone marrow;uterus;bile duct;pancreas;lung;gum;nasopharynx;trabecular meshwork;liver;testis;spleen;brain;bladder;stomach; superior cervical ganglion;smooth muscle;atrioventricular node;trigeminal ganglion; 0.06986 0.99162 -0.383807564 27.41802312 9.81527 0.35980 IL1F10 0.0039602428583005 0.646460279805334 0.349579477336365 interleukin 1 family member 10 (theta) FUNCTION: Cytokine with immunomodulatory activity. Alone, does not induce cytokine production, but reduces IL22 and IL17A production by T-cells in response to heat-killed Candida albicans. Reduces IL36G-induced production of IL8 by peripheral blood mononuclear cells. Increases IL6 production by dendritic cells stimulated by bacterial lipopolysaccharides (LPS). Ligand for IL-36R/IL1RL2. {ECO:0000269|PubMed:22315422}.; . TISSUE SPECIFICITY: Expressed in fetal skin, spleen and tonsil. Expressed mostly in the basal epithelia of skin and in proliferating B-cells of the tonsil.; unclassifiable (Anatomical System);lung;placenta; . 0.18773 . 0.571462851 81.99457419 35.33832 1.06803 IL1R1 0.362921430952917 0.636565704544527 0.000512864502555773 interleukin 1 receptor type 1 FUNCTION: Receptor for IL1A, IL1B and IL1RN. After binding to interleukin-1 associates with the corecptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex. {ECO:0000269|PubMed:10671496}.; . . ovary;colon;parathyroid;skin;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;liver;spleen;head and neck;kidney;stomach;aorta;peripheral nerve; adipose tissue;adrenal gland;placenta;ciliary ganglion;trigeminal ganglion; 0.18971 0.60130 0.086440867 60.47416844 126.73913 2.45532 IL1R2 1.95242791720407e-07 0.251997657884069 0.748002146873139 interleukin 1 receptor type 2 FUNCTION: Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B activities. Serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. Also modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors. {ECO:0000269|PubMed:10975853, ECO:0000269|PubMed:12530978, ECO:0000269|PubMed:7989776, ECO:0000269|PubMed:9862719}.; . . unclassifiable (Anatomical System);lymph node;cartilage;colon;blood;bone marrow;uterus;prostate;lung;larynx;bone;thyroid;head and neck;kidney;brain;stomach; superior cervical ganglion;placenta;fetal lung;whole blood;tonsil;bone marrow; 0.70120 0.27043 -0.710864321 14.5730125 77.72976 1.85814 IL1RAP 0.506746749056946 0.492413558853277 0.000839692089776977 interleukin 1 receptor accessory protein FUNCTION: Coreceptor for IL1RL2 in the IL-36 signaling system (By similarity). Coreceptor with IL1R1 in the IL-1 signaling system. Associates with IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor complex which mediates interleukin-1- dependent activation of NF-kappa-B and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Recruits TOLLIP to the signaling complex. Does not bind to interleukin-1 alone; binding of IL1RN to IL1R1, prevents its association with IL1R1 to form a signaling complex. The cellular response is modulated through a non- signaling association with the membrane IL1R2 decoy receptor. Secreted forms (isoforms 2 and 3) associate with secreted ligand- bound IL1R2 and increase the affinity of secreted IL1R2 for IL1B; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors. {ECO:0000250|UniProtKB:Q61730, ECO:0000269|PubMed:10799889, ECO:0000269|PubMed:12530978, ECO:0000269|PubMed:9371760}.; . TISSUE SPECIFICITY: Detected in liver, skin, placenta, thymus and lung. {ECO:0000269|PubMed:12530978}.; unclassifiable (Anatomical System);lymph node;heart;colon;blood;skin;bone marrow;uterus;prostate;whole body;lung;frontal lobe;thyroid;placenta;liver;head and neck;spleen;brain;mammary gland;bladder;stomach;gall bladder; superior cervical ganglion;subthalamic nucleus;fetal liver;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.79429 0.22309 -0.644723694 16.52512385 164.92286 2.80728 IL1RAPL1 0.996893678356441 0.00310615382799302 1.6781556545553e-07 interleukin 1 receptor accessory protein like 1 FUNCTION: May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in presynaptic and postsynaptic differentiation and dendritic spine formation in neurons. {ECO:0000269|PubMed:12783849, ECO:0000269|PubMed:15123616}.; . TISSUE SPECIFICITY: Detected at low levels in heart, skeletal muscle, ovary, skin, amygdala, caudate nucleus, corpus callosum, hippocampus, substantia nigra and thalamus. Detected at very low levels in tonsil, prostate, testis, small intestine, placenta, colon and fetal liver. {ECO:0000269|PubMed:10471494, ECO:0000269|PubMed:10882729}.; unclassifiable (Anatomical System);frontal lobe;skeletal muscle; dorsal root ganglion;occipital lobe;medulla oblongata;superior cervical ganglion;temporal lobe;pons;atrioventricular node;subthalamic nucleus;prefrontal cortex;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.78830 0.22741 -0.60427181 17.74593064 15.07771 0.54108 IL1RAPL2 0.973379475963156 0.026613945040013 6.57899683103226e-06 interleukin 1 receptor accessory protein like 2 . . TISSUE SPECIFICITY: Detected at low levels in fetal and adult brain, in particular in the frontal lobe, temporal lobe and cerebellum. Detected at very low levels in skin, liver, fetal ovary and in placenta. {ECO:0000269|PubMed:10882729, ECO:0000269|PubMed:11031108, ECO:0000269|PubMed:11587848}.; . . 0.30056 0.12272 -0.337894035 30.37272942 9.79385 0.35811 IL1RL1 1.28060324751977e-07 0.577317111815784 0.422682760123891 interleukin 1 receptor like 1 FUNCTION: Receptor for interleukin-33 (IL-33), its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. Possibly involved in helper T-cell function. {ECO:0000269|PubMed:16286016}.; . TISSUE SPECIFICITY: Highly expressed in kidney, lung, placenta, stomach, skeletal muscle, colon and small intestine. Isoform A is prevalently expressed in the lung, testis, placenta, stomach and colon. Isoform B is more abundant in the brain, kidney and the liver. Isoform C is not detected in brain, heart, liver, kidney and skeletal muscle. {ECO:0000269|PubMed:11478810}.; unclassifiable (Anatomical System);uterus;lung;placenta;liver;blood;spleen;kidney;brain;stomach;aorta;bone marrow; superior cervical ganglion;medulla oblongata;placenta;adrenal cortex;fetal lung;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13061 0.21023 2.780116508 99.03279075 8878.57051 20.33646 IL1RL2 1.96903985630201e-07 0.873537466131881 0.126462336964133 interleukin 1 receptor like 2 FUNCTION: Receptor for interleukin-36 (IL36A, IL36B and IL36G). After binding to interleukin-36 associates with the coreceptor IL1RAP to form the interleukin-36 receptor complex which mediates interleukin-36-dependent activation of NF-kappa-B, MAPK and other pathways (By similarity). The IL-36 signaling system is thought to be present in epithelial barriers and to take part in local inflammatory response; it is similar to the IL-1 system. Seems to be involved in skin inflammatory response by induction of the IL- 23/IL-17/IL-22 pathway. {ECO:0000250|UniProtKB:Q9ERS7, ECO:0000269|PubMed:11466363}.; . TISSUE SPECIFICITY: Expressed in synovial fibroblasts and articular chondrocytes. Expressed in keratinocytes and monocyte- derived dendritic cells. Expressed in monocytes and myeloid dendritic cells; at protein level. {ECO:0000269|PubMed:16646978, ECO:0000269|PubMed:24829417}.; cartilage;mammary gland;skin; superior cervical ganglion; 0.09088 0.10308 -0.174473069 40.59919792 669.58351 5.17465 IL1RN 0.340218948927042 0.645559637899344 0.0142214131736131 interleukin 1 receptor antagonist FUNCTION: Inhibits the activity of interleukin-1 by binding to receptor IL1R1 and preventing its association with the coreceptor IL1RAP for signaling. Has no interleukin-1 like activity. Binds functional interleukin-1 receptor IL1R1 with greater affinity than decoy receptor IL1R2; however, the physiological relevance of the latter association is unsure. {ECO:0000269|PubMed:7775431}.; DISEASE: Interleukin 1 receptor antagonist deficiency (DIRA) [MIM:612852]: A rare autoinflammatory disease of skin and bone resulting in sterile multifocal osteomyelitis, periostitis, and pustulosis from birth. The term autoinflammatory disease describes a group of disorders characterized by attacks of seemingly unprovoked inflammation without significant levels of autoantibodies and autoreactive T-cells. {ECO:0000269|PubMed:19494218}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: The intracellular form of IL1RN is predominantly expressed in epithelial cells.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;cochlea;larynx;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);heart;tongue;oral cavity;urinary;blood;lens;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; uterus corpus;superior cervical ganglion;tongue;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin;tonsil; 0.09392 0.71118 -0.692458599 14.96815287 19.76062 0.67491 IL2 0.784777636804067 0.208550475484199 0.00667188771173401 interleukin 2 FUNCTION: Produced by T-cells in response to antigenic or mitogenic stimulation, this protein is required for T-cell proliferation and other activities crucial to regulation of the immune response. Can stimulate B-cells, monocytes, lymphokine- activated killer cells, natural killer cells, and glioma cells.; DISEASE: Note=A chromosomal aberration involving IL2 is found in a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(4;16)(q26;p13) with involves TNFRSF17. {ECO:0000269|PubMed:1396583}.; . unclassifiable (Anatomical System);blood; superior cervical ganglion;ciliary ganglion; 0.42365 0.95626 0.301449681 71.80938901 5.78948 0.21835 IL2RA 0.881288719632373 0.118423307446338 0.000287972921289504 interleukin 2 receptor subunit alpha FUNCTION: Receptor for interleukin-2. The receptor is involved in the regulation of immune tolerance by controlling regulatory T cells (TREGs) activity. TREGs suppress the activation and expansion of autoreactive T cells. {ECO:0000269|PubMed:23416241, ECO:0000269|PubMed:24116927}.; DISEASE: Diabetes mellitus, insulin-dependent, 10 (IDDM10) [MIM:601942]: A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:17676041}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Immunodeficiency 41 with lymphoproliferation and autoimmunity (IMD41) [MIM:606367]: A disorder of immune dysregulation characterized by recurrent viral, fungal, and bacterial infections, lymphadenopathy, and variable autoimmune features, such as autoimmune enteropathy and eczematous skin lesions. {ECO:0000269|PubMed:23416241, ECO:0000269|PubMed:24116927}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);smooth muscle; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;skin;skeletal muscle; 0.06341 0.69509 -0.60427181 17.74593064 9.33051 0.34222 IL2RB 0.986756575573638 0.0132422461894242 1.17823693798071e-06 interleukin 2 receptor subunit beta FUNCTION: Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2.; . . medulla oblongata;ovary;salivary gland;intestine;colon;skin;uterus;prostate;endometrium;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;muscle;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;stomach;thymus; superior cervical ganglion; 0.53477 0.50898 0.444637294 77.91342298 218.42248 3.19492 IL2RG 0.957764471265316 0.0421336347305671 0.000101894004117024 interleukin 2 receptor subunit gamma FUNCTION: Common subunit for the receptors for a variety of interleukins.; DISEASE: Severe combined immunodeficiency X-linked T-cell- negative/B-cell-positive/NK-cell-negative (XSCID) [MIM:300400]: A form of severe combined immunodeficiency (SCID), a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development. {ECO:0000269|PubMed:7557965, ECO:0000269|PubMed:7668284, ECO:0000269|PubMed:7860773, ECO:0000269|PubMed:7937790, ECO:0000269|PubMed:8027558, ECO:0000269|PubMed:8088810, ECO:0000269|PubMed:8299698, ECO:0000269|PubMed:8401490, ECO:0000269|PubMed:8900089, ECO:0000269|PubMed:9049783, ECO:0000269|PubMed:9150740}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: X-linked combined immunodeficiency (XCID) [MIM:312863]: Less severe form of X-linked immunodeficiency with a less severe degree of deficiency in cellular and humoral immunity than that seen in XSCID. {ECO:0000269|PubMed:7883965, ECO:0000269|PubMed:9399950}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . umbilical cord;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;oesophagus;larynx;bone;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;breast;lung;placenta;liver;spleen;head and neck;kidney;aorta;stomach; superior cervical ganglion;whole blood; 0.14057 0.55422 -0.229483771 36.86010852 7.1435 0.26766 IL3 3.72135953228091e-09 0.0271924624487013 0.972807533829939 interleukin 3 FUNCTION: Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages.; . TISSUE SPECIFICITY: Activated T-cells, mast cells, natural killer cells.; unclassifiable (Anatomical System); superior cervical ganglion;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.01943 0.03187 0.525552348 80.57914603 83.42563 1.94206 IL3RA 1.10372786819782e-12 0.0223836254522467 0.97761637454665 interleukin 3 receptor subunit alpha FUNCTION: This is a receptor for interleukin-3.; . . unclassifiable (Anatomical System);medulla oblongata;cartilage;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;pancreas;prostate;optic nerve;whole body;lung;adrenal gland;macula lutea;alveolus;liver;testis;kidney;brain;mammary gland; atrioventricular node;trigeminal ganglion; 0.12674 . -0.086288664 47.11606511 25.93494 0.84256 IL4 0.168021415276942 0.771523104885581 0.0604554798374775 interleukin 4 FUNCTION: Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes.; DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. {ECO:0000269|PubMed:14681304}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);blood; superior cervical ganglion;temporal lobe;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.21843 0.85214 -0.273576253 33.97027601 6.99458 0.26129 IL4I1 0.262058044797637 0.732252115731556 0.00568983947080761 interleukin 4 induced 1 FUNCTION: Lysosomal L-amino-acid oxidase with highest specific activity with phenylalanine. May play a role in lysosomal antigen processing and presentation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is primarily found in immune tissues. {ECO:0000269|PubMed:12031486}.; lymphoreticular;medulla oblongata;sympathetic chain;skin;uterus;prostate;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;muscle;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;duodenum;alveolus;spleen;cervix;kidney;stomach; . 0.05581 0.16635 0.332586472 73.61405992 90.84017 2.05071 IL4R 0.0317438326163225 0.967866354123995 0.000389813259682031 interleukin 4 receptor FUNCTION: Receptor for both interleukin 4 and interleukin 13. Couples to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4/IL13 responses are involved in regulating IgE production and, chemokine and mucus production at sites of allergic inflammation. In certain cell types, can signal through activation of insulin receptor substrates, IRS1/IRS2. {ECO:0000269|PubMed:8124718}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed in activated T-cells.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;oral cavity;muscle;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta;cerebellum; superior cervical ganglion;lung;ciliary ganglion;white blood cells;whole blood;tonsil; 0.18090 0.57142 1.208829905 93.05260675 5155.0539 14.75747 IL5 0.0283744149089649 0.799902432048738 0.171723153042297 interleukin 5 FUNCTION: Factor that induces terminal differentiation of late- developing B-cells to immunoglobulin secreting cells.; . . unclassifiable (Anatomical System); superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12786 0.72066 -0.207437529 38.2814343 10.27318 0.37526 IL5RA 0.000332264657278137 0.947474474327963 0.0521932610147592 interleukin 5 receptor subunit alpha FUNCTION: This is the receptor for interleukin-5. The alpha chain binds to IL5.; . TISSUE SPECIFICITY: Expressed on eosinophils and basophils.; lung;testis;stomach; dorsal root ganglion;superior cervical ganglion;tongue;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;cingulate cortex; 0.26578 0.20782 0.308721233 72.59966973 140.24484 2.58424 IL6 0.289669116993916 0.689311732697402 0.0210191503086818 interleukin 6 FUNCTION: Cytokine with a wide variety of biological functions. It is a potent inducer of the acute phase response. Plays an essential role in the final differentiation of B-cells into Ig- secreting cells Involved in lymphocyte and monocyte differentiation. Acts on B-cells, T-cells, hepatocytes, hematopoietic progenitor cells and cells of the CNS. Required for the generation of T(H)17 cells. Also acts as a myokine. It is discharged into the bloodstream after muscle contraction and acts to increase the breakdown of fats and to improve insulin resistance. It induces myeloma and plasmacytoma growth and induces nerve cells differentiation.; DISEASE: Rheumatoid arthritis systemic juvenile (RASJ) [MIM:604302]: An inflammatory articular disorder with systemic- onset beginning before the age of 16. It represents a subgroup of juvenile arthritis associated with severe extraarticular features and occasionally fatal complications. During active phases of the disorder, patients display a typical daily spiking fever, an evanescent macular rash, lymphadenopathy, hepatosplenomegaly, serositis, myalgia and arthritis. {ECO:0000269|PubMed:9769329}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=A IL6 promoter polymorphism is associated with a lifetime risk of development of Kaposi sarcoma in HIV-infected men. {ECO:0000269|PubMed:11001912}.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;thyroid;bone;amniotic fluid;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;lens;skeletal muscle;lung;placenta;macula lutea;head and neck;kidney;stomach;aorta; superior cervical ganglion;smooth muscle;appendix;ciliary ganglion;fetal lung;pons;trigeminal ganglion; 0.15397 0.99747 0.725794416 85.98136353 133.86335 2.51633 IL6R 0.0478690367242407 0.947123581179278 0.00500738209648096 interleukin 6 receptor FUNCTION: Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation may lead to the regulation of the immune response, acute-phase reactions and hematopoiesis.; . TISSUE SPECIFICITY: Isoform 2 is expressed in peripheral blood mononuclear cells and weakly found in urine and serum.; unclassifiable (Anatomical System);lymphoreticular;heart;colon;blood;skin;skeletal muscle;retina;bone marrow;uterus;prostate;lung;frontal lobe;endometrium;larynx;nasopharynx;bone;liver;testis;head and neck;germinal center;brain;mammary gland;stomach; dorsal root ganglion;liver;ciliary ganglion;atrioventricular node;whole blood;trigeminal ganglion;skeletal muscle;parietal lobe;bone marrow; 0.11957 0.70728 -0.156065314 42.16206653 1450.71381 7.10856 IL6RP1 . . . interleukin 6 receptor pseudogene 1 . . . . . . . . . . . IL6ST 0.997842778499494 0.00215722092922236 5.71283989692817e-10 interleukin 6 signal transducer FUNCTION: Signal-transducing molecule. The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize IL6ST for initiating signal transmission. Binding of IL6 to IL6R induces IL6ST homodimerization and formation of a high-affinity receptor complex, which activates Janus kinases (PubMed:2261637). That causes phosphorylation of IL6ST tyrosine residues which in turn activates STAT3 (PubMed:19915009, PubMed:23294003). Mediates signals which regulate immune response, hematopoiesis, pain control and bone metabolism (By similarity). Has a role in embryonic development (By similarity). Does not bind IL6 (PubMed:2261637). Essential for survival of motor and sensory neurons and for differentiation of astrocytes (By similarity). Required for expression of TRPA1 in nociceptive neurons (By similarity). Required for the maintenance of PTH1R expression in the osteoblast lineage and for the stimulation of PTH-induced osteoblast differentiation (By similarity). Required for normal trabecular bone mass and cortical bone composition (By similarity). {ECO:0000250|UniProtKB:Q00560, ECO:0000269|PubMed:19915009, ECO:0000269|PubMed:2261637, ECO:0000269|PubMed:23294003}.; . TISSUE SPECIFICITY: Found in all the tissues and cell lines examined (PubMed:2261637). Expression not restricted to IL6 responsive cells (PubMed:2261637). Expressed in blood serum (at protein level) (PubMed:24629561). {ECO:0000269|PubMed:2261637, ECO:0000269|PubMed:24629561}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;testis;brain;tonsil;unclassifiable (Anatomical System);heart;lens;skeletal muscle;breast;lung;mesenchyma;nasopharynx;placenta;macula lutea;liver;hypopharynx;spleen;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.67923 0.76430 0.536463361 81.06864827 3018.2823 10.43351 IL6STP1 . . . interleukin 6 signal transducer (gp130, oncostatin M receptor) pseudogene 1 . . . unclassifiable (Anatomical System);skeletal muscle; . . . . . . . IL7 0.879873742046463 0.118691895526669 0.00143436242686804 interleukin 7 FUNCTION: Hematopoietic growth factor capable of stimulating the proliferation of lymphoid progenitors. It is important for proliferation during certain stages of B-cell maturation.; . . colon;skeletal muscle;lung;frontal lobe;larynx;placenta;bone;liver;pituitary gland;testis;head and neck;germinal center;brain;tonsil;stomach; testis;trigeminal ganglion; 0.10724 0.49624 0.21326276 67.71644256 134.94454 2.52665 IL7R 3.72072117299544e-06 0.584033746398945 0.415962532879882 interleukin 7 receptor FUNCTION: Receptor for interleukin-7. Also acts as a receptor for thymic stromal lymphopoietin (TSLP).; DISEASE: Severe combined immunodeficiency autosomal recessive T- cell-negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+) SCID) [MIM:608971]: A form of severe combined immunodeficiency (SCID), a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multiple sclerosis 3 (MS3) [MIM:612595]: A multifactorial, inflammatory, demyelinating disease of the central nervous system. Sclerotic lesions are characterized by perivascular infiltration of monocytes and lymphocytes and appear as indurated areas in pathologic specimens (sclerosis in plaques). The pathological mechanism is regarded as an autoimmune attack of the myelin sheath, mediated by both cellular and humoral immunity. Clinical manifestations include visual loss, extra-ocular movement disorders, paresthesias, loss of sensation, weakness, dysarthria, spasticity, ataxia and bladder dysfunction. Genetic and environmental factors influence susceptibility to the disease. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. A polymorphism at position 244 strongly influences susceptibility to multiple sclerosis. Overtransmission of the major 'C' allele coding for Thr-244 is detected in offspring affected with multiple sclerosis. In vitro analysis of transcripts from minigenes containing either 'C' allele (Thr-244) or 'T' allele (Ile-244) shows that the 'C' allele results in an approximately two-fold increase in the skipping of exon 6, leading to increased production of a soluble form of IL7R. Thus, the multiple sclerosis associated 'C' risk allele of IL7R would probably decrease membrane-bound expression of IL7R. As this risk allele is common in the general population, some additional triggers are probably required for the development and progression of MS.; . unclassifiable (Anatomical System);myocardium;lymph node;lung;nasopharynx;liver;hypopharynx;testis;spleen;blood;head and neck;thymus; . 0.55367 0.57993 0.933309256 89.82661005 173.34205 2.86616 IL9 0.000540879665166309 0.460273760594332 0.539185359740502 interleukin 9 FUNCTION: Supports IL-2 independent and IL-4 independent growth of helper T-cells.; . . unclassifiable (Anatomical System);kidney; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.05546 0.28027 0.147123112 64.11299835 154.84152 2.71917 IL9R 1.92052299627482e-06 0.682292615837246 0.317705463639757 interleukin 9 receptor FUNCTION: This is a receptor for interleukin-9.; . . unclassifiable (Anatomical System);lymphoreticular;placenta;colon;bladder; . 0.11807 0.15071 0.824892996 88.06912008 925.27543 5.90794 IL9RP1 . . . interleukin 9 receptor pseudogene 1 . . . . . . . . . . . IL9RP2 . . . interleukin 9 receptor pseudogene 2 . . . . . . . . . . . IL9RP3 . . . interleukin 9 receptor pseudogene 3 . . . . . . . . . . . IL9RP4 . . . interleukin 9 receptor pseudogene 4 . . . . . . . . . . . IL10 0.0291622262123568 0.923438882183691 0.0473988916039523 interleukin 10 FUNCTION: Inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells.; . TISSUE SPECIFICITY: Produced by a variety of cell lines, including T-cells, macrophages, mast cells and other cell types.; . . 0.47297 0.94462 0.03689118 56.64071715 5.64285 0.21135 IL10RA 0.968345855815418 0.0316440394522945 1.01047322872054e-05 interleukin 10 receptor subunit alpha FUNCTION: Receptor for IL10; binds IL10 with a high affinity.; . TISSUE SPECIFICITY: Spleen, thymus, and PBMC. Weak expression in pancreas, skeletal muscle, brain, heart, and kidney. Placenta, lung, and liver showed intermediate levels. Monocytes, B-cells, large granular lymphocytes, and T-cells express high levels.; lymphoreticular;colon;skin;bone marrow;uterus;optic nerve;whole body;frontal lobe;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;pancreas;lung;nasopharynx;placenta;liver;spleen;mammary gland;aorta; superior cervical ganglion;white blood cells;atrioventricular node;whole blood; 0.19186 0.40674 0.979225112 90.42816702 573.84824 4.86232 IL10RB 0.000334787198614454 0.820138702208122 0.179526510593263 interleukin 10 receptor subunit beta FUNCTION: Shared cell surface receptor required for the activation of five class 2 cytokines: IL10, IL22, IL26, IL28, and IFNL1. The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state. {ECO:0000269|PubMed:12469119, ECO:0000269|PubMed:15123776}.; DISEASE: Inflammatory bowel disease 25 (IBD25) [MIM:612567]: A chronic, relapsing inflammation of the gastrointestinal tract with a complex etiology. It is subdivided into Crohn disease and ulcerative colitis phenotypes. Crohn disease may affect any part of the gastrointestinal tract from the mouth to the anus, but most frequently it involves the terminal ileum and colon. Bowel inflammation is transmural and discontinuous; it may contain granulomas or be associated with intestinal or perianal fistulas. In contrast, in ulcerative colitis, the inflammation is continuous and limited to rectal and colonic mucosal layers; fistulas and granulomas are not observed. Both diseases include extraintestinal inflammation of the skin, eyes, or joints. {ECO:0000269|PubMed:19890111}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;myocardium;smooth muscle;ovary;colon;parathyroid;skin;bone marrow;prostate;bone;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;hypothalamus;adrenal cortex;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; superior cervical ganglion;whole blood; 0.08003 0.21287 0.305084559 72.22811984 2970.71423 10.33886 IL10RB-AS1 . . . IL10RB antisense RNA 1 (head to head) . . . . . . . . . . . IL11 0.427157856363006 0.540023927976171 0.0328182156608231 interleukin 11 FUNCTION: Cytokine that stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells and induces megakaryocyte maturation resulting in increased platelet production (PubMed:2145578). Also promotes the proliferation of hepatocytes in response to liver damage. Binding to its receptor formed by IL6ST and either IL11RA1 or IL11RA2 activates a signaling cascade that promotes cell proliferation (PubMed:12919066). Signaling leads to the activation of intracellular protein kinases and the phosphorylation of STAT3. {ECO:0000250|UniProtKB:P47873, ECO:0000269|PubMed:12919066, ECO:0000269|PubMed:2145578}.; . . unclassifiable (Anatomical System);lung;ovary;islets of Langerhans;placenta;colon;parathyroid;kidney;brain;skin; superior cervical ganglion;temporal lobe;pons;skeletal muscle; 0.12196 . . . 130.3752 2.48670 IL11RA 3.74046234601675e-17 0.00139071799289851 0.998609282007102 interleukin 11 receptor subunit alpha FUNCTION: Receptor for interleukin-11. The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex may be involved in the control of proliferation and/or differentiation of skeletogenic progenitor or other mesenchymal cells. Essential for the normal development of craniofacial bones and teeth. Restricts suture fusion and tooth number. {ECO:0000269|PubMed:21741611}.; . TISSUE SPECIFICITY: Expressed in a number of cell lines, including the myelogenous leukemia cell line K-562, the megakaryocytic leukemia cell line M-07e, the erythroleukemia cell line TF-1, and the osteosarcoma cell lines, MG-63 and SaOS-2. Also expressed in normal and malignant prostate epithelial cell lines. Expression levels are increased in prostate carcinoma. {ECO:0000269|PubMed:11141475}.; medulla oblongata;smooth muscle;ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;optic nerve;frontal lobe;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;lung;placenta;visual apparatus;liver;spleen;mammary gland; . 0.45286 0.08769 -0.003562597 53.72729417 88.49963 2.01667 IL12A 0.299096926040613 0.68138622863991 0.0195168453194772 interleukin 12A FUNCTION: Cytokine that can act as a growth factor for activated T and NK cells, enhance the lytic activity of NK/lymphokine- activated Killer cells, and stimulate the production of IFN-gamma by resting PBMC.; . . unclassifiable (Anatomical System);uterus;lung;heart;endometrium;hippocampus;testis;colon;brain;skin; . 0.07428 0.52467 0.237127192 68.98443029 32.69139 1.01638 IL12A-AS1 . . . IL12A antisense RNA 1 . . . . . . . . . . . IL12B 0.000223245843678324 0.745318642165004 0.254458111991318 interleukin 12B FUNCTION: Cytokine that can act as a growth factor for activated T and NK cells, enhance the lytic activity of NK/lymphokine- activated killer cells, and stimulate the production of IFN-gamma by resting PBMC. {ECO:0000269|PubMed:11114383}.; DISEASE: Immunodeficiency 29 (IMD29) [MIM:614890]: A form of Mendelian susceptibility to mycobacterial disease, a rare condition caused by impairment of interferon-gamma mediated immunity. It is characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. Clinical outcome severity depends on the degree of impairment of interferon-gamma mediated immunity. Some patients die of overwhelming mycobacterial disease with lepromatous-like lesions in early childhood, whereas others develop, later in life, disseminated but curable infections with tuberculoid granulomas. IMD29 is characterized by undetectable IL12B secretion from leukocytes. Affected individuals generally present with BCG disease after vaccination in childhood, and at least half also have Salmonella infection. Disease phenotype is relatively mild, and patients have a good prognosis. {ECO:0000269|PubMed:11753820, ECO:0000269|PubMed:9854038}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Psoriasis 11 (PSORS11) [MIM:612599]: A common, chronic inflammatory disease of the skin with multifactorial etiology. It is characterized by red, scaly plaques usually found on the scalp, elbows and knees. These lesions are caused by abnormal keratinocyte proliferation and infiltration of inflammatory cells into the dermis and epidermis. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System); superior cervical ganglion;trigeminal ganglion; 0.12577 0.76885 0.440999548 77.79547063 150.13365 2.67291 IL12RB1 1.17876777144483e-07 0.985490440584664 0.0145094415385592 interleukin 12 receptor subunit beta 1 FUNCTION: Functions as an interleukin receptor which binds interleukin-12 with low affinity and is involved in IL12 transduction. Associated with IL12RB2 it forms a functional, high affinity receptor for IL12. Associates also with IL23R to form the interleukin-23 receptor which functions in IL23 signal transduction probably through activation of the Jak-Stat signaling cascade. {ECO:0000269|PubMed:12023369}.; DISEASE: Immunodeficiency 30 (IMD30) [MIM:614891]: A form of Mendelian susceptibility to mycobacterial disease, a rare condition caused by impairment of interferon-gamma mediated immunity. It is characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. Clinical outcome severity depends on the degree of impairment of interferon-gamma mediated immunity. Some patients die of overwhelming mycobacterial disease with lepromatous-like lesions in early childhood, whereas others develop, later in life, disseminated but curable infections with tuberculoid granulomas. IMD30 has low penetrance, and affected individuals have relatively mild disease and good prognosis. BCG disease and salmonellosis are the most frequent infections in IMD30 patients. {ECO:0000269|PubMed:11424023}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);colon;skin; superior cervical ganglion;heart;skeletal muscle; 0.09525 0.32934 0.409650696 76.53927813 318.49258 3.78996 IL12RB2 4.50998691872981e-06 0.998044276070487 0.00195121394259452 interleukin 12 receptor subunit beta 2 FUNCTION: Receptor for interleukin-12. This subunit is the signaling component coupling to the JAK2/STAT4 pathway. Promotes the proliferation of T-cells as well as NK cells. Induces the promotion of T-cells towards the Th1 phenotype by strongly enhancing IFN-gamma production.; . TISSUE SPECIFICITY: Isoform 2 is expressed at similar levels in both naive and activated T-cells. {ECO:0000269|PubMed:9120388}.; unclassifiable (Anatomical System);uterus;frontal lobe;skin; trigeminal ganglion;skeletal muscle; 0.20926 0.19195 0.960822749 90.18636471 365.55933 4.04665 IL13 0.0257146912157871 0.785221505721428 0.189063803062784 interleukin 13 FUNCTION: Cytokine. Inhibits inflammatory cytokine production. Synergizes with IL2 in regulating interferon-gamma synthesis. May be critical in regulating inflammatory and immune responses.; DISEASE: Allergic rhinitis (ALRH) [MIM:607154]: A common disease with complex inheritance characterized by mucosal inflammation caused by allergen exposure. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . medulla oblongata;testis; superior cervical ganglion;testis - interstitial;testis;skeletal muscle; 0.24184 0.06921 0.148941568 64.31941496 16.36014 0.58024 IL13RA1 0.97917160586094 0.020810686258736 1.77078803243535e-05 interleukin 13 receptor subunit alpha 1 FUNCTION: Binds with low affinity to interleukin-13 (IL13). Together with IL4RA can form a functional receptor for IL13. Also serves as an alternate accessory protein to the common cytokine receptor gamma chain for interleukin-4 (IL4) signaling, but cannot replace the function of IL2RG in allowing enhanced interleukin-2 (IL2) binding activity.; . TISSUE SPECIFICITY: Ubiquitous. Highest levels in heart, liver, skeletal muscle and ovary; lowest levels in brain, lung and kidney. Also found in B-cells, T-cells and endothelial cells.; . . 0.46698 . -0.405853867 26.23260203 12.99891 0.47344 IL13RA2 7.6423500941326e-05 0.75348936158106 0.246434214917999 interleukin 13 receptor subunit alpha 2 FUNCTION: Binds as a monomer with high affinity to interleukin-13 (IL13), but not to interleukin-4 (IL4). {ECO:0000269|PubMed:20223216}.; . . unclassifiable (Anatomical System);medulla oblongata;ovary;salivary gland;intestine;pharynx;colon;blood;uterus;prostate;lung;endometrium;visual apparatus;iris;liver;testis;kidney;brain;bladder; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion; 0.05269 0.23192 0.12689526 63.00424628 11.55945 0.41808 IL15 0.917197526895697 0.0822494359768646 0.000553037127438259 interleukin 15 FUNCTION: Cytokine that stimulates the proliferation of T- lymphocytes. Stimulation by IL-15 requires interaction of IL-15 with components of IL-2R, including IL-2R beta and probably IL-2R gamma but not IL-2R alpha.; . TISSUE SPECIFICITY: Most abundant in placenta and skeletal muscle. It is also detected in the heart, lung, liver and kidney. IL15- S21AA is preferentially expressed in tissues such as testis and thymus.; unclassifiable (Anatomical System);cartilage;heart;ovary;lacrimal gland;adrenal cortex;colon;parathyroid;skin;skeletal muscle;uterus;pancreas;lung;adrenal gland;thyroid;placenta;testis;head and neck;spleen;kidney;brain;pineal gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.15704 0.59536 0.125076652 62.7388535 6.51506 0.24129 IL15RA 3.17110849041528e-08 0.049425460355515 0.9505745079334 interleukin 15 receptor subunit alpha FUNCTION: High-affinity receptor for interleukin-15. Can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells. Expression of different isoforms may alter or interfere with signal transduction. Isoform 5, isoform 6, isoform 7 and isoform 8 do not bind IL15. Signal transduction involves SYK. {ECO:0000269|PubMed:11714793, ECO:0000269|PubMed:8530383}.; . TISSUE SPECIFICITY: Isoform 1, isoform 3, isoform 4, isoform 5, isoform 6, isoform 7, isoform 8 and isoform 9 are widely expressed. Expressed in fetal brain with higher expression in the hippocampus and cerebellum than in cortex and thalamus. Higher levels of soluble sIL-15RA form in comparison with membrane-bound forms is present in all brain structures. {ECO:0000269|PubMed:10480910, ECO:0000269|PubMed:12114302, ECO:0000269|PubMed:8530383}.; . . 0.03677 0.12440 0.350995466 74.37485256 50.50641 1.39832 IL16 3.12223515361747e-05 0.999846962642696 0.000121815005767794 interleukin 16 FUNCTION: Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4.; FUNCTION: Isoform 3 is involved in cell cycle progression in T- cells. Appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells.; . TISSUE SPECIFICITY: Isoform 3 is expressed in hemopoietic tissues, such as resting T-cells, but is undetectable during active T-cell proliferation.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;spinal ganglion;bladder;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.10793 0.19169 -0.073557068 47.80018872 2443.28418 9.19334 IL17A 0.16720839132903 0.771850640612369 0.0609409680586014 interleukin 17A FUNCTION: Induces stromal cells to produce proinflammatory and hematopoietic cytokines. Enhances the surface expression of ICAM1/intracellular adhesion molecule 1 in fibroblasts.; . TISSUE SPECIFICITY: Restricted to activated memory T-cells.; unclassifiable (Anatomical System); dorsal root ganglion;uterus corpus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.14130 0.74044 -0.185391282 39.67916962 13.87501 0.50401 IL17B 0.00207428402959818 0.507429074305109 0.490496641665293 interleukin 17B FUNCTION: Stimulates the release of tumor necrosis factor alpha and IL-1-beta from the monocytic cell line THP-1.; . TISSUE SPECIFICITY: Expressed in adult pancreas, small intestine, stomach, spinal cord and testis. Less pronounced expression in prostate, colon mucosal lining, and ovary.; unclassifiable (Anatomical System);heart;choroid;fovea centralis;lens;retina;prostate;optic nerve;whole body;placenta;bone;macula lutea;liver;spleen; dorsal root ganglion;superior cervical ganglion;olfactory bulb;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09494 0.15654 -0.516085732 21.20193442 11.05294 0.40027 IL17C 0.000566477094969951 0.469604751839374 0.529828771065656 interleukin 17C FUNCTION: Cytokine that plays a crucial role in innate immunity of the epithelium, including to intestinal bacterial pathogens, in an autocrine manner. Stimulates the production of antibacterial peptides and proinflammatory molecules for host defense by signaling through the NF-kappa-B and MAPK pathways. Acts synergically with IL22 in inducing the expression of antibacterial peptides, including S100A8, S100A9, REG3A and REG3G. Synergy is also observed with TNF and IL1B in inducing DEFB2 from keratinocytes. Depending on the type of insult, may have both protective and pathogenic properties, either by maintaining epithelial homeostasis after an inflammatory challenge or by promoting inflammatory phenotype. Enhanced IL17C/IL17RE signaling may also lead to greater susceptibility to autoimmune diseases. {ECO:0000269|PubMed:21993848}.; . . lung; . 0.09681 . -0.334253673 30.70299599 42.02155 1.22385 IL17D 0.158810135100355 0.63758461102741 0.203605253872235 interleukin 17D FUNCTION: Induces expression of IL-6, IL-8, and GM-CSF from endothelial cells. {ECO:0000269|PubMed:12097364}.; . TISSUE SPECIFICITY: Expressed preferentially in adipose, skeletal muscle and CNS. {ECO:0000269|PubMed:12097364}.; unclassifiable (Anatomical System);medulla oblongata;heart;ovary;cerebellum cortex;islets of Langerhans;parathyroid;fovea centralis;skin;skeletal muscle;uterus;pancreas;prostate;whole body;lung;bone;placenta;thyroid;macula lutea;hippocampus;iris;testis;brain;aorta;cerebellum; amygdala;whole brain;superior cervical ganglion;hypothalamus;spinal cord;prefrontal cortex;globus pallidus;caudate nucleus;pons;cingulate cortex;parietal lobe;cerebellum; 0.11476 . 0.215080721 67.91696155 64.5038 1.64771 IL17F 0.0302739252616752 0.808925354778343 0.160800719959981 interleukin 17F FUNCTION: Stimulates the production of other cytokines such as IL- 6, IL-8 and granulocyte colony-stimulating factor, and can regulate cartilage matrix turnover. Stimulates PBMC and T-cell proliferation. Inhibits angiogenesis.; . TISSUE SPECIFICITY: Expressed in activated, but not resting, CD4+ T-cells and activated monocytes.; . . 0.07673 0.38440 0.305084559 72.22811984 537.66765 4.72703 IL17RA 0.119417929909631 0.880353867474885 0.000228202615484523 interleukin 17 receptor A FUNCTION: Receptor for IL17A, IL17F and, in dimer with IL17RE, for IL17C. Binds its IL17A ligand with low affinity, suggesting that additional components are involved in IL17A-induced signaling. {ECO:0000269|PubMed:19838198, ECO:0000269|PubMed:21993848}.; DISEASE: Candidiasis, familial, 5 (CANDF5) [MIM:613953]: A primary immunodeficiency disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans. {ECO:0000269|PubMed:21350122}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:21993848}.; unclassifiable (Anatomical System);colon;blood;skin;bone marrow;uterus;lung;synovium;adrenal gland;placenta;bone;visual apparatus;germinal center;kidney;tonsil;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;whole blood;bone marrow; 0.11771 0.20326 0.249861693 69.66265629 3302.1655 10.96810 IL17RB 3.50844752193209e-08 0.537925942161421 0.462074022754104 interleukin 17 receptor B FUNCTION: Receptor for the proinflammatory cytokines IL17B and IL17E. May play a role in controlling the growth and/or differentiation of hematopoietic cells. {ECO:0000269|PubMed:11058597}.; . TISSUE SPECIFICITY: Expressed in several endocrine tissues, mostly in fetal and adult liver, kidney, pancreas, testis, colon, brain and small intestine; not detected in peripheral blood leukocytes, lymphoid organs, and most cell lines.; smooth muscle;ovary;colon;parathyroid;skin;larynx;germinal center;spinal ganglion;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland; superior cervical ganglion;kidney; 0.11959 0.09113 1.023320772 91.04741684 1287.96846 6.75900 IL17RC 4.25361992744768e-10 0.931770131235803 0.068229868338835 interleukin 17 receptor C . DISEASE: Candidiasis, familial, 9 (CANDF9) [MIM:616445]: A disorder characterized by altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans. {ECO:0000269|PubMed:25918342}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, cartilage, colon, heart, intestine, kidney, liver, lung, muscle, placenta, and prostate. Low expression in thymus and leukocytes. Expressed (at protein level) in prostate and prostate cancer, skeletal muscle, kidney and placenta. {ECO:0000269|PubMed:11706037}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;parathyroid;choroid;skin;retina;uterus;prostate;lung;endometrium;synovium;larynx;bone;placenta;liver;testis;cervix;spleen;kidney;brain;stomach; superior cervical ganglion;liver;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.20317 . 2.094522466 97.86506251 1224.86104 6.61507 IL17RD 2.6354985095282e-05 0.982023020329808 0.0179506246850965 interleukin 17 receptor D FUNCTION: Feedback inhibitor of fibroblast growth factor mediated Ras-MAPK signaling and ERK activation. May inhibit FGF-induced FGFR1 tyrosine phosphorylation. Regulates the nuclear ERK signaling pathway by spatially blocking nuclear translocation of activated ERK without inhibiting cytoplasmic phosphorylation of ERK. Mediates JNK activation and may be involved in apoptosis. Might have a role in the early stages of fate specification of GnRH-secreting neurons (By similarity). {ECO:0000250, ECO:0000269|PubMed:12807873, ECO:0000269|PubMed:12958313, ECO:0000269|PubMed:15239952}.; . TISSUE SPECIFICITY: Expressed in umbilical vein endothelial cells and in several highly vascularized tissues such as kidney, colon, skeletal muscle, heart and small intestine. Highly expressed in ductal epithelial cells of salivary glands, seminal vesicles and the collecting tubules of the kidney. Isoform 1 is also highly expressed in both fetal and adult brain, pituitary, tonsils, spleen, adenoids, fetal kidney, liver, testes and ovary. Isoform 1 is also expressed at moderate levels in primary aortic endothelial cells and adrenal medulla, and at low levels in adrenal cortex. Isoform 4 is specifically and highly expressed in pituitary, fetal brain and umbilical vein endothelial cells. {ECO:0000269|PubMed:12807873}.; unclassifiable (Anatomical System);uterus;lung;heart;endometrium;testis;colon;kidney;brain;skin; dorsal root ganglion;superior cervical ganglion; 0.67490 0.12392 -0.172654315 40.63458363 2297.79347 8.87861 IL17RE 0.00861987839064516 0.990837286527723 0.000542835081631482 interleukin 17 receptor E FUNCTION: Specific functional receptor for IL17C. May be signaling through the NF-kappa-B and MAPK pathways. May require TRAF3IP2 /ACT1 for signaling. May be a crucial regulator in innate immunity to bacterial pathogens. Isoform 2 and isoform 4 may be either cytoplasmic inactive or dominant active forms. Isoform 3 and isoform 5 may act as soluble decoy receptors. {ECO:0000269|PubMed:21993848, ECO:0000269|PubMed:21993849}.; . TISSUE SPECIFICITY: Predominantly expressed in mucosal tissues with high levels in keratinocytes and colon epithelial cells. Very low expression in dermal fibroblasts. Expressed in various tumor cell lines. {ECO:0000269|PubMed:16310341, ECO:0000269|PubMed:21993848}.; unclassifiable (Anatomical System);heart;islets of Langerhans;colon;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;endometrium;placenta;macula lutea;testis;germinal center;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.10525 0.08638 2.066988646 97.80018872 289.62229 3.64005 IL17REL 0.327459012314709 0.66922240190996 0.00331858577533098 interleukin 17 receptor E-like . . . . . 0.48793 . 0.597144447 82.7435716 407.54891 4.23327 IL18 0.102774109232244 0.773867773072807 0.123358117694949 interleukin 18 FUNCTION: Augments natural killer cell activity in spleen cells and stimulates interferon gamma production in T-helper type I cells.; . . unclassifiable (Anatomical System);uterus;pancreas;optic nerve;lung;bone;liver;hypopharynx;head and neck;skin;skeletal muscle;stomach; superior cervical ganglion;temporal lobe;pons; 0.04056 0.55024 -0.009020804 52.8544468 1.83265 0.05745 IL18BP 3.32665579767765e-06 0.193255020320402 0.8067416530238 interleukin 18 binding protein FUNCTION: Isoform A binds to IL-18 and inhibits its activity. Functions as an inhibitor of the early TH1 cytokine response. {ECO:0000269|PubMed:10023777, ECO:0000269|PubMed:10655506}.; . TISSUE SPECIFICITY: Strongly expressed in heart, lung, placenta and spleen. {ECO:0000269|PubMed:10023777, ECO:0000269|PubMed:10094485}.; medulla oblongata;ovary;sympathetic chain;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;endometrium;larynx;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pineal body;muscle;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;tongue;appendix;skeletal muscle; 0.04076 0.07315 0.260991686 70.25831564 91.26045 2.05463 IL18R1 5.02097661201518e-07 0.632761132371185 0.367238365531154 interleukin 18 receptor 1 FUNCTION: Receptor for interleukin 18 (IL-18). Binding to the agonist leads to the activation of NF-kappa-B.; . TISSUE SPECIFICITY: Expressed in lung, leukocytes, spleen, liver, thymus, prostate, small intestine, colon, placenta, and heart, and is absent from brain, skeletal muscle, pancreas, and kidney. High level of expression in Hodgkin disease cell lines.; breast;uterus;lung;cartilage;ovary;heart;liver;colon;germinal center;skin;stomach;bone marrow; superior cervical ganglion; 0.10925 0.18628 0.286674996 71.49681529 72.87885 1.78217 IL18RAP 0.366507424726522 0.63339149311208 0.000101082161398204 interleukin 18 receptor accessory protein FUNCTION: Required for the high affinity binding of interleukin 18 (IL-18) to its receptor complex (By similarity). Together with IL18R1 mediates IL-18-dependent activation of NF-kappa-B and JNK. {ECO:0000250, ECO:0000269|PubMed:9792649}.; . TISSUE SPECIFICITY: Strongly expressed in peripheral blood leukocytes, spleen, lung, and, to a lesser extent, in colon, but not in any other tissue tested. Strongly expressed in T-cells polarized with IL-12. Specifically coexpressed with IL18R1 in Th1 cells. {ECO:0000269|PubMed:10925275, ECO:0000269|PubMed:11046021, ECO:0000269|PubMed:9792649}.; pancreas;liver;blood;kidney;brain;aorta; superior cervical ganglion;trigeminal ganglion;whole blood; 0.08779 0.17770 0.020302773 55.60863411 24.74148 0.81193 IL19 0.0203202325026012 0.904064812009938 0.0756149554874609 interleukin 19 FUNCTION: May play some important roles in inflammatory responses. Up-regulates IL-6 and TNF-alpha and induces apoptosis (By similarity). {ECO:0000250}.; . . uterus;lung;heart;skin; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.03111 0.14567 0.503505267 79.88912479 31.06448 0.98116 IL20 0.00253917759019062 0.783546149872194 0.213914672537615 interleukin 20 FUNCTION: Proinflammatory and angiogenic cytokine that may be involved in epidermal function and psoriasis. Angiogenic and proliferative activities are antagonized by IL10. May act through STAT3. {ECO:0000269|PubMed:16511554}.; . TISSUE SPECIFICITY: Expressed in most tissues and five major cell types: epithelial cells (primarily skin, buccal mucosa, tongue, nasal mucosa, lung, ureter, breast, prostate, fallopian tube, and adrenal gland), myoepithelial cells (mainly prostate), endothelial cells (mainly in small vessels or capillaries), macrophages, and skeletal muscle. Isoform 2 was detected in the lung tissue only. {ECO:0000269|PubMed:16908179}.; . . 0.15890 0.17874 0.104848986 61.49445624 32.68553 1.01582 IL20RA 0.00757531716048163 0.977001983699394 0.015422699140124 interleukin 20 receptor subunit alpha FUNCTION: The IL20RA/IL20RB dimer is a receptor for IL19, IL20 and IL24. The IL20RA/IL10RB dimer is a receptor for IL26.; . TISSUE SPECIFICITY: Widely expressed with highest levels in skin and testis and high levels in brain. Highly expressed in psoriatic skin. {ECO:0000269|PubMed:11163236, ECO:0000269|PubMed:14764663}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;lung;placenta;macula lutea;liver;head and neck;kidney; ciliary ganglion;atrioventricular node; 0.13796 0.11768 0.376678994 75.50719509 564.20193 4.82236 IL20RB 0.000354183473406977 0.829449278191053 0.17019653833554 interleukin 20 receptor subunit beta FUNCTION: The IL20RA/IL20RB dimer is a receptor for IL19, IL20 and IL24. The IL22RA1/IL20RB dimer is a receptor for IL20 and IL24.; . TISSUE SPECIFICITY: Widely expressed with highest levels in skin and testis. Highly expressed in psoriatic skin. {ECO:0000269|PubMed:11163236}.; unclassifiable (Anatomical System);smooth muscle;heart;skin;uterus;lung;larynx;gum;hypopharynx;testis;head and neck;cervix;kidney; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18571 0.12856 0.21689899 68.12927577 14.55613 0.52451 IL20RB-AS1 . . . IL20RB antisense RNA 1 . . . . . . . . . . . IL21 0.502190579590147 0.478440052013515 0.0193693683963374 interleukin 21 FUNCTION: Cytokine with immunoregulatory activity. May promote the transition between innate and adaptive immunity. Induces the production of IgG(1) and IgG(3) in B-cells (By similarity). May play a role in proliferation and maturation of natural killer (NK) cells in synergy with IL15. May regulate proliferation of mature B- and T-cells in response to activating stimuli. In synergy with IL15 and IL18 stimulates interferon gamma production in T-cells and NK cells. During T-cell mediated immune response may inhibit dendritic cells (DC) activation and maturation. {ECO:0000250, ECO:0000269|PubMed:11081504, ECO:0000269|PubMed:15178704}.; . TISSUE SPECIFICITY: Expressed in activated CD4-positive T-cells but not in CD8-positive T-cells, B-cells, or monocytes. {ECO:0000269|PubMed:11081504}.; unclassifiable (Anatomical System); superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.06207 0.15823 -0.09720619 46.20193442 2.45548 0.08997 IL21-AS1 . . . IL21 antisense RNA 1 . . . . . . . . . . . IL21R 0.846367843553844 0.153515954751929 0.000116201694226407 interleukin 21 receptor FUNCTION: This is a receptor for interleukin-21.; DISEASE: IL21R immunodeficiency (IL21RID) [MIM:615207]: An autosomal recessive primary immunodeficiency characterized by B- and T-cell defects and variable dysfunction of NK cells. Patients tend to have normal numbers of lymphocytes, but show defective class-switched B-cells, low IgG, defective antibody response, and defective T-cell responses to certain antigens. {ECO:0000269|PubMed:23440042}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Chromosomal aberrations involving IL21R is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;16)(q27;p11), with BCL6.; TISSUE SPECIFICITY: Selectively expressed in lymphoid tissues. Most highly expressed in thymus and spleen.; unclassifiable (Anatomical System);lymph node;lung;cartilage;testis;kidney;germinal center;brain;tonsil;aorta; superior cervical ganglion;trigeminal ganglion; 0.08969 0.21075 0.643056625 84.05284265 343.55035 3.92928 IL21R-AS1 . . . IL21R antisense RNA 1 . . . . . . . . . . . IL22 0.490718395700443 0.488244542170006 0.0210370621295509 interleukin 22 FUNCTION: Cytokine that contributes to the inflammatory response in vivo.; . . unclassifiable (Anatomical System);blood; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.08448 0.17914 0.369407109 74.95281906 46.53388 1.31727 IL22RA1 0.0644008505714252 0.932450632043171 0.00314851738540349 interleukin 22 receptor subunit alpha 1 FUNCTION: Component of the receptor for IL20, IL22 and IL24. Component of IL22 receptor formed by IL22RA1 and IL10RB enabling IL22 signaling via JAK/STAT pathways. IL22 also induces activation of MAPK1/MAPK3 and Akt kinases pathways. Component of one of the receptor for IL20 and IL24 formed by IL22RA1 and IL20RB also signaling through STATs activation. Mediates IL24 antiangiogenic activity as well as IL24 inhibitory effect on endothelial cell tube formation and differentiation. {ECO:0000269|PubMed:11035029, ECO:0000269|PubMed:11564763, ECO:0000269|PubMed:11706020, ECO:0000269|PubMed:12351624, ECO:0000269|PubMed:12941841, ECO:0000269|PubMed:17204547}.; . TISSUE SPECIFICITY: Expressed in colon, liver, lung, pancreas and kidney. No expression in immune cells such as monocytes, T-cells, and NK-cells. Expressed in keratinocytes of normal skin as well as in psoriatic skin lesion. Detected in normal blood brain barrier endothelial cells as well as in multiple sclerosis lesions; Strongly expressed on central nervous system vessels within infiltrated multiple sclerosis lesions. Overexpressed in synovial fluid cells from rheumatoid arthritis and spondyloarthropathy patients. {ECO:0000269|PubMed:12407026, ECO:0000269|PubMed:15308104, ECO:0000269|PubMed:17828272, ECO:0000269|PubMed:17900301, ECO:0000269|PubMed:18061474}.; unclassifiable (Anatomical System);pancreas;optic nerve;islets of Langerhans;larynx;liver;colon;spleen;bladder;skin;stomach; dorsal root ganglion;superior cervical ganglion;pancreas;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08485 0.16647 0.714657953 85.81623024 5253.66497 14.94750 IL22RA2 1.20924934270126e-09 0.0515132522134185 0.948486746577332 interleukin 22 receptor subunit alpha 2 FUNCTION: Isoform 2 is a receptor for IL22. Binds to IL22, prevents interaction with the functional IL-22R complex and blocks the activity of IL22 (in vitro). May play an important role as an IL22 antagonist in the regulation of inflammatory responses.; . TISSUE SPECIFICITY: Expressed in placenta, spleen, breast, skin and lung. Also detected in intestinal tract, testis, brain, heart and thymus. No expression found in prostate, bladder, kidney, ovary, muscle, bone marrow, liver and uterus. Isoform 1 is expressed only in placenta. Isoform 2 is expressed in placenta and breast and at lower level in spleen, skin, thymus and stomach. {ECO:0000269|PubMed:11481447, ECO:0000269|PubMed:11607789, ECO:0000269|PubMed:15201862}.; unclassifiable (Anatomical System);lung;testis; globus pallidus;ciliary ganglion;atrioventricular node; 0.04699 0.08149 -0.247889024 35.98726115 197.91924 3.04105 IL23A 0.842438306418319 0.154652742782329 0.00290895079935122 interleukin 23 subunit alpha FUNCTION: Associates with IL12B to form the IL-23 interleukin, a heterodimeric cytokine which functions in innate and adaptive immunity. IL-23 may constitute with IL-17 an acute response to infection in peripheral tissues. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R, activates the Jak- Stat signaling cascade, stimulates memory rather than naive T- cells and promotes production of proinflammatory cytokines. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis. {ECO:0000269|PubMed:11114383, ECO:0000269|PubMed:12023369, ECO:0000269|PubMed:16424222}.; . TISSUE SPECIFICITY: Secreted by activated dendritic and phagocytic cells and keratinocytes. Also expressed by dermal Langerhans cells (at protein level). {ECO:0000269|PubMed:11114383, ECO:0000269|PubMed:16424222}.; unclassifiable (Anatomical System);uterus;lymph node;lung;heart;islets of Langerhans;testis;blood;skin; . 0.38445 0.58278 -0.075159878 47.78839349 7.31511 0.27334 IL23R 0.00649529618715747 0.989490456075338 0.00401424773750431 interleukin 23 receptor FUNCTION: Associates with IL12RB1 to form the interleukin-23 receptor. Binds IL23 and mediates T-cells, NK cells and possibly certain macrophage/myeloid cells stimulation probably through activation of the Jak-Stat signaling cascade. IL23 functions in innate and adaptive immunity and may participate in acute response to infection in peripheral tissues. IL23 may be responsible for autoimmune inflammatory diseases and be important for tumorigenesis. {ECO:0000269|PubMed:12023369}.; DISEASE: Inflammatory bowel disease 17 (IBD17) [MIM:612261]: A chronic, relapsing inflammation of the gastrointestinal tract with a complex etiology. It is subdivided into Crohn disease and ulcerative colitis phenotypes. Crohn disease may affect any part of the gastrointestinal tract from the mouth to the anus, but most frequently it involves the terminal ileum and colon. Bowel inflammation is transmural and discontinuous; it may contain granulomas or be associated with intestinal or perianal fistulas. In contrast, in ulcerative colitis, the inflammation is continuous and limited to rectal and colonic mucosal layers; fistulas and granulomas are not observed. Both diseases include extraintestinal inflammation of the skin, eyes, or joints. {ECO:0000269|PubMed:17068223, ECO:0000269|PubMed:17804789}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed by monocytes, Th1, Th0, NK and dendritic cells. Isoform 1 is specifically expressed in NK cells. {ECO:0000269|PubMed:12023369, ECO:0000269|PubMed:16372191}.; . . 0.11254 0.33107 0.795569043 87.49115357 277.44165 3.56826 IL24 0.00271588782691559 0.795667242360985 0.201616869812099 interleukin 24 FUNCTION: Has antiproliferative properties on melanoma cells and may contribute to terminal cell differentiation.; . TISSUE SPECIFICITY: Up-regulated in melanoma cells induced to terminally differentiate.; unclassifiable (Anatomical System);lymph node;cartilage;colon;blood;bile duct;uterus;pancreas;prostate;lung;bone;placenta;germinal center;mammary gland;aorta;stomach;gall bladder; superior cervical ganglion;smooth muscle; 0.07542 0.22284 0.881944684 89.02453409 2267.8798 8.80547 IL25 3.62722298351536e-06 0.109883689608224 0.890112683168793 interleukin 25 FUNCTION: Induces activation of NF-kappa-B and stimulates production of the proinflammatory chemokine IL-8. Proinflammatory cytokine favoring Th2-type immune responses.; . TISSUE SPECIFICITY: Expressed at low levels in several tissues, including brain, kidney, lung, prostate, testis, spinal cord, adrenal gland, and trachea.; . . 0.12310 0.11938 -0.161524709 41.6430762 30.97695 0.97949 IL26 0.0527617615393175 0.862554542288827 0.084683696171855 interleukin 26 FUNCTION: May play a role in local mechanisms of mucosal immunity and seems to have a proinflammatory function. May play a role in inflammatory bowel disease. Activates STAT1 and STAT3, MAPK1/3 (ERK1/2), JUN and AKT. Induces expression of SOCS3, TNF-alpha and IL-8, secretion of IL-8 and IL-10 and surface expression of ICAM1. Decreases proliferation of intestinal epithelial cells. Is inhibited by heparin. {ECO:0000269|PubMed:14764663, ECO:0000269|PubMed:15178681, ECO:0000269|PubMed:18483078}.; . TISSUE SPECIFICITY: Expressed in HVS transformed T-cells but not other T-cell lines or primary stimulated T-cells. Expressed in colonic T-cells including Th17 inflammatory T-cells; the expression is significantly increased in serum of patients with Crohn's disease (at protein level). {ECO:0000269|PubMed:18483078}.; bone; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;tongue;trigeminal ganglion;skeletal muscle; 0.41535 0.16941 -0.185391282 39.67916962 15.12661 0.54409 IL27 0.927792677629213 0.0718163921931892 0.000390930177598388 interleukin 27 FUNCTION: Associates with EBI3 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. IL-27 has pro- and anti-inflammatory properties, that can regulate T- helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells, and that has diverse effects on innate immune cells. Among its target cells are CD4 T-helper cells which can differentiate in type 1 effector cells (TH1), type 2 effector cells (TH2) and IL17 producing helper T-cells (TH17). It drives rapid clonal expansion of naive but not memory CD4 T-cells. It also strongly synergizes with IL-12 to trigger interferon-gamma/IFN-gamma production of naive CD4 T-cells, binds to the cytokine receptor WSX-1/TCCR which appears to be required but not sufficient for IL-27-mediated signal transduction. IL-27 potentiate the early phase of TH1 response and suppress TH2 and TH17 differentiation. It induces the differentiation of TH1 cells via two distinct pathways, p38 MAPK/TBX21- and ICAM1/ITGAL/ERK-dependent pathways. It also induces STAT1, STAT3, STAT4 and STAT5 phosphorylation and activates TBX21/T-Bet via STAT1 with resulting IL12RB2 up- regulation, an event crucial to TH1 cell commitment. It suppresses the expression of GATA3, the inhibitor TH1 cells development. In CD8 T-cells, it activates STATs as well as GZMB. IL-27 reveals to be a potent inhibitor of TH17 cell development and of IL-17 production. Indeed IL27 alone is also able to inhibit the production of IL17 by CD4 and CD8 T-cells. While IL-27 suppressed the development of proinflammatory Th17 cells via STAT1, it inhibits the development of anti-inflammatory inducible regulatory T-cells, iTreg, independently of STAT1. IL-27 has also an effect on cytokine production, it suppresses proinflammatory cytokine production such as IL2, IL4, IL5 and IL6 and activates suppressors of cytokine signaling such as SOCS1 and SOCS3. Apart from suppression of cytokine production, IL-27 also antagonizes the effects of some cytokines such as IL6 through direct effects on T- cells. Another important role of IL-27 is its antitumor activity as well as its antiangiogenic activity with activation of production of antiangiogenic chemokines such as IP-10/CXCL10 and MIG/CXCL9. In vein endothelial cells, it induces IRF1/interferon regulatory factor 1 and increase the expression of MHC class II transactivator/CIITA with resulting up-regulation of major histocompatibility complex class II. IL-27 also demonstrates antiviral activity with inhibitory properties on HIV-1 replication. {ECO:0000269|PubMed:12121660, ECO:0000269|PubMed:14565860, ECO:0000269|PubMed:17068156, ECO:0000269|PubMed:18191724}.; . TISSUE SPECIFICITY: Expressed in monocytes and in placenta. {ECO:0000269|PubMed:12121660}.; lung; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.08462 . 0.215080721 67.91696155 1519.62628 7.24534 IL27RA 8.96991107032681e-07 0.980982372691539 0.0190167303173545 interleukin 27 receptor subunit alpha FUNCTION: Receptor for IL27. Requires IL6ST/gp130 to mediate signal transduction in response to IL27. This signaling system acts through STAT3 and STAT1. Involved in the regulation of Th1- type immune responses. Also appears to be involved in innate defense mechanisms. {ECO:0000269|PubMed:14764690}.; . TISSUE SPECIFICITY: Highly expressed in lymphoid tissues such as spleen, lymph nodes and peripheral blood leukocytes. Weakly expressed in other tissues examined including heart, brain, fetal and adult lung, liver, skeletal muscle, kidney, pancreas, prostate, testis, ovary, small intestine, kidney and colon. In the lymphoid system, higher level expression in CD4+ T-cell subsets than in CD8+ T-cell subsets. Also weaker expression in CD19+ B- cells and monocytes. {ECO:0000269|PubMed:11057672, ECO:0000269|PubMed:9600072}.; unclassifiable (Anatomical System);prostate;lymph node;ovary;heart;endometrium;bone;thyroid;placenta;parathyroid;germinal center;brain;tonsil; lymph node;white blood cells;atrioventricular node;whole blood;trigeminal ganglion;skeletal muscle;tonsil;thymus; 0.09264 0.19359 -0.086288664 47.11606511 575.25784 4.86504 IL31 0.150887238101552 0.777273526952143 0.071839234946305 interleukin 31 FUNCTION: Activates STAT3 and possibly STAT1 and STAT5 through the IL31 heterodimeric receptor composed of IL31RA and OSMR. IL31 may function in skin immunity. {ECO:0000269|PubMed:15184896}.; . TISSUE SPECIFICITY: Detected at low levels in testis, bone marrow, skeletal muscle, kidney, colon, thymus, small intestine and trachea. {ECO:0000269|PubMed:15184896}.; . . 0.13128 0.11455 -0.427900189 25.14744043 2.27422 0.07707 IL31RA 2.13041261180957e-15 0.054705574950713 0.945294425049285 interleukin 31 receptor A FUNCTION: Associates with OSMR to form the interleukin-31 receptor which activates STAT3 and to a lower extent STAT1 and STAT5. May function in skin immunity. {ECO:0000269|PubMed:11877449, ECO:0000269|PubMed:14504285, ECO:0000269|PubMed:15184896, ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:15627637}.; DISEASE: Amyloidosis, primary localized cutaneous, 2 (PLCA2) [MIM:613955]: A primary amyloidosis characterized by localized cutaneous amyloid deposition. This condition usually presents with itching (especially on the lower legs) and visible changes of skin hyperpigmentation and thickening that may be exacerbated by chronic scratching and rubbing. Primary localized cutaneous amyloidosis is often divided into macular and lichen subtypes although many affected individuals often show both variants coexisting. Lichen amyloidosis characteristically presents as a pruritic eruption of grouped hyperkeratotic papules with a predilection for the shins, calves, ankles and dorsa of feet and thighs. Papules may coalesce to form hyperkeratotic plaques that can resemble lichen planus, lichen simplex or nodular prurigo. Macular amyloidosis is characterized by small pigmented macules that may merge to produce macular hyperpigmentation, sometimes with a reticulate or rippled pattern. In macular and lichen amyloidosis, amyloid is deposited in the papillary dermis in association with grouped colloid bodies, thought to represent degenerate basal keratinocytes. The amyloid deposits probably reflect a combination of degenerate keratin filaments, serum amyloid P component, and deposition of immunoglobulins. {ECO:0000269|PubMed:19690585}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at low levels in testis, ovary, brain, prostate, placenta, thymus, bone marrow, trachea and skin. Detected in all of the myelomonocytic lineage. Expressed in CD14- and CD56-positive blood cells and by macrophages (at protein level). {ECO:0000269|PubMed:11877449, ECO:0000269|PubMed:14504285, ECO:0000269|PubMed:15184896, ECO:0000269|PubMed:16461143}.; . . 0.05216 0.23851 0.648517637 84.14720453 2284.73957 8.84274 IL32 3.7703925155889e-07 0.198314052550756 0.801685570409993 interleukin 32 FUNCTION: Cytokine that may play a role in innate and adaptive immune responses. It induces various cytokines such as TNFA/TNF- alpha and IL8. It activates typical cytokine signal pathways of NF-kappa-B and p38 MAPK. {ECO:0000269|PubMed:15664165}.; . TISSUE SPECIFICITY: Selectively expressed in lymphocytes. Expression is more prominent in immune cells than in non-immune cells. {ECO:0000269|PubMed:15664165}.; smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;endometrium;oesophagus;synovium;bone;thyroid;lymph;testis;amniotic fluid;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; whole blood; 0.05526 . 1.550689283 95.62396792 103.95589 2.20290 IL33 1.05455841268217e-08 0.0497642285606079 0.950235760893808 interleukin 33 FUNCTION: Cytokine that binds to and signals through the IL1RL1/ST2 receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells (PubMed:16286016). Involved in the maturation of Th2 cells inducing the secretion of T-helper type 2-associated cytokines. Also involved in activation of mast cells, basophils, eosinophils and natural killer cells. Acts as a chemoattractant for Th2 cells, and may function as an "alarmin", that amplifies immune responses during tissue injury (PubMed:17853410, PubMed:18836528). {ECO:0000269|PubMed:16286016, ECO:0000269|PubMed:17853410, ECO:0000269|PubMed:18836528}.; . TISSUE SPECIFICITY: Expressed at high level in high endothelial venules found in tonsils, Peyer patches and mesenteric lymph nodes. Almost undetectable in placenta. {ECO:0000269|PubMed:12819012}.; . . 0.05148 0.10662 0.41713504 76.95800896 167.61501 2.82852 IL34 0.114215553005568 0.858188460200317 0.0275959867941153 interleukin 34 FUNCTION: Cytokine that promotes the proliferation, survival and differentiation of monocytes and macrophages. Promotes the release of proinflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, and in the regulation of bone resorption. Signaling via CSF1R and its downstream effectors stimulates phosphorylation of MAPK1/ERK2 AND MAPK3/ERK1. {ECO:0000269|PubMed:18467591, ECO:0000269|PubMed:20489731, ECO:0000269|PubMed:20504948, ECO:0000269|PubMed:20829061}.; . TISSUE SPECIFICITY: Detected in the sinusoidal epithelium in the red pulp of spleen (at protein level). Predominantly expressed in spleen. Also detected in a range of other tissues including heart, brain, lung, liver, kidney, thymus, testis, ovary, small intestine, prostate and colon. {ECO:0000269|PubMed:18467591}.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;fovea centralis;choroid;lens;retina;pancreas;optic nerve;lung;bone;macula lutea;testis;spleen;kidney;mammary gland;brain; amygdala;whole brain;thalamus;superior cervical ganglion;occipital lobe;cerebellum peduncles;hypothalamus;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.23864 0.07227 0.841481379 88.35810333 232.37986 3.29666 IL36A 0.000123309813533248 0.390211565177031 0.609665125009436 interleukin 36, alpha FUNCTION: Cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP. Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T cells to drive tissue infiltration, cell maturation and cell proliferation. In cultured keratinocytes induces the expression of macrophage, T cell, and neutrophil chemokines, such as CCL3, CCL4, CCL5, CCL2, CCL17, CCL22, CL20, CCL5, CCL2, CCL17, CCL22, CXCL8, CCL20 and CXCL1, and the production of proinflammatory cytokines such as TNF-alpha, IL-8 and IL-6. In cultured monocytes upregulates expression of IL-1A, IL-1B and IL-6. In myeloid dendritic cells involved in cell maturation by upregulating surface expression of CD83, CD86 and HLA-DR. In monocyte-derived dendritic cells facilitates dendritic cell maturation and drives T cell proliferation. May play a role in proinflammatory effects in the lung. {ECO:0000269|PubMed:14734551, ECO:0000269|PubMed:21881584, ECO:0000269|PubMed:21965679, ECO:0000269|PubMed:24829417}.; . TISSUE SPECIFICITY: Expressed in immune system and fetal brain, but not in other tissues tested or in multiple hematopoietic cell lines. Predominantly expressed in skin keratinocytes but not in fibroblasts, endothelial cells or melanocytes. Increased in lesional psoriasis skin. {ECO:0000269|PubMed:11466363}.; . . 0.06775 0.09511 0.747842143 86.47676339 121.6017 2.40095 IL36B 0.00351729714336239 0.838463740144985 0.158018962711653 interleukin 36, beta FUNCTION: Cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP. Stimulates production of interleukin-6 and interleukin-8 in synovial fibrobasts, articular chondrocytes and mature adipocytes. Induces expression of a number of antimicrobial peptides including beta-defensins 4 and 103 as well as a number of matrix metalloproteases. Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T cells to drive tissue infiltration, cell maturation and cell proliferation. In cultured keratinocytes induces the expression of macrophage, T cell, and neutrophil chemokines, such as CCL3, CCL4, CCL5, CCL2, CCL17, CCL22, CL20, CCL5, CCL2, CCL17, CCL22, CXCL8, CCL20 and CXCL1, and the production of proinflammatory cytokines such as TNF-alpha, IL- 8 and IL-6. {ECO:0000269|PubMed:16646978, ECO:0000269|PubMed:20300079, ECO:0000269|PubMed:21242515, ECO:0000269|PubMed:21881584, ECO:0000269|PubMed:21965679, ECO:0000269|PubMed:24829417}.; . TISSUE SPECIFICITY: Expression at low levels in tonsil, bone marrow, heart, placenta, lung, testis and colon but not in any hematopoietic cell lines. Not detected in adipose tissue. Expressed at higher levels in psoriatic plaques than in symptomless psoriatic skin or healthy control skin. Increased levels are not detected in inflamed joint tissue. {ECO:0000269|PubMed:20300079, ECO:0000269|PubMed:21242515}.; unclassifiable (Anatomical System);brain; whole brain;dorsal root ganglion;superior cervical ganglion;occipital lobe;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05043 0.07939 0.393270925 76.04977589 114.00906 2.32709 IL36G 2.50412730985725e-05 0.309258481849081 0.69071647687782 interleukin 36, gamma FUNCTION: Cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP. Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T cells to drive tissue infiltration, cell maturation and cell proliferation. In cultured keratinocytes induces the expression of macrophage, T cell, and neutrophil chemokines, such as CCL3, CCL4, CCL5, CCL2, CCL17, CCL22, CL20, CCL5, CCL2, CCL17, CCL22, CXCL8, CCL20 and CXCL1; also stimulates its own expression and that of the prototypic cutaneous proinflammatory parameters TNF-alpha, S100A7/psoriasin and inducible NOS. May play a role in proinflammatory responses during particular neutrophilic airway inflammation: activates mitogen-activated protein kinases and NF-kappa B in primary lung fibroblasts, and stimulates the expression of IL-8 and CXCL3 and Th17 chemokine CCL20 in lung fibroblasts. May be involved in the innate immune response to fungal pathogens, such as Aspergillus fumigatus. {ECO:0000269|PubMed:11466363, ECO:0000269|PubMed:20870894, ECO:0000269|PubMed:21965679, ECO:0000269|PubMed:23095752, ECO:0000269|PubMed:23147407, ECO:0000269|PubMed:24829417}.; . TISSUE SPECIFICITY: Highly expressed in tissues containing epithelial cells: skin, lung, stomach and esophagus. Expressed in bronchial epithelial. In skin is expressed only in keratinocytes but not in fibroblasts, endothelial cells or melanocytes. Up- regulated in lesional psoriasis skin. Expressed in monocyte- derived dendritic cells and M1 macrophages. {ECO:0000269|PubMed:20870894, ECO:0000269|PubMed:23095752}.; unclassifiable (Anatomical System);lung;tongue;larynx;colon;head and neck; superior cervical ganglion;trigeminal ganglion; 0.04714 0.08399 0.3032669 72.009908 78.70088 1.87247 IL36RN 0.000972339640244069 0.58407451915708 0.414953141202676 interleukin 36 receptor antagonist FUNCTION: Inhibits the activity of interleukin-36 (IL36A,IL36B and IL36G) by binding to receptor IL1RL2 and preventing its association with the coreceptor IL1RAP for signaling. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor. Proposed to play a role in skin inflammation. May be involved in the innate immune response to fungal pathogens, such as Aspergillus fumigatus. May activate an anti-inflammatory signaling pathway by recruiting SIGIRR. {ECO:0000269|PubMed:11466363, ECO:0000269|PubMed:21965679, ECO:0000269|PubMed:23147407}.; DISEASE: Psoriasis 14, pustular (PSORS14) [MIM:614204]: A life- threatening disease defined by repeated flares of sudden onset consisting of diffuse erythematous skin eruption characterized by rapid coverage with pustules, high-grade fever, asthenia, marked leukocytosis, and elevated serum levels of C-reactive protein. {ECO:0000269|PubMed:21839423, ECO:0000269|PubMed:21848462, ECO:0000269|PubMed:22903787}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in skin keratinocytes but not in fibroblasts, endothelial cells or melanocytes. Detected also in the spleen, brain leukocyte and macrophage cell types. Increased in lesional psoriasis skin. {ECO:0000269|PubMed:11466363}.; unclassifiable (Anatomical System);lung;ovary;placenta;hypopharynx;parathyroid;head and neck; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.15223 0.12775 0.038710339 56.92380278 158.88685 2.75336 IL37 0.00783605765988603 0.782934741625233 0.209229200714881 interleukin 37 FUNCTION: Suppressor of innate inflammatory and immune responses involved in curbing excessive inflammation. This function requires SMAD3. Suppresses, or reduces, proinflammatory cytokine production, including IL1A and IL6, as well as CCL12, CSF1, CSF2, CXCL13, IL1B, IL23A and IL1RN, but spares anti-inflammatory cytokines. Inhibits dendritic cell activation. {ECO:0000269|PubMed:18390730, ECO:0000269|PubMed:20935647}.; . TISSUE SPECIFICITY: In general, low constitutive expression, if any, in healthy tissues; high expression in inflammatory counterparts, including in synovial tissues from individuals with active rheumatoid arthritis. Isoform A, isoform B and isoform C are expressed in testis, colon, placenta, lung and lymph node. Isoform D and isoform E were found only in testis and bone marrow. Whereas only isoform A is found in brain, only isoform B in kidney and only isoform C in heart. {ECO:0000269|PubMed:11145836, ECO:0000269|PubMed:20935647}.; lung;placenta;testis;colon; superior cervical ganglion;testis - seminiferous tubule;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.03816 0.07669 1.616843854 95.96013211 1666.56749 7.53757 ILDR1 7.93588407013792e-07 0.730210498831357 0.269788707580236 immunoglobulin like domain containing receptor 1 FUNCTION: Putative membrane receptor.; . TISSUE SPECIFICITY: Mainly expressed in prostate and to a lower extent in testis, pancreas, kidney, heart and liver. {ECO:0000269|PubMed:15381095}.; prostate;lung;ovary;heart;islets of Langerhans;placenta;testis;colon;kidney;germinal center; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.15121 0.09890 -0.018331246 52.2764803 2310.59269 8.90441 ILDR2 0.398939847020927 0.600671466473797 0.000388686505275666 immunoglobulin like domain containing receptor 2 FUNCTION: May be involved in lipid homeostasis and ER stress pathways. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;ovary;placenta;testis;parathyroid;brain;retina; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.39674 0.09140 -0.181750739 40.15687662 754.39853 5.44612 ILF2 0.997052017177466 0.00294795293257494 2.98899590729656e-08 interleukin enhancer binding factor 2 FUNCTION: Appears to function predominantly as a heterodimeric complex with ILF3. This complex may regulate transcription of the IL2 gene during T-cell activation. It can also promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA. Essential for the efficient reshuttling of ILF3 (isoform 1 and isoform 2) into the nucleus. {ECO:0000269|PubMed:10574923, ECO:0000269|PubMed:11739746, ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:9442054}.; . . lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;heart;hypothalamus;muscle;pharynx;blood;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.77435 0.15588 -0.031067188 51.03798066 4.82461 0.17675 ILF2P1 . . . interleukin enhancer binding factor 2 pseudogene 1 . . . . . . . . . . . ILF2P2 . . . interleukin enhancer binding factor 2 pseudogene 2 . . . . . . . . . . . ILF3 0.999996830604967 3.16939502443801e-06 8.64429079352486e-15 interleukin enhancer binding factor 3 FUNCTION: May facilitate double-stranded RNA-regulated gene expression at the level of post-transcription. Can act as a translation inhibitory protein which binds to coding sequences of acid beta-glucosidase (GCase) and other mRNAs and functions at the initiation phase of GCase mRNA translation, probably by inhibiting its binding to polysomes. Can regulate protein arginine N- methyltransferase 1 activity. May regulate transcription of the IL2 gene during T-cell activation. Can promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA. The phosphorylated form at Thr-188 and Thr-315, in concert with EIF2AK2/PKR can inhibit vesicular stomatitis virus (VSV) replication (By similarity). {ECO:0000250, ECO:0000269|PubMed:7519613, ECO:0000269|PubMed:9442054}.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;cornea;placenta;duodenum;head and neck;kidney;stomach;thymus;cerebellum; testis - interstitial;prostate;superior cervical ganglion;testis - seminiferous tubule;adrenal cortex;testis;globus pallidus;white blood cells;atrioventricular node;trigeminal ganglion;cerebellum; 0.78351 0.29990 -1.151821487 6.269167256 1006.84842 6.10898 ILF3-AS1 . . . ILF3 antisense RNA 1 (head to head) . . . . . . . . . . . ILK 0.0421959659732426 0.957551664334515 0.000252369692242563 integrin linked kinase FUNCTION: Receptor-proximal protein kinase regulating integrin- mediated signal transduction. May act as a mediator of inside-out integrin signaling. Focal adhesion protein part of the complex ILK-PINCH. This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway. Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B.; . TISSUE SPECIFICITY: Highly expressed in heart followed by skeletal muscle, pancreas and kidney. Weakly expressed in placenta, lung and liver.; myocardium;lymphoreticular;medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;iris;germinal center;brain;tonsil;heart;cartilage;pineal body;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; . 0.64136 0.59865 -0.692458599 14.96815287 53.76589 1.46097 ILKAP 0.99250779685517 0.00749076167198173 1.44147284806029e-06 ILK associated serine/threonine phosphatase FUNCTION: Protein phosphatase that may play a role in regulation of cell cycle progression via dephosphorylation of its substrates whose appropriate phosphorylation states might be crucial for cell proliferation. Selectively associates with integrin linked kinase (ILK), to modulate cell adhesion and growth factor signaling. Inhibits the ILK-GSK3B signaling axis and may play an important role in inhibiting oncogenic transformation. {ECO:0000269|PubMed:14990992}.; . TISSUE SPECIFICITY: Widely expressed. Highest levels expressed in striated muscle. Much lower levels evident in various smooth muscle tissues. {ECO:0000269|PubMed:11331582}.; ovary;sympathetic chain;colon;parathyroid;skin;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;aorta;peripheral nerve; superior cervical ganglion; 0.99445 0.10396 -0.271755481 34.31823543 16.60049 0.58557 ILVBL 1.13705980806844e-05 0.945293785551837 0.054694843850082 ilvB (bacterial acetolactate synthase)-like . . TISSUE SPECIFICITY: Expressed in all tissues tested, with highest expression in heart, pancreas and placenta. {ECO:0000269|PubMed:8954801}.; lymphoreticular;myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;blood;lens;bile duct;breast;pancreas;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;heart;thyroid;placenta;liver;kidney; 0.22645 0.17040 1.20517535 93.01722104 379.14108 4.10625 IMMP1L 0.0207131651278836 0.905448397283263 0.0738384375888538 inner mitochondrial membrane peptidase subunit 1 FUNCTION: Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO. {ECO:0000269|PubMed:15814844}.; . . unclassifiable (Anatomical System);myocardium;cartilage;islets of Langerhans;colon;uterus;prostate;whole body;lung;endometrium;thyroid;liver;pituitary gland;brain;mammary gland;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.25989 0.11651 -0.007201372 53.19061099 66.37425 1.67799 IMMP1LP1 . . . inner mitochondrial membrane peptidase subunit 1 pseudogene 1 . . . . . . . . . . . IMMP1LP2 . . . inner mitochondrial membrane peptidase subunit 1 pseudogene 2 . . . . . . . . . . . IMMP1LP3 . . . inner mitochondrial membrane peptidase subunit 1 pseudogene 3 . . . . . . . . . . . IMMP2L 0.0407609178597598 0.843178173476563 0.116060908663677 inner mitochondrial membrane peptidase subunit 2 FUNCTION: Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO. {ECO:0000269|PubMed:15814844}.; . TISSUE SPECIFICITY: Expressed in all tissues tested except adult liver and lung. {ECO:0000269|PubMed:11254443}.; unclassifiable (Anatomical System);smooth muscle;heart;colon;skin;uterus;prostate;lung;placenta;liver;testis;spleen;kidney; . 0.19555 0.14229 -0.073340031 48.11866006 39.49407 1.16596 IMMT 0.000945647236388923 0.99851349536446 0.000540857399151474 inner membrane mitochondrial protein FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology (PubMed:22114354, PubMed:25781180). {ECO:0000269|PubMed:22114354, ECO:0000269|PubMed:25781180}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;oesophagus;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;muscle;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; occipital lobe;testis - seminiferous tubule;testis;parietal lobe;skeletal muscle; 0.48938 0.38729 -0.442665927 24.53408823 3637.98851 11.70751 IMMTP1 . . . inner membrane mitochondrial protein pseudogene 1 . . . . . . . . . . . IMP3 5.33334042533681e-05 0.142148203220993 0.857798463374754 IMP3, U3 small nucleolar ribonucleoprotein FUNCTION: Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing. {ECO:0000269|PubMed:12655004}.; . . ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pineal body;pharynx;blood;lens;skeletal muscle;greater omentum;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus;cerebellum; whole brain;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.51232 0.11809 0.147123112 64.11299835 46.39739 1.31336 IMP3P1 . . . IMP3 pseudogene 1 . . . . . . . . . . . IMP3P2 . . . IMP3 pseudogene 2 . . . . . . . . . . . IMP4 0.000968217902139582 0.986628833324343 0.0124029487735172 IMP4 homolog, U3 small nucleolar ribonucleoprotein FUNCTION: Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing. {ECO:0000269|PubMed:12655004}.; . . lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; whole brain;liver;cingulate cortex;parietal lobe; 0.13874 0.12165 -0.135838822 43.77211607 791.68973 5.55087 IMPA1 0.0175360055513113 0.960550972487259 0.0219130219614299 inositol(myo)-1(or 4)-monophosphatase 1 FUNCTION: Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Has broad substrate specificity and can use myo- inositol monophosphates, myo-inositol 1,3-diphosphate, myo- inositol 1,4-diphosphate, scyllo-inositol-phosphate, D-galactose 1-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1- phosphate, beta-glycerophosphate, and 2'-AMP as substrates. {ECO:0000269|PubMed:17068342, ECO:0000269|PubMed:8718889, ECO:0000269|PubMed:9462881}.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;endometrium;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;breast;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;occipital lobe;superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;testis;trigeminal ganglion; 0.52457 0.38957 0.349177632 74.18023119 68.68136 1.71541 IMPA1P . . . inositol(myo)-1(or 4)-monophosphatase 1 pseudogene . . . . . . . . . . . IMPA2 0.237822649061139 0.755127914499542 0.00704943643931896 inositol(myo)-1(or 4)-monophosphatase 2 FUNCTION: Can use myo-inositol monophosphates, scylloinositol 1,4- diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'- AMP as substrates. Has been implicated as the pharmacological target for lithium Li(+) action in brain. {ECO:0000269|PubMed:17068342}.; . . ovary;salivary gland;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);heart;tongue;muscle;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; placenta;kidney;skeletal muscle; 0.53908 0.23623 0.327131069 73.27199811 212.72651 3.14791 IMPACT 3.31631338303807e-05 0.805458257631449 0.19450857923472 impact RWD domain protein FUNCTION: Translational regulator that ensures constant high levels of translation upon a variety of stress conditions, such as amino acid starvation, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation. Plays a role as a negative regulator of the EIF2AK4/GCN2 kinase activity; impairs GCN1- mediated EIF2AK4/GCN2 activation, and hence EIF2AK4/GCN2-mediated eIF-2-alpha phosphorylation and subsequent down-regulation of protein synthesis. May be required to regulate translation in specific neuronal cells under amino acid starvation conditions by preventing GCN2 activation and therefore ATF4 synthesis. Through its inhibitory action on EIF2AK4/GCN2, plays a role in differentiation of neuronal cells by stimulating neurite outgrowth. {ECO:0000250|UniProtKB:O55091}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at high level in brain. {ECO:0000269|PubMed:11116084, ECO:0000269|PubMed:11244491}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach; superior cervical ganglion;ciliary ganglion; 0.24331 0.11911 0.260991686 70.25831564 351.46693 3.97285 IMPAD1 0.327579022336398 0.656762425961695 0.0156585517019074 inositol monophosphatase domain containing 1 FUNCTION: May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',5'-bisphosphate produced by Golgi sulfotransferases during glycosaminoglycan sulfation. {ECO:0000250}.; DISEASE: Chondrodysplasia with joint dislocations, GPAPP type (CDP-GPAPP) [MIM:614078]: A condition consisting of congenital joint dislocations, chondrodysplasia with short stature, micrognathia and cleft palate, and a distinctive face. {ECO:0000269|PubMed:21549340}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;endometrium;thyroid;bone;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);heart;cartilage;spinal cord;blood;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;kidney;stomach; placenta;testis;trigeminal ganglion;parietal lobe; 0.22984 0.10568 -0.315847836 31.68789809 39.07796 1.15871 IMPDH1 0.00581185872999049 0.993226507694898 0.000961633575111018 IMP (inosine 5'-monophosphate) dehydrogenase 1 FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate- limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.; DISEASE: Retinitis pigmentosa 10 (RP10) [MIM:180105]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:11875049, ECO:0000269|PubMed:11875050, ECO:0000269|PubMed:16384941}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leber congenital amaurosis 11 (LCA11) [MIM:613837]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:16384941}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: IMP type I is the main species in normal leukocytes and type II predominates over type I in the tumor.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;pons; 0.69586 0.09849 -0.244249595 36.17008728 74.88549 1.81072 IMPDH1P1 . . . IMP (inosine monophosphate) dehydrogenase 1 pseudogene 1 . . . . . . . . . . . IMPDH1P2 . . . IMP (inosine monophosphate) dehydrogenase 1 pseudogene 2 . . . . . . . . . . . IMPDH1P3 . . . IMP (inosine monophosphate) dehydrogenase 1 pseudogene 3 . . . . . . . . . . . IMPDH1P4 . . . IMP (inosine monophosphate) dehydrogenase 1 pseudogene 4 . . . . . . . . . . . IMPDH1P5 . . . IMP (inosine monophosphate) dehydrogenase 1 pseudogene 5 . . . . . . . . . . . IMPDH1P6 . . . IMP (inosine monophosphate) dehydrogenase 1 pseudogene 6 . . . . . . . . . . . IMPDH1P7 . . . IMP (inosine monophosphate) dehydrogenase 1 pseudogene 7 . . . . . . . . . . . IMPDH1P8 . . . IMP (inosine monophosphate) dehydrogenase 1 pseudogene 8 . . . . . . . . . . . IMPDH1P9 . . . IMP (inosine monophosphate) dehydrogenase 1 pseudogene 9 . . . . . . . . . . . IMPDH1P10 . . . IMP (inosine monophosphate) dehydrogenase 1 pseudogene 10 . . . . . . . . . . . IMPDH1P11 . . . IMP (inosine monophosphate) dehydrogenase 1 pseudogene 11 . . . . . . . . . . . IMPDH2 0.00135316628366044 0.9908959313458 0.0077509023705395 IMP (inosine 5'-monophosphate) dehydrogenase 2 FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate- limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.; . TISSUE SPECIFICITY: IMP type I is the main species in normal leukocytes and type II predominates over type I in the tumor.; lymphoreticular;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;trabecular meshwork;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; tumor; 0.96503 0.39372 -0.648365105 16.35999056 20.66552 0.70197 IMPG1 6.13186468480682e-13 0.35464184454479 0.645358155454597 interphotoreceptor matrix proteoglycan 1 FUNCTION: May interact with hyaluronan which may serve to form a basic macromolecular scaffold comprising the insoluble interphotoreceptor matrix. {ECO:0000269|PubMed:9813076}.; DISEASE: Macular dystrophy, vitelliform, 4 (VMD4) [MIM:616151]: A form of macular dystrophy, a retinal disease in which various forms of deposits, pigmentary changes, and atrophic lesions are observed in the macula lutea. Vitelliform macular dystrophies are characterized by yellow, lipofuscin-containing deposits, usually localized at the center of the macula. VMD4 features include late- onset moderate visual impairment, small satellite drusen-like lesions in the foveal area, and preservation of retinal pigment epithelium reflectivity. {ECO:0000269|PubMed:23993198}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Abundantly expressed in retina where it is specifically expressed by cone and rod photoreceptor cells. Localizes to cone and rod photoreceptor cells surrounding the interphotoreceptor matrix of the retina. {ECO:0000269|PubMed:10601738, ECO:0000269|PubMed:9719680, ECO:0000269|PubMed:9813076}.; . . 0.26878 0.09179 0.694433477 85.28544468 2205.13484 8.64488 IMPG2 1.4748151437863e-08 0.997551473492941 0.00244851175890726 interphotoreceptor matrix proteoglycan 2 FUNCTION: Chondroitin sulfate- and hyaluronan-binding proteoglycan involved in the organization of interphotoreceptor matrix; may participate in the maturation and maintenance of the light- sensitive photoreceptor outer segment. Binds heparin. {ECO:0000269|PubMed:10702256}.; DISEASE: Retinitis pigmentosa 56 (RP56) [MIM:613581]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:20673862}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Macular dystrophy, vitelliform, 5 (VMD5) [MIM:616152]: A form of macular dystrophy, a retinal disease in which various forms of deposits, pigmentary changes, and atrophic lesions are observed in the macula lutea. Vitelliform macular dystrophies are characterized by yellow, lipofuscin-containing deposits, usually localized at the center of the macula. VMD5 features include late- onset moderate visual impairment and preservation of retinal pigment epithelium reflectivity. {ECO:0000269|PubMed:20673862, ECO:0000269|PubMed:25085631}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the retina. Expressed by photoreceptors of the interphotoreceptor matrix (IPM) surrounding both rods and cones. IPM occupies the subretinal space between the apices of the retinal pigment epithelium and the neural retina. Detected in the pineal gland. {ECO:0000269|PubMed:10542133, ECO:0000269|PubMed:10702256}.; unclassifiable (Anatomical System);optic nerve;pineal body;macula lutea;visual apparatus;fovea centralis;choroid;germinal center;lens;skeletal muscle;retina; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.11371 0.11319 -0.837696902 11.45317292 209.43193 3.12459 INA 0.29291701476286 0.686595637239416 0.0204873479977243 internexin neuronal intermediate filament protein alpha FUNCTION: Class-IV neuronal intermediate filament that is able to self-assemble. It is involved in the morphogenesis of neurons. It may form an independent structural network without the involvement of other neurofilaments or it may cooperate with NF-L to form the filamentous backbone to which NF-M and NF-H attach to form the cross-bridges.; . . . . 0.30146 0.26304 -0.095386216 46.48502005 174.52967 2.87390 INAFM1 . . . InaF motif containing 1 . . . . . . . . . . . INAFM2 . . . InaF motif containing 2 . . . . . . . . . . . INCA1 8.26123539486397e-09 0.0818776382209597 0.918122353517805 inhibitor of CDK, cyclin A1 interacting protein 1 . . TISSUE SPECIFICITY: Detected in testis, and at lower levels in ovary. Detected at very low levels in testis tumors. {ECO:0000269|PubMed:15159402}.; unclassifiable (Anatomical System);uterus;lung;heart;urinary;mammary gland;skin; . . . 0.21689899 68.12927577 280.10349 3.58648 INCENP 0.996086664513722 0.00391333304294333 2.44333441791966e-09 inner centromere protein FUNCTION: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Probably acts through association with AURKB or AURKC. Seems to bind directly to microtubules. Controls the kinetochore localization of BUB1. {ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:15316025, ECO:0000269|PubMed:16760428}.; . . unclassifiable (Anatomical System);smooth muscle;whole body;ovary;thyroid;testis;colon;cervix;head and neck;skin;thymus; superior cervical ganglion;globus pallidus; 0.16577 0.12728 0.832189686 88.12809625 6919.01907 17.71496 INE1 . . . inactivation escape 1 (non-protein coding) . . TISSUE SPECIFICITY: Highly expressed in pancreas, heart and liver followed by brain, placenta, lung, skeletal muscle and kidney. Mostly expressed in females. {ECO:0000269|PubMed:9244435}.; . . . . . . . . INE2 . . . inactivation escape 2 (non-protein coding) . . . . . . . . . . . INF2 0.999083287804995 0.000916712124084224 7.09207198846308e-11 inverted formin, FH2 and WH2 domain containing FUNCTION: Severs actin filaments and accelerates their polymerization and depolymerization. {ECO:0000250}.; DISEASE: Focal segmental glomerulosclerosis 5 (FSGS5) [MIM:613237]: A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation. {ECO:0000269|PubMed:20023659, ECO:0000269|PubMed:21258034, ECO:0000269|PubMed:21866090, ECO:0000269|PubMed:22971997, ECO:0000269|PubMed:25165188}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease, dominant, intermediate type, E (CMTDIE) [MIM:614455]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. The dominant intermediate type E is characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. Patients additionally manifest focal segmental glomerulonephritis, proteinuria, progression to end- stage renal disease, and a characteristic histologic pattern on renal biopsy. {ECO:0000269|PubMed:22187985, ECO:0000269|PubMed:24174593, ECO:0000269|PubMed:24750328, ECO:0000269|PubMed:25165188, ECO:0000269|PubMed:25676889}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. In the kidney, expression is apparent in podocytes and some tubule cells. {ECO:0000269|PubMed:20023659}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; dorsal root ganglion;medulla oblongata;superior cervical ganglion;olfactory bulb;spinal cord;temporal lobe;caudate nucleus;pons;atrioventricular node;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; . . -0.033100763 50.56027365 2152.91209 8.53891 ING1 0.0114357020023887 0.979963341247844 0.00860095674976668 inhibitor of growth family member 1 FUNCTION: Cooperates with p53/TP53 in the negative regulatory pathway of cell growth by modulating p53-dependent transcriptional activation. Implicated as a tumor suppressor gene. {ECO:0000269|PubMed:9440695}.; DISEASE: Squamous cell carcinoma of the head and neck (HNSCC) [MIM:275355]: A non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes. {ECO:0000269|PubMed:10866301}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 2 was expressed in all normal tissues and cells examined, as well as in all breast cancer and melanoma cell lines examined. Isoform 3 was expressed in testis, liver, and kidney, weakly expressed in colon and brain and not expressed in breast and cultured melanocytes. Isoform 4 was highly expressed in testis and weakly expressed in brain, but not expressed in breast, colon, kidney, melanocytes, breast cancer or melanoma cell lines. {ECO:0000269|PubMed:10626813}.; ovary;salivary gland;colon;parathyroid;skin;retina;uterus;prostate;whole body;larynx;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;pineal body;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;hippocampus;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.78935 0.17351 -0.512444034 21.55579146 154.20317 2.71419 ING2 0.283379994488456 0.694525974559904 0.0220940309516404 inhibitor of growth family member 2 FUNCTION: Seems to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, probably by enhancing acetylation of p53/TP53. Component of a mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity seems to be modulated by binding to phosphoinositides (PtdInsPs). {ECO:0000269|PubMed:11481424, ECO:0000269|PubMed:12859901}.; . TISSUE SPECIFICITY: Widely expressed. Higher expressed in colon- cancer tumor than in normal colon tissues. {ECO:0000269|PubMed:10072587}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;cochlea;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;blood;lens;skeletal muscle;lung;placenta;macula lutea;hippocampus;liver;amnion;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion; 0.87762 0.12971 -0.09720619 46.20193442 12.79007 0.46503 ING3 0.9936029551269 0.00639700475623129 4.01168685154417e-08 inhibitor of growth family member 3 FUNCTION: Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. {ECO:0000269|PubMed:12545155, ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:24463511}.; DISEASE: Squamous cell carcinoma of the head and neck (HNSCC) [MIM:275355]: A non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes. {ECO:0000269|PubMed:12080476}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, ovaries, placenta, prostate, skeletal muscle, small intestine, spleen, testis and thymus.; lymphoreticular;ovary;colon;skin;retina;uterus;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;bile duct;pancreas;lung;nasopharynx;internal ear;placenta;liver;spleen;kidney;mammary gland;stomach;thymus; dorsal root ganglion;medulla oblongata;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.97909 0.10706 -0.317668748 31.45789101 17.85718 0.62385 ING4 0.0521019243914109 0.927097528202936 0.020800547405653 inhibitor of growth family member 4 FUNCTION: Component of the HBO1 complex which has a histone H4- specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Through chromatin acetylation it may function in DNA replication. May inhibit tumor progression by modulating the transcriptional output of signaling pathways which regulate cell proliferation. Can suppress brain tumor angiogenesis through transcriptional repression of RELA/NFKB3 target genes when complexed with RELA. May also specifically suppress loss of contact inhibition elicited by activated oncogenes such as MYC. Represses hypoxia inducible factor's (HIF) activity by interacting with HIF prolyl hydroxylase 2 (EGLN1). Can enhance aopotosis induced by serum starvation in mammary epithelial cell line HC11 (By similarity). {ECO:0000250|UniProtKB:Q8C0D7, ECO:0000269|PubMed:12750254, ECO:0000269|PubMed:15029197, ECO:0000269|PubMed:15251430, ECO:0000269|PubMed:15528276, ECO:0000269|PubMed:15897452, ECO:0000269|PubMed:16387653}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;gum;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;kidney;mammary gland;thymus; occipital lobe;cerebellum peduncles;globus pallidus;atrioventricular node;cerebellum; 0.96198 0.17050 -0.029247611 51.40363293 22.09017 0.74209 ING5 0.445393628361777 0.553264061564212 0.00134231007401113 inhibitor of growth family member 5 FUNCTION: Component of the HBO1 complex which has a histone H4- specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Through chromatin acetylation it may regulate DNA replication and may function as a transcriptional coactivator. {ECO:0000269|PubMed:12750254, ECO:0000269|PubMed:16387653}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; ciliary ganglion;atrioventricular node;trigeminal ganglion; . 0.13434 -0.317668748 31.45789101 12.80248 0.46577 INGX . . . inhibitor of growth family, X-linked (pseudogene) FUNCTION: Seems to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, probably by enhancing acetylation of p53/TP53. Component of a mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity seems to be modulated by binding to phosphoinositides (PtdInsPs). {ECO:0000269|PubMed:11481424, ECO:0000269|PubMed:12859901}.; . TISSUE SPECIFICITY: Widely expressed. Higher expressed in colon- cancer tumor than in normal colon tissues. {ECO:0000269|PubMed:10072587}.; . . 0.16591 0.12971 -0.09720619 46.20193442 . . INHA 0.199710681546667 0.755471141838572 0.0448181766147612 inhibin alpha FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.; . TISSUE SPECIFICITY: Originally found in ovary (granulosa cells) and testis (Sertoli cells), but widely distributed in many tissues including brain and placenta. In adrenal cortex expression is limited to the zona reticularis and the innermost zona fasciculata in the normal gland, extending centripetally into the zona fasciculata in hyperplasia. Also found in adrenocortical tumors. Also expressed in prostate epithelium of benign prostatic hyperplasia, in regions of basal cell hyperplasia and in nonmalignant regions of high grade prostate cancer. Only circulating inhibin B is found in male, whereas circulating inhibins A and B are found in female. {ECO:0000269|PubMed:9506758}.; unclassifiable (Anatomical System);medulla oblongata;heart;ovary;hypothalamus;lens;skin;uterus;lung;placenta;thyroid;visual apparatus;liver;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;adrenal gland;placenta;testis; 0.35438 0.26019 0.084621747 60.31493277 307.90129 3.73451 INHBA 0.556279739729954 0.43076942821321 0.0129508320568366 inhibin beta A FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;optic nerve;endometrium;larynx;thyroid;bone;amniotic fluid;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;head and neck;stomach; . 0.91315 0.29335 -0.381986487 27.68931352 23.87044 0.78711 INHBA-AS1 . . . INHBA antisense RNA 1 . . . . . . . . . . . INHBB 0.916829217955213 0.0826114741551976 0.000559307889589032 inhibin beta B FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.; . . lacrimal gland;adrenal cortex;colon;fovea centralis;choroid;lens;retina;uterus;breast;prostate;optic nerve;lung;thyroid;macula lutea;hippocampus;visual apparatus;liver;testis;mammary gland; superior cervical ganglion;testis; 0.29367 0.25783 . . 1425.4818 7.04962 INHBC 0.083686116557619 0.871531515308899 0.0447823681334824 inhibin beta C FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.; . TISSUE SPECIFICITY: Expressed in benign prostatic hyperplasia. {ECO:0000269|PubMed:9428386}.; liver;spleen;stomach; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16556 0.18306 0.12689526 63.00424628 956.55034 5.98742 INHBE 7.68032635379316e-06 0.500761409607002 0.499230910066644 inhibin beta E FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.; . . unclassifiable (Anatomical System);bone;muscle;cervix; superior cervical ganglion;temporal lobe;liver;globus pallidus;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.13535 0.54564 -0.291981272 33.20358575 52.47928 1.43339 INIP 0.017451553253115 0.717632071171947 0.264916375574938 INTS3 and NABP interacting protein FUNCTION: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single- stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination- dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways. {ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}.; . . . . 0.26262 . 0.057118534 57.99716914 1.19806 0.03523 INMT 0.000120277973301167 0.385694999644525 0.614184722382174 indolethylamine N-methyltransferase FUNCTION: Functions as thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2- methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide. Plays an important role in the detoxification of selenium compounds (By similarity). Catalyzes the N-methylation of tryptamine and structurally related compounds. {ECO:0000250, ECO:0000269|PubMed:10552930}.; . TISSUE SPECIFICITY: Widely expressed. The highest levels were in thyroid, adrenal gland, adult and fetal lung. Intermediate levels in heart, placenta, skeletal muscle, testis, small intestine, pancreas, stomach, spinal cord, lymph node and trachea. Very low levels in adult and fetal kidney and liver, in adult spleen, thymus, ovary, colon and bone marrow. Not expressed in peripheral blood leukocytes and brain. {ECO:0000269|PubMed:10552930}.; unclassifiable (Anatomical System);lung;spleen; . 0.10895 0.11082 1.976952171 97.61146497 4681.43934 13.79634 INMT-FAM188B . . . INMT-FAM188B readthrough (NMD candidate) . . . . . . . . . 2.39611 0.08227 INO80 0.999999999807578 1.9242240322377e-10 3.83522802245517e-27 INO80 complex subunit FUNCTION: DNA helicase and probable main scaffold component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; according to PubMed:20687897 the contribution to DNA double-strand break repair appears to be largely indirect through transcriptional regulation. Recruited by YY1 to YY1-activated genes, where it acts as an essential coactivator. Binds DNA. In vitro, has double-stranded DNA-dependent ATPase activity. Involved in UV-damage excision repair, DNA replication and chromosome segregation during normal cell division cycle. {ECO:0000269|PubMed:16230350, ECO:0000269|PubMed:16298340, ECO:0000269|PubMed:17721549, ECO:0000269|PubMed:20237820, ECO:0000269|PubMed:20687897, ECO:0000269|PubMed:20855601, ECO:0000269|PubMed:21303910}.; . TISSUE SPECIFICITY: According to PubMed:10574462, widely expressed. According to PubMed:16298340, specifically expressed in brain, liver and pancreas. {ECO:0000269|PubMed:10574462, ECO:0000269|PubMed:16298340}.; ovary;colon;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.64254 0.10729 -1.100469982 6.929700401 172.04279 2.86101 INO80B 0.949554116037684 0.0502871545570275 0.000158729405288339 INO80 complex subunit B FUNCTION: Induces growth and cell cycle arrests at the G1 phase of the cell cycle. {ECO:0000269|PubMed:15556297}.; . . ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;endometrium;bone;testis;brain;tonsil;unclassifiable (Anatomical System);cartilage;blood;lens;pancreas;lung;placenta;visual apparatus;macula lutea;cervix;kidney;mammary gland;thymus; globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; . 0.10591 -0.207437529 38.2814343 33.25025 1.02762 INO80B-WBP1 . . . INO80B-WBP1 readthrough (NMD candidate) . . . . . . . . . . . INO80C 0.000502408928799958 0.445586484317471 0.553911106753729 INO80 complex subunit C FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;hypothalamus;parathyroid;skin;uterus;prostate;lung;adrenal gland;bone;placenta;visual apparatus;liver;spleen;kidney;brain;stomach; . 0.15413 0.08709 0.148941568 64.31941496 119.70597 2.38169 INO80D 0.99817951445727 0.00182048367630475 1.86642553578965e-09 INO80 complex subunit D FUNCTION: Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.; . . unclassifiable (Anatomical System);tongue;muscle;colon;blood;lens;uterus;breast;prostate;whole body;lung;frontal lobe;epididymis;bone;placenta;testis;germinal center;brain;mammary gland; medulla oblongata;superior cervical ganglion;temporal lobe;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.08535 -0.462894052 23.62585515 3203.94442 10.78870 INO80E 0.0174146851193449 0.891403714881665 0.0911815999989901 INO80 complex subunit E FUNCTION: Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; subthalamic nucleus;testis - interstitial;superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion;skin; 0.18786 0.11011 -0.073340031 48.11866006 41.31906 1.20769 INPP1 0.000237351689203819 0.757414148786887 0.242348499523909 inositol polyphosphate-1-phosphatase . . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in pancreas and kidney.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;larynx;iris;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;parietal lobe; 0.14458 0.14062 0.12689526 63.00424628 391.38452 4.16437 INPP4A 0.99488626390091 0.00511373514881648 9.50273404871227e-10 inositol polyphosphate-4-phosphatase type I A FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4- trisphosphate and inositol 3,4-bisphosphate.; . TISSUE SPECIFICITY: Isoform 1 is expressed in the platelets, MEG- 01 megakaryocytes and Jurkat T-cells. Isoform 2 is expressed in the brain. {ECO:0000269|PubMed:11485317}.; unclassifiable (Anatomical System);amygdala;colon;blood;skin;bone marrow;uterus;pancreas;whole body;lung;frontal lobe;adrenal gland;amnion;amniotic fluid;bladder; amygdala;occipital lobe;superior cervical ganglion;prefrontal cortex;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;cerebellum; 0.27149 0.11333 -1.240018202 5.461193678 195.99604 3.02944 INPP4B 0.998611010146477 0.00138898984552809 7.99530666049453e-12 inositol polyphosphate-4-phosphatase type II B FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4- trisphosphate and inositol 1,4-bisphosphate.; . TISSUE SPECIFICITY: Widely expressed with highest levels occurring in the skeletal muscle and heart. {ECO:0000269|PubMed:9295334}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;urinary;colon;parathyroid;skin;skeletal muscle;breast;uterus;bile duct;pancreas;lung;bone;placenta;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;skeletal muscle; 0.04918 0.10470 -0.440847477 24.59896202 99.84144 2.16508 INPP5A 0.942238413616355 0.0577597229531438 1.86343050147618e-06 inositol polyphosphate-5-phosphatase A FUNCTION: Major isoenzyme hydrolyzing the calcium-mobilizing second messenger Ins(1,4,5)P3, this is a signal-terminating reaction.; . TISSUE SPECIFICITY: Brain; high level in Purkinje cells.; myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;synovium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;adrenal cortex;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; whole brain;thalamus;superior cervical ganglion;medulla oblongata;cerebellum peduncles;caudate nucleus;pons;cingulate cortex;parietal lobe;cerebellum; 0.11516 0.20455 -0.422438699 25.64284029 1627.83313 7.46017 INPP5B 7.43289930464084e-09 0.998671211931892 0.00132878063520878 inositol polyphosphate-5-phosphatase B FUNCTION: Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events. {ECO:0000269|PubMed:7721860}.; . TISSUE SPECIFICITY: Platelets.; . . 0.15509 0.12734 -0.907472583 10.07313046 3086.49637 10.55544 INPP5D 0.167430840933568 0.832564138773755 5.02029267690789e-06 inositol polyphosphate-5-phosphatase D FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol- 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity. Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. {ECO:0000269|PubMed:12421919, ECO:0000269|PubMed:16682172}.; . TISSUE SPECIFICITY: Specifically expressed in immune and hematopoietic cells. Expressed in bone marrow and blood cells. Levels vary considerably within this compartment. Present in at least 74% of immature CD34+ cells, whereas within the more mature population of CD33+ cells, it is present in only 10% of cells. Present in the majority of T-cells, while it is present in a minority of B-cells (at protein level). {ECO:0000269|PubMed:8769125, ECO:0000269|PubMed:8874179, ECO:0000269|PubMed:9058707, ECO:0000269|PubMed:9108392}.; unclassifiable (Anatomical System);lymph node;ovary;lacrimal gland;sympathetic chain;colon;parathyroid;blood;skin;bone marrow;breast;uterus;prostate;lung;frontal lobe;placenta;iris;testis;spleen;germinal center;kidney;brain;thymus; dorsal root ganglion;superior cervical ganglion;white blood cells;ciliary ganglion;atrioventricular node;whole blood;trigeminal ganglion;skeletal muscle;tonsil;bone marrow; . 0.10540 . . 1963.99989 8.16671 INPP5E 0.388563848233216 0.609370054221142 0.00206609754564144 inositol polyphosphate-5-phosphatase E FUNCTION: Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns-P2, and phosphatidylinositol 4,5- bisphosphate to phosphatidylinositol 4-phosphate. Specific for lipid substrates, inactive towards water soluble inositol phosphates. {ECO:0000269|PubMed:10764818}.; DISEASE: Mental retardation, truncal obesity, retinal dystrophy, and micropenis (MORMS) [MIM:610156]: An autosomal recessive disorder characterized by moderate mental retardation, truncal obesity, congenital non-progressive retinal dystrophy, and micropenis in males. The phenotype is similar to Bardet-Biedl syndrome and Cohen syndrome Distinguishing features are the age of onset, the non-progressive nature of the visual impairment, lack of dysmorphic facies, skin or gingival infection, microcephaly, mottled retina, polydactyly, and testicular anomalies. {ECO:0000269|PubMed:19668215}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in brain, heart, pancreas, testis and spleen. {ECO:0000269|PubMed:10764818}.; . . 0.17417 0.11394 . . 107.34494 2.24812 INPP5F 0.00146883108535103 0.998530687106157 4.81808491868399e-07 inositol polyphosphate-5-phosphatase F FUNCTION: Inositol 5-phosphatase which acts on phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Hydrolyzes phosphatidylinositol 4,5- bisphosphate most effectively. Modulates AKT/GSK3B pathway by decreasing AKT and GSK3B phosphorylation. {ECO:0000269|PubMed:11274189, ECO:0000269|PubMed:17322895}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11274189}.; ovary;sympathetic chain;developmental;substantia nigra;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cerebellum cortex;nervous;islets of Langerhans;hypothalamus;spinal cord;blood;lens;skeletal muscle;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.16289 . -0.793601146 12.57372022 536.63529 4.72241 INPP5J 6.4309573309253e-12 0.0621872853177377 0.937812714675831 inositol polyphosphate-5-phosphatase J FUNCTION: Inositol 5-phosphatase, which converts inositol 1,4,5- trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4- phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate- binding proteins that are present at membranes ruffles (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;colon;parathyroid;choroid;skeletal muscle;retina;uterus;breast;prostate;lung;endometrium;thyroid;liver;head and neck;cervix;kidney;brain;mammary gland; superior cervical ganglion;cerebellum peduncles;thyroid;ciliary ganglion;atrioventricular node;fetal thyroid; 0.44430 0.14051 -0.224023033 37.4321774 1180.94022 6.52336 INPP5K 0.0133887227764052 0.979756347384334 0.00685492983926039 inositol polyphosphate-5-phosphatase K FUNCTION: Inositol 5-phosphatase which acts on inositol 1,4,5- trisphosphate, inositol 1,3,4,5-tetrakisphosphate, phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Has 6-fold higher affinity for phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5- trisphosphate. May negatively regulate assembly of the actin cytoskeleton. {ECO:0000269|PubMed:10753883}.; . TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in skeletal muscle, heart and kidney. {ECO:0000269|PubMed:10753883}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.11084 -0.066061882 48.77919321 74.79566 1.80970 INPPL1 0.00608952548790821 0.99390896443357 1.51007852148893e-06 inositol polyphosphate phosphatase like 1 FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol- 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (PubMed:21624956). Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma- RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification. {ECO:0000269|PubMed:11349134, ECO:0000269|PubMed:11739414, ECO:0000269|PubMed:12235291, ECO:0000269|PubMed:12676785, ECO:0000269|PubMed:12690104, ECO:0000269|PubMed:15668240, ECO:0000269|PubMed:17135240, ECO:0000269|PubMed:21624956, ECO:0000269|PubMed:23273569, ECO:0000269|PubMed:9660833}.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:12086927, ECO:0000269|PubMed:15687335}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; DISEASE: Note=Genetic variations in INPPL1 may be a cause of susceptibility to metabolic syndrome. Metabolic syndrome is characterized by diabetes, insulin resistance, hypertension, and hypertriglyceridemia is absent. {ECO:0000269|PubMed:15220217, ECO:0000269|PubMed:17557929}.; DISEASE: Opsismodysplasia (OPSMD) [MIM:258480]: A rare skeletal dysplasia involving delayed bone maturation. Clinical signs observed at birth include short limbs, small hands and feet, relative macrocephaly with a large anterior fontanel, and characteristic craniofacial abnormalities including a prominent brow, depressed nasal bridge, a small anteverted nose, and a relatively long philtrum. Death secondary to respiratory failure during the first few years of life has been reported, but there can be long-term survival. Typical radiographic findings include shortened long bones with very delayed epiphyseal ossification, severe platyspondyly, metaphyseal cupping, and characteristic abnormalities of the metacarpals and phalanges. {ECO:0000269|PubMed:23273569}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, most prominently in skeletal muscle, heart and brain. Present in platelets. Expressed in transformed myeloid cells and in primary macrophages, but not in peripheral blood monocytes. {ECO:0000269|PubMed:12676785, ECO:0000269|PubMed:12690104, ECO:0000269|PubMed:8530088, ECO:0000269|PubMed:9367831, ECO:0000269|PubMed:9660833}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;nervous;islets of Langerhans;urinary;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; thyroid; 0.12155 0.24744 -1.633317116 2.842651569 1349.46127 6.89699 INS 0.730321287731717 0.257334774904412 0.012343937363871 insulin FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.; DISEASE: Hyperproinsulinemia (HPRI) [MIM:616214]: An autosomal dominant condition characterized by elevated levels of serum proinsulin-like material. {ECO:0000269|PubMed:1601997, ECO:0000269|PubMed:2196279, ECO:0000269|PubMed:3470784, ECO:0000269|PubMed:4019786}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, insulin-dependent, 2 (IDDM2) [MIM:125852]: A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:18192540}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, permanent neonatal (PNDM) [MIM:606176]: A rare form of diabetes distinct from childhood- onset autoimmune diabetes mellitus type 1. It is characterized by insulin-requiring hyperglycemia that is diagnosed within the first months of life. Permanent neonatal diabetes requires lifelong therapy. {ECO:0000269|PubMed:17855560, ECO:0000269|PubMed:18162506}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Maturity-onset diabetes of the young 10 (MODY10) [MIM:613370]: A form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease. {ECO:0000269|PubMed:18162506, ECO:0000269|PubMed:18192540, ECO:0000269|PubMed:20226046}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . pancreas;islets of Langerhans; pancreas;superior cervical ganglion;beta cell islets;ciliary ganglion;trigeminal ganglion;parietal lobe;skeletal muscle; . . -0.075159878 47.78839349 2.77679 0.09927 INS-IGF2 0.0364414126480976 0.831715510751995 0.131843076599907 INS-IGF2 readthrough . . TISSUE SPECIFICITY: Expressed in pancreas, eye and, to a lower extent, in limb. {ECO:0000269|PubMed:16531418}.; myocardium;ovary;colon;fovea centralis;choroid;retina;uterus;optic nerve;whole body;frontal lobe;synovium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;muscle;lens;lung;placenta;macula lutea;visual apparatus;liver;spleen;mammary gland;aorta;peripheral nerve; pancreas;superior cervical ganglion;beta cell islets;ciliary ganglion;trigeminal ganglion;parietal lobe;skeletal muscle; . . -0.073340031 48.11866006 611.73703 4.99704 INSC 1.3427309129659e-09 0.338205483686509 0.66179451497076 inscuteable homolog (Drosophila) FUNCTION: May function as an adapter linking the Par3 complex to the GPSM1/GPSM2 complex (PubMed:16458856). Involved in spindle orientation during mitosis. May regulate cell proliferation and differentiation in the developing nervous system. May play a role in the asymmetric division of fibroblasts and participate in the process of stratification of the squamous epithelium (By similarity). {ECO:0000250|UniProtKB:Q3HNM7, ECO:0000305|PubMed:16458856}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in various tissues with stronger expression in liver, kidney and small intestine. Isoform 2 is abundantly expressed in small intestine and to a lower extent in lung and pancreas. {ECO:0000269|PubMed:12469229, ECO:0000269|PubMed:16458856}.; . . 0.24334 0.13495 0.892856963 89.28992687 1315.35282 6.81837 INSIG1 0.124543666409511 0.851542987681941 0.0239133459085473 insulin induced gene 1 FUNCTION: Mediates feedback control of cholesterol synthesis by controlling SCAP and HMGCR. Functions by blocking the processing of sterol regulatory element-binding proteins (SREBPs). Capable of retaining the SCAP-SREBF2 complex in the ER thus preventing it from escorting SREBPs to the Golgi. Initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligase, AMFR/gp78. May play a role in growth and differentiation of tissues involved in metabolic control. May play a regulatory role during G0/G1 transition of cell growth. {ECO:0000269|PubMed:12202038, ECO:0000269|PubMed:12535518, ECO:0000269|PubMed:16168377, ECO:0000269|PubMed:16399501, ECO:0000269|PubMed:16606821}.; . TISSUE SPECIFICITY: Expressed in all tissues tested with highest expression in the liver. {ECO:0000269|PubMed:12202038}.; lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;ciliary body;bladder;brain;tonsil;amygdala;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;duodenum;kidney;stomach;aorta; amygdala;prostate;superior cervical ganglion;adipose tissue;placenta;liver;tumor;ciliary ganglion; 0.13097 0.17106 -0.141298762 42.87567823 10.72887 0.38957 INSIG2 0.023277147220178 0.912999877632854 0.0637229751469679 insulin induced gene 2 FUNCTION: Mediates feedback control of cholesterol synthesis by controlling SCAP and HMGCR. Functions by blocking the processing of sterol regulatory element-binding proteins (SREBPs). Capable of retaining the SCAP-SREBF2 complex in the ER thus preventing it from escorting SREBPs to the Golgi. Seems to regulate the ubiquitin-mediated proteasomal degradation of HMGCR. {ECO:0000269|PubMed:12242332, ECO:0000269|PubMed:16606821}.; . . colon;parathyroid;skin;uterus;prostate;frontal lobe;bone;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;skeletal muscle; 0.25105 0.20499 -0.207437529 38.2814343 10.87534 0.39370 INSL3 0.0341265074058471 0.618242540767453 0.3476309518267 insulin like 3 FUNCTION: Seems to play a role in testicular function. May be a trophic hormone with a role in testicular descent in fetal life. Is a ligand for LGR8 receptor.; . TISSUE SPECIFICITY: Expressed in prenatal and postnatal Leydig cells. Found as well in the corpus luteum, trophoblast, fetal membranes and breast. {ECO:0000269|PubMed:7852540}.; unclassifiable (Anatomical System);medulla oblongata;placenta;testis; dorsal root ganglion;superior cervical ganglion;testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;testis;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.53725 0.11314 0.077132183 59.19438547 10.5625 0.38302 INSL4 2.05845917461986e-05 0.155293538811718 0.844685876596536 insulin like 4 FUNCTION: May play an important role in trophoblast development and in the regulation of bone formation.; . TISSUE SPECIFICITY: Expressed in placenta, uterus and in fetal perichondrium. Expression levels were increased in both early placentas and molar pregnancies and were reduced in choriocarcinoma cells. {ECO:0000269|PubMed:12414911, ECO:0000269|PubMed:9740319}.; whole body;ovary;placenta;liver;parathyroid;spleen; dorsal root ganglion;superior cervical ganglion;placenta; 0.15687 0.11117 0.705562627 85.52724699 52.14148 1.42753 INSL5 1.51756497878115e-05 0.131254989990159 0.868729834360053 insulin like 5 FUNCTION: May have a role in gut contractility or in thymic development and regulation. Activates RXFP4 with high potency and appears to be the endogenous ligand for this receptor.; . TISSUE SPECIFICITY: Highly expressed in rectum with lower levels in uterus and ascending and descending colon. {ECO:0000269|PubMed:10458910}.; . . 0.16210 0.16410 0.325313577 73.11276244 12.28435 0.44481 INSL6 4.56932984256453e-05 0.238162739418375 0.7617915672832 insulin like 6 FUNCTION: May have a role in sperm development and fertilization.; . TISSUE SPECIFICITY: Testis specific.; . . 0.07598 0.08456 0.553050905 81.54635527 605.09048 4.97883 INSM1 . . . insulinoma associated 1 FUNCTION: Sequence-specific DNA-binding transcriptional regulator that plays a key role in neurogenesis and neuroendocrine cell differentiation during embryonic and/or fetal development. Binds to the consensus sequence 5'-[TG][TC][TC][TT][GA]GGG[CG]A-3' in target promoters. Acts as a transcriptional repressor of NEUROD1 and INS expression via its interaction with cyclin CCND1 in a cell cycle-independent manner. Negatively regulates skeletal muscle- specific gene expression in endocrine cells of the pituitary by inhibiting the Notch signaling pathway. Represses target gene transcription by recruiting chromatin-modifying factors, such as HDAC1, HDAC2, HDAC3, KDM1A and RCOR1 histone deacetylases. Binds to its own promoter, suggesting autoregulation as a self-control feedback mechanism. Promotes the generation and expansion of neuronal basal progenitor cells in the developing neocortex. Involved in the differentiation of endocrine cells of the developing anterior pituitary gland, of the pancreas and intestine, and of sympatho-adrenal cells in the peripheral nervous system. Promotes cell cycle signaling arrest and inhibition of cellular proliferation. {ECO:0000269|PubMed:11842116, ECO:0000269|PubMed:16511571, ECO:0000269|PubMed:16569215, ECO:0000269|PubMed:18417529, ECO:0000269|PubMed:19124461}.; . TISSUE SPECIFICITY: Expressed in pancreatic duct cells. Expressed in several tumor cell lines of neuroendocrine origin including pheochromocytoma, medullary thyroid carcinoma, insulinoma, medulloblastoma, retinoblastoma, pheochromacytoma, medullary thyroid carcinoma and small cell lung carcinoma. {ECO:0000269|PubMed:12890672, ECO:0000269|PubMed:1634555}.; unclassifiable (Anatomical System);heart;islets of Langerhans;colon;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;lung;macula lutea;testis;germinal center;brain; fetal brain;cerebellum peduncles;beta cell islets;caudate nucleus;pons;trigeminal ganglion;pituitary;cerebellum; 0.12559 . . . 21.6187 0.72684 INSM2 . . . insulinoma-associated 2 FUNCTION: May function as a growth suppressor or tumor suppressor in liver cells and in certain neurons. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in heart, liver, skeletal muscle, kidney and pancreas, and, to a lesser extent, in brain, lung and spleen. In the pancreas, expressed in islet cells, including insulin- and glucagon-producing alpha- and beta-cells, but not in acinar cells (at protein level). Detected in adrenal glands, particularly in the deeper layer of the cortex (at protein level). {ECO:0000269|PubMed:21343251}.; unclassifiable (Anatomical System);brain;retina; . 0.15639 0.10520 0.283038099 71.26680821 140.55953 2.58625 INSR 0.186547844102196 0.813452149088413 6.8093906227771e-09 insulin receptor FUNCTION: Receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as docking proteins for other signaling proteins that contain Src- homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosines residues, including the p85 regulatory subunit of PI3K and SHP2. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway, which is responsible for most of the metabolic actions of insulin, and the Ras-MAPK pathway, which regulates expression of some genes and cooperates with the PI3K pathway to control cell growth and differentiation. Binding of the SH2 domains of PI3K to phosphotyrosines on IRS1 leads to the activation of PI3K and the generation of phosphatidylinositol-(3, 4, 5)-triphosphate (PIP3), a lipid second messenger, which activates several PIP3-dependent serine/threonine kinases, such as PDPK1 and subsequently AKT/PKB. The net effect of this pathway is to produce a translocation of the glucose transporter SLC2A4/GLUT4 from cytoplasmic vesicles to the cell membrane to facilitate glucose transport. Moreover, upon insulin stimulation, activated AKT/PKB is responsible for: anti- apoptotic effect of insulin by inducing phosphorylation of BAD; regulates the expression of gluconeogenic and lipogenic enzymes by controlling the activity of the winged helix or forkhead (FOX) class of transcription factors. Another pathway regulated by PI3K- AKT/PKB activation is mTORC1 signaling pathway which regulates cell growth and metabolism and integrates signals from insulin. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 thereby activating mTORC1 pathway. The Ras/RAF/MAP2K/MAPK pathway is mainly involved in mediating cell growth, survival and cellular differentiation of insulin. Phosphorylated IRS1 recruits GRB2/SOS complex, which triggers the activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to binding insulin, the insulin receptor can bind insulin-like growth factors (IGFI and IGFII). Isoform Short has a higher affinity for IGFII binding. When present in a hybrid receptor with IGF1R, binds IGF1. PubMed:12138094 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, PubMed:16831875 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin. {ECO:0000269|PubMed:12138094, ECO:0000269|PubMed:16314505, ECO:0000269|PubMed:16831875, ECO:0000269|PubMed:8257688, ECO:0000269|PubMed:8276809, ECO:0000269|PubMed:8452530, ECO:0000269|PubMed:9428692}.; DISEASE: Rabson-Mendenhall syndrome (RMS) [MIM:262190]: Severe insulin resistance syndrome characterized by insulin-resistant diabetes mellitus with pineal hyperplasia and somatic abnormalities. Typical features include coarse, senile-appearing facies, dental and skin abnormalities, abdominal distension, and phallic enlargement. Inheritance is autosomal recessive. {ECO:0000269|PubMed:10443650, ECO:0000269|PubMed:12023989, ECO:0000269|PubMed:17201797, ECO:0000269|PubMed:2365819, ECO:0000269|PubMed:8314008}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leprechaunism (LEPRCH) [MIM:246200]: Represents the most severe form of insulin resistance syndrome, characterized by intrauterine and postnatal growth retardation and death in early infancy. Inheritance is autosomal recessive. {ECO:0000269|PubMed:12538626, ECO:0000269|PubMed:12970295, ECO:0000269|PubMed:1607067, ECO:0000269|PubMed:1730625, ECO:0000269|PubMed:2365819, ECO:0000269|PubMed:2479553, ECO:0000269|PubMed:2834824, ECO:0000269|PubMed:7538143, ECO:0000269|PubMed:7815442, ECO:0000269|PubMed:8188715, ECO:0000269|PubMed:8326490, ECO:0000269|PubMed:8419945, ECO:0000269|PubMed:8636294, ECO:0000269|PubMed:9249867, ECO:0000269|PubMed:9703342}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:1470163, ECO:0000269|PubMed:1607076, ECO:0000269|PubMed:7657032}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Familial hyperinsulinemic hypoglycemia 5 (HHF5) [MIM:609968]: Familial hyperinsulinemic hypoglycemia [MIM:256450], also referred to as congenital hyperinsulinism, nesidioblastosis, or persistent hyperinsulinemic hypoglycemia of infancy (PPHI), is the most common cause of persistent hypoglycemia in infancy and is due to defective negative feedback regulation of insulin secretion by low glucose levels. {ECO:0000269|PubMed:15161766}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Insulin-resistant diabetes mellitus with acanthosis nigricans type A (IRAN type A) [MIM:610549]: Characterized by the association of severe insulin resistance (manifested by marked hyperinsulinemia and a failure to respond to exogenous insulin) with the skin lesion acanthosis nigricans and ovarian hyperandrogenism in adolescent female subjects. Women frequently present with hirsutism, acne, amenorrhea or oligomenorrhea, and virilization. This syndrome is different from the type B that has been demonstrated to be secondary to the presence of circulating autoantibodies against the insulin receptor. {ECO:0000269|PubMed:10733238, ECO:0000269|PubMed:11260230, ECO:0000269|PubMed:12107746, ECO:0000269|PubMed:12970295, ECO:0000269|PubMed:1563582, ECO:0000269|PubMed:1963473, ECO:0000269|PubMed:2002058, ECO:0000269|PubMed:2168397, ECO:0000269|PubMed:2365819, ECO:0000269|PubMed:2544998, ECO:0000269|PubMed:3283938, ECO:0000269|PubMed:8243830, ECO:0000269|PubMed:8288049, ECO:0000269|PubMed:8314008, ECO:0000269|PubMed:8388389, ECO:0000269|PubMed:9175790}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform Long and isoform Short are predominantly expressed in tissue targets of insulin metabolic effects: liver, adipose tissue and skeletal muscle but are also expressed in the peripheral nerve, kidney, pulmonary alveoli, pancreatic acini, placenta vascular endothelium, fibroblasts, monocytes, granulocytes, erythrocytes and skin. Isoform Short is preferentially expressed in fetal cells such as fetal fibroblasts, muscle, liver and kidney. Found as a hybrid receptor with IGF1R in muscle, heart, kidney, adipose tissue, skeletal muscle, hepatoma, fibroblasts, spleen and placenta (at protein level). Overexpressed in several tumors, including breast, colon, lung, ovary, and thyroid carcinomas. {ECO:0000269|PubMed:10207053, ECO:0000269|PubMed:2369896, ECO:0000269|PubMed:9202395, ECO:0000269|PubMed:9355755}.; ovary;colon;parathyroid;uterus;prostate;frontal lobe;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;lung;epididymis;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;pancreas;ovary;placenta;adrenal cortex;ciliary ganglion;atrioventricular node; 0.99973 0.94105 -2.140595475 1.492097193 141.47735 2.59553 INSRR 4.91565760465697e-07 0.999920299072368 7.92093618710879e-05 insulin receptor-related receptor FUNCTION: Receptor with tyrosine-protein kinase activity. Functions as a pH sensing receptor which is activated by increased extracellular pH. Activates an intracellular signaling pathway that involves IRS1 and AKT1/PKB. {ECO:0000269|PubMed:21641549}.; . . . . 0.62339 0.19592 -2.250890405 1.279782968 1815.11428 7.85768 INTS1 0.22412137484881 0.775878624960276 1.9091396689623e-10 integrator complex subunit 1 FUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes.; . . . . 0.15585 . -5.050633482 0.070771408 422.05224 4.29253 INTS2 0.999806217287338 0.000193782712336114 3.25408414087654e-13 integrator complex subunit 2 FUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes.; . . unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;skin;bone marrow;uterus;lung;alveolus;testis;germinal center;brain;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.77276 0.13043 -0.620857637 17.3566879 100.80715 2.17423 INTS3 0.999997023490929 2.97650907139141e-06 1.24357357741247e-17 integrator complex subunit 3 FUNCTION: Component of the Integrator complex. The Integrator complex is involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes.; . . ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.51743 0.13588 -1.287751345 5.03066761 26.14611 0.84795 INTS4 0.653071264464616 0.346928651216061 8.43193231679031e-08 integrator complex subunit 4 FUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes.; . . ovary;colon;parathyroid;choroid;vein;skin;bone marrow;uterus;frontal lobe;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;muscle;blood;breast;lung;placenta;liver;spleen;head and neck;cervix;mammary gland;stomach;aorta;cerebellum; . 0.16947 0.15282 -0.576764155 18.7839113 270.96358 3.52905 INTS4P1 . . . integrator complex subunit 4 pseudogene 1 . . . . . . . . . . . INTS4P2 . . . integrator complex subunit 4 pseudogene 2 . . . . . . . . . . . INTS5 0.999284368233793 0.000715627084442681 4.68176438406897e-09 integrator complex subunit 5 FUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes.; . . smooth muscle;ovary;umbilical cord;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cerebral cortex;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;liver;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cerebellum; 0.31626 0.12936 -0.971800989 8.946685539 92.50703 2.06784 INTS6 0.999996534735088 3.46526490164628e-06 1.074341730973e-14 integrator complex subunit 6 FUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. May have a tumor suppressor role; an ectopic expression suppressing tumor cell growth. {ECO:0000269|PubMed:15254679, ECO:0000269|PubMed:16239144}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:10467397}.; medulla oblongata;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;cerebellum cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.33292 0.17111 -0.867014353 10.72776598 40.90814 1.19861 INTS6-AS1 . . . INTS6 antisense RNA 1 . . . . . . . . . . . INTS6L . . . integrator complex subunit 6 like . . . . . 0.47840 0.09573 -0.067881249 48.69072895 . . INTS6L-AS1 . . . INTS6L antisense RNA 1 . . . . . . . . . . . INTS6P1 . . . integrator complex subunit 6 pseudogene 1 . . . . . . . . . . . INTS7 0.860980155121656 0.139019695607453 1.49270891142183e-07 integrator complex subunit 7 FUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Plays a role in DNA damage response (DDR) signaling during the S phase. {ECO:0000269|PubMed:21659603}.; . . . . 0.48825 . -0.512444034 21.55579146 128.53173 2.47098 INTS8 0.989948635386659 0.0100513645722156 4.11252566098957e-11 integrator complex subunit 8 FUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes.; . . ovary;salivary gland;developmental;intestine;colon;retina;prostate;whole body;cochlea;larynx;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;aorta;stomach; testis - interstitial;testis - seminiferous tubule;testis;white blood cells; 0.15044 0.13190 -0.574945567 18.90186365 90.45229 2.04680 INTS9 2.00066301787045e-06 0.971022759397708 0.028975239939274 integrator complex subunit 9 FUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes.; . . . . 0.18626 0.12663 -0.821100135 11.88369899 44.57866 1.27954 INTS10 0.984216594645776 0.0157833903291012 1.50251230851757e-08 integrator complex subunit 10 FUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes.; . . . . 0.11928 0.13453 -0.50880549 21.72682236 66.87523 1.68846 INTS12 0.687399443679649 0.311721065511513 0.000879490808837345 integrator complex subunit 12 FUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes.; . . smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pia mater;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach; testis - interstitial;atrioventricular node; 0.68398 0.11985 -0.404032746 26.53338051 28.48702 0.91240 INTU 3.66142698703447e-07 0.985898608362729 0.0141010254945725 inturned planar cell polarity protein FUNCTION: Plays a key role in ciliogenesis and embryonic development. Regulator of cilia formation by controlling the organization of the apical actin cytoskeleton and the positioning of the basal bodies at the apical cell surface, which in turn is essential for the normal orientation of elongating ciliary microtubules. Plays a key role in definition of cell polarity via its role in ciliogenesis but not via conversion extension. Has an indirect effect on hedgehog signaling (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;skeletal muscle;uterus;whole body;lung;endometrium;bone;hippocampus;liver;testis;brain;aorta;peripheral nerve; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skin; 0.10500 0.22276 -0.527216948 20.8893607 180.27164 2.91672 INVS 1.44663483353059e-06 0.99958819951557 0.000410353849596945 inversin FUNCTION: Required for normal renal development and establishment of left-right axis. Probably acts as a molecular switch between different Wnt signaling pathways. Inhibits the canonical Wnt pathway by targeting cytoplasmic disheveled (DVL1) for degradation by the ubiquitin-proteasome. This suggests that it is required in renal development to oppose the repression of terminal differentiation of tubular epithelial cells by Wnt signaling. Involved in the organization of apical junctions in kidney cells together with NPHP1, NPHP4 and RPGRIP1L/NPHP8 (By similarity). Does not seem to be strictly required for ciliogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:15852005, ECO:0000269|PubMed:18371931}.; DISEASE: Nephronophthisis 2 (NPHP2) [MIM:602088]: An autosomal recessive disorder resulting in end-stage renal disease. It is characterized by early onset and rapid progression. Phenotypic manifestations include enlarged kidneys, chronic tubulo- interstitial nephritis, anemia, hyperkalemic metabolic acidosis. Some patients also display situs inversus. Pathologically, it differs from later-onset nephronophthisis by the absence of medullary cysts and thickened tubular basement membranes, and by the presence of cortical microcysts. {ECO:0000269|PubMed:12872123}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Strongly expressed in the primary cilia of renal tubular cells. {ECO:0000269|PubMed:11935322, ECO:0000269|PubMed:12872123}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;colon;parathyroid;blood;fovea centralis;choroid;lens;skin;retina;bone marrow;bile duct;prostate;optic nerve;whole body;lung;placenta;macula lutea;testis;kidney;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.50921 0.21466 -0.569494998 19.04340646 234.27423 3.30759 IP6K1 0.235179980766781 0.757599326683381 0.00722069254983779 inositol hexakisphosphate kinase 1 FUNCTION: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4.; . . myocardium;ovary;sympathetic chain;colon;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;thymus; amygdala;whole brain;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.67586 0.11137 -0.203796826 38.81811748 39.28853 1.16277 IP6K2 0.989457702873501 0.0105389713616068 3.3257648926771e-06 inositol hexakisphosphate kinase 2 FUNCTION: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4. {ECO:0000269|PubMed:10574768}.; . . smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;germinal center;brain;heart;cartilage;blood;lens;skeletal muscle;breast;visual apparatus;liver;cervix;spleen;mammary gland;colon;parathyroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;olfactory bulb;testis - seminiferous tubule;cerebellum peduncles;testis;pons;atrioventricular node;cerebellum; 0.27477 0.08863 0.240763792 69.36777542 62.53795 1.61570 IP6K3 0.0485338526527661 0.928358834177403 0.0231073131698315 inositol hexakisphosphate kinase 3 FUNCTION: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4. {ECO:0000269|PubMed:11502751}.; . TISSUE SPECIFICITY: Detected in brain.; unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;optic nerve;lung;placenta;macula lutea;liver;spleen;germinal center;kidney;gall bladder; . 0.41021 0.09035 0.712836712 85.76315169 559.88619 4.80622 IPCEF1 0.399940590099527 0.59967368427699 0.000385725623483231 interaction protein for cytohesin exchange factors 1 FUNCTION: Enhances the promotion of guanine-nucleotide exchange by PSCD2 on ARF6 in a concentration-dependent manner. {ECO:0000250}.; . . unclassifiable (Anatomical System);amygdala;lymph node;cartilage;colon;blood;skeletal muscle;bone marrow;pancreas;prostate;frontal lobe;endometrium;nasopharynx;placenta;thyroid;kidney;brain;aorta; occipital lobe;subthalamic nucleus;medulla oblongata;thalamus;superior cervical ganglion;thyroid;temporal lobe;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; . . 0.328949044 73.41354093 57.76721 1.53559 IPMK 0.426106181687242 0.572340293239385 0.00155352507337262 inositol polyphosphate multikinase FUNCTION: Inositol phosphate kinase with a broad substrate specificity. Has a preference for inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) and inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4). {ECO:0000269|PubMed:12027805, ECO:0000269|PubMed:12223481}.; . TISSUE SPECIFICITY: Ubiquitous, with the highest expression in skeletal muscle, liver, placenta, lung, peripheral blood leukocytes, kidney, spleen and colon. {ECO:0000269|PubMed:12223481}.; . . 0.50963 0.09415 0.062575634 58.74026893 1147.67485 6.45706 IPMKP1 . . . inositol polyphosphate multikinase pseudogene 1 . . . . . . . . . . . IPO4 3.22469522365963e-06 0.999970484761316 2.62905434604313e-05 importin 4 FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of RPS3A. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. {ECO:0000250, ECO:0000269|PubMed:11823430}.; . . lymphoreticular;ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.35939 0.27606 -0.455627566 23.72611465 4610.80458 13.63441 IPO5 0.999998736678014 1.2633219858407e-06 3.76607492264734e-17 importin 5 FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. {ECO:0000250, ECO:0000269|PubMed:9687515}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;ciliary body;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;lung;mesenchyma;adrenal gland;placenta;head and neck;kidney;stomach;aorta; occipital lobe;testis - interstitial;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;cingulate cortex;parietal lobe; 0.97485 0.23683 -0.909290275 10.03184713 1001.72714 6.09631 IPO5P1 . . . importin 5 pseudogene 1 . . . . . . . . . . . IPO7 0.999998374732842 1.62526715768435e-06 3.43798220430327e-16 importin 7 FUNCTION: Functions in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with the importin-beta subunit KPNB1. Acting autonomously, is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with KPNB1 mediates the nuclear import of H1 histone and the Ran-binding site of IPO7 is not required but synergizes with that of KPNB1 in importin/substrate complex dissociation. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In vitro, mediates the nuclear import of HIV-1 reverse transcription complex (RTC) integrase. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. {ECO:0000269|PubMed:10228156, ECO:0000269|PubMed:12853482, ECO:0000269|PubMed:9687515}.; . . . . 0.84877 0.28646 -0.712684326 14.49634348 29.04313 0.92887 IPO7P1 . . . importin 7 pseudogene 1 . . . . . . . . . . . IPO7P2 . . . importin 7 pseudogene 2 . . . . . . . . . . . IPO8 0.97978380275245 0.0202161972012216 4.63284429558816e-11 importin 8 FUNCTION: Seems to function in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter- like protein in association with the importin-beta subunit KPNB1. Acting autonomously, is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro mediates the nuclear import of SRP19. {ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:9214382}.; . . unclassifiable (Anatomical System);lymphoreticular;heart;colon;skeletal muscle;prostate;lung;frontal lobe;placenta;thyroid;liver;spleen;germinal center;kidney;brain;stomach; superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion; 0.26379 0.17520 -0.907472583 10.07313046 130.85275 2.49143 IPO8P1 . . . importin 8 pseudogene 1 . . . . . . . . . . . IPO9 0.999992154750332 7.8452496646608e-06 3.21907575057543e-15 importin 9 FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of H2B histone (By similarity), RPS7 and RPL18A. Prevents the cytoplasmic aggregation of RPS7 and RPL18A by shielding exposed basic domains. May also import H2A, H3, H4 histones (By similarity), RPL4 and RPL6. {ECO:0000250, ECO:0000269|PubMed:11823430}.; . . ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;hypothalamus;muscle;pharynx;blood;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; amygdala;dorsal root ganglion;medulla oblongata;subthalamic nucleus;occipital lobe;cerebellum peduncles;prefrontal cortex;globus pallidus;atrioventricular node;trigeminal ganglion;cerebellum; 0.96730 0.33532 -1.287751345 5.03066761 43.92975 1.26258 IPO9-AS1 . . . IPO9 antisense RNA 1 . . . . . . . . . . . IPO11 0.996456954689181 0.00354304530760569 3.21337498626115e-12 importin 11 FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of UBE2E3, and of RPL12 (By similarity). {ECO:0000250, ECO:0000269|PubMed:11032817}.; . . ovary;sympathetic chain;colon;vein;skin;uterus;prostate;whole body;oesophagus;endometrium;bone;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;cervix;kidney; trigeminal ganglion; 0.69666 0.11055 -0.529034136 20.85987261 87.81015 2.00150 IPO13 0.972444338181171 0.0275556593866226 2.43220623083350e-09 importin 13 FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of UBC9, the RBM8A/MAGOH complex, PAX6 and probably other members of the paired homeobox family. Also mediates nuclear export of eIF-1A, and the cytoplasmic release of eIF-1A is triggered by the loading of import substrates onto IPO13. {ECO:0000250, ECO:0000269|PubMed:11447110, ECO:0000269|PubMed:15143176}.; . TISSUE SPECIFICITY: Expressed in fetal brain, heart, intestine and kidney. {ECO:0000269|PubMed:10745026}.; . . 0.69236 0.27035 -1.219785504 5.602736494 32.31894 1.01049 IPP 0.00253170996710155 0.994288980215481 0.00317930981741747 intracisternal A particle-promoted polypeptide FUNCTION: May play a role in organizing the actin cytoskeleton.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;lung;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;stomach; superior cervical ganglion;adrenal cortex;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10497 0.20305 -0.534490515 20.70063694 3153.34315 10.68608 IPPK 0.973790826181443 0.0262078923052992 1.28151325790516e-06 inositol-pentakisphosphate 2-kinase FUNCTION: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). InsP6 is involved in many processes such as mRNA export, non-homologous end-joining, endocytosis, ion channel regulation. It also protects cells from TNF-alpha-induced apoptosis. {ECO:0000269|PubMed:12084730, ECO:0000269|PubMed:15967797}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with high expression in heart, brain, testis and placenta. {ECO:0000269|PubMed:12084730}.; ovary;colon;fovea centralis;skin;uterus;prostate;endometrium;larynx;testis;germinal center;brain;artery;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.08903 0.11910 -0.023789244 52.09365416 659.85423 5.14987 IPPKP1 . . . inositol 1,3,4,5,6-pentakisphosphate 2-kinase pseudogene 1 . . . . . . . . . . . IPW . . . imprinted in Prader-Willi syndrome (non-protein coding) . . . . . . . . . . . IQCA1 0.00138117063159793 0.998305037306357 0.000313792062045218 IQ motif containing with AAA domain 1 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;cerebellum cortex;tongue;parathyroid;skin;uterus;prostate;lung;frontal lobe;larynx;nasopharynx;thyroid;placenta;pituitary gland;testis;head and neck;kidney;brain; atrioventricular node;skeletal muscle; 0.09290 0.09815 0.958999345 90.17456947 720.11382 5.32715 IQCA1-AS1 . . . IQCA1 antisense RNA 1 . . . . . . . . . . . IQCA1L . . . IQ motif containing with AAA domain 1 like . . . . . . . . . . . IQCB1 1.19705337503096e-07 0.985796860967368 0.0142030193272948 IQ motif containing B1 FUNCTION: Involved in ciliogenesis. {ECO:0000250}.; DISEASE: Senior-Loken syndrome 5 (SLSN5) [MIM:609254]: A renal- retinal disorder characterized by progressive wasting of the filtering unit of the kidney (nephronophthisis), with or without medullary cystic renal disease, and progressive eye disease. Typically this disorder becomes apparent during the first year of life. {ECO:0000269|PubMed:15723066}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed in fetal and adult tissues. Localized to the outer segments and connecting cilia of photoreceptor cells. Up-regulated in a number of primary colorectal and gastric tumors. {ECO:0000269|PubMed:15723066, ECO:0000269|PubMed:16322217}.; lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;skin;bone marrow;uterus;prostate;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.16973 0.17555 0.598963042 82.7789573 3536.66111 11.47062 IQCB2P . . . IQ motif containing B2 pseudogene . . . . . . . . . . . IQCC 2.25735733275782e-07 0.700252767560675 0.299747006703592 IQ motif containing C . . . unclassifiable (Anatomical System);uterus;prostate;frontal lobe;ovary;placenta;adrenal cortex;duodenum;cervix;brain; trigeminal ganglion; 0.04563 . 7.61E-05 53.98089172 1208.56981 6.58260 IQCD 7.66417947056825e-06 0.166256402788168 0.833735933032362 IQ motif containing D . . . unclassifiable (Anatomical System);lymph node;lung; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node;skin;skeletal muscle; 0.09845 . -0.312207497 32.05944798 184.29693 2.94638 IQCE 1.34472559079011e-25 7.40063906317543e-05 0.999925993609368 IQ motif containing E . . . unclassifiable (Anatomical System);heart;islets of Langerhans;colon;skin;uterus;optic nerve;lung;placenta;bone;testis;kidney;brain;stomach; testis - interstitial;superior cervical ganglion;fetal brain;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;atrioventricular node; 0.33418 0.09979 1.412766531 94.81599434 3894.51997 12.31004 IQCF1 0.0468541004756609 0.854881655977566 0.0982642435467734 IQ motif containing F1 FUNCTION: Involved in sperm capacitation and acrosome reaction. {ECO:0000250|UniProtKB:Q9D9K8}.; . . unclassifiable (Anatomical System);lung;hippocampus;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node; 0.08067 . 0.637604436 83.77565464 261.88841 3.47237 IQCF2 0.000296978107855683 0.568359303247969 0.431343718644176 IQ motif containing F2 . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.16033 . 0.503505267 79.88912479 91.61416 2.05820 IQCF3 0.127529596598468 0.780175280640993 0.0922951227605388 IQ motif containing F3 . . . . . . . 0.016664174 55.21939137 5.41422 0.20017 IQCF5 0.433199985636479 0.45952414045522 0.107275873908302 IQ motif containing F5 . . . . . . . 0.635788962 83.63411182 73.46 1.79122 IQCF5-AS1 . . . IQCF5 antisense RNA 1 . . . . . . . . . . . IQCF6 . . . IQ motif containing F6 . . . . . . . 0.812172405 87.75654636 1901.78976 8.02210 IQCG 3.61162236640437e-15 0.00287274971809736 0.997127250281899 IQ motif containing G . . . unclassifiable (Anatomical System);medulla oblongata;heart;colon;skin;bone marrow;uterus;lung;endometrium;larynx;adrenal gland;nasopharynx;bone;placenta;visual apparatus;testis;head and neck;brain; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;skin; 0.07281 0.07186 -0.023789244 52.09365416 3192.41973 10.76745 IQCH 2.69347323550457e-12 0.863657894471718 0.136342105525589 IQ motif containing H FUNCTION: May play a regulatory role in spermatogenesis. {ECO:0000269|PubMed:15897968}.; . TISSUE SPECIFICITY: Expressed in fetal and adult testis, in germ cells but not somatic cells. {ECO:0000269|PubMed:15897968}.; unclassifiable (Anatomical System);breast;uterus;medulla oblongata;lung;heart;thyroid;testis;brain;skin; testis - interstitial;superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion;parietal lobe; 0.36739 . -0.415165735 25.83746167 166.12327 2.81959 IQCH-AS1 . . . IQCH antisense RNA 1 . . . . . . . . . . . IQCJ 0.0984293652546805 0.866584162482585 0.0349864722627346 IQ motif containing J . . . . . 0.50682 . 0.103030231 61.2762444 0.65839 0.01023 IQCJ-SCHIP1 0.66050205956069 0.339451009810719 4.69306285918248e-05 IQCJ-SCHIP1 readthrough . . TISSUE SPECIFICITY: Isoform 5 and isoform 6 are highly expressed in the brain. Both isoforms derive from naturally occurring readthrough transcripts which produce IQCJ-SCHIP1 fusion proteins. {ECO:0000269|PubMed:17045569}.; unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;spinal cord;colon;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;lung;frontal lobe;placenta;bone;macula lutea;hippocampus;liver;testis;kidney;brain;stomach; . . . 0.060756528 58.52795471 82.52457 1.92888 IQCJ-SCHIP1-AS1 . . . IQCJ-SCHIP1 readthrough antisense RNA 1 . . . . . . . . . . . IQCK 0.0539326256943501 0.926313793670047 0.0197535806356027 IQ motif containing K . . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;thyroid;testis;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;macula lutea;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.25643 . 0.61555716 83.13871196 3811.72566 12.13593 IQGAP1 0.999976584550565 2.34154494354504e-05 6.41423432263871e-19 IQ motif containing GTPase activating protein 1 FUNCTION: Binds to activated CDC42 but does not stimulate its GTPase activity. It associates with calmodulin. Could serve as an assembly scaffold for the organization of a multimolecular complex that would interface incoming signals to the reorganization of the actin cytoskeleton at the plasma membrane. May promote neurite outgrowth. {ECO:0000269|PubMed:15695813}.; . TISSUE SPECIFICITY: Expressed in the placenta, lung, and kidney. A lower level expression is seen in the heart, liver, skeletal muscle and pancreas.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;gum;thyroid;amniotic fluid;germinal center;brain;bladder;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;larynx;bone;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;oral cavity;bile duct;pancreas;pia mater;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; uterus;superior cervical ganglion;ciliary ganglion;white blood cells;atrioventricular node;whole blood;trigeminal ganglion;fetal thyroid;skeletal muscle; 0.48921 0.29132 -1.232771118 5.537862703 137.51113 2.55135 IQGAP2 4.102950079501e-15 0.999751468473198 0.000248531526797701 IQ motif containing GTPase activating protein 2 FUNCTION: Binds to activated CDC42 and RAC1 but does not seem to stimulate their GTPase activity. Associates with calmodulin.; . TISSUE SPECIFICITY: Isoform 2 expression is enhanced in testis.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;cochlea;oesophagus;endometrium;larynx;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;islets of Langerhans;spinal cord;adrenal cortex;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach; fetal liver;superior cervical ganglion; 0.55958 0.25212 0.394900016 76.06157113 2834.87764 10.05992 IQGAP3 6.47051186060707e-16 0.999970782133491 2.9217866508624e-05 IQ motif containing GTPase activating protein 3 . . . unclassifiable (Anatomical System);lymph node;ovary;colon;blood;skin;bone marrow;breast;uterus;whole body;lung;larynx;bone;thyroid;testis;head and neck;germinal center;kidney;brain;mammary gland;stomach; subthalamic nucleus;testis - interstitial;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.22954 0.22033 -0.376786957 28.01958009 7742.20989 18.98627 IQSEC1 0.998506226942054 0.00149377190565318 1.15229268695012e-09 IQ motif and Sec7 domain 1 FUNCTION: Guanine nucleotide exchange factor for ARF1 and ARF6 (PubMed:24058294). Guanine nucleotide exchange factor activity is enhanced by lipid binding (PubMed:24058294). Accelerates GTP binding by ARFs of all three classes. Guanine nucleotide exchange protein for ARF6, mediating internalisation of beta-1 integrin. {ECO:0000269|PubMed:11226253, ECO:0000269|PubMed:16461286, ECO:0000269|PubMed:24058294}.; . TISSUE SPECIFICITY: Expressed in brain, ovary, heart, lung, liver, kidney and leukocytes. Moderate expression was also detected in lung, skeletal muscle, placenta, small intestine, pancreas, spleen and testis. {ECO:0000269|PubMed:11226253, ECO:0000269|PubMed:9872452}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;cerebellum; whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;cerebellum peduncles;temporal lobe;pons;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.20877 0.11731 -1.256630467 5.343241331 1214.79399 6.59475 IQSEC2 0.975390479204391 0.0246041031978036 5.41759780523116e-06 IQ motif and Sec7 domain 2 . . TISSUE SPECIFICITY: Expressed in brain, kidney and small intestine. Weakly expressed in placenta, pancreas, ovary, prostate and liver. {ECO:0000269|PubMed:9628581}.; . . 0.71095 0.09221 -0.516085732 21.20193442 76.29612 1.83098 IQSEC3 0.925104239220891 0.0748950318626797 7.28916429416534e-07 IQ motif and Sec7 domain 3 FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for ARF1. {ECO:0000269|PubMed:17981261}.; . TISSUE SPECIFICITY: Expressed specifically in the adult brain, predominantly in the cerebral cortex and the olfactory bulb, but not in the fetal brain. Expressed only in mature neurons, but not in undifferentiated neural stem precursor cells (NSPCs), nor in glioma cells. {ECO:0000269|PubMed:17981261}.; unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;optic nerve;whole body;lung;frontal lobe;larynx;macula lutea;testis;head and neck;kidney;brain;stomach;cerebellum; amygdala;whole brain;occipital lobe;medulla oblongata;cerebellum peduncles;temporal lobe;pons;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.52569 . -0.839512508 11.40009436 1171.33568 6.50545 IQSEC3P1 . . . IQ motif and Sec7 domain 3 pseudogene 1 . . . . . . . . . . . IQSEC3P2 . . . IQ motif and Sec7 domain 3 pseudogene 2 . . . . . . . . . . . IQSEC3P3 . . . IQ motif and Sec7 domain 3 pseudogene 3 . . . . . . . . . . . IQUB 3.23577428041204e-13 0.0759276946597718 0.924072305339904 IQ motif and ubiquitin domain containing FUNCTION: May play roles in cilia formation and/or maintenance. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;ovary;placenta;testis;parathyroid;kidney; subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.06897 0.08445 0.005534202 54.09884407 248.48433 3.39696 IRAIN . . . IGF1R antisense imprinted non-protein coding RNA . . . . . . . . . . . IRAK1 0.994301923500418 0.0056973383024823 7.38197099837815e-07 interleukin 1 receptor associated kinase 1 FUNCTION: Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor- signaling complex upon TLR activation. Association with MYD88 leads to IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates the interferon regulatory factor 7 (IRF7) to induce its activation and translocation to the nucleus, resulting in transcriptional activation of type I IFN genes, which drive the cell in an antiviral state. When sumoylated, translocates to the nucleus and phosphorylates STAT3. {ECO:0000269|PubMed:11397809, ECO:0000269|PubMed:12860405, ECO:0000269|PubMed:14684752, ECO:0000269|PubMed:15084582, ECO:0000269|PubMed:15465816, ECO:0000269|PubMed:15767370, ECO:0000269|PubMed:17997719, ECO:0000269|PubMed:20400509}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are ubiquitously expressed in all tissues examined, with isoform 1 being more strongly expressed than isoform 2. {ECO:0000269|PubMed:11397809}.; . . 0.17579 0.59389 0.687150476 85.17928757 144.97421 2.62306 IRAK1BP1 0.000864773844343313 0.791096560370248 0.208038665785409 interleukin 1 receptor associated kinase 1 binding protein 1 FUNCTION: Component of the IRAK1-dependent TNFRSF1A signaling pathway that leads to NF-kappa-B activation and is required for cell survival. Acts by enhancing RELA transcriptional activity (By similarity). {ECO:0000250}.; . . . . 0.10237 0.11227 0.238945317 69.20853975 101.047 2.17569 IRAK2 2.89785862103042e-08 0.735974656071015 0.264025314950399 interleukin 1 receptor associated kinase 2 FUNCTION: Binds to the IL-1 type I receptor following IL-1 engagement, triggering intracellular signaling cascades leading to transcriptional up-regulation and mRNA stabilization. {ECO:0000269|PubMed:10383454, ECO:0000269|PubMed:9374458}.; . TISSUE SPECIFICITY: Expressed in spleen, thymus, prostate, lung, liver, skeletal muscle, kidney, pancreas and peripheral blood leukocytes. {ECO:0000269|PubMed:9374458}.; unclassifiable (Anatomical System);lung;thyroid;liver;colon;cervix;spleen;brain; superior cervical ganglion;pancreas;trigeminal ganglion; 0.08234 0.17738 1.229050169 93.25902335 3567.96124 11.55238 IRAK3 3.58183663944626e-15 0.00550278642621449 0.994497213573782 interleukin 1 receptor associated kinase 3 FUNCTION: Inhibits dissociation of IRAK1 and IRAK4 from the Toll- like receptor signaling complex by either inhibiting the phosphorylation of IRAK1 and IRAK4 or stabilizing the receptor complex. {ECO:0000250|UniProtKB:Q8K4B2, ECO:0000269|PubMed:10383454}.; . TISSUE SPECIFICITY: Expressed predominantly in peripheral blood lymphocytes. {ECO:0000269|PubMed:10383454}.; lung;cartilage;endometrium;bone;placenta;testis;blood;brain;stomach;bone marrow; superior cervical ganglion; 0.12689 0.20924 -0.350843407 29.54116537 167.27542 2.82639 IRAK4 0.00057687169808497 0.974133033265918 0.0252900950359974 interleukin 1 receptor associated kinase 4 FUNCTION: Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways (PubMed:17878374). Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation to form the Myddosome together with IRAK2. Phosphorylates initially IRAK1, thus stimulating the kinase activity and intensive autophosphorylation of IRAK1. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino- mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA- IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates NCF1 and regulates NADPH oxidase activation after LPS stimulation suggesting a similar mechanism during microbial infections. {ECO:0000269|PubMed:11960013, ECO:0000269|PubMed:12538665, ECO:0000269|PubMed:15084582, ECO:0000269|PubMed:17217339, ECO:0000269|PubMed:17337443, ECO:0000269|PubMed:17878374, ECO:0000269|PubMed:17997719, ECO:0000269|PubMed:20400509, ECO:0000269|PubMed:24316379}.; DISEASE: Recurrent isolated invasive pneumococcal disease 1 (IPD1) [MIM:610799]: Recurrent invasive pneumococcal disease (IPD) is defined as two episodes of IPD occurring at least 1 month apart, whether caused by the same or different serotypes or strains. Recurrent IPD occurs in at least 2% of patients in most series, making IPD the most important known risk factor for subsequent IPD. {ECO:0000269|PubMed:16950813}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: IRAK4 deficiency (IRAK4D) [MIM:607676]: Causes extracellular pyogenic bacterial and fungal infections in otherwise healthy children. {ECO:0000269|PubMed:12637671, ECO:0000269|PubMed:12925671, ECO:0000269|PubMed:17878374, ECO:0000269|PubMed:19663824, ECO:0000269|PubMed:21057262, ECO:0000269|PubMed:24316379}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;ovary;colon;skin;skeletal muscle;prostate;whole body;endometrium;larynx;liver;testis;head and neck;spleen;germinal center;kidney;stomach;gall bladder; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05224 0.30207 -0.247889024 35.98726115 677.04206 5.19884 IREB2 0.999999730362402 2.69637598291087e-07 2.13753596112909e-17 iron responsive element binding protein 2 FUNCTION: RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'- UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA. {ECO:0000269|PubMed:7983023}.; . . colon;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.20840 0.31776 -0.837696902 11.45317292 83.73373 1.94797 IRF1 0.867788618113854 0.13213358607423 7.77958119156184e-05 interferon regulatory factor 1 FUNCTION: Transcriptional regulator which displays a remarkable functional diversity in the regulation of cellular responses. These include the regulation of IFN and IFN-inducible genes, host response to viral and bacterial infections, regulation of many genes expressed during hematopoiesis, inflammation, immune responses and cell proliferation and differentiation, regulation of the cell cycle and induction of growth arrest and programmed cell death following DNA damage. Stimulates both innate and acquired immune responses through the activation of specific target genes and can act as a transcriptional activator and repressor regulating target genes by binding to an interferon- stimulated response element (ISRE) in their promoters. Its target genes for transcriptional activation activity include: genes involved in anti-viral response, such as IFN-alpha/beta, DDX58/RIG-I, TNFSF10/TRAIL, OAS1/2, PIAS1/GBP, EIF2AK2/PKR and RSAD2/viperin; antibacterial response, such as NOS2/INOS; anti- proliferative response, such as p53/TP53, LOX and CDKN1A; apoptosis, such as BBC3/PUMA, CASP1, CASP7 and CASP8; immune response, such as IL7, IL12A/B and IL15, PTGS2/COX2 and CYBB; DNA damage responses and DNA repair, such as POLQ/POLH; MHC class I expression, such as TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B and B2M and MHC class II expression, such as CIITA. Represses genes involved in anti-proliferative response, such as BIRC5/survivin, CCNB1, CCNE1, CDK1, CDK2 and CDK4 and in immune response, such as FOXP3, IL4, ANXA2 and TLR4. Stimulates p53/TP53-dependent transcription through enhanced recruitment of EP300 leading to increased acetylation of p53/TP53. Plays an important role in immune response directly affecting NK maturation and activity, macrophage production of IL12, Th1 development and maturation of CD8+ T-cells. Also implicated in the differentiation and maturation of dendritic cells and in the suppression of regulatory T (Treg) cells development. Acts as a tumor suppressor and plays a role not only in antagonism of tumor cell growth but also in stimulating an immune response against tumor cells. {ECO:0000269|PubMed:15226432, ECO:0000269|PubMed:15509808, ECO:0000269|PubMed:17516545, ECO:0000269|PubMed:17942705, ECO:0000269|PubMed:18084608, ECO:0000269|PubMed:18497060, ECO:0000269|PubMed:18641303, ECO:0000269|PubMed:19404407, ECO:0000269|PubMed:19851330, ECO:0000269|PubMed:21389130, ECO:0000269|PubMed:22200613, ECO:0000269|PubMed:22367195}.; DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease. {ECO:0000269|PubMed:10395927, ECO:0000269|PubMed:9679752}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . smooth muscle;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;larynx;thyroid;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;islets of Langerhans;muscle;adrenal cortex;blood;lens;breast;greater omentum;pancreas;lung;nasopharynx;placenta;macula lutea;hippocampus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle; 0.72337 0.11079 -0.007201372 53.19061099 4.5089 0.16359 IRF2 0.382047181106152 0.615781271630557 0.00217154726329099 interferon regulatory factor 2 FUNCTION: Specifically binds to the upstream regulatory region of type I IFN and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)) and represses those genes. Also acts as an activator for several genes including H4 and IL7. Constitutively binds to the ISRE promoter to activate IL7. Involved in cell cycle regulation through binding the site II (HiNF-M) promoter region of H4 and activating transcription during cell growth. Antagonizes IRF1 transcriptional activation. {ECO:0000269|PubMed:12738767, ECO:0000269|PubMed:15226432, ECO:0000269|PubMed:18514056, ECO:0000269|PubMed:9540062}.; . TISSUE SPECIFICITY: Expressed throughout the epithelium of the colon. Also expressed in lamina propria. {ECO:0000269|PubMed:15226432}.; . . 0.52465 0.11616 -0.60427181 17.74593064 15.27758 0.54989 IRF2BP1 0.974430421605153 0.0255402133066683 2.93650881781589e-05 interferon regulatory factor 2 binding protein 1 FUNCTION: Acts as a transcriptional corepressor in a IRF2- dependent manner; this repression is not mediated by histone deacetylase activities. May act as an E3 ligase towards JDP2, enhancing its polyubiquitination. Represses ATF2-dependent transcriptional activation. {ECO:0000269|PubMed:12799427, ECO:0000269|PubMed:18671972}.; . . unclassifiable (Anatomical System);pancreas;lung;endometrium;islets of Langerhans;pineal body;placenta;visual apparatus;iris;brain;mammary gland;stomach;retina; liver;atrioventricular node; 0.54578 0.10923 0.104848986 61.49445624 128.83388 2.47373 IRF2BP2 0.470291318540817 0.505386519962977 0.0243221614962068 interferon regulatory factor 2 binding protein 2 FUNCTION: Acts as a transcriptional corepressor in a IRF2- dependent manner; this repression is not mediated by histone deacetylase activities. Represses the NFAT1-dependent transactivation of NFAT-responsive promoters. Acts as a coactivator of VEGFA expression in cardiac and skeletal muscle. {ECO:0000269|PubMed:12799427, ECO:0000269|PubMed:20702774, ECO:0000269|PubMed:21576369}.; . . . . 0.86306 0.10962 . . 584.28746 4.90195 IRF2BPL 0.968935346112199 0.0310171328402955 4.75210475054323e-05 interferon regulatory factor 2 binding protein-like FUNCTION: May contribute to the control of female reproductive function (By similarity). May play a role in gene transcription by transactivating GNRH1 promoter and repressing PENK promoter. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in the heart, moderately in skeletal muscle and pancreas, and weakly in brain, kidney, liver, testis, thyroid gland and lymphocytes. {ECO:0000269|PubMed:11095982}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;salivary gland;colon;skin;retina;bone marrow;pancreas;lung;adrenal gland;liver;testis;kidney;brain;bladder;mammary gland;stomach;thymus; skin;cerebellum; 0.69645 0.11157 . . 62.7394 1.62021 IRF3 0.00321741798317075 0.947800726835468 0.0489818551813616 interferon regulatory factor 3 FUNCTION: Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages.; . TISSUE SPECIFICITY: Expressed constitutively in a variety of tissues.; lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;iris;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; . 0.14498 0.33896 0.50895761 80.20169851 1605.94988 7.41953 IRF4 0.922220690010892 0.0777597147822235 1.959520688444e-05 interferon regulatory factor 4 FUNCTION: Transcriptional activator. Binds to the interferon- stimulated response element (ISRE) of the MHC class I promoter. Binds the immunoglobulin lambda light chain enhancer, together with PU.1. Probably plays a role in ISRE-targeted signal transduction mechanisms specific to lymphoid cells. Involved in CD8(+) dendritic cell differentiation by forming a complex with the BATF-JUNB heterodimer in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 and activation of genes (By similarity). {ECO:0000250|UniProtKB:Q64287}.; DISEASE: Multiple myeloma (MM) [MIM:254500]: A malignant tumor of plasma cells usually arising in the bone marrow and characterized by diffuse involvement of the skeletal system, hyperglobulinemia, Bence-Jones proteinuria and anemia. Complications of multiple myeloma are bone pain, hypercalcemia, renal failure and spinal cord compression. The aberrant antibodies that are produced lead to impaired humoral immunity and patients have a high prevalence of infection. Amyloidosis may develop in some patients. Multiple myeloma is part of a spectrum of diseases ranging from monoclonal gammopathy of unknown significance (MGUS) to plasma cell leukemia. {ECO:0000269|PubMed:9326949}. Note=The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving IRF4 has been found in multiple myeloma. Translocation t(6;14)(p25;q32) with the IgH locus.; TISSUE SPECIFICITY: Lymphoid cells.; . . 0.26812 0.30371 -0.602450568 17.91106393 170.24905 2.84687 IRF5 0.288476015651223 0.710591728047908 0.000932256300869171 interferon regulatory factor 5 FUNCTION: Transcription factor involved in the induction of interferons IFNA and INFB and inflammatory cytokines upon virus infection. Activated by TLR7 or TLR8 signaling. {ECO:0000269|PubMed:11303025, ECO:0000269|PubMed:15695821}.; DISEASE: Inflammatory bowel disease 14 (IBD14) [MIM:612245]: A chronic, relapsing inflammation of the gastrointestinal tract with a complex etiology. It is subdivided into Crohn disease and ulcerative colitis phenotypes. Crohn disease may affect any part of the gastrointestinal tract from the mouth to the anus, but most frequently it involves the terminal ileum and colon. Bowel inflammation is transmural and discontinuous; it may contain granulomas or be associated with intestinal or perianal fistulas. In contrast, in ulcerative colitis, the inflammation is continuous and limited to rectal and colonic mucosal layers; fistulas and granulomas are not observed. Both diseases include extraintestinal inflammation of the skin, eyes, or joints. {ECO:0000269|PubMed:17881657}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Systemic lupus erythematosus 10 (SLEB10) [MIM:612251]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:15657875}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Rheumatoid arthritis (RA) [MIM:180300]: An inflammatory disease with autoimmune features and a complex genetic component. It primarily affects the joints and is characterized by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures. {ECO:0000269|PubMed:17599733}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;colon;blood;skin;uterus;prostate;lung;bone;placenta;iris;alveolus;testis;germinal center;kidney;brain; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12643 0.20264 -0.359940251 28.93371078 5097.87875 14.63309 IRF5P1 . . . interferon regulatory factor 5 pseudogene 1 . . . . . . . . . . . IRF6 0.975119180790352 0.0248752528061661 5.56640348207681e-06 interferon regulatory factor 6 FUNCTION: Probable DNA-binding transcriptional activator. Key determinant of the keratinocyte proliferation-differentiation switch involved in appropriate epidermal development (By similarity). Plays a role in regulating mammary epithelial cell proliferation (By similarity). May regulate WDR65 transcription (By similarity). {ECO:0000250}.; DISEASE: Van der Woude syndrome 1 (VWS1) [MIM:119300]: An autosomal dominant developmental disorder characterized by lower lip pits, cleft lip and/or cleft palate. {ECO:0000269|PubMed:12219090, ECO:0000269|PubMed:12920575, ECO:0000269|PubMed:14618417, ECO:0000269|PubMed:14640121, ECO:0000269|PubMed:15300989, ECO:0000269|PubMed:17122170, ECO:0000269|PubMed:18478600}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Popliteal pterygium syndrome (PPS) [MIM:119500]: An autosomal dominant disorder characterized by oro-facial, skin and genital anomalies. Expressivity is variable. Clinical features include cleft lip/palate, lower lip cysts, syngnathia, congenital ankyloblepharon filiforme in some cases, bifid scrotum, hypoplastic scrotum, hypoplastic uterus, talipes equinovarus. {ECO:0000269|PubMed:12219090, ECO:0000269|PubMed:14640121, ECO:0000269|PubMed:19036739, ECO:0000269|PubMed:20803643}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Non-syndromic orofacial cleft 6 (OFC6) [MIM:608864]: A birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum. {ECO:0000269|PubMed:15317890, ECO:0000269|PubMed:21082654}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in normal mammary epithelial cells. Expression is reduced or absent in breast carcinomas. {ECO:0000269|PubMed:16049006}.; . . 0.81383 0.41336 -0.183570861 39.95046001 1316.0906 6.82157 IRF7 3.31354276199443e-07 0.329152014810891 0.670847653834833 interferon regulatory factor 7 FUNCTION: Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction via both the virus-activated, MyD88- independent pathway and the TLR-activated, MyD88-dependent pathway. Required during both the early and late phases of the IFN gene induction but is more critical for the late than for the early phase. Exists in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization where along with other coactivators it can activate transcription of the type I IFN and ISG genes. Can also play a role in regulating adaptive immune responses by inducing PSMB9/LMP2 expression, either directly or through induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can activate distinct gene expression programs in macrophages and regulate the anti-tumor properties of primary macrophages. {ECO:0000269|PubMed:11073981, ECO:0000269|PubMed:12374802, ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:17404045}.; DISEASE: Immunodeficiency 39 (IMD39) [MIM:616345]: A primary immunodeficiency causing severe, life-threatening acute respiratory distress upon infection with H1N1 influenza A. {ECO:0000269|PubMed:25814066}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly in spleen, thymus and peripheral blood leukocytes.; lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;white blood cells; 0.13455 0.36881 -0.26629572 34.81953291 243.98856 3.37082 IRF8 0.926540237878288 0.073442825977904 1.69361438082062e-05 interferon regulatory factor 8 FUNCTION: Specifically binds to the upstream regulatory region of type I IFN and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)). Plays a negative regulatory role in cells of the immune system. Involved in CD8(+) dendritic cell differentiation by forming a complex with the BATF-JUNB heterodimer in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF8 and activation of genes (By similarity). {ECO:0000250}.; DISEASE: Immunodeficiency 32A (IMD32A) [MIM:614893]: An immunologic disorder characterized by abnormal peripheral blood myeloid phenotype with a marked loss of CD11C-positive/CD1C dendritic cells, resulting in selective susceptibility to mycobacterial infections. {ECO:0000269|PubMed:21524210}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Immunodeficiency 32B (IMD32B) [MIM:614894]: A life- threatening pediatric disease characterized by monocyte and dendritic cell deficiency, myeloproliferation, and susceptibility to severe opportunistic infections, including disseminated BCG infection and oral candidiasis. {ECO:0000269|PubMed:21524210}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in lymphoid tissues. {ECO:0000269|PubMed:1460054, ECO:0000269|PubMed:23166356}.; unclassifiable (Anatomical System);lymph node;colon;blood;bone marrow;uterus;pancreas;endometrium;nasopharynx;testis;spleen;germinal center;brain;thymus; superior cervical ganglion;white blood cells; 0.11050 0.44945 -0.178111357 40.44585987 43.86054 1.26169 IRF9 0.631965597852179 0.367734094138371 0.000300308009449518 interferon regulatory factor 9 FUNCTION: Transcription factor that mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. IRF9/ISGF3G associates with the phosphorylated STAT1:STAT2 dimer to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state.; . . medulla oblongata;smooth muscle;ovary;foreskin;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;pineal body;blood;lens;skeletal muscle;breast;macula lutea;liver;spleen;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;epidermis;lacrimal gland;islets of Langerhans;hypothalamus;oral cavity;muscle;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus; . 0.48473 . -0.159704656 41.90846898 39.19666 1.16103 IRGC 0.0437355066124445 0.849455062965525 0.106809430422031 immunity-related GTPase family, cinema . . . unclassifiable (Anatomical System);medulla oblongata;lung;epididymis;placenta;hippocampus;testis;brain; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.15642 . -0.110153916 45.48832272 628.74642 5.05212 IRGM . . . immunity-related GTPase family, M FUNCTION: Putative GTPase which is required for clearance of acute protozoan and bacterial infections. Functions in innate immune response probably through regulation of autophagy. May regulate proinflammatory cytokine production and prevent endotoxemia upon infection. May also play a role in macrophages adhesion and motility (By similarity). {ECO:0000250, ECO:0000269|PubMed:16888103}.; DISEASE: Inflammatory bowel disease 19 (IBD19) [MIM:612278]: A chronic, relapsing inflammation of the gastrointestinal tract with a complex etiology. It is subdivided into Crohn disease and ulcerative colitis phenotypes. Crohn disease may affect any part of the gastrointestinal tract from the mouth to the anus, but most frequently it involves the terminal ileum and colon. Bowel inflammation is transmural and discontinuous; it may contain granulomas or be associated with intestinal or perianal fistulas. In contrast, in ulcerative colitis, the inflammation is continuous and limited to rectal and colonic mucosal layers; fistulas and granulomas are not observed. Both diseases include extraintestinal inflammation of the skin, eyes, or joints. {ECO:0000269|PubMed:17554261, ECO:0000269|PubMed:19174780, ECO:0000269|PubMed:21278745}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed (at protein level). Expressed in several tissues including colon, small bowel and peripheral blood leukocytes. {ECO:0000269|PubMed:16888103, ECO:0000269|PubMed:17554261}.; . . . . 0.567831482 81.78225997 279.04901 3.58090 IRGQ 0.00119722791198288 0.956861915221311 0.0419408568667065 immunity-related GTPase family, Q . . . . . 0.11132 0.10002 0.174625237 65.9648502 46.00143 1.30616 IRS1 0.218507352371316 0.781138664708349 0.000353982920335022 insulin receptor substrate 1 FUNCTION: May mediate the control of various cellular processes by insulin. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit (By similarity). {ECO:0000250, ECO:0000269|PubMed:16878150}.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:10206679, ECO:0000269|PubMed:12843189, ECO:0000269|PubMed:8723689}. Note=The gene represented in this entry may be involved in disease pathogenesis.; . smooth muscle;ovary;colon;skin;retina;uterus;prostate;whole body;cochlea;cerebral cortex;endometrium;thyroid;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;skeletal muscle;pancreas;lung;visual apparatus;liver;hypopharynx;amnion;head and neck;mammary gland;stomach;peripheral nerve; superior cervical ganglion;thyroid; 0.94505 0.81126 -1.297117862 4.965793819 759.0118 5.45781 IRS2 . . . insulin receptor substrate 2 FUNCTION: May mediate the control of various cellular processes by insulin.; . . . . 0.62318 0.75262 . . 971.5298 6.02460 IRS3P . . . insulin receptor substrate 3, pseudogene . . . . . . . . . . . IRS4 0.609434374357404 0.390200084785438 0.000365540857157489 insulin receptor substrate 4 FUNCTION: Acts as an interface between multiple growth factor receptors possessing tyrosine kinase activity, such as insulin receptor, IGF1R and FGFR1, and a complex network of intracellular signaling molecules containing SH2 domains. Involved in the IGF1R mitogenic signaling pathway. Promotes the AKT1 signaling pathway and BAD phosphorylation during insulin stimulation without activation of RPS6KB1 or the inhibition of apoptosis. Interaction with GRB2 enhances insulin-stimulated mitogen-activated protein kinase activity. May be involved in nonreceptor tyrosine kinase signaling in myoblasts. Plays a pivotal role in the proliferation/differentiation of hepatoblastoma cell through EPHB2 activation upon IGF1 stimulation. May play a role in the signal transduction in response to insulin and to a lesser extent in response to IL4 and GH on mitogenesis. Plays a role in growth, reproduction and glucose homeostasis. May act as negative regulators of the IGF1 signaling pathway by suppressing the function of IRS1 and IRS2. {ECO:0000269|PubMed:10531310, ECO:0000269|PubMed:10594015, ECO:0000269|PubMed:12639902, ECO:0000269|PubMed:17408801, ECO:0000269|PubMed:9553137}.; . TISSUE SPECIFICITY: Expressed in myoblasts. Expressed in liver and hepatocellular carcinoma. {ECO:0000269|PubMed:12639902, ECO:0000269|PubMed:17408801}.; . . 0.05500 0.20858 0.536463361 81.06864827 670.75013 5.17757 IRX1 0.00231065420659156 0.765943167530712 0.231746178262696 iroquois homeobox 1 . . . unclassifiable (Anatomical System);lung;heart;cochlea;islets of Langerhans;macula lutea;testis;fovea centralis;kidney;brain; . 0.28381 0.12155 . . 93.8628 2.08360 IRX1P1 . . . iroquois homeobox 1 pseudogene 1 . . . . . . . . . . . IRX2 0.648697596940709 0.345244394479749 0.00605800857954211 iroquois homeobox 2 . . . unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;fovea centralis;choroid;lens;skin;retina;uterus;breast;optic nerve;lung;cochlea;placenta;macula lutea;hypopharynx;liver;testis;head and neck;kidney;brain;mammary gland; . 0.53433 0.15230 . . 877.19497 5.76492 IRX3 . . . iroquois homeobox 3 FUNCTION: Transcription factor. Involved in SHH-dependent neural patterning. Together with NKX2-2 and NKX6-1 acts to restrict the generation of motor neurons to the appropriate region of the neural tube. Belongs to the class I proteins of neuronal progenitor factors, which are repressed by SHH signals. Involved in the transcriptional repression of MNX1 in non-motor neuron cells (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;salivary gland;muscle;parathyroid;skin;uterus;lung;placenta;hippocampus;liver;testis;cervix;kidney;brain;mammary gland; skeletal muscle; 0.78161 0.14363 . . 1394.92186 6.98593 IRX4 0.25376901140337 0.718146033009552 0.028084955587078 iroquois homeobox 4 FUNCTION: Likely to be an important mediator of ventricular differentiation during cardiac development.; . TISSUE SPECIFICITY: Predominantly expressed in cardiac ventricles.; unclassifiable (Anatomical System);uterus;prostate;lung;heart;thyroid;placenta;head and neck;skin; superior cervical ganglion;prostate;skeletal muscle; 0.68588 0.11869 . . 803.81043 5.58609 IRX4P1 . . . iroquois homeobox 4 pseudogene 1 . . . . . . . . . . . IRX5 . . . iroquois homeobox 5 FUNCTION: Establishes the cardiac repolarization gradient by its repressive actions on the KCND2 potassium-channel gene. Required for retinal cone bipolar cell differentiation. May regulate contrast adaptation in the retina and control specific aspects of visual function in circuits of the mammalian retina (By similarity). Could be involved in the regulation of both the cell cycle and apoptosis in prostate cancer cells. Involved in craniofacial and gonadal development. Modulates the migration of progenitor cell populations in branchial arches and gonads by repressing CXCL12. {ECO:0000250, ECO:0000269|PubMed:22581230}.; DISEASE: Hamamy syndrome (HMMS) [MIM:611174]: A syndrome characterized by severe hypertelorism, upslanting palpebral fissures, brachycephaly, abnormal ears, sloping shoulders, enamel hypoplasia, and osteopenia with repeated fractures. Additional features include myopia, mild to moderate sensorineural hearing loss, gonadal anomalies and borderline intelligence. {ECO:0000269|PubMed:22581230}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;skin;retina;uterus;lung;endometrium;bone;testis;kidney;mammary gland;brain;thymus; superior cervical ganglion;globus pallidus;atrioventricular node; 0.66381 0.13039 . . 1652.69996 7.51371 IRX6 2.81616051778102e-08 0.491500201645239 0.508499770193156 iroquois homeobox 6 . . . unclassifiable (Anatomical System);myocardium;heart;choroid;fovea centralis;lens;skin;retina;uterus;optic nerve;lung;visual apparatus;macula lutea;kidney; . 0.17334 0.09592 -0.754958418 13.57631517 395.74588 4.17946 ISCA1 0.77897388347489 0.213857118084624 0.00716899844048635 iron-sulfur cluster assembly 1 FUNCTION: Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway. Probably involved in the binding of an intermediate of Fe/S cluster assembly. {ECO:0000269|PubMed:15262227, ECO:0000269|PubMed:22323289}.; . TISSUE SPECIFICITY: Detected in cerebellum, kidney and heart. {ECO:0000269|PubMed:15262227}.; prostate; whole brain;amygdala;occipital lobe;thyroid;globus pallidus;cingulate cortex;cerebellum; 0.28070 0.11262 0.079165051 59.43029016 104.96047 2.21471 ISCA1P1 . . . iron-sulfur cluster assembly 1 pseudogene 1 . . . . . 0.21611 . . . . . ISCA1P2 . . . iron-sulfur cluster assembly 1 pseudogene 2 . . . . . . . . . . . ISCA1P3 . . . iron-sulfur cluster assembly 1 pseudogene 3 . . . . . . . . . . . ISCA1P4 . . . iron-sulfur cluster assembly 1 pseudogene 4 . . . . . . . . . . . ISCA1P5 . . . iron-sulfur cluster assembly 1 pseudogene 5 . . . . . . . . . . . ISCA1P6 . . . iron-sulfur cluster assembly 1 pseudogene 6 . . . . . . . . . . . ISCA2 6.27266246447634e-05 0.280417335140368 0.719519938234988 iron-sulfur cluster assembly 2 FUNCTION: Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway. May be involved in the binding of an intermediate of Fe/S cluster assembly. {ECO:0000269|PubMed:22323289}.; DISEASE: Multiple mitochondrial dysfunctions syndrome 4 (MMDS4) [MIM:616370]: A severe disorder of systemic energy metabolism, resulting in weakness, respiratory failure, lack of neurologic development, lactic acidosis, hyperglycinemia and early death. {ECO:0000269|PubMed:25539947}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;pituitary gland;liver;testis;colon;spleen;kidney;stomach; amygdala;whole brain;testis - interstitial;heart;thyroid;testis;cerebellum; 0.13274 . 0.079165051 59.43029016 12.04696 0.43695 ISCA2P1 . . . iron-sulfur cluster assembly 2 pseudogene 1 . . . . . . . . . . . ISCU 0.135947771003731 0.779918472140172 0.0841337568560975 iron-sulfur cluster assembly enzyme FUNCTION: Scaffold protein for the de novo synthesis of iron- sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins (PubMed:11060020). First, a [2Fe-2S] cluster is transiently assembled on the scaffold protein ISCU. In a second step, the cluster is released from ISCU, transferred to a glutaredoxin GLRX5, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISCU depends on the function of the cysteine desulfurase complex NFS1-LYRM4/ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase and ferredoxin, which receive their electrons from NADH (By similarity). {ECO:0000250|UniProtKB:Q03020, ECO:0000269|PubMed:11060020}.; . TISSUE SPECIFICITY: Detected in heart, liver, skeletal muscle, brain, pancreas, kidney, lung and placenta. {ECO:0000269|PubMed:11060020, ECO:0000269|PubMed:8875867}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;hippocampus;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;stomach; whole brain;amygdala; 0.45409 0.19342 0.057118534 57.99716914 45.61549 1.29777 ISCUP1 . . . iron-sulfur cluster assembly enzyme pseudogene 1 . . . . . . . . . . . ISG15 0.00984781293610986 0.600249312746062 0.389902874317828 ISG15 ubiquitin-like modifier FUNCTION: Ubiquitin-like protein which plays a key role in the innate immune response to viral infection either via its conjugation to a target protein (ISGylation) or via its action as a free or unconjugated protein. ISGylation involves a cascade of enzymatic reactions involving E1, E2, and E3 enzymes which catalyze the conjugation of ISG15 to a lysine residue in the target protein. Its target proteins include IFIT1, MX1/MxA, PPM1B, UBE2L6, UBA7, CHMP5, CHMP2A, CHMP4B and CHMP6. Can also isgylate: EIF2AK2/PKR which results in its activation, DDX58/RIG-I which inhibits its function in antiviral signaling response, EIF4E2 which enhances its cap structure-binding activity and translation- inhibition activity, UBE2N and UBE2E1 which negatively regulates their activity, IRF3 which inhibits its ubiquitination and degradation and FLNB which prevents its ability to interact with the upstream activators of the JNK cascade therby inhibiting IFNA- induced JNK signaling. Exhibits antiviral activity towards both DNA and RNA viruses, including influenza A, HIV-1 and Ebola virus. Restricts HIV-1 and ebola virus via disruption of viral budding. Inhibits the ubiquitination of HIV-1 Gag and host TSG101 and disrupts their interaction, thereby preventing assembly and release of virions from infected cells. Inhibits Ebola virus budding mediated by the VP40 protein by disrupting ubiquitin ligase activity of NEDD4 and its ability to ubiquitinate VP40. ISGylates influenza A virus NS1 protein which causes a loss of function of the protein and the inhibition of virus replication. The secreted form of ISG15 can: induce natural killer cell proliferation, act as a chemotactic factor for neutrophils and act as a IFN-gamma-inducing cytokine playing an essential role in antimycobacterial immunity. {ECO:0000269|PubMed:1373138, ECO:0000269|PubMed:16009940, ECO:0000269|PubMed:16112642, ECO:0000269|PubMed:16428300, ECO:0000269|PubMed:16434471, ECO:0000269|PubMed:16872604, ECO:0000269|PubMed:18305167, ECO:0000269|PubMed:19270716, ECO:0000269|PubMed:19357168, ECO:0000269|PubMed:2005397, ECO:0000269|PubMed:20133869, ECO:0000269|PubMed:20308324, ECO:0000269|PubMed:20639253, ECO:0000269|PubMed:21543490, ECO:0000269|PubMed:22693631, ECO:0000269|PubMed:22859821, ECO:0000269|PubMed:23229543, ECO:0000269|PubMed:7526157, ECO:0000269|PubMed:8550581}.; DISEASE: Immunodeficiency 38, with basal ganglia calcification (IMD38) [MIM:616126]: A primary immunodeficiency predisposing individuals to severe clinical disease upon infection with weakly virulent mycobacteria, including Mycobacterium bovis Bacille Calmette-Guerin (BCG) vaccines. Patients are also susceptible to Salmonella and Mycobacterium tubercolosis infections. Affected individuals have intracranial calcification. {ECO:0000269|PubMed:22859821}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in lymphoid cells, striated and smooth muscle, several epithelia and neurons. Expressed in neutrophils, monocytes and lymphocytes. Enhanced expression seen in pancreatic adenocarcinoma, endometrial cancer, and bladder cancer, as compared to non-cancerous tissue. In bladder cancer, the increase in expression exhibits a striking positive correlation with more advanced stages of the disease. {ECO:0000269|PubMed:22859821, ECO:0000269|PubMed:7490683}.; . . 0.10000 0.22633 -0.115612493 45.12856806 1374.86701 6.95277 ISG20 0.00609138684425968 0.735739489578701 0.258169123577039 interferon stimulated exonuclease gene 20kDa FUNCTION: Interferon-induced antiviral exoribonuclease that acts on single-stranded RNA and also has minor activity towards single- stranded DNA. Exhibits antiviral activity against RNA viruses including hepatitis C virus (HCV), hepatitis A virus (HAV) and yellow fever virus (YFV) in an exonuclease-dependent manner. May also play additional roles in the maturation of snRNAs and rRNAs, and in ribosome biogenesis. {ECO:0000269|PubMed:11401564, ECO:0000269|PubMed:12594219, ECO:0000269|PubMed:16033969, ECO:0000269|PubMed:21036379}.; . TISSUE SPECIFICITY: Highly expressed in peripheral blood leukocytes, spleen, thymus, colon and lung. Up regulated by E2 in estrogen receptor-positive breast cancer lines. {ECO:0000269|PubMed:9235947, ECO:0000269|PubMed:9569007}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; white blood cells;whole blood; 0.08196 . -0.229483771 36.86010852 41.33282 1.20828 ISG20L2 0.821397244338996 0.177746058550927 0.000856697110077251 interferon stimulated exonuclease gene 20kDa like 2 FUNCTION: 3'-> 5'-exoribonuclease involved in ribosome biogenesis in the processing of the 12S pre-rRNA. Displays a strong specificity for a 3'-end containing a free hydroxyl group. {ECO:0000269|PubMed:18065403}.; . . medulla oblongata;smooth muscle;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;blood;lens;skeletal muscle;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.11852 0.09039 0.349177632 74.18023119 253.36585 3.42569 ISL1 0.606135790074323 0.392022764595628 0.0018414453300493 ISL LIM homeobox 1 FUNCTION: Binds and regulates the promoters of the insulin, glucagon and somatostatin genes. Involved in the specificarion of motor neurons in cooperation with LHX3 and LDB1 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in subsets of neurons of the adrenal medulla and dorsal root ganglion, inner nuclear and ganglion cell layers in the retina, the pineal and some regions of the brain.; unclassifiable (Anatomical System);ovary;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;pancreas;prostate;optic nerve;lung;placenta;macula lutea;visual apparatus;testis;stomach; superior cervical ganglion;atrioventricular node; 0.39262 . -0.361761279 28.6329323 286.91147 3.62826 ISL2 0.329330132128272 0.655219496401539 0.0154503714701894 ISL LIM homeobox 2 FUNCTION: Transcriptional factor that defines subclasses of motoneurons that segregate into columns in the spinal cord and select distinct axon pathways. {ECO:0000250}.; . . unclassifiable (Anatomical System);optic nerve;ovary;macula lutea;testis;colon;fovea centralis;choroid;lens;stomach;retina; superior cervical ganglion;ciliary ganglion; 0.59758 0.15498 -0.494039303 22.09247464 45.67566 1.29837 ISLR 0.000436481987652303 0.418320139334292 0.581243378678056 immunoglobulin superfamily containing leucine-rich repeat . . TISSUE SPECIFICITY: Expressed in various tissues including retina, heart, skeletal muscle, prostate, ovary, small intestine, thyroid, adrenal cortex, testis, stomach and spinal cord. {ECO:0000269|PubMed:10512678, ECO:0000269|PubMed:9325048}.; medulla oblongata;smooth muscle;ovary;sympathetic chain;colon;choroid;skin;retina;uterus;prostate;whole body;oesophagus;endometrium;larynx;thyroid;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.56509 0.12316 -0.642904474 16.62538335 45.35589 1.29358 ISLR2 . . . immunoglobulin superfamily containing leucine-rich repeat 2 FUNCTION: Required for axon extension during neural development. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;frontal lobe;heart;testis;brain; testis - interstitial;pancreas;globus pallidus; 0.16242 0.11393 -0.600630256 18.06440198 281.12876 3.59155 ISM1 0.0542221895137127 0.92618229705861 0.0195955134276777 isthmin 1, angiogenesis inhibitor FUNCTION: Acts as an angiogenesis inhibitor. {ECO:0000250|UniProtKB:A2ATD1}.; . . unclassifiable (Anatomical System);medulla oblongata;heart;adrenal cortex;fovea centralis;choroid;lens;retina;optic nerve;lung;endometrium;adrenal gland;placenta;bone;macula lutea;liver;testis;kidney;mammary gland;brain; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.34107 0.12448 0.15257911 64.60839821 408.65229 4.23798 ISM1-AS1 . . . ISM1 antisense RNA 1 . . . . . . . . . . . ISM2 1.26338885002286e-05 0.830483456713884 0.169503909397616 isthmin 2 . . TISSUE SPECIFICITY: Expressed at high levels in the placenta and at moderate levels in the pancreas, kidney, heart, liver, lung, brain and skeletal muscle. {ECO:0000269|PubMed:15194193}.; unclassifiable (Anatomical System);uterus;prostate;ovary;heart;placenta;liver;testis;parathyroid;spleen;skin;aorta; dorsal root ganglion;superior cervical ganglion;placenta;atrioventricular node; 0.08069 0.10561 0.338046437 73.70252418 319.78579 3.79847 ISOC1 0.00529303405400188 0.892418157541678 0.10228880840432 isochorismatase domain containing 1 . . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;hypothalamus;pineal body;pharynx;blood;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;duodenum;liver;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; uterus;fetal liver;liver;kidney; 0.14661 . -0.227663163 37.11370606 20.03807 0.68426 ISOC2 0.0433194344015214 0.848646094733515 0.108034470864964 isochorismatase domain containing 2 . . . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;urinary;colon;blood;lens;skin;skeletal muscle;uterus;prostate;lung;adrenal gland;bone;visual apparatus;liver;testis;cervix;spleen;kidney;brain;tonsil;stomach; liver;trigeminal ganglion;skeletal muscle; 0.18588 0.10427 -0.071520315 48.34866714 78.693 1.87213 ISPD 0.00243660167412645 0.928181613521859 0.0693817848040143 isoprenoid synthase domain containing FUNCTION: Required for protein O-linked mannosylation. Probably acts as a nucleotidyltransferase involved in synthesis of a nucleotide sugar. Required for dystroglycan O-mannosylation. {ECO:0000269|PubMed:22522420, ECO:0000269|PubMed:22522421}.; DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C7 (MDDGC7) [MIM:616052]: A form of muscular dystrophy resulting from defective glycosylation of alpha-dystroglycan, and characterized by a limb-girdle phenotype with muscular weakness apparent after ambulation is achieved. MDDGC7 individuals do not show epilepsy, mental retardation, structural eye/brain abnormalities, or white matter changes. {ECO:0000269|PubMed:23390185}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed, with high expression in brain. {ECO:0000269|PubMed:22522420}.; . . . . . . 1279.20707 6.73590 ISPD-AS1 . . . ISPD antisense RNA 1 . . . . . . . . . . . IST1 0.0231106718602087 0.962089212364472 0.014800115775319 IST1, ESCRT-III associated factor FUNCTION: Proposed to be involved in specific functions of the ESCRT machinery. Is required for efficient abscission during cytokinesis, but not for HIV-1 budding. The involvement in the MVB pathway is not established. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. {ECO:0000269|PubMed:19129479, ECO:0000269|PubMed:19129480}.; . . myocardium;lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach; testis - seminiferous tubule;hypothalamus;placenta;spinal cord;prefrontal cortex;testis; 0.15283 0.12749 -0.492218069 22.35786742 65.04961 1.65843 ISX 0.00018915120761652 0.4729400638004 0.526870784991984 intestine specific homeobox FUNCTION: Transcription factor that regulates gene expression in intestine. May participate in vitamin A metabolism most likely by regulating BCO1 expression in the intestine (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);liver; . 0.09555 0.09639 1.26221942 93.55980184 1135.03292 6.42867 ISX-AS1 . . . ISX antisense RNA 1 . . . . . . . . . . . ISY1 0.998290706422744 0.00170928566726352 7.90999214498532e-09 ISY1 splicing factor homolog FUNCTION: May play a role in pre-mRNA splicing. {ECO:0000305}.; . . lymphoreticular;myocardium;ovary;salivary gland;intestine;colon;skin;uterus;prostate;oesophagus;endometrium;bone;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;kidney;mammary gland;stomach;aorta; . . . -0.09720619 46.20193442 1.79147 0.05655 ISY1-RAB43 0.99889493512477 0.00110506214383368 2.73139601465804e-09 ISY1-RAB43 readthrough FUNCTION: May play a role in pre-mRNA splicing. {ECO:0000305}.; . . . . . . -0.185391282 39.67916962 7.83216 0.28778 ISYNA1 0.00263929952719535 0.9829669421528 0.0143937583200043 inositol-3-phosphate synthase 1 FUNCTION: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the synthesis of all inositol-containing compounds. {ECO:0000269|PubMed:15024000}.; . TISSUE SPECIFICITY: Highly expressed in testis, ovary, heart, placenta and pancreas. Weakly expressed in blood leukocyte, thymus, skeletal muscle and colon. {ECO:0000269|PubMed:12941308}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;placenta;testis; . 0.16603 -0.622676946 17.30950696 83.36531 1.94102 ITCH 0.999990177147491 9.82285250327178e-06 5.56601641622752e-15 itchy E3 ubiquitin protein ligase FUNCTION: Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation. It is involved in the control of inflammatory signaling pathways. Is an essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of the complex after TNF stimulation. Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1. Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways. Regulates the transcriptional activity of several transcription factors, and probably plays an important role in the regulation of immune response. Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages. Critical regulator of T-helper (TH2) cytokine development through its ability to induce JUNB ubiquitination and degradation (By similarity). Ubiquitinates SNX9. Ubiquitinates CXCR4 and HGS/HRS and regulates sorting of CXCR4 to the degradative pathway. It is involved in the negative regulation of MAVS-dependent cellular antiviral responses. Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation. Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP. Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID. Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046). {ECO:0000250|UniProtKB:Q8C863, ECO:0000269|PubMed:14602072, ECO:0000269|PubMed:16387660, ECO:0000269|PubMed:17028573, ECO:0000269|PubMed:18628966, ECO:0000269|PubMed:18718448, ECO:0000269|PubMed:18718449, ECO:0000269|PubMed:19131965, ECO:0000269|PubMed:19592251, ECO:0000269|PubMed:19881509, ECO:0000269|PubMed:20068034, ECO:0000269|PubMed:20392206, ECO:0000269|PubMed:23146885, ECO:0000269|PubMed:25631046}.; DISEASE: Autoimmune disease, multisystem, with facial dysmorphism (ADMFD) [MIM:613385]: A disorder characterized by organomegaly, failure to thrive, developmental delay, dysmorphic features and autoimmune inflammatory cell infiltration of the lungs, liver and gut. {ECO:0000269|PubMed:20170897}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;larynx;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;cornea;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.59377 0.08471 -1.089312628 7.047652748 40.17092 1.18051 ITCH-AS1 . . . ITCH antisense RNA 1 . . . . . . . . . . . ITCH-IT1 . . . ITCH intronic transcript 1 . . . . . . . . . . . ITFG1 0.962023993456245 0.0379758747668202 1.31776934725981e-07 integrin alpha FG-GAP repeat containing 1 FUNCTION: Modulator of T-cell function. Has a protective effect in graft versus host disease model (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; medulla oblongata;smooth muscle;ovary;sympathetic chain;parathyroid;skin;retina;bone marrow;uterus;whole body;frontal lobe;endometrium;larynx;bone;thyroid;iris;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;skeletal muscle;pancreas;lung;adrenal gland;epididymis;trabecular meshwork;placenta;hippocampus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; amygdala;occipital lobe;thalamus;placenta;globus pallidus;caudate nucleus;cingulate cortex; 0.27895 0.10732 -0.359940251 28.93371078 38.21304 1.13471 ITFG1-AS1 . . . ITFG1 antisense RNA 1 . . . . . . . . . . . ITFG2 1.38956896751476e-06 0.833434348456329 0.166564261974704 integrin alpha FG-GAP repeat containing 2 . . . ovary;colon;retina;bone marrow;uterus;prostate;whole body;cochlea;thyroid;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;skeletal muscle; 0.12392 0.08912 -0.824740496 11.67728238 49.68317 1.38150 ITGA1 0.00237568458237799 0.997624074378156 2.4103946635786e-07 integrin subunit alpha 1 FUNCTION: Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G- E-R in collagen. Involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. {ECO:0000269|PubMed:15592458}.; . . smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;whole body;oesophagus;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.52354 0.10542 -0.06060434 48.88535032 3525.16744 11.45196 ITGA2 9.23087390177119e-09 0.999960004500544 3.99862685818173e-05 integrin subunit alpha 2 FUNCTION: Integrin alpha-2/beta-1 is a receptor for laminin, collagen, collagen C-propeptides, fibronectin and E-cadherin. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. It is responsible for adhesion of platelets and other cells to collagens, modulation of collagen and collagenase gene expression, force generation and organization of newly synthesized extracellular matrix.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;thyroid;bone;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;cervix;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.27783 0.62384 -0.23697515 36.32342534 1299.77706 6.78223 ITGA2B 4.07385209926142e-05 0.999955856586098 3.40489290910929e-06 integrin subunit alpha 2b FUNCTION: Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha- IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface.; DISEASE: Glanzmann thrombasthenia (GT) [MIM:273800]: A common inherited disease of platelet aggregation. It is characterized by mucocutaneous bleeding of mild-to-moderate severity. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb-IIIa complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the GPIIb-IIIa complex at reduced levels, have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. {ECO:0000269|PubMed:10607701, ECO:0000269|PubMed:11798398, ECO:0000269|PubMed:12083483, ECO:0000269|PubMed:12181054, ECO:0000269|PubMed:12424194, ECO:0000269|PubMed:12506038, ECO:0000269|PubMed:15099289, ECO:0000269|PubMed:15219201, ECO:0000269|PubMed:17018384, ECO:0000269|PubMed:20020534, ECO:0000269|PubMed:7508443, ECO:0000269|PubMed:7706461, ECO:0000269|PubMed:8282784, ECO:0000269|PubMed:8704171, ECO:0000269|PubMed:9215749, ECO:0000269|PubMed:9473221, ECO:0000269|PubMed:9722314, ECO:0000269|PubMed:9734640, ECO:0000269|PubMed:9763559, ECO:0000269|PubMed:9920835}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bleeding disorder, platelet-type 16 (BDPLT16) [MIM:187800]: An autosomal dominant form of congenital macrothrombocytopenia associated with platelet anisocytosis. It is a disorder of platelet production. Affected individuals may have no or only mildly increased bleeding tendency. In vitro studies show mild platelet functional abnormalities. {ECO:0000269|PubMed:21454453, ECO:0000269|PubMed:9834222}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 and isoform 2 were identified in platelets and megakaryocytes, but not in reticulocytes or in Jurkat and U-937 white blood cell line. Isoform 3 is expressed by leukemia, prostate adenocarcinoma and melanoma cells but not by platelets or normal prostate or breast epithelial cells.; unclassifiable (Anatomical System);breast;lung;whole body;placenta;testis;bone marrow; fetal liver;superior cervical ganglion;atrioventricular node;whole blood;skeletal muscle;bone marrow; 0.34180 0.10653 -0.326979057 30.90351498 3832.69791 12.18707 ITGA3 2.40911978006841e-05 0.999968669497302 7.23930489729508e-06 integrin subunit alpha 3 FUNCTION: Integrin alpha-3/beta-1 is a receptor for fibronectin, laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha- 3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. {ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:15181153}.; DISEASE: Interstitial lung disease, nephrotic syndrome, and epidermolysis bullosa, congenital (ILNEB) [MIM:614748]: A multiorgan disorder characterized by congenital nephrotic syndrome, interstitial lung disease, and epidermolysis bullosa. The respiratory and renal features predominate, and lung involvement accounts for the lethal course of the disease. {ECO:0000269|PubMed:22512483}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is widely expressed. Isoform 2 is expressed in brain and heart. In brain, both isoforms are exclusively expressed on vascular smooth muscle cells, whereas in heart isoform 1 is strongly expressed on vascular smooth muscle cells, isoform 2 is detected only on endothelial vein cells. {ECO:0000269|PubMed:9111516}.; lymphoreticular;ovary;sympathetic chain;colon;choroid;skin;bone marrow;uterus;prostate;larynx;bone;thyroid;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);cartilage;small intestine;heart;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.18721 0.57153 -0.879979233 10.5626327 1443.34738 7.08579 ITGA4 0.0288517021361378 0.971147542125189 7.55738673722991e-07 integrin subunit alpha 4 FUNCTION: Integrins alpha-4/beta-1 (VLA-4) and alpha-4/beta-7 are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha- 4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha- 4/beta-7 is also a receptor for MADCAM1. It recognizes the sequence L-D-T in MADCAM1. On activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells. {ECO:0000269|PubMed:19064666}.; . . unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;urinary;colon;blood;skin;skeletal muscle;prostate;lung;endometrium;cornea;liver;testis;spleen;kidney;germinal center;brain;stomach;thymus; fetal liver;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;whole blood;skeletal muscle; 0.37460 0.47635 -0.619039275 17.39797122 331.94634 3.87313 ITGA5 0.999798063012463 0.000201936987522458 1.47305810638295e-14 integrin subunit alpha 5 FUNCTION: Integrin alpha-5/beta-1 is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;bladder;brain;heart;cartilage;tongue;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;pancreas;lung;mesenchyma;placenta;head and neck;kidney;stomach;aorta; smooth muscle;heart;placenta;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.38116 0.54001 -0.859744935 10.92238736 278.91067 3.57989 ITGA6 0.00991360284214048 0.990086246800778 1.50357081347093e-07 integrin subunit alpha 6 FUNCTION: Integrin alpha-6/beta-1 is a receptor for laminin on platelets. Integrin alpha-6/beta-4 is a receptor for laminin in epithelial cells and it plays a critical structural role in the hemidesmosome. {ECO:0000269|PubMed:17303120}.; DISEASE: Epidermolysis bullosa letalis, with pyloric atresia (EB- PA) [MIM:226730]: An autosomal recessive, frequently lethal, epidermolysis bullosa with variable involvement of skin, nails, mucosa, and with variable effects on the digestive system. It is characterized by mucocutaneous fragility, aplasia cutis congenita, and gastrointestinal atresia, which most commonly affects the pylorus. Pyloric atresia is a primary manifestation rather than a scarring process secondary to epidermolysis bullosa. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Integrin alpha-6/beta-4 is predominantly expressed by epithelia. Isoforms containing segment X1 are ubiquitously expressed. Isoforms containing segment X1X2 are expressed in heart, kidney, placenta, colon, duodenum, myoblasts and myotubes, and in a limited number of cell lines; they are always coexpressed with the ubiquitous isoform containing segment X1. In some tissues (e.g. Salivary gland), isoforms containing cytoplasmic segment A and isoforms containing segment B are detected while in others, only isoforms containing one cytoplasmic segment are found (segment A in epidermis and segment B in kidney). {ECO:0000269|PubMed:7681434}.; myocardium;medulla oblongata;ovary;sympathetic chain;rectum;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;bladder;brain;gall bladder;heart;cartilage;tongue;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;cerebral cortex;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach; . 0.61813 0.48979 0.249861693 69.66265629 3306.75309 10.97922 ITGA7 1.80979797287063e-09 0.999585497375624 0.000414500814577502 integrin subunit alpha 7 FUNCTION: Integrin alpha-7/beta-1 is the primary laminin receptor on skeletal myoblasts and adult myofibers. During myogenic differentiation, it may induce changes in the shape and mobility of myoblasts, and facilitate their localization at laminin-rich sites of secondary fiber formation. It is involved in the maintenance of the myofibers cytoarchitecture as well as for their anchorage, viability and functional integrity. Isoform Alpha-7X2B and isoform Alpha-7X1B promote myoblast migration on laminin 1 and laminin 2/4, but isoform Alpha-7X1B is less active on laminin 1 (In vitro). Acts as Schwann cell receptor for laminin-2. Acts as a receptor of COMP and mediates its effect on vascular smooth muscle cells (VSMCs) maturation (By similarity). Required to promote contractile phenotype acquisition in differentiated airway smooth muscle (ASM) cells. {ECO:0000250, ECO:0000269|PubMed:10694445, ECO:0000269|PubMed:17641293, ECO:0000269|PubMed:9307969}.; DISEASE: Muscular dystrophy congenital due to integrin alpha-7 deficiency (MDCI) [MIM:613204]: A form of congenital muscular dystrophy. Patients present at birth, or within the first few months of life, with hypotonia, muscle weakness and often with joint contractures. {ECO:0000269|PubMed:9590299}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoforms containing segment A are predominantly expressed in skeletal muscle. Isoforms containing segment B are abundantly expressed in skeletal muscle, moderately in cardiac muscle, small intestine, colon, ovary and prostate and weakly in lung and testes. Isoforms containing segment X2D are expressed at low levels in fetal and adult skeletal muscle and in cardiac muscle, but are not detected in myoblasts and myotubes. In muscle fibers isoforms containing segment A and B are expressed at myotendinous and neuromuscular junctions; isoforms containing segment C are expressed at neuromuscular junctions and at extrasynaptic sites. Isoforms containing segments X1 or X2 or, at low levels, X1X2 are expressed in fetal and adult skeletal muscle (myoblasts and myotubes) and cardiac muscle. {ECO:0000269|PubMed:8626012}.; myocardium;medulla oblongata;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;subthalamic nucleus;optic nerve;endometrium;cerebral cortex;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;muscle;lens;skeletal muscle;lung;placenta;macula lutea;hippocampus;liver;spleen;kidney;stomach; amygdala;olfactory bulb;adipose tissue;tongue;spinal cord;ciliary ganglion;atrioventricular node;caudate nucleus;skeletal muscle; 0.26775 0.36635 0.170781634 65.34560038 592.64062 4.93434 ITGA8 5.01886012783355e-08 0.99998257224115 1.73775702491115e-05 integrin subunit alpha 8 FUNCTION: Integrin alpha-8/beta-1 functions in the genesis of kidney and probably of other organs by regulating the recruitment of mesenchymal cells into epithelial structures. It recognizes the sequence R-G-D in a wide array of ligands including TNC, FN1, SPP1 TGFB1, TGFB3 and VTN. NPNT is probably its functional ligand in kidney genesis. Neuronal receptor for TNC it mediates cell-cell interactions and regulates neurite outgrowth of sensory and motor neurons. {ECO:0000269|PubMed:12415008, ECO:0000269|PubMed:15721307}.; . TISSUE SPECIFICITY: Expressed in mesenchymal cells, including alveolar myofibroblasts, kidney mesangial cells and hepatic stellar cells and vascular and visceral smooth muscle (at protein level). {ECO:0000269|PubMed:10504498, ECO:0000269|PubMed:7768999}.; . . 0.19255 0.19038 -0.786348947 12.63269639 602.10061 4.96627 ITGA9 0.0961917478256693 0.903807695796409 5.56377921303544e-07 integrin subunit alpha 9 FUNCTION: Integrin alpha-9/beta-1 (ITGA9:ITGB1) is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E- I-D-G-I-E-L in cytotactin. {ECO:0000250}.; . TISSUE SPECIFICITY: In airway epithelium, in the basal layer of squamous epithelium, and in smooth muscle, skeletal muscle, and hepatocytes. Abundantly expressed in fetal lung and lung cancers. {ECO:0000269|PubMed:8245132, ECO:0000269|PubMed:8290272}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;tongue;hypothalamus;adrenal medulla;colon;skin;skeletal muscle;uterus;prostate;lung;bone;visual apparatus;liver;testis;head and neck;spleen;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.15689 0.28307 -1.098660656 6.95329087 296.69005 3.67562 ITGA9-AS1 . . . ITGA9 antisense RNA 1 . . . . . . . . . . . ITGA10 8.55370308285704e-11 0.999944354810156 5.56451043072989e-05 integrin subunit alpha 10 FUNCTION: Integrin alpha-10/beta-1 is a receptor for collagen.; . TISSUE SPECIFICITY: Widely expressed with highest expression in muscle and heart. Found in articular cartilage.; . . 0.53865 0.16452 1.274975588 93.67185657 1717.62595 7.64081 ITGA11 0.000116168936373859 0.999865363854724 1.8467208902093e-05 integrin subunit alpha 11 FUNCTION: Integrin alpha-11/beta-1 is a receptor for collagen.; . TISSUE SPECIFICITY: According to PubMed:10464311, highest levels of expression in uterus and heart, intermediate levels in skeletal muscle and intermediate to low levels in pancreas, kidney and placenta. According to PubMed:10486209, also found in brain, colon, lung, small intestine, stomach, testis, salivary glands, thyroid glands and prostate. Very low levels in peripheral blood lymphocytes, fetal brain and fetal liver. {ECO:0000269|PubMed:10464311}.; unclassifiable (Anatomical System);smooth muscle;cartilage;salivary gland;colon;skin;skeletal muscle;bone marrow;bile duct;breast;epididymis;thyroid;bone;liver;brain;mammary gland; globus pallidus;trigeminal ganglion;skeletal muscle; 0.17155 0.18585 -1.313764723 4.824251003 2503.51289 9.32628 ITGAD 6.33151638988354e-12 0.99767491871804 0.00232508127562836 integrin subunit alpha D FUNCTION: Integrin alpha-D/beta-2 is a receptor for ICAM3 and VCAM1. May play a role in the atherosclerotic process such as clearing lipoproteins from plaques and in phagocytosis of blood- borne pathogens, particulate matter, and senescent erythrocytes from the blood.; . TISSUE SPECIFICITY: Expressed moderately on myelomonocytic cell lines and subsets of peripheral blood leukocytes and strongly on tissue-specialized cells, including macrophages foam cells within atherosclerotic plaques, and on splenic red pulp macrophages.; . . 0.06435 . -0.516330081 20.97192734 219.3346 3.20327 ITGAE 7.98813572559606e-13 0.958766012166942 0.0412339878322591 integrin subunit alpha E FUNCTION: Integrin alpha-E/beta-7 is a receptor for E-cadherin. It mediates adhesion of intra-epithelial T-lymphocytes to epithelial cell monolayers.; . TISSUE SPECIFICITY: Expressed on a subclass of T-lymphocytes known as intra-epithelial lymphocytes which are located between mucosal epithelial cells.; ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;lens;lung;placenta;macula lutea;liver;kidney;mammary gland;aorta; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.10950 . 0.769703589 86.90728946 2363.23014 9.01981 ITGAL 0.430339544018475 0.569660434952072 2.10294527515732e-08 integrin subunit alpha L FUNCTION: Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. It is involved in a variety of immune phenomena including leukocyte-endothelial cell interaction, cytotoxic T-cell mediated killing, and antibody dependent killing by granulocytes and monocytes.; . TISSUE SPECIFICITY: Leukocytes.; unclassifiable (Anatomical System);lymph node;blood;skeletal muscle;bone marrow;retina;lung;larynx;nasopharynx;thyroid;testis;spleen;head and neck;germinal center;thymus; superior cervical ganglion;white blood cells;whole blood; 0.14610 0.42122 -0.859744935 10.92238736 1961.99344 8.15944 ITGAM 1.33563852516558e-08 0.999426147512272 0.000573839131342355 integrin subunit alpha M FUNCTION: Integrin alpha-M/beta-2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles. It is identical with CR-3, the receptor for the iC3b fragment of the third complement component. It probably recognizes the R-G-D peptide in C3b. Integrin alpha-M/beta-2 is also a receptor for fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides of fibrinogen gamma chain.; DISEASE: Systemic lupus erythematosus 6 (SLEB6) [MIM:609939]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:18204446, ECO:0000269|PubMed:18204448}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in monocytes and granulocytes.; unclassifiable (Anatomical System);heart;cartilage;blood;skin;bone marrow;uterus;lung;frontal lobe;placenta;bone;testis;germinal center;kidney;brain; whole blood;bone marrow; 0.10170 . -0.5879134 18.28261382 1577.73757 7.35022 ITGAV 0.477866430207163 0.522133566831843 2.96099473753337e-09 integrin subunit alpha V FUNCTION: The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands.; . . smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;testis;dura mater;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;pancreas;pia mater;lung;cornea;adrenal gland;placenta;hypopharynx;amnion;head and neck;kidney;stomach;aorta; caudate nucleus; 0.70819 0.59750 -1.480759435 3.686010852 427.47005 4.31886 ITGAX 6.11156995762923e-05 0.99993698249632 1.90180410406911e-06 integrin subunit alpha X FUNCTION: Integrin alpha-X/beta-2 is a receptor for fibrinogen. It recognizes the sequence G-P-R in fibrinogen. It mediates cell-cell interaction during inflammatory responses. It is especially important in monocyte adhesion and chemotaxis.; . TISSUE SPECIFICITY: Predominantly expressed in monocytes and granulocytes.; unclassifiable (Anatomical System);lymphoreticular;cartilage;colon;blood;fovea centralis;choroid;lens;retina;bone marrow;uterus;prostate;optic nerve;lung;larynx;nasopharynx;macula lutea;liver;head and neck;spleen;germinal center;kidney;brain; lymph node;whole blood; 0.09861 . -0.915030414 9.837225761 3879.17486 12.28742 ITGB1 0.914111640885177 0.0858873239601324 1.03515469099844e-06 integrin subunit beta 1 FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta- 1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha- 1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha- 3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha- 10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-4/beta-1 is a receptor for VCAM1. It recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. Isoform 2 interferes with isoform 1 resulting in a dominant negative effect on cell adhesion and migration (in vitro). When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and GNB2L1/RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen- dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. {ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:12473654, ECO:0000269|PubMed:16256741, ECO:0000269|PubMed:18804435, ECO:0000269|PubMed:19064666, ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:7523423}.; FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for human echoviruses 1 and 8 (PubMed:8411387). Acts as a receptor for cytomegalovirus/HHV-5 (PubMed:20660204). Acts as a receptor for Epstein-Barr virus/HHV-4 (PubMed:17945327). Integrin ITGA5:ITGB1 acts as a receptor for human parvovirus B19 (PubMed:12907437). Integrin ITGA2:ITGB1 acts as a receptor for human rotavirus (PubMed:12941907). Acts as a receptor for mammalian reovirus (PubMed:16501085). In case of HIV-1 infection, integrin ITGA5:ITGB1 binding to extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions (PubMed:10397733). {ECO:0000269|PubMed:10397733, ECO:0000269|PubMed:12907437, ECO:0000269|PubMed:12941907, ECO:0000269|PubMed:16501085, ECO:0000269|PubMed:17945327, ECO:0000269|PubMed:20660204, ECO:0000269|PubMed:8411387}.; . TISSUE SPECIFICITY: Isoform 1 is widely expressed, other isoforms are generally coexpressed with a more restricted distribution. Isoform 2 is expressed in skin, liver, skeletal muscle, cardiac muscle, placenta, umbilical vein endothelial cells, neuroblastoma cells, lymphoma cells, hepatoma cells and astrocytoma cells. Isoform 3 and isoform 4 are expressed in muscle, kidney, liver, placenta, cervical epithelium, umbilical vein endothelial cells, fibroblast cells, embryonal kidney cells, platelets and several blood cell lines. Isoform 4, rather than isoform 3, is selectively expressed in peripheral T-cells. Isoform 3 is expressed in non- proliferating and differentiated prostate gland epithelial cells and in platelets, on the surface of erythroleukemia cells and in various hematopoietic cell lines. Isoform 5 is expressed specifically in striated muscle (skeletal and cardiac muscle). {ECO:0000269|PubMed:1551917, ECO:0000269|PubMed:2249781, ECO:0000269|PubMed:7544298, ECO:0000269|PubMed:7545396, ECO:0000269|PubMed:7681433, ECO:0000269|PubMed:9494094}.; myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;uterus;superior cervical ganglion;uterus corpus;smooth muscle;adipose tissue;placenta;ciliary ganglion;skeletal muscle; 0.93571 0.85201 -1.177506449 5.944798301 15.5564 0.55468 ITGB1BP1 0.00190084865607946 0.904934990658553 0.0931641606853677 integrin subunit beta 1 binding protein 1 FUNCTION: Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin- dependent manner. Involved in the regulation of beta-1 integrin- containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion; inhibits beta-1 integrin clustering within FA by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin-and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion; reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation; modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development; acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter. {ECO:0000269|PubMed:11741838, ECO:0000269|PubMed:11807099, ECO:0000269|PubMed:11919189, ECO:0000269|PubMed:12473654, ECO:0000269|PubMed:15703214, ECO:0000269|PubMed:17916086, ECO:0000269|PubMed:20616313, ECO:0000269|PubMed:21768292, ECO:0000269|Ref.18}.; . TISSUE SPECIFICITY: Expressed in endothelial cells and fibroblasts (at protein level). Ubiquitously expressed. Expressed in intestine, colon, testis, ovary, thymus, spleen and prostate. {ECO:0000269|PubMed:9281591, ECO:0000269|PubMed:9867804}.; ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;kidney;mammary gland;aorta;stomach; dorsal root ganglion;whole brain;amygdala;medulla oblongata;superior cervical ganglion;occipital lobe;thalamus;temporal lobe;caudate nucleus;atrioventricular node;pons;subthalamic nucleus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.48621 0.15588 -0.273576253 33.97027601 9.29843 0.34126 ITGB1BP2 0.000383159415631921 0.841950162465139 0.157666678119229 integrin subunit beta 1 binding protein 2 FUNCTION: May play a role during maturation and/or organization of muscles cells.; . TISSUE SPECIFICITY: Expressed in skeletal and cardiac muscles but not in other tissues.; . . 0.15789 0.11665 -0.007201372 53.19061099 49.87337 1.38547 ITGB1P1 . . . integrin subunit beta 1 pseudogene 1 . . . . . . . . . . . ITGB2 3.87638472937311e-05 0.997791390835541 0.00216984531716531 integrin subunit beta 2 FUNCTION: Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrins alpha-M/beta-2 and alpha-X/beta-2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin alpha-X/beta-2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin alpha-M/beta-2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin alpha-M/beta-2 is also a receptor for factor X. Integrin alpha- D/beta-2 is a receptor for ICAM3 and VCAM1. Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation. {ECO:0000269|PubMed:18587400}.; DISEASE: Leukocyte adhesion deficiency 1 (LAD1) [MIM:116920]: LAD1 patients have recurrent bacterial infections and their leukocytes are deficient in a wide range of adhesion-dependent functions. {ECO:0000269|PubMed:1346613, ECO:0000269|PubMed:1347532, ECO:0000269|PubMed:1352501, ECO:0000269|PubMed:1590804, ECO:0000269|PubMed:1694220, ECO:0000269|PubMed:1968911, ECO:0000269|PubMed:20529581, ECO:0000269|PubMed:20549317, ECO:0000269|PubMed:7509236, ECO:0000269|PubMed:7686755, ECO:0000269|PubMed:9884339}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;smooth muscle;ovary;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;muscle;blood;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;white blood cells;whole blood;bone marrow; 0.24450 0.53069 -1.03070223 7.861523944 113.69861 2.32291 ITGB2-AS1 . . . ITGB2 antisense RNA 1 . . . . . . . . . . . ITGB3 0.141699544644917 0.858266504418921 3.39509361620008e-05 integrin subunit beta 3 FUNCTION: Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha- IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha- IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. Fibrinogen binding enhances SELP expression in activated platelets (By similarity). {ECO:0000250|UniProtKB:O54890, ECO:0000269|PubMed:9195946, ECO:0000303|PubMed:16322781, ECO:0000303|PubMed:17635696}.; DISEASE: Glanzmann thrombasthenia (GT) [MIM:273800]: A common inherited disease of platelet aggregation. It is characterized by mucocutaneous bleeding of mild-to-moderate severity. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb-IIIa complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the GPIIb-IIIa complex at reduced levels, have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. {ECO:0000269|PubMed:10233432, ECO:0000269|PubMed:11588040, ECO:0000269|PubMed:11897046, ECO:0000269|PubMed:12083483, ECO:0000269|PubMed:12353082, ECO:0000269|PubMed:1371279, ECO:0000269|PubMed:1438206, ECO:0000269|PubMed:15583747, ECO:0000269|PubMed:15634267, ECO:0000269|PubMed:15748237, ECO:0000269|PubMed:1602006, ECO:0000269|PubMed:20020534, ECO:0000269|PubMed:2392682, ECO:0000269|PubMed:8781422, ECO:0000269|PubMed:9215749, ECO:0000269|PubMed:9376589, ECO:0000269|PubMed:9684783, ECO:0000269|PubMed:9790984}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bleeding disorder, platelet-type 16 (BDPLT16) [MIM:187800]: An autosomal dominant form of congenital macrothrombocytopenia associated with platelet anisocytosis. It is a disorder of platelet production. Affected individuals may have no or only mildly increased bleeding tendency. In vitro studies show mild platelet functional abnormalities. {ECO:0000269|PubMed:18065693}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform beta-3A and isoform beta-3C are widely expressed. Isoform beta-3A is specifically expressed in osteoblast cells; isoform beta-3C is specifically expressed in prostate and testis.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lens;skeletal muscle;lung;cornea;placenta;macula lutea;liver;amnion;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;uterus corpus;superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;kidney;atrioventricular node;pons;trigeminal ganglion;whole blood;skeletal muscle; 0.54409 0.86055 -1.017713296 8.103326256 169.39233 2.84003 ITGB3BP 1.47054021720334e-05 0.408559846280516 0.591425448317312 integrin subunit beta 3 binding protein FUNCTION: Transcription coregulator that can have both coactivator and corepressor functions. Isoform 1, but not other isoforms, is involved in the coactivation of nuclear receptors for retinoid X (RXRs) and thyroid hormone (TRs) in a ligand-dependent fashion. In contrast, it does not coactivate nuclear receptors for retinoic acid, vitamin D, progesterone receptor, nor glucocorticoid. Acts as a coactivator for estrogen receptor alpha. Acts as a transcriptional corepressor via its interaction with the NFKB1 NF- kappa-B subunit, possibly by interfering with the transactivation domain of NFKB1. Induces apoptosis in breast cancer cells, but not in other cancer cells, via a caspase-2 mediated pathway that involves mitochondrial membrane permeabilization but does not require other caspases. May also act as an inhibitor of cyclin A- associated kinase. Also acts a component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. {ECO:0000269|PubMed:11713274, ECO:0000269|PubMed:12244126, ECO:0000269|PubMed:15082778, ECO:0000269|PubMed:15254226, ECO:0000269|PubMed:16622420}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in spleen, thymus, prostate, ovary, small intestine and white blood cells. Highly expressed in testis and colon. Isoform 4 is expressed in platelets, lymphocytes and granulocytes. {ECO:0000269|PubMed:11864709, ECO:0000269|PubMed:7593198}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pharynx;blood;skeletal muscle;bile duct;breast;lung;placenta;visual apparatus;liver;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09024 0.08559 -0.185391282 39.67916962 8.81462 0.32520 ITGB4 1.05348780207872e-11 0.999990674499279 9.32549018643716e-06 integrin subunit beta 4 FUNCTION: Integrin alpha-6/beta-4 is a receptor for laminin. Plays a critical structural role in the hemidesmosome of epithelial cells. Is required for the regulation of keratinocyte polarity and motility. {ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:19403692}.; DISEASE: Epidermolysis bullosa letalis, with pyloric atresia (EB- PA) [MIM:226730]: An autosomal recessive, frequently lethal, epidermolysis bullosa with variable involvement of skin, nails, mucosa, and with variable effects on the digestive system. It is characterized by mucocutaneous fragility, aplasia cutis congenita, and gastrointestinal atresia, which most commonly affects the pylorus. Pyloric atresia is a primary manifestation rather than a scarring process secondary to epidermolysis bullosa. {ECO:0000269|PubMed:10873890, ECO:0000269|PubMed:11251584, ECO:0000269|PubMed:11328943, ECO:0000269|PubMed:9422533, ECO:0000269|PubMed:9546354, ECO:0000269|PubMed:9792864, ECO:0000269|PubMed:9892956}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Generalized atrophic benign epidermolysis bullosa (GABEB) [MIM:226650]: A non-lethal, adult form of junctional epidermolysis bullosa characterized by life-long blistering of the skin, associated with hair and tooth abnormalities. {ECO:0000269|PubMed:10792571}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Integrin alpha-6/beta-4 is predominantly expressed by epithelia. Isoform beta-4D is also expressed in colon and placenta. Isoform beta-4E is also expressed in epidermis, lung, duodenum, heart, spleen and stomach.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;iris;testis;amniotic fluid;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;muscle;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;olfactory bulb;lung;placenta;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.16962 . -3.005715162 0.530785563 427.48664 4.31946 ITGB5 0.000480018789158923 0.998089627431449 0.0014303537793925 integrin subunit beta 5 FUNCTION: Integrin alpha-V/beta-5 (ITGAV:ITGB5) is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligand.; . . myocardium;lymphoreticular;ovary;foreskin;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;bladder;brain;gall bladder;heart;cartilage;tongue;urinary;adrenal cortex;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;aorta; superior cervical ganglion;adipose tissue;ciliary ganglion;atrioventricular node;skeletal muscle; 0.50894 0.22102 -0.282886048 33.53385232 1818.89628 7.86718 ITGB5-AS1 . . . ITGB5 antisense RNA 1 . . . . . . . . . . . ITGB6 1.90571778312696e-15 0.0269024096052202 0.973097590394778 integrin subunit beta 6 FUNCTION: Integrin alpha-V/beta-6 is a receptor for fibronectin and cytotactin. It recognizes the sequence R-G-D in its ligands. Internalisation of integrin alpha-V/beta-6 via clathrin-mediated endocytosis promotes carcinoma cell invasion. {ECO:0000269|PubMed:17545607}.; DISEASE: Amelogenesis imperfecta 1H (AI1H) [MIM:616221]: A disorder characterized by defective enamel formation, resulting in hypoplastic and hypomineralized tooth enamel that may be rough, pitted, and/or discolored. {ECO:0000269|PubMed:24305999, ECO:0000269|PubMed:24319098}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);smooth muscle;cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;skin;breast;uterus;pancreas;prostate;whole body;lung;larynx;placenta;hypopharynx;head and neck;kidney;brain;mammary gland;stomach; superior cervical ganglion;atrioventricular node;pons; 0.49818 0.25886 -0.593358137 18.22953527 250.787 3.41252 ITGB7 0.00265423920172315 0.996741035939924 0.00060472485835287 integrin subunit beta 7 FUNCTION: Integrin alpha-4/beta-7 (Peyer patches-specific homing receptor LPAM-1) is an adhesion molecule that mediates lymphocyte migration and homing to gut-associated lymphoid tissue (GALT). Integrin alpha-4/beta-7 interacts with the cell surface adhesion molecules MADCAM1 which is normally expressed by the vascular endothelium of the gastrointestinal tract. Interacts also with VCAM1 and fibronectin, an extracellular matrix component. It recognizes one or more domains within the alternatively spliced CS-1 region of fibronectin. Interactions involves the tripeptide L-D-T in MADCAM1, and L-D-V in fibronectin. Binds to HIV-1 gp120, thereby allowing the virus to enter GALT, which is thought to be the major trigger of AIDS disease. Interaction would involve a tripeptide L-D-I in HIV-1 gp120. Integrin alpha-E/beta-7 (HML-1) is a receptor for E-cadherin.; . TISSUE SPECIFICITY: Expressed in a variety of leukocyte lines.; unclassifiable (Anatomical System);lymphoreticular;lymph node;cartilage;colon;blood;bone marrow;breast;prostate;lung;endometrium;testis;brain;stomach; subthalamic nucleus;heart;white blood cells;ciliary ganglion;skeletal muscle; 0.10963 0.23174 -1.346642726 4.62962963 165.42925 2.81321 ITGB8 0.998351443978669 0.00164855455591999 1.46541057822551e-09 integrin subunit beta 8 FUNCTION: Integrin alpha-V/beta-8 is a receptor for fibronectin.; . TISSUE SPECIFICITY: Placenta, kidney, brain, ovary, uterus and in several transformed cells. Transiently expressed in 293 human embryonic kidney cells.; unclassifiable (Anatomical System);nervous;colon;skeletal muscle;breast;uterus;prostate;whole body;lung;endometrium;adrenal gland;larynx;placenta;amnion;hypopharynx;testis;head and neck;cervix;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.37327 0.22010 -0.821100135 11.88369899 155.5321 2.72541 ITGBL1 0.170877824203552 0.82854057783344 0.000581597963007633 integrin subunit beta like 1 . . TISSUE SPECIFICITY: Widely expressed in many tissues, but readily detectable only in aorta. {ECO:0000269|PubMed:10051402}.; . . 0.17697 0.12974 0.64123826 83.97617363 1434.7471 7.07106 ITIH1 4.79131815203759e-18 0.0401998913595158 0.959800108640484 inter-alpha-trypsin inhibitor heavy chain 1 FUNCTION: May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes.; . . unclassifiable (Anatomical System);heart;skeletal muscle;skin;uterus;whole body;lung;bone;liver;testis;spleen;mammary gland;gall bladder; superior cervical ganglion;fetal liver;adipose tissue;liver;appendix;fetal lung; 0.41572 0.15648 -0.830447013 11.52984194 3773.54939 12.02126 ITIH2 7.06617629312369e-10 0.964215857852165 0.0357841414412172 inter-alpha-trypsin inhibitor heavy chain 2 FUNCTION: May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes.; . TISSUE SPECIFICITY: Plasma.; unclassifiable (Anatomical System);heart;skeletal muscle;skin;uterus;whole body;lung;endometrium;liver;testis;spleen;brain;mammary gland;stomach; fetal liver;superior cervical ganglion;liver;pons;trigeminal ganglion; 0.19149 0.13139 0.146913314 63.8240151 965.90507 6.01217 ITIH3 6.66881160948057e-12 0.218856748846404 0.781143251146927 inter-alpha-trypsin inhibitor heavy chain 3 FUNCTION: May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes.; . . unclassifiable (Anatomical System);heart;ovary;cartilage;spinal cord;skin;uterus;pancreas;prostate;lung;visual apparatus;liver;testis;spleen; dorsal root ganglion;superior cervical ganglion;fetal liver;liver;fetal lung;trigeminal ganglion; 0.22459 0.11613 0.988349576 90.48714319 1061.2139 6.25087 ITIH4 4.63110952740984e-05 0.999884521941658 6.91669630681943e-05 inter-alpha-trypsin inhibitor heavy chain family member 4 FUNCTION: Type II acute-phase protein (APP) involved in inflammatory responses to trauma. May also play a role in liver development or regeneration. {ECO:0000269|PubMed:19263524}.; . TISSUE SPECIFICITY: Liver specific. {ECO:0000269|PubMed:7775381, ECO:0000269|PubMed:7805892}.; unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;parathyroid;blood;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;lung;cochlea;endometrium;epididymis;placenta;thyroid;macula lutea;liver;testis;head and neck;spleen;brain;cerebellum; . 0.33026 0.30576 -0.433580228 24.71691437 2178.33333 8.59639 ITIH4-AS1 . . . ITIH4 antisense RNA 1 . . . . . . . . . . . ITIH5 5.63852864594726e-13 0.192086048287872 0.807913951711564 inter-alpha-trypsin inhibitor heavy chain family member 5 FUNCTION: May act as a tumor suppressor.; . TISSUE SPECIFICITY: Abundantly expressed in placenta. Less abundant expression in mammary gland and ovary. Expression is barely detectable levels in all other tissues tested. {ECO:0000269|PubMed:14744536}.; unclassifiable (Anatomical System);ovary;heart;parathyroid;skin;uterus;whole body;lung;placenta;kidney;mammary gland;brain;gall bladder;thymus; dorsal root ganglion;superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.06712 0.11109 . . 1017.46752 6.13717 ITIH6 9.88847044832986e-11 0.154840293065059 0.845159706836056 inter-alpha-trypsin inhibitor heavy chain family member 6 . . . cartilage;bone;spinal cord;mammary gland;skin; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07794 . 2.568727078 98.7438075 765.43774 5.48050 ITK 1.49550808638438e-05 0.998259486010605 0.00172555890853078 IL2 inducible T-cell kinase FUNCTION: Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. When antigen presenting cells (APC) activate T-cell receptor (TCR), a series of phosphorylation lead to the recruitment of ITK to the cell membrane, in the vicinity of the stimulated TCR receptor, where it is phosphorylated by LCK. Phosphorylation leads to ITK autophosphorylation and full activation. Once activated, phosphorylates PLCG1, leading to the activation of this lipase and subsequent cleavage of its substrates. In turn, the endoplasmic reticulum releases calcium in the cytoplasm and the nuclear activator of activated T-cells (NFAT) translocates into the nucleus to perform its transcriptional duty. Phosphorylates 2 essential adapter proteins: the linker for activation of T-cells/LAT protein and LCP2. Then, a large number of signaling molecules such as VAV1 are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. {ECO:0000269|PubMed:12186560, ECO:0000269|PubMed:12682224, ECO:0000269|PubMed:21725281}.; DISEASE: Lymphoproliferative syndrome 1 (LPFS1) [MIM:613011]: A rare immunodeficiency characterized by extreme susceptibility to infection with Epstein-Barr virus (EBV). Inadequate immune response to EBV can have a fatal outcome. Clinical features include splenomegaly, lymphadenopathy, anemia, thrombocytopenia, pancytopenia, recurrent infections. There is an increased risk for lymphoma. {ECO:0000269|PubMed:19425169}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: T-cell lines and natural killer cell lines.; . . 0.56840 0.36677 -0.224023033 37.4321774 57.98934 1.53970 ITLN1 0.00489119365441958 0.966926189351296 0.0281826169942844 intelectin 1 FUNCTION: Has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes. Increases AKT phosphorylation in the absence and presence of insulin. May play a role in the defense system against microorganisms. May specifically recognize carbohydrate chains of pathogens and bacterial components containing galactofuranosyl residues, in a calcium-dependent manner. May be involved in iron metabolism. {ECO:0000269|PubMed:11313366, ECO:0000269|PubMed:16531507}.; . TISSUE SPECIFICITY: Highly expressed in omental adipose tissue where it is found in stromal vascular cells but not in fat cells but is barely detectable in subcutaneous adipose tissue (at protein level). Highly expressed in the small intestine. Also found in the heart, testis, colon, salivary gland, skeletal muscle, pancreas and thyroid and, to a lesser degree, in the uterus, spleen, prostate, lymph node and thymus. {ECO:0000269|PubMed:11181563, ECO:0000269|PubMed:11313366, ECO:0000269|PubMed:11747454, ECO:0000269|PubMed:16531507}.; unclassifiable (Anatomical System);meninges;urinary;colon;skeletal muscle;skin;pia mater;atrium;lung;liver;testis;spleen;dura mater;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07681 0.15307 -0.44448505 24.46331682 97.90988 2.13920 ITLN2 1.15271947267602e-05 0.587962452728983 0.41202602007629 intelectin 2 FUNCTION: May play a role in the defense system against pathogens. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed only in the small intestine. {ECO:0000269|PubMed:11181563}.; . . 0.02404 0.07581 0.799205007 87.58551545 431.00702 4.33148 ITM2A 0.84271835183677 0.154386273141259 0.0028953750219711 integral membrane protein 2A . . . . . 0.27062 0.12378 0.080983847 59.76055674 42.98965 1.24332 ITM2B 0.715126636356634 0.281665429135731 0.00320793450763504 integral membrane protein 2B FUNCTION: Plays a regulatory role in the processing of the beta- amyloid A4 precursor protein (APP) and acts as an inhibitor of the beta-amyloid peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites.; FUNCTION: Bri23 peptide prevents aggregation of APP beta-amyloid protein 42 peptide into toxic oligomers.; DISEASE: Cerebral amyloid angiopathy, ITM2B-related 1 (CAA-ITM2B1) [MIM:176500]: A disorder characterized by amyloid deposition in the walls of cerebral blood vessels and neurodegeneration in the central nervous system. Cerebral amyloid angiopathy, non-neuritic and perivascular plaques and neurofibrillary tangles are the predominant pathological lesions. Clinical features include progressive mental deterioration, spasticity and muscular rigidity. {ECO:0000269|PubMed:10391242, ECO:0000269|PubMed:10526337, ECO:0000269|PubMed:14656991}. Note=The disease is caused by mutations affecting the gene represented in this entry. A single base substitution at the stop codon of ITM2B generates a 277-residue precursor that is cleaved at the normal furin processing site to generate the ABri amyloidogenic peptide (PubMed:10391242). ABri accumulates in the brain and produces amyloid fibrils responsible for neuronal dysfunction and dementia. ABri peptide variant forms fibrils in vitro (PubMed:10526337). {ECO:0000269|PubMed:10391242, ECO:0000269|PubMed:10526337}.; DISEASE: Cerebral amyloid angiopathy, ITM2B-related 2 (CAA-ITM2B2) [MIM:117300]: A disorder characterized by amyloid deposition in the walls of the blood vessels of the cerebrum, choroid plexus, cerebellum, spinal cord and retina. Plaques and neurofibrillary tangles are observed in the hippocampus. Clinical features include progressive ataxia, dementia, cataracts and deafness. {ECO:0000269|PubMed:10781099, ECO:0000269|PubMed:14656991, ECO:0000269|PubMed:16091362}. Note=The disease is caused by mutations affecting the gene represented in this entry. A decamer duplication in the 3' region of ITM2B results in the production of the ADan amyloidogenic peptide (PubMed:10781099). ADan is generated by cleavage of the mutated precursor at the normal furin processing site. ADan accumulates in the brain and produces amyloid fibrils responsible for neuronal dysfunction and dementia. {ECO:0000269|PubMed:10781099}.; DISEASE: Retinal dystrophy with inner retinal dysfunction and ganglion cell abnormalities (RDGCA) [MIM:616079]: An autosomal dominant retinal dystrophy characterized by inner retinal dysfunction in association with ganglion cell abnormalities. Clinical features include mild photophobia, progressive loss of central vision, night blindness, and hyperreflectivity of nerve and ganglion cell layers. {ECO:0000269|PubMed:24026677}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Expressed in brain.; . . 0.22899 0.31462 -0.141298762 42.87567823 166.88489 2.82341 ITM2BP1 . . . integral membrane protein 2B pseudogene 1 . . . . . . . . . . . ITM2C 0.208530379146834 0.782193428062386 0.00927619279077952 integral membrane protein 2C FUNCTION: Negative regulator of beta amyloid peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C- terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:18452648, ECO:0000269|PubMed:19366692}.; . TISSUE SPECIFICITY: High levels in the brain, specifically in the cerebral cortex, medulla, amygdala, hippocampus, thalamus, caudate nucleus, cerebellum, olfactory lobe and spinal cord. Very low levels in other organs. {ECO:0000269|PubMed:11290423, ECO:0000269|PubMed:15606899}.; ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;duodenum;kidney;aorta;stomach;thymus; amygdala;whole brain;medulla oblongata;thalamus;occipital lobe;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.21096 0.11213 -0.358119787 29.16371786 80.18985 1.89337 ITPA 8.97319725886936e-05 0.784204544994953 0.215705723032458 inosine triphosphatase FUNCTION: Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. {ECO:0000255|HAMAP-Rule:MF_03148, ECO:0000269|PubMed:17090528}.; DISEASE: Epileptic encephalopathy, early infantile, 35 (EIEE35) [MIM:616647]: A form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. EIEE35 is characterized by onset of seizures in the first months of life associated with essentially no normal development. Many patients die in early childhood. {ECO:0000269|PubMed:26224535}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, liver, sex glands, thyroid and adrenal gland.; . . 0.05261 0.46909 0.060756528 58.52795471 879.41235 5.77498 ITPK1 0.987051326793078 0.0129431678048672 5.50540205475672e-06 inositol-tetrakisphosphate 1-kinase FUNCTION: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. Phosphorylates Ins(3,4,5,6)P4 at position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor of plasma membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5 is not. Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate (InsP6) pathway. Also acts as an inositol polyphosphate phosphatase that dephosphorylate Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 to Ins(1,3,4)P3, and Ins(1,3,4,5,6)P5 to Ins(3,4,5,6)P4. May also act as an isomerase that interconverts the inositol tetrakisphosphate isomers Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 in the presence of ADP and magnesium. Probably acts as the rate-limiting enzyme of the InsP6 pathway. Modifies TNF-alpha-induced apoptosis by interfering with the activation of TNFRSF1A-associated death domain. {ECO:0000269|PubMed:11909533, ECO:0000269|PubMed:12925536, ECO:0000269|PubMed:17616525}.; . TISSUE SPECIFICITY: Expressed in brain > heart > skeletal muscle = kidney = pancreas = liver = placenta > lung. In brain, it is expressed in cerebellum, cerebral cortex, medulla, spinal cord, occipital lobe, frontal lobe, temporal lobe and putamen. {ECO:0000269|PubMed:8662638}.; ovary;colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;brain;pineal gland;amygdala;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;blood;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; whole brain;dorsal root ganglion;amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;atrioventricular node;pons;caudate nucleus;skeletal muscle;uterus corpus;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.21083 0.11469 -0.446304853 24.33356924 84.85998 1.96260 ITPK1-AS1 . . . ITPK1 antisense RNA 1 . . . . . . . . . . . ITPKA 0.821022368669755 0.178116019769882 0.000861611560362586 inositol-trisphosphate 3-kinase A . . . medulla oblongata;lung;cartilage;hypothalamus;bone;placenta;hippocampus;testis;colon;blood;kidney;brain;stomach; whole brain;amygdala;subthalamic nucleus;occipital lobe;medulla oblongata;temporal lobe;prefrontal cortex;globus pallidus;pons;caudate nucleus;cingulate cortex;parietal lobe; 0.21376 0.12708 . . 45.24026 1.29149 ITPKB 0.998850076050969 0.00114990907582194 1.48732094036428e-08 inositol-trisphosphate 3-kinase B . . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; thalamus;subthalamic nucleus;olfactory bulb;hypothalamus;spinal cord;prefrontal cortex;globus pallidus;caudate nucleus;parietal lobe;cingulate cortex;cerebellum; 0.10372 0.11314 -0.25902169 34.96697334 5572.39775 15.42362 ITPKB-AS1 . . . ITPKB antisense RNA 1 . . . . . . . . . . . ITPKB-IT1 . . . ITPKB intronic transcript 1 . . . . . . . . . . . ITPKC 0.164215304256506 0.835156873570036 0.000627822173457721 inositol-trisphosphate 3-kinase C FUNCTION: Can phosphorylate inositol 2,4,5-triphosphate to inositol 2,4,5,6-tetraphosphate. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in pancreas, skeletal muscle, liver, placenta and weakly in kidney and brain. {ECO:0000269|PubMed:11085927}.; ovary;colon;parathyroid;choroid;skin;retina;uterus;optic nerve;larynx;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;liver;hypopharynx;spleen;head and neck;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skin;skeletal muscle;cerebellum; 0.29287 0.09326 -0.50880549 21.72682236 229.14861 3.27018 ITPR1 0.999999999994095 5.90486917436413e-12 3.23932294877579e-32 inositol 1,4,5-trisphosphate receptor type 1 FUNCTION: Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5- trisphosphate. Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1 (By similarity). Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways (By similarity). {ECO:0000250|UniProtKB:P11881}.; DISEASE: Spinocerebellar ataxia 15 (SCA15) [MIM:606658]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA15 is an autosomal dominant cerebellar ataxia (ADCA). It is very slow progressing form with a wide range of onset, ranging from childhood to adult. Most patients remain ambulatory. {ECO:0000269|PubMed:17590087, ECO:0000269|PubMed:18579805}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spinocerebellar ataxia 29 (SCA29) [MIM:117360]: An autosomal dominant, congenital spinocerebellar ataxia characterized by early motor delay, hypotonia and mild cognitive delay. Affected individuals develop a very slowly progressive or non-progressive gait and limb ataxia associated with cerebellar atrophy on brain imaging. Additional variable features include nystagmus, dysarthria, and tremor. {ECO:0000269|PubMed:22986007}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed.; ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;liver;cervix;spleen;kidney;mammary gland;aorta; whole brain;amygdala;occipital lobe;medulla oblongata;cerebellum peduncles;temporal lobe;pons;caudate nucleus;subthalamic nucleus;thyroid;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.48957 0.45360 -3.352519381 0.401037981 228.28209 3.26405 ITPR1-AS1 . . . ITPR1 antisense RNA 1 (head to head) . . . . . . . . . . . ITPR2 5.7359279512263e-11 0.999999999940341 2.29974168405986e-12 inositol 1,4,5-trisphosphate receptor type 2 FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. This release is regulated by cAMP both dependently and independently of PKA (By similarity). {ECO:0000250|UniProtKB:Q9Z329}.; DISEASE: Anhidrosis, isolated, with normal sweat glands (ANHD) [MIM:106190]: An autosomal recessive disorder characterized by generalized, isolated anhidrosis, severe heat intolerance, and morphologically normal eccrine sweat glands. Body growth, teeth, hair, nails, and skin are normal. {ECO:0000269|PubMed:25329695}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform Short is found in skeletal muscle and heart.; unclassifiable (Anatomical System);germinal center; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; 0.90112 0.20622 -1.641009998 2.777777778 698.25496 5.25954 ITPR3 4.97536705049387e-12 0.999999998115583 1.87944123431593e-09 inositol 1,4,5-trisphosphate receptor type 3 FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium.; . TISSUE SPECIFICITY: Expressed in intestinal crypt and villus epithelial cells.; . . 0.69563 . -4.091558817 0.165133286 605.21718 4.97953 ITPRIP 1.35269477140853e-05 0.393078368816165 0.60690810423612 inositol 1,4,5-trisphosphate receptor interacting protein FUNCTION: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5- triphosphate receptor (ITPR) Ca(2+) release. {ECO:0000269|PubMed:16990268}.; . TISSUE SPECIFICITY: Detected in brain where it is concentrated in cerebellar Purkinje cells (at protein level). {ECO:0000269|PubMed:16990268}.; colon;fovea centralis;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;adrenal cortex;blood;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skeletal muscle; 0.34404 0.13209 -0.552898813 19.86317528 126.56194 2.45063 ITPRIPL1 1.10905298650302e-07 0.186852911170271 0.81314697792443 inositol 1,4,5-trisphosphate receptor interacting protein-like 1 . . . unclassifiable (Anatomical System);medulla oblongata;pancreas;lung;heart;lacrimal gland;visual apparatus;testis;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.27008 0.10029 0.444637294 77.91342298 . . ITPRIPL2 0.0185033935717135 0.896702884773171 0.0847937216551158 inositol 1,4,5-trisphosphate receptor interacting protein-like 2 . . . . . . . 0.551232944 81.48148148 484.31785 4.52979 ITSN1 0.999999973635691 2.63643088082222e-08 1.03024379268079e-24 intersectin 1 FUNCTION: Acts as guanine nucleotide exchange factor (GEF) specific for the CDC42 GTPase (By similarity). Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2. Isoform 1 could be involved in brain-specific synaptic vesicle recycling. Inhibits ARHGAP31 activity toward RAC1. {ECO:0000250, ECO:0000269|PubMed:11744688, ECO:0000269|PubMed:22648170}.; . TISSUE SPECIFICITY: Isoform 2 is ubiquitous in adult and fetal tissues with high expression in skeletal muscle, heart, spleen, ovary, testis and all fetal tissues tested and low expression in thymus, blood, lung, liver and pancreas. Isoform 1 is expressed almost exclusively in the brain, in all brain regions. Not expressed in the spinal cord.; . . 0.71844 0.20204 -2.010049157 1.72210427 541.34142 4.73891 ITSN2 0.0244336907969597 0.975566309202489 5.51616705292503e-13 intersectin 2 FUNCTION: Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles (CCPs). Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000269|PubMed:19458185, ECO:0000269|PubMed:22648170, ECO:0000269|PubMed:23999003}.; . TISSUE SPECIFICITY: Expressed in melanocytes (PubMed:23999003). Ubiquitous. Isoform 1 is primarily expressed in adult heart and liver. {ECO:0000269|PubMed:23999003}.; ovary;developmental;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;liver;spleen;head and neck;cervix;kidney;aorta;stomach;cerebellum; dorsal root ganglion;medulla oblongata;superior cervical ganglion;tongue;atrioventricular node;pons;skeletal muscle;thyroid;prefrontal cortex;globus pallidus;appendix;testis;ciliary ganglion;trigeminal ganglion; 0.30109 0.18256 -0.512707122 21.42014626 4780.84117 14.02023 IV . . . inversus situs, viscerum . . . . . . . . . . . IVD 1.7312786559084e-11 0.0579628458354764 0.942037154147211 isovaleryl-CoA dehydrogenase . DISEASE: Isovaleric acidemia (IVA) [MIM:243500]: A metabolic disorder characterized by retarded psychomotor development, a peculiar odor resembling sweaty feet, an aversion to dietary protein, and pernicious vomiting, leading to acidosis and coma. The acute neonatal form leads to massive metabolic acidosis from the first days of life and rapid death. {ECO:0000269|PubMed:2063866, ECO:0000269|PubMed:22004070, ECO:0000269|PubMed:22350545, ECO:0000269|PubMed:23587913, ECO:0000269|PubMed:9665741}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;larynx;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;lung;cornea;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;liver;atrioventricular node; 0.10008 0.46183 -0.290161348 33.33923095 67.94876 1.70487 IVL 3.43124628664551e-09 0.0935048335500698 0.906495163018684 involucrin FUNCTION: Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia.; . TISSUE SPECIFICITY: Keratinocytes of epidermis and other stratified squamous epithelia.; . . 0.37637 . 0.53464283 81.00967209 386.0752 4.13780 IVNS1ABP 0.999065766116616 0.000934233516336977 3.67046667963877e-10 influenza virus NS1A binding protein FUNCTION: Plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats. Protects cells from cell death induced by actin destabilization; Protects neurons from dendritic spines and actin filaments damage induced by the actin-destabilizing cytochalasin B when overexpressed. Activates Erk signaling pathway when overexpressed in cultured cell lines (By similarity). May be a component of the cellular splicing machinery with a role in pre-mRNA splicing; may mediate the inhibition of splicing by NS/influenza virus NS1A protein. Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription. {ECO:0000250, ECO:0000269|PubMed:16582008}.; . . . . 0.27885 0.16516 -0.22584292 37.32012267 63.06651 1.62473 IWS1 0.986444880095647 0.0135551095670738 1.033727876714e-08 IWS1, SUPT6H interacting protein FUNCTION: Transcription factor which plays a key role in defining the composition of the RNA polymerase II (RNAPII) elongation complex and in modulating the production of mature mRNA transcripts. Acts as an assembly factor to recruit various factors to the RNAPII elongation complex and is recruited to the complex via binding to the transcription elongation factor SUPT6H bound to the C-terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone modifying enzymes (such as SETD2) to ensure proper mRNA splicing, efficient mRNA export and elongation-coupled H3K36 methylation, a signature chromatin mark of active transcription. {ECO:0000269|PubMed:17184735, ECO:0000269|PubMed:17234882, ECO:0000269|PubMed:19141475}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;nervous;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.29485 0.10290 0.176444282 66.07100731 273.87474 3.54559 IYD 0.0883091920429625 0.870370232658905 0.041320575298133 iodotyrosine deiodinase FUNCTION: Catalyzes the oxidative NADPH-dependent deiodination of monoiodotyrosine (L-MIT) or diiodotyrosine (L-DIT). Acts during the hydrolysis of thyroglobulin to liberate iodide, which can then reenter the hormone-producing pathways. Acts more efficiently on monoiodotyrosine than on diiodotyrosine. {ECO:0000269|PubMed:15289438}.; . TISSUE SPECIFICITY: Expressed at a high level in thyroid gland and at lower level in kidney and trachea. {ECO:0000269|PubMed:15289438}.; unclassifiable (Anatomical System);breast;smooth muscle;lung;thyroid;liver;colon;spleen;kidney;mammary gland;stomach; thyroid;ciliary ganglion;skeletal muscle;cerebellum; 0.09323 0.16732 1.997187788 97.66454352 652.18896 5.12233 IZUMO1 0.00241626337305742 0.981311504321056 0.0162722323058868 izumo sperm-egg fusion 1 FUNCTION: Essential sperm cell-surface protein required for fertilization by acting as a ligand for IZUMO1R/JUNO receptor on egg. The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. The ligand-receptor interaction probably does not act as a membrane 'fusogen'. {ECO:0000269|PubMed:15759005}.; . TISSUE SPECIFICITY: Sperm-specific (at protein level). Detectable on sperm surface only after the acrosome reaction. {ECO:0000269|PubMed:15759005}.; unclassifiable (Anatomical System);medulla oblongata;testis; . 0.02091 0.14042 -0.22584292 37.32012267 7.89951 0.29016 IZUMO1R . . . IZUMO1 receptor, JUNO FUNCTION: Receptor for IZUMO1 present at the cell surface of oocytes (oolemma), which is essential for gamete recognition and fertilization. The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. The ligand- receptor interaction probably does not act as a membrane 'fusogen'. Does not bind folate (By similarity). {ECO:0000250}.; . . . . . . . . . . IZUMO2 1.06861878364753e-05 0.571436237860881 0.428553075951283 IZUMO family member 2 . . . lung;testis; . 0.06271 0.05951 -0.161524709 41.6430762 . . IZUMO3 . . . IZUMO family member 3 . . . . . . . . . 186.4911 2.96524 IZUMO4 4.69904233416224e-08 0.214031976295796 0.785967976713781 IZUMO family member 4 . . TISSUE SPECIFICITY: Detected in sperm. {ECO:0000269|Ref.1}.; unclassifiable (Anatomical System);medulla oblongata;lung;ovary;cerebral cortex;oesophagus;hypothalamus;placenta;iris;testis;parathyroid;germinal center;brain; testis - interstitial;testis - seminiferous tubule;testis; 0.33266 . 0.062575634 58.74026893 106.42178 2.23844 JADE1 . . . jade family PHD finger 1 FUNCTION: Component of the HBO1 complex which has a histone H4- specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Transcriptional coactivator, it may also promote acetylation of nucleosomal histone H4 by KAT5. Promotes apoptosis. May act as a renal tumor suppressor. {ECO:0000269|PubMed:15502158, ECO:0000269|PubMed:16046545, ECO:0000269|PubMed:16387653}.; . TISSUE SPECIFICITY: Highly expressed in kidney. Also present in pancreas, liver and heart (at protein level). Down-regulated in renal cancer cells. {ECO:0000269|PubMed:12169691, ECO:0000269|PubMed:16046545}.; . . 0.82305 0.12723 -0.50880549 21.72682236 267.28633 3.50609 JADE2 . . . jade family PHD finger 2 FUNCTION: Component of the HBO1 complex which has a histone H4- specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. {ECO:0000269|PubMed:16387653}.; . . . . 0.54969 0.10930 -0.484940685 22.75300778 183.73703 2.94069 JADE3 . . . jade family PHD finger 3 FUNCTION: Component of the HBO1 complex which has a histone H4- specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. {ECO:0000269|PubMed:16387653}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in placenta and uterus. {ECO:0000269|PubMed:10775800}.; . . 0.41911 0.10105 -0.47017169 23.25430526 26.26202 0.85146 JADRR . . . JADE1 adjacent regulatory RNA . . . . . . . . . . . JAG1 0.999999615868819 3.84131180560308e-07 1.02421125982363e-17 jagged 1 FUNCTION: Ligand for multiple Notch receptors and involved in the mediation of Notch signaling. May be involved in cell-fate decisions during hematopoiesis. Seems to be involved in early and late stages of mammalian cardiovascular development. Inhibits myoblast differentiation (By similarity). Enhances fibroblast growth factor-induced angiogenesis (in vitro). {ECO:0000250, ECO:0000269|PubMed:18660822, ECO:0000269|PubMed:9462510}.; DISEASE: Alagille syndrome 1 (ALGS1) [MIM:118450]: A form of Alagille syndrome, an autosomal dominant multisystem disorder. It is clinically defined by hepatic bile duct paucity and cholestasis in association with cardiac, skeletal, and ophthalmologic manifestations. There are characteristic facial features and less frequent clinical involvement of the renal and vascular systems. {ECO:0000269|PubMed:10220506, ECO:0000269|PubMed:10533065, ECO:0000269|PubMed:11058898, ECO:0000269|PubMed:11139247, ECO:0000269|PubMed:11157803, ECO:0000269|PubMed:11180599, ECO:0000269|PubMed:12442286, ECO:0000269|PubMed:12497640, ECO:0000269|PubMed:15712272, ECO:0000269|PubMed:16575836, ECO:0000269|PubMed:23801938, ECO:0000269|PubMed:9207788, ECO:0000269|PubMed:9585603}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Tetralogy of Fallot (TOF) [MIM:187500]: A congenital heart anomaly which consists of pulmonary stenosis, ventricular septal defect, dextroposition of the aorta (aorta is on the right side instead of the left) and hypertrophy of the right ventricle. In this condition, blood from both ventricles (oxygen-rich and oxygen-poor) is pumped into the body often causing cyanosis. {ECO:0000269|PubMed:11152664}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues. In cervix epithelium expressed in undifferentiated subcolumnar reserve cells and squamous metaplasia. Expression is up-regulated in cervical squamous cell carcinoma. Expressed in bone marrow cell line HS-27a which supports the long-term maintenance of immature progenitor cells.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; dorsal root ganglion;uterus;superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skin; 0.66304 0.70469 -2.142391463 1.486199575 537.31129 4.72505 JAG2 0.990248880592838 0.00975111847464722 9.32514492675349e-10 jagged 2 FUNCTION: Putative Notch ligand involved in the mediation of Notch signaling. Involved in limb development (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in heart, placenta and skeletal muscle and to a lesser extend in pancreas. Very low expression in brain, lung, liver and kidney.; unclassifiable (Anatomical System);myocardium;lymph node;heart;ovary;hypothalamus;colon;parathyroid;blood;choroid;retina;uterus;prostate;lung;frontal lobe;endometrium;placenta;visual apparatus;duodenum;testis;brain;mammary gland;stomach;peripheral nerve; amygdala;medulla oblongata;superior cervical ganglion;prefrontal cortex;globus pallidus;pons;trigeminal ganglion;parietal lobe; 0.80195 0.35423 -1.295313867 4.989384289 1016.07158 6.13353 JAGN1 0.0230627329552788 0.767708956468001 0.20922831057672 jagunal homolog 1 FUNCTION: Endoplasmic reticulum transmembrane protein involved in vesicle-mediated transport, which is required for neutrophil function. Required for vesicle-mediated transport; it is however unclear whether it is involved in early secretory pathway or intracellular protein transport. Acts as a regulator of neutrophil function, probably via its role in vesicle-mediated transport: required for defense against fungal pathogens and for granulocyte colony-stimulating factor (GM-CSF) signaling pathway; possibly by regulating glycosylation and/or targeting of proteins contributing to the viability and migration of neutrophils. {ECO:0000269|PubMed:25129144, ECO:0000305}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:25129144}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;duodenum;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum; superior cervical ganglion;liver;globus pallidus;ciliary ganglion;atrioventricular node; 0.06841 . 0.148941568 64.31941496 178.87629 2.90587 JAK1 0.995909680354616 0.00409031962283366 2.25507499352604e-11 Janus kinase 1 FUNCTION: Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor. {ECO:0000269|PubMed:11909529}.; . TISSUE SPECIFICITY: Expressed at higher levels in primary colon tumors than in normal colon tissue. The expression level in metastatic colon tumors is comparable to the expression level in normal colon tissue. {ECO:0000269|PubMed:7896447}.; smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; thalamus;whole blood; 0.95076 0.17388 -1.330032624 4.688605803 66.80502 1.68715 JAK2 0.969034926832703 0.0309650730343205 1.32976647994419e-10 Janus kinase 2 FUNCTION: Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins. Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating CDKN1B. Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin. {ECO:0000269|PubMed:12023369, ECO:0000269|PubMed:19783980, ECO:0000269|PubMed:20098430, ECO:0000269|PubMed:21423214}.; DISEASE: Note=Chromosomal aberrations involving JAK2 are found in both chronic and acute forms of eosinophilic, lymphoblastic and myeloid leukemia. Translocation t(8;9)(p22;p24) with PCM1 links the protein kinase domain of JAK2 to the major portion of PCM1. Translocation t(9;12)(p24;p13) with ETV6.; DISEASE: Budd-Chiari syndrome (BDCHS) [MIM:600880]: A syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera. {ECO:0000269|PubMed:16707754}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Polycythemia vera (PV) [MIM:263300]: A myeloproliferative disorder characterized by abnormal proliferation of all hematopoietic bone marrow elements, erythroid hyperplasia, an absolute increase in total blood volume, but also by myeloid leukocytosis, thrombocytosis and splenomegaly. {ECO:0000269|PubMed:15781101, ECO:0000269|PubMed:15793561, ECO:0000269|PubMed:15858187, ECO:0000269|PubMed:16603627}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Thrombocythemia 3 (THCYT3) [MIM:614521]: A myeloproliferative disorder characterized by excessive platelet production, resulting in increased numbers of circulating platelets. It can be associated with spontaneous hemorrhages and thrombotic episodes. {ECO:0000269|PubMed:16325696, ECO:0000269|PubMed:22397670}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Myelofibrosis (MYELOF) [MIM:254450]: A disorder characterized by replacement of the bone marrow by fibrous tissue, occurring in association with a myeloproliferative disorder. Clinical manifestations may include anemia, pallor, splenomegaly, hypermetabolic state, petechiae, ecchymosis, bleeding, lymphadenopathy, hepatomegaly, portal hypertension. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. {ECO:0000269|PubMed:16247455}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed throughout most tissues. {ECO:0000269|PubMed:16424865}.; . . 0.93853 0.93439 -0.371072278 28.22009908 210.76885 3.13144 JAK3 0.995863799803735 0.0041362000817402 1.14524465678421e-10 Janus kinase 3 FUNCTION: Non-receptor tyrosine kinase involved in various processes such as cell growth, development, or differentiation. Mediates essential signaling events in both innate and adaptive immunity and plays a crucial role in hematopoiesis during T-cells development. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors sharing the common subunit gamma such as IL2R, IL4R, IL7R, IL9R, IL15R and IL21R. Following ligand binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, upon IL2R activation by IL2, JAK1 and JAK3 molecules bind to IL2R beta (IL2RB) and gamma chain (IL2RG) subunits inducing the tyrosine phosphorylation of both receptor subunits on their cytoplasmic domain. Then, STAT5A AND STAT5B are recruited, phosphorylated and activated by JAK1 and JAK3. Once activated, dimerized STAT5 translocates to the nucleus and promotes the transcription of specific target genes in a cytokine-specific fashion. {ECO:0000269|PubMed:11909529, ECO:0000269|PubMed:20440074, ECO:0000269|PubMed:7662955, ECO:0000269|PubMed:8022485}.; DISEASE: Severe combined immunodeficiency autosomal recessive T- cell-negative/B-cell-positive/NK-cell-negative (T(-)B(+)NK(-) SCID) [MIM:600802]: A form of severe combined immunodeficiency (SCID), a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development. {ECO:0000269|PubMed:10982185, ECO:0000269|PubMed:14615376, ECO:0000269|PubMed:7659163, ECO:0000269|PubMed:9354668, ECO:0000269|PubMed:9753072}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In NK cells and an NK-like cell line but not in resting T-cells or in other tissues. The S-form is more commonly seen in hematopoietic lines, whereas the B-form is detected in cells both of hematopoietic and epithelial origins. {ECO:0000269|PubMed:7535338}.; . . . 0.13509 -0.993849454 8.56334041 301.14007 3.69742 JAKMIP1 0.993166783894696 0.00683321417526534 1.93003838491814e-09 janus kinase and microtubule interacting protein 1 FUNCTION: Associates with microtubules and may play a role in the microtubule-dependent transport of the GABA-B receptor. May play a role in JAK1 signaling and regulate microtubule cytoskeleton rearrangements. {ECO:0000269|PubMed:14718537, ECO:0000269|PubMed:15277531, ECO:0000269|PubMed:17532644}.; . TISSUE SPECIFICITY: Predominantly expressed in neural tissues and lymphoid cells (at protein level). Isoform 2, isoform 3 and isoform 4 are specifically expressed in brain and retina. Isoform 1 and isoform 5 are also detected in liver, lung and skeletal muscle. Also detected in testis and to a lower extent spleen and intestine. {ECO:0000269|PubMed:15277531, ECO:0000269|PubMed:17761393}.; unclassifiable (Anatomical System);optic nerve;frontal lobe;hypothalamus;bone;macula lutea;testis;blood;fovea centralis;choroid;lens;brain;retina; subthalamic nucleus;temporal lobe;globus pallidus;cingulate cortex; 0.62649 0.10445 -1.618506764 2.925218212 44.3849 1.27299 JAKMIP2 0.999936528336512 6.34716633817458e-05 1.06053332560492e-13 janus kinase and microtubule interacting protein 2 . . TISSUE SPECIFICITY: Highly expressed in brain, moderately expressed in thymus, spleen and lung, and weakly expressed in kidney, liver and peripheral blood lymphocytes. Also expressed in adrenal and pituitary glands, as well as testis. {ECO:0000269|PubMed:15277531, ECO:0000269|PubMed:17572408}.; amygdala;unclassifiable (Anatomical System);heart;cerebellum cortex;hypothalamus;sympathetic chain;muscle;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;optic nerve;lung;cochlea;bone;macula lutea;visual apparatus;hippocampus;alveolus;brain;cerebellum; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.66287 0.12537 -1.199555187 5.761972163 105.04961 2.21693 JAKMIP2-AS1 . . . JAKMIP2 antisense RNA 1 . . . . . . . . . . . JAKMIP3 0.053931825098127 0.946033316776411 3.48581254621326e-05 Janus kinase and microtubule interacting protein 3 . . TISSUE SPECIFICITY: Specifically expressed in the CNS and endocrine tissues. Also detected in other tissues including heart, testis and prostate. {ECO:0000269|PubMed:17572408}.; . . 0.23757 0.10589 -1.741783094 2.418023119 1261.00407 6.69525 JAM2 0.148660697111206 0.847628407329751 0.00371089555904283 junctional adhesion molecule 2 FUNCTION: May play a role in the processes of lymphocyte homing to secondary lymphoid organs.; . TISSUE SPECIFICITY: Highest expression in the heart, placenta, lung, foreskin and lymph node. Prominently expressed on high endothelial venules, also present on the endothelia of other vessels. Localized to the intercellular boundaries of high endothelial cells. {ECO:0000269|PubMed:10779521}.; unclassifiable (Anatomical System);heart;hypothalamus;choroid;skin;uterus;lung;frontal lobe;placenta;liver;testis;spleen;brain;tonsil;thymus; superior cervical ganglion;testis;trigeminal ganglion; 0.04655 0.10225 0.527368849 80.73248408 364.51364 4.04101 JAM3 0.000178704009379398 0.890491410035774 0.109329885954847 junctional adhesion molecule 3 FUNCTION: Participates in cell-cell adhesion. It is a counter- receptor for ITGAM, mediating leukocyte-platelet interactions and is involved in the regulation of transepithelial migration of polymorphonuclear neutrophils (PMN). The soluble form is a mediator of angiogenesis. {ECO:0000269|PubMed:12208882, ECO:0000269|PubMed:15194813, ECO:0000269|PubMed:20592283}.; DISEASE: Hemorrhagic destruction of the brain with subependymal calcification and cataracts (HDBSCC) [MIM:613730]: A syndrome characterized by congenital cataracts and severe brain abnormalities apparently resulting from hemorrhagic destruction of the brain parenchyma, including the cerebral white matter and basal ganglia. Patients manifest profound developmental delay, and other neurologic features included seizures, spasticity, and hyperreflexia. The clinical course is very severe resulting in death in infancy. Brain imaging shows multifocal intraparenchymal hemorrhage with associated liquefaction and massive cystic degeneration, and calcification in the subependymal region and in brain tissue. {ECO:0000269|PubMed:21109224, ECO:0000269|PubMed:23255084}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest expression in placenta, brain and kidney. Significant expression is detected on platelets. Expressed in intestinal mucosa cells. Expressed in the vascular endothelium. Found in serum (at protein level). Also detected in the synovial fluid of patients with rheumatoid arthritis, psoriatic arthritis or ostearthritis (at protein level). {ECO:0000269|PubMed:11590146, ECO:0000269|PubMed:11944976, ECO:0000269|PubMed:12208882, ECO:0000269|PubMed:15194813, ECO:0000269|PubMed:15994945, ECO:0000269|PubMed:20592283}.; myocardium;ovary;parathyroid;choroid;vein;skin;bone marrow;uterus;prostate;atrium;whole body;frontal lobe;cerebral cortex;larynx;bone;thyroid;testis;amniotic fluid;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;spinal cord;urinary;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;head and neck;spleen;kidney;stomach;peripheral nerve;thymus; occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;olfactory bulb;testis - seminiferous tubule;placenta;prefrontal cortex;testis;ciliary ganglion;atrioventricular node;caudate nucleus;parietal lobe; 0.13106 0.14931 0.218717575 68.27081859 107.10268 2.24551 JAML . . . junction adhesion molecule like FUNCTION: Transmembrane protein of the plasma membrane of leukocytes that control their migration and activation through interaction with CXADR, a plasma membrane receptor found on adjacent epithelial and endothelial cells. The interaction between both receptors mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, AMICA1 induces downstream cell signaling events in gamma-delta T- cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T- cells that in turn stimulate epithelial tissues repair. It also controls the transmigration of leukocytes within epithelial and endothelial tissues through adhesive interactions with epithelial and endothelial CXADR. {ECO:0000269|PubMed:12869515, ECO:0000269|PubMed:15800062, ECO:0000269|PubMed:18948633, ECO:0000269|PubMed:19064666}.; . TISSUE SPECIFICITY: Expression is restricted to the hematopoietic tissues with the exception of liver. Expressed in fetal liver, spleen and thymus. Preferentially expressed by mature leukocytes (at protein level). {ECO:0000269|PubMed:12869515, ECO:0000269|PubMed:18948633, ECO:0000269|PubMed:19064666}.; . . 0.03348 0.11960 0.597144447 82.7435716 . . JARID2 0.999862193011047 0.000137806988251665 7.00959973201415e-13 jumonji and AT-rich interaction domain containing 2 FUNCTION: Regulator of histone methyltransferase complexes that plays an essential role in embryonic development, including heart and liver development, neural tube fusion process and hematopoiesis. Acts by modulating histone methyltransferase activity and promoting the recruitment of histone methyltransferase complexes to their target genes. Binds DNA and mediates the recruitment of the PRC2 complex to target genes in embryonic stem cells. Does not have histone demethylase activity but regulates activity of various histone methyltransferase complexes. In embryonic stem cells, it associates with the PRC2 complex and inhibits trimethylation of 'Lys-27' of histone H3 (H3K27me3) by the PRC2 complex, thereby playing a key role in differentiation of embryonic stem cells and normal development. In cardiac cells, it is required to repress expression of cyclin-D1 (CCND1) by activating methylation of 'Lys-9' of histone H3 (H3K9me) by the GLP1/EHMT1 and G9a/EHMT2 histone methyltransferases. Also acts as a transcriptional repressor of ANF via its interaction with GATA4 and NKX2-5. Participates in the negative regulation of cell proliferation signaling. {ECO:0000269|PubMed:20075857}.; . TISSUE SPECIFICITY: During embryogenesis, predominantly expressed in neurons and particularly in dorsal root ganglion cells.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;cerebellum peduncles;testis;trigeminal ganglion;cingulate cortex;cerebellum; 0.98339 0.18221 -1.741783094 2.418023119 264.05908 3.48721 JARID2-AS1 . . . JARID2 antisense RNA 1 . . . . . . . . . . . JAZF1 0.958302381623798 0.0415989251347452 9.86932414572269e-05 JAZF zinc finger 1 FUNCTION: Acts as a transcriptional corepressor of orphan nuclear receptor NR2C2 (PubMed:15302918). Inhibits expression of the gluconeogenesis enzyme PCK2 through inhibition of NR2C2 activity (By similarity). Also involved in transcriptional activation of NAMPT by promoting expression of PPARA and PPARD (By similarity). Plays a role in lipid metabolism by suppressing lipogenesis, increasing lipolysis and decreasing lipid accumulation in adipose tissue (By similarity). Plays a role in glucose homeostasis by improving glucose metabolism and insulin sensitivity (By similarity). {ECO:0000250|UniProtKB:Q80ZQ5, ECO:0000269|PubMed:15302918}.; . TISSUE SPECIFICITY: Highest expression in testis with moderate levels in colon, placenta, prostate and ovary and low levels in brain, spleen, liver and small intestine. {ECO:0000269|PubMed:15302918}.; ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;liver;spleen;mammary gland;aorta; testis - interstitial;testis;ciliary ganglion;atrioventricular node; 0.48995 0.10650 -0.229483771 36.86010852 7.70049 0.28399 JAZF1-AS1 . . . JAZF1 antisense RNA 1 . . . . . . . . . . . JBS . . . Jacobsen syndrome . . . . . . . . . . . JCHAIN . . . joining chain of multimeric IgA and IgM FUNCTION: Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces larger polymers. It also help to bind these immunoglobulins to secretory component. {ECO:0000250|UniProtKB:P01592}.; . . . . 0.06322 0.10505 -0.119252484 44.53880632 . . JDP2 0.856106109996034 0.141600764446697 0.00229312555726932 Jun dimerization protein 2 FUNCTION: Component of the AP-1 transcription factor that represses transactivation mediated by the Jun family of proteins. Involved in a variety of transcriptional responses associated with AP-1 such as UV-induced apoptosis, cell differentiation, tumorigenesis and antitumogeneris. Can also function as a repressor by recruiting histone deacetylase 3/HDAC3 to the promoter region of JUN. May control transcription via direct regulation of the modification of histones and the assembly of chromatin. {ECO:0000269|PubMed:12707301, ECO:0000269|PubMed:12903123, ECO:0000269|PubMed:16026868, ECO:0000269|PubMed:16518400}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;alveolus;kidney;mammary gland;stomach;aorta; . 0.10344 0.13249 -0.05129383 49.75819769 59.14386 1.55937 JHDM1D-AS1 . . . JHDM1D antisense RNA 1 (head to head) . . . . . . . . . . . JKAMP 0.0598976863876527 0.923247495611088 0.0168548180012587 JNK1/MAPK8-associated membrane protein FUNCTION: May be a regulator of the duration of MAPK8 activity in response to various stress stimuli. Facilitates degradation of misfolded endoplasmic reticulum (ER) luminal proteins through the recruitment of components of the proteasome and endoplasmic reticulum-associated degradation (ERAD) system (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;amniotic fluid;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;blood;lens;bile duct;pancreas;pia mater;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis; 0.06981 0.08772 -0.205617011 38.57631517 9.59423 0.35305 JKAMPP1 . . . JNK1/MAPK8-associated membrane protein pseudogene 1 . . . . . . . . . . . JMJD1C 0.999999999962643 3.73572110707239e-11 1.72817536618924e-27 jumonji domain containing 1C FUNCTION: Probable histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May be involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;urinary;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;liver;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;larynx;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;placenta;hippocampus;head and neck;kidney;stomach; pons;whole blood; 0.78890 0.11870 -0.553188106 19.81009672 5413.0011 15.16807 JMJD1C-AS1 . . . JMJD1C antisense RNA 1 . . . . . . . . . . . JMJD4 1.86970802268343e-07 0.246401246193047 0.753598566836151 jumonji domain containing 4 . . . . . 0.13494 . 0.040529541 57.15380986 1171.12584 6.50446 JMJD6 0.821640917971612 0.178184764354179 0.000174317674209254 jumonji domain containing 6 FUNCTION: Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Acts as a regulator of RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), thereby playing a role in histone code. However, histone arginine demethylation may not constitute the primary activity in vivo. Has no histone lysine demethylase activity. Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation: required for angiogenic sprouting by regulating the pre-mRNA splicing activity of U2AF2/U2AF65. Seems to be necessary for the regulation of macrophage cytokine responses. {ECO:0000269|PubMed:17947579, ECO:0000269|PubMed:19574390, ECO:0000269|PubMed:20684070, ECO:0000269|PubMed:21060799}.; . TISSUE SPECIFICITY: Highly expressed in the heart, skeletal muscle and kidney. Expressed at moderate or low level in brain, placenta, lung, liver, pancreas, spleen, thymus, prostate, testis and ovary. Up-regulated in many patients with chronic pancreatitis. Expressed in nursing thymic epithelial cells. {ECO:0000269|PubMed:15072554, ECO:0000269|PubMed:15622002, ECO:0000269|PubMed:9628581}.; ovary;salivary gland;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;thyroid;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;urinary;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;fetal brain;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.23316 0.19171 -0.582225231 18.44184949 21.04678 0.71295 JMJD7 0.23431095695057 0.758410910631949 0.00727813241748117 jumonji domain containing 7 . . . . . . 0.10269 0.554869705 81.59943383 341.7008 3.92051 JMJD7-PLA2G4B 9.15662350167561e-25 0.000441734513603934 0.999558265486396 JMJD7-PLA2G4B readthrough FUNCTION: Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position with a preference for arachidonoyl phospholipids. Has a much weaker activity than PLA2G4A. Isoform 3 has calcium-dependent activity against palmitoyl-arachidonyl-phosphatidylethanolamine and low level lysophospholipase activity but no activity against phosphatidylcholine. Isoform 5 does have activity against phosphatidylcholine. {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:16617059}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in brain, heart, liver, cerebellum and pancreas. Isoform 3 is widely expressed. {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:16617059}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;larynx;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;hypothalamus;muscle;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;cervix;spleen;head and neck;kidney;stomach;cerebellum; . 0.17884 . 0.48857149 79.4821892 . . JMJD8 3.79963968099618e-10 0.0137290986031446 0.986270901016892 jumonji domain containing 8 . . . myocardium;medulla oblongata;ovary;salivary gland;colon;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;synovium;larynx;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . . . 0.883760026 89.07171503 269.4043 3.52105 JMY 0.999722637107555 0.000277362873405938 1.90387288083709e-11 junction mediating and regulatory protein, p53 cofactor FUNCTION: Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic regulator of actin dynamics depending on conditions. In nucleus, acts as a cofactor that increases p53/TP53 response via its interaction with p300/EP300. Increases p53/TP53-dependent transcription and apoptosis, suggesting an important role in p53/TP53 stress response such as DNA damage. In cytoplasm, acts as a nucleation-promoting factor for both branched and unbranched actin filaments. Activates the Arp2/3 complex to induce branched actin filament networks. Also catalyzes actin polymerization in the absence of Arp2/3, creating unbranched filaments. Contributes to cell motility by controlling actin dynamics. May promote the rapid formation of a branched actin network by first nucleating new mother filaments and then activating Arp2/3 to branch off these filaments. The p53/TP53-cofactor and actin activator activities are regulated via its subcellular location (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;skeletal muscle;skin;retina;uterus;pancreas;lung;cochlea;placenta;hypopharynx;head and neck;germinal center; . . . 0.88921411 89.24274593 2992.00625 10.37986 JOSD1 0.319904564982739 0.663487646571258 0.0166077884460023 Josephin domain containing 1 FUNCTION: Deubiquitinates monoubiquitinated probes (in vitro). When ubiquitinated, cleaves 'Lys-63'-linked and 'Lys-48'-linked poly-ubiquitin chains (in vitro), hence may act as a deubiquitinating enzyme. May increase macropinocytosis and suppress clathrin- and caveolae-mediated endocytosis. May enhance membrane dynamics and cell motility independently of its catalytic activity. {ECO:0000269|PubMed:21118805, ECO:0000269|PubMed:23625928}.; . . ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;blood;skeletal muscle;breast;epididymis;trabecular meshwork;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;choroid;uterus;whole body;larynx;synovium;bone;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta;cerebellum; whole brain;fetal brain;prefrontal cortex;white blood cells; 0.54711 0.11809 -0.007201372 53.19061099 164.67004 2.80304 JOSD2 0.428022033640029 0.539353686842157 0.0326242795178143 Josephin domain containing 2 FUNCTION: Cleaves 'Lys-63'-linked poly-ubiquitin chains, and with lesser efficiency 'Lys-48'-linked poly-ubiquitin chains (in vitro). May act as a deubiquitinating enzyme. {ECO:0000269|PubMed:17696782, ECO:0000269|PubMed:21118805, ECO:0000269|PubMed:23625928}.; . . unclassifiable (Anatomical System);lymphoreticular;smooth muscle;islets of Langerhans;colon;parathyroid;choroid;skin;prostate;whole body;lung;bone;visual apparatus;liver;testis;kidney;brain;stomach; atrioventricular node;trigeminal ganglion; 0.15287 0.10732 . . 19.35766 0.66558 JPD . . . juvenile periodontitis . . . . . . . . . . . JPH1 0.706129632533951 0.293141817550106 0.000728549915943467 junctophilin 1 FUNCTION: Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH1 contributes to the construction of the skeletal muscle triad by linking the t-tubule (transverse-tubule) and SR (sarcoplasmic reticulum) membranes.; . TISSUE SPECIFICITY: Abundantly expressed in skeletal muscle. Very low levels in heart. {ECO:0000269|PubMed:10891348}.; unclassifiable (Anatomical System);heart;ovary;tongue;colon;parathyroid;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;prostate;optic nerve;lung;endometrium;bone;placenta;macula lutea;hippocampus;alveolus;testis;head and neck;cervix; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.62199 0.14032 0.090079492 60.64519934 307.58841 3.73294 JPH2 0.0145044420330593 0.956977846186801 0.0285177117801397 junctophilin 2 FUNCTION: Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH2 is necessary for proper intracellular Ca(2+) signaling in cardiac myocytes via its involvement in ryanodine receptor-mediated calcium ion release. Contributes to the construction of skeletal muscle triad junctions. {ECO:0000269|PubMed:20095964}.; DISEASE: Cardiomyopathy, familial hypertrophic 17 (CMH17) [MIM:613873]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:17509612}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Specifically expressed in skeletal muscle and heart. {ECO:0000269|PubMed:10891348}.; unclassifiable (Anatomical System);lung;testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.16388 0.14439 . . 3095.06571 10.57821 JPH3 0.986177997424036 0.0138155409546863 6.46162127731343e-06 junctophilin 3 FUNCTION: Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH3 is brain- specific and appears to have an active role in certain neurons involved in motor coordination and memory.; DISEASE: Huntington disease-like 2 (HDL2) [MIM:606438]: Huntington disease (HD) is a neurodegenerative disorder resulting primarily from the loss of medium spiny projection neurons in the striatum, especially in the caudate nucleus, and, to a lesser extent, atrophy of mesencephalic and cortical structures. The typical clinical picture of HD combines familial adult onset chorea and subcortical dementia that usually begin during the fourth decade of life. {ECO:0000269|PubMed:11914418, ECO:0000269|PubMed:14557581}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Specifically expressed in brain. {ECO:0000269|PubMed:10891348}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;lens;lung;placenta;macula lutea;hippocampus;visual apparatus;liver;spleen;kidney;mammary gland;stomach; amygdala; 0.13441 0.26404 -1.230963997 5.543760321 231.25612 3.28718 JPH4 0.987347572961713 0.0126472254828291 5.20155545836355e-06 junctophilin 4 FUNCTION: Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH4 is brain- specific and appears to have an active role in certain neurons involved in motor coordination and memory (By similarity). {ECO:0000250}.; . . ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney; subthalamic nucleus;cerebellum peduncles;pons;parietal lobe;cingulate cortex;cerebellum; 0.45841 . . . 70.97202 1.75481 JPX . . . JPX transcript, XIST activator (non-protein coding) . . . . . . . . . . . JRK . . . Jrk helix-turn-helix protein FUNCTION: May bind DNA. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed ubiquitously. {ECO:0000269|PubMed:9675132}.; . . . . . . . . JRKL 0.000583510618527107 0.898451903278732 0.100964586102741 JRK-like . . TISSUE SPECIFICITY: Abundantly expressed in the majority of tissues examined, including brain and skeletal muscle.; unclassifiable (Anatomical System);lung;cartilage;islets of Langerhans;bone;colon;kidney;mammary gland;bladder;skeletal muscle; ciliary ganglion; 0.20502 0.10447 -0.560178693 19.30879925 33.58807 1.03691 JRKL-AS1 . . . JRKL antisense RNA 1 . . . . . . . . . . . JSRP1 8.90273527204223e-10 0.0225945675621656 0.977405431547561 junctional sarcoplasmic reticulum protein 1 FUNCTION: Involved in skeletal muscle excitation/contraction coupling (EC), probably acting as a regulator of the voltage- sensitive calcium channel CACNA1S. EC is a physiological process whereby an electrical signal (depolarization of the plasma membrane) is converted into a chemical signal, a calcium gradient, by the opening of ryanodine receptor calcium release channels. May regulate CACNA1S membrane targeting and activity. {ECO:0000269|PubMed:22927026}.; . . unclassifiable (Anatomical System);uterus;whole body;muscle;colon;skeletal muscle; . 0.07887 0.07487 0.639420866 83.8995046 3088.21168 10.56049 JTB 0.645223905316483 0.348528769284235 0.00624732539928127 jumping translocation breakpoint FUNCTION: Required for normal cytokinesis during mitosis. Plays a role in the regulation of cell proliferation. May be a component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Increases AURKB activity. Inhibits apoptosis induced by TGFB1 (By similarity). Overexpression induces swelling of mitochondria and reduces mitochondrial membrane potential (By similarity). {ECO:0000250, ECO:0000269|PubMed:21225229}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in all normal human tissues studied but overexpressed or underexpressed in many of their malignant counterparts. {ECO:0000269|PubMed:10321732, ECO:0000269|PubMed:10762645, ECO:0000269|PubMed:17369841, ECO:0000269|PubMed:21225229}.; smooth muscle;ovary;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;epidermis;islets of Langerhans;urinary;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum;thymus; amygdala;whole brain;prostate;trachea;adrenal gland;thyroid;liver;kidney;cerebellum; 0.13614 0.09989 0.347360312 73.97381458 191.44507 3.00054 JTBP1 . . . jumping translocation breakpoint pseudogene 1 . . . . . . . . . . . JUN 0.46085190120742 0.51315901881126 0.0259890799813205 jun proto-oncogene FUNCTION: Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3'. Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. {ECO:0000269|PubMed:10995748, ECO:0000269|PubMed:17210646}.; . . . . 0.99951 0.13257 -0.185391282 39.67916962 15.62493 0.55720 JUNB 0.585014693290371 0.373047378140309 0.04193792856932 jun B proto-oncogene FUNCTION: Transcription factor involved in regulating gene activity following the primary growth factor response. Binds to the DNA sequence 5'-TGA[CG]TCA-3'.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;cerebral cortex;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;adrenal cortex;blood;lens;pancreas;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; ciliary ganglion; 0.96190 0.12736 . . 21.42094 0.72238 JUND 0.560887373754993 0.389592916266824 0.0495197099781822 jun D proto-oncogene FUNCTION: Transcription factor binding AP-1 sites. {ECO:0000269|PubMed:9989505}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;lung;placenta;macula lutea;visual apparatus;kidney;stomach;aorta;thymus; prefrontal cortex;adrenal cortex;cingulate cortex; 0.52380 . . . 36.56701 1.09595 JUP 0.0375345368925628 0.960977059421756 0.00148840368568153 junction plakoglobin FUNCTION: Common junctional plaque protein. The membrane- associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE- cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton (By similarity). {ECO:0000250}.; DISEASE: Naxos disease (NXD) [MIM:601214]: An autosomal recessive disorder characterized by the association of diffuse non- epidermolytic palmoplantar keratoderma with woolly hair and cardiac abnormalities such as dilated cardiomyopathy and arrhythmogenic right ventricular dysplasia. {ECO:0000269|PubMed:10902626}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 12 (ARVD12) [MIM:611528]: A congenital heart disease characterized by infiltration of adipose and fibrous tissue into the right ventricle and loss of myocardial cells, resulting in ventricular and supraventricular arrhythmias. {ECO:0000269|PubMed:17924338, ECO:0000269|PubMed:20031617}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;endometrium;oesophagus;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;amnion;hypopharynx;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; lung;heart;tongue;thyroid;placenta;liver;kidney;skin; 0.98957 0.33762 -1.657176494 2.736494456 400.41504 4.19810 KAAG1 0.0191912389509573 0.502144576795006 0.478664184254037 kidney associated antigen 1 . . TISSUE SPECIFICITY: Expressed in testis and kidney, and, at lower levels, in urinary bladder and liver. Expressed by a high proportion of tumors of various histologic origin, including melanomas, sarcomas and colorectal carcinomas. {ECO:0000269|PubMed:10601354}.; unclassifiable (Anatomical System);bile duct;lung;frontal lobe;visual apparatus;pituitary gland;liver;kidney; . 0.03783 0.06677 -0.053113545 49.38664779 5.84948 0.22022 KALRN 0.999996915329978 3.08467002159339e-06 5.55409347529539e-19 kalirin, RhoGEF kinase FUNCTION: Promotes the exchange of GDP by GTP. Activates specific Rho GTPase family members, thereby inducing various signaling mechanisms that regulate neuronal shape, growth, and plasticity, through their effects on the actin cytoskeleton. Induces lamellipodia independent of its GEF activity. {ECO:0000269|PubMed:10023074}.; DISEASE: Coronary heart disease 5 (CHDS5) [MIM:608901]: A multifactorial disease characterized by an imbalance between myocardial functional requirements and the capacity of the coronary vessels to supply sufficient blood flow. Decreased capacity of the coronary vessels is often associated with thickening and loss of elasticity of the coronary arteries. {ECO:0000269|PubMed:17357071}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 2 is brain specific. Highly expressed in cerebral cortex, putamen, amygdala, hippocampus and caudate nucleus. Weakly expressed in brain stem and cerebellum. Isoform 4 is expressed in skeletal muscle. {ECO:0000269|PubMed:10023074}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;cochlea;oesophagus;endometrium;thyroid;pituitary gland;iris;testis;ciliary body;brain;amygdala;unclassifiable (Anatomical System);heart;tongue;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;stomach; whole brain;amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;atrioventricular node;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.66718 . -3.651326374 0.271290399 881.44733 5.78506 KANK1 . . . KN motif and ankyrin repeat domains 1 FUNCTION: Involved in the control of cytoskeleton formation by regulating actin polymerization. Inhibits actin fiber formation and cell migration. Inhibits RhoA activity; the function involves phosphorylation through PI3K/Akt signaling and may depend on the competetive interaction with 14-3-3 adapter proteins to sequester them from active complexes. Inhibits the formation of lamellipodia but not of filopodia; the function may depend on the competetive interaction with BAIAP2 to block its association with activated RAC1. Inhibits fibronectin-mediated cell spreading; the function is partially mediated by BAIAP2. Inhibits neurite outgrowth. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. In the nucleus, is involved in beta-catenin-dependent activation of transcription. Potential tumor suppressor for renal cell carcinoma. {ECO:0000269|PubMed:16968744, ECO:0000269|PubMed:18458160, ECO:0000269|PubMed:19171758, ECO:0000269|PubMed:22084092}.; . TISSUE SPECIFICITY: Widely expressed. Isoform 1 is predominantly expressed in heart and kidney. Isoform 2 probably is widely expressed at basic levels. {ECO:0000269|PubMed:15823577}.; unclassifiable (Anatomical System);prostate;lung;thyroid;placenta;iris;testis;colon;spinal ganglion;skin;skeletal muscle;stomach;tonsil; . 0.51687 0.09889 -0.92088781 9.784147205 5958.40742 16.02905 KANK2 0.981511998562845 0.0184878918517659 1.0958538867554e-07 KN motif and ankyrin repeat domains 2 FUNCTION: Involved in transcription regulation by sequestering nuclear receptor coactivators, such as NCOA1, NCOA2 and NCOA3, in the cytoplasm; the function is deregulated by phosphorylation. Involved in the negative control of vitamin D receptor signaling pathway (PubMed:24671081). May be involved in the control of cytoskeleton formation by regulating actin polymerization. Involved in regulation of caspase-independent apoptosis; proposed to sequester AIFM1 in mitochondria and apoptotic stimuli lead to its proteasomal degradation allowing the release of AIFM1 to the nucleus (PubMed:22371500). May be involved in promotion of cell proliferation (By similarity). {ECO:0000250|UniProtKB:Q8BX02, ECO:0000269|PubMed:17476305, ECO:0000269|PubMed:22371500, ECO:0000269|PubMed:24671081}.; DISEASE: Palmoplantar keratoderma and woolly hair (PPKWH) [MIM:616099]: A disorder characterized by abnormal thickening of the skin on the palms and soles, in association with woolly scalp hair. Affected individuals manifest a variable degree of striate palmoplantar keratoderma, generally more severe on the soles. Leukonychia is more pronounced on the fingernails than toenails. Scalp hair, body hair, eyebrows, and eyelashes are sparse. The fifth toes show variable degrees of pseudoainhum, ranging from external rotation to a deep sulcus at the digitoplantar fold, accompanied by a bulbous appearance of the distal toe. {ECO:0000269|PubMed:24671081}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Strongly expressed in cervix, colon, heart, kidney and lung. Expressed in kidney glomerular podocytes and mesangial cells (at protein level). {ECO:0000269|PubMed:17996375, ECO:0000269|PubMed:20720434}.; myocardium;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;thyroid;bone;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;duodenum;cervix;stomach;peripheral nerve; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.33057 0.10549 0.591498354 82.37791932 392.42528 4.16843 KANK3 8.53381795135144e-06 0.760056754946035 0.239934711236013 KN motif and ankyrin repeat domains 3 FUNCTION: May be involved in the control of cytoskeleton formation by regulating actin polymerization.; . TISSUE SPECIFICITY: Strongly expressed in breast, liver, lung, skeletal muscle and kidney. {ECO:0000269|PubMed:17996375}.; unclassifiable (Anatomical System);myocardium;heart;colon;blood;choroid;lens;skin;uterus;prostate;optic nerve;whole body;lung;frontal lobe;bone;placenta;testis;kidney;brain;mammary gland;stomach; superior cervical ganglion;ciliary ganglion; 0.24503 0.09571 . . 13103.53163 24.58816 KANK4 5.3984986278488e-08 0.847577901345123 0.152422044669891 KN motif and ankyrin repeat domains 4 FUNCTION: May be involved in the control of cytoskeleton formation by regulating actin polymerization.; . TISSUE SPECIFICITY: Strongly expressed in colon, liver, lung, skeletal muscle and kidney. {ECO:0000269|PubMed:17996375}.; unclassifiable (Anatomical System);heart;ovary;tongue;muscle;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;cochlea;cerebral cortex;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;brain; dorsal root ganglion; 0.19021 0.09379 0.946083628 89.89738146 2487.39417 9.30920 KANSL1 0.999733505943003 0.000266494053502093 3.49489819993616e-12 KAT8 regulatory NSL complex subunit 1 FUNCTION: As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. {ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:22547026}.; . TISSUE SPECIFICITY: Expressed in the brain. {ECO:0000269|PubMed:11641718}.; . . 0.60193 0.13678 -0.321528174 30.95069592 5743.08683 15.71165 KANSL1-AS1 . . . KANSL1 antisense RNA 1 . . . . . . . . . . . KANSL1L 0.476930027111924 0.523069612905405 3.59982670624438e-07 KAT8 regulatory NSL complex subunit 1 like . . . . . 0.18367 . 0.246221394 69.56829441 348.30942 3.95515 KANSL2 0.404028496542896 0.595597632149893 0.000373871307210312 KAT8 regulatory NSL complex subunit 2 FUNCTION: As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. {ECO:0000269|PubMed:20018852}.; . . unclassifiable (Anatomical System);lymphoreticular;lymph node;heart;ovary;tongue;muscle;colon;larynx;bone;testis;head and neck;brain;stomach; . 0.36528 0.10953 0.150760231 64.51403633 280.01131 3.58546 KANSL3 0.994530636900608 0.00546933574631329 2.73530783367419e-08 KAT8 regulatory NSL complex subunit 3 FUNCTION: As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. {ECO:0000269|PubMed:20018852}.; . . lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;nervous;urinary;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;oesophagus;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.14496 0.10426 0.266447942 70.5826846 392.06112 4.16669 KANTR . . . KDM5C adjacent non-coding transcript . . . . . . . . . . . KARS 0.0859078130308862 0.913691304773705 0.000400882195408814 lysyl-tRNA synthetase FUNCTION: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of diadenosine oligophosphate (Ap4A), a signaling molecule involved in the activation of MITF transcriptional activity. Interacts with HIV-1 virus GAG protein, facilitating the selective packaging of tRNA(3)(Lys), the primer for reverse transcription initiation. {ECO:0000269|PubMed:15851690, ECO:0000269|PubMed:5338216}.; DISEASE: Charcot-Marie-Tooth disease, recessive, intermediate type, B (CMTRIB) [MIM:613641]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Recessive intermediate forms of Charcot-Marie-Tooth disease are characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. {ECO:0000269|PubMed:20920668}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal recessive, 89 (DFNB89) [MIM:613916]: A form of non-syndromic deafness characterized by bilateral, prelingual, moderate to severe hearing loss affecting all frequencies. {ECO:0000269|PubMed:23768514}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;gum;germinal center;brain;heart;cartilage;tongue;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;tumor;testis;white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.38207 0.35052 -0.929520514 9.683887709 1160.04303 6.48366 KARSP1 . . . lysyl-tRNA synthetase pseudogene 1 . . . . . . . . . . . KARSP2 . . . lysyl-tRNA synthetase pseudogene 2 . . . . . . . . . . . KARSP3 . . . lysyl-tRNA synthetase pseudogene 3 . . . . . . . . . . . KAT2A 0.40833206009159 0.59166493811404 3.00179436991838e-06 lysine acetyltransferase 2A FUNCTION: Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles. Also acetylates non- histone proteins, such as CEBPB (PubMed:17301242). Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. {ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:19103755}.; . TISSUE SPECIFICITY: Expressed in all tissues tested, with most abundant expression in ovary.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;spinal cord;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;amygdala;superior cervical ganglion;prefrontal cortex;globus pallidus;atrioventricular node;caudate nucleus;cingulate cortex;skeletal muscle;cerebellum; 0.97504 0.18545 -1.155457828 6.168907761 39.12932 1.16016 KAT2B 0.998926901286195 0.00107309869273854 2.10663383541072e-11 lysine acetyltransferase 2B FUNCTION: Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers. {ECO:0000269|PubMed:10675335, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:23932781, ECO:0000269|PubMed:8684459, ECO:0000269|PubMed:9707565}.; . TISSUE SPECIFICITY: Ubiquitously expressed but most abundant in heart and skeletal muscle. {ECO:0000269|PubMed:8684459}.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;peripheral nerve;parathyroid;choroid;fovea centralis;uterus;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;hippocampus;kidney;aorta;stomach;thymus; ciliary ganglion; 0.99728 0.62864 -0.334253673 30.70299599 106.89487 2.24328 KAT5 0.471177718664719 0.528776881492693 4.53998425885086e-05 lysine acetyltransferase 5 FUNCTION: Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. In case of HIV-1 infection, interaction with the viral Tat protein leads to KAT5 polyubiquitination and targets it to degradation. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2. Promotes FOXP3 acetylation and positively regulates its transcriptional repressor activity (PubMed:17360565). {ECO:0000269|PubMed:12776177, ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:15042092, ECO:0000269|PubMed:15121871, ECO:0000269|PubMed:15310756, ECO:0000269|PubMed:16141325, ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:17360565, ECO:0000269|PubMed:17996965, ECO:0000269|PubMed:19909775, ECO:0000269|PubMed:24463511}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;synovium;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum;thymus; superior cervical ganglion;testis;cerebellum; 0.97123 0.63540 -0.780646273 12.77423921 8.28063 0.30371 KAT6A 0.999999984631619 1.53683811507165e-08 1.65061216581298e-22 lysine acetyltransferase 6A FUNCTION: Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML. {ECO:0000269|PubMed:11742995, ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:12771199, ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:17925393, ECO:0000269|PubMed:23431171}.; DISEASE: Note=Chromosomal aberrations involving KAT6A may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with CREBBP (PubMed:8782817). Translocation t(8;22)(p11;q13) with EP300 (PubMed:10824998). KAT6A-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription (PubMed:11742995). Inversion inv(8)(p11;q13) generates the KAT6A-NCOA2 oncogene, which consists of the N-terminal part of KAT6A and the C-terminal part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and disrupts its function in transcription activation (PubMed:12676584). {ECO:0000269|PubMed:10824998, ECO:0000269|PubMed:11742995, ECO:0000269|PubMed:12676584, ECO:0000269|PubMed:8782817}.; DISEASE: Note=A chromosomal aberration involving KAT6A is a cause of therapy-related myelodysplastic syndrome. Translocation t(2;8)(p23;p11.2) with ASXL2 generates a KAT6A-ASXL2 fusion protein. {ECO:0000269|Ref.3}.; DISEASE: Mental retardation, autosomal dominant 32 (MRD32) [MIM:616268]: A form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD32 patients manifest intellectual disability, dysmorphic facial features, delayed psychomotor development, and lack of speech. {ECO:0000269|PubMed:25728775, ECO:0000269|PubMed:25728777}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;endometrium;bone;thyroid;iris;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;blood;breast;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;hypopharynx;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;trigeminal ganglion;skeletal muscle;parietal lobe;cerebellum; 0.91841 0.13598 -3.089379839 0.477707006 1366.73644 6.93520 KAT6B 0.999999922573337 7.74266627180357e-08 4.18933262864851e-20 lysine acetyltransferase 6B FUNCTION: Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. May be involved in cerebral cortex development. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. {ECO:0000269|PubMed:10497217, ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:16387653}.; DISEASE: Note=A chromosomal aberration involving KAT6B may be a cause acute myeloid leukemias. Translocation t(10;16)(q22;p13) with CREBBP. {ECO:0000269|PubMed:11157802}.; DISEASE: Ohdo syndrome, SBBYS variant (SBBYSS) [MIM:603736]: A syndrome characterized by distinctive facial appearance with severe blepharophimosis, an immobile mask-like face, a bulbous nasal tip, and a small mouth with a thin upper lip. The condition presents in infancy with severe hypotonia and feeding problems. Associated skeletal problems include joint laxity, abnormally long thumbs and great toes, and dislocated or hypoplastic patellae. Structural cardiac defects are present in around 50% of cases, and dental anomalies, including small and pointed teeth, are common. Optic atrophy and conductive or sensorineural deafness are repeatedly reported. Many affected individuals have abnormalities of thyroid structure or function. SBBYSS is usually associated with severe mental retardation, delayed motor milestones, and significantly impaired speech. {ECO:0000269|PubMed:22077973}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Genitopatellar syndrome (GTPTS) [MIM:606170]: A rare disorder consisting of microcephaly, severe psychomotor retardation, and characteristic coarse facial features, including broad nose and small or retracted chin, associated with congenital flexion contractures of the lower extremities, abnormal or missing patellae, and urogenital anomalies. {ECO:0000269|PubMed:22265014}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed, with high levels in heart, pancreas, testis and ovary. {ECO:0000269|PubMed:10497217}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;hypopharynx;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.81242 0.19371 -2.383253371 1.108752064 363.59118 4.03707 KAT7 0.999956770504954 4.32294900232431e-05 5.02275586765635e-12 lysine acetyltransferase 7 FUNCTION: Component of the HBO1 complex which has a histone H4- specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Through chromatin acetylation it may regulate DNA replication and act as a coactivator of TP53-dependent transcription. Specifically represses AR-mediated transcription. {ECO:0000269|PubMed:10438470, ECO:0000269|PubMed:10930412, ECO:0000269|PubMed:11278932, ECO:0000269|PubMed:16387653}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in testis. {ECO:0000269|PubMed:10438470, ECO:0000269|PubMed:10930412}.; myocardium;lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;germinal center;brain;heart;spinal cord;pharynx;blood;cerebrum;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;thymus;cerebellum; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.95423 . -0.049474214 50.01179523 29.2063 0.93328 KAT8 0.912576387976251 0.0873971693190813 2.64427046680062e-05 lysine acetyltransferase 8 FUNCTION: Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex. Can also acetylate TP53/p53 at 'Lys-120'. {ECO:0000269|PubMed:12397079, ECO:0000269|PubMed:15923642, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:22547026}.; . . ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;muscle;blood;skeletal muscle;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;testis;atrioventricular node;pons; 0.30126 0.11176 -0.251530012 35.42108988 162.71582 2.78529 KATNA1 0.00192587515145671 0.997114762909884 0.000959361938659046 katanin p60 (ATPase containing) subunit A 1 FUNCTION: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:10751153, ECO:0000269|PubMed:11870226, ECO:0000269|PubMed:19287380}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;bone;thyroid;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.25068 0.12099 -0.069700724 48.54328851 72.48477 1.77381 KATNAL1 0.946326582546448 0.0536657658649823 7.65158857001017e-06 katanin p60 subunit A like 1 FUNCTION: Regulates microtubule dynamics in Sertoli cells, a process that is essential for spermiogenesis and male fertility. Severs microtubules in an ATP-dependent manner, promoting rapid reorganization of cellular microtubule arrays (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis, restricted to Sertoli cells (at protein level). {ECO:0000269|PubMed:22654668}.; . . 0.33248 0.11564 -0.159704656 41.90846898 44.50855 1.27597 KATNAL2 0.000125861969085373 0.990282882886411 0.00959125514450365 katanin p60 subunit A like 2 FUNCTION: Severs microtubules in vitro in an ATP-dependent manner. This activity may promote rapid reorganization of cellular microtubule arrays. {ECO:0000255|HAMAP-Rule:MF_03025}.; . . unclassifiable (Anatomical System);lung;frontal lobe;thyroid;liver;testis;spleen;kidney;germinal center;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.16952 0.10613 -1.087493118 7.106628922 135.90402 2.53420 KATNB1 0.496734037043629 0.503258414052759 7.54890361204615e-06 katanin p80 (WD repeat containing) subunit B 1 FUNCTION: Participates in a complex which severs microtubules in an ATP-dependent manner. May act to target the enzymatic subunit of this complex to sites of action such as the centrosome. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:10751153}.; DISEASE: Lissencephaly 6, with microcephaly (LIS6) [MIM:616212]: A form of lissencephaly, a disorder of cortical development characterized by agyria or pachygyria and disorganization of the clear neuronal lamination of normal six-layered cortex. LIS6 features include hypoplasia of the corpus callosum, severe microcephaly and developmental delay. {ECO:0000269|PubMed:25521378, ECO:0000269|PubMed:25521379}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.31434 0.11315 -0.505170032 21.79759377 608.48655 4.98793 KATNBL1 0.0141547394809675 0.956357154142262 0.0294881063767707 katanin p80 subunit B-like 1 . . . . . 0.21983 0.10146 0.125076652 62.7388535 127.0851 2.45845 KATNBL1P1 . . . katanin p80 subunit B-like 1 pseudogene 1 . . . . . . . . . . . KATNBL1P2 . . . katanin p80 subunit B-like 1 pseudogene 2 . . . . . . . . . . . KATNBL1P3 . . . katanin p80 subunit B-like 1 pseudogene 3 . . . . . . . . . . . KATNBL1P4 . . . katanin p80 subunit B-like 1 pseudogene 4 . . . . . . . . . . . KATNBL1P5 . . . katanin p80 subunit B-like 1 pseudogene 5 . . . . . . . . . . . KATNBL1P6 . . . katanin p80 subunit B-like 1 pseudogene 6 . . . . . . . . . . . KAZALD1 0.000335811357601351 0.595155895163995 0.404508293478404 Kazal type serine peptidase inhibitor domain 1 FUNCTION: Involved in the proliferation of osteoblasts during bone formation and bone regeneration. Promotes matrix assembly (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);prostate;pancreas;optic nerve;lung;whole body;cartilage;oesophagus;bone;spleen;kidney;stomach;retina; prostate;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.11925 . 0.903992902 89.39018636 387.7143 4.14703 KAZN 0.144589791042949 0.855248608306057 0.000161600650994132 kazrin, periplakin interacting protein FUNCTION: Component of the cornified envelope of keratinocytes. May be involved in the interplay between adherens junctions and desmosomes. The function in the nucleus is not known. {ECO:0000269|PubMed:15337775}.; . TISSUE SPECIFICITY: Isoform 2, isoform 3 and isoform 4 are expressed in several cell lines including keratinocytes and bladder and epidermoid carcinoma (at protein level). Isoform 2, isoform 3 and isoform 4 are expressed in hair follicle and interfollicular epidermis (at protein level). {ECO:0000269|PubMed:15337775}.; unclassifiable (Anatomical System);cartilage;ovary;parathyroid;blood;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;lung;oesophagus;bone;placenta;macula lutea;testis;brain;aorta;stomach; whole brain;dorsal root ganglion;amygdala;occipital lobe;superior cervical ganglion;cerebellum peduncles;atrioventricular node;skeletal muscle;subthalamic nucleus;uterus corpus;placenta;prefrontal cortex;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; . . -0.506987379 21.76810569 4119.16946 12.74291 KBTBD2 0.991275949151835 0.00872362734784518 4.23500319974916e-07 kelch repeat and BTB domain containing 2 . . . ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;medulla oblongata;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle;cerebellum; 0.49279 0.11262 -0.670411825 15.61689078 15.2437 0.54762 KBTBD3 2.5976137143971e-05 0.760114281056092 0.239859742806764 kelch repeat and BTB domain containing 3 . . . . . 0.20490 0.12678 -0.380166007 27.88393489 77.29109 1.84658 KBTBD4 0.0180743639557145 0.960923812652089 0.0210018233921969 kelch repeat and BTB domain containing 4 . . . ovary;umbilical cord;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;thyroid;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;urinary;blood;pancreas;lung;epididymis;placenta;visual apparatus;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;ciliary ganglion;caudate nucleus; 0.38031 0.10841 -0.646543901 16.44255721 72.84218 1.78150 KBTBD6 0.934819360334992 0.0651189909347395 6.16487302686338e-05 kelch repeat and BTB domain containing 6 . . . . . 0.31104 . -0.424258538 25.56027365 46.52415 1.31697 KBTBD7 0.223860925044712 0.774484269990277 0.00165480496501039 kelch repeat and BTB domain containing 7 . . . . . 0.27658 0.10883 -0.934977358 9.465675867 38.24337 1.13557 KBTBD8 0.00167056987470839 0.971364254042452 0.0269651760828402 kelch repeat and BTB domain containing 8 . . . unclassifiable (Anatomical System);breast;lung;cartilage;liver;testis;colon;germinal center;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.19830 0.09958 0.064394823 58.84642604 1066.42592 6.26307 KBTBD11 0.273543144822399 0.634342323630557 0.092114531547044 kelch repeat and BTB domain containing 11 . . . developmental;colon;fovea centralis;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;testis;pineal gland;brain;unclassifiable (Anatomical System);amygdala;heart;tongue;blood;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;cerebellum; amygdala;occipital lobe;subthalamic nucleus;medulla oblongata;temporal lobe;prefrontal cortex;globus pallidus;pons;cingulate cortex;parietal lobe; 0.15962 . . . 52.53303 1.43494 KBTBD11-OT1 . . . KBTBD11 overlapping transcript 1 . . . . . . . . . . . KBTBD12 9.96465322017853e-13 0.0210860344460206 0.978913965552983 kelch repeat and BTB domain containing 12 . . . uterus;prostate;whole body;heart;hypothalamus;testis;skin;skeletal muscle; . 0.07973 0.09208 -0.111973265 45.35857514 84.18769 1.95354 KBTBD13 3.34282857078106e-05 0.20190797224838 0.798058599465912 kelch repeat and BTB domain containing 13 FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. {ECO:0000269|PubMed:22542517}.; DISEASE: Nemaline myopathy 6 (NEM6) [MIM:609273]: A form of nemaline myopathy characterized by childhood onset of slowly progressive proximal muscle weakness, exercise intolerance, and slow movements with stiff muscles. Patients are unable to run or correct themselves from falling over. {ECO:0000269|PubMed:21109227}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in skeletal muscle. {ECO:0000269|PubMed:21109227}.; . . . . . . 119.54299 2.37939 KCMF1 0.595292976154389 0.402689521873237 0.00201750197237428 potassium channel modulatory factor 1 FUNCTION: Has intrinsic E3 ubiquitin ligase activity and promotes ubiquitination. {ECO:0000269|PubMed:15581609}.; . . . . 0.12565 0.09229 -0.207437529 38.2814343 7.00971 0.26223 KCNA1 0.0518014558510951 0.86150834480816 0.0866901993407449 potassium voltage-gated channel subfamily A member 1 FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the kidney (PubMed:19903818). Contributes to the regulation of the membrane potential and nerve signaling, and prevents neuronal hyperexcitability (PubMed:17156368). Forms tetrameric potassium- selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:19912772). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:12077175, PubMed:17156368). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation of delayed rectifier potassium channels (PubMed:12077175, PubMed:17156368). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA1 forms a delayed-rectifier potassium channel that opens in response to membrane depolarization, followed by slow spontaneous channel closure (PubMed:19912772, PubMed:19968958, PubMed:19307729, PubMed:19903818). In contrast, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (PubMed:17156368). Regulates neuronal excitability in hippocampus, especially in mossy fibers and medial perforant path axons, preventing neuronal hyperexcitability. Response to toxins that are selective for KCNA1, respectively for KCNA2, suggests that heteromeric potassium channels composed of both KCNA1 and KCNA2 play a role in pacemaking and regulate the output of deep cerebellar nuclear neurons (By similarity). May function as down- stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons (By similarity). May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) release (By similarity). Plays a role in regulating the generation of action potentials and preventing hyperexcitability in myelinated axons of the vagus nerve, and thereby contributes to the regulation of heart contraction (By similarity). Required for normal neuromuscular responses (PubMed:11026449, PubMed:17136396). Regulates the frequency of neuronal action potential firing in response to mechanical stimuli, and plays a role in the perception of pain caused by mechanical stimuli, but does not play a role in the perception of pain due to heat stimuli (By similarity). Required for normal responses to auditory stimuli and precise location of sound sources, but not for sound perception (By similarity). The use of toxins that block specific channels suggest that it contributes to the regulation of the axonal release of the neurotransmitter dopamine (By similarity). Required for normal postnatal brain development and normal proliferation of neuronal precursor cells in the brain (By similarity). Plays a role in the reabsorption of Mg(2+) in the distal convoluted tubules in the kidney and in magnesium ion homeostasis, probably via its effect on the membrane potential (PubMed:23903368, PubMed:19307729). {ECO:0000250|UniProtKB:P10499, ECO:0000269|PubMed:11026449, ECO:0000269|PubMed:12077175, ECO:0000269|PubMed:15837928, ECO:0000269|PubMed:17136396, ECO:0000269|PubMed:17156368, ECO:0000269|PubMed:19307729, ECO:0000269|PubMed:19903818, ECO:0000269|PubMed:19912772, ECO:0000269|PubMed:19968958, ECO:0000269|PubMed:21106501, ECO:0000269|PubMed:23903368}.; DISEASE: Episodic ataxia 1 (EA1) [MIM:160120]: An autosomal dominant disorder characterized by brief episodes of ataxia and dysarthria. Neurological examination during and between the attacks demonstrates spontaneous, repetitive discharges in the distal musculature (myokymia) that arise from peripheral nerve. Nystagmus is absent. {ECO:0000269|PubMed:10355668, ECO:0000269|PubMed:11013453, ECO:0000269|PubMed:11026449, ECO:0000269|PubMed:15532032, ECO:0000269|PubMed:7842011, ECO:0000269|PubMed:8541859, ECO:0000269|PubMed:8871592, ECO:0000269|PubMed:9600245}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myokymia isolated 1 (MK1) [MIM:160120]: A condition characterized by spontaneous involuntary contraction of muscle fiber groups that can be observed as vermiform movement of the overlying skin. Electromyography typically shows continuous motor unit activity with spontaneous oligo- and multiplet-discharges of high intraburst frequency (myokymic discharges). Isolated spontaneous muscle twitches occur in many persons and have no grave significance. {ECO:0000269|PubMed:11026449, ECO:0000269|PubMed:17136396, ECO:0000269|PubMed:19307729}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected adjacent to nodes of Ranvier in juxtaparanodal zones in spinal cord nerve fibers, but also in paranodal regions in some myelinated spinal cord axons (at protein level) (PubMed:11086297). Detected in the islet of Langerhans (PubMed:21483673). {ECO:0000269|PubMed:11086297, ECO:0000269|PubMed:21483673}.; . . 0.68837 0.29918 -0.558357437 19.54470394 19.30329 0.66481 KCNA2 0.884173956445609 0.115556030273547 0.000270013280844154 potassium voltage-gated channel subfamily A member 2 FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the cardiovascular system. Prevents aberrant action potential firing and regulates neuronal output. Forms tetrameric potassium- selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:19912772, PubMed:8495559, PubMed:11211111, PubMed:23769686). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:8495559, PubMed:20220134). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation of delayed rectifier potassium channels. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA2 forms a delayed-rectifier potassium channel that opens in response to membrane depolarization, followed by slow spontaneous channel closure (PubMed:19912772, PubMed:23769686). In contrast, a heteromultimer formed by KCNA2 and KCNA4 shows rapid inactivation (PubMed:8495559). Regulates neuronal excitability and plays a role as pacemaker in the regulation of neuronal action potentials (By similarity). KCNA2- containing channels play a presynaptic role and prevent hyperexcitability and aberrant action potential firing (By similarity). Response to toxins that are selective for KCNA2- containing potassium channels suggests that in Purkinje cells, dendritic subthreshold KCNA2-containing potassium channels prevent random spontaneous calcium spikes, suppressing dendritic hyperexcitability without hindering the generation of somatic action potentials, and thereby play an important role in motor coordination (By similarity). Plays a role in the induction of long-term potentiation of neuron excitability in the CA3 layer of the hippocampus (By similarity). May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons (By similarity). May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) (By similarity). Contributes to the regulation of the axonal release of the neurotransmitter dopamine (By similarity). Reduced KCNA2 expression plays a role in the perception of neuropathic pain after peripheral nerve injury, but not acute pain (By similarity). Plays a role in the regulation of the time spent in non-rapid eye movement (NREM) sleep (By similarity). {ECO:0000250|UniProtKB:P63141, ECO:0000250|UniProtKB:P63142, ECO:0000269|PubMed:11211111, ECO:0000269|PubMed:19912772, ECO:0000269|PubMed:20220134, ECO:0000269|PubMed:23769686, ECO:0000269|PubMed:8495559, ECO:0000305}.; DISEASE: Epileptic encephalopathy, early infantile, 32 (EIEE32) [MIM:616366]: A form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. {ECO:0000269|PubMed:25477152, ECO:0000269|PubMed:25751627}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in brain cortex (PubMed:16473933). Detected in peroneal nerve in the juxtaparanodal regions of the node of Ranvier; expression is decreased in patients with diabetes mellitus that suffer from axonal neuropathy (PubMed:22649228). Detected in paranodal and juxtanodal zones in myelinated spinal cord (at protein level) (PubMed:11086297). {ECO:0000269|PubMed:11086297, ECO:0000269|PubMed:16473933, ECO:0000269|PubMed:22649228}.; unclassifiable (Anatomical System);optic nerve;macula lutea;fovea centralis;choroid;lens;retina; uterus corpus;globus pallidus;trigeminal ganglion;skeletal muscle; 0.43318 0.21500 -0.427900189 25.14744043 3.20723 0.11521 KCNA3 . . . potassium voltage-gated channel subfamily A member 3 FUNCTION: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.; . . . . 0.28695 0.22806 0.215080721 67.91696155 152.59276 2.70218 KCNA4 0.946234021376117 0.0535797981997496 0.000186180424133949 potassium voltage-gated channel subfamily A member 4 FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:19912772, PubMed:8495559). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:8495559). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA4 forms a potassium channel that opens in response to membrane depolarization, followed by rapid spontaneous channel closure (PubMed:19912772, PubMed:8495559). Likewise, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (PubMed:17156368). {ECO:0000269|PubMed:17156368, ECO:0000269|PubMed:19912772, ECO:0000269|PubMed:8495559}.; . TISSUE SPECIFICITY: Detected in heart ventricle. {ECO:0000269|PubMed:2001794}.; lung;germinal center; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.75288 0.15048 -0.53631094 20.53550366 21.51947 0.72500 KCNA5 0.000687391815094003 0.747420322165551 0.251892286019355 potassium voltage-gated channel subfamily A member 5 FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:12130714). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (PubMed:12130714). Homotetrameric channels display rapid activation and slow inactivation (PubMed:8505626, PubMed:12130714). May play a role in regulating the secretion of insulin in normal pancreatic islets. Isoform 2 exhibits a voltage-dependent recovery from inactivation and an excessive cumulative inactivation (PubMed:11524461). {ECO:0000269|PubMed:11524461, ECO:0000269|PubMed:12130714, ECO:0000269|PubMed:8505626}.; DISEASE: Atrial fibrillation, familial, 7 (ATFB7) [MIM:612240]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:16772329}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Pancreatic islets and insulinoma.; smooth muscle;islets of Langerhans;colon;choroid;fovea centralis;lens;retina;optic nerve;whole body;macula lutea;kidney;brain;stomach; superior cervical ganglion;hypothalamus;trigeminal ganglion; 0.24009 0.20636 0.799205007 87.58551545 249.24831 3.40181 KCNA6 0.961132595185659 0.0387845453189222 8.28594954185624e-05 potassium voltage-gated channel subfamily A member 6 FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient (PubMed:2347305, PubMed:14575698). The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:2347305, PubMed:14575698). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA6, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (By similarity). Homotetrameric channels display rapid activation and slow inactivation (PubMed:2347305). {ECO:0000250|UniProtKB:P17659, ECO:0000269|PubMed:14575698, ECO:0000269|PubMed:2347305}.; . . frontal lobe;liver;brain; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.13203 0.12092 -0.516085732 21.20193442 14.73713 0.53103 KCNA7 0.00825022329951349 0.791943734974387 0.1998060417261 potassium voltage-gated channel subfamily A member 7 FUNCTION: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart and kidney. {ECO:0000269|PubMed:11368907, ECO:0000269|PubMed:11896454}.; amniotic fluid;skeletal muscle; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11558 . -0.135838822 43.77211607 5899.09126 15.93224 KCNA10 0.00305948856082549 0.590610125617892 0.406330385821283 potassium voltage-gated channel subfamily A member 10 FUNCTION: Mediates voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. The channel activity is up-regulated by cAMP. {ECO:0000269|PubMed:10836990}.; . TISSUE SPECIFICITY: Detected in kidney, in proximal tubules, glomerular endothelium, in vascular endothelium and in smooth muscle cells. {ECO:0000269|PubMed:12444201}.; . . 0.19199 0.16616 -0.350843407 29.54116537 806.83881 5.59494 KCNAB1 0.0665503434443176 0.932841287012373 0.000608369543309942 potassium voltage-gated channel subfamily A member regulatory beta subunit 1 FUNCTION: Cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits (PubMed:7499366, PubMed:7603988, PubMed:17156368,PubMed:17540341, PubMed:19713757). Modulates action potentials via its effect on the pore-forming alpha subunits (By similarity). Promotes expression of the pore-forming alpha subunits at the cell membrane, and thereby increases channel activity (By similarity). Mediates closure of delayed rectifier potassium channels by physically obstructing the pore via its N-terminal domain and increases the speed of channel closure for other family members (PubMed:9763623). Promotes the closure of KCNA1, KCNA2 and KCNA5 channels (PubMed:7499366, PubMed:7890032, PubMed:7603988, PubMed:7649300, PubMed:8938711, PubMed:12077175, PubMed:12130714, PubMed:15361858, PubMed:17540341, PubMed:19713757). Accelerates KCNA4 channel closure (PubMed:7890032, PubMed:7649300, PubMed:7890764, PubMed:9763623). Accelerates the closure of heteromeric channels formed by KCNA1 and KCNA4 (PubMed:17156368). Accelerates the closure of heteromeric channels formed by KCNA2, KCNA5 and KCNA6 (By similarity). Isoform KvB1.2 has no effect on KCNA1, KCNA2 or KCNB1 (PubMed:7890032, PubMed:7890764). Enhances KCNB1 and KCNB2 channel activity (By similarity). Binds NADPH; this is required for efficient down-regulation of potassium channel activity (PubMed:17540341). Has NADPH-dependent aldoketoreductase activity (By similarity). Oxidation of the bound NADPH strongly decreases N-type inactivation of potassium channel activity (By similarity). {ECO:0000250|UniProtKB:P63143, ECO:0000250|UniProtKB:P63144, ECO:0000269|PubMed:12077175, ECO:0000269|PubMed:12130714, ECO:0000269|PubMed:15361858, ECO:0000269|PubMed:17156368, ECO:0000269|PubMed:17540341, ECO:0000269|PubMed:19713757, ECO:0000269|PubMed:7499366, ECO:0000269|PubMed:7603988, ECO:0000269|PubMed:7649300, ECO:0000269|PubMed:7890032, ECO:0000269|PubMed:7890764, ECO:0000269|PubMed:8938711, ECO:0000269|PubMed:9763623, ECO:0000305}.; . TISSUE SPECIFICITY: In brain, expression is most prominent in caudate nucleus, hippocampus and thalamus. Significant expression also detected in amygdala and subthalamic nucleus. Also expressed in both healthy and cardiomyopathic heart. Up to four times more abundant in left ventricle than left atrium. {ECO:0000269|PubMed:7603988, ECO:0000269|PubMed:8938711}.; unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;colon;fovea centralis;skin;skeletal muscle;retina;uterus;prostate;lung;frontal lobe;nasopharynx;thyroid;placenta;macula lutea;liver;testis;spleen;kidney;brain;mammary gland;aorta;cerebellum; whole brain;amygdala;dorsal root ganglion;superior cervical ganglion;occipital lobe;medulla oblongata;thyroid;prefrontal cortex;globus pallidus;caudate nucleus;pons;parietal lobe;cerebellum; 0.79875 0.16226 -0.44448505 24.46331682 211.38456 3.13509 KCNAB1-AS1 . . . KCNAB1 antisense RNA 1 . . . . . . . . . . . KCNAB1-AS2 . . . KCNAB1 antisense RNA 2 . . . . . . . . . . . KCNAB2 0.839972632374732 0.159897641226689 0.000129726398578682 potassium voltage-gated channel subfamily A regulatory beta subunit 2 FUNCTION: Cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits (PubMed:7649300, PubMed:11825900). Contributes to the regulation of nerve signaling, and prevents neuronal hyperexcitability (By similarity). Promotes expression of the pore-forming alpha subunits at the cell membrane, and thereby increases channel activity (By similarity). Promotes potassium channel closure via a mechanism that does not involve physical obstruction of the channel pore (PubMed:7649300, PubMed:11825900). Promotes KCNA4 channel closure (PubMed:7649300, PubMed:11825900). Modulates the functional properties of KCNA5 (By similarity). Enhances KCNB2 channel activity (By similarity). Binds NADPH and has NADPH- dependent aldoketoreductase activity (By similarity). Has broad substrate specificity and can catalyze the reduction of methylglyoxal, 9,10-phenanthrenequinone, prostaglandin J2, 4- nitrobenzaldehyde, 4-nitroacetophenone and 4-oxo-trans-2-nonenal (in vitro) (By similarity). {ECO:0000250|UniProtKB:P62482, ECO:0000250|UniProtKB:P62483, ECO:0000269|PubMed:11825900, ECO:0000269|PubMed:7649300}.; . TISSUE SPECIFICITY: Detected in myelinated nerve fibers in the spinal cord, in the juxtaparanodal region of the nodes of Ranvier, but also in the paranodal region (PubMed:11086297). Detected in hippocampus (at protein level) (PubMed:21357749). Detected in hippocampus (PubMed:7649300). {ECO:0000269|PubMed:11086297, ECO:0000269|PubMed:21357749, ECO:0000269|PubMed:7649300}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;cervix;kidney;stomach; amygdala;dorsal root ganglion;whole brain;superior cervical ganglion;thalamus;occipital lobe;medulla oblongata;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.35930 0.18619 -0.426079032 25.36565228 161.34463 2.77476 KCNAB3 6.03305809092679e-12 0.207529028050386 0.792470971943581 potassium voltage-gated channel subfamily A regulatory beta subunit 3 FUNCTION: Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Alters the functional properties of Kv1.5. {ECO:0000269|PubMed:9857044}.; . TISSUE SPECIFICITY: Brain specific. Most prominent expression in cerebellum. Weaker signals detected in cortex, occipital lobe, frontal lobe and temporal lobe. Not detected in spinal cord, heart, lung, liver, kidney, pancreas, placenta and skeletal muscle. {ECO:0000269|PubMed:9857044}.; unclassifiable (Anatomical System);optic nerve;macula lutea;testis;colon;fovea centralis;choroid;lens;retina; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.27947 . -0.293801652 32.93819297 67.31103 1.69797 KCNB1 0.982587869780031 0.0174098217265908 2.30849337863719e-06 potassium voltage-gated channel subfamily B member 1 FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. Contributes to the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neurons, muscle cells and endocrine cells and plays a role in homeostatic attenuation of electrical excitability throughout the brain (PubMed:23161216). Plays also a role in the regulation of exocytosis independently of its electrical function (By similarity). Forms tetrameric potassium- selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization (PubMed:8081723, PubMed:1283219, PubMed:10484328, PubMed:12560340, PubMed:19074135, PubMed:19717558, PubMed:24901643). Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB2; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1, creating a functionally diverse range of channel complexes (PubMed:10484328, PubMed:11852086, PubMed:12060745, PubMed:19074135, PubMed:19717558, PubMed:24901643). Heterotetrameric channel activity formed with KCNS3 show increased current amplitude with the threshold for action potential activation shifted towards more negative values in hypoxic-treated pulmonary artery smooth muscle cells (By similarity). Channel properties are also modulated by cytoplasmic ancillary beta subunits such as AMIGO1, KCNE1, KCNE2 and KCNE3, slowing activation and inactivation rate of the delayed rectifier potassium channels (By similarity). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Major contributor to the slowly inactivating delayed-rectifier voltage- gated potassium current in neurons of the central nervous system, sympathetic ganglion neurons, neuroendocrine cells, pancreatic beta cells, cardiomyocytes and smooth muscle cells. Mediates the major part of the somatodendritic delayed-rectifier potassium current in hippocampal and cortical pyramidal neurons and sympathetic superior cervical ganglion (CGC) neurons that acts to slow down periods of firing, especially during high frequency stimulation. Plays a role in the induction of long-term potentiation (LTP) of neuron excitability in the CA3 layer of the hippocampus (By similarity). Contributes to the regulation of glucose-induced action potential amplitude and duration in pancreatic beta cells, hence limiting calcium influx and insulin secretion (PubMed:23161216). Plays a role in the regulation of resting membrane potential and contraction in hypoxia-treated pulmonary artery smooth muscle cells. May contribute to the regulation of the duration of both the action potential of cardiomyocytes and the heart ventricular repolarization QT interval. Contributes to the pronounced pro-apoptotic potassium current surge during neuronal apoptotic cell death in response to oxidative injury. May confer neuroprotection in response to hypoxia/ischemic insults by suppressing pyramidal neurons hyperexcitability in hippocampal and cortical regions (By similarity). Promotes trafficking of KCNG3, KCNH1 and KCNH2 to the cell surface membrane, presumably by forming heterotetrameric channels with these subunits (PubMed:12060745). Plays a role in the calcium-dependent recruitment and release of fusion-competent vesicles from the soma of neurons, neuroendocrine and glucose- induced pancreatic beta cells by binding key components of the fusion machinery in a pore-independent manner (By similarity). {ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q03717, ECO:0000269|PubMed:10484328, ECO:0000269|PubMed:11852086, ECO:0000269|PubMed:12060745, ECO:0000269|PubMed:12560340, ECO:0000269|PubMed:1283219, ECO:0000269|PubMed:19074135, ECO:0000269|PubMed:19717558, ECO:0000269|PubMed:23161216, ECO:0000269|PubMed:24901643, ECO:0000269|PubMed:8081723}.; DISEASE: Epileptic encephalopathy, early infantile, 26 (EIEE26) [MIM:616056]: A form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. EIEE26 patients manifest multiple types of seizures, delayed psychomotor development, poor or absent speech, hypotonia, hypsarrhythmia. {ECO:0000269|PubMed:25164438}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in neocortical pyramidal cells (PubMed:24477962). Expressed in pancreatic beta cells (at protein level) (PubMed:12403834, PubMed:14988243). Expressed in brain, heart, lung, liver, colon, kidney and adrenal gland (PubMed:19074135). Expressed in the cortex, amygdala, cerebellum, pons, thalamus, hypothalamus, hippocampus and substantia nigra (PubMed:19074135). {ECO:0000269|PubMed:12403834, ECO:0000269|PubMed:14988243, ECO:0000269|PubMed:19074135, ECO:0000269|PubMed:24477962}.; . . 0.69855 0.14066 -0.045835247 50.34206181 123.58507 2.42029 KCNB2 0.954615847239045 0.0453791306689589 5.02209199640962e-06 potassium voltage-gated channel subfamily B member 2 FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and smooth muscle cells. Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization. Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB1; channel properties depend on the type of alpha subunits that are part of the channel. Can also form functional heterotetrameric channels with other alpha subunits that are non- conducting when expressed alone, such as KCNS1 and KCNS2, creating a functionally diverse range of channel complexes. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Contributes to the delayed-rectifier voltage-gated potassium current in cortical pyramidal neurons and smooth muscle cells. {ECO:0000250|UniProtKB:A6H8H5, ECO:0000250|UniProtKB:Q63099}.; . . . . 0.26567 0.11554 -1.107723888 6.829440906 126.18709 2.44478 KCNC1 0.70997213579973 0.286645072175769 0.00338279202450167 potassium voltage-gated channel subfamily C member 1 FUNCTION: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNC2, and possibly other family members as well. Contributes to fire sustained trains of very brief action potentials at high frequency in pallidal neurons. {ECO:0000250|UniProtKB:P25122}.; DISEASE: Epilepsy, progressive myoclonic 7 (EPM7) [MIM:616187]: A neurologic disorder characterized by progressive myoclonic epilepsy, manifesting in the first or second decades of life. Cognitive function may decline in some patients. Myoclonus is a brief, involuntary twitching of a muscle or a group of muscles. {ECO:0000269|PubMed:25401298}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);optic nerve;lung;frontal lobe;islets of Langerhans;macula lutea;testis;fovea centralis;choroid;lens;brain;retina; amygdala;whole brain;medulla oblongata;occipital lobe;superior cervical ganglion;cerebellum peduncles;temporal lobe;pons;skeletal muscle;subthalamic nucleus;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.12238 0.17686 -0.670411825 15.61689078 12.54992 0.45762 KCNC2 0.00359681821930559 0.953997927949849 0.0424052538308452 potassium voltage-gated channel subfamily C member 2 FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Contributes to the regulation of the fast action potential repolarization and in sustained high-frequency firing in neurons of the central nervous system. Homotetramer channels mediate delayed-rectifier voltage-dependent potassium currents that activate rapidly at high-threshold voltages and inactivate slowly. Forms tetrameric channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:15709110). Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNC1, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel. Channel properties may be modulated either by the association with ancillary subunits, such as KCNE1, KCNE2 or KCNE3 or indirectly by nitric oxide (NO) through a cGMP- and PKG- mediated signaling cascade, slowing channel activation and deactivation of delayed rectifier potassium channels (By similarity). Contributes to fire sustained trains of very brief action potentials at high frequency in retinal ganglion cells, thalamocortical and suprachiasmatic nucleus (SCN) neurons and in hippocampal and neocortical interneurons (PubMed:15709110). Sustained maximal action potential firing frequency in inhibitory hippocampal interneurons is negatively modulated by histamine H2 receptor activation in a cAMP- and protein kinase (PKA) phosphorylation-dependent manner. Plays a role in maintaining the fidelity of synaptic transmission in neocortical GABAergic interneurons by generating action potential (AP) repolarization at nerve terminals, thus reducing spike-evoked calcium influx and GABA neurotransmitter release. Required for long-range synchronization of gamma oscillations over distance in the neocortex. Contributes to the modulation of the circadian rhythm of spontaneous action potential firing in suprachiasmatic nucleus (SCN) neurons in a light-dependent manner (By similarity). {ECO:0000250|UniProtKB:P22462, ECO:0000250|UniProtKB:Q14B80, ECO:0000269|PubMed:15709110, ECO:0000305|PubMed:10414303, ECO:0000305|PubMed:11506885}.; . . unclassifiable (Anatomical System);ovary;parathyroid;fovea centralis;choroid;lens;retina;prostate;optic nerve;whole body;lung;frontal lobe;placenta;macula lutea;testis;brain; amygdala;subthalamic nucleus;superior cervical ganglion;temporal lobe;appendix;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.28515 0.09778 -0.824740496 11.67728238 45.56534 1.29687 KCNC3 0.850943334894472 0.148530845199587 0.000525819905941795 potassium voltage-gated channel subfamily C member 3 FUNCTION: This protein mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. {ECO:0000269|PubMed:16501573, ECO:0000269|PubMed:19953606, ECO:0000269|PubMed:21479265, ECO:0000269|PubMed:23734863, ECO:0000269|PubMed:25756792}.; DISEASE: Spinocerebellar ataxia 13 (SCA13) [MIM:605259]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA13 is an autosomal dominant cerebellar ataxia (ADCA) characterized by slow progression and variable age at onset, ranging from childhood to late adulthood. Mental retardation can be present in some patients. {ECO:0000269|PubMed:16501573, ECO:0000269|PubMed:19953606, ECO:0000269|PubMed:21479265, ECO:0000269|PubMed:23734863, ECO:0000269|PubMed:25152487, ECO:0000269|PubMed:25756792}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.34248 0.17819 . . 299.8305 3.69222 KCNC4 0.00053422527064709 0.88806364070724 0.111402134022113 potassium voltage-gated channel subfamily C member 4 FUNCTION: This protein mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.; . . . . 0.59042 0.15244 -0.418800956 25.79028073 907.43684 5.86060 KCNC4-AS1 . . . KCNC4 antisense RNA 1 (head to head) . . . . . . . . . . . KCND1 0.447025940564966 0.546567883250052 0.00640617618498254 potassium voltage-gated channel subfamily D member 1 FUNCTION: Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain, in particular in cerebellum and thalamus; detected at lower levels in the other parts of the brain. {ECO:0000269|PubMed:10729221}.; unclassifiable (Anatomical System);amygdala;heart;colon;brain; dorsal root ganglion;superior cervical ganglion;testis - interstitial;subthalamic nucleus;appendix;atrioventricular node;trigeminal ganglion; 0.47089 0.13841 -0.179930907 40.35739561 97.55084 2.13521 KCND2 0.980460832264043 0.0195385471509323 6.2058502495759e-07 potassium voltage-gated channel subfamily D member 2 FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Mediates the major part of the dendritic A-type current I(SA) in brain neurons (By similarity). This current is activated at membrane potentials that are below the threshold for action potentials. It regulates neuronal excitability, prolongs the latency before the first spike in a series of action potentials, regulates the frequency of repetitive action potential firing, shortens the duration of action potentials and regulates the back-propagation of action potentials from the neuronal cell body to the dendrites. Contributes to the regulation of the circadian rhytm of action potential firing in suprachiasmatic nucleus neurons, which regulates the circadian rhythm of locomotor activity (By similarity). Functions downstream of the metabotropic glutamate receptor GRM5 and plays a role in neuronal excitability and in nociception mediated by activation of GRM5 (By similarity). Mediates the transient outward current I(to) in rodent heart left ventricle apex cells, but not in human heart, where this current is mediated by another family member. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient (PubMed:10551270, PubMed:15454437, PubMed:14695263, PubMed:14623880, PubMed:14980201, PubMed:16934482, PubMed:24811166, PubMed:24501278). The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:11507158). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCND2 and KCND3; channel properties depend on the type of pore-forming alpha subunits that are part of the channel. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes. Interaction with specific isoforms of the regulatory subunits KCNIP1, KCNIP2, KCNIP3 or KCNIP4 strongly increases expression at the cell surface and thereby increases channel activity; it modulates the kinetics of channel activation and inactivation, shifts the threshold for channel activation to more negative voltage values, shifts the threshold for inactivation to less negative voltages and accelerates recovery after inactivation (PubMed:15454437, PubMed:14623880, PubMed:14980201, PubMed:19171772, PubMed:24501278, PubMed:24811166). Likewise, interaction with DPP6 or DPP10 promotes expression at the cell membrane and regulates both channel characteristics and activity (By similarity). {ECO:0000250|UniProtKB:Q63881, ECO:0000250|UniProtKB:Q9Z0V2, ECO:0000269|PubMed:10551270, ECO:0000269|PubMed:10729221, ECO:0000269|PubMed:11507158, ECO:0000269|PubMed:14623880, ECO:0000269|PubMed:14695263, ECO:0000269|PubMed:14980201, ECO:0000269|PubMed:15454437, ECO:0000269|PubMed:16934482, ECO:0000269|PubMed:19171772, ECO:0000269|PubMed:24501278, ECO:0000269|PubMed:24811166}.; DISEASE: Note=KNCD2 mutations have been found in a family with autism and epilepsy and may play a role in disease pathogenesis. Autism is a complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Epilepsy is characterized by paroxysmal transient disturbances of the electrical activity of the brain that may be manifested as episodic impairment or loss of consciousness, abnormal motor phenomena, psychic or sensory disturbances, or perturbation of the autonomic nervous system. {ECO:0000269|PubMed:24501278}.; DISEASE: Note=A KCND2 mutation leading to the production of a C- terminally truncated protein has been identified in a patient with epilepsy. Epilepsy is characterized by paroxysmal transient disturbances of the electrical activity of the brain that may be manifested as episodic impairment or loss of consciousness, abnormal motor phenomena, psychic or sensory disturbances, or perturbation of the autonomic nervous system. {ECO:0000269|PubMed:16934482}.; TISSUE SPECIFICITY: Detected in ovary, in corpus luteum and in granulosa and theca cells in the follicle (at protein level) (PubMed:15991246). Highly expressed throughout the brain (PubMed:10551270, PubMed:10729221). Detected in amygdala, caudate nucleus, cerebellum, hippocampus, substantia nigra and thalamus (PubMed:10551270, PubMed:10729221). Expression is not detectable or very low in heart, kidney, liver, lung, pancreas and skeletal muscle (PubMed:10551270, PubMed:10729221). Not detectable in human heart atrium (PubMed:12395204). {ECO:0000269|PubMed:10551270, ECO:0000269|PubMed:10729221, ECO:0000269|PubMed:12395204, ECO:0000269|PubMed:15991246}.; unclassifiable (Anatomical System);ovary;placenta;adrenal cortex;parathyroid; superior cervical ganglion;cerebellum peduncles;caudate nucleus;trigeminal ganglion;cerebellum; 0.21454 0.15244 -0.646543901 16.44255721 25.22755 0.82507 KCND3 0.803752595406802 0.196020425572708 0.00022697902048915 potassium voltage-gated channel subfamily D member 3 FUNCTION: Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits. {ECO:0000269|PubMed:10200233, ECO:0000269|PubMed:9843794}.; DISEASE: Spinocerebellar ataxia 19 (SCA19) [MIM:607346]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA19 is a relatively mild, cerebellar ataxic syndrome with cognitive impairment, pyramidal tract involvement, tremor and peripheral neuropathy, and mild atrophy of the cerebellar hemispheres and vermis. {ECO:0000269|PubMed:23280837, ECO:0000269|PubMed:23280838}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Brugada syndrome 9 (BRGDA9) [MIM:616399]: A tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs, the individual will faint and may die in a few minutes if the heart is not reset. {ECO:0000269|PubMed:21349352, ECO:0000269|PubMed:22457051}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in heart and brain, in particular in cortex, cerebellum, amygdala and caudate nucleus. Detected at lower levels in liver, skeletal muscle, kidney and pancreas. Isoform 1 predominates in most tissues. Isoform 1 and isoform 2 are detected at similar levels in brain, skeletal muscle and pancreas. {ECO:0000269|PubMed:10200233, ECO:0000269|PubMed:10729221, ECO:0000269|PubMed:9843794}.; lung;frontal lobe;brain; amygdala;occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;cerebellum peduncles;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.37542 0.19444 -0.80269335 12.23755603 16.29843 0.57745 KCND3-AS1 . . . KCND3 antisense RNA 1 . . . . . . . . . . . KCND3-IT1 . . . KCND3 intronic transcript 1 . . . . . . . . . . . KCNE1 0.00418613539147309 0.424177202813199 0.571636661795328 potassium voltage-gated channel subfamily E regulatory subunit 1 FUNCTION: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 (PubMed:19219384). Assembled with KCNQ1/KVLQT1 is proposed to form the slowly activating delayed rectifier cardiac potassium (IKs) channel. The outward current reaches its steady state only after 50 seconds. Assembled with KCNH2/HERG may modulate the rapidly activating component of the delayed rectifying potassium current in heart (IKr). {ECO:0000269|PubMed:19219384}.; DISEASE: Jervell and Lange-Nielsen syndrome 2 (JLNS2) [MIM:612347]: An autosomal recessive disorder characterized by congenital deafness, prolongation of the QT interval, syncopal attacks due to ventricular arrhythmias, and a high risk of sudden death. {ECO:0000269|PubMed:10400998, ECO:0000269|PubMed:9328483, ECO:0000269|PubMed:9354783}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Long QT syndrome 5 (LQT5) [MIM:613695]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. {ECO:0000269|PubMed:10400998, ECO:0000269|PubMed:10973849, ECO:0000269|PubMed:11692163, ECO:0000269|PubMed:16414944, ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:9354802, ECO:0000269|PubMed:9445165}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in lung, kidney, testis, ovaries, small intestine, peripheral blood leukocytes. Expressed in the heart (PubMed:19219384). Not detected in pancreas, spleen, prostate and colon. Restrictively localized in the apical membrane portion of epithelial cells. {ECO:0000269|PubMed:19219384, ECO:0000269|PubMed:9312006}.; nasopharynx;spleen;peripheral nerve; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.11648 0.33265 0.060756528 58.52795471 36.55249 1.09567 KCNE1B . . . potassium voltage-gated channel subfamily E regulatory subunit 1B . . . . . . . . . . . KCNE2 0.0010184057784747 0.369588226723981 0.629393367497544 potassium voltage-gated channel subfamily E regulatory subunit 2 FUNCTION: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. Associated with KCNH2/HERG is proposed to form the rapidly activating component of the delayed rectifying potassium current in heart (IKr). May associate with KCNQ2 and/or KCNQ3 and modulate the native M-type current. May associate with HCN1 and HCN2 and increase potassium current. Interacts with KCNQ1; forms an heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (PubMed:11101505). {ECO:0000250|UniProtKB:P63161, ECO:0000269|PubMed:10219239, ECO:0000269|PubMed:11101505}.; DISEASE: Atrial fibrillation, familial, 4 (ATFB4) [MIM:611493]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:15368194}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in brain, heart, skeletal muscle, pancreas, placenta, kidney, colon and thymus. A small but significant expression is found in liver, ovary, testis, prostate, small intestine and leukocytes. Very low expression, nearly undetectable, in lung and spleen. {ECO:0000269|PubMed:11034315}.; unclassifiable (Anatomical System);uterus;heart;mammary gland;skin;stomach; dorsal root ganglion;superior cervical ganglion;testis;pons;trigeminal ganglion;skeletal muscle; 0.08034 0.11142 0.281220278 71.07808445 35.75366 1.07485 KCNE3 0.444435272345118 0.454755496231033 0.100809231423849 potassium voltage-gated channel subfamily E regulatory subunit 3 FUNCTION: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 (PubMed:12954870). Associated with KCNC4/Kv3.4 is proposed to form the subthreshold voltage-gated potassium channel in skeletal muscle and to establish the resting membrane potential (RMP) in muscle cells. Associated with KCNQ1/KCLQT1 may form the intestinal cAMP-stimulated potassium channel involved in chloride secretion that produces a current with nearly instantaneous activation with a linear current-voltage relationship. {ECO:0000250|UniProtKB:Q9JJV7, ECO:0000269|PubMed:10646604, ECO:0000269|PubMed:12954870}.; . TISSUE SPECIFICITY: Expressed in hippocampal neurons (at protein level) (PubMed:12954870). Widely expressed with highest levels in kidney and moderate levels in small intestine. {ECO:0000269|PubMed:10646604, ECO:0000269|PubMed:12954870}.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;blood;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;uterus;pancreas;prostate;optic nerve;lung;thyroid;placenta;macula lutea;liver;testis;spleen;kidney;stomach;peripheral nerve; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13222 0.12708 0.191216164 66.57230479 18.94968 0.65395 KCNE4 0.560426843330162 0.389899821673829 0.049673334996009 potassium voltage-gated channel subfamily E regulatory subunit 4 FUNCTION: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. May associate with KCNQ1/KVLTQ1 and inhibit potassium current.; . TISSUE SPECIFICITY: Predominantly expressed in embryo and adult uterus. Low expression found in kidney, small intestine, lung and heart. {ECO:0000269|PubMed:12096056}.; unclassifiable (Anatomical System);breast;uterus;lung;heart;bone;placenta;visual apparatus;liver;lens;skin;retina; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skin; 0.33747 0.11474 -0.029247611 51.40363293 34.28207 1.04962 KCNE5 . . . potassium voltage-gated channel subfamily E regulatory subunit 5 FUNCTION: Potassium channel ancillary subunit that is essential for generation of some native K(+) currents by virtue of formation of heteromeric ion channel complex with voltage-gated potassium (Kv) channel pore-forming alpha subunits. Functions as an inhibitory beta-subunit of the repolarizing cardiac potassium ion channel KCNQ1. {ECO:0000269|PubMed:12324418}.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, brain, spinal cord and placenta. {ECO:0000269|PubMed:10493825}.; . . 0.23746 0.10633 . . . . KCNF1 0.498369029988399 0.4817194213423 0.0199115486693014 potassium voltage-gated channel modifier subfamily F member 1 FUNCTION: Putative voltage-gated potassium channel.; . TISSUE SPECIFICITY: Detected in heart, brain, liver, skeletal muscle, kidney and pancreas.; unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;colon;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;frontal lobe;macula lutea;brain; amygdala;whole brain;thalamus;occipital lobe;temporal lobe;prefrontal cortex;pons;caudate nucleus;parietal lobe; 0.31233 0.11262 -0.249709319 35.74545883 5.08322 0.18810 KCNG1 0.274579646128645 0.70171528923272 0.0237050646386352 potassium voltage-gated channel modifier subfamily G member 1 FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 (PubMed:19074135). {ECO:0000269|PubMed:19074135}.; . TISSUE SPECIFICITY: Expressed in brain and placenta, and at much lower levels in kidney and pancreas (PubMed:9434767). {ECO:0000269|PubMed:9434767}.; . . 0.11795 0.16271 -0.626318434 17.03231894 6.96535 0.25964 KCNG2 0.00583161969703067 0.727112291134204 0.267056089168765 potassium voltage-gated channel modifier subfamily G member 2 FUNCTION: Potassium channel subunit. Modulates channel activity by shifting the threshold and the half-maximal activation to more negative values.; . TISSUE SPECIFICITY: Highly expressed in heart, liver, skeletal muscle, kidney and pancreas. Detected at low levels in brain, lung and placenta.; . . 0.07234 0.13505 . . 3066.36483 10.52777 KCNG3 0.0405974403481221 0.84279813880664 0.116604420845238 potassium voltage-gated channel modifier subfamily G member 3 FUNCTION: Potassium channel subunit that does not form functional channels by itself (PubMed:11852086). Can form functional heterotetrameric channels with KCNB1; this promotes a reduction in the rate of activation and inactivation of the delayed rectifier voltage-gated potassium channel KCNB1 (PubMed:11852086, PubMed:19074135). {ECO:0000269|PubMed:11852086, ECO:0000269|PubMed:19074135}.; . TISSUE SPECIFICITY: Expressed in the brain, liver, testis, small intestine, colon, thymus and adrenal gland (PubMed:11852086, PubMed:12060745). {ECO:0000269|PubMed:11852086, ECO:0000269|PubMed:12060745}.; unclassifiable (Anatomical System); superior cervical ganglion;ciliary ganglion; 0.22411 0.11710 -0.339715008 30.06605331 6.68052 0.24646 KCNG4 3.97041784376579e-17 0.000104529505364527 0.999895470494635 potassium voltage-gated channel modifier subfamily G member 4 FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 (PubMed:19074135). {ECO:0000269|PubMed:19074135}.; . TISSUE SPECIFICITY: Highly expressed in brain, and at lower levels in liver, small intestine and colon.; unclassifiable (Anatomical System);lymph node;muscle; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;atrioventricular node;parietal lobe; 0.07718 0.10675 1.429318999 95.00471809 7132.56288 18.17108 KCNH1 0.333014560273438 0.666958823148044 2.66165785182411e-05 potassium voltage-gated channel subfamily H member 1 FUNCTION: Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel (PubMed:22732247). Channel properties may be modulated by subunit assembly, but not by cyclic nucleotides (By similarity). Mediates IK(NI) current in myoblasts (PubMed:9738473). Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (PubMed:23881642). {ECO:0000250|UniProtKB:Q60603, ECO:0000269|PubMed:22732247, ECO:0000269|PubMed:23881642, ECO:0000269|PubMed:9738473}.; DISEASE: Temple-Baraitser syndrome (TMBTS) [MIM:611816]: A developmental disorder characterized by intellectual disability, epilepsy, hypoplasia or aplasia of the thumb and great toe nails, and broadening and/or elongation of the thumbs and halluces, which have a tubular aspect. Some patients show facial dysmorphism. {ECO:0000269|PubMed:25420144}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Zimmermann-Laband syndrome 1 (ZLS1) [MIM:135500]: A disorder characterized by gingival fibromatosis, dysplastic or absent nails, finger abnormalities, hepatosplenomegaly, and abnormalities of the cartilage of the nose and/or ears. {ECO:0000269|PubMed:25915598}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in brain and in myoblasts at the onset of fusion, but not in other tissues. Detected in HeLa (cervical carcinoma), SH-SY5Y (neuroblastoma) and MCF-7 (epithelial tumor) cells, but not in normal epithelial cells.; . . 0.50653 0.21528 -1.085675268 7.147912243 34.51063 1.05386 KCNH1-IT1 . . . KCNH1 intronic transcript 1 . . . . . . . . . . . KCNH2 0.996051301626768 0.00394868603003694 1.2343194797632e-08 potassium voltage-gated channel subfamily H member 2 FUNCTION: Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr). Isoforms USO have no channel activity by themself, but modulates channel characteristics by forming heterotetramers with other isoforms which are retained intracellularly and undergo ubiquitin-dependent degradation. {ECO:0000269|PubMed:18559421}.; DISEASE: Long QT syndrome 2 (LQT2) [MIM:613688]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. Deafness is often associated with long QT syndrome type 2. {ECO:0000269|PubMed:10086971, ECO:0000269|PubMed:10187793, ECO:0000269|PubMed:10220144, ECO:0000269|PubMed:10517660, ECO:0000269|PubMed:10735633, ECO:0000269|PubMed:10862094, ECO:0000269|PubMed:10973849, ECO:0000269|PubMed:11170080, ECO:0000269|PubMed:12062363, ECO:0000269|PubMed:12354768, ECO:0000269|PubMed:12442276, ECO:0000269|PubMed:12621127, ECO:0000269|PubMed:15051636, ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:16414944, ECO:0000269|PubMed:16922724, ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:22314138, ECO:0000269|PubMed:7889573, ECO:0000269|PubMed:8635257, ECO:0000269|PubMed:8877771, ECO:0000269|PubMed:8914737, ECO:0000269|PubMed:9024139, ECO:0000269|PubMed:9452080, ECO:0000269|PubMed:9544837, ECO:0000269|PubMed:9600240, ECO:0000269|PubMed:9693036}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Short QT syndrome 1 (SQT1) [MIM:609620]: A heart disorder characterized by idiopathic persistently and uniformly short QT interval on ECG in the absence of structural heart disease in affected individuals. It causes syncope and sudden death. {ECO:0000269|PubMed:14676148, ECO:0000269|PubMed:15828882}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in heart and brain. Isoforms USO are frequently overexpressed in cancer cells. {ECO:0000269|PubMed:18559421}.; myocardium;ovary;parathyroid;fovea centralis;choroid;retina;uterus;optic nerve;pituitary gland;testis;pineal gland;brain;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;blood;lens;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;aorta;stomach;cerebellum; superior cervical ganglion;testis;ciliary ganglion;caudate nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle;bone marrow; 0.70537 0.29759 -1.460519861 3.809860816 1151.75419 6.46689 KCNH3 0.999889995234816 0.000110004755295738 9.8883441471509e-12 potassium voltage-gated channel subfamily H member 3 FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits an outward current with fast inactivation. Channel properties may be modulated by cAMP and subunit assembly.; . TISSUE SPECIFICITY: Detected only in brain, in particular in the telencephalon. Detected in the cerebral cortex, occipital pole, frontal and temporal lobe, putamen, amygdala, hippocampus and caudate nucleus.; unclassifiable (Anatomical System);uterus;lymph node;lung;frontal lobe;endometrium;visual apparatus;pituitary gland;blood;brain;peripheral nerve;cerebellum; . 0.30623 0.11566 -0.879979233 10.5626327 913.18144 5.87517 KCNH4 0.999978751386027 2.12486130829045e-05 8.90426559559555e-13 potassium voltage-gated channel subfamily H member 4 FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits an outward current, but shows no inactivation. Channel properties may be modulated by cAMP and subunit assembly.; . TISSUE SPECIFICITY: Detected only in brain, in particular in the telencephalon. Detected in putamen and caudate nucleus, and at lower levels in cerebral cortex, occipital and hippocampus.; frontal lobe;cartilage;placenta;brain;tonsil; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion; 0.36979 0.22290 -1.681037809 2.659825431 71.76069 1.76347 KCNH5 0.769049292397075 0.230950103173978 6.04428947686762e-07 potassium voltage-gated channel subfamily H member 5 FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a non-inactivating outward rectifying current. Channel properties may be modulated by cAMP and subunit assembly.; . TISSUE SPECIFICITY: Detected in brain, skeletal muscle, heart, placenta, lung and liver, and at low levels in kidney.; unclassifiable (Anatomical System);lung;testis;brain; dorsal root ganglion;superior cervical ganglion;temporal lobe;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.60136 0.12831 -1.460519861 3.809860816 2072.70312 8.38771 KCNH6 3.93932913677419e-17 0.0102221857790722 0.989777814220928 potassium voltage-gated channel subfamily H member 6 FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a slowly activating, rectifying current (By similarity). Channel properties may be modulated by cAMP and subunit assembly. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in prolactin-secreting adenomas. {ECO:0000269|PubMed:12634931}.; unclassifiable (Anatomical System);lung;pineal gland; superior cervical ganglion;ciliary ganglion;atrioventricular node;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.29959 0.16889 -0.606336534 17.51002595 660.24764 5.15277 KCNH7 0.984445949327848 0.015554050552074 1.20077772915683e-10 potassium voltage-gated channel subfamily H member 7 FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel. Channel properties may be modulated by cAMP and subunit assembly.; . TISSUE SPECIFICITY: Expressed in prolactin-secreting adenomas. {ECO:0000269|PubMed:12634931}.; unclassifiable (Anatomical System);islets of Langerhans;liver;kidney;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.44125 0.12972 -0.306750577 32.23047889 337.49195 3.90139 KCNH8 0.000102483662649291 0.99987540720136 2.21091359911008e-05 potassium voltage-gated channel subfamily H member 8 FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a slowly activating, outward rectifying current. Channel properties may be modulated by cAMP and subunit assembly.; . TISSUE SPECIFICITY: Primarily expressed in the nervous system. {ECO:0000269|PubMed:12890647}.; unclassifiable (Anatomical System);uterus;frontal lobe;hippocampus;liver;testis;colon;brain;skeletal muscle; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.13625 0.13809 -0.481306408 22.80018872 971.16191 6.02371 KCNIP1 0.0202319565749317 0.961863176033854 0.0179048673912145 potassium voltage-gated channel interacting protein 1 FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Regulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND1/Kv4.1 and KCND2/Kv4.2 currents. Increases the presence of KCND2 at the cell surface. {ECO:0000269|PubMed:10676964, ECO:0000269|PubMed:11423117, ECO:0000269|PubMed:12829703, ECO:0000269|PubMed:17187064}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in brain and kidney. Isoform 1 is also expressed in liver, pancreas, skeletal muscle, small intestine and testis. Isoform 2 is also expressed in lung, pancreas, leukocytes, prostate and thymus.; optic nerve;ovary;islets of Langerhans;macula lutea;fovea centralis;choroid;lens;brain;retina; dorsal root ganglion;superior cervical ganglion;temporal lobe;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.45059 0.13588 -0.007201372 53.19061099 17.19709 0.60441 KCNIP2 0.018688177733799 0.961275459376716 0.0200363628894845 potassium voltage-gated channel interacting protein 2 FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Modulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved in KCND2 and KCND3 trafficking to the cell surface. May be required for the expression of I(To) currents in the heart (By similarity). {ECO:0000250|UniProtKB:Q9JJ69, ECO:0000269|PubMed:10676964, ECO:0000269|PubMed:11287421, ECO:0000269|PubMed:11684073, ECO:0000269|PubMed:12297301, ECO:0000269|PubMed:12829703, ECO:0000269|PubMed:14623880}.; . TISSUE SPECIFICITY: Expressed in brain. Colocalizes with KCND2 in excitatory neurons including cortical and hippocampal CA1 pyramidal cells. Isoform 3 is expressed in heart and in umbilical vein endothelial cells. Not expressed in fetal heart. {ECO:0000269|PubMed:11263977, ECO:0000269|PubMed:11684073, ECO:0000269|PubMed:15356203}.; unclassifiable (Anatomical System);pancreas;lung;cartilage;heart;pineal body;placenta;hippocampus;testis;spleen;brain;skeletal muscle; superior cervical ganglion;trigeminal ganglion; 0.40849 0.15516 -0.295622497 32.61972163 19.51693 0.66921 KCNIP2-AS1 . . . KCNIP2 antisense RNA 1 . . . . . . . . . . . KCNIP3 0.852600760709297 0.146888893885524 0.000510345405178801 potassium voltage-gated channel interacting protein 3 FUNCTION: Calcium-dependent transcriptional repressor that binds to the DRE element of genes including PDYN and FOS. Affinity for DNA is reduced upon binding to calcium and enhanced by binding to magnesium. Seems to be involved in nociception (By similarity). {ECO:0000250|UniProtKB:Q9QXT8}.; FUNCTION: May play a role in the regulation of PSEN2 proteolytic processing and apoptosis. Together with PSEN2 involved in modulation of beta-amyloid formation. {ECO:0000269|PubMed:11259376, ECO:0000269|PubMed:11988022, ECO:0000269|PubMed:9771752}.; . TISSUE SPECIFICITY: Highly expressed in brain. Widely expressed at lower levels. Expression levels are elevated in brain cortex regions affected by Alzheimer disease. {ECO:0000269|PubMed:14720210}.; unclassifiable (Anatomical System);amygdala;heart;ovary;islets of Langerhans;parathyroid;skin;uterus;pancreas;lung;frontal lobe;placenta;hippocampus;testis;kidney;brain;thymus; . 0.15192 0.14302 -0.005381972 53.50908233 50.17835 1.39158 KCNIP4 0.967714666988821 0.032233051291218 5.22817199612624e-05 potassium voltage-gated channel interacting protein 4 FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Modulates KCND2 channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner (PubMed:11847232, PubMed:18957440, PubMed:23576435). Modulates KCND3/Kv4.3 currents (PubMed:23576435). Isoform 4 does not increase KCND2 expression at the cell membrane (PubMed:18957440). Isoform 4 retains KCND3 in the endoplasmic reticulum and negatively regulates its expression at the cell membrane. {ECO:0000250|UniProtKB:Q6PHZ8, ECO:0000269|PubMed:11847232, ECO:0000269|PubMed:18957440, ECO:0000269|PubMed:23576435}.; . TISSUE SPECIFICITY: Predominantly expressed in brain. {ECO:0000269|PubMed:11847232}.; unclassifiable (Anatomical System);frontal lobe;sympathetic chain;kidney;brain;skin;skeletal muscle; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;pons;atrioventricular node;cingulate cortex;skeletal muscle; 0.37064 . -0.339715008 30.06605331 5.58554 0.20809 KCNIP4-IT1 . . . KCNIP4 intronic transcript 1 . . . . . . . . . . . KCNJ1 0.001702478576957 0.704844451848626 0.293453069574417 potassium voltage-gated channel subfamily J member 1 FUNCTION: In the kidney, probably plays a major role in potassium homeostasis. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This channel is activated by internal ATP and can be blocked by external barium.; DISEASE: Bartter syndrome 2 (BS2) [MIM:241200]: An autosomal recessive disorder characterized by impaired salt reabsorption in the thick ascending loop of Henle with pronounced salt wasting, hypokalemic metabolic alkalosis, and varying degrees of hypercalciuria. Bartter syndrome type 2 is a life-threatening condition beginning in utero, with marked fetal polyuria that leads to polyhydramnios and premature delivery. Another hallmark is a marked hypercalciuria and, as a secondary consequence, the development of nephrocalcinosis and osteopenia. {ECO:0000269|PubMed:8841184, ECO:0000269|PubMed:9002665, ECO:0000269|PubMed:9727001}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In the kidney and pancreatic islets. Lower levels in skeletal muscle, pancreas, spleen, brain, heart and liver. {ECO:0000269|PubMed:7635463}.; unclassifiable (Anatomical System);thyroid;liver;kidney;germinal center; superior cervical ganglion;subthalamic nucleus;globus pallidus;kidney;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.10703 0.24116 -0.468351206 23.42533616 109.74629 2.27616 KCNJ2 0.820229027644725 0.178898897355253 0.000872075000021185 potassium voltage-gated channel subfamily J member 2 FUNCTION: Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium or cesium.; DISEASE: Long QT syndrome 7 (LQT7) [MIM:170390]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. Long QT syndrome type 7 manifests itself as a clinical triad consisting of potassium-sensitive periodic paralysis, ventricular ectopy and dysmorphic features. {ECO:0000269|PubMed:11371347, ECO:0000269|PubMed:12148092, ECO:0000269|PubMed:12163457, ECO:0000269|PubMed:16571646, ECO:0000269|PubMed:17324964}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Short QT syndrome 3 (SQT3) [MIM:609622]: A heart disorder characterized by idiopathic persistently and uniformly short QT interval on ECG in the absence of structural heart disease in affected individuals. It causes syncope and sudden death. SQT3 has a unique ECG phenotype characterized by asymmetrical T waves. {ECO:0000269|PubMed:15761194}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Atrial fibrillation, familial, 9 (ATFB9) [MIM:613980]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:15922306}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Heart, brain, placenta, lung, skeletal muscle, and kidney. Diffusely distributed throughout the brain.; unclassifiable (Anatomical System);lymph node;heart;ovary;colon;parathyroid;skin;uterus;whole body;lung;trabecular meshwork;placenta;thyroid;head and neck;cervix;kidney; superior cervical ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.42866 0.22085 -0.582225231 18.44184949 8.98775 0.32999 KCNJ2-AS1 . . . KCNJ2 antisense RNA 1 (head to head) . . . . . . . . . . . KCNJ3 0.989708242851416 0.0102886216896433 3.13545894078938e-06 potassium voltage-gated channel subfamily J member 3 FUNCTION: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat.; . . unclassifiable (Anatomical System);meninges;pia mater;atrium;small intestine;hippocampus;dura mater;kidney;skin;skeletal muscle; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.24361 0.18619 0.014844891 54.94810097 17.96218 0.62770 KCNJ4 0.825953321303081 0.170264058136531 0.00378262056038823 potassium voltage-gated channel subfamily J member 4 FUNCTION: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Heart, skeletal muscle, and several different brain regions including the hippocampus.; unclassifiable (Anatomical System);lung;frontal lobe;hippocampus;testis;brain; amygdala;whole brain;occipital lobe;medulla oblongata;temporal lobe;atrioventricular node;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.20912 . -0.890882376 10.30313753 4.6564 0.16728 KCNJ5 0.309232169469227 0.672733122866547 0.0180347076642252 potassium voltage-gated channel subfamily J member 5 FUNCTION: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external barium.; DISEASE: Familial hyperaldosteronism 3 (FH3) [MIM:613677]: A form of hyperaldosteronism characterized by hypertension secondary to massive adrenal mineralocorticoid production. Like patients with familial hyperaldosteronism type 1 (glucocorticoid-remediable aldosteronism), patients with FH3 present with childhood hypertension, elevated aldosteronism levels, and high levels of the hybrid steroids 18-oxocortisol and 18-hydroxycortisol. However, hypertension and aldosteronism are not reversed by administration of exogenous glucocorticoids and patients require adrenalectomy to control hypertension. {ECO:0000269|PubMed:21311022, ECO:0000269|PubMed:22203740, ECO:0000269|PubMed:22275527, ECO:0000269|PubMed:22308486, ECO:0000269|PubMed:22848660}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Somatic mutations in KCNJ5 have been found in aldosterone-producing adrenal adenomas and can be responsible for aldosteronism associated with cell autonomous proliferation. APAs are typically solitary, well circumscribed tumors diagnosed between ages 30 and 70. They come to medical attention due to new or worsening hypertension, often with hypokalemia. The precise role of KCNJ5 mutations in APA is under debate. They produce increased sodium conductance and cell depolarization, which in adrenal glomerulosa cells produces calcium entry, the signal for aldosterone production and cell proliferation. However, they may not be causative of APA development but may be a consequence of tumorigenesis, playing only a contributory role toward aldosterone overproduction and tumor growth (PubMed:22275527). Somatic mutations in KCNJ5 have not been found in non-aldosterone secreting adrenal adenomas suggesting that they are specifically associated with APA (PubMed:22275527 and PubMed:22848660). {ECO:0000269|PubMed:21311022, ECO:0000269|PubMed:22203740, ECO:0000269|PubMed:22275527, ECO:0000269|PubMed:22848660}.; TISSUE SPECIFICITY: Islets, exocrine pancreas and heart. Expressed in the adrenal cortex, particularly the zona glomerulosa. {ECO:0000269|PubMed:21311022}.; unclassifiable (Anatomical System);pancreas;adrenal cortex; superior cervical ganglion;subthalamic nucleus;adrenal cortex;ciliary ganglion; 0.14572 0.16657 -0.534490515 20.70063694 76.4282 1.83369 KCNJ6 0.812451385393419 0.186569335619315 0.000979278987265473 potassium voltage-gated channel subfamily J member 6 FUNCTION: This potassium channel may be involved in the regulation of insulin secretion by glucose and/or neurotransmitters acting through G-protein-coupled receptors. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium.; . TISSUE SPECIFICITY: Most abundant in cerebellum, and to a lesser degree in islets and exocrine pancreas.; unclassifiable (Anatomical System);lung;islets of Langerhans; superior cervical ganglion;occipital lobe;cerebellum peduncles;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.37660 0.21565 -0.361761279 28.6329323 7.54128 0.27972 KCNJ6-AS1 . . . KCNJ6 antisense RNA 1 . . . . . . . . . . . KCNJ8 0.256769967780786 0.737272856855202 0.00595717536401164 potassium voltage-gated channel subfamily J member 8 FUNCTION: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external barium (By similarity). {ECO:0000250}.; DISEASE: Sudden infant death syndrome (SIDS) [MIM:272120]: SIDS is the sudden death of an infant younger than 1 year that remains unexplained after a thorough case investigation, including performance of a complete autopsy, examination of the death scene, and review of clinical history. Pathophysiologic mechanisms for SIDS may include respiratory dysfunction, cardiac dysrhythmias, cardiorespiratory instability, and inborn errors of metabolism, but definitive pathogenic mechanisms precipitating an infant sudden death remain elusive. {ECO:0000269|PubMed:21836131}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly detected in fetal and adult heart. {ECO:0000269|PubMed:9573340}.; unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;skin;uterus;pancreas;prostate;lung;bone;placenta;thyroid;hippocampus;testis;kidney;brain;stomach; liver; 0.60588 0.20956 0.016664174 55.21939137 143.49708 2.61170 KCNJ9 0.583029242446481 0.406461636623188 0.010509120930331 potassium voltage-gated channel subfamily J member 9 FUNCTION: This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium (By similarity). {ECO:0000250}.; . . . . 0.52569 0.14151 -0.141298762 42.87567823 1625.2607 7.45399 KCNJ10 0.59838882297069 0.392323645072532 0.00928753195677858 potassium voltage-gated channel subfamily J member 10 FUNCTION: May be responsible for potassium buffering action of glial cells in the brain. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity). {ECO:0000250}.; DISEASE: Seizures, sensorineural deafness, ataxia, mental retardation, and electrolyte imbalance (SESAMES) [MIM:612780]: A complex disorder characterized by generalized seizures with onset in infancy, delayed psychomotor development, ataxia, sensorineural hearing loss, hypokalemia, metabolic alkalosis, and hypomagnesemia. {ECO:0000269|PubMed:19289823, ECO:0000269|PubMed:19420365, ECO:0000269|PubMed:22612257}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.18461 0.37501 0.150760231 64.51403633 260.8417 3.46792 KCNJ11 0.314724130416306 0.615339192465476 0.0699366771182174 potassium voltage-gated channel subfamily J member 11 FUNCTION: This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium (By similarity). Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with ABCC9. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation. {ECO:0000250, ECO:0000269|PubMed:17855752, ECO:0000269|PubMed:9831708}.; DISEASE: Familial hyperinsulinemic hypoglycemia 2 (HHF2) [MIM:601820]: Most common cause of persistent hypoglycemia in infancy. Unless early and aggressive intervention is undertaken, brain damage from recurrent episodes of hypoglycemia may occur. {ECO:0000269|PubMed:10204114, ECO:0000269|PubMed:12364426, ECO:0000269|PubMed:15562009, ECO:0000269|PubMed:15579781, ECO:0000269|PubMed:15807877, ECO:0000269|PubMed:15998776, ECO:0000269|PubMed:16332676, ECO:0000269|PubMed:16357843, ECO:0000269|PubMed:18596924, ECO:0000269|PubMed:19357197, ECO:0000269|PubMed:7847376, ECO:0000269|PubMed:8923010}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, permanent neonatal (PNDM) [MIM:606176]: A rare form of diabetes distinct from childhood- onset autoimmune diabetes mellitus type 1. It is characterized by insulin-requiring hyperglycemia that is diagnosed within the first months of life. Permanent neonatal diabetes requires lifelong therapy. {ECO:0000269|PubMed:15115830, ECO:0000269|PubMed:15292329, ECO:0000269|PubMed:15448106, ECO:0000269|PubMed:15448107, ECO:0000269|PubMed:15580558, ECO:0000269|PubMed:16609879, ECO:0000269|PubMed:16731833, ECO:0000269|PubMed:17213273, ECO:0000269|PubMed:17652641, ECO:0000269|PubMed:20022885}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Transient neonatal diabetes mellitus 3 (TNDM3) [MIM:610582]: Neonatal diabetes mellitus, defined as insulin- requiring hyperglycemia within the first month of life, is a rare entity. In about half of the neonates, diabetes is transient and resolves at a median age of 3 months, whereas the rest have a permanent form of diabetes. In a significant number of patients with transient neonatal diabetes mellitus, diabetes type 2 appears later in life. The onset and severity of TNDM3 is variable with childhood-onset diabetes, gestational diabetes or adult-onset diabetes described. {ECO:0000269|PubMed:15718250, ECO:0000269|PubMed:15784703}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in KCNJ11 may contribute to non-insulin- dependent diabetes mellitus (NIDDM), also known as diabetes mellitus type 2.; DISEASE: Maturity-onset diabetes of the young 13 (MODY13) [MIM:616329]: A form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease. {ECO:0000269|PubMed:22701567}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);islets of Langerhans;thyroid;visual apparatus;liver;duodenum;mammary gland; . 0.21623 0.42074 0.242582624 69.45623968 173.55232 2.86874 KCNJ12 1.42518086932541e-05 0.231737761410645 0.768247986780662 potassium voltage-gated channel subfamily J member 12 FUNCTION: Inward rectifying potassium channel that is activated by phosphatidylinositol 4,5-bisphosphate and that probably participates in controlling the resting membrane potential in electrically excitable cells. Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. {ECO:0000269|PubMed:12417321, ECO:0000269|PubMed:20921230, ECO:0000269|PubMed:7859381, ECO:0000269|PubMed:8647284}.; . . unclassifiable (Anatomical System);macula lutea;fovea centralis;kidney;lens;skeletal muscle; occipital lobe;cerebellum peduncles;skeletal muscle;cerebellum; 0.20340 0.17689 1.557965414 95.66525124 10310.05429 22.19442 KCNJ13 0.758052442479994 0.239950849691831 0.00199670782817478 potassium voltage-gated channel subfamily J member 13 FUNCTION: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ13 has a very low single channel conductance, low sensitivity to block by external barium and cesium, and no dependence of its inward rectification properties on the internal blocking particle magnesium.; DISEASE: Snowflake vitreoretinal degeneration (SVD) [MIM:193230]: Developmental and progressive hereditary eye disorder that affects multiple tissues within the eye. Diagnostic features of SVD include fibrillar degeneration of the vitreous humor, early-onset cataract, minute crystalline deposits in the neurosensory retina, and retinal detachment. {ECO:0000269|PubMed:18179896}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leber congenital amaurosis 16 (LCA16) [MIM:614186]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:21763485}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in small intestine. Expression is also detected in stomach, kidney, and all central nervous system regions tested with the exception of spinal cord.; ovary;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;iris;testis;dura mater;unclassifiable (Anatomical System);meninges;heart;adrenal cortex;lens;skeletal muscle;lung;pia mater;placenta;hippocampus;visual apparatus;macula lutea;liver;kidney; . 0.05716 0.12491 -0.161524709 41.6430762 1319.42816 6.83012 KCNJ14 8.51179265459349e-05 0.326662438438291 0.673252443635163 potassium voltage-gated channel subfamily J member 14 FUNCTION: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ14 gives rise to low-conductance channels with a low affinity to the channel blockers Barium and Cesium (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed preferentially in retina. {ECO:0000269|PubMed:10942728}.; ovary;choroid;fovea centralis;lens;retina;prostate;optic nerve;lung;macula lutea;iris;testis;brain;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.26130 0.15096 -0.069700724 48.54328851 105.81155 2.22916 KCNJ15 0.15046203852881 0.777382432652076 0.072155528819114 potassium voltage-gated channel subfamily J member 15 FUNCTION: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium.; . . unclassifiable (Anatomical System);prostate;pancreas;lung;endometrium;bone;thyroid;placenta;spleen;kidney;skeletal muscle; dorsal root ganglion;superior cervical ganglion;thyroid;atrioventricular node;kidney;whole blood;trigeminal ganglion;skeletal muscle; 0.16923 0.14593 0.062575634 58.74026893 515.73712 4.64408 KCNJ16 5.41974671317498e-06 0.430417259693994 0.569577320559293 potassium voltage-gated channel subfamily J member 16 FUNCTION: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ16 may be involved in the regulation of fluid and pH balance.; . TISSUE SPECIFICITY: Highly expressed in kidney, pancreas and thyroid gland.; unclassifiable (Anatomical System);lung;ovary;cochlea;islets of Langerhans;thyroid;placenta;liver;testis;parathyroid;amniotic fluid;kidney;brain;stomach; superior cervical ganglion;thyroid;kidney;fetal thyroid; 0.15212 0.14859 -0.911109353 9.961075725 257.66549 3.45216 KCNJ18 . . . potassium voltage-gated channel subfamily J member 18 FUNCTION: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. {ECO:0000269|PubMed:20074522}.; DISEASE: Thyrotoxic periodic paralysis 2 (TTPP2) [MIM:613239]: A sporadic muscular disorder characterized by episodic weakness and hypokalemia during a thyrotoxic state. It is clinically similar to hereditary hypokalemic periodic paralysis, except for the fact that hyperthyroidism is an absolute requirement for disease manifestation. The disease presents with recurrent episodes of acute muscular weakness of the four extremities that vary in severity from paresis to complete paralysis. Attacks are triggered by ingestion of a high carbohydrate load or strenuous physical activity followed by a period of rest. Thyrotoxic periodic paralysis can occur in association with any cause of hyperthyroidism, but is most commonly associated with Graves disease. {ECO:0000269|PubMed:20074522}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Specifically expressed in skeletal muscle. {ECO:0000269|PubMed:20074522}.; . . . . . . . . KCNK1 0.580150979004335 0.409097022183339 0.0107519988123259 potassium two pore domain channel subfamily K member 1 FUNCTION: Ion channel that contributes to passive transmembrane potassium transport and to the regulation of the resting membrane potential in brain astrocytes, but also in kidney and in other tissues (PubMed:15820677, PubMed:21653227). Forms dimeric channels through which potassium ions pass in accordance with their electrochemical gradient. The channel is selective for K(+) ions at physiological potassium concentrations and at neutral pH, but becomes permeable to Na(+) at subphysiological K(+) levels and upon acidification of the extracellular medium (PubMed:21653227, PubMed:22431633). The homodimer has very low potassium channel activity, when expressed in heterologous systems, and can function as weakly inward rectifying potassium channel (PubMed:8605869, PubMed:8978667, PubMed:15820677, PubMed:21653227, PubMed:22431633, PubMed:23169818, PubMed:25001086). Channel activity is modulated by activation of serotonin receptors (By similarity). Heterodimeric channels containing KCNK1 and KCNK2 have much higher activity, and may represent the predominant form in astrocytes (By similarity). Heterodimeric channels containing KCNK1 and KCNK3 or KCNK9 have much higher activity (PubMed:23169818). Heterodimeric channels formed by KCNK1 and KCNK9 may contribute to halothane- sensitive currents (PubMed:23169818). Mediates outward rectifying potassium currents in dentate gyrus granule cells and contributes to the regulation of their resting membrane potential (By similarity). Contributes to the regulation of action potential firing in dentate gyrus granule cells and down-regulates their intrinsic excitability (By similarity). In astrocytes, the heterodimer formed by KCNK1 and KCNK2 is required for rapid glutamate release in response to activation of G-protein coupled receptors, such as F2R and CNR1 (By similarity). Required for normal ion and water transport in the kidney (By similarity). Contributes to the regulation of the resting membrane potential of pancreatic beta cells (By similarity). The low channel activity of homodimeric KCNK1 may be due to sumoylation (PubMed:15820677, PubMed:20498050, PubMed:23169818). The low channel activity may be due to rapid internalization from the cell membrane and retention in recycling endosomes (PubMed:19959478). {ECO:0000250|UniProtKB:O08581, ECO:0000250|UniProtKB:Q9Z2T2, ECO:0000269|PubMed:15820677, ECO:0000269|PubMed:17693262, ECO:0000269|PubMed:19959478, ECO:0000269|PubMed:20498050, ECO:0000269|PubMed:21653227, ECO:0000269|PubMed:22282804, ECO:0000269|PubMed:22431633, ECO:0000269|PubMed:23169818, ECO:0000269|PubMed:25001086, ECO:0000269|PubMed:8605869, ECO:0000269|PubMed:8978667}.; . TISSUE SPECIFICITY: Detected in bronchial epithelial cells (PubMed:21964404). Detected in heart left atrium and left ventricle (PubMed:17478540). Detected in cardiac myocytes (at protein level) (PubMed:21653227). Widely expressed with high levels in heart, brain and kidney, and lower levels in colon, ovary, placenta, lung and liver (PubMed:8605869, PubMed:9362344). Highly expressed in cerebellum, and detected at lower levels in amygdala, caudate nucleus, brain cortex, hippocampus, putamen, substantia nigra, thalamus, dorsal root ganglion, spinal cord, pituitary, heart, kidney, lung, placenta, pancreas, stomach, small intestine, uterus and prostate (PubMed:11165377). Detected in right and left heart ventricle and atrium, and in heart Purkinje fibers (PubMed:17478540). Detected in bronchial epithelial cells (PubMed:21964404). {ECO:0000269|PubMed:11165377, ECO:0000269|PubMed:17478540, ECO:0000269|PubMed:21653227, ECO:0000269|PubMed:21964404, ECO:0000269|PubMed:8605869, ECO:0000269|PubMed:9362344}.; . . 0.27115 0.14766 -0.271755481 34.31823543 73.06137 1.78485 KCNK2 0.339842885035151 0.657147272523992 0.00300984244085656 potassium two pore domain channel subfamily K member 2 FUNCTION: Ion channel that contributes to passive transmembrane potassium transport (PubMed:23169818). Reversibly converts between a voltage-insensitive potassium leak channel and a voltage- dependent outward rectifying potassium channel in a phosphorylation-dependent manner (PubMed:11319556). In astrocytes, forms mostly heterodimeric potassium channels with KCNK1, with only a minor proportion of functional channels containing homodimeric KCNK2. In astrocytes, the heterodimer formed by KCNK1 and KCNK2 is required for rapid glutamate release in response to activation of G-protein coupled receptors, such as F2R and CNR1 (By similarity). {ECO:0000250|UniProtKB:P97438, ECO:0000269|PubMed:10784345, ECO:0000269|PubMed:11319556, ECO:0000269|PubMed:23169818}.; . TISSUE SPECIFICITY: Isoform 4 is detected in kidney, adrenal gland and brain where it is preferentially expressed in the amygdala but not found in thalamus, hypothalamus, hippocampus or substantia nigra. {ECO:0000269|PubMed:24196565}.; . . 0.12841 . -0.449946534 24.00330267 31.8264 1.00181 KCNK3 . . . potassium two pore domain channel subfamily K member 3 FUNCTION: pH-dependent, voltage-insensitive, background potassium channel protein. Rectification direction results from potassium ion concentration on either side of the membrane. Acts as an outward rectifier when external potassium concentration is low. When external potassium concentration is high, current is inward. {ECO:0000269|PubMed:23169818, ECO:0000269|PubMed:9312005}.; . TISSUE SPECIFICITY: Widespread expression in adult. Strongest expression in pancreas and placenta. Lower expression in brain, lung, prostate, heart, kidney, uterus, small intestine and colon.; unclassifiable (Anatomical System);ovary;islets of Langerhans;parathyroid;skin;uterus;pancreas;lung;endometrium;placenta;visual apparatus;pituitary gland;kidney;brain;pineal gland; adrenal gland;adrenal cortex; 0.22310 0.22973 . . 11.36951 0.41051 KCNK4 0.0424811996004613 0.929460348443949 0.0280584519555899 potassium two pore domain channel subfamily K member 4 FUNCTION: Voltage-insensitive potassium channel (PubMed:22282805). Channel opening is triggered by mechanical forces that deform the membrane (PubMed:22282805, PubMed:25471887, PubMed:25500157). Channel opening is triggered by raising the intracellular pH to basic levels (By similarity). The channel is inactive at 24 degrees Celsius (in vitro); raising the temperature to 37 degrees Celsius increases the frequency of channel opening, with a further increase in channel activity when the temperature is raised to 42 degrees Celsius (By similarity). Plays a role in the perception of pain caused by heat (By similarity). Plays a role in the sensory perception of pain caused by pressure (By similarity). {ECO:0000250|UniProtKB:G3V8V5, ECO:0000250|UniProtKB:O88454, ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:25471887, ECO:0000269|PubMed:25500157}.; . . . . 0.18373 . -0.203796826 38.81811748 1855.22636 7.93980 KCNK5 0.884297675252843 0.11543306490786 0.000269259839296882 potassium two pore domain channel subfamily K member 5 FUNCTION: pH-dependent, voltage insensitive, outwardly rectifying potassium channel. Outward rectification is lost at high external K(+) concentrations.; . TISSUE SPECIFICITY: Abundant expression in kidney, also detected in liver, placenta and small intestine. In the kidney, expression is restricted to the distal tubules and collecting ducts. Not expressed in proximal tubules or glomeruli.; unclassifiable (Anatomical System);cartilage;ovary;colon;blood;skeletal muscle;bone marrow;prostate;lung;epididymis;placenta;spleen;kidney;brain;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.50649 0.11394 7.61E-05 53.98089172 357.00957 4.00345 KCNK6 0.199609234281455 0.755531195422864 0.0448595702956816 potassium two pore domain channel subfamily K member 6 FUNCTION: Exhibits outward rectification in a physiological K(+) gradient and mild inward rectification in symmetrical K(+) conditions.; . TISSUE SPECIFICITY: Widespread expression, detected in all tissues tested except for skeletal muscle. Strongest expression in placenta, pancreas, heart, colon and spleen, lower levels detected in peripheral blood leukocytes, lung, liver, kidney and thymus. Lowest expression detected in brain.; unclassifiable (Anatomical System);uterus;heart;colon;brain;mammary gland;skin;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.23356 0.11987 -0.111973265 45.35857514 1153.23179 6.47083 KCNK7 6.42726120007493e-06 0.15099237336013 0.84900119937867 potassium two pore domain channel subfamily K member 7 FUNCTION: Probable potassium channel subunit. No channel activity observed in vitro as protein remains in the endoplasmic reticulum. May need to associate with an as yet unknown partner in order to reach the plasma membrane.; . . ovary;heart;parathyroid;blood;choroid;fovea centralis;lens;skin;retina;uterus;optic nerve;placenta;macula lutea;brain; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04674 0.09215 0.420771676 77.15852795 245.57417 3.38096 KCNK9 0.126993745644894 0.780156804961039 0.0928494493940668 potassium two pore domain channel subfamily K member 9 FUNCTION: pH-dependent, voltage-insensitive, background potassium channel protein. {ECO:0000269|PubMed:11042359, ECO:0000269|PubMed:11431495, ECO:0000269|PubMed:23169818}.; . TISSUE SPECIFICITY: Mainly found in the cerebellum. Also found in adrenal gland, kidney and lung. {ECO:0000269|PubMed:11042359, ECO:0000269|PubMed:11431495}.; unclassifiable (Anatomical System);brain; dorsal root ganglion;ciliary ganglion;cerebellum; 0.18509 0.12831 -0.383807564 27.41802312 5.61975 0.21065 KCNK10 0.00757969172842383 0.977010077045839 0.0154102312257369 potassium two pore domain channel subfamily K member 10 FUNCTION: Outward rectifying potassium channel. Produces rapidly activating and non-inactivating outward rectifier K(+) currents. Activated by arachidonic acid and other naturally occurring unsaturated free fatty acids.; . TISSUE SPECIFICITY: Abundantly expressed in pancreas and kidney and to a lower level in brain, testis, colon, and small intestine. Isoform b is strongly expressed in kidney (primarily in the proximal tubule) and pancreas, whereas isoform c is abundantly expressed in brain.; lung;hypothalamus;hypopharynx;testis;blood;head and neck;brain;bone marrow; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.54125 0.11207 -0.376526807 28.10804435 644.73304 5.10072 KCNK12 0.671633264361772 0.306973265211388 0.0213934704268403 potassium two pore domain channel subfamily K member 12 FUNCTION: Probable potassium channel subunit. No channel activity observed in heterologous systems. May need to associate with another protein to form a functional channel (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymphoreticular;lymph node;cerebral cortex;islets of Langerhans;placenta;colon;kidney;brain;stomach;tonsil; whole brain;amygdala;dorsal root ganglion;occipital lobe;olfactory bulb;cerebellum peduncles;spinal cord;pons;atrioventricular node;uterus corpus;globus pallidus;ciliary ganglion;cerebellum; 0.41832 0.14201 . . 10.01757 0.36631 KCNK13 0.258007859554083 0.714870965096752 0.0271211753491649 potassium two pore domain channel subfamily K member 13 FUNCTION: Potassium channel displaying weak inward rectification in symmetrical K(+) solution. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;testis;peripheral nerve; superior cervical ganglion;temporal lobe;globus pallidus;atrioventricular node; 0.12640 0.11070 0.553050905 81.54635527 986.81126 6.05493 KCNK15 0.106847941612793 0.775785236213698 0.117366822173509 potassium two pore domain channel subfamily K member 15 FUNCTION: Probable potassium channel subunit. No channel activity observed in heterologous systems. May need to associate with another protein to form a functional channel.; . TISSUE SPECIFICITY: Detected in pancreas, heart, placenta, lung, liver, kidney, ovary, testis, skeletal muscle and adrenal gland, and at lower levels in prostate, spleen and thyroid gland. {ECO:0000269|PubMed:11409881, ECO:0000269|PubMed:11680614}.; . . 0.08954 . 0.637604436 83.77565464 532.76648 4.70860 KCNK15-AS1 . . . KCNK15 antisense RNA 1 (head to head) . . . . . . . . . . . KCNK16 0.0113618650298823 0.842085123619896 0.146553011350221 potassium two pore domain channel subfamily K member 16 FUNCTION: Outward rectifying potassium channel. Produces rapidly activating and non-inactivating outward rectifier K(+) currents.; . TISSUE SPECIFICITY: Highly expressed in pancreas. Not detectable in the other tissues tested. {ECO:0000269|PubMed:12724142}.; . . 0.11229 0.08897 1.107875794 92.03821656 930.18111 5.91747 KCNK17 3.39348404854779e-06 0.345736954891678 0.654259651624273 potassium two pore domain channel subfamily K member 17 FUNCTION: Outward rectifying potassium channel. Produces rapidly activating and non-inactivating outward rectifier K(+) currents.; . . . . 0.12077 0.11244 -0.067881249 48.69072895 177.69987 2.89721 KCNK18 0.000349560661258946 0.603930593926677 0.395719845412064 potassium two pore domain channel subfamily K member 18 FUNCTION: Outward rectifying potassium channel. Produces rapidly activating outward rectifier K(+) currents. May function as background potassium channel that sets the resting membrane potential. Channel activity is directly activated by calcium signal. Activated by the G(q)-protein coupled receptor pathway. The calcium signal robustly activates the channel via calcineurin, whereas the anchoring of 14-3-3/YWHAH interferes with the return of the current to the resting state after activation. Inhibited also by arachidonic acid and other naturally occurring unsaturated free fatty acids. Channel activity is also enhanced by volatile anesthetics, such as isoflurane. Appears to be the primary target of hydroxy-alpha-sanshool, an ingredient of Schezuan pepper. May be involved in the somatosensory function with special respect to pain sensation (By similarity). {ECO:0000250, ECO:0000269|PubMed:12754259, ECO:0000269|PubMed:15562060}.; DISEASE: Migraine with or without aura 13 (MGR13) [MIM:613656]: A form of migraine transmitted in an autosomal dominant pattern. Migraine is a disabling symptom complex of periodic headaches, usually temporal and unilateral. Headaches are often accompanied by irritability, nausea, vomiting and photophobia, preceded by constriction of the cranial arteries. The two major subtypes are common migraine (migraine without aura) and classic migraine (migraine with aura). Classic migraine is characterized by recurrent attacks of reversible neurological symptoms (aura) that precede or accompany the headache. Aura may include a combination of sensory disturbances, such as blurred vision, hallucinations, vertigo, numbness and difficulty in concentrating and speaking. {ECO:0000269|PubMed:20871611}. Note=The disease is caused by mutations affecting the gene represented in this entry. Susceptibility to migraine has been shown to be conferred by a frameshift mutation that segregates with the disorder in a large multigenerational family. Migraine was associated with sensitivity to lights, sounds, and smells, as well as nausea and occasional vomiting. Triggers included fatigue, alcohol and bright lights. Mutations in KCNK18 are a rare cause of migraine.; TISSUE SPECIFICITY: Expressed specifically in dorsal root ganglion and trigeminal ganglion neurons. Detected at low levels in spinal cord. {ECO:0000269|PubMed:12754259, ECO:0000269|PubMed:15562060, ECO:0000269|PubMed:20871611}.; . . 0.20918 0.10825 0.354632714 74.58126917 146.92457 2.64016 KCNMA1 0.999216602851545 0.000783397146474872 1.97981597942242e-12 potassium calcium-activated channel subfamily M alpha 1 FUNCTION: Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca(2+), caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX).; DISEASE: Generalized epilepsy and paroxysmal dyskinesia (GEPD) [MIM:609446]: Epilepsy is one of the most common and debilitating neurological disorders. Paroxysmal dyskinesias are neurological disorders characterized by sudden, unpredictable, disabling attacks of involuntary movement often requiring life-long treatment. The coexistence of epilepsy and paroxysmal dyskinesia in the same individual or family is an increasingly recognized phenomenon. Patients manifest absence seizures, generalized tonic- clonic seizures, paroxysmal nonkinesigenic dyskinesia, involuntary dystonic or choreiform movements. Onset is usually in childhood and patients may have seizures only, dyskinesia only, or both. {ECO:0000269|PubMed:15937479}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Except in myocytes, it is almost ubiquitously expressed. {ECO:0000269|PubMed:11880513}.; salivary gland;colon;skin;uterus;prostate;optic nerve;cochlea;oesophagus;endometrium;bone;testis;germinal center;spinal ganglion;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;skeletal muscle;lung;liver;hypopharynx;head and neck;kidney;stomach; uterus;dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;uterus corpus;appendix;ciliary ganglion;atrioventricular node;cingulate cortex;skin; 0.76173 0.14035 -1.682848699 2.653927813 154.36657 2.71502 KCNMA1-AS1 . . . KCNMA1 antisense RNA 1 . . . . . . . . . . . KCNMA1-AS2 . . . KCNMA1 antisense RNA 2 . . . . . . . . . . . KCNMA1-AS3 . . . KCNMA1 antisense RNA 3 . . . . . . . . . . . KCNMB1 2.07038513299084e-05 0.281040585062264 0.718938711086406 potassium calcium-activated channel subfamily M regulatory beta subunit 1 FUNCTION: Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Increases the apparent Ca(2+)/voltage sensitivity of the KCNMA1 channel. It also modifies KCNMA1 channel kinetics and alters its pharmacological properties. It slows down the activation and the deactivation kinetics of the channel. Acts as a negative regulator of smooth muscle contraction by enhancing the calcium sensitivity to KCNMA1. Its presence is also a requirement for internal binding of the KCNMA1 channel opener dehydrosoyasaponin I (DHS-1) triterpene glycoside and for external binding of the agonist hormone 17-beta-estradiol (E2). Increases the binding activity of charybdotoxin (CTX) toxin to KCNMA1 peptide blocker by increasing the CTX association rate and decreasing the dissociation rate.; . TISSUE SPECIFICITY: Abundantly expressed in smooth muscle. Low levels of expression in most other tissues. Within the brain, relatively high levels found in hippocampus and corpus callosum.; unclassifiable (Anatomical System);smooth muscle;heart;colon;choroid;skin;uterus;prostate;whole body;lung;cerebral cortex;endometrium;bone;liver;testis;spleen;kidney;mammary gland;aorta; dorsal root ganglion;uterus;uterus corpus;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12091 0.13585 0.350995466 74.37485256 1645.74354 7.49745 KCNMB2 0.652459629699188 0.341682324879316 0.005858045421496 potassium calcium-activated channel subfamily M regulatory beta subunit 2 FUNCTION: Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Acts as a negative regulator that confers rapid and complete inactivation of KCNMA1 channel complex. May participate in KCNMA1 inactivation in chromaffin cells of the adrenal gland or in hippocampal CA1 neurons. {ECO:0000269|PubMed:10097176, ECO:0000269|PubMed:10377337}.; . TISSUE SPECIFICITY: Expressed in kidney, heart and brain. Highly expressed in ovary. Expressed at low level in other tissues. {ECO:0000269|PubMed:10097176, ECO:0000269|PubMed:10377337, ECO:0000269|PubMed:10692449}.; unclassifiable (Anatomical System);lung;islets of Langerhans;testis;kidney;brain; superior cervical ganglion;ciliary ganglion; 0.44038 0.12971 -0.185391282 39.67916962 13.27793 0.48237 KCNMB2-AS1 . . . KCNMB2 antisense RNA 1 . . . . . . . . . . . KCNMB3 2.57857245438483e-08 0.0438570775029935 0.956142896711282 potassium calcium-activated channel subfamily M regulatory beta subunit 3 FUNCTION: Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Alters the functional properties of the current expressed by the KCNMA1 channel. Isoform 2, isoform 3 and isoform 4 partially inactivate the current of KCNBMA. Isoform 4 induces a fast and incomplete inactivation of KCNMA1 channel that is detectable only at large depolarizations. In contrast, isoform 1 does not induce detectable inactivation of KCNMA1. Two or more subunits of KCNMB3 are required to block the KCNMA1 tetramer. {ECO:0000269|PubMed:10766764, ECO:0000269|PubMed:10864947}.; . TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 4 are widely expressed. Isoform 2 is expressed placenta, pancreas, kidney and heart. Isoform 1 and isoform 3 are highly expressed in pancreas and testis. {ECO:0000269|PubMed:10585773, ECO:0000269|PubMed:10692449, ECO:0000269|PubMed:10766764}.; unclassifiable (Anatomical System);uterus;lung;heart;placenta;visual apparatus;colon;testis;cervix;kidney;germinal center;skin; . 0.01150 0.06859 1.771210783 96.79169615 5060.61879 14.56904 KCNMB3P1 . . . potassium calcium-activated channel subfamily M regulatory beta subunit 3 pseudogene 1 . . . . . . . . . . . KCNMB4 0.829402296381292 0.167010280369296 0.00358742324941193 potassium calcium-activated channel subfamily M regulatory beta subunit 4 FUNCTION: Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Decreases the gating kinetics and calcium sensitivity of the KCNMA1 channel, but with fast deactivation kinetics. May decrease KCNMA1 channel openings at low calcium concentrations but increases channel openings at high calcium concentrations. Makes KCNMA1 channel resistant to 100 nM charybdotoxin (CTX) toxin concentrations. {ECO:0000269|PubMed:10692449, ECO:0000269|PubMed:10792058, ECO:0000269|PubMed:10828459}.; . TISSUE SPECIFICITY: Predominantly expressed in brain. In brain, it is expressed in the cerebellum, cerebral cortex, medulla, spinal cord, occipital pole, frontal lobe, temporal lobe, putamen, amygdala, caudate nucleus, corpus callosum, hippocampus, substantia nigra and thalamus. Weakly or not expressed in other tissues. {ECO:0000269|PubMed:10692449, ECO:0000269|PubMed:10828459}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;hypothalamus;pharynx;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;kidney;aorta; dorsal root ganglion;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex;cerebellum; 0.16613 0.12971 -0.031067188 51.03798066 6.88289 0.25611 KCNN1 0.931699633359926 0.0682309614078675 6.94052322059842e-05 potassium calcium-activated channel subfamily N member 1 FUNCTION: Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);visual apparatus;brain;stomach; amygdala;subthalamic nucleus;cingulate cortex; 0.12583 0.12237 . . 40.84763 1.19627 KCNN2 0.971048688574044 0.0289432128230798 8.09860287570867e-06 potassium calcium-activated channel subfamily N member 2 FUNCTION: Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.; . TISSUE SPECIFICITY: Expressed in atrial myocytes (at protein level). Widely expressed. {ECO:0000269|PubMed:13679367}.; unclassifiable (Anatomical System);uterus;prostate;lung;whole body;frontal lobe;heart;kidney;brain;skin; adrenal gland;spinal cord;trigeminal ganglion; 0.84883 0.12158 -0.846787714 11.05803255 28.20395 0.90392 KCNN3 0.864940881345047 0.135042441076715 1.66775782383611e-05 potassium calcium-activated channel subfamily N member 3 FUNCTION: Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.; . . unclassifiable (Anatomical System);prostate;lymph node;frontal lobe;tongue;islets of Langerhans;muscle;colon;blood;head and neck;kidney;germinal center;brain; . 0.20013 0.15553 -0.558357437 19.54470394 419.64938 4.27942 KCNN4 8.36465970463448e-06 0.756144231941342 0.243847403398954 potassium calcium-activated channel subfamily N member 4 FUNCTION: Forms a voltage-independent potassium channel that is activated by intracellular calcium (PubMed:26148990). Activation is followed by membrane hyperpolarization which promotes calcium influx. Required for maximal calcium influx and proliferation during the reactivation of naive T-cells. The channel is blocked by clotrimazole and charybdotoxin but is insensitive to apamin (PubMed:17157250, PubMed:18796614). {ECO:0000269|PubMed:17157250, ECO:0000269|PubMed:18796614, ECO:0000269|PubMed:26148990}.; DISEASE: Dehydrated hereditary stomatocytosis with or without pseudohyperkalemia and/or perinatal edema (DHS) [MIM:194380]: An autosomal dominant hemolytic anemia characterized by primary erythrocyte dehydration. DHS erythrocytes exhibit decreased total cation and potassium content that are not accompanied by a proportional net gain of sodium and water. DHS patients typically exhibit mild to moderate compensated hemolytic anemia, with an increased erythrocyte mean corpuscular hemoglobin concentration and a decreased osmotic fragility, both of which reflect cellular dehydration. Patients may also show perinatal edema and pseudohyperkalemia due to loss of potassium from red cells stored at room temperature. A minor proportion of red cells appear as stomatocytes on blood films. Complications such as splenomegaly and cholelithiasis, resulting from increased red cell trapping in the spleen and elevated bilirubin levels, respectively, may occur. The course of DHS is frequently associated with iron overload, which may lead to hepatosiderosis. {ECO:0000269|PubMed:26148990, ECO:0000269|PubMed:26178367, ECO:0000269|PubMed:26198474}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed in non-excitable tissues.; unclassifiable (Anatomical System);cartilage;ovary;lacrimal gland;developmental;colon;parathyroid;blood;skin;bone marrow;pancreas;prostate;optic nerve;lung;endometrium;bone;placenta;visual apparatus;liver;testis;spleen;germinal center;brain;mammary gland;stomach; trachea;placenta;ciliary ganglion; 0.16815 . -0.115612493 45.12856806 55.22576 1.49123 KCNQ1 2.45298673885324e-05 0.980167926851294 0.0198075432813177 potassium voltage-gated channel subfamily Q member 1 FUNCTION: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity) (PubMed:10646604). Associates with KCNE beta subunits that modulates current kinetics (By similarity) (PubMed:9312006, PubMed:9108097, PubMed:8900283, PubMed:10646604, PubMed:11101505, PubMed:19687231). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity) (PubMed:9312006, PubMed:9108097, PubMed:8900283, PubMed:10646604, PubMed:11101505). Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta- adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity) (PubMed:9312006, PubMed:9108097, PubMed:8900283, PubMed:10646604, PubMed:11101505). Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (PubMed:10713961). When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (PubMed:10646604). This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents (By similarity). During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP-induced jejunal chloride ions secretion (By similarity). Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion (By similarity). When associated with KCNE2, forms an heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (PubMed:11101505). When associated with KCNE4, inhibits voltage-gated potassium channel activity (PubMed:19687231). When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (PubMed:12324418). Also forms an heterotetramer with KCNQ5; has a voltage-gated potassium channel activity (PubMed:24855057). Binds with phosphatidylinositol 4,5- bisphosphate (PubMed:25037568). {ECO:0000250|UniProtKB:P97414, ECO:0000250|UniProtKB:Q9Z0N7, ECO:0000269|PubMed:10646604, ECO:0000269|PubMed:10713961, ECO:0000269|PubMed:11101505, ECO:0000269|PubMed:12324418, ECO:0000269|PubMed:19687231, ECO:0000269|PubMed:24855057, ECO:0000269|PubMed:25037568, ECO:0000269|PubMed:8900283, ECO:0000269|PubMed:9108097, ECO:0000269|PubMed:9312006}.; DISEASE: Long QT syndrome 1 (LQT1) [MIM:192500]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. {ECO:0000269|PubMed:10024302, ECO:0000269|PubMed:10220144, ECO:0000269|PubMed:10220146, ECO:0000269|PubMed:10367071, ECO:0000269|PubMed:10409658, ECO:0000269|PubMed:10482963, ECO:0000269|PubMed:10728423, ECO:0000269|PubMed:10973849, ECO:0000269|PubMed:11799244, ECO:0000269|PubMed:12442276, ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:16414944, ECO:0000269|PubMed:16922724, ECO:0000269|PubMed:18165683, ECO:0000269|PubMed:18400097, ECO:0000269|PubMed:19540844, ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:21241800, ECO:0000269|PubMed:24184248, ECO:0000269|PubMed:24269949, ECO:0000269|PubMed:24713462, ECO:0000269|PubMed:25037568, ECO:0000269|PubMed:25139741, ECO:0000269|PubMed:25705178, ECO:0000269|PubMed:8528244, ECO:0000269|PubMed:8818942, ECO:0000269|PubMed:8872472, ECO:0000269|PubMed:9024139, ECO:0000269|PubMed:9272155, ECO:0000269|PubMed:9302275, ECO:0000269|PubMed:9312006, ECO:0000269|PubMed:9323054, ECO:0000269|PubMed:9386136, ECO:0000269|PubMed:9482580, ECO:0000269|PubMed:9570196, ECO:0000269|PubMed:9641694, ECO:0000269|PubMed:9693036, ECO:0000269|PubMed:9702906, ECO:0000269|PubMed:9799083, ECO:0000269|PubMed:9927399, ECO:0000269|Ref.31}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Jervell and Lange-Nielsen syndrome 1 (JLNS1) [MIM:220400]: An autosomal recessive disorder characterized by congenital deafness, prolongation of the QT interval, syncopal attacks due to ventricular arrhythmias, and a high risk of sudden death. {ECO:0000269|PubMed:10090886, ECO:0000269|PubMed:10728423, ECO:0000269|PubMed:18400097, ECO:0000269|PubMed:18441444, ECO:0000269|PubMed:25705178, ECO:0000269|PubMed:9781056}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Atrial fibrillation, familial, 3 (ATFB3) [MIM:607554]: An autosomal dominant form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:12522251}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Short QT syndrome 2 (SQT2) [MIM:609621]: A heart disorder characterized by idiopathic persistently and uniformly short QT interval on ECG in the absence of structural heart disease in affected individuals. It causes syncope and sudden death. {ECO:0000269|PubMed:15159330}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:18711366, ECO:0000269|PubMed:18711367, ECO:0000269|PubMed:24390345}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Abundantly expressed in heart, pancreas, prostate, kidney, small intestine and peripheral blood leukocytes. Less abundant in placenta, lung, spleen, colon, thymus, testis and ovaries.; unclassifiable (Anatomical System);smooth muscle;heart;ovary;epidermis;colon;parathyroid;blood;skin;bone marrow;uterus;pancreas;prostate;lung;adrenal gland;thyroid;placenta;liver;testis;kidney;brain;mammary gland;stomach; pancreas;superior cervical ganglion;adrenal gland;thyroid;adrenal cortex;fetal thyroid;skeletal muscle; 0.32219 0.33671 -0.685180376 15.32200991 131.10283 2.49419 KCNQ1-AS1 . . . KCNQ1 antisense RNA 1 . . . . . . . . . . . KCNQ1DN . . . KCNQ1 downstream neighbor (non-protein coding) . . TISSUE SPECIFICITY: Shows reduced expression in Wilms' tumor samples. {ECO:0000269|PubMed:11056398}.; . . . . . . . . KCNQ1OT1 . . . KCNQ1 opposite strand/antisense transcript 1 (non-protein coding) . . . . . . . . . . . KCNQ2 0.99935609863785 0.000643900629781664 7.32368580232038e-10 potassium voltage-gated channel subfamily Q member 2 FUNCTION: Probably important in the regulation of neuronal excitability. Associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. KCNQ2/KCNQ3 current is blocked by linopirdine and XE991, and activated by the anticonvulsant retigabine. Muscarinic agonist oxotremorine-M strongly suppress KCNQ2/KCNQ3 current in cells in which cloned KCNQ2/KCNQ3 channels were coexpressed with M1 muscarinic receptors.; DISEASE: Seizures, benign familial neonatal 1 (BFNS1) [MIM:121200]: A disorder characterized by clusters of seizures occurring in the first days of life. Most patients have spontaneous remission by 12 months of age and show normal psychomotor development. Some rare cases manifest an atypical severe phenotype associated with epileptic encephalopathy and psychomotor retardation. The disorder is distinguished from benign familial infantile seizures by an earlier age at onset. In some patients, neonatal convulsions are followed later in life by myokymia, a benign condition characterized by spontaneous involuntary contractions of skeletal muscles fiber groups that can be observed as vermiform movement of the overlying skin. Electromyography typically shows continuous motor unit activity with spontaneous oligo- and multiplet-discharges of high intraburst frequency (myokymic discharges). Some patients may have isolated myokymia. {ECO:0000269|PubMed:11175290, ECO:0000269|PubMed:11572947, ECO:0000269|PubMed:14534157, ECO:0000269|PubMed:15249611, ECO:0000269|PubMed:9425895}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epileptic encephalopathy, early infantile, 7 (EIEE7) [MIM:613720]: An autosomal dominant seizure disorder characterized by infantile onset of refractory seizures with resultant delayed neurologic development and persistent neurologic abnormalities. {ECO:0000269|PubMed:12742592, ECO:0000269|PubMed:15249611}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In adult and fetal brain. Highly expressed in areas containing neuronal cell bodies, low in spinal chord and corpus callosum. Isoform 2 is preferentially expressed in differentiated neurons. Isoform 6 is prominent in fetal brain, undifferentiated neuroblastoma cells and brain tumors. {ECO:0000269|PubMed:10781098}.; unclassifiable (Anatomical System);lung;frontal lobe;islets of Langerhans;macula lutea;hippocampus;visual apparatus;duodenum;testis;fovea centralis;mammary gland;brain;retina; amygdala;superior cervical ganglion;cerebellum peduncles;hypothalamus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;fetal brain;testis - seminiferous tubule;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.49147 0.15128 -0.666770504 15.86459071 224.48708 3.24057 KCNQ3 0.985604293672352 0.0143956943441109 1.19835369881747e-08 potassium voltage-gated channel subfamily Q member 3 FUNCTION: Probably important in the regulation of neuronal excitability. Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs.; DISEASE: Seizures, benign familial neonatal 2 (BFNS2) [MIM:121201]: A disorder characterized by clusters of seizures occurring in the first days of life. Most patients have spontaneous remission by 12 months of age and show normal psychomotor development. The disorder is distinguished from benign familial infantile seizures by an earlier age at onset. {ECO:0000269|PubMed:10852552, ECO:0000269|PubMed:14534157, ECO:0000269|PubMed:9425900}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in KCNQ3 may be involved in epileptic disorders. These are characterized by paroxysmal transient disturbances of the electrical activity of the brain that may be manifested as episodic impairment or loss of consciousness, abnormal motor phenomena, psychic or sensory disturbances, or perturbation of the autonomic nervous system. {ECO:0000269|PubMed:22612257}.; TISSUE SPECIFICITY: Predominantly expressed in brain.; . . 0.77144 0.10905 -0.33061537 30.82094834 526.70339 4.68437 KCNQ4 0.985178281898531 0.0148214036876789 3.14413790434247e-07 potassium voltage-gated channel subfamily Q member 4 FUNCTION: Probably important in the regulation of neuronal excitability. May underlie a potassium current involved in regulating the excitability of sensory cells of the cochlea. KCNQ4 channels are blocked by linopirdin, XE991 and bepridil, whereas clofilium is without significant effect. Muscarinic agonist oxotremorine-M strongly suppress KCNQ4 current in CHO cells in which cloned KCNQ4 channels were coexpressed with M1 muscarinic receptors.; DISEASE: Deafness, autosomal dominant, 2A (DFNA2A) [MIM:600101]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:10025409, ECO:0000269|PubMed:10369879, ECO:0000269|PubMed:10571947, ECO:0000269|PubMed:10925378, ECO:0000269|PubMed:21242547}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the outer, but not the inner, sensory hair cells of the cochlea. Slightly expressed in heart, brain and skeletal muscle.; lymphoreticular;cartilage;colon;fovea centralis;choroid;lens;retina;optic nerve;epididymis;placenta;macula lutea;iris;mammary gland;brain;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12943 0.14391 -0.66859065 15.76433121 646.02 5.10359 KCNQ5 0.99953508656607 0.000464913420370416 1.3560026397726e-11 potassium voltage-gated channel subfamily Q member 5 FUNCTION: Probably important in the regulation of neuronal excitability. Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current. Insensitive to tetraethylammonium, but inhibited by barium, linopirdine and XE991. Activated by niflumic acid and the anticonvulsant retigabine. Muscarine suppresses KCNQ5 current in Xenopus oocytes in which cloned KCNQ5 channels were coexpressed with M(1) muscarinic receptors.; . TISSUE SPECIFICITY: Strongly expressed in brain and skeletal muscle. In brain, expressed in cerebral cortex, occipital pole, frontal lobe and temporal lobe. Lower levels in hippocampus and putamen. Low to undetectable levels in medulla, cerebellum and thalamus.; unclassifiable (Anatomical System);frontal lobe;thyroid;testis; dorsal root ganglion;superior cervical ganglion; 0.10905 0.11812 -0.732911333 14.07761264 200.0252 3.05539 KCNQ5-AS1 . . . KCNQ5 antisense RNA 1 . . . . . . . . . . . KCNQ5-IT1 . . . KCNQ5 intronic transcript 1 . . . . . . . . . . . KCNRG 0.00052028933781877 0.452516142378234 0.546963568283947 potassium channel regulator FUNCTION: Inhibits potassium fluxes in cells. May regulate Kv1 family channel proteins by retaining a fraction of channels in endomembranes. {ECO:0000269|PubMed:12650944, ECO:0000269|PubMed:19968958}.; . TISSUE SPECIFICITY: Ubiquitous in normal tissues and expressed in some tumor tissues. {ECO:0000269|PubMed:12650944}.; unclassifiable (Anatomical System);lung;lymph node;heart;ovary;endometrium;nasopharynx;testis;spleen;germinal center; . 0.11348 0.09449 0.349177632 74.18023119 38.82943 1.15002 KCNS1 0.362998541245244 0.625024884341753 0.0119765744130036 potassium voltage-gated channel modifier subfamily S member 1 FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage- gated potassium channel activation and deactivation rates of KCNB1 and KCNB2 (PubMed:10484328). {ECO:0000269|PubMed:10484328}.; . TISSUE SPECIFICITY: Detected in all tissues tested with the exception of skeletal muscle. Highly expressed in adult and fetal brain, fetal kidney and lung, and adult prostate and testis (PubMed:10484328). {ECO:0000269|PubMed:10484328}.; unclassifiable (Anatomical System);breast;uterus;frontal lobe;brain;skin; dorsal root ganglion;superior cervical ganglion;occipital lobe;medulla oblongata;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.07998 0.10975 . . 198.42651 3.04418 KCNS2 0.528896630632781 0.455178338494422 0.015925030872797 potassium voltage-gated channel modifier subfamily S member 2 FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage- gated potassium channel activation and deactivation rates of KCNB1 and KCNB2. {ECO:0000250|UniProtKB:O35174}.; . . unclassifiable (Anatomical System);lung;testis;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.31144 0.11207 -0.005381972 53.50908233 27.67414 0.88972 KCNS3 0.0160901263314807 0.883854636252446 0.100055237416073 potassium voltage-gated channel modifier subfamily S member 3 FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 (PubMed:10484328). Heterotetrameric channel activity formed with KCNB1 show increased current amplitude with the threshold for action potential activation shifted towards more negative values in hypoxic-treated pulmonary artery smooth muscle cells (By similarity). {ECO:0000250|UniProtKB:O88759, ECO:0000269|PubMed:10484328}.; . TISSUE SPECIFICITY: Detected in whole normal term placental and placental chorionic plate arteries and veins. Detected in syncytiotrophoblast and in blood vessel endothelium within intermediate villi and chorionic plate (at protein level) (PubMed:22943705). Detected in most tissues, but not in peripheral blood lymphocytes. The highest levels of expression are in lung (PubMed:10484328). {ECO:0000269|PubMed:10484328, ECO:0000269|PubMed:22943705}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;lens;skin;skeletal muscle;bile duct;uterus;lung;placenta;bone;visual apparatus;testis;spleen;kidney;brain;mammary gland;stomach; trigeminal ganglion; 0.65450 0.13782 0.444637294 77.91342298 220.59919 3.21164 KCNT1 0.00534873818795492 0.994649439299045 1.82251299989033e-06 potassium sodium-activated channel subfamily T member 1 FUNCTION: Outwardly rectifying potassium channel subunit that may coassemble with other Slo-type channel subunits. Activated by high intracellular sodium or chloride levels. Activated upon stimulation of G-protein coupled receptors, such as CHRM1 and GRIA1. May be regulated by calcium in the absence of sodium ions (in vitro) (By similarity). {ECO:0000250}.; DISEASE: Epileptic encephalopathy, early infantile, 14 (EIEE14) [MIM:614959]: A rare epileptic encephalopathy of infancy that combines pharmacoresistant seizures with developmental delay. This severe neurologic disorder is characterized by onset in the first 6 months of life of refractory focal seizures and arrest of psychomotor development. Ictal EEG shows discharges that arise randomly from various areas of both hemispheres and migrate from one brain region to another. {ECO:0000269|PubMed:23086397}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epilepsy, nocturnal frontal lobe, 5 (ENFL5) [MIM:615005]: An autosomal dominant focal epilepsy syndrome characterized by childhood onset of clusters of motor seizures during sleep. Some patients may develop behavioral or psychiatric manifestations and/or intellectual disability. The phenotype is more severe than observed in other genetic forms of nocturnal frontal lobe epilepsy. {ECO:0000269|PubMed:23086396}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest expression in liver, brain and spinal cord. Lowest expression in skeletal muscle. {ECO:0000269|PubMed:10718198}.; unclassifiable (Anatomical System);frontal lobe;testis;brain; . 0.10242 0.10521 -2.070835943 1.615947157 121.99362 2.40558 KCNT2 0.666802213991112 0.33319778539441 6.14478262493799e-10 potassium sodium-activated channel subfamily T member 2 FUNCTION: Outward rectifying potassium channel. Produces rapidly activating outward rectifier K(+) currents. Activated by high intracellular sodium and chloride levels. Channel activity is inhibited by ATP and by inhalation anesthetics, such as isoflurane (By similarity). Inhibited upon stimulation of G-protein coupled receptors, such as CHRM1 and GRIA1. {ECO:0000250, ECO:0000269|PubMed:14684870, ECO:0000269|PubMed:16687497}.; . . unclassifiable (Anatomical System);uterus;urinary;head and neck;kidney;brain;skeletal muscle; superior cervical ganglion;ciliary ganglion;pons; 0.56836 0.14357 -1.285933373 5.083746167 67.33123 1.69863 KCNU1 3.90823831937045e-12 0.978110281173249 0.0218897188228426 potassium calcium-activated channel subfamily U member 1 FUNCTION: Testis-specific potassium channel activated by both intracellular pH and membrane voltage that mediates export of K(+). May represent the primary spermatozoan K(+) current. In contrast to KCNMA1/SLO1, it is not activated by Ca(2+) or Mg(2+). Critical for fertility. May play an important role in sperm osmoregulation required for the acquisition of normal morphology and motility when faced with osmotic challenges, such as those experienced after mixing with seminal fluid and entry into the vagina. {ECO:0000269|PubMed:23129643}.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:9452476}.; . . . . -0.74406331 13.77683416 4629.08786 13.69118 KCNV1 0.778125704329582 0.220312271263713 0.00156202440670443 potassium voltage-gated channel modifier subfamily V member 1 FUNCTION: Potassium channel subunit that does not form functional channels by itself. Modulates KCNB1 and KCNB2 channel activity by shifting the threshold for inactivation to more negative values and by slowing the rate of inactivation. Can down-regulate the channel activity of KCNB1, KCNB2, KCNC4 and KCND1, possibly by trapping them in intracellular membranes. {ECO:0000269|PubMed:8670833, ECO:0000269|PubMed:9079713}.; . TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:12383276}.; unclassifiable (Anatomical System);amygdala;frontal lobe;hippocampus;brain; whole brain;amygdala;occipital lobe;prefrontal cortex;ciliary ganglion;cingulate cortex;parietal lobe;skeletal muscle; 0.51648 0.11262 -0.383807564 27.41802312 9.55845 0.35208 KCNV2 6.27109599144588e-17 0.000136850260745309 0.999863149739255 potassium voltage-gated channel modifier subfamily V member 2 FUNCTION: Potassium channel subunit. Modulates channel activity by shifting the threshold and the half-maximal activation to more negative values.; DISEASE: Cone dystrophy retinal 3B (RCD3B) [MIM:610356]: A rare form of cone dystrophy associated with supernormal rod responses. The disorder is characterized by reduced visual acuity, photoaversion, night blindness, and abnormal color vision. At an early age, the retina shows subtle depigmentation at the macula and, later, more obvious areas of atrophy. {ECO:0000269|PubMed:16909397}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in lung, liver, kidney, pancreas, spleen, thymus, prostate, testis, ovary and colon. {ECO:0000269|PubMed:12060745}.; . . 0.45075 0.12232 -0.837696902 11.45317292 768.96656 5.48914 KCP . . . kielin/chordin-like protein FUNCTION: Enhances bone morphogenetic protein (BMP) signaling in a paracrine manner. In contrast, it inhibits both the activin-A and TGFB1-mediated signaling pathways (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);pancreas;liver;kidney;skeletal muscle;cerebellum; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion; 0.10294 0.09762 . . . . KCTD1 0.934855730655081 0.0648427525640101 0.00030151678090867 potassium channel tetramerization domain containing 1 FUNCTION: May repress the transcriptional activity of AP-2 family members, including TFAP2A, TFAP2B and TFAP2C to various extent. {ECO:0000269|PubMed:18358072, ECO:0000269|PubMed:19115315}.; DISEASE: Scalp-ear-nipple syndrome (SENS) [MIM:181270]: A disease characterized by aplasia cutis congenita of the scalp, breast anomalies that range from hypothelia or athelia to amastia, and minor anomalies of the external ears. Less frequent clinical characteristics include nail dystrophy, dental anomalies, cutaneous syndactyly of the digits, and renal malformations. Penetrance appears to be high, although there is substantial variable expressivity within families. {ECO:0000269|PubMed:23541344}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in mammary gland, kidney, brain and ovary. {ECO:0000269|PubMed:18358072}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;endometrium;cerebral cortex;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;pancreas;lung;placenta;macula lutea;hippocampus;cervix;head and neck;kidney;mammary gland; amygdala;whole brain;medulla oblongata;subthalamic nucleus;occipital lobe;placenta;temporal lobe;prefrontal cortex;caudate nucleus;cingulate cortex;parietal lobe; 0.20055 0.11262 -0.405853867 26.23260203 261.92903 3.47336 KCTD2 0.0618999883050334 0.869453034720015 0.0686469769749516 potassium channel tetramerization domain containing 2 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pineal body;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;cerebellum; amygdala;whole brain;occipital lobe;cerebellum peduncles;prefrontal cortex;globus pallidus;testis;parietal lobe;cingulate cortex;cerebellum; 0.33043 0.10278 -0.361761279 28.6329323 2020.42022 8.27133 KCTD3 0.986866111092156 0.0131338869721498 1.93569396267884e-09 potassium channel tetramerization domain containing 3 . . TISSUE SPECIFICITY: Broadly expressed in normal tissues. {ECO:0000269|PubMed:10508479}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;thyroid;testis;middle ear;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;internal ear;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion; 0.51587 0.13949 -0.66859065 15.76433121 1901.50476 8.02069 KCTD4 0.0407045021423859 0.843047462190182 0.116248035667432 potassium channel tetramerization domain containing 4 . . . . . 0.23864 0.11262 -0.163345027 41.24793583 20.73489 0.70354 KCTD5 0.544871003960432 0.452092171993972 0.00303682404559655 potassium channel tetramerization domain containing 5 FUNCTION: Its interaction with CUL3 suggests that it may act as a substrate adapter in some E3 ligase complex. Does not affect the function of Kv channel Kv2.1/KCNB1, Kv1.2/KCNA2, Kv4.2/KCND2 and Kv3.4/KCNC4.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;bone;iris;testis;germinal center;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala; 0.25465 0.11262 -0.075159878 47.78839349 79.11446 1.87760 KCTD6 0.206951627204982 0.751066682091846 0.0419816907031718 potassium channel tetramerization domain containing 6 . . . colon;choroid;fovea centralis;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;iris;germinal center;brain;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;lens;bile duct;lung;hippocampus;macula lutea;liver;cervix;spleen;head and neck; whole brain;amygdala;cerebellum peduncles;cingulate cortex;cerebellum; 0.36543 0.09933 -0.053113545 49.38664779 2.28818 0.07729 KCTD7 0.496529665997915 0.503285825882055 0.000184508120030639 potassium channel tetramerization domain containing 7 FUNCTION: May be involved in the control of excitability of cortical neurons. {ECO:0000250}.; DISEASE: Epilepsy, progressive myoclonic 3, with or without intracellular inclusions (EPM3) [MIM:611726]: An autosomal recessive, severe, progressive myoclonic epilepsy with early onset. Multifocal myoclonic seizures begin between 16 and 24 months of age after normal initial development. Neurodegeneration and regression occur with seizure onset. Other features include mental retardation, dysarthria, truncal ataxia, and loss of fine finger movements. EEG shows slow dysrhythmia, multifocal and occasionally generalized epileptiform discharges. In some patients, ultrastructural findings on skin biopsies identify intracellular accumulation of autofluorescent lipopigment storage material, consistent with neuronal ceroid lipofuscinosis. {ECO:0000269|PubMed:17455289, ECO:0000269|PubMed:22606975, ECO:0000269|PubMed:22612257, ECO:0000269|PubMed:22693283, ECO:0000269|PubMed:22748208}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in KCTD7 are a cause of opsoclonus-myoclonus ataxia-like syndrome. Opsoclonus myoclonus ataxia syndrome (OMS) is a rare pervasive and frequently permanent disorder that usually develops in previously healthy children with normal premorbid psychomotor development and characterized by association of abnormal eye movements (opsoclonus), severe dyskinesia (myoclonus), cerebellar ataxia, functional regression, and behavioral problems. The syndrome is considered to be an immune- mediated disorder and may be tumor-associated or idiopathic. OMS is one of a few steroid responsive disorders of childhood. KCTD7 mutations have been found in a patient with an atypical clinical presentation characterized by non-epileptic myoclonus and ataxia commencing in early infancy, abnormal opsoclonus-like eye movements, improvement of clinical symptoms under steroid treatment, and subsequent development of generalized epilepsy (PubMed:22638565). {ECO:0000269|PubMed:22638565}.; . unclassifiable (Anatomical System);lymph node;ovary;hypothalamus;salivary gland;pharynx;colon;parathyroid;blood;skeletal muscle;bone marrow;breast;prostate;pancreas;whole body;lung;placenta;visual apparatus;liver;testis;germinal center;kidney;brain;bladder; superior cervical ganglion; 0.26482 . -0.648365105 16.35999056 42.56405 1.23535 KCTD8 0.291159282160617 0.688067477648101 0.0207732401912821 potassium channel tetramerization domain containing 8 FUNCTION: Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; . 0.43100 . -0.427900189 25.14744043 254.31464 3.43009 KCTD9 0.0733968308677995 0.926083873128874 0.000519296003326082 potassium channel tetramerization domain containing 9 . . . ovary;sympathetic chain;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;testis;brain;artery;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;hypopharynx;head and neck;cervix;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.10831 0.11262 -0.117432389 44.89266336 12.22101 0.44285 KCTD9P1 . . . potassium channel tetramerization domain containing 9 pseudogene 1 . . . . . . . . . . . KCTD9P2 . . . potassium channel tetramerization domain containing 9 pseudogene 2 . . . . . 0.13926 . . . . . KCTD9P3 . . . potassium channel tetramerization domain containing 9 pseudogene 3 . . . . . . . . . . . KCTD9P4 . . . potassium channel tetramerization domain containing 9 pseudogene 4 . . . . . . . . . . . KCTD9P5 . . . potassium channel tetramerization domain containing 9 pseudogene 5 . . . . . . . . . . . KCTD9P6 . . . potassium channel tetramerization domain containing 9 pseudogene 6 . . . . . . . . . . . KCTD10 0.17266981342374 0.813929908256683 0.0134002783195772 potassium channel tetramerization domain containing 10 FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. The BCR(BACURD3) E3 ubiquitin ligase complex mediates the ubiquitination of target proteins, leading to their degradation by the proteasome (By similarity). {ECO:0000250}.; . . myocardium;smooth muscle;ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;urinary;adrenal cortex;blood;lens;breast;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.31336 0.12378 -0.161524709 41.6430762 51.83226 1.42198 KCTD10P1 . . . potassium channel tetramerization domain containing 10 pseudogene 1 . . . . . . . . . . . KCTD11 0.447451322334745 0.524016154346848 0.0285325233184066 potassium channel tetramerization domain containing 11 FUNCTION: Plays a role as a marker and a regulator of neuronal differentiation; Up-regulated by a variety of neurogenic signals, such as retinoic acid, epidermal growth factor/EGF and NGFB/nerve growth factor. Induces apoptosis, growth arrest and the expression of cyclin-dependent kinase inhibitor CDKN1B. Plays a role as a tumor repressor and inhibits cell growth and tumorigenicity of medulloblastoma (MDB). Acts as an E3 ubiquitin-protein ligase towards HDAC1, leading to its proteasomal degradation. Functions as antagonist of the Hedgehog pathway on cell proliferation and differentiation by affecting the nuclear transfer of transcrition factor GLI1, thus maintaining cerebellar granule cells in undifferentiated state, this effect probably occurs via HDAC1 down-regulation, keeping GLI1 acetylated and inactive. When knock- down, Hedgehog antagonism is impaired and proliferation of granule cells is sustained. Activates the caspase cascade. {ECO:0000269|PubMed:15249678, ECO:0000269|PubMed:20081843, ECO:0000269|PubMed:21237243}.; . TISSUE SPECIFICITY: Higher expression in cerebellum than in whole brain and lower expression in medulloblastoma. {ECO:0000269|PubMed:15249678}.; unclassifiable (Anatomical System);heart;cartilage;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;pancreas;prostate;optic nerve;lung;cerebral cortex;endometrium;larynx;placenta;macula lutea;visual apparatus;head and neck;cervix;stomach; . 0.14624 0.10369 0.281220278 71.07808445 140.10669 2.58182 KCTD12 0.353531089443336 0.592495524190055 0.0539733863666092 potassium channel tetramerization domain containing 12 FUNCTION: Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Present in a variety of fetal organs, with highest expression levels in the cochlea and brain and, in stark contrast, is detected only at extremely low levels in adult organs, such as brain and lung. {ECO:0000269|PubMed:15357420}.; ovary;sympathetic chain;parathyroid;skin;retina;bone marrow;uterus;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;artery;pineal gland;unclassifiable (Anatomical System);amygdala;cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;blood;skeletal muscle;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.77608 0.12904 . . 23.60982 0.78285 KCTD13 0.79196093357248 0.206734676790167 0.00130438963735298 potassium channel tetramerization domain containing 13 FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in regulation of cytoskeleton structure. The BCR(BACURD1) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. {ECO:0000269|PubMed:19782033}.; . TISSUE SPECIFICITY: Expressed in a wide variety of tissues. {ECO:0000269|PubMed:11593007}.; colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;lens;breast;lung;placenta;hippocampus;macula lutea;kidney;cerebellum; whole brain;amygdala;superior cervical ganglion;occipital lobe;testis - interstitial;medulla oblongata;hypothalamus;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;cingulate cortex;cerebellum; 0.38266 0.08839 -0.339715008 30.06605331 12.10685 0.43891 KCTD14 0.00289299266628188 0.578482843689675 0.418624163644043 potassium channel tetramerization domain containing 14 . . . unclassifiable (Anatomical System);ovary;colon;retina;uterus;pancreas;prostate;whole body;lung;frontal lobe;endometrium;adrenal gland;larynx;bone;placenta;liver;testis;cervix;head and neck;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;pancreas;trachea;adrenal gland;cerebellum peduncles;liver;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.59245 . -0.314027422 31.9297004 346.75457 3.94908 KCTD15 0.130646194089883 0.780197334158339 0.089156471751778 potassium channel tetramerization domain containing 15 FUNCTION: During embryonic development, interferes with neural crest formation (By similarity). Inhibits AP2 transcriptional activity by interaction with its activation domain. {ECO:0000250, ECO:0000269|PubMed:23382213}.; . . unclassifiable (Anatomical System);lymph node;heart;ovary;islets of Langerhans;parathyroid;blood;lens;skin;skeletal muscle;retina;bone marrow;uterus;whole body;lung;placenta;visual apparatus;duodenum;testis;amniotic fluid;kidney;brain;mammary gland;stomach; superior cervical ganglion; 0.17041 0.12378 -0.427900189 25.14744043 22.17006 0.74394 KCTD16 0.959972607609424 0.0399382459277256 8.91464628502841e-05 potassium channel tetramerization domain containing 16 FUNCTION: Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization (By similarity). {ECO:0000250}.; . . . . 0.69249 . -0.069700724 48.54328851 61.06619 1.59065 KCTD17 0.0511169926059515 0.860718465491884 0.0881645419021647 potassium channel tetramerization domain containing 17 FUNCTION: Is a positive regulator of ciliogenesis, playing a crucial role in the initial steps of axoneme extension. It acts as a substrate-adapter for CUL3-RING ubiquitin ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of TCHP, a protein involved in ciliogenesis down-regulation (PubMed:25270598). May be involved in endoplasmic reticulum calcium ion homeostasis (PubMed:25983243). {ECO:0000269|PubMed:25270598, ECO:0000269|PubMed:25983243}.; . TISSUE SPECIFICITY: Highly expressed in brain. Highest expression is observed in the putamen and the thalamus. {ECO:0000269|PubMed:25983243}.; . . 0.12828 0.10832 0.082802743 60.09082331 544.15613 4.74685 KCTD18 0.000526111235034034 0.886183067373792 0.113290821391174 potassium channel tetramerization domain containing 18 . . . unclassifiable (Anatomical System);lymph node;heart;hypothalamus;colon;skin;retina;uterus;prostate;whole body;lung;frontal lobe;endometrium;nasopharynx;bone;thyroid;placenta;visual apparatus;hippocampus;liver;testis;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.22561 . 0.621009802 83.41589998 721.00753 5.33094 KCTD19 3.3389213065673e-08 0.982185723594779 0.017814243016008 potassium channel tetramerization domain containing 19 . . . unclassifiable (Anatomical System);hippocampus;testis; superior cervical ganglion;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.21126 . -0.416983034 25.82566643 706.10469 5.27896 KCTD20 0.399321757575798 0.598774686242636 0.00190355618156635 potassium channel tetramerization domain containing 20 FUNCTION: Promotes the phosphorylation of AKT family members. {ECO:0000250|UniProtKB:Q8CDD8}.; . . smooth muscle;salivary gland;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.10327 0.10439 -0.047654689 50.22410946 3868.93239 12.25745 KCTD21 0.29110859643231 0.627005060523901 0.0818863430437893 potassium channel tetramerization domain containing 21 . . . cartilage;ovary;hypothalamus;colon;parathyroid;blood;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;epididymis;thyroid;placenta;macula lutea;visual apparatus;hypopharynx;head and neck;cervix;brain;mammary gland;stomach; . 0.24297 0.11053 -0.538132194 20.26421326 31.67802 0.99706 KCTD21-AS1 . . . KCTD21 antisense RNA 1 . . . . . . . . . . . KDELC1 6.41764150689518e-06 0.892032262402843 0.10796131995565 KDEL motif containing 1 . . . . . 0.13538 0.09760 -0.091746757 46.91554612 4102.6627 12.70963 KDELC1P1 . . . KDEL motif containing 1 pseudogene 1 . . . . . . . . . . . KDELC2 1.57001885647098e-08 0.215914290981715 0.784085693318097 KDEL motif containing 2 . . . ovary;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach; ciliary ganglion;atrioventricular node; 0.15767 . 0.639420866 83.8995046 231.88434 3.29002 KDELR1 0.895487511877841 0.103510386738376 0.00100210138378258 KDEL endoplasmic reticulum protein retention receptor 1 FUNCTION: Required for the retention of luminal endoplasmic reticulum resident proteins via vesicular recycling. This receptor recognizes the C-terminal K-D-E-L motif. COPI-coated transport intermediates, either in the form of round vesicles or as tubular processes, mediate retrograde traffic of the KDEL receptor-ligand complexes. Also required for normal vesicular traffic through the Golgi. {ECO:0000269|PubMed:11703931}.; . . myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;tongue;urinary;pharynx;blood;lens;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; superior cervical ganglion; 0.11920 0.15080 -0.09720619 46.20193442 21.40603 0.72185 KDELR2 0.268728640616792 0.706420464781011 0.0248508946021967 KDEL endoplasmic reticulum protein retention receptor 2 FUNCTION: Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi. This receptor recognizes K-D-E-L.; . . medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; . 0.23673 0.12378 -0.383807564 27.41802312 9.23152 0.33814 KDELR3 2.25894610398846e-06 0.156657572285194 0.843340168768702 KDEL endoplasmic reticulum protein retention receptor 3 FUNCTION: Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi. This receptor recognizes K-D-E-L (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;ganglion;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;pineal body;urinary;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;smooth muscle;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.17303 0.09908 0.749657564 86.56522765 2529.74041 9.37985 KDF1 . . . keratinocyte differentiation factor 1 FUNCTION: Plays a role in the regulation of the epidermis formation during early development. Required both as an inhibitor of basal cell proliferation and a promoter of differentiation of basal progenitor cell progeny (By similarity). {ECO:0000250}.; . . . . 0.66147 . -0.066061882 48.77919321 . . KDM1A 0.991027964686515 0.00897203455302426 7.60461263406558e-10 lysine demethylase 1A FUNCTION: Histone demethylase that demethylates both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in ANDR-containing complexes, which mediates phosphorylation of 'Thr- 6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Effector of SNAI1-mediated transcription repression of E- cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7. {ECO:0000269|PubMed:12032298, ECO:0000269|PubMed:15620353, ECO:0000269|PubMed:16079795, ECO:0000269|PubMed:17805299, ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:20562920}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:16079795}.; ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;oesophagus;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;stomach;thymus; testis - interstitial;fetal brain;testis - seminiferous tubule;tumor;globus pallidus;testis; 0.41775 0.21102 -0.427900189 25.14744043 22.58422 0.75581 KDM1B 0.815087936736707 0.18491046442949 1.59883380341228e-06 lysine demethylase 1B FUNCTION: Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri- methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys- 36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4 (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);colon;skin;retina;uterus;breast;whole body;lung;frontal lobe;synovium;thyroid;duodenum;liver;testis;cervix;germinal center;brain;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.18554 0.12299 7.61E-05 53.98089172 389.96856 4.15858 KDM2A 0.999999954603642 4.53963582786952e-08 2.78719730777045e-19 lysine demethylase 2A FUNCTION: Histone demethylase that specifically demethylates 'Lys- 36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys- 36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis. {ECO:0000269|PubMed:16362057, ECO:0000269|PubMed:19001877}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in brain, testis and ovary, followed by lung. {ECO:0000269|PubMed:10231032}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;vein;uterus;oesophagus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;aorta; testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion;cerebellum; 0.41698 0.10384 -1.199555187 5.761972163 20.89045 0.70720 KDM2B 0.999785914187162 0.000214085812753871 8.39340211096639e-14 lysine demethylase 2B FUNCTION: Histone demethylase that demethylates 'Lys-4' and 'Lys- 36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' and dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. Preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. May also serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000269|PubMed:16362057, ECO:0000269|PubMed:17994099}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;blood;lens;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;stomach; medulla oblongata;superior cervical ganglion;ciliary ganglion;atrioventricular node;cerebellum; 0.38170 0.10945 -2.166248113 1.421325784 100.32428 2.17057 KDM3A 0.981756840004812 0.018243159987909 7.27860344466665e-12 lysine demethylase 3A FUNCTION: Histone demethylase that specifically demethylates 'Lys- 9' of histone H3, thereby playing a central role in histone code. Preferentially demethylates mono- and dimethylated H3 'Lys-9' residue, with a preference for dimethylated residue, while it has weak or no activity on trimethylated H3 'Lys-9'. Demethylation of Lys residue generates formaldehyde and succinate. Involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes, resulting in H3 'Lys-9' demethylation and transcriptional activation. Involved in spermatogenesis by regulating expression of target genes such as PRM1 and TMP1 which are required for packaging and condensation of sperm chromatin. Involved in obesity resistance through regulation of metabolic genes such as PPARA and UCP1. {ECO:0000269|PubMed:16603237}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.38273 0.11164 -0.725642751 14.24274593 545.1225 4.74884 KDM3B 0.999999999078234 9.21766233829003e-10 2.10266632308583e-23 lysine demethylase 3B FUNCTION: Histone demethylase that specifically demethylates 'Lys- 9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May have tumor suppressor activity. {ECO:0000269|PubMed:16603237}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in placenta, skeletal muscle, kidney, heart and liver. {ECO:0000269|PubMed:11087669, ECO:0000269|PubMed:11687974}.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex;skeletal muscle;cerebellum; 0.45381 0.09818 -0.749505784 13.74144845 603.13711 4.97115 KDM4A 0.999993865120135 6.13487986332268e-06 1.76840561478466e-15 lysine demethylase 4A FUNCTION: Histone demethylase that specifically demethylates 'Lys- 9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15927959}.; . . 0.18092 0.10689 -0.020150552 52.25288983 135.04266 2.52863 KDM4A-AS1 . . . KDM4A antisense RNA 1 . . . . . . . . . . . KDM4B 0.999934757141383 6.52428558467669e-05 2.76986412413416e-12 lysine demethylase 4B FUNCTION: Histone demethylase that specifically demethylates 'Lys- 9' of histone H3, thereby playing a role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Only able to demethylate trimethylated H3 'Lys-9', with a weaker activity than KDM4A, KDM4C and KDM4D. Demethylation of Lys residue generates formaldehyde and succinate. {ECO:0000269|PubMed:16603238}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);heart;epidermis;islets of Langerhans;muscle;adrenal cortex;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;cerebellum;thymus; dorsal root ganglion;amygdala;superior cervical ganglion;atrioventricular node;fetal thyroid;skeletal muscle;prostate;fetal brain;thyroid;placenta;prefrontal cortex;liver;ciliary ganglion;whole blood; 0.43365 0.11421 -2.565119811 0.837461665 40.68188 1.19189 KDM4C 0.000758734602622751 0.999235107356564 6.15804081338881e-06 lysine demethylase 4C FUNCTION: Histone demethylase that specifically demethylates 'Lys- 9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. {ECO:0000269|PubMed:16603238}.; . TISSUE SPECIFICITY: Overexpressed in several esophageal squamous cell carcinomas (ESCs). {ECO:0000269|PubMed:10987278}.; . . 0.70659 . -0.343575389 29.62373201 5314.03953 15.06707 KDM4D 0.149201646842992 0.833296545353516 0.0175018078034919 lysine demethylase 4D FUNCTION: Histone demethylase that specifically demethylates 'Lys- 9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys- 9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. {ECO:0000269|PubMed:16603238}.; . . unclassifiable (Anatomical System);heart;ovary;cartilage;parathyroid;skin;uterus;lung;placenta;thyroid;bone;testis;head and neck;brain; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;skeletal muscle; 0.20105 0.10132 0.64123826 83.97617363 307.94685 3.73504 KDM4E 0.764772097616784 0.233385171489315 0.0018427308939003 lysine demethylase 4E FUNCTION: Histone demethylase that specifically demethylates 'Lys- 9' of histone H3, thereby playing a central role in histone code. {ECO:0000269|PubMed:21914792}.; . . . . . . 2.192062755 98.10096721 536.33724 4.72175 KDM5A 0.999994827471308 5.17252869190073e-06 3.95854187154173e-19 lysine demethylase 5A FUNCTION: Histone demethylase that specifically demethylates 'Lys- 4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. May stimulate transcription mediated by nuclear receptors. May be involved in transcriptional regulation of Hox proteins during cell differentiation. May participate in transcriptional repression of cytokines such as CXCL12. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. In a histone demethylase-independent manner, acts as a coactivator of the CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2 and other clock-controlled genes and increases histone acetylation at PER1/2 promoters by inhibiting the activity of HDAC1 (By similarity). {ECO:0000250|UniProtKB:Q3UXZ9, ECO:0000269|PubMed:11358960, ECO:0000269|PubMed:15949438, ECO:0000269|PubMed:17320160, ECO:0000269|PubMed:17320161, ECO:0000269|PubMed:17320163}.; . . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;peripheral nerve; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;testis;white blood cells;fetal thyroid;whole blood;trigeminal ganglion; 0.60365 0.16050 -0.742251371 13.78862939 3460.15028 11.30856 KDM5B 5.09420142344633e-05 0.999949057816228 1.69537978640811e-10 lysine demethylase 5B FUNCTION: Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2 (By similarity). {ECO:0000250|UniProtKB:Q80Y84, ECO:0000269|PubMed:12657635, ECO:0000269|PubMed:16645588, ECO:0000269|PubMed:17320161, ECO:0000269|PubMed:17363312}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in testis. Down-regulated in melanoma and glioblastoma. Up-regulated in breast cancer (at protein level). {ECO:0000269|PubMed:10336460, ECO:0000269|PubMed:10616211, ECO:0000269|PubMed:10878660, ECO:0000269|PubMed:12237901, ECO:0000269|PubMed:15803180}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node; 0.69271 0.12823 -1.721531029 2.476999292 245.24685 3.37951 KDM5C 0.997842569241018 0.00215743064335851 1.15623558541791e-10 lysine demethylase 5C FUNCTION: Histone demethylase that specifically demethylates 'Lys- 4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Participates in transcriptional repression of neuronal genes by recruiting histone deacetylases and REST at neuron-restrictive silencer elements. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2 (By similarity). {ECO:0000250|UniProtKB:P41230, ECO:0000269|PubMed:17320160, ECO:0000269|PubMed:17320161, ECO:0000269|PubMed:17468742}.; DISEASE: Mental retardation, X-linked, syndromic, Claes-Jensen type (MRXSCJ) [MIM:300534]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXSCJ patients manifest mental retardation associated with variable features such as slowly progressive spastic paraplegia, seizures, facial dysmorphism. {ECO:0000269|PubMed:15586325, ECO:0000269|PubMed:16538222, ECO:0000269|PubMed:16541399, ECO:0000269|PubMed:23356856, ECO:0000269|PubMed:25666439}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues examined. Highest levels found in brain and skeletal muscle. {ECO:0000269|PubMed:15586325}.; smooth muscle;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;prostate;optic nerve;frontal lobe;larynx;synovium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;blood;lens;breast;adrenal gland;placenta;macula lutea;liver;head and neck;kidney;stomach;thymus; superior cervical ganglion;cerebellum peduncles;pons;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex;cerebellum; 0.23488 0.19342 -1.50825116 3.503184713 16.80604 0.59116 KDM5C-IT1 . . . KDM5C intronic transcript 1 . . . . . . . . . . . KDM5D 0.0151340441544138 0.877511526697815 0.107354429147771 lysine demethylase 5D FUNCTION: Histone demethylase that specifically demethylates 'Lys- 4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. May play a role in spermatogenesis. {ECO:0000269|PubMed:17320160, ECO:0000269|PubMed:17320162, ECO:0000269|PubMed:17351630}.; . . smooth muscle;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;prostate;optic nerve;frontal lobe;larynx;synovium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;blood;lens;breast;adrenal gland;placenta;macula lutea;liver;head and neck;kidney;stomach;thymus; . 0.22310 . . . 40.95228 1.19978 KDM5DP1 . . . lysine demethylase 5D pseudogene 1 . . . . . . . . . . . KDM6A 0.999987120523081 1.28794769079343e-05 1.07683082927076e-14 lysine demethylase 6A FUNCTION: Histone demethylase that specifically demethylates 'Lys- 27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Demethylation of 'Lys-27' of histone H3 is concomitant with methylation of 'Lys-4' of histone H3, and regulates the recruitment of the PRC1 complex and monoubiquitination of histone H2A. {ECO:0000269|PubMed:17761849, ECO:0000269|PubMed:17851529}.; DISEASE: Kabuki syndrome 2 (KABUK2) [MIM:300867]: A congenital mental retardation syndrome with additional features, including postnatal dwarfism, a peculiar facies characterized by long palpebral fissures with eversion of the lateral third of the lower eyelids, a broad and depressed nasal tip, large prominent earlobes, a cleft or high-arched palate, scoliosis, short fifth finger, persistence of fingerpads, radiographic abnormalities of the vertebrae, hands, and hip joints, and recurrent otitis media in infancy. {ECO:0000269|PubMed:22197486}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);heart;blood;lens;skeletal muscle;bile duct;breast;lung;adrenal gland;placenta;macula lutea;liver;spleen;mammary gland;stomach;aorta;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.98270 0.16837 -0.066061882 48.77919321 855.17792 5.70917 KDM6B 0.999994424921105 5.5750788942643e-06 2.83433950286005e-16 lysine demethylase 6B FUNCTION: Histone demethylase that specifically demethylates 'Lys- 27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Involved in inflammatory response by participating in macrophage differentiation in case of inflammation by regulating gene expression and macrophage differentiation. {ECO:0000269|PubMed:17825402, ECO:0000269|PubMed:17851529}.; . . myocardium;ovary;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;larynx;bone;testis;amniotic fluid;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;adrenal cortex;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis;ciliary ganglion;pons;atrioventricular node;whole blood;trigeminal ganglion;parietal lobe;skin;skeletal muscle; 0.20577 0.12653 -1.31556435 4.794762916 5734.22375 15.68691 KDM7A . . . lysine demethylase 7A FUNCTION: Histone demethylase required for brain development. Specifically demethylates dimethylated 'Lys-9' and 'Lys-27' (H3K9me2 and H3K27me2, respectively) of histone H3 and monomethylated histone H4 'Lys-20' residue (H4K20Me1), thereby playing a central role in histone code. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: in presence of H3K4me3, it has no demethylase activity toward H3K9me2, while it has high activity toward H3K27me2. Demethylates H3K9me2 in absence of H3K4me3. Has activity toward H4K20Me1 only when nucleosome is used as a substrate and when not histone octamer is used as substrate. {ECO:0000269|PubMed:20023638, ECO:0000269|PubMed:20194436, ECO:0000269|PubMed:20622853}.; . . . . 0.17354 0.09363 -0.176292081 40.56381222 138.33384 2.56055 KDM8 0.00726458481834173 0.976382066198515 0.0163533489831433 lysine demethylase 8 FUNCTION: Histone demethylase required for G2/M phase cell cycle progression. Specifically demethylates dimethylated 'Lys-36' (H3K36me2) of histone H3, an epigenetic repressive mark, thereby acting as a transcription activator. Regulates expression of CCNA1 (cyclin-A1), leading to regulate cancer cell proliferation. {ECO:0000269|PubMed:20457893}.; . TISSUE SPECIFICITY: Weakly expressed in most cells. Highly expressed in breast cancer cells. {ECO:0000269|PubMed:20457893}.; . . 0.08044 0.10501 -0.600630256 18.06440198 59.39799 1.56319 KDR 0.984488111789506 0.0155118882056108 4.88367877140077e-12 kinase insert domain receptor FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC. {ECO:0000269|PubMed:10102632, ECO:0000269|PubMed:10368301, ECO:0000269|PubMed:10600473, ECO:0000269|PubMed:11387210, ECO:0000269|PubMed:12649282, ECO:0000269|PubMed:1417831, ECO:0000269|PubMed:15026417, ECO:0000269|PubMed:15215251, ECO:0000269|PubMed:15962004, ECO:0000269|PubMed:16966330, ECO:0000269|PubMed:17303569, ECO:0000269|PubMed:18529047, ECO:0000269|PubMed:19668192, ECO:0000269|PubMed:19834490, ECO:0000269|PubMed:20080685, ECO:0000269|PubMed:20224550, ECO:0000269|PubMed:20705758, ECO:0000269|PubMed:21893193, ECO:0000269|PubMed:7929439, ECO:0000269|PubMed:9160888, ECO:0000269|PubMed:9804796, ECO:0000269|PubMed:9837777}.; DISEASE: Hemangioma, capillary infantile (HCI) [MIM:602089]: A condition characterized by dull red, firm, dome-shaped hemangiomas, sharply demarcated from surrounding skin, usually presenting at birth or occurring within the first two or three months of life. They result from highly proliferative, localized growth of capillary endothelium and generally undergo regression and involution without scarring. {ECO:0000269|PubMed:11807987, ECO:0000269|PubMed:18931684}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=Plays a major role in tumor angiogenesis. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.; TISSUE SPECIFICITY: Detected in cornea (at protein level). Widely expressed. {ECO:0000269|PubMed:19668192}.; colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;whole body;frontal lobe;cochlea;larynx;thyroid;bone;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;spinal cord;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; placenta;ciliary ganglion; 0.44385 0.13110 -1.139149039 6.393017221 2242.88737 8.73853 KDSR 0.472000395094808 0.526903054770297 0.00109655013489468 3-ketodihydrosphingosine reductase FUNCTION: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).; . TISSUE SPECIFICITY: Expressed in all tissues examined. Highest expression in placenta. High expression in lung, kidney, stomach and small intestine, low expression in heart, spleen and skeletal muscle. Weakly expressed in normal hematopoietic tissues. Higher expression in some T-cell malignancies and PHA-stimulated lymphocytes.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;trabecular meshwork;placenta;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;olfactory bulb;atrioventricular node; 0.71762 0.14417 -0.141298762 42.87567823 15.79709 0.56276 KEAP1 0.251629057539983 0.748110763621969 0.000260178838047378 kelch like ECH associated protein 1 FUNCTION: Acts as a substrate adapter protein for the E3 ubiquitin ligase complex formed by CUL3 and RBX1 and targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression. Retains NFE2L2/NRF2 and may also retain BPTF in the cytosol. Targets PGAM5 for ubiquitination and degradation by the proteasome. {ECO:0000269|PubMed:14585973, ECO:0000269|PubMed:15379550, ECO:0000269|PubMed:15572695, ECO:0000269|PubMed:15983046, ECO:0000269|PubMed:17046835}.; . TISSUE SPECIFICITY: Broadly expressed, with highest levels in skeletal muscle. {ECO:0000269|PubMed:15379550}.; lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; cerebellum; 0.23809 0.20935 -1.133409319 6.434300543 28.06422 0.90037 KEL 2.00929288413252e-16 0.0955724777724088 0.904427522227591 Kell blood group, metallo-endopeptidase FUNCTION: Zinc endopeptidase with endothelin-3-converting enzyme activity. Cleaves EDN1, EDN2 and EDN3, with a marked preference for EDN3. {ECO:0000269|PubMed:10438732}.; . TISSUE SPECIFICITY: Expressed at high levels in erythrocytes and testis (in Sertoli cells), and, at lower levels, in skeletal muscle, tonsils (in follicular dendritic cells), lymph node, spleen and appendix (at protein level). Also expressed in many adult and fetal nonerythroid tissues, including brain, spleen, lymph nodes and bone marrow. {ECO:0000269|PubMed:10891471, ECO:0000269|PubMed:11336649}.; unclassifiable (Anatomical System);breast;medulla oblongata;lung;bone;liver;alveolus;testis;spleen;skin; fetal liver;testis;ciliary ganglion; 0.24267 0.21794 -1.434847051 3.998584572 945.48608 5.95668 KERA 0.000414369553245371 0.641085840977118 0.358499789469637 keratocan FUNCTION: May be important in developing and maintaining corneal transparency and for the structure of the stromal matrix.; DISEASE: The autosomal recessive cornea plana 2 (CNA2) [MIM:217300]: In CNA2, the forward convex curvature is flattened, leading to a decrease in refraction, reduced visual activity, extreme hyperopia (usually plus 10 d or more), hazy corneal limbus, opacities in the corneal parenchyma, and marked arcus senilis (often detected at an early age). CNA2 is a rare disorder with a worldwide distribution, but a high prevalence in the Finnish population. {ECO:0000269|PubMed:10802664, ECO:0000269|PubMed:11726611}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Cornea. Increased expression in the stroma of keratoconus corneas. Also detected in trachea, and in low levels, in intestine, skeletal muscle, ovary, lung and putamen. {ECO:0000269|PubMed:11683372}.; unclassifiable (Anatomical System);lung;whole body;placenta;visual apparatus;testis; superior cervical ganglion;atrioventricular node;pons;skeletal muscle; 0.09885 0.26492 -0.448125345 24.19202642 41.66536 1.21386 KFM . . . Klippel-Feil malformation . . . . . . . . . . . KHDC1 6.80134798473891e-05 0.491467139933873 0.508464846586279 KH homology domain containing 1 . . . unclassifiable (Anatomical System);prostate;lung;kidney;brain; . 0.09427 . 0.038710339 56.92380278 694.65301 5.25432 KHDC1L 0.013352848445668 0.664292227007298 0.322354924547034 KH homology domain containing 1-like . . . . . . . 0.523736627 80.45529606 16.86354 0.59345 KHDC1P1 . . . KH homology domain containing 1 pseudogene 1 . . . . . . . . . . . KHDC3L 0.24120460893701 0.727607612149077 0.0311877789139127 KH domain containing 3 like, subcortical maternal complex member . DISEASE: Hydatidiform mole, recurrent, 2 (HYDM2) [MIM:614293]: A disorder characterized by excessive trophoblast development that produces a growing mass of tissue inside the uterus at the beginning of a pregnancy. It leads to abnormal pregnancies with no embryo, and cystic degeneration of the chorionic villi. {ECO:0000269|PubMed:21885028}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expression appears to be maximal in germinal vesicle oocytes, it tails off through metaphase II oocytes and is undetectable following the completion of the oocyte to embryo transition. {ECO:0000269|PubMed:21885028}.; . . 0.09220 0.08455 -0.005381972 53.50908233 522.85498 4.66613 KHDRBS1 0.94687645920226 0.0530867429628478 3.67978348919147e-05 KH domain containing, RNA binding, signal transduction associated 1 FUNCTION: Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain- containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to (PubMed:22253824). {ECO:0000269|PubMed:22253824}.; . TISSUE SPECIFICITY: Ubiquitously expressed in all tissue examined. Isoform 1 is expressed at lower levels in brain, skeletal muscle, and liver whereas isoform 3 is intensified in skeletal muscle and in liver. {ECO:0000269|PubMed:9013542}.; medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; amygdala;superior cervical ganglion;testis - seminiferous tubule;cerebellum peduncles;testis;cerebellum; 0.80327 0.08538 -0.251530012 35.42108988 14.61198 0.52651 KHDRBS2 0.142878302250928 0.85313087030216 0.00399082744691275 KH domain containing, RNA binding, signal transduction associated 2 FUNCTION: RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Its phosphorylation by FYN inhibits its ability to regulate splice site selection. Induces an increased concentration-dependent incorporation of exon in CD44 pre-mRNA by direct binding to purine-rich exonic enhancer. May function as an adapter protein for Src kinases during mitosis. Binds both poly(A) and poly(U) homopolymers. Phosphorylation by PTK6 inhibits its RNA-binding ability (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in brain, lung, kidney and small intestine. Weakly expressed in placenta, liver, spleen, thymus, ovary and colon. {ECO:0000269|PubMed:12549823}.; unclassifiable (Anatomical System);hypothalamus;brain; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin; 0.84596 0.10633 -0.091746757 46.91554612 113.59711 2.32140 KHDRBS3 0.868289437076458 0.131633546116515 7.70168070261876e-05 KH domain containing, RNA binding, signal transduction associated 3 FUNCTION: RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. May play a role as a negative regulator of cell growth. Inhibits cell proliferation. Involved in splice site selection of vascular endothelial growth factor. Induces an increased concentration-dependent incorporation of exon in CD44 pre-mRNA by direct binding to purine-rich exonic enhancer. RNA- binding abilities are down-regulated by tyrosine kinase PTK6. Involved in post-transcriptional regulation of HIV-1 gene expression. Binds preferentially to the 5'-[AU]UAAA-3' motif in vitro. {ECO:0000269|PubMed:10564820, ECO:0000269|PubMed:11741900, ECO:0000269|PubMed:15901763}.; . TISSUE SPECIFICITY: Ubiquitous with higher expression in testis, skeletal muscle and brain. Expressed in the kidney only in podocytes, the glomerular epithelial cells of the kidney. Strongly expressed after meiosis. {ECO:0000269|PubMed:10077576, ECO:0000269|PubMed:10332027, ECO:0000269|PubMed:10564820}.; medulla oblongata;ovary;salivary gland;intestine;colon;skin;retina;uterus;prostate;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);trophoblast;heart;hypothalamus;pharynx;blood;skeletal muscle;lung;cornea;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach; amygdala;whole brain;occipital lobe;superior cervical ganglion;medulla oblongata;testis - interstitial;temporal lobe;subthalamic nucleus;fetal brain;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.22489 0.16646 -0.60427181 17.74593064 8.36465 0.30585 KHK 5.36079485314004e-05 0.680282267540769 0.319664124510699 ketohexokinase FUNCTION: Catalyzes the phosphorylation of the ketose sugar fructose to fructose-1-phosphate. {ECO:0000269|PubMed:12941785}.; . TISSUE SPECIFICITY: Most abundant in liver, kidney, gut, spleen and pancreas. Low levels also found in adrenal, muscle, brain and eye. {ECO:0000269|PubMed:9799106}.; unclassifiable (Anatomical System);lymphoreticular;medulla oblongata;hypothalamus;colon;substantia nigra;fovea centralis;choroid;lens;retina;optic nerve;lung;frontal lobe;placenta;macula lutea;liver;testis;spleen;kidney;spinal ganglion;brain;stomach; superior cervical ganglion;medulla oblongata;occipital lobe;pons;atrioventricular node;skeletal muscle;fetal liver;subthalamic nucleus;liver;globus pallidus;appendix;ciliary ganglion;kidney;trigeminal ganglion;parietal lobe; 0.11472 0.24918 0.132352165 63.48785091 3306.22652 10.97643 KHNYN 1.39063137188499e-05 0.957699166785723 0.0422869269005578 KH and NYN domain containing . . . ovary;colon;skin;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;alveolus;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;placenta;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.13632 0.09490 -0.821100135 11.88369899 1285.96189 6.75059 KHSRP 0.99971122153684 0.000288777950147721 5.13012202336161e-10 KH-type splicing regulatory protein FUNCTION: Binds to the dendritic targeting element and may play a role in mRNA trafficking (By similarity). Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single- stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'- UTR, possibly by recruiting degradation machinery to ARE- containing mRNAs. {ECO:0000250, ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:8940189, ECO:0000269|PubMed:9136930}.; . TISSUE SPECIFICITY: Detected in neural and non-neural cell lines.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;urinary;pharynx;blood;lens;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;oesophagus;cerebral cortex;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;temporal lobe;testis;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.45176 0.15486 -0.690637458 15.12149092 19.12445 0.65912 KHSRPP1 . . . KH-type splicing regulatory protein pseudogene 1 . . . . . . . . . . . KIAA0040 . . . KIAA0040 . . . . . . . . . 94.60903 2.09509 KIAA0087 . . . KIAA0087 . . . prostate;macula lutea;blood;fovea centralis;brain;retina;bone marrow; superior cervical ganglion;appendix;skeletal muscle; . . . . 17.91578 0.62616 KIAA0100 0.26524374601424 0.734756253985716 4.45284695378705e-14 KIAA0100 FUNCTION: May be involved in membrane trafficking. {ECO:0000250|UniProtKB:K7VLR4}.; . TISSUE SPECIFICITY: Expressed in pancreas, placenta and up- regulated in breast carcinoma epithelial cells, ductal in situ carcinoma (DCIS), invasive breast carcinoma (IBC) and metastatic breast carcinoma cells (MET). {ECO:0000269|PubMed:16289875}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;nervous;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;duodenum;amnion;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion; 0.29654 . 0.330582712 73.42533616 987.79882 6.06210 KIAA0101 0.129504562347457 0.780205900136832 0.0902895375157108 KIAA0101 FUNCTION: PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with PCNA is disrupted, facilitating the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, facilitating the bypass of replication-fork-blocking lesions. Also acts as a regulator of centrosome number. {ECO:0000269|PubMed:21673012, ECO:0000269|PubMed:23000965}.; . TISSUE SPECIFICITY: Expressed predominantly in liver, pancreas and placenta. Not detected in heart or brain. Highly expressed in a number of tumors, especially esophageal tumors, in anaplastic thyroid carcinomas, adrenocortical carcinomas, and in non-small- cell lung cancer lines. {ECO:0000269|PubMed:11313979, ECO:0000269|PubMed:15789362, ECO:0000269|PubMed:22096502}.; ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; fetal liver;superior cervical ganglion;tumor;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;thymus;bone marrow; 0.76497 0.49034 -0.09720619 46.20193442 33.80011 1.04058 KIAA0125 . . . KIAA0125 . . . . . . . . . 28.99326 0.92695 KIAA0125P1 . . . KIAA0125 pseudogene 1 . . . . . . . . . . . KIAA0125P2 . . . KIAA0125 pseudogene 2 . . . . . . . . . . . KIAA0141 3.06120841888116e-10 0.281915894729241 0.718084104964638 KIAA0141 FUNCTION: Essential for the induction of death receptor-mediated apoptosis through the regulation of caspase activation. {ECO:0000269|PubMed:20563667}.; . TISSUE SPECIFICITY: Detected in liver, skeletal muscle, kidney, pancreas, spleen, thyroid, testis, ovary, small intestine and colon. {ECO:0000269|PubMed:8590280}.; lymphoreticular;myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;larynx;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;head and neck;spleen;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe; 0.04807 . 0.69078985 85.23826374 2730.37291 9.84899 KIAA0196 4.81024990398197e-13 0.996161201349434 0.00383879865008525 KIAA0196 FUNCTION: Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes seems to inhibit WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization, and which is involved in regulation of the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:19922875, PubMed:20498093). May be involved in axonal outgrowth. Involved in cellular localization of ADRB2 (PubMed:23085491). Involved in cellular trafficking of BLOC-1 complex cargos such as ATP7A and VAMP7 (PubMed:23676666). {ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20833645, ECO:0000269|PubMed:23085491, ECO:0000269|PubMed:23676666}.; DISEASE: Ritscher-Schinzel syndrome 1 (RTSC1) [MIM:220210]: A developmental malformation syndrome characterized by craniofacial abnormalities, congenital heart defects, and cerebellar brain malformations. Facial features include prominent occiput, prominent forehead, low-set ears, downslanting palpebral fissures, depressed nasal bridge, and micrognathia. Cardiac defects can include septal defects and aortic stenosis, among others, and brain imaging shows Dandy-Walker malformation, cerebellar vermis hypoplasia, posterior fossa cysts, and ventricular dilatation. Affected individuals have severe developmental delay. {ECO:0000269|PubMed:24065355}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed ubiquitously. {ECO:0000269|PubMed:20833645}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;cornea;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;pons;caudate nucleus;atrioventricular node;skin;parietal lobe; 0.38364 0.11995 -1.302541541 4.930408115 71.05517 1.75514 KIAA0196-AS1 . . . KIAA0196 antisense RNA 1 . . . . . . . . . . . KIAA0226L 2.02280092225205e-11 0.0633812377401641 0.936618762239608 KIAA0226-like . . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;endometrium;thyroid;testis;germinal center;brain;bladder;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;pharynx;blood;breast;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;kidney; testis - interstitial;testis; 0.04680 0.06933 0.602602982 82.87331918 1760.15857 7.74261 KIAA0232 0.99472089633487 0.00527910263801243 1.02711708513853e-09 KIAA0232 . . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;thyroid;germinal center;brain;amygdala;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;liver;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;cerebral cortex;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;cerebellum; amygdala;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.46058 0.12903 -1.721531029 2.476999292 470.48597 4.48840 KIAA0319 7.95792630986591e-12 0.859449550194053 0.140550449797989 KIAA0319 FUNCTION: Involved in neuronal migration during development of the cerebral neocortex. May function in a cell autonomous and a non- cell autonomous manner and play a role in appropriate adhesion between migrating neurons and radial glial fibers. May also regulate growth and differentiation of dendrites. {ECO:0000269|PubMed:19679544}.; DISEASE: Dyslexia 2 (DYX2) [MIM:600202]: A relatively common, complex cognitive disorder characterized by an impairment of reading performance despite adequate motivational, educational and intellectual opportunities. It is a multifactorial trait, with evidence for familial clustering and heritability. {ECO:0000269|PubMed:16600991}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in adult brain cortex and fetal frontal lobe (at protein level). Highly expressed in brain cortex, putamen, amygdala, hippocampus and cerebellum. {ECO:0000269|PubMed:12834540, ECO:0000269|PubMed:17846832}.; . . 0.29211 0.08786 0.699907041 85.30903515 1740.34304 7.70056 KIAA0319L 0.188543868959937 0.811455326407398 8.04632664388287e-07 KIAA0319 like FUNCTION: Possible role in axon guidance through interaction with RTN4R. {ECO:0000269|PubMed:20697954}.; . TISSUE SPECIFICITY: Expressed in cortical neurons in the brain cortex (at protein level). {ECO:0000269|PubMed:20697954}.; myocardium;ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pineal body;muscle;blood;skeletal muscle;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.21728 0.11320 -0.839512508 11.40009436 147.63214 2.64750 KIAA0355 0.877125217335467 0.122874250922698 5.31741835466633e-07 KIAA0355 . . . lymphoreticular;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;bone;testis;dura mater;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);meninges;cartilage;small intestine;heart;islets of Langerhans;skeletal muscle;breast;pia mater;lung;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.17403 . -1.120710825 6.605331446 243.60996 3.36841 KIAA0368 0.999999935694415 6.43055853332734e-08 3.70129999811081e-25 KIAA0368 FUNCTION: Adapter/scaffolding protein that binds to the 26S proteasome, motor proteins and other compartment specific proteins. May couple the proteasome to different compartments including endosome, endoplasmic reticulum and centrosome. May play a role in ERAD and other enhanced proteolyis. {ECO:0000269|PubMed:15496406, ECO:0000269|PubMed:20682791}.; . . smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;amniotic fluid;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;alveolus;head and neck;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;occipital lobe;cerebellum peduncles;globus pallidus;ciliary ganglion;pons;caudate nucleus;atrioventricular node;parietal lobe;skeletal muscle;cingulate cortex; 0.36321 0.08430 -0.031281682 50.5779665 4460.55222 13.39016 KIAA0391 1.7775756011591e-05 0.880329955660109 0.11965226858388 KIAA0391 FUNCTION: Functions in mitochondrial tRNA maturation. Part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/TRMT10C, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends. {ECO:0000269|PubMed:18984158}.; . . . . 0.03125 0.08326 0.154398214 64.73814579 935.18613 5.92876 KIAA0408 1.95785656687142e-06 0.882853197945351 0.117144844198082 KIAA0408 . . . . . 0.36998 . -0.663133267 15.94715735 1821.15649 7.87262 KIAA0430 0.999999565958546 4.34041453515202e-07 2.79065163663742e-18 KIAA0430 FUNCTION: Essential regulator of oogenesis required for female meiotic progression to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Probably acts via some RNA metabolic process, equivalent to the piRNA system in males, which mediates the repression of transposable elements during meiosis by forming complexes composed of RNAs and governs the methylation and subsequent repression of transposons. Also required to protect from DNA double-strand breaks (By similarity). {ECO:0000250}.; . . lymphoreticular;umbilical cord;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;bile duct;lung;placenta;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; subthalamic nucleus;occipital lobe;hypothalamus;prefrontal cortex;globus pallidus; 0.13621 0.10680 -1.519444051 3.450106157 272.29141 3.53706 KIAA0513 0.0758306424438943 0.921748231357443 0.00242112619866309 KIAA0513 . . TISSUE SPECIFICITY: Widely expressed, highest levels in cerebellum, brain cortex, hippocampus, pons, putamen and amygdala. Highly expressed in neurons, but also present in glial cells. Slightly higher expression in the dorsolateral prefrontal cortex of schizophrenic patients compared to control individuals. {ECO:0000269|PubMed:17010949}.; lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hypopharynx;head and neck;mammary gland;cerebellum; whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;temporal lobe;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.17721 0.10731 -0.468351206 23.42533616 3248.77899 10.85849 KIAA0556 1.30820565996232e-17 0.964214353884078 0.0357856461159222 KIAA0556 . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;pharynx;blood;lens;skeletal muscle;breast;lung;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - seminiferous tubule;testis;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.24714 0.09305 0.833999814 88.13399387 1341.46721 6.87531 KIAA0586 1.44868459274921e-12 0.921327184309087 0.0786728156894638 KIAA0586 FUNCTION: Required for ciliogenesis and sonic hedgehog/SHH signaling. {ECO:0000250|UniProtKB:E9PV87, ECO:0000250|UniProtKB:Q1G7G9}.; DISEASE: Joubert syndrome 23 (JBTS23) [MIM:616490]: A mild form of Joubert syndrome, a disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy, renal disease, liver fibrosis, and polydactyly. {ECO:0000269|PubMed:26096313}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;colon;blood;skin;retina;uterus;pancreas;prostate;lung;nasopharynx;trabecular meshwork;bone;placenta;visual apparatus;liver;testis;cervix;spleen;germinal center;brain;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis;pons;atrioventricular node;trigeminal ganglion; 0.11831 0.09402 0.611719262 82.96768106 722.34786 5.33549 KIAA0753 3.16922700490618e-19 0.0302375083391204 0.96976249166088 KIAA0753 FUNCTION: Involved in centriole duplication. Positively regulates CEP63 centrosomal localization. Required for WDR62 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:24613305, PubMed:26297806). {ECO:0000269|PubMed:26297806}.; . . medulla oblongata;colon;parathyroid;skin;uterus;prostate;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;lens;breast;pancreas;lung;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;globus pallidus; 0.22582 . 2.140462972 97.95942439 7301.0268 18.39538 KIAA0754 0.0210361269465471 0.962026533660541 0.0169373393929118 KIAA0754 . . . . . . . . . 524.5633 4.67394 KIAA0825 4.26150495630825e-07 0.1151895496216 0.884810024227904 KIAA0825 . . . breast;unclassifiable (Anatomical System);lung;ovary;spleen;blood;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.05662 . 0.237127192 68.98443029 2970.03785 10.33646 KIAA0895 0.00114571990792928 0.989055833737545 0.00979844635452559 KIAA0895 . . . unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;parathyroid;blood;skin;skeletal muscle;bone marrow;uterus;pancreas;whole body;lung;adrenal gland;nasopharynx;bone;thyroid;liver;testis;cervix;spleen;kidney;brain;mammary gland;stomach;gall bladder; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . -0.091746757 46.91554612 66.94642 1.69076 KIAA0895L 0.0184330576803288 0.961138312596208 0.0204286297234633 KIAA0895-like . . . smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;thyroid;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;cervix;kidney;mammary gland;stomach; . . . 0.150760231 64.51403633 718.9968 5.32337 KIAA0907 0.99711361843545 0.00288637582011582 5.7444339196238e-09 KIAA0907 . . . . . 0.44046 0.11262 -0.582225231 18.44184949 24.07472 0.79163 KIAA0922 0.999390132960342 0.000609867039613747 4.40362688116055e-14 KIAA0922 FUNCTION: Isoform 1: Membrane-associated form that antagonizes canonical Wnt signaling by triggering lysosome-dependent degradation of Wnt-activated LRP6. Regulates thymocyte proliferation. {ECO:0000269|PubMed:23690469}.; . TISSUE SPECIFICITY: Expressed in thymocytes. {ECO:0000269|PubMed:23690469}.; myocardium;smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.42290 0.08921 0.021910749 55.61453173 2182.5217 8.60927 KIAA0930 0.815289886693543 0.184518189729148 0.000191923577309413 KIAA0930 . . . lymphoreticular;ovary;salivary gland;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;cartilage;heart;small intestine;blood;breast;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;amygdala;superior cervical ganglion;medulla oblongata;hypothalamus;atrioventricular node;pons;caudate nucleus;skeletal muscle;prefrontal cortex;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.16326 0.09256 -0.977252525 8.799245105 22.55837 0.75396 KIAA1024 0.000865675748600288 0.984640022098172 0.0144943021532276 KIAA1024 . . . unclassifiable (Anatomical System);optic nerve;lung;islets of Langerhans;macula lutea;testis;fovea centralis;choroid;lens;brain;skin;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;adrenal gland;trigeminal ganglion;skeletal muscle;cerebellum; 0.12875 0.11437 0.235100429 68.59518754 1242.01695 6.65395 KIAA1024L . . . KIAA1024-like . . . . . 0.20064 . . . 51.62061 1.41828 KIAA1033 0.155503528869923 0.844496470733422 3.96655881315733e-10 KIAA1033 FUNCTION: Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes sems to inhibit WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization, and which is involved in the regulation of the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:19922875, PubMed:20498093). {ECO:0000250|UniProtKB:Q3UMB9, ECO:0000303|PubMed:21498477, ECO:0000305|PubMed:19922875, ECO:0000305|PubMed:20498093}.; DISEASE: Mental retardation, autosomal recessive 43 (MRT43) [MIM:615817]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:21498477}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;oral cavity;urinary;blood;skeletal muscle;pancreas;lung;placenta;liver;duodenum;cervix;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;spinal cord;globus pallidus;ciliary ganglion;white blood cells;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.20508 0.09840 0.205769367 67.49823071 290.22506 3.64571 KIAA1107 . . . KIAA1107 . . . . . 0.50292 0.07798 2.195683333 98.11276244 680.26302 5.21357 KIAA1109 3.91297690789911e-08 0.999999960870231 1.87010268666252e-25 KIAA1109 . . TISSUE SPECIFICITY: Highly expressed in testis and ovary. Weakly or not expressed in other tissues. {ECO:0000269|PubMed:16545529}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;cerebellum cortex;tongue;islets of Langerhans;hypothalamus;urinary;blood;lens;skeletal muscle;bile duct;breast;lung;epididymis;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;mammary gland;stomach;aorta; dorsal root ganglion;amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;hypothalamus;atrioventricular node;skin;skeletal muscle;prefrontal cortex;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.42532 . -1.562384295 3.214201463 2175.71619 8.58836 KIAA1143 0.025102469555063 0.781456207523658 0.193441322921279 KIAA1143 . . . ovary;salivary gland;intestine;colon;skin;bone marrow;prostate;whole body;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;pharynx;blood;skeletal muscle;bile duct;breast;lung;cornea;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; . 0.25801 . 0.525552348 80.57914603 194.68726 3.02453 KIAA1147 0.00204302025834016 0.912286608332474 0.0856703714091854 KIAA1147 FUNCTION: May play a role in neuritogenesis, as well as in neuronal recovery and/or restructuring in the hippocampus following transient cerebral ischemia. {ECO:0000250}.; . . . . 0.40791 . 0.306902668 72.38145789 46.03962 1.30736 KIAA1161 5.13052574184938e-10 0.0313459656128245 0.968654033874123 KIAA1161 FUNCTION: Putative glucosidase. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;cartilage;colon;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;frontal lobe;placenta;macula lutea;liver;spleen;kidney;brain;stomach; superior cervical ganglion;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.22604 . . . 3679.51308 11.79726 KIAA1191 0.00156087265921572 0.968895480405413 0.0295436469353716 KIAA1191 FUNCTION: Potential NADPH-dependent oxidoreductase. May be involved in the regulation of neuronal survival, differentiation and axonal outgrowth.; . TISSUE SPECIFICITY: Down-regulated in the occipital lobe of an early stage Alzheimer disease patients. {ECO:0000269|PubMed:17032350}.; smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;spinal cord;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta; . 0.28052 0.09365 -0.0274281 51.65723048 46.435 1.31427 KIAA1210 0.090793121231346 0.909191899585891 1.49791827630481e-05 KIAA1210 . . . . . . . 2.835279393 99.09766454 1224.70101 6.61405 KIAA1211 0.130364633073797 0.869595856294214 3.95106319893037e-05 KIAA1211 . . . unclassifiable (Anatomical System);lung;whole body;placenta;visual apparatus;testis;colon;germinal center;brain;skin; . . . 1.63326524 96.08398207 6840.95695 17.62408 KIAA1211L . . . KIAA1211-like . . . . . 0.17839 . . . 598.01365 4.95028 KIAA1217 0.0141678943279396 0.9858320165656 8.91064600879959e-08 KIAA1217 FUNCTION: Required for normal development of intervertebral disks. {ECO:0000250|UniProtKB:A2AQ25}.; . . colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;larynx;thyroid;bone;brain;unclassifiable (Anatomical System);heart;spinal cord;blood;lens;skeletal muscle;breast;lung;macula lutea;liver;hypopharynx;spleen;head and neck;kidney;stomach;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22162 0.09445 -3.009169053 0.524887945 2127.12642 8.49315 KIAA1257 1.74543485053087e-08 0.124774530287565 0.875225452258086 KIAA1257 . . . unclassifiable (Anatomical System);medulla oblongata;lung;whole body;testis;stomach; superior cervical ganglion;ciliary ganglion; 0.05969 0.08096 0.951720429 90.06251474 89.37584 2.03224 KIAA1324 2.14864520738644e-08 0.998570003732984 0.00142997478056437 KIAA1324 FUNCTION: May protect cells from cell death by inducing cytosolic vacuolization and upregulating the autophagy pathway. {ECO:0000269|PubMed:21072319}.; . TISSUE SPECIFICITY: Expressed in normal endometrium but overexpressed in endometroid tumors. {ECO:0000269|PubMed:16322283}.; . . 0.18892 0.10823 -0.501537595 21.83887709 267.58763 3.50758 KIAA1324L 0.000166955192879022 0.998513152749683 0.00131989205743749 KIAA1324-like . . . unclassifiable (Anatomical System);heart;cartilage;retina;lung;trabecular meshwork;thyroid;bone;visual apparatus;liver;testis;head and neck;brain;aorta;stomach; . 0.42256 . -0.396754488 26.97570182 453.25685 4.43012 KIAA1328 6.0725380486659e-05 0.894567112935896 0.105372161683618 KIAA1328 FUNCTION: Competes with SMC1 for binding to SMC3. May affect the availability of SMC3 to engage in the formation of multimeric protein complexes. {ECO:0000269|PubMed:15656913}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15656913}.; lung;cartilage;bone;visual apparatus;testis;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.32449 . 0.040529541 57.15380986 . . KIAA1429 0.999441598833336 0.000558401166656554 7.18794324544761e-15 KIAA1429 FUNCTION: Required for N6-methyladenosine (m6A) methylation of mRNAs, a modification that plays a role in the efficiency of mRNA splicing and processing (PubMed:24981863). Involved in mRNA splicing regulation, probably via its function in m6A methylation (Probable). {ECO:0000269|PubMed:24981863, ECO:0000305}.; . . ovary;colon;fovea centralis;skin;uterus;prostate;whole body;oesophagus;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;ciliary ganglion;atrioventricular node; 0.14550 0.10544 -1.365077992 4.5175749 278.01152 3.57281 KIAA1456 . . . KIAA1456 . . . . . 0.08688 0.08809 0.428052693 77.31186601 330.03285 3.86068 KIAA1462 0.104293752088672 0.895647758838687 5.84890726415775e-05 KIAA1462 . . . . . 0.12446 0.08908 1.219838911 93.16466148 1572.86658 7.33938 KIAA1468 0.999999559987516 4.40012484288651e-07 2.88508973483212e-18 KIAA1468 . . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;bone;thyroid;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;lacrimal gland;islets of Langerhans;blood;skeletal muscle;bile duct;breast;pancreas;pia mater;lung;nasopharynx;placenta;macula lutea;liver;spleen;kidney;mammary gland; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;occipital lobe;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skin; 0.18204 0.12098 -1.285933373 5.083746167 74.67048 1.80768 KIAA1522 0.802365146971355 0.197587909038305 4.69439903398035e-05 KIAA1522 . . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;amnion;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; . 0.11692 0.08324 0.431697208 77.32955886 1424.37091 7.04850 KIAA1524 5.75236747593882e-08 0.991649476552644 0.00835046592368076 KIAA1524 FUNCTION: Oncoprotein that inhibits PP2A and stabilizes MYC in human malignancies. Promotes anchorage-independent cell growth and tumor formation. {ECO:0000269|PubMed:17632056}.; . TISSUE SPECIFICITY: Expressed at low levels in most of the tissues. Overexpressed in head-and-neck squamous cell carcinomas (HNSCC). Present in liver cancer cells (at protein level). {ECO:0000269|PubMed:12118381, ECO:0000269|PubMed:17632056}.; unclassifiable (Anatomical System);ovary;heart;salivary gland;muscle;intestine;pharynx;colon;blood;breast;uterus;prostate;whole body;lung;visual apparatus;liver;spleen;germinal center;kidney;brain;pineal gland;bladder;thymus; dorsal root ganglion;superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.14654 0.10121 1.846456612 97.11606511 2367.40992 9.03223 KIAA1549 0.998645789892966 0.00135421009951753 7.51601382700902e-12 KIAA1549 . DISEASE: Note=A chromosomal aberration involving KIAA1549 is found in pilocytic astrocytoma. A tandem duplication of 2 Mb at 7q34 leads to the expression of a KIAA1549-BRAF fusion protein with a constitutive kinase activity and inducing cell transformation. {ECO:0000269|PubMed:18974108}.; . unclassifiable (Anatomical System);heart;muscle;colon;fovea centralis;choroid;lens;skin;retina;uterus;breast;pancreas;prostate;optic nerve;lung;frontal lobe;placenta;bone;macula lutea;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.46006 0.10368 1.659220063 96.23732012 8982.64039 20.55796 KIAA1549L 0.00370822940112543 0.99629114409317 6.26505704374445e-07 KIAA1549-like . . . . . 0.15339 0.07162 -3.240384062 0.442321302 369.11765 4.05907 KIAA1551 0.0364911089052999 0.963495968663988 1.29224307125059e-05 KIAA1551 . . . . . 0.09964 0.10384 2.846478562 99.1153574 3500.83046 11.39648 KIAA1586 1.77777131304971e-06 0.665696762326082 0.334301459902605 KIAA1586 . . . . . 0.08253 . 0.578735925 82.29535268 2026.7996 8.28178 KIAA1614 2.19336786808695e-13 0.114331848245567 0.885668151754213 KIAA1614 . . . . . 0.13398 . 0.879940821 88.90658174 1031.80761 6.17106 KIAA1614-AS1 . . . KIAA1614 antisense RNA 1 . . . . . . . . . . . KIAA1644 0.676861238307606 0.318457205628617 0.00468155606377717 KIAA1644 . . . . . . . -0.139478553 43.29440906 142.92745 2.60644 KIAA1671 . . . KIAA1671 . . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;pons;skeletal muscle; . . . . 239.04669 3.34052 KIAA1683 8.28481624156168e-06 0.980911152150867 0.0190805630328913 KIAA1683 . . . unclassifiable (Anatomical System);cartilage;ovary;heart;tongue;islets of Langerhans;colon;substantia nigra;parathyroid;blood;skin;uterus;pancreas;lung;placenta;thyroid;liver;testis;spleen;head and neck;brain;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;temporal lobe;testis;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07923 0.08035 3.760579722 99.61075725 2365.24197 9.02868 KIAA1715 0.00192358301419587 0.993370396678866 0.00470602030693838 KIAA1715 FUNCTION: Plays a role in tubular endoplasmic reticulum network formation and maintenance. May be involved in limb and central nervous system development. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;testis;dura mater;germinal center;bladder;brain;unclassifiable (Anatomical System);meninges;heart;spinal cord;adrenal cortex;blood;lens;breast;pia mater;lung;nasopharynx;placenta;macula lutea;liver;alveolus;spleen;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09046 0.27953 0.21689899 68.12927577 139.14568 2.57097 KIAA1755 2.32481835791205e-15 0.0575247306212479 0.94247526937875 KIAA1755 . . . unclassifiable (Anatomical System);prostate;pancreas;optic nerve;cartilage;heart;cerebral cortex;endometrium;iris;brain;retina;cerebellum; superior cervical ganglion;atrioventricular node; 0.03468 . 0.416947309 76.81646615 7862.82524 19.14747 KIAA1841 3.32934655708566e-06 0.996987479509464 0.00300919114397881 KIAA1841 . . . unclassifiable (Anatomical System);smooth muscle;lacrimal gland;colon;fovea centralis;skeletal muscle;retina;pancreas;prostate;lung;larynx;adrenal gland;synovium;placenta;bone;macula lutea;head and neck;cervix;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;adrenal gland;globus pallidus;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion; 0.15098 . -0.775187015 13.05142722 146.14924 2.63404 KIAA1958 0.0490021397440159 0.928215520363684 0.0227823398922999 KIAA1958 . . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;hypothalamus;pineal body;skin;retina;uterus;pancreas;lung;endometrium;larynx;bone;liver;testis;head and neck;cervix;kidney;brain;pineal gland;bladder; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.20231 . -0.955204708 9.170794999 72.59191 1.77648 KIAA2012 . . . KIAA2012 . . . . . . . . . . . KIAA2013 . . . KIAA2013 . . . . . 0.18356 . . . 458.56772 4.44616 KIAA2022 0.950542378844954 0.0494513915277112 6.22962733429486e-06 KIAA2022 FUNCTION: May be involved in neuronal development. {ECO:0000250}.; DISEASE: Mental retardation, X-linked 98 (MRX98) [MIM:300912]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRX98 patients show delayed psychomotor development, absent or poor speech development, and postnatal growth retardation, often with microcephaly. Some patients show autistic behavioral features, such as stereotypic hand movements and repetitive behaviors. Additional, more variable features include spasticity, axial hypotonia, seizures, drooling, gastroesophageal reflux, and lack of sphincter control. {ECO:0000269|PubMed:15466006, ECO:0000269|PubMed:23615299}. Note=The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving KIAA2022 is found in patients with severe mental retardation. Pericentric inversion inv(X)(p22.3;q13.2) with P2RY8 leading to inactivation of KIAA2022 (PubMed:15466006). {ECO:0000269|PubMed:15466006}.; . unclassifiable (Anatomical System);lung;ovary;endometrium;islets of Langerhans;placenta;parathyroid;kidney;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.50276 0.09638 -0.773369631 13.10450578 65.43999 1.66592 KIAA2026 . . . KIAA2026 . . . . . 0.48111 0.08981 . . 566.64511 4.83451 KIDINS220 0.0290445776929918 0.970955421052791 1.25421747106881e-09 kinase D-interacting substrate 220kDa FUNCTION: Promotes a prolonged MAP-kinase signaling by neurotrophins through activation of a Rap1-dependent mechanism. Provides a docking site for the CRKL-C3G complex, resulting in Rap1-dependent sustained ERK activation. May play an important role in regulating postsynaptic signal transduction through the syntrophin-mediated localization of receptor tyrosine kinases such as EPHA4. In cooperation with SNTA1 can enhance EPHA4-induced JAK/STAT activation. Plays a role in nerve growth factor (NGF)- induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth. May play a role in neurotrophin- and ephrin-mediated neuronal outgrowth and in axon guidance during neural development and in neuronal regeneration (By similarity). Modulates stress- induced apoptosis of melanoma cells via regulation of the MEK/ERK signaling pathway. {ECO:0000250, ECO:0000269|PubMed:18089783}.; . TISSUE SPECIFICITY: Abundant in developing and adult neural tissues as well as neuroendocrine cells and dendritic cells. Overexpressed in melanoma and melanoma cell lines. {ECO:0000269|PubMed:18089783}.; ovary;umbilical cord;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;thyroid;germinal center;brain;gall bladder;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; amygdala;dorsal root ganglion;thalamus;occipital lobe;superior cervical ganglion;hypothalamus;spinal cord;pons;atrioventricular node;skeletal muscle;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; . 0.58778 -2.24910054 1.29747582 2365.02521 9.02690 KIF1A 0.99998943706213 1.05629378704465e-05 1.11366234667812e-17 kinesin family member 1A FUNCTION: Motor for anterograde axonal transport of synaptic vesicle precursors. {ECO:0000250}.; DISEASE: Neuropathy, hereditary sensory, 2C (HSN2C) [MIM:614213]: A neurodegenerative disorder characterized by onset in the first decade of progressive distal sensory loss leading to ulceration and amputation of the fingers and toes. Affected individuals also develop distal muscle weakness, primarily affecting the lower limbs. {ECO:0000269|PubMed:21820098}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mental retardation, autosomal dominant 9 (MRD9) [MIM:614255]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:21376300}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in neurons. {ECO:0000269|PubMed:21376300}.; myocardium;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;cerebral cortex;bone;iris;testis;spinal ganglion;pineal gland;brain;unclassifiable (Anatomical System);amygdala;islets of Langerhans;hypothalamus;pineal body;blood;lens;skeletal muscle;breast;pancreas;lung;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;mammary gland;cerebellum; amygdala;whole brain;subthalamic nucleus;medulla oblongata;occipital lobe;temporal lobe;globus pallidus;pons;parietal lobe;cingulate cortex; 0.50155 0.15226 -3.665133381 0.265392781 117.91317 2.36023 KIF1B 0.999999999958917 4.10829820545469e-11 1.80480823849562e-29 kinesin family member 1B FUNCTION: Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility. Isoform 2 is required for induction of neuronal apoptosis. {ECO:0000269|PubMed:18334619}.; DISEASE: Neuroblastoma 1 (NBLST1) [MIM:256700]: A common neoplasm of early childhood arising from embryonic cells that form the primitive neural crest and give rise to the adrenal medulla and the sympathetic nervous system. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Pheochromocytoma (PCC) [MIM:171300]: A catecholamine- producing tumor of chromaffin tissue of the adrenal medulla or sympathetic paraganglia. The cardinal symptom, reflecting the increased secretion of epinephrine and norepinephrine, is hypertension, which may be persistent or intermittent. {ECO:0000269|PubMed:18334619}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 3 is abundant in the skeletal muscle. It is also expressed in fetal brain, lung and kidney, and adult heart, placenta, testis, ovary and small intestine. Isoform 2 is abundant in the brain and also expressed in fetal heart, lung, liver and kidney, and adult skeletal muscle, placenta, liver, kidney, heart, spleen, thymus, prostate, testis, ovary, small intestine, colon and pancreas. {ECO:0000269|PubMed:10762626, ECO:0000269|PubMed:11526494, ECO:0000269|PubMed:12888911}.; ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;gum;bone;thyroid;testis;amniotic fluid;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;spinal cord;adrenal cortex;blood;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach;cerebellum; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.20073 0.27386 -1.447883661 3.927813163 705.73842 5.27747 KIF1BP . . . KIF1 binding protein FUNCTION: Required for organization of axonal microtubules, and axonal outgrowth and maintenance during peripheral and central nervous system development. {ECO:0000269|PubMed:16225668, ECO:0000269|PubMed:20621975, ECO:0000269|PubMed:23427148}.; . TISSUE SPECIFICITY: Highly expressed in heart, brain, ovary, testis, spinal cord and all specific brain regions examined. Moderate expressed at intermediate level in all other adult tissues examined, as well as in fetal liver and brain. Not expressed in blood leukocytes. {ECO:0000269|PubMed:10574462, ECO:0000269|PubMed:16225668}.; . . 0.14379 0.15292 -0.334253673 30.70299599 . . KIF1C 0.470778561371856 0.529221362273241 7.6354902913803e-08 kinesin family member 1C FUNCTION: Motor required for the retrograde transport of Golgi vesicles to the endoplasmic reticulum. Has a microtubule plus end- directed motility. {ECO:0000269|PubMed:9685376}.; DISEASE: Spastic ataxia 2, autosomal recessive (SPAX2) [MIM:611302]: A neurologic disorder characterized by cerebellar ataxia, dysarthria, and variable spasticity of the lower limbs. Cognition is not affected. {ECO:0000269|PubMed:24319291}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues examined, with most abundant expression in heart and skeletal muscle. {ECO:0000269|PubMed:9685376}.; myocardium;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;uterus corpus;thalamus;medulla oblongata;heart;spinal cord;ciliary ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.76138 0.16258 -0.654057602 16.14177872 407.93858 4.23504 KIF2A 0.999339688994676 0.000660310226639107 7.78684518259639e-10 kinesin heavy chain member 2A FUNCTION: Plus end-directed microtubule-dependent motor required for normal brain development. May regulate microtubule dynamics during axonal growth. Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate. Required for normal spindle dynamics during mitosis. Promotes spindle turnover. Implicated in formation of bipolar mitotic spindles. Has microtubule depolymerization activity. {ECO:0000269|PubMed:15843429, ECO:0000269|PubMed:17538014, ECO:0000269|PubMed:18411309}.; DISEASE: Cortical dysplasia, complex, with other brain malformations 3 (CDCBM3) [MIM:615411]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Clinical features include early-onset epilepsy, and various malformations of cortical development such as agyria, posterior or frontal pachygyria, subcortical band heterotopia, and thin corpus callosum. {ECO:0000269|PubMed:23603762}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.18081 0.12580 0.260991686 70.25831564 198.77592 3.04642 KIF2B 3.73383408114166e-15 0.00078965537264857 0.999210344627348 kinesin family member 2B FUNCTION: Plus end-directed microtubule-dependent motor required for spindle assembly and chromosome movement. Has microtubule depolymerization activity. {ECO:0000269|PubMed:17538014}.; . TISSUE SPECIFICITY: Highest level in lung. High level in ovary, moderate levels in heart, kidney, placenta, skeletal muscle and spleen (at protein level). Pancreas and spleen express a shorter isoform (at protein level). {ECO:0000269|PubMed:17538014}.; unclassifiable (Anatomical System);medulla oblongata;lung;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.09175 0.09169 1.940150696 97.52300071 2439.30952 9.18412 KIF2C 0.01719407223229 0.982797843153839 8.08461387088155e-06 kinesin family member 2C FUNCTION: In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells. Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis. {ECO:0000269|PubMed:19060894, ECO:0000269|PubMed:21820309}.; . TISSUE SPECIFICITY: Expressed at high levels in thymus and testis, at low levels in small intestine, the mucosal lining of colon, and placenta, and at very low levels in spleen and ovary; expression is not detected in prostate, peripheral blood Leukocytes, heart, brain, lung, liver, skeletal muscle, kidney or pancreas. Isoform 2 is testis-specific. {ECO:0000269|PubMed:12383881, ECO:0000269|PubMed:9434124}.; . . 0.76465 0.14784 0.268267497 70.64166077 1507.41226 7.21366 KIF3A 0.992416127781631 0.00758385990988457 1.23084841489024e-08 kinesin family member 3A FUNCTION: Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro. Plays a role in primary cilia formation (By similarity). {ECO:0000250}.; . . . . 0.54259 0.24823 -0.626318434 17.03231894 3767.74634 12.00714 KIF3B 0.299149040547773 0.700815931947978 3.50275042495853e-05 kinesin family member 3B FUNCTION: Involved in tethering the chromosomes to the spindle pole and in chromosome movement. Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro (By similarity). {ECO:0000250}.; . . . . 0.38115 0.21061 -0.66859065 15.76433121 38.93055 1.15320 KIF3C 0.909864325651814 0.0901298824134501 5.791934735864e-06 kinesin family member 3C FUNCTION: Microtubule-based anterograde translocator for membranous organelles. {ECO:0000250}.; . . ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;thyroid;bone;testis;brain;artery;unclassifiable (Anatomical System);heart;cartilage;cerebellum cortex;islets of Langerhans;hypothalamus;spinal cord;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;mammary gland;aorta; whole brain;dorsal root ganglion;amygdala;thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.27355 0.10890 -0.753139731 13.67067705 112.66383 2.30815 KIF4A 0.999968444608122 3.15553917828172e-05 9.5526460657378e-14 kinesin family member 4A FUNCTION: Motor protein that translocates PRC1 to the plus ends of interdigitating spindle microtubules during the metaphase to anaphase transition, an essential step for the formation of an organized central spindle midzone and midbody and for successful cytokinesis. May play a role in mitotic chromosomal positioning and bipolar spindle stabilization. {ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105}.; . TISSUE SPECIFICITY: Highly expressed in hematopoietic tissues, fetal liver, spleen, thymus and adult thymus and bone marrow. Lower levels are found in heart, testis, kidney, colon and lung. {ECO:0000269|PubMed:10978527}.; . . . 0.11857 -0.754958418 13.57631517 1124.59701 6.39853 KIF4B 3.11373152293453e-19 0.00219585058836711 0.997804149411633 kinesin family member 4B FUNCTION: Motor protein that translocates PRC1 to the plus ends of interdigitating spindle microtubules during the metaphase to anaphase transition, an essential step for the formation of an organized central spindle midzone and midbody and for successful cytokinesis. May play a role in mitotic chromosomal positioning and bipolar spindle stabilization (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in testis. {ECO:0000269|PubMed:16201836}.; . . . 0.11857 1.140856814 92.36848313 5037.447 14.51218 KIF4CP . . . kinesin family member 4C, pseudogene . . . . . . . . . . . KIF5A 0.999979703146806 2.0296853192745e-05 1.33501206804528e-15 kinesin family member 5A FUNCTION: Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). {ECO:0000250}.; DISEASE: Spastic paraplegia 10, autosomal dominant (SPG10) [MIM:604187]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. {ECO:0000269|PubMed:12355402, ECO:0000269|PubMed:15452312, ECO:0000269|PubMed:16476820, ECO:0000269|PubMed:16489470, ECO:0000269|PubMed:18245137, ECO:0000269|PubMed:18853458, ECO:0000269|PubMed:21107874}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Distributed throughout the CNS but is highly enriched in subsets of neurons.; unclassifiable (Anatomical System);amygdala;sympathetic chain;choroid;fovea centralis;lens;skeletal muscle;retina;optic nerve;frontal lobe;larynx;hippocampus;macula lutea;head and neck;brain; dorsal root ganglion;whole brain;medulla oblongata;superior cervical ganglion;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.40931 0.17076 -1.30798293 4.877329559 77.87458 1.86087 KIF5B 0.761006987755031 0.23899300671926 5.52570966545901e-09 kinesin family member 5B FUNCTION: Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. {ECO:0000250}.; . . ovary;colon;parathyroid;skin;retina;uterus;prostate;frontal lobe;cochlea;endometrium;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;spinal cord;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;hypopharynx;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach; occipital lobe;medulla oblongata;testis - interstitial;superior cervical ganglion;pons;skeletal muscle;uterus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.57260 0.11650 -0.933156985 9.54824251 42.89767 1.24184 KIF5C 0.999515597151875 0.000484402774058485 7.40667461656175e-11 kinesin family member 5C FUNCTION: Mediates dendritic trafficking of mRNAs (By similarity). Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. {ECO:0000250}.; DISEASE: Cortical dysplasia, complex, with other brain malformations 2 (CDCBM2) [MIM:615282]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Clinical features include intrauterine growth retardation, fetal akinesia, seizures, microcephaly, lack of psychomotor development, and arthrogryposis. Brain imaging shows malformations of cortical development, including polymicrogyria, gyral simplification, and thin corpus callosum. {ECO:0000269|PubMed:23603762}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest expression in brain, prostate and testis, and moderate expression in kidney, small intestine and ovary.; . . 0.75500 . . . 88.6122 2.01914 KIF6 1.03952440427845e-16 0.225768255000911 0.774231744999089 kinesin family member 6 . . . lung;liver;testis;colon;spleen;lens;brain; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.09539 0.09484 0.295774947 71.64425572 487.42818 4.54431 KIF7 4.15765422074511e-08 0.986846970144433 0.0131529882790252 kinesin family member 7 FUNCTION: Essential for hedgehog signaling regulation: acts as both a negative and positive regulator of sonic hedgehog (Shh) and Indian hedgehog (Ihh) pathways, acting downstream of SMO, through both SUFU-dependent and -independent mechanisms (PubMed:21633164). Involved in the regulation of microtubular dynamics. Required for proper organization of the ciliary tip and control of ciliary localization of SUFU-GLI2 complexes (By similarity). Required for localization of GLI3 to cilia in response to Shh. Negatively regulates Shh signaling by preventing inappropriate activation of the transcriptional activator GLI2 in the absence of ligand. Positively regulates Shh signaling by preventing the processing of the transcription factor GLI3 into its repressor form. In keratinocytes, promotes the dissociation of SUFU-GLI2 complexes, GLI2 nuclear translocation and Shh signaling activation (By similarity). Involved in the regulation of epidermal differentiation and chondrocyte development (By similarity). {ECO:0000250, ECO:0000269|PubMed:21633164}.; DISEASE: Bardet-Biedl syndrome (BBS) [MIM:209900]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:21552264}. Note=The gene represented in this entry may act as a disease modifier. Heterozygous missense mutations in KIF7 may genetically interact with other BBS genes and contribute to disease manifestation and severity.; DISEASE: Hydrolethalus syndrome 2 (HLS2) [MIM:614120]: An embryonic lethal disorder characterized by hydrocephaly or anencephaly, postaxial polydactyly of the upper limbs, and pre- or postaxial polydactyly of the lower limbs. Duplication of the hallux is a common finding. {ECO:0000269|PubMed:21552264}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Acrocallosal syndrome (ACLS) [MIM:200990]: A syndrome characterized by hypogenesis or agenesis of the corpus callosum. Clinical features include postaxial polydactyly, hallux duplication, macrocephaly, craniofacial abnormalities, severe developmental delay and mental retardation. {ECO:0000269|PubMed:21552264, ECO:0000269|PubMed:23125460}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Joubert syndrome 12 (JBTS12) [MIM:200990]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. {ECO:0000269|PubMed:21633164}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pallister-Hall syndrome (PHS) [MIM:146510]: An autosomal dominant disorder characterized by a wide range of clinical manifestations. Clinical features include hypothalamic hamartoma, pituitary dysfunction, central or postaxial polydactyly, and syndactyly. Malformations are frequent in the viscera, e.g. anal atresia, bifid uvula, congenital heart malformations, pulmonary or renal dysplasia. {ECO:0000269|PubMed:21552264}. Note=The gene represented in this entry may be involved in disease pathogenesis.; TISSUE SPECIFICITY: Embryonic stem cells, melanotic melanoma and Jurkat T-cells. Expressed in heart, lung, liver, kidney, testis, retina, placenta, pancreas, colon, small intestin, prostate and thymus. {ECO:0000269|PubMed:21633164}.; . . 0.15677 0.10460 -0.27198537 33.97617363 8579.39436 20.01290 KIF9 2.17357320878688e-11 0.625671392479853 0.374328607498412 kinesin family member 9 . . . medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;thyroid;testis;brain;artery;bladder;unclassifiable (Anatomical System);heart;pharynx;blood;lens;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach;aorta;cerebellum; . 0.17471 . 0.20394914 67.45694739 190.70306 2.99611 KIF9-AS1 . . . KIF9 antisense RNA 1 . . . . . . . . . . . KIF11 0.999996042973183 3.95702681351941e-06 3.00342714766233e-15 kinesin family member 11 FUNCTION: Motor protein required for establishing a bipolar spindle. Blocking of KIF11 prevents centrosome migration and arrest cells in mitosis with monoastral microtubule arrays. {ECO:0000269|PubMed:19001501}.; DISEASE: Microcephaly with or without chorioretinopathy, lymphedema, or mental retardation (MCLMR) [MIM:152950]: An autosomal dominant disorder that involves an overlapping but variable spectrum of central nervous system and ocular developmental anomalies. Microcephaly ranges from mild to severe and is often associated with mild to moderate developmental delay and a characteristic facial phenotype with upslanting palpebral fissures, broad nose with rounded tip, long philtrum with thin upper lip, prominent chin, and prominent ears. Chorioretinopathy is the most common eye abnormality, but retinal folds, microphthalmia, and myopic and hypermetropic astigmatism have also been reported, and some individuals have no overt ocular phenotype. Congenital lymphedema, when present, is typically confined to the dorsa of the feet, and lymphoscintigraphy reveals the absence of radioactive isotope uptake from the webspaces between the toes. {ECO:0000269|PubMed:22284827}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;uterus;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;cervix;stomach; superior cervical ganglion;tumor;pons; 0.17569 0.13424 0.066214104 58.95848077 111.45197 2.29872 KIF12 1.78101316758064e-05 0.99342445365606 0.00655773621226393 kinesin family member 12 . . TISSUE SPECIFICITY: Expressed in fetal liver, adult brain and pancreatic islet as well as in kidney tumors, uterus cancer and pancreatic cancer. {ECO:0000269|PubMed:15643526}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;blood;bone marrow;uterus;pancreas;prostate;optic nerve;endometrium;placenta;liver;amniotic fluid;spleen;kidney;brain;mammary gland;stomach; superior cervical ganglion; 0.06566 0.09954 -0.132199953 43.97853267 986.00925 6.05404 KIF13A 0.999958505813411 4.14941865892296e-05 5.23014531016222e-19 kinesin family member 13A FUNCTION: Plus end-directed microtubule-dependent motor protein involved in intracellular transport and regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis and cytokinesis. Mediates the transport of M6PR- containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. Also required for the abcission step in cytokinesis: mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. {ECO:0000269|PubMed:19841138, ECO:0000269|PubMed:20208530}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in heart, brain and skeletal muscle. {ECO:0000269|PubMed:11374900, ECO:0000269|PubMed:11861365}.; unclassifiable (Anatomical System);heart;lacrimal gland;colon;parathyroid;skin;skeletal muscle;breast;uterus;lung;frontal lobe;endometrium;nasopharynx;bone;thyroid;placenta;visual apparatus;alveolus;hypopharynx;testis;head and neck;kidney;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14914 0.13297 -0.093786226 46.49681529 493.50968 4.56777 KIF13B 0.000199447010513076 0.99980055240626 5.83227045132573e-10 kinesin family member 13B FUNCTION: Involved in reorganization of the cortical cytoskeleton. Regulates axon formation by promoting the formation of extra axons. May be functionally important for the intracellular trafficking of MAGUKs and associated protein complexes. {ECO:0000269|PubMed:20194617}.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.14525 0.14744 -1.447883661 3.927813163 356.63148 3.99898 KIF14 6.0274856650418e-05 0.999939645712349 7.94310003111228e-08 kinesin family member 14 FUNCTION: Microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity (By similarity). Plays a role in many processes like cell division, cytokinesis and also in cell proliferation and apoptosis (PubMed:24784001, PubMed:16648480). During cytokinesis, targets to central spindle and midbody through its interaction with PRC1 and CIT respectively (PubMed:16431929). Regulates cell growth through regulation of cell cycle progression and cytokinesis (PubMed:24854087). During cell cycle progression acts through SCF-dependent proteasomal ubiquitin-dependent protein catabolic process which controls CDKN1B degradation, resulting in positive regulation of cyclins, including CCNE1, CCND1 and CCNB1 (PubMed:24854087). During late neurogenesis, regulates the cerebellar, cerebral cortex and olfactory bulb development through regulation of apoptosis, cell proliferation and cell division (By similarity). Also is required for chromosome congression and alignment during mitotic cell cycle process (PubMed:15843429). Regulates cell spreading, focal adhesion dynamics, and cell migration through its interaction with RADIL resulting in regulation of RAP1A-mediated inside-out integrin activation by tethering RADIL on microtubules (PubMed:23209302). {ECO:0000250|UniProtKB:L0N7N1, ECO:0000269|PubMed:15843429, ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:16648480, ECO:0000269|PubMed:23209302, ECO:0000269|PubMed:24784001, ECO:0000269|PubMed:24854087}.; DISEASE: Meckel syndrome 12 (MKS12) [MIM:616258]: A form of Meckel syndrome, a disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly. {ECO:0000269|PubMed:24128419}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.06815 0.11654 -0.027643533 51.41542817 315.29337 3.77299 KIF15 7.46949818975046e-13 0.999915678862163 8.43211370900205e-05 kinesin family member 15 FUNCTION: Plus-end directed kinesin-like motor enzyme involved in mitotic spindle assembly. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis, colon, thymus and in breast cancer. {ECO:0000269|PubMed:12747765}.; unclassifiable (Anatomical System);islets of Langerhans;colon;blood;skin;bile duct;prostate;whole body;lung;endometrium;larynx;bone;visual apparatus;liver;testis;head and neck;spleen;germinal center;brain;stomach; superior cervical ganglion; 0.37404 0.09484 1.833561474 97.05119132 745.72557 5.41975 KIF16B 4.35337119724975e-13 0.979012252186197 0.0209877478133678 kinesin family member 16B FUNCTION: Plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. Regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. {ECO:0000269|PubMed:15882625}.; . TISSUE SPECIFICITY: Primarily expressed in brain. Also present in kidney, liver, intestine, placenta, leukocytes, heart and skeletal muscle (at protein level). {ECO:0000269|PubMed:15882625}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;breast;lung;adrenal gland;hippocampus;macula lutea;hypopharynx;head and neck;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion; 0.44380 0.11092 0.440820717 77.70110875 982.89337 6.05135 KIF17 3.34364105878855e-13 0.144517331644821 0.855482668354845 kinesin family member 17 FUNCTION: Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B along microtubules. {ECO:0000250}.; . . unclassifiable (Anatomical System);pancreas;lung;frontal lobe;bone;placenta;testis;spleen;blood;brain; whole brain;testis - interstitial;subthalamic nucleus;temporal lobe;pons;atrioventricular node;cingulate cortex; 0.09445 . 0.841339968 88.30502477 1656.47509 7.52374 KIF18A 0.149441082550392 0.850552691258414 6.22619119470851e-06 kinesin family member 18A FUNCTION: Microtubule-depolymerizing kinesin which plays a role in chromosome congression by reducing the amplitude of preanaphase oscillations and slowing poleward movement during anaphase, thus suppressing chromosome movements. May stabilize the CENPE-BUB1B complex at the kinetochores during early mitosis and maintains CENPE levels at kinetochores during chromosome congression. {ECO:0000269|PubMed:17346968, ECO:0000269|PubMed:18267093, ECO:0000269|PubMed:18513970, ECO:0000269|PubMed:19625775}.; . . unclassifiable (Anatomical System);lymph node;ovary;parathyroid;blood;skin;bone marrow;uterus;prostate;lung;endometrium;placenta;liver;testis;cervix;germinal center;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;tumor;testis; 0.52985 0.09395 0.068033485 59.0351498 148.01915 2.65077 KIF18B 8.30836645790731e-05 0.982821946259397 0.017094970076024 kinesin family member 18B FUNCTION: In complex with KIF2C, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells. Its major role may be to transport KIF2C and/or MAPRE1 along microtubules. {ECO:0000269|PubMed:20600703, ECO:0000269|PubMed:21820309}.; . TISSUE SPECIFICITY: Shows a prominent expression in the amygdala. {ECO:0000269|PubMed:20600703}.; unclassifiable (Anatomical System);lymph node;liver;colon;brain; dorsal root ganglion;superior cervical ganglion;pons;trigeminal ganglion;cerebellum; 0.14668 . 0.472145421 78.85114414 245.1338 3.37806 KIF18BP1 . . . kinesin family member 18B pseudogene 1 . . . . . . . . . . . KIF19 5.3712342427336e-13 0.33256861421344 0.667431385786023 kinesin family member 19 FUNCTION: Plus end-directed microtubule-dependent motor protein that regulates the length of motile cilia by mediating depolymerization of microtubules at ciliary tips. {ECO:0000250}.; . . cerebral cortex;hypothalamus;hippocampus;liver;spinal ganglion; . . . 0.056905614 57.56074546 4492.44401 13.45856 KIF20A 1.91703489767524e-08 0.998316596702377 0.00168338412727385 kinesin family member 20A FUNCTION: Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved in recruitment of PLK1 to the central spindle. Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility. {ECO:0000269|PubMed:12939256}.; . . . . 0.43289 0.10799 -0.795417163 12.5324369 169.26622 2.83790 KIF20B 6.54546380494303e-10 0.999999974525903 2.4819550485028e-08 kinesin family member 20B FUNCTION: Plus-end-directed motor enzyme that is required for completion of cytokinesis (PubMed:11470801, PubMed:12740395). Required for proper midbody organization and abscission in polarized cortical stem cells. Plays a role in the regulation of neuronal polarization by mediating the transport of specific cargos. Participates in the mobilization of SHTN1 and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. Involved in cerebral cortex growth (By similarity). Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression (PubMed:17409436). {ECO:0000250|UniProtKB:Q80WE4, ECO:0000269|PubMed:11470801, ECO:0000269|PubMed:12740395, ECO:0000269|PubMed:17409436}.; . TISSUE SPECIFICITY: Brain, ovary, kidney and testis (at protein level) (PubMed:12740395). Overexpressed in bladder cancer cells (at protein level) (PubMed:17409436). Expressed in testis. Overexpressed in bladder cancer cells (PubMed:17409436). {ECO:0000269|PubMed:12740395, ECO:0000269|PubMed:17409436}.; ovary;colon;parathyroid;skin;uterus;oesophagus;bone;thyroid;testis;germinal center;bladder;pineal gland;unclassifiable (Anatomical System);heart;adrenal cortex;blood;skeletal muscle;pancreas;lung;adrenal gland;placenta;liver;duodenum;spleen;cervix;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;temporal lobe;ciliary ganglion;trigeminal ganglion; 0.16495 0.14628 1.960488957 97.55838641 10655.3583 22.46001 KIF21A 6.18012815847982e-05 0.99993819558097 3.1374452867389e-09 kinesin family member 21A FUNCTION: Microtubule-binding motor protein probably involved in neuronal axonal transport. In vitro, has a plus-end directed motor activity (By similarity). {ECO:0000250}.; DISEASE: Fibrosis of extraocular muscles, congenital, 1 (CFEOM1) [MIM:135700]: A congenital ocular motility disorder marked by restrictive ophthalmoplegia affecting extraocular muscles innervated by the oculomotor and/or trochlear nerves. It is clinically characterized by anchoring of the eyes in downward gaze, ptosis, and backward tilt of the head. Patients affected by congenital fibrosis of extraocular muscles type 1 show an absence of the superior division of the oculomotor nerve (cranial nerve III) and corresponding oculomotor subnuclei. {ECO:0000269|PubMed:14595441, ECO:0000269|PubMed:16157808, ECO:0000269|PubMed:17511870, ECO:0000269|PubMed:24715754}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;amygdala;subthalamic nucleus;occipital lobe;superior cervical ganglion;hypothalamus;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex; 0.20921 0.13882 -0.145152788 42.33899505 655.08963 5.13390 KIF21B 0.999414089961557 0.000585910038443189 3.30884019166903e-16 kinesin family member 21B FUNCTION: Microtubule-binding motor protein probably involved in neuronal dendritic transport. In vitro, has a plus-end directed motor activity (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);testis;brain; amygdala;superior cervical ganglion;occipital lobe;fetal brain;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.77280 0.11930 -2.914589271 0.577966502 413.35583 4.25806 KIF22 4.39968359378374e-06 0.990193921970511 0.00980167834589473 kinesin family member 22 FUNCTION: Kinesin family that is involved in spindle formation and the movements of chromosomes during mitosis and meiosis. Binds to microtubules and to DNA.; DISEASE: Spondyloepimetaphyseal dysplasia with joint laxity, 2 (SEMDJL2) [MIM:603546]: A bone disease characterized by short stature, distinctive midface retrusion, progressive knee malalignment (genu valgum and/or varum), generalized ligamentous laxity, and mild spinal deformity. Intellectual development is not impaired. Radiographic characteristics include significantly retarded epiphyseal ossification that evolves into epiphyseal dysplasia and precocious osteoarthritis, metaphyseal irregularities and vertical striations, constricted femoral neck, slender metacarpals and metatarsals, and mild thoracolumbar kyphosis or scoliosis with normal or mild platyspondyly. The most distinctive features for differential diagnosis of SEMDJL2 are the slender metacarpals and phalanges and the progressive degeneration of carpal bones; however, these 2 features are evident only in older children and young adults. The soft consistency of cartilage in the airways leads to laryngotracheomalacia with proneness to respiratory obstruction and inspiratory stridor in infancy and childhood. {ECO:0000269|PubMed:22152677, ECO:0000269|PubMed:22152678}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in bone, cartilage, joint capsule, ligament, skin, and primary cultured chondrocytes. {ECO:0000269|PubMed:22152677}.; lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.14142 0.19084 -0.264476624 34.8844067 226.41241 3.25089 KIF23 0.999999790749235 2.09250765227289e-07 4.71931133205812e-19 kinesin family member 23 FUNCTION: Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Essential for cytokinesis in Rho-mediated signaling. Required for the localization of ECT2 to the central spindle. Plus-end-directed motor enzyme that moves antiparallel microtubules in vitro. {ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:22522702}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;stomach;thymus; superior cervical ganglion; 0.90136 0.11063 -0.108334733 45.57088936 392.17175 4.16785 KIF24 7.56461062195694e-14 0.3778399292896 0.622160070710324 kinesin family member 24 FUNCTION: Microtubule-dependent motor protein that acts as a negative regulator of ciliogenesis by mediating recruitment of CCP110 to mother centriole in cycling cells, leading to restrict nucleation of cilia at centrioles. Mediates depolymerization of microtubules of centriolar origin, possibly to suppress aberrant cilia formation. {ECO:0000269|PubMed:21620453}.; . . lymphoreticular;umbilical cord;ovary;salivary gland;sympathetic chain;developmental;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;bile duct;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;pons;skeletal muscle; 0.47019 . 0.549230812 81.22788393 3029.55018 10.45319 KIF25 3.75351002915501e-09 0.0983683725406008 0.901631623705889 kinesin family member 25 FUNCTION: Negative regulator of amino acid starvation-induced autophagy. {ECO:0000269|PubMed:22354037}.; . . lung;frontal lobe;testis; superior cervical ganglion;cerebellum peduncles;testis;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle;skin; 0.04864 0.08777 1.936492053 97.50530786 587.48576 4.91639 KIF25-AS1 . . . KIF25 antisense RNA 1 . . . . . . . . . . . KIF26A 0.41090369131392 0.589081762603471 1.45460826091138e-05 kinesin family member 26A FUNCTION: Atypical kinesin that plays a key role in enteric neuron development. Acts by repressing a cell growth signaling pathway in the enteric nervous system development, possibly via its interaction with GRB2 that prevents GRB2-binding to SHC, thereby attenating the GDNF-Ret signaling. Binds to microtubules but lacks microtubule-based motility due to the absence of ATPase activity (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;muscle;skin;retina;uterus;pancreas;whole body;lung;placenta;visual apparatus;duodenum;spleen;brain;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.12325 . . . 787.9523 5.54132 KIF26B 0.999987955632678 1.20443672766354e-05 4.51999916582685e-14 kinesin family member 26B FUNCTION: Essential for embryonic kidney development. Plays an important role in the compact adhesion between mesenchymal cells adjacent to the ureteric buds, possibly by interacting with MYH10. This could lead to the establishment of the basolateral integrity of the mesenchyme and the polarized expression of ITGA8, which maintains the GDNF expression required for further ureteric bud attraction. Although it seems to lack ATPase activity it is constitutively associated with microtubules (By similarity). {ECO:0000250}.; . . . . 0.40768 . -0.588263851 18.26492097 1365.91175 6.93300 KIF27 1.3496944348062e-09 0.999872108563371 0.000127890086934403 kinesin family member 27 FUNCTION: Plays an essential role in motile ciliogenesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Testis, pancreatic islet, germ cell tumors and Jurkat T-cells.; unclassifiable (Anatomical System);ovary;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;breast;optic nerve;lung;nasopharynx;placenta;bone;macula lutea;liver;testis;spleen;kidney;brain; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle;skin; 0.07118 0.08861 0.257147149 69.72163246 3803.03299 12.11781 KIF28P . . . kinesin family member 28, pseudogene FUNCTION: Microtubule-dependent motor protein required for mitochondrion morhology and transport of mitochondria in neuronal cells. {ECO:0000250}.; . . . . . . . . . . KIFAP3 0.00197154943265453 0.998020748610313 7.70195703238241e-06 kinesin associated protein 3 FUNCTION: Involved in tethering the chromosomes to the spindle pole and in chromosome movement. Binds to the tail domain of the KIF3A/KIF3B heterodimer to form a heterotrimeric KIF3 complex and may regulate the membrane binding of this complex (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;cerebral cortex;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;spinal cord;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; whole brain;amygdala;testis - interstitial;medulla oblongata;thalamus;occipital lobe;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;testis;globus pallidus;parietal lobe;cerebellum; 0.32433 0.08966 -0.291981272 33.20358575 63.80856 1.63799 KIFC1 0.0155780337232565 0.983296143665597 0.00112582261114674 kinesin family member C1 FUNCTION: Minus end-directed microtubule-dependent motor required for bipolar spindle formation (PubMed:15843429). May contribute to movement of early endocytic vesicles (By similarity). Regulates cilium formation and structure (By similarity). {ECO:0000250|UniProtKB:Q9QWT9, ECO:0000269|PubMed:15843429}.; . . . . 0.37065 . 1.089464986 91.87308327 216.20809 3.17596 KIFC2 0.00134057888635577 0.998331875718534 0.000327545395109812 kinesin family member C2 FUNCTION: May play a role in microtubule-dependent retrograde axonal transport. May function as the motor for the transport of multivesicular body (MVB)-like organelles in dendrites (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;lacrimal gland;hypothalamus;colon;retina;uterus;breast;pancreas;whole body;lung;endometrium;hippocampus;testis;brain;stomach; . 0.54489 0.09921 . . 198.59296 3.04553 KIFC3 0.467893120006523 0.53210497349513 1.90649834651332e-06 kinesin family member C3 FUNCTION: Minus-end microtubule-dependent motor protein. Involved in apically targeted transport (By similarity). Required for zonula adherens maintenance. {ECO:0000250, ECO:0000269|PubMed:19041755}.; . . . . 0.25733 0.09885 -1.815166288 2.164425572 156.96484 2.73707 KIN 0.00322198747938574 0.994527707861238 0.00225030465937661 Kin17 DNA and RNA binding protein FUNCTION: Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro. {ECO:0000250|UniProtKB:Q8K339, ECO:0000269|PubMed:11880372, ECO:0000269|PubMed:12359749, ECO:0000269|PubMed:12754299, ECO:0000269|PubMed:12853634, ECO:0000269|PubMed:15831485, ECO:0000269|PubMed:17045609}.; . TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined, with highest levels in skeletal muscle, heart and testis. Differentially expressed in non-tumorigenic and tumorigenic cell lines. Highly expressed in proliferating epithelial keratinocyte cells in vitro (at protein level). {ECO:0000269|PubMed:10964102, ECO:0000269|PubMed:9266022}.; . . 0.22988 0.23939 -0.405853867 26.23260203 27.69585 0.89027 KIR2DL1 0.184502116558515 0.803684269542589 0.0118136138988961 killer cell immunoglobulin like receptor, two Ig domains and long cytoplasmic tail 1 FUNCTION: Receptor on natural killer (NK) cells for HLA-C alleles. Inhibits the activity of NK cells thus preventing cell lysis. {ECO:0000269|PubMed:18604210}.; . . breast;unclassifiable (Anatomical System);blood; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; . . 1.153790856 92.55720689 905.75657 5.85632 KIR2DL2 . . . killer cell immunoglobulin like receptor, two Ig domains and long cytoplasmic tail 2 FUNCTION: Receptor on natural killer (NK) cells for HLA-Cw1, 3, 7, and 8 allotypes. Inhibits the activity of NK cells thus preventing cell lysis. {ECO:0000269|PubMed:10097129}.; . . . . . . . . . . KIR2DL3 0.0380264991528057 0.929107951909751 0.0328655489374437 killer cell immunoglobulin like receptor, two Ig domains and long cytoplasmic tail 3 FUNCTION: Receptor on natural killer (NK) cells for HLA-C alleles (HLA-Cw1, HLA-Cw3 and HLA-Cw7). Inhibits the activity of NK cells thus preventing cell lysis.; . . . . . . 2.55223346 98.72611465 723.65296 5.34004 KIR2DL4 0.875263421473205 0.123155378409658 0.00158120011713691 killer cell immunoglobulin like receptor, two Ig domains and long cytoplasmic tail 4 FUNCTION: Receptor on natural killer (NK) cells for HLA-C alleles. Inhibits the activity of NK cells thus preventing cell lysis.; . . . . 0.08328 . . . 57.46111 1.52801 KIR2DL5A . . . killer cell immunoglobulin like receptor, two Ig domains and long cytoplasmic tail 5A FUNCTION: Receptor on natural killer (NK) cells for HLA-C alleles. Inhibits the activity of NK cells thus preventing cell lysis.; . . . . . . . . . . KIR2DL5B . . . killer cell immunoglobulin like receptor, two Ig domains and long cytoplasmic tail 5B FUNCTION: Receptor on natural killer (NK) cells for HLA-C alleles. Inhibits the activity of NK cells thus preventing cell lysis.; . . . . . . . . . . KIR2DP1 . . . killer cell immunoglobulin like receptor, two Ig domains pseudogene 1 . . . . . . . . . . . KIR2DS1 . . . killer cell immunoglobulin like receptor, two Ig domains and short cytoplasmic tail 1 FUNCTION: Receptor on natural killer (NK) cells for HLA-C alleles. Does not inhibit the activity of NK cells.; . . . . . . . . . . KIR2DS2 . . . killer cell immunoglobulin like receptor, two Ig domains and short cytoplasmic tail 2 FUNCTION: Receptor on natural killer (NK) cells for HLA-C alleles. Does not inhibit the activity of NK cells.; . . . . 0.19181 . . . . . KIR2DS3 . . . killer cell immunoglobulin like receptor, two Ig domains and short cytoplasmic tail 3 FUNCTION: Receptor on natural killer (NK) cells for HLA-C alleles. Does not inhibit the activity of NK cells.; . . . . . . . . . . KIR2DS4 . . . killer cell immunoglobulin like receptor, two Ig domains and short cytoplasmic tail 4 FUNCTION: Receptor on natural killer (NK) cells for HLA-C alleles. Does not inhibit the activity of NK cells. {ECO:0000269|PubMed:19858347}.; . . breast;blood; subthalamic nucleus;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; . . . . . . KIR2DS5 . . . killer cell immunoglobulin like receptor, two Ig domains and short cytoplasmic tail 5 FUNCTION: Receptor on natural killer (NK) cells for HLA-C alleles. Does not inhibit the activity of NK cells.; . . . . . . . . . . KIR3DL1 9.78327262907819e-06 0.552285382028147 0.447704834699223 killer cell immunoglobulin like receptor, three Ig domains and long cytoplasmic tail 1 FUNCTION: Receptor on natural killer (NK) cells for HLA Bw4 allele. Inhibits the activity of NK cells thus preventing cell lysis. {ECO:0000269|PubMed:22020283}.; . . unclassifiable (Anatomical System);skeletal muscle; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.05806 . 3.335364374 99.43382873 2335.80145 8.95125 KIR3DL2 0.221236755494515 0.770548043277148 0.00821520122833717 killer cell immunoglobulin like receptor, three Ig domains and long cytoplasmic tail 2 FUNCTION: Receptor on natural killer (NK) cells for HLA-A alleles. Inhibits the activity of NK cells thus preventing cell lysis.; . . unclassifiable (Anatomical System); . 0.06359 . . . 331.01777 3.86988 KIR3DL3 0.532094898665216 0.452354816279306 0.0155502850554781 killer cell immunoglobulin like receptor, three Ig domains and long cytoplasmic tail 3 FUNCTION: Receptor on natural killer cells. May inhibit the activity of NK cells thus preventing cell lysis. {ECO:0000303|PubMed:11513144}.; . . blood; superior cervical ganglion;trigeminal ganglion;skeletal muscle; . . . . 362.26283 4.02920 KIR3DP1 . . . killer cell immunoglobulin like receptor, three Ig domains pseudogene 1 . . TISSUE SPECIFICITY: Expressed in peripheral blood cells. {ECO:0000269|PubMed:15580659}.; . . . . . . . . KIR3DS1 . . . killer cell immunoglobulin like receptor, three Ig domains and short cytoplasmic tail 1 FUNCTION: Receptor on natural killer (NK) cells for HLA-C alleles. Does not inhibit the activity of NK cells.; . TISSUE SPECIFICITY: Expressed in NK and T-cell lines but not in B- lymphoblastoid cell lines or in a colon carcinoma cell line.; . . . . . . . . KIR3DX1 . . . killer cell immunoglobulin like receptor, three Ig domains X1 . . TISSUE SPECIFICITY: Expressed in NK-cells. {ECO:0000269|PubMed:16911775}.; unclassifiable (Anatomical System); dorsal root ganglion;occipital lobe;superior cervical ganglion;cerebellum peduncles;adrenal cortex;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.04440 . . . 217.91688 3.19122 KIRREL 0.95946008263139 0.0405391508741434 7.66494466546452e-07 kin of IRRE like (Drosophila) FUNCTION: Plays a significant role in the normal development and function of the glomerular permeability. Signaling protein that needs the presence of TEC kinases to fully trans-activate the transcription factor AP-1 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Abundantly expressed in kidney. Specifically expressed in podocytes of kidney glomeruli. {ECO:0000269|PubMed:11416156}.; unclassifiable (Anatomical System);bile duct;lung;ovary;heart;placenta;colon;kidney;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;thalamus;ciliary ganglion;kidney;caudate nucleus;atrioventricular node;trigeminal ganglion; 0.30283 0.12727 -0.731092527 14.13658882 139.83784 2.57981 KIRREL-IT1 . . . KIRREL intronic transcript 1 . . . . . . . . . . . KIRREL2 8.95380796903671e-06 0.982841684886012 0.0171493613060189 kin of IRRE like 2 (Drosophila) . . TISSUE SPECIFICITY: Highly expressed in beta-cells of the pancreatic islets. {ECO:0000269|PubMed:12837264}.; unclassifiable (Anatomical System);optic nerve;lung;islets of Langerhans;macula lutea;pituitary gland;fovea centralis;choroid;lens;retina; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;trigeminal ganglion; 0.14638 0.11066 0.670564357 84.70158056 2146.80952 8.52308 KIRREL3 0.977505780991965 0.022494041267198 1.77740836942909e-07 kin of IRRE like 3 (Drosophila) FUNCTION: Could be involved in the hematopoietic supportive capacity of stroma cells. {ECO:0000250}.; DISEASE: Mental retardation, autosomal dominant 4 (MRD4) [MIM:612581]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:19012874}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in fetal and adult brain. Also expressed in kidney, specifically in podocytes of kidney glomeruli. {ECO:0000269|PubMed:12424224, ECO:0000269|PubMed:19012874}.; . . 0.10610 . -1.392555112 4.269874971 232.60467 3.29808 KIRREL3-AS1 . . . KIRREL3 antisense RNA 1 . . . . . . . . . . . KIRREL3-AS2 . . . KIRREL3 antisense RNA 2 . . . . . . . . . . . KIRREL3-AS3 . . . KIRREL3 antisense RNA 3 . . . . . 0.17575 . . . . . KISS1 0.524779455234627 0.412573526489423 0.0626470182759497 KiSS-1 metastasis-suppressor FUNCTION: Metastasis suppressor protein in malignant melanomas and in some breast cancers. May regulate events downstream of cell- matrix adhesion, perhaps involving cytoskeletal reorganization. Generates a C-terminally amidated peptide, metastin which functions as the endogenous ligand of the G-protein coupled receptor GPR54. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis. Kp-10 is a decapeptide derived from the primary translation product, isolated in conditioned medium of first trimester trophoblast. Kp-10, but not other kisspeptins, increased intracellular Ca(2+) levels in isolated first trimester trophoblasts. Kp-10 is a paracrine/endocrine regulator in fine- tuning trophoblast invasion generated by the trophoblast itself. The receptor is also essential for normal gonadotropin-released hormone physiology and for puberty. The hypothalamic KiSS1/GPR54 system is a pivotal factor in central regulation of the gonadotropic axis at puberty and in adulthood. {ECO:0000269|PubMed:11060311, ECO:0000269|PubMed:11385580, ECO:0000269|PubMed:15500545, ECO:0000269|PubMed:9185708}.; DISEASE: Hypogonadotropic hypogonadism 13 with or without anosmia (HH13) [MIM:614842]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:22335740}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Very high expression in placenta, with the next highest level in testis and moderate levels in pancreas, liver, small intestine and brain at much lower levels. Expression levels increased in both early placentas and molar pregnancies and are reduced in choriocarcinoma cells. Expressed at higher levels in first trimester trophoblasts than at term of gestation, but only expressed in the villous trophoblast. {ECO:0000269|PubMed:11385580, ECO:0000269|PubMed:12414911, ECO:0000269|PubMed:15020672}.; . . 0.04228 0.15555 . . 2842.33323 10.07797 KISS1R 0.00397107374528621 0.64704714499434 0.348981781260374 KISS1 receptor FUNCTION: Receptor for metastin (kisspeptin-54 or kp-54), a C- terminally amidated peptide of KiSS1. KiSS1 is a metastasis suppressor protein that suppresses metastases in malignant melanomas and in some breast carcinomas without affecting tumorigenicity. The metastasis suppressor properties may be mediated in part by cell cycle arrest and induction of apoptosis in malignant cells. The receptor is essential for normal gonadotropin-released hormone physiology and for puberty. The hypothalamic KiSS1/KISS1R system is a pivotal factor in central regulation of the gonadotropic axis at puberty and in adulthood. The receptor is also probably involved in the regulation and fine- tuning of trophoblast invasion generated by the trophoblast itself. Analysis of the transduction pathways activated by the receptor identifies coupling to phospholipase C and intracellular calcium release through pertussis toxin-insensitive G(q) proteins. {ECO:0000269|PubMed:15020672}.; DISEASE: Hypogonadotropic hypogonadism 8 with or without anosmia (HH8) [MIM:614837]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:12944565, ECO:0000269|PubMed:14573733, ECO:0000269|PubMed:15598687, ECO:0000269|PubMed:17164310, ECO:0000269|PubMed:23643382, ECO:0000269|PubMed:25077900}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. The genetics of hypogonadotropic hypogonadism involves various modes of transmission. Oligogenic inheritance has been reported in some patients carrying mutations in KISS1R as well as in other HH- associated genes including FGFR1 and IL17RD (PubMed:23643382). {ECO:0000269|PubMed:23643382}.; DISEASE: Precocious puberty, central 1 (CPPB1) [MIM:176400]: A condition defined as the development of secondary sexual characteristics in boys and girls at a chronological age that is 2.5 standard deviations below the mean age at onset of puberty in the population. Central precocious puberty results from premature activation of the hypothalamic-pituitary-gonadal axis. {ECO:0000269|PubMed:18272894}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Most highly expressed in the pancreas, placenta and spinal cord, with lower-level of expression in peripheral blood leukocytes, kidney, lung, fetal liver, stomach, small intestine, testes, spleen, thymus, adrenal glands and lymph nodes. In the adult brain, expressed in the superior frontal gyrus, putamen, caudate nucleus, cingulate gyrus, nucleus accumbens, hippocampus, pons and amygdala, as well as the hypothalamus and pituitary. Expression levels are higher in early (7-9 weeks) than term placentas. Expression levels were increased in both early placentas and molar pregnancies and were reduced in choriocarcinoma cells. Expressed at higher levels in first trimester trophoblasts than at term of gestation. Also found in the extravillous trophoblast suggesting endocrine/paracrine activation mechanism. {ECO:0000269|PubMed:11385580, ECO:0000269|PubMed:11387329, ECO:0000269|PubMed:11414709, ECO:0000269|PubMed:11457843, ECO:0000269|PubMed:12414911, ECO:0000269|PubMed:15020672}.; unclassifiable (Anatomical System);placenta;colon;kidney; . 0.11779 0.15982 . . 123.53056 2.41951 KIT 0.999879540537062 0.000120459460441691 2.49611625464124e-12 KIT proto-oncogene receptor tyrosine kinase FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. In response to KITLG/SCF binding, KIT can activate several signaling pathways. Phosphorylates PIK3R1, PLCG1, SH2B2/APS and CBL. Activates the AKT1 signaling pathway by phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Activated KIT also transmits signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3, STAT5A and STAT5B. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KIT signaling is modulated by protein phosphatases, and by rapid internalization and degradation of the receptor. Activated KIT promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II), LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1. {ECO:0000269|PubMed:10397721, ECO:0000269|PubMed:12444928, ECO:0000269|PubMed:12511554, ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:17904548, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:21640708, ECO:0000269|PubMed:7520444, ECO:0000269|PubMed:9528781}.; DISEASE: Piebald trait (PBT) [MIM:172800]: Autosomal dominant genetic developmental abnormality of pigmentation characterized by congenital patches of white skin and hair that lack melanocytes. {ECO:0000269|PubMed:11074500, ECO:0000269|PubMed:1370874, ECO:0000269|PubMed:1376329, ECO:0000269|PubMed:1717985, ECO:0000269|PubMed:7687267, ECO:0000269|PubMed:8680409, ECO:0000269|PubMed:9450866, ECO:0000269|PubMed:9699740}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Gastrointestinal stromal tumor (GIST) [MIM:606764]: Common mesenchymal neoplasms arising in the gastrointestinal tract, most often in the stomach. They are histologically, immunohistochemically, and genetically different from typical leiomyomas, leiomyosarcomas, and schwannomas. Most GISTs are composed of a fairly uniform population of spindle-shaped cells. Some tumors are dominated by epithelioid cells or contain a mixture of spindle and epithelioid morphologies. Primary GISTs in the gastrointestinal tract commonly metastasize in the omentum and mesenteries, often as multiple nodules. However, primary tumors may also occur outside of the gastrointestinal tract, in other intra-abdominal locations, especially in the omentum and mesentery. {ECO:0000269|PubMed:11505412, ECO:0000269|PubMed:15824741, ECO:0000269|PubMed:9438854, ECO:0000269|PubMed:9697690}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Testicular germ cell tumor (TGCT) [MIM:273300]: A common malignancy in males representing 95% of all testicular neoplasms. TGCTs have various pathologic subtypes including: unclassified intratubular germ cell neoplasia, seminoma (including cases with syncytiotrophoblastic cells), spermatocytic seminoma, embryonal carcinoma, yolk sac tumor, choriocarcinoma, and teratoma. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. Note=The gene represented in this entry is involved in disease pathogenesis. Somatic mutations that lead to constitutive activation of KIT are detected in AML patients. These mutations fall into two classes, the most common being in-frame internal tandem duplications of variable length in the juxtamembrane region that disrupt the normal regulation of the kinase activity. Likewise, point mutations in the kinase domain can result in a constitutively activated kinase.; TISSUE SPECIFICITY: Isoform 1 and isoform 2 are detected in spermatogonia and Leydig cells. Isoform 3 is detected in round spermatids, elongating spermatids and spermatozoa (at protein level). Widely expressed. Detected in the hematopoietic system, the gastrointestinal system, in melanocytes and in germ cells. {ECO:0000269|PubMed:20601678, ECO:0000269|PubMed:2448137}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;cochlea;endometrium;thyroid;testis;pineal gland;brain;gall bladder;unclassifiable (Anatomical System);heart;cartilage;urinary;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;kidney;peripheral nerve; thalamus;thyroid; 0.43921 0.15300 -0.683363435 15.36329323 213.06132 3.15066 KITLG 0.508530401642626 0.487441483992909 0.00402811436446538 KIT ligand FUNCTION: Ligand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5- trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins.; DISEASE: Hyperpigmentation with or without hypopigmentation, familial progressive (FPHH) [MIM:145250]: A disorder characterized by hyperpigmented patches in the skin, present in early infancy and increasing in size and number with age. Hyperpigmentation has variable intensity, and sometimes is associated with cafe-au-lait macules and larger hypopigmented ash-leaf macules. {ECO:0000269|PubMed:19375057}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);prostate;whole body;skeletal muscle; medulla oblongata;superior cervical ganglion;tongue;appendix;ciliary ganglion;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.26732 0.80094 -0.183570861 39.95046001 47.03064 1.32630 KIZ . . . kizuna centrosomal protein FUNCTION: Centrosomal protein required for establishing a robust mitotic centrosome architecture that can endure the forces that converge on the centrosomes during spindle formation. Required for stabilizing the expanded pericentriolar material around the centriole. {ECO:0000269|PubMed:16980960}.; DISEASE: Retinitis pigmentosa 69 (RP69) [MIM:615780]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:24680887}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.03855 0.06663 . . . . KIZ-AS1 . . . KIZ antisense RNA 1 . . . . . . . . . . . KL 1.95267033273788e-05 0.972984941152301 0.0269955321443712 klotho FUNCTION: May have weak glycosidase activity towards glucuronylated steroids. However, it lacks essential active site Glu residues at positions 239 and 872, suggesting it may be inactive as a glycosidase in vivo. May be involved in the regulation of calcium and phosphorus homeostasis by inhibiting the synthesis of active vitamin D (By similarity). Essential factor for the specific interaction between FGF23 and FGFR1 (By similarity). {ECO:0000250}.; DISEASE: Tumoral calcinosis, hyperphosphatemic, familial (HFTC) [MIM:211900]: A severe metabolic disorder that manifests with hyperphosphatemia and massive calcium deposits in the skin and subcutaneous tissues. Some patients manifest recurrent, transient, painful swellings of the long bones associated with the radiographic findings of periosteal reaction and cortical hyperostosis and absence of skin involvement. {ECO:0000269|PubMed:17710231}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Present in cortical renal tubules (at protein level). Soluble peptide is present in serum and cerebrospinal fluid. Expressed in kidney, placenta, small intestine and prostate. Down-regulated in renal cell carcinomas, hepatocellular carcinomas, and in chronic renal failure kidney. {ECO:0000269|PubMed:10631108, ECO:0000269|PubMed:11043382, ECO:0000269|PubMed:11162628, ECO:0000269|PubMed:15135068, ECO:0000269|PubMed:9464267}.; . . 0.25552 0.49338 0.009173042 54.15782024 2673.80912 9.72427 KLB 0.0944730785192823 0.905512911954703 1.40095260143069e-05 klotho beta FUNCTION: Contributes to the transcriptional repression of cholesterol 7-alpha-hydroxylase (CYP7A1), the rate-limiting enzyme in bile acid synthesis. Probably inactive as a glycosidase. Increases the ability of FGFR1 and FGFR4 to bind FGF21 (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);liver;testis;spleen;mammary gland; superior cervical ganglion;trigeminal ganglion;parietal lobe; 0.22179 0.09831 0.339867479 73.7084218 1250.15924 6.67352 KLC1 0.51495533247325 0.485012288667326 3.23788594244359e-05 kinesin light chain 1 FUNCTION: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity.; . TISSUE SPECIFICITY: Found in a variety of tissues. Mostly abundant in brain and spine. {ECO:0000269|PubMed:14970196}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;optic nerve;frontal lobe;endometrium;thyroid;bone;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;hypopharynx;head and neck;cervix;stomach;cerebellum; amygdala;whole brain;dorsal root ganglion;thalamus;occipital lobe;medulla oblongata;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;atrioventricular node;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.22060 0.15408 -0.492218069 22.35786742 40.10824 1.17876 KLC2 0.997255173219259 0.00274482169957608 5.08116487617883e-09 kinesin light chain 2 FUNCTION: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity). {ECO:0000250}.; . . lymphoreticular;medulla oblongata;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;islets of Langerhans;muscle;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;stomach; amygdala;whole brain;medulla oblongata;subthalamic nucleus;cerebellum peduncles;temporal lobe;prefrontal cortex;caudate nucleus;pons;parietal lobe;cingulate cortex;cerebellum; 0.26457 0.11794 -0.933156985 9.54824251 1400.40421 6.99592 KLC3 3.15849310261577e-06 0.782705685255001 0.217291156251897 kinesin light chain 3 FUNCTION: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport.; . . . . 0.15574 0.13481 . . 169.71455 2.84217 KLC4 0.236002384577825 0.7639368734927 6.07419294754766e-05 kinesin light chain 4 FUNCTION: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity). {ECO:0000250}.; . . medulla oblongata;smooth muscle;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;pineal body;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.28613 0.10355 -0.262657925 34.93158764 230.66269 3.28293 KLF1 0.000201077104049452 0.485470374734123 0.514328548161827 Kruppel-like factor 1 (erythroid) FUNCTION: Transcription regulator of erythrocyte development that probably serves as a general switch factor during erythropoiesis. Is a dual regulator of fetal-to-adult globin switching. Binds to the CACCC box in the beta-globin gene promoter and acts as a preferential activator of this gene. Furthermore, it binds to the BCL11A promoter and activates expression of BCL11A, which in turn represses the HBG1 and HBG2 genes. This dual activity ensures that, in most adults, fetal hemoglobin levels are low. Able to activate CD44 and AQP1 promoters. When sumoylated, acts as a transcriptional repressor by promoting interaction with CDH2/MI2beta and also represses megakaryocytic differentiation. {ECO:0000250|UniProtKB:P46099, ECO:0000269|PubMed:25585695}.; DISEASE: Anemia, congenital dyserythropoietic, 4 (CDAN4) [MIM:613673]: A blood disorder characterized by ineffective erythropoiesis and hemolysis resulting in anemia. Circulating erythroblasts and erythroblasts in the bone marrow show various morphologic abnormalities. Affected individuals with CDA4 also have increased levels of fetal hemoglobin. {ECO:0000269|PubMed:21055716, ECO:0000269|PubMed:25585695}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expression restricted to adult bone marrow and fetal liver. Not expressed in myeloid nor lymphoid cell lines. {ECO:0000269|PubMed:8924208, ECO:0000269|PubMed:9119377}.; uterus;lung;heart;liver;colon;spleen;blood;brain;skin; superior cervical ganglion;fetal liver;skeletal muscle;bone marrow; 0.79306 0.13388 . . 2015.45625 8.26537 KLF2 0.741705189487728 0.247333223117687 0.0109615873945853 Kruppel-like factor 2 FUNCTION: Transcription factor that binds to the CACCC box in the promoter of target genes such as HBB/beta globin or NOV and activates their transcription. {ECO:0000269|PubMed:21063504}.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;sympathetic chain;colon;parathyroid;blood;skin;pancreas;lung;placenta;testis;cervix;germinal center;kidney;brain;stomach; superior cervical ganglion;white blood cells;trigeminal ganglion;whole blood; 0.09706 . . . 16.89756 0.59498 KLF2P1 . . . Kruppel-like factor 2 pseudogene 1 . . . . . . . . . . . KLF2P2 . . . Kruppel-like factor 2 pseudogene 2 . . . . . . . . . . . KLF2P3 . . . Kruppel-like factor 2 pseudogene 3 . . . . . . . . . . . KLF2P4 . . . Kruppel-like factor 2 pseudogene 4 . . . . . . . . . . . KLF3 0.800390629045236 0.198446528681798 0.00116284227296619 Kruppel-like factor 3 (basic) FUNCTION: Binds to the CACCC box of erythroid cell-expressed genes. May play a role in hematopoiesis (By similarity). {ECO:0000250}.; . . ovary;colon;skin;retina;bone marrow;uterus;prostate;larynx;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;placenta;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; kidney; 0.23149 0.11262 -0.736552314 13.93606983 21.33351 0.72028 KLF3-AS1 . . . KLF3 antisense RNA 1 . . . . . . . . . . . KLF3P1 . . . Kruppel-like factor 3 (basic) pseudogene 1 . . . . . . . . . . . KLF3P2 . . . Kruppel-like factor 3 (basic) pseudogene 2 . . . . . . . . . . . KLF4 0.981049995653145 0.0189359728022139 1.4031544641519e-05 Kruppel-like factor 4 (gut) FUNCTION: Transcription factor; can act both as activator and as repressor. Binds the 5'-CACCC-3' core sequence. Binds to the promoter region of its own gene and can activate its own transcription. Regulates the expression of key transcription factors during embryonic development. Plays an important role in maintaining embryonic stem cells, and in preventing their differentiation. Required for establishing the barrier function of the skin and for postnatal maturation and maintenance of the ocular surface. Involved in the differentiation of epithelial cells and may also function in skeletal and kidney development. Contributes to the down-regulation of p53/TP53 transcription. {ECO:0000269|PubMed:17308127, ECO:0000269|PubMed:20071344}.; . . . . 0.84018 0.40812 -0.448125345 24.19202642 53.32293 1.45041 KLF4P1 . . . Kruppel-like factor 4 (gut) pseudogene 1 . . . . . . . . . . . KLF5 0.871983359183675 0.127665511141587 0.000351129674737321 Kruppel-like factor 5 (intestinal) FUNCTION: Transcription factor that binds to GC box promoter elements. Activates the transcription of these genes.; . TISSUE SPECIFICITY: Expressed only in testis and placenta.; . . 0.76762 0.22337 -0.049474214 50.01179523 93.82432 2.08324 KLF6 0.925053295453051 0.0745171719012185 0.000429532645730356 Kruppel-like factor 6 FUNCTION: Transcriptional activator (By similarity). Binds a GC box motif. Could play a role in B-cell growth and development. {ECO:0000250}.; DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease. {ECO:0000269|PubMed:15824733}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Prostate cancer (PC) [MIM:176807]: A malignancy originating in tissues of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma. {ECO:0000269|PubMed:11752579}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in placenta followed by spleen, thymus, prostate, testis, small intestine and colon. Weakly expressed in pancreas, lung, liver, heart and skeletal muscle. Also expressed in fetal brain, spleen and thymus.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;oesophagus;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; dorsal root ganglion;olfactory bulb;lung;ciliary ganglion;white blood cells;atrioventricular node;trigeminal ganglion;skin;parietal lobe;skeletal muscle; 0.79945 0.32101 -0.073340031 48.11866006 79.62791 1.88582 KLF7 0.92993070889515 0.0697069431074503 0.000362347997400136 Kruppel-like factor 7 (ubiquitous) FUNCTION: Transcriptional activator. Binds in vitro to the CACCC motif of the beta-globin promoter and to the SP1 recognition sequence.; . TISSUE SPECIFICITY: Ubiquitous and highly expressed in brain and spinal cord in the adult, and in kidney and brain in the embryo.; unclassifiable (Anatomical System);cartilage;heart;colon;blood;skin;skeletal muscle;bone marrow;breast;uterus;lung;thyroid;placenta;liver;testis;amniotic fluid;head and neck;spleen;cervix;spinal ganglion;brain; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle;cerebellum; 0.73061 0.12095 -0.427900189 25.14744043 17.99179 0.62821 KLF7-IT1 . . . KLF7 intronic transcript 1 . . . . . . . . . . . KLF7P1 . . . kruppel-like factor 7 pseudogene 1 . . . . . . . . . . . KLF8 0.027862422377185 0.797273401807128 0.174864175815687 Kruppel-like factor 8 FUNCTION: Transcriptional repressor and activator. Binds to CACCC- boxes promoter elements. Also binds the GT-box of cyclin D1 promoter and mediates cell cycle progression at G(1) phase as a downstream target of focal adhesion kinase (FAK). {ECO:0000269|PubMed:10756197, ECO:0000269|PubMed:12820964, ECO:0000269|PubMed:16617055}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10756197}.; unclassifiable (Anatomical System);lymph node;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;optic nerve;lung;endometrium;larynx;nasopharynx;placenta;bone;macula lutea;testis;head and neck;kidney;brain;bladder; . 0.12318 0.06771 0.170987912 65.5579146 51.54272 1.41736 KLF8P1 . . . Kruppel-like factor 8 pseudogene 1 . . . . . . . . . . . KLF9 0.882452241010758 0.116191596721685 0.00135616226755676 Kruppel-like factor 9 FUNCTION: Transcription factor that binds to GC box promoter elements. Selectively activates mRNA synthesis from genes containing tandem repeats of GC boxes but represses genes with a single GC box. Acts as an epidermal circadian transcription factor regulating keratinocyte proliferation (PubMed:22711835). {ECO:0000269|PubMed:22711835}.; . TISSUE SPECIFICITY: Epidermis (at protein level). {ECO:0000269|PubMed:22711835}.; . . 0.99417 0.17365 0.347360312 73.97381458 40.41538 1.18634 KLF10 0.00342176655842149 0.834210438057833 0.162367795383746 Kruppel-like factor 10 FUNCTION: Transcriptional repressor which binds to the consensus sequence 5'-GGTGTG-3'. Plays a role in the regulation of the circadian clock; binds to the GC box sequence in the promoter of the core clock component ARTNL/BMAL1 and represses its transcriptional activity. Regulates the circadian expression of genes involved in lipogenesis, gluconeogenesis, and glycolysis in the liver. Represses the expression of PCK2, a rate-limiting step enzyme of gluconeogenesis (By similarity). May play a role in the cell cycle regulation. {ECO:0000250|UniProtKB:O89091, ECO:0000269|PubMed:8584037}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;gall bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; placenta;trigeminal ganglion; 0.62417 0.17296 0.374860183 75.43052607 239.0998 3.34100 KLF11 0.00111669037367127 0.834661225671721 0.164222083954608 Kruppel-like factor 11 FUNCTION: Transcription factor (PubMed:9748269, PubMed:10207080). Activates the epsilon- and gamma-globin gene promoters and, to a much lower degree, the beta-globin gene and represses promoters containing SP1-like binding inhibiting cell growth (PubMed:9748269, PubMed:10207080, PubMed:16131492). Represses transcription of SMAD7 which enhances TGF-beta signaling (By similarity). Induces apoptosis (By similarity). {ECO:0000250|UniProtKB:Q8K1S5, ECO:0000269|PubMed:10207080, ECO:0000269|PubMed:16131492}.; DISEASE: Maturity-onset diabetes of the young 7 (MODY7) [MIM:610508]: A form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease. {ECO:0000269|PubMed:15774581}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Higher expression in erythroid cells. {ECO:0000269|PubMed:10207080}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;bile duct;breast;lung;placenta;macula lutea;visual apparatus;liver;duodenum;alveolus;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion; 0.10813 0.12972 0.246221394 69.56829441 362.54594 4.03145 KLF12 0.982233162437981 0.0177548640073833 1.19735546353705e-05 Kruppel-like factor 12 FUNCTION: Confers strong transcriptional repression to the AP-2- alpha gene. Binds to a regulatory element (A32) in the AP-2-alpha gene promoter.; . . unclassifiable (Anatomical System);liver;spleen;blood;brain;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;uterus corpus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.86418 0.11566 -0.492218069 22.35786742 50.62728 1.40047 KLF13 0.629113650372402 0.34061263363776 0.030273715989838 Kruppel-like factor 13 FUNCTION: Represses transcription by binding to the BTE site, a GC-rich DNA element, in competition with the activator SP1. It also represses transcription by interacting with the corepressor Sin3A and HDAC1. Activates RANTES expression in T-cells. {ECO:0000269|PubMed:11477107}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;thymus; white blood cells;cingulate cortex;thymus; 0.89654 . . . 64.64844 1.64933 KLF14 0.21811382303303 0.647727035125632 0.134159141841338 Kruppel-like factor 14 . . . testis; superior cervical ganglion; 0.41888 . . . 2246.7996 8.75017 KLF15 0.435175998587426 0.533765089669094 0.03105891174348 Kruppel-like factor 15 FUNCTION: Transcriptional regulator that binds to the GA element of the CLCNKA promoter. Binds to the KCNIP2 promoter and regulates KCNIP2 circadian expression in the heart (By similarity). Is a repressor of CTGF expression, involved in the control of cardiac fibrosis. It is also involved in the control of cardiac hypertrophy acting through the inhibition of MEF2A and GATA4 (By similarity). Involved in podocyte differentiation (By similarity). Inhibits MYOCD activity. Is a negative regulator of TP53 acetylation. Inhibits NF-kappa-B activation through repression of EP300-dependent RELA acetylation. {ECO:0000250, ECO:0000269|PubMed:18586263, ECO:0000269|PubMed:20375365, ECO:0000269|PubMed:20566642, ECO:0000269|PubMed:23999430}.; DISEASE: Note=KLF15 deficiency results in loss of rhythmic QT variation and abnormal heart repolarization (PubMed:22367544). It may play a role in susceptibility to ventricular arrhythmias (PubMed:22367544), and development of pathological cardiac hypertrophy leading to heart failure (PubMed:20375365). {ECO:0000269|PubMed:20375365, ECO:0000269|PubMed:22367544}.; TISSUE SPECIFICITY: Highly expressed in liver, skeletal muscle, and kidney. Expressed in cardiomyocytes. Expression is highly reduced in cardiac tissue of patients with non-ischemic cardiomyopathy and aortic aneurysm, and in glomerular disease. Not expressed in bone marrow or lymphoid tissues. {ECO:0000269|PubMed:10982849, ECO:0000269|PubMed:17438289, ECO:0000269|PubMed:20375365, ECO:0000269|PubMed:22493483}.; unclassifiable (Anatomical System);choroid;fovea centralis;lens;skin;retina;uterus;optic nerve;placenta;macula lutea;kidney;spinal ganglion;brain;stomach; superior cervical ganglion;pons; 0.38172 0.14204 -0.670411825 15.61689078 27.49319 0.88509 KLF16 0.473218601321024 0.441203064762736 0.0855783339162408 Kruppel-like factor 16 FUNCTION: Transcription factor that binds GC and GT boxes and displaces Sp1 and Sp3 from these sequences. Modulates dopaminergic transmission in the brain (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;skin;retina;uterus;prostate;optic nerve;oesophagus;thyroid;bone;testis;spinal ganglion;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pharynx;blood;breast;pancreas;lung;visual apparatus;liver;kidney; dorsal root ganglion;occipital lobe;superior cervical ganglion;temporal lobe;pons;caudate nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.31168 . . . 205.09035 3.09415 KLF17 4.24588312614059e-09 0.0559412618797664 0.94405873387435 Kruppel-like factor 17 FUNCTION: Transcription repressor that binds to the promoter of target genes and prevents their expression. Acts as a negative regulator of epithelial-mesenchymal transition and metastasis in breast cancer. Specifically binds the 5'-CACCC-3' sequence in the promoter of ID1, a key metastasis regulator in breast cancer, and repress its expression. May be a germ cell-specific transcription factor that plays important roles in spermatid differentiation and oocyte development (By similarity). {ECO:0000250, ECO:0000269|PubMed:16460907}.; . . . . 0.04795 0.07008 0.066214104 58.95848077 2734.62808 9.85543 KLF17P1 . . . Kruppel-like factor 17 pseudogene 1 . . . . . . . . . . . KLF17P2 . . . Kruppel-like factor 17 pseudogene 2 . . . . . . . . . . . KLF18 . . . Kruppel-like factor 18 . . . . . . . . . . . KLHDC1 0.000148222869695322 0.992231316168544 0.00762046096176014 kelch domain containing 1 . . TISSUE SPECIFICITY: Widely expressed, with high levels in skeletal muscle, pancreas and liver. Undetectable in peripheral blood leukocytes. {ECO:0000269|PubMed:16964437}.; unclassifiable (Anatomical System);endometrium;islets of Langerhans;hypothalamus;pituitary gland;kidney;brain;skeletal muscle; . 0.54958 0.10540 -0.514264485 21.41424864 23.90691 0.78817 KLHDC2 0.157958962045693 0.841365121730839 0.000675916223467845 kelch domain containing 2 FUNCTION: Represses CREB3-mediated transcription by interfering with CREB3-DNA binding. {ECO:0000269|PubMed:11384994}.; . TISSUE SPECIFICITY: Widely expressed, with high levels in skeletal muscle, heart, pancreas and liver. Undetectable in peripheral blood leukocytes. {ECO:0000269|PubMed:11384994, ECO:0000269|PubMed:16964437}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;germinal center;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;vein;uterus;whole body;oesophagus;larynx;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; amygdala;medulla oblongata;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;testis;pons;cingulate cortex; 0.22342 0.14429 -0.758599262 13.32861524 79.87599 1.88856 KLHDC3 0.993829271351028 0.00616983173311697 8.96915855036746e-07 kelch domain containing 3 FUNCTION: May be involved in meiotic recombination process.; . . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;bone;testis;dura mater;unclassifiable (Anatomical System);lymph node;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;duodenum;kidney;stomach; whole brain;amygdala;occipital lobe;testis - interstitial;superior cervical ganglion;medulla oblongata;cerebellum peduncles;temporal lobe;pons;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.38180 0.27312 -0.383807564 27.41802312 6.97248 0.25988 KLHDC4 3.7052834500335e-19 0.000176598977747038 0.999823401022253 kelch domain containing 4 . . . medulla oblongata;ovary;colon;vein;skin;bone marrow;prostate;thyroid;bone;tonsil;unclassifiable (Anatomical System);cartilage;tongue;blood;bile duct;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.26115 0.10224 1.078370636 91.75513093 1623.0511 7.44905 KLHDC7A 2.58274593353359e-10 0.0401533632584768 0.959846636483249 kelch domain containing 7A . . . . . 0.29525 . 3.140446476 99.29228592 4901.74622 14.27407 KLHDC7B 0.000573066841521424 0.710411172382127 0.289015760776351 kelch domain containing 7B . . . . . 0.08097 . . . 3709.14161 11.88205 KLHDC8A 1.5912847668424e-05 0.658374530747989 0.341609556404342 kelch domain containing 8A . . . . . 0.16487 . -1.111360919 6.717386176 35.46193 1.07059 KLHDC8B 0.010421420264697 0.829598176959372 0.159980402775931 kelch domain containing 8B . DISEASE: Lymphoma, Hodgkin, classic (CHL) [MIM:236000]: A malignant disease characterized by progressive enlargement of the lymph nodes, spleen and general lymphoid tissue, and the presence of large, usually multinucleate, cells (Reed-Sternberg cells). Reed-Sternberg cells compose only 1-2% of the total tumor cell mass. The remainder is composed of a variety of reactive, mixed inflammatory cells consisting of lymphocytes, plasma cells, neutrophils, eosinophils and histiocytes. {ECO:0000269|PubMed:19706467}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. A variant in the 5'-UTR of KLHDC8B, responsible for decreasing its expression, is associated with classic Hodgkin lymphoma and segregates with the disease in some families (PubMed:19706467). {ECO:0000269|PubMed:19706467}.; DISEASE: Note=A chromosomal aberration disrupting KLHDC8B has been found in a family with the nodular sclerosis type of Hodgkin lymphoma. Translocation t(2,3)(q11.2;p21.31).; . medulla oblongata;ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;cerebral cortex;thyroid;bone;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;adrenal cortex;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;kidney;mammary gland; superior cervical ganglion;adrenal gland;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.29894 0.10946 -0.626318434 17.03231894 17.04371 0.59957 KLHDC9 5.36703786259885e-06 0.428527270232529 0.571467362729608 kelch domain containing 9 . . . . . 0.12036 0.08730 0.749657564 86.56522765 450.73191 4.41046 KLHDC10 0.996683789589299 0.00331617057556954 3.9835131727527e-08 kelch domain containing 10 FUNCTION: Participates in the oxidative stress-induced cell death through MAP3K5 activation. Inhibits PPP5C phosphatase activity on MAP3K5. {ECO:0000269|PubMed:23102700}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;optic nerve;whole body;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney; superior cervical ganglion;testis; . 0.11262 -0.251530012 35.42108988 93.6391 2.08180 KLHL1 0.00808344241005034 0.991320552123356 0.000596005466593396 kelch like family member 1 FUNCTION: May play a role in organizing the actin cytoskeleton of the brain cells.; . TISSUE SPECIFICITY: Highly expressed in brain.; . . 0.20894 0.13823 -0.442665927 24.53408823 90.47611 2.04715 KLHL2 0.99855485686333 0.00144513788344394 5.25322595834775e-09 kelch like family member 2 FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, such as NPTXR, leading most often to their proteasomal degradation (By similarity). Responsible for degradative ubiquitination of the WNK kinases WNK1, WNK3 and WNK4. Plays a role in the reorganization of the actin cytoskeleton. Promotes growth of cell projections in oligodendrocyte precursors. {ECO:0000250, ECO:0000269|PubMed:15715669, ECO:0000269|PubMed:23838290}.; . TISSUE SPECIFICITY: Ubiquitous. Detected throughout the brain. {ECO:0000269|PubMed:10397770}.; fovea centralis;choroid;retina;bone marrow;optic nerve;atrium;whole body;thyroid;testis;germinal center;artery;bladder;brain;unclassifiable (Anatomical System);amygdala;cartilage;hypothalamus;blood;lens;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;stomach;aorta; amygdala;whole brain;occipital lobe;medulla oblongata;superior cervical ganglion;subthalamic nucleus;prefrontal cortex;globus pallidus;caudate nucleus;pons;cingulate cortex;parietal lobe; 0.17076 0.16542 0.17280645 65.75843359 44.32914 1.27120 KLHL2P1 . . . kelch like family member 2 pseudogene 1 . . . . . . . . . . . KLHL3 0.924154761446343 0.0758415188204071 3.71973325002462e-06 kelch like family member 3 FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of ion transport in the distal nephron. The BCR(KLHL3) complex acts by mediating ubiquitination of WNK4, an inhibitor of potassium channel KCNJ1, leading to WNK4 degradation. {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:22406640, ECO:0000269|PubMed:23387299, ECO:0000269|PubMed:23453970, ECO:0000269|PubMed:23576762, ECO:0000269|PubMed:23665031}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:22406640}.; unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;skin;skeletal muscle;retina;uterus;whole body;lung;frontal lobe;endometrium;bone;thyroid;placenta;hippocampus;liver;testis;spleen;germinal center;kidney;brain;cerebellum; cerebellum peduncles;cerebellum; 0.28841 0.11001 -0.868835007 10.65109696 39.76309 1.17177 KLHL4 0.872766936888335 0.127162784235703 7.02788759628048e-05 kelch like family member 4 . . TISSUE SPECIFICITY: Expressed in adult fibroblasts and in a range of fetal tissues including tongue, palate, and mandible.; . . 0.40880 0.08583 -0.359940251 28.93371078 19.51878 0.66973 KLHL5 0.00136508018518131 0.997062601625655 0.00157231818916404 kelch like family member 5 . . TISSUE SPECIFICITY: Expressed in adrenal gland, ovary and thyroid gland and less abundantly in lymph node, prostate, spinal chord, testis and trachea.; ovary;developmental;colon;parathyroid;skin;uterus;prostate;frontal lobe;endometrium;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;skeletal muscle;breast;lung;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;globus pallidus;skeletal muscle; 0.61796 . -0.156065314 42.16206653 90.57721 2.04858 KLHL6 3.42666879196839e-06 0.797610641006917 0.202385932324291 kelch like family member 6 FUNCTION: Involved in B-lymphocyte antigen receptor signaling and germinal center formation. {ECO:0000250}.; . TISSUE SPECIFICITY: Found in germinal center B-cells. {ECO:0000269|PubMed:12617994}.; unclassifiable (Anatomical System);lymph node;ovary;placenta;parathyroid;germinal center;skeletal muscle; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.22527 0.11012 -0.907472583 10.07313046 190.44155 2.99478 KLHL6-AS1 . . . KLHL6 antisense RNA 1 . . . . . . . . . . . KLHL7 0.000319112118508392 0.997116372367919 0.00256451551357255 kelch like family member 7 FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. The BCR(KLHL7) complex acts by mediating ubiquitination and subsequent degradation of substrate proteins. Probably mediates 'Lys-48'-linked ubiquitination. {ECO:0000269|PubMed:21828050}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in adult and fetal heart, CNS and adult testis. {ECO:0000269|PubMed:16918702}.; myocardium;medulla oblongata;ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;larynx;bone;thyroid;pituitary gland;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;macula lutea;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.32974 0.12245 -0.758599262 13.32861524 16.38262 0.58049 KLHL7-AS1 . . . KLHL7 antisense RNA 1 (head to head) . . . . . . . . . . . KLHL8 0.00120835097187105 0.996919083905129 0.00187256512300034 kelch like family member 8 FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for The BCR(KLHL8) ubiquitin ligase complex mediates ubiquitination and degradation of RAPSN. {ECO:0000269|PubMed:19158078}.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;pituitary gland;testis;dura mater;germinal center;brain;pineal gland;unclassifiable (Anatomical System);meninges;heart;cartilage;cerebellum cortex;islets of Langerhans;urinary;adrenal cortex;skeletal muscle;breast;pia mater;lung;adrenal gland;placenta;visual apparatus;stomach; . 0.11818 0.10561 -0.690637458 15.12149092 27.79892 0.89272 KLHL9 0.988339534912071 0.0116562072791034 4.25780882524309e-06 kelch like family member 9 FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex mediates the ubiquitination of AURKB and controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:17543862, ECO:0000269|PubMed:19995937}.; . . unclassifiable (Anatomical System);lymph node;colon;skin;uterus;prostate;lung;frontal lobe;larynx;placenta;thyroid;visual apparatus;head and neck;kidney;mammary gland;stomach; medulla oblongata;superior cervical ganglion;prefrontal cortex;globus pallidus;skeletal muscle; 0.18274 0.11262 -0.247889024 35.98726115 98.57526 2.14575 KLHL10 0.931027664206448 0.0689011845185058 7.11512750464398e-05 kelch like family member 10 FUNCTION: May be a substrate-specific adapter of a CUL3-based E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins during spermatogenesis.; DISEASE: Spermatogenic failure 11 (SPGF11) [MIM:615081]: An infertility disorder caused by spermatogenesis defects. It results in decreased sperm motility, concentration, and multiple sperm structural defects. Oligozoospermia is usually observed in SPGF11 patients. In addition to oligozoospermia, teratozoospermia and moderate asthenozoospermia is observed in some cases. {ECO:0000269|PubMed:17047026}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);medulla oblongata;lung;testis; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.51675 0.11055 -0.025608647 51.91672564 80.82857 1.89990 KLHL11 0.0534677757011955 0.942312828595404 0.00421939570340068 kelch like family member 11 FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;whole body;liver;testis;pineal gland;skeletal muscle; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.42240 0.11262 -0.159704656 41.90846898 52.28961 1.42876 KLHL12 0.00808698785950803 0.988986222431729 0.00292678970876295 kelch like family member 12 FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a negative regulator of Wnt signaling pathway and ER-Golgi transport. The BCR(KLHL12) complex is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B). As part of the BCR(KLHL12) complex, also acts as a negative regulator of the Wnt signaling pathway by mediating ubiquitination and subsequent proteolysis of DVL3. The BCR(KLHL12) complex also mediates polyubiquitination of DRD4, without leading to degradation of DRD4. {ECO:0000269|PubMed:16547521, ECO:0000269|PubMed:18303015, ECO:0000269|PubMed:20100572, ECO:0000269|PubMed:22358839}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in testis and at lower levels in the submandibular salivary gland. {ECO:0000269|PubMed:15383316, ECO:0000269|PubMed:16108817}.; . . 0.25144 0.12378 -0.449946534 24.00330267 42.07693 1.22532 KLHL13 0.731977363371556 0.267469177450582 0.000553459177861127 kelch like family member 13 FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex mediates the ubiquitination of AURKB and controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:17543862, ECO:0000269|PubMed:19995937}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;bone;bladder;brain;unclassifiable (Anatomical System);heart;pharynx;blood;lens;breast;lung;placenta;macula lutea;hippocampus;visual apparatus;liver;cervix;kidney; caudate nucleus;skeletal muscle; 0.26598 0.09085 -0.22584292 37.32012267 26.10807 0.84741 KLHL14 0.0827221887035056 0.916851004210574 0.000426807085920975 kelch like family member 14 . . . unclassifiable (Anatomical System);uterus;lung;ovary;endometrium;placenta;visual apparatus;parathyroid;blood;germinal center;brain; superior cervical ganglion;trigeminal ganglion; 0.49787 . -0.979072682 8.752064166 49.14169 1.37053 KLHL15 0.954395214388248 0.0454814104272531 0.000123375184498553 kelch like family member 15 FUNCTION: Probable substrate-specific adapter of an E3 ubiquitin- protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000269|PubMed:14528312}.; . . unclassifiable (Anatomical System);smooth muscle;lymph node;ovary;urinary;colon;parathyroid;skin;bone marrow;breast;uterus;prostate;lung;endometrium;thyroid;placenta;visual apparatus;liver;testis;cervix;head and neck;germinal center;kidney;brain;stomach;peripheral nerve; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.60220 0.11136 -0.383807564 27.41802312 6.82731 0.25328 KLHL17 2.51676266070248e-07 0.722913600252338 0.277086148071396 kelch like family member 17 FUNCTION: Substrate-recognition component of some cullin-RING- based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. The BCR(KLHL17) mediates the ubiquitination and subsequenct degradation of GLUR6. May play a role in the actin-based neuronal function (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;salivary gland;colon;fovea centralis;choroid;lens;skin;retina;optic nerve;lung;endometrium;bone;macula lutea;hypopharynx;testis;head and neck;germinal center;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.09980 0.09909 -2.653369885 0.754895022 60.97395 1.58809 KLHL18 0.984175216789434 0.0158229583948505 1.82481571525308e-06 kelch like family member 18 . . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;blood;lens;skeletal muscle;breast;lung;mesenchyma;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis - interstitial;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cerebellum; 0.41058 0.10851 -0.890882376 10.30313753 57.4268 1.52706 KLHL20 0.0616770822299398 0.93818369178517 0.000139225984890647 kelch like family member 20 FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis (PubMed:20389280). The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'- linked ubiquitination (PubMed:24768539). Involved in anterograde Golgi to endosome transport by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting interaction between CORO7 and EPS15, thereby facilitating actin polymerization and post-Golgi trafficking (PubMed:24768539). Also acts as a regulator of endothelial migration during angiogenesis by controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin ligase complex acts as a regulator of neurite outgrowth by mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11 (PubMed:21670212). In case of tumor, the BCR(KLHL20) E3 ubiquitin ligase complex is involved in tumor hypoxia: following hypoxia, the BCR(KLHL20)complex mediates ubiquitination and degradation of PML, potentiating HIF-1 signaling and cancer progression (PubMed:21840486). {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:17395875, ECO:0000269|PubMed:20389280, ECO:0000269|PubMed:21670212, ECO:0000269|PubMed:21840486, ECO:0000269|PubMed:24768539}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;cochlea;larynx;testis;germinal center;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.20287 0.10893 -0.381986487 27.68931352 56.33899 1.50785 KLHL21 0.00107735176759231 0.828910193417516 0.170012454814892 kelch like family member 21 FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for efficient chromosome alignment and cytokinesis. The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of AURKB. Ubiquitination of AURKB by BCR(KLHL21) E3 ubiquitin ligase complex may not lead to its degradation by the proteasome. {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:19995937}.; . . . . 0.28451 0.11749 . . 169.34636 2.83918 KLHL22 0.702611047042905 0.297235372517687 0.000153580439408309 kelch like family member 22 FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of PLK1 at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. Monoubiquitination of PLK1 does not lead to PLK1 degradation. {ECO:0000269|PubMed:19995937, ECO:0000269|PubMed:23455478}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;synovium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;mesenchyma;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach;thymus; medulla oblongata;superior cervical ganglion;cerebellum peduncles;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.52594 0.11209 -1.199555187 5.761972163 26.86408 0.86770 KLHL23 0.0206607984994721 0.961961207567938 0.0173779939325901 kelch like family member 23 . . . unclassifiable (Anatomical System);uterus;heart;adrenal gland;visual apparatus;hippocampus;liver;spleen;spinal ganglion;brain;skeletal muscle; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.25193 0.12251 -0.53631094 20.53550366 47.19837 1.33113 KLHL24 0.252414430146934 0.74631296905748 0.00127260079558605 kelch like family member 24 FUNCTION: Specifically reduces kainate receptor-mediated currents in hippocampal neurons, most probably by modulating channel properties. {ECO:0000250}.; . . lymphoreticular;smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;breast;lung;placenta;spleen;head and neck;kidney;stomach; occipital lobe;superior cervical ganglion;tongue;adrenal cortex;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe;skin;skeletal muscle; 0.21414 0.11262 -0.780646273 12.77423921 734.84508 5.37741 KLHL25 2.20160691373916e-10 0.00996819524161713 0.990031804538222 kelch like family member 25 FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for translational homeostasis. The BCR(KLHL25) ubiquitin ligase complex acts by mediating ubiquitination of hypophosphorylated EIF4EBP1 (4E-BP1): ubiquitination and subsequent degradation of hypophosphorylated EIF4EBP1 (4E-BP1) probably serves as a homeostatic mechanism to maintain translation and prevent eIF4E inhibition when eIF4E levels are low. The BCR(KLHL25) complex does not target EIF4EBP1 (4E-BP1) when it is hyperphosphorylated or associated with eIF4E. {ECO:0000269|PubMed:22578813}.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;adrenal cortex;colon;parathyroid;lens;skin;skeletal muscle;uterus;pancreas;prostate;lung;frontal lobe;synovium;bone;placenta;testis;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex; 0.22225 0.11186 -1.567158756 3.190610993 489.79247 4.55444 KLHL26 6.67074241107322e-05 0.726154351900847 0.273778940675043 kelch like family member 26 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;lens;pancreas;lung;placenta;macula lutea;liver;head and neck;kidney;stomach;thymus; whole brain;amygdala;superior cervical ganglion;prefrontal cortex;pons;cingulate cortex;cerebellum; 0.13575 0.11250 -1.640558385 2.783675395 52.06948 1.42568 KLHL28 0.188871208958842 0.808781494910643 0.00234729613051517 kelch like family member 28 . . . unclassifiable (Anatomical System);heart;skin;skeletal muscle;retina;bone marrow;breast;uterus;prostate;lung;nasopharynx;placenta;liver;testis;spleen;cervix;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.23421 . 0.196671391 67.19155461 279.34212 3.58192 KLHL29 . . . kelch like family member 29 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;tongue;islets of Langerhans;muscle;urinary;colon;parathyroid;lens;skin;uterus;prostate;lung;frontal lobe;adrenal gland;bone;placenta;visual apparatus;liver;testis;head and neck;germinal center;kidney;brain;mammary gland; subthalamic nucleus;uterus corpus;superior cervical ganglion;adrenal cortex;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.74488 . -0.53631094 20.53550366 164.66985 2.80262 KLHL30 8.29725101843079e-11 0.0396281237508799 0.960371876166147 kelch like family member 30 . . . unclassifiable (Anatomical System);skeletal muscle; ciliary ganglion;trigeminal ganglion; 0.07834 . -0.262657925 34.93158764 2561.08705 9.45363 KLHL30-AS1 . . . KLHL30 antisense RNA 1 . . . . . . . . . . . KLHL31 0.0190832639670692 0.961463993704089 0.0194527423288421 kelch like family member 31 FUNCTION: Transcriptional repressor in MAPK/JNK signaling pathway to regulate cellular functions. Overexpression inhibits the transcriptional activities of both the TPA-response element (TRE) and serum response element (SRE). {ECO:0000269|PubMed:18719355}.; . . . . 0.27723 0.10718 0.022122107 55.69120075 214.20925 3.15893 KLHL32 0.509586628745803 0.490246623123266 0.000166748130931017 kelch like family member 32 . . . . . 0.08285 . -0.378346116 28.01368247 532.14159 4.70598 KLHL33 . . . kelch like family member 33 . . . . . 0.28345 . 1.68481378 96.37886294 3587.65052 11.59706 KLHL34 4.42258132212847e-05 0.234130878420816 0.765824895765963 kelch like family member 34 . . . . . 0.58710 . -0.095386216 46.48502005 58.40155 1.54794 KLHL35 1.35038973626761e-12 0.0018440367284156 0.998155963270234 kelch like family member 35 . . . . . . 0.11511 . . 89.19671 2.02976 KLHL36 0.939925902191205 0.0600239398622951 5.01579464997241e-05 kelch like family member 36 FUNCTION: Probable substrate-specific adapter of an E3 ubiquitin- protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000269|PubMed:14528312}.; . . unclassifiable (Anatomical System);lymph node;ovary;colon;parathyroid;lens;skeletal muscle;breast;greater omentum;lung;endometrium;placenta;visual apparatus;testis;germinal center;kidney;brain;bladder;stomach; . 0.16601 . -1.682848699 2.653927813 65.89224 1.67114 KLHL38 3.93864930044432e-06 0.371337003854983 0.628659057495716 kelch like family member 38 . . . heart; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; . . 0.519883383 80.37272942 2545.63685 9.42630 KLHL40 0.0781027060776258 0.910758742584772 0.0111385513376028 kelch like family member 40 FUNCTION: Required for skeletal muscle development. {ECO:0000269|PubMed:23746549}.; . TISSUE SPECIFICITY: Highly expressed in fetal (19, 23 and 31 weeks of gestation) and adult skeletal muscle; expression levels tend to be higher in fetal compared to postnatal muscles (at protein level). Aslo expressed in fetal and adult heart. {ECO:0000269|PubMed:23746549}.; . . 0.50192 . -0.905656269 10.12031139 255.37197 3.43793 KLHL41 0.0188120404902001 0.961337618505153 0.0198503410046464 kelch like family member 41 FUNCTION: Involved in skeletal muscle development and differentiation. Regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils. Required for pseudopod elongation in transformed cells. {ECO:0000250|UniProtKB:A2AUC9}.; DISEASE: Nemaline myopathy 9 (NEM9) [MIM:615731]: An autosomal recessive form of nemaline myopathy. Nemaline myopathies are muscular disorders characterized by muscle weakness of varying severity and onset, and abnormal thread-like or rod-shaped structures in muscle fibers on histologic examination. NEM9 phenotype is highly variable, ranging from death in infancy due to lack of antigravity movements, to slowly progressive distal muscle weakness with preserved ambulation later in childhood. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Sarcomeric muscle.; . . 0.87467 0.12353 0.198490371 67.30360934 153.84573 2.71170 KLHL42 0.438781823689429 0.554406257545518 0.00681191876505223 kelch like family member 42 FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL42) E3 ubiquitin ligase complex mediates the ubiquitination and subsequent degradation of KATNA1. Involved in microtubule dynamics throughout mitosis. {ECO:0000269|PubMed:19261606}.; . . . . 0.22816 0.10878 -0.471992905 23.03609342 14.77248 0.53203 KLK1 0.000319896608295988 0.584550996546889 0.415129106844815 kallikrein 1 FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.; . TISSUE SPECIFICITY: Isoform 2 is expressed in pancreas, salivary glands, kidney, colon, prostate gland, testis, spleen and the colon adenocarcinoma cell line T84. {ECO:0000269|PubMed:7749372}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;bone;thyroid;testis;brain;bladder;pineal gland;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;breast;pancreas;lung;adrenal gland;visual apparatus;liver;spleen;kidney;stomach; superior cervical ganglion;pancreas;salivary gland;beta cell islets;kidney;trigeminal ganglion; 0.03547 0.41982 0.68351529 85.03774475 1133.56294 6.42574 KLK2 0.00029249151077166 0.565053026439662 0.434654482049567 kallikrein related peptidase 2 FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.; . . unclassifiable (Anatomical System);prostate;lung;bone;testis;skeletal muscle;peripheral nerve;bone marrow; dorsal root ganglion;prostate;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.07864 . 0.551232944 81.48148148 250.88481 3.41301 KLK3 0.00347267051874821 0.836500778129925 0.160026551351327 kallikrein related peptidase 3 FUNCTION: Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum.; . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;colon;pharynx;blood;skin;skeletal muscle;bone marrow;breast;prostate;lung;liver;kidney;bladder;mammary gland;brain;peripheral nerve; prostate;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.60398 0.40961 0.20030965 67.3566879 169.21248 2.83705 KLK4 0.020194728883179 0.90360844710081 0.0761968240160114 kallikrein related peptidase 4 FUNCTION: Involved in enamel formation. {ECO:0000269|PubMed:15235027}.; . TISSUE SPECIFICITY: Expressed in prostate.; unclassifiable (Anatomical System);prostate;endometrium;blood;brain;bone marrow; prostate;ciliary ganglion; 0.10482 . 0.483275131 79.25218212 367.6481 4.05342 KLK5 0.0727607206770689 0.872366615520324 0.0548726638026072 kallikrein related peptidase 5 FUNCTION: May be involved in desquamation.; . TISSUE SPECIFICITY: Expressed in skin, breast, brain and testis. Expressed at the stratum granulosum of palmar skin. {ECO:0000269|PubMed:19190773}.; unclassifiable (Anatomical System);breast;lymph node;ovary;heart;endometrium;tongue;testis;cervix;head and neck;skin;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.16534 0.26726 -0.159704656 41.90846898 24.65564 0.81006 KLK6 0.497244483744415 0.498364741484275 0.00439077477130984 kallikrein related peptidase 6 FUNCTION: Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerization, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells treated with a neutralizing KLK6 antibody migrate less than control cells, suggesting a role in invasion and metastasis. {ECO:0000269|PubMed:11983703, ECO:0000269|PubMed:12878203, ECO:0000269|PubMed:12928483, ECO:0000269|PubMed:15557757, ECO:0000269|PubMed:16321973, ECO:0000269|PubMed:16987227}.; . TISSUE SPECIFICITY: In fluids, highest levels found in milk of lactating women followed by cerebrospinal fluid, nipple aspirate fluid and breast cyst fluid. Also found in serum, seminal plasma and some amniotic fluids and breast tumor cytosolic extracts. Not detected in urine. At the tissue level, highest concentrations found in glandular tissues such as salivary glands followed by lung, colon, fallopian tube, placenta, breast, pituitary and kidney. Not detected in skin, spleen, bone, thyroid, heart, ureter, liver, muscle, endometrium, testis, pancreas, seminal vesicle, ovary, adrenals and prostate. In brain, detected in gray matter neurons (at protein level). Colocalizes with pathological inclusions such as Lewy bodies and glial cytoplasmic inclusions. Overexpressed in primary breast tumors but not expressed in metastatic tumors. {ECO:0000269|PubMed:10997858, ECO:0000269|PubMed:11018688, ECO:0000269|PubMed:11668196, ECO:0000269|PubMed:12928483, ECO:0000269|PubMed:16800739}.; unclassifiable (Anatomical System);lymph node;ovary;tongue;colon;breast;uterus;pancreas;lung;frontal lobe;oesophagus;hippocampus;hypopharynx;liver;head and neck;spleen;kidney;brain;mammary gland;stomach; thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;hypothalamus;spinal cord;pons;caudate nucleus;cingulate cortex;parietal lobe; 0.19832 0.25650 0.038710339 56.92380278 299.69553 3.69118 KLK7 0.00688296460219149 0.759241894278668 0.23387514111914 kallikrein related peptidase 7 FUNCTION: May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6- Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|- Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines. {ECO:0000269|PubMed:23370777}.; . TISSUE SPECIFICITY: Abundantly expressed in the skin and is expressed by keratinocytes in the epidermis. Also expressed in the brain, mammary gland, cerebellum, spinal cord and kidney. Lower levels in salivary glands, uterus, thymus, thyroid, placenta, trachea and testis. Up-regulated in ovarian carcinoma, especially late-stage serous carcinoma, compared with normal ovaries and benign adenomas (at protein level). {ECO:0000269|PubMed:10974542, ECO:0000269|PubMed:12738725}.; unclassifiable (Anatomical System);lymph node;heart;ovary;tongue;hypothalamus;oral cavity;uterus;pancreas;lung;hypopharynx;amniotic fluid;head and neck;kidney;stomach; . 0.12861 0.15247 -0.514264485 21.41424864 72.70252 1.78016 KLK8 0.00338366631961467 0.950711062055128 0.045905271625257 kallikrein related peptidase 8 FUNCTION: Serine protease which is capable of degrading a number of proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Also cleaves L1CAM in response to increased neural activity. Induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Plays a role in the formation and maturation of orphan and small synaptic boutons in the Schaffer- collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is required for memory acquisition and synaptic plasticity. Involved in skin desquamation and keratinocyte proliferation. Plays a role in the secondary phase of pathogenesis following spinal cord injury. {ECO:0000269|PubMed:16337200}.; . TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in the pancreas. Isoform 2 is expressed in adult brain and hippocampus. Isoform 1 and isoform 2 are found in fetal brain and placenta. Detected in salivary gland, uterus, thymus, breast, testis and kidney but not in spleen, liver, lung or normal ovarian tissue. Displays an 11.5-fold increase in Alzheimer disease hippocampus compared to controls and is overexpressed in some ovarian carcinomas. Expressed at low levels in normal skin while high levels are found in psoriasis vulgaris, seborrheic keratosis, lichen planus and squamous cell carcinoma skin samples. Expressed in the keratinocytes. {ECO:0000269|PubMed:11309326, ECO:0000269|PubMed:11522960, ECO:0000269|PubMed:12147714, ECO:0000269|PubMed:17761692}.; unclassifiable (Anatomical System);lymph node;ovary;parathyroid;uterus;breast;lung;larynx;adrenal gland;placenta;testis;brain;stomach;gall bladder; superior cervical ganglion;tongue;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.05654 0.23924 -0.227663163 37.11370606 279.76148 3.58394 KLK9 0.00393894270251681 0.855147819559476 0.140913237738007 kallikrein related peptidase 9 . . TISSUE SPECIFICITY: Skin, thymus, trachea, cerebellum and spinal cord.; larynx; . 0.11602 . -0.117432389 44.89266336 31.36317 0.98869 KLK10 4.40787331105343e-05 0.40573903674001 0.59421688452688 kallikrein related peptidase 10 FUNCTION: Has a tumor-suppressor role for NES1 in breast and prostate cancer.; . TISSUE SPECIFICITY: Expressed in breast, ovary and prostate.; ovary;colon;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;testis;unclassifiable (Anatomical System);heart;tongue;oral cavity;lens;breast;pancreas;lung;macula lutea;hypopharynx;head and neck;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;tongue;atrioventricular node;trigeminal ganglion;tonsil;skeletal muscle; 0.12310 0.24673 0.264628794 70.5178108 835.64366 5.66066 KLK11 0.0574751215215554 0.924577874499974 0.0179470039784707 kallikrein related peptidase 11 FUNCTION: Possible multifunctional protease. Efficiently cleaves 'bz-Phe-Arg-4-methylcoumaryl-7-amide', a kallikrein substrate, and weakly cleaves other substrates for kallikrein and trypsin. Cleaves synthetic peptides after arginine but not lysine residues. {ECO:0000269|PubMed:10872828, ECO:0000269|PubMed:16467084}.; . TISSUE SPECIFICITY: Expressed in brain, skin and prostate. Isoform 1 is expressed preferentially in brain. Isoform 2 is expressed in prostate. Present in seminal plasma at concentrations ranging from 2 to 37 microg/mL (at protein level). {ECO:0000269|PubMed:10872828, ECO:0000269|PubMed:16467084}.; unclassifiable (Anatomical System);cartilage;heart;ovary;colon;uterus;prostate;lung;endometrium;nasopharynx;pituitary gland;testis;kidney;brain;stomach; prostate;trachea;tongue;testis;skin; 0.08623 . 0.885576705 89.14248644 704.29209 5.27373 KLK12 0.00182411651683503 0.71911149154365 0.279064391939515 kallikrein related peptidase 12 . . . testis;blood; superior cervical ganglion;tongue; 0.05058 0.13249 -0.025608647 51.91672564 291.08926 3.64931 KLK13 0.755462837830593 0.242478738652146 0.00205842351726122 kallikrein related peptidase 13 . . TISSUE SPECIFICITY: Expressed in prostate, breast, testis and salivary gland.; unclassifiable (Anatomical System);tongue;larynx;oral cavity;hypopharynx;testis;head and neck; dorsal root ganglion;superior cervical ganglion;tongue;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04775 0.09971 -0.159704656 41.90846898 120.56718 2.39208 KLK14 1.09820370579845e-09 0.0255388408387967 0.974461158062999 kallikrein related peptidase 14 FUNCTION: Serine-type endopeptidase with a dual trypsin-like and chymotrypsin-like substrate specificity. May activate/inactivate the proteinase-activated receptors F2R, F2RL1 and F2RL3 and other kallikreins including KLK1, KLK3, KLK5 and KLK11. May function in seminal clot liquefaction through direct cleavage of the semenogelin SEMG1 and SEMG2 and activation of KLK3. May function through desmoglein DSG1 cleavage in epidermal desquamation a process by which the most superficial corneocytes are shed from the skin surface. May be involved in several aspects of tumor progression including growth, invasion and angiogenesis. {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:16885167, ECO:0000269|PubMed:17158887, ECO:0000269|PubMed:17625593, ECO:0000269|PubMed:18056261, ECO:0000269|PubMed:18482984}.; . TISSUE SPECIFICITY: Highly expressed in CNS, bone marrow and fetal liver. Also expressed in breast, thyroid, kidney, colon, pancreas, spleen, prostate, uterus, small intestine, placenta and skeletal muscle. Among 40 tissues tested, the highest expression is detected in skin followed by breast and prostate (at protein level). Expressed in stratum corneum by sweat ducts and sweat glands and detected in sweat (at protein level). {ECO:0000269|PubMed:10969073, ECO:0000269|PubMed:11309303, ECO:0000269|PubMed:11352573, ECO:0000269|PubMed:16456535, ECO:0000269|PubMed:16800737, ECO:0000269|PubMed:17110383}.; unclassifiable (Anatomical System);lung; medulla oblongata;subthalamic nucleus;pons;atrioventricular node;skin;skeletal muscle; 0.05079 . 2.640472481 98.81457891 2522.43509 9.36448 KLK15 0.0465802581941977 0.854447511303955 0.0989722305018472 kallikrein related peptidase 15 FUNCTION: Protease whose physiological substrate is not yet known.; . TISSUE SPECIFICITY: Highest expression in the thyroid gland. Also expressed in the prostate, salivary, and adrenal glands and in the colon testis and kidney. {ECO:0000269|PubMed:11010966}.; lung;bone;testis; skeletal muscle; 0.18438 0.46018 0.883760026 89.07171503 163.77657 2.79585 KLKB1 4.7595385832154e-11 0.337984932346252 0.662015067606152 kallikrein B1 FUNCTION: The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin.; DISEASE: Prekallikrein deficiency (PKK deficiency) [MIM:612423]: This disorder is a blood coagulation defect. {ECO:0000269|PubMed:14652634, ECO:0000269|PubMed:17598838}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . islets of Langerhans;colon;fovea centralis;choroid;lens;retina;pancreas;optic nerve;lung;macula lutea;liver;testis;spleen;kidney;stomach; superior cervical ganglion;fetal liver;atrioventricular node;trigeminal ganglion; 0.47451 0.32850 1.425665442 94.97523001 . . KLKP1 . . . kallikrein pseudogene 1 . . TISSUE SPECIFICITY: Abundant expression is found in prostate, restricted to cells of epithelial origin in normal and diseased glands. Very low expression is detected in pancreas and ovary. {ECO:0000269|PubMed:18196551}.; . . . . . . . . KLLN . . . killin, p53-regulated DNA replication inhibitor FUNCTION: DNA-binding protein involved in S phase checkpoint control-coupled apoptosis by mediating p53/TP53-induced apoptosis. Has the ability to inhibit DNA synthesis and S phase arrest coupled to apoptosis. Has affinity to both double- and single- stranded DNA. {ECO:0000269|PubMed:18385383}.; DISEASE: Cowden syndrome 4 (CWS4) [MIM:615107]: A form of Cowden syndrome, a hamartomatous polyposis syndrome with age-related penetrance. Cowden syndrome is characterized by hamartomatous lesions affecting derivatives of ectodermal, mesodermal and endodermal layers, macrocephaly, facial trichilemmomas (benign tumors of the hair follicle infundibulum), acral keratoses, papillomatous papules, and elevated risk for development of several types of malignancy, particularly breast carcinoma in women and thyroid carcinoma in both men and women. Colon cancer and renal cell carcinoma have also been reported. Hamartomas can be found in virtually every organ, but most commonly in the skin, gastrointestinal tract, breast and thyroid. {ECO:0000269|PubMed:21177507}. Note=The gene represented in this entry is involved in disease pathogenesis. Germline KLLN methylation is common among patients with Cowden syndrome or Cowden-like syndrome and is associated with increased risks of breast and renal cancer over PTEN mutation-positive individuals (PubMed:21177507). {ECO:0000269|PubMed:21177507}.; . . . . . 1.012423333 90.829205 121.24747 2.39863 KLRA1P . . . killer cell lectin like receptor A1, pseudogene . . . . . 0.06731 0.18237 . . . . KLRB1 4.43124831904582e-06 0.392493551834019 0.607502016917662 killer cell lectin like receptor B1 FUNCTION: Plays an inhibitory role on natural killer (NK) cells cytotoxicity. Activation results in specific acid sphingomyelinase/SMPD1 stimulation with subsequent marked elevation of intracellular ceramide. Activation also leads to AKT1/PKB and RPS6KA1/RSK1 kinases stimulation as well as markedly enhanced T-cell proliferation induced by anti-CD3. Acts as a lectin that binds to the terminal carbohydrate Gal-alpha(1,3)Gal epitope as well as to the N-acetyllactosamine epitope. Binds also to CLEC2D/LLT1 as a ligand and inhibits NK cell-mediated cytotoxicity as well as interferon-gamma secretion in target cells. {ECO:0000269|PubMed:16455998, ECO:0000269|PubMed:16925668, ECO:0000269|PubMed:8077657}.; . TISSUE SPECIFICITY: Expressed in a subset of NK cells predominantly in intestinal epithelium and liver. Detected in peripheral blood T-cells and preferentially in adult T-cells with a memory antigenic phenotype. {ECO:0000269|PubMed:12100027, ECO:0000269|PubMed:8077657}.; unclassifiable (Anatomical System);heart;colon;blood;skin;uterus;pancreas;lung;nasopharynx;testis;spleen;kidney;brain;aorta;stomach; whole blood; 0.08541 . 0.393270925 76.04977589 4277.18133 13.00542 KLRC1 0.00117546106046322 0.842671170351783 0.156153368587753 killer cell lectin like receptor C1 FUNCTION: Plays a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells.; . TISSUE SPECIFICITY: Natural killer cells.; unclassifiable (Anatomical System);cervix;blood;retina; . 0.06459 0.19078 -0.05129383 49.75819769 9.13858 0.33334 KLRC2 0.00427823231663552 0.866490673386082 0.129231094297282 killer cell lectin like receptor C2 FUNCTION: Plays a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells.; . TISSUE SPECIFICITY: Natural killer cells.; . . 0.31584 0.11996 -0.029247611 51.40363293 8.14426 0.29990 KLRC3 0.204478935607772 0.752596328346716 0.0429247360455119 killer cell lectin like receptor C3 FUNCTION: Plays a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells.; . TISSUE SPECIFICITY: Natural killer cells.; . . 0.04762 . 0.637604436 83.77565464 572.10514 4.85416 KLRC4 0.00108734943903597 0.608463837851696 0.390448812709268 killer cell lectin like receptor C4 FUNCTION: May play a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells.; . TISSUE SPECIFICITY: Natural killer cells.; unclassifiable (Anatomical System);lung;germinal center;skeletal muscle;stomach; superior cervical ganglion; 0.05677 0.06758 0.3032669 72.009908 1.15532 0.03187 KLRC4-KLRK1 . . . KLRC4-KLRK1 readthrough FUNCTION: Function as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell-mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins including MICA, MICB, RAET1E, RAET1G, ULBP1, ULBP2, ULBP3 (ULBP2>ULBP1>ULBP3) and ULBP4. {ECO:0000269|PubMed:10426994, ECO:0000269|PubMed:11224526, ECO:0000269|PubMed:11777960, ECO:0000269|PubMed:15240696, ECO:0000269|PubMed:21898152, ECO:0000269|PubMed:23298206}.; . TISSUE SPECIFICITY: Expressed in natural killer (NK) cells, CD8(+) alpha-beta and gamma-delta T-cells. Expressed on essentially all CD56+CD3- NK cells from freshly isolated PBMC. Expressed in interferon-producing killer dendritic cells (IKDCs). {ECO:0000269|PubMed:10426993, ECO:0000269|PubMed:15294961, ECO:0000269|PubMed:16444266}.; . . . . . . 1.21964 0.04060 KLRD1 0.015657762831995 0.881087831806646 0.103254405361359 killer cell lectin like receptor D1 FUNCTION: Plays a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells.; . TISSUE SPECIFICITY: Natural killer cells.; unclassifiable (Anatomical System);placenta;liver;testis;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.09925 0.24245 0.369407109 74.95281906 9.48335 0.34992 KLRF1 0.00436476048223472 0.869132187940769 0.126503051576996 killer cell lectin like receptor F1 FUNCTION: Involved in the natural killer (NK)-mediated cytolysis of PHA-induced lymphoblasts.; . TISSUE SPECIFICITY: Strongly expressed in peripheral blood leukocytes and spleen, with weaker expression in lymph node and adult liver, and no expression detected in bone marrow, thymus, and fetal liver. Not expressed in brain, heart, placenta, lung, kidney, skeletal muscle, and pancreas. Within peripheral blood leukocyte and immunocyte cell lines, expression was predominant in NK cells but was also detected in monocytes. {ECO:0000269|PubMed:10671213}.; uterus;ovary;heart;skin; superior cervical ganglion;trigeminal ganglion; 0.11897 0.06780 0.393270925 76.04977589 529.89417 4.69876 KLRF2 . . . killer cell lectin like receptor F2 FUNCTION: C-type lectin-like receptor involved in natural killer cell mediated cytotoxicity and cytokine secretion in keratinocytes via its interaction with CLEC2A. {ECO:0000269|PubMed:20194751}.; . . . . . . . . 81.20681 1.90851 KLRG1 0.0580256114184196 0.867138989320881 0.0748353992606999 killer cell lectin like receptor G1 FUNCTION: Plays an inhibitory role on natural killer (NK) cells and T-cell functions upon binding to their non-MHC ligands. May mediate missing self recognition by binding to a highly conserved site on classical cadherins, enabling it to monitor expression of E-cadherin/CDH1, N-cadherin/CDH2 and R-cadherin/CDH4 on target cells. {ECO:0000269|PubMed:19604491}.; . TISSUE SPECIFICITY: Expressed specifically on natural killer (NK) cells and T-cells, mainly CD8 T-cells. {ECO:0000269|PubMed:15879103, ECO:0000269|PubMed:9842918}.; unclassifiable (Anatomical System);lymph node;heart;spinal cord;vein;skin;bone marrow;uterus;pancreas;prostate;whole body;lung;liver;testis;spleen;germinal center; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.00881 0.05178 0.014844891 54.94810097 27.02476 0.87340 KLRG2 4.20606730807966e-07 0.114348465991639 0.88565111340163 killer cell lectin like receptor G2 . . . unclassifiable (Anatomical System);lung; . 0.08890 . . . 2966.04741 10.32209 KLRK1 9.74878780699033e-10 0.0454877935697659 0.954512205455355 killer cell lectin like receptor K1 FUNCTION: Function as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell-mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins including MICA, MICB, RAET1E, RAET1G, ULBP1, ULBP2, ULBP3 (ULBP2>ULBP1>ULBP3) and ULBP4. {ECO:0000269|PubMed:10426994, ECO:0000269|PubMed:11224526, ECO:0000269|PubMed:11777960, ECO:0000269|PubMed:15240696, ECO:0000269|PubMed:21898152, ECO:0000269|PubMed:23298206}.; . TISSUE SPECIFICITY: Expressed in natural killer (NK) cells, CD8(+) alpha-beta and gamma-delta T-cells. Expressed on essentially all CD56+CD3- NK cells from freshly isolated PBMC. Expressed in interferon-producing killer dendritic cells (IKDCs). {ECO:0000269|PubMed:10426993, ECO:0000269|PubMed:15294961, ECO:0000269|PubMed:16444266}.; lung;ovary;placenta;testis;cervix;germinal center;skin; superior cervical ganglion; 0.10586 0.28197 -0.05129383 49.75819769 13.5893 0.49355 KMO 0.000261678764903106 0.996334958244951 0.00340336299014564 kynurenine 3-monooxygenase (kynurenine 3-hydroxylase) FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract.; . TISSUE SPECIFICITY: Highest levels in placenta and liver. Detectable in kidney. {ECO:0000269|PubMed:9237672}.; . . 0.06915 0.11180 0.663285274 84.55414013 406.82 4.22915 KMS . . . Kabuki mental retardation syndrome . . . . . . . . . . . KMT2A 1 1.87976006504377e-16 1.77900735852416e-42 lysine methyltransferase 2A FUNCTION: Histone methyltransferase that plays an essential role in early development and hematopoiesis. Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac). In the MLL1/MLL complex, it specifically mediates H3K4me, a specific tag for epigenetic transcriptional activation. Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity. Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9'. Required for transcriptional activation of HOXA9. Promotes PPP1R15A-induced apoptosis. Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-ARNTL/BMAL1 heterodimer. Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-ARNTL/BMAL1 to chromatin (By similarity). {ECO:0000250|UniProtKB:P55200, ECO:0000269|PubMed:10490642, ECO:0000269|PubMed:12453419, ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:19556245}.; DISEASE: Wiedemann-Steiner syndrome (WDSTS) [MIM:605130]: A syndrome characterized by hairy elbows (hypertrichosis cubiti), intellectual disability, a distinctive facial appearance, and short stature. Facial characteristics include long eyelashes, thick or arched eyebrows with a lateral flare, and downslanting and vertically narrow palpebral fissures. {ECO:0000269|PubMed:22795537}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Chromosomal aberrations involving KMT2A are a cause of acute leukemias. Translocation t(1;11)(q21;q23) with MLLT11/AF1Q; translocation t(3;11)(p21;q23) with NCKIPSD/AF3p21; translocation t(3,11)(q25,q23) with GMPS; translocation t(4;11)(q21;q23) with AFF1/MLLT2/AF4; insertion ins(5;11)(q31;q13q23) with AFF4/AF5Q31; translocation t(5;11)(q12;q23) with AF5-alpha/CENPK; translocation t(6;11)(q27;q23) with MLLT4/AF6; translocation t(9;11)(p22;q23) with MLLT3/AF9; translocation t(10;11)(p11.2;q23) with ABI1; translocation t(10;11)(p12;q23) with MLLT10/AF10; t(11;15)(q23;q14) with CASC5 and ZFYVE19; translocation t(11;17)(q23;q21) with MLLT6/AF17; translocation t(11;19)(q23;p13.3) with ELL; translocation t(11;19)(q23;p13.3) with MLLT1/ENL; translocation t(11;19)(q23;p23) with GAS7; translocation t(X;11)(q13;q23) with FOXO4/AFX1. Translocation t(3;11)(q28;q23) with LPP. Translocation t(10;11)(q22;q23) with TET1. Translocation t(9;11)(q34;q23) with DAB2IP. Translocation t(4;11)(p12;q23) with FRYL. Fusion proteins KMT2A-MLLT1, KMT2A- MLLT3 and KMT2A-ELL interact with PPP1R15A and, on the contrary to unfused KMT2A, inhibit PPP1R15A-induced apoptosis. {ECO:0000269|PubMed:10490642}.; DISEASE: Note=A chromosomal aberration involving KMT2A may be a cause of chronic neutrophilic leukemia. Translocation t(4;11)(q21;q23) with SEPT11. {ECO:0000269|PubMed:10490642}.; TISSUE SPECIFICITY: Heart, lung, brain and T- and B-lymphocytes.; . . 0.58012 0.48908 -3.347291482 0.406935598 416.01763 4.26932 KMT2B 0.999999997452585 2.54741448520368e-09 2.07210210721289e-24 lysine methyltransferase 2B FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in beta-globin locus transcription regulation by being recruited by NFE2. Plays an important role in controlling bulk H3K4me during oocyte growth and preimplantation development. Required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that preceeds resumption of meiosis, oocyte survival and normal zygotic genome activation. {ECO:0000269|PubMed:17707229}.; . TISSUE SPECIFICITY: Widely expressed. Highest levels in testis. Also found in brain, bone marrow, heart, muscle, kidney, placenta, spleen, thymus, prostate, ovary, intestine, colon, peripheral blood lymphocytes and pancreas. Often amplified in pancreatic carcinomas.; . . 0.69282 0.10507 -5.294103076 0.064873791 1636.68668 7.47877 KMT2C 0.999999999999997 2.53305448359176e-15 2.33643376123433e-47 lysine methyltransferase 2C FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Central component of the MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. KMT2C/MLL3 may be a catalytic subunit of this complex. May be involved in leukemogenesis and developmental disorder. {ECO:0000269|PubMed:17500065}.; . TISSUE SPECIFICITY: Highly expressed in testis and ovary, followed by brain and liver. Also expressed in placenta, peripherical blood, fetal thymus, heart, lung and kidney. Within brain, expression was highest in hippocampus, caudate nucleus, and substantia nigra. Not detected in skeletal muscle and fetal liver.; . . 0.46876 0.10649 -2.516369113 0.908233074 8094.45636 19.43020 KMT2D 0.999999999999995 5.39357356800153e-15 8.78426426981725e-44 lysine methyltransferase 2D FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone H3 (H3K4me). H3K4me represents a specific tag for epigenetic transcriptional activation. Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription. {ECO:0000269|PubMed:16603732, ECO:0000269|PubMed:17500065, ECO:0000269|PubMed:17851529}.; DISEASE: Kabuki syndrome 1 (KABUK1) [MIM:147920]: A congenital mental retardation syndrome with additional features, including postnatal dwarfism, a peculiar facies characterized by long palpebral fissures with eversion of the lateral third of the lower eyelids, a broad and depressed nasal tip, large prominent earlobes, a cleft or high-arched palate, scoliosis, short fifth finger, persistence of fingerpads, radiographic abnormalities of the vertebrae, hands, and hip joints, and recurrent otitis media in infancy. {ECO:0000269|PubMed:20711175, ECO:0000269|PubMed:21280141, ECO:0000269|PubMed:21607748, ECO:0000269|PubMed:21658225, ECO:0000269|PubMed:21671394, ECO:0000269|PubMed:22126750, ECO:0000269|PubMed:23320472, ECO:0000269|PubMed:23913813, ECO:0000269|PubMed:24739679}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in most adult tissues, including a variety of hematoipoietic cells, with the exception of the liver.; . . 0.69282 0.10507 -5.294103076 0.064873791 1281.52205 6.74114 KMT2E 0.999999994702687 5.29731303906743e-09 1.48807109962481e-21 lysine methyltransferase 2E FUNCTION: Histone methyltransferase that specifically mono- and dimethylates 'Lys-4' of histone H3 (H3K4me1 and H3K4me2). H3 'Lys- 4' methylation represents a specific tag for epigenetic transcriptional activation. Key regulator of hematopoiesis involved in terminal myeloid differentiation and in the regulation of hematopoietic stem cell (HSCs) self-renewal by a mechanism that involves DNA methylation. Plays an essential role in retinoic- acid-induced granulopoiesis by acting as a coactivator of RAR- alpha (RARA) in target gene promoters. Also acts as an important cell cycle regulator, participating in cell cycle regulatory network machinery at multiple cell cycle stages. Required to suppress inappropriate expression of S-phase-promoting genes and maintain expression of determination genes in quiescent cells. Overexpression inhibits cell cycle progression, while knockdown induces cell cycle arrest at both the G1 and G2/M phases.; . TISSUE SPECIFICITY: Widely expressed in both adult and fetal tissues. Highest levels of expression observed in fetal thymus and kidney and in adult hematopoietic tissues, jejunum and cerebellum. Isoform NKp44L is not detected on circulating cells from healthy individuals, but it is expressed on a large panel of the tumor and transformed cells. {ECO:0000269|PubMed:12101424, ECO:0000269|PubMed:23958951}.; . . 0.43067 0.11436 -1.449682288 3.904222694 397.35924 4.18819 KMT2E-AS1 . . . KMT2E antisense RNA 1 (head to head) . . . . . . . . . . . KMT5A . . . lysine methyltransferase 5A FUNCTION: Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF-beta response regulation and a positive role in cell migration. {ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:12121615, ECO:0000269|PubMed:15200950, ECO:0000269|PubMed:15933069, ECO:0000269|PubMed:15933070, ECO:0000269|PubMed:16517599, ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:23478445}.; . . . . 0.13779 0.14003 0.104848986 61.49445624 . . KMT5B . . . lysine methyltransferase 5B FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity). Plays a role in myogenesis by regulating the expression of target genes, such as EID3. {ECO:0000250, ECO:0000269|PubMed:23720823}.; . . . . 0.14235 0.10678 -0.953385901 9.206180703 . . KMT5C . . . lysine methyltransferase 5C FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity). {ECO:0000250}.; . . . . 0.23985 0.11489 . . . . KNCN 0.0295306711881479 0.589478145593608 0.380991183218244 kinocilin FUNCTION: May play a role in stabilizing dense microtubular networks or in vesicular trafficking. {ECO:0000250}.; . . . . 0.09058 . 0.325313577 73.11276244 132.84141 2.50643 KNDC1 4.44328480271007e-05 0.999952561277701 3.00587427194607e-06 kinase non-catalytic C-lobe domain (KIND) containing 1 FUNCTION: Probable guanine nucleotide exchange factor (GEF).; . TISSUE SPECIFICITY: Expressed specifically in the cerebral cortex. {ECO:0000269|Ref.1}.; unclassifiable (Anatomical System);heart;ovary;sympathetic chain;muscle;skeletal muscle;skin;retina;uterus;lung;frontal lobe;hippocampus;testis;brain; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.11621 0.09546 1.089385192 91.85539042 1045.18642 6.20522 KNG1 4.17299309157391e-08 0.805267507995502 0.194732450274567 kininogen 1 FUNCTION: (1) Kininogens are inhibitors of thiol proteases; (2) HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin- induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects: (4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of inflammation and causes (4E1) increase in vascular permeability, (4E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (4F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action); (5) LMW-kininogen inhibits the aggregation of thrombocytes; (6) LMW- kininogen is in contrast to HMW-kininogen not involved in blood clotting.; DISEASE: High molecular weight kininogen deficiency (HMWK deficiency) [MIM:228960]: Autosomal recessive coagulation defect. Patients with HWMK deficiency do not have a hemorrhagic tendency, but they exhibit abnormal surface-mediated activation of fibrinolysis. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Secreted in plasma. T-kinin is detected in malignant ovarian, colon and breast carcinomas, but not in benign tumors. {ECO:0000269|PubMed:2076202}.; unclassifiable (Anatomical System);prostate;cerebral cortex;liver;colon;spleen;kidney;stomach; dorsal root ganglion;fetal liver;superior cervical ganglion;liver;fetal lung;kidney;trigeminal ganglion;skeletal muscle; 0.34824 0.23627 0.202129237 67.42745931 2985.80429 10.37260 KNOP1 3.16682440044249e-05 0.565680292693018 0.434288039062978 lysine-rich nucleolar protein 1 . . . . . . . 0.044168103 57.40740741 384.55815 4.13205 KNOP1P1 . . . lysine-rich nucleolar protein 1 pseudogene 1 . . . . . . . . . . . KNOP1P2 . . . lysine-rich nucleolar protein 1 pseudogene 2 . . . . . . . . . . . KNOP1P3 . . . lysine-rich nucleolar protein 1 pseudogene 3 . . . . . . . . . . . KNOP1P4 . . . lysine-rich nucleolar protein 1 pseudogene 4 . . . . . . . . . . . KNOP1P5 . . . lysine-rich nucleolar protein 1 pseudogene 5 . . . . . . . . . . . KNSTRN 3.15834140854417e-07 0.531900518053429 0.46809916611243 kinetochore-localized astrin/SPAG5 binding protein FUNCTION: Essential component of the mitotic spindle required for faithful chromosome segregation and progression into anaphase (PubMed:19667759). Promotes the metaphase-to-anaphase transition and is required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture (PubMed:19667759, PubMed:22110139). The astrin (SPAG5)-kinastrin (SKAP) complex promotes stable microtubule- kinetochore attachments (PubMed:21402792). Required for kinetochore oscillations and dynamics of microtubule plus-ends during live cell mitosis, possibly by forming a link between spindle microtubule plus-ends and mitotic chromosomes to achieve faithful cell division (PubMed:23035123). May be involved in UV- induced apoptosis via its interaction with PRPF19; however, these results need additional evidences (PubMed:24718257). {ECO:0000269|PubMed:19667759, ECO:0000269|PubMed:21402792, ECO:0000269|PubMed:22110139, ECO:0000269|PubMed:23035123, ECO:0000305|PubMed:24718257}.; DISEASE: Note=Cutaneous squamous cell carcinomas (SCC): A malignancy of the skin. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes. Disease susceptibility is associated with variations affecting the gene represented in this entry. Variant Phe-24 appears specific for UV- associated malignancies (PubMed:25194279). {ECO:0000269|PubMed:25194279}.; TISSUE SPECIFICITY: Widely expressed, including in skin. {ECO:0000269|PubMed:25194279}.; . . 0.17264 0.09426 1.306318795 93.99622552 717.72807 5.31959 KNTC1 4.7771798324088e-32 0.0776560082747327 0.922343991725267 kinetochore associated 1 FUNCTION: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores (PubMed:11146660, PubMed:11590237, PubMed:15824131). Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex. {ECO:0000269|PubMed:11146660, ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:15824131, ECO:0000305}.; . TISSUE SPECIFICITY: High expression in testis.; unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;colon;blood;skin;uterus;bile duct;whole body;lung;bone;thyroid;placenta;visual apparatus;hypopharynx;liver;testis;cervix;head and neck;spleen;kidney;germinal center;brain;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;tumor; 0.53091 0.14549 0.48857149 79.4821892 2346.33497 8.97398 KPNA1 0.993000949687577 0.00699900032660291 4.99858197961744e-08 karyopherin subunit alpha 1 FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non- classical NLS.; . TISSUE SPECIFICITY: Expressed ubiquitously.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;bone;thyroid;iris;testis;dura mater;germinal center;brain;pineal gland;unclassifiable (Anatomical System);meninges;tongue;islets of Langerhans;hypothalamus;urinary;blood;lens;skeletal muscle;breast;pancreas;pia mater;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;fetal brain;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion; 0.91691 0.25567 -0.227663163 37.11370606 14.20019 0.51350 KPNA2 0.728640006952611 0.271243352538761 0.000116640508627257 karyopherin subunit alpha 2 FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.; . TISSUE SPECIFICITY: Expressed ubiquitously.; lymphoreticular;medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;skin;bone marrow;uterus;prostate;whole body;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;heart;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach;thymus; . 0.98833 0.48581 0.50895761 80.20169851 250.45366 3.40960 KPNA3 0.809823934177535 0.190167526800613 8.53902185185699e-06 karyopherin subunit alpha 3 FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non- classical NLS. Recognizes NLSs of influenza A virus nucleoprotein probably through ARM repeats 7-9.; . TISSUE SPECIFICITY: Ubiquitous. Highest levels in heart and skeletal muscle.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;dura mater;spinal ganglion;artery;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;oral cavity;muscle;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;superior cervical ganglion;testis - interstitial;testis;ciliary ganglion;atrioventricular node;parietal lobe;skeletal muscle; 0.70799 0.22385 -0.117432389 44.89266336 63.49368 1.63216 KPNA4 0.998180756390855 0.00181923440057135 9.20857410415931e-09 karyopherin subunit alpha 4 FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non- classical NLS. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS.; . TISSUE SPECIFICITY: Highly expressed in testis, ovary, small intestine, heart, skeletal muscle, lung and pancreas, but barely detectable in kidney, thymus, colon and peripheral blood leukocytes.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;atrium;whole body;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;pineal gland;artery;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.86481 0.44724 -0.139478553 43.29440906 13.68591 0.49653 KPNA5 0.00122321535722017 0.996936726082416 0.00184005856036374 karyopherin subunit alpha 5 FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates nuclear import of STAT1 homodimers and STAT1/STAT2 heterodimers by recognizing non- classical NLSs of STAT1 and STAT2 through ARM repeats 8-9. Recognizes influenza A virus nucleoprotein through ARM repeat 7-9 In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS.; . TISSUE SPECIFICITY: Testis.; unclassifiable (Anatomical System);skeletal muscle;uterus;whole body;lung;larynx;nasopharynx;bone;visual apparatus;liver;testis;head and neck;germinal center;brain; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.94652 . -0.957024976 9.088228356 163.50959 2.79162 KPNA6 0.988827605869537 0.0111723623395393 3.17909234100863e-08 karyopherin subunit alpha 6 FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000269|PubMed:10523667}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10523667}.; . . 0.91536 0.17050 -0.449946534 24.00330267 14.9217 0.53705 KPNA7 . . . karyopherin subunit alpha 7 FUNCTION: Functions in nuclear protein import. {ECO:0000250}.; . . pancreas; . . . 0.395088462 76.15003539 127.88953 2.46510 KPNB1 0.999994327501246 5.67249874675392e-06 7.22096099743542e-15 karyopherin subunit beta 1 FUNCTION: Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re- exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with IPO7 mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Imports SNAI1 and PRKCI into the nucleus. {ECO:0000269|PubMed:10228156, ECO:0000269|PubMed:11891849, ECO:0000269|PubMed:19386897, ECO:0000269|PubMed:9687515}.; . . lymphoreticular;ovary;colon;skin;retina;uterus;prostate;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;spinal cord;muscle;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; amygdala;thalamus;medulla oblongata;testis - interstitial;superior cervical ganglion;tumor;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.99948 0.55950 -0.624497208 17.16206653 28.74247 0.91953 KPRP 7.82565128996116e-14 0.00473834328306747 0.995261656716854 keratinocyte proline rich protein . . TISSUE SPECIFICITY: Expressed in the upper layer of epidermis and psoriasis (at protein level). Expressed in the upper layer of epidermis and psoriasis. {ECO:0000269|PubMed:16297201}.; . . 0.19123 0.07394 2.48969674 98.64354801 6510.14054 16.92534 KPTN 0.000791094717132057 0.982788438636042 0.0164204666468254 kaptin (actin binding protein) FUNCTION: Necessary for normal neuromorphogenesis. May be involved in actin dynamics. May play a role in producing the sensory apparatus in hair cells. May play a role in actin rearrangements that accompany platelet activation and stereocilia formation. {ECO:0000269|PubMed:10099934, ECO:0000269|PubMed:1372044, ECO:0000269|PubMed:24239382}.; DISEASE: Mental retardation, autosomal recessive 41 (MRT41) [MIM:615637]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT41 most consistent features are global developmental delay, macrocephaly with frontal bossing, high levels of anxiety, and some features suggestive of a pervasive developmental disorder. Less common features include fifth finger clinodactyly, recurrent pneumonia, and hepatosplenomegaly. {ECO:0000269|PubMed:24239382}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;optic nerve;oesophagus;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;pharynx;blood;lens;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland; . 0.19338 0.10313 -0.468351206 23.42533616 85.85828 1.97868 KRAS 0.00106119304255182 0.603148256118395 0.395790550839053 Kirsten rat sarcoma viral oncogene homolog FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays an important role in the regulation of cell proliferation (PubMed:23698361, PubMed:22711838). {ECO:0000269|PubMed:22711838, ECO:0000269|PubMed:23698361, ECO:0000305}.; DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. {ECO:0000269|PubMed:8955068}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages. {ECO:0000269|PubMed:17332249}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Noonan syndrome 3 (NS3) [MIM:609942]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. {ECO:0000269|PubMed:16474405, ECO:0000269|PubMed:16773572, ECO:0000269|PubMed:17056636, ECO:0000269|PubMed:17468812, ECO:0000269|PubMed:19396835}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease. {ECO:0000269|PubMed:14534542, ECO:0000269|PubMed:3034404, ECO:0000269|PubMed:7773929}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in KRAS are a cause of pylocytic astrocytoma (PA). Pylocytic astrocytomas are neoplasms of the brain and spinal cord derived from glial cells which vary from histologically benign forms to highly anaplastic and malignant tumors. {ECO:0000269|PubMed:16247081}.; DISEASE: Cardiofaciocutaneous syndrome 2 (CFC2) [MIM:615278]: A form of cardiofaciocutaneous syndrome, a multiple congenital anomaly disorder characterized by a distinctive facial appearance, heart defects and mental retardation. Heart defects include pulmonic stenosis, atrial septal defects and hypertrophic cardiomyopathy. Some affected individuals present with ectodermal abnormalities such as sparse, friable hair, hyperkeratotic skin lesions and a generalized ichthyosis-like condition. Typical facial features are similar to Noonan syndrome. They include high forehead with bitemporal constriction, hypoplastic supraorbital ridges, downslanting palpebral fissures, a depressed nasal bridge, and posteriorly angulated ears with prominent helices. CFC2 patients often do not have the skin abnormalities, such as ichthyosis, hyperkeratosis, and hemangioma observed in CFC1. {ECO:0000269|PubMed:16474404, ECO:0000269|PubMed:16474405, ECO:0000269|PubMed:17056636, ECO:0000269|PubMed:21797849}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=KRAS mutations are involved in cancer development. {ECO:0000269|PubMed:14534542, ECO:0000269|PubMed:1553789, ECO:0000269|PubMed:16533793, ECO:0000269|PubMed:3034404, ECO:0000269|PubMed:3627975, ECO:0000269|PubMed:6092920, ECO:0000269|PubMed:6695174, ECO:0000269|PubMed:7773929}.; . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;spinal cord;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;whole brain;amygdala;occipital lobe;superior cervical ganglion;atrioventricular node;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;cerebellum; 0.99997 0.53296 -0.141298762 42.87567823 3.46519 0.12617 KRASP1 . . . Kirsten rat sarcoma viral oncogene homolog pseudogene 1 . . . . . . . . . . . KRBA1 1.47475623545829e-12 0.0955016006784244 0.904498399320101 KRAB-A domain containing 1 . . TISSUE SPECIFICITY: Expressed in brain (cerebellum). {ECO:0000269|PubMed:11347906}.; unclassifiable (Anatomical System);heart;ovary;cartilage;lacrimal gland;blood;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;lung;endometrium;placenta;thyroid;bone;macula lutea;brain;stomach; . 0.07786 . . . 814.97375 5.61027 KRBA2 3.93218978879099e-07 0.202817552033298 0.797182054747723 KRAB-A domain containing 2 . . . nervous;thyroid;brain;skin; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; . . 0.042348793 57.31304553 129.10103 2.47648 KRBOX1 0.416823600155305 0.465916976545841 0.117259423298854 KRAB box domain containing 1 . . . . . . . . . 3471.76224 11.34170 KRBOX1-AS1 . . . KRBOX1 antisense RNA 1 . . . . . 0.06236 . . . . . KRBOX4 0.377824215699539 0.576314484160501 0.0458613001399595 KRAB box domain containing 4 . . TISSUE SPECIFICITY: Expressed in brain, ovary, testis, prostate, tonsil, heart, bone marrow, colon, breast and kidney. {ECO:0000269|PubMed:11944989}.; . . 0.10810 0.10926 0.435547893 77.45340882 11.87084 0.42983 KRCC1 0.187811675472145 0.762172979032137 0.050015345495718 lysine-rich coiled-coil 1 . . . smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;spinal cord;trigeminal ganglion; 0.27255 . 0.439181676 77.69521113 162.69814 2.78487 KREMEN1 0.372971655730604 0.624700394989237 0.00232794928015859 kringle containing transmembrane protein 1 FUNCTION: Receptor for Dickkopf protein. Cooperates with Dickkopf to block Wnt/beta-catenin signaling (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;lung;frontal lobe;heart;larynx;thyroid;testis;colon;head and neck;skin; . 0.24595 0.13527 0.398725314 76.35645199 1394.17886 6.98482 KREMEN2 0.414292182077592 0.577535976151703 0.00817184177070521 kringle containing transmembrane protein 2 FUNCTION: Receptor for Dickkopf protein. Cooperates with Dickkopf to block Wnt/beta-catenin signaling. Forms a ternary complex with Dkk1 and LRP6 and induces rapid endocytosis and removal of the Wnt receptor LRP6 from the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q8K1S7}.; . . unclassifiable (Anatomical System);heart;adrenal cortex;colon;blood;skin;uterus;placenta;visual apparatus;duodenum;cervix;kidney;brain;stomach; ciliary ganglion;skeletal muscle; 0.16451 0.10602 . . 3585.99813 11.58425 KRI1 8.4034020734588e-09 0.974373496190846 0.0256264954057521 KRI1 homolog . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;bile duct;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; white blood cells;skeletal muscle;thymus; 0.27424 0.09426 1.541397554 95.58858221 6629.49453 17.20782 KRIT1 0.0942382450327803 0.905747686407525 1.40685596943744e-05 KRIT1, ankyrin repeat containing FUNCTION: Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity (By similarity). Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-dependent and independent manner, and inhibits ERK1/2 phosphorylation indirectly through activation of the DELTA-NOTCH cascade. Acts in concert with CDH5 to establish and maintain correct endothelial cell polarity and vascular lumen and these effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction, and cell junction stabilization. Plays a role in integrin signaling via its interaction with ITGB1BP1; this prevents the interaction between ITGB1 and ITGB1BP1. Microtubule- associated protein that binds to phosphatidylinositol 4,5- bisphosphate (PIP2)-containing membranes in a GTP-bound RAP1- dependent manner. Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Regulates the homeostasis of intracellular ROS through an antioxidant pathway involving FOXO1 and SOD2. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS through the modulation of FOXO1 and SOD2 levels. {ECO:0000250, ECO:0000269|PubMed:11741838, ECO:0000269|PubMed:17916086, ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:20616044, ECO:0000269|PubMed:20668652, ECO:0000269|PubMed:21633110, ECO:0000269|Ref.20}.; DISEASE: Cerebral cavernous malformations 1 (CCM1) [MIM:116860]: A congenital vascular anomaly of the central nervous system that can result in hemorrhagic stroke, seizures, recurrent headaches, and focal neurologic deficits. The lesions are characterized by grossly enlarged blood vessels consisting of a single layer of endothelium and without any intervening neural tissue, ranging in diameter from a few millimeters to several centimeters. {ECO:0000269|PubMed:12172908}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Low levels in brain. Very weak expression found in heart and muscle. {ECO:0000269|PubMed:9285558}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);heart;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;placenta;liver;kidney;stomach; . 0.15958 0.41628 -0.865195027 10.79853739 57.40188 1.52611 KRR1 0.0193505805705808 0.976641064095888 0.00400835533353164 KRR1, small subunit (SSU) processome component, homolog (yeast) FUNCTION: Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (By similarity). {ECO:0000250}.; . . lymphoreticular;smooth muscle;ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;gum;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;amnion;liver;cervix;head and neck;kidney;aorta;stomach; subthalamic nucleus;atrioventricular node;trigeminal ganglion; 0.95942 0.37815 -0.291981272 33.20358575 2321.28377 8.92343 KRR1P1 . . . KRR1, small subunit (SSU) processome component, homolog (yeast) pseudogene 1 . . . . . . . . . . . KRT1 0.973618209444121 0.0263804880564507 1.30249942807804e-06 keratin 1 FUNCTION: May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein kinase C (RACK1/GNB2L1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK. {ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:21544310}.; DISEASE: Epidermolytic hyperkeratosis (EHK) [MIM:113800]: An autosomal dominant skin disorder characterized by widespread blistering and an ichthyotic erythroderma at birth that persist into adulthood. Histologically there is a diffuse epidermolytic degeneration in the lower spinous layer of the epidermis. Within a few weeks from birth, erythroderma and blister formation diminish and hyperkeratoses develop. {ECO:0000269|PubMed:10232403, ECO:0000269|PubMed:10688370, ECO:0000269|PubMed:10844506, ECO:0000269|PubMed:11531804, ECO:0000269|PubMed:12406348, ECO:0000269|PubMed:1380725, ECO:0000269|PubMed:1381288, ECO:0000269|PubMed:21271994, ECO:0000269|PubMed:7507151, ECO:0000269|PubMed:7507152, ECO:0000269|PubMed:7512983, ECO:0000269|PubMed:9856846}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ichthyosis hystrix, Curth-Macklin type (IHCM) [MIM:146590]: A genodermatosis with severe verrucous hyperkeratosis. Affected individuals manifest congenital verrucous black scale on the scalp, neck, and limbs with truncal erythema, palmoplantar keratoderma and keratoses on the lips, ears, nipples and buttocks. {ECO:0000269|PubMed:11286616}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Keratoderma, palmoplantar, non-epidermolytic (NEPPK) [MIM:600962]: A dermatological disorder characterized by well- demarcated hyperkeratosis is present over the palms and soles. A red band is frequently present at the periphery of the keratosis. It is usually non-transgredient, with a sharp demarcation of the lesions at the wrists. {ECO:0000269|PubMed:11286630, ECO:0000269|PubMed:7528239}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ichthyosis annular epidermolytic (AEI) [MIM:607602]: A skin disorder resembling bullous congenital ichthyosiform erythroderma. Affected individuals present with bullous ichthyosis in early childhood and hyperkeratotic lichenified plaques in the flexural areas and extensor surfaces at later ages. The feature that distinguishes AEI from BCIE is dramatic episodes of flares of annular polycyclic plaques with scale, which coalesce to involve most of the body surface and can persist for several weeks or even months. {ECO:0000269|PubMed:10053007, ECO:0000269|PubMed:10597140}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Keratoderma, palmoplantar, striate 3 (SPPK3) [MIM:607654]: A dermatological disorder characterized by thickening of the stratum corneum and epidermal layers on palms and soles. There is no involvement of non-palmoplantar skin, and both hair and nails are normal. {ECO:0000269|PubMed:11982762}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: The source of this protein is neonatal foreskin. The 67-kDa type II keratins are expressed in terminally differentiating epidermis.; unclassifiable (Anatomical System);heart;epidermis;adrenal medulla;blood;skin;uterus;lung;hypopharynx;liver;testis;head and neck;spleen;bladder;thymus; superior cervical ganglion;tongue;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.79851 0.61014 0.709197509 85.68058504 4311.14232 13.06797 KRT2 0.0673499186894365 0.929718636506901 0.00293144480366279 keratin 2 FUNCTION: Probably contributes to terminal cornification. Associated with keratinocyte activation, proliferation and keratinization. {ECO:0000269|PubMed:12598329, ECO:0000269|PubMed:1380918}.; DISEASE: Ichthyosis bullosa of Siemens (IBS) [MIM:146800]: A rare autosomal dominant skin disorder displaying a type of epidermolytic hyperkeratosis characterized by generalized erythema and extensive blistering from birth. Large, dark gray hyperkeratoses are observed in later weeks. The skin of IBS patients is unusually fragile and has a tendency to shed the outer layers of the epidermis, producing localized denuded areas (molting effect). IBS usually improves with age so that in most middle-aged patients the hyperkeratosis and keratotic lichenification is limited to the flexural folds of the major joints. {ECO:0000269|PubMed:10084318, ECO:0000269|PubMed:10233323, ECO:0000269|PubMed:10564334, ECO:0000269|PubMed:10620137, ECO:0000269|PubMed:10688369, ECO:0000269|PubMed:11167982, ECO:0000269|PubMed:11531804, ECO:0000269|PubMed:15949009, ECO:0000269|PubMed:7521371, ECO:0000269|PubMed:7524919, ECO:0000269|PubMed:8077693, ECO:0000269|PubMed:9036938, ECO:0000269|PubMed:9204966, ECO:0000269|PubMed:9804344, ECO:0000269|PubMed:9833038}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the upper spinous and granular suprabasal layers of normal adult epidermal tissues from most body sites including thigh, breast nipple, foot sole, penile shaft and axilla. Not present in foreskin, squamous metaplasias and carcinomas. Expression in hypertrophic and keloid scars begins in the deepest suprabasal layer. Weakly expressed in normal gingiva and tongue, however expression is induced in benign keratoses of lingual mucosa and in mild-to-moderate oral dysplasia with orthokeratinization. {ECO:0000269|PubMed:10233306, ECO:0000269|PubMed:12598329, ECO:0000269|PubMed:1380918}.; unclassifiable (Anatomical System);skin; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin; 0.15783 0.10965 0.292133603 71.59707478 2551.90953 9.43604 KRT3 1.92686672080473e-06 0.445801176186269 0.55419689694701 keratin 3 . . TISSUE SPECIFICITY: Cornea specific.; lung;visual apparatus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.15515 . 0.382138899 75.65463553 6781.55104 17.49745 KRT4 0.000566042966242136 0.993911631785719 0.00552232524803849 keratin 4 . DISEASE: White sponge nevus 1 (WSN1) [MIM:193900]: A rare disorder characterized by the presence of soft, white, and spongy plaques in the oral mucosa. The characteristic histopathologic features are epithelial thickening, parakeratosis, and vacuolization of the suprabasal layer of oral epithelial keratinocytes. Less frequently the mucous membranes of the nose, esophagus, genitalia and rectum are involved. {ECO:0000269|PubMed:10652003, ECO:0000269|PubMed:12828738}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in the suprabasal layer of the stratified epithelium of the esophagus, exocervix, vagina, mouth and lingual mucosa, and in cells and cell clusters in the mucosa and serous gland ducts of the esophageal submucosa (at protein level). Expressed widely in the exocervix and esophageal epithelium, with lowest levels detected in the basal cell layer. {ECO:0000269|PubMed:2452170}.; ovary;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;oesophagus;larynx;thyroid;bone;testis;tonsil;unclassifiable (Anatomical System);heart;oral cavity;lens;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;hypopharynx;head and neck;cervix;mammary gland;stomach; superior cervical ganglion;trachea;tongue;thyroid;ciliary ganglion;tonsil;skeletal muscle; 0.32980 0.21875 0.336225928 73.67893371 3276.78109 10.92393 KRT5 0.469327657850036 0.529553221328517 0.00111912082144647 keratin 5 . DISEASE: Epidermolysis bullosa simplex, Dowling-Meara type (DM- EBS) [MIM:131760]: A severe form of intraepidermal epidermolysis bullosa characterized by generalized herpetiform blistering, milia formation, dystrophic nails, and mucous membrane involvement. {ECO:0000269|PubMed:10730767, ECO:0000269|PubMed:12655565, ECO:0000269|PubMed:1372711, ECO:0000269|PubMed:16786515, ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:21623745, ECO:0000269|PubMed:8757772, ECO:0000269|PubMed:9036937, ECO:0000269|PubMed:9406827, ECO:0000269|PubMed:9989794, ECO:0000269|Ref.16}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa simplex, with migratory circinate erythema (EBSMCE) [MIM:609352]: A form of intraepidermal epidermolysis bullosa characterized by unusual migratory circinate erythema. Skin lesions appear from birth primarily on the hands, feet, and legs but spare nails, ocular epithelia and mucosae. Lesions heal with brown pigmentation but no scarring. Electron microscopy findings are distinct from those seen in the DM-EBS, with no evidence of tonofilament clumping. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa simplex, Weber-Cockayne type (WC- EBS) [MIM:131800]: A form of intraepidermal epidermolysis bullosa characterized by blistering limited to palmar and plantar areas of the skin. {ECO:0000269|PubMed:10782015, ECO:0000269|PubMed:12655565, ECO:0000269|PubMed:12707098, ECO:0000269|PubMed:14723728, ECO:0000269|PubMed:15140024, ECO:0000269|PubMed:15347343, ECO:0000269|PubMed:16786515, ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:21623745, ECO:0000269|PubMed:7506097, ECO:0000269|PubMed:7520042, ECO:0000269|PubMed:7688477, ECO:0000269|PubMed:8595431, ECO:0000269|PubMed:8807337, ECO:0000269|PubMed:9804357}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa simplex, Koebner type (K-EBS) [MIM:131900]: A form of intraepidermal epidermolysis bullosa characterized by generalized skin blistering. The phenotype is not fundamentally distinct from the Dowling-Meara type, although it is less severe. {ECO:0000269|PubMed:11407988, ECO:0000269|PubMed:11973334, ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:21623745, ECO:0000269|PubMed:7534039, ECO:0000269|PubMed:7686424, ECO:0000269|PubMed:9740251, ECO:0000269|PubMed:9989794}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa simplex, with mottled pigmentation (MP-EBS) [MIM:131960]: A form of intraepidermal epidermolysis bullosa characterized by blistering at acral sites and 'mottled' pigmentation of the trunk and proximal extremities with hyper- and hypopigmentation macules. {ECO:0000269|PubMed:10494094, ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:21623745, ECO:0000269|PubMed:8799157}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dowling-Degos disease 1 (DDD1) [MIM:179850]: An autosomal dominant genodermatosis. Affected individuals develop a postpubertal reticulate hyperpigmentation that is progressive and disfiguring, and small hyperkeratotic dark brown papules that affect mainly the flexures and great skin folds. Patients usually show no abnormalities of the hair or nails. {ECO:0000269|PubMed:16465624}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;larynx;gum;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);heart;lacrimal gland;tongue;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;macula lutea;visual apparatus;hypopharynx;head and neck;mammary gland; lung;trachea;tongue;tonsil;skin;thymus; 0.78233 0.59494 0.117584698 62.19037509 1967.54739 8.17400 KRT6A 0.948763036418681 0.0512033613009196 3.36022803994221e-05 keratin 6A FUNCTION: Epidermis-specific type I keratin involved in wound healing. Involved in the activation of follicular keratinocytes after wounding, while it does not play a major role in keratinocyte proliferation or migration. Participates in the regulation of epithelial migration by inhibiting the activity of SRC during wound repair. {ECO:0000250|UniProtKB:P50446}.; . TISSUE SPECIFICITY: Constitutively expressed in distinct types of epithelia such as those in oral mucosa, esophagus, papillae of tongue and hair follicle outer root sheath.; . . 0.31132 0.27311 0.714657953 85.81623024 2798.4726 9.98404 KRT6B 0.00479265544310742 0.966239227338555 0.0289681172183378 keratin 6B . . TISSUE SPECIFICITY: Constitutively expressed in distinct types of epithelia such as those in oral mucosa, esophagus, papillae of tongue and hair follicle outer root sheath.; unclassifiable (Anatomical System);heart;tongue;oral cavity;colon;skin;skeletal muscle;breast;uterus;pancreas;lung;oesophagus;larynx;gum;thyroid;placenta;visual apparatus;hypopharynx;cervix;head and neck;brain;mammary gland;bladder;aorta;stomach; superior cervical ganglion;tongue;atrioventricular node;trigeminal ganglion;skin;tonsil;skeletal muscle; 0.12487 . -0.304932527 32.24817174 532.75963 4.70795 KRT6C 4.10516812763235e-12 0.0131259010005479 0.986874098995347 keratin 6C . . TISSUE SPECIFICITY: Constitutively expressed in distinct types of epithelia such as those in oral mucosa, esophagus, papillae of tongue and hair follicle outer root sheath.; colon;skin;uterus;prostate;oesophagus;larynx;gum;thyroid;brain;bladder;unclassifiable (Anatomical System);tongue;oral cavity;skeletal muscle;breast;pancreas;lung;epididymis;adrenal gland;placenta;visual apparatus;hypopharynx;head and neck;cervix;mammary gland;stomach;aorta; . . . -0.170835809 40.65227648 8670.36163 20.14863 KRT7 2.78644976230631e-09 0.0830963264289383 0.916903670784612 keratin 7 FUNCTION: Blocks interferon-dependent interphase and stimulates DNA synthesis in cells. Involved in the translational regulation of the human papillomavirus type 16 E7 mRNA (HPV16 E7). {ECO:0000269|PubMed:10492017, ECO:0000269|PubMed:12072504}.; . TISSUE SPECIFICITY: Expressed in cultured epidermal, bronchial and mesothelial cells but absent in colon, ectocervix and liver. Observed throughout the glandular cells in the junction between stomach and esophagus but is absent in the esophagus. {ECO:0000269|PubMed:12359226, ECO:0000269|PubMed:2415537}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;urinary;colon;parathyroid;skin;breast;uterus;pancreas;prostate;lung;endometrium;placenta;visual apparatus;pituitary gland;liver;testis;amniotic fluid;cervix;kidney;brain;mammary gland;bladder;stomach; prostate;lung;smooth muscle;trachea;salivary gland;thyroid;placenta;fetal lung;fetal thyroid;skeletal muscle;skin; 0.32937 0.35293 1.067416815 91.66666667 400.49805 4.19868 KRT8 5.61440512780514e-06 0.673704609234957 0.326289776359915 keratin 8 FUNCTION: Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000269|PubMed:16000376}.; DISEASE: Cirrhosis (CIRRH) [MIM:215600]: A liver disease characterized by severe panlobular liver-cell swelling with Mallory body formation, prominent pericellular fibrosis, and marked deposits of copper. Clinical features include abdomen swelling, jaundice and pulmonary hypertension. {ECO:0000269|PubMed:12724528}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Observed in muscle fibers accumulating in the costameres of myoplasm at the sarcolemma membrane in structures that contain dystrophin and spectrin. Expressed in gingival mucosa and hard palate of the oral cavity. {ECO:0000269|PubMed:10973561, ECO:0000269|PubMed:16000376}.; lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;skin;uterus;prostate;endometrium;larynx;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;amnion;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; prostate;pancreas;lung;thyroid;placenta; . 0.83241 0.532823122 80.96249115 357.97558 4.00959 KRT8P1 . . . keratin 8 pseudogene 1 . . . . . . . . . . . KRT8P2 . . . keratin 8 pseudogene 2 . . . . . . . . . . . KRT8P3 . . . keratin 8 pseudogene 3 . . . . . . . . . . . KRT8P4 . . . keratin 8 pseudogene 4 . . . . . . . . . . . KRT8P5 . . . keratin 8 pseudogene 5 . . . . . . . . . . . KRT8P6 . . . keratin 8 pseudogene 6 . . . . . . . . . . . KRT8P7 . . . keratin 8 pseudogene 7 . . . . . . . . . . . KRT8P8 . . . keratin 8 pseudogene 8 . . . . . . . . . . . KRT8P9 . . . keratin 8 pseudogene 9 . . . . . . . . . . . KRT8P10 . . . keratin 8 pseudogene 10 . . . . . . . . . . . KRT8P11 . . . keratin 8 pseudogene 11 . . . . . 0.19551 . . . . . KRT8P12 . . . keratin 8 pseudogene 12 . . . . . . . . . . . KRT8P13 . . . keratin 8 pseudogene 13 . . . . . . . . . . . KRT8P14 . . . keratin 8 pseudogene 14 . . . . . . . . . . . KRT8P15 . . . keratin 8 pseudogene 15 . . . . . . . . . . . KRT8P16 . . . keratin 8 pseudogene 16 . . . . . . . . . . . KRT8P17 . . . keratin 8 pseudogene 17 . . . . . . . . . . . KRT8P18 . . . keratin 8 pseudogene 18 . . . . . . . . . . . KRT8P19 . . . keratin 8 pseudogene 19 . . . . . . . . . . . KRT8P20 . . . keratin 8 pseudogene 20 . . . . . . . . . . . KRT8P21 . . . keratin 8 pseudogene 21 . . . . . . . . . . . KRT8P22 . . . keratin 8 pseudogene 22 . . . . . . . . . . . KRT8P23 . . . keratin 8 pseudogene 23 . . . . . . . . . . . KRT8P24 . . . keratin 8 pseudogene 24 . . . . . . . . . . . KRT8P25 . . . keratin 8 pseudogene 25 . . . . . . . . . . . KRT8P26 . . . keratin 8 pseudogene 26 . . . . . . . . . . . KRT8P27 . . . keratin 8 pseudogene 27 . . . . . . . . . . . KRT8P28 . . . keratin 8 pseudogene 28 . . . . . . . . . . . KRT8P29 . . . keratin 8 pseudogene 29 . . . . . . . . . . . KRT8P30 . . . keratin 8 pseudogene 30 . . . . . . . . . . . KRT8P31 . . . keratin 8 pseudogene 31 . . . . . . . . . . . KRT8P32 . . . keratin 8 pseudogene 32 . . . . . . . . . . . KRT8P33 . . . keratin 8 pseudogene 33 . . . . . . . . . . . KRT8P34 . . . keratin 8 pseudogene 34 . . . . . . . . . . . KRT8P35 . . . keratin 8 pseudogene 35 . . . . . . . . . . . KRT8P36 . . . keratin 8 pseudogene 36 . . . . . . . . . . . KRT8P37 . . . keratin 8 pseudogene 37 . . . . . . . . . . . KRT8P38 . . . keratin 8 pseudogene 38 . . . . . . . . . . . KRT8P39 . . . keratin 8 pseudogene 39 . . . . . . . . . . . KRT8P40 . . . keratin 8 pseudogene 40 . . . . . . . . . . . KRT8P41 . . . keratin 8 pseudogene 41 . . . . . . . . . . . KRT8P42 . . . keratin 8 pseudogene 42 . . . . . . . . . . . KRT8P43 . . . keratin 8 pseudogene 43 . . . . . . . . . . . KRT8P44 . . . keratin 8 pseudogene 44 . . . . . . . . . . . KRT8P45 . . . keratin 8 pseudogene 45 . . . . . . . . . . . KRT8P46 . . . keratin 8 pseudogene 46 . . . . . . . . . . . KRT8P47 . . . keratin 8 pseudogene 47 . . . . . . . . . . . KRT8P48 . . . keratin 8 pseudogene 48 . . . . . . . . . . . KRT8P49 . . . keratin 8 pseudogene 49 . . . . . . . . . . . KRT8P50 . . . keratin 8 pseudogene 50 . . . . . . . . . . . KRT8P51 . . . keratin 8 pseudogene 51 . . . . . . . . . . . KRT9 0.00131873053723034 0.961722121391017 0.0369591480717532 keratin 9 FUNCTION: May serve an important special function either in the mature palmar and plantar skin tissue or in the morphogenetic program of the formation of these tissues. Plays a role in keratin filament assembly. {ECO:0000269|PubMed:10218578, ECO:0000269|PubMed:7507869}.; DISEASE: Keratoderma, palmoplantar, epidermolytic (EPPK) [MIM:144200]: A dermatological disorder characterized by diffuse thickening of the epidermis on the entire surface of palms and soles sharply bordered with erythematous margins. Some patients may present knuckle pads, thick pads of skin appearing over the proximal phalangeal joints. {ECO:0000269|PubMed:10632938, ECO:0000269|PubMed:10844507, ECO:0000269|PubMed:12072061, ECO:0000269|PubMed:12192490, ECO:0000269|PubMed:12838553, ECO:0000269|PubMed:12926810, ECO:0000269|PubMed:14675368, ECO:0000269|PubMed:15099359, ECO:0000269|PubMed:15115518, ECO:0000269|PubMed:15605275, ECO:0000269|PubMed:16911293, ECO:0000269|PubMed:16961539, ECO:0000269|PubMed:19874353, ECO:0000269|PubMed:20964665, ECO:0000269|PubMed:21715251, ECO:0000269|PubMed:7511021, ECO:0000269|PubMed:7512862, ECO:0000269|PubMed:7516304, ECO:0000269|PubMed:7523529, ECO:0000269|PubMed:7532199, ECO:0000269|PubMed:8647270, ECO:0000269|PubMed:9204965, ECO:0000269|PubMed:9856842}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the terminally differentiated epidermis of palms and soles. {ECO:0000269|PubMed:7507869}.; . . 0.16631 0.19904 -1.195919584 5.832743572 104.29558 2.20733 KRT10 0.0200626940208328 0.97613642933688 0.00380087664228697 keratin 10 . DISEASE: Epidermolytic hyperkeratosis (EHK) [MIM:113800]: An autosomal dominant skin disorder characterized by widespread blistering and an ichthyotic erythroderma at birth that persist into adulthood. Histologically there is a diffuse epidermolytic degeneration in the lower spinous layer of the epidermis. Within a few weeks from birth, erythroderma and blister formation diminish and hyperkeratoses develop. {ECO:0000269|PubMed:10201536, ECO:0000269|PubMed:1380725, ECO:0000269|PubMed:1381287, ECO:0000269|PubMed:21271994, ECO:0000269|PubMed:7507150, ECO:0000269|PubMed:7507152, ECO:0000269|PubMed:7508181, ECO:0000269|PubMed:7512983, ECO:0000269|Ref.7}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ichthyosis annular epidermolytic (AEI) [MIM:607602]: A skin disorder resembling bullous congenital ichthyosiform erythroderma. Affected individuals present with bullous ichthyosis in early childhood and hyperkeratotic lichenified plaques in the flexural areas and extensor surfaces at later ages. The feature that distinguishes AEI from BCIE is dramatic episodes of flares of annular polycyclic plaques with scale, which coalesce to involve most of the body surface and can persist for several weeks or even months. {ECO:0000269|PubMed:9036939, ECO:0000269|PubMed:9856845}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Erythroderma, ichthyosiform, congenital reticular (CRIE) [MIM:609165]: A rare skin condition characterized by slowly enlarging islands of normal skin surrounded by erythematous ichthyotic patches in a reticulated pattern. The condition starts in infancy as a lamellar ichthyosis, with small islands of normal skin resembling confetti appearing in late childhood and at puberty. Histopathologic findings include band-like parakeratosis, psoriasiform acanthosis, and vacuolization of keratinocytes with binucleated cells in the upper epidermis, sometimes associated with amyloid deposition in the dermis. Ultrastructural abnormalities include perinuclear shells formed from a network of fine filaments in the upper epidermis. {ECO:0000269|PubMed:20798280}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Seen in all suprabasal cell layers including stratum corneum.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;oesophagus;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;epidermis;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta; testis - interstitial;superior cervical ganglion;prostate;testis - seminiferous tubule;tongue;testis;skin; 0.54103 0.54019 0.220536484 68.38287332 1152.47941 6.46886 KRT12 9.44137233590707e-11 0.0809302885803022 0.919069711325284 keratin 12 FUNCTION: May play a unique role in maintaining the normal corneal epithelial function. Together with KRT3, essential for the maintenance of corneal epithelium integrity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Cornea specific. {ECO:0000269|PubMed:8759347}.; unclassifiable (Anatomical System);optic nerve;trabecular meshwork;macula lutea;visual apparatus;fovea centralis;choroid;lens;retina; superior cervical ganglion;globus pallidus;skeletal muscle; 0.21898 0.21502 0.50895761 80.20169851 717.36097 5.31581 KRT13 0.00166754074952747 0.890280100310334 0.108052358940138 keratin 13 . DISEASE: White sponge nevus 2 (WSN2) [MIM:615785]: A rare disorder characterized by the presence of soft, white, and spongy plaques in the oral mucosa. The characteristic histopathologic features are epithelial thickening, parakeratosis, and vacuolization of the suprabasal layer of oral epithelial keratinocytes. Less frequently the mucous membranes of the nose, esophagus, genitalia and rectum are involved. {ECO:0000269|PubMed:10561721, ECO:0000269|PubMed:11379896, ECO:0000269|PubMed:14600690, ECO:0000269|PubMed:7493031}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in some epidermal sweat gland ducts (at protein level) and in exocervix, esophagus and placenta. {ECO:0000269|PubMed:2483837}.; colon;skin;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;synovium;larynx;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);heart;tongue;oral cavity;urinary;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;hypopharynx;head and neck;cervix;mammary gland;stomach; trachea;tongue;tonsil; 0.09532 . 0.644875971 84.10002359 136.71209 2.54097 KRT14 0.0673429842229222 0.918586449601398 0.0140705661756797 keratin 14 FUNCTION: The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro. {ECO:0000269|PubMed:11724817}.; DISEASE: Epidermolysis bullosa simplex, Dowling-Meara type (DM- EBS) [MIM:131760]: A severe form of intraepidermal epidermolysis bullosa characterized by generalized herpetiform blistering, milia formation, dystrophic nails, and mucous membrane involvement. {ECO:0000269|PubMed:10583131, ECO:0000269|PubMed:10730767, ECO:0000269|PubMed:10733662, ECO:0000269|PubMed:10820403, ECO:0000269|PubMed:11710919, ECO:0000269|PubMed:12603865, ECO:0000269|PubMed:12655565, ECO:0000269|PubMed:12707098, ECO:0000269|PubMed:14987259, ECO:0000269|PubMed:16786515, ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:1717157, ECO:0000269|PubMed:7561171, ECO:0000269|PubMed:7688405, ECO:0000269|PubMed:8601736, ECO:0000269|PubMed:9804355, ECO:0000269|PubMed:9989794, ECO:0000269|Ref.30}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa simplex, Weber-Cockayne type (WC- EBS) [MIM:131800]: A form of intraepidermal epidermolysis bullosa characterized by blistering limited to palmar and plantar areas of the skin. {ECO:0000269|PubMed:10733662, ECO:0000269|PubMed:12603865, ECO:0000269|PubMed:12655565, ECO:0000269|PubMed:12707098, ECO:0000269|PubMed:14987259, ECO:0000269|PubMed:16786515, ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:7506097, ECO:0000269|PubMed:7506606, ECO:0000269|PubMed:7561171, ECO:0000269|PubMed:9284105, ECO:0000269|PubMed:9804357, ECO:0000269|PubMed:9989794}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa simplex, Koebner type (K-EBS) [MIM:131900]: A form of intraepidermal epidermolysis bullosa characterized by generalized skin blistering. The phenotype is not fundamentally distinct from the Dowling-Meara type, although it is less severe. {ECO:0000269|PubMed:10733662, ECO:0000269|PubMed:10820403, ECO:0000269|PubMed:11710919, ECO:0000269|PubMed:16786515, ECO:0000269|PubMed:1720261, ECO:0000269|PubMed:7526926, ECO:0000269|PubMed:7682883, ECO:0000269|PubMed:9989794, ECO:0000269|Ref.10, ECO:0000269|Ref.30}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa simplex, autosomal recessive 1 (EBSB1) [MIM:601001]: An intraepidermal epidermolysis bullosa characterized by localized blistering on the dorsal, lateral and plantar surfaces of the feet. {ECO:0000269|PubMed:7526933}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Naegeli-Franceschetti-Jadassohn syndrome (NFJS) [MIM:161000]: A rare autosomal dominant form of ectodermal dysplasia. The cardinal features are absence of dermatoglyphics (fingerprints), reticular cutaneous hyperpigmentation (starting at about the age of 2 years without a preceding inflammatory stage), palmoplantar keratoderma, hypohidrosis with diminished sweat gland function and discomfort provoked by heat, nail dystrophy, and tooth enamel defects. {ECO:0000269|PubMed:16960809}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dermatopathia pigmentosa reticularis (DPR) [MIM:125595]: A rare ectodermal dysplasia characterized by lifelong persistent reticulate hyperpigmentation, non-cicatricial alopecia, and nail dystrophy. Variable features include adermatoglyphia, hypohidrosis or hyperhidrosis, and palmoplantar hyperkeratosis. {ECO:0000269|PubMed:16960809}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in the basal layer, lowered within the more apically located layers specifically in the stratum spinosum, stratum granulosum but is not detected in stratum corneum. Strongly expressed in the outer root sheath of anagen follicles but not in the germinative matrix, inner root sheath or hair. Found in keratinocytes surrounding the club hair during telogen. {ECO:0000269|PubMed:9457912}.; unclassifiable (Anatomical System);cartilage;heart;tongue;hypothalamus;colon;skin;breast;uterus;prostate;optic nerve;lung;oesophagus;adrenal gland;larynx;gum;thyroid;placenta;visual apparatus;hypopharynx;head and neck;brain;mammary gland;bladder; dorsal root ganglion;lung;olfactory bulb;trachea;tongue;placenta;atrioventricular node;trigeminal ganglion;skin;tonsil;thymus; 0.32557 . -0.067881249 48.69072895 2570.30464 9.47522 KRT15 3.50793987342309e-15 0.00282390261147197 0.997176097388525 keratin 15 . . TISSUE SPECIFICITY: Expressed in a discontinuous manner in the basal cell layer of adult skin epidermis, but continuously in the basal layer of fetal skin epidermis and nail. Also expressed in the outer root sheath above the hair bulb in hair follicle (at protein level). Expressed homogeneously in all cell layers of the esophagus and exocervix, but detected in the basal cell layer only of oral mucosa, skin and in the basal plus the next two layers of the suprabasal epithelium of the palate. {ECO:0000269|PubMed:10084315, ECO:0000269|PubMed:2452170}.; colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;oesophagus;larynx;testis;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;lens;breast;lung;adrenal gland;nasopharynx;visual apparatus;macula lutea;spleen;head and neck;mammary gland;stomach; prostate;trachea;tongue;skin;tonsil;thymus; 0.13823 0.21326 0.801024817 87.65628686 1238.74499 6.64574 KRT16 2.17483656210401e-09 0.0721533494751693 0.927846648349994 keratin 16 FUNCTION: Epidermis-specific type I keratin that plays a key role in skin. Acts as a regulator of innate immunity in response to skin barrier breach: required for some inflammatory checkpoint for the skin barrier maintenance. {ECO:0000250|UniProtKB:Q9Z2K1}.; DISEASE: Pachyonychia congenita 1 (PC1) [MIM:167200]: An autosomal dominant ectodermal dysplasia characterized by hypertrophic nail dystrophy resulting in onchyogryposis (thickening and increase in curvature of the nail), palmoplantar keratoderma, follicular hyperkeratosis, and oral leukokeratosis. Hyperhidrosis of the hands and feet is usually present. {ECO:0000269|PubMed:10521820, ECO:0000269|PubMed:10606845, ECO:0000269|PubMed:10839714, ECO:0000269|PubMed:11359398, ECO:0000269|PubMed:11886499, ECO:0000269|PubMed:16250206, ECO:0000269|PubMed:17719747, ECO:0000269|PubMed:21160496, ECO:0000269|PubMed:21326300, ECO:0000269|PubMed:22668561, ECO:0000269|PubMed:24118415, ECO:0000269|PubMed:7539673}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Keratoderma, palmoplantar, non-epidermolytic, focal 1 (FNEPPK1) [MIM:613000]: A dermatological disorder characterized by non-epidermolytic palmoplantar keratoderma limited to the pressure points on the balls of the feet, with later mild involvement on the palms. Oral, genital and follicular keratotic lesions are often present. {ECO:0000269|PubMed:8595410}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Unilateral palmoplantar verrucous nevus (UPVN) [MIM:144200]: UPVN is characterized by a localized epidermolytic hyperkeratosis in parts of the right palm and the right sole, following the lines of Blaschko. {ECO:0000269|PubMed:10844556}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=KRT16 and KRT17 are coexpressed only in pathological situations such as metaplasias and carcinomas of the uterine cervix and in psoriasis vulgaris.; TISSUE SPECIFICITY: Expressed in the hair follicle, nail bed and in mucosal stratified squamous epithelia and, suprabasally, in oral epithelium and palmoplantar epidermis. Also found in luminal cells of sweat and mammary gland ducts.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;oesophagus;endometrium;larynx;gum;thyroid;brain;bladder;unclassifiable (Anatomical System);heart;tongue;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;epididymis;placenta;hypopharynx;head and neck;cervix;mammary gland;stomach; tongue;skin;skeletal muscle; 0.16969 0.47926 0.644875971 84.10002359 377.72971 4.09712 KRT16P1 . . . keratin 16 pseudogene 1 . . . . . . . . . . . KRT16P2 . . . keratin 16 pseudogene 2 . . . . . . . . . . . KRT16P3 . . . keratin 16 pseudogene 3 . . . . . . . . . . . KRT16P4 . . . keratin 16 pseudogene 4 . . . . . . . . . . . KRT16P5 . . . keratin 16 pseudogene 5 . . . . . . . . . . . KRT16P6 . . . keratin 16 pseudogene 6 . . . . . . . . . . . KRT17 7.07353949751571e-06 0.722413326404874 0.277579600055629 keratin 17 FUNCTION: Type I keratin involved in the formation and maintenance of various skin appendages, specifically in determining shape and orientation of hair (By similarity). Required for the correct growth of hair follicles, in particular for the persistence of the anagen (growth) state (By similarity). Modulates the function of TNF-alpha in the specific context of hair cycling. Regulates protein synthesis and epithelial cell growth through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway (By similarity). Involved in tissue repair. May be a marker of basal cell differentiation in complex epithelia and therefore indicative of a certain type of epithelial "stem cells". Acts as a promoter of epithelial proliferation by acting a regulator of immune response in skin: promotes Th1/Th17-dominated immune environment contributing to the development of basaloid skin tumors (By similarity). May act as an autoantigen in the immunopathogenesis of psoriasis, with certain peptide regions being a major target for autoreactive T-cells and hence causing their proliferation. {ECO:0000250|UniProtKB:Q9QWL7, ECO:0000269|PubMed:10844551, ECO:0000269|PubMed:15795121, ECO:0000269|PubMed:16713453}.; DISEASE: Pachyonychia congenita 2 (PC2) [MIM:167210]: An autosomal dominant ectodermal dysplasia characterized by hypertrophic nail dystrophy resulting in onchyogryposis (thickening and increase in curvature of the nail), palmoplantar keratoderma and hyperhidrosis, follicular hyperkeratosis, multiple epidermal cysts, absent/sparse eyebrow and body hair, and by the presence of natal teeth. {ECO:0000269|PubMed:10571744, ECO:0000269|PubMed:11348474, ECO:0000269|PubMed:11874497, ECO:0000269|PubMed:11886499, ECO:0000269|PubMed:15102078, ECO:0000269|PubMed:15795125, ECO:0000269|PubMed:16250206, ECO:0000269|PubMed:16620218, ECO:0000269|PubMed:16625196, ECO:0000269|PubMed:17719747, ECO:0000269|PubMed:18547302, ECO:0000269|PubMed:19470054, ECO:0000269|PubMed:21326300, ECO:0000269|PubMed:23278621, ECO:0000269|PubMed:23855588, ECO:0000269|PubMed:7539673, ECO:0000269|PubMed:9008238, ECO:0000269|PubMed:9767294}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Steatocystoma multiplex (SM) [MIM:184500]: Disease characterized by round or oval cystic tumors widely distributed on the back, anterior trunk, arms, scrotum, and thighs. {ECO:0000269|PubMed:16620218, ECO:0000269|PubMed:9008238, ECO:0000269|PubMed:9767294}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=KRT16 and KRT17 are coexpressed only in pathological situations such as metaplasias and carcinomas of the uterine cervix and in psoriasis vulgaris.; TISSUE SPECIFICITY: Expressed in the outer root sheath and medulla region of hair follicle specifically from eyebrow and beard, digital pulp, nail matrix and nail bed epithelium, mucosal stratified squamous epithelia and in basal cells of oral epithelium, palmoplantar epidermis and sweat and mammary glands. Also expressed in myoepithelium of prostate, basal layer of urinary bladder, cambial cells of sebaceous gland and in exocervix (at protein level). {ECO:0000269|PubMed:10651700, ECO:0000269|PubMed:10844551, ECO:0000269|PubMed:1281771, ECO:0000269|PubMed:2481679}.; ovary;salivary gland;intestine;colon;skin;uterus;prostate;larynx;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);trophoblast;tongue;muscle;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;head and neck;cervix;kidney; superior cervical ganglion;prostate;lung;trachea;tongue;globus pallidus;skin;skeletal muscle; . 0.22756 -0.244249595 36.17008728 729.66866 5.36212 KRT17P1 . . . keratin 17 pseudogene 1 . . . . . . . . . . . KRT17P2 . . . keratin 17 pseudogene 2 . . . . . . . . . . . KRT17P3 . . . keratin 17 pseudogene 3 . . . . . . . . . . . KRT17P4 . . . keratin 17 pseudogene 4 . . . . . . . . . . . KRT17P5 . . . keratin 17 pseudogene 5 . . . . . . . . . . . KRT17P6 . . . keratin 17 pseudogene 6 . . . . . . . . . . . KRT17P7 . . . keratin 17 pseudogene 7 . . . . . . . . . . . KRT17P8 . . . keratin 17 pseudogene 8 . . . . . . . . . . . KRT18 0.62478258844471 0.373648914604785 0.00156849695050502 keratin 18 FUNCTION: Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. {ECO:0000250, ECO:0000269|PubMed:15529338, ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8522591, ECO:0000269|PubMed:9298992, ECO:0000269|PubMed:9524113}.; DISEASE: Cirrhosis (CIRRH) [MIM:215600]: A liver disease characterized by severe panlobular liver-cell swelling with Mallory body formation, prominent pericellular fibrosis, and marked deposits of copper. Clinical features include abdomen swelling, jaundice and pulmonary hypertension. {ECO:0000269|PubMed:12724528, ECO:0000269|PubMed:9011570}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in colon, placenta, liver and very weakly in exocervix. Increased expression observed in lymph nodes of breast carcinoma. {ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:2422083, ECO:0000269|PubMed:2434380, ECO:0000269|PubMed:2434381}.; . . . 0.13495 -0.271755481 34.31823543 44.64658 1.28163 KRT18P1 . . . keratin 18 pseudogene 1 . . . . . . . . . . . KRT18P2 . . . keratin 18 pseudogene 2 . . . . . . . . . . . KRT18P3 . . . keratin 18 pseudogene 3 . . . . . . . . . . . KRT18P4 . . . keratin 18 pseudogene 4 . . . . . . . . . . . KRT18P5 . . . keratin 18 pseudogene 5 . . . . . . . . . . . KRT18P6 . . . keratin 18 pseudogene 6 . . . . . . . . . . . KRT18P7 . . . keratin 18 pseudogene 7 . . . . . . . . . . . KRT18P8 . . . keratin 18 pseudogene 8 . . . . . . . . . . . KRT18P9 . . . keratin 18 pseudogene 9 . . . . . . . . . . . KRT18P10 . . . keratin 18 pseudogene 10 . . . . . . . . . . . KRT18P11 . . . keratin 18 pseudogene 11 . . . . . . . . . . . KRT18P12 . . . keratin 18 pseudogene 12 . . . . . . . . . . . KRT18P13 . . . keratin 18 pseudogene 13 . . . . . . . . . . . KRT18P14 . . . keratin 18 pseudogene 14 . . . . . . . . . . . KRT18P15 . . . keratin 18 pseudogene 15 . . . . . . . . . . . KRT18P16 . . . keratin 18 pseudogene 16 . . . . . . . . . . . KRT18P17 . . . keratin 18 pseudogene 17 . . . . . . . . . . . KRT18P18 . . . keratin 18 pseudogene 18 . . . . . . . . . . . KRT18P19 . . . keratin 18 pseudogene 19 . . . . . . . . . . . KRT18P20 . . . keratin 18 pseudogene 20 . . . . . . . . . . . KRT18P21 . . . keratin 18 pseudogene 21 . . . . . . . . . . . KRT18P22 . . . keratin 18 pseudogene 22 . . . . . . . . . . . KRT18P23 . . . keratin 18 pseudogene 23 . . . . . . . . . . . KRT18P24 . . . keratin 18 pseudogene 24 . . . . . . . . . . . KRT18P25 . . . keratin 18 pseudogene 25 . . . . . . . . . . . KRT18P26 . . . keratin 18 pseudogene 26 . . . . . . . . . . . KRT18P27 . . . keratin 18 pseudogene 27 . . . . . . . . . . . KRT18P28 . . . keratin 18 pseudogene 28 . . . . . . . . . . . KRT18P29 . . . keratin 18 pseudogene 29 . . . . . . . . . . . KRT18P30 . . . keratin 18 pseudogene 30 . . . . . . . . . . . KRT18P31 . . . keratin 18 pseudogene 31 . . . . . . . . . . . KRT18P32 . . . keratin 18 pseudogene 32 . . . . . . . . . . . KRT18P33 . . . keratin 18 pseudogene 33 . . . . . . . . . . . KRT18P34 . . . keratin 18 pseudogene 34 . . . . . . . . . . . KRT18P35 . . . keratin 18 pseudogene 35 . . . . . . . . . . . KRT18P36 . . . keratin 18 pseudogene 36 . . . . . . . . . . . KRT18P37 . . . keratin 18 pseudogene 37 . . . . . . . . . . . KRT18P38 . . . keratin 18 pseudogene 38 . . . . . . . . . . . KRT18P39 . . . keratin 18 pseudogene 39 . . . . . . . . . . . KRT18P40 . . . keratin 18 pseudogene 40 . . . . . . . . . . . KRT18P41 . . . keratin 18 pseudogene 41 . . . . . . . . . . . KRT18P42 . . . keratin 18 pseudogene 42 . . . . . . . . . . . KRT18P43 . . . keratin 18 pseudogene 43 . . . . . . . . . . . KRT18P44 . . . keratin 18 pseudogene 44 . . . . . . . . . . . KRT18P45 . . . keratin 18 pseudogene 45 . . . . . . . . . . . KRT18P46 . . . keratin 18 pseudogene 46 . . . . . . . . . . . KRT18P47 . . . keratin 18 pseudogene 47 . . . . . . . . . . . KRT18P48 . . . keratin 18 pseudogene 48 . . . . . . . . . . . KRT18P49 . . . keratin 18 pseudogene 49 . . . . . . . . . . . KRT18P50 . . . keratin 18 pseudogene 50 . . . . . . . . . . . KRT18P51 . . . keratin 18 pseudogene 51 . . . . . . . . . . . KRT18P52 . . . keratin 18 pseudogene 52 . . . . . . . . . . . KRT18P53 . . . keratin 18 pseudogene 53 . . . . . . . . . . . KRT18P54 . . . keratin 18 pseudogene 54 . . . . . . . . . . . KRT18P55 . . . keratin 18 pseudogene 55 . . . . . . . . . . . KRT18P56 . . . keratin 18 pseudogene 56 . . . . . . . . . . . KRT18P57 . . . keratin 18 pseudogene 57 . . . . . . . . . . . KRT18P58 . . . keratin 18 pseudogene 58 . . . . . . . . . . . KRT18P59 . . . keratin 18 pseudogene 59 . . . . . . . . . . . KRT18P60 . . . keratin 18 pseudogene 60 . . . . . . . . . . . KRT18P61 . . . keratin 18 pseudogene 61 . . . . . . . . . . . KRT18P62 . . . keratin 18 pseudogene 62 . . . . . . . . . . . KRT18P63 . . . keratin 18 pseudogene 63 . . . . . . . . . . . KRT18P64 . . . keratin 18 pseudogene 64 . . . . . . . . . . . KRT18P65 . . . keratin 18 pseudogene 65 . . . . . . . . . . . KRT18P66 . . . keratin 18 pseudogene 66 . . . . . . . . . . . KRT18P67 . . . keratin 18 pseudogene 67 . . . . . . . . . . . KRT18P68 . . . keratin 18 pseudogene 68 . . . . . . . . . . . KRT19 0.0039364547878244 0.958391839575841 0.0376717056363349 keratin 19 FUNCTION: Involved in the organization of myofibers. Together with KRT8, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000269|PubMed:16000376}.; . TISSUE SPECIFICITY: Expressed in a defined zone of basal keratinocytes in the deep outer root sheath of hair follicles. Also observed in sweat gland and mammary gland ductal and secretory cells, bile ducts, gastrointestinal tract, bladder urothelium, oral epithelia, esophagus, ectocervical epithelium (at protein level). Expressed in epidermal basal cells, in nipple epidermis and a defined region of the hair follicle. Also seen in a subset of vascular wall cells in both the veins and artery of human umbilical cord, and in umbilical cord vascular smooth muscle. Observed in muscle fibers accumulating in the costameres of myoplasm at the sarcolemma in structures that contain dystrophin and spectrin. {ECO:0000269|PubMed:16000376, ECO:0000269|PubMed:2468493, ECO:0000269|PubMed:2469734}.; lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;endometrium;larynx;thyroid;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;urinary;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;thymus; . 0.10608 0.62860 -0.156065314 42.16206653 78.67902 1.87179 KRT19P1 . . . keratin 19 pseudogene 1 . . . . . . . . . . . KRT19P2 . . . keratin 19 pseudogene 2 . . . . . . . . . . . KRT19P3 . . . keratin 19 pseudogene 3 . . . . . . . . . . . KRT19P4 . . . keratin 19 pseudogene 4 . . . . . . . . . . . KRT19P6 . . . keratin 19 pseudogene 6 . . . . . . . . . . . KRT20 5.57987712160891e-06 0.672378198121624 0.327616222001254 keratin 20 FUNCTION: Plays a significant role in maintaining keratin filament organization in intestinal epithelia. When phosphorylated, plays a role in the secretion of mucin in the small intestine (By similarity). {ECO:0000250, ECO:0000269|PubMed:12857878, ECO:0000269|PubMed:16608857}.; . TISSUE SPECIFICITY: Expressed predominantly in the intestinal epithelium. Expressed in luminal cells of colonic mucosa. Also expressed in the Merkel cells of keratinized oral mucosa; specifically at the tips of some rete ridges of the gingival mucosa, in the basal layer of the palatal mucosa and in the taste buds of lingual mucosa. {ECO:0000269|PubMed:10973561, ECO:0000269|PubMed:1696264}.; unclassifiable (Anatomical System);small intestine;colon;kidney;skeletal muscle;stomach; pancreas;atrioventricular node; 0.33628 0.25521 0.176444282 66.07100731 89.49778 2.03437 KRT23 2.8268268115206e-08 0.292716317707153 0.707283654024579 keratin 23 . . . myocardium;medulla oblongata;ovary;colon;parathyroid;bone marrow;prostate;endometrium;larynx;thyroid;testis;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;breast;pancreas;lung;placenta;hypopharynx;alveolus;liver;spleen;head and neck;stomach; testis - interstitial;testis - seminiferous tubule;salivary gland;placenta;testis;whole blood;skin; 0.44802 0.12548 0.50895761 80.20169851 476.54561 4.51030 KRT24 5.0932770269769e-13 0.014237391569271 0.98576260843022 keratin 24 . . TISSUE SPECIFICITY: Highly expressed in keratinocytes, placenta, colon and spleen. Expressed at lower level in thymus and testis. {ECO:0000269|PubMed:12230514}.; heart;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;placenta;macula lutea;hypopharynx;testis;head and neck; superior cervical ganglion;placenta;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22178 0.06544 1.091286379 91.89667374 7498.09542 18.59961 KRT25 1.84752983103555e-06 0.673987727946471 0.326010424523698 keratin 25 FUNCTION: Essential for the proper assembly of type I and type II keratin protein complexes and formation of keratin intermediate filaments in the inner root sheath (irs). {ECO:0000250|UniProtKB:Q8VCW2}.; . TISSUE SPECIFICITY: Strongly expressed in skin and scalp, and weak expression observed in thymus and tongue. In the hair follicle, expressed in Henle layer, Huxley layer and in the inner root sheath cuticle of the hair follicle. Expression extends from the bulb region up to the point of differentiation into the three layers. Also present in the medulla of beard hair (at protein level). {ECO:0000269|PubMed:15617563, ECO:0000269|PubMed:16874310}.; heart; . 0.19429 0.10207 0.154398214 64.73814579 2065.19279 8.37548 KRT26 7.22811733131092e-10 0.135928948819062 0.864071050458126 keratin 26 . . TISSUE SPECIFICITY: Strongly expressed in skin and scalp, and weak expression observed in thymus and tongue. In the hair follicle, expression is restricted to the mid- to upper inner root sheath cuticle, being present slightly above the apex of the dermal papilla (at protein level). {ECO:0000269|PubMed:15617563, ECO:0000269|PubMed:16874310}.; heart; . 0.17637 . 1.464302001 95.23472517 2191.93566 8.62218 KRT27 8.00950013085285e-14 0.0048035191235066 0.995196480876413 keratin 27 FUNCTION: Essential for the proper assembly of type I and type II keratin protein complexes and formation of keratin intermediate filaments in the inner root sheath (irs). {ECO:0000250|UniProtKB:Q9Z320}.; . TISSUE SPECIFICITY: Strongly expressed in skin and scalp. In the hair follicle, expressed in Henle layer, Huxley layer and in the inner root sheath cuticle of the hair follicle. Expression extends from the bulb region up to the point of differentiation into the three layers. Also present in the medulla of beard hair (at protein level). {ECO:0000269|PubMed:15617563, ECO:0000269|PubMed:16874310}.; uterus;heart;skin; . 0.52706 0.10643 1.598424456 95.88346308 9407.33834 21.00993 KRT28 2.06905632889003e-07 0.444657273795555 0.555342519298813 keratin 28 FUNCTION: Essential for the proper assembly of types I and II keratin protein complexes and the formation of keratin intermediate filaments in the inner root sheath (irs). {ECO:0000250|UniProtKB:A6BLY7}.; . TISSUE SPECIFICITY: Strongly expressed in skin and scalp, and weak expression observed in thymus. In the hair follicle, expressed in Henle layer, Huxley layer and in the irs cuticle. Expression extends from the bulb region up to the point of differentiation into the three layers. Also present in the medulla of beard hair (at protein level). {ECO:0000269|PubMed:15617563, ECO:0000269|PubMed:16874310}.; unclassifiable (Anatomical System);uterus;heart;skin; . 0.23678 . 0.799205007 87.58551545 1734.99101 7.68359 KRT31 0.928538285568948 0.0713838571899355 7.78572411161715e-05 keratin 31 . . TISSUE SPECIFICITY: Present in scalp but not in hairless skin. Abundantly expressed in the differentiating cortex of growing (anagen) hair. Expression is restricted to the keratinocytes of the hair cortex and is absent from inner root sheath and medulla. {ECO:0000269|PubMed:9457912, ECO:0000269|PubMed:9756910}.; heart;muscle;colon;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;oesophagus;endometrium;larynx;thyroid;macula lutea;head and neck;cerebellum; trigeminal ganglion; 0.20184 0.20933 0.156217551 64.82071243 522.22335 4.66483 KRT32 1.20905836070872e-15 0.000782799319111556 0.999217200680887 keratin 32 . . TISSUE SPECIFICITY: Restricted to the hair cuticle.; unclassifiable (Anatomical System);lung;heart;colon; superior cervical ganglion;appendix;atrioventricular node;pons; 0.14668 0.17962 3.427299372 99.46331682 13006.68225 24.40066 KRT33A 2.0406295819065e-11 0.0174977715497919 0.982502228429802 keratin 33A . . TISSUE SPECIFICITY: Expressed in the hair follicles. {ECO:0000269|PubMed:9756910}.; heart; superior cervical ganglion;uterus corpus;cerebellum peduncles;trigeminal ganglion;skeletal muscle; 0.10214 0.12541 0.845119304 88.4170795 3414.0807 11.20769 KRT33B 2.3968705772229e-06 0.490002591687786 0.509995011441637 keratin 33B . . . kidney; superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.26309 . 0.733063566 86.27034678 554.64979 4.78478 KRT34 2.61055759222008e-06 0.507828623815407 0.492168765627001 keratin 34 . . TISSUE SPECIFICITY: Expressed in the hair follicles. {ECO:0000269|PubMed:9756910}.; cartilage;heart;skin;bone marrow; dorsal root ganglion;testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15959 0.14788 0.914904347 89.55531965 1341.18865 6.87423 KRT35 0.017032337828936 0.960141958881174 0.0228257032898901 keratin 35 . . TISSUE SPECIFICITY: Early expression in the hair follicle, mainly found in supramatricial cells and lowermost cortical cells of the hair bulb. {ECO:0000269|PubMed:8823373}.; uterus;heart;larynx;colon;head and neck;skin; atrioventricular node;trigeminal ganglion; 0.11567 0.11898 0.604424343 82.90280727 1949.21087 8.12325 KRT36 3.98218636136565e-09 0.10170318686634 0.898296809151474 keratin 36 . . TISSUE SPECIFICITY: Expressed in the hair follicles. {ECO:0000269|PubMed:9756910}.; lung;colon; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.15976 0.14169 1.445891753 95.12267044 6933.14128 17.74129 KRT37 0.000453720807150653 0.866781038533427 0.132765240659422 keratin 37 . . . colon; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.11467 0.11104 1.782126607 96.85067233 10272.91126 22.12143 KRT38 2.17177355501335e-05 0.724250939431988 0.275727342832462 keratin 38 . . . colon; . 0.08393 0.11230 -0.33061537 30.82094834 172.03352 2.86058 KRT39 8.45580252239315e-09 0.279099702346341 0.720900289197857 keratin 39 FUNCTION: May play a role in late hair differentiation.; . TISSUE SPECIFICITY: Expressed in skin and scalp. In the hair follicle, it is present in the upper hair cuticle and the upper cortex. Also present in the in the upper portion of beard hairs (at protein level). {ECO:0000269|PubMed:15617563, ECO:0000269|PubMed:17301834}.; placenta; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.08205 0.778977686 87.21396556 2188.61987 8.61734 KRT40 0.000203216938490707 0.905193581214071 0.0946032018474385 keratin 40 FUNCTION: May play a role in late hair differentiation.; . TISSUE SPECIFICITY: Expressed in skin and scalp. Also very weakly expressed in tongue, breast, colon and small intestine. In the hair follicle, it is specifically present in the upper hair cuticle. Not present in the upper cortex (at protein level). {ECO:0000269|PubMed:15617563, ECO:0000269|PubMed:17301834}.; . . . 0.08721 3.201139412 99.34536447 18636.39691 29.11113 KRT41P . . . keratin 41 pseudogene . . . . . . . . . . . KRT42P . . . keratin 42 pseudogene . . . . . 0.12701 . . . . . KRT43P . . . keratin 43 pseudogene . . . . . . . . . . . KRT71 3.12740120353346e-08 0.307921702058716 0.692078266667272 keratin 71 FUNCTION: Plays a central role in hair formation. Essential component of keratin intermediate filaments in the inner root sheath (IRS) of the hair follicle. {ECO:0000269|PubMed:22592156}.; DISEASE: Hypotrichosis 13 (HYPT13) [MIM:615896]: A form of hypotrichosis, a condition characterized by the presence of less than the normal amount of hair and abnormal hair follicles and shafts, which are thin and atrophic. The extent of scalp and body hair involvement can be very variable, within as well as between families. HYPT13 is characterized by sparse woolly hair. {ECO:0000269|PubMed:22592156}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in hair follicles from scalp. Specifically expressed in the inner root sheath (IRS) of the hair follicle. Present in the all 3 IRS layers: the cuticle, the Henle and the Huxley layers. Also detected in the pseudopods of specialized Huxley cells, termed Fluegelzellen, along the area of differentiated Henle cells (at protein level). {ECO:0000269|PubMed:11982755, ECO:0000269|PubMed:12648212, ECO:0000269|PubMed:16874310, ECO:0000269|PubMed:22592156}.; uterus;heart;skin; . 0.18273 0.10913 1.026965723 91.08870017 6944.13349 17.75451 KRT72 3.06920505425378e-05 0.791590647903091 0.208378660046366 keratin 72 FUNCTION: Has a role in hair formation. Specific component of keratin intermediate filaments in the inner root sheath (IRS) of the hair follicle (Probable). {ECO:0000305}.; . TISSUE SPECIFICITY: Highly expressed in hair follicles from scalp and eyebrow. Also expressed in palmoplantar epidermis. Not expressed in face skin despite the presence of fine hairs histologically. In hair, it is specifically present in the inner root sheath (IRS) of the hair follicle. Present in the IRS cuticle, but not in Henle or Huxley layers of the IRS. In the IRS cuticle, its presence is delayed up to the height of the apex of the dermal papilla (at protein level). {ECO:0000269|PubMed:11703281, ECO:0000269|PubMed:12648212, ECO:0000269|PubMed:16874310}.; unclassifiable (Anatomical System);lung;heart;testis; superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.23170 0.11154 0.958999345 90.17456947 11886.46988 23.56826 KRT73 2.00824929501873e-11 0.0331814027740038 0.966818597205914 keratin 73 FUNCTION: Has a role in hair formation. Specific component of keratin intermediate filaments in the inner root sheath (IRS) of the hair follicle (Probable). {ECO:0000305}.; . TISSUE SPECIFICITY: Highly expressed in hair follicles from scalp. In hair, it is specifically present in the inner root sheath (IRS) of the hair follicle. Present in the IRS cuticle, but not in Henle or Huxley layers of the IRS. In the IRS cuticle, it is expressed between the lowermost bulb region of the cuticle and the region where Henle cells undergo abrupt terminal differentiation. Detected up to the uppermost cortex region where cuticle cells terminally differentiate (at protein level). {ECO:0000269|PubMed:12648212, ECO:0000269|PubMed:16874310}.; uterus;heart;skin; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09067 0.10671 -0.126743121 44.0905874 1006.81614 6.10808 KRT73-AS1 . . . KRT73 antisense RNA 1 . . . . . . . . . . . KRT74 8.39640673732565e-09 0.154029266434043 0.84597072516955 keratin 74 FUNCTION: Has a role in hair formation. Specific component of keratin intermediate filaments in the inner root sheath (IRS) of the hair follicle (Probable). {ECO:0000305}.; DISEASE: Hypotrichosis 3 (HYPT3) [MIM:613981]: A condition characterized by the presence of less than the normal amount of hair. Affected individuals have normal hair in early childhood but experience progressive hair loss limited to the scalp beginning in the middle of the first decade and almost complete baldness by the third decade. Body hair, beard, eyebrows, axillary hair, teeth, and nails develop normally. {ECO:0000269|PubMed:21188418}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ectodermal dysplasia 7, hair/nail type (ECTD7) [MIM:614929]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures such as hair, teeth, nails and sweat glands, with or without any additional clinical sign. Each combination of clinical features represents a different type of ectodermal dysplasia. Ectodermal dysplasia of the hair/nail type is characterized by hypotrichosis and nail dystrophy without non- ectodermal or other ectodermal manifestations. {ECO:0000269|PubMed:24714551}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in hair follicles from scalp. In hair, it is specifically present in the inner root sheath (IRS) of the hair follicle. Present in the IRS Huxley layer, but not in Henle layer or cuticle of the IRS. In the IRS Huxley layer, it is expressed in specialized Huxley cells, termed 'Fluegelzellen, along the area of differentiated Henle cells (at protein level). {ECO:0000269|PubMed:12648212, ECO:0000269|PubMed:16874310, ECO:0000269|PubMed:24714551}.; lung;heart;testis; . 0.14828 0.11210 2.384902558 98.47841472 4847.27432 14.14529 KRT75 5.13559935197705e-07 0.6376895500251 0.362309936414965 keratin 75 FUNCTION: Plays a central role in hair and nail formation. Essential component of keratin intermediate filaments in the companion layer of the hair follicle.; DISEASE: Loose anagen hair syndrome (LAHS) [MIM:600628]: In LAHS, anagen hairs are easily pulled from the scalp. The hair is relatively sparse and does not grow long. Hair of fair color and hair shafts of reduced caliber, and an early age of onset are features. Usually the hairs are not fragile and there are no areas of breakage. {ECO:0000269|PubMed:11939812}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in hair follicles from scalp. Specifically expressed in the of the hair companion layer follicle, a single layered band of flat and vertically oriented cells between the cuboidal outer root sheath (ORS) cells and the inner root sheath (IRS) that stretches from the lowermost bulb region to the isthmus of the follicle. Also expressed in medullated hairs. In nails, it is almost exclusively present in the nail bed (at protein level). {ECO:0000269|PubMed:14675170, ECO:0000269|PubMed:15292489, ECO:0000269|PubMed:18032949, ECO:0000269|PubMed:9856802}.; unclassifiable (Anatomical System);uterus;heart;bone;brain;skin; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.09680 0.15592 2.515409172 98.67893371 4704.24385 13.83376 KRT76 6.27273672835566e-07 0.443932489040361 0.556066883685966 keratin 76 FUNCTION: Probably contributes to terminal cornification. {ECO:0000269|PubMed:1282112}.; . . . . 0.15911 . 1.249272484 93.46543996 5036.73118 14.50591 KRT77 1.05294123025074e-06 0.785358392015382 0.214640555043388 keratin 77 . . TISSUE SPECIFICITY: Expressed exclusively in skin. {ECO:0000269|PubMed:15737194}.; uterus;lung;heart;testis;skin; . 0.11671 . 2.289361599 98.30738382 4908.5509 14.28597 KRT78 2.05638911162984e-08 0.248737952337198 0.751262027098911 keratin 78 . . TISSUE SPECIFICITY: Expressed in tongue, but not in skin or in any other tissues or organs examined. {ECO:0000269|PubMed:15737194}.; optic nerve;heart;oral cavity;macula lutea;testis;head and neck;fovea centralis;choroid;lens;skeletal muscle;retina; . 0.03814 0.08126 1.337468036 94.28520878 3610.85354 11.63572 KRT79 2.9864941695015e-10 0.0827352266201211 0.917264773081229 keratin 79 . . TISSUE SPECIFICITY: Expressed in skeletal muscle, skin and scalp, but not in any other tissues or organs examined. {ECO:0000269|PubMed:15737194}.; alveolus;skin; . 0.09398 0.09924 1.337468036 94.28520878 1448.12521 7.09830 KRT80 5.43098446060312e-05 0.880827547650121 0.119118142505273 keratin 80 . . TISSUE SPECIFICITY: Weakly expressed in tongue, but not skin or in any other tissues or organs examined. {ECO:0000269|PubMed:15737194}.; . . 0.23962 0.10029 1.133561642 92.28591649 311.16336 3.75450 KRT81 2.1584354437647e-07 0.146464237541704 0.853535546614751 keratin 81 . . TISSUE SPECIFICITY: Abundantly expressed in the differentiating cortex of growing (anagen) hair. Expression is restricted to the keratinocytes of the hair cortex and is absent from inner root sheath and medulla. Expressed in malignant lymph node tissue in breast carcinoma tissue. {ECO:0000269|PubMed:7490069, ECO:0000269|PubMed:7528047, ECO:0000269|PubMed:9457912}.; . . 0.17758 0.15983 . . 2793.53872 9.97741 KRT82 2.61197625522827e-16 0.0011777617290528 0.998822238270947 keratin 82 . . . heart; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.09240 0.16011 0.962647641 90.19226233 2027.94663 8.28627 KRT83 1.70400143344448e-10 0.0600346734241968 0.939965326405403 keratin 83 . . TISSUE SPECIFICITY: Synthesis begins in the cortex 10-15 cell layers above the apex of the dermal papilla and ends abruptly in the middle of the cortex. {ECO:0000269|PubMed:9084137}.; unclassifiable (Anatomical System);breast;bile duct;pancreas;lung; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.27404 0.15921 0.75875178 86.82472281 3619.74667 11.66820 KRT84 9.43275724197859e-07 0.527916971670406 0.47208208505387 keratin 84 . . TISSUE SPECIFICITY: Expressed in the hair follicles. {ECO:0000269|PubMed:10692104}.; brain; . 0.09451 0.12228 1.381566496 94.62137297 6242.58699 16.53835 KRT85 0.00110914581875823 0.988635789210404 0.0102550649708378 keratin 85 . . TISSUE SPECIFICITY: Synthesis occurs immediately above a small population of matrix cells at the base of the hair bulb and the trichocytes lining the dermal papilla and extends upward through the matrix and ends in the lower part of the cortex of the hair shaft. {ECO:0000269|PubMed:9084137}.; heart;brain; dorsal root ganglion;superior cervical ganglion; 0.20655 0.15317 -0.462894052 23.62585515 564.44658 4.82439 KRT86 3.63965280007909e-05 0.596037597187161 0.403926006284838 keratin 86 . . TISSUE SPECIFICITY: Synthesis begins slightly higher in the hair shaft than HB1 and HB3 and continues much farther up, ending in the keratogeneous zone. {ECO:0000269|PubMed:9084137}.; . . 0.07111 0.14849 . . 332.90162 3.87800 KRT87P . . . keratin 87 pseudogene . . . . . . . 0.481458261 79.03986789 . . KRT88P . . . keratin 88 pseudogene . . . . . . . . . . . KRT89P . . . keratin 89 pseudogene FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.; FUNCTION: Spinorphin: functions as an endogenous inhibitor of enkephalin-degrading enzymes such as DPP3, and as a selective antagonist of the P2RX3 receptor which is involved in pain signaling, these properties implicate it as a regulator of pain and inflammation.; DISEASE: Heinz body anemias (HEIBAN) [MIM:140700]: Form of non- spherocytic hemolytic anemia of Dacie type 1. After splenectomy, which has little benefit, basophilic inclusions called Heinz bodies are demonstrable in the erythrocytes. Before splenectomy, diffuse or punctate basophilia may be evident. Most of these cases are probably instances of hemoglobinopathy. The hemoglobin demonstrates heat lability. Heinz bodies are observed also with the Ivemark syndrome (asplenia with cardiovascular anomalies) and with glutathione peroxidase deficiency. {ECO:0000269|PubMed:186485, ECO:0000269|PubMed:2599881, ECO:0000269|PubMed:6259091, ECO:0000269|PubMed:8704193}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Beta-thalassemia (B-THAL) [MIM:613985]: A form of thalassemia. Thalassemias are common monogenic diseases occurring mostly in Mediterranean and Southeast Asian populations. The hallmark of beta-thalassemia is an imbalance in globin-chain production in the adult HbA molecule. Absence of beta chain causes beta(0)-thalassemia, while reduced amounts of detectable beta globin causes beta(+)-thalassemia. In the severe forms of beta- thalassemia, the excess alpha globin chains accumulate in the developing erythroid precursors in the marrow. Their deposition leads to a vast increase in erythroid apoptosis that in turn causes ineffective erythropoiesis and severe microcytic hypochromic anemia. Clinically, beta-thalassemia is divided into thalassemia major which is transfusion dependent, thalassemia intermedia (of intermediate severity), and thalassemia minor that is asymptomatic. {ECO:0000269|PubMed:15481886, ECO:0000269|PubMed:2399911, ECO:0000269|PubMed:6166632, ECO:0000269|PubMed:7693620}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Sickle cell anemia (SKCA) [MIM:603903]: Characterized by abnormally shaped red cells resulting in chronic anemia and periodic episodes of pain, serious infections and damage to vital organs. Normal red blood cells are round and flexible and flow easily through blood vessels, but in sickle cell anemia, the abnormal hemoglobin (called Hb S) causes red blood cells to become stiff. They are C-shaped and resembles a sickle. These stiffer red blood cells can led to microvascular occlusion thus cutting off the blood supply to nearby tissues. {ECO:0000269|PubMed:13464827, ECO:0000269|Ref.10}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Beta-thalassemia, dominant, inclusion body type (B- THALIB) [MIM:603902]: An autosomal dominant form of beta thalassemia characterized by moderate anemia, lifelong jaundice, cholelithiasis and splenomegaly, marked morphologic changes in the red cells, erythroid hyperplasia of the bone marrow with increased numbers of multinucleate red cell precursors, and the presence of large inclusion bodies in the normoblasts, both in the marrow and in the peripheral blood after splenectomy. {ECO:0000269|PubMed:1971109}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Red blood cells. {ECO:0000269|PubMed:6539334}.; . . . 0.08201 -0.005381972 53.50908233 . . KRT90P . . . keratin 90 pseudogene . . . . . . . . . . . KRT125P . . . keratin 125 pseudogene . . . . . . . . . . . KRT126P . . . keratin 126 pseudogene . . . . . . . . . . . KRT127P . . . keratin 127 pseudogene . . . . . . . . . . . KRT128P . . . keratin 128 pseudogene . . . . . . . . . . . KRT222 0.00212668208955224 0.916161013982197 0.0817123039282507 keratin 222 . . . . . 0.34001 . -0.317668748 31.45789101 15.19746 0.54686 KRT223P . . . keratin 223 pseudogene . . . . . . . . . . . KRTAP1-1 0.00844297679609777 0.567445271869319 0.424111751334583 keratin associated protein 1-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in the middle/upper portions of the hair cortex, in the region termed the keratogenous zone. {ECO:0000269|PubMed:11279113}.; . . . . 0.571462851 81.99457419 1043.32111 6.19874 KRTAP1-3 0.653995931200051 0.321186667053979 0.0248174017459701 keratin associated protein 1-3 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in the middle/upper portions of the hair cortex, in the region termed the keratogenous zone. {ECO:0000269|PubMed:11279113}.; . . . . 1.170393003 92.68105685 399.50943 4.19518 KRTAP1-4 0.141056283086721 0.62710619275881 0.231837524154469 keratin associated protein 1-4 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in the middle/upper portions of the hair cortex, in the region termed the keratogenous zone. {ECO:0000269|PubMed:11279113}.; . . . . . . 1176.70894 6.51738 KRTAP1-5 0.00104646254171817 0.374374601608389 0.624578935849893 keratin associated protein 1-5 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in the middle/upper portions of the hair cortex, in the region termed the keratogenous zone. {ECO:0000269|PubMed:11279113}.; . . . . 1.282454727 93.71313989 1319.84804 6.83119 KRTAP2-1 . . . keratin associated protein 2-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}.; . . . . 0.24626 . . . 6079.05555 16.29512 KRTAP2-2 . . . keratin associated protein 2-2 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}.; . . . . . . . . 1131.88712 6.41892 KRTAP2-3 0.0777171995837597 0.541195918530488 0.381086881885752 keratin associated protein 2-3 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}.; . . . . 0.24626 . . . 4812.04517 14.06529 KRTAP2-4 0.0863483631962968 0.559066493763398 0.354585143040305 keratin associated protein 2-4 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed specifically in the middle/upper portions of the hair cortex, in the region termed the keratogenous zone. {ECO:0000269|PubMed:11279113}.; . . . . . . 478.68739 4.51784 KRTAP2-5P . . . keratin associated protein 2-5, pseudogene . . . . . . . . . . . KRTAP3-1 0.473819461178528 0.440900571191731 0.0852799676297407 keratin associated protein 3-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . . . 0.169169615 65.33380514 24.61387 0.80845 KRTAP3-2 0.474662317449609 0.440474942665146 0.0848627398852445 keratin associated protein 3-2 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . . 0.10204 0.525552348 80.57914603 3899.92964 12.32898 KRTAP3-3 0.00478766737481947 0.450207745482273 0.545004587142907 keratin associated protein 3-3 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Localized to the upper cortex of the hair shaft. {ECO:0000269|PubMed:11279113}.; . . . . 0.169169615 65.33380514 29.12862 0.93135 KRTAP3-4P . . . keratin associated protein 3-4, pseudogene . . . . . . . . . . . KRTAP4-1 0.179915848897162 0.645008419466903 0.175075731635935 keratin associated protein 4-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in the hair follicles. {ECO:0000269|PubMed:15955084}.; . . 0.05192 . . . 224.07397 3.23730 KRTAP4-2 0.00502474066236789 0.45977783007869 0.535197429258942 keratin associated protein 4-2 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.03816 . 0.591694063 82.45458835 27.83148 0.89409 KRTAP4-3 0.000536885200778008 0.269335990085373 0.73012712471385 keratin associated protein 4-3 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed specifically in the middle/uper portions of the hair cortex. Not detected in the hair matrix or cuticle. {ECO:0000269|PubMed:15955084}.; . . 0.07210 . 0.659651797 84.35362114 869.44066 5.74487 KRTAP4-4 0.00104159410283142 0.373550344709035 0.625408061188133 keratin associated protein 4-4 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in the hair follicles. {ECO:0000269|PubMed:15955084}.; . . 0.04701 . 1.793263958 96.88605803 2907.53582 10.22746 KRTAP4-5 0.0103879610309188 0.611610208445453 0.378001830523628 keratin associated protein 4-5 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in the hair follicles. {ECO:0000269|PubMed:15955084}.; muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.08431 . 1.258592195 93.50082567 7666.43242 18.81391 KRTAP4-6 0.0145001991223108 0.681126808559343 0.304372992318346 keratin associated protein 4-6 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in the hair follicles. {ECO:0000269|PubMed:15955084}.; meninges;pia mater;dura mater;skin; . . . . . 688.42146 5.23501 KRTAP4-7 1.11232560634725e-05 0.110363647335244 0.889625229408692 keratin associated protein 4-7 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in the hair follicles. {ECO:0000269|PubMed:15955084}.; . . . . 0.323496558 72.93583392 3093.65412 10.57314 KRTAP4-8 0.00977081898596453 0.598577343944767 0.391651837069268 keratin associated protein 4-8 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in the hair follicles. {ECO:0000269|PubMed:15955084}.; unclassifiable (Anatomical System);muscle; . 0.12236 . . . 6576.55433 17.09261 KRTAP4-9 0.00150378248703316 0.442094670326036 0.556401547186931 keratin associated protein 4-9 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in the hair follicles. {ECO:0000269|PubMed:15955084}.; unclassifiable (Anatomical System);muscle; dorsal root ganglion;testis - interstitial;superior cervical ganglion; 0.16136 . 0.812172405 87.75654636 1745.942 7.71103 KRTAP4-11 0.098639840039914 0.771488779545209 0.129871380414877 keratin associated protein 4-11 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in the hair follicles. {ECO:0000269|PubMed:15955084}.; . . 0.10960 . . . 5061.10619 14.57540 KRTAP4-12 0.741776468899415 0.247270251877923 0.0109532792226621 keratin associated protein 4-12 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in the hair follicles. {ECO:0000269|PubMed:15955084}.; . . 0.02326 0.11774 0.72761005 86.08162302 161.45954 2.77645 KRTAP4-16P 0.00549629574645564 0.477796261081606 0.516707443171938 keratin associated protein 4-16, pseudogene . . . . . . . . . 483.37073 4.52664 KRTAP5-1 0.000129615662038598 0.229558078474505 0.770312305863456 keratin associated protein 5-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in hair root but not in skin. Expressed also in lung, pancreas, ovary, testis. {ECO:0000269|PubMed:15144888}.; . . 0.08011 . 0.573279816 82.08303845 70.09909 1.73755 KRTAP5-2 0.000625082928112611 0.290969321458942 0.708405595612945 keratin associated protein 5-2 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to hair root, not detected in any other tissues. {ECO:0000269|PubMed:15144888}.; . . 0.07547 . 0.25917371 70.05779665 555.12431 4.78745 KRTAP5-3 0.262910457239172 0.638148141177212 0.0989414015836159 keratin associated protein 5-3 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to hair root, not detected in any other tissues. {ECO:0000269|PubMed:15144888}.; . . 0.11645 . 0.637604436 83.77565464 285.15099 3.61497 KRTAP5-4 0.00679370641134028 0.521495323698893 0.471710969889766 keratin associated protein 5-4 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to hair root, not detected in any other tissues. {ECO:0000269|PubMed:15144888}.; . . . . . . 311.80424 3.75819 KRTAP5-5 1.15231280702318e-05 0.112570492812768 0.887417984059162 keratin associated protein 5-5 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to hair root, not detected in any other tissues. {ECO:0000269|PubMed:15144888}.; . . 0.08966 0.08973 1.282454727 93.71313989 5592.532 15.47031 KRTAP5-6 0.000393980177015885 0.229400490038851 0.770205529784133 keratin associated protein 5-6 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in hair root and not in skin. Expressed also in liver and skeletal muscle. {ECO:0000269|PubMed:15144888}.; . . 0.11440 . 0.369407109 74.95281906 1632.09312 7.47008 KRTAP5-7 0.581964460910534 0.375188480483493 0.0428470586059729 keratin associated protein 5-7 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in hair root but not in skin. {ECO:0000269|PubMed:15144888}.; . . . . 1.036284653 91.1358811 1351.24246 6.90460 KRTAP5-8 0.006907479136412 0.524975036140808 0.46811748472278 keratin associated protein 5-8 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.07547 . 1.436808095 95.04600142 7193.00835 18.25942 KRTAP5-9 0.000861770573554934 0.341111959217963 0.658026270208482 keratin associated protein 5-9 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to hair root, not detected in any other tissues. Expressed in cuticle layers of differentiating hair follicles. {ECO:0000269|PubMed:15144888}.; . . 0.11645 . 2.949344402 99.16253833 2258.18516 8.78192 KRTAP5-10 0.191708884269112 0.647164714738541 0.161126400992347 keratin associated protein 5-10 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in hair root but not in skin. Expressed also in brain and skeletal muscle. {ECO:0000269|PubMed:15144888}.; . . 0.24244 . 1.082196027 91.79641425 5257.32188 14.96836 KRTAP5-11 0.033567491593056 0.614995679998546 0.351436828408398 keratin associated protein 5-11 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to hair root, not detected in any other tissues. {ECO:0000269|PubMed:15144888}.; . . 0.08346 . 0.681699246 84.93158764 56.92048 1.51855 KRTAP5-13P . . . keratin associated protein 5-13, pseudogene . . . . . . . . . . . KRTAP5-14P . . . keratin associated protein 5-14, pseudogene . . . . . . . . . . . KRTAP5-AS1 . . . KRTAP5-1/KRTAP5-2 antisense RNA 1 . . . . . . . . . . . KRTAP6-1 0.000321176229646924 0.20590409903307 0.793774724737283 keratin associated protein 6-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.04351 . 0.858082312 88.55862232 380.1146 4.11025 KRTAP6-2 0.165055211325206 0.640302486697303 0.194642301977491 keratin associated protein 6-2 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.06600 . -0.031067188 51.03798066 117.60277 2.35755 KRTAP6-3 0.532856911991667 0.407628903016927 0.0595141849914066 keratin associated protein 6-3 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.38130 . . . 160.69859 2.76804 KRTAP7-1 . . . keratin associated protein 7-1 (gene/pseudogene) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Expressed in the upper portion of the hair cortex.; . . . . . . . . KRTAP8-1 0.0205124822628118 0.515575120272189 0.463912397464999 keratin associated protein 8-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Is essentially restricted to only one vertical half of the hair forming compartment and in beard hairs is absent from the central medulla.; . . 0.13397 0.08760 0.323496558 72.93583392 56.45444 1.51068 KRTAP8-2P . . . keratin associated protein 8-2, pseudogene . . . . . . . . . . . KRTAP8-3P . . . keratin associated protein 8-3, pseudogene . . . . . . . . . . . KRTAP9-1 0.00139809073197777 0.427931077277832 0.570670831990191 keratin associated protein 9-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}.; . . . . . . . . 1284.99961 6.74744 KRTAP9-2 0.238025345648846 0.644889755939838 0.117084898411316 keratin associated protein 9-2 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.10002 0.10345 0.77170517 87.00754895 271.89991 3.53305 KRTAP9-3 0.0447129443011167 0.669224736806198 0.286062318892685 keratin associated protein 9-3 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.07475 0.10242 0.260991686 70.25831564 105.70515 2.22805 KRTAP9-4 0.000785606510373498 0.326037177482138 0.673177216007489 keratin associated protein 9-4 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . uterus;heart;skin; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; . 0.09959 0.43736446 77.56546355 48.3406 1.35533 KRTAP9-6 0.194495477706129 0.647489415157244 0.158015107136627 keratin associated protein 9-6 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}.; . . . . . . . . 1438.26747 7.07672 KRTAP9-7 0.00547082986165627 0.476855633298418 0.517673536839926 keratin associated protein 9-7 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}.; . . . . . . . . 370.17865 4.06303 KRTAP9-8 0.0437541258514207 0.665318333644027 0.290927540504552 keratin associated protein 9-8 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.13627 0.10412 0.148941568 64.31941496 59.95724 1.57115 KRTAP9-9 0.00729870640952065 0.536562679465343 0.456138614125136 keratin associated protein 9-9 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . . 0.10345 . . 5752.9952 15.75321 KRTAP9-10P . . . keratin associated protein 9-10, pseudogene . . . . . . . . . . . KRTAP9-11P . . . keratin associated protein 9-11, pseudogene . . . . . . . . . . . KRTAP9-12P . . . keratin associated protein 9-12, pseudogene . . . . . . . . . . . KRTAP10-1 0.106027011173101 0.775431099851016 0.118541888975883 keratin associated protein 10-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber cuticle, lying approximately 20 cell layers above the apex of the dermal papilla of the hair root; not detected in any other tissues. {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.; . . 0.10085 . 2.776469365 99.0150979 238.187 3.33574 KRTAP10-2 0.0170721058222492 0.713414240396791 0.26951365378096 keratin associated protein 10-2 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber cuticle, lying approximately 20 cell layers above the apex of the dermal papilla of the hair root; not detected in any other tissues. {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.; . . 0.10939 . 0.971952656 90.26893135 2694.09373 9.76825 KRTAP10-3 0.0652460719862998 0.729570320534343 0.205183607479358 keratin associated protein 10-3 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber cuticle, lying approximately 20 cell layers above the apex of the dermal papilla of the hair root; not detected in any other tissues. {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.; . . 0.13003 . 2.133152036 97.93583392 403.71116 4.21448 KRTAP10-4 0.00183072306913658 0.719852436469061 0.278316840461802 keratin associated protein 10-4 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to hair root, not detected in any other tissues.; . . 0.10738 0.09219 2.465816951 98.61405992 4315.36021 13.07698 KRTAP10-5 8.24781964419107e-05 0.321633814750585 0.678283707052974 keratin associated protein 10-5 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber cuticle, lying approximately 20 cell layers above the apex of the dermal papilla of the hair root; not detected in any other tissues. {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.; . . . . 1.953079981 97.54659118 4100.88283 12.70549 KRTAP10-6 1.55311497446653e-05 0.242389557480431 0.757594911369825 keratin associated protein 10-6 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber cuticle, lying approximately 20 cell layers above the apex of the dermal papilla of the hair root; not detected in any other tissues. {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.; . . . . 3.24344868 99.38664779 6418.15237 16.78541 KRTAP10-7 0.00759405487600206 0.777332391357004 0.215073553766994 keratin associated protein 10-7 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber cuticle, lying approximately 20 cell layers above the apex of the dermal papilla of the hair root; not detected in any other tissues. {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.; . . 0.11850 . . . 608.63787 4.98863 KRTAP10-8 5.20734368242563e-06 0.134436166004705 0.865558626651613 keratin associated protein 10-8 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber cuticle, lying approximately 20 cell layers above the apex of the dermal papilla of the hair root; not detected in any other tissues. {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.; optic nerve;macula lutea;fovea centralis;choroid;lens;retina; . 0.12167 . 0.995816767 90.62278839 209.1789 3.12232 KRTAP10-9 0.44279392690144 0.527737997852451 0.029468075246108 keratin associated protein 10-9 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber cuticle, lying approximately 20 cell layers above the apex of the dermal papilla of the hair root; not detected in any other tissues. {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.; . . . 0.09533 3.225032979 99.36895494 2027.16137 8.28477 KRTAP10-10 2.63978765634477e-05 0.177831208420617 0.82214239370282 keratin associated protein 10-10 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber cuticle, lying approximately 20 cell layers above the apex of the dermal papilla of the hair root; not detected in any other tissues. {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.; . . . . 3.642516455 99.54588346 11624.88241 23.32283 KRTAP10-11 0.00039520835434146 0.399685153065354 0.599919638580305 keratin associated protein 10-11 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber cuticle, lying approximately 20 cell layers above the apex of the dermal papilla of the hair root; not detected in any other tissues. {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.; . . . . 1.664578456 96.27860344 736.58011 5.38815 KRTAP10-12 0.114715057789637 0.778420859430687 0.106864082779677 keratin associated protein 10-12 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber cuticle, lying approximately 20 cell layers above the apex of the dermal papilla of the hair root; not detected in any other tissues. {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.; . . 0.23695 . 0.617373774 83.25076669 2557.27101 9.44190 KRTAP10-13P . . . keratin associated protein 10-13, pseudogene . . . . . . . . . . . KRTAP11-1 0.00426873037466338 0.662516422958614 0.333214846666723 keratin associated protein 11-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.22409 0.09008 0.659651797 84.35362114 3007.85811 10.41393 KRTAP12-1 0.0251971191873409 0.557356492328032 0.417446388484627 keratin associated protein 12-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber cuticle, lying approximately 20 cell layers above the apex of the dermal papilla of the hair root; not detected in any other tissues. {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.; . . 0.08446 . 0.880130671 88.9596603 326.06793 3.83859 KRTAP12-2 5.57611036071947e-05 0.145680265307596 0.854263973588797 keratin associated protein 12-2 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber cuticle, lying approximately 20 cell layers above the apex of the dermal papilla of the hair root; not detected in any other tissues. {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.; . . . 0.10307 1.750970652 96.67374381 685.01833 5.22538 KRTAP12-3 0.146058957278522 0.63050055069582 0.223440492025658 keratin associated protein 12-3 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber cuticle, lying approximately 20 cell layers above the apex of the dermal papilla of the hair root; not detected in any other tissues. {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.; . . . . 0.679884223 84.81363529 61.70736 1.60091 KRTAP12-4 0.00279068688913577 0.351196365952365 0.646012947158499 keratin associated protein 12-4 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber cuticle, lying approximately 20 cell layers above the apex of the dermal papilla of the hair root; not detected in any other tissues. {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.; . . 0.19357 . 0.035072054 56.2514744 9.5499 0.35184 KRTAP12-5P . . . keratin associated protein 12-5, pseudogene . . . . . . . . . . . KRTAP13-1 0.00711270612697186 0.531124975775477 0.461762318097551 keratin associated protein 13-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Weak expression seen in the late matrix and entire cortex area of the hair follicle. {ECO:0000269|PubMed:12359730}.; heart; superior cervical ganglion; 0.08913 . 0.815800671 87.8744987 115.58549 2.33772 KRTAP13-2 0.000843088326991207 0.337495729456115 0.661661182216894 keratin associated protein 13-2 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}.; . . . . 0.05734 . 1.328368696 94.12597311 1391.91764 6.98038 KRTAP13-3 0.000682837175576854 0.304161414710769 0.695155748113654 keratin associated protein 13-3 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}.; . . . . 0.02909 . -0.317668748 31.45789101 6.26023 0.23613 KRTAP13-4 0.0077412086854088 0.549008036361084 0.443250754953507 keratin associated protein 13-4 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.08248 . 1.238355121 93.31799953 78.28725 1.86598 KRTAP13-5P . . . keratin associated protein 13-5, pseudogene . . . . . . . . . . . KRTAP13-6P . . . keratin associated protein 13-6, pseudogene . . . . . . . . . . . KRTAP15-1 0.00443716984404986 0.435364224695321 0.560198605460629 keratin associated protein 15-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.06921 . 0.193034296 66.82000472 11.59854 0.42004 KRTAP16-1 . . . keratin associated protein 16-1 . . . . . 0.14655 . . . 4424.76535 13.33717 KRTAP17-1 0.54010776515575 0.403091780910294 0.0568004539339563 keratin associated protein 17-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.11394 . 0.21326276 67.71644256 2963.51846 10.31492 KRTAP19-1 0.0410480789430577 0.65360136821785 0.305350552839092 keratin associated protein 19-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Detected in the upper portion of the hair cortex.; . . 0.03251 . 0.103030231 61.2762444 61.55088 1.59834 KRTAP19-2 0.126076454825682 0.614588033845945 0.259335511328372 keratin associated protein 19-2 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.07479 . 0.457594962 78.16112291 164.84426 2.80473 KRTAP19-3 0.00440584340588175 0.433994573093307 0.561599583500811 keratin associated protein 19-3 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . uterus;heart;skin; . . . 0.279402865 70.86577023 44.53053 1.27686 KRTAP19-4 0.0238880027709709 0.546505113838731 0.429606883390298 keratin associated protein 19-4 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.06351 . 0.701931997 85.34442085 51.73899 1.42075 KRTAP19-5 0.00518271337885184 0.465959289119672 0.528857997501477 keratin associated protein 19-5 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.07982 . -0.229483771 36.86010852 22.09493 0.74262 KRTAP19-6 0.0203608220277465 0.514074495896709 0.465564682075545 keratin associated protein 19-6 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.02141 . 0.523736627 80.45529606 31.73683 0.99957 KRTAP19-7 0.14123495896819 0.627233802624796 0.231531238407014 keratin associated protein 19-7 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.06723 . -0.075159878 47.78839349 17.13623 0.60186 KRTAP19-8 0.00748612331236648 0.541916077977659 0.450597798709974 keratin associated protein 19-8 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.04611 . 0.147123112 64.11299835 10.50077 0.38156 KRTAP19-9P . . . keratin associated protein 19-9, pseudogene . . . . . . . . . . . KRTAP19-10P . . . keratin associated protein 19-10, pseudogene . . . . . . . . . . . KRTAP19-11P . . . keratin associated protein 19-11, pseudogene . . . . . . . . . . . KRTAP20-1 0.0232742114105319 0.541210176718189 0.435515611871279 keratin associated protein 20-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.13869 . 0.3455435 73.78509082 50.28346 1.39403 KRTAP20-2 0.137405132942761 0.624391552780924 0.238203314276315 keratin associated protein 20-2 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.03344 . 0.035072054 56.2514744 13.13352 0.47815 KRTAP20-3 . . . keratin associated protein 20-3 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.06366 . 0.145304857 63.81221986 1.03065 0.02606 KRTAP20-4 . . . keratin associated protein 20-4 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}.; . . . . 0.05441 . . . 0.19655 0.00400 KRTAP21-1 0.485522901924314 0.434855953441679 0.079621144634007 keratin associated protein 21-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . . . -0.09720619 46.20193442 35.12509 1.06519 KRTAP21-2 0.250319144790592 0.641963274862424 0.107717580346984 keratin associated protein 21-2 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.02857 . 0.501689326 79.7888653 442.3427 4.37748 KRTAP21-3 . . . keratin associated protein 21-3 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . . . 0.389637587 75.75489502 760.82107 5.46797 KRTAP21-4P . . . keratin associated protein 21-4, pseudogene . . . . . . . . . . . KRTAP22-1 0.124017870650419 0.612566234302353 0.263415895047228 keratin associated protein 22-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.08358 . 0.567831482 81.78225997 36.78629 1.10310 KRTAP22-2 . . . keratin associated protein 22-2 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}.; . . . . . . 0.389637587 75.75489502 3.07259 0.11088 KRTAP23-1 0.454990924430803 0.450003261290967 0.0950058142782295 keratin associated protein 23-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.17037 . 0.501689326 79.7888653 4.20263 0.15345 KRTAP24-1 9.16556642967582e-06 0.183195879403662 0.816794955029908 keratin associated protein 24-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Specific expression in the middle/upper hair cuticle. {ECO:0000269|PubMed:17235325}.; . . 0.05713 0.06593 0.106667882 61.73036093 431.33982 4.33389 KRTAP25-1 . . . keratin associated protein 25-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}.; . . . . . . 0.61192669 82.99716914 9.27842 0.34006 KRTAP26-1 0.0010066331061178 0.367553351082902 0.63144001581098 keratin associated protein 26-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . TISSUE SPECIFICITY: Localized high up in the well differentiated portion of the hair follicle cuticle (about 10-15 cell layers above the apex of the dermal papilla). {ECO:0000269|PubMed:18647308}.; placenta; . 0.07704 . 1.194256079 92.88747346 1234.582 6.63754 KRTAP27-1 1.08863813473516e-05 0.109038758866608 0.890950354752045 keratin associated protein 27-1 FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high- sulfur and high-glycine-tyrosine keratins.; . . . . 0.07394 . 0.681699246 84.93158764 1235.61613 6.64061 KRTAP29-1 . . . keratin associated protein 29-1 . . . . . . . . . 4514.68974 13.49316 KRTCAP2 0.0299704903065574 0.807557322435346 0.162472187258096 keratinocyte associated protein 2 . . TISSUE SPECIFICITY: Expressed in skin, heart, placental, liver, skeletal muscle, kidney, pancreas, keratinocytes and dermal fibroblasts. {ECO:0000269|PubMed:12752121}.; medulla oblongata;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;heart;adrenal gland;liver;testis; 0.28974 0.10851 -0.163345027 41.24793583 10.76059 0.39054 KRTCAP3 0.0445235342133754 0.850930012328714 0.104546453457911 keratinocyte associated protein 3 . . TISSUE SPECIFICITY: Expressed in skin, pancreas and keratinocytes. {ECO:0000269|PubMed:12752121}.; uterus;prostate;pancreas;lung;islets of Langerhans;larynx;colon;stomach; . 0.21532 . 0.148941568 64.31941496 58.73938 1.55429 KRTDAP 0.0753309193944416 0.872451995844373 0.0522170847611853 keratinocyte differentiation associated protein FUNCTION: May act as a soluble regulator of keratinocyte differentiation. May play an important role in embryonic skin morphogenesis. {ECO:0000269|PubMed:15140226}.; . TISSUE SPECIFICITY: Highly expressed in skin and detected at lower levels in thymus. In skin, found exclusively in lamellar granules of granular keratinocytes and in the intracellular space of the stratum corneum. Also highly expressed in oral mucosa, tongue, esophagus, and stomach, and at much lower levels in bladder and uterus. Not detected in gastrointestinal mucosa. {ECO:0000269|PubMed:15140226}.; heart;larynx;oral cavity;hypopharynx;testis;head and neck;skin;skeletal muscle; superior cervical ganglion;tongue;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.16729 0.10534 -0.053113545 49.38664779 5.57852 0.20762 KSR1 0.609182270949014 0.390802697318739 1.50317322471295e-05 kinase suppressor of ras 1 FUNCTION: Location-regulated scaffolding protein connecting MEK to RAF. Promotes MEK and RAF phosphorylation and activity through assembly of an activated signaling complex. By itself, it has no demonstrated kinase activity.; . . unclassifiable (Anatomical System);medulla oblongata;heart;ovary;colon;parathyroid;skin;retina;uterus;lung;frontal lobe;endometrium;placenta;amnion;hypopharynx;testis;cervix;head and neck;kidney;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.30789 0.15135 . . 702.71821 5.27148 KSR1P1 . . . kinase suppressor of ras 1 pseudogene 1 . . . . . . . . . . . KSR2 0.999946624685717 5.33753125847522e-05 1.6984977595526e-12 kinase suppressor of ras 2 FUNCTION: Location-regulated scaffold connecting MEK to RAF. Has very low protein kinase activity and can phosphorylate MAP2K1 at several Ser and Thr residues with very low efficiency (in vitro). Interaction with BRAF enhances KSR2-mediated phosphorylation of MAP2K1 (in vitro). Blocks MAP3K8 kinase activity and MAP3K8- mediated signaling. Acts as a negative regulator of MAP3K3- mediated activation of ERK, JNK and NF-kappa-B pathways, inhibiting MAP3K3-mediated interleukin-8 production. {ECO:0000269|PubMed:12975377, ECO:0000269|PubMed:16039990, ECO:0000269|PubMed:21441910}.; . TISSUE SPECIFICITY: Mainly expressed in brain and kidney. {ECO:0000269|PubMed:12975377}.; frontal lobe; . 0.40754 0.12029 . . 183.49029 2.93982 KSS . . . Kearns-Sayre syndrome . . . . . . . . . . . KTI12 0.0342938336572136 0.82476090527236 0.140945261070426 KTI12 chromatin associated homolog . . . . . 0.11555 0.10049 0.707379532 85.62750649 675.35751 5.19003 KTN1 0.639772920815945 0.360227079177522 6.53274755494176e-12 kinectin 1 FUNCTION: Receptor for kinesin thus involved in kinesin-driven vesicle motility. Accumulates in integrin-based adhesion complexes (IAC) upon integrin aggregation by fibronectin.; . TISSUE SPECIFICITY: High levels in peripheral blood lymphocytes, testis and ovary, lower levels in spleen, thymus, prostate, small intestine and colon.; lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;bladder;gall bladder;heart;cartilage;tongue;spinal cord;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;mesenchyma;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; amygdala;superior cervical ganglion;testis - interstitial;thalamus;medulla oblongata;hypothalamus;spinal cord;caudate nucleus;uterus;prostate;testis - seminiferous tubule;thyroid;prefrontal cortex;testis;ciliary ganglion;pituitary;parietal lobe; 0.38971 0.12837 -0.942503278 9.412597311 381.67904 4.11827 KTN1-AS1 . . . KTN1 antisense RNA 1 . . . cervix;lens; . 0.03642 . . . . . KWE . . . keratolytic winter erythema (Oudtshoorn skin disease) . . . . . . . . . . . KXD1 0.14091588201121 0.779324533959366 0.0797595840294245 KxDL motif containing 1 FUNCTION: Involved in endosomal cargo sorting. {ECO:0000250}.; . . myocardium;smooth muscle;ovary;salivary gland;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;iris;testis;germinal center;brain;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;cerebellum; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;parietal lobe;skeletal muscle;cingulate cortex; 0.18584 0.11114 0.571462851 81.99457419 1833.56504 7.89171 KY 1.0676447551172e-08 0.52150319522093 0.478496794102622 kyphoscoliosis peptidase FUNCTION: Probable cytoskeleton-associated protease required for normal muscle growth. Involved in function, maturation and stabilization of the neuromuscular junction. May act by cleaving muscle-specific proteins such as FLNC (By similarity). {ECO:0000250}.; . . uterus;ovary;heart;testis;blood;skin;bone marrow; . 0.39890 0.15002 -1.195919584 5.832743572 42.49824 1.23358 KYNU 1.82768855736828e-09 0.391796990708557 0.608203007463754 kynureninase FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity.; DISEASE: Hydroxykynureninuria (HYXKY) [MIM:236800]: An inborn error of amino acid metabolism characterized by massive urinary excretion of large amounts of kynurenine, 3-hydroxykynurenine and xanthurenic acid. Affected individuals manifest renal tubular dysfunction, metabolic acidosis, psychomotor retardation, non- progressive encephalopathy, and muscular hypertonia. {ECO:0000269|PubMed:17334708}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues tested (heart, brain placenta, lung, liver, skeletal muscle, kidney and pancreas). Highest levels found in placenta, liver and lung. Expressed in all brain regions. {ECO:0000269|PubMed:8706755, ECO:0000269|PubMed:9180257}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;cochlea;bone;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;placenta;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05824 0.10472 -0.600630256 18.06440198 62.38164 1.61248 KYNUP1 . . . kynureninase pseudogene 1 . . . . . . . . . . . KYNUP2 . . . kynureninase pseudogene 2 . . . . . . . . . . . KYNUP3 . . . kynureninase pseudogene 3 . . . . . . . . . . . L1CAM 0.999983695509006 1.6304490898956e-05 9.45168300094434e-14 L1 cell adhesion molecule FUNCTION: Cell adhesion molecule with an important role in the development of the nervous system. Involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc. Binds to axonin on neurons.; DISEASE: Hydrocephalus due to stenosis of the aqueduct of Sylvius (HSAS) [MIM:307000]: Hydrocephalus is a condition in which abnormal accumulation of cerebrospinal fluid in the brain causes increased intracranial pressure inside the skull. This is usually due to blockage of cerebrospinal fluid outflow in the brain ventricles or in the subarachnoid space at the base of the brain. In children is typically characterized by enlargement of the head, prominence of the forehead, brain atrophy, mental deterioration, and convulsions. In adults the syndrome includes incontinence, imbalance, and dementia. HSAS is characterized by mental retardation and enlarged brain ventricles. {ECO:0000269|PubMed:10797421, ECO:0000269|PubMed:12435569, ECO:0000269|PubMed:7562969, ECO:0000269|PubMed:7762552, ECO:0000269|PubMed:7881431, ECO:0000269|PubMed:7920659, ECO:0000269|PubMed:8401576, ECO:0000269|PubMed:8556302, ECO:0000269|PubMed:8929944, ECO:0000269|PubMed:9118141, ECO:0000269|PubMed:9195224, ECO:0000269|PubMed:9268105, ECO:0000269|PubMed:9521424, ECO:0000269|PubMed:9744477}. Note=The disease is caused by mutations affecting the gene represented in this entry. L1CAM mutations have also been found in few patients affected by hydrocephalus with Hirschsprung disease, suggesting a role of this gene acting either in a direct or indirect way in the pathogenesis of Hirschsprung disease (PubMed:22344793). {ECO:0000269|PubMed:22344793}.; DISEASE: Mental retardation, aphasia, shuffling gait, and adducted thumbs syndrome (MASA) [MIM:303350]: An X-linked recessive syndrome with a highly variable clinical spectrum. Main clinical features include spasticity and hyperreflexia of lower limbs, shuffling gait, mental retardation, aphasia and adducted thumbs. The features of spasticity have been referred to as complicated spastic paraplegia type 1 (SPG1). Some patients manifest corpus callosum hypoplasia and hydrocephalus. Inter- and intrafamilial variability is very wide, such that patients with hydrocephalus, MASA, SPG1, and agenesis of corpus callosum can be present within the same family. {ECO:0000269|PubMed:10805190, ECO:0000269|PubMed:11857550, ECO:0000269|PubMed:16816908, ECO:0000269|PubMed:7920659, ECO:0000269|PubMed:7920660, ECO:0000269|PubMed:9268105, ECO:0000269|PubMed:9300653, ECO:0000269|PubMed:9452110, ECO:0000269|PubMed:9832035}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spastic paraplegia 1, X-linked (SPG1) [MIM:303350]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. {ECO:0000269|PubMed:7562969, ECO:0000269|PubMed:7920659}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in L1CAM may contribute to Hirschsprung disease by modifying the effects of Hirschsprung disease- associated genes to cause intestinal aganglionosis. {ECO:0000269|PubMed:11857550}.; DISEASE: Agenesis of the corpus callosum, X-linked, partial (ACCPX) [MIM:304100]: A syndrome characterized by partial corpus callosum agenesis, hypoplasia of inferior vermis and cerebellum, mental retardation, seizures and spasticity. Other features include microcephaly, unusual facies, and Hirschsprung disease in some patients. {ECO:0000269|PubMed:16650080}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;ovary;sympathetic chain;colon;skin;retina;breast;uterus;pancreas;lung;frontal lobe;cerebral cortex;endometrium;larynx;placenta;visual apparatus;amnion;liver;head and neck;cervix;kidney;mammary gland;spinal ganglion;brain; amygdala;subthalamic nucleus;superior cervical ganglion;fetal brain;prefrontal cortex;globus pallidus;pons;trigeminal ganglion;cerebellum; 0.36722 . -1.304353358 4.91861288 94.25713 2.08898 L1RE1 . . . LINE1 retrotransposable element 1 FUNCTION: Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. May function as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded. {ECO:0000269|PubMed:11158327, ECO:0000269|PubMed:21937507, ECO:0000269|PubMed:8945518}.; . . . . . . . . . . L1RE2 . . . LINE1 retrotransposable element 2 . . . . . . . . . . . L1RE3 . . . LINE1 retrotransposable element 3 . . . . . . . . . . . L1RE4 . . . LINE1 retrotransposable element 4 . . . . . . . . . . . L1TD1 0.000340201048660737 0.822820452990442 0.176839345960897 LINE-1 type transposase domain containing 1 . . . . . 0.31943 0.07158 1.936492053 97.50530786 1046.59919 6.20893 L1TD1P1 . . . LINE-1 type transposase domain containing 1 pseudogene 1 . . . . . . . . . . . L2HGDH 0.309969498152224 0.689249835705755 0.000780666142020407 L-2-hydroxyglutarate dehydrogenase . . TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain, testis and muscle. Expressed to a lower extent in lymphocytes, fibroblasts, keratinocytes, placenta, bladder, small intestine, liver and bone marrow. {ECO:0000269|PubMed:15385440}.; unclassifiable (Anatomical System);uterus;lung;ovary;placenta;muscle;cervix;brain;peripheral nerve; superior cervical ganglion;globus pallidus; 0.39111 0.15887 0.018483465 55.44939844 155.34999 2.72333 L3HYPDH 1.52384322492068e-07 0.120752795080972 0.879247052534705 L-3-hydroxyproline dehydratase (trans-) FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline to Delta(1)-pyrroline-2-carboxylate (Pyr2C). May be required to degrade trans-3-hydroxy-L-proline from the diet and originating from the degradation of proteins such as collagen-IV that contain it. {ECO:0000269|PubMed:22528483}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:22528483}.; . . 0.10302 0.10230 0.328949044 73.41354093 623.92625 5.03864 L3MBTL1 2.0785493269036e-07 0.993446403001193 0.00655338914387425 l(3)mbt-like 1 (Drosophila) FUNCTION: Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post- translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis. {ECO:0000269|PubMed:17540172, ECO:0000269|PubMed:18408754, ECO:0000269|PubMed:20870719, ECO:0000269|PubMed:20870725}.; . TISSUE SPECIFICITY: Widely expressed. Expression is reduced in colorectal cancer cell line SW480 and promyelocytic leukemia cell line HL-60. {ECO:0000269|PubMed:10445843}.; . . 0.41701 0.10262 0.025760883 55.78556263 239.20304 3.34244 L3MBTL2 0.0130280434479328 0.986911838666868 6.01178851992325e-05 l(3)mbt-like 2 (Drosophila) FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. {ECO:0000269|PubMed:19233876}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;amniotic fluid;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;lens;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach;thymus; superior cervical ganglion;ciliary ganglion; 0.30184 0.10643 -1.172055164 6.027364945 286.32425 3.62314 L3MBTL3 0.999498723142149 0.000501276777339565 8.05113143848104e-11 l(3)mbt-like 3 (Drosophila) FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Required for normal maturation of myeloid progenitor cells (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);meninges;smooth muscle;heart;lacrimal gland;colon;blood;skin;skeletal muscle;bone marrow;uterus;prostate;pia mater;frontal lobe;visual apparatus;testis;dura mater;germinal center;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.63431 0.09837 -0.777005578 12.9747582 66.98885 1.69207 L3MBTL4 4.20004377573476e-08 0.942695624943074 0.0573043330564878 l(3)mbt-like 4 (Drosophila) FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;ovary;heart;epididymis;hippocampus;liver;testis;colon;spleen;kidney;lens;brain;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10682 . -0.953385901 9.206180703 899.26435 5.84010 L3MBTL4-AS1 . . . L3MBTL4 antisense RNA 1 . . . . . . . . . . . LACC1 4.63538843291218e-06 0.400785518196041 0.599209846415526 laccase domain containing 1 . DISEASE: Rheumatoid arthritis systemic juvenile (RASJ) [MIM:604302]: An inflammatory articular disorder with systemic- onset beginning before the age of 16. It represents a subgroup of juvenile arthritis associated with severe extraarticular features and occasionally fatal complications. During active phases of the disorder, patients display a typical daily spiking fever, an evanescent macular rash, lymphadenopathy, hepatosplenomegaly, serositis, myalgia and arthritis. {ECO:0000269|PubMed:25220867}. Note=The gene represented in this entry may be involved in disease pathogenesis.; . unclassifiable (Anatomical System);pancreas;lung;cartilage;endometrium;adrenal gland;bone;liver;testis;spleen; dorsal root ganglion;superior cervical ganglion;medulla oblongata;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15295 0.08991 0.018483465 55.44939844 2414.2291 9.12563 LACE1 2.79301253512425e-06 0.921850358019733 0.0781468489677318 lactation elevated 1 . . . . . 0.08986 0.15385 0.532823122 80.96249115 235.3731 3.31520 LACRT 8.87854549242137e-05 0.333488389306083 0.666422825238992 lacritin FUNCTION: Modulates secretion by lacrimal acinar cells.; . TISSUE SPECIFICITY: Expressed in secretory granules of many acinar cells in lacrimal gland and in scattered acinar cells of salivary glands.; breast;lacrimal gland;adrenal gland;thyroid;adrenal cortex;parathyroid;pineal gland; dorsal root ganglion;superior cervical ganglion;medulla oblongata;temporal lobe;globus pallidus;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.07212 0.08005 -0.141298762 42.87567823 4.61004 0.16543 LACTB 0.00265961207919234 0.935048311924227 0.0622920759965802 lactamase beta . . TISSUE SPECIFICITY: Expressed predominantly in skeletal muscle.; unclassifiable (Anatomical System);cartilage;heart;epidermis;islets of Langerhans;hypothalamus;colon;skin;uterus;breast;prostate;optic nerve;lung;frontal lobe;bone;placenta;visual apparatus;pituitary gland;liver;testis;spleen;kidney;brain;mammary gland;stomach;peripheral nerve; . 0.20152 0.12394 0.128714042 63.19886766 403.62925 4.21330 LACTB2 0.000281761255835968 0.789879446030944 0.209838792713221 lactamase beta 2 . . . colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;larynx;iris;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney; dorsal root ganglion;superior cervical ganglion; 0.14785 0.09084 -0.273576253 33.97027601 27.17329 0.87557 LACTB2-AS1 . . . LACTB2 antisense RNA 1 . . . . . . . . . . . LACTBL1 . . . lactamase beta like 1 . . . . . . . . . 3279.32208 10.92942 LAD1 4.12856291165876e-08 0.352837411804465 0.647162546909906 ladinin 1 FUNCTION: Anchoring filament protein which is a component of the basement membrane zone. {ECO:0000250}.; . . . . 0.10372 0.36542 0.845119304 88.4170795 1414.88538 7.02941 LAG3 0.109617010744363 0.889076637646457 0.0013063516091801 lymphocyte activating 3 FUNCTION: Involved in lymphocyte activation. Binds to HLA class-II antigens.; . TISSUE SPECIFICITY: On cell surface of activated NK and T- lymphocytes.; unclassifiable (Anatomical System);uterus;prostate;optic nerve;cartilage;heart;colon;spleen;blood;skin;stomach; superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion; 0.14204 0.15158 0.330767508 73.53739089 199.00051 3.04866 LAGE3 0.227379900839686 0.646719133300502 0.125900965859811 L antigen family member 3 FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. LAGE3 functions as a dimerization module for the complex (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12384295, ECO:0000269|PubMed:8786131}.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;blood;skeletal muscle;uterus;pancreas;prostate;lung;bone;placenta;liver;testis;spleen;germinal center;kidney;brain;mammary gland; whole brain;amygdala;subthalamic nucleus;medulla oblongata;temporal lobe;prefrontal cortex;liver;globus pallidus;pons;caudate nucleus;parietal lobe;cerebellum; 0.10037 0.08342 . . 62.82541 1.62247 LAGE3P1 . . . L antigen family member 3 pseudogene 1 . . . . . . . . . . . LAIR1 2.06316475615001e-05 0.71364781309932 0.286331555253119 leukocyte associated immunoglobulin like receptor 1 FUNCTION: Functions as an inhibitory receptor that plays a constitutive negative regulatory role on cytolytic function of natural killer (NK) cells, B-cells and T-cells. Activation by Tyr phosphorylation results in recruitment and activation of the phosphatases PTPN6 and PTPN11. It also reduces the increase of intracellular calcium evoked by B-cell receptor ligation. May also play its inhibitory role independently of SH2-containing phosphatases. Modulates cytokine production in CD4+ T-cells, down- regulating IL2 and IFNG production while inducing secretion of transforming growth factor beta. Down-regulates also IgG and IgE production in B-cells as well as IL8, IL10 and TNF secretion. Inhibits proliferation and induces apoptosis in myeloid leukemia cell lines as well as prevents nuclear translocation of NF-kappa-B p65 subunit/RELA and phosphorylation of I-kappa-B alpha/CHUK in these cells. Inhibits the differentiation of peripheral blood precursors towards dendritic cells. {ECO:0000269|PubMed:10229813, ECO:0000269|PubMed:10764762, ECO:0000269|PubMed:11069054, ECO:0000269|PubMed:11160222, ECO:0000269|PubMed:12072189, ECO:0000269|PubMed:15939744, ECO:0000269|PubMed:15950745, ECO:0000269|PubMed:16380958, ECO:0000269|PubMed:9285412, ECO:0000269|PubMed:9692876}.; . TISSUE SPECIFICITY: Expressed on the majority of peripheral mononuclear cells, including natural killer (NK) cells, T-cells, B-cells, monocytes, and dendritic cells. Highly expressed in naive T-cells and B-cells but no expression on germinal center B-cells. Abnormally low expression in naive B-cells from HIV-1 infected patients. Very low expression in NK cells from a patient with chronic active Epstein-Barr virus infection. {ECO:0000269|PubMed:10540327, ECO:0000269|PubMed:12757266, ECO:0000269|PubMed:14604962, ECO:0000269|PubMed:15950745}.; unclassifiable (Anatomical System);lymph node;heart;colon;blood;choroid;skin;bone marrow;breast;uterus;pancreas;prostate;lung;frontal lobe;endometrium;bone;placenta;iris;liver;spleen;kidney;mammary gland;brain;thymus; dorsal root ganglion;superior cervical ganglion;white blood cells;atrioventricular node;trigeminal ganglion;thymus;bone marrow; 0.03531 0.07153 1.530453833 95.52960604 114.09006 2.32785 LAIR2 0.00013897405806663 0.412386095320248 0.587474930621685 leukocyte associated immunoglobulin like receptor 2 . . . uterus;placenta; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.07022 . 0.371224249 75.12384996 330.9271 3.86934 LAKLG . . . lymphokine-activated killer cell ligand . . . . . . . . . . . LALBA 0.395945445252935 0.563467682835673 0.0405868719113921 lactalbumin alpha FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.; . TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.14095 0.20060 0.169169615 65.33380514 4.26837 0.15530 LAMA1 1.39176131837658e-24 0.999998922616768 1.07738323149492e-06 laminin subunit alpha 1 FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.; DISEASE: Poretti-Boltshauser syndrome (PTBHS) [MIM:615960]: An autosomal recessive disorder characterized by cerebellar dysplasia, cerebellar vermis atrophy, cerebellar cysts in most patients, high myopia, variable retinal dystrophy, and eye movement abnormalities including strabismus, ocular apraxia, nystagmus. Affected individuals have ataxia, delayed motor development, language impairment, and intellectual disability with variable severity. {ECO:0000269|PubMed:25105227}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;placenta;macula lutea;visual apparatus;liver;hypopharynx;head and neck;kidney; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.17438 . 0.731301069 86.21726822 6734.8647 17.42321 LAMA2 1.1846527263111e-24 0.999999997723819 2.27618135802507e-09 laminin subunit alpha 2 FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.; DISEASE: Merosin-deficient congenital muscular dystrophy 1A (MDC1A) [MIM:607855]: Characterized by difficulty walking, hypotonia, proximal weakness, hyporeflexia, and white matter hypodensity on MRI. {ECO:0000269|PubMed:11591858, ECO:0000269|PubMed:12552556}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Placenta, striated muscle, peripheral nerve, cardiac muscle, pancreas, lung, spleen, kidney, adrenal gland, skin, testis, meninges, choroid plexus, and some other regions of the brain; not in liver, thymus and bone.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;larynx;thyroid;bone;testis;brain;gall bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;adrenal cortex;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;adipose tissue;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.30049 0.63589 0.497724973 79.64142486 3368.62227 11.11486 LAMA3 4.40816622681492e-24 0.999999999654994 3.45006155204169e-10 laminin subunit alpha 3 FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.; DISEASE: Epidermolysis bullosa, junctional, Herlitz type (H-JEB) [MIM:226700]: An infantile and lethal form of junctional epidermolysis bullosa, a group of blistering skin diseases characterized by tissue separation which occurs within the dermo- epidermal basement In the Herlitz type, death occurs usually within the first six months of life. Occasionally, children survive to teens. It is marked by bullous lesions at birth and extensive denudation of skin and mucous membranes that may be hemorrhagic. {ECO:0000269|PubMed:7633458, ECO:0000269|PubMed:8530087}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Laryngoonychocutaneous syndrome (LOCS) [MIM:245660]: Autosomal recessive epithelial disorder confined to the Punjabi Muslim population. The condition is characterized by cutaneous erosions, nail dystrophy and exuberant vascular granulation tissue in certain epithelia, especially conjunctiva and larynx. {ECO:0000269|PubMed:12915477}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Skin; respiratory, urinary, and digestive epithelia and in other specialized tissues with prominent secretory or protective functions. Epithelial basement membrane, and epithelial cell tongue that migrates into a wound bed. A differential and focal expression of the subunit alpha-3 is observed in the CNS.; ovary;colon;parathyroid;skin;retina;uterus;prostate;endometrium;larynx;gum;thyroid;bone;testis;bladder;unclassifiable (Anatomical System);heart;cartilage;tongue;skeletal muscle;breast;pancreas;lung;placenta;liver;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;olfactory bulb;lung;placenta;globus pallidus;ciliary ganglion;fetal lung;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10300 0.40300 -2.056005418 1.633640009 2266.53598 8.79873 LAMA4 9.75012432919925e-09 0.9999999282783 6.1971575299291e-08 laminin subunit alpha 4 FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.; DISEASE: Cardiomyopathy, dilated 1JJ (CMD1JJ) [MIM:615235]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:17646580}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In adult, strong expression in heart, lung, ovary small and large intestines, placenta, liver; weak or no expression in skeletal muscle, kidney, pancreas, testis, prostate, brain. High expression in fetal lung and kidney. Expression in fetal and newborn tissues is observed in certain mesenchymal cells in tissues such as smooth muscle and dermis.; myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;iris;testis;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;tongue;spinal cord;urinary;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; uterus;dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13815 0.40001 -1.3304325 4.676810569 3392.7618 11.15233 LAMA5 0.943037981027839 0.0569620189721609 9.75172390273245e-22 laminin subunit alpha 5 FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.; . TISSUE SPECIFICITY: Expressed in heart, lung, kidney, skeletal muscle, pancreas, retina and placenta. Little or no expression in brain and liver.; ovary;adrenal medulla;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;larynx;thyroid;testis;dura mater;germinal center;spinal ganglion;brain;bladder;gall bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;urinary;blood;lens;breast;pancreas;pia mater;lung;epididymis;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; . 0.70971 . 3.125188892 99.28049068 9086.1435 20.60876 LAMA5-AS1 . . . LAMA5 antisense RNA 1 . . . . . . . . . . . LAMB1 1.79440028222301e-06 0.999998205428291 1.71426281071056e-10 laminin subunit beta 1 FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface. {ECO:0000269|PubMed:23472759}.; DISEASE: Lissencephaly 5 (LIS5) [MIM:615191]: An autosomal recessive brain malformation characterized by cobblestone changes in the cortex, more severe in the posterior region, and subcortical band heterotopia. Affected individuals have hydrocephalus, seizures, and severely delayed psychomotor development. {ECO:0000269|PubMed:23472759}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;frontal lobe;endometrium;cochlea;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;uterus;whole body;larynx;bone;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;adipose tissue;smooth muscle;olfactory bulb;fetal lung;ciliary ganglion;atrioventricular node; 0.83862 0.50146 -0.994232378 8.545647558 2293.09009 8.86833 LAMB2 7.45006902753361e-11 0.999999886164894 1.13760604992026e-07 laminin subunit beta 2 FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.; DISEASE: Pierson syndrome (PIERSS) [MIM:609049]: Characterized by nephrotic syndrome with neonatal onset, diffuse mesangial sclerosis and eye abnormalities with microcoria as the leading clinical feature. Death usually occurs within the first weeks of life. Disease severity depends on the mutation type: nontruncating LAMB2 mutations may display variable phenotypes ranging from a milder variant of Pierson syndrome to isolated congenital nephrotic syndrome. {ECO:0000269|PubMed:15367484, ECO:0000269|PubMed:16912710}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Nephrotic syndrome 5 with or without ocular abnormalities (NPHS5) [MIM:614199]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. NPHS5 is characterized by very early onset of progressive renal failure. A subset of patients may develop mild ocular anomalies, such as myopia, nystagmus, and strabismus. {ECO:0000269|PubMed:21236492}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;synovium;bone;testis;unclassifiable (Anatomical System);small intestine;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;internal ear;placenta;hypopharynx;head and neck;kidney;stomach;cerebellum; superior cervical ganglion; 0.17179 0.41907 -1.464556369 3.75678226 1285.70422 6.74954 LAMB2P1 . . . laminin subunit beta 2 pseudogene 1 . . . . . . . . . . . LAMB3 1.36402401238307e-09 0.999378217717037 0.000621780918938427 laminin subunit beta 3 FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.; DISEASE: Epidermolysis bullosa, junctional, Herlitz type (H-JEB) [MIM:226700]: An infantile and lethal form of junctional epidermolysis bullosa, a group of blistering skin diseases characterized by tissue separation which occurs within the dermo- epidermal basement In the Herlitz type, death occurs usually within the first six months of life. Occasionally, children survive to teens. It is marked by bullous lesions at birth and extensive denudation of skin and mucous membranes that may be hemorrhagic. {ECO:0000269|PubMed:7550237}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Generalized atrophic benign epidermolysis bullosa (GABEB) [MIM:226650]: A non-lethal, adult form of junctional epidermolysis bullosa characterized by life-long blistering of the skin, associated with hair and tooth abnormalities. {ECO:0000269|PubMed:17476356, ECO:0000269|PubMed:9767254}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Amelogenesis imperfecta 1A (AI1A) [MIM:104530]: A form of amelogenesis imperfecta, a disorder characterized by defective enamel formation. The enamel may be hypoplastic, hypomineralized or both, and affected teeth may be discoloured, sensitive or prone to disintegration. {ECO:0000269|PubMed:23632796, ECO:0000269|PubMed:23958762}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in the basement membranes (major component).; lymphoreticular;ovary;colon;skin;bone marrow;uterus;prostate;oesophagus;endometrium;larynx;gum;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);tongue;islets of Langerhans;urinary;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;alveolus;liver;head and neck;cervix;mammary gland;stomach;aorta; lung; 0.10251 0.32681 0.400378756 76.36234961 3287.08286 10.94320 LAMB4 3.21022487204354e-30 0.00261457264953261 0.997385427350467 laminin subunit beta 4 FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.; . . unclassifiable (Anatomical System);uterus;heart;skin; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skin; 0.09686 0.26112 -1.552781294 3.237791932 3441.9669 11.26972 LAMC1 0.999999624623106 3.75376893693012e-07 3.96446497756518e-19 laminin subunit gamma 1 FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.; . TISSUE SPECIFICITY: Found in the basement membranes (major component).; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;amnion;head and neck;kidney;stomach;aorta; smooth muscle;olfactory bulb;adipose tissue;heart;placenta;appendix;fetal lung; 0.17228 0.38763 -2.488226108 0.943618778 818.91934 5.62079 LAMC2 7.93300382052603e-05 0.999919362318044 1.30764375107454e-06 laminin subunit gamma 2 FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell- scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells. {ECO:0000269|PubMed:8265624}.; DISEASE: Epidermolysis bullosa, junctional, Herlitz type (H-JEB) [MIM:226700]: An infantile and lethal form of junctional epidermolysis bullosa, a group of blistering skin diseases characterized by tissue separation which occurs within the dermo- epidermal basement In the Herlitz type, death occurs usually within the first six months of life. Occasionally, children survive to teens. It is marked by bullous lesions at birth and extensive denudation of skin and mucous membranes that may be hemorrhagic. {ECO:0000269|PubMed:11810295, ECO:0000269|PubMed:8012393}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: The large variant is expressed only in specific epithelial cells of embryonic and neonatal tissues. In 17-week old embryo the small variant is found in cerebral cortex, lung, and distal tubes of kidney, but not in epithelia except for distal tubuli.; ovary;colon;parathyroid;skin;uterus;prostate;endometrium;larynx;gum;bone;thyroid;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;placenta;liver;hypopharynx;spleen;head and neck;kidney;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;lung;trigeminal ganglion;skeletal muscle; 0.09677 0.41301 0.551058225 81.3871196 1938.54056 8.10025 LAMC3 9.82326673498679e-11 0.998888700472002 0.00111129942976517 laminin subunit gamma 3 FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.; DISEASE: Cortical malformations occipital (OCCM) [MIM:614115]: A disease in which affected individuals develop seizures, sometimes associated with transient visual changes. Brain MRI shows both pachygyria and polymicrogyria restricted to the lateral occipital lobes. {ECO:0000269|PubMed:21572413}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Broadly expressed in: skin, heart, lung, and the reproductive tracts.; unclassifiable (Anatomical System);ovary;heart;cartilage;islets of Langerhans;colon;parathyroid;choroid;skin;uterus;pancreas;whole body;optic nerve;lung;frontal lobe;larynx;placenta;visual apparatus;liver;testis;head and neck;brain;gall bladder; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;placenta;adrenal cortex;testis; 0.15545 . 0.637377588 83.64000944 7208.01279 18.27431 LAMP1 0.978974558833222 0.0210073177325735 1.81234342044486e-05 lysosomal associated membrane protein 1 FUNCTION: Presents carbohydrate ligands to selectins. Also implicated in tumor cell metastasis.; . . smooth muscle;ovary;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;duodenum;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; placenta;thyroid;spinal cord;liver;kidney; 0.16910 0.79202 -0.200157416 39.11299835 392.80541 4.16901 LAMP1P1 . . . lysosomal associated membrane protein 1 pseudogene 1 . . . . . . . . . . . LAMP2 0.949783835469488 0.0500592363121834 0.000156928218328767 lysosomal associated membrane protein 2 FUNCTION: Implicated in tumor cell metastasis. May function in protection of the lysosomal membrane from autodigestion, maintenance of the acidic environment of the lysosome, adhesion when expressed on the cell surface (plasma membrane), and inter- and intracellular signal transduction. Protects cells from the toxic effects of methylating mutagens. {ECO:0000269|PubMed:8407947}.; DISEASE: Danon disease (DAND) [MIM:300257]: DAND is a lysosomal glycogen storage disease characterized by the clinical triad of cardiomyopathy, vacuolar myopathy and mental retardation. It is often associated with an accumulation of glycogen in muscle and lysosomes. {ECO:0000269|PubMed:15673802, ECO:0000269|PubMed:15907287}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform LAMP-2A is highly expressed in placenta, lung and liver, less in kidney and pancreas, low in brain and skeletal muscle. Isoform LAMP-2B is highly expressed in skeletal muscle, less in brain, placenta, lung, kidney and pancreas, very low in liver.; smooth muscle;ovary;skin;bone marrow;prostate;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;amnion;kidney;stomach;aorta; amygdala;prostate;occipital lobe;hypothalamus;placenta;spinal cord;prefrontal cortex;caudate nucleus;kidney;whole blood;parietal lobe; 0.49930 0.61796 0.106667882 61.73036093 29.76807 0.94900 LAMP3 0.833342526965146 0.165947623954927 0.000709849079926836 lysosomal associated membrane protein 3 FUNCTION: May play a role in dendritic cell function and in adaptive immunity. {ECO:0000269|PubMed:9768752}.; . TISSUE SPECIFICITY: Detected in tonsil interdigitating dendritic cells, in spleen, lymph node, Peyer's patches in the small instestine, in thymus medulla and in B-cells (at protein level). Expressed in lymphoid organs and dendritic cells. Expressed in lung. Up-regulated in carcinomas of the esophagus, colon, rectum, ureter, stomach, breast, fallopian tube, thyroid and parotid tissues. {ECO:0000269|PubMed:21930964, ECO:0000269|PubMed:9721848, ECO:0000269|PubMed:9768752}.; unclassifiable (Anatomical System);cartilage;ovary;breast;lung;oesophagus;larynx;nasopharynx;placenta;hypopharynx;testis;head and neck;brain;aorta;stomach; superior cervical ganglion;lung;testis;fetal lung;atrioventricular node;skeletal muscle; 0.12760 0.30104 -0.224023033 37.4321774 31.08249 0.98172 LAMP5 3.83650327709959e-08 0.104003259705179 0.895996701929789 lysosomal associated membrane protein family member 5 . . TISSUE SPECIFICITY: Expressed in plasmocytoid dendritic cells. Expressed in suprabasal skin keratinocytes and squamous cells (at protein level). Expressed in the brain and weakly in spleen and skin. Expressed in plasmocytoid dendritic cells. {ECO:0000269|PubMed:21642595}.; heart;hypothalamus;bone marrow;breast;pancreas;prostate;whole body;lung;frontal lobe;endometrium;thyroid;placenta;pituitary gland;liver;testis;head and neck;spleen;kidney;brain; whole brain;amygdala;subthalamic nucleus;medulla oblongata;occipital lobe;temporal lobe;prefrontal cortex;globus pallidus;pons;caudate nucleus;parietal lobe;cingulate cortex;cerebellum; 0.42339 . 0.260991686 70.25831564 2514.20203 9.34534 LAMP5-AS1 . . . LAMP5 antisense RNA 1 . . . . . . . . . . . LAMTOR1 0.435675722554207 0.533372086093681 0.0309521913521123 late endosomal/lysosomal adaptor, MAPK and MTOR activator 1 FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. LAMTOR1 is directly responsible for anchoring the Ragulator complex to membranes. Also required for late endosomes/lysosomes biogenesis it may regulate both the recycling of receptors through endosomes and the MAPK signaling pathway through recruitment of some of its components to late endosomes. May be involved in cholesterol homeostasis regulating LDL uptake and cholesterol release from late endosomes/lysosomes. May also play a role in RHOA activation. {ECO:0000269|PubMed:19654316, ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:20544018, ECO:0000269|PubMed:22980980}.; . . lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; . 0.41196 0.12971 -0.141298762 42.87567823 15.85969 0.56352 LAMTOR2 0.481086311682732 0.496380187385422 0.0225335009318465 late endosomal/lysosomal adaptor, MAPK and MTOR activator 2 FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2. {ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:22980980}.; DISEASE: Immunodeficiency due to defect in MAPBP-interacting protein (ID-MAPBPIP) [MIM:610798]: This form of primary immunodeficiency syndrome includes congenital neutropenia, partial albinism, short stature and B-cell and cytotoxic T-cell deficiency. {ECO:0000269|PubMed:17195838}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . 0.08266 0.035072054 56.2514744 2.63616 0.09609 LAMTOR3 0.68057944478499 0.314901012109651 0.00451954310535962 late endosomal/lysosomal adaptor, MAPK and MTOR activator 3 FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2. {ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:22980980}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion; 0.35412 0.10819 0.013025609 54.62962963 1.24663 0.04397 LAMTOR3P1 . . . late endosomal/lysosomal adaptor, MAPK and MTOR activator 3 pseudogene 1 . . . . . . . . . . . LAMTOR3P2 . . . late endosomal/lysosomal adaptor, MAPK and MTOR activator 3 pseudogene 2 . . . . . . . . . . . LAMTOR4 0.0256870248906026 0.785054693393394 0.189258281716003 late endosomal/lysosomal adaptor, MAPK and MTOR activator 4 FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. {ECO:0000269|PubMed:22980980}.; . . . . . 0.10747 -0.053113545 49.38664779 64.78507 1.65258 LAMTOR5 0.00711604756483594 0.765457097587251 0.227426854847913 late endosomal/lysosomal adaptor, MAPK and MTOR activator 5 FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. When complexed to BIRC5, interferes with apoptosome assembly, preventing recruitment of pro-caspase-9 to oligomerized APAF1, thereby selectively suppressing apoptosis initiated via the mitochondrial/cytochrome c pathway. Down-regulates hepatitis B virus (HBV) replication. {ECO:0000269|PubMed:12773388, ECO:0000269|PubMed:22980980}.; . TISSUE SPECIFICITY: Highly expressed in skeletal and cardiac muscle, followed by pancreas, kidney, liver, brain, placenta and lung. Elevated levels in both cancerous and non-cancerous liver tissue of patients with chronic HBV infection compared with hepatic tissue without HBV infection.; . . 0.13196 0.11967 0.705562627 85.52724699 1461.18225 7.12800 LAMTOR5-AS1 . . . LAMTOR5 antisense RNA 1 . . . . . . . . . . . LAMTOR5P1 . . . late endosomal/lysosomal adaptor, MAPK and MTOR activator 5 pseudogene 1 . . . . . . . . . . . LANCL1 9.92097579258599e-06 0.788573820345868 0.21141625867834 LanC like 1 FUNCTION: May play a role in EPS8 signaling. Binds glutathione. {ECO:0000269|PubMed:19528316}.; . TISSUE SPECIFICITY: Detected in erythrocytes, brain, kidney, testis, ovary, heart, lung, placenta and spleen (at protein level). Ubiquitous. Strongly expressed in brain, spinal cord, pituitary gland, kidney, heart, skeletal muscle, pancreas, ovary and testis. {ECO:0000269|PubMed:10944443, ECO:0000269|PubMed:15811525, ECO:0000269|PubMed:9512664}.; ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;amygdala;heart;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;kidney;aorta;stomach;thymus; whole brain;dorsal root ganglion;amygdala;testis - interstitial;occipital lobe;medulla oblongata;superior cervical ganglion;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;atrioventricular node;pons;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.23835 0.11610 0.242582624 69.45623968 94.51553 2.09329 LANCL1-AS1 . . . LANCL1 antisense RNA 1 . . . . . . . . . . . LANCL2 0.786760146345929 0.213181752551996 5.81011020749157e-05 LanC like 2 FUNCTION: Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes. {ECO:0000269|PubMed:19667068}.; . TISSUE SPECIFICITY: Expressed in brain and testis. {ECO:0000269|PubMed:11762191}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;blood;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;trigeminal ganglion;skeletal muscle; 0.11564 0.11840 -0.045835247 50.34206181 631.31618 5.06137 LANCL3 0.522828102456292 0.460514541556954 0.0166573559867538 LanC like 3 . . . . . 0.06197 0.09447 . . 42.24275 1.22945 LAP3 0.00122013401187321 0.989811258474164 0.00896860751396305 leucine aminopeptidase 3 FUNCTION: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.; . . lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;mesenchyma;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; testis - interstitial;testis; 0.21337 0.64287 -0.510624372 21.65015334 47.07269 1.32721 LAP3P1 . . . leucine aminopeptidase 3 pseudogene 1 . . . . . . . . . . . LAP3P2 . . . leucine aminopeptidase 3 pseudogene 2 . . . . . . . . . . . LAPTM4A 0.503802410255576 0.492021028781595 0.00417656096282905 lysosomal protein transmembrane 4 alpha FUNCTION: May function in the transport of nucleosides and/or nucleoside derivatives between the cytosol and the lumen of an intracellular membrane-bound compartment. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;adrenal cortex;blood;lens;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;placenta;thyroid;testis;kidney; 0.43282 0.10804 -0.139478553 43.29440906 119.75939 2.38284 LAPTM4B 3.42948861043789e-05 0.58303732129823 0.416928383815665 lysosomal protein transmembrane 4 beta . . . . . 0.48759 0.10563 -0.381986487 27.68931352 162.96113 2.78656 LAPTM4BP1 . . . lysosomal protein transmembrane 4 beta pseudogene 1 . . . . . . . . . . . LAPTM4BP2 . . . lysosomal protein transmembrane 4 beta pseudogene 2 . . . . . . . . . . . LAPTM5 0.735702166051801 0.261722388744452 0.00257544520374696 lysosomal protein transmembrane 5 FUNCTION: May have a special functional role during embryogenesis and in adult hematopoietic cells. {ECO:0000269|PubMed:8661146}.; . TISSUE SPECIFICITY: Preferentially expressed in adult hematopoietic tissues. High levels in lymphoid and myeloid tissues. Highly expressed in peripheral blood leukocytes, thymus, spleen and lung, followed by placenta, liver and kidney. {ECO:0000269|PubMed:8661146}.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;oesophagus;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pineal body;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;aorta;stomach;thymus; lymph node;white blood cells;whole blood;tonsil;thymus;bone marrow; 0.14904 0.13261 0.284856336 71.40835103 532.65399 4.70729 LARGE 0.958481011778369 0.0415188235959897 1.64625640953711e-07 like-glycosyltransferase FUNCTION: Bifunctional glycosyltransferase with both xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine- beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1) (PubMed:22223806). Phosphorylated O- mannosyl trisaccharid is required for binding laminin G-like domain-containing extracellular proteins with high affinity and plays a key role in skeletal muscle function and regeneration. LARGE elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure initiated by B3GNT1/B4GAT1 by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide (PubMed:25279699). {ECO:0000269|PubMed:15661757, ECO:0000269|PubMed:15752776, ECO:0000269|PubMed:21987822, ECO:0000269|PubMed:22223806, ECO:0000269|PubMed:25138275, ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699}.; DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A6 (MDDGA6) [MIM:613154]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with cobblestone lissencephaly and other brain anomalies, eye malformations, profound mental retardation, and death usually in the first years of life. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease. {ECO:0000269|PubMed:19067344, ECO:0000269|PubMed:19299310}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Highest expression in heart, brain and skeletal muscle. {ECO:0000269|PubMed:15752776}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;uterus;optic nerve;whole body;cochlea;endometrium;iris;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;muscle;pharynx;blood;skeletal muscle;breast;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;cerebellum; whole brain;occipital lobe;superior cervical ganglion;pons;caudate nucleus;trigeminal ganglion;parietal lobe;cerebellum; 0.08067 0.34914 -0.617221851 17.44515216 310.89903 3.75239 LARGE-AS1 . . . LARGE antisense RNA 1 . . . . . . . . . . . LARGE-IT1 . . . LARGE intronic transcript 1 . . . . . . . . . . . LARP1 0.9999521889832 4.78110167465247e-05 5.31840225155132e-14 La ribonucleoprotein domain family member 1 FUNCTION: RNA-binding protein that promotes translation of specific classes of mRNAs downstream of the mTORC1 complex. Associates with the mRNA 5'cap in an MTOR-dependent manner and associates with mRNAs containing a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs encoding for ribosomal proteins and several components of the translation machinery. Associates with actively translating ribosomes via interaction with PABPC1/PABP and stimulates translation of mRNAs containing a 5'TOP, thereby regulating cell growth and proliferation. {ECO:0000269|PubMed:20430826, ECO:0000269|PubMed:23711370, ECO:0000269|PubMed:24532714}.; . . myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;amygdala;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus;cerebellum; medulla oblongata;occipital lobe;thalamus;superior cervical ganglion;hypothalamus;temporal lobe;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;testis;parietal lobe;cingulate cortex;cerebellum; 0.27569 0.09050 -1.350267166 4.600141543 57.4938 1.52959 LARP1B 2.24164431739323e-06 0.999953445426085 4.4312929597087e-05 La ribonucleoprotein domain family member 1B . . . medulla oblongata;colon;skin;bone marrow;prostate;whole body;frontal lobe;endometrium;thyroid;bone;testis;germinal center;artery;brain;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;skeletal muscle;breast;lung;placenta;visual apparatus;liver;head and neck;kidney;aorta; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.65320 . 0.760574103 86.83062043 226.20479 3.24995 LARP1BP1 . . . La ribonucleoprotein domain family member 1B pseudogene 1 . . . . . . . . . . . LARP1BP2 . . . La ribonucleoprotein domain family member 1B pseudogene 2 . . . . . . . . . . . LARP1BP3 . . . La ribonucleoprotein domain family member 1B pseudogene 3 . . . . . . . . . . . LARP1P1 . . . La ribonucleoprotein domain family member 1 pseudogene 1 . . . . . . . . . . . LARP4 0.994628855689498 0.00537114323907517 1.07142682986482e-09 La ribonucleoprotein domain family member 4 FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:21834987}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;adrenal cortex;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.31621 . -0.754958418 13.57631517 537.72558 4.72769 LARP4B 0.999885803939474 0.000114196049694167 1.08313633779888e-11 La ribonucleoprotein domain family member 4B FUNCTION: Stimulates mRNA translation. {ECO:0000269|PubMed:20573744}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;placenta;testis;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.58444 0.10818 -1.063626766 7.484076433 58.52951 1.54984 LARP4P . . . La ribonucleoprotein domain family member 4 pseudogene . . . . . . . . . . . LARP6 0.882216412282497 0.116420388549018 0.00136319916848468 La ribonucleoprotein domain family member 6 FUNCTION: Regulates the coordinated translation of type I collagen alpha-1 and alpha-2 mRNAs, CO1A1 and CO1A2. Stabilizes mRNAs through high-affinity binding of a stem-loop structure in their 5' UTR. This regulation requires VIM and MYH10 filaments, and the helicase DHX9. {ECO:0000269|PubMed:20603131, ECO:0000269|PubMed:21746880, ECO:0000269|PubMed:22190748}.; . TISSUE SPECIFICITY: Expressed in numerous tissues. {ECO:0000269|PubMed:17383118}.; myocardium;ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;cerebral cortex;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;muscle;adrenal cortex;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland; whole brain;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;temporal lobe;pons;caudate nucleus;subthalamic nucleus;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex; 0.17235 0.11498 -0.290161348 33.33923095 28.78654 0.92036 LARP7 0.0150803234132968 0.983738828167994 0.00118084841870952 La ribonucleoprotein domain family member 7 FUNCTION: Negative transcriptional regulator of polymerase II genes, acting by means of the 7SK RNP system. Within the 7SK RNP complex, the positive transcription elongation factor b (P-TEFb) is sequestered in an inactive form, preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. {ECO:0000269|PubMed:18249148, ECO:0000269|PubMed:18483487}.; DISEASE: Alazami syndrome (ALAZS) [MIM:615071]: A syndromic form of primordial dwarfism, a condition characterized by severe growth restriction that has its onset in utero, and results in short stature and undersize. ALAZS patients manifest severe intellectual disability and distinct facial features including malar hypoplasia, deep-set eyes, broad nose, short philtrum, and macrostomia. Some patients have non-specific and inconsistent skeletal findings, for example, scoliosis and mild epiphyseal changes in the proximal phalanges, but no frank dysplasia. {ECO:0000269|PubMed:21937992, ECO:0000269|PubMed:22865833}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;pia mater;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;ciliary ganglion;pons;skeletal muscle; 0.49890 0.11332 0.242582624 69.45623968 898.22165 5.83839 LARP7P1 . . . La ribonucleoprotein domain family member 7 pseudogene 1 . . . . . . . . . . . LARP7P2 . . . La ribonucleoprotein domain family member 7 pseudogene 2 . . . . . . . . . . . LARP7P3 . . . La ribonucleoprotein domain family member 7 pseudogene 3 . . . . . . . . . . . LARP7P4 . . . La ribonucleoprotein domain family member 7 pseudogene 4 . . . . . . . . . . . LARS 2.27045044262368e-05 0.99997697275345 3.22742124085335e-07 leucyl-tRNA synthetase FUNCTION: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Exhibits a post-transfer editing activity to hydrolyze mischarged tRNAs. {ECO:0000269|PubMed:19426743}.; DISEASE: Infantile liver failure syndrome 1 (ILFS1) [MIM:615438]: A life-threatening disorder of hepatic function that manifests with acute liver failure in the first few months of life. Clinical features include anemia, renal tubulopathy, developmental delay, seizures, failure to thrive, and liver steatosis and fibrosis. {ECO:0000269|PubMed:22607940}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;bone;pituitary gland;testis;dura mater;spinal ganglion;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;muscle;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;amnion;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.76027 . -0.437212558 24.67563105 3699.75044 11.85134 LARS2 2.60643828587561e-07 0.999028422000348 0.000971317355822927 leucyl-tRNA synthetase 2, mitochondrial . . TISSUE SPECIFICITY: Ubiquitously expressed, but highest expression in tissues with high metabolic rates, such as skeletal muscle, heart, and kidney. {ECO:0000269|PubMed:20194621}.; ovary;salivary gland;intestine;colon;choroid;skin;uterus;prostate;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;pharynx;blood;lens;skeletal muscle;lung;cornea;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.52631 0.23328 -0.749505784 13.74144845 355.93789 3.99286 LARS2-AS1 . . . LARS2 antisense RNA 1 . . . . . . . . . . . LAS1L 0.892095595186022 0.107858801853445 4.56029605338138e-05 LAS1-like, ribosome biogenesis factor FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. Required for maturation of the 28S rRNA. Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. {ECO:0000269|PubMed:20647540, ECO:0000269|PubMed:22872859}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;choroid;skin;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;epididymis;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; uterus;superior cervical ganglion;tumor;white blood cells; 0.10697 0.08070 -0.093566408 46.7386176 7.8908 0.28968 LASP1 0.8667394350595 0.132870173708275 0.000390391232224815 LIM and SH3 protein 1 FUNCTION: Plays an important role in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;skin;bone marrow;prostate;frontal lobe;endometrium;germinal center;bladder;brain;tonsil;amygdala;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;uterus;cerebral cortex;larynx;testis;pineal gland;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; whole blood; 0.33295 0.11829 -0.449946534 24.00330267 12.83432 0.46825 LAT 0.0974332943635584 0.900968663655503 0.00159804198093857 linker for activation of T-cells FUNCTION: Required for TCR (T-cell antigen receptor)- and pre-TCR- mediated signaling, both in mature T-cells and during their development. Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Couples activation of these receptors and their associated kinases with distal intracellular events such as mobilization of intracellular calcium stores, PKC activation, MAPK activation or cytoskeletal reorganization through the recruitment of PLCG1, GRB2, GRAP2, and other signaling molecules. {ECO:0000269|PubMed:10072481}.; . TISSUE SPECIFICITY: Expressed in thymus, T-cells, NK cells, mast cells and, at lower levels, in spleen. Present in T-cells but not B-cells (at protein level). {ECO:0000269|PubMed:16160011, ECO:0000269|PubMed:9489702}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;macula lutea;spleen;head and neck;kidney;thymus; trigeminal ganglion;thymus; 0.15140 . -0.53631094 20.53550366 82.82682 1.93304 LAT2 0.000691063098880473 0.916242937788671 0.0830659991124487 linker for activation of T-cells family member 2 FUNCTION: Involved in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. May also be involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these receptors and their associated kinases with distal intracellular events through the recruitment of GRB2. {ECO:0000269|PubMed:12486104, ECO:0000269|PubMed:12514734, ECO:0000269|PubMed:15010370}.; DISEASE: Note=LAT2 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of LAT2 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease. {ECO:0000269|PubMed:11003705, ECO:0000269|PubMed:11124535, ECO:0000269|Ref.5}.; TISSUE SPECIFICITY: Highly expressed in spleen, peripheral blood lymphocytes, and germinal centers of lymph nodes. Also expressed in placenta, lung, pancreas and small intestine. Present in B- cells, NK cells and monocytes. Absent from T-cells (at protein level). {ECO:0000269|PubMed:11124535, ECO:0000269|PubMed:12486104, ECO:0000269|PubMed:12514734, ECO:0000269|PubMed:16160011}.; ovary;umbilical cord;colon;fovea centralis;choroid;bone marrow;retina;uterus;prostate;optic nerve;cerebral cortex;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;kidney; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle;bone marrow; 0.10315 0.09283 0.082802743 60.09082331 70.20994 1.73987 LATS1 0.999926526245065 7.34737541862348e-05 7.48586338898208e-13 large tumor suppressor kinase 1 FUNCTION: Negative regulator of YAP1 in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Acts as a tumor suppressor which plays a critical role in maintenance of ploidy through its actions in both mitotic progression and the G1 tetraploidy checkpoint. Negatively regulates G2/M transition by down-regulating CDK1 kinase activity. Involved in the control of p53 expression. Affects cytokinesis by regulating actin polymerization through negative modulation of LIMK1. May also play a role in endocrine function. {ECO:0000269|PubMed:10518011, ECO:0000269|PubMed:10831611, ECO:0000269|PubMed:15122335, ECO:0000269|PubMed:15220930, ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:19927127}.; . TISSUE SPECIFICITY: Expressed in all adult tissues examined except for lung and kidney. {ECO:0000269|PubMed:10518011}.; unclassifiable (Anatomical System);tongue;colon;skeletal muscle;breast;prostate;optic nerve;lung;frontal lobe;endometrium;adrenal gland;larynx;thyroid;placenta;liver;head and neck;amniotic fluid;germinal center;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.32242 0.58478 -0.018331246 52.2764803 171.57622 2.85672 LATS2 0.869216004378958 0.130780896571673 3.09904936910725e-06 large tumor suppressor kinase 2 FUNCTION: Negative regulator of YAP1 in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Acts as a tumor suppressor which plays a critical role in centrosome duplication, maintenance of mitotic fidelity and genomic stability. Negatively regulates G1/S transition by down-regulating cyclin E/CDK2 kinase activity. Negative regulator of the androgen receptor. Phosphorylates SNAI1 in the nucleus leading to its nuclear retention and stabilization, which enhances its epithelial-mesenchymal transition and tumor cell invasion/migration activities. This tumor-promoting activity is independent of its effects upon YAP1 or WWTR1/TAZ. {ECO:0000269|PubMed:10871863, ECO:0000269|PubMed:12853976, ECO:0000269|PubMed:15131260, ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:21952048}.; . TISSUE SPECIFICITY: Expressed at high levels in heart and skeletal muscle and at lower levels in all other tissues examined. {ECO:0000269|PubMed:10673337, ECO:0000269|PubMed:10871863}.; . . 0.32558 0.32796 0.363735434 74.71101675 2934.66572 10.27452 LATS2-AS1 . . . LATS2 antisense RNA 1 . . . . . . . . . . . LAX1 4.68312858821734e-07 0.3885378347778 0.611461696909342 lymphocyte transmembrane adaptor 1 FUNCTION: Negatively regulates TCR (T-cell antigen receptor)- mediated signaling in T-cells and BCR (B-cell antigen receptor)- mediated signaling in B-cells. {ECO:0000269|PubMed:12359715}.; . TISSUE SPECIFICITY: Expressed in spleen, thymus, and peripheral blood leukocytes. Expressed in several B-, T-, NK and monocyte cell lines. {ECO:0000269|PubMed:12359715}.; . . 0.10347 0.28192 1.241986644 93.38877094 207.06876 3.11003 LAYN 2.17830732747888e-06 0.470382627751758 0.529615193940915 layilin FUNCTION: Receptor for hyaluronate. {ECO:0000269|PubMed:11294894}.; . . . . 0.09996 0.09587 0.150760231 64.51403633 375.68623 4.08686 LBH 0.300590032052918 0.622552462937228 0.0768575050098534 limb bud and heart development FUNCTION: Transcriptional activator which may act in mitogen- activated protein kinase signaling pathway. {ECO:0000269|PubMed:17390236}.; . TISSUE SPECIFICITY: Highly expressed in heart, and expressed at low levels in placenta, lung, skeletal muscle, kidney and liver. {ECO:0000269|PubMed:17390236}.; . . 0.14420 . -0.007201372 53.19061099 187.45852 2.97403 LBHD1 . . . LBH domain containing 1 . . TISSUE SPECIFICITY: Expressed in bladder cancer tissues (at protein level). {ECO:0000269|PubMed:18828023}.; . . 0.06000 . 0.593509966 82.51356452 . . LBP 5.69197086647934e-14 0.0145250774474396 0.985474922552504 lipopolysaccharide binding protein FUNCTION: Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria (PubMed:7517398, PubMed:24120359). Acts as an affinity enhancer for CD14, facilitating its association with LPS. Promotes the release of cytokines in response to bacterial lipopolysaccharide (PubMed:7517398, PubMed:24120359). {ECO:0000269|PubMed:1698311, ECO:0000269|PubMed:20133493, ECO:0000269|PubMed:24120359, ECO:0000269|PubMed:7517398, ECO:0000305|PubMed:17481951}.; . TISSUE SPECIFICITY: Detected in blood serum (at protein level). {ECO:0000269|PubMed:2402637, ECO:0000269|PubMed:24120359}.; unclassifiable (Anatomical System);pancreas;liver;colon;spleen;kidney;skeletal muscle;gall bladder;stomach; fetal liver;superior cervical ganglion;testis - interstitial;liver;fetal lung;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.33578 0.18667 3.180902589 99.321774 2710.58988 9.79994 LBR 0.997025227192741 0.00297477155612145 1.25113737390106e-09 lamin B receptor FUNCTION: Anchors the lamina and the heterochromatin to the inner nuclear membrane. {ECO:0000269|PubMed:10828963}.; DISEASE: Pelger-Huet anomaly (PHA) [MIM:169400]: An autosomal dominant inherited abnormality of granulocytes, characterized by abnormal ovoid shape, reduced nuclear segmentation and an apparently looser chromatin structure. Some individuals occasionally have skeletal anomalies, developmental delay, and seizures. {ECO:0000269|PubMed:14617022}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Greenberg dysplasia (GRBGD) [MIM:215140]: A rare autosomal recessive chondrodystrophy characterized by early in utero lethality. Affected fetuses typically present with fetal hydrops, short-limbed dwarfism, and a marked disorganization of chondro-osseous calcification, and ectopic ossification centers. {ECO:0000269|PubMed:12618959}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Reynolds syndrome (REYNS) [MIM:613471]: A syndrome specifically associating limited cutaneous systemic sclerosis and primary biliary cirrhosis. It is characterized by liver disease, telangiectasia, abrupt onset of digital paleness or cyanosis in response to cold exposure or stress (Raynaud phenomenon), and variable features of scleroderma. The liver disease is characterized by pruritis, jaundice, hepatomegaly, increased serum alkaline phosphatase and positive serum mitochondrial autoantibodies, all consistent with primary biliary cirrhosis. {ECO:0000269|PubMed:20522425}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . lymphoreticular;smooth muscle;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;oral cavity;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; uterus;fetal liver;tumor;white blood cells;whole blood;thymus;bone marrow; 0.62297 0.29079 -0.707227564 14.71455532 157.9434 2.74500 LBX1 0.805820728845252 0.189117792903776 0.00506147825097197 ladybird homeobox 1 FUNCTION: Transcription factor required for the development of GABAergic interneurons in the dorsal horn of the spinal cord and migration and further development of hypaxial muscle precursor cells for limb muscles, diaphragm and hypoglossal cord. {ECO:0000250}.; . . . . 0.43455 0.26811 -0.295622497 32.61972163 14.04317 0.50950 LBX1-AS1 . . . LBX1 antisense RNA 1 (head to head) . . . . . . . . . . . LBX2 0.617324061969185 0.374733611118246 0.00794232691256902 ladybird homeobox 2 FUNCTION: Putative transcription factor. {ECO:0000250}.; . . uterus;bile duct;lymphoreticular;pancreas;lung;liver;brain;skin; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.08723 0.09503 0.082802743 60.09082331 2039.92144 8.32385 LBX2-AS1 . . . LBX2 antisense RNA 1 . . . . . . . . . . . LCA5 0.00428217416197877 0.994223193496687 0.00149463234133401 Leber congenital amaurosis 5 FUNCTION: Might be involved in minus end-directed microtubule transport.; DISEASE: Leber congenital amaurosis 5 (LCA5) [MIM:604537]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:17546029, ECO:0000269|PubMed:18000884, ECO:0000269|PubMed:18334959}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.16670 0.11088 -0.130380821 44.03161123 3626.18224 11.68454 LCA5L 1.90936191141484e-06 0.681046313248006 0.318951777390082 Leber congenital amaurosis 5-like . . . unclassifiable (Anatomical System);lung;placenta;testis;colon;kidney;stomach;retina; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;skin; 0.10860 . 1.023320772 91.04741684 867.83142 5.73737 LCAL1 . . . lung cancer associated lncRNA 1 . . . . . . . . . . . LCAT 0.496435716280553 0.499146401462736 0.00441788225671109 lecithin-cholesterol acyltransferase FUNCTION: Central enzyme in the extracellular metabolism of plasma lipoproteins. Synthesized mainly in the liver and secreted into plasma where it converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines on the surface of high and low density lipoproteins (HDLs and LDLs) (PubMed:10329423, PubMed:19065001, PubMed:26195816). The cholesterol ester is then transported back to the liver. Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines (PubMed:8820107). Also produced in the brain by primary astrocytes, and esterifies free cholesterol on nascent APOE- containing lipoproteins secreted from glia and influences cerebral spinal fluid (CSF) APOE- and APOA1 levels. Together with APOE and the cholesterol transporter ABCA1, plays a key role in the maturation of glial-derived, nascent lipoproteins. Required for remodeling high-density lipoprotein particles into their spherical forms (PubMed:10722751). {ECO:0000269|PubMed:10329423, ECO:0000269|PubMed:10722751, ECO:0000269|PubMed:14636062, ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:26195816, ECO:0000269|PubMed:8820107}.; DISEASE: Lecithin-cholesterol acyltransferase deficiency (LCATD) [MIM:245900]: A disorder of lipoprotein metabolism characterized by inadequate esterification of plasmatic cholesterol. Two clinical forms are recognized: complete LCAT deficiency and fish- eye disease. LCATD is generally referred to the complete form which is associated with absence of both alpha and beta LCAT activities resulting in esterification anomalies involving both HDL (alpha-LCAT activity) and LDL (beta-LCAT activity). It causes a typical triad of diffuse corneal opacities, target cell hemolytic anemia, and proteinuria with renal failure. {ECO:0000269|PubMed:11423760, ECO:0000269|PubMed:12957688, ECO:0000269|PubMed:15994445, ECO:0000269|PubMed:16051254, ECO:0000269|PubMed:16216249, ECO:0000269|PubMed:1681161, ECO:0000269|PubMed:1859405, ECO:0000269|PubMed:2370048, ECO:0000269|PubMed:7607641, ECO:0000269|PubMed:7711728, ECO:0000269|PubMed:8318557, ECO:0000269|PubMed:8432868, ECO:0000269|PubMed:8807342, ECO:0000269|PubMed:9007616, ECO:0000269|PubMed:9741700}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Fish-eye disease (FED) [MIM:136120]: A disorder of lipoprotein metabolism due to partial lecithin-cholesterol acyltransferase deficiency that affects only alpha-LCAT activity. FED is characterized by low plasma HDL and corneal opacities due to accumulation of cholesterol deposits in the cornea ('fish- eye'). {ECO:0000269|PubMed:1516702, ECO:0000269|PubMed:1571050, ECO:0000269|PubMed:15994445, ECO:0000269|PubMed:1737840, ECO:0000269|PubMed:21901787, ECO:0000269|PubMed:8620346, ECO:0000269|PubMed:9261271}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in blood plasma (PubMed:3458198, PubMed:8820107, PubMed:10222237). Detected in cerebral spinal fluid (at protein level) (PubMed:10222237). Detected in liver (PubMed:3797244, PubMed:3458198). Expressed mainly in brain, liver and testes. {ECO:0000269|PubMed:10222237, ECO:0000269|PubMed:3458198, ECO:0000269|PubMed:3797244, ECO:0000269|PubMed:8820107}.; ovary;colon;parathyroid;retina;uterus;prostate;whole body;endometrium;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;urinary;blood;lung;epididymis;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;mammary gland;stomach; fetal liver;superior cervical ganglion;liver;atrioventricular node;trigeminal ganglion;cerebellum; 0.12548 0.10955 -0.293801652 32.93819297 70.43658 1.74650 LCE1A 0.000409833656946099 0.234194561743381 0.765395604599673 late cornified envelope 1A FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . . . . 0.25431 . 0.03689118 56.64071715 25.22558 0.82480 LCE1B 0.0272674911272321 0.573384318634822 0.399348190237946 late cornified envelope 1B FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . TISSUE SPECIFICITY: Skin-specific. Expression was readily detected in adult trunk skin, adult arm skin, fetal skin, penal skin, vulva, esophagus and tongue. Not expressed in the cervix, rectum, lung, colon, or placenta. {ECO:0000269|PubMed:15854049}.; skin; . 0.07880 0.11017 0.591694063 82.45458835 190.98116 2.99744 LCE1C 0.0275164497301328 0.575224499331083 0.397259050938784 late cornified envelope 1C FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . . . . 0.05152 . 0.481458261 79.03986789 2222.87795 8.68571 LCE1D 0.00356754650118208 0.394337783918924 0.602094669579894 late cornified envelope 1D FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . . skin; . 0.13561 . 1.769400948 96.7740033 836.5874 5.66557 LCE1E 0.000399700058911427 0.231142231856685 0.768458068084404 late cornified envelope 1E FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . . . . 0.17184 . 1.238355121 93.31799953 1775.75049 7.78240 LCE1F 0.0294987722043082 0.589260865789988 0.381240362005704 late cornified envelope 1F FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . . skin; . 0.15826 . 0.325313577 73.11276244 1480.78795 7.16483 LCE2A 0.00619380141821062 0.502259241626944 0.491546956954846 late cornified envelope 2A FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . TISSUE SPECIFICITY: Skin-specific. Expression was readily detected in adult trunk skin, adult arm skin, fetal skin, penal skin, vulva, esophagus and tongue. Not expressed in the cervix, rectum, lung, colon, or placenta. {ECO:0000269|PubMed:15854049}.; . . 0.06337 0.09136 0.459411326 78.28497287 466.9305 4.47656 LCE2B 0.137251509220331 0.624272789829283 0.238475700950386 late cornified envelope 2B FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . . . . 0.10138 0.09125 0.948089677 89.95635763 1614.95917 7.43673 LCE2C 0.0226062040752681 0.535288863993912 0.44210493193082 late cornified envelope 2C FUNCTION: Precursors of the cornified envelope of the stratum.; . . . . 0.16618 . -0.029247611 51.40363293 146.92821 2.64056 LCE2D 0.139231288431163 0.625775007073132 0.234993704495705 late cornified envelope 2D FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . TISSUE SPECIFICITY: Skin-specific. Expression was readily detected in adult trunk skin, adult arm skin, fetal skin, penal skin, vulva, esophagus and tongue. Not expressed in the cervix, rectum, lung, colon, or placenta. {ECO:0000269|PubMed:15854049}.; . . 0.16109 . 0.769889969 86.95447039 46.70069 1.31998 LCE3A 0.496361201281267 0.429005501352037 0.0746332973666955 late cornified envelope 3A FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . . . . 0.09624 0.10180 0.257356108 69.83368719 40.88771 1.19773 LCE3B 0.039623989044318 0.646995989968824 0.313380020986858 late cornified envelope 3B FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . . . . 0.04897 0.06458 0.435547893 77.45340882 41.53382 1.21151 LCE3C 0.496169124945965 0.429111247024314 0.0747196280297208 late cornified envelope 3C FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . TISSUE SPECIFICITY: Skin-specific. Expression was readily detected in adult trunk skin, adult arm skin, fetal skin, penal skin, vulva, esophagus and tongue. Not expressed in the cervix, rectum, lung, colon, or placenta. {ECO:0000269|PubMed:15854049}.; bladder; . 0.06967 0.08197 0.635788962 83.63411182 171.36922 2.85501 LCE3D 7.91048601058223e-05 0.176358972819116 0.823561922320778 late cornified envelope 3D FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . . . . 0.05889 0.10635 0.104848986 61.49445624 378.65682 4.10225 LCE3E 0.0390009274705493 0.644004466395133 0.316994606134318 late cornified envelope 3E FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . TISSUE SPECIFICITY: Skin-specific. Expression was readily detected in adult trunk skin, adult arm skin, fetal skin, penal skin, vulva, esophagus and tongue. Not expressed in the cervix, rectum, lung, colon, or placenta. {ECO:0000269|PubMed:15854049}.; . . 0.05189 . -0.185391282 39.67916962 44.60336 1.28074 LCE4A 0.00328018180284451 0.379208073831541 0.617511744365614 late cornified envelope 4A FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . TISSUE SPECIFICITY: Skin-specific. Expression was readily detected in adult trunk skin, adult arm skin, fetal skin, penal skin, vulva, esophagus and tongue. Not expressed in the cervix, rectum, lung, colon, or placenta. {ECO:0000269|PubMed:15854049}.; unclassifiable (Anatomical System); . 0.09079 . 0.701931997 85.34442085 359.33814 4.01351 LCE5A 0.0767260194114967 0.74960163716502 0.173672343423483 late cornified envelope 5A FUNCTION: Precursors of the cornified envelope of the stratum corneum.; . . unclassifiable (Anatomical System); . 0.12966 . 0.880130671 88.9596603 55.8248 1.50031 LCE6A . . . late cornified envelope 6A FUNCTION: Precursors of the cornified envelope of the stratum corneum. {ECO:0000250}.; . . . . . . 0.057118534 57.99716914 102.12102 2.18487 LCEP1 . . . late cornified envelope pseudogene 1 . . . . . . . . . . . LCEP2 . . . late cornified envelope pseudogene 2 . . . . . . . . . . . LCEP3 . . . late cornified envelope pseudogene 3 . . . . . . . . . . . LCEP4 . . . late cornified envelope pseudogene 4 . . . . . . . . . . . LCK 0.999425040716645 0.000574956536777237 2.74657822291757e-09 LCK proto-oncogene, Src family tyrosine kinase FUNCTION: Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T- cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosines residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP70, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2, the microtubule-associated protein MAPT, RHOH or TYROBP. {ECO:0000269|PubMed:16339550, ECO:0000269|PubMed:16709819, ECO:0000269|PubMed:20028775, ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:20851766, ECO:0000269|PubMed:21269457, ECO:0000269|PubMed:22080863}.; DISEASE: Note=A chromosomal aberration involving LCK is found in leukemias. Translocation t(1;7)(p34;q34) with TCRB.; DISEASE: Immunodeficiency 22 (IMD22) [MIM:615758]: A primary immunodeficiency characterized by T-cell dysfunction. Affected individuals present with lymphopenia, recurrent infections, severe diarrhea, and failure to thrive. {ECO:0000269|PubMed:22985903}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed specifically in lymphoid cells.; unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;colon;blood;bone marrow;uterus;prostate;pancreas;lung;oesophagus;epididymis;larynx;liver;testis;head and neck;spleen;germinal center;brain;mammary gland;stomach;aorta;tonsil;thymus; lymph node;whole blood;thymus; 0.98770 . 0.439181676 77.69521113 239.70726 3.34580 LCLAT1 0.000175609752118781 0.888367979375592 0.11145641087229 lysocardiolipin acyltransferase 1 FUNCTION: Acyl-CoA:lysocardiolipin acyltransferase. Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities. Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors. Acts as a remodeling enzyme for cardiolipin, a major membrane polyglycerophospholipid. Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) with a relatively low activity. Required for establishment of the hematopoietic and endothelial lineages. {ECO:0000269|PubMed:16620771, ECO:0000269|PubMed:19075029}.; . TISSUE SPECIFICITY: Expressed at higher level in heart, kidney and pancreas than in brain, spleen, liver, lung, small intestine and placenta. {ECO:0000269|PubMed:16620771, ECO:0000269|PubMed:19075029}.; myocardium;ovary;parathyroid;skin;bone marrow;uterus;prostate;cochlea;endometrium;bone;testis;germinal center;brain;artery;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;mammary gland;aorta; dorsal root ganglion;pancreas;superior cervical ganglion;ciliary ganglion;atrioventricular node;skin;skeletal muscle; 0.29451 0.13582 -0.113792788 45.25831564 110.85613 2.29457 LCMT1 0.00155058401962153 0.968642834674275 0.0298065813061031 leucine carboxyl methyltransferase 1 FUNCTION: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues. {ECO:0000269|PubMed:10600115}.; . . . . 0.02237 0.10183 -0.494039303 22.09247464 21.02882 0.71243 LCMT1-AS1 . . . LCMT1 antisense RNA 1 . . . . . . . . . . . LCMT1-AS2 . . . LCMT1 antisense RNA 2 . . . . . . . . . . . LCMT2 7.26615001081782e-08 0.268667512827262 0.731332414511238 leucine carboxyl methyltransferase 2 FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA (By similarity). May methylate the carboxyl group of leucine residues to form alpha- leucine ester residues. {ECO:0000250}.; . . unclassifiable (Anatomical System);smooth muscle;tongue;colon;blood;fovea centralis;choroid;lens;skin;retina;uterus;breast;optic nerve;lung;endometrium;thyroid;placenta;macula lutea;testis;head and neck;germinal center;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;caudate nucleus;trigeminal ganglion;skeletal muscle;skin; 0.07788 0.11769 -0.042196577 50.49539986 231.36801 3.28766 LCN1 1.90926015198603e-07 0.0731386976286887 0.926861111445296 lipocalin 1 FUNCTION: Could play a role in taste reception. Could be necessary for the concentration and delivery of sapid molecules in the gustatory system. Can bind various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampicin and even to microbial siderophores. Exhibits an extremely wide ligand pocket.; . TISSUE SPECIFICITY: Mainly expressed in lachrymal and salivary glands. Also expressed in the prostate.; unclassifiable (Anatomical System);lacrimal gland;adrenal gland;thyroid;adrenal cortex;parathyroid;pineal gland; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.02759 0.12458 0.218717575 68.27081859 16.88068 0.59447 LCN1P1 . . . lipocalin 1 pseudogene 1 FUNCTION: May bind a variety of ligands including lipids. {ECO:0000250}.; . . . . 0.08318 . . . . . LCN1P2 . . . lipocalin 1 pseudogene 2 . . . . . . . . . . . LCN2 0.000596069473927577 0.718566244193382 0.28083768633269 lipocalin 2 FUNCTION: Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development. Binds iron through association with 2,5-dihydroxybenzoic acid (2,5- DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association of the iron-free form (apo-24p3) with the SLC22A17 (24p3R) receptor is followed by association with an intracellular siderophore, iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration. Involved in apoptosis due to interleukin-3 (IL3) deprivation: iron-loaded form increases intracellular iron concentration without promoting apoptosis, while iron-free form decreases intracellular iron levels, inducing expression of the proapoptotic protein BCL2L11/BIM, resulting in apoptosis. Involved in innate immunity, possibly by sequestrating iron, leading to limit bacterial growth. {ECO:0000269|PubMed:12453413}.; . TISSUE SPECIFICITY: Expressed in bone marrow and in tissues that are prone to exposure to microorganism. High expression is found in bone marrow as well as in uterus, prostate, salivary gland, stomach, appendix, colon, trachea and lung. Not found in the small intestine or peripheral blood leukocytes. {ECO:0000269|PubMed:9339356}.; ovary;umbilical cord;colon;skin;bone marrow;uterus;prostate;whole body;oesophagus;bone;thyroid;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;pharynx;blood;breast;pancreas;lung;nasopharynx;visual apparatus;hypopharynx;liver;head and neck;cervix;kidney;stomach; trachea;tongue;salivary gland;beta cell islets;fetal lung;bone marrow; 0.30951 0.64738 0.837848571 88.22835574 46.71083 1.32028 LCN6 2.55253161126526e-05 0.312217510114771 0.687756964569117 lipocalin 6 FUNCTION: May play a role in male fertility.; . TISSUE SPECIFICITY: Predominantly expressed in epididymis.; unclassifiable (Anatomical System);prostate;lung;epididymis;testis; testis;globus pallidus;ciliary ganglion;atrioventricular node; 0.06295 0.07966 0.505321956 80.00707714 126.96156 2.45728 LCN8 0.042675811681238 0.84735211114697 0.109972077171792 lipocalin 8 FUNCTION: May play a role in male fertility. May act as a retinoid carrier protein within the epididymis.; . . . . 0.03683 . 0.373041938 75.29488087 1010.88949 6.12169 LCN9 0.0148717290734386 0.8756212944252 0.109506976501361 lipocalin 9 . . . unclassifiable (Anatomical System); . 0.05739 0.09146 0.260991686 70.25831564 43.30235 1.25013 LCN10 0.00212801263084344 0.750038109477071 0.247833877892086 lipocalin 10 FUNCTION: May play a role in male fertility. May act as a retinoid carrier protein within the epididymis.; . . prostate;lung;ovary;endometrium;islets of Langerhans;epididymis;testis;colon;blood;kidney;gall bladder; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.09338 0.08687 0.505321956 80.00707714 582.25005 4.89235 LCN12 0.00153203676033422 0.682638242648607 0.315829720591059 lipocalin 12 FUNCTION: Binds all-trans retinoic acid and may act as a retinoid carrier protein within the epididymis. May play a role in male fertility (By similarity). {ECO:0000250}.; . . . . 0.06173 0.08318 0.439181676 77.69521113 54.20358 1.46937 LCN15 0.0068805976606108 0.759177255896618 0.233942146442771 lipocalin 15 . . . colon; . . . 0.483275131 79.25218212 24.85409 0.81568 LCNL1 0.00301595115191131 0.587502001110178 0.409482047737911 lipocalin-like 1 . . . . . . . 0.749657564 86.56522765 1398.64602 6.99481 LCOR 0.913200262247645 0.0866718078998549 0.000127929852499805 ligand dependent nuclear receptor corepressor FUNCTION: May act as transcription activator that binds DNA elements with the sequence 5'-CCCTATCGATCGATCTCTACCT-3' (By similarity). Repressor of ligand-dependent transcription activation by target nuclear receptors. Repressor of ligand- dependent transcription activation by ESR1, ESR2, NR3C1, PGR, RARA, RARB, RARG, RXRA and VDR. {ECO:0000250, ECO:0000269|PubMed:12535528}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12535528}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;islets of Langerhans;parathyroid;blood;retina;bone marrow;whole body;lung;adrenal gland;placenta;amnion;liver;testis;spleen;germinal center;brain;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.12408 0.08828 -0.005381972 53.50908233 43.02025 1.24391 LCORL 0.963114570470951 0.0368126752378267 7.27542912222256e-05 ligand dependent nuclear receptor corepressor like FUNCTION: May act as transcription activator that binds DNA elements with the sequence 5'-CCCTATCGATCGATCTCTACCT-3'. May play a role in spermatogenesis (By similarity). {ECO:0000250}.; . . ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;bone marrow;prostate;whole body;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);heart;tongue;pharynx;blood;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach; . 0.32111 . 0.371224249 75.12384996 232.92599 3.29998 LCP1 0.973076021263703 0.0269237015460021 2.77190294676437e-07 lymphocyte cytosolic protein 1 (L-plastin) FUNCTION: Actin-binding protein. Plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. Modulates the cell surface expression of IL2RA/CD25 and CD69. {ECO:0000269|PubMed:16636079, ECO:0000269|PubMed:17294403}.; DISEASE: Note=Chromosomal aberrations involving LCP1 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;13)(q27;q14), with BCL6. {ECO:0000269|PubMed:10469447}.; TISSUE SPECIFICITY: Detected in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia, in spleen and other lymph node-containing organs. Expressed in peripheral blood T- lymphocytes, neutrophils, monocytes, B-lymphocytes, and myeloid cells. {ECO:0000269|PubMed:3261603}.; lymphoreticular;umbilical cord;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;endometrium;oesophagus;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;bile duct;pancreas;lung;nasopharynx;placenta;liver;cervix;spleen;kidney;mammary gland;aorta;stomach;thymus; tumor;white blood cells;whole blood;tonsil;bone marrow;thymus; 0.64125 0.28792 0.108486928 61.90728946 86.54228 1.98639 LCP2 0.988900379914002 0.0110995888004278 3.1285570001601e-08 lymphocyte cytosolic protein 2 FUNCTION: Involved in T-cell antigen receptor mediated signaling.; . TISSUE SPECIFICITY: Highly expressed in spleen, thymus and peripheral blood leukocytes. Highly expressed also in T-cell and monocytic cell lines, expressed at lower level in B-cell lines. Not detected in fibroblast or neuroblastoma cell lines.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;heart;tongue;islets of Langerhans;hypothalamus;sympathetic chain;colon;parathyroid;blood;skin;bone marrow;uterus;prostate;pancreas;lung;nasopharynx;bone;placenta;liver;testis;head and neck;spleen;brain;gall bladder;aorta;thymus; superior cervical ganglion;white blood cells;whole blood;bone marrow;thymus; 0.26740 0.28725 -0.488577883 22.64685067 48.09107 1.34987 LCS1 . . . lymphedema-cholestasis syndrome 1 . . . . . . . . . . . LCT 0.0642550168201587 0.935744974226583 8.9532581372765e-09 lactase FUNCTION: LPH splits lactose in the small intestine.; DISEASE: Congenital lactase deficiency (COLACD) [MIM:223000]: Autosomal recessive, rare and severe gastrointestinal disorder. It is characterized by watery diarrhea in infants fed with breast milk or other lactose-containing formulas. An almost total lack of LCT activity is found in jejunal biopsy material of patients with congenital lactase deficiency. Opposite to congenital lactase deficiency, also known as lactose intolerance, is the most common enzyme deficiency worldwide. It is caused by developmental down- regulation of lactase activity during childhood or early adulthood. The decline of lactase activity is a normal physiological phenomenon; however, the majority of Northern Europeans have the ability to maintain lactase activity and digest lactose throughout life (lactase persistence). The down-regulation of lactase activity operates at the transcriptional level and it is associated with a noncoding variation in the MCM6 gene, located in the upstream vicinity of LCT. {ECO:0000269|PubMed:16400612}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Intestine.; unclassifiable (Anatomical System);lung;ovary;small intestine;placenta;testis;colon;parathyroid;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.10638 0.66554 -1.335817967 4.659117716 3628.57927 11.68781 LCTL 4.65245462491966e-08 0.823884859821086 0.176115093654368 lactase like . . . unclassifiable (Anatomical System);lung;adrenal gland;sympathetic chain;testis;colon;germinal center;vein;skin;stomach; superior cervical ganglion;olfactory bulb; 0.07484 0.13952 0.091899012 60.68058504 612.43709 5.00055 LDAH . . . lipid droplet associated hydrolase FUNCTION: Serine lipid hydrolase associated with lipid droplets. Highly expressed in macrophage-rich areas in atherosclerotic lesions, suggesting that it could promote cholesterol ester turnover in macrophages. {ECO:0000250|UniProtKB:Q8BVA5}.; . TISSUE SPECIFICITY: Present in macrophage-rich areas in atherosclerotic lesionsv(at protein level). {ECO:0000269|PubMed:24357060}.; . . 0.14386 . 0.861712133 88.6883699 . . LDB1 0.879454004833888 0.120485041287937 6.09538781754649e-05 LIM domain binding 1 FUNCTION: Binds to the LIM domain of a wide variety of LIM domain- containing transcription factors. May regulate the transcriptional activity of LIM-containing proteins by determining specific partner interactions. Plays a role in the development of interneurons and motor neurons in cooperation with LHX3 and ISL1. Acts synergistically with LHX1/LIM1 in axis formation and activation of gene expression. Acts with LMO2 in the regulation of red blood cell development, maintaining erythroid precursors in an immature state (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in a wide range of adult tissues including brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, lung and peripheral blood leukocytes. {ECO:0000269|PubMed:16815859}.; ovary;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;bile duct;breast;pancreas;lung;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; trigeminal ganglion;skeletal muscle; 0.86189 0.18619 -0.427900189 25.14744043 24.34364 0.79990 LDB2 0.97606785748877 0.0239270859282235 5.05658300613341e-06 LIM domain binding 2 FUNCTION: Binds to the LIM domain of a wide variety of LIM domain- containing transcription factors.; . . ovary;colon;parathyroid;skin;retina;uterus;whole body;frontal lobe;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;skeletal muscle;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.92781 0.11262 -0.471992905 23.03609342 9.47814 0.34943 LDB3 0.000214849555827575 0.995279650419609 0.00450550002456353 LIM domain binding 3 FUNCTION: May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton. {ECO:0000305}.; DISEASE: Left ventricular non-compaction 3 (LVNC3) [MIM:601493]: A disease due to an arrest of myocardial morphogenesis. It is characterized by a hypertrophic left ventricle with deep trabeculations and with poor systolic function, with or without associated left ventricular dilation. In some cases, it is associated with other congenital heart anomalies. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myopathy, myofibrillar, 4 (MFM4) [MIM:609452]: A neuromuscular disorder characterized by distal and proximal muscle weakness with signs of cardiomyopathy and neuropathy. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed primarily in skeletal muscle and to a lesser extent in heart. Also detected in brain and placenta. {ECO:0000269|PubMed:10427098}.; myocardium;sympathetic chain;parathyroid;skin;retina;uterus;prostate;atrium;whole body;frontal lobe;larynx;testis;artery;unclassifiable (Anatomical System);heart;hypothalamus;muscle;skeletal muscle;lung;adrenal gland;placenta;liver;head and neck;kidney;mammary gland;aorta; superior cervical ganglion;heart;tongue;ciliary ganglion;parietal lobe;skeletal muscle; 0.86741 0.32372 -0.900215512 10.16159472 751.34596 5.43680 LDHA 0.058657590294526 0.923941779282667 0.0174006304228071 lactate dehydrogenase A . DISEASE: Glycogen storage disease 11 (GSD11) [MIM:612933]: A metabolic disorder that results in exertional myoglobinuria, pain, cramps and easy fatigue. {ECO:0000269|PubMed:2334430}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;skin;prostate;bone;thyroid;testis;brain;bladder;pineal gland;unclassifiable (Anatomical System);lymph node;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;bile duct;breast;lung;adrenal gland;nasopharynx;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;stomach; adipose tissue;smooth muscle;ciliary ganglion; 0.43011 0.85387 -0.404032746 26.53338051 41.17522 1.20476 LDHAL6A 0.000200256316758105 0.723311358660448 0.276488385022794 lactate dehydrogenase A-like 6A FUNCTION: Displays an lactate dehydrogenase activity. Significantly increases the transcriptional activity of JUN, when overexpressed. {ECO:0000269|PubMed:18351441}.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:18351441}.; unclassifiable (Anatomical System);cartilage; . 0.08540 0.48270 -0.22584292 37.32012267 84.99755 1.96469 LDHAL6B 7.95326404010906e-07 0.0874529277915057 0.91254627688209 lactate dehydrogenase A-like 6B . . TISSUE SPECIFICITY: Testis specific.; unclassifiable (Anatomical System);medulla oblongata;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07610 0.41942 0.777157784 87.17857985 6583.95968 17.12685 LDHAL6CP . . . lactate dehydrogenase A-like 6C, pseudogene . . . . . . . . . . . LDHAL6DP . . . lactate dehydrogenase A-like 6D, pseudogene . . . . . . . . . . . LDHAL6EP . . . lactate dehydrogenase A-like 6E, pseudogene . . . . . . . . . . . LDHAL6FP . . . lactate dehydrogenase A-like 6F, pseudogene . . . . . . . . . . . LDHAP1 . . . lactate dehydrogenase A pseudogene 1 . . . . . . . . . . . LDHAP2 . . . lactate dehydrogenase A pseudogene 2 . . . . . . . . . . . LDHAP3 . . . lactate dehydrogenase A pseudogene 3 . . . . . . . . . . . LDHAP4 . . . lactate dehydrogenase A pseudogene 4 . . . . . . . . . . . LDHAP5 . . . lactate dehydrogenase A pseudogene 5 . . . . . . . . . . . LDHAP7 . . . lactate dehydrogenase A pseudogene 7 . . . . . . . . . . . LDHB 2.02750017037306e-05 0.471445046914224 0.528534678084072 lactate dehydrogenase B . DISEASE: Lactate dehydrogenase B deficiency (LDHBD) [MIM:614128]: A condition with no deleterious effects on health. LDHBD is of interest to laboratory medicine mainly because it can cause misdiagnosis in those disorders in which elevation of serum LDH is expected. {ECO:0000269|PubMed:10211631, ECO:0000269|PubMed:11509017, ECO:0000269|PubMed:1587525, ECO:0000269|PubMed:2334429, ECO:0000269|PubMed:8314553, ECO:0000269|PubMed:8462975, ECO:0000269|PubMed:8611651, ECO:0000269|PubMed:9929983, ECO:0000269|Ref.19}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;cochlea;endometrium;bladder;brain;tonsil;heart;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;placenta;head and neck;kidney;stomach;aorta;thymus; amygdala;thalamus;occipital lobe;medulla oblongata;hypothalamus;temporal lobe;spinal cord;tumor;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;kidney;parietal lobe;cingulate cortex; 0.54909 0.85056 -0.249709319 35.74545883 57.25382 1.52454 LDHBP1 . . . lactate dehydrogenase B pseudogene 1 . . . . . . . . . . . LDHBP2 . . . lactate dehydrogenase B pseudogene 2 . . . . . . . . . . . LDHBP3 . . . lactate dehydrogenase B pseudogene 3 . . . . . . . . . . . LDHC 0.000944178486057736 0.806721940982815 0.192333880531127 lactate dehydrogenase C FUNCTION: Possible role in sperm motility.; . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; testis - interstitial;testis - seminiferous tubule;appendix;testis;skeletal muscle; 0.06358 0.53640 0.41713504 76.95800896 185.56342 2.95821 LDHD 4.48718498001763e-06 0.84282486427637 0.15717064853865 lactate dehydrogenase D . . TISSUE SPECIFICITY: Expressed moderately in heart and liver and at lower levels in skeletal muscle and kidney. {ECO:0000269|PubMed:12127981}.; myocardium;cartilage;colon;fovea centralis;choroid;lens;retina;pancreas;optic nerve;lung;endometrium;placenta;macula lutea;liver;testis;spleen;kidney;brain;stomach; . 0.05979 0.18987 -0.44448505 24.46331682 162.36964 2.78319 LDLR 2.59266073718312e-16 0.0585944567653505 0.941405543234649 low density lipoprotein receptor FUNCTION: Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits.; DISEASE: Familial hypercholesterolemia (FH) [MIM:143890]: Common autosomal semi-dominant disease that affects about 1 in 500 individuals. The receptor defect impairs the catabolism of LDL, and the resultant elevation in plasma LDL-cholesterol promotes deposition of cholesterol in the skin (xanthelasma), tendons (xanthomas), and coronary arteries (atherosclerosis). {ECO:0000269|PubMed:10090484, ECO:0000269|PubMed:10206683, ECO:0000269|PubMed:10422803, ECO:0000269|PubMed:10447263, ECO:0000269|PubMed:10532689, ECO:0000269|PubMed:10660340, ECO:0000269|PubMed:10882754, ECO:0000269|PubMed:10978268, ECO:0000269|PubMed:10980548, ECO:0000269|PubMed:11298688, ECO:0000269|PubMed:11462246, ECO:0000269|PubMed:1446662, ECO:0000269|PubMed:1464748, ECO:0000269|PubMed:17142622, ECO:0000269|PubMed:17347910, ECO:0000269|PubMed:1867200, ECO:0000269|PubMed:19318025, ECO:0000269|PubMed:19319977, ECO:0000269|PubMed:22160468, ECO:0000269|PubMed:2318961, ECO:0000269|PubMed:24529145, ECO:0000269|PubMed:2569482, ECO:0000269|PubMed:2726768, ECO:0000269|PubMed:3263645, ECO:0000269|PubMed:3955657, ECO:0000269|PubMed:7550239, ECO:0000269|PubMed:7573037, ECO:0000269|PubMed:7583548, ECO:0000269|PubMed:7635461, ECO:0000269|PubMed:7635482, ECO:0000269|PubMed:7649546, ECO:0000269|PubMed:7649549, ECO:0000269|PubMed:8168830, ECO:0000269|PubMed:8347689, ECO:0000269|PubMed:8462973, ECO:0000269|PubMed:8664907, ECO:0000269|PubMed:8740918, ECO:0000269|PubMed:9026534, ECO:0000269|PubMed:9104431, ECO:0000269|PubMed:9143924, ECO:0000269|PubMed:9254862, ECO:0000269|PubMed:9259195, ECO:0000269|PubMed:9452094, ECO:0000269|PubMed:9452095, ECO:0000269|PubMed:9452118, ECO:0000269|PubMed:9654205, ECO:0000269|PubMed:9678702, ECO:0000269|PubMed:9852677, ECO:0000269|Ref.70}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;larynx;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;lacrimal gland;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;head and neck;cervix;kidney;stomach; lung;adrenal gland;adrenal cortex;ciliary ganglion;trigeminal ganglion; 0.42568 0.94311 -1.853858183 2.028780373 654.09994 5.13173 LDLRAD1 0.000101665235918743 0.577316980938709 0.422581353825373 low density lipoprotein receptor class A domain containing 1 . . . . . 0.11133 . 0.194852702 67.03231894 138.47283 2.56295 LDLRAD2 0.000195122663626231 0.479290574034651 0.520514303301723 low density lipoprotein receptor class A domain containing 2 . . . myocardium;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;substantia nigra;parathyroid;choroid;skin;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;iris;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; . 0.28027 . 0.014844891 54.94810097 46.83902 1.32299 LDLRAD3 0.0250893103934073 0.917067815032697 0.057842874573896 low density lipoprotein receptor class A domain containing 3 FUNCTION: May influence APP processing, resulting in a decrease in sAPP-alpha production and increased amyloidogenic P3 peptide production. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at high levels in brain, lung, skeletal muscle, and pancreas. Expressed at moderate levels in heart, placenta, and kidney but not detected in the liver. {ECO:0000269|PubMed:21795536}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;urinary;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland; dorsal root ganglion;atrioventricular node; 0.27136 . -0.201976964 38.98325077 478.04412 4.51407 LDLRAD4 0.377306395292768 0.61193310063918 0.0107605040680516 low density lipoprotein receptor class A domain containing 4 FUNCTION: Functions as a negative regulator of TGF-beta signaling and thereby probably plays a role in cell proliferation, differentiation, apoptosis, motility, extracellular matrix production and immunosuppression. In the canonical TGF-beta pathway, ZFYVE9/SARA recruits the intracellular signal transducer and transcriptional modulators SMAD2 and SMAD3 to the TGF-beta receptor. Phosphorylated by the receptor, SMAD2 and SMAD3 then form a heteromeric complex with SMAD4 that translocates to the nucleus to regulate transcription. Through interaction with SMAD2 and SMAD3, LDLRAD4 may compete with ZFYVE9 and SMAD4 and prevent propagation of the intracellular signal. {ECO:0000269|PubMed:24627487}.; . TISSUE SPECIFICITY: Expressed in lymphocytes. {ECO:0000269|PubMed:19461657}.; . . 0.53888 0.09904 -0.115612493 45.12856806 49.8811 1.38578 LDLRAD4-AS1 . . . LDLRAD4 antisense RNA 1 . . . . . . . . . . . LDLRAP1 2.90076895064709e-05 0.546687281071904 0.45328371123859 low density lipoprotein receptor adaptor protein 1 FUNCTION: Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes, but not in non-polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering in coated pits. May facilitate the endocytocis of LDLR and LDLR-LDL complexes from coated pits by stabilizing the interaction between the receptor and the structural components of the pits. May also be involved in the internalization of other LDLR family members. Binds to phosphoinositides, which regulate clathrin bud assembly at the cell surface. {ECO:0000269|PubMed:15728179}.; DISEASE: Hypercholesterolemia, autosomal recessive (ARH) [MIM:603813]: A familial condition characterized by elevated circulating cholesterol contained in either low-density lipoproteins alone or also in very-low-density lipoproteins. {ECO:0000269|PubMed:11326085}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at high levels in the kidney, liver, and placenta, with lower levels detectable in brain, heart, muscle, colon, spleen, intestine, lung, and leukocytes.; . . 0.21674 0.42456 0.373041938 75.29488087 186.26228 2.96392 LDOC1 0.575480326491493 0.379693292390632 0.0448263811178753 leucine zipper, down-regulated in cancer 1 FUNCTION: May have an important role in the development and/or progression of some cancers.; . TISSUE SPECIFICITY: Ubiquitously expressed with high levels in brain ant thyroid and low expression in placenta, liver and leukocytes. Expressed as well in six of the seven human breast cancer cell lines examined. {ECO:0000269|PubMed:10403563}.; . . 0.14859 0.10974 0.12325821 62.38499646 2.49325 0.09201 LDOC1L 0.142833061438218 0.779015537835942 0.07815140072584 leucine zipper, down-regulated in cancer 1-like . . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;lens;breast;pancreas;lung;macula lutea;visual apparatus;hippocampus;liver;alveolus;kidney;mammary gland;parietal lobe;thymus; . 0.15067 0.10415 -0.163345027 41.24793583 6.93848 0.25846 LEAP2 0.00789837798993102 0.553270497295538 0.438831124714531 liver expressed antimicrobial peptide 2 FUNCTION: Has an antimicrobial activity. {ECO:0000269|PubMed:20845358}.; . . lung;endometrium;liver;colon;spleen;kidney;brain; . 0.08491 0.10292 0.169169615 65.33380514 89.55996 2.03579 LECT1 6.68267008491628e-06 0.472043728418096 0.527949588911819 leukocyte cell derived chemotaxin 1 FUNCTION: Bifunctional growth regulator that stimulates the growth of cultured chondrocytes in the presence of basic fibroblast growth factor (FGF) but inhibits the growth of cultured vascular endothelial cells. May contribute to the rapid growth of cartilage and vascular invasion prior to the replacement of cartilage by bone during endochondral bone development. Inhibits in vitro tube formation and mobilization of endothelial cells. Plays a role as antiangiogenic factor in cardiac valves to suppress neovascularization. {ECO:0000269|PubMed:16980969}.; . TISSUE SPECIFICITY: Detected in cartilage and cardiac valves (at protein level). Detected in the laminae fibrosa, spongiosa and ventricularis layers of normal cardiac valves (at protein level). Expression is decreased cardiac valves of patients with valvular heart disease (at protein level). Weakly expressed in chondrosarcoma. {ECO:0000269|PubMed:16980969}.; . . 0.45997 0.15162 -0.203796826 38.81811748 606.48851 4.98233 LECT2 0.00580249401291057 0.726113613100741 0.268083892886348 leukocyte cell derived chemotaxin 2 FUNCTION: Has a neutrophil chemotactic activity. Also a positive regulator of chondrocyte proliferation.; . TISSUE SPECIFICITY: Highly expressed in adult and fetal liver and weakly in testis. Not expressed in bone marrow.; liver;spleen; fetal liver;superior cervical ganglion;testis - seminiferous tubule;liver;testis;ciliary ganglion;atrioventricular node;cingulate cortex; 0.10161 0.13484 0.43736446 77.56546355 136.26053 2.53699 LEF1 0.97013467744067 0.0298565754494101 8.74710991949862e-06 lymphoid enhancer binding factor 1 FUNCTION: Participates in the Wnt signaling pathway. Activates transcription of target genes in the presence of CTNNB1 and EP300. May play a role in hair cell differentiation and follicle morphogenesis. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by LEF1 and CTNNB1. Regulates T-cell receptor alpha enhancer function. Binds DNA in a sequence-specific manner. PIAG antagonizes both Wnt-dependent and Wnt-independent activation by LEF1 (By similarity). Isoform 3 lacks the CTNNB1 interaction domain and may be an antagonist for Wnt signaling. Isoform 5 transcriptionally activates the fibronectin promoter, binds to and represses transcription from the E-cadherin promoter in a CTNNB1- independent manner, and is involved in reducing cellular aggregation and increasing cell migration of pancreatic cancer cells. Isoform 1 transcriptionally activates MYC and CCND1 expression and enhances proliferation of pancreatic tumor cells. {ECO:0000250, ECO:0000269|PubMed:11266540, ECO:0000269|PubMed:19653274, ECO:0000269|PubMed:2010090}.; . TISSUE SPECIFICITY: Detected in thymus. Not detected in normal colon, but highly expressed in colon cancer biopsies and colon cancer cell lines. Expressed in several pancreatic tumors and weakly expressed in normal pancreatic tissue. Isoforms 1 and 5 are detected in several pancreatic cell lines. {ECO:0000269|PubMed:19653274}.; lymphoreticular;colon;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;blood;pancreas;lung;nasopharynx;head and neck;kidney;aorta;thymus; dorsal root ganglion;subthalamic nucleus;trigeminal ganglion;parietal lobe;skeletal muscle;thymus; 0.92691 0.83191 0.196671391 67.19155461 108.65686 2.26268 LEF1-AS1 . . . LEF1 antisense RNA 1 . . . . . . . . . . . LEFTY1 6.88020467750251e-05 0.493860304148411 0.506070893804814 left-right determination factor 1 FUNCTION: Required for left-right axis determination as a regulator of LEFTY2 and NODAL.; . . unclassifiable (Anatomical System);uterus;pancreas;ovary;endometrium;islets of Langerhans;colon;spleen;brain; . 0.52028 0.47239 1.416569784 94.85727766 2866.3756 10.13486 LEFTY2 0.122897476061549 0.852650621270417 0.0244519026680338 left-right determination factor 2 FUNCTION: Required for left-right (L-R) asymmetry determination of organ systems in mammals. May play a role in endometrial bleeding.; DISEASE: Left-right axis malformations (LRAM) [MIM:601877]: The defect includes left pulmonary isomerism, with cardiac anomalies characterized by complete atrioventricular canal defect and hypoplastic left ventricle, and interrupted inferior vena cava. {ECO:0000269|PubMed:10053005}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Mesenchymal cells of the endometrial stroma.; . . 0.57821 0.52666 0.327131069 73.27199811 536.93525 4.72439 LEKR1 . . . leucine, glutamate and lysine rich 1 . . . . . 0.14363 . 0.367590509 74.75819769 212.7695 3.14837 LELP1 0.000473718090816196 0.252535058042464 0.74699122386672 late cornified envelope-like proline-rich 1 . . . . . 0.16543 0.07942 0.191216164 66.57230479 13.81394 0.50152 LEMD1 0.00457260632601518 0.677099051998634 0.318328341675351 LEM domain containing 1 . . TISSUE SPECIFICITY: Testis-specific. Isoform 6 is detected in 17 of 18 colon cancer tissues examined. {ECO:0000269|PubMed:15254688}.; . . 0.12231 0.09637 . . 817.62897 5.61755 LEMD1-AS1 . . . LEMD1 antisense RNA 1 . . . . . . . . . . . LEMD2 0.302373361272148 0.696795916416705 0.000830722311147122 LEM domain containing 2 FUNCTION: Involved in nuclear structure organization (PubMed:16339967). Required for maintaining the integrity of the nuclear envelope (PubMed:17097643). {ECO:0000269|PubMed:16339967, ECO:0000269|PubMed:17097643}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:16339967}.; ovary;colon;parathyroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion; 0.22339 0.12131 . . 488.29843 4.54810 LEMD3 0.998968434807237 0.00103156509820159 9.45614970303094e-11 LEM domain containing 3 FUNCTION: Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest. {ECO:0000269|PubMed:15601644, ECO:0000269|PubMed:15647271}.; DISEASE: Melorheostosis (MEL) [MIM:155950]: Rare mesenchymal dysplasia and one of the sclerosing bone disorders. It is caused by a developmental error, with a sclerotomal distribution, frequently involving one limb. It may be asymptomatic, but pain, stiffness with limitation of motion, leg-length discrepancy and limb deformity may occur. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver and skeletal muscle.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;pituitary gland;testis;germinal center;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;urinary;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;head and neck;kidney;stomach;aorta;thymus; testis - interstitial;testis - seminiferous tubule; 0.48657 0.16103 -1.153638777 6.233781552 77.57342 1.85406 LENEP 0.0322826229786669 0.607280340641286 0.360437036380047 lens epithelial protein FUNCTION: May play a role in lens epithelial cell differentiation.; . . . . 0.15164 0.06756 0.235309407 68.71903751 26.57229 0.85931 LENG1 2.62557266408798e-09 0.0423864773012801 0.957613520073147 leukocyte receptor cluster (LRC) member 1 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;bile duct;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;thymus; . 0.53607 0.08499 0.062575634 58.74026893 184.87622 2.95119 LENG8 0.998395296073242 0.0016047038705761 5.618169533889e-11 leukocyte receptor cluster (LRC) member 8 . . . smooth muscle;ovary;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;thyroid;testis;amniotic fluid;dura mater;brain;unclassifiable (Anatomical System);meninges;lymph node;heart;lacrimal gland;tongue;islets of Langerhans;blood;pancreas;pia mater;lung;epididymis;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; . 0.14592 0.10396 -1.080231599 7.277659825 678.50553 5.20620 LENG8-AS1 . . . LENG8 antisense RNA 1 . . . . . . . . . . . LENG9 4.98776968397646e-10 0.0161014810964157 0.983898518404807 leukocyte receptor cluster (LRC) member 9 . . . unclassifiable (Anatomical System);lung; . 0.65040 . . . 4661.10154 13.75397 LEO1 0.999605969713844 0.000394030064827437 2.21328383545656e-10 LEO1 homolog, Paf1/RNA polymerase II complex component FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non- phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Involved in polyadenylation of mRNA precursors. Connects PAF1C to Wnt signaling. {ECO:0000269|PubMed:15632063, ECO:0000269|PubMed:15791002, ECO:0000269|PubMed:19345177, ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle and heart. Weakly expressed in placenta and liver. {ECO:0000269|PubMed:15791002}.; ovary;salivary gland;developmental;intestine;colon;parathyroid;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach; . 0.16469 0.15909 -1.111360919 6.717386176 76.3896 1.83267 LEP 0.318971026075485 0.613046386161323 0.0679825877631926 leptin FUNCTION: Key player in the regulation of energy balance and body weight control. Once released into the circulation, has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways (PubMed:17344214, PubMed:15899045, PubMed:19688109). In the hypothalamus, acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic for endothelial cell and affects innate and adaptive immunity (By similarity) (PubMed:8589726, PubMed:11460888, PubMed:19688109, PubMed:24340098, PubMed:25060689). In the arcuate nucleus of the hypothalamus, activates by depolarization POMC neurons inducing FOS and SOCS3 expression to release anorexigenic peptides and inhibits by hyperpolarization NPY neurons inducing SOCS3 with a consequent reduction on release of orexigenic peptides (By similarity). In addition to its known satiety inducing effect, has a modulatory role in nutrient absorption. In the intestine, reduces glucose absorption by enterocytes by activating PKC and leading to a sequential activation of p38, PI3K and ERK signaling pathways which exerts an inhibitory effect on glucose absorption (PubMed:24340098). Acts as a growth factor on certain tissues, through the activation of different signaling pathways increases expression of genes involved in cell cycle regulation such as CCND1, via JAK2-STAT3 pathway, or VEGFA, via MAPK1/3 and PI3K-AKT1 pathways (By similarity) (PubMed:17344214). May also play an apoptotic role via JAK2-STAT3 pathway and up-regulation of BIRC5 expression (PubMed:18242580). Pro-angiogenic, has mitogenic activity on vascular endothelial cells and plays a role in matrix remodeling by regulating the expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) (PubMed:11460888). In innate immunity, modulates the activity and function of neutrophils by increasing chemotaxis and the secretion of oxygen radicals. Increases phagocytosis by macrophages and enhances secretion of pro- inflammatory mediators. Increases cytotoxic ability of NK cells (Probable). Plays a pro-inflammatory role, in synergy with IL1B, by inducing NOS2 wich promotes the production of IL6, IL8 and Prostaglandin E2, through a signaling pathway that involves JAK2, PI3K, MAP2K1/MEK1 and MAPK14/p38 (PubMed:15899045, PubMed:19688109). In adaptive immunity, promotes the switch of memory T-cells towards T helper-1 cell immune responses (By similarity). Increases CD4(+)CD25(-) T cells proliferation and reduces autophagy during TCR (T cell receptor) stimulation, through MTOR signaling pathway activation and BCL2 up-regulation (PubMed:25060689). {ECO:0000250|UniProtKB:P41160, ECO:0000250|UniProtKB:P50596, ECO:0000269|PubMed:11460888, ECO:0000269|PubMed:15899045, ECO:0000269|PubMed:17344214, ECO:0000269|PubMed:18242580, ECO:0000269|PubMed:19688109, ECO:0000269|PubMed:24340098, ECO:0000269|PubMed:25060689, ECO:0000269|PubMed:8589726, ECO:0000305|PubMed:15122202, ECO:0000305|PubMed:25232147}.; DISEASE: Leptin deficiency (LEPD) [MIM:614962]: A rare disease characterized by low levels of serum leptin, severe hyperphagia and intractable obesity from an early age. {ECO:0000269|PubMed:9500540}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Adipose tissue is the main source of leptin it is also produced by other peripheral tissues such as the skeletal muscle (PubMed:7789654, PubMed:16052473, PubMed:12448771). Expressed by intercalated and striated tracts of submandibular and parotid salivary gland intralobular ducts (PubMed:12448771). Detected by fundic epithelium of the gastric mucosa (PubMed:10896907). Secreted into blood and gastric juice (PubMed:10896907). {ECO:0000269|PubMed:10896907, ECO:0000269|PubMed:12448771, ECO:0000269|PubMed:16052473, ECO:0000269|PubMed:7789654}.; unclassifiable (Anatomical System);cartilage;placenta;mammary gland;skeletal muscle; dorsal root ganglion;testis - interstitial;superior cervical ganglion;placenta;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.37030 0.78193 0.058937498 58.26256192 41.78794 1.21768 LEPR 0.999805342049916 0.00019465794204877 8.03551755018765e-12 leptin receptor FUNCTION: Receptor for obesity factor (leptin). On ligand binding, mediates signaling through JAK2/STAT3. Involved in the regulation of fat metabolism and, in a hematopoietic pathway, required for normal lymphopoiesis. May play a role in reproduction. Can also mediate the ERK/FOS signaling pathway (By similarity). {ECO:0000250}.; DISEASE: Leptin receptor deficiency (LEPRD) [MIM:614963]: A rare disease characterized by normal levels of serum leptin, hyperphagia and severe obesity from an early age. Additional features include alterations in immune function, and delayed puberty due to hypogonadotropic hypogonadism. {ECO:0000269|PubMed:9537324}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform A is expressed in fetal liver and in hematopoietic tissues and choroid plexus. In adults highest expression in heart, liver, small intestine, prostate and ovary. Low level in lung and kidney. Isoform B is highly expressed in hypothalamus.; unclassifiable (Anatomical System);heart;cartilage;colon;skeletal muscle;bone marrow;uterus;placenta;bone;trabecular meshwork;hippocampus;liver;testis;cervix;brain;peripheral nerve; dorsal root ganglion;superior cervical ganglion;fetal liver;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.55299 0.08243 -0.216746887 37.69757018 2800.90586 9.99290 LEPROT 0.0947893568489441 0.768843555769765 0.136367087381291 leptin receptor overlapping transcript FUNCTION: Negatively regulates leptin receptor (LEPR) cell surface expression, and thus decreases response to leptin. Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability. {ECO:0000269|PubMed:18042720, ECO:0000269|PubMed:19907080}.; . TISSUE SPECIFICITY: Expressed at the highest levels in heart and placenta and at a lesser extent in lung, liver, skeletal muscle, kidney and pancreas.; . . 0.23172 0.87580 -0.009020804 52.8544468 3.87804 0.14449 LEPROTL1 0.622320079235797 0.345781519976996 0.0318984007872078 leptin receptor overlapping transcript-like 1 FUNCTION: Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability. {ECO:0000269|PubMed:19907080}.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in heart, testis, adrenal gland, thymus, and spleen, and lowest expression in lung and skeletal muscle.; myocardium;ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;brain;gall bladder;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;alveolus;spleen;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;atrium;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;placenta;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.26166 0.09235 0.481458261 79.03986789 166.70851 2.82086 LETM1 0.0810547259175606 0.918503871373502 0.000441402708937353 leucine zipper and EF-hand containing transmembrane protein 1 FUNCTION: Crucial for the maintenance of mitochondrial tubular networks and for the assembly of the supercomplexes of the respiratory chain. Required for the maintenance of the tubular shape and cristae organization. {ECO:0000269|PubMed:18628306}.; . . salivary gland;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.10606 0.09638 0.538284722 81.08634112 641.37191 5.08923 LETM1P1 . . . leucine zipper and EF-hand containing transmembrane protein 1 pseudogene 1 . . . . . . . . . . . LETM1P2 . . . leucine zipper and EF-hand containing transmembrane protein 1 pseudogene 2 . . . . . . . . . . . LETM1P3 . . . leucine zipper and EF-hand containing transmembrane protein 1 pseudogene 3 . . . . . . . . . . . LETM2 1.34235674967667e-10 0.0987874918137866 0.901212508051978 leucine zipper and EF-hand containing transmembrane protein 2 . . . unclassifiable (Anatomical System);heart;cartilage;choroid;skin;bone marrow;uterus;whole body;lung;frontal lobe;liver;testis;kidney;brain;stomach; superior cervical ganglion;testis - interstitial;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09275 0.07424 1.084010791 91.8141071 110.11008 2.28066 LETMD1 0.793860582161175 0.205879032061735 0.000260385777090442 LETM1 domain containing 1 FUNCTION: Involved in tumorigenesis and may function as a negative regulator of the p53/TP53. {ECO:0000269|PubMed:12879013}.; . TISSUE SPECIFICITY: Kidney, liver, skeletal muscle, heart and brain. Overexpressed in various tumors including leukemia, lymphoma, and carcinomas of the breast, kidney, ovary, stomach, colon and uterine cervix. {ECO:0000269|PubMed:12879013}.; medulla oblongata;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;prefrontal cortex;appendix;ciliary ganglion;atrioventricular node;parietal lobe;cingulate cortex; 0.09789 0.07743 0.260991686 70.25831564 65.56731 1.66690 LEUTX . . . leucine twenty homeobox . . . . . . . . . 9.49527 0.35016 LEXM . . . lymphocyte expansion molecule . . . . . 0.07116 0.08588 1.798708763 96.91554612 . . LFNG 0.424039268574049 0.568359641656371 0.00760108976958064 LFNG O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase FUNCTION: Glycosyltransferase that initiates the elongation of O- linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Decreases the binding of JAGGED1 to NOTCH2 but not that of DELTA1. Essential mediator of somite segmentation and patterning (By similarity). {ECO:0000250}.; DISEASE: Spondylocostal dysostosis 3, autosomal recessive (SCDO3) [MIM:609813]: A condition of variable severity associated with vertebral and rib segmentation defects. The main skeletal malformations include fusion of vertebrae, hemivertebrae, fusion of certain ribs, and other rib malformations. Deformity of the chest and spine (severe scoliosis, kyphoscoliosis and lordosis) is a natural consequence of the malformation and leads to a dwarf- like appearance. As the thorax is small, infants frequently have respiratory insufficiency and repeated respiratory infections resulting in life-threatening complications in the first year of life. {ECO:0000269|PubMed:16385447}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;cartilage;colon;fovea centralis;choroid;lens;retina;bone marrow;prostate;optic nerve;lung;macula lutea;hypopharynx;head and neck;germinal center;kidney;brain;stomach;thymus; superior cervical ganglion;atrioventricular node;parietal lobe;skeletal muscle; 0.27035 0.18936 -0.045835247 50.34206181 24.41703 0.80311 LGALS1 0.00463689761502241 0.680040703909729 0.315322398475248 lectin, galactoside-binding, soluble, 1 FUNCTION: Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis. {ECO:0000269|PubMed:14617626, ECO:0000269|PubMed:18796645, ECO:0000269|PubMed:19497882, ECO:0000269|PubMed:24945728}.; . TISSUE SPECIFICITY: Expressed in placenta, maternal decidua and fetal membranes. Within placenta, expressed in trophoblasts, stromal cells, villous endothelium, syncytiotrophoblast apical membrane and villous stroma. Within fetal membranes, expressed in amnion, chorioamniotic mesenchyma and chorion (at protein level). Expressed in cardiac, smooth, and skeletal muscle, neurons, thymus, kidney and hematopoietic cells. {ECO:0000269|PubMed:18824694, ECO:0000269|PubMed:19497882}.; myocardium;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;iris;bladder;brain;tonsil;heart;cartilage;tongue;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;uterus;whole body;oesophagus;bone;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;hypothalamus;muscle;bile duct;pancreas;lung;pia mater;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; smooth muscle;lung;heart; 0.70473 0.62115 -0.029247611 51.40363293 11.17392 0.40417 LGALS2 0.0146890321396129 0.683740277996109 0.301570689864278 lectin, galactoside-binding, soluble, 2 FUNCTION: This protein binds beta-galactoside. Its physiological function is not yet known.; . . unclassifiable (Anatomical System);ovary;heart;salivary gland;intestine;pharynx;colon;blood;skin;breast;uterus;prostate;pancreas;synovium;nasopharynx;visual apparatus;liver;spleen;kidney;brain;bladder;gall bladder; kidney; 0.12147 0.14860 0.104848986 61.49445624 348.65408 3.95736 LGALS3 0.00017511393726883 0.457366472763046 0.542458413299685 lectin, galactoside-binding, soluble, 3 FUNCTION: Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis (By similarity). In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells. {ECO:0000250, ECO:0000269|PubMed:15181153, ECO:0000269|PubMed:19594635, ECO:0000269|PubMed:19616076}.; . TISSUE SPECIFICITY: A major expression is found in the colonic epithelium. It is also abundant in the activated macrophages. Expressed in fetal membranes. {ECO:0000269|PubMed:19497882}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;oesophagus;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;small intestine;lacrimal gland;tongue;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;alveolus;liver;cervix;spleen;kidney;mammary gland;stomach;thymus; . 0.34085 0.66067 0.927856124 89.70276008 1969.59272 8.17983 LGALS3BP 3.92643319809695e-07 0.357412318039707 0.642587289316973 lectin, galactoside-binding, soluble, 3 binding protein FUNCTION: Promotes intergrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells. {ECO:0000269|PubMed:11146440, ECO:0000269|PubMed:8034587, ECO:0000269|PubMed:9501082}.; . TISSUE SPECIFICITY: Ubiquitous. Detected in body fluids such as semen, milk, serum, tears, saliva and urine. Expressed by keratinocytes and fibroblasts. {ECO:0000269|PubMed:8034587, ECO:0000269|PubMed:8390986, ECO:0000269|PubMed:8757764}.; smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;bone marrow;uterus;prostate;endometrium;gum;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; heart;adrenal gland; 0.44538 0.20815 -0.973616687 8.8995046 60.77046 1.58489 LGALS4 6.568948476447e-06 0.707045744655664 0.29294768639586 lectin, galactoside-binding, soluble, 4 FUNCTION: Galectin that binds lactose and a related range of sugars. May be involved in the assembly of adherens junctions.; . . unclassifiable (Anatomical System);cartilage;small intestine;islets of Langerhans;adrenal medulla;colon;blood;bone marrow;pancreas;lung;placenta;liver;spleen;kidney;mammary gland;bladder;stomach;gall bladder; superior cervical ganglion;pancreas;liver;skeletal muscle; 0.10028 0.71569 -0.53631094 20.53550366 164.38826 2.79965 LGALS7 0.43376704344564 0.459290785160748 0.106942171393612 lectin, galactoside-binding, soluble, 7 FUNCTION: Could be involved in cell-cell and/or cell-matrix interactions necessary for normal growth control. Pro-apoptotic protein that functions intracellularly upstream of JNK activation and cytochrome c release. {ECO:0000269|PubMed:11706006}.; . TISSUE SPECIFICITY: Mainly expressed in stratified squamous epithelium.; . . . 0.13610 . . 34.84531 1.06094 LGALS7B 0.478395552225766 0.438571493465357 0.083032954308877 lectin, galactoside-binding, soluble, 7B FUNCTION: Could be involved in cell-cell and/or cell-matrix interactions necessary for normal growth control. Pro-apoptotic protein that functions intracellularly upstream of JNK activation and cytochrome c release. {ECO:0000269|PubMed:11706006}.; . TISSUE SPECIFICITY: Mainly expressed in stratified squamous epithelium.; unclassifiable (Anatomical System);heart;ovary;salivary gland;intestine;pharynx;colon;blood;skin;uterus;prostate;lung;cornea;larynx;visual apparatus;liver;cervix;kidney;brain;mammary gland;peripheral nerve; . . 0.25875 . . 5.82715 0.21998 LGALS8 0.000188797120394855 0.89697374449324 0.102837458386366 lectin, galactoside-binding, soluble, 8 FUNCTION: Lectin with a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans. {ECO:0000269|PubMed:21288902}.; . TISSUE SPECIFICITY: Ubiquitous. Selective expression by prostate carcinomas versus normal prostate and benign prostatic hypertrophy.; lymphoreticular;medulla oblongata;smooth muscle;ovary;sympathetic chain;substantia nigra;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;urinary;spinal cord;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;atrium;cerebral cortex;larynx;bone;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;hypothalamus;muscle;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;testis - interstitial;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;appendix;testis;trigeminal ganglion; 0.48105 0.17047 1.063778722 91.58410002 6987.34024 17.79441 LGALS8-AS1 . . . LGALS8 antisense RNA 1 . . . . . . . . . . . LGALS9 0.00139053962852711 0.964148727049041 0.0344607333224317 lectin, galactoside-binding, soluble, 9 FUNCTION: Binds galactosides (PubMed:18005988). Has high affinity for the Forssman pentasaccharide (PubMed:18005988). Ligand for HAVCR2/TIM3 (PubMed:16286920). Binding to HAVCR2 induces T-helper type 1 lymphocyte (Th1) death (PubMed:16286920). Also stimulates bactericidal activity in infected macrophages by causing macrophage activation and IL1B secretion which restricts intracellular bacterial growth (By similarity). Ligand for P4HB; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307). Ligand for CD44; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up- regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function (By similarity). Promotes ability of mesenchymal stromal cells to suppress T-cell proliferation (PubMed:23817958). Expands regulatory T cells and induces cytotoxic T cell apoptosis following virus infection (PubMed:20209097). Activates ERK1/2 phosphorylation inducing cytokine (IL-6, IL-8, IL-12) and chemokine (CCL2) production in mast and dendritic cells (PubMed:24465902, PubMed:16116184). Inhibits degranulation and induces apoptosis of mast cells (PubMed:24465902). Induces maturation and migration of dendritic cells (PubMed:25754930, PubMed:16116184). Inhibits natural killer (NK) cell function (PubMed:23408620). Can transform NK cell phenotype from peripheral to decidual during pregnancy (PubMed:25578313). Astrocyte derived galectin-9 enhances microglial TNF production (By similarity). May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. May provide the molecular basis for urate flux across cell membranes, allowing urate that is formed during purine metabolism to efflux from cells and serving as an electrogenic transporter that plays an important role in renal and gastrointestinal urate excretion (By similarity). Highly selective to the anion urate (By similarity). {ECO:0000250|UniProtKB:O08573, ECO:0000250|UniProtKB:P97840, ECO:0000269|PubMed:16116184, ECO:0000269|PubMed:16286920, ECO:0000269|PubMed:18005988, ECO:0000269|PubMed:18977853, ECO:0000269|PubMed:20209097, ECO:0000269|PubMed:21670307, ECO:0000269|PubMed:23408620, ECO:0000269|PubMed:23817958, ECO:0000269|PubMed:24465902, ECO:0000269|PubMed:25578313, ECO:0000269|PubMed:25754930}.; . TISSUE SPECIFICITY: Peripheral blood leukocytes and lymphatic tissues. Expressed in lung, liver, breast and kidney with higher levels in tumor endothelial cells than normal endothelium (at protein level) (PubMed:24333696). Expressed in trophoblast cells in decidua and placenta in pregnancy (at protein level) (PubMed:23242525, PubMed:25578313). Isoform 2 is the most abundant isoform expressed in endothelial cells (PubMed:24333696). Upon endothelial cell activation isoform 2 expression decreases while expression of isoform 3 and isoform 5 increases (PubMed:24333696). Isoform 4 decreases in pathological pregnancy (PubMed:23242525). {ECO:0000269|PubMed:23242525, ECO:0000269|PubMed:24333696, ECO:0000269|PubMed:25578313}.; ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;optic nerve;cerebral cortex;endometrium;bone;iris;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;pancreas;lung;placenta;liver;alveolus;spleen;kidney;mammary gland;stomach; white blood cells;bone marrow; 0.13572 0.22025 0.797386419 87.53833451 2358.5758 9.00919 LGALS9B . . . lectin, galactoside-binding, soluble, 9B FUNCTION: Binds galactosides. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;cartilage;ovary;placenta;alveolus;testis;choroid;germinal center;brain;stomach;tonsil; . . . . . 1350.76308 6.90243 LGALS9C 0.940115540676897 0.0598347001100741 4.9759213028552e-05 lectin, galactoside-binding, soluble, 9C FUNCTION: Binds galactosides. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;lung;cartilage;ovary;placenta;alveolus;testis;choroid;germinal center;brain;stomach;tonsil; . . . -0.315847836 31.68789809 319.8515 3.79900 LGALS9DP . . . lectin, galactoside-binding, soluble, 9D, pseudogene . . . . . . . . . . . LGALS12 2.6857353502622e-09 0.0813751634571547 0.91862483385711 lectin, galactoside-binding, soluble, 12 FUNCTION: Binds lactose. May participate in the apoptosis of adipocytes.; . TISSUE SPECIFICITY: Not widely expressed. Predominantly expressed in adipose tissue.; unclassifiable (Anatomical System);adrenal gland;iris;alveolus;blood;choroid;mammary gland;stomach;bone marrow; dorsal root ganglion;superior cervical ganglion;adipose tissue;ciliary ganglion;atrioventricular node; 0.07669 0.11723 0.663285274 84.55414013 301.56226 3.69950 LGALS13 6.77894375320678e-05 0.490783087746715 0.509149122815753 lectin, galactoside-binding, soluble, 13 FUNCTION: Binds beta-galactoside and lactose. Strong inducer of T- cell apoptosis. {ECO:0000269|PubMed:10527825, ECO:0000269|PubMed:19497882}.; . TISSUE SPECIFICITY: Detected in adult and fetal spleen, fetal kidney, adult urinary bladder and placenta. Placental expression originates predominantly from the syncytiotrophoblast. {ECO:0000269|PubMed:10527825, ECO:0000269|PubMed:19497882}.; ovary;placenta;liver;parathyroid;spleen; superior cervical ganglion;placenta;ciliary ganglion; 0.22880 0.15849 0.571462851 81.99457419 63.38702 1.62957 LGALS14 0.0100122793683261 0.823537378881487 0.166450341750187 lectin, galactoside-binding, soluble, 14 FUNCTION: Binds beta-galactoside and lactose. Strong inducer of T- cell apoptosis. {ECO:0000269|PubMed:19497882}.; . TISSUE SPECIFICITY: Highly expressed in placenta. {ECO:0000269|PubMed:11997112, ECO:0000269|PubMed:19497882}.; whole body;ovary;placenta;liver;parathyroid;spleen; dorsal root ganglion;superior cervical ganglion;placenta;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07595 0.11822 1.148343558 92.42745931 495.28106 4.57413 LGALS16 4.37119316925913e-05 0.232701543305526 0.767254744762781 lectin, galactoside-binding, soluble, 16 FUNCTION: Binds lactose with high affinity. Strong inducer of T- cell apoptosis. {ECO:0000269|PubMed:19497882}.; . . . . . . . . 89.48487 2.03330 LGALSL 0.670765299027282 0.324277998005584 0.00495670296713401 lectin, galactoside-binding-like FUNCTION: Does not bind lactose, and may not bind carbohydrates. {ECO:0000269|PubMed:18320588, ECO:0000269|PubMed:18433051}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;aorta; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; 0.15047 0.12256 0.125076652 62.7388535 27.99532 0.89900 LGI1 0.997175814162011 0.00282405281279352 1.33025195751924e-07 leucine-rich, glioma inactivated 1 FUNCTION: Regulates voltage-gated potassium channels assembled from KCNA1, KCNA4 and KCNAB1. It slows down channel inactivation by precluding channel closure mediated by the KCNAB1 subunit. Ligand for ADAM22 that positively regulates synaptic transmission mediated by AMPA-type glutamate receptors (By similarity). Plays a role in suppressing the production of MMP1/3 through the phosphatidylinositol 3-kinase/ERK pathway. May play a role in the control of neuroblastoma cell survival. {ECO:0000250, ECO:0000269|PubMed:15047712, ECO:0000269|PubMed:16518856}.; DISEASE: Epilepsy, familial temporal lobe, 1 (ETL1) [MIM:600512]: A focal form of epilepsy characterized by recurrent seizures that arise from foci within the temporal lobe. Seizures are usually accompanied by sensory symptoms, most often auditory in nature. {ECO:0000269|PubMed:11810107, ECO:0000269|PubMed:12205652, ECO:0000269|PubMed:12601709, ECO:0000269|PubMed:12771268, ECO:0000269|PubMed:15079010, ECO:0000269|PubMed:17296837, ECO:0000269|PubMed:17562837, ECO:0000269|PubMed:18625862, ECO:0000269|PubMed:19552651}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in neural tissues, especially in brain. Expression is reduced in low-grade brain tumors and significantly reduced or absent in malignant gliomas. Isoform 1 is absent in the cerebellum and is detectable in the occipital cortex and hippocampus; higher amounts are observed in the parietal and frontal cortices, putamen, and, particularly, in the temporal neocortex, where it is 3.5 times more abundant than in the hippocampus (at protein level). Isoform 3 shows the highest expression in the occipital cortex and the lowest in the hippocampus (at protein level). {ECO:0000269|PubMed:16518856, ECO:0000269|PubMed:16787412}.; . . 0.63786 0.32628 -0.714505427 14.4019816 9.15111 0.33358 LGI2 4.4155177153273e-05 0.852066662786432 0.147889182036415 leucine-rich repeat LGI family member 2 . . TISSUE SPECIFICITY: Brain, heart and placenta. {ECO:0000269|PubMed:12023020}.; unclassifiable (Anatomical System);meninges;ovary;cerebellum cortex;islets of Langerhans;blood;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;pia mater;lung;placenta;macula lutea;testis;dura mater;kidney;brain; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;uterus corpus;olfactory bulb;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.26964 0.11567 -0.312207497 32.05944798 1960.91632 8.15653 LGI3 1.94564245688285e-05 0.891582311258763 0.108398232316668 leucine-rich repeat LGI family member 3 FUNCTION: May participate in the regulation of neuronal exocytosis. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in brain and lung. {ECO:0000269|PubMed:12023020}.; unclassifiable (Anatomical System);prostate;optic nerve;lung;frontal lobe;islets of Langerhans;thyroid;hippocampus;brain;skin; amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.20339 0.12510 -1.065444789 7.425100259 379.05519 4.10568 LGI4 0.0263199127837975 0.919352223073855 0.054327864142347 leucine-rich repeat LGI family member 4 . . TISSUE SPECIFICITY: Widely expressed, with highest expression in brain. {ECO:0000269|PubMed:12023020}.; unclassifiable (Anatomical System);heart;ovary;colon;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;pancreas;prostate;optic nerve;lung;cochlea;cerebral cortex;nasopharynx;bone;macula lutea;testis;spinal ganglion;brain;peripheral nerve;thymus; . 0.08903 0.11980 -0.001743238 53.85114414 249.00287 3.39938 LGMD1G . . . limb girdle muscular dystrophy 1G (autosomal dominant) . . . . . . . . . . . LGMD1H . . . limb girdle muscular dystrophy 1H (autosomal dominant) . . . . . . . . . . . LGMN 0.00097489450100372 0.986740549161317 0.0122845563376795 legumain FUNCTION: Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation (By similarity). May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system. {ECO:0000250, ECO:0000269|PubMed:23776206}.; . TISSUE SPECIFICITY: Ubiquitous. Particularly abundant in kidney, heart and placenta.; myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;iris;brain;gall bladder;heart;cartilage;tongue;pineal body;urinary;blood;lens;skeletal muscle;epididymis;visual apparatus;macula lutea;liver;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);small intestine;lacrimal gland;islets of Langerhans;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; placenta;kidney; 0.18925 0.32479 -0.023789244 52.09365416 45.20813 1.29089 LGMNP1 . . . legumain pseudogene 1 . . . . . . . . . . . LGR4 0.994112645257008 0.00588734811670886 6.62628278813219e-09 leucine-rich repeat containing G protein-coupled receptor 4 FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Its function as activator of the Wnt signaling pathway is required for the development of various organs, including liver, kidney, intestine, bone, reproductive tract and eye. May also act as a receptor for norrin (NDP), such results however require additional confirmation in vivo. Required during spermatogenesis to activate the Wnt signaling pathway in peritubular myoid cells. Required for the maintenance of intestinal stem cells and Paneth cell differentiation in postnatal intestinal crypts. Acts as a regulator of bone formation and remodeling. Involved in kidney development; required for maintaining the ureteric bud in an undifferentiated state. Involved in the development of the anterior segment of the eye. Required during erythropoiesis. Also acts as a negative regulator of innate immunity by inhibiting TLR2/TLR4 associated pattern-recognition and proinflammatory cytokine production. Plays an important role in regulating the circadian rhythms of plasma lipids, partially through regulating the rhythmic expression of MTTP (By similarity). {ECO:0000250|UniProtKB:A2ARI4, ECO:0000269|PubMed:21693646, ECO:0000269|PubMed:21727895, ECO:0000269|PubMed:21909076, ECO:0000269|PubMed:22815884, ECO:0000269|PubMed:23444378, ECO:0000269|PubMed:23756652}.; DISEASE: Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal disorder characterized by decreased bone mass and deterioration of bone microarchitecture without alteration in the composition of bone. The result is fragile bones and an increased risk of fractures, even after minimal trauma. Osteoporosis is a chronic condition of multifactorial etiology and is usually clinically silent until a fracture occurs. {ECO:0000269|PubMed:23644456}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry. A LGR4 nonsense mutation creating a stop codon after position 126 (c.376C>T) is strongly associated with low bone mineral density and osteoporotic fractures (PubMed:23644456). This mutation probably causes degradation of the transcript by nonsense-mediated decay (NMD). The c.376C>T mutation is also associated with electrolyte imbalance, late onset of menarche and reduced testosterone levels, as well as an increased risk of squamous cell carcinoma of the skin and biliary tract cancer (PubMed:23644456). {ECO:0000269|PubMed:23644456}.; TISSUE SPECIFICITY: Expressed in multiple steroidogenic tissues: placenta, ovary, testis and adrenal. Expressed also in spinal cord, thyroid, stomach, trachea, heart, pancreas, kidney, prostate and spleen.; . . 0.46726 0.12964 -0.264476624 34.8844067 799.80536 5.57325 LGR5 1.13571270342706e-05 0.997432040162038 0.00255660271092758 leucine-rich repeat containing G protein-coupled receptor 5 FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a stem cell marker of the intestinal epithelium and the hair follicle. Upon binding to R- spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Involved in the development and/or maintenance of the adult intestinal stem cells during postembryonic development. {ECO:0000269|PubMed:21693646, ECO:0000269|PubMed:21727895, ECO:0000269|PubMed:21909076, ECO:0000269|PubMed:22815884, ECO:0000269|PubMed:23809763}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, placenta, spinal cord, and various region of brain. Expressed at the base of crypts in colonic and small mucosa stem cells. In premalignant cancer expression is not restricted to the cript base. Overexpressed in cancers of the ovary, colon and liver. {ECO:0000269|PubMed:12601349, ECO:0000269|PubMed:16575208, ECO:0000269|PubMed:19030762}.; unclassifiable (Anatomical System);amygdala;whole body;endometrium;placenta;liver;colon;skeletal muscle;stomach; superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;fetal thyroid;skin; 0.63909 0.14109 1.563447604 95.67704647 864.39851 5.73072 LGR6 4.08845719461255e-05 0.997948260919497 0.00201085450855727 leucine-rich repeat containing G protein-coupled receptor 6 FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a marker of multipotent stem cells in the epidermis. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. May act as a tumor suppressor. {ECO:0000269|PubMed:21727895, ECO:0000269|PubMed:22615920}.; . . unclassifiable (Anatomical System);heart;ovary;tongue;colon;skin;bone marrow;uterus;lung;larynx;visual apparatus;testis;head and neck;brain; globus pallidus;ciliary ganglion;atrioventricular node; 0.13208 . -0.097422643 45.69473933 876.8993 5.76241 LGSN 2.5899855281394e-07 0.291169715194655 0.708830025806793 lengsin, lens protein with glutamine synthetase domain FUNCTION: May act as a component of the cytoskeleton or as a chaperone for the reorganization of intermediate filament proteins during terminal differentiation in the lens. Does not seem to have enzymatic activity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Abundantly expressed in lens. {ECO:0000269|PubMed:12107413, ECO:0000269|PubMed:17010935}.; . . 0.06929 0.14121 0.622829232 83.47487615 267.72084 3.50957 LGTN . . . ligatin . . . . . 0.24884 0.13449 . . . . LHB 0.065600109491978 0.730304778369319 0.204095112138704 luteinizing hormone beta polypeptide FUNCTION: Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids.; . TISSUE SPECIFICITY: Pituitary gland.; unclassifiable (Anatomical System);lung;pituitary gland;testis;blood;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;pituitary;parietal lobe; 0.16761 0.47659 0.751474114 86.64779429 243.56684 3.36792 LHCGR 2.80154457660207e-08 0.490421431053641 0.509578540930913 luteinizing hormone/choriogonadotropin receptor FUNCTION: Receptor for lutropin-choriogonadotropic hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.; DISEASE: Luteinizing hormone resistance (LHR) [MIM:238320]: An autosomal recessive disorder characterized by unresponsiveness to luteinizing hormone, defective sexual development in males, and defective follicular development and ovulation, amenorrhea and infertility in females. Two forms of the disorder have been defined in males. Type 1 is a severe form characterized by complete 46,XY male pseudohermaphroditism, low testosterone and high luteinizing hormone levels, total lack of responsiveness to luteinizing and chorionic gonadotropin hormones, lack of breast development, and absent development of secondary male sex characteristics. Type 2, a milder form, displays a broader range of phenotypic expression ranging from micropenis to severe hypospadias. {ECO:0000269|PubMed:12050206, ECO:0000269|PubMed:15372531, ECO:0000269|PubMed:15472221, ECO:0000269|PubMed:19551906, ECO:0000269|PubMed:7719343, ECO:0000269|PubMed:8559204, ECO:0000269|PubMed:9215288, ECO:0000269|PubMed:9514160, ECO:0000269|PubMed:9626144, ECO:0000269|PubMed:9626653}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Gonadal and thyroid cells.; lung;testis; dorsal root ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.13036 0.42555 0.356452144 74.62845011 1328.76039 6.85266 LHFP 0.463787541652463 0.510752448795284 0.0254600095522526 lipoma HMGIC fusion partner . . TISSUE SPECIFICITY: Pancreas, kidney, skeletal muscle, liver, lung brain, heart, colon, small intestine, uterus, testis, prostate, thymus, spleen and placenta. {ECO:0000269|PubMed:10329012}.; . . 0.39211 . -0.09720619 46.20193442 21.82161 0.73472 LHFPL1 0.0706474575332219 0.739921912754523 0.189430629712255 lipoma HMGIC fusion partner-like 1 . . TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in lung, thymus, skeletal muscle, colon and ovary. {ECO:0000269|PubMed:15620218}.; . . 0.41862 0.10849 0.237127192 68.98443029 63.40001 1.62990 LHFPL2 0.0150144683952531 0.688146836889947 0.2968386947148 lipoma HMGIC fusion partner-like 2 . . TISSUE SPECIFICITY: Expressed in all tissues and cell lines examined except brain and peripheral blood leukocytes. {ECO:0000269|PubMed:9039502}.; . . 0.41077 0.10494 -0.073340031 48.11866006 60.10531 1.57339 LHFPL3 0.795069316295047 0.199083092248248 0.00584759145670525 lipoma HMGIC fusion partner-like 3 . . . . . 0.37590 0.08137 -0.229483771 36.86010852 83.8364 1.94971 LHFPL3-AS1 . . . LHFPL3 antisense RNA 1 . . . . . . . . . . . LHFPL3-AS2 . . . LHFPL3 antisense RNA 2 . . . . . . . . . . . LHFPL4 0.178387581231495 0.76693645570069 0.0546759630678145 lipoma HMGIC fusion partner-like 4 . . . unclassifiable (Anatomical System);lung;islets of Langerhans;retina; subthalamic nucleus; 0.42626 . -0.229483771 36.86010852 29.84895 0.95204 LHFPL5 0.494778072886935 0.484788859186782 0.0204330679262822 lipoma HMGIC fusion partner-like 5 FUNCTION: In the inner ear, may be a component of the hair cell's mechanotransduction machinery that functionally couples PCDH15 to the transduction channel. Regulates transducer channel conductance and is required for fast channel adaptation (By similarity). {ECO:0000250}.; DISEASE: Deafness, autosomal recessive, 67 (DFNB67) [MIM:610265]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:16459341, ECO:0000269|PubMed:16752389}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);hippocampus; superior cervical ganglion;atrioventricular node; 0.15116 0.13759 -0.339715008 30.06605331 35.90816 1.07827 LHPP 1.59687423011584e-06 0.236243715293698 0.763754687832072 phospholysine phosphohistidine inorganic pyrophosphate phosphatase FUNCTION: Phosphatase that hydrolyzes imidodiphosphate, 3- phosphohistidine and 6-phospholysine. Has broad substrate specificity and can also hydrolyze inorganic diphosphate, but with lower efficiency (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, and at lower levels in liver and kidney. Detected in thyroid (at protein level). Expressed in liver, kidney and moderately in brain. {ECO:0000269|PubMed:12801912, ECO:0000269|PubMed:16430861}.; . . . . 0.108486928 61.90728946 606.57632 4.98303 LHX1 0.289265565988382 0.68964812285504 0.0210863111565783 LIM homeobox 1 FUNCTION: Potential transcription factor. May play a role in early mesoderm formation and later in lateral mesoderm differentiation and neurogenesis. {ECO:0000269|PubMed:9212161}.; . TISSUE SPECIFICITY: Expressed in the brain, thymus, and tonsils. Expressed in samples from patients with chronic myeloid leukemia (CML) and in 58% of acute myeloid leukemia (AML) cell lines. {ECO:0000269|PubMed:9212161}.; unclassifiable (Anatomical System);optic nerve;lung;whole body;ovary;cervix;kidney; superior cervical ganglion;cerebellum peduncles;kidney;trigeminal ganglion; 0.86552 0.33462 0.150760231 64.51403633 193.33354 3.01652 LHX2 0.946789688867038 0.0530289120582877 0.000181399074674137 LIM homeobox 2 FUNCTION: Acts as a transcriptional activator. Stimulates the promoter of the alpha-glycoprotein gene. Transcriptional regulatory protein involved in the control of cell differentiation in developing lymphoid and neural cell types (By similarity). {ECO:0000250}.; . . . . 0.99245 0.23835 -0.117432389 44.89266336 . . LHX3 0.158417722579245 0.825870045098314 0.0157122323224415 LIM homeobox 3 FUNCTION: Acts as a transcriptional activator. Binds to and activates the promoter of the alpha-glycoprotein gene, and synergistically enhances transcription from the prolactin promoter in cooperation with POU1F1/Pit-1 (By similarity). Required for the establishment of the specialized cells of the pituitary gland and the nervous system. Involved in the development of interneurons and motor neurons in cooperation with LDB1 and ISL1. {ECO:0000250, ECO:0000269|PubMed:21149718}.; DISEASE: Pituitary hormone deficiency, combined, 3 (CPHD3) [MIM:221750]: Combined pituitary hormone deficiency is defined as the impaired production of growth hormone and one or more of the other five anterior pituitary hormones. CPHD3 is characterized by a complete deficit in all but one (adrenocorticotropin) anterior pituitary hormone and a rigid cervical spine leading to limited head rotation. {ECO:0000269|PubMed:10835633, ECO:0000269|PubMed:17327381}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . pineal gland; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;pituitary; 0.31215 0.25682 . . 27.96735 0.89736 LHX4 0.401093501395259 0.597028412855589 0.00187808574915273 LIM homeobox 4 FUNCTION: May play a critical role in the development of respiratory control mechanisms and in the normal growth and maturation of the lung. {ECO:0000250}.; DISEASE: Pituitary hormone deficiency, combined, 4 (CPHD4) [MIM:262700]: Combined pituitary hormone deficiency is defined as the impaired production of growth hormone and one or more of the other five anterior pituitary hormones. CPHD4 is characterized by complete or partial deficiencies of growth hormone, thyroid- stimulating hormone, luteinizing hormone, follicle stimulating hormone and adrenocorticotropic hormone. Clinical features include short stature, cerebellar defects, and small sella turcica. {ECO:0000269|PubMed:17527005, ECO:0000269|PubMed:18073311}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving LHX4 may be a cause of acute lymphoblastic leukemia. Translocation t(1;14)(q25;q32) with IGHG1. {ECO:0000269|PubMed:11567216}.; . unclassifiable (Anatomical System);uterus;brain;skeletal muscle; . 0.34908 0.20390 -0.446304853 24.33356924 3681.74246 11.81072 LHX4-AS1 . . . LHX4 antisense RNA 1 . . . . . . . . . . . LHX5 0.695818426257564 0.300282158448143 0.00389941529429328 LIM homeobox 5 FUNCTION: Plays an essential role in the regulation of neuronal differentiation and migration during development of the central nervous system.; . TISSUE SPECIFICITY: Expressed in fetal brain and in various regions of the adult central nervous system including the spinal cord, the thalamus, and the cerebellum.; unclassifiable (Anatomical System); dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;bone marrow; 0.55228 0.18572 0.014844891 54.94810097 23.15676 0.77249 LHX5-AS1 . . . LHX5 antisense RNA 1 (head to head) . . . . . . . . . . . LHX6 0.948528052712538 0.0514379566812512 3.39906062108088e-05 LIM homeobox 6 FUNCTION: Probable transcription factor required for the expression of a subset of genes involved in interneurons migration and development. Functions in the specification of cortical interneuron subtypes and in the migration of GABAergic interneuron precursors from the subpallium to the cerebral cortex (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;urinary;uterus;prostate;lung;endometrium;bone;placenta;visual apparatus;liver;testis;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion; 0.67128 0.14783 0.193034296 66.82000472 51.16379 1.40967 LHX8 0.663323206439864 0.335569026458995 0.00110776710114183 LIM homeobox 8 FUNCTION: Transcription factor involved in differentiation of certain neurons and mesenchymal cells. {ECO:0000250}.; . . hypothalamus;skin; superior cervical ganglion;adrenal gland;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.23784 0.15573 0.194852702 67.03231894 95.42382 2.10842 LHX9 0.941757643329135 0.0581959683528434 4.63883180218503e-05 LIM homeobox 9 FUNCTION: Involved in gonadal development. {ECO:0000250}.; . . unclassifiable (Anatomical System);whole body;visual apparatus;testis;colon; . 0.73616 0.22085 -0.117432389 44.89266336 47.87826 1.34412 LIAS 0.0614137585139882 0.935191347764876 0.00339489372113551 lipoic acid synthetase FUNCTION: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. {ECO:0000255|HAMAP-Rule:MF_03123}.; DISEASE: Pyruvate dehydrogenase lipoic acid synthetase deficiency (PDHLD) [MIM:614462]: An enzymatic defect resulting in an autosomal recessive disorder of mitochondrial metabolism. It is characterized by early-onset lactic acidosis, severe encephalomyopathy, and a pyruvate oxidation defect. Affected individuals have neonatal-onset epilepsy, poor growth, psychomotor retardation, muscular hypotonia, lactic acidosis, and elevated glycine concentration in plasma and urine. {ECO:0000269|PubMed:22152680}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;heart;cartilage;colon;substantia nigra;parathyroid;skeletal muscle;skin;prostate;whole body;lung;placenta;visual apparatus;liver;testis;spleen;kidney;brain;bladder;stomach; superior cervical ganglion;tongue;atrioventricular node;skeletal muscle; 0.10148 0.35804 -0.381986487 27.68931352 20.39287 0.69545 LIF 0.774442435814619 0.217983745885882 0.00757381829949919 leukemia inhibitory factor FUNCTION: LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes.; . . unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;skin;skeletal muscle;pancreas;lung;endometrium;larynx;bone;visual apparatus;hypopharynx;duodenum;amnion;head and neck;amniotic fluid;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;smooth muscle;globus pallidus;ciliary ganglion;pons;trigeminal ganglion; 0.24931 0.78312 0.283038099 71.26680821 140.99142 2.59068 LIFR 0.00100684330037545 0.998989056935355 4.09976426980015e-06 leukemia inhibitory factor receptor alpha FUNCTION: Signal-transducing molecule. May have a common pathway with IL6ST. The soluble form inhibits the biological activity of LIF by blocking its binding to receptors on target cells.; DISEASE: Stueve-Wiedemann syndrome (STWS) [MIM:601559]: Severe autosomal recessive condition and belongs to the group of the bent-bone dysplasias. SWS is characterized by bowing of the lower limbs, with internal cortical thickening, wide metaphyses with abnormal trabecular pattern, and camptodactyly. Additional features include feeding and swallowing difficulties, as well as respiratory distress and hyperthermic episodes, which cause death in the first months of life. The rare survivors develop progressive scoliosis, spontaneous fractures, bowing of the lower limbs, with prominent joints and dysautonomia symptoms, including temperature instability, absent corneal and patellar reflexes, and smooth tongue. {ECO:0000269|PubMed:14740318}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving LIFR is found in salivary gland pleiomorphic adenomas, the most common benign epithelial tumors of the salivary gland. Translocation t(5;8)(p13;q12) with PLAG1.; . unclassifiable (Anatomical System);ovary;parathyroid;skeletal muscle;prostate;whole body;lung;frontal lobe;endometrium;larynx;placenta;liver;testis;head and neck;spleen;kidney;spinal ganglion;brain;stomach; trigeminal ganglion; 0.71459 0.30916 -0.126743121 44.0905874 1747.13043 7.71496 LIFR-AS1 . . . LIFR antisense RNA 1 . . . . . . . . . . . LIG1 0.0177050971960458 0.982287160925901 7.74187805319547e-06 ligase I, DNA, ATP-dependent FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.; . . ovary;colon;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;alveolus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; testis - seminiferous tubule;testis;tumor; 0.97979 0.38753 0.36555769 74.7287096 466.53831 4.47469 LIG3 2.83467985577354e-06 0.999840866569437 0.000156298750707321 ligase III, DNA, ATP-dependent FUNCTION: Isoform 3 functions as heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand- break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. Isoform 1 is targeted to mitochondria, where it functions as DNA ligase in mitochondrial base-excision DNA repair (PubMed:10207110, PubMed:24674627). {ECO:0000269|PubMed:10207110, ECO:0000269|PubMed:24674627}.; . TISSUE SPECIFICITY: Testis, thymus, prostate and heart.; unclassifiable (Anatomical System);muscle;colon;blood;skin;skeletal muscle;bone marrow;breast;prostate;pancreas;whole body;endometrium;epididymis;nasopharynx;placenta;visual apparatus;liver;testis;cervix;spleen;germinal center;kidney;brain;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;pons;trigeminal ganglion;skeletal muscle; 0.32599 0.22247 -1.394367777 4.246284501 136.74536 2.54177 LIG4 0.0021012376555408 0.978167154243832 0.0197316081006271 ligase IV, DNA, ATP-dependent FUNCTION: Efficiently joins single-strand breaks in a double- stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA- dependent protein kinase complex DNA-PK to these DNA ends. {ECO:0000269|PubMed:10854421, ECO:0000269|PubMed:9809069}.; DISEASE: Severe combined immunodeficiency autosomal recessive T- cell-negative/B-cell-negative/NK-cell-positive with sensitivity to ionizing radiation (RSSCID) [MIM:602450]: A form of severe combined immunodeficiency, a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy with recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T- cell-mediated cellular immunity due to a defect in T-cell development. Individuals affected by RS-SCID show defects in the DNA repair machinery necessary for coding joint formation and the completion of V(D)J recombination. A subset of cells from such patients show increased radiosensitivity. {ECO:0000269|PubMed:16357942}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Testis, thymus, prostate and heart.; unclassifiable (Anatomical System);meninges;lymph node;hypothalamus;colon;parathyroid;skin;breast;pancreas;prostate;pia mater;lung;endometrium;bone;pituitary gland;hypopharynx;liver;testis;head and neck;dura mater;germinal center;kidney;brain;stomach;thymus; superior cervical ganglion;pons;trigeminal ganglion;parietal lobe; 0.40402 0.10018 -0.393118976 27.05237084 2224.18489 8.68899 LILRA1 1.53714503313697e-16 0.00086176251677758 0.999138237483222 leukocyte immunoglobulin like receptor A1 FUNCTION: May act as receptor for class I MHC antigens.; . TISSUE SPECIFICITY: Detected in monocytes and B-cells. {ECO:0000269|PubMed:9548455}.; unclassifiable (Anatomical System);blood;brain;bone marrow; whole blood;trigeminal ganglion; 0.03809 . 2.539299607 98.72021703 2966.18722 10.32448 LILRA2 6.88539478620464e-12 0.0177697011477937 0.982230298845321 leukocyte immunoglobulin like receptor A2 FUNCTION: Does not bind class I MHC antigens. {ECO:0000269|PubMed:19230061}.; . TISSUE SPECIFICITY: Expression levels are very low or not detectable on monocytes, T-cells, B-cells, dendritic cells and natural killer (NK) cells. {ECO:0000269|PubMed:9548455}.; unclassifiable (Anatomical System);testis;blood;kidney;brain;bone marrow; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;whole blood;bone marrow; 0.21687 . 3.228703513 99.37485256 778.15005 5.51910 LILRA3 0.00292535056682856 0.941785238540015 0.0552894108931565 leukocyte immunoglobulin like receptor A3 FUNCTION: Acts as soluble receptor for class I MHC antigens. Binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1 or LILRB2. Binds with high affinity to the surface of monocytes, leading to abolish LPS- induced TNF-alpha production by monocytes. {ECO:0000269|PubMed:21559424, ECO:0000269|PubMed:24085305}.; . TISSUE SPECIFICITY: Detected in B-cells, and at lower levels in natural killer (NK) cells. Detected in peripheral blood monocytes and lung. {ECO:0000269|PubMed:9278324, ECO:0000269|PubMed:9548455}.; unclassifiable (Anatomical System);thyroid;blood;head and neck;bone marrow; . 0.06888 . 3.561548721 99.50460014 1102.81114 6.34939 LILRA4 2.41242146420483e-12 0.0184479075895984 0.981552092407989 leukocyte immunoglobulin like receptor A4 FUNCTION: May act as receptor for class I MHC antigens. Ligand binding leads to the activation of eosinophils and to the release of RNASE2, IL4 and leukotriene C4. {ECO:0000269|PubMed:12529506}.; . TISSUE SPECIFICITY: Detected in eosinophils, neutrophils and monocytes. {ECO:0000269|PubMed:12529506}.; unclassifiable (Anatomical System);pancreas;lymph node;lung;bone;colon;spleen;blood;germinal center;brain;skin; . 0.04179 0.09437 0.536463361 81.06864827 445.02223 4.38966 LILRA5 4.62501414319651e-08 0.115503403356899 0.884496550392959 leukocyte immunoglobulin like receptor A5 FUNCTION: May play a role in triggering innate immune responses. Does not seem to play a role for any class I MHC antigen recognition. {ECO:0000269|PubMed:16675463}.; . TISSUE SPECIFICITY: Expressed mostly in tissues of the hematopoietic system, including bone marrow, spleen, lymph node and peripheral leukocytes. Among leukocytes, monocytes and neutrophils express the highest level. Expressed in CD14+ monocytes, but not in T-cells, B-cells or natural killer (NK) cells (at protein level). {ECO:0000269|PubMed:12393390}.; unclassifiable (Anatomical System);blood;bone marrow; superior cervical ganglion;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle; 0.07382 0.07049 -0.846787714 11.05803255 17.69999 0.61899 LILRA6 0.000155085820493477 0.872379218973555 0.127465695205951 leukocyte immunoglobulin like receptor A6 FUNCTION: May act as receptor for class I MHC antigens. {ECO:0000250}.; . . unclassifiable (Anatomical System);liver; . 0.04046 0.06599 1.888739204 97.30478887 2768.22177 9.93345 LILRB1 9.91093228638529e-06 0.985085150236259 0.0149049388314546 leukocyte immunoglobulin like receptor B1 FUNCTION: Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C and HLA-G alleles. Receptor for H301/UL18, a human cytomegalovirus class I MHC homolog. Ligand binding results in inhibitory signals and down-regulation of the immune response. Engagement of LILRB1 present on natural killer cells or T-cells by class I MHC molecules protects the target cells from lysis. Interaction with HLA-B or HLA-E leads to inhibition of the signal triggered by FCER1A and inhibits serotonin release. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions. {ECO:0000269|PubMed:11907092, ECO:0000269|PubMed:9285411, ECO:0000269|PubMed:9842885}.; . TISSUE SPECIFICITY: Expressed predominantly on B-cells and monocytes, and at lower levels on dendritic cells. Detected on a low percentage of T-cells and natural killer (NK) cells. {ECO:0000269|PubMed:9285411, ECO:0000269|PubMed:9842885}.; unclassifiable (Anatomical System);lung;cartilage;tongue;placenta;colon;blood;head and neck;kidney;germinal center;brain;bone marrow; white blood cells;whole blood; 0.10362 . 2.747042574 98.9797122 1065.62247 6.26025 LILRB2 7.82941210307178e-06 0.97937684662869 0.0206153239592069 leukocyte immunoglobulin like receptor B2 FUNCTION: Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C and HLA-G alleles. Involved in the down-regulation of the immune response and the development of tolerance. Competes with CD8A for binding to class I MHC antigens. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions. {ECO:0000269|PubMed:11875462, ECO:0000269|PubMed:12853576, ECO:0000269|PubMed:9548455, ECO:0000269|PubMed:9842885}.; . TISSUE SPECIFICITY: Expressed on monocytes and B-cells, and at lower levels on dendritic cells. Detected at low levels in natural killer (NK) cells. {ECO:0000269|PubMed:9548455, ECO:0000269|PubMed:9842885}.; unclassifiable (Anatomical System);lymph node;islets of Langerhans;colon;fovea centralis;choroid;lens;retina;uterus;pancreas;prostate;optic nerve;lung;epididymis;placenta;macula lutea;spleen;brain;mammary gland;aorta;stomach; white blood cells;whole blood;trigeminal ganglion; 0.31832 . 2.831581484 99.08586931 3895.89182 12.31761 LILRB3 0.0277606853655411 0.969891931131099 0.00234738350335964 leukocyte immunoglobulin like receptor B3 FUNCTION: May act as receptor for class I MHC antigens. Becomes activated upon coligation of LILRB3 and immune receptors, such as FCGR2B and the B-cell receptor. Down-regulates antigen-induced B- cell activation by recruiting phosphatases to its immunoreceptor tyrosine-based inhibitor motifs (ITIM). {ECO:0000250|UniProtKB:P97484}.; . TISSUE SPECIFICITY: Detected in monocytes and B-cells. {ECO:0000269|PubMed:9548455}.; unclassifiable (Anatomical System);lung;tongue;urinary;liver;colon;blood;head and neck;kidney;stomach;bone marrow; whole blood; 0.07088 . 1.756425229 96.70912951 1162.94093 6.49058 LILRB4 4.67012255733545e-08 0.374227411562693 0.625772541736081 leukocyte immunoglobulin like receptor B4 FUNCTION: Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C and HLA-G alleles. Involved in the down-regulation of the immune response and the development of tolerance, e.g. towards transplants. Interferes with TNFRSF5- signaling and NF-kappa-B up-regulation. Inhibits receptor-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions. {ECO:0000269|PubMed:11875462, ECO:0000269|PubMed:9151699}.; . TISSUE SPECIFICITY: Detected in monocytes, macrophages, dendritic cells, lung, natural killer cells and B-cells. {ECO:0000269|PubMed:9151699, ECO:0000269|PubMed:9278324, ECO:0000269|PubMed:9548455}.; unclassifiable (Anatomical System);smooth muscle;lung;ovary;endometrium;tongue;hypothalamus;placenta;colon;spleen;head and neck;kidney;brain;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07232 . 4.538441647 99.74640245 2838.35258 10.07119 LILRB5 7.17384783976138e-12 0.124265917104509 0.875734082888317 leukocyte immunoglobulin like receptor B5 FUNCTION: May act as receptor for class I MHC antigens.; . TISSUE SPECIFICITY: Detected in a natural killer (NK) cells. {ECO:0000269|PubMed:9548455}.; unclassifiable (Anatomical System);prostate;pancreas;cartilage;bone;placenta;liver;testis;spleen;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.05934 0.06828 0.786269343 87.29063458 2895.36837 10.19483 LILRP1 . . . leukocyte immunoglobulin-like receptor pseudogene 1 . . . . . 0.07088 . . . . . LILRP2 . . . leukocyte immunoglobulin-like receptor pseudogene 2 . . . . . 0.04179 . . . . . LIM2 0.000989156576930138 0.58781123540062 0.41119960802245 lens intrinsic membrane protein 2 FUNCTION: Present in the thicker 16-17 nm junctions of mammalian lens fiber cells, where it may contribute to cell junctional organization. Acts as a receptor for calmodulin. May play an important role in both lens development and cataractogenesis.; . TISSUE SPECIFICITY: Eye lens specific. {ECO:0000269|PubMed:12107413}.; whole body;lens; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.21035 0.20956 -0.53631094 20.53550366 32.81085 1.01834 LIMA1 1.28359617495965e-07 0.943007312073407 0.0569925595669752 LIM domain and actin binding 1 FUNCTION: Binds to actin monomers and filaments. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments. {ECO:0000269|PubMed:12566430}.; . TISSUE SPECIFICITY: Highly expressed in placenta, kidney, pancreas, prostate, ovary, spleen and heart. Also detected in lung, liver, brain, skeletal muscle, thymus, testis and intestine. Not detected in leukocytes. Isoform Beta expressed generally at very low levels. Isoform Alpha abundant in epithelial cells from mammary gland, prostate and in normal oral keratinocytes. Low levels in aortic endothelial cells and dermal fibroblasts. Not detectable in myocardium.; ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;testis;spinal ganglion;artery;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.19000 0.13884 -0.999300439 8.368719038 36.54684 1.09509 LIMCH1 0.999638378558411 0.000361621441288135 3.01013633614648e-13 LIM and calponin homology domains 1 . . . myocardium;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;heart;cartilage;adrenal cortex;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;developmental;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;bone;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;lung;pia mater;placenta;internal ear;hippocampus;hypopharynx;head and neck;kidney;aorta;stomach; amygdala;thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;olfactory bulb;hypothalamus;spinal cord;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.22998 0.08738 0.387604191 75.69591885 5384.20261 15.13173 LIMD1 0.127770680853122 0.871231499630751 0.0009978195161276 LIM domains containing 1 FUNCTION: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG- dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1- responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation. {ECO:0000269|PubMed:15542589, ECO:0000269|PubMed:20303269, ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:22286099}.; . TISSUE SPECIFICITY: Expressed in normal and breast cancer tissues (at protein level). Ubiquitous. {ECO:0000269|PubMed:10647888, ECO:0000269|PubMed:18712738}.; unclassifiable (Anatomical System);medulla oblongata;ovary;adrenal cortex;colon;skin;skeletal muscle;bone marrow;uterus;pancreas;whole body;lung;nasopharynx;thyroid;placenta;visual apparatus;hypopharynx;liver;testis;cervix;head and neck;spleen;germinal center;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.39532 0.09586 -0.396754488 26.97570182 86.15106 1.98183 LIMD1-AS1 . . . LIMD1 antisense RNA 1 . . . . . . . . . . . LIMD2 0.0176301694774636 0.719574233655606 0.262795596866931 LIM domain containing 2 . . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;lens;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;white blood cells;whole blood;tonsil; 0.37389 0.11262 0.147123112 64.11299835 11.52617 0.41588 LIME1 0.00033293549013144 0.368800212448147 0.630866852061721 Lck interacting transmembrane adaptor 1 FUNCTION: Involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and TCR (T-cell antigen receptor)-mediated T- cell signaling in T-cells. In absence of TCR signaling, may be involved in CD4-mediated inhibition of T-cell activation. Couples activation of these receptors and their associated kinases with distal intracellular events such as calcium mobilization or MAPK activation through the recruitment of PLCG2, GRB2, GRAP2, and other signaling molecules. {ECO:0000269|PubMed:14610046}.; . TISSUE SPECIFICITY: Expressed in peripheral blood lymphocytes, lymphoid tissues, and liver. Present in T-cells and plasma cells, and in various hematopoietic cell lines (at protein level). {ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:14610046, ECO:0000269|PubMed:16160011}.; unclassifiable (Anatomical System);heart;ovary;colon;blood;skin;uterus;pancreas;whole body;liver;cervix;spleen;kidney;brain;tonsil;stomach; . 0.10051 . . . 183.88388 2.94288 LIMK1 0.990896287164463 0.00910361771200914 9.5123527590164e-08 LIM domain kinase 1 FUNCTION: Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop. LIMK1 subsequently phosphorylates and inactivates the actin binding/depolymerizing factors cofilin-1/CFL1, cofilin- 2/CFL2 and destrin/DSTN, thereby preventing the cleavage of filamentous actin (F-actin), and stabilizing the actin cytoskeleton. In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation. Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly. Stimulates axonal outgrowth and may be involved in brain development. Isoform 3 has a dominant negative effect on actin cytoskeletal changes. Required for atypical chemokine receptor ACKR2-induced phosphorylation of cofilin (CFL1). {ECO:0000269|PubMed:10196227, ECO:0000269|PubMed:10436159, ECO:0000269|PubMed:11832213, ECO:0000269|PubMed:12807904, ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:16230460, ECO:0000269|PubMed:18028908, ECO:0000269|PubMed:23633677}.; DISEASE: Note=LIMK1 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region.; TISSUE SPECIFICITY: Highest expression in both adult and fetal nervous system. Detected ubiquitously throughout the different regions of adult brain, with highest levels in the cerebral cortex. Expressed to a lesser extent in heart and skeletal muscle.; lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;lens;lung;epididymis;adrenal gland;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland; whole brain;thalamus;temporal lobe;prefrontal cortex;globus pallidus;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.30864 0.32739 -0.821100135 11.88369899 175.30019 2.87950 LIMK2 0.00844040082440469 0.990999890294768 0.000559708880827038 LIM domain kinase 2 FUNCTION: Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro. {ECO:0000269|PubMed:10436159, ECO:0000269|PubMed:11018042}.; . TISSUE SPECIFICITY: Highest expression in the placenta; moderate level in liver, lung, kidney, and pancreas. LIMK2a is found to be more abundant then LIMK2b in liver, colon, stomach, and spleen, while in brain, kidney, and placenta LIMK2b is the dominant form. In adult lung, both LIMK2a and LIMK2b is nearly equally observed. {ECO:0000269|PubMed:8954941}.; smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;bladder;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; dorsal root ganglion;superior cervical ganglion;thyroid;placenta;spinal cord;ciliary ganglion;atrioventricular node;whole blood;trigeminal ganglion;skeletal muscle;skin; 0.26618 0.20570 0.113945049 62.14319415 767.32501 5.48678 LIMS1 0.347565207480817 0.649601345058845 0.002833447460338 LIM zinc finger domain containing 1 FUNCTION: Adapter protein in a cytoplasmic complex linking beta- integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Involved in the regulation of cell survival, cell proliferation and cell differentiation.; . TISSUE SPECIFICITY: Expressed in most tissues except in the brain.; ovary;salivary gland;intestine;colon;vein;skin;retina;uterus;prostate;whole body;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;pharynx;blood;skeletal muscle;breast;lung;placenta;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.85268 0.14897 . . 138.63474 2.56496 LIMS1-AS1 . . . LIMS1 antisense RNA 1 . . . . . . . . . . . LIMS2 1.13990016377388e-05 0.585518974714008 0.414469626284354 LIM zinc finger domain containing 2 FUNCTION: Adapter protein in a cytoplasmic complex linking beta- integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Plays a role in modulating cell spreading and migration. {ECO:0000269|PubMed:12167643}.; . . myocardium;ovary;sympathetic chain;colon;parathyroid;skin;uterus;prostate;endometrium;bone;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;lens;pancreas;lung;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; uterus;dorsal root ganglion;superior cervical ganglion;heart; 0.40061 0.11748 -0.800872469 12.33191791 54.15487 1.46813 LIMS3 . . . LIM zinc finger domain containing 3 . . TISSUE SPECIFICITY: Detected in testis. {ECO:0000269|Ref.1}.; unclassifiable (Anatomical System);uterus;prostate;smooth muscle;lung;ovary;placenta;testis;colon;brain;skin;stomach; . 0.25305 . . . . . LIMS4 . . . LIM zinc finger domain containing 4 . . . . . . . . . . . LIN7A 0.0411484963561707 0.929477752592678 0.0293737510511514 lin-7 homolog A, crumbs cell polarity complex component FUNCTION: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells. {ECO:0000269|PubMed:12967566}.; . TISSUE SPECIFICITY: Expressed in brain, testis, kidney, placenta and liver. {ECO:0000269|PubMed:11311936}.; unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;retina;optic nerve;lung;nasopharynx;macula lutea;liver;testis;spleen;kidney;mammary gland; testis - interstitial;testis - seminiferous tubule;adrenal cortex;testis;ciliary ganglion; 0.44116 0.22085 -0.163345027 41.24793583 13.24339 0.48162 LIN7B 0.838837249627908 0.160514335987946 0.000648414384145767 lin-7 homolog B, crumbs cell polarity complex component FUNCTION: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells. May increase the amplitude of ASIC3 acid-evoked currents by stabilizing the channel at the cell surface (By similarity). {ECO:0000250, ECO:0000269|PubMed:11742811}.; . . unclassifiable (Anatomical System);medulla oblongata;heart;islets of Langerhans;colon;skeletal muscle;prostate;lung;oesophagus;liver;testis;kidney;mammary gland;brain; medulla oblongata;subthalamic nucleus;temporal lobe;globus pallidus;pons;skeletal muscle; 0.26305 0.14229 -0.119252484 44.53880632 9.42202 0.34727 LIN7C 0.0300652295135779 0.924445889128026 0.0454888813583961 lin-7 homolog C, crumbs cell polarity complex component FUNCTION: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;bone;thyroid;testis;germinal center;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;cornea;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;cerebellum; amygdala;superior cervical ganglion;prefrontal cortex;trigeminal ganglion;skeletal muscle;cerebellum; 0.64364 0.15588 -0.251530012 35.42108988 17.52572 0.61515 LIN9 0.999926500458297 7.34995234040712e-05 1.82991217387044e-11 lin-9 DREAM MuvB core complex component FUNCTION: Acts as a tumor suppressor. Inhibits DNA synthesis. Its ability to inhibit oncogenic transformation is mediated through its association with RB1. Plays a role in the expression of genes required for the G1/S transition. {ECO:0000269|PubMed:15538385, ECO:0000269|PubMed:16730350}.; . TISSUE SPECIFICITY: Expressed in thymus and testis. {ECO:0000269|PubMed:15538385}.; ovary;salivary gland;intestine;colon;skin;uterus;prostate;endometrium;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;breast;lung;cornea;placenta;visual apparatus;liver;kidney;mammary gland;stomach;thymus; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.53389 0.42142 -0.492218069 22.35786742 458.30197 4.44554 LIN28A 0.196269887367842 0.757481140262298 0.0462489723698604 lin-28 homolog A FUNCTION: 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression (By similarity). Suppressor of microRNA (miRNA) biogenesis, including that of let- 7, miR107, miR-143 and miR-200c. Specifically binds miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits ZCCHC11/TUT4 uridylyltransferase. This results in the terminal uridylation of target pre-miRNAs (PubMed:19703396) (PubMed:22118463) (PubMed:22898984). Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:18951094, ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:22118463, ECO:0000269|PubMed:22898984}.; . TISSUE SPECIFICITY: Expressed in embryonic stem cells, placenta and testis. Tends to be up-regulated in HER2-overexpressing breast tumors. {ECO:0000269|PubMed:14688391, ECO:0000269|PubMed:15614775, ECO:0000269|PubMed:15722555, ECO:0000269|PubMed:22118463}.; unclassifiable (Anatomical System);ovary;placenta;brain; superior cervical ganglion; 0.92280 0.13294 -0.295622497 32.61972163 11.9347 0.43278 LIN28AP1 . . . LIN28A pseudogene 1 . . . . . . . . . . . LIN28AP2 . . . LIN28A pseudogene 2 . . . . . . . . . . . LIN28AP3 . . . LIN28A pseudogene 3 . . . . . . . . . . . LIN28B 0.721962206839986 0.275051337154342 0.00298645600567269 lin-28 homolog B FUNCTION: Suppressor of microRNA (miRNA) biogenesis, including that of let-7 and possibly of miR107, miR-143 and miR-200c. Binds primary let-7 transcripts (pri-let-7), including pri-let-7g and pri-let-7a-1, and sequester them in the nucleolus, away from the microprocessor complex, hence preventing their processing into mature miRNA (PubMed:22118463). Does not act on pri-miR21 (PubMed:22118463). The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state of embryonic stem cells by preventing let-7-mediated differentiation. When overexpressed, recruits ZCCHC11/TUT4 uridylyltransferase to pre-let-7 transcripts, leading to their terminal uridylation and degradation (PubMed:19703396). This activity might not be relevant in vivo, as LIN28B-mediated inhibition of let-7 miRNA maturation appears to be ZCCHC11- independent (PubMed:22118463). Interaction with target pre-miRNAs occurs via an 5'-GGAG-3' motif in the pre-miRNA terminal loop. Mediates MYC-induced let-7 repression (By similarity). When overexpressed, isoform 1 stimulates growth of the breast adenocarcinoma cell line MCF-7. Isoform 2 has no effect on cell growth. {ECO:0000250|UniProtKB:Q45KJ6, ECO:0000269|PubMed:16971064, ECO:0000269|PubMed:18951094, ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:22118463}.; . TISSUE SPECIFICITY: Expressed at high levels in the placenta and, at mucher lower, in testis and fetal liver (PubMed:16971064). Isoform 1 is only detected in placenta and in moderately and poorly differentiated hepatocellular carcinoma cells (at protein level). Isoform 2 is detected in fetal liver, non-tumor liver tissues, as well as well-differentiated tumor tissues (at protein level). Tends to be up-regulated in triple-negative (ER-,PR-,HER2-) breast tumors, as well as in liver, ovarian, and thyroid carcinomas (PubMed:22118463). {ECO:0000269|PubMed:16971064, ECO:0000269|PubMed:22118463}.; unclassifiable (Anatomical System);placenta;liver;spleen;kidney;skin; globus pallidus;ciliary ganglion;atrioventricular node; 0.62007 0.07116 0.03689118 56.64071715 16.34235 0.57948 LIN28B-AS1 . . . LIN28B antisense RNA 1 . . . . . . . . . . . LIN37 0.356935099324916 0.640430474542356 0.00263442613272731 lin-37 DREAM MuvB core complex component . . . unclassifiable (Anatomical System);heart;ovary;colon;blood;retina;breast;uterus;lung;bone;placenta;visual apparatus;liver;testis;spleen;kidney;brain;pineal gland;tonsil; dorsal root ganglion; 0.10138 0.12671 . . 118.47374 2.36865 LIN52 0.891966387273143 0.106942485935398 0.00109112679145873 lin-52 DREAM MuvB core complex component . . . . . 0.55600 0.12971 0.147123112 64.11299835 27.62583 0.88836 LIN54 0.999433598501497 0.000566400962684108 5.35819090223508e-10 lin-54 DREAM MuvB core complex component FUNCTION: Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In G0 phase, the complex binds to more than 800 promoters and is required for repression of E2F target genes. In S phase, the complex selectively binds to the promoters of G2/M genes whose products are required for mitosis and participates in their cell cycle dependent activation. In the complex, acts as a DNA-binding protein that binds the promoter of CDK1 in a sequence-specific manner.; . . unclassifiable (Anatomical System);medulla oblongata;islets of Langerhans;colon;blood;skin;bone marrow;breast;lung;cerebral cortex;endometrium;nasopharynx;thyroid;placenta;liver;testis;germinal center;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;temporal lobe;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15443 0.09114 -0.53631094 20.53550366 49.60061 1.37875 LINC-PINT . . . long intergenic non-protein coding RNA, p53 induced transcript . . . . . . . . . . . LINC-ROR . . . long intergenic non-protein coding RNA, regulator of reprogramming . . . . . . . . . . . LINC00028 . . . long intergenic non-protein coding RNA 28 . . . . . . . . . . . LINC00029 . . . long intergenic non-protein coding RNA 29 . . . . . 0.09319 . . . . . LINC00032 . . . long intergenic non-protein coding RNA 32 . . . . . . . . . . . LINC00051 . . . long intergenic non-protein coding RNA 51 . . . . . . . . . . . LINC00052 . . . long intergenic non-protein coding RNA 52 . . . . . 0.11103 . . . . . LINC00083 . . . long intergenic non-protein coding RNA 83 . . . . . . . . . . . LINC00092 . . . long intergenic non-protein coding RNA 92 . . . . . . . . . . . LINC00094 . . . long intergenic non-protein coding RNA 94 . . . . . . . . . . . LINC00102 . . . long intergenic non-protein coding RNA 102 . . . . . . . . . . . LINC00106 . . . long intergenic non-protein coding RNA 106 . . . . . . . . . . . LINC00111 . . . long intergenic non-protein coding RNA 111 . . . . . . . . . . . LINC00112 . . . long intergenic non-protein coding RNA 112 . . . . . . . . . . . LINC00113 . . . long intergenic non-protein coding RNA 113 . . . . . . . . . . . LINC00114 . . . long intergenic non-protein coding RNA 114 . . TISSUE SPECIFICITY: Expressed in a range of cell lines, including B-cell lymphoma and prostate. {ECO:0000269|PubMed:14693372}.; . . . . . . . . LINC00115 . . . long intergenic non-protein coding RNA 115 . . . . . . . . . . . LINC00116 . . . long intergenic non-protein coding RNA 116 . . . . . . . . . . . LINC00152 . . . long intergenic non-protein coding RNA 152 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; . 0.07288 . . . . . LINC00158 . . . long intergenic non-protein coding RNA 158 . . TISSUE SPECIFICITY: Expressed in fetal brain.; brain; . 0.07971 . . . . . LINC00159 . . . long intergenic non-protein coding RNA 159 . . . . . . . . . . . LINC00160 . . . long intergenic non-protein coding RNA 160 . . . . . . . . . . . LINC00161 . . . long intergenic non-protein coding RNA 161 . . . . . . . . . . . LINC00162 . . . long intergenic non-protein coding RNA 162 . . TISSUE SPECIFICITY: Detected in spleen, pancreas, hypothalamus, brain, sperm and lung. {ECO:0000269|PubMed:16826516}.; . . . . . . . . LINC00163 . . . long intergenic non-protein coding RNA 163 . . . . . . . . . . . LINC00165 . . . long intergenic non-protein coding RNA 165 . . . . . . . . . . . LINC00167 . . . long intergenic non-protein coding RNA 167 . . . . . . . . . . . LINC00173 . . . long intergenic non-protein coding RNA 173 . . . . . . . . . . . LINC00174 . . . long intergenic non-protein coding RNA 174 . . . . . . . . . . . LINC00176 . . . long intergenic non-protein coding RNA 176 . . . unclassifiable (Anatomical System);optic nerve;ovary;placenta;parathyroid; . 0.08825 . . . . . LINC00184 . . . long intergenic non-protein coding RNA 184 . . . . . . . . . . . LINC00189 . . . long intergenic non-protein coding RNA 189 . . . . . . . . . . . LINC00200 . . . long intergenic non-protein coding RNA 200 . . . . . . . . . . . LINC00202-1 . . . long intergenic non-protein coding RNA 202-1 . . . . . . . . . . . LINC00202-2 . . . long intergenic non-protein coding RNA 202-2 . . . . . . . . . . . LINC00205 . . . long intergenic non-protein coding RNA 205 . . TISSUE SPECIFICITY: Expressed in the thymus, skeletal muscle and trachea.; . . . . . . . . LINC00207 . . . long intergenic non-protein coding RNA 207 . . . testis; . . . . . . . LINC00208 . . . long intergenic non-protein coding RNA 208 . . . testis; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.07231 . . . . . LINC00210 . . . long intergenic non-protein coding RNA 210 . . . . . . . . . . . LINC00211 . . . long intergenic non-protein coding RNA 211 . . . . . . . . . . . LINC00216 . . . long intergenic non-protein coding RNA 216 . . . . . . . . . . . LINC00221 . . . long intergenic non-protein coding RNA 221 . . . . . . . . . . . LINC00222 . . . long intergenic non-protein coding RNA 222 . . . . . . . . . . . LINC00226 . . . long intergenic non-protein coding RNA 226 . . . . . . . . . . . LINC00229 . . . long intergenic non-protein coding RNA 229 . . . . . . . . . . . LINC00235 . . . long intergenic non-protein coding RNA 235 . . . . . . . . . . . LINC00237 . . . long intergenic non-protein coding RNA 237 . . . . . . . . . . . LINC00238 . . . long intergenic non-protein coding RNA 238 . . . unclassifiable (Anatomical System);lung;liver;testis; . 0.21849 . . . . . LINC00239 . . . long intergenic non-protein coding RNA 239 . . . . . . . . . . . LINC00240 . . . long intergenic non-protein coding RNA 240 . . . . . . . . . . . LINC00242 . . . long intergenic non-protein coding RNA 242 . . . . . . . . . . . LINC00243 . . . long intergenic non-protein coding RNA 243 . . . . . . . . . . . LINC00244 . . . long intergenic non-protein coding RNA 244 . . . . . . . . . . . LINC00251 . . . long intergenic non-protein coding RNA 251 . . . . . . . . . . . LINC00254 . . . long intergenic non-protein coding RNA 254 . . . . . . . . . . . LINC00260 . . . long intergenic non-protein coding RNA 260 . . . . . . . . . . . LINC00261 . . . long intergenic non-protein coding RNA 261 . . . . . . . . . . . LINC00264 . . . long intergenic non-protein coding RNA 264 . . . . . . . . . . . LINC00265 . . . long intergenic non-protein coding RNA 265 . . . unclassifiable (Anatomical System);colon;blood;retina;bone marrow;uterus;prostate;lung;frontal lobe;placenta;testis;germinal center;kidney;mammary gland;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . . . . . LINC00265-2P . . . long intergenic non-protein coding RNA 265-2, pseudogene . . . . . . . . . . . LINC00265-3P . . . long intergenic non-protein coding RNA 265-3, pseudogene . . . . . . . . . . . LINC00266-1 . . . long intergenic non-protein coding RNA 266-1 . . . tongue;islets of Langerhans;larynx;cervix;head and neck;kidney; . . . . . . . LINC00266-2P . . . long intergenic non-protein coding RNA 266-2, pseudogene . . . . . . . . . . . LINC00266-3 . . . long intergenic non-protein coding RNA 266-3 . . . . . . . . . . . LINC00266-4P . . . long intergenic non-protein coding RNA 266-4, pseudogene . . . . . . . . . . . LINC00268 . . . long intergenic non-protein coding RNA 268 . . . . . . . . . . . LINC00268-2P . . . long intergenic non-protein coding RNA 268-2, pseudogene . . . . . . . . . . . LINC00269 . . . long intergenic non-protein coding RNA 269 . . . . . 0.43899 . . . . . LINC00271 . . . long intergenic non-protein coding RNA 271 . . . . . . . . . . . LINC00272 . . . long intergenic non-protein coding RNA 272 . . . . . 0.05596 . . . . . LINC00273 . . . long intergenic non-protein coding RNA 273 . . . . . . . . . . . LINC00276 . . . long intergenic non-protein coding RNA 276 . . . . . . . . . . . LINC00278 . . . long intergenic non-protein coding RNA 278 . . . . . . . . . . . LINC00279 . . . long intergenic non-protein coding RNA 279 . . . . . . . . . . . LINC00280 . . . long intergenic non-protein coding RNA 280 . . . . . . . . . . . LINC00282 . . . long intergenic non-protein coding RNA 282 . . . . . . . . . . . LINC00283 . . . long intergenic non-protein coding RNA 283 . . . . . . . . . . . LINC00284 . . . long intergenic non-protein coding RNA 284 . . . . . . . . . . . LINC00290 . . . long intergenic non-protein coding RNA 290 . . . . . . . . . . . LINC00293 . . . long intergenic non-protein coding RNA 293 . . . . . . . . . . . LINC00294 . . . long intergenic non-protein coding RNA 294 . . . . . . . . . . . LINC00297 . . . long intergenic non-protein coding RNA 297 . . . . . . . . . . . LINC00298 . . . long intergenic non-protein coding RNA 298 . . . . . . . . . . . LINC00299 . . . long intergenic non-protein coding RNA 299 . . . . . . . . . . . LINC00301 . . . long intergenic non-protein coding RNA 301 . . . testis; . 0.06248 . . . . . LINC00302 . . . long intergenic non-protein coding RNA 302 . . . . . 0.29738 . . . . . LINC00303 . . . long intergenic non-protein coding RNA 303 . . . . . 0.06237 . . . . . LINC00304 . . . long intergenic non-protein coding RNA 304 . . . . . 0.11268 . . . . . LINC00305 . . . long intergenic non-protein coding RNA 305 . . . . . 0.06408 0.05838 . . . . LINC00307 . . . long intergenic non-protein coding RNA 307 . . . . . . . . . . . LINC00308 . . . long intergenic non-protein coding RNA 308 . . TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:12036298}.; . . 0.04068 . . . . . LINC00309 . . . long intergenic non-protein coding RNA 309 . . . . . . . . . . . LINC00310 . . . long intergenic non-protein coding RNA 310 . . TISSUE SPECIFICITY: Widely expressed; not found in breast. {ECO:0000269|PubMed:12036297}.; . . . . . . . . LINC00311 . . . long intergenic non-protein coding RNA 311 . . . . . 0.08673 . . . . . LINC00312 . . . long intergenic non-protein coding RNA 312 . . . . . . . . . . . LINC00313 . . . long intergenic non-protein coding RNA 313 . . TISSUE SPECIFICITY: Widely expressed; not found in heart and in muscle.; prostate;lung;pituitary gland;testis; ciliary ganglion; 0.10998 . . . . . LINC00314 . . . long intergenic non-protein coding RNA 314 . . . prostate; . 0.18504 . . . . . LINC00315 . . . long intergenic non-protein coding RNA 315 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12036297}.; . . 0.22277 . . . . . LINC00316 . . . long intergenic non-protein coding RNA 316 . . . . . . . . . . . LINC00317 . . . long intergenic non-protein coding RNA 317 . . . . . . . . . . . LINC00319 . . . long intergenic non-protein coding RNA 319 . . . unclassifiable (Anatomical System);lung;colon;skeletal muscle;stomach; . 0.08324 . . . . . LINC00320 . . . long intergenic non-protein coding RNA 320 . . . . . . . . . . . LINC00322 . . . long intergenic non-protein coding RNA 322 . . . . . . . . . . . LINC00323 . . . long intergenic non-protein coding RNA 323 . . . . . . . . . . . LINC00324 . . . long intergenic non-protein coding RNA 324 . . . unclassifiable (Anatomical System);heart;islets of Langerhans;fovea centralis;choroid;lens;skin;retina;optic nerve;lung;nasopharynx;macula lutea;testis;germinal center;brain; . 0.11213 . . . . . LINC00326 . . . long intergenic non-protein coding RNA 326 . . . . . . . . . . . LINC00327 . . . long intergenic non-protein coding RNA 327 . . . . . . . . . . . LINC00328 . . . long intergenic non-protein coding RNA 328 . . . . . . . . . . . LINC00328-2P . . . long intergenic non-protein coding RNA 328-2, pseudogene . . . . . . . . . . . LINC00330 . . . long intergenic non-protein coding RNA 330 . . . . . . . . . . . LINC00331 . . . long intergenic non-protein coding RNA 331 . . . . . . . . . . . LINC00332 . . . long intergenic non-protein coding RNA 332 . . . . . . . . . . . LINC00333 . . . long intergenic non-protein coding RNA 333 . . . . . . . . . . . LINC00334 . . . long intergenic non-protein coding RNA 334 . . . unclassifiable (Anatomical System);optic nerve;lung;visual apparatus;colon; . 0.14679 . . . . . LINC00336 . . . long intergenic non-protein coding RNA 336 . . . . . . . . . . . LINC00337 . . . long intergenic non-protein coding RNA 337 . . . . . . . . . . . LINC00339 . . . long intergenic non-protein coding RNA 339 . . . . . . . . . . . LINC00341 . . . long intergenic non-protein coding RNA 341 . . . . . . . . . . . LINC00342 . . . long intergenic non-protein coding RNA 342 . . . . . . . . . . . LINC00343 . . . long intergenic non-protein coding RNA 343 . . . . . . . . . . . LINC00345 . . . long intergenic non-protein coding RNA 345 . . . . . . . . . . . LINC00346 . . . long intergenic non-protein coding RNA 346 . . . . . . . . . 328.50602 3.85367 LINC00347 . . . long intergenic non-protein coding RNA 347 . . . . . . . . . . . LINC00348 . . . long intergenic non-protein coding RNA 348 . . . . . . . . . . . LINC00349 . . . long intergenic non-protein coding RNA 349 . . . . . . . . . . . LINC00350 . . . long intergenic non-protein coding RNA 350 . . . . . . . . . . . LINC00351 . . . long intergenic non-protein coding RNA 351 . . . . . . . . . . . LINC00352 . . . long intergenic non-protein coding RNA 352 . . . . . . . . . . . LINC00353 . . . long intergenic non-protein coding RNA 353 . . . . . . . . . . . LINC00354 . . . long intergenic non-protein coding RNA 354 . . . . . . . . . . . LINC00355 . . . long intergenic non-protein coding RNA 355 . . . . . . . . . . . LINC00358 . . . long intergenic non-protein coding RNA 358 . . . . . . . . . . . LINC00359 . . . long intergenic non-protein coding RNA 359 . . . . . . . . . . . LINC00362 . . . long intergenic non-protein coding RNA 362 . . . . . . . . . . . LINC00363 . . . long intergenic non-protein coding RNA 363 . . . . . . . . . . . LINC00364 . . . long intergenic non-protein coding RNA 364 . . . . . . . . . . . LINC00365 . . . long intergenic non-protein coding RNA 365 . . . . . . . . . . . LINC00366 . . . long intergenic non-protein coding RNA 366 . . . . . . . . . . . LINC00367 . . . long intergenic non-protein coding RNA 367 . . . . . . . . . . . LINC00368 . . . long intergenic non-protein coding RNA 368 . . . . . . . . . . . LINC00370 . . . long intergenic non-protein coding RNA 370 . . . . . . . . . . . LINC00371 . . . long intergenic non-protein coding RNA 371 . . . . . . . . . . . LINC00374 . . . long intergenic non-protein coding RNA 374 . . . . . . . . . . . LINC00375 . . . long intergenic non-protein coding RNA 375 . . . . . . . . . . . LINC00376 . . . long intergenic non-protein coding RNA 376 . . . . . . . . . . . LINC00377 . . . long intergenic non-protein coding RNA 377 . . . . . . . . . . . LINC00378 . . . long intergenic non-protein coding RNA 378 . . . . . . . . . . . LINC00379 . . . long intergenic non-protein coding RNA 379 . . . . . . . . . . . LINC00380 . . . long intergenic non-protein coding RNA 380 . . . . . . . . . . . LINC00381 . . . long intergenic non-protein coding RNA 381 . . . . . . . . . . . LINC00382 . . . long intergenic non-protein coding RNA 382 . . . . . . . . . . . LINC00383 . . . long intergenic non-protein coding RNA 383 . . . . . . . . . . . LINC00384 . . . long intergenic non-protein coding RNA 384 . . . . . . . . . . . LINC00385 . . . long intergenic non-protein coding RNA 385 . . . . . . . . . . . LINC00387 . . . long intergenic non-protein coding RNA 387 . . . . . . . . . . . LINC00388 . . . long intergenic non-protein coding RNA 388 . . . . . . . . . . . LINC00390 . . . long intergenic non-protein coding RNA 390 . . . . . . . . . . . LINC00391 . . . long intergenic non-protein coding RNA 391 . . . . . . . . . . . LINC00392 . . . long intergenic non-protein coding RNA 392 . . . . . . . . . . . LINC00393 . . . long intergenic non-protein coding RNA 393 . . . . . . . . . . . LINC00395 . . . long intergenic non-protein coding RNA 395 . . . . . . . . . . . LINC00396 . . . long intergenic non-protein coding RNA 396 . . . . . . . . . . . LINC00397 . . . long intergenic non-protein coding RNA 397 . . . . . . . . . . . LINC00398 . . . long intergenic non-protein coding RNA 398 . . . . . . . . . . . LINC00399 . . . long intergenic non-protein coding RNA 399 . . . . . . . . . . . LINC00400 . . . long intergenic non-protein coding RNA 400 . . . . . . . . . . . LINC00402 . . . long intergenic non-protein coding RNA 402 . . . . . . . . . . . LINC00403 . . . long intergenic non-protein coding RNA 403 . . . . . . . . . . . LINC00404 . . . long intergenic non-protein coding RNA 404 . . . . . . . . . . . LINC00407 . . . long intergenic non-protein coding RNA 407 . . . . . . . . . . . LINC00408 . . . long intergenic non-protein coding RNA 408 . . . . . . . . . . . LINC00410 . . . long intergenic non-protein coding RNA 410 . . . . . . . . . . . LINC00411 . . . long intergenic non-protein coding RNA 411 . . . . . . . . . . . LINC00412 . . . long intergenic non-protein coding RNA 412 . . . . . . . . . . . LINC00415 . . . long intergenic non-protein coding RNA 415 . . . . . . . . . . . LINC00421 . . . long intergenic non-protein coding RNA 421 . . . . . . . . . . . LINC00423 . . . long intergenic non-protein coding RNA 423 . . . . . . . . . . . LINC00424 . . . long intergenic non-protein coding RNA 424 . . . . . . . . . . . LINC00426 . . . long intergenic non-protein coding RNA 426 . . . . . . . . . . . LINC00427 . . . long intergenic non-protein coding RNA 427 . . . . . . . . . . . LINC00428 . . . long intergenic non-protein coding RNA 428 . . . . . . . . . . . LINC00430 . . . long intergenic non-protein coding RNA 430 . . . . . . . . . . . LINC00431 . . . long intergenic non-protein coding RNA 431 . . . . . . . . . . . LINC00433 . . . long intergenic non-protein coding RNA 433 . . . . . . . . . . . LINC00434 . . . long intergenic non-protein coding RNA 434 . . . . . . . . . . . LINC00437 . . . long intergenic non-protein coding RNA 437 . . . . . . . . . . . LINC00440 . . . long intergenic non-protein coding RNA 440 . . . . . . . . . . . LINC00441 . . . long intergenic non-protein coding RNA 441 . . . . . . . . . . . LINC00442 . . . long intergenic non-protein coding RNA 442 . . . . . . . . . . . LINC00443 . . . long intergenic non-protein coding RNA 443 . . . . . . . . . . . LINC00444 . . . long intergenic non-protein coding RNA 444 . . . . . . . . . . . LINC00445 . . . long intergenic non-protein coding RNA 445 . . . . . . . . . . . LINC00446 . . . long intergenic non-protein coding RNA 446 . . . . . . . . . . . LINC00448 . . . long intergenic non-protein coding RNA 448 . . . . . . . . . . . LINC00449 . . . long intergenic non-protein coding RNA 449 . . . . . . . . . . . LINC00452 . . . long intergenic non-protein coding RNA 452 . . . . . . . . . . . LINC00454 . . . long intergenic non-protein coding RNA 454 . . . . . . . . . . . LINC00456 . . . long intergenic non-protein coding RNA 456 . . . . . . . . . . . LINC00457 . . . long intergenic non-protein coding RNA 457 . . . . . . . . . . . LINC00458 . . . long intergenic non-protein coding RNA 458 . . . . . . . . . . . LINC00459 . . . long intergenic non-protein coding RNA 459 . . . . . . . . . . . LINC00460 . . . long intergenic non-protein coding RNA 460 . . . . . . . . . . . LINC00461 . . . long intergenic non-protein coding RNA 461 . . . . . . . . . . . LINC00462 . . . long intergenic non-protein coding RNA 462 . . . . . . . . . . . LINC00463 . . . long intergenic non-protein coding RNA 463 . . . . . . . . . . . LINC00466 . . . long intergenic non-protein coding RNA 466 . . . . . . . . . . . LINC00467 . . . long intergenic non-protein coding RNA 467 . . . . . 0.05100 . . . . . LINC00469 . . . long intergenic non-protein coding RNA 469 . . . . . 0.12168 . . . . . LINC00470 . . . long intergenic non-protein coding RNA 470 . . TISSUE SPECIFICITY: Retina-specific. {ECO:0000269|PubMed:11173868}.; lung;placenta;testis; . 0.11336 . . . . . LINC00471 . . . long intergenic non-protein coding RNA 471 . . . unclassifiable (Anatomical System);tongue;hippocampus; . 0.12385 . . . . . LINC00472 . . . long intergenic non-protein coding RNA 472 . . . . . . . . . . . LINC00473 . . . long intergenic non-protein coding RNA 473 FUNCTION: May play a role in cAMP-mediated gene transcription. {ECO:0000269|PubMed:22108211}.; . . . . . . . . . . LINC00474 . . . long intergenic non-protein coding RNA 474 . . . . . 0.40374 . . . . . LINC00475 . . . long intergenic non-protein coding RNA 475 . . . . . . . . . . . LINC00476 . . . long intergenic non-protein coding RNA 476 . . . unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;colon;prostate;optic nerve;lung;adrenal gland;nasopharynx;testis;head and neck;kidney;stomach; . 0.08253 . . . . . LINC00477 . . . long intergenic non-protein coding RNA 477 . . . . . . . . . . . LINC00479 . . . long intergenic non-protein coding RNA 479 . . . . . . . . . . . LINC00482 . . . long intergenic non-protein coding RNA 482 . . . ovary;bone;placenta;colon;parathyroid;kidney;stomach; . 0.32693 . . . . . LINC00483 . . . long intergenic non-protein coding RNA 483 . . . colon;stomach; . 0.11962 . . . . . LINC00484 . . . long intergenic non-protein coding RNA 484 . . . . . . . . . . . LINC00485 . . . long intergenic non-protein coding RNA 485 . . . . . . . . . . . LINC00486 . . . long intergenic non-protein coding RNA 486 . . . . . . . . . . . LINC00487 . . . long intergenic non-protein coding RNA 487 . . . . . . . . . . . LINC00488 . . . long intergenic non-protein coding RNA 488 . . . . . 0.06971 . . . . . LINC00489 . . . long intergenic non-protein coding RNA 489 . . . . . . . . . . . LINC00491 . . . long intergenic non-protein coding RNA 491 . . . . . . . . . . . LINC00492 . . . long intergenic non-protein coding RNA 492 . . . . . . . . . . . LINC00493 . . . long intergenic non-protein coding RNA 493 . . . . . . . . . . . LINC00494 . . . long intergenic non-protein coding RNA 494 . . . . . . . . . . . LINC00498 . . . long intergenic non-protein coding RNA 498 . . . . . . . . . . . LINC00499 . . . long intergenic non-protein coding RNA 499 . . . . . . . . . . . LINC00500 . . . long intergenic non-protein coding RNA 500 . . . . . . . . . . . LINC00501 . . . long intergenic non-protein coding RNA 501 . . . . . . . . . . . LINC00502 . . . long intergenic non-protein coding RNA 502 . . . . . . . . . . . LINC00504 . . . long intergenic non-protein coding RNA 504 . . . . . . . . . . . LINC00505 . . . long intergenic non-protein coding RNA 505 . . . . . . . . . . . LINC00506 . . . long intergenic non-protein coding RNA 506 . . . . . . . . . . . LINC00507 . . . long intergenic non-protein coding RNA 507 . . . . . . . . . . . LINC00508 . . . long intergenic non-protein coding RNA 508 . . . . . . . . . . . LINC00511 . . . long intergenic non-protein coding RNA 511 . . . . . . . . . . . LINC00514 . . . long intergenic non-protein coding RNA 514 . . . . . . . . . . . LINC00515 . . . long intergenic non-protein coding RNA 515 . . . . . . . . . . . LINC00517 . . . long intergenic non-protein coding RNA 517 . . . . . . . . . . . LINC00518 . . . long intergenic non-protein coding RNA 518 . . . . . 0.05537 . . . . . LINC00519 . . . long intergenic non-protein coding RNA 519 . . . . . . . . . . . LINC00520 . . . long intergenic non-protein coding RNA 520 . . . . . . . . . . . LINC00521 . . . long intergenic non-protein coding RNA 521 . . . testis; . 0.07780 . . . . . LINC00523 . . . long intergenic non-protein coding RNA 523 . . . uterus;placenta; . 0.10090 . . . . . LINC00524 . . . long intergenic non-protein coding RNA 524 . . . . . . . . . . . LINC00525 . . . long intergenic non-protein coding RNA 525 . . . . . . . . . . . LINC00526 . . . long intergenic non-protein coding RNA 526 . . . . . . . . . . . LINC00527 . . . long intergenic non-protein coding RNA 527 . . . . . . . . . . . LINC00528 . . . long intergenic non-protein coding RNA 528 . . . . . . . . . . . LINC00529 . . . long intergenic non-protein coding RNA 529 . . . . . . . . . . . LINC00533 . . . long intergenic non-protein coding RNA 533 . . . . . . . . . . . LINC00534 . . . long intergenic non-protein coding RNA 534 . . . . . . . . . . . LINC00535 . . . long intergenic non-protein coding RNA 535 . . . . . . . . . . . LINC00536 . . . long intergenic non-protein coding RNA 536 . . . . . . . . . . . LINC00537 . . . long intergenic non-protein coding RNA 537 . . . . . . . . . . . LINC00538 . . . long intergenic non-protein coding RNA 538 . . . . . . . . . . . LINC00539 . . . long intergenic non-protein coding RNA 539 . . . . . . . . . . . LINC00540 . . . long intergenic non-protein coding RNA 540 . . . . . . . . . . . LINC00543 . . . long intergenic non-protein coding RNA 543 . . . . . . . . . . . LINC00544 . . . long intergenic non-protein coding RNA 544 . . . . . . . . . . . LINC00545 . . . long intergenic non-protein coding RNA 545 . . . . . . . . . . . LINC00547 . . . long intergenic non-protein coding RNA 547 . . . . . . . . . . . LINC00548 . . . long intergenic non-protein coding RNA 548 . . . . . . . . . . . LINC00550 . . . long intergenic non-protein coding RNA 550 . . . . . . . . . . . LINC00551 . . . long intergenic non-protein coding RNA 551 . . . . . . . . . . . LINC00552 . . . long intergenic non-protein coding RNA 552 . . . . . . . . . . . LINC00554 . . . long intergenic non-protein coding RNA 554 . . . . . . . . . . . LINC00555 . . . long intergenic non-protein coding RNA 555 . . . . . . . . . . . LINC00556 . . . long intergenic non-protein coding RNA 556 . . . . . . . . . . . LINC00557 . . . long intergenic non-protein coding RNA 557 . . . . . . . . . . . LINC00558 . . . long intergenic non-protein coding RNA 558 . . . . . . . . . . . LINC00559 . . . long intergenic non-protein coding RNA 559 . . . . . . . . . . . LINC00560 . . . long intergenic non-protein coding RNA 560 . . . . . . . . . . . LINC00561 . . . long intergenic non-protein coding RNA 561 . . . . . . . . . . . LINC00562 . . . long intergenic non-protein coding RNA 562 . . . . . . . . . . . LINC00563 . . . long intergenic non-protein coding RNA 563 . . . . . . . . . . . LINC00564 . . . long intergenic non-protein coding RNA 564 . . . . . . . . . . . LINC00565 . . . long intergenic non-protein coding RNA 565 . . . . . . . . . . . LINC00566 . . . long intergenic non-protein coding RNA 566 . . . . . . . . . . . LINC00567 . . . long intergenic non-protein coding RNA 567 . . . . . . . . . . . LINC00570 . . . long intergenic non-protein coding RNA 570 . . . . . . . . . . . LINC00571 . . . long intergenic non-protein coding RNA 571 . . . . . . . . . . . LINC00572 . . . long intergenic non-protein coding RNA 572 . . . . . . . . . . . LINC00574 . . . long intergenic non-protein coding RNA 574 . . . . . . . . . . . LINC00575 . . . long intergenic non-protein coding RNA 575 . . TISSUE SPECIFICITY: Specifically expressed in retina and retinal pigment epithelium. {ECO:0000269|PubMed:15218245}.; . . . . . . . . LINC00578 . . . long intergenic non-protein coding RNA 578 . . . . . . . . . . . LINC00581 . . . long intergenic non-protein coding RNA 581 . . . . . . . . . . . LINC00582 . . . long intergenic non-protein coding RNA 582 . . . . . . . . . . . LINC00583 . . . long intergenic non-protein coding RNA 583 . . . . . 0.09986 . . . . . LINC00587 . . . long intergenic non-protein coding RNA 587 . . . . . 0.08908 . . . . . LINC00588 . . . long intergenic non-protein coding RNA 588 . . . . . 0.09645 . . . . . LINC00589 . . . long intergenic non-protein coding RNA 589 . . . . . . . . . . . LINC00592 . . . long intergenic non-protein coding RNA 592 . . . . . . . . . . . LINC00593 . . . long intergenic non-protein coding RNA 593 . . . . . . . . . . . LINC00594 . . . long intergenic non-protein coding RNA 594 . . . . . . . . . . . LINC00595 . . . long intergenic non-protein coding RNA 595 . . . . . . . . . . . LINC00596 . . . long intergenic non-protein coding RNA 596 . . . . . 0.04605 . . . . . LINC00597 . . . long intergenic non-protein coding RNA 597 . . TISSUE SPECIFICITY: Expressed in heart. {ECO:0000269|PubMed:11697146}.; . . . . . . . . LINC00598 . . . long intergenic non-protein coding RNA 598 FUNCTION: Catalyzes the post-translational addition of a tyrosine to the C-terminal end of detyrosinated alpha-tubulin. {ECO:0000250}.; . . . . 0.22088 0.14529 -0.071520315 48.34866714 . . LINC00599 . . . long intergenic non-protein coding RNA 599 . . . . . . . . . . . LINC00601 . . . long intergenic non-protein coding RNA 601 . . . . . . . . . . . LINC00602 . . . long intergenic non-protein coding RNA 602 . . . . . . . . . . . LINC00603 . . . long intergenic non-protein coding RNA 603 . . . . . . . . . . . LINC00604 . . . long intergenic non-protein coding RNA 604 . . . . . . . . . . . LINC00605 . . . long intergenic non-protein coding RNA 605 . . . . . . . . . . . LINC00606 . . . long intergenic non-protein coding RNA 606 . . . . . . . . . . . LINC00607 . . . long intergenic non-protein coding RNA 607 . . . . . . . . . . . LINC00608 . . . long intergenic non-protein coding RNA 608 . . . . . . . . . . . LINC00609 . . . long intergenic non-protein coding RNA 609 . . . . . . . . . . . LINC00610 . . . long intergenic non-protein coding RNA 610 . . . . . 0.07518 . . . . . LINC00612 . . . long intergenic non-protein coding RNA 612 . . . . . 0.14644 . . . . . LINC00613 . . . long intergenic non-protein coding RNA 613 . . . . . . . . . . . LINC00614 . . . long intergenic non-protein coding RNA 614 . . . . . . . . . . . LINC00615 . . . long intergenic non-protein coding RNA 615 . . . . . 0.06168 . . . . . LINC00616 . . . long intergenic non-protein coding RNA 616 . . . . . . . . . . . LINC00618 . . . long intergenic non-protein coding RNA 618 . . . . . . . . . . . LINC00619 . . . long intergenic non-protein coding RNA 619 . . . . . 0.15016 . . . . . LINC00620 . . . long intergenic non-protein coding RNA 620 . . . . . . . . . . . LINC00621 . . . long intergenic non-protein coding RNA 621 . . . . . . . . . . . LINC00622 . . . long intergenic non-protein coding RNA 622 . . . . . . . . . . . LINC00623 . . . long intergenic non-protein coding RNA 623 . . . . . . . . . . . LINC00624 . . . long intergenic non-protein coding RNA 624 . . . . . . . . . . . LINC00626 . . . long intergenic non-protein coding RNA 626 . . . . . . . . . . . LINC00628 . . . long intergenic non-protein coding RNA 628 . . . . . . . . . . . LINC00629 . . . long intergenic non-protein coding RNA 629 . . . . . . . . . . . LINC00630 . . . long intergenic non-protein coding RNA 630 . . . . . . . . . . . LINC00632 . . . long intergenic non-protein coding RNA 632 . . . . . . . . . 7.76113 0.28612 LINC00633 . . . long intergenic non-protein coding RNA 633 . . . . . . . . . . . LINC00634 . . . long intergenic non-protein coding RNA 634 . . . . . . . . . . . LINC00635 . . . long intergenic non-protein coding RNA 635 . . . . . . . . . . . LINC00636 . . . long intergenic non-protein coding RNA 636 . . . . . . . . . . . LINC00637 . . . long intergenic non-protein coding RNA 637 . . . . . . . . . . . LINC00638 . . . long intergenic non-protein coding RNA 638 . . . . . . . . . . . LINC00639 . . . long intergenic non-protein coding RNA 639 . . . . . . . . . . . LINC00640 . . . long intergenic non-protein coding RNA 640 . . . . . . . . . . . LINC00641 . . . long intergenic non-protein coding RNA 641 . . . . . . . . . . . LINC00642 . . . long intergenic non-protein coding RNA 642 . . . . . . . . . . . LINC00643 . . . long intergenic non-protein coding RNA 643 . . . . . . . . . . . LINC00644 . . . long intergenic non-protein coding RNA 644 . . . . . . . . . . . LINC00645 . . . long intergenic non-protein coding RNA 645 . . . . . . . . . . . LINC00648 . . . long intergenic non-protein coding RNA 648 . . . . . . . . . . . LINC00649 . . . long intergenic non-protein coding RNA 649 . . . . . . . . . . . LINC00652 . . . long intergenic non-protein coding RNA 652 . . . . . . . . . . . LINC00654 . . . long intergenic non-protein coding RNA 654 . . . . . . . . . . . LINC00656 . . . long intergenic non-protein coding RNA 656 . . . . . . . . . . . LINC00658 . . . long intergenic non-protein coding RNA 658 . . . . . . . . . . . LINC00659 . . . long intergenic non-protein coding RNA 659 . . . . . . . . . . . LINC00661 . . . long intergenic non-protein coding RNA 661 . . . . . . . . . . . LINC00662 . . . long intergenic non-protein coding RNA 662 . . . . . . . . . . . LINC00663 . . . long intergenic non-protein coding RNA 663 . . . . . . . . . . . LINC00664 . . . long intergenic non-protein coding RNA 664 . . . . . . . . . . . LINC00665 . . . long intergenic non-protein coding RNA 665 . . . . . . . . . . . LINC00667 . . . long intergenic non-protein coding RNA 667 . . . . . . . . . . . LINC00668 . . . long intergenic non-protein coding RNA 668 . . . . . . . . . . . LINC00670 . . . long intergenic non-protein coding RNA 670 . . . . . . . . . . . LINC00671 . . . long intergenic non-protein coding RNA 671 . . . . . . . . . . . LINC00672 . . . long intergenic non-protein coding RNA 672 . . . . . . . . . . . LINC00673 . . . long intergenic non-protein coding RNA 673 . . . . . . . . . . . LINC00674 . . . long intergenic non-protein coding RNA 674 . . . . . . . . . . . LINC00675 . . . long intergenic non-protein coding RNA 675 . . . . . . . . . . . LINC00676 . . . long intergenic non-protein coding RNA 676 . . . . . . . . . . . LINC00677 . . . long intergenic non-protein coding RNA 677 . . . . . . . . . . . LINC00678 . . . long intergenic non-protein coding RNA 678 . . . . . . . . . . . LINC00680 . . . long intergenic non-protein coding RNA 680 . . . . . . . . . . . LINC00681 . . . long intergenic non-protein coding RNA 681 . . . . . . . . . . . LINC00682 . . . long intergenic non-protein coding RNA 682 . . . . . . . . . . . LINC00683 . . . long intergenic non-protein coding RNA 683 . . . . . . . . . . . LINC00684 . . . long intergenic non-protein coding RNA 684 . . . . . . . . . . . LINC00685 . . . long intergenic non-protein coding RNA 685 . . . . . . . . . . . LINC00686 . . . long intergenic non-protein coding RNA 686 . . . . . . . . . . . LINC00687 . . . long intergenic non-protein coding RNA 687 . . . . . . . . . . . LINC00689 . . . long intergenic non-protein coding RNA 689 . . . . . . . . . . . LINC00690 . . . long intergenic non-protein coding RNA 690 . . . . . . . . . . . LINC00691 . . . long intergenic non-protein coding RNA 691 . . . . . . . . . . . LINC00692 . . . long intergenic non-protein coding RNA 692 . . . . . . . . . 76.32231 1.83132 LINC00693 . . . long intergenic non-protein coding RNA 693 . . . . . . . . . . . LINC00694 . . . long intergenic non-protein coding RNA 694 . . . . . . . . . . . LINC00696 0.211998268274444 0.64807046669602 0.139931265029535 long intergenic non-protein coding RNA 696 . . . . . . . . . 3.00885 0.10905 LINC00698 . . . long intergenic non-protein coding RNA 698 . . . . . . . . . . . LINC00700 . . . long intergenic non-protein coding RNA 700 . . . . . . . . . . . LINC00701 . . . long intergenic non-protein coding RNA 701 . . . . . . . . . . . LINC00702 . . . long intergenic non-protein coding RNA 702 . . . . . . . . . . . LINC00703 . . . long intergenic non-protein coding RNA 703 . . . . . . . . . . . LINC00704 . . . long intergenic non-protein coding RNA 704 . . . . . . . . . . . LINC00705 . . . long intergenic non-protein coding RNA 705 . . . . . . . . . . . LINC00706 . . . long intergenic non-protein coding RNA 706 . . . . . . . . . . . LINC00707 . . . long intergenic non-protein coding RNA 707 . . . . . . . . . . . LINC00708 . . . long intergenic non-protein coding RNA 708 . . . . . . . . . . . LINC00709 . . . long intergenic non-protein coding RNA 709 . . . . . . . . . . . LINC00710 . . . long intergenic non-protein coding RNA 710 . . . . . . . . . . . LINC00824 . . . long intergenic non-protein coding RNA 824 . . . . . . . . . . . LINC00836 . . . long intergenic non-protein coding RNA 836 . . . . . . . . . . . LINC00837 . . . long intergenic non-protein coding RNA 837 . . . . . . . . . . . LINC00838 . . . long intergenic non-protein coding RNA 838 . . . . . . . . . . . LINC00839 . . . long intergenic non-protein coding RNA 839 . . . . . . . . . . . LINC00840 . . . long intergenic non-protein coding RNA 840 . . . . . . . . . . . LINC00841 . . . long intergenic non-protein coding RNA 841 . . . . . . . . . . . LINC00842 . . . long intergenic non-protein coding RNA 842 . . . . . . . . . . . LINC00843 . . . long intergenic non-protein coding RNA 843 . . . . . . . . . . . LINC00844 . . . long intergenic non-protein coding RNA 844 . . . . . . . . . . . LINC00845 . . . long intergenic non-protein coding RNA 845 . . . . . . . . . . . LINC00846 . . . long intergenic non-protein coding RNA 846 . . . . . 0.16049 . . . . . LINC00847 . . . long intergenic non-protein coding RNA 847 . . . . . . . . . . . LINC00850 . . . long intergenic non-protein coding RNA 850 . . . . . . . . . . . LINC00851 . . . long intergenic non-protein coding RNA 851 . . . . . . . . . . . LINC00852 . . . long intergenic non-protein coding RNA 852 . . . . . . . . . . . LINC00853 . . . long intergenic non-protein coding RNA 853 . . . . . . . . . . . LINC00854 . . . long intergenic non-protein coding RNA 854 . . . . . . . . . . . LINC00856 . . . long intergenic non-protein coding RNA 856 . . . . . . . . . . . LINC00857 . . . long intergenic non-protein coding RNA 857 . . . . . . . . . . . LINC00858 . . . long intergenic non-protein coding RNA 858 . . . . . . . . . . . LINC00861 . . . long intergenic non-protein coding RNA 861 . . . . . . . . . . . LINC00862 . . . long intergenic non-protein coding RNA 862 . . . . . 0.12871 . . . . . LINC00863 . . . long intergenic non-protein coding RNA 863 . . . . . . . . . . . LINC00864 . . . long intergenic non-protein coding RNA 864 . . . . . . . . . . . LINC00865 . . . long intergenic non-protein coding RNA 865 . . . . . . . . . . . LINC00866 . . . long intergenic non-protein coding RNA 866 . . . . . . . . . . . LINC00867 . . . long intergenic non-protein coding RNA 867 . . . . . . . . . . . LINC00868 . . . long intergenic non-protein coding RNA 868 . . . . . . . . . . . LINC00869 . . . long intergenic non-protein coding RNA 869 . . . . . . . . . . . LINC00870 . . . long intergenic non-protein coding RNA 870 . . . . . . . . . . . LINC00871 . . . long intergenic non-protein coding RNA 871 . . . . . . . . . . . LINC00877 . . . long intergenic non-protein coding RNA 877 . . . . . . . . . . . LINC00879 . . . long intergenic non-protein coding RNA 879 . . . . . . . . . . . LINC00880 . . . long intergenic non-protein coding RNA 880 . . . . . . . . . . . LINC00881 . . . long intergenic non-protein coding RNA 881 . . . . . . . . . . . LINC00882 . . . long intergenic non-protein coding RNA 882 . . . . . . . . . . . LINC00884 . . . long intergenic non-protein coding RNA 884 . . . . . . . . . . . LINC00885 . . . long intergenic non-protein coding RNA 885 . . . . . . . . . . . LINC00886 . . . long intergenic non-protein coding RNA 886 . . . . . . . . . . . LINC00887 . . . long intergenic non-protein coding RNA 887 . . . . . . . . . . . LINC00888 . . . long intergenic non-protein coding RNA 888 . . . . . . . . . . . LINC00889 . . . long intergenic non-protein coding RNA 889 . . . . . . . . . . . LINC00890 . . . long intergenic non-protein coding RNA 890 . . . . . . . . . . . LINC00891 . . . long intergenic non-protein coding RNA 891 . . . . . . . . . . . LINC00892 . . . long intergenic non-protein coding RNA 892 . . . . . . . . . . . LINC00893 . . . long intergenic non-protein coding RNA 893 . . . . . . . . . . . LINC00894 . . . long intergenic non-protein coding RNA 894 . . . . . . . . . . . LINC00895 . . . long intergenic non-protein coding RNA 895 . . . . . . . . . . . LINC00896 . . . long intergenic non-protein coding RNA 896 . . . . . . . . . . . LINC00898 . . . long intergenic non-protein coding RNA 898 . . . . . . . . . . . LINC00899 . . . long intergenic non-protein coding RNA 899 . . . . . . . . . . . LINC00900 . . . long intergenic non-protein coding RNA 900 . . . . . . . . . . . LINC00901 . . . long intergenic non-protein coding RNA 901 . . . . . . . . . . . LINC00903 . . . long intergenic non-protein coding RNA 903 . . . . . . . . . . . LINC00904 . . . long intergenic non-protein coding RNA 904 . . . . . . . . . . . LINC00905 . . . long intergenic non-protein coding RNA 905 . . . . . . . . . . . LINC00906 . . . long intergenic non-protein coding RNA 906 . . . . . . . . . . . LINC00907 . . . long intergenic non-protein coding RNA 907 . . . . . . . . . . . LINC00908 . . . long intergenic non-protein coding RNA 908 . . . . . . . . . 1.92553 0.06060 LINC00909 . . . long intergenic non-protein coding RNA 909 . . . . . . . . . . . LINC00910 . . . long intergenic non-protein coding RNA 910 . . . . . . . . . . . LINC00911 . . . long intergenic non-protein coding RNA 911 . . . . . . . . . . . LINC00914 . . . long intergenic non-protein coding RNA 914 . . . . . 0.14379 . . . . . LINC00917 . . . long intergenic non-protein coding RNA 917 . . . . . . . . . . . LINC00919 . . . long intergenic non-protein coding RNA 919 . . . . . . . . . . . LINC00920 . . . long intergenic non-protein coding RNA 920 . . . . . . . . . . . LINC00921 . . . long intergenic non-protein coding RNA 921 . . . . . . . . . . . LINC00922 . . . long intergenic non-protein coding RNA 922 . . . . . . . . . . . LINC00923 . . . long intergenic non-protein coding RNA 923 . . . . . . . . . 31.91972 1.00405 LINC00924 . . . long intergenic non-protein coding RNA 924 . . . . . . . . . . . LINC00926 . . . long intergenic non-protein coding RNA 926 . . . . . . . . . . . LINC00927 . . . long intergenic non-protein coding RNA 927 . . . . . . . . . . . LINC00928 . . . long intergenic non-protein coding RNA 928 . . . . . . . . . . . LINC00929 . . . long intergenic non-protein coding RNA 929 . . . . . . . . . . . LINC00930 . . . long intergenic non-protein coding RNA 930 . . . . . . . . . . . LINC00933 . . . long intergenic non-protein coding RNA 933 . . . . . . . . . . . LINC00934 . . . long intergenic non-protein coding RNA 934 . . . . . . . . . . . LINC00935 . . . long intergenic non-protein coding RNA 935 . . . . . . . . . 87.61309 1.99869 LINC00936 . . . long intergenic non-protein coding RNA 936 . . . . . . . . . . . LINC00937 . . . long intergenic non-protein coding RNA 937 . . . . . . . . . . . LINC00938 . . . long intergenic non-protein coding RNA 938 . . . . . . . . . . . LINC00939 . . . long intergenic non-protein coding RNA 939 . . . . . . . . . . . LINC00940 . . . long intergenic non-protein coding RNA 940 . . . . . . . . . . . LINC00941 . . . long intergenic non-protein coding RNA 941 . . . . . . . . . . . LINC00942 . . . long intergenic non-protein coding RNA 942 . . . . . . . . . . . LINC00943 . . . long intergenic non-protein coding RNA 943 . . . . . . . . . . . LINC00944 . . . long intergenic non-protein coding RNA 944 . . . . . . . . . . . LINC00945 . . . long intergenic non-protein coding RNA 945 . . . . . . . . . . . LINC00950 . . . long intergenic non-protein coding RNA 950 . . . . . . . . . . . LINC00951 . . . long intergenic non-protein coding RNA 951 . . . . . . . . . . . LINC00954 . . . long intergenic non-protein coding RNA 954 . . . . . . . . . . . LINC00955 . . . long intergenic non-protein coding RNA 955 . . . . . . . . . 6653.86048 17.29032 LINC00957 . . . long intergenic non-protein coding RNA 957 . . . . . . . . . . . LINC00958 . . . long intergenic non-protein coding RNA 958 . . . . . . . . . . . LINC00959 . . . long intergenic non-protein coding RNA 959 . . . . . . . . . . . LINC00960 . . . long intergenic non-protein coding RNA 960 . . . . . . . . . . . LINC00961 . . . long intergenic non-protein coding RNA 961 . . . . . . . . . . . LINC00963 . . . long intergenic non-protein coding RNA 963 . . . . . . . . . . . LINC00964 . . . long intergenic non-protein coding RNA 964 . . . . . . . . . . . LINC00965 . . . long intergenic non-protein coding RNA 965 . . . . . . . . . . . LINC00967 . . . long intergenic non-protein coding RNA 967 . . . . . . . . . . . LINC00968 . . . long intergenic non-protein coding RNA 968 . . . . . . . . . . . LINC00969 . . . long intergenic non-protein coding RNA 969 . . . . . . . . . . . LINC00970 . . . long intergenic non-protein coding RNA 970 . . . . . . . . . . . LINC00971 . . . long intergenic non-protein coding RNA 971 . . . . . . . . . . . LINC00972 . . . long intergenic non-protein coding RNA 972 . . . . . . . . . . . LINC00973 . . . long intergenic non-protein coding RNA 973 . . . . . . . . . . . LINC00974 . . . long intergenic non-protein coding RNA 974 . . . . . . . . . . . LINC00976 . . . long intergenic non-protein coding RNA 976 . . . . . . . . . . . LINC00977 . . . long intergenic non-protein coding RNA 977 . . . . . . . . . . . LINC00982 . . . long intergenic non-protein coding RNA 982 . . . . . . . . . . . LINC00987 . . . long intergenic non-protein coding RNA 987 . . . . . . . . . . . LINC00989 . . . long intergenic non-protein coding RNA 989 . . . . . . . . . . . LINC00992 . . . long intergenic non-protein coding RNA 992 . . . . . . . . . . . LINC00993 . . . long intergenic non-protein coding RNA 993 . . . . . . . . . . . LINC00994 . . . long intergenic non-protein coding RNA 994 . . . . . . . . . . . LINC00996 . . . long intergenic non-protein coding RNA 996 . . . . . . . . . . . LINC00997 . . . long intergenic non-protein coding RNA 997 . . . . . . . . . . . LINC00998 . . . long intergenic non-protein coding RNA 998 . . . . . . . . . 0.74096 0.01268 LINC00999 . . . long intergenic non-protein coding RNA 999 . . . . . . . . . 3699.98958 11.85474 LINC01000 . . . long intergenic non-protein coding RNA 1000 . . . . . . . . . . . LINC01001 . . . long intergenic non-protein coding RNA 1001 . . . . . . . . . . . LINC01002 . . . long intergenic non-protein coding RNA 1002 . . . . . . . . . . . LINC01003 . . . long intergenic non-protein coding RNA 1003 . . . . . . . . . . . LINC01004 . . . long intergenic non-protein coding RNA 1004 . . . . . . . . . . . LINC01005 . . . long intergenic non-protein coding RNA 1005 . . . . . . . . . . . LINC01006 . . . long intergenic non-protein coding RNA 1006 . . TISSUE SPECIFICITY: Expressed only in testis. {ECO:0000269|PubMed:11890671}.; . . 0.11818 . . . . . LINC01007 . . . long intergenic non-protein coding RNA 1007 . . . . . . . . . . . LINC01010 . . . long intergenic non-protein coding RNA 1010 . . . . . . . . . . . LINC01011 . . . long intergenic non-protein coding RNA 1011 . . . . . . . . . . . LINC01012 . . . long intergenic non-protein coding RNA 1012 . . . . . . . . . . . LINC01013 . . . long intergenic non-protein coding RNA 1013 . . . . . . . . . . . LINC01014 . . . long intergenic non-protein coding RNA 1014 . . . . . . . . . . . LINC01015 . . . long intergenic non-protein coding RNA 1015 . . . . . . . . . . . LINC01016 . . . long intergenic non-protein coding RNA 1016 . . . . . . . . . . . LINC01017 . . . long intergenic non-protein coding RNA 1017 . . . . . . . . . . . LINC01018 . . . long intergenic non-protein coding RNA 1018 . . . . . . . . . . . LINC01019 . . . long intergenic non-protein coding RNA 1019 . . . . . . . . . . . LINC01020 . . . long intergenic non-protein coding RNA 1020 . . . . . . . . . . . LINC01021 . . . long intergenic non-protein coding RNA 1021 . . . . . . . . . . . LINC01022 . . . long intergenic non-protein coding RNA 1022 . . . . . . . . . . . LINC01023 . . . long intergenic non-protein coding RNA 1023 . . . . . . . . . . . LINC01024 . . . long intergenic non-protein coding RNA 1024 . . . . . . . . . . . LINC01028 . . . long intergenic non-protein coding RNA 1028 . . . . . . . . . . . LINC01029 . . . long intergenic non-protein coding RNA 1029 . . . . . . . . . . . LINC01030 . . . long intergenic non-protein coding RNA 1030 . . . . . . . . . . . LINC01031 . . . long intergenic non-protein coding RNA 1031 . . . . . . . . . . . LINC01032 . . . long intergenic non-protein coding RNA 1032 . . . . . . . . . . . LINC01033 . . . long intergenic non-protein coding RNA 1033 . . . . . . . . . . . LINC01034 . . . long intergenic non-protein coding RNA 1034 . . . . . . . . . . . LINC01035 . . . long intergenic non-protein coding RNA 1035 . . . . . . . . . . . LINC01036 . . . long intergenic non-protein coding RNA 1036 . . . . . . . . . . . LINC01037 . . . long intergenic non-protein coding RNA 1037 . . . . . . . . . . . LINC01038 . . . long intergenic non-protein coding RNA 1038 . . . . . . . . . . . LINC01039 . . . long intergenic non-protein coding RNA 1039 . . . . . . . . . . . LINC01040 . . . long intergenic non-protein coding RNA 1040 . . . . . . . . . . . LINC01043 . . . long intergenic non-protein coding RNA 1043 . . . . . . . . . . . LINC01044 . . . long intergenic non-protein coding RNA 1044 . . . . . . . . . . . LINC01046 . . . long intergenic non-protein coding RNA 1046 . . . . . . . . . . . LINC01047 . . . long intergenic non-protein coding RNA 1047 . . . . . . . . . . . LINC01048 . . . long intergenic non-protein coding RNA 1048 . . . . . . . . . . . LINC01049 . . . long intergenic non-protein coding RNA 1049 . . . . . . . . . . . LINC01050 . . . long intergenic non-protein coding RNA 1050 . . . . . . . . . . . LINC01052 . . . long intergenic non-protein coding RNA 1052 . . . . . . . . . . . LINC01053 . . . long intergenic non-protein coding RNA 1053 . . . . . . . . . . . LINC01054 . . . long intergenic non-protein coding RNA 1054 . . . . . . . . . . . LINC01055 . . . long intergenic non-protein coding RNA 1055 . . . . . . . . . . . LINC01056 . . . long intergenic non-protein coding RNA 1056 . . . . . . . . . . . LINC01057 . . . long intergenic non-protein coding RNA 1057 . . . . . . . . . . . LINC01058 . . . long intergenic non-protein coding RNA 1058 . . . . . . . . . . . LINC01059 . . . long intergenic non-protein coding RNA 1059 . . . . . . . . . . . LINC01060 . . . long intergenic non-protein coding RNA 1060 . . . . . . . . . . . LINC01061 . . . long intergenic non-protein coding RNA 1061 . . . . . . . . . . . LINC01063 . . . long intergenic non-protein coding RNA 1063 . . . . . . . . . . . LINC01065 . . . long intergenic non-protein coding RNA 1065 . . . . . . . . . . . LINC01066 . . . long intergenic non-protein coding RNA 1066 . . . . . . . . . . . LINC01067 . . . long intergenic non-protein coding RNA 1067 . . . . . . . . . . . LINC01068 . . . long intergenic non-protein coding RNA 1068 . . . . . . . . . . . LINC01069 . . . long intergenic non-protein coding RNA 1069 . . . . . . . . . . . LINC01070 . . . long intergenic non-protein coding RNA 1070 . . . . . . . . . . . LINC01072 . . . long intergenic non-protein coding RNA 1072 . . . . . . . . . . . LINC01073 . . . long intergenic non-protein coding RNA 1073 . . . . . . . . . . . LINC01074 . . . long intergenic non-protein coding RNA 1074 . . . . . . . . . . . LINC01075 . . . long intergenic non-protein coding RNA 1075 . . . . . . . . . . . LINC01076 . . . long intergenic non-protein coding RNA 1076 . . . . . . . . . . . LINC01077 . . . long intergenic non-protein coding RNA 1077 . . . . . . . . . . . LINC01078 . . . long intergenic non-protein coding RNA 1078 . . . . . . . . . . . LINC01079 . . . long intergenic non-protein coding RNA 1079 . . . . . . . . . . . LINC01080 . . . long intergenic non-protein coding RNA 1080 . . . . . . . . . . . LINC01081 . . . long intergenic non-protein coding RNA 1081 . . . . . . . . . . . LINC01082 . . . long intergenic non-protein coding RNA 1082 . . . . . . . . . . . LINC01085 . . . long intergenic non-protein coding RNA 1085 . . . . . . . . . . . LINC01087 . . . long intergenic non-protein coding RNA 1087 . . . . . . . . . . . LINC01088 . . . long intergenic non-protein coding RNA 1088 . . . . . . . . . . . LINC01089 . . . long intergenic non-protein coding RNA 1089 . . . . . . . . . . . LINC01090 . . . long intergenic non-protein coding RNA 1090 . . . . . . . . . . . LINC01091 . . . long intergenic non-protein coding RNA 1091 . . . . . . . . . . . LINC01093 . . . long intergenic non-protein coding RNA 1093 . . . . . . . . . . . LINC01094 . . . long intergenic non-protein coding RNA 1094 . . . . . . . . . . . LINC01095 . . . long intergenic non-protein coding RNA 1095 . . . . . . . . . . . LINC01096 . . . long intergenic non-protein coding RNA 1096 . . . . . . . . . . . LINC01097 . . . long intergenic non-protein coding RNA 1097 . . . . . . . . . . . LINC01098 . . . long intergenic non-protein coding RNA 1098 . . . . . . . . . 37.03765 1.10683 LINC01099 . . . long intergenic non-protein coding RNA 1099 . . . . . . . . . . . LINC01100 . . . long intergenic non-protein coding RNA 1100 . . . . . . . . . 922.0438 5.89670 LINC01101 . . . long intergenic non-protein coding RNA 1101 . . . . . . . . . 1382.1205 6.96600 LINC01102 . . . long intergenic non-protein coding RNA 1102 . . . . . . . . . . . LINC01103 . . . long intergenic non-protein coding RNA 1103 . . . . . . . . . . . LINC01104 . . . long intergenic non-protein coding RNA 1104 . . . . . . . . . . . LINC01105 . . . long intergenic non-protein coding RNA 1105 . . . . . . . . . . . LINC01106 . . . long intergenic non-protein coding RNA 1106 . . . . . . . . . . . LINC01107 . . . long intergenic non-protein coding RNA 1107 . . . . . . . . . . . LINC01108 . . . long intergenic non-protein coding RNA 1108 . . . . . . . . . . . LINC01109 . . . long intergenic non-protein coding RNA 1109 . . . . . . . . . . . LINC01111 . . . long intergenic non-protein coding RNA 1111 . . . . . . . . . . . LINC01114 . . . long intergenic non-protein coding RNA 1114 . . . . . . . . . . . LINC01115 . . . long intergenic non-protein coding RNA 1115 . . . . . . . . . . . LINC01116 . . . long intergenic non-protein coding RNA 1116 . . . . . . . . . . . LINC01117 . . . long intergenic non-protein coding RNA 1117 . . . . . . . . . . . LINC01118 . . . long intergenic non-protein coding RNA 1118 . . . . . . . . . 730.16422 5.36518 LINC01119 . . . long intergenic non-protein coding RNA 1119 . . . . . . . . . 1.39687 0.04958 LINC01120 . . . long intergenic non-protein coding RNA 1120 . . . . . . . . . . . LINC01121 . . . long intergenic non-protein coding RNA 1121 . . . . . . . . . . . LINC01122 . . . long intergenic non-protein coding RNA 1122 . . . . . . . . . . . LINC01123 . . . long intergenic non-protein coding RNA 1123 . . . . . . . . . . . LINC01124 . . . long intergenic non-protein coding RNA 1124 . . . . . . . . . 751.56713 5.43913 LINC01125 . . . long intergenic non-protein coding RNA 1125 . . . . . . . . . . . LINC01126 . . . long intergenic non-protein coding RNA 1126 . . . . . . . . . . . LINC01127 . . . long intergenic non-protein coding RNA 1127 . . . . . . . . . . . LINC01128 . . . long intergenic non-protein coding RNA 1128 . . . . . . . . . . . LINC01132 . . . long intergenic non-protein coding RNA 1132 . . . . . . . . . . . LINC01133 . . . long intergenic non-protein coding RNA 1133 . . . . . . . . . . . LINC01134 . . . long intergenic non-protein coding RNA 1134 . . . . . . . . . . . LINC01135 . . . long intergenic non-protein coding RNA 1135 . . . . . . . . . . . LINC01136 . . . long intergenic non-protein coding RNA 1136 . . . . . . . . . . . LINC01137 . . . long intergenic non-protein coding RNA 1137 . . . . . . . . . . . LINC01138 . . . long intergenic non-protein coding RNA 1138 . . . . . . . . . . . LINC01139 . . . long intergenic non-protein coding RNA 1139 . . . . . . . . . . . LINC01140 . . . long intergenic non-protein coding RNA 1140 . . . . . . . . . . . LINC01141 . . . long intergenic non-protein coding RNA 1141 . . . . . . . . . . . LINC01142 . . . long intergenic non-protein coding RNA 1142 . . . . . . . . . . . LINC01143 . . . long intergenic non-protein coding RNA 1143 . . . . . . . . . . . LINC01144 . . . long intergenic non-protein coding RNA 1144 . . . . . . . . . . . LINC01146 . . . long intergenic non-protein coding RNA 1146 . . . . . . . . . . . LINC01149 . . . long intergenic non-protein coding RNA 1149 . . . . . . . . . . . LINC01150 . . . long intergenic non-protein coding RNA 1150 . . . . . . . . . . . LINC01151 . . . long intergenic non-protein coding RNA 1151 . . . . . . . . . . . LINC01152 . . . long intergenic non-protein coding RNA 1152 . . . . . . . . . . . LINC01153 . . . long intergenic non-protein coding RNA 1153 . . . . . . . . . . . LINC01154 . . . long intergenic non-protein coding RNA 1154 . . . . . . . . . . . LINC01157 . . . long intergenic non-protein coding RNA 1157 . . . . . . . . . . . LINC01158 . . . long intergenic non-protein coding RNA 1158 . . . . . . . . . . . LINC01159 . . . long intergenic non-protein coding RNA 1159 . . . . . . . . . . . LINC01160 . . . long intergenic non-protein coding RNA 1160 . . . . . . . . . . . LINC01162 . . . long intergenic non-protein coding RNA 1162 . . . . . . . . . . . LINC01163 . . . long intergenic non-protein coding RNA 1163 . . . . . . . . . . . LINC01164 . . . long intergenic non-protein coding RNA 1164 . . . . . . . . . . . LINC01165 . . . long intergenic non-protein coding RNA 1165 . . . . . . . . . . . LINC01166 . . . long intergenic non-protein coding RNA 1166 . . . . . . . . . . . LINC01167 . . . long intergenic non-protein coding RNA 1167 . . . . . . . . . . . LINC01168 . . . long intergenic non-protein coding RNA 1168 . . . . . . . . . . . LINC01169 . . . long intergenic non-protein coding RNA 1169 . . . . . . . . . . . LINC01170 . . . long intergenic non-protein coding RNA 1170 . . . . . . . . . . . LINC01173 . . . long intergenic non-protein coding RNA 1173 . . . . . . . . . . . LINC01176 . . . long intergenic non-protein coding RNA 1176 . . . . . . . . . . . LINC01177 . . . long intergenic non-protein coding RNA 1177 . . . . . . . . . . . LINC01179 . . . long intergenic non-protein coding RNA 1179 . . . . . . . . . . . LINC01180 . . . long intergenic non-protein coding RNA 1180 . . . . . . . . . . . LINC01181 . . . long intergenic non-protein coding RNA 1181 . . . . . . . . . . . LINC01182 . . . long intergenic non-protein coding RNA 1182 . . . . . . . . . . . LINC01184 . . . long intergenic non-protein coding RNA 1184 . . . . . . . . . . . LINC01185 . . . long intergenic non-protein coding RNA 1185 . . . . . . . . . . . LINC01186 . . . long intergenic non-protein coding RNA 1186 . . . . . . . . . . . LINC01187 . . . long intergenic non-protein coding RNA 1187 . . . . . . . . . . . LINC01189 . . . long intergenic non-protein coding RNA 1189 . . . . . . . . . . . LINC01191 . . . long intergenic non-protein coding RNA 1191 . . . . . . . . . . . LINC01192 . . . long intergenic non-protein coding RNA 1192 . . . . . . . . . . . LINC01193 . . . long intergenic non-protein coding RNA 1193 . . . . . . . . . . . LINC01194 . . . long intergenic non-protein coding RNA 1194 . . . . . . . . . . . LINC01195 . . . long intergenic non-protein coding RNA 1195 . . . . . . . . . . . LINC01197 . . . long intergenic non-protein coding RNA 1197 . . . . . . . . . . . LINC01198 . . . long intergenic non-protein coding RNA 1198 . . . . . . . . . . . LINC01201 . . . long intergenic non-protein coding RNA 1201 . . . . . . . . . . . LINC01202 . . . long intergenic non-protein coding RNA 1202 . . . . . . . . . . . LINC01203 . . . long intergenic non-protein coding RNA 1203 . . . . . . . . . . . LINC01204 . . . long intergenic non-protein coding RNA 1204 . . . . . . . . . . . LINC01205 . . . long intergenic non-protein coding RNA 1205 . . . . . . . . . . . LINC01206 . . . long intergenic non-protein coding RNA 1206 . . . . . . . . . . . LINC01207 . . . long intergenic non-protein coding RNA 1207 . . . . . . . . . . . LINC01208 . . . long intergenic non-protein coding RNA 1208 . . . . . . . . . . . LINC01209 . . . long intergenic non-protein coding RNA 1209 . . . . . . . . . . . LINC01210 . . . long intergenic non-protein coding RNA 1210 . . . . . . . . . . . LINC01212 . . . long intergenic non-protein coding RNA 1212 . . . . . . . . . . . LINC01213 . . . long intergenic non-protein coding RNA 1213 . . . . . . . . . . . LINC01214 . . . long intergenic non-protein coding RNA 1214 . . . . . . . . . . . LINC01215 . . . long intergenic non-protein coding RNA 1215 . . . . . . . . . . . LINC01216 . . . long intergenic non-protein coding RNA 1216 . . . . . . . . . . . LINC01217 . . . long intergenic non-protein coding RNA 1217 . . . . . . . . . . . LINC01218 . . . long intergenic non-protein coding RNA 1218 . . . . . . . . . . . LINC01219 . . . long intergenic non-protein coding RNA 1219 . . . . . . . . . . . LINC01220 . . . long intergenic non-protein coding RNA 1220 . . . . . . . . . . . LINC01221 . . . long intergenic non-protein coding RNA 1221 . . . . . . . . . . . LINC01222 . . . long intergenic non-protein coding RNA 1222 . . . . . . . . . . . LINC01224 . . . long intergenic non-protein coding RNA 1224 . . . . . . . . . . . LINC01225 . . . long intergenic non-protein coding RNA 1225 . . . . . . . . . . . LINC01226 . . . long intergenic non-protein coding RNA 1226 . . . . . . . . . . . LINC01227 . . . long intergenic non-protein coding RNA 1227 . . . . . . . . . . . LINC01228 . . . long intergenic non-protein coding RNA 1228 . . . . . . . . . . . LINC01229 . . . long intergenic non-protein coding RNA 1229 . . . . . . . . . . . LINC01230 . . . long intergenic non-protein coding RNA 1230 . . . . . . . . . . . LINC01231 . . . long intergenic non-protein coding RNA 1231 . . . . . . . . . . . LINC01232 . . . long intergenic non-protein coding RNA 1232 . . . . . . . . . . . LINC01233 . . . long intergenic non-protein coding RNA 1233 . . . . . . . . . . . LINC01234 . . . long intergenic non-protein coding RNA 1234 . . . . . . . . . . . LINC01235 . . . long intergenic non-protein coding RNA 1235 . . . . . . . . . . . LINC01237 . . . long intergenic non-protein coding RNA 1237 . . . . . . . . . . . LINC01239 . . . long intergenic non-protein coding RNA 1239 . . . . . . . . . . . LINC01241 . . . long intergenic non-protein coding RNA 1241 . . . . . . . . . . . LINC01242 . . . long intergenic non-protein coding RNA 1242 . . . . . . . . . . . LINC01243 . . . long intergenic non-protein coding RNA 1243 . . . . . . . . . . . LINC01246 . . . long intergenic non-protein coding RNA 1246 . . . . . . . . . . . LINC01247 . . . long intergenic non-protein coding RNA 1247 . . . . . . . . . . . LINC01248 . . . long intergenic non-protein coding RNA 1248 . . . . . . . . . . . LINC01249 . . . long intergenic non-protein coding RNA 1249 . . . . . . . . . . . LINC01250 . . . long intergenic non-protein coding RNA 1250 . . . . . . . . . . . LINC01251 . . . long intergenic non-protein coding RNA 1251 . . . . . . . . . . . LINC01252 . . . long intergenic non-protein coding RNA 1252 . . . . . . . . . . . LINC01254 . . . long intergenic non-protein coding RNA 1254 . . . . . . . . . . . LINC01255 . . . long intergenic non-protein coding RNA 1255 . . . . . . . . . . . LINC01256 . . . long intergenic non-protein coding RNA 1256 . . . . . . . . . . . LINC01257 . . . long intergenic non-protein coding RNA 1257 . . . . . . . . . . . LINC01258 . . . long intergenic non-protein coding RNA 1258 . . . . . . . . . . . LINC01259 . . . long intergenic non-protein coding RNA 1259 . . . . . . . . . . . LINC01260 . . . long intergenic non-protein coding RNA 1260 . . . . . . . . . . . LINC01262 . . . long intergenic non-protein coding RNA 1262 . . . . . . . . . . . LINC01264 . . . long intergenic non-protein coding RNA 1264 . . . . . . . . . . . LINC01265 . . . long intergenic non-protein coding RNA 1265 . . . . . . . . . . . LINC01266 . . . long intergenic non-protein coding RNA 1266 . . . . . . . . . . . LINC01267 . . . long intergenic non-protein coding RNA 1267 . . . . . . . . . . . LINC01268 . . . long intergenic non-protein coding RNA 1268 . . . . . . . . . . . LINC01269 . . . long intergenic non-protein coding RNA 1269 . . . . . . . . . . . LINC01270 . . . long intergenic non-protein coding RNA 1270 . . . . . . . . . . . LINC01271 . . . long intergenic non-protein coding RNA 1271 . . . . . . . . . . . LINC01272 . . . long intergenic non-protein coding RNA 1272 . . . . . . . . . . . LINC01273 . . . long intergenic non-protein coding RNA 1273 . . . . . . . . . . . LINC01276 . . . long intergenic non-protein coding RNA 1276 . . . . . . . . . . . LINC01277 . . . long intergenic non-protein coding RNA 1277 . . . . . . . . . . . LINC01278 . . . long intergenic non-protein coding RNA 1278 . . . . . . . . . . . LINC01279 . . . long intergenic non-protein coding RNA 1279 . . . . . . . . . . . LINC01280 . . . long intergenic non-protein coding RNA 1280 . . . . . . . . . . . LINC01281 . . . long intergenic non-protein coding RNA 1281 . . . . . . . . . . . LINC01282 . . . long intergenic non-protein coding RNA 1282 . . . . . . . . . . . LINC01284 . . . long intergenic non-protein coding RNA 1284 . . . . . . . . . . . LINC01285 . . . long intergenic non-protein coding RNA 1285 . . . . . . . . . . . LINC01287 . . . long intergenic non-protein coding RNA 1287 . . . . . . . . . . . LINC01288 . . . long intergenic non-protein coding RNA 1288 . . . . . . . . . . . LINC01289 . . . long intergenic non-protein coding RNA 1289 . . . . . . . . . . . LINC01290 . . . long intergenic non-protein coding RNA 1290 . . . . . . . . . . . LINC01291 . . . long intergenic non-protein coding RNA 1291 . . . . . . . . . . . LINC01293 . . . long intergenic non-protein coding RNA 1293 . . . . . . . . . . . LINC01296 . . . long intergenic non-protein coding RNA 1296 . . . . . . . . . . . LINC01297 . . . long intergenic non-protein coding RNA 1297 . . . . . . . . . . . LINC01298 . . . long intergenic non-protein coding RNA 1298 . . . . . . . . . . . LINC01299 . . . long intergenic non-protein coding RNA 1299 . . . . . . . . . . . LINC01300 . . . long intergenic non-protein coding RNA 1300 . . . . . . . . . . . LINC01301 . . . long intergenic non-protein coding RNA 1301 . . . . . . . . . . . LINC01304 . . . long intergenic non-protein coding RNA 1304 . . . . . . . . . . . LINC01305 . . . long intergenic non-protein coding RNA 1305 . . . . . . . . . . . LINC01307 . . . long intergenic non-protein coding RNA 1307 . . . . . . . . . . . LINC01309 . . . long intergenic non-protein coding RNA 1309 . . . . . . . . . . . LINC01310 . . . long intergenic non-protein coding RNA 1310 . . . . . . . . . . . LINC01311 . . . long intergenic non-protein coding RNA 1311 . . . . . . . . . . . LINC01312 . . . long intergenic non-protein coding RNA 1312 . . . . . . . . . . . LINC01314 . . . long intergenic non-protein coding RNA 1314 . . . . . . . . . . . LINC01315 . . . long intergenic non-protein coding RNA 1315 . . . . . . . . . . . LINC01317 . . . long intergenic non-protein coding RNA 1317 . . . . . . . . . . . LINC01318 . . . long intergenic non-protein coding RNA 1318 . . . . . . . . . . . LINC01320 . . . long intergenic non-protein coding RNA 1320 . . . . . . . . . . . LINC01322 . . . long intergenic non-protein coding RNA 1322 . . . . . . . . . . . LINC01323 . . . long intergenic non-protein coding RNA 1323 . . . . . . . . . . . LINC01324 . . . long intergenic non-protein coding RNA 1324 . . . . . . . . . . . LINC01326 . . . long intergenic non-protein coding RNA 1326 . . . . . . . . . . . LINC01327 . . . long intergenic non-protein coding RNA 1327 . . . . . . . . . . . LINC01330 . . . long intergenic non-protein coding RNA 1330 . . . . . . . . . . . LINC01331 . . . long intergenic non-protein coding RNA 1331 . . . . . . . . . . . LINC01332 . . . long intergenic non-protein coding RNA 1332 . . . . . . . . . . . LINC01333 . . . long intergenic non-protein coding RNA 1333 . . . . . . . . . . . LINC01335 . . . long intergenic non-protein coding RNA 1335 . . . . . . . . . . . LINC01336 . . . long intergenic non-protein coding RNA 1336 . . . . . . . . . . . LINC01337 . . . long intergenic non-protein coding RNA 1337 . . . . . . . . . . . LINC01338 . . . long intergenic non-protein coding RNA 1338 . . . . . . . . . . . LINC01339 . . . long intergenic non-protein coding RNA 1339 . . . . . . . . . . . LINC01340 . . . long intergenic non-protein coding RNA 1340 . . . . . . . . . . . LINC01341 . . . long intergenic non-protein coding RNA 1341 . . . . . . . . . . . LINC01342 . . . long intergenic non-protein coding RNA 1342 . . . . . . . . . . . LINC01343 . . . long intergenic non-protein coding RNA 1343 . . . . . . . . . . . LINC01344 . . . long intergenic non-protein coding RNA 1344 . . . . . . . . . . . LINC01346 . . . long intergenic non-protein coding RNA 1346 . . . . . . . . . . . LINC01347 . . . long intergenic non-protein coding RNA 1347 . . . . . . . . . . . LINC01348 . . . long intergenic non-protein coding RNA 1348 . . . . . . . . . . . LINC01349 . . . long intergenic non-protein coding RNA 1349 . . . . . . . . . . . LINC01350 . . . long intergenic non-protein coding RNA 1350 . . . . . . . . . . . LINC01351 . . . long intergenic non-protein coding RNA 1351 . . . . . . . . . . . LINC01352 . . . long intergenic non-protein coding RNA 1352 . . . . . . . . . . . LINC01353 . . . long intergenic non-protein coding RNA 1353 . . . . . . . . . . . LINC01354 . . . long intergenic non-protein coding RNA 1354 . . . . . . . . . . . LINC01355 . . . long intergenic non-protein coding RNA 1355 . . . . . . . . . . . LINC01356 . . . long intergenic non-protein coding RNA 1356 . . . . . . . . . . . LINC01358 . . . long intergenic non-protein coding RNA 1358 . . . . . . . . . . . LINC01359 . . . long intergenic non-protein coding RNA 1359 . . . . . . . . . . . LINC01360 . . . long intergenic non-protein coding RNA 1360 . . . . . . . . . . . LINC01361 . . . long intergenic non-protein coding RNA 1361 . . . . . . . . . . . LINC01362 . . . long intergenic non-protein coding RNA 1362 . . . . . . . . . . . LINC01363 . . . long intergenic non-protein coding RNA 1363 . . . . . . . . . . . LINC01364 . . . long intergenic non-protein coding RNA 1364 . . . . . . . . . . . LINC01365 . . . long intergenic non-protein coding RNA 1365 . . . . . . . . . . . LINC01366 . . . long intergenic non-protein coding RNA 1366 . . . . . . . . . . . LINC01370 . . . long intergenic non-protein coding RNA 1370 . . . . . . . . . . . LINC01372 . . . long intergenic non-protein coding RNA 1372 . . . . . . . . . . . LINC01374 . . . long intergenic non-protein coding RNA 1374 . . . . . . . . . . . LINC01375 . . . long intergenic non-protein coding RNA 1375 . . . . . . . . . . . LINC01376 . . . long intergenic non-protein coding RNA 1376 . . . . . . . . . . . LINC01377 . . . long intergenic non-protein coding RNA 1377 . . . . . . . . . . . LINC01378 . . . long intergenic non-protein coding RNA 1378 . . . . . . . . . . . LINC01381 . . . long intergenic non-protein coding RNA 1381 . . . . . . . . . . . LINC01384 . . . long intergenic non-protein coding RNA 1384 . . . . . . . . . . . LINC01385 . . . long intergenic non-protein coding RNA 1385 . . . . . . . . . . . LINC01386 . . . long intergenic non-protein coding RNA 1386 . . . . . . . . . . . LINC01387 . . . long intergenic non-protein coding RNA 1387 . . . . . . . . . . . LINC01388 . . . long intergenic non-protein coding RNA 1388 . . . . . . . . . . . LINC01389 . . . long intergenic non-protein coding RNA 1389 . . . . . . . . . . . LINC01391 . . . long intergenic non-protein coding RNA 1391 . . . . . . . . . . . LINC01392 . . . long intergenic non-protein coding RNA 1392 . . . . . . . . . . . LINC01393 . . . long intergenic non-protein coding RNA 1393 . . . . . . . . . . . LINC01394 . . . long intergenic non-protein coding RNA 1394 . . . . . . . . . . . LINC01395 . . . long intergenic non-protein coding RNA 1395 . . . . . . . . . . . LINC01396 . . . long intergenic non-protein coding RNA 1396 . . . . . . . . . . . LINC01397 . . . long intergenic non-protein coding RNA 1397 . . . . . . . . . . . LINC01398 . . . long intergenic non-protein coding RNA 1398 . . . . . . . . . . . LINC01399 . . . long intergenic non-protein coding RNA 1399 . . . . . . . . . . . LINC01400 . . . long intergenic non-protein coding RNA 1400 . . . . . . . . . . . LINC01402 . . . long intergenic non-protein coding RNA 1402 . . . . . . . . . . . LINC01405 . . . long intergenic non-protein coding RNA 1405 . . . . . . . . . . . LINC01410 . . . long intergenic non-protein coding RNA 1410 . . . . . . . . . . . LINC01411 . . . long intergenic non-protein coding RNA 1411 . . . . . . . . . . . LINC01412 . . . long intergenic non-protein coding RNA 1412 . . . . . . . . . . . LINC01413 . . . long intergenic non-protein coding RNA 1413 . . . . . . . . . . . LINC01415 . . . long intergenic non-protein coding RNA 1415 . . . . . . . . . . . LINC01416 . . . long intergenic non-protein coding RNA 1416 . . . . . . . . . . . LINC01419 . . . long intergenic non-protein coding RNA 1419 . . . . . . . . . . . LINC01420 . . . long intergenic non-protein coding RNA 1420 . . . . . . . . . . . LINC01422 . . . long intergenic non-protein coding RNA 1422 . . . . . . . . . . . LINC01423 . . . long intergenic non-protein coding RNA 1423 . . . . . . . . . . . LINC01424 . . . long intergenic non-protein coding RNA 1424 . . . . . . . . . . . LINC01425 . . . long intergenic non-protein coding RNA 1425 . . . . . . . . . . . LINC01426 . . . long intergenic non-protein coding RNA 1426 . . . . . . . . . . . LINC01427 . . . long intergenic non-protein coding RNA 1427 . . . . . . . . . . . LINC01428 . . . long intergenic non-protein coding RNA 1428 . . . . . . . . . . . LINC01429 . . . long intergenic non-protein coding RNA 1429 . . . . . . . . . . . LINC01430 . . . long intergenic non-protein coding RNA 1430 . . . . . . . . . . . LINC01431 . . . long intergenic non-protein coding RNA 1431 . . . . . . . . . . . LINC01432 . . . long intergenic non-protein coding RNA 1432 . . . . . . . . . . . LINC01433 . . . long intergenic non-protein coding RNA 1433 . . . . . . . . . . . LINC01435 . . . long intergenic non-protein coding RNA 1435 . . . . . . . . . . . LINC01436 . . . long intergenic non-protein coding RNA 1436 . . . . . . . . . . . LINC01438 . . . long intergenic non-protein coding RNA 1438 . . . . . . . . . . . LINC01440 . . . long intergenic non-protein coding RNA 1440 . . . . . . . . . . . LINC01441 . . . long intergenic non-protein coding RNA 1441 . . . . . . . . . . . LINC01442 . . . long intergenic non-protein coding RNA 1442 . . . . . . . . . . . LINC01443 . . . long intergenic non-protein coding RNA 1443 . . . . . . . . . . . LINC01444 . . . long intergenic non-protein coding RNA 1444 . . . . . . . . . . . LINC01445 . . . long intergenic non-protein coding RNA 1445 . . . . . . . . . . . LINC01446 . . . long intergenic non-protein coding RNA 1446 . . . . . . . . . . . LINC01447 . . . long intergenic non-protein coding RNA 1447 . . . . . . . . . . . LINC01448 . . . long intergenic non-protein coding RNA 1448 . . . . . . . . . . . LINC01449 . . . long intergenic non-protein coding RNA 1449 . . . . . . . . . . . LINC01450 . . . long intergenic non-protein coding RNA 1450 . . . . . . . . . . . LINC01451 . . . long intergenic non-protein coding RNA 1451 . . . . . . . . . . . LINC01455 . . . long intergenic non-protein coding RNA 1455 . . . . . . . . . . . LINC01456 . . . long intergenic non-protein coding RNA 1456 . . . . . . . . . . . LINC01460 . . . long intergenic non-protein coding RNA 1460 . . . . . . . . . . . LINC01461 . . . long intergenic non-protein coding RNA 1461 . . . . . . . . . . . LINC01465 . . . long intergenic non-protein coding RNA 1465 . . . . . . . . . . . LINC01467 . . . long intergenic non-protein coding RNA 1467 . . . . . . . . . . . LINC01468 . . . long intergenic non-protein coding RNA 1468 . . . . . . . . . . . LINC01470 . . . long intergenic non-protein coding RNA 1470 . . . . . . . . . . . LINC01471 . . . long intergenic non-protein coding RNA 1471 . . . . . . . . . . . LINC01473 . . . long intergenic non-protein coding RNA 1473 . . . . . . . . . . . LINC01474 . . . long intergenic non-protein coding RNA 1474 . . . . . . . . . . . LINC01475 . . . long intergenic non-protein coding RNA 1475 . . . . . . . . . . . LINC01476 . . . long intergenic non-protein coding RNA 1476 . . . . . . . . . . . LINC01477 . . . long intergenic non-protein coding RNA 1477 . . . . . . . . . . . LINC01478 . . . long intergenic non-protein coding RNA 1478 . . . . . . . . . . . LINC01479 . . . long intergenic non-protein coding RNA 1479 . . . . . . . . . . . LINC01480 . . . long intergenic non-protein coding RNA 1480 . . . . . . . . . . . LINC01481 . . . long intergenic non-protein coding RNA 1481 . . . . . . . . . . . LINC01482 . . . long intergenic non-protein coding RNA 1482 . . . . . . . . . . . LINC01483 . . . long intergenic non-protein coding RNA 1483 . . . . . . . . . . . LINC01484 . . . long intergenic non-protein coding RNA 1484 . . . . . . . . . . . LINC01485 . . . long intergenic non-protein coding RNA 1485 . . . . . . . . . . . LINC01486 . . . long intergenic non-protein coding RNA 1486 . . . . . . . . . . . LINC01487 . . . long intergenic non-protein coding RNA 1487 . . . . . . . . . . . LINC01488 . . . long intergenic non-protein coding RNA 1488 . . . . . . . . . . . LINC01489 . . . long intergenic non-protein coding RNA 1489 . . . . . . . . . . . LINC01490 . . . long intergenic non-protein coding RNA 1490 . . . . . . . . . . . LINC01491 . . . long intergenic non-protein coding RNA 1491 . . . . . . . . . . . LINC01492 . . . long intergenic non-protein coding RNA 1492 . . . . . . . . . . . LINC01493 . . . long intergenic non-protein coding RNA 1493 . . . . . . . . . . . LINC01494 . . . long intergenic non-protein coding RNA 1494 . . . . . . . . . . . LINC01495 . . . long intergenic non-protein coding RNA 1495 . . . . . . . . . . . LINC01496 . . . long intergenic non-protein coding RNA 1496 . . . . . . . . . . . LINC01497 . . . long intergenic non-protein coding RNA 1497 . . . . . . . . . . . LINC01498 . . . long intergenic non-protein coding RNA 1498 . . . . . . . . . . . LINC01499 . . . long intergenic non-protein coding RNA 1499 . . . . . . . . . . . LINC01500 . . . long intergenic non-protein coding RNA 1500 . . . . . . . . . . . LINC01501 . . . long intergenic non-protein coding RNA 1501 . . . . . . . . . . . LINC01502 . . . long intergenic non-protein coding RNA 1502 . . . . . . . . . . . LINC01503 . . . long intergenic non-protein coding RNA 1503 . . . . . . . . . . . LINC01504 . . . long intergenic non-protein coding RNA 1504 . . . . . . . . . . . LINC01505 . . . long intergenic non-protein coding RNA 1505 . . . . . . . . . . . LINC01506 . . . long intergenic non-protein coding RNA 1506 . . . . . . . . . . . LINC01507 . . . long intergenic non-protein coding RNA 1507 . . . . . . . . . . . LINC01508 . . . long intergenic non-protein coding RNA 1508 . . . . . . . . . . . LINC01509 . . . long intergenic non-protein coding RNA 1509 . . . . . . . . . . . LINC01510 . . . long intergenic non-protein coding RNA 1510 . . . . . . . . . . . LINC01511 . . . long intergenic non-protein coding RNA 1511 . . . . . . . . . . . LINC01512 . . . long intergenic non-protein coding RNA 1512 . . . . . . . . . . . LINC01513 . . . long intergenic non-protein coding RNA 1513 . . . . . . . . . . . LINC01514 . . . long intergenic non-protein coding RNA 1514 . . . . . . . . . . . LINC01515 . . . long intergenic non-protein coding RNA 1515 . . . . . . . . . . . LINC01516 . . . long intergenic non-protein coding RNA 1516 . . . . . . . . . . . LINC01517 . . . long intergenic non-protein coding RNA 1517 . . . . . . . . . . . LINC01518 . . . long intergenic non-protein coding RNA 1518 . . . . . . . . . . . LINC01519 . . . long intergenic non-protein coding RNA 1519 . . . . . . . . . . . LINC01520 . . . long intergenic non-protein coding RNA 1520 . . . . . . . . . . . LINC01521 . . . long intergenic non-protein coding RNA 1521 . . . . . . . . . . . LINC01522 . . . long intergenic non-protein coding RNA 1522 . . . . . . . . . . . LINC01523 . . . long intergenic non-protein coding RNA 1523 . . . . . . . . . . . LINC01524 . . . long intergenic non-protein coding RNA 1524 . . . . . . . . . . . LINC01525 . . . long intergenic non-protein coding RNA 1525 . . . . . . . . . . . LINC01526 . . . long intergenic non-protein coding RNA 1526 . . . . . . . . . . . LINC01527 . . . long intergenic non-protein coding RNA 1527 . . . . . . . . . . . LINC01529 . . . long intergenic non-protein coding RNA 1529 . . . . . . . . . . . LINC01530 . . . long intergenic non-protein coding RNA 1530 . . . . . . . . . . . LINC01531 . . . long intergenic non-protein coding RNA 1531 . . . . . . . . . . . LINC01532 . . . long intergenic non-protein coding RNA 1532 . . . . . . . . . . . LINC01533 . . . long intergenic non-protein coding RNA 1533 . . . . . . . . . . . LINC01534 . . . long intergenic non-protein coding RNA 1534 . . . . . . . . . . . LINC01535 . . . long intergenic non-protein coding RNA 1535 . . . . . . . . . . . LINC01537 . . . long intergenic non-protein coding RNA 1537 . . . . . . . . . . . LINC01538 . . . long intergenic non-protein coding RNA 1538 . . . . . . . . . . . LINC01539 . . . long intergenic non-protein coding RNA 1539 . . . . . . . . . . . LINC01541 . . . long intergenic non-protein coding RNA 1541 . . . . . . . . . . . LINC01543 . . . long intergenic non-protein coding RNA 1543 . . . . . . . . . . . LINC01544 . . . long intergenic non-protein coding RNA 1544 . . . . . . . . . . . LINC01545 . . . long intergenic non-protein coding RNA 1545 . . . . . 0.10927 . . . . . LINC01546 . . . long intergenic non-protein coding RNA 1546 . . . . . . . . . . . LINC01547 . . . long intergenic non-protein coding RNA 1547 . . TISSUE SPECIFICITY: Not detected in any tissue tested.; . . 0.08870 . . . . . LINC01548 . . . long intergenic non-protein coding RNA 1548 . . . . . . . . . . . LINC01549 . . . long intergenic non-protein coding RNA 1549 . . . . . . . . . . . LINC01550 . . . long intergenic non-protein coding RNA 1550 . . . . . . . . . . . LINC01551 . . . long intergenic non-protein coding RNA 1551 . . . . . . . . . . . LINC01553 . . . long intergenic non-protein coding RNA 1553 . . . . . . . . . . . LINC01554 . . . long intergenic non-protein coding RNA 1554 . . . . . . . . . . . LINC01555 . . . long intergenic non-protein coding RNA 1555 . . . . . 0.13035 . . . . . LINC01556 . . . long intergenic non-protein coding RNA 1556 . . . . . 0.06774 . . . . . LINC01558 . . . long intergenic non-protein coding RNA 1558 . . . . . . . . . . . LINC01559 . . . long intergenic non-protein coding RNA 1559 . . . . . 0.07956 . . . . . LINC01560 . . . long intergenic non-protein coding RNA 1560 . . . . . 0.06430 . . . . . LINC01561 . . . long intergenic non-protein coding RNA 1561 . . . . . 0.02061 . . . . . LINC01562 . . . long intergenic non-protein coding RNA 1562 . . . . . . . . . . . LINC01563 . . . long intergenic non-protein coding RNA 1563 . . . . . . . . . . . LINC01564 . . . long intergenic non-protein coding RNA 1564 . . . . . . . . . . . LINC01565 . . . long intergenic non-protein coding RNA 1565 . . TISSUE SPECIFICITY: Expressed in fetus (aged from 7 to 8 weeks). Weakly expressed in lymphocytes. {ECO:0000269|PubMed:9307271}.; . . 0.13427 . 0.082802743 60.09082331 . . LINC01566 . . . long intergenic non-protein coding RNA 1566 . . . . . . . . . . . LINC01567 . . . long intergenic non-protein coding RNA 1567 . . . . . . . . . . . LINC01568 . . . long intergenic non-protein coding RNA 1568 . . . . . . . . . . . LINC01569 . . . long intergenic non-protein coding RNA 1569 . . . . . . . . . . . LINC01570 . . . long intergenic non-protein coding RNA 1570 . . . . . . . . . . . LINC01571 . . . long intergenic non-protein coding RNA 1571 . . . . . . . . . . . LINC01572 . . . long intergenic non-protein coding RNA 1572 . . . . . . . . . . . LINC01574 . . . long intergenic non-protein coding RNA 1574 . . . . . . . . . . . LINC01578 . . . long intergenic non-protein coding RNA 1578 . . . . . . . . . . . LINC01579 . . . long intergenic non-protein coding RNA 1579 . . . . . . . . . . . LINC01580 . . . long intergenic non-protein coding RNA 1580 . . . . . . . . . . . LINC01581 . . . long intergenic non-protein coding RNA 1581 . . . . . . . . . . . LINC01582 . . . long intergenic non-protein coding RNA 1582 . . . . . . . . . . . LINC01583 . . . long intergenic non-protein coding RNA 1583 . . . . . . . . . . . LINC01584 . . . long intergenic non-protein coding RNA 1584 . . . . . . . . . . . LINC01585 . . . long intergenic non-protein coding RNA 1585 . . . . . . . . . . . LINC01586 . . . long intergenic non-protein coding RNA 1586 . . . . . . . . . . . LINC01587 . . . long intergenic non-protein coding RNA 1587 . . TISSUE SPECIFICITY: Expressed in neuroblastoma.; . . 0.09950 . 0.215080721 67.91696155 . . LINC01588 . . . long intergenic non-protein coding RNA 1588 . . . . . . . 0.501689326 79.7888653 . . LINC01589 . . . long intergenic non-protein coding RNA 1589 . . . . . . . . . . . LINC01590 . . . long intergenic non-protein coding RNA 1590 . . . . . 0.07530 . . . . . LINC01591 . . . long intergenic non-protein coding RNA 1591 . . . . . . . . . . . LINC01592 . . . long intergenic non-protein coding RNA 1592 . . . . . . . . . . . LINC01593 . . . long intergenic non-protein coding RNA 1593 . . . . . . . . . . . LINC01594 . . . long intergenic non-protein coding RNA 1594 . . . . . . . . . . . LINC01595 . . . long intergenic non-protein coding RNA 1595 . . . . . . . . . . . LINC01596 . . . long intergenic non-protein coding RNA 1596 . . . . . . . . . . . LINC01597 . . . long intergenic non-protein coding RNA 1597 . . . . . . . . . . . LINC01598 . . . long intergenic non-protein coding RNA 1598 . . . . . . . . . . . LINC01599 . . . long intergenic non-protein coding RNA 1599 . . . . . . . 0.284856336 71.40835103 . . LINC01600 . . . long intergenic non-protein coding RNA 1600 . . . . . 0.01417 . 1.060147109 91.46614768 . . LINC01601 . . . long intergenic non-protein coding RNA 1601 . . . . . . . . . . . LINC01602 . . . long intergenic non-protein coding RNA 1602 . . . . . . . . . . . LINC01603 . . . long intergenic non-protein coding RNA 1603 . . . . . . . . . . . LINC01605 . . . long intergenic non-protein coding RNA 1605 . . . . . . . . . . . LINC01606 . . . long intergenic non-protein coding RNA 1606 . . . . . . . . . . . LINC01607 . . . long intergenic non-protein coding RNA 1607 . . . . . . . . . . . LINC01608 . . . long intergenic non-protein coding RNA 1608 . . . . . . . . . . . LINC01609 . . . long intergenic non-protein coding RNA 1609 . . . . . . . . . . . LINC01611 . . . long intergenic non-protein coding RNA 1611 . . . . . . . . . . . LINC01612 . . . long intergenic non-protein coding RNA 1612 . . . . . . . . . . . LINC01613 . . . long intergenic non-protein coding RNA 1613 . . . . . . . . . . . LINC01614 . . . long intergenic non-protein coding RNA 1614 . . . . . . . . . . . LINC01615 . . . long intergenic non-protein coding RNA 1615 . . . . . . . . . . . LINC01616 . . . long intergenic non-protein coding RNA 1616 . . . . . . . . . . . LINC01617 . . . long intergenic non-protein coding RNA 1617 . . . . . . . . . . . LINC01618 . . . long intergenic non-protein coding RNA 1618 . . . . . . . . . . . LINC01619 . . . long intergenic non-protein coding RNA 1619 . . . . . . . . . . . LINC01620 . . . long intergenic non-protein coding RNA 1620 . . . . . 0.09932 . . . . . LINC01621 . . . long intergenic non-protein coding RNA 1621 . . . . . . . . . . . LINC01622 . . . long intergenic non-protein coding RNA 1622 . . . . . . . . . . . LINC01623 . . . long intergenic non-protein coding RNA 1623 . . . . . . . . . . . LINC01624 . . . long intergenic non-protein coding RNA 1624 . . . . . . . . . . . LINC01625 . . . long intergenic non-protein coding RNA 1625 . . . . . . . . . . . LINC01626 . . . long intergenic non-protein coding RNA 1626 . . . . . . . . . . . LINC01627 . . . long intergenic non-protein coding RNA 1627 . . . . . . . . . . . LINC01628 . . . long intergenic non-protein coding RNA 1628 . . . . . . . . . . . LINC01629 . . . long intergenic non-protein coding RNA 1629 . . . . . . . . . . . LINCMD1 . . . long intergenic non-protein coding RNA, muscle differentiation 1 . . . . . . . . . . . LINGO1 0.952116231457105 0.0477444248934454 0.000139343649450088 leucine rich repeat and Ig domain containing 1 FUNCTION: Functional component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors (PubMed:14966521, PubMed:15694321). Is also an important negative regulator of oligodentrocyte differentiation and axonal myelination (PubMed:15895088). Acts in conjunction with RTN4 and RTN4R in regulating neuronal precursor cell motility during cortical development (By similarity). {ECO:0000250|UniProtKB:Q9D1T0, ECO:0000269|PubMed:14966521, ECO:0000269|PubMed:15694321, ECO:0000269|PubMed:15895088}.; . TISSUE SPECIFICITY: Expressed exclusively in the central nervous system. Highest level in the in amygdala, hippocampus, thalamus and cerebral cortex. In the rest of the brain a basal expression seems to be always present. Up-regulated in substantia nigra neurons from Parkinson disease patients. {ECO:0000269|PubMed:14686891, ECO:0000269|PubMed:15895088, ECO:0000269|PubMed:17726113}.; unclassifiable (Anatomical System);heart;hypothalamus;colon;skin;retina;uterus;frontal lobe;placenta;hippocampus;visual apparatus;iris;testis;brain; occipital lobe;trigeminal ganglion;cingulate cortex; 0.79024 0.17010 -1.42004951 4.104741684 25.40567 0.82910 LINGO1-AS1 . . . LINGO1 antisense RNA 1 . . . . . . . . . . . LINGO1-AS2 . . . LINGO1 antisense RNA 2 . . . . . . . . . . . LINGO2 0.807167303861535 0.19177565643363 0.00105703970483544 leucine rich repeat and Ig domain containing 2 . . . breast;uterus;heart;thyroid;placenta;brain;skin; subthalamic nucleus;superior cervical ganglion;temporal lobe;pons;skeletal muscle;cingulate cortex;parietal lobe; 0.94147 0.12751 -0.753139731 13.67067705 77.25303 1.84556 LINGO3 . . . leucine rich repeat and Ig domain containing 3 . . . . . . . . . 2438.11731 9.17677 LINGO4 0.00285409743434757 0.804361646836252 0.1927842557294 leucine rich repeat and Ig domain containing 4 . . . . . 0.12097 0.26787 -0.288341872 33.41589998 1669.58145 7.54261 LINS1 . . . lines homolog 1 . . TISSUE SPECIFICITY: Expressed in adult testis, prostate, prostate, spleen, thymus, skeletal muscle, fetal kidney and brain. {ECO:0000269|PubMed:12119551}.; . . 0.10673 0.08727 1.026965723 91.08870017 . . LIPA 0.0112778036759298 0.979948141957582 0.00877405436648853 lipase A, lysosomal acid type FUNCTION: Crucial for the intracellular hydrolysis of cholesteryl esters and triglycerides that have been internalized via receptor- mediated endocytosis of lipoprotein particles. Important in mediating the effect of LDL (low density lipoprotein) uptake on suppression of hydroxymethylglutaryl-CoA reductase and activation of endogenous cellular cholesteryl ester formation.; DISEASE: Wolman disease (WOD) [MIM:278000]: A severe manifestation of LIPA deficiency, leading to the accumulation of cholesteryl esters and triglycerides in most tissues of the body. WD occurs in infancy and is nearly always fatal before the age of 1 year. {ECO:0000269|PubMed:8146180}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cholesteryl ester storage disease (CESD) [MIM:278000]: A mild manifestation of LIPA deficiency, leading to the accumulation of cholesteryl esters and triglycerides in most tissues of the body. It is characterized by late-onset. {ECO:0000269|PubMed:8146180, ECO:0000269|PubMed:9633819}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;gum;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;kidney;aorta;stomach; medulla oblongata;superior cervical ganglion;occipital lobe;fetal liver;lymph node;adipose tissue;hypothalamus;spinal cord;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.10045 0.16605 0.150760231 64.51403633 2834.36604 10.05767 LIPB . . . lipase B, lysosomal acid type . . . . . . . . . . . LIPC 0.000171127202456162 0.970777614318492 0.0290512584790523 lipase C, hepatic type FUNCTION: Hepatic lipase has the capacity to catalyze hydrolysis of phospholipids, mono-, di-, and triglycerides, and acyl-CoA thioesters. It is an important enzyme in HDL metabolism. Hepatic lipase binds heparin.; DISEASE: Hepatic lipase deficiency (HL deficiency) [MIM:614025]: A disorder characterized by elevated levels of beta-migrating very low density lipoproteins, and abnormally triglyceride-rich low and high density lipoproteins. {ECO:0000269|PubMed:10660332, ECO:0000269|PubMed:1301939}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;heart;salivary gland;muscle;lung;bone;visual apparatus;liver;testis;spleen;cervix;kidney;tonsil;stomach; fetal liver;superior cervical ganglion;liver;atrioventricular node;trigeminal ganglion; 0.51036 0.36061 -0.705410796 14.77942911 112.71223 2.30929 LIPE 5.7325054658036e-09 0.844982480446884 0.15501751382061 lipase E, hormone sensitive type FUNCTION: In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production.; DISEASE: Lipodystrophy, familial partial, 6 (FPLD6) [MIM:615980]: A form of lipodystrophy characterized by abnormal subcutaneous fat distribution. Affected individuals have increased visceral fat, impaired lipolysis, dyslipidemia, hepatic steatosis, systemic insulin resistance, and diabetes. Some patients manifest muscular dystrophy. {ECO:0000269|PubMed:24848981}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);medulla oblongata;ovary;islets of Langerhans;colon;blood;fovea centralis;choroid;lens;retina;bone marrow;pancreas;prostate;optic nerve;lung;cerebral cortex;bone;macula lutea;testis;germinal center;kidney;brain;mammary gland; whole brain;occipital lobe;superior cervical ganglion;testis - interstitial;adipose tissue;spinal cord;adrenal cortex;atrioventricular node;testis - seminiferous tubule;adrenal gland;testis;ciliary ganglion;cingulate cortex; 0.19237 0.53191 0.547404288 81.13352206 859.94228 5.71910 LIPE-AS1 . . . LIPE antisense RNA 1 . . . . . . . . . . . LIPF 0.000753524618867874 0.924303489757166 0.0749429856239664 lipase F, gastric type . . . unclassifiable (Anatomical System);oesophagus;stomach; superior cervical ganglion;skeletal muscle; 0.06971 0.09918 0.505321956 80.00707714 1838.90283 7.90676 LIPG 8.35570265503166e-05 0.927203963992445 0.0727124789810051 lipase G, endothelial type FUNCTION: Has phospholipase and triglyceride lipase activities. Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins. Binds heparin.; . TISSUE SPECIFICITY: High level of expression in the liver, placenta, lung, thyroid, kidney, testis and in the corpus luteum of the ovary. Expressed also in coronary artery endothelial cells, umbilical vein endothelial cells and in hepatocytes and osteosarcoma cell lines. Not detected in heart, brain and muscle.; unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;colon;parathyroid;fovea centralis;skeletal muscle;breast;uterus;prostate;pancreas;whole body;lung;endometrium;oesophagus;epididymis;larynx;thyroid;placenta;macula lutea;liver;testis;head and neck;spleen;kidney;brain;stomach; superior cervical ganglion;smooth muscle;thyroid;placenta;pons;fetal thyroid;trigeminal ganglion; 0.18042 0.33572 0.486911049 79.46449634 1119.01613 6.38691 LIPH 2.13279458867521e-06 0.704506424756168 0.295491442449243 lipase H FUNCTION: Hydrolyzes specifically phosphatidic acid (PA) to produce 2-acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and fatty acid. Does not hydrolyze other phospholipids, like phosphatidylserine (PS), phosphatidylcholine (PC) and phosphatidylethanolamine (PE) or triacylglycerol (TG). {ECO:0000269|PubMed:12063250, ECO:0000269|PubMed:12963729}.; DISEASE: Woolly hair autosomal recessive 2 (ARWH2) [MIM:604379]: A hair shaft disorder characterized by fine and tightly curled hair. Compared to normal curly hair that is observed in some populations, woolly hair grows slowly and stops growing after a few inches. Under light microscopy, woolly hair shows some structural anomalies, including trichorrhexis nodosa and tapered ends. Some individuals may present with hypotrichosis. {ECO:0000269|PubMed:18830268}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Present in intestine (at protein level). Expressed in colon, prostate, kidney, pancreas, ovary, testis, intestine, lung and pancreas. Expressed at lower level in brain, spleen and heart. In hair, it is prominently expressed in hair follicles, including the stem cell-rich bulge region. {ECO:0000269|PubMed:12063250, ECO:0000269|PubMed:12213196, ECO:0000269|PubMed:12719377, ECO:0000269|PubMed:17095700}.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;blood;skin;skeletal muscle;uterus;pancreas;prostate;lung;nasopharynx;testis;stomach; atrioventricular node;skeletal muscle; 0.07005 . -0.314027422 31.9297004 109.3667 2.27204 LIPI 8.82542393516549e-09 0.158292274441953 0.841707716732623 lipase I FUNCTION: Hydrolyzes specifically phosphatidic acid (PA) to produce 2-acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and fatty acid. Does not hydrolyze other phospholipids, like phosphatidylserine (PS), phosphatidylcholine (PC) and phosphatidylethanolamine (PE) or triacylglycerol (TG). {ECO:0000269|PubMed:12963729}.; . TISSUE SPECIFICITY: Expressed in testis. Expressed exclusively at the connecting piece of the sperm. {ECO:0000269|PubMed:12719377, ECO:0000269|PubMed:12963729}.; unclassifiable (Anatomical System);lung;testis; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skin; 0.19156 . 1.197888504 92.95234725 4222.43767 12.93065 LIPJ 2.64340955679906e-07 0.294180629301256 0.705819106357788 lipase family member J . . . . . 0.09431 0.09134 1.396334339 94.70393961 631.96983 5.06565 LIPK 1.19029209489596e-08 0.186219598551197 0.813780389545882 lipase family member K FUNCTION: Plays a highly specific role in the last step of keratinocyte differentiation. May have an essential function in lipid metabolism of the most differentiated epidermal layers. {ECO:0000269|PubMed:17562024}.; . TISSUE SPECIFICITY: Exclusively expressed in the epidermis within the granular keratinocytes. {ECO:0000269|PubMed:17562024}.; . . 0.32646 0.09611 0.795569043 87.49115357 2178.36835 8.59800 LIPM 0.169253544600704 0.641874254738625 0.188872200660671 lipase family member M FUNCTION: Plays a highly specific role in the last step of keratinocyte differentiation. May have an essential function in lipid metabolism of the most differentiated epidermal layers. {ECO:0000269|PubMed:17562024}.; . TISSUE SPECIFICITY: Exclusively expressed in the epidermis within the granular keratinocytes. {ECO:0000269|PubMed:17562024}.; . . 0.19120 0.10251 0.61555716 83.13871196 653.58744 5.12956 LIPN 1.70698681214155e-07 0.234972515288598 0.76502731401272 lipase family member N FUNCTION: Plays a highly specific role in the last step of keratinocyte differentiation. May have an essential function in lipid metabolism of the most differentiated epidermal layers. {ECO:0000269|PubMed:17562024}.; DISEASE: Ichthyosis, congenital, autosomal recessive 8 (ARCI8) [MIM:613943]: A form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non-bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs. {ECO:0000269|PubMed:21439540}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in the epidermis in the granular keratinocytes. Also detected in other tissues, although at much lower levels, including lung and spleen. {ECO:0000269|PubMed:17562024, ECO:0000269|PubMed:21439540}.; . . 0.16098 . 0.597144447 82.7435716 402.09177 4.20686 LIPT1 6.17016770936916e-05 0.278077804203859 0.721860494119047 lipoyltransferase 1 FUNCTION: Catalyzes the transfer of the lipoyl group from lipoyl- AMP to the specific lysine residue of lipoyl domains of lipoate- dependent enzymes. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle and heart, moderately in kidney and pancreas, and detected at lower levels in liver, brain, placenta and lung. {ECO:0000269|PubMed:10103005}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;skin;uterus;breast;lung;thyroid;bone;testis;germinal center;kidney;brain; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node;parietal lobe; 0.12505 0.18216 -0.271755481 34.31823543 96.16612 2.11998 LIPT1P1 . . . lipoyltransferase 1 pseudogene 1 . . . . . . . . . . . LIPT2 . . . lipoyl(octanoyl) transferase 2 (putative) FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);skin;retina; . . . . . 1461.89585 7.13144 LITAF 0.313932119355222 0.615760583994144 0.0703072966506346 lipopolysaccharide-induced TNF factor FUNCTION: Probable role in regulating transcription of specific genes. May regulate through NFKB1 the expression of the CCL2/MCP-1 chemokine. May play a role in tumor necrosis factor alpha (TNF- alpha) gene expression.; DISEASE: Charcot-Marie-Tooth disease 1C (CMT1C) [MIM:601098]: A dominant demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot- Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. {ECO:0000269|PubMed:12525712, ECO:0000269|PubMed:15776429, ECO:0000269|PubMed:15786462}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in LITAF may be involved in extramammary Paget disease (EMPD) carcinogenesis. EMPD is a cancerous disease representing about 8% of all malignant skin cancers; it usually appears in the anogenital area and can be fatal by metastasizing to internal organs when left untreated for a long time. The clinical features are usually those of eczematous eruptions with weeping and crust formation. {ECO:0000269|PubMed:15197774}.; TISSUE SPECIFICITY: Ubiquitously and abundantly expressed. Expressed predominantly in the placenta, peripheral blood leukocytes, lymph nodes and spleen. {ECO:0000269|PubMed:10200294, ECO:0000269|PubMed:11274176}.; ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;placenta;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;olfactory bulb;trachea;placenta;ciliary ganglion;white blood cells;whole blood;trigeminal ganglion;bone marrow; 0.25348 0.20681 -0.049474214 50.01179523 22.0807 0.74156 LIX1 0.0166746879363502 0.959813014684849 0.0235122973788007 limb and CNS expressed 1 . . . unclassifiable (Anatomical System);ovary;hypothalamus;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;placenta;macula lutea;hippocampus;kidney;brain;ciliary body; superior cervical ganglion;spinal cord;trigeminal ganglion; 0.19106 0.11118 -0.249709319 35.74545883 31.6193 0.99482 LIX1L 0.116630313625694 0.877646880276628 0.00572280609767819 limb and CNS expressed 1 like . . . . . 0.44071 0.11262 -0.141298762 42.87567823 68.92383 1.72036 LKAAEAR1 . . . LKAAEAR motif containing 1 . . . . . . . . . . . LLGL1 0.977463207224722 0.0225367854637984 7.31148012663045e-09 lethal giant larvae homolog 1, scribble cell polarity complex component FUNCTION: Cortical cytoskeleton protein found in a complex involved in maintaining cell polarity and epithelial integrity. Involved in the regulation of mitotic spindle orientation, proliferation, differentiation and tissue organization of neuroepithelial cells. Involved in axonogenesis through RAB10 activation thereby regulating vesicular membrane trafficking toward the axonal plasma membrane. {ECO:0000269|PubMed:15735678, ECO:0000269|PubMed:16170365}.; . TISSUE SPECIFICITY: Expressed in brain, kidney, and muscle but is barely seen in heart and placenta. Down-regulated or lost in all cell lines and in most of the tumor samples analyzed. Loss was associated with advanced stage of the disease. {ECO:0000269|PubMed:15735678, ECO:0000269|PubMed:16170365, ECO:0000269|PubMed:7542763}.; ovary;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;lens;pancreas;lung;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18438 0.13272 -1.738187109 2.429818353 362.43498 4.03089 LLGL2 8.27305979414576e-07 0.999084867964045 0.000914304729975156 lethal giant larvae homolog 2, scribble cell polarity complex component FUNCTION: Part of a complex with GPSM2/LGN, PRKCI/aPKC and PARD6B/Par-6, which may ensure the correct organization and orientation of bipolar spindles for normal cell division. This complex plays roles in the initial phase of the establishment of epithelial cell polarity. {ECO:0000269|PubMed:15632202}.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;head and neck;cervix;kidney;stomach;cerebellum; kidney; . . 1.04528704 91.31280962 9919.23727 21.67473 LLPH 0.341447375249415 0.600039804125773 0.0585128206248122 LLP homolog, long-term synaptic facilitation (Aplysia) . . . colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;cerebellum cortex;islets of Langerhans;hypothalamus;blood;skeletal muscle;lung;nasopharynx;placenta;liver;cervix;kidney;stomach; . 0.22342 . 0.235309407 68.71903751 436.00348 4.35442 LLPH-AS1 . . . LLPH antisense RNA 1 (head to head) . . . . . . . . . . . LLPHP1 . . . LLP homolog, long-term synaptic facilitation (Aplysia) pseudogene 1 . . . . . . . . . . . LLPHP2 . . . LLP homolog, long-term synaptic facilitation (Aplysia) pseudogene 2 . . . . . . . . . . . LMAN1 0.486069838864669 0.513889662526844 4.04986084872227e-05 lectin, mannose binding 1 FUNCTION: Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. {ECO:0000269|PubMed:12717434, ECO:0000269|PubMed:13130098}.; DISEASE: Factor V and factor VIII combined deficiency 1 (F5F8D1) [MIM:227300]: A blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal. {ECO:0000269|PubMed:10090935, ECO:0000269|PubMed:19787799}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:13130098}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;lung;cornea;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.10190 0.17526 -0.045835247 50.34206181 760.68404 5.46719 LMAN1L 1.8808952583686e-09 0.228054068996172 0.771945929122933 lectin, mannose binding 1 like . . TISSUE SPECIFICITY: Highly expressed in normal and neoplastic prostate. Also expressed in cardiac atrium, salivary gland, spleen and selective cells in the CNS. {ECO:0000269|PubMed:11255007}.; unclassifiable (Anatomical System);prostate;cerebellum; prostate; 0.05079 0.09240 0.933309256 89.82661005 2073.79173 8.38925 LMAN2 0.0500442996260229 0.927871421051474 0.022084279322503 lectin, mannose binding 2 FUNCTION: Plays a role as an intracellular lectin in the early secretory pathway. Interacts with N-acetyl-D-galactosamine and high-mannose type glycans and may also bind to O-linked glycans. Involved in the transport and sorting of glycoproteins carrying high mannose-type glycans (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;duodenum;kidney;stomach; superior cervical ganglion;testis - seminiferous tubule;thyroid;liver;testis; 0.12943 0.14229 -0.754958418 13.57631517 88.77601 2.02091 LMAN2L 1.28590577344366e-07 0.356817102767415 0.643182768642007 lectin, mannose binding 2 like FUNCTION: May be involved in the regulation of export from the endoplasmic reticulum of a subset of glycoproteins. May function as a regulator of ERGIC-53. {ECO:0000269|PubMed:12878160}.; . TISSUE SPECIFICITY: Expressed in numerous tissues. Highest expression in skeletal muscle and kidney, intermediate levels in heart, liver and placenta, low levels in brain, thymus, spleen, small intestine and lung. {ECO:0000269|PubMed:12878160}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; . 0.21755 0.12712 -0.648365105 16.35999056 21.85645 0.73498 LMBR1 0.000687935571767197 0.998458121316073 0.00085394311215967 limb development membrane protein 1 FUNCTION: Putative membrane receptor.; DISEASE: Acheiropody (ACHP) [MIM:200500]: Very rare condition characterized by bilateral congenital amputations of the hands and feet. The specific malformative phenotype consists of a complete amputation of the distal epiphysis of the humerus, amputation of the tibial diaphysis and aplasia of the radius, ulna, fibula and of all the bones of the hands and feet. {ECO:0000269|PubMed:11090342}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Syndactyly 4 (SDTY4) [MIM:186200]: A form of syndactyly, a congenital anomaly of the hand or foot marked by persistence of the webbing between adjacent digits that are more or less completely attached. SDTY4 is characterized by complete bilateral syndactyly (involving all digits 1 to 5). A frequent association with polydactyly (with six metacarpals and six digits) has been reported. Feet are affected occasionally. {ECO:0000269|PubMed:18417549, ECO:0000269|PubMed:24456159}. Note=The disease is caused by mutations affecting the gene represented in this entry. Disease-causing mutations consists of duplications (89-589 kb) involving the ZPA regulatory sequence (ZRS), a SHH long-range cis-regulatory element, located in LMBR1 intron 5. The mutations do not alter normal LMBR1 expression and function, but affect SHH limb expression. {ECO:0000269|PubMed:24456159}.; DISEASE: Hypoplasia or aplasia of tibia with polydactyly (THYP) [MIM:188740]: An autosomal dominant disease characterized by hypoplastic or absent tibia, and polydactyly. {ECO:0000269|PubMed:19847792, ECO:0000269|PubMed:24777739, ECO:0000269|PubMed:24965254}. Note=The disease is caused by mutations affecting the gene represented in this entry. Disease- causing mutations are located in intron 5 of LMBR1. The mutations do not alter normal LMBR1 expression and function, but disrupt a long-range, cis-regulatory element of SHH expression contained in LMBR1 intron 5. {ECO:0000269|PubMed:19847792, ECO:0000269|PubMed:24777739, ECO:0000269|PubMed:24965254}.; DISEASE: Laurin-Sandrow syndrome (LSS) [MIM:135750]: A rare autosomal dominant disorder characterized by polysyndactyly of hands and/or feet, mirror image duplication of the feet, nasal defects, and loss of identity between fibula and tibia. Some patients do not have nasal abnormalities (segmental Laurin-Sandrow syndrome). {ECO:0000269|PubMed:24456159}. Note=The disease is caused by mutations affecting the gene represented in this entry. Disease-causing mutations consists of duplications (16-75 kb) involving the ZPA regulatory sequence (ZRS), a SHH long-range cis- regulatory element, located in LMBR1 intron 5. The mutations do not alter normal LMBR1 expression and function, but affect SHH limb expression. {ECO:0000269|PubMed:24456159}.; TISSUE SPECIFICITY: Widely expressed with strongest expression in heart and pancreas. {ECO:0000269|PubMed:10329000}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;lens;breast;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;duodenum;liver;spleen;head and neck;kidney;aorta;stomach; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.24736 0.12777 -0.53631094 20.53550366 220.61793 3.21210 LMBR1L 2.18323454000279e-06 0.974231011590121 0.0257668051753389 limb development membrane protein 1 like FUNCTION: Probable LCN1 receptor. May mediate LCN1 endocytosis. {ECO:0000269|PubMed:11287427, ECO:0000269|PubMed:12591932}.; . TISSUE SPECIFICITY: Expressed in testis, pituitary gland, adrenal gland, trachea, placenta, thymus, cerebellum, stomach, mammary gland, spinal cord. A weaker expression is detected in colon, pancreas, and prostate. {ECO:0000269|PubMed:11287427}.; medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;synovium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;head and neck;cervix;kidney;stomach;aorta;cerebellum;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.31339 0.10191 -0.646543901 16.44255721 178.30546 2.90327 LMBRD1 1.94347159526564e-06 0.969877437918152 0.0301206186102525 LMBR1 domain containing 1 FUNCTION: Probable lysosomal cobalamin transporter. Required to export cobalamin from lysosomes allowing its conversion to cofactors. Isoform 3 may play a role in the assembly of hepatitis delta virus (HDV). {ECO:0000269|PubMed:15956556, ECO:0000269|PubMed:19136951}.; DISEASE: Methylmalonic aciduria and homocystinuria type cblF (MMAHCF) [MIM:277380]: A disorder of cobalamin metabolism characterized by decreased levels of the coenzymes adenosylcobalamin (AdoCbl) and methylcobalamin (MeCbl). It is due to accumulation of free cobalamin in lysosomes, thus hindering its conversion to cofactors. Clinical features include developmental delay, stomatitis, glossitis, seizures and methylmalonic aciduria responsive to vitamin B12. {ECO:0000269|PubMed:19136951}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 3 is expressed in liver. {ECO:0000269|PubMed:15956556}.; . . 0.23148 0.10271 -0.558357437 19.54470394 2687.0579 9.75144 LMBRD2 0.0145652183487776 0.985383752765856 5.10288853664539e-05 LMBR1 domain containing 2 . . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;skeletal muscle;skin;retina;uterus;prostate;lung;thyroid;liver;testis;germinal center;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.17368 . -0.402212257 26.7338995 76.76148 1.83911 LMCD1 0.376043791136965 0.621682497408368 0.00227371145466678 LIM and cysteine rich domains 1 FUNCTION: Transcriptional cofactor that restricts GATA6 function by inhibiting DNA-binding, resulting in repression of GATA6 transcriptional activation of downstream target genes. Represses GATA6-mediated trans activation of lung- and cardiac tissue- specific promoters. Inhibits DNA-binding by GATA4 and GATA1 to the cTNC promoter (By similarity). Plays a critical role in the development of cardiac hypertrophy via activation of calcineurin/nuclear factor of activated T-cells signaling pathway. {ECO:0000250, ECO:0000269|PubMed:20026769}.; . TISSUE SPECIFICITY: Expressed in the heart (at protein level). Expressed in many tissues with highest abundance in skeletal muscle. {ECO:0000269|PubMed:20026769}.; smooth muscle;ovary;developmental;colon;parathyroid;choroid;skin;uterus;prostate;whole body;cerebral cortex;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;skeletal muscle; 0.20507 0.11381 -0.179930907 40.35739561 161.70706 2.77813 LMCD1-AS1 . . . LMCD1 antisense RNA 1 (head to head) . . . . . . . . . . . LMF1 1.14509473311795e-14 0.00566500534381505 0.994334994656173 lipase maturation factor 1 FUNCTION: Involved in the maturation of specific proteins in the endoplasmic reticulum. Required for maturation and transport of active lipoprotein lipase (LPL) through the secretory pathway. Each LMF1 molecule chaperones 50 or more molecules of LPL. {ECO:0000250, ECO:0000269|PubMed:24909692}.; DISEASE: Combined lipase deficiency (CLD) [MIM:246650]: Characterized by repeated episodes of pancreatitis, tuberous xanthomas and lipodystrophy and is caused by deficiency of both lipoprotein lipase (LPL) and hepatic triglyceride lipase (HTGL). {ECO:0000269|PubMed:17994020}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;ovary;colon;choroid;skin;retina;greater omentum;uterus;prostate;optic nerve;lung;endometrium;thyroid;placenta;liver;testis;spleen;germinal center;kidney;brain; amygdala;occipital lobe;superior cervical ganglion;testis - seminiferous tubule;liver;globus pallidus;appendix;parietal lobe; 0.10743 0.11836 1.230878375 93.26492097 1529.60384 7.26658 LMF1-AS1 . . . LMF1 antisense RNA 1 . . . . . . . . . . . LMF2 . . . lipase maturation factor 2 FUNCTION: Involved in the maturation of specific proteins in the endoplasmic reticulum. May be required for maturation and transport of active lipoprotein lipase (LPL) through the secretory pathway (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;islets of Langerhans;muscle;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; trigeminal ganglion;skeletal muscle; 0.14313 . -1.293511806 5.001179523 2091.17234 8.42309 LMLN 7.35628703193249e-06 0.999023801972595 0.000968841740372993 leishmanolysin like peptidase FUNCTION: Metalloprotease essential for the coordination of mitotic progression, and also plays a role in cell migration. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in all cell lines analyzed. {ECO:0000269|PubMed:19706689}.; unclassifiable (Anatomical System);medulla oblongata;lung;frontal lobe;placenta;trabecular meshwork;testis;cervix;brain;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.15253 0.45396 -0.488577883 22.64685067 1925.41511 8.07737 LMLN-AS1 . . . LMLN antisense RNA 1 . . . . . . . . . . . LMNA 0.993449023376761 0.00655076650730545 2.10115933918212e-07 lamin A/C FUNCTION: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone.; DISEASE: Emery-Dreifuss muscular dystrophy 2, autosomal dominant (EDMD2) [MIM:181350]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:10080180, ECO:0000269|PubMed:10739764, ECO:0000269|PubMed:10908904, ECO:0000269|PubMed:10939567, ECO:0000269|PubMed:11503164, ECO:0000269|PubMed:12032588, ECO:0000269|PubMed:12467752, ECO:0000269|PubMed:12649505, ECO:0000269|PubMed:14684700, ECO:0000269|PubMed:14985400, ECO:0000269|PubMed:15744034, ECO:0000269|PubMed:20848652}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Emery-Dreifuss muscular dystrophy 3, autosomal recessive (EDMD3) [MIM:616516]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:22431096}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1A (CMD1A) [MIM:115200]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:10580070, ECO:0000269|PubMed:11561226, ECO:0000269|PubMed:11897440, ECO:0000269|PubMed:12486434, ECO:0000269|PubMed:12628721, ECO:0000269|PubMed:12920062, ECO:0000269|PubMed:14684700, ECO:0000269|PubMed:15140538, ECO:0000269|PubMed:15219508, ECO:0000269|PubMed:16061563, ECO:0000269|PubMed:20160190, ECO:0000269|PubMed:21846512}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Lipodystrophy, familial partial, 2 (FPLD2) [MIM:151660]: A disorder characterized by the loss of subcutaneous adipose tissue in the lower parts of the body (limbs, buttocks, trunk). It is accompanied by an accumulation of adipose tissue in the face and neck causing a double chin, fat neck, or cushingoid appearance. Adipose tissue may also accumulate in the axillae, back, labia majora, and intraabdominal region. Affected patients are insulin-resistant and may develop glucose intolerance and diabetes mellitus after age 20 years, hypertriglyceridemia, and low levels of high density lipoprotein cholesterol. {ECO:0000269|PubMed:10587585, ECO:0000269|PubMed:10655060, ECO:0000269|PubMed:10739751, ECO:0000269|PubMed:12015247, ECO:0000269|PubMed:12196663, ECO:0000269|PubMed:12629077, ECO:0000269|PubMed:17250669, ECO:0000269|PubMed:24485160}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Limb-girdle muscular dystrophy 1B (LGMD1B) [MIM:159001]: An autosomal dominant degenerative myopathy with age-related atrioventricular cardiac conduction disturbances, dilated cardiomyopathy, and the absence of early contractures. Characterized by slowly progressive skeletal muscle weakness of the hip and shoulder girdles. Muscle biopsy shows mild dystrophic changes. {ECO:0000269|PubMed:10814726, ECO:0000269|PubMed:11525883, ECO:0000269|PubMed:12032588, ECO:0000269|PubMed:12673789, ECO:0000269|PubMed:15744034, ECO:0000269|PubMed:17136397}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease 2B1 (CMT2B1) [MIM:605588]: A recessive axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. {ECO:0000269|PubMed:11799477}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hutchinson-Gilford progeria syndrome (HGPS) [MIM:176670]: Rare genetic disorder characterized by features reminiscent of marked premature aging. {ECO:0000269|PubMed:12714972, ECO:0000269|PubMed:12768443, ECO:0000269|PubMed:12927431, ECO:0000269|PubMed:15060110, ECO:0000269|PubMed:15286156, ECO:0000269|PubMed:15622532, ECO:0000269|PubMed:21791255, ECO:0000269|PubMed:22355414, ECO:0000269|PubMed:23666920}. Note=The disease is caused by mutations affecting the gene represented in this entry. HGPS is caused by the toxic accumulation of a truncated form of lamin-A/C. This mutant protein, called progerin (isoform 6), acts to deregulate mitosis and DNA damage signaling, leading to premature cell death and senescence. The mutant form is mainly generated by a silent or missense mutation at codon 608 of prelamin A that causes activation of a cryptic splice donor site, resulting in production of isoform 6 with a deletion of 50 amino acids near the C terminus. Progerin lacks the conserved ZMPSTE24/FACE1 cleavage site and therefore remains permanently farnesylated. Thus, although it can enter the nucleus and associate with the nuclear envelope, it cannot incorporate normally into the nuclear lamina (PubMed:12714972). {ECO:0000269|PubMed:12714972}.; DISEASE: Cardiomyopathy, dilated, with hypergonadotropic hypogonadism (CMDHH) [MIM:212112]: A disorder characterized by the association of genital anomalies, hypergonadotropic hypogonadism and dilated cardiomyopathy. Patients can present other variable clinical manifestations including mental retardation, skeletal anomalies, scleroderma-like skin, graying and thinning of hair, osteoporosis. Dilated cardiomyopathy is characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. {ECO:0000269|PubMed:12927431, ECO:0000269|PubMed:17150192, ECO:0000269|PubMed:19283854}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mandibuloacral dysplasia with type A lipodystrophy (MADA) [MIM:248370]: A disorder characterized by mandibular and clavicular hypoplasia, acroosteolysis, delayed closure of the cranial suture, progeroid appearance, partial alopecia, soft tissue calcinosis, joint contractures, and partial lipodystrophy with loss of subcutaneous fat from the extremities. Adipose tissue in the face, neck and trunk is normal or increased. {ECO:0000269|PubMed:12075506, ECO:0000269|PubMed:15998779, ECO:0000269|PubMed:16278265}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Lethal tight skin contracture syndrome (LTSCS) [MIM:275210]: Rare disorder mainly characterized by intrauterine growth retardation, tight and rigid skin with erosions, prominent superficial vasculature and epidermal hyperkeratosis, facial features (small mouth, small pinched nose and micrognathia), sparse/absent eyelashes and eyebrows, mineralization defects of the skull, thin dysplastic clavicles, pulmonary hypoplasia, multiple joint contractures and an early neonatal lethal course. Liveborn children usually die within the first week of life. The overall prevalence of consanguineous cases suggested an autosomal recessive inheritance. {ECO:0000269|PubMed:15317753}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Heart-hand syndrome Slovenian type (HHS-Slovenian) [MIM:610140]: Heart-hand syndrome (HHS) is a clinically and genetically heterogeneous disorder characterized by the co- occurrence of a congenital cardiac disease and limb malformations. {ECO:0000269|PubMed:18611980}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Muscular dystrophy congenital LMNA-related (MDCL) [MIM:613205]: A form of congenital muscular dystrophy. Patients present at birth, or within the first few months of life, with hypotonia, muscle weakness and often with joint contractures. {ECO:0000269|PubMed:18551513}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in LMNA may cause a late-onset cardiocutaneous progeria syndrome characterized by cutaneous manifestations of aging appearing in the third decade of life, cardiac valve calcification and dysfunction, prominent atherosclerosis, and cardiomyopathy, leading to death on average in the fourth decade. {ECO:0000269|PubMed:23666920}.; TISSUE SPECIFICITY: In the arteries, prelamin-A/C accumulation is not observed in young healthy vessels but is prevalent in medial vascular smooth muscle cells (VSMCs) from aged individuals and in atherosclerotic lesions, where it often colocalizes with senescent and degenerate VSMCs. Prelamin-A/C expression increases with age and disease. In normal aging, the accumulation of prelamin-A/C is caused in part by the down-regulation of ZMPSTE24/FACE1 in response to oxidative stress. {ECO:0000269|PubMed:20458013}.; medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;urinary;lens;bile duct;breast;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;heart;tongue;placenta;ciliary ganglion;trigeminal ganglion; 0.55819 0.98592 -0.911109353 9.961075725 32.23482 1.00909 LMNB1 0.952857388391862 0.0471370877619899 5.52384614855893e-06 lamin B1 FUNCTION: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.; DISEASE: Leukodystrophy, demyelinating, autosomal dominant, adult- onset (ADLD) [MIM:169500]: A slowly progressive and fatal demyelinating leukodystrophy, presenting in the fourth or fifth decade of life. Clinically characterized by early autonomic abnormalities, pyramidal and cerebellar dysfunction, and symmetric demyelination of the CNS. It differs from multiple sclerosis and other demyelinating disorders in that neuropathology shows preservation of oligodendroglia in the presence of subtotal demyelination and lack of astrogliosis. {ECO:0000269|PubMed:16951681}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; tumor;ciliary ganglion;atrioventricular node; 0.93170 0.52130 -0.404032746 26.53338051 123.78072 2.42106 LMNB2 0.995599596829826 0.004400323704224 7.94659503185613e-08 lamin B2 FUNCTION: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.; DISEASE: Partial acquired lipodystrophy (APLD) [MIM:608709]: A rare childhood disease characterized by loss of subcutaneous fat from the face and trunk. Fat deposition on the pelvic girdle and lower limbs is normal or excessive. Most frequently, onset between 5 and 15 years of age. Most affected subjects are females and some show no other abnormality, but many develop glomerulonephritis, diabetes mellitus, hyperlipidemia, and complement deficiency. Mental retardation in some cases. APLD is a sporadic disorder of unknown etiology. {ECO:0000269|PubMed:16826530, ECO:0000269|PubMed:22768673}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epilepsy, progressive myoclonic 9 (EPM9) [MIM:616540]: An autosomal recessive form of progressive myoclonic epilepsy, a rare disease initially responsive to antiepileptic drugs which over time becomes refractory and can be associated with cognitive decline. EPM9 features include myoclonus, tonic-clonic seizures, ataxia, and psychomotor development. {ECO:0000269|PubMed:25954030}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;head and neck;kidney;stomach;thymus;cerebellum; tumor;cerebellum; 0.83760 0.24333 -1.129772626 6.505071951 299.25483 3.68858 LMNTD1 . . . lamin tail domain containing 1 . . . . . 0.14710 0.07473 1.642526957 96.14885586 . . LMNTD2 . . . lamin tail domain containing 2 . . . . . 0.06703 . . . . . LMO1 0.477078993256257 0.499737673648956 0.0231833330947862 LIM domain only 1 FUNCTION: May be involved in gene regulation within neural lineage cells potentially by direct DNA binding or by binding to other transcription factors. {ECO:0000269|PubMed:1703797}.; . TISSUE SPECIFICITY: Expressed mainly in the central nervous. Low level of expression in other tissues including thymus. {ECO:0000269|PubMed:2052354}.; unclassifiable (Anatomical System);breast;lung;islets of Langerhans;visual apparatus;muscle;choroid;brain; superior cervical ganglion;trigeminal ganglion; 0.78382 0.15588 -0.163345027 41.24793583 9.59633 0.35329 LMO2 0.753952192768922 0.236452305182285 0.00959550204879265 LIM domain only 2 FUNCTION: Acts with TAL1/SCL to regulate red blood cell development. Also acts with LDB1 to maintain erythroid precursors in an immature state.; DISEASE: Note=A chromosomal aberration involving LMO2 may be a cause of a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(11,14)(p13;q11) with TCRD.; . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;synovium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pineal body;adrenal cortex;blood;lung;adrenal gland;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach;aorta; superior cervical ganglion;uterus corpus;parietal lobe;skeletal muscle; 0.91591 0.38765 . . 26.24832 0.85065 LMO3 0.43420908358226 0.53452455144875 0.0312663649689897 LIM domain only 3 . . . colon;choroid;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;testis;bladder;brain;amygdala;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;muscle;skeletal muscle;breast;lung;placenta;hippocampus;visual apparatus;liver;spleen;kidney;peripheral nerve; whole brain;amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.63036 0.11809 0.035072054 56.2514744 0.85073 0.01713 LMO4 0.816026560670216 0.179590672622213 0.00438276670757016 LIM domain only 4 FUNCTION: Probable transcriptional factor. {ECO:0000250}.; . . . . 0.44177 0.12288 -0.251530012 35.42108988 7.4204 0.27546 LMO7 0.0416242513975852 0.958375730901258 1.7701156507577e-08 LIM domain 7 . . TISSUE SPECIFICITY: Widely expressed. Isoform 2 and isoform 4 are predominantly expressed in brain. {ECO:0000269|PubMed:11935316, ECO:0000269|PubMed:9826547}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;brain;gall bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;tongue;islets of Langerhans;urinary;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; globus pallidus;trigeminal ganglion;skeletal muscle; 0.07767 0.11900 0.470181588 78.8039632 4280.99271 13.01430 LMO7-AS1 . . . LMO7 antisense RNA 1 . . . . . . . . . . . LMO7DN . . . LMO7 downstream neighbor . . . . . . . . . . . LMO7DN-IT1 . . . LMO7DN intronic transcript 1 . . . . . . . . . . . LMOD1 0.790872726605776 0.207803781455149 0.00132349193907455 leiomodin 1 . . TISSUE SPECIFICITY: Smooth muscle (heart, skeletal muscle, colon and small intestine), a subset of striated muscle fibers, and at low level in thyroid. {ECO:0000269|PubMed:10520227, ECO:0000269|PubMed:11350761}.; . . 0.28864 0.23076 0.176444282 66.07100731 406.46794 4.22739 LMOD2 0.00499630318196295 0.885859469375506 0.109144227442532 leiomodin 2 FUNCTION: Increases the rate of actin polymerization (PubMed:25250574). {ECO:0000269|PubMed:25250574}.; . TISSUE SPECIFICITY: Specifically expressed in heart and skeletal muscles, with higher levels in heart (at protein level). Not expressed in other tissues. {ECO:0000269|PubMed:11318603, ECO:0000269|PubMed:25250574}.; unclassifiable (Anatomical System);myocardium;lung;heart;thyroid;liver;testis;skeletal muscle;peripheral nerve; superior cervical ganglion;skeletal muscle; . . 0.15257911 64.60839821 84.53262 1.95772 LMOD3 0.00805841552794795 0.930076136612243 0.0618654478598088 leiomodin 3 FUNCTION: Essential for the organization of sarcomeric actin thin filaments in skeletal muscle (PubMed:25250574). Increases the rate of actin polymerization (PubMed:25250574). {ECO:0000269|PubMed:25250574}.; DISEASE: Nemaline myopathy 10 (NEM10) [MIM:616165]: An autosomal recessive severe form of nemaline myopathy. Nemaline myopathies are muscular disorders characterized by muscle weakness of varying severity and onset, and abnormal thread-like or rod-shaped structures in muscle fibers on histologic examination. NEM10 is characterized by early-onset generalized muscle weakness and hypotonia with respiratory insufficiency and feeding difficulties. Additional features include arthrogryposis or congenital contractures, ophthalmoplegia, a history of prematurity, reduced fetal movements, and polyhydramnios. Most patients die of respiratory failure in early infancy. {ECO:0000269|PubMed:25250574}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in cardiac and at higher levels in skeletal muscles (at protein level). {ECO:0000269|PubMed:25250574}.; . . 0.04638 . 2.289361599 98.30738382 849.41203 5.69679 LMTK2 0.994402282503334 0.00559771631140626 1.18525954499385e-09 lemur tyrosine kinase 2 FUNCTION: Phosphorylates PPP1C, phosphorylase b and CFTR.; . TISSUE SPECIFICITY: Mainly expressed in skeletal muscle, and weakly in brain and pancreas. {ECO:0000269|PubMed:12393858}.; unclassifiable (Anatomical System);amygdala;ovary;islets of Langerhans;colon;parathyroid;blood;skeletal muscle;bone marrow;breast;pancreas;prostate;lung;frontal lobe;thyroid;placenta;pituitary gland;testis;germinal center;kidney;brain;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.32144 0.11774 -2.418488491 1.049775891 3315.40506 11.00713 LMTK3 . . . lemur tyrosine kinase 3 FUNCTION: Protein kinase which phosphorylates ESR1 (in vitro) and protects it against proteasomal degradation. May also regulate ESR1 levels indirectly via a PKC-AKT-FOXO3 pathway where it decreases the activity of PKC and the phosphorylation of AKT, thereby increasing binding of transcriptional activator FOXO3 to the ESR1 promoter and increasing ESR1 transcription (PubMed:21602804). Involved in endocytic trafficking of N-methyl- D-aspartate receptors (NMDAR) in neurons (By similarity). {ECO:0000250|UniProtKB:Q5XJV6, ECO:0000269|PubMed:21602804}.; . . unclassifiable (Anatomical System);optic nerve;frontal lobe;hippocampus;kidney;brain;retina; dorsal root ganglion;medulla oblongata;superior cervical ganglion;atrioventricular node;skeletal muscle;skin;bone marrow;subthalamic nucleus;fetal brain;liver;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.16037 . . . 180.94945 2.92455 LMX1A 0.901260324312874 0.0987034694209549 3.62062661712827e-05 LIM homeobox transcription factor 1 alpha FUNCTION: Acts as a transcriptional activator by binding to an A/T-rich sequence, the FLAT element, in the insulin gene promoter. Required for development of the roof plate and, in turn, for specification of dorsal cell fates in the CNS and developing vertebrae (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in many tissues. Not found in heart, liver, spleen and testis. Relatively highly expressed in fetal brain. Isoform LMX1A-4B is expressed in testis. {ECO:0000269|PubMed:12062816}.; optic nerve;lung;macula lutea;testis;fovea centralis;choroid;lens;retina; testis - interstitial;superior cervical ganglion; 0.37004 0.23021 -0.736552314 13.93606983 25.42005 0.82964 LMX1B 0.82273227003236 0.177096321646213 0.000171408321426952 LIM homeobox transcription factor 1 beta FUNCTION: Essential for the specification of dorsal limb fate at both the zeugopodal and autopodal levels.; . TISSUE SPECIFICITY: Expressed in most tissues. Highest levels in testis, thyroid, duodenum, skeletal muscle, and pancreatic islets.; unclassifiable (Anatomical System); superior cervical ganglion;testis - seminiferous tubule;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.35834 0.35026 -0.846787714 11.05803255 23.27331 0.77647 LNP1 0.00188517623884581 0.725834235527062 0.272280588234092 leukemia NUP98 fusion partner 1 . DISEASE: Note=A chromosomal aberration involving LNP1 is found in a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(3;11)(q12.2;p15.4) with NUP98. {ECO:0000269|PubMed:16467868}.; . . . 0.16885 0.10038 0.03689118 56.64071715 27.53827 0.88727 LNPEP 0.998308425894494 0.00169157404161828 6.38881202079317e-11 leucyl/cystinyl aminopeptidase FUNCTION: Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain. {ECO:0000269|PubMed:11389728, ECO:0000269|PubMed:11707427, ECO:0000269|PubMed:1731608}.; . TISSUE SPECIFICITY: Highly expressed in placenta, heart, kidney and small intestine. Detected at lower levels in neuronal cells in the brain, in skeletal muscle, spleen, liver, testes and colon. {ECO:0000269|PubMed:11389728, ECO:0000269|PubMed:8550619, ECO:0000269|PubMed:9177475}.; unclassifiable (Anatomical System);amygdala;ovary;heart;parathyroid;blood;skin;bone marrow;breast;lung;larynx;nasopharynx;placenta;liver;testis;cervix;head and neck;spleen;germinal center;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;placenta;ciliary ganglion; 0.07652 0.30451 0.181903047 66.2361406 2452.71206 9.21552 LNX1 0.0072436266198218 0.992057433845294 0.000698939534883735 ligand of numb-protein X 1, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NUMB. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of isoform p66 and isoform p72 of NUMB, but not that of isoform p71 or isoform p65 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in heart, placenta, kidney, pancreas and brain. {ECO:0000269|PubMed:11521506}.; medulla oblongata;ovary;foreskin;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; . 0.31424 0.15781 -1.194104514 5.850436424 109.44427 2.27278 LNX1-AS1 . . . LNX1 antisense RNA 1 . . . . . . . . . . . LNX1-AS2 . . . LNX1 antisense RNA 2 . . . . . . . . . . . LNX2 0.215281596114596 0.784644428888082 7.39749973219774e-05 ligand of numb-protein X 2 . . . unclassifiable (Anatomical System);cartilage;ovary;lacrimal gland;sympathetic chain;parathyroid;blood;breast;prostate;lung;endometrium;nasopharynx;thyroid;placenta;liver;testis;spleen;cervix;kidney;brain;mammary gland;stomach; dorsal root ganglion;ciliary ganglion;atrioventricular node; 0.19871 0.10229 -0.110153916 45.48832272 91.9101 2.06248 LOH1CR1 . . . loss of heterozygosity, 1, chromosomal region 1 . . . . . . . . . . . LOH12CR2 . . . loss of heterozygosity, 12, chromosomal region 2 (non-protein coding) . . . . . 0.08673 . . . 306.16498 3.72508 LOH19CR1 . . . loss of heterozygosity, 19, chromosomal region 1 . . . . . . . . . . . LONP1 0.999697932788122 0.000302067188440052 2.34376219791737e-11 lon peptidase 1, mitochondrial FUNCTION: ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single- stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site- specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters. Endogenous substrates include mitochondrial steroidogenic acute regulatory (StAR) protein. {ECO:0000255|HAMAP- Rule:MF_03120, ECO:0000269|PubMed:12198491, ECO:0000269|PubMed:15870080, ECO:0000269|PubMed:17420247, ECO:0000269|PubMed:8248235}.; . TISSUE SPECIFICITY: Duodenum, heart, lung and liver, but not thymus.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;ciliary body;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;kidney;stomach;aorta;cerebellum; whole brain;prostate;heart;adrenal gland;adrenal cortex;liver;tumor; 0.25059 0.42498 -1.822830336 2.140835103 621.42676 5.02732 LONP2 2.90605573607261e-16 0.0328849594152365 0.967115040584763 lon peptidase 2, peroxisomal FUNCTION: ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import (By similarity). May indirectly regulate peroxisomal fatty acid beta-oxidation through degradation of the self-processed forms of TYSND1. {ECO:0000255|HAMAP- Rule:MF_03121, ECO:0000269|PubMed:22002062}.; . . ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;tongue;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;oral cavity;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;cerebellum;thymus; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.06539 0.12237 -0.468351206 23.42533616 83.65184 1.94588 LONRF1 0.919751764265427 0.0802439385864351 4.29714813757909e-06 LON peptidase N-terminal domain and ring finger 1 . . . . . 0.13178 0.10078 . . 173.36463 2.86788 LONRF2 0.851045048927734 0.148933283637956 2.16674343098912e-05 LON peptidase N-terminal domain and ring finger 2 . . . . . 0.06760 . -0.089927255 46.99221515 3352.93866 11.09481 LONRF2P1 . . . LON peptidase N-terminal domain and ring finger 2 pseudogene 1 . . . . . . . . . . . LONRF2P2 . . . LON peptidase N-terminal domain and ring finger 2 pseudogene 2 . . . . . . . . . . . LONRF3 0.15337758764681 0.845908010333127 0.000714402020062295 LON peptidase N-terminal domain and ring finger 3 . . . unclassifiable (Anatomical System);breast;lung;thyroid;liver;testis;colon;kidney; superior cervical ganglion;trigeminal ganglion; 0.51561 0.10062 -0.157884861 42.05590941 71.13497 1.75614 LOR 0.179479999341018 0.644903259496565 0.175616741162416 loricrin FUNCTION: Major keratinocyte cell envelope protein.; DISEASE: Vohwinkel syndrome with ichthyosis (VSI) [MIM:604117]: A variant form of Vohwinkel syndrome without hearing loss and associated with ichthyosiform dermatosis. Clinical features include palmoplantar keratoderma, pseudoainhum and ichthyosis. Compact hyperkeratosis with round retained nuclei and hypergranulosis is observed on skin biopsies. {ECO:0000269|PubMed:12072018, ECO:0000269|PubMed:12615358, ECO:0000269|PubMed:9326323}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.21306 . . . 2088.42676 8.41846 LOX 0.97935777427103 0.0206387152914771 3.51043749306924e-06 lysyl oxidase FUNCTION: Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. In addition to cross-linking of extracellular matrix proteins, may have a direct role in tumor suppression.; . TISSUE SPECIFICITY: Heart, placenta, skeletal muscle, kidney, lung and pancreas. {ECO:0000269|PubMed:7706256}.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;skin;skeletal muscle;breast;bile duct;uterus;whole body;lung;mesenchyma;bone;placenta;visual apparatus;liver;testis;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;smooth muscle;adipose tissue;heart;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.39100 0.98092 0.215080721 67.91696155 868.16804 5.73987 LOXHD1 . . . lipoxygenase homology domains 1 FUNCTION: Involved in hearing. Required for normal function of hair cells in the inner ear (By similarity). {ECO:0000250, ECO:0000269|PubMed:19732867}.; DISEASE: Deafness, autosomal recessive, 77 (DFNB77) [MIM:613079]: A form of non-syndromic deafness characterized by preserved low- frequency hearing, and a trend toward mild to moderate mid- frequency and high-frequency hearing loss during childhood and adolescence. Hearing loss progresses to become moderate to severe at mid and high frequencies during adulthood. {ECO:0000269|PubMed:19732867}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;testis;blood;stomach;bone marrow; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.17569 0.10035 1.183126933 92.82849729 5524.46007 15.34688 LOXL1 . . . lysyl oxidase like 1 FUNCTION: Active on elastin and collagen substrates. {ECO:0000250}.; DISEASE: Exfoliation syndrome (XFS) [MIM:177650]: A disorder characterized by accumulation of abnormal fibrillar deposits in the anterior segment of the eye. In addition to being a cause of glaucoma and glaucomatous optic neuropathy, exfoliation syndrome has also been associated with lens zonule weakness, cataract formation, and systemic vascular complications due to deposition of exfoliation material in extraocular tissues. {ECO:0000269|PubMed:18037624, ECO:0000269|PubMed:19343041}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Susceptibility to exfoliation syndrome is conferred by a risk haplotype that includes two LOXL1 coding non-synonymous SNPs (Arg141Leu and Gly153Asp) and one intronic SNP. Arg141Leu and Gly153Asp are sufficient to confer disease susceptibility in some populations.; TISSUE SPECIFICITY: Expressed in ocular tissues including the iris, ciliary body, lens and optic nerve. Not detected in the retina. {ECO:0000269|PubMed:18037624}.; medulla oblongata;ovary;colon;fovea centralis;skin;retina;bone marrow;uterus;prostate;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;urinary;muscle;blood;lens;bile duct;breast;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;aorta; prostate;adipose tissue;smooth muscle;heart;placenta;testis;fetal lung;skeletal muscle; 0.93123 0.29496 . . 6205.01312 16.46886 LOXL1-AS1 . . . LOXL1 antisense RNA 1 . . . . . . . . . . . LOXL2 2.99731375478488e-07 0.981412018434168 0.0185876818344562 lysyl oxidase like 2 FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). When secreted in extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. When nuclear, acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E- cadherin, probably by mediating deamination of histone H3. Also involved in E-cadherin repression following hypoxia, a hallmark of epithelial to mesenchymal transition believed to amplify tumor aggressiveness, suggesting that it may play a role in tumor progression. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation. {ECO:0000269|PubMed:16096638, ECO:0000269|PubMed:20026874, ECO:0000269|PubMed:21233336, ECO:0000269|PubMed:21732535, ECO:0000269|PubMed:21835952, ECO:0000269|PubMed:22483618}.; . TISSUE SPECIFICITY: Expressed in many tissues. Highest expression in reproductive tissues, placenta, uterus and prostate. Up- regulated in a number of cancers cells and tissues.; . . 0.11697 0.09990 -1.587406381 3.113941967 316.28087 3.77670 LOXL3 5.65366567269509e-08 0.991443691496813 0.00855625196653065 lysyl oxidase like 3 FUNCTION: Both isoforms function as amine oxidases toward elastin and different types of collagens. Isoform 1 shows the highest activity toward collagen type VIII, while Isoform 2 presents the highest activity toward collagen type IV. {ECO:0000269|PubMed:17018530}.; . TISSUE SPECIFICITY: Isoform 1 ia predominantly detected in the heart, placenta, lung, and small intestine, while isoform 2 is more highly detected in the kidney, pancreas, spleen, and thymus, and is absent in lung. {ECO:0000269|PubMed:17018530}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;gum;bone;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; . 0.36983 0.16108 0.003714825 54.06935598 1582.47535 7.35746 LOXL4 2.14099281310303e-09 0.655942985209682 0.344057012649325 lysyl oxidase like 4 FUNCTION: May modulate the formation of a collagenous extracellular matrix.; . TISSUE SPECIFICITY: Expressed in many tissues, the highest levels among the tissues studied being in the skeletal muscle, testis and pancreas. Expressed in cartilage.; colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;bile duct;breast;pancreas;lung;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;peripheral nerve; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.28127 0.16497 -0.367438677 28.29087049 4349.01772 13.14516 LPA 2.4422277924849e-32 0.00753098838146121 0.992469011618539 lipoprotein, Lp(a) FUNCTION: Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330. {ECO:0000269|PubMed:2531657}.; . . lung;frontal lobe;adrenal cortex;liver;testis;spleen;kidney; superior cervical ganglion;liver;trigeminal ganglion; 0.07571 . . . 3944.17186 12.41719 LPAL1 . . . lipoprotein, Lp(a)-like 1 . . . . . . . . . . . LPAL2 . . . lipoprotein, Lp(a)-like 2, pseudogene . . TISSUE SPECIFICITY: Expressed in liver but not in other tissues tested. {ECO:0000269|PubMed:7749817}.; unclassifiable (Anatomical System); . 0.01465 . . . . . LPAR1 0.00141898105564211 0.666257490174915 0.332323528769443 lysophosphatidic acid receptor 1 FUNCTION: Receptor for lysophosphatidic acid (LPA) (PubMed:9070858, PubMed:19306925, PubMed:25025571, PubMed:26091040). Plays a role in the reorganization of the actin cytoskeleton, cell migration, differentiation and proliferation, and thereby contributes to the responses to tissue damage and infectious agents. Activates downstream signaling cascades via the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins. Signaling inhibits adenylyl cyclase activity and decreases cellular cAMP levels (PubMed:26091040). Signaling triggers an increase of cytoplasmic Ca(2+) levels (PubMed:19656035, PubMed:19733258, PubMed:26091040). Activates RALA; this leads to the activation of phospholipase C (PLC) and the formation of inositol 1,4,5-trisphosphate (PubMed:19306925). Signaling mediates activation of down-stream MAP kinases (By similarity). Contributes to the regulation of cell shape. Promotes Rho-dependent reorganization of the actin cytoskeleton in neuronal cells and neurite retraction (PubMed:26091040). Promotes the activation of Rho and the formation of actin stress fibers (PubMed:26091040). Promotes formation of lamellipodia at the leading edge of migrating cells via activation of RAC1 (By similarity). Through its function as lysophosphatidic acid receptor, plays a role in chemotaxis and cell migration, including responses to injury and wounding (PubMed:18066075, PubMed:19656035, PubMed:19733258). Plays a role in triggering inflammation in response to bacterial lipopolysaccharide (LPS) via its interaction with CD14. Promotes cell proliferation in response to lysophosphatidic acid. Required for normal skeleton development. May play a role in osteoblast differentiation. Required for normal brain development. Required for normal proliferation, survival and maturation of newly formed neurons in the adult dentate gyrus. Plays a role in pain perception and in the initiation of neuropathic pain (By similarity). {ECO:0000250|UniProtKB:P61793, ECO:0000269|PubMed:18066075, ECO:0000269|PubMed:19306925, ECO:0000269|PubMed:19656035, ECO:0000269|PubMed:19733258, ECO:0000269|PubMed:25025571, ECO:0000269|PubMed:26091040, ECO:0000269|PubMed:9070858, ECO:0000305|PubMed:11093753, ECO:0000305|PubMed:9069262}.; . TISSUE SPECIFICITY: Expressed in many adult organs, including brain, heart, colon, small intestine, placenta, prostate, ovary, pancreas, testes, spleen, skeletal muscle, and kidney. Little or no expression in liver, lung, thymus, or peripheral blood leukocytes (PubMed:9070858). Detected in lung fibroblasts from bronchoalveolar fluid from patients with idiopathic pulmonary fibrosis (PubMed:18066075). Detected in bone marrow-derived mesenchymal stem cells (PubMed:19733258). {ECO:0000269|PubMed:18066075, ECO:0000269|PubMed:19733258, ECO:0000269|PubMed:9070858}.; ovary;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;nervous;tongue;hypothalamus;urinary;skeletal muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;head and neck;mammary gland;stomach;aorta; dorsal root ganglion;thalamus;superior cervical ganglion;occipital lobe;medulla oblongata;hypothalamus;spinal cord;pons;atrioventricular node;caudate nucleus;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.57239 0.16622 -0.560178693 19.30879925 98.11251 2.14175 LPAR2 0.337269896843433 0.648186647697445 0.0145434554591211 lysophosphatidic acid receptor 2 FUNCTION: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Seems to be coupled to the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins. Plays a key role in phospholipase C-beta (PLC-beta) signaling pathway. Stimulates phospholipase C (PLC) activity in a manner that is independent of RALA activation. {ECO:0000269|PubMed:15143197, ECO:0000269|PubMed:19306925}.; . TISSUE SPECIFICITY: Expressed most abundantly in testes and peripheral blood leukocytes with less expression in pancreas, spleen, thymus and prostate. Little or no expression in heart, brain, placenta, lung, liver, skeletal muscle, kidney, ovary, small intestine, or colon.; . . 0.12042 0.15841 -0.337894035 30.37272942 33.10152 1.02508 LPAR3 0.786363329238024 0.207096501946281 0.00654016881569571 lysophosphatidic acid receptor 3 FUNCTION: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. May play a role in the development of ovarian cancer. Seems to be coupled to the G(i)/G(o) and G(q) families of heteromeric G proteins.; . TISSUE SPECIFICITY: Most abundantly expressed in prostate, testes, pancreas, and heart, with moderate levels in lung and ovary. No detectable expression in brain, placenta, liver, skeletal muscle, kidney, spleen, thymus, small intestine, colon, or peripheral blood leukocytes.; . . 0.21877 0.11959 -0.181750739 40.15687662 217.583 3.18936 LPAR4 0.0430359788704934 0.662310622954143 0.294653398175364 lysophosphatidic acid receptor 4 FUNCTION: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Transduces a signal by increasing the intracellular calcium ions and by stimulating adenylyl cyclase activity. The rank order of potency for agonists of this receptor is 1-oleoyl- > 1-stearoyl- > 1-palmitoyl- > 1-myristoyl- > 1- alkyl- > 1-alkenyl-LPA. {ECO:0000269|PubMed:12724320}.; . TISSUE SPECIFICITY: High expression in ovary. Not detected in the brain regions thalamus, putamen, caudate, frontal cortex, pons, hypothalamus and hippocampus. {ECO:0000269|PubMed:12724320}.; . . 0.75157 0.11530 0.281220278 71.07808445 40.58767 1.19013 LPAR5 0.0296429210794608 0.806050158585441 0.164306920335098 lysophosphatidic acid receptor 5 FUNCTION: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities.; . TISSUE SPECIFICITY: Not expressed in frontal cortex, basal forebrain, caudate putamen, thalamus, or hippocampus.; unclassifiable (Anatomical System);prostate;lymph node;lung;nasopharynx;hippocampus;testis;colon;germinal center;tonsil;retina; . 0.09268 0.10502 . . 59.94358 1.57052 LPAR6 0.0304365240746065 0.809647524940576 0.159915950984817 lysophosphatidic acid receptor 6 FUNCTION: Binds to oleoyl-L-alpha-lysophosphatidic acid (LPA). Intracellular cAMP is involved in the receptor activation. Important for the maintenance of hair growth and texture. {ECO:0000269|PubMed:18297070}.; DISEASE: Woolly hair autosomal recessive 1 with or without hypotrichosis (ARWH1) [MIM:278150]: A hair shaft disorder characterized by fine and tightly curled hair. Compared to normal curly hair that is observed in some populations, woolly hair grows slowly and stops growing after a few inches. Under light microscopy, woolly hair shows some structural anomalies, including trichorrhexis nodosa and tapered ends. Some individuals exhibit features of hypotrichosis. {ECO:0000269|PubMed:18297072}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hypotrichosis 8 (HYPT8) [MIM:278150]: A condition characterized by the presence of less than the normal amount of hair and abnormal hair follicles and shafts, which are thin and atrophic. The disorder affects the trunk and extremities as well as the scalp, and the eyebrows and eyelashes may also be involved, whereas beard, pubic, and axillary hairs are largely spared. In addition, patients can develop hyperkeratotic follicular papules, erythema, and pruritus in affected areas. In some patients with congenital hypotrichosis, monilethrix-like hairs showing elliptical nodes have been observed. {ECO:0000269|PubMed:18297070}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed ubiquitously, including in skin and hair follicle cells. Detected in both Henle's and Huxley's layers of the inner root sheath of the hair follicle and in suprabasal layers of the epidermis (at protein level). Expressed at low levels in peripheral blood leukocytes. {ECO:0000269|PubMed:11004484, ECO:0000269|PubMed:18297070, ECO:0000269|PubMed:18297072}.; sympathetic chain;colon;skin;bone marrow;uterus;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.21341 0.10005 0.016664174 55.21939137 44.89561 1.28670 LPCAT1 0.813682374432471 0.186309557634493 8.0679330360198e-06 lysophosphatidylcholine acyltransferase 1 FUNCTION: Possesses both acyltransferase and acetyltransferase activities (PubMed:16864775, PubMed:21498505). Activity is calcium-independent (By similarity). Mediates the conversion of 1- acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC) (PubMed:21498505). Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively (PubMed:16704971). May synthesize phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal role in respiratory physiology (PubMed:16864775). Involved in the regulation of lipid droplet number and size (PubMed:25491198). {ECO:0000250|UniProtKB:Q3TFD2, ECO:0000269|PubMed:16864775, ECO:0000269|PubMed:21498505, ECO:0000269|PubMed:25491198}.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;blood;lens;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;cerebellum;thymus; fetal brain;white blood cells; 0.09412 0.16593 -0.839512508 11.40009436 1127.55279 6.40531 LPCAT2 1.12519142457894e-06 0.938986400706654 0.0610124741019216 lysophosphatidylcholine acyltransferase 2 FUNCTION: Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-dependent. Involved in platelet- activating factor (PAF) biosynthesis by catalyzing the conversion of the PAF precursor, 1-O-alkyl-sn-glycero-3-phosphocholine (lyso- PAF) into 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (PAF). Also converts lyso-PAF to 1-O-alkyl-2-acyl-sn-glycero-3- phosphocholine (PC), a major component of cell membranes and a PAF precursor. Under resting conditions, acyltransferase activity is preferred. Upon acute inflammatory stimulus, acetyltransferase activity is enhanced and PAF synthesis increases. Also catalyzes the conversion of 1-acyl-sn-glycero-3-phosphocholine to 1,2- diacyl-sn-glycero-3-phosphocholine. {ECO:0000269|PubMed:20363836, ECO:0000269|PubMed:21498505}.; . . unclassifiable (Anatomical System);ovary;hypothalamus;colon;blood;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;optic nerve;lung;endometrium;placenta;macula lutea;testis;kidney;pineal gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07139 0.09595 0.418953042 77.06416608 133.52498 2.51078 LPCAT2BP . . . lysophosphatidylcholine acyltransferase 2b, pseudogene . . . . . . . . . . . LPCAT3 0.980678848782637 0.0193205475561777 6.0366118503348e-07 lysophosphatidylcholine acyltransferase 3 FUNCTION: Acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3- phosphocholine or PC) (LPCAT activity). Catalyzes also the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero- 3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn- glycero-3-phospho-L-serine or PS) (LPSAT activity). Has also weak lysophosphatidylethanolamine acyltransferase activity (LPEAT activity). Favors polyunsaturated fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs. Seems to be the major enzyme contributing to LPCAT activity in the liver. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. {ECO:0000269|PubMed:18195019, ECO:0000269|PubMed:18772128}.; . TISSUE SPECIFICITY: Highly expressed in liver, pancreas and adipose tissue. Very low expression in skeletal muscle and heart. Detected in neutrophils. {ECO:0000269|PubMed:18195019, ECO:0000269|PubMed:18772128}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; adipose tissue; 0.29518 0.15273 0.106667882 61.73036093 2937.33413 10.28162 LPCAT4 0.996222992113105 0.00377699681316211 1.10737325644827e-08 lysophosphatidylcholine acyltransferase 4 FUNCTION: Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates; converts lysophosphatidylethanolamine to phosphatidylethanolamine, lysophosphatidylcholine to phosphatidycholine, 1-alkenyl-lysophatidylethanolamine to 1- alkenyl-phosphatidylethanolamine, lysophosphatidylglycerol and alkyl-lysophosphatidylcholine to phosphatidylglycerol and alkyl- phosphatidylcholine, respectively. In contrast, has no lysophosphatidylinositol, glycerol-3-phosphate, diacylglycerol or lysophosphatidic acid acyltransferase activity. Prefers long chain acyl-CoAs (C16, C18) as acyl donors. {ECO:0000269|PubMed:18458083}.; . TISSUE SPECIFICITY: Widely expressed with predominant level in brain. {ECO:0000269|PubMed:16243729, ECO:0000269|PubMed:18458083}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;pharynx;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach; whole brain;amygdala;medulla oblongata;superior cervical ganglion;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.16947 0.11660 -0.404032746 26.53338051 36.06955 1.08339 LPGAT1 0.967547481345112 0.0324417694380192 1.07492168692498e-05 lysophosphatidylglycerol acyltransferase 1 FUNCTION: Lysophosphatidylglycerol (LPG) specific acyltransferase that recognizes various acyl-CoAs and LPGs as substrates but demonstrates a clear preference for long chain saturated fatty acyl-CoAs and oleoyl-CoA as acyl donors. Prefers oleoyl-LPG over palmitoyl-LPG as an acyl receptor and oleoyl-CoA over lauroyl-CoA as an acyl donor. {ECO:0000269|PubMed:15485873}.; . TISSUE SPECIFICITY: Highly expressed in liver and placenta. Also expressed in peripheral blood, lung, kidney and brain. Detected at lower levels in colon. {ECO:0000269|PubMed:15485873}.; . . 0.22377 0.11452 -0.029247611 51.40363293 11.31678 0.40709 LPGAT1P1 . . . lysophosphatidylglycerol acyltransferase 1 pseudogene 1 . . . . . . . . . . . LPIN1 2.34821042560306e-05 0.999793161122344 0.000183356773400473 lipin 1 FUNCTION: Plays important roles in controlling the metabolism of fatty acids at differents levels. Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis in the reticulum endoplasmic membrane. Acts also as a nuclear transcriptional coactivator for PPARGC1A/PPARA to modulate lipid metabolism gene expression (By similarity). Is involved in adipocyte differentiation. May also be involved in mitochondrial fission by converting phosphatidic acid to diacylglycerol (By similarity). {ECO:0000250}.; DISEASE: Myoglobinuria, acute recurrent, autosomal recessive (ARARM) [MIM:268200]: Recurrent myoglobinuria is characterized by recurrent attacks of rhabdomyolysis (necrosis or disintegration of skeletal muscle) associated with muscle pain and weakness and followed by excretion of myoglobin in the urine. Renal failure may occasionally occur. {ECO:0000269|PubMed:18817903}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Specifically expressed in skeletal muscle. Also abundant in adipose tissue. Lower levels in some portions of the digestive tract. {ECO:0000269|PubMed:17158099, ECO:0000269|PubMed:22134922}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;head and neck;kidney;stomach; amygdala;dorsal root ganglion;testis - interstitial;superior cervical ganglion;olfactory bulb;adipose tissue;pons;atrioventricular node;skeletal muscle;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.10780 0.17394 -1.192291254 5.862231658 2775.76 9.94879 LPIN2 0.673512974845848 0.326486955577325 6.95768266347941e-08 lipin 2 FUNCTION: Plays important roles in controlling the metabolism of fatty acids at differents levels. Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis in the reticulum endoplasmic membrane. Acts also as a nuclear transcriptional coactivator for PPARGC1A to modulate lipid metabolism (By similarity). {ECO:0000250}.; DISEASE: Majeed syndrome (MAJEEDS) [MIM:609628]: An autosomal recessive syndrome characterized by chronic recurrent multifocal osteomyelitis that is of early onset with a lifelong course, congenital dyserythropoietic anemia that presents as hypochromic, microcytic anemia during the first year of life and ranges from mild to transfusion-dependent, and transient inflammatory dermatosis, often manifesting as Sweet syndrome (neutrophilic skin infiltration). {ECO:0000269|PubMed:15994876}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in liver, lung, kidney, placenta, spleen, thymus, lymph node, prostate, testes, small intestine, and colon. {ECO:0000269|PubMed:15994876, ECO:0000269|PubMed:17158099}.; smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;pineal gland;bladder;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;aorta; superior cervical ganglion;fetal liver; 0.33992 0.15484 -0.793601146 12.57372022 235.5578 3.31663 LPIN3 4.43532236084843e-11 0.774166357703905 0.225833642251741 lipin 3 FUNCTION: Regulates fatty acid metabolism. Magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Significant expression in intestine and other regions of the gastrointestinal tract. {ECO:0000269|PubMed:17158099}.; . . 0.14721 0.10631 0.563976585 81.71738618 3872.39743 12.26866 LPL 3.33727737763241e-06 0.792834693752327 0.207161968970295 lipoprotein lipase FUNCTION: The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium (By similarity). {ECO:0000250}.; DISEASE: Lipoprotein lipase deficiency (LPL deficiency) [MIM:238600]: Recessive disorder usually manifesting in childhood. On a normal diet, patients often present with abdominal pain, hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and massive hypertriglyceridemia, sometimes complicated with acute pancreatitis. {ECO:0000269|PubMed:10660334, ECO:0000269|PubMed:10787434, ECO:0000269|PubMed:11068186, ECO:0000269|PubMed:11099402, ECO:0000269|PubMed:11134145, ECO:0000269|PubMed:11441134, ECO:0000269|PubMed:12204001, ECO:0000269|PubMed:12641539, ECO:0000269|PubMed:12966036, ECO:0000269|PubMed:1400331, ECO:0000269|PubMed:1479292, ECO:0000269|PubMed:14984478, ECO:0000269|PubMed:15185149, ECO:0000269|PubMed:1521525, ECO:0000269|PubMed:15256764, ECO:0000269|PubMed:15877202, ECO:0000269|PubMed:1598907, ECO:0000269|PubMed:1619366, ECO:0000269|PubMed:1639392, ECO:0000269|PubMed:1674945, ECO:0000269|PubMed:1702428, ECO:0000269|PubMed:1730727, ECO:0000269|PubMed:1752947, ECO:0000269|PubMed:1907278, ECO:0000269|PubMed:1969408, ECO:0000269|PubMed:1975597, ECO:0000269|PubMed:2010533, ECO:0000269|PubMed:2038366, ECO:0000269|PubMed:2110364, ECO:0000269|PubMed:2121025, ECO:0000269|PubMed:7647785, ECO:0000269|PubMed:7806969, ECO:0000269|PubMed:7906986, ECO:0000269|PubMed:7912254, ECO:0000269|PubMed:7999071, ECO:0000269|PubMed:8077845, ECO:0000269|PubMed:8096693, ECO:0000269|PubMed:8135797, ECO:0000269|PubMed:8288243, ECO:0000269|PubMed:8301230, ECO:0000269|PubMed:8325986, ECO:0000269|PubMed:8486765, ECO:0000269|PubMed:8728326, ECO:0000269|PubMed:8778602, ECO:0000269|PubMed:8858123, ECO:0000269|PubMed:8872057, ECO:0000269|PubMed:8956048, ECO:0000269|PubMed:8956052, ECO:0000269|PubMed:9279761, ECO:0000269|PubMed:9298816, ECO:0000269|PubMed:9498099, ECO:0000269|PubMed:9662394, ECO:0000269|PubMed:9714430, ECO:0000269|PubMed:9719626}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;medulla oblongata;olfactory bulb;adipose tissue;caudate nucleus;pons;atrioventricular node;skeletal muscle;fetal brain;placenta;ciliary ganglion;trigeminal ganglion; 0.36114 . 0.532823122 80.96249115 828.43667 5.64271 LPO 2.90912911352746e-11 0.264081681819632 0.735918318151277 lactoperoxidase FUNCTION: Antimicrobial agent which utilizes hydrogen peroxide and thiocyanate (SCN) to generate the antimicrobial substance hypothiocyanous acid (HOSCN) (By similarity). May contribute to airway host defense against infection. {ECO:0000250|UniProtKB:A5JUY8, ECO:0000269|PubMed:12626341}.; . TISSUE SPECIFICITY: Mammary gland; milk and salivary gland. Found in bronchial submucosal glands. {ECO:0000269|PubMed:12626341}.; cartilage;lacrimal gland;blood;skeletal muscle;bone marrow; superior cervical ganglion;subthalamic nucleus;trachea;salivary gland;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.15837 0.32199 -1.240018202 5.461193678 1144.41107 6.45117 LPP 0.582399908119384 0.417507007441914 9.30844387027762e-05 LIM domain containing preferred translocation partner in lipoma FUNCTION: May play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation of gene transcription. May be involved in signal transduction from cell adhesion sites to the nucleus allowing successful integration of signals arising from soluble factors and cell-cell adhesion sites. Also suggested to serve as a scaffold protein upon which distinct protein complexes are assembled in the cytoplasm and in the nucleus. {ECO:0000269|PubMed:10637295, ECO:0000269|Ref.2}.; DISEASE: Note=A chromosomal aberration involving LPP is associated with pulmonary chondroid hamartomas. Translocation t(3;12)(q27- q28;q14-q15) with HMGA2 is detected in pulmonary chondroid hamartomas.; DISEASE: Note=A chromosomal aberration involving LPP is associated with parosteal lipomas. Translocation t(3;12)(q28;q14) with HMGA2 is also shown in one parosteal lipoma.; DISEASE: Note=A chromosomal aberration involving LPP is associated with acute monoblastic leukemia. Translocation t(3;11)(q28;q23) with KMT2A/MLL1 is associated with acute monoblastic leukemia.; TISSUE SPECIFICITY: Expressed in a wide variety of tissues but no or very low expression in brain and peripheral leukocytes. {ECO:0000269|PubMed:10637295, ECO:0000269|PubMed:8812423}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;salivary gland;colon;skeletal muscle;uterus;breast;pancreas;prostate;lung;bone;testis;germinal center;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;atrioventricular node;skin;skeletal muscle;uterus;uterus corpus;prostate;testis - seminiferous tubule;appendix;testis;ciliary ganglion;trigeminal ganglion; 0.24469 0.15914 1.050838371 91.36588818 2291.9413 8.86320 LPP-AS1 . . . LPP antisense RNA 1 . . . . . . . . . . . LPP-AS2 . . . LPP antisense RNA 2 . . . . . . . . . . . LPXN 0.0172004433087515 0.960285294074859 0.0225142626163891 leupaxin FUNCTION: Transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF). Contributes to the regulation of cell adhesion, spreading and cell migration and acts as a negative regulator in integrin-mediated cell adhesion events. Suppresses the integrin-induced tyrosine phosphorylation of paxillin (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling. {ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:18451096, ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:20543562}.; . TISSUE SPECIFICITY: Macrophages, monocytes and osteoclasts (at protein level). Strongly expressed in cells and tissues of hematopoietic origin. Highest expression in lymphoid tissues such as spleen, lymph node, thymus and appendix and in the vascular smooth muscle. Lower levels in bone marrow and fetal liver. Also expressed in peripheral blood lymphocytes and a number of hematopoietic cell lines. Very low levels found in epithelial cell lines. Expressed in prostate cancer (PCa) cells and its expression intensity is directly linked to PCa progression. {ECO:0000269|PubMed:12674328, ECO:0000269|PubMed:18451096, ECO:0000269|PubMed:18497331}.; . . 0.39737 0.13400 0.018483465 55.44939844 220.53951 3.21071 LRAT 0.0969625060475692 0.770389678139562 0.132647815812869 lecithin retinol acyltransferase (phosphatidylcholine--retinol O-acyltransferase) FUNCTION: Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters. Retinyl esters are storage forms of vitamin A. LRAT plays a critical role in vision. It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis-retinaldehyde which is the chromophore for rhodopsin and the cone photopigments. {ECO:0000269|PubMed:9920938}.; DISEASE: Leber congenital amaurosis 14 (LCA14) [MIM:613341]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:11381255, ECO:0000269|PubMed:17011878, ECO:0000269|PubMed:18055821}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Hepatic stellate cells and endothelial cells (at protein level). Found at high levels in testis and liver, followed by retinal pigment epithelium, small intestine, prostate, pancreas and colon. Low expression observed in brain. In fetal tissues, expressed in retinal pigment epithelium and liver, and barely in the brain. {ECO:0000269|PubMed:18544127, ECO:0000269|PubMed:9920938}.; unclassifiable (Anatomical System);liver;testis;spleen;brain; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.09562 0.22456 0.03689118 56.64071715 48.55047 1.35958 LRBA 0.0442294366134414 0.955770563386559 1.53622058727772e-17 LPS responsive beige-like anchor protein FUNCTION: May be involved in coupling signal transduction and vesicle trafficking to enable polarized secretion and/or membrane deposition of immune effector molecules. {ECO:0000250}.; DISEASE: Immunodeficiency, common variable, 8, with autoimmunity (CVID8) [MIM:614700]: An autosomal recessive immunologic disorder associated with defective B-cell differentiation and decreased or absent antibody production. Affected individuals have early- childhood onset of recurrent infections, particularly respiratory infections, and also develop variable autoimmune disorders, including idiopathic thrombocytopenic purpura, autoimmune hemolytic anemia, and inflammatory bowel disease. {ECO:0000269|PubMed:22608502}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12160729}.; ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;iris;pituitary gland;testis;dura mater;germinal center;brain;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;pia mater;lung;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skin; 0.31593 . -2.513092117 0.925925926 4753.32179 13.94798 LRCH1 0.982396864430302 0.0176031159178159 1.96518818703732e-08 leucine-rich repeats and calponin homology (CH) domain containing 1 . . . unclassifiable (Anatomical System);heart;tongue;colon;blood;skin;bone marrow;breast;uterus;prostate;pancreas;whole body;lung;placenta;amnion;testis;cervix;head and neck;spleen;germinal center;mammary gland; ciliary ganglion;atrioventricular node; 0.16567 0.10276 0.003714825 54.06935598 336.92794 3.89975 LRCH2 0.915538078544407 0.0844377199000279 2.42015555649382e-05 leucine-rich repeats and calponin homology (CH) domain containing 2 . . . unclassifiable (Anatomical System);bone;liver; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.16063 0.09365 -0.007201372 53.19061099 42.20239 1.22827 LRCH3 1.19680658993201e-08 0.984194782562002 0.0158052054699324 leucine-rich repeats and calponin homology (CH) domain containing 3 . . . unclassifiable (Anatomical System);lymph node;heart;muscle;colon;blood;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;breast;optic nerve;lung;macula lutea;liver;testis;spleen;germinal center;kidney; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.25359 0.09814 -0.530852121 20.82448691 509.6375 4.62536 LRCH4 0.00017644288346698 0.998604093597113 0.00121946351941958 leucine-rich repeats and calponin homology (CH) domain containing 4 . . . lymphoreticular;medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;spleen;head and neck;cervix;mammary gland;aorta;stomach;thymus; . 0.17165 0.13466 -0.883608246 10.50365652 547.09868 4.75614 LRCOL1 . . . leucine-rich colipase like 1 . . . . . . . . . . . LRFN1 0.830755525384285 0.168504393705675 0.000740080910040251 leucine rich repeat and fibronectin type III domain containing 1 FUNCTION: Promotes neurite outgrowth in hippocampal neurons. Involved in the regulation and maintenance of excitatory synapses. Induces the clustering of excitatory postsynaptic proteins, including DLG4, DLGAP1, GRIA1 and GRIN1 (By similarity). {ECO:0000250}.; . . ovary;endometrium;bone;visual apparatus;brain;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;cingulate cortex;cerebellum; 0.48628 0.10733 . . 30.61696 0.97365 LRFN2 0.117460637188488 0.856182119461267 0.0263572433502445 leucine rich repeat and fibronectin type III domain containing 2 FUNCTION: Promotes neurite outgrowth in hippocampal neurons. Enhances the cell surface expression of 2 NMDA receptor subunits GRIN1 and GRIN2A. May play a role in redistributing DLG4 to the cell periphery (By similarity). {ECO:0000250}.; . . lymph node;frontal lobe;brain;stomach; . 0.24906 0.11684 -1.240018202 5.461193678 778.81291 5.52227 LRFN3 0.860302995582065 0.137574431513887 0.00212257290404777 leucine rich repeat and fibronectin type III domain containing 3 FUNCTION: Cell adhesion molecule that mediates homophilic cell- cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;parathyroid;choroid;skin;uterus;pancreas;lung;larynx;bone;placenta;head and neck;germinal center;kidney;brain;mammary gland;bladder;stomach;thymus; . 0.23922 0.11017 -0.420619508 25.72540694 559.95449 4.80689 LRFN4 0.942092245046717 0.0576835015251216 0.00022425342816151 leucine rich repeat and fibronectin type III domain containing 4 FUNCTION: Promotes neurite outgrowth in hippocampal neurons. May play a role in redistributing DLG4 to the cell periphery (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymphoreticular;urinary;colon;blood;uterus;pancreas;prostate;lung;larynx;bone;visual apparatus;duodenum;testis;kidney;brain;mammary gland;stomach; whole brain;amygdala;fetal brain;prefrontal cortex; 0.29958 0.11203 . . 1080.11643 6.30175 LRFN5 0.712324783241459 0.286991961304513 0.00068325545402804 leucine rich repeat and fibronectin type III domain containing 5 FUNCTION: Cell adhesion molecule that mediates homophilic cell- cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons. {ECO:0000269|PubMed:18227064, ECO:0000269|PubMed:18585462}.; . . unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;retina;uterus;prostate;optic nerve;whole body;lung;frontal lobe;macula lutea;testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;parietal lobe; 0.44439 0.10516 -0.868835007 10.65109696 34.24949 1.04764 LRG1 3.42349504526834e-05 0.360316217060419 0.639649547989129 leucine-rich alpha-2-glycoprotein 1 . . TISSUE SPECIFICITY: Plasma.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;blood;skin;bone marrow;breast;uterus;pancreas;lung;endometrium;placenta;liver;testis;kidney;brain;stomach;gall bladder; superior cervical ganglion;temporal lobe;liver;globus pallidus;atrioventricular node;pons;trigeminal ganglion; 0.09865 0.14889 0.400544645 76.40953055 1153.9259 6.47181 LRGUK 1.91691232979875e-08 0.991811264121865 0.00818871670901128 leucine-rich repeats and guanylate kinase domain containing FUNCTION: Involved in multiple aspects of sperm assembly including acrosome attachment, shaping of the sperm head and in the early aspects of axoneme development. {ECO:0000250|UniProtKB:Q9D5S7}.; . . unclassifiable (Anatomical System);lung;testis;stomach; superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12713 0.07447 1.807838544 96.95682944 3335.47852 11.05499 LRIF1 0.000245000652306933 0.923760093565572 0.0759949057821209 ligand dependent nuclear receptor interacting factor 1 FUNCTION: Represses the ligand-induced transcriptional activity of retinoic acid receptor alpha (RARA). This repression may occur through direct recruitment of histone deacetylases. {ECO:0000269|PubMed:17455211}.; . TISSUE SPECIFICITY: Widely expressed, with the highest expression levels in heart, liver and placenta. {ECO:0000269|PubMed:17455211}.; . . 0.06520 0.10313 -0.488577883 22.64685067 1294.73929 6.77271 LRIG1 0.835793558274592 0.164206208040023 2.33685385951547e-07 leucine-rich repeats and immunoglobulin-like domains 1 FUNCTION: Acts as a feedback negative regulator of signaling by receptor tyrosine kinases, through a mechanism that involves enhancement of receptor ubiquitination and accelerated intracellular degradation. {ECO:0000269|PubMed:15282549}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11414704}.; myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;lens;skeletal muscle;breast;pancreas;lung;cornea;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; prefrontal cortex; 0.74398 0.20510 0.332407981 73.54328851 4235.50177 12.94375 LRIG2 3.28910293719164e-12 0.889914078077476 0.110085921919235 leucine-rich repeats and immunoglobulin-like domains 2 . . TISSUE SPECIFICITY: Detected in all tissues analyzed. {ECO:0000269|PubMed:15145052}.; unclassifiable (Anatomical System);lung;cartilage;placenta;visual apparatus;liver;testis;colon;spleen;blood;kidney;brain;skeletal muscle;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13186 0.08593 -0.347208386 29.59424393 549.96935 4.76944 LRIG3 0.426287752609207 0.573711717677384 5.29713408941538e-07 leucine-rich repeats and immunoglobulin like domains 3 FUNCTION: May play a role in craniofacial and inner ear morphogenesis during embryonic development. May act within the otic vesicle epithelium to control formation of the lateral semicircular canal in the inner ear, possibly by restricting the expression of NTN1 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15203213}.; colon;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;gum;thyroid;bone;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;muscle;skeletal muscle;pancreas;lung;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.27502 0.12530 -0.723828344 14.26043878 171.34007 2.85415 LRIT1 2.92363820811623e-08 0.165811682107078 0.834188288656539 leucine-rich repeat, Ig-like and transmembrane domains 1 FUNCTION: Possible role in phototransduction. {ECO:0000303|PubMed:10777785}.; . . . . 0.13987 0.11302 -0.260839617 34.94928049 947.54435 5.96193 LRIT2 1.82785298018402e-09 0.0343561104287175 0.965643887743429 leucine-rich repeat, Ig-like and transmembrane domains 2 . . . . . 0.07641 . -0.262657925 34.93158764 2335.0259 8.94951 LRIT3 2.23302448594056e-08 0.0765387931942289 0.923461184475526 leucine-rich repeat, Ig-like and transmembrane domains 3 FUNCTION: Might facilitate FGFR1 exit from the endoplasmic reticulum to the Golgi. Could be a regulator of the FGFRs. {ECO:0000269|PubMed:22673519}.; DISEASE: Night blindness, congenital stationary, 1F (CSNB1F) [MIM:615058]: An autosomal recessive form of congenital stationary night blindness, a non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia. {ECO:0000269|PubMed:23246293}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);retina; dorsal root ganglion;subthalamic nucleus;testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.04978 . 1.910792163 97.4168436 9826.16415 21.60991 LRMP 0.0209127073492332 0.978939645563356 0.000147647087411046 lymphoid restricted membrane protein FUNCTION: Plays a role in the delivery of peptides to major histocompatibility complex (MHC) class I molecules; this occurs in a transporter associated with antigen processing (TAP)-independent manner. May play a role in taste signal transduction via ITPR3. May play a role during fertilization in pronucleus congression and fusion.; . TISSUE SPECIFICITY: Expressed at high levels in pre B-cells, mature B-cells and pre T-cells. Expressed at low levels in mature T-cells and plasma B-cells. Expressed in germinal center B-cells, splenic marginal zone cells and B-cell lymphomas. Expressed in neuronal cells in the cerebral cortex, epithelial cells in tonsil, adrenal glands, zymogen-producing cells in the stomach and epithelial cells in seminal vesicles. {ECO:0000269|PubMed:16739114, ECO:0000269|PubMed:8021504}.; ovary;salivary gland;intestine;colon;skin;bone marrow;prostate;endometrium;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach; prefrontal cortex;tumor;white blood cells;whole blood;tonsil; 0.37503 0.09709 0.264628794 70.5178108 5141.34096 14.73099 LRP1 1 1.45008684518029e-26 2.04766671977228e-66 LDL receptor related protein 1 FUNCTION: Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission.; . TISSUE SPECIFICITY: Most abundant in liver, brain and lung.; myocardium;ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;cerebral cortex;larynx;bone;thyroid;iris;testis;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;tongue;muscle;urinary;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;epididymis;placenta;visual apparatus;hippocampus;hypopharynx;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;adipose tissue;ciliary ganglion;pons;trigeminal ganglion; 0.65439 0.76644 -7.278555259 0.017692852 526.27186 4.68307 LRP1-AS . . . LRP1 antisense RNA . . . . . . . . . . . LRP1B 0.999999190192507 8.09807493334833e-07 4.74251015707574e-37 LDL receptor related protein 1B FUNCTION: Potential cell surface proteins that bind and internalize ligands in the process of receptor-mediated endocytosis.; . TISSUE SPECIFICITY: Expressed in thyroid gland and in salivary gland, as well as in adult and fetal brain. {ECO:0000269|PubMed:11384978}.; . . 0.62330 0.13316 -2.292084886 1.226704411 3259.72463 10.88020 LRP2 0.99999999999851 1.48993861047412e-12 3.65906499707677e-46 LDL receptor related protein 2 FUNCTION: Acts together with cubilin to mediate HDL endocytosis (By similarity). May participate in regulation of parathyroid- hormone and para-thyroid-hormone-related protein release. {ECO:0000250}.; . TISSUE SPECIFICITY: Absorptive epithelia, including renal proximal tubules.; unclassifiable (Anatomical System);ovary;spinal cord;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;breast;optic nerve;lung;epididymis;placenta;thyroid;macula lutea;iris;head and neck;kidney;mammary gland;brain; dorsal root ganglion;superior cervical ganglion;thyroid;ciliary ganglion;atrioventricular node;kidney;pons;trigeminal ganglion;skeletal muscle; 0.64775 0.54233 3.324377969 99.4220335 2032.71856 8.29976 LRP2BP 1.09566990321557e-06 0.560142607377868 0.439856296952229 LRP2 binding protein FUNCTION: May act as an adapter that regulates LRP2 function.; . . smooth muscle;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;bone;testis;germinal center;dura mater;brain;unclassifiable (Anatomical System);meninges;lymph node;heart;cartilage;islets of Langerhans;lens;breast;lung;pia mater;macula lutea;liver;spleen; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.53515 0.14080 -0.626318434 17.03231894 27.82914 0.89381 LRP3 0.0392366539527002 0.953983079507204 0.00678026654009584 LDL receptor related protein 3 FUNCTION: Probable receptor, which may be involved in the internalization of lipophilic molecules and/or signal transduction. Its precise role is however unclear, since it does not bind to very low density lipoprotein (VLDL) or to LRPAP1 in vitro.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in skeletal muscle and ovary. Expressed at intermediate level in heart, brain, liver, pancreas, prostate and small intestine. Weakly expressed in testis, colon and leukocyte. {ECO:0000269|PubMed:9693042}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;bone;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;urinary;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;kidney;mammary gland;stomach; pons; 0.18199 0.15191 . . 286.29049 3.62212 LRP4 0.10020880429216 0.899791195700632 7.20751508801609e-12 LDL receptor related protein 4 FUNCTION: Mediates SOST-dependent inhibition of bone formation. Functions as a specific facilitator of SOST-mediated inhibition of Wnt signaling. Plays a key role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between motor neuron and skeletal muscle. Directly binds AGRIN and recruits it to the MUSK signaling complex. Mediates the AGRIN- induced phosphorylation of MUSK, the kinase of the complex. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Alternatively, may be involved in the negative regulation of the canonical Wnt signaling pathway, being able to antagonize the LRP6-mediated activation of this pathway. More generally, has been proposed to function as a cell surface endocytic receptor binding and internalizing extracellular ligands for degradation by lysosomes. {ECO:0000269|PubMed:20381006, ECO:0000269|PubMed:21471202}.; DISEASE: Sclerosteosis 2 (SOST2) [MIM:614305]: A sclerosing bone dysplasia characterized by a generalized hyperostosis and sclerosis leading to a markedly thickened skull, with mandible, ribs, clavicles and all long bones also being affected. Due to narrowing of the foramina of the cranial nerves, facial nerve palsy, hearing loss and atrophy of the optic nerves can occur. Sclerosteosis is clinically and radiologically very similar to van Buchem disease, mainly differentiated by hand malformations and a large stature in sclerosteosis patients. {ECO:0000269|PubMed:21471202, ECO:0000269|PubMed:24234652}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myasthenic syndrome, congenital, 17 (CMS17) [MIM:616304]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. {ECO:0000269|PubMed:24234652}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in bone; present in osteoblasts and osteocytes. No expression is observed in osteoclast. Expressed in several regions of the brain. {ECO:0000269|PubMed:21471202}.; . . 0.57115 0.17022 -1.328641279 4.694503421 9909.87734 21.64220 LRP4-AS1 . . . LRP4 antisense RNA 1 . . . . . . . . . . . LRP5 0.998355570314237 0.00164442968332152 2.44158457138947e-12 LDL receptor related protein 5 FUNCTION: Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor- ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3- mediated phosphorylation and destruction of beta-catenin. Appears be required for postnatal control of vascular regression in the eye. Required for posterior patterning of the epiblast during gastrulation. {ECO:0000269|PubMed:11336703, ECO:0000269|PubMed:11448771, ECO:0000269|PubMed:14727154, ECO:0000269|PubMed:14731402, ECO:0000269|PubMed:15778503}.; DISEASE: Vitreoretinopathy, exudative 4 (EVR4) [MIM:601813]: A disorder of the retinal vasculature characterized by an abrupt cessation of growth of peripheral capillaries, leading to an avascular peripheral retina. This may lead to compensatory retinal neovascularization, which is thought to be induced by hypoxia from the initial avascular insult. New vessels are prone to leakage and rupture causing exudates and bleeding, followed by scarring, retinal detachment and blindness. Clinical features can be highly variable, even within the same family. Patients with mild forms of the disease are asymptomatic, and their only disease related abnormality is an arc of avascular retina in the extreme temporal periphery. {ECO:0000269|PubMed:15024691, ECO:0000269|PubMed:15346351, ECO:0000269|PubMed:15981244, ECO:0000269|PubMed:16929062, ECO:0000269|PubMed:19324841, ECO:0000269|PubMed:20340138, ECO:0000269|PubMed:24715757}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal disorder characterized by decreased bone mass and deterioration of bone microarchitecture without alteration in the composition of bone. The result is fragile bones and an increased risk of fractures, even after minimal trauma. Osteoporosis is a chronic condition of multifactorial etiology and is usually clinically silent until a fracture occurs. {ECO:0000269|PubMed:14727154, ECO:0000269|PubMed:15824851, ECO:0000269|PubMed:16234968}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Osteoporosis-pseudoglioma syndrome (OPPG) [MIM:259770]: A disease characterized by congenital or infancy-onset blindness and severe juvenile-onset osteoporosis and spontaneous fractures. Additional clinical manifestations may include microphthalmos, abnormalities of the iris, lens or vitreous, cataracts, short stature, microcephaly, ligamental laxity, mental retardation and hypotonia. {ECO:0000269|PubMed:11719191, ECO:0000269|PubMed:16252235, ECO:0000269|PubMed:16679074, ECO:0000269|PubMed:17437160, ECO:0000269|PubMed:18602879}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: High bone mass trait (HBM) [MIM:601884]: Rare phenotype characterized by exceptionally dense bones. HBM individuals show otherwise a completely normal skeletal structure and no other unusual clinical findings. {ECO:0000269|PubMed:11741193, ECO:0000269|PubMed:12015390, ECO:0000269|PubMed:15824861, ECO:0000269|PubMed:17295608}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Endosteal hyperostosis, Worth type (WENHY) [MIM:144750]: An autosomal dominant sclerosing bone dysplasia clinically characterized by elongation of the mandible, increased gonial angle, flattened forehead, and the presence of a slowly enlarging osseous prominence of the hard palate (torus palatinus). Serum calcium, phosphorus and alkaline phosphatase levels are normal. Radiologically, it is characterized by early thickening of the endosteum of long bones, the skull and of the mandible. With advancing age, the trabeculae of the metaphysis become thickened. WENHY becomes clinically and radiologically evident by adolescence, does not cause deformity except in the skull and mandible, and is not associated with bone pain or fracture. Affected patients have normal height, proportion, intelligence and longevity. {ECO:0000269|PubMed:12579474}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteopetrosis, autosomal dominant 1 (OPTA1) [MIM:607634]: A rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. OPTA1 is an autosomal dominant form characterized by generalized osteosclerosis most pronounced in the cranial vault. Patients are often asymptomatic, but some suffer from pain and hearing loss. It appears to be the only type of osteopetrosis not associated with an increased fracture rate. {ECO:0000269|PubMed:12579474}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Van Buchem disease 2 (VBCH2) [MIM:607636]: VBCH2 is an autosomal dominant sclerosing bone dysplasia characterized by cranial osteosclerosis, thickened calvaria and cortices of long bones, enlarged mandible and normal serum alkaline phosphatase levels. {ECO:0000269|PubMed:12579474}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, with the highest level of expression in the liver and in aorta. {ECO:0000269|PubMed:9790987}.; ovary;colon;parathyroid;choroid;skin;uterus;prostate;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;adrenal cortex;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;duodenum;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; . 0.07666 0.10394 -3.724445291 0.241802312 2445.60749 9.20072 LRP5L 3.87405123217097e-11 0.00690636993825028 0.993093630023009 LDL receptor related protein 5 like . . . . . 0.09203 . 0.756930627 86.79523473 937.76875 5.93572 LRP6 0.999978329943341 2.16700566586266e-05 5.31124675602577e-19 LDL receptor related protein 6 FUNCTION: Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor- ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3- mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation (By similarity). {ECO:0000250, ECO:0000269|PubMed:11357136, ECO:0000269|PubMed:11448771, ECO:0000269|PubMed:15778503, ECO:0000269|PubMed:16341017, ECO:0000269|PubMed:16513652, ECO:0000269|PubMed:17326769, ECO:0000269|PubMed:17400545, ECO:0000269|PubMed:19107203, ECO:0000269|PubMed:19293931, ECO:0000269|PubMed:19801552}.; DISEASE: Coronary artery disease, autosomal dominant, 2 (ADCAD2) [MIM:610947]: A common heart disease characterized by reduced or absent blood flow in one or more of the arteries that encircle and supply the heart. Its most important complication is acute myocardial infarction. {ECO:0000269|PubMed:17332414}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely coexpressed with LRP5 during embryogenesis and in adult tissues.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;parathyroid;blood;choroid;skin;skeletal muscle;breast;prostate;lung;frontal lobe;cornea;thyroid;placenta;visual apparatus;liver;spleen;cervix;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.47246 0.47221 -1.699477247 2.565463553 589.91488 4.92398 LRP8 0.999985760234446 1.42397652181836e-05 3.35876066425221e-13 LDL receptor related protein 8 FUNCTION: Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation. May also function as an endocytic receptor. {ECO:0000269|PubMed:12807892, ECO:0000269|PubMed:12899622, ECO:0000269|PubMed:12950167}.; DISEASE: Myocardial infarction 1 (MCI1) [MIM:608446]: A condition defined by the irreversible necrosis of heart muscle secondary to prolonged ischemia. {ECO:0000269|PubMed:17847002}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed mainly in brain and placenta. Also expressed in platelets and megakaryocytic cells. Not expressed in the liver. {ECO:0000269|PubMed:10218790, ECO:0000269|PubMed:10508213}.; ovary;salivary gland;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;bone;testis;bladder;brain;unclassifiable (Anatomical System);amygdala;pharynx;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;medulla oblongata;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;temporal lobe;testis;globus pallidus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.76530 0.26486 -0.883608246 10.50365652 1560.30616 7.31657 LRP10 0.000211411030039288 0.977954480363047 0.0218341086069136 LDL receptor related protein 10 FUNCTION: Probable receptor, which is involved in the internalization of lipophilic molecules and/or signal transduction. May be involved in the uptake of lipoprotein APOE in liver (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in blood leukocyte, lung, placenta, small intestine, liver, kidney, spleen, thymus, colon, skeletal muscle and heart. {ECO:0000269|PubMed:11123907}.; myocardium;medulla oblongata;ovary;salivary gland;colon;choroid;skin;retina;bone marrow;prostate;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;alveolus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;placenta;kidney;trigeminal ganglion;whole blood; 0.19861 0.12057 -0.130380821 44.03161123 489.35059 4.55317 LRP11 0.100969715328085 0.891713144969226 0.00731713970268879 LDL receptor related protein 11 . . . smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;lens;breast;pancreas;lung;placenta;head and neck;cervix;kidney;mammary gland;stomach; . 0.24657 . . . 3182.89784 10.74631 LRP12 0.969751548793752 0.0302480813141542 3.69892093567556e-07 LDL receptor related protein 12 FUNCTION: Probable receptor, which may be involved in the internalization of lipophilic molecules and/or signal transduction. May act as a tumor suppressor. {ECO:0000269|PubMed:12809483}.; . TISSUE SPECIFICITY: Widely expressed in heart, skeletal muscle, brain, lung, placenta and pancreas, but not in tissues consisting of a large number of epithelial cells, such as liver and kidney. Expressed at very low levels in a number of tumor-derived cell lines. {ECO:0000269|PubMed:9927190}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;sympathetic chain;developmental;adrenal cortex;parathyroid;skin;skeletal muscle;bile duct;uterus;lung;cochlea;endometrium;mesenchyma;bone;thyroid;placenta;visual apparatus;amnion;testis;head and neck;kidney;brain; testis - seminiferous tubule;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.82964 0.19728 -0.596992387 18.18825195 240.40002 3.34916 LRPAP1 0.00608430596153667 0.906837839029811 0.0870778550086523 LDL receptor related protein associated protein 1 FUNCTION: Interacts with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330.; DISEASE: Myopia 23, autosomal recessive (MYP23) [MIM:615431]: A refractive error of the eye, in which parallel rays from a distant object come to focus in front of the retina, vision being better for near objects than for far. {ECO:0000269|PubMed:23830514}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=In complex with the alpha-2-MR or gp330, it may have some role in the pathogenesis of membrane glomerular nephritis.; . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; amygdala;placenta;testis;caudate nucleus; 0.12830 0.12296 0.600782551 82.82613824 519.25317 4.65509 LRPPRC 0.000433777803620707 0.999566199139001 2.30573782504382e-08 leucine rich pentatricopeptide repeat containing FUNCTION: May play a role in RNA metabolism in both nuclei and mitochondria. In the nucleus binds to HNRPA1-associated poly(A) mRNAs and is part of nmRNP complexes at late stages of mRNA maturation which are possibly associated with nuclear mRNA export. May bind mature mRNA in the nucleus outer membrane. In mitochondria binds to poly(A) mRNA. Plays a role in translation or stability of mitochondrially encoded cytochrome c oxidase (COX) subunits. May be involved in transcription regulation. Cooperates with PPARGC1A to regulate certain mitochondrially encoded genes and gluconeogenic genes and may regulate docking of PPARGC1A to transcription factors. Seems to be involved in the transcription regulation of the multidrug-related genes MDR1 and MVP. Part of a nuclear factor that binds to the invMED1 element of MDR1 and MVP gene promoters. Binds single-stranded DNA (By similarity). {ECO:0000250, ECO:0000269|PubMed:11585913, ECO:0000269|PubMed:12832482, ECO:0000269|PubMed:15081402, ECO:0000269|PubMed:15139850, ECO:0000269|PubMed:15272088, ECO:0000269|PubMed:17050673}.; . TISSUE SPECIFICITY: Expressed ubiquitously. Expression is highest in heart, skeletal muscle, kidney and liver, intermediate in brain, non-mucosal colon, spleen and placenta, and lowest in small intestine, thymus, lung and peripheral blood leukocytes. {ECO:0000269|PubMed:11827465, ECO:0000269|PubMed:15139850}.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;pineal body;urinary;adrenal cortex;pharynx;blood;lens;breast;epididymis;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;placenta;hypopharynx;amnion;head and neck;kidney;stomach;aorta; thalamus;superior cervical ganglion;prefrontal cortex;tumor;globus pallidus;skeletal muscle;parietal lobe; 0.17853 0.32085 -1.651765382 2.765982543 423.11005 4.29551 LRR1 8.60725001636742e-07 0.304346731359191 0.695652407915808 leucine rich repeat protein 1 FUNCTION: May negatively regulate the 4-1BB-mediated signaling cascades which result in the activation of NK-kappaB and JNK1. Probable substrate recognition subunit of an ECS (Elongin BC- CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000269|PubMed:15601820}.; . TISSUE SPECIFICITY: Ubiquitous. Maximal expression was seen in the heart and skeletal muscle and minimal expression seen in the kidney.; medulla oblongata;ovary;salivary gland;intestine;colon;skin;prostate;whole body;endometrium;larynx;thyroid;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);pharynx;blood;breast;lung;nasopharynx;placenta;visual apparatus;liver;head and neck;cervix;kidney;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;pons;trigeminal ganglion; 0.07498 0.06845 -0.001743238 53.85114414 4122.57401 12.74709 LRRC1 0.573184205198454 0.426795462275249 2.03325262974631e-05 leucine rich repeat containing 1 . . TISSUE SPECIFICITY: Expressed strongly in testis and placenta, followed by heart, lung, kidney, thyroid, trachea, colon, prostate and pancreas. {ECO:0000269|PubMed:11440998}.; . . 0.27177 0.13168 -0.402212257 26.7338995 124.67686 2.42766 LRRC2 4.7683181051694e-05 0.655033876442869 0.344918440376079 leucine rich repeat containing 2 . . . unclassifiable (Anatomical System);myocardium;amygdala;heart;cartilage;colon;blood;skin;uterus;thyroid;head and neck;kidney;stomach; superior cervical ganglion;skeletal muscle; 0.29372 0.07609 1.24016994 93.34748762 2614.02922 9.57072 LRRC2-AS1 . . . LRRC2 antisense RNA 1 . . . . . . . . . . . LRRC3 0.00645694832852908 0.510887202221109 0.482655849450362 leucine rich repeat containing 3 . . TISSUE SPECIFICITY: Widely expressed; detected in testis, lung, small intestine, breast, brain, heart, bone marrow, placenta, colon, fetal brain, liver, fetal liver, thymus, salivary gland, spinal cord, spleen, trachea and adrenal gland.; unclassifiable (Anatomical System); subthalamic nucleus;superior cervical ganglion;atrioventricular node;skeletal muscle; 0.14351 0.12285 0.130533008 63.35810333 57.21127 1.52296 LRRC3-AS1 . . . LRRC3 antisense RNA 1 (head to head) . . . . . . . . . . . LRRC3B 0.228541145950027 0.646553399403529 0.124905454646444 leucine rich repeat containing 3B . . . . . 0.30334 0.11262 -0.185391282 39.67916962 3.24231 0.11680 LRRC3C . . . leucine rich repeat containing 3C . . . . . . . . . 245.87316 3.38290 LRRC3DN . . . LRRC3 downstream neighbor (non-protein coding) . . . . . . . . . 88.53413 2.01773 LRRC4 0.877360671606607 0.12232568593222 0.000313642461173227 leucine rich repeat containing 4 FUNCTION: Synaptic adhesion protein. Regulates the formation of exitatory synapses through the recruitment of pre-and-postsynaptic proteins. Organize the lamina/pathway-specific differentiation of dendrites. Plays a important role for auditory synaptic responses. Involved in the suppression of glioma (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in brain. {ECO:0000269|PubMed:15967442}.; unclassifiable (Anatomical System);ovary;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;lung;endometrium;epididymis;placenta;macula lutea;hippocampus;testis;kidney;mammary gland;brain; whole brain;superior cervical ganglion;parietal lobe;skeletal muscle; 0.42966 0.14781 -0.244249595 36.17008728 128.95739 2.47491 LRRC4B 0.297156810786189 0.683027350384703 0.0198158388291076 leucine rich repeat containing 4B FUNCTION: Synaptic adhesion protein. Regulates the formation of excitatory synapses. The trans-synaptic adhesion between LRRC4B and PTPRF regulates the formation of excitatory synapses in a bidirectional manner (By similarity). {ECO:0000250}.; . . . . 0.20925 0.11180 -0.381986487 27.68931352 759.08833 5.45937 LRRC4C 0.953730868705953 0.0461412230396495 0.00012790825439789 leucine rich repeat containing 4C FUNCTION: May promote neurite outgrowth of developing thalamic neurons. {ECO:0000269|PubMed:14595443}.; . TISSUE SPECIFICITY: Highly expressed in the cerebral cortex, including frontal, parietal and occipital lobes. Putamen, amygdala, hippocampus and medulla oblongata show moderate expression. Caudate nucleus and thalamus express small amounts, whereas other brain regions show very weak or no expression. {ECO:0000269|PubMed:14595443}.; unclassifiable (Anatomical System);optic nerve;lung;heart;macula lutea;testis;fovea centralis;choroid;lens;brain;skeletal muscle;retina; dorsal root ganglion;subthalamic nucleus;medulla oblongata;superior cervical ganglion;occipital lobe;globus pallidus;atrioventricular node;pons;trigeminal ganglion;parietal lobe;cingulate cortex; 0.85527 0.14229 -0.799052816 12.45576787 78.16654 1.86462 LRRC6 8.29727962409699e-08 0.723564559004431 0.276435358022773 leucine rich repeat containing 6 FUNCTION: May play a role in dynein arm assembly, hence essential for proper axoneme building for cilia motility. {ECO:0000269|PubMed:23122589}.; . TISSUE SPECIFICITY: Expressed predominantly in testis and in nasal epithelial cells. {ECO:0000269|PubMed:23122589}.; unclassifiable (Anatomical System);medulla oblongata;colon;parathyroid;breast;prostate;lung;nasopharynx;bone;hippocampus;testis;spleen;kidney; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.05652 0.10784 0.374860183 75.43052607 1596.16179 7.39021 LRRC6P1 . . . leucine rich repeat containing 6 pseudogene 1 . . . . . . . . . . . LRRC7 0.999998533487013 1.46651298723192e-06 1.09585617525584e-17 leucine rich repeat containing 7 FUNCTION: Required for normal synaptic spine architecture and function. Necessary for DISC1 and GRM5 localization to postsynaptic density complexes and for both N-methyl D-aspartate receptor-dependent and metabotropic glutamate receptor-dependent long term depression. {ECO:0000269|PubMed:11729199}.; . TISSUE SPECIFICITY: Brain-specific. Isoform 3 is ubiquitously expressed. {ECO:0000269|PubMed:12525888}.; unclassifiable (Anatomical System);whole body;lung;frontal lobe;testis;brain;skeletal muscle; dorsal root ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.42578 0.12755 -1.368693559 4.482189196 157.64981 2.74333 LRRC8A 0.916104676238055 0.0837780854423358 0.000117238319609253 leucine-rich repeat containing 8 family member A FUNCTION: Essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and may also conduct organic osmolytes like taurine. It is unclear whether LRRC8A constitutes a pore-forming subunit or whether it is closely associated with the pore and mediates channel properties such as ion selectivity. Involved in B-cell development: required for the pro-B cell to pre-B cell transition. Also required for T-cell development. {ECO:0000269|PubMed:14660746, ECO:0000269|PubMed:24725410, ECO:0000269|PubMed:24790029}.; DISEASE: Agammaglobulinemia 5, autosomal dominant (AGM5) [MIM:613506]: A primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life. {ECO:0000269|PubMed:14660746}. Note=The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving LRRC8 has been found in a patient with congenital agammaglobulinemia. Translocation t(9;20)(q33.2;q12). The translocation truncates the LRRC8 gene, resulting in deletion of the eighth, ninth, and half of the seventh LRR domains.; TISSUE SPECIFICITY: Expressed in brain, kidney, ovary, lung, liver, heart, and fetal brain and liver. Found at high levels in bone marrow; lower levels are detected in peripheral blood cells. Expressed on T-cells as well as on B-lineage cells. {ECO:0000269|PubMed:10718198, ECO:0000269|PubMed:14660746}.; smooth muscle;ovary;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;bone;testis;germinal center;ciliary body;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;hippocampus;head and neck;stomach; amygdala;lung;prefrontal cortex;cerebellum; 0.27091 0.11809 -1.572589134 3.161122906 71.68911 1.76247 LRRC8B 0.806424943328372 0.193356561835262 0.000218494836366841 leucine-rich repeat containing 8 family member B FUNCTION: Component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and may also conduct organic osmolytes like taurine. It is unclear whether LRRC8B constitutes a pore-forming subunit or whether it is closely associated with the pore (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);myocardium;heart;islets of Langerhans;sympathetic chain;colon;skeletal muscle;uterus;prostate;lung;cerebral cortex;thyroid;hippocampus;hypopharynx;liver;testis;head and neck;kidney;brain;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;occipital lobe;medulla oblongata;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;pons;parietal lobe;cingulate cortex; 0.73632 . -1.352082458 4.582448691 156.14969 2.73082 LRRC8C 0.0165279231134417 0.978422976825632 0.00504910006092605 leucine-rich repeat containing 8 family member C FUNCTION: Component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and may also conduct organic osmolytes like taurine. It is unclear whether LRRC8C constitutes a pore-forming subunit or whether it is closely associated with the pore. May play a role in adipogenesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at highest levels in skeletal muscle, and at moderate levels in heart, lung and peripheral blood leukocytes. {ECO:0000269|PubMed:15564382}.; . . 0.51382 0.11031 0.090079492 60.64519934 1405.17584 7.00594 LRRC8D 0.868441355312111 0.131481863165088 7.67815228015199e-05 leucine-rich repeat containing 8 family member D FUNCTION: Component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and may also conduct organic osmolytes like taurine. It is unclear whether LRRC8D constitutes a pore-forming subunit or whether it is closely associated with the pore (By similarity). Mediates the import of the antibiotic blasticidin-S into cell (PubMed:24782309). {ECO:0000250, ECO:0000269|PubMed:24782309}.; . . ovary;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;tongue;spinal cord;blood;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;hypothalamus;spinal cord;globus pallidus;caudate nucleus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.29903 0.11301 -0.777005578 12.9747582 66.19617 1.67571 LRRC8E 0.000781502371027772 0.927497409813153 0.0717210878158188 leucine-rich repeat containing 8 family member E FUNCTION: Component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and may also conduct organic osmolytes like taurine. It is unclear whether LRRC8E constitutes a pore-forming subunit or whether it is closely associated with the pore (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;uterus;prostate;lung;bone;placenta;thyroid;head and neck;kidney;bladder;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.20357 . 0.407828206 76.50979004 505.97189 4.61635 LRRC9 . . . leucine rich repeat containing 9 . . . unclassifiable (Anatomical System);lung;testis; subthalamic nucleus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.08452 . . . 859.87184 5.71827 LRRC10 0.00919176631881308 0.585554781964783 0.405253451716404 leucine rich repeat containing 10 FUNCTION: May play important roles in cardiac development and/or cardiac function. {ECO:0000250}.; . . . . 0.12064 0.10430 -0.137658575 43.57159707 79.35227 1.88239 LRRC10B . . . leucine rich repeat containing 10B . . . . . . . . . 24.34086 0.79964 LRRC14 0.00665273421562502 0.915049505592547 0.0782977601918277 leucine rich repeat containing 14 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;blood;lens;pancreas;lung;placenta;macula lutea;hypopharynx;liver;spleen;head and neck;kidney;stomach; subthalamic nucleus;superior cervical ganglion;testis - interstitial;tongue;temporal lobe;white blood cells;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.08387 0.11308 -1.001120478 8.321538099 31.69801 0.99762 LRRC14B 3.30673334839527e-09 0.0253827721589011 0.974617224534366 leucine rich repeat containing 14B . . . retina; superior cervical ganglion;fetal liver;skeletal muscle; . . . . 329.80992 3.85906 LRRC15 1.35693788842668e-06 0.216845703555042 0.783152939507069 leucine rich repeat containing 15 . . TISSUE SPECIFICITY: Brain and placenta.; unclassifiable (Anatomical System);heart;cartilage;skin;uterus;breast;pancreas;whole body;lung;placenta;bone;mammary gland;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.61867 0.15658 -0.903841325 10.14390186 2318.53141 8.91478 LRRC16A 0.502318842467879 0.497681155079786 2.4523342301656e-09 leucine rich repeat containing 16A FUNCTION: Binds CAPZA2 with high affinity and significantly decreases CAPZA2 affinity for actin barbed ends. Increases the rate of elongation from seeds in the presence of CAPZA2, however, seems unable to nucleate filaments. Rapidly uncaps barbed ends capped by CAPZA2 and enhances barbed-end actin polymerization (By similarity). May control actin dynamics in lamellipodia. Required for cell migration. {ECO:0000250, ECO:0000269|PubMed:16054028, ECO:0000269|PubMed:19846667}.; . TISSUE SPECIFICITY: Expressed in lung, placenta, small intestine, liver, thymus, colon, skeletal muscle, heart and brain. Higher expression in kidney. {ECO:0000269|PubMed:16054028}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;bile duct;breast;lung;placenta;macula lutea;visual apparatus;liver;amnion;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.27806 0.09713 -0.857930839 10.95187544 388.35252 4.15049 LRRC16B 4.86594856632392e-05 0.999951336091793 4.42254364760956e-09 leucine rich repeat containing 16B . . TISSUE SPECIFICITY: Widely expressed, with much higher levels in fetal tissues than in adult ones. Up-regulated in certain cancer tissues. {ECO:0000269|PubMed:21102520}.; unclassifiable (Anatomical System);colon;fovea centralis;choroid;lens;retina;optic nerve;lung;frontal lobe;larynx;macula lutea;testis;head and neck;brain;bladder;cerebellum; globus pallidus;trigeminal ganglion;skeletal muscle; 0.41974 . -0.65224539 16.15357396 4426.78806 13.34196 LRRC17 6.63875292520614e-08 0.141210172297392 0.858789761315079 leucine rich repeat containing 17 FUNCTION: Involved in bone homeostasis. Acts as a negative regulator of RANKL-induced osteoclast precursor differentiation from bone marrow precursors (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in osteoblast cell lines. Well expressed in ovary, heart, pancreas, skeletal muscle, lung, and fetal kidney and lung and only at the basal levels in the other tissues examined including adult kidney. More expressed in S-type neuroblastoma cells than in N-type neuroblastoma cells. {ECO:0000269|PubMed:19336404, ECO:0000269|PubMed:8982252}.; ovary;sympathetic chain;colon;fovea centralis;skin;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;pancreas;pia mater;lung;trabecular meshwork;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;smooth muscle;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.45399 0.10245 1.107875794 92.03821656 2289.54911 8.85466 LRRC18 0.00012417329035041 0.224436770081055 0.775439056628594 leucine rich repeat containing 18 FUNCTION: May be involved in the regulation of spermatogenesis and sperm maturation. {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;testis;cervix; uterus;testis - interstitial;testis; 0.14819 0.10438 0.242582624 69.45623968 3897.54567 12.32519 LRRC19 5.16703198852798e-05 0.436090502147142 0.563857827532973 leucine rich repeat containing 19 . . . . . 0.05655 0.06410 0.729426781 86.17008728 200.76015 3.06347 LRRC20 0.136831660590252 0.779835438347753 0.0833329010619949 leucine rich repeat containing 20 . . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach; atrioventricular node;trigeminal ganglion;skeletal muscle; 0.29080 0.11450 -0.293801652 32.93819297 40.72629 1.19335 LRRC23 0.000915908771944211 0.940073000268467 0.0590110909595885 leucine rich repeat containing 23 . . . medulla oblongata;ovary;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;spinal cord;blood;lens;skeletal muscle;lung;placenta;macula lutea;kidney;stomach; subthalamic nucleus;testis;ciliary ganglion;atrioventricular node;cerebellum; 0.24143 0.11683 -0.135838822 43.77211607 3968.69057 12.46393 LRRC24 0.775315502193512 0.223066101228905 0.00161839657758277 leucine rich repeat containing 24 . . . . . 0.18706 0.10259 . . 1876.3752 7.96752 LRRC25 0.943472206020923 0.0563167082955182 0.000211085683559275 leucine rich repeat containing 25 FUNCTION: May be involved in the activation of cells of innate and acquired immunity. {ECO:0000269|PubMed:12384430}.; . TISSUE SPECIFICITY: Expressed in plasmacytoid dendritic cells (PDC), monocyte-derived dendritic cells (MDDC), granulocytes, monocytes, B-lymphocytes, peripheral blood leukocytes, spleen, bone marrow, and, to a lesser extent, lymph nodes, fetal liver, and appendix but not in thymus. {ECO:0000269|PubMed:12384430}.; unclassifiable (Anatomical System);lung;islets of Langerhans;bone;placenta;spleen;blood;bone marrow; whole blood; 0.11613 0.11242 0.72761005 86.08162302 126.23224 2.44556 LRRC26 0.028439437509515 0.581893241025004 0.389667321465481 leucine rich repeat containing 26 FUNCTION: Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Required for the conversion of BK alpha channels from a high-voltage to a low- voltage activated channel type in non-excitable cells. These are characterized by negative membrane voltages and constant low levels of calcium. {ECO:0000269|PubMed:20613726, ECO:0000269|PubMed:22547800}.; . TISSUE SPECIFICITY: Isoform 1 is expressed highly in normal prostate and salivary gland, very weakly in colon, pancreas, and intestine, and not at all in other tissues. Isoform 1 is expressed highly in many cancer cell lines and in breast cancer, pancreatic cancer and colon cancer. Isoform 2 is expressed in cancer cell lines. {ECO:0000269|PubMed:16585525, ECO:0000269|PubMed:19250639}.; . . 0.19218 0.10444 . . 1485.495 7.17293 LRRC27 9.74868422732027e-14 0.0199017156143067 0.980098284385596 leucine rich repeat containing 27 . . . unclassifiable (Anatomical System);medulla oblongata;islets of Langerhans;colon;fovea centralis;choroid;lens;retina;pancreas;optic nerve;lung;macula lutea;iris;testis;kidney;brain;mammary gland;stomach; . 0.06510 . -0.793601146 12.57372022 330.4553 3.86501 LRRC28 8.59828754914425e-05 0.929674981724447 0.0702390354000613 leucine rich repeat containing 28 . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12816 0.11802 -0.404032746 26.53338051 157.2747 2.74082 LRRC29 0.00720375911547779 0.767721291605106 0.225074949279416 leucine rich repeat containing 29 FUNCTION: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation.; . TISSUE SPECIFICITY: Expressed in heart, kidney, liver, lung and pancreas. {ECO:0000269|PubMed:10531037}.; unclassifiable (Anatomical System);pancreas;optic nerve;macula lutea;spleen;fovea centralis;choroid;lens;brain;skin;retina; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16968 . 0.41713504 76.95800896 785.81577 5.53814 LRRC30 2.18765652608836e-08 0.0208599732158236 0.979140004907611 leucine rich repeat containing 30 . . . . . 0.14275 . 0.174625237 65.9648502 52.11032 1.42691 LRRC31 5.24031482355817e-06 0.865724635745389 0.134270123939787 leucine rich repeat containing 31 . . . ovary;thyroid;placenta;liver;spleen;parathyroid; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion; 0.08504 . 1.287903524 93.83698986 643.20122 5.09497 LRRC32 0.0215755256662984 0.908258716985275 0.0701657573484262 leucine rich repeat containing 32 . . TISSUE SPECIFICITY: Preferentially expressed in regulatory T-cells (T(regs)). {ECO:0000269|PubMed:21615933}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; heart;adrenal gland;placenta;adrenal cortex; 0.21008 0.13100 -1.214341017 5.67940552 334.14503 3.88452 LRRC34 5.88856097246935e-07 0.431575022220722 0.56842438892318 leucine rich repeat containing 34 . . . unclassifiable (Anatomical System);hypothalamus;fovea centralis;choroid;lens;skin;retina;prostate;optic nerve;lung;endometrium;macula lutea;visual apparatus;pituitary gland;testis;germinal center;kidney; . 0.08456 . 0.240763792 69.36777542 1908.82751 8.04611 LRRC34P1 . . . leucine rich repeat containing 34 pseudogene 1 . . . . . . . . . . . LRRC34P2 . . . leucine rich repeat containing 34 pseudogene 2 . . . . . . . . . . . LRRC36 3.63105528140864e-10 0.512459966317782 0.487540033319112 leucine rich repeat containing 36 . . . lung;heart;testis;colon;brain; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.29907 . 0.310540264 72.65864591 4709.63428 13.84451 LRRC37A 0.890487355591061 0.108382688832165 0.00112995557677389 leucine rich repeat containing 37A . . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);heart;lacrimal gland;muscle;blood;skeletal muscle;breast;lung;epididymis;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;stomach; . 0.03553 . . . 311.91441 3.75872 LRRC37A2 . . . leucine-rich repeat containing 37 member A2 . . . unclassifiable (Anatomical System);medulla oblongata;heart;ovary;colon;blood;skeletal muscle;bone marrow;breast;whole body;larynx;nasopharynx;thyroid;placenta;testis;head and neck;kidney;brain;gall bladder; . . . . . 461.8726 4.45668 LRRC37A3 . . . leucine-rich repeat containing 37 member A3 . . . medulla oblongata;smooth muscle;ovary;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;bladder;brain;gall bladder;unclassifiable (Anatomical System);heart;lacrimal gland;tongue;muscle;blood;skeletal muscle;breast;lung;epididymis;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;stomach; cerebellum; . . . . 193.95095 3.02097 LRRC37A4P . . . leucine-rich repeat containing 37 member A4, pseudogene . . . . . 0.07214 . . . . . LRRC37A5P . . . leucine-rich repeat containing 37 member A5, pseudogene . . . . . 0.10668 . . . . . LRRC37A6P . . . leucine-rich repeat containing 37 member A6, pseudogene . . . . . . . . . . . LRRC37A7P . . . leucine-rich repeat containing 37 member A7, pseudogene . . . . . . . . . . . LRRC37A8P . . . leucine-rich repeat containing 37 member A8, pseudogene . . . . . . . . . . . LRRC37A9P . . . leucine-rich repeat containing 37 member A9, pseudogene . . . . . . . . . . . LRRC37A10P . . . leucine-rich repeat containing 37 member A10, pseudogene . . . . . . . . . . . LRRC37A11P . . . leucine-rich repeat containing 37 member A11, pseudogene . . . . . . . . . . . LRRC37A12P . . . leucine-rich repeat containing 37 member A12, pseudogene . . . . . . . . . . . LRRC37A13P . . . leucine-rich repeat containing 37 member A13, pseudogene . . . . . . . . . . . LRRC37A14P . . . leucine-rich repeat containing 37 member A14, pseudogene . . . . . . . . . . . LRRC37A15P . . . leucine-rich repeat containing 37 member A15, pseudogene . . . . . . . . . . . LRRC37A16P . . . leucine-rich repeat containing 37 member A16, pseudogene . . . . . . . . . . . LRRC37A17P . . . leucine-rich repeat containing 37 member A17, pseudogene . . . . . . . . . . . LRRC37B 0.948665375189349 0.0513343446484413 2.80162209537382e-07 leucine rich repeat containing 37B . . . lymphoreticular;medulla oblongata;colon;skin;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;blood;breast;lung;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - interstitial;globus pallidus;testis;ciliary ganglion;atrioventricular node;skin;skeletal muscle; 0.02996 . 0.650339974 84.15310215 139.25633 2.57338 LRRC37BP1 . . . leucine rich repeat containing 37B pseudogene 1 . . . . . 0.11460 . . . . . LRRC38 . . . leucine rich repeat containing 38 FUNCTION: Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Modulates gating properties by producing a marked shift in the BK channel's voltage dependence of activation in the hyperpolarizing direction, and in the absence of calcium. {ECO:0000269|PubMed:22547800}.; . TISSUE SPECIFICITY: Mainly expressed in adrenal gland, thymus and skeletal muscle. {ECO:0000269|PubMed:22547800}.; . . 0.09642 0.09812 . . 2524.97056 9.37216 LRRC39 0.0397074605005753 0.953633354489866 0.00665918500955864 leucine rich repeat containing 39 . . . unclassifiable (Anatomical System);heart;ovary;parathyroid;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;optic nerve;whole body;lung;placenta;macula lutea;testis;germinal center;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.35137 0.09161 -0.558357437 19.54470394 419.98843 4.28121 LRRC40 2.64692039855136e-19 0.00103598459679784 0.998964015403202 leucine rich repeat containing 40 . . . . . 0.47479 0.10119 0.600782551 82.82613824 154.46973 2.71668 LRRC41 0.999804640576002 0.000195359226011043 1.97986665196877e-10 leucine rich repeat containing 41 FUNCTION: Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000269|PubMed:15601820}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;duodenum;head and neck;kidney;stomach;aorta;thymus; whole brain;superior cervical ganglion;testis - seminiferous tubule;heart;thyroid;placenta;prefrontal cortex;ciliary ganglion;atrioventricular node;cerebellum; 0.16957 . -0.44448505 24.46331682 1913.83525 8.05036 LRRC42 1.66639189391607e-06 0.651681784537144 0.348316549070962 leucine rich repeat containing 42 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;urinary;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach;aorta; superior cervical ganglion;atrioventricular node; 0.10409 . -0.111973265 45.35857514 79.22763 1.88034 LRRC43 6.70342212695841e-14 0.0159854856293826 0.98401451437055 leucine rich repeat containing 43 . . . unclassifiable (Anatomical System);lung;kidney;stomach; ciliary ganglion; 0.05087 . 0.404185162 76.48619958 2151.99418 8.53257 LRRC45 3.1506860909144e-06 0.932415565024256 0.0675812842896526 leucine rich repeat containing 45 FUNCTION: Component of the proteinaceous fiber-like linker between two centrioles, required for centrosome cohesion. {ECO:0000269|PubMed:24035387}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;stomach; . 0.19260 . -0.510624372 21.65015334 300.03856 3.69326 LRRC46 0.000135433194771157 0.85318912907374 0.146675437731489 leucine rich repeat containing 46 . . . unclassifiable (Anatomical System);medulla oblongata;lung;cartilage;hypothalamus;testis;germinal center;brain;retina; . 0.06667 . -0.047654689 50.22410946 249.90163 3.40570 LRRC47 0.60383218752352 0.394290079205508 0.00187773327097156 leucine rich repeat containing 47 . . . . . 0.17731 . -0.909290275 10.03184713 262.97721 3.48028 LRRC49 0.446510312132105 0.553478596746636 1.10911212591732e-05 leucine rich repeat containing 49 . . . myocardium;colon;parathyroid;fovea centralis;skin;retina;uterus;whole body;frontal lobe;endometrium;thyroid;pituitary gland;testis;amniotic fluid;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;bile duct;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland; . 0.18522 0.11023 -0.666770504 15.86459071 4621.78815 13.66012 LRRC52 0.00132907118787168 0.652146590650871 0.346524338161258 leucine rich repeat containing 52 FUNCTION: Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Modulates gating properties by producing a marked shift in the BK channel's voltage dependence of activation in the hyperpolarizing direction, and in the absence of calcium. KCNU1 channel auxiliary protein. May modulate KCNU1 gating properties. {ECO:0000269|PubMed:22547800, ECO:0000269|PubMed:23129643}.; . TISSUE SPECIFICITY: Mainly expressed in testis and skeletal muscle. {ECO:0000269|PubMed:22547800}.; placenta;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13483 . -0.091746757 46.91554612 184.69213 2.94900 LRRC53 . . . leucine rich repeat containing 53 . . . . . 0.50229 . . . 2132.91595 8.49786 LRRC55 0.677224186440864 0.318110263777901 0.0046655497812357 leucine rich repeat containing 55 FUNCTION: Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Modulates gating properties by producing a marked shift in the BK channel's voltage dependence of activation in the hyperpolarizing direction, and in the absence of calcium. {ECO:0000269|PubMed:22547800}.; . TISSUE SPECIFICITY: Mainly expressed in brain. {ECO:0000269|PubMed:22547800}.; . . 0.15676 . -0.558357437 19.54470394 579.47929 4.87799 LRRC56 0.000110646268059748 0.94853623072106 0.0513531230108804 leucine rich repeat containing 56 . . . unclassifiable (Anatomical System);medulla oblongata;lung;heart;endometrium;visual apparatus;testis;colon;kidney;germinal center;spinal ganglion; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.11729 . 2.383068283 98.4725171 1040.63565 6.19319 LRRC57 0.000686890124895267 0.74727556420712 0.252037545667985 leucine rich repeat containing 57 . . . unclassifiable (Anatomical System);lymph node;ovary;heart;islets of Langerhans;colon;parathyroid;choroid;skin;uterus;pancreas;lung;endometrium;larynx;placenta;hypopharynx;testis;cervix;head and neck;germinal center;kidney;brain;mammary gland;bladder;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.27840 0.10352 -0.075159878 47.78839349 14.00809 0.50850 LRRC58 0.0191326932920517 0.899445722411937 0.081421584296011 leucine rich repeat containing 58 . . . unclassifiable (Anatomical System);ovary;salivary gland;pharynx;colon;blood;skin;skeletal muscle;breast;prostate;lung;bone;placenta;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland;bladder;stomach; superior cervical ganglion;globus pallidus; 0.30500 0.11124 . . 59.13037 1.55874 LRRC59 0.482144865133273 0.512931923192543 0.00492321167418413 leucine rich repeat containing 59 FUNCTION: Required for nuclear import of FGF1, but not that of FGF2. Might regulate nuclear import of exogenous FGF1 by facilitating interaction with the nuclear import machinery and by transporting cytosolic FGF1 to, and possibly through, the nuclear pores. {ECO:0000269|PubMed:22321063}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11964394}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;placenta;duodenum;amnion;head and neck;kidney;stomach;thymus; superior cervical ganglion;adrenal gland; 0.09793 0.12605 -0.339715008 30.06605331 37.11 1.10883 LRRC61 0.00519555071411505 0.703717138409591 0.291087310876294 leucine rich repeat containing 61 . . . medulla oblongata;ovary;umbilical cord;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;endometrium;pituitary gland;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;epidermis;nervous;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;pancreas;lung;placenta;hippocampus;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; ciliary ganglion;trigeminal ganglion; 0.18478 0.09739 0.639420866 83.8995046 1738.13671 7.69402 LRRC63 . . . leucine rich repeat containing 63 . . . . . . . . . 729.77561 5.36365 LRRC66 9.28497779822103e-14 0.00523974746087225 0.994760252539035 leucine rich repeat containing 66 . . . breast;uterus;heart;pituitary gland;skin; . . . 0.42623145 77.29417315 147.10425 2.64220 LRRC69 . . . leucine rich repeat containing 69 . . . placenta; . . . . . 72.62196 1.77816 LRRC70 . . . leucine rich repeat containing 70 FUNCTION: Renders cells highly sensitive to the activation by cytokines and lipopolysaccharide (LPS). {ECO:0000269|PubMed:12767927}.; . TISSUE SPECIFICITY: Expressed at low levels in many tissues, including smooth muscle, brain, uterus, pancreas, cartilage, adipose, spleen and testis. {ECO:0000269|PubMed:12767927}.; unclassifiable (Anatomical System);prostate;smooth muscle;lung;placenta;testis;stomach;retina; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin; . . 0.768075923 86.8895966 85.82976 1.97833 LRRC71 0.00904921773201473 0.978944704414998 0.0120060778529876 leucine rich repeat containing 71 . . . . . 0.12805 . 1.041730357 91.28921916 4642.30851 13.70679 LRRC72 . . . leucine rich repeat containing 72 . . . . . . . . . 189.25967 2.98727 LRRC73 0.635116132508035 0.358059241808322 0.00682462568364239 leucine rich repeat containing 73 . . . . . 0.58454 . 0.03689118 56.64071715 79.00581 1.87726 LRRC74A . . . leucine rich repeat containing 74A . . . . . 0.34295 . -0.176292081 40.56381222 . . LRRC74B . . . leucine rich repeat containing 74B . . . . . . . . . . . LRRC75A . . . leucine rich repeat containing 75A . . . . . 0.22797 . 0.926041233 89.65557915 . . LRRC75A-AS1 . . . LRRC75A antisense RNA 1 . . . . . 0.01204 . . . . . LRRC75B . . . leucine rich repeat containing 75B . . . . . 0.08412 0.09623 1.576373448 95.7537155 . . LRRCC1 5.39715886159611e-19 0.0215550992245847 0.978444900775415 leucine rich repeat and coiled-coil centrosomal protein 1 FUNCTION: Required for the organization of the mitotic spindle. Maintains the structural integrity of centrosomes during mitosis. {ECO:0000269|PubMed:18728398}.; . . smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;endometrium;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;hypothalamus;pharynx;blood;lens;lung;macula lutea;visual apparatus;liver;cervix;kidney;stomach;aorta; testis;globus pallidus; 0.17250 0.09643 1.894214943 97.33427695 1340.281 6.87206 LRRD1 . . . leucine-rich repeats and death domain containing 1 . . . testis; . . . 0.257356108 69.83368719 3262.69222 10.89381 LRRFIP1 0.365512490408218 0.633984855953127 0.000502653638655243 leucine rich repeat (in FLII) interacting protein 1 FUNCTION: Transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. May control smooth muscle cells proliferation following artery injury through PDGFA repression. May also bind double-stranded RNA. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding. {ECO:0000269|PubMed:10364563, ECO:0000269|PubMed:14522076, ECO:0000269|PubMed:16199883, ECO:0000269|PubMed:19265123, ECO:0000269|PubMed:9705290}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9671805, ECO:0000269|PubMed:9705290}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;bladder;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;aorta;stomach;thymus; occipital lobe;superior cervical ganglion;pons;atrioventricular node;skeletal muscle;uterus;subthalamic nucleus;prostate;thyroid;globus pallidus;ciliary ganglion;trigeminal ganglion;whole blood;parietal lobe;cingulate cortex; 0.11014 0.08981 0.609894095 82.95588582 1129.28257 6.41308 LRRFIP1P1 . . . leucine rich repeat (in FLII) interacting protein 1 pseudogene 1 . . . . . . . . . . . LRRFIP2 4.80060455389411e-08 0.999981428944242 1.85230497121039e-05 leucine rich repeat (in FLII) interacting protein 2 FUNCTION: May function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta- catenin. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding. {ECO:0000269|PubMed:15677333, ECO:0000269|PubMed:19265123}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in heart and skeletal muscle. {ECO:0000269|PubMed:10366446}.; myocardium;smooth muscle;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;testis;dura mater;germinal center;brain;gall bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pia mater;lung;placenta;macula lutea;duodenum;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;parietal lobe;skeletal muscle; 0.12734 0.09642 -0.062423436 48.86765747 407.782 4.23386 LRRIQ1 6.84986559676448e-19 0.978762057942044 0.0212379420579561 leucine-rich repeats and IQ motif containing 1 . . . . . 0.09178 . 0.79541165 87.41448455 2235.96129 8.71864 LRRIQ3 3.22226837336838e-15 0.00517082541483622 0.994829174585161 leucine-rich repeats and IQ motif containing 3 . . . unclassifiable (Anatomical System);lung;testis; testis - interstitial;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06919 . 1.379742765 94.60368011 1020.69778 6.14814 LRRIQ4 0.00168554785571336 0.891546605635451 0.106767846508836 leucine-rich repeats and IQ motif containing 4 . . . unclassifiable (Anatomical System);lung;testis;colon;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; . 0.09875 0.334405942 73.64944562 1228.74002 6.62833 LRRK1 1.5909507477274e-05 0.999984068472531 2.20199917548977e-08 leucine-rich repeat kinase 1 . . . ovary;colon;fovea centralis;choroid;bone marrow;retina;optic nerve;larynx;thyroid;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;liver;alveolus;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13723 0.10871 -1.611828042 2.972399151 4789.19708 14.03707 LRRK2 7.5565041633134e-14 0.999999999739581 2.60343150694545e-10 leucine-rich repeat kinase 2 FUNCTION: Positively regulates autophagy through a calcium- dependent activation of the CaMKK/AMPK signaling pathway. The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes. Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner. Regulates neuronal process morphology in the intact central nervous system (CNS). Plays a role in synaptic vesicle trafficking. Phosphorylates PRDX3. Has GTPase activity. May play a role in the phosphorylation of proteins central to Parkinson disease. {ECO:0000269|PubMed:17114044, ECO:0000269|PubMed:18230735, ECO:0000269|PubMed:20949042, ECO:0000269|PubMed:21850687, ECO:0000269|PubMed:22012985, ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:24687852}.; DISEASE: Parkinson disease 8 (PARK8) [MIM:607060]: A slowly progressive neurodegenerative disorder characterized by bradykinesia, rigidity, resting tremor, postural instability, neuronal loss in the substantia nigra, and the presence of neurofibrillary MAPT (tau)-positive and Lewy bodies in some patients. {ECO:0000269|PubMed:15541308, ECO:0000269|PubMed:15541309, ECO:0000269|PubMed:15680455, ECO:0000269|PubMed:15680456, ECO:0000269|PubMed:15680457, ECO:0000269|PubMed:15726496, ECO:0000269|PubMed:15732108, ECO:0000269|PubMed:15811454, ECO:0000269|PubMed:15852371, ECO:0000269|PubMed:15880653, ECO:0000269|PubMed:15925109, ECO:0000269|PubMed:15929036, ECO:0000269|PubMed:16102999, ECO:0000269|PubMed:16157901, ECO:0000269|PubMed:16157908, ECO:0000269|PubMed:16157909, ECO:0000269|PubMed:16172858, ECO:0000269|PubMed:16240353, ECO:0000269|PubMed:16247070, ECO:0000269|PubMed:16250030, ECO:0000269|PubMed:16251215, ECO:0000269|PubMed:16272164, ECO:0000269|PubMed:16272257, ECO:0000269|PubMed:16298482, ECO:0000269|PubMed:16333314, ECO:0000269|PubMed:16533964, ECO:0000269|PubMed:18213618, ECO:0000269|PubMed:22956510}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the brain. Expressed in pyramidal neurons in all cortical laminae of the visual cortex, in neurons of the substantia nigra pars compacta and caudate putamen (at protein level). Expressed throughout the adult brain, but at a lower level than in heart and liver. Also expressed in placenta, lung, skeletal muscle, kidney and pancreas. In the brain, expressed in the cerebellum, cerebral cortex, medulla, spinal cord occipital pole, frontal lobe, temporal lobe and putamen. Expression is particularly high in brain dopaminoceptive areas. {ECO:0000269|PubMed:15541308, ECO:0000269|PubMed:15541309, ECO:0000269|PubMed:16532471, ECO:0000269|PubMed:17120249}.; unclassifiable (Anatomical System);breast;prostate;lung;cartilage;endometrium;larynx;bone;thyroid;hypopharynx;testis;blood;head and neck;kidney;germinal center;bone marrow; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle; 0.12213 . -1.128353123 6.510969568 3435.33983 11.24894 LRRN1 0.876589036506927 0.123092110241899 0.000318853251174102 leucine rich repeat neuronal 1 . . . unclassifiable (Anatomical System);heart;blood;choroid;lens;skeletal muscle;retina;bone marrow;prostate;whole body;lung;cochlea;larynx;bone;visual apparatus;iris;alveolus;testis;head and neck;spleen;kidney;brain; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.60918 0.11247 -0.595174814 18.21184242 256.23286 3.44332 LRRN2 0.220781250034657 0.770968252338636 0.0082504976267069 leucine rich repeat neuronal 2 . . TISSUE SPECIFICITY: Overamplified in malignant gliomas.; . . 0.10941 0.10476 -0.282886048 33.53385232 3908.91818 12.35946 LRRN3 0.686452349711702 0.31265993755316 0.000887712735138776 leucine rich repeat neuronal 3 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;testis;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;kidney; superior cervical ganglion;occipital lobe;medulla oblongata;fetal brain;ciliary ganglion;pons;trigeminal ganglion;cingulate cortex;parietal lobe; 0.40405 . -0.334253673 30.70299599 295.32285 3.66838 LRRN4 1.45171418519099e-08 0.11257051035762 0.887429475125238 leucine rich repeat neuronal 4 FUNCTION: May play an important role in hippocampus-dependent long-lasting memory. {ECO:0000250}.; . . . . 0.07746 0.09642 . . 3735.11945 11.94414 LRRN4CL 5.4372145884e-05 0.260644868929443 0.739300758924673 LRRN4 C-terminal like . . . unclassifiable (Anatomical System);pancreas;ovary;placenta;parathyroid;skin; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.14133 . . . 14.06155 0.51050 LRRTM1 0.951075572630596 0.0487773951782399 0.000147032191164654 leucine rich repeat transmembrane neuronal 1 FUNCTION: Exhibits strong synaptogenic activity, restricted to excitatory presynaptic differentiation, acting at both pre- and postsynaptic level. {ECO:0000250}.; . TISSUE SPECIFICITY: Predominantly expressed in forebrain regions including thalamus and cerebral cortex. {ECO:0000269|PubMed:12676565, ECO:0000269|PubMed:17667961}.; unclassifiable (Anatomical System);lung;frontal lobe;islets of Langerhans;hypothalamus;hippocampus;kidney;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus; 0.59691 0.11049 0.110306132 62.00165133 3435.77977 11.25190 LRRTM2 0.923558761887084 0.0763488143072367 9.24238056791379e-05 leucine rich repeat transmembrane neuronal 2 FUNCTION: Involved in the development and maintenance of excitatory synapse in the vertebrate nervous system. Regulates surface expression of AMPA receptors and instructs the development of functional glutamate release sites. Acts as a ligand for the presynaptic receptors NRXN1-A and NRXN1-B (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in neuronal tissues. {ECO:0000269|PubMed:12676565}.; unclassifiable (Anatomical System);lung;cartilage;visual apparatus;brain; amygdala;thalamus;occipital lobe;subthalamic nucleus;medulla oblongata;fetal brain;temporal lobe;prefrontal cortex;globus pallidus;pons;caudate nucleus;cingulate cortex;parietal lobe; 0.81720 0.11809 -0.60427181 17.74593064 13.54722 0.49181 LRRTM3 0.852645121301407 0.147250999715669 0.00010387898292459 leucine rich repeat transmembrane neuronal 3 FUNCTION: Exhibits a limited synaptogenic activity in vitro, restricted to excitatory presynaptic differentiation (By similarity). May play a role in the development and maintenance of the vertebrate nervous system. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in neuronal tissues. {ECO:0000269|PubMed:12676565}.; unclassifiable (Anatomical System);lung;islets of Langerhans;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.81417 0.11809 -0.271755481 34.31823543 262.06908 3.47385 LRRTM4 0.748069164341842 0.251469228727673 0.000461606930484901 leucine rich repeat transmembrane neuronal 4 FUNCTION: May play a role in the development and maintenance of the vertebrate nervous system. Exhibits strong synaptogenic activity, restricted to excitatory presynaptic differentiation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in neuronal tissues. {ECO:0000269|PubMed:12676565}.; . . 0.25599 0.10455 -0.271755481 34.31823543 38.18067 1.13355 LRSAM1 2.92723845718058e-05 0.99983709750114 0.000133630114287764 leucine rich repeat and sterile alpha motif containing 1 FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivate the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos (PubMed:15256501). Bacterial recognition protein that defends the cytoplasm from invasive pathogens (PubMed:23245322). Localizes to several intracellular bacterial pathogens and generates the bacteria- associated ubiquitin signal leading to autophagy-mediated intracellular bacteria degradation (xenophagy) (PubMed:23245322, PubMed:25484098). {ECO:0000269|PubMed:15256501, ECO:0000269|PubMed:23245322, ECO:0000269|PubMed:25484098}.; DISEASE: Charcot-Marie-Tooth disease 2P (CMT2P) [MIM:614436]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. {ECO:0000269|PubMed:20865121, ECO:0000269|PubMed:22012984}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in adult spinal cord motoneurons as well as in fetal spinal cord and muscle tissue. {ECO:0000269|PubMed:22012984}.; ovary;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;hypopharynx;spleen;head and neck;cervix;kidney;stomach;cerebellum;thymus; superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion; 0.38608 0.14307 -0.43902969 24.63434772 170.33172 2.84816 LRTM1 5.24712732718947e-09 0.0631776517246063 0.936822343028266 leucine-rich repeats and transmembrane domains 1 . . . unclassifiable (Anatomical System);heart;ovary;hypothalamus;pineal body;parathyroid;fovea centralis;skin;retina;uterus;pancreas;optic nerve;whole body;lung;placenta;macula lutea;visual apparatus;testis;pineal gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.29035 0.07711 0.819433854 87.98655343 203.32786 3.07743 LRTM2 0.739704570731645 0.257831521862328 0.00246390740602646 leucine-rich repeats and transmembrane domains 2 . . . unclassifiable (Anatomical System);optic nerve;macula lutea;fovea centralis;choroid;lens;brain;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.23348 0.11888 -0.534490515 20.70063694 213.67347 3.15433 LRTOMT 0.0145642639198667 0.447671833375687 0.537763902704447 leucine rich transmembrane and O-methyltransferase domain containing FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones (By similarity). Required for auditory function. {ECO:0000250|UniProtKB:P21964, ECO:0000269|PubMed:18794526}.; DISEASE: Deafness, autosomal recessive, 63 (DFNB63) [MIM:611451]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:18794526, ECO:0000269|PubMed:18953341}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;prostate;whole body;endometrium;larynx;bone;pituitary gland;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;kidney;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;globus pallidus;testis;ciliary ganglion;trigeminal ganglion; 0.10458 0.08912 0.330767508 73.53739089 85.65099 1.97518 LRWD1 2.01862470800891e-07 0.676473534366345 0.323526263771184 leucine-rich repeats and WD repeat domain containing 1 FUNCTION: Required for G1/S transition. Recruits and stabilizes the origin recognition complex (ORC) onto chromatin during G1 to establish pre-replication complex (preRC) and to heterochromatic sites in post-replicated cells. Binds a combination of DNA and histone methylation repressive marks on heterochromatin. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K20me3 and H4K27me3 in a cooperative manner with DNA methylation. Required for silencing of major satellite repeats. May be important ORC2, ORC3 and ORC4 stability. {ECO:0000269|PubMed:20850016, ECO:0000269|PubMed:20932478, ECO:0000269|PubMed:21029866, ECO:0000269|PubMed:22427655, ECO:0000269|PubMed:22645314}.; . TISSUE SPECIFICITY: Testis-specific. Drastically down-regulated in testis from patients with Sertoli cell-only syndrome (SCOS). {ECO:0000269|PubMed:17074343}.; medulla oblongata;ovary;colon;parathyroid;skin;uterus;prostate;oesophagus;endometrium;larynx;bone;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.13356 . 0.029399861 55.83274357 376.20765 4.08914 LSAMP 0.946283746572624 0.0536784145861162 3.78388412601314e-05 limbic system-associated membrane protein FUNCTION: Mediates selective neuronal growth and axon targeting. Contributes to the guidance of developing axons and remodeling of mature circuits in the limbic system. Essential for normal growth of the hyppocampal mossy fiber projection (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed on limbic neurons and fiber tracts as well as in single layers of the superior colliculus, spinal chord and cerebellum.; unclassifiable (Anatomical System);prostate;lung;cartilage;kidney;germinal center;lens;brain; superior cervical ganglion;temporal lobe;atrioventricular node;parietal lobe;cingulate cortex; 0.72117 0.19389 0.03689118 56.64071715 22.84835 0.76216 LSAMP-AS1 . . . LSAMP antisense RNA 1 . . . . . . . . . . . LSG1 6.58805364159815e-07 0.99381320467475 0.00618613651988567 large 60S subunit nuclear export GTPase 1 FUNCTION: GTPase required for the XPO1/CRM1-mediated nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm (Probable). {ECO:0000305|PubMed:16209721}.; . . smooth muscle;ovary;developmental;colon;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.13441 0.09745 0.428052693 77.31186601 477.81473 4.51281 LSINCT5 . . . long stress-induced non-coding transcript 5 . . . . . . . . . . . LSM1 0.931276896697764 0.0683780690368619 0.000345034265374014 LSM1 homolog, mRNA degradation associated FUNCTION: Plays a role in replication-dependent histone mRNA degradation. Binds specifically to the 3'-terminal U-tract of U6 snRNA. {ECO:0000269|PubMed:18172165}.; . TISSUE SPECIFICITY: Has elevated expression in pancreatic cancer and in several cancer-derived cell lines.; ovary;skin;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;nasopharynx;placenta;kidney;stomach;aorta; testis; 0.57135 0.13167 -0.053113545 49.38664779 3.53481 0.12937 LSM1P1 . . . LSM1 homolog, mRNA degradation associated pseudogene 1 . . . . . . . . . . . LSM1P2 . . . LSM1 homolog, mRNA degradation associated pseudogene 2 . . . . . . . . . . . LSM2 0.00596281731563641 0.73153138807898 0.262505794605384 LSM2 homolog, U6 small nuclear RNA and mRNA degradation associated FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA. May be involved in pre-mRNA splicing.; . . . . 0.49562 0.11809 0.189398298 66.31870724 . . LSM3 2.76631880023763e-05 0.324886903875069 0.675085432936928 LSM3 homolog, U6 small nuclear RNA and mRNA degradation associated FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA.; . . smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;germinal center;bladder;brain;heart;tongue;pineal body;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;vein;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;testis;pons;trigeminal ganglion;skeletal muscle; 0.13984 0.15588 -0.163345027 41.24793583 5.40745 0.19971 LSM3P1 . . . LSM3 homolog, U6 small nuclear RNA and mRNA degradation associated pseudogene 1 . . . . . . . . . . . LSM3P2 . . . LSM3 homolog, U6 small nuclear RNA and mRNA degradation associated pseudogene 2 . . . . . . . . . . . LSM3P3 . . . LSM3 homolog, U6 small nuclear RNA and mRNA degradation associated pseudogene 3 . . . . . . . . . . . LSM3P4 . . . LSM3 homolog, U6 small nuclear RNA and mRNA degradation associated pseudogene 4 . . . . . . . . . . . LSM3P5 . . . LSM3 homolog, U6 small nuclear RNA and mRNA degradation associated pseudogene 5 . . . . . . . . . . . LSM4 0.667371394425323 0.327513454136059 0.00511515143861798 LSM4 homolog, U6 small nuclear RNA and mRNA degradation associated FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach; whole brain;testis - interstitial;testis - seminiferous tubule;heart;testis;tumor; 0.32735 0.16306 -0.251530012 35.42108988 43.5254 1.25576 LSM5 0.0182319329650146 0.725921529317359 0.255846537717627 LSM5 homolog, U6 small nuclear RNA and mRNA degradation associated FUNCTION: Plays a role in U6 snRNP assembly and function. Binds to the 3' end of U6 snRNA, thereby facilitating formation of the spliceosomal U4/U6 duplex formation in vitro.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;oral cavity;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;cornea;placenta;macula lutea;visual apparatus;hypopharynx;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;tumor; 0.68416 0.11388 -0.031067188 51.03798066 5.18241 0.19274 LSM6 0.868075946393215 0.13009543766706 0.00182861593972542 LSM6 homolog, U6 small nuclear RNA and mRNA degradation associated FUNCTION: Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;whole body;lung;placenta;macula lutea;germinal center;kidney;brain;aorta;stomach; superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.90590 0.12378 0.101211609 60.95777306 6.02806 0.22746 LSM6P1 . . . LSM6 homolog, U6 small nuclear RNA and mRNA degradation associated pseudogene 1 . . . . . . . . . . . LSM6P2 . . . LSM6 homolog, U6 small nuclear RNA and mRNA degradation associated pseudogene 2 . . . . . . . . . . . LSM7 0.281731306604913 0.631076759930723 0.0871919334643641 LSM7 homolog, U6 small nuclear RNA and mRNA degradation associated FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA and is probably a component of the spliceosome.; . . medulla oblongata;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney; . 0.58063 . -0.031067188 51.03798066 . . LSM8 . . . LSM8 homolog, U6 small nuclear RNA associated FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA and is probably a component of the spliceosome.; . . . . 0.15013 0.12971 . . . . LSM10 0.615647823094396 0.350799189517227 0.0335529873883773 LSM10, U7 small nuclear RNA associated FUNCTION: Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing. Increases U7 snRNA levels but not histone 3'-end pre-mRNA processing activity, when overexpressed. Required for cell cycle progression from G1 to S phases. Binds specifically to U7 snRNA. Binds to the downstream cleavage product (DCP) of histone pre-mRNA in a U7 snRNP dependent manner. {ECO:0000269|PubMed:16914750}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;substantia nigra;parathyroid;choroid;skin;uterus;prostate;whole body;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;alveolus;liver;spleen;kidney; subthalamic nucleus;globus pallidus;atrioventricular node;skeletal muscle; 0.13326 0.10470 -0.031067188 51.03798066 28.38632 0.90884 LSM11 0.490844531335381 0.504545912788866 0.00460955587575254 LSM11, U7 small nuclear RNA associated FUNCTION: Component of the U7 snRNP complex that is involved in the histone 3'-end pre-mRNA processing (By similarity). Increases U7 snRNA levels but not histone 3'-end pre-mRNA processing activity, when overexpressed. Required for cell cycle progression from G1 to S phases. Binds specifically to the Sm-binding site of U7 snRNA. {ECO:0000250, ECO:0000269|PubMed:16914750}.; . . unclassifiable (Anatomical System);heart;ovary;colon;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;whole body;lung;placenta;macula lutea;testis;cervix;kidney;brain;mammary gland;bladder; testis - interstitial;testis;ciliary ganglion; 0.27857 0.11337 . . 113.73492 2.32367 LSM12 0.931681763448656 0.0679783074164928 0.000339929134850695 LSM12 homolog . . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;breast;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; . 0.44390 0.11262 0.169169615 65.33380514 36.37283 1.09024 LSM12P1 . . . LSM12 pseudogene 1 . . . . . . . . . . . LSM14A 0.383919740881151 0.615644169109221 0.000436090009627068 LSM14A mRNA processing body assembly factor FUNCTION: Essential for formation of P-bodies, cytoplasmic structures that provide storage sites for non-translating mRNAs. {ECO:0000269|PubMed:16484376, ECO:0000269|PubMed:17074753}.; . . . . 0.86899 0.12033 0.260991686 70.25831564 1032.62687 6.17382 LSM14B 0.967227480386856 0.0327615052838319 1.10143293117998e-05 LSM family member 14B FUNCTION: May play a role in control of mRNA translation. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;blood;retina;bone marrow;breast;prostate;whole body;optic nerve;lung;frontal lobe;placenta;pituitary gland;liver;testis;cervix;germinal center;kidney;mammary gland;brain;stomach;cerebellum; testis - interstitial;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;cerebellum; 0.13993 0.11141 -0.337894035 30.37272942 15.40523 0.55291 LSMEM1 0.00519486074970192 0.703689832596362 0.291115306653936 leucine-rich single-pass membrane protein 1 . . . . . 0.12705 . -0.053113545 49.38664779 9.36422 0.34438 LSMEM2 2.89143693080036e-05 0.332018829125268 0.667952256505424 leucine-rich single-pass membrane protein 2 . . . . . 0.38645 . -0.582225231 18.44184949 14.36223 0.51850 LSP1 0.259641696484575 0.73454814126425 0.00581016225117558 lymphocyte-specific protein 1 FUNCTION: May play a role in mediating neutrophil activation and chemotaxis. {ECO:0000250}.; . TISSUE SPECIFICITY: Activated T-lymphocytes.; lymphoreticular;myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;synovium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;lens;pancreas;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; lymph node;adrenal gland;adrenal cortex;white blood cells;whole blood;tonsil;thymus;bone marrow; 0.38605 . -0.044015879 50.44821892 246.58964 3.38823 LSP1P1 . . . lymphocyte-specific protein 1 pseudogene 1 . . . . . . . . . . . LSP1P2 . . . lymphocyte-specific protein 1 pseudogene 2 . . . . . . . . . . . LSP1P3 . . . lymphocyte-specific protein 1 pseudogene 3 . . . . . . . . . . . LSR 5.33569632293939e-08 0.629221238401226 0.37077870824181 lipolysis stimulated lipoprotein receptor FUNCTION: Probable role in the clearance of triglyceride-rich lipoprotein from blood. Binds chylomicrons, LDL and VLDL in presence of free fatty acids and allows their subsequent uptake in the cells (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;testis;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;heart;cartilage;islets of Langerhans;pharynx;blood;breast;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach; pancreas;prostate;lung;thyroid;placenta;liver; 0.60464 0.19878 -0.861560326 10.89289927 1011.48417 6.12442 LSS 0.000604838176127229 0.999353008248717 4.21535751560353e-05 lanosterol synthase (2,3-oxidosqualene-lanosterol cyclase) FUNCTION: Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus. {ECO:0000269|PubMed:7639730}.; . . unclassifiable (Anatomical System);lymph node;salivary gland;muscle;colon;lens;skeletal muscle;uterus;pancreas;prostate;lung;frontal lobe;placenta;visual apparatus;iris;liver;testis;spleen;brain;mammary gland;stomach; atrioventricular node; 0.09964 0.38626 0.540106923 81.09813635 1845.09003 7.92325 LST1 0.00253791495629015 0.550237863020987 0.447224222022723 leukocyte specific transcript 1 FUNCTION: Possible role in modulating immune responses. Induces morphological changes including production of filopodia and microspikes when overexpressed in a variety of cell types and may be involved in dendritic cell maturation. Isoform 1 and isoform 2 have an inhibitory effect on lymphocyte proliferation. {ECO:0000269|PubMed:10706707, ECO:0000269|PubMed:11478849}.; . TISSUE SPECIFICITY: Expressed in lung, tonsil, thymus, placenta, kidney, fetal spleen, fetal liver and brain. {ECO:0000269|PubMed:7590964, ECO:0000269|PubMed:9367684}.; unclassifiable (Anatomical System);cartilage;blood;parathyroid;bone marrow;uterus;pancreas;lung;placenta;testis;spleen;germinal center;kidney;brain; . 0.05318 . 0.013025609 54.62962963 345.6627 3.94413 LTA 0.743246562194033 0.245970562564895 0.0107828752410728 lymphotoxin alpha FUNCTION: Cytokine that in its homotrimeric form binds to TNFRSF1A/TNFR1, TNFRSF1B/TNFBR and TNFRSF14/HVEM. In its heterotrimeric form with LTB binds to TNFRSF3/LTBR. Lymphotoxin is produced by lymphocytes and cytotoxic for a wide range of tumor cells in vitro and in vivo.; DISEASE: Psoriatic arthritis (PSORAS) [MIM:607507]: An inflammatory, seronegative arthritis associated with psoriasis. It is a heterogeneous disorder ranging from a mild, non-destructive disease to a severe, progressive, erosive arthropathy. Five types of psoriatic arthritis have been defined: asymmetrical oligoarthritis characterized by primary involvement of the small joints of the fingers or toes; asymmetrical arthritis which involves the joints of the extremities; symmetrical polyarthritis characterized by a rheumatoid like pattern that can involve hands, wrists, ankles, and feet; arthritis mutilans, which is a rare but deforming and destructive condition; arthritis of the sacroiliac joints and spine (psoriatic spondylitis). {ECO:0000269|PubMed:12746914}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . . . 0.31616 . 0.525552348 80.57914603 4898.85973 14.25628 LTA4H 0.0494218192368297 0.950538206054696 3.99747084739619e-05 leukotriene A4 hydrolase FUNCTION: Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity. {ECO:0000269|PubMed:11917124, ECO:0000269|PubMed:12207002, ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:18804029, ECO:0000269|PubMed:1897988, ECO:0000269|PubMed:1975494, ECO:0000269|PubMed:2244921}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in monocytes, lymphocytes, neutrophils, reticulocytes, platelets and fibroblasts.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; lung;white blood cells;whole blood;bone marrow; 0.12042 0.20759 0.018483465 55.44939844 125.21901 2.43544 LTB 1.00562999342202e-05 0.192574725131991 0.807415218568075 lymphotoxin beta FUNCTION: Cytokine that binds to LTBR/TNFRSF3. May play a specific role in immune response regulation. Provides the membrane anchor for the attachment of the heterotrimeric complex to the cell surface. Isoform 2 is probably non-functional.; . TISSUE SPECIFICITY: Spleen and thymus.; . . 0.12915 . 0.369407109 74.95281906 118.13154 2.36367 LTB4R 0.677367973216978 0.302277046344606 0.0203549804384166 leukotriene B4 receptor FUNCTION: Receptor for extracellular ATP > UTP and ADP. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. May be the cardiac P2Y receptor involved in the regulation of cardiac muscle contraction through modulation of L-type calcium currents. Is a receptor for leukotriene B4, a potent chemoattractant involved in inflammation and immune response.; . TISSUE SPECIFICITY: Expressed at highest levels in heart, skeletal muscle and at lower levels in brain and liver. High level of expression in lymphoid tissues.; unclassifiable (Anatomical System);colon;blood;skin;retina;bone marrow;uterus;breast;lung;endometrium;thyroid;placenta;visual apparatus;testis;spleen;germinal center;kidney;brain;thymus; dorsal root ganglion;superior cervical ganglion;pons;trigeminal ganglion;cingulate cortex; 0.07534 0.09292 . . 66.79353 1.68683 LTB4R2 0.000267452650893406 0.545701473706859 0.454031073642247 leukotriene B4 receptor 2 FUNCTION: Low-affinity receptor for leukotrienes including leukotriene B4. Mediates chemotaxis of granulocytes and macrophages. The response is mediated via G-proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinities for the leukotrienes is LTB4 > 12-epi-LTB4 > LTB5 > LTB3.; . TISSUE SPECIFICITY: Widely expressed.; . . 0.16549 . 0.306902668 72.38145789 455.72449 4.43567 LTBP1 0.526234698119928 0.473765301863216 1.68559199616837e-11 latent transforming growth factor beta binding protein 1 FUNCTION: May be involved in the assembly, secretion and targeting of TGFB1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGFB1. May have a structural role in the extra cellular matrix (ECM).; . TISSUE SPECIFICITY: Isoform Long is found in fibroblasts.; myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;amygdala;heart;cartilage;pineal body;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);pancreas;lung;cornea;nasopharynx;placenta;duodenum;amnion;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;placenta;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.47380 0.14744 -0.44293645 24.46921444 877.89035 5.77162 LTBP2 0.0187346880945461 0.981265309490244 2.41520997363342e-09 latent transforming growth factor beta binding protein 2 FUNCTION: May play an integral structural role in elastic-fiber architectural organization and/or assembly.; DISEASE: Glaucoma 3, primary congenital, D (GLC3D) [MIM:613086]: An autosomal recessive form of primary congenital glaucoma (PCG). PCG is characterized by marked increase of intraocular pressure at birth or early childhood, large ocular globes (buphthalmos) and corneal edema. It results from developmental defects of the trabecular meshwork and anterior chamber angle of the eye that prevent adequate drainage of aqueous humor. {ECO:0000269|PubMed:19361779}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Microspherophakia and/or megalocornea, with ectopia lentis and with or without secondary glaucoma (MSPKA) [MIM:251750]: A rare disease characterized by smaller and more spherical lenses than normal bilaterally, an increased anteroposterior thickness of the lens, and highly myopic eyes. Lens dislocation or subluxation may occur, leading to defective accommodation. {ECO:0000269|PubMed:20617341}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Weill-Marchesani syndrome 3 (WMS3) [MIM:614819]: A rare connective tissue disorder characterized by short stature, brachydactyly, joint stiffness, and eye abnormalities including microspherophakia, ectopia lentis, severe myopia and glaucoma. {ECO:0000269|PubMed:22539340}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in lung, weakly expressed in heart, placenta, liver and skeletal muscle.; myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;thyroid;iris;testis;dura mater;spinal ganglion;brain;artery;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;spinal cord;lens;skeletal muscle;breast;pancreas;pia mater;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;aorta; dorsal root ganglion;superior cervical ganglion;smooth muscle;adipose tissue;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.34261 0.09147 -1.545648077 3.290870488 1221.56268 6.60795 LTBP3 0.996034358631329 0.00396564126533668 1.03334363835292e-10 latent transforming growth factor beta binding protein 3 FUNCTION: May be involved in the assembly, secretion and targeting of TGFB1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGFB1. May have a structural role in the extra cellular matrix (ECM).; DISEASE: Dental anomalies and short stature (DASS) [MIM:601216]: A disorder characterized by hypoplastic amelogenesis imperfecta, significant short stature, brachyolmia-like anomalies including platyspondyly with short pedicles, narrow intervertebral and interpedicular distances, rectangular-shaped vertebrae with posterior scalloping and herniation of the nuclei, and broad femoral necks. Dental anomalies include widely spaced, small, yellow teeth, oligodontia, and severely reduced to absent enamel. {ECO:0000269|PubMed:19344874}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 2 is expressed prominently in heart, skeletal muscle, prostate, testis, small intestine and ovary. Isoform 1 is strongly expressed in pancreas and liver.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;aorta;thymus; thyroid; 0.30397 0.12827 -0.93133804 9.613116301 914.10791 5.87861 LTBP4 0.99035873643018 0.00964126356829907 1.52042927724578e-12 latent transforming growth factor beta binding protein 4 FUNCTION: May be involved in the assembly, secretion and targeting of TGFB1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGFB1. May have a structural role in the extra cellular matrix (ECM) (By similarity). {ECO:0000250}.; DISEASE: Urban-Rifkin-Davis syndrome (URDS) [MIM:613177]: A syndrome characterized by disrupted pulmonary, gastrointestinal, urinary, musculoskeletal, craniofacial and dermal development. Clinical features include cutis laxa, mild cardiovascular lesions, respiratory distress with cystic and atelectatic changes in the lungs, and diverticulosis, tortuosity and stenosis at various levels of the intestinal tract. Craniofacial features include microretrognathia, flat midface, receding forehead and wide fontanelles. {ECO:0000269|PubMed:19836010}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, pancreas, uterus, and small intestine. Weakly expressed in placenta and lung. {ECO:0000269|PubMed:9271198, ECO:0000269|PubMed:9660815}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; uterus;superior cervical ganglion;thyroid; 0.19864 0.12290 . . 9734.18657 21.48310 LTBR 0.428683150276069 0.569793357010272 0.00152349271365942 lymphotoxin beta receptor FUNCTION: Receptor for the heterotrimeric lymphotoxin containing LTA and LTB, and for TNFS14/LIGHT. Promotes apoptosis via TRAF3 and TRAF5. May play a role in the development of lymphoid organs. {ECO:0000269|PubMed:10799510, ECO:0000269|PubMed:8171323}.; . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cerebral cortex;endometrium;bone;thyroid;iris;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion; 0.34022 0.53070 0.262810045 70.43524416 202.08421 3.06752 LTC4S 0.00216910624326774 0.516817692250853 0.48101320150588 leukotriene C4 synthase FUNCTION: Catalyzes the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4.; . TISSUE SPECIFICITY: Detected in lung, platelets and the myelogenous leukemia cell line KG-1 (at protein level). LTC4S activity is present in eosinophils, basophils, mast cells, certain phagocytic mononuclear cells, endothelial cells, vascular smooth muscle cells and platelets. {ECO:0000269|PubMed:7599836}.; unclassifiable (Anatomical System);prostate;lung;ovary;hypothalamus;placenta;testis;parathyroid;kidney;brain; spinal cord;liver; 0.12488 0.10849 . . 37.01667 1.10654 LTF 1.76023213454946e-13 0.332110461363874 0.66788953863595 lactotransferrin FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.; FUNCTION: Lactoferricin binds to the bacterial surface and is crucial for the bactericidal functions. Has some antiviral activity against papillomavirus infection. N-terminal region shows strong antifungal activity against C.albicans. Contains two BBXB heparin-binding consensus sequences that appear to form the predominate functional GAG-binding site.; FUNCTION: Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors.; FUNCTION: Isoform DeltaLf: transcription factor with antiproliferative properties and ability to induce cell cycle arrest. Binds to the DeltaLf response element found in the SKP1, BAX, DCPS, and SELH promoters.; . TISSUE SPECIFICITY: High levels are found in saliva and tears, intermediate levels in serum and plasma, and low levels in urine. In kidney, detected in the distal collecting tubules in the medulla but not in the cortical region or in blood vessels. Detected in peripheral blood neutrophils (at protein level). Isoform 1 and isoform DeltaLf are expressed in breast, prostate, spleen, pancreas, kidney, small intestine, lung, skeletal muscle, uterus, thymus and fetal liver. Isoform 1 is expressed in brain, testis and peripheral blood leukocytes; isoform DeltaLf is barely detectable in these tissues. Isoform DeltaLf is expressed in placenta, liver and ovary; isoform 1 is barely detectable in these tissues. In kidney, isoform 1 is expressed at high levels in the collecting tubules of the medulla but at very low levels in the cortex. {ECO:0000269|PubMed:10792619, ECO:0000269|PubMed:2981589, ECO:0000269|PubMed:9122171}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;brain;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;lacrimal gland;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;trachea;adrenal gland;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach; prostate;trachea;salivary gland;fetal lung;tonsil;bone marrow;thymus; . 0.31989 0.521707177 80.39631989 121.1482 2.39786 LTK 4.12009149040216e-21 0.00122792693410976 0.99877207306589 leukocyte receptor tyrosine kinase FUNCTION: Orphan receptor with a tyrosine-protein kinase activity. The exact function of this protein is not known. Studies with chimeric proteins (replacing its extracellular region with that of several known growth factor receptors, such as EGFR and CSFIR) demonstrate its ability to promote growth and specifically neurite outgrowth, and cell survival. Signaling appears to involve the PI3 kinase pathway. Involved in regulation of the secretory pathway involving endoplasmic reticulum (ER) export sites (ERESs) and ER to Golgi transport. {ECO:0000269|PubMed:20548102}.; . TISSUE SPECIFICITY: Expressed in non-hematopoietic cell lines and T- and B-cell lines. {ECO:0000269|PubMed:2156206}.; unclassifiable (Anatomical System);placenta;testis;blood;brain;retina; superior cervical ganglion;temporal lobe;ciliary ganglion;trigeminal ganglion;parietal lobe;skeletal muscle; 0.28182 . -0.769738365 13.16348195 944.3624 5.95493 LTN1 0.832714009845553 0.167285990137576 1.68709061566157e-11 listerin E3 ubiquitin protein ligase 1 FUNCTION: E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation (PubMed:23685075, PubMed:25132172, PubMed:25578875). Ubiquitination leads to VCP/p97 recruitment for extraction and degradation of the incomplete translation product (By similarity). {ECO:0000250|UniProtKB:Q04781, ECO:0000269|PubMed:23685075, ECO:0000269|PubMed:25132172, ECO:0000269|PubMed:25578875}.; . . medulla oblongata;umbilical cord;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;oesophagus;endometrium;larynx;testis;dura mater;germinal center;brain;artery;unclassifiable (Anatomical System);meninges;lymph node;heart;blood;skeletal muscle;greater omentum;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;head and neck;cervix;mammary gland;aorta;stomach; amygdala;superior cervical ganglion;occipital lobe;prefrontal cortex; 0.63029 0.09925 0.26079244 70.06369427 4364.96083 13.18197 LTV1 2.0508487464442e-05 0.974711128945768 0.0252683625667674 LTV1 ribosome biogenesis factor . . . . . 0.08359 0.09554 0.174625237 65.9648502 94.30361 2.09042 LTV1P1 . . . LTV1 ribosome biogenesis factor pseudogene 1 . . . . . . . . . . . LUADT1 . . . lung adenocarcinoma associated transcript 1 . . . . . . . . . . . LUC7L 0.164212796735953 0.83515936276741 0.000627840496636879 LUC7-like FUNCTION: May bind to RNA via its Arg/Ser-rich domain. {ECO:0000269|PubMed:11170747}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11170747}.; smooth muscle;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;hippocampus;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach; skeletal muscle; 0.53946 0.08557 0.040529541 57.15380986 47.06421 1.32691 LUC7L2 0.590287985521778 0.409694370505799 1.76439724227877e-05 LUC7-like 2 pre-mRNA splicing factor FUNCTION: May bind to RNA via its Arg/Ser-rich domain.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; dorsal root ganglion;superior cervical ganglion;thyroid;globus pallidus;pons;atrioventricular node;trigeminal ganglion; 0.44513 0.12065 0.148941568 64.31941496 190.27817 2.99390 LUC7L3 0.999974250781125 2.57492174531482e-05 1.42177381062829e-12 LUC7-like 3 pre-mRNA splicing factor FUNCTION: Binds cAMP regulatory element DNA sequence. May play a role in RNA splicing. {ECO:0000269|PubMed:16462885}.; . TISSUE SPECIFICITY: Widely expressed. Highest levels in heart, brain, pancreas, thymus, ovary, small intestine and peripheral blood leukocytes, as well as cerebellum, putamen and pituitary gland. Lowest levels in lung, liver and kidney. Also expressed in fetal tissues, including brain, heart, kidney, thymus and lung. {ECO:0000269|PubMed:10631324, ECO:0000269|PubMed:16462885}.; smooth muscle;ovary;sympathetic chain;substantia nigra;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;bone;pituitary gland;testis;dura mater;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;small intestine;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus; amygdala;superior cervical ganglion;subthalamic nucleus;occipital lobe;fetal brain;hypothalamus;spinal cord;prefrontal cortex;ciliary ganglion;skeletal muscle;parietal lobe;cingulate cortex; . . 0.016664174 55.21939137 41.0538 1.20300 LUC7L3P1 . . . LUC7-like 3 (S. cerevisiae) pseudogene 1 . . . . . . . . . . . LUCAT1 . . . lung cancer associated transcript 1 (non-protein coding) . . . . . . . . . . . LUM 0.101924740774409 0.77341593341443 0.12465932581116 lumican . . TISSUE SPECIFICITY: Cornea and other tissues.; myocardium;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;oesophagus;endometrium;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pancreas;lung;adrenal gland;placenta;visual apparatus;head and neck;kidney;mammary gland;stomach;aorta; uterus;uterus corpus;adipose tissue;olfactory bulb;ovary;placenta;appendix;fetal lung; 0.91425 0.29311 -0.05129383 49.75819769 36.05282 1.08311 LUNAR1 . . . leukemia-associated non-coding IGF1R activator RNA 1 . . . . . . . . . . . LURAP1 0.220934118593464 0.741964318346528 0.0371015630600084 leucine rich adaptor protein 1 FUNCTION: Acts as an activator of the canonical NF-kappa-B pathway and drive the production of proinflammatory cytokines. Promotes the antigen (Ag)-presenting and priming function of dendritic cells via the canonical NF-kappa-B pathway. In concert with MYO18A and CDC42BPA/CDC42BPB, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Activates CDC42BPA/CDC42BPB and targets it to actomyosin through its interaction with MYO18A, leading to MYL9/MLC2 phosphorylation and MYH9/MYH10-dependent actomyosin assembly in the lamella (By similarity). {ECO:0000250, ECO:0000269|PubMed:21048106}.; . . . . 0.20888 0.09526 0.483275131 79.25218212 189.23811 2.98683 LURAP1L 0.0766242694095508 0.749455038154983 0.173920692435466 leucine rich adaptor protein 1-like . . . . . 0.41470 . 0.305084559 72.22811984 133.01171 2.50722 LURAP1L-AS1 . . . LURAP1L antisense RNA 1 . . . . . . . . . . . LUZP1 0.287846256098982 0.712115254035043 3.8489865975496e-05 leucine zipper protein 1 . . . unclassifiable (Anatomical System);cartilage;ovary;adrenal cortex;colon;parathyroid;skeletal muscle;breast;uterus;pancreas;lung;frontal lobe;adrenal gland;larynx;bone;placenta;thyroid;alveolus;testis;amniotic fluid;head and neck;brain;pineal gland;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13523 . 0.34168906 73.72611465 889.12538 5.80869 LUZP2 8.71328292536607e-05 0.930798048343265 0.0691148188274816 leucine zipper protein 2 . . . prostate;frontal lobe;macula lutea;fovea centralis;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;medulla oblongata;cerebellum peduncles;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;cerebellum; 0.55855 0.10829 0.440999548 77.79547063 2728.40535 9.84471 LUZP4 0.00022131712724778 0.505421805255045 0.494356877617707 leucine zipper protein 4 FUNCTION: Export adapter involved in mRNA nuclear export. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway). Binds NXF1, enhances its RNA-binding activity and is required for its localization to the nuclear rim. Associates with the TREX complex via its interaction with the TREX components THOC1, THOC5 and DDX39B/UAP56. Capable of complementing knockdown of ALYREF/THOC4 and partially complementing a double ALYREF/UIF knockdown in vivo. Required for the growth of the melanoma cell line MeWo (PubMed:25662211). {ECO:0000269|PubMed:25662211}.; . TISSUE SPECIFICITY: Expressed specifically in testis. Also expressed in a wide variety of cancer types, but particularly high levels of expression observed in melanoma cells. {ECO:0000269|PubMed:12032826, ECO:0000269|PubMed:25662211}.; . . 0.01634 0.04632 0.483275131 79.25218212 19.40911 0.66765 LUZP4P1 . . . leucine zipper protein 4 pseudogene 1 . . . . . . . . . . . LUZP6 . . . leucine zipper protein 6 . . TISSUE SPECIFICITY: Widely expressed, highest levels found in brain, placenta, spleen, testis, and ovary. Up-regulated in some tumor cells. {ECO:0000269|PubMed:16982933}.; . . . . . . 42.26254 1.23004 LVRN . . . laeverin FUNCTION: Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo- maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met- MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C. {ECO:0000269|PubMed:17525158}.; . TISSUE SPECIFICITY: Specifically expressed in placenta and not in other tissues. Mainly found at the cell surface region of the extravillous trophoblasts. Detected on extravillous trophoblasts in the outer layer of the chorion laeve in the fetal membrane Not detected on either fetal amnionic epithelial cells or maternal decidual cells. Also detected in the migrating extravillous trophoblasts in the maternal decidual tissues (at protein level). {ECO:0000269|PubMed:14706636}.; . . . . 1.36500134 94.4621373 . . LXN 0.00362044465677788 0.842846800720104 0.153532754623118 latexin FUNCTION: Hardly reversible, non-competitive, and potent inhibitor of CPA1, CPA2 and CPA4. May play a role in inflammation. {ECO:0000269|PubMed:15738388}.; . TISSUE SPECIFICITY: Highly expressed in heart, prostate, ovary, kidney, pancreas, and colon, moderate or low in other tissues including brain. {ECO:0000269|PubMed:11455960}.; ovary;salivary gland;intestine;colon;parathyroid;vein;skin;uterus;prostate;whole body;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; uterus corpus; 0.21240 0.17288 1.260404852 93.53031375 356.73015 3.99954 LY6D 0.000620135417616238 0.289805615410092 0.709574249172291 lymphocyte antigen 6 complex, locus D FUNCTION: May act as a specification marker at earliest stage specification of lymphocytes between B- and T-cell development. Marks the earliest stage of B-cell specification.; . TISSUE SPECIFICITY: Expressed exclusively at the outer cell surface of transitional epithelia and the keratinocyte of stratified squamous epithelia.; unclassifiable (Anatomical System);heart;tongue;skin;uterus;pancreas;prostate;lung;oesophagus;larynx;placenta;head and neck;cervix;brain;stomach; tongue;adrenal cortex;ciliary ganglion;trigeminal ganglion;skeletal muscle;cingulate cortex;skin;tonsil; 0.07872 0.10450 0.3032669 72.009908 306.72203 3.72718 LY6E 0.733420181505572 0.254623225949824 0.0119565925446042 lymphocyte antigen 6 complex, locus E . . TISSUE SPECIFICITY: Widely expressed, predominantly in liver, kidney, ovary, spleen and peripheral blood Leukocytes.; lymphoreticular;ovary;salivary gland;intestine;colon;choroid;skin;retina;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; lung; 0.18673 0.18881 0.148941568 64.31941496 547.81646 4.76079 LY6G5B 0.000871193542460961 0.560217710209689 0.43891109624785 lymphocyte antigen 6 complex, locus G5B . . . . . . 0.20098 0.970138239 90.23354565 1091.25426 6.32264 LY6G5C 0.614670423249105 0.377208783878123 0.00812079287277211 lymphocyte antigen 6 complex, locus G5C FUNCTION: May have a role in hematopoietic cell differentiation.; . TISSUE SPECIFICITY: Detected in T-cell lines and fetal and adult lung. {ECO:0000269|PubMed:12079290}.; . . . . 0.501689326 79.7888653 . . LY6G6C 0.0016526950106923 0.460822655068755 0.537524649920553 lymphocyte antigen 6 complex, locus G6C . . TISSUE SPECIFICITY: Highly expressed at the leading edges of cells, on filopodia. {ECO:0000269|PubMed:17008713}.; . . 0.13290 0.09764 0.591694063 82.45458835 51.46381 1.41613 LY6G6D 0.542857604337903 0.442798608786499 0.0143437868755978 lymphocyte antigen 6 complex, locus G6D . . TISSUE SPECIFICITY: Expressed in the adult lung, and in fetal liver, lung, kidney, brain and spleen. {ECO:0000269|PubMed:12079290}.; . . . 0.08649 0.347360312 73.97381458 956.61953 5.98830 LY6G6E . . . lymphocyte antigen 6 complex, locus G6E (pseudogene) . . . . . 0.09001 . . . . . LY6G6F 2.55909344216693e-06 0.300839782461622 0.699157658444935 lymphocyte antigen 6 complex, locus G6F FUNCTION: May play a role in the downstream signal transduction pathways involving GRB2 and GRB7. {ECO:0000269|PubMed:12852788}.; . . . . . 0.08649 1.328368696 94.12597311 3009.43887 10.41637 LY6H 0.46060556878133 0.513360509673458 0.0260339215452121 lymphocyte antigen 6 complex, locus H . . TISSUE SPECIFICITY: Highly expressed in brain (cerebral cortex, amygdala, hippocampus and subthalamic nucleus) and in acute human leukemic cell line MOLT-3. Also found in lower levels in testis, pancreas, small intestine and colon.; unclassifiable (Anatomical System);lung;frontal lobe;ovary;hypothalamus;testis;colon;brain; whole brain;amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.15132 0.09479 -0.295622497 32.61972163 3.71295 0.13830 LY6K 0.000583632193494971 0.475674520846924 0.523741846959581 lymphocyte antigen 6 complex, locus K FUNCTION: May play a role in cell growth. {ECO:0000269|PubMed:18089789}.; . TISSUE SPECIFICITY: Specifically expressed in testis (at protein level). {ECO:0000269|PubMed:12516096, ECO:0000269|PubMed:18089789}.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;lung;cornea;larynx;bone;placenta;visual apparatus;liver;testis;cervix;head and neck;kidney;brain;mammary gland;bladder; . 0.08556 . . . 96.08332 2.11854 LY9 4.14080222823562e-10 0.327844132454945 0.672155867130974 lymphocyte antigen 9 FUNCTION: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. May participate in adhesion reactions between T lymphocytes and accessory cells by homophilic interaction. Promotes T-cell differentiation into a helper T-cell Th17 phenotype leading to increased IL-17 secretion; the costimulatory activity requires SH2D1A (PubMed:22184727). Promotes recruitment of RORC to the IL-17 promoter (PubMed:22989874). May be involved in the maintenance of peripheral cell tolerance by serving as a negative regulator of the immune response. May disable autoantibody responses and inhibit IFN-gamma secretion by CD4(+) T-cells. May negatively regulate the size of thymic innate CD8(+) T-cells and the development of invariant natural killer T (iNKT) cells (By similarity). {ECO:0000250|UniProtKB:Q01965, ECO:0000269|PubMed:22184727, ECO:0000269|PubMed:22989874}.; . TISSUE SPECIFICITY: Increased surface expression on T-cells of systemic lupus erythematosus (SLE) patients. {ECO:0000269|PubMed:22184727}.; unclassifiable (Anatomical System);pancreas;tongue;nasopharynx;liver;spleen;head and neck;germinal center;bone marrow; dorsal root ganglion;ciliary ganglion; 0.04720 . 0.113945049 62.14319415 137.03536 2.54536 LY75 3.63213139501385e-27 0.278342646040623 0.721657353959377 lymphocyte antigen 75 FUNCTION: Acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen- processing compartment (By similarity). Causes reduced proliferation of B-lymphocytes. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in spleen, thymus, colon and peripheral blood lymphocytes. Detected in myeloid and B-lymphoid cell lines. Isoform 2 and isoform 3 are expressed in malignant Hodgkin lymphoma cells called Hodgkin and Reed-Sternberg (HRS) cells. {ECO:0000269|PubMed:12824192, ECO:0000269|PubMed:9862343}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;lacrimal gland;colon;parathyroid;blood;skeletal muscle;bone marrow;breast;uterus;pancreas;lung;endometrium;nasopharynx;thyroid;placenta;alveolus;liver;testis;cervix;head and neck;germinal center;kidney; lymph node;thyroid;white blood cells;whole blood;tonsil;thymus; 0.08211 0.37130 3.821095209 99.62845011 5986.81997 16.12806 LY75-CD302 3.63213139501385e-27 0.278342646040623 0.721657353959377 LY75-CD302 readthrough FUNCTION: Acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen- processing compartment (By similarity). Causes reduced proliferation of B-lymphocytes. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in spleen, thymus, colon and peripheral blood lymphocytes. Detected in myeloid and B-lymphoid cell lines. Isoform 2 and isoform 3 are expressed in malignant Hodgkin lymphoma cells called Hodgkin and Reed-Sternberg (HRS) cells. {ECO:0000269|PubMed:12824192, ECO:0000269|PubMed:9862343}.; . . . . 4.067678684 99.66973343 . . LY86 9.98061892056217e-06 0.191795098358967 0.808194921022113 lymphocyte antigen 86 FUNCTION: May cooperate with CD180 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) and cytokine production. Important for efficient CD180 cell surface expression (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in B-cells, monocytes and tonsil.; unclassifiable (Anatomical System);lymph node;lung;islets of Langerhans;nasopharynx;placenta;alveolus;testis;colon;head and neck;germinal center;bone marrow; superior cervical ganglion;whole blood; 0.10086 0.16312 0.371224249 75.12384996 44.27632 1.26942 LY86-AS1 . . . LY86 antisense RNA 1 . . . . . . . . . . . LY96 2.41002321572206e-06 0.162303073630055 0.83769451634673 lymphocyte antigen 96 FUNCTION: Binds bacterial lipopolysaccharide (LPS) (PubMed:17803912, PubMed:17569869). Cooperates with TLR4 in the innate immune response to bacterial lipopolysaccharide (LPS), and with TLR2 in the response to cell wall components from Gram- positive and Gram-negative bacteria (PubMed:11160242, PubMed:11593030). Enhances TLR4-dependent activation of NF-kappa-B (PubMed:10359581). Cells expressing both LY96 and TLR4, but not TLR4 alone, respond to LPS (PubMed:10359581). {ECO:0000269|PubMed:10359581, ECO:0000269|PubMed:11160242, ECO:0000269|PubMed:11593030, ECO:0000269|PubMed:17569869, ECO:0000269|PubMed:17803912}.; . . unclassifiable (Anatomical System);uterus;lung;adrenal gland;placenta;testis;germinal center;brain; superior cervical ganglion;whole blood; 0.09202 0.17737 0.457594962 78.16112291 45.84024 1.30136 LYAR 0.000132448509465871 0.849858927864321 0.150008623626214 Ly1 antibody reactive . . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach;aorta; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.70550 0.11261 0.330767508 73.53739089 108.7561 2.26380 LYARP1 . . . Ly1 antibody reactive pseudogene 1 . . . . . . . . . . . LYG1 0.000104427732291753 0.583165354458264 0.416730217809444 lysozyme g1 . . . unclassifiable (Anatomical System);heart;ovary;colon;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;whole body;macula lutea;kidney;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skin; 0.05158 . -0.05129383 49.75819769 108.93484 2.26642 LYG2 5.77012180169849e-06 0.258301906424051 0.741692323454147 lysozyme g2 FUNCTION: May act as a potent antibacterial protein that may play a role in the innate immunity. {ECO:0000269|PubMed:21093056}.; . TISSUE SPECIFICITY: Strong expression detected in the eye and weak expression in the testis. No expression is observed in any other tissues. {ECO:0000269|PubMed:21093056}.; optic nerve;lung;macula lutea;testis;fovea centralis;choroid;lens;retina; . 0.20368 . 0.43736446 77.56546355 68.6004 1.71376 LYL1 0.672721211231352 0.306085089598218 0.0211936991704307 lymphoblastic leukemia associated hematopoiesis regulator 1 . DISEASE: Note=A chromosomal aberration involving LYL1 may be a cause of a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(7;19)(q35;p13) with TCRB.; . unclassifiable (Anatomical System);medulla oblongata;lymph node;colon;blood;uterus;lung;optic nerve;placenta;testis;germinal center;pineal gland;tonsil; fetal liver;testis - interstitial;testis - seminiferous tubule;testis;white blood cells;bone marrow; 0.13105 0.17996 . . 144.12857 2.61535 LYN 0.995480464487175 0.00451945068978845 8.48230367944098e-08 LYN proto-oncogene, Src family tyrosine kinase FUNCTION: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down- regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down- regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, PTK2B/PYK2, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Mediates phosphorylation of the BCR-ABL fusion protein. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3- kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr- 72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. {ECO:0000269|PubMed:10574931, ECO:0000269|PubMed:10748115, ECO:0000269|PubMed:10891478, ECO:0000269|PubMed:11435302, ECO:0000269|PubMed:11517336, ECO:0000269|PubMed:11825908, ECO:0000269|PubMed:14726379, ECO:0000269|PubMed:15795233, ECO:0000269|PubMed:16467205, ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:17977829, ECO:0000269|PubMed:18056483, ECO:0000269|PubMed:18070987, ECO:0000269|PubMed:18235045, ECO:0000269|PubMed:18577747, ECO:0000269|PubMed:18802065, ECO:0000269|PubMed:19290919, ECO:0000269|PubMed:20028775, ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:7687428}.; DISEASE: Note=Constitutively phosphorylated and activated in cells from a number of chronic myelogenous leukemia (CML) and acute myeloid leukemia (AML) patients. Mediates phosphorylation of the BCR-ABL fusion protein. Abnormally elevated expression levels or activation of LYN signaling may play a role in survival and proliferation of some types of cancer cells.; TISSUE SPECIFICITY: Detected in monocytes (at protein level). Detected in placenta, and in fetal brain, lung, liver and kidney. Widely expressed in a variety of organs, tissues, and cell types such as epidermoid, hematopoietic, and neuronal cells. Expressed in primary neuroblastoma tumors. {ECO:0000269|PubMed:3561390, ECO:0000269|PubMed:8064233}.; . . 0.80752 0.17206 -0.692458599 14.96815287 12.29428 0.44555 LYNX1 0.110678246204466 0.777234326837009 0.112087426958524 Ly6/neurotoxin 1 FUNCTION: Acts in different tissues through interaction to nicotinic acetylcholine receptors (nAChRs). In brain, isoform 2 modulates functional properties of nAChRs to prevent excessive excitation, and hence neurodegeneration. Enhances desensitization by increasing both the rate and extent of desensitization of alpha(4)beta(2) nAChRs and slowing recovery from desensitization. Promotes large amplitude ACh-evoked currents through alpha(4)beta(2) nAChRs (By similarity). Prevents plasticity in the primary visual cortex late in life (By similarity). In keratinocytes, isoform 3 delays differentiation and prevents apoptosis. {ECO:0000250, ECO:0000269|PubMed:16575903}.; . TISSUE SPECIFICITY: Isoform 3 is expressed at highest levels in cervix and esophagus, followed by adult and fetal skin. Expressed at lower levels in brain, lung, stomach, small intestine, colon, rectum, uterus, and thymus. Not detected in spleen nor bone marrow. In the epidermis, predominantly produced by keratinocytes of the suprabasal epidermal compartment (at protein level). In attached gingiva, produced at highest levels by basal cells located in the lowermost epithelial layers (at protein level). Up- regulated 3-fold in psoriatic lesional skin. Detected in serum (at protein level). {ECO:0000269|PubMed:12573258, ECO:0000269|PubMed:16575903}.; unclassifiable (Anatomical System);colon;choroid;fovea centralis;lens;retina;pancreas;lung;optic nerve;larynx;macula lutea;testis;head and neck;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;tongue;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.07396 0.12654 -0.26993514 34.59542345 73.0674 1.78518 LYPD1 0.000238591129314029 0.313658655115474 0.686102753755212 LY6/PLAUR domain containing 1 . . . unclassifiable (Anatomical System);uterus;pancreas;lung;testis;kidney;brain; amygdala;medulla oblongata;hypothalamus;appendix;atrioventricular node;caudate nucleus;pons; 0.21654 . 0.3032669 72.009908 18.3074 0.63566 LYPD2 0.0633022046112556 0.725387528592085 0.21131026679666 LY6/PLAUR domain containing 2 . . . optic nerve;lung;visual apparatus; . 0.06411 . 0.060756528 58.52795471 297.55923 3.67977 LYPD3 9.93205028627218e-09 0.0480717396291981 0.951928250438752 LY6/PLAUR domain containing 3 FUNCTION: Supports cell migration. May be involved in urothelial cell-matrix interactions. May be involved in tumor progression. {ECO:0000269|PubMed:11179665, ECO:0000269|PubMed:11245483, ECO:0000269|PubMed:12592373, ECO:0000269|PubMed:15012588}.; . TISSUE SPECIFICITY: Expressed in placenta, skin and urothelium. Found in suprabasal keratinocytes of chronic wounds. Weak expression is found in esophagus and peripheral blood mononuclear cells. Found in the majority of primary and metastatic transitional cell carcinomas (TCCs) and as well in breast cancer tissues, but not in adjacent normal tissues. High expression is found in the tumor component of some noninvasive superficial lesions and in invasive and metastatic urothelial cancers. {ECO:0000269|PubMed:11179665, ECO:0000269|PubMed:12592373, ECO:0000269|PubMed:15012588}.; unclassifiable (Anatomical System);ovary;heart;tongue;colon;skin;uterus;pancreas;prostate;lung;larynx;placenta;visual apparatus;hippocampus;hypopharynx;liver;head and neck;brain;mammary gland;bladder;stomach;thymus; dorsal root ganglion;superior cervical ganglion;prostate;tongue;placenta;skin;tonsil; 0.17337 0.12642 0.018483465 55.44939844 232.00794 3.29145 LYPD4 3.41494476753975e-05 0.359885051005679 0.640080799546645 LY6/PLAUR domain containing 4 . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; . 0.10738 0.09740 0.795569043 87.49115357 277.52057 3.56876 LYPD5 9.4450522196327e-05 0.561309446106372 0.438596103371432 LY6/PLAUR domain containing 5 . . . . . 0.12846 . 0.505321956 80.00707714 4335.73778 13.11321 LYPD6 0.000624825868659602 0.728228204294713 0.271146969836628 LY6/PLAUR domain containing 6 . . . unclassifiable (Anatomical System);heart;ovary;cartilage;lens;skin;bile duct;uterus;lung;placenta;bone;visual apparatus;pituitary gland;testis;kidney;brain;bladder; dorsal root ganglion;superior cervical ganglion;testis - interstitial;atrioventricular node;trigeminal ganglion;cerebellum; 0.36933 0.10759 -0.229483771 36.86010852 20.10254 0.68738 LYPD6B 0.00103350797846491 0.822095813140414 0.176870678881121 LY6/PLAUR domain containing 6B . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;cochlea;oesophagus;thyroid;bone;testis;bladder;brain;unclassifiable (Anatomical System);hypothalamus;pharynx;blood;lens;breast;lung;placenta;macula lutea;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . -0.161524709 41.6430762 127.69451 2.46393 LYPD8 . . . LY6/PLAUR domain containing 8 . . . . . . . . . . . LYPLA1 0.00849442588120882 0.933615032484653 0.0578905416341382 lysophospholipase I FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has depalmitoylating activity toward KCNMA1. Has low lysophospholipase activity. {ECO:0000269|PubMed:20418879, ECO:0000269|PubMed:22399288}.; . . medulla oblongata;ovary;colon;skin;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;adrenal cortex;blood;skeletal muscle;breast;pancreas;pia mater;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; prostate;superior cervical ganglion;placenta;testis;tumor;kidney;trigeminal ganglion; 0.65717 0.16156 0.393270925 76.04977589 373.52904 4.07720 LYPLA1P1 . . . lysophospholipase I pseudogene 1 . . . . . . . . . . . LYPLA1P2 . . . lysophospholipase I pseudogene 2 . . . . . . . . . . . LYPLA1P3 . . . lysophospholipase I pseudogene 3 . . . . . . . . . . . LYPLA2 0.979519145027567 0.0204638660097318 1.69889627016244e-05 lysophospholipase II FUNCTION: May hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has lysophospholipase activity (By similarity). Deacylates GAP43. {ECO:0000250, ECO:0000269|PubMed:21152083}.; . . . . 0.20635 0.10011 -0.295622497 32.61972163 4.69509 0.16866 LYPLA2P1 . . . lysophospholipase II pseudogene 1 . . . . . . . . . . . LYPLA2P2 . . . lysophospholipase II pseudogene 2 . . . . . . . . . . . LYPLA2P3 . . . lysophospholipase II pseudogene 3 . . . . . . . . . . . LYPLAL1 3.45406097372974e-08 0.0519232413227785 0.948076724136612 lysophospholipase like 1 FUNCTION: Has depalmitoylating activity toward KCNMA1. Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site. {ECO:0000269|PubMed:22052940, ECO:0000269|PubMed:22399288}.; . . . . 0.09828 0.07733 0.21689899 68.12927577 127.16813 2.46041 LYPLAL1-AS1 . . . LYPLAL1 antisense RNA 1 (head to head) . . . . . . . . . . . LYRM1 1.7941553165101e-05 0.261195252654803 0.738786805792032 LYR motif containing 1 FUNCTION: May promote cell proliferation and inhibition of apoptosis of preadipocytes. {ECO:0000269|PubMed:19022914}.; . TISSUE SPECIFICITY: High levels in adipose tissue. {ECO:0000269|PubMed:19022914}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;lens;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.17626 0.10112 0.148941568 64.31941496 40.01366 1.17643 LYRM2 0.0596813347506901 0.716876796857066 0.223441868392244 LYR motif containing 2 . . . . . 0.10963 . 0.391453969 75.87284737 1719.30322 7.64598 LYRM4 0.0402580402942408 0.649976116807293 0.309765842898466 LYR motif containing 4 FUNCTION: Required for nuclear and mitochondrial iron-sulfur protein biosynthesis. {ECO:0000269|PubMed:17331979, ECO:0000269|PubMed:19454487}.; . TISSUE SPECIFICITY: Reduced mRNA levels in Friedreich ataxia patients. {ECO:0000269|PubMed:17331979}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;alveolus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;temporal lobe;testis;globus pallidus; 0.05471 0.08661 . . 3625.9544 11.68126 LYRM4-AS1 . . . LYRM4 antisense RNA 1 . . . . . . . . . . . LYRM5 0.00088717027424368 0.345948172137964 0.653164657587792 LYR motif containing 5 . . . . . 0.12523 0.11262 -0.075159878 47.78839349 28.66939 0.91761 LYRM7 0.0135019993167191 0.666577990330351 0.31992001035293 LYR motif containing 7 FUNCTION: Assembly factor required for Rieske Fe-S protein UQCRFS1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane. {ECO:0000269|PubMed:23168492}.; DISEASE: Mitochondrial complex III deficiency, nuclear 8 (MC3DN8) [MIM:615838]: A form of mitochondrial complex III deficiency, a disorder of the mitochondrial respiratory chain resulting in a highly variable phenotype depending on which tissues are affected. Clinical features include mitochondrial encephalopathy, psychomotor retardation, ataxia, severe failure to thrive, liver dysfunction, renal tubulopathy, muscle weakness and exercise intolerance. {ECO:0000269|PubMed:24014394}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.09188 . 0.035072054 56.2514744 25.56997 0.83394 LYRM9 0.0450003073591636 0.670371777808648 0.284627914832188 LYR motif containing 9 . . . . . . . 0.057118534 57.99716914 22.4067 0.75132 LYSMD1 0.181950236021973 0.765197437307468 0.0528523266705592 LysM domain containing 1 . . . . . 0.09668 . 0.237127192 68.98443029 66.19138 1.67538 LYSMD2 0.256648623702389 0.640143607702724 0.103207768594886 LysM domain containing 2 . . . medulla oblongata;smooth muscle;ovary;colon;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pancreas;lung;placenta;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach; whole brain;amygdala;subthalamic nucleus;superior cervical ganglion;temporal lobe;globus pallidus;ciliary ganglion;cingulate cortex;cerebellum; 0.18370 . . . 268.01742 3.51306 LYSMD3 0.771815089892096 0.226494309998763 0.00169060010914104 LysM domain containing 3 . . . colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;liver;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.26054 0.09109 0.060756528 58.52795471 102.69924 2.19111 LYSMD4 1.73218412498145e-05 0.25650459309454 0.743478085064211 LysM domain containing 4 . . . unclassifiable (Anatomical System);lymph node;colon;skin;lung;oesophagus;placenta;bone;liver;testis;spleen;cervix;germinal center;brain;mammary gland; . 0.12214 . 1.818943827 96.98631753 4445.55355 13.36600 LYST 0.999978422869173 2.15771308269855e-05 5.0099958361365e-28 lysosomal trafficking regulator FUNCTION: May be required for sorting endosomal resident proteins into late multivesicular endosomes by a mechanism involving microtubules.; . TISSUE SPECIFICITY: Abundantly expressed in adult and fetal thymus, peripheral blood leukocytes, bone marrow and several regions of the adult brain.; . . 0.19342 . -3.039637526 0.495399858 1598.72637 7.39996 LYST-AS1 . . . LYST antisense RNA 1 . . . . . . . . . . . LYVE1 4.22095940703122e-07 0.210617362228082 0.789382215675977 lymphatic vessel endothelial hyaluronan receptor 1 FUNCTION: Ligand-specific transporter trafficking between intracellular organelles (TGN) and the plasma membrane. Plays a role in autocrine regulation of cell growth mediated by growth regulators containing cell surface retention sequence binding (CRS). May act as a hyaluronan (HA) transporter, either mediating its uptake for catabolism within lymphatic endothelial cells themselves, or its transport into the lumen of afferent lymphatic vessels for subsequent re-uptake and degradation in lymph nodes. {ECO:0000269|PubMed:10037799}.; . TISSUE SPECIFICITY: Mainly expressed in endothelial cells lining lymphatic vessels. {ECO:0000269|PubMed:10037799}.; ovary;colon;parathyroid;fovea centralis;choroid;vein;retina;uterus;optic nerve;whole body;cochlea;bone;pituitary gland;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;lens;skeletal muscle;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;fetal liver;placenta;adrenal cortex;appendix;fetal lung;ciliary ganglion;trigeminal ganglion; 0.45011 0.17510 0.174625237 65.9648502 191.53212 3.00143 LYZ 0.00137551693250335 0.659563513816053 0.339060969251444 lysozyme FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte- macrophage system and enhance the activity of immunoagents.; DISEASE: Amyloidosis 8 (AMYL8) [MIM:105200]: A hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash. {ECO:0000269|PubMed:8464497}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;prostate;larynx;thyroid;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);heart;small intestine;lacrimal gland;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; lymph node;trachea;salivary gland;thyroid;white blood cells;whole blood;tonsil;bone marrow;thymus; 0.05206 0.10095 0.3032669 72.009908 105.50557 2.22582 LYZL1 0.0486957459732464 0.857607841652871 0.093696412373883 lysozyme like 1 . . . . . 0.11688 0.13208 0.060756528 58.52795471 2249.95135 8.76184 LYZL2 3.25974148951073e-06 0.191157736091285 0.808839004167225 lysozyme like 2 . . TISSUE SPECIFICITY: Expressed in testis, epididymis and placenta. {ECO:0000269|PubMed:16014814}.; . . 0.10712 0.11669 0.084621747 60.31493277 217.1399 3.18520 LYZL4 0.112282902130519 0.777746254848326 0.109970843021155 lysozyme like 4 . . TISSUE SPECIFICITY: Expressed in testis and epididymis. {ECO:0000269|PubMed:16014814}.; unclassifiable (Anatomical System);lung;macula lutea;liver;testis;spleen;fovea centralis; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.09266 0.10955 -0.007201372 53.19061099 42.63012 1.23682 LYZL6 7.44688375794253e-05 0.305733992863965 0.694191538298456 lysozyme like 6 . . TISSUE SPECIFICITY: Expressed in testis and epididymis. {ECO:0000269|PubMed:16014814}.; medulla oblongata;lung;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.08732 0.10009 0.393270925 76.04977589 1283.21856 6.74534 LZIC 0.00197924734359642 0.735667359280997 0.262353393375406 leucine zipper and CTNNBIP1 domain containing . . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in kidney. Up-regulated in several cases of gastric cancers. {ECO:0000269|PubMed:11712074}.; . . 0.19790 0.10235 -0.053113545 49.38664779 27.22008 0.87639 LZTFL1 0.194102810474707 0.803674751952826 0.00222243757246646 leucine zipper transcription factor like 1 FUNCTION: Regulates ciliary localization of the BBSome complex. Together with the BBSome complex, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. May play a role in neurite outgrowth. May have tumor suppressor function. {ECO:0000269|PubMed:20233871, ECO:0000269|PubMed:22072986, ECO:0000269|PubMed:22510444}.; DISEASE: Bardet-Biedl syndrome 17 (BBS17) [MIM:615994]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:22510444, ECO:0000269|PubMed:23692385}. Note=The disease is caused by mutations affecting the gene represented in this entry. Patients carrying LZTFL1 mutations manifest mesoaxial polydactyly, a clinical feature very uncommon for Bardet-Biedl syndrome (PubMed:22510444 and PubMed:23692385). Some patients manifest situs inversus (PubMed:22510444). {ECO:0000269|PubMed:22510444}.; TISSUE SPECIFICITY: Expressed in prostate, ovary, stomach, pancreas, esophagus, breast, liver, bladder, kidney, thyroid, colon and lung (at protein level). Down-regulated in multiple primary tumors (at protein level). Detected in testis, heart, skeletal muscle, thymus, spleen, small intestine, and peripheral blood leukocytes. {ECO:0000269|PubMed:11352561, ECO:0000269|PubMed:20233871}.; medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;whole body;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach;aorta;thymus; subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;pons; 0.11544 0.10055 0.503505267 79.88912479 677.63529 5.20105 LZTR1 3.38323005538586e-52 2.05067110075144e-13 0.999999999999795 leucine-zipper-like transcription regulator 1 FUNCTION: Probable transcriptional regulator that may play a crucial role in embryogenesis.; DISEASE: Schwannomatosis 2 (SWNTS2) [MIM:615670]: A cancer predisposition syndrome in which patients develop multiple non- vestibular schwannomas, benign neoplasms that arise from Schwann cells of the cranial, peripheral, and autonomic nerves. {ECO:0000269|PubMed:24362817}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . ovary;colon;choroid;vein;skin;retina;uterus;prostate;optic nerve;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;trophoblast;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;breast;pancreas;lung;placenta;visual apparatus;liver;alveolus;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.21774 0.10131 -2.677226852 0.731304553 53.87534 1.46377 LZTS1 0.525971472516105 0.470507501238812 0.00352102624508299 leucine zipper, putative tumor suppressor 1 FUNCTION: Involved in the regulation of cell growth. May stabilize the active CDC2-cyclin B1 complex and thereby contribute to the regulation of the cell cycle and the prevention of uncontrolled cell proliferation. May act as a tumor suppressor. {ECO:0000269|PubMed:10097140, ECO:0000269|PubMed:11464283, ECO:0000269|PubMed:11504921}.; DISEASE: Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the esophagus. The most common types are esophageal squamous cell carcinoma and adenocarcinoma. Cancer of the esophagus remains a devastating disease because it is usually not detected until it has progressed to an advanced incurable stage. {ECO:0000269|PubMed:10097140}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in testis, prostate, spleen, thymus, ovary and brain. Detected at lower levels in heart, placenta, small intestine, colon, liver, kidney, skeletal muscle and pancreas. Not detectable in primary tumors from breast and prostate and in many cancer cell lines. {ECO:0000269|PubMed:10097140}.; unclassifiable (Anatomical System);uterus;ovary;heart;colon;brain;skin;thymus; whole brain;amygdala;medulla oblongata;superior cervical ganglion;temporal lobe;atrioventricular node;pons;caudate nucleus;skin;skeletal muscle;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.21066 0.21857 0.404185162 76.48619958 796.76728 5.56365 LZTS1-AS1 . . . LZTS1 antisense RNA 1 . . . . . . . . . . . LZTS2 0.875482095891018 0.124504456961646 1.34471473366496e-05 leucine zipper, putative tumor suppressor 2 FUNCTION: Negative regulator of katanin-mediated microtubule severing and release from the centrosome. Required for central spindle formation and the completion of cytokinesis. May negatively regulate axonal outgrowth by preventing the formation of microtubule bundles that are necessary for transport within the elongating axon. Negative regulator of the Wnt signaling pathway. Represses beta-catenin-mediated transcriptional activation by promoting the nuclear exclusion of beta-catenin. {ECO:0000255|HAMAP-Rule:MF_03026, ECO:0000269|PubMed:17000760, ECO:0000269|PubMed:17351128, ECO:0000269|PubMed:17950943, ECO:0000269|PubMed:18490357}.; . TISSUE SPECIFICITY: Highly expressed in prostate and testis, and at slightly lower levels in spleen, thymus, uterus, small intestine and colon. {ECO:0000269|PubMed:11709705}.; unclassifiable (Anatomical System);lymph node;hypothalamus;placenta;hippocampus;colon;brain;skin;retina;bone marrow; . 0.17802 0.11163 -1.195919584 5.832743572 130.62365 2.48985 M1AP 5.83274913656993e-12 0.0587963733685 0.941203626625667 meiosis 1 associated protein FUNCTION: Required for meiosis I progression during spermatogenesis. {ECO:0000250}.; . . . . 0.19416 0.09010 -0.422438699 25.64284029 194.07805 3.02142 M6PR 0.71302578173056 0.286295950618572 0.000678267650867887 mannose-6-phosphate receptor, cation dependent FUNCTION: Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6- phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex.; . . myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;urinary;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus;cerebellum; white blood cells; 0.73233 0.78953 -0.163345027 41.24793583 1471.06525 7.14753 MAA . . . microphthalmia or anophthalmia and associated anomalies . . . . . . . . . . . MAATS1 9.7774896920592e-10 0.904945227028894 0.0950547719933566 MYCBP-associated, testis expressed 1 FUNCTION: Isoform 4 may play a role in spermatogenesis. {ECO:0000269|PubMed:12223483}.; . TISSUE SPECIFICITY: Isoform 1 is strongly expressed in the liver. Isoform 4 is widely expressed, but strongly expressed in all spermatogenesis-related tissues, including the testis, the epithelium of cauda and the corpus epididymis, as well as the spermatid and mature sperm. Isoform 4 is also expressed in Leydig cells. Isoform 3 is expressed in the testis.; . . 0.06869 0.09515 0.872633161 88.87119604 840.25979 5.67623 MAB21L1 0.367416501981844 0.620997062184007 0.0115864358341497 mab-21-like 1 (C. elegans) FUNCTION: Required for several aspects of embryonic development including normal development of the eye. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, cerebellum and skeletal muscle. {ECO:0000269|PubMed:8733127}.; . . 0.79952 0.11262 -0.449946534 24.00330267 17.33297 0.60901 MAB21L2 0.803779158934581 0.195111771857282 0.00110906920813788 mab-21-like 2 (C. elegans) FUNCTION: Required for several aspects of embryonic development including normal development of the eye. {ECO:0000269|PubMed:24906020}.; DISEASE: Microphthalmia, syndromic, 14 (MCOPS14) [MIM:615877]: A form of microphthalmia, a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. MCOPS14 patients exhibit bilateral colobomatous microphthalmia or bilateral anophthalmia. Intellectual disability and rhizomelic skeletal dysplasia is present in some affected individuals. {ECO:0000269|PubMed:24906020}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);optic nerve;ovary;macula lutea;developmental;colon;fovea centralis;choroid;lens;brain;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;testis - interstitial;tongue;cerebellum peduncles;appendix;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.67997 0.12971 -0.339715008 30.06605331 10.58824 0.38520 MAB21L3 0.000490218809434059 0.877196306078614 0.122313475111952 mab-21-like 3 (C. elegans) . . . . . 0.24860 . -0.666770504 15.86459071 47.94272 1.34533 MACC1 7.56011564443965e-17 0.00109284341171094 0.998907156588289 metastasis associated in colon cancer 1 FUNCTION: Acts as a transcription activator for MET and as a key regulator of HGF-MET signaling. Promotes cell motility, proliferation and hepatocyte growth factor (HGF)-dependent scattering in vitro and tumor growth and metastasis in vivo. {ECO:0000269|PubMed:19098908}.; . TISSUE SPECIFICITY: Preferentially expressed in metastasizing tumors. {ECO:0000269|PubMed:19098908}.; unclassifiable (Anatomical System);breast;pancreas;lung;larynx;colon;head and neck;bone marrow; . . 0.09681 1.806007038 96.95093182 3010.79485 10.42126 MACC1-AS1 . . . MACC1 antisense RNA 1 . . . . . . . . . . . MACF1 1 6.8021650013566e-31 4.01532373290605e-81 microtubule-actin crosslinking factor 1 FUNCTION: Isoform 2 is a F-actin-binding protein which may play a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules. Plays an important role in ERBB2- dependent stabilization of microtubules at the cell cortex. Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane. Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics. May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4. Plays a key role in wound healing and epidermal cell migration. Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate MT dynamics and polarize hair follicle stem cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:15265687, ECO:0000269|PubMed:20937854}.; . TISSUE SPECIFICITY: Isoform 2 is ubiquitously expressed. Isoform 1 is expressed in cell lines NCI-H460, A-549 and HaCaT. Isoform 4 is expressed in heart, lung, pituitary and placenta, not found in brain, kidney, liver, pancreas or skeletal muscle. {ECO:0000269|PubMed:11845288, ECO:0000269|PubMed:16076900}.; lymphoreticular;smooth muscle;ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;mammary gland;colon;parathyroid;uterus;whole body;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; amygdala;medulla oblongata;thalamus;superior cervical ganglion;hypothalamus;spinal cord;pons;atrioventricular node;caudate nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.41854 . -3.915490887 0.206416608 6684.15405 17.31418 MACOM . . . macrophthalmia, colobomatous, with microcornea . . . . . . . . . . . MACROD1 0.00662476930110474 0.914679941804456 0.0786952888944388 MACRO domain containing 1 FUNCTION: Removes ADP-ribose from glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Plays a role in estrogen signaling. Binds to androgen receptor (AR) and amplifies the transactivation function of AR in response to androgen. May play an important role in carcinogenesis and/or progression of hormone-dependent cancers by feed-forward mechanism that activates ESR1 transactivation. Could be an ESR1 coactivator, providing a positive feedback regulatory loop for ESR1 signal transduction. Could be involved in invasive growth by down-regulating CDH1 in endometrial cancer cells. Enhances ESR1-mediated transcription activity. {ECO:0000269|PubMed:17893710, ECO:0000269|PubMed:17914104, ECO:0000269|PubMed:19022849, ECO:0000269|PubMed:19403568, ECO:0000269|PubMed:21257746, ECO:0000269|PubMed:23474712}.; DISEASE: Note=A chromosomal aberration involving MACROD1 is found in acute leukemia. Translocation t(11;21)(q13;q22) that forms a RUNX1-MACROD1 fusion protein. {ECO:0000269|PubMed:17532767}.; . ovary;salivary gland;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;brain;unclassifiable (Anatomical System);trophoblast;heart;islets of Langerhans;skeletal muscle;lung;placenta;visual apparatus;cervix;kidney;mammary gland;stomach; liver;kidney;skeletal muscle; 0.14321 0.14254 . . 52.96006 1.44453 MACROD2 0.0113567470210345 0.986855234324477 0.00178801865448882 MACRO domain containing 2 FUNCTION: Removes ADP-ribose from glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. {ECO:0000269|PubMed:21257746, ECO:0000269|PubMed:23474712}.; . . testis; subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.28415 . 0.463046108 78.58575136 3133.5596 10.66274 MACROD2-AS1 . . . MACROD2 antisense RNA 1 . . . . . . . . . . . MACROD2-IT1 . . . MACROD2 intronic transcript 1 . . . . . . . . . . . MAD1L1 2.03780827176675e-10 0.628404149435575 0.371595850360644 MAD1 mitotic arrest deficient-like 1 (yeast) FUNCTION: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. May recruit MAD2L1 to unattached kinetochores. Has a role in the correct positioning of the septum. Required for anchoring MAD2L1 to the nuclear periphery. Binds to the TERT promoter and represses telomerase expression, possibly by interfering with MYC binding. {ECO:0000269|PubMed:10049595, ECO:0000269|PubMed:12837246, ECO:0000269|PubMed:20133940}.; DISEASE: Note=Defects in MAD1L1 are involved in the development and/or progression of various types of cancer. {ECO:0000269|PubMed:10597320, ECO:0000269|PubMed:11423979}.; TISSUE SPECIFICITY: Expressed weakly at G0/G1 and highly at late S and G2/M phase.; unclassifiable (Anatomical System);heart;colon;skin;uterus;pancreas;prostate;lung;larynx;placenta;visual apparatus;liver;testis;head and neck;germinal center;brain;mammary gland;tonsil;stomach;thymus; liver;white blood cells; 0.61427 0.11427 -1.322782544 4.759377212 2213.90136 8.66443 MAD2L1 0.0131674546651585 0.861483837482861 0.125348707851981 MAD2 mitotic arrest deficient-like 1 (yeast) FUNCTION: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. Required for the execution of the mitotic checkpoint which monitors the process of kinetochore- spindle attachment and inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate. {ECO:0000269|PubMed:10700282, ECO:0000269|PubMed:11804586, ECO:0000269|PubMed:15024386}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; fetal liver;tumor;testis; 0.99211 0.15588 0.03689118 56.64071715 19.38659 0.66662 MAD2L1BP 0.0082444395179893 0.931639124922515 0.0601164355594955 MAD2L1 binding protein FUNCTION: May function to silence the spindle checkpoint and allow mitosis to proceed through anaphase by binding MAD2L1 after it has become dissociated from the MAD2L1-CDC20 complex. {ECO:0000269|PubMed:18022368}.; . . . . 0.12674 0.07753 -0.361761279 28.6329323 88.65626 2.02020 MAD2L1P1 . . . MAD2 mitotic arrest deficient-like 1 (yeast) pseudogene 1 . . . . . . . . . . . MAD2L2 0.202505866427509 0.787653807196396 0.00984032637609466 MAD2 mitotic arrest deficient-like 2 (yeast) FUNCTION: Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation. {ECO:0000269|PubMed:11459825, ECO:0000269|PubMed:11459826, ECO:0000269|PubMed:17296730, ECO:0000269|PubMed:17719540, ECO:0000269|PubMed:19443654}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11717438}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;mammary gland;stomach; . 0.86608 0.13382 0.058937498 58.26256192 12.78537 0.46479 MADCAM1 0.428374924492615 0.539079685971327 0.0325453895360578 mucosal vascular addressin cell adhesion molecule 1 FUNCTION: Cell adhesion leukocyte receptor expressed by mucosal venules, helps to direct lymphocyte traffic into mucosal tissues including the Peyer patches and the intestinal lamina propria. It can bind both integrin alpha-4/beta-7 and L-selectin, regulating both the passage and retention of leukocytes. Isoform 2, lacking the mucin-like domain, may be specialized in supporting integrin alpha-4/beta-7-dependent adhesion strengthening, independent of L- selectin binding.; . TISSUE SPECIFICITY: Highly expressed on high endothelial venules (HEV) and lamina propia venules found in the small intestine, and to a lesser extent in the colon and spleen. Very low levels of expression found in pancreas and brain. Not expressed in the thymus, prostate, ovaries, testis, heart, placenta, lung, liver, skeletal muscle, kidney or peripheral blood leukocytes. {ECO:0000269|PubMed:8609404, ECO:0000269|PubMed:8989586}.; unclassifiable (Anatomical System);lung;heart;macula lutea;testis;fovea centralis;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11932 . . . 394.94417 4.17539 MADD 0.000901823421065546 0.999098176249239 3.2969540515958e-10 MAP kinase activating death domain FUNCTION: Plays a significant role in regulating cell proliferation, survival and death through alternative mRNA splicing. Isoform 5 shows increased cell proliferation and isoform 2 shows decreased. Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms. Component of the TNFRSF1A signaling complex: MADD links TNFRSF1A with MAP kinase activation. Plays an important regulatory role in physiological cell death (TNF-alpha-induced, caspase-mediated apoptosis); isoform 1 is susceptible to inducing apoptosis, isoform 5 is resistant and isoform 3 and isoform 4 have no effect. {ECO:0000269|PubMed:11577081, ECO:0000269|PubMed:14716293, ECO:0000269|PubMed:14735464, ECO:0000269|PubMed:15007167, ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:9115275}.; . TISSUE SPECIFICITY: Highly expressed in fetal brain and kidney; adult testis, ovary, brain and heart. Isoform 5 is constitutively expressed in all tissues. Isoform 7 is expressed in fetal liver and in several cancer cell lines. {ECO:0000269|PubMed:14716293, ECO:0000269|PubMed:8988362, ECO:0000269|PubMed:9796103}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;small intestine;lacrimal gland;pineal body;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; whole brain;amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;cerebellum peduncles;temporal lobe;pons;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.35532 0.24703 -1.955181094 1.857749469 2594.76668 9.53267 MAEA 0.844858361058156 0.15502233484997 0.00011930409187425 macrophage erythroblast attacher FUNCTION: Plays a role in erythroblast enucleation and in the development of the mature macrophages. Mediates the attachment of erythroid cell to mature macrophages, in correlation with the presence of MAEA at cell surface of mature macrophages; This MAEA- mediated contact inhibits erythroid cells apoptosis. Participates to erythroblastic island formation, which is the functional unit of definitive erythropoiesis. Associates with F-actin to regulate actin distribution in erythroblasts and macrophages. May contribute to nuclear architecture and cells division events. {ECO:0000269|PubMed:16510120, ECO:0000269|PubMed:9763581}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16510120, ECO:0000269|PubMed:9763581}.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;germinal center;brain;tonsil;heart;cartilage;tongue;blood;skeletal muscle;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;uterus;whole body;cerebral cortex;larynx;synovium;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus;cerebellum; amygdala;whole brain;superior cervical ganglion;prefrontal cortex;cerebellum; 0.31925 0.30319 -0.846787714 11.05803255 43.49553 1.25546 MAEL 0.0212546382876771 0.978034080493548 0.00071128121877502 maelstrom spermatogenic transposon silencer FUNCTION: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Its association with piP- bodies suggests a participation in the secondary piRNAs metabolic process. Required for the localization of germ-cell factors to the meiotic nuage (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis-specific. Expressed in various cancer cell lines, probably due to demethylation of its promoter. {ECO:0000269|PubMed:19693694, ECO:0000269|Ref.1}.; . . 0.09752 0.10521 0.108486928 61.90728946 126.78283 2.45571 MAF 0.429001156450398 0.538593017028158 0.0324058265214434 v-maf avian musculoaponeurotic fibrosarcoma oncogene homolog FUNCTION: Acts as a transcriptional activator or repressor. Involved in embryonic lens fiber cell development. Recruits the transcriptional coactivators CREBBP and/or EP300 to crystallin promoters leading to up-regulation of crystallin gene during lens fiber cell differentiation. Activates the expression of IL4 in T helper 2 (Th2) cells. Increases T-cell susceptibility to apoptosis by interacting with MYB and decreasing BCL2 expression. Together with PAX6, transactivates strongly the glucagon gene promoter through the G1 element. Activates transcription of the CD13 proximal promoter in endothelial cells. Represses transcription of the CD13 promoter in early stages of myelopoiesis by affecting the ETS1 and MYB cooperative interaction. Involved in the initial chondrocyte terminal differentiation and the disappearance of hypertrophic chondrocytes during endochondral bone development. Binds to the sequence 5'-[GT]G[GC]N[GT]NCTCAGNN-3' in the L7 promoter. Binds to the T-MARE (Maf response element) sites of lens-specific alpha- and beta-crystallin gene promoters. Binds element G1 on the glucagon promoter. Binds an AT-rich region adjacent to the TGC motif (atypical Maf response element) in the CD13 proximal promoter in endothelial cells (By similarity). When overexpressed, represses anti-oxidant response element (ARE)- mediated transcription. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. Binds to the ARE sites of detoxifying enzyme gene promoters. {ECO:0000250, ECO:0000269|PubMed:12149651, ECO:0000269|PubMed:14998494, ECO:0000269|PubMed:15007382, ECO:0000269|PubMed:16247450, ECO:0000269|PubMed:19143053}.; DISEASE: Note=A chromosomal aberration involving MAF is found in some forms of multiple myeloma (MM). Translocation t(14;16)(q32.3;q23) with an IgH locus.; DISEASE: Cataract 21, multiple types (CTRCT21) [MIM:610202]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT21 includes cerulean and pulverulent cataracts. Cerulean cataracts are characterized by peripheral bluish and white opacifications organized in concentric layers with occasional central lesions arranged radially. The opacities are observed in the superficial layers of the fetal nucleus as well as the adult nucleus of the lens. Involvement is usually bilateral. Visual acuity is only mildly reduced in childhood. In adulthood, the opacifications may progress, making lens extraction necessary. Histologically the lesions are described as fusiform cavities between lens fibers which contain a deeply staining granular material. Although the lesions may take on various colors, a dull blue is the most common appearance and is responsible for the designation cerulean cataract. Pulverulent cataracts are characterized by a dust-like, 'pulverised' appearance of the opacities which can be found in any part of the lens. In some cases cataract is associated with microcornea without any other systemic anomaly or dysmorphism. Microcornea is defined by a corneal diameter inferior to 10 mm in both meridians in an otherwise normal eye. {ECO:0000269|PubMed:11772997, ECO:0000269|PubMed:16470690, ECO:0000269|PubMed:24664492}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ayme-Gripp syndrome (AYGRP) [MIM:601088]: A multisystem disorder characterized by congenital cataracts, sensorineural deafness, intellectual disability, seizures, brachycephaly, distinctive flat facial appearance, skeletal anomalies, mammary gland hypoplasia, and reduced growth. {ECO:0000269|PubMed:25865493}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in endothelial cells. {ECO:0000269|PubMed:17897790}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;optic nerve;lung;thyroid;placenta;macula lutea;liver;testis;spleen;cervix;germinal center;kidney;spinal ganglion;brain; tongue;kidney;trigeminal ganglion;skeletal muscle; 0.26048 . . . 30.63442 0.97421 MAF1 0.794024579551437 0.204706728209137 0.00126869223942616 MAF1 homolog, negative regulator of RNA polymerase III FUNCTION: Element of the mTORC1 signaling pathway that acts as a mediator of diverse signals and that represses RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA. {ECO:0000269|PubMed:20233713, ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20543138}.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;synovium;thyroid;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;urinary;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; . 0.10387 0.12654 -0.117432389 44.89266336 7.84886 0.28873 MAFA . . . v-maf avian musculoaponeurotic fibrosarcoma oncogene homolog A FUNCTION: Acts as a transcriptional factor. Specifically binds the insulin enhancer element RIPE3b and activates insulin gene expression. Cooperates synergistically with NEUROD1 and PDX1. Phosphorylation by GSK3 increases its transcriptional activity and is required for its oncogenic activity. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. {ECO:0000269|PubMed:12011435, ECO:0000269|PubMed:12368292, ECO:0000269|PubMed:15665000, ECO:0000269|PubMed:15993959, ECO:0000269|PubMed:18042454, ECO:0000269|PubMed:19143053}.; . . pancreas;whole body;islets of Langerhans;blood; . 0.31846 . . . 362.20244 4.02808 MAFA-AS1 . . . MAFA antisense RNA 1 . . . . . . . . . . . MAFB . . . v-maf avian musculoaponeurotic fibrosarcoma oncogene homolog B FUNCTION: Acts as a transcriptional activator or repressor. Plays a pivotal role in regulating lineage-specific hematopoiesis by repressing ETS1-mediated transcription of erythroid-specific genes in myeloid cells. Required for monocytic, macrophage, osteoclast, podocyte and islet beta cell differentiation. Involved in renal tubule survival and F4/80 maturation. Activates the insulin and glucagon promoters. Together with PAX6, transactivates weakly the glucagon gene promoter through the G1 element. SUMO modification controls its transcriptional activity and ability to specify macrophage fate. Binds element G1 on the glucagon promoter (By similarity). Involved either as an oncogene or as a tumor suppressor, depending on the cell context. {ECO:0000250|UniProtKB:P54841, ECO:0000269|PubMed:19143053}.; DISEASE: Multicentric carpotarsal osteolysis syndrome (MCTO) [MIM:166300]: A rare skeletal disorder, usually presenting in early childhood with a clinical picture mimicking juvenile rheumatoid arthritis. Progressive destruction of the carpal and tarsal bone usually occurs and other bones may also be involved. Chronic renal failure is a frequent component of the syndrome. Mental retardation and minor facial anomalies have been noted in some patients. {ECO:0000269|PubMed:22387013}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10444328}.; . . 0.67451 0.25991 -0.141298762 42.87567823 12.33675 0.44752 MAFD1 . . . major affective disorder 1 . . . . . . . . . . . MAFD2 . . . major affective disorder 2 . . . . . . . . . . . MAFF 0.042201121909027 0.658723067852476 0.299075810238497 v-maf avian musculoaponeurotic fibrosarcoma oncogene homolog F FUNCTION: Interacts with the upstream promoter region of the oxytocin receptor gene. May be a transcriptional enhancer in the up-regulation of the oxytocin receptor gene at parturition. Since it lacks a putative transactivation domain, it may behave as a transcriptional repressor when it dimerize among himself. May also serve as a transcriptional activator by dimerizing with other (usually larger) basic-zipper proteins and recruiting them to specific DNA-binding sites. May be involved in the cellular stress response.; . TISSUE SPECIFICITY: Expressed in the term myometrium and kidney.; unclassifiable (Anatomical System);smooth muscle;ovary;skin;skeletal muscle;retina;bone marrow;breast;pancreas;lung;larynx;thyroid;placenta;visual apparatus;testis;head and neck;spleen;cervix;brain;mammary gland;stomach; lung;placenta;adrenal cortex;ciliary ganglion;trigeminal ganglion; 0.25853 0.16061 . . 23.75237 0.78498 MAFG 0.625915690848724 0.343053250400764 0.0310310587505117 v-maf avian musculoaponeurotic fibrosarcoma oncogene homolog G FUNCTION: Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves. However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins and recruiting them to specific DNA-binding sites. Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor. Transcription factor, component of erythroid-specific transcription factor NF- E2. Activates globin gene expression when associated with NF-E2. May be involved in signal transduction of extracellular H(+) (By similarity). {ECO:0000250, ECO:0000269|PubMed:11154691}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Also expressed in heart and brain.; ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;iris;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;occipital lobe;ciliary ganglion;atrioventricular node;parietal lobe;cingulate cortex;cerebellum; 0.50062 0.15588 -0.361761279 28.6329323 3.26174 0.11772 MAFG-AS1 . . . MAFG antisense RNA 1 (head to head) . . . . . . . . . . . MAFIP . . . MAFF interacting protein (pseudogene) FUNCTION: Acts as coactivator of MAFF transcriptional activity. Inhibits cell growth and colony-forming efficiency. {ECO:0000269|PubMed:15881666, ECO:0000269|PubMed:16549056}.; . TISSUE SPECIFICITY: Strongly expressed in brain, kidney and ovary. Moderately expressed in liver, spleen, thymus, prostate, testis, small intestine and colon. Weakly expressed in heart, placenta, lung and leukocytes. {ECO:0000269|PubMed:15881666}.; . . 0.18404 0.14494 0.148941568 64.31941496 . . MAFK 0.557286406195743 0.391983491221053 0.0507301025832042 v-maf avian musculoaponeurotic fibrosarcoma oncogene homolog K FUNCTION: Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves. However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins and recruiting them to specific DNA-binding sites. Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor. {ECO:0000269|PubMed:9150357}.; . . unclassifiable (Anatomical System);lung;ovary;thyroid;placenta;visual apparatus;testis;parathyroid; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.18771 0.13279 0.125076652 62.7388535 24.39748 0.80257 MAFTRR . . . MAF transcriptional regulator RNA . . . . . . . . . . . MAG 0.540766816780039 0.459102687788933 0.000130495431027576 myelin associated glycoprotein FUNCTION: Adhesion molecule in postnatal neural development that mediates sialic-acid dependent cell-cell interactions between neuronal and myelinating cells. Preferentially binds to alpha-2,3- linked sialic acid (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;hypothalamus;sympathetic chain;parathyroid;uterus;lung;optic nerve;frontal lobe;cerebral cortex;placenta;hippocampus;testis;spinal ganglion;brain; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;caudate nucleus;pons;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.96455 0.26659 -0.196519234 39.20736023 432.98444 4.34233 MAGEA1 0.369816630513072 0.581787981556727 0.0483953879302008 MAGE family member A1 FUNCTION: May be involved in transcriptional regulation through interaction with SNW1 and recruiting histone deactelyase HDAC1. May inhibit notch intracellular domain (NICD) transactivation. May play a role in embryonal development and tumor transformation or aspects of tumor progression. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes. {ECO:0000269|PubMed:15316101}.; . TISSUE SPECIFICITY: Expressed in many tumors of several types, such as melanoma, head and neck squamous cell carcinoma, lung carcinoma and breast carcinoma, but not in normal tissues except for testes. Never expressed in kidney tumors, leukemias and lymphomas.; unclassifiable (Anatomical System);uterus;ovary;larynx;placenta;liver;duodenum;pharynx;head and neck;stomach; superior cervical ganglion;testis;trigeminal ganglion; 0.17288 0.14502 1.104245073 91.95564992 17.59768 0.61643 MAGEA2 . . . MAGE family member A2 FUNCTION: Reduces p53/TP53 transactivation function through recruitment of HDAC3 to p53/TP53 transcription sites. Also represses p73/TP73 activity. Proposed to enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. In vitro enhances ubiquitin ligase activity of TRIM28 and stimulates p53/TP53 ubiquitination by TRIM28 potentially in presence of Ubl-conjugating enzyme UBE2H. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May play a role in embryonal development and tumor transformation or aspects of tumor progression. In vitro promotes cell viability in melanoma cell lines. Antigen recognized on a melanoma by autologous cytolytic T- lymphocytes. Negatively regulates acetylation and sumoylation of PML and represses PML-induced p53/TP53 acetylation and activation. {ECO:0000269|PubMed:16847267, ECO:0000269|PubMed:17942928, ECO:0000269|PubMed:20864041, ECO:0000269|PubMed:22117195}.; . TISSUE SPECIFICITY: Expressed in many tumors of several types, such as melanoma, head and neck squamous cell carcinoma, lung carcinoma and breast carcinoma, but not in normal tissues except for testes.; . . 0.28874 . . . . . MAGEA2B . . . MAGE family member A2B FUNCTION: Reduces p53/TP53 transactivation function through recruitment of HDAC3 to p53/TP53 transcription sites. Also represses p73/TP73 activity. Proposed to enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. In vitro enhances ubiquitin ligase activity of TRIM28 and stimulates p53/TP53 ubiquitination by TRIM28 potentially in presence of Ubl-conjugating enzyme UBE2H. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May play a role in embryonal development and tumor transformation or aspects of tumor progression. In vitro promotes cell viability in melanoma cell lines. Antigen recognized on a melanoma by autologous cytolytic T- lymphocytes. Negatively regulates acetylation and sumoylation of PML and represses PML-induced p53/TP53 acetylation and activation. {ECO:0000269|PubMed:16847267, ECO:0000269|PubMed:17942928, ECO:0000269|PubMed:20864041, ECO:0000269|PubMed:22117195}.; . TISSUE SPECIFICITY: Expressed in many tumors of several types, such as melanoma, head and neck squamous cell carcinoma, lung carcinoma and breast carcinoma, but not in normal tissues except for testes.; unclassifiable (Anatomical System);ovary;salivary gland;adrenal cortex;intestine;pharynx;colon;blood;skin;prostate;lung;bone;placenta;visual apparatus;liver;testis;kidney;brain;mammary gland;bladder; . 0.28874 . . . . . MAGEA3 0.373340458941593 0.579395475954519 0.0472640651038874 MAGE family member A3 FUNCTION: Proposed to enhance ubiquitin ligase activity of RING- type zinc finger-containing E3 ubiquitin-protein ligases. May enhance ubiquitin ligase activity of TRIM28 and stimulate p53/TP53 ubiquitination by TRIM28. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May play a role in embryonal development and tumor transformation or aspects of tumor progression. In vitro promotes cell viability in melanoma cell lines. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes. {ECO:0000269|PubMed:20864041}.; . TISSUE SPECIFICITY: Expressed in many tumors of several types, such as melanoma, head and neck squamous cell carcinoma, lung carcinoma and breast carcinoma, but not in normal tissues except for testes and placenta. Never expressed in kidney tumors, Leukemias and lymphomas.; . . 0.03475 0.16113 -0.069700724 48.54328851 42.69896 1.23918 MAGEA4 0.744658642607292 0.244720467889159 0.0106208895035488 MAGE family member A4 FUNCTION: Not known, though may play a role in embryonal development and tumor transformation or aspects of tumor progression.; . TISSUE SPECIFICITY: Expressed in many tumors of several types, such as melanoma, head and neck squamous cell carcinoma, lung carcinoma and breast carcinoma, but not in normal tissues except for testes and placenta.; unclassifiable (Anatomical System);uterus;lymph node;ovary;larynx;placenta;liver;pharynx;head and neck;skin;stomach; dorsal root ganglion;superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion; 0.08384 0.10552 1.063778722 91.58410002 185.86048 2.95996 MAGEA5 . . . MAGE family member A5 FUNCTION: Not known, though may play a role tumor transformation or progression. In vitro promotes cell viability in melanoma cell lines. {ECO:0000269|PubMed:17942928}.; . . . . 0.06597 . . . . . MAGEA6 0.0941961048529208 0.768396688809994 0.137407206337085 MAGE family member A6 FUNCTION: Proposed to enhance ubiquitin ligase activity of RING- type zinc finger-containing E3 ubiquitin-protein ligases. May enhance ubiquitin ligase activity of TRIM28 and stimulate p53/TP53 ubiquitination by TRIM28. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May play a role in tumor transformation or aspects of tumor progression. In vitro promotes cell viability in melanoma cell lines. {ECO:0000269|PubMed:17942928, ECO:0000269|PubMed:20864041}.; . TISSUE SPECIFICITY: Expressed in many tumors of several types, such as melanoma, head and neck squamous cell carcinoma, lung carcinoma and breast carcinoma, but not in normal tissues except for testes.; unclassifiable (Anatomical System);lymph node;urinary;adrenal cortex;skin;breast;pancreas;prostate;lung;endometrium;bone;placenta;liver;testis;cervix;mammary gland;stomach; . 0.03847 . 0.863528995 88.74144845 400.64495 4.19927 MAGEA7P . . . MAGE family member A7, pseudogene . . . . . . . . . . . MAGEA8 0.238209592292099 0.644852135661235 0.116938272046667 MAGE family member A8 FUNCTION: Not known, though may play a role in embryonal development and tumor transformation or aspects of tumor progression.; . TISSUE SPECIFICITY: Expressed in many tumors of several types, such as melanoma, head and neck squamous cell carcinoma, lung carcinoma and breast carcinoma, but not in normal tissues except for testis and placenta.; unclassifiable (Anatomical System);uterus;endometrium;placenta;skin; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.06491 . 0.439181676 77.69521113 160.38966 2.76342 MAGEA8-AS1 . . . MAGEA8 antisense RNA 1 (head to head) . . . . . . . . . . . MAGEA9 . . . MAGE family member A9 FUNCTION: Not known, though may play a role in embryonal development and tumor transformation or aspects of tumor progression.; . TISSUE SPECIFICITY: Expressed in many tumors of several types, such as melanoma, head and neck squamous cell carcinoma, lung carcinoma and breast carcinoma, but not in normal tissues except for testes and placenta.; unclassifiable (Anatomical System);lymph node;lung;bone;urinary;liver; . 0.06993 0.07295 . . . . MAGEA9B . . . MAGE family member A9B FUNCTION: Not known, though may play a role in embryonal development and tumor transformation or aspects of tumor progression.; . TISSUE SPECIFICITY: Expressed in many tumors of several types, such as melanoma, head and neck squamous cell carcinoma, lung carcinoma and breast carcinoma, but not in normal tissues except for testes and placenta.; unclassifiable (Anatomical System);lymph node;lung;bone;urinary;liver; . . . . . 0.00042 0.00044 MAGEA10 0.305621878891437 0.620060579043199 0.0743175420653639 MAGE family member A10 FUNCTION: Not known, though may play a role in embryonal development and tumor transformation or aspects of tumor progression.; . TISSUE SPECIFICITY: Expressed in many tumors of several types, such as melanoma, head and neck squamous cell carcinoma, lung carcinoma and breast carcinoma, but not in normal tissues except for spermatogonia, spermatocytes and placenta. {ECO:0000269|PubMed:21710496}.; ovary;endometrium;larynx;placenta;adrenal cortex;liver;parathyroid;spleen;head and neck;skin; superior cervical ganglion;atrioventricular node; 0.05870 0.08346 0.260991686 70.25831564 12.88863 0.46998 MAGEA11 0.59454454715929 0.395873622604378 0.00958183023633216 MAGE family member A11 FUNCTION: Acts as androgen receptor coregulator that increases androgen receptor activity by modulating the receptors interdomain interaction. May play a role in embryonal development and tumor transformation or aspects of tumor progression. {ECO:0000269|PubMed:15684378}.; . TISSUE SPECIFICITY: Expressed in tumors of several types, such as melanoma, head and neck squamous cell carcinoma, lung carcinoma and breast carcinoma. Expressed in testis, ovary, prostate, cancerous prostate, breast and adrenal tissue. {ECO:0000269|PubMed:15684378}.; unclassifiable (Anatomical System);uterus;endometrium;bone;placenta; testis - interstitial;appendix;ciliary ganglion;skin;skeletal muscle; 0.18032 0.08078 0.971952656 90.26893135 131.77761 2.49892 MAGEA12 0.700103439261894 0.2833174893144 0.0165790714237061 MAGE family member A12 FUNCTION: Not known, though may play a role tumor transformation or progression. In vitro promotes cell viability in melanoma cell lines. {ECO:0000269|PubMed:17942928}.; . . unclassifiable (Anatomical System);prostate;placenta;liver;mammary gland;skin;stomach; . 0.03847 0.06765 0.060756528 58.52795471 33.0274 1.02284 MAGEA13P . . . MAGE family member A13, pseudogene . . . bone; superior cervical ganglion;ciliary ganglion;skeletal muscle; . . . . . . MAGEB1 0.0701338980445544 0.739012941505745 0.190853160449701 MAGE family member B1 . . TISSUE SPECIFICITY: Expressed only in testis.; . . 0.04619 0.08487 0.238945317 69.20853975 12.09972 0.43842 MAGEB2 0.00647981734401363 0.511622656343357 0.481897526312629 MAGE family member B2 FUNCTION: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. {ECO:0000269|PubMed:20864041}.; . TISSUE SPECIFICITY: Expressed in testis and placenta, and in a significant fraction of tumors of various histologic types.; . . 0.10499 0.08711 0.240763792 69.36777542 33.06343 1.02368 MAGEB3 0.66135267930598 0.315301112171769 0.0233462085222503 MAGE family member B3 . . TISSUE SPECIFICITY: Expressed in testis.; lung;testis; superior cervical ganglion;temporal lobe;globus pallidus;trigeminal ganglion; 0.03566 0.07810 1.060147109 91.46614768 11.36417 0.40953 MAGEB4 0.25505460782301 0.640620972320914 0.104324419856076 MAGE family member B4 . . TISSUE SPECIFICITY: Expressed in testis.; . . 0.02758 0.08448 -0.159704656 41.90846898 10.07341 0.36801 MAGEB5 0.114589765510266 0.602266239923126 0.283143994566608 MAGE family member B5 . . TISSUE SPECIFICITY: Expressed in testis. Not expressed in other normal tissues, but is expressed in tumors of different histological origins.; . . 0.02039 . . . 25.56137 0.83313 MAGEB6 0.386744087189912 0.570067568037765 0.043188344772323 MAGE family member B6 . . TISSUE SPECIFICITY: Expressed in testis. Not expressed in other normal tissues, but is expressed in tumors of different histological origins. {ECO:0000269|PubMed:10861452}.; . . 0.06211 . 0.576916344 82.25406936 488.31042 4.54874 MAGEB6P1 . . . MAGE family member B6 pseudogene 1 . . . . . . . . . . . MAGEB10 0.710701863627324 0.274301941845482 0.0149961945271949 MAGE family member B10 . . . . . 0.04559 . 1.502961964 95.39985846 128.01054 2.46628 MAGEB16 0.00166368220637961 0.462152092087568 0.536184225706053 MAGE family member B16 . . . . . . . 1.370655714 94.47393253 17.15182 0.60288 MAGEB17 0.0284362734443786 0.581870784450937 0.389692942104684 MAGE family member B17 . . . unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skin;skeletal muscle; . . . . 21.04355 0.71269 MAGEB18 0.040371281052756 0.650501680367259 0.309127038579985 MAGE family member B18 FUNCTION: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. {ECO:0000269|PubMed:20864041}.; . . unclassifiable (Anatomical System);testis; . 0.04525 0.08144 0.17280645 65.75843359 9.48328 0.34968 MAGEC1 . . . MAGE family member C1 . . TISSUE SPECIFICITY: Expressed in testis and in tumors of a wide variety of histologic types.; unclassifiable (Anatomical System);bone;testis;skin;stomach; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.03644 . 6.421180534 99.87025242 4106.66315 12.72208 MAGEC2 0.659070496768636 0.317133596143724 0.0237959070876394 MAGE family member C2 FUNCTION: Proposed to enhance ubiquitin ligase activity of RING- type zinc finger-containing E3 ubiquitin-protein ligases. In vitro enhances ubiquitin ligase activity of TRIM28 and stimulates p53/TP53 ubiquitination in presence of Ubl-conjugating enzyme UBE2H leading to p53/TP53 degradation. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzymes (E2) at the E3:substrate complex. {ECO:0000269|PubMed:20864041}.; . TISSUE SPECIFICITY: Not expressed in normal tissues, except in germ cells in the seminiferous tubules and in Purkinje cells of the cerebellum. Expressed in various tumors, including melanoma, lymphoma, as well as pancreatic cancer, mammary gland cancer, non- small cell lung cancer and liver cancer. In hepatocellular carcinoma, there is a inverse correlation between tumor differentiation and protein expression, i.e. the lower the differentiation, the higher percentage of expression. {ECO:0000269|PubMed:12097419, ECO:0000269|PubMed:12920247}.; unclassifiable (Anatomical System);medulla oblongata;lung;endometrium;bone;placenta;testis;skin; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis; 0.03033 0.10467 -0.181750739 40.15687662 31.54815 0.99315 MAGEC3 3.2490215491358e-08 0.175600217225979 0.824399750283806 MAGE family member C3 . . TISSUE SPECIFICITY: Expressed in testis. Not expressed in other normal tissues, but is expressed in tumors of different histological origins. {ECO:0000269|PubMed:10861452}.; . . 0.05794 . 1.35769336 94.43854683 803.76941 5.58529 MAGED1 0.982074597200181 0.0179229232018931 2.47959792610178e-06 MAGE family member D1 FUNCTION: Involved in the apoptotic response after nerve growth factor (NGF) binding in neuronal cells. Inhibits cell cycle progression, and facilitates NGFR-mediated apoptosis. May act as a regulator of the function of DLX family members. May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. Plays a role in the circadian rythm regulation. May act as RORA co-regulator, modulating the expression of core clock genes such as ARNTL/BMAL1 and NFIL3, induced, or NR1D1, repressed. {ECO:0000269|PubMed:20864041}.; . TISSUE SPECIFICITY: Expressed in bone marrow stromal cells from both multiple myeloma patients and healthy donors. Seems to be ubiquitously expressed.; lymphoreticular;ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;trophoblast;tongue;islets of Langerhans;muscle;lens;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;amnion;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;globus pallidus;parietal lobe;cerebellum; 0.32948 0.13624 -0.53631094 20.53550366 20.0446 0.68452 MAGED2 0.989729719490781 0.0102671610542663 3.11945495280764e-06 MAGE family member D2 . . TISSUE SPECIFICITY: Widely expressed in normal tissues.; lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;brain;gall bladder;tonsil;heart;cartilage;urinary;adrenal cortex;blood;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;synovium;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; . 0.51282 0.12075 -0.22584292 37.32012267 135.88459 2.53380 MAGED4 . . . MAGE family member D4 FUNCTION: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. {ECO:0000269|PubMed:20864041}.; . TISSUE SPECIFICITY: Expressed only in brain and ovary among normal tissues. Isoform 1 and isoform 2 are specifically expressed in glioma cells among cancer cells. Detected in some renal cell carcinoma samples. {ECO:0000269|PubMed:11406556, ECO:0000269|PubMed:16082191}.; . . . 0.10288 . . . . MAGED4B . . . MAGE family member D4B FUNCTION: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. {ECO:0000269|PubMed:20864041}.; . TISSUE SPECIFICITY: Expressed only in brain and ovary among normal tissues. Isoform 1 and isoform 2 are specifically expressed in glioma cells among cancer cells. Detected in some renal cell carcinoma samples. {ECO:0000269|PubMed:11406556, ECO:0000269|PubMed:16082191}.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;urinary;adrenal cortex;blood;lens;bile duct;pancreas;lung;placenta;visual apparatus;hypopharynx;spleen;head and neck;kidney;aorta;peripheral nerve; . . 0.10288 . . . . MAGEE1 0.699601223364713 0.296642831082961 0.00375594555232654 MAGE family member E1 FUNCTION: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. {ECO:0000269|PubMed:20864041}.; . . unclassifiable (Anatomical System);lymph node;lung;whole body;frontal lobe;ovary;cochlea;brain;retina; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;parietal lobe;cerebellum; 0.15502 0.10822 0.86534717 88.80042463 205.68788 3.09823 MAGEE2 1.52942226417517e-08 0.0616379246048891 0.938362060100888 MAGE family member E2 . . . . . 0.08950 . -0.200157416 39.11299835 3295.15538 10.96255 MAGEF1 0.0340314663613953 0.823845441571544 0.14212309206706 MAGE family member F1 FUNCTION: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. {ECO:0000269|PubMed:20864041}.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;spleen;kidney;mammary gland;stomach; amygdala;whole brain;thalamus;subthalamic nucleus;occipital lobe;cerebellum peduncles;globus pallidus;parietal lobe;cingulate cortex;pituitary;cerebellum; 0.05747 0.09580 1.150157577 92.46874263 2416.7128 9.13290 MAGEH1 0.338067798966747 0.602083949375113 0.0598482516581402 MAGE family member H1 . . . ovary;sympathetic chain;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;cerebral cortex;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;urinary;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;hippocampus;alveolus;spleen;kidney;mammary gland;stomach;aorta;thymus; amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;hypothalamus;caudate nucleus;pons;subthalamic nucleus;testis;cingulate cortex;parietal lobe;cerebellum; 0.22272 0.14229 -0.031067188 51.03798066 4.92607 0.18277 MAGEL2 0.922411269035569 0.0774927265392641 9.60044251669369e-05 MAGE family member L2 FUNCTION: Probably enhances ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases, possibly through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. Acts as a regulator of retrograde transport via its interaction with VPS35. Recruited to retromer-containing endosomes and promotes the formation of 'Lys- 63'-linked polyubiquitin chains at 'Lys-220' of WASH1 together with TRIM27, leading to promote endosomal F-actin assembly (PubMed:23452853). Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Significantly promotes the cytoplasmic accumulation of CLOCK (By similarity). {ECO:0000250|UniProtKB:Q9QZ04, ECO:0000269|PubMed:20864041, ECO:0000269|PubMed:23452853}.; . TISSUE SPECIFICITY: Expressed in placenta, fetal and adult brain. Not detected in heart and small intestine, very low levels in fibroblasts. Not expressed in brain of a Prader-Willi patient. {ECO:0000269|PubMed:10915770}.; . . . . . . 653.05336 5.12739 MAGI1 0.999615674506819 0.000384325493178334 2.89260951151553e-15 membrane associated guanylate kinase, WW and PDZ domain containing 1 FUNCTION: May play a role as scaffolding protein at cell-cell junctions. May regulate acid-induced ASIC3 currents by modulating its expression at the cell surface (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed with the exception of skeletal muscle. Isoform 1, isoform 2 and isoform 6 are highly expressed in colon, kidney, lung, liver, and pancreas. Isoform 5 is predominantly expressed in brain and heart. Isoform 3 and isoform 4 are highly expressed in pancreas and brain. {ECO:0000269|PubMed:11969287, ECO:0000269|PubMed:9647693, ECO:0000269|PubMed:9647739}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;fovea centralis;choroid;lens;retina;breast;prostate;optic nerve;lung;frontal lobe;trabecular meshwork;macula lutea;testis;brain;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;skeletal muscle;skin;globus pallidus;testis;ciliary ganglion;kidney;trigeminal ganglion;cingulate cortex;parietal lobe; 0.27232 0.12487 -1.383523256 4.358339231 581.76428 4.88893 MAGI1-AS1 . . . MAGI1 antisense RNA 1 . . . . . . . . . . . MAGI1-IT1 . . . MAGI1 intronic transcript 1 . . . . . . . . . . . MAGI2 0.883174386756098 0.116825612463389 7.80512906286322e-10 membrane associated guanylate kinase, WW and PDZ domain containing 2 FUNCTION: Seems to act as scaffold molecule at synaptic junctions by assembling neurotransmitter receptors and cell adhesion proteins. May play a role in regulating activin-mediated signaling in neuronal cells. Enhances the ability of PTEN to suppress AKT1 activation. Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth. {ECO:0000269|PubMed:10760291}.; . TISSUE SPECIFICITY: Specifically expressed in brain. {ECO:0000269|PubMed:9647693}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;cerebral cortex;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; whole brain;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cerebellum; 0.97884 0.10801 -2.076219205 1.598254305 91.7652 2.06070 MAGI2-AS1 . . . MAGI2 antisense RNA 1 . . . . . . . . . . . MAGI2-AS2 . . . MAGI2 antisense RNA 2 . . . . . . . . . . . MAGI2-AS3 . . . MAGI2 antisense RNA 3 . . . . . . . . . . . MAGI2-IT1 . . . MAGI2 intronic transcript 1 . . . . . . . . . . . MAGI3 0.570580157400499 0.42941983555302 7.04648048277631e-09 membrane associated guanylate kinase, WW and PDZ domain containing 3 FUNCTION: Acts as a scaffolding protein at cell-cell junctions, thereby regulating various cellular and signaling processes. Cooperates with PTEN to modulate the kinase activity of AKT1. Its interaction with PTPRB and tyrosine phosphorylated proteins suggests that it may link receptor tyrosine phosphatase with its substrates at the plasma membrane. In polarized epithelial cells, involved in efficient trafficking of TGFA to the cell surface. Regulates the ability of LPAR2 to activate ERK and RhoA pathways. Regulates the JNK signaling cascade via its interaction with FZD4 and VANGL2. {ECO:0000269|PubMed:10748157}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10748157}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;endometrium;thyroid;pituitary gland;testis;unclassifiable (Anatomical System);heart;pineal body;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;spleen;kidney;aorta; dorsal root ganglion;medulla oblongata;superior cervical ganglion;tongue;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.93064 0.10933 -0.925889687 9.754659118 136.27247 2.53739 MAGIX 0.0035921864657483 0.625416795910127 0.370991017624124 MAGI family member, X-linked . . . . . 0.03257 . . . 194.95324 3.02676 MAGOH 0.747938336088651 0.249816163740766 0.00224550017058258 mago homolog, exon junction complex core component FUNCTION: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP- bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly. {ECO:0000269|PubMed:12730685, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:22203037}.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.35556 0.12378 0.101211609 60.95777306 2.7415 0.09814 MAGOH2P . . . mago homolog 2, pseudogene . . . . . . . . . . . MAGOH3P . . . mago homolog 3, pseudogene . . . . . . . . . . . MAGOHB 0.0417829970477984 0.845468201323053 0.112748801629148 mago homolog B, exon junction complex core component FUNCTION: Involved in mRNA splicing and in the nonsense-mediated decay (NMD) pathway. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;bone;testis;brain;bladder;unclassifiable (Anatomical System);lacrimal gland;pharynx;blood;skeletal muscle;bile duct;breast;lung;cornea;adrenal gland;placenta;visual apparatus;liver;alveolus;cervix;kidney;mammary gland; cingulate cortex; 0.19666 0.10951 -0.053113545 49.38664779 . . MAGT1 0.887373875952856 0.112375163972092 0.000250960075051961 magnesium transporter 1 FUNCTION: May be involved in N-glycosylation through its association with N-oligosaccharyl transferase. May be involved in Mg(2+) transport in epithelial cells. {ECO:0000269|PubMed:15804357, ECO:0000269|PubMed:19717468}.; DISEASE: Immunodeficiency, X-linked, with magnesium defect, Epstein-Barr virus infection and neoplasia (XMEN) [MIM:300853]: A disease characterized by CD4 lymphopenia, severe chronic viral infections, and defective T-lymphocyte activation. {ECO:0000269|PubMed:21796205}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Expressed at very low levels in brain, lung and kidney. {ECO:0000269|PubMed:12887896, ECO:0000269|PubMed:15804357, ECO:0000269|PubMed:19717468}.; myocardium;smooth muscle;ovary;salivary gland;developmental;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;endometrium;synovium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;nervous;islets of Langerhans;oral cavity;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;thyroid;trigeminal ganglion; 0.11770 0.07889 0.104848986 61.49445624 25.04667 0.82051 MAK 9.62965218458322e-11 0.275710383432831 0.724289616470872 male germ cell associated kinase FUNCTION: Essential for the regulation of ciliary length and required for the long-term survival of photoreceptors (By similarity). Phosphorylates FZR1 in a cell cycle-dependent manner. Plays a role in the transcriptional coactivation of AR. Could play an important function in spermatogenesis. May play a role in chromosomal stability in prostate cancer cells. {ECO:0000250, ECO:0000269|PubMed:12084720, ECO:0000269|PubMed:16951154, ECO:0000269|PubMed:21986944}.; DISEASE: Retinitis pigmentosa 62 (RP62) [MIM:614181]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:21825139, ECO:0000269|PubMed:21835304}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in prostate cancer cell lines at generally higher levels than in normal prostate epithelial cell lines. Isoform 1 is expressed in kidney, testis, lung, trachea, and retina. Isoform 2 is retina-specific where it is expressed in rod and cone photoreceptors. {ECO:0000269|PubMed:12084720, ECO:0000269|PubMed:21825139}.; unclassifiable (Anatomical System);smooth muscle;heart;colon;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;optic nerve;lung;placenta;macula lutea;testis;germinal center;kidney; superior cervical ganglion;trigeminal ganglion;whole blood;skeletal muscle; 0.21288 0.10049 -0.356299879 29.31115829 211.0774 3.13327 MAK16 0.993980456078529 0.00601937306514698 1.70856324304438e-07 MAK16 homolog . . . ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.16311 0.09662 -0.337894035 30.37272942 391.2138 4.16379 MAL 0.78607902501438 0.207357317947645 0.0065636570379748 mal T-cell differentiation protein FUNCTION: Could be an important component in vesicular trafficking cycling between the Golgi complex and the apical plasma membrane. Could be involved in myelin biogenesis and/or myelin function.; . . ovary;umbilical cord;salivary gland;intestine;colon;choroid;skin;retina;uterus;prostate;frontal lobe;cochlea;oesophagus;iris;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;oral cavity;pharynx;blood;lens;breast;lung;placenta;visual apparatus;hippocampus;hypopharynx;liver;head and neck;kidney;stomach;aorta; dorsal root ganglion;olfactory bulb;tongue;spinal cord;kidney;caudate nucleus;parietal lobe; 0.18211 0.11902 -0.117432389 44.89266336 27.99238 0.89873 MAL2 0.458862107533214 0.514784598776585 0.0263532936902006 mal, T-cell differentiation protein 2 (gene/pseudogene) FUNCTION: Member of the machinery of polarized transport. Required for the indirect transcytotic route at the step of the egress of the transcytosing cargo from perinuclear endosomes in order for it to travel to the apical surface via a raft-dependent pathway. {ECO:0000269|PubMed:12370246}.; . TISSUE SPECIFICITY: Predominantly expressed in kidney, lung, and liver. Also found in thyroid gland, stomach and, at lower levels in testis and small intestine. {ECO:0000269|PubMed:11549320, ECO:0000269|PubMed:14576188}.; ovary;colon;parathyroid;bone marrow;uterus;prostate;whole body;endometrium;larynx;gum;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;breast;bile duct;pancreas;lung;placenta;amnion;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; thyroid; 0.66923 0.13327 . . 880.08654 5.77834 MALAT1 . . . metastasis associated lung adenocarcinoma transcript 1 (non-protein coding) . . . . . . . . . . . MALL 0.201463447177582 0.648012983515239 0.150523569307179 mal, T-cell differentiation protein-like . . . smooth muscle;ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;oesophagus;larynx;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;breast;pancreas;lung;mesenchyma;placenta;visual apparatus;liver;hypopharynx;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;tongue;trigeminal ganglion; 0.14473 0.18418 . . 3.30761 0.12068 MALRD1 . . . MAM and LDL receptor class A domain containing 1 . . . . . 0.14308 0.08110 . . 9167.21724 20.81809 MALSU1 1.78046134626036e-08 0.0353834147431926 0.964616567452194 mitochondrial assembly of ribosomal large subunit 1 FUNCTION: May function as a ribosomal silencing factor. Addition to isolated mitochondrial ribosomal subunits partially inhibits translation. Interacts with mitochondrial ribosomal protein L14 (MRPL14), probably blocking formation of intersubunit bridge B8, preventing association of the 28S and 39S ribosomal subunits and the formation of functional ribosomes, thus repressing translation. May also participate in the assembly and/or regulation of the stability of the large subunit of the mitochondrial ribosome. {ECO:0000269|PubMed:22238376}.; . . . . 0.03417 0.09065 -0.516085732 21.20193442 28.96376 0.92557 MALT1 0.994144577983795 0.00585541547742824 6.53877673411335e-09 MALT1 paracaspase FUNCTION: Enhances BCL10-induced activation of NF-kappa-B. Involved in nuclear export of BCL10. Binds to TRAF6, inducing TRAF6 oligomerization and activation of its ligase activity. Has ubiquitin ligase activity. MALT1-dependent BCL10 cleavage plays an important role in T-cell antigen receptor-induced integrin adhesion. {ECO:0000269|PubMed:11262391, ECO:0000269|PubMed:14695475, ECO:0000269|PubMed:18264101}.; DISEASE: Note=A chromosomal aberration involving MALT1 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(11;18)(q21;q21) with BIRC2. This translocation is found in approximately 50% of cytogenetically abnormal low-grade MALT lymphoma. {ECO:0000269|PubMed:10339464, ECO:0000269|PubMed:10523859, ECO:0000269|PubMed:10702396, ECO:0000269|PubMed:11090634}.; TISSUE SPECIFICITY: Highly expressed in peripheral blood mononuclear cells. Detected at lower levels in bone marrow, thymus and lymph node, and at very low levels in colon and lung.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;urinary;colon;skeletal muscle;breast;bile duct;prostate;pancreas;lung;endometrium;bone;placenta;visual apparatus;liver;testis;spleen;germinal center;kidney;mammary gland;artery;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;tumor;white blood cells;ciliary ganglion;atrioventricular node;tonsil;skeletal muscle; 0.14206 0.16644 -0.135838822 43.77211607 105.10537 2.21841 MAMDC2 0.00417147485342542 0.99551351116411 0.000315013982464913 MAM domain containing 2 . . . . . 0.24293 0.10608 0.224175308 68.48903043 1026.20998 6.15638 MAMDC2-AS1 . . . MAMDC2 antisense RNA 1 . . . . . . . . . . . MAMDC4 2.5961065070387e-35 7.02181015239044e-07 0.999999297818985 MAM domain containing 4 FUNCTION: Probably involved in the sorting and selective transport of receptors and ligands across polarized epithelia. {ECO:0000250|UniProtKB:Q63191}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;parathyroid;uterus;whole body;lung;optic nerve;endometrium;placenta;liver;testis;brain; liver;atrioventricular node;trigeminal ganglion; 0.14516 0.10004 1.886893658 97.2811984 675.66597 5.19223 MAML1 0.998362055817934 0.00163790895173724 3.52303291697343e-08 mastermind like transcriptional coactivator 1 FUNCTION: Acts as a transcriptional coactivator for NOTCH proteins. Has been shown to amplify NOTCH-induced transcription of HES1. Enhances phosphorylation and proteolytic turnover of the NOTCH intracellular domain in the nucleus through interaction with CDK8. Binds to CREBBP/CBP which promotes nucleosome acetylation at NOTCH enhancers and activates transcription. Induces phosphorylation and localization of CREBBP to nuclear foci. Plays a role in hematopoietic development by regulating NOTCH-mediated lymphoid cell fate decisions. {ECO:0000269|PubMed:11101851, ECO:0000269|PubMed:11390662, ECO:0000269|PubMed:12050117, ECO:0000269|PubMed:15546612, ECO:0000269|PubMed:17317671}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in heart, pancreas, peripheral blood leukocytes and spleen. {ECO:0000269|PubMed:11101851}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;medulla oblongata;prefrontal cortex;pons;trigeminal ganglion;cerebellum; 0.56824 0.10646 0.229636184 68.56569946 1245.10841 6.66424 MAML2 0.998525114326019 0.00147488455688672 1.11709469550226e-09 mastermind like transcriptional coactivator 2 FUNCTION: Acts as a transcriptional coactivator for NOTCH proteins. Has been shown to amplify NOTCH-induced transcription of HES1. Potentiates activation by NOTCH3 and NOTCH4 more efficiently than MAML1 or MAML3. {ECO:0000269|PubMed:12370315, ECO:0000269|PubMed:12386158, ECO:0000269|PubMed:12539049}.; DISEASE: Note=A chromosomal aberration involving MAML2 is found in mucoepidermoid carcinomas, benign Warthin tumors and clear cell hidradenomas. Translocation t(11;19)(q21;p13) with CRTC1. The fusion protein consists of the N-terminus of CRTC1 joined to the C-terminus of MAML2. The reciprocal fusion protein consisting of the N-terminus of MAML2 joined to the C-terminus of CRTC1 has been detected in a small number of mucoepidermoid carcinomas. {ECO:0000269|PubMed:15729701}.; TISSUE SPECIFICITY: Widely expressed with high levels detected in placenta, salivary gland and skeletal muscle. {ECO:0000269|PubMed:14720503}.; . . 0.28735 0.13371 0.207589927 67.52182118 1240.98759 6.64881 MAML3 0.32989504838315 0.670077664581583 2.72870352662948e-05 mastermind like transcriptional coactivator 3 FUNCTION: Acts as a transcriptional coactivator for NOTCH proteins. Has been shown to amplify NOTCH-induced transcription of HES1. {ECO:0000269|PubMed:12370315, ECO:0000269|PubMed:12386158}.; . . unclassifiable (Anatomical System);visual apparatus;colon;germinal center; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.24850 0.10364 0.029399861 55.83274357 1196.42907 6.56243 MAMLD1 0.840109494669231 0.159255787834181 0.00063471749658808 mastermind like domain containing 1 FUNCTION: Transactivates the HES3 promoter independently of NOTCH proteins. HES3 is a non-canonical NOTCH target gene which lacks binding sites for RBPJ. {ECO:0000269|PubMed:18162467}.; DISEASE: Hypospadias 2, X-linked (HYSP2) [MIM:300758]: A common malformation in which the urethra opens on the ventral side of the penis, due to developmental arrest of urethral fusion. The opening can be located glandular, penile, or even more posterior in the scrotum or perineum. Hypospadias is a feature of several syndromic disorders, including the androgen insensitivity syndrome and Opitz syndrome. {ECO:0000269|PubMed:17086185}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in fetal brain, fetal ovary and fetal testis. Expressed in adult brain, ovary, skin, testis, uterus. Highly expressed in skeletal muscle. {ECO:0000269|PubMed:18162467}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;liver;spleen;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.71086 0.14494 . . 250.34255 3.40814 MAMSTR 0.00123325809401916 0.635915779609763 0.362850962296218 MEF2 activating motif and SAP domain containing transcriptional regulator FUNCTION: Transcriptional coactivator. Stimulates the transcriptional activity of MEF2C. Stimulates MYOD1 activity in part via MEF2, resulting in an enhancement of skeletal muscle differentiation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, brain, placenta and spleen. {ECO:0000269|PubMed:16818234}.; lung;whole body;ovary;bone;visual apparatus;duodenum;brain;stomach;skin; . . . -0.227663163 37.11370606 125.24327 2.43582 MAN1A1 0.803866877079253 0.196123819610013 9.30331073416279e-06 mannosidase alpha class 1A member 1 FUNCTION: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).; . . . . 0.03949 0.10316 -0.468351206 23.42533616 52.98086 1.44514 MAN1A2 0.996263145196637 0.00373684401482372 1.07885390080065e-08 mannosidase alpha class 1A member 2 FUNCTION: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).; . TISSUE SPECIFICITY: Highest levels of expression in placenta and testis.; ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;hypopharynx;head and neck;cervix;kidney;mammary gland;aorta;peripheral nerve;cerebellum; occipital lobe;superior cervical ganglion;placenta;prefrontal cortex;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex; 0.50876 0.10038 0.018483465 55.44939844 62.48727 1.61473 MAN1A2P1 . . . mannosidase alpha class 1A member 2 pseudogene 1 . . . . . . . . . . . MAN1B1 2.62916999838095e-06 0.916062053229839 0.0839353176001631 mannosidase alpha class 1B member 1 FUNCTION: Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2). {ECO:0000269|PubMed:12090241, ECO:0000269|PubMed:18003979}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10409699, ECO:0000269|PubMed:10521544}.; . . 0.31651 . 0.187364432 66.28921916 . . MAN1B1-AS1 . . . MAN1B1 antisense RNA 1 (head to head) . . . . . . . . . . . MAN1C1 0.0490480402547963 0.950752127269844 0.00019983247535918 mannosidase alpha class 1C member 1 FUNCTION: Involved in the maturation of Asn-linked oligosaccharides. Trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce first Man(8)GlcNAc(2) then Man(6)GlcNAc and a small amount of Man(5)GlcNAc.; . TISSUE SPECIFICITY: Expressed in most tissues with the exception of lung, muscle and pancreas. Highly expressed in placenta.; ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);islets of Langerhans;adrenal cortex;lens;pancreas;lung;epididymis;placenta;macula lutea;liver;spleen;kidney;stomach; superior cervical ganglion;placenta;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;cerebellum; 0.15248 0.10921 -0.466531444 23.51380042 215.96008 3.17320 MAN2A1 0.0186444331521237 0.981355273225412 2.9362246399254e-07 mannosidase alpha class 2A member 1 FUNCTION: Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway.; . . medulla oblongata;ovary;colon;parathyroid;skin;retina;bone marrow;prostate;whole body;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);urinary;skeletal muscle;bile duct;breast;pancreas;lung;placenta;liver;duodenum;spleen;kidney;stomach; medulla oblongata;occipital lobe;prefrontal cortex;cingulate cortex;parietal lobe; 0.49831 0.29427 -1.565353375 3.202406228 3122.10723 10.62155 MAN2A2 3.60787631910875e-09 0.999239909906014 0.000760086486110081 mannosidase alpha class 2A member 2 FUNCTION: Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pineal body;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; trigeminal ganglion;cingulate cortex;skeletal muscle; 0.13322 0.11297 -1.447883661 3.927813163 1132.88434 6.42184 MAN2B1 1.56344757218082e-12 0.92819683187995 0.0718031681184867 mannosidase alpha class 2B member 1 FUNCTION: Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. Cleaves all known types of alpha-mannosidic linkages.; DISEASE: Mannosidosis, alpha B, lysosomal (MANSA) [MIM:248500]: A lysosomal storage disease characterized by accumulation of unbranched oligosaccharide chains. This accumulation is expressed histologically as cytoplasmic vacuolation predominantly in the CNS and parenchymatous organs. Depending on the clinical findings at the age of onset, a severe infantile (type I) and a mild juvenile (type II) form of alpha-mannosidosis are recognized. There is considerable variation in the clinical expression with mental retardation, recurrent infections, impaired hearing and Hurler- like skeletal changes being the most consistent abnormalities. {ECO:0000269|PubMed:12718372, ECO:0000269|PubMed:15712269, ECO:0000269|PubMed:22161967, ECO:0000269|PubMed:9158146, ECO:0000269|PubMed:9758606, ECO:0000269|PubMed:9915946}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;breast;bile duct;pancreas;lung;adrenal gland;mesenchyma;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;white blood cells;whole blood; 0.06035 0.22441 0.121225147 62.22576079 2735.34889 9.86188 MAN2B2 4.35731486928261e-18 0.0380467275348678 0.961953272465132 mannosidase alpha class 2B member 2 . . . colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;thyroid;bone;iris;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;urinary;lens;breast;lung;placenta;macula lutea;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; . 0.11522 0.16871 2.377654115 98.46661949 4293.60359 13.02320 MAN2C1 2.94181816484649e-25 0.00043587592635208 0.999564124073648 mannosidase alpha class 2C member 1 . . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;larynx;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.25399 0.26675 -0.095604385 46.20783204 574.28122 4.86436 MANBA 1.14972215660264e-11 0.727297950817334 0.272702049171168 mannosidase beta FUNCTION: Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of all N-linked glycoprotein oligosaccharides.; DISEASE: Mannosidosis, beta A, lysosomal (MANSB) [MIM:248510]: An autosomal recessive lysosomal storage disease of glycoprotein catabolism. Clinical features are heterogeneous with a wide range of symptoms and age of onset. The disease is associated with a range of neurological involvement, including various degrees of mental retardation in most of the cases, hearing loss and speech impairment, hypotonia, epilepsy and peripheral neuropathy. Affected individuals have a profound reduction in beta A mannosidase activity in plasma, fibroblasts and leukocytes. {ECO:0000269|PubMed:9384606}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;oesophagus;endometrium;larynx;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;liver;amnion;spleen;head and neck;kidney;stomach;cerebellum; . 0.10723 0.33098 -0.615405356 17.47464025 1194.85123 6.55841 MANBAL 0.169240549562547 0.641869694951406 0.188889755486048 mannosidase beta like . . . . . 0.19019 . -0.09720619 46.20193442 8.93109 0.32855 MANEA 0.000414997365079232 0.854028007033884 0.145556995601037 mannosidase endo-alpha . . TISSUE SPECIFICITY: Highly expressed in the liver and kidney. Expressed at lower levels in muscle, pancreas, heart, placenta, lung and brain. {ECO:0000269|PubMed:15677381}.; ovary;colon;parathyroid;skin;bone marrow;uterus;endometrium;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;adrenal cortex;skeletal muscle;lung;nasopharynx;trabecular meshwork;placenta;hippocampus;visual apparatus;liver;spleen;kidney; superior cervical ganglion;trigeminal ganglion; 0.47462 0.10826 0.132352165 63.48785091 1247.59973 6.67042 MANEA-AS1 . . . MANEA antisense RNA 1 (head to head) . . . . . . . . . . . MANEAL 0.00438904419096243 0.869856678028845 0.125754277780193 mannosidase endo-alpha like . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;pituitary gland;testis;brain;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.69800 0.12971 -0.227663163 37.11370606 140.7447 2.58867 MANF 0.327002524454327 0.60856209040644 0.0644353851392325 mesencephalic astrocyte derived neurotrophic factor FUNCTION: Selectively promotes the survival of dopaminergic neurons of the ventral mid-brain. Modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. Enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons (By similarity). Inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death. {ECO:0000250, ECO:0000269|PubMed:12794311, ECO:0000269|PubMed:18561914}.; . . . . 0.28503 0.13484 -0.009020804 52.8544468 7.01241 0.26247 MANSC1 0.000352735755361128 0.605908441706491 0.393738822538148 MANSC domain containing 1 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11896457}.; unclassifiable (Anatomical System);cartilage;lacrimal gland;islets of Langerhans;adrenal cortex;colon;blood;skin;skeletal muscle;retina;bone marrow;uterus;lung;endometrium;nasopharynx;thyroid;placenta;visual apparatus;duodenum;liver;testis;spleen;brain;stomach; superior cervical ganglion;trigeminal ganglion; 0.21982 0.07670 0.110306132 62.00165133 322.59341 3.81394 MANSC4 . . . MANSC domain containing 4 . . . . . . . 0.525552348 80.57914603 701.87819 5.26924 MAOA 0.993222490508762 0.00677638143562597 1.12805561227422e-06 monoamine oxidase A FUNCTION: Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine.; DISEASE: Brunner syndrome (BRUNS) [MIM:300615]: A form of X-linked non-dysmorphic mild mental retardation. Male patients are affected by borderline mental retardation and exhibit abnormal behavior, including disturbed regulation of impulsive aggression. Obligate female carriers have normal intelligence and behavior. {ECO:0000269|PubMed:8211186}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Heart, liver, duodenum, blood vessels and kidney.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;bladder;brain;tonsil;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;testis;spinal ganglion;unclassifiable (Anatomical System);small intestine;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;kidney;stomach; superior cervical ganglion;adipose tissue;thyroid;placenta;ciliary ganglion;atrioventricular node;kidney; 0.08627 . -0.139478553 43.29440906 17.16659 0.60339 MAOB 0.970339617070938 0.0296517838534074 8.59907565467876e-06 monoamine oxidase B FUNCTION: Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine.; . . . . 0.50272 0.48057 -0.626318434 17.03231894 20.86837 0.70615 MAP1A 0.999688997602479 0.000311002397312926 2.08464013886132e-13 microtubule associated protein 1A FUNCTION: Structural protein involved in the filamentous cross- bridging between microtubules and other skeletal elements.; . TISSUE SPECIFICITY: Brain.; ovary;sympathetic chain;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;cerebellum cortex;tongue;nervous;hypothalamus;spinal cord;muscle;lens;skeletal muscle;breast;lung;cornea;epididymis;placenta;macula lutea;hippocampus;hypopharynx;amnion;head and neck;stomach; whole brain;amygdala;dorsal root ganglion;thalamus;superior cervical ganglion;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.83227 0.19426 1.159219819 92.61028544 6409.37455 16.76427 MAP1B 0.999986247796098 1.3752203901724e-05 5.17235865024753e-16 microtubule associated protein 1B FUNCTION: Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B may play a role in the cytoskeletal changes that accompany neurite extension. Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269|PubMed:18195017}.; . . smooth muscle;ovary;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;ganglion;frontal lobe;endometrium;bone;testis;amniotic fluid;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);amygdala;trophoblast;cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;hypothalamus;spinal cord;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;aorta;peripheral nerve; amygdala;subthalamic nucleus;occipital lobe;fetal brain;cerebellum peduncles;globus pallidus;ciliary ganglion;pons;parietal lobe;cingulate cortex;cerebellum; 0.92753 0.37282 -2.216367922 1.350554376 286.31145 3.62263 MAP1LC3A 0.739731534985187 0.249075138104472 0.0111933269103412 microtubule associated protein 1 light chain 3 alpha FUNCTION: Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. {ECO:0000269|PubMed:20713600}.; . TISSUE SPECIFICITY: Most abundant in heart, brain, liver, skeletal muscle and testis but absent in thymus and peripheral blood leukocytes. {ECO:0000269|PubMed:12740394}.; colon;fovea centralis;skin;retina;uterus;prostate;optic nerve;frontal lobe;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;muscle;pancreas;lung;hippocampus;macula lutea;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; . 0.09841 0.09617 -0.009020804 52.8544468 1.17647 0.03321 MAP1LC3B 0.0617608767755467 0.869383451410605 0.0688556718138482 microtubule associated protein 1 light chain 3 beta FUNCTION: Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway. {ECO:0000269|PubMed:20418806, ECO:0000269|PubMed:23209295, ECO:0000269|PubMed:24089205}.; . TISSUE SPECIFICITY: Most abundant in heart, brain, skeletal muscle and testis. Little expression observed in liver. {ECO:0000269|PubMed:12740394}.; ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;spinal cord;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;small intestine;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;cerebellum; whole brain;amygdala;subthalamic nucleus;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;parietal lobe;cerebellum; 0.20660 0.11809 0.147123112 64.11299835 37.98673 1.12808 MAP1LC3B2 0.0237056854362151 0.772253270998396 0.204041043565389 microtubule associated protein 1 light chain 3 beta 2 FUNCTION: Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;hypothalamus;colon;parathyroid;skin;prostate;pancreas;whole body;lung;larynx;placenta;liver;testis;head and neck;spleen;germinal center;kidney;brain; . . . 0.571462851 81.99457419 365.21722 4.04383 MAP1LC3BP1 . . . microtubule associated protein 1 light chain 3 beta pseudogene 1 . . . . . . . . . . . MAP1LC3C 0.000381762122487153 0.393317232184594 0.606301005692919 microtubule associated protein 1 light chain 3 gamma FUNCTION: Ubiquitin-like modifier that plays a crucial role in antibacterial autophagy (xenophagy) through the selective binding of CALCOCO2. Recruites all ATG8 family members to infecting bacteria such as S.Typhimurium. {ECO:0000269|PubMed:23022382}.; . TISSUE SPECIFICITY: Most abundant in placenta, lung and ovary. {ECO:0000269|PubMed:12740394}.; unclassifiable (Anatomical System); superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.12325 0.08709 0.058937498 58.26256192 29.74673 0.94844 MAP1LC3P . . . microtubule associated protein 1 light chain 3 pseudogene . . . . . . . . . . . MAP1S 0.637852410524494 0.361862646220291 0.000284943255213966 microtubule associated protein 1S FUNCTION: Microtubule-associated protein that mediates aggregation of mitochondria resulting in cell death and genomic destruction (MAGD). Plays a role in anchoring the microtubule organizing center to the centrosomes. Binds to DNA. Plays a role in apoptosis. Involved in the formation of microtubule bundles (By similarity). {ECO:0000250, ECO:0000269|PubMed:15899810, ECO:0000269|PubMed:17234756}.; . TISSUE SPECIFICITY: Expressed in neurons (at protein level). Expressed in spermatocytes, spermatids and spermatozoa. Expressed in the cerebral cortex. Highly expressed in testis. Moderately expressed in the brain, colon, heart, kidney, liver, lung, placenta, small intestine, spleen and stomach. Weakly expressed in muscle. {ECO:0000269|PubMed:11827465, ECO:0000269|PubMed:14627543, ECO:0000269|PubMed:17658481}.; smooth muscle;ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;blood;pancreas;lung;placenta;visual apparatus;liver;alveolus;spleen;kidney;stomach;peripheral nerve; amygdala;subthalamic nucleus;testis - interstitial;medulla oblongata;testis - seminiferous tubule;temporal lobe;prefrontal cortex;testis;globus pallidus;pons;cingulate cortex;parietal lobe; 0.15009 0.12908 . . 2292.92017 8.86491 MAP2 0.999983364970244 1.66350296565264e-05 9.92523637144291e-14 microtubule associated protein 2 FUNCTION: The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules.; . . colon;fovea centralis;skin;whole body;frontal lobe;cerebral cortex;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;hypothalamus;skeletal muscle;breast;pancreas;lung;hippocampus;macula lutea;spleen;kidney;mammary gland;stomach; occipital lobe;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;caudate nucleus;trigeminal ganglion;parietal lobe; 0.28644 0.25532 -1.313764723 4.824251003 424.49113 4.30507 MAP2K1 0.994501270366062 0.00549805295620231 6.76677735529064e-07 mitogen-activated protein kinase kinase 1 FUNCTION: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation, predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements. One target of the MAPK/ERK cascade is peroxisome proliferator- activated receptor gamma (PPARG), a nuclear receptor that promotes differentiation and apoptosis. MAP2K1/MEK1 has been shown to export PPARG from the nucleus. The MAPK/ERK cascade is also involved in the regulation of endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC), as well as in the fragmentation of the Golgi apparatus during mitosis. {ECO:0000269|PubMed:14737111, ECO:0000269|PubMed:17101779}.; DISEASE: Cardiofaciocutaneous syndrome 3 (CFC3) [MIM:615279]: A form of cardiofaciocutaneous syndrome, a multiple congenital anomaly disorder characterized by a distinctive facial appearance, heart defects and mental retardation. Heart defects include pulmonic stenosis, atrial septal defects and hypertrophic cardiomyopathy. Some affected individuals present with ectodermal abnormalities such as sparse, friable hair, hyperkeratotic skin lesions and a generalized ichthyosis-like condition. Typical facial features are similar to Noonan syndrome. They include high forehead with bitemporal constriction, hypoplastic supraorbital ridges, downslanting palpebral fissures, a depressed nasal bridge, and posteriorly angulated ears with prominent helices. Distinctive features of CFC3 include macrostomia and horizontal shape of palpebral fissures. {ECO:0000269|PubMed:16439621, ECO:0000269|PubMed:18042262}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, with extremely low levels in brain. {ECO:0000269|PubMed:1281467}.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.94061 0.84890 -0.449946534 24.00330267 4.89315 0.18138 MAP2K1P1 . . . mitogen-activated protein kinase kinase 1 pseudogene 1 . . . . . . . . . . . MAP2K2 0.86326115931858 0.136320885012997 0.00041795566842237 mitogen-activated protein kinase kinase 2 FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. Activates the ERK1 and ERK2 MAP kinases (By similarity). {ECO:0000250}.; DISEASE: Cardiofaciocutaneous syndrome 4 (CFC4) [MIM:615280]: A form of cardiofaciocutaneous syndrome, a multiple congenital anomaly disorder characterized by a distinctive facial appearance, heart defects and mental retardation. Heart defects include pulmonic stenosis, atrial septal defects and hypertrophic cardiomyopathy. Some affected individuals present with ectodermal abnormalities such as sparse, friable hair, hyperkeratotic skin lesions and a generalized ichthyosis-like condition. Typical facial features are similar to Noonan syndrome. They include high forehead with bitemporal constriction, hypoplastic supraorbital ridges, downslanting palpebral fissures, a depressed nasal bridge, and posteriorly angulated ears with prominent helices. {ECO:0000269|PubMed:16439621, ECO:0000269|PubMed:18042262, ECO:0000269|PubMed:20358587}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;smooth muscle;ovary;salivary gland;sympathetic chain;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; amygdala;prefrontal cortex;testis;pons;cingulate cortex; 0.88489 0.51187 -0.800872469 12.33191791 40.94266 1.19949 MAP2K3 0.000496052997398823 0.968531857314201 0.0309720896883996 mitogen-activated protein kinase kinase 3 FUNCTION: Dual specificity kinase. Is activated by cytokines and environmental stress in vivo. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinase p38.; DISEASE: Note=Defects in MAP2K3 may be involved in colon cancer.; TISSUE SPECIFICITY: Abundant expression is seen in the skeletal muscle. It is also widely expressed in other tissues.; lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;fetal liver;trigeminal ganglion;whole blood;skeletal muscle;bone marrow; 0.23537 0.33997 0.108486928 61.90728946 81.19169 1.90782 MAP2K4 0.997002550124826 0.00299729605083 1.53824343859195e-07 mitogen-activated protein kinase kinase 4 FUNCTION: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K7/MKK7, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The phosphorylation of the Thr residue by MAP2K7/MKK7 seems to be the prerequisite for JNK activation at least in response to proinflammatory cytokines, while other stimuli activate both MAP2K4/MKK4 and MAP2K7/MKK7 which synergistically phosphorylate JNKs. MAP2K4 is required for maintaining peripheral lymphoid homeostasis. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Whereas MAP2K7/MKK7 exclusively activates JNKs, MAP2K4/MKK4 additionally activates the p38 MAPKs MAPK11, MAPK12, MAPK13 and MAPK14. {ECO:0000269|PubMed:7716521}.; . TISSUE SPECIFICITY: Abundant expression is seen in the skeletal muscle. It is also widely expressed in other tissues.; ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; amygdala;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;hypothalamus;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.45395 0.66098 -0.273576253 33.97027601 11.62223 0.42077 MAP2K4P1 . . . mitogen-activated protein kinase kinase 4 pseudogene 1 . . . . . . . . . . . MAP2K5 0.475918460790794 0.524072678884284 8.86032492278e-06 mitogen-activated protein kinase kinase 5 FUNCTION: Acts as a scaffold for the formation of a ternary MAP3K2/MAP3K3-MAP3K5-MAPK7 signaling complex. Activation of this pathway appears to play a critical role in protecting cells from stress-induced apoptosis, neuronal survival and cardiac development and angiogenesis. {ECO:0000269|PubMed:7759517, ECO:0000269|PubMed:9384584}.; . TISSUE SPECIFICITY: Expressed in many adult tissues. Abundant in heart and skeletal muscle.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;spleen;cervix;kidney; whole brain;testis - interstitial;subthalamic nucleus;uterus corpus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.38366 0.21895 -0.692458599 14.96815287 37.4829 1.11572 MAP2K6 0.951049683729579 0.0489490876424219 1.22862799879303e-06 mitogen-activated protein kinase kinase 6 FUNCTION: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. With MAP3K3/MKK3, catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinases p38 MAPK11, MAPK12, MAPK13 and MAPK14 and plays an important role in the regulation of cellular responses to cytokines and all kinds of stresses. Especially, MAP2K3/MKK3 and MAP2K6/MKK6 are both essential for the activation of MAPK11 and MAPK13 induced by environmental stress, whereas MAP2K6/MKK6 is the major MAPK11 activator in response to TNF. MAP2K6/MKK6 also phosphorylates and activates PAK6. The p38 MAP kinase signal transduction pathway leads to direct activation of transcription factors. Nuclear targets of p38 MAP kinase include the transcription factors ATF2 and ELK1. Within the p38 MAPK signal transduction pathway, MAP3K6/MKK6 mediates phosphorylation of STAT4 through MAPK14 activation, and is therefore required for STAT4 activation and STAT4-regulated gene expression in response to IL-12 stimulation. The pathway is also crucial for IL-6-induced SOCS3 expression and down-regulation of IL-6-mediated gene induction; and for IFNG- dependent gene transcription. Has a role in osteoclast differentiation through NF-kappa-B transactivation by TNFSF11, and in endochondral ossification and since SOX9 is another likely downstream target of the p38 MAPK pathway. MAP2K6/MKK6 mediates apoptotic cell death in thymocytes. Acts also as a regulator for melanocytes dendricity, through the modulation of Rho family GTPases. {ECO:0000269|PubMed:10961885, ECO:0000269|PubMed:11727828, ECO:0000269|PubMed:15550393, ECO:0000269|PubMed:20869211, ECO:0000269|PubMed:8622669, ECO:0000269|PubMed:8626699, ECO:0000269|PubMed:8663074, ECO:0000269|PubMed:9218798}.; . TISSUE SPECIFICITY: Isoform 2 is only expressed in skeletal muscle. Isoform 1 is expressed in skeletal muscle, heart, and in lesser extent in liver or pancreas. {ECO:0000269|PubMed:8621675}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;spleen;kidney; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.82258 0.33817 -0.317668748 31.45789101 8.85591 0.32591 MAP2K7 0.985719994203379 0.0142730058910696 6.99990555178526e-06 mitogen-activated protein kinase kinase 7 FUNCTION: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The monophosphorylation of JNKs on the Thr residue is sufficient to increase JNK activity indicating that MAP2K7/MKK7 is important to trigger JNK activity, while the additional phosphorylation of the Tyr residue by MAP2K4/MKK4 ensures optimal JNK activation. Has a specific role in JNK signal transduction pathway activated by proinflammatory cytokines. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. {ECO:0000269|PubMed:9312068, ECO:0000269|PubMed:9372971, ECO:0000269|PubMed:9535930, ECO:0000269|Ref.5}.; . TISSUE SPECIFICITY: Ubiquitous; with highest level of expression in skeletal muscle. Isoform 3 is found at low levels in placenta, fetal liver, and skeletal muscle. {ECO:0000269|PubMed:16442502, ECO:0000269|PubMed:9372971, ECO:0000269|PubMed:9535930}.; . . 0.81541 . -0.514264485 21.41424864 25.26477 0.82588 MAP3K1 0.998072118460426 0.00192788152179145 1.77823081190551e-11 mitogen-activated protein kinase kinase kinase 1 FUNCTION: Component of a protein kinase signal transduction cascade. Activates the ERK and JNK kinase pathways by phosphorylation of MAP2K1 and MAP2K4. Activates CHUK and IKBKB, the central protein kinases of the NF-kappa-B pathway. {ECO:0000269|PubMed:9808624}.; DISEASE: 46,XY sex reversal 6 (SRXY6) [MIM:613762]: A disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females. {ECO:0000269|PubMed:21129722}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.21339 0.15001 -1.236390924 5.520169851 5093.25281 14.61378 MAP3K2 0.999560916816359 0.000439081759684218 1.4239571592295e-09 mitogen-activated protein kinase kinase kinase 2 FUNCTION: Component of a protein kinase signal transduction cascade. Regulates the JNK and ERK5 pathways by phosphorylating and activating MAP2K5 and MAP2K7 (By similarity). Plays a role in caveolae kiss-and-run dynamics. {ECO:0000250, ECO:0000269|PubMed:10713157, ECO:0000269|PubMed:16001074}.; . . unclassifiable (Anatomical System);ovary;blood;parathyroid;fovea centralis;choroid;lens;skeletal muscle;skin;retina;optic nerve;placenta;macula lutea;liver;germinal center;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cerebellum; 0.61232 0.17004 -0.291981272 33.20358575 84.02396 1.95179 MAP3K3 0.999526986907979 0.000473013022126373 6.98948959925783e-11 mitogen-activated protein kinase kinase kinase 3 FUNCTION: Component of a protein kinase signal transduction cascade. Mediates activation of the NF-kappa-B, AP1 and DDIT3 transcriptional regulators. {ECO:0000269|PubMed:12912994, ECO:0000269|PubMed:14661019, ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:9006902}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;hypothalamus;pharynx;blood;lens;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; . 0.79837 0.23984 -1.06726444 7.372021703 91.94105 2.06355 MAP3K4 0.999991910638856 8.08936114380136e-06 5.81448537015288e-18 mitogen-activated protein kinase kinase kinase 4 FUNCTION: Component of a protein kinase signal transduction cascade. Activates the CSBP2, P38 and JNK MAPK pathways, but not the ERK pathway. Specifically phosphorylates and activates MAP2K4 and MAP2K6. {ECO:0000269|PubMed:12052864, ECO:0000269|PubMed:9305639}.; . TISSUE SPECIFICITY: Expressed at high levels in heart, placenta, skeletal muscle and pancreas, and at lower levels in other tissues. {ECO:0000269|PubMed:9305639}.; smooth muscle;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach; uterus corpus;testis - seminiferous tubule;prefrontal cortex;testis;cingulate cortex; 0.74725 0.11364 -1.076610636 7.324840764 496.64564 4.58050 MAP3K5 0.995107743453563 0.00489225654500715 1.42967211593086e-12 mitogen-activated protein kinase kinase kinase 5 FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signaling for determination of cell fate such as differentiation and survival. Plays a crucial role in the apoptosis signal transduction pathway through mitochondria-dependent caspase activation. MAP3K5/ASK1 is required for the innate immune response, which is essential for host defense against a wide range of pathogens. Mediates signal transduction of various stressors like oxidative stress as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) or lipopolysaccharide (LPS). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K4/SEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs control the transcription factors activator protein-1 (AP-1). {ECO:0000269|PubMed:10411906, ECO:0000269|PubMed:10688666, ECO:0000269|PubMed:10849426, ECO:0000269|PubMed:11029458, ECO:0000269|PubMed:11154276, ECO:0000269|PubMed:11689443, ECO:0000269|PubMed:11920685, ECO:0000269|PubMed:12697749, ECO:0000269|PubMed:14688258, ECO:0000269|PubMed:14749717, ECO:0000269|PubMed:15023544, ECO:0000269|PubMed:16129676, ECO:0000269|PubMed:17220297, ECO:0000269|PubMed:23102700, ECO:0000269|PubMed:8940179, ECO:0000269|PubMed:8974401, ECO:0000269|PubMed:9564042, ECO:0000269|PubMed:9774977}.; . TISSUE SPECIFICITY: Abundantly expressed in heart and pancreas.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;aorta;stomach;cerebellum; amygdala;superior cervical ganglion;subthalamic nucleus;occipital lobe;adrenal gland;spinal cord;adrenal cortex;prefrontal cortex;globus pallidus;caudate nucleus; 0.53784 0.55740 -0.705410796 14.77942911 272.93273 3.54158 MAP3K6 4.90980509511437e-15 0.733604279615901 0.266395720384094 mitogen-activated protein kinase kinase kinase 6 FUNCTION: Component of a protein kinase signal transduction cascade. Activates the JNK, but not ERK or p38 kinase pathways. {ECO:0000269|PubMed:17210579, ECO:0000269|PubMed:9875215}.; . . myocardium;ovary;colon;fovea centralis;choroid;skin;uterus;prostate;optic nerve;bone;pituitary gland;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;adrenal cortex;breast;pancreas;lung;placenta;macula lutea;cervix;kidney;mammary gland;stomach; fetal lung;ciliary ganglion;skin; 0.14635 0.10817 0.369203982 74.77589054 3475.08367 11.34775 MAP3K7 0.998336232242865 0.00166376625853662 1.49859858138454e-09 mitogen-activated protein kinase kinase kinase 7 FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR). Ceramides are also able to activate MAP3K7/TAK1. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs, c-jun N-terminal kinases (JNKs) and I-kappa-B kinase complex (IKK). Both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1), while nuclear factor-kappa B is activated by IKK. MAP3K7 activates also IKBKB and MAPK8/JNK1 in response to TRAF6 signaling and mediates BMP2- induced apoptosis. In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B. Promotes TRIM5 capsid-specific restriction activity. {ECO:0000269|PubMed:10094049, ECO:0000269|PubMed:11460167, ECO:0000269|PubMed:12589052, ECO:0000269|PubMed:16845370, ECO:0000269|PubMed:16893890, ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:8663074, ECO:0000269|PubMed:9079627}.; . TISSUE SPECIFICITY: Isoform 1A is the most abundant in ovary, skeletal muscle, spleen and blood mononuclear cells. Isoform 1B is highly expressed in brain, kidney and small intestine. Isoform 1C is the major form in prostate. Isoform 1D is the less abundant form. {ECO:0000269|PubMed:11118615}.; . . 0.79955 0.33817 -0.427900189 25.14744043 14.73281 0.53078 MAP3K7CL 0.0022653891673035 0.762165277356839 0.235569333475858 MAP3K7 C-terminal like . . TISSUE SPECIFICITY: Detected in lung and peripheral blood leukocytes. Expressed predominantly in peripheral blood leukocytes and ubiquitously in adult and fetal tissues. Also expressed strongly in breast carcinoma GI-101, colon adenocarcinoma GI-112, and prostatic adenocarcinoma PC3. {ECO:0000269|PubMed:15168726}.; . . 0.05637 0.06544 0.193034296 66.82000472 114.14784 2.32860 MAP3K8 0.870951295340519 0.128975742296884 7.29623625970077e-05 mitogen-activated protein kinase kinase kinase 8 FUNCTION: Required for lipopolysaccharide (LPS)-induced, TLR4- mediated activation of the MAPK/ERK pathway in macrophages, thus being critical for production of the proinflammatory cytokine TNF- alpha (TNF) during immune responses. Involved in the regulation of T-helper cell differentiation and IFNG expression in T-cells. Involved in mediating host resistance to bacterial infection through negative regulation of type I interferon (IFN) production. In vitro, activates MAPK/ERK pathway in response to IL1 in an IRAK1-independent manner, leading to up-regulation of IL8 and CCL4. Transduces CD40 and TNFRSF1A signals that activate ERK in B- cells and macrophages, and thus may play a role in the regulation of immunoglobulin production. May also play a role in the transduction of TNF signals that activate JNK and NF-kappa-B in some cell types. In adipocytes, activates MAPK/ERK pathway in an IKBKB-dependent manner in response to IL1B and TNF, but not insulin, leading to induction of lipolysis. Plays a role in the cell cycle. Isoform 1 shows some transforming activity, although it is much weaker than that of the activated oncogenic variant. {ECO:0000269|PubMed:11342626, ECO:0000269|PubMed:12667451, ECO:0000269|PubMed:15169888, ECO:0000269|PubMed:16371247, ECO:0000269|PubMed:1833717, ECO:0000269|PubMed:19001140, ECO:0000269|PubMed:19754427, ECO:0000269|PubMed:19808894}.; . TISSUE SPECIFICITY: Expressed in several normal tissues and human tumor-derived cell lines.; unclassifiable (Anatomical System);ovary;heart;colon;parathyroid;blood;vein;skin;breast;uterus;prostate;lung;endometrium;bone;placenta;liver;testis;spleen;germinal center;kidney;brain;mammary gland;stomach;thymus; atrioventricular node;trigeminal ganglion;skeletal muscle; 0.23246 0.26689 -0.890882376 10.30313753 67.96559 1.70520 MAP3K9 0.92339517875996 0.0766046649977411 1.56242299098393e-07 mitogen-activated protein kinase kinase kinase 9 FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade through the phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7 which in turn activate the JNKs. The MKK/JNK signaling pathway regulates stress response via activator protein-1 (JUN) and GATA4 transcription factors. Plays also a role in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. {ECO:0000269|PubMed:11416147, ECO:0000269|PubMed:15610029}.; DISEASE: Note=May play a role in esophageal cancer susceptibility and/or development.; TISSUE SPECIFICITY: Expressed in epithelial tumor cell lines of colonic, breast and esophageal origin. {ECO:0000269|PubMed:8477742}.; . . 0.14753 0.13060 -1.54510635 3.30856334 319.51976 3.79581 MAP3K10 0.792721034473586 0.20722532420765 5.36413187641228e-05 mitogen-activated protein kinase kinase kinase 10 FUNCTION: Activates the JUN N-terminal pathway. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain and skeletal muscle.; unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;colon;blood;skin;retina;bone marrow;uterus;prostate;whole body;lung;frontal lobe;bone;placenta;liver;testis;spleen;kidney;brain;stomach; subthalamic nucleus;superior cervical ganglion;temporal lobe;globus pallidus;pons;caudate nucleus;trigeminal ganglion;skeletal muscle;parietal lobe;cerebellum; 0.30295 0.15476 -1.131590109 6.481481481 105.32483 2.22175 MAP3K11 0.170283101085365 0.829692885728124 2.40131865104259e-05 mitogen-activated protein kinase kinase kinase 11 FUNCTION: Activates the JUN N-terminal pathway. Required for serum-stimulated cell proliferation and for mitogen and cytokine activation of MAPK14 (p38), MAPK3 (ERK) and MAPK8 (JNK1) through phosphorylation and activation of MAP2K4/MKK4 and MAP2K7/MKK7. Plays a role in mitogen-stimulated phosphorylation and activation of BRAF, but does not phosphorylate BRAF directly. Influences microtubule organization during the cell cycle. {ECO:0000269|PubMed:12529434, ECO:0000269|PubMed:15258589, ECO:0000269|PubMed:8195146, ECO:0000269|PubMed:9003778}.; . TISSUE SPECIFICITY: Expressed in a wide variety of normal and neoplastic tissues including fetal lung, liver, heart and kidney, and adult lung, liver, heart, kidney, placenta, skeletal muscle, pancreas and brain. {ECO:0000269|PubMed:8183572, ECO:0000269|PubMed:8195146}.; ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion; 0.22896 0.24839 -0.707227564 14.71455532 113.33006 2.31799 MAP3K12 0.99998181311032 1.81868890707178e-05 6.09539636704436e-13 mitogen-activated protein kinase kinase kinase 12 FUNCTION: May be an activator of the JNK/SAPK pathway. Phosphorylates beta-casein, histone 1 and myelin basic protein in vitro.; . TISSUE SPECIFICITY: Highly expressed in brain and kidney.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;urinary;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; whole brain;cerebellum peduncles;pons;trigeminal ganglion;cingulate cortex;skeletal muscle;cerebellum; 0.39883 0.12346 -0.578583623 18.71903751 151.97483 2.69639 MAP3K13 0.966849138305972 0.0331508578467231 3.84730515187287e-09 mitogen-activated protein kinase kinase kinase 13 FUNCTION: Activates the JUN N-terminal pathway through activation of the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3 to regulate the activation of NF-kappa-B in the cytosol. This activation is kinase-dependent and involves activating the IKK complex, the IKBKB-containing complex that phosphorylates inhibitors of NF-kappa-B. {ECO:0000269|PubMed:11726277, ECO:0000269|PubMed:12492477, ECO:0000269|PubMed:9353328}.; . TISSUE SPECIFICITY: Expressed in the adult brain, liver, placenta and pancreas, with expression strongest in the pancreas. {ECO:0000269|PubMed:9353328}.; unclassifiable (Anatomical System);lung;frontal lobe;testis;blood;kidney;brain;skeletal muscle;retina; subthalamic nucleus;superior cervical ganglion;occipital lobe;prefrontal cortex;globus pallidus;kidney;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.29073 0.10740 -0.372889896 28.20240623 147.0655 2.64138 MAP3K14 . . . mitogen-activated protein kinase kinase kinase 14 FUNCTION: Lymphotoxin beta-activated kinase which seems to be exclusively involved in the activation of NF-kappa-B and its transcriptional activity. Promotes proteolytic processing of NFKB2/P100, which leads to activation of NF-kappa-B via the non- canonical pathway. Could act in a receptor-selective manner. {ECO:0000269|PubMed:15084608}.; . TISSUE SPECIFICITY: Weakly expressed in testis, small intestine, spleen, thymus, peripheral blood leukocytes, prostate, ovary and colon. {ECO:0000269|PubMed:9020361}.; unclassifiable (Anatomical System);smooth muscle;lymph node;heart;ovary;tongue;colon;parathyroid;skin;skeletal muscle;uterus;prostate;lung;endometrium;bone;placenta;testis;cervix;head and neck;kidney;brain;mammary gland;tonsil;stomach;thymus; . 0.18826 0.57524 . . . . MAP3K14-AS1 . . . MAP3K14 antisense RNA 1 . . . . . . . . . . . MAP3K15 1.01372441429332e-28 1.47252090356323e-05 0.999985274790964 mitogen-activated protein kinase kinase kinase 15 FUNCTION: May function in a signal transduction pathway that is activated by various cell stresses and leads to apoptosis. {ECO:0000269|PubMed:20362554}.; . TISSUE SPECIFICITY: Isoform 2 and isoform 3 are widely expressed. Isoform 2 highest levels are observed in fetal brain, and isoform 3 highest levels in pancreas, peripheral blood leukocytes, fetal brain and spleen. {ECO:0000269|PubMed:20362554}.; lymphoreticular;ovary;parathyroid;skin;uterus;prostate;whole body;endometrium;bone;iris;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;lymph node;cartilage;islets of Langerhans;adrenal cortex;bile duct;pia mater;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach; . 0.11038 0.09392 . . 348.40562 3.95570 MAP3K19 3.69884742626308e-14 0.265330279624279 0.734669720375684 mitogen-activated protein kinase kinase kinase 19 . . . . . 0.08636 0.06857 2.05224859 97.77659825 3281.38813 10.93768 MAP4 0.99884872439436 0.00115127499491701 6.10722614686932e-10 microtubule associated protein 4 FUNCTION: Non-neuronal microtubule-associated protein. Promotes microtubule assembly. {ECO:0000269|PubMed:10791892}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;tonsil;gall bladder;heart;cartilage;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;choroid;fovea centralis;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; amygdala;whole brain;dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;atrioventricular node;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.10803 0.14652 0.411473843 76.55697098 7952.87694 19.27712 MAP4K1 0.991409179038241 0.00859082082340268 1.3835597709909e-10 mitogen-activated protein kinase kinase kinase kinase 1 FUNCTION: Serine/threonine-protein kinase, which may play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway. May play a role in hematopoietic lineage decisions and growth regulation. Able to autophosphorylate. {ECO:0000269|PubMed:24362026, ECO:0000269|PubMed:8824585}.; . TISSUE SPECIFICITY: Expressed primarily in hematopoietic organs, including bone marrow, spleen and thymus. Also expressed at very low levels in lung, kidney, mammary glands and small intestine. {ECO:0000269|PubMed:8824585}.; unclassifiable (Anatomical System);lymph node;ovary;salivary gland;intestine;pharynx;colon;blood;fovea centralis;skin;skeletal muscle;retina;breast;prostate;lung;endometrium;larynx;macula lutea;visual apparatus;liver;testis;head and neck;germinal center;kidney;brain;bladder; superior cervical ganglion;lymph node;tumor;white blood cells;pons;trigeminal ganglion;skeletal muscle;parietal lobe;tonsil;thymus; 0.74545 . -0.556537043 19.72753008 102.29658 2.18597 MAP4K2 6.47662241204138e-05 0.999892501182302 4.27325935774661e-05 mitogen-activated protein kinase kinase kinase kinase 2 FUNCTION: Serine/threonine-protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Acts as a MAPK kinase kinase kinase (MAP4K) and is an upstream activator of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway and to a lesser extend of the p38 MAPKs signaling pathway. Required for the efficient activation of JNKs by TRAF6-dependent stimuli, including pathogen-associated molecular patterns (PAMPs) such as polyinosine-polycytidine (poly(IC)), lipopolysaccharides (LPS), lipid A, peptidoglycan (PGN), or bacterial flagellin. To a lesser degree, IL-1 and engagement of CD40 also stimulate MAP4K2-mediated JNKs activation. The requirement for MAP4K2/GCK is most pronounced for LPS signaling, and extends to LPS stimulation of c-Jun phosphorylation and induction of IL-8. Enhances MAP3K1 oligomerization, which may relieve N-terminal mediated MAP3K1 autoinhibition and lead to activation following autophosphorylation. Mediates also the SAP/JNK signaling pathway and the p38 MAPKs signaling pathway through activation of the MAP3Ks MAP3K10/MLK2 and MAP3K11/MLK3. May play a role in the regulation of vesicle targeting or fusion. regulation of vesicle targeting or fusion. {ECO:0000269|PubMed:11784851, ECO:0000269|PubMed:15456887, ECO:0000269|PubMed:17584736, ECO:0000269|PubMed:7477268, ECO:0000269|PubMed:7515885, ECO:0000269|PubMed:9712898}.; . TISSUE SPECIFICITY: Highly expressed in germinal center but not mantle zone B-cells. Also expressed in lung, brain and placenta and at lower levels in other tissues examined. {ECO:0000269|PubMed:7515885}.; ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;muscle;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;spleen;cervix;kidney;mammary gland; superior cervical ganglion;globus pallidus;ciliary ganglion;skeletal muscle; 0.17730 0.74195 -1.03794674 7.832035858 323.64323 3.82250 MAP4K3 0.804701046466324 0.195298950414867 3.11880859016523e-09 mitogen-activated protein kinase kinase kinase kinase 3 FUNCTION: May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway. {ECO:0000269|PubMed:9275185}.; . TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined, with high levels in heart, brain, placenta, skeletal muscle, kidney and pancreas and lower levels in lung and liver. {ECO:0000269|PubMed:9275185}.; smooth muscle;ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;hypothalamus;adrenal cortex;skeletal muscle;bile duct;breast;lung;adrenal gland;placenta;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;appendix;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.56204 0.10762 -0.50880549 21.72682236 80.58132 1.89646 MAP4K4 0.999998979047087 1.02095291326414e-06 2.24158036977468e-17 mitogen-activated protein kinase kinase kinase kinase 4 FUNCTION: Serine/threonine kinase that may play a role in the response to environmental stress and cytokines such as TNF-alpha. Appears to act upstream of the JUN N-terminal pathway. Phosphorylates SMAD1 on Thr-322. {ECO:0000269|PubMed:21690388, ECO:0000269|PubMed:9890973}.; . TISSUE SPECIFICITY: Appears to be ubiquitous. Expressed in all tissue types examined. Isoform 5 appears to be more abundant in the brain. Isoform 4 is predominant in the liver, skeletal muscle and placenta. {ECO:0000269|PubMed:9890973}.; myocardium;lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;brain;bladder;heart;cartilage;tongue;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;aorta;stomach; medulla oblongata;superior cervical ganglion;ciliary ganglion;cingulate cortex;parietal lobe; 0.51487 0.22596 -1.442099697 3.951403633 72.59332 1.77682 MAP4K5 0.944269981947709 0.0557299483401183 6.97121731348964e-08 mitogen-activated protein kinase kinase kinase kinase 5 FUNCTION: May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway. {ECO:0000269|PubMed:9038372}.; . TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined, with high levels in the ovary, testis and prostate. {ECO:0000269|PubMed:9038372}.; ovary;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;breast;pancreas;lung;placenta;visual apparatus;head and neck;cervix;kidney;stomach; superior cervical ganglion;trigeminal ganglion; 0.39478 0.14996 -0.727458245 14.19556499 952.53004 5.97246 MAP6 0.0131669155399533 0.95428932482825 0.0325437596317963 microtubule associated protein 6 FUNCTION: Involved in microtubule stabilization in many cell types, including neuronal cells. Specifically has microtubule cold stabilizing activity. Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with TMEM106B. {ECO:0000269|PubMed:24357581}.; . TISSUE SPECIFICITY: Expressed in brain (at protein level). Expressed in spinal chord. Isoform 2 expression is up-regulated in the prefrontal cortex (Brodmann's area 46) of patients with schizophrenia (postmortem brain study). {ECO:0000269|PubMed:14692697, ECO:0000269|PubMed:16624526}.; unclassifiable (Anatomical System);islets of Langerhans;fovea centralis;choroid;lens;skin;retina;prostate;optic nerve;lung;frontal lobe;placenta;macula lutea;liver;pituitary gland;testis;spleen;kidney;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;pons; 0.06551 0.07302 . . 152.156 2.69804 MAP6D1 0.0518280033537145 0.694708864476984 0.253463132169301 MAP6 domain containing 1 FUNCTION: May have microtubule-stabilizing activity. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;heart;hypothalamus;spinal cord;colon;blood;skin;whole body;lung;frontal lobe;placenta;visual apparatus;hippocampus;testis;germinal center;kidney;brain;stomach;cerebellum; amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.07209 0.08717 . . 46.1694 1.30916 MAP7 0.929880601613702 0.0701192736895609 1.24696736852857e-07 microtubule associated protein 7 FUNCTION: Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in the redistribution of TRPV4 toward the membrane and may link cytoskeletal microfilaments. {ECO:0000269|PubMed:11719555, ECO:0000269|PubMed:8408219, ECO:0000269|PubMed:9989799}.; . TISSUE SPECIFICITY: Expressed in the skin and cells of epithelial origin. Predominantly expressed in the suprabasal layers of the normal epidermis and relatively abundant in squamous cell carcinomas but barely detectable in basal cell carcinomas. {ECO:0000269|PubMed:8408219, ECO:0000269|PubMed:9989799}.; umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; whole brain;amygdala;medulla oblongata;testis - interstitial;occipital lobe;thalamus;testis - seminiferous tubule;hypothalamus;spinal cord;prefrontal cortex;testis;caudate nucleus;parietal lobe; 0.65344 0.12871 0.494191824 79.62373201 671.81801 5.17977 MAP7D1 0.973584103721944 0.0264156318551709 2.64422884539566e-07 MAP7 domain containing 1 . . . myocardium;lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;amygdala;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;oesophagus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;thymus;cerebellum; amygdala;whole brain;medulla oblongata;thalamus;occipital lobe;hypothalamus;prefrontal cortex;caudate nucleus;pons;cingulate cortex;parietal lobe;cerebellum; 0.09390 0.09098 -0.33061537 30.82094834 1321.90429 6.83977 MAP7D2 0.555948304937886 0.44402830108066 2.33939814536377e-05 MAP7 domain containing 2 . . . unclassifiable (Anatomical System);colon;fovea centralis;choroid;lens;retina;breast;optic nerve;lung;frontal lobe;endometrium;placenta;bone;macula lutea;germinal center;kidney;brain; amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.27137 . 0.022122107 55.69120075 1061.86646 6.25368 MAP7D3 1.12703445169542e-07 0.783692144184084 0.216307743112471 MAP7 domain containing 3 FUNCTION: Promotes the assembly and stability of microtubules. {ECO:0000269|PubMed:22142902, ECO:0000269|PubMed:24927501}.; . . ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;hippocampus;liver;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;medulla oblongata;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05241 0.07326 0.979225112 90.42816702 43.0623 1.24569 MAP9 5.17494979120361e-12 0.0548854448824103 0.945114555112415 microtubule associated protein 9 FUNCTION: Involved in organization of the bipolar mitotic spindle. Required for bipolar spindle assembly, mitosis progression and cytokinesis. May act by stabilizing interphase microtubules. {ECO:0000269|PubMed:16049101}.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;prostate;lung;nasopharynx;bone;placenta;pituitary gland;hypopharynx;testis;head and neck;germinal center;brain;mammary gland;pineal gland; medulla oblongata;subthalamic nucleus;cerebellum peduncles;temporal lobe;prefrontal cortex;appendix;cingulate cortex; 0.12642 0.11218 1.578193463 95.76551073 5536.05514 15.38508 MAP10 1.29356795750669e-14 0.00608605050631308 0.993913949493674 microtubule associated protein 10 FUNCTION: Microtubule-associated protein (MAP) that plays a role in the regulation of cell division; promotes microtubule stability and participates in the organization of the spindle midzone and normal progress of cytokinesis. {ECO:0000269|PubMed:23264731}.; . TISSUE SPECIFICITY: Expressed in different cell lines (at protein level). {ECO:0000269|PubMed:23264731}.; . . 0.12315 . 0.74035066 86.34701581 2031.21473 8.29376 MAPK1 0.981866085911696 0.0181213228573161 1.25912309879935e-05 mitogen-activated protein kinase 1 FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Mediates phosphorylation of TPR in respons to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;cerebellum; . 0.99874 0.98274 -0.405853867 26.23260203 7.31409 0.27310 MAPK1IP1L 0.389494276372223 0.568111073350825 0.0423946502769521 mitogen-activated protein kinase 1 interacting protein 1-like . . . . . 0.62594 . -0.273576253 33.97027601 13.12196 0.47716 MAPK3 0.409692328374644 0.588548311484377 0.00175936014097912 mitogen-activated protein kinase 3 FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. {ECO:0000269|PubMed:10393181, ECO:0000269|PubMed:10617468, ECO:0000269|PubMed:12110590, ECO:0000269|PubMed:12356731, ECO:0000269|PubMed:12974390, ECO:0000269|PubMed:15788397, ECO:0000269|PubMed:15952796, ECO:0000269|PubMed:16581800, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:8325880, ECO:0000269|PubMed:9155018, ECO:0000269|PubMed:9480836}.; . . medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;brain;amygdala;heart;cartilage;blood;lens;skeletal muscle;breast;visual apparatus;liver;cervix;spleen;mammary gland;peripheral nerve;colon;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hypopharynx;amnion;head and neck;kidney;stomach; amygdala;medulla oblongata;occipital lobe;temporal lobe;prefrontal cortex;caudate nucleus; 0.96804 0.99301 -0.405853867 26.23260203 19.21066 0.66196 MAPK4 0.319051500545285 0.677400193850312 0.00354830560440343 mitogen-activated protein kinase 4 FUNCTION: Atypical MAPK protein. Phosphorylates microtubule- associated protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed with MAPKAPK5 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPKAPK5, ERK4/MAPK4 is phosphorylated at Ser-186 and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK4/MAPK4. May promote entry in the cell cycle (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: High expression in heart and brain.; . . 0.16623 0.09994 -0.510624372 21.65015334 61.21268 1.59257 MAPK6 0.533146358713183 0.466170492282658 0.000683149004158449 mitogen-activated protein kinase 6 FUNCTION: Atypical MAPK protein. Phosphorylates microtubule- associated protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed with MAPKAPK5 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPKAPK5, ERK3/MAPK6 is phosphorylated at Ser-189 and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6. May promote entry in the cell cycle (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highest expression in the skeletal muscle, followed by the brain. Also found in heart, placenta, lung, liver, pancreas, kidney and skin fibroblasts.; ovary;salivary gland;intestine;colon;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;cerebellum cortex;tongue;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;cervix;head and neck;kidney;mammary gland;stomach; medulla oblongata;subthalamic nucleus;occipital lobe;prefrontal cortex; 0.74379 0.27057 -0.666770504 15.86459071 305.73832 3.72351 MAPK6PS1 . . . mitogen-activated protein kinase 6 pseudogene 1 . . . . . . . . . . . MAPK6PS2 . . . mitogen-activated protein kinase 6 pseudogene 2 . . . . . . . . . . . MAPK6PS3 . . . mitogen-activated protein kinase 6 pseudogene 3 . . . . . . . . . . . MAPK6PS4 . . . mitogen-activated protein kinase 6 pseudogene 4 . . . . . . . . . . . MAPK6PS5 . . . mitogen-activated protein kinase 6 pseudogene 5 . . . . . . . . . . . MAPK6PS6 . . . mitogen-activated protein kinase 6 pseudogene 6 . . . . . . . . . . . MAPK7 0.232913565027181 0.765566672622905 0.0015197623499135 mitogen-activated protein kinase 7 FUNCTION: Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras- independent and MAP2K5-dependent pathway. May have a role in muscle cell differentiation. May be important for endothelial function and maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact specifically with one another and not with MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth factor-induced cell cycle progression. Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction. {ECO:0000269|PubMed:11254654, ECO:0000269|PubMed:11278431, ECO:0000269|PubMed:22869143, ECO:0000269|PubMed:9384584, ECO:0000269|PubMed:9790194}.; . TISSUE SPECIFICITY: Expressed in many adult tissues. Abundant in heart, placenta, lung, kidney and skeletal muscle. Not detectable in liver. {ECO:0000269|PubMed:7759517}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;muscle;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; superior cervical ganglion;testis;pons;trigeminal ganglion;skeletal muscle; 0.61708 0.20605 -1.306167152 4.889124794 121.12067 2.39747 MAPK8 0.98360211806986 0.0163958902974064 1.99163273377422e-06 mitogen-activated protein kinase 8 FUNCTION: Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK8/JNK1. In turn, MAPK8/JNK1 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. Phosphorylates the replication licensing factor CDT1, inhibiting the interaction between CDT1 and the histone H4 acetylase HBO1 to replication origins. Loss of this interaction abrogates the acetylation required for replication initiation. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including p53/TP53 and Yes-associates protein YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Contributes to the survival of erythroid cells by phosphorylating the antagonist of cell death BAD upon EPO stimulation. Mediates starvation-induced BCL2 phosphorylation, BCL2 dissociation from BECN1, and thus activation of autophagy. Phosphorylates STMN2 and hence regulates microtubule dynamics, controlling neurite elongation in cortical neurons. In the developing brain, through its cytoplasmic activity on STMN2, negatively regulates the rate of exit from multipolar stage and of radial migration from the ventricular zone. Phosphorylates several other substrates including heat shock factor protein 4 (HSF4), the deacetylase SIRT1, ELK1, or the E3 ligase ITCH. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock (PubMed:22441692). {ECO:0000269|PubMed:22441692}.; . . lung;frontal lobe;larynx;urinary;testis;colon;cervix;head and neck;germinal center;brain;mammary gland;stomach; dorsal root ganglion;atrioventricular node; 0.95654 0.99518 -0.339715008 30.06605331 8.79547 0.32472 MAPK8IP1 0.999000973193662 0.000999016250239955 1.05560976261772e-08 mitogen-activated protein kinase 8 interacting protein 1 FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK- regulated activity by retaining JNK in the cytoplasm and inhibiting JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (By similarity). Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response. {ECO:0000250}.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:10700186}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in brain. Expressed in neurons, localizing to neurite tips in differentiating cells. Also expressed in the pancreas, testis and prostate. Low levels in heart, ovary and small intestine. Decreased levels in pancreatic beta cells sensitize cells to IL-1-beta-induced apoptosis.; medulla oblongata;ovary;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;endometrium;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;adrenal cortex;lens;bile duct;lung;placenta;macula lutea;hippocampus;visual apparatus;kidney;stomach;cerebellum; dorsal root ganglion;whole brain;superior cervical ganglion;occipital lobe;thalamus;medulla oblongata;olfactory bulb;cerebellum peduncles;caudate nucleus;pons;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;amygdala;testis - interstitial;spinal cord;temporal lobe;atrioventricular node;skeletal muscle;prefrontal cortex;parietal lobe;cerebellum; 0.37921 0.26087 -0.622676946 17.30950696 99.70372 2.16325 MAPK8IP2 0.997524779751463 0.00247512382091166 9.64276249785317e-08 mitogen-activated protein kinase 8 interacting protein 2 FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. JIP2 inhibits IL1 beta-induced apoptosis in insulin-secreting cells. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed mainly in the brain and pancreas, including insulin-secreting cells. In the nervous system, more abundantly expressed in the cerebellum, pituitary gland, occipital lobe and the amygdala. Also expressed in fetal brain. Very low levels found in uterus, ovary, prostate, colon, testis, adrenal gland, thyroid gland and salivary gland.; unclassifiable (Anatomical System);ovary;islets of Langerhans;temporal lobe;fovea centralis;choroid;lens;retina;pancreas;optic nerve;lung;frontal lobe;oesophagus;placenta;bone;macula lutea;hippocampus;testis;mammary gland;brain;stomach;cerebellum; amygdala;dorsal root ganglion;whole brain;superior cervical ganglion;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;atrioventricular node;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.29180 0.22984 . . 227.93493 3.25982 MAPK8IP3 0.999999970922629 2.90773714073159e-08 9.41711660543873e-20 mitogen-activated protein kinase 8 interacting protein 3 FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:12189133}.; . . ovary;sympathetic chain;colon;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;mammary gland;stomach;peripheral nerve;cerebellum;thymus; amygdala;medulla oblongata;superior cervical ganglion;thalamus;occipital lobe;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.31764 0.18911 -2.649793416 0.766690257 619.3755 5.02096 MAPK8IPP . . . mitogen-activated protein kinase 8 interacting protein, pseudogene . . . . . . . . . . . MAPK9 0.00956433819094729 0.988140252847699 0.00229540896135339 mitogen-activated protein kinase 9 FUNCTION: Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption. When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock (PubMed:22441692). {ECO:0000269|PubMed:22441692}.; . . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;small intestine;heart;cartilage;hypothalamus;muscle;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;head and neck;kidney;mammary gland;stomach; amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;subthalamic nucleus;cerebellum peduncles;prefrontal cortex;pons;trigeminal ganglion;cingulate cortex;cerebellum; 0.96540 0.80000 -0.626318434 17.03231894 23.43443 0.78099 MAPK10 0.834149756443907 0.1658212741789 2.89693771931362e-05 mitogen-activated protein kinase 10 FUNCTION: Serine/threonine-protein kinase involved in various processes such as neuronal proliferation, differentiation, migration and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress- activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK10/JNK3. In turn, MAPK10/JNK3 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. Plays regulatory roles in the signaling pathways during neuronal apoptosis. Phosphorylates the neuronal microtubule regulator STMN2. Acts in the regulation of the beta-amyloid precursor protein/APP signaling during neuronal differentiation by phosphorylating APP. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the photic regulation of the circadian clock (PubMed:22441692). {ECO:0000269|PubMed:11718727, ECO:0000269|PubMed:22441692}.; DISEASE: Note=A chromosomal aberration involving MAPK10 has been found in a single patient with pharmacoresistant epileptic encephalopathy. Translocation t(Y;4)(q11.2;q21) which causes MAPK10 truncation. {ECO:0000269|PubMed:16249883}.; TISSUE SPECIFICITY: Specific to a subset of neurons in the nervous system. Present in the hippocampus and areas, cerebellum, striatum, brain stem, and weakly in the spinal cord. Very weak expression in testis and kidney.; choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;brain;spinal ganglion;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;lung;adrenal gland;nasopharynx;hippocampus;macula lutea;kidney;stomach; amygdala;dorsal root ganglion;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;temporal lobe;caudate nucleus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.91846 0.62410 -0.449946534 24.00330267 24.35774 0.80097 MAPK11 0.472036682263674 0.526867071015643 0.00109624672068275 mitogen-activated protein kinase 11 FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK11 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK11 functions are mostly redundant with those of MAPK14. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane- associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Additional examples of p38 MAPK substrates are the FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. {ECO:0000269|PubMed:10330143, ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:15356147, ECO:0000269|PubMed:9430721, ECO:0000269|PubMed:9687510}.; . TISSUE SPECIFICITY: Highest levels in the brain and heart. Also expressed in the placenta, lung, liver, skeletal muscle, kidney and pancreas.; unclassifiable (Anatomical System);amygdala;ovary;colon;prostate;lung;frontal lobe;placenta;thyroid;duodenum;liver;testis;mammary gland;brain;stomach; dorsal root ganglion;superior cervical ganglion;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.59709 0.50513 -0.139478553 43.29440906 107.73914 2.25371 MAPK12 0.0136200575011183 0.979692625025979 0.00668731747290312 mitogen-activated protein kinase 12 FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in myoblast differentiation and also in the down-regulation of cyclin D1 in response to hypoxia in adrenal cells suggesting MAPK12 may inhibit cell proliferation while promoting differentiation. Phosphorylates DLG1. Following osmotic shock, MAPK12 in the cell nucleus increases its association with nuclear DLG1, thereby causing dissociation of DLG1-SFPQ complexes. This function is independent of its catalytic activity and could affect mRNA processing and/or gene transcription to aid cell adaptation to osmolarity changes in the environment. Regulates UV-induced checkpoint signaling and repair of UV-induced DNA damage and G2 arrest after gamma- radiation exposure. MAPK12 is involved in the regulation of SLC2A1 expression and basal glucose uptake in L6 myotubes; and negatively regulates SLC2A4 expression and contraction-mediated glucose uptake in adult skeletal muscle. C-Jun (JUN) phosphorylation is stimulated by MAPK14 and inhibited by MAPK12, leading to a distinct AP-1 regulation. MAPK12 is required for the normal kinetochore localization of PLK1, prevents chromosomal instability and supports mitotic cell viability. MAPK12-signaling is also positively regulating the expansion of transient amplifying myogenic precursor cells during muscle growth and regeneration. {ECO:0000269|PubMed:10848581, ECO:0000269|PubMed:14592936, ECO:0000269|PubMed:17724032, ECO:0000269|PubMed:20605917, ECO:0000269|PubMed:21172807, ECO:0000269|PubMed:8633070, ECO:0000269|PubMed:9430721}.; DISEASE: Note=MAPK is overexpressed in highly metastatic breast cancer cell lines and its expression is preferentially associated with basal-like and metastatic phenotypes of breast tumor samples.; TISSUE SPECIFICITY: Highly expressed in skeletal muscle and heart. {ECO:0000269|PubMed:11991731, ECO:0000269|PubMed:8633070}.; unclassifiable (Anatomical System);cartilage;salivary gland;muscle;fovea centralis;choroid;lens;skin;skeletal muscle;retina;pancreas;optic nerve;lung;endometrium;placenta;bone;macula lutea;liver;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.45860 0.43657 -0.354480518 29.42911064 776.33339 5.51752 MAPK13 5.48349848830244e-07 0.861251984262847 0.138747467387304 mitogen-activated protein kinase 13 FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK13 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK13 is one of the less studied p38 MAPK isoforms. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in the regulation of protein translation by phosphorylating and inactivating EEF2K. Involved in cytoskeletal remodeling through phosphorylation of MAPT and STMN1. Mediates UV irradiation induced up-regulation of the gene expression of CXCL14. Plays an important role in the regulation of epidermal keratinocyte differentiation, apoptosis and skin tumor development. Phosphorylates the transcriptional activator MYB in response to stress which leads to rapid MYB degradation via a proteasome-dependent pathway. MAPK13 also phosphorylates and down-regulates PRKD1 during regulation of insulin secretion in pancreatic beta cells. {ECO:0000269|PubMed:11500363, ECO:0000269|PubMed:11943212, ECO:0000269|PubMed:15632108, ECO:0000269|PubMed:17256148, ECO:0000269|PubMed:18006338, ECO:0000269|PubMed:18367666, ECO:0000269|PubMed:20478268, ECO:0000269|PubMed:9731215}.; . TISSUE SPECIFICITY: Expressed in testes, pancreas, small intestine, lung and kidney. Abundant in macrophages, also present in neutrophils, CD4+ T-cells, and endothelial cells. {ECO:0000269|PubMed:10201954, ECO:0000269|PubMed:9374491}.; medulla oblongata;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;cervix;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.36762 0.09211 -0.113792788 45.25831564 61.50802 1.59802 MAPK14 0.997467188213903 0.00253270979371188 1.01992385401025e-07 mitogen-activated protein kinase 14 FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK14 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. MAPK14 interacts also with casein kinase II, leading to its activation through autophosphorylation and further phosphorylation of TP53/p53. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF- induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin ligase SIAH2, regulating its activity towards EGLN3. MAPK14 may also inhibit the lysosomal degradation pathway of autophagy by interfering with the intracellular trafficking of the transmembrane protein ATG9. Another function of MAPK14 is to regulate the endocytosis of membrane receptors by different mechanisms that impinge on the small GTPase RAB5A. In addition, clathrin-mediated EGFR internalization induced by inflammatory cytokines and UV irradiation depends on MAPK14- mediated phosphorylation of EGFR itself as well as of RAB5A effectors. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF- kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Phosphorylates CDC25B and CDC25C which is required for binding to 14-3-3 proteins and leads to initiation of a G2 delay after ultraviolet radiation. Phosphorylates TIAR following DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA degradation. The p38 MAPKs may also have kinase-independent roles, which are thought to be due to the binding to targets in the absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14, and, although OGT does not seem to be phosphorylated by MAPK14, their interaction increases upon MAPK14 activation induced by glucose deprivation. This interaction may regulate OGT activity by recruiting it to specific targets such as neurofilament H, stimulating its O-Glc-N-acylation. Required in mid-fetal development for the growth of embryo-derived blood vessels in the labyrinth layer of the placenta. Also plays an essential role in developmental and stress-induced erythropoiesis, through regulation of EPO gene expression. Isoform MXI2 activation is stimulated by mitogens and oxidative stress and only poorly phosphorylates ELK1 and ATF2. Isoform EXIP may play a role in the early onset of apoptosis. Phosphorylates S100A9 at 'Thr-113'. {ECO:0000269|PubMed:10330143, ECO:0000269|PubMed:10747897, ECO:0000269|PubMed:10943842, ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:11333986, ECO:0000269|PubMed:15905572, ECO:0000269|PubMed:16932740, ECO:0000269|PubMed:17003045, ECO:0000269|PubMed:17724032, ECO:0000269|PubMed:19893488, ECO:0000269|PubMed:20188673, ECO:0000269|PubMed:20932473, ECO:0000269|PubMed:9430721, ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9792677, ECO:0000269|PubMed:9858528}.; . TISSUE SPECIFICITY: Brain, heart, placenta, pancreas and skeletal muscle. Expressed to a lesser extent in lung, liver and kidney.; myocardium;smooth muscle;ovary;colon;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;whole blood;trigeminal ganglion;skeletal muscle;bone marrow; 0.94805 0.91733 -0.161524709 41.6430762 22.88461 0.76322 MAPK15 1.28603703609388e-16 0.00287818334504674 0.997121816654953 mitogen-activated protein kinase 15 FUNCTION: In vitro, phosphorylates MBP. {ECO:0000269|PubMed:11875070, ECO:0000269|PubMed:16484222}.; . TISSUE SPECIFICITY: Widely expressed with a maximal expression in lung and kidney. {ECO:0000269|PubMed:11875070, ECO:0000269|PubMed:16484222}.; unclassifiable (Anatomical System);lung;ovary;endometrium;oesophagus;larynx;testis;colon;kidney;brain; . 0.15685 0.17839 0.565800595 81.72918141 972.94541 6.02994 MAPKAP1 0.999736598475665 0.00026340111431083 4.10023944900312e-10 mitogen-activated protein kinase associated protein 1 FUNCTION: Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient- insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Within mTORC2, MAPKAP1 is required for complex formation and mTORC2 kinase activity. MAPKAP1 inhibits MAP3K2 by preventing its dimerization and autophosphorylation. Inhibits HRAS and KRAS signaling. Enhances osmotic stress-induced phosphorylation of ATF2 and ATF2-mediated transcription. Involved in ciliogenesis, regulates cilia length through its interaction with CCDC28B independently of mTORC2 complex. {ECO:0000269|PubMed:15988011, ECO:0000269|PubMed:16962653, ECO:0000269|PubMed:17043309, ECO:0000269|PubMed:17054722, ECO:0000269|PubMed:17303383, ECO:0000269|PubMed:23727834}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in heart and skeletal muscle. {ECO:0000269|PubMed:15988011}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; testis - interstitial;testis - seminiferous tubule;testis;kidney;pons;atrioventricular node; 0.25319 0.27473 -0.712684326 14.49634348 48.85088 1.36353 MAPKAPK2 0.996185444591235 0.00381427837953776 2.77029226759295e-07 mitogen-activated protein kinase-activated protein kinase 2 FUNCTION: Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, ELAVL1, HNRNPA0, HSF1, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat- shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilize GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. {ECO:0000269|PubMed:10383393, ECO:0000269|PubMed:11844797, ECO:0000269|PubMed:12456657, ECO:0000269|PubMed:12565831, ECO:0000269|PubMed:14499342, ECO:0000269|PubMed:14517288, ECO:0000269|PubMed:15014438, ECO:0000269|PubMed:15629715, ECO:0000269|PubMed:16278218, ECO:0000269|PubMed:16456544, ECO:0000269|PubMed:17481585, ECO:0000269|PubMed:18021073, ECO:0000269|PubMed:20932473, ECO:0000269|PubMed:8093612, ECO:0000269|PubMed:8280084, ECO:0000269|PubMed:8774846}.; . TISSUE SPECIFICITY: Expressed in all tissues examined.; ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;amygdala;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.43299 0.18157 -0.648365105 16.35999056 4514.62293 13.48820 MAPKAPK3 2.71040946081621e-06 0.753371957230254 0.246625332360286 mitogen-activated protein kinase-activated protein kinase 3 FUNCTION: Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, cell migration, chromatin remodeling and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38- alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. MAPKAPK2 and MAPKAPK3, share the same function and substrate specificity, but MAPKAPK3 kinase activity and level in protein expression are lower compared to MAPKAPK2. Phosphorylates HSP27/HSPB1, KRT18, KRT20, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins, such as TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. Also acts as a modulator of Polycomb-mediated repression. {ECO:0000269|PubMed:10383393, ECO:0000269|PubMed:15563468, ECO:0000269|PubMed:18021073, ECO:0000269|PubMed:20599781, ECO:0000269|PubMed:8626550, ECO:0000269|PubMed:8774846}.; . TISSUE SPECIFICITY: Widely expressed, with a higher expression level observed in heart and skeletal muscle. No expression in brain. {ECO:0000269|PubMed:8622688, ECO:0000269|PubMed:8626550}.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pineal body;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;alveolus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; heart;skeletal muscle; 0.17159 0.16628 -0.249709319 35.74545883 16.06114 0.56832 MAPKAPK5 0.0234226025504899 0.973553774974803 0.00302362247470688 mitogen-activated protein kinase-activated protein kinase 5 FUNCTION: Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras- induced senescence and phosphorylating p53/TP53. Involved in post- transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement. {ECO:0000269|PubMed:17254968, ECO:0000269|PubMed:17728103, ECO:0000269|PubMed:19166925, ECO:0000269|PubMed:21329882, ECO:0000269|PubMed:9628874}.; . TISSUE SPECIFICITY: Expressed ubiquitously. {ECO:0000269|PubMed:9628874}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;lens;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; testis - interstitial;white blood cells;atrioventricular node; 0.52108 0.13844 -0.626318434 17.03231894 70.79113 1.75115 MAPKAPK5-AS1 . . . MAPKAPK5 antisense RNA 1 . . . . . . . . . . . MAPKAPK5P1 . . . mitogen-activated protein kinase-activated protein kinase 5 pseudogene 1 . . . . . . . . . . . MAPKBP1 0.999024889896837 0.000975110103157844 5.65832706858721e-15 mitogen-activated protein kinase binding protein 1 FUNCTION: Involved in JNK signaling pathway. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;fovea centralis;skin;skeletal muscle;retina;uterus;lung;frontal lobe;endometrium;thyroid;placenta;macula lutea;pituitary gland;hypopharynx;liver;testis;head and neck;germinal center;brain;cerebellum;thymus; amygdala;occipital lobe;olfactory bulb;fetal brain;cerebellum peduncles;prefrontal cortex;testis;skeletal muscle;cerebellum; 0.48838 0.09070 -0.650434134 16.15947157 2715.51858 9.81481 MAPRE1 0.968087388852693 0.0318618121412823 5.07990060250134e-05 microtubule associated protein RP/EB family member 1 FUNCTION: Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration. {ECO:0000269|PubMed:12388762, ECO:0000269|PubMed:16109370, ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:21646404}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10644998}.; . . 0.94827 0.14604 -0.249709319 35.74545883 25.09501 0.82104 MAPRE1P1 . . . MAPRE1 pseudogene 1 . . . . . . . . . . . MAPRE1P2 . . . MAPRE1 pseudogene 2 . . . . . . . . . . . MAPRE1P3 . . . MAPRE1 pseudogene 3 . . . . . . . . . . . MAPRE2 0.96964473730636 0.0303461554802575 9.10721338289419e-06 microtubule associated protein RP/EB family member 2 FUNCTION: May be involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in different tumor cell lines. Up- regulated in activated B- and T-lymphocytes. {ECO:0000269|PubMed:9233623}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;gall bladder;tonsil;amygdala;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;colon;parathyroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum;thymus; amygdala;whole brain;dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;atrioventricular node;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.80943 0.12479 -0.207437529 38.2814343 13.16819 0.47939 MAPRE3 0.799864407370243 0.19896424145679 0.00117135117296724 microtubule associated protein RP/EB family member 3 FUNCTION: Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity). {ECO:0000250, ECO:0000269|PubMed:19255245}.; . TISSUE SPECIFICITY: Predominantly expressed in brain and muscle. {ECO:0000269|PubMed:10644998}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;brain;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;pineal body;muscle;pharynx;blood;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;alveolus;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; amygdala;whole brain;medulla oblongata;occipital lobe;testis - interstitial;temporal lobe;pons;atrioventricular node;skeletal muscle;skin;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;cerebellum; 0.91834 0.11809 -0.273576253 33.97027601 0.75283 0.01312 MAPT 4.68264962282433e-05 0.962905044662688 0.0370481288410833 microtubule associated protein tau FUNCTION: Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N- terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. {ECO:0000269|PubMed:21985311}.; DISEASE: Note=In Alzheimer disease, the neuronal cytoskeleton in the brain is progressively disrupted and replaced by tangles of paired helical filaments (PHF) and straight filaments, mainly composed of hyperphosphorylated forms of TAU (PHF-TAU or AD P- TAU). O-GlcNAcylation is greatly reduced in Alzheimer disease brain cerebral cortex leading to an increase in TAU/MAPT phosphorylations. {ECO:0000269|PubMed:14517953}.; DISEASE: Frontotemporal dementia (FTD) [MIM:600274]: A form of dementia characterized by pathologic finding of frontotemporal lobar degeneration, presenile dementia with behavioral changes, deterioration of cognitive capacities and loss of memory. In some cases, parkinsonian symptoms are prominent. Neuropathological changes include frontotemporal atrophy often associated with atrophy of the basal ganglia, substantia nigra, amygdala. In most cases, protein tau deposits are found in glial cells and/or neurons. {ECO:0000269|PubMed:10208578, ECO:0000269|PubMed:10214944, ECO:0000269|PubMed:10489057, ECO:0000269|PubMed:10553987, ECO:0000269|PubMed:10802785, ECO:0000269|PubMed:11071507, ECO:0000269|PubMed:11117541, ECO:0000269|PubMed:11585254, ECO:0000269|PubMed:11889249, ECO:0000269|PubMed:11921059, ECO:0000269|PubMed:12473774, ECO:0000269|PubMed:12509859, ECO:0000269|PubMed:15883319, ECO:0000269|PubMed:16240366, ECO:0000269|PubMed:9629852, ECO:0000269|PubMed:9641683, ECO:0000269|PubMed:9736786, ECO:0000269|PubMed:9789048, ECO:0000269|PubMed:9973279}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pick disease of the brain (PIDB) [MIM:172700]: A rare form of dementia pathologically defined by severe atrophy, neuronal loss and gliosis. It is characterized by the occurrence of tau-positive inclusions, swollen neurons (Pick cells) and argentophilic neuronal inclusions known as Pick bodies that disproportionally affect the frontal and temporal cortical regions. Clinical features include aphasia, apraxia, confusion, anomia, memory loss and personality deterioration. {ECO:0000269|PubMed:10604746, ECO:0000269|PubMed:11089577, ECO:0000269|PubMed:11117542, ECO:0000269|PubMed:11601501, ECO:0000269|PubMed:11891833}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in MAPT are a cause of corticobasal degeneration (CBD). It is marked by extrapyramidal signs and apraxia and can be associated with memory loss. Neuropathologic features may overlap Alzheimer disease, progressive supranuclear palsy, and Parkinson disease.; DISEASE: Progressive supranuclear palsy 1 (PSNP1) [MIM:601104]: Characterized by akinetic-rigid syndrome, supranuclear gaze palsy, pyramidal tract dysfunction, pseudobulbar signs and cognitive capacities deterioration. Neurofibrillary tangles and gliosis but no amyloid plaques are found in diseased brains. Most cases appear to be sporadic, with a significant association with a common haplotype including the MAPT gene and the flanking regions. Familial cases show an autosomal dominant pattern of transmission with incomplete penetrance; genetic analysis of a few cases showed the occurrence of tau mutations, including a deletion of Asn-613. {ECO:0000269|PubMed:10534245, ECO:0000269|PubMed:11220749, ECO:0000269|PubMed:12325083, ECO:0000269|PubMed:14991828, ECO:0000269|PubMed:14991829, ECO:0000269|PubMed:16157753}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Parkinson-dementia syndrome (PARDE) [MIM:260540]: A syndrome characterized by parkinsonism, tremor, rigidity, dementia, ophthalmoparesis and pyramidal signs. Neurofibrillary degeneration occurs in the hippocampus, basal ganglia and brainstem nuclei. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in neurons. Isoform PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.; unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;prostate;optic nerve;whole body;lung;frontal lobe;synovium;macula lutea;visual apparatus;testis;cervix;kidney;brain;cerebellum; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.27076 0.92692 2.18457126 98.08917197 4302.22642 13.05898 MAPT-AS1 . . . MAPT antisense RNA 1 . . . . . . . . . . . MAPT-IT1 . . . MAPT intronic transcript 1 . . . . . . . . . . . MARC1 8.19879290549747e-05 0.767162606917133 0.232755405153812 mitochondrial amidoxime reducing component 1 FUNCTION: As a component of an N-hydroxylated prodrug-converting complex required to reduce N-hydroxylated prodrugs, such as benzamidoxime. Also able to reduce N(omega)-hydroxy-L-arginine (NOHA) and N(omega)-hydroxy-N(delta)-methyl-L-arginine (NHAM) into L-arginine and N(delta)-methyl-L-arginine, respectively. {ECO:0000269|PubMed:19053771}.; . . . . 0.46950 0.10047 0.108486928 61.90728946 413.54129 4.25865 MARC2 0.0326007029745028 0.926665497772998 0.0407337992524991 mitochondrial amidoxime reducing component 2 FUNCTION: As a component of the benzamidoxime prodrug-converting complex required to reduce N-hydroxylated prodrugs, such as benzamidoxime. Also able to reduce N(omega)-hydroxy-L-arginine (NOHA) and N(omega)-hydroxy-N(delta)-methyl-L-arginine (NHAM) into L-arginine and N(delta)-methyl-L-arginine, respectively. {ECO:0000269|PubMed:21029045}.; . . unclassifiable (Anatomical System);ovary;colon;parathyroid;retina;uterus;prostate;lung;hippocampus;liver;testis;spleen;kidney;brain;stomach; superior cervical ganglion;liver;ciliary ganglion;kidney;trigeminal ganglion; 0.14100 0.11466 -0.139478553 43.29440906 394.05308 4.17365 MARCH1 0.218777254594417 0.743415367083308 0.0378073783222749 membrane associated ring-CH-type finger 1 FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of TFRC, CD86, FAS and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. By constitutively ubiquitinating MHC class II proteins in immature dendritic cells, down-regulates their cell surface localization thus sequestering them in the intracellular endosomal system. {ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:18305173, ECO:0000269|PubMed:18389477, ECO:0000269|PubMed:19117940}.; . TISSUE SPECIFICITY: Expressed in antigen presenting cells, APCs, located in lymph nodes and spleen. Also expressed in lung. Expression is high in follicular B-cells, moderate in dendritic cells and low in splenic T-cells. {ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:17255932}.; unclassifiable (Anatomical System);lung;heart;placenta;testis;brain; dorsal root ganglion;superior cervical ganglion;uterus corpus;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;parietal lobe; 0.18151 0.08172 0.038710339 56.92380278 232.12956 3.29476 MARCH2 0.246993249094028 0.72329629624302 0.0297104546629523 membrane associated ring-CH-type finger 2 FUNCTION: E3 ubiquitin-protein ligase that may mediate ubiquitination of TFRC and CD86, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May be involved in endosomal trafficking through interaction with STX6. {ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:15689499, ECO:0000269|PubMed:16428329}.; . TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:14722266}.; lymphoreticular;medulla oblongata;ovary;umbilical cord;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;pharynx;blood;lens;lung;cornea;nasopharynx;macula lutea;visual apparatus;liver;kidney;mammary gland; . 0.25198 . -0.025608647 51.91672564 2146.33729 8.52150 MARCH3 0.636727871339738 0.356542253419104 0.00672987524115773 membrane associated ring-CH-type finger 3 FUNCTION: E3 ubiquitin-protein ligase which may be involved in endosomal trafficking. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (By similarity). {ECO:0000250}.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;stomach; superior cervical ganglion;testis; 0.73374 0.11466 -0.426079032 25.36565228 76.02084 1.82692 MARCH4 0.0162584104874255 0.959386499212039 0.0243550903005355 membrane associated ring-CH-type finger 4 FUNCTION: E3 ubiquitin-protein ligase that may mediate ubiquitination of MHC-I and CD4, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. {ECO:0000269|PubMed:14722266}.; . TISSUE SPECIFICITY: Expressed in brain and placenta. {ECO:0000269|PubMed:14722266}.; unclassifiable (Anatomical System);bile duct;pancreas;lung;cartilage;ovary;islets of Langerhans;placenta;liver;parathyroid;brain;skin; dorsal root ganglion;subthalamic nucleus;medulla oblongata;superior cervical ganglion;appendix;pons;trigeminal ganglion; 0.19753 0.10475 -0.670411825 15.61689078 48.17156 1.35230 MARCH5 0.898062228933406 0.101744126269002 0.000193644797592168 membrane associated ring-CH-type finger 5 FUNCTION: Mitochondrial E3 ubiquitin-protein ligase that plays a crucial role in the control of mitochondrial morphology by acting as a positive regulator of mitochondrial fission. May play a role in the prevention of cell senescence acting as a regulator of mitochondrial quality control. Promotes ubiquitination of FIS1, DNM1L and MFN1. {ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:17606867, ECO:0000269|PubMed:19741096, ECO:0000269|PubMed:20103533}.; . TISSUE SPECIFICITY: Expressed in brain, heart, liver, lung, spleen, stomach, testis, skeletal and muscle. {ECO:0000269|PubMed:16874301}.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;muscle;pancreas;lung;pia mater;cornea;placenta;hippocampus;duodenum;hypopharynx;amnion;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skeletal muscle; 0.55418 0.11809 -0.141298762 42.87567823 13.96731 0.50650 MARCH6 0.999995976388274 4.02361172603786e-06 1.28071470223936e-16 membrane associated ring-CH-type finger 6 FUNCTION: E3 ubiquitin-protein ligase that promotes ubiquitination of DIO2, leading to its degradation. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May cooperate with UBE2G1. {ECO:0000269|PubMed:15673284, ECO:0000269|PubMed:19651899}.; . TISSUE SPECIFICITY: Present in brain (at protein level). {ECO:0000269|PubMed:15673284}.; ovary;skin;retina;bone marrow;prostate;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;superior cervical ganglion;testis - seminiferous tubule;placenta;prefrontal cortex;testis;pons;parietal lobe;cingulate cortex;cerebellum; 0.27751 0.13948 -0.558357437 19.54470394 27.26345 0.87856 MARCH7 0.977026371329949 0.0229734414286718 1.87241379041223e-07 membrane associated ring-CH-type finger 7 FUNCTION: E3 ubiquitin-protein ligase which may specifically enhance the E2 activity of HIP2. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. {ECO:0000269|PubMed:16868077}.; . . ovary;salivary gland;colon;skin;bone marrow;uterus;prostate;whole body;cochlea;larynx;bone;thyroid;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;spinal cord;pharynx;blood;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;thyroid;testis;atrioventricular node;whole blood;trigeminal ganglion;skeletal muscle; 0.24486 0.24407 0.734883636 86.29983487 1245.25743 6.66630 MARCH8 1.37263384630584e-05 0.395762596776184 0.604223676885353 membrane associated ring-CH-type finger 8 FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of CD86 and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. May also promote ubiquitination and endocytosis of TFRC and FAS. {ECO:0000269|PubMed:12582153, ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:18389477, ECO:0000269|PubMed:19117940, ECO:0000269|PubMed:19566897}.; . TISSUE SPECIFICITY: Broadly expressed. Present in immature dendritic cells (at protein level). {ECO:0000269|PubMed:12582153, ECO:0000269|PubMed:14722266}.; unclassifiable (Anatomical System);medulla oblongata;lymph node;ovary;colon;parathyroid;blood;skin;skeletal muscle;retina;bone marrow;uterus;lung;placenta;visual apparatus;liver;testis;spleen;germinal center;kidney;thymus; fetal liver;superior cervical ganglion;bone marrow; 0.10231 0.10000 0.68351529 85.03774475 3469.57167 11.33868 MARCH9 0.350280135696905 0.636540752048736 0.0131791122543586 membrane associated ring-CH-type finger 9 FUNCTION: E3 ubiquitin-protein ligase that may mediate ubiquitination of MHC-I, CD4 and ICAM1, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. {ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:17174307}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:14722266}.; ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;bone;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;muscle;blood;lens;pancreas;lung;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.20905 0.11158 . . 32.43835 1.01273 MARCH10 3.44665140099752e-16 0.00514147708469985 0.9948585229153 membrane associated ring-CH-type finger 10 FUNCTION: E3 ubiquitin-protein ligase (Probable). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. {ECO:0000305}.; . . unclassifiable (Anatomical System);lung;endometrium;testis;kidney; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.04149 . 1.804178316 96.93913659 4640.20063 13.70158 MARCH11 0.0024662431250002 0.778180214452812 0.219353542422188 membrane associated ring-CH-type finger 11 FUNCTION: E3 ubiquitin-protein ligase that mediates polyubiquitination of CD4. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May play a role in ubuquitin-dependent protein sorting in developmenting spermatids (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;testis;kidney; . . . . . 20.69433 0.70249 MARCKS 0.266490060221299 0.636923987194479 0.0965859525842222 myristoylated alanine rich protein kinase C substrate FUNCTION: MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein.; . . . . 0.57210 0.35330 . . 121.70769 2.40288 MARCKSL1 0.653774932497598 0.321362497202042 0.0248625703003598 MARCKS-like 1 FUNCTION: Controls cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation. When unphosphorylated, induces cell migration. When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration. May also affect cancer cell migration. May be involved in coupling the protein kinase C and calmodulin signal transduction systems (By similarity). {ECO:0000250}.; . . . . 0.61449 0.17821 -0.273576253 33.97027601 27.31638 0.87992 MARCKSL1P1 . . . MARCKS-like 1 pseudogene 1 . . . . . . . . . . . MARCKSL1P2 . . . MARCKS-like 1 pseudogene 2 . . . . . . . . . . . MARCKSP1 . . . myristoylated alanine-rich protein kinase C substrate pseudogene 1 . . . . . . . . . . . MARCO 6.41628014969988e-08 0.872393291168398 0.1276066446688 macrophage receptor with collagenous structure FUNCTION: Pattern recognition receptor (PRR). Binds Gram-positive and Gram-negative bacteria.; . . unclassifiable (Anatomical System);pancreas;lung;cartilage;ovary;placenta;liver;alveolus;testis;colon;spleen;brain; lymph node; 0.06400 0.24721 -0.374708069 28.15522529 845.48074 5.68855 MARK1 0.990825675842053 0.00917432399543601 1.62510777359466e-10 microtubule affinity regulating kinase 1 FUNCTION: Serine/threonine-protein kinase involved in cell polarity and microtubule dynamics regulation. Phosphorylates DCX, MAP2, MAP4 and MAPT/TAU. Involved in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). {ECO:0000269|PubMed:11433294, ECO:0000269|PubMed:17573348}.; DISEASE: Note=Genetic variations in MARK1 may be associated with susceptibility to autism. MARK1 is overexpressed in the prefrontal cortex of patients with autism and causes changes in the function of cortical dendrites.; TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, brain, fetal brain and fetal kidney. {ECO:0000269|PubMed:9108484}.; . . 0.45401 0.13142 -0.314027422 31.9297004 747.99292 5.42594 MARK2 0.999900854654153 9.91453381702912e-05 7.67654020875497e-12 microtubule affinity regulating kinase 2 FUNCTION: Serine/threonine-protein kinase involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4, MAPT/TAU, and RAB11FIP2. Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule- dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells. {ECO:0000269|PubMed:11433294, ECO:0000269|PubMed:12429843, ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15158914, ECO:0000269|PubMed:15324659, ECO:0000269|PubMed:15365179, ECO:0000269|PubMed:16775013, ECO:0000269|PubMed:16980613, ECO:0000269|PubMed:18626018, ECO:0000269|PubMed:20194617}.; . TISSUE SPECIFICITY: High levels of expression in heart, brain, skeletal muscle and pancreas, lower levels observed in lung, liver and kidney. {ECO:0000269|PubMed:9730619}.; ovary;salivary gland;colon;parathyroid;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;muscle;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; medulla oblongata;placenta;prefrontal cortex;globus pallidus;ciliary ganglion;pons;trigeminal ganglion; 0.39504 0.34562 -0.712684326 14.49634348 15.77604 0.56200 MARK2P1 . . . microtubule affinity regulating kinase 2 pseudogene 1 . . . . . . . . . . . MARK2P2 . . . microtubule affinity regulating kinase 2 pseudogene 2 . . . . . . . . . . . MARK2P3 . . . microtubule affinity regulating kinase 2 pseudogene 3 . . . . . . . . . . . MARK2P4 . . . microtubule affinity regulating kinase 2 pseudogene 4 . . . . . . . . . . . MARK2P5 . . . microtubule affinity regulating kinase 2 pseudogene 5 . . . . . . . . . . . MARK2P6 . . . microtubule affinity regulating kinase 2 pseudogene 6 . . . . . . . . . . . MARK2P7 . . . microtubule affinity regulating kinase 2 pseudogene 7 . . . . . . . . . . . MARK2P8 . . . microtubule affinity regulating kinase 2 pseudogene 8 . . . . . . . . . . . MARK2P9 . . . microtubule affinity regulating kinase 2 pseudogene 9 . . . . . . . . . . . MARK2P10 . . . microtubule affinity regulating kinase 2 pseudogene 10 . . . . . . . . . . . MARK2P11 . . . microtubule affinity regulating kinase 2 pseudogene 11 . . . . . . . . . . . MARK2P12 . . . microtubule affinity regulating kinase 2 pseudogene 12 . . . . . . . . . . . MARK2P13 . . . microtubule affinity regulating kinase 2 pseudogene 13 . . . . . . . . . . . MARK2P14 . . . microtubule affinity regulating kinase 2 pseudogene 14 . . . . . . . . . . . MARK2P15 . . . microtubule affinity regulating kinase 2 pseudogene 15 . . . . . . . . . . . MARK2P16 . . . microtubule affinity regulating kinase 2 pseudogene 16 . . . . . . . . . . . MARK2P17 . . . microtubule affinity regulating kinase 2 pseudogene 17 . . . . . . . . . . . MARK3 6.11449031625676e-05 0.999709581869532 0.000229273227305541 microtubule affinity regulating kinase 3 FUNCTION: Involved in the specific phosphorylation of microtubule- associated proteins for tau, MAP2 and MAP4. Phosphorylates CDC25C on 'Ser-216'. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. {ECO:0000269|PubMed:16980613}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; occipital lobe;subthalamic nucleus;globus pallidus;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.39837 0.16331 -0.686998355 15.26893135 323.68369 3.82357 MARK3P1 . . . microtubule affinity regulating kinase 3 pseudogene 1 . . . . . . . . . . . MARK3P2 . . . microtubule affinity regulating kinase 3 pseudogene 2 . . . . . . . . . . . MARK3P3 . . . microtubule affinity regulating kinase 3 pseudogene 3 . . . . . . . . . . . MARK4 0.999932135718548 6.78642663847999e-05 1.5067507803828e-11 microtubule affinity regulating kinase 4 . . TISSUE SPECIFICITY: Ubiquitous. Isoform 2 is brain-specific. {ECO:0000269|PubMed:11326310}.; ovary;salivary gland;colon;parathyroid;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;tongue;pineal body;muscle;blood;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; whole brain;amygdala;occipital lobe;superior cervical ganglion;thalamus;medulla oblongata;testis - interstitial;temporal lobe;caudate nucleus;pons;subthalamic nucleus;testis - seminiferous tubule;fetal brain;prefrontal cortex;globus pallidus;testis;parietal lobe;cingulate cortex;cerebellum; 0.53977 0.13986 -0.979072682 8.752064166 41.9327 1.22179 MARS 2.73685367110748e-12 0.964698031023982 0.0353019689732809 methionyl-tRNA synthetase . DISEASE: Interstitial lung and liver disease (ILLD) [MIM:615486]: An autosomal recessive, life-threatening disorder characterized by respiratory insufficiency and progressive liver disease with onset in infancy or early childhood. Clinical features include failure to thrive, hypotonia, intermittent lactic acidosis, aminoaciduria, hypothyroidism, interstitial lung disease, pulmonary alveolar proteinosis, anemia, and liver canalicular cholestasis, steatosis, and iron deposition. {ECO:0000269|PubMed:24103465}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease 2U (CMT2U) [MIM:616280]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. CMT2U is a slowly progressive, autosomal dominant form characterized by late-adult onset. {ECO:0000269|PubMed:23729695, ECO:0000269|PubMed:24354524}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;urinary;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;pons;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.65836 0.50194 -0.971800989 8.946685539 107.62904 2.25222 MARS2 1.41647403486977e-06 0.616210322245082 0.383788261280883 methionyl-tRNA synthetase 2, mitochondrial . DISEASE: Spastic ataxia 3, autosomal recessive (SPAX3) [MIM:611390]: A neurologic disorder characterized by cerebellar ataxia, ataxic gait, spasticity, and hyperreflexia. Other variable features include dysarthria, dysmetria, mild cognitive impairment, urinary urgency and dystonic positioning. {ECO:0000269|PubMed:22448145}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Combined oxidative phosphorylation deficiency 25 (COXPD25) [MIM:616430]: A mitochondrial disorder resulting in developmental delay, growth failure, and sensorineural hearing loss. {ECO:0000269|PubMed:25754315}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;skeletal muscle;bone marrow;uterus;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;cervix;germinal center;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.08629 0.19271 -0.844966979 11.1759849 108.54012 2.26044 MARVELD1 . . . MARVEL domain containing 1 FUNCTION: Microtubule-associated protein that exhibits cell cycle- dependent localization and can inhibit cell proliferation and migration. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed in normal tissues. Down- regulated in multiple primary tumors. {ECO:0000269|PubMed:19364627}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; . 0.18825 0.13502 . . 4.39773 0.15990 MARVELD2 4.23034393772305e-11 0.0964769530251862 0.90352304693251 MARVEL domain containing 2 FUNCTION: Plays a role in the formation of the epithelial barriers. The separation of the endolymphatic and perilymphatic spaces of the organ of Corti from one another by epithelial barriers is required for normal hearing. {ECO:0000269|PubMed:17186462}.; DISEASE: Deafness, autosomal recessive, 49 (DFNB49) [MIM:610153]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:17186462}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);breast;lung;islets of Langerhans;thyroid;placenta;liver;spleen;blood; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.45607 0.10461 -0.354480518 29.42911064 903.85534 5.85375 MARVELD3 0.000303793592671722 0.803405490278026 0.196290716129303 MARVEL domain containing 3 FUNCTION: As a component of tight junctions, plays a role in paracellular ion conductivity. {ECO:0000269|PubMed:20028514}.; . . unclassifiable (Anatomical System);ovary;tongue;islets of Langerhans;colon;parathyroid;prostate;lung;endometrium;placenta;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skin;cingulate cortex; 0.35452 0.08177 0.066214104 58.95848077 3563.83766 11.54287 MAS1 0.000870823408355688 0.560125759420113 0.439003417171532 MAS1 proto-oncogene, G protein-coupled receptor FUNCTION: Receptor for angiotensin 1-7 (By similarity). Acts specifically as a functional antagonist of AGTR1 (angiotensin-2 type 1 receptor), although it up-regulates AGTR1 receptor levels. Positive regulation of AGTR1 levels occurs through activation of the G-proteins GNA11 and GNAQ, and stimulation of the protein kinase C signaling cascade. The antagonist effect on AGTR1 function is probably due to AGTR1 being physically altered by MAS1. {ECO:0000250, ECO:0000269|PubMed:15809376, ECO:0000269|PubMed:16611642}.; DISEASE: Note=The MAS oncogene has a weak focus-inducing activity in transfected NIH 3T3 cells. {ECO:0000269|PubMed:3708691}.; . . . 0.08027 0.19012 -0.778825328 12.88039632 31.19407 0.98423 MAS1L 0.000466205666114264 0.430965835589735 0.568567958744151 MAS1 proto-oncogene like, G protein-coupled receptor . . . . . 0.10087 . 1.574555842 95.73602265 62.56808 1.61699 MAS1LP1 . . . MAS1L pseudogene 1 . . . . . . . . . . . MASP1 9.74280364714267e-06 0.984728107220104 0.0152621499762488 mannan binding lectin serine peptidase 1 FUNCTION: Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5. {ECO:0000269|PubMed:11485744}.; DISEASE: 3MC syndrome 1 (3MC1) [MIM:257920]: A disorder characterized by facial dysmorphism that includes hypertelorism, blepharophimosis, blepharoptosis and highly arched eyebrows, cleft lip and/or palate, craniosynostosis, learning disability and genital, limb and vesicorenal anomalies. The term 3MC syndrome includes Carnevale, Mingarelli, Malpuech, and Michels syndromes. {ECO:0000269|PubMed:21258343}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Protein of the plasma which is primarily expressed by liver. {ECO:0000269|PubMed:11485744, ECO:0000269|PubMed:8018603, ECO:0000269|PubMed:8240317, ECO:0000269|PubMed:9367419}.; unclassifiable (Anatomical System);heart;muscle;colon;skin;skeletal muscle;uterus;prostate;lung;endometrium;nasopharynx;placenta;bone;liver;testis;spleen;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.29873 0.17266 -0.630196893 16.8141071 551.38054 4.77477 MASP2 1.58468707892368e-14 0.00685741965318751 0.993142580346796 mannan binding lectin serine peptidase 2 FUNCTION: Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase. {ECO:0000269|PubMed:10946292}.; DISEASE: MASP2 deficiency (MASPD) [MIM:613791]: A disorder that results in autoimmune manifestations, recurrent severe infections, and chronic inflammatory disease. {ECO:0000269|PubMed:12904520, ECO:0000269|PubMed:17252003}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma.; . . 0.12363 0.19027 0.942426495 89.89148384 1037.81374 6.18949 MAST1 0.999999024385856 9.75614144330927e-07 2.00678648960552e-17 microtubule associated serine/threonine kinase 1 FUNCTION: Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins (By similarity). {ECO:0000250|UniProtKB:Q9R1L5}.; . . unclassifiable (Anatomical System);ovary;sympathetic chain;muscle;parathyroid;fovea centralis;choroid;lens;retina;uterus;optic nerve;lung;frontal lobe;placenta;bone;macula lutea;visual apparatus;pituitary gland;cervix;brain;stomach;peripheral nerve; amygdala;whole brain;medulla oblongata;occipital lobe;superior cervical ganglion;cerebellum peduncles;temporal lobe;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.49290 0.10962 -1.905192093 1.940316112 47.92543 1.34473 MAST2 5.44402882251562e-11 0.999978456635017 2.15433105424678e-05 microtubule associated serine/threonine kinase 2 FUNCTION: Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins. Functions in a multi-protein complex in spermatid maturation. Regulates lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B activation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Abundant in the testis. {ECO:0000269|PubMed:8902215}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;spleen;kidney;mammary gland;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.34982 0.10610 -0.158112528 41.92026421 5581.08597 15.44690 MAST3 0.998925260617839 0.00107473936101564 2.11449286865648e-11 microtubule associated serine/threonine kinase 3 . . . unclassifiable (Anatomical System);amygdala;ovary;islets of Langerhans;colon;blood;fovea centralis;skin;bone marrow;prostate;lung;frontal lobe;endometrium;bone;placenta;macula lutea;liver;testis;germinal center;kidney;brain;mammary gland;stomach; amygdala;whole brain;subthalamic nucleus;thalamus;medulla oblongata;occipital lobe;temporal lobe;prefrontal cortex;globus pallidus;pons;caudate nucleus;parietal lobe;cingulate cortex; 0.30471 0.11609 -1.54510635 3.30856334 517.24571 4.64990 MAST4 0.00813023877986137 0.991869761152038 6.81004097743866e-11 microtubule associated serine/threonine kinase family member 4 . . TISSUE SPECIFICITY: Highly expressed in most normal human tissues, with an exception of in testis, small intestine, colon and peripheral blood leukocyte. {ECO:0000269|PubMed:17086981}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;urinary;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;tongue;prefrontal cortex;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion; 0.25200 0.08190 -0.21518231 37.7034678 1048.70314 6.21915 MAST4-AS1 . . . MAST4 antisense RNA 1 . . . . . . . . . . . MAST4-IT1 . . . MAST4 intronic transcript 1 . . . . . . . . . . . MASTL 1.08232471911869e-08 0.761360383627881 0.238639605548872 microtubule associated serine/threonine kinase like FUNCTION: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited. Phosphorylates histone protein in vitro; however such activity is unsure in vivo. May be involved in megakaryocyte differentiation. {ECO:0000269|PubMed:12890928, ECO:0000269|PubMed:19680222, ECO:0000269|PubMed:19793917, ECO:0000269|PubMed:20538976, ECO:0000269|PubMed:20818157}.; DISEASE: Thrombocytopenia 2 (THC2) [MIM:188000]: Thrombocytopenia is defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting. {ECO:0000269|PubMed:12890928}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;tongue;adrenal cortex;colon;skin;skeletal muscle;retina;uterus;endometrium;bone;placenta;visual apparatus;liver;head and neck;spleen;cervix;germinal center;aorta;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.29611 0.11101 1.137205722 92.32719981 709.51008 5.29096 MAT1A 0.754129517901618 0.24544038143215 0.000430100666232146 methionine adenosyltransferase 1A FUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP.; DISEASE: Methionine adenosyltransferase deficiency (MATD) [MIM:250850]: An inborn error of metabolism resulting in isolated hypermethioninemia. Most patients have no clinical abnormalities, although some neurologic symptoms may be present in rare cases with severe loss of methionine adenosyltransferase activity. {ECO:0000269|PubMed:10677294, ECO:0000269|PubMed:7560086, ECO:0000269|PubMed:8770875, ECO:0000269|PubMed:9042912}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in liver.; . . 0.91599 0.37582 -0.780646273 12.77423921 20.15228 0.68946 MAT2A 0.733230032010008 0.266224105220222 0.000545862769770294 methionine adenosyltransferase 2A FUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP.; . . lymphoreticular;ovary;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;muscle;blood;breast;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;globus pallidus; 0.81185 0.31462 -0.516085732 21.20193442 4.73287 0.17259 MAT2B 0.252497397412429 0.741318276446667 0.00618432614090406 methionine adenosyltransferase 2B FUNCTION: Non-catalytic regulatory subunit of S-adenosylmethionine synthetase 2 (MAT2A), an enzyme that catalyzes the formation of S- adenosylmethionine from methionine and ATP. Regulates the activity of S-adenosylmethionine synthetase 2 by changing its kinetic properties, rendering the enzyme more susceptible to S- adenosylmethionine inhibition. {ECO:0000269|PubMed:10644686}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10644686, ECO:0000269|PubMed:11337507}.; medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;germinal center;bladder;brain;heart;pharynx;blood;lens;breast;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach; superior cervical ganglion;occipital lobe;globus pallidus;kidney;whole blood;parietal lobe; 0.76157 0.29199 -0.337894035 30.37272942 31.67303 0.99678 MATK 0.000234672612755097 0.995791087480245 0.0039742399069995 megakaryocyte-associated tyrosine kinase FUNCTION: Could play a significant role in the signal transduction of hematopoietic cells. May regulate tyrosine kinase activity of SRC-family members in brain by specifically phosphorylating their C-terminal regulatory tyrosine residue which acts as a negative regulatory site. It may play an inhibitory role in the control of T-cell proliferation. {ECO:0000269|PubMed:9171348}.; . TISSUE SPECIFICITY: Expressed in various myeloid cell lines, detected in brain and lung.; unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;fovea centralis;choroid;lens;retina;optic nerve;lung;placenta;bone;macula lutea;visual apparatus;testis;spleen;kidney;brain; amygdala;cingulate cortex; 0.59292 . -0.554717505 19.79830149 318.0379 3.78730 MATN1 0.00527398583990045 0.892018470061123 0.102707544098976 matrilin 1, cartilage matrix protein FUNCTION: Cartilage matrix protein is a major component of the extracellular matrix of non-articular cartilage. It binds to collagen.; . . . . 0.21978 0.16522 -0.754958418 13.57631517 93.06889 2.07356 MATN1-AS1 . . . MATN1 antisense RNA 1 . . . . . . . . . . . MATN2 7.29384689107479e-09 0.96901464096881 0.0309853517373436 matrilin 2 FUNCTION: Involved in matrix assembly. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;heart;small intestine;islets of Langerhans;pineal body;sympathetic chain;colon;parathyroid;skin;skeletal muscle;retina;bile duct;prostate;whole body;lung;cochlea;larynx;thyroid;placenta;visual apparatus;liver;testis;head and neck;kidney;brain;stomach; dorsal root ganglion;uterus;superior cervical ganglion;olfactory bulb;thyroid;testis;appendix;ciliary ganglion;trigeminal ganglion; 0.20800 0.10274 1.212491971 93.06440198 3407.60054 11.18430 MATN3 1.61181027463323e-06 0.411332992198478 0.588665395991247 matrilin 3 FUNCTION: Major component of the extracellular matrix of cartilage and may play a role in the formation of extracellular filamentous networks.; DISEASE: Spondyloepimetaphyseal dysplasia MATN3-related (SEMD- MATN3) [MIM:608728]: A bone disease characterized by disproportionate early-onset dwarfism, bowing of the lower limbs, lumbar lordosis and normal hands. Skeletal abnormalities include short, wide and stocky long bones with severe epiphyseal and metaphyseal changes, hypoplastic iliac bones and flat, ovoid vertebral bodies. {ECO:0000269|PubMed:15121775}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteoarthritis 2 (OS2) [MIM:140600]: A degenerative disease of the joints characterized by degradation of the hyaline articular cartilage and remodeling of the subchondral bone with sclerosis. Clinical symptoms include pain and joint stiffness often leading to significant disability and joint replacement. In the hand, osteoarthritis can develop in the distal interphalangeal and the first carpometacarpal (base of thumb) and proximal interphalangeal joints. Patients with osteoarthritis may have one, a few, or all of these sites affected. {ECO:0000269|PubMed:12736871}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed only in cartilaginous tissues, such as vertebrae, ribs and shoulders.; . . 0.11303 0.12928 0.486911049 79.46449634 344.1362 3.93478 MATN4 9.70350471147918e-05 0.939351156678841 0.0605518082740442 matrilin 4 FUNCTION: Major component of the extracellular matrix of cartilage.; . TISSUE SPECIFICITY: Embryonic kidney, lung and placenta.; unclassifiable (Anatomical System);whole body;cartilage;skin; superior cervical ganglion;skeletal muscle; 0.24344 . 1.289723716 93.85468271 5885.50575 15.88894 MATR3 0.999818897618359 0.000181102217028636 1.64612773735409e-10 matrin 3 FUNCTION: May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. {ECO:0000269|PubMed:11525732}.; DISEASE: Amyotrophic lateral sclerosis 21 (ALS21) [MIM:606070]: A neurodegenerative disorder affecting upper and lower motor neurons, resulting in muscle weakness and respiratory failure. Some patients may develop myopathic features or dementia. {ECO:0000269|PubMed:19344878, ECO:0000269|PubMed:24686783, ECO:0000269|PubMed:25771394}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;lymphoreticular;ovary;umbilical cord;adrenal medulla;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;amygdala;heart;cartilage;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;colon;fovea centralis;uterus;whole body;oesophagus;cerebral cortex;larynx;bone;pituitary gland;testis;dura mater;spinal ganglion;artery;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;mesenchyma;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;cerebellum; amygdala;thalamus;medulla oblongata;occipital lobe;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.72582 . -0.648365105 16.35999056 27.25144 0.87802 MAU2 0.999717755369344 0.000282244532479343 9.81762562435626e-11 MAU2 sister chromatid cohesion factor FUNCTION: Required for association of the cohesin complex with chromatin during interphase. Plays a role in sister chromatid cohesion and normal progression through prometaphase. {ECO:0000269|PubMed:16682347, ECO:0000269|PubMed:16802858}.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;iris;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;cerebellum; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle;cerebellum; 0.26949 . -0.758599262 13.32861524 16.10564 0.57035 MAVS 1.76704995629944e-07 0.23925895739706 0.760740865897944 mitochondrial antiviral signaling protein FUNCTION: Required for innate immune defense against viruses. Acts downstream of DDX58/RIG-I and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFN-beta and RANTES (CCL5). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state. Upon viral infection, peroxisomal MAVS induces the rapid interferon- independent expression of defense factors that provide short-term protection, whereas mitochondrial MAVS activates an interferon- dependent signaling pathway with delayed kinetics, which amplifies and stabilizes the antiviral response. May activate the same pathways following detection of extracellular dsRNA by TLR3. May protect cells from apoptosis. {ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453, ECO:0000269|PubMed:16153868, ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:20451243}.; . TISSUE SPECIFICITY: Present in T-cells, monocytes, epithelial cells and hepatocytes (at protein level). Ubiquitously expressed, with highest levels in heart, skeletal muscle, liver, placenta and peripheral blood leukocytes. {ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453, ECO:0000269|PubMed:16153868}.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;larynx;bone;thyroid;iris;testis;brain;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;head and neck;cervix;kidney;stomach; . . . 0.137810868 63.63529134 5516.18319 15.32413 MAX 0.951898293348912 0.0479607736451581 0.000140933005929462 MYC associated factor X FUNCTION: Transcription regulator. Forms a sequence-specific DNA- binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a repressor. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity.; . TISSUE SPECIFICITY: High levels found in the brain, heart and lung while lower levels are seen in the liver, kidney and skeletal muscle.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; occipital lobe;superior cervical ganglion;heart;atrioventricular node;trigeminal ganglion;whole blood;cingulate cortex;cerebellum; 0.25005 0.57266 -0.229483771 36.86010852 6.72855 0.24787 MAZ 0.953969621751156 0.0459041105514777 0.000126267697366157 MYC associated zinc finger protein FUNCTION: May function as a transcription factor with dual roles in transcription initiation and termination. Binds to two sites, ME1a1 and ME1a2, within the MYC promoter having greater affinity for the former. Also binds to multiple G/C-rich sites within the promoter of the Sp1 family of transcription factors. Regulates inflammation-induced expression of serum amyloid A proteins. {ECO:0000269|PubMed:12270922}.; . TISSUE SPECIFICITY: Present in kidney, liver and brain. In the brain, highest levels are found in motor cortex and midfrontal cortex (at protein level). {ECO:0000269|PubMed:10727212}.; lymphoreticular;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;epididymis;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;occipital lobe;subthalamic nucleus;medulla oblongata;cerebellum peduncles;temporal lobe;prefrontal cortex;caudate nucleus;pons;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.32161 0.20668 . . 18.8914 0.65240 MB 0.337840557859152 0.602220324586096 0.0599391175547518 myoglobin FUNCTION: Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.; . . unclassifiable (Anatomical System);myocardium;heart;tongue;muscle;fovea centralis;choroid;lens;skeletal muscle;retina;greater omentum;prostate;optic nerve;whole body;lung;macula lutea;visual apparatus;liver;testis;head and neck;spleen;thymus; superior cervical ganglion;heart;tongue;thyroid;skeletal muscle; 0.15813 0.61197 -0.273576253 33.97027601 9.27312 0.33958 MB21D1 2.61494381328063e-05 0.524465993746887 0.47550785681498 Mab-21 domain containing 1 FUNCTION: Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (cGAMP) from ATP and GTP. Catalysis involves both the formation of a 2',5' phosphodiester linkage at the GpA step and the formation of a 3',5' phosphodiester linkage at the ApG step, producing c[G(2',5')pA(3',5')p]. Has antiviral activity by acting as a key cytosolic DNA sensor, the presence of double- stranded DNA (dsDNA) in the cytoplasm being a danger signal that triggers the immune responses. Binds cytosolic DNA directly, leading to activation and synthesis of cGAMP, a second messenger that binds to and activates TMEM173/STING, thereby triggering type-I interferon production. cGAMP can be transferred between cells by virtue of packaging within viral particles contributing to IFN-induction in newly infected cells in a cGAS-independent but TMEM173/STING-dependent manner (PubMed:26229115). {ECO:0000269|PubMed:21478870, ECO:0000269|PubMed:23258413, ECO:0000269|PubMed:23707061, ECO:0000269|PubMed:23707065, ECO:0000269|PubMed:23722159, ECO:0000269|PubMed:24116191, ECO:0000269|PubMed:24462292, ECO:0000269|PubMed:25131990, ECO:0000269|PubMed:26229115, ECO:0000269|PubMed:26300263}.; . TISSUE SPECIFICITY: Expressed in the monocytic cell line THP1. {ECO:0000269|PubMed:23258413}.; prostate;lung;liver;alveolus;testis;cervix;spleen;brain; superior cervical ganglion;globus pallidus; 0.04939 . 0.240763792 69.36777542 133.6489 2.51237 MB21D2 0.385737570551862 0.604157711838247 0.0101047176098909 Mab-21 domain containing 2 . . . . . 0.56025 . -0.26993514 34.59542345 153.06828 2.70590 MBD1 0.959615951476631 0.0403840174395487 3.1083820309789e-08 methyl-CpG binding domain protein 1 FUNCTION: Transcriptional repressor that binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binding is abolished by the presence of 7-mG that is produced by DNA damage by methylmethanesulfonate (MMS). Acts as transcriptional repressor and plays a role in gene silencing by recruiting AFT7IP, which in turn recruits factors such as the histone methyltransferase SETDB1. Probably forms a complex with SETDB1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Isoform 1 and isoform 2 can also repress transcription from unmethylated promoters. {ECO:0000269|PubMed:10454587, ECO:0000269|PubMed:10648624, ECO:0000269|PubMed:12665582, ECO:0000269|PubMed:12697822, ECO:0000269|PubMed:12711603, ECO:0000269|PubMed:14555760, ECO:0000269|PubMed:14610093, ECO:0000269|PubMed:15327775, ECO:0000269|PubMed:9207790, ECO:0000269|PubMed:9774669}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9207790}.; medulla oblongata;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;urinary;adrenal cortex;blood;lens;bile duct;breast;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;cervix;kidney;stomach; amygdala;whole brain;temporal lobe;prefrontal cortex;testis;white blood cells; 0.76365 0.15639 -0.754958418 13.57631517 1288.3223 6.76006 MBD2 0.989310018452397 0.0106865404707124 3.44107689083681e-06 methyl-CpG binding domain protein 2 FUNCTION: Binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binds hemimethylated DNA as well. Recruits histone deacetylases and DNA methyltransferases. Acts as transcriptional repressor and plays a role in gene silencing. Functions as a scaffold protein, targeting GATAD2A and GATAD2B to chromatin to promote repression. May enhance the activation of some unmethylated cAMP-responsive promoters. {ECO:0000269|PubMed:10471499, ECO:0000269|PubMed:10947852, ECO:0000269|PubMed:12665568, ECO:0000269|PubMed:16415179, ECO:0000269|PubMed:24307175, ECO:0000269|PubMed:9774669}.; . TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney, stomach, testis and placenta. {ECO:0000269|PubMed:10050851}.; smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;oesophagus;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;salivary gland;thyroid;testis;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.56421 0.32769 -0.09720619 46.20193442 27.90165 0.89627 MBD3 0.919323880451979 0.0801584308409568 0.000517688707064024 methyl-CpG binding domain protein 3 FUNCTION: Acts as transcriptional repressor and plays a role in gene silencing. Does not bind to DNA by itself (PubMed:12124384). Binds to DNA with a preference for sites containing methylated CpG dinucleotides (in vitro). Binds to a lesser degree DNA containing unmethylated CpG dinucleotides (PubMed:24307175). Recruits histone deacetylases and DNA methyltransferases. {ECO:0000269|PubMed:10947852, ECO:0000269|PubMed:12124384, ECO:0000269|PubMed:18644863, ECO:0000269|PubMed:23361464, ECO:0000269|PubMed:24307175, ECO:0000269|PubMed:9774669}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;bladder;brain;heart;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach; amygdala;thalamus;placenta;temporal lobe;prefrontal cortex;testis;cingulate cortex;cerebellum; 0.20735 0.12884 -0.824740496 11.67728238 15.11169 0.54359 MBD3L1 1.30309193734163e-05 0.12058328226356 0.879403686817067 methyl-CpG binding domain protein 3-like 1 FUNCTION: Transcriptional repressor. {ECO:0000269|PubMed:12504854}.; . TISSUE SPECIFICITY: Highly expressed in testis. Detected at low levels in pancreas. Not detected in the other tissues tested. {ECO:0000269|PubMed:12504854}.; lung;testis; . 0.03590 0.09574 0.439181676 77.69521113 155.97675 2.72957 MBD3L2 . . . methyl-CpG binding domain protein 3-like 2 . . TISSUE SPECIFICITY: Detected at low levels in several somatic tissues. Highly expressed in the ovarian teratocarcinoma cell line PA-1. {ECO:0000269|PubMed:12504854}.; . . . 0.06771 . . 21.93031 0.73788 MBD3L3 0.208438985597134 0.648145657120889 0.143415357281977 methyl-CpG binding domain protein 3-like 3 . . . unclassifiable (Anatomical System); . . . . . 29.34109 0.93878 MBD3L4 . . . methyl-CpG binding domain protein 3-like 4 . . . . . . . . . . . MBD3L5 . . . methyl-CpG binding domain protein 3-like 5 . . . unclassifiable (Anatomical System);placenta; . . . . . 40.51674 1.18867 MBD4 1.69561035781758e-06 0.863540233182888 0.136458071206754 methyl-CpG binding domain 4 DNA glycosylase FUNCTION: Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein. {ECO:0000269|PubMed:10097147, ECO:0000269|PubMed:10930409}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;hypothalamus;blood;bile duct;pancreas;lung;trabecular meshwork;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;white blood cells;trigeminal ganglion;whole blood;skeletal muscle; 0.42467 0.17669 0.621009802 83.41589998 804.24964 5.58850 MBD5 0.999852333253027 0.000147666726713591 2.0259064874505e-11 methyl-CpG binding domain protein 5 FUNCTION: Binds to heterochromatin. Does not interact with either methylated or unmethylated DNA (in vitro).; DISEASE: Mental retardation, autosomal dominant 1 (MRD1) [MIM:156200]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:17847001}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in heart, placenta, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:12529184}.; . . 0.52171 0.09580 -2.122133515 1.515687662 165.21581 2.81194 MBD6 0.963657500420421 0.0363419159115369 5.83668042360562e-07 methyl-CpG binding domain protein 6 FUNCTION: Binds to heterochromatin. Does not interact with either methylated or unmethylated DNA (in vitro).; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;muscle;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; . 0.33922 0.09983 -1.458708104 3.821656051 217.67142 3.18983 MBIP 2.39687346293752e-05 0.914505474706467 0.0854705565589039 MAP3K12 binding inhibitory protein 1 FUNCTION: Inhibits the MAP3K12 activity to induce the activation of the JNK/SAPK pathway. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. {ECO:0000269|PubMed:19103755}.; . TISSUE SPECIFICITY: Ubiquitous. High expression seen in the heart and lung.; medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;atrium;whole body;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;stomach;aorta; superior cervical ganglion;thyroid;ciliary ganglion;pons;atrioventricular node; 0.06000 0.07955 -0.049474214 50.01179523 41.41017 1.21004 MBL1P . . . mannose-binding lectin (protein A) 1, pseudogene . . . . . . . . . . . MBL2 0.000741511520333564 0.525620984570989 0.473637503908677 mannose binding lectin 2 FUNCTION: Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages. May bind DNA. {ECO:0000269|PubMed:14515269}.; . TISSUE SPECIFICITY: Plasma protein produced mainly in the liver. {ECO:0000269|PubMed:18006063}.; . . 0.77683 0.45536 0.41713504 76.95800896 2524.07787 9.36640 MBL3P . . . mannose-binding lectin family member 3, pseudogene . . . . . . . . . . . MBLAC1 0.313958463301017 0.615746599350126 0.0702949373488567 metallo-beta-lactamase domain containing 1 . . . . . . . . . 459.46604 4.44740 MBLAC2 0.000280100214502958 0.555672863565542 0.444047036219955 metallo-beta-lactamase domain containing 2 . . . unclassifiable (Anatomical System);lymph node;ovary;colon;parathyroid;fovea centralis;skin;skeletal muscle;bone marrow;breast;prostate;lung;endometrium;placenta;macula lutea;liver;testis;germinal center;kidney;brain;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion; . . -0.516085732 21.20193442 16.8055 0.59091 MBNL1 0.981577652065926 0.0184196956566116 2.6522774624852e-06 muscleblind like splicing regulator 1 FUNCTION: Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. Regulates the TNNT2 exon 5 skipping through competition with U2AF2. Inhibits the formation of the spliceosome A complex on intron 4 of TNNT2 pre-mRNA. Binds to the stem-loop structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Binds to the 5'-YGCU(U/G)Y- 3'consensus sequence. Binds to the IR RNA. Binds to expanded CUG repeat RNA, which folds into a hairpin structure containing GC base pairs and bulged, unpaired U residues. {ECO:0000269|PubMed:10970838, ECO:0000269|PubMed:15257297, ECO:0000269|PubMed:16946708, ECO:0000269|PubMed:18335541, ECO:0000269|PubMed:19470458}.; DISEASE: Corneal dystrophy, Fuchs endothelial, 3 (FECD3) [MIM:613267]: A late-onset form of Fuchs endothelial corneal dystrophy, a disease caused by loss of endothelium of the central cornea. It is characterized by focal wart-like guttata that arise from Descemet membrane and develop in the central cornea, epithelial blisters, reduced vision and pain. Descemet membrane is thickened by abnormal collagenous deposition. {ECO:0000269|PubMed:25593321}. Note=The protein represented in this entry is involved in disease pathogenesis. In corneal endothelial cells from patients, MBNL1 is sequestered by TCF4 RNAs containing pathogenic CUG triplet repeat expansions. This results in missplicing of essential MBNL1-regulated mRNAs. {ECO:0000269|PubMed:25593321}.; TISSUE SPECIFICITY: Highly expressed in cardiac, skeletal muscle and during myoblast differentiation. Weakly expressed in other tissues (at protein level). Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:10970838, ECO:0000269|PubMed:11929853}.; smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;choroid;uterus;oesophagus;bone;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;mesenchyma;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;uterus;lymph node;prefrontal cortex;ciliary ganglion;white blood cells;atrioventricular node;whole blood;skeletal muscle;tonsil; 0.82263 0.24974 -0.449946534 24.00330267 17.3524 0.60952 MBNL1-AS1 . . . MBNL1 antisense RNA 1 . . . . . . . . . . . MBNL2 0.900896116763864 0.0989238701780478 0.000180013058088339 muscleblind like splicing regulator 2 FUNCTION: Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. RNA-binding protein that binds to 5'ACACCC-3' core sequence, termed zipcode, within the 3'UTR of ITGA3. Binds to CUG triplet repeat expansion in myotonic dystrophy muscle cells by sequestering the target RNAs. Seems to regulate expression and localization of ITGA3 by transporting it from the nucleus to cytoplasm at adhesion plaques. May play a role in myotonic dystrophy pathophysiology (DM). {ECO:0000269|PubMed:15257297, ECO:0000269|PubMed:16273094, ECO:0000269|PubMed:16946708}.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:11929853}.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;amniotic fluid;germinal center;brain;gall bladder;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;developmental;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach; amygdala;dorsal root ganglion;occipital lobe;medulla oblongata;thalamus;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.05644 0.07965 -0.293801652 32.93819297 21.49435 0.72448 MBNL3 0.833044765960916 0.166241948463365 0.000713285575718907 muscleblind like splicing regulator 3 FUNCTION: Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. May play a role in myotonic dystrophy pathophysiology (DM). Could inhibit terminal muscle differentiation, acting at approximately the time of myogenin induction. {ECO:0000269|PubMed:12297108, ECO:0000269|PubMed:15257297}.; . TISSUE SPECIFICITY: Highly expressed in the placenta. {ECO:0000269|PubMed:11929853}.; . . 0.17066 0.10090 -0.251530012 35.42108988 8.30653 0.30442 MBOAT1 8.84450886798244e-07 0.918337857992802 0.0816612575563111 membrane bound O-acyltransferase domain containing 1 FUNCTION: Acyltransferase which mediates the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L- serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3- phospho-L-serine or PS) (LPSAT activity). Prefers oleoyl-CoA as the acyl donor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. {ECO:0000269|PubMed:18772128}.; . TISSUE SPECIFICITY: Expressed in neutrophils. {ECO:0000269|PubMed:18772128}.; unclassifiable (Anatomical System);cartilage;ovary;tongue;hypothalamus;colon;skeletal muscle;breast;uterus;pancreas;prostate;lung;cochlea;endometrium;bone;thyroid;placenta;liver;testis;head and neck;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12941 0.10324 7.61E-05 53.98089172 939.76003 5.94270 MBOAT2 0.71697037979262 0.283002834391279 2.6785816100694e-05 membrane bound O-acyltransferase domain containing 2 FUNCTION: Acyltransferase which mediates the conversion of lysophosphatidylethanolamine (1-acyl-sn-glycero-3- phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2- diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity). Catalyzes also the acylation of lysophosphatidic acid (LPA) into phosphatidic acid (PA) (LPAAT activity). Has also a very weak lysophosphatidylcholine acyltransferase (LPCAT activity). Prefers oleoyl-CoA as the acyl donor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. {ECO:0000269|PubMed:18772128}.; . TISSUE SPECIFICITY: Expressed in neutrophils. {ECO:0000269|PubMed:18772128}.; ovary;colon;parathyroid;uterus;prostate;whole body;endometrium;larynx;thyroid;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;cerebellum cortex;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;liver;hypopharynx;spleen;head and neck;cervix;kidney;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.15786 0.10789 0.084621747 60.31493277 188.80659 2.98329 MBOAT4 . . . membrane bound O-acyltransferase domain containing 4 FUNCTION: Mediates the octanoylation of ghrelin at 'Ser-3'. Can use a variety of fatty acids as substrates including octanoic acid, decanoic acid and tetradecanoic acid. {ECO:0000269|PubMed:18443287}.; . TISSUE SPECIFICITY: Expressed predominantly in stomach with moderate levels in pancreas and relatively low levels in most other tissues. {ECO:0000269|PubMed:18443287}.; . . 0.23427 0.10875 1.23654218 93.29440906 215.80004 3.17043 MBOAT7 0.0463195894764606 0.928933403865893 0.0247470066576465 membrane bound O-acyltransferase domain containing 7 FUNCTION: Acyltransferase which mediates the conversion of lysophosphatidylinositol (1-acylglycerophosphatidylinositol or LPI) into phosphatidylinositol (1,2-diacyl-sn-glycero-3- phosphoinositol or PI) (LPIAT activity). Prefers arachidonoyl-CoA as the acyl donor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. {ECO:0000269|PubMed:18094042, ECO:0000269|PubMed:18772128}.; . TISSUE SPECIFICITY: Overexpressed in metastatic breast and bladder carcinomas relative to normal breast epithelium and urothelium. {ECO:0000269|PubMed:18772128}.; lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;muscle;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach; amygdala;adrenal gland;testis;atrioventricular node;whole blood; 0.17977 . -0.534490515 20.70063694 76.85541 1.84081 MBP 0.568470953651191 0.419743501038047 0.0117855453107614 myelin basic protein FUNCTION: The classic group of MBP isoforms (isoform 4-isoform 14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The smaller isoforms might have an important role in remyelination of denuded axons in multiple sclerosis. The non- classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T- cells and neural cells. Differential splicing events combined with optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function. Induces T-cell proliferation. {ECO:0000269|PubMed:8544862}.; DISEASE: Note=The reduction in the surface charge of citrullinated and/or methylated MBP could result in a weakened attachment to the myelin membrane. This mechanism could be operative in demyelinating diseases such as chronical multiple sclerosis (MS), and fulminating MS (Marburg disease).; TISSUE SPECIFICITY: MBP isoforms are found in both the central and the peripheral nervous system, whereas Golli-MBP isoforms are expressed in fetal thymus, spleen and spinal cord, as well as in cell lines derived from the immune system. {ECO:0000269|PubMed:7504278}.; sympathetic chain;substantia nigra;choroid;skin;uterus;subthalamic nucleus;optic nerve;ganglion;frontal lobe;cochlea;cerebral cortex;larynx;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);heart;nervous;hypothalamus;spinal cord;cerebrum;skeletal muscle;lung;adrenal gland;hippocampus;visual apparatus;head and neck;cerebellum; dorsal root ganglion;amygdala;whole brain;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;atrioventricular node;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.14601 . 0.196671391 67.19155461 215.57722 3.16951 MBS1 . . . Moebius syndrome 1 . . . . . . . . . . . MBS2 . . . Moebius syndrome 2 . . . . . . . . . . . MBS3 . . . Moebius syndrome 3 . . . . . . . . . . . MBTD1 0.995179972273057 0.00481992846208499 9.92648578604745e-08 mbt domain containing 1 FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility (By similarity). Specifically binds to monomethylated and dimethylated 'Lys-20' on histone H4. {ECO:0000250, ECO:0000269|PubMed:19841675}.; DISEASE: Note=A chromosomal aberration involving MBTD1 is a cause of acute poorly differentiated myeloid leukemia. Translocation (10;17)(p15;q21) with ZMYND11. {ECO:0000269|PubMed:23915195}.; . . . 0.35989 0.08298 0.060756528 58.52795471 10.32812 0.37647 MBTPS1 0.131749475403802 0.868250203407335 3.21188863610488e-07 membrane bound transcription factor peptidase, site 1 FUNCTION: Serine protease that catalyzes the first step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs). Other known substrates are BDNF, GNPTAB and ATF6. Cleaves after hydrophobic or small residues, provided that Arg or Lys is in position P4. Cleaves known substrates after Arg- Ser-Val-Leu (SERBP-2), Arg-His-Leu-Leu (ATF6), Arg-Gly-Leu-Thr (BDNF) and its own propeptide after Arg-Arg-Leu-Leu. Mediates the protein cleavage of GNPTAB into subunit alpha and beta, thereby participating in biogenesis of lysosomes. {ECO:0000269|PubMed:21719679}.; . TISSUE SPECIFICITY: Widely expressed.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;adrenal cortex;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;bile duct;pancreas;lung;placenta;hippocampus;duodenum;amnion;head and neck;kidney;stomach;thymus;cerebellum; subthalamic nucleus;superior cervical ganglion;atrioventricular node; 0.26153 0.50208 -1.297117862 4.965793819 219.33799 3.20420 MBTPS2 0.94019932230867 0.0597510940110085 4.95836803217321e-05 membrane bound transcription factor peptidase, site 2 FUNCTION: Intramembrane proteolysis of sterol-regulatory element- binding proteins (SREBPs) within the first transmembrane segment thereby releasing the N-terminal segment with a portion of the transmembrane segment attached. Site-2 cleavage comes after site-1 cleavage which takes place in the lumenal loop.; DISEASE: Olmsted syndrome, X-linked (OLMSX) [MIM:300918]: A rare congenital disorder characterized by bilateral mutilating palmoplantar keratoderma and periorificial keratotic plaques with severe itching at all lesions. Diffuse alopecia, constriction of digits, and onychodystrophy have also been reported. Infections and squamous cell carcinomas can arise on the keratotic areas. The digital constriction may progress to autoamputation of fingers and toes. {ECO:0000269|PubMed:22931912}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Keratosis follicularis spinulosa decalvans X-linked (KFSDX) [MIM:308800]: A rare disorder affecting the skin and the eye. Affected men show thickening of the skin of the neck, ears, and extremities, especially the palms and soles, loss of eyebrows, eyelashes and beard, thickening of the eyelids with blepharitis and ectropion, and corneal degeneration. {ECO:0000269|PubMed:20672378}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, muscle, kidney and pancreas.; . . 0.24032 . -0.560178693 19.30879925 16.72407 0.58811 MC1R 3.24606043304287e-07 0.0523706924672196 0.947628982926737 melanocortin 1 receptor FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.; DISEASE: Melanoma, cutaneous malignant 5 (CMM5) [MIM:613099]: A malignant neoplasm of melanocytes, arising de novo or from a pre- existing benign nevus, which occurs most often in the skin but also may involve other sites. {ECO:0000269|PubMed:17434924, ECO:0000269|PubMed:19338054}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Melanocytes and corticoadrenal tissue.; . . . 0.68939 0.34168906 73.72611465 1416.53832 7.03613 MC2R 0.0574474574260785 0.7111202500256 0.231432292548322 melanocortin 2 receptor FUNCTION: Receptor for corticotropin (ACTH). This receptor is mediated by G proteins (G(s)) which activate adenylate cyclase (cAMP). {ECO:0000269|PubMed:19329486, ECO:0000269|PubMed:20371771}.; . TISSUE SPECIFICITY: Melanocytes and corticoadrenal tissue.; unclassifiable (Anatomical System);medulla oblongata;adrenal gland;thyroid;adrenal cortex;parathyroid;pineal gland; dorsal root ganglion;amygdala;occipital lobe;superior cervical ganglion;adrenal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.17469 0.52384 0.262810045 70.43524416 260.73178 3.46743 MC3R 0.0013603798509996 0.422685183586886 0.575954436562114 melanocortin 3 receptor FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH. This receptor is mediated by G proteins which activate adenylate cyclase. Required for expression of anticipatory patterns of activity and wakefulness during periods of limited nutrient availability and for the normal regulation of circadian clock activity in the brain. {ECO:0000250|UniProtKB:P33033}.; . TISSUE SPECIFICITY: Brain, placental, and gut tissues.; unclassifiable (Anatomical System); superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.13487 . -0.402212257 26.7338995 2468.0282 9.25836 MC4R 1.53624620586494e-05 0.132149128826259 0.867835508711682 melanocortin 4 receptor FUNCTION: Receptor specific to the heptapeptide core common to adrenocorticotropic hormone and alpha-, beta-, and gamma-MSH. Plays a central role in energy homeostasis and somatic growth. This receptor is mediated by G proteins that stimulate adenylate cyclase (cAMP). {ECO:0000269|PubMed:12646665}.; . TISSUE SPECIFICITY: Brain, placental, and gut tissues.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;trigeminal ganglion; 0.22850 0.56135 -0.179930907 40.35739561 194.7764 3.02587 MC5R 0.00108831422696949 0.381354922436538 0.617556763336492 melanocortin 5 receptor FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. This receptor is a possible mediator of the immunomodulation properties of melanocortins.; . TISSUE SPECIFICITY: Expressed in the brain but not in the melanoma cells.; unclassifiable (Anatomical System); superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13468 0.23177 0.062575634 58.74026893 2353.40815 8.98979 MCAM 0.0547531292437873 0.945078711726646 0.000168159029566359 melanoma cell adhesion molecule FUNCTION: Plays a role in cell adhesion, and in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. Its expression may allow melanoma cells to interact with cellular elements of the vascular system, thereby enhancing hematogeneous tumor spread. Could be an adhesion molecule active in neural crest cells during embryonic development. Acts as surface receptor that triggers tyrosine phosphorylation of FYN and PTK2/FAK1, and a transient increase in the intracellular calcium concentration. {ECO:0000269|PubMed:11036077, ECO:0000269|PubMed:8292890}.; . TISSUE SPECIFICITY: Detected in endothelial cells in vascular tissue throughout the body. May appear at the surface of neural crest cells during their embryonic migration. Appears to be limited to vascular smooth muscle in normal adult tissues. Associated with tumor progression and the development of metastasis in human malignant melanoma. Expressed most strongly on metastatic lesions and advanced primary tumors and is only rarely detected in benign melanocytic nevi and thin primary melanomas with a low probability of metastasis.; ovary;sympathetic chain;skin;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;bladder;brain;amygdala;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;lung;mesenchyma;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;thymus;cerebellum; dorsal root ganglion;superior cervical ganglion;adipose tissue;placenta;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.28201 0.33127 -0.861560326 10.89289927 396.25709 4.18236 MCAT 0.00012348797323243 0.619836973891018 0.38003953813575 malonyl-CoA-acyl carrier protein transacylase FUNCTION: Catalyzes the transfer of a malonyl moiety from malonyl- CoA to the free thiol group of the phosphopantetheine arm of the mitochondrial ACP protein (NDUFAB1). This suggests the existence of the biosynthesis of fatty acids in mitochondrias. {ECO:0000269|PubMed:12882974}.; . . ovary;colon;parathyroid;skin;uterus;prostate;whole body;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;oral cavity;muscle;pharynx;skeletal muscle;breast;pancreas;lung;placenta;hippocampus;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion; 0.22233 0.31758 -0.045835247 50.34206181 2696.25295 9.77246 MCC 2.25777940265897e-08 0.998667875003995 0.00133210241821145 mutated in colorectal cancers FUNCTION: Candidate for the putative colorectal tumor suppressor gene located at 5q21. Suppresses cell proliferation and the Wnt/b- catenin pathway in colorectal cancer cells. Inhibits DNA binding of b-catenin/TCF/LEF transcription factors. Involved in cell migration independently of RAC1, CDC42 and p21-activated kinase (PAK) activation (PubMed:18591935, PubMed:19555689, PubMed:22480440). Represses the beta-catenin pathway (canonical Wnt signaling pathway) in a CCAR2-dependent manner by sequestering CCAR2 to the cytoplasm, thereby impairing its ability to inhibit SIRT1 which is involved in the deacetylation and negative regulation of beta-catenin (CTNB1) transcriptional activity (PubMed:24824780). {ECO:0000269|PubMed:18591935, ECO:0000269|PubMed:19555689, ECO:0000269|PubMed:22480440, ECO:0000269|PubMed:24824780}.; . TISSUE SPECIFICITY: Expressed in a variety of tissues.; unclassifiable (Anatomical System);heart;islets of Langerhans;salivary gland;developmental;colon;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;optic nerve;lung;macula lutea;visual apparatus;liver;testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.69326 0.10991 -1.427629082 4.039867893 2866.95837 10.13715 MCCC1 2.51105898766941e-05 0.99594563886363 0.00402925054649339 methylcrotonoyl-CoA carboxylase 1 FUNCTION: Biotin-attachment subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3- methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism. {ECO:0000269|PubMed:17360195}.; DISEASE: 3-methylcrotonoyl-CoA carboxylase 1 deficiency (MCC1D) [MIM:210200]: An autosomal recessive disorder of leucine catabolism. The phenotype is variable, ranging from neonatal onset with severe neurological involvement to asymptomatic adults. There is a characteristic organic aciduria with massive excretion of 3- hydroxyisovaleric acid and 3-methylcrotonylglycine, usually in combination with a severe secondary carnitine deficiency. {ECO:0000269|PubMed:11170888, ECO:0000269|PubMed:11181649, ECO:0000269|PubMed:11406611, ECO:0000269|PubMed:16010683, ECO:0000269|PubMed:17968484, ECO:0000269|PubMed:21071250, ECO:0000269|PubMed:22150417, ECO:0000269|PubMed:22264772, ECO:0000269|PubMed:22642865, ECO:0000269|Ref.6}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;mesenchyma;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; medulla oblongata;kidney; 0.33009 0.27594 -0.863377021 10.84571833 4416.0126 13.29903 MCCC1-AS1 . . . MCCC1 antisense RNA 1 . . . . . . . . . . . MCCC2 4.09035244002361e-08 0.940771768682395 0.0592281904140803 methylcrotonoyl-CoA carboxylase 2 FUNCTION: Carboxyltransferase subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3- methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism. {ECO:0000269|PubMed:17360195}.; DISEASE: 3-methylcrotonoyl-CoA carboxylase 2 deficiency (MCC2D) [MIM:210210]: An autosomal recessive disorder of leucine catabolism. The phenotype is variable, ranging from neonatal onset with severe neurological involvement to asymptomatic adults. There is a characteristic organic aciduria with massive excretion of 3- hydroxyisovaleric acid and 3-methylcrotonylglycine, usually in combination with a severe secondary carnitine deficiency. {ECO:0000269|PubMed:11170888, ECO:0000269|PubMed:11181649, ECO:0000269|PubMed:11406611, ECO:0000269|PubMed:16010683, ECO:0000269|PubMed:17968484, ECO:0000269|PubMed:21071250, ECO:0000269|PubMed:22150417, ECO:0000269|PubMed:22264772, ECO:0000269|PubMed:22642865}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);islets of Langerhans;colon;skeletal muscle;breast;uterus;prostate;lung;endometrium;bone;thyroid;placenta;visual apparatus;liver;testis;spleen;cervix;kidney;brain;stomach; superior cervical ganglion;kidney;atrioventricular node;trigeminal ganglion; 0.03572 0.18035 -0.224023033 37.4321774 68.762 1.71805 MCCD1 0.00896309387231422 0.580183255412683 0.410853650715002 mitochondrial coiled-coil domain 1 . . TISSUE SPECIFICITY: Widely expressed. Expressed in adult and fetal liver, kidney and lung. Expressed in fetal brain. Weakly expressed in fetal spleen. {ECO:0000269|PubMed:14527716}.; . . . . 0.880130671 88.9596603 345.4913 3.94302 MCCD1P1 . . . mitochondrial coiled-coil domain 1 pseudogene 1 . . . . . . . . . . . MCCD1P2 . . . mitochondrial coiled-coil domain 1 pseudogene 2 . . . . . . . . . . . MCDR1 . . . macular dystrophy, retinal, 1 (North Carolina type) . . . . . . . . . . . MCDR3 . . . macular dystrophy, retinal 3 . . . . . . . . . . . MCDR4 . . . macular dystrophy, retinal, 4 (North Carolina type with progressive sensorineural hearing loss) . . . . . . . . . . . MCDR5 . . . macular dystrophy 5 . . . . . . . . . . . MCEE 0.00211926018791901 0.511926790619057 0.485953949193024 methylmalonyl-CoA epimerase . DISEASE: Methylmalonyl-CoA epimerase deficiency (MCEED) [MIM:251120]: Autosomal recessive inborn error of amino acid metabolism, involving valine, threonine, isoleucine and methionine. This organic aciduria may present in the neonatal period with life-threatening metabolic acidosis, hyperammonemia, feeding difficulties, pancytopenia and coma. {ECO:0000269|PubMed:16752391}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pharynx;colon;parathyroid;skin;prostate;whole body;lung;cochlea;endometrium;nasopharynx;bone;placenta;liver;testis;spleen;germinal center;kidney;mammary gland;gall bladder; . 0.07276 0.16109 0.681699246 84.93158764 1975.19885 8.18568 MCEMP1 . . . mast cell-expressed membrane protein 1 . . TISSUE SPECIFICITY: Expressed specifically in mast cells. Found primarily in lung. {ECO:0000269|PubMed:15953541}.; . . 0.01638 . 1.082196027 91.79641425 . . MCF2 0.943290929446168 0.0567089977123991 7.28414326385666e-08 MCF.2 cell line derived transforming sequence FUNCTION: Guanine nucleotide exchange factor (GEF) that modulates the Rho family of GTPases. Promotes the conversion of some member of the Rho family GTPase from the GDP-bound to the GTP-bound form. Isoform 1 exhibits no activity toward RHOA, RAC1 or CDC42. Isoform 2 exhibits decreased GEF activity toward CDC42. Isoform 3 exhibits a weak but significant activity toward RAC1 and CDC42. Isoform 4 exhibits significant activity toward RHOA and CDC42. The truncated DBL oncogene is active toward RHOA, RAC1 and CDC42.; DISEASE: Note=MCF2 and DBL represent two activated versions of the same proto-oncogene. {ECO:0000305}.; TISSUE SPECIFICITY: Isoform 1 is expressed only in brain. Isoform 3 is expressed in heart, kidney, spleen, liver and testis. Isoform 4 is expressed in brain, heart, kidney, testis, placenta, stomach and peripheral blood. The protein is detectable in brain, heart, kidney, intestine, muscle, lung and testis. {ECO:0000269|PubMed:12445822}.; unclassifiable (Anatomical System);amygdala;islets of Langerhans;choroid;fovea centralis;lens;skin;retina;optic nerve;frontal lobe;macula lutea;testis;brain; thalamus;temporal lobe;testis;globus pallidus;ciliary ganglion;skeletal muscle; 0.19088 0.41436 0.86534717 88.80042463 141.40855 2.59391 MCF2L 0.79554140444058 0.204458592014441 3.54497870249889e-09 MCF.2 cell line derived transforming sequence like FUNCTION: Guanine nucleotide exchange factor that potentially links pathways that signal through RAC1, RHOA and CDC42. Catalyzes guanine nucleotide exchange on RHOA and CDC42 and interacts specifically with the GTP-bound form of RAC1, suggesting that it functions as an effector of RAC1. May also participate in axonal transport in the brain. Becomes activated and highly tumorigenic by truncation of the N-terminus (By similarity). Isoform 5 activates CDC42. {ECO:0000250, ECO:0000269|PubMed:15157669}.; . . myocardium;ovary;colon;parathyroid;skin;retina;uterus;prostate;endometrium;synovium;bone;brain;unclassifiable (Anatomical System);heart;cartilage;cerebellum cortex;hypothalamus;pineal body;lung;placenta;hippocampus;visual apparatus;liver;kidney;mammary gland;stomach; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.10770 . -1.580210337 3.137532437 557.3223 4.79548 MCF2L-AS1 . . . MCF2L antisense RNA 1 . . . . . . . . . . . MCF2L2 1.61269129905986e-12 0.999318944621419 0.000681055376968077 MCF.2 cell line derived transforming sequence-like 2 FUNCTION: Probably functions as a guanine nucleotide exchange factor. {ECO:0000250}.; . TISSUE SPECIFICITY: Significantly expressed in brain and modestly in pancreas, brain and testis. {ECO:0000269|PubMed:18259684}.; unclassifiable (Anatomical System);lung;islets of Langerhans;larynx;bone;placenta;testis;colon;head and neck;brain;mammary gland;skeletal muscle;cerebellum; superior cervical ganglion;appendix; 0.57276 0.09212 0.854236942 88.51144138 3783.20077 12.04253 MCFD2 0.0699912352148666 0.738757755369312 0.191251009415822 multiple coagulation factor deficiency 2 FUNCTION: The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Plays a role in the secretion of coagulation factors. {ECO:0000269|PubMed:12717434}.; DISEASE: Factor V and factor VIII combined deficiency 2 (F5F8D2) [MIM:613625]: A blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal. {ECO:0000269|PubMed:12717434, ECO:0000269|PubMed:18685427, ECO:0000269|PubMed:20491958}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;adrenal gland;thyroid;placenta;adrenal cortex;testis; 0.17526 0.12632 -0.163345027 41.24793583 17.07467 0.60110 MCFD2P1 . . . multiple coagulation factor deficiency 2 pseudogene 1 . . . . . . . . . . . MCHR1 0.00114839274760266 0.620384174641167 0.378467432611231 melanin concentrating hormone receptor 1 FUNCTION: Receptor for melanin-concentrating hormone, coupled to both G proteins that inhibit adenylyl cyclase and G proteins that activate phosphoinositide hydrolysis. {ECO:0000269|PubMed:10421367}.; . TISSUE SPECIFICITY: Highest level in brain, particularly in the frontal cortex and hypothalamus, lower levels in the liver and heart.; unclassifiable (Anatomical System);lung;islets of Langerhans;hippocampus;testis;brain; dorsal root ganglion;superior cervical ganglion;pons; 0.09969 0.17262 0.001895464 54.03397028 280.64368 3.58952 MCHR2 3.50210575927378e-05 0.587613971916937 0.41235100702547 melanin concentrating hormone receptor 2 FUNCTION: Receptor for melanin-concentrating hormone, coupled to G proteins that activate phosphoinositide hydrolysis.; . TISSUE SPECIFICITY: Specifically expressed in the brain, with highest levels in cerebral cortex, hippocampus and amygdala. No expression detected in the cerebellum, thalamus or hypothalamus.; unclassifiable (Anatomical System);lung;placenta;testis;brain;peripheral nerve; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;skeletal muscle; 0.12259 0.16977 -0.26993514 34.59542345 61.26517 1.59417 MCHR2-AS1 . . . MCHR2 antisense RNA 1 . . . . . . . . . . . MCIDAS . . . multiciliate differentiation and DNA synthesis associated cell cycle protein FUNCTION: Transcription regulator specifically required for multiciliate cell differentiation. Acts in a multiprotein complex containing E2F4 and E2F5 that binds and activates genes required for centriole biogenesis. Required for the deuterosome-mediated acentriolar pathway (PubMed:25048963). Plays a role in mitotic cell cycle progression by promoting cell cycle exit. Modulates GMNN activity by reducing its affinity for CDT1 (PubMed:21543332, PubMed:24064211). {ECO:0000250|UniProtKB:Q08B36, ECO:0000269|PubMed:21543332, ECO:0000269|PubMed:24064211, ECO:0000269|PubMed:25048963}.; DISEASE: Note=Ciliary dyskinesia, primary (CILDN): A disorder characterized by abnormalities of motile cilia. Chronic recurrent infections of the upper (rhinitis, otitis media, nasal polyps and sinusitis) and lower airways (recurrent pneumonia, bronchiectasis, chronic obstructive airway disease caused by mucociliary clearance). The disease is caused by mutations affecting the gene represented in this entry. Respiratory epithelial cells carry only one or two cilia per cell. {ECO:0000269|PubMed:25048963}.; . . . . . . . 52.64668 1.43710 MCKD2 . . . medullary cystic kidney disease 2 (autosomal dominant) . . . . . . . . . . . MCL1 0.950092967336216 0.0497525085311388 0.000154524132645392 myeloid cell leukemia 1 FUNCTION: Involved in the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. Mediates its effects by interactions with a number of other regulators of apoptosis. Isoform 1 inhibits apoptosis. Isoform 2 promotes apoptosis. {ECO:0000269|PubMed:10766760, ECO:0000269|PubMed:16543145}.; . . myocardium;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;oesophagus;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;placenta;ciliary ganglion;white blood cells;atrioventricular node;trigeminal ganglion;whole blood; 0.53325 0.48065 -0.183570861 39.95046001 40.92143 1.19891 MCM2 0.509038119651144 0.490955018476224 6.86187263212273e-06 minichromosome maintenance complex component 2 FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division. {ECO:0000269|PubMed:8175912}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;duodenum;liver;cervix;spleen;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;tumor;testis;trigeminal ganglion;bone marrow; 0.99381 0.12905 -0.946125119 9.377211607 416.94158 4.27348 MCM3 6.37332148340467e-07 0.998670951547654 0.00132841112019807 minichromosome maintenance complex component 3 FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for DNA replication and cell proliferation.; . . lymphoreticular;ovary;salivary gland;intestine;colon;substantia nigra;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;larynx;bone;thyroid;iris;pituitary gland;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;muscle;pharynx;blood;lens;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;tumor; 0.96475 0.27545 -0.929520514 9.683887709 1157.63897 6.47970 MCM3AP 0.837366650314123 0.162633349608656 7.72207255527323e-11 minichromosome maintenance complex component 3 associated protein FUNCTION: Isoform GANP: Essential for the generation of high- affinity B-cells against T-cell-dependent antigens by affecting somatic hypermutation at the IgV-regions. May have stimulation- dependent DNA primase activity that would generate extra RNA primers in very rapidely proliferating cells and would support clonal expansion of differentiating B-cells (By similarity). Involved in the nuclear export of poly(A)-containing mRNAs by acting as a scaffold for the TREX-2 complex. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. {ECO:0000250, ECO:0000269|PubMed:22307388}.; . . smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;oral cavity;muscle;pancreas;lung;cornea;placenta;hypopharynx;head and neck;kidney;stomach;thymus; whole brain;dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;prefrontal cortex;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15960 0.13932 -2.549125491 0.866949752 2976.75211 10.34847 MCM3AP-AS1 . . . MCM3AP antisense RNA 1 . . . . . 0.10258 . . . . . MCM4 0.000301842295939908 0.999133313690633 0.000564844013427293 minichromosome maintenance complex component 4 FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. {ECO:0000269|PubMed:9305914}.; DISEASE: Natural killer cell and glucocorticoid deficiency with DNA repair defect (NKGCD) [MIM:609981]: An autosomal recessive disorder characterized by severe intra- and extrauterine growth retardation, microcephaly, decreased numbers of natural killer cells, and recurrent viral infections, most often affecting the respiratory tract and leading to respiratory failure. Affected individuals also have adrenal insufficiency requiring corticosteroid replacement therapy and may have an increased susceptibility to cancer. {ECO:0000269|PubMed:22354167, ECO:0000269|PubMed:22354170, ECO:0000269|PubMed:22499342}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; testis - interstitial;superior cervical ganglion;fetal liver;testis;tumor;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.95279 0.15521 -1.104093597 6.894314697 105.86637 2.23027 MCM5 0.56369250698601 0.436303046677459 4.44633653035734e-06 minichromosome maintenance complex component 5 FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (By similarity). Interacts with MCMBP. {ECO:0000250}.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;pharynx;blood;lens;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;kidney;mammary gland;stomach; fetal liver;prostate;testis - interstitial;placenta;testis;tumor;white blood cells;trigeminal ganglion;skeletal muscle;tonsil;bone marrow;thymus; 0.97196 0.19034 -0.43902969 24.63434772 341.56112 3.91942 MCM6 0.998482019514362 0.00151798024315844 2.42479922054783e-10 minichromosome maintenance complex component 6 FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. {ECO:0000269|PubMed:9305914}.; . . medulla oblongata;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;mesenchyma;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; fetal liver;tumor; 0.98070 0.20620 -0.574945567 18.90186365 110.05376 2.27954 MCM7 1.4578327477307e-13 0.168721479536772 0.831278520463082 minichromosome maintenance complex component 7 FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for S-phase checkpoint activation upon UV-induced damage. {ECO:0000269|PubMed:15210935, ECO:0000269|PubMed:15538388, ECO:0000269|PubMed:9305914}.; . . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;prostate;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;breast;epididymis;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;uterus;whole body;oesophagus;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;hypothalamus;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;cerebellum; . 0.93576 0.41417 -1.258440978 5.307855626 1601.37434 7.40241 MCM8 1.92893351081766e-10 0.954436717444186 0.0455632823629208 minichromosome maintenance 8 homologous recombination repair factor FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in homologous recombination repair following DNA interstrand cross-links and plays a key role during gametogenesis. The MCM8- MCM9 complex probably acts as a hexameric helicase downstream of the Fanconi anemia proteins BRCA2 and RAD51 and is required to process aberrant forks into homologous recombination substrates and to orchestrate homologous recombination with resection, fork stabilization and fork restart. May also play a non-essential for DNA replication: may be involved in the activation of the prereplicative complex (pre-RC) during G(1) phase by recruiting CDC6 to the origin recognition complex (ORC). Binds chromatin throughout the cell cycle. {ECO:0000269|PubMed:22771115}.; DISEASE: Premature ovarian failure 10 (POF10) [MIM:612885]: An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol. {ECO:0000269|PubMed:25437880}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest levels in placenta, lung and pancreas. Low levels in skeletal muscle and kidney. Expressed in various tumors with highest levels in colon and lung cancers. {ECO:0000269|PubMed:12771218}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;muscle;colon;lens;skin;skeletal muscle;uterus;prostate;bone;thyroid;placenta;liver;testis;head and neck;germinal center;kidney;brain;mammary gland;stomach;cerebellum; globus pallidus; 0.24617 0.19778 1.407269618 94.78650625 3710.46351 11.88891 MCM8-AS1 . . . MCM8 antisense RNA 1 . . . . . . . . . . . MCM9 0.0039178276020221 0.958174024708846 0.0379081476891314 minichromosome maintenance 9 homologous recombination repair factor FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in homologous recombination repair following DNA interstrand cross-links and plays a key role during gametogenesis. The MCM8- MCM9 complex probably acts as a hexameric helicase downstream of the Fanconi anemia proteins BRCA2 and RAD51 and is required to process aberrant forks into homologous recombination substrates and to orchestrate homologous recombination with resection, fork stabilization and fork restart. {ECO:0000269|PubMed:22771115}.; DISEASE: Ovarian dysgenesis 4 (ODG4) [MIM:616185]: A disorder characterized by lack of spontaneous pubertal development, primary amenorrhea, uterine hypoplasia, and hypergonadotropic hypogonadism as a result of streak gonads. {ECO:0000269|PubMed:25480036}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);breast;lung;hypothalamus;thyroid;testis;germinal center;brain;stomach;retina; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.24948 . . . 657.30492 5.13970 MCM10 5.09300719404944e-11 0.939900312725175 0.0600996872238948 minichromosome maintenance 10 replication initiation factor FUNCTION: Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. Additionally, plays a role in preventing DNA damage during replication. Key effector of the RBBP6 and ZBTB38-mediated regulation of DNA-replication and common fragile sites stability; acts as a direct target of transcriptional repression by ZBTB38 (PubMed:24726359). {ECO:0000269|PubMed:11095689, ECO:0000269|PubMed:15136575, ECO:0000269|PubMed:17699597, ECO:0000269|PubMed:19608746, ECO:0000269|PubMed:24726359}.; . . unclassifiable (Anatomical System);lymph node;pharynx;blood;bone marrow;uterus;prostate;lung;larynx;bone;placenta;visual apparatus;liver;testis;germinal center;brain;mammary gland;stomach; tumor; 0.26444 0.13689 -0.034919861 50.5425808 1763.81603 7.75848 MCMBP 0.998215054692028 0.00178494352915133 1.77882058998094e-09 minichromosome maintenance complex binding protein FUNCTION: Associated component of the MCM complex that acts as a regulator of DNA replication. Binds to the MCM complex during late S phase and promotes the disassembly of the MCM complex from chromatin, thereby acting as a key regulator of pre-replication complex (pre-RC) unloading from replicated DNA. Can dissociate the MCM complex without addition of ATP; probably acts by destabilizing interactions of each individual subunits of the MCM complex. Required for sister chromatid cohesion. {ECO:0000269|PubMed:20090939, ECO:0000269|PubMed:21196493}.; . . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12436 0.11074 -0.646543901 16.44255721 170.73949 2.85030 MCMDC2 5.68685507134259e-06 0.876833130434864 0.123161182710064 minichromosome maintenance domain containing 2 . . . . . 0.10566 . 1.155610133 92.59259259 1739.20281 7.69794 MCOLN1 0.0370559727759663 0.962635965112643 0.000308062111390885 mucolipin 1 FUNCTION: Cation channel probably playing a role in the endocytic pathway and in the control of membrane trafficking of proteins and lipids. Could play a major role in Ca(2+) transport regulating lysosomal exocytosis. {ECO:0000269|PubMed:12459486, ECO:0000269|PubMed:14749347}.; . TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues. {ECO:0000269|PubMed:10973263, ECO:0000269|PubMed:11013137, ECO:0000269|PubMed:11030752}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;lens;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach; whole brain;placenta; 0.23870 0.17168 -0.93133804 9.613116301 110.33833 2.28554 MCOLN2 1.32269877326023e-10 0.181408264315285 0.818591735552445 mucolipin 2 . . . lung;placenta;testis;colon; ciliary ganglion;atrioventricular node; 0.08507 0.08339 0.711016566 85.72776598 775.19853 5.51041 MCOLN3 3.77973883718057e-07 0.940625182563496 0.0593744394626201 mucolipin 3 . . . unclassifiable (Anatomical System);cartilage;ovary;heart;islets of Langerhans;adrenal cortex;parathyroid;skin;skeletal muscle;bile duct;uterus;lung;bone;placenta;kidney;brain;mammary gland; adrenal gland;adrenal cortex;pituitary; 0.10220 0.13323 -0.690637458 15.12149092 55.13455 1.48779 MCPH1 5.16507030687178e-18 0.00309537586807128 0.996904624131929 microcephalin 1 FUNCTION: Implicated in chromosome condensation and DNA damage induced cellular responses. May play a role in neurogenesis and regulation of the size of the cerebral cortex. {ECO:0000269|PubMed:12046007, ECO:0000269|PubMed:15199523, ECO:0000269|PubMed:15220350}.; DISEASE: Microcephaly 1, primary, autosomal recessive (MCPH1) [MIM:251200]: A disease defined as a head circumference more than 3 standard deviations below the age-related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. Despite this marked reduction in size, the gyral pattern is relatively well preserved, with no major abnormality in cortical architecture. Affected individuals are mentally retarded. Primary microcephaly is further defined by the absence of other syndromic features or significant neurological deficits due to degenerative brain disorder. Some MCHP1 patients also present growth retardation, short stature, and misregulated chromosome condensation as indicated by a high number of prophase-like cells detected in routine cytogenetic preparations and poor-quality metaphase G-banding. {ECO:0000269|PubMed:12046007, ECO:0000269|PubMed:15199523, ECO:0000269|PubMed:16211557}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in fetal brain, liver and kidney. {ECO:0000269|PubMed:12046007}.; unclassifiable (Anatomical System);tongue;colon;skeletal muscle;uterus;lung;frontal lobe;endometrium;placenta;bone;visual apparatus;hippocampus;liver;testis;head and neck;germinal center;brain;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;skeletal muscle; 0.07794 0.99968 1.39439264 94.65675867 4877.16069 14.19752 MCPH1-AS1 . . . MCPH1 antisense RNA 1 . . . . . . . . . . . MCRS1 0.0665356264871206 0.932855787705388 0.000608585807491463 microspherule protein 1 FUNCTION: Modulates the transcription repressor activity of DAXX by recruiting it to the nucleolus. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. May also be an inhibitor of TERT telomerase activity. {ECO:0000269|PubMed:11948183, ECO:0000269|PubMed:15044100, ECO:0000269|PubMed:20018852}.; . TISSUE SPECIFICITY: Detected in testis, and at lower levels in spleen, thymus, prostate, uterus, small intestine, colon and leukocytes.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; heart;testis - seminiferous tubule;testis;pons;cingulate cortex; 0.56709 0.14229 -0.47017169 23.25430526 19.99946 0.68166 MCS . . . Miles-Carpenter X-linked mental retardation syndrome . . . . . . . . . . . MCTP1 0.00988911824115707 0.990107196180482 3.68557836071386e-06 multiple C2 and transmembrane domain containing 1 . . . unclassifiable (Anatomical System);prostate;ovary;heart;nasopharynx;bone;testis;blood;brain;bone marrow; superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;caudate nucleus;skin; 0.65576 0.08898 -1.506435464 3.544468035 969.67998 6.02016 MCTP2 7.9294335387251e-41 5.43277081555083e-09 0.999999994567229 multiple C2 domains, transmembrane 2 FUNCTION: Might play a role in the development of cardiac outflow tract. {ECO:0000269|PubMed:23773997}.; DISEASE: Note=Heterozygosity for a 2.2-Mb deletion at chromosome 15q26.2, encompassing MCTP2, has been identified in a 10-year-old girl and her 3-year-old half brother, who had both coarctation of the aorta associated with dysmorphic features and ventricular septal defects. An intragenic MCTP2 duplication, leading to premature truncation (F697X) within the first transmembrane region of the protein, has also been observed in a male patient with a non-syndromic complex cardiac malformation involving coarctation, hypoplastic left heart, mitral atresia, bicuspid aortic valve and muscular ventricular septal defect. Although the link between left ventricular outflow tract malformations and MCTP2 could not be established, it has been proposed that defects in the MCTP2 gene may contribute to phenotype. This hypothesis is supported by the observation that Xenopus laevis embryos treated with MCTP2 morpholinos show no evidence of endocardial cushion formation at any level of the developing outflow tract (PubMed:23773997). {ECO:0000269|PubMed:23773997}.; . unclassifiable (Anatomical System);pancreas;lung;ovary;bone;placenta;pituitary gland;liver;testis;colon;parathyroid;spleen;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11281 0.09580 -0.189246284 39.30761972 1492.80371 7.18685 MCTS1 0.825030345869128 0.171133649732589 0.00383600439828272 malignant T-cell amplified sequence 1 FUNCTION: Anti-oncogene that plays a role in cell cycle regulation; decreases cell doubling time and anchorage-dependent growth; shortens the duration of G1 transit time and G1/S transition. When constituvely expressed, increases CDK4 and CDK6 kinases activity and CCND1/cyclin D1 protein level, as well as G1 cyclin/CDK complex formation. Involved in translation initiation; promotes recruitment of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. Plays a role as translation enhancer; recruits the density-regulated protein/DENR and binds to the cap complex of the 5'-terminus of mRNAs, subsequently altering the mRNA translation profile; up- regulates protein levels of BCL2L2, TFDP1, MRE11A, CCND1 and E2F1, while mRNA levels remains constant. Hyperactivates DNA damage signaling pathway; increased gamma-irradiation-induced phosphorylation of histone H2AX, and induces damage foci formation. Increases the overall number of chromosomal abnormalities such as larger chromosomes formation and multiples chromosomal fusions when overexpressed in gamma-irradiated cells. May play a role in promoting lymphoid tumor development: lymphoid cell lines overexpressing MCTS1 exhibit increased growth rates and display increased protection against apoptosis. May contribute to the pathogenesis and progression of breast cancer via promotion of angiogenesis through the decline of inhibitory THBS1/thrombospondin-1, and inhibition of apoptosis. Involved in the process of proteasome degradation to down-regulate Tumor suppressor p53/TP53 in breast cancer cell; Positively regulates phosphorylation of MAPK1 and MAPK3. Involved in translation initiation; promotes aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. {ECO:0000269|PubMed:10440924, ECO:0000269|PubMed:11709712, ECO:0000269|PubMed:12637315, ECO:0000269|PubMed:15897892, ECO:0000269|PubMed:16322206, ECO:0000269|PubMed:16982740, ECO:0000269|PubMed:17016429, ECO:0000269|PubMed:17416211, ECO:0000269|PubMed:20713520, ECO:0000269|PubMed:9766643}.; . TISSUE SPECIFICITY: Ubiquitous. Over-expressed in T-cell lymphoid cell lines and in non-Hodgkin lymphoma cell lines as well as in a subset of primary large B-cell lymphomas. {ECO:0000269|PubMed:9766643}.; . . 0.58881 0.19788 0.323496558 72.93583392 17.94998 0.62744 MCTS2P . . . malignant T-cell amplified sequence 2, pseudogene . . . . . 0.58881 . . . . . MCU 0.980775509208689 0.0192215449740043 2.94581730686664e-06 mitochondrial calcium uniporter FUNCTION: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways (PubMed:21685888, PubMed:21685886, PubMed:23101630, PubMed:22904319, PubMed:23178883, PubMed:22829870, PubMed:22822213, PubMed:24332854, PubMed:26341627). Activity is regulated by MICU1 and MICU2. At low Ca(2+) levels MCU activity is down-regulated by MICU2; at higher Ca(2+) levels MICU1 increases MCU activity (PubMed:24560927). Regulates glucose-dependent insulin secretion in pancreatic beta- cells by regulating mitochondrial calcium uptake (PubMed:22904319, PubMed:22829870). Involved in buffering the amplitude of systolic calcium rises in cardiomyocytes (PubMed:22822213). {ECO:0000269|PubMed:21685886, ECO:0000269|PubMed:21685888, ECO:0000269|PubMed:22822213, ECO:0000269|PubMed:22829870, ECO:0000269|PubMed:22904319, ECO:0000269|PubMed:23101630, ECO:0000269|PubMed:23178883, ECO:0000269|PubMed:24332854, ECO:0000269|PubMed:24560927, ECO:0000269|PubMed:26341627}.; . . colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lacrimal gland;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.56025 . -0.117432389 44.89266336 48.28843 1.35442 MCUR1 0.00156303078281646 0.882401550157539 0.116035419059645 mitochondrial calcium uniporter regulator 1 FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU) required for calcium entry into mitochondrion. Plays a direct role in uniporter-mediated calcium uptake, possibly via a direct interaction with MCU. {ECO:0000269|PubMed:23178883}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:23178883}.; . . 0.16149 . . . 1067.1477 6.26495 MDC1 0.00094184680344876 0.999053640460675 4.51273587610487e-06 mediator of DNA damage checkpoint 1 FUNCTION: Required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. May serve as a scaffold for the recruitment of DNA repair and signal transduction proteins to discrete foci of DNA damage marked by 'Ser-139' phosphorylation of histone H2AFX. Also required for downstream events subsequent to the recruitment of these proteins. These include phosphorylation and activation of the ATM, CHEK1 and CHEK2 kinases, and stabilization of TP53 and apoptosis. ATM and CHEK2 may also be activated independently by a parallel pathway mediated by TP53BP1. {ECO:0000269|PubMed:12475977, ECO:0000269|PubMed:12499369, ECO:0000269|PubMed:12551934, ECO:0000269|PubMed:12607003, ECO:0000269|PubMed:12607004, ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:12611903, ECO:0000269|PubMed:14695167, ECO:0000269|PubMed:15201865, ECO:0000269|PubMed:15377652}.; . TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:12499369}.; . . 0.74372 . 5.197716727 99.83486671 3278.70938 10.92667 MDC1-AS1 . . . MDC1 antisense RNA 1 . . . . . . . . . . . MDFI 0.144418737080253 0.77872808403789 0.0768531788818575 MyoD family inhibitor FUNCTION: Inhibits the transactivation activity of the Myod family of myogenic factors and represses myogenesis. Acts by associating with Myod family members and retaining them in the cytoplasm by masking their nuclear localization signals. Can also interfere with the DNA-binding activity of Myod family members. Plays an important role in trophoblast and chondrogenic differentiation. Regulates the transcriptional activity of TCF7L1/TCF3 by interacting directly with TCF7L1/TCF3 and preventing it from binding DNA. Binds to the axin complex, resulting in an increase in the level of free beta-catenin. Affects axin regulation of the WNT and JNK signaling pathways (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);colon;choroid;skin;retina;uterus;pancreas;prostate;whole body;lung;cerebral cortex;placenta;bone;visual apparatus;testis;kidney;brain; superior cervical ganglion;testis - interstitial;trigeminal ganglion;skeletal muscle; 0.47616 0.18455 -0.137658575 43.57159707 120.89326 2.39670 MDFIC . . . MyoD family inhibitor domain containing FUNCTION: Acts as a transcriptional activator or repressor. Inhibits the transcriptional activation of Zic family proteins ZIC1, ZIC2 and ZIC3. Retains nuclear Zic proteins ZIC1, ZIC2 and ZIC3 in the cytoplasm. Modulates the expression from both cellular and viral promoters. Down-regulates Tat-dependent transcription of the human immunodeficiency virus type 1 (HIV-1) LTR by interacting with HIV-1 Tat and Rev and impairing their nuclear import, probably by rendering the NLS domains inaccessible to importin- beta. Also stimulates activation of human T-cell leukemia virus type I (HTLV-I) LTR. Binds to the axin complex, resulting in an increase in the level of free beta-catenin. Affects axin regulation of the WNT and JNK signaling pathways. {ECO:0000269|PubMed:10671520, ECO:0000269|PubMed:12192039, ECO:0000269|PubMed:12944466, ECO:0000269|PubMed:16260749, ECO:0000269|Ref.6}.; . TISSUE SPECIFICITY: Expressed in lymphoid organs (spleen, thymus, peripheral blood leukocytes) as well as prostate, uterus and small intestine. {ECO:0000269|PubMed:10671520}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;bone;testis;germinal center;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;alveolus;liver;kidney;mammary gland;stomach;aorta; superior cervical ganglion;uterus corpus;adipose tissue;appendix;white blood cells;pons;skeletal muscle; 0.10205 0.18498 . . 42.00441 1.22326 MDGA1 0.995236956713737 0.00476303933821579 3.94804666932354e-09 MAM domain containing glycosylphosphatidylinositol anchor 1 FUNCTION: Required for radial migration of cortical neurons in the superficial layer of the neocortex (By similarity). Plays a role in the formation or maintenance of inhibitory synapses. May function by inhibiting the activity of NLGN2. {ECO:0000250, ECO:0000269|PubMed:23248271}.; . TISSUE SPECIFICITY: Has been found in brain, heart, skeletal muscle and kidney. Found to be overexpressed in tumor tissues.; unclassifiable (Anatomical System);heart;colon;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;frontal lobe;macula lutea;iris;testis;germinal center;kidney;brain;cerebellum;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;uterus corpus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;skin; 0.15426 . -1.126142808 6.564048125 1105.28503 6.35226 MDGA2 0.993216871367626 0.0067831192641061 9.36826788457279e-09 MAM domain containing glycosylphosphatidylinositol anchor 2 FUNCTION: May be involved in cell-cell interactions. {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in Leydig cells, syncytiotrophoblast, duodenal villi epithelial cells and neutrophils from kidney and cutaneous squamous cell carcinoma (at protein level). {ECO:0000269|PubMed:19997561}.; unclassifiable (Anatomical System);uterus;heart;bone;visual apparatus;lens;brain;skin;skeletal muscle;aorta;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.60446 0.11151 -1.017713296 8.103326256 2231.78204 8.70709 MDH1 0.982634617401256 0.0173540634388212 1.13191599226307e-05 malate dehydrogenase 1 . . . ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;thyroid;bladder;brain;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;cerebral cortex;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach;aorta; amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.18839 0.62085 -0.207437529 38.2814343 36.87035 1.10453 MDH1B 5.81111250194294e-12 0.0586709204725838 0.941329079521605 malate dehydrogenase 1B . . . . . 0.13728 0.09156 -0.110153916 45.48832272 290.8378 3.64828 MDH2 0.177605135901673 0.809688717406996 0.0127061466913312 malate dehydrogenase 2 . . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;choroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;synovium;bone;iris;testis;germinal center;brain;artery;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;greater omentum;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; amygdala;whole brain;medulla oblongata;superior cervical ganglion;heart;temporal lobe;pons;skeletal muscle;prefrontal cortex;liver;globus pallidus;kidney;cerebellum; 0.32327 0.90548 -0.334253673 30.70299599 208.93323 3.11958 MDK 0.0224327842650619 0.76305337873341 0.214513837001528 midkine (neurite growth-promoting factor 2) FUNCTION: Developmentally regulated, secreted growth factor homologous to pleiotrophin (PTN), which has heparin binding activity. Binds anaplastic lymphoma kinase (ALK) which induces ALK activation and subsequent phosphorylation of the insulin receptor substrate (IRS1), followed by the activation of mitogen-activated protein kinase (MAPK) and PI3-kinase, and the induction of cell proliferation. Involved in neointima formation after arterial injury, possibly by mediating leukocyte recruitment. Also involved in early fetal adrenal gland development (By similarity). {ECO:0000250, ECO:0000269|PubMed:12122009, ECO:0000269|PubMed:1768439}.; . TISSUE SPECIFICITY: Expressed in various tumor cell lines. In insulinoma tissue predominantly expressed in precancerous lesions. {ECO:0000269|PubMed:17379400}.; ovary;colon;parathyroid;choroid;skin;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;synovium;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;pharynx;breast;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.38956 . 0.057118534 57.99716914 4.23961 0.15437 MDM1 5.78287888907171e-08 0.961965994214538 0.0380339479566729 Mdm1 nuclear protein FUNCTION: Microtubule-binding protein that negatively regulates centriole duplication. Binds to and stabilizes microtubules (PubMed:26337392). {ECO:0000269|PubMed:26337392}.; . . ovary;colon;substantia nigra;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;gum;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;skeletal muscle;bile duct;lung;adrenal gland;mesenchyma;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;stomach; amygdala;superior cervical ganglion;testis - seminiferous tubule;temporal lobe;appendix;testis;globus pallidus;trigeminal ganglion; 0.42256 0.10900 0.383960053 75.66053314 1434.83695 7.07219 MDM2 0.995410847609102 0.00458906434124163 8.80496559131227e-08 MDM2 proto-oncogene FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation. {ECO:0000269|PubMed:12821780, ECO:0000269|PubMed:15053880, ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:15632057, ECO:0000269|PubMed:16337594, ECO:0000269|PubMed:17290220, ECO:0000269|PubMed:19098711, ECO:0000269|PubMed:19219073, ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:19965871, ECO:0000269|PubMed:20173098, ECO:0000269|PubMed:20385133, ECO:0000269|PubMed:20858735, ECO:0000269|PubMed:22128911}.; DISEASE: Note=Seems to be amplified in certain tumors (including soft tissue sarcomas, osteosarcomas and gliomas). A higher frequency of splice variants lacking p53 binding domain sequences was found in late-stage and high-grade ovarian and bladder carcinomas. Four of the splice variants show loss of p53 binding.; TISSUE SPECIFICITY: Ubiquitous. Isoform Mdm2-A, isoform Mdm2-B, isoform Mdm2-C, isoform Mdm2-D, isoform Mdm2-E, isoform Mdm2-F and isoform Mdm2-G are observed in a range of cancers but absent in normal tissues.; unclassifiable (Anatomical System);ovary;heart;salivary gland;muscle;colon;parathyroid;blood;skeletal muscle;bone marrow;bile duct;breast;frontal lobe;thyroid;placenta;amnion;cervix;germinal center;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;globus pallidus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.97206 0.64023 -0.516085732 21.20193442 15.85758 0.56327 MDM4 0.998569577969579 0.00143039670950824 2.5320912809597e-08 MDM4, p53 regulator FUNCTION: Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions. {ECO:0000269|PubMed:16163388, ECO:0000269|PubMed:16511572}.; . TISSUE SPECIFICITY: Expressed in all tissues tested with high levels in thymus.; . . 0.83600 0.15993 0.084621747 60.31493277 152.98123 2.70549 MDN1 0.999999999489064 5.10936052209766e-10 1.27550885482691e-47 midasin AAA ATPase 1 FUNCTION: Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits. {ECO:0000250}.; . . . . 0.36790 0.09560 0.593567936 82.51946214 7714.21393 18.89924 MDP1 0.00152615928709452 0.87938848111776 0.119085359595145 magnesium-dependent phosphatase 1 FUNCTION: Magnesium-dependent phosphatase which may act as a tyrosine phosphatase. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney; . . . -0.05129383 49.75819769 1631.17778 7.46760 MDRV . . . muscular dystrophy, with rimmed vacuoles . . . . . . . . . . . MDS2 0.0429655728784688 0.662011892249917 0.295022534871614 myelodysplastic syndrome 2 translocation associated . . TISSUE SPECIFICITY: Highly expressed in peripheral blood leukocytes, spleen, thymus, kidney, pancreas and lung. {ECO:0000269|PubMed:12203785}.; . . 0.06917 . . . 3048.37206 10.49529 ME1 2.22311340829984e-10 0.239085964707002 0.760914035070687 malic enzyme 1, NADP(+)-dependent, cytosolic . . TISSUE SPECIFICITY: Expressed in all tissues tested including liver, placenta and white adipose tissue. {ECO:0000269|PubMed:7622060, ECO:0000269|PubMed:8187880}.; . . 0.15024 0.19766 -0.26629572 34.81953291 221.88912 3.22048 ME2 1.17412339312961e-07 0.985410833476723 0.014589049110938 malic enzyme 2, NAD(+)-dependent, mitochondrial . . . lymphoreticular;myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;trigeminal ganglion; 0.10782 0.14795 0.463046108 78.58575136 717.54115 5.31808 ME2P1 . . . malic enzyme 2, NAD(+)-dependent, mitochondrial pseudogene 1 . . . . . . . . . . . ME3 1.1418824476976e-05 0.9877460703053 0.0122425108702234 malic enzyme 3, NADP(+)-dependent, mitochondrial . . TISSUE SPECIFICITY: Expressed predominantly in organs with a low- division rate.; myocardium;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;endometrium;testis;pineal gland;brain;unclassifiable (Anatomical System);islets of Langerhans;lens;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;hippocampus;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;skeletal muscle; 0.21938 0.18427 -0.821100135 11.88369899 2619.18186 9.59290 MEA1 0.0434012333734021 0.848806820150508 0.10779194647609 male-enhanced antigen 1 FUNCTION: May play an important role in spermatogenesis and/or testis development.; . TISSUE SPECIFICITY: Highly expressed in testis.; lymphoreticular;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;pancreas;lung;cornea;placenta;head and neck;kidney;stomach;aorta;thymus; subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;hypothalamus;prefrontal cortex;globus pallidus;testis;caudate nucleus;pons;cingulate cortex;parietal lobe; 0.59479 0.27766 0.215080721 67.91696155 278.31327 3.57483 MEAF6 0.730388139479782 0.269048651591429 0.000563208928789487 MYST/Esa1 associated factor 6 FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. {ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:18794358}.; DISEASE: Note=A chromosomal aberration involving MEAF6 may be a cause of endometrial stromal tumors. Translocation t(1;6)(p34;p21) with PHF1. {ECO:0000269|PubMed:22761769}.; . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;cerebral cortex;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach;aorta; amygdala;superior cervical ganglion;testis;cingulate cortex;pituitary; 0.18507 0.10264 -0.09720619 46.20193442 5.77712 0.21811 MEAF6P1 . . . MYST/Esa1-associated factor 6 pseudogene 1 . . . . . . . . . . . MECOM 0.999085313439389 0.000914686212000441 3.4861021653468e-10 MDS1 and EVI1 complex locus FUNCTION: Functions as a transcriptional regulator binding to DNA sequences in the promoter region of target genes and regulating positively or negatively their expression. Oncogene which plays a role in development, cell proliferation and differentiation. May also play a role in apoptosis through regulation of the JNK and TGF-beta signaling. Involved in hematopoiesis. {ECO:0000269|PubMed:10856240, ECO:0000269|PubMed:11568182, ECO:0000269|PubMed:15897867, ECO:0000269|PubMed:16462766, ECO:0000269|PubMed:19767769, ECO:0000269|PubMed:9665135}.; DISEASE: Note=A chromosomal aberration involving EVI1 is a cause of chronic myelogenous leukemia (CML). Translocation t(3;21)(q26;q22) with RUNX1/AML1. {ECO:0000269|PubMed:8313895}.; . ovary;salivary gland;intestine;colon;vein;skin;retina;bone marrow;uterus;prostate;endometrium;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;skeletal muscle;pancreas;lung;nasopharynx;visual apparatus;liver;head and neck;kidney;stomach; atrioventricular node; 0.47994 0.30246 -0.993849454 8.56334041 1129.59722 6.41503 MECP2 0.698089047724915 0.298098137470804 0.00381281480428095 methyl-CpG binding protein 2 FUNCTION: Chromosomal protein that binds to methylated DNA. It can bind specifically to a single methyl-CpG pair. It is not influenced by sequences flanking the methyl-CpGs. Mediates transcriptional repression through interaction with histone deacetylase and the corepressor SIN3A. Binds both 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC)-containing DNA, with a preference for 5-methylcytosine (5mC). {ECO:0000250|UniProtKB:Q9Z2D6}.; DISEASE: Angelman syndrome (AS) [MIM:105830]: A neurodevelopmental disorder characterized by severe motor and intellectual retardation, ataxia, frequent jerky limb movements and flapping of the arms and hands, hypotonia, seizures, absence of speech, frequent smiling and episodes of paroxysmal laughter, open-mouthed expression revealing the tongue. {ECO:0000269|PubMed:11283202}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Mental retardation, X-linked, syndromic, 13 (MRXS13) [MIM:300055]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXS13 patients manifest mental retardation associated with other variable features such as spasticity, episodes of manic depressive psychosis, increased tone and macroorchidism. {ECO:0000269|PubMed:10986043, ECO:0000269|PubMed:11007980, ECO:0000269|PubMed:11309367, ECO:0000269|PubMed:11805248, ECO:0000269|PubMed:11885030, ECO:0000269|PubMed:12161600, ECO:0000269|PubMed:12325019, ECO:0000269|PubMed:12615169, ECO:0000269|PubMed:16966553}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Rett syndrome (RTT) [MIM:312750]: An X-linked dominant neurodevelopmental disorder, and one of the most common causes of mental retardation in females. Patients appear to develop normally until 6 to 18 months of age, then gradually lose speech and purposeful hand movements, and develop microcephaly, seizures, autism, ataxia, mental retardation and stereotypic hand movements. After initial regression, the condition stabilizes and patients usually survive into adulthood. {ECO:0000269|PubMed:10508514, ECO:0000269|PubMed:10577905, ECO:0000269|PubMed:10745042, ECO:0000269|PubMed:10767337, ECO:0000269|PubMed:10814719, ECO:0000269|PubMed:10944854, ECO:0000269|PubMed:10991688, ECO:0000269|PubMed:10991689, ECO:0000269|PubMed:11055898, ECO:0000269|PubMed:11241840, ECO:0000269|PubMed:11269512, ECO:0000269|PubMed:11283202, ECO:0000269|PubMed:11376998, ECO:0000269|PubMed:11402105, ECO:0000269|PubMed:11706982, ECO:0000269|PubMed:11738883, ECO:0000269|PubMed:12161600, ECO:0000269|PubMed:12567420, ECO:0000269|PubMed:12966522, ECO:0000269|PubMed:12966523, ECO:0000269|PubMed:15034579, ECO:0000269|PubMed:15057977}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Autism, X-linked 3 (AUTSX3) [MIM:300496]: A complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation. {ECO:0000269|PubMed:12770674}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Encephalopathy, neonatal severe, due to MECP2 mutations (ENS-MECP2) [MIM:300673]: A neurodevelopmental disorder characterized by severe neonatal encephalopathy, developmental delay, mental retardation, microcephaly, seizures. Additional features include respiratory insufficiency and central hypoventilation, gastroesophageal reflux, axial hypotonia, hyperreflexia and dyskinetic movements. {ECO:0000269|PubMed:11238684}. Note=The disease is caused by mutations affecting the gene represented in this entry. The MECP2 gene is mutated in Rett syndrome, a severe neurodevelopmental disorder that almost always occurs in females. Although it was first thought that MECP2 mutations causing Rett syndrome were lethal in males, later reports identified a severe neonatal encephalopathy in surviving male sibs of patients with Rett syndrome. Additional reports have confirmed a severe phenotype in males with Rett syndrome-associated MECP2 mutations.; DISEASE: Mental retardation, X-linked, syndromic, Lubs type (MRXSL) [MIM:300260]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXSL patients manifest mental retardation associated with variable features. They include swallowing dysfunction and gastroesophageal reflux with secondary recurrent respiratory infections, hypotonia, mild myopathy and characteristic facies such as downslanting palpebral fissures, hypertelorism and a short nose with a low nasal bridge. {ECO:0000269|PubMed:16080119}. Note=The disease is caused by mutations affecting the gene represented in this entry. Increased dosage of MECP2 due to gene duplication appears to be responsible for the mental retardation phenotype.; TISSUE SPECIFICITY: Present in all adult somatic tissues tested.; ovary;adrenal medulla;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;cerebellum peduncles;prefrontal cortex;globus pallidus;pons;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.43937 0.69428 -0.885424753 10.4623732 83.03146 1.93651 MECR 0.0036031322030062 0.987096560482991 0.0093003073140025 mitochondrial trans-2-enoyl-CoA reductase FUNCTION: Oxidoreductase with a preference for short and medium chain substrates, including trans-2-hexenoyl-CoA (C6), trans-2- decenoyl-CoA (C10), and trans-2-hexadecenoyl-CoA (C16). May play a role in mitochondrial fatty acid synthesis. {ECO:0000269|PubMed:18479707}.; . TISSUE SPECIFICITY: Highly expressed in skeletal and heart muscle. Expressed at lower level in placenta, liver, kidney and pancreas. Weakly or not expressed in lung. {ECO:0000269|PubMed:12654921}.; ovary;colon;parathyroid;skin;uterus;prostate;whole body;oesophagus;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; subthalamic nucleus; 0.41571 0.11118 0.707379532 85.62750649 93.08303 2.07392 MED1 0.999990934196945 9.06580303267369e-06 2.26260897672473e-14 mediator complex subunit 1 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967, PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). {ECO:0000269|PubMed:10406464, ECO:0000269|PubMed:11867769, ECO:0000269|PubMed:12037571, ECO:0000269|PubMed:12218053, ECO:0000269|PubMed:12556447, ECO:0000269|PubMed:14636573, ECO:0000269|PubMed:15340084, ECO:0000269|PubMed:15471764, ECO:0000269|PubMed:15989967, ECO:0000269|PubMed:16574658, ECO:0000269|PubMed:24245781, ECO:0000269|PubMed:9653119}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9444950, ECO:0000269|PubMed:9653119}.; smooth muscle;ovary;salivary gland;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;epididymis;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;ciliary ganglion;white blood cells;trigeminal ganglion;parietal lobe;skeletal muscle; 0.87934 0.30413 -1.54691447 3.284972871 103.17229 2.19369 MED4 0.06162002785339 0.92224040785559 0.0161395642910194 mediator complex subunit 4 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.; . . medulla oblongata;smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;hypothalamus;oral cavity;bile duct;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; . 0.23352 0.13917 0.371224249 75.12384996 60.37955 1.57945 MED4-AS1 . . . MED4 antisense RNA 1 . . . . . . . . . . . MED6 0.0149679496565466 0.957722047589607 0.0273100027538468 mediator complex subunit 6 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:16595664}.; . . unclassifiable (Anatomical System);lymph node;tongue;colon;skin;skeletal muscle;breast;bile duct;prostate;pancreas;lung;bone;thyroid;visual apparatus;liver;testis;head and neck;spleen;kidney;brain;pineal gland;mammary gland;aorta;stomach; occipital lobe;white blood cells;trigeminal ganglion; 0.27220 0.12456 -0.251530012 35.42108988 19.14886 0.66015 MED6P1 . . . mediator complex subunit 6 pseudogene 1 . . . . . . . . . . . MED7 0.215739810584496 0.745430941193402 0.0388292482221021 mediator complex subunit 7 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;uterus;prostate;frontal lobe;cochlea;bone;thyroid;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;pons;trigeminal ganglion;skin; 0.34236 0.11809 0.525552348 80.57914603 71.89389 1.76547 MED8 8.1582621367423e-06 0.513447415132637 0.486544426605226 mediator complex subunit 8 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. May play a role as a target recruitment subunit in E3 ubiquitin-protein ligase complexes and thus in ubiquitination and subsequent proteasomal degradation of target proteins.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;endometrium;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;spinal cord;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.09740 0.08981 -0.205617011 38.57631517 21.34091 0.72081 MED9 0.315748748937312 0.614791127482031 0.0694601235806567 mediator complex subunit 9 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.; . . medulla oblongata;ovary;salivary gland;colon;fovea centralis;skin;uterus;frontal lobe;endometrium;iris;testis;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;lens;bile duct;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle;parietal lobe; 0.21731 0.11795 0.191216164 66.57230479 150.29468 2.67537 MED10 0.0397210577852175 0.840693447834137 0.119585494380645 mediator complex subunit 10 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;oesophagus;bone;thyroid;testis;germinal center;spinal ganglion;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;spleen;kidney;aorta;stomach; whole brain;superior cervical ganglion; 0.55477 0.11838 -0.075159878 47.78839349 4.43767 0.16105 MED11 7.54804274594897e-06 0.164878460933838 0.835113991023416 mediator complex subunit 11 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.13931 0.12628 0.013025609 54.62962963 5.65246 0.21205 MED12 0.999999998786565 1.21343475006275e-09 4.10769027540817e-23 mediator complex subunit 12 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. This subunit may specifically regulate transcription of targets of the Wnt signaling pathway and SHH signaling pathway. {ECO:0000269|PubMed:16565090, ECO:0000269|PubMed:16595664, ECO:0000269|PubMed:17000779}.; DISEASE: Lujan-Fryns syndrome (LUJFRYS) [MIM:309520]: Clinically, Lujan-Fryns syndrome can be distinguished from Opitz-Kaveggia syndrome by tall stature, hypernasal voice, hyperextensible digits and high nasal root. {ECO:0000269|PubMed:17369503}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ohdo syndrome, X-linked (OHDOX) [MIM:300895]: A syndrome characterized by mental retardation, feeding problems, and distinctive facial appearance with coarse facial features, severe blepharophimosis, ptosis, a bulbous nose, micrognathia and a small mouth. Dental hypoplasia and deafness can be considered as common manifestations of the syndrome. Male patients show cryptorchidism and scrotal hypoplasia. {ECO:0000269|PubMed:23395478}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10198638}.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;tongue;muscle;urinary;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;head and neck;cervix;kidney;stomach; adrenal gland; 0.46180 0.30592 -0.997481928 8.47487615 62.96611 1.62344 MED12L 0.99999927637145 7.23628549938227e-07 5.51117031177717e-24 mediator complex subunit 12 like FUNCTION: May be a component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}.; . . uterus;unclassifiable (Anatomical System);lung;heart;placenta;liver;testis;spleen;germinal center;brain;skin; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.38473 0.10234 -2.535908408 0.884642604 2054.448 8.35414 MED13 0.999999999944093 5.59073939016301e-11 2.28032880502861e-26 mediator complex subunit 13 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:16595664}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10198638}.; ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;hypothalamus;pharynx;blood;skeletal muscle;breast;bile duct;lung;placenta;visual apparatus;hypopharynx;duodenum;liver;spleen;head and neck;kidney;stomach;thymus; superior cervical ganglion;prefrontal cortex;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;skeletal muscle; 0.54617 0.13379 -1.425829947 4.051663128 348.29344 3.95460 MED13L 0.999999998677147 1.32285336955783e-09 2.07545059525534e-24 mediator complex subunit 13 like FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. This subunit may specifically regulate transcription of targets of the Wnt signaling pathway and SHH signaling pathway.; DISEASE: Note=A chromosomal aberration involving MED13L is found in a patient with transposition of the great arteries, dextro- looped and mental retardation. Translocation t(12;17)(q24.1;q21). {ECO:0000269|PubMed:14638541}.; TISSUE SPECIFICITY: Highly expressed in brain (cerebellum), heart (aorta), skeletal muscle, kidney, placenta and peripheral blood leukocytes. Highly expressed in fetal brain. {ECO:0000269|PubMed:14638541, ECO:0000269|PubMed:15145061}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; subthalamic nucleus;superior cervical ganglion;fetal brain;prefrontal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.80264 0.11567 -2.736273894 0.690021231 206.98599 3.10912 MED13P1 . . . mediator complex subunit 13 pseudogene 1 . . . . . . . . . . . MED14 0.999999382308837 6.17691162623187e-07 1.6098668904851e-16 mediator complex subunit 14 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:15340088, ECO:0000269|PubMed:15625066, ECO:0000269|PubMed:16595664}.; . TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;atrium;whole body;endometrium;oesophagus;larynx;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;epididymis;trabecular meshwork;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.68346 0.15290 -0.356299879 29.31115829 65.00362 1.65713 MED14OS . . . MED14 opposite strand . . . . . . . . . . . MED14P1 . . . mediator complex subunit 14 pseudogene 1 . . . . . . . . . . . MED15 0.960808622998609 0.0391913711650731 5.83631815978549e-09 mediator complex subunit 15 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Required for cholesterol-dependent gene regulation. Positively regulates the Nodal signaling pathway. {ECO:0000269|PubMed:12167862, ECO:0000269|PubMed:16630888, ECO:0000269|PubMed:16799563}.; . TISSUE SPECIFICITY: Expressed in all tissues examined, including heart, brain, lung, spleen, thymus, pancreas, blood leukocyte and placenta. However, the level of expression varied, with highest expression in the placenta and peripheral blood and lowest in the pancreas and kidney. {ECO:0000269|PubMed:11024300}.; lymphoreticular;myocardium;medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion; 0.73008 0.16585 -1.464150033 3.780372729 97.67863 2.13739 MED15P1 . . . mediator complex subunit 15 pseudogene 1 . . . . . . . . . . . MED15P3 . . . mediator complex subunit 15 pseudogene 3 . . . . . . . . . . . MED15P4 . . . mediator complex subunit 15 pseudogene 4 . . . . . . . . . . . MED15P5 . . . mediator complex subunit 15 pseudogene 5 . . . . . . . . . . . MED15P6 . . . mediator complex subunit 15 pseudogene 6 . . . . . . . . . . . MED15P7 . . . mediator complex subunit 15 pseudogene 7 . . . . . . . . . . . MED15P8 . . . mediator complex subunit 15 pseudogene 8 . . . . . . . . . . . MED15P9 . . . mediator complex subunit 15 pseudogene 9 . . . . . . . . . . . MED16 0.0187661183097687 0.980378376725149 0.000855504965082603 mediator complex subunit 16 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:10198638, ECO:0000269|PubMed:10235266}.; . . medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;adrenal cortex;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;skeletal muscle; 0.11694 0.12544 -2.73449852 0.701816466 593.04028 4.93572 MED17 3.88512441026693e-06 0.988331580049 0.0116645348265903 mediator complex subunit 17 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:16595664}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10198638}.; ovary;salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;stomach;thymus; . 0.08721 0.13056 -0.778825328 12.88039632 91.46386 2.05641 MED18 0.000448333946024653 0.423435756708827 0.576115909345148 mediator complex subunit 18 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.; . . . . 0.07430 0.12815 -0.073340031 48.11866006 26.75181 0.86635 MED19 0.683790051387125 0.296975939632807 0.019234008980068 mediator complex subunit 19 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;stomach;aorta;thymus; superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;atrioventricular node;trigeminal ganglion; 0.23390 0.09980 -0.009020804 52.8544468 18.86274 0.65163 MED20 0.48894272078137 0.489751134983363 0.0213061442352671 mediator complex subunit 20 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;atrium;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;aorta;stomach; dorsal root ganglion;medulla oblongata;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.11746 0.09517 -0.095386216 46.48502005 5.16999 0.19204 MED21 0.0580450998864159 0.86715269476293 0.0748022053506535 mediator complex subunit 21 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:15249124, ECO:0000269|PubMed:9660976}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;iris;testis;spinal ganglion;brain;pineal gland;bladder;unclassifiable (Anatomical System);trophoblast;cartilage;heart;adrenal cortex;pharynx;blood;breast;pancreas;lung;adrenal gland;mesenchyma;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.16820 0.22983 -0.009020804 52.8544468 0.847 0.01669 MED22 0.00632213991393259 0.910460433393173 0.0832174266928946 mediator complex subunit 22 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.; . . ovary;colon;choroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;lens;breast;pancreas;lung;placenta;visual apparatus;macula lutea;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.19191 0.11142 -0.071520315 48.34866714 58.19318 1.54382 MED23 0.150657691204943 0.849342306714803 2.08025487697261e-09 mediator complex subunit 23 FUNCTION: Required for transcriptional activation subsequent to the assembly of the pre-initiation complex (By similarity). Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors. Required for transcriptional activation by adenovirus E1A protein. Required for ELK1-dependent transcriptional activation in response to activated Ras signaling. {ECO:0000250, ECO:0000269|PubMed:10353252, ECO:0000269|PubMed:14759369, ECO:0000269|PubMed:16595664}.; DISEASE: Mental retardation, autosomal recessive 18 (MRT18) [MIM:614249]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:21868677}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;colon;skin;uterus;prostate;frontal lobe;cerebral cortex;larynx;bone;testis;amniotic fluid;germinal center;brain;gall bladder;unclassifiable (Anatomical System);heart;adrenal cortex;skeletal muscle;breast;lung;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.12285 0.15367 -1.131590109 6.481481481 64.0853 1.64122 MED24 8.98959437658566e-09 0.99504615460403 0.00495383640637555 mediator complex subunit 24 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:12218053, ECO:0000269|PubMed:16595664}.; . TISSUE SPECIFICITY: Ubiquitous. Abundant in skeletal muscle, heart and placenta. {ECO:0000269|PubMed:9653119}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;thymus; testis; 0.21562 0.13192 -1.414605945 4.134229771 85.15958 1.96749 MED25 0.00112987749552536 0.998451305646219 0.000418816858256046 mediator complex subunit 25 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Required for RARA/RXRA-mediated transcription. {ECO:0000269|PubMed:14657022, ECO:0000269|PubMed:14983011, ECO:0000269|PubMed:17641689}.; DISEASE: Basel-Vanagaite-Smirin-Yosef syndrome (BVSYS) [MIM:616449]: An autosomal recessive syndrome characterized by eye, brain, cardiac and palatal abnormalities as well as growth retardation, microcephaly and severe intellectual disability. {ECO:0000269|PubMed:25792360}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. Highest levels in brain, heart, kidney, peripheral leukocytes, placenta, skeletal muscle and spleen. {ECO:0000269|PubMed:14657022, ECO:0000269|PubMed:14983011}.; medulla oblongata;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;lens;breast;pancreas;macula lutea;visual apparatus;liver;cervix;head and neck;kidney;stomach; superior cervical ganglion;testis - seminiferous tubule;adrenal cortex;globus pallidus;trigeminal ganglion;skeletal muscle; 0.15992 0.14846 -0.532670911 20.78320359 75.1226 1.81409 MED26 0.948549941884627 0.0514161037982289 3.39543171441838e-05 mediator complex subunit 26 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors.; . . unclassifiable (Anatomical System);lymphoreticular;pancreas;lung;ovary;placenta;liver;testis;spleen;skin; . 0.37459 . -1.219785504 5.602736494 57.77804 1.53591 MED27 0.00360424731766106 0.954104443021125 0.0422913096612143 mediator complex subunit 27 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:10882111, ECO:0000269|PubMed:9989412}.; . . smooth muscle;ovary;salivary gland;colon;skin;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;oesophagus;endometrium;synovium;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;duodenum;liver;spleen;cervix;kidney;stomach; superior cervical ganglion;subthalamic nucleus;testis;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.17514 0.10935 -0.471992905 23.03609342 100.73367 2.17386 MED28 0.00785226414652491 0.783300701617309 0.208847034236166 mediator complex subunit 28 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. May be part of a complex containing NF2/merlin that participates in cellular signaling to the actin cytoskeleton downstream of tyrosine kinase signaling pathways. {ECO:0000269|PubMed:15467741}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in vascular tissues such as placenta, testis and liver. {ECO:0000269|PubMed:15467741}.; unclassifiable (Anatomical System);trophoblast;heart;ovary;islets of Langerhans;colon;parathyroid;choroid;vein;uterus;pancreas;lung;frontal lobe;adrenal gland;thyroid;placenta;liver;spleen;germinal center;kidney;brain;mammary gland; testis;atrioventricular node;trigeminal ganglion; 0.12502 0.16583 -0.05129383 49.75819769 27.92413 0.89654 MED28P1 . . . mediator complex subunit 28 pseudogene 1 . . . . . . . . . . . MED28P2 . . . mediator complex subunit 28 pseudogene 2 . . . . . . . . . . . MED28P3 . . . mediator complex subunit 28 pseudogene 3 . . . . . . . . . . . MED28P4 . . . mediator complex subunit 28 pseudogene 4 . . . . . . . . . . . MED28P5 . . . mediator complex subunit 28 pseudogene 5 . . . . . . . . . . . MED28P6 . . . mediator complex subunit 28 pseudogene 6 . . . . . . . . . . . MED28P7 . . . mediator complex subunit 28 pseudogene 7 . . . . . . . . . . . MED28P8 . . . mediator complex subunit 28 pseudogene 8 . . . . . . . . . . . MED29 0.00101225805500751 0.592845475481582 0.406142266463411 mediator complex subunit 29 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:15555573}.; . TISSUE SPECIFICITY: Widely expressed in embryo and adult. {ECO:0000269|PubMed:15555573}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);heart;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach; amygdala;hypothalamus;prefrontal cortex;globus pallidus; 0.13661 0.10845 -0.361761279 28.6329323 20.91416 0.70746 MED30 0.606541510277703 0.384770925387378 0.00868756433491867 mediator complex subunit 30 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:11909976, ECO:0000269|PubMed:16595664}.; . TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. {ECO:0000269|PubMed:11909976}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;frontal lobe;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;breast;lung;adrenal gland;placenta;visual apparatus;liver;spleen;kidney;mammary gland; . 0.50685 0.13588 0.281220278 71.07808445 114.26306 2.32898 MED31 0.000283388364942475 0.558198446044474 0.441518165590583 mediator complex subunit 31 FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.; . . fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;thyroid;testis;germinal center;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;blood;lens;skeletal muscle;pancreas;lung;pia mater;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.14472 0.11809 0.013025609 54.62962963 . . MEDAG 0.000667054100444806 0.741438389331924 0.257894556567631 mesenteric estrogen-dependent adipogenesis FUNCTION: Involved in processes that promote adipocyte differentiation, lipid accumulation, and glucose uptake in mature adipocytes. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in the visceral fat depot. {ECO:0000269|PubMed:22510272}.; . . 0.39658 . -0.183570861 39.95046001 435.40313 4.35200 MEF2A 0.737169983273076 0.262307544407043 0.000522472319881006 myocyte enhancer factor 2A FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle- specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation. Associates with chromatin to the ZNF16 promoter. {ECO:0000269|PubMed:11904443, ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:15834131, ECO:0000269|PubMed:16371476, ECO:0000269|PubMed:16484498, ECO:0000269|PubMed:16563226, ECO:0000269|PubMed:21468593, ECO:0000269|PubMed:9858528}.; DISEASE: Coronary artery disease, autosomal dominant, 1 (ADCAD1) [MIM:608320]: A common heart disease characterized by reduced or absent blood flow in one or more of the arteries that encircle and supply the heart. Its most important complication is acute myocardial infarction. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform MEF2 and isoform MEFA are expressed only in skeletal and cardiac muscle and in the brain. Isoform RSRFC4 and isoform RSRFC9 are expressed in all tissues examined. {ECO:0000269|PubMed:1516833, ECO:0000269|PubMed:1748287}.; myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;mesenchyma;nasopharynx;placenta;head and neck;kidney;stomach;aorta;cerebellum; amygdala;whole brain;occipital lobe;medulla oblongata;thalamus;superior cervical ganglion;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.75286 0.23693 -0.314027422 31.9297004 66.20773 1.67636 MEF2AP1 . . . myocyte enhancer factor 2A pseudogene 1 . . . . . . . . . . . MEF2B 0.590447262915793 0.407452111810519 0.00210062527368732 myocyte enhancer factor 2B FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle- specific genes. Activates transcription via this element. May be involved in muscle-specific and/or growth factor-related transcription.; . TISSUE SPECIFICITY: Expressed in skeletal and cardiac muscle and brain.; unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;colon;parathyroid;blood;skeletal muscle;retina;uterus;pancreas;prostate;lung;frontal lobe;thyroid;placenta;liver;testis;spleen;germinal center;brain;stomach;peripheral nerve; superior cervical ganglion;tumor;skeletal muscle; 0.16431 0.09173 -0.60427181 17.74593064 163.09668 2.78867 MEF2BNBP1 . . . MEF2B neighbor pseudogene 1 . . . . . . . . . . . MEF2C 0.00424617418418377 0.988383682679559 0.00737014313625715 myocyte enhancer factor 2C FUNCTION: Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle- specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells. May also be involved in neurogenesis and in the development of cortical architecture (By similarity). Isoform 3 and isoform 4, which lack the repressor domain, are more active than isoform 1 and isoform 2. {ECO:0000250, ECO:0000269|PubMed:11904443, ECO:0000269|PubMed:15340086, ECO:0000269|PubMed:15831463, ECO:0000269|PubMed:15834131, ECO:0000269|PubMed:9069290, ECO:0000269|PubMed:9384584}.; DISEASE: Mental retardation, autosomal dominant 20 (MRD20) [MIM:613443]: A disorder characterized by severe mental retardation, absent speech, hypotonia, poor eye contact and stereotypic movements. Dysmorphic features include high broad forehead with variable small chin, short nose with anteverted nares, large open mouth, upslanted palpebral fissures and prominent eyebrows. Some patients have seizures. {ECO:0000269|PubMed:19592390}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain and skeletal muscle. {ECO:0000269|PubMed:9798649}.; myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;larynx;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;tongue;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;peripheral nerve; whole brain;amygdala;medulla oblongata;occipital lobe;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.97825 0.09412 0.057118534 57.99716914 6.52455 0.24153 MEF2C-AS1 . . . MEF2C antisense RNA 1 . . . . . . . . . . . MEF2D 0.998547093289291 0.00145288040850399 2.63022049317052e-08 myocyte enhancer factor 2D FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle- specific, growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. Plays a critical role in the regulation of neuronal apoptosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:10849446, ECO:0000269|PubMed:11904443, ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:15743823, ECO:0000269|PubMed:15834131}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;synovium;bone;iris;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;medulla oblongata;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.86578 0.19297 -0.624497208 17.16206653 24.10793 0.79190 MEFV 1.12014488205382e-08 0.531732189990104 0.468267798808448 Mediterranean fever FUNCTION: Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma. Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1, ATG16L1, and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy. Acts as an autophagy receptor for the degradation of several inflammasome components, including CASP1, NLRP1 and NLRP3, hence preventing excessive IL1B- and IL18- mediated inflammation (PubMed:16785446, PubMed:17431422, PubMed:26347139). However, it may also have a positive effect in the inflammatory pathway. In different experimental systems, it has been shown to activate IL1B production (PubMed:16037825). It has also been shown to be required for PSTPIP1-induced PYCARD oligomerization and for formation of inflammasomes. Recruits PSTPIP1 to inflammasomes, and is required for PSTPIP1 oligomerization (PubMed:10807793, PubMed:11468188, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923). {ECO:0000269|PubMed:10807793, ECO:0000269|PubMed:11468188, ECO:0000269|PubMed:16037825, ECO:0000269|PubMed:16785446, ECO:0000269|PubMed:17431422, ECO:0000269|PubMed:17964261, ECO:0000269|PubMed:18577712, ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923, ECO:0000269|PubMed:26347139}.; DISEASE: Familial Mediterranean fever, autosomal recessive (ARFMF) [MIM:249100]: A hereditary periodic fever syndrome characterized by recurrent episodic fever, serosal inflammation and pain in the abdomen, chest or joints. It is frequently complicated by reactive amyloidosis, which leads to renal failure and can be prophylactically treated with colchicine. {ECO:0000269|PubMed:10024914, ECO:0000269|PubMed:10090880, ECO:0000269|PubMed:10234504, ECO:0000269|PubMed:10364520, ECO:0000269|PubMed:10612841, ECO:0000269|PubMed:10842288, ECO:0000269|PubMed:10854105, ECO:0000269|PubMed:11470495, ECO:0000269|PubMed:15024744, ECO:0000269|PubMed:16378925, ECO:0000269|PubMed:16730661, ECO:0000269|PubMed:23031807, ECO:0000269|PubMed:24929125, ECO:0000269|PubMed:26347139, ECO:0000269|PubMed:9288094, ECO:0000269|PubMed:9288758, ECO:0000269|PubMed:9668175}. Note=The disease is caused by mutations affecting the gene represented in this entry. The disease-associated mutations in the B30.2/SPRY domain perturb ULK1 recruitment and autophagic degradation of inflammasome components, including NLRP3, and hence may contribute to the inflammatory phenotype associated with ARFMF. {ECO:0000269|PubMed:26347139}.; DISEASE: Familial Mediterranean fever, autosomal dominant (ADFMF) [MIM:134610]: A hereditary periodic fever syndrome characterized by periodic fever, serosal inflammation and pain in the abdomen, chest or joints as seen also in the autosomal recessive form of the disease. It is associated with reactive renal amyloidosis and characterized by colchicine unresponsiveness. {ECO:0000269|PubMed:10787449, ECO:0000269|PubMed:14679589}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes, particularly in mature granulocytes and to a lesser extent in monocytes but not in lymphocytes. Detected in spleen, lung and muscle, probably as a result of leukocyte infiltration in these tissues. Not expressed in thymus, prostate, testis, ovary, small intestine, colon, heart, brain, placenta, liver, kidney, pancreas. Expression detected in several myeloid leukemic, colon cancer, and prostate cancer cell lines. {ECO:0000269|PubMed:10666224, ECO:0000269|PubMed:10807793, ECO:0000269|PubMed:11115844}.; blood;bone marrow; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.08760 0.21433 1.18861158 92.84619014 1463.7814 7.13488 MEG3 . . . maternally expressed 3 (non-protein coding) . . . . . 0.45272 . . . . . MEG8 . . . maternally expressed 8 (non-protein coding) . . . . . . . . . . . MEG9 . . . maternally expressed 9 (non-protein coding) . . . . . . . . . . . MEGF6 4.42421031130217e-15 0.994620434269407 0.00537956573058837 multiple EGF like domains 6 . . . unclassifiable (Anatomical System);myocardium;heart;ovary;urinary;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;prostate;optic nerve;lung;placenta;macula lutea;testis;kidney;brain; . 0.11042 0.09881 2.072624965 97.81198396 6730.46373 17.39874 MEGF8 0.973137204425084 0.0268627955749157 2.627423540134e-16 multiple EGF like domains 8 . DISEASE: Carpenter syndrome 2 (CRPT2) [MIM:614976]: An autosomal recessive multiple congenital malformation disorder characterized by multisuture craniosynostosis and polysyndactyly of the hands and feet, in association with abnormal left-right patterning and other features, most commonly obesity, umbilical hernia, cryptorchidism, and congenital heart disease. {ECO:0000269|PubMed:23063620}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;parathyroid;skin;retina;uterus;optic nerve;frontal lobe;gum;bone;testis;bladder;brain;spinal ganglion;unclassifiable (Anatomical System);heart;cartilage;muscle;lens;breast;bile duct;lung;placenta;visual apparatus;liver;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.72681 0.12244 -4.008216118 0.188723756 506.62522 4.61892 MEGF9 0.921919104573547 0.077983329034089 9.7566392364507e-05 multiple EGF like domains 9 . . . . . 0.08401 0.07492 -0.380166007 27.88393489 119.86779 2.38477 MEGF10 0.994324945081641 0.00567505490820436 1.01543340542837e-11 multiple EGF like domains 10 FUNCTION: Membrane receptor involved in phagocytosis by macrophages of apoptotic cells. Cooperates with ABCA1 within the process of engulfment. Promotes the formation of large intracellular vacuoles and may be responsible for the uptake of amyloid-beta peptides. May also function in the mosaic spacing of specific neuron subtypes in the retina through homotypic retinal neuron repulsion. Mosaics provide a mechanism to distribute each cell type evenly across the retina, ensuring that all parts of the visual field have access to a full set of processing elements. May play role in cell adhesion and motility. Is also an essential factor in the regulation of myogenesis. Controls the balance between skeletal muscle satellite cells proliferation and differentiation problably through regulation of the notch signaling pathway. {ECO:0000269|PubMed:17498693, ECO:0000269|PubMed:17643423, ECO:0000269|PubMed:20828568, ECO:0000269|PubMed:22101682}.; DISEASE: Myopathy, early-onset, areflexia, respiratory distress, and dysphagia (EMARDD) [MIM:614399]: An autosomal recessive congenital myopathy characterized by onset at birth, or early in infancy, of respiratory distress caused by diaphragmatic weakness. Additional features are dysphagia resulting in poor feeding, failure to thrive, poor head control, facial weakness, cleft palate, contractures and scoliosis. Affected individuals become ventilator-dependent, and most require feeding by gastrostomy. The disorder results in severe muscle weakness and most patients never achieve walking. Death from respiratory failure in childhood occurs in about half of patients. Muscle biopsies from affected individuals show myopathic changes, replacement of myofibers with fatty tissue, small and incompletely fused muscle fibers, and variation in fiber size. Short regions of sarcomeric disorganization with few or no mitochondria (minicores) have been observed in some cases. {ECO:0000269|PubMed:22101682, ECO:0000269|PubMed:22371254}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);amygdala;heart;cartilage;hypothalamus;muscle;frontal lobe;bone;visual apparatus;alveolus;head and neck;pineal gland;brain; amygdala;medulla oblongata;occipital lobe;hypothalamus;caudate nucleus;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.09064 0.12411 -1.208913043 5.720688842 1243.14935 6.65909 MEGF11 2.5182184269378e-24 0.000112092785981292 0.999887907214019 multiple EGF like domains 11 FUNCTION: May regulate the mosaic spacing of specific neuron subtypes in the retina through homotypic retinal neuron repulsion. Mosaics provide a mechanism to distribute each cell type evenly across the retina, ensuring that all parts of the visual field have access to a full set of processing elements (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;visual apparatus;testis;kidney;brain; whole brain;dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;cerebellum peduncles;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.35561 0.08845 -0.635637306 16.76102854 4063.5662 12.63975 MEHMO . . . mental retardation, epileptic seizures, hypogonadism and -genitalism, microcephaly and obesity syndrome . . . . . . . . . . . MEI1 1.21592363387865e-08 0.999343450377943 0.000656537462821233 meiotic double-stranded break formation protein 1 FUNCTION: Required for normal meiotic chromosome synapsis. May be involved in the formation of meiotic double-strand breaks (DSBs) in spermatocytes (By similarity). {ECO:0000250|UniProtKB:Q9D4I2}.; . TISSUE SPECIFICITY: Expressed predominantly in testis. Weakly expressed in spleen and thymus. {ECO:0000269|PubMed:16683055}.; unclassifiable (Anatomical System);lung;testis; . 0.08112 . -0.457443171 23.70252418 1408.29264 7.01152 MEI4 . . . meiotic double-stranded break formation protein 4 FUNCTION: Required for meiotic DNA double-strand break formation. {ECO:0000250}.; . . . . . . . . 529.28518 4.69549 MEIG1 0.0531737986074582 0.698909229858591 0.24791697153395 meiosis/spermiogenesis associated 1 FUNCTION: Essential for spermiogenesis. {ECO:0000250}.; . . . . 0.14007 0.09549 0.347360312 73.97381458 29.92716 0.95591 MEIKIN . . . meiotic kinetochore factor FUNCTION: Key regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase- mediated cleavage. Acts by facilitating kinetochore mono- orientation during meiosis I, when kinetochores on sister chromosomes face the same direction and are thus captured and pulled by spindle fibers from the same pole. Also required to prevent cleavage of cohesin at centromeres during meiosis I, possibly by acting as a regulator of the shugoshin-dependent protection pathway. Acts in collaboration with PLK1: required for PLK1 enrichemnt to kinetochores. Not required during meiosis II or mitosis. {ECO:0000250|UniProtKB:Q5F2C3}.; . . . . . . . . . . MEIOB 9.45110442754297e-07 0.178667759338626 0.821331295550932 meiosis specific with OB domains FUNCTION: Single-stranded DNA-binding protein required for homologous recombination in meiosis I. Required for double strand breaks (DSBs) repair and crossover formation and promotion of faithful and complete synapsis. Not required for the initial loading of recombinases but required to maintain a proper number of RAD51 and DMC1 foci after the zygotene stage. May act by ensuring the stabilization of recombinases, which is required for successful homology search and meiotic recombination. Displays Single-stranded DNA 3'-5' exonuclease activity in vitro (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: In fetal gonads, specifically expressed in the ovary starting at the 14th weeks post fertilization. {ECO:0000269|PubMed:24068956}.; . . 0.13047 . 0.995816767 90.62278839 2666.37405 9.71386 MEIOC . . . meiosis specific with coiled-coil domain . . . . . . . 0.643056625 84.05284265 . . MEIS1 0.99088519686075 0.00911247429222156 2.32884702805072e-06 Meis homeobox 1 FUNCTION: Acts as a transcriptional regulator of PAX6. Acts as a transcriptional activator of PF4 in complex with PBX1 or PBX2. Required for hematopoiesis, megakaryocyte lineage development and vascular patterning. May function as a cofactor for HOXA7 and HOXA9 in the induction of myeloid leukemias. {ECO:0000269|PubMed:12609849}.; . TISSUE SPECIFICITY: Expressed at low level in normal immunohepatopoietic tissues, including the fetal liver. Expressed in a subset of myeloid leukemia cell lines, with the highest expression seen in those with a megakaryocytic-erythroid phenotype. Also expressed at high levels in the cerebellum.; smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;endometrium;thyroid;testis;ciliary body;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;head and neck;kidney;stomach; uterus;superior cervical ganglion;adrenal gland;appendix;pons;cerebellum; 0.84073 0.23021 -0.317668748 31.45789101 129.87684 2.48316 MEIS1-AS2 . . . MEIS1 antisense RNA 2 . . . . . . . . . . . MEIS1-AS3 . . . MEIS1 antisense RNA 3 . . . . . . . . . . . MEIS2 0.994254955106549 0.00574489245792612 1.52435524776903e-07 Meis homeobox 2 FUNCTION: Involved in transcriptional regulation. Binds to HOX or PBX proteins to form dimers, or to a DNA-bound dimer of PBX and HOX proteins and thought to have a role in stabilization of the homeoprotein-DNA complex. Isoform 3/Meis2B is required for the activity of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element; MEIS2 is not involved in complex DNA-binding. Probably in complex with PBX1, is involved in transcriptional regulation by KLF4. Isoform 3/Meis2B and isoform 4/Meis2D can bind to a EPHA8 promoter sequence containing the DNA motif 5'-CGGTCA-3'; in cooperation with a PBX protein (such as PBX2) is proposed to be involved in the transcriptional activation of EPHA8 in the developing midbrain. May be involved in regulation of myeloid differentiation. Can bind to the DNA sequence 5'-TGACAG-3'in the activator ACT sequence of the D(1A) dopamine receptor (DRD1) promoter and activate DRD1 transcription; isoform 5/Meis2E cannot activate DRD1 transcription. {ECO:0000269|PubMed:10764806, ECO:0000269|PubMed:11279116, ECO:0000269|PubMed:21746878}.; . TISSUE SPECIFICITY: Expressed in various tissues. Expressed at high level in the lymphoid organs of hematopoietic tissues. Also expressed in some regions of the brain, such as the putamen.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;lens;skeletal muscle;bile duct;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;aorta;stomach; uterus;amygdala;medulla oblongata;prostate;superior cervical ganglion;fetal brain;prefrontal cortex;caudate nucleus;pons; 0.62057 0.16306 -0.404032746 26.53338051 27.01195 0.87232 MEIS3 0.000113442628590687 0.950137230617103 0.0497493267543068 Meis homeobox 3 FUNCTION: Transcriptional regulator which directly modulates PDPK1 expression, thus promoting survival of pancreatic beta-cells. Also regulates expression of NDFIP1, BNIP3, and CCNG1. {ECO:0000250|UniProtKB:P97368}.; . . cartilage;tongue;islets of Langerhans;colon;lung;frontal lobe;cornea;larynx;placenta;thyroid;testis;head and neck;kidney;brain;mammary gland;stomach; . 0.18471 . -0.134019284 43.90776126 120.0041 2.38823 MEIS3P1 . . . Meis homeobox 3 pseudogene 1 . . . . . 0.18471 . -0.134019284 43.90776126 . . MEIS3P2 . . . Meis homeobox 3 pseudogene 2 . . . unclassifiable (Anatomical System);optic nerve;lung;heart;bone;macula lutea;fovea centralis;choroid;lens;retina; . . . . . . . MELAS . . . mitochondrial encephalomyopathy, lactic acidosis, and stroke-like episodes . . . . . . . . . . . MELK 1.8665175196218e-08 0.855175379036026 0.144824602298799 maternal embryonic leucine zipper kinase FUNCTION: Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation and carcinogenesis. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14, possibly leading to affect mammary carcinogenesis by mediating inhibition of the pro-apoptotic function of BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis. {ECO:0000269|PubMed:11802789, ECO:0000269|PubMed:12400006, ECO:0000269|PubMed:14699119, ECO:0000269|PubMed:15908796, ECO:0000269|PubMed:16216881, ECO:0000269|PubMed:17280616}.; DISEASE: Note=Defects in MELK are associated with some cancers, such as brain or breast cancers. Expression is dramatically increased in aggressive undifferentiated tumors, correlating with poor patient outcome in breast and brain cancers, suggesting a role in tumor-initiating cells and proliferation via its function in cell proliferation regulation.; TISSUE SPECIFICITY: Expressed in placenta, kidney, thymus, testis, ovary and intestine. {ECO:0000269|PubMed:8724849}.; lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;amniotic fluid;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;breast;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;kidney;stomach; testis - interstitial;tumor;testis;trigeminal ganglion; 0.44409 0.17917 0.622829232 83.47487615 504.02932 4.60800 MELTF . . . melanotransferrin FUNCTION: Involved in iron cellular uptake. Seems to be internalized and then recycled back to the cell membrane. Binds a single atom of iron per subunit. Could also bind zinc. {ECO:0000269|PubMed:7556058}.; . TISSUE SPECIFICITY: Found predominantly in human melanomas and in certain fetal tissues; also found in liver, epithelium, umbilical chord, placenta and sweat gland ducts.; . . 0.10835 0.16262 -0.093786226 46.49681529 . . MEMO1 0.876156693867831 0.12377786257988 6.54435522894351e-05 mediator of cell motility 1 FUNCTION: May control cell migration by relaying extracellular chemotactic signals to the microtubule cytoskeleton. Mediator of ERBB2 signaling. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Is required for breast carcinoma cell migration. {ECO:0000269|PubMed:15156151, ECO:0000269|PubMed:20937854}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;muscle;pharynx;blood;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;visual apparatus;duodenum;liver;spleen;cervix;kidney;stomach;aorta;peripheral nerve; . 0.73073 0.14281 0.013025609 54.62962963 29.85889 0.95287 MEMO1P1 . . . mediator of cell motility 1 pseudogene 1 . . . . . . . . . . . MEMO1P2 . . . mediator of cell motility 1 pseudogene 2 . . . . . . . . . . . MEMO1P3 . . . mediator of cell motility 1 pseudogene 3 . . . . . . . . . . . MEMO1P4 . . . mediator of cell motility 1 pseudogene 4 . . . . . . . . . . . MEMO1P5 . . . mediator of cell motility 1 pseudogene 5 . . . . . . . . . . . MEN1 0.999190000895056 0.000809992773506418 6.33143767171756e-09 menin 1 FUNCTION: Essential component of a MLL/SET1 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3 (H3K4). Functions as a transcriptional regulator. Binds to the TERT promoter and represses telomerase expression. Plays a role in TGFB1-mediated inhibition of cell-proliferation, possibly regulating SMAD3 transcriptional activity. Represses JUND-mediated transcriptional activation on AP1 sites, as well as that mediated by NFKB subunit RELA. Positively regulates HOXC8 and HOXC6 gene expression. May be involved in normal hematopoiesis through the activation of HOXA9 expression (By similarity). May be involved in DNA repair. {ECO:0000250, ECO:0000269|PubMed:11274402, ECO:0000269|PubMed:11526476, ECO:0000269|PubMed:12837246, ECO:0000269|PubMed:12874027, ECO:0000269|PubMed:14992727}.; DISEASE: Familial isolated hyperparathyroidism (FIHP) [MIM:145000]: Autosomal dominant disorder characterized by hypercalcemia, elevated parathyroid hormone (PTH) levels, and uniglandular or multiglandular parathyroid tumors. {ECO:0000269|PubMed:10634381, ECO:0000269|PubMed:10664521, ECO:0000269|PubMed:12016470, ECO:0000269|PubMed:12699448, ECO:0000269|PubMed:9792884, ECO:0000269|PubMed:9843042, ECO:0000269|PubMed:9888389}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;choroid;skin;bone marrow;uterus;subthalamic nucleus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;nervous;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;breast;bile duct;pancreas;lung;epididymis;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;stomach;peripheral nerve;thymus; medulla oblongata;superior cervical ganglion;ciliary ganglion;pons;skeletal muscle;cerebellum; 0.51278 . -0.26993514 34.59542345 52.48808 1.43370 MEOX1 0.0653974038800068 0.870906199869556 0.0636963962504376 mesenchyme homeobox 1 FUNCTION: Mesodermal transcription factor that plays a key role in somitogenesis and is specifically required for sclerotome development. Required for maintenance of the sclerotome polarity and formation of the cranio-cervical joints (PubMed:23290072, PubMed:24073994). Binds specifically to the promoter of target genes and regulates their expression. Activates expression of NKX3-2 in the sclerotome. Activates expression of CDKN1A and CDKN2A in endothelial cells, acting as a regulator of vascular cell proliferation. While it activates CDKN1A in a DNA-dependent manner, it activates CDKN2A in a DNA-independent manner. Required for hematopoietic stem cell (HSCs) induction via its role in somitogenesis: specification of HSCs occurs via the deployment of a specific endothelial precursor population, which arises within a sub-compartment of the somite named endotome. {ECO:0000250|UniProtKB:F1Q4R9, ECO:0000250|UniProtKB:P32442, ECO:0000269|PubMed:23290072, ECO:0000269|PubMed:24073994}.; DISEASE: Klippel-Feil syndrome 2, autosomal recessive (KFS2) [MIM:214300]: A skeletal disorder characterized by congenital fusion of cervical vertebrae. It is due to a failure in the normal segmentation of vertebrae during the early weeks of fetal development. The clinical triad consists of short neck, low posterior hairline, and limited neck movement. {ECO:0000269|PubMed:23290072, ECO:0000269|PubMed:24073994}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;ovary;cartilage;muscle;parathyroid;skin;uterus;prostate;whole body;lung;placenta;bone;testis;spinal ganglion;brain;aorta; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.83330 0.10463 0.639420866 83.8995046 1445.29004 7.09034 MEOX2 0.6852347181888 0.310442542402344 0.00432273940885601 mesenchyme homeobox 2 FUNCTION: Mesodermal transcription factor that plays a key role in somitogenesis and is required for sclerotome development (By similarity). Activates expression of CDKN1A and CDKN2A in endothelial cells, acting as a regulator of vascular cell proliferation. While it activates CDKN1A in a DNA-dependent manner, it activates CDKN2A in a DNA-independent manner (PubMed:22206000). May have a regulatory role when quiescent vascular smooth muscle cells reenter the cell cycle. {ECO:0000250|UniProtKB:P32443, ECO:0000269|PubMed:22206000}.; . TISSUE SPECIFICITY: Embryo and placenta.; unclassifiable (Anatomical System);meninges;cartilage;heart;ovary;parathyroid;skin;uterus;pia mater;whole body;lung;mesenchyma;placenta;visual apparatus;duodenum;testis;spleen;dura mater;spinal ganglion;brain;aorta; superior cervical ganglion;placenta;fetal lung;ciliary ganglion; 0.85518 0.14644 -0.0274281 51.65723048 754.05784 5.44457 MEOX2-AS1 . . . MEOX2 antisense RNA 1 (head to head) . . . . . . . . . . . MEP1A 5.76708569342659e-07 0.965504925564474 0.0344944977269568 meprin A subunit alpha . . . unclassifiable (Anatomical System);lung;whole body;islets of Langerhans;liver;colon;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13860 0.14733 1.337468036 94.28520878 3075.87984 10.54032 MEP1AP1 . . . meprin A subunit alpha pseudogene 1 . . . . . . . . . . . MEP1AP2 . . . meprin A subunit alpha pseudogene 2 . . . . . . . . . . . MEP1AP3 . . . meprin A subunit alpha pseudogene 3 . . . . . . . . . . . MEP1AP4 . . . meprin A subunit alpha pseudogene 4 . . . . . . . . . . . MEP1B 6.31312023820361e-21 0.00042541558706191 0.999574584412938 meprin A subunit beta FUNCTION: Membrane metallopeptidase that sheds many membrane-bound proteins. Exhibits a strong preference for acidic amino acids at the P1' position. Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components. {ECO:0000269|PubMed:21693781}.; . TISSUE SPECIFICITY: The major site of expression is the brush border membrane of small intestinal and kidney epithelial cells. {ECO:0000269|PubMed:12387727}.; unclassifiable (Anatomical System);small intestine;thyroid;skeletal muscle; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.16324 0.13511 0.75875178 86.82472281 1007.09424 6.11170 MEPCE 0.996809251755068 0.00319071198813421 3.62567976376877e-08 methylphosphate capping enzyme FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA, leading to stabilize it. {ECO:0000269|PubMed:17643375}.; . TISSUE SPECIFICITY: Expressed in chronic myeloid leukemia cells, adrenal gland, brain, cerebellum, kidney, lung, mammary gland and testis. Weakly or not expressed in other tissues. {ECO:0000269|PubMed:12358911}.; ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;uterus;prostate;whole body;larynx;bone;thyroid;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis;cerebellum; 0.55155 0.10709 -0.890882376 10.30313753 83.03091 1.93616 MEPE 0.362907708690344 0.625107552317813 0.0119847389918431 matrix extracellular phosphoglycoprotein FUNCTION: Promotes renal phosphate excretion and modulates mineralization. {ECO:0000269|PubMed:14962809}.; . TISSUE SPECIFICITY: Expressed by osteoblasts. Secreted from oncogenic hypophosphataemic tumors.; bone; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; 0.23694 0.15614 1.666397606 96.29039868 213.8891 3.15571 MER5 . . . antigen identified by monoclonal antibody 2D8 . . . . . . . . . . . MERTK 9.66187266673099e-08 0.999182497160147 0.000817406221126584 MER proto-oncogene, tyrosine kinase FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis). Ligand binding at the cell surface induces autophosphorylation of MERTK on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with GRB2 or PLCG2 and induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK signaling plays a role in various processes such as macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization and engulfment. Functions in the retinal pigment epithelium (RPE) as a regulator of rod outer segments fragments phagocytosis. Plays also an important role in inhibition of Toll- like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3. {ECO:0000269|PubMed:17005688}.; DISEASE: Retinitis pigmentosa 38 (RP38) [MIM:613862]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:11062461}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Not expressed in normal B- and T-lymphocytes but is expressed in numerous neoplastic B- and T-cell lines. Highly expressed in testis, ovary, prostate, lung, and kidney, with lower expression in spleen, small intestine, colon, and liver.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;thyroid;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;nervous;hypothalamus;urinary;lens;skeletal muscle;lung;trabecular meshwork;placenta;macula lutea;liver;hypopharynx;spleen;head and neck;kidney;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.10218 0.24392 0.874458024 88.88888889 1308.80238 6.80451 MESDC1 0.683511245523063 0.297206987808389 0.0192817666685486 mesoderm development candidate 1 . . . unclassifiable (Anatomical System);smooth muscle;lymph node;cartilage;ovary;muscle;urinary;colon;skin;retina;uterus;whole body;lung;cochlea;bone;placenta;visual apparatus;pituitary gland;testis;germinal center;kidney;brain;mammary gland;aorta;stomach; superior cervical ganglion;cerebellum; 0.18134 0.11112 . . 59.90617 1.57020 MESDC2 0.846200196402005 0.151069811231261 0.00272999236673473 mesoderm development candidate 2 FUNCTION: Chaperone specifically assisting the folding of beta- propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). Acts as a modulator of the Wnt pathway through chaperoning the coreceptors of the canonical Wnt pathway, LRP5 and LRP6, to the plasma membrane. Essential for specification of embryonic polarity and mesoderm induction. {ECO:0000269|PubMed:15014448, ECO:0000269|PubMed:17488095}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;choroid;fovea centralis;uterus;bone;pituitary gland;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach; . 0.14237 0.11718 -0.273576253 33.97027601 60.19333 1.57594 MESP1 0.000120662134814298 0.221067446794415 0.778811891070771 mesoderm posterior bHLH transcription factor 1 FUNCTION: Transcription factor. Plays a role in the epithelialization of somitic mesoderm and in the development of cardiac mesoderm. Defines the rostrocaudal patterning of the somites by participating in distinct Notch pathways (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);prostate;cartilage;islets of Langerhans;hippocampus;pituitary gland;colon;kidney;brain;stomach; amygdala;prostate;skeletal muscle; 0.12317 0.12345 . . 2530.55722 9.38371 MESP2 0.0114095574924346 0.842669745098476 0.145920697409089 mesoderm posterior bHLH transcription factor 2 FUNCTION: Transcription factor with important role in somitogenesis. Defines the rostrocaudal patterning of the somite by participating in distinct Notch pathways. Regulates also the FGF signaling pathway. Specifies the rostral half of the somites. Generates rostro-caudal polarity of somites by down-regulating in the presumptive rostral domain DLL1, a Notch ligand. Participates in the segment border formation by activating in the anterior presomitic mesoderm LFNG, a negative regulator of DLL1-Notch signaling. Acts as a strong suppressor of Notch activity. Together with MESP1 is involved in the epithelialization of somitic mesoderm and in the development of cardiac mesoderm.; DISEASE: Spondylocostal dysostosis 2, autosomal recessive (SCDO2) [MIM:608681]: A condition of variable severity associated with vertebral and rib segmentation defects. The main skeletal malformations include fusion of vertebrae, hemivertebrae, fusion of certain ribs, and other rib malformations. Deformity of the chest and spine (severe scoliosis, kyphoscoliosis and lordosis) is a natural consequence of the malformation and leads to a dwarf- like appearance. As the thorax is small, infants frequently have respiratory insufficiency and repeated respiratory infections resulting in life-threatening complications in the first year of life. {ECO:0000269|PubMed:15122512}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . uterus; . 0.10825 0.14089 . . 732.01673 5.37053 MEST 0.997526693420813 0.00247321033331032 9.6245876892374e-08 mesoderm specific transcript . . TISSUE SPECIFICITY: Highly expressed in hydatidiform moles, but barely expressed in dermoid cysts. Biallelic expression is detected in blood lymphocytes. Seems to imprinted in an isoform- specific manner rather than in a tissue-specific manner in lymphocytes. Isoform 1 is expressed only from the paternal allele. Isoform 2 is expressed from both the paternal allele and the maternal allele. {ECO:0000269|PubMed:8884280, ECO:0000269|PubMed:9192843}.; medulla oblongata;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;cochlea;bladder;brain;amygdala;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;peripheral nerve;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;pia mater;adrenal gland;placenta;hippocampus;head and neck;kidney;aorta;stomach; placenta;fetal lung; 0.50986 0.22263 -0.029247611 51.40363293 30.98883 0.98005 MESTIT1 . . . MEST intronic transcript 1, antisense RNA . . . . . . . . . . . MESTP1 . . . mesoderm specific transcript pseudogene 1 . . . . . . . . . . . MESTP2 . . . mesoderm specific transcript pseudogene 2 . . . . . . . . . . . MESTP3 . . . mesoderm specific transcript pseudogene 3 . . . . . . . . . . . MESTP4 . . . mesoderm specific transcript pseudogene 4 . . . . . . . . . . . MET 0.996412863765497 0.00358713623119108 3.31186204848282e-12 MET proto-oncogene, receptor tyrosine kinase FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Promotes also differentiation and proliferation of hematopoietic cells.; DISEASE: Note=Activation of MET after rearrangement with the TPR gene produces an oncogenic protein.; DISEASE: Note=Defects in MET may be associated with gastric cancer.; DISEASE: Hepatocellular carcinoma (HCC) [MIM:114550]: A primary malignant neoplasm of epithelial liver cells. The major risk factors for HCC are chronic hepatitis B virus (HBV) infection, chronic hepatitis C virus (HCV) infection, prolonged dietary aflatoxin exposure, alcoholic cirrhosis, and cirrhosis due to other causes. {ECO:0000269|PubMed:9927037}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Renal cell carcinoma papillary (RCCP) [MIM:605074]: A subtype of renal cell carcinoma tending to show a tubulo-papillary architecture formed by numerous, irregular, finger-like projections of connective tissue. Renal cell carcinoma is a heterogeneous group of sporadic or hereditary carcinoma derived from cells of the proximal renal tubular epithelium. {ECO:0000269|PubMed:10327054, ECO:0000269|PubMed:10417759, ECO:0000269|PubMed:10433944, ECO:0000269|PubMed:9140397, ECO:0000269|PubMed:9563489}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A common allele in the promoter region of the MET shows genetic association with susceptibility to autism in some families. Functional assays indicate a decrease in MET promoter activity and altered binding of specific transcription factor complexes.; DISEASE: Note=MET activating mutations may be involved in the development of a highly malignant, metastatic syndrome known as cancer of unknown primary origin (CUP) or primary occult malignancy. Systemic neoplastic spread is generally a late event in cancer progression. However, in some instances, distant dissemination arises at a very early stage, so that metastases reach clinical relevance before primary lesions. Sometimes, the primary lesions cannot be identified in spite of the progresses in the diagnosis of malignancies.; TISSUE SPECIFICITY: Expressed in normal hepatocytes as well as in epithelial cells lining the stomach, the small and the large intestine. Found also in basal keratinocytes of esophagus and skin. High levels are found in liver, gastrointestinal tract, thyroid and kidney. Also present in the brain. {ECO:0000269|PubMed:1719465, ECO:0000269|PubMed:1917129}.; smooth muscle;ovary;salivary gland;intestine;colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; dorsal root ganglion;fetal liver;superior cervical ganglion;thyroid;placenta;globus pallidus;appendix;fetal lung;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.75318 0.52967 -0.455627566 23.72611465 467.67031 4.48154 METAP1 0.0435476826328097 0.929380848764676 0.027071468602514 methionyl aminopeptidase 1 FUNCTION: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle. {ECO:0000255|HAMAP- Rule:MF_03174, ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:17114291}.; . . medulla oblongata;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;oesophagus;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;islets of Langerhans;urinary;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.65805 0.15224 -0.141298762 42.87567823 26.96708 0.87096 METAP1D 1.55557888019336e-06 0.404676324182735 0.595322120238384 methionyl aminopeptidase type 1D (mitochondrial) FUNCTION: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed (By similarity). May play a role in colon tumorigenesis. {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16568094}.; . TISSUE SPECIFICITY: Overexpressed in colon cancer cell lines and colon tumors as compared to normal tissues (at protein level). {ECO:0000269|PubMed:16568094}.; unclassifiable (Anatomical System);heart;ovary;salivary gland;colon;skin;uterus;lung;bone;liver;testis;spleen;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; . . -0.093566408 46.7386176 1129.38456 6.41406 METAP2 0.906382727005543 0.093610885917978 6.38707647888518e-06 methionyl aminopeptidase 2 FUNCTION: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N- terminal Met-Val and Met-Thr sequences in vivo.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach; testis - interstitial;testis;globus pallidus;pons; 0.67899 0.16647 -0.80269335 12.23755603 89.69569 2.03685 METRN 0.0818044356695418 0.756314310750114 0.161881253580344 meteorin, glial cell differentiation regulator FUNCTION: Involved in both glial cell differentiation and axonal network formation during neurogenesis. Promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Also induces axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;parathyroid;lens;skin;uterus;pancreas;prostate;optic nerve;whole body;lung;epididymis;placenta;hippocampus;testis;kidney;brain;mammary gland;stomach; whole brain;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;subthalamic nucleus;thyroid;parietal lobe;cingulate cortex; 0.09766 . . . 106.50756 2.23993 METRNL 0.860216826347564 0.137657183728399 0.00212598992403748 meteorin, glial cell differentiation regulator-like FUNCTION: Hormone induced following exercise or cold exposure that promotes energy expenditure. Induced either in the skeletal muscle after exercise or in adipose tissue following cold exposure and is present in the circulation. Able to stimulate energy expenditure associated with the browning of the white fat depots and improves glucose tolerance. Does not promote an increase in a thermogenic gene program via direct action on adipocytes, but acts by stimulating several immune cell subtypes to enter the adipose tissue and activate their prothermogenic actions. Stimulates an eosinophil-dependent increase in IL4 expression and promotes alternative activation of adipose tissue macrophages, which are required for the increased expression of the thermogenic and anti- inflammatory gene programs in fat. Required for some cold-induced thermogenic responses, suggesting a role in metabolic adaptations to cold temperatures (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in the skeletal muscle, in subcutaneous adipose tissue, epididymal white adipose tissue depots and heart. Also expressed in brown adipose tissues and kidney. {ECO:0000269|PubMed:24393292, ECO:0000269|PubMed:24906147}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;lung;placenta;macula lutea;visual apparatus;alveolus;cervix;kidney;mammary gland;stomach; placenta; 0.17503 0.10846 -0.089927255 46.99221515 161.36194 2.77561 METTL1 0.0059156174332639 0.904087526058367 0.0899968565083694 methyltransferase like 1 FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. {ECO:0000255|HAMAP-Rule:MF_03055, ECO:0000269|PubMed:12403464}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10329009}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;aorta; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.20409 0.13876 -0.626318434 17.03231894 9.19072 0.33574 METTL2A 1.7733777443887e-05 0.880024542781861 0.119957723440695 methyltransferase like 2A FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase that mediates 3-methylcytidine modification of some tRNAs. {ECO:0000250}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;synovium;bone;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;hypothalamus;pharynx;blood;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;cervix;head and neck;kidney;mammary gland;stomach;cerebellum; . 0.15531 0.10504 0.194852702 67.03231894 98.29016 2.14356 METTL2B 0.0827090983733214 0.915190408555786 0.0021004930708931 methyltransferase like 2B FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase that mediates 3-methylcytidine modification of some tRNAs. {ECO:0000269|PubMed:21518805}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;synovium;bone;bladder;brain;unclassifiable (Anatomical System);cartilage;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; medulla oblongata;superior cervical ganglion;atrioventricular node; 0.10107 0.09297 -0.135838822 43.77211607 1492.98007 7.18918 METTL3 0.00100496545950933 0.996557338469112 0.00243769607137886 methyltransferase like 3 FUNCTION: N6-methyltransferase that methylates adenosine residues of some RNAs and acts as a regulator of the circadian clock, differentiation of embryonic stem cells and primary miRNA processing. N6-methyladenosine (m6A), which takes place at the 5'- [AG]GAC-3' consensus sites of some mRNAs, plays a role in the efficiency of mRNA splicing, processing, translation efficiency, editing and mRNA stability (PubMed:22575960, PubMed:24284625, PubMed:25719671, PubMed:25799998, PubMed:26321680, PubMed:26593424, PubMed:9409616). M6A regulates the length of the circadian clock: acts as a early pace-setter in the circadian loop by putting mRNA production on a fast-track for facilitating nuclear processing, thereby providing an early point of control in setting the dynamics of the feedback loop (By similarity). M6A also acts as a regulator of mRNA stability: in embryonic stem cells (ESCs), m6A methylation of mRNAs encoding key naive pluripotency-promoting transcripts results in transcript destabilization, promoting differentiation of ESCs (By similarity). M6A also takes place in other RNA molecules, such as primary miRNA (pri-miRNAs) (PubMed:25799998). Mediates methylation of pri-miRNAs, marking them for recognition and processing by DGCR8 (PubMed:25799998). {ECO:0000250|UniProtKB:Q8C3P7, ECO:0000269|PubMed:22575960, ECO:0000269|PubMed:24284625, ECO:0000269|PubMed:25719671, ECO:0000269|PubMed:25799998, ECO:0000269|PubMed:26321680, ECO:0000269|PubMed:26593424, ECO:0000269|PubMed:9409616}.; . TISSUE SPECIFICITY: Widely expressed at low level. Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes. {ECO:0000269|PubMed:9409616}.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;cerebellum cortex;islets of Langerhans;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;cingulate cortex; 0.69158 0.12397 -0.093566408 46.7386176 76.47824 1.83538 METTL4 2.54716995117714e-05 0.920412883905149 0.0795616443953393 methyltransferase like 4 FUNCTION: Probable methyltransferase. {ECO:0000250}.; . . ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;urinary;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;stomach;aorta; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11158 . 0.553050905 81.54635527 1409.08979 7.01263 METTL5 0.00367271509116605 0.844989237918917 0.151338046989917 methyltransferase like 5 FUNCTION: Probable methyltransferase. {ECO:0000250}.; . . smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;spinal cord;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;placenta;hypopharynx;amnion;head and neck;kidney;stomach;aorta; amygdala;superior cervical ganglion;atrioventricular node;skeletal muscle;cingulate cortex; 0.35214 0.11553 -0.073340031 48.11866006 108.7736 2.26417 METTL6 0.000603417643377884 0.721089792555113 0.278306789801509 methyltransferase like 6 FUNCTION: Probable methyltransferase. {ECO:0000250}.; . . . . 0.04760 0.09964 -0.207437529 38.2814343 19.16525 0.66041 METTL7A 0.00551876494694803 0.716033316699912 0.27844791835314 methyltransferase like 7A FUNCTION: Probable methyltransferase. {ECO:0000250}.; . . medulla oblongata;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta;cerebellum; occipital lobe;superior cervical ganglion;cerebellum peduncles;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;thyroid;liver;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion;parietal lobe; 0.09028 0.09677 0.103030231 61.2762444 256.52929 3.44578 METTL7AP1 . . . methyltransferase like 7A pseudogene 1 . . . . . . . . . . . METTL7B 0.522330681005523 0.460950676558789 0.0167186424356876 methyltransferase like 7B FUNCTION: Probable methyltransferase. {ECO:0000250}.; . . . . 0.07897 0.10944 1.106059595 91.985138 288.21431 3.63492 METTL8 1.43717079201752e-09 0.0298724402924714 0.970127558270358 methyltransferase like 8 FUNCTION: Probable methyltransferase. {ECO:0000250}.; . . . . 0.20386 0.07675 . . 238.74156 3.33669 METTL8P1 . . . methyltransferase like 8 pseudogene 1 . . . . . . . . . . . METTL9 0.377292454639358 0.61194592123578 0.010761624124862 methyltransferase like 9 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;urinary;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; amygdala;adrenal gland;kidney;bone marrow; 0.26755 0.11380 -0.141298762 42.87567823 2.36913 0.08046 METTL10 0.371286245054088 0.617458101963761 0.0112556529821508 methyltransferase like 10 FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that methylates elongation factor 1-alpha. {ECO:0000255|HAMAP-Rule:MF_03188}.; . . lung;endometrium;tongue;blood;head and neck;kidney;brain;skin; . 0.06922 0.07026 0.459411326 78.28497287 310.08465 3.74555 METTL11B . . . methyltransferase like 11B FUNCTION: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]- Pro-Lys when the initiator Met is cleaved. Specifically catalyzes monomethylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and Pro in the Pro-Pro-Lys motif. May activate NTMT1 by priming its substrates for trimethylation. {ECO:0000269|PubMed:24090352}.; . . . . 0.60417 . 1.659136225 96.23142251 2358.61723 9.01096 METTL12 0.00946026365697049 0.81466857573382 0.175871160609209 methyltransferase like 12 FUNCTION: Putative methyltransferase. {ECO:0000250}.; . . . . . . 0.705562627 85.52724699 786.73721 5.53973 METTL13 0.00133198019797483 0.997039390241058 0.00162862956096761 methyltransferase like 13 . . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;gum;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;placenta;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum; superior cervical ganglion;temporal lobe;testis;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.24943 0.10191 -0.663133267 15.94715735 3322.76582 11.02115 METTL14 0.847165775043653 0.152829525293165 4.6996631820576e-06 methyltransferase like 14 FUNCTION: N6-methyltransferase that methylates adenosine residues of some mRNAs and acts as a regulator of the circadian clock and differentiation of embryonic stem cells. N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in the efficiency of mRNA splicing, processing and mRNA stability (PubMed:24316715, PubMed:24407421, PubMed:25719671). M6A regulates the length of the circadian clock: acts as a early pace-setter in the circadian loop. M6A also acts as a regulator of mRNA stability: in embryonic stem cells (ESCs), m6A methylation of mRNAs encoding key naive pluripotency-promoting transcripts results in transcript destabilization (By similarity). {ECO:0000250|UniProtKB:Q3UIK4, ECO:0000269|PubMed:24316715, ECO:0000269|PubMed:24407421, ECO:0000269|PubMed:25719671}.; . . . . . . -0.273576253 33.97027601 7.7701 0.28660 METTL15 0.000155430996855608 0.669866682866977 0.329977886136167 methyltransferase like 15 FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase. {ECO:0000250}.; . . unclassifiable (Anatomical System);tongue;urinary;colon;blood;skin;retina;uterus;prostate;lung;frontal lobe;endometrium;trabecular meshwork;thyroid;hippocampus;liver;testis;head and neck;germinal center;kidney;stomach; dorsal root ganglion;superior cervical ganglion;skeletal muscle; 0.09582 . -0.115612493 45.12856806 255.83929 3.43989 METTL15P1 . . . methyltransferase like 15 pseudogene 1 FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase. {ECO:0000250}.; . . . . . . . . . . METTL15P2 . . . methyltransferase like 15 pseudogene 2 . . . . . . . . . . . METTL15P3 . . . methyltransferase like 15 pseudogene 3 . . . . . . . . . . . METTL16 0.997289420410487 0.00271055523603636 2.43534772333339e-08 methyltransferase like 16 FUNCTION: Probable methyltransferase. {ECO:0000250}.; . . lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;muscle;pharynx;blood;lens;skeletal muscle;breast;lung;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.17686 0.09836 -0.069700724 48.54328851 193.2261 3.01341 METTL17 5.78059529660905e-08 0.646694376886109 0.353305565307938 methyltransferase like 17 FUNCTION: May be a component of the mitochondrial small ribosomal subunit. {ECO:0000250}.; . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;oesophagus;larynx;bone;testis;amniotic fluid;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;urinary;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis;trigeminal ganglion; 0.05727 0.07637 0.04598748 57.47817882 465.89657 4.47096 METTL18 0.0289350542238762 0.802682114857846 0.168382830918278 methyltransferase like 18 FUNCTION: Probable histidine methyltransferase. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;hypothalamus;parathyroid;fovea centralis;uterus;whole body;lung;bone;placenta;macula lutea;liver;testis;cervix;spleen;germinal center;kidney;brain;mammary gland;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.12761 0.08273 0.439181676 77.69521113 1940.98335 8.10886 METTL21A 0.0521776538764983 0.861926664263252 0.08589568186025 methyltransferase like 21A FUNCTION: Protein-lysine methyltransferase that selectively trimethylates residues in heat shock protein 70 (HSP70) family members. Contributes to the in vivo trimethylation of Lys residues in HSPA1 and HSPA8. In vitro methylates 'Lys-561' in HSPA1, 'Lys- 564' in HSPA2, 'Lys-585' in HSPA5, 'Lys-563' in HSPA6 and 'Lys- 561' in HSPA8. {ECO:0000269|PubMed:22948820, ECO:0000269|PubMed:23349634, ECO:0000269|PubMed:23921388}.; . . unclassifiable (Anatomical System);lung;ovary;islets of Langerhans;colon;blood;stomach; subthalamic nucleus;trigeminal ganglion; 0.14675 0.10816 0.128714042 63.19886766 231.58015 3.28860 METTL21AP1 . . . methyltransferase like 21A pseudogene 1 . . . . . . . . . . . METTL21B 0.00509293953556655 0.699606424276455 0.295300636187978 methyltransferase like 21B FUNCTION: Protein-lysine methyltransferase. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;islets of Langerhans;muscle;skin;uterus;lung;frontal lobe;endometrium;placenta;bone;visual apparatus;liver;spleen;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13375 . 0.461228372 78.46190139 45.37973 1.29388 METTL21C 3.55322885209736e-06 0.200196982144609 0.799799464626539 methyltransferase like 21C FUNCTION: Protein-lysine methyltransferase. {ECO:0000269|PubMed:22948820}.; . . uterus;lung;ovary;heart;placenta;liver;testis;parathyroid;spleen;brain;skin; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . 0.927856124 89.70276008 110.21268 2.28367 METTL21EP . . . methyltransferase like 21E, pseudogene FUNCTION: Protein-lysine methyltransferase. {ECO:0000250}.; . . . . . . . . . . METTL22 3.9572283065224e-08 0.563917147581318 0.436082812846399 methyltransferase like 22 FUNCTION: Protein N-lysine methyltransferase. In vitro methylates KIN. {ECO:0000269|PubMed:23349634}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;cerebellum; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;pons; . . 0.578735925 82.29535268 1474.64323 7.15214 METTL23 0.113237609183132 0.778025357292159 0.108737033524709 methyltransferase like 23 FUNCTION: Probable methyltransferase. {ECO:0000250}.; DISEASE: Mental retardation, autosomal recessive 44 (MRT44) [MIM:615942]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT44 manifestations include mild to severe cognitive impairment, delayed psychomotor development, seizures in some patients, and dysmorphic features. {ECO:0000269|PubMed:24501276, ECO:0000269|PubMed:24626631}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;uterus;prostate;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;urinary;bile duct;lung;placenta;trabecular meshwork;liver;spleen;cervix;kidney;stomach; . . 0.08223 0.349177632 74.18023119 73.16169 1.78753 METTL24 0.0127144819891321 0.857102317998208 0.13018320001266 methyltransferase like 24 . . . . . 0.19932 . 1.260404852 93.53031375 566.50994 4.83384 METTL25 1.64825272550087e-07 0.848092354519789 0.151907480654939 methyltransferase like 25 FUNCTION: Putative methyltransferase. {ECO:0000250}.; . . . . 0.15629 . 0.312359769 72.71172446 505.29182 4.61249 MEX3A 0.881462711195155 0.117151444852249 0.00138584395259624 mex-3 RNA binding family member A FUNCTION: RNA binding protein, may be involved in post- transcriptional regulatory mechanisms.; . TISSUE SPECIFICITY: Highest levels found in fetal brain and testis. Detected also in thymus, salivary gland and uterus. {ECO:0000269|PubMed:17267406}.; . . . . -0.361761279 28.6329323 17.73394 0.61950 MEX3B 0.201034761193953 0.754683018866433 0.0442822199396136 mex-3 RNA binding family member B FUNCTION: RNA-binding protein. May be involved in post- transcriptional regulatory mechanisms.; . TISSUE SPECIFICITY: Highest levels found in fetal brain and testis. Detected in the adult intestinal epithelium, specifically in goblet cell at protein level. {ECO:0000269|PubMed:17267406}.; unclassifiable (Anatomical System);uterus;lung;whole body;cartilage;heart;endometrium;visual apparatus;testis;brain;skin; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;fetal brain;testis;ciliary ganglion;atrioventricular node;pons; 0.55049 0.11089 -0.756778259 13.44656759 41.15512 1.20418 MEX3C 0.946417957993422 0.0533974527225274 0.000184589284050219 mex-3 RNA binding family member C FUNCTION: E3 ubiquitin ligase responsible for the post- transcriptional regulation of common HLA-A allotypes. Binds to the 3' UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation. {ECO:0000269|PubMed:22863774, ECO:0000269|PubMed:23446422}.; DISEASE: Note=Genetic variations in MEX3C may be associated with susceptibility to essential hypertension. {ECO:0000269|PubMed:17015768}.; TISSUE SPECIFICITY: Highest levels found in fetal brain and testis. Also expressed in thymus, salivary gland and uterus. Highly expressed in cells of the innate immune system, in particular activated NK cells. Week expression in the intestine. {ECO:0000269|PubMed:17267406, ECO:0000269|PubMed:22863774}.; . . 0.63235 0.15588 -0.336073593 30.55555556 326.84728 3.84343 MEX3D . . . mex-3 RNA binding family member D FUNCTION: RNA binding protein, may be involved in post- transcriptional regulatory mechanisms. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed in all the cell lines and tissues tested. {ECO:0000269|PubMed:17267406}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;lens;skin;uterus;prostate;lung;placenta;bone;testis;brain;aorta;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;placenta;ciliary ganglion;trigeminal ganglion;cerebellum; 0.18574 . . . 93.70349 2.08216 MFAP1 0.986958816915287 0.0130411366226566 4.64620565546203e-08 microfibrillar associated protein 1 FUNCTION: Component of the elastin-associated microfibrils.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pineal body;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach; . 0.13624 0.11689 0.104848986 61.49445624 51.38972 1.41459 MFAP1P1 . . . microfibrillar associated protein 1 pseudogene 1 . . . . . . . . . . . MFAP2 0.000124328486872189 0.621321006978178 0.37855466453495 microfibrillar associated protein 2 FUNCTION: Component of the elastin-associated microfibrils.; . . . . 0.90467 0.13595 -0.185391282 39.67916962 51.29213 1.41244 MFAP3 0.00844477902532272 0.795941014464117 0.195614206510561 microfibrillar associated protein 3 FUNCTION: Component of the elastin-associated microfibrils.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;lacrimal gland;islets of Langerhans;adrenal cortex;colon;skin;skeletal muscle;uterus;breast;lung;placenta;testis;amniotic fluid;germinal center;brain;stomach; superior cervical ganglion;atrioventricular node; 0.07195 0.10356 -0.538132194 20.26421326 40.83868 1.19598 MFAP3L 0.910529966045715 0.0887965499641764 0.000673483990108888 microfibrillar associated protein 3 like FUNCTION: May participate in the nuclear signaling of EGFR and MAPK1/ERK2. May a have a role in metastasis. {ECO:0000269|PubMed:24735981}.; . TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|Ref.1}.; unclassifiable (Anatomical System);meninges;heart;ovary;colon;parathyroid;blood;skin;skeletal muscle;retina;bone marrow;uterus;pia mater;lung;frontal lobe;endometrium;placenta;visual apparatus;liver;testis;dura mater;kidney;brain; dorsal root ganglion;amygdala;superior cervical ganglion;medulla oblongata;testis - interstitial;hypothalamus;spinal cord;pons;skeletal muscle;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.54249 0.11146 -0.448125345 24.19202642 47.20222 1.33143 MFAP4 0.559557121872237 0.4377407326369 0.00270214549086373 microfibrillar associated protein 4 FUNCTION: Could be involved in calcium-dependent cell adhesion or intercellular interactions.; . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;heart;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; uterus;uterus corpus;adipose tissue;tongue;placenta;fetal lung;trigeminal ganglion; 0.34017 0.11177 -0.471992905 23.03609342 23.28081 0.77700 MFAP5 0.348683723133855 0.64850742585186 0.00280885101428455 microfibrillar associated protein 5 FUNCTION: May play a role in hematopoiesis. In the cardiovascular system, could regulate growth factors or participate in cell signaling in maintaining large vessel integrity (By similarity). Component of the elastin-associated microfibrils (PubMed:8557636). {ECO:0000250|UniProtKB:Q9QZJ6, ECO:0000269|PubMed:8557636}.; DISEASE: Aortic aneurysm, familial thoracic 9 (AAT9) [MIM:616166]: A disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance. {ECO:0000269|PubMed:25434006}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;pancreas;lung;mesenchyma;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;adipose tissue;smooth muscle;heart;atrioventricular node;skeletal muscle;uterus;uterus corpus;trachea;placenta;ciliary ganglion;trigeminal ganglion; 0.73608 0.10282 -0.339715008 30.06605331 12.81236 0.46676 MFF 0.375813389382855 0.623722443499874 0.000464167117271209 mitochondrial fission factor FUNCTION: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface. May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles. {ECO:0000269|PubMed:18353969, ECO:0000269|PubMed:23530241}.; . TISSUE SPECIFICITY: Highly expressed in heart, kidney, liver, brain, muscle, and stomach. {ECO:0000269|PubMed:18353969}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;bone;pituitary gland;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; amygdala;medulla oblongata;thalamus;occipital lobe;testis - interstitial;superior cervical ganglion;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;parietal lobe;cingulate cortex; 0.21007 0.15644 -0.069700724 48.54328851 4719.66421 13.87150 MFGE8 0.000594281860541287 0.900508873282962 0.0988968448564962 milk fat globule-EGF factor 8 protein FUNCTION: Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization (By similarity). Contributes to phagocytic removal of apoptotic cells in many tissues. Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction. Binds specifically to rotavirus and inhibits its replication. {ECO:0000250, ECO:0000269|PubMed:19204935}.; . TISSUE SPECIFICITY: Mammary epithelial cell surfaces and aortic media. Overexpressed in several carcinomas.; myocardium;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;synovium;bone;thyroid;pituitary gland;testis;amniotic fluid;pineal gland;spinal ganglion;brain;unclassifiable (Anatomical System);trophoblast;cartilage;heart;tongue;epidermis;islets of Langerhans;pineal body;urinary;adrenal cortex;blood;pancreas;lung;epididymis;placenta;visual apparatus;duodenum;liver;head and neck;spleen;kidney;mammary gland;stomach;thymus; adipose tissue;atrioventricular node;trigeminal ganglion; 0.33667 . -0.532670911 20.78320359 1241.25294 6.64984 MFHAS1 2.22820045783843e-05 0.97739547900159 0.0225822389938315 malignant fibrous histiocytoma amplified sequence 1 . . TISSUE SPECIFICITY: Ubiquitously expressed. Overexpressed in malignant fibrous histiocytomas. {ECO:0000269|PubMed:9973190}.; unclassifiable (Anatomical System);colon;blood;fovea centralis;choroid;lens;skeletal muscle;retina;breast;optic nerve;whole body;lung;frontal lobe;endometrium;thyroid;macula lutea;germinal center;brain;tonsil;stomach; dorsal root ganglion;fetal liver;superior cervical ganglion; 0.10540 0.11626 -1.188670131 5.891719745 167.02037 2.82384 MFI2-AS1 . . . MFI2 antisense RNA 1 . . . . . . . . . . . MFN1 0.0190381900124968 0.980927452467839 3.43575196640892e-05 mitofusin 1 FUNCTION: Essential transmembrane GTPase, which mediates mitochondrial fusion. Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission. MFN1 acts independently of the cytoskeleton. Overexpression induces the formation of mitochondrial networks. {ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:12475957, ECO:0000269|PubMed:12759376, ECO:0000269|PubMed:23921378}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed at slightly higher level in kidney and heart. Isoform 2 may be overexpressed in some tumors, such as lung cancers. {ECO:0000269|PubMed:11751411, ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:12759376}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hypopharynx;liver;cervix;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.82846 0.13128 -0.246069119 36.06982779 58.55807 1.55048 MFN2 0.999816094005639 0.000183905959782382 3.45786897475224e-11 mitofusin 2 FUNCTION: Essential transmembrane GTPase, which mediates mitochondrial fusion. Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission. MFN2 acts independently of the cytoskeleton. It therefore plays a central role in mitochondrial metabolism and may be associated with obesity and/or apoptosis processes. Overexpression induces the formation of mitochondrial networks. Plays an important role in the regulation of vascular smooth muscle cell proliferation. Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy). Is required for PARK2 recruitment to dysfunctional mitochondria. Involved in the control of unfolded protein response (UPR) upon ER stress including activation of apoptosis and autophagy during ER stress. Acts as an upstream regulator of EIF2AK3 and suppresses EIF2AK3 activation under basal conditions. {ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:15322553, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23921378}.; DISEASE: Charcot-Marie-Tooth disease 2A2 (CMT2A2) [MIM:609260]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. {ECO:0000269|PubMed:15064763, ECO:0000269|PubMed:15549395, ECO:0000269|PubMed:22206013}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Neuropathy, hereditary motor and sensory, 6A (HMSN6A) [MIM:601152]: An autosomal dominant neurologic disorder characterized by optic atrophy and peripheral sensorimotor neuropathy manifesting as axonal Charcot-Marie-Tooth disease. Charcot-Marie-Tooth disease is a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. It is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies and primary peripheral axonal neuropathies. Peripheral axonal neuropathies are characterized by signs of axonal regeneration in the absence of obvious myelin alterations, and normal or slightly reduced nerve conduction velocities. {ECO:0000269|PubMed:16437557}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous; expressed at low level. Highly expressed in heart and kidney. {ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:12759376}.; myocardium;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; subthalamic nucleus;medulla oblongata;superior cervical ganglion;thalamus;pons;trigeminal ganglion;skeletal muscle; 0.08391 0.09223 -0.773369631 13.10450578 69.79508 1.73324 MFNG 1.32485976962964e-07 0.205529364327886 0.794470503186137 MFNG O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase FUNCTION: Glycosyltransferase involved in the elongation of O- linked ligands to activate Notch signaling. Possesses fucose- specific beta-1,3-N-acetylglucosaminyltransferase activity. {ECO:0000269|PubMed:10935626}.; . . lymphoreticular;smooth muscle;ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;bone;thyroid;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;skeletal muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;spleen;kidney;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;white blood cells;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.42000 0.10546 -0.424258538 25.56027365 75.28747 1.81510 MFRP 5.34353005764772e-08 0.629541941386614 0.370458005178085 membrane frizzled-related protein FUNCTION: May play a role in eye development. {ECO:0000269|PubMed:15976030}.; DISEASE: Nanophthalmos 2 (NNO2) [MIM:609549]: Rare autosomal recessive disorder of eye development characterized by extreme hyperopia and small functional eyes. {ECO:0000269|PubMed:15976030}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Microphthalmia, isolated, 5 (MCOP5) [MIM:611040]: A disorder characterized by posterior microphthalmia, retinitis pigmentosa, foveoschisis and optic disk drusen. Microphthalmia is a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues. Ocular abnormalities like opacities of the cornea and lens, scaring of the retina and choroid, and other abnormalities may also be present. {ECO:0000269|PubMed:17167404}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Specifically expressed in brain. Strongly expressed in medulla oblongata and to a lower extent in hippocampus and corpus callosum. Expressed in keratinocytes. {ECO:0000269|PubMed:11263980, ECO:0000269|PubMed:16442268}.; . . 0.18417 0.09689 -0.527216948 20.8893607 1049.17527 6.22008 MFSD1 1.01997314131748e-09 0.495698444221558 0.504301554758469 major facilitator superfamily domain containing 1 . . . lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;amniotic fluid;germinal center;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;trabecular meshwork;macula lutea;liver;spleen;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;dura mater;spinal ganglion;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;mesenchyma;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; trachea;thyroid;white blood cells;whole blood;bone marrow; 0.10879 0.10900 0.198490371 67.30360934 814.92439 5.60946 MFSD1P1 . . . major facilitator superfamily domain containing 1 pseudogene 1 . . . . . . . . . . . MFSD2A 0.917671219949033 0.0823241915872023 4.58846376465806e-06 major facilitator superfamily domain containing 2A FUNCTION: Sodium-dependent lysophosphatidylcholine (LPC) symporter, which plays an essential role for blood-brain barrier formation and function. Specifically expressed in endothelium of the blood-brain barrier of micro-vessels and transports LPC into the brain. Transport of LPC is essential because it constitutes the major mechanism by which docosahexaenoic acid (DHA), an omega- 3 fatty acid that is essential for normal brain growth and cognitive function, enters the brain. Transports LPC carrying long-chain fatty acids such LPC oleate and LPC palmitate with a minimum acyl chain length of 14 carbons. Does not transport docosahexaenoic acid in unesterified fatty acid. Specifically required for blood-brain barrier formation and function, probably by mediating lipid transport. Not required for central nervous system vascular morphogenesis (By similarity). Acts as a transporter for tunicamycin, an inhibitor of asparagine-linked glycosylation. In placenta, acts as a receptor for ERVFRD- 1/syncytin-2 and is required for trophoblast fusion (PubMed:18988732). {ECO:0000250|UniProtKB:Q9DA75, ECO:0000269|PubMed:18988732, ECO:0000269|PubMed:21677192, ECO:0000269|PubMed:23177091, ECO:0000269|PubMed:26005868}.; DISEASE: Microcephaly 15, primary, autosomal recessive (MCPH15) [MIM:616486]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. {ECO:0000269|PubMed:26005865, ECO:0000269|PubMed:26005868}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In placenta, associated with trophoblast cells. {ECO:0000269|PubMed:18988732}.; . . 0.08021 0.09539 -0.492218069 22.35786742 78.73994 1.87316 MFSD2B 1.76078145058686e-07 0.413485772382411 0.586514051539444 major facilitator superfamily domain containing 2B . . . unclassifiable (Anatomical System);blood; . . . 0.444637294 77.91342298 557.71715 4.79749 MFSD3 2.01615229921387e-08 0.0380307831460187 0.961969196692458 major facilitator superfamily domain containing 3 . . . unclassifiable (Anatomical System);myocardium;lymph node;ovary;parathyroid;skin;bone marrow;pancreas;prostate;optic nerve;lung;endometrium;bone;placenta;iris;pituitary gland;testis;cervix;kidney;brain;stomach; . 0.12023 0.10537 . . 160.73646 2.76888 MFSD4A . . . major facilitator superfamily domain containing 4A . . . . . 0.20172 . 0.573279816 82.08303845 . . MFSD4B . . . major facilitator superfamily domain containing 4B FUNCTION: May function as a sodium-dependent glucose transporter. {ECO:0000250}.; . . . . 0.04180 0.11038 0.132352165 63.48785091 . . MFSD4BP1 . . . major facilitator superfamily domain containing 4B pseudogene 1 . . . . . . . . . . . MFSD5 0.102466254658811 0.864685251225847 0.0328484941153423 major facilitator superfamily domain containing 5 FUNCTION: Mediates high-affinity intracellular uptake of the rare oligo-element molybdenum. {ECO:0000269|PubMed:21464289}.; . TISSUE SPECIFICITY: Expressed ubiquitously but at relatively higher levels in the olfactory bulb and the skeletal muscle. {ECO:0000269|PubMed:21044875}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve;thymus; superior cervical ganglion;trigeminal ganglion; 0.20191 0.10930 -0.780646273 12.77423921 32.59428 1.01413 MFSD6 0.00184669369540055 0.974611906751371 0.0235413995532287 major facilitator superfamily domain containing 6 . . TISSUE SPECIFICITY: Widely expressed. Expression levels in peripheral blood mononuclear cells are highly variable between individuals, including no expression at all. {ECO:0000269|PubMed:20123006}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach; trigeminal ganglion; . 0.10258 0.512596355 80.29606039 2734.07758 9.85114 MFSD6L 2.39664500541186e-08 0.148713474898371 0.851286501135179 major facilitator superfamily domain containing 6-like . . . unclassifiable (Anatomical System);medulla oblongata;pancreas;lung;testis; . . . 2.649589997 98.83227176 4643.95961 13.71201 MFSD7 2.75660020784589e-12 0.0199442224339674 0.980055777563276 major facilitator superfamily domain containing 7 . . . ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;bone;iris;testis;brain;unclassifiable (Anatomical System);cartilage;epidermis;spinal cord;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;kidney;mammary gland; superior cervical ganglion;trigeminal ganglion;cingulate cortex; 0.04674 . -0.843147538 11.2762444 101.24781 2.17789 MFSD8 4.66812963476778e-06 0.958856052720704 0.0411392791496613 major facilitator superfamily domain containing 8 FUNCTION: May be a carrier that transport small solutes by using chemiosmotic ion gradients. {ECO:0000305}.; DISEASE: Macular dystrophy with central cone involvement (CCMD) [MIM:616170]: An ocular disease characterized by decreased visual acuity, slight pigmentary changes and color vision abnormalities, becoming apparent in the third to sixth decade of life. Fundus anomalies are variable and include bull's eye maculopathy, severe atrophy of central fovea, relatively spared fovea with surrounding atrophic ring, central retinal pigment epithelium and/or choroid changes, pale or atrophic peripapillary area, pale optic disk, relatively spared periphery, and slightly or moderately attenuated vessels. {ECO:0000269|PubMed:25227500}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at very low levels in all tissues tested. {ECO:0000269|PubMed:17564970}.; myocardium;ovary;salivary gland;colon;fovea centralis;skin;uterus;prostate;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;stomach; ciliary ganglion;atrioventricular node; 0.09416 0.11832 0.242582624 69.45623968 736.42663 5.38661 MFSD9 7.72060377762361e-06 0.501855497749383 0.498136781646839 major facilitator superfamily domain containing 9 . . . unclassifiable (Anatomical System);ovary;colon;blood;fovea centralis;choroid;lens;retina;bone marrow;pancreas;optic nerve;lung;macula lutea;liver;spleen;germinal center;brain;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10254 . 0.380318343 75.63104506 710.21598 5.29472 MFSD10 3.01777310462786e-07 0.314312594230622 0.685687103992067 major facilitator superfamily domain containing 10 FUNCTION: Confers cellular resistance to apoptosis induced by the non-steroidal anti-inflammatory drugs indomethacin and diclofenac. May act as an efflux pump. {ECO:0000269|PubMed:17362938}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; prostate;lung;fetal brain;thyroid;white blood cells;bone marrow; 0.12831 0.10983 -1.153638777 6.233781552 150.12015 2.67249 MFSD11 0.0045322819249491 0.988750232076835 0.00671748599821638 major facilitator superfamily domain containing 11 . . . lymphoreticular;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;stomach;thymus; . 0.04387 . -0.648365105 16.35999056 47.0924 1.32781 MFSD12 1.07410212559189e-09 0.168952160617341 0.831047838308557 major facilitator superfamily domain containing 12 . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;duodenum;cervix;kidney;mammary gland; superior cervical ganglion;testis - seminiferous tubule;atrioventricular node;skeletal muscle; 0.14519 . -0.257204135 34.97876858 1194.23215 6.55740 MFSD13A . . . major facilitator superfamily domain containing 13A . . . . . 0.21960 . -1.375949569 4.393724935 . . MFSD13B . . . major facilitator superfamily domain containing 13B . . . . . . . . . . . MFSD14A . . . major facilitator superfamily domain containing 14A . . . . . 0.62140 0.10989 -0.205617011 38.57631517 . . MFSD14B . . . major facilitator superfamily domain containing 14B . . . . . 0.48594 0.11455 -0.314027422 31.9297004 . . MFSD14C . . . major facilitator superfamily domain containing 14C . . . . . 0.21594 . . . . . MGA 0.999999999646878 3.53121545104251e-10 3.40513274862468e-27 MGA, MAX dimerization protein FUNCTION: Functions as a dual-specificity transcription factor, regulating the expression of both MAX-network and T-box family target genes. Functions as a repressor or an activator. Binds to 5'-AATTTCACACCTAGGTGTGAAATT-3' core sequence and seems to regulate MYC-MAX target genes. Suppresses transcriptional activation by MYC and inhibits MYC-dependent cell transformation. Function activated by heterodimerization with MAX. This heterodimerization serves the dual function of both generating an E-box-binding heterodimer and simultaneously blocking interaction of a corepressor (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;colon;bone marrow;uterus;breast;lung;bone;liver;testis;spleen;cervix;kidney;brain;stomach; superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;skeletal muscle; 0.96192 . -0.613924518 17.48053786 3694.31204 11.84454 MGAM 1.5473423744435e-23 0.818824940819818 0.181175059180182 maltase-glucoamylase FUNCTION: May serve as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition. May play a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing.; . TISSUE SPECIFICITY: Expressed in small intestine, granulocyte, and kidney but not in salivary gland or pancreas.; . . 0.40996 0.57507 2.364972666 98.44892663 6504.31939 16.91441 MGAM2 . . . maltase-glucoamylase 2 (putative) . . . . . . . . . . . MGARP 0.0238241579491463 0.773068662323572 0.203107179727282 mitochondria localized glutamic acid rich protein FUNCTION: Plays a role in the trafficking of mitochondria along microtubules. Regulates the kinesin-mediated axonal transport of mitochondria to nerve terminals along microtubules during hypoxia. Participates in the translocation of TRAK2/GRIF1 from the cytoplasm to the mitochondrion. Also plays a role in steroidogenesis through maintenance of mitochondrial abundance and morphology (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the brain, adrenal gland and corneal endothelium (CE). Expressed in steroid-producing cells of the ovary and testis (at protein level). Expressed in steroid- producing cells of the ovary and testis. Weakly expressed in placenta. Expressed in corneal endothelial cells. {ECO:0000269|PubMed:12036975, ECO:0000269|PubMed:12770732, ECO:0000269|PubMed:16565373, ECO:0000269|PubMed:19325000, ECO:0000269|PubMed:19528298}.; . . . 0.08313 0.705562627 85.52724699 351.5806 3.97452 MGAT1 0.690362903375764 0.305523576894261 0.00411351972997538 mannosyl (alpha-1,3-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase FUNCTION: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.; . TISSUE SPECIFICITY: Appears to be present in all tissues.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;aorta;thymus;cerebellum; placenta; 0.25119 0.13626 0.198490371 67.30360934 75.58464 1.82016 MGAT2 0.955031701312776 0.0448491735208821 0.00011912516634148 mannosyl (alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase FUNCTION: Catalyzes an essential step in the conversion of oligo- mannose to complex N-glycans.; DISEASE: Congenital disorder of glycosylation 2A (CDG2A) [MIM:212066]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:11228641, ECO:0000269|PubMed:8808595}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;blood;skeletal muscle;bile duct;breast;lung;placenta;macula lutea;liver;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;testis;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.17885 . 0.084621747 60.31493277 48.86632 1.36383 MGAT2P1 . . . MGAT2 pseudogene 1 . . . . . . . . . . . MGAT2P2 . . . MGAT2 pseudogene 2 . . . . . . . . . . . MGAT3 0.460179519269915 0.534013724225994 0.00580675650409192 mannosyl (beta-1,4-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase FUNCTION: It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides.; . . unclassifiable (Anatomical System);lymph node;ovary;parathyroid;blood;skin;skeletal muscle;bone marrow;breast;uterus;prostate;lung;nasopharynx;placenta;visual apparatus;liver;testis;cervix;spleen;kidney;brain;stomach; whole brain;dorsal root ganglion;amygdala;thalamus;superior cervical ganglion;cerebellum peduncles;temporal lobe;ciliary ganglion;pons;caudate nucleus;trigeminal ganglion;cingulate cortex;cerebellum; 0.19915 0.20010 -0.578583623 18.71903751 37.62301 1.12002 MGAT3-AS1 . . . MGAT3 antisense RNA 1 . . . . . . . . . . . MGAT4A 0.0598161748111026 0.940037636876036 0.000146188312860848 mannosyl (alpha-1,3-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isozyme A FUNCTION: Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N- linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains. Involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression of SLC2A2 in pancreatic beta cells.; . TISSUE SPECIFICITY: Expressed in pancreas, spleen, thymus, prostate, small intestine, peripheral blood leukocytes and lymph node. Strongly overexpressed in choriocarcinoma cancer cell lines. Down-regulated in pancreatic cancer. {ECO:0000269|PubMed:10024668}.; unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;colon;skeletal muscle;uterus;prostate;lung;placenta;testis;germinal center;kidney;brain;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;pons; 0.34187 0.12087 0.040529541 57.15380986 148.07025 2.65159 MGAT4B 0.813383750750224 0.186608145515221 8.10373455434228e-06 mannosyl (alpha-1,3-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isozyme B FUNCTION: Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N- linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains. Has lower affinities for donors or acceptors than MGAT4A, suggesting that, under physiological conditions, it is not the main contributor in N- glycan biosynthesis.; . TISSUE SPECIFICITY: Widely expressed. Strongly overexpressed in pancreatic cancer. {ECO:0000269|PubMed:10372966}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; superior cervical ganglion;liver; 0.12375 0.10711 0.069852974 59.10592121 221.21859 3.21722 MGAT4C 0.0111690534801191 0.948246208284896 0.0405847382349845 MGAT4 family member C FUNCTION: Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N- linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains (By similarity). Does not catalyze the transfer of GlcNAc to the Manalpha1-6 arm to form GlcNAcBeta1-4Manalpha1-6 linkage ('GnT-VI' activity). {ECO:0000250, ECO:0000269|PubMed:10962001}.; . TISSUE SPECIFICITY: Expressed in heart, adrenal gland, testis, liver, brain and fetal brain. Not expressed in pancreas. {ECO:0000269|PubMed:10570912}.; unclassifiable (Anatomical System);frontal lobe;hypothalamus;thyroid; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.38230 0.37294 -0.203796826 38.81811748 199.35087 3.05135 MGAT4D . . . MGAT4 family member D . . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:16773575}.; . . . . . . . . MGAT4EP . . . MGAT4 family member E, pseudogene . . . . . . . . . . . MGAT5 0.999925016569622 7.49834264906442e-05 3.88747248575933e-12 mannosyl (alpha-1,6-)-glycoprotein beta-1,6-N-acetyl-glucosaminyltransferase FUNCTION: Catalyzes the addition of N-acetylglucosamine in beta 1- 6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides.; . . frontal lobe;placenta;colon;blood;stomach;bone marrow; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.10094 0.58469 -1.265702118 5.237084218 49.71155 1.38242 MGAT5B 0.126104149453102 0.873853913207111 4.1937339787356e-05 mannosyl (alpha-1,6-)-glycoprotein beta-1,6-N-acetyl-glucosaminyltransferase, isozyme B FUNCTION: Glycosyltransferase that acts on alpha-linked mannose of N-glycans and O-mannosyl glycans. Catalyzes the transfer of N- acetylglucosamine (GlcNAc) to the beta 1-6 linkage of the mannose residue of GlcNAcbeta1,2-Manalpha on both the alpha1,3- and alpha1,6-linked mannose arms in the core structure of N-glycan. Also acts on the GlcNAcbeta1,2-Manalpha1-Ser/Thr moiety, forming a 2,6-branched structure in brain O-mannosyl glycan. Plays an active role in modulating integrin and laminin-dependent adhesion and migration of neuronal cells via its activity in the O-mannosyl glycan pathway. {ECO:0000269|PubMed:12941944, ECO:0000269|PubMed:14617637, ECO:0000269|PubMed:14623122, ECO:0000269|PubMed:16606368, ECO:0000269|PubMed:16857188}.; . TISSUE SPECIFICITY: Predominantly expressed in brain. Expressed in all area of the adult and fetal brain Also expressed at much lower level in testis, spleen and thymus. {ECO:0000269|PubMed:12941944, ECO:0000269|PubMed:14623122}.; unclassifiable (Anatomical System);pancreas;lung;frontal lobe;macula lutea;liver;cervix;spleen;fovea centralis;brain; superior cervical ganglion;subthalamic nucleus;temporal lobe;globus pallidus;trigeminal ganglion;cingulate cortex; 0.25697 0.13883 -0.925889687 9.754659118 2349.60092 8.98100 MGEA5 0.71410354161128 0.285895327699705 1.13068901479863e-06 meningioma expressed antigen 5 (hyaluronidase) FUNCTION: Isoform 1: Cleaves GlcNAc but not GalNAc from O- glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4- methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl- beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:11148210). Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714). {ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:20673219, ECO:0000269|PubMed:22365600, ECO:0000269|PubMed:24088714}.; . TISSUE SPECIFICITY: Ubiquitous. Shows highest expression in the brain, placenta and pancreas. {ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11341771}.; myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;cornea;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;thymus;cerebellum; amygdala;dorsal root ganglion;superior cervical ganglion;testis - interstitial;occipital lobe;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.66670 0.20993 -0.402212257 26.7338995 83.89905 1.95040 MGLL 0.00459891048076127 0.87582786102513 0.119573228494109 monoglyceride lipase FUNCTION: Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain (By similarity). Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth (PubMed:20079333). {ECO:0000250|UniProtKB:O35678, ECO:0000269|PubMed:20079333}.; . TISSUE SPECIFICITY: Detected in adipose tissue, lung, liver, kidney, brain and heart. {ECO:0000269|PubMed:11470505}.; lymphoreticular;colon;vein;skin;uterus;prostate;frontal lobe;bone;testis;germinal center;brain;artery;pineal gland;unclassifiable (Anatomical System);amygdala;heart;cartilage;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;kidney;stomach;aorta;thymus; whole brain;occipital lobe;subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;prefrontal cortex;liver;globus pallidus;pons;cingulate cortex;parietal lobe;cerebellum; 0.09761 0.21358 -0.249709319 35.74545883 54.1178 1.46688 MGME1 0.0036143276897704 0.95424815990784 0.0421375124023891 mitochondrial genome maintenance exonuclease 1 FUNCTION: Metal-dependent single-stranded DNA (ssDNA) exonuclease involved in mitochondrial genome maintenance. Has preference for 5'-3' exonuclease activity but is also capable of endoduclease activity on linear substrates. Necessary for maintenance of proper 7S DNA levels. Probably involved in mitochondrial DNA (mtDNA) repair, possibly via the processing of displaced DNA containing Okazaki fragments during RNA-primed DNA synthesis on the lagging strand or via processing of DNA flaps during long-patch base excision repair. Specifically binds 5-hydroxymethylcytosine (5hmC)-containing DNA in stem cells. {ECO:0000255|HAMAP- Rule:MF_03030, ECO:0000269|PubMed:23313956, ECO:0000269|PubMed:23358826}.; DISEASE: Mitochondrial DNA depletion syndrome 11 (MTDPS11) [MIM:615084]: An autosomal recessive mitochondrial disorder characterized by onset in childhood or adulthood of progressive external ophthalmoplegia, muscle weakness and atrophy, exercise intolerance, and respiratory insufficiency due to muscle weakness. More variable features include spinal deformity, emaciation, and cardiac abnormalities. Skeletal muscle biopsies show deletion and depletion of mitochondrial DNA (mtDNA) with variable defects in respiratory chain enzyme activities. {ECO:0000269|PubMed:23313956}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . . . 0.30247 0.09838 0.68351529 85.03774475 246.46564 3.38774 MGMT 9.20505516948058e-09 0.0460062313171542 0.953993759477791 O-6-methylguanine-DNA methyltransferase FUNCTION: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.; . . medulla oblongata;ovary;colon;skin;uterus;prostate;endometrium;bone;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;lymph node;heart;islets of Langerhans;lens;skeletal muscle;pancreas;pia mater;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;testis - seminiferous tubule;liver;kidney;trigeminal ganglion; 0.05151 0.55289 0.617373774 83.25076669 1043.67715 6.20059 MGP 0.00672833394383241 0.754952375204292 0.238319290851875 matrix Gla protein FUNCTION: Associates with the organic matrix of bone and cartilage. Thought to act as an inhibitor of bone formation.; DISEASE: Keutel syndrome (KTLS) [MIM:245150]: An autosomal recessive disorder characterized by abnormal cartilage calcification, peripheral pulmonary stenosis neural hearing loss and midfacial hypoplasia. {ECO:0000269|PubMed:9916809}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;medulla oblongata;ovary;skin;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;bladder;brain;tonsil;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;pancreas;lung;pia mater;cornea;adrenal gland;placenta;hippocampus;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;adipose tissue;heart;ovary;salivary gland;adrenal cortex;atrioventricular node;fetal thyroid;uterus;uterus corpus;trachea;adrenal gland;testis;appendix;ciliary ganglion;trigeminal ganglion; 0.15737 . 0.769889969 86.95447039 1109.41047 6.36667 MGRN1 0.450177891211047 0.549768815966675 5.32928222780923e-05 mahogunin ring finger 1, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase. Mediates monoubiquitination at multiple sites of TSG101 in the presence of UBE2D1, but not of UBE2G1, nor UBE2H. Plays a role in the regulation of endosome-to- lysosome trafficking. Impairs MC1R- and MC4R-signaling by competing with GNAS-binding to MCRs and inhibiting agonist-induced cAMP production. Does not inhibit ADRB2-signaling. Does not promote MC1R ubiquitination. {ECO:0000269|PubMed:17229889, ECO:0000269|PubMed:19703557, ECO:0000269|PubMed:19737927}.; . . ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; medulla oblongata;prefrontal cortex;caudate nucleus;pons;cingulate cortex;skeletal muscle;parietal lobe; 0.49083 0.14252 -1.771059651 2.300070771 320.50189 3.80327 MGST1 0.0140289444910937 0.674416119534267 0.31155493597464 microsomal glutathione S-transferase 1 FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a wide substrate specificity.; . TISSUE SPECIFICITY: Highly expressed in liver.; lymphoreticular;umbilical cord;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;hypothalamus;pharynx;blood;breast;bile duct;pancreas;lung;cornea;adrenal gland;epididymis;placenta;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; adipose tissue;adrenal gland;liver;adrenal cortex; 0.12370 0.22917 -0.229483771 36.86010852 21.00485 0.71086 MGST2 0.0551505663366712 0.864863167806323 0.0799862658570059 microsomal glutathione S-transferase 2 FUNCTION: Can catalyze the production of LTC4 from LTA4 and reduced glutathione. Can catalyze the conjugation of 1-chloro-2,4- dinitrobenzene with reduced glutathione.; . TISSUE SPECIFICITY: Liver, spleen, skeletal muscle, heart, adrenals, pancreas, prostate, testis, fetal liver, and fetal spleen. Very low expression in lung, brain, placenta and bone marrow.; ovary;umbilical cord;colon;parathyroid;skin;uterus;prostate;whole body;bone;thyroid;testis;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;stomach;aorta; . 0.16194 0.15089 0.43736446 77.56546355 88.97039 2.02480 MGST3 0.00715304129824559 0.921141286826006 0.0717056718757481 microsomal glutathione S-transferase 3 FUNCTION: Also functions as a glutathione peroxidase.; . TISSUE SPECIFICITY: Predominantly expressed in heart, skeletal muscle, and adrenal cortex. Also found in brain, placenta, liver, kidney, pancreas, thyroid, testis and ovary. Almost absent in lung, thymus and peripheral blood leukocytes.; . . 0.07625 0.16151 -0.09720619 46.20193442 101.29268 2.17863 MHAC . . . microhydranencephaly . . . . . . . . . . . MHRT . . . myosin heavy chain-associated RNA transcript . . . . . . . . . . . MHS2 . . . malignant hyperthermia susceptibility 2 . . . . . . . . . . . MHS4 . . . malignant hyperthermia susceptibility 4 . . . . . . . . . . . MHS6 . . . malignant hyperthermia susceptibility 6 . . . . . . . . . . . MIA 0.00695373031106117 0.918827362869632 0.0742189068193069 melanoma inhibitory activity FUNCTION: Elicits growth inhibition on melanoma cells in vitro as well as some other neuroectodermal tumors, including gliomas.; . TISSUE SPECIFICITY: All malignant melanoma cell lines tested and infrequently in glioma cell lines.; ovary;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;optic nerve;frontal lobe;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;epididymis;placenta;visual apparatus;macula lutea;liver;spleen;kidney;mammary gland;stomach;thymus; amygdala;dorsal root ganglion;whole brain;occipital lobe;medulla oblongata;olfactory bulb;hypothalamus;temporal lobe;spinal cord;white blood cells;atrioventricular node;placenta;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.09732 0.08632 0.169169615 65.33380514 27.29132 0.87938 MIA-RAB4B . . . MIA-RAB4B readthrough (NMD candidate) . . . . . . . . . . . MIA2 0.000208820494041296 0.908098694110289 0.09169248539567 melanoma inhibitory activity 2 FUNCTION: May play a role in the pathophysiology of liver disease and may serve as a marker of liver damage.; . TISSUE SPECIFICITY: Highly expressed in liver and weakly in testis. Expression was higher in patients with severe fibrosis or inflammation and chronic hepatitis.; liver;kidney; medulla oblongata;superior cervical ganglion;temporal lobe;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.18559 0.10293 1.133561642 92.28591649 1216.13549 6.59678 MIA3 0.47138810555393 0.528611893816441 6.29629454818653e-10 melanoma inhibitory activity family member 3 FUNCTION: Required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers. May participate in cargo loading of COL7A1 at endoplasmic reticulum exit sites by binding to COPII coat subunits Sec23/24 and guiding SH3-bound COL7A1 into a growing carrier. Does not play a role in global protein secretion and is apparently specific to COL7A1 cargo loading. However, it may participate in secretion of other proteins in cells that do not secrete COL7A1. {ECO:0000269|PubMed:19269366}.; . TISSUE SPECIFICITY: Broadly expressed, except in bone marrow and peripheral blood mononuclear cells. Down-regulated in melanoma tissue. {ECO:0000269|PubMed:15183315, ECO:0000269|PubMed:17044017}.; ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;thyroid;bone;pituitary gland;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;oral cavity;spinal cord;urinary;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;spleen;kidney;mammary gland;stomach; dorsal root ganglion;medulla oblongata;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;pons;cingulate cortex; 0.06611 0.08834 0.793580678 87.34371314 1337.25355 6.86774 MIAT . . . myocardial infarction associated transcript (non-protein coding) . . . . . . . . . . . MIATNB . . . MIAT neighbor (non-protein coding) . . . . . . . . . . . MIB1 1.00071804997675e-44 1.39960124771605e-09 0.999999998600399 mindbomb E3 ubiquitin protein ligase 1 FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors. Probably mediates ubiquitination and subsequent proteasomal degradation of DAPK1, thereby antagonizing anti-apoptotic effects of DAPK1 to promote TNF- induced apoptosis (By similarity). Involved in ubiquitination of centriolar satellite CEP131, CEP290 and PCM1 proteins and hence inhibits primary cilium formation in proliferating cells. Mediates 'Lys-63'-linked polyubiquitination of TBK1, which probably participates in kinase activation. {ECO:0000250, ECO:0000269|PubMed:24121310}.; DISEASE: Left ventricular non-compaction 7 (LVNC7) [MIM:615092]: A disease due to an arrest of myocardial morphogenesis. It is characterized by a hypertrophic left ventricle with deep trabeculations and with poor systolic function, with or without associated left ventricular dilation. In some cases, it is associated with other congenital heart anomalies. {ECO:0000269|PubMed:23314057}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed at low level. Expressed at higher level in spinal cord, ovary, whole brain, and all specific brain regions examined. {ECO:0000269|PubMed:10718198}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;muscle;skeletal muscle;bile duct;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;skin; 0.49684 0.29035 -1.42004951 4.104741684 51.07097 1.40814 MIB2 0.000158543294053226 0.99842018462645 0.00142127207949637 mindbomb E3 ubiquitin protein ligase 2 FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, and to a lesser extent in heart, brain and kidney. {ECO:0000269|PubMed:14507647}.; unclassifiable (Anatomical System);islets of Langerhans;colon;parathyroid;skin;uterus;breast;pancreas;prostate;lung;endometrium;bone;thyroid;visual apparatus;hippocampus;testis;spleen;cervix;kidney;brain;stomach; . 0.17639 0.12919 -0.033100763 50.56027365 2011.5952 8.25644 MIC7 . . . antigen identified by monoclonal antibody 28.3.7 . . . . . . . . . . . MIC12 . . . antigen identified by monoclonal antibody 30.2A8 . . . . . . . . . . . MICA 0.000378019716342188 0.621049072527639 0.378572907756019 MHC class I polypeptide-related sequence A FUNCTION: Seems to have no role in antigen presentation. Acts as a stress-induced self-antigen that is recognized by gamma delta T- cells. Ligand for the KLRK1/NKG2D receptor. Binding to KLRK1 leads to cell lysis. {ECO:0000269|PubMed:10426993, ECO:0000269|PubMed:11224526, ECO:0000269|PubMed:11491531, ECO:0000269|PubMed:11777960, ECO:0000269|PubMed:9497295}.; DISEASE: Note=Anti-MICA antibodies and ligand shedding are involved in the progression of monoclonal gammopathy of undetermined significance (MGUS)to multiple myeloma.; DISEASE: Psoriasis 1 (PSORS1) [MIM:177900]: A common, chronic inflammatory disease of the skin with multifactorial etiology. It is characterized by red, scaly plaques usually found on the scalp, elbows and knees. These lesions are caused by abnormal keratinocyte proliferation and infiltration of inflammatory cells into the dermis and epidermis. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Psoriatic arthritis (PSORAS) [MIM:607507]: An inflammatory, seronegative arthritis associated with psoriasis. It is a heterogeneous disorder ranging from a mild, non-destructive disease to a severe, progressive, erosive arthropathy. Five types of psoriatic arthritis have been defined: asymmetrical oligoarthritis characterized by primary involvement of the small joints of the fingers or toes; asymmetrical arthritis which involves the joints of the extremities; symmetrical polyarthritis characterized by a rheumatoid like pattern that can involve hands, wrists, ankles, and feet; arthritis mutilans, which is a rare but deforming and destructive condition; arthritis of the sacroiliac joints and spine (psoriatic spondylitis). {ECO:0000269|PubMed:10323458}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed with the exception of the central nervous system where it is absent. Expressed predominantly in gastric epithelium and also in monocytes, keratinocytes, endothelial cells, fibroblasts and in the outer layer of Hassal's corpuscles within the medulla of normal thymus. In skin, expressed mainly in the keratin layers, basal cells, ducts and follicles. Also expressed in many, but not all, epithelial tumors of lung, breast, kidney, ovary, prostate and colon. In thyomas, overexpressed in cortical and medullar epithelial cells. Tumors expressing MICA display increased levels of gamma delta T-cells. {ECO:0000269|PubMed:10359807, ECO:0000269|PubMed:10363723, ECO:0000269|PubMed:10691930, ECO:0000269|PubMed:12902493, ECO:0000269|PubMed:17565371, ECO:0000269|PubMed:8901601, ECO:0000269|PubMed:9396860}.; . . 0.09530 . 3.705115949 99.56357632 7608.07917 18.71369 MICAL1 2.54826851751808e-12 0.991538625545858 0.00846137445159358 microtubule associated monooxygenase, calponin and LIM domain containing 1 FUNCTION: Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin. Acts by modifying actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization (Probable). Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. Also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L; acts by antagonizing STK38 and STK38L activation by MST1/STK4. {ECO:0000269|PubMed:18305261, ECO:0000269|PubMed:21864500, ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in the thymus, lung, spleen, kidney, testis and hematopoietic cells. {ECO:0000269|PubMed:11827972}.; lymphoreticular;myocardium;medulla oblongata;smooth muscle;ovary;sympathetic chain;developmental;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;bile duct;pancreas;lung;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;peripheral nerve; white blood cells;trigeminal ganglion; 0.07106 0.10182 -0.782729853 12.63859401 2032.7154 8.29826 MICAL2 0.132223746243123 0.867775934645877 3.19111000286756e-07 microtubule associated monooxygenase, calponin and LIM domain containing 2 FUNCTION: Nuclear monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin and regulates the SRF signaling. Acts by modifying nuclear actin subunits through the addition of oxygen to form methionine- sulfoxide, leading to promote actin filament severing and prevent repolymerization. Acts as a key regulator of the SRF signaling pathway elicited by nerve growth factor and serum: mediates oxidation and subsequent depolymerization of nuclear actin, leading to increase MKL1/MRTF-A presence in the nucleus and promote SRF:MKL1/MRTF-A-dependent gene transcription. Does not activate SRF:MKL1/MRTF-A through RhoA. {ECO:0000269|PubMed:23927065, ECO:0000269|PubMed:24440334}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;oesophagus;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;blood;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; whole brain;subthalamic nucleus;occipital lobe;medulla oblongata;cerebellum peduncles;temporal lobe;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.35711 0.10318 0.549230812 81.22788393 597.9475 4.94889 MICAL3 0.999997947705208 2.05229479232798e-06 5.02763556714005e-18 microtubule associated monooxygenase, calponin and LIM domain containing 3 FUNCTION: Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin. Acts by modifying actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization. Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process. {ECO:0000269|PubMed:21596566, ECO:0000269|PubMed:24440334}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15694364}.; unclassifiable (Anatomical System);breast;whole body;frontal lobe;hypopharynx;colon;amniotic fluid;blood;head and neck;brain;skin;bone marrow; superior cervical ganglion;fetal brain;cerebellum peduncles;prefrontal cortex;globus pallidus;cerebellum; 0.16348 0.11890 0.409523754 76.51568766 1942.66989 8.11317 MICALCL 5.41818008026451e-16 0.00348587643796465 0.996514123562035 MICAL C-terminal like FUNCTION: May cooperate with MAPK1/ERK2 via an intracellular signal transduction pathway in the morphogenetic development of round spermatids to spermatozoa. {ECO:0000250}.; . . lung;bone;testis;colon; superior cervical ganglion;trigeminal ganglion; 0.03902 0.07299 2.535637851 98.7084218 915.19655 5.88377 MICALL1 0.000381388681523539 0.989977120000833 0.00964149131764312 MICAL like 1 FUNCTION: Probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, may act as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation. May be involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking. Alternatively, may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. May indirectly play a role in neurite outgrowth. {ECO:0000269|PubMed:19864458, ECO:0000269|PubMed:20801876, ECO:0000269|PubMed:21795389, ECO:0000269|PubMed:23596323}.; . . ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;lung;placenta;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.07935 0.08744 -0.793601146 12.57372022 4414.15439 13.29429 MICALL2 7.76189169980639e-17 0.00411634708296264 0.995883652917037 MICAL like 2 FUNCTION: Effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecules transport to the plasma membrane and actin cytoskeleton reorganization. Regulates the endocytic recycling of occludins, claudins and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. In parallel, may regulate actin cytoskeleton reorganization directly through interaction with F-actin or indirectly through actinins and filamins. Most probably involved in the processes of epithelial cell differentiation, cell spreading and neurite outgrowth (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;amnion;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion; 0.27411 0.08337 1.39439264 94.65675867 907.55182 5.86145 MICB 0.000284376917984568 0.791564707446551 0.208150915635464 MHC class I polypeptide-related sequence B FUNCTION: Seems to have no role in antigen presentation. Acts as a stress-induced self-antigen that is recognized by gamma delta T cells. Ligand for the KLRK1/NKG2D receptor. Binding to KLRK1 leads to cell lysis. {ECO:0000269|PubMed:11491531, ECO:0000269|PubMed:11777960, ECO:0000269|PubMed:9497295}.; DISEASE: Rheumatoid arthritis (RA) [MIM:180300]: An inflammatory disease with autoimmune features and a complex genetic component. It primarily affects the joints and is characterized by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures. {ECO:0000269|PubMed:17003176}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. The MICB*004 allele is associated with rheumatoid arthritis.; DISEASE: Note=Genetic variation in MICB is associated with cytomegalovirus and herpes simplex virus I seropositivity and this may be associated with schizophrenia risk.; TISSUE SPECIFICITY: Widely expressed with the exception of the central nervous system where it is absent. Expressed in many, but not all, epithelial tumors of lung, breast, kidney, ovary, prostate and colon. In hepatocellular carcinomas, expressed in tumor cells but not in surrounding non-cancerous tissue. {ECO:0000269|PubMed:10359807, ECO:0000269|PubMed:12569559, ECO:0000269|PubMed:17565371}.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;bone marrow;breast;prostate;pancreas;lung;larynx;liver;testis;head and neck;spleen;kidney;brain;bladder; . . . 1.818943827 96.98631753 922.94413 5.89929 MICC . . . MHC class I polypeptide-related sequence C (pseudogene) . . . . . . . . . . . MICD . . . MHC class I polypeptide-related sequence D (pseudogene) . . . . . . . . . . . MICE . . . MHC class I polypeptide-related sequence E (pseudogene) . . . . . . . . . . . MICF . . . MHC class I polypeptide-related sequence F (pseudogene) . . . . . . . . . . . MICG . . . MHC class I polypeptide-related sequence G (pseudogene) . . . . . . . . . . . MICU1 1.67853966108127e-10 0.112016182759103 0.887983817073043 mitochondrial calcium uptake 1 FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU) required to increase calcium uptake by MCU when cytoplasmic calcium is high. MICU1 and MICU2 form a disulfide-linked heterodimer that stimulate and inhibit MCU activity, respectively. MICU1 acts as a stimulator of MCU that senses calcium level via its EF-hand domains: enhances MCU opening at high Ca(2+) concentration, allowing a rapid response of mitochondria to Ca(2+) signals generated in the cytoplasm. Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake. Induces T-helper 1-mediated autoreactivity, which is accompanied by the release of IFNG. {ECO:0000269|PubMed:16002733, ECO:0000269|PubMed:20693986, ECO:0000269|PubMed:22904319, ECO:0000269|PubMed:23101630, ECO:0000269|PubMed:23747253, ECO:0000269|PubMed:24313810, ECO:0000269|PubMed:24332854, ECO:0000269|PubMed:24503055, ECO:0000269|PubMed:24560927, ECO:0000269|PubMed:26341627}.; DISEASE: Myopathy with extrapyramidal signs (MPXPS) [MIM:615673]: An autosomal recessive disorder characterized by early-onset proximal muscle weakness with a static course and moderately to grossly elevated serum creatine kinase levels accompanied by learning difficulties. Most patients develop subtle extrapyramidal motor signs that progress to a debilitating disorder of involuntary movement with variable features, including chorea, tremor, dystonic posturing and orofacial dyskinesia. Additional variable features include ataxia, microcephaly, ophthalmoplegia, ptosis, optic atrophy and axonal peripheral neuropathy. {ECO:0000269|PubMed:24336167}. Note=The disease is caused by mutations affecting the gene represented in this entry. The complex phenotype is due to alterations in mitochondrial calcium signaling characterized by increased mitochondrial Ca(2+) load (PubMed:24336167). {ECO:0000269|PubMed:24336167}.; TISSUE SPECIFICITY: Expressed in epithelial cell lines. Strongly expressed in epidermal keratinocytes and dermal endothelial cells. {ECO:0000269|PubMed:16002733, ECO:0000269|PubMed:9806765}.; lymphoreticular;myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;oesophagus;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;head and neck;kidney;aorta;stomach; medulla oblongata;superior cervical ganglion;occipital lobe;cerebellum peduncles;pons;atrioventricular node;skeletal muscle;globus pallidus;ciliary ganglion;kidney;parietal lobe;cingulate cortex;cerebellum; 0.22588 0.15808 -0.448125345 24.19202642 81.88875 1.91816 MICU2 2.60205517637133e-13 0.0352697159569386 0.964730284042801 mitochondrial calcium uptake 2 FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU) required to limit calcium uptake by MCU when cytoplasmic calcium is low. MICU1 and MICU2 form a disulfide-linked heterodimer that stimulate and inhibit MCU activity, respectively. MICU2 acts as a gatekeeper of MCU that senses calcium level via its EF-hand domains: prevents channel opening at resting Ca(2+), avoiding energy dissipation and cell-death triggering. {ECO:0000269|PubMed:24503055, ECO:0000269|PubMed:24560927}.; . . . . 0.50666 0.10135 0.174625237 65.9648502 110.42298 2.28667 MICU3 3.12316752281864e-06 0.931688824736748 0.0683080520957295 mitochondrial calcium uptake family member 3 FUNCTION: May play a role in mitochondrial calcium uptake. {ECO:0000250}.; . . . . 0.12251 . -0.736552314 13.93606983 1124.88873 6.40046 MID1 0.500724578255505 0.498395692284394 0.000879729460100733 midline 1 FUNCTION: Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. {ECO:0000269|PubMed:10400985, ECO:0000269|PubMed:11685209, ECO:0000269|PubMed:22613722}.; DISEASE: Opitz GBBB syndrome 1 (GBBB1) [MIM:300000]: A congenital midline malformation syndrome characterized by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, cleft lip/palate, laryngotracheoesophageal abnormalities, imperforate anus, developmental delay and congenital heart defects. {ECO:0000269|PubMed:11030761, ECO:0000269|PubMed:15558842, ECO:0000269|PubMed:9354791, ECO:0000269|PubMed:9718340}. Note=The disease is caused by mutations affecting the gene represented in this entry. MID1 mutations produce proteins with a decreased affinity for microtubules.; TISSUE SPECIFICITY: In the fetus, highest expression found in kidney, followed by brain and lung. Expressed at low levels in fetal liver. In the adult, most abundant in heart, placenta and brain.; myocardium;ovary;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;skeletal muscle;pia mater;lung;placenta;visual apparatus;liver;spleen;head and neck;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.17732 0.28993 -0.780646273 12.77423921 73.04018 1.78418 MID1IP1 0.489439187483796 0.43276952654233 0.0777912859738738 MID1 interacting protein 1 FUNCTION: Plays a role in the regulation of lipogenesis in liver. Up-regulates ACACA enzyme activity. Required for efficient lipid biosynthesis, including triacylglycerol, diacylglycerol and phospholipid. Involved in stabilization of microtubules (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;hypothalamus;muscle;blood;lens;skeletal muscle;pancreas;lung;epididymis;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; occipital lobe;thalamus;prefrontal cortex;caudate nucleus;parietal lobe;skeletal muscle; 0.35938 0.11809 0.103030231 61.2762444 13.60679 0.49454 MID1IP1-AS1 . . . MID1IP1 antisense RNA 1 . . . . . . . . . . . MID2 0.985076414331709 0.0149220057635706 1.57990472020797e-06 midline 2 FUNCTION: May play a role in microtubule stabilization. {ECO:0000303|PubMed:24115387}.; DISEASE: Mental retardation, X-linked 101 (MRX101) [MIM:300928]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non- syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. MRX101 clinical features include global developmental delay, hyperactivity often with aggressive outbursts, and seizures in some patients. Several affected individuals have long face, prominent ears, and squint or strabismus. {ECO:0000269|PubMed:24115387}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Low level in fetal kidney and lung, and in adult prostate, ovary and small intestine.; unclassifiable (Anatomical System);pancreas;lung;cartilage;islets of Langerhans;hypothalamus;thyroid;testis;choroid;kidney;retina; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex;skin; 0.58459 0.14063 -0.26993514 34.59542345 192.2938 3.00586 MIDN 0.0490626513742138 0.928196479163388 0.0227408694623981 midnolin FUNCTION: May be involved in regulation of genes related to neurogenesis in the nucleolus. {ECO:0000250}.; . . myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;thymus; . 0.31744 0.10986 -1.263883952 5.260674687 155.683 2.72666 MIEF1 0.0628938325307641 0.921465905895044 0.0156402615741921 mitochondrial elongation factor 1 FUNCTION: Mitochondrial outer membrane protein which regulates mitochondrial fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Regulates DNM1L GTPase activity and DNM1L oligomerization. Binds ADP and can also bind GDP, although with lower affinity. Does not bind CDP, UDP, ATP, AMP or GTP. Inhibits DNM1L GTPase activity in the absence of bound ADP. Requires ADP to stimulate DNM1L GTPase activity and the assembly of DNM1L into long, oligomeric tubules with a spiral pattern, as opposed to the ring-like DNM1L oligomers observed in the absence of bound ADP. Does not require ADP for its function in recruiting DNM1L. {ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560, ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:23530241, ECO:0000269|PubMed:23921378, ECO:0000269|PubMed:24515348}.; . TISSUE SPECIFICITY: Expression is relatively high in heart, skeletal muscle, pancreas and kidney. {ECO:0000269|PubMed:21701560}.; . . 0.12261 0.09986 0.420771676 77.15852795 1019.99486 6.14357 MIEF2 0.0770145219184436 0.872406053741442 0.0505794243401143 mitochondrial elongation factor 2 FUNCTION: Mitochondrial outer membrane protein which regulates mitochondrial fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Regulates DNM1L GTPase activity. {ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:23530241, ECO:0000269|PubMed:23921378}.; . TISSUE SPECIFICITY: Expressed in all tissues tested with highest expression in heart and skeletal muscle. {ECO:0000269|PubMed:11997338}.; . . 0.09602 0.10726 -0.532670911 20.78320359 1380.44839 6.96049 MIEN1 0.773016772764501 0.21927896726755 0.00770425996794949 migration and invasion enhancer 1 FUNCTION: Increases cell migration by inducing filopodia formation at the leading edge of migrating cells. Plays a role in regulation of apoptosis, possibly through control of CASP3. May be involved in a redox-related process. {ECO:0000269|PubMed:19503095, ECO:0000269|PubMed:21628459}.; . TISSUE SPECIFICITY: Among normal tissues, present only in Leydig cells. Strongly up-regulated in breast cancers and in brain cancer distant metastasis (at protein level). Up-regulated in prostate cancer cells and in the higher grades of prostate adenocarcinoma (at protein level). {ECO:0000269|PubMed:17121940, ECO:0000269|PubMed:19503095}.; . . 0.19784 . 0.057118534 57.99716914 14.24609 0.51525 MIER1 0.96629546639685 0.0337044356878882 9.79152618815934e-08 MIER1 transcriptional regulator FUNCTION: Transcriptional repressor regulating the expression of a number of genes including SP1 target genes. Probably functions through recruitment of HDAC1 a histone deacetylase involved in chromatin silencing. {ECO:0000269|PubMed:12482978}.; . TISSUE SPECIFICITY: Ubiquitously expressed, but at very low levels. However, consistent level of expression are observed in heart, testis, thyroid, ovary and adrenal gland. Transcripts are up-regulated in breast carcinoma cell lines and tumor. {ECO:0000269|PubMed:12242014, ECO:0000269|PubMed:9813250}.; myocardium;ovary;sympathetic chain;developmental;rectum;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.11236 0.11486 -0.071520315 48.34866714 224.62581 3.24151 MIER2 0.977262862888772 0.0227362351661571 9.01945070556463e-07 MIER family member 2 FUNCTION: Transcriptional repressor. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;ovary;colon;parathyroid;skin;retina;prostate;lung;frontal lobe;endometrium;larynx;bone;placenta;pituitary gland;liver;testis;cervix;head and neck;spleen;germinal center;kidney;brain;stomach;peripheral nerve; subthalamic nucleus;superior cervical ganglion;testis;atrioventricular node;parietal lobe;skeletal muscle; 0.24964 . -1.148192153 6.316348195 267.17865 3.50509 MIER3 0.999216429515142 0.000783564645104032 5.83975371410868e-09 MIER family member 3 FUNCTION: Transcriptional repressor. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;islets of Langerhans;hypothalamus;blood;lens;bile duct;lung;placenta;macula lutea;liver;alveolus;kidney; . 0.50948 . -0.381986487 27.68931352 208.40438 3.11594 MIF 0.0324842227823062 0.608514802773886 0.359000974443808 macrophage migration inhibitory factor (glycosylation-inhibiting factor) FUNCTION: Pro-inflammatory cytokine. Involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti- inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity. {ECO:0000269|PubMed:15908412, ECO:0000269|PubMed:17443469, ECO:0000269|PubMed:23776208}.; DISEASE: Rheumatoid arthritis systemic juvenile (RASJ) [MIM:604302]: An inflammatory articular disorder with systemic- onset beginning before the age of 16. It represents a subgroup of juvenile arthritis associated with severe extraarticular features and occasionally fatal complications. During active phases of the disorder, patients display a typical daily spiking fever, an evanescent macular rash, lymphadenopathy, hepatosplenomegaly, serositis, myalgia and arthritis. {ECO:0000269|PubMed:11508429}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. {ECO:0000305}.; . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;brain;artery;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;bile duct;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;liver;cervix;kidney;mammary gland;aorta;stomach; . 0.18607 0.37501 0.687150476 85.17928757 10.85213 0.39273 MIF-AS1 . . . MIF antisense RNA 1 . . . . . . . . . . . MIF4GD 3.58018633061673e-05 0.592434275687323 0.407529922449371 MIF4G domain containing FUNCTION: Functions in replication-dependent translation of histone mRNAs which differ from other eukaryotic mRNAs in that they do not end with a poly-A tail but a stem-loop. May participate in circularizing those mRNAs specifically enhancing their translation. {ECO:0000269|PubMed:18025107}.; . . myocardium;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; . 0.03324 . -0.183570861 39.95046001 1028.74548 6.16188 MIIP 1.96191775619765e-15 0.00200554599828121 0.997994454001717 migration and invasion inhibitory protein FUNCTION: Inhibits glioma cells invasion and down-regulates adhesion- and motility-associated genes such as NFKB2 and ICAM1. Exhibits opposing effects to IGFBP2 on cell invasion. {ECO:0000269|PubMed:14617774}.; . TISSUE SPECIFICITY: Ubiquitous. Isoform 1 is expressed in brain but underexpressed in glioma tissues, at protein level. Isoform 2 is not detected in normal organs, but is expressed in gliomas with increasing levels with glioma progression. On the contrary, at protein level, isoform 2 is not detected in gliomas, suggesting that this isoform is unstable in glioma cells. {ECO:0000269|PubMed:14617774}.; medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;testis;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; . . 0.69078985 85.23826374 1342.11428 6.87639 MILR1 . . . mast cell immunoglobulin-like receptor 1 FUNCTION: Immunoglobulin-like receptor which plays an inhibitory role in degranulation of mast cells. Negatively regulates IgE- mediated mast cell activation and suppresses the type I immediate hypersensitivity reaction (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in myeloid cells (dendritic cells, macrophages and neutrophils, weak expression on B-cells but not in T-cells or natural killer cells), peripheral blood basophils and mast cells (at protein level). {ECO:0000269|PubMed:20526344}.; . . 0.04185 0.07188 . . . . MIMT1 . . . MER1 repeat containing imprinted transcript 1 (non-protein coding) . . . . . . . . . . . MINA 1.5762094096492e-05 0.864091545793902 0.135892692112001 MYC induced nuclear antigen FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Is involved in the demethylation of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. Also catalyzes the hydroxylation of 60S ribosomal protein L27a on 'His-39'. May play an important role in cell growth and survival. May be involved in ribosome biogenesis, most likely during the assembly process of pre-ribosomal particles. {ECO:0000269|PubMed:12091391, ECO:0000269|PubMed:14695334, ECO:0000269|PubMed:15534111, ECO:0000269|PubMed:15819408, ECO:0000269|PubMed:15897898, ECO:0000269|PubMed:17317935, ECO:0000269|PubMed:19502796, ECO:0000269|PubMed:23103944}.; . TISSUE SPECIFICITY: Expressed in liver, skeletal muscle, heart, pancreas, and placenta. Not detected in brain, lung or kidney. Expressed in several lung cancer tissues, but is barely detected in the adjacent non-cancerous tissues. Also highly expressed in several esophageal squamous cell carcinoma (ESCC), and colon cancer tissues, and in various cancer cell lines. {ECO:0000269|PubMed:14695334, ECO:0000269|PubMed:15534111, ECO:0000269|PubMed:15897898, ECO:0000269|PubMed:19502796}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;hippocampus;macula lutea;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;thyroid;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12921 0.11605 7.61E-05 53.98089172 3706.92143 11.86837 MINCR . . . MYC-induced long noncoding RNA . . . . . . . . . . . MINK1 0.999984021507432 1.59784925675217e-05 7.45447666193251e-16 misshapen-like kinase 1 FUNCTION: Serine/threonine kinase which acts as a negative regulator of Ras-related Rap2-mediated signal transduction to control neuronal structure and AMPA receptor trafficking. Required for normal synaptic density, dendrite complexity, as well as surface AMPA receptor expression in hippocampal neurons. Can activate the JNK and MAPK14/p38 pathways and mediates stimulation of the stress-activated protein kinase MAPK14/p38 MAPK downstream of the Raf/ERK pathway. Phosphorylates: TANC1 upon stimulation by RAP2A, MBP and SMAD1. Has an essential function in negative selection of thymocytes, perhaps by coupling NCK1 to activation of JNK1.; . TISSUE SPECIFICITY: Expressed in the brain, isoform 2 is more abundant than isoform 1. Isoform 3 is ubiquitously expressed. Isoform 1 is most abundant in the skeletal muscle. Isoform 4 is ubiquitously expressed with relative high levels in brain, skeletal muscle, pancreas and testis. {ECO:0000269|PubMed:15469942}.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; amygdala;dorsal root ganglion;whole brain;medulla oblongata;occipital lobe;thalamus;superior cervical ganglion;spinal cord;atrioventricular node;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.46968 0.13857 -1.456898556 3.862939372 2119.37505 8.47592 MINOS1 0.348880394858809 0.595441544090373 0.0556780610508182 mitochondrial inner membrane organizing system 1 FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. {ECO:0000269|PubMed:22114354}.; . . . . 0.46057 0.09989 0.013025609 54.62962963 1.11711 0.03030 MINOS1-NBL1 0.0681079828537187 0.735277191270599 0.196614825875682 MINOS1-NBL1 readthrough FUNCTION: Possible candidate as a tumor suppressor gene of neuroblastoma. May play an important role in preventing cells from entering the final stage (G1/S) of the transformation process.; . TISSUE SPECIFICITY: Most abundant in normal lung and meningioma.; . . . . . . 19.17431 0.66067 MINOS1P1 . . . mitochondrial inner membrane organizing system 1 pseudogene 1 . . . . . . . . . . . MINOS1P2 . . . mitochondrial inner membrane organizing system 1 pseudogene 2 . . . . . . . . . . . MINOS1P3 . . . mitochondrial inner membrane organizing system 1 pseudogene 3 . . . . . . . . . . . MINOS1P4 . . . mitochondrial inner membrane organizing system 1 pseudogene 4 . . . . . . . . . . . MINPP1 0.454406266536868 0.54434013453342 0.00125359892971174 multiple inositol-polyphosphate phosphatase 1 FUNCTION: Acts as a phosphoinositide 5- and phosphoinositide 6- phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Also acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3- phosphoglycerate. May play a role in bone development (endochondral ossification). {ECO:0000269|PubMed:18413611}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in kidney, liver and placenta. {ECO:0000269|PubMed:9923613}.; . . 0.92582 0.12952 -0.626318434 17.03231894 16.64118 0.58633 MIOS 0.00143566907100511 0.998504239526214 6.00914027812632e-05 missing oocyte, meiosis regulator, homolog (Drosophila) FUNCTION: As a component of the GATOR2 complex, inhibits GATOR1 complex, an inhibitor of the amino acid-sensing branch of the TORC1 pathway.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;unclassifiable (Anatomical System);heart;cerebellum cortex;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;medulla oblongata;testis - seminiferous tubule;testis;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; . . -0.953385901 9.206180703 70.06975 1.73689 MIOX 4.60477630861768e-12 0.0140399274833725 0.985960072512023 myo-inositol oxygenase . . TISSUE SPECIFICITY: Kidney specific.; unclassifiable (Anatomical System);lung;adrenal gland;bone;thyroid;adrenal cortex;colon;parathyroid;kidney;pineal gland;mammary gland;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;kidney; 0.17947 0.12797 -0.200157416 39.11299835 99.70995 2.16398 MIOXP1 . . . myo-inositol oxygenase pseudogene 1 . . . . . . . . . . . MIP 0.677914765017758 0.317450025187699 0.00463520979454267 major intrinsic protein of lens fiber FUNCTION: Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core (By similarity). {ECO:0000250}.; DISEASE: Cataract 15, multiple types (CTRCT15) [MIM:615274]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT15 includes polymorphic, progressive punctate lamellar, cortical, anterior and posterior polar, nonprogressive lamellar with sutural opacities, embryonic nuclear, and pulverulent cortical, among others. {ECO:0000269|PubMed:10802646, ECO:0000269|PubMed:11001937, ECO:0000269|PubMed:16564824, ECO:0000269|PubMed:17893667, ECO:0000269|PubMed:17960133, ECO:0000269|PubMed:20361015, ECO:0000269|PubMed:21245956}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Major component of lens fiber gap junctions.; optic nerve;macula lutea;visual apparatus;fovea centralis;choroid;lens;retina; . 0.18404 0.14494 0.148941568 64.31941496 213.46635 3.15296 MIPEP 8.49063579888535e-07 0.995681945041719 0.00431720589470084 mitochondrial intermediate peptidase FUNCTION: Cleaves proteins, imported into the mitochondrion, to their mature size.; . . . . 0.14579 0.12054 0.624649618 83.53385232 570.57063 4.84602 MIPEPP1 . . . mitochondrial intermediate peptidase pseudogene 1 . . . . . . . . . . . MIPEPP2 . . . mitochondrial intermediate peptidase pseudogene 2 . . . . . . . . . . . MIPEPP3 . . . mitochondrial intermediate peptidase pseudogene 3 . . . . . . . . . . . MIPOL1 6.81655610731612e-06 0.899072396668388 0.100920786775505 mirror-image polydactyly 1 . . TISSUE SPECIFICITY: Expressed very weakly in heart, liver, skeletal muscle, kidney, pancreas and fetal kidney. Not detected in brain, placenta and lung. {ECO:0000269|PubMed:11954550}.; unclassifiable (Anatomical System);lung;thyroid;visual apparatus;testis;blood;head and neck;skeletal muscle;stomach; subthalamic nucleus;olfactory bulb;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05246 0.09163 -0.712684326 14.49634348 75.79942 1.82421 MIR1-1 . . . microRNA 1-1 . . . . . . . . . . . MIR1-1HG . . . MIR1-1 host gene . . . . . 0.06937 . 0.815800671 87.8744987 . . MIR1-2 . . . microRNA 1-2 . . . . . . . . . . . MIR7-1 . . . microRNA 7-1 . . . . . . . . . . . MIR7-2 . . . microRNA 7-2 . . . . . . . . . . . MIR7-3 . . . microRNA 7-3 . . . . . . . . . . . MIR7-3HG . . . MIR7-3 host gene . . TISSUE SPECIFICITY: High expression in pituitary gland and weak in pancreas. {ECO:0000269|PubMed:11854097}.; unclassifiable (Anatomical System);lung;pituitary gland; . 0.04600 0.06751 . . . . MIR9-1 . . . microRNA 9-1 . . . . . . . . . . . MIR9-2 . . . microRNA 9-2 . . . . . . . . . . . MIR9-3 . . . microRNA 9-3 . . . . . . . . . . . MIR9-3HG . . . MIR9-3 host gene . . . . . . . . . . . MIR10A . . . microRNA 10a . . . . . . . . . . . MIR10B . . . microRNA 10b . . . . . . . . . . . MIR15A . . . microRNA 15a . . . . . . . . . . . MIR15B . . . microRNA 15b . . . . . . . . . . . MIR16-1 . . . microRNA 16-1 . . . . . . . . . . . MIR16-2 . . . microRNA 16-2 . . . . . . . . . . . MIR17 . . . microRNA 17 . . . . . . . . . . . MIR17HG . . . miR-17-92 cluster host gene . . TISSUE SPECIFICITY: Highly expressed in B-cell lymphoma and lung cancer.; . . 0.16478 . . . . . MIR18A . . . microRNA 18a . . . . . . . . . . . MIR18B . . . microRNA 18b . . . . . . . . . . . MIR19A . . . microRNA 19a . . . . . . . . . . . MIR19B1 . . . microRNA 19b-1 . . . . . . . . . . . MIR19B2 . . . microRNA 19b-2 . . . . . . . . . . . MIR20A . . . microRNA 20a . . . . . . . . . . . MIR20B . . . microRNA 20b . . . . . . . . . . . MIR21 . . . microRNA 21 . . . . . . . . . . . MIR22 . . . microRNA 22 . . . . . . . . . . . MIR22HG . . . MIR22 host gene . . . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;blood;skin;uterus;pancreas;prostate;whole body;lung;endometrium;adrenal gland;bone;thyroid;placenta;visual apparatus;pituitary gland;liver;spleen;kidney;brain;mammary gland;stomach; . 0.08097 . . . . . MIR23A . . . microRNA 23a . . . . . . . . . . . MIR23B . . . microRNA 23b . . . . . . . . . . . MIR23C . . . microRNA 23c . . . . . . . . . . . MIR24-1 . . . microRNA 24-1 . . . . . . . . . . . MIR24-2 . . . microRNA 24-2 . . . . . . . . . . . MIR25 . . . microRNA 25 . . . . . . . . . . . MIR26A1 . . . microRNA 26a-1 . . . . . . . . . . . MIR26A2 . . . microRNA 26a-2 . . . . . . . . . . . MIR26B . . . microRNA 26b . . . . . . . . . . . MIR27A . . . microRNA 27a . . . . . . . . . . . MIR27B . . . microRNA 27b . . . . . . . . . . . MIR28 . . . microRNA 28 . . . . . . . . . . . MIR29A . . . microRNA 29a . . . . . . . . . . . MIR29B1 . . . microRNA 29b-1 . . . . . . . . . . . MIR29B2 . . . microRNA 29b-2 . . . . . . . . . . . MIR29C . . . microRNA 29c . . . . . . . . . . . MIR30A . . . microRNA 30a . . . . . . . . . . . MIR30B . . . microRNA 30b . . . . . . . . . . . MIR30C1 . . . microRNA 30c-1 . . . . . . . . . . . MIR30C2 . . . microRNA 30c-2 . . . . . . . . . . . MIR30D . . . microRNA 30d . . . . . . . . . . . MIR30E . . . microRNA 30e . . . . . . . . . . . MIR31 . . . microRNA 31 . . . . . . . . . . . MIR31HG . . . MIR31 host gene . . . cervix; . . . . . . . MIR32 . . . microRNA 32 . . . . . . . . . . . MIR33A . . . microRNA 33a . . . . . . . . . . . MIR33B . . . microRNA 33b . . . . . . . . . . . MIR34A . . . microRNA 34a . . . . . . . . . . . MIR34AHG . . . MIR34A host gene . . . . . . . . . . . MIR34B . . . microRNA 34b . . . . . . . . . . . MIR34C . . . microRNA 34c . . . . . . . . . . . MIR92A1 . . . microRNA 92a-1 . . . . . . . . . . . MIR92A2 . . . microRNA 92a-2 . . . . . . . . . . . MIR92B . . . microRNA 92b . . . . . . . . . . . MIR93 . . . microRNA 93 . . . . . . . . . . . MIR95 . . . microRNA 95 . . . . . . . . . . . MIR96 . . . microRNA 96 . . . . . . . . . . . MIR98 . . . microRNA 98 . . . . . . . . . . . MIR99A . . . microRNA 99a . . . . . . . . . . . MIR99AHG . . . mir-99a-let-7c cluster host gene . . . . . 0.72058 . . . . . MIR99B . . . microRNA 99b . . . . . . . . . . . MIR100 . . . microRNA 100 . . . . . . . . . . . MIR100HG . . . mir-100-let-7a-2 cluster host gene . . . . . . . . . . . MIR101-1 . . . microRNA 101-1 . . . . . . . . . . . MIR101-2 . . . microRNA 101-2 . . . . . . . . . . . MIR103A1 . . . microRNA 103a-1 . . . . . . . . . . . MIR103A2 . . . microRNA 103a-2 . . . . . . . . . . . MIR103B1 . . . microRNA 103b-1 . . . . . . . . . . . MIR103B2 . . . microRNA 103b-2 . . . . . . . . . . . MIR105-1 . . . microRNA 105-1 . . . . . . . . . . . MIR105-2 . . . microRNA 105-2 . . . . . . . . . . . MIR106A . . . microRNA 106a . . . . . . . . . . . MIR106B . . . microRNA 106b . . . . . . . . . . . MIR107 . . . microRNA 107 . . . . . . . . . . . MIR122 . . . microRNA 122 . . . . . . . . . . . MIR124-1 . . . microRNA 124-1 . . . . . . . . . . . MIR124-2 . . . microRNA 124-2 . . . . . . . . . . . MIR124-2HG . . . MIR124-2 host gene . . . . . . . . . . . MIR124-3 . . . microRNA 124-3 . . . . . . . . . . . MIR125A . . . microRNA 125a . . . . . . . . . . . MIR125B1 . . . microRNA 125b-1 . . . . . . . . . . . MIR125B2 . . . microRNA 125b-2 . . . . . . . . . . . MIR126 . . . microRNA 126 . . . . . . . . . . . MIR127 . . . microRNA 127 . . . . . . . . . . . MIR128-1 . . . microRNA 128-1 . . . . . . . . . . . MIR128-2 . . . microRNA 128-2 . . . . . . . . . . . MIR129-1 . . . microRNA 129-1 . . . . . . . . . . . MIR129-2 . . . microRNA 129-2 . . . . . . . . . . . MIR130A . . . microRNA 130a . . . . . . . . . . . MIR130B . . . microRNA 130b . . . . . . . . . . . MIR132 . . . microRNA 132 . . . . . . . . . . . MIR133A1 . . . microRNA 133a-1 . . . . . . . . . . . MIR133A1HG . . . MIR133A1 host gene . . . . . . . . . . . MIR133A2 . . . microRNA 133a-2 . . . . . . . . . . . MIR133B . . . microRNA 133b . . . . . . . . . . . MIR134 . . . microRNA 134 . . . . . . . . . . . MIR135A1 . . . microRNA 135a-1 . . . . . . . . . . . MIR135A2 . . . microRNA 135a-2 . . . . . . . . . . . MIR135B . . . microRNA 135b . . . . . . . . . . . MIR136 . . . microRNA 136 . . . . . . . . . . . MIR137 . . . microRNA 137 . . . . . . . . . . . MIR137HG . . . MIR137 host gene . . . . . . . . . . . MIR138-1 . . . microRNA 138-1 . . . . . . . . . . . MIR138-2 . . . microRNA 138-2 . . . . . . . . . . . MIR139 . . . microRNA 139 . . . . . . . . . . . MIR140 . . . microRNA 140 . . . . . . . . . . . MIR141 . . . microRNA 141 . . . . . . . . . . . MIR142 . . . microRNA 142 . . . . . . . . . . . MIR143 . . . microRNA 143 . . . . . . . . . . . MIR144 . . . microRNA 144 . . . . . . . . . . . MIR145 . . . microRNA 145 . . . . . . . . . . . MIR146A . . . microRNA 146a . . . . . . . . . . . MIR146B . . . microRNA 146b . . . . . . . . . . . MIR147A . . . microRNA 147a . . . . . . . . . . . MIR147B . . . microRNA 147b . . . . . . . . . . . MIR148A . . . microRNA 148a . . . . . . . . . . . MIR148B . . . microRNA 148b . . . . . . . . . . . MIR149 . . . microRNA 149 . . . . . . . . . . . MIR150 . . . microRNA 150 . . . . . . . . . . . MIR151A . . . microRNA 151a . . . . . . . . . . . MIR151B . . . microRNA 151b . . . . . . . . . . . MIR152 . . . microRNA 152 . . . . . . . . . . . MIR153-1 . . . microRNA 153-1 . . . . . . . . . . . MIR153-2 . . . microRNA 153-2 . . . . . . . . . . . MIR154 . . . microRNA 154 . . . . . . . . . . . MIR155 . . . microRNA 155 . . . . . . . . . . . MIR155HG . . . MIR155 host gene . . . . . . . . . . . MIR181A1 . . . microRNA 181a-1 . . . . . . . . . . . MIR181A1HG . . . MIR181A1 host gene . . . . . . . . . . . MIR181A2 . . . microRNA 181a-2 . . . . . . . . . . . MIR181A2HG . . . MIR181A2 host gene . . . . . . . . . . . MIR181B1 . . . microRNA 181b-1 . . . . . . . . . . . MIR181B2 . . . microRNA 181b-2 . . . . . . . . . . . MIR181C . . . microRNA 181c . . . . . . . . . . . MIR181D . . . microRNA 181d . . . . . . . . . . . MIR182 . . . microRNA 182 . . . . . . . . . . . MIR183 . . . microRNA 183 . . . . . . . . . . . MIR184 . . . microRNA 184 . . . . . . . . . . . MIR185 . . . microRNA 185 . . . . . . . . . . . MIR186 . . . microRNA 186 . . . . . . . . . . . MIR187 . . . microRNA 187 . . . . . . . . . . . MIR188 . . . microRNA 188 . . . . . . . . . . . MIR190A . . . microRNA 190a . . . . . . . . . . . MIR190B . . . microRNA 190b . . . . . . . . . . . MIR191 . . . microRNA 191 . . . . . . . . . . . MIR192 . . . microRNA 192 . . . . . . . . . . . MIR193A . . . microRNA 193a . . . . . . . . . . . MIR193B . . . microRNA 193b . . . . . . . . . . . MIR193BHG . . . MIR193B host gene . . . . . . . . . . . MIR194-1 . . . microRNA 194-1 . . . . . . . . . . . MIR194-2 . . . microRNA 194-2 . . . . . . . . . . . MIR194-2HG . . . MIR194-2 host gene . . . . . . . . . . . MIR195 . . . microRNA 195 . . . . . . . . . . . MIR196A1 . . . microRNA 196a-1 . . . . . . . . . . . MIR196A2 . . . microRNA 196a-2 . . . . . . . . . . . MIR196B . . . microRNA 196b . . . . . . . . . . . MIR197 . . . microRNA 197 . . . . . . . . . . . MIR198 . . . microRNA 198 . . . . . . . . . . . MIR199A1 . . . microRNA 199a-1 . . . . . . . . . . . MIR199A2 . . . microRNA 199a-2 . . . . . . . . . . . MIR199B . . . microRNA 199b . . . . . . . . . . . MIR200A . . . microRNA 200a . . . . . . . . . . . MIR200B . . . microRNA 200b . . . . . . . . . . . MIR200C . . . microRNA 200c . . . . . . . . . . . MIR202 . . . microRNA 202 . . . . . . . . . . . MIR202HG . . . MIR202 host gene . . . . . 0.15527 . . . . . MIR203A . . . microRNA 203a . . . . . . . . . . . MIR203B . . . microRNA 203b . . . . . . . . . . . MIR204 . . . microRNA 204 . . . . . . . . . . . MIR205 . . . microRNA 205 . . . . . . . . . . . MIR205HG . . . MIR205 host gene . . . . . . . . . . . MIR206 . . . microRNA 206 . . . . . . . . . . . MIR208A . . . microRNA 208a . . . . . . . . . . . MIR208B . . . microRNA 208b . . . . . . . . . . . MIR210 . . . microRNA 210 . . . . . . . . . . . MIR210HG . . . MIR210 host gene . . . . . . . . . . . MIR211 . . . microRNA 211 . . . . . . . . . . . MIR212 . . . microRNA 212 . . . . . . . . . . . MIR214 . . . microRNA 214 . . . . . . . . . . . MIR215 . . . microRNA 215 . . . . . . . . . . . MIR216A . . . microRNA 216a . . . . . . . . . . . MIR216B . . . microRNA 216b . . . . . . . . . . . MIR217 . . . microRNA 217 . . . . . . . . . . . MIR217HG . . . MIR217 host gene . . . . . . . . . . . MIR218-1 . . . microRNA 218-1 . . . . . . . . . . . MIR218-2 . . . microRNA 218-2 . . . . . . . . . . . MIR219A1 . . . microRNA 219a-1 . . . . . . . . . . . MIR219A2 . . . microRNA 219a-2 . . . . . . . . . . . MIR219B . . . microRNA 219b . . . . . . . . . . . MIR221 . . . microRNA 221 . . . . . . . . . . . MIR222 . . . microRNA 222 . . . . . . . . . . . MIR222HG . . . MIR222 host gene . . . . . . . . . . . MIR223 . . . microRNA 223 . . . . . . . . . . . MIR224 . . . microRNA 224 . . . . . . . . . . . MIR296 . . . microRNA 296 . . . . . . . . . . . MIR297 . . . microRNA 297 . . . . . . . . . . . MIR298 . . . microRNA 298 . . . . . . . . . . . MIR299 . . . microRNA 299 . . . . . . . . . . . MIR300 . . . microRNA 300 . . . . . . . . . . . MIR301A . . . microRNA 301a . . . . . . . . . . . MIR301B . . . microRNA 301b . . . . . . . . . . . MIR302A . . . microRNA 302a . . . . . . . . . . . MIR302B . . . microRNA 302b . . . . . . . . . . . MIR302C . . . microRNA 302c . . . . . . . . . . . MIR302D . . . microRNA 302d . . . . . . . . . . . MIR302E . . . microRNA 302e . . . . . . . . . . . MIR302F . . . microRNA 302f . . . . . . . . . . . MIR320A . . . microRNA 320a . . . . . . . . . . . MIR320B1 . . . microRNA 320b-1 . . . . . . . . . . . MIR320B2 . . . microRNA 320b-2 . . . . . . . . . . . MIR320C1 . . . microRNA 320c-1 . . . . . . . . . . . MIR320C2 . . . microRNA 320c-2 . . . . . . . . . . . MIR320D1 . . . microRNA 320d-1 . . . . . . . . . . . MIR320D2 . . . microRNA 320d-2 . . . . . . . . . . . MIR320E . . . microRNA 320e . . . . . . . . . . . MIR323A . . . microRNA 323a . . . . . . . . . . . MIR323B . . . microRNA 323b . . . . . . . . . . . MIR324 . . . microRNA 324 . . . . . . . . . . . MIR325 . . . microRNA 325 . . . . . . . . . . . MIR325HG . . . MIR325 host gene . . . . . . . . . . . MIR326 . . . microRNA 326 . . . . . . . . . . . MIR328 . . . microRNA 328 . . . . . . . . . . . MIR329-1 . . . microRNA 329-1 . . . . . . . . . . . MIR329-2 . . . microRNA 329-2 . . . . . . . . . . . MIR330 . . . microRNA 330 . . . . . . . . . . . MIR331 . . . microRNA 331 . . . . . . . . . . . MIR335 . . . microRNA 335 . . . . . . . . . . . MIR337 . . . microRNA 337 . . . . . . . . . . . MIR338 . . . microRNA 338 . . . . . . . . . . . MIR339 . . . microRNA 339 . . . . . . . . . . . MIR340 . . . microRNA 340 . . . . . . . . . . . MIR342 . . . microRNA 342 . . . . . . . . . . . MIR345 . . . microRNA 345 . . . . . . . . . . . MIR346 . . . microRNA 346 . . . . . . . . . . . MIR361 . . . microRNA 361 . . . . . . . . . . . MIR362 . . . microRNA 362 . . . . . . . . . . . MIR363 . . . microRNA 363 . . . . . . . . . . . MIR365A . . . microRNA 365a . . . . . . . . . . . MIR365B . . . microRNA 365b . . . . . . . . . . . MIR367 . . . microRNA 367 . . . . . . . . . . . MIR369 . . . microRNA 369 . . . . . . . . . . . MIR370 . . . microRNA 370 . . . . . . . . . . . MIR371A . . . microRNA 371a . . . . . . . . . . . MIR371B . . . microRNA 371b . . . . . . . . . . . MIR372 . . . microRNA 372 . . . . . . . . . . . MIR373 . . . microRNA 373 . . . . . . . . . . . MIR374A . . . microRNA 374a . . . . . . . . . . . MIR374B . . . microRNA 374b . . . . . . . . . . . MIR374C . . . microRNA 374c . . . . . . . . . . . MIR375 . . . microRNA 375 . . . . . . . . . . . MIR376A1 . . . microRNA 376a-1 . . . . . . . . . . . MIR376A2 . . . microRNA 376a-2 . . . . . . . . . . . MIR376B . . . microRNA 376b . . . . . . . . . . . MIR376C . . . microRNA 376c . . . . . . . . . . . MIR377 . . . microRNA 377 . . . . . . . . . . . MIR378A . . . microRNA 378a . . . . . . . . . . . MIR378B . . . microRNA 378b . . . . . . . . . . . MIR378C . . . microRNA 378c . . . . . . . . . . . MIR378D1 . . . microRNA 378d-1 . . . . . . . . . . . MIR378D2 . . . microRNA 378d-2 . . . . . . . . . . . MIR378E . . . microRNA 378e . . . . . . . . . . . MIR378F . . . microRNA 378f . . . . . . . . . . . MIR378G . . . microRNA 378g . . . . . . . . . . . MIR378H . . . microRNA 378h . . . . . . . . . . . MIR378I . . . microRNA 378i . . . . . . . . . . . MIR378J . . . microRNA 378j . . . . . . . . . . . MIR379 . . . microRNA 379 . . . . . . . . . . . MIR380 . . . microRNA 380 . . . . . . . . . . . MIR381 . . . microRNA 381 . . . . . . . . . . . MIR381HG . . . MIR381 host gene . . . . . . . . . . . MIR382 . . . microRNA 382 . . . . . . . . . . . MIR383 . . . microRNA 383 . . . . . . . . . . . MIR384 . . . microRNA 384 . . . . . . . . . . . MIR409 . . . microRNA 409 . . . . . . . . . . . MIR410 . . . microRNA 410 . . . . . . . . . . . MIR411 . . . microRNA 411 . . . . . . . . . . . MIR412 . . . microRNA 412 . . . . . . . . . . . MIR421 . . . microRNA 421 . . . . . . . . . . . MIR422A . . . microRNA 422a . . . . . . . . . . . MIR423 . . . microRNA 423 . . . . . . . . . . . MIR424 . . . microRNA 424 . . . . . . . . . . . MIR425 . . . microRNA 425 . . . . . . . . . . . MIR429 . . . microRNA 429 . . . . . . . . . . . MIR431 . . . microRNA 431 . . . . . . . . . . . MIR432 . . . microRNA 432 . . . . . . . . . . . MIR433 . . . microRNA 433 . . . . . . . . . . . MIR448 . . . microRNA 448 . . . . . . . . . . . MIR449A . . . microRNA 449a . . . . . . . . . . . MIR449B . . . microRNA 449b . . . . . . . . . . . MIR449C . . . microRNA 449c . . . . . . . . . . . MIR450A1 . . . microRNA 450a-1 . . . . . . . . . . . MIR450A2 . . . microRNA 450a-2 . . . . . . . . . . . MIR450B . . . microRNA 450b . . . . . . . . . . . MIR451A . . . microRNA 451a . . . . . . . . . . . MIR451B . . . microRNA 451b . . . . . . . . . . . MIR452 . . . microRNA 452 . . . . . . . . . . . MIR454 . . . microRNA 454 . . . . . . . . . . . MIR455 . . . microRNA 455 . . . . . . . . . . . MIR466 . . . microRNA 466 . . . . . . . . . . . MIR483 . . . microRNA 483 . . . . . . . . . . . MIR484 . . . microRNA 484 . . . . . . . . . . . MIR485 . . . microRNA 485 . . . . . . . . . . . MIR486-1 . . . microRNA 486-1 . . . . . . . . . . . MIR486-2 . . . microRNA 486-2 . . . . . . . . . . . MIR487A . . . microRNA 487a . . . . . . . . . . . MIR487B . . . microRNA 487b . . . . . . . . . . . MIR488 . . . microRNA 488 . . . . . . . . . . . MIR489 . . . microRNA 489 . . . . . . . . . . . MIR490 . . . microRNA 490 . . . . . . . . . . . MIR491 . . . microRNA 491 . . . . . . . . . . . MIR492 . . . microRNA 492 . . . . . . . . . . . MIR493 . . . microRNA 493 . . . . . . . . . . . MIR494 . . . microRNA 494 . . . . . . . . . . . MIR495 . . . microRNA 495 . . . . . . . . . . . MIR496 . . . microRNA 496 . . . . . . . . . . . MIR497 . . . microRNA 497 . . . . . . . . . . . MIR497HG . . . mir-497-195 cluster host gene . . . . . . . . . . . MIR498 . . . microRNA 498 . . . . . . . . . . . MIR499A . . . microRNA 499a . . . . . . . . . . . MIR499B . . . microRNA 499b . . . . . . . . . . . MIR500A . . . microRNA 500a . . . . . . . . . . . MIR500B . . . microRNA 500b . . . . . . . . . . . MIR501 . . . microRNA 501 . . . . . . . . . . . MIR502 . . . microRNA 502 . . . . . . . . . . . MIR503 . . . microRNA 503 . . . . . . . . . . . MIR503HG . . . MIR503 host gene . . . . . . . . . . . MIR504 . . . microRNA 504 . . . . . . . . . . . MIR505 . . . microRNA 505 . . . . . . . . . . . MIR506 . . . microRNA 506 . . . . . . . . . . . MIR507 . . . microRNA 507 . . . . . . . . . . . MIR508 . . . microRNA 508 . . . . . . . . . . . MIR509-1 . . . microRNA 509-1 . . . . . . . . . . . MIR509-2 . . . microRNA 509-2 . . . . . . . . . . . MIR509-3 . . . microRNA 509-3 . . . . . . . . . . . MIR510 . . . microRNA 510 . . . . . . . . . . . MIR511 . . . microRNA 511 . . . . . . . . . . . MIR512-1 . . . microRNA 512-1 . . . . . . . . . . . MIR512-2 . . . microRNA 512-2 . . . . . . . . . . . MIR513A1 . . . microRNA 513a-1 . . . . . . . . . . . MIR513A2 . . . microRNA 513a-2 . . . . . . . . . . . MIR513B . . . microRNA 513b . . . . . . . . . . . MIR513C . . . microRNA 513c . . . . . . . . . . . MIR514A1 . . . microRNA 514a-1 . . . . . . . . . . . MIR514A2 . . . microRNA 514a-2 . . . . . . . . . . . MIR514A3 . . . microRNA 514a-3 . . . . . . . . . . . MIR514B . . . microRNA 514b . . . . . . . . . . . MIR515-1 . . . microRNA 515-1 . . . . . . . . . . . MIR515-2 . . . microRNA 515-2 . . . . . . . . . . . MIR516A1 . . . microRNA 516a-1 . . . . . . . . . . . MIR516A2 . . . microRNA 516a-2 . . . . . . . . . . . MIR516B1 . . . microRNA 516b-1 . . . . . . . . . . . MIR516B2 . . . microRNA 516b-2 . . . . . . . . . . . MIR517A . . . microRNA 517a . . . . . . . . . . . MIR517B . . . microRNA 517b . . . . . . . . . . . MIR517C . . . microRNA 517c . . . . . . . . . . . MIR518A1 . . . microRNA 518a-1 . . . . . . . . . . . MIR518A2 . . . microRNA 518a-2 . . . . . . . . . . . MIR518B . . . microRNA 518b . . . . . . . . . . . MIR518C . . . microRNA 518c . . . . . . . . . . . MIR518D . . . microRNA 518d . . . . . . . . . . . MIR518E . . . microRNA 518e . . . . . . . . . . . MIR518F . . . microRNA 518f . . . . . . . . . . . MIR519A1 . . . microRNA 519a-1 . . . . . . . . . . . MIR519A2 . . . microRNA 519a-2 . . . . . . . . . . . MIR519B . . . microRNA 519b . . . . . . . . . . . MIR519C . . . microRNA 519c . . . . . . . . . . . MIR519D . . . microRNA 519d . . . . . . . . . . . MIR519E . . . microRNA 519e . . . . . . . . . . . MIR520A . . . microRNA 520a . . . . . . . . . . . MIR520B . . . microRNA 520b . . . . . . . . . . . MIR520C . . . microRNA 520c . . . . . . . . . . . MIR520D . . . microRNA 520d . . . . . . . . . . . MIR520E . . . microRNA 520e . . . . . . . . . . . MIR520F . . . microRNA 520f . . . . . . . . . . . MIR520G . . . microRNA 520g . . . . . . . . . . . MIR520H . . . microRNA 520h . . . . . . . . . . . MIR521-1 . . . microRNA 521-1 . . . . . . . . . . . MIR521-2 . . . microRNA 521-2 . . . . . . . . . . . MIR522 . . . microRNA 522 . . . . . . . . . . . MIR523 . . . microRNA 523 . . . . . . . . . . . MIR524 . . . microRNA 524 . . . . . . . . . . . MIR525 . . . microRNA 525 . . . . . . . . . . . MIR526A1 . . . microRNA 526a-1 . . . . . . . . . . . MIR526A2 . . . microRNA 526a-2 . . . . . . . . . . . MIR526B . . . microRNA 526b . . . . . . . . . . . MIR527 . . . microRNA 527 . . . . . . . . . . . MIR532 . . . microRNA 532 . . . . . . . . . . . MIR539 . . . microRNA 539 . . . . . . . . . . . MIR541 . . . microRNA 541 . . . . . . . . . . . MIR542 . . . microRNA 542 . . . . . . . . . . . MIR543 . . . microRNA 543 . . . . . . . . . . . MIR544A . . . microRNA 544a . . . . . . . . . . . MIR544B . . . microRNA 544b . . . . . . . . . . . MIR545 . . . microRNA 545 . . . . . . . . . . . MIR548A1 . . . microRNA 548a-1 . . . . . . . . . . . MIR548A2 . . . microRNA 548a-2 . . . . . . . . . . . MIR548A3 . . . microRNA 548a-3 . . . . . . . . . . . MIR548AA1 . . . microRNA 548aa-1 . . . . . . . . . . . MIR548AA2 . . . microRNA 548aa-2 . . . . . . . . . . . MIR548AB . . . microRNA 548ab . . . . . . . . . . . MIR548AC . . . microRNA 548ac . . . . . . . . . . . MIR548AD . . . microRNA 548ad . . . . . . . . . . . MIR548AE1 . . . microRNA 548ae-1 . . . . . . . . . . . MIR548AE2 . . . microRNA 548ae-2 . . . . . . . . . . . MIR548AG1 . . . microRNA 548ag-1 . . . . . . . . . . . MIR548AG2 . . . microRNA 548ag-2 . . . . . . . . . . . MIR548AH . . . microRNA 548ah . . . . . . . . . . . MIR548AI . . . microRNA 548ai . . . . . . . . . . . MIR548AJ1 . . . microRNA 548aj-1 . . . . . . . . . . . MIR548AJ2 . . . microRNA 548aj-2 . . . . . . . . . . . MIR548AK . . . microRNA 548ak . . . . . . . . . . . MIR548AL . . . microRNA 548al . . . . . . . . . . . MIR548AM . . . microRNA 548am . . . . . . . . . . . MIR548AN . . . microRNA 548an . . . . . . . . . . . MIR548AO . . . microRNA 548ao . . . . . . . . . . . MIR548AP . . . microRNA 548ap . . . . . . . . . . . MIR548AQ . . . microRNA 548aq . . . . . . . . . . . MIR548AR . . . microRNA 548ar . . . . . . . . . . . MIR548AS . . . microRNA 548as . . . . . . . . . . . MIR548AT . . . microRNA 548at . . . . . . . . . . . MIR548AU . . . microRNA 548au . . . . . . . . . . . MIR548AV . . . microRNA 548av . . . . . . . . . . . MIR548AW . . . microRNA 548aw . . . . . . . . . . . MIR548AX . . . microRNA 548ax . . . . . . . . . . . MIR548AY . . . microRNA 548ay . . . . . . . . . . . MIR548AZ . . . microRNA 548az . . . . . . . . . . . MIR548B . . . microRNA 548b . . . . . . . . . . . MIR548BA . . . microRNA 548ba . . . . . . . . . . . MIR548BB . . . microRNA 548bb . . . . . . . . . . . MIR548C . . . microRNA 548c . . . . . . . . . . . MIR548D1 . . . microRNA 548d-1 . . . . . . . . . . . MIR548D2 . . . microRNA 548d-2 . . . . . . . . . . . MIR548E . . . microRNA 548e . . . . . . . . . . . MIR548F1 . . . microRNA 548f-1 . . . . . . . . . . . MIR548F2 . . . microRNA 548f-2 . . . . . . . . . . . MIR548F3 . . . microRNA 548f-3 . . . . . . . . . . . MIR548F4 . . . microRNA 548f-4 . . . . . . . . . . . MIR548F5 . . . microRNA 548f-5 . . . . . . . . . . . MIR548G . . . microRNA 548g . . . . . . . . . . . MIR548H1 . . . microRNA 548h-1 . . . . . . . . . . . MIR548H2 . . . microRNA 548h-2 . . . . . . . . . . . MIR548H3 . . . microRNA 548h-3 . . . . . . . . . . . MIR548H4 . . . microRNA 548h-4 . . . . . . . . . . . MIR548H5 . . . microRNA 548h-5 . . . . . . . . . . . MIR548I1 . . . microRNA 548i-1 . . . . . . . . . . . MIR548I2 . . . microRNA 548i-2 . . . . . . . . . . . MIR548I3 . . . microRNA 548i-3 . . . . . . . . . . . MIR548I4 . . . microRNA 548i-4 . . . . . . . . . . . MIR548J . . . microRNA 548j . . . . . . . . . . . MIR548K . . . microRNA 548k . . . . . . . . . . . MIR548L . . . microRNA 548l . . . . . . . . . . . MIR548M . . . microRNA 548m . . . . . . . . . . . MIR548N . . . microRNA 548n . . . . . . . . . . . MIR548O . . . microRNA 548o . . . . . . . . . . . MIR548O2 . . . microRNA 548o-2 . . . . . . . . . . . MIR548P . . . microRNA 548p . . . . . . . . . . . MIR548Q . . . microRNA 548q . . . . . . . . . . . MIR548S . . . microRNA 548s . . . . . . . . . . . MIR548T . . . microRNA 548t . . . . . . . . . . . MIR548U . . . microRNA 548u . . . . . . . . . . . MIR548V . . . microRNA 548v . . . . . . . . . . . MIR548W . . . microRNA 548w . . . . . . . . . . . MIR548X . . . microRNA 548x . . . . . . . . . . . MIR548X2 . . . microRNA 548x-2 . . . . . . . . . . . MIR548XHG . . . MIR548X host gene . . . . . . . . . . . MIR548Y . . . microRNA 548y . . . . . . . . . . . MIR548Z . . . microRNA 548z . . . . . . . . . . . MIR549A . . . microRNA 549a . . . . . . . . . . . MIR550A1 . . . microRNA 550a-1 . . . . . . . . . . . MIR550A2 . . . microRNA 550a-2 . . . . . . . . . . . MIR550A3 . . . microRNA 550a-3 . . . . . . . . . . . MIR550B1 . . . microRNA 550b-1 . . . . . . . . . . . MIR550B2 . . . microRNA 550b-2 . . . . . . . . . . . MIR551A . . . microRNA 551a . . . . . . . . . . . MIR551B . . . microRNA 551b . . . . . . . . . . . MIR552 . . . microRNA 552 . . . . . . . . . . . MIR553 . . . microRNA 553 . . . . . . . . . . . MIR554 . . . microRNA 554 . . . . . . . . . . . MIR555 . . . microRNA 555 . . . . . . . . . . . MIR556 . . . microRNA 556 . . . . . . . . . . . MIR557 . . . microRNA 557 . . . . . . . . . . . MIR558 . . . microRNA 558 . . . . . . . . . . . MIR559 . . . microRNA 559 . . . . . . . . . . . MIR561 . . . microRNA 561 . . . . . . . . . . . MIR562 . . . microRNA 562 . . . . . . . . . . . MIR563 . . . microRNA 563 . . . . . . . . . . . MIR564 . . . microRNA 564 . . . . . . . . . . . MIR566 . . . microRNA 566 . . . . . . . . . . . MIR567 . . . microRNA 567 . . . . . . . . . . . MIR568 . . . microRNA 568 . . . . . . . . . . . MIR569 . . . microRNA 569 . . . . . . . . . . . MIR570 . . . microRNA 570 . . . . . . . . . . . MIR571 . . . microRNA 571 . . . . . . . . . . . MIR572 . . . microRNA 572 . . . . . . . . . . . MIR573 . . . microRNA 573 . . . . . . . . . . . MIR574 . . . microRNA 574 . . . . . . . . . . . MIR575 . . . microRNA 575 . . . . . . . . . . . MIR576 . . . microRNA 576 . . . . . . . . . . . MIR577 . . . microRNA 577 . . . . . . . . . . . MIR578 . . . microRNA 578 . . . . . . . . . . . MIR579 . . . microRNA 579 . . . . . . . . . . . MIR580 . . . microRNA 580 . . . . . . . . . . . MIR581 . . . microRNA 581 . . . . . . . . . . . MIR582 . . . microRNA 582 . . . . . . . . . . . MIR583 . . . microRNA 583 . . . . . . . . . . . MIR584 . . . microRNA 584 . . . . . . . . . . . MIR585 . . . microRNA 585 . . . . . . . . . . . MIR586 . . . microRNA 586 . . . . . . . . . . . MIR587 . . . microRNA 587 . . . . . . . . . . . MIR588 . . . microRNA 588 . . . . . . . . . . . MIR589 . . . microRNA 589 . . . . . . . . . . . MIR590 . . . microRNA 590 . . . . . . . . . . . MIR591 . . . microRNA 591 . . . . . . . . . . . MIR592 . . . microRNA 592 . . . . . . . . . . . MIR593 . . . microRNA 593 . . . . . . . . . . . MIR595 . . . microRNA 595 . . . . . . . . . . . MIR596 . . . microRNA 596 . . . . . . . . . . . MIR597 . . . microRNA 597 . . . . . . . . . . . MIR598 . . . microRNA 598 . . . . . . . . . . . MIR599 . . . microRNA 599 . . . . . . . . . . . MIR600 . . . microRNA 600 . . . . . . . . . . . MIR600HG . . . MIR600 host gene . . . . . . . . . . . MIR601 . . . microRNA 601 . . . . . . . . . . . MIR602 . . . microRNA 602 . . . . . . . . . . . MIR603 . . . microRNA 603 . . . . . . . . . . . MIR604 . . . microRNA 604 . . . . . . . . . . . MIR605 . . . microRNA 605 . . . . . . . . . . . MIR606 . . . microRNA 606 . . . . . . . . . . . MIR607 . . . microRNA 607 . . . . . . . . . . . MIR608 . . . microRNA 608 . . . . . . . . . . . MIR609 . . . microRNA 609 . . . . . . . . . . . MIR610 . . . microRNA 610 . . . . . . . . . . . MIR611 . . . microRNA 611 . . . . . . . . . . . MIR612 . . . microRNA 612 . . . . . . . . . . . MIR613 . . . microRNA 613 . . . . . . . . . . . MIR614 . . . microRNA 614 . . . . . . . . . . . MIR615 . . . microRNA 615 . . . . . . . . . . . MIR616 . . . microRNA 616 . . . . . . . . . . . MIR617 . . . microRNA 617 . . . . . . . . . . . MIR618 . . . microRNA 618 . . . . . . . . . . . MIR619 . . . microRNA 619 . . . . . . . . . . . MIR620 . . . microRNA 620 . . . . . . . . . . . MIR621 . . . microRNA 621 . . . . . . . . . . . MIR622 . . . microRNA 622 . . . . . . . . . . . MIR623 . . . microRNA 623 . . . . . . . . . . . MIR624 . . . microRNA 624 . . . . . . . . . . . MIR625 . . . microRNA 625 . . . . . . . . . . . MIR626 . . . microRNA 626 . . . . . . . . . . . MIR627 . . . microRNA 627 . . . . . . . . . . . MIR628 . . . microRNA 628 . . . . . . . . . . . MIR629 . . . microRNA 629 . . . . . . . . . . . MIR630 . . . microRNA 630 . . . . . . . . . . . MIR631 . . . microRNA 631 . . . . . . . . . . . MIR632 . . . microRNA 632 . . . . . . . . . . . MIR633 . . . microRNA 633 . . . . . . . . . . . MIR634 . . . microRNA 634 . . . . . . . . . . . MIR635 . . . microRNA 635 . . . . . . . . . . . MIR636 . . . microRNA 636 . . . . . . . . . . . MIR637 . . . microRNA 637 . . . . . . . . . . . MIR638 . . . microRNA 638 . . . . . . . . . . . MIR639 . . . microRNA 639 . . . . . . . . . . . MIR640 . . . microRNA 640 . . . . . . . . . . . MIR641 . . . microRNA 641 . . . . . . . . . . . MIR642A . . . microRNA 642a . . . . . . . . . . . MIR642B . . . microRNA 642b . . . . . . . . . . . MIR643 . . . microRNA 643 . . . . . . . . . . . MIR644A . . . microRNA 644a . . . . . . . . . . . MIR645 . . . microRNA 645 . . . . . . . . . . . MIR646 . . . microRNA 646 . . . . . . . . . . . MIR646HG . . . MIR646 host gene . . . . . . . . . . . MIR647 . . . microRNA 647 . . . . . . . . . . . MIR648 . . . microRNA 648 . . . . . . . . . . . MIR649 . . . microRNA 649 . . . . . . . . . . . MIR650 . . . microRNA 650 . . . . . . . . . . . MIR651 . . . microRNA 651 . . . . . . . . . . . MIR652 . . . microRNA 652 . . . . . . . . . . . MIR653 . . . microRNA 653 . . . . . . . . . . . MIR654 . . . microRNA 654 . . . . . . . . . . . MIR655 . . . microRNA 655 . . . . . . . . . . . MIR656 . . . microRNA 656 . . . . . . . . . . . MIR657 . . . microRNA 657 . . . . . . . . . . . MIR658 . . . microRNA 658 . . . . . . . . . . . MIR659 . . . microRNA 659 . . . . . . . . . . . MIR660 . . . microRNA 660 . . . . . . . . . . . MIR661 . . . microRNA 661 . . . . . . . . . . . MIR662 . . . microRNA 662 . . . . . . . . . . . MIR663A . . . microRNA 663a . . . . . . . . . . . MIR663AHG . . . MIR663A host gene . . . . . . . . . . . MIR663B . . . microRNA 663b . . . . . . . . . . . MIR664A . . . microRNA 664a . . . . . . . . . . . MIR664B . . . microRNA 664b . . . . . . . . . . . MIR665 . . . microRNA 665 . . . . . . . . . . . MIR668 . . . microRNA 668 . . . . . . . . . . . MIR670 . . . microRNA 670 . . . . . . . . . . . MIR670HG . . . MIR670 host gene . . . . . . . . . . . MIR671 . . . microRNA 671 . . . . . . . . . . . MIR675 . . . microRNA 675 . . . . . . . . . . . MIR676 . . . microRNA 676 . . . . . . . . . . . MIR708 . . . microRNA 708 . . . . . . . . . . . MIR711 . . . microRNA 711 . . . . . . . . . . . MIR718 . . . microRNA 718 . . . . . . . . . . . MIR744 . . . microRNA 744 . . . . . . . . . . . MIR758 . . . microRNA 758 . . . . . . . . . . . MIR759 . . . microRNA 759 . . . . . . . . . . . MIR760 . . . microRNA 760 . . . . . . . . . . . MIR761 . . . microRNA 761 . . . . . . . . . . . MIR762 . . . microRNA 762 . . . . . . . . . . . MIR762HG . . . MIR762 host gene . . . . . . . . . . . MIR764 . . . microRNA 764 . . . . . . . . . . . MIR765 . . . microRNA 765 . . . . . . . . . . . MIR766 . . . microRNA 766 . . . . . . . . . . . MIR767 . . . microRNA 767 . . . . . . . . . . . MIR769 . . . microRNA 769 . . . . . . . . . . . MIR770 . . . microRNA 770 . . . . . . . . . . . MIR802 . . . microRNA 802 . . . . . . . . . . . MIR873 . . . microRNA 873 . . . . . . . . . . . MIR874 . . . microRNA 874 . . . . . . . . . . . MIR875 . . . microRNA 875 . . . . . . . . . . . MIR876 . . . microRNA 876 . . . . . . . . . . . MIR877 . . . microRNA 877 . . . . . . . . . . . MIR885 . . . microRNA 885 . . . . . . . . . . . MIR887 . . . microRNA 887 . . . . . . . . . . . MIR888 . . . microRNA 888 . . . . . . . . . . . MIR889 . . . microRNA 889 . . . . . . . . . . . MIR890 . . . microRNA 890 . . . . . . . . . . . MIR891A . . . microRNA 891a . . . . . . . . . . . MIR891B . . . microRNA 891b . . . . . . . . . . . MIR892A . . . microRNA 892a . . . . . . . . . . . MIR892B . . . microRNA 892b . . . . . . . . . . . MIR892C . . . microRNA 892c . . . . . . . . . . . MIR920 . . . microRNA 920 . . . . . . . . . . . MIR921 . . . microRNA 921 . . . . . . . . . . . MIR922 . . . microRNA 922 . . . . . . . . . . . MIR924 . . . microRNA 924 . . . . . . . . . . . MIR924HG . . . MIR924 host gene . . . . . . . . . . . MIR933 . . . microRNA 933 . . . . . . . . . . . MIR934 . . . microRNA 934 . . . . . . . . . . . MIR935 . . . microRNA 935 . . . . . . . . . . . MIR936 . . . microRNA 936 . . . . . . . . . . . MIR937 . . . microRNA 937 . . . . . . . . . . . MIR938 . . . microRNA 938 . . . . . . . . . . . MIR939 . . . microRNA 939 . . . . . . . . . . . MIR940 . . . microRNA 940 . . . . . . . . . . . MIR941-1 . . . microRNA 941-1 . . . . . . . . . . . MIR941-2 . . . microRNA 941-2 . . . . . . . . . . . MIR941-3 . . . microRNA 941-3 . . . . . . . . . . . MIR941-4 . . . microRNA 941-4 . . . . . . . . . . . MIR941-5 . . . microRNA 941-5 . . . . . . . . . . . MIR942 . . . microRNA 942 . . . . . . . . . . . MIR943 . . . microRNA 943 . . . . . . . . . . . MIR944 . . . microRNA 944 . . . . . . . . . . . MIR1178 . . . microRNA 1178 . . . . . . . . . . . MIR1179 . . . microRNA 1179 . . . . . . . . . . . MIR1180 . . . microRNA 1180 . . . . . . . . . . . MIR1181 . . . microRNA 1181 . . . . . . . . . . . MIR1182 . . . microRNA 1182 . . . . . . . . . . . MIR1183 . . . microRNA 1183 . . . . . . . . . . . MIR1184-1 . . . microRNA 1184-1 . . . . . . . . . . . MIR1184-2 . . . microRNA 1184-2 . . . . . . . . . . . MIR1184-3 . . . microRNA 1184-3 . . . . . . . . . . . MIR1185-1 . . . microRNA 1185-1 . . . . . . . . . . . MIR1185-2 . . . microRNA 1185-2 . . . . . . . . . . . MIR1193 . . . microRNA 1193 . . . . . . . . . . . MIR1197 . . . microRNA 1197 . . . . . . . . . . . MIR1199 . . . microRNA 1199 . . . . . . . . . . . MIR1200 . . . microRNA 1200 . . . . . . . . . . . MIR1202 . . . microRNA 1202 . . . . . . . . . . . MIR1203 . . . microRNA 1203 . . . . . . . . . . . MIR1204 . . . microRNA 1204 . . . . . . . . . . . MIR1205 . . . microRNA 1205 . . . . . . . . . . . MIR1206 . . . microRNA 1206 . . . . . . . . . . . MIR1207 . . . microRNA 1207 . . . . . . . . . . . MIR1208 . . . microRNA 1208 . . . . . . . . . . . MIR1224 . . . microRNA 1224 . . . . . . . . . . . MIR1225 . . . microRNA 1225 . . . . . . . . . . . MIR1226 . . . microRNA 1226 . . . . . . . . . . . MIR1227 . . . microRNA 1227 . . . . . . . . . . . MIR1228 . . . microRNA 1228 . . . . . . . . . . . MIR1229 . . . microRNA 1229 . . . . . . . . . . . MIR1231 . . . microRNA 1231 . . . . . . . . . . . MIR1233-1 . . . microRNA 1233-1 . . . . . . . . . . . MIR1233-2 . . . microRNA 1233-2 . . . . . . . . . . . MIR1234 . . . microRNA 1234 . . . . . . . . . . . MIR1236 . . . microRNA 1236 . . . . . . . . . . . MIR1237 . . . microRNA 1237 . . . . . . . . . . . MIR1238 . . . microRNA 1238 . . . . . . . . . . . MIR1243 . . . microRNA 1243 . . . . . . . . . . . MIR1244-1 . . . microRNA 1244-1 . . . . . . . . . . . MIR1244-2 . . . microRNA 1244-2 . . . . . . . . . . . MIR1244-3 . . . microRNA 1244-3 . . . . . . . . . . . MIR1244-4 . . . microRNA 1244-4 . . . . . . . . . . . MIR1245A . . . microRNA 1245a . . . . . . . . . . . MIR1245B . . . microRNA 1245b . . . . . . . . . . . MIR1246 . . . microRNA 1246 . . . . . . . . . . . MIR1247 . . . microRNA 1247 . . . . . . . . . . . MIR1248 . . . microRNA 1248 . . . . . . . . . . . MIR1249 . . . microRNA 1249 . . . . . . . . . . . MIR1250 . . . microRNA 1250 . . . . . . . . . . . MIR1251 . . . microRNA 1251 . . . . . . . . . . . MIR1252 . . . microRNA 1252 . . . . . . . . . . . MIR1253 . . . microRNA 1253 . . . . . . . . . . . MIR1254-1 . . . microRNA 1254-1 . . . . . . . . . . . MIR1254-2 . . . microRNA 1254-2 . . . . . . . . . . . MIR1255A . . . microRNA 1255a . . . . . . . . . . . MIR1255B1 . . . microRNA 1255b-1 . . . . . . . . . . . MIR1255B2 . . . microRNA 1255b-2 . . . . . . . . . . . MIR1256 . . . microRNA 1256 . . . . . . . . . . . MIR1257 . . . microRNA 1257 . . . . . . . . . . . MIR1258 . . . microRNA 1258 . . . . . . . . . . . MIR1260A . . . microRNA 1260a . . . . . . . . . . . MIR1260B . . . microRNA 1260b . . . . . . . . . . . MIR1261 . . . microRNA 1261 . . . . . . . . . . . MIR1262 . . . microRNA 1262 . . . . . . . . . . . MIR1263 . . . microRNA 1263 . . . . . . . . . . . MIR1264 . . . microRNA 1264 . . . . . . . . . . . MIR1265 . . . microRNA 1265 . . . . . . . . . . . MIR1266 . . . microRNA 1266 . . . . . . . . . . . MIR1267 . . . microRNA 1267 . . . . . . . . . . . MIR1268A . . . microRNA 1268a . . . . . . . . . . . MIR1268B . . . microRNA 1268b . . . . . . . . . . . MIR1269A . . . microRNA 1269a . . . . . . . . . . . MIR1269B . . . microRNA 1269b . . . . . . . . . . . MIR1270 . . . microRNA 1270 . . . . . . . . . . . MIR1271 . . . microRNA 1271 . . . . . . . . . . . MIR1272 . . . microRNA 1272 . . . . . . . . . . . MIR1273A . . . microRNA 1273a . . . . . . . . . . . MIR1273C . . . microRNA 1273c . . . . . . . . . . . MIR1273D . . . microRNA 1273d . . . . . . . . . . . MIR1273E . . . microRNA 1273e . . . . . . . . . . . MIR1273F . . . microRNA 1273f . . . . . . . . . . . MIR1273G . . . microRNA 1273g . . . . . . . . . . . MIR1273H . . . microRNA 1273h . . . . . . . . . . . MIR1275 . . . microRNA 1275 . . . . . . . . . . . MIR1276 . . . microRNA 1276 . . . . . . . . . . . MIR1277 . . . microRNA 1277 . . . . . . . . . . . MIR1278 . . . microRNA 1278 . . . . . . . . . . . MIR1279 . . . microRNA 1279 . . . . . . . . . . . MIR1281 . . . microRNA 1281 . . . . . . . . . . . MIR1282 . . . microRNA 1282 . . . . . . . . . . . MIR1283-1 . . . microRNA 1283-1 . . . . . . . . . . . MIR1283-2 . . . microRNA 1283-2 . . . . . . . . . . . MIR1284 . . . microRNA 1284 . . . . . . . . . . . MIR1285-1 . . . microRNA 1285-1 . . . . . . . . . . . MIR1285-2 . . . microRNA 1285-2 . . . . . . . . . . . MIR1286 . . . microRNA 1286 . . . . . . . . . . . MIR1287 . . . microRNA 1287 . . . . . . . . . . . MIR1288 . . . microRNA 1288 . . . . . . . . . . . MIR1289-1 . . . microRNA 1289-1 . . . . . . . . . . . MIR1289-2 . . . microRNA 1289-2 . . . . . . . . . . . MIR1290 . . . microRNA 1290 . . . . . . . . . . . MIR1291 . . . microRNA 1291 . . . . . . . . . . . MIR1292 . . . microRNA 1292 . . . . . . . . . . . MIR1293 . . . microRNA 1293 . . . . . . . . . . . MIR1294 . . . microRNA 1294 . . . . . . . . . . . MIR1295A . . . microRNA 1295a . . . . . . . . . . . MIR1295B . . . microRNA 1295b . . . . . . . . . . . MIR1296 . . . microRNA 1296 . . . . . . . . . . . MIR1297 . . . microRNA 1297 . . . . . . . . . . . MIR1298 . . . microRNA 1298 . . . . . . . . . . . MIR1299 . . . microRNA 1299 . . . . . . . . . . . MIR1301 . . . microRNA 1301 . . . . . . . . . . . MIR1302-1 . . . microRNA 1302-1 . . . . . . . . . . . MIR1302-2 . . . microRNA 1302-2 . . . . . . . . . . . MIR1302-3 . . . microRNA 1302-3 . . . . . . . . . . . MIR1302-4 . . . microRNA 1302-4 . . . . . . . . . . . MIR1302-5 . . . microRNA 1302-5 . . . . . . . . . . . MIR1302-6 . . . microRNA 1302-6 . . . . . . . . . . . MIR1302-7 . . . microRNA 1302-7 . . . . . . . . . . . MIR1302-8 . . . microRNA 1302-8 . . . . . . . . . . . MIR1302-9 . . . microRNA 1302-9 . . . . . . . . . . . MIR1302-10 . . . microRNA 1302-10 . . . . . . . . . . . MIR1302-11 . . . microRNA 1302-11 . . . . . . . . . . . MIR1303 . . . microRNA 1303 . . . . . . . . . . . MIR1304 . . . microRNA 1304 . . . . . . . . . . . MIR1305 . . . microRNA 1305 . . . . . . . . . . . MIR1306 . . . microRNA 1306 . . . . . . . . . . . MIR1307 . . . microRNA 1307 . . . . . . . . . . . MIR1321 . . . microRNA 1321 . . . . . . . . . . . MIR1322 . . . microRNA 1322 . . . . . . . . . . . MIR1323 . . . microRNA 1323 . . . . . . . . . . . MIR1324 . . . microRNA 1324 . . . . . . . . . . . MIR1343 . . . microRNA 1343 . . . . . . . . . . . MIR1468 . . . microRNA 1468 . . . . . . . . . . . MIR1469 . . . microRNA 1469 . . . . . . . . . . . MIR1470 . . . microRNA 1470 . . . . . . . . . . . MIR1471 . . . microRNA 1471 . . . . . . . . . . . MIR1537 . . . microRNA 1537 . . . . . . . . . . . MIR1538 . . . microRNA 1538 . . . . . . . . . . . MIR1539 . . . microRNA 1539 . . . . . . . . . . . MIR1587 . . . microRNA 1587 . . . . . . . . . . . MIR1825 . . . microRNA 1825 . . . . . . . . . . . MIR1827 . . . microRNA 1827 . . . . . . . . . . . MIR1908 . . . microRNA 1908 . . . . . . . . . . . MIR1909 . . . microRNA 1909 . . . . . . . . . . . MIR1910 . . . microRNA 1910 . . . . . . . . . . . MIR1911 . . . microRNA 1911 . . . . . . . . . . . MIR1912 . . . microRNA 1912 . . . . . . . . . . . MIR1913 . . . microRNA 1913 . . . . . . . . . . . MIR1914 . . . microRNA 1914 . . . . . . . . . . . MIR1915 . . . microRNA 1915 . . . . . . . . . . . MIR1972-1 . . . microRNA 1972-1 . . . . . . . . . . . MIR1972-2 . . . microRNA 1972-2 . . . . . . . . . . . MIR1973 . . . microRNA 1973 . . . . . . . . . . . MIR1976 . . . microRNA 1976 . . . . . . . . . . . MIR2052 . . . microRNA 2052 . . . . . . . . . . . MIR2052HG . . . MIR2052 host gene . . . . . . . . . . . MIR2053 . . . microRNA 2053 . . . . . . . . . . . MIR2054 . . . microRNA 2054 . . . . . . . . . . . MIR2110 . . . microRNA 2110 . . . . . . . . . . . MIR2113 . . . microRNA 2113 . . . . . . . . . . . MIR2114 . . . microRNA 2114 . . . . . . . . . . . MIR2115 . . . microRNA 2115 . . . . . . . . . . . MIR2116 . . . microRNA 2116 . . . . . . . . . . . MIR2117 . . . microRNA 2117 . . . . . . . . . . . MIR2117HG . . . MIR2117 host gene . . . . . . . . . . . MIR2276 . . . microRNA 2276 . . . . . . . . . . . MIR2277 . . . microRNA 2277 . . . . . . . . . . . MIR2278 . . . microRNA 2278 . . . . . . . . . . . MIR2355 . . . microRNA 2355 . . . . . . . . . . . MIR2392 . . . microRNA 2392 . . . . . . . . . . . MIR2467 . . . microRNA 2467 . . . . . . . . . . . MIR2681 . . . microRNA 2681 . . . . . . . . . . . MIR2682 . . . microRNA 2682 . . . . . . . . . . . MIR2861 . . . microRNA 2861 . . . . . . . . . . . MIR2909 . . . microRNA 2909 . . . . . . . . . . . MIR3064 . . . microRNA 3064 . . . . . . . . . . . MIR3065 . . . microRNA 3065 . . . . . . . . . . . MIR3074 . . . microRNA 3074 . . . . . . . . . . . MIR3115 . . . microRNA 3115 . . . . . . . . . . . MIR3116-1 . . . microRNA 3116-1 . . . . . . . . . . . MIR3116-2 . . . microRNA 3116-2 . . . . . . . . . . . MIR3117 . . . microRNA 3117 . . . . . . . . . . . MIR3118-1 . . . microRNA 3118-1 . . . . . . . . . . . MIR3118-2 . . . microRNA 3118-2 . . . . . . . . . . . MIR3118-3 . . . microRNA 3118-3 . . . . . . . . . . . MIR3118-4 . . . microRNA 3118-4 . . . . . . . . . . . MIR3119-1 . . . microRNA 3119-1 . . . . . . . . . . . MIR3119-2 . . . microRNA 3119-2 . . . . . . . . . . . MIR3120 . . . microRNA 3120 . . . . . . . . . . . MIR3121 . . . microRNA 3121 . . . . . . . . . . . MIR3122 . . . microRNA 3122 . . . . . . . . . . . MIR3123 . . . microRNA 3123 . . . . . . . . . . . MIR3124 . . . microRNA 3124 . . . . . . . . . . . MIR3125 . . . microRNA 3125 . . . . . . . . . . . MIR3126 . . . microRNA 3126 . . . . . . . . . . . MIR3127 . . . microRNA 3127 . . . . . . . . . . . MIR3128 . . . microRNA 3128 . . . . . . . . . . . MIR3129 . . . microRNA 3129 . . . . . . . . . . . MIR3130-1 . . . microRNA 3130-1 . . . . . . . . . . . MIR3130-2 . . . microRNA 3130-2 . . . . . . . . . . . MIR3131 . . . microRNA 3131 . . . . . . . . . . . MIR3132 . . . microRNA 3132 . . . . . . . . . . . MIR3133 . . . microRNA 3133 . . . . . . . . . . . MIR3134 . . . microRNA 3134 . . . . . . . . . . . MIR3135A . . . microRNA 3135a . . . . . . . . . . . MIR3135B . . . microRNA 3135b . . . . . . . . . . . MIR3136 . . . microRNA 3136 . . . . . . . . . . . MIR3137 . . . microRNA 3137 . . . . . . . . . . . MIR3138 . . . microRNA 3138 . . . . . . . . . . . MIR3139 . . . microRNA 3139 . . . . . . . . . . . MIR3140 . . . microRNA 3140 . . . . . . . . . . . MIR3141 . . . microRNA 3141 . . . . . . . . . . . MIR3142 . . . microRNA 3142 . . . . . . . . . . . MIR3142HG . . . MIR3142 host gene . . . . . . . . . . . MIR3143 . . . microRNA 3143 . . . . . . . . . . . MIR3144 . . . microRNA 3144 . . . . . . . . . . . MIR3145 . . . microRNA 3145 . . . . . . . . . . . MIR3146 . . . microRNA 3146 . . . . . . . . . . . MIR3147 . . . microRNA 3147 . . . . . . . . . . . MIR3148 . . . microRNA 3148 . . . . . . . . . . . MIR3149 . . . microRNA 3149 . . . . . . . . . . . MIR3150A . . . microRNA 3150a . . . . . . . . . . . MIR3150B . . . microRNA 3150b . . . . . . . . . . . MIR3151 . . . microRNA 3151 . . . . . . . . . . . MIR3152 . . . microRNA 3152 . . . . . . . . . . . MIR3153 . . . microRNA 3153 . . . . . . . . . . . MIR3154 . . . microRNA 3154 . . . . . . . . . . . MIR3155A . . . microRNA 3155a . . . . . . . . . . . MIR3155B . . . microRNA 3155b . . . . . . . . . . . MIR3156-1 . . . microRNA 3156-1 . . . . . . . . . . . MIR3156-2 . . . microRNA 3156-2 . . . . . . . . . . . MIR3156-3 . . . microRNA 3156-3 . . . . . . . . . . . MIR3157 . . . microRNA 3157 . . . . . . . . . . . MIR3158-1 . . . microRNA 3158-1 . . . . . . . . . . . MIR3158-2 . . . microRNA 3158-2 . . . . . . . . . . . MIR3159 . . . microRNA 3159 . . . . . . . . . . . MIR3160-1 . . . microRNA 3160-1 . . . . . . . . . . . MIR3160-2 . . . microRNA 3160-2 . . . . . . . . . . . MIR3161 . . . microRNA 3161 . . . . . . . . . . . MIR3162 . . . microRNA 3162 . . . . . . . . . . . MIR3163 . . . microRNA 3163 . . . . . . . . . . . MIR3164 . . . microRNA 3164 . . . . . . . . . . . MIR3165 . . . microRNA 3165 . . . . . . . . . . . MIR3166 . . . microRNA 3166 . . . . . . . . . . . MIR3167 . . . microRNA 3167 . . . . . . . . . . . MIR3168 . . . microRNA 3168 . . . . . . . . . . . MIR3169 . . . microRNA 3169 . . . . . . . . . . . MIR3170 . . . microRNA 3170 . . . . . . . . . . . MIR3171 . . . microRNA 3171 . . . . . . . . . . . MIR3173 . . . microRNA 3173 . . . . . . . . . . . MIR3174 . . . microRNA 3174 . . . . . . . . . . . MIR3175 . . . microRNA 3175 . . . . . . . . . . . MIR3176 . . . microRNA 3176 . . . . . . . . . . . MIR3177 . . . microRNA 3177 . . . . . . . . . . . MIR3178 . . . microRNA 3178 . . . . . . . . . . . MIR3179-1 . . . microRNA 3179-1 . . . . . . . . . . . MIR3179-2 . . . microRNA 3179-2 . . . . . . . . . . . MIR3179-3 . . . microRNA 3179-3 . . . . . . . . . . . MIR3179-4 . . . microRNA 3179-4 . . . . . . . . . . . MIR3180-1 . . . microRNA 3180-1 . . . . . . . . . . . MIR3180-2 . . . microRNA 3180-2 . . . . . . . . . . . MIR3180-3 . . . microRNA 3180-3 . . . . . . . . . . . MIR3180-4 . . . microRNA 3180-4 . . . . . . . . . . . MIR3180-5 . . . microRNA 3180-5 . . . . . . . . . . . MIR3181 . . . microRNA 3181 . . . . . . . . . . . MIR3182 . . . microRNA 3182 . . . . . . . . . . . MIR3183 . . . microRNA 3183 . . . . . . . . . . . MIR3184 . . . microRNA 3184 . . . . . . . . . . . MIR3185 . . . microRNA 3185 . . . . . . . . . . . MIR3186 . . . microRNA 3186 . . . . . . . . . . . MIR3187 . . . microRNA 3187 . . . . . . . . . . . MIR3188 . . . microRNA 3188 . . . . . . . . . . . MIR3189 . . . microRNA 3189 . . . . . . . . . . . MIR3190 . . . microRNA 3190 . . . . . . . . . . . MIR3191 . . . microRNA 3191 . . . . . . . . . . . MIR3192 . . . microRNA 3192 . . . . . . . . . . . MIR3193 . . . microRNA 3193 . . . . . . . . . . . MIR3194 . . . microRNA 3194 . . . . . . . . . . . MIR3195 . . . microRNA 3195 . . . . . . . . . . . MIR3196 . . . microRNA 3196 . . . . . . . . . . . MIR3197 . . . microRNA 3197 . . . . . . . . . . . MIR3198-1 . . . microRNA 3198-1 . . . . . . . . . . . MIR3198-2 . . . microRNA 3198-2 . . . . . . . . . . . MIR3199-1 . . . microRNA 3199-1 . . . . . . . . . . . MIR3199-2 . . . microRNA 3199-2 . . . . . . . . . . . MIR3200 . . . microRNA 3200 . . . . . . . . . . . MIR3201 . . . microRNA 3201 . . . . . . . . . . . MIR3202-1 . . . microRNA 3202-1 . . . . . . . . . . . MIR3202-2 . . . microRNA 3202-2 . . . . . . . . . . . MIR3529 . . . microRNA 3529 . . . . . . . . . . . MIR3591 . . . microRNA 3591 . . . . . . . . . . . MIR3605 . . . microRNA 3605 . . . . . . . . . . . MIR3606 . . . microRNA 3606 . . . . . . . . . . . MIR3607 . . . microRNA 3607 . . . . . . . . . . . MIR3609 . . . microRNA 3609 . . . . . . . . . . . MIR3610 . . . microRNA 3610 . . . . . . . . . . . MIR3611 . . . microRNA 3611 . . . . . . . . . . . MIR3612 . . . microRNA 3612 . . . . . . . . . . . MIR3613 . . . microRNA 3613 . . . . . . . . . . . MIR3614 . . . microRNA 3614 . . . . . . . . . . . MIR3615 . . . microRNA 3615 . . . . . . . . . . . MIR3616 . . . microRNA 3616 . . . . . . . . . . . MIR3617 . . . microRNA 3617 . . . . . . . . . . . MIR3618 . . . microRNA 3618 . . . . . . . . . . . MIR3619 . . . microRNA 3619 . . . . . . . . . . . MIR3620 . . . microRNA 3620 . . . . . . . . . . . MIR3621 . . . microRNA 3621 . . . . . . . . . . . MIR3622A . . . microRNA 3622a . . . . . . . . . . . MIR3622B . . . microRNA 3622b . . . . . . . . . . . MIR3646 . . . microRNA 3646 . . . . . . . . . . . MIR3648-1 . . . microRNA 3648-1 . . . . . . . . . . . MIR3648-2 . . . microRNA 3648-2 . . . . . . . . . . . MIR3649 . . . microRNA 3649 . . . . . . . . . . . MIR3650 . . . microRNA 3650 . . . . . . . . . . . MIR3651 . . . microRNA 3651 . . . . . . . . . . . MIR3652 . . . microRNA 3652 . . . . . . . . . . . MIR3653 . . . microRNA 3653 . . . . . . . . . . . MIR3654 . . . microRNA 3654 . . . . . . . . . . . MIR3655 . . . microRNA 3655 . . . . . . . . . . . MIR3656 . . . microRNA 3656 . . . . . . . . . . . MIR3657 . . . microRNA 3657 . . . . . . . . . . . MIR3658 . . . microRNA 3658 . . . . . . . . . . . MIR3659 . . . microRNA 3659 . . . . . . . . . . . MIR3660 . . . microRNA 3660 . . . . . . . . . . . MIR3661 . . . microRNA 3661 . . . . . . . . . . . MIR3662 . . . microRNA 3662 . . . . . . . . . . . MIR3663 . . . microRNA 3663 . . . . . . . . . . . MIR3663HG . . . MIR3663 host gene . . . . . . . . . . . MIR3664 . . . microRNA 3664 . . . . . . . . . . . MIR3665 . . . microRNA 3665 . . . . . . . . . . . MIR3666 . . . microRNA 3666 . . . . . . . . . . . MIR3667 . . . microRNA 3667 . . . . . . . . . . . MIR3668 . . . microRNA 3668 . . . . . . . . . . . MIR3670-1 . . . microRNA 3670-1 . . . . . . . . . . . MIR3670-2 . . . microRNA 3670-2 . . . . . . . . . . . MIR3670-3 . . . microRNA 3670-3 . . . . . . . . . . . MIR3670-4 . . . microRNA 3670-4 . . . . . . . . . . . MIR3671 . . . microRNA 3671 . . . . . . . . . . . MIR3672 . . . microRNA 3672 . . . . . . . . . . . MIR3674 . . . microRNA 3674 . . . . . . . . . . . MIR3675 . . . microRNA 3675 . . . . . . . . . . . MIR3677 . . . microRNA 3677 . . . . . . . . . . . MIR3678 . . . microRNA 3678 . . . . . . . . . . . MIR3679 . . . microRNA 3679 . . . . . . . . . . . MIR3680-1 . . . microRNA 3680-1 . . . . . . . . . . . MIR3680-2 . . . microRNA 3680-2 . . . . . . . . . . . MIR3681 . . . microRNA 3681 . . . . . . . . . . . MIR3681HG . . . MIR3681 host gene . . . . . . . . . . . MIR3682 . . . microRNA 3682 . . . . . . . . . . . MIR3683 . . . microRNA 3683 . . . . . . . . . . . MIR3684 . . . microRNA 3684 . . . . . . . . . . . MIR3685 . . . microRNA 3685 . . . . . . . . . . . MIR3686 . . . microRNA 3686 . . . . . . . . . . . MIR3687-1 . . . microRNA 3687-1 . . . . . . . . . . . MIR3687-2 . . . microRNA 3687-2 . . . . . . . . . . . MIR3688-1 . . . microRNA 3688-1 . . . . . . . . . . . MIR3688-2 . . . microRNA 3688-2 . . . . . . . . . . . MIR3689A . . . microRNA 3689a . . . . . . . . . . . MIR3689B . . . microRNA 3689b . . . . . . . . . . . MIR3689C . . . microRNA 3689c . . . . . . . . . . . MIR3689D1 . . . microRNA 3689d-1 . . . . . . . . . . . MIR3689D2 . . . microRNA 3689d-2 . . . . . . . . . . . MIR3689E . . . microRNA 3689e . . . . . . . . . . . MIR3689F . . . microRNA 3689f . . . . . . . . . . . MIR3690 . . . microRNA 3690 . . . . . . . . . . . MIR3691 . . . microRNA 3691 . . . . . . . . . . . MIR3692 . . . microRNA 3692 . . . . . . . . . . . MIR3713 . . . microRNA 3713 . . . . . . . . . . . MIR3714 . . . microRNA 3714 . . . . . . . . . . . MIR3907 . . . microRNA 3907 . . . . . . . . . . . MIR3908 . . . microRNA 3908 . . . . . . . . . . . MIR3909 . . . microRNA 3909 . . . . . . . . . . . MIR3910-1 . . . microRNA 3910-1 . . . . . . . . . . . MIR3910-2 . . . microRNA 3910-2 . . . . . . . . . . . MIR3911 . . . microRNA 3911 . . . . . . . . . . . MIR3912 . . . microRNA 3912 . . . . . . . . . . . MIR3913-1 . . . microRNA 3913-1 . . . . . . . . . . . MIR3913-2 . . . microRNA 3913-2 . . . . . . . . . . . MIR3914-1 . . . microRNA 3914-1 . . . . . . . . . . . MIR3914-2 . . . microRNA 3914-2 . . . . . . . . . . . MIR3915 . . . microRNA 3915 . . . . . . . . . . . MIR3916 . . . microRNA 3916 . . . . . . . . . . . MIR3917 . . . microRNA 3917 . . . . . . . . . . . MIR3918 . . . microRNA 3918 . . . . . . . . . . . MIR3919 . . . microRNA 3919 . . . . . . . . . . . MIR3920 . . . microRNA 3920 . . . . . . . . . . . MIR3921 . . . microRNA 3921 . . . . . . . . . . . MIR3922 . . . microRNA 3922 . . . . . . . . . . . MIR3923 . . . microRNA 3923 . . . . . . . . . . . MIR3924 . . . microRNA 3924 . . . . . . . . . . . MIR3925 . . . microRNA 3925 . . . . . . . . . . . MIR3926-1 . . . microRNA 3926-1 . . . . . . . . . . . MIR3926-2 . . . microRNA 3926-2 . . . . . . . . . . . MIR3927 . . . microRNA 3927 . . . . . . . . . . . MIR3928 . . . microRNA 3928 . . . . . . . . . . . MIR3929 . . . microRNA 3929 . . . . . . . . . . . MIR3934 . . . microRNA 3934 . . . . . . . . . . . MIR3935 . . . microRNA 3935 . . . . . . . . . . . MIR3936 . . . microRNA 3936 . . . . . . . . . . . MIR3937 . . . microRNA 3937 . . . . . . . . . . . MIR3938 . . . microRNA 3938 . . . . . . . . . . . MIR3939 . . . microRNA 3939 . . . . . . . . . . . MIR3940 . . . microRNA 3940 . . . . . . . . . . . MIR3941 . . . microRNA 3941 . . . . . . . . . . . MIR3942 . . . microRNA 3942 . . . . . . . . . . . MIR3943 . . . microRNA 3943 . . . . . . . . . . . MIR3944 . . . microRNA 3944 . . . . . . . . . . . MIR3945 . . . microRNA 3945 . . . . . . . . . . . MIR3945HG . . . MIR3945 host gene . . . . . . . . . . . MIR3960 . . . microRNA 3960 . . . . . . . . . . . MIR3972 . . . microRNA 3972 . . . . . . . . . . . MIR3973 . . . microRNA 3973 . . . . . . . . . . . MIR3974 . . . microRNA 3974 . . . . . . . . . . . MIR3975 . . . microRNA 3975 . . . . . . . . . . . MIR3976 . . . microRNA 3976 . . . . . . . . . . . MIR3976HG . . . MIR3976 host gene . . . . . . . . . . . MIR3977 . . . microRNA 3977 . . . . . . . . . . . MIR3978 . . . microRNA 3978 . . . . . . . . . . . MIR4251 . . . microRNA 4251 . . . . . . . . . . . MIR4252 . . . microRNA 4252 . . . . . . . . . . . MIR4253 . . . microRNA 4253 . . . . . . . . . . . MIR4254 . . . microRNA 4254 . . . . . . . . . . . MIR4255 . . . microRNA 4255 . . . . . . . . . . . MIR4256 . . . microRNA 4256 . . . . . . . . . . . MIR4257 . . . microRNA 4257 . . . . . . . . . . . MIR4258 . . . microRNA 4258 . . . . . . . . . . . MIR4259 . . . microRNA 4259 . . . . . . . . . . . MIR4260 . . . microRNA 4260 . . . . . . . . . . . MIR4261 . . . microRNA 4261 . . . . . . . . . . . MIR4262 . . . microRNA 4262 . . . . . . . . . . . MIR4263 . . . microRNA 4263 . . . . . . . . . . . MIR4264 . . . microRNA 4264 . . . . . . . . . . . MIR4265 . . . microRNA 4265 . . . . . . . . . . . MIR4266 . . . microRNA 4266 . . . . . . . . . . . MIR4267 . . . microRNA 4267 . . . . . . . . . . . MIR4268 . . . microRNA 4268 . . . . . . . . . . . MIR4269 . . . microRNA 4269 . . . . . . . . . . . MIR4270 . . . microRNA 4270 . . . . . . . . . . . MIR4271 . . . microRNA 4271 . . . . . . . . . . . MIR4272 . . . microRNA 4272 . . . . . . . . . . . MIR4273 . . . microRNA 4273 . . . . . . . . . . . MIR4274 . . . microRNA 4274 . . . . . . . . . . . MIR4275 . . . microRNA 4275 . . . . . . . . . . . MIR4276 . . . microRNA 4276 . . . . . . . . . . . MIR4277 . . . microRNA 4277 . . . . . . . . . . . MIR4278 . . . microRNA 4278 . . . . . . . . . . . MIR4279 . . . microRNA 4279 . . . . . . . . . . . MIR4280 . . . microRNA 4280 . . . . . . . . . . . MIR4281 . . . microRNA 4281 . . . . . . . . . . . MIR4282 . . . microRNA 4282 . . . . . . . . . . . MIR4283-1 . . . microRNA 4283-1 . . . . . . . . . . . MIR4283-2 . . . microRNA 4283-2 . . . . . . . . . . . MIR4284 . . . microRNA 4284 . . . . . . . . . . . MIR4285 . . . microRNA 4285 . . . . . . . . . . . MIR4286 . . . microRNA 4286 . . . . . . . . . . . MIR4287 . . . microRNA 4287 . . . . . . . . . . . MIR4288 . . . microRNA 4288 . . . . . . . . . . . MIR4289 . . . microRNA 4289 . . . . . . . . . . . MIR4290 . . . microRNA 4290 . . . . . . . . . . . MIR4290HG . . . MIR4290 host gene . . . . . . . . . . . MIR4291 . . . microRNA 4291 . . . . . . . . . . . MIR4292 . . . microRNA 4292 . . . . . . . . . . . MIR4293 . . . microRNA 4293 . . . . . . . . . . . MIR4294 . . . microRNA 4294 . . . . . . . . . . . MIR4295 . . . microRNA 4295 . . . . . . . . . . . MIR4296 . . . microRNA 4296 . . . . . . . . . . . MIR4297 . . . microRNA 4297 . . . . . . . . . . . MIR4298 . . . microRNA 4298 . . . . . . . . . . . MIR4299 . . . microRNA 4299 . . . . . . . . . . . MIR4300 . . . microRNA 4300 . . . . . . . . . . . MIR4300HG . . . MIR4300 host gene . . . . . . . . . . . MIR4301 . . . microRNA 4301 . . . . . . . . . . . MIR4302 . . . microRNA 4302 . . . . . . . . . . . MIR4303 . . . microRNA 4303 . . . . . . . . . . . MIR4304 . . . microRNA 4304 . . . . . . . . . . . MIR4305 . . . microRNA 4305 . . . . . . . . . . . MIR4306 . . . microRNA 4306 . . . . . . . . . . . MIR4307 . . . microRNA 4307 . . . . . . . . . . . MIR4307HG . . . MIR4307 host gene . . . . . . . . . . . MIR4308 . . . microRNA 4308 . . . . . . . . . . . MIR4309 . . . microRNA 4309 . . . . . . . . . . . MIR4310 . . . microRNA 4310 . . . . . . . . . . . MIR4311 . . . microRNA 4311 . . . . . . . . . . . MIR4312 . . . microRNA 4312 . . . . . . . . . . . MIR4313 . . . microRNA 4313 . . . . . . . . . . . MIR4314 . . . microRNA 4314 . . . . . . . . . . . MIR4315-1 . . . microRNA 4315-1 . . . . . . . . . . . MIR4315-2 . . . microRNA 4315-2 . . . . . . . . . . . MIR4316 . . . microRNA 4316 . . . . . . . . . . . MIR4317 . . . microRNA 4317 . . . . . . . . . . . MIR4318 . . . microRNA 4318 . . . . . . . . . . . MIR4319 . . . microRNA 4319 . . . . . . . . . . . MIR4320 . . . microRNA 4320 . . . . . . . . . . . MIR4321 . . . microRNA 4321 . . . . . . . . . . . MIR4322 . . . microRNA 4322 . . . . . . . . . . . MIR4323 . . . microRNA 4323 . . . . . . . . . . . MIR4324 . . . microRNA 4324 . . . . . . . . . . . MIR4325 . . . microRNA 4325 . . . . . . . . . . . MIR4326 . . . microRNA 4326 . . . . . . . . . . . MIR4327 . . . microRNA 4327 . . . . . . . . . . . MIR4328 . . . microRNA 4328 . . . . . . . . . . . MIR4329 . . . microRNA 4329 . . . . . . . . . . . MIR4330 . . . microRNA 4330 . . . . . . . . . . . MIR4417 . . . microRNA 4417 . . . . . . . . . . . MIR4418 . . . microRNA 4418 . . . . . . . . . . . MIR4419A . . . microRNA 4419a . . . . . . . . . . . MIR4419B . . . microRNA 4419b . . . . . . . . . . . MIR4420 . . . microRNA 4420 . . . . . . . . . . . MIR4421 . . . microRNA 4421 . . . . . . . . . . . MIR4422 . . . microRNA 4422 . . . . . . . . . . . MIR4423 . . . microRNA 4423 . . . . . . . . . . . MIR4424 . . . microRNA 4424 . . . . . . . . . . . MIR4425 . . . microRNA 4425 . . . . . . . . . . . MIR4426 . . . microRNA 4426 . . . . . . . . . . . MIR4427 . . . microRNA 4427 . . . . . . . . . . . MIR4428 . . . microRNA 4428 . . . . . . . . . . . MIR4429 . . . microRNA 4429 . . . . . . . . . . . MIR4430 . . . microRNA 4430 . . . . . . . . . . . MIR4431 . . . microRNA 4431 . . . . . . . . . . . MIR4432 . . . microRNA 4432 . . . . . . . . . . . MIR4432HG . . . MIR4432 host gene . . . . . . . . . . . MIR4433A . . . microRNA 4433a . . . . . . . . . . . MIR4433B . . . microRNA 4433b . . . . . . . . . . . MIR4434 . . . microRNA 4434 . . . . . . . . . . . MIR4435-1 . . . microRNA 4435-1 . . . . . . . . . . . MIR4435-2 . . . microRNA 4435-2 . . . . . . . . . . . MIR4435-2HG . . . MIR4435-2 host gene . . . . . 0.07288 . . . . . MIR4436A . . . microRNA 4436a . . . . . . . . . . . MIR4436B1 . . . microRNA 4436b-1 . . . . . . . . . . . MIR4436B2 . . . microRNA 4436b-2 . . . . . . . . . . . MIR4437 . . . microRNA 4437 . . . . . . . . . . . MIR4438 . . . microRNA 4438 . . . . . . . . . . . MIR4439 . . . microRNA 4439 . . . . . . . . . . . MIR4440 . . . microRNA 4440 . . . . . . . . . . . MIR4441 . . . microRNA 4441 . . . . . . . . . . . MIR4442 . . . microRNA 4442 . . . . . . . . . . . MIR4443 . . . microRNA 4443 . . . . . . . . . . . MIR4444-1 . . . microRNA 4444-1 . . . . . . . . . . . MIR4444-2 . . . microRNA 4444-2 . . . . . . . . . . . MIR4445 . . . microRNA 4445 . . . . . . . . . . . MIR4446 . . . microRNA 4446 . . . . . . . . . . . MIR4447 . . . microRNA 4447 . . . . . . . . . . . MIR4448 . . . microRNA 4448 . . . . . . . . . . . MIR4449 . . . microRNA 4449 . . . . . . . . . . . MIR4450 . . . microRNA 4450 . . . . . . . . . . . MIR4451 . . . microRNA 4451 . . . . . . . . . . . MIR4452 . . . microRNA 4452 . . . . . . . . . . . MIR4453 . . . microRNA 4453 . . . . . . . . . . . MIR4454 . . . microRNA 4454 . . . . . . . . . . . MIR4455 . . . microRNA 4455 . . . . . . . . . . . MIR4456 . . . microRNA 4456 . . . . . . . . . . . MIR4457 . . . microRNA 4457 . . . . . . . . . . . MIR4458 . . . microRNA 4458 . . . . . . . . . . . MIR4458HG . . . MIR4458 host gene . . . . . . . . . . . MIR4459 . . . microRNA 4459 . . . . . . . . . . . MIR4460 . . . microRNA 4460 . . . . . . . . . . . MIR4461 . . . microRNA 4461 . . . . . . . . . . . MIR4462 . . . microRNA 4462 . . . . . . . . . . . MIR4463 . . . microRNA 4463 . . . . . . . . . . . MIR4464 . . . microRNA 4464 . . . . . . . . . . . MIR4465 . . . microRNA 4465 . . . . . . . . . . . MIR4466 . . . microRNA 4466 . . . . . . . . . . . MIR4467 . . . microRNA 4467 . . . . . . . . . . . MIR4468 . . . microRNA 4468 . . . . . . . . . . . MIR4469 . . . microRNA 4469 . . . . . . . . . . . MIR4470 . . . microRNA 4470 . . . . . . . . . . . MIR4471 . . . microRNA 4471 . . . . . . . . . . . MIR4472-1 . . . microRNA 4472-1 . . . . . . . . . . . MIR4472-2 . . . microRNA 4472-2 . . . . . . . . . . . MIR4473 . . . microRNA 4473 . . . . . . . . . . . MIR4474 . . . microRNA 4474 . . . . . . . . . . . MIR4475 . . . microRNA 4475 . . . . . . . . . . . MIR4476 . . . microRNA 4476 . . . . . . . . . . . MIR4477A . . . microRNA 4477a . . . . . . . . . . . MIR4477B . . . microRNA 4477b . . . . . . . . . . . MIR4478 . . . microRNA 4478 . . . . . . . . . . . MIR4479 . . . microRNA 4479 . . . . . . . . . . . MIR4480 . . . microRNA 4480 . . . . . . . . . . . MIR4481 . . . microRNA 4481 . . . . . . . . . . . MIR4482 . . . microRNA 4482 . . . . . . . . . . . MIR4483 . . . microRNA 4483 . . . . . . . . . . . MIR4484 . . . microRNA 4484 . . . . . . . . . . . MIR4485 . . . microRNA 4485 . . . . . . . . . . . MIR4486 . . . microRNA 4486 . . . . . . . . . . . MIR4487 . . . microRNA 4487 . . . . . . . . . . . MIR4488 . . . microRNA 4488 . . . . . . . . . . . MIR4489 . . . microRNA 4489 . . . . . . . . . . . MIR4490 . . . microRNA 4490 . . . . . . . . . . . MIR4491 . . . microRNA 4491 . . . . . . . . . . . MIR4492 . . . microRNA 4492 . . . . . . . . . . . MIR4493 . . . microRNA 4493 . . . . . . . . . . . MIR4494 . . . microRNA 4494 . . . . . . . . . . . MIR4495 . . . microRNA 4495 . . . . . . . . . . . MIR4496 . . . microRNA 4496 . . . . . . . . . . . MIR4497 . . . microRNA 4497 . . . . . . . . . . . MIR4498 . . . microRNA 4498 . . . . . . . . . . . MIR4499 . . . microRNA 4499 . . . . . . . . . . . MIR4500 . . . microRNA 4500 . . . . . . . . . . . MIR4500HG . . . MIR4500 host gene . . . . . . . . . . . MIR4501 . . . microRNA 4501 . . . . . . . . . . . MIR4502 . . . microRNA 4502 . . . . . . . . . . . MIR4503 . . . microRNA 4503 . . . . . . . . . . . MIR4504 . . . microRNA 4504 . . . . . . . . . . . MIR4505 . . . microRNA 4505 . . . . . . . . . . . MIR4506 . . . microRNA 4506 . . . . . . . . . . . MIR4507 . . . microRNA 4507 . . . . . . . . . . . MIR4508 . . . microRNA 4508 . . . . . . . . . . . MIR4509-1 . . . microRNA 4509-1 . . . . . . . . . . . MIR4509-2 . . . microRNA 4509-2 . . . . . . . . . . . MIR4509-3 . . . microRNA 4509-3 . . . . . . . . . . . MIR4510 . . . microRNA 4510 . . . . . . . . . . . MIR4511 . . . microRNA 4511 . . . . . . . . . . . MIR4512 . . . microRNA 4512 . . . . . . . . . . . MIR4513 . . . microRNA 4513 . . . . . . . . . . . MIR4514 . . . microRNA 4514 . . . . . . . . . . . MIR4515 . . . microRNA 4515 . . . . . . . . . . . MIR4516 . . . microRNA 4516 . . . . . . . . . . . MIR4517 . . . microRNA 4517 . . . . . . . . . . . MIR4518 . . . microRNA 4518 . . . . . . . . . . . MIR4519 . . . microRNA 4519 . . . . . . . . . . . MIR4520-1 . . . microRNA 4520-1 . . . . . . . . . . . MIR4520-2 . . . microRNA 4520-2 . . . . . . . . . . . MIR4521 . . . microRNA 4521 . . . . . . . . . . . MIR4522 . . . microRNA 4522 . . . . . . . . . . . MIR4523 . . . microRNA 4523 . . . . . . . . . . . MIR4524A . . . microRNA 4524a . . . . . . . . . . . MIR4524B . . . microRNA 4524b . . . . . . . . . . . MIR4525 . . . microRNA 4525 . . . . . . . . . . . MIR4526 . . . microRNA 4526 . . . . . . . . . . . MIR4527 . . . microRNA 4527 . . . . . . . . . . . MIR4528 . . . microRNA 4528 . . . . . . . . . . . MIR4529 . . . microRNA 4529 . . . . . . . . . . . MIR4530 . . . microRNA 4530 . . . . . . . . . . . MIR4531 . . . microRNA 4531 . . . . . . . . . . . MIR4532 . . . microRNA 4532 . . . . . . . . . . . MIR4533 . . . microRNA 4533 . . . . . . . . . . . MIR4534 . . . microRNA 4534 . . . . . . . . . . . MIR4535 . . . microRNA 4535 . . . . . . . . . . . MIR4536-1 . . . microRNA 4536-1 . . . . . . . . . . . MIR4536-2 . . . microRNA 4536-2 . . . . . . . . . . . MIR4537 . . . microRNA 4537 . . . . . . . . . . . MIR4538 . . . microRNA 4538 . . . . . . . . . . . MIR4539 . . . microRNA 4539 . . . . . . . . . . . MIR4540 . . . microRNA 4540 . . . . . . . . . . . MIR4632 . . . microRNA 4632 . . . . . . . . . . . MIR4633 . . . microRNA 4633 . . . . . . . . . . . MIR4634 . . . microRNA 4634 . . . . . . . . . . . MIR4635 . . . microRNA 4635 . . . . . . . . . . . MIR4636 . . . microRNA 4636 . . . . . . . . . . . MIR4637 . . . microRNA 4637 . . . . . . . . . . . MIR4638 . . . microRNA 4638 . . . . . . . . . . . MIR4639 . . . microRNA 4639 . . . . . . . . . . . MIR4640 . . . microRNA 4640 . . . . . . . . . . . MIR4641 . . . microRNA 4641 . . . . . . . . . . . MIR4642 . . . microRNA 4642 . . . . . . . . . . . MIR4643 . . . microRNA 4643 . . . . . . . . . . . MIR4644 . . . microRNA 4644 . . . . . . . . . . . MIR4645 . . . microRNA 4645 . . . . . . . . . . . MIR4646 . . . microRNA 4646 . . . . . . . . . . . MIR4647 . . . microRNA 4647 . . . . . . . . . . . MIR4648 . . . microRNA 4648 . . . . . . . . . . . MIR4649 . . . microRNA 4649 . . . . . . . . . . . MIR4650-1 . . . microRNA 4650-1 . . . . . . . . . . . MIR4650-2 . . . microRNA 4650-2 . . . . . . . . . . . MIR4651 . . . microRNA 4651 . . . . . . . . . . . MIR4652 . . . microRNA 4652 . . . . . . . . . . . MIR4653 . . . microRNA 4653 . . . . . . . . . . . MIR4654 . . . microRNA 4654 . . . . . . . . . . . MIR4655 . . . microRNA 4655 . . . . . . . . . . . MIR4656 . . . microRNA 4656 . . . . . . . . . . . MIR4657 . . . microRNA 4657 . . . . . . . . . . . MIR4658 . . . microRNA 4658 . . . . . . . . . . . MIR4659A . . . microRNA 4659a . . . . . . . . . . . MIR4659B . . . microRNA 4659b . . . . . . . . . . . MIR4660 . . . microRNA 4660 . . . . . . . . . . . MIR4661 . . . microRNA 4661 . . . . . . . . . . . MIR4662A . . . microRNA 4662a . . . . . . . . . . . MIR4662B . . . microRNA 4662b . . . . . . . . . . . MIR4663 . . . microRNA 4663 . . . . . . . . . . . MIR4664 . . . microRNA 4664 . . . . . . . . . . . MIR4665 . . . microRNA 4665 . . . . . . . . . . . MIR4666A . . . microRNA 4666a . . . . . . . . . . . MIR4666B . . . microRNA 4666b . . . . . . . . . . . MIR4667 . . . microRNA 4667 . . . . . . . . . . . MIR4668 . . . microRNA 4668 . . . . . . . . . . . MIR4669 . . . microRNA 4669 . . . . . . . . . . . MIR4670 . . . microRNA 4670 . . . . . . . . . . . MIR4671 . . . microRNA 4671 . . . . . . . . . . . MIR4672 . . . microRNA 4672 . . . . . . . . . . . MIR4673 . . . microRNA 4673 . . . . . . . . . . . MIR4674 . . . microRNA 4674 . . . . . . . . . . . MIR4675 . . . microRNA 4675 . . . . . . . . . . . MIR4676 . . . microRNA 4676 . . . . . . . . . . . MIR4677 . . . microRNA 4677 . . . . . . . . . . . MIR4678 . . . microRNA 4678 . . . . . . . . . . . MIR4679-1 . . . microRNA 4679-1 . . . . . . . . . . . MIR4679-2 . . . microRNA 4679-2 . . . . . . . . . . . MIR4680 . . . microRNA 4680 . . . . . . . . . . . MIR4681 . . . microRNA 4681 . . . . . . . . . . . MIR4682 . . . microRNA 4682 . . . . . . . . . . . MIR4683 . . . microRNA 4683 . . . . . . . . . . . MIR4684 . . . microRNA 4684 . . . . . . . . . . . MIR4685 . . . microRNA 4685 . . . . . . . . . . . MIR4686 . . . microRNA 4686 . . . . . . . . . . . MIR4687 . . . microRNA 4687 . . . . . . . . . . . MIR4688 . . . microRNA 4688 . . . . . . . . . . . MIR4689 . . . microRNA 4689 . . . . . . . . . . . MIR4690 . . . microRNA 4690 . . . . . . . . . . . MIR4691 . . . microRNA 4691 . . . . . . . . . . . MIR4692 . . . microRNA 4692 . . . . . . . . . . . MIR4693 . . . microRNA 4693 . . . . . . . . . . . MIR4694 . . . microRNA 4694 . . . . . . . . . . . MIR4695 . . . microRNA 4695 . . . . . . . . . . . MIR4696 . . . microRNA 4696 . . . . . . . . . . . MIR4697 . . . microRNA 4697 . . . . . . . . . . . MIR4697HG . . . MIR4697 host gene . . . . . . . . . . . MIR4698 . . . microRNA 4698 . . . . . . . . . . . MIR4699 . . . microRNA 4699 . . . . . . . . . . . MIR4700 . . . microRNA 4700 . . . . . . . . . . . MIR4701 . . . microRNA 4701 . . . . . . . . . . . MIR4703 . . . microRNA 4703 . . . . . . . . . . . MIR4704 . . . microRNA 4704 . . . . . . . . . . . MIR4705 . . . microRNA 4705 . . . . . . . . . . . MIR4706 . . . microRNA 4706 . . . . . . . . . . . MIR4707 . . . microRNA 4707 . . . . . . . . . . . MIR4708 . . . microRNA 4708 . . . . . . . . . . . MIR4709 . . . microRNA 4709 . . . . . . . . . . . MIR4710 . . . microRNA 4710 . . . . . . . . . . . MIR4711 . . . microRNA 4711 . . . . . . . . . . . MIR4712 . . . microRNA 4712 . . . . . . . . . . . MIR4713 . . . microRNA 4713 . . . . . . . . . . . MIR4714 . . . microRNA 4714 . . . . . . . . . . . MIR4715 . . . microRNA 4715 . . . . . . . . . . . MIR4716 . . . microRNA 4716 . . . . . . . . . . . MIR4717 . . . microRNA 4717 . . . . . . . . . . . MIR4718 . . . microRNA 4718 . . . . . . . . . . . MIR4719 . . . microRNA 4719 . . . . . . . . . . . MIR4720 . . . microRNA 4720 . . . . . . . . . . . MIR4721 . . . microRNA 4721 . . . . . . . . . . . MIR4722 . . . microRNA 4722 . . . . . . . . . . . MIR4723 . . . microRNA 4723 . . . . . . . . . . . MIR4724 . . . microRNA 4724 . . . . . . . . . . . MIR4725 . . . microRNA 4725 . . . . . . . . . . . MIR4726 . . . microRNA 4726 . . . . . . . . . . . MIR4727 . . . microRNA 4727 . . . . . . . . . . . MIR4728 . . . microRNA 4728 . . . . . . . . . . . MIR4729 . . . microRNA 4729 . . . . . . . . . . . MIR4730 . . . microRNA 4730 . . . . . . . . . . . MIR4731 . . . microRNA 4731 . . . . . . . . . . . MIR4732 . . . microRNA 4732 . . . . . . . . . . . MIR4733 . . . microRNA 4733 . . . . . . . . . . . MIR4734 . . . microRNA 4734 . . . . . . . . . . . MIR4735 . . . microRNA 4735 . . . . . . . . . . . MIR4736 . . . microRNA 4736 . . . . . . . . . . . MIR4737 . . . microRNA 4737 . . . . . . . . . . . MIR4738 . . . microRNA 4738 . . . . . . . . . . . MIR4739 . . . microRNA 4739 . . . . . . . . . . . MIR4740 . . . microRNA 4740 . . . . . . . . . . . MIR4741 . . . microRNA 4741 . . . . . . . . . . . MIR4742 . . . microRNA 4742 . . . . . . . . . . . MIR4743 . . . microRNA 4743 . . . . . . . . . . . MIR4744 . . . microRNA 4744 . . . . . . . . . . . MIR4745 . . . microRNA 4745 . . . . . . . . . . . MIR4746 . . . microRNA 4746 . . . . . . . . . . . MIR4747 . . . microRNA 4747 . . . . . . . . . . . MIR4748 . . . microRNA 4748 . . . . . . . . . . . MIR4749 . . . microRNA 4749 . . . . . . . . . . . MIR4750 . . . microRNA 4750 . . . . . . . . . . . MIR4751 . . . microRNA 4751 . . . . . . . . . . . MIR4752 . . . microRNA 4752 . . . . . . . . . . . MIR4753 . . . microRNA 4753 . . . . . . . . . . . MIR4754 . . . microRNA 4754 . . . . . . . . . . . MIR4755 . . . microRNA 4755 . . . . . . . . . . . MIR4756 . . . microRNA 4756 . . . . . . . . . . . MIR4757 . . . microRNA 4757 . . . . . . . . . . . MIR4758 . . . microRNA 4758 . . . . . . . . . . . MIR4759 . . . microRNA 4759 . . . . . . . . . . . MIR4760 . . . microRNA 4760 . . . . . . . . . . . MIR4761 . . . microRNA 4761 . . . . . . . . . . . MIR4762 . . . microRNA 4762 . . . . . . . . . . . MIR4763 . . . microRNA 4763 . . . . . . . . . . . MIR4764 . . . microRNA 4764 . . . . . . . . . . . MIR4765 . . . microRNA 4765 . . . . . . . . . . . MIR4766 . . . microRNA 4766 . . . . . . . . . . . MIR4767 . . . microRNA 4767 . . . . . . . . . . . MIR4768 . . . microRNA 4768 . . . . . . . . . . . MIR4769 . . . microRNA 4769 . . . . . . . . . . . MIR4770 . . . microRNA 4770 . . . . . . . . . . . MIR4771-1 . . . microRNA 4771-1 . . . . . . . . . . . MIR4771-2 . . . microRNA 4771-2 . . . . . . . . . . . MIR4772 . . . microRNA 4772 . . . . . . . . . . . MIR4773-1 . . . microRNA 4773-1 . . . . . . . . . . . MIR4773-2 . . . microRNA 4773-2 . . . . . . . . . . . MIR4774 . . . microRNA 4774 . . . . . . . . . . . MIR4775 . . . microRNA 4775 . . . . . . . . . . . MIR4776-1 . . . microRNA 4776-1 . . . . . . . . . . . MIR4776-2 . . . microRNA 4776-2 . . . . . . . . . . . MIR4777 . . . microRNA 4777 . . . . . . . . . . . MIR4778 . . . microRNA 4778 . . . . . . . . . . . MIR4779 . . . microRNA 4779 . . . . . . . . . . . MIR4780 . . . microRNA 4780 . . . . . . . . . . . MIR4781 . . . microRNA 4781 . . . . . . . . . . . MIR4782 . . . microRNA 4782 . . . . . . . . . . . MIR4783 . . . microRNA 4783 . . . . . . . . . . . MIR4784 . . . microRNA 4784 . . . . . . . . . . . MIR4785 . . . microRNA 4785 . . . . . . . . . . . MIR4786 . . . microRNA 4786 . . . . . . . . . . . MIR4787 . . . microRNA 4787 . . . . . . . . . . . MIR4788 . . . microRNA 4788 . . . . . . . . . . . MIR4789 . . . microRNA 4789 . . . . . . . . . . . MIR4790 . . . microRNA 4790 . . . . . . . . . . . MIR4791 . . . microRNA 4791 . . . . . . . . . . . MIR4792 . . . microRNA 4792 . . . . . . . . . . . MIR4793 . . . microRNA 4793 . . . . . . . . . . . MIR4794 . . . microRNA 4794 . . . . . . . . . . . MIR4795 . . . microRNA 4795 . . . . . . . . . . . MIR4796 . . . microRNA 4796 . . . . . . . . . . . MIR4797 . . . microRNA 4797 . . . . . . . . . . . MIR4798 . . . microRNA 4798 . . . . . . . . . . . MIR4799 . . . microRNA 4799 . . . . . . . . . . . MIR4800 . . . microRNA 4800 . . . . . . . . . . . MIR4801 . . . microRNA 4801 . . . . . . . . . . . MIR4802 . . . microRNA 4802 . . . . . . . . . . . MIR4803 . . . microRNA 4803 . . . . . . . . . . . MIR4804 . . . microRNA 4804 . . . . . . . . . . . MIR4999 . . . microRNA 4999 . . . . . . . . . . . MIR5000 . . . microRNA 5000 . . . . . . . . . . . MIR5001 . . . microRNA 5001 . . . . . . . . . . . MIR5002 . . . microRNA 5002 . . . . . . . . . . . MIR5003 . . . microRNA 5003 . . . . . . . . . . . MIR5004 . . . microRNA 5004 . . . . . . . . . . . MIR5006 . . . microRNA 5006 . . . . . . . . . . . MIR5007 . . . microRNA 5007 . . . . . . . . . . . MIR5008 . . . microRNA 5008 . . . . . . . . . . . MIR5009 . . . microRNA 5009 . . . . . . . . . . . MIR5010 . . . microRNA 5010 . . . . . . . . . . . MIR5011 . . . microRNA 5011 . . . . . . . . . . . MIR5047 . . . microRNA 5047 . . . . . . . . . . . MIR5087 . . . microRNA 5087 . . . . . . . . . . . MIR5088 . . . microRNA 5088 . . . . . . . . . . . MIR5089 . . . microRNA 5089 . . . . . . . . . . . MIR5090 . . . microRNA 5090 . . . . . . . . . . . MIR5091 . . . microRNA 5091 . . . . . . . . . . . MIR5092 . . . microRNA 5092 . . . . . . . . . . . MIR5093 . . . microRNA 5093 . . . . . . . . . . . MIR5094 . . . microRNA 5094 . . . . . . . . . . . MIR5095 . . . microRNA 5095 . . . . . . . . . . . MIR5096 . . . microRNA 5096 . . . . . . . . . . . MIR5100 . . . microRNA 5100 . . . . . . . . . . . MIR5186 . . . microRNA 5186 . . . . . . . . . . . MIR5187 . . . microRNA 5187 . . . . . . . . . . . MIR5188 . . . microRNA 5188 . . . . . . . . . . . MIR5189 . . . microRNA 5189 . . . . . . . . . . . MIR5190 . . . microRNA 5190 . . . . . . . . . . . MIR5191 . . . microRNA 5191 . . . . . . . . . . . MIR5192 . . . microRNA 5192 . . . . . . . . . . . MIR5193 . . . microRNA 5193 . . . . . . . . . . . MIR5194 . . . microRNA 5194 . . . . . . . . . . . MIR5195 . . . microRNA 5195 . . . . . . . . . . . MIR5196 . . . microRNA 5196 . . . . . . . . . . . MIR5197 . . . microRNA 5197 . . . . . . . . . . . MIR5571 . . . microRNA 5571 . . . . . . . . . . . MIR5572 . . . microRNA 5572 . . . . . . . . . . . MIR5579 . . . microRNA 5579 . . . . . . . . . . . MIR5580 . . . microRNA 5580 . . . . . . . . . . . MIR5581 . . . microRNA 5581 . . . . . . . . . . . MIR5582 . . . microRNA 5582 . . . . . . . . . . . MIR5583-1 . . . microRNA 5583-1 . . . . . . . . . . . MIR5583-2 . . . microRNA 5583-2 . . . . . . . . . . . MIR5584 . . . microRNA 5584 . . . . . . . . . . . MIR5585 . . . microRNA 5585 . . . . . . . . . . . MIR5586 . . . microRNA 5586 . . . . . . . . . . . MIR5587 . . . microRNA 5587 . . . . . . . . . . . MIR5588 . . . microRNA 5588 . . . . . . . . . . . MIR5589 . . . microRNA 5589 . . . . . . . . . . . MIR5590 . . . microRNA 5590 . . . . . . . . . . . MIR5591 . . . microRNA 5591 . . . . . . . . . . . MIR5680 . . . microRNA 5680 . . . . . . . . . . . MIR5681A . . . microRNA 5681a . . . . . . . . . . . MIR5681B . . . microRNA 5681b . . . . . . . . . . . MIR5682 . . . microRNA 5682 . . . . . . . . . . . MIR5683 . . . microRNA 5683 . . . . . . . . . . . MIR5684 . . . microRNA 5684 . . . . . . . . . . . MIR5685 . . . microRNA 5685 . . . . . . . . . . . MIR5687 . . . microRNA 5687 . . . . . . . . . . . MIR5688 . . . microRNA 5688 . . . . . . . . . . . MIR5689 . . . microRNA 5689 . . . . . . . . . . . MIR5689HG . . . MIR5689 host gene . . . . . . . . . . . MIR5690 . . . microRNA 5690 . . . . . . . . . . . MIR5691 . . . microRNA 5691 . . . . . . . . . . . MIR5692A1 . . . microRNA 5692a-1 . . . . . . . . . . . MIR5692A2 . . . microRNA 5692a-2 . . . . . . . . . . . MIR5692B . . . microRNA 5692b . . . . . . . . . . . MIR5692C1 . . . microRNA 5692c-1 . . . . . . . . . . . MIR5692C2 . . . microRNA 5692c-2 . . . . . . . . . . . MIR5693 . . . microRNA 5693 . . . . . . . . . . . MIR5694 . . . microRNA 5694 . . . . . . . . . . . MIR5695 . . . microRNA 5695 . . . . . . . . . . . MIR5696 . . . microRNA 5696 . . . . . . . . . . . MIR5697 . . . microRNA 5697 . . . . . . . . . . . MIR5698 . . . microRNA 5698 . . . . . . . . . . . MIR5699 . . . microRNA 5699 . . . . . . . . . . . MIR5700 . . . microRNA 5700 . . . . . . . . . . . MIR5701-1 . . . microRNA 5701-1 . . . . . . . . . . . MIR5701-2 . . . microRNA 5701-2 . . . . . . . . . . . MIR5701-3 . . . microRNA 5701-3 . . . . . . . . . . . MIR5702 . . . microRNA 5702 . . . . . . . . . . . MIR5703 . . . microRNA 5703 . . . . . . . . . . . MIR5704 . . . microRNA 5704 . . . . . . . . . . . MIR5705 . . . microRNA 5705 . . . . . . . . . . . MIR5706 . . . microRNA 5706 . . . . . . . . . . . MIR5707 . . . microRNA 5707 . . . . . . . . . . . MIR5708 . . . microRNA 5708 . . . . . . . . . . . MIR5739 . . . microRNA 5739 . . . . . . . . . . . MIR5787 . . . microRNA 5787 . . . . . . . . . . . MIR6068 . . . microRNA 6068 . . . . . . . . . . . MIR6069 . . . microRNA 6069 . . . . . . . . . . . MIR6070 . . . microRNA 6070 . . . . . . . . . . . MIR6071 . . . microRNA 6071 . . . . . . . . . . . MIR6072 . . . microRNA 6072 . . . . . . . . . . . MIR6073 . . . microRNA 6073 . . . . . . . . . . . MIR6074 . . . microRNA 6074 . . . . . . . . . . . MIR6075 . . . microRNA 6075 . . . . . . . . . . . MIR6076 . . . microRNA 6076 . . . . . . . . . . . MIR6077 . . . microRNA 6077 . . . . . . . . . . . MIR6078 . . . microRNA 6078 . . . . . . . . . . . MIR6079 . . . microRNA 6079 . . . . . . . . . . . MIR6080 . . . microRNA 6080 . . . . . . . . . . . MIR6081 . . . microRNA 6081 . . . . . . . . . . . MIR6082 . . . microRNA 6082 . . . . . . . . . . . MIR6083 . . . microRNA 6083 . . . . . . . . . . . MIR6084 . . . microRNA 6084 . . . . . . . . . . . MIR6085 . . . microRNA 6085 . . . . . . . . . . . MIR6086 . . . microRNA 6086 . . . . . . . . . . . MIR6087 . . . microRNA 6087 . . . . . . . . . . . MIR6088 . . . microRNA 6088 . . . . . . . . . . . MIR6089 . . . microRNA 6089 . . . . . . . . . . . MIR6090 . . . microRNA 6090 . . . . . . . . . . . MIR6124 . . . microRNA 6124 . . . . . . . . . . . MIR6125 . . . microRNA 6125 . . . . . . . . . . . MIR6126 . . . microRNA 6126 . . . . . . . . . . . MIR6127 . . . microRNA 6127 . . . . . . . . . . . MIR6128 . . . microRNA 6128 . . . . . . . . . . . MIR6129 . . . microRNA 6129 . . . . . . . . . . . MIR6130 . . . microRNA 6130 . . . . . . . . . . . MIR6131 . . . microRNA 6131 . . . . . . . . . . . MIR6132 . . . microRNA 6132 . . . . . . . . . . . MIR6133 . . . microRNA 6133 . . . . . . . . . . . MIR6134 . . . microRNA 6134 . . . . . . . . . . . MIR6165 . . . microRNA 6165 . . . . . . . . . . . MIR6499 . . . microRNA 6499 . . . . . . . . . . . MIR6500 . . . microRNA 6500 . . . . . . . . . . . MIR6501 . . . microRNA 6501 . . . . . . . . . . . MIR6502 . . . microRNA 6502 . . . . . . . . . . . MIR6503 . . . microRNA 6503 . . . . . . . . . . . MIR6504 . . . microRNA 6504 . . . . . . . . . . . MIR6505 . . . microRNA 6505 . . . . . . . . . . . MIR6506 . . . microRNA 6506 . . . . . . . . . . . MIR6507 . . . microRNA 6507 . . . . . . . . . . . MIR6508 . . . microRNA 6508 . . . . . . . . . . . MIR6509 . . . microRNA 6509 . . . . . . . . . . . MIR6510 . . . microRNA 6510 . . . . . . . . . . . MIR6511A1 . . . microRNA 6511a-1 . . . . . . . . . . . MIR6511A2 . . . microRNA 6511a-2 . . . . . . . . . . . MIR6511A3 . . . microRNA 6511a-3 . . . . . . . . . . . MIR6511A4 . . . microRNA 6511a-4 . . . . . . . . . . . MIR6511B1 . . . microRNA 6511b-1 . . . . . . . . . . . MIR6511B2 . . . microRNA 6511b-2 . . . . . . . . . . . MIR6512 . . . microRNA 6512 . . . . . . . . . . . MIR6513 . . . microRNA 6513 . . . . . . . . . . . MIR6514 . . . microRNA 6514 . . . . . . . . . . . MIR6515 . . . microRNA 6515 . . . . . . . . . . . MIR6516 . . . microRNA 6516 . . . . . . . . . . . MIR6715A . . . microRNA 6715a . . . . . . . . . . . MIR6715B . . . microRNA 6715b . . . . . . . . . . . MIR6716 . . . microRNA 6716 . . . . . . . . . . . MIR6717 . . . microRNA 6717 . . . . . . . . . . . MIR6718 . . . microRNA 6718 . . . . . . . . . . . MIR6719 . . . microRNA 6719 . . . . . . . . . . . MIR6720 . . . microRNA 6720 . . . . . . . . . . . MIR6721 . . . microRNA 6721 . . . . . . . . . . . MIR6722 . . . microRNA 6722 . . . . . . . . . . . MIR6723 . . . microRNA 6723 . . . . . . . . . . . MIR6724-1 . . . microRNA 6724-1 . . . . . . . . . . . MIR6724-2 . . . microRNA 6724-2 . . . . . . . . . . . MIR6724-3 . . . microRNA 6724-3 . . . . . . . . . . . MIR6724-4 . . . microRNA 6724-4 . . . . . . . . . . . MIR6726 . . . microRNA 6726 . . . . . . . . . . . MIR6727 . . . microRNA 6727 . . . . . . . . . . . MIR6728 . . . microRNA 6728 . . . . . . . . . . . MIR6729 . . . microRNA 6729 . . . . . . . . . . . MIR6730 . . . microRNA 6730 . . . . . . . . . . . MIR6731 . . . microRNA 6731 . . . . . . . . . . . MIR6732 . . . microRNA 6732 . . . . . . . . . . . MIR6733 . . . microRNA 6733 . . . . . . . . . . . MIR6734 . . . microRNA 6734 . . . . . . . . . . . MIR6735 . . . microRNA 6735 . . . . . . . . . . . MIR6736 . . . microRNA 6736 . . . . . . . . . . . MIR6737 . . . microRNA 6737 . . . . . . . . . . . MIR6738 . . . microRNA 6738 . . . . . . . . . . . MIR6739 . . . microRNA 6739 . . . . . . . . . . . MIR6740 . . . microRNA 6740 . . . . . . . . . . . MIR6741 . . . microRNA 6741 . . . . . . . . . . . MIR6742 . . . microRNA 6742 . . . . . . . . . . . MIR6743 . . . microRNA 6743 . . . . . . . . . . . MIR6744 . . . microRNA 6744 . . . . . . . . . . . MIR6745 . . . microRNA 6745 . . . . . . . . . . . MIR6746 . . . microRNA 6746 . . . . . . . . . . . MIR6747 . . . microRNA 6747 . . . . . . . . . . . MIR6748 . . . microRNA 6748 . . . . . . . . . . . MIR6749 . . . microRNA 6749 . . . . . . . . . . . MIR6750 . . . microRNA 6750 . . . . . . . . . . . MIR6751 . . . microRNA 6751 . . . . . . . . . . . MIR6752 . . . microRNA 6752 . . . . . . . . . . . MIR6753 . . . microRNA 6753 . . . . . . . . . . . MIR6754 . . . microRNA 6754 . . . . . . . . . . . MIR6755 . . . microRNA 6755 . . . . . . . . . . . MIR6756 . . . microRNA 6756 . . . . . . . . . . . MIR6757 . . . microRNA 6757 . . . . . . . . . . . MIR6758 . . . microRNA 6758 . . . . . . . . . . . MIR6759 . . . microRNA 6759 . . . . . . . . . . . MIR6760 . . . microRNA 6760 . . . . . . . . . . . MIR6761 . . . microRNA 6761 . . . . . . . . . . . MIR6762 . . . microRNA 6762 . . . . . . . . . . . MIR6763 . . . microRNA 6763 . . . . . . . . . . . MIR6764 . . . microRNA 6764 . . . . . . . . . . . MIR6765 . . . microRNA 6765 . . . . . . . . . . . MIR6766 . . . microRNA 6766 . . . . . . . . . . . MIR6767 . . . microRNA 6767 . . . . . . . . . . . MIR6768 . . . microRNA 6768 . . . . . . . . . . . MIR6769A . . . microRNA 6769a . . . . . . . . . . . MIR6769B . . . microRNA 6769b . . . . . . . . . . . MIR6770-1 . . . microRNA 6770-1 . . . . . . . . . . . MIR6770-2 . . . microRNA 6770-2 . . . . . . . . . . . MIR6770-3 . . . microRNA 6770-3 . . . . . . . . . . . MIR6771 . . . microRNA 6771 . . . . . . . . . . . MIR6772 . . . microRNA 6772 . . . . . . . . . . . MIR6773 . . . microRNA 6773 . . . . . . . . . . . MIR6774 . . . microRNA 6774 . . . . . . . . . . . MIR6775 . . . microRNA 6775 . . . . . . . . . . . MIR6776 . . . microRNA 6776 . . . . . . . . . . . MIR6777 . . . microRNA 6777 . . . . . . . . . . . MIR6778 . . . microRNA 6778 . . . . . . . . . . . MIR6779 . . . microRNA 6779 . . . . . . . . . . . MIR6780A . . . microRNA 6780a . . . . . . . . . . . MIR6780B . . . microRNA 6780b . . . . . . . . . . . MIR6781 . . . microRNA 6781 . . . . . . . . . . . MIR6782 . . . microRNA 6782 . . . . . . . . . . . MIR6783 . . . microRNA 6783 . . . . . . . . . . . MIR6784 . . . microRNA 6784 . . . . . . . . . . . MIR6785 . . . microRNA 6785 . . . . . . . . . . . MIR6786 . . . microRNA 6786 . . . . . . . . . . . MIR6787 . . . microRNA 6787 . . . . . . . . . . . MIR6788 . . . microRNA 6788 . . . . . . . . . . . MIR6789 . . . microRNA 6789 . . . . . . . . . . . MIR6790 . . . microRNA 6790 . . . . . . . . . . . MIR6791 . . . microRNA 6791 . . . . . . . . . . . MIR6792 . . . microRNA 6792 . . . . . . . . . . . MIR6793 . . . microRNA 6793 . . . . . . . . . . . MIR6794 . . . microRNA 6794 . . . . . . . . . . . MIR6795 . . . microRNA 6795 . . . . . . . . . . . MIR6796 . . . microRNA 6796 . . . . . . . . . . . MIR6797 . . . microRNA 6797 . . . . . . . . . . . MIR6798 . . . microRNA 6798 . . . . . . . . . . . MIR6799 . . . microRNA 6799 . . . . . . . . . . . MIR6800 . . . microRNA 6800 . . . . . . . . . . . MIR6801 . . . microRNA 6801 . . . . . . . . . . . MIR6802 . . . microRNA 6802 . . . . . . . . . . . MIR6803 . . . microRNA 6803 . . . . . . . . . . . MIR6804 . . . microRNA 6804 . . . . . . . . . . . MIR6805 . . . microRNA 6805 . . . . . . . . . . . MIR6806 . . . microRNA 6806 . . . . . . . . . . . MIR6807 . . . microRNA 6807 . . . . . . . . . . . MIR6808 . . . microRNA 6808 . . . . . . . . . . . MIR6809 . . . microRNA 6809 . . . . . . . . . . . MIR6810 . . . microRNA 6810 . . . . . . . . . . . MIR6811 . . . microRNA 6811 . . . . . . . . . . . MIR6812 . . . microRNA 6812 . . . . . . . . . . . MIR6813 . . . microRNA 6813 . . . . . . . . . . . MIR6814 . . . microRNA 6814 . . . . . . . . . . . MIR6815 . . . microRNA 6815 . . . . . . . . . . . MIR6816 . . . microRNA 6816 . . . . . . . . . . . MIR6817 . . . microRNA 6817 . . . . . . . . . . . MIR6818 . . . microRNA 6818 . . . . . . . . . . . MIR6819 . . . microRNA 6819 . . . . . . . . . . . MIR6820 . . . microRNA 6820 . . . . . . . . . . . MIR6821 . . . microRNA 6821 . . . . . . . . . . . MIR6822 . . . microRNA 6822 . . . . . . . . . . . MIR6823 . . . microRNA 6823 . . . . . . . . . . . MIR6824 . . . microRNA 6824 . . . . . . . . . . . MIR6825 . . . microRNA 6825 . . . . . . . . . . . MIR6826 . . . microRNA 6826 . . . . . . . . . . . MIR6827 . . . microRNA 6827 . . . . . . . . . . . MIR6828 . . . microRNA 6828 . . . . . . . . . . . MIR6829 . . . microRNA 6829 . . . . . . . . . . . MIR6830 . . . microRNA 6830 . . . . . . . . . . . MIR6831 . . . microRNA 6831 . . . . . . . . . . . MIR6832 . . . microRNA 6832 . . . . . . . . . . . MIR6833 . . . microRNA 6833 . . . . . . . . . . . MIR6834 . . . microRNA 6834 . . . . . . . . . . . MIR6835 . . . microRNA 6835 . . . . . . . . . . . MIR6836 . . . microRNA 6836 . . . . . . . . . . . MIR6837 . . . microRNA 6837 . . . . . . . . . . . MIR6838 . . . microRNA 6838 . . . . . . . . . . . MIR6839 . . . microRNA 6839 . . . . . . . . . . . MIR6840 . . . microRNA 6840 . . . . . . . . . . . MIR6841 . . . microRNA 6841 . . . . . . . . . . . MIR6842 . . . microRNA 6842 . . . . . . . . . . . MIR6843 . . . microRNA 6843 . . . . . . . . . . . MIR6844 . . . microRNA 6844 . . . . . . . . . . . MIR6845 . . . microRNA 6845 . . . . . . . . . . . MIR6846 . . . microRNA 6846 . . . . . . . . . . . MIR6847 . . . microRNA 6847 . . . . . . . . . . . MIR6848 . . . microRNA 6848 . . . . . . . . . . . MIR6849 . . . microRNA 6849 . . . . . . . . . . . MIR6850 . . . microRNA 6850 . . . . . . . . . . . MIR6851 . . . microRNA 6851 . . . . . . . . . . . MIR6852 . . . microRNA 6852 . . . . . . . . . . . MIR6853 . . . microRNA 6853 . . . . . . . . . . . MIR6854 . . . microRNA 6854 . . . . . . . . . . . MIR6855 . . . microRNA 6855 . . . . . . . . . . . MIR6856 . . . microRNA 6856 . . . . . . . . . . . MIR6857 . . . microRNA 6857 . . . . . . . . . . . MIR6858 . . . microRNA 6858 . . . . . . . . . . . MIR6859-1 . . . microRNA 6859-1 . . . . . . . . . . . MIR6859-2 . . . microRNA 6859-2 . . . . . . . . . . . MIR6859-3 . . . microRNA 6859-3 . . . . . . . . . . . MIR6859-4 . . . microRNA 6859-4 . . . . . . . . . . . MIR6860 . . . microRNA 6860 . . . . . . . . . . . MIR6861 . . . microRNA 6861 . . . . . . . . . . . MIR6862-1 . . . microRNA 6862-1 . . . . . . . . . . . MIR6862-2 . . . microRNA 6862-2 . . . . . . . . . . . MIR6863 . . . microRNA 6863 . . . . . . . . . . . MIR6864 . . . microRNA 6864 . . . . . . . . . . . MIR6865 . . . microRNA 6865 . . . . . . . . . . . MIR6866 . . . microRNA 6866 . . . . . . . . . . . MIR6867 . . . microRNA 6867 . . . . . . . . . . . MIR6868 . . . microRNA 6868 . . . . . . . . . . . MIR6869 . . . microRNA 6869 . . . . . . . . . . . MIR6870 . . . microRNA 6870 . . . . . . . . . . . MIR6871 . . . microRNA 6871 . . . . . . . . . . . MIR6872 . . . microRNA 6872 . . . . . . . . . . . MIR6873 . . . microRNA 6873 . . . . . . . . . . . MIR6874 . . . microRNA 6874 . . . . . . . . . . . MIR6875 . . . microRNA 6875 . . . . . . . . . . . MIR6876 . . . microRNA 6876 . . . . . . . . . . . MIR6877 . . . microRNA 6877 . . . . . . . . . . . MIR6878 . . . microRNA 6878 . . . . . . . . . . . MIR6879 . . . microRNA 6879 . . . . . . . . . . . MIR6880 . . . microRNA 6880 . . . . . . . . . . . MIR6881 . . . microRNA 6881 . . . . . . . . . . . MIR6882 . . . microRNA 6882 . . . . . . . . . . . MIR6883 . . . microRNA 6883 . . . . . . . . . . . MIR6884 . . . microRNA 6884 . . . . . . . . . . . MIR6885 . . . microRNA 6885 . . . . . . . . . . . MIR6886 . . . microRNA 6886 . . . . . . . . . . . MIR6887 . . . microRNA 6887 . . . . . . . . . . . MIR6888 . . . microRNA 6888 . . . . . . . . . . . MIR6889 . . . microRNA 6889 . . . . . . . . . . . MIR6890 . . . microRNA 6890 . . . . . . . . . . . MIR6891 . . . microRNA 6891 . . . . . . . . . . . MIR6892 . . . microRNA 6892 . . . . . . . . . . . MIR6893 . . . microRNA 6893 . . . . . . . . . . . MIR6894 . . . microRNA 6894 . . . . . . . . . . . MIR6895 . . . microRNA 6895 . . . . . . . . . . . MIR7106 . . . microRNA 7106 . . . . . . . . . . . MIR7107 . . . microRNA 7107 . . . . . . . . . . . MIR7108 . . . microRNA 7108 . . . . . . . . . . . MIR7109 . . . microRNA 7109 . . . . . . . . . . . MIR7110 . . . microRNA 7110 . . . . . . . . . . . MIR7111 . . . microRNA 7111 . . . . . . . . . . . MIR7112 . . . microRNA 7112 . . . . . . . . . . . MIR7113 . . . microRNA 7113 . . . . . . . . . . . MIR7114 . . . microRNA 7114 . . . . . . . . . . . MIR7150 . . . microRNA 7150 . . . . . . . . . . . MIR7151 . . . microRNA 7151 . . . . . . . . . . . MIR7152 . . . microRNA 7152 . . . . . . . . . . . MIR7153 . . . microRNA 7153 . . . . . . . . . . . MIR7154 . . . microRNA 7154 . . . . . . . . . . . MIR7155 . . . microRNA 7155 . . . . . . . . . . . MIR7156 . . . microRNA 7156 . . . . . . . . . . . MIR7157 . . . microRNA 7157 . . . . . . . . . . . MIR7158 . . . microRNA 7158 . . . . . . . . . . . MIR7159 . . . microRNA 7159 . . . . . . . . . . . MIR7160 . . . microRNA 7160 . . . . . . . . . . . MIR7161 . . . microRNA 7161 . . . . . . . . . . . MIR7162 . . . microRNA 7162 . . . . . . . . . . . MIR7515 . . . microRNA 7515 . . . . . . . . . . . MIR7515HG . . . MIR7515 host gene . . . . . . . . . . . MIR7641-1 . . . microRNA 7641-1 . . . . . . . . . . . MIR7641-2 . . . microRNA 7641-2 . . . . . . . . . . . MIR7702 . . . microRNA 7702 . . . . . . . . . . . MIR7703 . . . microRNA 7703 . . . . . . . . . . . MIR7704 . . . microRNA 7704 . . . . . . . . . . . MIR7705 . . . microRNA 7705 . . . . . . . . . . . MIR7706 . . . microRNA 7706 . . . . . . . . . . . MIR7843 . . . microRNA 7843 . . . . . . . . . . . MIR7844 . . . microRNA 7844 . . . . . . . . . . . MIR7845 . . . microRNA 7845 . . . . . . . . . . . MIR7846 . . . microRNA 7846 . . . . . . . . . . . MIR7847 . . . microRNA 7847 . . . . . . . . . . . MIR7848 . . . microRNA 7848 . . . . . . . . . . . MIR7849 . . . microRNA 7849 . . . . . . . . . . . MIR7850 . . . microRNA 7850 . . . . . . . . . . . MIR7851 . . . microRNA 7851 . . . . . . . . . . . MIR7852 . . . microRNA 7852 . . . . . . . . . . . MIR7853 . . . microRNA 7853 . . . . . . . . . . . MIR7854 . . . microRNA 7854 . . . . . . . . . . . MIR7855 . . . microRNA 7855 . . . . . . . . . . . MIR7856 . . . microRNA 7856 . . . . . . . . . . . MIR7973-1 . . . microRNA 7973-1 . . . . . . . . . . . MIR7973-2 . . . microRNA 7973-2 . . . . . . . . . . . MIR7974 . . . microRNA 7974 . . . . . . . . . . . MIR7975 . . . microRNA 7975 . . . . . . . . . . . MIR7976 . . . microRNA 7976 . . . . . . . . . . . MIR7977 . . . microRNA 7977 . . . . . . . . . . . MIR7978 . . . microRNA 7978 . . . . . . . . . . . MIR8052 . . . microRNA 8052 . . . . . . . . . . . MIR8053 . . . microRNA 8053 . . . . . . . . . . . MIR8054 . . . microRNA 8054 . . . . . . . . . . . MIR8055 . . . microRNA 8055 . . . . . . . . . . . MIR8056 . . . microRNA 8056 . . . . . . . . . . . MIR8057 . . . microRNA 8057 . . . . . . . . . . . MIR8058 . . . microRNA 8058 . . . . . . . . . . . MIR8059 . . . microRNA 8059 . . . . . . . . . . . MIR8060 . . . microRNA 8060 . . . . . . . . . . . MIR8061 . . . microRNA 8061 . . . . . . . . . . . MIR8062 . . . microRNA 8062 . . . . . . . . . . . MIR8063 . . . microRNA 8063 . . . . . . . . . . . MIR8064 . . . microRNA 8064 . . . . . . . . . . . MIR8065 . . . microRNA 8065 . . . . . . . . . . . MIR8066 . . . microRNA 8066 . . . . . . . . . . . MIR8067 . . . microRNA 8067 . . . . . . . . . . . MIR8068 . . . microRNA 8068 . . . . . . . . . . . MIR8069-1 . . . microRNA 8069-1 . . . . . . . . . . . MIR8069-2 . . . microRNA 8069-2 . . . . . . . . . . . MIR8070 . . . microRNA 8070 . . . . . . . . . . . MIR8071-1 . . . microRNA 8071-1 . . . . . . . . . . . MIR8071-2 . . . microRNA 8071-2 . . . . . . . . . . . MIR8072 . . . microRNA 8072 . . . . . . . . . . . MIR8073 . . . microRNA 8073 . . . . . . . . . . . MIR8074 . . . microRNA 8074 . . . . . . . . . . . MIR8075 . . . microRNA 8075 . . . . . . . . . . . MIR8076 . . . microRNA 8076 . . . . . . . . . . . MIR8077 . . . microRNA 8077 . . . . . . . . . . . MIR8078 . . . microRNA 8078 . . . . . . . . . . . MIR8079 . . . microRNA 8079 . . . . . . . . . . . MIR8080 . . . microRNA 8080 . . . . . . . . . . . MIR8081 . . . microRNA 8081 . . . . . . . . . . . MIR8082 . . . microRNA 8082 . . . . . . . . . . . MIR8083 . . . microRNA 8083 . . . . . . . . . . . MIR8084 . . . microRNA 8084 . . . . . . . . . . . MIR8085 . . . microRNA 8085 . . . . . . . . . . . MIR8086 . . . microRNA 8086 . . . . . . . . . . . MIR8087 . . . microRNA 8087 . . . . . . . . . . . MIR8088 . . . microRNA 8088 . . . . . . . . . . . MIR8089 . . . microRNA 8089 . . . . . . . . . . . MIR8485 . . . microRNA 8485 . . . . . . . . . . . MIR9500 . . . microRNA 9500 . . . . . . . . . . . MIRLET7A1 . . . microRNA let-7a-1 . . . . . . . . . . . MIRLET7A2 . . . microRNA let-7a-2 . . . . . . . . . . . MIRLET7A3 . . . microRNA let-7a-3 . . . . . . . . . . . MIRLET7B . . . microRNA let-7b . . . . . . . . . . . MIRLET7BHG . . . MIRLET7B host gene . . . . . . . . . . . MIRLET7C . . . microRNA let-7c . . . . . . . . . . . MIRLET7D . . . microRNA let-7d . . . . . . . . . . . MIRLET7DHG . . . MIRLET7D host gene . . . . . . . . . . . MIRLET7E . . . microRNA let-7e . . . . . . . . . . . MIRLET7F1 . . . microRNA let-7f-1 . . . . . . . . . . . MIRLET7F2 . . . microRNA let-7f-2 . . . . . . . . . . . MIRLET7G . . . microRNA let-7g . . . . . . . . . . . MIRLET7I . . . microRNA let-7i . . . . . . . . . . . MIS12 0.020597647163852 0.748234116706836 0.231168236129312 MIS12 kinetochore complex component FUNCTION: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and for kinetochore formation during mitosis. {ECO:0000269|PubMed:12515822, ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}.; . . . . 0.34444 . -0.117432389 44.89266336 44.57401 1.27895 MIS18A 0.0517219632264389 0.861418530350431 0.0868595064231305 MIS18 kinetochore protein A FUNCTION: Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. {ECO:0000269|PubMed:17199038}.; . TISSUE SPECIFICITY: Detected in testis. {ECO:0000269|PubMed:17199038}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;islets of Langerhans;oral cavity;blood;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node; 0.40279 0.10442 -0.095386216 46.48502005 45.79481 1.30106 MIS18A-AS1 . . . MIS18A antisense RNA 1 . . . . . . . . . . . MIS18BP1 2.3000916264824e-05 0.999045194740016 0.000931804343719396 MIS18 binding protein 1 FUNCTION: Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. {ECO:0000269|PubMed:17199038, ECO:0000269|PubMed:17339379}.; . . lymphoreticular;ovary;sympathetic chain;colon;parathyroid;vein;bone marrow;uterus;prostate;whole body;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;skeletal muscle;lung;placenta;liver;cervix;kidney;stomach; superior cervical ganglion;uterus corpus;prefrontal cortex;white blood cells;atrioventricular node;pons;skeletal muscle; 0.25957 0.06969 1.743518989 96.6383581 1469.92348 7.14407 MISP 1.94870607708529e-10 0.0340981730187013 0.965901826786428 mitotic spindle positioning FUNCTION: Plays a role in mitotic spindle orientation and mitotic progression. Regulates the distribution of dynactin at the cell cortex in a PLK1-dependent manner, thus stabilizing cortical and astral microtubule attachments required for proper mitotic spindle positioning. May link microtubules to the actin cytospkeleton and focal adhesions. May be required for directed cell migration and centrosome orientation. May also be necessary for proper stacking of the Golgi apparatus. {ECO:0000269|PubMed:23509069, ECO:0000269|PubMed:23574715}.; . . . . 0.13168 . -0.031281682 50.5779665 693.62656 5.25135 MITD1 0.00170794026951473 0.893086914534668 0.105205145195817 microtubule interacting and trafficking domain containing 1 FUNCTION: Required for efficient abscission at the end of cytokinesis, together with components of the ESCRT-III complex. {ECO:0000269|PubMed:23015756, ECO:0000269|PubMed:23045692}.; . . ovary;colon;parathyroid;substantia nigra;retina;uterus;prostate;whole body;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;pancreas;lung;trabecular meshwork;placenta;hippocampus;liver;spleen;kidney;mammary gland; . 0.16841 0.28430 -0.095386216 46.48502005 33.23832 1.02733 MITF 0.997810643539312 0.00218934199546777 1.44652203575945e-08 microphthalmia-associated transcription factor FUNCTION: Transcription factor that regulates the expression of genes with essential roles in cell differentiation, proliferation and survival. Binds to symmetrical DNA sequences (E-boxes) (5'- CACGTG-3') found in the promoters of target genes, such as BCL2 and tyrosinase (TYR). Plays an important role in melanocyte development by regulating the expression of tyrosinase (TYR) and tyrosinase-related protein 1 (TYRP1). Plays a critical role in the differentiation of various cell types, such as neural crest- derived melanocytes, mast cells, osteoclasts and optic cup-derived retinal pigment epithelium. {ECO:0000269|PubMed:10587587, ECO:0000269|PubMed:22647378}.; DISEASE: Waardenburg syndrome 2A (WS2A) [MIM:193510]: WS2 is a genetically heterogeneous, autosomal dominant disorder characterized by sensorineural deafness, pigmentary disturbances, and absence of dystopia canthorum. The frequency of deafness is higher in WS2 than in WS1. {ECO:0000269|PubMed:8589691}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Waardenburg syndrome 2, with ocular albinism, autosomal recessive (WS2-OA) [MIM:103470]: A disorder characterized by the association of features typical of Waardenburg syndrome type 2 with ocular albinism. Patients manifest reduced visual acuity, albinotic fundus, deafness, hypomelanosis. {ECO:0000269|PubMed:9647758}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Tietz syndrome (TIETZS) [MIM:103500]: Autosomal dominant disorder characterized by generalized hypopigmentation and profound, congenital, bilateral deafness. Penetrance is complete. {ECO:0000269|PubMed:10851256}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Melanoma, cutaneous malignant 8 (CMM8) [MIM:614456]: A malignant neoplasm of melanocytes, arising de novo or from a pre- existing benign nevus, which occurs most often in the skin but also may involve other sites. {ECO:0000269|PubMed:22012259, ECO:0000269|PubMed:22080950}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform M is exclusively expressed in melanocytes and melanoma cells. Isoform A and isoform H are widely expressed in many cell types including melanocytes and retinal pigment epithelium (RPE). Isoform C is expressed in many cell types including RPE but not in melanocyte-lineage cells. Isoform Mdel is widely expressed in melanocytes, melanoma cell lines and tissues, but almost undetectable in non-melanoma cell lines. {ECO:0000269|PubMed:20163701}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);heart;tongue;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach; uterus;superior cervical ganglion;uterus corpus;skeletal muscle; 0.85090 0.42299 -0.556537043 19.72753008 59.31124 1.56128 MIXL1 0.0428902666081295 0.661691598332125 0.295418135059746 Mix paired-like homeobox FUNCTION: Transcription factor that play a central role in proper axial mesendoderm morphogenesis and endoderm formation. Required for efficient differentiation of cells from the primitive streak stage to blood, by acting early in the recruitment and/or expansion of mesodermal progenitors to the hemangioblastic and hematopoietic lineages. Also involved in the morphogenesis of the heart and the gut during embryogenesis. Acts as a negative regulator of brachyury expression (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Restricted to progenitors and secondary lymph tissues. In normal hematopoiesis, it is restricted to immature B- and T-lymphoid cells. Present in differentiating embryonic stem cells (at protein level). {ECO:0000269|PubMed:12070013, ECO:0000269|PubMed:16433620, ECO:0000269|PubMed:17303500}.; . . 0.17758 0.24913 . . 113.81555 2.32595 MKI67 4.17035383841505e-16 0.998663438695794 0.00133656130420545 marker of proliferation Ki-67 FUNCTION: Thought to be required for maintaining cell proliferation.; . . . . 0.62381 . 7.633856952 99.91153574 13447.4791 25.13173 MKI67P1 . . . marker of proliferation Ki-67 pseudogene 1 . . . . . . . . . . . MKKS 4.23711359687125e-09 0.0558747414747711 0.944125254288115 McKusick-Kaufman syndrome FUNCTION: Probable molecular chaperone. Assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. May play a role in protein processing in limb, cardiac and reproductive system development. May play a role in cytokinesis. {ECO:0000269|PubMed:20080638}.; DISEASE: McKusick-Kaufman syndrome (MKKS) [MIM:236700]: Autosomal recessive developmental disorder. It is characterized by hydrometrocolpos, postaxial polydactyly and congenital heart defects. {ECO:0000269|PubMed:10802661}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bardet-Biedl syndrome 6 (BBS6) [MIM:605231]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:10973238, ECO:0000269|PubMed:10973251, ECO:0000269|PubMed:11179009, ECO:0000269|PubMed:11567139, ECO:0000269|PubMed:12107442, ECO:0000269|PubMed:12677556, ECO:0000269|PubMed:12920096, ECO:0000269|PubMed:15666242, ECO:0000269|PubMed:15770229, ECO:0000269|PubMed:21344540, ECO:0000269|PubMed:22152675}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues.; myocardium;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;gum;bladder;brain;heart;pharynx;blood;lens;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;thymus; thalamus;subthalamic nucleus;medulla oblongata;occipital lobe;temporal lobe;prefrontal cortex;globus pallidus;pons;caudate nucleus;parietal lobe;cingulate cortex; 0.46757 0.30578 0.354632714 74.58126917 1649.27798 7.50495 MKL1 0.54032417291881 0.459649314253924 2.6512827266241e-05 megakaryoblastic leukemia (translocation) 1 FUNCTION: Transcriptional coactivator of serum response factor (SRF) with the potential to modulate SRF target genes. Suppresses TNF-induced cell death by inhibiting activation of caspases; its transcriptional activity is indispensable for the antiapoptotic function. It may up-regulate antiapoptotic molecules, which in turn inhibit caspase activation (By similarity). {ECO:0000250}.; DISEASE: Note=A chromosomal aberration involving MKL1 may be a cause of acute megakaryoblastic leukemia. Translocation t(1;22)(p13;q13) with RBM15. Although both reciprocal fusion transcripts are detected in acute megakaryoblastic leukemia (AMKL, FAB-M7), the RBM15-MKL1 chimeric protein has all the putative functional domains encoded by each gene and is the candidate oncogene.; TISSUE SPECIFICITY: Ubiquitously expressed, has been detected in lung, placenta, small intestine, liver, kidney, spleen, thymus, colon, muscle, heart and brain.; lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;pons;atrioventricular node;skeletal muscle;prefrontal cortex;appendix;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.20383 0.12175 -0.525400547 20.91295117 655.74551 5.13463 MKL2 0.999938115504898 6.18844926664995e-05 2.43529372915539e-12 MKL/myocardin-like 2 FUNCTION: Acts as a transcriptional coactivator of serum response factor (SRF). Required for skeletal myogenic differentiation. {ECO:0000269|PubMed:14565952}.; DISEASE: Note=A chromosomal aberration involving C11orf95 is found in 3 chondroid lipomas. Translocation t(11;16)(q13;p13) with C11orf95 produces a C11orf95-MKL2 fusion protein (PubMed:20607705). {ECO:0000269|PubMed:20607705}.; . ovary;colon;parathyroid;skin;retina;uterus;prostate;frontal lobe;cochlea;endometrium;larynx;thyroid;bone;pituitary gland;testis;dura mater;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);meninges;lymph node;heart;lacrimal gland;islets of Langerhans;adrenal cortex;skeletal muscle;breast;pia mater;lung;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; whole brain;amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;temporal lobe;pons;atrioventricular node;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.38756 0.08351 -1.548724932 3.273177636 106.48563 2.23956 MKLN1 0.999577504819181 0.00042249512773885 5.30802732506694e-11 muskelin 1 FUNCTION: Acts as a mediator of cell spreading and cytoskeletal responses to the extracellular matrix component THBS1. {ECO:0000250|UniProtKB:O89050}.; . . ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;gall bladder;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;cerebellum cortex;lacrimal gland;pancreas;lung;cornea;placenta;head and neck;kidney;aorta;thymus; testis - interstitial;testis - seminiferous tubule; 0.35761 0.14611 -0.427900189 25.14744043 19.26303 0.66403 MKLN1-AS . . . MKLN1 antisense RNA . . . . . . . . . . . MKNK1 0.000222399042685413 0.979402273271978 0.0203753276853363 MAP kinase interacting serine/threonine kinase 1 FUNCTION: May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7- methylguanosine-containing mRNA cap. {ECO:0000269|PubMed:11463832, ECO:0000269|PubMed:15350534, ECO:0000269|PubMed:9155018, ECO:0000269|PubMed:9878069}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15350534}.; ovary;developmental;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;pharynx;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;head and neck;spleen;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.23466 0.14377 0.328949044 73.41354093 69.37164 1.72729 MKNK1-AS1 . . . MKNK1 antisense RNA 1 . . . . . . . . . . . MKNK2 9.33657569741937e-06 0.777281387488606 0.222709275935696 MAP kinase interacting serine/threonine kinase 2 FUNCTION: Serine/threonine-protein kinase that phosphorylates SFPQ/PSF, HNRNPA1 and EIF4E. May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap. Required for mediating PP2A-inhibition-induced EIF4E phosphorylation. Triggers EIF4E shuttling from cytoplasm to nucleus. Isoform 1 displays a high basal kinase activity, but isoform 2 exhibits a very low kinase activity. Acts as a mediator of the suppressive effects of IFNgamma on hematopoiesis. Negative regulator for signals that control generation of arsenic trioxide As(2)O(3)-dependent apoptosis and anti-leukemic responses. Involved in anti-apoptotic signaling in response to serum withdrawal. {ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:11463832, ECO:0000269|PubMed:12897141, ECO:0000269|PubMed:16111636, ECO:0000269|PubMed:17965020, ECO:0000269|PubMed:18299328, ECO:0000269|PubMed:20823271, ECO:0000269|PubMed:20927323, ECO:0000269|PubMed:21149447}.; . TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined. Isoform 2 is expressed at higher levels in the ovary than is isoform 1. {ECO:0000269|PubMed:11013076}.; ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;amniotic fluid;germinal center;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;oesophagus;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus;cerebellum; lung;adipose tissue;tongue;white blood cells;skeletal muscle; 0.18067 0.14759 -0.576764155 18.7839113 742.98614 5.41125 MKNK2P1 . . . MAP kinase interacting serine/threonine kinase 2 pseudogene 1 . . . . . . . . . . . MKRN1 0.97942365116225 0.0205728659562162 3.48288153345145e-06 makorin ring finger protein 1 FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include FILIP1, p53/TP53, CDKN1A and TERT. Keeps cells alive by suppressing p53/TP53 under normal conditions, but stimulates apoptosis by repressing CDKN1A under stress conditions. Acts as a negative regulator of telomerase. Has negative and positive effects on RNA polymerase II-dependent transcription. {ECO:0000269|PubMed:16785614, ECO:0000269|PubMed:19536131}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10843807, ECO:0000269|PubMed:16785614}.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta; amygdala;whole brain;testis - interstitial;subthalamic nucleus;fetal liver;testis - seminiferous tubule;prefrontal cortex;testis;cingulate cortex;bone marrow; 0.71986 0.11424 0.040529541 57.15380986 1492.95866 7.18801 MKRN2 0.407628906147087 0.590583964765416 0.00178712908749726 makorin ring finger protein 2 FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11597136}.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;oesophagus;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;placenta;duodenum;kidney;stomach;thymus;cerebellum; testis;cingulate cortex; 0.16410 0.11505 -0.670411825 15.61689078 39.01949 1.15639 MKRN2OS . . . MKRN2 opposite strand . . . . . . . . . . . MKRN3 0.0235775059313367 0.913738499268745 0.0626839947999181 makorin ring finger protein 3 FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. {ECO:0000250, ECO:0000269|PubMed:19066619}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10196367}.; unclassifiable (Anatomical System);lung;placenta;muscle;testis;brain; superior cervical ganglion;testis - interstitial;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.02784 0.11011 -1.131590109 6.481481481 26.65655 0.86283 MKRN3-AS1 . . . MKRN3 antisense RNA 1 . . . . . . . . . . . MKRN4P . . . makorin ring finger protein 4, pseudogene FUNCTION: May act as a E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. {ECO:0000250}.; . . . . . . . . . . MKRN5P . . . makorin ring finger protein 5, pseudogene . . . . . . . . . . . MKRN6P . . . makorin ring finger protein 6, pseudogene . . . . . . . . . . . MKRN7P . . . makorin ring finger protein 7, pseudogene . . . . . . . . . . . MKRN8P . . . makorin ring finger protein 8, pseudogene . . . . . . . . . . . MKRN9P . . . makorin ring finger protein 9, pseudogene . . . . . . 0.11424 . . . . MKS1 3.9743813098665e-09 0.932522593869199 0.0674774021564196 Meckel syndrome, type 1 FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Involved in centrosome migration to the apical cell surface during early ciliogenesis. Required for ciliary structure and function, including a role in regulating length and appropriate number through modulating centrosome duplication. Required for cell branching morphology. {ECO:0000269|PubMed:17185389, ECO:0000269|PubMed:19515853}.; DISEASE: Meckel syndrome 1 (MKS1) [MIM:249000]: A disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly. {ECO:0000269|PubMed:16415886, ECO:0000269|PubMed:19466712}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bardet-Biedl syndrome 13 (BBS13) [MIM:615990]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:18327255}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;skin;uterus;prostate;endometrium;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;blood;lung;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; trigeminal ganglion;skeletal muscle; 0.06784 0.35722 -0.044015879 50.44821892 116.58991 2.34839 MKX 0.882320086401519 0.117398446613279 0.00028146698520135 mohawk homeobox FUNCTION: May act as a morphogenetic regulator of cell adhesion. {ECO:0000250}.; . . . . 0.24677 . 0.661468037 84.4420854 292.97977 3.66012 MKX-AS1 . . . MKX antisense RNA 1 . . . . . . . . . . . MLANA 1.07616714222612e-08 0.0263976566371137 0.973602332601215 melan-A FUNCTION: Involved in melanosome biogenesis by ensuring the stability of GPR143. Plays a vital role in the expression, stability, trafficking, and processing of melanocyte protein PMEL, which is critical to the formation of stage II melanosomes. {ECO:0000269|PubMed:15695812, ECO:0000269|PubMed:19717472}.; . TISSUE SPECIFICITY: Expression is restricted to melanoma and melanocyte cell lines and retina.; . . 0.12847 0.37619 -0.229483771 36.86010852 21.71058 0.73104 MLC1 5.02796269549306e-05 0.870613504425602 0.129336215947443 megalencephalic leukoencephalopathy with subcortical cysts 1 FUNCTION: Regulates the response of astrocytes to hypo-osmosis by promoting calcium influx. {ECO:0000269|PubMed:22328087}.; . TISSUE SPECIFICITY: Expressed in the brain, with highest levels found in the amygdala, nucleus caudatus, thalamus and hippocampus. {ECO:0000269|PubMed:11326298}.; unclassifiable (Anatomical System);lymph node;ovary;hypothalamus;blood;parathyroid;fovea centralis;choroid;lens;retina;bone marrow;prostate;optic nerve;whole body;lung;frontal lobe;bone;placenta;macula lutea;hippocampus;liver;testis;spleen;brain;cerebellum; whole brain;amygdala;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;bone marrow;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.31831 0.20556 -0.001743238 53.85114414 1442.93116 7.08466 MLEC 0.470920638317783 0.523721899376268 0.00535746230594852 malectin FUNCTION: Carbohydrate-binding protein with a strong ligand preference for Glc2-N-glycan. May play a role in the early steps of protein N-glycosylation (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;muscle;urinary;blood;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;pancreas;prostate;testis - seminiferous tubule;adrenal gland;adrenal cortex;liver;testis;kidney;skeletal muscle; 0.39007 0.11952 -0.141298762 42.87567823 7.94711 0.29182 MLECP1 . . . malectin pseudogene 1 . . . . . . . . . . . MLF1 1.28387834312483e-06 0.594694001236843 0.405304714884814 myeloid leukemia factor 1 FUNCTION: Involved in lineage commitment of primary hemopoietic progenitors by restricting erythroid formation and enhancing myeloid formation. Interferes with erythropoietin-induced erythroid terminal differentiation by preventing cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. Suppresses RFWD2/COP1 activity via CSN3 which activates p53 and induces cell cycle arrest. Binds DNA and affects the expression of a number of genes so may function as a transcription factor in the nucleus. {ECO:0000269|PubMed:15861129}.; DISEASE: Note=A chromosomal aberration involving MLF1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with NPM1/NPM. {ECO:0000269|PubMed:8570204}.; TISSUE SPECIFICITY: Most abundant in testis, ovary, skeletal muscle, heart, kidney and colon. Low expression in spleen, thymus and peripheral blood leukocytes.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;endometrium;larynx;bone;testis;brain;bladder;pineal gland;amygdala;unclassifiable (Anatomical System);heart;hypothalamus;muscle;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;alveolus;head and neck;kidney;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;caudate nucleus; 0.19151 0.11316 0.527368849 80.73248408 318.32634 3.78943 MLF2 0.921484672213679 0.078416369484898 9.8958301423105e-05 myeloid leukemia factor 2 . . TISSUE SPECIFICITY: Ubiquitously expressed.; myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;bladder;brain;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; amygdala;whole brain;medulla oblongata;occipital lobe;temporal lobe;pons;caudate nucleus;subthalamic nucleus;liver;prefrontal cortex;globus pallidus;kidney;cingulate cortex;parietal lobe;cerebellum; 0.42867 0.12378 -0.361761279 28.6329323 20.01153 0.68244 MLH1 0.739578311354265 0.260420832084964 8.56560772014109e-07 mutL homolog 1 FUNCTION: Heterodimerizes with PMS2 to form MutL alpha, a component of the post-replicative DNA mismatch repair system (MMR). DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH6) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS- heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Heterodimerizes with MLH3 to form MutL gamma which plays a role in meiosis. {ECO:0000269|PubMed:16873062, ECO:0000269|PubMed:18206974}.; DISEASE: Mismatch repair cancer syndrome (MMRCS) [MIM:276300]: An autosomal recessive, rare, childhood cancer predisposition syndrome encompassing a broad tumor spectrum. This includes hematological malignancies, central nervous system tumors, Lynch syndrome-associated malignancies such as colorectal tumors as well as multiple intestinal polyps, embryonic tumors and rhabdomyosarcoma. Multiple cafe-au-lait macules, a feature reminiscent of neurofibromatosis type 1, are often found as first manifestation of the underlying cancer. Areas of skin hypopigmentation have also been reported in MMRCS patients. {ECO:0000269|PubMed:17440981, ECO:0000269|PubMed:7661930}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Muir-Torre syndrome (MRTES) [MIM:158320]: Rare autosomal dominant disorder characterized by sebaceous neoplasms and visceral malignancy. {ECO:0000269|PubMed:8751876}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in MLH1 may contribute to lobular carcinoma in situ (LCIS), a non-invasive neoplastic disease of the breast.; DISEASE: Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of endometrium, the mucous lining of the uterus. Most endometrial cancers are adenocarcinomas, cancers that begin in cells that make and release mucus and other fluids. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=Some epigenetic changes can be transmitted unchanged through the germline (termed 'epigenetic inheritance'). Evidence that this mechanism occurs in humans is provided by the identification of individuals in whom 1 allele of the MLH1 gene is epigenetically silenced throughout the soma (implying a germline event). These individuals are affected by HNPCC but does not have identifiable mutations in MLH1, even though it is silenced, which demonstrates that an epimutation can phenocopy a genetic disease.; TISSUE SPECIFICITY: Colon, lymphocytes, breast, lung, spleen, testis, prostate, thyroid, gall bladder and heart.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;iris;pituitary gland;testis;brain;bladder;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;skeletal muscle; 0.71276 0.88182 0.512596355 80.29606039 1715.16552 7.63437 MLH3 0.000425002178066797 0.999505008262115 6.99895598186252e-05 mutL homolog 3 FUNCTION: Probably involved in the repair of mismatches in DNA.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:11317354}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;testis;dura mater;germinal center;spinal ganglion;brain;bladder;pineal gland;unclassifiable (Anatomical System);meninges;cartilage;tongue;islets of Langerhans;lens;skeletal muscle;pia mater;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;whole blood; 0.18623 0.15260 1.861141507 97.16324605 2004.72123 8.24605 MLIP 1.01588135455232e-11 0.0426144200481502 0.957385579941691 muscular LMNA-interacting protein . . TISSUE SPECIFICITY: Primarily expressed in heart and skeletal muscle. Also detected in liver. {ECO:0000269|PubMed:21498514}.; unclassifiable (Anatomical System);uterus;lung;heart;thyroid;testis;brain;skin; . 0.72786 . 0.244401822 69.50931824 1655.11076 7.51997 MLIP-AS1 . . . MLIP antisense RNA 1 . . . . . . . . . . . MLIP-IT1 . . . MLIP intronic transcript 1 . . . . . . . . . . . MLK7-AS1 . . . MLK7 antisense RNA 1 . . . . . . . . . . . MLKL 7.47865621818672e-14 0.0170431341565531 0.982956865843372 mixed lineage kinase domain-like FUNCTION: Pseudokinase that plays a key role in TNF-induced necroptosis, a programmed cell death process. Activated following phosphorylation by RIPK3, leading to homotrimerization, localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage. Does not have protein kinase activity. {ECO:0000269|PubMed:22265413, ECO:0000269|PubMed:22265414, ECO:0000269|PubMed:22421439, ECO:0000269|PubMed:24316671}.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;colon;skin;skeletal muscle;bile duct;uterus;pancreas;larynx;thyroid;bone;placenta;alveolus;liver;head and neck;spleen;germinal center;kidney;thymus; superior cervical ganglion;atrioventricular node; 0.02723 0.04872 0.957177419 90.14508139 93.23619 2.07786 MLLT1 0.991457207548845 0.00854080524480281 1.98720635194548e-06 myeloid/lymphoid or mixed-lineage leukemia; translocated to, 1 FUNCTION: Component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. {ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948}.; DISEASE: Note=A chromosomal aberration involving MLLT1 is associated with acute leukemias. Translocation t(11;19)(q23;p13.3) with KMT2A/MLL1. The result is a rogue activator protein.; . unclassifiable (Anatomical System);breast;lung;thyroid;colon;head and neck; superior cervical ganglion;uterus corpus;placenta;trigeminal ganglion;skeletal muscle; 0.20636 0.30727 -0.622676946 17.30950696 165.56508 2.81449 MLLT3 0.99559104959863 0.00440855587835513 3.94523014669062e-07 myeloid/lymphoid or mixed-lineage leukemia; translocated to, 3 FUNCTION: Component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. {ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948}.; DISEASE: Note=A chromosomal aberration involving MLLT3 is associated with acute leukemias. Translocation t(9;11)(p22;q23) with KMT2A/MLL1. The result is a rogue activator protein.; . unclassifiable (Anatomical System);meninges;ovary;islets of Langerhans;colon;skeletal muscle;skin;retina;pia mater;frontal lobe;bone;visual apparatus;hippocampus;liver;dura mater;kidney;brain;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.51420 0.20297 -0.359940251 28.93371078 58.09904 1.54192 MLLT4 0.999998021628688 1.9783713118175e-06 3.80916870071128e-20 myeloid/lymphoid or mixed-lineage leukemia; translocated to, 4 FUNCTION: Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton.; DISEASE: Note=A chromosomal aberration involving MLLT4 is associated with acute leukemias. Translocation t(6;11)(q27;q23) with KMT2A/MLL1. The result is a rogue activator protein.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;spinal cord;urinary;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;head and neck;spleen;kidney;mammary gland;aorta;stomach; uterus corpus;medulla oblongata;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.84566 0.37758 -2.357622074 1.138240151 317.70932 3.78412 MLLT4-AS1 . . . MLLT4 antisense RNA 1 (head to head) . . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10382971}.; . . . . . . . . MLLT6 0.998762157265753 0.00123784200547267 7.28774060496164e-10 myeloid/lymphoid or mixed-lineage leukemia; translocated to, 6 . DISEASE: Note=A chromosomal aberration involving MLLT6 is associated with acute leukemias. Translocation t(11;17)(q23;q21) with KMT2A/MLL1. The result is a rogue activator protein.; . lymphoreticular;smooth muscle;colon;skin;retina;uterus;prostate;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;lacrimal gland;islets of Langerhans;muscle;blood;skeletal muscle;breast;pancreas;lung;epididymis;adrenal gland;placenta;liver;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;atrioventricular node; 0.50287 0.15426 -0.020150552 52.25288983 264.58482 3.48969 MLLT10 0.999583699307582 0.000416300690321547 2.09646253381871e-12 myeloid/lymphoid or mixed-lineage leukemia; translocated to, 10 FUNCTION: Probably involved in transcriptional regulation. In vitro or as fusion protein with KMT2A/MLL1 has transactivation activity. Binds to cruciform DNA. {ECO:0000269|PubMed:17868029}.; DISEASE: Note=A chromosomal aberration involving MLLT10 is associated with diffuse histiocytic lymphomas. Translocation t(10;11)(p13;q14) with PICALM.; TISSUE SPECIFICITY: Expressed abundantly in testis.; unclassifiable (Anatomical System);ovary;islets of Langerhans;blood;skin;skeletal muscle;retina;bone marrow;uterus;lung;endometrium;thyroid;placenta;liver;testis;head and neck;spleen;germinal center;kidney;brain;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.67081 0.17676 -1.282303301 5.130927105 89.1514 2.02869 MLLT10P1 . . . myeloid/lymphoid or mixed-lineage leukemia; translocated to, 10 pseudogene 1 . . . . . . . . . . . MLLT10P2 . . . myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 10 pseudogene 2 . . . . . . . . . . . MLLT11 0.473311552387312 0.441156320720034 0.0855321268926536 myeloid/lymphoid or mixed-lineage leukemia; translocated to, 11 FUNCTION: Cofactor for the transcription factor TCF7 (PubMed:26079538). Involved in regulation of lymphoid development by driving multipotent hematopoietic progenitor cells towards a T cell fate (PubMed:21715312). {ECO:0000269|PubMed:21715312, ECO:0000269|PubMed:26079538}.; DISEASE: Note=A chromosomal aberration involving MLLT11 is found in acute leukemias. Translocation t(1;11)(q21;q23) with KMT2A/MLL1.; TISSUE SPECIFICITY: Expressed in myoepithelial cells of normal breast tissue (at protein level) (PubMed:26079538). Highly expressed in thymus (PubMed:7833468). Expressed in colon, small intestine, prostate and ovary. Not detected in peripheral blood lymphocytes and spleen (PubMed:7833468). {ECO:0000269|PubMed:26079538, ECO:0000269|PubMed:7833468}.; . . 0.12346 . 0.035072054 56.2514744 3.38586 0.12319 MLN 0.00165857384360036 0.461534840986229 0.536806585170171 motilin FUNCTION: Plays an important role in the regulation of interdigestive gastrointestinal motility and indirectly causes rhythmic contraction of duodenal and colonic smooth muscle.; . . stomach; superior cervical ganglion;liver;ciliary ganglion;skeletal muscle; 0.01681 0.07632 0.369407109 74.95281906 32.85418 1.01946 MLNR 0.0465876752547782 0.8544593720959 0.0989529526493222 motilin receptor FUNCTION: Receptor for motilin. {ECO:0000269|PubMed:11322507}.; . TISSUE SPECIFICITY: Expressed only in thyroid, stomach, and bone marrow.; unclassifiable (Anatomical System);testis; superior cervical ganglion; 0.19209 0.11347 . . 83.27787 1.93998 MLPH 0.00125354964830075 0.9969698425912 0.00177660776049879 melanophilin FUNCTION: Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor protein MYO5A. {ECO:0000269|PubMed:12062444}.; DISEASE: Griscelli syndrome 3 (GS3) [MIM:609227]: Rare autosomal recessive disorder characterized by pigmentary dilution of the skin and hair, the presence of large clumps of pigment in hair shafts, and an accumulation of melanosomes in melanocytes, without other clinical manifestations. {ECO:0000269|PubMed:12897212}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;prostate;trachea;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.49203 0.18515 0.494191824 79.62373201 636.84728 5.07635 MLST8 0.629654086289634 0.370039390831287 0.000306522879079415 MTOR associated protein, LST8 homolog FUNCTION: Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1- mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, LST8 interacts directly with MTOR and enhances its kinase activity. In nutrient- poor conditions, stabilizes the MTOR-RPTOR interaction and favors RPTOR-mediated inhibition of MTOR activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum- induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. {ECO:0000269|PubMed:12718876, ECO:0000269|PubMed:15467718}.; . TISSUE SPECIFICITY: Broadly expressed, with highest levels in skeletal muscle, heart and kidney. {ECO:0000269|PubMed:12408816}.; medulla oblongata;ovary;salivary gland;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; whole brain;prostate;cerebellum peduncles;thyroid;prefrontal cortex;testis; . . -0.448125345 24.19202642 21.33132 0.71976 MLX 0.469292431570312 0.525284190881133 0.0054233775485548 MLX, MAX dimerization protein FUNCTION: Transcription regulator. Forms a sequence-specific DNA- binding protein complex with MAD1, MAD4, MNT, WBSCR14 and MLXIP which recognizes the core sequence 5'-CACGTG-3'. The TCFL4-MAD1, TCFL4-MAD4, TCFL4-WBSCR14 complexes are transcriptional repressors. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation. {ECO:0000269|PubMed:10593926, ECO:0000269|PubMed:12446771, ECO:0000269|PubMed:16782875}.; . TISSUE SPECIFICITY: Expressed in all tissues tested, including spleen, thymus, prostate, ovary, intestine, colon, peripheral blood leukocyte, heart, liver, skeletal muscle and kidney. Lower levels of expression in testis, brain, placenta and lung. {ECO:0000269|PubMed:10593926}.; ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;germinal center;brain;gall bladder;heart;cartilage;tongue;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;placenta;duodenum;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;heart;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04989 0.13122 -0.007201372 53.19061099 3130.54792 10.64725 MLXIP 0.975747589022912 0.0242513532019434 1.05777514409684e-06 MLX interacting protein FUNCTION: Binds DNA as a heterodimer with MLX and activates transcription. Binds to the canonical E box sequence 5'-CACGTG-3'. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation. {ECO:0000250|UniProtKB:Q2VPU4, ECO:0000269|PubMed:12446771, ECO:0000269|PubMed:16782875}.; . TISSUE SPECIFICITY: Widely expressed in adult tissues. Most abundant in skeletal muscle. {ECO:0000269|PubMed:11073985}.; myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;brain;heart;urinary;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;colon;choroid;fovea centralis;uterus;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;small intestine;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;amnion;head and neck;kidney;stomach;aorta;cerebellum; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.16616 0.11073 . . 1241.38763 6.65087 MLXIPL 0.676823094036297 0.323136714776754 4.01911869489009e-05 MLX interacting protein like FUNCTION: Transcriptional repressor. Binds to the canonical and non-canonical E box sequences 5'-CACGTG-3' (By similarity). {ECO:0000250}.; DISEASE: Note=WBSCR14 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of WBSCR14 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease. {ECO:0000269|PubMed:10780788}.; TISSUE SPECIFICITY: Expressed in liver, heart, kidney, cerebellum and intestinal tissues.; unclassifiable (Anatomical System);medulla oblongata;islets of Langerhans;colon;parathyroid;uterus;pancreas;lung;cerebral cortex;endometrium;bone;visual apparatus;liver;testis;cervix;spleen;kidney;brain;stomach; dorsal root ganglion;adrenal cortex;testis;atrioventricular node; 0.73744 . 0.602602982 82.87331918 1395.13643 6.98704 MLYCD 0.000280848275880868 0.789285897071259 0.21043325465286 malonyl-CoA decarboxylase FUNCTION: Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation. {ECO:0000269|PubMed:10455107, ECO:0000269|PubMed:15003260, ECO:0000269|PubMed:18314420, ECO:0000269|PubMed:23482565}.; DISEASE: Malonyl-CoA decarboxylase deficiency (MLYCD deficiency) [MIM:248360]: Autosomal recessive disease characterized by abdominal pain, chronic constipation, episodic vomiting, metabolic acidosis and malonic aciduria. {ECO:0000269|PubMed:10417274}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in fibroblasts and hepatoblastoma cells (at protein level). Expressed strongly in heart, liver, skeletal muscle, kidney and pancreas. Expressed in myotubes. Expressed weakly in brain, placenta, spleen, thymus, testis, ovary and small intestine. {ECO:0000269|PubMed:10455107, ECO:0000269|PubMed:18314420}.; smooth muscle;ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; liver; 0.17570 0.17831 . . 204.97186 3.09234 MMAA 0.00318180827221776 0.985737088441782 0.0110811032860003 methylmalonic aciduria (cobalamin deficiency) cblA type FUNCTION: Probable GTPase. May function as chaperone. May be involved in the transport of cobalamin (Cbl) into mitochondria for the final steps of adenosylcobalamin (AdoCbl) synthesis.; . TISSUE SPECIFICITY: Widely expressed. Highest expression is observed in liver and skeletal muscle.; unclassifiable (Anatomical System);prostate;lung;whole body;cartilage;liver;testis;colon;spleen;kidney;brain;skeletal muscle; globus pallidus;atrioventricular node;trigeminal ganglion; 0.10781 0.09901 -0.690637458 15.12149092 559.05839 4.80219 MMAB 0.00387716022324201 0.852896852275611 0.143225987501147 methylmalonic aciduria (cobalamin deficiency) cblB type . . TISSUE SPECIFICITY: Expressed in liver and skeletal muscle.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);heart;hypothalamus;muscle;pharynx;blood;lens;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;aorta;stomach; dorsal root ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.20305 0.22303 0.328949044 73.41354093 2188.29828 8.61572 MMACHC 5.25633027461793e-14 0.00374905914489824 0.996250940855049 methylmalonic aciduria (cobalamin deficiency) cblC type, with homocystinuria FUNCTION: May be involved in the binding and intracellular trafficking of cobalamin (vitamin B12).; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in fetal liver. Also expressed in spleen, lymph node, thymus and bone marrow. Weakly or not expressed in peripheral blood leukocytes. {ECO:0000269|PubMed:16311595}.; . . 0.09288 0.16617 -0.134019284 43.90776126 493.57119 4.56840 MMADHC 0.02077684339759 0.961983388072452 0.0172397685299578 methylmalonic aciduria and homocystinuria, cblD type FUNCTION: Involved in cobalamin metabolism. {ECO:0000269|PubMed:18385497}.; . TISSUE SPECIFICITY: Widely expressed at high levels. {ECO:0000269|PubMed:18385497}.; myocardium;medulla oblongata;smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; testis - interstitial;testis; 0.17434 0.13266 0.483275131 79.25218212 308.88027 3.74082 MMD 0.0136446548070045 0.955351202958083 0.0310041422349128 monocyte to macrophage differentiation-associated FUNCTION: Involved in the dynamics of lysosomal membranes associated with microglial activation following brain lesion. {ECO:0000250}.; . TISSUE SPECIFICITY: Exhibits relatively ubiquitous expression with preferential expression in mature (in vitro differentiated) macrophages. {ECO:0000269|PubMed:16044242}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;uterus;whole body;frontal lobe;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;islets of Langerhans;hypothalamus;spinal cord;urinary;blood;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; amygdala;whole brain;occipital lobe;superior cervical ganglion;fetal brain;placenta;pons;caudate nucleus;cingulate cortex;parietal lobe; 0.43375 0.42641 -0.141298762 42.87567823 4.54236 0.16405 MMD2 0.00091686259327882 0.801573149446021 0.1975099879607 monocyte to macrophage differentiation associated 2 . . TISSUE SPECIFICITY: Shows restricted expression with highest levels in brain and testis. {ECO:0000269|PubMed:16044242}.; . . 0.09986 . -0.626318434 17.03231894 17.3922 0.61029 MME 2.19309064304115e-08 0.998611289353043 0.00138868871605033 membrane metallo-endopeptidase FUNCTION: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (PubMed:15283675, PubMed:8168535). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (PubMed:17101991). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 (PubMed:15283675). Involved in the degradation of atrial natriuretic factor (ANF) (PubMed:2531377, PubMed:2972276). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers (PubMed:20876573). {ECO:0000269|PubMed:15283675, ECO:0000269|PubMed:17101991, ECO:0000269|PubMed:20876573, ECO:0000269|PubMed:2531377, ECO:0000269|PubMed:2972276}.; . . lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;cerebral cortex;endometrium;larynx;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;pharynx;blood;skeletal muscle;pancreas;lung;cornea;mesenchyma;placenta;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;olfactory bulb;adipose tissue;kidney;atrioventricular node;whole blood;skeletal muscle; 0.80395 0.69624 -0.685180376 15.32200991 140.44703 2.58504 MME-AS1 . . . MME antisense RNA 1 . . . . . . . . . . . MMEL1 8.87673673427084e-13 0.864055213068136 0.135944786930977 membrane metallo-endopeptidase-like 1 FUNCTION: Metalloprotease involved in sperm function, possibly by modulating the processes of fertilization and early embryonic development. Degrades a broad variety of small peptides with a preference for peptides shorter than 3 kDa containing neutral bulky aliphatic or aromatic amino acid residues. Shares the same substrate specificity with MME and cleaves peptides at the same amide bond (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Predominantly expressed in testis. Weakly expressed in brain, kidney and heart. {ECO:0000269|PubMed:11560781}.; unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;developmental;colon;blood;uterus;breast;lung;bone;iris;testis;brain;mammary gland;stomach; . 0.08338 0.20014 -0.657684922 16.09459778 200.55931 3.06168 MMGT1 0.408287058485805 0.554383478846356 0.037329462667839 membrane magnesium transporter 1 FUNCTION: Mediates Mg(2+) transport. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;pineal body;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; subthalamic nucleus;atrioventricular node; 0.45286 0.10896 0.079165051 59.43029016 9.42062 0.34703 MMP1 2.48971498237184e-15 0.0023076482318425 0.997692351768155 matrix metallopeptidase 1 FUNCTION: Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity. {ECO:0000269|PubMed:1645757}.; . . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;colon;parathyroid;vein;skin;skeletal muscle;uterus;pancreas;whole body;lung;oesophagus;larynx;bone;placenta;liver;head and neck;kidney;aorta;stomach; lung;smooth muscle;heart;beta cell islets;atrioventricular node; 0.48655 0.80999 0.733063566 86.27034678 129.75686 2.48198 MMP2 0.791258492355506 0.208730431261586 1.10763829078663e-05 matrix metallopeptidase 2 FUNCTION: Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14.; FUNCTION: Isoform 2: Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro- inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.; DISEASE: Multicentric osteolysis, nodulosis, and arthropathy (MONA) [MIM:259600]: An autosomal recessive syndrome characterized by severe multicentric osteolysis with predominant involvement of the hands and feet. Additional features include coarse face, corneal opacities, patches of thickened, hyperpigmented skin, hypertrichosis and gum hypertrophy. {ECO:0000269|PubMed:11431697, ECO:0000269|PubMed:15691365, ECO:0000269|PubMed:16542393}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate. {ECO:0000269|PubMed:11751392}.; smooth muscle;ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;iris;amniotic fluid;brain;gall bladder;heart;cartilage;tongue;urinary;spinal cord;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;colon;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;synovium;bone;testis;unclassifiable (Anatomical System);muscle;bile duct;pancreas;lung;placenta;hypopharynx;amnion;head and neck;kidney;aorta;stomach; uterus;superior cervical ganglion;uterus corpus;adipose tissue;smooth muscle;heart;placenta;appendix;testis;fetal lung;trigeminal ganglion;skin; 0.87847 0.96194 -0.064242613 48.844067 187.45648 2.97359 MMP3 3.50440404382942e-08 0.325775147054244 0.674224817901716 matrix metallopeptidase 3 FUNCTION: Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.; DISEASE: Coronary heart disease 6 (CHDS6) [MIM:614466]: A multifactorial disease characterized by an imbalance between myocardial functional requirements and the capacity of the coronary vessels to supply sufficient blood flow. Decreased capacity of the coronary vessels is often associated with thickening and loss of elasticity of the coronary arteries. {ECO:0000269|PubMed:12477941, ECO:0000269|PubMed:8662692}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. A polymorphism in the MMP3 promoter region is associated with the risk of coronary heart disease and myocardial infarction, due to lower MMP3 proteolytic activity and higher extracellular matrix deposition in atherosclerotic lesions.; . unclassifiable (Anatomical System);medulla oblongata;cartilage;colon;skeletal muscle;skin;lung;endometrium;cornea;larynx;trabecular meshwork;bone;head and neck;stomach; ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12669 0.86628 -0.664951379 15.91177164 40.62824 1.19072 MMP7 1.6572045692897e-09 0.0617529363744917 0.938247061968304 matrix metallopeptidase 7 FUNCTION: Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase. {ECO:0000269|PubMed:2550050}.; . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;endometrium;thyroid;testis;amniotic fluid;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;breast;pancreas;lung;cornea;nasopharynx;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;beta cell islets;skeletal muscle; 0.08942 0.56774 0.330767508 73.53739089 662.47866 5.15860 MMP8 1.17621282658989e-19 0.000173027326382539 0.999826972673618 matrix metallopeptidase 8 FUNCTION: Can degrade fibrillar type I, II, and III collagens.; . TISSUE SPECIFICITY: Neutrophils.; unclassifiable (Anatomical System);liver;blood;skin;bone marrow; dorsal root ganglion;superior cervical ganglion;bone marrow; 0.13160 0.28283 1.576373448 95.7537155 358.71858 4.01127 MMP9 2.78769685742866e-08 0.489395135285362 0.510604836837669 matrix metallopeptidase 9 FUNCTION: May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide. {ECO:0000269|PubMed:1480034}.; DISEASE: Intervertebral disc disease (IDD) [MIM:603932]: A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain. {ECO:0000269|PubMed:18455130}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Metaphyseal anadysplasia 2 (MANDP2) [MIM:613073]: A bone development disorder characterized by skeletal anomalies that resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia. {ECO:0000269|PubMed:19615667}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Produced by normal alveolar macrophages and granulocytes.; . . 0.23955 0.97212 0.668743049 84.68388771 5737.9082 15.70339 MMP10 1.98053112611486e-13 0.00817930161176316 0.991820698388039 matrix metallopeptidase 10 FUNCTION: Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase.; . . unclassifiable (Anatomical System);heart;ovary;tongue;colon;vein;skin;skeletal muscle;uterus;lung;endometrium;larynx;epididymis;alveolus;hypopharynx;duodenum;head and neck; uterus corpus;testis - interstitial; 0.09719 0.63407 1.13538281 92.30360934 779.07324 5.52465 MMP11 6.59354935689745e-05 0.903908694140083 0.0960253703663486 matrix metallopeptidase 11 FUNCTION: May play an important role in the progression of epithelial malignancies.; . TISSUE SPECIFICITY: Specifically expressed in stromal cells of breast carcinomas.; ovary;colon;parathyroid;skin;uterus;prostate;whole body;oesophagus;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland; uterus;superior cervical ganglion;uterus corpus;placenta;pons;trigeminal ganglion;skeletal muscle; 0.21422 0.37763 -0.156065314 42.16206653 157.09784 2.73915 MMP12 . . . matrix metallopeptidase 12 FUNCTION: May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.; . TISSUE SPECIFICITY: Found in alveolar macrophages but not in peripheral blood monocytes.; unclassifiable (Anatomical System);colon;breast;uterus;pancreas;lung;endometrium;nasopharynx;thyroid;placenta;liver;head and neck;spleen;cervix;aorta;stomach; dorsal root ganglion;superior cervical ganglion;appendix;atrioventricular node;trigeminal ganglion; 0.15904 0.66783 . . . . MMP13 2.16777707829054e-05 0.903988305864836 0.0959900163643816 matrix metallopeptidase 13 FUNCTION: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CTGF. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CTGF. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion. {ECO:0000269|PubMed:16167086, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:19615667, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:8207000, ECO:0000269|PubMed:8576151, ECO:0000269|PubMed:8603731, ECO:0000269|PubMed:8663255, ECO:0000269|PubMed:9065415}.; DISEASE: Spondyloepimetaphyseal dysplasia Missouri type (SEMD-MO) [MIM:602111]: A bone disease characterized by moderate to severe metaphyseal changes, mild epiphyseal involvement, rhizomelic shortening of the lower limbs with bowing of the femora and/or tibiae, coxa vara, genu varum and pear-shaped vertebrae in childhood. Epimetaphyseal changes improve with age. {ECO:0000269|PubMed:16167086}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Metaphyseal anadysplasia 1 (MANDP1) [MIM:602111]: A bone development disorder characterized by skeletal anomalies that resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia. {ECO:0000269|PubMed:19615667}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Metaphyseal dysplasia, Spahr type (MDST) [MIM:250400]: An autosomal recessive, rare disease characterized by moderate short stature, mild genua vara, and radiographic signs of metaphyseal dysplasia, but no biochemical signs of rickets. {ECO:0000269|PubMed:24648384, ECO:0000269|PubMed:24781753}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in fetal cartilage and calvaria, in chondrocytes of hypertrophic cartilage in vertebrae and in the dorsal end of ribs undergoing ossification, as well as in osteoblasts and periosteal cells below the inner periosteal region of ossified ribs. Detected in chondrocytes from in joint cartilage that have been treated with TNF and IL1B, but not in untreated chondrocytes. Detected in T lymphocytes. Detected in breast carcinoma tissue. {ECO:0000269|PubMed:8207000, ECO:0000269|PubMed:8798568, ECO:0000269|PubMed:9056642, ECO:0000269|PubMed:9562863}.; unclassifiable (Anatomical System);smooth muscle;ovary;cartilage;tongue;parathyroid;bone marrow;prostate;whole body;lung;cochlea;internal ear;placenta;thyroid;bone;pituitary gland;middle ear; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.37295 0.63694 -0.955204708 9.170794999 109.30422 2.27054 MMP14 0.987123657228178 0.0128761202196609 2.2255216131877e-07 matrix metallopeptidase 14 FUNCTION: Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro- MMP2. {ECO:0000269|PubMed:12714657, ECO:0000269|PubMed:20837484, ECO:0000269|PubMed:22065321}.; DISEASE: Winchester syndrome (WNCHRS) [MIM:277950]: A disease characterized by severe osteolysis in the hands and feet, generalized osteoporosis, bone thinning, and absence of subcutaneous nodules. Various additional features include coarse face, corneal opacities, gum hypertrophy, and EKG changes. {ECO:0000269|PubMed:22922033}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors. {ECO:0000269|PubMed:18223680}.; unclassifiable (Anatomical System);lymphoreticular;smooth muscle;colon;fovea centralis;choroid;lens;skin;retina;uterus;breast;optic nerve;lung;larynx;placenta;thyroid;macula lutea;hypopharynx;head and neck;kidney;brain;mammary gland;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;smooth muscle;adipose tissue;heart;atrioventricular node;pons;skin;skeletal muscle;uterus corpus;trachea;placenta;appendix;ciliary ganglion;kidney;trigeminal ganglion;cingulate cortex;cerebellum; 0.54891 0.55746 0.04598748 57.47817882 1317.7477 6.82691 MMP15 0.651305092372326 0.348643802137726 5.11054899481725e-05 matrix metallopeptidase 15 FUNCTION: Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A. {ECO:0000269|PubMed:9461298}.; . TISSUE SPECIFICITY: Appeared to be synthesized preferentially in liver, placenta, testis, colon and intestine. Substantial amounts are also detected in pancreas, kidney, lung, heart and skeletal muscle.; ovary;colon;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;thyroid;bone;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;hippocampus;liver;duodenum;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;placenta;thyroid;testis;fetal thyroid;trigeminal ganglion; 0.08096 0.20321 -0.661316159 16.02382637 2268.35273 8.81222 MMP16 0.916974083764173 0.0830212274497754 4.68878605121261e-06 matrix metallopeptidase 16 FUNCTION: Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells. {ECO:0000269|PubMed:11278606}.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, ovary and small intestine. Isoform Short is found in the ovary.; unclassifiable (Anatomical System);lung;cartilage;heart;tongue;placenta;visual apparatus;testis;head and neck;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21595 0.19444 -0.381986487 27.68931352 33.08522 1.02452 MMP17 1.14744032526495e-06 0.570171312588168 0.429827539971507 matrix metallopeptidase 17 FUNCTION: Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin.; . TISSUE SPECIFICITY: Expressed in brain, leukocytes, colon, ovary testis and breast cancer. Expressed also in many transformed and non-transformed cell types.; unclassifiable (Anatomical System);amygdala;lymph node;lung;endometrium;hippocampus;colon;blood;brain;mammary gland;skin;retina; amygdala;prefrontal cortex;globus pallidus;caudate nucleus;skeletal muscle; 0.17978 0.20186 -0.325161626 30.92120783 2581.35279 9.50286 MMP19 1.45383844369831e-13 0.0251332872323478 0.974866712767507 matrix metallopeptidase 19 FUNCTION: Endopeptidase that degrades various components of the extracellular matrix, such as aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis. Hydrolyzes collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin. {ECO:0000269|PubMed:10809722, ECO:0000269|PubMed:10922468}.; . TISSUE SPECIFICITY: Expressed in mammary gland, placenta, lung, pancreas, ovary, small intestine, spleen, thymus, prostate, testis colon, heart and blood vessel walls. Not detected in brain and peripheral blood leukocytes. Also expressed in the synovial fluid of normal and rheumatoid patients (PubMed:8920941). {ECO:0000269|PubMed:8920941}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;uterus corpus;adipose tissue;placenta;fetal lung;pons;trigeminal ganglion;skeletal muscle; 0.44209 0.14603 -0.130380821 44.03161123 161.61686 2.77771 MMP20 1.62632042148573e-08 0.219975816214923 0.780024167521872 matrix metallopeptidase 20 FUNCTION: Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. {ECO:0000269|PubMed:10922468, ECO:0000269|PubMed:9398237}.; DISEASE: Amelogenesis imperfecta, hypomaturation type, 2A2 (AI2A2) [MIM:612529]: A defect of enamel formation. The disorder involves both primary and secondary dentitions. The teeth have a shiny agar jelly appearance and the enamel is softer than normal. Brown pigment is present in middle layers of enamel. {ECO:0000269|PubMed:15744043}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed specifically in the enamel organ.; unclassifiable (Anatomical System);lung;testis; dorsal root ganglion;uterus corpus;atrioventricular node; 0.06084 0.14127 1.423841958 94.96933239 1981.9007 8.20326 MMP21 3.21016423544875e-07 0.53538371623282 0.464615962750756 matrix metallopeptidase 21 FUNCTION: May have an important and specific function in tumor progression and embryogenesis. Cleaves alpha-1-antitrypsin.; . TISSUE SPECIFICITY: Identified in fetal brain, kidney and liver. In adult tissues found primarily in ovary, kidney, liver, lung, placenta, brain and peripheral blood leukocytes. Expressed as well in various cancer cell lines. {ECO:0000269|PubMed:12490321, ECO:0000269|PubMed:12617721}.; . . 0.09338 0.13098 -0.201976964 38.98325077 314.41591 3.77140 MMP23A . . . matrix metallopeptidase 23A (pseudogene) FUNCTION: Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Predominantly expressed in ovary, testis and prostate. {ECO:0000269|PubMed:9988691}.; uterus;myocardium;medulla oblongata;prostate;lung;whole body;heart;testis;colon;kidney; . 0.09338 0.16249 -0.201976964 38.98325077 . . MMP23B . . . matrix metallopeptidase 23B FUNCTION: Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Predominantly expressed in ovary, testis and prostate. {ECO:0000269|PubMed:9988691}.; pancreas;heart;placenta;spleen; . . 0.16249 . . 2.1497 0.07187 MMP24 0.0287623289506785 0.960471418966348 0.0107662520829736 matrix metallopeptidase 24 FUNCTION: Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence. Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia. Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence. May play a role in axonal growth. Able to activate progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Predominantly expressed in brain, kidney, pancreas and lung. Overexpressed in a series of brain tumors, including astrocytomas and glioblastomas. {ECO:0000269|PubMed:10363975}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pineal body;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;cervix;kidney;mammary gland;stomach;cerebellum; subthalamic nucleus;superior cervical ganglion;fetal brain;cerebellum peduncles;ciliary ganglion;trigeminal ganglion;cingulate cortex;cerebellum; 0.12575 0.15424 -0.622676946 17.30950696 146.60758 2.63812 MMP24-AS1 . . . MMP24 antisense RNA 1 . . . . . 0.43993 . . . . . MMP25 1.64577846493364e-06 0.859275983227905 0.14072237099363 matrix metallopeptidase 25 FUNCTION: May activate progelatinase A.; . TISSUE SPECIFICITY: Expressed predominantly in leukocytes, lung and spleen. Expressed also in colon carcinoma, astrocytoma and glioblastomas.; unclassifiable (Anatomical System);lung;heart;alveolus;testis;colon;spleen;blood;brain;mammary gland;bone marrow; thalamus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;whole blood;cingulate cortex;skeletal muscle; 0.42899 0.31045 -0.21856543 37.66218448 647.31237 5.10791 MMP25-AS1 . . . MMP25 antisense RNA 1 . . . . . . . . . . . MMP26 0.0221718840532987 0.910034403108323 0.0677937128383781 matrix metallopeptidase 26 FUNCTION: May hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin and alpha-1 proteinase inhibitor. Is also able to activate progelatinase B.; . TISSUE SPECIFICITY: Expressed specifically in uterus and placenta. Is also widely expressed in malignant tumors from different sources as well as in diverse tumor cell lines.; unclassifiable (Anatomical System);medulla oblongata;ovary;endometrium;placenta;parathyroid; dorsal root ganglion;superior cervical ganglion; 0.03443 0.10320 0.373041938 75.29488087 886.55948 5.80023 MMP27 2.34681280025563e-10 0.135019211392543 0.864980788372776 matrix metallopeptidase 27 FUNCTION: Matrix metalloproteinases degrade protein components of the extracellular matrix such as fibronectin, laminin, gelatins and/or collagens. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in B-cells (PubMed:14506071). Expressed in a subset of endometrial macrophages related to menstruation and in ovarian and peritoneal endometriotic lesions (at protein level)(PubMed:24810263). {ECO:0000269|PubMed:14506071, ECO:0000269|PubMed:24810263}.; uterus;heart;skin; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.10183 0.11847 1.179479654 92.79311158 3648.05472 11.73391 MMP28 0.000139259587966798 0.238350313523973 0.76151042688806 matrix metallopeptidase 28 FUNCTION: Can degrade casein. Could play a role in tissues homeostasis and repair.; . TISSUE SPECIFICITY: Expressed at high levels in testes and lung. Low levels are detected in kidney, pancreas and skin. Also expressed in fetal lung, brain, skeletal muscle and kidney. Expressed selectively in keratinocytes. Widely expressed in several carcinomas as well. Is up-regulated in response to injury in the skin.; unclassifiable (Anatomical System);myocardium;medulla oblongata;cartilage;colon;fovea centralis;choroid;lens;retina;pancreas;prostate;optic nerve;lung;larynx;placenta;bone;macula lutea;testis;cervix;brain;stomach; superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion; 0.08032 0.20389 0.21326276 67.71644256 27.51027 0.88618 MMRN1 9.35082142599867e-17 0.00883523144061894 0.991164768559381 multimerin 1 FUNCTION: Carrier protein for platelet (but not plasma) factor V/Va. Plays a role in the storage and stabilization of factor V in platelets. Upon release following platelet activation, may limit platelet and plasma factor Va-dependent thrombin generation. Ligand for integrin alpha-IIb/beta-3 and integrin alpha-V/beta-3 on activated platelets, and may function as an extracellular matrix or adhesive protein. {ECO:0000269|PubMed:16363244, ECO:0000269|PubMed:19132231, ECO:0000269|PubMed:7629143}.; DISEASE: Note=Deficiency in multimerin-1 due to proteolytic degradation within the platelet alpha granules is associated with an autosomal dominant bleeding disorder (factor V Quebec). {ECO:0000269|PubMed:8652809}.; TISSUE SPECIFICITY: Synthesized by endothelial cells and megakaryocytes. Stored in platelet alpha granules and endothelial cell Weibel-Palade bodies, following activation of these cells, it is released and attached to megakaryocytes, platelets, endothelium and subendothelium of blood vessels. Not found in plasma. Found in vascular tissues such as placenta, lung, and liver. {ECO:0000269|PubMed:7629143, ECO:0000269|PubMed:8514871}.; unclassifiable (Anatomical System);cartilage;heart;small intestine;islets of Langerhans;vein;skin;skeletal muscle;uterus;prostate;optic nerve;whole body;lung;nasopharynx;visual apparatus;duodenum;liver;testis;spleen;spinal ganglion;brain;aorta;tonsil;gall bladder; appendix;skeletal muscle; 0.13885 0.16819 0.347157132 73.79688606 483.52708 4.52727 MMRN2 2.4897545819111e-10 0.253584448631956 0.746415551119069 multimerin 2 FUNCTION: Inhibits endothelial cells motility and acts as a negative regulator of angiogenesis; it downregulates KDR activation by binding VEGFA. {ECO:0000269|PubMed:22020326}.; . TISSUE SPECIFICITY: Endothelium. {ECO:0000269|PubMed:11559704}.; . . 0.12982 0.09752 -0.505170032 21.79759377 1879.00646 7.97170 MMS19 0.831821999461453 0.168177950075242 5.04633048788238e-08 MMS19 homolog, cytosolic iron-sulfur assembly component FUNCTION: Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription. As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery. {ECO:0000269|PubMed:11071939, ECO:0000269|PubMed:11328871, ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:22678361, ECO:0000269|PubMed:22678362}.; . TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in testis. {ECO:0000269|PubMed:11071939, ECO:0000269|PubMed:11328871}.; ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;testis; 0.21908 . -0.014692675 52.35314933 3051.13847 10.50027 MMS22L 0.671142491080048 0.328857506005889 2.91406354411424e-09 MMS22 like, DNA repair protein FUNCTION: Component of the MMS22L-TONSL complex, a complex that stimulates the recombination-dependent repair of stalled or collapsed replication forks. The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication by promoting homologous recombination-mediated repair of replication fork- associated double-strand breaks. It may act by mediating the assembly of RAD51 filaments on ssDNA. {ECO:0000269|PubMed:21055983, ECO:0000269|PubMed:21055984, ECO:0000269|PubMed:21055985}.; . . unclassifiable (Anatomical System);uterus;lung;ovary;heart;bone;testis;cervix;mammary gland;skin; . 0.11262 . 0.319642692 72.82967681 4046.66353 12.60320 MMVP1 . . . myxomatous mitral valve prolapse 1 . . . . . . . . . . . MMVP2 . . . myxomatous mitral valve prolapse 2 . . . . . . . . . . . MN1 . . . meningioma (disrupted in balanced translocation) 1 FUNCTION: Transcriptional activator which specifically regulates expression of TBX22 in the posterior region of the developing palate. Required during later stages of palate development for growth and medial fusion of the palatal shelves. Promotes maturation and normal function of calvarial osteoblasts, including expression of the osteoclastogenic cytokine TNFSF11/RANKL. Necessary for normal development of the membranous bones of the skull (By similarity). May play a role in tumor suppression (Probable). {ECO:0000250|UniProtKB:D3YWE6, ECO:0000305|PubMed:7731706}.; DISEASE: Note=A chromosomal aberration involving MN1 may be a cause of acute myeloid leukemia (AML). Translocation t(12;22)(p13;q11) with ETV6. {ECO:0000269|PubMed:7731705}.; DISEASE: Note=Defects in MN1 involved in the development of meningiomas, slowly growing benign tumors derived from the arachnoidal cap cells of the leptomeninges, the soft coverings of the brain and spinal cord. Meningiomas are believed to be the most common primary tumors of the central nervous system in man. {ECO:0000269|PubMed:7731706}.; . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;skin;skeletal muscle;uterus;optic nerve;lung;cochlea;placenta;liver;testis;head and neck;kidney;brain;aorta;stomach; medulla oblongata;superior cervical ganglion;fetal brain;appendix;caudate nucleus;pons;skeletal muscle; 0.29108 . . . 959.02985 5.99624 MNAT1 3.96573933428392e-12 0.012862658704785 0.987137341291249 MNAT1, CDK activating kinase assembly factor FUNCTION: Stabilizes the cyclin H-CDK7 complex to form a functional CDK-activating kinase (CAK) enzymatic complex. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II. {ECO:0000269|PubMed:10024882}.; . TISSUE SPECIFICITY: Highest levels in colon and testis. Moderate levels are present thymus, prostate, ovary, and small intestine. The lowest levels are found in spleen and leukocytes.; umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;kidney;mammary gland;stomach;aorta; occipital lobe;pons;cingulate cortex; 0.90941 0.28104 -0.139478553 43.29440906 41.98331 1.22297 MND1 1.27812915374527e-05 0.610561521972746 0.389425696735716 meiotic nuclear divisions 1 FUNCTION: Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination during meiosis (By similarity). Stimulates both DMC1- and RAD51-mediated homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks. {ECO:0000250|UniProtKB:Q8K396, ECO:0000269|PubMed:16407260}.; . . unclassifiable (Anatomical System);smooth muscle;lymph node;ovary;salivary gland;intestine;pharynx;colon;blood;uterus;prostate;lung;bone;visual apparatus;liver;testis;kidney;brain;bladder;stomach; dorsal root ganglion;tumor;atrioventricular node;skeletal muscle; 0.56425 0.11102 -0.251530012 35.42108988 49.79072 1.38394 MNDA 7.23077353015599e-11 0.0191281715971344 0.980871828330558 myeloid cell nuclear differentiation antigen FUNCTION: May act as a transcriptional activator/repressor in the myeloid lineage. Plays a role in the granulocyte/monocyte cell- specific response to interferon. Stimulates the DNA binding of the transcriptional repressor protein YY1.; . TISSUE SPECIFICITY: Expressed constitutively in cells of the myeloid lineage. Found in promyelocyte stage cells as well as in all other stage cells including peripheral blood monocytes and granulocytes. Also appear in myeloblast cells in some cases of acute myeloid Leukemia. {ECO:0000269|PubMed:8175894}.; . . 0.07316 0.09787 0.198490371 67.30360934 173.57037 2.86960 MNS1 5.52556154828089e-14 0.027356564023119 0.972643435976826 meiosis specific nuclear structural 1 FUNCTION: May play a role in the control of meiotic division and germ cell differentiation through regulation of pairing and recombination during meiosis. {ECO:0000250}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;testis;bladder;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;kidney; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10262 0.11474 0.132352165 63.48785091 362.55925 4.03201 MNT 0.96048045983846 0.0394331804764303 8.63596851100192e-05 MAX network transcriptional repressor FUNCTION: Binds DNA as a heterodimer with MAX and represses transcription. Binds to the canonical E box sequence 5'-CACGTG-3' and, with higher affinity, to 5'-CACGCG-3'.; . . unclassifiable (Anatomical System);lung;lacrimal gland;blood;germinal center;bone marrow; amygdala;subthalamic nucleus;globus pallidus; 0.39337 0.10229 -0.756778259 13.44656759 319.6925 3.79741 MNX1 . . . motor neuron and pancreas homeobox 1 FUNCTION: Putative transcription factor involved in pancreas development and function.; . TISSUE SPECIFICITY: Expressed in lymphoid and pancreatic tissues.; unclassifiable (Anatomical System);pancreas;lung;islets of Langerhans;colon;stomach; beta cell islets;ciliary ganglion; 0.36239 . . . 18.67801 0.64518 MNX1-AS1 . . . MNX1 antisense RNA 1 (head to head) . . . . . . . . . . . MNX1-AS2 . . . MNX1 antisense RNA 2 . . . . . . . . . . . MOAP1 0.00140363613553352 0.663920629406613 0.334675734457853 modulator of apoptosis 1 FUNCTION: Required for death receptor-dependent apoptosis. When associated with RASSF1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF10 stimulation. {ECO:0000269|PubMed:15949439}.; . TISSUE SPECIFICITY: Widely expressed, with high levels in heart and brain. {ECO:0000269|PubMed:19366867}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;whole body;frontal lobe;cerebral cortex;endometrium;synovium;thyroid;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;cerebellum; amygdala;whole brain;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.19634 0.15764 0.639420866 83.8995046 91.52402 2.05748 MOB1A 0.853010254514718 0.144565336562317 0.00242440892296485 MOB kinase activator 1A FUNCTION: Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38 and STK38L. Acts cooperatively with STK3/MST2 to activate STK38. {ECO:0000269|PubMed:15197186, ECO:0000269|PubMed:18362890, ECO:0000269|PubMed:19739119}.; . TISSUE SPECIFICITY: Adrenal gland, bone marrow, brain, placenta, prostate, salivary gland, skeletal muscle, testis, thymus, thyroid gland, heart, spinal cord, fetal brain and fetal liver. {ECO:0000269|PubMed:19739119}.; . . 0.73699 0.14582 -0.009020804 52.8544468 4.3605 0.15829 MOB1AP1 . . . MOB kinase activator 1A pseudogene 1 . . . . . . . . . . . MOB1AP2 . . . MOB kinase activator 1A pseudogene 2 . . . . . . . . . . . MOB1B 0.00797371498062726 0.786007549493484 0.206018735525889 MOB kinase activator 1B FUNCTION: Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38L. {ECO:0000269|PubMed:15067004, ECO:0000269|PubMed:19739119}.; . TISSUE SPECIFICITY: Adrenal gland, bone marrow, brain, lung, placenta, prostate, salivary gland, skeletal muscle, testis, thymus, thyroid gland, uterus, colon with mucosa, fetal brain and fetal liver. {ECO:0000269|PubMed:19739119}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;lung;trabecular meshwork;placenta;visual apparatus;liver;alveolus;kidney;mammary gland; . 0.51845 0.10077 -0.207437529 38.2814343 10.66649 0.38714 MOB2 0.641498728519639 0.352045824426503 0.00645544705385823 MOB kinase activator 2 FUNCTION: Stimulates the autophosphorylation and kinase activity of STK38 and STK38L. {ECO:0000269|PubMed:15067004}.; . . smooth muscle;ovary;colon;substantia nigra;vein;skin;retina;prostate;optic nerve;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;bile duct;pancreas;lung;placenta;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; globus pallidus;trigeminal ganglion; . . -0.449946534 24.00330267 69.28198 1.72432 MOB3A 0.002927403350296 0.581043643048751 0.416028953600953 MOB kinase activator 3A FUNCTION: May regulate the activity of kinases. {ECO:0000250}.; . . lymphoreticular;ovary;colon;substantia nigra;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;thyroid;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;aorta;thymus; . 0.11462 . -0.246069119 36.06982779 53.79943 1.46190 MOB3B 0.0303777770401778 0.809387473821484 0.160234749138338 MOB kinase activator 3B FUNCTION: May regulate the activity of kinases. {ECO:0000250}.; . . ovary;colon;parathyroid;skin;retina;uterus;prostate;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;spinal cord;lens;bile duct;pancreas;lung;epididymis;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus; skeletal muscle; 0.36665 0.11262 0.014844891 54.94810097 38.00866 1.12866 MOB3C 0.0340049542449835 0.927563967863623 0.0384310778913931 MOB kinase activator 3C FUNCTION: May regulate the activity of kinases. {ECO:0000250}.; . . medulla oblongata;smooth muscle;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;thyroid;bone;iris;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;trigeminal ganglion; 0.29932 0.11262 0.749657564 86.56522765 772.68593 5.50173 MOB4 0.777832909994367 0.220599257674469 0.00156783233116359 MOB family member 4, phocein FUNCTION: May play a role in membrane trafficking, specifically in membrane budding reactions. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; dorsal root ganglion;medulla oblongata;occipital lobe;superior cervical ganglion;adrenal cortex;atrioventricular node;pons;skeletal muscle;adrenal gland;placenta;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.22402 0.15588 -0.009020804 52.8544468 . . MOBP 0.592010032536213 0.368084899976214 0.0399050674875728 myelin-associated oligodendrocyte basic protein FUNCTION: May play a role in compacting or stabilizing the myelin sheath, possibly by binding the negatively charged acidic phospholipids of the cytoplasmic membrane. {ECO:0000250}.; . . amygdala;unclassifiable (Anatomical System);lung;frontal lobe;hippocampus;testis;brain; amygdala;whole brain;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.09965 0.12884 0.035072054 56.2514744 7.47275 0.27759 MOCOS 6.10346244046287e-07 0.968000788271662 0.0319986013820944 molybdenum cofactor sulfurase FUNCTION: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. In vitro, the C-terminal domain is able to reduce N-hydroxylated prodrugs, such as benzamidoxime. {ECO:0000255|HAMAP-Rule:MF_03050, ECO:0000269|PubMed:16973608}.; DISEASE: Xanthinuria 2 (XU2) [MIM:603592]: A disorder characterized by excretion of very large amounts of xanthine in the urine and a tendency to form xanthine stones. Uric acid is strikingly diminished in serum and urine. In addition, patients suffering of xanthinuria 2 cannot metabolize allopurinol into oxypurinol due to dual deficiency of xanthine dehydrogenase and aldehyde oxidase. {ECO:0000269|PubMed:11302742, ECO:0000269|PubMed:14624414, ECO:0000269|PubMed:17368066, ECO:0000269|Ref.11}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;heart;salivary gland;intestine;pharynx;colon;parathyroid;blood;skin;breast;uterus;prostate;lung;bone;thyroid;placenta;visual apparatus;liver;cervix;head and neck;kidney;brain;bladder;stomach; superior cervical ganglion;liver;atrioventricular node;trigeminal ganglion; 0.12530 0.15110 1.719633471 96.49091767 3793.86145 12.08539 MOCS1 0.000969834096250532 0.944103195842034 0.0549269700617154 molybdenum cofactor synthesis 1 FUNCTION: Isoform MOCS1A and isoform MOCS1B probably form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z). {ECO:0000269|PubMed:11891227}.; DISEASE: Molybdenum cofactor deficiency, complementation group A (MOCODA) [MIM:252150]: An autosomal recessive metabolic disorder leading to the pleiotropic loss of molybdoenzyme activities. It is clinically characterized by onset in infancy of poor feeding, intractable seizures, severe psychomotor retardation, and death in early childhood in most patients. {ECO:0000269|PubMed:12754701, ECO:0000269|PubMed:16021469, ECO:0000269|PubMed:9731530, ECO:0000269|PubMed:9921896}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform MOCS1A and isoform 2 are widely expressed. {ECO:0000269|PubMed:12208140, ECO:0000269|PubMed:9731530}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;iris;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;spinal cord;pharynx;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;hippocampus;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;peripheral nerve;cerebellum; superior cervical ganglion;liver;trigeminal ganglion;skeletal muscle; 0.05245 0.13458 0.112125503 62.09601321 1286.77948 6.75269 MOCS1P1 . . . molybdenum cofactor synthesis 1 pseudogene 1 . . . . . . . . . . . MOCS2 0.0404518496138402 0.842456407227278 0.117091743158882 molybdenum cofactor synthesis 2 FUNCTION: Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group. {ECO:0000255|HAMAP-Rule:MF_03052, ECO:0000269|PubMed:12732628, ECO:0000269|PubMed:15073332}.; . TISSUE SPECIFICITY: Highest levels are found in heart and skeletal muscle. Lower levels are present in brain, kidney and pancreas. Very low levels are found in lung and peripheral blood leukocytes. {ECO:0000269|PubMed:10053003}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;bile duct;lung;pia mater;cornea;adrenal gland;placenta;kidney;aorta;stomach; amygdala;occipital lobe;prefrontal cortex;caudate nucleus;kidney;parietal lobe; 0.06955 0.17480 0.527368849 80.73248408 319.54879 3.79634 MOCS3 1.13606849844989e-05 0.361997761788619 0.637990877526397 molybdenum cofactor synthesis 3 FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. {ECO:0000255|HAMAP-Rule:MF_03049, ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:19017811}.; . . unclassifiable (Anatomical System);lymphoreticular;medulla oblongata;adrenal cortex;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;endometrium;placenta;macula lutea;hippocampus;testis;spleen;mammary gland;brain;gall bladder;cerebellum; superior cervical ganglion;globus pallidus;atrioventricular node; 0.18836 0.19563 -0.358119787 29.16371786 58.74896 1.55492 MOCS3P1 . . . molybdenum cofactor synthesis 3 pseudogene 1 . . . . . . . . . . . MOCS3P2 . . . molybdenum cofactor synthesis 3 pseudogene 2 . . . . . . . . . . . MOG 0.103680312661872 0.889321575289883 0.00699811204824536 myelin oligodendrocyte glycoprotein FUNCTION: Mediates homophilic cell-cell adhesion (By similarity). Minor component of the myelin sheath. May be involved in completion and/or maintenance of the myelin sheath and in cell- cell communication. {ECO:0000250}.; . TISSUE SPECIFICITY: Found exclusively in the CNS, where it is localized on the surface of myelin and oligodendrocyte cytoplasmic membranes.; . . 0.47310 . 0.859896574 88.62349611 1003.46673 6.10083 MOGAT1 2.12658352177613e-06 0.273948797184795 0.726049076231683 monoacylglycerol O-acyltransferase 1 FUNCTION: Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Probably not involved in absorption of dietary fat in the small intestine (By similarity). {ECO:0000250}.; . . . . 0.15446 0.08618 0.775339069 87.13729653 2012.08574 8.25793 MOGAT2 0.218649112879292 0.772932608058237 0.00841827906247086 monoacylglycerol O-acyltransferase 2 FUNCTION: Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity. {ECO:0000269|PubMed:12621063}.; . TISSUE SPECIFICITY: Highly expressed in liver, small intestine, colon, stomach and kidney. {ECO:0000269|PubMed:12621063, ECO:0000269|PubMed:12824082}.; unclassifiable (Anatomical System);colon;skeletal muscle;stomach; . 0.19433 0.09948 0.97558591 90.37508846 794.49974 5.55805 MOGAT3 2.40335585035369e-10 0.0201417139208159 0.979858285838848 monoacylglycerol O-acyltransferase 3 FUNCTION: Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Also able to catalyze the terminal step in triacylglycerol synthesis by using diacylglycerol and fatty acyl-CoA as substrates. Has a preference toward palmitoyl-CoA and oleoyl-CoA. May be involved in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. {ECO:0000269|PubMed:12618427}.; . TISSUE SPECIFICITY: Selectively expressed in the digestive system. Highly expressed in the ileum, and at lower level in jejunum, duodenum, colon, cecum and the rectum. Not expressed in the stomach and the esophagus and trachea. Expressed at very low level in liver. {ECO:0000269|PubMed:12618427}.; unclassifiable (Anatomical System);colon; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.25469 0.10813 0.218717575 68.27081859 360.93757 4.02135 MOGS 3.25166586108679e-09 0.505438901677738 0.494561095070596 mannosyl-oligosaccharide glucosidase FUNCTION: Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor in a highly specific manner.; DISEASE: Type IIb congenital disorder of glycosylation (CDGIIb) [MIM:606056]: Characterized by marked generalized hypotonia and hypomotility of the neonate, dysmorphic features, including a prominent occiput, short palpebral fissures, retrognathia, high arched palate, generalized edema, and hypoplastic genitalia. Symptoms of the infant included hepatomegaly, hypoventilation, feeding problems and seizures. The clinical course was progressive and the infant did not survive more than a few months. {ECO:0000269|PubMed:10788335}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;spinal cord;urinary;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;placenta; . . 1.133561642 92.28591649 454.95313 4.43259 MOK 5.96438032193124e-17 0.00183066609027121 0.998169333909729 MOK protein kinase FUNCTION: Able to phosphorylate several exogenous substrates and to undergo autophosphorylation. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in heart, brain, lung, kidney, and pancreas, and at very low levels in placenta, liver and skeletal muscle. Detected in retina.; ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;lens;pancreas;lung;placenta;macula lutea;liver;kidney;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;parietal lobe; 0.14379 . 1.023320772 91.04741684 2990.39023 10.37744 MON1A 0.00636811048934964 0.973991798703935 0.019640090806715 MON1 homolog A, secretory trafficking associated FUNCTION: Plays an important in membrane trafficking through the secretory apparatus. Not involved in endocytic trafficking to lysosomes (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymphoreticular;cartilage;ovary;salivary gland;colon;skin;uterus;pancreas;prostate;lung;bone;placenta;visual apparatus;iris;testis;cervix;spleen;germinal center;kidney;brain;mammary gland; thyroid; 0.28281 0.10472 -0.578583623 18.71903751 57.82324 1.53654 MON1B 0.229740475197793 0.768694064875337 0.00156545992687021 MON1 homolog B, secretory trafficking associated . . . medulla oblongata;ovary;colon;skin;retina;bone marrow;uterus;prostate;cerebral cortex;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;muscle;blood;skeletal muscle;breast;pancreas;lung;placenta;hippocampus;liver;amnion;spleen;head and neck;cervix;kidney;stomach; . 0.06754 0.10285 -0.907472583 10.07313046 134.73036 2.52267 MON2 0.982708262602224 0.0172917373977232 5.28514742851255e-14 MON2 homolog, regulator of endosome-to-Golgi trafficking FUNCTION: May be required for traffic between late Golgi and early endosomes. {ECO:0000250}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;cochlea;thyroid;bone;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;lacrimal gland;islets of Langerhans;urinary;spinal cord;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;medulla oblongata;atrioventricular node;trigeminal ganglion;fetal thyroid;parietal lobe;skeletal muscle;cingulate cortex; 0.37081 0.10848 -0.834069467 11.49445624 7838.39289 19.07509 MORC1 0.000240876467310313 0.999752643924723 6.47960796673609e-06 MORC family CW-type zinc finger 1 FUNCTION: Required for spermatogenesis. {ECO:0000250|UniProtKB:Q9WVL5}.; . . unclassifiable (Anatomical System);testis; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skin;parietal lobe;skeletal muscle; 0.06655 0.09880 0.494191824 79.62373201 3103.27543 10.59600 MORC1-AS1 . . . MORC1 antisense RNA 1 . . . . . . . . . . . MORC2 0.999967480342235 3.25196577439514e-05 2.07997303366644e-14 MORC family CW-type zinc finger 2 FUNCTION: Exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY, possibly preventing its dephosphorylation (PubMed:24286864). May act as a transcriptional repressor (PubMed:20225202). Down-regulates CA9 expression (PubMed:20110259). {ECO:0000269|PubMed:20110259, ECO:0000269|PubMed:20225202, ECO:0000269|PubMed:24286864}.; . TISSUE SPECIFICITY: Highly expressed in smooth muscle, pancreas and testis.; lymphoreticular;smooth muscle;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;thyroid;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;lens;breast;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.41624 0.10960 -1.684662147 2.630337344 84.18167 1.95319 MORC2-AS1 . . . MORC2 antisense RNA 1 . . . . . . . . . . . MORC3 0.999874192317744 0.000125807679481262 2.77474496438007e-12 MORC family CW-type zinc finger 3 FUNCTION: Nuclear factor which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism (PubMed:20501696). Sumoylated MORC3-NBs can also associate with PML-NBs (PubMed:20501696). Recruits TP53 and SP100 to PML-NBs, thus regulating TP53 activity (PubMed:17332504). Binds RNA in vitro (PubMed:11927593). May be required for influenza A transcription during viral infection (PubMed:26202233). {ECO:0000269|PubMed:11927593, ECO:0000269|PubMed:17332504, ECO:0000269|PubMed:20501696, ECO:0000269|PubMed:26202233}.; . TISSUE SPECIFICITY: Expressed in heart, placenta, skeletal muscle, brain, pancreas, lung, liver, but not kidney. {ECO:0000269|PubMed:11927593}.; . . 0.58926 0.11049 -0.710864321 14.5730125 49.01849 1.36809 MORC4 0.993467674426918 0.0065322833500342 4.22230474379083e-08 MORC family CW-type zinc finger 4 . . TISSUE SPECIFICITY: Expressed at low levels in normal tissues, with highest expression levels in placenta and testis. Expression is significantly increased in subset of diffuse large B-cell lymphomas. {ECO:0000269|PubMed:17608765}.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;skin;retina;breast;uterus;prostate;lung;cochlea;endometrium;larynx;thyroid;placenta;liver;testis;head and neck;kidney;spinal ganglion;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;placenta;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.15522 0.08297 -0.356299879 29.31115829 61.37534 1.59642 MORF4 . . . mortality factor 4 (pseudogene) . . . . . . 0.19621 . . . . MORF4L1 0.802941002940311 0.197012433401919 4.65636577706866e-05 mortality factor 4 like 1 FUNCTION: Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Also component of the mSin3A complex which acts to repress transcription by deacetylation of nucleosomal histones. Required for homologous recombination repair (HRR) and resistance to mitomycin C (MMC). Involved in the localization of PALB2, BRCA2 and RAD51, but not BRCA1, to DNA-damage foci. {ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:20332121}.; . . myocardium;lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;gum;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; amygdala;medulla oblongata;thalamus;fetal brain;hypothalamus;temporal lobe;prefrontal cortex;globus pallidus;testis;parietal lobe;cingulate cortex;cerebellum; . 0.19621 -0.05129383 49.75819769 26.79444 0.86689 MORF4L1P1 . . . mortality factor 4 like 1 pseudogene 1 . . . . . . . . . . . MORF4L1P2 . . . mortality factor 4 like 1 pseudogene 2 . . . . . . . . . . . MORF4L1P3 . . . mortality factor 4 like 1 pseudogene 3 . . . . . . . . . . . MORF4L1P4 . . . mortality factor 4 like 1 pseudogene 4 . . . . . . . . . . . MORF4L1P5 . . . mortality factor 4 like 1 pseudogene 5 . . . . . . . . . . . MORF4L1P6 . . . mortality factor 4 like 1 pseudogene 6 . . . . . . . . . . . MORF4L1P7 . . . mortality factor 4 like 1 pseudogene 7 . . . . . . . . . . . MORF4L2 0.636394719546278 0.335007239196296 0.0285980412574262 mortality factor 4 like 2 FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Also component of the MSIN3A complex which acts to repress transcription by deacetylation of nucleosomal histones.; . . myocardium;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;occipital lobe;prefrontal cortex;globus pallidus; 0.48688 0.09554 -0.053113545 49.38664779 7.49271 0.27830 MORF4L2-AS1 . . . MORF4L2 antisense RNA 1 . . . . . . . . . . . MORF4L2P1 . . . mortality factor 4 like 2 pseudogene 1 . . . . . . . . . . . MORN1 7.87931445985798e-07 0.728750567696362 0.271248644372192 MORN repeat containing 1 . . . . . 0.07005 0.08705 -0.08446956 47.15145081 143.76824 2.61373 MORN2 . . . MORN repeat containing 2 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;endometrium;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;hypothalamus;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;visual apparatus;liver;alveolus;kidney;stomach; . 0.18872 0.09032 0.389637587 75.75489502 541.51493 4.73957 MORN3 1.82555353991208e-06 0.25327952587189 0.74671864857457 MORN repeat containing 3 . . . unclassifiable (Anatomical System);placenta;visual apparatus;testis;vein; . 0.09413 . -0.115612493 45.12856806 49.06116 1.36870 MORN4 0.182745760595456 0.764798605007906 0.0524556343966379 MORN repeat containing 4 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;whole body;bone;testis;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;bile duct;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach; ciliary ganglion; 0.13547 0.08087 -0.09720619 46.20193442 49.33279 1.37388 MORN5 0.00166333543671728 0.699986315975997 0.298350348587286 MORN repeat containing 5 . . . . . 0.08475 . 0.238945317 69.20853975 52.60039 1.43648 MOS 0.149307838238506 0.777668895594908 0.0730232661665856 v-mos Moloney murine sarcoma viral oncogene homolog . . TISSUE SPECIFICITY: Expressed specifically in testis during spermatogenesis.; . . 0.21517 0.21247 0.016664174 55.21939137 724.85863 5.34384 MOSPD1 0.871382679379854 0.126905380853753 0.00171193976639306 motile sperm domain containing 1 . . . . . 0.17029 0.10531 -0.009020804 52.8544468 272.98628 3.54208 MOSPD2 0.992713930090269 0.00728472351624045 1.34639349027255e-06 motile sperm domain containing 2 . . . . . 0.25737 . -0.161524709 41.6430762 103.49449 2.19774 MOSPD3 0.00160694416950915 0.885826192848679 0.112566862981812 motile sperm domain containing 3 . . . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;bone;iris;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);heart;hypothalamus;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;spleen;stomach; testis - interstitial;superior cervical ganglion;testis;globus pallidus;atrioventricular node; 0.02804 0.07169 0.082802743 60.09082331 36.42902 1.09110 MOV10 0.998090427630705 0.00190957228343549 8.58599684525584e-11 Mov10 RISC complex RNA helicase FUNCTION: Probable RNA helicase. Required for RNA-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA- mediated cleavage of complementary mRNAs by RISC. Also required for RNA-directed transcription and replication of the human hepatitis delta virus (HDV). Interacts with small capped HDV RNAs derived from genomic hairpin structures that mark the initiation sites of RNA-dependent HDV RNA transcription. {ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:17507929, ECO:0000269|PubMed:18552826, ECO:0000269|PubMed:22791714}.; . . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;muscle;lens;skeletal muscle;bile duct;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.25340 0.14147 -1.682848699 2.653927813 63.42167 1.63022 MOV10L1 5.748157114955e-10 0.999564704939224 0.000435294485960671 Mov10 RISC complex RNA helicase like 1 FUNCTION: Putative RNA helicase. Isoform 1 may play a role in male germ cell development.; . TISSUE SPECIFICITY: Isoform 1 is specifically expressed in testis.; unclassifiable (Anatomical System);uterus;lung;optic nerve;macula lutea;testis;colon;fovea centralis;choroid;lens;brain;retina; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; 0.08630 0.12601 -0.694532205 14.83840528 7325.51336 18.41075 MOXD1 8.99118348991882e-11 0.266204625717657 0.733795374192431 monooxygenase, DBH-like 1 . . TISSUE SPECIFICITY: Highly expressed in lung, kidney, brain and spinal cord. {ECO:0000269|PubMed:15337741, ECO:0000269|PubMed:9751809}.; ovary;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;cochlea;thyroid;bone;testis;spinal ganglion;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;pancreas;lung;adrenal gland;placenta;spleen;stomach; amygdala;superior cervical ganglion;atrioventricular node; 0.12508 0.23100 -0.799052816 12.45576787 155.89106 2.72832 MOXD2P . . . monooxygenase, DBH-like 2, pseudogene . . . . . . . . . . . MPC1 0.145968077163696 0.778420165138115 0.0756117576981895 mitochondrial pyruvate carrier 1 FUNCTION: Mediates the uptake of pyruvate into mitochondria. {ECO:0000269|PubMed:22628558}.; DISEASE: Mitochondrial pyruvate carrier deficiency (MPYCD) [MIM:614741]: An autosomal recessive metabolic disorder characterized by severely delayed psychomotor development, mild dysmorphic features, hepatomegaly, marked metabolic acidosis, hyperlactacidemia with normal lactate/pyruvate, and encephalopathy. Some patients have epilepsy and peripheral neuropathy. {ECO:0000269|PubMed:22628558}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.17498 0.09893 0.257356108 69.83368719 59.70872 1.56892 MPC1L . . . mitochondrial pyruvate carrier 1-like . . . . . . . . . . . MPC2 0.449429466744431 0.522427122179462 0.0281434110761073 mitochondrial pyruvate carrier 2 FUNCTION: Mediates the uptake of pyruvate into mitochondria. {ECO:0000269|PubMed:22628558}.; . . . . 0.22019 0.09609 0.501689326 79.7888653 143.21224 2.60927 MPDU1 0.144211427826061 0.837200260703171 0.0185883114707676 mannose-P-dolichol utilization defect 1 FUNCTION: Required for normal utilization of mannose-dolichol phosphate (Dol-P-Man) in the synthesis of N-linked and O-linked oligosaccharides and GPI anchors. {ECO:0000250}.; DISEASE: Congenital disorder of glycosylation 1F (CDG1F) [MIM:609180]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:11733556, ECO:0000269|PubMed:11733564}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; fetal liver;heart;liver;kidney; 0.11090 . 0.439181676 77.69521113 1904.15514 8.02774 MPDZ . . . multiple PDZ domain crumbs cell polarity complex component FUNCTION: Interacts with HTR2C and provokes its clustering at the cell surface (By similarity). Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses. {ECO:0000250, ECO:0000269|PubMed:11150294, ECO:0000269|PubMed:15312654}.; DISEASE: Hydrocephalus, non-syndromic, autosomal recessive 2 (HYC2) [MIM:615219]: A disease characterized by a disturbance of cerebrospinal fluid circulation causing accumulation of ventricular cerebrospinal fluid, which results in progressive ventricular dilatation with onset in utero. Affected individuals may have neurologic impairment. {ECO:0000269|PubMed:23240096}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in heart, brain, placenta, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:9537516}.; ovary;sympathetic chain;colon;vein;skin;retina;uterus;prostate;atrium;whole body;frontal lobe;cochlea;endometrium;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;spinal cord;urinary;skeletal muscle;breast;pancreas;adrenal gland;placenta;visual apparatus;liver;spleen;kidney;thymus; amygdala;thalamus;occipital lobe;superior cervical ganglion;hypothalamus;spinal cord;atrioventricular node;pons;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.38934 0.15403 1.388989266 94.64496343 1523.83536 7.25359 MPE . . . malignant proliferation, eosinophil . . . . . . . . . . . MPEG1 3.45678304248647e-12 0.0118671883520566 0.988132811644487 macrophage expressed 1 . . TISSUE SPECIFICITY: Expressed in macrophages and peripheral blood monocytes. {ECO:0000269|PubMed:7888681}.; unclassifiable (Anatomical System);lymph node;nasopharynx;blood;germinal center;skeletal muscle;bone marrow; superior cervical ganglion; . . 0.161677043 64.96225525 1833.11332 7.89034 MPFD . . . myopathy with fiber type disproportion . . . . . . . . . . . MPG 4.23694995903237e-09 0.105315291343071 0.894684704419979 N-methylpurine DNA glycosylase FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.; . . lymphoreticular;ovary;salivary gland;developmental;colon;parathyroid;choroid;vein;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; prostate;liver;skeletal muscle; 0.11550 0.41751 -0.844966979 11.1759849 51.80076 1.42136 MPHOSPH6 0.00120843421582984 0.631491022844828 0.367300542939342 M-phase phosphoprotein 6 FUNCTION: RNA-binding protein that associates with the RNA exosome complex. Involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA and may play a role in recruiting the RNA exosome complex to pre-rRNA; this function may include C1D. {ECO:0000269|PubMed:17412707}.; . . ovary;umbilical cord;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;spinal cord;pharynx;blood;lens;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland; superior cervical ganglion;globus pallidus;ciliary ganglion; 0.14077 0.10615 0.459411326 78.28497287 289.36397 3.63851 MPHOSPH8 0.930242309438753 0.0697570823662564 6.08194990565266e-07 M-phase phosphoprotein 8 FUNCTION: Heterochromatin component that specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes recruitment of proteins that mediate epigenetic repression (PubMed:20871592, PubMed:26022416). Mediates recruitment of the HUSH complex to H3K9me3 sites: the HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3 (PubMed:26022416). Binds H3K9me and promotes DNA methylation by recruiting DNMT3A to target CpG sites; these can be situated within the coding region of the gene (PubMed:20871592). Mediates down-regulation of CDH1 expression (PubMed:20871592). {ECO:0000269|PubMed:20871592, ECO:0000269|PubMed:26022416}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;cerebral cortex;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;occipital lobe;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe; 0.10351 0.09166 -0.242430445 36.22906346 300.14804 3.69378 MPHOSPH9 0.000759987146945632 0.999233869397979 6.14345507497e-06 M-phase phosphoprotein 9 . . . lymphoreticular;ovary;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;stomach;cerebellum; testis - interstitial;superior cervical ganglion;prefrontal cortex;globus pallidus;skeletal muscle;pituitary;thymus; 0.16591 0.08911 -0.214928658 37.7388535 739.49466 5.39891 MPHOSPH10 0.585921552769244 0.414060147725815 1.82995049405936e-05 M-phase phosphoprotein 10 FUNCTION: Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;uterus;prostate;whole body;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;trabecular meshwork;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; subthalamic nucleus;hypothalamus;spinal cord;prefrontal cortex;white blood cells;ciliary ganglion;pons;whole blood; 0.48801 0.09118 1.86668643 97.19863175 9091.34729 20.66015 MPI 0.000142827839143154 0.860935796392372 0.138921375768485 mannose phosphate isomerase FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.; . TISSUE SPECIFICITY: Expressed in all tissues, but more abundant in heart, brain and skeletal muscle.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;germinal center;bladder;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;pineal body;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;macula lutea;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; testis - interstitial;thalamus;superior cervical ganglion;medulla oblongata;cerebellum peduncles;prefrontal cortex;liver;testis;pons;cingulate cortex;parietal lobe; 0.14693 0.62156 -0.157884861 42.05590941 104.24485 2.20659 MPL 1.43928006099179e-06 0.990133479329018 0.00986508139092072 MPL proto-oncogene, thrombopoietin receptor FUNCTION: Receptor for thrombopoietin. May represent a regulatory molecule specific for TPO-R-dependent immune responses.; DISEASE: Congenital amegakaryocytic thrombocytopenia (CAMT) [MIM:604498]: Disease characterized by isolated thrombocytopenia and megakaryocytopenia with no physical anomalies. {ECO:0000269|PubMed:16470591}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Thrombocythemia 2 (THCYT2) [MIM:601977]: A myeloproliferative disorder characterized by excessive platelet production, resulting in increased numbers of circulating platelets. It can be associated with spontaneous hemorrhages and thrombotic episodes. {ECO:0000269|PubMed:14764528, ECO:0000269|PubMed:23441089, ECO:0000269|PubMed:25538044}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myelofibrosis with myeloid metaplasia (MMM) [MIM:254450]: A chronic myeloproliferative disorder characterized by replacement of the bone marrow by fibrous tissue, extramedullary hematopoiesis, anemia, leukoerythroblastosis and hepatosplenomegaly. {ECO:0000269|PubMed:16834459, ECO:0000269|PubMed:16868251}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at a low level in a large number of cells of hematopoietic origin. Isoform 1 and isoform 2 are always found to be coexpressed.; . . 0.71041 0.28241 -0.530852121 20.82448691 264.93653 3.49416 MPLKIP 0.00205835193328243 0.505816061609331 0.492125586457387 M-phase specific PLK1 interacting protein FUNCTION: May play a role in maintenance of cell cycle integrity by regulating mitosis or cytokinesis. {ECO:0000269|PubMed:17310276}.; DISEASE: Trichothiodystrophy 4, non-photosensitive (TTD4) [MIM:234050]: A form of trichothiodystrophy, an autosomal recessive disease characterized by sulfur-deficient brittle hair and multisystem variable abnormalities. The spectrum of clinical features varies from mild disease with only hair involvement to severe disease with cutaneous, neurologic and profound developmental defects. Ichthyosis, intellectual and developmental disabilities, decreased fertility, abnormal characteristics at birth, ocular abnormalities, short stature, and infections are common manifestations. There are both photosensitive and non- photosensitive forms of the disorder. TTD4 patients do not manifest cutaneous photosensitivity. {ECO:0000269|PubMed:15645389}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at highest levels in liver and kidney; intermediate expression in skeletal muscle, pancreas, heart and placenta; low expression in brain and lung. Expressed in epidermis and hair follicles. {ECO:0000269|PubMed:11829489, ECO:0000269|PubMed:15645389}.; . . 0.18069 0.14228 . . 15.6055 0.55619 MPND 0.0157249668320667 0.958765221268823 0.0255098118991106 MPN domain containing FUNCTION: Probable protease. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymphoreticular;ovary;tongue;urinary;colon;parathyroid;choroid;skin;uterus;prostate;pancreas;lung;larynx;bone;placenta;visual apparatus;liver;testis;head and neck;spleen;kidney;brain; . 0.08480 0.09646 0.174625237 65.9648502 331.04684 3.87042 MPO 1.74837167117931e-09 0.383748731732064 0.616251266519564 myeloperoxidase FUNCTION: Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity.; DISEASE: Myeloperoxidase deficiency (MPOD) [MIM:254600]: A disorder characterized by decreased myeloperoxidase activity in neutrophils and monocytes that results in disseminated candidiasis. {ECO:0000269|PubMed:7904599, ECO:0000269|PubMed:8142659, ECO:0000269|PubMed:9354683, ECO:0000269|PubMed:9637725}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;umbilical cord;blood;fovea centralis;choroid;lens;retina;bone marrow;optic nerve;whole body;lung;frontal lobe;bone;placenta;thyroid;macula lutea;liver;testis;spleen;kidney;brain;thymus; superior cervical ganglion;trigeminal ganglion;bone marrow; 0.42352 0.90163 -0.148789446 42.29771172 954.37593 5.97949 MPP1 0.940116717603012 0.0598335256524197 4.97567445687262e-05 membrane protein, palmitoylated 1 FUNCTION: Essential regulator of neutrophil polarity. Regulates neutrophil polarization by regulating AKT1 phosphorylation through a mechanism that is independent of PIK3CG activity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17584769}.; . . 0.88624 0.10499 -0.181750739 40.15687662 18.73693 0.64673 MPP2 0.00258050734391977 0.99432586936594 0.00309362329014041 membrane protein, palmitoylated 2 . . . unclassifiable (Anatomical System);medulla oblongata;ovary;islets of Langerhans;sympathetic chain;muscle;parathyroid;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;breast;optic nerve;lung;frontal lobe;placenta;thyroid;macula lutea;pituitary gland;testis;cervix;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.58879 0.11658 -1.021348453 7.997169144 72.75543 1.78050 MPP3 1.99785500256477e-05 0.998839895019379 0.00114012643059518 membrane protein, palmitoylated 3 . . . unclassifiable (Anatomical System);prostate;pancreas;lung;ovary;pineal body;liver;testis;spleen;brain;skin;skeletal muscle;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;cerebellum; 0.85478 0.12185 -0.376526807 28.10804435 705.34657 5.27672 MPP4 5.87636433014139e-09 0.848765536507873 0.151234457615763 membrane protein, palmitoylated 4 FUNCTION: May play a role in retinal photoreceptors development. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the retina (at protein level). Highly expressed in the retina. Lower amounts are detected in brain, testis, ARPE-19, RPE/choroid and fetal eye. Isoform 5 is retina-specific. {ECO:0000269|PubMed:11414766, ECO:0000269|PubMed:12384283, ECO:0000269|PubMed:15558731, ECO:0000269|PubMed:15914641}.; unclassifiable (Anatomical System);optic nerve;macula lutea;fovea centralis;choroid;lens;retina; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.85297 0.09080 -0.464712395 23.5727766 2222.64295 8.68406 MPP5 0.660477587444664 0.339512911678648 9.50087668784989e-06 membrane protein, palmitoylated 5 FUNCTION: May play a role in tight junctions biogenesis and in the establishment of cell polarity in epithelial cells. May modulate SC6A1/GAT1-mediated GABA uptake by stabilizing the transporter. Required for localization of EZR to the apical membrane of parietal cells and may play a role in the dynamic remodeling of the apical cytoskeleton (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the retina (at protein level). {ECO:0000269|PubMed:15558731, ECO:0000269|PubMed:15914641}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;bone;thyroid;pituitary gland;testis;brain;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;adrenal gland;mesenchyma;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;thymus; superior cervical ganglion;pons;trigeminal ganglion; 0.97356 0.13722 0.466683681 78.73908941 326.43073 3.84236 MPP6 0.930676770761374 0.069320271122048 2.95811657816094e-06 membrane protein, palmitoylated 6 . . TISSUE SPECIFICITY: Abundant in testis, brain, and kidney with lower levels detectable in other tissues.; ovary;colon;parathyroid;skin;uterus;cochlea;endometrium;bone;testis;germinal center;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;bile duct;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;testis; 0.90973 0.11809 -0.093566408 46.7386176 40.20421 1.18196 MPP7 8.57971709426373e-07 0.979788465024234 0.0202106770040562 membrane protein, palmitoylated 7 FUNCTION: Acts as an important adapter that promotes epithelial cell polarity and tight junction formation via its interaction with DLG1. Involved in the assembly of protein complexes at sites of cell-cell contact. {ECO:0000269|PubMed:17332497}.; . . unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;colon;blood;uterus;lung;placenta;liver;testis;bladder;cerebellum; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.82513 0.10875 -0.821100135 11.88369899 183.38307 2.93894 MPPE1 8.3419136485111e-06 0.755610046590957 0.244381611495394 metallophosphoesterase 1 FUNCTION: Metallophosphoesterase required for transport of GPI- anchor proteins from the endoplasmic reticulum to the Golgi. Acts in lipid remodeling steps of GPI-anchor maturation by mediating the removal of a side-chain ethanolamine-phosphate (EtNP) from the second Man (Man2) of the GPI intermediate, an essential step for efficient transport of GPI-anchor proteins. {ECO:0000269|PubMed:19837036}.; . TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:11978971}.; ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;oesophagus;endometrium;larynx;bone;thyroid;pituitary gland;germinal center;ciliary body;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;blood;lens;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;spleen;kidney;stomach; whole brain;thalamus;occipital lobe;hypothalamus;thyroid;white blood cells;caudate nucleus;trigeminal ganglion;whole blood;skeletal muscle; 0.06785 0.08299 0.398725314 76.35645199 324.3481 3.82786 MPPE1P1 . . . metallophosphoesterase 1 pseudogene 1 . . . . . . . . . . . MPPED1 0.283449525180926 0.694468664245007 0.0220818105740674 metallophosphoesterase domain containing 1 FUNCTION: May have metallophosphoesterase activity (in vitro). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed predominantly in adult brain.; whole body; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; . 0.11686 -0.582225231 18.44184949 33.93248 1.04227 MPPED2 0.970565201803493 0.0293932119092438 4.15862872629768e-05 metallophosphoesterase domain containing 2 FUNCTION: Displays low metallophosphoesterase activity (in vitro). May play a role in the development of the nervous system (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed predominantly in fetal brain.; unclassifiable (Anatomical System);heart;hypothalamus;sympathetic chain;muscle;skeletal muscle;uterus;whole body;lung;endometrium;pituitary gland;head and neck;germinal center;kidney;brain; superior cervical ganglion;thyroid;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.06622 0.12378 -0.229483771 36.86010852 15.67728 0.55948 MPRIP 0.870658011638398 0.129341963429151 2.49324512265143e-08 myosin phosphatase Rho interacting protein FUNCTION: Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F- actin-binding region leads to disassembly of stress fibers in neuronal cells. {ECO:0000250|UniProtKB:P97434, ECO:0000269|PubMed:15545284, ECO:0000269|PubMed:16257966}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;gall bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; superior cervical ganglion;fetal liver;globus pallidus;ciliary ganglion;atrioventricular node;cerebellum; . 0.15964 -1.302541541 4.930408115 . . MPRIP-AS1 . . . MPRIP antisense RNA 1 . . . . . . . . . . . MPRIPP1 . . . myosin phosphatase Rho interacting protein pseudogene 1 . . . . . . . . . . . MPST 0.00677646845635564 0.756302320461948 0.236921211081696 mercaptopyruvate sulfurtransferase FUNCTION: Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H(2)S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions (By similarity). {ECO:0000250}.; DISEASE: Note=Aberrant MPST activity is found in a few cases of mercaptolactate-cysteine disulfiduria (MCDU) characterized by the appearance of large quantaties of the sulfur-containing amino acid, beta-mercaptolactate-cysteine disulfide, in the urine (PubMed:4973015, PubMed:4690911 and PubMed:6945862). Some cases have associated mental retardation (PubMed:4973015 and PubMed:6945862).; . medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;iris;germinal center;brain;gall bladder;heart;cartilage;urinary;adrenal cortex;lens;skeletal muscle;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; testis - seminiferous tubule;liver;kidney; 0.08268 . . . 74.0253 1.79726 MPTX1 . . . mucosal pentraxin 1 (pseudogene) . . TISSUE SPECIFICITY: Not expressed in the intestinal tract including ascending colon, descending colon and rectum. Not expressed in the human colon cancer cell lines HT-29 and CaCo-2. {ECO:0000269|PubMed:18850182}.; . . . . . . . . MPV17 1.10286841801097e-08 0.0510669037894889 0.948933085181827 MpV17 mitochondrial inner membrane protein FUNCTION: Involved in mitochondria homeostasis. May be involved in the metabolism of reactive oxygen species and control of oxidative phosphorylation and mitochondrial DNA (mtDNA) maintenance.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in pancreas, kidney, muscle, liver, lung, placenta, brain and heart. {ECO:0000269|PubMed:16582910}.; lymphoreticular;medulla oblongata;ovary;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;breast;pancreas;lung;placenta;visual apparatus;alveolus;hypopharynx;head and neck;kidney;mammary gland;aorta;stomach; . 0.10703 . -0.273576253 33.97027601 20.34527 0.69415 MPV17L 0.000500982038571006 0.445025462355648 0.55447355560578 MPV17 mitochondrial membrane protein-like FUNCTION: Isoform 1 participates in reactive oxygen species metablism by up- or down-regulation of the genes of antioxidant enzymes. {ECO:0000269|PubMed:16631601}.; . TISSUE SPECIFICITY: Isoform 1 is detected in the kidney (at protein level). Isoform 1 and isoform 2 are expressed in the kidney, heart, liver, lung, pancreas and skeletal muscle. {ECO:0000269|PubMed:16631601}.; uterus; ciliary ganglion;atrioventricular node;trigeminal ganglion; . . . . 1.18921 0.03456 MPV17L2 1.67296107198305e-07 0.127199435362106 0.872800397341786 MPV17 mitochondrial membrane protein-like 2 FUNCTION: Required for the assembly and stability of the mitochondrial ribosome (PubMed:24948607). Is a positive regulator of mitochondrial protein synthesis (PubMed:24948607). {ECO:0000269|PubMed:24948607}.; . . smooth muscle;ovary;colon;substantia nigra;parathyroid;fovea centralis;skin;retina;uterus;whole body;frontal lobe;thyroid;bone;pituitary gland;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;adrenal cortex;bile duct;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; . . . 0.03689118 56.64071715 1728.0677 7.67188 MPZ 0.691715780756532 0.30422459794857 0.00405962129489815 myelin protein zero FUNCTION: Creation of an extracellular membrane face which guides the wrapping process and ultimately compacts adjacent lamellae.; DISEASE: Charcot-Marie-Tooth disease 1B (CMT1B) [MIM:118200]: A dominant demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot- Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. {ECO:0000269|PubMed:10214757, ECO:0000269|PubMed:10545037, ECO:0000269|PubMed:10737979, ECO:0000269|PubMed:10965800, ECO:0000269|PubMed:11437164, ECO:0000269|PubMed:11438991, ECO:0000269|PubMed:11445635, ECO:0000269|PubMed:11835375, ECO:0000269|PubMed:12207932, ECO:0000269|PubMed:12221176, ECO:0000269|PubMed:12402337, ECO:0000269|PubMed:12497641, ECO:0000269|PubMed:12707985, ECO:0000269|PubMed:12845552, ECO:0000269|PubMed:14711881, ECO:0000269|PubMed:15036333, ECO:0000269|PubMed:16488608, ECO:0000269|PubMed:7504284, ECO:0000269|PubMed:7505151, ECO:0000269|PubMed:7527371, ECO:0000269|PubMed:7530774, ECO:0000269|PubMed:7550231, ECO:0000269|PubMed:7688964, ECO:0000269|PubMed:7693129, ECO:0000269|PubMed:7693130, ECO:0000269|PubMed:7694726, ECO:0000269|PubMed:8664899, ECO:0000269|PubMed:8797476, ECO:0000269|PubMed:8816708, ECO:0000269|PubMed:8835320, ECO:0000269|PubMed:8844219, ECO:0000269|PubMed:8990016, ECO:0000269|PubMed:9187667, ECO:0000269|PubMed:9217235, ECO:0000269|PubMed:9452091, ECO:0000269|PubMed:9452099, ECO:0000269|PubMed:9633821, ECO:0000269|Ref.40}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease 2I (CMT2I) [MIM:607677]: A dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. {ECO:0000269|PubMed:11835375, ECO:0000269|PubMed:14638973, ECO:0000269|PubMed:15241803, ECO:0000269|PubMed:9595994}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease 2J (CMT2J) [MIM:607736]: A dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. Charcot-Marie-Tooth disease type 2J is characterized by the association of axonal peripheral neuropathy with hearing loss and pupillary abnormalities such as Adie pupil. {ECO:0000269|PubMed:10071056, ECO:0000269|PubMed:11080237, ECO:0000269|PubMed:15326256, ECO:0000269|PubMed:16775239}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Adie pupil (ADIEP) [MIM:103100]: A stationary, benign disorder characterized by tonic, sluggishly reacting pupil and hypoactive or absent tendon reflexes. Adie pupil is a characteristic of Charcot-Marie-Tooth disease type 2J. {ECO:0000269|PubMed:16775239}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease, dominant, intermediate type, D (CMTDID) [MIM:607791]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. The dominant intermediate type D is characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. {ECO:0000269|PubMed:10406984}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Dejerine-Sottas syndrome (DSS) [MIM:145900]: A severe degenerating neuropathy of the demyelinating Charcot-Marie-Tooth disease category, with onset by age 2 years. Characterized by motor and sensory neuropathy with very slow nerve conduction velocities, increased cerebrospinal fluid protein concentrations, hypertrophic nerve changes, delayed age of walking as well as areflexia. There are both autosomal dominant and autosomal recessive forms of Dejerine-Sottas syndrome. {ECO:0000269|PubMed:11438991, ECO:0000269|PubMed:11596785, ECO:0000269|PubMed:11835375, ECO:0000269|PubMed:12497641, ECO:0000269|PubMed:7506095, ECO:0000269|PubMed:8630052, ECO:0000269|PubMed:8816708, ECO:0000269|PubMed:9187667, ECO:0000269|PubMed:9222756, ECO:0000269|PubMed:9452055, ECO:0000269|PubMed:9452091, ECO:0000269|PubMed:9633821}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Neuropathy, congenital hypomyelinating or amyelinating (CHN) [MIM:605253]: A severe degenerating neuropathy that results from a congenital impairment in myelin formation. It is clinically characterized by early onset of hypotonia, areflexia, distal muscle weakness, and very slow nerve conduction velocities (as low as 3m/s). Some patients manifest nearly complete absence of spontaneous limb movements, respiratory distress at birth, and complete absence of myelin shown by electron microscopy of peripheral nerves. Inheritance can be autosomal dominant or recessive. {ECO:0000269|PubMed:15184631}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Roussy-Levy syndrome (ROULS) [MIM:180800]: Autosomal dominant disorder that resembles Charcot-Marie-Tooth disease type 1 in that it presents with foot deformity, weakness and atrophy of distal limb muscles, especially the peronei, and absent tendon reflexes. The phenotype differs, however, in that it includes static tremor of the upper limbs and gait ataxia. {ECO:0000269|PubMed:10553995}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found only in peripheral nervous system Schwann cells.; unclassifiable (Anatomical System);lymph node;heart;sympathetic chain;choroid;skin;uterus;whole body;lung;cerebral cortex;cochlea;testis;spinal ganglion;brain; dorsal root ganglion;superior cervical ganglion;olfactory bulb;spinal cord;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.72873 0.09309 -0.207437529 38.2814343 15.36913 0.55165 MPZL1 0.327816834049089 0.65655306497754 0.0156301009733712 myelin protein zero like 1 FUNCTION: Cell surface receptor, which is involved in signal transduction processes. Recruits PTPN11/SHP-2 to the cell membrane and is a putative substrate of PTPN11/SHP-2. Is a major receptor for concanavalin-A (ConA) and is involved in cellular signaling induced by ConA, which probably includes Src family tyrosine- protein kinases. Isoform 3 seems to have a dominant negative role; it blocks tyrosine phosphorylation of MPZL1 induced by ConA. Isoform 1, but not isoform 2 and isoform 3, may be involved in regulation of integrin-mediated cell motility. {ECO:0000269|PubMed:11751924, ECO:0000269|PubMed:12410637}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in heart, placenta, kidney and pancreas. Isoform 3 is relatively abundant in hematopoietic tissues and fetal liver. Isoform 1 and isoform 3 are expressed in CD14- PB monocytes and pre-B cell progenitors. Isoform 3 appears to be the major isoform in CD34- promyelocytic and promonocytic cells. During differentiation in monocytic cells, the expression level of isoform 3 decreases and that of isoform 1 increases. Isoform 1 is prominent in stromal cells and, to a lesser extent, in umbilical vein endothelial cells and erythroid progenitors. Isoform 2 is expressed in a erythroid progenitor cell line. {ECO:0000269|PubMed:12410637, ECO:0000269|PubMed:12684038, ECO:0000269|PubMed:9792637}.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;trachea;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.08905 . -0.317668748 31.45789101 9.79957 0.35883 MPZL2 1.21919862877634e-11 0.0067327615061836 0.993267238481624 myelin protein zero like 2 FUNCTION: Mediates homophilic cell-cell adhesion.; . TISSUE SPECIFICITY: Expressed in thymocytes and thymic stromal cells; expression elevated in some T-cell leukemias.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;thyroid;testis;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;pancreas;pia mater;lung;nasopharynx;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;stomach; superior cervical ganglion;trachea;trigeminal ganglion; 0.27645 0.20477 -0.049474214 50.01179523 116.00455 2.34305 MPZL3 6.52170419480443e-09 0.0376828263337776 0.962317167144518 myelin protein zero like 3 FUNCTION: Mediates homophilic cell-cell adhesion. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);heart;lacrimal gland;urinary;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;cerebellum; 0.17771 0.09333 0.505321956 80.00707714 673.78365 5.18490 MR1 5.61258291225197e-09 0.123269594511886 0.876730399875531 major histocompatibility complex, class I-related FUNCTION: Antigen-presenting molecule specialized in presenting microbial vitamin B metabolites. Involved in the development and expansion of a small population of T-cells expressing an invariant T-cell receptor alpha chain called mucosal-associated invariant T- cells (MAIT). MAIT lymphocytes are preferentially located in the gut lamina propria and therefore may be involved in monitoring commensal flora or serve as a distress signal. Expression and MAIT cell recognition seem to be ligand-dependent. {ECO:0000269|PubMed:12794138, ECO:0000269|PubMed:19416870}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7624800}.; unclassifiable (Anatomical System);cartilage;urinary;colon;blood;bone marrow;breast;prostate;whole body;lung;nasopharynx;placenta;thyroid;kidney;brain; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08251 0.10385 0.485092724 79.37603208 76.43978 1.83403 MRAP 0.0106384158711261 0.832650160868931 0.156711423259943 melanocortin 2 receptor accessory protein FUNCTION: Modulator of melanocortin receptors (MC1R, MC2R, MC3R, MC4R and MC5R). Acts by increasing ligand-sensitivity of melanocortin receptors and enhancing generation of cAMP by the receptors. Required both for MC2R trafficking to the cell surface of adrenal cells and for signaling in response to corticotropin (ACTH). May be involved in the intracellular trafficking pathways in adipocyte cells. {ECO:0000269|PubMed:15654338, ECO:0000269|PubMed:19329486, ECO:0000269|PubMed:20371771}.; . TISSUE SPECIFICITY: Expressed in adrenal cortex, testis, breast, thyroid, lymph node, ovary and fat. Expressed in adipose tissues. {ECO:0000269|PubMed:15654338}.; smooth muscle;ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;optic nerve;thyroid;testis;dura mater;brain;pineal gland;unclassifiable (Anatomical System);meninges;adrenal cortex;blood;lens;lung;pia mater;adrenal gland;placenta;macula lutea;liver;spleen;stomach; . 0.16367 0.35707 0.373041938 75.29488087 118.27623 2.36597 MRAP2 0.00034873923097844 0.376989484300756 0.622661776468265 melanocortin 2 receptor accessory protein 2 FUNCTION: Modulator of melanocortin receptor 4 (MC4R), a receptor involved in energy homeostasis. Plays a central role in the control of energy homeostasis and body weight regulation by increasing ligand-sensitivity of MC4R and MC4R-mediated generation of cAMP (By similarity). May also act as a negative regulator of MC2R: competes with MRAP for binding to MC2R and impairs the binding of corticotropin (ACTH) to MC2R. May also regulate activity of other melanocortin receptors (MC1R, MC3R and MC5R); however, additional evidences are required in vivo. {ECO:0000250, ECO:0000269|PubMed:19329486, ECO:0000269|PubMed:20371771}.; DISEASE: Obesity (OBESITY) [MIM:601665]: A condition characterized by an increase of body weight beyond the limitation of skeletal and physical requirements, as the result of excessive accumulation of body fat. {ECO:0000269|PubMed:23869016}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the adrenal gland and brain. Not expressed in other tissues. {ECO:0000269|PubMed:19329486}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;pharynx;blood;lens;breast;lung;macula lutea;visual apparatus;alveolus;liver;head and neck;kidney;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;cerebellum; 0.18450 0.10957 -0.229483771 36.86010852 17.29025 0.60646 MRAS 0.859946833275581 0.137916447460866 0.00213671926355291 muscle RAS oncogene homolog FUNCTION: May serve as an important signal transducer for a novel upstream stimuli in controlling cell proliferation. Weakly activates the MAP kinase pathway. {ECO:0000269|PubMed:16630891}.; . TISSUE SPECIFICITY: Expression highly restricted to the brain and heart.; unclassifiable (Anatomical System);amygdala;cartilage;pineal body;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;breast;optic nerve;whole body;lung;placenta;bone;macula lutea;liver;kidney;brain; occipital lobe;subthalamic nucleus;superior cervical ganglion;pons;cingulate cortex;cerebellum; 0.26655 0.17821 -0.141298762 42.87567823 32.79778 1.01806 MRC1 0.975871402342468 0.0241031500466073 2.5447610925172e-05 mannose receptor, C type 1 FUNCTION: Mediates the endocytosis of glycoproteins by macrophages. Binds both sulfated and non-sulfated polysaccharide chains.; . . unclassifiable (Anatomical System);cartilage;ovary;colon;parathyroid;blood;uterus;prostate;whole body;lung;cochlea;endometrium;placenta;visual apparatus;liver;testis;spleen;kidney;brain;mammary gland;stomach; . 0.19821 0.20954 . . 3681.90554 11.81409 MRC2 0.985888157648222 0.014111842347907 3.87074685551274e-12 mannose receptor, C type 2 FUNCTION: May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). {ECO:0000269|PubMed:10683150, ECO:0000269|PubMed:12972549}.; . TISSUE SPECIFICITY: Ubiquitous with low expression in brain, placenta, lung, kidney, pancreas, spleen, thymus and colon. Expressed in endothelial cells, fibroblasts and macrophages. Highly expressed in fetal lung and kidney. {ECO:0000269|PubMed:10683150, ECO:0000269|PubMed:8702911}.; lymphoreticular;smooth muscle;ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;oesophagus;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;urinary;lens;skeletal muscle;pancreas;lung;adrenal gland;mesenchyma;epididymis;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;heart;trigeminal ganglion; 0.68336 0.13319 -1.163005113 6.086341118 972.4639 6.02816 MRE11A 0.00115883260457516 0.998759384401325 8.17829941004754e-05 MRE11 homolog A, double strand break repair nuclease FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand- specific 3'-5' exonuclease activity, which are provided by MRE11A. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11A to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation.; DISEASE: Ataxia-telangiectasia-like disorder 1 (ATLD1) [MIM:604391]: A rare disorder characterized by progressive cerebellar ataxia, dysarthria, abnormal eye movements, and absence of telangiectasia. ATLD patients show normal levels of total IgG, IgA and IgM, although there may be reduced levels of specific functional antibodies. At the cellular level, ATLD exhibits hypersensitivity to ionizing radiation and radioresistant DNA synthesis. {ECO:0000269|PubMed:10612394}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in MRE11A can be a cause of nephronophthisis-related ciliopathies (NPHP-RC), a group of recessive diseases that affect kidney, retina and brain. A homozygous truncating mutation MRE11A has been found in patients with cerebellar vermis hypoplasia, ataxia and dysarthria. {ECO:0000269|PubMed:22863007}.; . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;skeletal muscle;lung;mesenchyma;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; uterus corpus;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.99941 0.50288 0.044168103 57.40740741 206.95821 3.10867 MRE11B . . . MRE11 homolog B, double strand break repair nuclease (pseudogene) . . . . . . . . . . . MREG 5.96360913088242e-06 0.262726735048635 0.737267301342234 melanoregulin FUNCTION: Plays a role in the incorporation of pigments into hair. May function in membrane fusion and regulate the biogenesis of disk membranes of photoreceptor rod cells (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in photoreceptor cells (at protein level). {ECO:0000269|PubMed:17260955}.; medulla oblongata;colon;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pineal body;blood;skeletal muscle;bile duct;lung;placenta;macula lutea;visual apparatus;liver;alveolus;head and neck;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;cerebellum; 0.13470 0.96763 0.170987912 65.5579146 31.6616 0.99622 MREGP1 . . . melanoregulin pseudogene 1 . . . . . . . . . . . MRFAP1 0.177064470221167 0.644285911920836 0.178649617857997 Morf4 family associated protein 1 . . . smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;larynx;thyroid;iris;pituitary gland;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;heart;lacrimal gland;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;bile duct;breast;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; amygdala;medulla oblongata;subthalamic nucleus;occipital lobe;thalamus;hypothalamus;temporal lobe;globus pallidus;caudate nucleus;pons;parietal lobe;cingulate cortex; 0.17082 0.11262 -0.207437529 38.2814343 3.7415 0.13922 MRFAP1L1 0.008908008002048 0.578868962689642 0.41222302930831 Morf4 family associated protein 1 like 1 . . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;gum;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;spinal cord;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;atrium;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; amygdala;subthalamic nucleus;occipital lobe;hypothalamus;prefrontal cortex;globus pallidus;pons;parietal lobe;cingulate cortex; 0.16044 0.11262 0.125076652 62.7388535 42.65034 1.23741 MRGBP 0.905748427840226 0.0934824205144273 0.000769151645346868 MRG/MORF4L binding protein FUNCTION: Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage.; . . . . 0.16118 0.11581 -0.185391282 39.67916962 9.54557 0.35160 MRGPRD 0.000404522656857286 0.404007495211053 0.595587982132089 MAS related GPR family member D FUNCTION: May regulate nociceptor function and/or development, including the sensation or modulation of pain. Functions as a specific membrane receptor for beta-alanine. Beta-alanine at micromolar doses specifically evoked Ca(2+) influx in cells expressing the receptor. Beta-alanine decreases forskolin- stimulated cAMP production in cells expressing the receptor, suggesting that the receptor couples with G-protein G(q) and G(i).; . . . . 0.07967 0.09679 0.663285274 84.55414013 76.11481 1.82793 MRGPRE 4.75586456400976e-05 0.243185161822913 0.756767279531447 MAS related GPR family member E FUNCTION: Orphan receptor. May regulate nociceptor function and/or development, including the sensation or modulation of pain.; . . . . 0.09574 0.11120 0.174625237 65.9648502 1096.03191 6.33504 MRGPRF 0.370675550581141 0.581207198680727 0.048117250738132 MAS related GPR family member F FUNCTION: Orphan receptor. May bind to a neuropeptide and may regulate nociceptor function and/or development, including the sensation or modulation of pain (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;heart;ovary;salivary gland;colon;choroid;skin;retina;uterus;pancreas;prostate;lung;endometrium;bone;placenta;liver;testis;spleen;kidney;brain;mammary gland;stomach;peripheral nerve; uterus;dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.15647 . -0.203796826 38.81811748 2327.15872 8.93732 MRGPRF-AS1 . . . MRGPRF antisense RNA 1 . . . . . . . . . . . MRGPRG . . . MAS related GPR family member G FUNCTION: Orphan receptor. May regulate nociceptor function and/or development, including the sensation or modulation of pain (By similarity). {ECO:0000250}.; . . . . 0.05294 . 1.056521908 91.38358103 278.12112 3.57382 MRGPRG-AS1 . . . MRGPRG antisense RNA 1 . . . . . . . . . . . MRGPRX1 0.0831473169654194 0.757902180777439 0.158950502257142 MAS related GPR family member X1 FUNCTION: Orphan receptor. Probably involved in the function of nociceptive neurons. May regulate nociceptor function and/or development, including the sensation or modulation of pain. Potently activated by enkephalins including BAM22 (bovine adrenal medulla peptide 22) and BAM (8-22). BAM22 is the most potent compound and evoked a large and dose-dependent release of intracellular calcium in stably transfected cells. G(alpha)q proteins are involved in the calcium-signaling pathway. Activated by the antimalarial drug, chloroquine. May mediate chloroquine- induced itch, in a histamine-independent manner. {ECO:0000269|PubMed:11850634, ECO:0000269|PubMed:20004959}.; . TISSUE SPECIFICITY: Uniquely localized in a subset of small dorsal root and trigeminal sensory neurons. {ECO:0000269|PubMed:11850634}.; unclassifiable (Anatomical System);trophoblast; superior cervical ganglion;ciliary ganglion;pons;skeletal muscle; . 0.06245 0.687150476 85.17928757 200.35311 3.05853 MRGPRX2 0.00249061218606174 0.546202975430796 0.451306412383142 MAS related GPR family member X2 FUNCTION: Mast cell-specific receptor for basic secretagogues, i.e. cationic amphiphilic drugs, as well as endo- or exogenous peptides, consisting of a basic head group and a hydrophobic core (PubMed:25517090). Recognizes and binds small molecules containing a cyclized tetrahydroisoquinoline (THIQ), such as non-steroidal neuromuscular blocking drugs (NMBDs), including tubocurarine and atracurium. In response to these compounds, mediates pseudo- allergic reactions characterized by histamine release, inflammation and airway contraction (By similarity). Acts as a receptor for a number of other ligands, including peptides and alkaloids, such as cortistatin-14, proadrenomedullin N-terminal peptides PAMP-12 and, at lower extent, PAMP-20, antibacterial protein LL-37, PMX-53 peptide, beta-defensins, and complanadine A. {ECO:0000250|UniProtKB:Q3KNA1, ECO:0000269|PubMed:15823563, ECO:0000269|PubMed:21441599, ECO:0000269|PubMed:22069323, ECO:0000269|PubMed:23698749, ECO:0000269|PubMed:24930830, ECO:0000269|PubMed:25517090, ECO:0000305|PubMed:12915402}.; . TISSUE SPECIFICITY: Mainly expressed in mast cells. Has a limited expression profile, both peripheral and within the central nervous system, with highest levels in dorsal root ganglion (PubMed:12915402). Detected in blood vessels, scattered lymphocytes, and gastrointestinal ganglia (at protein level) (PubMed:16161007). {ECO:0000269|PubMed:12915402, ECO:0000269|PubMed:16161007}.; medulla oblongata; . 0.07292 0.08330 1.750970652 96.67374381 2664.98207 9.70970 MRGPRX3 2.86211366895334e-08 0.0244040561886465 0.975595915190217 MAS related GPR family member X3 FUNCTION: Orphan receptor. Probably involved in the function of nociceptive neurons. May regulate nociceptor function and/or development, including the sensation or modulation of pain. Potently activated by enkephalins (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Uniquely localized in a subset of small dorsal root and trigeminal sensory neurons. {ECO:0000269|PubMed:11850634}.; . . 0.07307 . 1.464302001 95.23472517 314.5827 3.77193 MRGPRX4 0.00181856462826359 0.480193921145132 0.517987514226604 MAS related GPR family member X4 FUNCTION: Orphan receptor. Probably involved in the function of nociceptive neurons. May regulate nociceptor function and/or development, including the sensation or modulation of pain. Potently activated by enkephalins (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Uniquely localized in a subset of small dorsal root and trigeminal sensory neurons. {ECO:0000269|PubMed:11850634}.; unclassifiable (Anatomical System);skeletal muscle; dorsal root ganglion;superior cervical ganglion;pons; 0.01155 0.05295 1.864866726 97.1809389 1005.84423 6.10717 MRI1 0.000533201017712655 0.69529083552785 0.304175963454438 methylthioribose-1-phosphate isomerase 1 FUNCTION: Catalyzes the interconversion of methylthioribose-1- phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1- P). Independently from catalytic activity, promotes cell invasion in response to constitutive RhoA activation by promoting FAK tyrosine phosphorylation and stress fiber turnover. {ECO:0000255|HAMAP-Rule:MF_03119, ECO:0000269|PubMed:19620624}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach; . . . 0.50895761 80.20169851 295.74482 3.67200 MRLN . . . myoregulin FUNCTION: Inhibits the activity of ATP2A1/SERCA1 ATPase in sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+), thereby acting as a key regulator of skeletal muscle activity. Its high expression in adult skeletal muscle, suggests that it constitutes the predominant regulator of ATP2A1/SERCA1 in adult skeletal muscle. {ECO:0000250|UniProtKB:Q9CV60, ECO:0000269|PubMed:25640239}.; . . . . 0.01681 0.07632 0.369407109 74.95281906 . . MRM1 5.92768053664856e-05 0.463340314179979 0.536600409014655 mitochondrial rRNA methyltransferase 1 FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O- methylguanosine at position 1145 (Gm1145) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA. {ECO:0000269|PubMed:25074936}.; . . unclassifiable (Anatomical System);lymphoreticular;islets of Langerhans;urinary;colon;bone marrow;prostate;lung;bone;placenta;duodenum;liver;testis;cervix;germinal center;brain;stomach; superior cervical ganglion;cingulate cortex; 0.06432 0.09973 0.218717575 68.27081859 657.53647 5.14188 MRO 0.000178042221372106 0.698824831115749 0.300997126662879 maestro . . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11401430}.; unclassifiable (Anatomical System);medulla oblongata;lymph node;lung;iris;testis;kidney;skeletal muscle; dorsal root ganglion;superior cervical ganglion;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05661 0.10002 0.284856336 71.40835103 6637.73489 17.24298 MROH1 0.587142254682183 0.41241642788069 0.000441317437127016 maestro heat like repeat family member 1 . . . . . . . . . 77.45123 1.85066 MROH2A 0.314233041801318 0.488421857526398 0.197345100672285 maestro heat like repeat family member 2A . . . . . . . . . 5521.07721 15.33928 MROH2B 1.28868466121395e-26 0.0250058459524975 0.974994154047502 maestro heat like repeat family member 2B . . . . . . 0.08456 1.598375034 95.87756546 6887.10584 17.68880 MROH3P . . . maestro heat like repeat family member 3, pseudogene . . . . . . . . . . . MROH4P . . . maestro heat like repeat family member 4, pseudogene . . . . . . . . . . . MROH5 . . . maestro heat like repeat family member 5 . . . . . . . 4.384391577 99.74050484 . . MROH6 1.27469283128293e-10 0.0959450723837583 0.904054927488772 maestro heat like repeat family member 6 . . . . . 0.09651 . . . 5423.17081 15.18270 MROH7 6.65107650339551e-19 0.0879533250326989 0.912046674967301 maestro heat like repeat family member 7 . . . . . . . 1.756436346 96.71502713 7259.49576 18.34958 MROH7-TTC4 . . . MROH7-TTC4 readthrough (NMD candidate) . . . . . . . . . 6.75121 0.24928 MROH8 . . . maestro heat like repeat family member 8 . . . . . 0.07427 . . . . . MROH9 2.468587335044e-06 0.909667308222488 0.0903302231901767 maestro heat like repeat family member 9 . . . . . 0.05304 . 2.513579985 98.67303609 678.48375 5.20546 MROS . . . Melkersson-Rosenthal syndrome . . . . . . . . . . . MRPL1 3.2125698010729e-05 0.79982706132052 0.20014081298147 mitochondrial ribosomal protein L1 . . . unclassifiable (Anatomical System);trophoblast;umbilical cord;ovary;heart;islets of Langerhans;colon;parathyroid;blood;lens;skin;skeletal muscle;uterus;whole body;lung;placenta;liver;testis;spleen;germinal center;kidney;brain;aorta;stomach;gall bladder; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.43480 . 0.284856336 71.40835103 424.39081 4.30388 MRPL2 0.00159372149990342 0.969676672120424 0.0287296063796722 mitochondrial ribosomal protein L2 . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;pharynx;blood;lens;bile duct;breast;lung;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland; superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion; 0.07342 0.06610 -0.560178693 19.30879925 61.36506 1.59610 MRPL2P1 . . . mitochondrial ribosomal protein L2 pseudogene 1 . . . . . . . . . . . MRPL3 2.80524857561429e-08 0.291587912235958 0.708412059711556 mitochondrial ribosomal protein L3 . DISEASE: Combined oxidative phosphorylation deficiency 9 (COXPD9) [MIM:614582]: A mitochondrial disease characterized by failure to thrive, poor feeding, hypertrophic cardiomyopathy, hepatomegaly, and psychomotor retardation. Death in infancy has been observed in some cases. {ECO:0000269|PubMed:21786366}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;urinary;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.15972 0.13142 -0.091746757 46.91554612 132.30265 2.50327 MRPL3P1 . . . mitochondrial ribosomal protein L3 pseudogene 1 . . . . . . . . . . . MRPL4 1.13185886619774e-07 0.33543628370437 0.664563603109744 mitochondrial ribosomal protein L4 . . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pineal body;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; whole brain;medulla oblongata;cerebellum peduncles;temporal lobe;tumor;parietal lobe;cerebellum; 0.05217 0.10832 0.198490371 67.30360934 1535.10751 7.28081 MRPL9 0.0513078499662132 0.927410340887057 0.02128180914673 mitochondrial ribosomal protein L9 . . . . . 0.36354 0.09101 1.016049644 90.86459071 1292.47416 6.76744 MRPL9P1 . . . mitochondrial ribosomal protein L9 pseudogene 1 . . . . . . . . . . . MRPL10 0.288891351405341 0.689959841522737 0.0211488070719228 mitochondrial ribosomal protein L10 . . . lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;iris;germinal center;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;kidney;stomach;aorta;thymus;cerebellum; whole brain;liver;tumor;globus pallidus;kidney; 0.09517 0.08326 -0.095386216 46.48502005 1367.62968 6.93629 MRPL11 2.04235979758032e-05 0.279100512299417 0.720879064102607 mitochondrial ribosomal protein L11 . . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;skin;bone marrow;retina;uterus;prostate;whole body;optic nerve;endometrium;larynx;bone;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;pancreas;lung;cornea;placenta;visual apparatus;macula lutea;liver;cervix;head and neck;spleen;kidney;mammary gland;stomach; superior cervical ganglion;lung;heart;liver;tumor;testis; 0.47525 0.13169 -0.05129383 49.75819769 14.57849 0.52576 MRPL11P2 . . . mitochondrial ribosomal protein L11 pseudogene 2 . . . . . . . . . . . MRPL11P3 . . . mitochondrial ribosomal protein L11 pseudogene 3 . . . . . . . . . . . MRPL12 0.0501971389457513 0.859596440495307 0.0902064205589412 mitochondrial ribosomal protein L12 . . . lymphoreticular;myocardium;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;germinal center;brain;tonsil;heart;pineal body;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;oesophagus;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);trophoblast;lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;hypopharynx;duodenum;head and neck;kidney;stomach;thymus; superior cervical ganglion;heart;temporal lobe;liver;testis;kidney;pons;trigeminal ganglion;skeletal muscle; 0.79543 0.13234 0.038710339 56.92380278 563.54854 4.81967 MRPL13 7.01924287122997e-07 0.274557628244179 0.725441669831534 mitochondrial ribosomal protein L13 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pineal body;spinal cord;muscle;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;stomach; . 0.09884 0.22151 0.060756528 58.52795471 30.69703 0.97643 MRPL14 0.0369989874032739 0.833373913779711 0.129627098817015 mitochondrial ribosomal protein L14 FUNCTION: Forms part of 2 intersubunit bridges in the assembled ribosome. Upon binding to MALSU1 intersubunit bridge formation is blocked, preventing ribosome formation and repressing translation (Probable). {ECO:0000305|PubMed:22829778}.; . . . . 0.08082 0.09192 -0.141298762 42.87567823 12.35488 0.44801 MRPL14P1 . . . mitochondrial ribosomal protein L14 pseudogene 1 . . . . . . . . . . . MRPL15 1.33578833013651e-05 0.390780750373163 0.609205891743536 mitochondrial ribosomal protein L15 . . . ovary;skin;retina;prostate;optic nerve;endometrium;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;pineal body;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;placenta;duodenum;kidney;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.37483 0.12040 0.284856336 71.40835103 140.6933 2.58827 MRPL15P1 . . . mitochondrial ribosomal protein L15 pseudogene 1 . . . . . . . . . . . MRPL16 0.00310865625311475 0.818806896002005 0.178084447744881 mitochondrial ribosomal protein L16 FUNCTION: Component of the large subunit of mitochondrial ribosome.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;subthalamic nucleus;globus pallidus;testis;ciliary ganglion;kidney;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.07378 0.11430 0.595326758 82.66100495 269.11267 3.51855 MRPL17 0.464121315693857 0.51047821121567 0.0254004730904729 mitochondrial ribosomal protein L17 . . TISSUE SPECIFICITY: Detected in adrenal gland, mammary gland and adipose tissue. {ECO:0000269|PubMed:10931946}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;oesophagus;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach;cerebellum; testis; 0.10020 0.13015 0.080983847 59.76055674 25.66004 0.83609 MRPL18 0.000794102804498299 0.775329022776281 0.223876874419221 mitochondrial ribosomal protein L18 FUNCTION: Together with thiosulfate sulfurtransferase (TST), acts as a mitochondrial import factor for the cytosolic 5S rRNA. The precursor form shows RNA chaperone activity; is able to fold the 5S rRNA into an import-competent conformation that is recognized by rhodanese (TST). Both the cytoplasmic and mitochondrial forms are able to bind to the helix IV-loop D in the gamma domain of the 5S rRNA. {ECO:0000269|PubMed:21685364}.; . . . . 0.03112 0.11253 0.325313577 73.11276244 19.53969 0.67050 MRPL19 0.00131859090035099 0.859675070686426 0.139006338413223 mitochondrial ribosomal protein L19 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;cornea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.09457 0.08563 -0.293801652 32.93819297 123.22581 2.41758 MRPL20 0.000171803357075406 0.691280353635067 0.308547843007857 mitochondrial ribosomal protein L20 . . . lymphoreticular;ovary;skin;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;cartilage;pineal body;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.09346 0.14981 0.125076652 62.7388535 226.10236 3.24901 MRPL20P1 . . . mitochondrial ribosomal protein L20 pseudogene 1 . . . . . . . . . . . MRPL21 5.45959674014109e-08 0.126704419849534 0.873295525554498 mitochondrial ribosomal protein L21 . . . myocardium;ovary;colon;substantia nigra;parathyroid;skin;bone marrow;uterus;prostate;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);hypothalamus;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; . 0.04970 . 0.949904335 90.00943619 127.12035 2.45962 MRPL22 3.44167883429456e-07 0.335322044408833 0.664677611423283 mitochondrial ribosomal protein L22 . . . ovary;salivary gland;intestine;colon;parathyroid;vein;skin;uterus;prostate;whole body;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;cornea;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; testis - interstitial;testis;ciliary ganglion; 0.09439 0.08687 -0.137658575 43.57159707 294.18961 3.66322 MRPL22P1 . . . mitochondrial ribosomal protein L22 pseudogene 1 . . . . . . . . . . . MRPL23 1.45650190962038e-06 0.122913099857619 0.877085443640471 mitochondrial ribosomal protein L23 . . . . . 0.11672 . 1.106059595 91.985138 1735.57978 7.68489 MRPL23-AS1 . . . MRPL23 antisense RNA 1 . . . . . . . . . . . MRPL24 0.00149122661138067 0.876410627092064 0.122098146296555 mitochondrial ribosomal protein L24 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;kidney;mammary gland;stomach;cerebellum;thymus; heart;testis;kidney;skeletal muscle; 0.20113 0.08675 0.503505267 79.88912479 51.84691 1.42229 MRPL27 0.385344633134836 0.571057732562536 0.0435976343026282 mitochondrial ribosomal protein L27 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;whole body;bone;testis;amniotic fluid;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;oral cavity;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; subthalamic nucleus;temporal lobe; 0.21657 0.11067 -0.093566408 46.7386176 159.06986 2.75588 MRPL28 2.41661968324225e-08 0.0800621657026926 0.919937810131111 mitochondrial ribosomal protein L28 . . TISSUE SPECIFICITY: Found in a variety of normal tissues including spleen, testes, thymus, liver, kidney, brain, adrenal, lung and retinal tissue.; ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;heart;cartilage;islets of Langerhans;muscle;blood;skeletal muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;duodenum;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;atrioventricular node;trigeminal ganglion; 0.10879 0.10667 1.019682101 90.97664544 1443.82845 7.08693 MRPL30 0.543252452898348 0.442446467781108 0.0143010793205438 mitochondrial ribosomal protein L30 . . . myocardium;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pharynx;blood;breast;bile duct;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; globus pallidus;trigeminal ganglion;skeletal muscle; 0.03845 . 0.503505267 79.88912479 32.53769 1.01301 MRPL30P1 . . . mitochondrial ribosomal protein L30 pseudogene 1 . . . . . . . . . . . MRPL30P2 . . . mitochondrial ribosomal protein L30 pseudogene 2 . . . . . . . . . . . MRPL32 0.00129078014499608 0.856620000884288 0.142089218970716 mitochondrial ribosomal protein L32 . . . medulla oblongata;ovary;umbilical cord;foreskin;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;bladder;brain;heart;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta; ciliary ganglion;atrioventricular node; 0.10597 0.09522 0.283038099 71.26680821 52.50569 1.43401 MRPL32P1 . . . mitochondrial ribosomal protein L32 pseudogene 1 . . . . . . . . . . . MRPL33 0.749164756585824 0.240720283605278 0.0101149598088976 mitochondrial ribosomal protein L33 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;iris;testis;dura mater;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);meninges;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pia mater;lung;cornea;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;stomach;aorta; occipital lobe;adrenal gland;adrenal cortex;globus pallidus;testis;kidney; 0.07220 0.06654 -0.009020804 52.8544468 . . MRPL34 0.0401284434162437 0.649372174404957 0.310499382178799 mitochondrial ribosomal protein L34 . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;kidney;mammary gland;stomach;aorta; testis - interstitial;liver;testis; 0.10809 0.10423 . . 10.96292 0.39613 MRPL35 0.0209370095571054 0.906206936906767 0.0728560535361278 mitochondrial ribosomal protein L35 . . . smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;bone;thyroid;testis;germinal center;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;alveolus;duodenum;liver;spleen;kidney;mammary gland;aorta;stomach; tumor; 0.06977 0.08231 0.371224249 75.12384996 2473.66756 9.26961 MRPL35P1 . . . mitochondrial ribosomal protein L35 pseudogene 1 . . . . . . . . . . . MRPL35P2 . . . mitochondrial ribosomal protein L35 pseudogene 2 . . . . . . . . . . . MRPL35P3 . . . mitochondrial ribosomal protein L35 pseudogene 3 . . . . . . . . . . . MRPL35P4 . . . mitochondrial ribosomal protein L35 pseudogene 4 . . . . . . . . . . . MRPL36 0.254818113331356 0.640690714295417 0.104491172373227 mitochondrial ribosomal protein L36 FUNCTION: Component of the large subunit of the mitochondrial ribosome. {ECO:0000305}.; . . . . 0.13201 0.08098 -0.073340031 48.11866006 19.96463 0.68010 MRPL36P1 . . . mitochondrial ribosomal protein L36 pseudogene 1 . . . . . . . . . . . MRPL37 0.000268371179907098 0.931658288665419 0.0680733401546739 mitochondrial ribosomal protein L37 . . . ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;larynx;testis;unclassifiable (Anatomical System);lymph node;trophoblast;hypothalamus;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus; fetal liver;superior cervical ganglion;heart;liver;tumor;kidney; 0.33669 0.07784 0.020302773 55.60863411 4624.843 13.68599 MRPL37P1 . . . mitochondrial ribosomal protein L37 pseudogene 1 . . . . . . . . . . . MRPL38 4.08583632282511e-06 0.604508332153175 0.395487582010502 mitochondrial ribosomal protein L38 . . . medulla oblongata;ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;iris;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;aorta; . 0.11479 . 0.022122107 55.69120075 483.612 4.52790 MRPL39 0.000718691512555642 0.980539318585935 0.0187419899015089 mitochondrial ribosomal protein L39 . . TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed. Isoform 2 is heart-specific.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;muscle;adrenal cortex;pharynx;blood;lens;breast;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;alveolus;liver;spleen;kidney;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.14902 0.11367 0.222355725 68.44184949 95.66892 2.11384 MRPL40 0.0200816914982677 0.903191255645186 0.0767270528565462 mitochondrial ribosomal protein L40 . . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9790763}.; myocardium;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;gum;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;oral cavity;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; kidney;skeletal muscle; 0.04425 0.06146 0.082802743 60.09082331 1821.1164 7.87126 MRPL40P1 . . . mitochondrial ribosomal protein L40 pseudogene 1 . . . . . . . . . . . MRPL41 0.213388424979656 0.648015827962758 0.138595747057585 mitochondrial ribosomal protein L41 FUNCTION: Component of the mitochondrial ribosome large subunit. Also involved in apoptosis and cell cycle. Enhances p53/TP53 stability, thereby contributing to p53/TP53-induced apoptosis in response to growth-inhibitory condition. Enhances p53/TP53 translocation to the mitochondria. Has the ability to arrest the cell cycle at the G1 phase, possibly by stabilizing the CDKN1A and CDKN1B (p27Kip1) proteins. {ECO:0000269|PubMed:16024796, ECO:0000269|PubMed:16256947}.; . TISSUE SPECIFICITY: Present in kidney, liver, thymus and testis, and at lower level in brain and spleen (at protein level). {ECO:0000269|PubMed:15547950}.; . . 0.08838 0.11067 0.03689118 56.64071715 21.00646 0.71112 MRPL42 0.0278815666313714 0.79737330295254 0.174745130416089 mitochondrial ribosomal protein L42 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;pharynx;blood;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;cervix;head and neck;kidney;mammary gland;aorta;stomach; fetal liver;testis - interstitial;smooth muscle;testis - seminiferous tubule;testis;tumor;white blood cells; 0.03676 0.06595 -0.251530012 35.42108988 54.00078 1.46532 MRPL42P1 . . . mitochondrial ribosomal protein L42 pseudogene 1 . . . . . . . . . . . MRPL42P2 . . . mitochondrial ribosomal protein L42 pseudogene 2 . . . . . . . . . . . MRPL42P3 . . . mitochondrial ribosomal protein L42 pseudogene 3 . . . . . . . . . . . MRPL42P4 . . . mitochondrial ribosomal protein L42 pseudogene 4 . . . . . . . . . . . MRPL42P5 . . . mitochondrial ribosomal protein L42 pseudogene 5 . . . . . . . . . . . MRPL42P6 . . . mitochondrial ribosomal protein L42 pseudogene 6 . . . . . . . . . . . MRPL43 0.000110895960635175 0.821609330499861 0.178279773539503 mitochondrial ribosomal protein L43 . . TISSUE SPECIFICITY: High relative levels in skeletal muscle and testis. Lower levels of expression in the heart, brain, placenta, lung, liver, kidney, pancreas, spleen, thymus, prostate, ovary, small intestine, colon and leukocytes. Expression is coregulated with PEO1. {ECO:0000269|PubMed:15509589}.; ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve; . 0.16806 0.09630 -0.049474214 50.01179523 33.61939 1.03776 MRPL44 9.27743859396845e-06 0.328144990348741 0.671845732212665 mitochondrial ribosomal protein L44 FUNCTION: Component of the 39S subunit of mitochondrial ribosome. May have a function in the assembly/stability of nascent mitochondrial polypeptides exiting the ribosome. {ECO:0000269|PubMed:23315540}.; DISEASE: Combined oxidative phosphorylation deficiency 16 (COXPD16) [MIM:615395]: An autosomal recessive, mitochondrial disorder characterized by hypertrophic cardiomyopathy, liver steatosis, and decreased levels of mitochondrial complexes I and IV in heart and skeletal muscle. {ECO:0000269|PubMed:23315540}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;oesophagus;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;bile duct;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.09442 0.11530 -0.26993514 34.59542345 239.19614 3.34196 MRPL45 0.00150596984840505 0.967500649552912 0.0309933805986833 mitochondrial ribosomal protein L45 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.18707 . 0.17280645 65.75843359 2160.94669 8.55003 MRPL45P1 . . . mitochondrial ribosomal protein L45 pseudogene 1 . . . . . . . . . . . MRPL45P2 . . . mitochondrial ribosomal protein L45 pseudogene 2 . . . . . . . . . . . MRPL46 8.03007555320251e-07 0.293933195135839 0.706066001856605 mitochondrial ribosomal protein L46 . . . . . 0.05934 0.09052 0.661468037 84.4420854 491.98042 4.56141 MRPL47 0.000142436318907292 0.860542657671655 0.139314906009438 mitochondrial ribosomal protein L47 . . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;lymph node;heart;tongue;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;alveolus;hypopharynx;liver;head and neck;cervix;kidney;aorta;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.07379 . 0.43736446 77.56546355 1044.21759 6.20337 MRPL48 0.138891984829277 0.841256690974221 0.0198513241965017 mitochondrial ribosomal protein L48 . . . myocardium;smooth muscle;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;caudate nucleus;trigeminal ganglion;skeletal muscle;skin;parietal lobe; 0.11788 0.09364 0.014844891 54.94810097 193.07651 3.01163 MRPL48P1 . . . mitochondrial ribosomal protein L48 pseudogene 1 . . . . . . . . . . . MRPL49 0.0423029188906129 0.846578094496108 0.111118986613279 mitochondrial ribosomal protein L49 . . TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;hypothalamus;muscle;pancreas;lung;mesenchyma;nasopharynx;placenta;head and neck;kidney;stomach;thymus; superior cervical ganglion;adrenal gland;kidney;trigeminal ganglion; 0.10382 0.15671 -0.007201372 53.19061099 49.68748 1.38211 MRPL49P1 . . . mitochondrial ribosomal protein L49 pseudogene 1 . . . . . . . . . . . MRPL49P2 . . . mitochondrial ribosomal protein L49 pseudogene 2 . . . . . . . . . . . MRPL50 0.00031841038474517 0.583534851153072 0.416146738462183 mitochondrial ribosomal protein L50 . . . . . 0.18454 . 0.104848986 61.49445624 658.09535 5.14478 MRPL50P1 . . . mitochondrial ribosomal protein L50 pseudogene 1 . . . . . . . . . . . MRPL50P2 . . . mitochondrial ribosomal protein L50 pseudogene 2 . . . . . . . . . . . MRPL50P3 . . . mitochondrial ribosomal protein L50 pseudogene 3 . . . . . . . . . . . MRPL50P4 . . . mitochondrial ribosomal protein L50 pseudogene 4 . . . . . . . . . . . MRPL51 0.0667471984789823 0.871325201495017 0.0619276000260009 mitochondrial ribosomal protein L51 . . . lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;choroid;vein;uterus;whole body;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; . 0.07664 0.07413 0.147123112 64.11299835 21.44743 0.72369 MRPL51P1 . . . mitochondrial ribosomal protein L51 pseudogene 1 . . . . . . . . . . . MRPL51P2 . . . mitochondrial ribosomal protein L51 pseudogene 2 . . . . . . . . . . . MRPL52 0.000108205112146637 0.590927605202958 0.408964189684896 mitochondrial ribosomal protein L52 . . . unclassifiable (Anatomical System);meninges;heart;ovary;epidermis;colon;parathyroid;vein;skin;skeletal muscle;bone marrow;uterus;pia mater;lung;placenta;visual apparatus;dura mater;kidney;brain;aorta;stomach; subthalamic nucleus;globus pallidus;caudate nucleus;kidney;parietal lobe; 0.02834 0.04392 0.569646743 81.88841708 17.44704 0.61182 MRPL53 0.222249430173565 0.647347561862582 0.130403007963853 mitochondrial ribosomal protein L53 . . . ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;larynx;bone;thyroid;testis;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; . 0.09402 . 0.747842143 86.47676339 103.35035 2.19626 MRPL53P1 . . . mitochondrial ribosomal protein L53 pseudogene 1 . . . . . . . . . . . MRPL54 0.0856958675435356 0.760716383516738 0.153587748939727 mitochondrial ribosomal protein L54 . . . lymphoreticular;smooth muscle;ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;endometrium;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;pineal body;muscle;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;duodenum;spleen;kidney;mammary gland;stomach;aorta; . 0.08231 . -0.095386216 46.48502005 26.39683 0.85471 MRPL55 0.000411107916634712 0.639364740121283 0.360224151962082 mitochondrial ribosomal protein L55 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;tongue;hypothalamus;lens;skeletal muscle;pancreas;lung;placenta;hippocampus;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.04690 0.08654 0.283038099 71.26680821 163.07847 2.78782 MRPL57 . . . mitochondrial ribosomal protein L57 . . . . . 0.11025 . 0.325313577 73.11276244 . . MRPL57P1 . . . mitochondrial ribosomal protein L57 pseudogene 1 . . . . . . . . . . . MRPL57P2 . . . mitochondrial ribosomal protein L57 pseudogene 2 . . . . . . . . . . . MRPL57P3 . . . mitochondrial ribosomal protein L57 pseudogene 3 . . . . . . . . . . . MRPL57P6 . . . mitochondrial ribosomal protein L57 pseudogene 6 . . . . . . . . . . . MRPL57P7 . . . mitochondrial ribosomal protein L57 pseudogene 7 . . . . . . . . . . . MRPL57P8 . . . mitochondrial ribosomal protein L57 pseudogene 8 . . . . . . . . . . . MRPL57P9 . . . mitochondrial ribosomal protein L57 pseudogene 9 . . . . . . . . . . . MRPL57P10 . . . mitochondrial ribosomal protein L57 pseudogene 10 . . . . . . . . . . . MRPS2 0.0372234054354855 0.834025329431176 0.128751265133339 mitochondrial ribosomal protein S2 . . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; cerebellum; 0.16286 0.15786 0.597144447 82.7435716 356.20608 3.99508 MRPS5 0.0063387043052427 0.989503760067921 0.00415753562683672 mitochondrial ribosomal protein S5 . . . smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;oesophagus;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.05227 0.08107 -0.244249595 36.17008728 267.95715 3.51207 MRPS5P3 . . . mitochondrial ribosomal protein S5 pseudogene 3 . . . . . . . . . . . MRPS5P4 . . . mitochondrial ribosomal protein S5 pseudogene 4 . . . . . . . . . . . MRPS6 0.136243672723326 0.779891797315878 0.0838645299607967 mitochondrial ribosomal protein S6 . . . . . 0.10161 0.04472 0.058937498 58.26256192 41.76645 1.21709 MRPS6P1 . . . mitochondrial ribosomal protein S6 pseudogene 1 . . . . . . . . . . . MRPS6P2 . . . mitochondrial ribosomal protein S6 pseudogene 2 . . . . . . . . . . . MRPS6P4 . . . mitochondrial ribosomal protein S6 pseudogene 4 . . . . . . . . . . . MRPS7 0.00249161801672261 0.780072611807382 0.217435770175895 mitochondrial ribosomal protein S7 . . . myocardium;lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;iris;germinal center;bladder;brain;tonsil;heart;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;hypothalamus;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; thalamus;globus pallidus;testis;trigeminal ganglion;parietal lobe;skeletal muscle; 0.06331 0.23960 0.72761005 86.08162302 255.36308 3.43744 MRPS7P1 . . . mitochondrial ribosomal protein S7 pseudogene 1 . . . . . . . . . . . MRPS7P2 . . . mitochondrial ribosomal protein S7 pseudogene 2 . . . . . . . . . . . MRPS9 3.35947244572882e-06 0.937535660519142 0.0624609800084121 mitochondrial ribosomal protein S9 . . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;uterus;prostate;endometrium;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;breast;lung;nasopharynx;placenta;visual apparatus;liver;kidney;mammary gland;stomach; . 0.30338 0.08725 0.396906589 76.30927105 109.2592 2.26979 MRPS10 0.0282121460745838 0.922237700686103 0.0495501532393127 mitochondrial ribosomal protein S10 . . . ovary;salivary gland;intestine;colon;vein;skin;retina;bone marrow;uterus;prostate;endometrium;bone;thyroid;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach;aorta;cerebellum; amygdala;superior cervical ganglion;pons;parietal lobe;skeletal muscle; 0.19668 0.10229 -0.0274281 51.65723048 31.89637 1.00349 MRPS10P1 . . . mitochondrial ribosomal protein S10 pseudogene 1 . . . . . . . . . . . MRPS10P2 . . . mitochondrial ribosomal protein S10 pseudogene 2 . . . . . . . . . . . MRPS10P5 . . . mitochondrial ribosomal protein S10 pseudogene 5 . . . . . . . . . . . MRPS11 0.000434481626027353 0.651388587946471 0.348176930427502 mitochondrial ribosomal protein S11 . . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; whole brain;heart;liver;testis; 0.08933 0.10502 -0.093566408 46.7386176 326.37982 3.84074 MRPS11P1 . . . mitochondrial ribosomal protein S11 pseudogene 1 . . . . . . . . . . . MRPS12 0.0104262673685507 0.612392218885611 0.377181513745838 mitochondrial ribosomal protein S12 . . . lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;iris;testis;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;hippocampus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum; whole brain;superior cervical ganglion;lung;heart;liver;tumor;ciliary ganglion;trigeminal ganglion; 0.31923 0.17492 -0.139478553 43.29440906 162.82289 2.78572 MRPS14 0.00165874458756506 0.699407520399682 0.298933735012752 mitochondrial ribosomal protein S14 . . . . . 0.10899 . -0.229483771 36.86010852 7.82029 0.28731 MRPS15 0.000342016118820908 0.949346716561291 0.0503112673198877 mitochondrial ribosomal protein S15 . . . . . 0.10308 0.06601 -0.093566408 46.7386176 163.76941 2.79543 MRPS15P1 . . . mitochondrial ribosomal protein S15 pseudogene 1 . . . . . . . . . . . MRPS15P2 . . . mitochondrial ribosomal protein S15 pseudogene 2 . . . . . . . . . . . MRPS16 0.0827659032788113 0.757458736183698 0.15977536053749 mitochondrial ribosomal protein S16 . DISEASE: Combined oxidative phosphorylation deficiency 2 (COXPD2) [MIM:610498]: A mitochondrial disease resulting in fatal neonatal metabolic acidosis with agenesis of the corpus callosum. {ECO:0000269|PubMed:15505824}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.05236 0.07936 0.193034296 66.82000472 316.49138 3.77828 MRPS16P1 . . . mitochondrial ribosomal protein S16 pseudogene 1 . . . . . . . . . . . MRPS16P2 . . . mitochondrial ribosomal protein S16 pseudogene 2 . . . . . . . . . . . MRPS16P3 . . . mitochondrial ribosomal protein S16 pseudogene 3 . . . . . . . . . . . MRPS17 0.74281378474708 0.246353362473677 0.0108328527792424 mitochondrial ribosomal protein S17 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;iris;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; . 0.17221 0.11928 0.237127192 68.98443029 106.31598 2.23733 MRPS17P1 . . . mitochondrial ribosomal protein S17 pseudogene 1 . . . . . . . . . . . MRPS17P3 . . . mitochondrial ribosomal protein S17 pseudogene 3 . . . . . . . . . . . MRPS17P5 . . . mitochondrial ribosomal protein S17 pseudogene 5 . . . . . . . . . . . MRPS17P6 . . . mitochondrial ribosomal protein S17 pseudogene 6 . . . . . . . . . . . MRPS17P7 . . . mitochondrial ribosomal protein S17 pseudogene 7 . . . . . . . . . . . MRPS17P9 . . . mitochondrial ribosomal protein S17 pseudogene 9 . . . . . . . . . . . MRPS18A 0.00112610816941113 0.835990191467555 0.162883700363034 mitochondrial ribosomal protein S18A . . . . . 0.05851 0.07240 -0.161524709 41.6430762 103.23438 2.19442 MRPS18AP1 . . . mitochondrial ribosomal protein S18A pseudogene 1 . . . . . . . . . . . MRPS18B 0.000565208886259378 0.894789520646845 0.104645270466896 mitochondrial ribosomal protein S18B . . . lymphoreticular;medulla oblongata;ovary;umbilical cord;skin;corpus callosum;bone marrow;prostate;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;cerebral cortex;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; . 0.09861 . -0.049474214 50.01179523 389.2125 4.15453 MRPS18BP1 . . . mitochondrial ribosomal protein S18B pseudogene 1 . . . . . . . . . . . MRPS18BP2 . . . mitochondrial ribosomal protein S18B pseudogene 2 . . . . . . . . . . . MRPS18C 0.00897318619515012 0.806107920724748 0.184918893080102 mitochondrial ribosomal protein S18C . . . ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;bile duct;breast;lung;cornea;adrenal gland;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion; 0.06122 0.08072 0.169169615 65.33380514 8.0551 0.29562 MRPS18CP2 . . . mitochondrial ribosomal protein S18C pseudogene 2 . . . . . . . . . . . MRPS18CP3 . . . mitochondrial ribosomal protein S18C pseudogene 3 . . . . . . . . . . . MRPS18CP4 . . . mitochondrial ribosomal protein S18C pseudogene 4 . . . . . . . . . . . MRPS18CP5 . . . mitochondrial ribosomal protein S18C pseudogene 5 . . . . . . . . . . . MRPS18CP6 . . . mitochondrial ribosomal protein S18C pseudogene 6 . . . . . . . . . . . MRPS21 0.353450051428985 0.592547299997293 0.0540026485737218 mitochondrial ribosomal protein S21 . . . lymphoreticular;ovary;umbilical cord;foreskin;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;tongue;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;uterus;cerebral cortex;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;lung;cornea;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;testis - interstitial;medulla oblongata;superior cervical ganglion;temporal lobe;pons;trigeminal ganglion;cingulate cortex; . 0.06721 0.924227736 89.61429582 856.957 5.71331 MRPS21P1 . . . mitochondrial ribosomal protein S21 pseudogene 1 . . . . . . . . . . . MRPS21P2 . . . mitochondrial ribosomal protein S21 pseudogene 2 . . . . . . . . . . . MRPS21P3 . . . mitochondrial ribosomal protein S21 pseudogene 3 . . . . . . . . . . . MRPS21P4 . . . mitochondrial ribosomal protein S21 pseudogene 4 . . . . . . . . . . . MRPS21P5 . . . mitochondrial ribosomal protein S21 pseudogene 5 . . . . . . . . . . . MRPS21P6 . . . mitochondrial ribosomal protein S21 pseudogene 6 . . . . . . . . . . . MRPS21P7 . . . mitochondrial ribosomal protein S21 pseudogene 7 . . . . . . . . . . . MRPS21P8 . . . mitochondrial ribosomal protein S21 pseudogene 8 . . . . . . . . . . . MRPS21P9 . . . mitochondrial ribosomal protein S21 pseudogene 9 . . . . . . . . . . . MRPS22 6.39409151183266e-05 0.900500032926545 0.0994360261583364 mitochondrial ribosomal protein S22 . DISEASE: Combined oxidative phosphorylation deficiency 5 (COXPD5) [MIM:611719]: A mitochondrial disease resulting in severe metabolic acidosis, edema, hypertrophic cardiomyopathy, tubulopathy, and hypotonia. {ECO:0000269|PubMed:17873122}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;gum;bone;iris;pituitary gland;testis;germinal center;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;testis - interstitial;testis;globus pallidus;trigeminal ganglion;skeletal muscle;parietal lobe; 0.05494 0.20364 0.439181676 77.69521113 116.21802 2.34458 MRPS22P1 . . . mitochondrial ribosomal protein S22 pseudogene 1 . . . . . . . . . . . MRPS23 0.0494860578184962 0.928059969795396 0.0224539723861082 mitochondrial ribosomal protein S23 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;spinal cord;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;trabecular meshwork;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; whole brain;occipital lobe;adrenal gland;tumor;testis;white blood cells; 0.11485 0.07926 -0.317668748 31.45789101 40.1519 1.17992 MRPS23P1 . . . mitochondrial ribosomal protein S23 pseudogene 1 . . . . . . . . . . . MRPS24 0.0016576685245083 0.699271576568638 0.299070754906853 mitochondrial ribosomal protein S24 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;synovium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; . 0.07088 0.08259 0.569646743 81.88841708 455.81027 4.43690 MRPS24P1 . . . mitochondrial ribosomal protein S24 pseudogene 1 . . . . . . . . . . . MRPS25 0.545528804168266 0.440414241896924 0.0140569539348105 mitochondrial ribosomal protein S25 . . . myocardium;lymphoreticular;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;iris;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;cornea;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.11900 0.09780 0.125076652 62.7388535 16.19965 0.57440 MRPS25P1 . . . mitochondrial ribosomal protein S25 pseudogene 1 . . . . . . . . . . . MRPS26 0.187857587540762 0.762148524558743 0.049993887900495 mitochondrial ribosomal protein S26 . . . . . 0.10007 0.08706 . . 10.24285 0.37333 MRPS27 0.0285866865587268 0.969166797408084 0.00224651603318908 mitochondrial ribosomal protein S27 . . . lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;amygdala;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach;aorta; globus pallidus;tumor;caudate nucleus;kidney;cingulate cortex;cerebellum; 0.05095 0.08353 0.485092724 79.37603208 2175.55407 8.58676 MRPS28 0.000355479735890669 0.380405835274599 0.61923868498951 mitochondrial ribosomal protein S28 . . . myocardium;smooth muscle;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;head and neck;kidney;mammary gland;stomach; whole brain; 0.27868 0.09721 0.903992902 89.39018636 367.35561 4.05172 MRPS30 5.58147796749342e-05 0.884305639815306 0.11563854540502 mitochondrial ribosomal protein S30 . . TISSUE SPECIFICITY: Heart, skeletal muscle, kidney and liver. Lower expression in placenta and peripheral blood leukocytes. {ECO:0000269|PubMed:10640817, ECO:0000269|PubMed:11279123}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;whole brain;superior cervical ganglion;testis;atrioventricular node;pons;trigeminal ganglion;cingulate cortex; 0.35441 0.10047 0.753291803 86.71266808 151.99909 2.69680 MRPS31 4.09360421604781e-05 0.840491848119614 0.159467215838226 mitochondrial ribosomal protein S31 . . . unclassifiable (Anatomical System);whole body;nasopharynx;colon;blood;skeletal muscle;bone marrow; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;temporal lobe;prefrontal cortex;testis;ciliary ganglion; 0.17192 0.06840 0.040529541 57.15380986 2389.9021 9.06971 MRPS31P1 . . . mitochondrial ribosomal protein S31 pseudogene 1 . . . . . . . . . . . MRPS31P2 . . . mitochondrial ribosomal protein S31 pseudogene 2 . . . . . . . . . . . MRPS31P4 . . . mitochondrial ribosomal protein S31 pseudogene 4 . . . . . . . . . . . MRPS31P5 . . . mitochondrial ribosomal protein S31 pseudogene 5 . . . . . . . . . . . MRPS33 0.00339571782411825 0.61323109958273 0.383373182593152 mitochondrial ribosomal protein S33 . . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;pituitary gland;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;breast;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; testis - interstitial;testis; 0.08462 0.07050 0.147123112 64.11299835 217.29715 3.18566 MRPS33P1 . . . mitochondrial ribosomal protein S33 pseudogene 1 . . . . . . . . . . . MRPS33P2 . . . mitochondrial ribosomal protein S33 pseudogene 2 . . . . . . . . . . . MRPS33P3 . . . mitochondrial ribosomal protein S33 pseudogene 3 . . . . . . . . . . . MRPS33P4 . . . mitochondrial ribosomal protein S33 pseudogene 4 . . . . . . . . . . . MRPS34 5.52343942722583e-05 0.262763565636208 0.73718119996952 mitochondrial ribosomal protein S34 FUNCTION: Required for mitochondrial translation, plays a role in maintaining the stability of the small ribosomal subunit and the 12S rRNA that are required for mitoribosome formation. {ECO:0000250|UniProtKB:Q9JIK9}.; . . lymphoreticular;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; whole brain;tumor; 0.16298 0.24455 . . 5530.24827 15.35450 MRPS35 0.0409282753572301 0.952710888182005 0.00636083646076451 mitochondrial ribosomal protein S35 . . . lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;germinal center;bladder;brain;gall bladder;amygdala;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;salivary gland;intestine;colon;parathyroid;uterus;whole body;bone;pituitary gland;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; thalamus;superior cervical ganglion;subthalamic nucleus;medulla oblongata;kidney;parietal lobe; 0.04816 0.08045 -0.179930907 40.35739561 598.28164 4.95167 MRPS35P1 . . . mitochondrial ribosomal protein S35 pseudogene 1 . . . . . . . . . . . MRPS35P2 . . . mitochondrial ribosomal protein S35 pseudogene 2 . . . . . . . . . . . MRPS35P3 . . . mitochondrial ribosomal protein S35 pseudogene 3 . . . . . . . . . . . MRPS36 0.746558796887922 0.2430356863353 0.0104055167767775 mitochondrial ribosomal protein S36 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;cochlea;bone;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pharynx;blood;lung;cornea;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.12511 0.11308 -0.009020804 52.8544468 51.6496 1.41890 MRPS36P1 . . . mitochondrial ribosomal protein S36 pseudogene 1 . . . . . . . . . . . MRPS36P2 . . . mitochondrial ribosomal protein S36 pseudogene 2 . . . . . . . . . . . MRPS36P3 . . . mitochondrial ribosomal protein S36 pseudogene 3 . . . . . . . . . . . MRPS36P4 . . . mitochondrial ribosomal protein S36 pseudogene 4 . . . . . . . . . . . MRPS36P5 . . . mitochondrial ribosomal protein S36 pseudogene 5 . . . . . . . . . . . MRPS36P6 . . . mitochondrial ribosomal protein S36 pseudogene 6 . . . . . . . . . . . MRRF 3.57943059722468e-05 0.368057121236867 0.631907084457161 mitochondrial ribosome recycling factor FUNCTION: Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another (By similarity). {ECO:0000250}.; . . ovary;sympathetic chain;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;endometrium;gum;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;blood;skeletal muscle;bile duct;lung;placenta;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.22804 0.22529 0.194852702 67.03231894 81.62818 1.91333 MRRFP1 . . . mitochondrial ribosome recycling factor pseudogene 1 . . . . . . . . . . . MRS2 8.84583170646535e-05 0.984233251015226 0.0156782906677093 MRS2, magnesium transporter FUNCTION: Magnesium transporter that may mediate the influx of magnesium into the mitochondrial matrix. {ECO:0000269|PubMed:11401429}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;cochlea;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;epididymis;placenta;macula lutea;visual apparatus;liver;cervix;kidney;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.26068 0.46457 0.310540264 72.65864591 1243.15937 6.66012 MRS2P1 . . . MRS2 pseudogene 1 . . . . . . . . . . . MRS2P2 . . . MRS2 pseudogene 2 . . . . . . . . . . . MRSD . . . mental retardation-skeletal dysplasia . . . . . . . . . . . MRT4 . . . mental retardation, non-syndromic, autosomal recessive, 4 . . . . . . . . . . . MRT8 . . . mental retardation, non-syndromic, autosomal recessive, 8 . . . . . . . . . . . MRT9 . . . mental retardation, non-syndromic, autosomal recessive, 9 . . . . . . . . . . . MRT10 . . . mental retardation, non-syndromic, autosomal recessive, 10 . . . . . . . . . . . MRT11 . . . mental retardation, non-syndromic, autosomal recessive, 11 . . . . . . . . . . . MRT17 . . . mental retardation, non-syndromic, autosomal recessive, 17 . . . . . . . . . . . MRT18 . . . mental retardation, non-syndromic, autosomal recessive, 18 . . . . . . . . . . . MRT19 . . . mental retardation, non-syndromic, autosomal recessive, 19 . . . . . . . . . . . MRT20 . . . mental retardation, non-syndromic, autosomal recessive, 20 . . . . . . . . . . . MRT22 . . . mental retardation, non-syndromic, autosomal recessive, 22 . . . . . . . . . . . MRT23 . . . mental retardation, non-syndromic, autosomal recessive, 23 . . . . . . . . . . . MRT24 . . . mental retardation, non-syndromic, autosomal recessive, 24 . . . . . . . . . . . MRT25 . . . mental retardation, non-syndromic, autosomal recessive, 25 . . . . . . . . . . . MRT26 . . . mental retardation, non-syndromic, autosomal recessive, 26 . . . . . . . . . . . MRT27 . . . mental retardation, non-syndromic, autosomal recessive, 27 . . . . . . . . . . . MRT28 . . . mental retardation, non-syndromic, autosomal recessive, 28 . . . . . . . . . . . MRTO4 0.869977920352301 0.129656255969218 0.000365823678480529 MRT4 homolog, ribosome maturation factor FUNCTION: Component of the ribosome assembly machinery. Nuclear paralog of the ribosomal protein P0, it binds pre-60S subunits at an early stage of assembly in the nucleolus, and is replaced by P0 in cytoplasmic pre-60S subunits and mature 80S ribosomes. {ECO:0000269|PubMed:20083226}.; . . . . 0.25998 0.13531 -0.337894035 30.37272942 63.66233 1.63507 MRVI1 0.00184121524712682 0.997951296541003 0.000207488211870323 murine retrovirus integration site 1 homolog FUNCTION: Plays a role as NO/PRKG1-dependent regulator of IP3- induced calcium release; its phosphorylation by PRKG1 inhibits bradykinin and IP3-induced calcium release from intracellular stores. Recruits PRKG1 to the endoplasmic reticulum and may mediate the assembly of PRKG1 and ITPR1 in a macrocomplex. Involved in PRKG1 signaling cascade leading to inhibition of platelet activation and aggregation. Mediates also NO-dependent inhibition of calcium signaling in gastrointestinal smooth muscle contributing to NO-dependent relaxation. {ECO:0000269|PubMed:14729908}.; . TISSUE SPECIFICITY: Expressed in the colon, rectum, and cultured colonic smooth muscle. Detected in various cancer cell lines. {ECO:0000269|PubMed:10321731, ECO:0000269|PubMed:14729908}.; unclassifiable (Anatomical System);amygdala;heart;ovary;fovea centralis;choroid;lens;skeletal muscle;skin;retina;bone marrow;uterus;pancreas;optic nerve;lung;frontal lobe;placenta;macula lutea;visual apparatus;testis;brain;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.26509 0.11044 2.074301918 97.81788158 1191.5599 6.54536 MRVI1-AS1 . . . MRVI1 antisense RNA 1 . . . . . . . . . . . MRX4 . . . mental retardation, X-linked 4 . . . . . . . . . . . MRX5 . . . mental retardation, X-linked 5 . . . . . . . . . . . MRX6 . . . mental retardation, X-linked 6 (Okinawa type) . . . . . . . . . . . MRX7 . . . mental retardation, X-linked 7 . . . . . . . . . . . MRX8 . . . mental retardation, X-linked 8 . . . . . . . . . . . MRX11 . . . mental retardation, X-linked 11 . . . . . . . . . . . MRX14 . . . mental retardation, X-linked 14 . . . . . . . . . . . MRX15 . . . mental retardation, X-linked 15 . . . . . . . . . . . MRX17 . . . mental retardation, X-linked 17 . . . . . . . . . . . MRX18 . . . mental retardation, X-linked 18 . . . . . . . . . . . MRX20 . . . mental retardation, X-linked 20 . . . . . . . . . . . MRX23 . . . mental retardation, X-linked 23 . . . . . . . . . . . MRX24 . . . mental retardation, X-linked 24 . . . . . . . . . . . MRX25 . . . mental retardation, X-linked 25 . . . . . . . . . . . MRX26 . . . mental retardation, X-linked 26 . . . . . . . . . . . MRX27 . . . mental retardation, X-linked 27 . . . . . . . . . . . MRX28 . . . mental retardation, X-linked 28 . . . . . . . . . . . MRX31 . . . mental retardation, X-linked 31 . . . . . . . . . . . MRX37 . . . mental retardation, X-linked 37 . . . . . . . . . . . MRX39 . . . mental retardation, X-linked 39 . . . . . . . . . . . MRX40 . . . mental retardation, X-linked 40 . . . . . . . . . . . MRX42 . . . mental retardation, X-linked 42 . . . . . . . . . . . MRX49 . . . mental retardation, X-linked 49 . . . . . . . . . . . MRX50 . . . mental retardation, X-linked 50 . . . . . . . . . . . MRX51 . . . mental retardation, X-linked 51 . . . . . . . . . . . MRX53 . . . mental retardation, X-linked 53 . . . . . . . . . . . MRX56 . . . mental retardation, X-linked 56 . . . . . . . . . . . MRX57 . . . mental retardation, X-linked 57 . . . . . . . . . . . MRX61 . . . mental retardation, X-linked 61 . . . . . . . . . . . MRX64 . . . mental retardation, X-linked 64 . . . . . . . . . . . MRX65 . . . mental retardation, X-linked 65 . . . . . . . . . . . MRX66 . . . mental retardation, X-linked 66 . . . . . . . . . . . MRX67 . . . mental retardation, X-linked 67 . . . . . . . . . . . MRX69 . . . mental retardation, X-linked 69 . . . . . . . . . . . MRX70 . . . mental retardation, X-linked 70 . . . . . . . . . . . MRX71 . . . mental retardation, X-linked 71 . . . . . . . . . . . MRX73 . . . mental retardation, X-linked 73 . . . . . . . . . . . MRX75 . . . mental retardation, X-linked 75 . . . . . . . . . . . MRX77 . . . mental retardation, X-linked 77 . . . . . . . . . . . MRX78 . . . mental retardation, X-linked 78 . . . . . . . . . . . MRX80 . . . mental retardation, X-linked 80 . . . . . . . . . . . MRX81 . . . mental retardation, X-linked 81 . . . . . . . . . . . MRX82 . . . mental retardation, X-linked 82 . . . . . . . . . . . MRX84 . . . mental retardation, X-linked 84 . . . . . . . . . . . MRX86 . . . mental retardation, X-linked 86 . . . . . . . . . . . MRXS7 . . . mental retardation, X-linked, syndromic 7 . . . . . . . . . . . MRXS11 . . . mental retardation, X-linked, syndromic 11 . . . . . . . . . . . MS . . . multiple sclerosis . . . . . . . . . . . MS4A1 0.0153881692917396 0.879278820442794 0.105333010265466 membrane spanning 4-domains A1 FUNCTION: This protein may be involved in the regulation of B-cell activation and proliferation.; DISEASE: Immunodeficiency, common variable, 5 (CVID5) [MIM:613495]: A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low. {ECO:0000269|PubMed:20038800}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed on B-cells.; unclassifiable (Anatomical System);lymph node;ovary;salivary gland;intestine;pharynx;colon;parathyroid;blood;skin;breast;prostate;pancreas;lung;nasopharynx;liver;testis;germinal center;kidney;brain;bladder; superior cervical ganglion;lymph node;tonsil; 0.19097 0.09550 -0.317668748 31.45789101 28.96649 0.92585 MS4A2 6.49875397938143e-05 0.482069848377851 0.517865164082355 membrane spanning 4-domains A2 FUNCTION: High affinity receptor that binds to the Fc region of immunoglobulins epsilon. Aggregation of FCER1 by multivalent antigens is required for the full mast cell response, including the release of preformed mediators (such as histamine) by degranulation and de novo production of lipid mediators and cytokines. Also mediates the secretion of important lymphokines. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators responsible for the manifestations of allergy.; . TISSUE SPECIFICITY: Found on the surface of mast cells and basophils.; smooth muscle;lung;kidney; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.03710 0.15195 0.905808022 89.4373673 1187.44171 6.53535 MS4A3 4.21112895152531e-05 0.397266709320955 0.60269117938953 membrane spanning 4-domains A3 FUNCTION: Hematopoietic modulator for the G1-S cell cycle transition. Modulates the level of phosphorylation of cyclin- dependent kinase 2 (CDK2) through its direct binding to cyclin- dependent kinase inhibitor 3 (CDKN3/KAP). {ECO:0000269|PubMed:11781350}.; . TISSUE SPECIFICITY: Expressed specifically in hematopoietic cells and tissues.; unclassifiable (Anatomical System);prostate;lung;frontal lobe;liver;blood;bone marrow; bone marrow; 0.07309 0.05063 -0.139478553 43.29440906 19.46533 0.66843 MS4A4A 0.000743081971054817 0.762665916390349 0.236591001638596 membrane spanning 4-domains A4A FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex.; . TISSUE SPECIFICITY: Variable expression in multiple hemopoietic cell lines.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cerebral cortex;endometrium;thyroid;bone;testis;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;placenta; 0.03811 0.05629 0.238945317 69.20853975 673.97104 5.18636 MS4A4E 0.515839923885565 0.41790743071398 0.0662526454004551 membrane spanning 4-domains A4E . . . . . 0.02177 . . . 263.68261 3.48424 MS4A5 0.00920453847809139 0.810265378410147 0.180530083111761 membrane spanning 4-domains A5 FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex.; . TISSUE SPECIFICITY: Expressed at high level in the testis. Detected also in the pancreas, heart and in the brain.; medulla oblongata;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14523 0.08404 0.837848571 88.22835574 577.26453 4.87185 MS4A6A 1.49231954313632e-09 0.0159432336132779 0.984056764894403 membrane spanning 4-domains A6A FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex.; . TISSUE SPECIFICITY: Variable expression in some B-cell, myelomonocytic, and erythroleukemia cell lines.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;dura mater;germinal center;brain;pineal gland;artery;gall bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;skeletal muscle;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hypopharynx;liver;spleen;head and neck;kidney;aorta;stomach; . 0.07184 0.08228 0.483275131 79.25218212 255.99932 3.44087 MS4A6E 0.72055108088883 0.265828100887964 0.013620818223206 membrane spanning 4-domains A6E FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex.; . TISSUE SPECIFICITY: Expressed by malignant and fetal tissue at very low levels.; unclassifiable (Anatomical System);lung;liver;testis;spleen; . 0.00560 0.03892 0.43736446 77.56546355 1624.73138 7.45276 MS4A7 9.27325316417502e-06 0.328072292209666 0.67191843453717 membrane spanning 4-domains A7 FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex.; . TISSUE SPECIFICITY: Ubiquitous expression in normal tissues. Expression is more elevated in adult liver, lung, spleen, and heart than in their fetal counterparts, and is higher in normal tissues than in the cancerous tissue or cell lines. Low levels of expression were detected in the promonocytic stage, whereas high levels of expression were detected in mature monocytes.; ovary;colon;parathyroid;skin;uterus;prostate;frontal lobe;cerebral cortex;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;pancreas;lung;nasopharynx;placenta;liver;spleen;kidney;mammary gland;stomach;thymus; . 0.06038 . 1.038098315 91.20665251 262.16905 3.47484 MS4A8 0.00260921171410416 0.7884934719356 0.208897316350296 membrane spanning 4-domains A8 FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex.; . TISSUE SPECIFICITY: Expressed by hematopoietic tissues and cells lines.; . . 0.08275 0.08259 -0.271755481 34.31823543 12.45228 0.45220 MS4A10 1.79435429349408e-08 0.0675489606262636 0.932451021430194 membrane spanning 4-domains A10 FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex.; . . . . 0.04542 0.06848 0.352813824 74.49280491 256.68523 3.44725 MS4A12 4.95569370765756e-05 0.427986954905229 0.571963488157694 membrane spanning 4-domains A12 FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex.; . . unclassifiable (Anatomical System);colon;kidney;stomach; superior cervical ganglion;trigeminal ganglion; 0.02191 0.04881 0.21689899 68.12927577 7061.94176 17.98564 MS4A13 0.0538658364526184 0.863671897836642 0.0824622657107393 membrane spanning 4-domains A13 FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex. {ECO:0000250}.; . . . . 0.02541 . 0.525552348 80.57914603 58.72726 1.55365 MS4A14 2.18827547869555e-16 0.0010611283918267 0.998938871608173 membrane spanning 4-domains A14 FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;cartilage;ovary;placenta;testis;parathyroid;germinal center;mammary gland;bladder; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.01901 0.04275 1.738023664 96.63246049 1401.7534 6.99926 MS4A15 0.0384681974305748 0.83747803388546 0.124053768683966 membrane spanning 4-domains A15 FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex. {ECO:0000250}.; . . lung;cartilage;colon; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.11624 . 0.705562627 85.52724699 3456.33473 11.29059 MS4A18 . . . membrane spanning 4-domains A18 . . . . . . . . . 64.77397 1.65226 MSANTD1 0.32217221350423 0.611281859032603 0.066545927463167 Myb/SANT DNA binding domain containing 1 . . . . . . 0.08948 . . 1420.1775 7.04063 MSANTD2 0.70997170666646 0.289328092453974 0.000700200879566312 Myb/SANT DNA binding domain containing 2 . . . . . 0.49552 0.10347 -0.449946534 24.00330267 22.28117 0.74710 MSANTD2P1 . . . Myb/SANT DNA binding domain containing 2 pseudogene 1 . . . . . . . . . . . MSANTD3 0.063002985781323 0.869971724177805 0.067025290040872 Myb/SANT DNA binding domain containing 3 . . TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:15334068}.; . . . 0.34677 -0.073340031 48.11866006 228.95203 3.26876 MSANTD3-TMEFF1 . . . MSANTD3-TMEFF1 readthrough FUNCTION: May inhibit NODAL and BMP signaling during neural patterning (By similarity). May be a tumor suppressor in brain cancers. {ECO:0000250, ECO:0000269|PubMed:12743596}.; . TISSUE SPECIFICITY: Expressed predominantly in brain, and at lower levels in heart, placenta and skeletal muscle. Down-regulated in brain tumors as compared to control brain tissues. {ECO:0000269|PubMed:12743596}.; . . . . . . . . MSANTD4 0.00546195429080008 0.970281867758188 0.0242561779510117 Myb/SANT DNA binding domain containing 4 with coiled-coils . . . . . 0.39183 . -0.339715008 30.06605331 10.53049 0.38229 MSBP1 . . . minisatellite binding protein 1 . . . . . . . . . . . MSBP2 . . . minisatellite binding protein 2 . . . . . . . . . . . MSC 0.673682720909904 0.305299055130873 0.0210182239592229 musculin FUNCTION: Transcription repressor capable of inhibiting the transactivation capability of TCF3/E47. May play a role in regulating antigen-dependent B-cell differentiation.; . TISSUE SPECIFICITY: Expressed in lymphoid tissues, B-cell lines and activated B-cells.; unclassifiable (Anatomical System);bile duct;lung;heart;bone;placenta;muscle;colon;kidney;skin;skeletal muscle;stomach; skeletal muscle; 0.32450 0.16823 0.191216164 66.57230479 28.48319 0.91213 MSC-AS1 . . . MSC antisense RNA 1 . . . . . . . . . . . MSD . . . microcephaly with spastic diplegia (Paine syndrome) . . . . . . . . . . . MSGN1 0.191097329641165 0.647084342934823 0.161818327424013 mesogenin 1 FUNCTION: Involved in specifying the paraxial, but not dorsal, mesoderm. May regulate the expression of T-box transcription factors required for mesoderm formation and differentiation (By similarity). {ECO:0000250}.; . . . . 0.27477 0.10402 0.170987912 65.5579146 68.58512 1.71343 MSH2 0.867725630709854 0.13227423852494 1.30765205239918e-07 mutS homolog 2 FUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2- MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis. {ECO:0000269|PubMed:10078208, ECO:0000269|PubMed:10660545, ECO:0000269|PubMed:15064730, ECO:0000269|PubMed:17611581, ECO:0000269|PubMed:9564049, ECO:0000269|PubMed:9822679, ECO:0000269|PubMed:9822680}.; DISEASE: Hereditary non-polyposis colorectal cancer 1 (HNPCC1) [MIM:120435]: An autosomal dominant disease associated with marked increase in cancer susceptibility. It is characterized by a familial predisposition to early-onset colorectal carcinoma (CRC) and extra-colonic tumors of the gastrointestinal, urological and female reproductive tracts. HNPCC is reported to be the most common form of inherited colorectal cancer in the Western world. Clinically, HNPCC is often divided into two subgroups. Type I is characterized by hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon. Type II is characterized by increased risk for cancers in certain tissues such as the uterus, ovary, breast, stomach, small intestine, skin, and larynx in addition to the colon. Diagnosis of classical HNPCC is based on the Amsterdam criteria: 3 or more relatives affected by colorectal cancer, one a first degree relative of the other two; 2 or more generation affected; 1 or more colorectal cancers presenting before 50 years of age; exclusion of hereditary polyposis syndromes. The term 'suspected HNPCC' or 'incomplete HNPCC' can be used to describe families who do not or only partially fulfill the Amsterdam criteria, but in whom a genetic basis for colon cancer is strongly suspected. {ECO:0000269|PubMed:10375096, ECO:0000269|PubMed:10386556, ECO:0000269|PubMed:10528862, ECO:0000269|PubMed:10573010, ECO:0000269|PubMed:10612836, ECO:0000269|PubMed:10777691, ECO:0000269|PubMed:10829038, ECO:0000269|PubMed:11726306, ECO:0000269|PubMed:11870161, ECO:0000269|PubMed:11920458, ECO:0000269|PubMed:12112654, ECO:0000269|PubMed:12124176, ECO:0000269|PubMed:12132870, ECO:0000269|PubMed:12200596, ECO:0000269|PubMed:12362047, ECO:0000269|PubMed:12373605, ECO:0000269|PubMed:12655564, ECO:0000269|PubMed:12655568, ECO:0000269|PubMed:12658575, ECO:0000269|PubMed:14635101, ECO:0000269|PubMed:15046096, ECO:0000269|PubMed:15300854, ECO:0000269|PubMed:15342696, ECO:0000269|PubMed:15365995, ECO:0000269|PubMed:15613555, ECO:0000269|PubMed:15870828, ECO:0000269|PubMed:15896463, ECO:0000269|PubMed:15991316, ECO:0000269|PubMed:15996210, ECO:0000269|PubMed:16451135, ECO:0000269|PubMed:17101317, ECO:0000269|PubMed:17128465, ECO:0000269|PubMed:18561205, ECO:0000269|PubMed:18625694, ECO:0000269|PubMed:22371642, ECO:0000269|PubMed:7874129, ECO:0000269|PubMed:8261515, ECO:0000269|PubMed:8700523, ECO:0000269|PubMed:8872463, ECO:0000269|PubMed:9048925, ECO:0000269|PubMed:9240418, ECO:0000269|PubMed:9298827, ECO:0000269|PubMed:9311737, ECO:0000269|PubMed:9419403, ECO:0000269|PubMed:9559627, ECO:0000269|PubMed:9718327}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Muir-Torre syndrome (MRTES) [MIM:158320]: Rare autosomal dominant disorder characterized by sebaceous neoplasms and visceral malignancy. {ECO:0000269|PubMed:7713503}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of endometrium, the mucous lining of the uterus. Most endometrial cancers are adenocarcinomas, cancers that begin in cells that make and release mucus and other fluids. {ECO:0000305|PubMed:11306449, ECO:0000305|PubMed:21642682}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10856833}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;stomach;thymus; superior cervical ganglion;trigeminal ganglion; 0.99705 0.69313 -2.033907235 1.680820948 376.88542 4.09255 MSH3 4.56585570518733e-23 0.00229475190964188 0.997705248090358 mutS homolog 3 FUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS beta which binds to DNA mismatches thereby initiating DNA repair. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. MutS beta recognizes large insertion- deletion loops (IDL) up to 13 nucleotides long. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis.; DISEASE: Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of endometrium, the mucous lining of the uterus. Most endometrial cancers are adenocarcinomas, cancers that begin in cells that make and release mucus and other fluids. {ECO:0000305|PubMed:8782829}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;heart;muscle;colon;skin;skeletal muscle;bone marrow;breast;uterus;lung;nasopharynx;bone;placenta;hippocampus;liver;testis;cervix;germinal center;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.47698 0.19216 -0.079012906 47.25760793 3510.45198 11.43030 MSH4 3.6994716527544e-15 0.255035447329483 0.744964552670513 mutS homolog 4 FUNCTION: Involved in meiotic recombination. Required for reciprocal recombination and proper segregation of homologous chromosomes at meiosis.; . TISSUE SPECIFICITY: Testis and ovary specific.; unclassifiable (Anatomical System);lung;developmental;testis; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.45352 0.09452 0.202129237 67.42745931 524.99689 4.67524 MSH5 6.13879541730601e-08 0.99968233514959 0.00031760346245614 mutS homolog 5 FUNCTION: Involved in meiotic recombination. Facilitate crossovers between homologs during meiosis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous, but highly expressed in testis, and thymus.; . . 0.17868 . 0.134171522 63.57041755 1222.62198 6.61100 MSH5-SAPCD1 . . . MSH5-SAPCD1 readthrough (NMD candidate) . . . . . . . . . . . MSH6 . . . mutS homolog 6 FUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction. {ECO:0000269|PubMed:10078208, ECO:0000269|PubMed:10660545, ECO:0000269|PubMed:15064730, ECO:0000269|PubMed:23622243, ECO:0000269|PubMed:9564049, ECO:0000269|PubMed:9822679, ECO:0000269|PubMed:9822680}.; DISEASE: Hereditary non-polyposis colorectal cancer 5 (HNPCC5) [MIM:614350]: An autosomal dominant disease associated with marked increase in cancer susceptibility. It is characterized by a familial predisposition to early-onset colorectal carcinoma (CRC) and extra-colonic tumors of the gastrointestinal, urological and female reproductive tracts. HNPCC is reported to be the most common form of inherited colorectal cancer in the Western world. Clinically, HNPCC is often divided into two subgroups. Type I is characterized by hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon. Type II is characterized by increased risk for cancers in certain tissues such as the uterus, ovary, breast, stomach, small intestine, skin, and larynx in addition to the colon. Diagnosis of classical HNPCC is based on the Amsterdam criteria: 3 or more relatives affected by colorectal cancer, one a first degree relative of the other two; 2 or more generation affected; 1 or more colorectal cancers presenting before 50 years of age; exclusion of hereditary polyposis syndromes. The term 'suspected HNPCC' or 'incomplete HNPCC' can be used to describe families who do not or only partially fulfill the Amsterdam criteria, but in whom a genetic basis for colon cancer is strongly suspected. {ECO:0000269|PubMed:10480359, ECO:0000269|PubMed:10521294, ECO:0000269|PubMed:11586295, ECO:0000269|PubMed:12658575, ECO:0000269|PubMed:14974087, ECO:0000269|PubMed:15365995, ECO:0000269|PubMed:9354786}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of endometrium, the mucous lining of the uterus. Most endometrial cancers are adenocarcinomas, cancers that begin in cells that make and release mucus and other fluids. {ECO:0000269|PubMed:11153917, ECO:0000269|PubMed:14961575}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Mismatch repair cancer syndrome (MMRCS) [MIM:276300]: An autosomal recessive, rare, childhood cancer predisposition syndrome encompassing a broad tumor spectrum. This includes hematological malignancies, central nervous system tumors, Lynch syndrome-associated malignancies such as colorectal tumors as well as multiple intestinal polyps, embryonic tumors and rhabdomyosarcoma. Multiple cafe-au-lait macules, a feature reminiscent of neurofibromatosis type 1, are often found as first manifestation of the underlying cancer. Areas of skin hypopigmentation have also been reported in MMRCS patients. {ECO:0000269|PubMed:17557300}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; fetal liver;testis - interstitial;testis - seminiferous tubule;tumor;testis;pons; 0.97386 0.77704 -2.250890405 1.279782968 1431.22959 7.06202 MSI1 0.997146450593471 0.00285341298165255 1.36424876836027e-07 musashi RNA binding protein 1 FUNCTION: RNA binding protein that regulates the expression of target mRNAs at the translation level. Regulates expression of the NOTCH1 antagonist NUMB. Binds RNA containing the sequence 5'- GUUAGUUAGUUAGUU-3' and other sequences containing the pattern 5'- [GA]U(1-3)AGU-3'. May play a role in the proliferation and maintenance of stem cells in the central nervous system (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in fetal kidney, brain, liver and lung, and in adult brain and pancreas. Detected in hepatoma cell lines. {ECO:0000269|PubMed:12054577, ECO:0000269|PubMed:9790759}.; unclassifiable (Anatomical System);optic nerve;lung;islets of Langerhans;macula lutea;visual apparatus;testis;fovea centralis;choroid;lens;brain;mammary gland;retina; superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.66447 0.10166 -0.161524709 41.6430762 9.92984 0.36366 MSI2 0.963858041525188 0.0361279107592833 1.40477155282637e-05 musashi RNA binding protein 2 FUNCTION: RNA binding protein that regulates the expression of target mRNAs at the translation level. May play a role in the proliferation and maintenance of stem cells in the central nervous system (By similarity). {ECO:0000250}.; DISEASE: Note=Chromosomal aberrations involving MSI2 may contribute to disease progression in chronic myeloid leukemia. Translocation t(7;17)(p15;q23) with HOXA9; translocation t(7;17)(q32-34;q23). {ECO:0000269|PubMed:12649177}.; TISSUE SPECIFICITY: Ubiquitous; detected at low levels. {ECO:0000269|PubMed:12649177}.; ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;larynx;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;blood;breast;lung;placenta;visual apparatus;head and neck;kidney;stomach;thymus;peripheral nerve; . 0.22637 0.09832 0.12689526 63.00424628 34.77251 1.05981 MSK9 . . . antigen identified by monoclonal antibody K15 . . . . . . . . . . . MSK10 . . . antigen identified by monoclonal antibody AJ425 . . . . . . . . . . . MSK32 . . . antigen identified by monoclonal antibody K66 . . . . . . . . . . . MSK38 . . . antigen identified by monoclonal antibody O5 . . . . . . . . . . . MSL1 0.984496890643832 0.0154945441810883 8.56517507985571e-06 male-specific lethal 1 homolog (Drosophila) FUNCTION: Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-16' (H4K16ac) which is implicated in the formation of higher-order chromatin structure. Greatly enhances MSL2 E3 ubiquitin ligase activity, promoting monoubiquitination of histone H2B at 'Lys-34' (H2BK34Ub). This modification in turn stimulates histone H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1. In the MSL complex, acts as a scaffold to tether MSL3 and KAT8 together for enzymatic activity regulation. {ECO:0000269|PubMed:16227571, ECO:0000269|PubMed:21726816, ECO:0000269|PubMed:22547026}.; . . myocardium;smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; . . 0.11809 -0.05129383 49.75819769 15.73772 0.56099 MSL2 0.889663741822694 0.110098385504215 0.00023787267309062 male-specific lethal 2 homolog (Drosophila) FUNCTION: Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure. Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histine H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1. {ECO:0000269|PubMed:21726816}.; . . myocardium;ovary;colon;parathyroid;skin;retina;prostate;cochlea;larynx;thyroid;testis;germinal center;bladder;pineal gland;brain;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;breast;lung;nasopharynx;placenta;head and neck;kidney;stomach; testis - interstitial;atrioventricular node;thymus; 0.97168 0.11809 -0.534490515 20.70063694 33.66822 1.03860 MSL3 0.945646874379395 0.0543141482304778 3.89773901272031e-05 male-specific lethal 3 homolog (Drosophila) FUNCTION: May be involved in chromatin remodeling and transcriptional regulation. May have a role in X inactivation. Component of the MSL complex which is responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure. Specifically recognizes histone H4 monomethylated at 'Lys-20' (H4K20Me1) in a DNA-dependent manner and is proposed to be involved in chromosomal targeting of the MSL complex. {ECO:0000269|PubMed:16227571, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:20657587, ECO:0000269|PubMed:20943666, ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:22547026}.; . TISSUE SPECIFICITY: Expressed in many tissues including liver, pancreas, heart, lung, kidney, skeletal muscle, brain, and placenta, with highest expression in skeletal muscle and heart.; medulla oblongata;ovary;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;ganglion;endometrium;bone;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;pia mater;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.24055 0.09764 -0.22584292 37.32012267 17.48541 0.61336 MSL3P1 . . . male-specific lethal 3 homolog (Drosophila) pseudogene 1 FUNCTION: May be involved in chromatin remodeling and transcriptional regulation. {ECO:0000250}.; . . . . . . . . . . MSLN 2.47687992428564e-15 0.00852087563207934 0.991479124367918 mesothelin FUNCTION: Membrane-anchored forms may play a role in cellular adhesion.; DISEASE: Note=Antibodies against MSLN are detected in patients with mesothelioma and ovarian cancer. {ECO:0000269|PubMed:15897581}.; TISSUE SPECIFICITY: Expressed in lung. Expressed at low levels in heart, placenta and kidney. Expressed in mesothelial cells. Highly expressed in mesotheliomas, ovarian cancers, and some squamous cell carcinomas (at protein level). {ECO:0000269|PubMed:16857795, ECO:0000269|PubMed:7665620}.; . . 0.05939 0.20004 0.727438058 85.98726115 736.52579 5.38738 MSLNL 3.46249568874859e-16 0.00515536660041712 0.994844633399583 mesothelin-like FUNCTION: May play a role in cellular adhesion. {ECO:0000250}.; . . . . . 0.08816 . . 8423.58489 19.79571 MSMB 0.0987031872923106 0.771528727271376 0.129768085436313 microseminoprotein, beta- . . TISSUE SPECIFICITY: Strongly expressed in prostate, liver, kidney, breast and penis. Also expressed in pancreas, esophagus, stomach, deodenum, colon, trachea, lung, salivary glands and fallopian tube. PSP94 is expressed in lung and breast, whereas PSP57 is found in kidney and bladder. {ECO:0000269|PubMed:7566962, ECO:0000269|PubMed:7671139}.; unclassifiable (Anatomical System);prostate;lung;nasopharynx;liver;testis;blood;skeletal muscle;stomach; superior cervical ganglion;prostate;trachea;ciliary ganglion;trigeminal ganglion;skin; 0.02289 0.13116 0.013025609 54.62962963 4.1653 0.15230 MSMO1 0.137137230699618 0.842568820887668 0.0202939484127138 methylsterol monooxygenase 1 FUNCTION: Catalyzes the first step in the removal of the two C-4 methyl groups of 4,4-dimethylzymosterol. {ECO:0000250|UniProtKB:P53045}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;blood;lens;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;colon;parathyroid;choroid;fovea centralis;whole body;larynx;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);small intestine;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;fetal liver;adipose tissue;lung;adrenal gland;spinal cord;prefrontal cortex;adrenal cortex; 0.56568 0.18718 0.703746784 85.42108988 165.73002 2.81661 MSMP 0.443121280696342 0.527477303764641 0.029401415539017 microseminoprotein, prostate associated . . TISSUE SPECIFICITY: Detected in prostate epithelium (at protein level). Detected in trachea and testis. Highly expressed in the human prostate cancer cell line PC-3. {ECO:0000269|PubMed:17338636}.; . . . . 0.369407109 74.95281906 334.71536 3.88832 MSN 0.993557145802077 0.00644185749776522 9.96700157425185e-07 moesin FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. May inhibit herpes simplex virus 1 infection at an early stage. {ECO:0000269|PubMed:21549406}.; . TISSUE SPECIFICITY: In all tissues and cultured cells studied.; ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);tongue;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;amnion;liver;spleen;head and neck;kidney;mammary gland;stomach; lung;ciliary ganglion;white blood cells;fetal lung;kidney;whole blood;bone marrow; 0.86283 0.45280 -0.229483771 36.86010852 9.07879 0.33190 MSNP1 . . . moesin pseudogene 1 . . . . . . . . . . . MSR1 8.20826841073278e-16 0.00231197938905193 0.997688020610947 macrophage scavenger receptor 1 FUNCTION: Membrane glycoproteins implicated in the pathologic deposition of cholesterol in arterial walls during atherogenesis. Two types of receptor subunits exist. These receptors mediate the endocytosis of a diverse group of macromolecules, including modified low density lipoproteins (LDL). Isoform III does not internalize acetylated LDL.; DISEASE: Barrett esophagus (BE) [MIM:614266]: A condition characterized by a metaplastic change in which normal esophageal squamous epithelium is replaced by a columnar and intestinal-type epithelium. Patients with Barrett esophagus have an increased risk of esophageal adenocarcinoma. The main cause of Barrett esophagus is gastroesophageal reflux. The retrograde movement of acid and bile salts from the stomach into the esophagus causes prolonged injury to the esophageal epithelium and induces chronic esophagitis, which in turn is believed to trigger the pathologic changes. {ECO:0000269|PubMed:21791690}. Note=The disease may be caused by mutations affecting the gene represented in this entry. Genetic variants in MSR1 have been found in individuals with Barrett esophagus and are thought to contribute to disease susceptibility.; TISSUE SPECIFICITY: Isoform I, isoform II and isoform III are expressed in monocyte-derived macrophages. {ECO:0000269|PubMed:9548586}.; lymphoreticular;lung;heart;placenta;liver;alveolus;testis;colon;kidney;aorta; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.58615 0.09635 0.001895464 54.03397028 2782.0455 9.96638 MSRA 1.69976100303061e-06 0.244066994155208 0.755931306083789 methionine sulfoxide reductase A FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.; . TISSUE SPECIFICITY: Ubiquitous. Highest expression in adult kidney and cerebellum, followed by liver, heart ventricles, bone marrow and hippocampus.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;blood;lens;lung;placenta;macula lutea;hypopharynx;head and neck;kidney; superior cervical ganglion;cerebellum peduncles;liver;globus pallidus;kidney;cingulate cortex;skeletal muscle;parietal lobe;cerebellum;bone marrow; 0.09000 0.33654 -0.957024976 9.088228356 55.03667 1.48622 MSRB1 0.00310471105797646 0.593792964662346 0.403102324279677 methionine sulfoxide reductase B1 FUNCTION: Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post- translational modification that takes place on specific residue. Acts as a regulator of actin assembly by reducing methionine (R)- sulfoxide mediated by MICALs (MICAL1, MICAL2 or MICAL3) on actin, thereby promoting filament repolymerization. Plays a role in innate immunity by reducing oxidized actin, leading to actin repolymerization in macrophages (By similarity). {ECO:0000250}.; . . . . 0.08905 . 0.058937498 58.26256192 741.27623 5.40508 MSRB1P1 . . . methionine sulfoxide reductase B1 pseudogene 1 . . . . . . . . . . . MSRB2 0.00424761100040581 0.661459160899397 0.334293228100198 methionine sulfoxide reductase B2 FUNCTION: Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post- translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance. {ECO:0000269|PubMed:18424444}.; . TISSUE SPECIFICITY: Ubiquitous. Detected in retina, ocular ciliary body, skeletal muscle, heart, colon, bone marrow, cerebellum, small intestine, fetal brain, fetal liver, kidney, spinal cord, lung, placenta and prostate. {ECO:0000269|PubMed:10375640, ECO:0000269|PubMed:15914630}.; . . 0.18804 0.16681 0.659651797 84.35362114 323.78261 3.82464 MSRB3 0.00702679578516966 0.763111797741439 0.229861406473391 methionine sulfoxide reductase B3 FUNCTION: Catalyzes the reduction of free and protein-bound methionine sulfoxide to methionine. Isoform 2 is essential for hearing. {ECO:0000269|PubMed:14699060, ECO:0000269|PubMed:21185009}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15914630, ECO:0000269|PubMed:21185009}.; colon;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;amniotic fluid;brain;gall bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach;aorta;peripheral nerve;thymus; dorsal root ganglion;ciliary ganglion;trigeminal ganglion; 0.17382 0.12021 -0.449946534 24.00330267 32.68876 1.01610 MSS51 4.16498200099113e-05 0.843183940224811 0.156774409955179 MSS51 mitochondrial translational activator . . . . . 0.19839 . 0.468503535 78.79806558 914.17442 5.87947 MST1 1.72735679966035e-10 0.818517714613279 0.181482285213985 macrophage stimulating 1 . DISEASE: Note=MST1 variant Cys-689 may be associated with inflammatory bowel disease (IBD), a chronic, relapsing inflammation of the gastrointestinal tract with a complex etiology. It is unsure whether Cys-689 itself or a variation in linkage disequilibrium with Cys-689 is responsible for the association with IBD. {ECO:0000269|PubMed:19079170, ECO:0000269|PubMed:20228799}.; . . . . 0.10249 -0.418800956 25.79028073 1665.2271 7.53379 MST1L . . . macrophage stimulating 1-like . . . . . . . . . . . MST1P2 . . . macrophage stimulating 1 (hepatocyte growth factor-like) pseudogene 2 . . . . . . . . . . . MST1R 1.6934911102813e-20 0.0200568760985158 0.979943123901484 macrophage stimulating 1 receptor FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to MST1 ligand. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces autophosphorylation of RON on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1 or the adapter GAB1. Recruitment of these downstream effectors by RON leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. RON signaling activates the wound healing response by promoting epithelial cell migration, proliferation as well as survival at the wound site. Plays also a role in the innate immune response by regulating the migration and phagocytic activity of macrophages. Alternatively, RON can also promote signals such as cell migration and proliferation in response to growth factors other than MST1 ligand. {ECO:0000269|PubMed:18836480, ECO:0000269|PubMed:7939629, ECO:0000269|PubMed:9764835}.; . TISSUE SPECIFICITY: Expressed in colon, skin, lung and bone marrow. {ECO:0000269|PubMed:8062829}.; unclassifiable (Anatomical System);breast;uterus;prostate;pancreas;lung;gum;testis;colon;cervix;skeletal muscle;stomach; superior cervical ganglion; 0.32649 0.15357 -1.77692783 2.288275537 981.386 6.04778 MSTN 0.812914735546533 0.186112611168579 0.0009726532848878 myostatin FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth.; DISEASE: Muscle hypertrophy (MSLHP) [MIM:614160]: A condition characterized by increased muscle bulk and strength. Affected individuals are exceptionally strong. {ECO:0000269|PubMed:15215484}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;whole body;muscle;retina; superior cervical ganglion;trigeminal ganglion; 0.83937 0.74393 0.663285274 84.55414013 913.77022 5.87603 MSTO1 0.0418044849918912 0.952035870763108 0.00615964424500064 misato 1, mitochondrial distribution and morphology regulator FUNCTION: Involved in the regulation of mitochondrial distribution and morphology. {ECO:0000269|PubMed:17349998}.; . TISSUE SPECIFICITY: Present in all cell lines tested (at protein level). Widely expressed. {ECO:0000269|PubMed:17349998}.; ovary;sympathetic chain;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;cerebral cortex;oesophagus;endometrium;larynx;gum;bone;thyroid;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;pharynx;skeletal muscle;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . . . . . 2464.41702 9.24715 MSTO2P . . . misato family member 2, pseudogene . . . . . . . . . . . MSX1 0.275361731184646 0.633641369341214 0.0909968994741406 msh homeobox 1 FUNCTION: Acts as a transcriptional repressor. May play a role in limb-pattern formation. Acts in cranofacial development and specifically in odontogenesis. Expression in the developing nail bed mesenchyme is important for nail plate thickness and integrity. {ECO:0000269|PubMed:11369996, ECO:0000269|PubMed:12807959}.; DISEASE: Tooth agenesis selective 1 (STHAG1) [MIM:106600]: A form of selective tooth agenesis, a common anomaly characterized by the congenital absence of one or more teeth. Selective tooth agenesis without associated systemic disorders has sometimes been divided into 2 types: oligodontia, defined as agenesis of 6 or more permanent teeth, and hypodontia, defined as agenesis of less than 6 teeth. The number in both cases does not include absence of third molars (wisdom teeth). Tooth agenesis selective type 1 can be associated with orofacial cleft in some patients. {ECO:0000269|PubMed:12097313, ECO:0000269|PubMed:8696335}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=MSX1 is deleted in some patients with Wolf- Hirschhorn syndrome (WHS). WHS results from sub-telomeric deletions in the short arm of chromosome 4. {ECO:0000305|PubMed:1969845}.; DISEASE: Ectodermal dysplasia 3, Witkop type (ECTD3) [MIM:189500]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures such as hair, teeth, nails and sweat glands, with or without any additional clinical sign. Each combination of clinical features represents a different type of ectodermal dysplasia. ECTD3 is characterized by abnormalities largely limited largely to teeth (some of which are missing) and nails (which are poorly formed early in life, especially toenails). This condition is distinguished from anhidrotic ectodermal dysplasia by autosomal dominant inheritance and little involvement of hair and sweat glands. The teeth are not as severely affected. {ECO:0000269|PubMed:11369996}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Non-syndromic orofacial cleft 5 (OFC5) [MIM:608874]: A birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum. {ECO:0000269|PubMed:12807959}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the developing nail bed mesenchyme. {ECO:0000269|PubMed:11369996}.; . . 0.83114 0.60631 . . 590.93175 4.92812 MSX2 0.42149241575751 0.544391297516308 0.0341162867261824 msh homeobox 2 FUNCTION: Acts as a transcriptional regulator in bone development. Represses the ALPL promoter activity and antogonizes the stimulatory effect of DLX5 on ALPL expression during osteoblast differentiation. Probable morphogenetic role. May play a role in limb-pattern formation. In osteoblasts, suppresses transcription driven by the osteocalcin FGF response element (OCFRE). Binds to the homeodomain-response element of the ALPL promoter. {ECO:0000269|PubMed:12145306}.; DISEASE: Parietal foramina 1 (PFM1) [MIM:168500]: Autosomal dominant disease characterized by oval defects of the parietal bones caused by deficient ossification around the parietal notch, which is normally obliterated during the fifth fetal month. {ECO:0000269|PubMed:10742103, ECO:0000269|PubMed:10767351}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Parietal foramina with cleidocranial dysplasia (PFMCCD) [MIM:168550]: Combines skull defects in the form of enlarged parietal foramina and deficient ossification of the clavicles. {ECO:0000269|PubMed:14571277}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Craniosynostosis 2 (CRS2) [MIM:604757]: A primary abnormality of skull growth involving premature fusion of one or more cranial sutures. The growth velocity of the skull often cannot match that of the developing brain resulting in an abnormal head shape and, in some cases, increased intracranial pressure, which must be treated promptly to avoid permanent neurodevelopmental disability. CRS2 is characterized by either fronto-orbital recession, or frontal bossing, or turribrachycephaly, or cloverleaf skull. Associated features include severe headache, high incidence of visual problems (myopia or hyperopia), and short first metatarsals. Intelligence is normal. {ECO:0000269|PubMed:23918290, ECO:0000269|PubMed:23949913, ECO:0000269|PubMed:8106171}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;optic nerve;whole body;lung;oesophagus;placenta;macula lutea;liver;testis;spleen;mammary gland;stomach; placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.82018 0.34240 . . 17.20507 0.60467 MSX2P1 . . . msh homeobox 2 pseudogene 1 . . . . . . . . . . . MT-ATP6 . . . mitochondrially encoded ATP synthase 6 FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.; DISEASE: Neuropathy, ataxia, and retinitis pigmentosa (NARP) [MIM:551500]: A syndrome characterized by variable combination of developmental delay, psychomotor retardation, hearing loss, optic atrophy and retinitis pigmentosa, dementia, seizures, ataxia, proximal neurogenic muscle weakness, and sensory neuropathy. {ECO:0000269|PubMed:2137962}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leber hereditary optic neuropathy (LHON) [MIM:535000]: A maternally inherited disease resulting in acute or subacute loss of central vision, due to optic nerve dysfunction. Cardiac conduction defects and neurological defects have also been described in some patients. LHON results from primary mitochondrial DNA mutations affecting the respiratory chain complexes. {ECO:0000269|PubMed:7726182}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. {ECO:0000269|PubMed:17352390, ECO:0000269|PubMed:8395787, ECO:0000269|PubMed:9270604, ECO:0000269|PubMed:9501263, ECO:0000269|PubMed:9556461}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial infantile bilateral striatal necrosis (MIBSN) [MIM:500003]: Bilateral striatal necrosis is a neurological disorder resembling Leigh syndrome. {ECO:0000269|PubMed:7668837}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial complex V deficiency, mitochondrial 1 (MC5DM1) [MIM:516060]: A mitochondrial disorder with heterogeneous clinical manifestations including neuropathy, ataxia, hypertrophic cardiomyopathy. Hypertrophic cardiomyopathy can present with negligible to extreme hypertrophy, minimal to extensive fibrosis and myocyte disarray, absent to severe left ventricular outflow tract obstruction, and distinct septal contours/morphologies with extremely varying clinical course. {ECO:0000269|PubMed:16049925, ECO:0000269|PubMed:18055910}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myopathy, lactic acidosis, and sideroblastic anemia 3 (MLASA3) [MIM:500011]: A rare mitochondrial disorder characterized by sideroblastic anemia, muscle weakness, and exercise intolerance associated with persistent lactic acidemia. Additional MLASA3 features are failure to thrive, hearing loss, epilepsy, stroke- like episodes, and severe developmental delay. {ECO:0000269|PubMed:25037980}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;skin;bone marrow;uterus;subthalamic nucleus;prostate;frontal lobe;thyroid;pituitary gland;testis;dura mater;brain;tonsil;unclassifiable (Anatomical System);meninges;heart;nervous;tongue;hypothalamus;urinary;adrenal cortex;blood;skeletal muscle;breast;pia mater;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;hypopharynx;head and neck;mammary gland;stomach;thymus; . 0.70819 . . . . . MT-ATP8 . . . mitochondrially encoded ATP synthase 8 FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). {ECO:0000250}.; DISEASE: Mitochondrial complex V deficiency, mitochondrial 2 (MC5DM2) [MIM:516070]: A mitochondrial disorder with heterogeneous clinical manifestations including neuropathy, ataxia, hypertrophic cardiomyopathy. Hypertrophic cardiomyopathy can present with negligible to extreme hypertrophy, minimal to extensive fibrosis and myocyte disarray, absent to severe left ventricular outflow tract obstruction, and distinct septal contours/morphologies with extremely varying clinical course. {ECO:0000269|PubMed:19188198}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.15855 . . . . . MT-CO1 . . . mitochondrially encoded cytochrome c oxidase I FUNCTION: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.; DISEASE: Leber hereditary optic neuropathy (LHON) [MIM:535000]: A maternally inherited disease resulting in acute or subacute loss of central vision, due to optic nerve dysfunction. Cardiac conduction defects and neurological defects have also been described in some patients. LHON results from primary mitochondrial DNA mutations affecting the respiratory chain complexes. {ECO:0000269|PubMed:1322638}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=MT-CO1 may play a role in the pathogenesis of acquired idiopathic sideroblastic anemia, a disease characterized by inadequate formation of heme and excessive accumulation of iron in mitochondria. Mitochondrial iron overload may be attributable to mutations of mitochondrial DNA because these can cause respiratory chain dysfunction, thereby impairing reduction of ferric iron to ferrous iron. The reduced form of iron is essential to the last step of mitochondrial heme biosynthesis. {ECO:0000269|PubMed:9389715, ECO:0000269|PubMed:9851701}.; DISEASE: Mitochondrial complex IV deficiency (MT-C4D) [MIM:220110]: A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs. Features include hypertrophic cardiomyopathy, hepatomegaly and liver dysfunction, hypotonia, muscle weakness, exercise intolerance, developmental delay, delayed motor development and mental retardation. Some affected individuals manifest a fatal hypertrophic cardiomyopathy resulting in neonatal death. A subset of patients manifest Leigh syndrome. {ECO:0000269|PubMed:12140182, ECO:0000269|PubMed:16284789}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Recurrent myoglobinuria mitochondrial (RM-MT) [MIM:550500]: Recurrent myoglobinuria is characterized by recurrent attacks of rhabdomyolysis (necrosis or disintegration of skeletal muscle) associated with muscle pain and weakness, and followed by excretion of myoglobin in the urine. {ECO:0000269|PubMed:10980727}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Deafness, sensorineural, mitochondrial (DFNM) [MIM:500008]: A form of non-syndromic deafness with maternal inheritance. Affected individuals manifest progressive, postlingual, sensorineural hearing loss involving high frequencies. {ECO:0000269|PubMed:10577941}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:16407113}. Note=The gene represented in this entry may be involved in disease pathogenesis.; . umbilical cord;colon;parathyroid;skin;bone marrow;uterus;cerebral cortex;thyroid;pituitary gland;dura mater;brain;artery;pineal gland;unclassifiable (Anatomical System);meninges;heart;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pia mater;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;stomach;aorta;thymus; . 0.14951 . . . . . MT-CO2 . . . mitochondrially encoded cytochrome c oxidase II FUNCTION: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1.; DISEASE: Mitochondrial complex IV deficiency (MT-C4D) [MIM:220110]: A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs. Features include hypertrophic cardiomyopathy, hepatomegaly and liver dysfunction, hypotonia, muscle weakness, exercise intolerance, developmental delay, delayed motor development and mental retardation. Some affected individuals manifest a fatal hypertrophic cardiomyopathy resulting in neonatal death. A subset of patients manifest Leigh syndrome. {ECO:0000269|PubMed:10486321}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;umbilical cord;colon;skin;bone marrow;uterus;prostate;frontal lobe;thyroid;pituitary gland;dura mater;brain;artery;tonsil;unclassifiable (Anatomical System);meninges;trophoblast;heart;nervous;tongue;hypothalamus;adrenal cortex;blood;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;liver;head and neck;kidney;stomach;aorta; . 0.12842 . . . . . MT-CO3 . . . mitochondrially encoded cytochrome c oxidase III FUNCTION: Subunits I, II and III form the functional core of the enzyme complex.; DISEASE: Leber hereditary optic neuropathy (LHON) [MIM:535000]: A maternally inherited disease resulting in acute or subacute loss of central vision, due to optic nerve dysfunction. Cardiac conduction defects and neurological defects have also been described in some patients. LHON results from primary mitochondrial DNA mutations affecting the respiratory chain complexes. {ECO:0000269|PubMed:8240356}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial complex IV deficiency (MT-C4D) [MIM:220110]: A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs. Features include hypertrophic cardiomyopathy, hepatomegaly and liver dysfunction, hypotonia, muscle weakness, exercise intolerance, developmental delay, delayed motor development and mental retardation. Some affected individuals manifest a fatal hypertrophic cardiomyopathy resulting in neonatal death. A subset of patients manifest Leigh syndrome. {ECO:0000269|PubMed:8630495}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Recurrent myoglobinuria mitochondrial (RM-MT) [MIM:550500]: Recurrent myoglobinuria is characterized by recurrent attacks of rhabdomyolysis (necrosis or disintegration of skeletal muscle) associated with muscle pain and weakness, and followed by excretion of myoglobin in the urine. {ECO:0000269|PubMed:8630495}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Mitochondrial encephalomyopathy with lactic acidosis and stroke-like episodes syndrome (MELAS) [MIM:540000]: Genetically heterogeneous disorder, characterized by episodic vomiting, seizures, and recurrent cerebral insults resembling strokes and causing hemiparesis, hemianopsia, or cortical blindness. {ECO:0000269|PubMed:18587274, ECO:0000269|PubMed:7496173}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;subthalamic nucleus;frontal lobe;endometrium;thyroid;amniotic fluid;brain;heart;tongue;adrenal cortex;blood;skeletal muscle;breast;liver;alveolus;spleen;mammary gland;colon;parathyroid;vein;uterus;cerebral cortex;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;trophoblast;lymph node;islets of Langerhans;hypothalamus;lung;pia mater;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; . 0.23031 . . . . . MT-CYB . . . mitochondrially encoded cytochrome b FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. {ECO:0000250}.; DISEASE: Note=Defects in MT-CYB are a rare cause of mitochondrial dysfunction underlying different myopathies. They include mitochondrial encephalomyopathy, hypertrophic cardiomyopathy (HCM), and sporadic mitochondrial myopathy (MM). In mitochondrial myopathy, exercise intolerance is the predominant symptom. Additional features include lactic acidosis, muscle weakness and/or myoglobinuria. Defects in MTCYB are also found in cases of exercise intolerance accompanied by deafness, mental retardation, retinitis pigmentosa, cataract, growth retardation, epilepsy (multisystem disorder). {ECO:0000269|PubMed:11047755, ECO:0000269|PubMed:11601507}.; DISEASE: Cardiomyopathy, infantile histiocytoid (CMIH) [MIM:500000]: A heart disease characterized by the presence of pale granular foamy histiocyte-like cells within the myocardium. It usually affects children younger than 2 years of age, with a clear predominance of females over males. Infants present with dysrhythmia or cardiac arrest. The clinical course is usually fulminant, sometimes simulating sudden infant death syndrome. {ECO:0000269|PubMed:10960495}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leber hereditary optic neuropathy (LHON) [MIM:535000]: A maternally inherited disease resulting in acute or subacute loss of central vision, due to optic nerve dysfunction. Cardiac conduction defects and neurological defects have also been described in some patients. LHON results from primary mitochondrial DNA mutations affecting the respiratory chain complexes. {ECO:0000269|PubMed:1732158}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry.; . smooth muscle;ovary;umbilical cord;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;frontal lobe;cerebral cortex;thyroid;pituitary gland;amniotic fluid;dura mater;brain;artery;pineal gland;unclassifiable (Anatomical System);meninges;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pia mater;lung;adrenal gland;placenta;liver;head and neck;stomach;aorta;thymus; . 0.09075 . . . . . MT-LIPCAR . . . mitochondrially encoded long non-coding cardiac associated RNA . . . . . . . . . . . MT-ND1 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.; DISEASE: Leber hereditary optic neuropathy (LHON) [MIM:535000]: A maternally inherited disease resulting in acute or subacute loss of central vision, due to optic nerve dysfunction. Cardiac conduction defects and neurological defects have also been described in some patients. LHON results from primary mitochondrial DNA mutations affecting the respiratory chain complexes. {ECO:0000269|PubMed:1417830, ECO:0000269|PubMed:1674640, ECO:0000269|PubMed:1900003, ECO:0000269|PubMed:1928099, ECO:0000269|PubMed:2018041}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial encephalomyopathy with lactic acidosis and stroke-like episodes syndrome (MELAS) [MIM:540000]: Genetically heterogeneous disorder, characterized by episodic vomiting, seizures, and recurrent cerebral insults resembling strokes and causing hemiparesis, hemianopsia, or cortical blindness. {ECO:0000269|PubMed:8723687}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Alzheimer disease mitochondrial (AD-MT) [MIM:502500]: Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. {ECO:0000269|PubMed:8104867}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:15265369, ECO:0000269|PubMed:7733935}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:24105702}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;smooth muscle;ovary;colon;skin;bone marrow;uterus;subthalamic nucleus;prostate;frontal lobe;cerebral cortex;larynx;thyroid;pituitary gland;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;lymph node;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pia mater;lung;hypopharynx;liver;head and neck;cervix;mammary gland;stomach; . 0.17585 . . . . . MT-ND2 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.; DISEASE: Leber hereditary optic neuropathy (LHON) [MIM:535000]: A maternally inherited disease resulting in acute or subacute loss of central vision, due to optic nerve dysfunction. Cardiac conduction defects and neurological defects have also been described in some patients. LHON results from primary mitochondrial DNA mutations affecting the respiratory chain complexes. {ECO:0000269|PubMed:1732158, ECO:0000269|PubMed:1900003}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Alzheimer disease mitochondrial (AD-MT) [MIM:502500]: Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. {ECO:0000269|PubMed:1370613}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;thyroid;pituitary gland;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;liver;head and neck;stomach; . 0.13682 . . . . . MT-ND3 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. {ECO:0000269|PubMed:17152068}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:11456298, ECO:0000269|PubMed:14705112, ECO:0000269|PubMed:20818383}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;umbilical cord;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;cerebral cortex;bone;thyroid;pituitary gland;testis;brain;pineal gland;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;hypopharynx;alveolus;liver;head and neck;kidney;mammary gland;stomach;aorta; . 0.13003 . . . . . MT-ND4 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.; DISEASE: Leber hereditary optic neuropathy (LHON) [MIM:535000]: A maternally inherited disease resulting in acute or subacute loss of central vision, due to optic nerve dysfunction. Cardiac conduction defects and neurological defects have also been described in some patients. LHON results from primary mitochondrial DNA mutations affecting the respiratory chain complexes. {ECO:0000269|PubMed:1959931, ECO:0000269|PubMed:3201231, ECO:0000269|PubMed:9452107}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leber hereditary optic neuropathy with dystonia (LDYT) [MIM:500001]: Part of a spectrum of Leber hereditary optic neuropathy. It is characterized by the association of optic atrophy and central vision loss with dystonia. {ECO:0000269|PubMed:8644732}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial encephalomyopathy with lactic acidosis and stroke-like episodes syndrome (MELAS) [MIM:540000]: Genetically heterogeneous disorder, characterized by episodic vomiting, seizures, and recurrent cerebral insults resembling strokes and causing hemiparesis, hemianopsia, or cortical blindness. {ECO:0000269|PubMed:1323207}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;bone marrow;prostate;frontal lobe;cerebral cortex;larynx;bone;thyroid;pituitary gland;testis;dura mater;brain;artery;bladder;pineal gland;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;breast;pia mater;lung;adrenal gland;hypopharynx;alveolus;liver;head and neck;kidney;stomach;aorta;thymus; . 0.12900 . . . . . MT-ND4L . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.; DISEASE: Leber hereditary optic neuropathy (LHON) [MIM:535000]: A maternally inherited disease resulting in acute or subacute loss of central vision, due to optic nerve dysfunction. Cardiac conduction defects and neurological defects have also been described in some patients. LHON results from primary mitochondrial DNA mutations affecting the respiratory chain complexes. {ECO:0000269|PubMed:8680405}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;bone marrow;prostate;cerebral cortex;larynx;thyroid;pituitary gland;testis;dura mater;brain;artery;bladder;pineal gland;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;breast;pia mater;lung;adrenal gland;nasopharynx;visual apparatus;hippocampus;hypopharynx;liver;head and neck;kidney;stomach;aorta;thymus; . 0.13922 . . . . . MT-ND5 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.; DISEASE: Leber hereditary optic neuropathy (LHON) [MIM:535000]: A maternally inherited disease resulting in acute or subacute loss of central vision, due to optic nerve dysfunction. Cardiac conduction defects and neurological defects have also been described in some patients. LHON results from primary mitochondrial DNA mutations affecting the respiratory chain complexes. {ECO:0000269|PubMed:16240359, ECO:0000269|PubMed:1732158, ECO:0000269|PubMed:1900003, ECO:0000269|PubMed:8213825}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. {ECO:0000269|PubMed:11938446, ECO:0000269|PubMed:12796552, ECO:0000269|PubMed:17400793}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:20818383}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial encephalomyopathy with lactic acidosis and stroke-like episodes syndrome (MELAS) [MIM:540000]: Genetically heterogeneous disorder, characterized by episodic vomiting, seizures, and recurrent cerebral insults resembling strokes and causing hemiparesis, hemianopsia, or cortical blindness. {ECO:0000269|PubMed:12509858, ECO:0000269|PubMed:15767514, ECO:0000269|PubMed:17400793, ECO:0000269|PubMed:9299505}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;smooth muscle;ovary;umbilical cord;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;amygdala;heart;tongue;nervous;blood;skeletal muscle;breast;liver;spleen;mammary gland;colon;parathyroid;uterus;whole body;cerebral cortex;larynx;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;lung;pia mater;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;adrenal gland;liver;prefrontal cortex;globus pallidus;kidney;parietal lobe;cingulate cortex;cerebellum; . . . . . . MT-ND6 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.; DISEASE: Leber hereditary optic neuropathy (LHON) [MIM:535000]: A maternally inherited disease resulting in acute or subacute loss of central vision, due to optic nerve dysfunction. Cardiac conduction defects and neurological defects have also been described in some patients. LHON results from primary mitochondrial DNA mutations affecting the respiratory chain complexes. {ECO:0000269|PubMed:10447650, ECO:0000269|PubMed:11133798, ECO:0000269|PubMed:1417830, ECO:0000269|PubMed:8854108, ECO:0000269|PubMed:9452107}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leber hereditary optic neuropathy with dystonia (LDYT) [MIM:500001]: Part of a spectrum of Leber hereditary optic neuropathy. It is characterized by the association of optic atrophy and central vision loss with dystonia. {ECO:0000269|PubMed:8016139, ECO:0000269|PubMed:8644732}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial encephalomyopathy with lactic acidosis and stroke-like episodes syndrome (MELAS) [MIM:540000]: Genetically heterogeneous disorder, characterized by episodic vomiting, seizures, and recurrent cerebral insults resembling strokes and causing hemiparesis, hemianopsia, or cortical blindness. {ECO:0000269|PubMed:11781695}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:14595656, ECO:0000269|PubMed:20818383}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;smooth muscle;ovary;colon;choroid;bone marrow;uterus;prostate;frontal lobe;cerebral cortex;larynx;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;nervous;tongue;islets of Langerhans;hypothalamus;breast;lung;placenta;liver;hypopharynx;head and neck;kidney;mammary gland;stomach; . 0.13612 . . . . . MT-RNR1 . . . mitochondrially encoded 12S RNA . . . . . . . . . . . MT-RNR2 . . . mitochondrially encoded 16S RNA FUNCTION: Plays a role as a neuroprotective factor. Protects against death induced by multiple different familial Alzheimer disease genes and beta amyloid proteins in Alzheimer disease. Suppresses apoptosis by binding to BAX and preventing the translocation of BAX from the cytosol to mitochondria. Binds to IGFBP3 and specifically blocks IGFBP3-induced cell death Induces chemotaxis of mononuclear phagocytes via FPR2. Reduces the aggregation and fibrillary formation by suppressing the effect of APP on mononuclear phagocytes and acts by competitively inhibiting the access of FPRL1 to APP. {ECO:0000269|PubMed:11371646, ECO:0000269|PubMed:11717357, ECO:0000269|PubMed:12732850, ECO:0000269|PubMed:14561895, ECO:0000269|PubMed:15153530}.; . TISSUE SPECIFICITY: Expressed in the heart, skeletal muscles, kidney and liver. Lesser but significant expression is observed in the brain and the gastrointestinal tract. Expressed in the AD brain, where it is found in some of the large intact neurons of the occipital lobes and small and round reactive glial cells in the hippocampus. {ECO:0000269|PubMed:11371646, ECO:0000269|PubMed:12009529, ECO:0000269|PubMed:19477263}.; . . . . . . . . MT-TA . . . mitochondrially encoded tRNA alanine . . . . . . . . . . . MT-TC . . . mitochondrially encoded tRNA cysteine . . . . . . . . . . . MT-TD . . . mitochondrially encoded tRNA aspartic acid . . . . . . . . . . . MT-TE . . . mitochondrially encoded tRNA glutamic acid . . . . . . . . . . . MT-TF . . . mitochondrially encoded tRNA phenylalanine . . . . . . . . . . . MT-TG . . . mitochondrially encoded tRNA glycine . . . . . . . . . . . MT-TH . . . mitochondrially encoded tRNA histidine . . . . . . . . . . . MT-TI . . . mitochondrially encoded tRNA isoleucine . . . . . . . . . . . MT-TK . . . mitochondrially encoded tRNA lysine . . . . . . . . . . . MT-TL1 . . . mitochondrially encoded tRNA leucine 1 (UUA/G) . . . . . . . . . . . MT-TL2 . . . mitochondrially encoded tRNA leucine 2 (CUN) . . . . . . . . . . . MT-TM . . . mitochondrially encoded tRNA methionine . . . . . . . . . . . MT-TN . . . mitochondrially encoded tRNA asparagine . . . . . . . . . . . MT-TP . . . mitochondrially encoded tRNA proline FUNCTION: Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces (PubMed:23475612, PubMed:8939939, PubMed:26224785, PubMed:25108285, PubMed:22236406). Required for the secretion of plasma lipoproteins that contain apolipoprotein B (PubMed:23475612, PubMed:8939939, PubMed:26224785). {ECO:0000269|PubMed:22236406, ECO:0000269|PubMed:23475612, ECO:0000269|PubMed:25108285, ECO:0000269|PubMed:26224785, ECO:0000269|PubMed:8939939}.; DISEASE: Abetalipoproteinemia (ABL) [MIM:200100]: An autosomal recessive disorder of lipoprotein metabolism. Affected individuals produce virtually no circulating apolipoprotein B-containing lipoproteins (chylomicrons, VLDL, LDL, lipoprotein(A)). Malabsorption of the antioxidant vitamin E occurs, leading to spinocerebellar and retinal degeneration. {ECO:0000269|PubMed:10679949, ECO:0000269|PubMed:10946006, ECO:0000269|PubMed:22236406, ECO:0000269|PubMed:23475612, ECO:0000269|PubMed:25108285, ECO:0000269|PubMed:26224785, ECO:0000269|PubMed:8939939}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver and small intestine. Also found in ovary, testis and kidney. {ECO:0000269|PubMed:7961826}.; . . 0.36424 0.44963 1.42749112 94.99292286 . . MT-TQ . . . mitochondrially encoded tRNA glutamine . . . . . . . . . . . MT-TR . . . mitochondrially encoded tRNA arginine . . . . . . . . . . . MT-TS1 . . . mitochondrially encoded tRNA serine 1 (UCN) . . . . . . . . . . . MT-TS2 . . . mitochondrially encoded tRNA serine 2 (AGU/C) . . . . . . . . . . . MT-TT . . . mitochondrially encoded tRNA threonine . . . . . . . . . . . MT-TV . . . mitochondrially encoded tRNA valine . . . . . . . . . . . MT-TW . . . mitochondrially encoded tRNA tryptophan . . . . . . . . . . . MT-TY . . . mitochondrially encoded tRNA tyrosine . . . . . . . . . . . MT1A 0.0077761859390121 0.549963564027749 0.442260250033239 metallothionein 1A FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.; . . optic nerve;macula lutea;blood;fovea centralis;choroid;lens;retina; . 0.10097 . 0.567831482 81.78225997 3587.00557 11.59065 MT1B 0.248269442186515 0.642508257407468 0.109222300406017 metallothionein 1B FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.; . . unclassifiable (Anatomical System);liver;spleen; . 0.06450 0.16997 0.413500896 76.67492333 133.70913 2.51316 MT1CP . . . metallothionein 1C, pseudogene . . . . . . . . . . . MT1DP . . . metallothionein 1D, pseudogene FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals. {ECO:0000250}.; . . . . . . . . . . MT1E 0.659212996447356 0.317019350693266 0.0237676528593777 metallothionein 1E FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;synovium;bone;thyroid;pituitary gland;testis;brain;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;heart;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; fetal liver;lung;adrenal gland;liver;kidney;fetal thyroid;skeletal muscle; . 0.15601 0.435547893 77.45340882 47.81219 1.34291 MT1F 0.0538496988016702 0.700952045446527 0.245198255751803 metallothionein 1F FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.; . . unclassifiable (Anatomical System);lung;iris;liver;skin; fetal liver;superior cervical ganglion;lung;thyroid;adrenal cortex;liver;fetal lung;kidney;fetal thyroid;skeletal muscle; 0.24058 0.14928 0.613741468 83.06794055 97.05152 2.12868 MT1G 0.00811948407601034 0.559134110463901 0.432746405460089 metallothionein 1G FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.; . . . . 0.12315 . 0.057118534 57.99716914 20.37147 0.69519 MT1H 0.0548412149416522 0.703870717471748 0.2412880675866 metallothionein 1H FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.; . . unclassifiable (Anatomical System);pancreas;epididymis;visual apparatus;liver;spleen;lens;skin;retina; fetal liver;pancreas;lung;thyroid;liver;adrenal cortex;fetal lung;kidney;fetal thyroid;skeletal muscle; 0.68743 . 1.124481678 92.1207832 377.95581 4.09826 MT1HL1 0.0200621262324532 0.511088561995091 0.468849311772455 metallothionein 1H-like 1 FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. {ECO:0000250}.; . . . . . . . . 93.79969 2.08288 MT1IP . . . metallothionein 1I, pseudogene . . . . . . . . . . . MT1JP . . . metallothionein 1J, pseudogene . . . . . . 0.15601 . . . . MT1L . . . metallothionein 1L (gene/pseudogene) FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in reticulocytes.; . . . 0.15601 . . . . MT1M 9.83543934507332e-05 0.198305665625703 0.801595979980846 metallothionein 1M FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.; . . . . 0.00348 0.03565 0.347360312 73.97381458 40.34675 1.18459 MT1P1 . . . metallothionein 1 pseudogene 1 . . . . . . . . . . . MT1P3 . . . metallothionein 1 pseudogene 3 . . . . . . 0.15601 . . . . MT1X 0.0496111915968201 0.687384967227537 0.263003841175643 metallothionein 1X FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.; . . . . 0.11711 . 0.235309407 68.71903751 25.15059 0.82239 MT1XP1 . . . metallothionein 1X pseudogene 1 . . . . . . . . . . . MT2A 0.0538691874978182 0.701010300605284 0.245120511896898 metallothionein 2A FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.; . . myocardium;lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;amniotic fluid;bladder;brain;gall bladder;heart;cartilage;tongue;pineal body;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;bone;testis;artery;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;head and neck;kidney;stomach;aorta; fetal liver;adipose tissue;lung;adrenal gland;liver;adrenal cortex;fetal lung;atrioventricular node;kidney;skeletal muscle; 0.08702 0.26701 0.12325821 62.38499646 8.73698 0.32185 MT2P1 . . . metallothionein 2 pseudogene 1 . . . . . . . . . . . MT3 0.254133469605707 0.640891028149311 0.104975502244982 metallothionein 3 FUNCTION: Binds heavy metals. Contains three zinc and three copper atoms per polypeptide chain and only a negligible amount of cadmium. Inhibits survival and neurite formation of cortical neurons in vitro.; . TISSUE SPECIFICITY: Abundant in a subset of astrocytes in the normal human brain, but greatly reduced in the Alzheimer disease (AD) brain.; unclassifiable (Anatomical System);hypothalamus;spinal cord;adrenal cortex;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;frontal lobe;adrenal gland;macula lutea;hippocampus;testis;brain;cerebellum; . 0.14047 0.25971 0.323496558 72.93583392 12.54736 0.45713 MT4 0.0079945846958122 0.555840621875314 0.436164793428874 metallothionein 4 FUNCTION: Seems to bind zinc and copper. Could play a special role in regulating zinc metabolism during the differentiation of stratified epithelia.; . . . . 0.27119 0.25263 0.657836546 84.27105449 493.8284 4.56904 MT7SDNA . . . mitochondrially encoded 7S DNA . . . . . . . . . . . MTA1 0.999747857218867 0.00025214270654208 7.45903969799387e-11 metastasis associated 1 FUNCTION: Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator. As a part of the histone-deacetylase multiprotein complex (NuRD), regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA. In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3, PAX5 and SUMO2, independent of the NuRD complex. Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3. Plays a role in the inflammatory responses, both as a target and as a component of the NF-kappa-B signaling and regulates a subset of proinflammatory cytokines such as IL1B, MIP2, and TNF. Regulates p53-dependent and -independent DNA repair processes following genotoxic stress. Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair. Plays an important role in tumorigenesis, tumor invasion, and metastasis. Involved in the epigenetic regulation of ESR1 expression in breast cancer in a TFAP2C, IFI16 and HDAC4/5/6-dependent manner. Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light-dark (LD) cycles. Positively regulates the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1. Regulates deacetylation of ARNTL/BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1- mediated transcription repression. Isoform Short binds to ESR1 and sequesters it in the cytoplasm and enhances its non-genomic responses. {ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:17671180, ECO:0000269|PubMed:17922032, ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24413532}.; . TISSUE SPECIFICITY: Widely expressed. High expression in brain, liver, kidney, and cardiac muscle, ovaries, adrenal glands and virgin mammary glands. Higher in tumors than in adjacent normal tissue from the same individual. Up-regulated in a wide variety of cancers including breast, liver, ovarian, and colorectal cancer and its expression levels are closely correlated with tumor aggressiveness and metastasis. {ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:24970816}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;tumor;trigeminal ganglion;skeletal muscle; 0.88976 0.22648 -1.061810361 7.519462137 2414.87209 9.12745 MTA2 0.978013018375655 0.0219869476278507 3.39964940866736e-08 metastasis associated 1 family member 2 FUNCTION: May be involved in the regulation of gene expression as repressor and activator. The repression might be related to covalent modification of histone proteins.; . TISSUE SPECIFICITY: Widely expressed.; colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;hippocampus;liver;amnion;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;uterus corpus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.89596 0.27826 -1.023168368 7.944090587 17.92383 0.62693 MTA3 0.855163471897877 0.144816430532587 2.00975695366521e-05 metastasis associated 1 family member 3 FUNCTION: Plays a role in maintenance of the normal epithelial architecture through the repression of SNAI1 transcription in a histone deacetylase-dependent manner, and thus the regulation of E-cadherin levels. Contributes to transcriptional repression by BCL6. {ECO:0000269|PubMed:12705869, ECO:0000269|PubMed:15454082}.; . TISSUE SPECIFICITY: Expressed in germinal centers of lymphoid tissues. No expression in nonepithelial cells. {ECO:0000269|PubMed:12705869}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.83041 0.14229 -0.602450568 17.91106393 51.94859 1.42352 MTAP 0.000179316285483304 0.700327060491942 0.299493623222575 methylthioadenosine phosphorylase FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S- adenosylmethionine. Has broad substrate specificity with 6- aminopurine nucleosides as preferred substrates. {ECO:0000255|HAMAP-Rule:MF_03155, ECO:0000269|PubMed:3091600}.; DISEASE: Note=Loss of MTAP activity may play a role in human cancer. MTAP loss has been reported in a number of cancers, including osteosarcoma, malignant melanoma and gastric cancer.; TISSUE SPECIFICITY: Ubiquitously expressed.; . . 0.17705 0.35026 -0.381986487 27.68931352 3870.61383 12.26118 MTAPP1 . . . methylthioadenosine phosphorylase pseudogene 1 . . . . . . . . . . . MTAPP2 . . . methylthioadenosine phosphorylase pseudogene 2 . . . . . . . . . . . MTATP6P1 . . . mitochondrially encoded ATP synthase 6 pseudogene 1 . . . . . . . . . . . MTATP6P2 . . . mitochondrially encoded ATP synthase 6 pseudogene 2 . . . . . . . . . . . MTATP6P3 . . . mitochondrially encoded ATP synthase 6 pseudogene 3 . . . . . . . . . . . MTATP6P4 . . . mitochondrially encoded ATP synthase 6 pseudogene 4 . . . . . . . . . . . MTATP6P5 . . . mitochondrially encoded ATP synthase 6 pseudogene 5 . . . . . . . . . . . MTATP6P6 . . . mitochondrially encoded ATP synthase 6 pseudogene 6 . . . . . . . . . . . MTATP6P7 . . . mitochondrially encoded ATP synthase 6 pseudogene 7 . . . . . . . . . . . MTATP6P8 . . . mitochondrially encoded ATP synthase 6 pseudogene 8 . . . . . . . . . . . MTATP6P9 . . . mitochondrially encoded ATP synthase 6 pseudogene 9 . . . . . . . . . . . MTATP6P10 . . . mitochondrially encoded ATP synthase 6 pseudogene 10 . . . . . . . . . . . MTATP6P11 . . . mitochondrially encoded ATP synthase 6 pseudogene 11 . . . . . . . . . . . MTATP6P12 . . . mitochondrially encoded ATP synthase 6 pseudogene 12 . . . . . . . . . . . MTATP6P13 . . . mitochondrially encoded ATP synthase 6 pseudogene 13 . . . . . . . . . . . MTATP6P14 . . . mitochondrially encoded ATP synthase 6 pseudogene 14 . . . . . . . . . . . MTATP6P15 . . . mitochondrially encoded ATP synthase 6 pseudogene 15 . . . . . . . . . . . MTATP6P16 . . . mitochondrially encoded ATP synthase 6 pseudogene 16 . . . . . . . . . . . MTATP6P17 . . . mitochondrially encoded ATP synthase 6 pseudogene 17 . . . . . . . . . . . MTATP6P18 . . . mitochondrially encoded ATP synthase 6 pseudogene 18 . . . . . . . . . . . MTATP6P19 . . . mitochondrially encoded ATP synthase 6 pseudogene 19 . . . . . . . . . . . MTATP6P20 . . . mitochondrially encoded ATP synthase 6 pseudogene 20 . . . . . . . . . . . MTATP6P21 . . . mitochondrially encoded ATP synthase 6 pseudogene 21 . . . . . . . . . . . MTATP6P22 . . . mitochondrially encoded ATP synthase 6 pseudogene 22 . . . . . . . . . . . MTATP6P23 . . . mitochondrially encoded ATP synthase 6 pseudogene 23 . . . . . . . . . . . MTATP6P24 . . . mitochondrially encoded ATP synthase 6 pseudogene 24 . . . . . . . . . . . MTATP6P25 . . . mitochondrially encoded ATP synthase 6 pseudogene 25 . . . . . . . . . . . MTATP6P26 . . . mitochondrially encoded ATP synthase 6 pseudogene 26 . . . . . . . . . . . MTATP6P27 . . . mitochondrially encoded ATP synthase 6 pseudogene 27 . . . . . . . . . . . MTATP6P28 . . . mitochondrially encoded ATP synthase 6 pseudogene 28 . . . . . . . . . . . MTATP6P29 . . . mitochondrially encoded ATP synthase 6 pseudogene 29 . . . . . . . . . . . MTATP6P30 . . . mitochondrially encoded ATP synthase 6 pseudogene 30 . . . . . . . . . . . MTATP6P31 . . . mitochondrially encoded ATP synthase 6 pseudogene 31 . . . . . . . . . . . MTATP8P1 . . . mitochondrially encoded ATP synthase 8 pseudogene 1 . . . . . . . . . . . MTATP8P2 . . . mitochondrially encoded ATP synthase 8 pseudogene 2 . . . . . . . . . . . MTATP8P3 . . . mitochondrially encoded ATP synthase 8 pseudogene 3 . . . . . . . . . . . MTATP8P4 . . . mitochondrially encoded ATP synthase 8 pseudogene 4 . . . . . . . . . . . MTATT . . . mitochondrially encoded membrane attachment site . . . . . . . . . . . MTBP 1.71020418457244e-07 0.998224554400032 0.00177527457954934 MDM2 binding protein FUNCTION: Inhibits cell migration in vitro and suppresses the invasive behavior of tumor cells (By similarity). May play a role in MDM2-dependent p53/TP53 homeostasis in unstressed cells. Inhibits autoubiquitination of MDM2, thereby enhancing MDM2 stability. This promotes MDM2-mediated ubiquitination of p53/TP53 and its subsequent degradation. {ECO:0000250, ECO:0000269|PubMed:15632057}.; . . unclassifiable (Anatomical System);whole body;frontal lobe;tongue;adrenal gland;bone;thyroid;placenta;liver;testis;head and neck;brain;skeletal muscle;thymus; . 0.12969 0.09906 0.826715241 88.09271054 500.02874 4.59007 MTCH1 0.964878856015847 0.0351080625998294 1.30813843230847e-05 mitochondrial carrier 1 FUNCTION: Potential mitochondrial transporter. May play a role in apoptosis. {ECO:0000269|PubMed:12377771}.; . TISSUE SPECIFICITY: Widely expressed with a predominant expression in brain. {ECO:0000269|PubMed:10551805}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;amygdala;cartilage;adrenal cortex;lens;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;colon;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;aorta;stomach;cerebellum; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;thyroid;prefrontal cortex;globus pallidus;parietal lobe;cerebellum; 0.15739 0.11063 -0.185391282 39.67916962 263.40004 3.48226 MTCH2 0.166788403447163 0.832602198967749 0.000609397585087671 mitochondrial carrier 2 FUNCTION: The substrate transported is not yet known. Induces mitochondrial depolarization.; . . medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;bladder;brain;tonsil;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;testis;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; testis - interstitial;testis - seminiferous tubule;liver;testis;kidney; 0.40403 . 0.637604436 83.77565464 2590.74426 9.52271 MTCL1 . . . microtubule crosslinking factor 1 FUNCTION: Microtubule-associated factor involved in the late phase of epithelial polarization and microtubule dynamics regulation. Plays a role in the development and maintenance of non-centrosomal microtubule bundles at the lateral membrane in polarized epithelial cells. {ECO:0000269|PubMed:23902687}.; . . . . 0.32389 0.10012 -1.295874499 4.971691437 . . MTCL1P1 . . . MTCL1 pseudogene 1 . . . . . . . . . . . MTCO1P1 . . . MT-CO1 pseudogene 1 . . . . . . . . . . . MTCO1P2 . . . MT-CO1 pseudogene 2 . . . . . . . . . . . MTCO1P3 . . . MT-CO1 pseudogene 3 . . . . . . . . . . . MTCO1P4 . . . MT-CO1 pseudogene 4 . . . . . . . . . . . MTCO1P5 . . . MT-CO1 pseudogene 5 . . . . . . . . . . . MTCO1P6 . . . MT-CO1 pseudogene 6 . . . . . . . . . . . MTCO1P7 . . . MT-CO1 pseudogene 7 . . . . . . . . . . . MTCO1P8 . . . MT-CO1 pseudogene 8 . . . . . . . . . . . MTCO1P9 . . . MT-CO1 pseudogene 9 . . . . . . . . . . . MTCO1P10 . . . MT-CO1 pseudogene 10 . . . . . . . . . . . MTCO1P11 . . . MT-CO1 pseudogene 11 . . . . . . . . . . . MTCO1P12 . . . MT-CO1 pseudogene 12 . . . . . . . . . . . MTCO1P13 . . . MT-CO1 pseudogene 13 . . . . . . . . . . . MTCO1P14 . . . MT-CO1 pseudogene 14 . . . . . . . . . . . MTCO1P15 . . . MT-CO1 pseudogene 15 . . . . . . . . . . . MTCO1P16 . . . MT-CO1 pseudogene 16 . . . . . . . . . . . MTCO1P17 . . . MT-CO1 pseudogene 17 . . . . . . . . . . . MTCO1P18 . . . MT-CO1 pseudogene 18 . . . . . . . . . . . MTCO1P19 . . . MT-CO1 pseudogene 19 . . . . . . . . . . . MTCO1P20 . . . MT-CO1 pseudogene 20 . . . . . . . . . . . MTCO1P21 . . . MT-CO1 pseudogene 21 . . . . . . . . . . . MTCO1P22 . . . MT-CO1 pseudogene 22 . . . . . . . . . . . MTCO1P23 . . . MT-CO1 pseudogene 23 . . . . . . . . . . . MTCO1P24 . . . MT-CO1 pseudogene 24 . . . . . . . . . . . MTCO1P25 . . . MT-CO1 pseudogene 25 . . . . . . . . . . . MTCO1P26 . . . MT-CO1 pseudogene 26 . . . . . . . . . . . MTCO1P27 . . . MT-CO1 pseudogene 27 . . . . . . . . . . . MTCO1P28 . . . MT-CO1 pseudogene 28 . . . . . . . . . . . MTCO1P29 . . . MT-CO1 pseudogene 29 . . . . . . . . . . . MTCO1P30 . . . MT-CO1 pseudogene 30 . . . . . . . . . . . MTCO1P31 . . . MT-CO1 pseudogene 31 . . . . . . . . . . . MTCO1P32 . . . MT-CO1 pseudogene 32 . . . . . . . . . . . MTCO1P33 . . . MT-CO1 pseudogene 33 . . . . . . . . . . . MTCO1P34 . . . MT-CO1 pseudogene 34 . . . . . . . . . . . MTCO1P35 . . . MT-CO1 pseudogene 35 . . . . . . . . . . . MTCO1P36 . . . MT-CO1 pseudogene 36 . . . . . . . . . . . MTCO1P37 . . . MT-CO1 pseudogene 37 . . . . . . . . . . . MTCO1P38 . . . MT-CO1 pseudogene 38 . . . . . . . . . . . MTCO1P39 . . . MT-CO1 pseudogene 39 . . . . . . . . . . . MTCO1P40 . . . MT-CO1 pseudogene 40 . . . . . . . . . . . MTCO1P41 . . . MT-CO1 pseudogene 41 . . . . . . . . . . . MTCO1P42 . . . MT-CO1 pseudogene 42 . . . . . . . . . . . MTCO1P43 . . . MT-CO1 pseudogene 43 . . . . . . . . . . . MTCO1P44 . . . MT-CO1 pseudogene 44 . . . . . . . . . . . MTCO1P45 . . . MT-CO1 pseudogene 45 . . . . . . . . . . . MTCO1P46 . . . MT-CO1 pseudogene 46 . . . . . . . . . . . MTCO1P47 . . . MT-CO1 pseudogene 47 . . . . . . . . . . . MTCO1P48 . . . MT-CO1 pseudogene 48 . . . . . . . . . . . MTCO1P49 . . . MT-CO1 pseudogene 49 . . . . . . . . . . . MTCO1P50 . . . MT-CO1 pseudogene 50 . . . . . . . . . . . MTCO1P51 . . . MT-CO1 pseudogene 51 . . . . . . . . . . . MTCO1P52 . . . MT-CO1 pseudogene 52 . . . . . . . . . . . MTCO1P53 . . . MT-CO1 pseudogene 53 . . . . . . . . . . . MTCO1P54 . . . MT-CO1 pseudogene 54 . . . . . . . . . . . MTCO1P55 . . . MT-CO1 pseudogene 55 . . . . . . . . . . . MTCO1P56 . . . MT-CO1 pseudogene 56 . . . . . . . . . . . MTCO2P1 . . . MT-CO2 pseudogene 1 . . . . . . . . . . . MTCO2P2 . . . MT-CO2 pseudogene 2 . . . . . . . . . . . MTCO2P3 . . . MT-CO2 pseudogene 3 . . . . . . . . . . . MTCO2P4 . . . MT-CO2 pseudogene 4 . . . . . . . . . . . MTCO2P5 . . . MT-CO2 pseudogene 5 . . . . . . . . . . . MTCO2P6 . . . MT-CO2 pseudogene 6 . . . . . . . . . . . MTCO2P7 . . . MT-CO2 pseudogene 7 . . . . . . . . . . . MTCO2P8 . . . MT-CO2 pseudogene 8 . . . . . . . . . . . MTCO2P9 . . . MT-CO2 pseudogene 9 . . . . . . . . . . . MTCO2P10 . . . MT-CO2 pseudogene 10 . . . . . . . . . . . MTCO2P11 . . . MT-CO2 pseudogene 11 . . . . . . . . . . . MTCO2P12 . . . MT-CO2 pseudogene 12 . . . . . . . . . . . MTCO2P13 . . . MT-CO2 pseudogene 13 . . . . . . . . . . . MTCO2P14 . . . MT-CO2 pseudogene 14 . . . . . . . . . . . MTCO2P15 . . . MT-CO2 pseudogene 15 . . . . . . . . . . . MTCO2P16 . . . MT-CO2 pseudogene 16 . . . . . . . . . . . MTCO2P17 . . . MT-CO2 pseudogene 17 . . . . . . . . . . . MTCO2P18 . . . MT-CO2 pseudogene 18 . . . . . . . . . . . MTCO2P19 . . . MT-CO2 pseudogene 19 . . . . . . . . . . . MTCO2P20 . . . MT-CO2 pseudogene 20 . . . . . . . . . . . MTCO2P21 . . . MT-CO2 pseudogene 21 . . . . . . . . . . . MTCO2P22 . . . MT-CO2 pseudogene 22 . . . . . . . . . . . MTCO2P23 . . . MT-CO2 pseudogene 23 . . . . . . . . . . . MTCO2P24 . . . MT-CO2 pseudogene 24 . . . . . . . . . . . MTCO2P25 . . . MT-CO2 pseudogene 25 . . . . . . . . . . . MTCO2P26 . . . MT-CO2 pseudogene 26 . . . . . . . . . . . MTCO2P27 . . . MT-CO2 pseudogene 27 . . . . . . . . . . . MTCO2P28 . . . MT-CO2 pseudogene 28 . . . . . . . . . . . MTCO2P29 . . . MT-CO2 pseudogene 29 . . . . . . . . . . . MTCO2P30 . . . MT-CO2 pseudogene 30 . . . . . . . . . . . MTCO2P31 . . . MT-CO2 pseudogene 31 . . . . . . . . . . . MTCO2P32 . . . MT-CO2 pseudogene 32 . . . . . . . . . . . MTCO2P33 . . . MT-CO2 pseudogene 33 . . . . . . . . . . . MTCO3P1 . . . MT-CO3 pseudogene 1 . . . . . . . . . . . MTCO3P2 . . . MT-CO3 pseudogene 2 . . . . . . . . . . . MTCO3P3 . . . MT-CO3 pseudogene 3 . . . . . . . . . . . MTCO3P4 . . . MT-CO3 pseudogene 4 . . . . . . . . . . . MTCO3P5 . . . MT-CO3 pseudogene 5 . . . . . . . . . . . MTCO3P6 . . . MT-CO3 pseudogene 6 . . . . . . . . . . . MTCO3P7 . . . MT-CO3 pseudogene 7 . . . . . . . . . . . MTCO3P8 . . . MT-CO3 pseudogene 8 . . . . . . . . . . . MTCO3P9 . . . MT-CO3 pseudogene 9 . . . . . . . . . . . MTCO3P10 . . . MT-CO3 pseudogene 10 . . . . . . . . . . . MTCO3P11 . . . MT-CO3 pseudogene 11 . . . . . . . . . . . MTCO3P12 . . . MT-CO3 pseudogene 12 . . . . . 0.15855 . . . . . MTCO3P13 . . . MT-CO3 pseudogene 13 . . . . . . . . . . . MTCO3P14 . . . MT-CO3 pseudogene 14 . . . . . . . . . . . MTCO3P15 . . . MT-CO3 pseudogene 15 . . . . . . . . . . . MTCO3P16 . . . MT-CO3 pseudogene 16 . . . . . . . . . . . MTCO3P17 . . . MT-CO3 pseudogene 17 . . . . . . . . . . . MTCO3P18 . . . MT-CO3 pseudogene 18 . . . . . . . . . . . MTCO3P19 . . . MT-CO3 pseudogene 19 . . . . . . . . . . . MTCO3P20 . . . MT-CO3 pseudogene 20 . . . . . . . . . . . MTCO3P21 . . . MT-CO3 pseudogene 21 . . . . . . . . . . . MTCO3P22 . . . MT-CO3 pseudogene 22 . . . . . . . . . . . MTCO3P23 . . . MT-CO3 pseudogene 23 . . . . . . . . . . . MTCO3P24 . . . MT-CO3 pseudogene 24 . . . . . . . . . . . MTCO3P25 . . . MT-CO3 pseudogene 25 . . . . . . . . . . . MTCO3P26 . . . MT-CO3 pseudogene 26 . . . . . . . . . . . MTCO3P27 . . . MT-CO3 pseudogene 27 . . . . . . . . . . . MTCO3P28 . . . MT-CO3 pseudogene 28 . . . . . . . . . . . MTCO3P29 . . . MT-CO3 pseudogene 29 . . . . . . . . . . . MTCO3P30 . . . MT-CO3 pseudogene 30 . . . . . . . . . . . MTCO3P31 . . . MT-CO3 pseudogene 31 . . . . . . . . . . . MTCO3P32 . . . MT-CO3 pseudogene 32 . . . . . . . . . . . MTCO3P33 . . . MT-CO3 pseudogene 33 . . . . . . . . . . . MTCO3P34 . . . MT-CO3 pseudogene 34 . . . . . . . . . . . MTCO3P35 . . . MT-CO3 pseudogene 35 . . . . . . . . . . . MTCO3P36 . . . MT-CO3 pseudogene 36 . . . . . . . . . . . MTCO3P37 . . . MT-CO3 pseudogene 37 . . . . . . . . . . . MTCO3P38 . . . MT-CO3 pseudogene 38 . . . . . . . . . . . MTCO3P39 . . . MT-CO3 pseudogene 39 . . . . . . . . . . . MTCO3P40 . . . MT-CO3 pseudogene 40 . . . . . . . . . . . MTCO3P41 . . . MT-CO3 pseudogene 41 . . . . . . . . . . . MTCO3P42 . . . MT-CO3 pseudogene 42 . . . . . . . . . . . MTCO3P43 . . . MT-CO3 pseudogene 43 . . . . . . . . . . . MTCO3P44 . . . MT-CO3 pseudogene 44 . . . . . . . . . . . MTCO3P45 . . . MT-CO3 pseudogene 45 . . . . . . . . . . . MTCO3P46 . . . MT-CO3 pseudogene 46 . . . . . . . . . . . MTCP1 0.342313098947147 0.599511413059822 0.0581754879930306 mature T-cell proliferation 1 FUNCTION: Enhances the phosphorylation and activation of AKT1 and AKT2. {ECO:0000269|PubMed:10983986}.; . TISSUE SPECIFICITY: Not found at a significant level in any tissue.; cervix;germinal center; . 0.21172 . 0.145304857 63.81221986 2.98111 0.10837 MTCSB1 . . . mitochondrially encoded conserved sequence block I . . . . . . . . . . . MTCSB2 . . . mitochondrially encoded conserved sequence block II . . . . . . . . . . . MTCSB3 . . . mitochondrially encoded conserved sequence block III . . . . . . . . . . . MTCYBP1 . . . MT-CYB pseudogene 1 . . . . . . . . . . . MTCYBP2 . . . MT-CYB pseudogene 2 . . . . . . . . . . . MTCYBP3 . . . MT-CYB pseudogene 3 . . . . . . . . . . . MTCYBP4 . . . MT-CYB pseudogene 4 . . . . . . . . . . . MTCYBP5 . . . MT-CYB pseudogene 5 . . . . . . . . . . . MTCYBP6 . . . MT-CYB pseudogene 6 . . . . . . . . . . . MTCYBP7 . . . MT-CYB pseudogene 7 . . . . . . . . . . . MTCYBP8 . . . MT-CYB pseudogene 8 . . . . . . . . . . . MTCYBP9 . . . MT-CYB pseudogene 9 . . . . . . . . . . . MTCYBP10 . . . MT-CYB pseudogene 10 . . . . . . . . . . . MTCYBP11 . . . MT-CYB pseudogene 11 . . . . . . . . . . . MTCYBP12 . . . MT-CYB pseudogene 12 . . . . . . . . . . . MTCYBP13 . . . MT-CYB pseudogene 13 . . . . . . . . . . . MTCYBP14 . . . MT-CYB pseudogene 14 . . . . . . . . . . . MTCYBP15 . . . MT-CYB pseudogene 15 . . . . . . . . . . . MTCYBP16 . . . MT-CYB pseudogene 16 . . . . . . . . . . . MTCYBP17 . . . MT-CYB pseudogene 17 . . . . . . . . . . . MTCYBP18 . . . MT-CYB pseudogene 18 . . . . . . . . . . . MTCYBP19 . . . MT-CYB pseudogene 19 . . . . . . . . . . . MTCYBP20 . . . MT-CYB pseudogene 20 . . . . . . . . . . . MTCYBP21 . . . MT-CYB pseudogene 21 . . . . . . . . . . . MTCYBP22 . . . MT-CYB pseudogene 22 . . . . . . . . . . . MTCYBP23 . . . MT-CYB pseudogene 23 . . . . . . . . . . . MTCYBP24 . . . MT-CYB pseudogene 24 . . . . . . . . . . . MTCYBP25 . . . MT-CYB pseudogene 25 . . . . . . . . . . . MTCYBP26 . . . MT-CYB pseudogene 26 . . . . . . . . . . . MTCYBP27 . . . MT-CYB pseudogene 27 . . . . . . . . . . . MTCYBP28 . . . MT-CYB pseudogene 28 . . . . . . . . . . . MTCYBP29 . . . MT-CYB pseudogene 29 . . . . . . . . . . . MTCYBP30 . . . MT-CYB pseudogene 30 . . . . . . . . . . . MTCYBP31 . . . MT-CYB pseudogene 31 . . . . . . . . . . . MTCYBP32 . . . MT-CYB pseudogene 32 . . . . . . . . . . . MTDH 0.721809341419168 0.278165221279176 2.54373016567053e-05 metadherin FUNCTION: Downregulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF- kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance. {ECO:0000269|PubMed:15927426, ECO:0000269|PubMed:16452207, ECO:0000269|PubMed:18316612, ECO:0000269|PubMed:19111877}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in muscle-dominating organs such as skeletal muscle, heart, tongue and small intestine and in endocrine glands such as thyroid and adrenal gland. Overexpressed in various cancers including breast, brain, prostate, melanoma and glioblastoma multiforme. {ECO:0000269|PubMed:15927426}.; myocardium;lymphoreticular;ovary;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;head and neck;kidney;stomach;thymus; amygdala;superior cervical ganglion;medulla oblongata;prefrontal cortex;white blood cells;trigeminal ganglion;cingulate cortex;parietal lobe; 0.42250 0.14254 -0.424258538 25.56027365 333.467 3.87963 MTERF1 . . . mitochondrial transcription termination factor 1 FUNCTION: Transcription termination factor. Binds to a 28 bp region within the tRNA(Leu(uur)) gene at a position immediately adjacent to and downstream of the 16S rRNA gene; this region comprises a tridecamer sequence critical for directing accurate termination. Binds DNA along the major grove and promotes DNA bending and partial unwinding. Promotes base flipping. Transcription termination activity appears to be polarized with highest specificity for transcripts initiated on the light strand. {ECO:0000269|PubMed:20550934}.; . . . . 0.07799 0.07345 0.396906589 76.30927105 . . MTERF2 . . . mitochondrial transcription termination factor 2 FUNCTION: Binds promoter DNA and regulates mitochondrial transcription. Required for normal levels of transcription, both for mRNA and tRNA. Required for normal mitochondrial protein synthesis, assembly of respiratory complexes and normal mitochondrial function (By similarity). {ECO:0000250, ECO:0000269|PubMed:16226716, ECO:0000269|PubMed:19366608}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, liver and pancreas. {ECO:0000269|PubMed:16226716}.; . . 0.07927 0.07822 0.639420866 83.8995046 . . MTERF3 . . . mitochondrial transcription termination factor 3 FUNCTION: Binds promoter DNA and regulates initiation of transcription. Required for normal mitochondrial transcription, and for normal assembly of mitochondrial respiratory complexes. Required for normal mitochondrial function (By similarity). {ECO:0000250, ECO:0000269|PubMed:17662942}.; . TISSUE SPECIFICITY: Highly expressed in heart, liver, kidney and testis. Detected at lower levels in brain, spleen and lung. {ECO:0000269|PubMed:17662942}.; . . 0.45357 0.08910 0.553050905 81.54635527 . . MTERF4 . . . mitochondrial transcription termination factor 4 FUNCTION: Regulator of mitochondrial ribosome biogenesis and translation. Binds to mitochondrial ribosomal RNAs 16S, 12S and 7S and targets NSUN4 RNA methyltransferase to the mitochondrial large ribosomal subunit (39S). {ECO:0000269|PubMed:21531335}.; . . . . 0.09584 0.07784 0.240763792 69.36777542 . . MTF1 0.991394717050406 0.00860520007699817 8.28725959972157e-08 metal-regulatory transcription factor 1 FUNCTION: Activates the metallothionein I promoter. Binds to the metal responsive element (MRE). {ECO:0000269|PubMed:8065932}.; . . . . 0.88579 0.09665 7.61E-05 53.98089172 88.53093 2.01737 MTF2 0.994599740764267 0.00540023271949103 2.65162418480256e-08 metal response element binding transcription factor 2 FUNCTION: Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex, leading to enhance PRC2 H3K27me3 methylation activity. Regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation. Promotes recruitment of the PRC2 complex to the inactive X chromosome in differentiating XX ES cells and PRC2 recruitment to target genes in undifferentiated ES cells. Required to repress Hox genes by enhancing H3K27me3 methylation of the PRC2 complex. In some conditions may act as an inhibitor of PRC2 activity: able to activate the CDKN2A gene and promote cellular senescence by suppressing the catalytic activity of the PRC2 complex locally. Binds to the metal-regulating-element (MRE) of MT1A gene promoter (By similarity). {ECO:0000250}.; . . . . 0.93479 0.10208 -0.558357437 19.54470394 44.59794 1.27984 MTFMT 0.000216329665423534 0.911766402901333 0.0880172674332428 mitochondrial methionyl-tRNA formyltransferase FUNCTION: Formylates methionyl-tRNA in mitochondria. A single tRNA(Met) gene gives rise to both an initiator and an elongator species via an unknown mechanism (By similarity). {ECO:0000250}.; DISEASE: Combined oxidative phosphorylation deficiency 15 (COXPD15) [MIM:614947]: An autosomal recessive, mitochondrial, neurologic disorder characterized by features of Leigh syndrome and combined oxidative phosphorylation deficiency. Clinical features include mild global developmental delay, white matter abnormalities, ataxia, incoordination, speech and reading difficulties, T2-weighted hyperintensities in the basal ganglia, corpus callosum, and brainstem. {ECO:0000269|PubMed:21907147}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. {ECO:0000269|PubMed:22499348}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;parathyroid;skeletal muscle;prostate;lung;frontal lobe;placenta;thyroid;testis;mammary gland;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.82422 0.12092 0.705562627 85.52724699 452.93697 4.42827 MTFP1 0.316869739233121 0.614187775658895 0.0689424851079838 mitochondrial fission process 1 FUNCTION: Involved in the mitochondrial division probably by regulating membrane fission. Loss-of-function induces the release of cytochrome c, which activates the caspase cascade and leads to apoptosis. {ECO:0000269|PubMed:15155745, ECO:0000269|PubMed:15985469}.; . . lymphoreticular;umbilical cord;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; . . . -0.139478553 43.29440906 . . MTFR1 2.18012894299362e-05 0.725039272759523 0.274938925951047 mitochondrial fission regulator 1 FUNCTION: May play a role in mitochondrial aerobic respiration. May also regulate mitochondrial organization and fission (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;adrenal cortex;blood;skeletal muscle;bile duct;breast;lung;placenta;visual apparatus;liver;duodenum;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11549 0.07647 -0.271755481 34.31823543 49.51178 1.37662 MTFR1L 0.431750877541367 0.561071437118803 0.00717768533982989 mitochondrial fission regulator 1 like . . . . . 0.10337 . -0.181750739 40.15687662 282.03745 3.59612 MTFR2 0.000151538368941259 0.869231680200369 0.130616781430689 mitochondrial fission regulator 2 FUNCTION: May play a role in mitochondrial aerobic respiration essentially in the testis. Can also promote mitochondrial fission (By similarity). {ECO:0000250}.; . . . . 0.12915 . 0.442818085 77.8544468 171.35461 2.85458 MTG1 0.0626719606528276 0.921602536724375 0.0157255026227974 mitochondrial ribosome-associated GTPase 1 FUNCTION: Plays a role in the regulation of the mitochondrial ribosome assembly and of translational activity. Displays mitochondrial GTPase activity. {ECO:0000269|PubMed:23396448}.; . . . . 0.07408 . -0.578583623 18.71903751 8.97144 0.32927 MTG2 0.000608857161369286 0.903183313781914 0.096207829056717 mitochondrial ribosome-associated GTPase 2 FUNCTION: Plays a role in the regulation of the mitochondrial ribosome assembly and of translational activity. Displays GTPase activity. Involved in the ribosome maturation process. {ECO:0000269|PubMed:17054726, ECO:0000269|PubMed:23396448}.; . . . . 0.06936 0.08669 0.536463361 81.06864827 314.23159 3.76981 MTHFD1 0.605609113854515 0.394390757729368 1.28416117233796e-07 methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1, methenyltetrahydrofolate cyclohydrolase, formyltetrahydrofolate synthetase . DISEASE: Neural tube defects, folate-sensitive (NTDFS) [MIM:601634]: The most common NTDs are open spina bifida (myelomeningocele) and anencephaly. {ECO:0000269|PubMed:12384833, ECO:0000269|PubMed:16552426, ECO:0000269|PubMed:9611072}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; DISEASE: Note=MTHFD1 deficiency, due to mutation in this gene, can cause a metabolic syndrome with variable features including hyperhomocysteinemia, megaloblastic anemia, hemolytic uremic syndrome (HUS), severe combined immunodeficiency, microangiopathy and retinopathy. Symptoms improve after treatment with hydroxocobalamin, betaine and folinic acid. {ECO:0000269|PubMed:21813566, ECO:0000269|PubMed:25633902}.; TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;thyroid;iris;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;spinal cord;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;liver;kidney;skeletal muscle; 0.77953 0.21031 0.380318343 75.63104506 2881.0731 10.16705 MTHFD1L 0.0825195293160823 0.917479751480695 7.19203222439943e-07 methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1-like FUNCTION: May provide the missing metabolic reaction required to link the mitochondria and the cytoplasm in the mammalian model of one-carbon folate metabolism in embryonic an transformed cells complementing thus the enzymatic activities of MTHFD2. {ECO:0000250, ECO:0000269|PubMed:16171773}.; . TISSUE SPECIFICITY: Detected in most tissues, highest expression found in placenta, thymus and brain. Low expression is found in liver and skeletal muscle. Up-regulated in colon adenocarcinoma. {ECO:0000269|PubMed:12937168, ECO:0000269|PubMed:15013446}.; . . 0.08466 0.26137 -0.350843407 29.54116537 277.38146 3.56775 MTHFD1P1 . . . methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1 pseudogene 1 . . . . . . . . . . . MTHFD2 0.151202634179126 0.84520092821355 0.00359643760732401 methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase . . . lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach; tumor;white blood cells;skeletal muscle; 0.55857 0.25511 -0.229483771 36.86010852 38.50372 1.14192 MTHFD2L 0.000263184973008233 0.777231884814297 0.222504930212695 methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2-like . . TISSUE SPECIFICITY: Isoform 1, isoform 4 and isoform 5 are expressed in brain and placenta. {ECO:0000269|PubMed:21163947}.; unclassifiable (Anatomical System);medulla oblongata;cartilage;islets of Langerhans;hypothalamus;colon;parathyroid;bone marrow;prostate;whole body;lung;endometrium;larynx;hippocampus;liver;testis;head and neck;kidney;brain;thymus; dorsal root ganglion; 0.10257 0.28143 -0.359940251 28.93371078 35.86805 1.07770 MTHFD2P1 . . . methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase pseudogene 1 . . . . . . . . . . . MTHFD2P2 . . . methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase pseudogene 2 . . . . . . . . . . . MTHFD2P3 . . . methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase pseudogene 3 . . . . . . . . . . . MTHFD2P4 . . . methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase pseudogene 4 . . . . . . . . . . . MTHFD2P5 . . . methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase pseudogene 5 . . . . . . . . . . . MTHFD2P6 . . . methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase pseudogene 6 . . . . . . . . . . . MTHFD2P7 . . . methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase pseudogene 7 . . . . . . . . . . . MTHFR 2.45515809266206e-07 0.900732805922013 0.0992669485621777 methylenetetrahydrofolate reductase (NAD(P)H) FUNCTION: Catalyzes the conversion of 5,10- methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co- substrate for homocysteine remethylation to methionine. {ECO:0000269|PubMed:25736335}.; DISEASE: Methylenetetrahydrofolate reductase deficiency (MTHFRD) [MIM:236250]: Autosomal recessive disorder with a wide range of features including homocysteinuria, homocysteinemia [MIM:603174], developmental delay, severe mental retardation, perinatal death, psychiatric disturbances, and later-onset neurodegenerative disorders. {ECO:0000269|PubMed:10679944, ECO:0000269|PubMed:20236116, ECO:0000269|PubMed:25736335, ECO:0000269|PubMed:7726158, ECO:0000269|PubMed:8940272, ECO:0000269|PubMed:9781030}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. {ECO:0000269|PubMed:15534175}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Neural tube defects, folate-sensitive (NTDFS) [MIM:601634]: The most common NTDs are open spina bifida (myelomeningocele) and anencephaly. {ECO:0000269|PubMed:10323741, ECO:0000269|PubMed:7564788, ECO:0000269|PubMed:8826441}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . . . 0.13143 0.90853 0.093718683 60.71007313 4524.99996 13.51805 MTHFS 0.0406510504988124 0.842923193228791 0.116425756272396 5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase) FUNCTION: Contributes to tetrahydrofolate metabolism. Helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids. Catalyzes the irreversible conversion of 5-formyltetrahydrofolate (5-FTHF) to yield 5,10- methenyltetrahydrofolate. {ECO:0000269|PubMed:8522195}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; medulla oblongata;temporal lobe;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.11060 0.22864 0.03689118 56.64071715 50.25348 1.39281 MTHFSD 3.76450383104559e-09 0.0985308147307845 0.901469181504712 methenyltetrahydrofolate synthetase domain containing . . . unclassifiable (Anatomical System);lymph node;ovary;heart;colon;blood;bone marrow;whole body;lung;cerebral cortex;oesophagus;epididymis;thyroid;placenta;testis;cervix;head and neck;germinal center;kidney;spinal ganglion;brain;aorta; . 0.09755 0.09128 1.309952855 94.01981599 2917.56396 10.24622 MTHPR . . . mitochondrially encoded replication primer . . . . . . . . . . . MTHSP1 . . . mitochondrially encoded major H-strand promoter . . . . . . . . . . . MTHSP2 . . . mitochondrially encoded minor H-strand promoter . . . . . . . . . . . MTIF2 9.07160853775263e-08 0.913238313037716 0.0867615962461982 mitochondrial translational initiation factor 2 FUNCTION: One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.; . TISSUE SPECIFICITY: Expressed in all tissues examined. Highest level in skeletal muscle.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;lens;skeletal muscle;breast;lung;trabecular meshwork;placenta;macula lutea;liver;hypopharynx;alveolus;head and neck;cervix;kidney;stomach; tumor;white blood cells;pons; 0.26104 0.19736 -0.885424753 10.4623732 69.04388 1.72135 MTIF2P1 . . . mitochondrial translational initiation factor 2 pseudogene 1 . . . . . . . . . . . MTIF3 0.0296353067663883 0.923982041010771 0.0463826522228408 mitochondrial translational initiation factor 3 FUNCTION: IF-3 binds to the 28S ribosomal subunit and shifts the equilibrum between 55S ribosomes and their 39S and 28S subunits in favor of the free subunits, thus enhancing the availability of 28S subunits on which protein synthesis initiation begins. {ECO:0000269|PubMed:12095986}.; . . . . 0.00894 0.03979 0.505321956 80.00707714 46.07108 1.30766 MTL3P . . . metallothionein-like 3, pseudogene . . . . . . . . . . . MTL5 0.0332214023664625 0.958077962730627 0.00870063490291033 metallothionein-like 5, testis-specific (tesmin) FUNCTION: May have a role in spermatogenesis. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed specifically in testis.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;optic nerve;testis;brain;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node; 0.08133 0.14319 0.551232944 81.48148148 461.30216 4.45421 MTLSP . . . mitochondrially encoded L-strand promoter . . . . . . . . . . . MTM1 0.999351773879244 0.000648222441858714 3.67889752928532e-09 myotubularin 1 FUNCTION: Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Has also been shown to dephosphorylate phosphotyrosine- and phosphoserine- containing peptides. Negatively regulates EGFR degradation through regulation of EGFR trafficking from the late endosome to the lysosome. Plays a role in vacuolar formation and morphology. Regulates desmin intermediate filament assembly and architecture. Plays a role in mitochondrial morphology and positioning. Required for skeletal muscle maintenance but not for myogenesis. {ECO:0000269|PubMed:10900271, ECO:0000269|PubMed:11001925, ECO:0000269|PubMed:12646134, ECO:0000269|PubMed:14722070, ECO:0000269|PubMed:21135508, ECO:0000269|PubMed:9537414}.; DISEASE: Myopathy, centronuclear, X-linked (CNMX) [MIM:310400]: A congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers. {ECO:0000269|PubMed:10063835, ECO:0000269|PubMed:10466421, ECO:0000269|PubMed:10502779, ECO:0000269|PubMed:11793470, ECO:0000269|PubMed:12031625, ECO:0000269|PubMed:12522554, ECO:0000269|PubMed:12859411, ECO:0000269|PubMed:17005396, ECO:0000269|PubMed:19129059, ECO:0000269|PubMed:9285787, ECO:0000269|PubMed:9305655, ECO:0000269|PubMed:9829274}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;endometrium;bone;testis;amniotic fluid;germinal center;brain;gall bladder;unclassifiable (Anatomical System);small intestine;heart;cartilage;hypothalamus;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;stomach;aorta;thymus; . 0.31653 0.10908 -0.516085732 21.20193442 16.92439 0.59626 MTMR1 0.982418902141347 0.0175806193886354 4.78470017728504e-07 myotubularin related protein 1 FUNCTION: Lipid phosphatase that has high specificity for phosphatidylinositol 3-phosphate and has no activity with phosphatidylinositol (3,5)-bisphosphate. {ECO:0000269|PubMed:11733541}.; . . . . 0.40027 0.17628 -0.093566408 46.7386176 23.17742 0.77408 MTMR2 0.212768599766799 0.787228295192622 3.10504057926517e-06 myotubularin related protein 2 FUNCTION: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate. {ECO:0000269|PubMed:11733541, ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:21372139}.; DISEASE: Charcot-Marie-Tooth disease 4B1 (CMT4B1) [MIM:601382]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot- Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie-Tooth disease are designated CMT4. {ECO:0000269|PubMed:10802647, ECO:0000269|PubMed:12398840}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lens;skeletal muscle;bile duct;lung;placenta;visual apparatus;macula lutea;liver;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;testis - interstitial;prefrontal cortex;testis;trigeminal ganglion; 0.13038 0.21752 0.330767508 73.53739089 1688.18554 7.57552 MTMR3 0.994951612157603 0.0050483878046937 3.77037776212988e-11 myotubularin related protein 3 FUNCTION: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate. May also dephosphorylate proteins phosphorylated on Ser, Thr, and Tyr residues (PubMed:10733931). {ECO:0000269|PubMed:10733931, ECO:0000269|PubMed:11676921}.; . . medulla oblongata;ovary;salivary gland;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;placenta;visual apparatus;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.24100 0.11999 -0.902027742 10.1556971 326.83215 3.84289 MTMR4 0.997305474235374 0.00269452572438795 4.02384896460670e-11 myotubularin related protein 4 FUNCTION: Dephosphorylates proteins phosphorylated on Ser, Thr, and Tyr residues and low molecular weight phosphatase substrate para-nitrophenylphosphate. Phosphorylates phosphatidylinositol 3,4,5-trisphosphate (PIP3). {ECO:0000269|PubMed:11302699}.; . TISSUE SPECIFICITY: Expressed in brain, heart, kidney, spleen, liver, colon, testis, muscle, placenta, thyroid gland, pancreas, ovary, prostate, skin, peripheral blood, and bone marrow. {ECO:0000269|PubMed:11302699}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; medulla oblongata;superior cervical ganglion;cerebellum peduncles;pons;subthalamic nucleus;placenta;prefrontal cortex;testis;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.58620 . -0.551080959 19.93394669 10154.99993 21.97903 MTMR6 3.01310181922185e-06 0.983398194913008 0.0165987919851726 myotubularin related protein 6 FUNCTION: Phosphatase that acts on lipids with a phosphoinositol headgroup. Acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4+ T-cells possibly by decreasing intracellular levels of phosphatidylinositol 3 phosphatase. Negatively regulates proliferation of reactivated CD4+ T-cells. {ECO:0000269|PubMed:15831468, ECO:0000269|PubMed:16847315}.; . TISSUE SPECIFICITY: Expressed in CD4+ T-cells. {ECO:0000269|PubMed:16847315}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;meninges;lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;pia mater;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;aorta; amygdala; 0.31020 0.15707 0.953537969 90.08610521 4034.99654 12.59109 MTMR7 1.63743798338027e-09 0.822474656912603 0.177525341449959 myotubularin related protein 7 FUNCTION: Phosphatase that acts on lipids with a phosphoinositol headgroup. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed specifically in brain.; lung;islets of Langerhans;testis;brain; medulla oblongata;atrioventricular node;pons;trigeminal ganglion; 0.18115 0.12052 -1.126142808 6.564048125 760.94421 5.46875 MTMR8 1.33537060083682e-11 0.0261650738523496 0.973834926134297 myotubularin related protein 8 FUNCTION: Phosphatase that acts on lipids with a phosphoinositol headgroup. {ECO:0000305}.; . . lung;endometrium;placenta;brain; . 0.12800 0.08493 -0.773369631 13.10450578 70.77385 1.75016 MTMR9 0.210866148969841 0.789056593762587 7.72572675718502e-05 myotubularin related protein 9 FUNCTION: Probable pseudophosphatase. Contains a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase (Potential). {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in many tissues.; lymphoreticular;medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland; amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;cerebellum peduncles;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.09655 0.11430 -0.819281839 11.93677754 192.38541 3.00675 MTMR9LP . . . myotubularin related protein 9-like, pseudogene . . . . . . . . . . . MTMR10 0.0350497967234235 0.96461483762857 0.000335365648006566 myotubularin related protein 10 FUNCTION: Probable pseudophosphatase. Contains a Glu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase (Potential). {ECO:0000305}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;amygdala;unclassifiable (Anatomical System);cartilage;heart;small intestine;lacrimal gland;cerebellum cortex;islets of Langerhans;urinary;blood;skeletal muscle;bile duct;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;head and neck;spleen;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04354 . 0.378498378 75.58386412 720.47875 5.32943 MTMR11 7.32567938847539e-13 0.614341170755124 0.385658829244144 myotubularin related protein 11 FUNCTION: Probable pseudophosphatase. Contains a Glu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase (Potential). {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in bone marrow, spleen and thymus. {ECO:0000269|PubMed:17498563}.; unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;skeletal muscle;uterus;pancreas;prostate;lung;cochlea;adrenal gland;bone;placenta;pituitary gland;liver;testis;kidney;brain;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.10609 0.14121 0.314179756 72.75300778 2455.98065 9.22480 MTMR12 0.997884435033356 0.00211556442189225 5.44751607464504e-10 myotubularin related protein 12 FUNCTION: Catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularin intracellular location. {ECO:0000269|PubMed:11504939, ECO:0000269|PubMed:12847286}.; . TISSUE SPECIFICITY: Ubiquitous with prominent expression in brain, heart, kidney, placenta, and lung. {ECO:0000269|PubMed:11504939}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;thymus; . 0.18842 0.11936 0.134171522 63.57041755 230.19094 3.27962 MTMR14 0.00293982096906861 0.996954460199686 0.000105718831245735 myotubularin related protein 14 FUNCTION: Lipid phosphatase which efficiently dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P) and PtdIns(3,5)P2; inactive toward PtdIns4P, PtdIns(3,4)P2, PtdIns(4,5)P2 and PtdIns(3,4,5)P3. {ECO:0000269|PubMed:17008356}.; . TISSUE SPECIFICITY: Expressed in various tissues, including heart, skeletal muscle, placenta, liver, lung, kidney and pancreas. {ECO:0000269|PubMed:17008356}.; ovary;colon;substantia nigra;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;lens;breast;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.30998 0.11304 -0.911109353 9.961075725 98.92051 2.15158 MTND1P1 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 1 . . . . . . . . . . . MTND1P2 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 2 . . . . . . . . . . . MTND1P3 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 3 . . . . . . . . . . . MTND1P4 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 4 . . . . . . . . . . . MTND1P5 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 5 . . . . . . . . . . . MTND1P6 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 6 . . . . . . . . . . . MTND1P7 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 7 . . . . . . . . . . . MTND1P8 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 8 . . . . . . . . . . . MTND1P9 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 9 . . . . . . . . . . . MTND1P10 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 10 . . . . . . . . . . . MTND1P11 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 11 . . . . . . . . . . . MTND1P12 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 12 . . . . . . . . . . . MTND1P13 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 13 . . . . . . . . . . . MTND1P14 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 14 . . . . . . . . . . . MTND1P15 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 15 . . . . . . . . . . . MTND1P16 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 16 . . . . . . . . . . . MTND1P17 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 17 . . . . . . . . . . . MTND1P18 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 18 . . . . . . . . . . . MTND1P19 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 19 . . . . . . . . . . . MTND1P20 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 20 . . . . . . . . . . . MTND1P21 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 21 . . . . . . . . . . . MTND1P22 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 22 . . . . . . . . . . . MTND1P23 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 23 . . . . . . . . . . . MTND1P24 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 24 . . . . . . . . . . . MTND1P25 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 25 . . . . . . . . . . . MTND1P26 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 26 . . . . . . . . . . . MTND1P27 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 27 . . . . . . . . . . . MTND1P28 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 28 . . . . . . . . . . . MTND1P29 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 29 . . . . . . . . . . . MTND1P30 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 30 . . . . . . . . . . . MTND1P31 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 31 . . . . . . . . . . . MTND1P32 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 32 . . . . . . . . . . . MTND1P33 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 33 . . . . . . . . . . . MTND1P34 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 34 . . . . . . . . . . . MTND1P35 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 35 . . . . . . . . . . . MTND1P36 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 pseudogene 36 . . . . . . . . . . . MTND2P1 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 1 . . . . . . . . . . . MTND2P2 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 2 . . . . . . . . . . . MTND2P3 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 3 . . . . . . . . . . . MTND2P4 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 4 . . . . . . . . . . . MTND2P5 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 5 . . . . . . . . . . . MTND2P6 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 6 . . . . . . . . . . . MTND2P7 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 7 . . . . . . . . . . . MTND2P8 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 8 . . . . . . . . . . . MTND2P9 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 9 . . . . . . . . . . . MTND2P10 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 10 . . . . . . . . . . . MTND2P11 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 11 . . . . . . . . . . . MTND2P12 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 12 . . . . . . . . . . . MTND2P13 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 13 . . . . . . . . . . . MTND2P14 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 14 . . . . . . . . . . . MTND2P15 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 15 . . . . . . . . . . . MTND2P16 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 16 . . . . . . . . . . . MTND2P17 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 17 . . . . . . . . . . . MTND2P18 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 18 . . . . . . . . . . . MTND2P19 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 19 . . . . . . . . . . . MTND2P20 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 20 . . . . . . . . . . . MTND2P21 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 21 . . . . . . . . . . . MTND2P22 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 22 . . . . . . . . . . . MTND2P23 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 23 . . . . . . . . . . . MTND2P24 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 24 . . . . . . . . . . . MTND2P25 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 25 . . . . . . . . . . . MTND2P26 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 26 . . . . . . . . . . . MTND2P27 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 27 . . . . . . . . . . . MTND2P28 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 28 . . . . . . . . . . . MTND2P29 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 29 . . . . . . . . . . . MTND2P30 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 30 . . . . . . . . . . . MTND2P31 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 31 . . . . . . . . . . . MTND2P32 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 32 . . . . . . . . . . . MTND2P33 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 33 . . . . . . . . . . . MTND2P34 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 34 . . . . . . . . . . . MTND2P35 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 35 . . . . . . . . . . . MTND2P36 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 36 . . . . . . . . . . . MTND2P37 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 37 . . . . . . . . . . . MTND2P38 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 38 . . . . . . . . . . . MTND2P39 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 39 . . . . . . . . . . . MTND2P40 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 pseudogene 40 . . . . . . . . . . . MTND3P1 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 1 . . . . . . . . . . . MTND3P2 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 2 . . . . . . . . . . . MTND3P3 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 3 . . . . . . . . . . . MTND3P4 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 4 . . . . . . . . . . . MTND3P5 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 5 . . . . . . . . . . . MTND3P6 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 6 . . . . . . . . . . . MTND3P7 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 7 . . . . . . . . . . . MTND3P8 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 8 . . . . . . . . . . . MTND3P9 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 9 . . . . . . . . . . . MTND3P10 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 10 . . . . . . . . . . . MTND3P11 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 11 . . . . . . . . . . . MTND3P12 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 12 . . . . . . . . . . . MTND3P13 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 13 . . . . . . . . . . . MTND3P14 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 14 . . . . . . . . . . . MTND3P15 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 15 . . . . . . . . . . . MTND3P16 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 16 . . . . . . . . . . . MTND3P17 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 17 . . . . . . . . . . . MTND3P18 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 18 . . . . . . . . . . . MTND3P19 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 19 . . . . . . . . . . . MTND3P20 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 20 . . . . . . . . . . . MTND3P21 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 21 . . . . . . . . . . . MTND3P22 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 22 . . . . . . . . . . . MTND3P23 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 23 . . . . . . . . . . . MTND3P24 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 24 . . . . . . . . . . . MTND3P25 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 3 pseudogene 25 . . . . . . . . . . . MTND4LP1 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 1 . . . . . . . . . . . MTND4LP2 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 2 . . . . . . . . . . . MTND4LP3 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 3 . . . . . . . . . . . MTND4LP4 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 4 . . . . . . . . . . . MTND4LP5 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 5 . . . . . . . . . . . MTND4LP6 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 6 . . . . . . . . . . . MTND4LP7 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 7 . . . . . . . . . . . MTND4LP8 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 8 . . . . . . . . . . . MTND4LP9 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 9 . . . . . . . . . . . MTND4LP10 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 10 . . . . . . . . . . . MTND4LP11 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 11 . . . . . . . . . . . MTND4LP12 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 12 . . . . . . . . . . . MTND4LP13 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 13 . . . . . . . . . . . MTND4LP14 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 14 . . . . . . . . . . . MTND4LP15 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 15 . . . . . . . . . . . MTND4LP16 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 16 . . . . . . . . . . . MTND4LP17 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 17 . . . . . . . . . . . MTND4LP18 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 18 . . . . . . . . . . . MTND4LP19 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 19 . . . . . . . . . . . MTND4LP20 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 20 . . . . . . . . . . . MTND4LP21 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 21 . . . . . . . . . . . MTND4LP22 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 22 . . . . . . . . . . . MTND4LP23 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 23 . . . . . . . . . . . MTND4LP24 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 24 . . . . . . . . . . . MTND4LP25 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 25 . . . . . . . . . . . MTND4LP26 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 26 . . . . . . . . . . . MTND4LP27 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 27 . . . . . . . . . . . MTND4LP28 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 28 . . . . . . . . . . . MTND4LP29 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 29 . . . . . . . . . . . MTND4LP30 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 30 . . . . . 0.13922 . . . . . MTND4LP31 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4L pseudogene 31 . . . . . . . . . . . MTND4P1 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 1 . . . . . . . . . . . MTND4P2 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 2 . . . . . . . . . . . MTND4P3 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 3 . . . . . . . . . . . MTND4P4 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 4 . . . . . . . . . . . MTND4P5 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 5 . . . . . . . . . . . MTND4P6 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 6 . . . . . . . . . . . MTND4P7 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 7 . . . . . . . . . . . MTND4P8 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 8 . . . . . . . . . . . MTND4P9 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 9 . . . . . . . . . . . MTND4P10 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 10 . . . . . . . . . . . MTND4P11 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 11 . . . . . . . . . . . MTND4P12 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 12 . . . . . . . . . . . MTND4P13 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 13 . . . . . . . . . . . MTND4P14 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 14 . . . . . . . . . . . MTND4P15 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 15 . . . . . . . . . . . MTND4P16 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 16 . . . . . . . . . . . MTND4P17 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 17 . . . . . . . . . . . MTND4P18 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 18 . . . . . . . . . . . MTND4P19 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 19 . . . . . . . . . . . MTND4P20 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 20 . . . . . . . . . . . MTND4P21 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 21 . . . . . . . . . . . MTND4P22 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 22 . . . . . . . . . . . MTND4P23 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 23 . . . . . . . . . . . MTND4P24 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 24 . . . . . . . . . . . MTND4P25 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 25 . . . . . . . . . . . MTND4P26 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 26 . . . . . . . . . . . MTND4P27 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 27 . . . . . . . . . . . MTND4P28 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 28 . . . . . . . . . . . MTND4P29 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 29 . . . . . . . . . . . MTND4P30 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 30 . . . . . . . . . . . MTND4P31 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 31 . . . . . . . . . . . MTND4P32 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 32 . . . . . . . . . . . MTND4P33 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 33 . . . . . . . . . . . MTND4P34 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 34 . . . . . . . . . . . MTND4P35 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 35 . . . . . . . . . . . MTND4P36 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 4 pseudogene 36 . . . . . . . . . . . MTND5P1 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 1 . . . . . . . . . . . MTND5P2 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 2 . . . . . . . . . . . MTND5P3 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 3 . . . . . . . . . . . MTND5P4 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 4 . . . . . . . . . . . MTND5P5 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 5 . . . . . . . . . . . MTND5P6 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 6 . . . . . . . . . . . MTND5P7 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 7 . . . . . . . . . . . MTND5P8 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 8 . . . . . . . . . . . MTND5P9 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 9 . . . . . . . . . . . MTND5P10 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 10 . . . . . . . . . . . MTND5P11 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 11 . . . . . . . . . . . MTND5P12 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 12 . . . . . . . . . . . MTND5P13 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 13 . . . . . . . . . . . MTND5P14 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 14 . . . . . . . . . . . MTND5P15 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 15 . . . . . . . . . . . MTND5P16 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 16 . . . . . . . . . . . MTND5P17 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 17 . . . . . . . . . . . MTND5P18 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 18 . . . . . . . . . . . MTND5P19 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 19 . . . . . . . . . . . MTND5P20 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 20 . . . . . . . . . . . MTND5P21 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 21 . . . . . . . . . . . MTND5P22 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 22 . . . . . . . . . . . MTND5P23 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 23 . . . . . . . . . . . MTND5P24 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 24 . . . . . . . . . . . MTND5P25 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 25 . . . . . . . . . . . MTND5P26 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 26 . . . . . . . . . . . MTND5P27 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 27 . . . . . . . . . . . MTND5P28 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 28 . . . . . . . . . . . MTND5P29 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 29 . . . . . . . . . . . MTND5P30 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 30 . . . . . . . . . . . MTND5P31 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 31 . . . . . . . . . . . MTND5P32 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 32 . . . . . . . . . . . MTND5P33 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 33 . . . . . . . . . . . MTND5P34 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 34 . . . . . . . . . . . MTND5P35 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 35 . . . . . . . . . . . MTND5P36 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 36 . . . . . . . . . . . MTND5P37 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 37 . . . . . . . . . . . MTND5P38 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 38 . . . . . . . . . . . MTND5P39 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 39 . . . . . . . . . . . MTND5P40 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 40 . . . . . . . . . . . MTND5P41 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 5 pseudogene 41 . . . . . . . . . . . MTND6P1 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 1 . . . . . . . . . . . MTND6P2 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 2 . . . . . . . . . . . MTND6P3 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 3 . . . . . . . . . . . MTND6P4 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 4 . . . . . . . . . . . MTND6P5 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 5 . . . . . . . . . . . MTND6P6 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 6 . . . . . . . . . . . MTND6P7 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 7 . . . . . . . . . . . MTND6P8 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 8 . . . . . . . . . . . MTND6P9 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 9 . . . . . . . . . . . MTND6P10 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 10 . . . . . . . . . . . MTND6P11 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 11 . . . . . . . . . . . MTND6P12 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 12 . . . . . . . . . . . MTND6P13 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 13 . . . . . . . . . . . MTND6P14 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 14 . . . . . . . . . . . MTND6P15 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 15 . . . . . . . . . . . MTND6P16 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 16 . . . . . . . . . . . MTND6P17 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 17 . . . . . . . . . . . MTND6P18 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 18 . . . . . . . . . . . MTND6P19 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 19 . . . . . . . . . . . MTND6P20 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 20 . . . . . . . . . . . MTND6P21 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 21 . . . . . . . . . . . MTND6P22 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 22 . . . . . . . . . . . MTND6P23 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 23 . . . . . . . . . . . MTND6P24 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 24 . . . . . . . . . . . MTND6P25 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 25 . . . . . . . . . . . MTND6P26 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 26 . . . . . . . . . . . MTND6P27 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 27 . . . . . . . . . . . MTND6P28 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 28 . . . . . . . . . . . MTND6P29 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 29 . . . . . . . . . . . MTND6P30 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 30 . . . . . . . . . . . MTND6P31 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 31 . . . . . . . . . . . MTND6P32 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 32 . . . . . . . . . . . MTND6P33 . . . mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 6 pseudogene 33 . . . . . . . . . . . MTNR1A 0.00303239205970951 0.588680835306882 0.408286772633408 melatonin receptor 1A FUNCTION: High affinity receptor for melatonin. Likely to mediates the reproductive and circadian actions of melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibit adenylate cyclase activity.; . TISSUE SPECIFICITY: Expressed in hypophyseal pars tuberalis and hypothalamic suprachiasmatic nuclei (SCN). Hippocampus.; . . 0.08459 0.13624 0.220536484 68.38287332 210.0956 3.12779 MTNR1B 0.00870272985599477 0.801025518488245 0.19027175165576 melatonin receptor 1B FUNCTION: High affinity receptor for melatonin. Likely to mediates the reproductive and circadian actions of melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibit adenylate cyclase activity.; . TISSUE SPECIFICITY: Expressed in retina and less in brain and hippocampus.; unclassifiable (Anatomical System); superior cervical ganglion;testis;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.11268 0.13769 -0.021969881 52.14673272 324.5184 3.82947 MTO1 9.81851398890532e-05 0.999328320262741 0.00057349459737014 mitochondrial tRNA translation optimization 1 FUNCTION: Involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs. {ECO:0000269|PubMed:12011058}.; . TISSUE SPECIFICITY: Ubiquitously expressed in various tissues, but with a markedly elevated expression in tissues of high metabolic rates including cochlea. {ECO:0000269|PubMed:12011058}.; smooth muscle;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;urinary;blood;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis;pons; 0.06615 0.16082 -0.198338176 39.17197452 89.78549 2.03827 MTOHR . . . mitochondrially encoded heavy strand origin of replication . . . . . . . . . . . MTOLR . . . mitochondrially encoded light strand origin of replication . . . . . . . . . . . MTOR 0.999999999999676 3.23627074202987e-13 2.27376199784302e-37 mechanistic target of rapamycin FUNCTION: Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals. MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins. Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2). Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E). Moreover, phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein synthesis by modulating the activity of their downstream targets including ribosomal protein S6, eukaryotic translation initiation factor EIF4B, and the inhibitor of translation initiation PDCD4. Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1- mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1- pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex. Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor. In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1. To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A. mTORC1 also negatively regulates autophagy through phosphorylation of ULK1. Under nutrient sufficiency, phosphorylates ULK1 at 'Ser- 758', disrupting the interaction with AMPK and preventing activation of ULK1. Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP. mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor. Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules. As part of the mTORC2 complex MTOR may regulate other cellular processes including survival and organization of the cytoskeleton. Plays a critical role in the phosphorylation at 'Ser-473' of AKT1, a pro-survival effector of phosphoinositide 3-kinase, facilitating its activation by PDK1. mTORC2 may regulate the actin cytoskeleton, through phosphorylation of PRKCA, PXN and activation of the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or RAC1B. mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422'. Regulates osteoclastogensis by adjusting the expression of CEBPB isoforms (By similarity). {ECO:0000250|UniProtKB:Q9JLN9, ECO:0000269|PubMed:12087098, ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12150926, ECO:0000269|PubMed:12231510, ECO:0000269|PubMed:12718876, ECO:0000269|PubMed:14651849, ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15545625, ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:18497260, ECO:0000269|PubMed:18762023, ECO:0000269|PubMed:18925875, ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20537536, ECO:0000269|PubMed:21659604, ECO:0000269|PubMed:23429703, ECO:0000269|PubMed:23429704}.; DISEASE: Smith-Kingsmore syndrome (SKS) [MIM:616638]: An autosomal dominant syndrome characterized by intellectual disability, macrocephaly, seizures, umbilical hernia, and facial dysmorphic features. {ECO:0000269|PubMed:25851998, ECO:0000269|PubMed:26542245}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in numerous tissues, with highest levels in testis. {ECO:0000269|PubMed:12408816, ECO:0000269|PubMed:7809080}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; occipital lobe;testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle;parietal lobe;bone marrow; 0.97466 0.17086 -3.492013613 0.342061807 98.86161 2.15012 MTOR-AS1 . . . MTOR antisense RNA 1 . . . . . . . . . . . MTPAP 0.91057549736558 0.0894188277423309 5.6748920892874e-06 mitochondrial poly(A) polymerase FUNCTION: Polymerase that creates the 3' poly(A) tail of mitochondrial transcripts. Can use all four nucleotides, but has higher activity with ATP and UTP (in vitro). Plays a role in replication-dependent histone mRNA degradation. May be involved in the terminal uridylation of mature histone mRNAs before their degradation is initiated. Might be responsible for the creation of some UAA stop codons which are not encoded in mtDNA. {ECO:0000269|PubMed:15547249, ECO:0000269|PubMed:15769737, ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:20970105, ECO:0000269|PubMed:21292163}.; . TISSUE SPECIFICITY: Ubiquitous, with stronger expression in tissues with high energy requirements: heart, brain, and skeletal muscle. {ECO:0000269|PubMed:15547249}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;ganglion;endometrium;larynx;gum;bone;testis;brain;gall bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;mesenchyma;placenta;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; subthalamic nucleus;trigeminal ganglion;skeletal muscle; 0.08210 0.07339 -0.179930907 40.35739561 83.82931 1.94936 MTPN 0.754654166903489 0.235824956098047 0.00952087699846391 myotrophin FUNCTION: Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity (By similarity). Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy. {ECO:0000250, ECO:0000269|PubMed:10329199, ECO:0000269|PubMed:16895918, ECO:0000269|PubMed:20625546}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10329199}.; . . 0.73968 0.20297 0.079165051 59.43029016 . . MTR 2.84377203137864e-07 0.999992598355724 7.11726707232775e-06 5-methyltetrahydrofolate-homocysteine methyltransferase FUNCTION: Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity). {ECO:0000250}.; DISEASE: Homocystinuria-megaloblastic anemia, cblG complementation type (HMAG) [MIM:250940]: An autosomal recessive inborn error of metabolism resulting from defects in the cobalamin-dependent pathway that converts homocysteine to methionine. It causes delayed psychomotor development, megaloblastic anemia, homocystinuria, and hypomethioninemia. {ECO:0000269|PubMed:8968736, ECO:0000269|PubMed:8968737}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Neural tube defects, folate-sensitive (NTDFS) [MIM:601634]: The most common NTDs are open spina bifida (myelomeningocele) and anencephaly. {ECO:0000269|PubMed:12375236}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Expressed at the highest levels in pancreas, heart, brain, skeletal muscle and placenta. Expressed at lower levels in lung, liver and kidney.; . . 0.69075 0.68662 0.253503589 69.70393961 2789.30502 9.97299 MTRF1 1.54398173133647e-07 0.837961562312085 0.162038283289742 mitochondrial translational release factor 1 FUNCTION: Mitochondrial peptide chain release factor that directs the termination of translation in response to the peptide chain non-cognate termination stop codons AGG and AGA.; . . . . 0.07859 0.09749 0.64123826 83.97617363 508.43448 4.62342 MTRF1L 4.39782481222077e-07 0.215254349071532 0.784745211145987 mitochondrial translational release factor 1 like FUNCTION: Mitochondrial peptide chain release factor that directs the termination of translation in response to the peptide chain termination codons UAA and UAG. {ECO:0000269|PubMed:17803939}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level). {ECO:0000269|PubMed:17803939}.; . . 0.15951 0.11918 0.038710339 56.92380278 1362.06825 6.92643 MTRF1LP1 . . . mitochondrial translational release factor 1 like pseudogene 1 . . . . . . . . . . . MTRF1LP2 . . . mitochondrial translational release factor 1 like pseudogene 2 . . . . . . . . . . . MTRNR2L1 . . . MT-RNR2-like 1 FUNCTION: Plays a role as a neuroprotective and antiapoptotic factor. {ECO:0000250|UniProtKB:Q8IVG9}.; . TISSUE SPECIFICITY: Highly expressed in the kidney, heart muscle and testis. {ECO:0000269|PubMed:19477263}.; . . . . . . 2.7844 0.09973 MTRNR2L2 . . . MT-RNR2-like 2 FUNCTION: Plays a role as a neuroprotective and antiapoptotic factor. {ECO:0000250|UniProtKB:Q8IVG9}.; . TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in kidney, heart, skeletal muscles and brain. {ECO:0000269|PubMed:19477263}.; . . . . . . 22.30248 0.74815 MTRNR2L3 . . . MT-RNR2-like 3 FUNCTION: Plays a role as a neuroprotective and antiapoptotic factor. {ECO:0000250|UniProtKB:Q8IVG9}.; . TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in kidney, heart, skeletal muscles and brain. {ECO:0000269|PubMed:19477263}.; . . . . . . 111.65901 2.30023 MTRNR2L4 . . . MT-RNR2-like 4 FUNCTION: Plays a role as a neuroprotective and antiapoptotic factor. {ECO:0000250|UniProtKB:Q8IVG9}.; . TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in kidney, heart, skeletal muscles and brain. {ECO:0000269|PubMed:19477263}.; . . . . . . . . MTRNR2L5 . . . MT-RNR2-like 5 FUNCTION: Plays a role as a neuroprotective and antiapoptotic factor. {ECO:0000250|UniProtKB:Q8IVG9, ECO:0000269|PubMed:19477263}.; . TISSUE SPECIFICITY: Expressed in testis and brain. {ECO:0000269|PubMed:19477263}.; . . . . . . 1618.50988 7.44165 MTRNR2L6 . . . MT-RNR2-like 6 FUNCTION: Plays a role as a neuroprotective and antiapoptotic factor. {ECO:0000250|UniProtKB:Q8IVG9}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle and testis. {ECO:0000269|PubMed:19477263}.; . . . . . . 4.81382 0.17583 MTRNR2L7 . . . MT-RNR2-like 7 FUNCTION: Plays a role as a neuroprotective and antiapoptotic factor. {ECO:0000250|UniProtKB:Q8IVG9}.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:19477263}.; . . . . . . 7.50054 0.27854 MTRNR2L8 . . . MT-RNR2-like 8 FUNCTION: Plays a role as a neuroprotective and antiapoptotic factor. {ECO:0000250|UniProtKB:Q8IVG9}.; . TISSUE SPECIFICITY: Highly expressed in the kidney, heart muscle and testis. Not expressed in skeletal muscle. {ECO:0000269|PubMed:19477263}.; . . . . . . 1.89325 0.05902 MTRNR2L9 . . . MT-RNR2-like 9 FUNCTION: Plays a role as a neuroprotective and antiapoptotic factor. {ECO:0000250|UniProtKB:Q8IVG9}.; . TISSUE SPECIFICITY: Highly expressed in the kidney, heart muscle and testis. {ECO:0000269|PubMed:19477263}.; . . . . . . 0.6781 0.01089 MTRNR2L10 . . . MT-RNR2-like 10 FUNCTION: Plays a role as a neuroprotective and antiapoptotic factor. {ECO:0000250|UniProtKB:Q8IVG9}.; . TISSUE SPECIFICITY: Expressed in mature brain, thyroid gland and testis. {ECO:0000269|PubMed:19477263}.; . . . . . . 18.73606 0.64647 MTRNR2L11 . . . MT-RNR2-like 11 (pseudogene) FUNCTION: Plays a role as a neuroprotective and antiapoptotic factor. {ECO:0000250|UniProtKB:Q8IVG9}.; . . . . . . . . 1.68591 0.05475 MTRNR2L12 . . . MT-RNR2-like 12 FUNCTION: Plays a role as a neuroprotective and antiapoptotic factor. {ECO:0000250|UniProtKB:Q8IVG9}.; . . . . . . . . 11.63141 0.42175 MTRNR2L13 . . . MT-RNR2-like 13 FUNCTION: Plays a role as a neuroprotective and antiapoptotic factor. {ECO:0000250|UniProtKB:Q8IVG9}.; . . . . . . . . 1.92553 0.06037 MTRNR3 . . . mitochondrially encoded 5S-like sequence . . . . . . . . . . . MTRR 4.10850052026828e-07 0.987986630251082 0.0120129588988662 5-methyltetrahydrofolate-homocysteine methyltransferase reductase FUNCTION: Involved in the reductive regeneration of cob(I)alamin (vitamin B12) cofactor required for the maintenance of methionine synthase in a functional state. Necessary for utilization of methylgroups from the folate cycle, thereby affecting transgenerational epigenetic inheritance. Folate pathway donates methyl groups necessary for cellular methylation and affects different pathways such as DNA methylation, possibly explaining the transgenerational epigenetic inheritance effects. {ECO:0000269|PubMed:17892308}.; DISEASE: Neural tube defects, folate-sensitive (NTDFS) [MIM:601634]: The most common NTDs are open spina bifida (myelomeningocele) and anencephaly. {ECO:0000269|PubMed:10444342, ECO:0000269|PubMed:12375236}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in all tissues tested, particularly abundant in skeletal muscle.; lymphoreticular;ovary;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;ciliary ganglion; 0.03480 0.30511 1.429318999 95.00471809 6235.77022 16.51838 MTSS1 0.999823848176415 0.000176151669719805 1.53865186069616e-10 metastasis suppressor 1 FUNCTION: May be related to cancer progression or tumor metastasis in a variety of organ sites, most likely through an interaction with the actin cytoskeleton.; . TISSUE SPECIFICITY: Expressed in many tissues, including spleen, thymus, prostate, testis, uterus, colon, and peripheral blood. {ECO:0000269|PubMed:12082544}.; myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;larynx;thyroid;testis;germinal center;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;cerebellum; dorsal root ganglion;superior cervical ganglion;fetal brain;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.37107 0.99898 -0.819281839 11.93677754 484.4754 4.53168 MTSS1L 0.86986055007454 0.130124336922377 1.51130030829013e-05 metastasis suppressor 1-like FUNCTION: May function in actin bundling. {ECO:0000269|PubMed:14752106}.; . . smooth muscle;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;larynx;bone;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;blood;lens;lung;placenta;macula lutea;visual apparatus;amnion;head and neck;kidney;mammary gland; superior cervical ganglion;subthalamic nucleus;globus pallidus;skeletal muscle;parietal lobe;cerebellum; . 0.12220 -1.548724932 3.273177636 236.86198 3.32283 MTTAS . . . mitochondrially encoded termination associate sequence . . . . . . . . . . . MTTER . . . mitochondrially encoded transcription terminator . . . . . . . . . . . MTTFH . . . mitochondrially encoded transcription factor binding site H . . . . . . . . . . . MTTFL . . . mitochondrially encoded transcription factor binding site L . . . . . . . . . . . MTTFX . . . mitochondrially encoded transcription factor binding site X . . . . . . . . . . . MTTFY . . . mitochondrially encoded transcription factor binding site Y . . . . . . . . . . . MTTP 0.0125833671870721 0.987353372328962 6.32604839653909e-05 microsomal triglyceride transfer protein FUNCTION: Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces (PubMed:23475612, PubMed:8939939, PubMed:26224785, PubMed:25108285, PubMed:22236406). Required for the secretion of plasma lipoproteins that contain apolipoprotein B (PubMed:23475612, PubMed:8939939, PubMed:26224785). {ECO:0000269|PubMed:22236406, ECO:0000269|PubMed:23475612, ECO:0000269|PubMed:25108285, ECO:0000269|PubMed:26224785, ECO:0000269|PubMed:8939939}.; DISEASE: Abetalipoproteinemia (ABL) [MIM:200100]: An autosomal recessive disorder of lipoprotein metabolism. Affected individuals produce virtually no circulating apolipoprotein B-containing lipoproteins (chylomicrons, VLDL, LDL, lipoprotein(A)). Malabsorption of the antioxidant vitamin E occurs, leading to spinocerebellar and retinal degeneration. {ECO:0000269|PubMed:10679949, ECO:0000269|PubMed:10946006, ECO:0000269|PubMed:22236406, ECO:0000269|PubMed:23475612, ECO:0000269|PubMed:25108285, ECO:0000269|PubMed:26224785, ECO:0000269|PubMed:8939939}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver and small intestine. Also found in ovary, testis and kidney. {ECO:0000269|PubMed:7961826}.; unclassifiable (Anatomical System);small intestine;colon;fovea centralis;skeletal muscle;prostate;macula lutea;liver;testis;spleen;kidney;artery;brain;aorta; ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.36424 0.44963 1.42749112 94.99292286 5043.47891 14.52475 MTURN . . . maturin, neural progenitor differentiation regulator homolog (Xenopus) FUNCTION: May be involved in early neuronal development. {ECO:0000250}.; . . . . 0.13842 . 0.013025609 54.62962963 5.36859 0.19924 MTUS1 1.1438280194915e-05 0.999473951936987 0.000514609782818489 microtubule associated tumor suppressor 1 FUNCTION: Cooperates with AGTR2 to inhibit ERK2 activation and cell proliferation. May be required for AGTR2 cell surface expression. Together with PTPN6, induces UBE2V2 expression upon angiotensin-II stimulation. Isoform 1 inhibits breast cancer cell proliferation, delays the progression of mitosis by prolonging metaphase and reduces tumor growth. {ECO:0000269|PubMed:12692079, ECO:0000269|PubMed:19794912}.; DISEASE: Hepatocellular carcinoma (HCC) [MIM:114550]: A primary malignant neoplasm of epithelial liver cells. The major risk factors for HCC are chronic hepatitis B virus (HBV) infection, chronic hepatitis C virus (HCV) infection, prolonged dietary aflatoxin exposure, alcoholic cirrhosis, and cirrhosis due to other causes. {ECO:0000269|PubMed:16650523}. Note=The gene represented in this entry may be involved in disease pathogenesis.; TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). Highly expressed in brain. Down-regulated in ovarian carcinoma, pancreas carcinoma, colon carcinoma and head and neck squamous cell carcinoma (HNSCC). Isoform 1 is the major isoform in most peripheral tissues. Isoform 2 is abundant in most peripheral tissues. Isoform 3 is the major isoform in brain, female reproductive tissues, thyroid and heart. Within brain it is highly expressed in corpus callosum and pons. Isoform 6 is brain- specific, it is the major isoform in cerebellum and fetal brain. {ECO:0000269|PubMed:10697957, ECO:0000269|PubMed:12692079, ECO:0000269|PubMed:15123706, ECO:0000269|PubMed:16270321, ECO:0000269|PubMed:16887298, ECO:0000269|PubMed:16969489, ECO:0000269|PubMed:17656251}.; lymphoreticular;medulla oblongata;ovary;skin;retina;prostate;optic nerve;frontal lobe;ganglion;endometrium;thyroid;bladder;brain;heart;cartilage;tongue;pineal body;urinary;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;vein;whole body;larynx;bone;testis;artery;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; medulla oblongata;superior cervical ganglion;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;spinal cord;caudate nucleus;skeletal muscle;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.16371 0.10477 2.096551086 97.87096013 1447.42658 7.09602 MTUS2 0.330673093548944 0.669299788389221 2.71180618352002e-05 microtubule associated tumor suppressor candidate 2 FUNCTION: Binds microtubules. Together with MAPRE1 may target the microtubule depolymerase KIF2C to the plus-end of microtubules. May regulate the dynamics of microtubules at their growing distal tip. {ECO:0000269|PubMed:19543227}.; . TISSUE SPECIFICITY: Detected in embryonic stem cells differentiating to cardiomyocytes. {ECO:0000269|PubMed:19806667}.; unclassifiable (Anatomical System);myocardium;pancreas;lung;heart;brain;skeletal muscle; prefrontal cortex;cingulate cortex; 0.10856 . 0.527183578 80.58504364 1047.45515 6.21264 MTUS2-AS1 . . . MTUS2 antisense RNA 1 . . . cervix; . . . . . . . MTUS2-AS2 . . . MTUS2 antisense RNA 2 . . . . . . . . . . . MTX1 0.198221290051836 0.7915101129951 0.0102685969530647 metaxin 1 FUNCTION: Involved in transport of proteins into the mitochondrion. Essential for embryonic development (By similarity). {ECO:0000250}.; . . ovary;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;muscle;adrenal cortex;lens;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.29766 0.09818 . . 105.73081 2.22842 MTX1P1 . . . metaxin 1 pseudogene 1 . . . . . . . . . . . MTX2 0.0813718081793007 0.908198261911208 0.010429929909491 metaxin 2 FUNCTION: Involved in transport of proteins into the mitochondrion. {ECO:0000269|PubMed:10381257}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;atrium;whole body;cochlea;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; amygdala;occipital lobe;medulla oblongata;thalamus;testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle;parietal lobe; 0.19209 0.11454 0.058937498 58.26256192 116.70844 2.35068 MTX3 0.10035111705881 0.865704468111771 0.033944414829419 metaxin 3 FUNCTION: Could function in transport of proteins into the mitochondrion. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;skeletal muscle;skin;retina;uterus;whole body;lung;hippocampus;liver;testis;kidney;mammary gland;brain; . 0.30585 0.10254 0.505321956 80.00707714 861.67074 5.72574 MUC1 0.730964975196719 0.268475369314863 0.000559655488418492 mucin 1, cell surface associated FUNCTION: The alpha subunit has cell adhesive properties. Can act both as an adhesion and an anti-adhesion protein. May provide a protective layer on epithelial cells against bacterial and enzyme attack.; DISEASE: Note=MUC1/CA 15-3 is used as a serological clinical marker of breast cancer to monitor response to breast cancer treatment and disease recurrence (PubMed:20816948). Decreased levels over time may be indicative of a positive response to treatment. Conversely, increased levels may indicate disease progression. At an early stage disease, only 21% of patients exhibit high MUC1/CA 15-3 levels, that is why CA 15-3 is not a useful screening test. Most antibodies target the highly immunodominant core peptide domain of 20 amino acid (APDTRPAPGSTAPPAHGVTS) tandem repeats. Some antibodies recognize glycosylated epitopes. {ECO:0000269|PubMed:20816948}.; DISEASE: Medullary cystic kidney disease 1 (MCKD1) [MIM:174000]: A form of tubulointerstitial nephropathy characterized by formation of renal cysts at the corticomedullary junction. It is characterized by adult onset of impaired renal function and salt wasting resulting in end-stage renal failure by the sixth decade. {ECO:0000269|PubMed:23396133}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed on the apical surface of epithelial cells, especially of airway passages, breast and uterus. Also expressed in activated and unactivated T-cells. Overexpressed in epithelial tumors, such as breast or ovarian cancer and also in non-epithelial tumor cells. Isoform 7 is expressed in tumor cells only. {ECO:0000269|PubMed:15513966, ECO:0000269|PubMed:9212228}.; myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;larynx;bone;testis;germinal center;bladder;brain;gall bladder;unclassifiable (Anatomical System);trophoblast;lymph node;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;fetal lung;kidney;atrioventricular node;trigeminal ganglion; 0.02475 0.07165 . . 124.93626 2.42999 MUC2 4.54632231934197e-05 0.999954536577177 1.99629886229882e-10 mucin 2, oligomeric mucus/gel-forming FUNCTION: Coats the epithelia of the intestines, airways, and other mucus membrane-containing organs. Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces. Major constituent of both the inner and outer mucus layers of the colon and may play a role in excluding bacteria from the inner mucus layer. {ECO:0000269|PubMed:19432394}.; . TISSUE SPECIFICITY: Colon, small intestine, colonic tumors, bronchus, cervix and gall bladder.; unclassifiable (Anatomical System);colon;blood;skeletal muscle;stomach;bone marrow; superior cervical ganglion;atrioventricular node; 0.12651 . . . 13226.52773 24.78411 MUC3A . . . mucin 3A, cell surface associated FUNCTION: Major glycoprotein component of a variety of mucus gels. Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces. May be involved in ligand binding and intracellular signaling. {ECO:0000269|PubMed:10405327}.; . TISSUE SPECIFICITY: Broad specificity; small intestine, colon, colonic tumors, heart, liver, thymus, prostate, pancreas and gall bladder. {ECO:0000269|PubMed:11289722}.; unclassifiable (Anatomical System);hypopharynx;colon;mammary gland; dorsal root ganglion;prostate;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; . . . . 4720.00036 13.87692 MUC3B . . . mucin 3B, cell surface associated FUNCTION: Major glycoprotein component of a variety of mucus gels. Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Fetal and adult small intestine and fetal and adult colon. {ECO:0000269|PubMed:10973822, ECO:0000269|PubMed:11289722}.; . . . . . . . . MUC4 . . . mucin 4, cell surface associated FUNCTION: May play a role in tumor progression. Ability to promote tumor growth may be mainly due to repression of apoptosis as opposed to proliferation. Has anti-adhesive properties. Seems to alter cellular behavior through both anti-adhesive effects on cell-cell and cell-extracellular matrix interactions and in its ability to act as an intramembrane ligand for ERBB2. Plays an important role in cell proliferation and differentiation of epithelial cells by inducing specific phosphorylation of ERBB2. The MUC4-ERBB2 complex causes site-specific phosphorylation of the ERBB2 'Tyr-1248'. In polarized epithelilal cells segragates ERBB2 and other ERBB receptors and prevents ERBB2 from acting as a coreceptor. The interaction with ERBB2 leads to enhanced expression of CDKN1B. The formation of a MUC4-ERBB2-ERBB3-NRG1 complex leads to down-regulation of CDKN1B, resulting in repression of apoptosis and stimulation of proliferation. {ECO:0000269|PubMed:12102554, ECO:0000269|PubMed:16049287, ECO:0000269|PubMed:16814944, ECO:0000269|PubMed:16914178}.; . TISSUE SPECIFICITY: Expressed in the thymus, thyroid, lung, trachea, esophagus, stomach, small intestine, colon, testis, prostate, ovary, uterus, placenta, and mammary and salivary glands. Expressed in carcinomas arising from some of these epithelia, such as lung cancers, squamous cell carcinomas of the upper aerodigestive tract, mammary carcinomas, biliary tract, colon, and cervix cancers. Minimally or not expressed in the normal pancreas or chronic pancreatitis, but is highly expressed in pancreatic tumors and pancreatic tumor cell lines. {ECO:0000269|PubMed:10024507, ECO:0000269|PubMed:10880978, ECO:0000269|PubMed:10920259, ECO:0000269|PubMed:16814944}.; unclassifiable (Anatomical System);tongue;colon;skeletal muscle;uterus;prostate;lung;endometrium;larynx;nasopharynx;thyroid;placenta;visual apparatus;hypopharynx;cervix;head and neck;germinal center;kidney;brain;stomach; prostate;superior cervical ganglion;trachea;trigeminal ganglion;skeletal muscle; 0.37408 . 6.320387277 99.8643548 14250.21522 26.01128 MUC5AC . . . mucin 5AC, oligomeric mucus/gel-forming FUNCTION: Gel-forming glycoprotein of gastric and respiratoy tract epithelia that protects the mucosa from infection and chemical damage by binding to inhaled microrganisms and particles that are subsequently removed by the mucocilary system.; . TISSUE SPECIFICITY: Highly expressed in surface mucosal cells of respiratory tract and stomach epithelia. Overexpressed in a number of carcinomas. Also expressed in Barrett's esophagus epithelium and in the proximal duodenum. {ECO:0000269|PubMed:14535999, ECO:0000269|PubMed:7513696}.; unclassifiable (Anatomical System);pancreas;colon;kidney;stomach; . 0.15646 . . . 993.41134 6.07467 MUC5B 0.999999706471312 2.93528688420844e-07 6.11965786257582e-25 mucin 5B, oligomeric mucus/gel-forming FUNCTION: Gel-forming mucin that is thought to contribute to the lubricating and viscoelastic properties of whole saliva and cervical mucus.; DISEASE: Pulmonary fibrosis, idiopathic (IPF) [MIM:178500]: A lung disease characterized by shortness of breath, radiographically evident diffuse pulmonary infiltrates, and varying degrees of inflammation and fibrosis on biopsy. In some cases, the disorder can be rapidly progressive and characterized by sequential acute lung injury with subsequent scarring and end-stage lung disease. {ECO:0000269|PubMed:21506741, ECO:0000269|PubMed:21506748}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. A common polymorphism in the promoter of MUC5B is associated with familial interstitial pneumonia and idiopathic pulmonary fibrosis, suggesting that dysregulated MUC5B expression in the lung may be involved in the pathogenesis of pulmonary fibrosis (PubMed:21506741). {ECO:0000269|PubMed:21506741}.; TISSUE SPECIFICITY: Expressed on surface airway epithelia. Expressed mainly in mucous cells of submucosal glands of airway tissues. Highly expressed in the sublingual gland. Also found in submaxillary glands, endocervix, gall bladder, and pancreas. {ECO:0000269|PubMed:11713095, ECO:0000269|PubMed:8554565, ECO:0000269|PubMed:9147051, ECO:0000269|PubMed:9164870}.; unclassifiable (Anatomical System);ovary;tongue;islets of Langerhans;colon;breast;pancreas;lung;trachea;endometrium;larynx;thyroid;head and neck;cervix;mammary gland;stomach; superior cervical ganglion;trachea;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07831 . 16.52445195 99.97640953 6531.39188 16.99148 MUC6 1.08683766450872e-32 4.75108941711418e-05 0.999952489105829 mucin 6, oligomeric mucus/gel-forming FUNCTION: May provide a mechanism for modulation of the composition of the protective mucus layer related to acid secretion or the presence of bacteria and noxious agents in the lumen. Plays an important role in the cytoprotection of epithelial surfaces and are used as tumor markers in a variety of cancers. May play a role in epithelial organogenesis. {ECO:0000269|PubMed:10209489, ECO:0000269|PubMed:10330458, ECO:0000269|PubMed:11988092}.; . TISSUE SPECIFICITY: Expressed in the regenerative zone of gastric antrum, gastric body mucosa and gastric incisura mucosa. Expressed in the deeper mucous glands of gastric antrum. Overexpressed in Helicobacter pylori infected gastric epithelium. Highly expressed in duodenal Brunner's glands, gall bladder, seminal vesicle, pancreatic centroacinar cells and ducts, and periductal glands of the common bile duct. {ECO:0000269|PubMed:10209489, ECO:0000269|PubMed:10330458, ECO:0000269|PubMed:11988092, ECO:0000269|PubMed:15280409, ECO:0000269|PubMed:9422745}.; . . 0.16113 0.17704 1.26225728 93.56569946 5602.29835 15.48599 MUC7 9.13857519573247e-05 0.338220138032117 0.661688476215926 mucin 7, secreted FUNCTION: May function in a protective capacity by promoting the clearance of bacteria in the oral cavity and aiding in mastication, speech, and swallowing. Binds P.aeruginosa pili. {ECO:0000269|PubMed:11378823, ECO:0000269|PubMed:8104046}.; DISEASE: Asthma (ASTHMA) [MIM:600807]: The most common chronic disease affecting children and young adults. It is a complex genetic disorder with a heterogeneous phenotype, largely attributed to the interactions among many genes and between these genes and the environment. It is characterized by recurrent attacks of paroxysmal dyspnea, with wheezing due to spasmodic contraction of the bronchi. {ECO:0000269|PubMed:11378823}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in salivary gland tissues and only in those that contain mucous acinar cells (e.g. sublingual and submandibular glands) and not in salivary glands containing only serous acinar cells (e.g. parotid gland). {ECO:0000269|PubMed:1445223, ECO:0000269|PubMed:7690757}.; unclassifiable (Anatomical System);lung;heart;adrenal gland;thyroid;adrenal cortex;parathyroid;spleen;pineal gland;skeletal muscle; superior cervical ganglion;prostate;trachea;salivary gland;thyroid;liver; 0.05901 0.13341 2.462184029 98.58457183 2234.27781 8.71039 MUC8 . . . mucin 8 . . . . . 0.13360 . . . 12799.77951 24.28002 MUC12 . . . mucin 12, cell surface associated FUNCTION: Involved in epithelial cell protection, adhesion modulation, and signaling. May be involved in epithelial cell growth regulation. Stimulated by both cytokine TNF-alpha and TGF- beta in intestinal epithelium. {ECO:0000269|PubMed:17058067}.; . TISSUE SPECIFICITY: Ubiquitous, with higher expression in colon. Down-regulated in colorectal cancer as well as in the colon of patients with ulcerative colitis (UC) and Crohn's disease (CD). {ECO:0000269|PubMed:10463611, ECO:0000269|PubMed:17058067}.; unclassifiable (Anatomical System);heart;ovary;salivary gland;sympathetic chain;intestine;pharynx;colon;blood;skin;uterus;prostate;lung;cornea;visual apparatus;liver;kidney;brain;mammary gland; superior cervical ganglion;ciliary ganglion;kidney; 0.09711 . . . 8273.45926 19.64989 MUC13 0.0251339159380931 0.961757148451379 0.0131089356105282 mucin 13, cell surface associated FUNCTION: Epithelial and hemopoietic transmembrane mucin that may play a role in cell signaling.; . TISSUE SPECIFICITY: Highly expressed in epithelial tissues, particularly those of the gastrointestinal and respiratory tracts, such as large intestine and trachea, followed by kidney, small intestine, appendix and stomach. {ECO:0000269|PubMed:11278439}.; unclassifiable (Anatomical System);small intestine;ovary;colon;skeletal muscle;bile duct;pancreas;lung;endometrium;bone;liver;kidney;brain;stomach; trigeminal ganglion; 0.01493 0.04178 . . 629.1592 5.05568 MUC15 3.93192149563272e-05 0.384754928046934 0.615205752738109 mucin 15, cell surface associated FUNCTION: May play a role in the cell adhesion to the extracellular matrix.; . TISSUE SPECIFICITY: Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocyte, bone marrow, lymph node and lung. {ECO:0000269|PubMed:12047385}.; unclassifiable (Anatomical System);heart;ovary;parathyroid;skin;uterus;prostate;lung;placenta;hippocampus;liver;pituitary gland;testis;spleen;kidney;brain; dorsal root ganglion;superior cervical ganglion;placenta;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10577 0.09834 0.705562627 85.52724699 67.58957 1.70060 MUC16 . . . mucin 16, cell surface associated FUNCTION: Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in corneal and conjunctival epithelia (at protein level). Overexpressed in ovarian carcinomas and ovarian low malignant potential (LMP) tumors as compared to the expression in normal ovarian tissue and ovarian adenomas. {ECO:0000269|PubMed:11369781, ECO:0000269|PubMed:12218296, ECO:0000269|PubMed:16384952}.; . . 0.05884 . 29.75317221 100 23894.83454 31.77381 MUC17 . . . mucin 17, cell surface associated FUNCTION: Probably plays a role in maintaining homeostasis on mucosal surfaces. {ECO:0000269|PubMed:17990980}.; . TISSUE SPECIFICITY: Expressed almost exclusively in the intestine. Expression is especially high in both the duodenum and transverse colon. Expressed in mature absorptive cells of the small intestinal villi. No expression is detected in goblet cells. Highly expressed in pancreatic adenocarcinoma tissue (at protein level). Expression is not detectable in normal pancreas, in pancreatitis or in cell lines derived from other cancers. {ECO:0000269|PubMed:11855812, ECO:0000269|PubMed:16737958, ECO:0000269|PubMed:9299468}.; unclassifiable (Anatomical System);pancreas;colon;skeletal muscle;stomach; dorsal root ganglion;ciliary ganglion;trigeminal ganglion; 0.01571 . 16.94869906 99.98230715 4366.26914 13.19122 MUC19 . . . mucin 19, oligomeric FUNCTION: May function in ocular mucus homeostasis. {ECO:0000269|PubMed:18184611}.; . TISSUE SPECIFICITY: Expressed corneal epithelial cells, conjunctival goblet and epithelial cells and lacrimal gland cells (at protein level). Expressed by mucous cells of the submandibular gland and submucosal gland of the trachea. Expressed by middle ear epithelial cells. {ECO:0000269|PubMed:12882755, ECO:0000269|PubMed:17667140, ECO:0000269|PubMed:18184611}.; . . 0.11557 . . . 41933.48624 39.90294 MUC20 . . . mucin 20, cell surface associated FUNCTION: May regulate MET signaling cascade. Seems to decrease hepatocyte growth factor (HGF)-induced transient MAPK activation. Blocks GRB2 recruitment to MET thus suppressing the GRB2-RAS pathway. Inhibits HGF-induced proliferation of MMP1 and MMP9 expression. {ECO:0000269|PubMed:15314156}.; . TISSUE SPECIFICITY: Highly expressed in kidney, moderately in placenta, lung, prostate, liver, and digestive system. In the kidney, localized in the proximal tubules but not in the glomerulus or distal tubules. Detected in most of the male urogenital tract epithelia, with the exception of epididymis. {ECO:0000269|PubMed:14565953, ECO:0000269|PubMed:16997931}.; ovary;developmental;colon;skin;retina;uterus;prostate;optic nerve;endometrium;testis;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;stomach; . . 0.05395 . . 2482.91489 9.29408 MUC20P1 . . . mucin 20, cell surface associated pseudogene 1 . . . . . . . . . . . MUC21 0.331419151101163 0.606016804582376 0.0625640443164608 mucin 21, cell surface associated . . TISSUE SPECIFICITY: Expressed in lung, large intestine, thymus, and testis. Expressed in normal and malignant bronchial epithelial cells. {ECO:0000269|PubMed:17977904}.; . . 0.06345 . 2.443759208 98.56098136 1799.23935 7.82391 MUC22 . . . mucin 22 . . TISSUE SPECIFICITY: Expressed in lung by serous cells of the submucosal gland (at protein level). Detected in the placenta, lung and testis. {ECO:0000269|PubMed:20981447}.; . . . . . . 35553.29937 36.89264 MUCL1 1.14812282999876e-05 0.206715199057216 0.793273319714484 mucin like 1 FUNCTION: May play a role as marker for the diagnosis of metastatic breast cancer. {ECO:0000269|PubMed:12019145, ECO:0000269|PubMed:12595743, ECO:0000269|PubMed:15684711}.; . TISSUE SPECIFICITY: Expressed in mammary, salivary glands and prostate. Also detected in lung. Mainly expressed in cancer cell lines of breast origin. Highly expressed in lymph node-positive compared with node-negative tumors. Detected in all lymph node containing metastatic cells. {ECO:0000269|PubMed:12019145, ECO:0000269|PubMed:12595743, ECO:0000269|PubMed:15096563}.; unclassifiable (Anatomical System);breast;heart;placenta;hypopharynx;head and neck;mammary gland;skin;skeletal muscle; . 0.03884 . -0.163345027 41.24793583 6.09954 0.23051 MUL1 3.48969973575906e-06 0.350442133807748 0.649554376492517 mitochondrial E3 ubiquitin protein ligase 1 FUNCTION: Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. The function may implicate its ability to sumoylate DNM1L. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response. Can mediate DDX58 sumoylation and disrupt its polyubiquitination. {ECO:0000269|PubMed:18207745, ECO:0000269|PubMed:18213395, ECO:0000269|PubMed:18591963, ECO:0000269|PubMed:19407830, ECO:0000269|PubMed:22410793, ECO:0000269|PubMed:23399697}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in the heart, skeletal muscle, placenta, kidney and liver. Barely detectable in colon and thymus. {ECO:0000269|PubMed:18213395, ECO:0000269|PubMed:18591963}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; skeletal muscle; 0.15498 0.12243 0.020302773 55.60863411 104.01635 2.20437 MUM1 0.032092632530893 0.967523953543619 0.000383413925487492 melanoma associated antigen (mutated) 1 FUNCTION: Involved in the DNA damage response pathway by contributing to the maintenance of chromatin architecture. Recruited to the vicinity of DNA breaks by TP53BP1 and plays an accessory role to facilitate damage-induced chromatin changes and promoting chromatin relaxation. Required for efficient DNA repair and cell survival following DNA damage. {ECO:0000269|PubMed:20347427}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;oesophagus;endometrium;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;hippocampus;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;occipital lobe;medulla oblongata;caudate nucleus;atrioventricular node;pons;subthalamic nucleus;testis - seminiferous tubule;testis;globus pallidus;trigeminal ganglion;parietal lobe; 0.07150 0.13329 -0.661316159 16.02382637 285.13749 3.61395 MUM1L1 0.635560374421233 0.357641219906586 0.0067984056721807 melanoma associated antigen (mutated) 1-like 1 . . . unclassifiable (Anatomical System);medulla oblongata;heart;ovary;parathyroid;skeletal muscle;skin;uterus;prostate;lung;placenta;liver;testis; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node; 0.08614 . 0.240763792 69.36777542 20.88173 0.70641 MUPP . . . major urinary protein, pseudogene . . . . . . . . . . . MURC 3.72846528183563e-07 0.106874150023717 0.893125477129755 muscle-related coiled-coil protein FUNCTION: Induces RHOA activation and activates NPPA transcription and myofibrillar organization through the Rho/ROCK signaling pathway. {ECO:0000269|PubMed:18332105}.; . . unclassifiable (Anatomical System);ovary;heart;placenta;parathyroid;skeletal muscle;retina; . . . -0.312207497 32.05944798 150.4094 2.67661 MUS81 1.5772598767523e-06 0.9913231066052 0.00867531613492383 MUS81 structure-specific endonuclease subunit FUNCTION: Interacts with EME1 and EME2 to form a DNA structure- specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks. {ECO:0000269|PubMed:11741546, ECO:0000269|PubMed:12374758, ECO:0000269|PubMed:12686547, ECO:0000269|PubMed:12721304, ECO:0000269|PubMed:14617801, ECO:0000269|PubMed:15805243, ECO:0000269|PubMed:17289582, ECO:0000269|PubMed:19595721, ECO:0000269|PubMed:19596235}.; . TISSUE SPECIFICITY: Widely expressed.; medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.62476 0.18734 0.778977686 87.21396556 6006.78657 16.18304 MUSK 8.17346413889496e-05 0.999172309707052 0.000745955651558853 muscle, skeletal, receptor tyrosine kinase FUNCTION: Receptor tyrosine kinase which plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between the motor neuron and the skeletal muscle (PubMed:25537362). Recruitment of AGRIN by LRP4 to the MUSK signaling complex induces phosphorylation and activation of MUSK, the kinase of the complex. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. May regulate AChR phosphorylation and clustering through activation of ABL1 and Src family kinases which in turn regulate MUSK. DVL1 and PAK1 that form a ternary complex with MUSK are also important for MUSK-dependent regulation of AChR clustering. May positively regulate Rho family GTPases through FNTA. Mediates the phosphorylation of FNTA which promotes prenylation, recruitment to membranes and activation of RAC1 a regulator of the actin cytoskeleton and of gene expression. Other effectors of the MUSK signaling include DNAJA3 which functions downstream of MUSK. May also play a role within the central nervous system by mediating cholinergic responses, synaptic plasticity and memory formation (By similarity). {ECO:0000250, ECO:0000269|PubMed:25537362}.; DISEASE: Myasthenic syndrome, congenital, 9, associated with acetylcholine receptor deficiency (CMS9) [MIM:616325]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS9 is a disorder of postsynaptic neuromuscular transmission, due to deficiency of AChR at the endplate that results in low amplitude of the miniature endplate potential and current. {ECO:0000269|PubMed:15496425, ECO:0000269|PubMed:19949040, ECO:0000269|PubMed:20371544, ECO:0000269|PubMed:23326516, ECO:0000269|PubMed:24183479}. Note=The disease is caused by mutations affecting the gene represented in this entry. MUSK mutations lead to decreased agrin- dependent AChR aggregation, a critical step in the formation of the neuromuscular junction.; DISEASE: Fetal akinesia deformation sequence (FADS) [MIM:208150]: A clinically and genetically heterogeneous group of disorders with congenital malformations related to impaired fetal movement. Clinical features include fetal akinesia, intrauterine growth retardation, polyhydramnios, arthrogryposis, pulmonary hypoplasia, craniofacial abnormalities, and cryptorchidism. {ECO:0000269|PubMed:25537362, ECO:0000269|PubMed:25612909}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . whole body;tongue;head and neck;retina; superior cervical ganglion;globus pallidus;trigeminal ganglion;skeletal muscle; 0.44177 0.77855 0.516238257 80.33734371 1294.3217 6.77166 MUSTN1 0.00175218786439621 0.472617229435585 0.525630582700018 musculoskeletal, embryonic nuclear protein 1 FUNCTION: May be involved in the development and regeneration of the musculoskeletal system. {ECO:0000250}.; . . . . . . 0.369407109 74.95281906 29.55297 0.94430 MUT 5.92436972896757e-18 0.00645800866024609 0.993541991339754 methylmalonyl-CoA mutase FUNCTION: Involved in the degradation of several amino acids, odd- chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species.; DISEASE: Methylmalonic aciduria type mut (MMAM) [MIM:251000]: An often fatal disorder of organic acid metabolism. Common clinical features include lethargy, vomiting, failure to thrive, hypotonia, neurological deficit and early death. Two forms of the disease are distinguished by the presence (mut-) or absence (mut0) of residual enzyme activity. Mut0 patients have more severe neurological manifestations of the disease than do MUT- patients. MMAM is unresponsive to vitamin B12 therapy. {ECO:0000269|PubMed:10923046, ECO:0000269|PubMed:11350191, ECO:0000269|PubMed:1346616, ECO:0000269|PubMed:1351030, ECO:0000269|PubMed:15643616, ECO:0000269|PubMed:15781192, ECO:0000269|PubMed:16281286, ECO:0000269|PubMed:1670635, ECO:0000269|PubMed:1977311, ECO:0000269|PubMed:7909321, ECO:0000269|PubMed:7912889, ECO:0000269|PubMed:9285782, ECO:0000269|PubMed:9452100, ECO:0000269|PubMed:9554742}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;gum;bone;thyroid;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;skeletal muscle;bile duct;breast;lung;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;amygdala;fetal liver;superior cervical ganglion;medulla oblongata;temporal lobe;prefrontal cortex;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11346 0.69122 0.20030965 67.3566879 2774.75191 9.94221 MUTYH 8.56708501585961e-11 0.444669652553542 0.555330347360787 mutY DNA glycosylase FUNCTION: Involved in oxidative DNA damage repair. Initiates repair of A*oxoG to C*G by removing the inappropriately paired adenine base from the DNA backbone. Possesses both adenine and 2- OH-A DNA glycosylase activities. {ECO:0000269|PubMed:10684930}.; DISEASE: Familial adenomatous polyposis 2 (FAP2) [MIM:608456]: A condition characterized by the development of multiple colorectal adenomatous polyps, benign neoplasms derived from glandular epithelium. Some affected individuals may develop colorectal carcinoma. {ECO:0000269|PubMed:11818965, ECO:0000269|PubMed:12606733, ECO:0000269|PubMed:12853198, ECO:0000269|PubMed:15366000, ECO:0000269|PubMed:18091433, ECO:0000269|PubMed:19953527}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease. {ECO:0000269|PubMed:15273732}. Note=The gene represented in this entry may be involved in disease pathogenesis. Somatic mutations contribute to the development of a sub-set of sporadic gastric cancers in carriers of Helicobacter pylori (PubMed:15273732). {ECO:0000269|PubMed:15273732}.; . unclassifiable (Anatomical System);lymph node;sympathetic chain;colon;skeletal muscle;skin;pancreas;prostate;lung;hippocampus;testis;spleen;brain;stomach;cerebellum; subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;globus pallidus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.13463 0.29137 0.112125503 62.09601321 1736.8913 7.69141 MVB12A 0.000679169344270236 0.914542667336119 0.084778163319611 multivesicular body subunit 12A FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in the ligand-mediated internalization and down- regulation of EGF receptor. {ECO:0000269|PubMed:16895919}.; . TISSUE SPECIFICITY: Ubiquitously expressed except in skeletal muscle. {ECO:0000269|PubMed:16895919}.; . . 0.09158 . 0.350995466 74.37485256 188.19304 2.97888 MVB12B 0.622016653573598 0.377655534484813 0.000327811941588864 multivesicular body subunit 12B FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies.; . . . . 0.10578 . -0.471992905 23.03609342 8.63033 0.31683 MVD 2.16344313538101e-12 0.0090134439976643 0.990986556000172 mevalonate diphosphate decarboxylase FUNCTION: Performs the first committed step in the biosynthesis of isoprenes.; . TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, lung, liver, brain, pancreas, kidney and placenta. {ECO:0000269|PubMed:8626466}.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus; adipose tissue; 0.30837 0.19754 -1.061810361 7.519462137 115.38317 2.33582 MVK 0.0421613966473064 0.95175801502389 0.00608058832880385 mevalonate kinase FUNCTION: May be a regulatory site in cholesterol biosynthetic pathway.; DISEASE: Mevalonic aciduria (MEVA) [MIM:610377]: Accumulation of mevalonic acid which causes a variety of symptoms such as psychomotor retardation, dysmorphic features, cataracts, hepatosplenomegaly, lymphadenopathy, anemia, hypotonia, myopathy, and ataxia. {ECO:0000269|PubMed:10401001, ECO:0000269|PubMed:10417275, ECO:0000269|PubMed:11313768, ECO:0000269|PubMed:11313769, ECO:0000269|PubMed:1377680}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hyperimmunoglobulinemia D and periodic fever syndrome (HIDS) [MIM:260920]: Autosomal recessive disease characterized by recurrent episodes of unexplained high fever associated with skin rash, diarrhea, adenopathy (swollen, tender lymph nodes), arthralgias and/or arthritis. Concentration of IgD, and often IgA, are above normal. {ECO:0000269|PubMed:10369261, ECO:0000269|PubMed:10369262, ECO:0000269|PubMed:11313768, ECO:0000269|PubMed:11313769, ECO:0000269|PubMed:15536479}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Porokeratosis 3, multiple types (POROK3) [MIM:175900]: A form of porokeratosis, a disorder of faulty keratinization characterized by one or more atrophic patches surrounded by a distinctive hyperkeratotic ridgelike border called the cornoid lamella. The keratotic lesions can progress to overt cutaneous neoplasms, typically squamous cell carcinomas. Multiple clinical variants of porokeratosis are recognized, including porokeratosis of Mibelli, linear porokeratosis, disseminated superficial actinic porokeratosis, palmoplantar porokeratosis, and punctate porokeratosis. Different clinical presentations can be observed among members of the same family. Individuals expressing more than one variant have also been reported. {ECO:0000269|PubMed:22983302, ECO:0000269|PubMed:24781643}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;muscle;lens;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;tongue;liver;adrenal cortex;testis;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04253 0.31770 -0.201976964 38.98325077 295.50649 3.67097 MVP 0.00744852498762191 0.991880267637244 0.000671207375134512 major vault protein FUNCTION: Required for normal vault structure. Vaults are multi- subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo- cytoplasmic transport. Down-regulates INFG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases. {ECO:0000269|PubMed:15133037, ECO:0000269|PubMed:16418217, ECO:0000269|PubMed:16441665}.; . TISSUE SPECIFICITY: Present in most normal tissues. Higher expression observed in epithelial cells with secretory and excretory functions, as well as in cells chronically exposed to xenobiotics, such as bronchial cells and cells lining the intestine. Overexpressed in many multidrug-resistant cancer cells.; ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;choroid;fovea centralis;uterus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;nasopharynx;placenta;amnion;head and neck;kidney;stomach;aorta; superior cervical ganglion;kidney;skeletal muscle; 0.12911 0.21917 -0.813834387 12.05472989 340.52664 3.91613 MX1 4.50420824011591e-09 0.575332818262854 0.424667177232938 MX dynamin like GTPase 1 FUNCTION: Interferon-induced dynamin-like GTPase with antiviral activity against a wide range of RNA viruses and some DNA viruses. Its target viruses include negative-stranded RNA viruses and HBV through binding and inactivation of their ribonucleocapsid. May also antagonize reoviridae and asfarviridae replication. Inhibits thogoto virus (THOV) replication by preventing the nuclear import of viral nucleocapsids. Inhibits La Crosse virus (LACV) replication by sequestering viral nucleoprotein in perinuclear complexes, preventing genome amplification, budding, and egress. Inhibits influenza A virus (IAV) replication by decreasing or delaying NP synthesis and by blocking endocytic traffic of incoming virus particles. Enhances ER stress-mediated cell death after influenza virus infection. May regulate the calcium channel activity of TRPCs. {ECO:0000269|PubMed:11880649, ECO:0000269|PubMed:14687945, ECO:0000269|PubMed:14752052, ECO:0000269|PubMed:15047845, ECO:0000269|PubMed:15355513, ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:16202617, ECO:0000269|PubMed:16413306, ECO:0000269|PubMed:17374778, ECO:0000269|PubMed:18668195, ECO:0000269|PubMed:19109387, ECO:0000269|PubMed:21900240, ECO:0000269|PubMed:21992152}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;ciliary body;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;pharynx;blood;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.17049 0.49792 -0.393118976 27.05237084 3350.64074 11.08910 MX2 7.0102685339018e-08 0.970520731484966 0.0294791984123486 MX dynamin like GTPase 2 FUNCTION: Interferon-induced dynamin-like GTPase with potent antiviral activity against human immunodeficiency virus type 1 (HIV-1). Acts by targeting the viral capsid and affects the nuclear uptake and/or stability of the HIV-1 replication complex and the subsequent chromosomal integration of the proviral DNA. Exhibits antiviral activity also against simian immunodeficiency virus (SIV-mnd). May play a role in regulating nucleocytoplasmic transport and cell-cycle progression. {ECO:0000269|PubMed:15184662, ECO:0000269|PubMed:24048477, ECO:0000269|PubMed:24055605, ECO:0000269|PubMed:24121441}.; . . myocardium;colon;choroid;skin;bone marrow;uterus;prostate;bone;thyroid;testis;germinal center;spinal ganglion;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;blood;pancreas;lung;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;mammary gland;stomach;thymus; superior cervical ganglion;trigeminal ganglion;whole blood; 0.03742 . -0.349025639 29.55885822 94.69013 2.09653 MXD1 0.388108480553253 0.601963686037386 0.00992783340936109 MAX dimerization protein 1 FUNCTION: Transcriptional repressor. MAD binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. MAD thus antagonizes MYC transcriptional activity by competing for MAX.; . . unclassifiable (Anatomical System);optic nerve;frontal lobe;larynx;placenta;macula lutea;testis;colon;head and neck;fovea centralis;choroid;lens;retina;bone marrow; testis - interstitial;atrioventricular node;bone marrow; 0.93750 0.13242 -0.317668748 31.45789101 29.2168 0.93438 MXD3 0.00156992894615881 0.687819363945677 0.310610707108164 MAX dimerization protein 3 FUNCTION: Transcriptional repressor. Binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. Antagonizes MYC transcriptional activity by competing for MAX and suppresses MYC dependent cell transformation (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;stomach; superior cervical ganglion;skeletal muscle;cingulate cortex; 0.16091 . . . 55.14457 1.48841 MXD4 0.896936709353244 0.102096453226381 0.000966837420374718 MAX dimerization protein 4 FUNCTION: Transcriptional repressor. Binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. Antagonizes MYC transcriptional activity by competing for MAX and suppresses MYC dependent cell transformation (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; superior cervical ganglion;cerebellum peduncles;liver;skeletal muscle;cerebellum; 0.21248 0.09412 -0.251530012 35.42108988 10.71937 0.38908 MXI1 0.707739926081003 0.292114388529353 0.000145685389643289 MAX interactor 1, dimerization protein FUNCTION: Transcriptional repressor. MXI1 binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. MXI1 thus antagonizes MYC transcriptional activity by competing for MAX.; . TISSUE SPECIFICITY: High levels found in the brain, heart and lung while lower levels are seen in the liver, kidney and skeletal muscle.; ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; amygdala;medulla oblongata;occipital lobe;subthalamic nucleus;superior cervical ganglion;prefrontal cortex;globus pallidus;caudate nucleus;cingulate cortex;parietal lobe;bone marrow;cerebellum; 0.63737 0.18081 -0.205617011 38.57631517 84.75085 1.96085 MXRA5 0.376484079502154 0.62351208802034 3.83247750622588e-06 matrix-remodelling associated 5 . DISEASE: Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis. {ECO:0000269|PubMed:22696596}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;developmental;colon;parathyroid;skin;bone marrow;uterus;whole body;cochlea;thyroid;bone;testis;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;urinary;skeletal muscle;breast;pancreas;lung;placenta;liver;alveolus;head and neck;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;tongue;adrenal gland;adrenal cortex;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.22610 0.09488 1.571005596 95.68294409 3459.79358 11.30556 MXRA5Y . . . matrix-remodelling associated 5, Y-linked (pseudogene) . . . . . . . . . . . MXRA7 0.013741641700292 0.670187729194539 0.316070629105169 matrix-remodelling associated 7 . . . unclassifiable (Anatomical System);ovary;fovea centralis;choroid;lens;skeletal muscle;bone marrow;retina;optic nerve;lung;placenta;thyroid;macula lutea;testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;caudate nucleus;skeletal muscle; 0.08082 . . . 4093.64805 12.69309 MXRA8 0.00471297228153819 0.965656662782626 0.029630364935836 matrix-remodelling associated 8 FUNCTION: May play a role in the maturation and maintenance of blood-brain barrier. {ECO:0000250}.; . . ovary;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;adipose tissue;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14206 . . . 333.33635 3.87909 MYADM 0.148243111806785 0.777921095034753 0.0738357931584624 myeloid-associated differentiation marker . . TISSUE SPECIFICITY: Widely expressed. Not detected in thymus. {ECO:0000269|PubMed:12075932}.; medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;bone;thyroid;iris;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; ciliary ganglion; 0.15638 0.10764 -0.293801652 32.93819297 48.27411 1.35351 MYADML . . . myeloid-associated differentiation marker-like (pseudogene) . . . medulla oblongata;testis; superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;skin;skeletal muscle; 0.11654 . . . . . MYADML2 . . . myeloid-associated differentiation marker-like 2 . . . unclassifiable (Anatomical System);prostate;optic nerve;lung;whole body;macula lutea;liver;testis;fovea centralis;choroid;lens;skeletal muscle;retina; ciliary ganglion;atrioventricular node; . . 0.746027844 86.40599198 420.13389 4.28240 MYB 0.88184751057148 0.118152009810623 4.79617896487538e-07 MYB proto-oncogene, transcription factor FUNCTION: Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells.; . . unclassifiable (Anatomical System);lymph node;heart;colon;blood;fovea centralis;choroid;lens;retina;bone marrow;breast;bile duct;prostate;optic nerve;lung;endometrium;macula lutea;visual apparatus;liver;testis;spleen;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;skin;bone marrow; 0.93168 0.77718 0.088260113 60.56853031 208.30192 3.11503 MYB-AS1 . . . MYB antisense RNA 1 . . . . . . . . . . . MYBBP1A 1.69244645255186e-17 0.279235871440417 0.720764128559583 MYB binding protein (P160) 1a FUNCTION: May activate or repress transcription via interactions with sequence specific DNA-binding proteins. Repression may be mediated at least in part by histone deacetylase activity (HDAC activity). Acts as a corepressor and in concert with CRY1, represses the transcription of the core circadian clock component PER2. Preferentially binds to dimethylated histone H3 'Lys-9' (H3K9me2) on the PER2 promoter. {ECO:0000250|UniProtKB:Q7TPV4}.; . . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; . 0.60642 0.22970 2.304470256 98.33097429 3633.07146 11.69436 MYBL1 0.998332687390342 0.00166730516501322 7.44464444504363e-09 MYB proto-oncogene like 1 FUNCTION: Strong transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Could have a role in the proliferation and/or differentiation of neurogenic, spermatogenic and B-lymphoid cells.; . TISSUE SPECIFICITY: Expressed in a variety of lymphoid and solid tumor lines cultured in vitro.; . . 0.84106 0.19640 -0.290161348 33.33923095 79.17999 1.87897 MYBL2 0.992108233056559 0.0078916998934838 6.7049957262832e-08 MYB proto-oncogene like 2 FUNCTION: Transcription factor involved in the regulation of cell survival, proliferation, and differentiation. Transactivates the expression of the CLU gene. {ECO:0000269|PubMed:10770937}.; . . lymphoreticular;ovary;salivary gland;colon;skin;uterus;prostate;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;muscle;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; tumor; 0.97546 0.25596 0.178263593 66.12998349 1412.27415 7.02045 MYBPC1 0.657926418342859 0.342073565345755 1.6311385668266e-08 myosin binding protein C, slow type FUNCTION: Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.; DISEASE: Arthrogryposis, distal, 1B (DA1B) [MIM:614335]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. Distal arthrogryposis type 1 is characterized largely by camptodactyly and clubfoot. Hypoplasia and/or absence of some interphalangeal creases is common. The shoulders and hips are less frequently affected. {ECO:0000269|PubMed:20045868}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Lethal congenital contracture syndrome 4 (LCCS4) [MIM:614915]: A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy and congenital non-progressive joint contractures. The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth. {ECO:0000269|PubMed:22610851}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;hypothalamus;muscle;spinal cord;lens;skeletal muscle;greater omentum;lung;nasopharynx;hippocampus;macula lutea;liver;hypopharynx;alveolus;head and neck;mammary gland;stomach;peripheral nerve; thalamus;tongue;thyroid;skeletal muscle; 0.16355 0.20781 -1.172055164 6.027364945 1525.33329 7.25713 MYBPC2 4.01401681109932e-17 0.0720250693344076 0.927974930665592 myosin binding protein C, fast type FUNCTION: Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.; . . unclassifiable (Anatomical System);lung;heart;synovium;thyroid;liver;parathyroid;spleen;skeletal muscle;stomach; testis - interstitial;tongue;thyroid;temporal lobe;testis;skeletal muscle; 0.18597 . 2.37207375 98.45482425 2908.93676 10.23449 MYBPC3 1.35053975034244e-06 0.999906932680101 9.17167801485317e-05 myosin binding protein C, cardiac FUNCTION: Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.; DISEASE: Cardiomyopathy, familial hypertrophic 4 (CMH4) [MIM:115197]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:11499718, ECO:0000269|PubMed:11499719, ECO:0000269|PubMed:11815426, ECO:0000269|PubMed:12379228, ECO:0000269|PubMed:12628722, ECO:0000269|PubMed:12707239, ECO:0000269|PubMed:12818575, ECO:0000269|PubMed:12951062, ECO:0000269|PubMed:12974739, ECO:0000269|PubMed:14563344, ECO:0000269|PubMed:15114369, ECO:0000269|PubMed:15519027, ECO:0000269|PubMed:15563892, ECO:0000269|PubMed:16004897, ECO:0000269|PubMed:16199542, ECO:0000269|PubMed:18403758, ECO:0000269|PubMed:18929575, ECO:0000269|PubMed:18957093, ECO:0000269|PubMed:23840593, ECO:0000269|PubMed:7744002, ECO:0000269|PubMed:9048664, ECO:0000269|PubMed:9541104, ECO:0000269|PubMed:9541115, ECO:0000269|PubMed:9562578}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1MM (CMD1MM) [MIM:615396]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:20215591}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=MYBPC3 mutations may be involved in restrictive cardiomyopathy (RCM), a rare non-ischemic myocardial disease. RCM is characterized by restrictive ventricular-filling physiology in the presence of normal or reduced diastolic and/or systolic volumes (of 1 or both ventricles), biatrial enlargement, and normal ventricular wall thickness. {ECO:0000269|PubMed:26163040}.; DISEASE: Left ventricular non-compaction 10 (LVNC10) [MIM:615396]: A disease due to an arrest of myocardial morphogenesis. It is characterized by a hypertrophic left ventricle with deep trabeculations and with poor systolic function, with or without associated left ventricular dilation. In some cases, it is associated with other congenital heart anomalies. {ECO:0000269|PubMed:21551322}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);myocardium;lung;heart;synovium;placenta;liver;testis;spleen; superior cervical ganglion;heart; 0.49203 0.21433 -0.534756622 20.54140127 1069.38163 6.26965 MYBPH 3.22430226765915e-11 0.0436671220923578 0.956332877875399 myosin binding protein H FUNCTION: Binds to myosin; probably involved in interaction with thick myofilaments in the A-band.; . TISSUE SPECIFICITY: Skeletal muscle.; unclassifiable (Anatomical System);heart;tongue;blood;parathyroid;uterus;pancreas;prostate;whole body;lung;visual apparatus;testis;head and neck;kidney;brain; superior cervical ganglion;tongue;skeletal muscle; 0.08610 0.11814 -0.26629572 34.81953291 1522.90266 7.25241 MYBPHL 0.00461844098878081 0.964932234945796 0.0304493240654229 myosin binding protein H-like . . . unclassifiable (Anatomical System);optic nerve;ovary;macula lutea;liver;spleen;fovea centralis;choroid;lens;brain;stomach;retina; . . 0.10520 0.600782551 82.82613824 175.54717 2.88252 MYC . . . v-myc avian myelocytomatosis viral oncogene homolog FUNCTION: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'- CAC[GA]TG-3'. Activates the transcription of growth-related genes.; DISEASE: Note=A chromosomal aberration involving MYC may be a cause of a form of B-cell chronic lymphocytic leukemia. Translocation t(8;12)(q24;q22) with BTG1. {ECO:0000269|PubMed:2069907}.; DISEASE: Burkitt lymphoma (BL) [MIM:113970]: A form of undifferentiated malignant lymphoma commonly manifested as a large osteolytic lesion in the jaw or as an abdominal mass. {ECO:0000269|PubMed:2166998, ECO:0000269|PubMed:8220424}. Note=The gene represented in this entry is involved in disease pathogenesis. Chromosomal aberrations involving MYC are usually found in Burkitt lymphoma. Translocations t(8;14), t(8;22) or t(2;8) which juxtapose MYC to one of the heavy or light chain immunoglobulin gene loci.; . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;cochlea;larynx;bone;thyroid;testis;spinal ganglion;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; lung;tumor;white blood cells;ciliary ganglion;trigeminal ganglion;skin; 0.70121 0.98749 -0.003562597 53.72729417 227.85179 3.25935 MYCBP 0.739328409179167 0.249430526639295 0.0112410641815377 MYC binding protein FUNCTION: May control the transcriptional activity of MYC. Stimulates the activation of E box-dependent transcription by MYC.; . TISSUE SPECIFICITY: Highly expressed in heart, placenta, pancreas, skeletal muscle and kidney. Also present at low levels in lung.; . . 0.20298 . 0.101211609 60.95777306 4.72747 0.17167 MYCBP2 1 3.34881873209318e-19 1.00531286043132e-54 MYC binding protein 2, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of TSC2/tuberin. Interacts with the E2 enzymes UBE2D1, UBE2D3 and UBE2L3 (in vitro). May function as a facilitator or regulator of transcriptional activation by MYC. May have a role during synaptogenesis. {ECO:0000269|PubMed:18308511}.; . TISSUE SPECIFICITY: Expressed in all tissues examined, expression is exceptionally abundant in brain and thymus. Colocalizes with TSC1 and TSC2 along the neurites and in the growth cones. Colocalized with TSC1 in one of the filopodial extensions at the tip of a growth cone. {ECO:0000269|PubMed:9689053}.; myocardium;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;urinary;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; amygdala;whole brain;medulla oblongata;testis - interstitial;occipital lobe;thalamus;adipose tissue;hypothalamus;temporal lobe;white blood cells;caudate nucleus;pons;subthalamic nucleus;prostate;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;tonsil; 0.51896 0.10950 -0.328796968 30.86223166 523.10259 4.66678 MYCBP2-AS1 . . . MYCBP2 antisense RNA 1 . . . . . . . . . . . MYCBP2-AS2 . . . MYCBP2 antisense RNA 2 . . . . . . . . . . . MYCBPAP 0.00173300584771018 0.9982211652365 4.58289157895159e-05 MYCBP associated protein FUNCTION: May play a role in spermatogenesis. May be involved in synaptic processes (By similarity). {ECO:0000250|UniProtKB:Q69CM7, ECO:0000269|PubMed:12151104}.; . TISSUE SPECIFICITY: Expressed specifically in testis. {ECO:0000269|PubMed:12151104}.; unclassifiable (Anatomical System);medulla oblongata;smooth muscle;lung;placenta;testis; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.09337 0.08885 2.011818712 97.67633876 2351.86361 8.98627 MYCL 0.3588124729359 0.628828519284873 0.0123590077792268 v-myc avian myelocytomatosis viral oncogene lung carcinoma derived homolog . . . . . 0.51310 0.42245 -0.093566408 46.7386176 27.78536 0.89218 MYCLK1 . . . v-myc avian myelocytomatosis viral oncogene homolog-like 1 . . . . . . . . . . . MYCLP1 . . . MYCL pseudogene 1 . . TISSUE SPECIFICITY: Detected in adult testis. {ECO:0000269|PubMed:1711681}.; . . 0.29635 . . . . . MYCLP2 . . . MYCL pseudogene 2 . . . . . . . . . . . MYCLP3 . . . MYCL pseudogene 3 . . . . . . . . . . . MYCN 0.913862107818068 0.0855264491199464 0.000611443061986198 v-myc avian myelocytomatosis viral oncogene neuroblastoma derived homolog FUNCTION: Positively regulates the transcription of NCYM in neuroblastoma cells (PubMed:24391509). {ECO:0000269|PubMed:24391509}.; DISEASE: Note=Amplification of the N-MYC gene is associated with a variety of human tumors, most frequently neuroblastoma, where the level of amplification appears to increase as the tumor progresses. {ECO:0000269|PubMed:2834684}.; DISEASE: Feingold syndrome 1 (FGLDS1) [MIM:164280]: A syndrome characterized by variable combinations of esophageal and duodenal atresias, microcephaly, learning disability, mental retardation, and limb malformations. Hand and foot abnormalities may include hypoplastic thumbs, clinodactyly of second and fifth fingers, syndactyly (characteristically between second and third and fourth and fifth toes), and shortened or absent middle phalanges. Cardiac and renal malformations, vertebral anomalies, and deafness have also been described. {ECO:0000269|PubMed:15821734, ECO:0000269|PubMed:16906565}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the neuronal cells of the cerebrum, neuroblastomas and thyroid tumors (at protein level). {ECO:0000269|PubMed:24391509}.; unclassifiable (Anatomical System);ovary;heart;salivary gland;muscle;intestine;pharynx;colon;blood;skin;breast;uterus;prostate;lung;endometrium;bone;placenta;visual apparatus;liver;testis;kidney;brain;bladder;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;heart;fetal brain;placenta;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.99386 0.67090 -0.383807564 27.41802312 25.75116 0.83879 MYCNOS . . . MYCN opposite strand FUNCTION: Regulates stability of MYCN in neuroblastoma cells by inhibiting GSK3B-mediated MYCN phosphorylation. Inhibits GSK3B activity by promoting its phosphorylation at 'Ser-9' (PubMed:24391509). {ECO:0000269|PubMed:24391509}.; . TISSUE SPECIFICITY: Expressed in the neuronal cells of the cerebrum and cerebellum, spermatocytes of the testis, pancreatic cells and also the heart. Expressed in both primary and metastatic neuroblastomas and in thyroid tumors (at protein level). Expression is associated with poor prognosis in neuroblastoma. Expressed in the fetal brain, lung, liver and kidney at varying low levels. {ECO:0000269|PubMed:1419902, ECO:0000269|PubMed:24391509}.; . . . . . . . . MYCNUT . . . MYCN upstream transcript (non-protein coding) . . . . . . . . . . . MYCT1 6.34322649393561e-05 0.477102325674928 0.522834242060133 myc target 1 FUNCTION: May regulate certain MYC target genes, MYC seems to be a direct upstream transcriptional activator. Does not seem to significantly affect growth cell capacity. Overexpression seems to mediate many of the known phenotypic features associated with MYC, including promotion of apoptosis, alteration of morphology, enhancement of anchorage-independent growth, tumorigenic conversion, promotion of genomic instability, and inhibition of hematopoietic differentiation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Down-regulated in gastric cancer tissues.; . . 0.71820 0.09518 0.549415813 81.38122199 1709.96613 7.62536 MYD88 0.711854614335331 0.287458769360846 0.000686616303822229 myeloid differentiation primary response 88 FUNCTION: Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response. Acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Increases IL-8 transcription. Involved in IL-18-mediated signaling pathway. Activates IRF1 resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes. MyD88-mediated signaling in intestinal epithelial cells is crucial for maintenance of gut homeostasis and controls the expression of the antimicrobial lectin REG3G in the small intestine. {ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:18292575, ECO:0000269|PubMed:19506249, ECO:0000269|PubMed:24316379, ECO:0000269|PubMed:9013863}.; DISEASE: MYD88 deficiency (MYD88D) [MIM:612260]: Patients suffer from autosomal recessive, life-threatening, often recurrent pyogenic bacterial infections, including invasive pneumococcal disease, and die between 1 and 11 months of age. Surviving patients are otherwise healthy, with normal resistance to other microbes, and their clinical status improved with age. {ECO:0000269|PubMed:18669862, ECO:0000269|PubMed:21057262, ECO:0000269|PubMed:24316379}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in MYD88 are frequently found in many hematological malignancies, such as activated B-cell type diffuse large B-cell lymphoma (ABC-DLBCL), Waldenstroem's macroglobulinemia, cutaneous diffuse large B cell lymphoma (CBCL) and primary central nervous system lymphoma (PCNSL). {ECO:0000269|PubMed:21179087, ECO:0000269|PubMed:22931316}.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8957090}.; . . 0.18000 0.12170 -0.339715008 30.06605331 26.17859 0.84849 MYDGF . . . myeloid-derived growth factor FUNCTION: Bone marrow-derived monocyte and paracrine-acting protein that promotes cardiac myocyte survival and adaptive angiogenesis for cardiac protection and/or repair after myocardial infarction (MI). Stimulates endothelial cell proliferation through a MAPK1/3-, STAT3- and CCND1-mediated signaling pathway. Inhibits cardiac myocyte apoptosis in a PI3K/AKT-dependent signaling pathway (By similarity). Involved in endothelial cell proliferation and angiogenesis (PubMed:25581518). {ECO:0000250|UniProtKB:Q9CPT4, ECO:0000269|PubMed:25581518}.; . TISSUE SPECIFICITY: Expressed in bone marrow cells (PubMed:25581518). Expressed in synovial tissue. Found in synovial fluid of patients with arthropaties (PubMed:17362502). {ECO:0000269|PubMed:17362502, ECO:0000269|PubMed:25581518}.; . . 0.08462 0.13843 0.215080721 67.91696155 . . MYEF2 0.999492304383741 0.000507695205838329 4.10420197766535e-10 myelin expression factor 2 FUNCTION: Transcriptional repressor of the myelin basic protein gene (MBP). Binds to the proximal MB1 element 5'-TTGTCC-3' of the MBP promoter. Its binding to MB1 and function are inhibited by PURA (By similarity). {ECO:0000250}.; . . ovary;sympathetic chain;colon;parathyroid;skin;bone marrow;retina;uterus;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;artery;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;skeletal muscle;lung;placenta;liver;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.38490 0.30764 -0.069700724 48.54328851 638.26971 5.08207 MYEOV 0.00119290607835127 0.628674434811683 0.370132659109966 myeloma overexpressed . . . unclassifiable (Anatomical System);heart;ovary;colon;blood;skin;bile duct;pancreas;prostate;lung;placenta;bone;liver;brain;stomach; ciliary ganglion;atrioventricular node; 0.09702 . 1.953079981 97.54659118 2321.02204 8.91997 MYEOV2 0.000104799265064917 0.583940662652844 0.415954538082091 myeloma overexpressed 2 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;testis;bladder;brain;unclassifiable (Anatomical System);pharynx;blood;lens;skeletal muscle;lung;placenta;visual apparatus;macula lutea;liver;cervix;kidney;stomach; subthalamic nucleus;globus pallidus;pons;parietal lobe; 0.13578 . 0.505321956 80.00707714 120.27931 2.38938 MYF5 0.0019034048050669 0.727788035616357 0.270308559578576 myogenic factor 5 FUNCTION: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation. Together with MYOG and MYOD1, co-occupies muscle-specific gene promoter core region during myogenesis. Induces fibroblasts to differentiate into myoblasts. Probable sequence specific DNA-binding protein.; . . uterus;heart;developmental;kidney;skin; superior cervical ganglion;skeletal muscle; 0.97978 0.30366 -0.538132194 20.26421326 20.32434 0.69389 MYF6 0.0762860430466965 0.872435389097328 0.0512785678559758 myogenic factor 6 FUNCTION: Involved in muscle differentiation (myogenic factor). Induces fibroblasts to differentiate into myoblasts. Probable sequence specific DNA-binding protein.; . TISSUE SPECIFICITY: Skeletal muscle.; uterus;ovary;heart;placenta;liver;parathyroid;kidney;brain;skin;skeletal muscle; superior cervical ganglion;uterus corpus;ciliary ganglion;skeletal muscle;cerebellum; 0.90058 0.28104 0.03689118 56.64071715 35.19539 1.06576 MYH1 1.29393709923033e-29 0.0418523093978184 0.958147690602182 myosin, heavy chain 1, skeletal muscle, adult FUNCTION: Muscle contraction.; . . unclassifiable (Anatomical System);heart;larynx;bone;thyroid;visual apparatus;spinal cord;muscle;liver;hypopharynx;testis;head and neck;skeletal muscle; superior cervical ganglion;tongue;thyroid;pons;trigeminal ganglion;skeletal muscle; 0.69127 0.30625 -1.080656478 7.248171739 785.49267 5.53734 MYH2 1.37482849584656e-08 0.999999978595694 7.65602138836142e-09 myosin, heavy chain 2, skeletal muscle, adult FUNCTION: Muscle contraction. Required for cytoskeleton organization (By similarity). {ECO:0000250}.; DISEASE: Myopathy, proximal, and ophthalmoplegia (MYPOP) [MIM:605637]: A muscular disorder characterized by mild-to- moderate muscle weakness, ophthalmoplegia, and contractures at birth in some patients. Muscle biopsies from patients show predominance of type 1 fibers and small or absent type 2A fibers. The disease is non-progressive or it progresses very slowly. Inheritance is autosomal dominant or recessive. {ECO:0000269|PubMed:11114175}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;tongue;spinal cord;muscle;skeletal muscle;retina;uterus;greater omentum;prostate;lung;larynx;epididymis;thyroid;visual apparatus;alveolus;hypopharynx;liver;testis;head and neck;peripheral nerve; tongue;thyroid;fetal thyroid;skeletal muscle; 0.89178 0.23115 -2.091107194 1.568766218 218.35437 3.19353 MYH3 3.59579597228138e-13 0.999999918275077 8.17245637005245e-08 myosin, heavy chain 3, skeletal muscle, embryonic FUNCTION: Muscle contraction.; DISEASE: Arthrogryposis, distal, 2A (DA2A) [MIM:193700]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA2A is characterized by contractures of the hands and feet, oropharyngeal abnormalities, scoliosis, and a distinctive face that includes a very small oral orifice, puckered lips, and an H- shaped dimple of the chin. {ECO:0000269|PubMed:16642020}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Arthrogryposis, distal, 2B (DA2B) [MIM:601680]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA2B is characterized by contractures of the hands and feet, and a distinctive face characterized by prominent nasolabial folds, small mouth and downslanting palpebral fissures. {ECO:0000269|PubMed:16642020}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Arthrogryposis, distal, 8 (DA8) [MIM:178110]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. {ECO:0000269|PubMed:25957469}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in fetal bone, thymus, placenta, heart, brain, and liver. {ECO:0000269|PubMed:25957469}.; unclassifiable (Anatomical System);heart;tongue;developmental;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;pancreas;optic nerve;whole body;lung;thyroid;macula lutea;visual apparatus;liver;testis;kidney;mammary gland; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.43095 0.21181 -1.554570334 3.225996697 602.04688 4.96558 MYH4 8.81492134588241e-35 0.00377769577362119 0.996222304226379 myosin, heavy chain 4, skeletal muscle FUNCTION: Muscle contraction.; . . . . 0.56363 0.18807 0.137618858 63.62349611 3768.81674 12.01419 MYH6 1.27598576115295e-17 0.998347116523782 0.0016528834762179 myosin, heavy chain 6, cardiac muscle, alpha FUNCTION: Muscle contraction.; DISEASE: Atrial septal defect 3 (ASD3) [MIM:614089]: A congenital heart malformation characterized by incomplete closure of the wall between the atria resulting in blood flow from the left to the right atria. {ECO:0000269|PubMed:15735645}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, familial hypertrophic 14 (CMH14) [MIM:613251]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:11815426, ECO:0000269|PubMed:15998695}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1EE (CMD1EE) [MIM:613252]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:15998695}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Sick sinus syndrome 3 (SSS3) [MIM:614090]: The term 'sick sinus syndrome' encompasses a variety of conditions caused by sinus node dysfunction. The most common clinical manifestations are syncope, presyncope, dizziness, and fatigue. Electrocardiogram typically shows sinus bradycardia, sinus arrest, and/or sinoatrial block. Episodes of atrial tachycardias coexisting with sinus bradycardia ('tachycardia-bradycardia syndrome') are also common in this disorder. SSS occurs most often in the elderly associated with underlying heart disease or previous cardiac surgery, but can also occur in the fetus, infant, or child without heart disease or other contributing factors. {ECO:0000269|PubMed:21378987}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. The lifetime risk of being diagnosed with sick sinus syndrome is higher for carriers of variant p.Arg721Trp than for non-carriers. {ECO:0000269|PubMed:21378987}.; . unclassifiable (Anatomical System);myocardium;heart;tongue;muscle;skeletal muscle;whole body;atrium;lung;epididymis;thyroid;liver;head and neck; heart;fetal thyroid;skeletal muscle; 0.84563 0.11625 -2.784931854 0.660533145 5098.77916 14.63955 MYH7 0.000145766291646031 0.999854233523213 1.85141250905742e-10 myosin, heavy chain 7, cardiac muscle, beta FUNCTION: Muscle contraction.; DISEASE: Cardiomyopathy, familial hypertrophic 1 (CMH1) [MIM:192600]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:10065021, ECO:0000269|PubMed:10329202, ECO:0000269|PubMed:10521296, ECO:0000269|PubMed:10563488, ECO:0000269|PubMed:10679957, ECO:0000269|PubMed:10862102, ECO:0000269|PubMed:11113006, ECO:0000269|PubMed:11133230, ECO:0000269|PubMed:11214007, ECO:0000269|PubMed:11424919, ECO:0000269|PubMed:11733062, ECO:0000269|PubMed:11861413, ECO:0000269|PubMed:11968089, ECO:0000269|PubMed:12081993, ECO:0000269|PubMed:12566107, ECO:0000269|PubMed:12590187, ECO:0000269|PubMed:12707239, ECO:0000269|PubMed:12818575, ECO:0000269|PubMed:12820698, ECO:0000269|PubMed:12951062, ECO:0000269|PubMed:12974739, ECO:0000269|PubMed:12975413, ECO:0000269|PubMed:1417858, ECO:0000269|PubMed:15358028, ECO:0000269|PubMed:15483641, ECO:0000269|PubMed:1552912, ECO:0000269|PubMed:15563892, ECO:0000269|PubMed:15856146, ECO:0000269|PubMed:15858117, ECO:0000269|PubMed:16199542, ECO:0000269|PubMed:16267253, ECO:0000269|PubMed:1638703, ECO:0000269|PubMed:16650083, ECO:0000269|PubMed:16938236, ECO:0000269|PubMed:17372140, ECO:0000269|PubMed:18175163, ECO:0000269|PubMed:18403758, ECO:0000269|PubMed:1975517, ECO:0000269|PubMed:25182012, ECO:0000269|PubMed:7581410, ECO:0000269|PubMed:7731997, ECO:0000269|PubMed:7848441, ECO:0000269|PubMed:7874131, ECO:0000269|PubMed:8250038, ECO:0000269|PubMed:8254035, ECO:0000269|PubMed:8268932, ECO:0000269|PubMed:8282798, ECO:0000269|PubMed:8343162, ECO:0000269|PubMed:8435239, ECO:0000269|PubMed:8483915, ECO:0000269|PubMed:8655135, ECO:0000269|PubMed:8899546, ECO:0000269|PubMed:9544842, ECO:0000269|PubMed:9822100, ECO:0000269|PubMed:9829907}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myopathy, myosin storage, autosomal dominant (MSMA) [MIM:608358]: A rare congenital myopathy characterized by subsarcolemmal hyalinized bodies in type 1 muscle fibers. {ECO:0000269|PubMed:14520662, ECO:0000269|PubMed:15136674, ECO:0000269|PubMed:16684601, ECO:0000269|PubMed:17336526}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Scapuloperoneal myopathy MYH7-related (SPMM) [MIM:181430]: Progressive muscular atrophia beginning in the lower legs and affecting the shoulder region earlier and more severely than distal arm. {ECO:0000269|PubMed:17336526}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1S (CMD1S) [MIM:613426]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:11106718, ECO:0000269|PubMed:12379228, ECO:0000269|PubMed:15769782, ECO:0000269|PubMed:18506004, ECO:0000269|PubMed:21127202, ECO:0000269|PubMed:21846512}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myopathy, distal, 1 (MPD1) [MIM:160500]: A muscular disorder characterized by early-onset selective weakness of the great toe and ankle dorsiflexors, followed by weakness of the finger extensors. Mild proximal weakness occasionally develops years later after the onset of the disease. {ECO:0000269|PubMed:15322983, ECO:0000269|PubMed:17548557}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myopathy, myosin storage, autosomal recessive (MSMB) [MIM:255160]: An autosomal recessive form of myosin storage myopathy, a muscle disease characterized by subsarcolemmal accumulation of hyalinized bodies in type 1 muscle fibers. MSMB clinical features include muscle weakness, type II respiratory failure and cardiac failure, due to hypertrophic cardiomyopathy. {ECO:0000269|PubMed:25666907}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Both wild type and variant Gln-403 are detected in skeletal muscle (at protein level). {ECO:0000269|PubMed:8514894}.; unclassifiable (Anatomical System);greater omentum;myocardium;prostate;lung;heart;larynx;muscle;testis;head and neck;skeletal muscle;peripheral nerve; heart;tongue;skeletal muscle; 0.43904 0.16764 -3.644803418 0.283085633 108.56923 2.26118 MYH7B 1.33080887914663e-23 0.792349352705738 0.207650647294262 myosin, heavy chain 7B, cardiac muscle, beta FUNCTION: Involved in muscle contraction. {ECO:0000269|PubMed:11919279}.; . TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, testis, and all specific brain regions examined. Slightly lower expression was detected in ovary and kidney, and intermediate expression was detected in lung, pancreas, spleen and liver. {ECO:0000269|PubMed:10819331}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;ganglion;endometrium;thyroid;bone;iris;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;urinary;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;kidney;mammary gland;stomach;thymus; superior cervical ganglion;liver;caudate nucleus; 0.15291 0.32389 -0.893455413 10.17338995 2287.01575 8.85125 MYH8 1.60588948783826e-34 0.00279306190160839 0.997206938098392 myosin, heavy chain 8, skeletal muscle, perinatal FUNCTION: Muscle contraction.; DISEASE: Carney complex variant (CACOV) [MIM:608837]: Carney complex is a multiple neoplasia syndrome characterized by spotty skin pigmentation, cardiac and other myxomas, endocrine tumors, and psammomatous melanotic schwannomas. Familial cardiac myxomas are associated with spotty pigmentation of the skin and other phenotypes, including primary pigmented nodular adrenocortical dysplasia, extracardiac (frequently cutaneous) myxomas, schwannomas, and pituitary, thyroid, testicular, bone, ovarian, and breast tumors. Cardiac myxomas do not develop in all patients with the Carney complex, but affected patients have at least two features of the complex or one feature and a clinically significant family history. {ECO:0000269|PubMed:15282353}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Arthrogryposis, distal, 7 (DA7) [MIM:158300]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA7 is characterized by an inability to open the mouth fully (trismus) and pseudocamptodactyly in which wrist dorsiflexion, but not volarflexion, produces involuntary flexion contracture of distal and proximal interphalangeal joints. Additional features include shortened hamstring muscles and short stature. {ECO:0000269|PubMed:15282353, ECO:0000269|PubMed:20949528}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . uterus;prostate;pancreas;whole body;heart;bone;visual apparatus;kidney;skin; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion; 0.49096 0.18702 -0.685494642 15.27482897 5045.02924 14.53105 MYH9 0.999999999912023 8.79766471006807e-11 2.8170225087734e-27 myosin, heavy chain 9, non-muscle FUNCTION: Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10. {ECO:0000269|PubMed:20052411}.; DISEASE: May-Hegglin anomaly (MHA) [MIM:155100]: A disorder characterized by thrombocytopenia, giant platelets and Dohle body- like inclusions in peripheral blood leukocytes. appearing as highly parallel paracrystalline bodies. {ECO:0000269|PubMed:10973260, ECO:0000269|PubMed:12533692, ECO:0000269|PubMed:12792306}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Sebastian syndrome (SBS) [MIM:605249]: Autosomal dominant macrothrombocytopenia characterized by thrombocytopenia, giant platelets and leukocyte inclusions that are smaller and less organized than in May-Hegglin anomaly. {ECO:0000269|PubMed:12533692}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Fechtner syndrome (FTNS) [MIM:153640]: Autosomal dominant macrothrombocytopenia characterized by thrombocytopenia, giant platelets and leukocyte inclusions that are small and poorly organized. Additionally, FTNS is distinguished by Alport-like clinical features of sensorineural deafness, cataracts and nephritis. {ECO:0000269|PubMed:10973259, ECO:0000269|PubMed:11776386, ECO:0000269|PubMed:12533692, ECO:0000269|PubMed:12792306}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Alport syndrome, with macrothrombocytopenia (APSM) [MIM:153650]: An autosomal dominant disorder characterized by the association of ocular lesions, sensorineural hearing loss and nephritis (Alport syndrome) with platelet defects. {ECO:0000269|PubMed:11590545}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epstein syndrome (EPS) [MIM:153650]: An autosomal dominant disorder characterized by the association of macrothrombocytopathy, sensorineural hearing loss and nephritis. {ECO:0000269|PubMed:11752022, ECO:0000269|PubMed:11935325, ECO:0000269|PubMed:12533692, ECO:0000269|PubMed:12792306, ECO:0000269|PubMed:16969870}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal dominant, 17 (DFNA17) [MIM:603622]: A form of deafness characterized by progressive high frequency hearing impairment and cochleosaccular degeneration. {ECO:0000269|PubMed:11023810}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Macrothrombocytopenia and progressive sensorineural deafness (MPSD) [MIM:600208]: An autosomal dominant disorder characterized by the association of macrothrombocytopathy and progressive sensorineural hearing loss without renal dysfunction. {ECO:0000269|PubMed:12621333}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Subjects with mutations in the motor domain of MYH9 present with severe thrombocytopenia and develop nephritis and deafness before the age of 40 years, while those with mutations in the tail domain have a much lower risk of noncongenital complications and significantly higher platelet counts. The clinical course of patients with mutations in the four most frequently affected residues of MYH9 (responsible for 70% of MYH9- related cases) were evaluated. Mutations at residue 1933 do not induce kidney damage or cataracts and cause deafness only in the elderly, those in position 702 result in severe thrombocytopenia and produce nephritis and deafness at a juvenile age, while alterations at residue 1424 or 1841 result in intermediate clinical pictures.; DISEASE: Note=Genetic variations in MYH9 are associated with non- diabetic end stage renal disease (ESRD).; TISSUE SPECIFICITY: In the kidney, expressed in the glomeruli. Also expressed in leukocytes. {ECO:0000269|PubMed:11752022, ECO:0000269|PubMed:1912569}.; smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;ganglion;endometrium;cochlea;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;uterus;oesophagus;larynx;bone;testis;artery;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;cornea;placenta;hippocampus;amnion;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;bone marrow; 0.30613 0.64366 -1.993966113 1.745694739 1763.68591 7.75715 MYH10 0.999997549727666 2.45027233389188e-06 5.31384517930789e-22 myosin, heavy chain 10, non-muscle FUNCTION: Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the central part but not the margins of spreading cells), and lamellipodial extension; this function is mechanically antagonized by MYH9. {ECO:0000269|PubMed:20052411, ECO:0000269|PubMed:20603131}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in cerebellum and spinal chord. Isoform 2 is expressed in cerebrum and retina. Isoform 3 is expressed in the cerebrum and to a much lower extent in cerebellum. {ECO:0000269|PubMed:7782316}.; ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;bladder;brain;amygdala;heart;cartilage;tongue;pineal body;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;oesophagus;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;oral cavity;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;aorta; superior cervical ganglion;prefrontal cortex;globus pallidus;cingulate cortex; 0.84700 . -2.076219205 1.598254305 198.82672 3.04687 MYH11 0.998956488496709 0.00104351150329115 2.264158565604e-18 myosin, heavy chain 11, smooth muscle FUNCTION: Muscle contraction.; DISEASE: Note=A chromosomal aberration involving MYH11 is found in acute myeloid leukemia of M4EO subtype. Pericentric inversion inv(16)(p13;q22). The inversion produces a fusion protein consisting of the 165 N-terminal residues of CBF-beta (PEPB2) and the tail region of MYH11.; DISEASE: Aortic aneurysm, familial thoracic 4 (AAT4) [MIM:132900]: A disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance. {ECO:0000269|PubMed:16444274}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Smooth muscle; expressed in the umbilical artery, bladder, esophagus and trachea. Isoform 1 is mostly found in slowly contracting tonic muscles. {ECO:0000269|PubMed:16000639}.; myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;bladder;gall bladder;heart;cartilage;blood;skeletal muscle;trabecular meshwork;visual apparatus;liver;spleen;mammary gland;colon;parathyroid;choroid;uterus;cerebral cortex;synovium;larynx;bone;pituitary gland;testis;artery;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; superior cervical ganglion;testis - interstitial;ovary;skeletal muscle;uterus;uterus corpus;prostate;trachea;testis - seminiferous tubule;placenta;liver;appendix;testis;ciliary ganglion;fetal lung;trigeminal ganglion; 0.80889 0.40016 -3.099214965 0.465911772 2033.84967 8.30427 MYH13 1.88615995107426e-29 0.014239931349782 0.985760068650218 myosin, heavy chain 13, skeletal muscle FUNCTION: Fast twitching myosin mediating the high-velocity and low-tension contractions of specific striated muscles. {ECO:0000269|PubMed:23908353}.; . TISSUE SPECIFICITY: Specifically expressed in extraocular and laryngeal muscles. {ECO:0000269|PubMed:12110653}.; . . 0.48597 0.18810 -0.635977455 16.74333569 5547.032 15.40045 MYH14 0.999847921380196 0.000152078619804206 6.11640125875656e-17 myosin, heavy chain 14, non-muscle FUNCTION: Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. {ECO:0000250}.; DISEASE: Deafness, autosomal dominant, 4A (DFNA4A) [MIM:600652]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:15015131, ECO:0000269|PubMed:16222661}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peripheral neuropathy, myopathy, hoarseness, and hearing loss (PNMHH) [MIM:614369]: A complex phenotype of progressive peripheral neuropathy and distal myopathy, with later onset of hoarseness and hearing loss. Affected individuals develop distal muscle weakness at a mean age of 10.6 years, followed by progressive atrophy of these muscles. The lower limbs are more severely affected than the upper limbs, and the muscle weakness first affects anterior leg muscles and later posterior leg muscles. {ECO:0000269|PubMed:21480433}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: High levels of expression are found in brain (highest in corpus callosum), heart, kidney, liver, lung, small intestine, colon and skeletal muscle. Expression is low in organs composed mainly of smooth muscle, such as aorta, uterus and urinary bladder. No detectable expression is found in thymus, spleen, placenta and lymphocytes. {ECO:0000269|PubMed:12909352, ECO:0000269|PubMed:14594953, ECO:0000269|PubMed:19240025}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;oesophagus;larynx;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;lacrimal gland;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;macula lutea;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;kidney;trigeminal ganglion;skeletal muscle;skin; 0.22477 0.14506 -2.236665977 1.309271054 1826.33006 7.88079 MYH15 4.73936233784156e-39 0.000158733641428619 0.999841266358571 myosin, heavy chain 15 FUNCTION: Muscle contraction. {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;prostate;hypothalamus;placenta;liver;colon; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10968 0.09113 0.464695413 78.59754659 3550.47942 11.51131 MYH16 . . . myosin, heavy chain 16 pseudogene FUNCTION: Has most probably lost the function in masticatory muscles contraction suspected for its homologs in dog (AC F1PT61) and apes. {ECO:0000303|PubMed:15042088}.; . . lung;testis; . 0.14587 . . . . . MYHAS . . . myosin heavy chain gene cluster antisense RNA . . . . . . . . . . . MYL1 0.0633863743158515 0.870138600780874 0.066475024903275 myosin light chain 1 FUNCTION: Regulatory light chain of myosin. Does not bind calcium.; . . unclassifiable (Anatomical System);ovary;heart;tongue;muscle;parathyroid;skeletal muscle;greater omentum;pancreas;prostate;whole body;lung;larynx;placenta;visual apparatus;alveolus;hypopharynx;liver;head and neck;spleen;thymus; superior cervical ganglion;tongue;thyroid;fetal thyroid;skeletal muscle; 0.59705 . -0.049474214 50.01179523 32.63324 1.01469 MYL2 0.0168131337644691 0.888138290534909 0.0950485757006216 myosin light chain 2 FUNCTION: Contractile protein that plays a role in heart development and function (By similarity). Following phosphorylation, plays a role in cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion; as a consequence of the increase in maximum contraction force and calcium sensitivity of contraction force. These events altogether slow down myosin kinetics and prolong duty cycle resulting in accumulated myosins being cooperatively recruited to actin binding sites to sustain thin filament activation as a means to fine-tune myofilament calcium sensitivity to force (By similarity). During cardiogenesis plays an early role in cardiac contractility by promoting cardiac myofibril assembly (By similarity). {ECO:0000250|UniProtKB:P08733, ECO:0000250|UniProtKB:P51667}.; DISEASE: Cardiomyopathy, familial hypertrophic 10 (CMH10) [MIM:608758]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. Rarely, patients present a variant of familial hypertrophic cardiomyopathy, characterized by mid-left ventricular chamber thickening. {ECO:0000269|PubMed:11102452, ECO:0000269|PubMed:12404107, ECO:0000269|PubMed:12707239, ECO:0000269|PubMed:12818575, ECO:0000269|PubMed:8673105, ECO:0000269|PubMed:9535554}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;heart;tongue;muscle;skin;skeletal muscle;uterus;greater omentum;prostate;whole body;lung;epididymis;larynx;bone;visual apparatus;alveolus;liver;testis;head and neck;germinal center; heart;tongue;thyroid;fetal thyroid;skeletal muscle; 0.24856 0.27335 -0.273576253 33.97027601 4.93524 0.18346 MYL3 0.888080620769772 0.11072439612989 0.00119498310033762 myosin light chain 3 FUNCTION: Regulatory light chain of myosin. Does not bind calcium.; DISEASE: Cardiomyopathy, familial hypertrophic 8 (CMH8) [MIM:608751]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. Rarely, patients present a variant of familial hypertrophic cardiomyopathy, characterized by mid-left ventricular chamber thickening. {ECO:0000269|PubMed:12021217, ECO:0000269|PubMed:12707239, ECO:0000269|PubMed:23594557, ECO:0000269|PubMed:8673105}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);myocardium;heart;muscle;skin;skeletal muscle;uterus;pancreas;prostate;lung;bone;liver;testis;kidney;brain;thymus; superior cervical ganglion;heart;trigeminal ganglion;skeletal muscle; 0.07780 0.22685 -0.383807564 27.41802312 7.89568 0.28992 MYL4 0.000175624794353708 0.457949949862897 0.541874425342749 myosin light chain 4 FUNCTION: Regulatory light chain of myosin. Does not bind calcium.; . . unclassifiable (Anatomical System);myocardium;heart;blood;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;whole body;lung;macula lutea;visual apparatus;liver;testis;spleen;germinal center;pineal gland; superior cervical ganglion;fetal liver;heart;trigeminal ganglion;skeletal muscle;bone marrow; 0.89649 0.23208 0.038710339 56.92380278 63.42409 1.63054 MYL5 4.42986035820118e-08 0.0599169140985966 0.9400830416028 myosin light chain 5 . . TISSUE SPECIFICITY: Expressed in fetal skeletal muscle and retina.; . . 0.20822 . 1.372468937 94.48572777 760.07335 5.46406 MYL6 0.256616370152787 0.715950407777271 0.027433222069942 myosin light chain 6 FUNCTION: Regulatory light chain of myosin. Does not bind calcium.; . . myocardium;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;vein;uterus;whole body;synovium;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;duodenum;kidney;stomach;aorta; superior cervical ganglion;smooth muscle;heart;globus pallidus;ciliary ganglion; 0.17736 0.17050 0.281220278 71.07808445 101.36352 2.17936 MYL6B 0.00373381128610738 0.847429292044168 0.148836896669725 myosin light chain 6B FUNCTION: Regulatory light chain of myosin. Does not bind calcium.; . . ovary;salivary gland;developmental;intestine;colon;parathyroid;choroid;prostate;optic nerve;bone;pituitary gland;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;spinal cord;muscle;pharynx;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;alveolus;cervix;kidney;mammary gland;stomach;thymus; amygdala;whole brain;medulla oblongata;testis - interstitial;occipital lobe;hypothalamus;temporal lobe;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;fetal brain;prefrontal cortex;globus pallidus;testis;cingulate cortex;parietal lobe; 0.11121 0.10864 -0.317668748 31.45789101 13.07717 0.47617 MYL6BP1 . . . myosin light chain 6B pseudogene 1 . . . . . . . . . . . MYL6P1 . . . myosin light chain 6 pseudogene 1 . . . . . . . . . . . MYL6P2 . . . myosin light chain 6 pseudogene 2 . . . . . . . . . . . MYL6P3 . . . myosin light chain 6 pseudogene 3 . . . . . . . . . . . MYL6P4 . . . myosin light chain 6 pseudogene 4 . . . . . . . . . . . MYL6P5 . . . myosin light chain 6 pseudogene 5 . . . . . . . . . . . MYL7 3.65494513796836e-06 0.203237501627064 0.796758843427798 myosin light chain 7 . . TISSUE SPECIFICITY: Predominantly expressed in adult atrial muscle. {ECO:0000269|PubMed:1429676}.; myocardium;pancreas;lung;whole body;heart;liver;testis;spleen; heart; 0.55028 0.13374 0.170987912 65.5579146 16.76811 0.58964 MYL8P . . . myosin light chain 8, pseudogene . . . . . . . . . . . MYL9 0.0660421350679322 0.731210254134931 0.202747610797136 myosin light chain 9 FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion.; . TISSUE SPECIFICITY: Smooth muscle tissues and in some, but not all, nonmuscle cells.; myocardium;medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;oesophagus;endometrium;bone;thyroid;iris;testis;amniotic fluid;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pineal body;muscle;adrenal cortex;lens;skeletal muscle;bile duct;pancreas;lung;trachea;adrenal gland;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;mammary gland;aorta;stomach;peripheral nerve; dorsal root ganglion;testis - interstitial;smooth muscle;olfactory bulb;adipose tissue;ovary;heart;adrenal cortex;uterus;uterus corpus;prostate;trachea;testis - seminiferous tubule;adrenal gland;placenta;appendix;testis;ciliary ganglion; 0.28375 0.14896 -0.163345027 41.24793583 11.43011 0.41271 MYL10 0.00804655016342347 0.787601238979506 0.204352210857071 myosin light chain 10 . . . . . . . -0.405853867 26.23260203 129.96827 2.48355 MYL12A 0.00150150767485969 0.4417978090091 0.55670068331604 myosin light chain 12A FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity). {ECO:0000250}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;amniotic fluid;bladder;brain;gall bladder;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;bone;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;kidney;stomach;aorta;thymus; . . . 0.035072054 56.2514744 12.59471 0.45985 MYL12AP1 . . . myosin light chain 12A pseudogene 1 . . . . . . . . . . . MYL12B 0.290511998767659 0.627274200590041 0.0822138006423001 myosin light chain 12B FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Phosphorylation triggers actin polymerization in vascular smooth muscle. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity). {ECO:0000250, ECO:0000269|PubMed:10965042}.; . TISSUE SPECIFICITY: Ubiquitously expressed in various hematopoietic cells. {ECO:0000269|PubMed:11436981, ECO:0000269|PubMed:18480596}.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;vein;uterus;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;kidney;stomach;aorta; adipose tissue;placenta;whole blood; . . 0.035072054 56.2514744 . . MYL12BP1 . . . myosin light chain 12B pseudogene 1 . . . . . . . . . . . MYL12BP2 . . . myosin light chain 12B pseudogene 2 . . . . . . . . . . . MYLIP 0.020226886854297 0.961861861428331 0.0179112517173721 myosin regulatory light chain interacting protein FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Activity depends on E2 enzymes of the UBE2D family. Proteasomal degradation of MRLC leads to inhibit neurite outgrowth in presence of NGF by counteracting the stabilization of MRLC by saposin-like protein (CNPY2/MSAP) and reducing CNPY2-stimulated neurite outgrowth. Acts as a sterol- dependent inhibitor of cellular cholesterol uptake by mediating ubiquitination and subsequent degradation of LDLR. {ECO:0000269|PubMed:10593918, ECO:0000269|PubMed:12826659, ECO:0000269|PubMed:14550572, ECO:0000269|PubMed:19520913, ECO:0000269|PubMed:20427281, ECO:0000269|PubMed:22109552}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10593918}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; placenta;testis; 0.20114 0.15161 0.352813824 74.49280491 86.29181 1.98393 MYLK 9.37919861515833e-06 0.999990573775839 4.70255455066167e-08 myosin light chain kinase FUNCTION: Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA- dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis. {ECO:0000269|PubMed:11113114, ECO:0000269|PubMed:11976941, ECO:0000269|PubMed:15020676, ECO:0000269|PubMed:15825080, ECO:0000269|PubMed:16284075, ECO:0000269|PubMed:16723733, ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:18710790, ECO:0000269|PubMed:19826488, ECO:0000269|PubMed:20139351, ECO:0000269|PubMed:20181817, ECO:0000269|PubMed:20375339, ECO:0000269|PubMed:20453870}.; DISEASE: Aortic aneurysm, familial thoracic 7 (AAT7) [MIM:613780]: A disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance. {ECO:0000269|PubMed:21055718}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Smooth muscle and non-muscle isozymes are expressed in a wide variety of adult and fetal tissues and in cultured endothelium with qualitative expression appearing to be neither tissue- nor development-specific. Non-muscle isoform 2 is the dominant splice variant expressed in various tissues. Telokin has been found in a wide variety of adult and fetal tissues. Accumulates in well differentiated enterocytes of the intestinal epithelium in response to tumor necrosis factor (TNF). {ECO:0000269|PubMed:10536370, ECO:0000269|PubMed:16835238, ECO:0000269|PubMed:20053363, ECO:0000269|PubMed:8575746}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;ciliary body;brain;gall bladder;heart;cartilage;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;artery;spinal ganglion;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;aorta;stomach; uterus;uterus corpus;prostate;testis - interstitial;appendix;testis; 0.23578 . -0.323627113 30.93300307 6562.91179 17.06993 MYLK-AS1 . . . MYLK antisense RNA 1 . . . . . . . . . . . MYLK-AS2 . . . MYLK antisense RNA 2 . . . . . . . . . . . MYLK2 0.220320911579183 0.777967366007585 0.00171172241323242 myosin light chain kinase 2 FUNCTION: Implicated in the level of global muscle contraction and cardiac function. Phosphorylates a specific serine in the N- terminus of a myosin light chain. {ECO:0000269|PubMed:11733062}.; . TISSUE SPECIFICITY: Heart and skeletal muscles. Increased expression in the apical tissue compared to the interventricular septal tissue.; . . 0.34893 0.14961 -0.242430445 36.22906346 296.01659 3.67304 MYLK3 0.14096753512483 0.858863138249247 0.000169326625922834 myosin light chain kinase 3 FUNCTION: Kinase that phosphorylates MYL2 in vitro. Promotes sarcomere formation in cardiomyocytes and increases cardiomyocyte contractility (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Restricted to heart. {ECO:0000269|PubMed:17885681}.; . . 0.10078 0.14157 -1.262067713 5.284265157 1693.81387 7.58697 MYLK4 1.65850133719676e-11 0.0296860765262981 0.970313923457117 myosin light chain kinase family member 4 . . . unclassifiable (Anatomical System);atrium;lung;heart;cochlea;endometrium;testis;kidney;bladder; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.21886 0.11770 0.418953042 77.06416608 2435.02572 9.16576 MYLKP1 . . . myosin light chain kinase pseudogene 1 . . . . . . . . . . . MYLPF 0.602001132166449 0.388981163846745 0.00901770398680528 myosin light chain, phosphorylatable, fast skeletal muscle . . TISSUE SPECIFICITY: Expressed in fetal and adult skeletal muscle. {ECO:0000269|PubMed:14756420}.; unclassifiable (Anatomical System);heart;tongue;muscle;developmental;blood;skeletal muscle;bone marrow;greater omentum;prostate;pancreas;whole body;lung;visual apparatus;alveolus;liver;testis;head and neck;spleen;kidney;mammary gland;peripheral nerve; tongue;thyroid;testis;fetal thyroid;skeletal muscle; . . -0.273576253 33.97027601 26.03649 0.84633 MYMY1 . . . moyamoya disease 1 . . . . . . . . . . . MYMY3 . . . moyamoya disease 3 . . . . . . . . . . . MYNN 0.650144393600751 0.349600695752897 0.000254910646352206 myoneurin . . TISSUE SPECIFICITY: Mainly expressed in the neuromuscular system. Located in and around synaptic myonuclei in adult muscle. Expression is dysregulated after nerve injury. Also found in the testis, ovary and placenta. {ECO:0000269|PubMed:10873615, ECO:0000269|PubMed:14694499}.; ovary;colon;parathyroid;skin;uterus;prostate;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;liver;hypopharynx;amnion;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.31126 0.10229 -0.314027422 31.9297004 65.43237 1.66559 MYO1A 1.94521735757924e-35 4.23822671139102e-06 0.999995761773289 myosin IA FUNCTION: Involved in directing the movement of organelles along actin filaments. {ECO:0000305}.; . . unclassifiable (Anatomical System);ovary;colon;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe; 0.06968 0.09806 0.79175097 87.30832744 1076.47129 6.28850 MYO1B 0.878004107551654 0.121995892412533 3.58125246077405e-11 myosin IB FUNCTION: Motor protein that may participate in process critical to neuronal development and function such as cell migration, neurite outgrowth and vesicular transport. {ECO:0000250}.; . . ovary;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;islets of Langerhans;pancreas;lung;pia mater;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;heart;ciliary ganglion;trigeminal ganglion;skin;skeletal muscle; 0.16430 0.14154 -1.216154 5.667610285 114.8554 2.33278 MYO1C 3.89020504800004e-08 0.999974909788734 2.50513092150798e-05 myosin IC FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes. {ECO:0000269|PubMed:24636949}.; . . smooth muscle;ovary;salivary gland;colon;choroid;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;synovium;larynx;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;placenta;visual apparatus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.24832 0.21196 -1.113491624 6.634819533 761.68047 5.47188 MYO1D 3.30325770821959e-09 0.999137494888209 0.000862501808533007 myosin ID FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in many tissues. Highest levels in brain, followed by lung and ovary; expression is lowest in spleen.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;nervous;tongue;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; adipose tissue;thyroid; 0.88849 0.15388 -0.639268965 16.70794999 274.32626 3.54760 MYO1E 0.0479778930717418 0.952022092725196 1.42030619920592e-08 myosin IE FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain. Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14. {ECO:0000269|PubMed:11940582, ECO:0000269|PubMed:17257598, ECO:0000269|PubMed:20860408}.; . TISSUE SPECIFICITY: Expressed in the immune system. In the kidney, predominantly expressed in the glomerulus, including podocytes. {ECO:0000269|PubMed:21458045, ECO:0000269|PubMed:21756023}.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;fetal liver;atrioventricular node;trigeminal ganglion;bone marrow; 0.38966 0.13153 -1.142761145 6.375324369 113.48807 2.31950 MYO1F 0.158022191479258 0.841977806619034 1.90170815920205e-09 myosin IF FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;blood;fovea centralis;choroid;lens;retina;bone marrow;uterus;pancreas;optic nerve;lung;nasopharynx;bone;placenta;macula lutea;iris;alveolus;testis;kidney;brain;mammary gland; white blood cells;whole blood;bone marrow; 0.37121 0.20079 -1.828205761 2.123142251 209.12294 3.12186 MYO1G 7.64108904488102e-07 0.999791514134283 0.000207721756812161 myosin IG FUNCTION: Unconventional myosin required during immune response for detection of rare antigen-presenting cells by regulating T- cell migration. Unconventional myosins are actin-based motor molecules with ATPase activity and serve in intracellular movements. Acts as a regulator of T-cell migration by generating membrane tension, enforcing cell-intrinsic meandering search, thereby enhancing detection of rare antigens during lymph-node surveillance, enabling pathogen eradication. Also required in B- cells, where it regulates different membrane/cytoskeleton- dependent processes. Involved in Fc-gamma receptor (Fc-gamma-R) phagocytosis. {ECO:0000250|UniProtKB:Q5SUA5}.; . TISSUE SPECIFICITY: Specifically expressed in hematopoietic cells. {ECO:0000269|PubMed:11544309, ECO:0000269|PubMed:20071333}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;cartilage;heart;colon;blood;skin;bone marrow;uterus;optic nerve;lung;placenta;alveolus;liver;testis;cervix;spleen;germinal center;thymus; superior cervical ganglion;ciliary ganglion;white blood cells;trigeminal ganglion; 0.15053 0.12225 -0.832257622 11.50625147 1726.64144 7.66669 MYO1H 2.91611360098295e-17 0.365254710934844 0.634745289065156 myosin IH FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). {ECO:0000250}.; . . uterus;heart;bone;skin; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.18215 . -0.547447733 19.99882048 2516.66481 9.35299 MYO3A 6.58594533648526e-30 0.00399130898019486 0.996008691019805 myosin IIIA FUNCTION: Probable actin-based motor with a protein kinase activity. Probably plays a role in vision and hearing. {ECO:0000269|PubMed:12032315}.; . TISSUE SPECIFICITY: Strongest expression in retina, retinal pigment epithelial cells, cochlea and pancreas.; unclassifiable (Anatomical System);breast;lung;whole body;islets of Langerhans;hypothalamus;testis;retina; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.16492 0.16519 0.999350036 90.6581741 8149.62252 19.48902 MYO3B 4.47146671165632e-20 0.847647937712886 0.152352062287114 myosin IIIB FUNCTION: Probable actin-based motor with a protein kinase activity.; . TISSUE SPECIFICITY: Expressed in retina, kidney and testis.; unclassifiable (Anatomical System);lung;testis; superior cervical ganglion;testis - interstitial;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.18147 . 2.32796338 98.37815523 4646.99712 13.72770 MYO5A 0.992129667219065 0.00787033278093503 1.28468099484988e-17 myosin VA FUNCTION: Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation. {ECO:0000269|PubMed:10448864}.; DISEASE: Griscelli syndrome 3 (GS3) [MIM:609227]: Rare autosomal recessive disorder characterized by pigmentary dilution of the skin and hair, the presence of large clumps of pigment in hair shafts, and an accumulation of melanosomes in melanocytes, without other clinical manifestations. {ECO:0000269|PubMed:12897212}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Elejalde syndrome (ELEJAS) [MIM:256710]: Autosomal recessive condition characterized by skin hypopigmentation, the presence of large clumps of pigment in hair shafts, silvery-gray hair, accumulation of melanosomes in melanocytes and primary neurological abnormalities. Elejalde syndrome may be the same entity as Griscelli syndrome type I. {ECO:0000269|PubMed:12058346}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in melanocytes.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;thyroid;bone;testis;germinal center;ciliary body;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;temporal lobe;ciliary ganglion;pons;trigeminal ganglion; 0.52387 0.38794 -1.40918166 4.146025006 1840.50511 7.91363 MYO5B 5.4231747689238e-10 0.999999838766977 1.60690705836165e-07 myosin VB FUNCTION: May be involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Required in a complex with RAB11A and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Together with RAB11A participates in CFTR trafficking to the plasma membrane and TF (transferrin) recycling in nonpolarized cells. Together with RAB11A and RAB8A participates in epithelial cell polarization. Together with RAB25 regulates transcytosis. {ECO:0000269|PubMed:21206382, ECO:0000269|PubMed:21282656}.; DISEASE: Diarrhea 2, with microvillus atrophy (DIAR2) [MIM:251850]: A disease characterized by onset of intractable life-threatening watery diarrhea during infancy. Two forms are recognized: early-onset microvillus inclusion disease with diarrhea beginning in the neonatal period, and late-onset, with first symptoms appearing after 3 or 4 months of life. {ECO:0000269|PubMed:18724368, ECO:0000269|PubMed:19006234, ECO:0000269|PubMed:20186687, ECO:0000269|PubMed:21206382, ECO:0000269|PubMed:24138727, ECO:0000269|PubMed:24892806}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;testis;dura mater;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;lens;skeletal muscle;bile duct;breast;pia mater;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;pons;kidney;trigeminal ganglion;skeletal muscle; 0.24660 0.18021 -0.371352359 28.20830385 8115.22364 19.46932 MYO5BP1 . . . myosin VB pseudogene 1 . . . . . . . . . . . MYO5BP2 . . . myosin VB pseudogene 2 . . . . . . . . . . . MYO5BP3 . . . myosin VB pseudogene 3 . . . . . . . . . . . MYO5C 4.34872218862826e-18 0.999935519974499 6.44800255007283e-05 myosin VC FUNCTION: May be involved in transferrin trafficking. Likely to power actin-based membrane trafficking in many physiologically crucial tissues.; . TISSUE SPECIFICITY: Expressed chiefly in non-neuronal tissues. Particularly abundant in epithelial and glandular tissues including pancreas, prostate, mammary, stomach, colon and lung. {ECO:0000269|PubMed:11870218}.; ovary;umbilical cord;colon;retina;uterus;prostate;endometrium;cerebral cortex;thyroid;testis;spinal ganglion;bladder;unclassifiable (Anatomical System);cartilage;lacrimal gland;islets of Langerhans;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.56649 0.24906 0.308535022 72.38735551 3687.50192 11.83098 MYO6 0.0177883990936548 0.982211600378647 5.27698444208756e-10 myosin VI FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets. Required for structural integrity of inner ear hair cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:10519557, ECO:0000269|PubMed:11447109, ECO:0000269|PubMed:16507995, ECO:0000269|PubMed:16949370}.; DISEASE: Deafness, autosomal dominant, 22 (DFNA22) [MIM:606346]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA22 is progressive and postlingual, with onset during childhood. By the age of approximately 50 years, affected individuals invariably have profound sensorineural deafness. {ECO:0000269|PubMed:11468689}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal recessive, 37 (DFNB37) [MIM:607821]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:12687499}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, sensorineural, with hypertrophic cardiomyopathy (DFNHCM) [MIM:606346]: An autosomal dominant sensorineural deafness associated with hypertrophic cardiomyopathy. {ECO:0000269|PubMed:15060111}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in most tissues examined including heart, brain, placenta, pancreas, spleen, thymus, prostate, testis, ovary, small intestine and colon. Highest levels in brain, pancreas, testis and small intestine. Also expressed in fetal brain and cochlea. Isoform 1 and isoform 2, containing the small insert, and isoform 4, containing neither insert, are expressed in unpolarized epithelial cells. {ECO:0000269|PubMed:9259267}.; . . 0.26137 0.31948 -0.369255208 28.25548478 419.15519 4.27823 MYO7A 5.37673856270135e-25 0.207164598627406 0.792835401372594 myosin VIIA FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. In the retina, plays an important role in the renewal of the outer photoreceptor disks. Plays an important role in the distribution and migration of retinal pigment epithelial (RPE) melanosomes and phagosomes, and in the regulation of opsin transport in retinal photoreceptors. In the inner ear, plays an important role in differentiation, morphogenesis and organization of cochlear hair cell bundles. Involved in hair-cell vesicle trafficking of aminoglycosides, which are known to induce ototoxicity (By similarity). Motor protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal hearing. {ECO:0000250, ECO:0000269|PubMed:19643958, ECO:0000269|PubMed:21493626, ECO:0000269|PubMed:21687988, ECO:0000269|PubMed:21709241}.; DISEASE: Usher syndrome 1B (USH1B) [MIM:276900]: USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa with sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). USH1 is characterized by profound congenital sensorineural deafness, absent vestibular function and prepubertal onset of progressive retinitis pigmentosa leading to blindness. {ECO:0000269|PubMed:10094549, ECO:0000269|PubMed:10364543, ECO:0000269|PubMed:10447383, ECO:0000269|PubMed:10930322, ECO:0000269|PubMed:12112664, ECO:0000269|PubMed:15660226, ECO:0000269|PubMed:16679490, ECO:0000269|PubMed:23559863, ECO:0000269|PubMed:24831256, ECO:0000269|PubMed:25798947, ECO:0000269|PubMed:7870171, ECO:0000269|PubMed:8900236, ECO:0000269|PubMed:9002678, ECO:0000269|PubMed:9382091, ECO:0000269|PubMed:9718356}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal recessive, 2 (DFNB2) [MIM:600060]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:9171832, ECO:0000269|PubMed:9171833}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal dominant, 11 (DFNA11) [MIM:601317]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA11 is characterized by onset after complete speech acquisition and subsequent gradual progression. {ECO:0000269|PubMed:15121790, ECO:0000269|PubMed:15221449, ECO:0000269|PubMed:15300860, ECO:0000269|PubMed:9354784}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in MYO7A may be a cause of Leber congenital amaurosis (LCA), a severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near- absent pupillary responses, photophobia, high hyperopia and keratoconus.; TISSUE SPECIFICITY: Expressed in the pigment epithelium and the photoreceptor cells of the retina. Also found in kidney, liver, testis, cochlea, lymphocytes. Not expressed in brain. {ECO:0000269|PubMed:19643958, ECO:0000269|PubMed:21493626, ECO:0000269|PubMed:21709241}.; unclassifiable (Anatomical System);medulla oblongata;ovary;colon;parathyroid;choroid;retina;breast;uterus;prostate;optic nerve;lung;endometrium;adrenal gland;thyroid;placenta;visual apparatus;liver;testis;spleen;germinal center;kidney;brain;pineal gland;peripheral nerve; superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;adrenal gland;adrenal cortex;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12096 0.33881 -2.513092117 0.925925926 4945.67513 14.33992 MYO7B 6.3829496749846e-16 0.999852792996655 0.000147207003344335 myosin VIIB FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. May be have a role in the apical membranes of transporting epithelia (By similarity). {ECO:0000250}.; . . liver;brain;skeletal muscle; dorsal root ganglion;medulla oblongata;testis - interstitial;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.11748 . 1.019668216 90.92356688 5040.89055 14.51846 MYO9A 0.999991725771394 8.2742286060295e-06 3.49330660269938e-24 myosin IXA FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Regulates Rho activity in neurons, has a role in the regulation of neuronal morphology and function (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Found to be expressed in testis and placenta, and at lower levels in all the examined tissues with the exception of liver. Isoform 5 was found in leukocytes but not in brain, retina or testis. {ECO:0000269|PubMed:10409426}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;cingulate cortex; 0.76633 0.11338 -0.702137274 14.78532673 1190.95284 6.54335 MYO9B 0.999998877096737 1.12290326289238e-06 1.15724672992804e-18 myosin IXB FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. May be involved in the remodeling of the actin cytoskeleton. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions. Also acts as a GTPase activating protein on Rho.; . TISSUE SPECIFICITY: Expressed predominantly in peripheral blood leukocytes and at lower levels, in thymus, spleen, testis, prostate, ovary, brain, small intestine and lung.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; dorsal root ganglion;medulla oblongata;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle;parietal lobe; 0.19211 0.36423 -0.858313724 10.92828497 547.26349 4.75747 MYO10 0.00396952046057879 0.996030479531536 7.88547499780373e-12 myosin X FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. May play a role in neurite outgrowth and axon guidance. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation. Plays a role in formation of the podosome belt in osteoclasts. {ECO:0000269|PubMed:16894163, ECO:0000269|PubMed:18570893}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10984435}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;tongue;spinal cord;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach; dorsal root ganglion;amygdala;occipital lobe;superior cervical ganglion;prefrontal cortex;appendix;caudate nucleus;trigeminal ganglion; 0.45378 0.20308 -1.611828042 2.972399151 8073.2738 19.39142 MYO15A . . . myosin XVA FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. Required for the arrangement of stereocilia in mature hair bundles (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in pituitary. Also expressed at lower levels in adult brain, kidney, liver, lung, pancreas, placenta and skeletal muscle. Not expressed in brain. In the pituitary, highly expressed in anterior gland cells. {ECO:0000269|PubMed:10552926}.; unclassifiable (Anatomical System);medulla oblongata;lung;ovary;testis;blood; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.38072 0.15993 -1.25610141 5.349138948 5977.14295 16.09179 MYO15B . . . myosin XVB FUNCTION: Unknown, due to the absence of a functional motor domain.; . TISSUE SPECIFICITY: Detected in brain, stomach and kidney.; sympathetic chain;colon;skin;bone marrow;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;small intestine;cartilage;blood;skeletal muscle;breast;lung;epididymis;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; . 0.14983 0.11459 . . 4109.50851 12.72624 MYO16 0.998667245865902 0.00133275413409514 2.45208657910204e-15 myosin XVI FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. May be involved in targeting of the catalytic subunit of protein phosphatase 1 during brain development. Activates PI3K and concomitantly recruits the WAVE1 complex to the close vicinity of PI3K and regulates neuronal morphogenesis (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);optic nerve;lung;macula lutea;liver;spleen;fovea centralis;choroid;lens;retina; dorsal root ganglion;superior cervical ganglion;fetal brain;testis - seminiferous tubule;temporal lobe;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.36502 0.09267 0.062366261 58.53385232 6065.52777 16.24806 MYO16-AS1 . . . MYO16 antisense RNA 1 . . . . . . . . . . . MYO16-AS2 . . . MYO16 antisense RNA 2 . . . . . . . . . . . MYO18A 0.999417503618365 0.000582496381634401 3.26206223663743e-16 myosin XVIIIA FUNCTION: May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. May be involved in the maintenance of the stromal cell architectures required for cell to cell contact. {ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:19837035, ECO:0000269|PubMed:23345592}.; . . myocardium;ovary;sympathetic chain;colon;choroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; . 0.45342 0.14389 -1.618952458 2.895730125 551.10541 4.77410 MYO18B 2.61207132683228e-15 0.999996059999035 3.94000096240262e-06 myosin XVIIIB FUNCTION: May be involved in intracellular trafficking of the muscle cell when in the cytoplasm, whereas entering the nucleus, may be involved in the regulation of muscle specific genes. May play a role in the control of tumor development and progression; restored MYO18B expression in lung cancer cells suppresses anchorage-independent growth.; . TISSUE SPECIFICITY: Selectively expressed in cardiac and skeletal muscles. Weakly expressed in testis, pancreas, placenta, prostate, lung and thymus.; unclassifiable (Anatomical System);lymph node;heart;larynx;visual apparatus;liver;testis;spleen;head and neck;skeletal muscle;retina; atrioventricular node; 0.16167 0.10792 1.205427351 93.02311866 5231.65918 14.90607 MYO19 2.43129360080767e-18 0.0516761389340699 0.94832386106593 myosin XIX FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. MYO19 is involved in mitochondrial motility. {ECO:0000269|PubMed:19932026}.; . TISSUE SPECIFICITY: Widely expressed in multiple tissues and cell lines. {ECO:0000269|PubMed:19932026}.; lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.23398 . 0.521707177 80.39631989 3142.45814 10.67569 MYOC 5.01978488588844e-08 0.387163844675163 0.612836105126988 myocilin FUNCTION: Secreted glycoprotein regulating the activation of different signaling pathways in adjacent cells to control different processes including cell adhesion, cell-matrix adhesion, cytoskeleton organization and cell migration. Promotes substrate adhesion, spreading and formation of focal contacts. Negatively regulates cell-matrix adhesion and stress fiber assembly through Rho protein signal transduction. Modulates the organization of actin cytoskeleton by stimulating the formation of stress fibers through interactions with components of Wnt signaling pathways. Promotes cell migration through activation of PTK2 and the downstream phosphatidylinositol 3-kinase signaling. Plays a role in bone formation and promotes osteoblast differentiation in a dose-dependent manner through mitogen-activated protein kinase signaling. Mediates myelination in the peripheral nervous system through ERBB2/ERBB3 signaling. Plays a role as a regulator of muscle hypertrophy through the components of dystrophin-associated protein complex. Involved in positive regulation of mitochondrial depolarization. Plays a role in neurite outgrowth. May participate in the obstruction of fluid outflow in the trabecular meshwork. {ECO:0000250|UniProtKB:O70624, ECO:0000269|PubMed:17516541, ECO:0000269|PubMed:17984096, ECO:0000269|PubMed:18855004, ECO:0000269|PubMed:19188438, ECO:0000269|PubMed:19959812, ECO:0000269|PubMed:21656515, ECO:0000269|PubMed:23629661, ECO:0000269|PubMed:23897819}.; DISEASE: Glaucoma 1, open angle, A (GLC1A) [MIM:137750]: A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. {ECO:0000269|PubMed:10196380, ECO:0000269|PubMed:10330365, ECO:0000269|PubMed:10340788, ECO:0000269|PubMed:10644174, ECO:0000269|PubMed:10798654, ECO:0000269|PubMed:10819638, ECO:0000269|PubMed:10873982, ECO:0000269|PubMed:10916185, ECO:0000269|PubMed:10980537, ECO:0000269|PubMed:11004290, ECO:0000269|PubMed:11774072, ECO:0000269|PubMed:12189160, ECO:0000269|PubMed:12356829, ECO:0000269|PubMed:12362081, ECO:0000269|PubMed:12442283, ECO:0000269|PubMed:12860809, ECO:0000269|PubMed:12872267, ECO:0000269|PubMed:15025728, ECO:0000269|PubMed:15255110, ECO:0000269|PubMed:15534471, ECO:0000269|PubMed:16401791, ECO:0000269|PubMed:17210859, ECO:0000269|PubMed:17499207, ECO:0000269|PubMed:9005853, ECO:0000269|PubMed:9328473, ECO:0000269|PubMed:9345106, ECO:0000269|PubMed:9361308, ECO:0000269|PubMed:9490287, ECO:0000269|PubMed:9510647, ECO:0000269|PubMed:9521427, ECO:0000269|PubMed:9535666, ECO:0000269|PubMed:9697688, ECO:0000269|PubMed:9792882, ECO:0000269|PubMed:9863594}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Glaucoma 3, primary congenital, A (GLC3A) [MIM:231300]: An autosomal recessive form of primary congenital glaucoma (PCG). PCG is characterized by marked increase of intraocular pressure at birth or early childhood, large ocular globes (buphthalmos) and corneal edema. It results from developmental defects of the trabecular meshwork and anterior chamber angle of the eye that prevent adequate drainage of aqueous humor. {ECO:0000269|PubMed:15733270}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. MYOC mutations may contribute to GLC3A via digenic inheritance with CYP1B1 and/or another locus associated with the disease (PubMed:15733270). {ECO:0000269|PubMed:15733270}.; TISSUE SPECIFICITY: Detected in aqueous humor (PubMed:12697062). Detected in the eye (at protein level) (PubMed:11431441). Widely expressed. Highly expressed in various types of muscle, ciliary body, papillary sphincter, skeletal muscle, heart, and bone marrow-derived mesenchymal stem cells. Expressed predominantly in the retina. In normal eyes, found in the inner uveal meshwork region and the anterior portion of the meshwork. In contrast, in many glaucomatous eyes, it is found in more regions of the meshwork and seems to be expressed at higher levels than in normal eyes, regardless of the type or clinical severity of glaucoma. The myocilin 35 kDa fragment is detected in aqueous humor and at to a lesser extend in iris and ciliary body. {ECO:0000269|PubMed:11431441, ECO:0000269|PubMed:12697062, ECO:0000269|PubMed:15795224}.; unclassifiable (Anatomical System);heart;colon;skeletal muscle;skin;retina;uterus;prostate;optic nerve;lung;cochlea;cerebral cortex;trabecular meshwork;thyroid;visual apparatus;iris;testis;ciliary body;brain;aorta;stomach; trachea;tongue;thyroid;ciliary ganglion;skeletal muscle; 0.49164 0.41045 -0.134019284 43.90776126 839.33434 5.67376 MYOCD 0.934596479106262 0.0654034164100375 1.04483700515866e-07 myocardin FUNCTION: Smooth muscle cells (SM) and cardiac muscle cells- specific transcriptional factor which uses the canonical single or multiple CArG boxes DNA sequence. Acts as a cofactor of serum response factor (SRF) with the potential to modulate SRF-target genes. Plays a crucial role in cardiogenesis and differentiation of the smooth muscle cell lineage (myogenesis) (By similarity). {ECO:0000250, ECO:0000269|PubMed:12640126}.; . TISSUE SPECIFICITY: Expressed in heart, aorta, and in smooth muscle cell-containing tissues: stomach, bladder, small intestine, colon, lung, placenta and uterus. Very faint expression in prostate and skeletal muscle. {ECO:0000269|PubMed:12640126, ECO:0000269|PubMed:20385216}.; placenta;testis; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.45281 0.21621 -0.679732631 15.39278132 548.16617 4.76212 MYOD1 2.68321885548831e-05 0.179408522932306 0.820564644879139 myogenic differentiation 1 FUNCTION: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation. Together with MYF5 and MYOG, co-occupies muscle-specific gene promoter core region during myogenesis. Induces fibroblasts to differentiate into myoblasts. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both proteins (By similarity). {ECO:0000250}.; . . optic nerve;lymph node;ovary;placenta;macula lutea;muscle;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina; superior cervical ganglion;subthalamic nucleus;atrioventricular node;skeletal muscle; 0.98457 0.81987 -0.139478553 43.29440906 46.46862 1.31517 MYOF 2.08401244116976e-36 0.259659118287117 0.740340881712883 myoferlin FUNCTION: Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in myoblast and endothelial cells (at protein level). Highly expressed in cardiac and skeletal muscles. Also present in lung, and at very low levels in kidney, placenta and brain. {ECO:0000269|PubMed:11959863, ECO:0000269|PubMed:17702744, ECO:0000269|PubMed:18502764}.; smooth muscle;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;endometrium;larynx;bone;thyroid;iris;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;amnion;alveolus;hypopharynx;liver;cervix;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion; 0.19502 0.13376 -0.435697896 24.68152866 2094.22471 8.43082 MYOG 0.740012060346863 0.248827750953353 0.0111601886997848 myogenin (myogenic factor 4) FUNCTION: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation, cell cycle exit and muscle atrophy. Essential for the development of functional embryonic skeletal fiber muscle differentiation. However is dispensable for postnatal skeletal muscle growth; phosphorylation by CAMK2G inhibits its transcriptional activity in respons to muscle activity. Required for the recruitment of the FACT complex to muscle-specific promoter regions, thus promoting gene expression initiation. During terminal myoblast differentiation, plays a role as a strong activator of transcription at loci with an open chromatin structure previously initiated by MYOD1. Together with MYF5 and MYOD1, co-occupies muscle-specific gene promoter core regions during myogenesis. Cooperates also with myocyte-specific enhancer factor MEF2D and BRG1-dependent recruitment of SWI/SNF chromatin- remodeling enzymes to alter chromatin structure at myogenic late gene promoters. Facilitates cell cycle exit during terminal muscle differentiation through the up-regulation of miR-20a expression, which in turn represses genes involved in cell cycle progression. Binds to the E-box containing (E1) promoter region of the miR-20a gene. Plays also a role in preventing reversal of muscle cell differentiation. Contributes to the atrophy-related gene expression in adult denervated muscles. Induces fibroblasts to differentiate into myoblasts (By similarity). {ECO:0000250}.; . . lung;placenta;testis; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.77981 0.62662 0.549415813 81.38122199 191.78546 3.00276 MYOM1 1.077002599654e-21 0.781731913199784 0.218268086800217 myomesin 1 FUNCTION: Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent.; . . myocardium;heart;ovary;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;atrium;lung;placenta;bone;macula lutea;visual apparatus;liver;testis;brain;stomach; dorsal root ganglion;skeletal muscle; 0.11853 0.11159 0.560208936 81.67610285 5839.02483 15.83754 MYOM2 1.48718449693549e-55 7.78222893875632e-11 0.999999999922178 myomesin 2 FUNCTION: Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent.; . . myocardium;colon;choroid;fovea centralis;skin;retina;uterus;optic nerve;atrium;frontal lobe;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);heart;spinal cord;lens;skeletal muscle;lung;placenta;macula lutea;liver;alveolus;head and neck;kidney;peripheral nerve; skeletal muscle; 0.22436 0.11601 -0.500487825 21.84477471 8300.21663 19.71178 MYOM3 9.28408886540307e-28 0.0102845049702553 0.989715495029745 myomesin 3 FUNCTION: May link the intermediate filament cytoskeleton to the M-disk of the myofibrils in striated muscle. {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;smooth muscle;heart;muscle;liver;kidney;skin;skeletal muscle; dorsal root ganglion;medulla oblongata;superior cervical ganglion;globus pallidus;ciliary ganglion;caudate nucleus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.13881 0.09984 1.162914409 92.65156877 15097.7948 26.68075 MYOT 2.64170747311334e-05 0.923791149959938 0.076182432965331 myotilin FUNCTION: Component of a complex of multiple actin cross-linking proteins. Involved in the control of myofibril assembly and stability at the Z lines in muscle cells. {ECO:0000269|PubMed:12499399}.; DISEASE: Myopathy, myofibrillar, 3 (MFM3) [MIM:609200]: A neuromuscular disorder characterized by progressive skeletal muscle weakness greater distally than proximally, tight heel cords, hyporeflexia, cardiomyopathy and peripheral neuropathy in some patients. Affected muscle exhibits disorganization and streaming of the Z-line, presence of large hyaline structures, excessive accumulation of myotilin and other ectopically expressed proteins and prominent congophilic deposits. {ECO:0000269|PubMed:15111675}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spheroid body myopathy (SBM) [MIM:182920]: Autosomal dominant form of myofibrillar myopathy (MFM), characterized by slowly progressing proximal muscle weakness and dysarthric nasal speech. There is no evidence of cardiomyopathy. Muscle biopsy shows spheroid bodies within the type I muscle fibers. {ECO:0000269|PubMed:16380616}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level). Expressed in skeletal muscle, heart, bone marrow and thyroid gland. {ECO:0000269|PubMed:10369880, ECO:0000269|PubMed:10486214}.; unclassifiable (Anatomical System);heart;ovary;sympathetic chain;parathyroid;skin;skeletal muscle;uterus;prostate;whole body;lung;larynx;trabecular meshwork;placenta;liver;testis;head and neck;brain; superior cervical ganglion;tongue;thyroid;appendix;atrioventricular node;skeletal muscle; 0.60563 0.22710 -0.312207497 32.05944798 256.5888 3.44676 MYOZ1 0.00459210288836828 0.875641999508722 0.11976589760291 myozenin 1 FUNCTION: Myozenins may serve as intracellular binding proteins involved in linking Z-disk proteins such as alpha-actinin, gamma- filamin, TCAP/telethonin, LDB3/ZASP and localizing calcineurin signaling to the sarcomere. Plays an important role in the modulation of calcineurin signaling. May play a role in myofibrillogenesis.; . TISSUE SPECIFICITY: Expressed primarily in skeletal muscle. Detected at lower levels in heart, prostate and pancreas. {ECO:0000269|PubMed:10984498, ECO:0000269|PubMed:11114196, ECO:0000269|PubMed:11171996}.; unclassifiable (Anatomical System);heart;ovary;muscle;choroid;skin;skeletal muscle;greater omentum;uterus;prostate;whole body;lung;larynx;testis;head and neck;spleen;kidney; dorsal root ganglion;superior cervical ganglion;tongue;thyroid;atrioventricular node;skeletal muscle; 0.41152 0.11414 -0.626318434 17.03231894 38.94344 1.15349 MYOZ2 0.016734637788662 0.88769284647615 0.0955725157351877 myozenin 2 FUNCTION: Myozenins may serve as intracellular binding proteins involved in linking Z line proteins such as alpha-actinin, gamma- filamin, TCAP/telethonin, LDB3/ZASP and localizing calcineurin signaling to the sarcomere. Plays an important role in the modulation of calcineurin signaling. May play a role in myofibrillogenesis.; . TISSUE SPECIFICITY: Expressed specifically in heart and skeletal muscle. {ECO:0000269|PubMed:11114196, ECO:0000269|PubMed:11161785}.; unclassifiable (Anatomical System);myocardium;ovary;heart;parathyroid;skin;skeletal muscle;uterus;prostate;pancreas;whole body;atrium;lung;larynx;placenta;visual apparatus;liver;testis;head and neck;spleen;aorta; superior cervical ganglion;heart;tongue;globus pallidus;ciliary ganglion;atrioventricular node;pons;fetal thyroid;trigeminal ganglion;skeletal muscle; 0.50755 0.15774 -0.273576253 33.97027601 52.9147 1.44360 MYOZ3 0.346673295762729 0.639783666230783 0.0135430380064879 myozenin 3 FUNCTION: Myozenins may serve as intracellular binding proteins involved in linking Z line proteins such as alpha-actinin, gamma- filamin, TCAP/telethonin, LDB3/ZASP and localizing calcineurin signaling to the sarcomere. Plays an important role in the modulation of calcineurin signaling. May play a role in myofibrillogenesis.; . TISSUE SPECIFICITY: Expressed specifically in skeletal muscle. Not detected in heart. {ECO:0000269|PubMed:11842093}.; uterus;greater omentum;prostate;pancreas;lung;ovary;heart;placenta;testis;parathyroid;brain;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;tongue;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09553 0.11637 0.393270925 76.04977589 439.3292 4.36836 MYP1 . . . myopia 1 (X-linked) . . . . . . . . . . . MYP2 . . . myopia 2 (high grade, autosomal dominant) . . . . . . . . . . . MYP3 . . . myopia 3 (high grade, autosomal dominant) . . . . . . . . . . . MYP4 . . . myopia 4 (high grade, autosomal dominant) . . . . . . . . . . . MYP5 . . . myopia 5 (high grade, autosomal dominant) . . . . . . . . . . . MYP7 . . . myopia 7 . . . . . . . . . . . MYP8 . . . myopia 8 . . . . . . . . . . . MYP9 . . . myopia 9 . . . . . . . . . . . MYP10 . . . myopia 10 . . . . . . . . . . . MYP11 . . . myopia 11 (high grade, autosomal dominant) . . . . . . . . . . . MYP12 . . . myopia 12 (high grade, autosomal dominant) . . . . . . . . . . . MYP13 . . . myopia 13 . . . . . . . . . . . MYP14 . . . myopia 14 . . . . . . . . . . . MYP15 . . . myopia 15 . . . . . . . . . . . MYP16 . . . myopia 16 . . . . . . . . . . . MYP17 . . . myopia 17 . . . . . . . . . . . MYP18 . . . myopia 18 (high grade, autosomal recessive) . . . . . . . . . . . MYPN 0.065221396704038 0.934778389796576 2.13499386101245e-07 myopalladin FUNCTION: Component of the sarcomere that tethers together nebulin (skeletal muscle) and nebulette (cardiac muscle) to alpha-actinin, at the Z lines. {ECO:0000269|PubMed:11309420}.; DISEASE: Cardiomyopathy, familial hypertrophic 22 (CMH22) [MIM:615248]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:22286171}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, familial restrictive 4 (RCM4) [MIM:615248]: A heart disorder characterized by impaired filling of the ventricles with reduced diastolic volume, in the presence of normal or near normal wall thickness and systolic function. {ECO:0000269|PubMed:22286171}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in adult skeletal muscle and fetal heart. {ECO:0000269|PubMed:11309420}.; unclassifiable (Anatomical System);cartilage;heart;ovary;parathyroid;skin;skeletal muscle;bone marrow;uterus;pancreas;larynx;placenta;visual apparatus;liver;head and neck;cervix;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.28635 0.11116 0.813798382 87.76244397 15598.30352 27.00260 MYPOP 0.810391050855017 0.184859339461597 0.00474960968338677 Myb-related transcription factor, partner of profilin FUNCTION: Transcriptional repressor; DNA-binding protein that specifically recognizes the core sequence 5'-YAAC[GT]G-3'. Dimerization with PFN1 reduces its DNA-binding capacity (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);prostate;optic nerve;lung;ovary;placenta;testis;colon;parathyroid;choroid;kidney;germinal center;brain; dorsal root ganglion;superior cervical ganglion;medulla oblongata;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; . . . . 174.64302 2.87476 MYRF 0.999847803435962 0.000152196559625376 4.41242092188235e-12 myelin regulatory factor FUNCTION: Myelin regulatory factor: Consitutes a precursor of the transcription factor. Mediates the autocatalytic cleavage that releases the Myelin regulatory factor, N-terminal component that specifically activates transcription of central nervous system (CNS) myelin genes (PubMed:23966832). {ECO:0000269|PubMed:23966832}.; FUNCTION: Myelin regulatory factor, N-terminal: Transcription factor that specifically activates expression of myelin genes such as MBP, MOG, MAG and PLP1 during oligodendrocyte (OL) maturation, thereby playing a central role in oligodendrocyte maturation and CNS myelination. Specifically recognizes and binds DNA sequence 5'-CTGGYAC-3' in the regulatory regions of myelin-specific genes and directly activates their expression. Not only required during oligodendrocyte differentiation but is also required on an ongoing basis for the maintenance of expression of myelin genes and for the maintenance of a mature, viable oligodendrocyte phenotype (PubMed:23966832). {ECO:0000269|PubMed:23966832}.; . TISSUE SPECIFICITY: Expressed in lung, ARPE-19 cell line, brainstem, uterus and, to a lesser extent, in basal ganglion and liver. Weakly expressed in cerebellum and retina. {ECO:0000269|PubMed:10828591}.; . . 0.22352 0.10570 -1.082044518 7.242274121 229.21291 3.27206 MYRFL . . . myelin regulatory factor-like . . . . . 0.11494 . . . 3336.78291 11.06066 MYRIP 0.000902541100654773 0.99898030370838 0.000117155190965105 myosin VIIA and Rab interacting protein FUNCTION: Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor proteins MYO5A and MYO7A. May link RAB27A-containing vesicles to actin filaments. Functions as a protein kinase A-anchoring protein (AKAP). May act as a scaffolding protein that links PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in brain, skin, heart, adrenal medulla, pancreas, intestine, liver, kidney, muscle and testis.; unclassifiable (Anatomical System);heart;islets of Langerhans;colon;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;macula lutea;liver;testis;germinal center;kidney;brain;cerebellum; whole brain;amygdala;occipital lobe;prefrontal cortex;globus pallidus;caudate nucleus;atrioventricular node;cingulate cortex; 0.41161 0.10795 -0.725642751 14.24274593 930.89733 5.91920 MYSA . . . myasthenic (Lambert-Eaton) syndrome antigen A . . . . . . . . . . . MYSM1 0.0202316448544944 0.979762002689363 6.35245614292827e-06 Myb like, SWIRM and MPN domains 1 FUNCTION: Metalloprotease that specifically deubiquitinates monoubiquitinated histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Preferentially deubiquitinates monoubiquitinated H2A in hyperacetylated nucleosomes. Deubiquitination of histone H2A leads to facilitate the phosphorylation and dissociation of histone H1 from the nucleosome. Acts as a coactivator by participating in the initiation and elongation steps of androgen receptor (AR)-induced gene activation. {ECO:0000269|PubMed:17707232}.; . . . . 0.27246 . 0.156217551 64.82071243 3151.9457 10.68348 MYT1 0.999871801547028 0.000128198452384449 5.87800988379665e-13 myelin transcription factor 1 FUNCTION: Binds to the promoter regions of proteolipid proteins of the central nervous system. May play a role in the development of neurons and oligodendrogalia in the CNS. May regulate a critical transition point in oligodendrocyte lineage development by modulating oligodendrocyte progenitor proliferation relative to terminal differentiation and up-regulation of myelin gene transcription. {ECO:0000269|PubMed:14962745}.; . TISSUE SPECIFICITY: Mostly in developing nervous system. Expressed in neural progenitors and oligodendrocyte lineage cells. More highly expressed in oligodendrocyte progenitors than in differentiated oligodendrocytes. {ECO:0000269|PubMed:8530187}.; unclassifiable (Anatomical System);islets of Langerhans;choroid;fovea centralis;lens;retina;optic nerve;lung;visual apparatus;macula lutea;liver;spleen;pineal gland;brain; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.93840 0.11581 -1.631512986 2.848549186 268.65953 3.51606 MYT1L 0.999963989377009 3.60106223397139e-05 6.51249064780453e-13 myelin transcription factor 1 like FUNCTION: May function as a panneural transcription factor associated with neuronal differentiation. May play a role in the development of neurons and oligodendrogalia in the CNS (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;frontal lobe;islets of Langerhans;hypothalamus;macula lutea;visual apparatus;testis;fovea centralis;brain; whole brain;amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.30683 0.11638 -1.506435464 3.544468035 525.36937 4.67655 MYT1L-AS1 . . . MYT1L antisense RNA 1 . . . . . . . . . . . MYZAP 2.21367341168049e-09 0.427793000456869 0.572206997329458 myocardial zonula adherens protein FUNCTION: Plays a role in cellular signaling via Rho-related GTP- binding proteins and subsequent activation of transcription factor SRF (By similarity). Targets TJP1 to cell junctions. In cortical neurons, may play a role in glutaminergic signal transduction through interaction with the NMDA receptor subunit GRIN1 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in heart, liver, skeletal muscle, placenta, small intestine, lung, prostate and testis. {ECO:0000269|PubMed:15233991, ECO:0000269|PubMed:20093627}.; . . . 0.10192 0.622829232 83.47487615 1698.56598 7.59846 MZB1 0.0038114549410852 0.638216757169053 0.357971787889862 marginal zone B and B1 cell specific protein FUNCTION: Associates with immunoglobulin M (IgM) heavy and light chains and promotes IgM assembly and secretion. May exert its effect by acting as a molecular chaperone or as an oxidoreductase as it displays a low level of oxidoreductase activity (By similarity). Isoform 2 may be involved in regulation of apoptosis. Helps to diversify peripheral B-cell functions by regulating Ca(2+) stores, antibody secretion and integrin activation. {ECO:0000250, ECO:0000269|PubMed:11350957, ECO:0000269|PubMed:21688198}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in adult brain, small intestine and lymphoid tissues such as thymus and spleen. Expression is frequently lower in intestinal-type gastric cancer. In obese patients, more abundant in omental than in subcutaneous fat. {ECO:0000269|PubMed:11350957, ECO:0000269|PubMed:12792799, ECO:0000269|PubMed:19805157}.; . . . . 0.060756528 58.52795471 70.25017 1.74186 MZF1 1.81494742445282e-06 0.67015972207576 0.329838462976815 myeloid zinc finger 1 FUNCTION: Binds to target promoter DNA and functions as trancription regulator. Regulates transcription from the PADI1 and CDH2 promoter. May be one regulator of transcriptional events during hemopoietic development. {ECO:0000269|PubMed:15541732, ECO:0000269|PubMed:17851584}.; . TISSUE SPECIFICITY: Preferentially expressed in differentiating myeloid cells. Detected in osteoblasts. {ECO:0000269|PubMed:15541732}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;muscle;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;liver;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;thyroid;temporal lobe;prefrontal cortex;globus pallidus;trigeminal ganglion;skeletal muscle;skin; 0.31082 0.18136 1.249272484 93.46543996 3566.96451 11.54921 MZF1-AS1 . . . MZF1 antisense RNA 1 . . . . . . . . . . . MZT1 0.611862318159052 0.353619484037631 0.0345181978033173 mitotic spindle organizing protein 1 FUNCTION: Required for gamma-tubulin complex recruitment to the centrosome. {ECO:0000269|PubMed:20360068}.; . . . . . 0.10461 0.169169615 65.33380514 3.02213 0.10974 MZT1P1 . . . mitotic spindle organizing protein 1 pseudogene 1 . . . . . . . . . . . MZT1P2 . . . mitotic spindle organizing protein 1 pseudogene 2 . . . . . . . . . . . MZT2A 0.0055676765947401 0.480414045121943 0.514018278283317 mitotic spindle organizing protein 2A . . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;bone;testis;brain;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; whole brain;amygdala;prostate;heart;temporal lobe;liver;parietal lobe;cingulate cortex; 0.09927 . . . 1716.53786 7.63823 MZT2B 0.575112152377793 0.37994715177859 0.0449406958436171 mitotic spindle organizing protein 2B . . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;bone;thyroid;testis;brain;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; whole brain;heart;thyroid;temporal lobe;liver;globus pallidus; . 0.10220 . . 85.59106 1.97308 N4BP1 0.361226867556661 0.63825346903564 0.000519663407699237 NEDD4 binding protein 1 FUNCTION: Inhibitor of the E3 ubiquitin-protein ligase ITCH. Acts by interacting with the second WW domain of ITCH, leading to compete with ITCH's substrates and impairing ubiquitination of substrates (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in heart, lung, brain, liver, skeletal muscle, pancreas, kidney, spleen, testis and ovary. {ECO:0000269|PubMed:9734811}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;whole blood;parietal lobe;skeletal muscle;cerebellum; 0.41643 0.09692 -0.534490515 20.70063694 74.3472 1.80062 N4BP2 0.000473118175100564 0.999514740777524 1.21410473750688e-05 NEDD4 binding protein 2 FUNCTION: Has 5'-polynucleotide kinase and nicking endonuclease activity. May play a role in DNA repair or recombination. {ECO:0000269|PubMed:12730195}.; . . unclassifiable (Anatomical System);heart;ovary;tongue;parathyroid;skin;skeletal muscle;uterus;breast;lung;frontal lobe;placenta;liver;testis;head and neck;spleen;brain;stomach; . 0.35382 0.09331 0.947914422 89.91507431 2737.46366 9.86403 N4BP2L1 0.945268895282581 0.0545364381352709 0.000194666582148561 NEDD4 binding protein 2-like 1 . . . ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;hippocampus;liver;spleen;kidney;thymus; dorsal root ganglion;medulla oblongata;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.08124 . 0.125076652 62.7388535 7.18931 0.27073 N4BP2L2 3.06127675841692e-06 0.776849444039117 0.223147494684125 NEDD4 binding protein 2-like 2 . . . medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;pancreas;lung;cornea;adrenal gland;placenta;head and neck;kidney;stomach;aorta; . 0.16888 0.06138 1.828058774 97.03349847 852.42265 5.70339 N4BP2L2-IT2 . . . N4BPL2 intronic transcript 2 . . . . . . . . . . . N4BP3 0.276863142105786 0.718122470495249 0.0050143873989648 NEDD4 binding protein 3 . . . unclassifiable (Anatomical System);lymph node;endometrium;placenta;colon;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; . . -0.466531444 23.51380042 502.34425 4.59903 N6AMT1 0.00987178467583436 0.821358578351083 0.168769636973082 N-6 adenine-specific DNA methyltransferase 1 (putative) FUNCTION: Heterodimeric methyltransferase that catalyzes N5- methylation of ETF1 on 'Gln-185', using S-adenosyl L-methionine as methyl donor. ETF1 needs to be complexed to ERF3 in its GTP-bound form to be efficiently methylated. May play a role in the modulation of arsenic-induced toxicity. May be involved in the conversion of monomethylarsonous acid (3+) into the less toxic dimethylarsonic acid. {ECO:0000269|PubMed:18539146, ECO:0000269|PubMed:21193388}.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in parathyroid and pituitary glands, followed by adrenal gland and kidney, and lowest expression in leukocytes and mammary gland. {ECO:0000269|PubMed:21193388}.; unclassifiable (Anatomical System);medulla oblongata;ovary;islets of Langerhans;skeletal muscle;skin;mesenchyma;nasopharynx;placenta;liver;spleen;germinal center;kidney;brain;aorta; superior cervical ganglion;testis;pons;trigeminal ganglion;skeletal muscle; 0.48968 0.09594 0.72761005 86.08162302 1301.02352 6.78541 NAA10 0.188427799697794 0.761843850440136 0.0497283498620694 N(alpha)-acetyltransferase 10, NatA catalytic subunit FUNCTION: Catalytic subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. Without NAA15, displays epsilon (internal) acetyltransferase activity towards HIF1A, thereby promoting its degradation. Represses MYLK kinase activity by acetylation, and thus represses tumor cell migration. Acetylates, and stabilizes TSC2, thereby repressing mTOR activity and suppressing cancer development. {ECO:0000269|PubMed:12464182, ECO:0000269|PubMed:15496142, ECO:0000269|PubMed:19826488, ECO:0000269|PubMed:20145209}.; DISEASE: N-terminal acetyltransferase deficiency (NATD) [MIM:300855]: An enzymatic deficiency resulting in postnatal growth failure with severe delays and dysmorphic features. It is clinically characterized by wrinkled forehead, prominent eyes, widely opened anterior and posterior fontanels, downsloping palpebral fissures, thickened lids, large ears, flared nares, hypoplastic alae, short columella, protruding upper lip, and microretrognathia. There are also delayed closing of fontanels and broad great toes. Skin is characterized by redundancy or laxity with minimal subcutaneous fat, cutaneous capillary malformations, and very fine hair and eyebrows. Death results from cardiogenic shock following arrhythmia. {ECO:0000269|PubMed:21700266}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Microphthalmia, syndromic, 1 (MCOPS1) [MIM:309800]: A rare syndrome defined by the canonical features of unilateral or bilateral microphthalmia or anophthalmia and defects in the skeletal and genitourinary systems. Microphthalmia is a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. Anomalies of the digits, teeth, and ears are hallmarks of MCOPS1. Intellectual disability ranges from mild to severe, with self-mutilating behaviors and seizures in severely affected MCOPS1 individuals. {ECO:0000269|PubMed:24431331}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12464182}.; . . 0.57545 0.28104 -0.031067188 51.03798066 . . NAA11 0.00282227496929348 0.573127357687315 0.424050367343391 N(alpha)-acetyltransferase 11, NatA catalytic subunit FUNCTION: Displays alpha (N-terminal) acetyltransferase activity. Proposed alternative catalytic subunit of the N-terminal acetyltransferase A (NatA) complex. {ECO:0000269|PubMed:16638120}.; . TISSUE SPECIFICITY: Present in several cell lines, with highest levels in MCF-7 cells (at protein level). {ECO:0000269|PubMed:16638120}.; bile duct;placenta;testis;skin; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.15668 0.09160 0.014844891 54.94810097 127.74995 2.46432 NAA15 0.998576839501621 0.00142316029118254 2.07196968300901e-10 N(alpha)-acetyltransferase 15, NatA auxiliary subunit FUNCTION: Auxillary subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. Required to control retinal neovascularization in adult ocular endothelial cells. In complex with XRCC6 and XRCC5 (Ku80), up-regulates transcription from the osteocalcin promoter. {ECO:0000269|PubMed:11687548, ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:15496142}.; . TISSUE SPECIFICITY: Expressed at high levels in testis and in ocular endothelial cells. Also found in brain (corpus callosum), heart, colon, bone marrow and at lower levels in most adult tissues, including thyroid, liver, pancreas, mammary and salivary glands, lung, ovary, urogenital system and upper gastrointestinal tract. Overexpressed in gastric cancer, in papillary thyroid carcinomas and in a Burkitt lymphoma cell line (Daudi). Specifically suppressed in abnormal proliferating blood vessels in eyes of patients with proliferative diabetic retinopathy. {ECO:0000269|PubMed:11687548, ECO:0000269|PubMed:12087473, ECO:0000269|PubMed:12140756}.; smooth muscle;ovary;umbilical cord;salivary gland;rectum;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;lung;mesenchyma;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;aorta;stomach;cerebellum;thymus; superior cervical ganglion; 0.99020 0.19761 -0.890882376 10.30313753 36.48516 1.09367 NAA16 1.70534181115751e-10 0.946688891149964 0.0533111086795014 N(alpha)-acetyltransferase 16, NatA auxiliary subunit FUNCTION: Auxillary subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity.; . . . . 0.78720 0.13369 -0.775187015 13.05142722 679.42749 5.21135 NAA20 0.0136063641752257 0.865460517534334 0.12093311829044 N(alpha)-acetyltransferase 20, NatB catalytic subunit FUNCTION: Catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp, Met-Glu, Met-Asn and Met-Gln. Proteins with cell cycle functions are overrepresented in the pool of NatB substrates. Required for maintaining the structure and function of actomyosin fibers and for proper cellular migration. {ECO:0000269|PubMed:18570629}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; . 0.14086 0.09481 -0.163345027 41.24793583 3.49703 0.12662 NAA25 0.999989964284881 1.00357151174945e-05 1.18662967211022e-15 N(alpha)-acetyltransferase 25, NatB auxiliary subunit FUNCTION: Non-catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp-Glu. May play a role in normal cell-cycle progression. {ECO:0000269|PubMed:18570629}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;spinal cord;blood;lens;skeletal muscle;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle;cingulate cortex; 0.37094 0.10762 -0.111973265 45.35857514 2728.20466 9.84256 NAA30 0.97371507084361 0.0262534931011809 3.14360552085932e-05 N(alpha)-acetyltransferase 30, NatC catalytic subunit FUNCTION: Catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. Catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. Necessary for the lysosomal localization and function of ARL8B sugeesting that ARL8B is a NatC substrate. {ECO:0000269|PubMed:19398576}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;liver;kidney; amygdala;dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.41910 0.10366 -0.161524709 41.6430762 41.50435 1.21121 NAA35 0.999995236725095 4.76327488149504e-06 2.33184561803092e-14 N(alpha)-acetyltransferase 35, NatC auxiliary subunit FUNCTION: Auxillary component of the N-terminal acetyltransferase C (NatC) complex which catalyzes acetylation of N-terminal methionine residues. Involved in regulation of apoptosis and proliferation of smooth muscle cells. {ECO:0000269|PubMed:19398576}.; . . unclassifiable (Anatomical System);lung;cartilage;ovary;tongue;larynx;visual apparatus;colon;head and neck;skin;bone marrow; superior cervical ganglion;testis - interstitial;testis;atrioventricular node;pons;parietal lobe;skeletal muscle; 0.40467 0.11180 -0.135838822 43.77211607 112.15397 2.30400 NAA38 0.00827246331155774 0.792407991508499 0.199319545179943 N(alpha)-acetyltransferase 38, NatC auxiliary subunit FUNCTION: Auxillary component of the N-terminal acetyltransferase C (NatC) complex which catalyzes acetylation of N-terminal methionine residues. {ECO:0000269|PubMed:19398576}.; . . lymphoreticular;myocardium;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;cochlea;endometrium;synovium;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;pharynx;blood;breast;pia mater;lung;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;tumor;testis;trigeminal ganglion; 0.17113 0.08269 0.079165051 59.43029016 2.54182 0.09451 NAA40 0.00544668374828987 0.970204183521199 0.0243491327305108 N(alpha)-acetyltransferase 40, NatD catalytic subunit FUNCTION: Responsible for the acetylation of the N-terminal residues of histones H4 and H2A. {ECO:0000269|PubMed:21935442}.; . . lymphoreticular;colon;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cerebellum cortex;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;head and neck;cervix;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15839 0.10522 -0.47017169 23.25430526 88.58642 2.01879 NAA50 0.876848812692325 0.12162150882853 0.00152967847914566 N(alpha)-acetyltransferase 50, NatE catalytic subunit FUNCTION: Probable catalytic component of the NAA11-NAA15 complex which displays alpha (N-terminal) acetyltransferase activity. {ECO:0000269|PubMed:16507339}.; . . myocardium;lymphoreticular;ovary;skin;retina;prostate;optic nerve;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;bladder;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta; skeletal muscle; 0.80645 0.17331 -0.031067188 51.03798066 10.03414 0.36656 NAA60 0.908883491873174 0.0904109766327165 0.000705531494109029 N(alpha)-acetyltransferase 60, NatF catalytic subunit FUNCTION: Histone acetyltransferase localized in the Golgi apparatus that mediates acetylation of free histone H4, thereby facilitating nucleosome assembly. Has a preference for free histone H4 'Lys-20'(H4K20ac), 'Lys-79'(H4K79ac) and 'Lys-91' (H4K91ac). Also displays alpha (N-terminal) acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase. {ECO:0000269|PubMed:21750686, ECO:0000269|PubMed:21981917}.; . . unclassifiable (Anatomical System);ovary;colon;parathyroid;skeletal muscle;retina;breast;prostate;lung;frontal lobe;placenta;pituitary gland;testis;cervix;germinal center;kidney;brain;mammary gland;stomach; superior cervical ganglion;liver;testis;kidney;skeletal muscle;cerebellum; . 0.09888 -0.227663163 37.11370606 98.98733 2.15340 NAAA 3.31295406720326e-06 0.791502930232311 0.208493756813622 N-acylethanolamine acid amidase FUNCTION: Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N- palmitoylethanolamine > N-myristoylethanolamine > N- lauroylethanolamine = N-stearoylethanolamine > N- arachidonoylethanolamine > N-oleoylethanolamine. Also exhibits weak hydrolytic activity against the ceramides N- lauroylsphingosine and N-palmitoylsphingosine. {ECO:0000269|PubMed:15655246}.; . TISSUE SPECIFICITY: Expressed in numerous tissues, with highest levels in liver and kidney, followed by pancreas. {ECO:0000269|PubMed:10610717}.; smooth muscle;ovary;colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;endometrium;iris;testis;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;prostate;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09972 0.21870 1.750970652 96.67374381 756.95877 5.45235 NAALAD2 7.02449643708852e-15 0.107927063340717 0.892072936659276 N-acetylated alpha-linked acidic dipeptidase 2 FUNCTION: Has N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Also exhibits a dipeptidyl-peptidase IV type activity. Inactivate the peptide neurotransmitter N- acetylaspartylglutamate. {ECO:0000269|PubMed:10085079}.; . TISSUE SPECIFICITY: Highest expression in the testis. Also found in ovary and spleen. Weak expression in prostate, heart and placenta. In brain, expressed in striatum, parietal cortex and ventral striatum with lower levels in hippocampus, brain stem, putamen and superior colliculus.; unclassifiable (Anatomical System);heart;hypothalamus;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;placenta;bone;macula lutea;liver;pituitary gland;testis;spleen; dorsal root ganglion;testis - seminiferous tubule;pons;pituitary; 0.18941 0.10482 0.068033485 59.0351498 2106.21853 8.44943 NAALADL1 3.83011320553878e-12 0.162417830895896 0.837582169100274 N-acetylated alpha-linked acidic dipeptidase-like 1 FUNCTION: NAALADase-like activity unknown. Has no NAAG hydrolyzing activity. Exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Mainly expressed in the distal small intestine. Also expressed in the spleen and testis. Weak expression in the brain, locating mainly to the brain stem, amygdala, thalamus and ventral striatum. Isoform 2 and 3 isoform 3 are found in the small intestine and colon.; unclassifiable (Anatomical System);ovary;parathyroid;choroid;fovea centralis;lens;bone marrow;retina;prostate;optic nerve;lung;placenta;macula lutea;liver;spleen;cervix;kidney;tonsil; dorsal root ganglion;uterus corpus;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07139 0.11247 -1.014084315 8.16230243 572.14408 4.85484 NAALADL2 3.04144463822372e-06 0.983611170766517 0.0163857877888447 N-acetylated alpha-linked acidic dipeptidase-like 2 FUNCTION: May be catalytically inactive.; . TISSUE SPECIFICITY: Expressed at higher level in kidney and placenta. In embryo, it is mainly confined to duodenal and stomach endoderm, mesonephros, metanephros and pancreas.; unclassifiable (Anatomical System);breast;prostate;lung;endometrium;liver;colon;spleen;kidney;mammary gland;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;temporal lobe;appendix;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.20621 . 1.337468036 94.28520878 3850.40605 12.22768 NAALADL2-AS1 . . . NAALADL2 antisense RNA 1 . . . . . . . . . . . NAALADL2-AS2 . . . NAALADL2 antisense RNA 2 . . . . . . . . . . . NAALADL2-AS3 . . . NAALADL2 antisense RNA 3 . . . . . . . . . . . NAB1 0.84850840841026 0.151379695946544 0.000111895643196339 NGFI-A binding protein 1 FUNCTION: Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2. {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform Short is found in myeloid leukemia cell line KG-1.; ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin;cerebellum; 0.36064 0.13428 -0.492218069 22.35786742 53.26891 1.44979 NAB2 0.987535197753901 0.0124597878419114 5.01440418706631e-06 NGFI-A binding protein 2 FUNCTION: Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2. Isoform 2 lacks repression ability (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed at low levels. Highly expressed in melanoma cell lines.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;lung;adrenal gland;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;adrenal cortex;ciliary ganglion;cerebellum; 0.73374 0.16468 -0.025608647 51.91672564 62.0737 1.60573 NABP1 0.014256968227511 0.870911478539709 0.11483155323278 nucleic acid binding protein 1 FUNCTION: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. In the SOSS complex, acts as a sensor of single-stranded DNA that binds to single-stranded DNA, in particular to polypyrimidines. The SOSS complex associates with DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways. {ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}.; . . . . 0.19391 0.08567 -0.295622497 32.61972163 13.80326 0.50127 NABP2 0.956804648100521 0.0430875917614544 0.000107760138024435 nucleic acid binding protein 2 FUNCTION: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. In the SOSS complex, acts as a sensor of single-stranded DNA that binds to single-stranded DNA, in particular to polypyrimidines. The SOSS complex associates with DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways. {ECO:0000269|PubMed:18449195, ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}.; . . . . 0.29478 . -0.141298762 42.87567823 1.67296 0.05407 NACA 0.0203382171134431 0.975936478686294 0.00372530420026288 nascent polypeptide-associated complex alpha subunit FUNCTION: Cardiac- and muscle-specific transcription factor. May act to regulate the expression of genes involved in the development of myotubes. Plays a critical role in ventricular cardiomyocyte expansion and regulates postnatal skeletal muscle growth and regeneration. Involved in the organized assembly of thick and thin filaments of myofibril sarcomeres (By similarity). {ECO:0000250}.; . . myocardium;ovary;skin;bone marrow;prostate;optic nerve;cochlea;endometrium;germinal center;bladder;brain;tonsil;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;choroid;vein;uterus;whole body;oesophagus;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;lung;pia mater;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; superior cervical ganglion;olfactory bulb;fetal brain;white blood cells;skin; . 0.20297 1.646168225 96.17834395 2967.33181 10.32927 NACA2 0.0989262820990375 0.771668522652617 0.129405195248346 nascent polypeptide-associated complex alpha subunit 2 FUNCTION: Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites) (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed specifically in testis and skeletal muscle. {ECO:0000269|PubMed:16201836}.; . . 0.71213 . 0.949904335 90.00943619 5130.16159 14.72439 NACA3P . . . NACA family member 3 pseudogene . . . lymphoreticular;smooth muscle;ovary;salivary gland;developmental;intestine;colon;parathyroid;choroid;vein;skin;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;stomach; . . . . . . . NACAD 0.365728808142491 0.481211374286363 0.153059817571146 NAC alpha domain containing FUNCTION: May prevent inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). May bind to nascent polypeptide chains as they emerge from the ribosome and block their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. May also reduce the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites) (By similarity). {ECO:0000250}.; . . . . 0.10874 . . . 1993.12822 8.22682 NACAP1 . . . nascent polypeptide associated complex alpha subunit pseudogene 1 . . . . . . 0.20297 . . . . NACAP2 . . . nascent polypeptide associated complex alpha subunit pseudogene 2 . . . . . . . . . . . NACAP3 . . . nascent polypeptide associated complex alpha subunit pseudogene 3 . . . . . . . . . . . NACAP4 . . . nascent polypeptide associated complex alpha subunit pseudogene 4 . . . . . . . . . . . NACAP5 . . . nascent polypeptide associated complex alpha subunit pseudogene 5 . . . . . . . . . . . NACAP6 . . . nascent polypeptide associated complex alpha subunit pseudogene 6 . . . . . . . . . . . NACAP7 . . . nascent polypeptide associated complex alpha subunit pseudogene 7 . . . . . . . . . . . NACC1 0.964946936209724 0.0349889541485904 6.41096416860307e-05 nucleus accumbens associated 1 FUNCTION: Functions as a transcriptional repressor. Seems to function as a transcriptional corepressor in neuronal cells through recruitment of HDAC3 and HDAC4. Contributes to tumor progression, and tumor cell proliferation and survival. This may be mediated at least in part through repressing transcriptional activity of GADD45GIP1. Required for recruiting the proteasome from the nucleus to the cytoplasm and dendritic spines. {ECO:0000269|PubMed:17130457, ECO:0000269|PubMed:17804717}.; . TISSUE SPECIFICITY: Overexpressed in several types of carcinomas including ovarian serous carcinomas. Expression levels positively correlate with tumor recurrence in ovarian serous carcinomas, and intense immunoreactivity in primary ovarian tumors predicts early recurrence. Up-regulated in ovarian carcinomas after chemotherapy, suggesting a role in development of chemotherapy resistance in ovarian cancer. {ECO:0000269|PubMed:17130457, ECO:0000269|PubMed:17391728}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;synovium;bone;thyroid;iris;amniotic fluid;brain;gall bladder;unclassifiable (Anatomical System);lacrimal gland;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;cerebellum; ciliary ganglion;trigeminal ganglion; 0.16313 0.11162 -0.203796826 38.81811748 38.02344 1.12952 NACC2 0.13460734119916 0.780024959507155 0.0853676992936853 NACC family member 2 FUNCTION: Functions as a transcriptional repressor through its association with the NuRD complex. Recruits the NuRD complex to the promoter of MDM2, leading to the repression of MDM2 transcription and subsequent stability of p53/TP53. {ECO:0000269|PubMed:22926524}.; . . unclassifiable (Anatomical System);ovary;colon;blood;parathyroid;fovea centralis;choroid;lens;retina;breast;optic nerve;lung;placenta;bone;macula lutea;testis;kidney;brain;stomach; amygdala;dorsal root ganglion;thalamus;superior cervical ganglion;spinal cord;atrioventricular node;pons;skeletal muscle;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cerebellum; 0.28414 . . . 225.34531 3.24620 NADK 0.00126768961404905 0.990233968756823 0.00849834162912831 NAD kinase . . TISSUE SPECIFICITY: Widely expressed but not detected in skeletal muscle. {ECO:0000269|PubMed:11594753}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;amnion;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;adrenal gland;testis;ciliary ganglion;whole blood;cingulate cortex; 0.15314 0.18640 -0.111973265 45.35857514 176.4511 2.88899 NADK2 0.90764788651388 0.0923459469655381 6.16652058198707e-06 NAD kinase 2, mitochondrial FUNCTION: Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to yield NADP(+). Can use both ATP or inorganic polyphosphate as the phosphoryl donor. Also has weak NADH kinase activity in vitro; however NADH kinase activity is much weaker than the NAD(+) kinase activity and may not be relevant in vivo. {ECO:0000269|PubMed:23212377}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:23212377}.; . . 0.15579 . 0.527368849 80.73248408 212.10983 3.14104 NADK2-AS1 . . . NADK2 antisense RNA 1 . . . . . . . . . . . NADSYN1 2.45472937261485e-09 0.969981925052082 0.0300180724931886 NAD synthetase 1 . . . medulla oblongata;smooth muscle;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;thyroid;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; trigeminal ganglion; 0.09024 0.10139 -0.20947578 37.78013682 1360.80497 6.92425 NAE1 1.90378758487526e-07 0.992581419896544 0.00741838972469705 NEDD8 activating enzyme E1 subunit 1 FUNCTION: Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation. {ECO:0000269|PubMed:10207026, ECO:0000269|PubMed:10722740, ECO:0000269|PubMed:12740388}.; . TISSUE SPECIFICITY: Ubiquitous in fetal tissues. Expressed throughout the adult brain. {ECO:0000269|PubMed:8626687}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;pharynx;blood;breast;bile duct;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;kidney;mammary gland;stomach;aorta;cerebellum;peripheral nerve; testis - interstitial;testis - seminiferous tubule;testis; 0.66005 0.14921 -0.26993514 34.59542345 214.0129 3.15755 NAF1 0.959542886987655 0.0404385074399686 1.86055723763834e-05 nuclear assembly factor 1 ribonucleoprotein FUNCTION: RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex and disappears during maturation of the complex and is replaced by NOLA1/GAR1 to yield mature H/ACA snoRNPs complex. Probably competes with NOLA1/GAR1 for binding with DKC1/NOLA4. {ECO:0000269|PubMed:16618814}.; . . unclassifiable (Anatomical System);lung;cartilage;ovary;hypothalamus;placenta;visual apparatus;liver;testis;parathyroid;brain;pineal gland;stomach;bone marrow; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15147 . 0.527368849 80.73248408 164.89693 2.80643 NAGA 2.01989868135176e-06 0.693033151136458 0.306964828964861 N-acetylgalactosaminidase, alpha- FUNCTION: Removes terminal alpha-N-acetylgalactosamine residues from glycolipids and glycopeptides. Required for the breakdown of glycolipids. {ECO:0000269|PubMed:9741689}.; DISEASE: Schindler disease (SCHIND) [MIM:609241]: Form of NAGA deficiency characterized by early-onset neuroaxonal dystrophy and neurological signs (convulsion during fever, epilepsy, psychomotor retardation and hypotonia). NAGA deficiency is typically classified in three main phenotypes: NAGA deficiency type I (Schindler disease or Schindler disease type I) with severe manifestations; NAGA deficiency type II (Kanzazi disease or Schindler disease type II) which is mild; NAGA deficiency type III (Schindler disease type III) characterized by mild-to-moderate neurologic manifestations. NAGA deficiency results in the increased urinary excretion of glycopeptides and oligosaccharides containing alpha-N-acetylgalactosaminyl moieties. Inheritance is autosomal recessive. {ECO:0000269|PubMed:2243144, ECO:0000269|PubMed:8782044}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Kanzaki disease (KANZD) [MIM:609242]: Autosomal recessive disorder characterized by late-onset, angiokeratoma corporis diffusum and mild intellectual impairment. {ECO:0000269|PubMed:11251574, ECO:0000269|PubMed:8040340}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.33821 0.39417 -0.312207497 32.05944798 37.25215 1.11055 NAGK 8.57690899485212e-09 0.155835774544122 0.844164216878969 N-acetylglucosamine kinase FUNCTION: Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway: although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded. Also has ManNAc kinase activity. {ECO:0000269|PubMed:22692205}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10824116}.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;spinal cord;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;oesophagus;cerebral cortex;bone;testis;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;kidney;stomach;aorta;thymus; superior cervical ganglion; 0.08338 0.13359 -0.492218069 22.35786742 67.15995 1.69535 NAGLU 0.000404074411747293 0.990706107682953 0.00888981790529948 N-acetylglucosaminidase, alpha FUNCTION: Involved in the degradation of heparan sulfate.; DISEASE: Charcot-Marie-Tooth disease 2V (CMT2V) [MIM:616491]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. CMT2V is an autosomal dominant sensory neuropathy with late onset. The main clinical feature is recurrent leg pain that progresses to constant painful paraesthesias in the feet and later the hands. As it evolves, some patients develop a mild sensory ataxia. {ECO:0000269|PubMed:25818867}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver, ovary, peripheral blood leukocytes, testis, prostate, spleen, colon, lung, placenta and kidney.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;muscle;blood;lens;lung;epididymis;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.11426 0.52849 -0.753139731 13.67067705 231.78531 3.28955 NAGPA 2.86322915528202e-07 0.306197599604429 0.693802114072655 N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase FUNCTION: Catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P- mannose moieties, which are formed in the first step. Also hydrolyzes UDP-GlcNAc, a sugar donor for Golgi N- acetylglucosaminyltransferases. {ECO:0000269|PubMed:23572527}.; DISEASE: Note=Defects in NAGPA have been suggested to play a role in susceptibility to persistent stuttering. Stuttering is a common speech disorder characterized by repetitions, prolongations, and interruptions in the flow of speech. {ECO:0000269|PubMed:20147709}.; TISSUE SPECIFICITY: Isoform 2 may be brain-specific.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;breast;pancreas;lung;mesenchyma;placenta;visual apparatus;hippocampus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach; whole brain;amygdala;medulla oblongata;occipital lobe;prefrontal cortex;cingulate cortex;parietal lobe; 0.09060 0.27387 0.001895464 54.03397028 257.44881 3.45118 NAGPA-AS1 . . . NAGPA antisense RNA 1 . . . . . . . . . . . NAGS 4.88883525644423e-05 0.66044252420122 0.339508587446215 N-acetylglutamate synthase FUNCTION: Plays a role in the regulation of ureagenesis by producing the essential cofactor N-acetylglutamate (NAG), thus modulating carbamoylphosphate synthase I (CPSI) activity.; DISEASE: N-acetylglutamate synthase deficiency (NAGSD) [MIM:237310]: Rare autosomal recessively inherited metabolic disorder leading to severe neonatal or late-onset hyperammonemia without increased excretion of orotic acid. Clinical symptoms are somnolence, tachypnea, feeding difficulties, a severe neurologic presentation characterized by uncontrollable movements, developmental delay, visual impairment, failure to thrive and hyperammonemia precipitated by the introduction of high-protein diet or febrile illness. {ECO:0000269|PubMed:12754705, ECO:0000269|PubMed:15878741}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in the adult liver, kidney and small intestine. Weakly expressed in the fetal liver, lung, pancreas, placenta, heart and brain tissue. {ECO:0000269|PubMed:12459178, ECO:0000269|PubMed:12754705}.; unclassifiable (Anatomical System);prostate;lung;cartilage;thyroid;liver;colon;spleen;brain; globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13901 0.26860 -0.339715008 30.06605331 133.26482 2.50841 NAIF1 0.0225455776754148 0.763902249949659 0.213552172374926 nuclear apoptosis inducing factor 1 FUNCTION: Induces apoptosis. {ECO:0000269|PubMed:16378748}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16378748}.; . . 0.41553 0.10990 0.038710339 56.92380278 37.90247 1.12520 NAIP 0.000869318190199381 0.559751454474357 0.439379227335443 NLR family, apoptosis inhibitory protein FUNCTION: Anti-apoptotic protein which acts by inhibiting the activities of CASP3, CASP7 and CASP9. Can inhibit the autocleavage of pro-CASP9 and cleavage of pro-CASP3 by CASP9. Capable of inhibiting CASP9 autoproteolysis at 'Asp-315' and decreasing the rate of auto proteolysis at 'Asp-330'. Acts as a mediator of neuronal survival in pathological conditions. Prevents motor- neuron apoptosis induced by a variety of signals. Possible role in the prevention of spinal muscular atrophy that seems to be caused by inappropriate persistence of motor-neuron apoptosis: mutated or deleted forms of NAIP have been found in individuals with severe spinal muscular atrophy.; . TISSUE SPECIFICITY: Expressed in motor neurons, but not in sensory neurons. Found in liver and placenta, and to a lesser extent in spinal cord.; ovary;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;subthalamic nucleus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;bone;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;alveolus;liver;head and neck;kidney;stomach;aorta;peripheral nerve; . 0.33294 0.10896 . . 65.58464 1.66788 NALCN 0.000169004064103246 0.999830995905605 3.02922973192422e-11 sodium leak channel, non-selective FUNCTION: Voltage-independent, cation-nonselective channel which is permeable to sodium, potassium and calcium ions. Responsible for the background sodium ion leak current in neurons and controls neuronal excitability. Activated either by neuropeptides substance P or neurotensin. Required for normal respiratory rhythm and neonatal survival (By similarity). {ECO:0000250, ECO:0000269|PubMed:17448995}.; DISEASE: Hypotonia, infantile, with psychomotor retardation and characteristic facies (IHPRF) [MIM:615419]: A neurodegenerative disease characterized by variable degrees of hypotonia, speech impairment, intellectual disability, pyramidal signs, subtle facial dysmorphism, and chronic constipation. Some patients manifest neuroaxonal dystrophy, optic atrophy, unmyelinated axons and spheroid bodies in tissue biopsies. {ECO:0000269|PubMed:23749988, ECO:0000269|PubMed:24075186}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Congenital contractures of the limbs and face, hypotonia, and developmental delay (CLIFAHDD) [MIM:616266]: A disease characterized by congenital contractures of the limbs and face, resulting in characteristic facial features, abnormal tone, most commonly manifested as hypotonia, and variable degrees of developmental delay. {ECO:0000269|PubMed:25683120}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;parathyroid;skin;skeletal muscle;uterus;pancreas;lung;frontal lobe;placenta;bone;liver;head and neck;brain; amygdala;dorsal root ganglion;whole brain;occipital lobe;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.43129 0.10307 -1.611264137 2.984194385 137.54866 2.55255 NALCN-AS1 . . . NALCN antisense RNA 1 . . . . . . . . . . . NALT1 . . . NOTCH1 associated lncRNA in T-cell acute lymphoblastic leukemia 1 . . . . . . . . . . . NAMA . . . non-protein coding RNA, associated with MAP kinase pathway and growth arrest . . . . . . . . . . . NAMPT 0.982566484474744 0.017431200048574 2.31547668166928e-06 nicotinamide phosphoribosyltransferase FUNCTION: Catalyzes the condensation of nicotinamide with 5- phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma. Plays a role in the modulation of circadian clock function. NAMPT-dependent oscillatory production of NAD regulates oscillation of clock target gene expression by releasing the core clock component: CLOCK-ARNTL/BMAL1 heterodimer from NAD-dependent SIRT1-mediated suppression (By similarity). {ECO:0000250|UniProtKB:Q99KQ4, ECO:0000269|PubMed:24130902}.; . TISSUE SPECIFICITY: Expressed in large amounts in bone marrow, liver tissue, and muscle. Also present in heart, placenta, lung, and kidney tissues.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; superior cervical ganglion;adrenal cortex;fetal lung;ciliary ganglion;trigeminal ganglion;whole blood;skeletal muscle; 0.78463 0.23065 -0.295622497 32.61972163 12.6544 0.46182 NAMPTP1 . . . nicotinamide phosphoribosyltransferase pseudogene 1 . . . . . . . . . . . NAMPTP2 . . . nicotinamide phosphoribosyltransferase pseudogene 2 . . . . . . . . . . . NAMPTP3 . . . nicotinamide phosphoribosyltransferase pseudogene 3 . . . . . . . . . . . NANOG 0.911618852133588 0.0877283496450058 0.000652798221406596 Nanog homeobox FUNCTION: Transcription regulator involved in inner cell mass and embryonic stem (ES) cells proliferation and self-renewal. Imposes pluripotency on ES cells and prevents their differentiation towards extraembryonic endoderm and trophectoderm lineages. Blocks bone morphogenetic protein-induced mesoderm differentiation of ES cells by physically interacting with SMAD1 and interfering with the recruitment of coactivators to the active SMAD transcriptional complexes. Acts as a transcriptional activator or repressor. Binds optimally to the DNA consensus sequence 5'-TAAT[GT][GT]-3' or 5'- [CG][GA][CG]C[GC]ATTAN[GC]-3'. Able to autorepress its expression in differentiating (ES) cells: binds to its own promoter following interaction with ZNF281/ZFP281, leading to recruitment of the NuRD complex and subsequent repression of expression. When overexpressed, promotes cells to enter into S phase and proliferation. {ECO:0000269|PubMed:15983365, ECO:0000269|PubMed:16000880, ECO:0000269|PubMed:16391521}.; . TISSUE SPECIFICITY: Expressed in testicular carcinoma and derived germ cell tumors (at protein level). Expressed in fetal gonads, ovary and testis. Also expressed in ovary teratocarcinoma cell line and testicular embryonic carcinoma. Not expressed in many somatic organs and oocytes. {ECO:0000269|PubMed:12787504, ECO:0000269|PubMed:12787505, ECO:0000269|PubMed:14990856, ECO:0000269|PubMed:15982323, ECO:0000269|PubMed:16391521}.; unclassifiable (Anatomical System);epididymis;blood;brain;bone marrow; subthalamic nucleus;superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; . 0.34248 0.237127192 68.98443029 137.67876 2.55535 NANOGNB . . . NANOG neighbor homeobox . . . . . . . 0.812172405 87.75654636 94.80364 2.09869 NANOGNBP1 . . . NANOGNB pseudogene 1 . . . . . . . . . . . NANOGNBP2 . . . NANOGNB pseudogene 2 . . . . . . . . . . . NANOGNBP3 . . . NANOGNB pseudogene 3 . . . . . . . . . . . NANOGP1 . . . Nanog homeobox pseudogene 1 FUNCTION: Probable transcriptional regulator.; . . . . . 0.07629 . . . . NANOGP2 . . . Nanog homeobox pseudogene 2 . . . . . . . . . . . NANOGP3 . . . Nanog homeobox pseudogene 3 . . . . . . . . . . . NANOGP4 . . . Nanog homeobox pseudogene 4 . . . . . . . . . . . NANOGP5 . . . Nanog homeobox pseudogene 5 . . . . . . . . . . . NANOGP6 . . . Nanog homeobox pseudogene 6 . . . . . . . . . . . NANOGP7 . . . Nanog homeobox pseudogene 7 . . . . . . . . . . . NANOGP8 . . . Nanog homeobox pseudogene 8 FUNCTION: May act as a transcription regulator (By similarity). When overexpressed, promotes entry of cells into S phase and cell proliferation. {ECO:0000250, ECO:0000269|PubMed:16623708}.; . TISSUE SPECIFICITY: Expressed in osteosarcoma cancer cell line (at protein level), breast and urinary bladder tissues, and also osteosarcoma, hepatoma, and breast adenocarcinoma cancer cell lines. {ECO:0000269|PubMed:16623708}.; . . . 0.34248 . . . . NANOGP9 . . . Nanog homeobox pseudogene 9 . . . . . . . . . . . NANOGP10 . . . Nanog homeobox pseudogene 10 . . . . . . . . . . . NANOGP11 . . . Nanog homeobox pseudogene 11 . . . . . . . . . . . NANOS1 0.180809141007575 0.645218069745757 0.173972789246668 nanos homolog 1 (Drosophila) FUNCTION: May act as a translational repressor which regulates translation of specific mRNAs by forming a complex with PUM2 that associates with the 3'-UTR of mRNA targets. Capable of interfering with the proadhesive and anti-invasive functions of E-cadherin. Up-regulates the production of MMP14 to promote tumor cell invasion. {ECO:0000269|PubMed:17047063, ECO:0000269|PubMed:18223680}.; DISEASE: Spermatogenic failure 12 (SPGF12) [MIM:615413]: An infertility disorder caused by spermatogenesis defects. It results in decreased sperm motility, concentration, and multiple sperm structural defects. Non-obstructive azoospermia, oligozoospermia and oligo-astheno-teratozoospermia are features observed in SPGF12 patients. {ECO:0000269|PubMed:23315541}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Testis and ovary (at protein level). Predominantly expressed in testis. Specifically expressed during germline development. In adult tissues, it is mainly expressed in spermatogonia, the stem cells of the germline. Also expressed during meiosis in spermatocytes. Not present in late, post-meiotic stage germ cells. Expressed in fetal ovaries, while it is weakly or not expressed in mature postmeiotic oocytes, suggesting that it may be expressed in premeiotic female germ cells. Expressed at high levels only in the E-cadherin deficient cell lines. Highly expressed in lung carcinomas and mostly detected in invasive tumor cells and its expression correlates with tumor aggressiveness. {ECO:0000269|PubMed:12690449, ECO:0000269|PubMed:17047063, ECO:0000269|PubMed:18223680, ECO:0000269|PubMed:19168546, ECO:0000269|PubMed:21421998}.; unclassifiable (Anatomical System);heart;ovary;colon;skin;uterus;whole body;lung;placenta;alveolus;liver;testis;cervix;brain; . 0.20088 0.61198 -1.006844617 8.209483369 215.11184 3.16490 NANOS2 0.575905924394273 0.379399578956063 0.044694496649664 nanos homolog 2 (Drosophila) FUNCTION: Plays a key role in the sexual differentiation of germ cells by promoting the male fate but suppressing the female fate. Represses the female fate pathways by suppressing meiosis, which in turn results in the promotion of the male fate. Maintains the suppression of meiosis by preventing STRA8 expression, which is required for premeiotic DNA replication, after CYP26B1 is decreased. Regulates the localization of the CCR4-NOT deadenylation complex to P-bodies and plays a role in recruiting the complex to trigger the degradation of mRNAs involved in meiosis. Required for the maintenance of the spermatogonial stem cell population. Not essential for the assembly of P-bodies but is required for the maintenance of their normal state (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis and ovary. Expression found in several spermatogenic stages: in cells on the periphery of the tubules which could correspond to spermatogonia, in spermatocytes and in round spermatids (at protein level). {ECO:0000269|PubMed:19168545, ECO:0000269|PubMed:21421998}.; medulla oblongata;testis; . 0.27334 0.51048 -0.029247611 51.40363293 11.49546 0.41442 NANOS3 0.0079050763229906 0.784485441000211 0.207609482676799 nanos homolog 3 (Drosophila) FUNCTION: Plays a role in the maintenance of the undifferentiated state of germ cells regulating the spermatogonia cell cycle and inducing a prolonged transit in G1 phase. Affects cell proliferation probably by repressing translation of specific mRNAs. Maintains the germ cell lineage by suppressing both Bax- dependent and -independent apoptotic pathways. Essential in the early stage embryo to protect the migrating primordial germ cells (PGCs) from apoptosis. {ECO:0000269|PubMed:21421998}.; . TISSUE SPECIFICITY: Ovary, testis and brain (at protein level). In the ovaries, expressed during multiple stages of oogenesis, including primordial, primary, secondary and antral follicles with the highest expression in the oocytes. In the testis, expressed in germ cells, type A spermatogonia (SA), primary spermatocytes (S1), round spermatids (S3) and elongated spermatids. {ECO:0000269|PubMed:21421998}.; lung;islets of Langerhans;placenta;testis; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.24842 0.26228 0.035072054 56.2514744 196.82667 3.03390 NANP 0.0265416473766969 0.790067075648714 0.183391276974589 N-acetylneuraminic acid phosphatase . . . unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;colon;skin;skeletal muscle;uterus;pancreas;lung;endometrium;bone;placenta;thyroid;visual apparatus;hippocampus;duodenum;testis;kidney;brain;peripheral nerve; dorsal root ganglion;superior cervical ganglion;medulla oblongata;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.16969 0.17115 -0.404032746 26.53338051 23.21428 0.77541 NANS 0.00017687867479135 0.697441707338089 0.30238141398712 N-acetylneuraminate synthase FUNCTION: Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3- deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N- acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively.; . TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;optic nerve;whole body;bone;iris;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum;thymus; prostate; 0.18924 . 0.418953042 77.06416608 1715.96875 7.63695 NAP1L1 0.993880985311057 0.00611883684841006 1.77840533190357e-07 nucleosome assembly protein 1 like 1 FUNCTION: May be involved in modulating chromatin formation and contribute to regulation of cell proliferation.; . TISSUE SPECIFICITY: Ubiquitously expressed.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;urinary;pharynx;blood;lens;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; uterus;amygdala;occipital lobe;prefrontal cortex;tumor;globus pallidus;white blood cells;fetal lung;cingulate cortex; 0.99691 0.18271 -0.251530012 35.42108988 6.18996 0.23379 NAP1L1P1 . . . nucleosome assembly protein 1 like 1 pseudogene 1 . . . . . . . . . . . NAP1L1P2 . . . nucleosome assembly protein 1 like 1 pseudogene 2 . . . . . . . . . . . NAP1L1P3 . . . nucleosome assembly protein 1 like 1 pseudogene 3 . . . . . . . . . . . NAP1L2 0.791659153831853 0.202228073900035 0.00611277226811172 nucleosome assembly protein 1 like 2 FUNCTION: Acidic protein which may be involved in interactions with other proteins or DNA. {ECO:0000250}.; . . . . 0.56678 0.09955 -0.117432389 44.89266336 182.38162 2.93283 NAP1L3 0.411770225900925 0.551774213677836 0.0364555604212389 nucleosome assembly protein 1 like 3 . . . . . 0.31812 0.07894 0.128714042 63.19886766 47.69679 1.34140 NAP1L4 0.995731030115456 0.00426889609051307 7.37940307783493e-08 nucleosome assembly protein 1 like 4 . . TISSUE SPECIFICITY: Ubiquitous. Biallelically expressed in fetal and adult tissues. Highest levels in testis.; . . 0.45495 0.10887 -0.159704656 41.90846898 741.74824 5.40816 NAP1L4P1 . . . nucleosome assembly protein 1 like 4 pseudogene 1 . . . . . . . . . . . NAP1L4P2 . . . nucleosome assembly protein 1 like 4 pseudogene 2 . . . . . . . . . . . NAP1L4P3 . . . nucleosome assembly protein 1 like 4 pseudogene 3 . . . . . . . . . . . NAP1L5 0.788624389923416 0.205020261028637 0.00635534904794695 nucleosome assembly protein 1 like 5 . . TISSUE SPECIFICITY: Predominantly expressed in brain. {ECO:0000269|PubMed:12383514}.; frontal lobe;islets of Langerhans;hypothalamus;hippocampus;pituitary gland;colon;blood;kidney;brain;skin;retina; . 0.35011 0.11038 -0.317668748 31.45789101 24.87885 0.81649 NAP1L6 . . . nucleosome assembly protein 1 like 6 . . . . . 0.06144 . . . 11.2914 0.40636 NAPA 0.974655184511478 0.0253389889428886 5.8265456333634e-06 NSF attachment protein alpha FUNCTION: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;iris;germinal center;brain;ciliary body;tonsil;heart;cartilage;urinary;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus; liver;cerebellum; 0.52819 0.12971 -0.0274281 51.65723048 22.57709 0.75528 NAPA-AS1 . . . NAPA antisense RNA 1 . . . . . . . . . . . NAPB 0.989108778039473 0.010887619980802 3.6019797251312e-06 NSF attachment protein beta FUNCTION: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus. {ECO:0000250}.; . . . . 0.31367 0.13588 -0.073340031 48.11866006 50.87866 1.40537 NAPEPLD 0.0627214993961428 0.921572092277848 0.0157064083260096 N-acyl phosphatidylethanolamine phospholipase D FUNCTION: Hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce N-acylethanolamines (NAEs) and phosphatidic acid. Responsible for the generation of anandamide (N- arachidonoylethanolamine), the ligand of cannabinoid and vanilloid receptors (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;spinal cord;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;kidney;stomach;aorta;cerebellum; testis;appendix; 0.15677 0.18537 -0.003562597 53.72729417 1116.28859 6.38112 NAPG 0.0861319351364347 0.911903668989041 0.00196439587452475 NSF attachment protein gamma FUNCTION: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus.; . . unclassifiable (Anatomical System);heart;ovary;tongue;colon;parathyroid;blood;skin;skeletal muscle;uterus;lung;frontal lobe;endometrium;placenta;liver;head and neck;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.14938 0.12747 -0.205617011 38.57631517 311.6003 3.75714 NAPGP1 . . . N-ethylmaleimide-sensitive factor attachment protein, gamma pseudogene 1 . . . . . . . . . . . NAPGP2 . . . N-ethylmaleimide-sensitive factor attachment protein, gamma pseudogene 2 . . . . . . . . . . . NAPRT . . . nicotinate phosphoribosyltransferase FUNCTION: Catalyzes the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN). Essential for NA to increase cellular NAD levels and prevent oxidative stress of the cells. {ECO:0000269|PubMed:17604275}.; . . . . 0.06027 0.11356 -1.017713296 8.103326256 . . NAPSA 7.95882589543694e-07 0.492144376518278 0.507854827599132 napsin A aspartic peptidase FUNCTION: May be involved in processing of pneumocyte surfactant precursors.; . TISSUE SPECIFICITY: Expressed predominantly in adult lung (type II pneumocytes) and kidney and in fetal lung. Low levels in adult spleen and very low levels in peripheral blood leukocytes.; unclassifiable (Anatomical System);uterus;prostate;lung;cartilage;placenta;testis;colon;spleen;kidney;brain;stomach; . 0.09046 0.12971 -0.044015879 50.44821892 742.06691 5.40970 NAPSB . . . napsin B aspartic peptidase, pseudogene FUNCTION: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus. {ECO:0000250}.; . . . . 0.02668 0.05504 -0.073340031 48.11866006 . . NARF 0.00122491910128246 0.989855758750274 0.00891932214844339 nuclear prelamin A recognition factor . . TISSUE SPECIFICITY: Ubiquitous. Predominantly expressed in skeletal muscle, heart and brain. {ECO:0000269|PubMed:10514485}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;muscle;urinary;adrenal cortex;blood;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.04693 0.10014 -1.153638777 6.233781552 63.53572 1.63313 NARF-IT1 . . . NARF intronic transcript 1 . . . . . . . . . . . NARFL 1.04511224704187e-05 0.939217349166646 0.0607721997108833 nuclear prelamin A recognition factor-like FUNCTION: Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. Seems to negatively regulate the level of HIF1A expression, although this effect could be indirect. {ECO:0000269|PubMed:16956324, ECO:0000269|PubMed:18270200}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16956324}.; ovary;salivary gland;sympathetic chain;intestine;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;frontal lobe;synovium;bone;testis;dura mater;spinal ganglion;brain;bladder;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;heart;lacrimal gland;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;breast;pia mater;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; superior cervical ganglion; 0.06012 0.18388 -0.106515707 45.60627506 230.54488 3.28103 NARS 3.48085840763395e-07 0.996847825350489 0.00315182656367035 asparaginyl-tRNA synthetase . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;pineal body;lens;breast;bile duct;pancreas;pia mater;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; amygdala;thalamus;subthalamic nucleus;medulla oblongata;occipital lobe;hypothalamus;prefrontal cortex;globus pallidus;pons;caudate nucleus;parietal lobe;cingulate cortex; 0.44774 0.15015 -0.512444034 21.55579146 45.92925 1.30376 NARS2 0.000838255657065933 0.996003119948156 0.00315862439477773 asparaginyl-tRNA synthetase 2, mitochondrial (putative) . DISEASE: Combined oxidative phosphorylation deficiency 24 (COXPD24) [MIM:616239]: An autosomal recessive mitochondrial disorder with wide phenotypic variability. Some patients have a milder form affecting only skeletal muscle, whereas others may have a more severe disorder, reminiscent of Alpers syndrome. Alpers syndrome is a progressive neurodegenerative disorder that presents in infancy or early childhood and is characterized by diffuse degeneration of cerebral gray matter. {ECO:0000269|PubMed:25385316, ECO:0000269|PubMed:25629079}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=NARS2 mutations may be the cause of deafness, autosomal recessive, 94 (DFNB94). DFNB94 is a form of non- syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:25807530}.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. {ECO:0000269|PubMed:25807530}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;colon;parathyroid;skin;uterus;prostate;frontal lobe;cochlea;larynx;bone;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);islets of Langerhans;blood;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;skeletal muscle;parietal lobe; 0.12213 0.10840 -0.288341872 33.41589998 121.64357 2.40172 NARSP1 . . . asparaginyl-tRNA synthetase pseudogene 1 . . . . . . . . . . . NARSP2 . . . asparaginyl-tRNA synthetase pseudogene 2 . . . . . . . . . . . NASP 0.470216299614197 0.529737965351055 4.57350347475462e-05 nuclear autoantigenic sperm protein FUNCTION: Required for DNA replication, normal cell cycle progression and cell proliferation. Forms a cytoplasmic complex with HSP90 and H1 linker histones and stimulates HSP90 ATPase activity. NASP and H1 histone are subsequently released from the complex and translocate to the nucleus where the histone is released for binding to DNA (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is testis- and sperm-specific.; lymphoreticular;medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;placenta;duodenum;head and neck;kidney;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;fetal brain;hypothalamus;spinal cord;prefrontal cortex;tumor;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.82873 0.14655 -0.176292081 40.56381222 111.92131 2.30362 NASPP1 . . . nuclear autoantigenic sperm protein pseudogene 1 . . . . . . . . . . . NAT1 2.8541046904519e-10 0.0116083648466182 0.988391634867971 N-acetyltransferase 1 (arylamine N-acetyltransferase) FUNCTION: Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate several known carcinogens.; . . unclassifiable (Anatomical System);islets of Langerhans;colon;parathyroid;retina;bile duct;prostate;lung;endometrium;placenta;pituitary gland;liver;testis;spleen;germinal center;kidney;mammary gland;artery;aorta;stomach; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08420 0.09203 0.905808022 89.4373673 97.68317 2.13775 NAT2 0.0226078662097717 0.764368131772909 0.213024002017319 N-acetyltransferase 2 (arylamine N-acetyltransferase) FUNCTION: Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate several known carcinogens.; . . unclassifiable (Anatomical System);islets of Langerhans;bone;liver;colon; dorsal root ganglion;superior cervical ganglion;medulla oblongata;ciliary ganglion; 0.02662 0.09150 1.840996754 97.08657702 5863.36984 15.88033 NAT6 0.402945153314903 0.558346890613092 0.0387079560720051 N-acetyltransferase 6 FUNCTION: Seems to be involved in N-acetylation. Acts on peptides with a N-terminal Met followed by Asp/Glu/Asn. May act as a tumor suppressor. {ECO:0000269|PubMed:10644992}.; . TISSUE SPECIFICITY: Strongly expressed in heart and skeletal muscle, followed by brain and pancreas, with weak expression in kidney, liver, and lung and no expression in placenta.; unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;parathyroid;choroid;skin;skeletal muscle;uterus;breast;optic nerve;lung;endometrium;placenta;bone;testis;cervix;brain;stomach; . 0.11387 0.07765 0.352813824 74.49280491 676.76691 5.19810 NAT8 0.0756516923219644 0.748028448401462 0.176319859276573 N-acetyltransferase 8 (putative) FUNCTION: Acetylates the free alpha-amino group of cysteine S- conjugates to form mercapturic acids (PubMed:20392701). This is the final step in a major route for detoxification of a wide variety of reactive electrophiles which starts with their incorporation into glutathione S-conjugates. The glutathione S- conjugates are then further processed into cysteine S-conjugates and finally mercapturic acids which are water soluble and can be readily excreted in urine or bile. Alternatively, may have a lysine N-acetyltransferase activity catalyzing peptidyl-lysine N6- acetylation of various proteins. Thereby, may regulate apoptosis through the acetylation and the regulation of the expression of PROM1 (PubMed:24556617). May also regulate amyloid beta-peptide secretion through acetylation of BACE1 and the regulation of its expression in neurons (PubMed:19011241). {ECO:0000269|PubMed:19011241, ECO:0000269|PubMed:20392701, ECO:0000269|PubMed:24556617}.; . TISSUE SPECIFICITY: Preferentially expressed in liver and kidney. Also detected in brain (at protein level). {ECO:0000269|PubMed:22267734, ECO:0000269|PubMed:9852678}.; unclassifiable (Anatomical System);liver;colon;spleen;kidney;skin;skeletal muscle;stomach; fetal liver;superior cervical ganglion;liver;kidney;trigeminal ganglion;skeletal muscle; 0.27887 0.74184 0.863528995 88.74144845 193.28372 3.01563 NAT8B . . . N-acetyltransferase 8B (putative, gene/pseudogene) FUNCTION: May have a lysine N-acetyltransferase activity catalyzing peptidyl-lysine N6-acetylation of various proteins. Thereby, may regulate apoptosis through the acetylation and the regulation of the expression of PROM1 (PubMed:24556617). May also regulate amyloid beta-peptide secretion through acetylation of BACE1 and the regulation of its expression in neurons (PubMed:19011241). {ECO:0000269|PubMed:19011241, ECO:0000269|PubMed:24556617}.; . . . . . . . . . . NAT8L 0.32467788359779 0.609879484350098 0.0654426320521117 N-acetyltransferase 8 like FUNCTION: Plays a role in the regulation of lipogenesis by producing N-acetylaspartate acid (NAA), a brain-specific metabolite. NAA occurs in high concentration in brain and its hydrolysis plays a significant part in the maintenance of intact white matter. Promotes dopamine uptake by regulating TNF-alpha expression. Attenuates methamphetamine-induced inhibition of dopamine uptake. {ECO:0000269|PubMed:19524112}.; DISEASE: N-acetylaspartate deficiency (NACED) [MIM:614063]: A metabolic disorder resulting in truncal ataxia, marked developmental delay, seizures, and secondary microcephaly. {ECO:0000269|PubMed:19807691}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:19807691}.; unclassifiable (Anatomical System);hypothalamus;sympathetic chain;fovea centralis;choroid;lens;skin;retina;optic nerve;lung;frontal lobe;endometrium;thyroid;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland; superior cervical ganglion;globus pallidus;trigeminal ganglion; 0.22242 . . . 9.68268 0.35594 NAT9 0.0806611770519349 0.872056254460805 0.04728256848726 N-acetyltransferase 9 (putative) . . . lymphoreticular;ovary;colon;skin;prostate;optic nerve;endometrium;gum;thyroid;bone;iris;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;muscle;blood;pancreas;lung;adrenal gland;placenta;liver;duodenum;head and neck;kidney;mammary gland;stomach; atrioventricular node; 0.04369 0.11392 0.43736446 77.56546355 1013.18122 6.12806 NAT10 1.05399824567495e-13 0.968312893349446 0.0316871066504486 N-acetyltransferase 10 FUNCTION: RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs (PubMed:25653167). Catalyzes the formation of N(4)-acetylcytidine (ac4C) at positions 1337 and 1842 in 18S rRNA (By similarity). Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis (PubMed:25653167). Catalyzes the formation of ac4C in serine and leucine tRNAs (By similarity). Requires the tRNA-binding adapter protein THUMBD1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (PubMed:25653167). Can acetylate both histones and microtubules. Histone acetylation may regulate transcription and mitotic chromosome de-condensation. Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization. Acetylates alpha-tubulin, which may affect microtubule stability and cell division (PubMed:14592445, PubMed:17631499, PubMed:18082603, PubMed:19303003). {ECO:0000250|UniProtKB:P53914, ECO:0000255|HAMAP-Rule:MF_03211, ECO:0000269|PubMed:14592445, ECO:0000269|PubMed:17631499, ECO:0000269|PubMed:18082603, ECO:0000269|PubMed:19303003, ECO:0000269|PubMed:25653167}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;larynx;bone;testis;unclassifiable (Anatomical System);pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;cerebellum; superior cervical ganglion; 0.15338 0.13614 -0.545632343 20.02241095 436.76809 4.35684 NAT14 0.143168129273969 0.628583926724858 0.228247944001173 N-acetyltransferase 14 (putative) FUNCTION: Probable acetyltransferase that binds the 5'-GGACTACAG- 3' sequence of coproporphyrinogen oxidase promoter. Able to activate transcription of a reporter construct in vitro.; . TISSUE SPECIFICITY: Expressed in K-562 and HeLa cell lines and in brain. {ECO:0000269|PubMed:10873651}.; myocardium;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;peripheral nerve;cerebellum;thymus; superior cervical ganglion;temporal lobe;thymus; 0.13794 0.11410 . . 1038.06513 6.19042 NAT16 5.90939217834721e-05 0.462717500269771 0.537223405808446 N-acetyltransferase 16 (putative) FUNCTION: Probable N-acetyltransferase. Shows only trace activity toward L-His and no N-acetyltransferase activity toward other amino acids. The physiological substrate of this enzyme is unknown. {ECO:0000269|PubMed:24121108}.; . . optic nerve;lung;macula lutea;fovea centralis;choroid;lens;brain;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.20979 . -0.293801652 32.93819297 1555.43451 7.30940 NATD1 . . . N-acetyltransferase domain containing 1 . . . . . . . . . . . NATP . . . N-acetyltransferase pseudogene . . . . . . . . . . . NAV1 0.999999985195655 1.48043448433666e-08 3.68050288077943e-21 neuron navigator 1 FUNCTION: May be involved in neuronal migration. {ECO:0000250}.; . TISSUE SPECIFICITY: Broadly expressed at low levels. Expressed at high levels in heart, skeletal muscle and placenta. {ECO:0000269|PubMed:12062803, ECO:0000269|PubMed:12079279}.; ovary;adrenal medulla;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;bladder;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;occipital lobe;pons;atrioventricular node;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.18086 0.14662 -1.604060442 3.013682472 1610.37191 7.42689 NAV2 0.997517125070282 0.00248287492971757 4.577302831581e-16 neuron navigator 2 FUNCTION: Possesses 3' to 5' helicase activity and exonuclease activity. Involved in neuronal development, specifically in the development of different sensory organs. {ECO:0000269|PubMed:12214280, ECO:0000269|PubMed:15158073}.; . TISSUE SPECIFICITY: Highly expressed in the brain, kidney and liver. Also expressed in the thyroid, mammary gland, spinal cord, heart, placenta and lung. Abundantly expressed in colon cancers. {ECO:0000269|PubMed:11904404, ECO:0000269|PubMed:12062803, ECO:0000269|PubMed:12079279, ECO:0000269|PubMed:12214280}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;fetal brain;spinal cord;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.41631 0.11088 -1.555318186 3.22009908 8281.16376 19.67042 NAV2-AS1 . . . NAV2 antisense RNA 1 . . . . . . . . . . . NAV2-AS2 . . . NAV2 antisense RNA 2 . . . . . . . . . . . NAV2-AS3 . . . NAV2 antisense RNA 3 . . . . . . . . . . . NAV2-AS4 . . . NAV2 antisense RNA 4 . . . . . . . . . . . NAV2-AS5 . . . NAV2 antisense RNA 5 . . . . . . . . . . . NAV2-IT1 . . . NAV2 intronic transcript 1 . . . . . . . . . . . NAV3 0.999999398861806 6.01138193965489e-07 4.23433117806603e-22 neuron navigator 3 FUNCTION: May regulate IL2 production by T-cells. May be involved in neuron regeneration. {ECO:0000269|PubMed:16166283}.; DISEASE: Note=A chromosomal aberration disrupting NAV3 has been found in patients with Sezary syndrome (PubMed:16166283). Translocation t(12;18)(q21;q21.2) (PubMed:16166283). {ECO:0000269|PubMed:16166283}.; TISSUE SPECIFICITY: Highly expressed in brain. Expressed at low levels in heart and placenta. Present in activated T-cells but not in resting T-cells (at protein level). Down-regulated in primary neuroblastoma. {ECO:0000269|PubMed:12062803, ECO:0000269|PubMed:12079279, ECO:0000269|PubMed:15158073, ECO:0000269|PubMed:16166283}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;larynx;bone;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;hypothalamus;lens;skeletal muscle;lung;pia mater;placenta;macula lutea;visual apparatus;hypopharynx;head and neck;stomach; whole brain;amygdala;dorsal root ganglion;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;olfactory bulb;adipose tissue;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;atrioventricular node;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.80090 0.11717 -2.045202892 1.645435244 577.63321 4.87321 NAXD . . . NAD(P)HX dehydratase FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. {ECO:0000255|HAMAP-Rule:MF_03157}.; . . . . . 0.08515 0.755110637 86.7539514 . . NAXE . . . NAD(P)HX epimerase FUNCTION: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S- specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. {ECO:0000255|HAMAP-Rule:MF_03159}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in kidney, heart and liver. Present in cerebrospinal fluid and urine but not in serum from healthy patients. Present in serum of sepsis patients (at protein level). {ECO:0000269|PubMed:11991719}.; . . 0.38712 0.08568 -0.404032746 26.53338051 . . NBAS 1.89431039938141e-25 0.999906723486475 9.32765135248294e-05 neuroblastoma amplified sequence FUNCTION: Involved in Golgi-to-endoplasmic reticulum (ER) retrograde tranport; the function is proposed to depend on its association in the NRZ complex which is believed to play a role in SNARE assembly at the ER (PubMed:19369418). {ECO:0000269|PubMed:19369418, ECO:0000305}.; DISEASE: Infantile liver failure syndrome 2 (ILFS2) [MIM:616483]: A form of infantile liver failure syndrome, a life-threatening disorder of hepatic function that manifests with acute liver failure in the first few months of life. Clinical features include anemia, renal tubulopathy, developmental delay, seizures, failure to thrive, and liver steatosis and fibrosis. {ECO:0000269|PubMed:26073778}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=NBAS mutations have been found in a multisystem disease affecting the liver, eye, immune system, connective tissue, and bone. Clinical manifestations include a progeroid appearance, short stature, slender bones, epiphyseal dysplasia with multiple phalangeal pseudo-epiphyses, cervical instability, myelopathy, elevated transaminases, hypogammaglobulinemia, reduced natural killer cells, Pelger-Huet anomaly of granulocytes, and in some cases retinal dystrophy and optic atrophy. {ECO:0000269|PubMed:26286438}.; TISSUE SPECIFICITY: Broadly expressed, with highest levels in heart and skeletal muscle, and lowest levels in liver, small intestine and thymus. Well expressed in retinal ganglion cells, epidermal skin cells, and leukocytes. Up-regulated together with N-myc in some neuroblastoma cell lines. {ECO:0000269|PubMed:10882752, ECO:0000269|PubMed:12706883, ECO:0000269|PubMed:20577004, ECO:0000269|PubMed:9926938}.; ovary;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;testis - interstitial;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex; . . -0.224542487 37.33191791 2659.86206 9.69933 NBAT1 . . . neuroblastoma associated transcript 1 . . . . . . . . . . . NBEA 0.999999999999975 2.45004772769829e-14 6.16522429217222e-36 neurobeachin FUNCTION: Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the membrane. May anchor the kinase to cytoskeletal and/or organelle-associated proteins (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Predominant in many brain structures. Also expressed at medium levels in spleen, thymus, prostate, testis and ovary. Low level expression is seen in heart, kidney, pancreas, skeletal muscle and intestine. {ECO:0000269|PubMed:12160729}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;iris;pituitary gland;testis;bladder;brain;unclassifiable (Anatomical System);heart;lacrimal gland;cerebellum cortex;islets of Langerhans;pineal body;spinal cord;pharynx;blood;lens;skeletal muscle;breast;lung;macula lutea;liver;head and neck;kidney;aorta;peripheral nerve; amygdala;dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;occipital lobe;medulla oblongata;fetal brain;prefrontal cortex;globus pallidus;pons;atrioventricular node;caudate nucleus;cingulate cortex; 0.50570 . -1.889004548 1.981599434 952.61584 5.97334 NBEAL1 1.09294225815105e-10 0.999998397262597 1.60262810870003e-06 neurobeachin like 1 . . TISSUE SPECIFICITY: Highly expressed in brain, kidney, prostate and testis. Weakly expressed in ovary, small intestine, colon and peripheral blood leukocytes. May be correlative to several tumors, such as ovary serous adenocarcinoma and metastasis mammary gland carcinoma breast. {ECO:0000269|PubMed:15193433}.; unclassifiable (Anatomical System);breast;lung;cartilage;nasopharynx;placenta;visual apparatus;testis;bladder; dorsal root ganglion;superior cervical ganglion;medulla oblongata;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.41452 0.09301 1.192277263 92.85208776 746.62671 5.42052 NBEAL2 0.862533062213951 0.137466937786046 3.37266891699803e-15 neurobeachin like 2 FUNCTION: Probably involved in thrombopoiesis. Plays a role in the development or secretion of alpha-granules, that contain several growth factors important for platelet biogenesis. {ECO:0000269|PubMed:21765411, ECO:0000269|PubMed:21765412}.; . TISSUE SPECIFICITY: Expressed in megakaryocytes. {ECO:0000269|PubMed:21765411}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;tongue;trigeminal ganglion;whole blood;skeletal muscle;cerebellum; . . -3.116122747 0.460014154 5607.70532 15.49385 NBEAP1 . . . neurobeachin pseudogene 1 . . TISSUE SPECIFICITY: Expressed in prostate and testis. {ECO:0000269|PubMed:12160729, ECO:0000269|PubMed:9159141}.; . . . . . . . . NBEAP2 . . . neurobeachin pseudogene 2 . . . . . . . . . . . NBEAP3 . . . neurobeachin pseudogene 3 . . . . . . . . . . . NBEAP4 . . . neurobeachin pseudogene 4 . . . . . . . . . . . NBEAP5 . . . neurobeachin pseudogene 5 . . . . . . . . . . . NBEAP6 . . . neurobeachin pseudogene 6 . . . . . . . . . . . NBL1 0.108864872574092 0.776589165703011 0.114545961722897 neuroblastoma 1, DAN family BMP antagonist FUNCTION: Possible candidate as a tumor suppressor gene of neuroblastoma. May play an important role in preventing cells from entering the final stage (G1/S) of the transformation process.; . TISSUE SPECIFICITY: Most abundant in normal lung and meningioma.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;endometrium;oesophagus;synovium;bone;thyroid;iris;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;whole brain;prostate;superior cervical ganglion;temporal lobe;ciliary ganglion;trigeminal ganglion; 0.33126 0.23193 0.014844891 54.94810097 0.71398 0.01156 NBN 1.74403595456629e-10 0.594331223102722 0.405668776722875 nibrin FUNCTION: Component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11A. RAD50 may be required to bind DNA ends and hold them in close proximity. NBN modulate the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. NBN also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. NBN is a major player in the control of intra-S-phase checkpoint and there is some evidence that NBN is involved in G1 and G2 checkpoints. The roles of NBS1/MRN encompass DNA damage sensor, signal transducer, and effector, which enable cells to maintain DNA integrity and genomic stability. Forms a complex with RBBP8 to link DNA double-strand break sensing to resection. Enhances AKT1 phosphorylation possibly by association with the mTORC2 complex. {ECO:0000269|PubMed:10888888, ECO:0000269|PubMed:15616588, ECO:0000269|PubMed:19759395, ECO:0000269|PubMed:23762398, ECO:0000269|PubMed:9705271}.; DISEASE: Nijmegen breakage syndrome (NBS) [MIM:251260]: A disorder characterized by chromosomal instability, radiation sensitivity, microcephaly, growth retardation, immunodeficiency and predisposition to cancer, particularly to lymphoid malignancies. {ECO:0000269|PubMed:9590180}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:14684699}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Aplastic anemia (AA) [MIM:609135]: A form of anemia in which the bone marrow fails to produce adequate numbers of peripheral blood elements. It is characterized by peripheral pancytopenia and marrow hypoplasia. {ECO:0000269|PubMed:15338273}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; DISEASE: Note=Defects in NBN might play a role in the pathogenesis of childhood acute lymphoblastic leukemia (ALL). {ECO:0000269|PubMed:11325820}.; TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in testis.; ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;hypopharynx;head and neck;kidney;mammary gland;stomach; amygdala;dorsal root ganglion;medulla oblongata;superior cervical ganglion;testis - interstitial;subthalamic nucleus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.84431 0.65315 1.644346333 96.16654871 2534.24314 9.39528 NBPF1 . . . neuroblastoma breakpoint family member 1 . . TISSUE SPECIFICITY: Widely expressed. The only tissue which shows a weak expression is kidney. {ECO:0000269|PubMed:16079250}.; colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;aorta;stomach;peripheral nerve; . . . . . 10963.86792 22.82724 NBPF2P . . . neuroblastoma breakpoint family member 2, pseudogene . . . . . . . . . . . NBPF3 1.98380335692613e-11 0.378787941923582 0.621212058056581 neuroblastoma breakpoint family member 3 . . TISSUE SPECIFICITY: Expressed in testis and fetal heart, as well as in non small cell lung carcinoma and neuroblastoma cell line. {ECO:0000269|PubMed:16079250}.; unclassifiable (Anatomical System);heart;hypothalamus;colon;skin;breast;bile duct;uterus;pancreas;whole body;lung;ganglion;larynx;bone;thyroid;pituitary gland;liver;testis;head and neck;brain;stomach; . 0.06699 . 3.60019308 99.52819061 1664.61558 7.53254 NBPF4 0.346635143601408 0.484928287907278 0.168436568491314 neuroblastoma breakpoint family member 4 . . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:16079250}.; . . . . . . 29.38781 0.93989 NBPF5P . . . neuroblastoma breakpoint family member 5, pseudogene . . TISSUE SPECIFICITY: Expressed in brain and medulla. {ECO:0000269|PubMed:16079250}.; . . 0.03005 . . . . . NBPF6 0.0874538512080049 0.561173736827633 0.351372411964362 neuroblastoma breakpoint family member 6 . . . colon; . . . . . 3780.70014 12.03898 NBPF7 . . . neuroblastoma breakpoint family member 7 . . . . . 0.03207 . . . . . NBPF8 . . . neuroblastoma breakpoint family member 8 . . TISSUE SPECIFICITY: Expressed in the mammary gland. {ECO:0000269|PubMed:16079250}.; colon; . . . . . . . NBPF9 . . . neuroblastoma breakpoint family member 9 . . TISSUE SPECIFICITY: Expressed in a neuroblastoma cell line. {ECO:0000269|PubMed:16079250}.; smooth muscle;ovary;rectum;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;oral cavity;bile duct;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; . . . . . . . NBPF10 2.80946400390907e-13 0.648067715568221 0.351932284431498 neuroblastoma breakpoint family member 10 . . . unclassifiable (Anatomical System);heart;colon;blood;skeletal muscle;bone marrow;breast;uterus;prostate;lung;frontal lobe;endometrium;larynx;thyroid;placenta;liver;testis;head and neck;germinal center;brain;mammary gland;bladder;stomach; . . . . . 1794.31538 7.81853 NBPF11 . . . neuroblastoma breakpoint family member 11 . . TISSUE SPECIFICITY: Expressed in spinal cord. {ECO:0000269|PubMed:16079250}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;uterus;cerebral cortex;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; . 0.06080 . . . 216.28705 3.17735 NBPF12 0.210636207445938 0.780274993521761 0.00908879903230108 neuroblastoma breakpoint family member 12 . . TISSUE SPECIFICITY: Widely expressed with highest levels in brain, ovary, mammary gland, skin and adipose tissue. Also expressed in testis. Detected in a number of tumors including osteosarcoma, mammary carcinoma and hepatocellular carcinoma. {ECO:0000269|PubMed:11948409, ECO:0000269|PubMed:16079250}.; unclassifiable (Anatomical System);heart;blood;skeletal muscle;bone marrow;breast;lung;thyroid;placenta;hypopharynx;testis;head and neck;amniotic fluid;germinal center;brain;mammary gland;stomach;thymus; . . . . . 2179.23584 8.60443 NBPF13P . . . neuroblastoma breakpoint family member 13, pseudogene . . . . . . . . . . . NBPF14 . . . neuroblastoma breakpoint family member 14 . . TISSUE SPECIFICITY: Expressed in spleen and fetal liver. {ECO:0000269|PubMed:16079250}.; smooth muscle;rectum;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;colon;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus;cerebellum; . 0.01532 . . . . . NBPF15 0.123939063679527 0.779965540136469 0.0960953961840039 neuroblastoma breakpoint family member 15 . . TISSUE SPECIFICITY: Ubiquitously expressed with a higher expression observed in breast and liver. Also expressed in neuroblastoma cell line. {ECO:0000269|PubMed:16079250}.; . . . . . . 11.22617 0.40490 NBPF17P . . . neuroblastoma breakpoint family member 17, pseudogene . . . . . . . . . . . NBPF18P . . . neuroblastoma breakpoint family member 18, pseudogene . . . . . . . . . . . NBPF19 . . . neuroblastoma breakpoint family member 19 . . . . . . . . . . . NBPF20 0.000445919208521471 0.86436378451906 0.135190296272419 neuroblastoma breakpoint family member 20 . . . . . . . . . 231.53373 3.28813 NBPF21P . . . neuroblastoma breakpoint family member 21, pseudogene . . . . . . . . . . . NBPF22P . . . neuroblastoma breakpoint family member 22, pseudogene . . . . . . . . . . . NBPF25P . . . neuroblastoma breakpoint family member 25, pseudogene . . . . . . . . . . . NBPF26 . . . neuroblastoma breakpoint family member 26 . . . . . . . . . . . NBR1 0.000436706949984189 0.999230855189195 0.000332437860821183 neighbor of BRCA1 gene 1 FUNCTION: Acts probably as a receptor for selective autophagosomal degradation of ubiquitinated targets. {ECO:0000269|PubMed:19250911}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; . . 0.867166666 88.81811748 3800.47731 12.10337 NBR2 . . . neighbor of BRCA1 gene 2 (non-protein coding) . . TISSUE SPECIFICITY: Ubiquitous.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;whole body;lung;frontal lobe;placenta;visual apparatus;liver;kidney;brain;bladder; testis - seminiferous tubule;ciliary ganglion;pons;trigeminal ganglion; 0.45783 . . . . . NCALD 0.817423495231911 0.178281702719719 0.00429480204836999 neurocalcin delta FUNCTION: May be involved in the calcium-dependent regulation of rhodopsin phosphorylation. Binds three calcium ions.; . TISSUE SPECIFICITY: Retina, cerebrum, cerebellum, brain stem, spinal cord, testis, ovary and small intestine.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; whole brain;medulla oblongata;thalamus;occipital lobe;superior cervical ganglion;hypothalamus;temporal lobe;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.06735 0.14624 0.080983847 59.76055674 13.73229 0.49778 NCAM1 . . . neural cell adhesion molecule 1 FUNCTION: This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.; . . ovary;sympathetic chain;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;larynx;thyroid;bone;testis;amniotic fluid;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;hypothalamus;pineal body;muscle;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;alveolus;spleen;head and neck;kidney; dorsal root ganglion;whole brain;amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;thalamus;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.98514 0.88469 . . 1534.73665 7.27843 NCAM1-AS1 . . . NCAM1 antisense RNA1 . . . . . . . . . . . NCAM2 0.922157338297282 0.0778424989260149 1.62776703504757e-07 neural cell adhesion molecule 2 FUNCTION: May play important roles in selective fasciculation and zone-to-zone projection of the primary olfactory axons.; . TISSUE SPECIFICITY: Expressed most strongly in adult and fetal brain.; unclassifiable (Anatomical System);amygdala;heart;ovary;salivary gland;intestine;pharynx;colon;blood;skin;uterus;prostate;lung;cornea;endometrium;visual apparatus;liver;testis;kidney;brain;mammary gland; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.30776 0.12163 -0.686998355 15.26893135 4005.66748 12.52704 NCAN 0.154546738217425 0.845452078734711 1.18304786489467e-06 neurocan FUNCTION: May modulate neuronal adhesion and neurite growth during development by binding to neural cell adhesion molecules (NG-CAM and N-CAM). Chondroitin sulfate proteoglycan; binds to hyaluronic acid.; . TISSUE SPECIFICITY: Brain.; unclassifiable (Anatomical System);lung;frontal lobe;cerebellum cortex;tongue;placenta;hippocampus;testis;head and neck;brain;mammary gland;skeletal muscle;aorta; amygdala;whole brain;medulla oblongata;thalamus;superior cervical ganglion;occipital lobe;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.12672 0.16486 -1.741783094 2.418023119 650.1368 5.11512 NCAPD2 5.92581370196276e-08 0.99999938020446 5.60537402513132e-07 non-SMC condensin I complex subunit D2 FUNCTION: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. May target the condensin complex to DNA via its C-terminal domain. {ECO:0000269|PubMed:11136719}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;bladder;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pineal body;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; heart;testis;tumor; 0.05507 0.11966 -0.053328617 48.95022411 2486.10649 9.30731 NCAPD2P1 . . . non-SMC condensin I complex subunit D2 pseudogene 1 . . . . . . . . . . . NCAPD3 0.0731520869970458 0.926847912705656 2.97298000803384e-10 non-SMC condensin II complex subunit D3 FUNCTION: Regulatory subunit of the condensin-2 complex, a complex which establishes mitotic chromosome architecture and is involved in physical rigidity of the chromatid axis. {ECO:0000269|PubMed:14532007}.; . . . . 0.21247 0.09970 -0.374974929 28.11983958 451.0484 4.41414 NCAPG 0.618144197205832 0.381855233176669 5.69617498748479e-07 non-SMC condensin I complex subunit G FUNCTION: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. {ECO:0000269|PubMed:11136719}.; . TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:10910072}.; lymphoreticular;ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;tongue;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;cervix;head and neck;kidney;mammary gland;stomach;thymus; testis - interstitial;fetal liver;tumor;skeletal muscle; 0.24901 0.09279 -0.416983034 25.82566643 1334.35827 6.86127 NCAPG2 0.975711232780226 0.0242887668596066 3.60166996976958e-10 non-SMC condensin II complex subunit G2 FUNCTION: Regulatory subunit of the condensin-2 complex, a complex which establishes mitotic chromosome architecture and is involved in physical rigidity of the chromatid axis. {ECO:0000269|PubMed:14532007}.; . . lymphoreticular;medulla oblongata;ovary;developmental;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;muscle;blood;skeletal muscle;breast;lung;placenta;visual apparatus;head and neck;kidney;stomach; testis - interstitial;testis;ciliary ganglion; 0.73419 0.16411 1.271321208 93.65416372 521.0071 4.66158 NCAPGP1 . . . non-SMC condensin I complex subunit G pseudogene 1 . . . . . . . . . . . NCAPGP2 . . . non-SMC condensin I complex subunit G pseudogene 2 . . . . . . . . . . . NCAPH 0.0321635838191526 0.967759034331468 7.73818493796491e-05 non-SMC condensin I complex subunit H FUNCTION: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. {ECO:0000269|PubMed:11136719}.; . TISSUE SPECIFICITY: Widely expressed at low level. Expressed in proliferating cells. {ECO:0000269|PubMed:11694586}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;tongue;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;fetal liver;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.63999 0.12261 -0.308569083 32.17150271 208.65384 3.11640 NCAPH2 0.652832372947923 0.347157427556805 1.01994952714402e-05 non-SMC condensin II complex subunit H2 FUNCTION: Regulatory subunit of the condensin-2 complex, a complex that seems to provide chromosomes with an additional level of organization and rigidity and in establishing mitotic chromosome architecture. May play a role in lineage-specific role in T-cell development (By similarity). {ECO:0000250, ECO:0000269|PubMed:14532007}.; . . medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;hypothalamus;muscle;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.12174 0.09691 -0.21856543 37.66218448 2077.26388 8.39538 NCBP1 0.99995610858717 4.38914126165233e-05 2.13402856698178e-13 nuclear cap binding protein subunit 1 FUNCTION: Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5'-end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure. Associates with NCBP3 to form an alternative cap- binding complex (CBC) which plays a key role in mRNA export and is particularly important in cellular stress situations such as virus infections. The conventional CBC with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus whereas the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role only in mRNA export. NCBP1/CBP80 is required for cell growth and viability (PubMed:26382858). {ECO:0000269|PubMed:11551508, ECO:0000269|PubMed:12093754, ECO:0000269|PubMed:15059963, ECO:0000269|PubMed:15361857, ECO:0000269|PubMed:16186820, ECO:0000269|PubMed:16317009, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:17873884, ECO:0000269|PubMed:18369367, ECO:0000269|PubMed:19632182, ECO:0000269|PubMed:19648179, ECO:0000269|PubMed:26382858, ECO:0000269|PubMed:7651522, ECO:0000269|PubMed:8069914}.; . . . . 0.08605 0.15385 -0.179930907 40.35739561 103.23186 2.19406 NCBP2 0.266930249458524 0.707853904497226 0.0252158460442496 nuclear cap binding protein subunit 2 FUNCTION: Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5' end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2, thereby being required for miRNA- mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure. The conventional cap-binding complex with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus (PubMed:26382858). {ECO:0000269|PubMed:11551508, ECO:0000269|PubMed:15361857, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:17363367, ECO:0000269|PubMed:17873884, ECO:0000269|PubMed:18369367, ECO:0000269|PubMed:19632182, ECO:0000269|PubMed:26382858}.; . . medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;nasopharynx;placenta;amnion;head and neck;kidney;stomach;aorta; dorsal root ganglion;medulla oblongata;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;pons;trigeminal ganglion; 0.25497 0.17821 -0.053113545 49.38664779 1.24123 0.04352 NCBP2-AS1 . . . NCBP2 antisense RNA 1 . . . . . . . . . . . NCBP2-AS2 . . . NCBP2 antisense RNA 2 (head to head) . . . . . . . . . . . NCBP2L 0.129669930064103 0.617934477867454 0.252395592068443 nuclear cap binding protein subunit 2-like . . . . . 0.07291 0.12110 . . 185.15733 2.95470 NCBP3 . . . nuclear cap binding subunit 3 FUNCTION: Associates with NCBP1/CBP80 to form an alternative cap- binding complex (CBC) which plays a key role in mRNA export. NCBP3 serves as adapter protein linking the capped RNAs (m7GpppG-capped RNA) to NCBP1/CBP80. Unlike the conventional CBC with NCBP2 which binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus, the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role in only mRNA export. The alternative CBC is particularly important in cellular stress situations such as virus infections and the NCBP3 activity is critical to inhibit virus growth (PubMed:26382858). {ECO:0000269|PubMed:26382858}.; . . . . 0.11837 . 0.328949044 73.41354093 . . NCCRP1 0.000145564407364416 0.655694749628317 0.344159685964319 non-specific cytotoxic cell receptor protein 1 homolog (zebrafish) FUNCTION: Promotes cell proliferation. {ECO:0000269|PubMed:22087255}.; . TISSUE SPECIFICITY: Expressed in the esophagus, oral cavity, skin, tongue and reproductive organs. {ECO:0000269|PubMed:22087255}.; unclassifiable (Anatomical System);prostate;lung;placenta; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.13623 . . 33.13985 1.02537 NCDN 0.99673508374991 0.00326472675257506 1.89497514958218e-07 neurochondrin FUNCTION: Probably involved in signal transduction, in the nervous system, via increasing cell surface localization of GRM5 and positively regulating its signaling (By similarity). Required for the spatial learning process. Acts as a negative regulator of Ca(2+)-calmodulin-dependent protein kinase 2 (CaMK2) phosphorylation. May play a role in modulating melanin- concentrating hormone-mediated functions via its interaction with MCHR1 that interferes with G protein-coupled signal transduction. May be involved in bone metabolism. May also be involved in neurite outgrowth. {ECO:0000250, ECO:0000269|PubMed:16945926}.; . TISSUE SPECIFICITY: Abundantly expressed in whole adult brain and in all individual brain regions examined, including spinal cord. Weakly expressed in ovary, testis, fetal brain and small intestine. {ECO:0000269|PubMed:10524216, ECO:0000269|PubMed:9628581}.; unclassifiable (Anatomical System);lymphoreticular;hypothalamus;salivary gland;sympathetic chain;uterus;pancreas;lung;frontal lobe;endometrium;bone;placenta;hippocampus;duodenum;testis;kidney;brain;mammary gland;stomach; dorsal root ganglion;amygdala;whole brain;occipital lobe;medulla oblongata;thalamus;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;pons;atrioventricular node;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.41926 0.12779 -0.979072682 8.752064166 17.19104 0.60416 NCEH1 0.00107451129620312 0.828482011748665 0.170443476955132 neutral cholesterol ester hydrolase 1 FUNCTION: Hydrolyzes 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor. May be responsible for cholesterol ester hydrolysis in macrophages, thereby contributing to the development of atherosclerosis. Also involved in organ detoxification by hydrolyzing exogenous organophosphorus compounds. May contribute to cancer pathogenesis by promoting tumor cell migration. {ECO:0000269|PubMed:17052608}.; . TISSUE SPECIFICITY: Expressed in monocyte-derived macrophages. Up- regulated in invasive melanoma and breast carcinoma cell lines. {ECO:0000269|PubMed:12149457, ECO:0000269|PubMed:18782767}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;testis;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; whole brain;amygdala;subthalamic nucleus;medulla oblongata;cingulate cortex; 0.16519 0.14523 0.086440867 60.47416844 1172.78397 6.50744 NCF1 0.92335956129349 0.0761859036418008 0.000454535064708967 neutrophil cytosolic factor 1 FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). {ECO:0000269|PubMed:19801500, ECO:0000269|PubMed:2547247, ECO:0000269|PubMed:2550933}.; DISEASE: Granulomatous disease, chronic, cytochrome-b-positive 1, autosomal recessive (CGD1) [MIM:233700]: A disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life-threatening bacterial/fungal infections. {ECO:0000269|PubMed:11133775, ECO:0000269|PubMed:23910690}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in peripheral blood monocytes and neutrophils (at protein level). {ECO:0000269|PubMed:2547247, ECO:0000269|PubMed:2550933}.; lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney; . 0.56817 0.38363 . . 42.50316 1.23387 NCF1B . . . neutrophil cytosolic factor 1B pseudogene FUNCTION: May be required for activation of the latent NADPH oxidase (necessary for superoxide production). {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;endometrium;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pharynx;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney; . . 0.11535 . . . . NCF1C . . . neutrophil cytosolic factor 1C pseudogene FUNCTION: May be required for activation of the latent NADPH oxidase (necessary for superoxide production). {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;endometrium;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pharynx;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney; . 0.17774 0.11639 . . . . NCF2 8.50962248758179e-05 0.996458601411404 0.00345630236372062 neutrophil cytosolic factor 2 FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). {ECO:0000269|PubMed:12207919}.; DISEASE: Granulomatous disease, chronic, cytochrome-b-positive 2, autosomal recessive (CGD2) [MIM:233710]: A disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life-threatening bacterial/fungal infections. {ECO:0000269|PubMed:10498624, ECO:0000269|PubMed:10598813, ECO:0000269|PubMed:11112388, ECO:0000269|PubMed:16937026, ECO:0000269|PubMed:18625437, ECO:0000269|PubMed:19624736, ECO:0000269|PubMed:20167518, ECO:0000269|PubMed:23910690, ECO:0000269|PubMed:8286749, ECO:0000269|PubMed:9070911}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.11638 0.32400 1.308134829 94.01391838 4481.78688 13.42911 NCF4 7.89904665161403e-06 0.506646454549928 0.493345646403421 neutrophil cytosolic factor 4 FUNCTION: Component of the NADPH-oxidase, a multicomponent enzyme system responsible for the oxidative burst in which electrons are transported from NADPH to molecular oxygen, generating reactive oxidant intermediates. It may be important for the assembly and/or activation of the NADPH-oxidase complex. {ECO:0000269|PubMed:8280052}.; DISEASE: Granulomatous disease, chronic, cytochrome-b-positive 3, autosomal recessive (CGD3) [MIM:613960]: A disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life-threatening bacterial/fungal infections. {ECO:0000269|PubMed:19692703}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expression is restricted to hematopoietic cells.; unclassifiable (Anatomical System);lymph node;cartilage;umbilical cord;ovary;heart;colon;blood;choroid;skeletal muscle;bone marrow;uterus;pancreas;lung;nasopharynx;bone;placenta;liver;testis;spleen;germinal center;brain; whole blood;trigeminal ganglion;bone marrow; 0.11590 . -0.777005578 12.9747582 53.52119 1.45383 NCK1 0.00103502587808822 0.822339267918255 0.176625706203657 NCK adaptor protein 1 FUNCTION: Adapter protein which associates with tyrosine- phosphorylated growth factor receptors, such as KDR and PDGFRB, or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in the DNA damage response, not in the detection of the damage by ATM/ATR, but for efficient activation of downstream effectors, such as that of CHEK2. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling. Modulates the activation of EIF2AK2/PKR by dsRNA. May play a role in cell adhesion and migration through interaction with ephrin receptors. {ECO:0000269|PubMed:10026169, ECO:0000269|PubMed:16835242, ECO:0000269|PubMed:17803907, ECO:0000269|PubMed:18835251, ECO:0000269|PubMed:23358419, ECO:0000269|PubMed:9430661}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;skin;bone marrow;uterus;prostate;cochlea;endometrium;larynx;gum;thyroid;testis;amniotic fluid;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;cartilage;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;pia mater;lung;nasopharynx;placenta;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.85327 0.61145 0.12689526 63.00424628 232.12384 3.29429 NCK1-AS1 . . . NCK1 antisense RNA 1 (head to head) . . . . . . . . . . . NCK2 0.702843117670504 0.293520717930389 0.00363616439910716 NCK adaptor protein 2 FUNCTION: Adapter protein which associates with tyrosine- phosphorylated growth factor receptors or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in ELK1- dependent transcriptional activation in response to activated Ras signaling. {ECO:0000269|PubMed:10026169, ECO:0000269|PubMed:16835242}.; . TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;salivary gland;colon;parathyroid;skin;uterus;endometrium;thyroid;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;lens;bile duct;breast;pancreas;lung;placenta;visual apparatus;cervix;kidney;mammary gland;stomach; whole brain;testis - seminiferous tubule;prefrontal cortex;testis; 0.24804 0.25902 -0.714505427 14.4019816 20.00595 0.68218 NCKAP1 0.999999990714008 9.28599176475315e-09 5.83999076488527e-21 NCK associated protein 1 FUNCTION: Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1.; . TISSUE SPECIFICITY: Expressed in all tissues examined except peripheral blood leukocytes, with highest expression in brain, heart, and skeletal muscle.; smooth muscle;ovary;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;duodenum;head and neck;kidney;stomach;aorta;cerebellum; occipital lobe;prefrontal cortex; 0.53149 0.18619 -1.199555187 5.761972163 23.37723 0.77966 NCKAP1L 0.990439663587777 0.00956033640486208 7.36049330044647e-12 NCK associated protein 1 like . . TISSUE SPECIFICITY: Expressed only in cells of hematopoietic origin.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;thymus; superior cervical ganglion;white blood cells;pons;trigeminal ganglion;skeletal muscle;bone marrow; 0.46204 0.10469 -0.459259448 23.69072895 714.8596 5.30902 NCKAP5 0.524874191725049 0.475125798111646 1.01633047376373e-08 NCK associated protein 5 . . TISSUE SPECIFICITY: Expressed in fetal and adult brain, leukocytes and fetal fibroblasts.; unclassifiable (Anatomical System);liver;spleen;vein; . . . 0.648405397 84.12951168 8032.79536 19.33390 NCKAP5-IT1 . . . NCKAP5 intronic transcript 1 . . . . . . . . . . . NCKAP5L 0.56561925191278 0.434376370923886 4.37716333345718e-06 NCK associated protein 5 like FUNCTION: Regulates microtubule organization and stabilization. Promotes microtubule growth and bundling formation and stabilizes microtubules by increasing intense acetylation of microtubules (PubMed:26482847, PubMed:26485573). Both tubulin-binding and homodimer formation are required for NCKAP5L-mediated microtubule bundle formation (PubMed:26485573). {ECO:0000269|PubMed:26482847, ECO:0000269|PubMed:26485573}.; . . ovary;salivary gland;intestine;colon;choroid;skin;prostate;bone;iris;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;lung;cornea;placenta;visual apparatus;liver;kidney;mammary gland;stomach; dorsal root ganglion;cingulate cortex; 0.18038 . -0.789972689 12.61500354 3489.39376 11.37205 NCKIPSD 0.00713136165785669 0.992153677411265 0.000714960930878775 NCK interacting protein with SH3 domain FUNCTION: Has an important role in stress fiber formation induced by active diaphanous protein homolog 1 (DRF1). Induces microspike formation, in vivo (By similarity). In vitro, stimulates N-WASP- induced ARP2/3 complex activation in the absence of CDC42 (By similarity). May play an important role in the maintenance of sarcomeres and/or in the assembly of myofibrils into sarcomeres. Implicated in regulation of actin polymerization and cell adhesion. Plays a role in angiogenesis. {ECO:0000250, ECO:0000269|PubMed:22419821}.; . TISSUE SPECIFICITY: Highest expression in heart, brain, skeletal muscle, kidney and liver. Lower levels in placenta, lung, small intestine and leukocytes. Weak expression in colon, thymus and spleen. {ECO:0000269|PubMed:10619843}.; medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;larynx;testis;germinal center;spinal ganglion;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;nervous;urinary;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;liver;duodenum;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;thalamus;medulla oblongata;superior cervical ganglion;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.09081 0.10906 -0.995664936 8.539749941 112.44382 2.30664 NCL 0.999106738363181 0.000893261307775556 3.29043462204896e-10 nucleolin FUNCTION: Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. {ECO:0000269|PubMed:10393184}.; . . ovary;rectum;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;bladder;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;pia mater;lung;cornea;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; . 0.98769 0.73546 -0.686998355 15.26893135 112.77476 2.30967 NCLN 0.509474338262742 0.490358767877402 0.000166893859856295 nicalin FUNCTION: May antagonize Nodal signaling and subsequent organization of axial structures during mesodermal patterning. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in pancreas and skeletal muscle and, at lower levels, in heart. {ECO:0000269|PubMed:15257293}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cerebral cortex;endometrium;larynx;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;spleen;head and neck;cervix;kidney;mammary gland;stomach; adrenal gland;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.67347 0.11432 -0.598810865 18.13517339 1613.74845 7.43427 NCLP1 . . . nucleolin pseudogene 1 . . . . . . . . . . . NCLP2 . . . nucleolin pseudogene 2 . . . . . . . . . . . NCMAP 0.0672670336239585 0.733653909410087 0.199079056965955 non-compact myelin associated protein FUNCTION: Plays a role in myelin formation. {ECO:0000250}.; . . . . 0.21983 . 0.369407109 74.95281906 214.87735 3.16214 NCOA1 0.999077342831501 0.000922657167902116 5.9688283718924e-13 nuclear receptor coactivator 1 FUNCTION: Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3. {ECO:0000269|PubMed:10449719, ECO:0000269|PubMed:12954634, ECO:0000269|PubMed:7481822, ECO:0000269|PubMed:9223281, ECO:0000269|PubMed:9223431, ECO:0000269|PubMed:9296499, ECO:0000269|PubMed:9427757}.; DISEASE: Note=A chromosomal aberration involving NCOA1 is a cause of rhabdomyosarcoma. Translocation t(2;2)(q35;p23) with PAX3 generates the NCOA1-PAX3 oncogene consisting of the N-terminus part of PAX3 and the C-terminus part of NCOA1. The fusion protein acts as a transcriptional activator. Rhabdomyosarcoma is the most common soft tissue carcinoma in childhood, representing 5-8% of all malignancies in children. {ECO:0000269|PubMed:15313887}.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15313887, ECO:0000269|PubMed:9427757}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;urinary;blood;lens;skeletal muscle;breast;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; amygdala;subthalamic nucleus;occipital lobe;medulla oblongata;superior cervical ganglion;fetal brain;prefrontal cortex;globus pallidus;pons;trigeminal ganglion;cingulate cortex;skeletal muscle;parietal lobe; 0.97746 0.38479 -2.190107324 1.38594008 158.73637 2.75127 NCOA2 0.999997381929581 2.6180704177938e-06 1.09814225070386e-15 nuclear receptor coactivator 2 FUNCTION: Transcriptional coactivator for steroid receptors and nuclear receptors. Coactivator of the steroid binding domain (AF- 2) but not of the modulating N-terminal domain (AF-1). Required with NCOA1 to control energy balance between white and brown adipose tissues. Critical regulator of glucose metabolism regulation, acts as RORA coactivator to specifically modulate G6PC expression. Involved in the positive regulation of the transcriptional activity of the glucocorticoid receptor NR3C1 by sumoylation enhancer RWDD3. Positively regulates the circadian clock by acting as a transcriptional coactivator for the CLOCK- ARNTL/BMAL1 heterodimer (By similarity). {ECO:0000250|UniProtKB:Q61026, ECO:0000269|PubMed:23508108, ECO:0000269|PubMed:9430642}.; DISEASE: Note=Chromosomal aberrations involving NCOA2 may be a cause of acute myeloid leukemias. Inversion inv(8)(p11;q13) generates the KAT6A-NCOA2 oncogene, which consists of the N- terminal part of KAT6A and the C-terminal part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and disrupts its function in transcription activation. {ECO:0000269|PubMed:12676584, ECO:0000269|PubMed:15657427, ECO:0000269|PubMed:9558366}.; . lymphoreticular;ovary;sympathetic chain;colon;bone marrow;retina;cerebral cortex;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;blood;skeletal muscle;lung;placenta;liver;spleen;head and neck;cervix;kidney;stomach;cerebellum; amygdala;superior cervical ganglion;prefrontal cortex;testis;ciliary ganglion;atrioventricular node;whole blood;trigeminal ganglion;skeletal muscle;cerebellum; 0.93035 0.31722 -1.03432138 7.855626327 200.44329 3.05943 NCOA3 0.999916717705241 8.32822947574228e-05 1.70283344666859e-15 nuclear receptor coactivator 3 FUNCTION: Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit.; . TISSUE SPECIFICITY: Widely expressed. High expression in heart, skeletal muscle, pancreas and placenta. Low expression in brain, and very low in lung, liver and kidney.; ovary;salivary gland;developmental;intestine;colon;choroid;skin;bone marrow;uterus;frontal lobe;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);pharynx;blood;skeletal muscle;bile duct;breast;lung;cornea;epididymis;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;lymph node;placenta;temporal lobe;white blood cells;ciliary ganglion;pons;trigeminal ganglion;cingulate cortex;skeletal muscle;tonsil; 0.74944 0.12630 -1.232771118 5.537862703 2649.41599 9.66014 NCOA4 0.00856580592851277 0.988741046429618 0.00269314764186892 nuclear receptor coactivator 4 FUNCTION: Enhances the androgen receptor transcriptional activity in prostate cancer cells. Ligand-independent coactivator of the peroxisome proliferator-activated receptor (PPAR) gamma. {ECO:0000269|PubMed:10347167}.; . TISSUE SPECIFICITY: Widely expressed. Also detected in adipose tissues and in different cell lines. Isoform Beta is only expressed in testis.; myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;ganglion;endometrium;cochlea;thyroid;germinal center;bladder;brain;heart;tongue;urinary;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;uterus;whole body;bone;testis;dura mater;pineal gland;spinal ganglion;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach; fetal liver;whole blood;bone marrow; 0.56013 0.29233 1.462485515 95.2111347 323.45545 3.82143 NCOA4P1 . . . nuclear receptor coactivator 4 pseudogene 1 . . . . . . . . . . . NCOA5 0.996800143883867 0.00319984872839713 7.38773605841583e-09 nuclear receptor coactivator 5 FUNCTION: Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC in response to 17-beta-estradiol (E2). {ECO:0000269|PubMed:15073177}.; . TISSUE SPECIFICITY: Widely expressed.; lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;spleen;cervix;kidney;stomach;cerebellum;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.45557 0.12260 -0.955204708 9.170794999 43.91183 1.26199 NCOA6 0.990815417122809 0.0091845828705188 6.67196118783723e-12 nuclear receptor coactivator 6 FUNCTION: Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Coactivates expression in an agonist- and AF2-dependent manner. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ERs), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Probably functions as a general coactivator, rather than just a nuclear receptor coactivator. May also be involved in the coactivation of the NF-kappa-B pathway. May coactivate expression via a remodeling of chromatin and its interaction with histone acetyltransferase proteins.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, prostate, testis and ovary; weakly expressed in lung, thymus and small intestine.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;fetal brain;testis; 0.88710 0.35515 -2.017802488 1.710309035 647.96778 5.10935 NCOA7 0.960907672037716 0.0390923221626879 5.79959583767213e-09 nuclear receptor coactivator 7 FUNCTION: Enhances the transcriptional activities of several nuclear receptors. Involved in the coactivation of different nuclear receptors, such as ESR1, THRB, PPARG and RARA. {ECO:0000269|PubMed:11971969}.; . TISSUE SPECIFICITY: Highly expressed in brain. Weakly expressed in mammary gland, ovary, uterus, prostate, stomach, bladder, spinal cord and pancreas. Expressed in cancer cell line. {ECO:0000269|PubMed:11971969}.; smooth muscle;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;trachea;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;parietal lobe;cerebellum; 0.10866 0.09333 -0.196519234 39.20736023 1154.66608 6.47379 NCOA7-AS1 . . . NCOA7 antisense RNA 1 . . . . . . . . . . . NCOR1 0.999999999256818 7.43181966487626e-10 7.07586816741009e-30 nuclear receptor corepressor 1 FUNCTION: Mediates transcriptional repression by certain nuclear receptors. Part of a complex which promotes histone deacetylation and the formation of repressive chromatin structures which may impede the access of basal transcription factors. Participates in the transcriptional repressor activity produced by BCL6. {ECO:0000269|PubMed:14527417}.; . . ovary;salivary gland;colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;aorta;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;atrioventricular node;pons;caudate nucleus;skin;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.57767 0.62451 -2.137013188 1.49799481 297.95501 3.68236 NCOR1P1 . . . nuclear receptor corepressor 1 pseudogene 1 . . . . . 0.21276 . . . . . NCOR1P2 . . . nuclear receptor corepressor 1 pseudogene 2 . . . . . . . . . . . NCOR1P3 . . . nuclear receptor corepressor 1 pseudogene 3 . . . . . . . . . . . NCOR2 0.999999722324534 2.776754656696e-07 3.18879523265011e-22 nuclear receptor corepressor 2 FUNCTION: Transcriptional corepressor. Mediates the transcriptional repression activity of some nuclear receptors by promoting chromatin condensation, thus preventing access of the basal transcription. Isoform 1 and isoform 5 have different affinities for different nuclear receptors. Involved in the regulation BCL6-dependent of the germinal center (GC) reactions, mainly through the control of the GC B-cells proliferation and survival. {ECO:0000269|PubMed:18212045, ECO:0000269|PubMed:23911289}.; . TISSUE SPECIFICITY: Ubiquitous. High levels of expression are detected in lung, spleen and brain.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;amygdala;heart;cartilage;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; amygdala;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;kidney;trigeminal ganglion;skeletal muscle;cingulate cortex;parietal lobe; 0.88446 0.49851 -2.599674564 0.819768813 6335.441 16.64984 NCR1 7.81574025316709e-05 0.921155148416073 0.0787666941813951 natural cytotoxicity triggering receptor 1 FUNCTION: Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis. {ECO:0000269|PubMed:9730896}.; . TISSUE SPECIFICITY: Selectively expressed by both resting and activated NK cells. {ECO:0000269|PubMed:9730896}.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.05368 0.27304 -0.003562597 53.72729417 254.70415 3.43254 NCR2 0.000163783304597834 0.681097618145827 0.318738598549575 natural cytotoxicity triggering receptor 2 FUNCTION: Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis. {ECO:0000269|PubMed:10049942}.; . TISSUE SPECIFICITY: Selectively expressed by activated NK cells and by in vitro cultured (i.e. activated) TCRg/d lymphoid cells. {ECO:0000269|PubMed:10049942}.; . . 0.02257 0.16100 1.241986644 93.38877094 72.70052 1.77983 NCR3 0.00146130688438596 0.672558728354152 0.325979964761462 natural cytotoxicity triggering receptor 3 FUNCTION: Cytotoxicity-activating receptor that contributes to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis. Engagement of NCR3 by BAG6 also promotes dendritic cell (DC) maturation, both through killing those DCs that did not properly acquire a mature phenotype, and inducing NK cells to release TNFA and IFNG, which promotes DC maturation. {ECO:0000269|PubMed:10562324, ECO:0000269|PubMed:15784725, ECO:0000269|PubMed:18852879}.; . TISSUE SPECIFICITY: Selectively expressed by all resting and activated NK cells and weakly expressed in spleen. {ECO:0000269|PubMed:10562324, ECO:0000269|Ref.2}.; unclassifiable (Anatomical System);lung;cartilage;ovary;placenta;parathyroid;spleen;blood;kidney;germinal center;brain;aorta; . 0.04585 . 0.77170517 87.00754895 180.14774 2.91585 NCR3LG1 . . . natural killer cell cytotoxicity receptor 3 ligand 1 FUNCTION: Triggers NCR3-dependent natural killer cell activation. {ECO:0000269|PubMed:19528259}.; . TISSUE SPECIFICITY: Not detected in any normal tissue tested. Expressed at the surface of several tumor cell lines including T and B-lymphomas, myeloid leukemias, melanomas, carcinomas and large T SV40 antigen-transformed cells (at protein level). {ECO:0000269|PubMed:19528259}.; . . . . . . 408.46733 4.23739 NCRUPAR . . . non-protein coding RNA, upstream of F2R/PAR1 . . . . . . . . . . . NCS1 0.947220876195482 0.0526013827102496 0.000177741094268131 neuronal calcium sensor 1 FUNCTION: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin (By similarity). Stimulates PI4KB kinase activity (By similarity). Involved in long-term synaptic plasticity through its interaction with PICK1 (By similarity). May also play a role in neuron differentiation through inhibition of the activity of N- type voltage-gated calcium channel (By similarity). {ECO:0000250}.; . . . . 0.18713 0.18619 -0.141298762 42.87567823 2.47706 0.09110 NCSTN 0.999982342874537 1.76571248953442e-05 5.67191097468923e-13 nicastrin FUNCTION: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta- amyloid precursor protein). It probably represents a stabilizing cofactor required for the assembly of the gamma-secretase complex.; DISEASE: Acne inversa, familial, 1 (ACNINV1) [MIM:142690]: A chronic relapsing inflammatory disease of the hair follicles characterized by recurrent draining sinuses, painful skin abscesses, and disfiguring scars. Manifestations typically appear after puberty. {ECO:0000269|PubMed:20929727, ECO:0000269|PubMed:21430701, ECO:0000269|PubMed:21495993}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11396676}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;gum;thyroid;iris;amniotic fluid;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach; placenta;testis; 0.56190 0.35558 -0.578583623 18.71903751 139.26492 2.57378 NCSTNP1 . . . nicastrin pseudogene 1 . . . . . . . . . . . NDC1 0.937525025656544 0.0624745145748446 4.59768611372693e-07 NDC1 transmembrane nucleoporin FUNCTION: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane. {ECO:0000269|PubMed:16600873, ECO:0000269|PubMed:16702233}.; . . . . 0.85737 0.10883 -0.089927255 46.99221515 181.94916 2.93065 NDC80 0.00148617426184344 0.99823142071337 0.000282405024786862 NDC80 kinetochore complex component FUNCTION: Acts as a component of the essential kinetochore- associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity (PubMed:9315664, PubMed:12351790, PubMed:14654001, PubMed:14699129, PubMed:15062103, PubMed:15235793, PubMed:15239953, PubMed:15548592, PubMed:16732327). Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (PubMed:15548592). The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules (PubMed:23085020). {ECO:0000269|PubMed:12351790, ECO:0000269|PubMed:14654001, ECO:0000269|PubMed:14699129, ECO:0000269|PubMed:15062103, ECO:0000269|PubMed:15235793, ECO:0000269|PubMed:15239953, ECO:0000269|PubMed:15548592, ECO:0000269|PubMed:16732327, ECO:0000269|PubMed:23085020, ECO:0000269|PubMed:9315664}.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;fetal liver;testis - seminiferous tubule;tumor;skeletal muscle; 0.71777 0.44721 -0.224023033 37.4321774 1749.20507 7.72153 NDE1 0.0471095482859516 0.947758383411676 0.00513206830237232 nudE neurodevelopment protein 1 FUNCTION: Required for centrosome duplication and formation and function of the mitotic spindle. Essential for the development of the cerebral cortex. May regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a post- mitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex. {ECO:0000269|PubMed:17600710, ECO:0000269|PubMed:21529752}.; DISEASE: Lissencephaly 4 (LIS4) [MIM:614019]: A neurodevelopmental disorder characterized by lissencephaly, severe brain atrophy, extreme microcephaly, and profound mental retardation. {ECO:0000269|PubMed:21529751, ECO:0000269|PubMed:21529752}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Microhydranencephaly (MHAC) [MIM:605013]: A severe neurodevelopmental disorder characterized by microcephaly, severe motor and mental retardation, spasticity, and brain malformations that include gross dilation of the ventricles with complete absence of the cerebral hemispheres or severe delay in their development. {ECO:0000269|PubMed:22526350}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the neuroepithelium throughout the developing brain, including the cerebral cortex and cerebellum. {ECO:0000269|PubMed:21529752}.; lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;synovium;bone;pituitary gland;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;muscle;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach;thymus; dorsal root ganglion;occipital lobe;superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion;skin;bone marrow; 0.47017 0.16922 -0.822919685 11.76574664 1055.06218 6.23591 NDE1P1 . . . nudE neurodevelopment protein 1 pseudogene 1 . . . . . . . . . . . NDE1P2 . . . nudE neurodevelopment protein 1 pseudogene 2 . . . . . . . . . . . NDEL1 0.979221293391323 0.0207751386672432 3.5679414333951e-06 nudE neurodevelopment protein 1 like 1 FUNCTION: Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Plays a role, together with DISC1, in the regulation of neurite outgrowth. Required for mitosis in some cell types but appears to be dispensible for mitosis in cortical neuronal progenitors, which instead requires NDE1. Facilitates the polymerization of neurofilaments from the individual subunits NEFH and NEFL. {ECO:0000269|PubMed:12556484, ECO:0000269|PubMed:14970193, ECO:0000269|PubMed:16291865, ECO:0000269|PubMed:17600710}.; . TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. {ECO:0000269|PubMed:16005531}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;larynx;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach; whole brain;amygdala;adrenal cortex;globus pallidus;caudate nucleus; 0.66639 0.17888 0.060756528 58.52795471 76.40125 1.83335 NDFIP1 0.920196502722478 0.0792998972758372 0.000503600001684777 Nedd4 family interacting protein 1 FUNCTION: Activates HECT domain-containing E3 ubiquitin-protein ligases, including NEDD4 and ITCH, and consequently modulates the stability of their targets. As a result, controls many cellular processes. Prevents chronic T-helper cells-mediated inflammation by activating ITCH and thus controlling JUNB degradation (By similarity). In cortical neurons, mediates the ubiquitination of SLC11A2/DMT1 by NEDD4L, leading to down-regulation of the divalent metal transporter and protection of the cells from cobalt and iron toxicity (PubMed:19706893). Modulates EGFR signaling through multiple pathways. In particular, may regulate the ratio of AKT1- to-MAPK8 signaling in response to EGF, acting on AKT1 probably through PTEN destabilization and on MAPK8 through ITCH-dependent MAP2K4 inactivation. As a result, may control cell growth rate (PubMed:20534535). Enhances the ubiquitination of BRAT1 mediated by E3 ubiquitin-protein ligases: NEDD4, NEDD4L and ITCH, and is required for the nuclear localization of ubiquitinated BRAT1 (PubMed:25631046). {ECO:0000250|UniProtKB:Q8R0W6, ECO:0000269|PubMed:19343052, ECO:0000269|PubMed:19706893, ECO:0000269|PubMed:20534535, ECO:0000269|PubMed:25631046}.; . TISSUE SPECIFICITY: Widely expressed. Higher levels are detected in cerebellum, pituitary, thalamus, kidney, liver, testis, salivary glands and placenta. Also expressed in fetal brain, kidney and lung. {ECO:0000269|PubMed:11748237}.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach;aorta;cerebellum; whole brain;amygdala;occipital lobe;thalamus;subthalamic nucleus;thyroid;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.20518 0.12378 -0.163345027 41.24793583 73.36914 1.78988 NDFIP1P1 . . . Nedd4 family interacting protein 1 pseudogene 1 . . . . . . . . . . . NDFIP2 0.801878730067158 0.196982258857621 0.00113901107522054 Nedd4 family interacting protein 2 FUNCTION: Activates HECT domain-containing E3 ubiquitin-protein ligases, including ITCH, NEDD4, NEDD4L, SMURF2, WWP1 and WWP2, and consequently modulates the stability of their targets. As a result, may control many cellular processes. Recruits ITCH, NEDD4 and SMURF2 to endosomal membranes. May modulate EGFR signaling. {ECO:0000269|PubMed:12761501, ECO:0000269|PubMed:19343052, ECO:0000269|PubMed:20534535}.; . TISSUE SPECIFICITY: Expressed in brain, lung, heart, skeletal muscle, kidney, liver and placenta. {ECO:0000269|PubMed:12796489}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;stomach; amygdala;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;pons;atrioventricular node;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.14456 0.10625 0.327131069 73.27199811 599.78046 4.95722 NDFIP2-AS1 . . . NDFIP2 antisense RNA 1 . . . . . . . . . . . NDN 0.470364294438916 0.505326048661179 0.0243096568999054 necdin, MAGE family member FUNCTION: Growth suppressor that facilitates the entry of the cell into cell cycle arrest. Functionally similar to the retinoblastoma protein it binds to and represses the activity of cell-cycle- promoting proteins such as SV40 large T antigen, adenovirus E1A, and the transcription factor E2F. Necdin also interacts with p53 and works in an additive manner to inhibit cell growth. Functions also as transcription factor and binds directly to specific guanosine-rich DNA sequences (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Almost ubiquitous. Detected in fetal brain, lung, liver and kidney; in adult heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine and colon. Not detected in peripheral blood leukocytes. In brain, restricted to post- mitotic neurons.; salivary gland;colon;fovea centralis;choroid;vein;skin;retina;optic nerve;frontal lobe;cochlea;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;hypothalamus;adrenal cortex;lens;pancreas;lung;placenta;macula lutea;hippocampus;alveolus;spleen;head and neck;kidney;stomach;thymus; amygdala;hypothalamus; 0.28380 0.20471 0.21689899 68.12927577 66.28525 1.67701 NDNF 0.152719665162684 0.830492869422141 0.016787465415175 neuron-derived neurotrophic factor FUNCTION: Promotes matrix assembly and cell adhesiveness (By similarity). Promotes neuron migration, growth and survival as well as neurite outgrowth (PubMed:20969804). Promotes endothelial cell survival, vessel formation and plays an important role in the process of revascularization through NOS3-dependent mechanisms (PubMed:24706764). {ECO:0000250|UniProtKB:Q8C119, ECO:0000269|PubMed:20969804, ECO:0000269|PubMed:24706764}.; . . . . 0.61496 0.10970 -0.666770504 15.86459071 185.31511 2.95689 NDOR1 2.60774272635224e-05 0.98176021282178 0.0182137097509559 NADPH dependent diflavin oxidoreductase 1 FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins (By similarity). Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis. Transfers electrons from NADPH to the Fe/S cluster of CIAPIN1. {ECO:0000255|HAMAP-Rule:MF_03178, ECO:0000269|PubMed:10625700, ECO:0000269|PubMed:20802492, ECO:0000269|PubMed:23596212}.; . TISSUE SPECIFICITY: Low expression in brain, heart, kidney, pancreas, prostate and skeletal muscle. Highest levels in the placenta. Expressed in cancer cell lines including promyelocytic leukemia, HeLaS3, chronic myelagenous leukemia, lymphoblastic leukemia, Burkitt's lymphoma, colorectal adenocarcinoma, lung carcinoma, and melanoma G-361. {ECO:0000269|PubMed:12871939}.; unclassifiable (Anatomical System);lung;frontal lobe;endometrium;bone;hippocampus;colon;blood;germinal center;spinal ganglion;brain;skin;retina; testis - seminiferous tubule;skeletal muscle;cingulate cortex; 0.12811 0.13299 0.984695213 90.46355272 1910.00407 8.04752 NDP 0.64382884136087 0.329215735282968 0.0269554233561623 Norrie disease (pseudoglioma) FUNCTION: Activates the canonical Wnt signaling pathway through FZD4 and LRP5 coreceptor. Plays a central role in retinal vascularization by acting as a ligand for FZD4 that signals via stabilizing beta-catenin (CTNNB1) and activating LEF/TCF-mediated transcriptional programs. Acts in concert with TSPAN12 to activate FZD4 independently of the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1). May be involved in a pathway that regulates neural cell differentiation and proliferation. Possible role in neuroectodermal cell-cell interaction.; DISEASE: Vitreoretinopathy, exudative 2 (EVR2) [MIM:305390]: A disorder of the retinal vasculature characterized by an abrupt cessation of growth of peripheral capillaries, leading to an avascular peripheral retina. This may lead to compensatory retinal neovascularization, which is thought to be induced by hypoxia from the initial avascular insult. New vessels are prone to leakage and rupture causing exudates and bleeding, followed by scarring, retinal detachment and blindness. Clinical features can be highly variable, even within the same family. Patients with mild forms of the disease are asymptomatic, and their only disease related abnormality is an arc of avascular retina in the extreme temporal periphery. {ECO:0000269|PubMed:16163268, ECO:0000269|PubMed:16970763, ECO:0000269|PubMed:17296899, ECO:0000269|PubMed:17325173, ECO:0000269|PubMed:8252044, ECO:0000269|PubMed:8946107, ECO:0000269|PubMed:9143917}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the outer nuclear, inner nuclear and ganglion cell layers of the retina, and in fetal and adult brain. {ECO:0000269|PubMed:10452356}.; . . 0.41414 0.47945 0.279402865 70.86577023 21.00936 0.71138 NDP-AS1 . . . NDP antisense RNA 1 . . . . . . . . . . . NDRG1 0.0538232412513876 0.945324473039239 0.000852285709372896 N-myc downstream regulated 1 FUNCTION: Stress-responsive protein involved in hormone responses, cell growth, and differentiation. Acts as a tumor suppressor in many cell types. Necessary but not sufficient for p53/TP53- mediated caspase activation and apoptosis. Has a role in cell trafficking, notably of the Schwann cell, and is necessary for the maintenance and development of the peripheral nerve myelin sheath. Required for vesicular recycling of CDH1 and TF. May also function in lipid trafficking. Protects cells from spindle disruption damage. Functions in p53/TP53-dependent mitotic spindle checkpoint. Regulates microtubule dynamics and maintains euploidy. {ECO:0000269|PubMed:15247272, ECO:0000269|PubMed:15377670, ECO:0000269|PubMed:17786215, ECO:0000269|PubMed:9766676}.; DISEASE: Charcot-Marie-Tooth disease 4D (CMT4D) [MIM:601455]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot- Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie-Tooth disease are designated CMT4. {ECO:0000269|PubMed:10831399}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous; expressed most prominently in placental membranes and prostate, kidney, small intestine, and ovary tissues. Also expressed in heart, brain, skeletal muscle, lung, liver and pancreas. Low levels in peripheral blood leukocytes and in tissues of the immune system. Expressed mainly in epithelial cells. Also found in Schwann cells of peripheral neurons. Reduced expression in adenocarcinomas compared to normal tissues. In colon, prostate and placental membranes, the cells that border the lumen show the highest expression. {ECO:0000269|PubMed:12432451, ECO:0000269|PubMed:8939898, ECO:0000269|PubMed:9251681, ECO:0000269|PubMed:9605764}.; myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;ganglion;frontal lobe;endometrium;cochlea;thyroid;germinal center;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;prostate;superior cervical ganglion;olfactory bulb;spinal cord;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion; 0.36581 0.38096 -0.268115223 34.70747818 162.03964 2.78108 NDRG2 0.126597034289842 0.872388563164072 0.0010144025460861 NDRG family member 2 FUNCTION: Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation. {ECO:0000269|PubMed:12845671, ECO:0000269|PubMed:16103061, ECO:0000269|PubMed:21247902}.; . TISSUE SPECIFICITY: Highly expressed in brain, heart, skeletal muscle and salivary gland, and moderately in kidney and liver. Expressed in dendritic cells, but not in other blood cells. Expression levels are low in pancreatic and liver cancer tissues; absent in meningioma. Expressed in low-grade gliomas but present at low levels in glioblastoma. Isoform 1 and isoform 2 are present in brain neurons and up-regulated in Alzheimer disease (at protein level). {ECO:0000269|PubMed:11352569, ECO:0000269|PubMed:11936845, ECO:0000269|PubMed:12845671, ECO:0000269|PubMed:14572661, ECO:0000269|PubMed:15207261, ECO:0000269|PubMed:15526377, ECO:0000269|PubMed:16103061}.; myocardium;smooth muscle;ovary;sympathetic chain;colon;parathyroid;choroid;skin;retina;uterus;prostate;frontal lobe;oesophagus;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;hypothalamus;muscle;urinary;lens;skeletal muscle;pancreas;lung;epididymis;placenta;hippocampus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach; whole brain;amygdala;medulla oblongata;subthalamic nucleus;occipital lobe;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;prefrontal cortex;globus pallidus;caudate nucleus;pons;cingulate cortex;parietal lobe;cerebellum; 0.15361 0.10322 0.040529541 57.15380986 83.82612 1.94901 NDRG3 0.919621043818656 0.0803746410837246 4.31509761960486e-06 NDRG family member 3 . . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain. {ECO:0000269|PubMed:11352569}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;muscle;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; whole brain;amygdala;thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.17547 0.07693 -0.60427181 17.74593064 34.06382 1.04453 NDRG4 0.0198090719902488 0.976318227591751 0.0038727004180002 NDRG family member 4 FUNCTION: Contributes to the maintenance of intracerebral BDNF levels within the normal range, which is necessary for the preservation of spatial learning and the resistance to neuronal cell death caused by ischemic stress (By similarity). May enhance growth factor-induced ERK1 and ERK2 phosphorylation, including that induced by PDGF and FGF. May attenuate NGF-promoted ELK1 phosphorylation in a microtubule-dependent manner. {ECO:0000250, ECO:0000269|PubMed:12755708}.; . TISSUE SPECIFICITY: Expressed predominantly in brain and heart (at protein level). In the brain, detected in astrocytes. Isoform 1 and isoform 2 are only expressed in brain. Isoform 3 is expressed in both heart and brain. Up-regulated in glioblastoma multiforme cells. {ECO:0000269|PubMed:11352569, ECO:0000269|PubMed:12755708, ECO:0000269|PubMed:19592488}.; myocardium;sympathetic chain;colon;substantia nigra;fovea centralis;vein;retina;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;testis;spinal ganglion;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;islets of Langerhans;hypothalamus;pineal body;lens;skeletal muscle;breast;pancreas;lung;macula lutea;visual apparatus;hippocampus;spleen;head and neck;stomach;cerebellum;thymus; dorsal root ganglion;amygdala;whole brain;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.23089 0.12093 -0.778825328 12.88039632 32.25148 1.00965 NDST1 0.998138371728285 0.0018616278729017 3.98813674923818e-10 N-deacetylase/N-sulfotransferase 1 FUNCTION: Essential bifunctional enzyme that catalyzes both the N- deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Compared to other NDST enzymes, its presence is absolutely required. Participates in biosynthesis of heparan sulfate that can ultimately serve as L- selectin ligands, thereby playing a role in inflammatory response. {ECO:0000269|PubMed:10758005, ECO:0000269|PubMed:12634318}.; . TISSUE SPECIFICITY: Widely expressed. Expression is most abundant in heart, liver and pancreas.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;thyroid;bone;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;hypopharynx;head and neck;cervix;kidney; superior cervical ganglion;testis - interstitial;tongue;pons;fetal thyroid;trigeminal ganglion;skeletal muscle; 0.75606 0.18509 -1.747196778 2.359046945 49.57817 1.37784 NDST2 0.052949614092355 0.947014505127191 3.58807804540948e-05 N-deacetylase/N-sulfotransferase 2 FUNCTION: Essential bifunctional enzyme that catalyzes both the N- deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. {ECO:0000269|PubMed:10758005, ECO:0000269|PubMed:12634318, ECO:0000269|PubMed:16343444}.; . . ovary;colon;fovea centralis;choroid;bone marrow;uterus;prostate;frontal lobe;cerebral cortex;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach;cerebellum; globus pallidus;trigeminal ganglion; 0.66905 0.13798 -1.704901154 2.518282614 128.24621 2.46824 NDST3 0.0201167463351311 0.979851594566064 3.16590988054978e-05 N-deacetylase/N-sulfotransferase 3 FUNCTION: Essential bifunctional enzyme that catalyzes both the N- deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has high deacetylase activity but low sulfotransferase activity. {ECO:0000269|PubMed:9915799}.; . TISSUE SPECIFICITY: Expressed in brain, kidney, liver, fetal and adult lung, adult pancreas, placenta, fetal spleen and fetal thymus. Not detected in adult/ fetal heart and skeletal muscle. {ECO:0000269|PubMed:9915799}.; unclassifiable (Anatomical System);lung;hippocampus;liver;spleen;brain;skeletal muscle;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.35349 0.11979 -0.997481928 8.47487615 32.32357 1.01077 NDST4 0.0823391729749423 0.917657259809557 3.56721550086743e-06 N-deacetylase/N-sulfotransferase 4 FUNCTION: Essential bifunctional enzyme that catalyzes both the N- deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has low deacetylase activity but high sulfotransferase activity (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System); trigeminal ganglion; 0.50057 0.10408 -0.042196577 50.49539986 255.16462 3.43597 NDUFA1 0.580718048098361 0.376059374098937 0.0432225778027025 NADH:ubiquinone oxidoreductase subunit A1 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . TISSUE SPECIFICITY: Primarily expressed in heart and skeletal muscle.; . . 0.00084 1.02E-3 0.279402865 70.86577023 2.94825 0.10678 NDUFA2 0.339536516355874 0.601199248102735 0.0592642355413913 NADH:ubiquinone oxidoreductase subunit A2 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;bile duct;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta; whole brain;superior cervical ganglion;testis - seminiferous tubule;heart;temporal lobe;liver;testis;skeletal muscle; 0.32026 0.18095 0.191216164 66.57230479 11.36697 0.41002 NDUFA3 0.00138556181931516 0.426199874155837 0.572414564024848 NADH:ubiquinone oxidoreductase subunit A3 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;trophoblast;heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;pia mater;lung;cornea;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; . 0.10837 . 0.191216164 66.57230479 26.31742 0.85336 NDUFA3P1 . . . NADH:ubiquinone oxidoreductase subunit A3 pseudogene 1 . . . . . . . . . . . NDUFA3P2 . . . NADH:ubiquinone oxidoreductase subunit A3 pseudogene 2 . . . . . . . . . . . NDUFA3P3 . . . NADH:ubiquinone oxidoreductase subunit A3 pseudogene 3 . . . . . . . . . . . NDUFA3P4 . . . NADH:ubiquinone oxidoreductase subunit A3 pseudogene 4 . . . . . . . . . . . NDUFA3P5 . . . NADH:ubiquinone oxidoreductase subunit A3 pseudogene 5 . . . . . . . . . . . NDUFA3P6 . . . NADH:ubiquinone oxidoreductase subunit A3 pseudogene 6 . . . . . . . . . . . NDUFA4 0.480021717091325 0.497273743121045 0.0227045397876302 NDUFA4, mitochondrial complex associated FUNCTION: Cytochrome c oxidase (COX, complex IV) is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. Required for complex IV maintenance. {ECO:0000269|PubMed:22902835}.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. {ECO:0000269|PubMed:23746447}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;substantia nigra;skin;retina;bone marrow;prostate;optic nerve;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;vein;uterus;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;placenta;hippocampus;duodenum;kidney;stomach;aorta; amygdala;whole brain;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;kidney;cingulate cortex;parietal lobe;cerebellum; 0.66236 0.23021 -0.09720619 46.20193442 6.83162 0.25375 NDUFA4L2 0.0142523749586636 0.677631917988011 0.308115707053325 NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 4-like 2 . . . . . 0.49332 0.14339 -0.119252484 44.53880632 11.78619 0.42640 NDUFA4P1 . . . NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 4, 9kDa, pseudogene 1 . . . . . . . . . . . NDUFA4P2 . . . NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 4, 9kDa, pseudogene 2 . . . . . . . . . . . NDUFA5 0.173963053327748 0.768983966531575 0.0570529801406768 NADH:ubiquinone oxidoreductase subunit A5 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . TISSUE SPECIFICITY: Expressed in all tissues examined with highest levels in heart, skeletal muscle and brain.; myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;atrium;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pia mater;lung;adrenal gland;placenta;hippocampus;duodenum;kidney;stomach;aorta;thymus; amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;hypothalamus;temporal lobe;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;thyroid;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;pituitary; 0.10685 . -0.185391282 39.67916962 2.068 0.06691 NDUFA5P1 . . . NADH:ubiquinone oxidoreductase subunit A5 pseudogene 1 . . . . . . . . . . . NDUFA5P2 . . . NADH:ubiquinone oxidoreductase subunit A5 pseudogene 2 . . . . . . . . . . . NDUFA5P3 . . . NADH:ubiquinone oxidoreductase subunit A5 pseudogene 3 . . . . . . . . . . . NDUFA5P4 . . . NADH:ubiquinone oxidoreductase subunit A5 pseudogene 4 . . . . . . . . . . . NDUFA5P5 . . . NADH:ubiquinone oxidoreductase subunit A5 pseudogene 5 . . . . . . . . . . . NDUFA5P6 . . . NADH:ubiquinone oxidoreductase subunit A5 pseudogene 6 . . . . . . . . . . . NDUFA5P7 . . . NADH:ubiquinone oxidoreductase subunit A5 pseudogene 7 . . . . . . . . . . . NDUFA5P8 . . . NADH:ubiquinone oxidoreductase subunit A5 pseudogene 8 . . . . . . . . . . . NDUFA5P9 . . . NADH:ubiquinone oxidoreductase subunit A5 pseudogene 9 . . . . . . . . . . . NDUFA5P10 . . . NADH:ubiquinone oxidoreductase subunit A5 pseudogene 10 . . . . . . . . . . . NDUFA5P11 . . . NADH:ubiquinone oxidoreductase subunit A5 pseudogene 11 . . . . . . . . . . . NDUFA5P12 . . . NADH:ubiquinone oxidoreductase subunit A5 pseudogene 12 . . . . . . . . . . . NDUFA6 0.00325949355170513 0.604349357267289 0.392391149181006 NADH:ubiquinone oxidoreductase subunit A6 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . . . 0.09570 0.33627 0.459411326 78.28497287 2105.13885 8.44632 NDUFA6-AS1 . . . NDUFA6 antisense RNA 1 (head to head) . . . . . . . . . . . NDUFA7 0.00402195717519935 0.649780929015901 0.3461971138089 NADH:ubiquinone oxidoreductase subunit A7 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . myocardium;ovary;umbilical cord;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;pineal body;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;placenta;kidney;stomach;aorta; whole brain;thalamus;heart;tumor;white blood cells;cingulate cortex;skeletal muscle; 0.13721 0.13250 0.569646743 81.88841708 169.17891 2.83662 NDUFA8 0.202476373061858 0.753815958553697 0.0437076683844445 NADH:ubiquinone oxidoreductase subunit A8 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . . . 0.41640 0.22613 -0.229483771 36.86010852 28.71647 0.91898 NDUFA8P1 . . . NADH:ubiquinone oxidoreductase subunit A8 pseudogene 1 . . . . . . . . . . . NDUFA9 0.542744183961533 0.457127358993726 0.000128457044741012 NADH:ubiquinone oxidoreductase subunit A9 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . ovary;skin;bone marrow;retina;prostate;ganglion;frontal lobe;endometrium;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;amnion;kidney;stomach;aorta; superior cervical ganglion;heart;kidney;trigeminal ganglion;skeletal muscle; 0.16620 0.16982 0.308721233 72.59966973 156.86301 2.73582 NDUFA9P1 . . . NADH:ubiquinone oxidoreductase subunit A9 pseudogene 1 . . . . . . . . . . . NDUFA10 0.00138793990464123 0.964065844321483 0.0345462157738758 NADH:ubiquinone oxidoreductase subunit A10 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;hippocampus;duodenum;kidney;aorta;stomach;thymus;cerebellum; whole brain;amygdala;thalamus;occipital lobe;superior cervical ganglion;hypothalamus;prefrontal cortex;pons;caudate nucleus;kidney;parietal lobe;skeletal muscle; 0.06690 0.10997 0.060756528 58.52795471 1093.05276 6.32741 NDUFA11 0.538189295082718 0.404301171955952 0.0575095329613297 NADH:ubiquinone oxidoreductase subunit A11 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:18306244}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;thyroid;germinal center;bladder;brain;heart;pineal body;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; whole brain;prostate;heart;liver; 0.06215 0.08575 . . 709.05965 5.28871 NDUFA12 0.00201599261273099 0.739345907767269 0.25863809962 NADH:ubiquinone oxidoreductase subunit A12 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. {ECO:0000269|PubMed:21617257}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve; whole brain;occipital lobe;superior cervical ganglion;testis - interstitial;medulla oblongata;hypothalamus;temporal lobe;caudate nucleus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.09390 0.11187 -0.09720619 46.20193442 10.36158 0.37720 NDUFA12P1 . . . NADH:ubiquinone oxidoreductase subunit A12 pseudogene 1 . . . . . . . . . . . NDUFA13 0.000121026586319051 0.386817455064848 0.613061518348833 NADH:ubiquinone oxidoreductase subunit A13 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes. {ECO:0000269|PubMed:12628925, ECO:0000269|PubMed:12867595, ECO:0000269|PubMed:15753091}.; DISEASE: Hurthle cell thyroid carcinoma (HCTC) [MIM:607464]: A rare type of thyroid cancer accounting for only about 3-10% of all differentiated thyroid cancers. These neoplasms are considered a variant of follicular carcinoma of the thyroid and are referred to as follicular carcinoma, oxyphilic type. {ECO:0000269|PubMed:15841082}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, with highest expression in heart, skeletal muscle, liver, kidney and placenta. In intestinal mucosa, down-regulated in areas involved in Crohn disease and ulcerative colitis. {ECO:0000269|PubMed:10924506}.; myocardium;lymphoreticular;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;pineal body;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;kidney;stomach;aorta;thymus; whole brain;thalamus;heart;hypothalamus;temporal lobe;liver;prefrontal cortex;kidney;cingulate cortex; 0.06426 0.14628 -0.007201372 53.19061099 33.76885 1.04001 NDUFAB1 0.755255332218331 0.235287388255422 0.00945727952624691 NADH:ubiquinone oxidoreductase subunit AB1 FUNCTION: Carrier of the growing fatty acid chain in fatty acid biosynthesis in mitochondria. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity). {ECO:0000250}.; . . myocardium;lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;duodenum;kidney;stomach;aorta; amygdala;whole brain;thalamus;heart;temporal lobe;globus pallidus;skeletal muscle;parietal lobe; 0.22360 0.43943 -0.207437529 38.2814343 9.57874 0.35281 NDUFAB1P1 . . . NADH:ubiquinone oxidoreductase subunit AB1 pseudogene 1 . . . . . . . . . . . NDUFAF1 0.00389629034560786 0.853600408241442 0.14250330141295 NADH:ubiquinone oxidoreductase complex assembly factor 1 FUNCTION: Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11935339}.; myocardium;medulla oblongata;ovary;colon;skin;uterus;prostate;whole body;bone;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;pineal body;lung;placenta;visual apparatus;liver;alveolus;spleen;cervix;kidney;stomach; medulla oblongata;superior cervical ganglion;occipital lobe;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion;cingulate cortex; 0.10476 . 0.575097644 82.1656051 1855.29644 7.94118 NDUFAF2 3.85650772594405e-07 0.108920021662416 0.891079592686811 NADH:ubiquinone oxidoreductase complex assembly factor 2 FUNCTION: Acts as a molecular chaperone for mitochondrial complex I assembly. {ECO:0000269|PubMed:16200211}.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:16200211}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in ESCC cells. Also expressed in heart, skeletal muscle, liver, and in fibroblasts. {ECO:0000269|PubMed:15774466, ECO:0000269|PubMed:16200211}.; medulla oblongata;ovary;salivary gland;intestine;colon;skin;prostate;optic nerve;whole body;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;kidney;stomach; trigeminal ganglion;skeletal muscle; 0.01203 0.05242 0.080983847 59.76055674 12.55307 0.45787 NDUFAF3 4.85972513641338e-05 0.659149597640362 0.340801805108274 NADH:ubiquinone oxidoreductase complex assembly factor 3 FUNCTION: Essential factor for the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). {ECO:0000269|PubMed:19463981}.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:19463981}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;skin;retina;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; testis - interstitial;heart;testis - seminiferous tubule;liver;testis; 0.16011 0.12634 -0.251530012 35.42108988 254.16433 3.42960 NDUFAF4 0.382015184836328 0.6075958119059 0.010389003257772 NADH:ubiquinone oxidoreductase complex assembly factor 4 FUNCTION: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). May be involved in cell proliferation and survival of hormone-dependent tumor cells. May be a regulator of breast tumor cell invasion. {ECO:0000269|PubMed:14871833, ECO:0000269|PubMed:17001319, ECO:0000269|PubMed:18179882}.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:18179882}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.22360 0.09422 0.014844891 54.94810097 14.54287 0.52350 NDUFAF4P1 . . . NADH:ubiquinone oxidoreductase complex assembly factor 4 pseudogene 1 . . . . . . . . . . . NDUFAF4P2 . . . NADH:ubiquinone oxidoreductase complex assembly factor 4 pseudogene 2 . . . . . . . . . . . NDUFAF4P3 . . . NADH:ubiquinone oxidoreductase complex assembly factor 4 pseudogene 3 . . . . . . . . . . . NDUFAF4P4 . . . NADH:ubiquinone oxidoreductase complex assembly factor 4 pseudogene 4 . . . . . . . . . . . NDUFAF5 1.00133797830871e-05 0.790272798804403 0.209717187815813 NADH:ubiquinone oxidoreductase complex assembly factor 5 FUNCTION: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I, MT-ND1) at early stages. May have methyltransferase activity. {ECO:0000269|PubMed:18940309}.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:18940309}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. {ECO:0000269|PubMed:19542079}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.08553 0.10455 -0.800872469 12.33191791 54.68626 1.48060 NDUFAF6 2.90617936538145e-05 0.781523317479598 0.218447620726748 NADH:ubiquinone oxidoreductase complex assembly factor 6 FUNCTION: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I) at early stages. May play a role in the biogenesis of MT-ND1. {ECO:0000269|PubMed:18614015, ECO:0000269|PubMed:22019594}.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:18614015}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.10816 0.09832 -0.161524709 41.6430762 43.71035 1.25843 NDUFAF7 1.17734908571096e-11 0.0464098987580467 0.95359010123018 NADH:ubiquinone oxidoreductase complex assembly factor 7 FUNCTION: Involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). {ECO:0000269|PubMed:20406883}.; . . . . 0.22953 0.09190 -0.356299879 29.31115829 750.13869 5.43214 NDUFB1 0.311678002538598 0.61694903260808 0.0713729648533223 NADH:ubiquinone oxidoreductase subunit B1 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;pituitary gland;testis;dura mater;brain;bladder;pineal gland;unclassifiable (Anatomical System);meninges;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;pia mater;lung;cornea;adrenal gland;macula lutea;visual apparatus;liver;alveolus;kidney;mammary gland;aorta; whole brain;thalamus;medulla oblongata;hypothalamus;temporal lobe;liver;kidney;skeletal muscle;cerebellum; 0.02658 0.04730 0.103030231 61.2762444 10.56417 0.38326 NDUFB1P1 . . . NADH:ubiquinone oxidoreductase subunit B1 pseudogene 1 . . . . . . . . . . . NDUFB1P2 . . . NADH:ubiquinone oxidoreductase subunit B1 pseudogene 2 . . . . . . . . . . . NDUFB2 0.0118150668313523 0.638823553475245 0.349361379693402 NADH:ubiquinone oxidoreductase subunit B2 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . myocardium;ovary;salivary gland;developmental;intestine;colon;vein;skin;retina;uterus;prostate;whole body;bone;thyroid;pituitary gland;testis;bladder;brain;unclassifiable (Anatomical System);trophoblast;heart;cartilage;tongue;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;visual apparatus;duodenum;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; whole brain;medulla oblongata;thalamus;occipital lobe;heart;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;globus pallidus;kidney;parietal lobe;cingulate cortex;cerebellum; 0.04878 0.09800 -0.09720619 46.20193442 27.26479 0.87884 NDUFB2-AS1 . . . NDUFB2 antisense RNA 1 . . . . . . . . . . . NDUFB2P1 . . . NADH:ubiquinone oxidoreductase subunit B2 pseudogene 2 . . . . . . . . . . . NDUFB3 0.0425652843014725 0.660300175382732 0.297134540315796 NADH:ubiquinone oxidoreductase subunit B3 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;thyroid;pituitary gland;testis;dura mater;brain;bladder;gall bladder;unclassifiable (Anatomical System);meninges;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; whole brain;amygdala;occipital lobe;thalamus;spinal cord;globus pallidus;skeletal muscle; 0.07174 . 0.21326276 67.71644256 9.41646 0.34679 NDUFB3P1 . . . NADH:ubiquinone oxidoreductase subunit B3 pseudogene 1 . . . . . . . . . . . NDUFB3P2 . . . NADH:ubiquinone oxidoreductase subunit B3 pseudogene 2 . . . . . . . . . . . NDUFB3P3 . . . NADH:ubiquinone oxidoreductase subunit B3 pseudogene 3 . . . . . . . . . . . NDUFB3P4 . . . NADH:ubiquinone oxidoreductase subunit B3 pseudogene 4 . . . . . . . . . . . NDUFB3P5 . . . NADH:ubiquinone oxidoreductase subunit B3 pseudogene 5 . . . . . . . . . . . NDUFB4 0.00226606590074798 0.762222522738923 0.235511411360329 NADH:ubiquinone oxidoreductase subunit B4 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve; whole brain;heart;adrenal gland;liver;testis;cerebellum; . 0.12941 -0.119252484 44.53880632 7.63734 0.28209 NDUFB4P1 . . . NADH:ubiquinone oxidoreductase subunit B4 pseudogene 1 . . . . . . . . . . . NDUFB4P2 . . . NADH:ubiquinone oxidoreductase subunit B4 pseudogene 2 . . . . . . . . . . . NDUFB4P3 . . . NADH:ubiquinone oxidoreductase subunit B4 pseudogene 3 . . . . . . . . . . . NDUFB4P4 . . . NADH:ubiquinone oxidoreductase subunit B4 pseudogene 4 . . . . . . . . . . . NDUFB4P5 . . . NADH:ubiquinone oxidoreductase subunit B4 pseudogene 5 . . . . . . . . . . . NDUFB4P6 . . . NADH:ubiquinone oxidoreductase subunit B4 pseudogene 6 . . . . . . . . . . . NDUFB4P7 . . . NADH:ubiquinone oxidoreductase subunit B4 pseudogene 7 . . . . . . . . . . . NDUFB4P8 . . . NADH:ubiquinone oxidoreductase subunit B4 pseudogene 8 . . . . . . . . . . . NDUFB4P9 . . . NADH:ubiquinone oxidoreductase subunit B4 pseudogene 9 . . . . . . . . . . . NDUFB4P10 . . . NADH:ubiquinone oxidoreductase subunit B4 pseudogene 10 . . . . . . . . . . . NDUFB4P11 . . . NADH:ubiquinone oxidoreductase subunit B4 pseudogene 11 . . . . . . . . . . . NDUFB4P12 . . . NADH:ubiquinone oxidoreductase subunit B4 pseudogene 12 . . . . . . . . . . . NDUFB5 0.00344108897309257 0.835086357031065 0.161472553995842 NADH:ubiquinone oxidoreductase subunit B5 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;synovium;bone;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach;aorta; whole brain;amygdala;superior cervical ganglion;medulla oblongata;temporal lobe;pons;kidney;cingulate cortex;skeletal muscle; 0.10317 0.14954 0.147123112 64.11299835 . . NDUFB5P1 . . . NADH:ubiquinone oxidoreductase subunit B5 pseudogene 1 . . . . . . . . . . . NDUFB5P2 . . . NADH:ubiquinone oxidoreductase subunit B5 pseudogene 2 . . . . . . . . . . . NDUFB6 0.0472184480336986 0.855447429444241 0.097334122522061 NADH:ubiquinone oxidoreductase subunit B6 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;bone;thyroid;pituitary gland;testis;dura mater;brain;bladder;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;heart;lacrimal gland;hypothalamus;adrenal cortex;pharynx;blood;bile duct;breast;pia mater;lung;epididymis;adrenal gland;visual apparatus;liver;duodenum;kidney; amygdala;whole brain;testis - interstitial;testis - seminiferous tubule;testis; 0.05689 0.26128 0.125076652 62.7388535 19.40679 0.66740 NDUFB7 0.0454659220811184 0.672207600541108 0.282326477377773 NADH:ubiquinone oxidoreductase subunit B7 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;pituitary gland;testis;brain;bladder;tonsil;gall bladder;unclassifiable (Anatomical System);trophoblast;heart;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; whole brain;liver;skeletal muscle;cingulate cortex; 0.38141 0.15417 -0.339715008 30.06605331 40.50571 1.18809 NDUFB8 0.350528579843796 0.636316988384963 0.013154431771241 NADH:ubiquinone oxidoreductase subunit B8 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;gum;iris;germinal center;brain;bladder;tonsil;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; amygdala;whole brain;dorsal root ganglion;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.12135 0.12730 -0.183570861 39.95046001 48.6425 1.36019 NDUFB8P1 . . . NADH:ubiquinone oxidoreductase subunit B8 pseudogene 1 . . . . . . . . . . . NDUFB8P2 . . . NADH:ubiquinone oxidoreductase subunit B8 pseudogene 2 . . . . . . . . . . . NDUFB8P3 . . . NADH:ubiquinone oxidoreductase subunit B8 pseudogene 3 . . . . . . . . . . . NDUFB9 0.0428894468164687 0.929436510196884 0.0276740429866468 NADH:ubiquinone oxidoreductase subunit B9 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . lymphoreticular;ovary;skin;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;pineal body;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;kidney;stomach;thymus; medulla oblongata;testis - interstitial;subthalamic nucleus;cerebellum peduncles;temporal lobe;testis;globus pallidus;caudate nucleus;kidney;parietal lobe;skeletal muscle;cerebellum; 0.09195 0.14651 0.25917371 70.05779665 50.03574 1.38822 NDUFB9P1 . . . NADH:ubiquinone oxidoreductase subunit B9 pseudogene 1 . . . . . . . . . . . NDUFB9P2 . . . NADH:ubiquinone oxidoreductase subunit B9 pseudogene 2 . . . . . . . . . . . NDUFB9P3 . . . NADH:ubiquinone oxidoreductase subunit B9 pseudogene 3 . . . . . . . . . . . NDUFB10 0.0466299139856533 0.854526808408879 0.0988432776054679 NADH:ubiquinone oxidoreductase subunit B10 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . myocardium;ovary;salivary gland;foreskin;intestine;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;larynx;thyroid;iris;pituitary gland;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; whole brain;heart;liver;skeletal muscle; 0.06368 0.09902 -0.471992905 23.03609342 20.73017 0.70328 NDUFB10P1 . . . NADH:ubiquinone oxidoreductase subunit B10 pseudogene 1 . . . . . . . . . . . NDUFB10P2 . . . NADH:ubiquinone oxidoreductase subunit B10 pseudogene 2 . . . . . . . . . . . NDUFB11 0.750858556039213 0.239212377137508 0.00992906682327835 NADH:ubiquinone oxidoreductase subunit B11 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;myocardium;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;nasopharynx;visual apparatus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; whole brain;heart;liver;skeletal muscle; 0.10488 0.33510 -0.053113545 49.38664779 4.9633 0.18462 NDUFB11P1 . . . NADH:ubiquinone oxidoreductase subunit B11 pseudogene 1 . . . . . . . . . . . NDUFC1 0.459572169037874 0.514205032111546 0.0262227988505809 NADH:ubiquinone oxidoreductase subunit C1 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . myocardium;smooth muscle;ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;lung;cornea;adrenal gland;hippocampus;kidney;stomach;aorta; . 0.07997 0.11700 0.057118534 57.99716914 20.04544 0.68478 NDUFC2 0.625235914208963 0.343570339761155 0.0311937460298821 NADH:ubiquinone oxidoreductase subunit C2 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;brain;bladder;heart;cartilage;nervous;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;cerebral cortex;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; whole brain;dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;skeletal muscle;skin;subthalamic nucleus;adrenal gland;liver;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;cerebellum; 0.03912 0.07026 0.125076652 62.7388535 4.63842 0.16636 NDUFC2-KCTD14 0.626507873919539 0.342602303448653 0.0308898226318076 NDUFC2-KCTD14 readthrough FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.; . . . . . . 0.325313577 73.11276244 249.3193 3.40327 NDUFS1 3.9665516500916e-09 0.932360001915056 0.067639994118392 NADH:ubiquinone oxidoreductase core subunit S1 FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized. {ECO:0000250}.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:11349233}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;heart;cartilage;pineal body;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach;thymus;cerebellum; amygdala;subthalamic nucleus;occipital lobe;globus pallidus;skeletal muscle; 0.11116 0.37016 -0.887242605 10.43288511 91.54067 2.05784 NDUFS2 0.99773539454649 0.00226460227504564 3.17846400805859e-09 NADH:ubiquinone oxidoreductase core subunit S2 FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:11220739}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.31274 0.41890 0.485092724 79.37603208 1000.4517 6.09270 NDUFS3 0.0471370341289045 0.928741937085628 0.0241210287854675 NADH:ubiquinone oxidoreductase core subunit S3 FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;skin;retina;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pineal body;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; whole brain;superior cervical ganglion;subthalamic nucleus;medulla oblongata;heart;liver;caudate nucleus;pons;cingulate cortex; 0.26971 0.36662 -0.161524709 41.6430762 27.09868 0.87476 NDUFS4 0.00416499574013875 0.862886208969689 0.132948795290173 NADH:ubiquinone oxidoreductase subunit S4 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:9463323}.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:9463323}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;umbilical cord;skin;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;trophoblast;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;kidney;aorta;stomach; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.37681 0.10800 -0.60427181 17.74593064 31.58455 0.99399 NDUFS5 0.0982173317228148 0.771219460079055 0.13056320819813 NADH:ubiquinone oxidoreductase subunit S5 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . . . 0.09713 0.10634 -0.141298762 42.87567823 25.45813 0.83125 NDUFS5P1 . . . NADH:ubiquinone oxidoreductase subunit S5 pseudogene 1 . . . . . . . . . . . NDUFS5P2 . . . NADH:ubiquinone oxidoreductase subunit S5 pseudogene 2 . . . . . . . . . . . NDUFS5P3 . . . NADH:ubiquinone oxidoreductase subunit S5 pseudogene 3 . . . . . . . . . . . NDUFS5P4 . . . NADH:ubiquinone oxidoreductase subunit S5 pseudogene 4 . . . . . . . . . . . NDUFS5P5 . . . NADH:ubiquinone oxidoreductase subunit S5 pseudogene 5 . . . . . . . . . . . NDUFS5P6 . . . NADH:ubiquinone oxidoreductase subunit S5 pseudogene 6 . . . . . . . . . . . NDUFS5P7 . . . NADH:ubiquinone oxidoreductase subunit S5 pseudogene 7 . . . . . . . . . . . NDUFS6 0.00026220073529281 0.328608653253187 0.67112914601152 NADH:ubiquinone oxidoreductase subunit S6 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;heart;hypothalamus;pineal body;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; liver;skeletal muscle; 0.05838 0.10785 -0.163345027 41.24793583 19.92703 0.67880 NDUFS6P1 . . . NADH:ubiquinone oxidoreductase subunit S6 pseudogene 1 . . . . . . . . . . . NDUFS7 0.750835828529347 0.246992094575531 0.00217207689512191 NADH:ubiquinone oxidoreductase core subunit S7 FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. {ECO:0000269|PubMed:10360771}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:10330338}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;thyroid;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;head and neck;cervix;mammary gland;stomach; thalamus;liver;skeletal muscle; 0.08650 . -0.183570861 39.95046001 1347.6338 6.88830 NDUFS8 0.0141745022672731 0.870248177993959 0.115577319738768 NADH:ubiquinone oxidoreductase core subunit S8 FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). May donate electrons to ubiquinone. {ECO:0000250}.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. {ECO:0000269|PubMed:9837812}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;medulla oblongata;ovary;salivary gland;adrenal medulla;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; heart;temporal lobe;liver;pons;kidney;skeletal muscle; 0.17284 0.25567 -0.205617011 38.57631517 13.23411 0.48113 NDUFV1 9.82538524288839e-05 0.940281859560334 0.0596198865872373 NADH:ubiquinone oxidoreductase core subunit V1 FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. {ECO:0000269|PubMed:10080174}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. {ECO:0000269|PubMed:10080174, ECO:0000269|PubMed:11349233}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;medulla oblongata;ovary;salivary gland;colon;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;dura mater;germinal center;brain;tonsil;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;skeletal muscle;pancreas;pia mater;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; whole brain;thalamus;globus pallidus;pons;skeletal muscle;parietal lobe;cingulate cortex; 0.15424 0.25968 -1.48620052 3.632932295 55.6395 1.49906 NDUFV2 0.00763022340313864 0.926145796139763 0.0662239804570987 NADH:ubiquinone oxidoreductase core subunit V2 FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.; . . myocardium;ovary;skin;retina;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;choroid;uterus;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;nasopharynx;internal ear;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; . 0.32091 0.21589 0.12689526 63.00424628 352.83558 3.97840 NDUFV2-AS1 . . . NDUFV2 antisense RNA 1 . . . . . . . . . . . NDUFV2P1 . . . NADH:ubiquinone oxidoreductase core subunit V2 pseudogene 1 . . . . . . . . . . . NDUFV3 4.32515643200341e-09 0.106542176103264 0.893457819571579 NADH:ubiquinone oxidoreductase subunit V3 FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.; . . medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;germinal center;brain;bladder;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;placenta;head and neck;kidney;stomach;aorta; . 0.03873 0.08985 0.334405942 73.64944562 649.37112 5.11367 NEAT1 . . . nuclear paraspeckle assembly transcript 1 (non-protein coding) . . . . . . . . . . . NEB 4.08103130095905e-17 1 1.10854011697251e-32 nebulin FUNCTION: This giant muscle protein may be involved in maintaining the structural integrity of sarcomeres and the membrane system associated with the myofibrils. Binds and stabilize F-actin.; . TISSUE SPECIFICITY: Muscle specific. Located in the thin filament of striated muscle.; unclassifiable (Anatomical System);heart;ovary;tongue;spinal cord;developmental;parathyroid;skeletal muscle;prostate;whole body;lung;cochlea;adrenal gland;larynx;bone;placenta;visual apparatus;alveolus;hypopharynx;liver;head and neck;mammary gland;peripheral nerve; dorsal root ganglion;superior cervical ganglion;tongue;thyroid;ciliary ganglion;atrioventricular node;trigeminal ganglion;fetal thyroid;skin;skeletal muscle; 0.14944 0.37867 0.878121232 88.90068412 21877.60222 30.87204 NEBL 5.76983793061894e-24 0.00932031573671352 0.990679684263287 nebulette FUNCTION: Binds to actin and plays an important role in the assembly of the Z-disk. Isoform 2 might play a role in the assembly of focal adhesion. {ECO:0000269|PubMed:15004028}.; . TISSUE SPECIFICITY: Abundantly expressed in cardiac muscle, but not in skeletal or smooth muscle. Localized to Z-lines in cardiac cells and to dense bodies in nonmuscle cells. Isoform 2 is expressed in non-muscle cells such as in fibroblasts.; . . 0.56868 0.10631 0.567625503 81.74687426 2561.02103 9.45167 NEBL-AS1 . . . NEBL antisense RNA 1 . . . . . . . . . . . NECAB1 0.377811814333756 0.619945079431796 0.00224310623444804 N-terminal EF-hand calcium binding protein 1 . . TISSUE SPECIFICITY: Expressed in brain (at protein level). {ECO:0000269|PubMed:12044471}.; . . 0.38409 . -0.073340031 48.11866006 21.60602 0.72658 NECAB2 . . . N-terminal EF-hand calcium binding protein 2 . . TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:12044471}.; unclassifiable (Anatomical System);trabecular meshwork;kidney;brain; amygdala;whole brain;medulla oblongata;thalamus;occipital lobe;hypothalamus;temporal lobe;pons;caudate nucleus;prefrontal cortex;liver;globus pallidus;kidney;trigeminal ganglion;parietal lobe;cingulate cortex; 0.13866 0.11297 -0.126743121 44.0905874 2833.50108 10.05093 NECAB3 0.797631144685702 0.202121581985031 0.00024727332926661 N-terminal EF-hand calcium binding protein 3 FUNCTION: Inhibits the interaction of APBA2 with beta-amyloid precursor protein (APP), and hence allows formation of beta- amyloid. {ECO:0000269|PubMed:10833507}.; . TISSUE SPECIFICITY: Strongly expressed in heart and skeletal muscle, moderately in brain and pancreas. {ECO:0000269|PubMed:10833507, ECO:0000269|PubMed:12044471}.; myocardium;ovary;colon;skin;prostate;optic nerve;frontal lobe;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;breast;lung;placenta;liver;alveolus;spleen;cervix;kidney;stomach;thymus; trigeminal ganglion;skeletal muscle; 0.20601 0.08986 . . 157.83453 2.74416 NECAP1 0.0409114385552469 0.929470668658138 0.0296178927866148 NECAP endocytosis associated 1 FUNCTION: Involved in endocytosis. {ECO:0000250}.; DISEASE: Epileptic encephalopathy, early infantile, 21 (EIEE21) [MIM:615833]: A severe disease characterized by intractable seizures, profound global developmental delay, and persistent severe axial hypotonia as well as appendicular hypertonia. {ECO:0000269|PubMed:24399846}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;thyroid;pituitary gland;testis;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;lens;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach;aorta;cerebellum; amygdala;occipital lobe;superior cervical ganglion;subthalamic nucleus;medulla oblongata;prefrontal cortex;globus pallidus;parietal lobe;cerebellum; 0.24690 . -0.095386216 46.48502005 52.81142 1.44019 NECAP1P1 . . . NECAP endocytosis associated 1 pseudogene 1 . . . . . . . . . . . NECAP1P2 . . . NECAP endocytosis associated 1 pseudogene 2 . . . . . . . . . . . NECAP2 6.86667313977443e-05 0.732062980329071 0.267868352939531 NECAP endocytosis associated 2 FUNCTION: Involved in endocytosis. {ECO:0000250}.; . . lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;testis - seminiferous tubule;placenta;testis;trigeminal ganglion; 0.19676 0.09753 0.639420866 83.8995046 38.32294 1.13730 NECTIN1 . . . nectin cell adhesion molecule 1 FUNCTION: Promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between PVRL1/nectin-1 and PVRL3/nectin-3 and between PVRL1/nectin-1 and PVRL4/nectin-4. Has some neurite outgrowth- promoting activity. {ECO:0000269|PubMed:21980294}.; DISEASE: Ectodermal dysplasia, Margarita Island type (EDMI) [MIM:225060]: An autosomal recessive form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. It is a syndrome characterized by the association of cleft lip/palate, ectodermal dysplasia (sparse short and dry scalp hair, sparse eyebrows and eyelashes), and partial syndactyly of the fingers and/or toes. Two thirds of the patients do not manifest oral cleft but present with abnormal teeth and nails. {ECO:0000269|PubMed:10932188}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Non-syndromic orofacial cleft 7 (OFC7) [MIM:225060]: A birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum. {ECO:0000269|PubMed:10932188}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.16543 0.24625 -0.238793231 36.3116301 . . NECTIN2 . . . nectin cell adhesion molecule 2 FUNCTION: Probable cell adhesion protein. {ECO:0000269|PubMed:9657005}.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.11419 0.17465 0.556689353 81.63481953 . . NECTIN3 . . . nectin cell adhesion molecule 3 FUNCTION: Plays a role in cell-cell adhesion through heterophilic trans-interactions with nectin-like proteins or nectins, such as trans-interaction with PVRL2/nectin-2 at Sertoli-spermatid junctions. Trans-interaction with PVR induces activation of CDC42 and RAC small G proteins through common signaling molecules such as SRC and RAP1. Also involved in the formation of cell-cell junctions, including adherens junctions and synapses. Induces endocytosis-mediated down-regulation of PVR from the cell surface, resulting in reduction of cell movement and proliferation. Plays a role in the morphology of the ciliary body. {ECO:0000269|PubMed:16216929}.; . TISSUE SPECIFICITY: Predominantly expressed in testis and placenta as well as in many cell lines, including epithelial cell lines. {ECO:0000269|PubMed:11024295}.; . . 0.54577 0.18610 0.018483465 55.44939844 . . NECTIN4 . . . nectin cell adhesion molecule 4 FUNCTION: Seems to be involved in cell adhesion through trans- homophilic and -heterophilic interactions, the latter including specifically interactions with PVRL2/nectin-1. Does not act as receptor for alpha-herpesvirus entry into cells.; DISEASE: Ectodermal dysplasia-syndactyly syndrome 1 (EDSS1) [MIM:613573]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. EDSS1 is characterized by the association of hair and teeth abnormalities with cutaneous syndactyly of the hands and/or feet. Hair morphologic abnormalities include twists at irregular intervals (pilli torti) and swelling along the shafts, particularly associated with areas of breakage. Dental findings consist of abnormally widely spaced teeth, with peg- shaped and conical crowns. Patients have normal sweating. {ECO:0000269|PubMed:20691405}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in placenta. Not detected in normal breast epithelium but expressed in breast carcinoma. {ECO:0000269|PubMed:11544254, ECO:0000269|PubMed:17474988}.; . . 0.15294 0.12598 -0.334253673 30.70299599 . . NEDD1 0.221564198564528 0.778366195035982 6.96063994907171e-05 neural precursor cell expressed, developmentally down-regulated 1 FUNCTION: Required for mitosis progression. Promotes the nucleation of microtubules from the spindle. {ECO:0000269|PubMed:19029337, ECO:0000269|PubMed:19509060}.; . . medulla oblongata;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;larynx;testis;germinal center;bladder;gall bladder;unclassifiable (Anatomical System);heart;urinary;blood;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion; 0.22134 0.12157 -0.556537043 19.72753008 73.47165 1.79155 NEDD4 6.44185120812023e-09 0.999932973487047 6.70200711017922e-05 neural precursor cell expressed, developmentally down-regulated 4, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Specifically ubiquitinates 'Lys-63' in target proteins (PubMed:23644597). Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes. Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes. Promotes ubiquitination of RAPGEF2. According to PubMed:18562292 the direct link between NEDD4 and PTEN regulation through polyubiquitination described in PubMed:17218260 is questionable. Involved in ubiquitination of ERBB4 intracellular domain E4ICD. Involved in the budding of many viruses. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. Ubiquitinates TNK2 and regulates EGF-induced degradation of EGFR and TNF2. Involved in the ubiquitination of ebola virus VP40 protein and this ubiquitination plays a role in facilitating viral budding. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046). {ECO:0000269|PubMed:11598133, ECO:0000269|PubMed:17218260, ECO:0000269|PubMed:18305167, ECO:0000269|PubMed:18562292, ECO:0000269|PubMed:20086093, ECO:0000269|PubMed:21399620, ECO:0000269|PubMed:21765395, ECO:0000269|PubMed:23644597, ECO:0000269|PubMed:25631046}.; . . myocardium;smooth muscle;ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;optic nerve;whole body;bone;testis;spinal ganglion;brain;artery;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;spinal cord;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.30475 0.21064 0.301240539 71.70912951 1901.14136 8.01788 NEDD4L 0.999966646256687 3.33537432909956e-05 2.21232522043548e-14 neural precursor cell expressed, developmentally down-regulated 4-like, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Inhibits TGF-beta signaling by triggering SMAD2 and TGFBR1 ubiquitination and proteasome-dependent degradation. Promotes ubiquitination and internalization of various plasma membrane channels such as ENaC, Nav1.2, Nav1.3, Nav1.5, Nav1.7, Nav1.8, Kv1.3, EAAT1 or CLC5. Promotes ubiquitination and degradation of SGK1 and TNK2. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000250|UniProtKB:Q8CFI0, ECO:0000269|PubMed:12911626, ECO:0000269|PubMed:15040001, ECO:0000269|PubMed:15217910, ECO:0000269|PubMed:15489223, ECO:0000269|PubMed:15496141, ECO:0000269|PubMed:15576372, ECO:0000269|PubMed:19144635, ECO:0000269|PubMed:23999003, ECO:0000269|PubMed:25631046}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in prostate, pancreas and kidney (PubMed:14615060, PubMed:15496141, PubMed:19664597). Expressed in melanocytes (PubMed:23999003). {ECO:0000269|PubMed:14615060, ECO:0000269|PubMed:15496141, ECO:0000269|PubMed:19664597, ECO:0000269|PubMed:23999003}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;epididymis;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; occipital lobe;superior cervical ganglion;medulla oblongata;subthalamic nucleus;fetal brain;cerebellum peduncles;prefrontal cortex;globus pallidus;caudate nucleus;pons;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.46900 0.25588 -1.197736472 5.785562633 42.02222 1.22415 NEDD8 0.429440681272929 0.538251115365261 0.0323082033618102 neural precursor cell expressed, developmentally down-regulated 8 FUNCTION: Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C- APPBP1 and linkage to the E2 enzyme UBE2M. Attachment of NEDD8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins. {ECO:0000269|PubMed:10318914, ECO:0000269|PubMed:10597293, ECO:0000269|PubMed:11953428}.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, spleen, thymus, prostate, testis, ovary, colon and leukocytes. {ECO:0000269|PubMed:10597293, ECO:0000269|PubMed:9353319}.; myocardium;lymphoreticular;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;placenta;kidney;stomach;aorta;thymus; subthalamic nucleus;occipital lobe;thalamus;smooth muscle;hypothalamus;temporal lobe;globus pallidus;cingulate cortex; 0.55729 0.17050 0.101211609 60.95777306 . . NEDD8-MDP1 . . . NEDD8-MDP1 readthrough . . . . . . . . . 1.20885 0.03747 NEDD9 0.534981125014028 0.464991213449718 2.7661536253666e-05 neural precursor cell expressed, developmentally down-regulated 9 FUNCTION: Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. May function in transmitting growth control signals between focal adhesions at the cell periphery and the mitotic spindle in response to adhesion or growth factor signals initiating cell proliferation. May play an important role in integrin beta-1 or B cell antigen receptor (BCR) mediated signaling in B- and T-cells. Integrin beta-1 stimulation leads to recruitment of various proteins including CRK, NCK and SHPTP2 to the tyrosine phosphorylated form.; . TISSUE SPECIFICITY: Widely expressed. Higher levels detected in kidney, lung, and placenta. Also detected in T-cells, B-cells and diverse cell lines. The protein has been detected in lymphocytes, in diverse cell lines, and in lung tissues.; . . 0.38853 0.23740 -0.371072278 28.22009908 279.64751 3.58344 NEFH 0.00126104058830359 0.959545068001346 0.03919389141035 neurofilament, heavy polypeptide FUNCTION: Neurofilaments usually contain three intermediate filament proteins: L, M, and H which are involved in the maintenance of neuronal caliber. NF-H has an important function in mature axons that is not subserved by the two smaller NF proteins.; DISEASE: Amyotrophic lateral sclerosis (ALS) [MIM:105400]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. {ECO:0000269|PubMed:7849698}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;pineal body;sympathetic chain;substantia nigra;fovea centralis;choroid;skeletal muscle;skin;retina;uterus;prostate;lung;macula lutea;visual apparatus;hippocampus;testis;kidney;mammary gland;brain;cerebellum; whole brain;amygdala;dorsal root ganglion;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;subthalamic nucleus;prostate;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.18142 0.21216 0.246221394 69.56829441 2276.00942 8.82068 NEFHP1 . . . neurofilament, heavy polypeptide pseudogene 1 . . . . . . . . . . . NEFL . . . neurofilament, light polypeptide FUNCTION: Neurofilaments usually contain three intermediate filament proteins: L, M, and H which are involved in the maintenance of neuronal caliber.; DISEASE: Charcot-Marie-Tooth disease 1F (CMT1F) [MIM:607734]: A dominant demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot- Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. CMT1F is characterized by onset in infancy or childhood (range 1 to 13 years). {ECO:0000269|PubMed:12566280, ECO:0000269|PubMed:14733962, ECO:0000269|PubMed:15241803}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease 2E (CMT2E) [MIM:607684]: A dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. {ECO:0000269|PubMed:10841809, ECO:0000269|PubMed:11220745, ECO:0000269|PubMed:12481988, ECO:0000269|PubMed:15241803, ECO:0000269|PubMed:22206013}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;thyroid;testis;bladder;brain;unclassifiable (Anatomical System);amygdala;hypothalamus;pharynx;blood;breast;pancreas;lung;macula lutea;visual apparatus;liver;kidney;stomach; dorsal root ganglion;whole brain;amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.69753 0.65776 . . . . NEFLP1 . . . neurofilament, light polypeptide pseudogene 1 . . . . . . . . . . . NEFM 0.0359563283297322 0.956312095459574 0.00773157621069373 neurofilament, medium polypeptide FUNCTION: Neurofilaments usually contain three intermediate filament proteins: L, M, and H which are involved in the maintenance of neuronal caliber.; . . ovary;salivary gland;sympathetic chain;intestine;colon;substantia nigra;fovea centralis;choroid;skin;retina;prostate;optic nerve;frontal lobe;cochlea;testis;bladder;pineal gland;brain;unclassifiable (Anatomical System);amygdala;islets of Langerhans;spinal cord;pharynx;blood;lens;breast;lung;macula lutea;visual apparatus;liver;kidney; whole brain;amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.53048 0.35105 0.248041348 69.61547535 137.04623 2.54576 NEFMP1 . . . neurofilament, medium polypeptide pseudogene 1 . . . . . . . . . . . NEGR1 0.951349394977358 0.048621097749997 2.95072726448686e-05 neuronal growth regulator 1 FUNCTION: May be involved in cell-adhesion. May function as a trans-neural growth-promoting factor in regenerative axon sprouting in the mammalian brain (By similarity). {ECO:0000250}.; . . ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;bone;testis;artery;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;tongue;islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;head and neck;kidney;aorta; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle;skin; 0.12675 0.13596 -0.26993514 34.59542345 118.1789 2.36405 NEGR1-IT1 . . . NEGR1 intronic transcript 1 . . . . . . . . . . . NEIL1 0.000108858344700828 0.947466900141098 0.0524242415142007 nei like DNA glycosylase 1 FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 8- oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches. Specifically binds 5- hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC. {ECO:0000269|PubMed:11904416, ECO:0000269|PubMed:12200441, ECO:0000269|PubMed:12509226, ECO:0000269|PubMed:14522990}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11904416}.; colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;islets of Langerhans;adrenal cortex;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; superior cervical ganglion; 0.14249 0.18443 0.797386419 87.53833451 155.96943 2.72915 NEIL2 2.11099583099423e-09 0.0373523962526455 0.962647601636359 nei like DNA glycosylase 2 FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double-stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. {ECO:0000269|PubMed:12097317, ECO:0000269|PubMed:14522990, ECO:0000269|PubMed:15175427, ECO:0000269|PubMed:15339932}.; . TISSUE SPECIFICITY: Detected in testis, skeletal muscle, heart, brain, placenta, lung, pancreas, kidney and liver. {ECO:0000269|PubMed:12097317}.; colon;fovea centralis;skin;bone marrow;uterus;prostate;optic nerve;larynx;thyroid;bone;iris;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney; . 0.05320 0.07746 0.134171522 63.57041755 323.01045 3.81875 NEIL3 3.54834979186504e-07 0.556963408731072 0.443036236433949 nei like DNA glycosylase 3 FUNCTION: DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA). In vitro, displays strong glycosylase activity towards the hydantoin lesions spiroiminodihydantoin (Sp) and guanidinohydantoin (Gh) in both ssDNA and dsDNA; also recognizes FapyA, FapyG, 5-OHU, 5-OHC, 5- OHMH, Tg and 8-oxoA lesions in ssDNA. No activity on 8-oxoG detected. Also shows weak DNA-(apurinic or apyrimidinic site) lyase activity. In vivo, appears to be the primary enzyme involved in removing Sp and Gh from ssDNA in neonatal tissues. Seems to be an important facilitator of cell proliferation in certain populations, for example neural stem/progenitor cells and tumor cells, suggesting a role in replication-associated DNA repair. {ECO:0000269|PubMed:12433996, ECO:0000269|PubMed:19170771, ECO:0000269|PubMed:22569481, ECO:0000269|PubMed:23755964}.; . TISSUE SPECIFICITY: Expressed in keratinocytes and embryonic fibroblasts (at protein level). Also detected in thymus, testis and fetal lung primary fibroblasts. {ECO:0000269|PubMed:12433996, ECO:0000269|PubMed:16428305, ECO:0000269|PubMed:19426544, ECO:0000269|PubMed:22365498}.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;uterus;pancreas;lung;cornea;bone;visual apparatus;liver;testis;spleen;germinal center;kidney;brain;mammary gland;tonsil; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.04798 0.07588 2.157029472 98.01250295 2050.68609 8.34807 NEK1 4.21851213590427e-12 0.995853220529245 0.0041467794665363 NIMA related kinase 1 FUNCTION: Phosphorylates serines and threonines, but also appears to possess tyrosine kinase activity. Implicated in the control of meiosis (By similarity). Involved in cilium assembly. In response to injury that includes DNA damage, NEK1 phosphorylates VDAC1 to limit mitochondrial cell death. {ECO:0000250, ECO:0000269|PubMed:20230784, ECO:0000269|PubMed:21211617}.; . TISSUE SPECIFICITY: High fetal expression in the brain and kidney. {ECO:0000269|PubMed:21211617}.; . . 0.59582 0.09298 -0.08265057 47.20452937 1485.56231 7.17409 NEK2 8.72367756771365e-07 0.917003430300363 0.0829956973318805 NIMA related kinase 2 FUNCTION: Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGOL1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates CEP68 and CNTLN directly or indirectly (PubMed:24554434). NEK2-mediated phosphorylation of CEP68 promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis (PubMed:25704143). Involved in the regulation of centrosome disjunction (PubMed:26220856). {ECO:0000269|PubMed:11742531, ECO:0000269|PubMed:12857871, ECO:0000269|PubMed:14978040, ECO:0000269|PubMed:15358203, ECO:0000269|PubMed:15388344, ECO:0000269|PubMed:17283141, ECO:0000269|PubMed:17621308, ECO:0000269|PubMed:17626005, ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:18297113, ECO:0000269|PubMed:20034488, ECO:0000269|PubMed:21076410, ECO:0000269|PubMed:24554434, ECO:0000269|PubMed:25704143, ECO:0000269|PubMed:26220856}.; FUNCTION: Isoform 2: Not present in the nucleolus and, in contrast to isoform 1, does not phosphorylate and activate NEK11 in G1/S- arrested cells. {ECO:0000269|PubMed:15161910}.; DISEASE: Retinitis pigmentosa 67 (RP67) [MIM:615565]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:24043777}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in peripheral blood T-cells and a wide variety of transformed cell types. Isoform 1 and isoform 4 are expressed in the testis. Up- regulated in various cancer cell lines, as well as primary breast tumors. {ECO:0000269|PubMed:11742531, ECO:0000269|PubMed:15659832}.; . . 0.85196 0.20525 -0.314027422 31.9297004 1335.03725 6.86235 NEK2P1 . . . NEK2 pseudogene 1 . . . . . . . . . . . NEK2P2 . . . NEK2 pseudogene 2 . . . . . . . . . . . NEK2P3 . . . NEK2 pseudogene 3 . . . . . . . . . . . NEK2P4 . . . NEK2 pseudogene 4 . . . . . . . . . . . NEK3 5.05530998545056e-10 0.2050211419488 0.794978857545669 NIMA related kinase 3 FUNCTION: Protein kinase which influences neuronal morphogenesis and polarity through effects on microtubules. Regulates microtubule acetylation in neurons. Contributes to prolactin- mediated phosphorylation of PXN and VAV2. Implicated in prolactin- mediated cytoskeletal reorganization and motility of breast cancer cells through mechanisms involving RAC1 activation and phosphorylation of PXN and VAV2. {ECO:0000269|PubMed:15618286, ECO:0000269|PubMed:17297458}.; . TISSUE SPECIFICITY: Up-regulated in malignant versus normal breast tissue. Isoform 2 shows a high level of expression in testis, ovary and brain. {ECO:0000269|PubMed:12063396, ECO:0000269|PubMed:17297458}.; ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;pharynx;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach; medulla oblongata;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11626 0.08877 0.198490371 67.30360934 4105.4212 12.71378 NEK4 1.21649867284356e-12 0.723083982574176 0.276916017424607 NIMA related kinase 4 FUNCTION: Protein kinase that seems to act exclusively upon threonine residues (By similarity). Required for normal entry into proliferative arrest after a limited number of cell divisions, also called replicative senescence. Required for normal cell cycle arrest in response to double-stranded DNA damage. {ECO:0000250|UniProtKB:Q9Z1J2, ECO:0000269|PubMed:22851694}.; . TISSUE SPECIFICITY: Highest expression in adult heart, followed by pancreas, skeletal muscle, brain, testis, retina, liver, kidney, lung and placenta. Present in most primary carcinomas. {ECO:0000269|PubMed:21685204, ECO:0000269|PubMed:8208544}.; unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;retina;bile duct;breast;optic nerve;lung;larynx;placenta;macula lutea;visual apparatus;hippocampus;liver;testis;head and neck;spleen;mammary gland;brain; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.50058 0.07388 -0.354480518 29.42911064 2610.91537 9.56871 NEK4P1 . . . NIMA-related kinase 4 pseudogene 1 . . . . . . . . . . . NEK4P2 . . . NIMA-related kinase 4 pseudogene 2 . . . . . . . . . . . NEK4P3 . . . NIMA-related kinase 4 pseudogene 3 . . . . . . . . . . . NEK5 5.03282784249709e-20 0.00278424950867335 0.997215750491327 NIMA related kinase 5 . . . unclassifiable (Anatomical System);nasopharynx; . 0.09009 . 1.067416815 91.66666667 1028.78233 6.16280 NEK6 0.644137660973949 0.355593089530199 0.000269249495851818 NIMA related kinase 6 FUNCTION: Protein kinase which plays an important role in mitotic cell cycle progression. Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, RPS6KB1, TRIP4, STAT3 and histones H1 and H3. Phosphorylates KIF11 to promote mitotic spindle formation. Involved in G2/M phase cell cycle arrest induced by DNA damage. Inhibition of activity results in apoptosis. May contribute to tumorigenesis by suppressing p53/TP53-induced cancer cell senescence. {ECO:0000269|PubMed:12054534, ECO:0000269|PubMed:14563848, ECO:0000269|PubMed:18728393, ECO:0000269|PubMed:19001501, ECO:0000269|PubMed:19414596, ECO:0000269|PubMed:20407017, ECO:0000269|PubMed:20873783, ECO:0000269|PubMed:21099361}.; . TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart and skeletal muscle. Up-regulated in a variety of malignant cancers, such as breast, colon, lung, and gastric cancers. {ECO:0000269|PubMed:12054534, ECO:0000269|PubMed:20407017}.; lymphoreticular;ovary;salivary gland;intestine;colon;vein;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;spinal cord;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;visual apparatus;alveolus;liver;cervix;spleen;kidney;mammary gland;stomach;peripheral nerve; . 0.12306 0.11384 -0.359940251 28.93371078 287.30993 3.63133 NEK7 0.707657760923798 0.292196429696946 0.000145809379256424 NIMA related kinase 7 FUNCTION: Protein kinase which plays an important role in mitotic cell cycle progression. Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis. Phosphorylates RPS6KB1. {ECO:0000269|PubMed:17101132, ECO:0000269|PubMed:17586473, ECO:0000269|PubMed:19414596}.; . TISSUE SPECIFICITY: Highly expressed in lung, muscle, testis, brain, heart, liver, leukocyte and spleen. Lower expression in ovary, prostate and kidney. No expression seen in small intestine. {ECO:0000269|PubMed:11701951}.; . . 0.24935 0.11215 -0.029247611 51.40363293 55.39612 1.49342 NEK8 1.56481397745759e-06 0.991225969616824 0.00877246556919812 NIMA related kinase 8 FUNCTION: Required for renal tubular integrity. May regulate local cytoskeletal structure in kidney tubule epithelial cells. May regulate ciliary biogenesis through targeting of proteins to the cilia (By similarity). Plays a role in organogenesis and is involved in the regulation of the Hippo signaling pathway. {ECO:0000250, ECO:0000269|PubMed:23418306}.; DISEASE: Renal-hepatic-pancreatic dysplasia 2 (RHPD2) [MIM:615415]: A form of renal-hepatic-pancreatic dysplasia, a disease characterized by cystic malformations of the kidneys, liver, and pancreas. The pathological findings consist of multicystic dysplastic kidneys, dilated and dysgenetic bile ducts, a dysplastic pancreas with dilated ducts, cysts, fibrosis and inflammatory infiltrates. {ECO:0000269|PubMed:23418306}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest expression in thyroid, adrenal gland and skin. Low levels in spleen, colon and uterus. Overexpressed in breast tumors, with highest expression in infiltrating ductal carcinomas and moderate levels in mucinous adenocarcinoma. {ECO:0000269|PubMed:15019993}.; lymph node;ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;pancreas;lung;bone;liver;kidney;brain;bladder;tonsil; . 0.28199 0.10688 -1.241834664 5.414012739 57.54525 1.53085 NEK9 1.19201671010644e-06 0.999889087482619 0.000109720500670704 NIMA related kinase 9 FUNCTION: Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2. Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues. Important for G1/S transition and S phase progression. Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively. {ECO:0000269|PubMed:12840024, ECO:0000269|PubMed:14660563, ECO:0000269|PubMed:19941817}.; . TISSUE SPECIFICITY: Most abundant in heart, liver, kidney and testis. Also expressed in smooth muscle cells and fibroblasts.; myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;pineal body;blood;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; testis - interstitial;testis - seminiferous tubule;trigeminal ganglion; 0.44488 0.31694 -0.416983034 25.82566643 437.85332 4.36229 NEK10 0.000236569051864242 0.998962324925598 0.000801106022537347 NIMA related kinase 10 . . . unclassifiable (Anatomical System);testis;kidney;mammary gland;brain; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.11051 0.08242 0.887394731 89.18966737 2811.17729 10.00845 NEK11 3.82253260833349e-17 0.010043176894889 0.989956823105111 NIMA related kinase 11 FUNCTION: Protein kinase which plays an important role in the G2/M checkpoint response to DNA damage. Controls degradation of CDC25A by directly phosphorylating it on residues whose phosphorylation is required for BTRC-mediated polyubiquitination and degradation. {ECO:0000269|PubMed:12154088, ECO:0000269|PubMed:19734889, ECO:0000269|PubMed:20090422}.; . TISSUE SPECIFICITY: Poorly expressed in cerebellum, trachea, lung, appendix, and uterus. {ECO:0000269|PubMed:12154088}.; unclassifiable (Anatomical System);uterus;heart;endometrium;nasopharynx;visual apparatus;liver;spleen;brain;skin; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08876 0.09037 0.470324112 78.82755367 3204.70892 10.79137 NELFA 0.166888720234175 0.830123964586294 0.00298731517953144 negative elongation factor complex member A FUNCTION: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. Probably required to interact with the RNA polymerase II complex. {ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:12563561, ECO:0000269|PubMed:12612062}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in heart, brain, placenta, liver, skeletal muscle, kidney and pancreas. Expressed at lower level in adult lung. Expressed in fetal brain, lung, liver and kidney. {ECO:0000269|PubMed:10409432, ECO:0000269|PubMed:11150502, ECO:0000269|PubMed:12612062}.; . . 0.16002 0.14644 -1.107723888 6.829440906 94.08279 2.08611 NELFB 0.748854269451641 0.25105284322434 9.28873240188253e-05 negative elongation factor complex member B FUNCTION: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. May be able to induce chromatin unfolding. {ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:12612062}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, lung, placenta, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:12612062}.; . . 0.13224 0.27504 -1.353899809 4.558858221 55.98028 1.50283 NELFCD 0.205977810131081 0.793941076278776 8.11135901437602e-05 negative elongation factor complex member C/D FUNCTION: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. {ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:12612062}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, lung, placenta, liver, skeletal and cardiac muscle, adrenal, thyroid, kidney and pancreas. {ECO:0000269|PubMed:11030415, ECO:0000269|PubMed:12612062}.; . . 0.20699 0.42266 -1.199555187 5.761972163 20.6141 0.70093 NELFE 0.756273167199129 0.24372334423072 3.48857015135704e-06 negative elongation factor complex member E FUNCTION: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. {ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:11940650, ECO:0000269|PubMed:12612062}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, lung, placenta, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:12612062}.; . . 0.49740 0.10878 -0.005381972 53.50908233 167.20906 2.82554 NELL1 2.16981597021605e-09 0.992335059980809 0.00766493784937517 neural EGFL like 1 FUNCTION: Plays a role in the control of cell growth and differentiation. Promotes osteoblast cell differentiation and terminal mineralization. {ECO:0000269|PubMed:21723284}.; . . unclassifiable (Anatomical System);ovary;blood;parathyroid;skeletal muscle;prostate;lung;frontal lobe;placenta;bone;alveolus;testis;kidney;brain; amygdala;whole brain;superior cervical ganglion;subthalamic nucleus;temporal lobe;cingulate cortex; 0.16311 0.14813 0.207589927 67.52182118 890.70295 5.81461 NELL2 0.999853571748522 0.000146428250665758 8.12627537843588e-13 neural EGFL like 2 FUNCTION: Required for neuron survival through the modulation of MAPK pathways (By similarity). Involved in the regulation of hypothalamic GNRH secretion and the control of puberty (By similarity). {ECO:0000250|UniProtKB:Q62918}.; . . lymphoreticular;sympathetic chain;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;bone;pituitary gland;testis;dura mater;pineal gland;brain;unclassifiable (Anatomical System);amygdala;meninges;heart;cerebellum cortex;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pia mater;lung;trabecular meshwork;macula lutea;visual apparatus;hippocampus;duodenum;hypopharynx;head and neck;cerebellum; whole brain;amygdala;occipital lobe;medulla oblongata;subthalamic nucleus;fetal brain;temporal lobe;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.35773 0.13434 -0.615405356 17.47464025 320.18616 3.80220 NEMF 0.981706446227217 0.0182935537713002 1.48282376568502e-12 nuclear export mediator factor FUNCTION: Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. NEMF is responsible for selective recognition of stalled 60S subunits by recognizing an exposed, nascent chain-conjugated tRNA moiety. NEMF is important for the stable association of LTN1 to the complex (PubMed:25578875). May indirectly play a role in nuclear export (PubMed:16103875). {ECO:0000269|PubMed:16103875, ECO:0000269|PubMed:25578875}.; . TISSUE SPECIFICITY: Expressed in brain, heart, liver, lung, spleen, and skeletal muscle. Also expressed at lower levels in stomach and testis. {ECO:0000269|PubMed:16103875}.; smooth muscle;ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;cochlea;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;spinal cord;blood;lens;skeletal muscle;bile duct;breast;lung;trabecular meshwork;placenta;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; amygdala;superior cervical ganglion;prefrontal cortex;globus pallidus; 0.95132 . -1.703090605 2.535975466 82.89587 1.93339 NEMP1 . . . nuclear envelope integral membrane protein 1 . . . . . 0.27183 . 0.837848571 88.22835574 . . NEMP2 . . . nuclear envelope integral membrane protein 2 . . . . . . . 0.21326276 67.71644256 . . NENF 0.00299100360136081 0.585701217096877 0.411307779301763 neudesin neurotrophic factor FUNCTION: Acts as a neurotrophic factor in postnatal mature neurons enhancing neuronal survival. Promotes cell proliferation and neurogenesis in undifferentiated neural pro-genitor cells at the embryonic stage and inhibits differentiation of astrocyte. Its neurotrophic activity is exerted via MAPK1/ERK2, MAPK3/ERK1 and AKT1/AKT pathways. Neurotrophic activity is enhanced by binding to heme. Acts also as an anorexigenic neurotrophic factor that contributes to energy balance (By similarity). Plays a role in the human tumorigenesis (PubMed:22748190). {ECO:0000250|UniProtKB:Q9CQ45, ECO:0000269|PubMed:22748190}.; . TISSUE SPECIFICITY: Ubiquitously expressed with high expression in heart. Over-expressed in various tumors including carcinomas of the uterine cervix, lymphoma, colon, lung, skin and leukemia, as well as carcinoma of the breast. {ECO:0000269|PubMed:22748190}.; . . 0.13631 0.11882 . . 26.72337 0.86472 NENFP1 . . . neudesin neurotrophic factor pseudogene 1 . . . . . . . . . . . NENFP2 . . . neudesin neurotrophic factor pseudogene 2 . . . . . . . . . . . NENFP3 . . . neudesin neurotrophic factor pseudogene 3 . . . . . . . . . . . NEO1 0.99985462014738 0.000145379852618776 1.33861214617782e-15 neogenin 1 FUNCTION: Multi-functional cell surface receptor regulating cell adhesion in many diverse developmental processes, including neural tube and mammary gland formation, myogenesis and angiogenesis. Receptor for members of the BMP, netrin, and repulsive guidance molecule (RGM) families. Netrin-Neogenin interactions result in a chemoattractive axon guidance response and cell-cell adhesion, the interaction between NEO1/Neogenin and RGMa and RGMb induces a chemorepulsive response. {ECO:0000269|PubMed:21149453}.; . TISSUE SPECIFICITY: Widely expressed and also in cancer cell lines.; lymphoreticular;ovary;developmental;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;cochlea;cerebral cortex;larynx;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;peripheral nerve; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.26252 0.18028 -1.300731691 4.948100967 235.79115 3.31758 NEPNP . . . nephrocan, pseudogene . . . . . . . . . . . NES 2.06955630735523e-05 0.998895316480858 0.00108398795606821 nestin FUNCTION: Required for brain and eye development. Promotes the disassembly of phosphorylated vimentin intermediate filaments (IF) during mitosis and may play a role in the trafficking and distribution of IF proteins and other cellular factors to daughter cells during progenitor cell division. Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: CNS stem cells.; unclassifiable (Anatomical System);heart;ovary;muscle;colon;skin;skeletal muscle;retina;uterus;whole body;lung;endometrium;epididymis;placenta;testis;kidney;brain;mammary gland;aorta; dorsal root ganglion;superior cervical ganglion;olfactory bulb; 0.07538 0.65053 0.968131324 90.20405756 854.26648 5.70752 NET1 0.0668541946676421 0.933023449480261 0.000122355852097007 neuroepithelial cell transforming 1 FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase. May be involved in activation of the SAPK/JNK pathway Stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death. {ECO:0000269|PubMed:21373644}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8649828}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;cerebellum cortex;tongue;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;placenta; 0.27641 0.08443 -0.554717505 19.79830149 228.80755 3.26782 NETO1 0.949402709104517 0.0505959558163628 1.33507912073101e-06 neuropilin and tolloid like 1 FUNCTION: Involved in the development and/or maintenance of neuronal circuitry. Accessory subunit of the neuronal N-methyl-D- aspartate receptor (NMDAR) critical for maintaining the abundance of GRIN2A-containing NMDARs in the postsynaptic density. Regulates long-term NMDA receptor-dependent synaptic plasticity and cognition, at least in the context of spatial learning and memory (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are retina-specific. Isoform 3 is found in retina as well as at lower levels in adult and fetal brain. {ECO:0000269|PubMed:11943477}.; unclassifiable (Anatomical System);prostate;frontal lobe;hippocampus;brain;bladder;skin;retina; . 0.30139 0.39279 0.753291803 86.71266808 261.68297 3.47187 NETO2 0.158399551223246 0.841464187690664 0.000136261086090096 neuropilin and tolloid like 2 FUNCTION: Accessory subunit of neuronal kainate-sensitive glutamate receptors, GRIK2 and GRIK3. Increases kainate-receptor channel activity, slowing the decay kinetics of the receptors, without affecting their expression at the cell surface, and increasing the open probability of the receptor channels. Modulates the agonist sensitivity of kainate receptors. Slows the decay of kainate receptor-mediated excitatory postsynaptic currents (EPSCs), thus directly influencing synaptic transmission (By similarity). {ECO:0000250}.; . . parathyroid;fovea centralis;choroid;skin;retina;bone marrow;optic nerve;frontal lobe;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;adrenal cortex;blood;lens;bile duct;pancreas;lung;adrenal gland;macula lutea;hippocampus;liver;hypopharynx;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;fetal brain;ciliary ganglion;atrioventricular node;caudate nucleus;skeletal muscle; 0.17156 0.11389 -0.404032746 26.53338051 133.98421 2.51752 NEU1 1.93153899716433e-05 0.89070620188867 0.109274482721358 neuraminidase 1 (lysosomal sialidase) FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage. {ECO:0000269|PubMed:8985184}.; DISEASE: Sialidosis (SIALIDOSIS) [MIM:256550]: Lysosomal storage disease occurring as two types with various manifestations. Type 1 sialidosis (cherry red spot-myoclonus syndrome or normosomatic type) is late-onset and it is characterized by the formation of cherry red macular spots in childhood, progressive debilitating myoclonus, insiduous visual loss and rarely ataxia. The diagnosis can be confirmed by the screening of the urine for sialyloligosaccharides. Type 2 sialidosis (also known as dysmorphic type) occurs as several variants of increasing severity with earlier age of onset. It is characterized by the presence of abnormal somatic features including coarse facies and dysostosis multiplex, vertebral deformities, mental retardation, cherry-red spot/myoclonus, sialuria, cytoplasmic vacuolation of peripheral lymphocytes, bone marrow cells and conjunctival epithelial cells. {ECO:0000269|PubMed:10944856, ECO:0000269|PubMed:11063730, ECO:0000269|PubMed:11279074, ECO:0000269|PubMed:11829139, ECO:0000269|PubMed:14695530, ECO:0000269|PubMed:8985184, ECO:0000269|PubMed:9054950}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in pancreas, followed by skeletal muscle, kidney, placenta, heart, lung and liver. Weakly expressed in brain. {ECO:0000269|PubMed:8985184, ECO:0000269|PubMed:9054950}.; . . 0.17199 . -0.227663163 37.11370606 212.23656 3.14196 NEU2 3.08678522547744e-12 0.00577545902272974 0.994224540974183 neuraminidase 2 (cytosolic sialidase) FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins, oligosaccharides and gangliosides. {ECO:0000269|PubMed:14613940, ECO:0000269|PubMed:22228546}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, fetal liver and embryonic carcinoma cell line NT2-D1. {ECO:0000269|PubMed:10191093}.; . . 0.13477 0.35490 0.132352165 63.48785091 508.10281 4.62278 NEU3 1.64057530076216e-06 0.239599960772303 0.760398398652396 neuraminidase 3 (membrane sialidase) FUNCTION: Plays a role in modulating the ganglioside content of the lipid bilayer at the level of membrane-bound sialyl glycoconjugates. {ECO:0000269|PubMed:10861246, ECO:0000269|PubMed:20511247}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle, testis, adrenal gland and thymus, followed by pancreas, liver, heart and thymus. Weakly expressed in kidney, placenta, brain and lung. {ECO:0000269|PubMed:10861246}.; unclassifiable (Anatomical System);endometrium;germinal center;mammary gland;bone marrow; dorsal root ganglion;superior cervical ganglion;atrioventricular node;kidney;skeletal muscle;cingulate cortex; 0.30742 0.30362 -0.134019284 43.90776126 322.31299 3.81180 NEU4 0.00027758289159766 0.553721055993974 0.446001361114428 neuraminidase 4 (sialidase) FUNCTION: May function in lysosomal catabolism of sialylated glycoconjugates. Has sialidase activity towards synthetic substrates, such as 2'-(4-methylumbelliferyl)-alpha-D-N- acetylneuraminic acid (4-MU-NANA or 4MU-NeuAc). Has a broad substrate specificity being active on glycoproteins, oligosaccharides and sialylated glycolipids. {ECO:0000269|PubMed:14962670, ECO:0000269|PubMed:15213228}.; . TISSUE SPECIFICITY: Ubiquitous with higher expression in heart, skeletal muscle, liver and placenta. {ECO:0000269|PubMed:14962670}.; unclassifiable (Anatomical System);lung;testis;brain; . 0.16791 0.22163 . . 445.2511 4.39211 NEURL1 . . . neuralized E3 ubiquitin protein ligase 1 FUNCTION: Plays a role in hippocampal-dependent synaptic plasticity, learning and memory. Involved in the formation of spines and functional synaptic contacts by modulating the translational activity of the cytoplasmic polyadenylation element- binding protein CPEB3. Promotes ubiquitination of CPEB3, and hence induces CPEB3-dependent mRNA translation activation of glutamate receptor GRIA1 and GRIA2. Can function as an E3 ubiquitin-protein ligase to activate monoubiquitination of JAG1 (in vitro), thereby regulating the Notch pathway. Acts as a tumor suppressor; inhibits malignant cell transformation of medulloblastoma (MB) cells by inhibiting the Notch signaling pathway. {ECO:0000269|PubMed:20847082}.; . TISSUE SPECIFICITY: Expressed in brain, testis, pituitary gland, pancreas and bone marrow. Also poorly expressed in an malignant astrocytomas and several neuroectodermal tumor cell lines. Weakly expressed in medulloblastoma (MB) compared with normal cerebellar tissues. {ECO:0000269|PubMed:11585928, ECO:0000269|PubMed:9519875}.; . . 0.70795 0.11132 . . 1151.79628 6.46787 NEURL1-AS1 . . . NEURL1 antisense RNA 1 . . . . . . . . . . . NEURL1B 0.370536573297444 0.480094712575494 0.149368714127062 neuralized E3 ubiquitin protein ligase 1B FUNCTION: E3 ubiquitin-protein ligase involved in regulation of the Notch pathway through influencing the stability and activity of several Notch ligands. {ECO:0000269|PubMed:19723503}.; . TISSUE SPECIFICITY: Highest expression in brain, prostate and small intestine. In the brain the levels are higher in fetal than in adult stage. In the adult brain the highest levels are detected in the olfactory system, cerebellar cortex, optic nerve and the frontal lobe. {ECO:0000269|PubMed:19723503}.; . . . . . . 214.68822 3.16031 NEURL2 0.00262021372533022 0.557097301794746 0.440282484479924 neuralized E3 ubiquitin protein ligase 2 FUNCTION: Plays an important role in the process of myofiber differentiation and maturation. Probable substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of proteins. Probably contributes to catalysis through recognition and positioning of the substrate and the ubiquitin-conjugating enzyme. During myogenesis, controls the ubiquitination and degradation of the specific pool of CTNNB1/beta-catenin located at the sarcolemma (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed specifically in skeletal and cardiac muscles. {ECO:0000269|PubMed:14960280}.; . . 0.18861 0.10842 0.215080721 67.91696155 241.20889 3.35444 NEURL3 . . . neuralized E3 ubiquitin protein ligase 3 FUNCTION: E3 ubiquitin-protein ligase. Seems to utilize UBE2E1. In vitro, generates polyubiquitin chains via non-canonical lysine residues suggesting that it is not involved in tagging substrates for proteasomal degradation (By similarity). {ECO:0000250}.; . . prostate;pancreas;lung;islets of Langerhans;alveolus; . . . . . . . NEURL4 0.999976734381758 2.32656182396547e-05 1.86164693075256e-15 neuralized E3 ubiquitin protein ligase 4 FUNCTION: Promotes CCP110 ubiquitination and proteasome-dependent degradation. By counteracting accumulation of CP110, maintains normal centriolar homeostasis and preventing formation of ectopic microtubular organizing centers. {ECO:0000269|PubMed:22261722, ECO:0000269|PubMed:22441691}.; . TISSUE SPECIFICITY: Widely expressed at high levels (including brain). {ECO:0000269|PubMed:11347906}.; colon;fovea centralis;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lung;placenta;visual apparatus;macula lutea;liver;hypopharynx;spleen;head and neck;cervix;kidney; . . . -0.181977442 39.95635763 3553.47984 11.52075 NEUROD1 0.138071318356774 0.779702188595173 0.0822264930480534 neuronal differentiation 1 FUNCTION: Acts as a transcriptional activator: mediates transcriptional activation by binding to E box-containing promoter consensus core sequences 5'-CANNTG-3'. Associates with the p300/CBP transcription coactivator complex to stimulate transcription of the secretin gene as well as the gene encoding the cyclin-dependent kinase inhibitor CDKN1A. Contributes to the regulation of several cell differentiation pathways, like those that promote the formation of early retinal ganglion cells, inner ear sensory neurons, granule cells forming either the cerebellum or the dentate gyrus cell layer of the hippocampus, endocrine islet cells of the pancreas and enteroendocrine cells of the small intestine. Together with PAX6 or SIX3, is required for the regulation of amacrine cell fate specification. Also required for dendrite morphogenesis and maintenance in the cerebellar cortex. Associates with chromatin to enhancer regulatory elements in genes encoding key transcriptional regulators of neurogenesis (By similarity). {ECO:0000250}.; DISEASE: Maturity-onset diabetes of the young 6 (MODY6) [MIM:606394]: A form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease. {ECO:0000269|PubMed:10545951}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);pancreas;lung;frontal lobe;cerebellum cortex;islets of Langerhans;pineal body;macula lutea;visual apparatus;head and neck;fovea centralis;brain;skeletal muscle;retina; . 0.97789 0.73737 -0.115612493 45.12856806 106.68073 2.24105 NEUROD2 0.729792595092759 0.257796545370281 0.0124108595369605 neuronal differentiation 2 FUNCTION: Transcriptional regulator implicated in neuronal determination. Mediates calcium-dependent transcription activation by binding to E box-containing promoter. Critical factor essential for the repression of the genetic program for neuronal differentiation; prevents the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. Induces transcription of ZEB1, which in turn represses neuronal differentiation by down-regulating REST expression. Plays a role in the establishment and maturation of thalamocortical connections; involved in the segregation of thalamic afferents into distinct barrel domains within layer VI of the somatosensory cortex. Involved in the development of the cerebellar and hippocampal granular neurons, neurons in the basolateral nucleus of amygdala and the hypothalamic-pituitary axis. Associates with chromatin to the DPYSL3 E box-containing promoter (By similarity). {ECO:0000250}.; . . frontal lobe;cerebral cortex;brain; amygdala;superior cervical ganglion;cerebellum peduncles;temporal lobe;globus pallidus;atrioventricular node;pons;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.72201 0.14140 0.035072054 56.2514744 18.18079 0.63335 NEUROD4 0.140552618676384 0.779378214206593 0.0800691671170232 neuronal differentiation 4 FUNCTION: Probably acts as a transcriptional activator. Mediates neuronal differentiation. Required for the regulation of amacrine cell fate specification in the retina (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);optic nerve;macula lutea;visual apparatus;fovea centralis;choroid;lens;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.41307 0.14868 0.883760026 89.07171503 133.06333 2.50762 NEUROD6 0.681645767008427 0.313880356697681 0.00447387629389159 neuronal differentiation 6 FUNCTION: Activates E box-dependent transcription in collaboration with TCF3/E47. May be a trans-acting factor involved in the development and maintenance of the mammalian nervous system. Transactivates the promoter of its own gene (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);frontal lobe;hippocampus;brain;skeletal muscle; amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;subthalamic nucleus;fetal brain;temporal lobe;globus pallidus;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.72067 0.18619 -0.273576253 33.97027601 14.23098 0.51475 NEUROG1 5.1362785698948e-05 0.139222888136537 0.860725749077764 neurogenin 1 FUNCTION: Acts as a transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Associates with chromatin to enhancer regulatory elements in genes encoding key transcriptional regulators of neurogenesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expression restricted to the embryonic nervous system.; unclassifiable (Anatomical System);visual apparatus;brain; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.64756 0.38610 0.503505267 79.88912479 56.26827 1.50628 NEUROG2 0.361612796522161 0.587255726278337 0.0511314771995015 neurogenin 2 FUNCTION: Transcriptional regulator. Involved in neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3').; . . uterus;whole body;heart;testis;brain;skin; superior cervical ganglion;skeletal muscle;parietal lobe; 0.30601 0.24992 0.25917371 70.05779665 122.3088 2.40867 NEUROG3 0.00111669288987821 0.614276436481165 0.384606870628957 neurogenin 3 FUNCTION: Acts as a transcriptional regulator. Together with NKX2- 2, initiates transcriptional activation of NEUROD1. Involved in neurogenesis. Also required for the specification of a common precursor of the 4 pancreatic endocrine cell types (By similarity). {ECO:0000250}.; DISEASE: Diarrhea 4, malabsorptive, congenital (DIAR4) [MIM:610370]: A disease characterized by severe, life-threatening watery diarrhea associated with generalized malabsorption and a paucity of enteroendocrine cells. {ECO:0000269|PubMed:16855267}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.07092 0.20005 0.237127192 68.98443029 2336.07111 8.95300 NEXN 3.66202095881219e-06 0.997369300096627 0.00262703788241395 nexilin (F actin binding protein) FUNCTION: Involved in regulating cell migration through association with the actin cytoskeleton. Has an essential role in the maintenance of Z line and sarcomere integrity. {ECO:0000269|PubMed:12053183, ECO:0000269|PubMed:15823560, ECO:0000269|PubMed:19881492}.; DISEASE: Cardiomyopathy, familial hypertrophic 20 (CMH20) [MIM:613876]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:20970104}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Abundantly expressed in heart and skeletal muscle, and at lower levels in placenta, lung, liver and pancreas. Also expressed in HeLaS3 and MOLT-4 cell lines. {ECO:0000269|PubMed:12053183, ECO:0000269|PubMed:15823560, ECO:0000269|PubMed:19881492}.; smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;atrium;whole body;cochlea;thyroid;testis;artery;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;tongue;hypothalamus;skeletal muscle;lung;adrenal gland;nasopharynx;placenta;liver;head and neck;kidney;stomach;aorta; . 0.19167 0.10259 -0.045835247 50.34206181 1371.33421 6.94727 NEXN-AS1 . . . NEXN antisense RNA 1 . . . . . . . . . . . NF1 0.999999845570262 1.54429738043446e-07 1.06071944201526e-27 neurofibromin 1 FUNCTION: Stimulates the GTPase activity of Ras. NF1 shows greater affinity for Ras GAP, but lower specific activity. May be a regulator of Ras activity. {ECO:0000269|PubMed:2121371, ECO:0000269|PubMed:8417346}.; DISEASE: Neurofibromatosis 1 (NF1) [MIM:162200]: A disease characterized by patches of skin pigmentation (cafe-au-lait spots), Lisch nodules of the iris, tumors in the peripheral nervous system and fibromatous skin tumors. Individuals with the disorder have increased susceptibility to the development of benign and malignant tumors. {ECO:0000269|PubMed:10220149, ECO:0000269|PubMed:10336779, ECO:0000269|PubMed:10607834, ECO:0000269|PubMed:10712197, ECO:0000269|PubMed:10980545, ECO:0000269|PubMed:11258625, ECO:0000269|PubMed:11735023, ECO:0000269|PubMed:11857752, ECO:0000269|PubMed:12522551, ECO:0000269|PubMed:12552569, ECO:0000269|PubMed:12746402, ECO:0000269|PubMed:1302608, ECO:0000269|PubMed:15060124, ECO:0000269|PubMed:15146469, ECO:0000269|PubMed:15520408, ECO:0000269|PubMed:15523642, ECO:0000269|PubMed:15948193, ECO:0000269|PubMed:17160901, ECO:0000269|PubMed:2114220, ECO:0000269|PubMed:21838856, ECO:0000269|PubMed:23758643, ECO:0000269|PubMed:24413922, ECO:0000269|PubMed:7981679, ECO:0000269|PubMed:8081387, ECO:0000269|PubMed:8544190, ECO:0000269|PubMed:8807336, ECO:0000269|PubMed:8834249, ECO:0000269|PubMed:9003501, ECO:0000269|PubMed:9101300, ECO:0000269|PubMed:9150739, ECO:0000269|PubMed:9298829, ECO:0000269|PubMed:9668168}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Watson syndrome (WTSN) [MIM:193520]: A syndrome characterized by the presence of pulmonary stenosis, cafe-au-lait spots, and mental retardation. It is considered as an atypical form of neurofibromatosis. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Familial spinal neurofibromatosis (FSNF) [MIM:162210]: Considered to be an alternative form of neurofibromatosis, showing multiple spinal tumors. {ECO:0000269|PubMed:11704931}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Neurofibromatosis-Noonan syndrome (NFNS) [MIM:601321]: Characterized by manifestations of both NF1 and Noonan syndrome (NS). NS is a disorder characterized by dysmorphic facial features, short stature, hypertelorism, cardiac anomalies, deafness, motor delay, and a bleeding diathesis. {ECO:0000269|PubMed:12707950, ECO:0000269|PubMed:16380919, ECO:0000269|PubMed:19845691}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. Note=The gene represented in this entry may be involved in disease pathogenesis.; TISSUE SPECIFICITY: Detected in brain, peripheral nerve, lung, colon and muscle. {ECO:0000269|PubMed:8417346}.; medulla oblongata;ovary;salivary gland;intestine;colon;skin;prostate;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;spinal cord;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;amnion;hypopharynx;alveolus;liver;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;occipital lobe;testis - interstitial;medulla oblongata;cerebellum peduncles;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.60010 0.90845 -3.091147521 0.471809389 198.4465 3.04463 NF1P1 . . . neurofibromin 1 pseudogene 1 . . . . . . . . . . . NF1P2 . . . neurofibromin 1 pseudogene 2 . . . . . . . . . . . NF1P3 . . . neurofibromin 1 pseudogene 3 . . . . . . . . . . . NF1P4 . . . neurofibromin 1 pseudogene 4 . . . . . . . . . . . NF1P5 . . . neurofibromin 1 pseudogene 5 . . . . . . . . . . . NF1P6 . . . neurofibromin 1 pseudogene 6 . . . . . . . . . . . NF1P7 . . . neurofibromin 1 pseudogene 7 . . . . . . . . . . . NF1P8 . . . neurofibromin 1 pseudogene 8 . . . . . . . . . . . NF1P9 . . . neurofibromin 1 pseudogene 9 . . . . . . . . . . . NF1P10 . . . neurofibromin 1 pseudogene 10 . . . . . . . . . . . NF1P11 . . . neurofibromin 1 pseudogene 11 . . . . . . . . . . . NF1P12 . . . neurofibromin 1 pseudogene 12 . . . . . . . . . . . NF2 0.999923343294104 7.66566856224408e-05 2.02732737141178e-11 neurofibromin 2 (merlin) FUNCTION: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:20159598, ECO:0000269|PubMed:20178741}.; DISEASE: Neurofibromatosis 2 (NF2) [MIM:101000]: Genetic disorder characterized by bilateral vestibular schwannomas (formerly called acoustic neuromas), schwannomas of other cranial and peripheral nerves, meningiomas, and ependymomas. It is inherited in an autosomal dominant fashion with full penetrance. Affected individuals generally develop symptoms of eighth-nerve dysfunction in early adulthood, including deafness and balance disorder. Although the tumors of NF2 are histologically benign, their anatomic location makes management difficult, and patients suffer great morbidity and mortality. {ECO:0000269|PubMed:10090912, ECO:0000269|PubMed:10790209, ECO:0000269|PubMed:12709270, ECO:0000269|PubMed:20445339, ECO:0000269|PubMed:7666400, ECO:0000269|PubMed:7759081, ECO:0000269|PubMed:7913580, ECO:0000269|PubMed:8081368, ECO:0000269|PubMed:8230593, ECO:0000269|PubMed:8566958, ECO:0000269|PubMed:8698340, ECO:0000269|PubMed:9643284}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Schwannomatosis 1 (SWNTS1) [MIM:162091]: A cancer syndrome in which patients develop multiple non-vestibular schwannomas, benign neoplasms that arise from Schwann cells of the cranial, peripheral, and autonomic nerves. {ECO:0000269|PubMed:18072270}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive neoplasm of the serosal lining of the chest. It appears as broad sheets of cells, with some regions containing spindle- shaped, sarcoma-like cells and other regions showing adenomatous patterns. Pleural mesotheliomas have been linked to exposure to asbestos. {ECO:0000269|PubMed:12136076}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Isoform 1 and isoform 3 are predominant. Isoform 4, isoform 5 and isoform 6 are expressed moderately. Isoform 8 is found at low frequency. Isoform 7, isoform 9 and isoform 10 are not expressed in adult tissues, with the exception of adult retina expressing isoform 10. Isoform 9 is faintly expressed in fetal brain, heart, lung, skeletal muscle and spleen. Fetal thymus expresses isoforms 1, 7, 9 and 10 at similar levels.; lymphoreticular;medulla oblongata;ovary;colon;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;tongue;skeletal muscle;pancreas;lung;epididymis;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;cerebellum; dorsal root ganglion;testis - interstitial;medulla oblongata;superior cervical ganglion;prefrontal cortex;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.97456 0.35707 -0.868835007 10.65109696 30.21856 0.96366 NFAM1 0.0260796215955231 0.918933413561883 0.0549869648425936 NFAT activating protein with ITAM motif 1 FUNCTION: May function in immune system as a receptor which activates via the calcineurin/NFAT-signaling pathway the downstream cytokine gene promoters. Activates the transcription of IL-13 and TNF-alpha promoters. May be involved in the regulation of B-cell, but not T-cell, development. Overexpression activates downstream effectors without ligand binding or antibody cross- linking. {ECO:0000269|PubMed:12615919, ECO:0000269|PubMed:15143214}.; . TISSUE SPECIFICITY: Highly expressed in neutrophils, primary monocytes, mast cells, monocytic cell lines and lymphocytes. Also expressed in spleen B and T-cells, and lung. Expressed at low level in non-immune tissue. {ECO:0000269|PubMed:12615919, ECO:0000269|PubMed:15143214}.; unclassifiable (Anatomical System);cartilage;ovary;colon;parathyroid;blood;bone marrow;lung;frontal lobe;bone;placenta;testis;spleen;kidney;nose;brain; superior cervical ganglion; 0.06307 0.08109 -0.135838822 43.77211607 169.80945 2.84345 NFASC 0.998762678321666 0.00123732167808735 2.46947351907627e-13 neurofascin FUNCTION: Cell adhesion, ankyrin-binding protein which may be involved in neurite extension, axonal guidance, synaptogenesis, myelination and neuron-glial cell interactions. {ECO:0000250}.; . . unclassifiable (Anatomical System);smooth muscle;heart;islets of Langerhans;lens;skeletal muscle;skin;breast;uterus;prostate;optic nerve;lung;frontal lobe;thyroid;placenta;bone;visual apparatus;testis;kidney;mammary gland;brain;peripheral nerve; dorsal root ganglion;amygdala;thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;olfactory bulb;hypothalamus;spinal cord;caudate nucleus;atrioventricular node;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.24989 0.19733 -1.802562453 2.211606511 2596.27063 9.53865 NFAT5 0.999990941723713 9.05827628705949e-06 1.87070279345487e-16 nuclear factor of activated T-cells 5, tonicity-responsive FUNCTION: Transcription factor involved in the transcriptional regulation of osmoprotective and inflammatory genes. Regulates hypertonicity-induced cellular accumulation of osmolytes.; . TISSUE SPECIFICITY: Highest levels in skeletal muscle, brain, heart and peripheral blood leukocytes. Also expressed in placenta, lung, liver, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine and colon.; ovary;developmental;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;cingulate cortex; 0.85493 0.30152 -1.372317395 4.446803491 79.19061 1.87966 NFATC1 0.969219887746034 0.0307797260215426 3.86232423810996e-07 nuclear factor of activated T-cells, cytoplasmic, calcineurin-dependent 1 FUNCTION: Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 or IL-4 gene transcription. Also controls gene expression in embryonic cardiac cells. Could regulate not only the activation and proliferation but also the differentiation and programmed death of T-lymphocytes as well as lymphoid and non-lymphoid cells.; . TISSUE SPECIFICITY: Expressed in thymus, peripheral leukocytes as T-cells and spleen. Isoforms A are preferentially expressed in effector T-cells (thymus and peripheral leukocytes) whereas isoforms B and isoforms C are preferentially expressed in naive T- cells (spleen). Isoforms B are expressed in naive T-cells after first antigen exposure and isoforms A are expressed in effector T- cells after second antigen exposure. Isoforms IA are widely expressed but not detected in liver nor pancreas, neural expression is strongest in corpus callosum. Isoforms IB are expressed mostly in muscle, cerebellum, placenta and thymus, neural expression in fetal and adult brain, strongest in corpus callosum. {ECO:0000269|PubMed:18675896}.; myocardium;smooth muscle;umbilical cord;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.26703 0.65916 -1.846676608 2.052370842 1895.12903 8.00523 NFATC2 0.99925103106598 0.000748968719836581 2.14183569577398e-10 nuclear factor of activated T-cells, cytoplasmic, calcineurin-dependent 2 FUNCTION: Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2, IL-3, IL-4, TNF-alpha or GM-CSF. Promotes invasive migration through the activation of GPC6 expression and WNT5A signaling pathway. {ECO:0000269|PubMed:15790681, ECO:0000269|PubMed:21871017}.; . TISSUE SPECIFICITY: Expressed in thymus, spleen, heart, testis, brain, placenta, muscle and pancreas. Isoform 1 is highly expressed in the small intestine, heart, testis, prostate, thymus, placenta and thyroid. Isoform 3 is highly expressed in stomach, uterus, placenta, trachea and thyroid. {ECO:0000269|PubMed:8668213}.; . . 0.92588 0.42851 -1.568966504 3.178815758 251.55874 3.41642 NFATC2IP 0.00232734526476926 0.924316270562338 0.073356384172893 nuclear factor of activated T-cells, cytoplasmic, calcineurin-dependent 2 interacting protein FUNCTION: In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-driven transcription of a specific subset of cytokine genes, including IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4 promoter; this leads to enhancement of histone H4 'Arg-3'- methylation and facilitates subsequent histone acetylation at the IL4 locus, thus promotes robust cytokine expression (By similarity). Down-regulates formation of poly-SUMO chains by UBE2I/UBC9 (By similarity). {ECO:0000250}.; . . ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;synovium;bone;iris;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;urinary;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; amygdala;superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;pons;skeletal muscle;parietal lobe;cerebellum; 0.09600 0.09851 . . 582.07381 4.89098 NFATC3 0.998062457612728 0.0019375419476304 4.39641999260978e-10 nuclear factor of activated T-cells, cytoplasmic, calcineurin-dependent 3 FUNCTION: Acts as a regulator of transcriptional activation. Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2. {ECO:0000269|PubMed:18815128}.; . TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in thymus and is also found in peripheral blood leukocytes and kidney. Isoform 2 is predominantly expressed in skeletal muscle and is also found in thymus, kidney, testis, spleen, prostate, ovary, small intestine, heart, placenta and pancreas. Isoform 3 is expressed in thymus and kidney. Isoform 4 is expressed in thymus and skeletal muscle.; lymphoreticular;myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;urinary;blood;lens;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;white blood cells;skeletal muscle;thymus; 0.70920 0.16325 0.161677043 64.96225525 342.05761 3.92216 NFATC4 0.985383663547882 0.014616032635945 3.03816172762597e-07 nuclear factor of activated T-cells, cytoplasmic, calcineurin-dependent 4 FUNCTION: Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 and IL- 4. Transcriptionally repressed by estrogen receptors; this inhibition is further enhanced by estrogen. Increases the transcriptional activity of PPARG and has a direct role in adipocyte differentiation. May play an important role in myotube differentiation. May play a critical role in cardiac development and hypertrophy. May play a role in deafferentation-induced apoptosis of sensory neurons. {ECO:0000269|PubMed:11997522, ECO:0000269|PubMed:17213202, ECO:0000269|PubMed:18668201, ECO:0000269|PubMed:7749981}.; . TISSUE SPECIFICITY: Highly expressed in placenta, lung, kidney, testis and ovary. Weakly expressed in spleen and thymus. Not expressed in peripheral blood lymphocytes. Detected in hippocampus. {ECO:0000269|PubMed:18675896}.; myocardium;smooth muscle;ovary;colon;parathyroid;choroid;skin;retina;uterus;optic nerve;endometrium;synovium;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.83949 0.17286 0.249861693 69.66265629 4496.21287 13.46349 NFE2 0.688914373837473 0.306913801525545 0.00417182463698123 nuclear factor, erythroid 2 FUNCTION: Component of the NF-E2 complex essential for regulating erythroid and megakaryocytic maturation and differentiation. Binds to the hypersensitive site 2 (HS2) of the beta-globin control region (LCR). This subunit (NFE2) recognizes the TCAT/C sequence of the AP-1-like core palindrome present in a number of erythroid and megakaryocytic gene promoters. Requires MAFK or other small MAF proteins for binding to the NF-E2 motif. May play a role in all aspects of hemoglobin production from globin and heme synthesis to procurement of iron. {ECO:0000269|PubMed:11154691, ECO:0000269|PubMed:16287851}.; . TISSUE SPECIFICITY: Expressed in hematopoietic cells and also in colon and testis.; unclassifiable (Anatomical System);cartilage;umbilical cord;heart;ovary;parathyroid;blood;bone marrow;lung;placenta;visual apparatus;liver;testis;spleen;cervix;kidney;brain;bladder;thymus; whole blood;bone marrow; 0.50725 0.35980 -0.273576253 33.97027601 16.01387 0.56681 NFE2L1 0.998123949191488 0.00187604088295068 9.92556082430234e-09 nuclear factor, erythroid 2 like 1 FUNCTION: Activates erythroid-specific, globin gene expression.; . . myocardium;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;amygdala;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; whole brain;dorsal root ganglion;occipital lobe;superior cervical ganglion;thalamus;olfactory bulb;hypothalamus;spinal cord;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;adrenal gland;prefrontal cortex;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion;parietal lobe;cingulate cortex; 0.73510 0.16019 -1.464150033 3.780372729 46.66378 1.31908 NFE2L2 0.686008361900756 0.313100050643991 0.000891587455252868 nuclear factor, erythroid 2 like 2 FUNCTION: Transcription activator that binds to antioxidant response (ARE) elements in the promoter regions of target genes. Important for the coordinated up-regulation of genes in response to oxidative stress. May be involved in the transcriptional activation of genes of the beta-globin cluster by mediating enhancer activity of hypersensitive site 2 of the beta-globin locus control region. {ECO:0000269|PubMed:11035812}.; . TISSUE SPECIFICITY: Widely expressed. Highest expression in adult muscle, kidney, lung, liver and in fetal muscle.; . . 0.54711 0.10126 0.042348793 57.31304553 65.31614 1.66331 NFE2L3 1.09962052794343e-07 0.185995009899898 0.814004880138049 nuclear factor, erythroid 2 like 3 FUNCTION: Activates erythroid-specific, globin gene expression.; . TISSUE SPECIFICITY: Highly expressed in human placenta and also in B-cell and monocyte cell lines. Low expression in heart, brain, lung, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:10037736}.; unclassifiable (Anatomical System);lymph node;ovary;heart;islets of Langerhans;sympathetic chain;colon;uterus;bile duct;prostate;whole body;lung;endometrium;adrenal gland;larynx;placenta;liver;head and neck;germinal center;kidney;brain;stomach;peripheral nerve;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.50592 0.09520 0.202129237 67.42745931 537.43024 4.72571 NFE2L3P1 . . . nuclear factor, erythroid 2 like 3 pseudogene 1 . . . . . . . . . . . NFE2L3P2 . . . nuclear factor, erythroid 2 like 3 pseudogene 2 . . . . . . . . . . . NFE4 . . . nuclear factor, erythroid 4 FUNCTION: Functions as part of the SSP (stage selector protein) complex, a complex that contributes to the preferential expression of the gamma-gene in fetal erythroid cells by facilitating the interaction of the gamma-globin genes with enhancer elements contained in the locus control region (LCR). The complex binds to the stage selector element (SSE) in the proximal gamma-globin promoter. In contrast, isoform 2 acts as a repressor of gamma- globin gene expression by preventing NFE2 and RNA polymerase II recruitment to the promoter. {ECO:0000269|PubMed:11003662, ECO:0000269|PubMed:15084587, ECO:0000269|PubMed:16263792}.; . TISSUE SPECIFICITY: Specifically expressed in fetal liver, cord blood and bone marrow. Also expressed in the K562 and HEL cell lines, which constitutively express the fetal globin genes. {ECO:0000269|PubMed:11003662}.; . . . . . . . . NFIA 0.999555166212873 0.000444832317303599 1.4698236213465e-09 nuclear factor I/A FUNCTION: Recognizes and binds the palindromic sequence 5'- TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.; . . myocardium;smooth muscle;colon;skin;uterus;prostate;frontal lobe;cochlea;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;hypothalamus;skeletal muscle;lung;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;stomach;cerebellum; . 0.35017 0.36076 -0.538132194 20.26421326 12.88084 0.46973 NFIA-AS1 . . . NFIA antisense RNA 1 . . . . . . . . . . . NFIA-AS2 . . . NFIA antisense RNA 2 . . . . . . . . . . . NFIB 0.990809167018789 0.00919035182897158 4.81152239298282e-07 nuclear factor I/B FUNCTION: Recognizes and binds the palindromic sequence 5'- TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.; . . . . 0.94482 0.41901 -0.449946534 24.00330267 16.65407 0.58684 NFIC 0.842498930517079 0.157376805502965 0.000124263979955481 nuclear factor I/C (CCAAT-binding transcription factor) FUNCTION: Recognizes and binds the palindromic sequence 5'- TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;iris;testis;brain;tonsil;unclassifiable (Anatomical System);cartilage;lacrimal gland;islets of Langerhans;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;cervix;head and neck;kidney;mammary gland;stomach;thymus;cerebellum; tongue;liver;adrenal cortex;fetal thyroid;cingulate cortex;skeletal muscle;parietal lobe; 0.45733 0.61712 -0.666770504 15.86459071 245.76412 3.38193 NFIL3 0.948599643399575 0.0512340085085488 0.000166348091876394 nuclear factor, interleukin 3 regulated FUNCTION: Acts as a transcriptional regulator that recognizes and binds to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many cellular and viral promoters. Represses transcription from promoters with activating transcription factor (ATF) sites. Represses promoter activity in osteoblasts (By similarity). Represses transcriptional activity of PER1 (By similarity). Represses transcriptional activity of PER2 via the B- site on the promoter (By similarity). Activates transcription from the interleukin-3 promoter in T-cells. Competes for the same consensus-binding site with PAR DNA-binding factors (DBP, HLF and TEF) (By similarity). Component of the circadian clock that acts as a negative regulator for the circadian expression of PER2 oscillation in the cell-autonomous core clock (By similarity). Protects pro-B cells from programmed cell death (By similarity). {ECO:0000250, ECO:0000269|PubMed:1620116, ECO:0000269|PubMed:7565758, ECO:0000269|PubMed:8836190}.; . TISSUE SPECIFICITY: Expressed in bladder stomach, thyroid, spinal cord, lymph node, trachea, adrenal gland, bone marrow and muscle. {ECO:0000269|PubMed:10942106}.; medulla oblongata;ovary;sympathetic chain;colon;parathyroid;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;head and neck;cervix;kidney;stomach;aorta; superior cervical ganglion;adrenal cortex;ciliary ganglion;skeletal muscle; 0.32654 0.23272 -0.025608647 51.91672564 75.34728 1.81645 NFIX 0.989066455193014 0.010929908430559 3.63637642745578e-06 nuclear factor I/X (CCAAT-binding transcription factor) FUNCTION: Recognizes and binds the palindromic sequence 5'- TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.; DISEASE: Sotos syndrome 2 (SOTOS2) [MIM:614753]: A form of Sotos syndrome, a childhood overgrowth syndrome characterized by prenatal and postnatal overgrowth, developmental delay, mental retardation, advanced bone age, and abnormal craniofacial morphology. SOTOS2 patients have macrocephaly, long narrow face, high forehead, slender habitus, scoliosis, and unusual behavior characterized especially by anxiety. {ECO:0000269|PubMed:22301465}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Marshall-Smith syndrome (MRSHSS) [MIM:602535]: A distinct malformation syndrome characterized by accelerated skeletal maturation, relative failure to thrive, respiratory difficulties, mental retardation, and unusual facies, including prominent forehead, shallow orbits, blue sclerae, depressed nasal bridge, and micrognathia. Additional skeletal findings include long and thin tubular bones, broad middle phalanges with relatively narrow distal phalanges, and scoliosis. {ECO:0000269|PubMed:20673863}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:20673863}.; ovary;colon;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;amniotic fluid;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;mammary gland;stomach; trigeminal ganglion; 0.35172 0.09375 -0.273576253 33.97027601 1.20885 0.03724 NFKB1 0.994260375128404 0.00573962361155129 1.26004505564412e-09 nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105. {ECO:0000269|PubMed:15485931}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;atrium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;nasopharynx;placenta;kidney;stomach; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion; 0.93844 0.94648 -0.483123186 22.78249587 84.42133 1.95667 NFKB2 0.999696457724303 0.00030354227089764 4.79909204369052e-12 nuclear factor of kappa light polypeptide gene enhancer in B-cells 2 FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF- kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14- activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65. In concert with RELB, regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK- ARNTL/BMAL1 heterodimer. {ECO:0000269|PubMed:7925301}.; DISEASE: Note=A chromosomal aberration involving NFKB2 is found in a case of B-cell non Hodgkin lymphoma (B-NHL). Translocation t(10;14)(q24;q32) with IGHA1. The resulting oncogene is also called Lyt-10C alpha variant.; DISEASE: Note=A chromosomal aberration involving NFKB2 is found in a cutaneous T-cell leukemia (C-TCL) cell line. This rearrangement produces the p80HT gene which codes for a truncated 80 kDa protein (p80HT).; DISEASE: Note=In B-cell leukemia (B-CLL) cell line, LB40 and EB308, can be found after heterogeneous chromosomal aberrations, such as internal deletions.; DISEASE: Immunodeficiency, common variable, 10 (CVID10) [MIM:615577]: A primary immunodeficiency characterized by childhood-onset of recurrent infections, hypogammaglobulinemia, and decreased numbers of memory and marginal zone B-cells. Some patients may develop autoimmune features and have circulating autoantibodies. An unusual feature is central adrenal insufficiency. {ECO:0000269|PubMed:24140114, ECO:0000269|PubMed:25524009}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;colon;skin;uterus;prostate;endometrium;thyroid;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;blood;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; temporal lobe;trigeminal ganglion;skeletal muscle;tonsil; 0.82248 0.47581 -0.778825328 12.88039632 68.14775 1.70783 NFKBIA 0.97935202641697 0.0206306411448845 1.73324381455554e-05 NFKB inhibitor alpha FUNCTION: Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and proinflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription. {ECO:0000269|PubMed:7479976}.; DISEASE: Ectodermal dysplasia, anhidrotic, with T-cell immunodeficiency autosomal dominant (ADEDAID) [MIM:612132]: A form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. This form of ectodermal dysplasia is associated with decreased production of pro-inflammatory cytokines and certain interferons, rendering patients susceptible to infection. {ECO:0000269|PubMed:14523047, ECO:0000269|PubMed:18412279}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;umbilical cord;skin;retina;bone marrow;prostate;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;islets of Langerhans;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;kidney;stomach;aorta;thymus; adrenal cortex;white blood cells;fetal lung;trigeminal ganglion; 0.90002 0.92612 -0.271755481 34.31823543 27.87219 0.89545 NFKBIB 0.249570217341025 0.744083745089406 0.00634603756956875 NFKB inhibitor beta FUNCTION: Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. However, the unphosphorylated form resynthesized after cell stimulation is able to bind NF-kappa-B allowing its transport to the nucleus and protecting it to further NFKBIA- dependent inactivation. Association with inhibitor kappa B- interacting NKIRAS1 and NKIRAS2 prevent its phosphorylation rendering it more resistant to degradation, explaining its slower degradation.; . TISSUE SPECIFICITY: Expressed in all tissues examined.; unclassifiable (Anatomical System);medulla oblongata;sympathetic chain;colon;blood;skin;breast;uterus;pancreas;prostate;lung;frontal lobe;cochlea;bone;placenta;iris;duodenum;liver;testis;cervix;spleen;germinal center;kidney;brain;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;liver;testis;atrioventricular node;trigeminal ganglion; 0.51159 0.63966 -0.556537043 19.72753008 70.11925 1.73821 NFKBID 0.795064373784277 0.204679478364207 0.000256147851515819 NFKB inhibitor delta FUNCTION: May regulate the expression of IL-2, IL-6, and other cytokines through regulation on NF-kappa-B activity. Functions in the regulation of inflammatory responses. May also regulate TCR- induced negative selection of thymocytes (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;colon;blood;fovea centralis;choroid;lens;retina;optic nerve;lung;placenta;thyroid;macula lutea;liver;spleen;germinal center;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14214 0.09456 -0.205617011 38.57631517 710.32342 5.29547 NFKBIE 0.548429215223667 0.448618212961179 0.00295257181515467 NFKB inhibitor epsilon FUNCTION: Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. Inhibits DNA-binding of NF-kappa-B p50-p65 and p50-c-Rel complexes. {ECO:0000269|PubMed:9315679}.; . TISSUE SPECIFICITY: Highly expressed in spleen, testis and lung, followed by kidney, pancreas, heart, placenta and brain. Also expressed in granulocytes and macrophages.; lymphoreticular;ovary;salivary gland;intestine;colon;choroid;skin;bone marrow;uterus;prostate;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;pharynx;blood;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion; 0.13910 0.16375 . . 676.72743 5.19737 NFKBIL1 0.816647169800353 0.183164767297989 0.000188062901658534 NFKB inhibitor like 1 FUNCTION: Involved in the regulation of innate immune response. Acts as negative regulator of Toll-like receptor and interferon- regulatory factor (IRF) signaling pathways. Contributes to the negative regulation of transcriptional activation of NF-kappa-B target genes in response to endogenous proinflammatory stimuli. {ECO:0000269|PubMed:20829348}.; . TISSUE SPECIFICITY: Detected in different cell types including monocytes, T-cells, B-cells and hepatocytes.; . . 0.11802 . 0.03689118 56.64071715 36.61435 1.09910 NFKBIZ 0.999616951200414 0.000383047778562741 1.02102343555193e-09 NFKB inhibitor zeta FUNCTION: Involved in regulation of NF-kappa-B transcription factor complexes. Inhibits NF-kappa-B activity without affecting its nuclear translocation upon stimulation. Inhibits DNA-binding of RELA and NFKB1/p50, and of the NF-kappa-B p65-p50 heterodimer and the NF-kappa-B p50-p50 homodimer. Seems also to activate NF- kappa-B-mediated transcription. In vitro, upon association with NFKB1/p50 has transcriptional activation activity and, together with NFKB1/p50 and RELA, is recruited to LCN2 promoters. Promotes transcription of LCN2 and DEFB4. Is recruited to IL-6 promoters and activates IL-6 but decreases TNF-alpha production in response to LPS. Seems to be involved in the induction of inflammatory genes activated through TLR/IL-1 receptor signaling. May promote apoptosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:16513645, ECO:0000269|PubMed:16622025}.; . TISSUE SPECIFICITY: Expressed at high levels in peripheral blood leukocytes and lung, at moderate levels in liver, placenta, and at low levels in spleen, kidney, skeletal muscle and heart. {ECO:0000269|PubMed:16513645}.; smooth muscle;ovary;colon;skin;retina;bone marrow;uterus;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;spinal cord;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;fetal lung;ciliary ganglion;white blood cells;atrioventricular node; 0.49089 0.09707 -0.622676946 17.30950696 64.66853 1.65031 NFRKB 0.752744578187088 0.247255415715441 6.09747015349587e-09 nuclear factor related to kappaB binding protein FUNCTION: Binds to the DNA consensus sequence 5'-GGGGAATCTCC-3'. {ECO:0000269|PubMed:18922472}.; . TISSUE SPECIFICITY: Expressed in thymus, brain, testes, spleen and liver. {ECO:0000269|PubMed:1777480}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;muscle;colon;skin;skeletal muscle;retina;uterus;prostate;lung;adrenal gland;bone;placenta;visual apparatus;liver;testis;germinal center;brain;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21273 0.12979 -2.651579643 0.76079264 181.58645 2.92847 NFS1 0.832120909457389 0.167849146105863 2.99444367479753e-05 NFS1 cysteine desulfurase FUNCTION: Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron- sulfur (Fe-S) clusters. May be involved in the biosynthesis of molybdenum cofactor. {ECO:0000269|PubMed:18650437}.; . TISSUE SPECIFICITY: Predominantly expressed in heart and skeletal muscle. Also found in brain, liver and pancreas.; unclassifiable (Anatomical System);ovary;islets of Langerhans;hypothalamus;salivary gland;intestine;pharynx;colon;blood;prostate;visual apparatus;liver;testis;kidney;brain;bladder; . 0.11752 0.38012 -0.426079032 25.36565228 33.49158 1.03381 NFU1 0.000687750920306089 0.747523853126558 0.251788395953136 NFU1 iron-sulfur cluster scaffold FUNCTION: Iron-sulfur cluster scaffold protein which can assemble [4Fe-2S] clusters and deliver them to target proteins. {ECO:0000269|PubMed:12886008}.; DISEASE: Multiple mitochondrial dysfunctions syndrome 1 (MMDS1) [MIM:605711]: A severe disorder of systemic energy metabolism, resulting in weakness, respiratory failure, lack of neurologic development, lactic acidosis, hyperglycinemia and early death. Some patients show failure to thrive, pulmonary hypertension, hypotonia and irritability. Biochemical features include severe combined deficiency of the 2-oxoacid dehydrogenases, defective lipoic acid synthesis and reduction in activity of mitochondrial respiratory chain complexes. {ECO:0000269|PubMed:21944046, ECO:0000269|PubMed:22077971}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Expression in adult lung is weak compared to fetal lung. {ECO:0000269|PubMed:12915448}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;cerebellum cortex;tongue;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;hippocampus;alveolus;head and neck;kidney;stomach;peripheral nerve; superior cervical ganglion;globus pallidus;trigeminal ganglion; 0.56883 0.14403 0.415317661 76.81056853 744.72427 5.41588 NFU1P1 . . . NFU1 iron-sulfur cluster scaffold pseudogene 1 . . . . . . . . . . . NFU1P2 . . . NFU1 iron-sulfur cluster scaffold pseudogene 2 . . . . . . . . . . . NFX1 0.386441238708853 0.613558731884033 2.94071142530114e-08 nuclear transcription factor, X-box binding 1 FUNCTION: Binds to the X-box motif of MHC class II genes and represses their expression. May play an important role in regulating the duration of an inflammatory response by limiting the period in which MHC class II molecules are induced by interferon-gamma. Isoform 3 binds to the X-box motif of TERT promoter and represses its expression. Together with PABPC1 or PABPC4, isoform 1 acts as a coactivator for TERT expression. Mediates E2-dependent ubiquitination. {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:15371341, ECO:0000269|PubMed:17267499}.; . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;spinal ganglion;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.44031 . -1.591018721 3.084453881 335.711 3.89158 NFXL1 0.0078889795648465 0.992109983761132 1.03667402135526e-06 nuclear transcription factor, X-box binding like 1 . . . unclassifiable (Anatomical System);ovary;islets of Langerhans;urinary;colon;parathyroid;blood;skin;prostate;lung;cochlea;endometrium;placenta;visual apparatus;testis;germinal center;kidney;brain; . 0.11984 0.07985 0.222355725 68.44184949 4983.51379 14.41291 NFYA 0.0220592707694253 0.974636289016496 0.00330444021407863 nuclear transcription factor Y subunit alpha FUNCTION: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'- CCAAT-3' box motif found in the promoters of its target genes. NF- Y can function as both an activator and a repressor, depending on its interacting cofactors. NF-YA positively regulates the transcription of the core clock component ARNTL/BMAL1. {ECO:0000269|PubMed:12741956}.; . . medulla oblongata;ovary;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;thyroid;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;lacrimal gland;hypothalamus;blood;breast;lung;placenta;visual apparatus;duodenum;cervix;kidney;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.98942 0.19444 -0.207437529 38.2814343 18.86158 0.65137 NFYAP1 . . . nuclear transcription factor Y subunit alpha pseudogene 1 . . . . . . . . . . . NFYB 0.00327375770291337 0.827223731645094 0.169502510651993 nuclear transcription factor Y subunit beta FUNCTION: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'- CCAAT-3' box motif found in the promoters of its target genes. NF- Y can function as both an activator and a repressor, depending on its interacting cofactors.; . . myocardium;smooth muscle;ovary;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;thyroid;pituitary gland;testis;amniotic fluid;dura mater;germinal center;brain;pineal gland;unclassifiable (Anatomical System);meninges;cartilage;heart;tongue;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;trigeminal ganglion;parietal lobe; 0.82614 0.23984 0.101211609 60.95777306 6.01187 0.22629 NFYC 0.631959350371475 0.367740324961642 0.000300324666883349 nuclear transcription factor Y subunit gamma FUNCTION: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'- CCAAT-3' box motif found in the promoters of its target genes. NF- Y can function as both an activator and a repressor, depending on its interacting cofactors.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;muscle;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;peripheral nerve; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;heart;testis;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle;cerebellum; 0.69643 0.11852 -0.427900189 25.14744043 10.27145 0.37502 NFYC-AS1 . . . NFYC antisense RNA 1 . . . . . . . . . . . NGB 0.00253179978703355 0.549720102979612 0.447748097233355 neuroglobin FUNCTION: Involved in oxygen transport in the brain. Hexacoordinate globin, displaying competitive binding of oxygen or the distal His residue to the iron atom. Not capable of penetrating cell membranes. The deoxygenated form exhibits nitrite reductase activity inhibiting cellular respiration via NO-binding to cytochrome c oxidase. Involved in neuroprotection during oxidative stress. May exert its anti-apoptotic activity by acting to reset the trigger level of mitochondrial cytochrome c release necessary to commit the cells to apoptosis. {ECO:0000269|PubMed:11029004, ECO:0000269|PubMed:11473128, ECO:0000269|PubMed:18416560, ECO:0000269|PubMed:21190290, ECO:0000269|PubMed:21296891}.; . TISSUE SPECIFICITY: Predominantly expressed in brain, the strongest expression is seen in the frontal lobe, the subthalamic nucleus and the thalamus. {ECO:0000269|PubMed:11029004}.; unclassifiable (Anatomical System);optic nerve;lung;whole body;hypothalamus;macula lutea;fovea centralis;choroid;lens;brain;retina;cerebellum; superior cervical ganglion;globus pallidus;atrioventricular node;pons;skeletal muscle; 0.16158 0.38360 0.169169615 65.33380514 44.45895 1.27507 NGDN 6.84417480572023e-07 0.699495389865153 0.300503925717367 neuroguidin FUNCTION: Involved in the translational repression of cytoplasmic polyadenylation element (CPE)-containing mRNAs. {ECO:0000250}.; . . . . 0.12759 0.15813 -0.224023033 37.4321774 210.22103 3.12870 NGEF 0.949825524634906 0.0501731681335563 1.30723153731779e-06 neuronal guanine nucleotide exchange factor FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) which differentially activates the GTPases RHOA, RAC1 and CDC42. Plays a role in axon guidance regulating ephrin-induced growth cone collapse and dendritic spine morphogenesis. Upon activation by ephrin through EPHA4, the GEF activity switches toward RHOA resulting in its activation. Activated RHOA promotes cone retraction at the expense of RAC1- and CDC42-stimulated growth cone extension (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in brain specifically in caudate nucleus and to a lower extent in amygdala and hippocampus. Also detected in lung. {ECO:0000269|PubMed:10777665}.; unclassifiable (Anatomical System);cartilage;colon;fovea centralis;choroid;lens;retina;uterus;pancreas;prostate;optic nerve;lung;cerebral cortex;endometrium;bone;macula lutea;visual apparatus;hippocampus;liver;testis;spleen;kidney;brain;stomach; . 0.30052 0.12355 -0.33061537 30.82094834 85.46834 1.97133 NGF 0.704368811874854 0.2797022454076 0.0159289427175468 nerve growth factor FUNCTION: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades through those receptor tyrosine kinase to regulate neuronal proliferation, differentiation and survival. Inhibits metalloproteinase dependent proteolysis of platelet glycoprotein VI (PubMed:20164177). {ECO:0000269|PubMed:20164177}.; DISEASE: Neuropathy, hereditary sensory and autonomic, 5 (HSAN5) [MIM:608654]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by sensory and/or autonomic abnormalities. HSAN5 patients manifest loss of pain perception and impaired temperature sensitivity, ulcers, and in some cases self- mutilation. The autonomic involvement is variable. {ECO:0000269|PubMed:14976160, ECO:0000269|PubMed:22302274}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.15014 0.95621 0.106667882 61.73036093 2170.14248 8.57715 NGFR 0.238222215108748 0.754753802946829 0.00702398194442268 nerve growth factor receptor FUNCTION: Plays a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, probably by regulating RAB31 activity, and thereby contributes to the regulation of insulin-dependent glucose uptake (By similarity). Low affinity receptor which can bind to NGF, BDNF, NT-3, and NT-4. Can mediate cell survival as well as cell death of neural cells. Necessary for the circadian oscillation of the clock genes ARNTL/BMAL1, PER1, PER2 and NR1D1 in the suprachiasmatic nucleus (SCN) of the brain and in liver and of the genes involved in glucose and lipid metabolism in the liver. {ECO:0000250, ECO:0000269|PubMed:14966521, ECO:0000269|PubMed:23785138}.; . . unclassifiable (Anatomical System);heart;ovary;colon;fovea centralis;choroid;lens;skin;retina;pancreas;prostate;optic nerve;lung;cerebral cortex;synovium;placenta;thyroid;bone;macula lutea;duodenum;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;olfactory bulb;ciliary ganglion;atrioventricular node; 0.45788 0.74431 -0.203796826 38.81811748 290.02902 3.64468 NGLY1 2.20290079449091e-10 0.645404621836809 0.354595377942901 N-glycanase 1 FUNCTION: Specifically deglycosylates the denatured form of N- linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl- glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high- mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins. {ECO:0000269|PubMed:14749736, ECO:0000269|PubMed:15358861}.; DISEASE: Congenital disorder of deglycosylation (CDDG) [MIM:615273]: A multisystem disorder characterized by developmental delay, hypotonia, abnormal involuntary movements and alacrima or poor tear production. Other features include microcephaly, intractable seizures, abnormal eye movements and evidence of liver dysfunction, probably due to cytoplasmic accumulation of storage material in vacuoles. {ECO:0000269|PubMed:22581936, ECO:0000269|PubMed:24651605}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;salivary gland;colon;fovea centralis;skin;retina;bone marrow;uterus;frontal lobe;cochlea;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;skeletal muscle;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;hippocampus;alveolus;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.51164 0.55689 -0.554717505 19.79830149 105.92118 2.23101 NGRN 0.0224062148151509 0.91069722481565 0.0668965603691993 neugrin, neurite outgrowth associated FUNCTION: May be involved in neuronal differentiation.; . TISSUE SPECIFICITY: Expressed at high levels in heart, brain and skeletal muscle. In brain, mainly expressed in neurons rather than glial cells. {ECO:0000269|PubMed:11118320}.; medulla oblongata;ovary;salivary gland;intestine;colon;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;larynx;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.03947 . -0.047654689 50.22410946 226.47856 3.25183 NHCP1 . . . non-histone chromosome protein 1 . . . . . . . . . . . NHEJ1 0.027184525357164 0.961121519407895 0.0116939552349407 non-homologous end joining factor 1 FUNCTION: DNA repair protein involved in DNA nonhomologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. May serve as a bridge between XRCC4 and the other NHEJ factors located at DNA ends, or may participate in reconfiguration of the end bound NHEJ factors to allow XRCC4 access to the DNA termini. It may act in concert with XRCC6/XRCC5 (Ku) to stimulate XRCC4-mediated joining of blunt ends and several types of mismatched ends that are noncomplementary or partially complementary (PubMed:16439204, PubMed:16439205, PubMed:17470781). Binds DNA in a length-dependent manner (PubMed:17317666). {ECO:0000269|PubMed:16439204, ECO:0000269|PubMed:16439205, ECO:0000269|PubMed:17317666, ECO:0000269|PubMed:17470781}.; DISEASE: Severe combined immunodeficiency due to NHEJ1 deficiency (NHEJ1-SCID) [MIM:611291]: SCID refers to a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia and low or absent antibody levels. Patients with SCID present in infancy with recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development. NHEJ1-SCID is characterized by a profound T- and B-lymphocytopenia associated with increased cellular sensitivity to ionizing radiation, microcephaly and growth retardation. Some patients may manifest SCID with sensitivity to ionizing radiation without microcephaly and mild growth retardation, probably due to hypomorphic NHEJ1 mutations. {ECO:0000269|PubMed:16439204, ECO:0000269|PubMed:16439205}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving NHEJ1 is found in a patient with polymicrogyria. Translocation t(2;7)(q35;p22). {ECO:0000269|PubMed:12604777}.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:16439204}.; unclassifiable (Anatomical System);cartilage;ovary;colon;parathyroid;skin;whole body;lung;placenta;liver;testis;germinal center;kidney;brain;bladder;mammary gland; . 0.07587 0.07898 0.040529541 57.15380986 382.80607 4.12516 NHLH1 0.640239274537506 0.332020665089661 0.0277400603728324 nescient helix-loop-helix 1 FUNCTION: May serve as DNA-binding protein and may be involved in the control of cell-type determination, possibly within the developing nervous system.; . . unclassifiable (Anatomical System);lung;visual apparatus;pituitary gland;brain; medulla oblongata;spinal cord;temporal lobe;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.37040 0.20312 -0.009020804 52.8544468 14.53159 0.52300 NHLH2 0.537457456619661 0.404760832670278 0.0577817107100603 nescient helix-loop-helix 2 FUNCTION: May serve as DNA-binding protein and may be involved in the control of cell-type determination, possibly within the developing nervous system.; . . unclassifiable (Anatomical System);lung;visual apparatus;hippocampus;brain;retina; dorsal root ganglion;superior cervical ganglion;uterus corpus;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;skin; 0.64351 0.13588 0.12325821 62.38499646 2.03184 0.06623 NHLRC1 0.0360065335308677 0.830381472217118 0.133611994252014 NHL repeat containing E3 ubiquitin protein ligase 1 FUNCTION: E3 ubiquitin-protein ligase. Together with the phosphatase EPM2A/laforin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. In complex with EPM2A/laforin and HSP70, suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Ubiquitinates the glycogen-targeting protein phosphatase subunits PPP1R3C/PTG and PPP1R3D in a laforin-dependent manner and targets them for proteasome-dependent degradation, thus decreasing glycogen accumulation. Polyubiquitinates EPM2A/laforin and ubiquitinates AGL and targets them for proteasome-dependent degradation. Also promotes proteasome-independent protein degradation through the macroautophagy pathway. {ECO:0000269|PubMed:15930137, ECO:0000269|PubMed:17908927, ECO:0000269|PubMed:18070875, ECO:0000269|PubMed:19036738, ECO:0000269|PubMed:21505799, ECO:0000269|PubMed:23624058}.; DISEASE: Epilepsy, progressive myoclonic 2 (EPM2) [MIM:254780]: An autosomal recessive and severe form of adolescent-onset progressive epilepsy. Typically, as seizures increase in frequency, cognitive function declines towards dementia, and affected individuals die usually within 10 years after onset. EPM2 occurs worldwide, but it is particularly common in the mediterranean countries of southern Europe and northern Africa, in southern India and in the Middle East. At the cellular level, it is characterized by accumulation of starch-like polyglucosans called Lafora bodies (LBs) that are most abundant in organs with the highest glucose metabolism: brain, heart, liver and skeletal muscle. Among other conditions involving polyglucosans, EPM2 is unique in that the inclusions are in neuronal dendrites but not axons and the forming polyglucosan fibrils are associated with the endoplasmic reticulum. {ECO:0000269|PubMed:12958597, ECO:0000269|PubMed:15781812, ECO:0000269|PubMed:16021330, ECO:0000269|PubMed:18311786, ECO:0000269|PubMed:21505799}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, cerebellum, spinal cord, medulla, heart, liver, skeletal muscle and pancreas. {ECO:0000269|PubMed:12958597}.; uterus;lung;whole body;heart;islets of Langerhans;skin; pons;trigeminal ganglion;skeletal muscle; 0.24085 0.18321 0.21689899 68.12927577 2230.52751 8.70379 NHLRC2 0.000339054634985002 0.98829225544538 0.0113686899196351 NHL repeat containing 2 . . . . . 0.08465 0.09945 0.665103516 84.6131163 2265.55871 8.79705 NHLRC3 0.00380865629106237 0.956846435831419 0.0393449078775189 NHL repeat containing 3 . . . . . 0.04986 0.09681 0.619191319 83.36282142 219.33709 3.20374 NHLRC4 0.00242750693328775 0.328232934409655 0.669339558657058 NHL repeat containing 4 . . . . . . . 0.103030231 61.2762444 222.85262 3.22795 NHP2 0.0342616850367737 0.824649538855987 0.14108877610724 NHP2 ribonucleoprotein FUNCTION: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ("psi") residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme. {ECO:0000269|PubMed:15044956}.; DISEASE: Dyskeratosis congenita, autosomal recessive, 2 (DKCB2) [MIM:613987]: A rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy. {ECO:0000269|PubMed:18523010}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, colon, heart, kidney, ovary, pancreas, placenta, prostate, skeletal muscle, small intestine, spleen, testis and thymus. Also expressed at lower levels in the liver. {ECO:0000269|PubMed:12020816}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum;thymus; whole brain;cerebellum peduncles;globus pallidus;pons;parietal lobe; 0.60362 0.15588 0.415317661 76.81056853 26.41417 0.85525 NHP2P1 . . . NHP2 ribonucleoprotein pseudogene 1 . . . . . . . . . . . NHP2P2 . . . NHP2 ribonucleoprotein pseudogene 2 . . . . . . . . . . . NHS 0.999461888794772 0.000538108867991715 2.3372366573934e-09 NHS actin remodeling regulator FUNCTION: May function in cell morphology by maintaining the integrity of the circumferential actin ring and controlling lamellipod formation. Involved in the regulation eye, tooth, brain and craniofacial development. {ECO:0000269|PubMed:20332100}.; DISEASE: Cataract 40 (CTRCT40) [MIM:302200]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT40 manifests as a congenital nuclear opacity with severe visual impairment in affected males. Heterozygous females have suture cataracts and only slight reduction in vision. In some cases, cataract is associated with microcornea without any other systemic anomaly or dysmorphism. Microcornea is defined by a corneal diameter inferior to 10 mm in both meridians in an otherwise normal eye. {ECO:0000269|PubMed:19414485}. Note=The disease is caused by mutations affecting the gene represented in this entry. Caused by copy number variations predicted to result in altered transcriptional regulation of the NHS gene: a 0.8 Mb segmental duplication-triplication encompassing the NHS, SCML1 and RAI2 genes, and an 4.8 kb intragenic deletion in NHS intron 1.; TISSUE SPECIFICITY: Detected at low levels in all tissues analyzed. Detected in fetal and adult brain, lens, retina, retinal pigment epithelium, placenta, lymphocytes and fibroblasts. Levels in retinal pigment epithelium, placenta, lymphocytes, and fibroblasts are very low. Expressed also in kidney, lung and thymus. {ECO:0000269|PubMed:14564667, ECO:0000269|PubMed:15466011}.; . . 0.17736 0.14772 -0.725642751 14.24274593 725.51652 5.34764 NHS-AS1 . . . NHS antisense RNA 1 . . . . . . . . . . . NHSL1 . . . NHS like 1 . . TISSUE SPECIFICITY: Widely expressed. Expressed in adult and fetal brain, fetal eyes, adult lens, kidney, liver and intestine. {ECO:0000269|PubMed:15466011}.; ovary;rectum;colon;parathyroid;fovea centralis;choroid;skin;retina;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bone;iris;testis;pineal gland;brain;unclassifiable (Anatomical System);small intestine;cartilage;hypothalamus;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16939 0.08813 1.534092314 95.56499174 516.80632 4.64861 NHSL2 0.812282091450701 0.183093553768422 0.00462435478087669 NHS like 2 . . . . . 0.16714 . . . 884.1075 5.79180 NICN1 0.257245528868092 0.715462857626776 0.0272916135051321 nicolin 1 . . TISSUE SPECIFICITY: High expression level is found in brain, testis, liver and kidney. Weak expression in spleen, leukocytes, small intestine and colon. {ECO:0000269|PubMed:12392556}.; unclassifiable (Anatomical System);lymphoreticular;heart;colon;fovea centralis;skin;skeletal muscle;retina;uterus;prostate;whole body;lung;frontal lobe;nasopharynx;bone;placenta;macula lutea;liver;testis;spleen;kidney;brain;mammary gland;stomach; amygdala;dorsal root ganglion;whole brain;superior cervical ganglion;occipital lobe;temporal lobe;pons;subthalamic nucleus;testis;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.16132 0.10145 -0.161524709 41.6430762 45.91837 1.30346 NICN2P . . . nicolin 2, pseudogene . . . . . . . . . . . NID1 0.000366475613763869 0.999629978391408 3.54599482860533e-06 nidogen 1 FUNCTION: Sulfated glycoprotein widely distributed in basement membranes and tightly associated with laminin. Also binds to collagen IV and perlecan. It probably has a role in cell- extracellular matrix interactions.; . . myocardium;smooth muscle;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; dorsal root ganglion;uterus;fetal liver;superior cervical ganglion;adipose tissue;smooth muscle;placenta;appendix;fetal lung;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.78515 0.35093 0.446303541 77.92521821 4897.5976 14.25037 NID2 6.95346797158758e-07 0.999989562010083 9.7426431201922e-06 nidogen 2 FUNCTION: Cell adhesion glycoprotein which is widely distributed in basement membranes. Binds to collagens I and IV, to perlecan and to laminin 1. Does not bind fibulins. It probably has a role in cell-extracellular matrix interactions.; . TISSUE SPECIFICITY: Heart, placenta and bone. Less in pancreas, kidney and skeletal muscle.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;cochlea;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;spinal cord;urinary;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach; heart;placenta;fetal thyroid; 0.75123 0.20667 3.602297049 99.53408823 1392.55812 6.98260 NIDDM1 . . . non-insulin-dependent diabetes mellitus (common, type 2) 1 . . . . . . . . . . . NIDDM2 . . . non-insulin-dependent diabetes mellitus (common, type 2) 2 . . . . . . . . . . . NIF3L1 0.00517700548052124 0.968729093913037 0.0260939006064414 NGG1 interacting factor 3 like 1 FUNCTION: May function as a transcriptional corepressor through its interaction with COPS2, negatively regulating the expression of genes involved in neuronal differentiation. {ECO:0000250|UniProtKB:Q9EQ80}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; amygdala;whole brain;thalamus;occipital lobe;placenta; 0.04516 0.10937 -0.380166007 27.88393489 2750.43724 9.88777 NIFK . . . nucleolar protein interacting with the FHA domain of MKI67 . . . . . 0.34753 0.09419 -0.315847836 31.68789809 169.61896 2.84174 NIFK-AS1 . . . NIFK antisense RNA 1 . . . . . . . . . . . NIFKP1 . . . nucleolar protein interacting with the FHA domain of MKI67 pseudogene 1 . . . . . . . . . . . NIFKP2 . . . nucleolar protein interacting with the FHA domain of MKI67 pseudogene 2 . . . . . . . . . . . NIFKP3 . . . nucleolar protein interacting with the FHA domain of MKI67 pseudogene 3 . . . . . . . . . . . NIFKP4 . . . nucleolar protein interacting with the FHA domain of MKI67 pseudogene 4 . . . . . . . . . . . NIFKP5 . . . nucleolar protein interacting with the FHA domain of MKI67 pseudogene 5 . . . . . . . . . . . NIFKP6 . . . nucleolar protein interacting with the FHA domain of MKI67 pseudogene 6 . . . . . . . . . . . NIFKP7 . . . nucleolar protein interacting with the FHA domain of MKI67 pseudogene 7 . . . . . . . . . . . NIFKP8 . . . nucleolar protein interacting with the FHA domain of MKI67 pseudogene 8 . . . . . . . . . . . NIFKP9 . . . nucleolar protein interacting with the FHA domain of MKI67 pseudogene 9 . . . . . . . . . . . NIM1K . . . NIM1 serine/threonine protein kinase . . . . . . . -0.556537043 19.72753008 58.77349 1.55556 NIN 8.93549269098595e-06 0.999991064089644 4.17665416311809e-10 ninein FUNCTION: Centrosomal protein required in the positioning and anchorage of the microtubule minus-end in epithelial cells. May also act as a centrosome maturation factor. May play a role in microtubule nucleation. Overexpression does not perturb nucleation or elongation of microtubules but suppresses release of microtubules. {ECO:0000269|PubMed:15190203}.; DISEASE: Seckel syndrome 7 (SCKL7) [MIM:614851]: A rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and mental retardation. {ECO:0000269|PubMed:22933543}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart and skeletal muscle. Isoform 1 is more expressed than isoform 5. {ECO:0000269|PubMed:11004522, ECO:0000269|PubMed:11162463}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;spinal cord;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; . 0.24219 0.17458 0.069649268 59.04694503 2716.57662 9.81907 NINJ1 0.0612939091849242 0.720787414799621 0.217918676015455 ninjurin 1 FUNCTION: Homophilic cell adhesion molecule that promotes axonal growth. May play a role in nerve regeneration and in the formation and function of other tissues. Cell adhesion requires divalent cations.; . TISSUE SPECIFICITY: Widely expressed in both adult and embryonic tissues, primarily those of epithelial origin.; . . 0.09530 0.17630 0.349177632 74.18023119 34.66435 1.05697 NINJ2 0.0201388621613476 0.744209952217455 0.235651185621197 ninjurin 2 FUNCTION: Homophilic cell adhesion molecule that promotes axonal growth. May play a role in nerve regeneration and in the formation and function of other tissues.; . TISSUE SPECIFICITY: Widely expressed. In adult, higher expression in the bone marrow and peripheral blood lymphocytes, medium in the lung, lymph node, thyroid, uterus, thymus, spleen, prostate and skeletal muscle, lower in the liver, placenta, brain, heart and kidney. In embryo, higher expression in the thymus, heart and liver, lower in the spleen, lung, brain and kidney.; unclassifiable (Anatomical System);myocardium;cartilage;ovary;islets of Langerhans;hypothalamus;parathyroid;blood;fovea centralis;skeletal muscle;uterus;pancreas;whole body;lung;bone;placenta;macula lutea;liver;spleen;germinal center;brain; occipital lobe;thalamus;hypothalamus;bone marrow; 0.12837 0.10083 0.038710339 56.92380278 124.44042 2.42650 NINL 3.96830789193205e-33 1.36144093423783e-05 0.999986385590658 ninein like FUNCTION: Involved in the microtubule organization in interphase cells. Overexpression induces the fragmentation of the Golgi, and causes lysosomes to disperse toward the cell periphery; it also interferes with mitotic spindle assembly. May play a role in ovarian carcinogenesis. {ECO:0000269|PubMed:12852856, ECO:0000269|PubMed:16254247, ECO:0000269|PubMed:18538832}.; . TISSUE SPECIFICITY: Expressed in KYSE-150 esophageal carcinoma, HeLa cervical carcinoma and U2OS osteosarcoma cells. Expression is regulated in a cell cycle-dependent manner and peaks during G2/M phase (at protein level). Expressed in fetal heart, skeletal muscle, liver, lung and cochlea, and in adult brain, testis, kidney and retina. {ECO:0000269|PubMed:17403670, ECO:0000269|PubMed:18826961}.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;hypothalamus;sympathetic chain;parathyroid;breast;lung;endometrium;thyroid;visual apparatus;liver;pituitary gland;testis;head and neck;spleen;kidney;brain;cerebellum;peripheral nerve; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . 1.423820054 94.9398443 1402.91031 7.00260 NIP7 0.603152382697747 0.387914564134153 0.00893305316810066 NIP7, nucleolar pre-rRNA processing protein FUNCTION: Required for proper 34S pre-rRNA processing and 60S ribosome subunit assembly. {ECO:0000269|PubMed:22195017}.; . TISSUE SPECIFICITY: Expressed in hematopoietic stem/progenitor cells. {ECO:0000269|PubMed:15522784}.; ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;kidney;mammary gland;stomach; skeletal muscle; 0.19859 0.11357 -0.207437529 38.2814343 16.54614 0.58430 NIP7P1 . . . NIP7, nucleolar pre-rRNA processing protein pseudogene 1 . . . . . . . . . . . NIP7P2 . . . NIP7, nucleolar pre-rRNA processing protein pseudogene 2 . . . . . . . . . . . NIP7P3 . . . NIP7, nucleolar pre-rRNA processing protein pseudogene 3 . . . . . . . . . . . NIPA1 0.214097495852355 0.746506727985289 0.0393957761623563 non imprinted in Prader-Willi/Angelman syndrome 1 FUNCTION: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+) (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in neuronal tissues. {ECO:0000269|PubMed:14508710}.; ovary;colon;parathyroid;fovea centralis;skin;retina;prostate;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;cerebellum;thymus; dorsal root ganglion;temporal lobe;trigeminal ganglion; 0.42378 0.15245 -0.317668748 31.45789101 542.75784 4.74288 NIPA2 0.487193753650621 0.508067405117162 0.00473884123221637 non imprinted in Prader-Willi/Angelman syndrome 2 FUNCTION: Acts as a selective Mg(2+) transporter. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14508708}.; ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;gum;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;adrenal gland;placenta;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;amygdala;occipital lobe;superior cervical ganglion;pons; 0.19107 0.12213 -0.025608647 51.91672564 88.07429 2.00820 NIPA2P1 . . . non imprinted in Prader-Willi/Angelman syndrome 2 pseudogene 1 . . . . . . . . . . . NIPA2P2 . . . non imprinted in Prader-Willi/Angelman syndrome 2 pseudogene 2 . . . . . . . . . . . NIPA2P3 . . . non imprinted in Prader-Willi/Angelman syndrome 2 pseudogene 3 . . . . . . . . . . . NIPA2P4 . . . non imprinted in Prader-Willi/Angelman syndrome 2 pseudogene 4 . . . . . . . . . . . NIPA2P5 . . . non imprinted in Prader-Willi/Angelman syndrome 2 pseudogene 5 . . . . . . . . . . . NIPAL1 3.20929588480326e-09 0.0476042652817047 0.952395731509 NIPA like domain containing 1 FUNCTION: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+), Cu(2+) and Co(2+) but to a much less extent than Mg(2+) (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;whole body;placenta;liver;spleen;brain; dorsal root ganglion;superior cervical ganglion;placenta;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.12886 . 0.595326758 82.66100495 1596.75027 7.39631 NIPAL2 5.79287299169819e-06 0.6804162525285 0.319577954598508 NIPA like domain containing 2 . . . unclassifiable (Anatomical System);heart;ovary;lacrimal gland;parathyroid;blood;skin;skeletal muscle;breast;uterus;prostate;lung;larynx;nasopharynx;placenta;visual apparatus;testis;head and neck;germinal center;kidney;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14747 . 0.194852702 67.03231894 55.49379 1.49687 NIPAL3 0.000454711893618813 0.964781375827042 0.0347639122793392 NIPA like domain containing 3 . . . ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;pineal gland;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus;cerebellum; uterus corpus;superior cervical ganglion;pons;skeletal muscle;cerebellum; 0.26909 0.10159 -0.800872469 12.33191791 56.32941 1.50722 NIPAL4 0.000898828686270022 0.798047148420568 0.201054022893162 NIPA like domain containing 4 FUNCTION: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Ba(2+), Mn(2+), Sr(2+) and Co(2+) but to a much less extent than Mg(2+) (By similarity). May be a receptor for ligands (trioxilins A3 and B3) from the hepoxilin pathway. {ECO:0000250, ECO:0000269|PubMed:15317751}.; . TISSUE SPECIFICITY: Highly expressed in brain, lung, stomach, keratinocytes and leukocytes, and in all other tissues tested except liver, thyroid and fetal brain. {ECO:0000269|PubMed:15317751, ECO:0000269|PubMed:17557927}.; unclassifiable (Anatomical System);uterus;heart;larynx;blood;head and neck;brain;bladder;skin;stomach; ciliary ganglion;atrioventricular node;skeletal muscle; . . 0.132352165 63.48785091 465.33653 4.46847 NIPBL 1 9.20137767442571e-18 1.38152926385215e-43 Nipped-B homolog (Drosophila) FUNCTION: Probably plays a structural role in chromatin. Involved in sister chromatid cohesion, possibly by interacting with the cohesin complex (By similarity). {ECO:0000250}.; DISEASE: Cornelia de Lange syndrome 1 (CDLS1) [MIM:122470]: A form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. Characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies. {ECO:0000269|PubMed:15146185, ECO:0000269|PubMed:15146186, ECO:0000269|PubMed:15318302, ECO:0000269|PubMed:20124326, ECO:0000269|PubMed:20358602, ECO:0000269|PubMed:21934712, ECO:0000269|PubMed:23254390, ECO:0000269|PubMed:25447906}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart, skeletal muscle, fetal and adult liver, fetal and adult kidney. Expressed at intermediates level in thymus, placenta, peripheral leukocyte and small intestine. Weakly or not expressed in brain, colon, spleen and lung. {ECO:0000269|PubMed:15146185, ECO:0000269|PubMed:15146186}.; ovary;umbilical cord;salivary gland;intestine;colon;skin;bone marrow;uterus;whole body;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;adrenal cortex;pharynx;blood;breast;lung;cornea;nasopharynx;placenta;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;medulla oblongata;white blood cells;atrioventricular node;pons;skeletal muscle;uterus;testis - seminiferous tubule;appendix;ciliary ganglion;trigeminal ganglion;whole blood;parietal lobe; 0.94334 0.10487 -2.44943873 1.014390186 759.33568 5.46172 NIPBL-AS1 . . . NIPBL antisense RNA 1 (head to head) . . . . . . . . . . . NIPSNAP1 0.979278956519241 0.0207174999030472 3.54357771222898e-06 nipsnap homolog 1 (C. elegans) . . TISSUE SPECIFICITY: Ubiquitous. Highest expression in liver.; lymphoreticular;smooth muscle;ovary;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;subthalamic nucleus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;pons;kidney;atrioventricular node;cingulate cortex;skeletal muscle;cerebellum; 0.54821 . -0.053113545 49.38664779 15.04047 0.54057 NIPSNAP3A 1.63591359584979e-05 0.428855983104694 0.571127657759348 nipsnap homolog 3A (C. elegans) . . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in liver, kidney and muscle. Expressed at intermediate level in brain, heart, colon, thymus, kidney, small intestine, placenta, lung, leukocytes and spleen. {ECO:0000269|PubMed:12427096}.; . . 0.08666 0.09772 -0.071520315 48.34866714 222.55123 3.22561 NIPSNAP3B 0.0238829678663823 0.914462179846099 0.0616548522875191 nipsnap homolog 3B (C. elegans) . . . . . 0.13687 0.10504 1.350418743 94.35008257 4805.16924 14.05398 NISCH 0.817101389344283 0.182898547141011 6.35147052661531e-08 nischarin FUNCTION: Acts either as the functional imidazoline-1 receptor (I1R) candidate or as a membrane-associated mediator of the I1R signaling. Binds numerous imidazoline ligands that induces initiation of cell-signaling cascades triggering to cell survival, growth and migration. Its activation by the agonist rilmenidine induces an increase in phosphorylation of mitogen-activated protein kinases MAPK1 and MAPK3 in rostral ventrolateral medulla (RVLM) neurons that exhibited rilmenidine-evoked hypotension (By similarity). Blocking its activation with efaroxan abolished rilmenidine-induced mitogen-activated protein kinase phosphorylation in RVLM neurons (By similarity). Acts as a modulator of Rac-regulated signal transduction pathways (By similarity). Suppresses Rac1-stimulated cell migration by interacting with PAK1 and inhibiting its kinase activity (By similarity). Also blocks Pak-independent Rac signaling by interacting with RAC1 and inhibiting Rac1-stimulated NF-kB response element and cyclin D1 promoter activation (By similarity). Inhibits also LIMK1 kinase activity by reducing LIMK1 'Tyr-508' phosphorylation (By similarity). Inhibits Rac-induced cell migration and invasion in breast and colon epithelial cells (By similarity). Inhibits lamellipodia formation, when overexpressed (By similarity). Plays a role in protection against apoptosis. Involved in association with IRS4 in the enhancement of insulin activation of MAPK1 and MAPK3. When overexpressed, induces a redistribution of cell surface ITGA5 integrin to intracellular endosomal structures. {ECO:0000250, ECO:0000269|PubMed:10882231, ECO:0000269|PubMed:12868002, ECO:0000269|PubMed:15028619, ECO:0000269|PubMed:15028621, ECO:0000269|PubMed:15475348}.; . TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 4 are expressed in brain. Isoform 1 is expressed in endocrine tissues. {ECO:0000269|PubMed:15028621, ECO:0000269|PubMed:9851558}.; lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;tonsil;amygdala;heart;cartilage;tongue;urinary;spinal cord;blood;lens;skeletal muscle;visual apparatus;liver;cervix;mammary gland;peripheral nerve;colon;parathyroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;cerebellum; whole brain;amygdala;testis - interstitial;occipital lobe;superior cervical ganglion;cerebellum peduncles;hypothalamus;caudate nucleus;pons;atrioventricular node;prostate;prefrontal cortex;globus pallidus;testis;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.10682 0.15402 -2.309939295 1.197216325 289.95693 3.64314 NIT1 0.000861524962795638 0.935471599080999 0.0636668759562059 nitrilase 1 FUNCTION: Plays a role in cell growth and apoptosis: loss of expression promotes cell growth and resistance to DNA damage stress. Has tumor suppressor properties that enhances the apoptotic responsiveness in cancer cells; this effect is additive to the tumor suppressor activity of FHIT. It is also a negative regulator of primary T-cells. Has apparently no omega-amidase activity such as NIT2 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in heart, brain, placenta, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:9671749}.; . . 0.25171 0.13527 0.150760231 64.51403633 1304.81858 6.79601 NIT2 1.59970723969675e-10 0.0578947231453202 0.942105276694709 nitrilase family member 2 FUNCTION: Has a omega-amidase activity. The role of omega-amidase is to remove potentially toxic intermediates by converting alpha- ketoglutaramate and alpha-ketosuccinamate to biologically useful alpha-ketoglutarate and oxaloacetate, respectively. Overexpression decreases the colony-forming capacity of cultured cells by arresting cells in the G2 phase of the cell cycle. {ECO:0000269|PubMed:17488281, ECO:0000269|PubMed:19595734}.; . TISSUE SPECIFICITY: Detected in fetal brain (at protein level). Ubiquitous. Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, prostate, spleen, thymus, prostate, testis, ovary, small intestine and colon. {ECO:0000269|PubMed:14528910, ECO:0000269|PubMed:17488281}.; . . 0.08988 0.19269 -0.80269335 12.23755603 36.32911 1.08881 NKAIN1 0.615737172831643 0.376214157591412 0.00804866957694434 Na+/K+ transporting ATPase interacting 1 . . . unclassifiable (Anatomical System);retina;whole body;lung;frontal lobe;adrenal gland;placenta;visual apparatus;alveolus;duodenum;testis;mammary gland;brain;peripheral nerve; superior cervical ganglion;fetal brain;cerebellum peduncles;trigeminal ganglion;cerebellum; 0.72245 0.10462 0.058937498 58.26256192 14.50675 0.52125 NKAIN1P1 . . . Na+/K+ transporting ATPase interacting 1 pseudogene 1 . . . . . . . . . . . NKAIN2 0.00783238533852385 0.928062091303548 0.0641055233579282 Na+/K+ transporting ATPase interacting 2 . . TISSUE SPECIFICITY: Expressed in fetal brain. Weakly expressed in adult brain and thymus. Not expressed in any other normal tissue examined. {ECO:0000269|PubMed:11979551}.; . . 0.35628 . -0.163345027 41.24793583 15.60658 0.55645 NKAIN3 0.0101794431862366 0.826063635269787 0.163756921543976 Na+/K+ transporting ATPase interacting 3 . . . . . 0.19069 . 0.237127192 68.98443029 1689.46651 7.57934 NKAIN4 0.0237171845496393 0.772332707947099 0.203950107503262 Na+/K+ transporting ATPase interacting 4 . . . . . 0.09242 . 1.104245073 91.95564992 4413.97067 13.28955 NKAP 0.99551390816983 0.00448568023787944 4.1159229032321e-07 NFKB activating protein FUNCTION: Acts as a transcriptional repressor. Plays a role as a transcriptional corepressor of the Notch-mediated signaling required for T-cell development. Also involved in the TNF and IL-1 induced NF-kappa-B activation. Associates with chromatin at the Notch-regulated SKP2 promoter. {ECO:0000269|PubMed:14550261, ECO:0000269|PubMed:19409814}.; . . . . 0.42748 0.10231 -0.251530012 35.42108988 625.32683 5.04360 NKAPL 0.000165621301014734 0.881026933052885 0.1188074456461 NFKB activating protein like . . . unclassifiable (Anatomical System);heart;pineal body;muscle;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;adrenal gland;macula lutea;pituitary gland;testis;pineal gland; . 0.04673 0.07261 1.817129195 96.96862468 2619.99769 9.59492 NKAPP1 . . . NFKB activating protein pseudogene 1 . . . . . . . . . . . NKD1 0.997929798892685 0.00207013874328632 6.23640285957211e-08 naked cuticle homolog 1 (Drosophila) FUNCTION: Cell autonomous antagonist of the canonical Wnt signaling pathway. May activate a second Wnt signaling pathway that controls planar cell polarity. {ECO:0000269|PubMed:11752446, ECO:0000269|PubMed:15687260, ECO:0000269|PubMed:16567647}.; . TISSUE SPECIFICITY: Expressed in colon, heart, kidney, leukocyte, liver, lung, ovary, pancreas, placenta, prostate, skeletal muscle, small intestine and spleen. {ECO:0000269|PubMed:11604995}.; unclassifiable (Anatomical System);ovary;colon;parathyroid;fovea centralis;choroid;lens;retina;uterus;prostate;optic nerve;lung;endometrium;placenta;macula lutea;visual apparatus;liver;testis;spleen;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.19067 0.16973 -0.822919685 11.76574664 68.69321 1.71640 NKD2 2.35583650240863e-05 0.502435481158655 0.497540960476321 naked cuticle homolog 2 (Drosophila) FUNCTION: Cell autonomous antagonist of the canonical Wnt signaling pathway. May activate a second Wnt signaling pathway that controls planar cell polarity (By similarity). Required for processing of TGFA and for targeting of TGFA to the basolateral membrane of polarized epithelial cells. {ECO:0000250, ECO:0000269|PubMed:15064403, ECO:0000269|PubMed:17553928}.; . TISSUE SPECIFICITY: Expressed in kidney, lung, pancreas and spleen. {ECO:0000269|PubMed:11604995}.; unclassifiable (Anatomical System);heart;blood;fovea centralis;skin;retina;uterus;pancreas;lung;placenta;bone;macula lutea;testis;spleen;mammary gland;brain; adrenal gland; 0.13879 0.10209 . . 216.7969 3.18243 NKG7 0.00400666235764945 0.648963206983579 0.347030130658772 natural killer cell granule protein 7 . . TISSUE SPECIFICITY: Expressed in activated T-cells, in kidney, liver, lung and pancreas. Not expressed in brain, heart, or skeletal muscle. Expressed at high levels in TCR gamma delta- expressing CTL clones, and in some TCR alpha beta-expressing CTL clones (both CD4+ and CD8+), but is not expressed in other TCR alpha beta-expressing CTL clones and in cell lines representing B- cells, monocytes, and myeloid cells.; smooth muscle;ovary;salivary gland;intestine;colon;choroid;skin;bone marrow;prostate;endometrium;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;kidney; lymph node;liver;white blood cells;whole blood;bone marrow; 0.06376 0.09350 0.12689526 63.00424628 131.63164 2.49734 NKILA . . . NF-kappaB interacting long non-coding RNA . . . . . . . . . . . NKIRAS1 0.0348877719884207 0.826778542163431 0.138333685848148 NFKB inhibitor interacting Ras-like 1 FUNCTION: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and mediating cytoplasmic retention of p65/RELA NF-kappa-B subunit. It is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB. {ECO:0000269|PubMed:10657303, ECO:0000269|PubMed:12672800, ECO:0000269|PubMed:15024091}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10657303}.; . . 0.12057 0.11210 -0.075159878 47.78839349 9.80399 0.35907 NKIRAS2 0.063309457660652 0.870105664936667 0.0665848774026805 NFKB inhibitor interacting Ras-like 2 FUNCTION: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and nuclear localization of p65/RELA NF- kappa-B subunit. It is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10657303}.; lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;head and neck;kidney;mammary gland;stomach; liver;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15900 0.11809 -0.207437529 38.2814343 3.24501 0.11703 NKPD1 1.88741865526868e-09 0.0182927553906281 0.981707242721953 NTPase, KAP family P-loop domain containing 1 . . . lung;ovary; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.16964 . . . 1008.34076 6.11624 NKRF 0.955812168094543 0.0440737950650344 0.00011403684042265 NFKB repressing factor FUNCTION: Interacts with a specific negative regulatory element (NRE) 5'-AATTCCTCTGA-3' to mediate transcriptional repression of certain NK-kappa-B responsive genes. Involved in the constitutive silencing of the interferon beta promoter, independently of the virus-induced signals, and in the inhibition of the basal and cytokine-induced iNOS promoter activity. Also involved in the regulation of IL-8 transcription. {ECO:0000269|PubMed:12381793}.; . TISSUE SPECIFICITY: Widely and constitutively expressed. Expressed at lower level in colon, peripheral blood lymphocytes, lung and kidney.; pancreas;hypothalamus;hippocampus;spleen;brain; occipital lobe;prefrontal cortex;globus pallidus;skeletal muscle; 0.48621 0.20971 -0.538132194 20.26421326 17.80669 0.62232 NKS1 . . . natural killer cell susceptibility 1 . . . . . . . . . . . NKTR 0.991877509743874 0.00812249025512626 9.99254202157362e-13 natural killer cell triggering receptor FUNCTION: Component of a putative tumor-recognition complex. Involved in the function of NK cells.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;amygdala;heart;cartilage;tongue;urinary;spinal cord;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;internal ear;placenta;head and neck;kidney;stomach; superior cervical ganglion;uterus corpus;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.48078 0.15418 0.099178678 60.75725407 1233.02574 6.63549 NKX1-1 0.188420302823464 0.646693156936687 0.164886540239849 NK1 homeobox 1 . . TISSUE SPECIFICITY: Expressed in hemopoietic progenitor cells. {ECO:0000269|PubMed:7518789}.; . . . . . . 59.73293 1.56924 NKX1-2 . . . NK1 homeobox 2 FUNCTION: May function in cell specification, particularly in the CNS. {ECO:0000250}.; . . . . . . . . 1240.59153 6.64779 NKX2-1 0.0819264859161676 0.871861122086998 0.0462123919968347 NK2 homeobox 1 FUNCTION: Transcription factor that binds and activates the promoter of thyroid specific genes such as thyroglobulin, thyroperoxidase, and thyrotropin receptor. Crucial in the maintenance of the thyroid differentiation phenotype. May play a role in lung development and surfactant homeostasis. Forms a regulatory loop with GRHL2 that coordinates lung epithelial cell morphogenesis and differentiation. Activates the transcription of GNRHR and plays a role in enhancing the circadian oscillation of its gene expression. Represses the transcription of the circadian transcriptional repressor NR1D1 (By similarity). {ECO:0000250|UniProtKB:P23441, ECO:0000250|UniProtKB:P50220}.; DISEASE: Chorea, hereditary benign (BHC) [MIM:118700]: A rare autosomal dominant movement disorder, defined by early onset in childhood, a stable or non-progressive course of chorea, and no mental deterioration. Chorea is characterized by involuntary, forcible, rapid, jerky movements that may be subtle or become confluent, markedly altering normal patterns of movement. {ECO:0000269|PubMed:11971878, ECO:0000269|PubMed:15955952}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Choreoathetosis and congenital hypothyroidism with or without pulmonary dysfunction (CAHTP) [MIM:610978]: An autosomal dominant disorder that manifests in infancy with neurological disturbances, hypothyroidism, and respiratory problems. It is characterized by movement abnormalities beginning with muscular hypotonia followed by the development of chorea, athetosis, dystonia, ataxia, and dysarthria. {ECO:0000269|PubMed:11854318, ECO:0000269|PubMed:11854319, ECO:0000269|PubMed:15289765, ECO:0000269|PubMed:24714694}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Thyroid and lung.; unclassifiable (Anatomical System);prostate;lung;cartilage;endometrium;thyroid;testis;brain;stomach; superior cervical ganglion;lung;thyroid;fetal lung;fetal thyroid;skeletal muscle; 0.81487 0.52282 1.273147413 93.66595895 44.04874 1.26407 NKX2-1-AS1 . . . NKX2-1 antisense RNA 1 . . . . . . . . . . . NKX2-2 0.337334271714038 0.648129386105543 0.0145363421804189 NK2 homeobox 2 FUNCTION: Acts as a transcriptional activator. Required for the maintenance of NEUROD1 expression in the horomone-producing endocrine cells of the pancreas. May be involved in specifying diencephalic neuromeric boundaries, and in controlling the expression of genes that play a role in axonal guidance. Associates with chromatin at the NEUROD1 promoter region. Binds to a subset of consensus elements within the NEUROD1 promoter (By similarity). {ECO:0000250}.; . . . . 0.48097 0.24974 0.505321956 80.00707714 296.89141 3.67718 NKX2-2-AS1 . . . NKX2-2 antisense RNA 1 . . . . . . . . . . . NKX2-3 0.802089179396299 0.192584953970388 0.00532586663331289 NK2 homeobox 3 FUNCTION: Transcription factor. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;testis;head and neck; . 0.73974 0.20183 . . 41.16019 1.20447 NKX2-4 0.278447692496314 0.63241985839706 0.0891324491066263 NK2 homeobox 4 FUNCTION: Probable transcription factor.; . . myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;bile duct;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.31409 0.13858 . . 15.26552 0.54888 NKX2-5 0.858647741285937 0.139163428944853 0.00218882976921002 NK2 homeobox 5 FUNCTION: Implicated in commitment to and/or differentiation of the myocardial lineage. Acts as a transcriptional activator of ANF in cooperation with GATA4 (By similarity). It is transcriptionally controlled by PBX1 and acts as a transcriptional repressor of CDKN2B (By similarity). It is required for spleen development. {ECO:0000250|UniProtKB:P42582, ECO:0000269|PubMed:22560297}.; DISEASE: Tetralogy of Fallot (TOF) [MIM:187500]: A congenital heart anomaly which consists of pulmonary stenosis, ventricular septal defect, dextroposition of the aorta (aorta is on the right side instead of the left) and hypertrophy of the right ventricle. In this condition, blood from both ventricles (oxygen-rich and oxygen-poor) is pumped into the body often causing cyanosis. {ECO:0000269|PubMed:10587520, ECO:0000269|PubMed:11714651, ECO:0000269|PubMed:14607454}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Conotruncal heart malformations (CTHM) [MIM:217095]: A group of congenital heart defects involving the outflow tracts. Examples include truncus arteriosus communis, double-outlet right ventricle and transposition of great arteries. Truncus arteriosus communis is characterized by a single outflow tract instead of a separate aorta and pulmonary artery. In transposition of the great arteries, the aorta arises from the right ventricle and the pulmonary artery from the left ventricle. In double outlet of the right ventricle, both the pulmonary artery and aorta arise from the right ventricle. {ECO:0000269|PubMed:14607454, ECO:0000269|PubMed:17891434}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hypothyroidism, congenital, non-goitrous, 5 (CHNG5) [MIM:225250]: A non-autoimmune condition characterized by resistance to thyroid-stimulating hormone (TSH) leading to increased levels of plasma TSH and low levels of thyroid hormone. CHNG5 presents variable severity depending on the completeness of the defect. Most patients are euthyroid and asymptomatic, with a normal sized thyroid gland. Only a subset of patients develop hypothyroidism and present a hypoplastic thyroid gland. {ECO:0000269|PubMed:16418214}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ventricular septal defect 3 (VSD3) [MIM:614432]: A common form of congenital cardiovascular anomaly that may occur alone or in combination with other cardiac malformations. It can affect any portion of the ventricular septum, resulting in abnormal communications between the two lower chambers of the heart. Classification is based on location of the communication, such as perimembranous, inlet, outlet (infundibular), central muscular, marginal muscular, or apical muscular defect. Large defects that go unrepaired may give rise to cardiac enlargement, congestive heart failure, pulmonary hypertension, Eisenmenger's syndrome, delayed fetal brain development, arrhythmias, and even sudden cardiac death. {ECO:0000269|PubMed:21110066, ECO:0000269|PubMed:21165553}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hypoplastic left heart syndrome 2 (HLHS2) [MIM:614435]: A syndrome due to defective development of the aorta proximal to the entrance of the ductus arteriosus, and hypoplasia of the left ventricle and mitral valve. As a result of the abnormal circulation, the ductus arteriosus and foramen ovale are patent and the right atrium, right ventricle, and pulmonary artery are enlarged. {ECO:0000269|PubMed:14607454, ECO:0000269|PubMed:15810002}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed only in the heart.; unclassifiable (Anatomical System);lung;liver;duodenum;testis;colon;head and neck;brain; subthalamic nucleus;heart;ciliary ganglion;trigeminal ganglion;cingulate cortex;bone marrow; 0.62436 0.47891 -0.095386216 46.48502005 88.0871 2.00890 NKX2-6 0.00352254257656912 0.392026087233783 0.604451370189648 NK2 homeobox 6 FUNCTION: Acts as a transcriptional activator (PubMed:15649947). In conjunction with NKX2-5, may play a role in both pharyngeal and cardiac embryonic development. {ECO:0000250|UniProtKB:P43688, ECO:0000269|PubMed:15649947}.; DISEASE: Conotruncal heart malformations (CTHM) [MIM:217095]: A group of congenital heart defects involving the outflow tracts. Examples include truncus arteriosus communis, double-outlet right ventricle and transposition of great arteries. Truncus arteriosus communis is characterized by a single outflow tract instead of a separate aorta and pulmonary artery. In transposition of the great arteries, the aorta arises from the right ventricle and the pulmonary artery from the left ventricle. In double outlet of the right ventricle, both the pulmonary artery and aorta arise from the right ventricle. {ECO:0000269|PubMed:15649947, ECO:0000269|PubMed:24421281, ECO:0000269|PubMed:25195019, ECO:0000269|PubMed:25380965}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System); . 0.05676 0.10591 . . 141.44844 2.59472 NKX2-8 0.243402674501059 0.643712174783966 0.112885150714975 NK2 homeobox 8 . . . uterus;lung;testis;brain; atrioventricular node;trigeminal ganglion; 0.11517 0.10751 . . 107.29647 2.24663 NKX3-1 0.000884340872180055 0.563460739330189 0.435654919797631 NK3 homeobox 1 FUNCTION: Transcription factor, which binds preferentially the consensus sequence 5'-TAAGT[AG]-3' and can behave as a transcriptional repressor. Plays an important role in normal prostate development, regulating proliferation of glandular epithelium and in the formation of ducts in prostate. Acts as a tumor suppressor controlling prostate carcinogenesis, as shown by the ability to inhibit proliferation and invasion activities of PC-3 prostate cancer cells. {ECO:0000269|PubMed:19462257}.; . TISSUE SPECIFICITY: Highly expressed in the prostate and, at a lower level, in the testis. {ECO:0000269|PubMed:9226374, ECO:0000269|PubMed:9537602}.; unclassifiable (Anatomical System);prostate;skeletal muscle; dorsal root ganglion;testis - interstitial;superior cervical ganglion;medulla oblongata;atrioventricular node;pons;skeletal muscle;prostate;trachea;testis - seminiferous tubule;appendix;testis;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.46205 0.15429 . . 170.68976 2.84987 NKX3-2 0.0584925207834858 0.713863808445759 0.227643670770756 NK3 homeobox 2 FUNCTION: Transcriptional repressor that acts as a negative regulator of chondrocyte maturation. PLays a role in distal stomach development; required for proper antral-pyloric morphogenesis and development of antral-type epithelium. In concert with GSC, defines the structural components of the middle ear; required for tympanic ring and gonium development and in the regulation of the width of the malleus (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at highest levels in cartilage, bone (osteosarcoma) and gut (small intestine and colon), whereas moderate expression is seen in trachea and brain. Expressed in visceral mesoderm and embryonic skeleton. {ECO:0000269|PubMed:20004766}.; . . 0.28515 0.14063 . . 66.07302 1.67505 NKX6-1 0.501554506769164 0.478986787192358 0.0194587060384781 NK6 homeobox 1 FUNCTION: Transcription factor which binds to specific A/T-rich DNA sequences in the promoter regions of a number of genes. Involved in transcriptional regulation in islet beta cells. Binds to the insulin promoter and is involved in regulation of the insulin gene. Together with NKX2-2 and IRX3 acts to restrict the generation of motor neurons to the appropriate region of the neural tube. Belongs to the class II proteins of neuronal progenitor factors, which are induced by SHH signals (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Pancreatic beta cells.; islets of Langerhans; superior cervical ganglion;skeletal muscle; 0.21345 0.25687 . . 58.71686 1.55334 NKX6-2 0.0134613071846023 0.665957387071743 0.320581305743655 NK6 homeobox 2 . . TISSUE SPECIFICITY: Highest expression in brain. {ECO:0000269|PubMed:11210186}.; . . 0.33405 0.16815 . . 67.16099 1.69568 NKX6-3 0.190054225881154 0.64693957917436 0.163006194944486 NK6 homeobox 3 FUNCTION: Putative transcription factor, which may be involved in patterning of central nervous system and pancreas. {ECO:0000250}.; . . . . 0.15538 . 0.457594962 78.16112291 94.30015 2.09006 NLE1 0.0539875179436926 0.945164267787533 0.000848214268774512 notchless homolog 1 (Drosophila) FUNCTION: Plays a role in regulating Notch activity. Plays a role in regulating the expression of CDKN1A and several members of the Wnt pathway, probably via its effects on Notch activity. Required during embryogenesis for inner mass cell survival (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;islets of Langerhans;colon;skin;skeletal muscle;prostate;lung;endometrium;thyroid;placenta;visual apparatus;liver;testis;spleen;cervix;kidney;brain;mammary gland;stomach; superior cervical ganglion;tumor;ciliary ganglion; 0.26927 0.20307 0.310540264 72.65864591 748.33609 5.42671 NLGN1 0.755797511974091 0.24411687026759 8.5617758319247e-05 neuroligin 1 FUNCTION: Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Required to maintain wakefulness quality and normal synchrony of cerebral cortex activity during wakefulness and sleep. {ECO:0000250|UniProtKB:Q99K10}.; . TISSUE SPECIFICITY: Expressed in the blood vessel walls (at protein level). Detected in brain, and at lower levels in pancreas islet beta cells. {ECO:0000269|PubMed:18755801, ECO:0000269|PubMed:19926856}.; unclassifiable (Anatomical System);smooth muscle;hypothalamus;fovea centralis;choroid;lens;skin;retina;optic nerve;whole body;lung;frontal lobe;placenta;macula lutea;visual apparatus;testis;kidney;brain; amygdala;superior cervical ganglion;occipital lobe;prefrontal cortex;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.34175 0.13453 -1.397999468 4.193205945 58.37576 1.54762 NLGN1-AS1 . . . NLGN1 antisense RNA 1 . . . . . . . . . . . NLGN2 0.992624700343966 0.00737391257704089 1.38707899332909e-06 neuroligin 2 FUNCTION: Transmembrane scaffolding protein involved in cell-cell interactions via its interactions with neurexin family members. Mediates cell-cell interactions both in neurons and in other types of cells, such as Langerhans beta cells. Plays a role in synapse function and synaptic signal transmission, especially via gamma- aminobutyric acid receptors (GABA(A) receptors). Functions by recruiting and clustering synaptic proteins. Promotes clustering of postsynaptic GABRG2 and GPHN. Modulates signaling by inhibitory synapses, and thereby plays a role in controlling the ratio of signaling by excitatory and inhibitory synapses and information processing. Required for normal signal amplitude from inhibitory synapses, but is not essential for normal signal frequency. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. Mediates cell-cell interactions between Langerhans beta cells and modulates insulin secretion (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the blood vessel walls. Detected in colon, brain and pancreas islets of Langerhans (at protein level). Detected in brain, and at lower levels in pancreas islet beta cells. {ECO:0000269|PubMed:18755801, ECO:0000269|PubMed:19926856}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;larynx;thyroid;bone;pituitary gland;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;lens;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;mammary gland;stomach; . 0.30972 0.11262 -1.023168368 7.944090587 110.83072 2.29420 NLGN3 0.896227168388092 0.103570017870681 0.000202813741227002 neuroligin 3 FUNCTION: Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and may mediate its effects by clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. May also play a role in glia-glia or glia-neuron interactions in the developing peripheral nervous system (By similarity). {ECO:0000250, ECO:0000269|PubMed:15620359}.; DISEASE: Asperger syndrome, X-linked, 1 (ASPGX1) [MIM:300494]: A syndrome with features similar to autism. Affected individuals exhibit qualitative impairment in social interaction, as manifest by impairment in the use of non-verbal behaviors such as eye-to- eye gaze, facial expression, body postures, and gestures, failure to develop appropriate peer relationships, and lack of social sharing or reciprocity. Patients also exhibit restricted, repetitive and stereotyped patterns of behavior, interests, and activities, including abnormal preoccupation with certain activities and inflexible adherence to routines or rituals. Asperger syndrome is primarily distinguished from autism by the higher cognitive abilities and a more normal and timely development of language and communicative phrases. {ECO:0000269|PubMed:12669065}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the blood vessel walls (at protein level). Detected in throughout the brain and in spinal cord. Detected in brain, and at lower levels in pancreas islet beta cells. {ECO:0000269|PubMed:10767552, ECO:0000269|PubMed:18755801, ECO:0000269|PubMed:19926856}.; unclassifiable (Anatomical System);amygdala;cerebellum cortex;hypothalamus;retina;prostate;lung;frontal lobe;endometrium;placenta;hippocampus;liver;testis;brain; globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.53317 0.21177 -0.53631094 20.53550366 33.9705 1.04312 NLGN4X 0.932298559009719 0.0676335693083231 6.78716819574591e-05 neuroligin 4, X-linked FUNCTION: Putative neuronal cell surface protein involved in cell- cell-interactions.; DISEASE: Asperger syndrome, X-linked, 2 (ASPGX2) [MIM:300497]: A syndrome with features similar to autism. Affected individuals exhibit qualitative impairment in social interaction, as manifest by impairment in the use of non-verbal behaviors such as eye-to- eye gaze, facial expression, body postures, and gestures, failure to develop appropriate peer relationships, and lack of social sharing or reciprocity. Patients also exhibit restricted, repetitive and stereotyped patterns of behavior, interests, and activities, including abnormal preoccupation with certain activities and inflexible adherence to routines or rituals. Asperger syndrome is primarily distinguished from autism by the higher cognitive abilities and a more normal and timely development of language and communicative phrases. {ECO:0000269|PubMed:14963808}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at highest levels in heart. Expressed at lower levels in liver, skeletal muscle and pancreas and at very low levels in brain. {ECO:0000269|PubMed:11368788}.; unclassifiable (Anatomical System);amygdala;cartilage;heart;ovary;islets of Langerhans;parathyroid;skin;skeletal muscle;retina;uterus;breast;prostate;whole body;lung;placenta;visual apparatus;duodenum;liver;spinal ganglion;brain;bladder;thymus; whole brain;amygdala;dorsal root ganglion;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.81566 0.22678 -0.844966979 11.1759849 301.91426 3.70106 NLGN4Y 0.645547566883988 0.32786714316938 0.0265852899466319 neuroligin 4, Y-linked FUNCTION: Putative neuronal cell surface protein involved in cell- cell-interactions.; . TISSUE SPECIFICITY: Expressed in fetal and adult brain, prostate and testis. {ECO:0000269|PubMed:12815422}.; unclassifiable (Anatomical System);amygdala;heart;ovary;cartilage;parathyroid;vein;skeletal muscle;retina;bone marrow;pancreas;prostate;lung;placenta;visual apparatus;pituitary gland;testis;spleen;kidney;brain; superior cervical ganglion; 0.23279 . . . 12.46737 0.45319 NLGN4Y-AS1 . . . NLGN4Y antisense RNA 1 . . . . . . . . . . . NLK 0.998934346648365 0.00106564099666598 1.23549687860426e-08 nemo-like kinase FUNCTION: Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Activation of this pathway causes binding to and phosphorylation of the histone methyltransferase SETDB1. The NLK- SETDB1 complex subsequently interacts with PPARG, leading to methylation of PPARG target promoters at histone H3K9 and transcriptional silencing. The resulting loss of PPARG target gene transcription inhibits adipogenesis and promotes osteoblastogenesis in mesenchymal stem cells (MSCs). Negative regulator of the canonical Wnt/beta-catenin signaling pathway. Binds to and phosphorylates TCF7L2/TCF4 and LEF1, promoting the dissociation of the TCF7L2/LEF1/beta-catenin complex from DNA, as well as the ubiquitination and subsequent proteolysis of LEF1. Together these effects inhibit the transcriptional activation of canonical Wnt/beta-catenin target genes. Negative regulator of the Notch signaling pathway. Binds to and phosphorylates NOTCH1, thereby preventing the formation of a transcriptionally active ternary complex of NOTCH1, RBPJ/RBPSUH and MAML1. Negative regulator of the MYB family of transcription factors. Phosphorylation of MYB leads to its subsequent proteolysis while phosphorylation of MYBL1 and MYBL2 inhibits their interaction with the coactivator CREBBP. Other transcription factors may also be inhibited by direct phosphorylation of CREBBP itself. Acts downstream of IL6 and MAP3K7/TAK1 to phosphorylate STAT3, which is in turn required for activation of NLK by MAP3K7/TAK1. Upon IL1B stimulus, cooperates with ATF5 to activate the transactivation activity of C/EBP subfamily members. Phosphorylates ATF5 but also stabilizes ATF5 protein levels in a kinase-independent manner (PubMed:25512613). {ECO:0000250|UniProtKB:O54949, ECO:0000269|PubMed:12482967, ECO:0000269|PubMed:14960582, ECO:0000269|PubMed:15004007, ECO:0000269|PubMed:15764709, ECO:0000269|PubMed:17952062, ECO:0000269|PubMed:20061393, ECO:0000269|PubMed:20118921, ECO:0000269|PubMed:20874444, ECO:0000269|PubMed:21454679, ECO:0000269|PubMed:25512613}.; . . . . 0.96706 0.16306 -0.494039303 22.09247464 16.84134 0.59320 NLN 3.59597227684907e-07 0.985541392010036 0.0144582483927363 neurolysin FUNCTION: Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;brain;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;heart;adrenal cortex;pharynx;blood;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;cervix;kidney;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.39163 0.14364 -0.354480518 29.42911064 1132.42209 6.41990 NLRC3 1.03344697218477e-12 0.0780522905374355 0.921947709461531 NLR family, CARD domain containing 3 FUNCTION: May modulate T-cell activation. Decreases the transcription of genes that are normally up-regulated after T-cell stimulation. Delays degradation of NFKBIA/IKBA. {ECO:0000269|PubMed:15705585}.; . TISSUE SPECIFICITY: Detected in peripheral blood mononuclear cells. {ECO:0000269|PubMed:15705585}.; ovary;parathyroid;fovea centralis;skin;uterus;prostate;whole body;endometrium;bone;lymph;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;adrenal cortex;blood;lung;placenta;macula lutea;liver;spleen;kidney;stomach; superior cervical ganglion;placenta;ciliary ganglion;trigeminal ganglion; 0.14525 0.11201 . . . . NLRC4 4.35115119359313e-08 0.812547999873244 0.187451956615244 NLR family, CARD domain containing 4 FUNCTION: Key component of inflammasomes that indirectly senses specific proteins from pathogenic bacteria and fungi and responds by assembling an inflammasome complex that promotes caspase-1 activation, cytokine production and macrophage pyroptosis. {ECO:0000269|PubMed:15107016}.; DISEASE: Autoinflammation with infantile enterocolitis (AIFEC) [MIM:616050]: An autosomal dominant disorder characterized by neonatal-onset enterocolitis, periodic fever, and fatal or near- fatal episodes of autoinflammation. Affected individuals tend to have poor overall growth and gastrointestinal symptoms in infancy, recurrent febrile episodes with splenomegaly, and sometimes hematologic disturbances, arthralgias, or myalgias. {ECO:0000269|PubMed:25217959, ECO:0000269|PubMed:25217960}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Familial cold autoinflammatory syndrome 4 (FCAS4) [MIM:616115]: A form of autoinflammatory syndrome, a rare autosomal dominant systemic disease characterized by recurrent episodes of maculopapular rash associated with arthralgias, myalgias, fever and chills, swelling of the extremities, and conjunctivitis after generalized exposure to cold. {ECO:0000269|PubMed:25385754}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 2 is expressed ubiquitously, although highly expressed in lung and spleen. Isoform 1 is highly expressed in lung, followed by leukocytes especially monocytes, lymph node, colon, brain, prostate, placenta, spleen, bone marrow and fetal liver. Isoform 4 is only detected in brain.; unclassifiable (Anatomical System);pancreas;lung;cerebellum cortex;islets of Langerhans;liver;testis;spleen;blood;kidney;bladder; . 0.12366 0.32056 -0.595174814 18.21184242 68.31876 1.71047 NLRC5 6.71793792873124e-05 0.999932817837553 2.78316003125497e-09 NLR family, CARD domain containing 5 FUNCTION: Probable regulator of the NF-kappa-B and type I interferon signaling pathways. May also regulate the type II interferon signaling pathway. Plays a role in homeostatic control of innate immunity and in antiviral defense mechanisms. {ECO:0000269|PubMed:20061403, ECO:0000269|PubMed:20434986}.; . TISSUE SPECIFICITY: Expressed in spleen, thymus, lung, brain, tonsil, heart and prostate. {ECO:0000269|PubMed:20061403, ECO:0000269|PubMed:20434986}.; ovary;colon;skin;bone marrow;uterus;prostate;larynx;bone;thyroid;testis;germinal center;spinal ganglion;bladder;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;skeletal muscle;breast;pancreas;lung;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;globus pallidus;white blood cells;atrioventricular node;trigeminal ganglion; 0.07927 0.08967 0.514279338 80.30195801 898.09245 5.83754 NLRP1 2.07780022793946e-12 0.949551161552522 0.0504488384454007 NLR family, pyrin domain containing 1 FUNCTION: As the sensor component of the NLRP1 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of NLRP1, CASP1, and possibly PYCARD. Recruitement of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP1 inflammasome is also required for HMGB1 secretion. The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death (PubMed:22665479, PubMed:17418785). May be activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, in a NOD2-dependent manner (PubMed:18511561). Contrary to its mouse ortholog, not activated by Bacillus anthracis lethal toxin (PubMed:19651869). It is unclear whether isoform 2 is involved in inflammasome formation. It is not cleaved within the FIIND domain, does not assemble into specks, nor promote IL1B release (PubMed:22665479). However, in an vitro cell-free system, it has been shown to be activated by MDP (PubMed:17349957). Binds ATP (PubMed:11113115, PubMed:15212762). {ECO:0000250|UniProtKB:A1Z198, ECO:0000269|PubMed:11113115, ECO:0000269|PubMed:15212762, ECO:0000269|PubMed:17349957, ECO:0000269|PubMed:17418785, ECO:0000269|PubMed:18511561, ECO:0000269|PubMed:19651869, ECO:0000269|PubMed:22665479}.; DISEASE: Vitiligo-associated multiple autoimmune disease 1 (VAMAS1) [MIM:606579]: A disorder characterized by the association of vitiligo with several autoimmune and autoinflammatory diseases including autoimmune thyroid disease, rheumatoid arthritis and systemic lupus erythematosus. {ECO:0000269|PubMed:17377159}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Corneal intraepithelial dyskeratosis and ectodermal dysplasia (CIDED) [MIM:615225]: A disease characterized by keratopathy with neovascularization, bilateral corneal opacification, palmoplantar hyperkeratosis, dyshidrosis, and dystrophic nails. {ECO:0000269|PubMed:23349227}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed (PubMed:11113115, PubMed:17164409). Abundantly expressed in primary immune cells (isoform 1 and isoform 2), including in neutrophils, monocytes/macrophages, dendritic cells (mostly Langerhans cells), and B- and T-lymphocytes (at protein level) (PubMed:15285719, PubMed:17164409). Strongly expressed in epithelial cells lining the glandular epithelium, such as that of the gastrointestinal tract (stomach, small intestine, colon), the respiratory tract (trachea and bronchi), and the endometrial and endocervical glands, gallbladder, prostate, and breast (at protein level). In testis, expressed in spermatogonia and primary spermatocytes, but not in Sertoli cells (at protein level). In the brain, expressed in neurons, in particular in pyramidal ones and in oligodendrocytes, but not detected in microglia (at protein level) (PubMed:17164409). Expressed in adult and fetal ocular tissues, including in adult and 24-week old fetal choroid, sclera, cornea, and optic nerve, as well as in adult retina and fetal retina/retinal pigment epithelium (PubMed:23349227). {ECO:0000269|PubMed:11113115, ECO:0000269|PubMed:15285719, ECO:0000269|PubMed:17164409, ECO:0000269|PubMed:23349227}.; unclassifiable (Anatomical System);lymph node;cartilage;urinary;blood;skin;bone marrow;uterus;lung;larynx;nasopharynx;placenta;thyroid;bone;liver;head and neck;germinal center;stomach;thymus; dorsal root ganglion;superior cervical ganglion;lymph node;white blood cells;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle; 0.06255 . 2.710374887 98.94432649 2525.66979 9.37408 NLRP2 1.8750543162871e-20 0.00299768137519909 0.997002318624801 NLR family, pyrin domain containing 2 FUNCTION: Suppresses TNF- and CD40-induced NFKB1 activity at the level of the IKK complex, by inhibiting NFKBIA degradation induced by TNF. When associated with PYCARD, activates CASP1, leading to the secretion of mature proinflammatory cytokine IL1B. May be a component of the inflammasome, a protein complex which also includes PYCARD, CARD8 and CASP1 and whose function would be the activation of proinflammatory caspases. {ECO:0000269|PubMed:15456791}.; . TISSUE SPECIFICITY: Expressed at high levels in lung, placenta and thymus and at lower levels in ovary, intestine and brain. {ECO:0000269|PubMed:15456791}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;lens;breast;lung;epididymis;placenta;macula lutea;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;placenta;testis;pons;atrioventricular node; 0.84299 0.12808 1.199631139 92.95824487 1690.10482 7.58061 NLRP2P . . . NLR family, pyrin domain containing 2 pseudogene FUNCTION: May function as a negative regulator of NF-kappa-B by preventing RELA/p65 phosphorylation at 'Ser-536', thereby inhibiting its transcriptional activity. Through NF-kappa-B regulation may control cytokine release upon Toll-like receptors activation and therefore play a role in modulation of innate immunity. May also play a role in cell cycle progression and apoptotic process. {ECO:0000269|PubMed:24871464}.; . TISSUE SPECIFICITY: Expressed in all tissues tested, including spleen, lymph node, thymus, tonsil, peripheral blood leukocyte, bone marrow, liver, heart, brain, placenta, lung, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:24871464}.; . . 0.25519 0.12490 -0.0274281 51.65723048 . . NLRP3 0.447262679111629 0.552726293142197 1.1027746174155e-05 NLR family, pyrin domain containing 3 FUNCTION: As the sensor component of the NLRP3 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of NLRP3, PYCARD and CASP1 (and possibly CASP4 and CASP5). Recruitement of proCASP1 to the inflammasome promotes its activation and CASP1- catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP3 inflammasome is also required for HMGB1 secretion (PubMed:22801494). The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death. Under resting conditions, NLRP3 is autoinhibited. NLRP3 activation stimuli include extracellular ATP, reactive oxygen species, K(+) efflux, crystals of monosodium urate or cholesterol, beta-amyloid fibers, environmental or industrial particles and nanoparticles, etc. However, it is unclear what constitutes the direct NLRP3 activator. Independently of inflammasome activation, regulates the differentiation of T helper 2 (Th2) cells and has a role in Th2 cell-dependent asthma and tumor growth (By similarity). During Th2 differentiation, required for optimal IRF4 binding to IL4 promoter and for IRF4-dependent IL4 transcription. Binds to the consensus DNA sequence 5'- GRRGGNRGAG-3'. May also participate in the transcription of IL5, IL13, GATA3, CCR3, CCR4 and MAF (By similarity). {ECO:0000250|UniProtKB:Q8R4B8, ECO:0000269|PubMed:22801494, ECO:0000305|PubMed:23305783}.; DISEASE: Familial cold autoinflammatory syndrome 1 (FCAS1) [MIM:120100]: A rare autosomal dominant systemic inflammatory disease characterized by recurrent episodes of maculopapular rash associated with arthralgias, myalgias, fever and chills, swelling of the extremities, and conjunctivitis after generalized exposure to cold. Rarely, some patients may also develop late-onset renal amyloidosis. {ECO:0000269|PubMed:11687797, ECO:0000269|PubMed:11992256, ECO:0000269|PubMed:12355493, ECO:0000269|PubMed:12522564, ECO:0000269|PubMed:15593220, ECO:0000269|PubMed:17284928, ECO:0000269|PubMed:24952504}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Muckle-Wells syndrome (MWS) [MIM:191900]: A hereditary periodic fever syndrome characterized by fever, chronic recurrent urticaria, arthralgias, progressive sensorineural deafness, and reactive renal amyloidosis. The disease may be severe if generalized reactive amyloidosis occurs. {ECO:0000269|PubMed:11687797, ECO:0000269|PubMed:11992256, ECO:0000269|PubMed:12355493, ECO:0000269|PubMed:15593220, ECO:0000269|PubMed:24952504}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Chronic infantile neurologic cutaneous and articular syndrome (CINCA) [MIM:607115]: Rare congenital inflammatory disorder characterized by a triad of neonatal onset of cutaneous symptoms, chronic meningitis, and joint manifestations with recurrent fever and inflammation. {ECO:0000269|PubMed:12032915, ECO:0000269|PubMed:12483741, ECO:0000269|PubMed:14630794, ECO:0000269|PubMed:15231984, ECO:0000269|PubMed:15334500, ECO:0000269|PubMed:15593220, ECO:0000269|PubMed:24952504}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in macrophages. Also expressed in dendritic cells, B- and T-cells (at protein level) (PubMed:11786556) (PubMed:17164409). Expressed in LPS-treated granulocytes, but not in resting cells (at protein level) (PubMed:17164409). Expression in monocytes is very weak (at protein level) (PubMed:17164409). Expressed in stratified non- keratinizing squamous epithelium, including oral, esophageal and ectocervical mucosa and in the Hassall's corpuscles in the thymus. Also, detected in the stratified epithelium covering the bladder and ureter (transitional mucosa) (at protein level) (PubMed:17164409). Expressed in chondrocytes (PubMed:12032915). Expressed at low levels in resting osteoblasts (PubMed:17907925). {ECO:0000269|PubMed:11786556, ECO:0000269|PubMed:12032915, ECO:0000269|PubMed:17164409, ECO:0000269|PubMed:17907925}.; unclassifiable (Anatomical System);lung;liver;testis;colon;spleen;blood;brain; subthalamic nucleus;superior cervical ganglion;appendix;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.41725 0.10512 -0.946125119 9.377211607 78.62534 1.87076 NLRP3P1 . . . NLR family, pyrin domain containing 3 pseudogene 1 . . . . . . . . . . . NLRP4 5.15963125034554e-05 0.992920234388579 0.00702816929891764 NLR family, pyrin domain containing 4 FUNCTION: May be involved in inflammation and recognition of cytosolic pathogen-associated molecular patterns (PAMPs) not intercepted by membrane-bound receptors. Acts as a negative regulator of the type I interferon signaling pathway by serving as an adapter to promote DTX4-mediated ubiquitination of activated TBK1, and its subsequent degradation. Suppresses NF-kappaB induction by the cytokines TNFA and IL1B, suggesting that it operates at a point of convergence in these two cytokine signaling pathways. {ECO:0000269|PubMed:12093792, ECO:0000269|PubMed:22388039}.; . . unclassifiable (Anatomical System);lymph node;bone;placenta;testis;germinal center;tonsil; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; 0.07498 0.09698 0.216698013 67.92285916 73.01576 1.78351 NLRP5 1.2399666413552e-07 0.997190143532511 0.00280973247082509 NLR family, pyrin domain containing 5 FUNCTION: As a member of the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions. {ECO:0000250}.; . TISSUE SPECIFICITY: Oocyte-specific.; . . 0.05999 . 0.179893931 66.1358811 2994.59421 10.38714 NLRP6 . . . NLR family, pyrin domain containing 6 FUNCTION: As the sensor component of the NLRP6 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of NLRP6, PYCARD and CASP1 (and possibly CASP4 and CASP5). Recruitement of proCASP1 to the inflammasome promotes its activation and CASP1- catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. The precise NLRP6 activation stimulus has not been identified yet (By similarity) (PubMed:12387869). Essential for gut mucosal self-renewal and proliferation. Maintains intestinal homeostasis and a healthy intestinal microbiota. This function is, at least partially, mediated by IL18, and not IL1B, produced by nonhematopoietic cells. Influences intestinal barrier function and microbial homeostasis through the regulation of goblet cell mucus secretion. Acts by promoting autophagy in goblet cells, an essential step for mucus granule exocytosis. Its role in goblet cell physiology is inflammasome- dependent, but IL1B- and IL18-independent. During systemic bacterial infections, may negatively regulate inflammatory signaling and inhibit the influx of monocytes and neutrophils to the circulation and to the peritoneum. May promote peripheral nerve recovery following injury via an inflammasome-independent mechanism (By similarity). {ECO:0000250|UniProtKB:Q91WS2, ECO:0000250|UniProtKB:Q96P20, ECO:0000269|PubMed:12387869}.; . TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes, predominantly in granulocytes and, at lower levels, in CD4(+) and CD8(+) T cells. Expressed in colonic myofibroblasts (at protein level) (PubMed:21593405). {ECO:0000269|PubMed:12387869, ECO:0000269|PubMed:21593405}.; unclassifiable (Anatomical System);trabecular meshwork;colon; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.13321 0.11045 1.271321208 93.65416372 1076.87015 6.29039 NLRP7 1.09578252131213e-12 0.150540998794787 0.849459001204118 NLR family, pyrin domain containing 7 FUNCTION: Inhibits CASP1/caspase-1-dependent IL1B secretion. {ECO:0000269|PubMed:15817483}.; DISEASE: Hydatidiform mole, recurrent, 1 (HYDM1) [MIM:231090]: A disorder characterized by excessive trophoblast development that produces a growing mass of tissue inside the uterus at the beginning of a pregnancy. It leads to abnormal pregnancies with no embryo, and cystic degeneration of the chorionic villi. {ECO:0000269|PubMed:16462743, ECO:0000269|PubMed:19246479}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in numerous tissues including uterus and ovary, with low levels in heart and brain. Not detected in skeletal muscle. {ECO:0000269|PubMed:15817483, ECO:0000269|PubMed:16462743}.; unclassifiable (Anatomical System);lymphoreticular;medulla oblongata;trophoblast;lung;epididymis;nasopharynx;skin;tonsil; . 0.06942 0.12139 0.326933865 73.11866006 142.92313 2.60603 NLRP8 1.26212772903126e-18 0.00259981789592667 0.997400182104073 NLR family, pyrin domain containing 8 FUNCTION: Involved in inflammation. {ECO:0000305}.; . . . . 0.06985 0.08291 1.881347656 97.25171031 919.5136 5.89411 NLRP9 5.6781831723167e-17 0.00659052435199195 0.993409475648008 NLR family, pyrin domain containing 9 FUNCTION: Involved in inflammation. {ECO:0000305}.; . . unclassifiable (Anatomical System);uterus;prostate;endometrium;germinal center;bone marrow; . 0.08152 0.08232 -0.101059488 45.67704647 299.47541 3.69014 NLRP9P1 . . . NLR family, pyrin domain containing 9 pseudogene 1 . . . . . . . . . . . NLRP10 5.09582300313282e-12 0.00775464286254946 0.992245357132355 NLR family, pyrin domain containing 10 FUNCTION: Inhibits autoprocessing of CASP1, CASP1-dependent IL1B secretion, PYCARD aggregation and PYCARD-mediated apoptosis but not apoptosis induced by FAS or BID. Displays anti-inflammatory activity. Plays a role in adaptive immunity through control of dendritic cell-mediated transport of antigen to the lymph nodes from peripheral sites. Required for immunity against C.albicans infection. Involved in the innate immune response by contributing to proinflammatory cytokine release in response to invasive bacterial infection. {ECO:0000269|PubMed:15096476, ECO:0000269|PubMed:20393137, ECO:0000269|PubMed:22672233}.; . TISSUE SPECIFICITY: Highly expressed in basal and suprabasal epidermal cell layers with lower levels in dermal fibroblast cells (at protein level). Widely expressed with highest levels in heart, brain and skeletal muscle. Also expressed in liver, colon, dermis and epidermis. Little expression detected in myeloid cells or peripheral blood mononuclear cells. {ECO:0000269|PubMed:15096476, ECO:0000269|PubMed:22672233}.; placenta; dorsal root ganglion;skeletal muscle; 0.11535 0.10299 0.047806932 57.51946214 421.81177 4.29074 NLRP11 3.91867923050963e-06 0.988470738531499 0.0115253427892703 NLR family, pyrin domain containing 11 FUNCTION: Involved in inflammation. {ECO:0000305}.; . . lymph node;bone;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04487 0.06561 -0.297664722 32.27176221 559.29309 4.80353 NLRP12 3.14396082720475e-27 8.08678631622353e-06 0.999991913213684 NLR family, pyrin domain containing 12 FUNCTION: May mediate activation of CASP1 via ASC and promote activation of NF-kappa-B via IKK.; DISEASE: Familial cold autoinflammatory syndrome 2 (FCAS2) [MIM:611762]: A rare autosomal dominant systemic inflammatory disease characterized by recurrent episodes of maculopapular rash associated with arthralgias, myalgias, fever and chills, swelling of the extremities, and conjunctivitis after generalized exposure to cold. {ECO:0000269|PubMed:18230725}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected only in peripheral blood leukocytes, predominantly in eosinophils and granulocytes, and at lower levels in monocytes. {ECO:0000269|PubMed:11167794}.; unclassifiable (Anatomical System);lung;cartilage;placenta;blood;mammary gland;stomach;bone marrow; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.12567 . -0.44655933 24.21561689 3345.45185 11.08055 NLRP13 5.16423954441725e-14 0.0947748366268572 0.905225163373091 NLR family, pyrin domain containing 13 FUNCTION: Involved in inflammation. {ECO:0000305}.; . . . . 0.04573 0.08030 0.060545906 58.26845954 442.50965 4.37930 NLRP14 9.14864568100148e-23 0.000130215666848176 0.999869784333152 NLR family, pyrin domain containing 14 FUNCTION: May be involved in inflammation and spermatogenesis.; . . aorta; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05911 0.13911 1.789458545 96.88016042 2775.09442 9.94440 NLRX1 9.83505664629216e-22 0.000273996406761091 0.999726003593239 NLR family member X1 FUNCTION: Participates in antiviral signaling. Acts as a negative regulator of MAVS-mediated antiviral responses, through the inhibition of the virus-induced RLH (RIG-like helicase)-MAVS interaction (PubMed:18200010). Has no inhibitory function on NF- Kappa-B and type 1 interferon signaling pathways, but enhances NF- Kappa-B and JUN N-terminal kinase dependent signaling through the production of reactive oxygen species (PubMed:18219313). {ECO:0000269|PubMed:18200010, ECO:0000269|PubMed:18219313}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Strongest expression in mammary gland, heart and muscle. Detected in HeLa, HEK293T, THP-1, HL-60, Raji and Jurkat cell lines (at protein level). {ECO:0000269|PubMed:15952891, ECO:0000269|PubMed:18200010, ECO:0000269|PubMed:18219313}.; medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;epididymis;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; trigeminal ganglion; 0.09449 0.13433 0.192828665 66.58410002 983.19891 6.05225 NM . . . neutrophil migration . . . . . . . . . . . NMB 0.156904105323652 0.775545962661086 0.0675499320152614 neuromedin B FUNCTION: Stimulates smooth muscle contraction in a manner similar to that of bombesin.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;thyroid;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.30873 . 0.413500896 76.67492333 1096.45075 6.33695 NMBR 0.000742388919470671 0.525872445884738 0.473385165195792 neuromedin B receptor FUNCTION: Receptor for neuromedin-B.; . TISSUE SPECIFICITY: Expressed in epididymis (at protein level). {ECO:0000269|PubMed:20736409}.; unclassifiable (Anatomical System);lung;testis;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.18003 0.10439 0.468503535 78.79806558 1320.72182 6.83548 NMD3 4.4226191654738e-05 0.991223131334922 0.00873264247342328 NMD3 ribosome export adaptor FUNCTION: Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit. {ECO:0000269|PubMed:12724356, ECO:0000269|PubMed:12773398}.; . . colon;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;oesophagus;larynx;bone;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;skeletal muscle;breast;bile duct;lung;adrenal gland;nasopharynx;placenta;alveolus;hypopharynx;liver;cervix;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07893 0.10797 -0.512444034 21.55579146 81.92408 1.91851 NMD3P1 . . . NMD3 ribosome export adaptor pseudogene 1 . . . . . . . . . . . NMD3P2 . . . NMD3 ribosome export adaptor pseudogene 2 . . . . . . . . . . . NME1 0.00777448651598859 0.781534012997115 0.210691500486896 NME/NM23 nucleoside diphosphate kinase 1 FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein- coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair. {ECO:0000269|PubMed:12628186, ECO:0000269|PubMed:16818237, ECO:0000269|PubMed:8810265}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in heart, brain, placenta, lung, liver, skeletal muscle, pancreas, spleen and thymus. Expressed in lung carcinoma cell lines but not in normal lung tissues. Isoform 2 is ubiquitously expressed and its expression is also related to tumor differentiation. Isoform 3 is ubiquitously expressed. {ECO:0000269|PubMed:10512675, ECO:0000269|PubMed:12601555, ECO:0000269|PubMed:16442775}.; lymphoreticular;smooth muscle;umbilical cord;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;iris;bladder;brain;tonsil;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;synovium;bone;testis;pineal gland;unclassifiable (Anatomical System);trophoblast;lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; . . 0.46077 -0.119252484 44.53880632 3.03238 0.11019 NME1-NME2 0.010430774313355 0.945152217753745 0.0444170079328997 NME1-NME2 readthrough FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752). Exhibits histidine protein kinase activity. {ECO:0000269|PubMed:15249197, ECO:0000269|PubMed:20946858, ECO:0000269|PubMed:8392752}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:16442775}.; . . . . -0.361761279 28.6329323 . . NME1P1 . . . NME/NM23 nucleoside diphosphate kinase 1 pseudogene 1 . . . . . . . . . . . NME2 0.010430774313355 0.945152217753745 0.0444170079328997 NME/NM23 nucleoside diphosphate kinase 2 FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752). Exhibits histidine protein kinase activity. {ECO:0000269|PubMed:15249197, ECO:0000269|PubMed:20946858, ECO:0000269|PubMed:8392752}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:16442775}.; . . . 0.46077 -0.185391282 39.67916962 29.95472 0.95674 NME2P1 . . . NME/NM23 nucleoside diphosphate kinase 2 pseudogene 1 FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity). {ECO:0000250}.; . . myocardium;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;pituitary gland;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;lung;cornea;nasopharynx;placenta;visual apparatus;alveolus;hypopharynx;liver;head and neck;kidney;mammary gland; . 0.12487 . . . . . NME3 2.37397506636629e-06 0.0865042031310129 0.913493422893921 NME/NM23 nucleoside diphosphate kinase 3 FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis.; . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;spleen;kidney;mammary gland;stomach; whole brain;prostate;thyroid;white blood cells; 0.27797 0.18492 . . 94.46567 2.09186 NME4 0.134065501683573 0.780061241391203 0.0858732569252242 NME/NM23 nucleoside diphosphate kinase 4 FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Through the catalyzed exchange of gamma- phosphate between di- and triphosphonucleosides participates in regulation of intracellular nucleotide homeostasis (PubMed:10799505). Binds to anionic phospholipids, predominantly to cardiolipin; the binding inhibits its phosphotransfer activity (PubMed:18635542, PubMed:23150663). Acts as mitochondria-specific NDK; its association with cardiolipin-containing mitochondrial inner membrane is coupled to respiration suggesting that ADP locally regenerated in the mitochondrion innermembrane space by its activity is directly taken up via ANT ADP/ATP translocase into the matrix space to stimulate respiratory ATP regeneration (PubMed:18635542). Proposed to increase GTP-loading on dynamin- related GTPase OPA1 in mitochondria (PubMed:24970086). In vitro can induce liposome cross-linking suggesting that it can cross- link inner and outer membranes to form contact sites, and promotes intermembrane migration of anionic phosphoplipids. Promotes the redistribution of cardiolipin between the mitochondrial inner membrane and outer membrane which is implicated in pro-apoptotic signaling (PubMed:18635542, PubMed:17028143, PubMed:23150663). {ECO:0000269|PubMed:10799505, ECO:0000269|PubMed:17028143, ECO:0000269|PubMed:18635542, ECO:0000269|PubMed:23150663, ECO:0000305, ECO:0000305|PubMed:24970086}.; . TISSUE SPECIFICITY: Widely distributed. Found at very high levels in prostate, heart, liver, small intestine, and skeletal muscle tissues, and in low amounts in the brain and in blood leukocytes.; medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;oesophagus;larynx;bone;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; prostate;liver; 0.15047 0.14883 -0.538132194 20.26421326 17.60529 0.61668 NME5 0.570640716006077 0.417771698486597 0.0115875855073256 NME/NM23 family member 5 FUNCTION: Does not seem to have NDK kinase activity. Confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes including Gpx5. May play a role in spermiogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in testis germinal cells.; unclassifiable (Anatomical System);meninges;heart;ovary;lacrimal gland;adrenal cortex;parathyroid;skin;uterus;pancreas;pia mater;whole body;lung;frontal lobe;visual apparatus;testis;dura mater;kidney; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;pons;trigeminal ganglion;skeletal muscle; 0.16576 . 0.3032669 72.009908 28.15255 0.90228 NME6 9.2163606322478e-05 0.789133812913842 0.210774023479835 NME/NM23 nucleoside diphosphate kinase 6 FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Inhibitor of p53-induced apoptosis.; . TISSUE SPECIFICITY: Expressed at a moderately low level in many tissues. Most abundant in kidney, prostate, ovary, intestine, and spleen.; unclassifiable (Anatomical System);lymph node;ovary;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;breast;prostate;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;kidney;brain;bladder;aorta; . 0.08133 0.09292 -0.405853867 26.23260203 22.60901 0.75660 NME7 0.00352847685132706 0.986892214562281 0.00957930858639145 NME/NM23 family member 7 FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.; . . . . 0.84867 0.13229 -0.47017169 23.25430526 105.29339 2.22138 NME8 2.02524932547695e-21 0.00155662067506793 0.998443379324932 NME/NM23 family member 8 FUNCTION: Probably required during the final stages of sperm tail maturation in the testis and/or epididymis, where extensive disulfide bonding of fibrous sheath (FS) proteins occurs. May be involved in the reduction of disulfide bonds within the sperm FS components. In vitro, it has neither NDP kinase nor reducing activity on disulfide bonds.; DISEASE: Ciliary dyskinesia, primary, 6 (CILD6) [MIM:610852]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:17360648}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Testis-specific. Expressed only in primary spermatocytes and round spermatids. {ECO:0000269|PubMed:11737268}.; . . 0.04717 0.10719 0.468503535 78.79806558 2237.38652 8.72361 NME9 2.62520678425012e-05 0.762167869459032 0.237805878473125 NME/NM23 family member 9 FUNCTION: May be a regulator of microtubule physiology.; . TISSUE SPECIFICITY: Detected at very low levels in testis, lung and brain. {ECO:0000269|PubMed:12569107}.; uterus;unclassifiable (Anatomical System);prostate;lung;islets of Langerhans;nasopharynx;thyroid;hypopharynx;head and neck;bladder;retina; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; 0.09393 0.09655 0.373041938 75.29488087 92.30584 2.06641 NMI 6.22629202890385e-09 0.069682364569707 0.930317629204001 N-myc and STAT interactor FUNCTION: May be involved in augmenting coactivator protein recruitment to a group of sequence-specific transcription factors. Augments cytokine-mediated STAT transcription. Enhances CBP/p300 coactivator protein recruitment to STAT1 and STAT5.; . TISSUE SPECIFICITY: Expressed in all adult and fetal tissues except brain and skin. More abundant in fetal tissues especially liver.; smooth muscle;ovary;umbilical cord;colon;skin;uterus;prostate;cochlea;endometrium;bone;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;cartilage;islets of Langerhans;blood;skeletal muscle;bile duct;pancreas;pia mater;lung;nasopharynx;placenta;alveolus;cervix;kidney;mammary gland;stomach; superior cervical ganglion;white blood cells;whole blood; 0.73060 0.10082 -0.492218069 22.35786742 33.89416 1.04199 NMNAT1 0.22529193858776 0.738984467515519 0.0357235938967218 nicotinamide nucleotide adenylyltransferase 1 FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NaAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+). Protects against axonal degeneration following mechanical or toxic insults. {ECO:0000269|PubMed:17402747}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in skeletal muscle, heart and kidney. Also expressed in the liver pancreas and placenta. Widely expressed throughout the brain. {ECO:0000269|PubMed:11027696, ECO:0000269|PubMed:11891043}.; . . 0.14901 . 0.148941568 64.31941496 34.67179 1.05754 NMNAT1P1 . . . NMNAT1 pseudogene 1 . . . . . . . . . . . NMNAT1P2 . . . NMNAT1 pseudogene 2 . . . . . . . . . . . NMNAT1P3 . . . NMNAT1 pseudogene 3 . . . . . . . . . . . NMNAT1P4 . . . NMNAT1 pseudogene 4 . . . . . . . . . . . NMNAT1P5 . . . NMNAT1 pseudogene 5 . . . . . . . . . . . NMNAT2 0.943848445340391 0.056109249112936 4.23055466732985e-05 nicotinamide nucleotide adenylyltransferase 2 FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency. Cannot use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NaAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+). {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}.; . TISSUE SPECIFICITY: Highly expressed in brain, in particular in cerebrum, cerebellum, occipital lobe, frontal lobe, temporal lobe and putamen. Also found in the heart, skeletal muscle, pancreas and islets of Langerhans. {ECO:0000269|PubMed:12359228, ECO:0000269|PubMed:14516279, ECO:0000269|PubMed:16118205}.; unclassifiable (Anatomical System);meninges;cartilage;ovary;colon;parathyroid;blood;skin;skeletal muscle;retina;bone marrow;bile duct;pia mater;lung;frontal lobe;cochlea;thyroid;placenta;liver;pituitary gland;testis;dura mater;kidney;brain;stomach;cerebellum; amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.61231 0.13362 -0.029247611 51.40363293 1726.91284 7.66799 NMNAT3 5.34376100617257e-08 0.0667221280175402 0.93327781854485 nicotinamide nucleotide adenylyltransferase 3 FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, can use NAD(+), NADH, NaAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+). Protects against axonal degeneration following injury. {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}.; . TISSUE SPECIFICITY: Expressed in lung and spleen with lower levels in placenta and kidney. {ECO:0000269|PubMed:12574164, ECO:0000269|PubMed:16118205}.; unclassifiable (Anatomical System);islets of Langerhans;colon;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;prostate;optic nerve;lung;larynx;macula lutea;visual apparatus;liver;testis;head and neck;spleen;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.29917 0.13272 0.084621747 60.31493277 62.22081 1.60926 NMRAL1 0.000731170681969894 0.759536947034358 0.239731882283672 NmrA-like family domain containing 1 FUNCTION: Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer. {ECO:0000269|PubMed:17496144, ECO:0000269|PubMed:18263583, ECO:0000269|PubMed:19254724}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;visual apparatus;alveolus;liver;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; liver; 0.14728 0.11106 -0.066061882 48.77919321 592.47958 4.93227 NMRK1 0.00106636786756072 0.827244463839378 0.171689168293061 nicotinamide riboside kinase 1 FUNCTION: Catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN). The enzyme also phosphorylates the antitumor drugs tiazofurin and 3- deazaguanosine. {ECO:0000269|PubMed:15137942}.; . . . . 0.06630 0.10289 0.837848571 88.22835574 81.00692 1.90472 NMRK2 1.16630399616328e-07 0.103948737069836 0.896051146299764 nicotinamide riboside kinase 2 FUNCTION: Catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN). Reduces laminin matrix deposition and cell adhesion to laminin, but not to fibronectin. Involved in the regulation of PXN at the protein level and of PXN tyrosine phosphorylation. May play a role in the regulation of terminal myogenesis. {ECO:0000269|PubMed:10613898, ECO:0000269|PubMed:15137942}.; . TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and, at a much lower level, in the heart (at protein level). No expression in brain, kidney, liver, lung, pancreas nor placenta. {ECO:0000269|PubMed:10613898}.; . . 0.47100 0.14229 0.240763792 69.36777542 244.945 3.37613 NMS 2.78112452887771e-10 0.0419121086648981 0.95808789105699 neuromedin S FUNCTION: Implicated in the regulation of circadian rhythms through autocrine and/or paracrine actions. {ECO:0000250}.; . . . . 0.08170 0.12880 0.25917371 70.05779665 1820.09065 7.86854 NMT1 0.998500520689071 0.00149947356308185 5.74784700265837e-09 N-myristoyltransferase 1 FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. {ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:9353336, ECO:0000269|PubMed:9506952}.; . TISSUE SPECIFICITY: Heart, gut, kidney, liver and placenta.; lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;oesophagus;larynx;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;mesenchyma;nasopharynx;placenta;head and neck;kidney;stomach;aorta; superior cervical ganglion;thalamus;subthalamic nucleus;testis - interstitial;medulla oblongata;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.60291 0.10471 -0.560178693 19.30879925 14.72014 0.53052 NMT2 0.317678321422733 0.682172975290269 0.000148703286998297 N-myristoyltransferase 2 FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. {ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:9506952}.; . . . . 0.10625 0.09225 -0.205617011 38.57631517 25.86293 0.84175 NMTRL-TAA1-1 . . . nuclear-encoded mitochondrial transfer RNA-Leu (TAA) 1-1 . . . . . . . . . . . NMTRL-TAA2-1 . . . nuclear-encoded mitochondrial transfer RNA-Leu (TAA) 2-1 . . . . . . . . . . . NMTRL-TAA3-1 . . . nuclear-encoded mitochondrial transfer RNA-Leu (TAA) 3-1 . . . . . . . . . . . NMTRL-TAA4-1 . . . nuclear-encoded mitochondrial transfer RNA-Leu (TAA) 4-1 . . . . . . . . . . . NMTRL-TAA5-1 . . . nuclear-encoded mitochondrial transfer RNA-Leu (TAA) 5-1 . . . . . . . . . . . NMTRL-TAA6-1 . . . nuclear-encoded mitochondrial transfer RNA-Leu (TAA) 6-1 . . . . . . . . . . . NMTRP-TGG1-1 . . . nuclear-encoded mitochondrial transfer RNA-Pro (TGG) 1-1 . . . . . . . . . . . NMTRQ-CTG1-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (CTG) 1-1 . . . . . . . . . . . NMTRQ-TTG1-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (TTG) 1-1 . . . . . . . . . . . NMTRQ-TTG2-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (TTG) 2-1 . . . . . . . . . . . NMTRQ-TTG3-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (TTG) 3-1 . . . . . . . . . . . NMTRQ-TTG4-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (TTG) 4-1 . . . . . . . . . . . NMTRQ-TTG5-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (TTG) 5-1 . . . . . . . . . . . NMTRQ-TTG6-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (TTG) 6-1 . . . . . . . . . . . NMTRQ-TTG7-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (TTG) 7-1 . . . . . . . . . . . NMTRQ-TTG8-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (TTG) 8-1 . . . . . . . . . . . NMTRQ-TTG9-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (TTG) 9-1 . . . . . . . . . . . NMTRQ-TTG10-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (TTG) 10-1 . . . . . . . . . . . NMTRQ-TTG11-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (TTG) 11-1 . . . . . . . . . . . NMTRQ-TTG12-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (TTG) 12-1 . . . . . . . . . . . NMTRQ-TTG13-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (TTG) 13-1 . . . . . . . . . . . NMTRQ-TTG14-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (TTG) 14-1 . . . . . . . . . . . NMTRQ-TTG15-1 . . . nuclear-encoded mitochondrial transfer RNA-Gln (TTG) 15-1 . . . . . . . . . . . NMTRS-TGA1-1 . . . nuclear-encoded mitochondrial transfer RNA-Ser (TGA) 1-1 . . . . . . . . . . . NMTRS-TGA2-1 . . . nuclear-encoded mitochondrial transfer RNA-Ser (TGA) 2-1 . . . . . . . . . . . NMTRS-TGA3-1 . . . nuclear-encoded mitochondrial transfer RNA-Ser (TGA) 3-1 . . . . . . . . . . . NMTRV-TAC1-1 . . . nuclear-encoded mitochondrial transfer RNA-Val (TAC) 1-1 . . . . . . . . . . . NMU 0.00893184170488053 0.936761208597597 0.0543069496975226 neuromedin U FUNCTION: Stimulates muscle contractions of specific regions of the gastrointestinal tract. In humans, NmU stimulates contractions of the ileum and urinary bladder.; . TISSUE SPECIFICITY: Expressed throughout the enteric nervous system with highest levels being found in the jejunum.; unclassifiable (Anatomical System);lymph node;lung;ovary;hypothalamus;thyroid;testis;colon;cervix;blood;head and neck;brain;stomach; whole brain;tongue;tumor; 0.41619 . 0.481458261 79.03986789 1181.8687 6.52536 NMUR1 1.07262381171516e-05 0.352148783341033 0.647840490420849 neuromedin U receptor 1 FUNCTION: Receptor for the neuromedin-U and neuromedin-S neuropeptides. {ECO:0000250, ECO:0000269|PubMed:10899166}.; . TISSUE SPECIFICITY: Expressed in greatest abundance in peripheral organs, particularly in elements of the gastrointestinal and urogenital systems with highest levels in testes. In central nervous system structures express levels are much lower than those seen in peripheral organs. Within the CNS, has been detected in highest abundance in the cerebellum, dorsal root ganglia, hippocampus, and spinal cord. {ECO:0000269|PubMed:10899166, ECO:0000269|PubMed:9782091}.; unclassifiable (Anatomical System);optic nerve;bone;spleen;skeletal muscle; superior cervical ganglion;temporal lobe;trigeminal ganglion;skeletal muscle; 0.10873 . 0.266447942 70.5826846 611.83006 4.99915 NMUR2 0.421657260997351 0.570605939899117 0.00773679910353184 neuromedin U receptor 2 FUNCTION: Receptor for the neuromedin-U and neuromedin-S neuropeptides. {ECO:0000250, ECO:0000269|PubMed:10899166}.; . TISSUE SPECIFICITY: Predominantly expressed in the CNS, particularly in the medulla oblongata, pontine reticular formation, spinal cord, and thalamus. High level in testis whereas lower levels are present in a variety of peripheral tissues including the gastrointestinal tract, genitourinary tract, liver, pancreas, adrenal gland, thyroid gland, lung, trachea, spleen and thymus. {ECO:0000269|PubMed:10887190, ECO:0000269|PubMed:10894543, ECO:0000269|PubMed:10899166, ECO:0000269|PubMed:11010960}.; unclassifiable (Anatomical System);uterus;heart;testis;brain;skin;stomach; . 0.11625 0.10378 1.376101648 94.5329087 2423.32741 9.14747 NNAT 0.112567959949874 0.777831553498789 0.109600486551337 neuronatin FUNCTION: May participate in the maintenance of segment identity in the hindbrain and pituitary development, and maturation or maintenance of the overall structure of the nervous system. May function as a regulatory subunit of ion channels.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;thyroid;pituitary gland;testis;germinal center;brain;bladder;amygdala;unclassifiable (Anatomical System);heart;tongue;hypothalamus;pharynx;blood;lens;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;aorta; whole brain;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;globus pallidus;parietal lobe;cingulate cortex;pituitary; 0.49738 . 0.079165051 59.43029016 1.1333 0.03098 NNMT 0.00427916395502723 0.663036560776022 0.332684275268951 nicotinamide N-methyltransferase FUNCTION: Catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is important for biotransformation of many drugs and xenobiotic compounds.; . TISSUE SPECIFICITY: Predominantly expressed in the liver. A lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. Not detected in the brain or pancreas.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;choroid;skin;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;alveolus;liver;cervix;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; superior cervical ganglion;adipose tissue;smooth muscle;heart;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.47129 0.20232 -0.47017169 23.25430526 26.41448 0.85552 NNO1 . . . nanophthalmos 1 . . . . . . . . . . . NNT 0.99955047731355 0.000449522673957905 1.24921717048606e-11 nicotinamide nucleotide transhydrogenase FUNCTION: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane. May play a role in reactive oxygen species (ROS) detoxification in the adrenal gland. {ECO:0000269|PubMed:22634753}.; . TISSUE SPECIFICITY: Widely expressed with expression most readily detectable in adrenal, heart, kidney, thyroid and adipose tissues. {ECO:0000269|PubMed:22634753}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;atrium;cochlea;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;hippocampus;amnion;liver;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;occipital lobe;globus pallidus;skeletal muscle; 0.37225 0.09181 -0.394936437 27.02878037 828.99367 5.64434 NNT-AS1 . . . NNT antisense RNA 1 . . . . . . . . . . . NOA1 0.000579556702703894 0.994079859319422 0.00534058397787376 nitric oxide associated 1 FUNCTION: Involved in regulation of mitochondrial protein translation and respiration. Plays a role in mitochondria-mediated cell death. May act as a scaffolding protein or stabilizer of respiratory chain supercomplexes. Binds GTP. {ECO:0000269|PubMed:19103604}.; . . ovary;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.05900 0.07572 0.464864541 78.69190847 949.48768 5.96632 NOB1 8.61136358207129e-08 0.292883366995587 0.707116546890777 NIN1/RPN12 binding protein 1 homolog FUNCTION: May play a role in mRNA degradation.; . TISSUE SPECIFICITY: Detected in liver, lung, placenta, endothelial cells and spleen. {ECO:0000269|PubMed:16172919, ECO:0000269|PubMed:1791827}.; lymphoreticular;medulla oblongata;ovary;skin;retina;prostate;optic nerve;endometrium;gum;thyroid;iris;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.12273 . -0.154246007 42.22694032 2859.41631 10.11657 NOBOX 3.74460520566748e-05 0.826163299243734 0.173799254704209 NOBOX oogenesis homeobox FUNCTION: Transcription factor which may play a role in oogenesis. Binds preferentially to the DNA sequences 5'-TAATTG-3', 5'-TAGTTG- 3' and 5'-TAATTA-3' (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in ovaries, testes and pancreas. Expressed within all stages of the adult female germline, from primordial follicles through to MII oocytes. {ECO:0000269|PubMed:16597639}.; . . . . . . 2025.04128 8.27730 NOC2L 1.33038194561114e-19 0.0025628417280481 0.997437158271952 NOC2 like nucleolar associated transcriptional repressor FUNCTION: Acts as an inhibitor of histone acetyltransferase activity; prevents acetylation of all core histones by the EP300/p300 histone acetyltransferase at p53/TP53-regulated target promoters in a histone deacetylases (HDAC)-independent manner. Acts as a transcription corepressor of p53/TP53- and TP63-mediated transactivation of the p21/CDKN1A promoter. Involved in the regulation of p53/TP53-dependent apoptosis. Associates together with TP63 isoform TA*-gamma to the p21/CDKN1A promoter. {ECO:0000269|PubMed:16322561, ECO:0000269|PubMed:20123734, ECO:0000269|PubMed:20959462}.; . . unclassifiable (Anatomical System);prostate;epididymis;larynx;testis;colon;head and neck;choroid;stomach; . 0.24042 0.13894 0.036678689 56.26916726 783.46189 5.53337 NOC2LP1 . . . NOC2 like nucleolar associated transcriptional repressor pseudogene 1 . . . . . . . . . . . NOC2LP2 . . . NOC2 like nucleolar associated transcriptional repressor pseudogene 2 . . . . . . . . . . . NOC3L 1.14013419227493e-06 0.999421494124096 0.000577365741711336 NOC3 like DNA replication regulator FUNCTION: May be required for adipogenesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in colon, heart, kidney, liver, lung, placenta, skeletal muscle, small intestine, spleen and thymus. {ECO:0000269|PubMed:15564382}.; . . 0.38194 0.09807 2.13680094 97.95352678 5112.17074 14.69156 NOC4L . . . nucleolar complex associated 4 homolog . . . medulla oblongata;ovary;sympathetic chain;colon;skin;retina;bone marrow;uterus;endometrium;bone;iris;pituitary gland;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;blood;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node; 0.54310 0.11298 -1.280491183 5.16631281 149.35551 2.66469 NOCT . . . nocturnin FUNCTION: Circadian deadenylase which plays an important role in post-transcriptional regulation of metabolic genes under circadian control. Degrades poly(A) tails of specific target mRNAs leading to their degradation and suppression of translation. Exerts a rhythmic post-transcriptional control of genes necessary for metabolic functions including nutrient absorption, glucose/insulin sensitivity, lipid metabolism, adipogenesis, inflammation and osteogenesis. Plays an important role in favoring adipogenesis over osteoblastogenesis and acts as a key regulator of the adipogenesis/osteogenesis balance. Promotes adipogenesis by activating PPARG transcriptional activity in a deadenylase- independent manner by facilitating its nuclear translocation. Regulates circadian expression of NOS2 in the liver and negatively regulates the circadian expression of IGF1 in the bone. Critical for proper development of early embryos (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Adipose tissue. Expression is higher in subcutaneous adipose tissue as compared to visceral adipose tissue. {ECO:0000269|PubMed:22331129}.; . . 0.27107 0.17200 0.062575634 58.74026893 . . NOD1 5.05414452036266e-13 0.0517942861460554 0.948205713853439 nucleotide binding oligomerization domain containing 1 FUNCTION: Enhances caspase-9-mediated apoptosis. Induces NF-kappa- B activity via RIPK2 and IKK-gamma. Confers responsiveness to intracellular bacterial lipopolysaccharides (LPS). Forms an intracellular sensing system along with ARHGEF2 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIPK2 dependent NF-kappa-B signaling pathway activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides but also in the activation of NF-kappa-B by Shigella effector proteins IpgB2 and OspB. Recruits NLRP10 to the cell membrane following bacterial infection. {ECO:0000269|PubMed:11058605, ECO:0000269|PubMed:17054981, ECO:0000269|PubMed:19043560, ECO:0000269|PubMed:22672233}.; . TISSUE SPECIFICITY: Highly expressed in adult heart, skeletal muscle, pancreas, spleen and ovary. Also detected in placenta, lung, liver, kidney, thymus, testis, small intestine and colon.; ovary;colon;skin;bone marrow;uterus;whole body;larynx;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;blood;skeletal muscle;pancreas;lung;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;stomach; temporal lobe;ciliary ganglion;skin; 0.09284 0.26053 -0.455627566 23.72611465 3999.69559 12.51514 NOD2 5.52076952261577e-19 0.00307648971441875 0.996923510285581 nucleotide binding oligomerization domain containing 2 FUNCTION: Involved in gastrointestinal immunity. Upon stimulation by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, binds the proximal adapter receptor-interacting RIPK2, which recruits ubiquitin ligases as XIAP, BIRC2, BIRC3 and the LUBAC complex, triggering activation of MAP kinases and activation of NF-kappa-B signaling. This in turn leads to the transcriptional activation of hundreds of genes involved in immune response. Required for MDP-induced NLRP1-dependent CASP1 activation and IL1B release in macrophages (PubMed:18511561). {ECO:0000269|PubMed:18511561, ECO:0000269|PubMed:23806334}.; DISEASE: Blau syndrome (BLAUS) [MIM:186580]: A rare autosomal dominant disorder characterized by early-onset granulomatous arthritis, uveitis and skin rash. {ECO:0000269|PubMed:11528384, ECO:0000269|PubMed:15812565, ECO:0000269|PubMed:19116920, ECO:0000269|PubMed:19169908, ECO:0000269|PubMed:19479837, ECO:0000269|PubMed:20199415, ECO:0000269|PubMed:24960071, ECO:0000269|PubMed:25093298, ECO:0000269|PubMed:25692065, ECO:0000269|PubMed:25724124}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Inflammatory bowel disease 1 (IBD1) [MIM:266600]: A chronic, relapsing inflammation of the gastrointestinal tract with a complex etiology. It is subdivided into Crohn disease and ulcerative colitis phenotypes. Crohn disease may affect any part of the gastrointestinal tract from the mouth to the anus, but most frequently it involves the terminal ileum and colon. Bowel inflammation is transmural and discontinuous; it may contain granulomas or be associated with intestinal or perianal fistulas. In contrast, in ulcerative colitis, the inflammation is continuous and limited to rectal and colonic mucosal layers; fistulas and granulomas are not observed. Both diseases include extraintestinal inflammation of the skin, eyes, or joints. {ECO:0000269|PubMed:11385576}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Sarcoidosis early-onset (EOS) [MIM:609464]: A form of sarcoidosis manifesting in children younger than 4 years of age. Sarcoidosis is an idiopathic, systemic, inflammatory disease characterized by the formation of immune granulomas in involved organs. Granulomas predominantly invade the lungs and the lymphatic system, but also skin, liver, spleen, eyes and other organs may be involved. Early-onset sarcoidosis is quite rare and has a distinct triad of skin, joint and eye disorders, without apparent pulmonary involvement. Compared with an asymptomatic and sometimes naturally disappearing course of the disease in older children, early-onset sarcoidosis is progressive and in many cases causes severe complications, such as blindness, joint destruction and visceral involvement. {ECO:0000269|PubMed:15459013, ECO:0000269|PubMed:19116920, ECO:0000269|PubMed:19359344, ECO:0000269|PubMed:25093298}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Monocytes-specific.; smooth muscle;lung;heart;endometrium;placenta;colon;blood;kidney;skeletal muscle;bone marrow; superior cervical ganglion;white blood cells;whole blood;skeletal muscle; 0.13546 0.69333 0.574934281 82.08893607 510.43568 4.62729 NODAL 0.947214573997477 0.0526076317711598 0.00017779423136274 nodal growth differentiation factor FUNCTION: Essential for mesoderm formation and axial patterning during embryonic development. {ECO:0000250}.; DISEASE: Heterotaxy, visceral, 5, autosomal (HTX5) [MIM:270100]: A form of visceral heterotaxy, a complex disorder due to disruption of the normal left-right asymmetry of the thoracoabdominal organs. Visceral heterotaxy or situs ambiguus results in randomization of the placement of visceral organs, including the heart, lungs, liver, spleen, and stomach. The organs are oriented randomly with respect to the left-right axis and with respect to one another. It can been associated with variety of congenital defects including cardiac malformations. HTX5 clinical features include situs inversus viscerum or situs ambiguus, congenital heart defect, transposition of the great vessels ventricular septal defect, atrial septal defect, truncus communis, and dextrocardia. {ECO:0000269|PubMed:19064609, ECO:0000269|PubMed:9354794}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;hypothalamus;thyroid;testis;head and neck;brain; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.65696 0.42609 -0.293801652 32.93819297 34.37162 1.05103 NOG 0.682857447957634 0.297748473014533 0.0193940790278328 noggin FUNCTION: Inhibitor of bone morphogenetic proteins (BMP) signaling which is required for growth and patterning of the neural tube and somite. Essential for cartilage morphogenesis and joint formation. Inhibits chondrocyte differentiation through its interaction with GDF5 (PubMed:21976273). {ECO:0000269|PubMed:12478285, ECO:0000269|PubMed:21976273}.; DISEASE: Symphalangism, proximal 1A (SYM1A) [MIM:185800]: A disease characterized by the hereditary absence of the proximal interphalangeal joints. Distal interphalangeal joints are less frequently involved and metacarpophalangeal joints are rarely affected whereas carpal bone malformation and fusion are common. In the lower extremities, tarsal bone coalition is common. Conductive hearing loss is seen and is due to fusion of the stapes to the petrous part of the temporal bone. {ECO:0000269|PubMed:10080184, ECO:0000269|PubMed:11846737, ECO:0000269|PubMed:11857750, ECO:0000269|PubMed:15770128}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multiple synostoses syndrome 1 (SYNS1) [MIM:186500]: A bone disease characterized by multiple progressive joint fusions that commonly involve proximal interphalangeal, tarsal-carpal, humeroradial and cervical spine joints. Additional features can include progressive conductive deafness and facial dysmorphism. {ECO:0000269|PubMed:10080184, ECO:0000269|PubMed:20503332}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Tarsal-carpal coalition syndrome (TCC) [MIM:186570]: Autosomal dominant disorder characterized by fusion of the carpals, tarsals and phalanges, short first metacarpals causing brachydactyly, and humeroradial fusion. TCC is allelic to SYM1, and different mutations in NOG can result in either TCC or SYM1 in different families. {ECO:0000269|PubMed:11545688}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Stapes ankylosis with broad thumb and toes (SABTS) [MIM:184460]: Congenital autosomal dominant disorder that includes hyperopia, a hemicylindrical nose, broad thumbs, great toes, and other minor skeletal anomalies but lacked carpal and tarsal fusion and symphalangism. {ECO:0000269|PubMed:12089654}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Brachydactyly B2 (BDB2) [MIM:611377]: A form of brachydactyly characterized by hypoplasia/aplasia of distal phalanges in combination with distal symphalangism, fusion of carpal/tarsal bones and partial cutaneous syndactyly. {ECO:0000269|PubMed:17668388}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);prostate;placenta;kidney; . 0.77327 0.72890 0.347360312 73.97381458 12.77341 0.46429 NOL3 0.0005364757507069 0.458633925596851 0.540829598652443 nucleolar protein 3 FUNCTION: Isoform 1: May be involved in RNA splicing. {ECO:0000269|PubMed:10196175}.; DISEASE: Myoclonus, familial cortical (FCM) [MIM:614937]: An autosomal dominant neurologic condition characterized by adult onset of cortical myoclonus manifest as involuntary jerks or movements affecting the face and limbs. Affected individuals can also experience falls without seizure activity or loss of consciousness. {ECO:0000269|PubMed:22926851}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle. Detected at low levels in placenta, liver, kidney and pancreas.; medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; heart;adrenal cortex;skeletal muscle; 0.08489 0.13982 0.125076652 62.7388535 82.97218 1.93512 NOL4 0.998788438158561 0.00121156114980721 6.91631669963232e-10 nucleolar protein 4 . . TISSUE SPECIFICITY: Expressed predominantly in fetal brain, adult brain and testis. {ECO:0000269|PubMed:9813152}.; unclassifiable (Anatomical System);prostate;lung;frontal lobe;endometrium;islets of Langerhans;macula lutea;visual apparatus;testis;fovea centralis;brain;skeletal muscle;retina;cerebellum; occipital lobe;subthalamic nucleus;testis - interstitial;globus pallidus;cingulate cortex; 0.33775 0.11098 -0.66859065 15.76433121 32.86908 1.01975 NOL4L . . . nucleolar protein 4-like . . . . . 0.66654 0.11152 -1.045216355 7.661004954 . . NOL6 0.999078031560119 0.000921968436936674 2.9444717644071e-12 nucleolar protein 6 . . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;macula lutea;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.21138 0.11067 -0.231522913 36.36470866 535.96118 4.71978 NOL7 0.0109601211451256 0.94742735179383 0.0416125270610442 nucleolar protein 7 . . TISSUE SPECIFICITY: Expressed in numerous tissues. Particularly prevalent in the adrenal gland, thyroid gland, heart and skeletal muscle. {ECO:0000269|PubMed:16205646}.; . . 0.26621 0.10639 0.25917371 70.05779665 93.27101 2.07822 NOL8 4.48669269210147e-08 0.947261224620237 0.0527387305128356 nucleolar protein 8 FUNCTION: Plays an essential role in the survival of diffuse-type gastric cancer cells. Acts as a nucleolar anchoring protein for DDX47. May be involved in regulation of gene expression at the post-transcriptional level or in ribosome biogenesis in cancer cells. {ECO:0000269|PubMed:14660641, ECO:0000269|PubMed:15132771, ECO:0000269|PubMed:16963496}.; . TISSUE SPECIFICITY: Expressed in various diffuse-type gastric cancers. Detected at lower levels in skeletal muscle. {ECO:0000269|PubMed:15132771}.; sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;stomach;aorta; superior cervical ganglion;lymph node;tumor;white blood cells; 0.31951 0.08280 1.87399391 97.22222222 781.04628 5.53020 NOL8P1 . . . nucleolar protein 8 pseudogene 1 . . . . . . . . . . . NOL9 0.0044702400177699 0.994124916695113 0.00140484328711699 nucleolar protein 9 FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing. The kinase activity is required for the processing of the 32S precursor into 5.8S and 28S rRNAs, more specifically for the generation of the major 5.8S(S) form. In vitro, has both DNA and RNA 5'-kinase activities. Probably binds RNA. {ECO:0000269|PubMed:21063389}.; . . . . 0.11396 0.08878 -0.688817379 15.20405756 89.12472 2.02763 NOL10 0.80330394780875 0.19669415444774 1.89774350966986e-06 nucleolar protein 10 . . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;lacrimal gland;tongue;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;lung;mesenchyma;nasopharynx;placenta;macula lutea;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion; 0.28400 0.09752 0.308721233 72.59966973 1681.61121 7.55777 NOL11 0.0278293532112974 0.972074351766979 9.6295021723611e-05 nucleolar protein 11 FUNCTION: Ribosome biogenesis factor. May be required for both optimal rDNA transcription and small subunit (SSU) pre-rRNA processing at sites A', A0, 1 and 2b. {ECO:0000269|PubMed:22916032}.; . . ovary;skin;bone marrow;prostate;frontal lobe;ganglion;endometrium;cochlea;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;adrenal cortex;pharynx;blood;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.49790 0.07984 0.290313621 71.56758669 595.1741 4.93918 NOL12 0.0905536976948761 0.869666736744092 0.0397795655610315 nucleolar protein 12 FUNCTION: May bind to 28S rRNA. {ECO:0000250}.; . . . . 0.54147 0.20818 -0.0274281 51.65723048 245.68135 3.38145 NOLC1 0.246823454180935 0.75312153484921 5.50109698541532e-05 nucleolar and coiled-body phosphoprotein 1 FUNCTION: Related to nucleologenesis, may play a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus. It has intrinsic GTPase and ATPase activities. May play an important role in transcription catalyzed by RNA polymerase I.; . . . . 0.62189 0.13712 -0.045835247 50.34206181 420.66675 4.28359 NOM1 0.000163382709301448 0.993194821423644 0.00664179586705483 nucleolar protein with MIF4G domain 1 FUNCTION: Plays a role in targeting PPP1CA to the nucleolus. {ECO:0000269|PubMed:17965019}.; . TISSUE SPECIFICITY: Expressed in heart and skeletal muscle. {ECO:0000269|PubMed:10329000}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;prostate;lung;frontal lobe;nasopharynx;placenta;visual apparatus;liver;testis;head and neck;kidney;brain;mammary gland;bladder;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.08574 . 1.161078613 92.64567115 11545.2868 23.22841 NOMO1 . . . NODAL modulator 1 FUNCTION: May antagonize Nodal signaling. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in colon tumor tissue and in adjacent normal colonic mucosa.; ovary;colon;vein;skin;retina;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;amnion;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve;cerebellum; . . 0.10050 . . 534.93703 4.71517 NOMO2 . . . NODAL modulator 2 FUNCTION: May antagonize Nodal signaling and subsequent organization of axial structures during mesodermal patterning, via its interaction with NCLN. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in pancreas and skeletal muscle and, at lower levels, in heart. {ECO:0000269|PubMed:15257293}.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;cornea;adrenal gland;placenta;duodenum;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; . 0.10593 . . 370.47787 4.06416 NOMO3 . . . NODAL modulator 3 FUNCTION: May antagonize Nodal signaling. {ECO:0000250}.; . . ovary;colon;vein;skin;retina;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;amnion;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve;cerebellum; . 0.26611 0.10188 . . 1093.47746 6.32836 NONO 0.993946500321612 0.00605264383937654 8.55839011610727e-07 non-POU domain containing, octamer-binding FUNCTION: DNA- and RNA binding protein, involved in several nuclear processes. Binds the conventional octamer sequence in double-stranded DNA. Also binds single-stranded DNA and RNA at a site independent of the duplex site. Involved in pre-mRNA splicing, probably as a heterodimer with SFPQ. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. Together with PSPC1, required for the formation of nuclear paraspeckles. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends. In vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. NONO is involved in transcriptional regulation. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP- dependent transcriptional avtivity. NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. {ECO:0000269|PubMed:10858305, ECO:0000269|PubMed:11525732, ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:15590677, ECO:0000269|PubMed:22416126}.; DISEASE: Note=A chromosomal aberration involving NONO may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X;X)(p11.2;q13.1) with TFE3. {ECO:0000269|PubMed:9393982}.; TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Also found in a number of breast tumor cell lines. {ECO:0000269|PubMed:9341872}.; lymphoreticular;ovary;salivary gland;intestine;colon;skin;retina;prostate;whole body;frontal lobe;bone;testis;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;muscle;pharynx;blood;lens;bile duct;pancreas;lung;cornea;mesenchyma;nasopharynx;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; tumor;white blood cells;skeletal muscle;thymus;cerebellum; 0.89285 0.54626 0.103030231 61.2762444 16.56353 0.58532 NONOP1 . . . non-POU domain containing, octamer-binding pseudogene 1 . . . . . . . . . . . NONOP2 . . . non-POU domain containing, octamer-binding pseudogene 2 . . . . . . . . . . . NOP2 0.0489276422808689 0.951031750708106 4.06070110250553e-05 NOP2 nucleolar protein FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 4447 in 28S rRNA (Probable). May play a role in the regulation of the cell cycle and the increased nucleolar activity that is associated with the cell proliferation (Probable). {ECO:0000305, ECO:0000305|PubMed:23913415}.; . . unclassifiable (Anatomical System);lymph node;ovary;heart;colon;fovea centralis;vein;skin;skeletal muscle;breast;uterus;prostate;pancreas;lung;nasopharynx;bone;thyroid;macula lutea;liver;testis;spleen;germinal center;ciliary body;brain;mammary gland;stomach; . 0.98712 0.10969 0.380318343 75.63104506 390.95425 4.16321 NOP9 6.32257639700667e-06 0.972452673137333 0.0275410042862697 NOP9 nucleolar protein . . . . . 0.01998 0.15268 0.981046964 90.45765511 1963.61001 8.16235 NOP10 0.802013758916469 0.192654939113943 0.00533130196958781 NOP10 ribonucleoprotein FUNCTION: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ("psi") residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme. {ECO:0000269|PubMed:15044956}.; DISEASE: Dyskeratosis congenita, autosomal recessive, 1 (DKCB1) [MIM:224230]: A rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy. {ECO:0000269|PubMed:17507419}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;germinal center;bladder;brain;tonsil;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;vein;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; uterus corpus;lung;heart;kidney;whole blood; 0.42565 . 0.301449681 71.80938901 18.54283 0.64158 NOP14 0.0174491653147605 0.982542924230981 7.91045425894889e-06 NOP14 nucleolar protein FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm (By similarity). {ECO:0000250}.; . . myocardium;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;corpus striatum;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;blood;lens;breast;bile duct;lung;placenta;macula lutea;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13414 0.10550 0.565800595 81.72918141 4116.58038 12.73874 NOP14-AS1 . . . NOP14 antisense RNA 1 . . . . . . . . . . . NOP16 0.145044756925216 0.836554687447806 0.0184005556269774 NOP16 nucleolar protein . . . unclassifiable (Anatomical System);prostate;ovary;islets of Langerhans;testis;colon;blood;germinal center;stomach; superior cervical ganglion;tumor;skeletal muscle; . . 0.014844891 54.94810097 395.77746 4.18004 NOP56 0.973256819691124 0.0267429077033917 2.72605484371601e-07 NOP56 ribonucleoprotein FUNCTION: Involved in the early to middle stages of 60S ribosomal subunit biogenesis. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such U3, U8 and U14 snoRNAs. {ECO:0000269|PubMed:12777385, ECO:0000269|PubMed:15574333}.; DISEASE: Spinocerebellar ataxia 36 (SCA36) [MIM:614153]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA36 is characterized by complicated clinical features, with ataxia as the first symptom, followed by characteristic late-onset involvement of the motor neuron system. Ataxic symptoms, such as gait and truncal instability, ataxic dysarthria, and uncoordinated limbs, start in late forties to fifties. Characteristically, affected individuals exhibit tongue atrophy with fasciculation. Progression of motor neuron involvement is typically limited to the tongue and main proximal skeletal muscles in both upper and lower extremities. {ECO:0000269|PubMed:21683323}. Note=The disease is caused by mutations affecting the gene represented in this entry. Caused by large hexanucleotide CGCCTG repeat expansions within intron 1. These expansions induce RNA foci and sequester the RNA-binding protein SRSF2. In addition, the transcription of MIR1292, a microRNA gene located just 19 bp 3' of the GGCCTG repeat, is significantly decreased.; . . . 0.99035 0.37745 -0.442665927 24.53408823 2441.81313 9.18965 NOP56P1 . . . NOP56 ribonucleoprotein pseudogene 1 . . . . . . . . . . . NOP56P2 . . . NOP56 ribonucleoprotein pseudogene 2 . . . . . . . . . . . NOP56P3 . . . NOP56 ribonucleoprotein pseudogene 3 . . . . . . . . . . . NOP58 0.509478886469782 0.490487322346714 3.37911835042842e-05 NOP58 ribonucleoprotein FUNCTION: Required for 60S ribosomal subunit biogenesis (By similarity). Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such as U3, U8 and U14 snoRNAs. {ECO:0000250, ECO:0000269|PubMed:15574333, ECO:0000269|PubMed:17636026, ECO:0000269|PubMed:19620283}.; . TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;skin;bone marrow;prostate;cochlea;thyroid;amniotic fluid;germinal center;brain;tonsil;heart;cartilage;urinary;adrenal cortex;pharynx;blood;skeletal muscle;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;uterus;whole body;oesophagus;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;pia mater;cornea;nasopharynx;placenta;hippocampus;amnion;kidney;stomach; . . . -0.47017169 23.25430526 30.9563 0.97894 NORAD . . . non-coding RNA activated by DNA damage . . . . . . . . . . . NOS1 0.998694760625134 0.001305239374809 5.69203679160769e-14 nitric oxide synthase 1 FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR.; . TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed: detected in skeletal muscle and brain, also in testis, lung and kidney, and at low levels in heart, adrenal gland and retina. Not detected in the platelets. Isoform 3 is expressed only in testis. Isoform 4 is detected in testis, skeletal muscle, lung, and kidney, at low levels in the brain, but not in the heart and adrenal gland.; unclassifiable (Anatomical System);ovary;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;cingulate cortex; 0.16966 0.61198 -1.006844617 8.209483369 3681.52283 11.80735 NOS1AP 0.119913961376149 0.878969228443268 0.00111681018058304 nitric oxide synthase 1 adaptor protein FUNCTION: Adapter protein involved in neuronal nitric-oxide (NO) synthesis regulation via its association with nNOS/NOS1. The complex formed with NOS1 and synapsins is necessary for specific NO and synapsin functions at a presynaptic level. Mediates an indirect interaction between NOS1 and RASD1 leading to enhance the ability of NOS1 to activate RASD1. Competes with DLG4 for interaction with NOS1, possibly affecting NOS1 activity by regulating the interaction between NOS1 and DLG4 (By similarity). {ECO:0000250}.; . . testis;colon;brain;mammary gland; dorsal root ganglion;amygdala;whole brain;superior cervical ganglion;occipital lobe;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.36398 0.41336 0.018483465 55.44939844 61.59812 1.59995 NOS2 7.26084821392684e-09 0.998625922369478 0.0013740703696734 nitric oxide synthase 2 FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body (PubMed:7531687, PubMed:7544004). In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2 (By similarity). As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH on 'Cys-247' implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM (PubMed:25417112). Involved in inflammation, enhances the synthesis of proinflammatory mediators such as IL6 and IL8 (PubMed:19688109). {ECO:0000250|UniProtKB:P29477, ECO:0000269|PubMed:19688109, ECO:0000269|PubMed:25417112, ECO:0000269|PubMed:7531687, ECO:0000269|PubMed:7544004}.; . TISSUE SPECIFICITY: Expressed in the liver, retina, bone cells and airway epithelial cells of the lung. Not expressed in the platelets.; unclassifiable (Anatomical System);breast;lung;cartilage;ovary;nasopharynx;testis;colon;blood;brain;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.17004 0.94961 -1.675620402 2.689313517 2728.58132 9.84685 NOS2P1 . . . nitric oxide synthase 2 pseudogene 1 . . . . . 0.38531 . . . . . NOS2P2 . . . nitric oxide synthase 2 pseudogene 2 . . . . . . . . . . . NOS2P3 . . . nitric oxide synthase 2 pseudogene 3 . . . . . . . . . . . NOS2P4 . . . nitric oxide synthase 2 pseudogene 4 . . . . . . . . . . . NOS3 2.21161070571318e-05 0.999969698517901 8.18537504200916e-06 nitric oxide synthase 3 FUNCTION: Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.; DISEASE: Note=Variation in NOS3 seem to be associated with susceptibility to coronary spasm. {ECO:0000269|PubMed:11740345, ECO:0000269|PubMed:9737779}.; TISSUE SPECIFICITY: Platelets, placenta, liver and kidney. {ECO:0000269|PubMed:7515611}.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;whole body;lung;bone;placenta;macula lutea;liver;testis;spleen;brain;mammary gland;stomach;thymus; placenta;testis;parietal lobe; 0.24036 0.80830 -1.096852975 6.965086105 363.12652 4.03595 NOSIP 0.00230156568092138 0.923349231718922 0.0743492026001562 nitric oxide synthase interacting protein FUNCTION: Negatively regulates nitric oxide production by inducing NOS1 and NOS3 translocation to actin cytoskeleton and inhibiting their enzymatic activity. {ECO:0000269|PubMed:11149895, ECO:0000269|PubMed:15548660, ECO:0000269|PubMed:16135813}.; . TISSUE SPECIFICITY: Expressed in heart, brain and lung. Present in endothelial cells (at protein level). {ECO:0000269|PubMed:11149895}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;kidney;mammary gland;stomach;cerebellum; testis - interstitial;testis - seminiferous tubule;testis; 0.19980 0.11118 -0.339715008 30.06605331 11.67325 0.42346 NOSTRIN 3.5797265988291e-10 0.509459127166122 0.490540872475906 nitric oxide synthase trafficking FUNCTION: Multivalent adapter protein which may decrease NOS3 activity by inducing its translocation away from the plasma membrane. {ECO:0000269|PubMed:12446846, ECO:0000269|PubMed:16234328, ECO:0000269|PubMed:16807357}.; . TISSUE SPECIFICITY: Expressed at highest levels in heart, kidney, placenta and lung, and at lowest levels in brain, thymus and spleen. Present in vascular endothelial cells and placenta. Over- expressed in placenta from women with pre-eclampsia (at protein level). {ECO:0000269|PubMed:12446846, ECO:0000269|PubMed:15847871}.; unclassifiable (Anatomical System);cartilage;colon;prostate;whole body;lung;endometrium;nasopharynx;thyroid;placenta;testis;kidney;brain;mammary gland;aorta;tonsil;stomach; trigeminal ganglion; 0.32093 0.07890 1.2860853 93.80160415 1520.59946 7.24769 NOTCH1 0.999999994320622 5.67937835833025e-09 7.21902176912796e-23 notch 1 FUNCTION: Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4+ and CD8+ cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis. May enhance HIF1A function by sequestering HIF1AN away from HIF1A. Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury. Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). {ECO:0000269|PubMed:20616313}.; DISEASE: Aortic valve disease 1 (AOVD1) [MIM:109730]: A common defect in the aortic valve in which two rather than three leaflets are present. It is often associated with aortic valve calcification, stenosis and insufficiency. In extreme cases, the blood flow may be so restricted that the left ventricle fails to grow, resulting in hypoplastic left heart syndrome. {ECO:0000269|PubMed:16025100}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Adams-Oliver syndrome 5 (AOS5) [MIM:616028]: A form of Adams-Oliver syndrome, a disorder characterized by the congenital absence of skin (aplasia cutis congenita) in combination with transverse limb defects. Aplasia cutis congenita can be located anywhere on the body, but in the vast majority of the cases, it is present on the posterior parietal region where it is often associated with an underlying defect of the parietal bones. Limb abnormalities are typically limb truncation defects affecting the distal phalanges or entire digits (true ectrodactyly). Only rarely, metatarsals/metacarpals or more proximal limb structures are also affected. Apart from transverse limb defects, syndactyly, most commonly of second and third toes, can also be observed. The clinical features are highly variable and can also include cardiovascular malformations, brain abnormalities and vascular defects such as cutis marmorata and dilated scalp veins. {ECO:0000269|PubMed:25132448}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In fetal tissues most abundant in spleen, brain stem and lung. Also present in most adult tissues where it is found mainly in lymphoid tissues.; smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;muscle;urinary;blood;breast;pancreas;lung;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.94531 0.91608 -3.510304589 0.330266572 576.67829 4.86776 NOTCH2 0.999999993249444 6.75055638780422e-09 4.50238441288997e-24 notch 2 FUNCTION: Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs (By similarity). Involved in bone remodeling and homeostasis. In collaboration with RELA/p65 enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation. Positively regulates self-renewal of liver cancer cells (PubMed:25985737). {ECO:0000250|UniProtKB:O35516, ECO:0000269|PubMed:21378985, ECO:0000269|PubMed:21378989, ECO:0000269|PubMed:25985737}.; DISEASE: Alagille syndrome 2 (ALGS2) [MIM:610205]: A form of Alagille syndrome, an autosomal dominant multisystem disorder. It is clinically defined by hepatic bile duct paucity and cholestasis in association with cardiac, skeletal, and ophthalmologic manifestations. There are characteristic facial features and less frequent clinical involvement of the renal and vascular systems. {ECO:0000269|PubMed:16773578}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hajdu-Cheney syndrome (HJCYS) [MIM:102500]: A rare skeletal disorder characterized by the association of facial anomalies, acro-osteolysis, general osteoporosis, insufficient ossification of the skull, and periodontal disease (premature loss of permanent teeth). Other features include cleft palate, congenital heart defects, polycystic kidneys, orthopedic problems and anomalies of the genitalia, intestines and eyes. {ECO:0000269|PubMed:21378985, ECO:0000269|PubMed:21378989}. Note=The disease is caused by mutations affecting the gene represented in this entry. NOTCH2 mutations associated with Hajdu- Cheney syndrome cluster to the last coding exon of the gene. This suggests that the mutant mRNA products may escape nonsense- mediated decay and the resulting truncated NOTCH2 proteins act in a gain-of-function manner.; TISSUE SPECIFICITY: Expressed in the brain, heart, kidney, lung, skeletal muscle and liver. Ubiquitously expressed in the embryo. {ECO:0000269|PubMed:21378985}.; ovary;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;pineal body;urinary;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;uterus;whole body;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;bile duct;pancreas;lung;pia mater;nasopharynx;placenta;hypopharynx;amnion;head and neck;kidney;stomach;thymus; superior cervical ganglion;testis - seminiferous tubule;placenta;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.95316 0.43816 -1.819260363 2.14673272 449.73773 4.40739 NOTCH2NL 0.00010062258971701 0.575070488622283 0.424828888788 notch 2 N-terminal like FUNCTION: May function in the Notch signaling pathway and regulate neutrophil differentiation. {ECO:0000269|PubMed:14673143}.; . TISSUE SPECIFICITY: Widely expressed with higher levels in leukocytes and lymph nodes. {ECO:0000269|PubMed:14673143}.; medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;synovium;bone;testis;germinal center;unclassifiable (Anatomical System);heart;tongue;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;macula lutea;alveolus;head and neck;cervix;kidney;mammary gland;stomach;aorta; uterus;prostate;olfactory bulb;testis - seminiferous tubule;testis;white blood cells;ciliary ganglion; 0.13774 . 0.657836546 84.27105449 3.00594 0.10883 NOTCH2P1 . . . notch 2 pseudogene 1 . . . . . . . . . . . NOTCH3 0.207712384985181 0.792287613907435 1.10738381497939e-09 notch 3 FUNCTION: Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs (By similarity). {ECO:0000250}.; DISEASE: Cerebral arteriopathy with subcortical infarcts and leukoencephalopathy, autosomal dominant (CADASIL) [MIM:125310]: A cerebrovascular disease characterized by multiple subcortical infarcts, pseudobulbar palsy, dementia, and the presence of granular deposits in small cerebral arteries producing ischemic stroke. {ECO:0000269|PubMed:10227618, ECO:0000269|PubMed:10371548, ECO:0000269|PubMed:10802807, ECO:0000269|PubMed:10854111, ECO:0000269|PubMed:11058919, ECO:0000269|PubMed:11102981, ECO:0000269|PubMed:11559313, ECO:0000269|PubMed:11755616, ECO:0000269|PubMed:11810186, ECO:0000269|PubMed:12136071, ECO:0000269|PubMed:12146805, ECO:0000269|PubMed:12589106, ECO:0000269|PubMed:12810003, ECO:0000269|PubMed:15229130, ECO:0000269|PubMed:15300988, ECO:0000269|PubMed:15364702, ECO:0000269|PubMed:15378071, ECO:0000269|PubMed:15818833, ECO:0000269|PubMed:16009764, ECO:0000269|PubMed:24000151, ECO:0000269|PubMed:9388399}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myofibromatosis, infantile 2 (IMF2) [MIM:615293]: A rare mesenchymal disorder characterized by the development of benign tumors in the skin, striated muscles, bones, and, more rarely, visceral organs. Subcutaneous or soft tissue nodules commonly involve the skin of the head, neck, and trunk. Skeletal and muscular lesions occur in about half of the patients. Lesions may be solitary or multicentric, and they may be present at birth or become apparent in early infancy or occasionally in adult life. Visceral lesions are associated with high morbidity and mortality. {ECO:0000269|PubMed:23731542}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed in fetal and adult tissues.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cerebral cortex;oesophagus;endometrium;larynx;bone;testis;spinal ganglion;brain;artery;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;blood;lens;breast;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; superior cervical ganglion;placenta;temporal lobe;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.85677 0.19684 -1.286322754 5.036565228 1985.01297 8.21061 NOTCH4 1.19532150508521e-10 0.999993035219917 6.9646605505226e-06 notch 4 FUNCTION: Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. May regulate branching morphogenesis in the developing vascular system (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in the heart, moderately in the lung and placenta and at low levels in the liver, skeletal muscle, kidney, pancreas, spleen, lymph node, thymus, bone marrow and fetal liver. No expression was seen in adult brain or peripheral blood leukocytes.; . . 0.37424 . 0.1505561 64.32531257 4975.85094 14.38235 NOTO . . . notochord homeobox FUNCTION: Transcription regulator acting downstream of both FOXA2 and T during notochord development. Required for node morphogenesis. Is essential for cilia formation in the posterior notochord (PNC) and for left-right patterning; acts upstream of FOXJ1 and RFX3 in this process and is required for the expression of various components important for axonemal assembly and function. Plays a role in regulating axial versus paraxial cell fate (By similarity). {ECO:0000250}.; . . . . . . . . 793.50713 5.55406 NOTUM 0.000860399771955871 0.984521788918401 0.0146178113096432 notum pectinacetylesterase homolog (Drosophila) FUNCTION: Carboxylesterase that acts as a key negative regulator of the Wnt signaling pathway by specifically mediating depalmitoleylation of WNT proteins. Serine palmitoleylation of WNT proteins is required for efficient binding to frizzled receptors (PubMed:25731175). {ECO:0000269|PubMed:25731175}.; . TISSUE SPECIFICITY: Rarely expressed in adult normal tissues. {ECO:0000269|PubMed:18429952}.; . . 0.24251 0.12435 -0.468351206 23.42533616 393.9962 4.17307 NOV 0.113896789353618 0.858381110049151 0.0277221005972312 nephroblastoma overexpressed FUNCTION: Immediate-early protein playing a role in various cellular processes including proliferation, adhesion, migration, differentiation and survival (PubMed:15181016, PubMed:15611078, PubMed:12695522, PubMed:21344378, PubMed:12050162). Acts by binding to integrins or membrane receptors such as NOTCH1 (PubMed:12695522, PubMed:21344378, PubMed:15611078). Essential regulator of hematopoietic stem and progenitor cell function (PubMed:17463287). Inhibits myogenic differentiation through the activation of Notch-signaling pathway (PubMed:12050162). Inhibits vascular smooth muscle cells proliferation by increasing expression of cell-cycle regulators such as CDKN2B or CDKN1A independently of TGFB1 signaling (PubMed:20139355). Ligand of integrins ITGAV:ITGB3 and ITGA5:ITGB1, acts directly upon endothelial cells to stimulate pro-angiogenic activities and induces angiogenesis. In endothelial cells, supports cell adhesion, induces directed cell migration (chemotaxis) and promotes cell survival (PubMed:12695522). Plays also a role in cutaneous wound healing acting as integrin receptor ligand. Supports skin fibroblast adhesion through ITGA5:ITGB1 and ITGA6:ITGB1 and induces fibroblast chemotaxis through ITGAV:ITGB5. Seems to enhance bFGF-induced DNA synthesis in fibroblasts (PubMed:15611078). Involved in bone regeneration as a negative regulator (By similarity). Enhances the articular chondrocytic phenotype, whereas it repressed the one representing endochondral ossification (PubMed:21871891). Impairs pancreatic beta-cell function, inhibits beta-cell proliferation and insulin secretion (By similarity). Plays a role as negative regulator of endothelial pro-inflammatory activation reducing monocyte adhesion, its anti- inflammatory effects occur secondary to the inhibition of NF- kappaB signaling pathway (PubMed:21063504). Contributes to the control and coordination of inflammatory processes in atherosclerosis (By similarity). Attenuates inflammatory pain through regulation of IL1B- and TNF-induced MMP9, MMP2 and CCL2 expression. Inhibits MMP9 expression through ITGB1 engagement (PubMed:21871891). {ECO:0000250|UniProtKB:Q64299, ECO:0000269|PubMed:12050162, ECO:0000269|PubMed:12695522, ECO:0000269|PubMed:15181016, ECO:0000269|PubMed:15611078, ECO:0000269|PubMed:17463287, ECO:0000269|PubMed:20139355, ECO:0000269|PubMed:21063504, ECO:0000269|PubMed:21344378, ECO:0000269|PubMed:21871891}.; . TISSUE SPECIFICITY: Expressed in endiothelial cells (at protein level) (PubMed:21063504). Expressed in bone marrow, thymic cells and nephroblastoma. Increased expression in Wilms tumor of the stromal type. {ECO:0000269|PubMed:1756408, ECO:0000269|PubMed:21063504}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;thyroid;bone;testis;spinal ganglion;brain;artery;pineal gland;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;macula lutea;hippocampus;liver;cervix;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;adrenal gland;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.83597 0.17974 0.12689526 63.00424628 2107.61012 8.45098 NOVA1 0.977721706151375 0.0222573918762337 2.090197239108e-05 neuro-oncological ventral antigen 1 FUNCTION: May regulate RNA splicing or metabolism in a specific subset of developing neurons.; . TISSUE SPECIFICITY: Brain.; unclassifiable (Anatomical System);breast;lung;cochlea;pharynx;testis;blood;brain;retina; whole brain;superior cervical ganglion;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;pons;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.95470 0.11773 -0.692458599 14.96815287 152.84098 2.70383 NOVA1-AS1 . . . NOVA1 antisense RNA 1 (head to head) . . . . . . . . . . . NOVA2 . . . neuro-oncological ventral antigen 2 FUNCTION: May regulate RNA splicing or metabolism in a specific subset of developing neurons (By similarity). Binds single strand RNA. {ECO:0000250}.; . TISSUE SPECIFICITY: Brain. Expression restricted to astrocytes.; unclassifiable (Anatomical System);cartilage;colon;parathyroid;fovea centralis;choroid;lens;retina;pancreas;optic nerve;lung;frontal lobe;macula lutea;testis;kidney;brain; superior cervical ganglion;temporal lobe;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.42514 . -0.207437529 38.2814343 6.39019 0.23941 NOX1 0.000386451550813002 0.956605075682027 0.0430084727671597 NADPH oxidase 1 FUNCTION: NOH-1S is a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes and other tissues. It participates in the regulation of cellular pH and is blocked by zinc. NOH-1L is a pyridine nucleotide-dependent oxidoreductase that generates superoxide and might conduct H(+) ions as part of its electron transport mechanism, whereas NOH-1S does not contain an electron transport chain.; . TISSUE SPECIFICITY: NOH-1L is detected in colon, uterus, prostate, and colon carcinoma, but not in peripheral blood leukocytes. NOH- 1S is detected only in colon and colon carcinoma cells.; unclassifiable (Anatomical System);colon; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11233 0.28224 0.420771676 77.15852795 232.74962 3.29903 NOX3 3.57964894206844e-09 0.762595495722907 0.237404500697444 NADPH oxidase 3 FUNCTION: NADPH oxidase which constitutively produces superoxide upon formation of a complex with CYBA/p22phox. Plays a role in the biogenesis of otoconia/otolith, which are crystalline structures of the inner ear involved in the perception of gravity. {ECO:0000269|PubMed:15824103}.; . . . . 0.16604 0.28834 -0.486758915 22.69992923 3560.05559 11.53654 NOX4 8.15748090375783e-07 0.995429406527313 0.00456977772459647 NADPH oxidase 4 FUNCTION: Constitutive NADPH oxidase which generates superoxide intracellularly upon formation of a complex with CYBA/p22phox. Regulates signaling cascades probably through phosphatases inhibition. May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium channel and HIF1A activity. May regulate insulin signaling cascade. May play a role in apoptosis, bone resorption and lipolysaccharide-mediated activation of NFKB. May produce superoxide in the nucleus and play a role in regulating gene expression upon cell stimulation. Isoform 3 is not functional. Isoform 5 and isoform 6 display reduced activity.; . TISSUE SPECIFICITY: Expressed by distal tubular cells in kidney cortex and in endothelial cells (at protein level). Widely expressed. Strongly expressed in kidney and to a lower extent in heart, adipocytes, hepatoma, endothelial cells, skeletal muscle, brain, several brain tumor cell lines and airway epithelial cells. {ECO:0000269|PubMed:11032835, ECO:0000269|PubMed:11376945, ECO:0000269|PubMed:15210697, ECO:0000269|PubMed:16324151}.; unclassifiable (Anatomical System);heart;ovary;developmental;colon;parathyroid;fovea centralis;skin;uterus;pancreas;larynx;placenta;macula lutea;head and neck;kidney;brain;artery;aorta;stomach; superior cervical ganglion;atrioventricular node;kidney;trigeminal ganglion; 0.19980 0.32998 0.112125503 62.09601321 5273.56078 15.00336 NOX5 1.72408872311278e-13 0.052919440150048 0.94708055984978 NADPH oxidase, EF-hand calcium binding domain 5 FUNCTION: Calcium-dependent NADPH oxidase that generates superoxide. Also functions as a calcium-dependent proton channel and may regulate redox-dependent processes in lymphocytes and spermatozoa. May play a role in cell growth and apoptosis. Isoform v2 and isoform v5 are involved in endothelial generation of reactive oxygen species (ROS), proliferation and angiogenesis and contribute to endothelial response to thrombin. {ECO:0000269|PubMed:11483596, ECO:0000269|PubMed:12686516, ECO:0000269|PubMed:17275676}.; . TISSUE SPECIFICITY: Mainly expressed in pachytene spermatocytes of testis and in lymphocyte-rich areas of spleen and lymph nodes. Isoform v1 is expressed in spleen. Isoform v2 is expressed in testis. Also detected in ovary, placenta, pancreas, cardiac fibroblasts. Expressed in B-cells and prostate malignant cells. Isoform v1 and isoform v3 are expressed in epithelial colorectal adenocarcinoma cells. Isoform v2 and isoform v4 are expressed in endothelial cells. Isoform v1, isoform v2, isoform v3 and isoform v4 are expressed in pulmonary artery smooth muscle cells. Isoform v2 and isoform v5 are expressed in microvascular endothelial cells (at protein level). {ECO:0000269|PubMed:11376945, ECO:0000269|PubMed:11483596, ECO:0000269|PubMed:12686516, ECO:0000269|PubMed:16179589, ECO:0000269|PubMed:16339585, ECO:0000269|PubMed:17275676}.; . . 0.10914 0.76607 1.581840753 95.7891012 2826.15362 10.02852 NOXA1 4.73427762914004e-06 0.851003662245781 0.148991603476589 NADPH oxidase activator 1 FUNCTION: Functions as an activator of NOX1, a superoxide- producing NADPH oxidase. Functions in the production of reactive oxygen species (ROS) which participate in a variety of biological processes including host defense, hormone biosynthesis, oxygen sensing and signal transduction. May also activate CYBB/gp91phox and NOX3. {ECO:0000269|PubMed:12657628, ECO:0000269|PubMed:12716910, ECO:0000269|PubMed:14617635, ECO:0000269|PubMed:14978110, ECO:0000269|PubMed:15181005, ECO:0000269|PubMed:15824103, ECO:0000269|PubMed:17602954, ECO:0000269|PubMed:19755710}.; . TISSUE SPECIFICITY: Widely expressed. Detected in pancreas, liver, kidney, spleen, prostate, small intestine and colon. {ECO:0000269|PubMed:12716910}.; unclassifiable (Anatomical System);lymphoreticular;lung;islets of Langerhans;hippocampus;colon;blood;kidney;brain;stomach;retina;bone marrow; . 0.11005 0.14742 0.756930627 86.79523473 726.33402 5.35221 NOXO1 3.17355817693735e-11 0.0118082310605687 0.988191768907696 NADPH oxidase organizer 1 FUNCTION: Constitutively potentiates the superoxide-generating activity of NOX1 and NOX3 and is required for the biogenesis of otoconia/otolith, which are crystalline structures of the inner ear involved in the perception of gravity. Isoform 3 is more potent than isoform 1 in activating NOX3. Together with NOXA1, may also substitute to NCF1/p47phox and NCF2/p67phox in supporting the phagocyte NOX2/gp91phox superoxide-generating activity. {ECO:0000269|PubMed:12657628, ECO:0000269|PubMed:14617635, ECO:0000269|PubMed:15326186, ECO:0000269|PubMed:15824103, ECO:0000269|PubMed:15949904, ECO:0000269|PubMed:16329988, ECO:0000269|PubMed:17126813, ECO:0000269|PubMed:19755710}.; . TISSUE SPECIFICITY: Expressed in testis, small and large intestines, liver, kidney and pancreas. Isoform 3 is mainly expressed in colon. Isoform 1 is preferentially expressed in testis. {ECO:0000269|PubMed:12657628, ECO:0000269|PubMed:15326186, ECO:0000269|PubMed:15949904}.; uterus;lung;frontal lobe;heart;liver;colon;skin; . 0.06260 0.13930 0.240763792 69.36777542 563.1205 4.81832 NOXRED1 0.118495407678092 0.855525773204156 0.025978819117752 NADP-dependent oxidoreductase domain containing 1 FUNCTION: Probable oxidoreductase. {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;testis; superior cervical ganglion; 0.05549 . -0.404032746 26.53338051 16.10819 0.57060 NPAP1 0.273009365565849 0.721810071646943 0.00518056278720751 nuclear pore associated protein 1 FUNCTION: May be involved in spermatogenesis.; . TISSUE SPECIFICITY: Testis-specific in adults. In fetal brain expressed only from the paternal allele. {ECO:0000269|PubMed:10783265, ECO:0000269|PubMed:17337158, ECO:0000269|PubMed:20020165}.; . . 0.05519 0.05806 3.546886998 99.49280491 286.08933 3.62008 NPAP1P1 . . . nuclear pore associated protein 1 pseudogene 1 . . . . . . . . . . . NPAP1P2 . . . nuclear pore associated protein 1 pseudogene 2 . . . . . . . . . . . NPAP1P3 . . . nuclear pore associated protein 1 pseudogene 3 . . . . . . . . . . . NPAP1P4 . . . nuclear pore associated protein 1 pseudogene 4 . . . . . . . . . . . NPAP1P5 . . . nuclear pore associated protein 1 pseudogene 5 . . . . . . . . . . . NPAP1P6 . . . nuclear pore associated protein 1 pseudogene 6 . . . . . . . . . . . NPAP1P7 . . . nuclear pore associated protein 1 pseudogene 7 . . . . . . . . . . . NPAP1P8 . . . nuclear pore associated protein 1 pseudogene 8 . . . . . . . . . . . NPAS1 0.916472527076156 0.0834115469357856 0.000115925988058454 neuronal PAS domain protein 1 FUNCTION: May control regulatory pathways relevant to schizophrenia and to psychotic illness. May play a role in late central nervous system development by modulating EPO expression in response to cellular oxygen level (By similarity). {ECO:0000250}.; . . . . 0.15447 0.13220 . . 52.08231 1.42598 NPAS2 0.990888561613575 0.00911143759670137 7.89723477231129e-10 neuronal PAS domain protein 2 FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time- keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. The NPAS2-ARNTL/BMAL1 heterodimer positively regulates the expression of MAOA, F7 and LDHA and modulates the circadian rhythm of daytime contrast sensitivity by regulating the rhythmic expression of adenylate cyclase type 1 (ADCY1) in the retina. NPAS2 plays an important role in sleep homeostasis and in maintaining circadian behaviors in normal light/dark and feeding conditions and in the effective synchronization of feeding behavior with scheduled food availability. Regulates the gene transcription of key metabolic pathways in the liver and is involved in DNA damage response by regulating several cell cycle and DNA repair genes. {ECO:0000269|PubMed:11441146, ECO:0000269|PubMed:11441147, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:18439826, ECO:0000269|PubMed:18819933}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;adrenal cortex;lens;skeletal muscle;bile duct;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney; amygdala;whole brain;superior cervical ganglion;occipital lobe;subthalamic nucleus;prefrontal cortex;globus pallidus;caudate nucleus;cingulate cortex;skeletal muscle; 0.21897 0.22837 -0.506987379 21.76810569 5079.47281 14.59455 NPAS3 0.980548669706538 0.0194512061004182 1.24193044101877e-07 neuronal PAS domain protein 3 FUNCTION: May play a broad role in neurogenesis. May control regulatory pathways relevant to schizophrenia and to psychotic illness (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed in the adult brain.; unclassifiable (Anatomical System);ovary;endometrium;hypothalamus;placenta;testis;parathyroid;kidney;brain; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;skin; 0.30103 0.14620 -1.350267166 4.600141543 902.6267 5.84777 NPAS4 0.424264241074538 0.5754152948702 0.000320464055261607 neuronal PAS domain protein 4 FUNCTION: Acts as a transcriptional activator in the presence of ARNT. Can activate the CME (CNS midline enhancer) element and the expression of the drebrin gene. {ECO:0000269|PubMed:14701734}.; . TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:14701734}.; unclassifiable (Anatomical System);optic nerve;lung; . 0.53997 0.11506 -0.663133267 15.94715735 65.91909 1.67179 NPAT 0.14267656931501 0.857322057955882 1.37272910763771e-06 nuclear protein, co-activator of histone transcription FUNCTION: Required for progression through the G1 and S phases of the cell cycle and for S phase entry. Activates transcription of the histone H2A, histone H2B, histone H3 and histone H4 genes in conjunction with MIZF. Also positively regulates the ATM, MIZF and PRKDC promoters. Transcriptional activation may be accomplished at least in part by the recruitment of the NuA4 histone acetyltransferase (HAT) complex to target gene promoters. {ECO:0000269|PubMed:10995386, ECO:0000269|PubMed:10995387, ECO:0000269|PubMed:12665581, ECO:0000269|PubMed:12724424, ECO:0000269|PubMed:14585971, ECO:0000269|PubMed:14612403, ECO:0000269|PubMed:15555599, ECO:0000269|PubMed:15988025, ECO:0000269|PubMed:16131487, ECO:0000269|PubMed:17163457, ECO:0000269|PubMed:17826007, ECO:0000269|PubMed:17967892, ECO:0000269|PubMed:17974976, ECO:0000269|PubMed:9472014}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:8743993, ECO:0000269|PubMed:8923007}.; unclassifiable (Anatomical System);heart;adrenal cortex;colon;blood;skeletal muscle;uterus;lung;nasopharynx;liver;spleen;germinal center;brain; dorsal root ganglion;superior cervical ganglion;skeletal muscle; 0.92712 0.25795 0.631940882 83.58103326 1730.99718 7.67708 NPB 0.428299526299304 0.461507755119247 0.110192718581449 neuropeptide B FUNCTION: May be involved in the regulation of feeding, neuroendocrine system, memory, learning and in the afferent pain pathway. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed in the central nervous system. High levels are found in substantia nigra, hypothalamus, hyppocampus, spinal cord, placenta and fetal brain; lower levels are found in testis, uterus and ovary. Also detected at high levels in colorectal adenocarcinoma.; lung;cervix;stomach; . . 0.16458 . . 36.25255 1.08625 NPBWR1 0.00013240681272579 0.232138834307135 0.767728758880139 neuropeptides B/W receptor 1 FUNCTION: Interacts specifically with a number of opioid ligands. Receptor for neuropeptides B and W, which may be involved in neuroendocrine system regulation, food intake and the organization of other signals. Has a higher affinity for neuropeptide B.; . TISSUE SPECIFICITY: Found in cerebellum and frontal cortex. Detected at high levels in hippocampus, amygdala and trachea; at moderate levels in fetal brain, pituitary gland and prostate. Not in caudate, accumbens, kidney or liver. Also detected at high levels in lung carcinoma. {ECO:0000269|PubMed:12401809}.; . . 0.11220 0.13827 0.461228372 78.46190139 718.60671 5.32186 NPBWR2 0.0022243335643839 0.52212534191115 0.475650324524466 neuropeptides B/W receptor 2 FUNCTION: Interacts specifically with a number of opioid ligands. Receptor for neuropeptides B and W, which may be involved in neuroendocrine system regulation, food intake and the organization of other signals.; . TISSUE SPECIFICITY: Detected at high levels in caudate nucleus, hyppocampus and amygdala; at moderate levels in the adult brain, thalamus, parietal cortex, pituitary gland, adrenal gland and lymph nodes. {ECO:0000269|PubMed:12401809}.; . . 0.11295 0.14675 -0.420619508 25.72540694 192.47244 3.00852 NPC1 0.000213375031005479 0.999785064439965 1.56052902935862e-06 Niemann-Pick disease, type C1 FUNCTION: Intracellular cholesterol transporter which acts in concert with NPC2 and plays an important role in the egress of cholesterol from the endosomal/lysosomal compartment. Both NPC1 and NPC2 function as the cellular 'tag team duo' (TTD) to catalyze the mobilization of cholesterol within the multivesicular environment of the late endosome (LE) to effect egress through the limiting bilayer of the LE. NPC2 binds unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes and transfers it to the cholesterol-binding pocket of the N-terminal domain of NPC1. Cholesterol binds to NPC1 with the hydroxyl group buried in the binding pocket and is exported from the limiting membrane of late endosomes/ lysosomes to the ER and plasma membrane by an unknown mechanism. Binds oxysterol with higher affinity than cholesterol. May play a role in vesicular trafficking in glia, a process that may be crucial for maintaining the structural and functional integrity of nerve terminals. {ECO:0000269|PubMed:18772377, ECO:0000269|PubMed:19563754}.; DISEASE: Niemann-Pick disease C1 (NPC1) [MIM:257220]: A lysosomal storage disorder that affects the viscera and the central nervous system. It is due to defective intracellular processing and transport of low-density lipoprotein derived cholesterol. It causes accumulation of cholesterol in lysosomes, with delayed induction of cholesterol homeostatic reactions. Niemann-Pick disease type C1 has a highly variable clinical phenotype. Clinical features include variable hepatosplenomegaly and severe progressive neurological dysfunction such as ataxia, dystonia and dementia. The age of onset can vary from infancy to late adulthood. An allelic variant of Niemann-Pick disease type C1 is found in people with Nova Scotia ancestry. Patients with the Nova Scotian clinical variant are less severely affected. {ECO:0000269|PubMed:10480349, ECO:0000269|PubMed:10521290, ECO:0000269|PubMed:10521297, ECO:0000269|PubMed:11182931, ECO:0000269|PubMed:11333381, ECO:0000269|PubMed:11349231, ECO:0000269|PubMed:11479732, ECO:0000269|PubMed:11545687, ECO:0000269|PubMed:11754101, ECO:0000269|PubMed:12401890, ECO:0000269|PubMed:12408188, ECO:0000269|PubMed:12554680, ECO:0000269|PubMed:12955717, ECO:0000269|PubMed:15774455, ECO:0000269|PubMed:16098014, ECO:0000269|PubMed:16126423, ECO:0000269|PubMed:16802107, ECO:0000269|PubMed:9211849, ECO:0000269|PubMed:9634529}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; uterus corpus;superior cervical ganglion;testis - seminiferous tubule;adrenal gland;adrenal cortex;appendix;trigeminal ganglion;parietal lobe; 0.19658 0.22977 -0.047872282 50.01769285 5752.71243 15.74487 NPC1L1 1.37380138652805e-10 0.983840205062038 0.0161597948005823 NPC1 like 1 FUNCTION: Plays a major role in cholesterol homeostasis. Is critical for the uptake of cholesterol across the plasma membrane of the intestinal enterocyte. Is the direct molecular target of ezetimibe, a drug that inhibits cholesterol absorption. Lack of activity leads to multiple lipid transport defects. The protein may have a function in the transport of multiple lipids and their homeostasis, and may play a critical role in regulating lipid metabolism. Acts as a negative regulator of NPC2 and down- regulates its expression and secretion by inhibiting its maturation and accelerating its degradation. {ECO:0000269|PubMed:15928087, ECO:0000269|PubMed:22095670}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in liver. Also expressed in small intestine, pancreas, kidney, lung, pancreas, spleen, heart, gall bladder, brain, testis, stomach and muscle. {ECO:0000269|PubMed:10783261, ECO:0000269|PubMed:14976318, ECO:0000269|PubMed:15671032}.; unclassifiable (Anatomical System);pancreas;islets of Langerhans;gall bladder; fetal liver;liver;trigeminal ganglion; 0.12878 0.18680 1.377872212 94.53880632 380.20775 4.11083 NPC2 0.00870069266662882 0.800986289914481 0.19031301741889 Niemann-Pick disease, type C2 FUNCTION: Intracellular cholesterol transporter which acts in concert with NPC1 and plays an important role in the egress of cholesterol from the endosomal/lysosomal compartment. Both NPC1 and NPC2 function as the cellular 'tag team duo' (TTD) to catalyze the mobilization of cholesterol within the multivesicular environment of the late endosome (LE) to effect egress through the limiting bilayer of the LE. NPC2 binds unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes and transfers it to the cholesterol-binding pocket of the N-terminal domain of NPC1. Cholesterol binds to NPC1 with the hydroxyl group buried in the binding pocket and is exported from the limiting membrane of late endosomes/ lysosomes to the ER and plasma membrane by an unknown mechanism. The secreted form of NCP2 regulates biliary cholesterol secretion via stimulation of ABCG5/ABCG8-mediated cholesterol transport. {ECO:0000269|PubMed:17018531, ECO:0000269|PubMed:18772377, ECO:0000269|PubMed:18823126}.; DISEASE: Niemann-Pick disease C2 (NPC2) [MIM:607625]: A lysosomal storage disorder that affects the viscera and the central nervous system. It is due to defective intracellular processing and transport of low-density lipoprotein derived cholesterol. It causes accumulation of cholesterol in lysosomes, with delayed induction of cholesterol homeostatic reactions. Niemann-Pick disease type C2 has a highly variable clinical phenotype. Clinical features include variable hepatosplenomegaly and severe progressive neurological dysfunction such as ataxia, dystonia and dementia. The age of onset can vary from infancy to late adulthood. {ECO:0000269|PubMed:11125141, ECO:0000269|PubMed:11567215, ECO:0000269|PubMed:12447927, ECO:0000269|PubMed:12955717, ECO:0000269|PubMed:15937921, ECO:0000269|PubMed:16126423}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Epididymis. {ECO:0000269|PubMed:19664597}.; myocardium;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;blood;lens;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;small intestine;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;aorta; olfactory bulb;testis; 0.19835 0.22085 0.281220278 71.07808445 18.41517 0.63823 NPCDR1 . . . nasopharyngeal carcinoma, down-regulated 1 . . . . . . . . . 7899.64516 19.18412 NPDC1 0.703401664363711 0.292982516778916 0.0036158188573737 neural proliferation, differentiation and control, 1 FUNCTION: Suppresses oncogenic transformation in neural and non- neural cells and down-regulates neural cell proliferation. Might be involved in transcriptional regulation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Strongly expressed in adult brain; especially in hippocampus, frontal lobe and temporal lobe.; . . 0.14897 0.19122 -0.290161348 33.33923095 89.39143 2.03259 NPEPL1 1.80492173035865e-07 0.241920172228577 0.75807964727925 aminopeptidase-like 1 FUNCTION: Probably catalyzes the removal of unsubstituted N- terminal amino acids from various peptides.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11853319}.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;oesophagus;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13562 0.13216 -0.731092527 14.13658882 149.17566 2.66264 NPEPPS 0.999905920388338 9.40796049061771e-05 6.75588035534856e-12 aminopeptidase puromycin sensitive FUNCTION: Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. May act as regulator of neuropeptide activity. Plays a role in the antigen-processing pathway for MHC class I molecules. Involved in the N-terminal trimming of cytotoxic T-cell epitope precursors. Digests the poly-Q peptides found in many cellular proteins. Digests tau from normal brain more efficiently than tau from Alzheimer disease brain. {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:11062501, ECO:0000269|PubMed:17154549, ECO:0000269|PubMed:17318184, ECO:0000269|PubMed:19917696}.; . TISSUE SPECIFICITY: Detected in liver, epithelium of renal tubules, epithelium of small and large intestine, gastric epithelial cells, and alveoli of the lung (at protein level). {ECO:0000269|PubMed:10978616}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;brain;heart;cartilage;tongue;blood;lens;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;colon;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;thalamus;superior cervical ganglion;medulla oblongata;occipital lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.20640 0.20026 0.042348793 57.31304553 51.85467 1.42259 NPFF 0.000253702225634586 0.32332819972455 0.676418098049815 neuropeptide FF-amide peptide precursor FUNCTION: Morphine modulating peptides. Have wide-ranging physiologic effects, including the modulation of morphine-induced analgesia, elevation of arterial blood pressure, and increased somatostatin secretion from the pancreas. Neuropeptide FF potentiates and sensitizes ASIC1 and ASIC3 channels. {ECO:0000269|PubMed:11587714}.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;colon;skin;uterus;whole body;lung;epididymis;testis;germinal center;kidney;brain; . 0.06874 . 0.103030231 61.2762444 108.33954 2.25894 NPFFR1 4.68664713029487e-09 0.0162408819112486 0.983759113402104 neuropeptide FF receptor 1 FUNCTION: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system.; . . unclassifiable (Anatomical System); superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.11899 0.10483 . . 1602.3358 7.40363 NPFFR2 9.71482184173607e-06 0.550768575097805 0.449221710080353 neuropeptide FF receptor 2 FUNCTION: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system.; . TISSUE SPECIFICITY: Isoform 1 is abundant in placenta. Relatively highly expressed in thymus, testis, and small intestine. Expressed at low levels in several tissues including spleen, prostate, brain, heart, ovary, colon, kidney, lung, liver and pancreas and not expressed in skeletal muscle and leukocytes. Isoform 2 expression is highest in placenta (but at relatively low level compared to isoform 1). Very low level of expression in numerous tissues including adipose tissue and many brain regions. Isoform 3 is expressed in brain and heart and, at lower levels, in kidney, liver, lung and pancreas. {ECO:0000269|PubMed:10079187}.; unclassifiable (Anatomical System);whole body;bone;placenta;skin; superior cervical ganglion;trigeminal ganglion;cerebellum; 0.05487 0.07766 0.356452144 74.62845011 304.67673 3.71671 NPHP1 1.36518515099961e-08 0.986831155795405 0.0131688305527432 nephronophthisis 1 (juvenile) FUNCTION: Together with BCAR1 it may play a role in the control of epithelial cell polarity. Involved in the organization of apical junctions in kidney cells together with NPHP4 and RPGRIP1L/NPHP8 (By similarity). Does not seem to be strictly required for ciliogenesis (By similarity). Seems to help to recruit PTK2B/PYK2 to cell matrix adhesions, thereby initiating phosphorylation of PTK2B/PYK2 and PTK2B/PYK2-dependent signaling. May play a role in the regulation of intraflagellar transport (IFT) during cilia assembly. Required for normal retina development. In connecting photoreceptor cilia influences the movement of some IFT proteins such as IFT88 and WDR19. Involved in spermatogenesis (By similarity). {ECO:0000250}.; DISEASE: Nephronophthisis 1 (NPHP1) [MIM:256100]: An autosomal recessive inherited disease characterized by anemia, polyuria, polydipsia, isosthenuria and death in uremia. Symmetrical destruction of the kidneys involving both tubules and glomeruli occurs. The underlying pathology is a chronic tubulo-interstitial nephropathy with characteristic tubular basement membrane thickening and medullary cyst formation. Associations with extrarenal symptoms, especially ocular lesions, are frequent. The age at death ranges from about 4 to 15 years. {ECO:0000269|PubMed:10839884}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Senior-Loken syndrome 1 (SLSN1) [MIM:266900]: A renal- retinal disorder characterized by progressive wasting of the filtering unit of the kidney (nephronophthisis), with or without medullary cystic renal disease, and progressive eye disease. Typically this disorder becomes apparent during the first year of life. {ECO:0000269|PubMed:9856524}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Joubert syndrome 4 (JBTS4) [MIM:609583]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. Joubert syndrome type 4 is a phenotypically mild form. {ECO:0000269|PubMed:15138899}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widespread expression, with highest levels in pituitary gland, spinal cord, thyroid gland, testis, skeletal muscle, lymph node and trachea. Weakly expressed in heart, kidney and pancreas. Expressed in nasal epithelial cells (at protein level). {ECO:0000269|PubMed:16308564}.; unclassifiable (Anatomical System);lymphoreticular;cartilage;ovary;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;optic nerve;whole body;lung;endometrium;placenta;bone;macula lutea;testis;kidney;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.10905 0.17761 0.066214104 58.95848077 200.55285 3.06123 NPHP3 1.41114914876655e-09 0.999975717255994 2.4281332856978e-05 nephronophthisis 3 (adolescent) FUNCTION: Required for normal ciliary development and function. Inhibits disheveled-1-induced canonical Wnt-signaling activity and may also play a role in the control of non-canonical Wnt signaling which regulates planar cell polarity. Probably acts as a molecular switch between different Wnt signaling pathways. Required for proper convergent extension cell movements. {ECO:0000269|PubMed:18371931}.; DISEASE: Renal-hepatic-pancreatic dysplasia 1 (RHPD1) [MIM:208540]: A disease characterized by cystic malformations of the kidneys, liver, and pancreas. The pathological findings consist of multicystic dysplastic kidneys, dilated and dysgenetic bile ducts, a dysplastic pancreas with dilated ducts, cysts, fibrosis and inflammatory infiltrates. {ECO:0000269|PubMed:18371931}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Meckel syndrome 7 (MKS7) [MIM:267010]: A disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly. {ECO:0000269|PubMed:18371931}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed at low level. Expressed in heart, placenta, liver, skeletal muscle, kidney and pancreas. Expressed at very low level in brain and lung. {ECO:0000269|PubMed:12872122}.; smooth muscle;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;thyroid;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;lens;breast;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;liver;spleen;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; . 0.19642 -1.010461444 8.197688134 367.4987 4.05285 NPHP3-ACAD11 . . . NPHP3-ACAD11 readthrough (NMD candidate) . . . . . . . . . . . NPHP3-AS1 . . . NPHP3 antisense RNA 1 . . . . . . . . . . . NPHP4 1.29374352876183e-17 0.420064566411385 0.579935433588615 nephronophthisis 4 FUNCTION: Involved in the organization of apical junctions in kidney cells together with NPHP1 and RPGRIP1L/NPHP8. Does not seem to be strictly required for ciliogenesis. {ECO:0000250}.; DISEASE: Note=Ciliary dysfunction leads to a broad spectrum of disorders, collectively termed ciliopathies. Overlapping clinical features include retinal degeneration, renal cystic disease, skeletal abnormalities, fibrosis of various organ, and a complex range of anatomical and functional defects of the central and peripheral nervous system. The ciliopathy range of diseases includes Meckel-Gruber syndrome, Bardet-Biedl syndrome, Joubert syndrome, nephronophtisis, Senior-Loken syndrome, and Jeune asphyxiating thoracic dystrophy among others. Single-locus allelism is insufficient to explain the variable penetrance and expressivity of such disorders, leading to the suggestion that variations across multiple sites of the ciliary proteome, including NPHP4, influence the clinical outcome (PubMed:21258341). {ECO:0000269|PubMed:21258341}.; DISEASE: Senior-Loken syndrome 4 (SLSN4) [MIM:606996]: A renal- retinal disorder characterized by progressive wasting of the filtering unit of the kidney (nephronophthisis), with or without medullary cystic renal disease, and progressive eye disease. Typically this disorder becomes apparent during the first year of life. {ECO:0000269|PubMed:12244321, ECO:0000269|PubMed:15776426}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in kidney, skeletal muscle, heart and liver, and to a lesser extent in brain and lung. {ECO:0000269|PubMed:12244321}.; . . 0.12343 0.16808 0.569383166 81.78815758 1128.55982 6.40920 NPHS1 7.72410839762903e-11 0.998432313989147 0.00156768593361226 NPHS1 nephrin FUNCTION: Seems to play a role in the development or function of the kidney glomerular filtration barrier. Regulates glomerular vascular permeability. May anchor the podocyte slit diaphragm to the actin cytoskeleton. Plays a role in skeletal muscle formation through regulation of myoblast fusion (By similarity). {ECO:0000250}.; DISEASE: Nephrotic syndrome 1 (NPHS1) [MIM:256300]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. {ECO:0000269|PubMed:10652016, ECO:0000269|PubMed:11317351, ECO:0000269|PubMed:17290294, ECO:0000269|PubMed:18503012, ECO:0000269|PubMed:18614772, ECO:0000269|PubMed:20172850, ECO:0000269|PubMed:22009864, ECO:0000269|PubMed:22565185, ECO:0000269|PubMed:9660941, ECO:0000269|PubMed:9915943}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Specifically expressed in podocytes of kidney glomeruli.; lung;islets of Langerhans; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;pons;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; . 0.53507 0.683343061 84.94928049 3107.13056 10.60620 NPHS2 0.00896414230475842 0.978868154023753 0.0121677036714883 NPHS2 podocin FUNCTION: Plays a role in the regulation of glomerular permeability, acting probably as a linker between the plasma membrane and the cytoskeleton.; DISEASE: Nephrotic syndrome 2 (NPHS2) [MIM:600995]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. The disorder is resistant to steroid treatment and progresses to end- stage renal failure in the first or second decades. Some patients show later onset of the disorder. {ECO:0000269|PubMed:10742096, ECO:0000269|PubMed:15253708, ECO:0000269|PubMed:17899208, ECO:0000269|PubMed:20947785, ECO:0000269|PubMed:22565185, ECO:0000269|PubMed:22578956, ECO:0000269|PubMed:23242530, ECO:0000269|PubMed:23913389, ECO:0000269|PubMed:24072147, ECO:0000269|PubMed:24227627}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Almost exclusively expressed in the podocytes of fetal and mature kidney glomeruli.; . . 0.26596 0.26659 0.016664174 55.21939137 360.80001 4.02079 NPIPA1 0.495053838627117 0.429723800055115 0.0752223613177684 nuclear pore complex interacting protein family member A1 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11586358}.; . . 0.38431 . . . 21.22367 0.71740 NPIPA2 . . . nuclear pore complex interacting protein family member A2 . . . . . . . . . 2.85956 0.10132 NPIPA3 . . . nuclear pore complex interacting protein family member A3 . . . . . . . . . . . NPIPA5 0.544994923114436 0.399982282636708 0.0550227942488559 nuclear pore complex interacting protein family member A5 . . . . . . . . . 569.25309 4.83992 NPIPA7 . . . nuclear pore complex interacting protein family member A7 . . . . . . . . . 8.77283 0.32352 NPIPA8 . . . nuclear pore complex interacting protein family member A8 . . . . . . . . . 6.61005 0.24481 NPIPB1P . . . nuclear pore complex interacting protein family member B1, pseudogene . . . . . . . . . . . NPIPB3 0.502865157452298 0.425381677261229 0.0717531652864734 nuclear pore complex interacting protein family member B3 . . . . . . . . . 1.79035 0.05632 NPIPB4 . . . nuclear pore complex interacting protein family member B4 . . . . . . . . . 51.37695 1.41397 NPIPB5 . . . nuclear pore complex interacting protein family member B5 . . . . . . . . . 58.57075 1.55080 NPIPB6 0.636136511561843 0.335207164938546 0.028656323499611 nuclear pore complex interacting protein family member B6 . . . . . . . . . 364.15712 4.03989 NPIPB7 0.151766813480617 0.633938905619912 0.214294280899471 nuclear pore complex interacting protein family member B7 . . . . . . . . . 10.81094 0.39224 NPIPB8 0.0142295046002752 0.44319519808439 0.542575297315335 nuclear pore complex interacting protein family member B8 . . . . . . . . . 2357.32348 9.00566 NPIPB9 . . . nuclear pore complex interacting protein family member B9 . . . . . . . . . 12.50658 0.45491 NPIPB11 . . . nuclear pore complex interacting protein family member B11 . . . . . . . . . 203.86765 3.08149 NPIPB15 0.00027793232809077 0.553992949116608 0.445729118555301 nuclear pore complex interacting protein family member B15 . . . . . . . . . 760.64985 5.46640 NPIPP1 . . . nuclear pore complex interacting protein pseudogene 1 . . . smooth muscle;ovary;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;pituitary gland;testis;germinal center;brain;artery;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;spinal cord;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;aorta;stomach;cerebellum; . . . . . . . NPL 4.51265435659546e-07 0.381841105999711 0.618158442734854 N-acetylneuraminate pyruvate lyase (dihydrodipicolinate synthase) FUNCTION: Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate. It prevents sialic acids from being recycled and returning to the cell surface. Involved in the N- glycolylneuraminic acid (Neu5Gc) degradation pathway. Although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 2 is expressed in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocyte. {ECO:0000269|PubMed:16147865}.; unclassifiable (Anatomical System);heart;cartilage;hypothalamus;skin;retina;uterus;pancreas;whole body;lung;placenta;liver;spleen;kidney;brain; fetal liver;placenta;kidney;whole blood;bone marrow; 0.34777 0.58368 -0.203796826 38.81811748 73.43315 1.79088 NPLOC4 0.998697457532177 0.00130253838993325 4.07788969475712e-09 NPL4 homolog, ubiquitin recognition factor FUNCTION: The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at highest levels in brain, heart, skeletal muscle, kidney and fetal liver. {ECO:0000269|PubMed:11574150}.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;colon;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; testis - interstitial;testis; 0.25927 . -0.710864321 14.5730125 9.35712 0.34390 NPM1 0.959043977290382 0.0409368393802872 1.91833293311069e-05 nucleophosmin (nucleolar phosphoprotein B23, numatrin) FUNCTION: Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double- stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade (PubMed:22528486). {ECO:0000269|PubMed:12882984, ECO:0000269|PubMed:16107701, ECO:0000269|PubMed:17015463, ECO:0000269|PubMed:18809582, ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:20352051, ECO:0000269|PubMed:21084279, ECO:0000269|PubMed:22002061, ECO:0000269|PubMed:22528486}.; DISEASE: Note=A chromosomal aberration involving NPM1 is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with ALK. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated. {ECO:0000269|PubMed:8122112, ECO:0000269|PubMed:8633037}.; DISEASE: Note=A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA. {ECO:0000269|PubMed:8562957}.; DISEASE: Note=A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1. {ECO:0000269|PubMed:8570204}.; DISEASE: Note=Defects in NPM1 are associated with acute myelogenous leukemia (AML). Mutations in exon 12 affecting the C- terminus of the protein are associated with an aberrant cytoplasmic location. {ECO:0000269|PubMed:15659725}.; . lymphoreticular;ovary;skin;retina;bone marrow;prostate;endometrium;thyroid;bladder;brain;gall bladder;tonsil;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;kidney;stomach;aorta;thymus; tumor; 0.69972 0.57854 -0.339715008 30.06605331 9.85051 0.36100 NPM1P1 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 1 . . . . . . . . . . . NPM1P2 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 2 . . . . . . . . . . . NPM1P3 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 3 . . . . . . . . . . . NPM1P4 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 4 . . . . . . . . . . . NPM1P5 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 5 . . . . . . . . . . . NPM1P6 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 6 . . . . . . . . . . . NPM1P7 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 7 . . . . . . . . . . . NPM1P8 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 8 . . . . . . . . . . . NPM1P9 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 9 . . . . . . . . . . . NPM1P10 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 10 . . . . . . . . . . . NPM1P11 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 11 . . . . . . . . . . . NPM1P12 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 12 . . . . . . . . . . . NPM1P13 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 13 . . . . . . . . . . . NPM1P14 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 14 . . . unclassifiable (Anatomical System);liver;spleen; . . . . . . . NPM1P17 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 17 . . . . . . . . . . . NPM1P18 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 18 . . . . . . . . . . . NPM1P19 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 19 . . . . . . . . . . . NPM1P20 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 20 . . . . . . . . . . . NPM1P21 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 21 . . . . . . . . . . . NPM1P22 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 22 . . . . . . . . . . . NPM1P23 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 23 . . . . . . . . . . . NPM1P24 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 24 . . . . . . . . . . . NPM1P25 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 25 . . . . . . . . . . . NPM1P26 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 26 . . . . . . . . . . . NPM1P27 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 27 . . . . . . . . . . . NPM1P28 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 28 . . . . . . . . . . . NPM1P29 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 29 . . . . . . . . . . . NPM1P30 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 30 . . . . . . . . . . . NPM1P31 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 31 . . . . . . . . . . . NPM1P32 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 32 . . . . . . . . . . . NPM1P33 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 33 . . . . . . . . . . . NPM1P34 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 34 . . . . . . . . . . . NPM1P35 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 35 . . . . . . . . . . . NPM1P36 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 36 . . . . . . . . . . . NPM1P37 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 37 . . . . . . . . . . . NPM1P38 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 38 . . . . . . . . . . . NPM1P39 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 39 . . . . . . . . . . . NPM1P40 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 40 . . . . . . . . . . . NPM1P41 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 41 . . . . . . . . . . . NPM1P42 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 42 . . . . . . . . . . . NPM1P43 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 43 . . . . . . . . . . . NPM1P44 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 44 . . . . . . . . . . . NPM1P45 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 45 . . . . . . . . . . . NPM1P46 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 46 . . . . . . . . . . . NPM1P47 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 47 . . . . . . . . . . . NPM1P48 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 48 . . . . . . . . . . . NPM1P49 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 49 . . . . . . . . . . . NPM1P50 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 50 . . . . . . . . . . . NPM1P51 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 51 . . . . . . . . . . . NPM1P52 . . . nucleophosmin 1 (nucleolar phosphoprotein B23, numatrin) pseudogene 52 . . . . . . . . . . . NPM2 0.000671457222251747 0.742753534881182 0.256575007896567 nucleophosmin/nucleoplasmin 2 FUNCTION: Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Probably involved in sperm DNA decondensation during fertilization. {ECO:0000269|PubMed:21863821}.; . . lung;islets of Langerhans;brain;skin; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion; 0.12957 0.09000 0.393270925 76.04977589 138.35046 2.56095 NPM3 0.85917647558232 0.138656000982213 0.00216752343546749 nucleophosmin/nucleoplasmin 3 FUNCTION: May act as a chaperone.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11722795}.; . . 0.73959 0.10608 0.014844891 54.94810097 5.2041 0.19413 NPNT 7.28477742725992e-06 0.977249604984983 0.0227431102375899 nephronectin FUNCTION: Functional ligand of integrin alpha-8/beta-1 in kidney development. Regulates the expression of GDNF with integrin alpha- 8/beta-1 which is essential for kidney development. May also play a role in the development and function of various tissues, regulating cell adhesion, spreading and survival through the binding of several integrins (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in kidney and lung and to a lower extent in brain, pregnant uterus, placenta, thyroid gland and blood vessels. {ECO:0000269|PubMed:15754038}.; smooth muscle;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;oesophagus;endometrium;thyroid;bone;testis;spinal ganglion;brain;artery;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;kidney;mammary gland;stomach;aorta; trachea; 0.18295 0.10008 1.802352368 96.92734135 3116.98407 10.60876 NPPA 0.0169316348826086 0.711820304077818 0.271248061039574 natriuretic peptide A FUNCTION: Hormone playing a key role in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. Also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus. Specifically binds and stimulates the cGMP production of the NPR1 receptor. Binds the clearance receptor NPR3. {ECO:0000269|PubMed:1672777}.; DISEASE: Atrial standstill 2 (ATRST2) [MIM:615745]: A rare arrhythmia characterized by the absence of electrical and mechanical activity in the atria. Electrocardiographically, it is characterized by bradycardia, the absence of P waves, and a junctional narrow complex escape rhythm. {ECO:0000269|PubMed:23275345}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Atrial fibrillation, familial, 6 (ATFB6) [MIM:612201]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:18614783}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.07695 0.58080 0.859896574 88.62349611 1308.42229 6.80239 NPPA-AS1 . . . NPPA antisense RNA 1 . . . . . . . . . . . NPPB 0.00038006045771278 0.392500235081355 0.607119704460932 natriuretic peptide B FUNCTION: Cardiac hormone which may function as a paracrine antifibrotic factor in the heart. Also plays a key role in cardiovascular homeostasis through natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. Specifically binds and stimulates the cGMP production of the NPR1 receptor. Binds the clearance receptor NPR3. {ECO:0000269|PubMed:1672777}.; . TISSUE SPECIFICITY: Brain and also in atria, but at much lower levels than ANP.; . . 0.05989 . 0.525552348 80.57914603 41.12591 1.20388 NPPC 0.32306534692621 0.610784105632511 0.0661505474412791 natriuretic peptide C FUNCTION: Hormone which plays a role in endochondral ossification through regulation of cartilaginous growth plate chondrocytes proliferation and differentiation. May also be vasoactive and natriuretic. Specifically binds and stimulates the cGMP production of the NPR2 receptor. Binds the clearance receptor NPR3 (By similarity). {ECO:0000250, ECO:0000269|PubMed:1672777}.; . . . . 0.27433 0.24057 0.035072054 56.2514744 39.47303 1.16538 NPR1 0.000172508543840191 0.999775772021892 5.17194342676126e-05 natriuretic peptide receptor 1 FUNCTION: Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Has guanylate cyclase activity upon binding of the ligand. {ECO:0000269|PubMed:1672777}.; . . . . 0.25987 0.31819 -0.238793231 36.3116301 1510.90255 7.21833 NPR2 0.991660781814467 0.00833921815950228 2.60307150135618e-11 natriuretic peptide receptor 2 FUNCTION: Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth. {ECO:0000269|PubMed:15146390, ECO:0000269|PubMed:1672777, ECO:0000269|PubMed:24001744, ECO:0000269|PubMed:24471569}.; DISEASE: Acromesomelic dysplasia, Maroteaux type (AMDM) [MIM:602875]: An autosomal recessive acromesomelic chondrodysplasia. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). AMDM is characterized by axial skeletal involvement with wedging of vertebral bodies. In AMDM all skeletal elements are present but show abnormal rates of linear growth. {ECO:0000269|PubMed:15146390}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epiphyseal chondrodysplasia, Miura type (ECDM) [MIM:615923]: An overgrowth syndrome characterized by tall stature, long hands and feet with arachnodactyly, macrodactyly of the great toes, scoliosis, coxa valga and slipped capital femoral epiphysis. {ECO:0000269|PubMed:22870295, ECO:0000269|PubMed:23827346, ECO:0000269|PubMed:24057292, ECO:0000269|PubMed:24259409}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Short stature with non-specific skeletal abnormalities (SNSK) [MIM:616255]: A condition characterized by short stature, defined as a height less than 2 SD below normal, and no endocrine abnormalities. {ECO:0000269|PubMed:24001744, ECO:0000269|PubMed:24471569}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;larynx;thyroid;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;pineal body;adrenal cortex;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;hypothalamus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.19990 0.26645 -1.043396569 7.71408351 52.97375 1.44484 NPR3 0.00309926266837596 0.985402925257705 0.0114978120739191 natriuretic peptide receptor 3 FUNCTION: Receptor for the natriuretic peptide hormones, binding with similar affinities atrial natriuretic peptide NPPA/ANP, brain natriuretic peptide NPPB/BNP, and C-type natriuretic peptide NPPC/CNP. May function as a clearance receptor for NPPA, NPPB and NPPC, regulating their local concentrations and effects. May regulate diuresis, blood pressure and skeletal development. Does not have guanylate cyclase activity.; . . unclassifiable (Anatomical System);lymph node;heart;cartilage;tongue;sympathetic chain;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;optic nerve;lung;bone;macula lutea;liver;testis;kidney; superior cervical ganglion;salivary gland;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.75114 0.17796 -0.003562597 53.72729417 1772.52944 7.77840 NPRL2 0.345174793559064 0.654236049863242 0.000589156577694223 NPR2-like, GATOR1 complex subunit FUNCTION: Suppresses Src-dependent tyrosine phosphorylation and activation of PDPK1 and its downstream signaling. Down-regulates PDPK1 kinase activity by interfering with tyrosine phosphorylation at 'Tyr-9', 'Tyr-373' and 'Tyr-376' residues. May act as a tumor suppressor. Suppresses cell growth and enhances sensitivity to various anticancer drugs. As a component of the GATOR1 complex, inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC-containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. {ECO:0000269|PubMed:18616680, ECO:0000269|PubMed:23723238}.; . TISSUE SPECIFICITY: Most abundant in skeletal muscle, followed by brain, liver and pancreas, with lower amounts in lung, kidney, placenta and heart. Expressed in most lung cancer cell lines tested.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; . 0.21733 0.11687 -0.427900189 25.14744043 11.96438 0.43376 NPRL3 0.468162601085399 0.53070830050402 0.00112909841058109 NPR3-like, GATOR1 complex subunit FUNCTION: As a component of the GATOR1 complex, inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC- containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. {ECO:0000269|PubMed:23723238}.; . TISSUE SPECIFICITY: Widely expressed.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;blood;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;trigeminal ganglion;bone marrow; 0.16374 0.14659 -0.003562597 53.72729417 172.98896 2.86401 NPS 0.0001000801288686 0.200158900562599 0.799741019308533 neuropeptide S FUNCTION: Modulates arousal and anxiety. May play an important anorexigenic role (By similarity). Binds to its receptor NPSR1 with nanomolar affinity to increase intracellular calcium concentrations (PubMed:15312648, PubMed:16790440). {ECO:0000250, ECO:0000269|PubMed:15312648, ECO:0000269|PubMed:16790440}.; . . . . 0.00487 0.01430 0.880130671 88.9596603 413.07599 4.25510 NPSR1 8.1777016956916e-07 0.73630552484359 0.26369365738624 neuropeptide S receptor 1 FUNCTION: G-protein coupled receptor for neuropeptide S (NPS) (PubMed:16790440). Promotes mobilization of intracellular Ca(2+) stores (PubMed:16790440). Inhibits cell growth in response to NPS binding (PubMed:15947423). Involved in pathogenesis of asthma and other IgE-mediated diseases. {ECO:0000269|PubMed:15312648, ECO:0000269|PubMed:15947423, ECO:0000269|PubMed:16790440}.; . TISSUE SPECIFICITY: Isoform 4 is ubiquitous; it is detected in glandular epithelia of bronchus, stomach, small intestine, colon, uterus, esophagus, spleen, kidney, pancreas, prostate and breast. Isoform 1 is detected in uterus, colon and prostate, and in the smooth muscle cell layer in bronchial and arterial walls (at protein level) (PubMed:15947423). Isoform 1 is predominantly expressed in smooth muscle. Isoform 4 is predominantly expressed in epithelial cells. In bronchial biopsies, it is expressed in smooth muscle cells of asthma patients, but not in control patients; whereas in epithelial cells, its expression is consistently stronger in asthma patients. {ECO:0000269|PubMed:15073379, ECO:0000269|PubMed:15947423}.; iris;liver;spleen;brain;stomach; . 0.23423 0.19297 1.335644081 94.24982307 5094.13552 14.62021 NPSR1-AS1 . . . NPSR1 antisense RNA 1 . . . . . . . . . . . NPTN 0.9889178530056 0.0110783883033282 3.75869107220361e-06 neuroplastin FUNCTION: Probable homophilic and heterophilic cell adhesion molecule involved in long term potentiation at hippocampal excitatory synapses through activation of p38MAPK. May also regulate neurite outgrowth by activating the FGFR1 signaling pathway. May play a role in synaptic plasticity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed. Isoform 2 is expressed in brain cortex and cerebellum (at protein level). {ECO:0000269|PubMed:17196182, ECO:0000269|Ref.1}.; smooth muscle;ovary;sympathetic chain;substantia nigra;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;bladder;brain;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;mesenchyma;adrenal gland;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;aorta;stomach;cerebellum; whole brain;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;atrioventricular node;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.25773 0.14896 -0.449946534 24.00330267 19.08857 0.65834 NPTN-IT1 . . . NPTN intronic transcript 1 . . . . . . . . . . . NPTX1 0.426444496739896 0.566089052442718 0.00746645081738643 neuronal pentraxin 1 FUNCTION: May be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses. {ECO:0000250}.; . . unclassifiable (Anatomical System);amygdala;ovary;cartilage;cerebellum cortex;adrenal cortex;parathyroid;lens;skeletal muscle;retina;pancreas;prostate;whole body;lung;frontal lobe;cornea;adrenal gland;placenta;testis;brain;cerebellum; amygdala;whole brain;superior cervical ganglion;occipital lobe;medulla oblongata;cerebellum peduncles;temporal lobe;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.37320 0.18467 -0.291981272 33.20358575 668.26251 5.17027 NPTX2 0.0975684543323326 0.866963208647986 0.0354683370196809 neuronal pentraxin 2 FUNCTION: Likely to play role in the modification of cellular properties that underlie long-term plasticity. Binds to agar matrix in a calcium-dependent manner (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Brain, pancreas, liver, heart and skeletal muscle. Highest levels are seen in the testis.; unclassifiable (Anatomical System);medulla oblongata;islets of Langerhans;adrenal cortex;fovea centralis;choroid;lens;retina;uterus;pancreas;optic nerve;lung;endometrium;macula lutea;visual apparatus;hippocampus;pituitary gland;testis;germinal center;kidney;brain; whole brain;dorsal root ganglion;amygdala;testis - interstitial;medulla oblongata;occipital lobe;thalamus;hypothalamus;temporal lobe;adrenal cortex;pons;subthalamic nucleus;testis - seminiferous tubule;adrenal gland;globus pallidus;testis;cingulate cortex;parietal lobe;pituitary; 0.46919 0.28778 . . 84.41527 1.95597 NPTXR . . . neuronal pentraxin receptor FUNCTION: May be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses. {ECO:0000250}.; . . unclassifiable (Anatomical System);amygdala;heart;ovary;urinary;colon;skin;retina;uterus;pancreas;lung;frontal lobe;thyroid;bone;visual apparatus;hippocampus;kidney;brain;mammary gland;cerebellum; amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;temporal lobe;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; . 0.10912 . . 70.10859 1.73788 NPVF 0.00264028304563325 0.558740011475008 0.438619705479359 neuropeptide VF precursor FUNCTION: Neuropeptide RFRP-1 acts as a potent negative regulator of gonadotropin synthesis and secretion. Neuropeptides NPSF and NPVF efficiently inhibit forskolin-induced production of cAMP, but RFRP-2 shows no inhibitory activity. Neuropeptide RFRP-1 induces secretion of prolactin in rats. Neuropeptide NPVF blocks morphine- induced analgesia. {ECO:0000269|PubMed:11025660, ECO:0000269|PubMed:20027225}.; . TISSUE SPECIFICITY: Isoform 1 is specifically expressed in the retina. Neuropeptides RFRP-1 and NPVF are detected in the hypothalamus. {ECO:0000269|PubMed:11951088, ECO:0000269|PubMed:20027225}.; unclassifiable (Anatomical System);optic nerve;macula lutea;fovea centralis;choroid;lens;retina; uterus corpus;superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.19108 0.08938 0.3032669 72.009908 2823.76874 10.02405 NPW . . . neuropeptide W FUNCTION: Plays a regulatory role in the organization of neuroendocrine signals accessing the anterior pituitary gland. Stimulates water drinking and food intake. May play a role in the hypothalamic response to stress (By similarity). NPW23 activates GPR7 and GPR8 more efficiently than NPW30. {ECO:0000250}.; . TISSUE SPECIFICITY: Detected at high levels in the substantia nigra, fetal kidney and trachea; at lower levels in testis, uterus, ovary and placenta. Not detectable in many regions of the central nervous system. Also detected at high levels in lymphoblastic leukemia and colorectal adenocarcinoma.; uterus;prostate;lung;heart;islets of Langerhans;testis;colon;brain;skin; . 0.09706 0.10012 . . 1589.73494 7.37563 NPY 0.588186085546856 0.401728706131859 0.0100852083212856 neuropeptide Y FUNCTION: NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone.; . TISSUE SPECIFICITY: One of the most abundant peptides in the nervous system. Also found in some chromaffin cells of the adrenal medulla.; unclassifiable (Anatomical System);prostate;frontal lobe;islets of Langerhans;hypothalamus;placenta;sympathetic chain;alveolus;brain;peripheral nerve; dorsal root ganglion;whole brain;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;temporal lobe;adrenal cortex;atrioventricular node;caudate nucleus;pons;skeletal muscle;prostate;subthalamic nucleus;fetal brain;globus pallidus;trigeminal ganglion;parietal lobe; 0.57260 0.64138 0.21326276 67.71644256 128.38214 2.46941 NPY1R 0.651605218674681 0.342491778368604 0.00590300295671544 neuropeptide Y receptor Y1 FUNCTION: Receptor for neuropeptide Y and peptide YY. The rank order of affinity of this receptor for pancreatic polypeptides is NPY > [Pro-34] PYY, PYY and [Leu-31, Pro-34] NPY > NPY (2-36) > [Ile-31, Gln-34] PP and PYY (3-36) > PP > NPY free acid.; . . unclassifiable (Anatomical System);smooth muscle;heart;colon;skeletal muscle;retina;breast;pancreas;placenta;bone;liver;testis;kidney;brain;aorta; fetal brain;prefrontal cortex; 0.41681 0.19926 -0.183570861 39.95046001 29.23782 0.93548 NPY2R 0.188394784935151 0.761861539011059 0.0497436760537903 neuropeptide Y receptor Y2 FUNCTION: Receptor for neuropeptide Y and peptide YY. The rank order of affinity of this receptor for pancreatic polypeptides is PYY > NPY > PYY (3-36) > NPY (2-36) > [Ile-31, Gln-34] PP > [Leu- 31, Pro-34] NPY > PP, [Pro-34] PYY and NPY free acid.; . TISSUE SPECIFICITY: High levels in amygdala, corpus callosum, hippocampus and subthalamic nucleus. Also detectable in caudate nucleus, hypothalamus and substantia nigra.; unclassifiable (Anatomical System);amygdala;sympathetic chain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.28425 0.15796 -0.580403979 18.58928993 48.91254 1.36566 NPY4R 6.11597013241374e-09 0.0189782625125119 0.981021731371518 neuropeptide Y receptor Y4 FUNCTION: Receptor for neuropeptide Y and peptide YY. The rank order of affinity of this receptor for pancreatic polypeptides is PP, PP (2-36) and [Ile-31, Gln-34] PP > [Pro-34] PYY > PYY and [Leu-31, Pro-34] NPY > NPY > PYY (3-36) and NPY (2-36) > PP (13- 36) > PP (31-36) > NPY free acid.; . TISSUE SPECIFICITY: Highest levels found in brain, coronary artery and ileum. Low levels in pancreas and kidney. Detected in colon and small intestine.; . . 0.12400 0.11900 1.069238311 91.68435952 310.30902 3.74765 NPY5R 0.491800967519258 0.487324549014832 0.0208744834659106 neuropeptide Y receptor Y5 FUNCTION: Receptor for neuropeptide Y and peptide YY. The activity of this receptor is mediated by G proteins that inhibit adenylate cyclase activity. Seems to be associated with food intake. Could be involved in feeding disorders.; . TISSUE SPECIFICITY: Brain; hypothalamus.; unclassifiable (Anatomical System);brain; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.23661 0.13733 -0.139478553 43.29440906 10.8537 0.39297 NPY6R . . . neuropeptide Y receptor Y6 (pseudogene) FUNCTION: When expressed, is unable to bind pancreatic polypeptide (PP), neuropeptide Y (NPY), or peptide YY (PYY), suggesting that either it is functionally inactive or that it may have acquired a pancreatic polypeptide-independent function. {ECO:0000269|PubMed:8910290, ECO:0000269|PubMed:8910373}.; . TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, gastrointestinal tissues, spleen, brain and adrenal glands. {ECO:0000269|PubMed:8910290, ECO:0000269|PubMed:8910373}.; . . 0.65049 . . . . . NQO1 4.52404699215664e-11 0.0145364274635126 0.985463572491247 NAD(P)H dehydrogenase, quinone 1 FUNCTION: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;placenta;hippocampus;kidney;stomach;aorta; superior cervical ganglion;adipose tissue;smooth muscle;ciliary ganglion;atrioventricular node; 0.12965 0.75487 0.549415813 81.38122199 3330.11414 11.03804 NQO2 1.26932724907491e-05 0.381548811458025 0.618438495269484 NAD(P)H dehydrogenase, quinone 2 FUNCTION: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. {ECO:0000269|PubMed:18254726}.; . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;bone;thyroid;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; adrenal gland;liver;adrenal cortex;globus pallidus;kidney;skeletal muscle; 0.09392 0.22856 0.463046108 78.58575136 307.45871 3.73137 NR1D1 0.946085418280096 0.0539068433042574 7.73841564616607e-06 nuclear receptor subfamily 1 group D member 1 FUNCTION: Transcriptional repressor which coordinates circadian rhythm and metabolic pathways in a heme-dependent manner. Integral component of the complex transcription machinery that governs circadian rhythmicity and forms a critical negative limb of the circadian clock by directly repressing the expression of core clock components ARTNL/BMAL1, CLOCK and CRY1. Also regulates genes involved in metabolic functions, including lipid and bile acid metabolism, adipogenesis, gluconeogenesis and the macrophage inflammatory response. Acts as a receptor for heme which stimulates its interaction with the NCOR1/HDAC3 corepressor complex, enhancing transcriptional repression. Recognizes two classes of DNA response elements within the promoter of its target genes and can bind to DNA as either monomers or homodimers, depending on the nature of the response element. Binds as a monomer to a response element composed of the consensus half-site motif 5'-[A/G]GGTCA-3' preceded by an A/T-rich 5' sequence (RevRE), or as a homodimer to a direct repeat of the core motif spaced by two nucleotides (RevDR-2). Acts as a potent competitive repressor of ROR alpha (RORA) function and regulates the levels of its ligand heme by repressing the expression of PPARGC1A, a potent inducer of heme synthesis. Regulates lipid metabolism by repressing the expression of APOC3 and by influencing the activity of sterol response element binding proteins (SREBPs); represses INSIG2 which interferes with the proteolytic activation of SREBPs which in turn govern the rhythmic expression of enzymes with key functions in sterol and fatty acid synthesis. Regulates gluconeogenesis via repression of G6PC and PEPCK and adipocyte differentiation via repression of PPARG. Regulates glucagon release in pancreatic alpha-cells via the AMPK-NAMPT-SIRT1 pathway and the proliferation, glucose-induced insulin secretion and expression of key lipogenic genes in pancreatic-beta cells. Positively regulates bile acid synthesis by increasing hepatic expression of CYP7A1 via repression of NR0B2 and NFIL3 which are negative regulators of CYP7A1. Modulates skeletal muscle oxidative capacity by regulating mitochondrial biogenesis and autophagy; controls mitochondrial biogenesis and respiration by interfering with the STK11-PRKAA1/2-SIRT1-PPARGC1A signaling pathway. Represses the expression of SERPINE1/PAI1, an important modulator of cardiovascular disease and the expression of inflammatory cytokines and chemokines in macrophages. Represses gene expression at a distance in macrophages by inhibiting the transcription of enhancer-derived RNAs (eRNAs). Plays a role in the circadian regulation of body temperature and negatively regulates thermogenic transcriptional programs in brown adipose tissue (BAT); imposes a circadian oscillation in BAT activity, increasing body temperature when awake and depressing thermogenesis during sleep. In concert with NR2E3, regulates transcriptional networks critical for photoreceptor development and function. In addition to its activity as a repressor, can also act as a transcriptional activator. In the ovarian granulosa cells acts as a transcriptional activator of STAR which plays a role in steroid biosynthesis. In collaboration with SP1, activates GJA1 transcription in a heme-independent manner. {ECO:0000269|PubMed:12021280, ECO:0000269|PubMed:15761026, ECO:0000269|PubMed:16968709, ECO:0000269|PubMed:18006707, ECO:0000269|PubMed:19710360, ECO:0000269|PubMed:1971514, ECO:0000269|PubMed:21479263, ECO:0000269|PubMed:22184247, ECO:0000269|PubMed:23398316, ECO:0000269|PubMed:2539258}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in the liver, adipose tissue, skeletal muscle and brain. Also expressed in endothelial cells (ECs), vascular smooth muscle cells (VSMCs) and macrophages. Expression oscillates diurnally in the suprachiasmatic nucleus (SCN) of the hypothalamus as well as in peripheral tissues. Expression increases during the differentiation of pre-adipocytes into mature adipocytes. Expressed at high levels in some squamous carcinoma cell lines. {ECO:0000269|PubMed:2539258}.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;iris;brain;amygdala;cartilage;spinal cord;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;hippocampus;duodenum;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;thalamus;superior cervical ganglion;occipital lobe;medulla oblongata;olfactory bulb;cerebellum peduncles;pons;caudate nucleus;skin;skeletal muscle;prefrontal cortex;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.31694 0.20061 -0.777005578 12.9747582 78.75848 1.87384 NR1D2 0.631421779865195 0.368276459333803 0.000301760801002155 nuclear receptor subfamily 1 group D member 2 FUNCTION: Transcriptional repressor which coordinates circadian rhythm and metabolic pathways in a heme-dependent manner. Integral component of the complex transcription machinery that governs circadian rhythmicity and forms a critical negative limb of the circadian clock by directly repressing the expression of core clock components ARNTL/BMAL1 and CLOCK. Also regulates genes involved in metabolic functions, including lipid metabolism and the inflammatory response. Acts as a receptor for heme which stimulates its interaction with the NCOR1/HDAC3 corepressor complex, enhancing transcriptional repression. Recognizes two classes of DNA response elements within the promoter of its target genes and can bind to DNA as either monomers or homodimers, depending on the nature of the response element. Binds as a monomer to a response element composed of the consensus half-site motif 5'-[A/G]GGTCA-3' preceded by an A/T-rich 5' sequence (RevRE), or as a homodimer to a direct repeat of the core motif spaced by two nuclegotides (RevDR-2). Acts as a potent competitive repressor of ROR alpha (RORA) function and also negatively regulates the expression of NR1D1. Regulates lipid and energy homeostasis in the skeletal muscle via repression of genes involved in lipid metabolism and myogenesis including: CD36, FABP3, FABP4, UCP3, SCD1 and MSTN. Regulates hepatic lipid metabolism via the repression of APOC3. Represses gene expression at a distance in macrophages by inhibiting the transcription of enhancer-derived RNAs (eRNAs). In addition to its activity as a repressor, can also act as a transcriptional activator. Acts as a transcriptional activator of the sterol regulatory element-binding protein 1 (SREBF1) and the inflammatory mediator interleukin-6 (IL6) in the skeletal muscle. {ECO:0000269|PubMed:17892483, ECO:0000269|PubMed:17996965}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in the liver, adipose tissue, skeletal muscle and brain. Expression oscillates diurnally in the suprachiasmatic nucleus (SCN) of the hypothalamus as well as in peripheral tissues.; sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;cerebral cortex;larynx;thyroid;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney; superior cervical ganglion;occipital lobe;subthalamic nucleus;prefrontal cortex;trigeminal ganglion;parietal lobe;cerebellum; 0.22956 0.15835 0.088260113 60.56853031 88.31362 2.01384 NR1H2 0.821872624160323 0.177953678657954 0.000173697181723459 nuclear receptor subfamily 1 group H member 2 FUNCTION: Nuclear receptor. Binds preferentially to double- stranded oligonucleotide direct repeats having the consensus half- site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4). Regulates cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8; DLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism (By similarity). Exhibits a ligand-dependent transcriptional activation activity (PubMed:25661920). {ECO:0000250|UniProtKB:Q60644, ECO:0000269|PubMed:25661920}.; . TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;bladder;brain;ciliary body;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;temporal lobe;ciliary ganglion;caudate nucleus;atrioventricular node; 0.79654 0.75430 -0.490397599 22.50530786 3311.59288 10.99036 NR1H3 0.856185983167695 0.14371668768425 9.73291480547849e-05 nuclear receptor subfamily 1 group H member 3 FUNCTION: Nuclear receptor. Interaction with RXR shifts RXR from its role as a silent DNA-binding partner to an active ligand- binding subunit in mediating retinoid responses through target genes defined by LXRES. LXRES are DR4-type response elements characterized by direct repeats of two similar hexanuclotide half- sites spaced by four nucleotides. Plays an important role in the regulation of cholesterol homeostasis, regulating cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism (By similarity). Exhibits a ligand-dependent transcriptional activation activity (PubMed:25661920). {ECO:0000250|UniProtKB:Q9Z0Y9, ECO:0000269|PubMed:25661920}.; . TISSUE SPECIFICITY: Visceral organs specific expression. Strong expression was found in liver, kidney and intestine followed by spleen and to a lesser extent the adrenals.; . . 0.95723 0.54243 -0.646543901 16.44255721 37.64316 1.12060 NR1H4 0.161696750786205 0.837656648657839 0.000646600555955824 nuclear receptor subfamily 1 group H member 4 FUNCTION: Ligand-activated transcription factor. Receptor for bile acids such as chenodeoxycholic acid, lithocholic acid and deoxycholic acid. Represses the transcription of the cholesterol 7-alpha-hydroxylase gene (CYP7A1) through the induction of NR0B2 or FGF19 expression, via two distinct mechanisms. Activates the intestinal bile acid-binding protein (IBABP). Activates the transcription of bile salt export pump ABCB11 by directly recruiting histone methyltransferase CARM1 to this locus. {ECO:0000269|PubMed:10334992, ECO:0000269|PubMed:10334993, ECO:0000269|PubMed:12718892, ECO:0000269|PubMed:12815072, ECO:0000269|PubMed:15471871, ECO:0000269|PubMed:18621523, ECO:0000269|PubMed:19410460, ECO:0000269|PubMed:19586769}.; . . unclassifiable (Anatomical System);heart;liver;testis;spleen;blood;kidney; fetal liver;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.54158 0.65462 0.194852702 67.03231894 69.49242 1.72960 NR1H5P . . . nuclear receptor subfamily 1 group H member 5, pseudogene . . . . . . . . . . . NR1I2 0.000129416843964785 0.846347083052094 0.153523500103941 nuclear receptor subfamily 1 group I member 2 FUNCTION: Nuclear receptor that binds and is activated by variety of endogenous and xenobiotic compounds. Transcription factor that activates the transcription of multiple genes involved in the metabolism and secretion of potentially harmful xenobiotics, drugs and endogenous compounds. Activated by the antibiotic rifampicin and various plant metabolites, such as hyperforin, guggulipid, colupulone, and isoflavones. Response to specific ligands is species-specific. Activated by naturally occurring steroids, such as pregnenolone and progesterone. Binds to a response element in the promoters of the CYP3A4 and ABCB1/MDR1 genes. {ECO:0000269|PubMed:11297522, ECO:0000269|PubMed:11668216, ECO:0000269|PubMed:12578355, ECO:0000269|PubMed:18768384, ECO:0000269|PubMed:19297428, ECO:0000269|PubMed:9727070}.; . TISSUE SPECIFICITY: Expressed in liver, colon and small intestine.; lung;liver;testis;colon;spleen;stomach; superior cervical ganglion;uterus corpus;liver;pons;trigeminal ganglion;skeletal muscle; 0.45180 0.65028 -0.552898813 19.86317528 99.56266 2.15923 NR1I3 0.000355219683159767 0.951707576895908 0.0479372034209321 nuclear receptor subfamily 1 group I member 3 FUNCTION: Binds and transactivates the retinoic acid response elements that control expression of the retinoic acid receptor beta 2 and alcohol dehydrogenase 3 genes. Transactivates both the phenobarbital responsive element module of the human CYP2B6 gene and the CYP3A4 xenobiotic response element.; . TISSUE SPECIFICITY: Predominantly expressed in liver.; . . 0.33475 0.34786 -0.646543901 16.44255721 37.30618 1.11227 NR1I4 . . . nuclear receptor subfamily 1 group I member 4 . . . . . . . . . . . NR2C1 0.98233319709664 0.0176667049165164 9.79868440149149e-08 nuclear receptor subfamily 2 group C member 1 FUNCTION: Orphan nuclear receptor. Binds the IR7 element in the promoter of its own gene in an autoregulatory negative feedback mechanism. Primarily repressor of a broad range of genes. Binds to hormone response elements (HREs) consisting of two 5'-AGGTCA-3' half site direct repeat consensus sequences. Together with NR2C2, forms the core of the DRED (direct repeat erythroid-definitive) complex that represses embryonic and fetal globin transcription. Also activator of OCT4 gene expression. May be involved in stem cell proliferation and differentiation. Mediator of retinoic acid- regulated preadipocyte proliferation. {ECO:0000269|PubMed:12093804, ECO:0000269|PubMed:17010934}.; . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;optic nerve;whole body;cochlea;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;pineal body;pharynx;blood;lens;bile duct;pancreas;lung;cornea;mesenchyma;placenta;visual apparatus;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;appendix;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.19199 0.14442 -0.514264485 21.41424864 61.68056 1.60027 NR2C2 0.994140346353249 0.00585949367140173 1.59975349612202e-07 nuclear receptor subfamily 2 group C member 2 FUNCTION: Orphan nuclear receptor that can act as a repressor or activator of transcription. An important repressor of nuclear receptor signaling pathways such as retinoic acid receptor, retinoid X, vitamin D3 receptor, thyroid hormone receptor and estrogen receptor pathways. May regulate gene expression during the late phase of spermatogenesis. Together with NR2C1, forms the core of the DRED (direct repeat erythroid-definitive) complex that represses embryonic and fetal globin transcription including that of GATA1. Binds to hormone response elements (HREs) consisting of two 5'-AGGTCA-3' half site direct repeat consensus sequences. Plays a fundamental role in early embryonic development and embryonic stem cells. Required for normal spermatogenesis and cerebellum development. Appears to be important for neurodevelopmentally regulated behavior (By similarity). Activates transcriptional activity of LHCG. Antagonist of PPARA-mediated transactivation. {ECO:0000250, ECO:0000269|PubMed:10347174, ECO:0000269|PubMed:10644740, ECO:0000269|PubMed:17974920, ECO:0000269|PubMed:7779113, ECO:0000269|PubMed:9556573}.; . . unclassifiable (Anatomical System);smooth muscle;ovary;pineal body;parathyroid;skeletal muscle;bone marrow;breast;optic nerve;lung;endometrium;larynx;bone;placenta;thyroid;visual apparatus;liver;testis;head and neck;brain;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.19105 0.18410 -0.88906181 10.36801132 23.28419 0.77727 NR2C2AP 0.527167735331819 0.456701463337857 0.0161308013303232 nuclear receptor 2C2 associated protein FUNCTION: May act as a repressor of NR2C2-mediated transactivation by suppressing the binding between NR2C2/TR4 and the TR4-response element in target genes. {ECO:0000269|PubMed:12486131}.; . TISSUE SPECIFICITY: Expressed in all tissues examined, with highest expression in heart, skeletal muscle and pancreas. {ECO:0000269|PubMed:12486131}.; unclassifiable (Anatomical System);uterus;prostate;lung;cartilage;synovium;nasopharynx;colon;blood;kidney;skin;stomach; . 0.33729 0.09457 -0.075159878 47.78839349 8.91247 0.32783 NR2E1 0.990508625123308 0.00948880336798655 2.57150870518978e-06 nuclear receptor subfamily 2 group E member 1 FUNCTION: Orphan receptor that binds DNA as a monomer to hormone response elements (HRE) containing an extended core motif half- site sequence 5'-AAGGTCA-3' in which the 5' flanking nucleotides participate in determining receptor specificity (By similarity). May be required to pattern anterior brain differentiation. Involved in the regulation of retinal development and essential for vision. During retinogenesis, regulates PTEN-Cyclin D expression via binding to the promoter region of PTEN and suppressing its activity (By similarity). May be involved in retinoic acid receptor (RAR) regulation in retinal cells. {ECO:0000250}.; . TISSUE SPECIFICITY: Brain specific. Present in all brain sections tested, highest levels in the caudate nucleus and hippocampus, weakest levels in the thalamus. {ECO:0000269|PubMed:9628820}.; . . 0.65810 0.11906 -0.251530012 35.42108988 12.0367 0.43646 NR2E3 . . . nuclear receptor subfamily 2 group E member 3 FUNCTION: Orphan nuclear receptor of retinal photoreceptor cells. Transcriptional factor that is an activator of rod development and repressor of cone development. Binds the promoter region of a number of rod- and cone-specific genes, including rhodopsin, M- and S-opsin and rod-specific phosphodiesterase beta subunit. Enhances rhodopsin expression. Represses M- and S-cone opsin expression. {ECO:0000269|PubMed:15689355, ECO:0000269|PubMed:24069298}.; DISEASE: Enhanced S cone syndrome (ESCS) [MIM:268100]: Autosomal recessive retinopathy in which patients have increased sensitivity to blue light; perception of blue light is mediated by what is normally the least populous cone photoreceptor subtype, the S (short wavelength, blue) cones. ESCS is also associated with visual loss, with night blindness occurring from early in life, varying degrees of L (long, red)- and M (middle, green)-cone vision, and retinal degeneration. {ECO:0000269|PubMed:10655056, ECO:0000269|PubMed:11071390, ECO:0000269|PubMed:12963616, ECO:0000269|PubMed:15459973, ECO:0000269|PubMed:16225923, ECO:0000269|PubMed:18294254, ECO:0000269|PubMed:19006237}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa 37 (RP37) [MIM:611131]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:17564971, ECO:0000269|PubMed:19006237}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Eye specific; found solely in the outer nuclear layer of the adult neurosensory retina, where the nuclei of cone and rod photoreceptors reside. {ECO:0000269|PubMed:15689355}.; optic nerve;ovary;macula lutea;fovea centralis;skeletal muscle;retina; superior cervical ganglion;uterus corpus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.64613 0.52323 . . . . NR2F1 . . . nuclear receptor subfamily 2 group F member 1 FUNCTION: Coup (chicken ovalbumin upstream promoter) transcription factor binds to the ovalbumin promoter and, in conjunction with another protein (S300-II) stimulates initiation of transcription. Binds to both direct repeats and palindromes of the 5'-AGGTCA-3' motif. Represses transcriptional activity of LHCG. {ECO:0000269|PubMed:10644740, ECO:0000269|PubMed:11682620}.; DISEASE: Bosch-Boonstra-Schaaf optic atrophy syndrome (BBSOAS) [MIM:615722]: An autosomal dominant disorder characterized by optic atrophy associated with developmental delay and intellectual disability. Most patients also have evidence of cerebral visual impairment. {ECO:0000269|PubMed:24462372}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;colon;parathyroid;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;iris;testis;ciliary body;brain;unclassifiable (Anatomical System);hypothalamus;muscle;pharynx;skeletal muscle;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion; 0.74960 0.11262 -0.339715008 30.06605331 3.34161 0.12228 NR2F1-AS1 . . . NR2F1 antisense RNA 1 . . . . . . . . . . . NR2F2 0.916704230117823 0.0827343239698361 0.000561445912340593 nuclear receptor subfamily 2 group F member 2 FUNCTION: Ligand-activated transcription factor. Activated by high concentrations of 9-cis-retinoic acid and all-trans-retinoic acid, but not by dexamethasone, cortisol or progesterone (in vitro). Regulation of the apolipoprotein A-I gene transcription. Binds to DNA site A. {ECO:0000269|PubMed:18798693, ECO:0000269|PubMed:1899293, ECO:0000269|PubMed:9343308}.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.87052 0.29199 -0.405853867 26.23260203 4.70588 0.16913 NR2F2-AS1 . . . NR2F2 antisense RNA 1 . . . . . . . . . . . NR2F6 0.152636356323805 0.776806782046474 0.0705568616297209 nuclear receptor subfamily 2 group F member 6 FUNCTION: Transcription factor predominantly involved in transcriptional repression. Binds to promoter/enhancer response elements that contain the imperfect 5'-AGGTCA-3' direct or inverted repeats with various spacings which are also recognized by other nuclear hormone receptors. Involved in modulation of hormonal responses. Represses transcriptional activity of the lutropin-choriogonadotropic hormone receptor/LHCGR gene, the renin/REN gene and the oxytocin-neurophysin/OXT gene. Represses the triiodothyronine-dependent and -independent transcriptional activity of the thyroid hormone receptor gene in a cell type- specific manner. The corepressing function towards thyroid hormone receptor beta/THRB involves at least in part the inhibition of THRB binding to triiodothyronine response elements (TREs) by NR2F6. Inhibits NFATC transcription factor DNA binding and subsequently its transcriptional activity. Acts as transcriptional repressor of IL-17 expression in Th-17 differentiated CD4(+) T cells and may be involved in induction and/or maintenance of peripheral immunological tolerance and autoimmunity. Involved in development of forebrain circadian clock; is required early in the development of the locus coeruleus (LC). {ECO:0000269|PubMed:10644740, ECO:0000269|PubMed:10713182, ECO:0000269|PubMed:11682620, ECO:0000269|PubMed:18701084}.; . TISSUE SPECIFICITY: Expressed in heart, placenta, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:10713182}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;hypothalamus;urinary;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;medulla oblongata;subthalamic nucleus;placenta;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.18760 0.16075 . . 106.06539 2.23436 NR3C1 0.311618465710419 0.68822533660083 0.000156197688750331 nuclear receptor subfamily 3 group C member 1 FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth. Involved in chromatin remodeling. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic genes expression. {ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:17635946, ECO:0000269|PubMed:19141540, ECO:0000269|PubMed:21664385}.; DISEASE: Glucocorticoid resistance, generalized (GCCR) [MIM:615962]: An autosomal dominant disease characterized by increased plasma cortisol concentration and high urinary free cortisol, resistance to adrenal suppression by dexamethasone, and the absence of Cushing syndrome typical signs. Clinical features include hypoglycemia, hypertension, metabolic alkalosis, chronic fatigue and profound anxiety. {ECO:0000269|PubMed:11589680, ECO:0000269|PubMed:11701741, ECO:0000269|PubMed:12050230, ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:1704018, ECO:0000269|PubMed:17635946, ECO:0000269|PubMed:7683692}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. In the heart, detected in left and right atria, left and right ventricles, aorta, apex, intraventricular septum, and atrioventricular node as well as whole adult and fetal heart. {ECO:0000269|PubMed:10902803}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;bile duct;lung;pia mater;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach; dorsal root ganglion;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;whole blood;cingulate cortex;parietal lobe; 0.99538 0.92999 -0.156065314 42.16206653 135.29579 2.53062 NR3C1P1 . . . nuclear receptor subfamily 3 group C member 1 pseudogene 1 . . . . . . . . . . . NR3C2 0.925088552607185 0.0749112998189749 1.47573840454127e-07 nuclear receptor subfamily 3 group C member 2 FUNCTION: Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels. {ECO:0000269|PubMed:3037703}.; DISEASE: Pseudohypoaldosteronism 1, autosomal dominant (PHA1A) [MIM:177735]: A salt wasting disease resulting from target organ unresponsiveness to mineralocorticoids. PHA1A is a mild form characterized by target organ defects confined to kidney. Patients may present with neonatal renal salt wasting with hyperkalaemic acidosis despite high aldosterone levels. These patients improve with age and usually become asymptomatic without treatment. {ECO:0000269|PubMed:16972228}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Early-onset hypertension with severe exacerbation in pregnancy (EOHSEP) [MIM:605115]: Inheritance is autosomal dominant. The disease is characterized by the onset of severe hypertension before the age of 20, and by suppression of aldosterone secretion. {ECO:0000269|PubMed:10884226}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Highly expressed in distal tubules, convoluted tubules and cortical collecting duct in kidney, and in sweat glands. Detected at lower levels in cardiomyocytes, in epidermis and in colon enterocytes. {ECO:0000269|PubMed:11518808, ECO:0000269|PubMed:9141514}.; ovary;salivary gland;intestine;colon;choroid;fovea centralis;retina;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;testis;brain;bladder;spinal ganglion;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;pharynx;blood;lens;skeletal muscle;bile duct;lung;placenta;visual apparatus;macula lutea;liver;kidney;mammary gland;stomach;aorta; amygdala; 0.29425 0.50236 -0.352661697 29.48808681 128.61669 2.47138 NR4A1 0.959497620910649 0.0404837215404801 1.86575488707803e-05 nuclear receptor subfamily 4 group A member 1 FUNCTION: Orphan nuclear receptor. May act concomitantly with NURR1 in regulating the expression of delayed-early genes during liver regeneration. Binds the NGFI-B response element (NBRE) 5'- AAAAGGTCA-3' (By similarity). May inhibit NF-kappa-B transactivation of IL2. Participates in energy homeostasis by sequestrating the kinase STK11 in the nucleus, thereby attenuating cytoplasmic AMPK activation. {ECO:0000250, ECO:0000269|PubMed:15466594, ECO:0000269|PubMed:22983157}.; . TISSUE SPECIFICITY: Fetal muscle and adult liver, brain and thyroid.; myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.29307 0.62403 -1.241834664 5.414012739 439.58062 4.36958 NR4A2 0.991432865508232 0.00856513339870417 2.00109306377146e-06 nuclear receptor subfamily 4 group A member 2 FUNCTION: Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. It is crucial for expression of a set of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons (By similarity). {ECO:0000250, ECO:0000269|PubMed:17184956}.; . TISSUE SPECIFICITY: Expressed in a number of cell lines of T-cell, B-cell and fibroblast origin. Strong expression in brain tissue.; smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;cerebral cortex;endometrium;thyroid;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;cartilage;lacrimal gland;islets of Langerhans;blood;skeletal muscle;breast;pancreas;pia mater;lung;liver;cervix;kidney;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;olfactory bulb;trachea;cerebellum peduncles;adrenal gland;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.64744 0.60715 -0.626318434 17.03231894 29.24717 0.93603 NR4A3 . . . nuclear receptor subfamily 4 group A member 3 FUNCTION: Transcriptional activator that binds to regulatory elements in promoter regions in a cell- and response element (target)-specific manner. Induces gene expression by binding as monomers to the NR4A1 response element (NBRE) 5'-AAAAGGTCA-3' site and as homodimers to the Nur response element (NurRE) site in the promoter of their regulated target genes (By similarity). Plays a role in the regulation of proliferation, survival and differentiation of many different cell types and also in metabolism and inflammation. Mediates proliferation of vascular smooth muscle, myeloid progenitor cell and type B pancreatic cells; promotes mitogen-induced vascular smooth muscle cell proliferation through transactivation of SKP2 promoter by binding a NBRE site (By similarity). Upon PDGF stimulation, stimulates vascular smooth muscle cell proliferation by regulating CCND1 and CCND2 expression. In islets, induces type B pancreatic cell proliferation through up-regulation of genes that activate cell cycle, as well as genes that cause degradation of the CDKN1A (By similarity). Negatively regulates myeloid progenitor cell proliferation by repressing RUNX1 in a NBRE site-independent manner. During inner ear, plays a role as a key mediator of the proliferative growth phase of semicircular canal development (By similarity). Mediates also survival of neuron and smooth muscle cells; mediates CREB-induced neuronal survival, and during hippocampus development, plays a critical role in pyramidal cell survival and axonal guidance. Is required for S phase entry of the cell cycle and survival of smooth muscle cells by inducing CCND1, resulting in RB1 phosphorylation. Binds to NBRE motif in CCND1 promoter, resulting in the activation of the promoter and CCND1 transcription (By similarity). Plays also a role in inflammation; upon TNF stimulation, mediates monocyte adhesion by inducing the expression of VCAM1 and ICAM1 by binding to the NBRE consensus site (By similarity) (PubMed:20558821). In mast cells activated by Fc-epsilon receptor cross-linking, promotes the synthesis and release of cytokines but impairs events leading to degranulation (By similarity). Plays also a role in metabolism; by modulating feeding behavior; and by playing a role in energy balance by inhibiting the glucocorticoid-induced orexigenic neuropeptides AGRP expression, at least in part by forming a complex with activated NR3C1 on the AGRP- glucocorticoid response element (GRE), and thus weakening the DNA binding activity of NR3C1. Upon catecholamines stimulation, regulates gene expression that controls oxidative metabolism in skeletal muscle (By similarity). Plays a role in glucose transport by regulating translocation of the SLC2A4 glucose transporter to the cell surface (PubMed:24022864). Finally, during gastrulation plays a crucial role in the formation of anterior mesoderm by controlling cell migration. Inhibits adipogenesis (By similarity). Also participates in cardiac hypertrophy by activating PARP1 (By similarity). {ECO:0000250|UniProtKB:P51179, ECO:0000250|UniProtKB:Q9QZB6, ECO:0000269|PubMed:20558821, ECO:0000269|PubMed:24022864}.; DISEASE: Ewing sarcoma (ES) [MIM:612219]: A highly malignant, metastatic, primitive small round cell tumor of bone and soft tissue that affects children and adolescents. It belongs to the Ewing sarcoma family of tumors, a group of morphologically heterogeneous neoplasms that share the same cytogenetic features. They are considered neural tumors derived from cells of the neural crest. Ewing sarcoma represents the less differentiated form of the tumors. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving NR4A3 is found in patients with Erwing sarcoma. Translocation t(9;22)(q22- 31;q11-12) with EWSR1.; DISEASE: Note=A chromosomal aberration involving NR4A3 is a cause of a form of extraskeletal myxoid chondrosarcomas (EMC). Translocation t(9;17)(q22;q11) with TAF2N.; TISSUE SPECIFICITY: Isoform alpha is highly expressed in skeletal muscle. Isoform beta is highly expressed in skeletal muscle and low expressed in fetal brain and placenta.; unclassifiable (Anatomical System);cartilage;ovary;heart;colon;blood;skin;skeletal muscle;retina;uterus;prostate;pancreas;lung;endometrium;larynx;liver;testis;cervix;head and neck;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;adrenal cortex;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.71461 0.18411 -0.339715008 30.06605331 1958.05838 8.14638 NR5A1 0.94752349831578 0.05230130074586 0.000175200938360336 nuclear receptor subfamily 5 group A member 1 FUNCTION: Transcriptional activator. Seems to be essential for sexual differentiation and formation of the primary steroidogenic tissues. Binds to the Ad4 site found in the promoter region of steroidogenic P450 genes such as CYP11A, CYP11B and CYP21B. Also regulates the AMH/Muellerian inhibiting substance gene as well as the AHCH and STAR genes. 5'-YCAAGGYC-3' and 5'-RRAGGTCA-3' are the consensus sequences for the recognition by NR5A1. The SFPQ-NONO- NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. Binds phosphatidylcholine (By similarity). Binds phospholipids with a phosphatidylinositol (PI) headgroup, in particular PI(3,4)P2 and PI(3,4,5)P3. Activated by the phosphorylation of NR5A1 by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. {ECO:0000250, ECO:0000269|PubMed:17210646}.; DISEASE: 46,XY sex reversal 3 (SRXY3) [MIM:612965]: A condition characterized by male-to-female sex reversal in the presence of a normal 46,XY karyotype. {ECO:0000269|PubMed:10369247, ECO:0000269|PubMed:11932325, ECO:0000269|PubMed:17200175, ECO:0000269|PubMed:17694559}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Adrenocortical insufficiency, without ovarian defect (ACIWOD) [MIM:184757]: A disorder that is characterized by severe 'slackness,' muscular hypotonia. There is decreased sodium, increased potassium and elevated ACTH. {ECO:0000269|PubMed:11038323}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Premature ovarian failure 7 (POF7) [MIM:612964]: An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol. {ECO:0000269|PubMed:19246354}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spermatogenic failure 8 (SPGF8) [MIM:613957]: An infertility disorder characterized by spermatogenesis failure and severe oligozoospermia. {ECO:0000269|PubMed:20887963}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.91339 0.68017 -0.047654689 50.22410946 26.71465 0.86418 NR5A2 0.959085110774338 0.0409141049076162 7.84318046127832e-07 nuclear receptor subfamily 5 group A member 2 FUNCTION: Binds to the sequence element 5'-AACGACCGACCTTGAG-3' of the enhancer II of hepatitis B virus genes, a critical cis-element of their expression and regulation. May be responsible for the liver-specific activity of enhancer II, probably in combination with other hepatocyte transcription factors. Key regulator of cholesterol 7-alpha-hydroxylase gene (CYP7A) expression in liver. May also contribute to the regulation of pancreas-specific genes and play important roles in embryonic development.; . TISSUE SPECIFICITY: Abundantly expressed in pancreas, less in liver, very low levels in heart and lung. Expressed in the Hep-G2 cell line. Isoform 1 and isoform 2 seem to be present in fetal and adult liver and Hep-G2 cells.; unclassifiable (Anatomical System);pancreas;lung;whole body;endometrium;islets of Langerhans;hypothalamus;adrenal cortex;liver;colon;spleen;kidney;skeletal muscle; dorsal root ganglion;superior cervical ganglion;uterus corpus;adrenal cortex;atrioventricular node;trigeminal ganglion; 0.92242 0.40488 -0.291981272 33.20358575 139.12538 2.57057 NR6A1 0.992320028072041 0.00767966192775224 3.10000207267874e-07 nuclear receptor subfamily 6 group A member 1 FUNCTION: Orphan nuclear receptor. Binds to a response element containing the sequence 5'-TCAAGGTCA-3'. May be involved in the regulation of gene expression in germ cell development during gametogenesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Shows highest expression in the germ cells of the adult testis. {ECO:0000269|PubMed:8982251, ECO:0000269|PubMed:9134503, ECO:0000269|PubMed:9177477, ECO:0000269|PubMed:9493564, ECO:0000269|PubMed:9537518}.; unclassifiable (Anatomical System);lung;whole body;ovary;bone;placenta;testis;brain;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.86449 0.19571 -0.381986487 27.68931352 99.6297 2.16143 NRADDP . . . neurotrophin receptor associated death domain, pseudogene . . . . . . . . . . . NRAP 2.58648973238176e-31 0.0571142271033052 0.942885772896695 nebulin related anchoring protein FUNCTION: May be involved in anchoring the terminal actin filaments in the myofibril to the membrane and in transmitting tension from the myofibrils to the extracellular matrix. {ECO:0000250|UniProtKB:Q80XB4}.; . TISSUE SPECIFICITY: Expressed in cardiac and skeletal muscle. {ECO:0000269|PubMed:12789664}.; unclassifiable (Anatomical System);myocardium;heart;tongue;spinal cord;muscle;skin;skeletal muscle;uterus;prostate;atrium;lung;endometrium;larynx;thyroid;liver;testis;head and neck;spleen;kidney;peripheral nerve; medulla oblongata;superior cervical ganglion;heart;tongue;thyroid;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.05787 0.09828 3.124488925 99.27459306 23930.22381 32.12143 NRARP 0.150570049374677 0.633254986845833 0.21617496377949 NOTCH-regulated ankyrin repeat protein FUNCTION: Downstream effector of Notch signaling. Involved in the regulation of liver cancer cells self-renewal (PubMed:25985737). May play a role in the formation of somites (By similarity). {ECO:0000250, ECO:0000269|PubMed:25985737, ECO:0000305|PubMed:25985737}.; . . . . . 0.14061 0.191216164 66.57230479 14.14474 0.51175 NRAS 0.912772900891261 0.0865957868835444 0.000631312225194307 neuroblastoma RAS viral (v-ras) oncogene homolog FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.; DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages. {ECO:0000269|PubMed:17332249}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Noonan syndrome 6 (NS6) [MIM:613224]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. {ECO:0000269|PubMed:19966803}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: RAS-associated autoimmune leukoproliferative disorder (RALD) [MIM:614470]: A disorder of apoptosis, characterized by chronic accumulation of non-malignant lymphocytes, defective lymphocyte apoptosis, and an increased risk for the development of hematologic malignancies. {ECO:0000269|PubMed:17517660}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Melanocytic nevus syndrome, congenital (CMNS) [MIM:137550]: A syndrome characterized by congenital pigmentary skin lesions which can occur at any site and can cover most of the body surface. These lesions may or may not be hairy. Congenital melanocytic nevi are associated with neuromelanosis (the presence of melanin-producing cells within the brain parenchyma or leptomeninges). Less commonly they are associated with malignant melanoma in childhood, both in the skin and the central nervous system. CMNS patients also tend to have a characteristic facial appearance, including wide or prominent forehead, periorbital fullness, small short nose with narrow nasal bridge, round face, full cheeks, prominent premaxilla, and everted lower lip. {ECO:0000269|PubMed:18633438, ECO:0000269|PubMed:23392294}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Melanosis, neurocutaneous (NCMS) [MIM:249400]: A rare congenital disease characterized by the presence of giant or multiple melanocytic nevi on the skin, foci of melanin-producing cells within the brain parenchyma, and infiltration of leptomeninges by abnormal melanin deposits. Neurologic abnormalities include seizures, hydrocephalus, arachnoid cysts, tumors, and syringomyelia. Some patients may develop malignant melanoma. {ECO:0000269|PubMed:23392294}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Keratinocytic non-epidermolytic nevus (KNEN) [MIM:162900]: Epidermal nevi of the common, non-organoid and non- epidermolytic type are benign skin lesions and may vary in their extent from a single (usually linear) lesion to widespread and systematized involvement. They may be present at birth or develop early during childhood. {ECO:0000269|PubMed:22499344}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.99971 0.12378 0.013025609 54.62962963 3.64814 0.13463 NRAV . . . negative regulator of antiviral response (non-protein coding) . . . . . . . . . . . NR0B1 0.791995494731047 0.201918233930728 0.00608627133822449 nuclear receptor subfamily 0 group B member 1 FUNCTION: Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency (By similarity). {ECO:0000250}.; DISEASE: X-linked adrenal hypoplasia congenital (XL-AHC) [MIM:300200]: Developmental disorder of the adrenal gland that results in profound hormonal deficiencies and is lethal if untreated. It is characterized by the absence of the permanent zone of the adrenal cortex and by a structural disorganization of the glands. Hypogonadotropic hypogonadism (HHG) is frequently associated with this disorder. HHG is a condition resulting from or characterized by abnormally decreased gonadal function, with retardation of growth and sexual development. {ECO:0000269|PubMed:10323730, ECO:0000269|PubMed:10341858, ECO:0000269|PubMed:10675358, ECO:0000269|PubMed:11113848, ECO:0000269|PubMed:11443184, ECO:0000269|PubMed:11748852, ECO:0000269|PubMed:11788621, ECO:0000269|PubMed:12629128, ECO:0000269|PubMed:15800903, ECO:0000269|PubMed:7990958, ECO:0000269|PubMed:9003500, ECO:0000269|PubMed:9063431, ECO:0000269|PubMed:9360549, ECO:0000269|PubMed:9529340}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: 46,XY sex reversal 2 (SRXY2) [MIM:300018]: A condition characterized by male-to-female sex reversal in the presence of a normal 46,XY karyotype. {ECO:0000269|PubMed:9486644}. Note=The disease is caused by mutations affecting the gene represented in this entry. XY individuals with a duplication of part of the short arm of the X chromosome and an intact SRY gene develop as females. The single X chromosome in these individuals does not undergo X- chromosome inactivation; therefore, these individuals presumably carry 2 active copies of genes, including the NR0B1 gene, in the duplicated region. Individuals with deletion of this region develop as males. Genes within the dosage-sensitive sex reversal region are, therefore, not essential for testis development, but, when present in a double dose, interfere with testis formation.; . . . 0.64126 0.61027 -0.494039303 22.09247464 24.92876 0.81890 NR0B2 5.83479715619009e-08 0.0369402372823879 0.963059704369641 nuclear receptor subfamily 0 group B member 2 FUNCTION: Acts as a transcriptional regulator. Acts as a negative regulator of receptor-dependent signaling pathways. Specifically inhibits transactivation of the nuclear receptor with whom it interacts. Inhibits transcriptional activity of NEUROD1 on E-box- containing promoter by interfering with the coactivation function of the p300/CBP-mediated trancription complex for NEUROD1. {ECO:0000269|PubMed:14752053}.; DISEASE: Obesity (OBESITY) [MIM:601665]: A condition characterized by an increase of body weight beyond the limitation of skeletal and physical requirements, as the result of excessive accumulation of body fat. {ECO:0000269|PubMed:11136233}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver. Low levels of expression were detected in heart and pancreas. {ECO:0000269|PubMed:8650544}.; unclassifiable (Anatomical System);pancreas;lung;heart;liver;testis;spleen;kidney;stomach; liver;trigeminal ganglion;skeletal muscle; 0.67563 0.66122 -0.025608647 51.91672564 397.54169 4.18993 NRBF2 0.0821062414135336 0.87183050477831 0.0460632538081567 nuclear receptor binding factor 2 FUNCTION: May modulate transcriptional activation by target nuclear receptors. Can act as transcriptional activator (in vitro). {ECO:0000269|PubMed:15610520}.; . TISSUE SPECIFICITY: Detected in keratinocytes, liver and placenta (PubMed:15610520). Expressed in a subset of cells in pediatric medulloblastoma (PubMed:18619852). {ECO:0000269|PubMed:15610520, ECO:0000269|PubMed:18619852}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;frontal lobe;bone;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;breast;lung;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney; trigeminal ganglion;whole blood; 0.84854 0.10163 0.525552348 80.57914603 54.15187 1.46781 NRBF2P1 . . . nuclear receptor binding factor 2 pseudogene 1 . . . . . . . . . . . NRBF2P2 . . . nuclear receptor binding factor 2 pseudogene 2 . . . . . . . . . . . NRBF2P3 . . . nuclear receptor binding factor 2 pseudogene 3 . . . . . . . . . . . NRBF2P4 . . . nuclear receptor binding factor 2 pseudogene 4 . . . . . . . . . . . NRBF2P5 . . . nuclear receptor binding factor 2 pseudogene 5 . . . . . . . . . . . NRBP1 0.999548511025196 0.000451488666432833 3.0837066184899e-10 nuclear receptor binding protein 1 FUNCTION: May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases. Binding to the NS3 protein of dengue virus type 2 appears to subvert this activity into the alteration of the intracellular membrane structure associated with flaviviral replication. {ECO:0000269|PubMed:11956649, ECO:0000269|PubMed:15084397, ECO:0000303|PubMed:11956649}.; . TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined with high levels in the testis. {ECO:0000269|PubMed:10843813}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;testis; 0.12588 0.12378 -0.271755481 34.31823543 113.73854 2.32405 NRBP2 0.00241294545324528 0.927375310056955 0.0702117444897998 nuclear receptor binding protein 2 FUNCTION: May regulate apoptosis of neural progenitor cells during their differentiation. {ECO:0000250}.; . . ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;stomach;aorta; pons;parietal lobe; 0.14009 . . . 302.68543 3.70523 NRCAM 0.456484598308671 0.543515398204428 3.48690051831786e-09 neuronal cell adhesion molecule FUNCTION: Cell adhesion protein that is required for normal responses to cell-cell contacts in brain and in the peripheral nervous system. Plays a role in neurite outgrowth in response to contactin binding. Plays a role in mediating cell-cell contacts between Schwann cells and axons. Plays a role in the formation and maintenance of the nodes of Ranvier on myelinated axons. Nodes of Ranvier contain clustered sodium channels that are crucial for the saltatory propagation of action potentials along myelinated axons. During development, nodes of Ranvier are formed by the fusion of two heminodes. Required for normal clustering of sodium channels at heminodes; not required for the formation of mature nodes with normal sodium channel clusters. Required, together with GLDN, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier. {ECO:0000250|UniProtKB:Q810U4}.; . TISSUE SPECIFICITY: Detected in all the examined tissues. In the brain it was detected in the amygdala, caudate nucleus, corpus callosum, hippocampus, hypothalamus, substantia nigra, subthalamic nucleus and thalamus.; ovary;sympathetic chain;parathyroid;substantia nigra;fovea centralis;choroid;vein;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;testis;pineal gland;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;hippocampus;visual apparatus;alveolus;kidney; dorsal root ganglion;amygdala;whole brain;superior cervical ganglion;occipital lobe;thalamus;medulla oblongata;testis - interstitial;hypothalamus;temporal lobe;pons;atrioventricular node;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.48559 0.25070 -1.366884746 4.505779665 161.09406 2.77224 NRDC . . . nardilysin convertase FUNCTION: Cleaves peptide substrates on the N-terminus of arginine residues in dibasic pairs.; . TISSUE SPECIFICITY: Primarily in adult heart, skeletal muscle, and testis and at much lower levels in other tissues.; . . 0.53838 0.10330 -1.03613328 7.843831092 . . NRDE2 6.49344106983731e-10 0.991255240065238 0.00874475928541817 NRDE-2, necessary for RNA interference, domain containing . . . . . 0.06778 0.09826 0.281016493 70.87756546 413.62891 4.25984 NREP 0.563643143236761 0.387749285662164 0.0486075711010747 neuronal regeneration related protein FUNCTION: May have roles in neural function. Ectopic expression augments motility of gliomas. Promotes also axonal regeneration (By similarity). May also have functions in cellular differentiation (By similarity). Induces differentiation of fibroblast into myofibroblast and myofibroblast ameboid migration. Increases retinoic-acid regulation of lipid-droplet biogenesis (By similarity). Down-regulates the expression of TGFB1 and TGFB2 but not of TGFB3 (By similarity). May play a role in the regulation of alveolar generation. {ECO:0000250, ECO:0000269|PubMed:11358844, ECO:0000269|PubMed:16229809}.; . TISSUE SPECIFICITY: Expressed in lung (at protein level). {ECO:0000269|PubMed:16484684}.; . . 0.35283 . 0.72397987 85.91648974 72.00969 1.76680 NREP-AS1 . . . NREP antisense RNA 1 . . . . . . . . . . . NRF1 0.996970242690309 0.0030295994084876 1.5790120341632e-07 nuclear respiratory factor 1 FUNCTION: Transcription factor that activates the expression of the EIF2S1 (EIF2-alpha) gene. Links the transcriptional modulation of key metabolic genes to cellular growth and development. Implicated in the control of nuclear genes required for respiration, heme biosynthesis, and mitochondrial DNA transcription and replication.; . TISSUE SPECIFICITY: Ubiquitously expressed with strongest expression in skeletal muscle.; colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;macula lutea;visual apparatus;liver;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle;bone marrow; 0.24788 . -0.449946534 24.00330267 8.75807 0.32233 NRG1 0.947798761974756 0.0521997940021905 1.44402305313546e-06 neuregulin 1 FUNCTION: Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. The multiple isoforms perform diverse functions such as inducing growth and differentiation of epithelial, glial, neuronal, and skeletal muscle cells; inducing expression of acetylcholine receptor in synaptic vesicles during the formation of the neuromuscular junction; stimulating lobuloalveolar budding and milk production in the mammary gland and inducing differentiation of mammary tumor cells; stimulating Schwann cell proliferation; implication in the development of the myocardium such as trabeculation of the developing heart. Isoform 10 may play a role in motor and sensory neuron development. {ECO:0000269|PubMed:1348215, ECO:0000269|PubMed:7902537}.; DISEASE: Note=A chromosomal aberration involving NRG1 produces gamma-heregulin. Translocation t(8;11) with TENM4. The translocation fuses the 5'-end of TENM4 to NRG1 (isoform 8). The product of this translocation was first thought to be an alternatively spliced isoform. Gamma-heregulin is a soluble activating ligand for the ERBB2-ERBB3 receptor complex and acts as an autocrine growth factor in a specific breast cancer cell line (MDA-MB-175). Not detected in breast carcinoma samples, including ductal, lobular, medullary, and mucinous histological types, neither in other breast cancer cell lines.; TISSUE SPECIFICITY: Type I isoforms are the predominant forms expressed in the endocardium. Isoform alpha is expressed in breast, ovary, testis, prostate, heart, skeletal muscle, lung, placenta liver, kidney, salivary gland, small intestine and brain, but not in uterus, stomach, pancreas, and spleen. Isoform 3 is the predominant form in mesenchymal cells and in non-neuronal organs, whereas isoform 6 is the major neuronal form. Isoform 8 is expressed in spinal cord and brain. Isoform 9 is the major form in skeletal muscle cells; in the nervous system it is expressed in spinal cord and brain. Also detected in adult heart, placenta, lung, liver, kidney, and pancreas. Isoform 10 is expressed in nervous system: spinal cord motor neurons, dorsal root ganglion neurons, and brain. Predominant isoform expressed in sensory and motor neurons. Not detected in adult heart, placenta, lung, liver, skeletal muscle, kidney, and pancreas. Not expressed in fetal lung, liver and kidney. Type IV isoforms are brain-specific. {ECO:0000269|PubMed:17565985}.; unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;colon;parathyroid;fovea centralis;pancreas;frontal lobe;larynx;bone;placenta;macula lutea;amnion;liver;testis;head and neck;kidney;spinal ganglion;mammary gland;brain;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.87877 0.60823 1.072886248 91.70794999 7029.68062 17.87534 NRG1-IT1 . . . NRG1 intronic transcript 1 . . . . . . . . . . . NRG1-IT3 . . . NRG1 intronic transcript 3 . . . . . . . . . . . NRG2 0.995154288008006 0.0048456114300886 1.00561905496729e-07 neuregulin 2 FUNCTION: Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. May also promote the heterodimerization with the EGF receptor.; . TISSUE SPECIFICITY: Restricted to the cerebellum in the adult.; unclassifiable (Anatomical System);lung;ovary;islets of Langerhans;bone;placenta;testis;parathyroid;brain;thymus; uterus corpus;superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.87096 0.14813 . . 357.16396 4.00512 NRG3 0.210337990089114 0.789584347569158 7.76623417286177e-05 neuregulin 3 FUNCTION: Direct ligand for the ERBB4 tyrosine kinase receptor. Binding results in ligand-stimulated tyrosine phosphorylation and activation of the receptor. Does not bind to the EGF receptor, ERBB2 or ERBB3 receptors. May be a survival factor for oligodendrocytes. {ECO:0000269|PubMed:16478787, ECO:0000269|PubMed:9275162}.; . TISSUE SPECIFICITY: Highly expressed in most regions of the brain with the exception of corpus callosum. Expressed at lower level in testis. Not detected in heart, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, ovary, small intestine, colon and peripheral blood leukocytes.; . . 0.15680 0.10280 -0.464712395 23.5727766 868.61501 5.74237 NRG3-AS1 . . . NRG3 antisense RNA 1 . . . . . . . . . . . NRG4 0.0243875467702028 0.776856136666136 0.198756316563661 neuregulin 4 FUNCTION: Low affinity ligand for the ERBB4 tyrosine kinase receptor. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. Does not bind to the ERBB1, ERBB2 and ERBB3 receptors (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;larynx;testis;head and neck; dorsal root ganglion;superior cervical ganglion;testis - interstitial;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.06755 0.08128 0.191216164 66.57230479 70.25627 1.74219 NRGN 0.536942023282865 0.405084010806187 0.0579739659109485 neurogranin FUNCTION: Acts as a "third messenger" substrate of protein kinase C-mediated molecular cascades during synaptic development and remodeling. Binds to calmodulin in the absence of calcium (By similarity). {ECO:0000250}.; . . ovary;adrenal medulla;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;blood;lens;lung;epididymis;hippocampus;macula lutea;liver;spleen;kidney;stomach; amygdala;whole brain;occipital lobe;medulla oblongata;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;whole blood;cingulate cortex;parietal lobe; 0.39546 0.19444 . . . . NRIP1 0.991172158226933 0.00882740583035223 4.35942715177398e-07 nuclear receptor interacting protein 1 FUNCTION: Modulates transcriptional activation by steroid receptors such as NR3C1, NR3C2 and ESR1. Also modulates transcriptional repression by nuclear hormone receptors. Positive regulator of the circadian clock gene expression: stimulates transcription of ARNTL/BMAL1, CLOCK and CRY1 by acting as a coactivator for RORA and RORC. {ECO:0000269|PubMed:10364267, ECO:0000269|PubMed:11509661, ECO:0000269|PubMed:11518808, ECO:0000269|PubMed:12554755, ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:21628546, ECO:0000269|PubMed:7641693}.; . . colon;parathyroid;vein;skin;uterus;prostate;whole body;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);heart;islets of Langerhans;adrenal cortex;pharynx;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;visual apparatus;alveolus;liver;head and neck;kidney;aorta; superior cervical ganglion;prefrontal cortex;skeletal muscle; 0.82566 0.19891 1.387050485 94.63906582 1330.90849 6.85481 NRIP2 9.12047384069789e-08 0.168075485785188 0.831924423010074 nuclear receptor interacting protein 2 FUNCTION: Down-regulates transcriptional activation by nuclear receptors such as NR1F2. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymphoreticular;heart;colon;fovea centralis;choroid;lens;retina;optic nerve;lung;cerebral cortex;larynx;nasopharynx;placenta;macula lutea;hippocampus;head and neck;mammary gland;cerebellum; dorsal root ganglion;testis - interstitial;occipital lobe;thalamus;superior cervical ganglion;olfactory bulb;cerebellum peduncles;ciliary ganglion;atrioventricular node;cerebellum; 0.07424 0.08683 -0.358119787 29.16371786 57.47479 1.52864 NRIP3 2.34631014081811e-05 0.501587461397401 0.49838907550119 nuclear receptor interacting protein 3 . . . unclassifiable (Anatomical System);ovary;cartilage;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;pancreas;optic nerve;lung;adrenal gland;placenta;bone;macula lutea;hippocampus;liver;testis;spleen;brain; dorsal root ganglion;amygdala;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;testis - interstitial;cerebellum peduncles;temporal lobe;pons;atrioventricular node;subthalamic nucleus;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.10654 . 0.148941568 64.31941496 105.28116 2.22063 NRIR . . . negative regulator of interferon response (non-protein coding) . . . . . . . . . . . NRK 0.763369951142185 0.23662991771023 1.31147584802052e-07 Nik related kinase FUNCTION: May phosphorylate cofilin-1 and induce actin polymerization through this process, during the late stages of embryogenesis. Involved in the TNF-alpha-induced signaling pathway (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;skin;uterus;pancreas;prostate;whole body;lung;adrenal gland;bone;placenta;visual apparatus;liver;testis;spleen;kidney; . 0.32580 0.31202 . . 2428.62657 9.15478 NRL 0.0797351085798011 0.753718216651323 0.166546674768875 neural retina leucine zipper FUNCTION: Transcription factor which regulates the expression of several rod-specific genes, in cluding RHO and PDE6B. {ECO:0000250}.; DISEASE: Retinitis pigmentosa 27 (RP27) [MIM:613750]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:10192380, ECO:0000269|PubMed:22334370}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Retinal degeneration autosomal recessive clumped pigment type (RDCP) [MIM:162080]: A retinopathy characterized by night blindness since early childhood, consistent with a severe reduction in rod function. Color vision is normal although there is a relatively enhanced function of short-wavelength-sensitive cones in the macula. Signs of retinal degeneration and clusters of clumped pigment deposits in the peripheral fundus at the level of the retinal pigment epithelium are present. {ECO:0000269|PubMed:15591106}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Neural retina.; . . 0.86356 0.42194 . . 19.01373 0.65679 NRM 0.142577186791213 0.779059245141488 0.0783635680672984 nurim (nuclear envelope membrane protein) . . . lymphoreticular;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;heart;cartilage;muscle;blood;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;amnion;head and neck;kidney; superior cervical ganglion;atrioventricular node; 0.13518 . 0.014844891 54.94810097 81.08439 1.90609 NRN1 0.823897693087707 0.17220012295799 0.00390218395430363 neuritin 1 FUNCTION: Promotes neurite outgrowth and especially branching of neuritic processes in primary hippocampal and cortical cells. {ECO:0000250}.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;skin;retina;uterus;whole body;cerebral cortex;endometrium;bone;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;muscle;pharynx;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland; whole brain;amygdala;occipital lobe;subthalamic nucleus;medulla oblongata;cerebellum peduncles;temporal lobe;globus pallidus;pons;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.51462 0.15495 0.147123112 64.11299835 22.02062 0.73998 NRN1L 0.000386710849157266 0.395678857190381 0.603934431960462 neuritin 1 like . . . unclassifiable (Anatomical System);whole body;islets of Langerhans;placenta;visual apparatus;retina; . 0.11416 . 0.905808022 89.4373673 1489.44633 7.18105 NRON . . . non-protein coding RNA, repressor of NFAT . . . . . . . . . . . NRP1 0.996035953147062 0.00396404634275357 5.10184095268186e-10 neuropilin 1 FUNCTION: The membrane-bound isoform 1 is a receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. It mediates the chemorepulsant activity of semaphorins. It binds to semaphorin 3A, The PLGF-2 isoform of PGF, The VEGF-165 isoform of VEGF and VEGF-B. Coexpression with KDR results in increased VEGF-165 binding to KDR as well as increased chemotaxis. It may regulate VEGF-induced angiogenesis.; . TISSUE SPECIFICITY: The expression of isoforms 1 and 2 does not seem to overlap. Isoform 1 is expressed by the blood vessels of different tissues. In the developing embryo it is found predominantly in the nervous system. In adult tissues, it is highly expressed in heart and placenta; moderately in lung, liver, skeletal muscle, kidney and pancreas; and low in adult brain. Isoform 2 is found in liver hepatocytes, kidney distal and proximal tubules.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;amniotic fluid;brain;gall bladder;heart;cartilage;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;mesenchyma;placenta;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;smooth muscle;heart;placenta;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.55370 0.31930 -0.484940685 22.75300778 1287.3147 6.75480 NRP2 0.0017116502518865 0.998241695276228 4.66544718852771e-05 neuropilin 2 FUNCTION: High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;oesophagus;endometrium;synovium;bone;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;heart;temporal lobe;pons;atrioventricular node;skeletal muscle;uterus corpus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.30972 0.15109 -1.080231599 7.277659825 168.69076 2.83534 NRROS 0.457686197904668 0.536397728747274 0.0059160733480579 negative regulator of reactive oxygen species FUNCTION: Negative regulator of reactive oxygen species (ROS) that limits ROS production by phagocytes during inflammatory response, thereby playing a role during host defense. Acts via direct interaction with CYBB/NOX2 monomer that impairs interaction between CYBB/NOX2 and CYBA/p22-phox and formation of a stable NOX2 complex (By similarity). May play a critical role in desensitizing TLR signaling through inhibition of Toll-like receptor-mediated NF-kappa-B activation and cytokine production. {ECO:0000250, ECO:0000269|PubMed:23545260}.; . TISSUE SPECIFICITY: Ubiquitous, with high level of expression found in bone marrow, thymus, liver, lung, intestine and spleen. {ECO:0000269|PubMed:23545260}.; . . 0.41725 . -0.683363435 15.36329323 56.29039 1.50691 NRSN1 0.00430725148247795 0.664429679022083 0.331263069495439 neurensin 1 FUNCTION: May play an important role in neural organelle transport, and in transduction of nerve signals or in nerve growth. May play a role in neurite extension. May play a role in memory consolidation (By similarity). {ECO:0000250|UniProtKB:P97799, ECO:0000269|PubMed:12463420}.; . TISSUE SPECIFICITY: Expressed in brain. Not detectable in other tissues tested. {ECO:0000269|PubMed:12463420}.; . . 0.09070 0.10273 -0.073340031 48.11866006 73.97355 1.79659 NRSN2 0.00197331172132976 0.497025179763159 0.501001508515511 neurensin 2 FUNCTION: May play a role in maintenance and/or transport of vesicles.; . . . . 0.15867 0.09641 0.17280645 65.75843359 1003.69741 6.10174 NRSN2-AS1 . . . NRSN2 antisense RNA 1 . . . . . . . . . . . NRTN 0.100149118623238 0.77241038687516 0.127440494501602 neurturin FUNCTION: Supports the survival of sympathetic neurons in culture. May regulate the development and maintenance of the CNS. Might control the size of non-neuronal cell population such as haemopoietic cells.; DISEASE: Note=Genetic variations in NRTN may contribute to Hirschsprung disease, in association with mutations of RET gene, and possibly mutations in other loci. Hirschsprung disease is a disorder of neural crest development is characterized by the absence of intramural ganglion cells in the hindgut, often resulting in intestinal obstruction. {ECO:0000269|PubMed:9700200}.; . optic nerve;lung;islets of Langerhans;macula lutea;muscle;colon;fovea centralis;choroid;lens;retina; superior cervical ganglion;temporal lobe;spinal cord;liver;trigeminal ganglion;fetal thyroid;skeletal muscle; 0.15132 0.21020 . . 496.17675 4.57859 NRXN1 0.999948738356297 5.12616436900203e-05 1.27524581181075e-14 neurexin 1 FUNCTION: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion by forming intracellular junctions through binding to neuroligins. May play a role in formation or maintenance of synaptic junctions. May mediate intracellular signaling. May play a role in angiogenesis (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;frontal lobe;cochlea;islets of Langerhans;liver;testis;kidney;brain;skeletal muscle;aorta; dorsal root ganglion;whole brain;amygdala;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.09022 . -1.787693635 2.246992215 110.12577 2.28141 NRXN2 0.999895574015252 0.000104425984676312 7.21667723548835e-14 neurexin 2 FUNCTION: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion.; . . unclassifiable (Anatomical System);amygdala;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;frontal lobe;thyroid;bone;macula lutea;visual apparatus;testis;kidney;brain; dorsal root ganglion;amygdala;whole brain;superior cervical ganglion;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;atrioventricular node;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.24191 0.10189 -2.164449385 1.427223402 1296.88776 6.77694 NRXN3 0.999855500755767 0.000144499225015791 1.92167040578683e-11 neurexin 3 FUNCTION: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May play a role in angiogenesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the blood vessel walls (at protein level). {ECO:0000269|PubMed:19926856}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;aorta; dorsal root ganglion;whole brain;amygdala;medulla oblongata;thalamus;occipital lobe;superior cervical ganglion;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.61924 0.11925 -1.548724932 3.273177636 47.34272 1.33505 NSA2 0.686235240727363 0.312875153436806 0.000889605835830562 NSA2, ribosome biogenesis homolog FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. May play a part in the quality control of pre-60S particles (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;synovium;bone;testis;artery;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;duodenum;kidney;stomach;aorta; superior cervical ganglion;testis - seminiferous tubule;white blood cells;trigeminal ganglion; . . -0.383807564 27.41802312 98.21908 2.14284 NSD1 0.999999999179163 8.20837166672382e-10 2.65740686219434e-26 nuclear receptor binding SET domain protein 1 FUNCTION: Histone methyltransferase. Preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4 (in vitro). Transcriptional intermediary factor capable of both negatively or positively influencing transcription, depending on the cellular context. {ECO:0000269|PubMed:21196496}.; DISEASE: Beckwith-Wiedemann syndrome (BWS) [MIM:130650]: A disorder characterized by anterior abdominal wall defects including exomphalos (omphalocele), pre- and postnatal overgrowth, and macroglossia. Additional less frequent complications include specific developmental defects and a predisposition to embryonal tumors. {ECO:0000269|PubMed:14997421}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving NSD1 is found in childhood acute myeloid leukemia. Translocation t(5;11)(q35;p15.5) with NUP98.; DISEASE: Note=A chromosomal aberration involving NSD1 is found in an adult form of myelodysplastic syndrome (MDS). Insertion of NUP98 into NSD1 generates a NUP98-NSD1 fusion product. {ECO:0000269|PubMed:15382262}.; TISSUE SPECIFICITY: Expressed in the fetal/adult brain, kidney, skeletal muscle, spleen, and the thymus, and faintly in the lung.; myocardium;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;germinal center;brain;heart;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;lung;cornea;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;testis - interstitial;fetal liver;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.66088 0.24150 -1.552781294 3.237791932 2326.46017 8.93558 NSDHL 0.940558049226598 0.0592024804268681 0.000239470346533647 NAD(P) dependent steroid dehydrogenase-like FUNCTION: Involved in the sequential removal of two C-4 methyl groups in post-squalene cholesterol biosynthesis. {ECO:0000269|PubMed:14506130}.; DISEASE: CK syndrome (CKS) [MIM:300831]: A disorder characterized by mild to severe cognitive impairment, seizures, microcephaly, cerebral cortical malformations, dysmorphic facial features, and thin body habitus. {ECO:0000269|PubMed:21129721}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Brain, heart, liver, lung, kidney, skin and placenta.; . . 0.08041 0.18938 -0.201976964 38.98325077 20.58651 0.69988 NSF 0.713682130183303 0.286180941386584 0.000136928430113278 N-ethylmaleimide sensitive factor FUNCTION: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin. Interaction with AMPAR subunit GRIA2 leads to influence GRIA2 membrane cycling (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;germinal center;bladder;brain;amygdala;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;kidney;stomach;cerebellum; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.54424 0.29957 . . 13.46033 0.48907 NSFL1C 0.159362129254894 0.837377543729625 0.00326032701548009 NSFL1 (p97) cofactor (p47) FUNCTION: Reduces the ATPase activity of VCP. Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis. May play a role in VCP- mediated formation of transitional endoplasmic reticulum (tER) (By similarity). Inhibits the activity of CTSL (in vitro). {ECO:0000250}.; . . lymphoreticular;myocardium;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;oral cavity;muscle;bile duct;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;whole brain;superior cervical ganglion;prefrontal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex;parietal lobe; 0.18377 0.13185 -0.203796826 38.81811748 3937.05807 12.39786 NSFP1 . . . N-ethylmaleimide-sensitive factor pseudogene 1 . . . . . . . . . . . NSL1 0.043155916748521 0.929416496757575 0.0274275864939039 NSL1, MIS12 kinetochore complex component FUNCTION: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. {ECO:0000269|PubMed:16585270}.; . . . . 0.14391 0.11428 0.260991686 70.25831564 711.86266 5.30224 NSMAF 3.1837468420093e-08 0.999185679415122 0.00081428874740948 neutral sphingomyelinase activation associated factor FUNCTION: Couples the p55 TNF-receptor (TNF-R55 / TNFR1) to neutral sphingomyelinase (N-SMASE). Specifically binds to the N- smase activation domain of TNF-R55. May regulate ceramide production by N-SMASE.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;iris;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;cerebrum;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.39382 0.12404 -0.130380821 44.03161123 1327.81547 6.84836 NSMCE1 0.0383884146167725 0.929183579968334 0.032428005414894 NSE1 homolog, SMC5-SMC6 complex component FUNCTION: Component of the SMC5-SMC6 complex, a complex involved in DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT- associated PML bodies (APBs). Has in vitro ubiquitin ligase activity in presence of NDNL2. Is involved in positive regulation of response to DNA damage stimulus. {ECO:0000269|PubMed:18086888, ECO:0000269|PubMed:20864041}.; . . smooth muscle;umbilical cord;ovary;salivary gland;intestine;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;liver;testis;kidney; 0.07999 0.10413 -0.005381972 53.50908233 2158.61986 8.54685 NSMCE2 0.0724507212755206 0.87234285031195 0.0552064284125295 NSE2/MMS21 homolog, SMC5-SMC6 complex SUMO ligase FUNCTION: E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination. Is not be required for the stability of the complex. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Acts as a E3 ligase mediating SUMO attachment to various proteins such as SMC6L1 and TRAX, the shelterin complex subunits TERF1, TERF2, TINF2 and TERF2IP, and maybe the cohesin components RAD21 and STAG2. Required for recruitment of telomeres to PML nuclear bodies. SUMO protein-ligase activity is required for the prevention of DNA damage-induced apoptosis by facilitating DNA repair, and for formation of APBs in ALT cell lines. Required for sister chromatid cohesion during prometaphase and mitotic progression. {ECO:0000269|PubMed:16055714, ECO:0000269|PubMed:16810316, ECO:0000269|PubMed:17589526, ECO:0000269|PubMed:19502785}.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;optic nerve;whole body;bone;thyroid;iris;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pharynx;blood;breast;lung;cornea;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06866 0.09049 -0.073340031 48.11866006 32.39941 1.01161 NSMCE3 . . . NSE3 homolog, SMC5-SMC6 complex component FUNCTION: Component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). In vitro enhances ubiquitin ligase activity of NSMCE1. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May be a growth suppressor that facilitates the entry of the cell into cell cycle arrest. {ECO:0000269|PubMed:20864041}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11782285}.; . . 0.09755 0.11283 0.505321956 80.00707714 . . NSMCE4A 0.0859469951564236 0.912081600262937 0.00197140458063955 NSE4 homolog A, SMC5-SMC6 complex component FUNCTION: Component of the SMC5-SMC6 complex, a complex involved in DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT- associated PML bodies (APBs). Is involved in positive regulation of response to DNA damage stimulus. {ECO:0000269|PubMed:18086888}.; . . . . 0.44880 0.10758 -0.161524709 41.6430762 183.88388 2.94244 NSMF 0.0465461743281801 0.95238467951481 0.00106914615700998 NMDA receptor synaptonuclear signaling and neuronal migration factor FUNCTION: Couples NMDA-sensitive glutamate receptor signaling to the nucleus and triggers long-lasting changes in the cytoarchitecture of dendrites and spine synapse processes. Part of the cAMP response element-binding protein (CREB) shut-off signaling pathway. Stimulates outgrowth of olfactory axons and migration of gonadotropin-releasing hormone (GnRH) and luteinizing-hormone-releasing hormone (LHRH) neuronal cells. {ECO:0000269|PubMed:20025934}.; DISEASE: Hypogonadotropic hypogonadism 9 with or without anosmia (HH9) [MIM:614838]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:15362570, ECO:0000269|PubMed:21700882, ECO:0000269|PubMed:23643382}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. The genetics of hypogonadotropic hypogonadism involves various modes of transmission. Oligogenic inheritance has been reported in some patients carrying mutations in NSMF as well as in other HH-associated genes including FGFR1 (PubMed:23643382). {ECO:0000269|PubMed:23643382}.; TISSUE SPECIFICITY: Highly expressed in adult and fetal brain. Weakly expressed in heart, liver, spleen, testis, small intestine, skeletal muscle, peripheral white blood cells and kidney. {ECO:0000269|PubMed:15362570, ECO:0000269|PubMed:20025934}.; . . 0.15334 0.23802 -0.538132194 20.26421326 17.60779 0.61694 NSRP1 0.10480150549491 0.893787050628594 0.00141144387649575 nuclear speckle splicing regulatory protein 1 FUNCTION: RNA-binding protein that mediates pre-mRNA alternative splicing regulation. {ECO:0000269|PubMed:21296756}.; . TISSUE SPECIFICITY: Expressed in dendritic cells, T-cells, B-cells and natural killer cells. Expressed in secondary lymphoid organs such as spleen and mesenteric, axillary and brachial lymph nodes. {ECO:0000269|PubMed:21296756}.; lymphoreticular;smooth muscle;umbilical cord;ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;artery;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;skeletal muscle;bile duct;breast;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.24559 . 0.420771676 77.15852795 338.29708 3.90411 NSRP1P1 . . . nuclear speckle splicing regulatory protein 1 pseudogene 1 . . . . . . . . . . . NSUN2 0.961845836118256 0.0381541369043303 2.69774134045809e-08 NOP2/Sun RNA methyltransferase family member 2 FUNCTION: RNA methyltransferase that methylates tRNAs, and possibly RNA polymerase III transcripts. Methylates cytosine to 5- methylcytosine (m5C) at positions 34 and 48 of intron-containing tRNA(Leu)(CAA) precursors, and at positions 48, 49 and 50 of tRNA(Gly)(GCC) precursors. May act downstream of Myc to regulate epidermal cell growth and proliferation. Required for proper spindle assembly and chromosome segregation, independently of its methyltransferase activity. {ECO:0000269|PubMed:17071714, ECO:0000269|PubMed:19596847, ECO:0000269|PubMed:22995836}.; DISEASE: Mental retardation, autosomal recessive 5 (MRT5) [MIM:611091]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:22541559, ECO:0000269|PubMed:22541562}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in adult and fetal brain and in lymphoblastoid cells. {ECO:0000269|PubMed:22541559}.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;blood;bile duct;pancreas;lung;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach;peripheral nerve; medulla oblongata;globus pallidus;tumor;ciliary ganglion;white blood cells;atrioventricular node;trigeminal ganglion; 0.74820 0.18812 -0.995664936 8.539749941 534.84252 4.71452 NSUN3 2.56992377769436e-07 0.290029460205474 0.709970282802148 NOP2/Sun RNA methyltransferase family member 3 FUNCTION: May have S-adenosyl-L-methionine-dependent methyl- transferase activity. {ECO:0000305}.; . . unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;skin;uterus;pancreas;prostate;cochlea;liver;testis;spleen;germinal center;kidney;brain;stomach; superior cervical ganglion;testis;skeletal muscle; 0.86583 0.09603 -0.227663163 37.11370606 112.64508 2.30778 NSUN4 1.38867585570257e-06 0.833330911809064 0.16666769951508 NOP2/Sun RNA methyltransferase family member 4 FUNCTION: Involved in mitochondrial ribosome assembly. 5- methylcytosine rRNA methyltransferase that probably is involved in mitochondrial ribosome small subunit (SSU) maturation by methylation of mitochondrial 12S rRNA; the function is independent of MTERFD2/MTERF4 and assembled mitochondrial ribosome large subunit (LSU). Targeted to LSU by MTERFD2/MTERF4 and probably is involved in a final step in ribosome biogenesis to ensure that SSU and LSU are assembled. In vitro can methylate 16S rRNA of the LSU; the methylation is enhanced by MTERFD/MTERF4. {ECO:0000269|PubMed:21531335, ECO:0000269|PubMed:23022348}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;whole body;frontal lobe;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; . 0.07301 0.09376 0.352813824 74.49280491 5162.16633 14.77743 NSUN5 1.45415268581091e-06 0.840643908852638 0.159354636994677 NOP2/Sun RNA methyltransferase family member 5 FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 3782 in 28S rRNA. {ECO:0000305|PubMed:23913415}.; . TISSUE SPECIFICITY: Ubiquitous. Detected in placenta, heart and skeletal muscle. {ECO:0000269|PubMed:11978965, ECO:0000269|PubMed:12073013}.; myocardium;lymphoreticular;ovary;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;optic nerve;oesophagus;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;blood;skeletal muscle;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.87077 0.10593 0.023941474 55.75607455 245.36413 3.38000 NSUN5P1 . . . NOP2/Sun RNA methyltransferase family member 5 pseudogene 1 . . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12073013}.; . . 0.08300 . . . . . NSUN5P2 . . . NOP2/Sun RNA methyltransferase family member 5 pseudogene 2 FUNCTION: May have S-adenosyl-L-methionine-dependent methyl- transferase activity. {ECO:0000305}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11978965, ECO:0000269|PubMed:12073013}.; . . 0.90829 . . . . . NSUN6 1.72775122895768e-14 0.007214788565578 0.992785211434405 NOP2/Sun RNA methyltransferase family member 6 FUNCTION: May have S-adenosyl-L-methionine-dependent methyl- transferase activity. {ECO:0000305}.; . . . . 0.97908 0.09906 -0.201976964 38.98325077 77.68152 1.85576 NSUN7 0.048551891347876 0.950446784089519 0.00100132456260494 NOP2/Sun RNA methyltransferase family member 7 FUNCTION: May have S-adenosyl-L-methionine-dependent methyl- transferase activity. {ECO:0000305}.; . . unclassifiable (Anatomical System);lymph node;heart;skin;uterus;prostate;lung;endometrium;placenta;visual apparatus;liver;testis;spleen;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;temporal lobe;globus pallidus;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.08101 . 1.354051915 94.39726351 268.57457 3.51456 NT3 . . . 3'-nucleotidase . . . . . . . . . . . NT5C 0.0126488300759267 0.85644249134493 0.130908678579143 5', 3'-nucleotidase, cytosolic FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP.; . TISSUE SPECIFICITY: Detected in skeletal muscle, heart and pancreas. {ECO:0000269|PubMed:10681516}.; ovary;salivary gland;foreskin;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;epidermis;islets of Langerhans;muscle;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach;thymus; trigeminal ganglion;skeletal muscle; 0.08212 . 0.014844891 54.94810097 70.4325 1.74617 NT5C1A 8.15238589051518e-05 0.766070891990437 0.233847584150658 5'-nucleotidase, cytosolic IA FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides and has a broad substrate specificity. Helps to regulate adenosine levels in heart during ischemia and hypoxia. {ECO:0000269|PubMed:11133996}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Detected at intermediate levels in heart, brain, kidney and pancreas. {ECO:0000269|PubMed:11133996}.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.15617 0.24339 -0.22584292 37.32012267 67.24127 1.69699 NT5C1B 3.45087072878803e-05 0.945093286327139 0.0548722049655729 5'-nucleotidase, cytosolic IB FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Helps to regulate adenosine levels (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in testis, placenta and pancreas. Detected at lower levels in heart, kidney, liver and lung. {ECO:0000269|PubMed:11690631}.; unclassifiable (Anatomical System);lung;bone;testis; dorsal root ganglion;superior cervical ganglion;occipital lobe;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle; . 0.15553 0.512596355 80.29606039 . . NT5C1B-RDH14 5.06962994365991e-05 0.96658461721405 0.0333646864865135 NT5C1B-RDH14 readthrough FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Helps to regulate adenosine levels (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in testis, placenta and pancreas. Detected at lower levels in heart, kidney, liver and lung. {ECO:0000269|PubMed:11690631}.; . . . . 0.53464283 81.00967209 459.27724 4.44678 NT5C2 0.0521978626707803 0.947620851321781 0.000181286007439058 5'-nucleotidase, cytosolic II FUNCTION: May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides.; DISEASE: Spastic paraplegia 45, autosomal recessive (SPG45) [MIM:613162]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. Some SPG45 patients manifest mental retardation, contractures and learning disability. {ECO:0000269|PubMed:24482476}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;gum;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;lacrimal gland;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;duodenum;liver;spleen;head and neck;kidney;stomach; thyroid;skeletal muscle; 0.65780 0.28104 -0.203796826 38.81811748 602.61593 4.96836 NT5C3A 0.0123721939228459 0.952227978261799 0.0353998278153547 5'-nucleotidase, cytosolic IIIA FUNCTION: Nucleotidase which shows specific activity towards cytidine monophosphate (CMP) and 7-methylguanosine monophosphate (m(7)GMP) (PubMed:24603684). CMP seems to be the preferred substrate (PubMed:15968458). {ECO:0000269|PubMed:15968458, ECO:0000269|PubMed:24603684}.; DISEASE: P5N deficiency (P5ND) [MIM:266120]: Autosomal recessive condition causing hemolytic anemia characterized by marked basophilic stippling and the accumulation of high concentrations of pyrimidine nucleotides within the erythrocyte. It is implicated in the anemia of lead poisoning and is possibly associated with learning difficulties. {ECO:0000269|PubMed:11369620, ECO:0000269|PubMed:12930399, ECO:0000269|PubMed:15238149, ECO:0000269|PubMed:15604219, ECO:0000269|PubMed:15968458, ECO:0000269|PubMed:16461318, ECO:0000269|PubMed:18499901, ECO:0000269|PubMed:25153905}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoforms 1, 3 and 4 are expressed in reticulocytes. Isoform 4 is hardly detectable in bone marrow and fetal liver. {ECO:0000269|PubMed:11369620, ECO:0000269|PubMed:15238149}.; . . 0.20158 0.29586 0.12689526 63.00424628 81.15003 1.90678 NT5C3AP1 . . . 5'-nucleotidase, cytosolic IIIA pseudogene 1 . . . . . . . . . . . NT5C3B 7.88066852140565e-05 0.759504671581304 0.240416521733482 5'-nucleotidase, cytosolic IIIB FUNCTION: Specifically hydrolyzes 7-methylguanosine monophosphate (m(7)GMP) to 7-methylguanosine and inorganic phosphate (PubMed:23223233, PubMed:24603684). The specific activity for m(7)GMP may protect cells against undesired salvage of m(7)GMP and its incorporation into nucleic acids (PubMed:23223233). Also has weak activity for CMP (PubMed:23223233, PubMed:24603684). UMP and purine nucleotides are poor substrates (PubMed:23223233). {ECO:0000269|PubMed:23223233, ECO:0000269|PubMed:24603684}.; . . . . 0.11640 0.15562 0.41713504 76.95800896 37.26362 1.11084 NT5CP1 . . . 5',3'-nucleotidase, cytosolic pseudogene 1 . . . . . . . . . . . NT5CP2 . . . 5',3'-nucleotidase, cytosolic pseudogene 2 . . . . . . . . . . . NT5CP3 . . . 5',3'-nucleotidase, cytosolic pseudogene 3 . . . . . . . . . . . NT5DC1 0.326411116423151 0.672905210232213 0.000683673344635831 5'-nucleotidase domain containing 1 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;lens;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; . 0.10358 0.09886 -0.025608647 51.91672564 65.63311 1.66918 NT5DC2 0.0046088659492231 0.988832015057307 0.0065591189934702 5'-nucleotidase domain containing 2 . . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; heart;tumor; 0.48705 0.09949 -0.799052816 12.45576787 2140.52286 8.51361 NT5DC3 0.000112402109573626 0.988650397963276 0.0112371999271499 5'-nucleotidase domain containing 3 . . TISSUE SPECIFICITY: Expressed in brain, placenta, skeletal muscle, pancreas, testis, uterus, and small intestine. Reduced expression in pancreatic cancer cells. {ECO:0000269|PubMed:15547748}.; . . 0.19414 0.11177 -0.558357437 19.54470394 59.34157 1.56160 NT5DC4 . . . 5'-nucleotidase domain containing 4 . . . liver; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.09819 0.09665 . . 773.99562 5.50567 NT5E 2.33633611917161e-06 0.723448285618301 0.276549378045579 5'-nucleotidase ecto FUNCTION: Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities. {ECO:0000269|PubMed:21933152}.; DISEASE: Calcification of joints and arteries (CALJA) [MIM:211800]: A condition characterized by adult-onset calcification of the lower extremity arteries, including the iliac, femoral and tibial arteries, and hand and foot capsule joints. Age of onset has been reported as early as the second decade of life, usually involving intense joint pain or calcification in the hands. {ECO:0000269|PubMed:21288095}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;skeletal muscle;bile duct;breast;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;amnion;head and neck;cervix;kidney;stomach; superior cervical ganglion; 0.21941 0.46348 0.044168103 57.40740741 510.28896 4.62600 NT5M 3.30164509841504e-05 0.35410320539971 0.645863778149305 5',3'-nucleotidase, mitochondrial FUNCTION: Dephosphorylates specifically the 5' and 2'(3')- phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP. {ECO:0000269|PubMed:10899995}.; . TISSUE SPECIFICITY: Highly expressed in heart, brain and skeletal muscle. Detected at very low levels in kidney and pancreas. {ECO:0000269|PubMed:10899995}.; . . 0.13579 . -0.05129383 49.75819769 24.82415 0.81461 NTAN1 0.0158736622184606 0.958947288832671 0.025179048948868 N-terminal asparagine amidase FUNCTION: Side-chain deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N- terminal asparagine to aspartate by PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N- terminal peptidyl Asn. {ECO:0000269|PubMed:21375249}.; . . salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; . 0.20159 0.11495 0.082802743 60.09082331 4983.81502 14.41905 NTAN1P1 . . . N-terminal asparagine amidase pseudogene 1 . . . . . . . . . . . NTAN1P2 . . . N-terminal asparagine amidase pseudogene 2 . . . . . . . . . . . NTAN1P3 . . . N-terminal asparagine amidase pseudogene 3 . . . . . . . . . . . NTF3 0.854440385007675 0.145066088404758 0.000493526587567177 neurotrophin 3 FUNCTION: Seems to promote the survival of visceral and proprioceptive sensory neurons.; . TISSUE SPECIFICITY: Brain and peripheral tissues.; unclassifiable (Anatomical System);prostate;pancreas;lung;whole body;cartilage;ovary;placenta;iris;testis; superior cervical ganglion;liver;skeletal muscle;cerebellum; 0.35201 0.52992 -0.073340031 48.11866006 726.21579 5.34917 NTF4 0.107582900179627 0.776088949568223 0.116328150252149 neurotrophin 4 FUNCTION: Target-derived survival factor for peripheral sensory sympathetic neurons.; . TISSUE SPECIFICITY: Highest levels in prostate, lower levels in thymus, placenta, and skeletal muscle. Expressed in embryonic and adult tissues.; unclassifiable (Anatomical System);uterus;lung;whole body;ovary;placenta;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin; 0.29638 0.24195 . . 960.40211 5.99978 NTF6A . . . neurotrophin 6 alpha (pseudogene) . . . . . . . . . . . NTF6B . . . neurotrophin 6 beta (pseudogene) . . . . . . . . . . . NTF6G . . . neurotrophin 6 gamma (pseudogene) . . . . . . . . . . . NTHL1 1.76610950574232e-09 0.0336769252235339 0.966323073010356 nth-like DNA glycosylase 1 FUNCTION: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N- glycosidic bond, leaving an AP site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines. Has also 8-oxo-7,8-dihydroguanine (8-oxoG) DNA glycosylase activity. Acts preferentially on DNA damage opposite guanine residues in DNA. Is able to process lesions in nucleosomes without requiring or inducing nucleosome disruption. {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:10882850, ECO:0000269|PubMed:11328882, ECO:0000269|PubMed:11380260, ECO:0000269|PubMed:11695910, ECO:0000269|PubMed:12140329, ECO:0000269|PubMed:12144783, ECO:0000269|PubMed:12519758, ECO:0000269|PubMed:14734554, ECO:0000269|PubMed:15533839, ECO:0000269|PubMed:17923696, ECO:0000269|PubMed:20005182, ECO:0000269|PubMed:20110254, ECO:0000269|PubMed:21930793, ECO:0000269|PubMed:8990169, ECO:0000269|PubMed:9045706, ECO:0000269|PubMed:9705289, ECO:0000269|PubMed:9890904}.; DISEASE: Familial adenomatous polyposis 3 (FAP3) [MIM:616415]: A form of familial adenomatous polyposis, a condition characterized by the development of multiple colorectal adenomatous polyps, benign neoplasms derived from glandular epithelium. Some affected individuals may develop colorectal carcinoma. {ECO:0000269|PubMed:25938944}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed with highest levels in heart and lowest levels in lung and liver. {ECO:0000269|PubMed:8990169, ECO:0000269|PubMed:9831664}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);islets of Langerhans;pineal body;muscle;lens;bile duct;breast;pancreas;lung;macula lutea;visual apparatus;liver;spleen;kidney;stomach; liver;globus pallidus;ciliary ganglion; 0.75412 0.21572 -0.580403979 18.58928993 66.89353 1.68912 NTM 0.525365693930018 0.471096681658928 0.0035376244110539 neurotrimin FUNCTION: Neural cell adhesion molecule.; . . . . . . 0.196671391 67.19155461 83.18418 1.93894 NTM-AS1 . . . NTM antisense RNA 1 . . . . . . . . . . . NTM-IT . . . NTM intronic transcript . . . . . . . . . . . NTMT1 0.40245053975409 0.558711476432485 0.0388379838134251 N-terminal Xaa-Pro-Lys N-methyltransferase 1 FUNCTION: Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by METTL11B-mediated monomethylation. Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1. {ECO:0000269|PubMed:20481588, ECO:0000269|PubMed:20668449, ECO:0000269|PubMed:24090352}.; . . . . 0.17098 0.12378 -0.494039303 22.09247464 28.00537 0.89927 NTN1 . . . netrin 1 FUNCTION: Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either DCC or some UNC5 receptors will lead to axon attraction or repulsion, respectively. It also serve as a survival factor via its association with its receptors which prevent the initiation of apoptosis. Involved in tumorigenesis by regulating apoptosis. {ECO:0000269|PubMed:15343335}.; . TISSUE SPECIFICITY: Widely expressed in normal adult tissues with highest levels in heart, small intestine, colon, liver and prostate. Reduced expression in brain tumors and neuroblastomas. Expressed in epididymis (at protein level). {ECO:0000269|PubMed:20736409, ECO:0000269|PubMed:9950216}.; . . 0.95071 0.25454 -0.626318434 17.03231894 24.88991 0.81675 NTN3 5.82214181383073e-05 0.697834039845601 0.30210773873626 netrin 3 FUNCTION: Netrins control guidance of CNS commissural axons and peripheral motor axons. {ECO:0000250}.; . TISSUE SPECIFICITY: Spinal cord. {ECO:0000269|PubMed:9143507}.; unclassifiable (Anatomical System);ovary;colon; dorsal root ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.47754 0.10351 . . 229.98938 3.27725 NTN4 0.994426784918463 0.00557318644176298 2.86397738356225e-08 netrin 4 FUNCTION: May play an important role in neural, kidney and vascular development. Promotes neurite elongation from olfactory bulb explants. {ECO:0000269|PubMed:11038171}.; . TISSUE SPECIFICITY: Expressed in kidney, spleen, mammary gland, aorta, heart, ovary, prostate and fetal spleen. {ECO:0000269|PubMed:11038171}.; lymphoreticular;ovary;sympathetic chain;parathyroid;skin;uterus;prostate;atrium;frontal lobe;bone;testis;amniotic fluid;dura mater;spinal ganglion;artery;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;hypothalamus;skeletal muscle;pancreas;pia mater;lung;mesenchyma;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;aorta; ciliary ganglion;atrioventricular node; 0.48712 0.12197 -0.264476624 34.8844067 444.94905 4.38905 NTN5 3.27017246498834e-06 0.555956623491013 0.444040106336522 netrin 5 . . . lymph node;thyroid;muscle; superior cervical ganglion;testis - interstitial;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; . . . . 187.17976 2.97051 NTNG1 0.4410311282378 0.558686773779811 0.000282097982388769 netrin G1 FUNCTION: Involved in controlling patterning and neuronal circuit formation at the laminar, cellular, subcellular and synaptic levels. Promotes neurite outgrowth of both axons and dendrites. {ECO:0000269|PubMed:21946559}.; . TISSUE SPECIFICITY: Highly expressed in the thalamus, with very low expression, if any, in other tissues. {ECO:0000269|PubMed:14595443, ECO:0000269|PubMed:15901489}.; unclassifiable (Anatomical System);heart;ovary;sympathetic chain;parathyroid;skin;retina;uterus;prostate;whole body;lung;placenta;testis;kidney;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05194 0.10396 -0.670411825 15.61689078 24.24751 0.79723 NTNG2 0.829583230038295 0.170262871757257 0.000153898204448399 netrin G2 FUNCTION: Involved in controlling patterning and neuronal circuit formation at the laminar, cellular, subcellular and synaptic levels. Promotes neurite outgrowth of both axons and dendrites. {ECO:0000269|PubMed:21946559}.; . . unclassifiable (Anatomical System);amygdala;islets of Langerhans;adrenal cortex;blood;fovea centralis;choroid;lens;bone marrow;retina;optic nerve;frontal lobe;macula lutea;kidney;brain; subthalamic nucleus;occipital lobe;globus pallidus;cingulate cortex; 0.31508 0.12093 -0.26993514 34.59542345 76.98382 1.84250 NTPCR 1.70241673676366e-05 0.254217412204253 0.745765563628379 nucleoside-triphosphatase, cancer-related FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency. {ECO:0000269|PubMed:17291528}.; . . . . 0.09838 0.11813 0.415317661 76.81056853 131.83629 2.50011 NTRK1 0.000424899217244118 0.997871876590652 0.00170322419210427 neurotrophic tyrosine kinase, receptor, type 1 FUNCTION: Receptor tyrosine kinase involved in the development and the maturation of the central and peripheral nervous systems through regulation of proliferation, differentiation and survival of sympathetic and nervous neurons. High affinity receptor for NGF which is its primary ligand, it can also bind and be activated by NTF3/neurotrophin-3. However, NTF3 only supports axonal extension through NTRK1 but has no effect on neuron survival. Upon dimeric NGF ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades driving cell survival and differentiation. Through SHC1 and FRS2 activates a GRB2-Ras-MAPK cascade that regulates cell differentiation and survival. Through PLCG1 controls NF-Kappa-B activation and the transcription of genes involved in cell survival. Through SHC1 and SH2B1 controls a Ras- PI3 kinase-AKT1 signaling cascade that is also regulating survival. In absence of ligand and activation, may promote cell death, making the survival of neurons dependent on trophic factors.; DISEASE: Congenital insensitivity to pain with anhidrosis (CIPA) [MIM:256800]: Characterized by a congenital insensitivity to pain, anhidrosis (absence of sweating), absence of reaction to noxious stimuli, self-mutilating behavior, and mental retardation. This rare autosomal recessive disorder is also known as congenital sensory neuropathy with anhidrosis or hereditary sensory and autonomic neuropathy type IV or familial dysautonomia type II. {ECO:0000269|PubMed:10090906, ECO:0000269|PubMed:10233776, ECO:0000269|PubMed:10330344, ECO:0000269|PubMed:10567924, ECO:0000269|PubMed:10861667, ECO:0000269|PubMed:10982191, ECO:0000269|PubMed:11310631, ECO:0000269|PubMed:22302274, ECO:0000269|PubMed:8696348}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Chromosomal aberrations involving NTRK1 are found in papillary thyroid carcinomas (PTCs) (PubMed:2869410, PubMed:7565764, PubMed:1532241). Translocation t(1;3)(q21;q11) with TFG generates the TRKT3 (TRK-T3) transcript by fusing TFG to the 3'-end of NTRK1 (PubMed:7565764). A rearrangement with TPM3 generates the TRK transcript by fusing TPM3 to the 3'-end of NTRK1 (PubMed:2869410). An intrachromosomal rearrangement that links the protein kinase domain of NTRK1 to the 5'-end of the TPR gene forms the fusion protein TRK-T1. TRK-T1 is a 55 kDa protein reacting with antibodies against the C-terminus of the NTRK1 protein (PubMed:1532241). {ECO:0000269|PubMed:1532241, ECO:0000269|PubMed:2869410, ECO:0000269|PubMed:7565764}.; TISSUE SPECIFICITY: Isoform TrkA-I is found in most non-neuronal tissues. Isoform TrkA-II is primarily expressed in neuronal cells. TrkA-III is specifically expressed by pluripotent neural stem and neural crest progenitors. {ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:8325889}.; optic nerve;whole body;bone;placenta;macula lutea;head and neck;fovea centralis;choroid;lens;brain;retina; superior cervical ganglion;adipose tissue;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.20750 0.68852 -0.058785319 48.90894079 774.82794 5.50883 NTRK2 0.999893180098198 0.00010681989259615 9.20538720560863e-12 neurotrophic tyrosine kinase, receptor, type 2 FUNCTION: Receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity. Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin- 4. Alternatively can also bind NTF3/neurotrophin-3 which is less efficient in activating the receptor but regulates neuron survival through NTRK2. Upon ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades. Through SHC1, FRS2, SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for instance neuronal differentiation including neurite outgrowth. Through the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade that mainly regulates growth and survival. Through PLCG1 and the downstream protein kinase C-regulated pathways controls synaptic plasticity. Thereby, plays a role in learning and memory by regulating both short term synaptic function and long-term potentiation. PLCG1 also leads to NF-Kappa-B activation and the transcription of genes involved in cell survival. Hence, it is able to suppress anoikis, the apoptosis resulting from loss of cell-matrix interactions. May also play a role in neutrophin- dependent calcium signaling in glial cells and mediate communication between neurons and glia. {ECO:0000269|PubMed:15494731}.; DISEASE: Obesity, hyperphagia, and developmental delay (OBHD) [MIM:613886]: A disorder characterized by early-onset obesity, hyperphagia, and severe developmental delay in motor function, speech, and language. {ECO:0000269|PubMed:15494731}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform TrkB is expressed in the central and peripheral nervous system. In the central nervous system (CNS), expression is observed in the cerebral cortex, hippocampus, thalamus, choroid plexus, granular layer of the cerebellum, brain stem, and spinal cord. In the peripheral nervous system, it is expressed in many cranial ganglia, the ophthalmic nerve, the vestibular system, multiple facial structures, the submaxillary glands, and dorsal root ganglia. Isoform TrkB-T1 is mainly expressed in the brain but also detected in other tissues including pancreas, kidney and heart. Isoform TrkB-T-Shc is predominantly expressed in the brain. {ECO:0000269|PubMed:11798182, ECO:0000269|PubMed:7936202}.; ovary;colon;choroid;fovea centralis;skin;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;larynx;bone;thyroid;testis;dura mater;brain;amygdala;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;lens;skeletal muscle;pancreas;pia mater;lung;visual apparatus;hippocampus;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; amygdala;whole brain;superior cervical ganglion;thalamus;medulla oblongata;occipital lobe;olfactory bulb;hypothalamus;spinal cord;temporal lobe;caudate nucleus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;thyroid;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.41887 0.47757 -0.488577883 22.64685067 57.05784 1.52075 NTRK3 0.978536238427813 0.0214637295373554 3.20348318267821e-08 neurotrophic tyrosine kinase, receptor, type 3 FUNCTION: Receptor tyrosine kinase involved in nervous system and probably heart development. Upon binding of its ligand NTF3/neurotrophin-3, NTRK3 autophosphorylates and activates different signaling pathways, including the phosphatidylinositol 3-kinase/AKT and the MAPK pathways, that control cell survival and differentiation. {ECO:0000269|PubMed:25196463}.; DISEASE: Note=Defects in NTRK3 are associated with susceptibility to congenital heart defects (CHD). A disease characterized by congenital developmental abnormalities involving structures of the heart. CHD are the most common major birth defects and the leading cause of death from congenital malformations. {ECO:0000269|PubMed:25196463}.; TISSUE SPECIFICITY: Widely expressed but mainly in nervous tissue. Isoform 2 is expressed at higher levels in adult brain than in fetal brain.; unclassifiable (Anatomical System);prostate;frontal lobe;lacrimal gland;cerebral cortex;islets of Langerhans;kidney;brain;retina; dorsal root ganglion;medulla oblongata;superior cervical ganglion;occipital lobe;olfactory bulb;cerebellum peduncles;pons;caudate nucleus;skin;subthalamic nucleus;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;amygdala;testis - interstitial;temporal lobe;atrioventricular node;skeletal muscle;fetal brain;prefrontal cortex;appendix;parietal lobe;cerebellum; 0.31634 0.52685 -1.993409678 1.757489974 54.70856 1.48153 NTRK3-AS1 . . . NTRK3 antisense RNA 1 . . . . . . . . . . . NTS 7.97101367921064e-06 0.169847003984828 0.830145025001492 neurotensin FUNCTION: Neurotensin may play an endocrine or paracrine role in the regulation of fat metabolism. It causes contraction of smooth muscle.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;hypothalamus;skin;uterus;pancreas;prostate;whole body;endometrium;larynx;duodenum;pituitary gland;head and neck;brain;stomach; superior cervical ganglion; 0.68978 0.36104 0.147123112 64.11299835 11.91425 0.43179 NTSR1 9.72930758301054e-08 0.174082562870597 0.825917339836327 neurotensin receptor 1 (high affinity) FUNCTION: G-protein coupled receptor for the tridecapeptide neurotensin (NTS) (PubMed:8381365, PubMed:21725197, PubMed:23140271). Signaling is effected via G proteins that activate a phosphatidylinositol-calcium second messenger system. Signaling leads to the activation of downstream MAP kinases and protects cells against apoptosis (PubMed:21725197). {ECO:0000269|PubMed:21725197, ECO:0000269|PubMed:23140271, ECO:0000269|PubMed:8381365}.; . TISSUE SPECIFICITY: Expressed in prostate (at protein level). Detected in colon and peripheral blood mononuclear cells. Detected at very low levels in brain. {ECO:0000269|PubMed:20048080, ECO:0000269|PubMed:8381365}.; . . 0.17660 0.31062 0.670564357 84.70158056 362.32153 4.02976 NTSR2 2.52586411261305e-05 0.310591599824646 0.689383141534228 neurotensin receptor 2 FUNCTION: Receptor for the tridecapeptide neurotensin. It is associated with G proteins that activate a phosphatidylinositol- calcium second messenger system.; . TISSUE SPECIFICITY: Expressed in prostate (at protein level). {ECO:0000269|PubMed:20048080}.; unclassifiable (Anatomical System);lung;ganglion;hypothalamus;testis;brain; whole brain;dorsal root ganglion;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;hypothalamus;temporal lobe;pons;atrioventricular node;caudate nucleus;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.13596 0.11051 . . 188.32662 2.98021 NUAK1 0.189029672518911 0.81049348700443 0.000476840476659594 NUAK family kinase 1 FUNCTION: Serine/threonine-protein kinase involved in various processes such as cell adhesion, regulation of cell ploidy and senescence, cell proliferation and tumor progression. Phosphorylates ATM, CASP6, LATS1, PPP1R12A and p53/TP53. Acts as a regulator of cellular senescence and cellular ploidy by mediating phosphorylation of 'Ser-464' of LATS1, thereby controlling its stability. Controls cell adhesion by regulating activity of the myosin protein phosphatase 1 (PP1) complex. Acts by mediating phosphorylation of PPP1R12A subunit of myosin PP1: phosphorylated PPP1R12A then interacts with 14-3-3, leading to reduced dephosphorylation of myosin MLC2 by myosin PP1. May be involved in DNA damage response: phosphorylates p53/TP53 at 'Ser-15' and 'Ser- 392' and is recruited to the CDKN1A/WAF1 promoter to participate to transcription activation by p53/TP53. May also act as a tumor malignancy-associated factor by promoting tumor invasion and metastasis under regulation and phosphorylation by AKT1. Suppresses Fas-induced apoptosis by mediating phosphorylation of CASP6, thereby suppressing the activation of the caspase and the subsequent cleavage of CFLAR. Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with STK11, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair (PubMed:25329316). {ECO:0000269|PubMed:12409306, ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15060171, ECO:0000269|PubMed:15273717, ECO:0000269|PubMed:19927127, ECO:0000269|PubMed:20354225, ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:25329316}.; . TISSUE SPECIFICITY: Expressed at high levels in heart and brain, and at lower levels in skeletal muscle, kidney, ovary, placenta, lung and liver. Highly up-regulated in colorectal cancer cell lines. {ECO:0000269|PubMed:14982852}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;frontal lobe;larynx;thyroid;bone;spinal ganglion;brain;unclassifiable (Anatomical System);small intestine;heart;cartilage;hypothalamus;spinal cord;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;amnion;spleen;head and neck;stomach; whole brain;occipital lobe;superior cervical ganglion;medulla oblongata;subthalamic nucleus;temporal lobe;prefrontal cortex;globus pallidus;pons;cingulate cortex;parietal lobe;cerebellum; 0.37286 0.14253 -0.552898813 19.86317528 2302.47786 8.88204 NUAK2 3.1843015314192e-05 0.939297786849046 0.0606703701356398 NUAK family kinase 2 FUNCTION: Stress-activated kinase involved in tolerance to glucose starvation. Induces cell-cell detachment by increasing F-actin conversion to G-actin. Expression is induced by CD95 or TNF-alpha, via NF-kappa-B. Protects cells from CD95-mediated apoptosis and is required for the increased motility and invasiveness of CD95- activated tumor cells. Able to phosphorylate 'Ser-464' of LATS1. {ECO:0000269|PubMed:14575707, ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15345718, ECO:0000269|PubMed:19927127}.; . . . . 0.11370 0.12009 -0.661316159 16.02382637 742.00604 5.40893 NUB1 1.14912569365706e-05 0.946016051333734 0.0539724574093294 negative regulator of ubiquitin-like proteins 1 FUNCTION: Specific down-regulator of the NEDD8 conjugation system. Recruits NEDD8, UBD, and their conjugates to the proteasome for degradation. Isoform 1 promotes the degradation of NEDD8 more efficiently than isoform 2. {ECO:0000269|PubMed:16707496}.; . TISSUE SPECIFICITY: Widely expressed with lowest expression in the pancreas for isoform 1 and in leukocytes, liver, prostate and skeletal muscle for isoform 2.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; . 0.11773 -0.334253673 30.70299599 592.13155 4.93157 NUBP1 6.66279855269194e-08 0.256954491149521 0.743045442222494 nucleotide binding protein 1 FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery (PubMed:18573874). Required for maturation of extramitochondrial Fe-S proteins (PubMed:18573874). The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins (PubMed:18573874). Implicated in the regulation of centrosome duplication (By similarity). Negatively regulates cilium formation and structure (By similarity). {ECO:0000250|UniProtKB:Q9R060, ECO:0000269|PubMed:18573874}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.35540 0.08246 -0.069700724 48.54328851 911.06882 5.87088 NUBP2 0.00881682223602247 0.803199651510901 0.187983526253077 nucleotide binding protein 2 FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Negatively regulates cilium formation and structure. {ECO:0000250|UniProtKB:Q9R061, ECO:0000255|HAMAP-Rule:MF_03039}.; . TISSUE SPECIFICITY: Widely expressed with highest expression in skeletal muscle.; smooth muscle;ovary;salivary gland;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;bone;iris;germinal center;brain;tonsil;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; . 0.08572 0.13089 -0.576764155 18.7839113 118.42893 2.36711 NUBPL 0.00200988228068456 0.977018242607453 0.0209718751118629 nucleotide binding protein like FUNCTION: Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). May deliver of one or more Fe-S clusters to complex I subunits. {ECO:0000269|PubMed:19752196}.; . TISSUE SPECIFICITY: Highest expression in liver and kidney. expressed at significant levels in small intestine and brain (at protein level). {ECO:0000269|PubMed:19752196}.; unclassifiable (Anatomical System);cartilage;skeletal muscle;skin;breast;frontal lobe;larynx;placenta;liver;head and neck;germinal center;kidney;brain;stomach; superior cervical ganglion;globus pallidus;pons; 0.04404 0.09104 0.439181676 77.69521113 53.30545 1.45010 NUCB1 4.16610548641566e-05 0.990461239661481 0.00949709928365486 nucleobindin 1 FUNCTION: Major calcium-binding protein of the Golgi. May have a role in calcium homeostasis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed both in fetal and adult heart, lung, liver, kidney and brain, and in adult skeletal muscle, placenta and pancreas.; lymphoreticular;medulla oblongata;smooth muscle;ovary;salivary gland;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;iris;pituitary gland;testis;amniotic fluid;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;islets of Langerhans;hypothalamus;spinal cord;muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;amnion;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; placenta;liver;kidney; 0.12231 0.23155 -0.887242605 10.43288511 145.51458 2.62794 NUCB1-AS1 . . . NUCB1 antisense RNA 1 . . . . . . . . . . . NUCB2 8.58987882667095e-08 0.492001158366137 0.507998755735074 nucleobindin 2 FUNCTION: Calcium-binding protein. May have a role in calcium homeostasis.; . TISSUE SPECIFICITY: Predominantly expressed in spleen, testis and normal stomach. {ECO:0000269|PubMed:12087473}.; ovary;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;oral cavity;blood;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;liver;head and neck;kidney;mammary gland;stomach;thymus; testis - interstitial;trachea;salivary gland;testis; 0.31941 0.09807 -0.293801652 32.93819297 4347.97507 13.13601 NUCKS1 0.979237657935801 0.0207447721922549 1.75698719442369e-05 nuclear casein kinase and cyclin-dependent kinase substrate 1 . . TISSUE SPECIFICITY: Widely expressed, with highest levels in thyroid gland, prostate and uterus and in fetal liver, thymus and lung. {ECO:0000269|PubMed:15381070}.; smooth muscle;ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;retina;uterus;prostate;atrium;whole body;oesophagus;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;lung;cornea;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; subthalamic nucleus;medulla oblongata;superior cervical ganglion;prefrontal cortex;trigeminal ganglion;cingulate cortex;cerebellum; 0.90068 0.13281 -0.119252484 44.53880632 4.59039 0.16497 NUCKS1P1 . . . nuclear casein kinase and cyclin-dependent kinase substrate 1 pseudogene 1 . . . . . . . . . . . NUDC 0.822775133437605 0.177053571824108 0.000171294738286976 nudC nuclear distribution protein FUNCTION: Plays a role in neurogenesis and neuronal migration (By similarity). Necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Necessary for cytokinesis and cell proliferation. {ECO:0000250, ECO:0000269|PubMed:12679384, ECO:0000269|PubMed:12852857}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in fetal liver, kidney, lung and brain. Highly expressed in adult pancreas, kidney, skeletal muscle, liver, lung, placenta, prostate, brain and heart. {ECO:0000269|PubMed:10210332, ECO:0000269|PubMed:10453739}.; lymphoreticular;ovary;salivary gland;developmental;colon;parathyroid;fovea centralis;choroid;skin;uterus;prostate;optic nerve;larynx;thyroid;pituitary gland;testis;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;tongue;blood;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.34972 0.09134 -0.516085732 21.20193442 29.80518 0.95093 NUDCD1 3.84054787465333e-06 0.947156956941349 0.0528392025107758 NudC domain containing 1 . . TISSUE SPECIFICITY: Isoform 1 is specifically expressed in leukemias and a variety of solid tumor cell lines and is also detected in testis and heart. Isoform 2 is predominantly expressed in testis and weakly expressed in tumor cells. {ECO:0000269|PubMed:11416219, ECO:0000269|PubMed:14688378}.; ovary;salivary gland;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; ciliary ganglion;atrioventricular node; 0.19623 0.08363 0.951720429 90.06251474 3244.62786 10.85038 NUDCD2 0.000812082193063064 0.545061614093985 0.454126303712952 NudC domain containing 2 FUNCTION: May regulate the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone. {ECO:0000269|PubMed:20133715}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;bone marrow;uterus;prostate;whole body;cochlea;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland; . 0.31509 0.11809 -0.339715008 30.06605331 2.40691 0.08476 NUDCD3 0.706731711814528 0.292544237198458 0.000724050987014193 NudC domain containing 3 . . . lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;greater omentum;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta;cerebellum; amygdala;dorsal root ganglion;whole brain;medulla oblongata;superior cervical ganglion;atrioventricular node;pons;skeletal muscle;skin;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.16646 0.10559 -0.025608647 51.91672564 1744.96605 7.70972 NUDCP1 . . . nudC nucelar distribution protein pseudogene 1 . . . . . . . . . . . NUDCP2 . . . nudC nucelar distribution protein pseudogene 2 . . . . . . . . . . . NUDT1 1.28825205663006e-09 0.0146275301928261 0.985372468518922 nudix hydrolase 1 FUNCTION: Antimutagenic. Acts as a sanitizing enzyme for oxidized nucleotide pools, thus suppressing cell dysfunction and death induced by oxidative stress. Hydrolyzes 8-oxo-dGTP, 8-oxo-dATP and 2-OH-dATP, thus preventing misincorporation of oxidized purine nucleoside triphosphates into DNA and subsequently preventing A:T to C:G and G:C to T:A transversions. Able to hydrolyze also the corresponding ribonucleotides, 2-OH-ATP, 8-oxo-GTP and 8-oxo-ATP. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA. {ECO:0000269|PubMed:10373420, ECO:0000269|PubMed:10608900, ECO:0000269|PubMed:11139615, ECO:0000269|PubMed:12857738, ECO:0000269|PubMed:22556419}.; . TISSUE SPECIFICITY: Widely expressed with highest expression in thymus, testis, embryo and proliferating blood lymphocytes. {ECO:0000269|PubMed:9211940}.; unclassifiable (Anatomical System);lymph node;ovary;heart;islets of Langerhans;colon;parathyroid;fovea centralis;bone marrow;prostate;optic nerve;whole body;lung;bone;placenta;macula lutea;liver;testis;spleen;kidney;brain;stomach; testis - interstitial;heart;testis;white blood cells;thymus; 0.42630 0.18011 -0.025608647 51.91672564 148.84611 2.66060 NUDT2 0.00236774773837517 0.535391464143074 0.46224078811855 nudix hydrolase 2 FUNCTION: Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;iris;testis;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;temporal lobe;trigeminal ganglion;skeletal muscle; 0.10188 0.10884 0.147123112 64.11299835 14.88232 0.53580 NUDT3 0.876816622471426 0.121652663717912 0.00153071381066131 nudix hydrolase 3 FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction. InsP6 (inositol hexakisphophate) is not a substrate. Acts as a negative regulator of the ERK1/2 pathway. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5- phosphoribose 1-diphosphate. {ECO:0000269|PubMed:9822604}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in brain, heart, pancreas and liver. Also expressed in placenta, lung and kidney. {ECO:0000269|PubMed:9822604}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;pancreas;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;thalamus;medulla oblongata;occipital lobe;prefrontal cortex;pons;skeletal muscle;cingulate cortex;parietal lobe;cerebellum; 0.37849 0.16306 0.058937498 58.26256192 19.49364 0.66869 NUDT4 0.164174989201243 0.773028100439007 0.0627969103597494 nudix hydrolase 4 FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphate Ap6A, but not Ap5A. The major reaction products are ADP and p4a from Ap6A. Also able to hydrolyze 5-phosphoribose 1-diphosphate. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA. {ECO:0000269|PubMed:10777568}.; . TISSUE SPECIFICITY: Expressed in heart and, at lower level in skeletal muscle, pancreas and kidney. {ECO:0000269|PubMed:10777568}.; smooth muscle;ovary;salivary gland;intestine;rectum;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion;globus pallidus;pons;trigeminal ganglion;skeletal muscle; 0.51983 0.10488 -0.09720619 46.20193442 0.72963 0.01223 NUDT4P1 . . . nudix hydrolase 4 pseudogene 1 . . . . . . . . . . . NUDT4P2 . . . nudix hydrolase 4 pseudogene 2 . . . . . . . . . . . NUDT5 0.0094606868155339 0.940101992093862 0.050437321090604 nudix hydrolase 5 FUNCTION: Hydrolyzes with similar activities ADP-ribose ADP- mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP. Can also hydrolyze other nucleotide sugars with low activity. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA. {ECO:0000269|PubMed:17052728}.; . TISSUE SPECIFICITY: Widely expressed. Most abundant in liver.; . . 0.49777 0.14244 -0.073340031 48.11866006 23.32139 0.77833 NUDT6 0.000761661984062648 0.925256766467975 0.0739815715479624 nudix hydrolase 6 FUNCTION: May contribute to the regulation of cell proliferation. {ECO:0000269|PubMed:11266510}.; . TISSUE SPECIFICITY: Detected in liver, kidney and esophagus (at protein level). Ubiquitous. {ECO:0000269|PubMed:11266510, ECO:0000269|PubMed:17569023}.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;lung;cochlea;bone;thyroid;placenta;visual apparatus;liver;testis;spleen;kidney;brain; . 0.29660 0.25552 0.639420866 83.8995046 1690.80174 7.58188 NUDT7 0.00010793192750074 0.366455243529806 0.633436824542693 nudix hydrolase 7 FUNCTION: Coenzyme A diphosphatase which mediates the cleavage of CoA, CoA esters and oxidized CoA with similar efficiencies, yielding 3',5'-ADP and the corresponding 4'-phosphopantetheine derivative as products. CoA into 3',5'-ADP and 4'- phosphopantetheine. Has no activity toward NDP-sugars, CDP- alcohols, (deoxy)nucleoside 5'-triphosphates, nucleoside 5'-di or monophosphates, diadenosine polyphosphates, NAD, NADH, NADP, NADPH or thymidine-5'-monophospho-p-nitrophenyl ester. May be required to eliminate oxidized CoA from peroxisomes, or regulate CoA and acyl-CoA levels in this organelle in response to metabolic demand. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in liver, kidney, pancreas, pituitary, small intestine, spleen, heart and placenta. Weakly expressed in brain. {ECO:0000269|PubMed:11415433}.; unclassifiable (Anatomical System);prostate;lung;heart;islets of Langerhans;liver;testis;spleen;kidney;brain;artery;aorta; . 0.10158 0.09498 0.328949044 73.41354093 1470.46036 7.14638 NUDT8 0.0032881681662429 0.606249796153678 0.390462035680079 nudix hydrolase 8 FUNCTION: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. {ECO:0000250}.; . . unclassifiable (Anatomical System);bile duct;lung;umbilical cord;bone;testis;blood;brain; liver;ciliary ganglion;kidney; 0.13320 0.10828 . . 175.09017 2.87778 NUDT9 1.2725661032482e-05 0.831657511112226 0.168329763226742 nudix hydrolase 9 FUNCTION: Hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'- phosphate.; . TISSUE SPECIFICITY: Ubiquitously expressed but isoform 1 is the most predominant isoform. {ECO:0000269|PubMed:12427752}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;lens;skeletal muscle;bile duct;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach;aorta; medulla oblongata;superior cervical ganglion;testis - seminiferous tubule;testis;pons;atrioventricular node;trigeminal ganglion; 0.06718 0.12768 0.084621747 60.31493277 131.08372 2.49379 NUDT9P1 . . . nudix hydrolase 9 pseudogene 1 . . . . . . . . . . . NUDT10 . . . nudix hydrolase 10 FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate. {ECO:0000269|PubMed:12105228}.; . TISSUE SPECIFICITY: Mainly expressed in testis and, at lower level in brain. According to PubMed:12121577, it is widely expressed. {ECO:0000269|PubMed:12105228, ECO:0000269|PubMed:12121577}.; smooth muscle;ovary;salivary gland;intestine;colon;skin;uterus;prostate;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney; . 0.13144 0.11150 -0.075159878 47.78839349 8.27976 0.30347 NUDT11 0.699091254686775 0.284172768228286 0.0167359770849398 nudix hydrolase 11 FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate. {ECO:0000269|PubMed:12105228}.; . TISSUE SPECIFICITY: Mainly expressed in testis and, at lower level in brain. According to PubMed:12121577, it is also expressed in pancreas and weakly expressed in thymus, prostate, ovary, lung, small intestine and heart. {ECO:0000269|PubMed:12105228, ECO:0000269|PubMed:12121577}.; . . 0.31410 0.11809 -0.075159878 47.78839349 1.0912 0.02807 NUDT12 3.27725302698986e-11 0.0230805473093826 0.976919452657845 nudix hydrolase 12 FUNCTION: Hydrolyzes NAD(P)H to NMNH and AMP (2',5'-ADP), and diadenosine diphosphate to AMP. Has also activity towards NAD(P)(+), ADP-ribose and diadenosine triphosphate. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle. {ECO:0000269|PubMed:12790796}.; . . unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;pineal body;colon;skin;retina;pancreas;prostate;whole body;lung;cerebral cortex;endometrium;bone;placenta;liver;testis;kidney;brain;stomach; . 0.07793 0.12990 0.286674996 71.49681529 92.25456 2.06569 NUDT13 5.7285446566616e-07 0.426251179405617 0.573748247739917 nudix hydrolase 13 . . TISSUE SPECIFICITY: Highly expressed in metastasis-suppressed chromosome 6 melanoma hybrids. {ECO:0000269|Ref.6}.; islets of Langerhans;blood;skin;bone marrow;uterus;lung;nasopharynx;bone;thyroid;liver;testis;head and neck;spleen;cervix;kidney;brain; atrioventricular node;trigeminal ganglion; 0.16121 0.10081 0.907624513 89.46685539 570.22167 4.84466 NUDT14 0.000705232590146412 0.514992598891912 0.484302168517941 nudix hydrolase 14 FUNCTION: Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and ADP-ribose to ribose 5-phosphate and AMP. The physiological substrate is probably UDP-glucose. Poor activity on other substrates such as ADP-glucose, CDP-glucose, GDP-glucose and GDP- mannose.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;fovea centralis;skin;skeletal muscle;uterus;pancreas;prostate;whole body;lung;ganglion;placenta;macula lutea;kidney;mammary gland;aorta;tonsil;stomach; amygdala; 0.17065 0.11746 -0.359940251 28.93371078 57.83832 1.53686 NUDT15 0.0972295800796055 0.770570077347182 0.132200342573212 nudix hydrolase 15 FUNCTION: Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can degrade 8-oxo-dGTP in vitro, suggesting that it may remove an oxidatively damaged form of guanine (7,8-dihydro-8- oxoguanine) from DNA and the nucleotide pool, thereby preventing misincorporation of 8-oxo-dGTP into DNA thus preventing A:T to C:G transversions. Its substrate specificity in vivo however remains unclear (By similarity). May have a role in DNA synthesis and cell cycle progression through the interaction with PCNA. {ECO:0000250, ECO:0000269|PubMed:19419956, ECO:0000269|PubMed:22556419}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;stomach; . 0.52299 . 0.03689118 56.64071715 485.28356 4.53736 NUDT15P1 . . . nudix hydrolase 15 pseudogene 1 . . . . . . . . . . . NUDT15P2 . . . nudix hydrolase 15 pseudogene 2 . . . . . . . . . . . NUDT16 0.00146067601382414 0.43641080184346 0.562128522142716 nudix hydrolase 16 FUNCTION: RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal- dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms (PubMed:20385596, PubMed:26121039). The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP (PubMed:20385596). Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions (PubMed:20385596). {ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:18820299, ECO:0000269|PubMed:20385596, ECO:0000269|PubMed:21070968, ECO:0000269|PubMed:21337011, ECO:0000269|PubMed:26121039}.; . TISSUE SPECIFICITY: Expressed strongly in lung, kidney, adrenal gland, testis, heart and brain. {ECO:0000269|PubMed:20385596}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lacrimal gland;tongue;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach;peripheral nerve; kidney;trigeminal ganglion; 0.22475 . . . 161.74115 2.77897 NUDT16L1 0.0204493837015027 0.746948481188834 0.232602135109663 nudix hydrolase 16 like 1 FUNCTION: Probable adapter protein, which may link syndecan-4 (SDC4) and paxilin (TGFB1I1 and PXN) receptors (By similarity). Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA. {ECO:0000250}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;muscle;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;stomach;thymus; . 0.30898 . -0.0274281 51.65723048 12.74325 0.46380 NUDT16P1 . . . nudix hydrolase 16 pseudogene 1 . . . . . 0.10767 . . . . . NUDT17 0.00537990843402384 0.969857421749484 0.0247626698164921 nudix hydrolase 17 FUNCTION: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;urinary;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.27987 . -0.22584292 37.32012267 225.12642 3.24432 NUDT18 0.000135276357888308 0.407317540641914 0.592547183000197 nudix hydrolase 18 FUNCTION: Mediates the hydrolyzis of oxidized nucleoside diphosphate derivatives. Hydrolyzes 8-oxo-7,8-dihydroguanine (8- oxo-Gua)-containing deoxyribo- and ribonucleoside diphosphates to the monophosphates. Hydrolyzes 8-oxo-dGDP and 8-oxo-GDP with the same efficiencies. Hydrolyzes also 8-OH-dADP and 2-OH-dADP. Exhibited no or minimal hydrolyzis activity against 8-oxo-dGTP, 8- oxo-GTP, dGTP, GTP, dGDP and GDP. Probably removes oxidized guanine nucleotides from both the DNA and RNA precursor pools. {ECO:0000269|PubMed:22556419}.; . . unclassifiable (Anatomical System);islets of Langerhans;salivary gland;colon;blood;fovea centralis;choroid;lens;retina;bone marrow;uterus;prostate;optic nerve;lung;endometrium;placenta;macula lutea;visual apparatus;liver;spleen;brain; dorsal root ganglion;superior cervical ganglion;appendix;atrioventricular node;pons; 0.10666 0.11108 . . 74.26129 1.79995 NUDT19 1.09335740830484e-05 0.201396500446099 0.798592565979818 nudix hydrolase 19 FUNCTION: Coenzyme A diphosphatase that mediates the hydrolysis of a wide range of CoA esters, including choloyl-CoA and branched- chain fatty-acyl-CoA esters. At low substrate concentrations medium and long-chain fatty-acyl-CoA esters are the primary substrates (By similarity). {ECO:0000250}.; . . . . 0.10205 0.28800 0.349177632 74.18023119 1234.58673 6.63856 NUDT19P1 . . . nudix hydrolase 19 pseudogene 1 . . . . . . . . . . . NUDT19P2 . . . nudix hydrolase 19 pseudogene 2 . . . . . . . . . . . NUDT19P3 . . . nudix hydrolase 19 pseudogene 3 . . . . . . . . . . . NUDT19P4 . . . nudix hydrolase 19 pseudogene 4 . . . . . . . . . . . NUDT19P5 . . . nudix hydrolase 19 pseudogene 5 . . . . . . . . . . . NUDT21 0.947296445770822 0.0525264495455145 0.00017710468366331 nudix hydrolase 21 FUNCTION: Component of the cleavage factor Im (CFIm) complex that plays a key role in pre-mRNA 3'-processing. Involved in association with CPSF6 or CPSF7 in pre-MRNA 3'-end poly(A) site cleavage and poly(A) addition. NUDT21/CPSF5 binds to cleavage and polyadenylation RNA substrates. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA. Binds to, but does not hydrolyze mono- and di-adenosine nucleotides. May have a role in mRNA export. {ECO:0000269|PubMed:14690600, ECO:0000269|PubMed:20479262, ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:21295486, ECO:0000269|PubMed:8626397, ECO:0000269|PubMed:9659921}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.76918 0.13588 -0.009020804 52.8544468 . . NUDT21P1 . . . nudix hydrolase 21 pseudogene 1 . . . . . . . . . . . NUDT22 0.000315497036403361 0.810015543530748 0.189668959432849 nudix hydrolase 22 . . . ovary;colon;skin;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;skeletal muscle;pancreas;lung;placenta;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; . 0.10836 . 0.350995466 74.37485256 1470.25232 7.14523 NUF2 6.55912662381588e-05 0.976315603072249 0.0236188056615134 NUF2, NDC80 kinetochore complex component FUNCTION: Acts as a component of the essential kinetochore- associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity (PubMed:12438418, PubMed:14654001, PubMed:15062103, PubMed:15235793, PubMed:15239953, PubMed:15548592, PubMed:17535814). Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (PubMed:15548592). The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules (PubMed:23085020). {ECO:0000269|PubMed:12438418, ECO:0000269|PubMed:14654001, ECO:0000269|PubMed:15062103, ECO:0000269|PubMed:15235793, ECO:0000269|PubMed:15239953, ECO:0000269|PubMed:15548592, ECO:0000269|PubMed:17535814, ECO:0000269|PubMed:23085020}.; . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;cochlea;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;urinary;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;visual apparatus;liver;spleen;kidney;stomach;thymus; testis - interstitial;testis - seminiferous tubule;tumor;testis;ciliary ganglion; 0.28246 0.12378 -0.067881249 48.69072895 1402.19748 7.00148 NUFIP1 3.91687077980072e-06 0.82085529897725 0.17914078415197 nuclear fragile X mental retardation protein interacting protein 1 FUNCTION: Binds RNA. {ECO:0000269|PubMed:10556305}.; . TISSUE SPECIFICITY: Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocyte, heart, brain, placenta, lung, liver, skeletal muscle, kidney, and pancreas. {ECO:0000269|PubMed:10556305}.; . . 0.55277 . -0.200157416 39.11299835 50.37843 1.39556 NUFIP1P . . . nuclear fragile X mental retardation protein interacting protein 1 pseudogene . . . . . . . . . . . NUFIP2 0.992086080094595 0.00791227180433367 1.64810107142472e-06 nuclear fragile X mental retardation protein interacting protein 2 FUNCTION: Binds RNA. {ECO:0000269|PubMed:12837692}.; . . ovary;sympathetic chain;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;atrium;whole body;frontal lobe;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;urinary;blood;skeletal muscle;breast;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.46476 0.11709 0.532823122 80.96249115 235.28095 3.31472 NUGGC 1.95612770357102e-07 0.872652111798325 0.127347692588905 nuclear GTPase, germinal center associated FUNCTION: Plays a role as replication-related GTPase protein in germinal center B-cell. {ECO:0000269|PubMed:19734146}.; . TISSUE SPECIFICITY: Expressed in germinal center B-cell and in lymphomas derived from germinal center B-cell. {ECO:0000269|PubMed:19734146}.; . . 0.16222 . 0.674210096 84.7487615 2657.77618 9.69519 NUMA1 0.999999245387494 7.54612506367232e-07 3.64108585204338e-21 nuclear mitotic apparatus protein 1 FUNCTION: Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority if the nuclear volume (PubMed:10075938). Required for maintenance and establishment of the mitotic spindle poles during symmetric cell divisions, functioning as a tether linking bulk microtubules of the spindle to centrosomes (PubMed:7769006, PubMed:11956313, PubMed:26195665). Also required for proper alignment of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). {ECO:0000269|PubMed:11956313, ECO:0000269|PubMed:1541636, ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:7769006, ECO:0000305|PubMed:10075938, ECO:0000305|PubMed:21816348}.; . . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;ganglion;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;brain;tonsil;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;synovium;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;cornea;placenta;duodenum;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;subthalamic nucleus;medulla oblongata;prostate;thyroid;placenta;prefrontal cortex;globus pallidus;trigeminal ganglion;skeletal muscle; 0.08730 0.25361 -0.547766672 19.96933239 1078.38006 6.29606 NUMB 0.0243991693428803 0.972755138233218 0.00284569242390159 numb homolog (Drosophila) FUNCTION: Plays a role in the process of neurogenesis. Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate. Not required for the proliferation of neural progenitor cells before the onset of neurogenesis. Also involved postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. May also mediate local repair of brain ventricular wall damage.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;thymus;cerebellum; superior cervical ganglion;whole blood;skeletal muscle; 0.75852 0.26361 -0.334253673 30.70299599 128.12894 2.46785 NUMBL 0.751917062061139 0.247993310695927 8.96272429340355e-05 numb homolog (Drosophila)-like FUNCTION: Plays a role in the process of neurogenesis. Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate. Not required for the proliferation of neural progenitor cells before the onset of embryonic neurogenesis. Also required postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. Negative regulator of NF-kappa-B signaling pathway. The inhibition of NF- kappa-B activation is mediated at least in part, by preventing MAP3K7IP2 to interact with polyubiquitin chains of TRAF6 and RIPK1 and by stimulating the 'Lys-48'-linked polyubiquitination and degradation of TRAF6 in cortical neurons. {ECO:0000269|PubMed:18299187, ECO:0000269|PubMed:20079715}.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;lung;larynx;macula lutea;visual apparatus;hippocampus;testis;head and neck;germinal center;brain;stomach; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.29841 0.18720 . . 384.55777 4.13147 NUP35 0.123687364628472 0.871147141308391 0.00516549406313709 nucleoporin 35kDa FUNCTION: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs). Can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC. {ECO:0000269|PubMed:15703211}.; . . medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;prostate;cochlea;bone;testis;ciliary body;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;pharynx;blood;breast;lung;nasopharynx;placenta;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.86824 0.12727 -0.494039303 22.09247464 28.16387 0.90283 NUP37 0.000998328030395386 0.946046953636513 0.0529547183330918 nucleoporin 37kDa FUNCTION: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. {ECO:0000269|PubMed:17363900}.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;colorectal;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.94826 0.12971 -0.339715008 30.06605331 23.07873 0.76984 NUP43 3.54205607988959e-06 0.803512485907625 0.196483972036295 nucleoporin 43kDa FUNCTION: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. {ECO:0000269|PubMed:17363900}.; . . ovary;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;skeletal muscle;breast;pancreas;lung;placenta;liver;duodenum;spleen;head and neck;stomach; tumor;skeletal muscle; 0.48504 . -0.381986487 27.68931352 249.75864 3.40424 NUP50 0.238540627987742 0.754455593426809 0.00700377858544939 nucleoporin 50kDa FUNCTION: Component of the nuclear pore complex that has a direct role in nuclear protein import. Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin- alpha:beta-cargo complex and importin recycling. Interacts with multiple transport receptor proteins including CDKN1B. This interaction is required for correct intracellular transport and degradation of CDKN1B. {ECO:0000269|PubMed:20016008}.; . TISSUE SPECIFICITY: Ubiquitous. Highest levels in testis, peripheral blood leukocytes and fetal liver.; unclassifiable (Anatomical System);ovary;colon;parathyroid;blood;skin;skeletal muscle;bone marrow;breast;uterus;prostate;pancreas;lung;frontal lobe;cerebral cortex;larynx;bone;thyroid;placenta;visual apparatus;hypopharynx;liver;testis;cervix;head and neck;germinal center;kidney;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex;parietal lobe; 0.92579 0.12020 -0.758599262 13.32861524 30.63427 0.97393 NUP50-AS1 . . . NUP50 antisense RNA 1 (head to head) . . . . . . . . . . . NUP50P1 . . . nucleoporin 50 pseudogene 1 . . . . . . . . . . . NUP50P2 . . . nucleoporin 50 pseudogene 2 . . . . . . . . . . . NUP50P3 . . . nucleoporin 50 pseudogene 3 . . . . . . . . . . . NUP54 0.96017275018188 0.0398265165134165 7.33304703855902e-07 nucleoporin 54kDa FUNCTION: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;gum;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.96744 0.14012 -0.203796826 38.81811748 2712.9658 9.80844 NUP58 . . . nucleoporin 58kDa FUNCTION: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250}.; . . . . 0.24910 0.07945 -0.222203495 37.54423213 . . NUP58P1 . . . nucleoporin 58kDa pseudogene 1 . . . . . . . . . . . NUP62 0.804394184233739 0.190444309159041 0.00516150660722009 nucleoporin 62kDa FUNCTION: Essential component of the nuclear pore complex. The N- terminal is probably involved in nucleocytoplasmic transport. The C-terminal is probably involved in protein-protein interaction via coiled-coil formation and may function in anchorage of p62 to the pore complex.; DISEASE: Infantile striatonigral degeneration (SNDI) [MIM:271930]: Neurological disorder characterized by symmetrical degeneration of the caudate nucleus, putamen, and occasionally the globus pallidus, with little involvement of the rest of the brain. The clinical features include developmental regression, choreoathetosis, dystonia, spasticity, dysphagia, failure to thrive, nystagmus, optic atrophy, and mental retardation. {ECO:0000269|PubMed:16786527}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;brain;bladder;tonsil;gall bladder;cartilage;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;uterus;whole body;oesophagus;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;adrenal gland;placenta;duodenum;head and neck;kidney;stomach;aorta; . 0.72112 . -0.529034136 20.85987261 771.89326 5.49936 NUP62CL 0.00439455220578126 0.668694611162625 0.326910836631594 nucleoporin 62kDa C-terminal like . . . . . 0.06215 0.06465 0.813985927 87.81552253 . . NUP85 0.999782631941592 0.000217368047894546 1.05138469875288e-11 nucleoporin 85kDa FUNCTION: Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP98/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2- activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl- inositol 3-kinase-Rac-lammellipodium protrusion cascade. {ECO:0000269|PubMed:12718872, ECO:0000269|PubMed:15995708, ECO:0000269|PubMed:16807356}.; . . lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus;cerebellum; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;cerebellum; 0.32422 0.09458 -0.93133804 9.613116301 117.6478 2.35793 NUP88 4.69521177860175e-06 0.998153166830671 0.00184213795755049 nucleoporin 88kDa FUNCTION: Essential component of nuclear pore complex.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;spinal cord;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;lung;mesenchyma;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; testis - interstitial;testis - seminiferous tubule;testis; 0.90813 0.10329 -1.105907904 6.86482661 151.96324 2.69515 NUP93 0.00486804388235231 0.995129867291184 2.08882646394378e-06 nucleoporin 93kDa FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor nucleoporins, but not NUP153 and TPR, to the NPC. {ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:15703211}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;kidney;stomach;thymus; testis - interstitial;heart;testis - seminiferous tubule;tumor;testis;white blood cells;thymus; 0.98118 0.10229 -1.414605945 4.134229771 297.65678 3.68080 NUP98 0.999999978537761 2.14622390954503e-08 3.72352682770285e-22 nucleoporin 98kDa FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Nup98 and Nup96 are involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC. {ECO:0000269|PubMed:15229283}.; DISEASE: Note=A chromosomal aberration involving NUP98 is found in a form of acute myeloid leukemia. Translocation t(7;11)(p15;p15) with HOXA9. Translocation t(11;17)(p15;p13) with PHF23. {ECO:0000269|PubMed:16028218}.; DISEASE: Note=A chromosomal aberration involving NUP98 is found in childhood acute myeloid leukemia. Translocation t(5;11)(q35;p15.5) with NSD1. Translocation t(8;11)(p11.2;p15) with WHSC1L1. {ECO:0000269|PubMed:16028218}.; DISEASE: Note=A chromosomal aberration involving NUP98 is found in a form of therapy-related myelodysplastic syndrome. Translocation t(11;20)(p15;q11) with TOP1. {ECO:0000269|PubMed:16028218}.; DISEASE: Note=A chromosomal aberration involving NUP98 is found in a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(3;11)(q12.2;p15.4) with LNP1. {ECO:0000269|PubMed:16028218}.; DISEASE: Note=A chromosomal aberration involving NUP98 is associated with pediatric acute myeloid leukemia (AML) with intermediate characteristics between M2-M3 French-American-British (FAB) subtypes. Translocation t(9;11)(p22;p15) with PSIP1/LEDGF. The chimeric transcript is an in-frame fusion of NUP98 exon 8 to PSIP1/LEDGF exon 4. {ECO:0000269|PubMed:16028218}.; DISEASE: Note=A chromosomal aberration involving NUP98 has been identified in acute leukemias. Translocation t(6;11)(q24.1;p15.5) with CCDC28A. The chimeric transcript is an in-frame fusion of NUP98 exon 13 to CCDC28A exon 2. Ectopic expression of NUP98- CCDC28A in mouse promotes the proliferative capacity and self- renewal potential of hematopoietic progenitors and rapidly induced fatal myeloproliferative neoplasms and defects in the differentiation of the erythro-megakaryocytic lineage. {ECO:0000269|PubMed:16028218}.; . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;cerebrum;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.93410 0.18896 -1.288117155 5.012974758 833.00074 5.65331 NUP107 1.19844636512887e-06 0.999994342658185 4.45889545021602e-06 nucleoporin 107kDa FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Required for the assembly of peripheral proteins into the NPC. May anchor NUP62 to the NPC. {ECO:0000269|PubMed:12552102, ECO:0000269|PubMed:15229283}.; . . medulla oblongata;ovary;salivary gland;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;gum;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.90958 0.15492 -0.552898813 19.86317528 107.69069 2.25334 NUP133 0.0662324196154904 0.933767538239003 4.21455061718299e-08 nucleoporin 133kDa FUNCTION: Involved in poly(A)+ RNA transport. {ECO:0000269|PubMed:11684705}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;prefrontal cortex; 0.52299 0.24825 0.518060413 80.35503657 2797.4806 9.98183 NUP153 0.999994457328352 5.54267164638933e-06 1.38099893717627e-15 nucleoporin 153kDa FUNCTION: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat- containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:22253824}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;epididymis;placenta;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; testis - interstitial;superior cervical ganglion;fetal liver;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.98695 0.10551 0.839507251 88.23425336 6828.76712 17.57298 NUP155 0.990594276419902 0.00940572357980869 2.895637528669e-13 nucleoporin 155kDa FUNCTION: Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport. {ECO:0000250|UniProtKB:Q99P88}.; DISEASE: Atrial fibrillation, familial, 15 (ATFB15) [MIM:615770]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:19070573}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues tested, including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; ovary;salivary gland;developmental;intestine;colon;skin;uterus;prostate;whole body;larynx;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);heart;adrenal cortex;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;head and neck;cervix;kidney;stomach; testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node; 0.93001 0.11682 -1.899770452 1.963906582 108.44065 2.25931 NUP160 0.023979152527532 0.976020847403988 6.8480319318896e-11 nucleoporin 160kDa FUNCTION: Involved in poly(A)+ RNA transport. {ECO:0000269|PubMed:11684705}.; . . . . 0.86986 0.12061 -1.765639221 2.323661241 750.99342 5.43602 NUP188 0.987079307345649 0.0129206926543463 5.22540424083661e-15 nucleoporin 188kDa FUNCTION: May function as a component of the nuclear pore complex (NPC).; DISEASE: Note=Copy number variations of NUP188 gene may be a cause of heterotaxy, a congenital heart disease resulting from abnormalities in left-right (LR) body patterning. {ECO:0000269|PubMed:21282601}.; . lymphoreticular;ovary;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;hippocampus;alveolus;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;appendix;globus pallidus;testis;atrioventricular node; 0.66275 0.12628 -1.24580687 5.3668318 450.47399 4.40923 NUP205 0.999998807559353 1.19244064720533e-06 9.19465502116307e-23 nucleoporin 205kDa FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor NUP62 and other nucleoporins, but not NUP153 and TPR, to the NPC. {ECO:0000269|PubMed:15229283}.; . . lymphoreticular;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.97107 0.12226 -0.959131779 9.005661713 597.38765 4.94611 NUP210 1.45347383950117e-10 0.99999474007441 5.25978024226153e-06 nucleoporin 210kDa FUNCTION: Nucleoporin essential for nuclear pore assembly and fusion, nuclear pore spacing, as well as structural integrity. {ECO:0000269|PubMed:14517331}.; . TISSUE SPECIFICITY: Ubiquitous expression, with highest levels in lung, liver, pancreas, testis, and ovary, intermediate levels in brain, kidney, and spleen, and lowest levels in heart and skeletal muscle. {ECO:0000269|PubMed:10048485}.; lymphoreticular;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;iris;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;thymus;bone marrow; 0.16749 0.13858 -2.012488705 1.716206653 589.39177 4.92260 NUP210L 0.144640619732186 0.855359380264052 3.76153732545379e-12 nucleoporin 210kDa like . . . unclassifiable (Anatomical System);lung;testis;germinal center; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node; 0.08973 0.07662 -0.654057602 16.14177872 3525.19978 11.45507 NUP210P1 . . . nucleoporin 210kDa pseudogene 1 . . . lung;testis; superior cervical ganglion;testis - interstitial;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.04743 . . . . . NUP210P2 . . . nucleoporin 210kDa pseudogene 2 . . . . . . . . . . . NUP210P3 . . . nucleoporin 210kDa pseudogene 3 . . . . . . . . . . . NUP214 0.993841692882668 0.00615830711731106 2.07859800395001e-14 nucleoporin 214kDa FUNCTION: May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex.; DISEASE: Note=A chromosomal aberration involving NUP214 is found in a subset of acute myeloid leukemia (AML); also known as acute non-lymphocytic leukemia. Translocation t(6;9)(p23;q34) with DEK. It results in the formation of a DEK-CAN fusion gene. {ECO:0000269|PubMed:1549122}.; DISEASE: Note=A chromosomal aberration involving NUP214 is found in some cases of acute undifferentiated leukemia (AUL). Translocation t(6;9)(q21;q34.1) with SET. {ECO:0000269|PubMed:1630450}.; TISSUE SPECIFICITY: Expressed in thymus, spleen, bone marrow, kidney, brain and testis, but hardly in all other tissues or in whole embryos during development.; ovary;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;muscle;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;trigeminal ganglion; 0.27605 0.21595 -2.148407177 1.474404341 352.78408 3.97785 NUPL2 3.67028875429224e-05 0.597871618629769 0.402091678482689 nucleoporin like 2 FUNCTION: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. In case of infection by HIV-1, it may participate in the docking of viral Vpr at the nuclear envelope. {ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:16000379}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10358091}.; ovary;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;cochlea;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;blood;lens;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; testis - interstitial;occipital lobe;testis - seminiferous tubule;testis; 0.15391 0.10755 0.773521534 87.06062751 1121.33165 6.39368 NUPR1 0.00754108860242725 0.543462869981283 0.44899604141629 nuclear protein 1, transcriptional regulator FUNCTION: Chromatin-binding protein that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Interacts with MSL1 and inhibits its activity on histone H4 'Lys-16' acetylation (H4K16ac). Binds the RELB promoter and activates its transcription, leading to the transactivation of IER3. The NUPR1/RELB/IER3 survival pathway may provide pancreatic ductal adenocarcinoma with remarkable resistance to cell stress, such as starvation or gemcitabine treatment. In breast cancer cells, NUPR1 overexpression leads to the activation of PI3K/AKT signaling pathway, CDKN1A/p21 phosphorylation and relocalization from the nucleus to the cytoplasm, leading to resistance to chemotherapeutic agents, such as doxorubicin. {ECO:0000269|PubMed:19650074, ECO:0000269|PubMed:22565310, ECO:0000269|PubMed:22858377}.; . TISSUE SPECIFICITY: Widely expressed, with high levels in liver, pancreas, prostate, ovary, colon, thyroid, spinal cord, trachea and adrenal gland, moderate levels in heart, placenta, lung, skeletal muscle, kidney, testis, small intestine, stomach and lymph node, and low levels in brain, spleen, thymus and bone marrow. Not detected in peripheral blood leukocytes. {ECO:0000269|PubMed:10092851}.; myocardium;smooth muscle;ovary;salivary gland;colon;parathyroid;choroid;skin;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;hypothalamus;adrenal cortex;skeletal muscle;pancreas;lung;cornea;epididymis;trabecular meshwork;placenta;visual apparatus;liver;duodenum;spleen;kidney;mammary gland;stomach;peripheral nerve; adipose tissue; . . 0.125076652 62.7388535 36.66537 1.10053 NUPR2 . . . nuclear protein 2, transcriptional regulator FUNCTION: Acts as a transcriptional repressor by inhibiting gene expression at the NUPR1 promoter in a p53/TP53-dependent manner in cancer cells (PubMed:25899918). Involved in the G1 cell cycle arrest, and in a decrease in cell viability and cell proliferation (PubMed:25899918). Plays a role as a negative regulator of the protumoral factor NUPR1 (PubMed:25899918). {ECO:0000269|PubMed:25899918}.; . . . . . . . . . . NUS1 0.869942889520546 0.128294971511176 0.00176213896827777 NUS1 dehydrodolichyl diphosphate synthase subunit FUNCTION: With DHDDS, forms the dehydrodolichyl diphosphate syntase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precusrosor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol. Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator. {ECO:0000269|PubMed:16835300, ECO:0000269|PubMed:21572394, ECO:0000269|PubMed:25066056}.; DISEASE: Note=Defects in NUS1 are the cause of a congenital disorder of glycosylation (CDG) characterized by reduced protein glycosylation and altered dolichol profiles in the urine and serum. Affected individuals manifest profound psychomotor retardation, refractory epilepsy, congenital scoliosis, hearing deficit, and visual impairment with macular lesions. {ECO:0000269|PubMed:25066056}.; . . . 0.51934 0.12046 . . 34.05813 1.04425 NUS1P1 . . . NUS1 dehydrodolichyl diphosphate synthase subunit pseudogene 1 . . . . . . . . . . . NUS1P2 . . . NUS1 dehydrodolichyl diphosphate synthase subunit pseudogene 2 . . . . . . . . . . . NUS1P3 . . . NUS1 dehydrodolichyl diphosphate synthase subunit pseudogene 3 . . . . . . . . . . . NUS1P4 . . . NUS1 dehydrodolichyl diphosphate synthase subunit pseudogene 4 . . . . . . . . . . . NUSAP1 0.00510251786113418 0.968284667460729 0.0266128146781369 nucleolar and spindle associated protein 1 FUNCTION: Microtubule-associated protein with the capacity to bundle and stabilize microtubules (By similarity). May associate with chromosomes and promote the organization of mitotic spindle microtubules around them. {ECO:0000250, ECO:0000269|PubMed:12963707}.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;epididymis;nasopharynx;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;fetal liver;superior cervical ganglion;tumor;ciliary ganglion;trigeminal ganglion;thymus; 0.62029 0.09082 0.374860183 75.43052607 5197.51378 14.83789 NUTF2 0.885150385053397 0.113572329599871 0.00127728534673216 nuclear transport factor 2 FUNCTION: Facilitates protein transport into the nucleus. Interacts with the nucleoporin p62 and with Ran. Acts at a relatively late stage of nuclear protein import, subsequent to the initial docking of nuclear import ligand at the nuclear envelope. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import.; . . ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;breast;bile duct;pancreas;lung;cornea;trabecular meshwork;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach;aorta; whole brain;superior cervical ganglion;liver;testis;skeletal muscle; 0.63688 0.14560 -0.009020804 52.8544468 1.21425 0.03903 NUTF2P2 . . . nuclear transport factor 2 pseudogene 2 . . . . . . . . . . . NUTF2P3 . . . nuclear transport factor 2 pseudogene 3 . . . . . . . . . . . NUTF2P4 . . . nuclear transport factor 2 pseudogene 4 . . . . . . . . . . . NUTF2P5 . . . nuclear transport factor 2 pseudogene 5 . . . . . . . . . . . NUTF2P6 . . . nuclear transport factor 2 pseudogene 6 . . . . . . . . . . . NUTF2P7 . . . nuclear transport factor 2 pseudogene 7 . . . . . . . . . . . NUTF2P8 . . . nuclear transport factor 2 pseudogene 8 . . . . . . . . . . . NUTM1 0.00598112649294294 0.993096367561548 0.000922505945509492 NUT midline carcinoma, family member 1 . DISEASE: Note=A chromosomal aberration involving NUT is found in a rare, aggressive, and lethal carcinoma arising in midline organs of young people. Translocation t(15;19)(q14;p13) with BRD4 which produces a BRD4-NUT fusion protein. {ECO:0000269|PubMed:12543779}.; DISEASE: Note=A chromosomal aberration involving NUT is found in a rare, aggressive, and lethal carcinoma arising in midline organs of young people. Translocation t(15;9)(q14;q34) with BRD3 which produces a BRD3-NUT fusion protein. {ECO:0000269|PubMed:12543779}.; TISSUE SPECIFICITY: Specifically expressed in testis. {ECO:0000269|PubMed:12543779}.; . . 0.10314 0.08894 1.431149089 95.02241095 2356.45511 9.00213 NUTM2A 0.672316972777699 0.306415252515349 0.021267774706952 NUT family member 2A . . . . . 0.01294 . . . 1333.788 6.85912 NUTM2A-AS1 . . . NUTM2A antisense RNA 1 . . . . . . . . . . . NUTM2B 0.841786847408577 0.155272461881595 0.00294069070982765 NUT family member 2B . . . . . . . . . 421.0619 4.28418 NUTM2B-AS1 . . . NUTM2B antisense RNA 1 . . . . . . . . . . . NUTM2D 0.227557523833091 0.646694335847721 0.125748140319189 NUT family member 2D . . . . . 0.01294 . . . 4268.05044 12.98771 NUTM2E . . . NUT family member 2E . . . . . . . . . 137.48629 2.55095 NUTM2F . . . NUT family member 2F . . . . . 0.02184 . . . 3005.91421 10.40417 NUTM2G . . . NUT family member 2G . . . . . 0.07276 . 0.99945266 90.6935598 350.17766 3.96731 NUTM2HP . . . NUT family member 2H, pseudogene . . . . . . . . . . . NVL 7.75724236417881e-12 0.991543591501351 0.00845640849089143 nuclear VCP-like FUNCTION: Participates in the assembly of the telomerase holoenzyme and effecting of telomerase activity via its interaction with TERT (PubMed:22226966). May play a role in 60S ribosomal subunit biogenesis (PubMed:15469983, PubMed:16782053). {ECO:0000269|PubMed:15469983, ECO:0000269|PubMed:16782053, ECO:0000269|PubMed:22226966}.; . TISSUE SPECIFICITY: Widely expressed. Highest level of expression in heart, placenta, skeletal muscle, pancreas and retina. {ECO:0000269|PubMed:9286697}.; ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;ganglion;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;trophoblast;heart;islets of Langerhans;hypothalamus;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;kidney;stomach; uterus corpus;superior cervical ganglion;skeletal muscle; 0.10354 0.11916 0.558509856 81.67020524 427.87942 4.32006 NWD1 1.37145309271971e-19 0.00966014847147486 0.990339851528525 NACHT and WD repeat domain containing 1 FUNCTION: May play a role in the control of androgen receptor (AR) protein steady-state levels. {ECO:0000269|PubMed:24681825}.; . TISSUE SPECIFICITY: Expressed at highest levels in prostate, followed by testis, retina, trachea and optic nerve. Also detected in brain, epididymis, lung, vagina and pituitary. In the prostate, tends to be up-regulated during malignant progression compared to normal epithelium (at protein level). {ECO:0000269|PubMed:24681825}.; meninges;prostate;pia mater;lung;frontal lobe;larynx;nasopharynx;head and neck;dura mater;skin;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12729 . 1.760151744 96.7386176 5709.80646 15.67049 NWD2 . . . NACHT and WD repeat domain containing 2 . . . . . 0.87439 . 0.310540264 72.65864591 . . NXF1 0.998990474742992 0.00100952523885547 1.81528632959311e-11 nuclear RNA export factor 1 FUNCTION: Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway). The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the TREX complex. ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1 heterodimer for export. {ECO:0000269|PubMed:18364396, ECO:0000269|PubMed:19165146, ECO:0000269|PubMed:9660949}.; . TISSUE SPECIFICITY: Expressed ubiquitously.; ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;pineal body;blood;breast;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.58705 0.16040 -0.66859065 15.76433121 35.98594 1.08112 NXF2 . . . nuclear RNA export factor 2 FUNCTION: Involved in the export of mRNA from the nucleus to the cytoplasm.; . TISSUE SPECIFICITY: Expressed almost exclusively in testis. Also expressed in several cancers. {ECO:0000269|PubMed:12704671}.; lung;bone;thyroid;testis;head and neck;kidney; . 0.14556 0.09389 . . . . NXF2B 0.760751147925074 0.230359807828964 0.00888904424596137 nuclear RNA export factor 2B FUNCTION: Involved in the export of mRNA from the nucleus to the cytoplasm.; . TISSUE SPECIFICITY: Expressed almost exclusively in testis. Also expressed in several cancers. {ECO:0000269|PubMed:12704671}.; . . 0.12120 . . . . . NXF3 0.00853781286314966 0.988756250624808 0.00270593651204275 nuclear RNA export factor 3 FUNCTION: May function as a tissue-specific nuclear mRNA export factor.; . TISSUE SPECIFICITY: Expressed at high level in testis and at low level in a small number of tissues.; . . 0.56583 0.08542 -0.359940251 28.93371078 9.08387 0.33238 NXF4 . . . nuclear RNA export factor 4 pseudogene . . . testis; . 0.15298 0.08341 . . . . NXF5 0.00420784516244663 0.96130537346915 0.0344867813684029 nuclear RNA export factor 5 FUNCTION: Could be involved in the export of mRNA from the nucleus to the cytoplasm. Could also have a role in polarized cytoplasmic transport and localization of mRNA in neurons.; DISEASE: Note=A chromosomal aberration involving NXF5 has been observed in one patient with a syndromic form of mental retardation and short stature. Pericentric inversion inv(X)(p21.1;q22) that interrupts NXF5. {ECO:0000269|PubMed:11566096}.; . . . 0.19810 . 1.929210393 97.45812692 107.8307 2.25521 NXN 0.86063738959499 0.139273118276939 8.94921280711636e-05 nucleoredoxin FUNCTION: Functions as a redox-dependent negative regulator of the Wnt signaling pathway, possibly by preventing ubiquitination of DVL3 by the BCR(KLHL12) complex. May also function as a transcriptional regulator act as a regulator of protein phosphatase 2A (PP2A) (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;thyroid;bone;testis;brain;pineal gland;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;liver;head and neck;kidney;peripheral nerve; prostate;superior cervical ganglion;lung;trigeminal ganglion;skeletal muscle; 0.29418 0.11588 -0.822919685 11.76574664 183.88473 2.94331 NXNL1 0.0616906043285848 0.721719330779874 0.216590064891542 nucleoredoxin-like 1 FUNCTION: May play a role in cone cell viability, slowing down cone degeneration, does not seem to play a role in degenerating rods. {ECO:0000250}.; . . unclassifiable (Anatomical System);retina;cerebellum; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22946 0.15907 . . 56.7191 1.51445 NXNL2 0.477417234289534 0.439073168814314 0.0835095968961514 nucleoredoxin-like 2 FUNCTION: May be involved in the maintenance of both the function and the viability of sensory neurons, including photoreceptors and olfactory neurons. {ECO:0000250}.; . . . . 0.13940 0.11402 0.347360312 73.97381458 151.58957 2.69267 NXNP1 . . . nucleoredoxin pseudogene 1 . . . . . . . . . . . NXPE1 3.48609216284613e-10 0.013053176090485 0.986946823560906 neurexophilin and PC-esterase domain family member 1 . . . . . 0.06271 . 1.087645262 91.8494928 4139.53327 12.76804 NXPE2 0.244911849376349 0.643352609902007 0.111735540721644 neurexophilin and PC-esterase domain family member 2 . . . . . 0.11501 . 1.43862044 95.05779665 537.77239 4.72835 NXPE2P1 . . . neurexophilin and PC-esterase domain family member 2 pseudogene 1 . . . . . . . . . . . NXPE3 0.402099827242488 0.596036396999902 0.0018637757576102 neurexophilin and PC-esterase domain family member 3 . . . . . 0.09010 . -0.933156985 9.54824251 82.38899 1.92750 NXPE4 2.74741341116275e-08 0.160279639419271 0.839720333106595 neurexophilin and PC-esterase domain family member 4 . . . . . 0.08693 0.08939 2.954785999 99.17433357 2117.75451 8.47280 NXPH1 0.555861072202942 0.431146431908025 0.0129924958890325 neurexophilin 1 FUNCTION: May be signaling molecules that resemble neuropeptides and that act by binding to alpha-neurexins and possibly other receptors. {ECO:0000305}.; . . . . 0.12574 . -0.383807564 27.41802312 7.97032 0.29253 NXPH2 0.798014407186903 0.196360803862114 0.00562478895098308 neurexophilin 2 FUNCTION: May be signaling molecules that resemble neuropeptides and that act by binding to alpha-neurexins and possibly other receptors. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in brain and kidney.; unclassifiable (Anatomical System);ovary;developmental;kidney;brain;retina; . 0.43799 0.10891 -0.163345027 41.24793583 12.14463 0.43965 NXPH3 0.793272419563662 0.200741228238333 0.00598635219800515 neurexophilin 3 FUNCTION: May be signaling molecules that resemble neuropeptides. Ligand for alpha-neurexins (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highest level in brain.; unclassifiable (Anatomical System);uterus;heart;placenta;urinary;brain;skin;stomach;cerebellum; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle;cerebellum; 0.16040 0.10420 -0.139478553 43.29440906 18.74987 0.64725 NXPH4 0.462095793940255 0.512140499991911 0.0257637060678332 neurexophilin 4 FUNCTION: May be signaling molecules that resemble neuropeptides and that act by binding to alpha-neurexins and possibly other receptors. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in brain, spleen, and testis.; unclassifiable (Anatomical System);heart;cartilage;muscle;blood;fovea centralis;choroid;lens;skin;retina;optic nerve;lung;placenta;bone;macula lutea;visual apparatus;testis;germinal center;kidney;brain;mammary gland;gall bladder; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.06674 . -0.095386216 46.48502005 452.3782 4.42458 NXT1 0.574740218091013 0.380203391853098 0.0450563900558896 nuclear transport factor 2-like export factor 1 FUNCTION: Stimulator of protein export for NES-containing proteins. Also plays a role in the nuclear export of U1 snRNA, tRNA, and mRNA. The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5. {ECO:0000269|PubMed:10567585, ECO:0000269|PubMed:10848583, ECO:0000269|PubMed:11259602, ECO:0000269|PubMed:19165146}.; . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;muscle;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; testis - seminiferous tubule;testis; 0.10930 0.12971 -0.09720619 46.20193442 3.21101 0.11543 NXT1P1 . . . NTF2-like export factor 1 pseudogene 1 . . . . . . . . . . . NXT2 0.777280517968738 0.215400937119853 0.00731854491140953 nuclear transport factor 2-like export factor 2 FUNCTION: Regulator of protein export for NES-containing proteins. Also plays a role in mRNA nuclear export.; . . ovary;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;adrenal cortex;skeletal muscle;bile duct;breast;pancreas;lung;placenta;liver;head and neck;kidney;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion; 0.00230 0.02889 0.013025609 54.62962963 1.49817 0.05093 NYAP1 0.990932129553248 0.00906740490605262 4.65540698808497e-07 neuronal tyrosine phosphorylated phosphoinositide-3-kinase adaptor 1 FUNCTION: Activates PI3K and concomitantly recruits the WAVE1 complex to the close vicinity of PI3K and regulates neuronal morphogenesis. {ECO:0000250}.; . . unclassifiable (Anatomical System);islets of Langerhans;brain; . 0.40311 . -1.240018202 5.461193678 99.93954 2.16727 NYAP2 0.906196258132315 0.0937720346138807 3.17072538043049e-05 neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adaptor 2 FUNCTION: Activates PI3K and concomitantly recruits the WAVE1 complex to the close vicinity of PI3K and regulates neuronal morphogenesis. {ECO:0000250}.; . . medulla oblongata;frontal lobe;endometrium; dorsal root ganglion;superior cervical ganglion;fetal liver;testis;ciliary ganglion;atrioventricular node;pons;skeletal muscle;skin; . . -0.020150552 52.25288983 158.7708 2.75169 NYNRIN 0.000549672204856649 0.999440540647652 9.787147491215e-06 NYN domain and retroviral integrase containing . . . medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;testis;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;breast;lung;placenta;hippocampus;visual apparatus;macula lutea;liver;head and neck;kidney; fetal liver;superior cervical ganglion;fetal brain;placenta;fetal lung;cerebellum; 0.20740 0.09696 -1.00503845 8.215380986 650.17192 5.11584 NYS2 . . . nystagmus 2, congenital autosomal dominant . . . . . . . . . . . NYS3 . . . nystagmus 3, congenital autosomal dominant . . . . . . . . . . . NYS4 . . . nystagmus 4, congenital autosomal dominant . . . . . . . . . . . NYX 0.0624131502401644 0.723387042464111 0.214199807295725 nyctalopin . . TISSUE SPECIFICITY: Expressed in kidney and retina. Also at low levels in brain, testis and muscle. Within the retina, expressed in the inner segment of photoreceptors, outer and inner nuclear layers and the ganglion cell layer. {ECO:0000269|PubMed:11062471, ECO:0000269|PubMed:11062472}.; kidney; dorsal root ganglion;ciliary ganglion;pons;atrioventricular node; 0.21755 0.23824 . . 76.8456 1.84047 OA3 . . . ocular albinism 3 (autosomal recessive) . . . . . . . . . . . OACYLP . . . O-acyltransferase like, pseudogene . . . . . . . . . . . OAF 0.00616888335875156 0.738219403153239 0.25561171348801 out at first homolog . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;oesophagus;endometrium;bone;thyroid;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;nervous;pharynx;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;amnion;spleen;kidney;mammary gland;stomach;thymus; . 0.22538 0.11129 0.150760231 64.51403633 2549.59731 9.43020 OAP . . . osteoarthrosis, precocious . . . . . . . . . . . OARD1 0.12375137115757 0.852078186744035 0.0241704420983948 O-acyl-ADP-ribose deacylase 1 FUNCTION: Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Catalyzes the deacylation of O- acetyl-ADP-ribose, O-propionyl-ADP-ribose and O-butyryl-ADP- ribose, yielding ADP-ribose plus acetate, propionate and butyrate, respectively.; . . . . 0.41684 . -0.117432389 44.89266336 23.06778 0.76958 OAS1 0.00123924128980461 0.958663067572877 0.0400976911373186 2'-5'-oligoadenylate synthetase 1 FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. The secreted form displays antiviral effect against vesicular stomatitis virus (VSV), herpes simplex virus type 2 (HSV-2), and encephalomyocarditis virus (EMCV) and stimulates the alternative antiviral pathway independent of RNase L. {ECO:0000269|PubMed:12799444, ECO:0000269|PubMed:18931074, ECO:0000269|PubMed:19923450, ECO:0000269|PubMed:23319625}.; . . medulla oblongata;ovary;colon;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;oral cavity;muscle;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion; 0.02387 0.18982 1.311772884 94.03750885 404.61652 4.21858 OAS2 1.89091809637863e-14 0.0280093446261667 0.971990655373814 2'-5'-oligoadenylate synthetase 2 FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. {ECO:0000269|PubMed:10464285, ECO:0000269|PubMed:19923450, ECO:0000269|PubMed:9880569}.; . . unclassifiable (Anatomical System);lymphoreticular;smooth muscle;heart;ovary;colon;blood;vein;skin;bone marrow;breast;uterus;lung;nasopharynx;placenta;liver;testis;cervix;germinal center;brain; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07914 0.10385 -1.083859071 7.195093182 31.80189 1.00041 OAS3 1.82237568934062e-23 0.000186791663001452 0.999813208336998 2'-5'-oligoadenylate synthetase 3 FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes preferentially dimers of 2'-5'- oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. Displays antiviral activity against Chikungunya virus (CHIKV), Dengue virus, Sindbis virus (SINV) and Semliki forest virus (SFV). {ECO:0000269|PubMed:19056102, ECO:0000269|PubMed:19923450, ECO:0000269|PubMed:9880533}.; . TISSUE SPECIFICITY: Present at high level in placenta trophoblast.; unclassifiable (Anatomical System);smooth muscle;lymph node;heart;tongue;islets of Langerhans;colon;skin;skeletal muscle;retina;breast;uterus;prostate;pancreas;lung;frontal lobe;larynx;bone;placenta;hypopharynx;liver;head and neck;germinal center;brain;mammary gland;bladder;stomach;peripheral nerve; . 0.09411 . -0.255386946 34.98466619 831.35724 5.64923 OASD . . . ocular albinism and sensorineural deafness . . . . . . . . . . . OASL 5.07293522290638e-12 0.0148594912432892 0.985140508751638 2'-5'-oligoadenylate synthetase like FUNCTION: Does not have 2'-5'-OAS activity, but can bind double- stranded RNA. Displays antiviral activity against encephalomyocarditis virus (EMCV) and hepatitis C virus (HCV) via an alternative antiviral pathway independent of RNase L. {ECO:0000269|PubMed:18931074, ECO:0000269|PubMed:20074559, ECO:0000269|PubMed:9826176}.; . TISSUE SPECIFICITY: Expressed in most tissues, with the highest levels in primary blood Leukocytes and other hematopoietic system tissues, colon, stomach and to some extent in testis.; unclassifiable (Anatomical System);hypothalamus;colon;skeletal muscle;bone marrow;uterus;pancreas;prostate;lung;oesophagus;larynx;nasopharynx;bone;thyroid;alveolus;liver;testis;cervix;brain;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.10031 0.10724 -0.398573136 26.92852088 65.07146 1.66071 OAT 0.000721947397616178 0.980652088262413 0.0186259643399706 ornithine aminotransferase . DISEASE: Hyperornithinemia with gyrate atrophy of choroid and retina (HOGA) [MIM:258870]: A disorder clinically characterized by a triad of progressive chorioretinal degeneration, early cataract formation, and type II muscle fiber atrophy. Characteristic chorioretinal atrophy with progressive constriction of the visual fields leads to blindness at the latest during the sixth decade of life. Patients generally have normal intelligence. {ECO:0000269|PubMed:1612597, ECO:0000269|PubMed:1737786, ECO:0000269|PubMed:23076989, ECO:0000269|PubMed:2793865, ECO:0000269|PubMed:3375240, ECO:0000269|PubMed:7668253, ECO:0000269|PubMed:7887415}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.17989 0.64248 -0.758599262 13.32861524 35.22668 1.06690 OATP1 . . . ornithine aminotransferase pseudogene 1 . . . . . . . . . . . OAZ1 0.0889951573895078 0.870164343893438 0.0408404987170542 ornithine decarboxylase antizyme 1 FUNCTION: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake by binding to and targeting ODC1 for degradation (PubMed:17900240). Stabilizes AZIN2 by interfering with its ubiquitination. Also inhibits cellular uptake of polyamines by inactivating the polyamine uptake transporter. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. Involved in the translocation of AZNI2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol. {ECO:0000269|PubMed:12097147, ECO:0000269|PubMed:17900240}.; . . myocardium;lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;thyroid;germinal center;brain;heart;cartilage;urinary;adrenal cortex;blood;lens;greater omentum;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus;cerebellum; amygdala;whole brain;heart;placenta;whole blood;cingulate cortex;cerebellum;bone marrow; 0.25753 0.17559 . . 3445.77791 11.27865 OAZ2 0.866153028384412 0.131948233720101 0.00189873789548664 ornithine decarboxylase antizyme 2 FUNCTION: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake by binding to ODC1 without promoting its degradation (PubMed:17900240). Involved in the translocation of AZNI2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol. {ECO:0000269|PubMed:17900240}.; . . . . 0.70388 . . . 17.63191 0.61771 OAZ3 9.17261329992055e-05 0.554969770749449 0.444938503117552 ornithine decarboxylase antizyme 3 FUNCTION: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake by binding to ODC1 without promoting its degradation (PubMed:17900240). Stabilizes AZIN2 by interfering with its ubiquitination. Involved in the translocation of AZNI2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol. Probably plays a key role in spermatogenesis by regulating the intracellular concentration of polyamines in haploid germ cells. {ECO:0000269|PubMed:17900240}.; . TISSUE SPECIFICITY: Testis specific.; unclassifiable (Anatomical System);lung;heart;liver;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.24911 0.11506 . . 74.93989 1.81173 OBFC1 1.32529699599379e-05 0.838151934839213 0.161834812190827 oligonucleotide/oligosaccharide-binding fold containing 1 FUNCTION: Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation (PubMed:19854130). However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha (PubMed:22964711, PubMed:22763445). The CST complex facilitates recovery from many forms of exogenous DNA damage; seems to be involved in the re- initiation of DNA replication at repaired forks and/or dormant origins (PubMed:25483097). Required for efficicient replication of the duplex region of the telomere. Promotes efficient replication of lagging-strand telomeres (PubMed:22863775, PubMed:22964711). Promotes general replication start following replication-fork stalling implicating new origin firing (PubMed:22863775). May be in involved in C-strand fill-in during late S/G2 phase independent of ot its role in telomere duplex replication (PubMed:23142664). {ECO:0000269|PubMed:19648609, ECO:0000269|PubMed:19854130, ECO:0000269|PubMed:22763445, ECO:0000269|PubMed:22863775, ECO:0000269|PubMed:22964711, ECO:0000269|PubMed:23142664, ECO:0000269|PubMed:25483097, ECO:0000305|PubMed:23851344}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;bile duct;breast;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;kidney;stomach; testis - interstitial;tongue;testis; 0.06080 0.09168 0.350995466 74.37485256 48.55031 1.35928 OBP2A 0.000133913764845764 0.405424902750989 0.594441183484165 odorant binding protein 2A FUNCTION: Probably binds and transports small hydrophobic volatile molecules with a higher affinity for aldehydes and large fatty acids. {ECO:0000269|PubMed:12044155}.; . TISSUE SPECIFICITY: Strongly expressed in the nasal structures, salivary and lachrymal glands, and lung.; . . 0.05229 0.08021 1.328368696 94.12597311 7734.45791 18.95125 OBP2B 0.182972936041483 0.764684023377452 0.0523430405810655 odorant binding protein 2B FUNCTION: Probably binds and transports small hydrophobic volatile molecules.; . TISSUE SPECIFICITY: Strongly expressed in genital sphere organs such as the prostate and mammary glands.; . . 0.07451 . 0.593509966 82.51356452 9.30105 0.34150 OBSCN 5.35738960908037e-91 1.16848963531787e-06 0.999998831510365 obscurin, cytoskeletal calmodulin and titin-interacting RhoGEF FUNCTION: Involved in myofibrillogenesis. Seems to be involved in assembly of myosin into sarcomeric A bands in striated muscle. Isoform 3 together with ANK1 isoform Mu17/Ank1.5 may provide a molecular link between the sarcoplasmic reticulum and myofibrils. {ECO:0000269|PubMed:11448995, ECO:0000269|PubMed:16205939}.; DISEASE: Note=A chromosomal aberration involving OBSCN has been found in Wilms tumor. Translocation t(1;7)(q42;p15) with PTHB1. {ECO:0000269|PubMed:12618763}.; . unclassifiable (Anatomical System);cartilage;heart;ovary;muscle;colon;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;breast;optic nerve;lung;frontal lobe;larynx;thyroid;placenta;macula lutea;hypopharynx;duodenum;head and neck;kidney;brain; dorsal root ganglion;occipital lobe;medulla oblongata;superior cervical ganglion;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;adrenal gland;globus pallidus;ciliary ganglion;cerebellum; 0.18040 0.12775 . . 33482.92348 35.92354 OBSL1 6.64137887872857e-16 0.777707243511558 0.222292756488442 obscurin-like 1 FUNCTION: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695, PubMed:24793696). Acts as a regulator of the Cul7-RING(FBXW8) ubiquitin-protein ligase, playing a critical role in the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Required to localize CUL7 to the Golgi apparatus in neurons. {ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24793695, ECO:0000269|PubMed:24793696}.; . TISSUE SPECIFICITY: Widely expressed, with predominant levels found in the heart. {ECO:0000269|PubMed:17289344}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;muscle;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;macula lutea;liver;hypopharynx;head and neck;kidney;mammary gland;thymus; dorsal root ganglion;uterus corpus;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;thyroid;testis;atrioventricular node; 0.18328 . -0.814205844 12.01934418 4573.34304 13.56826 OC90 8.16819622863985e-09 0.151717451954263 0.84828253987754 otoconin 90 FUNCTION: It is unlikely that this protein has phospholipase A2 activity.; . . frontal lobe; dorsal root ganglion;superior cervical ganglion;pancreas;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;parietal lobe;skeletal muscle;cerebellum; 0.04900 0.11324 0.446457185 77.97829677 2254.92856 8.77020 OCA2 7.67937025845118e-12 0.641478269876385 0.358521730115936 OCA2 melanosomal transmembrane protein FUNCTION: Could be involved in the transport of tyrosine, the precursor to melanin synthesis, within the melanocyte. Regulates the pH of melanosome and the melanosome maturation. One of the components of the mammalian pigmentary system. Seems to regulate the post-translational processing of tyrosinase, which catalyzes the limiting reaction in melanin synthesis. May serve as a key control point at which ethnic skin color variation is determined. Major determinant of brown and/or blue eye color. {ECO:0000269|PubMed:11310796, ECO:0000269|PubMed:15262401, ECO:0000269|PubMed:18252222, ECO:0000269|PubMed:22234890, ECO:0000269|PubMed:7601462}.; DISEASE: Albinism, oculocutaneous, 2 (OCA2) [MIM:203200]: An autosomal recessive disorder in which the biosynthesis of melanin pigment is reduced in skin, hair, and eyes. Although affected infants may appear at birth to have complete absence of melanin pigment, most patients acquire small amounts of pigment with age. Visual anomalies include decreased acuity and nystagmus. The phenotype is highly variable. The hair of affected individuals may turn darker with age, and pigmented nevi or freckles may be seen. African and African American individuals may have yellow hair and blue-gray or hazel irides. One phenotypic variant, 'brown OCA,' has been described in African and African American populations and is characterized by light brown hair and skin color and gray to tan irides. {ECO:0000269|PubMed:10649493, ECO:0000269|PubMed:10671067, ECO:0000269|PubMed:10987646, ECO:0000269|PubMed:12713581, ECO:0000269|PubMed:12727022, ECO:0000269|PubMed:12876664, ECO:0000269|PubMed:17385796, ECO:0000269|PubMed:23504663, ECO:0000269|PubMed:7762554, ECO:0000269|PubMed:7874125, ECO:0000269|PubMed:9259203}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);optic nerve;lung;heart;synovium;placenta;brain;pineal gland;skin;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.12316 0.36621 0.126687467 62.75064874 2610.71907 9.56469 OCA5 . . . oculocutaneous albinism 5 (autosomal recessive) . . . . . . . . . . . OCEL1 0.00014470501488926 0.654410582841867 0.345444712143244 occludin/ELL domain containing 1 . . . unclassifiable (Anatomical System);cartilage;colon;parathyroid;fovea centralis;choroid;lens;retina;bone marrow;optic nerve;whole body;lung;cochlea;synovium;nasopharynx;placenta;macula lutea;liver;testis;spleen;germinal center;brain;pineal gland;aorta; liver; 0.10176 0.08021 0.709197509 85.68058504 1659.64521 7.52625 OCIAD1 4.71641550912238e-06 0.850436077149463 0.149559206435028 OCIA domain containing 1 . . TISSUE SPECIFICITY: Isoform 1 is highly expressed in many tissues, including testis, brain, placenta, ovary, prostate and mammary gland. Isoform 2 expression is restricted to the central nervous system including brain, cerebellum and spinal cord. {ECO:0000269|PubMed:11162530}.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;spinal cord;adrenal cortex;blood;lens;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;atrium;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;oral cavity;bile duct;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach; whole brain;amygdala;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.07701 0.09936 -0.071520315 48.34866714 28.80665 0.92091 OCIAD1-AS1 . . . OCIAD1 antisense RNA 1 . . . . . . . . . . . OCIAD2 0.00459157056484811 0.875627444626888 0.119780984808264 OCIA domain containing 2 . . . unclassifiable (Anatomical System);heart;pineal body;colon;parathyroid;skin;retina;uterus;prostate;whole body;lung;thyroid;liver;spleen;kidney;brain;aorta;stomach; kidney; 0.07209 0.07289 0.591694063 82.45458835 72.83431 1.78117 OCIAD2P1 . . . OCIA domain containing 2 pseudogene 1 . . . . . . . . . . . OCLM 0.0173290392628945 0.481734391585593 0.500936569151512 oculomedin . . TISSUE SPECIFICITY: Expressed in eye trabeculum; also expressed in retina.; . . . . . . 8.43166 0.30776 OCLN 0.491025450228121 0.508026582461961 0.000947967309918372 occludin FUNCTION: May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. It is able to induce adhesion when expressed in cells lacking tight junctions. {ECO:0000269|PubMed:19114660}.; DISEASE: Band-like calcification with simplified gyration and polymicrogyria (BLCPMG) [MIM:251290]: A neurologic disorder with characteristic clinical and neuroradiologic features that mimic intrauterine TORCH infection in the absence of evidence of infection. Affected individuals have congenital microcephaly, intracranial calcifications, and severe developmental delay. {ECO:0000269|PubMed:20727516}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Localized at tight junctions of both epithelial and endothelial cells. Highly expressed in kidney. Not detected in testis.; unclassifiable (Anatomical System);lymph node;adrenal cortex;colon;parathyroid;skeletal muscle;breast;uterus;whole body;lung;frontal lobe;adrenal gland;thyroid;placenta;duodenum;liver;testis;spleen;kidney;brain;pineal gland;stomach; . 0.37931 0.39545 0.483275131 79.25218212 78.93207 1.87692 OCM 5.57372955370736e-06 0.139591068770976 0.86040335749947 oncomodulin FUNCTION: Has some calmodulin-like activity with respect to enzyme activation and growth regulation. Binds two calcium ions.; . . unclassifiable (Anatomical System); . 0.15102 0.16206 0.43736446 77.56546355 113.18627 2.31610 OCM2 0.0800687372958595 0.754149340309966 0.165781922394175 oncomodulin 2 . . . unclassifiable (Anatomical System); . 0.15102 0.11809 0.413500896 76.67492333 34.46225 1.05244 OCRL 0.999918298029263 8.17019659461247e-05 4.79124191777583e-12 oculocerebrorenal syndrome of Lowe FUNCTION: Converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate. Also converts inositol 1,4,5- trisphosphate to inositol 1,4-bisphosphate and inositol 1,3,4,5- tetrakisphosphate to inositol 1,3,4-trisphosphate. May function in lysosomal membrane trafficking by regulating the specific pool of phosphatidylinositol 4,5-bisphosphate that is associated with lysosomes. Involved in primary cilia assembly. {ECO:0000269|PubMed:22228094, ECO:0000269|PubMed:22543976}.; DISEASE: Lowe oculocerebrorenal syndrome (OCRL) [MIM:309000]: X- linked multisystem disorder affecting eyes, nervous system, and kidney. It is characterized by hydrophthalmia, cataract, mental retardation, vitamin D-resistant rickets, aminoaciduria, and reduced ammonia production by the kidney. Ocular abnormalities include cataract, glaucoma, microphthalmos, and decreased visual acuity. Developmental delay, hypotonia, behavior abnormalities, and areflexia are also present. Renal tubular involvement is characterized by impaired reabsorption of bicarbonate, amino acids, and phosphate. Musculoskeletal abnormalities such as joint hypermobility, dislocated hips, and fractures may develop as consequences of renal tubular acidosis and hypophosphatemia. Cataract is the only significant manifestation in carriers and is detected by slit-lamp examination. {ECO:0000269|PubMed:10767176, ECO:0000269|PubMed:10923037, ECO:0000269|PubMed:19168822, ECO:0000269|PubMed:20133602, ECO:0000269|PubMed:21031565, ECO:0000269|PubMed:21233288, ECO:0000269|PubMed:9199559, ECO:0000269|PubMed:9632163, ECO:0000269|PubMed:9682219, ECO:0000269|PubMed:9788721}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dent disease 2 (DD2) [MIM:300555]: A renal disease belonging to the 'Dent disease complex', a group of disorders characterized by proximal renal tubular defect, hypercalciuria, nephrocalcinosis, and renal insufficiency. The spectrum of phenotypic features is remarkably similar in the various disorders, except for differences in the severity of bone deformities and renal impairment. Characteristic abnormalities include low-molecular-weight proteinuria and other features of Fanconi syndrome, such as glycosuria, aminoaciduria, and phosphaturia, but typically do not include proximal renal tubular acidosis. Progressive renal failure is common, as are nephrocalcinosis and kidney stones. {ECO:0000269|PubMed:15627218, ECO:0000269|PubMed:17384968, ECO:0000269|PubMed:21031565}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Brain, skeletal muscle, heart, kidney, lung, placenta and fibroblasts. Expressed in the retina and the retinal pigment epithelium. {ECO:0000269|PubMed:22543976}.; colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;thyroid;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;adrenal cortex;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;hippocampus;visual apparatus;liver;cervix;head and neck;mammary gland;stomach; superior cervical ganglion; 0.33365 0.09724 -0.247889024 35.98726115 56.95289 1.51918 OCSTAMP . . . osteoclast stimulatory transmembrane protein FUNCTION: Probable cell surface receptor that plays a role in cellular fusion and cell differentiation. Cooperates with DCSTAMP in modulating cell-cell fusion in both osteoclasts and foreign body giant cells (FBGCs). Involved in osteoclast bone resorption. Promotes osteoclast differentiation and may play a role in the multinucleated osteoclast maturation (By similarity). {ECO:0000250}.; . . . . 0.04961 . 0.237127192 68.98443029 310.4637 3.74976 ODAM 1.16193333896843e-13 0.0059784928281019 0.994021507171782 odontogenic, ameloblast asssociated FUNCTION: Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF and expression of downstream factors such as ROCK. Plays a role in attachment of the junctional epithelium to the tooth surface. {ECO:0000269|PubMed:25911094}.; . TISSUE SPECIFICITY: Expressed in the junctional epithelium of healthy teeth. In periodontitis, absent in the pocket epithelium of the diseased periodontium but is detected in the gingival crevicular fluid. {ECO:0000269|PubMed:25911094}.; . . 0.09799 . 0.260991686 70.25831564 1694.26448 7.58952 ODC1 0.950802102507626 0.0491675508277189 3.03466646555914e-05 ornithine decarboxylase 1 FUNCTION: Key enzyme of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. {ECO:0000269|PubMed:17900240}.; . . lymphoreticular;ovary;skin;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;aorta; prostate;testis - interstitial;testis - seminiferous tubule;tumor;testis; 0.26949 0.39778 -0.446304853 24.33356924 50.41837 1.39648 ODCP . . . ornithine decarboxylase pseudogene . . . . . . . . . . . ODF1 0.417383751319128 0.574629914083107 0.00798633459776456 outer dense fiber of sperm tails 1 FUNCTION: Component of the outer dense fibers (ODF) of spermatozoa. ODF are filamentous structures located on the outside of the axoneme in the midpiece and principal piece of the mammalian sperm tail and may help to maintain the passive elastic structures and elastic recoil of the sperm tail.; . TISSUE SPECIFICITY: Testis.; unclassifiable (Anatomical System);lung;testis; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node; 0.49644 0.10958 0.595326758 82.66100495 4051.14892 12.60725 ODF2 0.365893592358874 0.634105565886238 8.41754887994117e-07 outer dense fiber of sperm tails 2 FUNCTION: Seems to be a major component of sperm tail outer dense fibers (ODF). ODFs are filamentous structures located on the outside of the axoneme in the midpiece and principal piece of the mammalian sperm tail and may help to maintain the passive elastic structures and elastic recoil of the sperm tail. May have a modulating influence on sperm motility. Functions as a general scaffold protein that is specifically localized at the distal/subdistal appendages of mother centrioles. Component of the centrosome matrix required for the localization of PLK1 and NIN to the centrosomes. Required for the formation and/or maintenance of normal CETN1 assembly. {ECO:0000269|PubMed:16966375}.; . TISSUE SPECIFICITY: Testis-specific (at protein level). Highly expressed in cytoplasm of step 2 round spermatids. Detected in the middle piece and extends to about half the principal piece of the sperm tails. {ECO:0000269|PubMed:10381817}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;blood;lens;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion; 0.51434 0.14684 -0.683363435 15.36329323 135.29651 2.53102 ODF2-AS1 . . . ODF2 antisense RNA 1 . . . . . . . . . . . ODF2L 3.32070872906533e-09 0.509856274879658 0.490143721799633 outer dense fiber of sperm tails 2 like . . . colon;fovea centralis;bone marrow;prostate;whole body;endometrium;thyroid;pituitary gland;testis;spinal ganglion;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;cervix;spleen;kidney;stomach; . 0.09086 0.08344 -0.220384297 37.6032083 719.8393 5.32564 ODF3 0.586974862090879 0.402841641448495 0.0101834964606263 outer dense fiber of sperm tails 3 FUNCTION: Outer dense fibers are filamentous structures located on the outside of the axoneme in the midpiece and principal piece of the mammalian sperm tail. May help to maintain the passive elastic structures and elastic recoil of the sperm tail.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:11870087, ECO:0000269|Ref.2}.; testis; . 0.18037 0.10950 0.174625237 65.9648502 456.66332 4.43875 ODF3B 0.00916745822195973 0.809610408024332 0.181222133753708 outer dense fiber of sperm tails 3B . . . . . . . . . 346.54234 3.94853 ODF3L1 5.18159832927925e-07 0.234676017276446 0.765323464563721 outer dense fiber of sperm tails 3-like 1 . . . unclassifiable (Anatomical System);uterus;lung;heart;hippocampus;testis;skin; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skin; 0.12211 . 0.839664339 88.29912715 1109.51668 6.36763 ODF3L2 0.00314258776622615 0.59642381131668 0.400433600917094 outer dense fiber of sperm tails 3-like 2 . . . lung;testis; . 0.10249 0.10690 . . 1099.14153 6.34460 ODF4 0.000650823794005864 0.498151182043221 0.501197994162773 outer dense fiber of sperm tails 4 FUNCTION: Component of the outer dense fibers (ODF) of spermatozoa which could be involved in sperm tail structure, sperm movement and general organization of cellular cytoskeleton. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis and sperm; especially localized to sperm tail (at protein level). {ECO:0000269|PubMed:12728016}.; unclassifiable (Anatomical System);testis;stomach; . 0.11716 0.08420 0.661468037 84.4420854 526.20221 4.68176 OED . . . Oregon eye disease . . . . . . . . . . . OFC1 . . . orofacial cleft 1 . . . . . . . . . . . OFC2 . . . orofacial cleft 2 . . . . . . . . . . . OFC3 . . . orofacial cleft 3 . . . . . . . . . . . OFCC1 . . . orofacial cleft 1 candidate 1 . DISEASE: Note=A chromosomal aberration involving OFCC1 is found in patients with orofacial cleft. {ECO:0000269|PubMed:15218257}.; . . . 0.04418 . . . 2022.19175 8.27431 OFD1 0.982887661849247 0.0171123198200509 1.83307022668329e-08 oral-facial-digital syndrome 1 FUNCTION: Component of the centrioles controlling mother and daughter centrioles length. Recruits to the centriole IFT88 and centriole distal appendage-specific proteins including CEP164. Involved in the biogenesis of the cilium, a centriole-associated function. The cilium is a cell surface projection found in many vertebrate cells required to transduce signals important for development and tissue homeostasis. Plays an important role in development by regulating Wnt signaling and the specification of the left-right axis. Only OFD1 localized at the centriolar satellites is removed by autophagy, which is an important step in the ciliogenesis regulation (By similarity). {ECO:0000250}.; DISEASE: Simpson-Golabi-Behmel syndrome 2 (SGBS2) [MIM:300209]: A severe variant of Simpson-Golabi-Behmel syndrome, a condition characterized by pre- and postnatal overgrowth (gigantism), facial dysmorphism and a variety of inconstant visceral and skeletal malformations. {ECO:0000269|PubMed:16783569}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Joubert syndrome 10 (JBTS10) [MIM:300804]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. {ECO:0000269|PubMed:19800048}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa 23 (RP23) [MIM:300424]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:22619378}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Expressed in 9 and 14 weeks old embryos in metanephric mesenchyme, oral mucosa, lung, heart, nasal and cranial cartilage, and brain. Expressed in metanephros, brain, tongue, and limb. {ECO:0000269|PubMed:12595504}.; unclassifiable (Anatomical System);ovary;adrenal cortex;blood;parathyroid;skin;skeletal muscle;bile duct;lung;cochlea;adrenal gland;thyroid;pituitary gland;testis;kidney;brain;pineal gland;stomach; white blood cells; 0.11030 0.17799 -0.176292081 40.56381222 82.1386 1.92266 OFD1P1Y . . . OFD1 pseudogene 1, Y-linked . . . . . . . . . . . OFD1P2Y . . . OFD1 pseudogene 2, Y-linked . . . . . . . . . . . OFD1P3Y . . . OFD1 pseudogene 3, Y-linked . . . . . . . . . . . OFD1P4Y . . . OFD1 pseudogene 4, Y-linked . . . . . . . . . . . OFD1P5Y . . . OFD1 pseudogene 5, Y-linked . . . . . . . . . . . OFD1P6Y . . . OFD1 pseudogene 6, Y-linked . . . . . . . . . . . OFD1P7Y . . . OFD1 pseudogene 7, Y-linked . . . . . . . . . . . OFD1P8Y . . . OFD1 pseudogene 8, Y-linked . . . . . . . . . . . OFD1P9Y . . . OFD1 pseudogene 9, Y-linked . . . . . . . . . . . OFD1P10Y . . . OFD1 pseudogene 10, Y-linked . . . . . . . . . . . OFD1P11Y . . . OFD1 pseudogene 11, Y-linked . . . . . . . . . . . OFD1P12Y . . . OFD1 pseudogene 12, Y-linked . . . . . . . . . . . OFD1P13Y . . . OFD1 pseudogene 13, Y-linked . . . . . . . . . . . OFD1P14Y . . . OFD1 pseudogene 14, Y-linked . . . . . . . . . . . OFD1P15Y . . . OFD1 pseudogene 15, Y-linked . . . . . . . . . . . OFD1P16Y . . . OFD1 pseudogene 16, Y-linked . . . . . . . . . . . OFD1P17 . . . OFD1 pseudogene 17 . . . . . . . . . . . OFD1P18Y . . . OFD1 pseudogene 18, Y-linked . . . . . . . . . . . OGDH 0.993695121200126 0.00630487847910136 3.20772784356781e-10 oxoglutarate dehydrogenase FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).; . . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;thyroid;iris;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;tongue;urinary;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;cerebellum; skeletal muscle; 0.54935 0.63558 -0.484940685 22.75300778 342.2782 3.92270 OGDHL 3.46920930995895e-05 0.999448323950038 0.00051698395686286 oxoglutarate dehydrogenase-like . . . . . 0.38269 0.15417 -0.542003971 20.02830856 835.83729 5.66148 OGFOD1 1.29448940600909e-08 0.562911552780545 0.437088434274561 2-oxoglutarate and iron dependent oxygenase domain containing 1 FUNCTION: Prolyl 3-hydroxylase that catalyzes 3-hydroxylation of 'Pro-62' of small ribosomal subunit RPS23, thereby regulating protein translation termination efficiency. Involved in stress granule formation. {ECO:0000269|PubMed:20154146, ECO:0000269|PubMed:24550447, ECO:0000269|PubMed:24550462}.; . . myocardium;lymphoreticular;medulla oblongata;ovary;skin;bone marrow;prostate;frontal lobe;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;spinal cord;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;uterus;whole body;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;muscle;bile duct;pancreas;lung;pia mater;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; dorsal root ganglion;globus pallidus;atrioventricular node;parietal lobe; 0.05254 0.08979 -0.754958418 13.57631517 565.27472 4.82911 OGFOD1P1 . . . 2-oxoglutarate and iron dependent oxygenase domain containing 1 pseudogene 1 . . . . . . . . . . . OGFOD2 3.80505928088838e-07 0.199287431273479 0.800712188220593 2-oxoglutarate and iron dependent oxygenase domain containing 2 . . . medulla oblongata;ovary;parathyroid;fovea centralis;choroid;retina;prostate;optic nerve;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;urinary;lens;breast;lung;adrenal gland;placenta;visual apparatus;macula lutea;liver;spleen;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13328 0.10117 -0.44448505 24.46331682 86.22985 1.98288 OGFOD3 0.000595568731470111 0.900749959568053 0.0986544717004766 2-oxoglutarate and iron dependent oxygenase domain containing 3 . . . . . . . 0.823072022 88.03963199 1655.19196 7.52123 OGFR 0.0134181696647606 0.979748621321965 0.00683320901327414 opioid growth factor receptor FUNCTION: Receptor for opioid growth factor (OGF), also known as Met-enkephalin. Seems to be involved in growth regulation.; . TISSUE SPECIFICITY: Highly expressed in the heart and liver, moderately in skeletal muscle and kidney and to a lesser extent in brain and pancreas. Expressed in fetal tissues including liver and kidney.; ovary;salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;iris;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.13141 0.11230 1.047190339 91.34229771 572.15443 4.85552 OGFR-AS1 . . . OGFR antisense RNA 1 . . . . . . . . . . . OGFRL1 0.000150358853454911 0.868156691416164 0.131692949730381 opioid growth factor receptor-like 1 . . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16192744}.; . . 0.10678 0.07446 -0.383807564 27.41802312 2205.74516 8.64651 OGFRP1 . . . opioid growth factor receptor pseudogene 1 . . . . . . . . . . . OGG1 7.80168038151753e-08 0.472215070905161 0.527784851078036 8-oxoguanine DNA glycosylase FUNCTION: DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N- methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta- lyase activity that nicks DNA 3' to the lesion.; . TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;lens;breast;lung;nasopharynx;placenta;macula lutea;hippocampus;visual apparatus;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.26466 0.46593 0.711016566 85.72776598 216.52388 3.18012 OGN 0.00751075016804017 0.924958795609399 0.067530454222561 osteoglycin FUNCTION: Induces bone formation in conjunction with TGF-beta-1 or TGF-beta-2.; . TISSUE SPECIFICITY: Bone.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;pituitary gland;testis;brain;artery;unclassifiable (Anatomical System);heart;cartilage;pineal body;lens;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; uterus;superior cervical ganglion;olfactory bulb;ciliary ganglion;atrioventricular node; 0.47942 . -0.427900189 25.14744043 11.70696 0.42493 OGT 0.999947206587498 5.27934043286238e-05 8.17291341794328e-12 O-linked N-acetylglucosamine (GlcNAc) transferase FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta- linked N-acetylglucosamine (O-GlcNAc). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling. Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity (PubMed:22923583). Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich transcription start sites of active genes via its interaction with TET proteins (TET1, TET2 or TET3) (PubMed:22121020, PubMed:23353889). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:20018852). O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex (PubMed:24474760). Regulates circadian oscillation of the clock genes and glucose homeostasis in the liver. Stabilizes clock proteins ARNTL/BMAL1 and CLOCK through O-glycosylation, which prevents their ubiquitination and subsequent degradation. Promotes the CLOCK-ARNTL/BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2 and CRY1/2 (PubMed:12150998, PubMed:18288188, PubMed:19377461, PubMed:19451179, PubMed:20018868, PubMed:20200153, PubMed:21285374, PubMed:15361863). {ECO:0000269|PubMed:12150998, ECO:0000269|PubMed:15361863, ECO:0000269|PubMed:18288188, ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:20018868, ECO:0000269|PubMed:20200153, ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:22121020, ECO:0000269|PubMed:22923583, ECO:0000269|PubMed:23353889, ECO:0000269|PubMed:24474760}.; DISEASE: Note=Regulation of OGT activity and altered O- GlcNAcylations are implicated in diabetes and Alzheimer disease. O-GlcNAcylation of AKT1 affects insulin signaling and, possibly diabetes. Reduced O-GlcNAcylations and resulting increased phosphorylations of MAPT/TAU are observed in Alzheimer disease (AD) brain cerebrum.; TISSUE SPECIFICITY: Highly expressed in pancreas and to a lesser extent in skeletal muscle, heart, brain and placenta. Present in trace amounts in lung and liver. {ECO:0000269|PubMed:9083068}.; . . 0.35867 0.32553 -0.405853867 26.23260203 6.35942 0.23824 OIP5 1.53697409243863e-08 0.03248538411218 0.967514600518079 Opa interacting protein 5 FUNCTION: Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. {ECO:0000269|PubMed:17199038}.; . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;pharynx;blood;bile duct;breast;lung;placenta;visual apparatus;hippocampus;liver;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.49278 0.09047 0.150760231 64.51403633 228.44848 3.26499 OIP5-AS1 . . . OIP5 antisense RNA 1 . . . . . . . . . . . OIT3 1.03779931784183e-09 0.297727472523604 0.702272526438597 oncoprotein induced transcript 3 FUNCTION: May be involved in hepatocellular function and development. {ECO:0000269|PubMed:12939600}.; . TISSUE SPECIFICITY: Liver-specific. Expressed only in the hepatocytes. Down-regulated in hepatocellular carcinoma (HCC) and HCC cell lines. {ECO:0000269|PubMed:12939600}.; unclassifiable (Anatomical System);pancreas;whole body;heart;placenta;liver;spleen;kidney;brain; . 0.31381 0.10522 -0.997481928 8.47487615 77.72101 1.85712 OLA1 0.0436206997457236 0.950605710878449 0.00577358937582728 Obg-like ATPase 1 FUNCTION: Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP. {ECO:0000255|HAMAP- Rule:MF_03167}.; . TISSUE SPECIFICITY: Expressed in all tissues tested but its expression is more abundant in testis, liver, lung, and brain. Overexpressed in several malignancies, including cancers of the colon, rectum, ovary, lung, stomach, and uterus.; ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;vein;uterus;whole body;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;mesenchyma;adrenal gland;placenta;hippocampus;head and neck;kidney;aorta;stomach;thymus; amygdala;occipital lobe;medulla oblongata;subthalamic nucleus;prefrontal cortex;globus pallidus;tumor;parietal lobe;cingulate cortex; 0.52914 0.25278 -0.227663163 37.11370606 829.8618 5.64597 OLA1P1 . . . Obg-like ATPase 1 pseudogene 1 . . . . . . . . . . . OLA1P2 . . . Obg-like ATPase 1 pseudogene 2 . . . . . . . . . . . OLA1P3 . . . Obg-like ATPase 1 pseudogene 3 . . . . . . . . . . . OLAH 0.00132846389180959 0.860733367438326 0.137938168669865 oleoyl-ACP hydrolase FUNCTION: In fatty acid biosynthesis chain termination and release of the free fatty acid product is achieved by hydrolysis of the thio ester by a thioesterase I, a component of the fatty acid synthetase complex. The chain length of the released fatty acid is usually C16. However, in the mammary glands of non-ruminant mammals, and in the uropygial gland of certain waterfowl there exists a second thioesterase which releases medium-chain length fatty acids (C8 to C2) (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 2 is up-regulated in bone marrow- derived mononuclear cells of rheumatoid arthritis patients. {ECO:0000269|PubMed:17082220}.; . . 0.09576 0.06903 0.461228372 78.46190139 95.67275 2.11420 OLFM1 0.935993730569587 0.0639473938490701 5.88755813426184e-05 olfactomedin 1 FUNCTION: Contributes to the regulation of axonal growth in the embryonic and adult central nervous system by inhibiting interactions between RTN4R and LINGO1. Inhibits RTN4R-mediated axon growth cone collapse (By similarity). May play an important role in regulating the production of neural crest cells by the neural tube (By similarity). May be required for normal responses to olfactory stimuli (By similarity). {ECO:0000250|UniProtKB:O88998, ECO:0000250|UniProtKB:Q9IAK4}.; . . sympathetic chain;colon;substantia nigra;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;adrenal cortex;lens;breast;pancreas;lung;macula lutea;visual apparatus;hippocampus;head and neck;cervix;kidney;stomach;aorta; whole brain;amygdala;dorsal root ganglion;occipital lobe;superior cervical ganglion;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;atrioventricular node;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.74779 0.25659 -0.60427181 17.74593064 14.88235 0.53605 OLFM2 0.964592021100157 0.0353422463126433 6.57325872001542e-05 olfactomedin 2 FUNCTION: Involved in transforming growth factor beta (TGF-beta)- induced smooth muscle differentiation. TGF-beta induces expression and nuclear translocation of OLFM2 where it binds to SRF, causing its dissociation from the transcriptional repressor HEY2/HERP1 and facilitating binding of SRF to target genes (PubMed:25298399). Plays a role in AMPAR complex organization (By similarity). {ECO:0000250|UniProtKB:Q8BM13, ECO:0000269|PubMed:25298399}.; . TISSUE SPECIFICITY: Expressed in aortic smooth muscle (at protein level). {ECO:0000269|PubMed:25298399}.; unclassifiable (Anatomical System);medulla oblongata;cartilage;tongue;hypothalamus;skin;skeletal muscle;retina;prostate;lung;bone;placenta;visual apparatus;liver;testis;head and neck;spleen;brain;bladder;mammary gland;stomach;cerebellum;thymus; superior cervical ganglion;medulla oblongata; 0.17007 0.12771 -0.003562597 53.72729417 3718.37392 11.91299 OLFM3 6.96790168770402e-05 0.909807971999372 0.0901223489837513 olfactomedin 3 . . TISSUE SPECIFICITY: In the eye, expressed in trabecular meshwork and neural retina; in non-ocular tissues, expressed in brain and lung. {ECO:0000269|PubMed:12019210}.; unclassifiable (Anatomical System);hypothalamus;bone;hippocampus;brain;skeletal muscle; whole brain;amygdala;thalamus;superior cervical ganglion;occipital lobe;subthalamic nucleus;hypothalamus;prefrontal cortex;globus pallidus;atrioventricular node;cingulate cortex; 0.25872 0.12209 -0.758599262 13.32861524 134.81144 2.52506 OLFM4 2.41040640655975e-06 0.491169665025947 0.508827924567646 olfactomedin 4 FUNCTION: May promote proliferation of pancreatic cancer cells by favoring the transition from the S to G2/M phase. In myeloid leukemic cell lines, inhibits cell growth and induces cell differentiation and apoptosis. May play a role in the inhibition of EIF4EBP1 phosphorylation/deactivation. Facilitates cell adhesion, most probably through interaction with cell surface lectins and cadherin. {ECO:0000269|PubMed:16566923, ECO:0000269|PubMed:17270022, ECO:0000269|PubMed:20724538}.; . TISSUE SPECIFICITY: Expressed during myeloid lineage development. Much higher expression in bone marrow neutrophils than in peripheral blood neutrophils (at protein level). Strongly expressed in the prostate, small intestine and colon and moderately expressed in the bone marrow and stomach. Overexpressed in some pancreatic cancer tissues. {ECO:0000269|PubMed:11867215, ECO:0000269|PubMed:16566923, ECO:0000269|PubMed:17270022, ECO:0000269|PubMed:20724538}.; unclassifiable (Anatomical System);heart;small intestine;islets of Langerhans;colon;skin;skeletal muscle;breast;uterus;pancreas;prostate;lung;endometrium;larynx;nasopharynx;head and neck;kidney;brain;mammary gland;stomach; pancreas;prostate;testis - seminiferous tubule;salivary gland;beta cell islets;bone marrow; 0.31239 0.10441 0.532823122 80.96249115 120.77265 2.39478 OLFM5P . . . olfactomedin family member 5, pseudogene . . . . . . . . . . . OLFML1 0.000497436648326104 0.879096360891188 0.120406202460486 olfactomedin like 1 . . TISSUE SPECIFICITY: Mainly expressed in the small intestine, liver, lung and heart. {ECO:0000269|PubMed:18708057}.; unclassifiable (Anatomical System);heart;tongue;colon;skin;skeletal muscle;uterus;lung;endometrium;synovium;thyroid;placenta;visual apparatus;hypopharynx;liver;testis;head and neck;spleen;spinal ganglion;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;fetal lung;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.30532 . 1.153790856 92.55720689 1643.14245 7.48997 OLFML2A 1.74427014386868e-05 0.877871093665085 0.122111463633476 olfactomedin like 2A . . TISSUE SPECIFICITY: In the kidney expressed only by podocytes, wherein they localize to major processes. {ECO:0000269|PubMed:22913984}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;lung;trabecular meshwork;placenta;macula lutea;liver;spleen;kidney;stomach; dorsal root ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13462 . -0.727458245 14.19556499 423.79429 4.29910 OLFML2B 3.02036832631922e-06 0.983453240451246 0.0165437391804281 olfactomedin like 2B . . . smooth muscle;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;nervous;lens;pancreas;lung;placenta;macula lutea;visual apparatus;head and neck;kidney;stomach; testis - interstitial;superior cervical ganglion;testis; 0.28100 . 1.229050169 93.25902335 819.22455 5.62241 OLFML3 0.000588286969051829 0.89937273799367 0.100038975037278 olfactomedin like 3 FUNCTION: Secreted scaffold protein that plays an essential role in dorsoventral patterning during early development. Stabilizes axial formation by restricting chordin (CHRD) activity on the dorsal side. Acts by facilitating the association between the tolloid proteases and their substrate chordin (CHRD), leading to enhance chordin (CHRD) degradation (By similarity). May have matrix-related function involved in placental and embryonic development, or play a similar role in other physiological processes. {ECO:0000250, ECO:0000269|PubMed:15280020}.; . TISSUE SPECIFICITY: Abundant in placenta, moderate in liver and heart, whereas fairly weak in other tissues examined. On term placenta, mainly localized extracellularly surrounding the syncytiotrophoblastic cells and very rarely expressed in the maternal decidua layer. {ECO:0000269|PubMed:15280020}.; medulla oblongata;ovary;colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.66863 0.10981 0.064394823 58.84642604 80.4714 1.89543 OLIG1 0.119038216281687 0.607345449616053 0.273616334102259 oligodendrocyte transcription factor 1 FUNCTION: Promotes formation and maturation of oligodendrocytes, especially within the brain. Cooperates with OLIG2 to establish the pMN domain of the embryonic neural tube (By similarity). {ECO:0000250, ECO:0000269|PubMed:10719889}.; . TISSUE SPECIFICITY: Expressed in the brain, in oligodendrocytes. Strongly expressed in oligodendrogliomas, while expression is weak to moderate in astrocytomas. Expression in glioblastomas is highly variable. {ECO:0000269|PubMed:11526205}.; unclassifiable (Anatomical System);optic nerve;frontal lobe;cartilage;hypothalamus;kidney;brain; amygdala;dorsal root ganglion;medulla oblongata;superior cervical ganglion;caudate nucleus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.29247 0.20085 . . 90.24889 2.04395 OLIG2 0.203764106544774 0.648098779773518 0.148137113681708 oligodendrocyte lineage transcription factor 2 FUNCTION: Required for oligodendrocyte and motor neuron specification in the spinal cord, as well as for the development of somatic motor neurons in the hindbrain. Cooperates with OLIG1 to establish the pMN domain of the embryonic neural tube. Antagonist of V2 interneuron and of NKX2-2-induced V3 interneuron development (By similarity). {ECO:0000250}.; DISEASE: Note=A chromosomal aberration involving OLIG2 may be a cause of a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(14;21)(q11.2;q22) with TCRA. {ECO:0000269|PubMed:10737801}.; TISSUE SPECIFICITY: Expressed in the brain, in oligodendrocytes. Strongly expressed in oligodendrogliomas, while expression is weak to moderate in astrocytomas. Expression in glioblastomas highly variable. {ECO:0000269|PubMed:11498220, ECO:0000269|PubMed:11526205}.; unclassifiable (Anatomical System);lung;frontal lobe;placenta;testis;brain;pineal gland; amygdala;whole brain;occipital lobe;superior cervical ganglion;medulla oblongata;thalamus;hypothalamus;spinal cord;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.57578 0.35982 . . 39.23901 1.16190 OLIG3 0.672757859435387 0.306055148219542 0.0211869923450703 oligodendrocyte transcription factor 3 FUNCTION: May determine the distinct specification program of class A neurons in the dorsal part of the spinal cord and suppress specification of class B neurons.; . . . . 0.53116 0.11146 -0.293801652 32.93819297 263.50017 3.48325 OLMALINC . . . oligodendrocyte maturation-associated long intergenic non-coding RNA . . . . . . . . . . . OLR1 0.297321524092708 0.698448127138837 0.00423034876845516 oxidized low density lipoprotein receptor 1 FUNCTION: Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro- oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro- atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram- positive bacteria. {ECO:0000269|PubMed:11821063, ECO:0000269|PubMed:12354387, ECO:0000269|PubMed:9052782}.; DISEASE: Note=Independent association genetic studies have implicated OLR1 gene variants in myocardial infarction susceptibility.; DISEASE: Note=OLR1 may be involved in Alzheimer disease (AD). Involvement in AD is however unclear: according to some authors (PubMed:12354387, PubMed:12810610 and PubMed:15976314), variations in OLR1 modify the risk of AD, while according to other (PubMed:15000751 and PubMed:15060104) they do not. {ECO:0000269|PubMed:12384789, ECO:0000269|PubMed:12807963, ECO:0000269|PubMed:15860461}.; TISSUE SPECIFICITY: Expressed at high level in endothelial cells and vascular-rich organs such as placenta, lung, liver and brain, aortic intima, bone marrow, spinal cord and substantia nigra. Also expressed at the surface of dendritic cells. Widely expressed at intermediate and low level. {ECO:0000269|PubMed:12354387, ECO:0000269|PubMed:9052782, ECO:0000269|PubMed:9828121}.; unclassifiable (Anatomical System);ovary;cartilage;islets of Langerhans;hypothalamus;adrenal cortex;colon;parathyroid;blood;breast;uterus;lung;adrenal gland;nasopharynx;placenta;thyroid;liver;testis;spleen;cervix;kidney;brain;pineal gland;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10124 0.34693 -0.117432389 44.89266336 721.79422 5.33246 OMA1 3.51132911001781e-09 0.313920966861236 0.686079029627435 OMA1 zinc metallopeptidase FUNCTION: Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of OPA1 at S1 position, leading to OPA1 inactivation and negative regulation of mitochondrial fusion. May also cleave UQCC3 under these conditions. Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions. {ECO:0000250|UniProtKB:Q9D8H7, ECO:0000269|PubMed:20038677}.; . TISSUE SPECIFICITY: Widely expressed, with strong expression in the heart, skeletal muscle, kidney and liver. {ECO:0000269|PubMed:12886954}.; unclassifiable (Anatomical System);lymph node;sympathetic chain;blood;skin;bone marrow;prostate;lung;placenta;liver;testis;spleen;germinal center;kidney;artery;aorta; superior cervical ganglion;ciliary ganglion; 0.10525 0.09087 1.243805243 93.41825902 1554.83717 7.30581 OMD 0.00235083281027152 0.769211649806646 0.228437517383083 osteomodulin FUNCTION: May be implicated in biomineralization processes. Has a function in binding of osteoblasts via the alpha(V)beta(3)- integrin (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Bone specific.; . . 0.09031 0.17674 0.328949044 73.41354093 373.77779 4.07833 OMG 0.863213191754022 0.134777581181454 0.00200922706452406 oligodendrocyte myelin glycoprotein FUNCTION: Cell adhesion molecule contributing to the interactive process required for myelination in the central nervous system.; . TISSUE SPECIFICITY: Oligodendrocytes and myelin of the central nervous system.; unclassifiable (Anatomical System);optic nerve;whole body;frontal lobe;hypothalamus;macula lutea;hippocampus;amniotic fluid;fovea centralis;choroid;lens;brain;retina; whole brain;amygdala;thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.39406 0.19007 0.12689526 63.00424628 324.94171 3.83215 OMP 0.045566820595818 0.672601756707073 0.281831422697109 olfactory marker protein FUNCTION: May act as a modulator of the olfactory signal- transduction cascade.; . TISSUE SPECIFICITY: Uniquely associated with mature olfactory receptor neurons.; . . . . 0.306902668 72.38145789 424.24013 4.30268 ONECUT1 0.209132853423149 0.749696277278877 0.041170869297974 one cut homeobox 1 FUNCTION: Transcriptional activator. Binds the consensus sequence 5'-DHWATTGAYTWWD-3' on a variety of gene promoters such as those of HNF3B and TTR. Important for liver genes transcription.; . TISSUE SPECIFICITY: Highly expressed in liver; lower expression in testis and skin.; liver;spleen; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.42280 0.17114 -0.26993514 34.59542345 132.01687 2.50169 ONECUT2 0.903998414160395 0.0951954149676696 0.000806170871935834 one cut homeobox 2 FUNCTION: Transcriptional activator. Activates the transcription of a number of liver genes such as HNF3B.; . . lung;islets of Langerhans; subthalamic nucleus;trigeminal ganglion; 0.11843 0.18435 -0.60427181 17.74593064 16.33351 0.57897 ONECUT3 . . . one cut homeobox 3 FUNCTION: Transcriptional activator. Binds the consensus DNA sequence 5'-DHWATTGAYTWWD-3' on a variety of gene promoters such as those of HNF3B and TTR (By similarity). {ECO:0000250}.; . . . . 0.08086 . . . 9.33211 0.34246 OOEP 0.230723598205906 0.735184883425643 0.0340915183684508 oocyte expressed protein FUNCTION: As a member of the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions. {ECO:0000250}.; . . . . 0.12865 0.09415 0.459411326 78.28497287 162.24685 2.78234 OOEP-AS1 . . . OOEP antisense RNA 1 . . . . . . . . . . . OOSP1 . . . oocyte secreted protein 1, pseudogene FUNCTION: May be involved in cell differentiation. {ECO:0000250}.; . . . . . . . . 14.90307 0.53655 OOSP1P1 . . . oocyte secreted protein 1 pseudogene 1 . . . . . . . . . . . OOSP1P2 . . . oocyte secreted protein 1 pseudogene 2 . . . . . . . . . . . OOSP2 . . . oocyte secreted protein 2 . . . . . 0.07049 0.09177 0.080983847 59.76055674 39.74924 1.17148 OPA1 0.994351455893758 0.00564854410421099 2.03129392027805e-12 OPA1, mitochondrial dynamin like GTPase FUNCTION: Dynamin-related GTPase required for mitochondrial fusion and regulation of apoptosis. May form a diffusion barrier for proteins stored in mitochondrial cristae. Proteolytic processing in response to intrinsic apoptotic signals may lead to disassembly of OPA1 oligomers and release of the caspase activator cytochrome C (CYCS) into the mitochondrial intermembrane space. May also play a role in mitochondrial genome maintenance. {ECO:0000250|UniProtKB:P58281, ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:18158317}.; DISEASE: Optic atrophy 1 (OPA1) [MIM:165500]: A condition that features progressive visual loss in association with optic atrophy. Atrophy of the optic disk indicates a deficiency in the number of nerve fibers which arise in the retina and converge to form the optic disk, optic nerve, optic chiasm and optic tracts. OPA1 is characterized by an insidious onset of visual impairment in early childhood with moderate to severe loss of visual acuity, temporal optic disk pallor, color vision deficits, and centrocecal scotoma of variable density. {ECO:0000269|PubMed:11017079, ECO:0000269|PubMed:11017080, ECO:0000269|PubMed:11440988, ECO:0000269|PubMed:11440989, ECO:0000269|PubMed:11810270, ECO:0000269|PubMed:12036970, ECO:0000269|PubMed:12566046, ECO:0000269|PubMed:14961560, ECO:0000269|PubMed:15948788, ECO:0000269|PubMed:16513463, ECO:0000269|PubMed:16617242, ECO:0000269|PubMed:18204809, ECO:0000269|PubMed:18360822, ECO:0000269|PubMed:19319978, ECO:0000269|PubMed:19325939, ECO:0000269|PubMed:19969356, ECO:0000269|PubMed:22382025, ECO:0000269|PubMed:22857269, ECO:0000269|PubMed:23401657}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dominant optic atrophy plus syndrome (DOA+) [MIM:125250]: A neurologic disorder characterized most commonly by an insidious onset of visual loss and sensorineural hearing loss in childhood with variable presentation of other clinical manifestations including progressive external ophthalmoplegia, muscle cramps, hyperreflexia, and ataxia. There appears to be a wide range of intermediate phenotypes. {ECO:0000269|PubMed:15531309, ECO:0000269|PubMed:16240368, ECO:0000269|PubMed:18065439, ECO:0000269|PubMed:18158317, ECO:0000269|PubMed:18195150, ECO:0000269|PubMed:23387428}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in retina. Also expressed in brain, testis, heart and skeletal muscle. Isoform 1 expressed in retina, skeletal muscle, heart, lung, ovary, colon, thyroid gland, leukocytes and fetal brain. Isoform 2 expressed in colon, liver, kidney, thyroid gland and leukocytes. Low levels of all isoforms expressed in a variety of tissues. {ECO:0000269|PubMed:11017079, ECO:0000269|PubMed:11017080, ECO:0000269|PubMed:11810270}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;amniotic fluid;germinal center;brain;amygdala;heart;cartilage;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; amygdala;dorsal root ganglion;superior cervical ganglion;occipital lobe;medulla oblongata;pons;caudate nucleus;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.38942 0.34500 -0.573127851 18.96083982 4690.70964 13.80167 OPA1-AS1 . . . OPA1 antisense RNA 1 . . . . . . . . . . . OPA2 . . . optic atrophy 2 (obscure) . . . . . . . . . . . OPA3 0.00412066593618986 0.861427420119089 0.134451913944722 optic atrophy 3 (autosomal recessive, with chorea and spastic paraplegia) FUNCTION: May play some role in mitochondrial processes.; DISEASE: Optic atrophy 3 (OPA3) [MIM:165300]: A condition that features progressive visual loss in association with optic atrophy. Atrophy of the optic disk indicates a deficiency in the number of nerve fibers which arise in the retina and converge to form the optic disk, optic nerve, optic chiasm and optic tracts. OPA3 is associated with cataract and a neurologic disorder characterized by extrapyramidal signs and ataxia. {ECO:0000269|PubMed:15342707}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Most prominent expression in skeletal muscle and kidney. {ECO:0000269|PubMed:11668429}.; unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;colon;fovea centralis;choroid;lens;skin;retina;uterus;prostate;pancreas;optic nerve;lung;placenta;macula lutea;visual apparatus;liver;testis;spleen;kidney;germinal center;brain; superior cervical ganglion;medulla oblongata;globus pallidus;skeletal muscle; 0.13937 0.15819 0.371224249 75.12384996 20.97956 0.70981 OPA4 . . . optic atrophy 4 (autosomal dominant) . . . . . . . . . . . OPA5 . . . optic atrophy 5 (autosomal dominant) . . . . . . . . . . . OPA6 . . . optic atrophy 6 (autosomal recessive) . . . . . . . . . . . OPA8 . . . optic atrophy 8 (autosomal dominant) . . . . . . . . . . . OPALIN 0.0606427546253694 0.868789073961413 0.0705681714132178 oligodendrocytic myelin paranodal and inner loop protein . . TISSUE SPECIFICITY: Brain specific. {ECO:0000269|PubMed:11814680}.; . . 0.06444 0.06676 0.415317661 76.81056853 70.31485 1.74385 OPCML 0.578155981232135 0.419519452815074 0.0023245659527909 opioid binding protein/cell adhesion molecule-like FUNCTION: Binds opioids in the presence of acidic lipids; probably involved in cell contact.; DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease. {ECO:0000269|PubMed:12819783}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);amygdala;developmental;blood;parathyroid;fovea centralis;choroid;lens;bone marrow;retina;optic nerve;ganglion;frontal lobe;macula lutea;testis;brain;cerebellum; . 0.58428 0.18409 -0.359940251 28.93371078 18.89153 0.65266 OPCML-IT1 . . . OPCML intronic transcript 1 . . . . . . . . . . . OPCML-IT2 . . . OPCML intronic transcript 2 . . . . . . . . . . . OPEM . . . ophthalmoplegia, external, with myopia . . . . . . . . . . . OPHN1 0.999448414550568 0.000551582967021653 2.4824104842069e-09 oligophrenin 1 FUNCTION: Stimulates GTP hydrolysis of members of the Rho family. Its action on RHOA activity and signaling is implicated in growth and stabilization of dendritic spines, and therefore in synaptic function. Critical for the stabilization of AMPA receptors at postsynaptic sites. Critical for the regulation of synaptic vesicle endocytosis at presynaptic terminals. Required for the localization of NR1D1 to dendrites, can suppress its repressor activity and protect it from proteasomal degradation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain.; unclassifiable (Anatomical System);lymph node;heart;tongue;colon;blood;parathyroid;skeletal muscle;bone marrow;uterus;breast;lung;frontal lobe;head and neck;brain;mammary gland; . 0.15537 0.19705 0.50895761 80.20169851 175.03264 2.87649 OPLAH 2.99003379437065e-11 0.887670230594218 0.112329769375881 5-oxoprolinase (ATP-hydrolysing) FUNCTION: Catalyzes the cleavage of 5-oxo-L-proline to form L- glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.; DISEASE: 5-oxoprolinase deficiency (OPLAHD) [MIM:260005]: A disorder characterized by calcium oxalate/carbonate urolithiasis, and excessive urinary 5-oxo-L-proline. Affected individuals have recurrent episodes of vomiting, diarrhea, and abdominal pain. {ECO:0000269|PubMed:21651516}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.11816 0.18621 . . 2315.28938 8.91132 OPN1LW 0.907796474628102 0.0914763234501897 0.000727201921708029 opsin 1 (cone pigments), long-wave-sensitive FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.; DISEASE: Colorblindness, partial, protan series (CBP) [MIM:303900]: A color vision defect characterized by a dichromasy in which red and green are confused, with loss of luminance and shift of brightness and hue curves toward the short wave end of the spectrum. Dichromasy is due to the use of only two types of photoreceptors, blue plus red in deuteranopia and blue plus green in protanopia. {ECO:0000269|PubMed:12051694}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Blue cone monochromacy (BCM) [MIM:303700]: A rare X- linked congenital stationary cone dysfunction syndrome characterized by the absence of functional long wavelength- sensitive and medium wavelength-sensitive cones in the retina. Color discrimination is severely impaired from birth, and vision is derived from the remaining preserved blue (S) cones and rod photoreceptors. BCM typically presents with reduced visual acuity, pendular nystagmus, and photophobia. Patients often have myopia. {ECO:0000269|PubMed:8213841, ECO:0000269|PubMed:8666378}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: The three color pigments are found in the cone photoreceptor cells.; . . 0.25203 . 0.839664339 88.29912715 352.91669 3.97896 OPN1MW 0.502014146694304 0.425860571792497 0.072125281513199 opsin 1 (cone pigments), medium-wave-sensitive FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. {ECO:0000305|PubMed:12051694, ECO:0000305|PubMed:1302020, ECO:0000305|PubMed:2937147}.; DISEASE: Colorblindness, partial, deutan series (CBD) [MIM:303800]: A color vision defect characterized by a dichromasy in which red and green are confused, without loss of luminance or shift or shortening of the spectrum. Dichromasy is due to the use of only two types of photoreceptors, blue plus red in deuteranopia and blue plus green in protanopia. {ECO:0000269|PubMed:12051694, ECO:0000269|PubMed:1302020}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Blue cone monochromacy (BCM) [MIM:303700]: A rare X- linked congenital stationary cone dysfunction syndrome characterized by the absence of functional long wavelength- sensitive and medium wavelength-sensitive cones in the retina. Color discrimination is severely impaired from birth, and vision is derived from the remaining preserved blue (S) cones and rod photoreceptors. BCM typically presents with reduced visual acuity, pendular nystagmus, and photophobia. Patients often have myopia. {ECO:0000269|PubMed:8666378}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cone dystrophy 5 (COD5) [MIM:303700]: A X-linked cone dystrophy. Cone dystrophies are retinal dystrophies characterized by progressive degeneration of the cone photoreceptors with preservation of rod function, as indicated by electroretinogram. However, some rod involvement may be present in some cone dystrophies, particularly at late stage. Affected individuals suffer from photophobia, loss of visual acuity, color vision and central visual field. Another sign is the absence of macular lesions for many years. Cone dystrophies are distinguished from the cone-rod dystrophies in which some loss of peripheral vision also occurs. {ECO:0000269|PubMed:20579627}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: The three color pigments are found in the cone photoreceptor cells. {ECO:0000305|PubMed:2937147}.; . . 0.10272 0.14545 . . 5.57416 0.20739 OPN1MW2 0.574117353273909 0.380632029883726 0.0452506168423654 opsin 1 (cone pigments), medium-wave-sensitive 2 FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. {ECO:0000250|UniProtKB:P04001}.; . . . . . 0.14493 . . 4.80972 0.17536 OPN1MW3 . . . opsin 1 (cone pigments), medium-wave-sensitive 3 FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. {ECO:0000250|UniProtKB:P04001}.; . . . . . . . . . . OPN1SW 0.369090989256908 0.619466939914262 0.0114420708288299 opsin 1 (cone pigments), short-wave-sensitive FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.; DISEASE: Tritan color blindness (CBT) [MIM:190900]: A disorder of vision characterized by a selective deficiency of blue spectral sensitivity. {ECO:0000269|PubMed:1386496, ECO:0000269|PubMed:1531728}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: The three color pigments are found in the cone photoreceptor cells.; unclassifiable (Anatomical System);heart;cartilage;choroid;fovea centralis;lens;skin;retina;uterus;prostate;optic nerve;bone;macula lutea;stomach; superior cervical ganglion;caudate nucleus;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.10000 0.32832 -0.734731259 14.01863647 70.90056 1.75381 OPN3 0.846289039558313 0.15314002692004 0.000570933521646732 opsin 3 FUNCTION: May play a role in encephalic photoreception.; . TISSUE SPECIFICITY: Strongly expressed in brain. Highly expressed in the preoptic area and paraventricular nucleus of the hypothalamus. Shows highly patterned expression in other regions of the brain, being enriched in selected regions of the cerebral cortex, cerebellar Purkinje cells, a subset of striatal neurons, selected thalamic nuclei, and a subset of interneurons in the ventral horn of the spinal cord.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach; whole brain;superior cervical ganglion;placenta;cingulate cortex;parietal lobe; 0.18445 0.20063 0.15257911 64.60839821 559.13945 4.80286 OPN4 1.101892100262e-06 0.56137074338679 0.43862815472111 opsin 4 FUNCTION: Photoreceptor required for regulation of circadian rhythm. Contributes to pupillar reflex and other non-image forming responses to light. May be able to isomerize covalently bound all- trans retinal back to 11-cis retinal (By similarity). {ECO:0000250, ECO:0000269|PubMed:10632589, ECO:0000269|PubMed:15674244}.; . TISSUE SPECIFICITY: Eye. Expression is restricted within the ganglion and amacrine cell layers of the retina. {ECO:0000269|PubMed:10632589}.; unclassifiable (Anatomical System);retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09899 0.17920 0.270087468 70.69473933 356.90259 4.00177 OPN5 0.948752683071951 0.0512136975957582 3.36193322904072e-05 opsin 5 . . TISSUE SPECIFICITY: Detected in brain and retina and cell lines derived from neural retina. {ECO:0000269|PubMed:14623103}.; lung;testis; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.27804 0.15139 -0.560178693 19.30879925 27.90162 0.89600 OPRD1 0.109062189113339 0.776662874592307 0.114274936294355 opioid receptor, delta 1 FUNCTION: G-protein coupled receptor that functions as receptor for endogenous enkephalins and for a subset of other opioids. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain and in opiate-mediated analgesia. Plays a role in developing analgesic tolerance to morphine. {ECO:0000269|PubMed:22184124, ECO:0000269|PubMed:7808419, ECO:0000269|PubMed:8201839}.; . TISSUE SPECIFICITY: Detected in oocytes (at protein level). Detected in brain cortex, hypothalamus, hippocampus and olfactory bulb. Detected in oocytes. {ECO:0000269|PubMed:22417668, ECO:0000269|PubMed:7808419}.; ovary; trigeminal ganglion; 0.38858 0.34596 -0.139478553 43.29440906 296.04535 3.67407 OPRK1 0.0188155191797378 0.898090681253453 0.0830937995668089 opioid receptor, kappa 1 FUNCTION: G-protein coupled opioid receptor that functions as receptor for endogenous alpha-neoendorphins and dynorphins, but has low affinity for beta-endorphins. Also functions as receptor for various synthetic opioids and for the psychoactive diterpene salvinorin A. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain. Plays a role in mediating reduced physical activity upon treatment with synthetic opioids. Plays a role in the regulation of salivation in response to synthetic opioids. May play a role in arousal and regulation of autonomic and neuroendocrine functions. {ECO:0000269|PubMed:12004055, ECO:0000269|PubMed:22437504, ECO:0000269|PubMed:7624359, ECO:0000269|PubMed:8060324}.; . TISSUE SPECIFICITY: Detected in brain and placenta. {ECO:0000269|PubMed:7624359, ECO:0000269|PubMed:8060324}.; unclassifiable (Anatomical System);placenta; superior cervical ganglion;trigeminal ganglion; 0.14819 0.24365 -0.291981272 33.20358575 95.00702 2.10157 OPRL1 0.602075924384072 0.388911890648894 0.00901218496703404 opiate receptor-like 1 FUNCTION: G-protein coupled opioid receptor that functions as receptor for the endogenous neuropeptide nociceptin. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling via G proteins mediates inhibition of adenylate cyclase activity and calcium channel activity. Arrestins modulate signaling via G proteins and mediate the activation of alternative signaling pathways that lead to the activation of MAP kinases. Plays a role in modulating nociception and the perception of pain. Plays a role in the regulation of locomotor activity by the neuropeptide nociceptin. {ECO:0000269|PubMed:11238602, ECO:0000269|PubMed:12568343, ECO:0000269|PubMed:22596163, ECO:0000269|PubMed:23086955, ECO:0000269|PubMed:8137918}.; . TISSUE SPECIFICITY: Detected in blood leukocytes. {ECO:0000269|PubMed:7500847}.; breast;unclassifiable (Anatomical System);medulla oblongata;prostate;lymph node;lung;hypothalamus;placenta;testis;kidney;brain;peripheral nerve; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.10147 . -0.400392389 26.85185185 52.02575 1.42444 OPRM1 4.20778097354752e-05 0.844762544857138 0.155195377333126 opioid receptor, mu 1 FUNCTION: Receptor for endogenous opioids such as beta-endorphin and endomorphin. Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone. Agonist binding to the receptor induces coupling to an inactive GDP-bound heterotrimeric G-protein complex and subsequent exchange of GDP for GTP in the G-protein alpha subunit leading to dissociation of the G-protein complex with the free GTP-bound G-protein alpha and the G-protein beta- gamma dimer activating downstream cellular effectors. The agonist- and cell type-specific activity is predominantly coupled to pertussis toxin-sensitive G(i) and G(o) G alpha proteins, GNAI1, GNAI2, GNAI3 and GNAO1 isoforms Alpha-1 and Alpha-2, and to a lesser extend to pertussis toxin-insensitive G alpha proteins GNAZ and GNA15. They mediate an array of downstream cellular responses, including inhibition of adenylate cyclase activity and both N-type and L-type calcium channels, activation of inward rectifying potassium channels, mitogen-activated protein kinase (MAPK), phospholipase C (PLC), phosphoinositide/protein kinase (PKC), phosphoinositide 3-kinase (PI3K) and regulation of NF-kappa-B. Also couples to adenylate cyclase stimulatory G alpha proteins. The selective temporal coupling to G-proteins and subsequent signaling can be regulated by RGSZ proteins, such as RGS9, RGS17 and RGS4. Phosphorylation by members of the GPRK subfamily of Ser/Thr protein kinases and association with beta-arrestins is involved in short-term receptor desensitization. Beta-arrestins associate with the GPRK-phosphorylated receptor and uncouple it from the G-protein thus terminating signal transduction. The phosphorylated receptor is internalized through endocytosis via clathrin-coated pits which involves beta-arrestins. The activation of the ERK pathway occurs either in a G-protein-dependent or a beta-arrestin-dependent manner and is regulated by agonist- specific receptor phosphorylation. Acts as a class A G-protein coupled receptor (GPCR) which dissociates from beta-arrestin at or near the plasma membrane and undergoes rapid recycling. Receptor down-regulation pathways are varying with the agonist and occur dependent or independent of G-protein coupling. Endogenous ligands induce rapid desensitization, endocytosis and recycling whereas morphine induces only low desensitization and endocytosis. Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties. Involved in neurogenesis. Isoform 12 couples to GNAS and is proposed to be involved in excitatory effects. Isoform 16 and isoform 17 do not bind agonists but may act through oligomerization with binding- competent OPRM1 isoforms and reduce their ligand binding activity.; . TISSUE SPECIFICITY: Expressed in brain. Isoform 16 and isoform 17 are detected in brain. {ECO:0000269|PubMed:16580639}.; . . 0.17109 0.28049 1.912614283 97.42863883 2304.1461 8.88891 OPRPN . . . opiorphin prepropeptide FUNCTION: Opiorphin is an endogenous inhibitor of neprilysin and aminopeptidase N. Inhibits the breakdown of substance P, Mca-BK2 and Met-enkephalin by neprilysin in vitro with IC(50) values of 29 uM, 33 uM and 33 uM respectively. Inhibits the breakdown of Ala- pNA by aminopeptidase N in vitro with an IC(50) of 65 uM. Has a potent analgesic effect when administered to rats by intravenous injection. {ECO:0000269|PubMed:17101991}.; . TISSUE SPECIFICITY: Abundantly expressed in lacrimal gland where it found in the secretory endpieces. Also expressed at modest levels in the submandibular gland.; . . 0.03239 0.04195 -0.227663163 37.11370606 . . OPTC 4.3127291120927e-07 0.115962123532501 0.884037445194587 opticin FUNCTION: Binds collagen fibrils. {ECO:0000250}.; . TISSUE SPECIFICITY: Retina, iris, ligament, skin and fetal liver. {ECO:0000269|PubMed:12019215}.; . . 0.07883 0.13567 0.643056625 84.05284265 998.43006 6.08818 OPTN 4.99023423032989e-07 0.847327296999855 0.152672203976722 optineurin FUNCTION: Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Negatively regulates the induction of IFNB in response to RNA virus infection. Plays a neuroprotective role in the eye and optic nerve. Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8-mediated endocytic trafficking, such as of transferrin receptor (TFRC/TfR); regulates Rab8 recruitnment to tubules emanating from the endocytic recycling compartment. Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy), such as cytoplasmic Salmonella enterica, and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. May constitute a cellular target for adenovirus E3 14.7, an inhibitor of TNF-alpha functions, thereby affecting cell death. {ECO:0000269|PubMed:11834836, ECO:0000269|PubMed:15837803, ECO:0000269|PubMed:20085643, ECO:0000269|PubMed:20174559, ECO:0000269|PubMed:21617041, ECO:0000269|PubMed:22854040}.; DISEASE: Glaucoma 1, open angle, E (GLC1E) [MIM:137760]: A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. {ECO:0000269|PubMed:11834836, ECO:0000269|PubMed:12939304, ECO:0000269|PubMed:14597044, ECO:0000269|PubMed:15226658, ECO:0000269|PubMed:15326130, ECO:0000269|PubMed:15557444}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Glaucoma, normal pressure (NPG) [MIM:606657]: A primary glaucoma characterized by intraocular pression consistently within the statistically normal population range. {ECO:0000269|PubMed:15370540}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Amyotrophic lateral sclerosis 12 (ALS12) [MIM:613435]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. {ECO:0000269|PubMed:20428114}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Present in aqueous humor of the eye (at protein level). Highly expressed in trabecular meshwork. Expressed nonpigmented ciliary epithelium, retina, brain, adrenal cortex, fetus, lymphocyte, fibroblast, skeletal muscle, heart, liver, brain and placenta. {ECO:0000269|PubMed:11834836, ECO:0000269|PubMed:9488477}.; ovary;colon;substantia nigra;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;iris;pituitary gland;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;blood;lens;skeletal muscle;breast;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;alveolus;amnion;spleen;head and neck;kidney;mammary gland;stomach; amygdala;occipital lobe;subthalamic nucleus;spinal cord;prefrontal cortex;ciliary ganglion;pons;caudate nucleus;parietal lobe;skeletal muscle;cingulate cortex; 0.12825 0.21998 -0.578583623 18.71903751 339.76712 3.91067 OR1A1 0.000357575232051276 0.381458900963601 0.618183523804348 olfactory receptor family 1 subfamily A member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07025 0.09052 0.595326758 82.66100495 4438.37319 13.34676 OR1A2 0.0132146515884 0.662146961854295 0.324638386557305 olfactory receptor family 1 subfamily A member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03235 0.09480 1.350418743 94.35008257 6346.67435 16.67042 OR1AA1P . . . olfactory receptor family 1 subfamily AA member 1 pseudogene . . . . . . . . . . . OR1AB1P . . . olfactory receptor family 1 subfamily AB member 1 pseudogene . . . . . . . . . . . OR1AC1P . . . olfactory receptor family 1 subfamily AC member 1 pseudogene . . . . . . . . . . . OR1B1 0.000898340840427638 0.56686545959417 0.432236199565402 olfactory receptor family 1 subfamily B member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05291 . 1.15197334 92.52182118 6554.83979 17.04737 OR1C1 0.25334262466403 0.641119464367942 0.105537910968028 olfactory receptor family 1 subfamily C member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.507139401 80.10143902 228.0725 3.26264 OR1D2 0.00238256215176167 0.53672125062157 0.460896187226668 olfactory receptor family 1 subfamily D member 2 FUNCTION: Odorant receptor which may be involved in sperm chemotaxis. Bourgeonal is a strong chemoattractant for sperm in vitro and is shown to be a strong agonist for OR1D2 in vitro. May also function in olfactory reception. {ECO:0000269|PubMed:12663925, ECO:0000269|PubMed:15458659, ECO:0000269|PubMed:16820410}.; . TISSUE SPECIFICITY: Expressed in testis. Expressed in spermatozoa (at protein level). Expressed in olfactory epithelium. {ECO:0000269|PubMed:12663925, ECO:0000269|PubMed:15458659, ECO:0000269|PubMed:16820410}.; . . 0.24373 0.08710 1.0178651 90.91766926 2083.61947 8.40767 OR1D3P . . . olfactory receptor family 1 subfamily D member 3 pseudogene . . . . . . . . . . . OR1D4 . . . olfactory receptor family 1 subfamily D member 4 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.08460 . . . . OR1D5 0.712159402893277 0.27305365355763 0.0147869435490924 olfactory receptor family 1 subfamily D member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.08460 . . 2713.21922 9.81056 OR1E1 0.111199867995703 0.7774067126464 0.111393419357897 olfactory receptor family 1 subfamily E member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . prostate;lung;testis; trigeminal ganglion; 0.09799 0.08677 -0.227663163 37.11370606 88.36326 2.01490 OR1E2 0.0208740723340844 0.750594108571474 0.228531819094442 olfactory receptor family 1 subfamily E member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . unclassifiable (Anatomical System); . 0.16023 . 0.837848571 88.22835574 731.06744 5.36900 OR1E3 . . . olfactory receptor family 1 subfamily E member 3 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR1F1 8.87979193240061e-05 0.187719594610657 0.812191607470019 olfactory receptor family 1 subfamily F member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.17796 0.09522 1.754604356 96.69733428 3311.79424 10.99315 OR1F2P . . . olfactory receptor family 1 subfamily F member 2 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR1F12 . . . olfactory receptor family 1 subfamily F member 12 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR1G1 0.00871100712695252 0.574102336273632 0.417186656599415 olfactory receptor family 1 subfamily G member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . unclassifiable (Anatomical System); superior cervical ganglion;appendix;atrioventricular node;pons; 0.05755 . 0.150760231 64.51403633 623.71949 5.03793 OR1H1P . . . olfactory receptor family 1 subfamily H member 1 pseudogene . . . . . . . . . . . OR1I1 0.00172068988698609 0.468941613560332 0.529337696552682 olfactory receptor family 1 subfamily I member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04546 0.08475 2.263666797 98.22481717 10847.98862 22.57901 OR1J1 0.00802465330021941 0.556637924661737 0.435337422038044 olfactory receptor family 1 subfamily J member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13053 0.08213 1.306318795 93.99622552 341.55836 3.91887 OR1J2 0.00168244963116285 0.464407148501438 0.533910401867399 olfactory receptor family 1 subfamily J member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10660 . 0.396906589 76.30927105 1301.75288 6.78752 OR1J4 0.240446421040762 0.644379840188907 0.11517373877033 olfactory receptor family 1 subfamily J member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09622 . -0.381986487 27.68931352 40.37985 1.18517 OR1K1 0.000145199061585828 0.420704370680689 0.579150430257725 olfactory receptor family 1 subfamily K member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.02083 . -0.244249595 36.17008728 262.8572 3.47780 OR1L1 0.000185743012731064 0.276543930447153 0.723270326540115 olfactory receptor family 1 subfamily L member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04272 . 0.92967242 89.79122435 539.59598 4.73297 OR1L3 0.000337194097420875 0.371032330644552 0.628630475258027 olfactory receptor family 1 subfamily L member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.15708 . 2.307780051 98.3368719 2216.32254 8.67096 OR1L4 0.0431650560794194 0.662856490262943 0.293978453657637 olfactory receptor family 1 subfamily L member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.27416 0.07615 1.662761848 96.24911536 88.47426 2.01596 OR1L6 0.0106956620736813 0.617807008458063 0.371497329468256 olfactory receptor family 1 subfamily L member 6 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.16197 0.08174 0.994001092 90.5579146 255.17587 3.43646 OR1L8 0.325912944324476 0.609181504769892 0.0649055509056317 olfactory receptor family 1 subfamily L member 8 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.14081 . 0.575097644 82.1656051 310.4246 3.74870 OR1M1 0.000183470437180503 0.274814153613617 0.725002375949202 olfactory receptor family 1 subfamily M member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08575 0.09971 0.709197509 85.68058504 176.58105 2.88942 OR1M4P . . . olfactory receptor family 1 subfamily M member 4 pseudogene . . . . . . . . . . . OR1N1 0.00294378453634941 0.582252551858394 0.414803663605256 olfactory receptor family 1 subfamily N member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08027 . 0.485092724 79.37603208 1720.71703 7.65114 OR1N2 0.00140501047777096 0.428882321657453 0.569712667864776 olfactory receptor family 1 subfamily N member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.12216 . 0.863528995 88.74144845 1107.72506 6.36186 OR1P1 . . . olfactory receptor family 1 subfamily P member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR1Q1 0.000120115267773362 0.220537894853418 0.779341989878809 olfactory receptor family 1 subfamily Q member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.20608 0.09577 0.92967242 89.79122435 1344.27495 6.88397 OR1R1P . . . olfactory receptor family 1 subfamily R member 1 pseudogene . . . . . . . . . . . OR1S1 0.00790090049807544 0.553338259516024 0.438760839985901 olfactory receptor family 1 subfamily S member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.08520 1.377921151 94.56829441 3340.27802 11.06633 OR1S2 0.0010633304095779 0.377210448786122 0.6217262208043 olfactory receptor family 1 subfamily S member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13512 0.08176 0.108486928 61.90728946 1060.46079 6.24806 OR1X1P . . . olfactory receptor family 1 subfamily X member 1 pseudogene . . . . . . . . . . . OR1X5P . . . olfactory receptor family 1 subfamily X member 5 pseudogene . . . . . . . . . . . OR2A1 0.646778691858269 0.326898949199275 0.0263223589424553 olfactory receptor family 2 subfamily A member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . 192.91253 3.01030 OR2A1-AS1 . . . OR2A1 antisense RNA 1 . . . . . . . . . . . OR2A2 0.391377425515877 0.566763373485884 0.0418592009982392 olfactory receptor family 2 subfamily A member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 1.174022298 92.72823779 3286.92365 10.94044 OR2A3P . . . olfactory receptor family 2 subfamily A member 3 pseudogene . . . . . . . . . . . OR2A4 0.684827959840006 0.29611510075582 0.0190569394041737 olfactory receptor family 2 subfamily A member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . lung;thyroid;liver;hypopharynx;colon;spleen;blood;head and neck;bone marrow; . . 0.08111 . . 333.95088 3.88234 OR2A5 2.24250803002605e-05 0.162741061812673 0.837236513107026 olfactory receptor family 2 subfamily A member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.15294 . 1.464302001 95.23472517 7106.98152 18.12758 OR2A7 . . . olfactory receptor family 2 subfamily A member 7 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.08111 . . 946.38876 5.95843 OR2A9P . . . olfactory receptor family 2 subfamily A member 9 pseudogene . . . . . . . . . . . OR2A12 0.000159693166175513 0.255917372564833 0.743922934268991 olfactory receptor family 2 subfamily A member 12 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.527368849 80.73248408 444.58497 4.38722 OR2A13P . . . olfactory receptor family 2 subfamily A member 13 pseudogene . . . . . . . . . . . OR2A14 0.00212703548326032 0.512696116668436 0.485176847848303 olfactory receptor family 2 subfamily A member 14 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 1.06196211 91.507431 77.78414 1.85882 OR2A15P . . . olfactory receptor family 2 subfamily A member 15 pseudogene . . . . . . . . . . . OR2A20P . . . olfactory receptor family 2 subfamily A member 20 pseudogene . . . . . 0.15294 . . . . . OR2A25 0.34776329142618 0.596141393272603 0.0560953153012172 olfactory receptor family 2 subfamily A member 25 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.396906589 76.30927105 1023.77723 6.15088 OR2A41P . . . olfactory receptor family 2 subfamily A member 41 pseudogene . . . . . . . . . . . OR2A42 0.595675111848453 0.365456366197146 0.0388685219544015 olfactory receptor family 2 subfamily A member 42 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.09216 . . 154.60164 2.71876 OR2AD1P . . . olfactory receptor family 2 subfamily AD member 1 pseudogene . . . . . . . . . . . OR2AE1 0.00537432026972538 0.710644083171911 0.283981596558363 olfactory receptor family 2 subfamily AE member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04794 0.08406 1.041730357 91.28921916 828.72005 5.64353 OR2AF1P . . . olfactory receptor family 2 subfamily AF member 1 pseudogene . . . . . . . . . . . OR2AG1 8.87524222679285e-06 0.0971959949050094 0.902795129852764 olfactory receptor family 2 subfamily AG member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10010 0.11969 1.907156687 97.38145789 972.44809 6.02727 OR2AG2 0.216721901668246 0.647828415353731 0.135449682978023 olfactory receptor family 2 subfamily AG member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.15101 . 0.753291803 86.71266808 2398.36517 9.08947 OR2AH1P . . . olfactory receptor family 2 subfamily AH member 1 pseudogene . . . . . . . . . . . OR2AI1P . . . olfactory receptor family 2 subfamily AI member 1 pseudogene . . . . . . . . . . . OR2AJ1 0.0152833137797469 0.457013798674776 0.527702887545477 olfactory receptor family 2 subfamily AJ member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.07697 . . 118.03568 2.36329 OR2AK2 0.0159576976321787 0.700259347200566 0.283782955167255 olfactory receptor family 2 subfamily AK member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.20784 0.08823 1.396334339 94.70393961 2892.1576 10.18555 OR2AL1P . . . olfactory receptor family 2 subfamily AL member 1 pseudogene . . . . . . . . . . . OR2AM1P . . . olfactory receptor family 2 subfamily AM member 1 pseudogene . . . . . . . . . . . OR2AO1P . . . olfactory receptor family 2 subfamily AO member 1 pseudogene . . . . . . . . . . . OR2AP1 0.00290394574305701 0.357954462991494 0.639141591265449 olfactory receptor family 2 subfamily AP member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06072 0.07752 . . 792.91605 5.55327 OR2AQ1P . . . olfactory receptor family 2 subfamily AQ member 1 pseudogene . . . . . . . . . . . OR2AS1P . . . olfactory receptor family 2 subfamily AS member 1 pseudogene . . . . . . . . . . . OR2AS2P . . . olfactory receptor family 2 subfamily AS member 2 pseudogene . . . . . . . . . . . OR2AT1P . . . olfactory receptor family 2 subfamily AT member 1 pseudogene . . . . . . . . . . . OR2AT2P . . . olfactory receptor family 2 subfamily AT member 2 pseudogene . . . . . . . . . . . OR2AT4 0.0460851530028238 0.674606296947873 0.279308550049303 olfactory receptor family 2 subfamily AT member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13894 . 0.461228372 78.46190139 156.25725 2.73207 OR2B2 6.86720334316105e-05 0.293561169178199 0.706370158788369 olfactory receptor family 2 subfamily B member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08844 . 1.194256079 92.88747346 903.05828 5.84948 OR2B3 0.0013369321318042 0.419369457079468 0.579293610788728 olfactory receptor family 2 subfamily B member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.07349 -0.071520315 48.34866714 44.56192 1.27835 OR2B4P . . . olfactory receptor family 2 subfamily B member 4 pseudogene . . . . . . . . . . . OR2B6 0.0407309275321611 0.84310874527055 0.116160327197289 olfactory receptor family 2 subfamily B member 6 FUNCTION: Odorant receptor. {ECO:0000305}.; . . liver;spleen; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion; 0.08386 . -0.025608647 51.91672564 720.20671 5.32867 OR2B7P . . . olfactory receptor family 2 subfamily B member 7 pseudogene . . . . . . . . . . . OR2B8P . . . olfactory receptor family 2 subfamily B member 8 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR2B11 0.0215165179641658 0.755899102106295 0.222584379929539 olfactory receptor family 2 subfamily B member 11 FUNCTION: Odorant receptor. {ECO:0000305}.; . . larynx;head and neck; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.20408 . 2.309597117 98.34866714 10997.07756 22.87003 OR2BH1P . . . olfactory receptor family 2 subfamily BH member 1 pseudogene . . . . . . . . . . . OR2C1 0.0975481717862837 0.770782580230736 0.13166924798298 olfactory receptor family 2 subfamily C member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10846 . 1.131742211 92.26232602 3183.81879 10.75159 OR2C3 0.114992646561768 0.778490322399812 0.10651703103842 olfactory receptor family 2 subfamily C member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09087 . 0.92967242 89.79122435 599.30859 4.95514 OR2D2 5.50847424198125e-07 0.0709484231064733 0.929051026046103 olfactory receptor family 2 subfamily D member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.18602 . 2.175443036 98.06558151 3996.34126 12.50327 OR2D3 0.00308950663827612 0.592727969118813 0.404182524242911 olfactory receptor family 2 subfamily D member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . liver; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07780 0.07280 1.107875794 92.03821656 7683.58187 18.84784 OR2E1P . . . olfactory receptor family 2 subfamily E member 1 pseudogene . . . . . . . . . . . OR2F1 0.00428737773717987 0.66344502756373 0.33226759469909 olfactory receptor family 2 subfamily F member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.08305 0.196671391 67.19155461 2219.19719 8.67587 OR2F2 0.000573456091648581 0.472091341096116 0.527335202812235 olfactory receptor family 2 subfamily F member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.619191319 83.36282142 4160.05658 12.80601 OR2G1P . . . olfactory receptor family 2 subfamily G member 1 pseudogene . . . . . . . . . . . OR2G2 0.0571280420634526 0.710263500096905 0.232608457839642 olfactory receptor family 2 subfamily G member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13745 . 1.572740636 95.70653456 4397.08882 13.25183 OR2G3 0.0570926577558068 0.710168058511643 0.23273928373255 olfactory receptor family 2 subfamily G member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 1.77302331 96.80938901 3597.0752 11.60991 OR2G6 0.0097517007736297 0.598160078905714 0.392088220320656 olfactory receptor family 2 subfamily G member 6 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.08737 0.777157784 87.17857985 2113.92535 8.46187 OR2H1 0.0449040613109769 0.851616220687114 0.103479718001909 olfactory receptor family 2 subfamily H member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07748 . 1.594792159 95.83628214 557.37033 4.79615 OR2H2 0.0899459247726437 0.764866675243176 0.14518739998418 olfactory receptor family 2 subfamily H member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.11129 . 0.639420866 83.8995046 2195.65784 8.62542 OR2H4P . . . olfactory receptor family 2 subfamily H member 4 pseudogene . . . . . . . . . . . OR2H5P . . . olfactory receptor family 2 subfamily H member 5 pseudogene . . . . . . . . . . . OR2I1P . . . olfactory receptor family 2 subfamily I member 1 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR2J1 0.0174945019459341 0.7181015617827 0.264403936271366 olfactory receptor family 2 subfamily J member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.12456 . . . 8503.25217 19.94659 OR2J2 0.0107267189301636 0.618421861528154 0.370851419541683 olfactory receptor family 2 subfamily J member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08007 . 1.574555842 95.73602265 5958.84578 16.03795 OR2J3 0.0281435008681581 0.798727626786482 0.17312887234536 olfactory receptor family 2 subfamily J member 3 FUNCTION: Odorant receptor involved in the detection of the flavor compound cis-3-hexen-1-ol (C3HEX), a compound typically described as 'green grassy' or the smell of 'cut grass'. {ECO:0000269|PubMed:22714804}.; . . . . 0.09624 . 0.815800671 87.8744987 993.2965 6.07287 OR2J4P . . . olfactory receptor family 2 subfamily J member 4 pseudogene . . . . . . . . . . . OR2K2 0.00146151785432729 0.436523002007017 0.562015480138656 olfactory receptor family 2 subfamily K member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.12462 0.08302 0.332586472 73.61405992 952.14168 5.97158 OR2L1P . . . olfactory receptor family 2 subfamily L member 1 pseudogene . . . . . . . . . . . OR2L2 0.00186774816903584 0.485665938411558 0.512466313419407 olfactory receptor family 2 subfamily L member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08499 0.08678 1.019682101 90.97664544 650.65007 5.11800 OR2L3 6.39176609224206e-05 0.283107844653649 0.716828237685429 olfactory receptor family 2 subfamily L member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04593 0.09315 1.128108522 92.19155461 2290.45899 8.85807 OR2L5 7.10964719988903e-05 0.298725196806421 0.70120370672158 olfactory receptor family 2 subfamily L member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06898 0.08930 . . 909.16901 5.86231 OR2L6P . . . olfactory receptor family 2 subfamily L member 6 pseudogene . . . . . . . . . . . OR2L8 0.179168619944803 0.766561924413301 0.0542694556418958 olfactory receptor family 2 subfamily L member 8 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05102 0.09448 2.396009417 98.49020996 223.42356 3.23122 OR2L9P . . . olfactory receptor family 2 subfamily L member 9 pseudogene . . . . . . . . . . . OR2L13 0.0144191909265063 0.679992608187369 0.305588200886125 olfactory receptor family 2 subfamily L member 13 FUNCTION: Odorant receptor. {ECO:0000305}.; . . unclassifiable (Anatomical System);brain; . 0.12185 0.08854 0.595326758 82.66100495 760.16705 5.46484 OR2M1P . . . olfactory receptor family 2 subfamily M member 1 pseudogene . . . . . 0.09306 . . . . . OR2M2 0.000216664687987796 0.29893105507531 0.700852280236703 olfactory receptor family 2 subfamily M member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08110 . 1.131742211 92.26232602 172.54754 2.86187 OR2M3 0.0671997116609769 0.733522064753469 0.199278223585554 olfactory receptor family 2 subfamily M member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09306 . 1.488170966 95.3467799 143.14241 2.60846 OR2M4 0.000224877765407964 0.304549927565904 0.695225194668688 olfactory receptor family 2 subfamily M member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06099 . 0.41713504 76.95800896 81.92453 1.91886 OR2M5 0.00156615505507947 0.45010462076408 0.54832922418084 olfactory receptor family 2 subfamily M member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07654 . 2.33165376 98.38405284 958.84659 5.99448 OR2M7 0.012356410379401 0.648204884912167 0.339438704708432 olfactory receptor family 2 subfamily M member 7 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10388 . 2.131332486 97.91814107 3155.42063 10.69910 OR2N1P . . . olfactory receptor family 2 subfamily N member 1 pseudogene . . . . . . . . . . . OR2P1P . . . olfactory receptor family 2 subfamily P member 1 pseudogene . . . . . . . . . . . OR2Q1P . . . olfactory receptor family 2 subfamily Q member 1 pseudogene . . . . . . . . . . . OR2R1P . . . olfactory receptor family 2 subfamily R member 1 pseudogene . . . . . . . . . . . OR2S1P . . . olfactory receptor family 2 subfamily S member 1 pseudogene . . . . . . . . . . . OR2S2 0.000575667126931314 0.279088544790144 0.720335788082925 olfactory receptor family 2 subfamily S member 2 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.22752 . 2.375767748 98.46072187 3310.70243 10.98478 OR2T1 7.28824697455401e-07 0.0832233263771379 0.916775944798165 olfactory receptor family 2 subfamily T member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.07394 0.576916344 82.25406936 302.9944 3.70992 OR2T2 0.692627480778694 0.289610412685744 0.0177621065355616 olfactory receptor family 2 subfamily T member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.21723 0.10332 0.995816767 90.62278839 50.05023 1.38853 OR2T3 0.358715347130465 0.589151461296391 0.052133191573144 olfactory receptor family 2 subfamily T member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08784 . 1.15197334 92.52182118 2365.58513 9.03046 OR2T4 0.337136812366449 0.602641800452354 0.0602213871811971 olfactory receptor family 2 subfamily T member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07315 . 2.153387652 98.00070771 14058.26037 25.67049 OR2T5 0.620583476697508 0.347093155596074 0.0323233677064179 olfactory receptor family 2 subfamily T member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05312 0.07583 . . 1554.59962 7.30462 OR2T6 0.0505815474387303 0.690654728542337 0.258763724018933 olfactory receptor family 2 subfamily T member 6 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05317 0.09506 2.463998608 98.59046945 4829.42945 14.09940 OR2T7 0.100403453856641 0.772559569825796 0.127036976317563 olfactory receptor family 2 subfamily T member 7 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . 3352.05838 11.09195 OR2T8 0.71743769729565 0.268516453657689 0.014045849046661 olfactory receptor family 2 subfamily T member 8 FUNCTION: Odorant receptor. {ECO:0000305}.; . . lung; . . . . . 13352.74449 24.91984 OR2T10 0.000155748840698714 0.252629734763023 0.747214516396279 olfactory receptor family 2 subfamily T member 10 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.09903 1.683000003 96.35527247 668.53341 5.17173 OR2T11 2.01105703156492e-05 0.153322187916743 0.846657701512941 olfactory receptor family 2 subfamily T member 11 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09102 0.07555 1.86304987 97.17504128 633.70154 5.06921 OR2T12 0.0170417020619487 0.71307075703234 0.269887540905711 olfactory receptor family 2 subfamily T member 12 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05061 0.09523 2.465816951 98.61405992 2483.52171 9.29597 OR2T27 0.000134198174502552 0.233779400278912 0.766086401546585 olfactory receptor family 2 subfamily T member 27 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.330767508 73.53739089 4720.23419 13.88234 OR2T29 0.476864535017878 0.439355692401997 0.0837797725801249 olfactory receptor family 2 subfamily T member 29 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.07583 . . 6299.17719 16.57856 OR2T32P . . . olfactory receptor family 2 subfamily T member 32 pseudogene . . . . . . . . . . . OR2T33 0.0164922028007124 0.706716696729739 0.276791100469549 olfactory receptor family 2 subfamily T member 33 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10124 0.09346 1.219937511 93.19414956 662.98621 5.16078 OR2T34 0.746970217903766 0.242670506614907 0.0103592754813271 olfactory receptor family 2 subfamily T member 34 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 1.039913547 91.25973107 2760.32398 9.91599 OR2T35 0.536149911036962 0.405579762223612 0.0582703267394252 olfactory receptor family 2 subfamily T member 35 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.10265 . . 8897.86165 20.38471 OR2U1P . . . olfactory receptor family 2 subfamily U member 1 pseudogene . . . . . . . . . . . OR2U2P . . . olfactory receptor family 2 subfamily U member 2 pseudogene . . . . . . . . . . . OR2V1 1.7436947905009e-08 0.0182691259764814 0.981730856586571 olfactory receptor family 2 subfamily V member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . 1292.43967 6.76638 OR2V2 0.225731243700957 0.646939687726139 0.127329068572903 olfactory receptor family 2 subfamily V member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.21240 . 0.661468037 84.4420854 646.29043 5.10431 OR2W1 0.0865618905271982 0.76161557996086 0.151822529511941 olfactory receptor family 2 subfamily W member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.12105 . 0.613741468 83.06794055 3001.9101 10.39930 OR2W2P . . . olfactory receptor family 2 subfamily W member 2 pseudogene . . . . . . . . . . . OR2W3 0.079635091424146 0.753588012937454 0.1667768956384 olfactory receptor family 2 subfamily W member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . liver;spleen;blood; atrioventricular node; . . 2.397825098 98.50790281 12341.4493 23.88234 OR2W4P . . . olfactory receptor family 2 subfamily W member 4 pseudogene . . . . . . . . . . . OR2W5 . . . olfactory receptor family 2 subfamily W member 5 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03576 . . . . . OR2W6P . . . olfactory receptor family 2 subfamily W member 6 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR2X1P . . . olfactory receptor family 2 subfamily X member 1 pseudogene . . . . . . . . . . . OR2Y1 5.15790392859341e-07 0.0683298816611474 0.93166960254846 olfactory receptor family 2 subfamily Y member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.10116 1.640710091 96.13116301 485.02714 4.53420 OR2Z1 1.26516520297013e-08 0.0151411609606116 0.984858826387736 olfactory receptor family 2 subfamily Z member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03911 . -0.600630256 18.06440198 92.82759 2.07070 OR3A1 0.0295684605043502 0.80570309390925 0.1647284455864 olfactory receptor family 3 subfamily A member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13388 0.12197 1.664578456 96.27860344 329.34294 3.85798 OR3A2 0.564393310538053 0.42344152743376 0.0121651620281869 olfactory receptor family 3 subfamily A member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.10860 1.284269037 93.76621845 1951.498 8.12902 OR3A3 0.416001527528029 0.548578793460988 0.0354196790109831 olfactory receptor family 3 subfamily A member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.08451 0.525552348 80.57914603 4974.65453 14.37626 OR3A4P . . . olfactory receptor family 3 subfamily A member 4 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03393 . . . . . OR3A5P . . . olfactory receptor family 3 subfamily A member 5 pseudogene . . . . . . . . . . . OR3B1P . . . olfactory receptor family 3 subfamily B member 1 pseudogene . . . . . . . . . . . OR3D1P . . . olfactory receptor family 3 subfamily D member 1 pseudogene . . . . . . . . . . . OR4A1P . . . olfactory receptor family 4 subfamily A member 1 pseudogene . . . . . . . . . . . OR4A2P . . . olfactory receptor family 4 subfamily A member 2 pseudogene . . . . . . . . . . . OR4A3P . . . olfactory receptor family 4 subfamily A member 3 pseudogene . . . . . . . . . . . OR4A4P . . . olfactory receptor family 4 subfamily A member 4 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.08669 . . . . OR4A5 . . . olfactory receptor family 4 subfamily A member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 1.379742765 94.60368011 1521.02291 7.25005 OR4A6P . . . olfactory receptor family 4 subfamily A member 6 pseudogene . . . . . . . . . . . OR4A7P . . . olfactory receptor family 4 subfamily A member 7 pseudogene . . . . . . . . . . . OR4A8 . . . olfactory receptor family 4 subfamily A member 8 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR4A9P . . . olfactory receptor family 4 subfamily A member 9 pseudogene . . . . . . . . . . . OR4A10P . . . olfactory receptor family 4 subfamily A member 10 pseudogene . . . . . . . . . . . OR4A11P . . . olfactory receptor family 4 subfamily A member 11 pseudogene . . . . . . . . . . . OR4A12P . . . olfactory receptor family 4 subfamily A member 12 pseudogene . . . . . . . . . . . OR4A13P . . . olfactory receptor family 4 subfamily A member 13 pseudogene . . . . . 0.21252 . . . . . OR4A14P . . . olfactory receptor family 4 subfamily A member 14 pseudogene . . . . . . . . . . . OR4A15 . . . olfactory receptor family 4 subfamily A member 15 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08837 0.09327 -0.574945567 18.90186365 359.46379 4.01407 OR4A16 2.61340194128249e-05 0.176866443227184 0.823107422753403 olfactory receptor family 4 subfamily A member 16 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13831 . 0.022122107 55.69120075 5074.62516 14.58816 OR4A17P . . . olfactory receptor family 4 subfamily A member 17 pseudogene . . . . . . . . . . . OR4A18P . . . olfactory receptor family 4 subfamily A member 18 pseudogene . . . . . . . . . . . OR4A19P . . . olfactory receptor family 4 subfamily A member 19 pseudogene . . . . . . . . . . . OR4A21P . . . olfactory receptor family 4 subfamily A member 21 pseudogene . . . . . . . . . . . OR4A40P . . . olfactory receptor family 4 subfamily A member 40 pseudogene . . . . . . . . . . . OR4A41P . . . olfactory receptor family 4 subfamily A member 41 pseudogene . . . . . . . . . . . OR4A42P . . . olfactory receptor family 4 subfamily A member 42 pseudogene . . . . . . . . . . . OR4A43P . . . olfactory receptor family 4 subfamily A member 43 pseudogene . . . . . . . . . . . OR4A44P . . . olfactory receptor family 4 subfamily A member 44 pseudogene . . . . . . . . . . . OR4A45P . . . olfactory receptor family 4 subfamily A member 45 pseudogene . . . . . . . . . . . OR4A46P . . . olfactory receptor family 4 subfamily A member 46 pseudogene . . . . . . . . . . . OR4A47 1.43390782604699e-05 0.127184261130637 0.872801399791102 olfactory receptor family 4 subfamily A member 47 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.08669 0.867166666 88.81811748 585.01763 4.90333 OR4A48P . . . olfactory receptor family 4 subfamily A member 48 pseudogene . . . . . . . . . . . OR4A49P . . . olfactory receptor family 4 subfamily A member 49 pseudogene . . . . . . . . . . . OR4A50P . . . olfactory receptor family 4 subfamily A member 50 pseudogene . . . . . . . . . . . OR4B1 0.0109380186584993 0.622554900343301 0.3665070809982 olfactory receptor family 4 subfamily B member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08410 0.09408 1.041730357 91.28921916 1163.11366 6.49157 OR4B2P . . . olfactory receptor family 4 subfamily B member 2 pseudogene . . . . . . . . . . . OR4C1P . . . olfactory receptor family 4 subfamily C member 1 pseudogene . . . . . . . . . . . OR4C2P . . . olfactory receptor family 4 subfamily C member 2 pseudogene . . . . . . . . . . . OR4C3 0.00874513097467769 0.574935520574959 0.416319348450363 olfactory receptor family 4 subfamily C member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05877 . -0.067881249 48.69072895 407.80638 4.23445 OR4C4P . . . olfactory receptor family 4 subfamily C member 4 pseudogene . . . . . 0.03375 . . . . . OR4C5 0.0165676629621224 0.472836156971854 0.510596180066023 olfactory receptor family 4 subfamily C member 5 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.15522 . . . 4982.12533 14.39455 OR4C6 1.0819424863645e-05 0.108661812346424 0.891327368228712 olfactory receptor family 4 subfamily C member 6 FUNCTION: Odorant receptor. {ECO:0000305}.; . . placenta; . 0.07812 . 0.154398214 64.73814579 2035.0433 8.30878 OR4C7P . . . olfactory receptor family 4 subfamily C member 7 pseudogene . . . . . . . . . . . OR4C9P . . . olfactory receptor family 4 subfamily C member 9 pseudogene . . . . . . . . . . . OR4C10P . . . olfactory receptor family 4 subfamily C member 10 pseudogene . . . . . . . . . . . OR4C11 1.40886744095212e-06 0.0642327465971182 0.935765844535441 olfactory receptor family 4 subfamily C member 11 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10561 . 1.796891089 96.90375088 2460.54814 9.23410 OR4C12 0.23821319029955 0.644851399048853 0.116935410651597 olfactory receptor family 4 subfamily C member 12 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.350995466 74.37485256 3162.15952 10.71740 OR4C13 8.59262892850206e-09 0.0120690296059355 0.987930961801436 olfactory receptor family 4 subfamily C member 13 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.955356963 90.10969568 228.22547 3.26358 OR4C14P . . . olfactory receptor family 4 subfamily C member 14 pseudogene . . . . . . . . . . . OR4C15 3.39409709462154e-11 0.00332014752144274 0.996679852444616 olfactory receptor family 4 subfamily C member 15 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03606 . 1.890561548 97.3165841 3098.18252 10.58837 OR4C16 . . . olfactory receptor family 4 subfamily C member 16 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07415 . 2.469464962 98.61995754 5426.28301 15.19003 OR4C45 . . . olfactory receptor family 4 subfamily C member 45 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03375 . . . . . OR4C46 8.76630664507137e-07 0.0488872912731288 0.951111832096207 olfactory receptor family 4 subfamily C member 46 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.17314 . 1.469764896 95.28190611 10416.81228 22.30627 OR4C48P . . . olfactory receptor family 4 subfamily C member 48 pseudogene . . . . . . . . . . . OR4C49P . . . olfactory receptor family 4 subfamily C member 49 pseudogene . . . . . . . . . . . OR4C50P . . . olfactory receptor family 4 subfamily C member 50 pseudogene . . . . . . . . . . . OR4D1 0.000295713706769417 0.348430794664513 0.651273491628718 olfactory receptor family 4 subfamily D member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.15258 . 0.883760026 89.07171503 2214.93713 8.66606 OR4D2 0.0138443702712982 0.671711897515468 0.314443732213234 olfactory receptor family 4 subfamily D member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07605 0.09185 1.77302331 96.80938901 2263.68073 8.79200 OR4D5 0.00186757114304027 0.485646453354072 0.512485975502888 olfactory receptor family 4 subfamily D member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.15364 0.08789 0.575097644 82.1656051 580.9057 4.88551 OR4D6 0.0150121178988349 0.68811544375241 0.296872438348756 olfactory receptor family 4 subfamily D member 6 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10146 . 2.886778618 99.13894787 4858.02255 14.17423 OR4D7P . . . olfactory receptor family 4 subfamily D member 7 pseudogene . . . . . . . . . . . OR4D8P . . . olfactory receptor family 4 subfamily D member 8 pseudogene . . . . . . . . . . . OR4D9 4.8854167946133e-05 0.246608821508183 0.753342324323871 olfactory receptor family 4 subfamily D member 9 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03540 0.08178 1.664578456 96.27860344 539.3985 4.73231 OR4D10 0.0640123916557904 0.72694562906311 0.2090419792811 olfactory receptor family 4 subfamily D member 10 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . -0.336073593 30.55555556 992.09784 6.06928 OR4D11 0.000895035311998553 0.347427464832913 0.651677499855089 olfactory receptor family 4 subfamily D member 11 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.11488 0.08063 -0.047654689 50.22410946 212.53385 3.14608 OR4D12P . . . olfactory receptor family 4 subfamily D member 12 pseudogene . . . . . . . . . . . OR4E1 . . . olfactory receptor family 4 subfamily E member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR4E2 0.000222164124943235 0.302707440159442 0.697070395715615 olfactory receptor family 4 subfamily E member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.352813824 74.49280491 1033.3232 6.17567 OR4F1P . . . olfactory receptor family 4 subfamily F member 1 pseudogene . . . . . . . . . . . OR4F2P . . . olfactory receptor family 4 subfamily F member 2 pseudogene . . . . . . . . . . . OR4F3 . . . olfactory receptor family 4 subfamily F member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.08067 . . . . OR4F4 0.54595605565204 0.399365949908743 0.0546779944392172 olfactory receptor family 4 subfamily F member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06092 0.06978 . . 61.05371 1.59033 OR4F5 0.176329298172162 0.644086264144236 0.179584437683602 olfactory receptor family 4 subfamily F member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06092 0.07159 . . 113.16669 2.31572 OR4F6 1.34347941087799e-05 0.224656819324412 0.775329745881479 olfactory receptor family 4 subfamily F member 6 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07657 0.09369 1.150157577 92.46874263 85.13152 1.96644 OR4F7P . . . olfactory receptor family 4 subfamily F member 7 pseudogene . . . . . . . . . . . OR4F8P . . . olfactory receptor family 4 subfamily F member 8 pseudogene . . . . . . . . . . . OR4F13P . . . olfactory receptor family 4 subfamily F member 13 pseudogene . . . . . . 0.07269 . . . . OR4F14P . . . olfactory receptor family 4 subfamily F member 14 pseudogene . . . . . . . . . . . OR4F15 0.205470537627522 0.648135443752866 0.146394018619613 olfactory receptor family 4 subfamily F member 15 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.07116 0.751474114 86.64779429 616.86938 5.01391 OR4F16 . . . olfactory receptor family 4 subfamily F member 16 FUNCTION: Odorant receptor. {ECO:0000305}.; . . heart;skeletal muscle; . . 0.08067 . . . . OR4F17 0.505111518356241 0.42411078527551 0.0707776963682487 olfactory receptor family 4 subfamily F member 17 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.06796 . . 28.5008 0.91295 OR4F21 . . . olfactory receptor family 4 subfamily F member 21 FUNCTION: Odorant receptor. {ECO:0000305}.; . . heart;skeletal muscle; . 0.17397 . . . 20.56388 0.69884 OR4F28P . . . olfactory receptor family 4 subfamily F member 28 pseudogene . . . . . . . . . . . OR4F29 . . . olfactory receptor family 4 subfamily F member 29 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.08067 . . . . OR4G1P . . . olfactory receptor family 4 subfamily G member 1 pseudogene . . . . . . . . . . . OR4G2P . . . olfactory receptor family 4 subfamily G member 2 pseudogene . . . frontal lobe; . . . . . . . OR4G3P . . . olfactory receptor family 4 subfamily G member 3 pseudogene . . . . . . . . . . . OR4G4P . . . olfactory receptor family 4 subfamily G member 4 pseudogene . . . . . . . . . . . OR4G6P . . . olfactory receptor family 4 subfamily G member 6 pseudogene . . . . . . . . . . . OR4G11P . . . olfactory receptor family 4 subfamily G member 11 pseudogene . . . . . . . . . . . OR4H6P . . . olfactory receptor family 4 subfamily H member 6 pseudogene . . . . . . . . . . . OR4H12P . . . olfactory receptor family 4 subfamily H member 12 pseudogene . . . . . . . . . . . OR4K1 2.21165537903248e-06 0.0830941563795939 0.916903631965027 olfactory receptor family 4 subfamily K member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07771 0.08637 1.376101648 94.5329087 4709.77196 13.84989 OR4K2 8.6747089870991e-06 0.0959497343041198 0.904041590986893 olfactory receptor family 4 subfamily K member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.16321 0.09621 0.707379532 85.62750649 1467.85369 7.14062 OR4K3 . . . olfactory receptor family 4 subfamily K member 3 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR4K4P . . . olfactory receptor family 4 subfamily K member 4 pseudogene . . . . . . . . . . . OR4K5 0.000430658354321092 0.415769511038526 0.583799830607153 olfactory receptor family 4 subfamily K member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07634 0.07407 1.506587076 95.41165369 1357.12749 6.91332 OR4K6P . . . olfactory receptor family 4 subfamily K member 6 pseudogene . . . . . . . . . . . OR4K7P . . . olfactory receptor family 4 subfamily K member 7 pseudogene . . . . . . . . . . . OR4K8P . . . olfactory receptor family 4 subfamily K member 8 pseudogene . . . . . . . . . . . OR4K11P . . . olfactory receptor family 4 subfamily K member 11 pseudogene . . . . . . . . . . . OR4K12P . . . olfactory receptor family 4 subfamily K member 12 pseudogene . . . . . . . . . . . OR4K13 6.75517891131211e-05 0.291138012273805 0.708794435937081 olfactory receptor family 4 subfamily K member 13 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09835 0.09066 0.374860183 75.43052607 239.02977 3.34005 OR4K14 0.027453438192046 0.79510883899297 0.177437722814984 olfactory receptor family 4 subfamily K member 14 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06895 0.06354 0.507139401 80.10143902 1589.72852 7.37441 OR4K15 0.635537854800151 0.335670373328485 0.0287917718713639 olfactory receptor family 4 subfamily K member 15 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05132 0.09060 1.620475625 96.01321066 9710.33902 21.39036 OR4K16P . . . olfactory receptor family 4 subfamily K member 16 pseudogene . . . . . . . . . . . OR4K17 0.047180154158617 0.678731579053989 0.274088266787394 olfactory receptor family 4 subfamily K member 17 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06415 0.08130 0.350995466 74.37485256 4409.10844 13.28482 OR4L1 0.00278340671476074 0.570129295270425 0.427087298014814 olfactory receptor family 4 subfamily L member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.27910 . 2.219554466 98.15404577 10875.94722 22.61941 OR4M1 0.00516878743080707 0.702654668795087 0.292176543774106 olfactory receptor family 4 subfamily M member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.08778 1.063778722 91.58410002 2395.09734 9.08587 OR4M2 . . . olfactory receptor family 4 subfamily M member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . lung;testis; . 0.05315 0.08153 3.177250279 99.31587639 740.16744 5.40199 OR4N1P . . . olfactory receptor family 4 subfamily N member 1 pseudogene . . . . . . . . . . . OR4N2 0.0737889122932416 0.745164659516631 0.181046428190128 olfactory receptor family 4 subfamily N member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . lung;testis; . . 0.08855 2.263666797 98.22481717 1961.48908 8.15799 OR4N3P . . . olfactory receptor family 4 subfamily N member 3 pseudogene . . . . . . . . . . . OR4N4 0.0180506007874978 0.724040025240097 0.257909373972405 olfactory receptor family 4 subfamily N member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . testis; dorsal root ganglion;superior cervical ganglion;testis - interstitial;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.09536 0.07409 2.241610517 98.18353385 4448.2419 13.37082 OR4N5 0.235716665504507 0.645344379094542 0.118938955400951 olfactory receptor family 4 subfamily N member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09451 0.07204 1.219937511 93.19414956 658.04093 5.14405 OR4P1P . . . olfactory receptor family 4 subfamily P member 1 pseudogene . . . . . . . . . . . OR4P4 0.0573838007216111 0.710950195278255 0.231666004000134 olfactory receptor family 4 subfamily P member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13743 . 1.174022298 92.72823779 3446.82642 11.28163 OR4Q1P . . . olfactory receptor family 4 subfamily Q member 1 pseudogene . . . . . . . . . . . OR4Q2 . . . olfactory receptor family 4 subfamily Q member 2 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.19141 . . . . . OR4Q3 . . . olfactory receptor family 4 subfamily Q member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.08889 0.799205007 87.58551545 561.26319 4.81092 OR4R1P . . . olfactory receptor family 4 subfamily R member 1 pseudogene . . . . . . . . . . . OR4R2P . . . olfactory receptor family 4 subfamily R member 2 pseudogene . . . . . . . . . . . OR4R3P . . . olfactory receptor family 4 subfamily R member 3 pseudogene . . . . . . . . . . . OR4S1 0.00461719061361746 0.443095935091054 0.552286874295329 olfactory receptor family 4 subfamily S member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03696 . 0.554869705 81.59943383 311.04793 3.75397 OR4S2 0.00103860294519937 0.373042627332009 0.625918769722792 olfactory receptor family 4 subfamily S member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.15926 0.09532 2.041296411 97.74121255 4654.68631 13.74344 OR4T1P . . . olfactory receptor family 4 subfamily T member 1 pseudogene . . . . . . . . . . . OR4U1P . . . olfactory receptor family 4 subfamily U member 1 pseudogene . . . . . . . . . . . OR4V1P . . . olfactory receptor family 4 subfamily V member 1 pseudogene . . . . . . . . . . . OR4W1P . . . olfactory receptor family 4 subfamily W member 1 pseudogene . . . . . . . . . . . OR4X1 0.00015767458987061 0.254240706362463 0.745601619047666 olfactory receptor family 4 subfamily X member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05662 . 2.065168262 97.79429111 6408.13182 16.75374 OR4X2 1.10988723254503e-08 0.0140229613596627 0.985977027541465 olfactory receptor family 4 subfamily X member 2 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.17278 . -0.312207497 32.05944798 157.44764 2.74208 OR4X7P . . . olfactory receptor family 4 subfamily X member 7 pseudogene . . . . . . . . . . . OR5A1 2.02941693534639e-05 0.278199244992986 0.721780460837661 olfactory receptor family 5 subfamily A member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.15302 0.10052 0.92967242 89.79122435 293.42915 3.66116 OR5A2 0.0014039822282672 0.428741189456241 0.569854828315492 olfactory receptor family 5 subfamily A member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09610 0.09786 0.418953042 77.06416608 1723.98697 7.66150 OR5AC1 . . . olfactory receptor family 5 subfamily AC member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR5AC2 5.95935728781755e-05 0.273193159139336 0.726747247287786 olfactory receptor family 5 subfamily AC member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06257 . 0.707379532 85.62750649 302.82193 3.70784 OR5AC4P . . . olfactory receptor family 5 subfamily AC member 4 pseudogene . . . . . . . . . . . OR5AH1P . . . olfactory receptor family 5 subfamily AH member 1 pseudogene . . . . . . . . . . . OR5AK1P . . . olfactory receptor family 5 subfamily AK member 1 pseudogene . . . . . . . . . . . OR5AK2 2.87905465610352e-07 0.0488687323596804 0.951130979734854 olfactory receptor family 5 subfamily AK member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . unclassifiable (Anatomical System); superior cervical ganglion;ciliary ganglion;atrioventricular node; . . 0.332586472 73.61405992 381.31084 4.11541 OR5AK3P . . . olfactory receptor family 5 subfamily AK member 3 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR5AK4P . . . olfactory receptor family 5 subfamily AK member 4 pseudogene . . . . . . . . . . . OR5AL1 . . . olfactory receptor family 5 subfamily AL member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR5AL2P . . . olfactory receptor family 5 subfamily AL member 2 pseudogene . . . . . . . . . . . OR5AM1P . . . olfactory receptor family 5 subfamily AM member 1 pseudogene . . . . . . . . . . . OR5AN1 0.00117731258117152 0.395606215344097 0.603216472074732 olfactory receptor family 5 subfamily AN member 1 FUNCTION: Odorant receptor involved in the detection of muscone. {ECO:0000269|PubMed:24361078}.; . . . . 0.09274 0.09481 0.395088462 76.15003539 69.39809 1.72762 OR5AN2P . . . olfactory receptor family 5 subfamily AN member 2 pseudogene . . . . . . . . . . . OR5AO1P . . . olfactory receptor family 5 subfamily AO member 1 pseudogene . . . . . . . . . . . OR5AP1P . . . olfactory receptor family 5 subfamily AP member 1 pseudogene . . . . . . . . . . . OR5AP2 0.0692232333224351 0.737363703132048 0.193413063545517 olfactory receptor family 5 subfamily AP member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . brain; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.12998 0.09727 0.707379532 85.62750649 1048.17202 6.21543 OR5AQ1P . . . olfactory receptor family 5 subfamily AQ member 1 pseudogene . . . . . . . . . . . OR5AR1 0.000179721317392242 0.271932903978608 0.727887374704 olfactory receptor family 5 subfamily AR member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.19335 . 0.108486928 61.90728946 500.98062 4.59327 OR5AS1 0.255635872734436 0.640448366841254 0.103915760424309 olfactory receptor family 5 subfamily AS member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05900 . 0.753291803 86.71266808 152.51869 2.70052 OR5AU1 1.41823424059493e-06 0.0644772163294922 0.935521365436267 olfactory receptor family 5 subfamily AU member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.11253 0.09523 0.845119304 88.4170795 696.21601 5.25581 OR5AW1P . . . olfactory receptor family 5 subfamily AW member 1 pseudogene . . . . . . . . . . . OR5AZ1P . . . olfactory receptor family 5 subfamily AZ member 1 pseudogene . . . . . . . . . . . OR5B1P . . . olfactory receptor family 5 subfamily B member 1 pseudogene . . . . . . . . . . . OR5B2 0.0056353700412876 0.482871369301052 0.511493260657661 olfactory receptor family 5 subfamily B member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08349 0.09439 0.729426781 86.17008728 2464.0354 9.24528 OR5B3 0.00100172727895397 0.36670067100573 0.632297601715316 olfactory receptor family 5 subfamily B member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07042 0.07888 2.151571682 97.9948101 9250.4919 20.84499 OR5B10P . . . olfactory receptor family 5 subfamily B member 10 pseudogene . . . . . . . . . . . OR5B12 0.310930146470037 0.617339743417035 0.0717301101129273 olfactory receptor family 5 subfamily B member 12 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09599 . 0.92967242 89.79122435 93.33985 2.07965 OR5B15P . . . olfactory receptor family 5 subfamily B member 15 pseudogene . . . . . . . . . . . OR5B17 0.0772363405801556 0.750329431827111 0.172434227592734 olfactory receptor family 5 subfamily B member 17 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04519 . 0.885576705 89.14248644 261.40357 3.47089 OR5B19P . . . olfactory receptor family 5 subfamily B member 19 pseudogene . . . . . . . . . . . OR5B21 9.44945209297068e-05 0.194097713685814 0.805807791793256 olfactory receptor family 5 subfamily B member 21 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.18883 . 0.018483465 55.44939844 397.48226 4.18877 OR5BA1P . . . olfactory receptor family 5 subfamily BA member 1 pseudogene . . . . . . . . . . . OR5BB1P . . . olfactory receptor family 5 subfamily BB member 1 pseudogene . . . . . . . . . . . OR5BC1P . . . olfactory receptor family 5 subfamily BC member 1 pseudogene . . . . . . . . . . . OR5BD1P . . . olfactory receptor family 5 subfamily BD member 1 pseudogene . . . . . . . . . . . OR5BE1P . . . olfactory receptor family 5 subfamily BE member 1 pseudogene . . . . . . . . . . . OR5BH1P . . . olfactory receptor family 5 subfamily BH member 1 pseudogene . . . . . . . . . . . OR5BJ1P . . . olfactory receptor family 5 subfamily BJ member 1 pseudogene . . . . . . . . . . . OR5BK1P . . . olfactory receptor family 5 subfamily BK member 1 pseudogene . . . . . . . . . . . OR5BL1P . . . olfactory receptor family 5 subfamily BL member 1 pseudogene . . . . . . . . . . . OR5BM1P . . . olfactory receptor family 5 subfamily BM member 1 pseudogene . . . . . . . . . . . OR5BN1P . . . olfactory receptor family 5 subfamily BN member 1 pseudogene . . . . . . . . . . . OR5BN2P . . . olfactory receptor family 5 subfamily BN member 2 pseudogene . . . . . . . . . . . OR5BP1P . . . olfactory receptor family 5 subfamily BP member 1 pseudogene . . . . . . . . . . . OR5BQ1P . . . olfactory receptor family 5 subfamily BQ member 1 pseudogene . . . . . . . . . . . OR5BR1P . . . olfactory receptor family 5 subfamily BR member 1 pseudogene . . . . . . . . . . . OR5BS1P . . . olfactory receptor family 5 subfamily BS member 1 pseudogene . . . . . . . . . . . OR5BT1P . . . olfactory receptor family 5 subfamily BT member 1 pseudogene . . . . . . . . . . . OR5C1 0.000111246308040193 0.371760618397653 0.628128135294307 olfactory receptor family 5 subfamily C member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.15125 0.08976 -0.089927255 46.99221515 156.0106 2.73040 OR5D2P . . . olfactory receptor family 5 subfamily D member 2 pseudogene . . . . . . . . . . . OR5D3P . . . olfactory receptor family 5 subfamily D member 3 pseudogene . . . . . 0.42488 . . . . . OR5D13 1.73555819538654e-07 0.0364563104935672 0.963543515950613 olfactory receptor family 5 subfamily D member 13 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05586 0.08754 0.949904335 90.00943619 965.41913 6.01040 OR5D14 0.000814344980968998 0.331830308874843 0.667355346144188 olfactory receptor family 5 subfamily D member 14 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09415 0.08667 1.885103181 97.26940316 5246.56113 14.92674 OR5D15P . . . olfactory receptor family 5 subfamily D member 15 pseudogene . . . . . . . . . . . OR5D16 2.33685393272016e-07 0.0433164424948573 0.956683323819749 olfactory receptor family 5 subfamily D member 16 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07627 . -0.069700724 48.54328851 523.9054 4.66873 OR5D17P . . . olfactory receptor family 5 subfamily D member 17 pseudogene . . . . . . . . . . . OR5D18 0.000954997598444594 0.358435159767656 0.6406098426339 olfactory receptor family 5 subfamily D member 18 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.11145 . 0.485092724 79.37603208 428.76611 4.32426 OR5E1P . . . olfactory receptor family 5 subfamily E member 1 pseudogene . . . . . 0.26480 . . . . . OR5F1 0.00647381424823331 0.511429817923607 0.482096367828159 olfactory receptor family 5 subfamily F member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.02327 0.09298 1.221756288 93.21184242 1094.58502 6.32931 OR5F2P . . . olfactory receptor family 5 subfamily F member 2 pseudogene . . . . . . . . . . . OR5G1P . . . olfactory receptor family 5 subfamily G member 1 pseudogene . . . . . . . . . . . OR5G3 . . . olfactory receptor family 5 subfamily G member 3 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR5G4P . . . olfactory receptor family 5 subfamily G member 4 pseudogene . . . . . . . . . . . OR5G5P . . . olfactory receptor family 5 subfamily G member 5 pseudogene . . . . . . . . . . . OR5H1 0.0674147765122453 0.733942261585014 0.19864296190274 olfactory receptor family 5 subfamily H member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09303 . 1.2860853 93.80160415 1317.76423 6.82798 OR5H2 1.56486567272373e-05 0.133508818436743 0.866475532906529 olfactory receptor family 5 subfamily H member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09088 0.08456 1.616843854 95.96013211 1080.75372 6.30364 OR5H3P . . . olfactory receptor family 5 subfamily H member 3 pseudogene . . . . . . . . . . . OR5H4P . . . olfactory receptor family 5 subfamily H member 4 pseudogene . . . . . . . . . . . OR5H5P . . . olfactory receptor family 5 subfamily H member 5 pseudogene . . . . . . . . . . . OR5H6 4.75403468374202e-05 0.243136431849952 0.75681602780321 olfactory receptor family 5 subfamily H member 6 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.11788 . 2.708468798 98.93253126 4962.18899 14.35805 OR5H7P . . . olfactory receptor family 5 subfamily H member 7 pseudogene . . . . . . . . . . . OR5H8 . . . olfactory receptor family 5 subfamily H member 8 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR5H14 0.000175213979260701 0.268422219736275 0.731402566284464 olfactory receptor family 5 subfamily H member 14 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09902 . 1.820761234 97.009908 426.14655 4.31286 OR5H15 1.77804938664206e-06 0.0733810467918568 0.926617175158757 olfactory receptor family 5 subfamily H member 15 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.11043 . 1.976952171 97.61146497 1829.2528 7.88488 OR5I1 0.237661331801561 0.644963503482557 0.117375164715882 olfactory receptor family 5 subfamily I member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05169 0.08722 1.107875794 92.03821656 1547.27415 7.29508 OR5J1P . . . olfactory receptor family 5 subfamily J member 1 pseudogene . . . . . . . . . . . OR5J2 0.000124682157643135 0.224920754937606 0.774954562904751 olfactory receptor family 5 subfamily J member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13232 . 0.639420866 83.8995046 259.33322 3.46102 OR5J7P . . . olfactory receptor family 5 subfamily J member 7 pseudogene . . . . . . . . . . . OR5K1 9.41011918854772e-05 0.193663892376489 0.806242006431626 olfactory receptor family 5 subfamily K member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.09296 1.374284246 94.51521585 597.45283 4.94681 OR5K2 9.18743788922924e-05 0.191189757417028 0.808718368204079 olfactory receptor family 5 subfamily K member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04662 0.08767 0.262810045 70.43524416 499.27281 4.58816 OR5K3 0.00192053079542076 0.491409669793416 0.506669799411163 olfactory receptor family 5 subfamily K member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.11094 . 1.885103181 97.26940316 4882.5213 14.20921 OR5K4 9.27165287016062e-07 0.0504942900381496 0.949504782796563 olfactory receptor family 5 subfamily K member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09144 . 1.484536216 95.31729181 4489.11023 13.44381 OR5L1 5.93920385495045e-07 0.0390268690372639 0.960972537042351 olfactory receptor family 5 subfamily L member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06073 0.09152 0.795569043 87.49115357 1193.77829 6.55439 OR5L2 0.000593860863455805 0.283530726439668 0.715875412696876 olfactory receptor family 5 subfamily L member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03996 0.09038 0.775339069 87.13729653 1325.91355 6.84513 OR5M1 0.0473826725341121 0.679478631663584 0.273138695802304 olfactory receptor family 5 subfamily M member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06561 . 0.951720429 90.06251474 5674.60384 15.58127 OR5M2P . . . olfactory receptor family 5 subfamily M member 2 pseudogene . . . . . . . . . . . OR5M3 1.24690874517497e-05 0.215977365807479 0.784010165105069 olfactory receptor family 5 subfamily M member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.14217 0.09170 0.464864541 78.69190847 759.40012 5.46250 OR5M4P . . . olfactory receptor family 5 subfamily M member 4 pseudogene . . . . . . . . . . . OR5M5P . . . olfactory receptor family 5 subfamily M member 5 pseudogene . . . . . . . . . . . OR5M6P . . . olfactory receptor family 5 subfamily M member 6 pseudogene . . . . . . . . . . . OR5M7P . . . olfactory receptor family 5 subfamily M member 7 pseudogene . . . . . . . . . . . OR5M8 0.00973388346897511 0.597770449474793 0.392495667056232 olfactory receptor family 5 subfamily M member 8 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04047 . 0.841481379 88.35810333 138.83566 2.56736 OR5M9 0.00775094260115899 0.549274355475895 0.442974701922946 olfactory receptor family 5 subfamily M member 9 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07075 . 1.975133784 97.58197688 1230.44948 6.63140 OR5M10 0.0077276318820004 0.548636055836768 0.443636312281231 olfactory receptor family 5 subfamily M member 10 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.775339069 87.13729653 411.77099 4.25037 OR5M11 0.000762549638271515 0.321291880489449 0.677945569872279 olfactory receptor family 5 subfamily M member 11 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 1.063778722 91.58410002 887.6616 5.80277 OR5M12P . . . olfactory receptor family 5 subfamily M member 12 pseudogene . . . . . . . . . . . OR5M13P . . . olfactory receptor family 5 subfamily M member 13 pseudogene . . . . . 0.06561 . . . . . OR5M14P . . . olfactory receptor family 5 subfamily M member 14 pseudogene . . . . . . . . . . . OR5P1P . . . olfactory receptor family 5 subfamily P member 1 pseudogene . . . . . . . . . . . OR5P2 0.0101383238709392 0.60643828648796 0.383423389641101 olfactory receptor family 5 subfamily P member 2 FUNCTION: Odorant receptor (Potential). May be involved in taste perception. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in the tongue.; . . 0.17296 0.09548 1.129924507 92.23283793 4691.49759 13.80700 OR5P3 0.615021497256301 0.351267152399287 0.0337113503444123 olfactory receptor family 5 subfamily P member 3 FUNCTION: Odorant receptor (Potential). May be involved in taste perception. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in the tongue.; . . 0.12130 . 0.485092724 79.37603208 277.07039 3.56372 OR5P4P . . . olfactory receptor family 5 subfamily P member 4 pseudogene . . . . . . . . . . . OR5R1 2.18602853058181e-05 0.160489264405262 0.839488875309432 olfactory receptor family 5 subfamily R member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.15302 . 3.33171773 99.42793112 7769.63608 19.00389 OR5S1P . . . olfactory receptor family 5 subfamily S member 1 pseudogene . . . . . . . . . . . OR5T1 0.000130890000678226 0.230740113528662 0.76912899647066 olfactory receptor family 5 subfamily T member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06852 . -0.157884861 42.05590941 59.43898 1.56383 OR5T2 0.0010790748626569 0.37982989576237 0.619091029374973 olfactory receptor family 5 subfamily T member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.17193 . 1.287903524 93.83698986 878.10876 5.77246 OR5T3 1.28424640234906e-05 0.119606743834106 0.88038041370187 olfactory receptor family 5 subfamily T member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09677 0.08393 1.039913547 91.25973107 432.70741 4.34113 OR5V1 0.00344261897900665 0.6162051314672 0.380352249553793 olfactory receptor family 5 subfamily V member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.751474114 86.64779429 3259.42879 10.87476 OR5W1P . . . olfactory receptor family 5 subfamily W member 1 pseudogene . . . . . . . . . . . OR5W2 0.0488123221166674 0.684615691426679 0.266571986456654 olfactory receptor family 5 subfamily W member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05992 0.06923 1.728918179 96.55579146 1839.65934 7.91088 OR6A2 0.267851555384992 0.636442930135331 0.095705514479677 olfactory receptor family 6 subfamily A member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.19207 . 1.021500656 91.01792876 239.6053 3.34484 OR6B1 3.06652361670517e-05 0.341677093981229 0.658292240782604 olfactory receptor family 6 subfamily B member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.174625237 65.9648502 1917.05731 8.05745 OR6B2 0.695947064753924 0.286823056140215 0.0172298791058614 olfactory receptor family 6 subfamily B member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13825 0.09850 1.196071381 92.92285916 4244.11657 12.95689 OR6B3 0.0646108476974636 0.728231678974262 0.207157473328274 olfactory receptor family 6 subfamily B member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06088 0.09957 0.108486928 61.90728946 492.40952 4.56332 OR6C1 0.0123858709297222 0.648701912118391 0.338912216951887 olfactory receptor family 6 subfamily C member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 1.530453833 95.52960604 3896.97889 12.32140 OR6C2 0.658293420139718 0.317756185657838 0.0239503942024432 olfactory receptor family 6 subfamily C member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . unclassifiable (Anatomical System); . . 0.11295 1.218120595 93.15876386 662.72604 5.15932 OR6C3 0.000123119568975691 0.22343112266249 0.776445757768534 olfactory receptor family 6 subfamily C member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.14007 0.10647 0.707379532 85.62750649 1751.17995 7.72547 OR6C4 1.10236491400675e-07 0.0279988216442483 0.97200106811926 olfactory receptor family 6 subfamily C member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03406 . 0.50895761 80.20169851 1677.89767 7.55398 OR6C5P . . . olfactory receptor family 6 subfamily C member 5 pseudogene . . . . . . . . . . . OR6C6 0.0658375506091577 0.730792749606101 0.203369699784742 olfactory receptor family 6 subfamily C member 6 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09997 . 1.728918179 96.55579146 546.83816 4.75415 OR6C7P . . . olfactory receptor family 6 subfamily C member 7 pseudogene . . . . . . . . . . . OR6C64P . . . olfactory receptor family 6 subfamily C member 64 pseudogene . . . . . . . . . . . OR6C65 0.00106148732110602 0.376902082725001 0.622036429953893 olfactory receptor family 6 subfamily C member 65 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.194852702 67.03231894 39.72275 1.17061 OR6C66P . . . olfactory receptor family 6 subfamily C member 66 pseudogene . . . . . . . . . . . OR6C68 0.000123416793775027 0.223715260602837 0.776161322603388 olfactory receptor family 6 subfamily C member 68 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 1.106059595 91.985138 3504.15039 11.41182 OR6C69P . . . olfactory receptor family 6 subfamily C member 69 pseudogene . . . . . . . . . . . OR6C70 1.41010421459543e-05 0.126005266228344 0.87398063272951 olfactory receptor family 6 subfamily C member 70 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.639420866 83.8995046 238.14166 3.33430 OR6C71P . . . olfactory receptor family 6 subfamily C member 71 pseudogene . . . . . . . . . . . OR6C72P . . . olfactory receptor family 6 subfamily C member 72 pseudogene . . . . . . . . . . . OR6C73P . . . olfactory receptor family 6 subfamily C member 73 pseudogene . . . . . . . . . . . OR6C74 0.0780086954370734 0.751407540481278 0.170583764081648 olfactory receptor family 6 subfamily C member 74 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 1.616843854 95.96013211 7801.38315 19.02158 OR6C75 0.0484775642216433 0.683433958113682 0.268088477664674 olfactory receptor family 6 subfamily C member 75 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . -0.071520315 48.34866714 230.34576 3.28009 OR6C76 0.00102177135806382 0.370167046011293 0.628811182630643 olfactory receptor family 6 subfamily C member 76 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.927856124 89.70276008 495.27861 4.57349 OR6D1P . . . olfactory receptor family 6 subfamily D member 1 pseudogene . . . . . . . . . . . OR6E1P . . . olfactory receptor family 6 subfamily E member 1 pseudogene . . . . . . . . . . . OR6F1 0.000152779476135538 0.250123450814563 0.749723769709302 olfactory receptor family 6 subfamily F member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . testis; ciliary ganglion;atrioventricular node; 0.09027 0.08104 0.797386419 87.53833451 583.9975 4.89921 OR6J1 0.40685269362071 0.469471356155525 0.123675950223765 olfactory receptor family 6 subfamily J member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06829 0.07212 . . 5757.63733 15.76157 OR6K1P . . . olfactory receptor family 6 subfamily K member 1 pseudogene . . . . . . . . . . . OR6K2 6.62918854479771e-05 0.288383861640924 0.711549846473628 olfactory receptor family 6 subfamily K member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06550 . 0.486911049 79.46449634 729.70391 5.36289 OR6K3 0.0069063678864482 0.524941295052005 0.468152337061547 olfactory receptor family 6 subfamily K member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10249 0.09681 1.019682101 90.97664544 4283.56654 13.01875 OR6K4P . . . olfactory receptor family 6 subfamily K member 4 pseudogene . . . . . . . . . . . OR6K5P . . . olfactory receptor family 6 subfamily K member 5 pseudogene . . . . . . . . . . . OR6K6 0.0104831042185149 0.61354693086792 0.375969964913565 olfactory receptor family 6 subfamily K member 6 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03874 0.06430 2.686408225 98.87355508 6212.56709 16.47872 OR6L1P . . . olfactory receptor family 6 subfamily L member 1 pseudogene . . . . . . . . . . . OR6L2P . . . olfactory receptor family 6 subfamily L member 2 pseudogene . . . . . . . . . . . OR6M1 0.00196364804612078 0.496006378533623 0.502029973420257 olfactory receptor family 6 subfamily M member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.09049 1.106059595 91.985138 3457.2206 11.29358 OR6M2P . . . olfactory receptor family 6 subfamily M member 2 pseudogene . . . . . . . . . . . OR6M3P . . . olfactory receptor family 6 subfamily M member 3 pseudogene . . . . . . . . . . . OR6N1 0.00123986038668199 0.40517677279443 0.593583366818888 olfactory receptor family 6 subfamily N member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08147 0.08554 1.2860853 93.80160415 1681.62077 7.55904 OR6N2 0.0234399156655135 0.770399510070692 0.206160574263794 olfactory receptor family 6 subfamily N member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06677 0.08246 0.240763792 69.36777542 173.81188 2.87046 OR6P1 . . . olfactory receptor family 6 subfamily P member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06961 0.09055 3.061477042 99.24510498 924.84353 5.90534 OR6Q1 0.00486335445142141 0.690031463499381 0.305105182049198 olfactory receptor family 6 subfamily Q member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03556 . 2.039482001 97.73531493 8733.14093 20.19483 OR6R1P . . . olfactory receptor family 6 subfamily R member 1 pseudogene . . . . . . . . . . . OR6R2P . . . olfactory receptor family 6 subfamily R member 2 pseudogene . . . . . . . . . . . OR6S1 0.000222105368534211 0.302667394928052 0.697110499703414 olfactory receptor family 6 subfamily S member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13466 . 1.420201535 94.92215145 4876.76824 14.19168 OR6T1 7.96194444184611e-05 0.31607314871724 0.683847231838342 olfactory receptor family 6 subfamily T member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06047 . 1.508403067 95.42344893 190.9138 2.99655 OR6U2P . . . olfactory receptor family 6 subfamily U member 2 pseudogene . . . . . . . . . . . OR6V1 0.0764745296511436 0.749238390636333 0.174287079712523 olfactory receptor family 6 subfamily V member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 1.284269037 93.76621845 2037.2887 8.31932 OR6W1P . . . olfactory receptor family 6 subfamily W member 1 pseudogene . . . . . 0.06410 . . . . . OR6X1 0.00034659635921149 0.375893989788664 0.623759413852125 olfactory receptor family 6 subfamily X member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.08714 1.063778722 91.58410002 613.06404 5.00547 OR6Y1 0.0179818972231652 0.7233202205239 0.258697882252935 olfactory receptor family 6 subfamily Y member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.14953 0.08724 1.486352457 95.32908705 2006.35393 8.24902 OR7A1P . . . olfactory receptor family 7 subfamily A member 1 pseudogene . . . . . . . . . . . OR7A2P . . . olfactory receptor family 7 subfamily A member 2 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.14980 . . . . . OR7A3P . . . olfactory receptor family 7 subfamily A member 3 pseudogene . . . . . . . . . . . OR7A5 0.00139716936458155 0.427804156486131 0.570798674149288 olfactory receptor family 7 subfamily A member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03067 . 0.751474114 86.64779429 378.79994 4.10339 OR7A8P . . . olfactory receptor family 7 subfamily A member 8 pseudogene . . . . . . . . . . . OR7A10 0.00799298151690713 0.555798032455026 0.436208986028067 olfactory receptor family 7 subfamily A member 10 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06006 . 1.241986644 93.38877094 2606.77431 9.55666 OR7A11P . . . olfactory receptor family 7 subfamily A member 11 pseudogene . . . . . . . . . . . OR7A15P . . . olfactory receptor family 7 subfamily A member 15 pseudogene . . . . . . . . . . . OR7A17 0.000117083033671137 0.217577672181651 0.782305244784678 olfactory receptor family 7 subfamily A member 17 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05617 . 0.973768544 90.33970276 5166.56719 14.79080 OR7A18P . . . olfactory receptor family 7 subfamily A member 18 pseudogene . . . . . . . . . . . OR7A19P . . . olfactory receptor family 7 subfamily A member 19 pseudogene . . . . . . . . . . . OR7C1 0.220027090245229 0.647565890605505 0.132407019149266 olfactory receptor family 7 subfamily C member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04419 . 1.68481378 96.37886294 1256.02466 6.68179 OR7C2 0.0424490324584504 0.659798785638134 0.297752181903416 olfactory receptor family 7 subfamily C member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06353 0.09697 0.597144447 82.7435716 391.7792 4.16495 OR7D1P . . . olfactory receptor family 7 subfamily D member 1 pseudogene . . . . . . . . . . . OR7D2 0.0925271219188337 0.767080495274743 0.140392382806424 olfactory receptor family 7 subfamily D member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.12848 0.09473 -0.203796826 38.81811748 142.40142 2.60320 OR7D4 8.94371114921136e-06 0.0976185268001864 0.902372529488664 olfactory receptor family 7 subfamily D member 4 FUNCTION: Odorant receptor. Selectively activated by androstenone and the related odorous steroid androstadienone.; . TISSUE SPECIFICITY: Nasal olfactory epithelium. {ECO:0000269|PubMed:17509148}.; thyroid; . 0.12581 0.08118 0.553050905 81.54635527 1688.91918 7.57679 OR7D11P . . . olfactory receptor family 7 subfamily D member 11 pseudogene . . . . . . . . . . . OR7E1P . . . olfactory receptor family 7 subfamily E member 1 pseudogene . . . . . . . . . . . OR7E2P . . . olfactory receptor family 7 subfamily E member 2 pseudogene . . . . . . . . . . . OR7E4P . . . olfactory receptor family 7 subfamily E member 4 pseudogene . . . . . . . . . . . OR7E5P . . . olfactory receptor family 7 subfamily E member 5 pseudogene . . . . . 0.07804 . . . . . OR7E7P . . . olfactory receptor family 7 subfamily E member 7 pseudogene . . . . . . . . . . . OR7E8P . . . olfactory receptor family 7 subfamily E member 8 pseudogene . . . . . . . . . . . OR7E10P . . . olfactory receptor family 7 subfamily E member 10 pseudogene . . . . . . . . . . . OR7E11P . . . olfactory receptor family 7 subfamily E member 11 pseudogene . . . . . . . . . . . OR7E12P . . . olfactory receptor family 7 subfamily E member 12 pseudogene . . . . . . . . . . . OR7E13P . . . olfactory receptor family 7 subfamily E member 13 pseudogene . . . . . . . . . . . OR7E14P . . . olfactory receptor family 7 subfamily E member 14 pseudogene . . . . . . . . . . . OR7E15P . . . olfactory receptor family 7 subfamily E member 15 pseudogene . . . . . . . . . . . OR7E16P . . . olfactory receptor family 7 subfamily E member 16 pseudogene . . . . . . . . . . . OR7E18P . . . olfactory receptor family 7 subfamily E member 18 pseudogene . . . . . . . . . . . OR7E19P . . . olfactory receptor family 7 subfamily E member 19 pseudogene . . . . . . . . . . . OR7E21P . . . olfactory receptor family 7 subfamily E member 21 pseudogene . . . . . . . . . . . OR7E22P . . . olfactory receptor family 7 subfamily E member 22 pseudogene . . . . . . . . . . . OR7E23P . . . olfactory receptor family 7 subfamily E member 23 pseudogene . . . . . . . . . . . OR7E24 0.298717571187412 0.623457380476641 0.0778250483359469 olfactory receptor family 7 subfamily E member 24 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.15381 . 0.040529541 57.15380986 622.4966 5.03227 OR7E25P . . . olfactory receptor family 7 subfamily E member 25 pseudogene . . . unclassifiable (Anatomical System);testis; . 0.15381 . . . . . OR7E26P . . . olfactory receptor family 7 subfamily E member 26 pseudogene . . . . . . . . . . . OR7E28P . . . olfactory receptor family 7 subfamily E member 28 pseudogene . . . . . . . . . . . OR7E29P . . . olfactory receptor family 7 subfamily E member 29 pseudogene . . . . . . . . . . . OR7E31P . . . olfactory receptor family 7 subfamily E member 31 pseudogene . . . . . . . . . . . OR7E33P . . . olfactory receptor family 7 subfamily E member 33 pseudogene . . . . . . . . . . . OR7E35P . . . olfactory receptor family 7 subfamily E member 35 pseudogene . . . . . . . . . . . OR7E36P . . . olfactory receptor family 7 subfamily E member 36 pseudogene . . . . . . . . . . . OR7E37P . . . olfactory receptor family 7 subfamily E member 37 pseudogene . . . . . . . . . . . OR7E38P . . . olfactory receptor family 7 subfamily E member 38 pseudogene . . . . . . . . . . . OR7E39P . . . olfactory receptor family 7 subfamily E member 39 pseudogene . . . . . . . . . . . OR7E41P . . . olfactory receptor family 7 subfamily E member 41 pseudogene . . . . . . . . . . . OR7E43P . . . olfactory receptor family 7 subfamily E member 43 pseudogene . . . . . . . . . . . OR7E46P . . . olfactory receptor family 7 subfamily E member 46 pseudogene . . . . . . . . . . . OR7E47P . . . olfactory receptor family 7 subfamily E member 47 pseudogene . . . . . . . . . . . OR7E53P . . . olfactory receptor family 7 subfamily E member 53 pseudogene . . . . . . . . . . . OR7E55P . . . olfactory receptor family 7 subfamily E member 55 pseudogene . . . . . . . . . . . OR7E59P . . . olfactory receptor family 7 subfamily E member 59 pseudogene . . . . . . . . . . . OR7E62P . . . olfactory receptor family 7 subfamily E member 62 pseudogene . . . . . . . . . . . OR7E66P . . . olfactory receptor family 7 subfamily E member 66 pseudogene . . . . . . . . . . . OR7E83P . . . olfactory receptor family 7 subfamily E member 83 pseudogene . . . . . . . . . . . OR7E84P . . . olfactory receptor family 7 subfamily E member 84 pseudogene . . . . . . . . . . . OR7E85P . . . olfactory receptor family 7 subfamily E member 85 pseudogene . . . . . 0.09351 . . . . . OR7E86P . . . olfactory receptor family 7 subfamily E member 86 pseudogene . . . . . . . . . . . OR7E87P . . . olfactory receptor family 7 subfamily E member 87 pseudogene . . . . . . . . . . . OR7E89P . . . olfactory receptor family 7 subfamily E member 89 pseudogene . . . . . . . . . . . OR7E90P . . . olfactory receptor family 7 subfamily E member 90 pseudogene . . . . . . . . . . . OR7E91P . . . olfactory receptor family 7 subfamily E member 91 pseudogene . . . . . 0.10504 . . . . . OR7E93P . . . olfactory receptor family 7 subfamily E member 93 pseudogene . . . . . . . . . . . OR7E94P . . . olfactory receptor family 7 subfamily E member 94 pseudogene . . . . . . . . . . . OR7E96P . . . olfactory receptor family 7 subfamily E member 96 pseudogene . . . . . . . . . . . OR7E97P . . . olfactory receptor family 7 subfamily E member 97 pseudogene . . . . . . . . . . . OR7E99P . . . olfactory receptor family 7 subfamily E member 99 pseudogene . . . . . . . . . . . OR7E100P . . . olfactory receptor family 7 subfamily E member 100 pseudogene . . . . . . . . . . . OR7E101P . . . olfactory receptor family 7 subfamily E member 101 pseudogene . . . . . . . . . . . OR7E102P . . . olfactory receptor family 7 subfamily E member 102 pseudogene . . . . . . . . . . . OR7E104P . . . olfactory receptor family 7 subfamily E member 104 pseudogene . . . . . . . . . . . OR7E105P . . . olfactory receptor family 7 subfamily E member 105 pseudogene . . . . . . . . . . . OR7E106P . . . olfactory receptor family 7 subfamily E member 106 pseudogene . . . . . . . . . . . OR7E108P . . . olfactory receptor family 7 subfamily E member 108 pseudogene . . . . . . . . . . . OR7E109P . . . olfactory receptor family 7 subfamily E member 109 pseudogene . . . . . . . . . . . OR7E110P . . . olfactory receptor family 7 subfamily E member 110 pseudogene . . . . . . . . . . . OR7E111P . . . olfactory receptor family 7 subfamily E member 111 pseudogene . . . . . . . . . . . OR7E115P . . . olfactory receptor family 7 subfamily E member 115 pseudogene . . . . . . . . . . . OR7E116P . . . olfactory receptor family 7 subfamily E member 116 pseudogene . . . . . . . . . . . OR7E117P . . . olfactory receptor family 7 subfamily E member 117 pseudogene . . . . . . . . . . . OR7E121P . . . olfactory receptor family 7 subfamily E member 121 pseudogene . . . . . . . . . . . OR7E122P . . . olfactory receptor family 7 subfamily E member 122 pseudogene . . . . . . . . . . . OR7E125P . . . olfactory receptor family 7 subfamily E member 125 pseudogene . . . heart; . . . . . . . OR7E126P . . . olfactory receptor family 7 subfamily E member 126 pseudogene . . . . . . . . . . . OR7E128P . . . olfactory receptor family 7 subfamily E member 128 pseudogene . . . . . . . . . . . OR7E129P . . . olfactory receptor family 7 subfamily E member 129 pseudogene . . . . . 0.09351 . . . . . OR7E130P . . . olfactory receptor family 7 subfamily E member 130 pseudogene . . . . . . . . . . . OR7E136P . . . olfactory receptor family 7 subfamily E member 136 pseudogene . . . . . . . . . . . OR7E140P . . . olfactory receptor family 7 subfamily E member 140 pseudogene . . . . . . . . . . . OR7E145P . . . olfactory receptor family 7 subfamily E member 145 pseudogene . . . . . . . . . . . OR7E148P . . . olfactory receptor family 7 subfamily E member 148 pseudogene . . . . . . . . . . . OR7E149P . . . olfactory receptor family 7 subfamily E member 149 pseudogene . . . . . . . . . . . OR7E154P . . . olfactory receptor family 7 subfamily E member 154 pseudogene . . . unclassifiable (Anatomical System);ovary;heart; . . . . . . . OR7E155P . . . olfactory receptor family 7 subfamily E member 155 pseudogene . . . . . . . . . . . OR7E156P . . . olfactory receptor family 7 subfamily E member 156 pseudogene . . . . . . . . . . . OR7E157P . . . olfactory receptor family 7 subfamily E member 157 pseudogene . . . . . . . . . . . OR7E158P . . . olfactory receptor family 7 subfamily E member 158 pseudogene . . . . . . . . . . . OR7E159P . . . olfactory receptor family 7 subfamily E member 159 pseudogene . . . . . . . . . . . OR7E160P . . . olfactory receptor family 7 subfamily E member 160 pseudogene . . . . . . . . . . . OR7E161P . . . olfactory receptor family 7 subfamily E member 161 pseudogene . . . blood; . . . . . . . OR7E162P . . . olfactory receptor family 7 subfamily E member 162 pseudogene . . . . . . . . . . . OR7E163P . . . olfactory receptor family 7 subfamily E member 163 pseudogene . . . . . . . . . . . OR7G1 0.0757166763743766 0.748125210290128 0.176158113335496 olfactory receptor family 7 subfamily G member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06744 . 1.638895725 96.11347016 5464.52834 15.22686 OR7G2 0.00709376609761956 0.530564101874821 0.462342132027559 olfactory receptor family 7 subfamily G member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.02448 . 1.129924507 92.23283793 428.91516 4.32547 OR7G3 0.405963699611883 0.556113052380355 0.037923248007762 olfactory receptor family 7 subfamily G member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06601 . 1.26221942 93.55980184 5002.40642 14.44369 OR7G15P . . . olfactory receptor family 7 subfamily G member 15 pseudogene . . . . . . . . . . . OR7H1P . . . olfactory receptor family 7 subfamily H member 1 pseudogene . . . . . . . . . . . OR7H2P . . . olfactory receptor family 7 subfamily H member 2 pseudogene . . . . . . . . . . . OR7K1P . . . olfactory receptor family 7 subfamily K member 1 pseudogene . . . . . . . . . . . OR7L1P . . . olfactory receptor family 7 subfamily L member 1 pseudogene . . . . . . . . . . . OR7M1P . . . olfactory receptor family 7 subfamily M member 1 pseudogene . . . . . . . . . . . OR8A1 0.058828646142404 0.714727181823896 0.2264441720337 olfactory receptor family 8 subfamily A member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . lung;placenta;testis; . 0.07708 0.09311 1.374284246 94.51521585 3304.70284 10.97088 OR8A2P . . . olfactory receptor family 8 subfamily A member 2 pseudogene . . . . . . . . . . . OR8A3P . . . olfactory receptor family 8 subfamily A member 3 pseudogene . . . . . . . . . . . OR8B1P . . . olfactory receptor family 8 subfamily B member 1 pseudogene . . . . . . . . . . . OR8B2 0.205712840071851 0.648138811766819 0.14614834816133 olfactory receptor family 8 subfamily B member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08605 . 0.483275131 79.25218212 2804.16977 9.99734 OR8B3 0.618283247505984 0.348824361609536 0.0328923908844799 olfactory receptor family 8 subfamily B member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . lung;testis; . 0.06909 0.08394 0.284856336 71.40835103 358.87056 4.01239 OR8B4 0.707743835067628 0.276829096184305 0.0154270687480679 olfactory receptor family 8 subfamily B member 4 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13208 0.08318 0.573279816 82.08303845 9093.4222 20.68608 OR8B5P . . . olfactory receptor family 8 subfamily B member 5 pseudogene . . . . . . . . . . . OR8B6P . . . olfactory receptor family 8 subfamily B member 6 pseudogene . . . . . . . . . . . OR8B7P . . . olfactory receptor family 8 subfamily B member 7 pseudogene . . . . . . . . . . . OR8B8 0.00555520538174593 0.479958664998398 0.514486129619856 olfactory receptor family 8 subfamily B member 8 FUNCTION: Odorant receptor (Potential). May be involved in taste perception. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in the tongue and testis.; . . 0.08971 0.09325 0.440999548 77.79547063 118.92462 2.37248 OR8B9P . . . olfactory receptor family 8 subfamily B member 9 pseudogene . . . . . . . . . . . OR8B10P . . . olfactory receptor family 8 subfamily B member 10 pseudogene . . . . . . . . . . . OR8B12 0.178075255695636 0.644551407273955 0.177373337030409 olfactory receptor family 8 subfamily B member 12 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.12278 0.09030 0.306902668 72.38145789 677.93116 5.20252 OR8C1P . . . olfactory receptor family 8 subfamily C member 1 pseudogene . . . . . . . . . . . OR8D1 0.215921298613233 0.647880602903584 0.136198098483183 olfactory receptor family 8 subfamily D member 1 FUNCTION: Odorant receptor (Potential). May be involved in taste perception. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in the tongue.; . . 0.06284 0.08809 1.24016994 93.34748762 6107.80716 16.33313 OR8D2 0.616576837370082 0.35010410187564 0.0333190607542789 olfactory receptor family 8 subfamily D member 2 (gene/pseudogene) FUNCTION: Odorant receptor (Potential). May be involved in taste perception. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in the tongue.; . . 0.05768 . 0.617373774 83.25076669 5053.17595 14.55000 OR8D4 0.0504863379478631 0.690338377009959 0.259175285042177 olfactory receptor family 8 subfamily D member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . skeletal muscle; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.03701 0.07683 2.862900621 99.12715263 6924.05567 17.72811 OR8F1P . . . olfactory receptor family 8 subfamily F member 1 pseudogene . . . . . . . . . . . OR8G1 0.285950158784041 0.629287326852309 0.0847625143636506 olfactory receptor family 8 subfamily G member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08665 . . . . . OR8G2 . . . olfactory receptor family 8 subfamily G member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04416 . . . . . OR8G3P . . . olfactory receptor family 8 subfamily G member 3 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR8G5 0.652742658849299 0.322183030972474 0.025074310178227 olfactory receptor family 8 subfamily G member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . 7840.90509 19.09307 OR8G7P . . . olfactory receptor family 8 subfamily G member 7 pseudogene . . . . . . . . . . . OR8H1 1.46607275128529e-05 0.128762572922252 0.871222766350235 olfactory receptor family 8 subfamily H member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07846 0.09152 1.15197334 92.52182118 276.94956 3.56220 OR8H2 0.000858971946429471 0.340573478740903 0.658567549312667 olfactory receptor family 8 subfamily H member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08538 0.08065 2.864716199 99.13305025 1348.78414 6.89373 OR8H3 7.94648072869994e-07 0.0461917940288714 0.953807411323056 olfactory receptor family 8 subfamily H member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09125 0.08415 2.263666797 98.22481717 1294.03828 6.77060 OR8I1P . . . olfactory receptor family 8 subfamily I member 1 pseudogene . . . . . . . . . . . OR8I2 0.000129181427224364 0.229153838542186 0.770716980030589 olfactory receptor family 8 subfamily I member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.01952 0.08329 1.508403067 95.42344893 1227.75264 6.62425 OR8I4P . . . olfactory receptor family 8 subfamily I member 4 pseudogene . . . . . . . . . . . OR8J1 4.47462093270338e-06 0.123571509341245 0.876424016037822 olfactory receptor family 8 subfamily J member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10042 0.07773 1.197888504 92.95234725 1872.29205 7.95780 OR8J2 . . . olfactory receptor family 8 subfamily J member 2 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR8J3 0.0655570233337098 0.730215835800835 0.204227140865455 olfactory receptor family 8 subfamily J member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07259 0.08651 1.462485515 95.2111347 2248.19968 8.75683 OR8K1 0.00203916386705507 0.503859413649203 0.494101422483742 olfactory receptor family 8 subfamily K member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09676 0.09084 1.752786166 96.68553904 4622.84814 13.67045 OR8K2P . . . olfactory receptor family 8 subfamily K member 2 pseudogene . . . . . . . . . . . OR8K3 4.46100866088346e-06 0.225882288090676 0.774113250900664 olfactory receptor family 8 subfamily K member 3 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08613 0.08960 0.308721233 72.59966973 196.92571 3.03479 OR8K4P . . . olfactory receptor family 8 subfamily K member 4 pseudogene . . . . . . . . . . . OR8K5 4.10692348788277e-07 0.0599616781685604 0.940037911139091 olfactory receptor family 8 subfamily K member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.16118 . 0.995816767 90.62278839 842.54719 5.68197 OR8L1P . . . olfactory receptor family 8 subfamily L member 1 pseudogene . . . . . . . . . . . OR8Q1P . . . olfactory receptor family 8 subfamily Q member 1 pseudogene . . . . . . . . . . . OR8R1P . . . olfactory receptor family 8 subfamily R member 1 pseudogene . . . . . . . . . . . OR8S1 3.08155201788778e-06 0.10025696505614 0.899739953391842 olfactory receptor family 8 subfamily S member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04627 0.05223 1.730733976 96.56758669 4340.63383 13.12232 OR8S21P . . . olfactory receptor family 8 subfamily S member 21 pseudogene . . . . . . . . . . . OR8T1P . . . olfactory receptor family 8 subfamily T member 1 pseudogene . . . . . . . . . . . OR8U1 0.0134541405146474 0.665847853867636 0.320698005617717 olfactory receptor family 8 subfamily U member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 1.907156687 97.38145789 2268.30969 8.80885 OR8U8 . . . olfactory receptor family 8 subfamily U member 8 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR8U9 . . . olfactory receptor family 8 subfamily U member 9 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR8V1P . . . olfactory receptor family 8 subfamily V member 1 pseudogene . . . . . . . . . . . OR8X1P . . . olfactory receptor family 8 subfamily X member 1 pseudogene . . . . . . . . . . . OR9A1P . . . olfactory receptor family 9 subfamily A member 1 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR9A2 8.86431291599995e-05 0.333226863735568 0.666684493135272 olfactory receptor family 9 subfamily A member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09283 0.09500 0.751474114 86.64779429 616.13038 5.01250 OR9A3P . . . olfactory receptor family 9 subfamily A member 3 pseudogene . . . . . . . . . . . OR9A4 0.000344414708783223 0.374773940200244 0.624881645090972 olfactory receptor family 9 subfamily A member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.128714042 63.19886766 135.73189 2.53340 OR9G1 0.00099531584115889 0.365582069751775 0.633422614407067 olfactory receptor family 9 subfamily G member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.09296 1.241986644 93.38877094 1973.00729 8.18276 OR9G2P . . . olfactory receptor family 9 subfamily G member 2 pseudogene . . . . . . . . . . . OR9G3P . . . olfactory receptor family 9 subfamily G member 3 pseudogene . . . . . . . . . . . OR9G4 0.000306987549777873 0.354770626030247 0.644922386419975 olfactory receptor family 9 subfamily G member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07854 0.08913 -0.023789244 52.09365416 2091.30541 8.42464 OR9G9 . . . olfactory receptor family 9 subfamily G member 9 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.09296 . . . . OR9H1P . . . olfactory receptor family 9 subfamily H member 1 pseudogene . . . . . . . . . . . OR9I1 0.612331301435911 0.353271132349334 0.0343975662147542 olfactory receptor family 9 subfamily I member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06279 0.09587 0.306902668 72.38145789 52.0836 1.42629 OR9I2P . . . olfactory receptor family 9 subfamily I member 2 pseudogene . . . . . . . . . . . OR9I3P . . . olfactory receptor family 9 subfamily I member 3 pseudogene . . . . . . . . . . . OR9K1P . . . olfactory receptor family 9 subfamily K member 1 pseudogene . . . . . . . . . . . OR9K2 9.7525214366511e-05 0.197409133043041 0.802493341742592 olfactory receptor family 9 subfamily K member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.16409 . 0.729426781 86.17008728 8169.48118 19.50880 OR9L1P . . . olfactory receptor family 9 subfamily L member 1 pseudogene . . . . . . . . . . . OR9M1P . . . olfactory receptor family 9 subfamily M member 1 pseudogene . . . . . . . . . . . OR9N1P . . . olfactory receptor family 9 subfamily N member 1 pseudogene . . . . . . . . . . . OR9P1P . . . olfactory receptor family 9 subfamily P member 1 pseudogene . . . . . . . . . . . OR9Q1 0.00859489705714355 0.571243280996574 0.420161821946282 olfactory receptor family 9 subfamily Q member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04867 0.08183 0.531004228 80.87992451 186.32302 2.96436 OR9Q2 1.29909599868149e-07 0.0586595634428623 0.941340306647538 olfactory receptor family 9 subfamily Q member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04920 0.08208 -0.071520315 48.34866714 2455.49367 9.22109 OR9R1P . . . olfactory receptor family 9 subfamily R member 1 pseudogene . . . . . . . . . . . OR9S24P . . . olfactory receptor family 9 subfamily S member 24 pseudogene . . . . . . . . . . . OR10A2 0.000920372164321628 0.352136045976689 0.646943581858989 olfactory receptor family 10 subfamily A member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.21490 . 0.753291803 86.71266808 8490.86892 19.90294 OR10A3 4.36193036936385e-09 0.0298280066540189 0.970171988984051 olfactory receptor family 10 subfamily A member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 0.729426781 86.17008728 136.21904 2.53659 OR10A4 2.78490991495933e-05 0.183051126339016 0.816921024561835 olfactory receptor family 10 subfamily A member 4 FUNCTION: Odorant receptor (Potential). May be involved in taste perception. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in the tongue.; . . 0.31527 0.16928 2.019241996 97.71172446 4842.41101 14.12803 OR10A5 0.00842213119189341 0.566918986184764 0.424658882623343 olfactory receptor family 10 subfamily A member 5 FUNCTION: Odorant receptor (Potential). May be involved in taste perception. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in the tongue.; . . 0.22394 . 2.19749864 98.11866006 565.77518 4.83181 OR10A6 8.59245281840639e-09 0.0442101165272871 0.95578987488026 olfactory receptor family 10 subfamily A member 6 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . placenta; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.09966 0.09149 0.909442382 89.49634348 5206.43979 14.86504 OR10A7 0.268100024278158 0.636354232644919 0.0955457430769234 olfactory receptor family 10 subfamily A member 7 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.09069 0.619191319 83.36282142 278.69851 3.57837 OR10AA1P . . . olfactory receptor family 10 subfamily AA member 1 pseudogene . . . . . . . . . . . OR10AB1P . . . olfactory receptor family 10 subfamily AB member 1 pseudogene . . . unclassifiable (Anatomical System); . . . . . . . OR10AC1 . . . olfactory receptor family 10 subfamily AC member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000250}.; . . . . . . . . . . OR10AD1 0.00351676157654617 0.620822373806952 0.375660864616502 olfactory receptor family 10 subfamily AD member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . uterus;brain;skeletal muscle; . 0.16737 . 1.550689283 95.62396792 4408.04892 13.27065 OR10AE1P . . . olfactory receptor family 10 subfamily AE member 1 pseudogene . . . . . . . . . . . OR10AE3P . . . olfactory receptor family 10 subfamily AE member 3 pseudogene . . . . . . . . . . . OR10AF1P . . . olfactory receptor family 10 subfamily AF member 1 pseudogene . . . . . . . . . . . OR10AG1 0.000135734106384808 0.235176430629609 0.764687835264007 olfactory receptor family 10 subfamily AG member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07631 . 1.68481378 96.37886294 264.33118 3.48870 OR10AH1P . . . olfactory receptor family 10 subfamily AH member 1 pseudogene . . . . . . . . . . . OR10AK1P . . . olfactory receptor family 10 subfamily AK member 1 pseudogene . . . . . . . . . . . OR10B1P . . . olfactory receptor family 10 subfamily B member 1 pseudogene . . . . . . . . . . . OR10C1 0.227592079399406 0.646689488367273 0.12571843223332 olfactory receptor family 10 subfamily C member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03156 . 3.708735068 99.56947393 3414.90468 11.21063 OR10D1P . . . olfactory receptor family 10 subfamily D member 1 pseudogene . . . . . . . . . . . OR10D3 . . . olfactory receptor family 10 subfamily D member 3 (putative) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . 10270.53772 22.08539 OR10D4P . . . olfactory receptor family 10 subfamily D member 4 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.12822 . . . . . OR10D5P . . . olfactory receptor family 10 subfamily D member 5 pseudogene . . . . . . . . . . . OR10G1P . . . olfactory receptor family 10 subfamily G member 1 pseudogene . . . . . . . . . . . OR10G2 0.0460936473447754 0.674638866121624 0.2792674865336 olfactory receptor family 10 subfamily G member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13624 0.09458 1.886919751 97.29299363 7031.45496 17.88897 OR10G3 0.234560474406909 0.645560256808772 0.119879268784318 olfactory receptor family 10 subfamily G member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.12713 0.09782 1.174022298 92.72823779 733.81635 5.37359 OR10G4 0.216924072224088 0.647814526967306 0.135261400808606 olfactory receptor family 10 subfamily G member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10362 0.09649 2.309597117 98.34866714 10402.74701 22.26866 OR10G5P . . . olfactory receptor family 10 subfamily G member 5 pseudogene . . . . . . . . . . . OR10G6 . . . olfactory receptor family 10 subfamily G member 6 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.14447 . . . 268.93852 3.51755 OR10G7 0.00712210899720655 0.531402926447936 0.461474964554857 olfactory receptor family 10 subfamily G member 7 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06744 0.08917 1.774838537 96.82118424 459.74042 4.44864 OR10G8 0.636591633450699 0.33485471639471 0.0285536501545908 olfactory receptor family 10 subfamily G member 8 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06440 0.08304 0.797386419 87.53833451 1290.49257 6.76216 OR10G9 0.00713845173418904 0.531885237280803 0.460976310985008 olfactory receptor family 10 subfamily G member 9 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05817 0.09497 3.688480395 99.5576787 1919.79326 8.06598 OR10H1 0.637065115563279 0.334487775331887 0.0284471091048344 olfactory receptor family 10 subfamily H member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . unclassifiable (Anatomical System); . 0.15432 0.09500 0.575097644 82.1656051 2707.23222 9.78935 OR10H2 0.00763643549782811 0.546121608042627 0.446241956459545 olfactory receptor family 10 subfamily H member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . unclassifiable (Anatomical System); superior cervical ganglion;temporal lobe;atrioventricular node;trigeminal ganglion;parietal lobe; 0.12728 0.10763 0.643056625 84.05284265 4473.34923 13.41447 OR10H3 0.00545455982092705 0.476252805770147 0.518292634408926 olfactory receptor family 10 subfamily H member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03086 0.08278 1.418384579 94.89266336 5310.16335 15.05995 OR10H4 0.000560233320852483 0.275254899684407 0.72418486699474 olfactory receptor family 10 subfamily H member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04487 0.08772 1.019682101 90.97664544 2390.88939 9.07509 OR10H5 0.0439530042449772 0.666138750762936 0.289908244992087 olfactory receptor family 10 subfamily H member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05526 0.09533 1.910792163 97.4168436 5294.08243 15.03864 OR10J1 1.59229720392064e-08 0.017323565852277 0.982676418224751 olfactory receptor family 10 subfamily J member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.11524 . 1.129924507 92.23283793 1835.21965 7.89718 OR10J2P . . . olfactory receptor family 10 subfamily J member 2 pseudogene . . . . . . . . . . . OR10J3 0.00103942838422063 0.373182835725917 0.625777735889862 olfactory receptor family 10 subfamily J member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04060 . 0.308721233 72.59966973 992.93356 6.07198 OR10J4 . . . olfactory receptor family 10 subfamily J member 4 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR10J5 0.723391071464347 0.263368102220756 0.0132408263148963 olfactory receptor family 10 subfamily J member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.30428 . -0.22584292 37.32012267 67.49878 1.70027 OR10J6P . . . olfactory receptor family 10 subfamily J member 6 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03845 . . . . . OR10J7P . . . olfactory receptor family 10 subfamily J member 7 pseudogene . . . . . . . . . . . OR10J8P . . . olfactory receptor family 10 subfamily J member 8 pseudogene . . . . . . . . . . . OR10J9P . . . olfactory receptor family 10 subfamily J member 9 pseudogene . . . . . . . . . . . OR10K1 0.0130991891900967 0.660334072816591 0.326566737993312 olfactory receptor family 10 subfamily K member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05794 . 0.663285274 84.55414013 467.43558 4.47967 OR10K2 8.0533546777969e-05 0.17807676307355 0.821842703379672 olfactory receptor family 10 subfamily K member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07463 . 1.618658506 95.99551781 328.43592 3.85313 OR10N1P . . . olfactory receptor family 10 subfamily N member 1 pseudogene . . . . . . . . . . . OR10P1 0.0192350794042469 0.7358700696154 0.244894850980353 olfactory receptor family 10 subfamily P member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.21437 0.10335 0.464864541 78.69190847 1307.06382 6.80026 OR10Q1 0.254569448021136 0.640763742236328 0.104666809742536 olfactory receptor family 10 subfamily Q member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07668 0.07570 0.64123826 83.97617363 2199.79696 8.63514 OR10Q2P . . . olfactory receptor family 10 subfamily Q member 2 pseudogene . . . . . . . . . . . OR10R1P . . . olfactory receptor family 10 subfamily R member 1 pseudogene . . . . . . . . . . . OR10R2 0.0443756510558884 0.667864544208507 0.287759804735605 olfactory receptor family 10 subfamily R member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.14974 0.09467 1.840996754 97.08657702 10099.65241 21.90954 OR10R3P . . . olfactory receptor family 10 subfamily R member 3 pseudogene . . . . . 0.13304 . . . . . OR10S1 0.00188929864169299 0.488026831581824 0.510083869776483 olfactory receptor family 10 subfamily S member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06145 . 0.907624513 89.46685539 3679.90391 11.80062 OR10T1P . . . olfactory receptor family 10 subfamily T member 1 pseudogene . . . . . . . . . . . OR10T2 0.0631105268901614 0.724960969166777 0.211928503943061 olfactory receptor family 10 subfamily T member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.16058 . 2.065168262 97.79429111 5428.19223 15.19737 OR10U1P . . . olfactory receptor family 10 subfamily U member 1 pseudogene . . . . . . . . . . . OR10V1 0.00168146463399745 0.464289284023819 0.534029251342183 olfactory receptor family 10 subfamily V member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08090 . 1.15197334 92.52182118 1741.67257 7.70448 OR10V2P . . . olfactory receptor family 10 subfamily V member 2 pseudogene . . . . . . . . . . . OR10V3P . . . olfactory receptor family 10 subfamily V member 3 pseudogene . . . . . . . . . . . OR10V7P . . . olfactory receptor family 10 subfamily V member 7 pseudogene . . . . . . . . . . . OR10W1 0.0473260213246962 0.679270148627569 0.273403830047735 olfactory receptor family 10 subfamily W member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07543 0.07846 1.150157577 92.46874263 1071.57724 6.27529 OR10X1 0.00590274236426999 0.492345311835715 0.501751945800015 olfactory receptor family 10 subfamily X member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08571 . 1.510221359 95.4470394 681.57373 5.21799 OR10Y1P . . . olfactory receptor family 10 subfamily Y member 1 pseudogene . . . . . . . . . . . OR10Z1 0.00736423007934796 0.53844840670515 0.454187363215502 olfactory receptor family 10 subfamily Z member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09959 . 0.729426781 86.17008728 1805.03731 7.84143 OR11A1 0.0434844025575059 0.664197042078463 0.292318555364031 olfactory receptor family 11 subfamily A member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.16540 . 0.483275131 79.25218212 1063.16218 6.25743 OR11G1P . . . olfactory receptor family 11 subfamily G member 1 pseudogene . . . . . . . . . . . OR11G2 0.000228689713102011 0.307115351252079 0.692655959034819 olfactory receptor family 11 subfamily G member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 1.196071381 92.92285916 9479.23527 21.06633 OR11H1 0.769596446937656 0.222380256120757 0.00802329694158618 olfactory receptor family 11 subfamily H member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.15451 . . . 2284.58829 8.84104 OR11H2 . . . olfactory receptor family 11 subfamily H member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR11H3P . . . olfactory receptor family 11 subfamily H member 3 pseudogene . . . . . . . . . . . OR11H4 6.22542213030787e-05 0.27934185048653 0.720595895292167 olfactory receptor family 11 subfamily H member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07071 . 1.063778722 91.58410002 409.89856 4.24388 OR11H5P . . . olfactory receptor family 11 subfamily H member 5 pseudogene . . . . . . . . . . . OR11H6 0.0210491564058505 0.752064458465758 0.226886385128391 olfactory receptor family 11 subfamily H member 6 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08481 . 2.019241996 97.71172446 8513.14465 19.96858 OR11H7 . . . olfactory receptor family 11 subfamily H member 7 (gene/pseudogene) FUNCTION: Odorant receptor. Activated by isovaleric acid. {ECO:0000269|PubMed:17973576}.; . . . . 0.07923 . . . . . OR11H12 0.798398679764048 0.196005182043499 0.00559613819245291 olfactory receptor family 11 subfamily H member 12 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . 4405.8371 13.26123 OR11H13P . . . olfactory receptor family 11 subfamily H member 13 pseudogene . . . . . . . . . . . OR11I1P . . . olfactory receptor family 11 subfamily I member 1 pseudogene . . . . . . . . . . . OR11J1P . . . olfactory receptor family 11 subfamily J member 1 pseudogene . . . . . . . . . . . OR11J2P . . . olfactory receptor family 11 subfamily J member 2 pseudogene . . . . . . . . . . . OR11J5P . . . olfactory receptor family 11 subfamily J member 5 pseudogene . . . . . . . . . . . OR11J6P . . . olfactory receptor family 11 subfamily J member 6 pseudogene . . . . . . . . . . . OR11J7P . . . olfactory receptor family 11 subfamily J member 7 pseudogene . . . . . . . . . . . OR11K1P . . . olfactory receptor family 11 subfamily K member 1 pseudogene . . . . . . . . . . . OR11K2P . . . olfactory receptor family 11 subfamily K member 2 pseudogene . . . . . . . . . . . OR11L1 0.0194798581395402 0.738184807539006 0.242335334321453 olfactory receptor family 11 subfamily L member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07130 . 1.019682101 90.97664544 55.19603 1.49091 OR11M1P . . . olfactory receptor family 11 subfamily M member 1 pseudogene . . . . . . . . . . . OR11N1P . . . olfactory receptor family 11 subfamily N member 1 pseudogene . . . . . . . . . . . OR11P1P . . . olfactory receptor family 11 subfamily P member 1 pseudogene . . . . . . . . . . . OR11Q1P . . . olfactory receptor family 11 subfamily Q member 1 pseudogene . . . . . . . . . . . OR12D1 . . . olfactory receptor family 12 subfamily D member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR12D2 0.601033125257784 0.361579013281779 0.0373878614604366 olfactory receptor family 12 subfamily D member 2 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.02358 . 3.105608558 99.25690021 5578.30294 15.43913 OR12D3 1.34136303903671e-05 0.122545946687898 0.877440639681712 olfactory receptor family 12 subfamily D member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.09385 0.21689899 68.12927577 438.87138 4.36715 OR13A1 0.000212216731545614 0.295834024354584 0.70395375891387 olfactory receptor family 13 subfamily A member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.14904 . 0.376678994 75.50719509 1990.19012 8.21797 OR13C1P . . . olfactory receptor family 13 subfamily C member 1 pseudogene . . . . . . . . . . . OR13C2 0.0443479877615874 0.667752318051629 0.287899694186784 olfactory receptor family 13 subfamily C member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13865 . 0.663285274 84.55414013 14215.00056 25.92354 OR13C3 0.000119523876421113 0.21996375397383 0.779916722149749 olfactory receptor family 13 subfamily C member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.15532 . 0.286674996 71.49681529 1081.21243 6.30649 OR13C4 5.657035075097e-08 0.0362828016228026 0.963717141806847 olfactory receptor family 13 subfamily C member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10812 . -0.003562597 53.72729417 185.52923 2.95777 OR13C5 0.624784091356639 0.343913698467062 0.031302210176299 olfactory receptor family 13 subfamily C member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.12688 . 2.48605694 98.63765039 12426.40269 23.93697 OR13C6P . . . olfactory receptor family 13 subfamily C member 6 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR13C7 . . . olfactory receptor family 13 subfamily C member 7 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR13C8 0.0123180644765934 0.647555910868925 0.340126024654482 olfactory receptor family 13 subfamily C member 8 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.24953 . 0.485092724 79.37603208 253.29039 3.42423 OR13C9 0.0436652352628204 0.664949899213065 0.291384865524115 olfactory receptor family 13 subfamily C member 9 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.27917 . 1.218120595 93.15876386 9128.01739 20.79137 OR13D1 0.010955869467886 0.622900104949093 0.366144025583021 olfactory receptor family 13 subfamily D member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10084 . 1.618658506 95.99551781 1559.31454 7.31418 OR13D2P . . . olfactory receptor family 13 subfamily D member 2 pseudogene . . . . . . . . . . . OR13D3P . . . olfactory receptor family 13 subfamily D member 3 pseudogene . . . . . . . . . . . OR13E1P . . . olfactory receptor family 13 subfamily E member 1 pseudogene . . . . . . . . . . . OR13F1 0.00023179177042085 0.309183759877649 0.69058444835193 olfactory receptor family 13 subfamily F member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.17032 . 1.596607091 95.87166785 1940.52304 8.10456 OR13G1 0.00566795772598196 0.484045699058747 0.510286343215271 olfactory receptor family 13 subfamily G member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.22485 0.10738 1.350418743 94.35008257 5802.9988 15.78675 OR13H1 0.0660742164107133 0.7312754780704 0.202650305518887 olfactory receptor family 13 subfamily H member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.11475 . 0.549415813 81.38122199 69.50651 1.72994 OR13I1P . . . olfactory receptor family 13 subfamily I member 1 pseudogene . . . . . . . . . . . OR13J1 1.00804374676836e-05 0.104426605312566 0.895563314249967 olfactory receptor family 13 subfamily J member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.11663 . -0.380166007 27.88393489 58.36389 1.54731 OR13K1P . . . olfactory receptor family 13 subfamily K member 1 pseudogene . . . . . . . . . . . OR13Z1P . . . olfactory receptor family 13 subfamily Z member 1 pseudogene . . . . . . . . . . . OR13Z2P . . . olfactory receptor family 13 subfamily Z member 2 pseudogene . . . . . . . . . . . OR13Z3P . . . olfactory receptor family 13 subfamily Z member 3 pseudogene . . . . . . . . . . . OR14A2 . . . olfactory receptor family 14 subfamily A member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.06906 . . 1091.88118 6.32360 OR14A16 0.00599837462277144 0.495647248214816 0.498354377162412 olfactory receptor family 14 subfamily A member 16 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.02441 . 0.639420866 83.8995046 359.657 4.01575 OR14C36 0.0101800694540978 0.607312413621903 0.382507516923999 olfactory receptor family 14 subfamily C member 36 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.01620 . 0.817616644 87.95116773 5808.16315 15.80361 OR14I1 2.99510561937582e-05 0.190368587056954 0.809601461886852 olfactory receptor family 14 subfamily I member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09440 . 1.153790856 92.55720689 1822.92534 7.87670 OR14J1 8.02406099709927e-08 0.023264879315774 0.976735040443616 olfactory receptor family 14 subfamily J member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06276 0.08756 0.21689899 68.12927577 68.17572 1.70882 OR14K1 0.00240709203730588 0.538907063777173 0.458685844185521 olfactory receptor family 14 subfamily K member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . 0.08133 . . 276.99209 3.56271 OR14L1P . . . olfactory receptor family 14 subfamily L member 1 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR51A1P . . . olfactory receptor family 51 subfamily A member 1 pseudogene . . . . . . . . . . . OR51A2 0.645582291191579 0.327839859990568 0.0265778488178535 olfactory receptor family 51 subfamily A member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10302 0.08951 3.75107138 99.60485964 3043.58628 10.48535 OR51A3P . . . olfactory receptor family 51 subfamily A member 3 pseudogene . . . . . . . . . . . OR51A4 0.239072288434888 0.64467337965686 0.116254331908252 olfactory receptor family 51 subfamily A member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07099 0.09096 1.68481378 96.37886294 548.15212 4.76145 OR51A5P . . . olfactory receptor family 51 subfamily A member 5 pseudogene . . . . . . . . . . . OR51A6P . . . olfactory receptor family 51 subfamily A member 6 pseudogene . . . . . . . . . . . OR51A7 1.657185671764e-06 0.0704884902393961 0.929509852574932 olfactory receptor family 51 subfamily A member 7 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03268 0.05702 0.418953042 77.06416608 516.23047 4.64796 OR51A8P . . . olfactory receptor family 51 subfamily A member 8 pseudogene . . . . . . . . . . . OR51A9P . . . olfactory receptor family 51 subfamily A member 9 pseudogene . . . . . . . . . . . OR51A10P . . . olfactory receptor family 51 subfamily A member 10 pseudogene . . . . . . . . . . . OR51AB1P . . . olfactory receptor family 51 subfamily AB member 1 pseudogene . . . . . . . . . . . OR51B2 0.0073551857029565 0.538189025547549 0.454455788749495 olfactory receptor family 51 subfamily B member 2 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06951 . 0.909442382 89.49634348 4943.3171 14.31586 OR51B3P . . . olfactory receptor family 51 subfamily B member 3 pseudogene . . . . . . . . . . . OR51B4 0.0123392431471372 0.647914629314826 0.339746127538037 olfactory receptor family 51 subfamily B member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10891 . 1.931026376 97.46992215 1903.2026 8.02492 OR51B5 0.000317629351949324 0.360616190266197 0.639066180381853 olfactory receptor family 51 subfamily B member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05550 . 2.219554466 98.15404577 7062.79586 17.99963 OR51B6 0.00017487774428757 0.268158241282387 0.731666880973326 olfactory receptor family 51 subfamily B member 6 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13753 . 3.532159363 99.48100967 14772.15484 26.38112 OR51B8P . . . olfactory receptor family 51 subfamily B member 8 pseudogene . . . . . . . . . . . OR51C1P . . . olfactory receptor family 51 subfamily C member 1 pseudogene . . . . . . . . . . . OR51C4P . . . olfactory receptor family 51 subfamily C member 4 pseudogene . . . . . . . . . . . OR51D1 0.0017095838447418 0.467632919540354 0.530657496614904 olfactory receptor family 51 subfamily D member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.25418 . 1.640710091 96.13116301 433.90945 4.34777 OR51E1 0.000349920575007864 0.377591465235593 0.622058614189399 olfactory receptor family 51 subfamily E member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . TISSUE SPECIFICITY: Highly expressed in prostate. Very low levels may be detected in some other tissues, such as placenta, skeletal muscle, heart, ovary and testis. Up-regulated in prostate cancers. {ECO:0000269|PubMed:15313197, ECO:0000269|PubMed:16206286}.; . . 0.17451 0.11227 0.328949044 73.41354093 334.06362 3.88343 OR51E2 0.00369122591258073 0.631298213131504 0.365010560955915 olfactory receptor family 51 subfamily E member 2 FUNCTION: Probable G protein-coupled receptor that is activated by the short chain fatty acids (SCFA) acetate and propionate. In response to SCFA, may positively regulate renin secretion and increase blood pressure (PubMed:23401498). May also be activated by steroid hormones and regulate cell proliferation (PubMed:19389702). May also function as an olfactory receptor being activated by beta-ionone (PubMed:19389702). {ECO:0000269|PubMed:19389702, ECO:0000269|PubMed:23401498}.; . TISSUE SPECIFICITY: Mainly expressed in the prostate. Also expressed in spleen, liver, olfactory epithelium and medulla oblongata. {ECO:0000269|PubMed:11707321, ECO:0000269|PubMed:16491480}.; . . 0.20083 0.11196 0.130533008 63.35810333 65.56756 1.66722 OR51F1 0.0539403351067528 0.701222668284688 0.244836996608559 olfactory receptor family 51 subfamily F member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.11039 . 2.397825098 98.50790281 9692.6735 21.32962 OR51F2 0.000112097120181894 0.373105345033184 0.626782557846634 olfactory receptor family 51 subfamily F member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.12500 . 0.306902668 72.38145789 535.49226 4.71715 OR51F3P . . . olfactory receptor family 51 subfamily F member 3 pseudogene . . . . . . . . . . . OR51F4P . . . olfactory receptor family 51 subfamily F member 4 pseudogene . . . . . . . . . . . OR51F5P . . . olfactory receptor family 51 subfamily F member 5 pseudogene . . . . . . . . . . . OR51G1 6.15802285365321e-05 0.277799077497321 0.722139342274142 olfactory receptor family 51 subfamily G member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04836 . 2.351894251 98.41354093 1081.18526 6.30554 OR51G2 0.00310073735008262 0.593515122753923 0.403384139895994 olfactory receptor family 51 subfamily G member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10498 0.08421 0.374860183 75.43052607 747.24621 5.42439 OR51H1 . . . olfactory receptor family 51 subfamily H member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13076 . . . . . OR51H2P . . . olfactory receptor family 51 subfamily H member 2 pseudogene . . . . . . . . . . . OR51I1 0.00237702705500239 0.536225263919922 0.461397709025076 olfactory receptor family 51 subfamily I member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.24519 . 2.754408354 98.99150743 7055.76054 17.97170 OR51I2 0.00088895679609386 0.56458879360722 0.434522249596686 olfactory receptor family 51 subfamily I member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05306 . 1.219937511 93.19414956 4811.48427 14.05963 OR51J1 . . . olfactory receptor family 51 subfamily J member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07982 . . . 7084.95896 18.09882 OR51K1P . . . olfactory receptor family 51 subfamily K member 1 pseudogene . . . . . . . . . . . OR51L1 0.0155803661202956 0.695527505404252 0.288892128475453 olfactory receptor family 51 subfamily L member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05274 . 1.574555842 95.73602265 1109.65792 6.36955 OR51M1 0.253410703966009 0.641099924492721 0.105489371541271 olfactory receptor family 51 subfamily M member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.11778 0.08420 2.043113937 97.74711017 3393.90915 11.15523 OR51N1P . . . olfactory receptor family 51 subfamily N member 1 pseudogene . . . . . . . . . . . OR51P1P . . . olfactory receptor family 51 subfamily P member 1 pseudogene . . . . . . . . . . . OR51Q1 0.00368505396031344 0.630936593319196 0.365378352720491 olfactory receptor family 51 subfamily Q member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . hypothalamus; . 0.12799 . 2.754408354 98.99150743 12173.23218 23.67045 OR51R1P . . . olfactory receptor family 51 subfamily R member 1 pseudogene . . . . . . . . . . . OR51S1 0.00381804007088034 0.638588917450903 0.357593042478217 olfactory receptor family 51 subfamily S member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10187 0.08499 1.796891089 96.90375088 3774.65651 12.03188 OR51T1 0.0197223467998845 0.740436337607138 0.239841315592977 olfactory receptor family 51 subfamily T member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10565 0.08739 -0.091746757 46.91554612 101.15146 2.17643 OR51V1 0.00371474051452938 0.632670094039797 0.363615165445674 olfactory receptor family 51 subfamily V member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04549 . 0.909442382 89.49634348 1109.79708 6.37052 OR52A1 0.00107001892950523 0.378326449809351 0.620603531261143 olfactory receptor family 52 subfamily A member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06221 0.08834 0.551232944 81.48148148 1671.29873 7.54640 OR52A4P . . . olfactory receptor family 52 subfamily A member 4 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03962 . . . . . OR52A5 0.000168133883560112 0.449260324028937 0.550571542087503 olfactory receptor family 52 subfamily A member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04918 0.09717 1.24016994 93.34748762 211.07936 3.13372 OR52B1P . . . olfactory receptor family 52 subfamily B member 1 pseudogene . . . . . . . . . 392.85365 4.16959 OR52B2 5.17756813877584e-05 0.254146270458786 0.745801953859826 olfactory receptor family 52 subfamily B member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . 2.085405872 97.82967681 579.93852 4.88209 OR52B3P . . . olfactory receptor family 52 subfamily B member 3 pseudogene . . . . . . . . . . . OR52B4 0.000229944721320279 0.307954233766111 0.691815821512569 olfactory receptor family 52 subfamily B member 4 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . -0.047654689 50.22410946 2558.74137 9.44385 OR52B5P . . . olfactory receptor family 52 subfamily B member 5 pseudogene . . . . . . . . . . . OR52B6 0.0735885276233448 0.74484601971856 0.181565452658095 olfactory receptor family 52 subfamily B member 6 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08867 0.07722 1.907156687 97.38145789 210.58907 3.13098 OR52D1 0.00367438578175141 0.630310018989075 0.366015595229173 olfactory receptor family 52 subfamily D member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.21520 . 0.553050905 81.54635527 3127.66018 10.64209 OR52E1 . . . olfactory receptor family 52 subfamily E member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR52E2 0.0004277489192399 0.414485901698365 0.585086349382395 olfactory receptor family 52 subfamily E member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05617 0.08911 2.441940525 98.55508375 3799.02 12.09977 OR52E3P . . . olfactory receptor family 52 subfamily E member 3 pseudogene . . . . . . . . . . . OR52E4 4.45011681541019e-07 0.0627888216175277 0.937210733370791 olfactory receptor family 52 subfamily E member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13169 0.06895 1.708681962 96.45553197 6972.28194 17.76777 OR52E5 . . . olfactory receptor family 52 subfamily E member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.41288 . . . . . OR52E6 0.0680948880246383 0.73525224713312 0.196652864842241 olfactory receptor family 52 subfamily E member 6 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.04695 0.05431 3.087169574 99.25100259 9604.25876 21.24007 OR52E7P . . . olfactory receptor family 52 subfamily E member 7 pseudogene . . . . . . . . . . . OR52E8 0.0166920375816032 0.709059944000298 0.274248018418099 olfactory receptor family 52 subfamily E member 8 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.14356 . 1.0858272 91.82000472 1046.46948 6.20800 OR52H1 0.0130705992596721 0.659882256132292 0.327047144608036 olfactory receptor family 52 subfamily H member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.24701 . 2.48605694 98.63765039 6742.78937 17.43550 OR52H2P . . . olfactory receptor family 52 subfamily H member 2 pseudogene . . . . . . . . . . . OR52I1 0.0620560888985741 0.722567661773364 0.215376249328062 olfactory receptor family 52 subfamily I member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.09874 . . . 1934.53482 8.09166 OR52I2 0.0745578369232702 0.746368106766525 0.179074056310205 olfactory receptor family 52 subfamily I member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.08065 . 1.153790856 92.55720689 4462.09614 13.39501 OR52J1P . . . olfactory receptor family 52 subfamily J member 1 pseudogene . . . . . . . . . . . OR52J2P . . . olfactory receptor family 52 subfamily J member 2 pseudogene . . . . . . . . . . . OR52J3 0.00101254779687311 0.592907903964062 0.406079548239065 olfactory receptor family 52 subfamily J member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.10425 0.08862 1.820761234 97.009908 11563.33574 23.27537 OR52K1 1.7549622716681e-05 0.142249761617229 0.857732688760055 olfactory receptor family 52 subfamily K member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07862 0.08655 0.50895761 80.20169851 2111.37015 8.45876 OR52K2 1.59479439547175e-06 0.068958407051623 0.931039998153982 olfactory receptor family 52 subfamily K member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.21815 0.08956 1.442251694 95.08138712 3031.82713 10.46059 OR52K3P . . . olfactory receptor family 52 subfamily K member 3 pseudogene . . . . . 0.40126 . . . . . OR52L1 0.00634036042025339 0.743561193248518 0.250098446331229 olfactory receptor family 52 subfamily L member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.11975 . 1.644346333 96.16654871 3616.46546 11.65193 OR52L2P . . . olfactory receptor family 52 subfamily L member 2 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.16964 . . . . . OR52M1 4.69164554510947e-06 0.126873222732574 0.873122085621881 olfactory receptor family 52 subfamily M member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07112 0.08344 0.158037129 64.85020052 467.174 4.47780 OR52M2P . . . olfactory receptor family 52 subfamily M member 2 pseudogene . . . . . . . . . . . OR52N1 0.0204785353882855 0.747202370961336 0.232319093650378 olfactory receptor family 52 subfamily N member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.22118 . 1.374284246 94.51521585 5899.1842 15.94095 OR52N2 7.30570712567745e-05 0.168905810874981 0.831021132053762 olfactory receptor family 52 subfamily N member 2 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05480 0.04810 1.886919751 97.29299363 3659.33447 11.75714 OR52N3P . . . olfactory receptor family 52 subfamily N member 3 pseudogene . . . . . . . . . . . OR52N4 3.29464855948091e-05 0.200348071879843 0.799618981634562 olfactory receptor family 52 subfamily N member 4 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.06695 . 1.728918179 96.55579146 2179.08089 8.60282 OR52N5 0.0492919635950094 0.686286875033783 0.264421161371208 olfactory receptor family 52 subfamily N member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.05793 0.07573 0.086440867 60.47416844 884.70367 5.79349 OR52P1P . . . olfactory receptor family 52 subfamily P member 1 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR52P2P . . . olfactory receptor family 52 subfamily P member 2 pseudogene . . . blood;bone marrow; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; . . . . . . OR52Q1P . . . olfactory receptor family 52 subfamily Q member 1 pseudogene . . . . . . . . . . . OR52R1 6.92486080039828e-06 0.157295423297779 0.84269765184142 olfactory receptor family 52 subfamily R member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.13632 . 2.019241996 97.71172446 6851.12331 17.64985 OR52S1P . . . olfactory receptor family 52 subfamily S member 1 pseudogene . . . . . . . . . . . OR52T1P . . . olfactory receptor family 52 subfamily T member 1 pseudogene . . . . . . . . . . . OR52U1P . . . olfactory receptor family 52 subfamily U member 1 pseudogene . . . . . . . . . . . OR52V1P . . . olfactory receptor family 52 subfamily V member 1 pseudogene . . . . . . . . . . . OR52W1 0.000404092684374612 0.403809521882977 0.595786385432648 olfactory receptor family 52 subfamily W member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03474 0.05491 0.861712133 88.6883699 427.43055 4.31826 OR52X1P . . . olfactory receptor family 52 subfamily X member 1 pseudogene . . . . . . . . . . . OR52Y1P . . . olfactory receptor family 52 subfamily Y member 1 pseudogene . . . . . . . . . . . OR52Z1 . . . olfactory receptor family 52 subfamily Z member 1 (gene/pseudogene) FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.11127 . . . . . OR55B1P . . . olfactory receptor family 55 subfamily B member 1 pseudogene . . . . . . . . . . . OR56A1 0.263101576969007 0.638084288827718 0.0988141342032753 olfactory receptor family 56 subfamily A member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.12687 0.08823 -0.690637458 15.12149092 110.34935 2.28592 OR56A3 7.11292351711341e-08 0.0414354865883437 0.958564442282421 olfactory receptor family 56 subfamily A member 3 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.24194 . -0.117432389 44.89266336 13.24382 0.48187 OR56A4 0.307699476267042 0.619006729502357 0.0732937942306002 olfactory receptor family 56 subfamily A member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.23269 . -0.556537043 19.72753008 975.32688 6.03885 OR56A5 . . . olfactory receptor family 56 subfamily A member 5 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR56A7P . . . olfactory receptor family 56 subfamily A member 7 pseudogene . . . . . . . . . . . OR56B1 1.26988881075159e-08 0.0151742489821094 0.984825738319002 olfactory receptor family 56 subfamily B member 1 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.07225 . 1.885103181 97.26940316 345.2485 3.94082 OR56B2P . . . olfactory receptor family 56 subfamily B member 2 pseudogene FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . . . . . . . OR56B3P 9.25160420643862e-07 0.0504312739432979 0.949567800896281 olfactory receptor family 56 subfamily B member 3 pseudogene . . . . . . . . . 80.87719 1.90162 OR56B4 1.18644352031201e-05 0.11442575430975 0.885562381255047 olfactory receptor family 56 subfamily B member 4 FUNCTION: Odorant receptor. {ECO:0000305}.; . . . . 0.03012 . 0.084621747 60.31493277 75.35292 1.81678 ORAI1 0.00305335775445046 0.590175076167614 0.406771566077936 ORAI calcium release-activated calcium modulator 1 FUNCTION: Ca(2+) release-activated Ca(2+) (CRAC) channel subunit which mediates Ca(2+) influx following depletion of intracellular Ca(2+) stores and channel activation by the Ca(2+) sensor, STIM1 (PubMed:16582901, PubMed:16645049, PubMed:16733527, PubMed:16766533, PubMed:16807233, PubMed:19249086, PubMed:23307288, PubMed:24351972, PubMed:24591628). CRAC channels are the main pathway for Ca(2+) influx in T-cells and promote the immune response to pathogens by activating the transcription factor NFAT (PubMed:16582901). {ECO:0000269|PubMed:16582901, ECO:0000269|PubMed:16645049, ECO:0000269|PubMed:16733527, ECO:0000269|PubMed:16766533, ECO:0000269|PubMed:16807233, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:23307288, ECO:0000269|PubMed:24351972, ECO:0000269|PubMed:24591628}.; DISEASE: Immunodeficiency 9 (IMD9) [MIM:612782]: An immune disorder characterized by recurrent infections, impaired activation and proliferative response of T-cells, decreased T-cell production of cytokines, and normal lymphocytes counts and serum immunoglobulin levels. In surviving patients ectodermal dysplasia with anhidrosis and non-progressive myopathy may be observed. {ECO:0000269|PubMed:16147976, ECO:0000269|PubMed:16582901}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myopathy, tubular aggregate, 2 (TAM2) [MIM:615883]: A rare congenital myopathy characterized by regular arrays of membrane tubules on muscle biopsies without additional histopathological hallmarks. Tubular aggregates in muscle are structures of variable appearance consisting of an outer tubule containing either one or more microtubule-like structures or amorphous material. TAM2 patients have myopathy and pupillary abnormalities. {ECO:0000269|PubMed:24591628}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;larynx;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;lens;breast;pancreas;lung;placenta;macula lutea;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;occipital lobe;medulla oblongata;cerebellum peduncles;atrioventricular node;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.09752 0.14115 0.104848986 61.49445624 31.83841 1.00209 ORAI2 0.336548283911044 0.602993263378899 0.0604584527100569 ORAI calcium release-activated calcium modulator 2 FUNCTION: Ca(2+) release-activated Ca(2+)-like (CRAC-like) channel subunit which mediates Ca(2+) influx and increase in Ca(2+)- selective current by synergy with the Ca(2+) sensor, STIM1. {ECO:0000269|PubMed:16807233, ECO:0000269|PubMed:17452328}.; . . unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;sympathetic chain;colon;parathyroid;blood;lens;skin;skeletal muscle;bone marrow;pancreas;whole body;lung;placenta;visual apparatus;testis;spleen;germinal center;kidney;brain;mammary gland;aorta;tonsil; amygdala;superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion; 0.32320 0.11154 -0.293801652 32.93819297 30.34586 0.96755 ORAI3 0.0109506896081293 0.622799997997814 0.366249312394057 ORAI calcium release-activated calcium modulator 3 FUNCTION: Key regulator or component of store-operated Ca(2+) channel and transcription factor NFAT nuclear import. {ECO:0000250}.; . . colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cerebellum cortex;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;spleen;kidney;peripheral nerve;thymus; dorsal root ganglion;liver;testis;ciliary ganglion; 0.16914 0.09768 -0.339715008 30.06605331 31.15212 0.98311 ORAOV1 0.0329902568453812 0.820059919459471 0.146949823695148 oral cancer overexpressed 1 . . TISSUE SPECIFICITY: Widely expressed. Highly expressed in placenta, kidney and skeletal muscle. {ECO:0000269|PubMed:12172009}.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;skin;skeletal muscle;pancreas;prostate;lung;cochlea;cerebral cortex;oesophagus;endometrium;bone;thyroid;placenta;liver;testis;head and neck;spleen;kidney;brain;stomach; . 0.15947 0.12706 0.080983847 59.76055674 124.59578 2.42688 ORAOV1P1 . . . oral cancer overexpressed 1 pseudogene 1 . . . . . . . . . . . ORC1 3.38880226667018e-05 0.999857812941869 0.000108299035464404 origin recognition complex subunit 1 FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.; DISEASE: Meier-Gorlin syndrome 1 (MGORS1) [MIM:224690]: A syndrome characterized by bilateral microtia, aplasia/hypoplasia of the patellae, and severe intrauterine and postnatal growth retardation with short stature and poor weight gain. Additional clinical findings include anomalies of cranial sutures, microcephaly, apparently low-set and simple ears, microstomia, full lips, highly arched or cleft palate, micrognathia, genitourinary tract anomalies, and various skeletal anomalies. While almost all cases have primordial dwarfism with substantial prenatal and postnatal growth retardation, not all cases have microcephaly, and microtia and absent/hypoplastic patella are absent in some. Despite the presence of microcephaly, intellect is usually normal. {ECO:0000269|PubMed:21358631, ECO:0000269|PubMed:21358632, ECO:0000269|PubMed:21358633}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.89876 0.11978 0.606246644 82.93229535 571.04641 4.84738 ORC2 0.971869811180841 0.0281298798516093 3.0896754952185e-07 origin recognition complex subunit 2 FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre- replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K20me3 and H4K27me3. Stabilizes LRWD1, by protecting it from ubiquitin- mediated proteasomal degradation. Also stabilizes ORC3. {ECO:0000269|PubMed:22427655, ECO:0000269|PubMed:22935713}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;lens;skeletal muscle;bile duct;breast;lung;adrenal gland;placenta;macula lutea;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; testis - interstitial;testis; 0.95283 0.12160 -0.181750739 40.15687662 43.67226 1.25694 ORC3 0.00030999720359409 0.999579882090058 0.000110120706347436 origin recognition complex subunit 3 FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre- replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3. {ECO:0000269|PubMed:22427655}.; . . ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;whole body;cochlea;endometrium;bone;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;lung;adrenal gland;mesenchyma;nasopharynx;placenta;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; occipital lobe;testis - interstitial;testis - seminiferous tubule;hypothalamus;spinal cord;prefrontal cortex;testis; 0.88456 0.11674 0.666922772 84.64260439 1402.00648 7.00037 ORC4 2.29195436096199e-06 0.901650213085149 0.0983474949604902 origin recognition complex subunit 4 FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre- replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3. {ECO:0000269|PubMed:22427655}.; DISEASE: Meier-Gorlin syndrome 2 (MGORS2) [MIM:613800]: A syndrome characterized by bilateral microtia, aplasia/hypoplasia of the patellae, and severe intrauterine and postnatal growth retardation with short stature and poor weight gain. Additional clinical findings include anomalies of cranial sutures, microcephaly, apparently low-set and simple ears, microstomia, full lips, highly arched or cleft palate, micrognathia, genitourinary tract anomalies, and various skeletal anomalies. While almost all cases have primordial dwarfism with substantial prenatal and postnatal growth retardation, not all cases have microcephaly, and microtia and absent/hypoplastic patella are absent in some. Despite the presence of microcephaly, intellect is usually normal. {ECO:0000269|PubMed:21358631, ECO:0000269|PubMed:21358632}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;muscle;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;thymus; amygdala;superior cervical ganglion;pons; 0.76699 0.11947 0.817616644 87.95116773 3039.47353 10.47790 ORC5 2.288348167214e-05 0.909773870587217 0.090203245931111 origin recognition complex subunit 5 FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre- replication complex necessary to initiate DNA replication.; . TISSUE SPECIFICITY: Abundant in spleen, ovary, prostate, testis, and colon mucosa. {ECO:0000269|PubMed:9765232}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;lens;skeletal muscle;retina;uterus;pancreas;prostate;lung;endometrium;nasopharynx;bone;thyroid;hippocampus;pituitary gland;liver;testis;amniotic fluid;head and neck;spleen;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;testis - interstitial;medulla oblongata;atrioventricular node;pons;skeletal muscle;uterus corpus;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.97972 0.13032 -0.666770504 15.86459071 137.26977 2.54815 ORC6 0.000734225790234647 0.76034605059129 0.238919723618475 origin recognition complex subunit 6 FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre- replication complex necessary to initiate DNA replication. Does not bind histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3. {ECO:0000269|PubMed:22427655}.; DISEASE: Meier-Gorlin syndrome 3 (MGORS3) [MIM:613803]: A syndrome characterized by bilateral microtia, aplasia/hypoplasia of the patellae, and severe intrauterine and postnatal growth retardation with short stature and poor weight gain. Additional clinical findings include anomalies of cranial sutures, microcephaly, apparently low-set and simple ears, microstomia, full lips, highly arched or cleft palate, micrognathia, genitourinary tract anomalies, and various skeletal anomalies. While almost all cases have primordial dwarfism with substantial prenatal and postnatal growth retardation, not all cases have microcephaly, and microtia and absent/hypoplastic patella are absent in some. Despite the presence of microcephaly, intellect is usually normal. {ECO:0000269|PubMed:21358632}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymphoreticular;smooth muscle;lymph node;hypothalamus;muscle;colon;skin;uterus;pancreas;lung;cochlea;placenta;visual apparatus;liver;head and neck;spleen;cervix;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.29023 0.10279 -0.405853867 26.23260203 19.61392 0.67284 ORM1 0.13235751069872 0.846071192107266 0.0215712971940142 orosomucoid 1 FUNCTION: Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability in the body. Appears to function in modulating the activity of the immune system during the acute-phase reaction. {ECO:0000269|PubMed:17008009, ECO:0000269|PubMed:17321687}.; . TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; unclassifiable (Anatomical System);prostate;lung;heart;liver;spleen;blood;skeletal muscle;gall bladder;bone marrow; prostate;fetal liver;liver;fetal lung;bone marrow; 0.17776 0.31679 0.21689899 68.12927577 37.2782 1.11141 ORM2 0.0050434836061214 0.886951633732912 0.108004882660966 orosomucoid 2 FUNCTION: Functions as transport protein in the blood stream. Binds various hydrophobic ligands in the interior of its beta- barrel domain. Also binds synthetic drugs and influences their distribution and availability. Appears to function in modulating the activity of the immune system during the acute-phase reaction. {ECO:0000269|PubMed:21349832}.; . TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; . . 0.32983 . 0.795569043 87.49115357 359.22805 4.01295 ORMDL1 0.0758238996219523 0.748284411952413 0.175891688425635 ORMDL sphingolipid biosynthesis regulator 1 FUNCTION: Negative regulator of sphingolipid synthesis. {ECO:0000269|PubMed:20182505}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in adult and fetal heart, brain, lung, liver, skeletal muscle and kidney. Expressed in adult pancreas and placenta and in fetal spleen abd thymus. Expressed at intermediate level in pancreas, placenta and brain but low in skeletal muscle and lung. {ECO:0000269|PubMed:12093374}.; ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;urinary;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;liver;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;small intestine;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach; . 0.43801 0.11262 -0.053113545 49.38664779 12.31085 0.44654 ORMDL2 0.15086877829343 0.777278292422879 0.0718529292836902 ORMDL sphingolipid biosynthesis regulator 2 FUNCTION: Negative regulator of sphingolipid synthesis. {ECO:0000269|PubMed:20182505}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in adult and fetal heart, brain, lung, liver, skeletal muscle and kidney. Expressed in adult pancreas and placenta and in fetal spleen abd thymus. {ECO:0000269|PubMed:12093374}.; umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);trophoblast;heart;islets of Langerhans;pharynx;blood;lens;breast;bile duct;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;liver;testis;ciliary ganglion;trigeminal ganglion; 0.19061 0.07904 -0.141298762 42.87567823 29.25711 0.93630 ORMDL3 0.721819207253289 0.264730554771976 0.0134502379747346 ORMDL sphingolipid biosynthesis regulator 3 FUNCTION: Negative regulator of sphingolipid synthesis. May indirectly regulate endoplasmic reticulum-mediated Ca(+2) signaling. {ECO:0000269|PubMed:20182505}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in adult and fetal heart, brain, lung, liver, skeletal muscle and kidney. Expressed in adult pancreas and placenta and in fetal spleen abd thymus. {ECO:0000269|PubMed:12093374}.; smooth muscle;ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; . 0.63192 0.13480 -0.229483771 36.86010852 4.59795 0.16520 OS9 1.13151214875817e-07 0.933380258819073 0.0666196280297121 osteosarcoma amplified 9, endoplasmic reticulum lectin FUNCTION: Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4. {ECO:0000269|PubMed:17932042, ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18417469, ECO:0000269|PubMed:19084021, ECO:0000269|PubMed:19346256, ECO:0000269|PubMed:21172656}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Found as well in all tumor cell lines analyzed, amplified in sarcomas. Highly expressed in osteosarcoma SJSA-1 and rhabdomyosarcoma Rh30 cell lines. Isoform 2 is the major isoform detected in all cell types examined.; lymphoreticular;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;synovium;larynx;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;cerebellum; superior cervical ganglion;trigeminal ganglion;skeletal muscle;cerebellum; . . -0.821100135 11.88369899 192.39758 3.00719 OSBP 0.999542555149074 0.00045744483789075 1.30353841499858e-11 oxysterol binding protein FUNCTION: Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum (PubMed:24209621). Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol (PubMed:15746430, PubMed:17428193). Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly (PubMed:15746430). Regulates cholesterol efflux by decreasing ABCA1 stability (PubMed:18450749). {ECO:0000269|PubMed:15746430, ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:18450749, ECO:0000269|PubMed:24209621}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11278871}.; lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;placenta;globus pallidus;ciliary ganglion;kidney;pons;atrioventricular node;skin;cerebellum; 0.48572 0.13977 -0.80269335 12.23755603 49.57201 1.37723 OSBP2 0.0361487444611796 0.963786474207338 6.47813314823687e-05 oxysterol binding protein 2 FUNCTION: Binds 7-ketocholesterol.; . TISSUE SPECIFICITY: Expressed mainly in retina, testis, and fetal liver. {ECO:0000269|PubMed:11278871}.; medulla oblongata;ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;bone;testis;pineal gland;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;blood;lens;breast;lung;placenta;macula lutea;hippocampus;liver;cervix;spleen;thymus; fetal liver;superior cervical ganglion;testis - interstitial;testis; 0.14253 0.10732 -0.571310997 19.01391838 199.19663 3.05045 OSBPL1A 4.1067927420582e-05 0.999955566326889 3.36574569059604e-06 oxysterol binding protein like 1A FUNCTION: Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3- phosphate (By similarity). Stabilizes GTP-bound RAB7A on late endosomes/lysosomes and alters functional properties of late endocytic compartments via its interaction with RAB7A (PubMed:16176980). Binds 25-hydroxycholesterol and cholesterol (PubMed:17428193). {ECO:0000250, ECO:0000269|PubMed:16176980, ECO:0000269|PubMed:17428193}.; . . ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; amygdala;whole brain;superior cervical ganglion;medulla oblongata;thalamus;occipital lobe;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.22358 0.10964 -0.416983034 25.82566643 320.10051 3.80167 OSBPL2 0.50491184114321 0.494915243231484 0.000172915625306228 oxysterol binding protein like 2 FUNCTION: Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3- phosphate (PubMed:11279184). Binds 25-hydroxycholesterol (PubMed:17428193). {ECO:0000269|PubMed:11279184, ECO:0000269|PubMed:17428193}.; . TISSUE SPECIFICITY: Widely expressed.; ovary;sympathetic chain;adrenal medulla;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;larynx;bone;thyroid;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;cingulate cortex; 0.12104 0.10546 -0.600630256 18.06440198 27.76557 0.89190 OSBPL3 0.00266192967168592 0.997333073944741 4.99638357294414e-06 oxysterol binding protein like 3 FUNCTION: Binds 25-hydroxycholesterol and cholesterol. {ECO:0000269|PubMed:17428193}.; . TISSUE SPECIFICITY: Isoform 1a, isoform 1b, isoform 1c and isoform 1d are highly expressed in brain, bone marrow, colon, kidney, lung, skeletal muscle, spleen, thymus and thyroid. Not expressed in heart and liver. Isoform 2a, isoform 2b, isoform 2c and isoform 2d are expressed in brain, bone marrow, kidney, skeletal muscle, spleen, thymus and thyroid. Not expressed in heart, liver and lung.; smooth muscle;ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;breast;pancreas;lung;epididymis;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach;thymus; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10986 0.10723 -0.659500046 16.07100731 85.50056 1.97168 OSBPL5 0.000848897697066133 0.999023159262222 0.000127943040711918 oxysterol binding protein like 5 FUNCTION: Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:23934110, PubMed:26206935). May cooperate with NPC1 to mediate the exit of cholesterol from endosomes/lysosomes (PubMed:21220512). Binds 25-hydroxycholesterol and cholesterol (PubMed:17428193). {ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:21220512, ECO:0000269|PubMed:23934110, ECO:0000269|PubMed:26206935}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12504849, ECO:0000269|PubMed:21220512}.; ovary;colon;substantia nigra;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;bone;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;spleen;head and neck;cervix;kidney;mammary gland;stomach; globus pallidus;ciliary ganglion;atrioventricular node; 0.09208 0.09279 -0.518142664 20.96013211 1420.31089 7.04175 OSBPL6 0.999012303789089 0.000987696207428625 3.48255163111922e-12 oxysterol binding protein like 6 FUNCTION: Weakly binds 25-hydroxycholesterol. {ECO:0000269|PubMed:17428193}.; . TISSUE SPECIFICITY: Expressed in brain and striated muscle (at protein level) (PubMed:14593528). Widely expressed (PubMed:11735225). Expressed in skeletal muscle (PubMed:14593528).; ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;bladder;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;alveolus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;aorta;stomach;thymus; amygdala;superior cervical ganglion;thyroid;atrioventricular node; 0.20553 0.09486 -1.304353358 4.91861288 690.81813 5.24020 OSBPL7 0.181605380199765 0.81839375286788 8.66932355728307e-07 oxysterol binding protein like 7 . . TISSUE SPECIFICITY: Expressed in epithelium of small and large intestines (at protein level). Expressed in stomach, duodenum, jejunum, ascending colon, spleen, thymus, lymph node, trachea and leukocytes. {ECO:0000269|PubMed:14593528}.; colon;choroid;fovea centralis;retina;prostate;subthalamic nucleus;optic nerve;frontal lobe;endometrium;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;tongue;blood;lens;skeletal muscle;pancreas;lung;hippocampus;macula lutea;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18157 0.09721 -0.837696902 11.45317292 151.61085 2.69309 OSBPL8 0.988348145917672 0.011651853790361 2.91966766592276e-10 oxysterol binding protein like 8 FUNCTION: Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:26206935). Binds oxysterol, 25- hydroxycholesterol and cholesterol (PubMed:17428193, PubMed:17991739, PubMed:21698267). {ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:17991739, ECO:0000269|PubMed:21698267, ECO:0000269|PubMed:26206935}.; . TISSUE SPECIFICITY: Widely expressed (PubMed:11735225). Expressed at higher level in macrophages (PubMed:17991739). {ECO:0000269|PubMed:11735225, ECO:0000269|PubMed:17991739}.; lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; medulla oblongata;superior cervical ganglion;prefrontal cortex;ciliary ganglion;caudate nucleus;pons;whole blood;cingulate cortex; 0.77324 0.11113 -0.512444034 21.55579146 62.14451 1.60766 OSBPL9 0.998515312665247 0.00148468710503499 2.29718027847538e-10 oxysterol binding protein like 9 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11735225}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;trabecular meshwork;placenta;visual apparatus;duodenum;liver;spleen;kidney;mammary gland;aorta;stomach;cerebellum;thymus; . 0.50706 0.12272 -0.201976964 38.98325077 101.20374 2.17716 OSBPL9P1 . . . oxysterol binding protein like 9 pseudogene 1 . . . . . . . . . . . OSBPL9P2 . . . oxysterol binding protein like 9 pseudogene 2 . . . . . . . . . . . OSBPL9P3 . . . oxysterol binding protein like 9 pseudogene 3 . . . . . . . . . . . OSBPL9P4 . . . oxysterol binding protein like 9 pseudogene 4 . . . . . . . . . . . OSBPL9P5 . . . oxysterol binding protein like 9 pseudogene 5 . . . . . . . . . . . OSBPL9P6 . . . oxysterol binding protein like 9 pseudogene 6 . . . . . . . . . . . OSBPL10 0.000141845926676448 0.998191559296411 0.00166659477691254 oxysterol binding protein like 10 FUNCTION: Probable lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane. Its ability to bind phosphatidylserine, suggests that it specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P (PubMed:23934110) (Probable). Plays a role in negative regulation of lipid biosynthesis (PubMed:19554302). Negatively regulates APOB secretion from hepatocytes (PubMed:19554302, PubMed:22906437). Binds cholesterol and acidic phospholipids (PubMed:22906437). Also binds 25-hydroxycholesterol (PubMed:17428193). Binds phosphatidylserine (PubMed:23934110). {ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:19554302, ECO:0000269|PubMed:22906437, ECO:0000269|PubMed:23934110, ECO:0000305}.; . . . . 0.47192 0.11305 -0.773369631 13.10450578 3159.74291 10.71216 OSBPL10-AS1 . . . OSBPL10 antisense RNA 1 . . . . . . . . . . . OSBPL11 0.898599332497567 0.101399077809429 1.58969300424025e-06 oxysterol binding protein like 11 FUNCTION: Plays a role in regulating ADIPOQ and FABP4 levels in differentiating adipocytes and is also involved in regulation of adipocyte triglyceride storage (PubMed:23028956). Weakly binds 25- hydroxycholesterol (PubMed:17428193). {ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:23028956}.; . TISSUE SPECIFICITY: Present at highest levels in ovary, testis, kidney, liver, stomach, brain, and adipose tissue. Strong expression (at protein level) in epithelial cells of kidney tubules, testicular tubules, caecum, and skin (PubMed:20599956). Present at low levels in subcutaneous and visceral adipose tissue (at protein level)(PubMed:23028956). {ECO:0000269|PubMed:20599956, ECO:0000269|PubMed:23028956}.; myocardium;ovary;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;adipose tissue;trigeminal ganglion;whole blood;skeletal muscle; 0.33855 0.09701 -0.80269335 12.23755603 27.29428 0.87965 OSCAR 0.632157857460211 0.360840876772405 0.00700126576738423 osteoclast associated, immunoglobulin-like receptor FUNCTION: Regulator of osteoclastogenesis which plays an important bone-specific function in osteoclast differentiation. {ECO:0000250}.; . . bile duct;unclassifiable (Anatomical System);lung;lacrimal gland;liver;colon;testis;kidney;stomach;bone marrow; . 0.08634 . . . 318.67773 3.79156 OSCP1 0.000148146568416105 0.964663155803661 0.0351886976279227 organic solute carrier partner 1 FUNCTION: May be involved in drug clearance in the placenta. {ECO:0000269|PubMed:16006562}.; . TISSUE SPECIFICITY: Expressed predominantly in testis, also found in placenta and to a lesser extent in thymus and small intestine; abundantly expressed in tumor-derived cell lines (PubMed:16006562). Ubiquitously expressed (PubMed:12819961). {ECO:0000269|PubMed:12819961, ECO:0000269|PubMed:16006562}.; medulla oblongata;ovary;colon;parathyroid;choroid;fovea centralis;retina;optic nerve;whole body;endometrium;iris;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;lens;breast;lung;nasopharynx;placenta;macula lutea;liver;spleen;kidney;stomach; superior cervical ganglion;pancreas;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;skeletal muscle; 0.16381 0.09851 0.575097644 82.1656051 3737.53252 11.95110 OSER1 0.00872888785285661 0.935348049933993 0.0559230622131505 oxidative stress responsive serine-rich 1 . . . . . 0.28255 0.11586 -0.095386216 46.48502005 3501.9588 11.40261 OSER1-AS1 . . . OSER1 antisense RNA 1 (head to head) . . . . . . . . . . . OSGEP 1.79721398649986e-05 0.88174189546578 0.118240132394355 O-sialoglycoprotein endopeptidase FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. {ECO:0000255|HAMAP-Rule:MF_03180}.; . TISSUE SPECIFICITY: Widely expressed at low level. Expressed in heart, placenta, liver, kidney, lung, brain, skeletal muscle and pancreas. {ECO:0000269|PubMed:12039036}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;larynx;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;pineal body;muscle;blood;lens;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; trigeminal ganglion; 0.12819 0.23572 -0.293801652 32.93819297 29.79622 0.95065 OSGEPL1 0.000202433816403507 0.725530508535496 0.2742670576481 O-sialoglycoprotein endopeptidase-like 1 FUNCTION: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance. {ECO:0000255|HAMAP-Rule:MF_03179}.; . TISSUE SPECIFICITY: Widely expressed, with maximum expression in pituitary gland, prostate, rectum and uterus. {ECO:0000269|PubMed:19694617}.; medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;retina;prostate;optic nerve;whole body;endometrium;testis;bladder;brain;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;lens;lung;nasopharynx;placenta;macula lutea;hippocampus;visual apparatus;liver;spleen;kidney; occipital lobe;superior cervical ganglion;globus pallidus; . 0.10254 -0.0274281 51.65723048 237.72291 3.32904 OSGEPL1-AS1 . . . OSGEPL1 antisense RNA 1 . . . . . . . . . . . OSGIN1 0.0160506254451066 0.959154891963333 0.0247944825915602 oxidative stress induced growth inhibitor 1 FUNCTION: Regulates the differentiation and proliferation of normal cells through the regulation of cell death. {ECO:0000269|PubMed:11459809, ECO:0000269|PubMed:14570898}.; . TISSUE SPECIFICITY: Ubiquitous. Highest expression in the ovary, testis, kidney, and liver. {ECO:0000269|PubMed:11459809, ECO:0000269|PubMed:14570898}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;salivary gland;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;pancreas;optic nerve;lung;macula lutea;liver;testis;kidney;brain;mammary gland; superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12211 0.09812 -0.014692675 52.35314933 316.10707 3.77617 OSGIN2 0.988642484366364 0.0113567073761464 8.08257489477589e-07 oxidative stress induced growth inhibitor family member 2 FUNCTION: May be involved in meiosis or the maturation of germ cells.; . TISSUE SPECIFICITY: Ubiquitous. Expressed at higher levels in testis and ovary.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lens;skeletal muscle;breast;pancreas;lung;macula lutea;liver;cervix;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.08530 0.13153 -0.380166007 27.88393489 235.93423 3.31901 OSM 0.397920808045078 0.562031101609489 0.0400480903454327 oncostatin M FUNCTION: Growth regulator. Inhibits the proliferation of a number of tumor cell lines. Stimulates proliferation of AIDS-KS cells. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells. Uses both type I OSM receptor (heterodimers composed of LIPR and IL6ST) and type II OSM receptor (heterodimers composed of OSMR and IL6ST). Involved in the maturation of fetal hepatocytes, thereby promoting liver development and regeneration (By similarity). {ECO:0000250, ECO:0000269|PubMed:1542792, ECO:0000269|PubMed:1542793}.; . . unclassifiable (Anatomical System);uterus;lung;ovary;heart;urinary;colon;spleen;blood;kidney;skin; . 0.17800 0.71680 -0.249709319 35.74545883 68.19067 1.70915 OSMR 3.10306262078619e-11 0.892176394465496 0.107823605503473 oncostatin M receptor FUNCTION: Associates with IL31RA to form the IL31 receptor. Binds IL31 to activate STAT3 and possibly STAT1 and STAT5. Capable of transducing OSM-specific signaling events. {ECO:0000269|PubMed:15184896, ECO:0000269|PubMed:8999038}.; DISEASE: Amyloidosis, primary localized cutaneous, 1 (PLCA1) [MIM:105250]: A primary amyloidosis characterized by localized cutaneous amyloid deposition. This condition usually presents with itching (especially on the lower legs) and visible changes of skin hyperpigmentation and thickening that may be exacerbated by chronic scratching and rubbing. Primary localized cutaneous amyloidosis is often divided into macular and lichen subtypes although many affected individuals often show both variants coexisting. Lichen amyloidosis characteristically presents as a pruritic eruption of grouped hyperkeratotic papules with a predilection for the shins, calves, ankles and dorsa of feet and thighs. Papules may coalesce to form hyperkeratotic plaques that can resemble lichen planus, lichen simplex or nodular prurigo. Macular amyloidosis is characterized by small pigmented macules that may merge to produce macular hyperpigmentation, sometimes with a reticulate or rippled pattern. In macular and lichen amyloidosis, amyloid is deposited in the papillary dermis in association with grouped colloid bodies, thought to represent degenerate basal keratinocytes. The amyloid deposits probably reflect a combination of degenerate keratin filaments, serum amyloid P component, and deposition of immunoglobulins. {ECO:0000269|PubMed:18179886, ECO:0000269|PubMed:19690585}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at relatively high levels in all neural cells as well as fibroblast, epithelial and a variety of tumor cell lines. {ECO:0000269|PubMed:8999038}.; unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;skin;skeletal muscle;breast;uterus;pancreas;prostate;lung;larynx;bone;thyroid;placenta;visual apparatus;iris;hypopharynx;liver;testis;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skin; 0.16709 0.08659 1.58549778 95.80679406 1984.40709 8.20914 OSMR-AS1 . . . OSMR antisense RNA 1 (head to head) . . . . . . . . . . . OSR1 0.774760147238011 0.217694901543592 0.00754495121839741 odd-skipped related transciption factor 1 FUNCTION: Transcription factor that plays a role in the regulation of embryonic heart and urogenital development. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in adult colon, small intestine, prostate, testis, and fetal lung. {ECO:0000269|PubMed:12119563}.; unclassifiable (Anatomical System);medulla oblongata;heart;ovary;urinary;parathyroid;blood;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;lung;trabecular meshwork;placenta;macula lutea;testis;spleen;brain;stomach; superior cervical ganglion; 0.38669 . 0.038710339 56.92380278 17.33473 0.60927 OSR2 0.56668220898551 0.421366948166257 0.0119508428482329 odd-skipped related transciption factor 2 . . . unclassifiable (Anatomical System);medulla oblongata;heart;ovary;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;prostate;optic nerve;lung;endometrium;placenta;macula lutea;visual apparatus;testis;kidney;brain;mammary gland; uterus;testis - interstitial;uterus corpus;superior cervical ganglion;adipose tissue;testis - seminiferous tubule;testis; 0.58800 0.13405 0.058937498 58.26256192 64.83954 1.65355 OST4 . . . oligosaccharyltransferase complex subunit 4, non-catalytic FUNCTION: May be involved in N-glycosylation through its association with N-oligosaccharyl transferase. {ECO:0000250}.; . . . . . . . . . . OSTC 0.608151848832313 0.383275311429526 0.0085728397381618 oligosaccharyltransferase complex subunit (non-catalytic) . . . lymphoreticular;smooth muscle;ovary;skin;bone marrow;prostate;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;salivary gland;intestine;colon;parathyroid;uterus;whole body;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;kidney;stomach;aorta; . . . 0.013025609 54.62962963 10.78349 0.39151 OSTCP1 . . . oligosaccharyltransferase complex subunit pseudogene 1 . . . . . . . . . . . OSTCP2 . . . oligosaccharyltransferase complex subunit pseudogene 2 . . . . . . . . . . . OSTCP3 . . . oligosaccharyltransferase complex subunit pseudogene 3 . . . . . . . . . . . OSTCP4 . . . oligosaccharyltransferase complex subunit pseudogene 4 . . . . . . . . . . . OSTCP5 . . . oligosaccharyltransferase complex subunit pseudogene 5 . . . . . . . . . . . OSTCP6 . . . oligosaccharyltransferase complex subunit pseudogene 6 . . . . . . . . . . . OSTCP7 . . . oligosaccharyltransferase complex subunit pseudogene 7 . . . . . . . . . . . OSTCP8 . . . oligosaccharyltransferase complex subunit pseudogene 8 . . . . . . . . . . . OSTF1 0.666040393255519 0.332879697705486 0.00107990903899479 osteoclast stimulating factor 1 FUNCTION: Induces bone resorption, acting probably through a signaling cascade which results in the secretion of factor(s) enhancing osteoclast formation and activity. {ECO:0000269|PubMed:10092216}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Present in osteoclasts (at protein level). {ECO:0000269|PubMed:10092216}.; myocardium;smooth muscle;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);islets of Langerhans;blood;lens;skeletal muscle;lung;placenta;macula lutea;hippocampus;visual apparatus;head and neck;kidney;mammary gland; white blood cells;whole blood; 0.15610 0.21533 -0.273576253 33.97027601 12.77658 0.46454 OSTF1P1 . . . osteoclast stimulating factor 1 pseudogene 1 . . . . . . . . . . . OSTM1 0.0604714184790487 0.92291737210129 0.0166112094196612 osteopetrosis associated transmembrane protein 1 FUNCTION: Required for osteoclast and melanocyte maturation and function. {ECO:0000250, ECO:0000269|PubMed:21527911}.; DISEASE: Osteopetrosis, autosomal recessive 5 (OPTB5) [MIM:259720]: A rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Recessive osteopetrosis commonly manifests in early infancy with macrocephaly, feeding difficulties, evolving blindness and deafness, bone marrow failure, severe anemia, and hepatosplenomegaly. Deafness and blindness are generally thought to represent effects of pressure on nerves. OPTB5 patients manifest primary central nervous system involvement in addition to the classical stigmata of severe bone sclerosis, growth failure, anemia, thrombocytopenia and visual impairment with optic atrophy. {ECO:0000269|PubMed:12627228, ECO:0000269|PubMed:16813530}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;bone;pituitary gland;testis;dura mater;germinal center;spinal ganglion;brain;pineal gland;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;pia mater;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;amnion;kidney;mammary gland;stomach;aorta; trigeminal ganglion; 0.10607 0.18075 -0.361761279 28.6329323 302.78784 3.70732 OSTM1-AS1 . . . OSTM1 antisense RNA 1 . . . . . . . . . . . OSTN 0.0858560507076122 0.760884836722085 0.153259112570302 osteocrin FUNCTION: Appears to modulate osteoblastic differentiation. Could also function as an autocrine and paracrine factor linked to glucose metabolism in skeletal muscle (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in bone.; . . 0.25029 0.12267 0.169169615 65.33380514 47.54611 1.33898 OSTN-AS1 . . . OSTN antisense RNA 1 . . . . . . . . . . . OTC 0.981017899946665 0.0189680099511948 1.4090102139748e-05 ornithine carbamoyltransferase . DISEASE: Ornithine carbamoyltransferase deficiency (OTCD) [MIM:311250]: An X-linked disorder of the urea cycle which causes a form of hyperammonemia. Mutations with no residual enzyme activity are always expressed in hemizygote males by a very severe neonatal hyperammonemic coma that generally proves to be fatal. Heterozygous females are either asymptomatic or express orotic aciduria spontaneously or after protein intake. The disorder is treatable with supplemental dietary arginine and low protein diet. The arbitrary classification of patients into the 'neonatal' group (clinical hyperammonemia in the first few days of life) and 'late' onset (clinical presentation after the neonatal period) has been used to differentiate severe from mild forms. {ECO:0000269|PubMed:10070627, ECO:0000269|PubMed:10502831, ECO:0000269|PubMed:10737985, ECO:0000269|PubMed:11793483, ECO:0000269|PubMed:1480464, ECO:0000269|PubMed:1671317, ECO:0000269|PubMed:1721894, ECO:0000269|PubMed:2347583, ECO:0000269|PubMed:2474822, ECO:0000269|PubMed:3170748, ECO:0000269|PubMed:7474905, ECO:0000269|PubMed:7951259, ECO:0000269|PubMed:8019569, ECO:0000269|PubMed:8081373, ECO:0000269|PubMed:8081398, ECO:0000269|PubMed:8099056, ECO:0000269|PubMed:8530002, ECO:0000269|PubMed:8807340, ECO:0000269|PubMed:8830175, ECO:0000269|PubMed:8956038, ECO:0000269|PubMed:8956045, ECO:0000269|PubMed:9143919, ECO:0000269|PubMed:9266388, ECO:0000269|PubMed:9286441, ECO:0000269|PubMed:9452024, ECO:0000269|PubMed:9452049, ECO:0000269|PubMed:9452065, ECO:0000269|Ref.32, ECO:0000269|Ref.43}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Mainly expressed in liver and intestinal mucosa.; unclassifiable (Anatomical System);whole body;liver;spleen; dorsal root ganglion;superior cervical ganglion;fetal liver;ciliary ganglion;trigeminal ganglion;skin; 0.22278 0.85665 0.082802743 60.09082331 1072.1412 6.27812 OTOA 4.15629802750077e-08 0.997268265433472 0.00273169300354801 otoancorin FUNCTION: May act as an adhesion molecule.; DISEASE: Deafness, autosomal recessive, 22 (DFNB22) [MIM:607039]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:11972037}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . alveolus;testis;colon;kidney; . 0.28984 0.09529 -0.817464788 11.97806086 1136.37759 6.43062 OTOF 4.32599885952291e-25 0.776042930923555 0.223957069076445 otoferlin FUNCTION: Key calcium ion sensor involved in the Ca(2+)-triggered synaptic vesicle-plasma membrane fusion and in the control of neurotransmitter release at these output synapses. Interacts in a calcium-dependent manner to the presynaptic SNARE proteins at ribbon synapses of cochlear inner hair cells (IHCs) to trigger exocytosis of neurotransmitter. Also essential to synaptic exocytosis in immature outer hair cells (OHCs). May also play a role within the recycling of endosomes (By similarity). {ECO:0000250}.; DISEASE: Deafness, autosomal recessive, 9 (DFNB9) [MIM:601071]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:10192385, ECO:0000269|PubMed:12127154, ECO:0000269|PubMed:16097006, ECO:0000269|PubMed:16283880, ECO:0000269|PubMed:16371502}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Auditory neuropathy, autosomal recessive, 1 (AUNB1) [MIM:601071]: A form of sensorineural hearing loss with absent or severely abnormal auditory brainstem response, in the presence of normal cochlear outer hair cell function and normal otoacoustic emissions. Auditory neuropathies result from a lesion in the area including the inner hair cells, connections between the inner hair cells and the cochlear branch of the auditory nerve, the auditory nerve itself and auditory pathways of the brainstem. In some cases AUNB1 phenotype can be temperature sensitive. {ECO:0000269|PubMed:16371502, ECO:0000269|PubMed:18381613}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 and isoform 3 are found in adult brain. Isoform 2 is expressed in the fetus and in adult brain, heart, placenta, skeletal muscle and kidney.; bone;spinal cord;brain; . 0.50924 . -0.107001106 45.57678698 7402.5338 18.47280 OTOG . . . otogelin FUNCTION: Glycoprotein specific to acellular membranes of the inner ear. May be required for the anchoring of the otoconial membranes and cupulae to the underlying neuroepithelia in the vestibule. May be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. May play a role in mechanotransduction processes (By similarity). {ECO:0000250}.; DISEASE: Deafness, autosomal recessive, 18B (DFNB18B) [MIM:614945]: A form of non-syndromic deafness characterized by a moderate hearing impairment, which can be associated with vestibular dysfunction, and a flat to shallow "U" or slightly downsloping shaped audiograms. {ECO:0000269|PubMed:23122587}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.08265 . . . 14123.45118 25.75321 OTOGL 3.7282457621613e-31 0.131969855124343 0.868030144875657 otogelin like . . TISSUE SPECIFICITY: Expressed at high levels in fetal inner ear and heart. Low levels in fetal skeletal muscle, kidney, spleen and colon. Not detected in fetal liver, lung, brain, nor in fetal stomach. In adult tissues, highest levels in brain, kidney, heart and retina. Relatively low levels in lung, spleen and duodenum. Not detected in adult skeletal muscle, liver, nor testis. {ECO:0000269|PubMed:23122586}.; lung;cochlea;islets of Langerhans;kidney;stomach; subthalamic nucleus;appendix;ciliary ganglion;skeletal muscle; 0.06243 0.09167 . . 10439.70705 22.34420 OTOL1 1.71727944749843e-07 0.129061811311718 0.870938016960338 otolin 1 . . . . . . . 0.062575634 58.74026893 5302.06277 15.04573 OTOP1 7.31470990584692e-16 0.00112154209373963 0.99887845790626 otopetrin 1 FUNCTION: Required for normal formation of otoconia in the inner ear. Inhibits P2Y purinoceptors. Modulates calcium homeostasis and influx of calcium in response to extracellular ATP (By similarity). {ECO:0000250}.; . . frontal lobe; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09443 . 0.424410872 77.25878745 1114.22669 6.37726 OTOP2 3.08382306848341e-09 0.163686761789245 0.836313235126932 otopetrin 2 . . . medulla oblongata;colon; superior cervical ganglion;globus pallidus;atrioventricular node;pons;skeletal muscle; 0.23023 . -0.264476624 34.8844067 237.01506 3.32474 OTOP3 9.57033698502344e-06 0.78191533558218 0.218075094080835 otopetrin 3 . . . optic nerve;macula lutea;fovea centralis;choroid;lens;retina; . 0.16381 0.10374 0.916727815 89.56711489 433.78621 4.34716 OTOR 0.0148213358106119 0.685546432499258 0.29963223169013 otoraplin . . TISSUE SPECIFICITY: Highly expressed in cochlea.; cochlea;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.18164 0.12811 0.391453969 75.87284737 2536.79409 9.40108 OTOS 2.78890336245965e-07 0.0479792511069281 0.952020470002735 otospiralin FUNCTION: May be essential for the survival of the neurosensory epithelium of the inner ear. {ECO:0000250}.; . TISSUE SPECIFICITY: Ear specific.; unclassifiable (Anatomical System);brain; . 0.22046 0.10905 -0.007201372 53.19061099 13.99394 0.50825 OTP 0.848003249176535 0.14934994716946 0.00264680365400585 orthopedia homeobox FUNCTION: Probably involved in the differentiation of hypothalamic neuroendocrine cells.; . . unclassifiable (Anatomical System);lung;visual apparatus;testis; atrioventricular node;trigeminal ganglion; 0.22992 . . . 49.2632 1.37174 OTSC1 . . . otosclerosis 1 . . . . . . . . . . . OTSC2 . . . otosclerosis 2 . . . . . . . . . . . OTSC3 . . . otosclerosis 3 . . . . . . . . . . . OTSC4 . . . otosclerosis 4 . . . . . . . . . . . OTSC5 . . . otosclerosis 5 . . . . . . . . . . . OTSC6 . . . otosclerosis 6 . . . . . . . . . . . OTSC7 . . . otosclerosis 7 . . . . . . . . . . . OTSC8 . . . otosclerosis 8 . . . . . . . . . . . OTSC9 . . . otosclerosis 9 . . . . . . . . . . . OTSC10 . . . otosclerosis 10 . . . . . . . . . . . OTUB1 0.945238199205908 0.0545668605053037 0.000194940288788099 OTU deubiquitinase, ubiquitin aldehyde binding 1 FUNCTION: Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy. Isoform 1 destabilizes RNF128, leading to prevent anergy. In contrast, isoform 2 stabilizes RNF128 and promotes anergy. Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates deubiquitination of 'Lys- 48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains. Not able to cleave di-ubiquitin. Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin.; . TISSUE SPECIFICITY: Isoform 1 is ubiquitous. Isoform 2 is expressed only in lymphoid tissues such as tonsils, lymph nodes and spleen, as well as peripheral blood mononuclear cells. {ECO:0000269|PubMed:12704427, ECO:0000269|PubMed:14661020}.; lymphoreticular;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;cerebral cortex;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;trophoblast;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;thymus;cerebellum; dorsal root ganglion;amygdala;whole brain;medulla oblongata;superior cervical ganglion;thalamus;occipital lobe;temporal lobe;atrioventricular node;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.10445 . -0.007201372 53.19061099 92.14011 2.06462 OTUB2 9.30774599769382e-06 0.328670793173595 0.671319899080407 OTU deubiquitinase, ubiquitin aldehyde binding 2 FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'- linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:12704427, ECO:0000269|PubMed:18954305, ECO:0000269|PubMed:23827681}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in brain. {ECO:0000269|PubMed:12704427}.; unclassifiable (Anatomical System);colon;blood;skeletal muscle;bone marrow;uterus;pancreas;prostate;lung;placenta;visual apparatus;testis;brain;stomach; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.73348 0.11262 -0.0274281 51.65723048 151.18302 2.68814 OTUD1 . . . OTU deubiquitinase 1 FUNCTION: Deubiquitinating enzyme that specifically hydrolyzes 'Lys-63'-linked polyubiquitin to monoubiquitin. {ECO:0000269|PubMed:23827681}.; . . . . 0.22330 . . . 67.80095 1.70389 OTUD3 2.62536799027489e-05 0.762179781239835 0.237793965080262 OTU deubiquitinase 3 FUNCTION: Deubiquitinating enzyme that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. Also hydrolyzes heterotypic (mixed and branched) and homotypic chains. {ECO:0000269|PubMed:23827681}.; . . . . 0.12584 0.10296 0.349177632 74.18023119 428.43399 4.32246 OTUD4 0.999916478365076 8.3521634717015e-05 2.06982755746082e-13 OTU deubiquitinase 4 FUNCTION: Deubiquitinating enzyme that specifically hydrolyzes 'Lys-48'-linked polyubiquitin. {ECO:0000269|PubMed:23827681}.; . . unclassifiable (Anatomical System);ovary;salivary gland;pharynx;colon;blood;breast;prostate;lung;nasopharynx;visual apparatus;liver;testis;kidney;brain;bladder; dorsal root ganglion;testis - interstitial;superior cervical ganglion;prefrontal cortex;appendix;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.46205 0.12897 -0.993849454 8.56334041 130.30354 2.48591 OTUD4P1 . . . OTUD4 pseudogene 1 . . . . . . . . . . . OTUD5 0.97654856924968 0.0234277090053809 2.37217449387089e-05 OTU deubiquitinase 5 FUNCTION: Deubiquitinating enzyme that functions as negative regulator of the innate immune system. Acts via TRAF3 deubiquitination and subsequent suppression of type I interferon (IFN) production. Has peptidase activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave 'Lys-11'- linked ubiquitin chains (in vitro). {ECO:0000269|PubMed:17991829, ECO:0000269|PubMed:22245969, ECO:0000269|PubMed:23827681}.; . TISSUE SPECIFICITY: Expressed in various tissues, including the liver and placenta, as well as in peripheral blood leukocytes. {ECO:0000269|PubMed:17991829}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;gum;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;cerebellum;thymus; . 0.36816 0.10475 -0.163345027 41.24793583 14.84731 0.53404 OTUD6A 0.573824004405944 0.380833696723453 0.045342298870603 OTU deubiquitinase 6A FUNCTION: Deubiquitinating enzyme that hydrolyzes 'Lys-27'-, 'Lys- 29'- and 'Lys-33'-linked polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked ubiquitin chains. {ECO:0000269|PubMed:23827681}.; . . . . 0.05168 0.09337 0.237127192 68.98443029 11.44776 0.41393 OTUD6B 6.25843988413621e-08 0.0730312656528757 0.926968671762726 OTU domain containing 6B . . . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;lung;nasopharynx;placenta;hippocampus;liver;mammary gland;stomach; dorsal root ganglion;occipital lobe;subthalamic nucleus;superior cervical ganglion;globus pallidus;kidney;trigeminal ganglion; 0.08686 0.09530 0.705562627 85.52724699 177.93559 2.89894 OTUD6B-AS1 . . . OTUD6B antisense RNA 1 (head to head) . . . . . . . . . . . OTUD7A 0.97459544138619 0.025403372230056 1.18638375358984e-06 OTU deubiquitinase 7A FUNCTION: Has deubiquitinating activity towards 'Lys-11'-linked polyubiquitin chains. {ECO:0000269|PubMed:20622874, ECO:0000269|PubMed:23827681}.; . . unclassifiable (Anatomical System);frontal lobe;kidney;retina; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;skin; 0.24200 0.11597 -1.153638777 6.233781552 218.07197 3.19168 OTUD7B 0.100123440515689 0.89981383595629 6.27235280207442e-05 OTU deubiquitinase 7B FUNCTION: Negative regulator of the non-canonical NF-kappa-B pathway that acts by mediating deubiquitination of TRAF3, an inhibitor of the NF-kappa-B pathway, thereby acting as a negative regulator of B-cell responses. In response to non-canonical NF- kappa-B stimuli, deubiquitinates 'Lys-48'-linked polyubiquitin chains of TRAF3, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B. Negatively regulates mucosal immunity against infections. Mediates deubiquitination of EGFR. Has deubiquitinating activity toward 'Lys-11', 'Lys-48' or 'Lys-63'- linked polyubiquitin chains. In vitro, has preference for 'Lys- 11'-linked polyubiquitin chains; however such data are unsure in vivo. Hydrolyzes both linear and branched forms of polyubiquitin. {ECO:0000269|PubMed:11463333, ECO:0000269|PubMed:12682062, ECO:0000269|PubMed:18178551, ECO:0000269|PubMed:20622874, ECO:0000269|PubMed:22179831, ECO:0000269|PubMed:23827681}.; . TISSUE SPECIFICITY: Widely expressed. Abundant in kidney, heart and fetal liver. Expressed differentially among B-cells at distinct developmental stages. Higher expression seen in primary immature B-cells as compared to the mature cells. {ECO:0000269|PubMed:11463333, ECO:0000269|PubMed:12682062}.; . . 0.14330 0.09974 -1.087493118 7.106628922 77.98101 1.86257 OTULIN . . . OTU deubiquitinase with linear linkage specificity FUNCTION: Deubiquitinase that specifically removes linear ('Met- 1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. Associates with the LUBAC complex via direct interaction with RNF31 and counteracts its action by cleaving linear polyubiquitin chains to substrates. Required during angiogenesis, craniofacial and neuronal development by regulating the canonical Wnt signaling together with the LUBAC complex. Acts as a negative regulator of NF-kappa-B by counteracting activity of the LUBAC complex. Plays a key role in innate immune response: required to restrict linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation, probably to limit NOD2-dependent proinflammatory signaling. {ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0000269|PubMed:23806334, ECO:0000269|PubMed:23827681}.; . . . . 0.10641 0.10279 0.459411326 78.28497287 . . OTX1 0.219807903535165 0.742724003805782 0.0374680926590524 orthodenticle homeobox 1 FUNCTION: Probably plays a role in the development of the brain and the sense organs. Can bind to the BCD target sequence (BTS): 5'-TCTAATCCC-3'.; . TISSUE SPECIFICITY: Expressed in brain. Detected in the anterior part of the neural fetal retina (at protein level). {ECO:0000269|PubMed:19414065}.; unclassifiable (Anatomical System);ovary;colon;choroid;fovea centralis;lens;retina;breast;optic nerve;lung;visual apparatus;macula lutea;brain;stomach; . 0.15090 0.27707 -0.095386216 46.48502005 58.85689 1.55683 OTX2 0.744599586946362 0.253068111543947 0.00233230150969102 orthodenticle homeobox 2 FUNCTION: Probably plays a role in the development of the brain and the sense organs. Can bind to the BCD target sequence (BTS): 5'-TCTAATCCC-3'.; DISEASE: Microphthalmia, syndromic, 5 (MCOPS5) [MIM:610125]: Patients manifest unilateral or bilateral microphthalmia/clinical anophthalmia and variable additional features including pituitary dysfunction, coloboma, microcornea, cataract, retinal dystrophy, hypoplasia or agenesis of the optic nerve, agenesis of the corpus callosum, developmental delay, joint laxity, hypotonia, and seizures. Microphthalmia is a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. {ECO:0000269|PubMed:15846561, ECO:0000269|PubMed:20396904, ECO:0000269|PubMed:22577225, ECO:0000269|PubMed:24167467}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pituitary hormone deficiency, combined, 6 (CPHD6) [MIM:613986]: Combined pituitary hormone deficiency is defined as the impaired production of growth hormone and one or more of the other five anterior pituitary hormones. CPHD6 patients manifest neonatal hypoglycemia, and deficiencies of growth hormone, thyroid-stimulating hormone, luteinizing hormone, follicle stimulating hormone and adrenocorticotropic hormone. {ECO:0000269|PubMed:18728160}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Retinal dystrophy, early-onset, with or without pituitary dysfunction (RDEOP) [MIM:610125]: An autosomal dominant ocular disease characterized by pattern dystrophy of the retinal pigment epithelium, and photoreceptor degeneration. Mild developmental anomalies include optic nerve head dysplasia, microcornea, and Rathke's cleft cyst. Some patients manifest pituary dysfunction. {ECO:0000269|PubMed:19956411, ECO:0000269|PubMed:25293953}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain.; unclassifiable (Anatomical System);optic nerve;whole body;pineal body;macula lutea;visual apparatus;fovea centralis;choroid;lens;brain;retina; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.93317 0.34375 -0.383807564 27.41802312 8.14355 0.29966 OTX2-AS1 . . . OTX2 antisense RNA 1 (head to head) . . . . . . . . . . . OTX2P1 . . . orthodenticle homeobox 2 pseudogene 1 . . . . . . . . . . . OVAAL . . . ovarian adenocarcinoma amplified long non-coding RNA . . . . . . . . . . . OVCA2 3.94781518236935e-05 0.220556883979446 0.77940363786873 ovarian tumor suppressor candidate 2 . . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11979432, ECO:0000269|PubMed:8616839}.; medulla oblongata;ovary;sympathetic chain;colon;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;oesophagus;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . . . -0.207437529 38.2814343 17.7925 0.62180 OVCH1 1.53112390015935e-28 1.87770677054756e-05 0.999981222932295 ovochymase 1 . . . lung;testis; dorsal root ganglion;superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05800 . . . 4524.95189 13.51306 OVCH1-AS1 . . . OVCH1 antisense RNA 1 . . . . . . . . . 205.72001 3.09914 OVCH2 7.83188711149752e-14 0.00911842507052183 0.9908815749294 ovochymase 2 (gene/pseudogene) . . . . . 0.04808 . . . . . OVGP1 0.000935883751426529 0.986059587270554 0.0130045289780199 oviductal glycoprotein 1 FUNCTION: Binds to oocyte zona pellucida in vivo. May play a role in the fertilization process and/or early embryonic development.; . TISSUE SPECIFICITY: Oviduct.; . . 0.06541 0.12012 1.624117298 96.03090351 2799.2734 9.98625 OVOL1 0.676795693517501 0.318519855394276 0.00468445108822278 ovo like zinc finger 1 FUNCTION: Putative transcription factor. Involved in hair formation and spermatogenesis. May function in the differentiation and/or maintenance of the urogenital system (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in fetal kidney, and also in adult pancreas and placenta. Not expressed in intestine, peripheral blood lymphocytes and ovary.; unclassifiable (Anatomical System);trophoblast;heart;ovary;colon;parathyroid;skin;skeletal muscle;uterus;pancreas;lung;endometrium;epididymis;placenta;liver;testis;spleen;mammary gland;bladder; superior cervical ganglion;testis;trigeminal ganglion;parietal lobe; 0.42471 0.11484 -0.271755481 34.31823543 56.66493 1.51382 OVOL1-AS1 . . . OVOL1 antisense RNA 1 . . . . . . . . . . . OVOL2 0.436097284181233 0.533040290738024 0.0308624250807431 ovo like zinc finger 2 FUNCTION: Zinc-finger transcription repressor factor. Plays a critical role to maintain the identity of epithelial lineages by suppressing epithelial-to mesenchymal transition mainly through the up-regulation of ZEB1 expression. Positively regulates neuronal differentiation (By similarity). Suppresses cell cycling and terminal differentiation of keratinocytes by directly repressing MYC and NOTCH1. {ECO:0000250, ECO:0000269|PubMed:19700410}.; . TISSUE SPECIFICITY: Expressed in testis, ovary, heart and skeletal muscle. {ECO:0000269|PubMed:12213202}.; unclassifiable (Anatomical System);uterus;lung;ovary;lacrimal gland;endometrium;islets of Langerhans;colon;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;temporal lobe;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.82560 0.11062 -0.249709319 35.74545883 149.7231 2.66798 OVOL3 . . . ovo like zinc finger 3 FUNCTION: May act as a transcription regulator. {ECO:0000250}.; . . cartilage;ovary;testis; superior cervical ganglion; . . . . 282.3436 3.59765 OXA1L 5.96038677388776e-09 0.40458518411878 0.595414809920834 oxidase (cytochrome c) assembly 1-like FUNCTION: Required for the insertion of integral membrane proteins into the mitochondrial inner membrane. Essential for the activity and assembly of cytochrome oxidase. Required for the correct biogenesis of ATP synthase and complex I in mitochondria. {ECO:0000269|PubMed:17936786, ECO:0000269|PubMed:7991568}.; . . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;alveolus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; fetal liver;white blood cells; 0.07416 0.09045 0.935129812 89.86199575 2985.34106 10.37018 OXCT1 0.267382736691876 0.732571418313359 4.58449947652094e-05 3-oxoacid CoA-transferase 1 FUNCTION: Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate.; . TISSUE SPECIFICITY: Abundant in heart, followed in order by kidney, brain, and muscle, whereas in liver it is undetectable; also detectable in leukocytes and fibroblasts.; lymphoreticular;myocardium;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;atrium;whole body;frontal lobe;endometrium;gum;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;adrenal cortex;skeletal muscle;pancreas;lung;adrenal gland;trabecular meshwork;placenta;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; amygdala;whole brain;thalamus;medulla oblongata;subthalamic nucleus;occipital lobe;cerebellum peduncles;temporal lobe;globus pallidus;caudate nucleus;cingulate cortex;parietal lobe; 0.10026 . -0.203796826 38.81811748 78.01979 1.86291 OXCT1-AS1 . . . OXCT1 antisense RNA 1 . . . . . . . . . . . OXCT2 . . . 3-oxoacid CoA-transferase 2 FUNCTION: Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:11756565}.; . . 0.25381 . . . 56.45684 1.51099 OXCT2P1 . . . 3-oxoacid CoA-transferase 2 pseudogene 1 . . . . . . . . . . . OXER1 4.76881321179725e-07 0.0653288848491265 0.934670638269552 oxoeicosanoid (OXE) receptor 1 FUNCTION: Receptor for eicosanoids and polyunsaturated fatty acids such as 5-oxo-6E,8Z,11Z,14Z-eicosatetraenoic acid (5-OXO-ETE), 5(S)-hydroperoxy-6E,8Z,11Z,14Z-eicosatetraenoic acid (5(S)-HPETE) and arachidonic acid. Seems to be coupled to the G(i)/G(o), families of heteromeric G proteins. {ECO:0000269|PubMed:12065583, ECO:0000269|PubMed:12606753}.; . TISSUE SPECIFICITY: Expressed in various tissues except brain. Expression is more intense in liver, kidney, peripheral leukocyte, lung, and spleen than in other tissues. Highly expressed in eosinophils, neutrophils, and lung macrophages. {ECO:0000269|PubMed:12065583, ECO:0000269|PubMed:12606753}.; . . 0.13374 . 1.003094668 90.77022883 994.58026 6.07647 OXGR1 0.000863935505500482 0.558408050629124 0.440728013865376 oxoglutarate receptor 1 FUNCTION: Receptor for alpha-ketoglutarate. Seems to act exclusively through a G(q)-mediated pathway (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in kidney and, to a lower extend, in placenta. Not detected in brain tissues including the frontal cortex, caudate putamen, thalamus, hypothalamus, hippocampus or pons.; visual apparatus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.20210 0.11382 -0.516085732 21.20193442 36.88334 1.10482 OXLD1 0.0414232246772906 0.65528942867811 0.3032873466446 oxidoreductase-like domain containing 1 . . . . . 0.11925 . 0.237127192 68.98443029 38.06297 1.13125 OXNAD1 2.37384753438508e-05 0.504031051417448 0.495945210107208 oxidoreductase NAD-binding domain containing 1 . . . unclassifiable (Anatomical System);medulla oblongata;lymph node;cartilage;heart;islets of Langerhans;colon;skin;skeletal muscle;bile duct;uterus;pancreas;lung;nasopharynx;bone;placenta;visual apparatus;liver;cervix;spleen;kidney;brain;stomach;cerebellum; . 0.02498 0.08483 0.174625237 65.9648502 4855.63615 14.16263 OXR1 0.488534430030687 0.511463942684252 1.62728506091009e-06 oxidation resistance 1 FUNCTION: May be involved in protection from oxidative damage. {ECO:0000269|PubMed:11114193, ECO:0000269|PubMed:15060142}.; . . ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;hypothalamus;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;whole brain;superior cervical ganglion;occipital lobe;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.18219 0.10646 -1.085675268 7.147912243 108.08784 2.25745 OXSM 0.00330641693750777 0.828808827327341 0.167884755735151 3-oxoacyl-ACP synthase, mitochondrial FUNCTION: May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function. {ECO:0000269|PubMed:15668256}.; . TISSUE SPECIFICITY: Widely expressed. Higher expression in heart, skeletal muscle, liver and kidney which contain high levels of active mitochondria. {ECO:0000269|PubMed:15668256}.; medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;urinary;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.04336 0.48800 0.150760231 64.51403633 451.64336 4.41844 OXSR1 0.989117555735273 0.0108824144587223 2.98060046457564e-08 oxidative stress responsive 1 FUNCTION: Regulates downstream kinases in response to environmental stress. May also have a function in regulating the actin cytoskeleton. {ECO:0000269|PubMed:14707132, ECO:0000303|PubMed:14707132}.; . TISSUE SPECIFICITY: Ubiquitously expressed in all tissue examined. {ECO:0000269|PubMed:10083736}.; ovary;sympathetic chain;colon;parathyroid;skin;uterus;prostate;frontal lobe;cochlea;endometrium;larynx;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;spleen;head and neck;cervix;kidney;stomach;peripheral nerve;cerebellum; dorsal root ganglion;trigeminal ganglion; 0.52576 0.14445 -0.293801652 32.93819297 1902.58992 8.02351 OXT 0.62795746033166 0.34149653357964 0.0305460060886998 oxytocin/neurophysin I prepropeptide FUNCTION: Neurophysin 1 specifically binds oxytocin.; . . kidney; hypothalamus;ciliary ganglion;skeletal muscle; 0.08922 0.34498 . . 3.58877 0.13051 OXTR 5.74322739893592e-05 0.268079451304128 0.731863116421882 oxytocin receptor FUNCTION: Receptor for oxytocin. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol- calcium second messenger system.; . . unclassifiable (Anatomical System);heart;ovary;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;placenta;macula lutea;visual apparatus;liver;brain; superior cervical ganglion;atrioventricular node; 0.11987 0.23953 0.64123826 83.97617363 1649.79782 7.50620 P1 . . . P one antigen (P blood group) . . . . . . . . . . . P2RX1 6.46551928902605e-08 0.434777719269784 0.565222216075024 purinergic receptor P2X 1 FUNCTION: Ligand-gated ion channel with relatively high calcium permeability. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle. Seems to be linked to apoptosis, by increasing the intracellular concentration of calcium in the presence of ATP, leading to programmed cell death (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;ovary;placenta;blood;bone marrow; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08402 0.17067 -0.490397599 22.50530786 52.89202 1.44267 P2RX2 9.69419848481171e-12 0.0217044379558391 0.978295562034467 purinergic receptor P2X 2 FUNCTION: Ion channel gated by extracellular ATP involved in a variety of cellular responses, such as excitatory postsynaptic responses in sensory neurons, neuromuscular junctions (NMJ) formation, hearing, perception of taste and peristalsis. In the inner ear, regulates sound transduction and auditory neurotransmission, outer hair cell electromotility, inner ear gap junctions, and K(+) recycling. Mediates synaptic transmission between neurons and from neurons to smooth muscle. {ECO:0000269|PubMed:23345450}.; DISEASE: Deafness, autosomal dominant, 41 (DFNA41) [MIM:608224]: A form of non-syndromic deafness characterized by onset of progressive sensorineural hearing loss usually in the second decade. The hearing loss is severe and ultimately affects all frequencies. Exposure to noise exacerbates the hearing loss, particularly at high frequencies. {ECO:0000269|PubMed:23345450, ECO:0000269|PubMed:24211385}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . kidney; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.46386 0.16229 -0.622676946 17.30950696 137.45964 2.55055 P2RX3 0.0114975811361225 0.979967754571655 0.00853466429222313 purinergic receptor P2X 3 FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel.; . . unclassifiable (Anatomical System); superior cervical ganglion;ciliary ganglion; 0.31742 0.15938 -0.025608647 51.91672564 1523.99976 7.25477 P2RX4 2.36800653754896e-09 0.141594724828765 0.858405272803228 purinergic receptor P2X 4 FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel. This receptor is insensitive to the antagonists PPADS and suramin. {ECO:0000269|PubMed:10515189}.; . . lymphoreticular;ovary;sympathetic chain;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;head and neck;kidney;stomach; superior cervical ganglion;cerebellum peduncles;placenta;kidney;skeletal muscle; 0.22959 0.24180 -0.044015879 50.44821892 1838.0499 7.90402 P2RX5 1.83109272499805e-05 0.884114140044988 0.115867549027762 purinergic receptor P2X 5 FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel.; . TISSUE SPECIFICITY: Expressed at high levels in brain and immune system.; ovary;salivary gland;colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;endometrium;testis;germinal center;bladder;brain;tonsil;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;macula lutea;visual apparatus;liver;spleen;cervix;kidney; whole brain;lymph node;tumor;tonsil; 0.06657 0.10722 0.622829232 83.47487615 148.45371 2.65609 P2RX5-TAX1BP3 . . . P2RX5-TAX1BP3 readthrough (NMD candidate) . . . . . . . . . . . P2RX6 1.87852665747002e-07 0.425831988213323 0.574167823934012 purinergic receptor P2X 6 FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed predominantly in skeletal muscle.; unclassifiable (Anatomical System);ovary;muscle;colon;parathyroid;lens;skeletal muscle;retina;optic nerve;lung;placenta;testis;spleen;brain; dorsal root ganglion;medulla oblongata;superior cervical ganglion;cerebellum peduncles;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;appendix;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.05817 0.12210 -0.176292081 40.56381222 495.75077 4.57540 P2RX6P . . . purinergic receptor P2X 6 pseudogene . . . . . . . . . . . P2RX7 3.78969928544417e-06 0.987919909845021 0.012076300455694 purinergic receptor P2X 7 FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel. Responsible for ATP-dependent lysis of macrophages through the formation of membrane pores permeable to large molecules. Could function in both fast synaptic transmission and the ATP-mediated lysis of antigen-presenting cells.; . TISSUE SPECIFICITY: Widely expressed with highest levels in brain and immune tissues. {ECO:0000269|PubMed:15896293}.; unclassifiable (Anatomical System);lymphoreticular;pancreas;thyroid;liver;brain;mammary gland;skin; occipital lobe;superior cervical ganglion;prefrontal cortex;parietal lobe; 0.13346 0.19158 2.826067329 99.07407407 10100.50875 21.94414 P2RY1 0.581732803893959 0.407649240493614 0.0106179556124267 purinergic receptor P2Y1 FUNCTION: Receptor for extracellular adenine nucleotides such as ATP and ADP. In platelets binding to ADP leads to mobilization of intracellular calcium ions via activation of phospholipase C, a change in platelet shape, and probably to platelet aggregation. {ECO:0000269|PubMed:9442040}.; . . unclassifiable (Anatomical System);lung;liver;colon; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.38844 0.24568 -0.317668748 31.45789101 29.97125 0.95785 P2RY2 0.0704719841364836 0.872118357164122 0.0574096586993942 purinergic receptor P2Y2 FUNCTION: Receptor for ATP and UTP coupled to G-proteins that activate a phosphatidylinositol-calcium second messenger system. The affinity range is UTP = ATP > ATP-gamma-S >> 2-methylthio-ATP = ADP.; . TISSUE SPECIFICITY: Spleen, testis, kidney, liver, lung, heart and brain.; unclassifiable (Anatomical System);lung;ovary;endometrium;placenta;adrenal cortex;colon;parathyroid;brain;skeletal muscle;stomach; superior cervical ganglion;olfactory bulb;placenta;atrioventricular node;skeletal muscle; 0.13685 0.28559 0.665103516 84.6131163 1735.9734 7.68750 P2RY4 0.340711070430522 0.60048768822135 0.0588012413481282 pyrimidinergic receptor P2Y4 FUNCTION: Receptor for UTP and UDP coupled to G-proteins that activate a phosphatidylinositol-calcium second messenger system. Not activated by ATP or ADP.; . TISSUE SPECIFICITY: Pancreas.; . . 0.09602 0.16824 1.462485515 95.2111347 680.61335 5.21578 P2RY6 4.63834764452777e-07 0.0642984410075727 0.935701095157663 pyrimidinergic receptor P2Y6 FUNCTION: Receptor for extracellular UDP > UTP > ATP. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system.; . . unclassifiable (Anatomical System);ovary;colon;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;placenta;thyroid;macula lutea;liver;spleen;kidney;aorta; . 0.10066 0.17927 -0.890882376 10.30313753 41.40219 1.20975 P2RY8 0.0128441170894152 0.656261423889961 0.330894459020623 purinergic receptor P2Y8 FUNCTION: Probable receptor for purines coupled to G-proteins.; . TISSUE SPECIFICITY: Barely detectable in normal blood leukocytes. Weaker expression was seen in heart, kidney and lung. Not detected in brain. {ECO:0000269|PubMed:11004484, ECO:0000269|PubMed:15466006}.; . . 0.08168 0.11931 -0.247889024 35.98726115 941.82081 5.95055 P2RY10 0.690389561601064 0.291483213132493 0.0181272252664432 purinergic receptor P2Y10 FUNCTION: Putative receptor for purines coupled to G-proteins.; . TISSUE SPECIFICITY: Weakly expressed in blood leukocytes. {ECO:0000269|PubMed:11004484}.; unclassifiable (Anatomical System);pancreas;placenta;blood;germinal center; trigeminal ganglion; 0.33437 0.11285 -0.007201372 53.19061099 7.38443 0.27475 P2RY10P1 . . . purinergic receptor P2Y10 pseudogene 1 . . . . . . . . . . . P2RY10P2 . . . purinergic receptor P2Y10 pseudogene 2 . . . . . . . . . . . P2RY11 9.07591188729782e-08 0.0902244521805021 0.909775457060379 purinergic receptor P2Y11 FUNCTION: Receptor for ATP and ADP coupled to G-proteins that activate both phosphatidylinositol-calcium and adenylyl cyclase second messenger systems. Not activated by UTP or UDP.; . TISSUE SPECIFICITY: Highest expression in liver and spleen. {ECO:0000269|PubMed:11278528}.; lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;lacrimal gland;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; . . 0.13481 0.297596326 71.67964142 17.17523 0.60365 P2RY12 0.107032257879275 0.775862577886172 0.117105164234553 purinergic receptor P2Y12 FUNCTION: Receptor for ADP and ATP coupled to G-proteins that inhibit the adenylyl cyclase second messenger system. Not activated by UDP and UTP. Required for normal platelet aggregation and blood coagulation. {ECO:0000269|PubMed:11104774, ECO:0000269|PubMed:11196645, ECO:0000269|PubMed:11502873, ECO:0000269|PubMed:12578987, ECO:0000269|PubMed:24670650, ECO:0000269|PubMed:24784220}.; DISEASE: Bleeding disorder, platelet-type 8 (BDPLT8) [MIM:609821]: A condition characterized by mild to moderate mucocutaneous bleeding, and excessive bleeding after surgery or trauma. The defect is due to severe impairment of platelet response to ADP resulting in defective platelet aggregation. {ECO:0000269|PubMed:11196645, ECO:0000269|PubMed:12578987, ECO:0000269|PubMed:25428217}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in the platelets, lower levels in the brain. Lowest levels in the lung, appendix, pituitary and adrenal gland. Expressed in the spinal cord and in the fetal brain. {ECO:0000269|PubMed:11104774, ECO:0000269|PubMed:11196645, ECO:0000269|PubMed:11502873}.; unclassifiable (Anatomical System);optic nerve;hypothalamus;nasopharynx;macula lutea;fovea centralis;choroid;spinal ganglion;lens;brain;skeletal muscle;retina; . 0.06958 0.16086 -0.181750739 40.15687662 53.58581 1.45662 P2RY13 0.327928323861021 0.608033115283354 0.0640385608556252 purinergic receptor P2Y13 FUNCTION: Receptor for ADP. Coupled to G(i)-proteins. May play a role in hematopoiesis and the immune system. {ECO:0000269|PubMed:11546776}.; . TISSUE SPECIFICITY: Strong expression in spleen and adult brain. Lower expression in placenta, lung, liver, spinal cord, thymus, small intestine, uterus, stomach, testis, fetal brain, and adrenal gland. Not detected in pancreas, heart, kidney, skeletal muscle, ovary or fetal aorta. Clearly detected in lymph node and bone marrow, weakly detected in peripheral blood mononuclear cells (PBMC) and in peripheral blood leukocytes (PBL), but not detected in polymorphonuclear cells (PMN). In the brain, detected in all brain regions examined.; unclassifiable (Anatomical System);uterus;lung;heart;nasopharynx;liver;testis;colon;spleen;brain;skin; atrioventricular node;whole blood; 0.27253 . 0.21689899 68.12927577 33.56453 1.03635 P2RY14 0.000377084300253391 0.39106519469804 0.608557721001707 purinergic receptor P2Y14 FUNCTION: Receptor for UDP-glucose and other UDP-sugar coupled to G-proteins. Not activated by ATP, ADP, UTP or ATP. {ECO:0000269|PubMed:10753868}.; . TISSUE SPECIFICITY: Highest expression in the placenta, adipose tissue, stomach and intestine, intermediate levels in the brain, spleen, lung and heart, lowest levels in the kidney.; unclassifiable (Anatomical System);heart;cartilage;skin;bone marrow;uterus;endometrium;nasopharynx;placenta;liver;testis;kidney;stomach; trigeminal ganglion; 0.08228 0.10836 0.042348793 57.31304553 87.89074 2.00397 P3H1 . . . prolyl 3-hydroxylase 1 FUNCTION: Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro- Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts. {ECO:0000269|PubMed:10951563}.; DISEASE: Osteogenesis imperfecta 8 (OI8) [MIM:610915]: A form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI8 is characterized by disproportionate short stature, severe osteoporosis, shortening of the long bones, white sclerae, a round face and a short barrel- shaped chest. {ECO:0000269|PubMed:17277775, ECO:0000269|PubMed:19088120}. Note=The disease is caused by mutations affecting the gene represented in this entry. A splice site mutation leading to the absence of isoform 1 has been reported in 2 OI8 patients. Isoform 1 is the only form predicted to be located in the endoplasmic reticulum, which the appropriate location for the catalysis of collagen hydroxylation. These patients show indeed severely reduced COL1A1 hydroxylation (PubMed:19088120). {ECO:0000269|PubMed:19088120}.; . . . 0.14358 0.12757 0.360092658 74.68152866 . . P3H2 . . . prolyl 3-hydroxylase 2 FUNCTION: Shows prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types II, IV and V. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in heart, placenta, lung, liver, skeletal muscle and kidney. Expression localized to the epithelia of bile ducts and to the sacroplasm of heart muscle and skeletal muscle. In the pancreas, localized to a subpopulation of Langerhans islet cells and in the salivary gland, expressed in acinar cells. {ECO:0000269|PubMed:15063763}.; . . 0.14234 0.13152 -0.554717505 19.79830149 . . P3H2-AS1 . . . P3H2 antisense RNA 1 . . . . . . . . . . . P3H3 . . . prolyl 3-hydroxylase 3 FUNCTION: Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V. {ECO:0000250}.; . TISSUE SPECIFICITY: Weak expression in heart, lung, ovary and skeletal muscle. {ECO:0000269|PubMed:8723724}.; . . . 0.30492 . . . . P3H4 . . . prolyl 3-hydroxylase family member 4 (non-enzymatic) . . . . . . . -0.291981272 33.20358575 . . P4HA1 0.776076094613878 0.223910392632457 1.35127536649998e-05 prolyl 4-hydroxylase subunit alpha 1 FUNCTION: Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;amniotic fluid;germinal center;brain;bladder;amygdala;cartilage;heart;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;spleen;cervix;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;thymus; superior cervical ganglion;smooth muscle;atrioventricular node;skeletal muscle; 0.32947 0.34511 -0.293801652 32.93819297 56.28383 1.50659 P4HA2 6.46128411074688e-05 0.998890679641442 0.00104470751745102 prolyl 4-hydroxylase subunit alpha 2 FUNCTION: Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.; DISEASE: Note=P4HA2 mutations may be a cause of myopia, a refractive error of the eye, in which parallel rays from a distant object come to focus in front of the retina, vision being better for near objects than for far. {ECO:0000269|PubMed:25741866}.; . ovary;sympathetic chain;skin;prostate;endometrium;thyroid;iris;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;oesophagus;bone;pituitary gland;testis;pineal gland;artery;unclassifiable (Anatomical System);lymph node;muscle;bile duct;pancreas;lung;adrenal gland;mesenchyma;placenta;amnion;head and neck;kidney;stomach;aorta; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.30813 0.19318 -0.997481928 8.47487615 87.86929 2.00326 P4HA2-AS1 . . . P4HA2 antisense RNA 1 . . . . . . . . . . . P4HA3 1.60495574125891e-07 0.844015527731083 0.155984311773343 prolyl 4-hydroxylase subunit alpha 3 FUNCTION: Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. {ECO:0000269|PubMed:12874193, ECO:0000269|PubMed:14500733}.; . TISSUE SPECIFICITY: Highly expressed in placenta, liver and fetal skin. Weakly expressed in fetal epiphyseal cartilage, fetal liver, fibroblast, lung and skeletal muscle. Expressed also in fibrous cap of carotid atherosclerotic lesions. {ECO:0000269|PubMed:12874193, ECO:0000269|PubMed:14500733}.; unclassifiable (Anatomical System);cartilage;ovary;parathyroid;bone marrow;pancreas;prostate;lung;larynx;placenta;visual apparatus;testis;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.06249 0.11304 0.066214104 58.95848077 3135.20649 10.66532 P4HB 0.968508654303976 0.0314813694335645 9.97626245917797e-06 prolyl 4-hydroxylase subunit beta FUNCTION: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307). {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:12485997, ECO:0000269|PubMed:21670307}.; DISEASE: Cole-Carpenter syndrome 1 (CLCRP1) [MIM:112240]: A form of Cole-Carpenter syndrome, a disorder characterized by features of osteogenesis imperfecta such as bone deformities and severe bone fragility with frequent fractures, in association with craniosynostosis, ocular proptosis, hydrocephalus, growth failure and distinctive facial features. Craniofacial findings include marked frontal bossing, midface hypoplasia, and micrognathia. Despite the craniosynostosis and hydrocephalus, intellectual development is normal. CLCRP1 inheritance is autosomal dominant. {ECO:0000269|PubMed:25683117}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;choroid;vein;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;oesophagus;larynx;gum;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;urinary;pharynx;blood;lens;pancreas;lung;cornea;placenta;visual apparatus;duodenum;liver;cervix;head and neck;kidney;mammary gland;stomach;thymus; prostate;pancreas;smooth muscle;lung;adipose tissue;trachea;heart;adrenal gland;thyroid;placenta;beta cell islets;liver; 0.48061 0.59875 -0.844966979 11.1759849 30.43817 0.97004 P4HTM 0.0232749358306657 0.973672949951591 0.00305211421774331 prolyl 4-hydroxylase, transmembrane (endoplasmic reticulum) FUNCTION: Catalyzes the post-translational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. {ECO:0000269|PubMed:17726031}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in adult pancreas, heart, skeletal muscle, brain, placenta, kidney and adrenal gland. Expressed at lower levels in epiphyseal cartilage and in fibroblasts. {ECO:0000269|PubMed:12163023, ECO:0000269|PubMed:17726031}.; lymphoreticular;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;liver;spleen;cervix;kidney;stomach;cerebellum; amygdala;whole brain;thalamus;subthalamic nucleus;medulla oblongata;occipital lobe;cerebellum peduncles;temporal lobe;prefrontal cortex;globus pallidus;caudate nucleus;pons;cingulate cortex;parietal lobe;cerebellum; . 0.15276 -0.091746757 46.91554612 45.49118 1.29567 PA2G4 0.998000990941836 0.00199895179543159 5.72627320635504e-08 proliferation-associated 2G4 FUNCTION: May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly. Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site) (By similarity). Regulates cell proliferation, differentiation, and survival. Isoform 1 suppresses apoptosis whereas isoform 2 promotes cell differentiation (By similarity). {ECO:0000250|UniProtKB:P50580, ECO:0000250|UniProtKB:Q6AYD3, ECO:0000269|PubMed:11268000, ECO:0000269|PubMed:12682367, ECO:0000269|PubMed:15064750, ECO:0000269|PubMed:15583694, ECO:0000269|PubMed:16832058}.; . TISSUE SPECIFICITY: Isoform 2 is undetectable whereas isoform 1 is strongly expressed in cancer cells (at protein level). Isoform 1 and isoform 2 are widely expressed, including heart, brain, lung, pancreas, skeletal muscle, kidney, placenta and liver. {ECO:0000269|PubMed:10682683, ECO:0000269|PubMed:15064750, ECO:0000269|PubMed:19037095}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;oesophagus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;pons;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.95977 0.22256 -0.295622497 32.61972163 7.18834 0.27050 PA2G4P1 . . . proliferation-associated 2G4 pseudogene 1 . . . . . . . . . . . PA2G4P2 . . . proliferation-associated 2G4 pseudogene 2 . . . . . . . . . . . PA2G4P3 . . . proliferation-associated 2G4 pseudogene 3 . . . . . . . . . . . PA2G4P4 . . . proliferation-associated 2G4 pseudogene 4 . . . . . . . . . . . PA2G4P5 . . . proliferation-associated 2G4 pseudogene 5 . . . . . . . . . . . PA2G4P6 . . . proliferation-associated 2G4 pseudogene 6 . . . . . . . . . . . PAAF1 1.03087812740244e-06 0.781422950468797 0.218576018653075 proteasomal ATPase associated factor 1 FUNCTION: Inhibits proteasome 26S assembly and proteolytic activity by impairing the association of the 19S regulatory complex with the 20S core. In case of HIV-1 infection, recruited by viral Tat to the HIV-1 promoter, where it promotes the recruitment of 19S regulatory complex through dissociation of the proteasome 26S. This presumably promotes provirus transcription efficiency. Protects SUPT6H from proteasomal degradation. {ECO:0000269|PubMed:15831487, ECO:0000269|PubMed:17289585, ECO:0000269|PubMed:22316138}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in kidney, brain and testis. {ECO:0000269|PubMed:15831487}.; myocardium;medulla oblongata;ovary;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; medulla oblongata;thalamus;testis - interstitial;occipital lobe;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;parietal lobe;cingulate cortex; 0.25014 0.10385 0.240763792 69.36777542 1949.66297 8.12469 PABPC1 0.999692442888147 0.00030755699082751 1.21026042493738e-10 poly(A) binding protein, cytoplasmic 1 FUNCTION: Binds the poly(A) tail of mRNA, including that of its own transcript. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA- binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding- region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability (PubMed:25480299). {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:17212783, ECO:0000269|PubMed:18447585, ECO:0000269|PubMed:20573744, ECO:0000269|PubMed:25480299}.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; testis - interstitial;adipose tissue;testis - seminiferous tubule;trachea;tongue;salivary gland;tumor;testis;white blood cells;whole blood;tonsil; 0.49883 0.45280 -0.383807564 27.41802312 3992.89486 12.49537 PABPC1L 0.993349750139363 0.00665003187334357 2.17987293939796e-07 poly(A) binding protein, cytoplasmic 1-like . . . ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;gum;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;lens;skeletal muscle;bile duct;breast;lung;placenta;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;pancreas;globus pallidus;tumor;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.15102 0.13776 0.068033485 59.0351498 1817.63152 7.86174 PABPC1L2A 0.343427413800262 0.485436453741489 0.171136132458248 poly(A) binding protein, cytoplasmic 1-like 2A . . . . . 0.15542 0.14229 . . . . PABPC1L2B . . . poly(A) binding protein, cytoplasmic 1-like 2B . . . . . 0.19306 0.14229 . . . . PABPC1L2B-AS1 . . . PABPC1L2B antisense RNA 1 (head to head) . . . . . . . . . . . PABPC1P1 . . . poly(A) binding protein, cytoplasmic 1 pseudogene 1 . . . . . . . . . . . PABPC1P2 . . . poly(A) binding protein, cytoplasmic 1 pseudogene 2 . . . . . 0.08062 . . . . . PABPC1P3 . . . poly(A) binding protein, cytoplasmic 1 pseudogene 3 . . . . . . . . . . . PABPC1P4 . . . poly(A) binding protein, cytoplasmic 1 pseudogene 4 . . . . . . . . . . . PABPC1P5 . . . poly(A) binding protein, cytoplasmic 1 pseudogene 5 . . . . . . . . . . . PABPC1P6 . . . poly(A) binding protein, cytoplasmic 1 pseudogene 6 . . . . . . . . . . . PABPC1P7 . . . poly(A) binding protein, cytoplasmic 1 pseudogene 7 . . . . . . . . . . . PABPC1P8 . . . poly(A) binding protein, cytoplasmic 1 pseudogene 8 . . . . . . . . . . . PABPC1P9 . . . poly(A) binding protein, cytoplasmic 1 pseudogene 9 . . . . . . . . . . . PABPC1P10 . . . poly(A) binding protein, cytoplasmic 1 pseudogene 10 . . . . . . . . . . . PABPC1P11 . . . poly(A) binding protein, cytoplasmic 1 pseudogene 11 . . . . . . . . . . . PABPC1P12 . . . poly(A) binding protein, cytoplasmic 1 pseudogene 12 . . . . . . . . . . . PABPC1P13 . . . poly(A) binding protein, cytoplasmic 1 pseudogene 13 . . . . . . . . . . . PABPC3 3.37207246022607e-11 0.0448138506039034 0.955186149362376 poly(A) binding protein, cytoplasmic 3 FUNCTION: Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism. Binds poly(A) with a slightly lower affinity as compared to PABPC1.; . TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:11328870}.; medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;thyroid;testis;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;heart;lacrimal gland;islets of Langerhans;oral cavity;muscle;urinary;pharynx;blood;breast;pia mater;lung;cornea;visual apparatus;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;pancreas;fetal liver;adipose tissue;testis - seminiferous tubule;testis;tumor;white blood cells;whole blood;tonsil; 0.97364 0.13848 0.69078985 85.23826374 2676.52948 9.72844 PABPC4 0.992493064403533 0.00750687626683521 5.93296316732998e-08 poly(A) binding protein, cytoplasmic 4 (inducible form) FUNCTION: Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at low levels in resting normal T cells; following T-cell activation, however, mRNA levels are rapidly up-regulated.; . . 0.96930 0.20953 -0.912929826 9.902099552 14.62192 0.52726 PABPC4L 0.220668248086012 0.647506311624677 0.13182544028931 poly(A) binding protein, cytoplasmic 4-like FUNCTION: May bind RNA. {ECO:0000305}.; . . . . . . . . 100.67321 2.17350 PABPC5 0.362703122825983 0.5865374886945 0.0507593884795175 poly(A) binding protein, cytoplasmic 5 FUNCTION: Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in fetal brain and in a range of adult tissues.; ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;lung;visual apparatus;liver;testis;kidney;brain;bladder; . 0.16437 0.13707 -0.05129383 49.75819769 26.71979 0.86445 PABPC5-AS1 . . . PABPC5 antisense RNA 1 . . . . . . . . . . . PABPN1 0.599824569306877 0.398233145949032 0.00194228474409118 poly(A) binding protein, nuclear 1 FUNCTION: Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affinity of poly(A) polymerase for RNA. Is also present at various stages of mRNA metabolism including nucleocytoplasmic trafficking and nonsense-mediated decay (NMD) of mRNA. Cooperates with SKIP to synergistically activate E-box-mediated transcription through MYOD1 and may regulate the expression of muscle-specific genes. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation (By similarity). {ECO:0000250, ECO:0000269|PubMed:11371506, ECO:0000269|PubMed:11689481}.; DISEASE: Oculopharyngeal muscular dystrophy (OPMD) [MIM:164300]: A form of late-onset slowly progressive myopathy characterized by eyelid ptosis, dysphagia and, sometimes by other cranial and limb- muscle involvement. {ECO:0000269|PubMed:12673802}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; ovary;substantia nigra;skin;retina;bone marrow;prostate;ganglion;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;urinary;spinal cord;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;uterus;whole body;oesophagus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;adrenal gland;placenta;duodenum;head and neck;kidney;stomach; amygdala;whole brain;testis - interstitial;occipital lobe;superior cervical ganglion;medulla oblongata;cerebellum peduncles;temporal lobe;pons;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.05190 0.27247 . . 18.08202 0.63078 PABPN1L 2.65471049687625e-11 0.00553015877413551 0.994469841199317 poly(A) binding protein, nuclear 1-like (cytoplasmic) FUNCTION: Binds the poly(A) tail of mRNA. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in various adult tissues. {ECO:0000269|PubMed:18483763}.; . . . . 1.618658506 95.99551781 218.57109 3.19631 PABX . . . pseudoautosomal boundary region, X-linked . . . . . . . . . . . PABY . . . pseudoautosomal boundary region, Y-linked . . . . . . . . . . . PACERR . . . PTGS2 antisense NFKB1 complex-mediated expression regulator RNA . . . . . . . . . . . PACRG 0.000104676937493315 0.811798152811216 0.18809717025129 PARK2 co-regulated FUNCTION: Suppresses cell death induced by accumulation of unfolded Pael receptor (Pael-R, a substrate of Parkin). Facilitates the formation of inclusions consisting of Pael-R, molecular chaperones, protein degradation molecules and itself when proteasome is inhibited. May play an important role in the formation of Lewy bodies and protection of dopaminergic neurons against Parkinson disease. {ECO:0000269|PubMed:14532270}.; . TISSUE SPECIFICITY: Expressed in all immune tissues, spleen, lymph nodes, thymus, tonsils, leukocyte and bone marrow. Expressed also in heart, brain, skeletal muscle, kidney, lung and pancreas. Expressed in primary Schwann cells and very weakly by monocyte- derived macrophages the primary host cells of Mycobacterium leprae, the causative agent of leprosy. Component of Lewy bodies, intraneuronal inclusions found in the brain of Parkinson disease patients. {ECO:0000269|PubMed:14737177}.; unclassifiable (Anatomical System);lung;endometrium;nasopharynx;pituitary gland;testis;kidney; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.11571 0.17324 -0.404032746 26.53338051 57.10759 1.52201 PACRG-AS1 . . . PACRG antisense RNA 1 . . . . . . . . . . . PACRG-AS2 . . . PACRG antisense RNA 2 . . . . . . . . . . . PACRG-AS3 . . . PACRG antisense RNA 3 . . . . . . . . . . . PACRGL 9.13794781278667e-08 0.168250679715419 0.831749228905102 PARK2 co-regulated like . . . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;blood;skeletal muscle;lung;placenta;visual apparatus;alveolus;liver;spleen;kidney;stomach; . 0.12908 . 0.371224249 75.12384996 91.07162 2.05321 PACS1 0.999906351685189 9.36483134592207e-05 1.35179936117096e-12 phosphofurin acidic cluster sorting protein 1 FUNCTION: Coat protein that is involved in the localization of trans-Golgi network (TGN) membrane proteins that contain acidic cluster sorting motifs. Controls the endosome-to-Golgi trafficking of furin and mannose-6-phosphate receptor by connecting the acidic-cluster-containing cytoplasmic domain of these molecules with the adapter-protein complex-1 (AP-1) of endosomal clathrin- coated membrane pits. Involved in HIV-1 nef-mediated removal of MHC-I from the cell surface to the TGN. {ECO:0000269|PubMed:11331585}.; DISEASE: Mental retardation, autosomal dominant 17 (MRD17) [MIM:615009]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD17 patients have intellectual disability in combination with distinct craniofacial features and genital abnormalities. {ECO:0000269|PubMed:23159249}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;pineal body;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; dorsal root ganglion;superior cervical ganglion;adrenal cortex;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin; 0.26293 0.11490 -1.087493118 7.106628922 47.23702 1.33233 PACS2 0.999324515491581 0.000675484341887352 1.66531841324838e-10 phosphofurin acidic cluster sorting protein 2 FUNCTION: Multifunctional sorting protein that controls the endoplasmic reticulum (ER)-mitochondria communication, including the apposition of mitochondria with the ER and ER homeostasis. In addition, in response to apoptic inducer, translocates BIB to mitochondria, which initiates a sequence of events including the formation of mitochondrial truncated BID, the release of cytochrome c, the activation of caspase-3 thereby causing cell death. May also be involved in ion channel trafficking, directing acidic cluster-containing ion channels to distinct subcellular compartments. {ECO:0000269|PubMed:15692563, ECO:0000269|PubMed:15692567}.; . TISSUE SPECIFICITY: Broadly expressed, with greatest levels in skeletal muscle followed by heart, brain, pancreas and testis. {ECO:0000269|PubMed:15692567}.; medulla oblongata;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;synovium;bone;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;placenta;hippocampus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;thymus; amygdala;medulla oblongata;hypothalamus;spinal cord;prefrontal cortex;caudate nucleus;skeletal muscle; 0.21981 0.13261 -0.725642751 14.24274593 817.87625 5.61917 PACSIN1 0.991339222233708 0.00865872271544928 2.0550508424042e-06 protein kinase C and casein kinase substrate in neurons 1 FUNCTION: Plays a role in the reorganization of the microtubule cytoskeleton via its interaction with MAPT; this decreases microtubule stability and inhibits MAPT-induced microtubule polymerization. Plays a role in cellular transport processes by recruiting DNM1, DNM2 and DNM3 to membranes. Plays a role in the reorganization of the actin cytoskeleton and in neuron morphogenesis via its interaction with COBL and WASL, and by recruiting COBL to the cell cortex. Plays a role in the regulation of neurite formation, neurite branching and the regulation of neurite length. Required for normal synaptic vesicle endocytosis; this process retrieves previously released neurotransmitters to accommodate multiple cycles of neurotransmission. Required for normal excitatory and inhibitory synaptic transmission (By similarity). Binds to membranes via its F-BAR domain and mediates membrane tubulation. {ECO:0000250, ECO:0000269|PubMed:19549836, ECO:0000269|PubMed:22573331, ECO:0000269|PubMed:23236520}.; . TISSUE SPECIFICITY: Highly expressed in brain and, at much lower levels, in heart and pancreas. {ECO:0000269|PubMed:11179684}.; unclassifiable (Anatomical System);amygdala;lymph node;fovea centralis;choroid;lens;retina;uterus;prostate;optic nerve;lung;frontal lobe;macula lutea;visual apparatus;testis;germinal center;brain;tonsil;cerebellum; amygdala;dorsal root ganglion;whole brain;thalamus;superior cervical ganglion;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.29818 0.20704 -0.137658575 43.57159707 108.56082 2.26081 PACSIN2 0.270395757339363 0.72938364555749 0.000220597103147422 protein kinase C and casein kinase substrate in neurons 2 FUNCTION: Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle- mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus. May also play a role in the formation of caveolae at the cell membrane. Recruits DNM2 to caveolae, and thereby plays a role in caveola-mediated endocytosis. {ECO:0000269|PubMed:21610094, ECO:0000269|PubMed:21693584, ECO:0000269|PubMed:23129763, ECO:0000269|PubMed:23236520, ECO:0000269|PubMed:23596323}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:11179684}.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.24823 0.20703 0.044168103 57.40740741 250.49463 3.41008 PACSIN3 0.0167930476176259 0.978273746212628 0.00493320616974631 protein kinase C and casein kinase substrate in neurons 3 FUNCTION: Plays a role in endocytosis and regulates internalization of plasma membrane proteins. Overexpression impairs internalization of SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:11082044}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in heart and skeletal muscle, intermediate levels in placenta, liver and pancreas, and very low levels in brain, lung and kidney. {ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:11179684}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; temporal lobe;adrenal cortex;pons;skeletal muscle;parietal lobe; 0.49122 0.20173 -0.532670911 20.78320359 1052.93556 6.23032 PADI1 5.26823569922429e-11 0.201148236770241 0.798851763177077 peptidyl arginine deiminase, type I FUNCTION: Catalyzes the deimination of arginine residues of proteins. {ECO:0000250}.; . TISSUE SPECIFICITY: Epidermis, prostate, testis, placenta, spleen and thymus. {ECO:0000269|PubMed:12416996}.; . . 0.18537 0.11110 -0.459259448 23.69072895 385.00713 4.13435 PADI2 0.000124031218347057 0.997856841262624 0.00201912751902852 peptidyl arginine deiminase, type II FUNCTION: Catalyzes the deimination of arginine residues of proteins. {ECO:0000250}.; . . . . 0.12376 0.13983 -0.50335344 21.80938901 199.41631 3.05180 PADI3 4.68791671509589e-10 0.348282167928484 0.651717831602725 peptidyl arginine deiminase, type III FUNCTION: Catalyzes the deimination of arginine residues of proteins.; . TISSUE SPECIFICITY: Hair follicles, and epidermis at very low levels.; . . 0.48688 0.13071 1.851941967 97.1455532 1956.43372 8.13914 PADI4 1.30424837822011e-09 0.547876115664516 0.452123883031236 peptidyl arginine deiminase, type IV FUNCTION: Catalyzes the citrullination/deimination of arginine residues of proteins such as histones, thereby playing a key role in histone code and regulation of stem cell maintenance. Citrullinates histone H1 at 'Arg-54' (to form H1R54ci), histone H3 at 'Arg-2', 'Arg-8', 'Arg-17' and/or 'Arg-26' (to form H3R2ci, H3R8ci, H3R17ci, H3R26ci, respectively) and histone H4 at 'Arg-3' (to form H4R3ci). Acts as a key regulator of stem cell maintenance by mediating citrullination of histone H1: citrullination of 'Arg- 54' of histone H1 (H1R54ci) results in H1 displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. Promotes profound chromatin decondensation during the innate immune response to infection in neutrophils by mediating formation of H1R54ci. Citrullination of histone H3 prevents their methylation by CARM1 and HRMT1L2/PRMT1 and represses transcription. Citrullinates EP300/P300 at 'Arg-2142', which favors its interaction with NCOA2/GRIP1. {ECO:0000269|PubMed:15339660, ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:15731352, ECO:0000269|PubMed:16567635, ECO:0000269|PubMed:18209087, ECO:0000269|PubMed:21245532}.; DISEASE: Rheumatoid arthritis (RA) [MIM:180300]: An inflammatory disease with autoimmune features and a complex genetic component. It primarily affects the joints and is characterized by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures. {ECO:0000269|PubMed:12833157}. Note=The gene represented in this entry may be involved in disease pathogenesis. The association to rheumatoid arthritis was initially thought to result from increased citrullination of target proteins (PubMed:12833157). However, variants that have been associated to rheumatoid arthritis (Ser-55, Ala-82 and Ala-112) do not affect the catalytic activity or the citrullination activity of PADI4, suggesting that these variants may affect the mRNA stability rather than the protein (PubMed:21245532). {ECO:0000269|PubMed:12833157, ECO:0000269|PubMed:21245532}.; TISSUE SPECIFICITY: Expressed in eosinophils and neutrophils, not expressed in peripheral monocytes or lymphocytes. {ECO:0000269|PubMed:11435484}.; bone marrow; skeletal muscle;bone marrow; 0.08126 . 2.230515739 98.17173862 609.89444 4.99213 PADI6 . . . peptidyl arginine deiminase, type VI FUNCTION: Catalyzes the deimination of arginine residues of proteins. May be involved in cytoskeletal reorganization in the egg and early embryo (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ovary, testis and peripheral blood leukocytes. {ECO:0000269|PubMed:15625577}.; . . 0.06559 0.10000 . . . . PAEP 0.0316183735787673 0.81467678550802 0.153704840913213 progestagen-associated endometrial protein FUNCTION: This protein is, quantitatively, the main protein synthesized and secreted in the endometrium from mid-luteal phase of the menstrual cycle and during the first semester of pregnancy.; . . unclassifiable (Anatomical System);uterus;prostate;lung;whole body;ovary;heart;placenta;testis;parathyroid;skin; uterus;superior cervical ganglion;placenta;skeletal muscle;parietal lobe; 0.08291 0.20405 0.349177632 74.18023119 19.13589 0.65938 PAF1 0.845472629917094 0.154522528709509 4.84137339666061e-06 PAF1 homolog, Paf1/RNA polymerase II complex component FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non- phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Connects PAF1C with the RNF20/40 E3 ubiquitin-protein ligase complex. Involved in polyadenylation of mRNA precursors. Has oncogenic activity in vivo and in vitro. {ECO:0000269|PubMed:16491129, ECO:0000269|PubMed:19410543, ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742, ECO:0000269|PubMed:20541477, ECO:0000269|PubMed:21329879, ECO:0000269|PubMed:22419161}.; . . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;placenta;duodenum;head and neck;kidney;stomach; whole brain;testis - interstitial;thalamus;testis - seminiferous tubule;hypothalamus;testis; 0.43419 0.22085 -0.291981272 33.20358575 45.70516 1.29897 PAFAH1B1 0.99963285344523 0.000367145633958329 9.20812115446463e-10 platelet activating factor acetylhydrolase 1b regulatory subunit 1 FUNCTION: Required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet- activating factor (PAF) by removing the acetyl group at the SN-2 position (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. {ECO:0000250, ECO:0000269|PubMed:15173193}.; DISEASE: Lissencephaly 1 (LIS1) [MIM:607432]: A classical lissencephaly. It is characterized by agyria or pachygyria and disorganization of the clear neuronal lamination of normal six- layered cortex. The cortex is abnormally thick and poorly organized with 4 primitive layers. Associated with enlarged and dysmorphic ventricles and often hypoplasia of the corpus callosum. {ECO:0000269|PubMed:11502906, ECO:0000269|PubMed:15007136, ECO:0000269|PubMed:9063735}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Subcortical band heterotopia (SBH) [MIM:607432]: SBH is a mild brain malformation of the lissencephaly spectrum. It is characterized by bilateral and symmetric plates or bands of gray matter found in the central white matter between the cortex and cerebral ventricles, cerebral convolutions usually appearing normal. {ECO:0000269|PubMed:10441340, ECO:0000269|PubMed:14581661}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Miller-Dieker lissencephaly syndrome (MDLS) [MIM:247200]: A contiguous gene deletion syndrome of chromosome 17p13.3, characterized by classical lissencephaly and distinct facial features. Additional congenital malformations can be part of the condition. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Fairly ubiquitous expression in both the frontal and occipital areas of the brain.; . . 0.80941 0.50577 -0.405853867 26.23260203 4.95413 0.18439 PAFAH1B1P1 . . . platelet activating factor acetylhydrolase 1b regulatory subunit 1 pseudogene 1 . . . . . . . . . . . PAFAH1B1P2 . . . platelet activating factor acetylhydrolase 1b regulatory subunit 1 pseudogene 2 . . . . . . . . . . . PAFAH1B2 0.962029472445706 0.0378923393836712 7.81881706223275e-05 platelet activating factor acetylhydrolase 1b catalytic subunit 2 FUNCTION: Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9144386}.; unclassifiable (Anatomical System);sympathetic chain;colon;blood;skeletal muscle;bone marrow;lung;endometrium;placenta;thyroid;visual apparatus;liver;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.65851 0.15588 -0.075159878 47.78839349 4.02051 0.14794 PAFAH1B3 0.0210579182279272 0.906607992632308 0.0723340891397645 platelet activating factor acetylhydrolase 1b catalytic subunit 3 FUNCTION: Inactivates paf by removing the acetyl group at the sn-2 position. This is a catalytic subunit. Plays an important role during the development of brain.; . TISSUE SPECIFICITY: In the adult, expressed in brain, skeletal muscle, kidney, thymus, spleen, colon, testis, ovary and peripheral blood leukocytes. In the fetus, highest expression occurs in brain.; myocardium;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; fetal brain;tumor;white blood cells;cerebellum; 0.49007 0.14502 -0.295622497 32.61972163 6.82839 0.25352 PAFAH2 2.68539651867445e-07 0.497624678366765 0.502375053093584 platelet activating factor acetylhydrolase 2 FUNCTION: Has a marked selectivity for phospholipids with short acyl chains at the sn-2 position. May share a common physiologic function with the plasma-type enzyme.; . TISSUE SPECIFICITY: Broadly expressed in different tissues, but high in B- and T-lymphocytes. In brain, expression is restricted to amygdala and frontal cortex.; . . 0.13153 . -0.402212257 26.7338995 141.07833 2.59230 PAG1 0.0108372777343039 0.946925777144078 0.0422369451216181 phosphoprotein membrane anchor with glycosphingolipid microdomains 1 FUNCTION: Negatively regulates TCR (T-cell antigen receptor)- mediated signaling in T-cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Promotes CSK activation and recruitment to lipid rafts, which results in LCK inhibition. Inhibits immunological synapse formation by preventing dynamic arrangement of lipid raft proteins. May be involved in cell adhesion signaling. {ECO:0000269|PubMed:10790433}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Present in germinal center B-cells, plasma cells, T-cells, monocytes and platelets (at protein level). {ECO:0000269|PubMed:10790433, ECO:0000269|PubMed:16160011}.; lymphoreticular;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;testis;germinal center;dura mater;brain;unclassifiable (Anatomical System);meninges;cartilage;blood;lens;skeletal muscle;breast;lung;pia mater;placenta;macula lutea;liver;kidney;stomach; occipital lobe;cerebellum peduncles;placenta;white blood cells;parietal lobe;tonsil;bone marrow;thymus; 0.31303 0.14344 -0.66859065 15.76433121 44.4288 1.27418 PAGE1 0.389289495504708 0.568257236648625 0.0424532678466669 PAGE family member 1 . . TISSUE SPECIFICITY: Isolated from prostate cancer cell lines; expression associated with progression to androgen insensitive phenotype. Expressed in normal testis and at lower level in normal placenta.; . . 0.15185 0.09600 0.569646743 81.88841708 79.9222 1.88994 PAGE2 0.201620359247133 0.648020177983849 0.150359462769017 PAGE family member 2 . . . . . . 0.03208 0.435547893 77.45340882 1.70768 0.05587 PAGE2B 0.203304959214182 0.648085015013889 0.148610025771929 PAGE family member 2B . . . . . . . 0.3455435 73.78509082 21.85826 0.73525 PAGE3 0.050523543150726 0.690462112900729 0.259014343948545 PAGE family member 3 . . . . . 0.10062 . . . 30.35599 0.96810 PAGE4 0.648195518447356 0.325782457043927 0.0260220245087161 PAGE family member 4 . . TISSUE SPECIFICITY: Preferentially expressed in normal male and female reproductive tissues, prostate, testis, fallopian tube, uterus, and placenta, as well as in prostate cancer, testicular cancer, and uterine cancer.; uterus;prostate;lung;ovary;heart;placenta;liver;testis;parathyroid;spleen;skin; superior cervical ganglion;placenta;trigeminal ganglion;skeletal muscle; 0.29425 0.09777 0.057118534 57.99716914 1.17841 0.03344 PAGE5 0.0712543126666454 0.740976769669533 0.187768917663822 PAGE family member 5 . . . placenta;skin; . 0.09840 . 0.501689326 79.7888653 29.1887 0.93300 PAGR1 0.500965910941921 0.479492393424287 0.0195416956337922 PAXIP1 associated glutamate-rich protein 1 . . . . . 0.20386 0.24282 . . 21.15276 0.71504 PAH 1.19519744629961e-10 0.307448665079143 0.692551334801337 phenylalanine hydroxylase . DISEASE: Phenylketonuria (PKU) [MIM:261600]: Autosomal recessive inborn error of phenylalanine metabolism, due to severe phenylalanine hydroxylase deficiency. It is characterized by blood concentrations of phenylalanine persistently above 1200 mumol (normal concentration 100 mumol) which usually causes mental retardation (unless low phenylalanine diet is introduced early in life). They tend to have light pigmentation, rashes similar to eczema, epilepsy, extreme hyperactivity, psychotic states and an unpleasant 'mousy' odor. {ECO:0000269|PubMed:10200057, ECO:0000269|PubMed:10679941, ECO:0000269|PubMed:11180595, ECO:0000269|PubMed:11385716, ECO:0000269|PubMed:11461196, ECO:0000269|PubMed:12501224, ECO:0000269|PubMed:1355066, ECO:0000269|PubMed:1363837, ECO:0000269|PubMed:1363838, ECO:0000269|PubMed:1671810, ECO:0000269|PubMed:1672290, ECO:0000269|PubMed:1672294, ECO:0000269|PubMed:1679030, ECO:0000269|PubMed:1709636, ECO:0000269|PubMed:1975559, ECO:0000269|PubMed:2014802, ECO:0000269|PubMed:22513348, ECO:0000269|PubMed:22526846, ECO:0000269|PubMed:23792259, ECO:0000269|PubMed:2564729, ECO:0000269|PubMed:2615649, ECO:0000269|PubMed:2840952, ECO:0000269|PubMed:7833954, ECO:0000269|PubMed:8068076, ECO:0000269|PubMed:8406445, ECO:0000269|PubMed:8889590, ECO:0000269|PubMed:9048935, ECO:0000269|PubMed:9101291, ECO:0000269|PubMed:9452061, ECO:0000269|PubMed:9452062, ECO:0000269|PubMed:9521426, ECO:0000269|PubMed:9600453, ECO:0000269|PubMed:9792407, ECO:0000269|PubMed:9950317}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Non-phenylketonuria hyperphenylalaninemia (Non-PKU HPA) [MIM:261600]: Mild form of phenylalanine hydroxylase deficiency characterized by phenylalanine levels persistently below 600 mumol, which allows normal intellectual and behavioral development without treatment. Non-PKU HPA is usually caused by the combined effect of a mild hyperphenylalaninemia mutation and a severe one. {ECO:0000269|PubMed:1358789, ECO:0000269|PubMed:8088845, ECO:0000269|PubMed:8098245, ECO:0000269|PubMed:9521426, ECO:0000269|PubMed:9852673}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hyperphenylalaninemia (HPA) [MIM:261600]: Mildest form of phenylalanine hydroxylase deficiency. {ECO:0000269|PubMed:11385716, ECO:0000269|PubMed:11935335, ECO:0000269|PubMed:12501224, ECO:0000269|PubMed:1358789, ECO:0000269|PubMed:23792259, ECO:0000269|PubMed:8088845, ECO:0000269|PubMed:8098245, ECO:0000269|PubMed:9521426, ECO:0000269|PubMed:9852673}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;whole body;islets of Langerhans;liver;testis;spleen;kidney;mammary gland;gall bladder; superior cervical ganglion;fetal liver;liver;ciliary ganglion;kidney; 0.13031 0.85678 -0.709045403 14.673272 115.70583 2.33963 PAICS 0.0683141233819019 0.917925756020774 0.0137601205973241 phosphoribosylaminoimidazole carboxylase; phosphoribosylaminoimidazolesuccinocarboxamide synthase . . . ovary;skin;retina;bone marrow;prostate;optic nerve;gum;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;synovium;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;pia mater;lung;mesenchyma;adrenal gland;placenta;hippocampus;duodenum;kidney;stomach; superior cervical ganglion;tumor;atrioventricular node; 0.88960 0.21066 1.038098315 91.20665251 355.28243 3.98618 PAICSP1 . . . phosphoribosylaminoimidazole carboxylase, phosphoribosylaminoimidazole succinocarboxamide synthetase pseudogene 1 . . . . . . . . . . . PAICSP2 . . . phosphoribosylaminoimidazole carboxylase, phosphoribosylaminoimidazole succinocarboxamide synthetase pseudogene 2 . . . . . . . . . . . PAICSP3 . . . phosphoribosylaminoimidazole carboxylase, phosphoribosylaminoimidazole succinocarboxamide synthetase pseudogene 3 . . . . . . . . . . . PAICSP4 . . . phosphoribosylaminoimidazole carboxylase, phosphoribosylaminoimidazole succinocarboxamide synthetase pseudogene 4 . . . . . . . . . . . PAICSP5 . . . phosphoribosylaminoimidazole carboxylase, phosphoribosylaminoimidazole succinocarboxamide synthetase pseudogene 5 . . . . . . . . . . . PAICSP6 . . . phosphoribosylaminoimidazole carboxylase, phosphoribosylaminoimidazole succinocarboxamide synthetase pseudogene 6 . . . . . . . . . . . PAICSP7 . . . phosphoribosylaminoimidazole carboxylase, phosphoribosylaminoimidazole succinocarboxamide synthetase pseudogene 7 . . . . . . . . . . . PAIP1 0.994278972453478 0.00572087666377646 1.50882745883882e-07 poly(A) binding protein interacting protein 1 FUNCTION: Acts as a coactivator in the regulation of translation initiation of poly(A)-containing mRNAs. Its stimulatory activity on translation is mediated via its action on PABPC1. Competes with PAIP2 for binding to PABPC1. Its association with EIF4A and PABPC1 may potentiate contacts between mRNA termini. May also be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:9548260}.; . . ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;thyroid;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;urinary;blood;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;liver;head and neck;kidney;mammary gland;stomach; . 0.57673 0.10619 -0.427900189 25.14744043 26.70534 0.86391 PAIP1P1 . . . poly(A) binding protein interacting protein 1 pseudogene 1 . . . . . . . . . . . PAIP2 0.79947261034215 0.195010811108424 0.00551657854942593 poly(A) binding protein interacting protein 2 FUNCTION: Acts as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. Its inhibitory activity on translation is mediated via its action on PABPC1. Displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. Its association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization. {ECO:0000269|PubMed:11172725}.; . TISSUE SPECIFICITY: Expressed at highest level in testis, but also abundant in brain, cervix, lung, ovary, placenta, adipose tissue, thymus and thyroid. {ECO:0000269|PubMed:16804161}.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;bladder;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;larynx;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta; . 0.54489 . 0.035072054 56.2514744 4.37129 0.15898 PAIP2B 0.0917531004004723 0.766439806276359 0.141807093323168 poly(A) binding protein interacting protein 2B FUNCTION: Inhibits translation of capped and polyadenylated mRNAs by displacing PABPC1 from the poly(A) tail. {ECO:0000269|PubMed:16804161}.; . TISSUE SPECIFICITY: Expressed in brain, cervix, heart, liver, ovary, kidney, prostate and testis. {ECO:0000269|PubMed:16804161}.; ovary;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;atrium;frontal lobe;thyroid;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;oral cavity;spinal cord;blood;lens;skeletal muscle;lung;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; amygdala;dorsal root ganglion;occipital lobe;medulla oblongata;thalamus;hypothalamus;spinal cord;prefrontal cortex;pons;caudate nucleus;cingulate cortex;parietal lobe;cerebellum; 0.39472 0.11262 -0.119252484 44.53880632 29.57337 0.94485 PAK1 0.670970123358133 0.329021272069359 8.60457250836789e-06 p21 protein (Cdc42/Rac)-activated kinase 1 FUNCTION: Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus. In podocytes, promotes NR3C2 nuclear localization. Required for atypical chemokine receptor ACKR2- induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F- actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation. Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion (PubMed:25766321). {ECO:0000269|PubMed:10551809, ECO:0000269|PubMed:11733498, ECO:0000269|PubMed:12624090, ECO:0000269|PubMed:12876277, ECO:0000269|PubMed:14585966, ECO:0000269|PubMed:15611088, ECO:0000269|PubMed:15831477, ECO:0000269|PubMed:15833848, ECO:0000269|PubMed:16278681, ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089, ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:23633677, ECO:0000269|PubMed:25766321, ECO:0000269|PubMed:8805275, ECO:0000269|PubMed:9032240, ECO:0000269|PubMed:9395435, ECO:0000269|PubMed:9528787}.; . TISSUE SPECIFICITY: Overexpressed in gastric cancer cells and tissues (at protein level) (PubMed:25766321). {ECO:0000269|PubMed:25766321}.; smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);small intestine;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; subthalamic nucleus;occipital lobe;cerebellum peduncles;pons; 0.92793 0.34632 -0.60427181 17.74593064 13.31064 0.48361 PAK1IP1 0.368163912185113 0.629420477966172 0.00241560984871526 PAK1 interacting protein 1 FUNCTION: Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which have been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42. {ECO:0000269|PubMed:11371639}.; . TISSUE SPECIFICITY: Expressed in brain, colon, heart, kidney, liver, lung, muscle, peripheral blood leukocytes, placenta, small intestine, spleen and thymus. {ECO:0000269|PubMed:11371639}.; . . 0.59576 0.12304 0.150760231 64.51403633 205.11068 3.09461 PAK2 0.938688563524374 0.0613092699819085 2.16649371706767e-06 p21 protein (Cdc42/Rac)-activated kinase 2 FUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Full-length PAK2 stimulates cell survival and cell growth. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Phosphorylates JUN and plays an important role in EGF- induced cell proliferation. Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP. Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis. On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway. Caspase- activated PAK2 phosphorylates MKNK1 and reduces cellular translation. {ECO:0000269|PubMed:12853446, ECO:0000269|PubMed:15234964, ECO:0000269|PubMed:16617111, ECO:0000269|PubMed:19923322, ECO:0000269|PubMed:21177766, ECO:0000269|PubMed:21317288, ECO:0000269|PubMed:21724829, ECO:0000269|PubMed:9171063}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Higher levels seen in skeletal muscle, ovary, thymus and spleen.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;oesophagus;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;placenta;hypopharynx;amnion;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;atrioventricular node;whole blood;trigeminal ganglion;skeletal muscle; 0.80630 0.27444 -0.339715008 30.06605331 12.07124 0.43719 PAK3 0.987004716625695 0.0129941585901874 1.12478411716737e-06 p21 protein (Cdc42/Rac)-activated kinase 3 FUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, or cell cycle regulation. Plays a role in dendrite spine morphogenesis as well as synapse formation and plasticity. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Additionally, phosphorylates TNNI3/troponin I to modulate calcium sensitivity and relaxation kinetics of thin myofilaments. May also be involved in early neuronal development. {ECO:0000269|PubMed:21177870}.; DISEASE: Mental retardation, X-linked 30 (MRX30) [MIM:300558]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non- syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. {ECO:0000269|PubMed:10946356, ECO:0000269|PubMed:12884430, ECO:0000269|PubMed:9731525}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Restricted to the nervous system. Highly expressed in postmitotic neurons of the developing and postnatal cerebral cortex and hippocampus. {ECO:0000269|PubMed:12890786}.; unclassifiable (Anatomical System);lung;whole body;adrenal gland;islets of Langerhans;placenta;liver;pituitary gland;brain;retina; amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;atrioventricular node;pons;subthalamic nucleus;trachea;prefrontal cortex;appendix;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.47997 . -0.405853867 26.23260203 6.17161 0.23308 PAK4 0.701123853426304 0.298720216947658 0.000155929626038043 p21 protein (Cdc42/Rac)-activated kinase 4 FUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN. {ECO:0000269|PubMed:11278822, ECO:0000269|PubMed:11313478, ECO:0000269|PubMed:14560027, ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:20507994, ECO:0000269|PubMed:20631255, ECO:0000269|PubMed:20805321}.; . TISSUE SPECIFICITY: Highest expression in prostate, testis and colon.; medulla oblongata;ovary;salivary gland;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;bone;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;lens;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;peripheral nerve; superior cervical ganglion;prostate;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;kidney;trigeminal ganglion;parietal lobe; 0.48044 0.30047 -0.488577883 22.64685067 120.47431 2.39092 PAK6 0.00128179098336292 0.990351368849981 0.0083668401666559 p21 protein (Cdc42/Rac)-activated kinase 6 FUNCTION: Serine/threonine protein kinase that plays a role in the regulation of gene transcription. The kinase activity is induced by various effectors including AR or MAP2K6/MAPKK6. Phosphorylates the DNA-binding domain of androgen receptor/AR and thereby inhibits AR-mediated transcription. Inhibits also ESR1-mediated transcription. May play a role in cytoskeleton regulation by interacting with IQGAP1. May protect cells from apoptosis through phosphorylation of BAD. {ECO:0000269|PubMed:14573606, ECO:0000269|PubMed:20054820}.; . TISSUE SPECIFICITY: Selectively expressed in brain and testis, with lower levels in multiple tissues including prostate and breast. {ECO:0000269|PubMed:11278661, ECO:0000269|PubMed:11773441}.; unclassifiable (Anatomical System);medulla oblongata;smooth muscle;ovary;islets of Langerhans;colon;parathyroid;prostate;lung;endometrium;placenta;thyroid;testis;kidney;brain;cerebellum; superior cervical ganglion;pons;cingulate cortex; 0.24042 0.21894 0.738527175 86.34111819 1078.09603 6.29512 PAK7 0.998363566588201 0.00163639826064323 3.51511554757178e-08 p21 protein (Cdc42/Rac)-activated kinase 7 FUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions. {ECO:0000269|PubMed:12897128, ECO:0000269|PubMed:16014608, ECO:0000269|PubMed:16581795, ECO:0000269|PubMed:18465753, ECO:0000269|PubMed:20564219}.; . TISSUE SPECIFICITY: Predominantly expressed in brain.; unclassifiable (Anatomical System);hypothalamus;fovea centralis;choroid;lens;retina;uterus;optic nerve;whole body;lung;frontal lobe;hippocampus;macula lutea;testis;brain; amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;cerebellum peduncles;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.42358 0.23310 -0.220384297 37.6032083 1365.4426 6.93191 PALB2 1.32628496864351e-10 0.770851368791479 0.229148631075892 partner and localizer of BRCA2 FUNCTION: Plays a critical role in homologous recombination repair (HRR) through its ability to recruit BRCA2 and RAD51 to DNA breaks. Strongly stimulates the DNA strand-invasion activity of RAD51, stabilizes the nucleoprotein filament against a disruptive BRC3-BRC4 polypeptide and helps RAD51 to overcome the suppressive effect of replication protein A (RPA). Functionally cooperates with RAD51AP1 in promoting of D-loop formation by RAD51. Serves as the molecular scaffold in the formation of the BRCA1-PALB2-BRCA2 complex which is essential for homologous recombination. Via its WD repeats is proposed to scaffold a HR complex containing RAD51C and BRCA2 which is thought to play a role in HR-mediated DNA repair. Essential partner of BRCA2 that promotes the localization and stability of BRCA2. Also enables its recombinational repair and checkpoint functions of BRCA2. May act by promoting stable association of BRCA2 with nuclear structures, allowing BRCA2 to escape the effects of proteasome-mediated degradation. Binds DNA with high affinity for D loop, which comprises single-stranded, double-stranded and branched DNA structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with BRCA2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. {ECO:0000269|PubMed:16793542, ECO:0000269|PubMed:19369211, ECO:0000269|PubMed:19423707, ECO:0000269|PubMed:20871615, ECO:0000269|PubMed:20871616, ECO:0000269|PubMed:22941656, ECO:0000269|PubMed:24141787, ECO:0000269|PubMed:24485656}.; DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:17287723, ECO:0000269|PubMed:22241545}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Breast cancer susceptibility is strongly associated with PALB2 truncating mutations. Conversely, rare missense mutations do not strongly influence breast cancer risk (PubMed:22241545). {ECO:0000269|PubMed:22241545}.; DISEASE: Fanconi anemia complementation group N (FANCN) [MIM:610832]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:17200672}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pancreatic cancer 3 (PNCA3) [MIM:613348]: A malignant neoplasm of the pancreas. Tumors can arise from both the exocrine and endocrine portions of the pancreas, but 95% of them develop from the exocrine portion, including the ductal epithelium, acinar cells, connective tissue, and lymphatic tissue. {ECO:0000269|PubMed:19264984}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymphoreticular;lymph node;cartilage;colon;skin;skeletal muscle;pancreas;whole body;lung;bone;thyroid;testis;cervix;germinal center;kidney;brain;stomach; superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;pons; 0.16352 0.27931 0.321464691 72.85326728 296.6407 3.67511 PALD1 0.000887741362023023 0.998992285438471 0.000119973199505935 phosphatase domain containing, paladin 1 . . TISSUE SPECIFICITY: Expressed in endothelial cells, and in certain larger vessels, in mural cells. In the brain, possibly expressed in microglia. Expressed in peripheral blood mononuclear cells (at protein level). {ECO:0000269|PubMed:22354871}.; . . 0.59302 0.10897 1.214325842 93.08209483 3105.97963 10.60365 PALLD 6.63951548296594e-05 0.999925260432497 8.34441267351915e-06 palladin, cytoskeletal associated protein FUNCTION: Cytoskeletal protein required for organization of normal actin cytoskeleton. Roles in establishing cell morphology, motility, cell adhesion and cell-extracellular matrix interactions in a variety of cell types. May function as a scaffolding molecule with the potential to influence both actin polymerization and the assembly of existing actin filaments into higher-order arrays. Binds to proteins that bind to either monomeric or filamentous actin. Localizes at sites where active actin remodeling takes place, such as lamellipodia and membrane ruffles. Different isoforms may have functional differences. Involved in the control of morphological and cytoskeletal changes associated with dendritic cell maturation. Involved in targeting ACTN to specific subcellular foci. {ECO:0000269|PubMed:11598191, ECO:0000269|PubMed:15147863, ECO:0000269|PubMed:17537434}.; DISEASE: Pancreatic cancer 1 (PNCA1) [MIM:606856]: A malignant neoplasm of the pancreas. Tumors can arise from both the exocrine and endocrine portions of the pancreas, but 95% of them develop from the exocrine portion, including the ductal epithelium, acinar cells, connective tissue, and lymphatic tissue. {ECO:0000269|PubMed:17194196, ECO:0000269|PubMed:17415588}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=Genetic variations in PALLD may be associated with susceptibility to myocardial infarction. {ECO:0000269|PubMed:16175505}.; TISSUE SPECIFICITY: Detected in both muscle and non-muscle tissues. High expression in prostate, ovary, colon, and kidney. Not detected in spleen, skeletal muscle, lung and peripheral blood lymphocytes (at protein level). Protein is overexpressed in FA6, HPAF, IMIM-PC2, SUIT-2 and PancTu-II sporadic pancreatic cancer cell lines. {ECO:0000269|PubMed:11598191}.; myocardium;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;gall bladder;heart;cartilage;adrenal cortex;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;atrium;larynx;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;lung;cornea;adrenal gland;placenta;duodenum;head and neck;kidney;stomach;aorta; superior cervical ganglion;medulla oblongata;testis - interstitial;adipose tissue;atrioventricular node;pons;skeletal muscle;skin;uterus;uterus corpus;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion; 0.28047 0.11181 0.143271594 63.67067705 2096.91654 8.43392 PALM 0.393531038933643 0.596933844675819 0.00953511639053789 paralemmin FUNCTION: Involved in plasma membrane dynamics and cell process formation. Isoform 1 and isoform 2 are necessary for axonal and dendritic filopodia induction, for dendritic spine maturation and synapse formation in a palmitoylation-dependent manner. {ECO:0000269|PubMed:14978216}.; . TISSUE SPECIFICITY: Widely expressed with highest expression in brain and testis and intermediate expression in heart and adrenal gland.; ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;whole body;frontal lobe;cerebral cortex;iris;testis;brain;unclassifiable (Anatomical System);lymph node;heart;lens;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; amygdala;medulla oblongata;superior cervical ganglion;occipital lobe;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.06315 0.10784 -0.777005578 12.9747582 65.05459 1.65941 PALM2 0.00389317095880877 0.957881889526451 0.0382249395147403 paralemmin 2 . . TISSUE SPECIFICITY: Expressed in infantile heart and muscle, and fibroblasts. {ECO:0000269|PubMed:11478809}.; breast;hypothalamus; . . 0.12902 -0.113792788 45.25831564 62.549 1.61635 PALM2-AKAP2 0.0665179535302839 0.933457080309722 2.4966159993969e-05 PALM2-AKAP2 readthrough FUNCTION: Binds to regulatory subunit (RII) of protein kinase A. May be involved in establishing polarity in signaling systems or in integrating PKA-RII isoforms with downstream effectors to capture, amplify and focus diffuse, trans-cellular signals carried by cAMP (By similarity). {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;larynx;bone;testis;amniotic fluid;germinal center;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;amnion;liver;spleen;head and neck;kidney;mammary gland;aorta;peripheral nerve;thymus; . . . 1.148180302 92.40386884 2618.43206 9.59088 PALM3 . . . paralemmin 3 FUNCTION: ATP-binding protein, which may act as a adapter in the Toll-like receptor (TLR) signaling. {ECO:0000269|PubMed:21187075}.; . . visual apparatus;bladder;stomach; . . . 1.594792159 95.83628214 1531.99318 7.27369 PALMD 0.0369520095811702 0.955626744958893 0.00742124545993653 palmdelphin . . TISSUE SPECIFICITY: Ubiquitous. Most abundant in cardiac and skeletal muscle. {ECO:0000269|PubMed:11707320}.; ovary;colon;parathyroid;vein;skin;retina;uterus;whole body;endometrium;thyroid;bone;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;lacrimal gland;urinary;skeletal muscle;breast;pancreas;pia mater;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach;peripheral nerve; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.80086 0.11019 0.733063566 86.27034678 371.79053 4.06926 PAM 0.0304443970438953 0.969554906122705 6.96833399643426e-07 peptidylglycine alpha-amidating monooxygenase FUNCTION: Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.; . . myocardium;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;ganglion;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;trachea;placenta; 0.58805 0.27052 -0.328796968 30.86223166 352.99827 3.97951 PAM16 0.144011543598339 0.778804604635976 0.0771838517656851 presequence translocase-associated motor 16 homolog (S. cerevisiae) FUNCTION: Regulates ATP-dependent protein translocation into the mitochondrial matrix. Inhibits DNAJC19 stimulation of HSPA9/Mortalin ATPase activity. {ECO:0000269|PubMed:20053669}.; DISEASE: Spondylometaphyseal dysplasia, Megarbane-Dagher-Melike type (SMDMDM) [MIM:613320]: An autosomal recessive disease characterized by pre- and postnatal short stature, developmental delay, dysmorphic facial appearance, narrow chest, prominent abdomen, platyspondyly, and short limbs. {ECO:0000269|PubMed:24786642}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15704001}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;optic nerve;whole body;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;hypothalamus;pineal body;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;caudate nucleus;skeletal muscle; . . 0.391453969 75.87284737 1292.77907 6.76955 PAMR1 4.62835775540526e-21 0.000682611676426069 0.999317388323574 peptidase domain containing associated with muscle regeneration 1 FUNCTION: May play a role in regeneration of skeletal muscle. {ECO:0000250}.; . . ovary;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;endometrium;cerebral cortex;testis;brain;unclassifiable (Anatomical System);cartilage;lens;skeletal muscle;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;spleen;kidney;stomach; uterus corpus;olfactory bulb;smooth muscle;hypothalamus;placenta;spinal cord;liver;prefrontal cortex;trigeminal ganglion; . . -0.501537595 21.83887709 1513.51941 7.23240 PAN2 0.946674806799818 0.0533251926833666 5.16815163154097e-10 PAN2 poly(A) specific ribonuclease subunit FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA when the poly(A) stretch is bound by poly(A)-binding protein (PABP), which is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:14583602, ECO:0000269|PubMed:16284618}.; . . medulla oblongata;ovary;colon;parathyroid;skin;bone marrow;uterus;subthalamic nucleus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis;white blood cells;skeletal muscle; 0.73763 0.10787 -0.617221851 17.44515216 133.50785 2.51039 PAN3 0.999989677110545 1.03228893020409e-05 1.53421959485413e-13 PAN3 poly(A) specific ribonuclease subunit FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA when the poly(A) stretch is bound by poly(A)-binding protein (PABP), which is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with PABP and to miRNA targets via its interaction with GW182 family proteins. {ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:14583602, ECO:0000269|PubMed:23932717}.; . . ovary;colon;skin;uterus;prostate;whole body;endometrium;pituitary gland;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;hypothalamus;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.60810 0.11045 -0.488577883 22.64685067 100.08959 2.16910 PAN3-AS1 . . . PAN3 antisense RNA 1 . . . . . . . . . . . PANCR . . . PITX2 adjacent non-coding RNA . . . . . . . . . . . PANDAR . . . promoter of CDKN1A antisense DNA damage activated RNA . . . . . . . . . . . PANK1 0.00212214971137582 0.978412915305998 0.0194649349826256 pantothenate kinase 1 FUNCTION: Plays a role in the physiological regulation of the intracellular CoA concentration. {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is expressed at high levels in brain, heart, kidney, liver, skeletal muscle and testis. Isoform 2 is detected at much lower levels in kidney, liver, brain and testis and is not detected in heart or skeletal muscle. {ECO:0000269|PubMed:14523052}.; unclassifiable (Anatomical System);heart;hypothalamus;colon;fovea centralis;skin;skeletal muscle;uterus;prostate;whole body;lung;endometrium;larynx;macula lutea;visual apparatus;liver;testis;cervix;head and neck;germinal center;kidney;brain;stomach; dorsal root ganglion;fetal liver;superior cervical ganglion;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;cerebellum; 0.54625 0.11856 0.283038099 71.26680821 936.198 5.93311 PANK2 0.0107918334564396 0.979863257508497 0.00934490903506371 pantothenate kinase 2 FUNCTION: May be the master regulator of the CoA biosynthesis. {ECO:0000250}.; DISEASE: Hypoprebetalipoproteinemia, acanthocytosis, retinitis pigmentosa, and pallidal degeneration (HARP) [MIM:607236]: Rare syndrome with many clinical similarities to PKAN. {ECO:0000269|PubMed:12058097}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11479594}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis;globus pallidus;parietal lobe; 0.46091 0.19230 -0.227663163 37.11370606 668.52907 5.17100 PANK3 0.000282412768333647 0.93576874401443 0.063948843217236 pantothenate kinase 3 FUNCTION: Plays a role in the physiological regulation of the intracellular CoA concentration. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in the liver. {ECO:0000269|PubMed:11479594}.; smooth muscle;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;amygdala;fetal liver;subthalamic nucleus;superior cervical ganglion;fetal brain;temporal lobe;prefrontal cortex;skeletal muscle;cingulate cortex; 0.09997 0.09515 0.215080721 67.91696155 1081.15841 6.30459 PANK4 0.945333401831958 0.0546662699748923 3.28193149951221e-07 pantothenate kinase 4 FUNCTION: Plays a role in the physiological regulation of the intracellular CoA concentration. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in the muscle. {ECO:0000269|PubMed:11479594}.; . . 0.12805 0.12180 -0.971800989 8.946685539 3192.4997 10.77011 PANO1 . . . proapoptotic nucleolar protein 1 FUNCTION: Apoptosis-inducing protein that modulates the tumor suppressor function of CDKN2A/p14ARF. Enhances the stability of CDKN2A/p14ARF protein by protecting it from degradation. May act as a tumor suppressor (PubMed:22094112). {ECO:0000269|PubMed:22094112}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:22094112}.; . . . . . . . . PANX1 0.00309549630219255 0.945442253435796 0.0514622502620109 pannexin 1 FUNCTION: Structural component of the gap junctions and the hemichannels. May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis. {ECO:0000269|PubMed:16908669, ECO:0000269|PubMed:20829356}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;gum;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;kidney; dorsal root ganglion;atrioventricular node; 0.11613 0.11090 0.352813824 74.49280491 791.17388 5.54689 PANX2 0.0149007665484345 0.875833926760201 0.109265306691365 pannexin 2 FUNCTION: Structural component of the gap junctions and the hemichannels. {ECO:0000250}.; . . unclassifiable (Anatomical System);fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;bone;macula lutea;liver;mammary gland;brain;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;cerebellum peduncles;globus pallidus;ciliary ganglion; 0.21680 0.11297 . . 62.28412 1.61023 PANX3 0.00188124156678788 0.903836589047435 0.0942821693857772 pannexin 3 FUNCTION: Structural component of the gap junctions and the hemichannels.; . . whole body;ovary;placenta;parathyroid; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.22764 0.10945 0.308721233 72.59966973 216.58313 3.18058 PAOX 0.0004355557754425 0.861038475329913 0.138525968894645 polyamine oxidase (exo-N4-amino) FUNCTION: Flavoenzyme which catalyzes the oxidation of N(1)- acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity: N(1)-acetylspermine = N(1)- acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not oxidize spermidine. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs.; . TISSUE SPECIFICITY: Widely expressed. Not detected in spleen. Expressed at lower level in neoplastic tissues. {ECO:0000269|PubMed:12477380}.; unclassifiable (Anatomical System);heart;urinary;colon;skin;uterus;pancreas;prostate;optic nerve;placenta;testis;spleen;germinal center;kidney;brain;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;liver;testis;trigeminal ganglion; 0.14887 0.18516 0.53464283 81.00967209 242.81953 3.36455 PAPD4 0.000956870232763351 0.998511360188335 0.000531769578901851 PAP associated domain containing 4 FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs. Does not play a role in replication-dependent histone mRNA degradation.; . TISSUE SPECIFICITY: Expressed in brain. Within brain, it is expressed in cerebellum, hippocampus and medulla. {ECO:0000269|PubMed:15987818}.; ovary;colon;parathyroid;bone marrow;uterus;prostate;whole body;cochlea;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;bile duct;lung;adrenal gland;nasopharynx;placenta;liver;spleen;kidney;mammary gland;aorta;stomach; superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19948 . -0.22584292 37.32012267 75.54621 1.81881 PAPD5 0.99850644091945 0.00149353094798133 2.8132568905338e-08 PAP associated domain containing 5 FUNCTION: Catalytic subunit of a TRAMP-like complex which has a poly(A) RNA polymerase activity and is involved in a post- transcriptional quality control mechanism. Polyadenylation with short oligo(A) tails is required for the degradative activity of the exosome on several of its nuclear RNA substrates. Doesn't need a cofactor for polyadenylation activity (in vitro). Plays a role in replication-dependent histone mRNA degradation, probably through terminal uridylation of mature histone mRNAs. May play a role in sister chromatid cohesion. {ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:21788334}.; . . unclassifiable (Anatomical System);cartilage;heart;colon;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;pancreas;optic nerve;lung;placenta;bone;macula lutea;liver;testis;spleen;germinal center;brain;stomach; testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.14950 0.10484 -0.183570861 39.95046001 164.93167 2.80770 PAPD7 0.998369133901838 0.00163083123786077 3.48603009169274e-08 PAP associated domain containing 7 FUNCTION: Catalytic subunit of a TRAMP-like complex which has a poly(A) RNA polymerase activity and is involved in a post- transcriptional quality control mechanism. Polyadenylation with short oligo(A) tails is required for the degradative activity of the exosome on several of its nuclear RNA substrates. Has no terminal uridylyltransferase activity, and does not play a role in replication-dependent histone mRNA degradation via uridylation. {ECO:0000269|PubMed:23376078}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;cerebellum; 0.58738 0.16698 -0.999300439 8.368719038 36.51276 1.09424 PAPLN 5.13478634877696e-22 0.0182917161835849 0.981708283816415 papilin, proteoglycan-like sulfated glycoprotein . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;larynx;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;blood;lens;skeletal muscle;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.46142 0.11057 1.269469192 93.60698278 5174.824 14.79749 PAPOLA 0.999971689697056 2.83103025815281e-05 3.62436570764317e-13 poly(A) polymerase alpha FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus. {ECO:0000269|PubMed:19224921}.; . . lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;lung;cornea;placenta;duodenum;hypopharynx;amnion;head and neck;kidney;stomach;aorta; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;thyroid;testis;white blood cells;atrioventricular node;trigeminal ganglion; 0.90955 0.10702 -0.626318434 17.03231894 20.93686 0.70876 PAPOLB 0.0371791800354128 0.92889357682969 0.033927243134897 poly(A) polymerase beta . . TISSUE SPECIFICITY: Testis specific.; . . 0.40832 . . . 3421.26119 11.22238 PAPOLG 0.989888395224926 0.0101116037558142 1.01925995191809e-09 poly(A) polymerase gamma FUNCTION: Responsible for the post-transcriptional adenylation of the 3'-terminal of mRNA precursors and several small RNAs including signal recognition particle (SRP) RNA, nuclear 7SK RNA, U2 small nuclear RNA, and ribosomal 5S RNA. {ECO:0000269|PubMed:11287430, ECO:0000269|PubMed:11463842}.; . TISSUE SPECIFICITY: Expressed predominantly in testis, and weakly in other tissues. Overexpressed in several tumors. {ECO:0000269|PubMed:11463842}.; unclassifiable (Anatomical System);lymph node;colon;fovea centralis;skin;skeletal muscle;bone marrow;breast;prostate;whole body;lung;frontal lobe;endometrium;nasopharynx;thyroid;placenta;macula lutea;testis;head and neck;germinal center;kidney;brain;stomach; superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.43167 0.10515 -0.867014353 10.72776598 33.48625 1.03325 PAPPA 0.967751416645701 0.0322485832072149 1.47084296619914e-10 pregnancy-associated plasma protein A, pappalysin 1 FUNCTION: Metalloproteinase which specifically cleaves IGFBP-4 and IGFBP-5, resulting in release of bound IGF. Cleavage of IGFBP-4 is dramatically enhanced by the presence of IGF, whereas cleavage of IGFBP-5 is slightly inhibited by the presence of IGF. {ECO:0000269|PubMed:10077652, ECO:0000269|PubMed:10913121, ECO:0000269|PubMed:11522292}.; . TISSUE SPECIFICITY: High levels in placenta and pregnancy serum. In placenta, expressed in X cells in septa and anchoring villi, and in syncytiotrophoblasts in the chorionic villi. Lower levels are found in a variety of other tissues including kidney, myometrium, endometrium, ovaries, breast, prostate, bone marrow, colon, fibroblasts and osteoblasts. {ECO:0000269|PubMed:10077652, ECO:0000269|PubMed:10491647, ECO:0000269|PubMed:7508748, ECO:0000269|PubMed:7526035}.; unclassifiable (Anatomical System);breast;uterus;frontal lobe;ovary;placenta;muscle;liver;colon;parathyroid;stomach; superior cervical ganglion;smooth muscle;heart;placenta;trigeminal ganglion;cingulate cortex; 0.63154 0.23252 -1.40197889 4.157820241 415.66933 4.26873 PAPPA-AS1 . . . PAPPA antisense RNA 1 . . TISSUE SPECIFICITY: Expressed in placenta with lower expression in brain, kidney and testis. {ECO:0000269|PubMed:15656990}.; . . 0.75587 0.10909 0.580556395 82.31304553 3435.95715 11.25487 PAPPA-AS2 . . . PAPPA antisense RNA 2 . . . . . . . . . . . PAPPA2 0.00125005429153315 0.998749822747399 1.22961068148874e-07 pappalysin 2 FUNCTION: Metalloproteinase which specifically cleaves IGFBP-5. Shows limited proteolysis toward IGFBP-3. {ECO:0000269|PubMed:11264294}.; . TISSUE SPECIFICITY: Expressed abundantly in placenta, and non- pregnant mammary gland with low expression in the kidney, fetal brain and pancreas. {ECO:0000269|PubMed:11264294, ECO:0000269|PubMed:11597188}.; . . 0.37518 0.11692 -1.49019634 3.615239443 422.84473 4.29432 PAPSS1 2.62383558845094e-06 0.979925200787317 0.020072175377095 3'-phosphoadenosine 5'-phosphosulfate synthase 1 FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate- activation pathway. Also involved in the biosynthesis of sulfated L-selectin ligands in endothelial cells.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;alveolus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; amygdala;occipital lobe;medulla oblongata;spinal cord;prefrontal cortex;globus pallidus;pons; 0.36930 0.16756 -0.799052816 12.45576787 122.72357 2.41293 PAPSS2 2.50259228647192e-07 0.902865249859049 0.0971344998817226 3'-phosphoadenosine 5'-phosphosulfate synthase 2 FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate- activation pathway. May have a important role in skeletogenesis during postnatal growth (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in cartilage and adrenal gland. {ECO:0000269|PubMed:19474428}.; ovary;colon;parathyroid;choroid;skin;retina;uterus;whole body;oesophagus;endometrium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;mesenchyma;nasopharynx;placenta;visual apparatus;liver;alveolus;spleen;kidney;mammary gland;aorta; dorsal root ganglion;superior cervical ganglion;smooth muscle;adrenal gland;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.21677 0.16810 -0.332434268 30.74427931 673.25486 5.18197 PAQR3 0.0203917043787596 0.961902709448688 0.0177055861725529 progestin and adipoQ receptor family member III FUNCTION: Functions as a spatial regulator of RAF1 kinase by sequestrating it to the Golgi. {ECO:0000269|PubMed:18547165}.; . TISSUE SPECIFICITY: Widely expressed in a range of tissues. {ECO:0000269|PubMed:16044242}.; ovary;colon;parathyroid;vein;uterus;prostate;larynx;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);hypothalamus;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;prefrontal cortex;testis; 0.48094 0.10471 -0.337894035 30.37272942 25.76026 0.83906 PAQR4 6.76132750226625e-05 0.29127163179264 0.708660754932338 progestin and adipoQ receptor family member IV . . TISSUE SPECIFICITY: Relatively widely expressed in a range of tissues. {ECO:0000269|PubMed:16044242}.; lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;ganglion;frontal lobe;oesophagus;endometrium;synovium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; amygdala;whole brain;occipital lobe;thalamus;hypothalamus;spinal cord;prefrontal cortex;caudate nucleus;parietal lobe; 0.17846 . -0.47017169 23.25430526 109.1139 2.26717 PAQR5 0.153782976698066 0.829637631318501 0.0165793919834328 progestin and adipoQ receptor family member V FUNCTION: Steroid membrane receptor. Binds progesterone. May be involved in oocyte maturation. {ECO:0000269|PubMed:12601167}.; . TISSUE SPECIFICITY: Expressed in the brain, lung, kidney, colon, adrenal and lung. {ECO:0000269|PubMed:12601167, ECO:0000269|PubMed:16044242}.; unclassifiable (Anatomical System);lung;cartilage;pituitary gland;liver;testis;colon;parathyroid;cervix;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;kidney;trigeminal ganglion;skeletal muscle; 0.14514 0.14477 -0.025608647 51.91672564 348.67946 3.95791 PAQR6 0.000721604365184446 0.75697361141466 0.242304784220155 progestin and adipoQ receptor family member VI . . TISSUE SPECIFICITY: Expressed at a low level in brain. {ECO:0000269|PubMed:16044242}.; unclassifiable (Anatomical System);hypothalamus;spinal cord;blood;prostate;lung;frontal lobe;cerebral cortex;hippocampus;testis;germinal center;kidney;brain;stomach;cerebellum; amygdala;dorsal root ganglion;whole brain;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.06273 0.07312 -0.26993514 34.59542345 88.63888 2.01985 PAQR7 0.0093107679780527 0.812118364295537 0.17857086772641 progestin and adipoQ receptor family member VII FUNCTION: Steroid membrane receptor. Binds progesterone in vitro. May be involved in oocyte maturation. {ECO:0000269|PubMed:12601167}.; . TISSUE SPECIFICITY: Expressed in a wide range of tissues including ovary, testis, placenta, uterus and bladder. {ECO:0000269|PubMed:12601167, ECO:0000269|PubMed:16044242}.; . . 0.15560 0.11007 -0.157884861 42.05590941 501.62525 4.59455 PAQR8 0.17786881683175 0.76718309095928 0.0549480922089703 progestin and adipoQ receptor family member VIII FUNCTION: Steroid membrane receptor. Binds progesterone. May be involved in oocyte maturation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain and spinal cord. Also expressed in kidney and testis. {ECO:0000269|PubMed:11676489, ECO:0000269|PubMed:12601167, ECO:0000269|PubMed:16044242}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;bone marrow;prostate;whole body;frontal lobe;cochlea;endometrium;iris;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;blood;lens;skeletal muscle;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach; . 0.27883 0.14100 -0.60427181 17.74593064 18.17095 0.63284 PAQR9 0.80079430697556 0.193786000730388 0.00541969229405191 progestin and adipoQ receptor family member IX . . TISSUE SPECIFICITY: Expression levels vary widely in a range of tissues. {ECO:0000269|PubMed:16044242}.; testis; . 0.53274 0.10894 -0.426079032 25.36565228 136.3731 2.53898 PAQR9-AS1 . . . PAQR9 antisense RNA 1 . . . . . . . . . . . PARD3 0.938527049620697 0.0614729503731739 6.12936820415353e-12 par-3 family cell polarity regulator FUNCTION: Adapter protein involved in asymmetrical cell division and cell polarization processes. Seems to play a central role in the formation of epithelial tight junctions. Targets the phosphatase PTEN to cell junctions. Involved in Schwann cell peripheral myelination (By similarity). Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons. {ECO:0000250, ECO:0000269|PubMed:19812038}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12234671}.; smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;thyroid;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;tongue;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.51139 0.29803 -0.918644703 9.807737674 320.74398 3.80380 PARD3-AS1 . . . PARD3 antisense RNA 1 . . . . . . . . . . . PARD3B 8.64518813873327e-08 0.999805592248964 0.000194321299154202 par-3 family cell polarity regulator beta FUNCTION: Putative adapter protein involved in asymmetrical cell division and cell polarization processes. May play a role in the formation of epithelial tight junctions.; . TISSUE SPECIFICITY: Highly expressed in kidney, lung and skeletal muscle. Expressed at intermediate levels in brain, heart, placenta, liver and pancreas. Isoform 1 is predominant, while isoform 2 and isoform 3 are expressed at lower levels.; unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;breast;optic nerve;lung;macula lutea;amnion;testis;kidney; superior cervical ganglion;subthalamic nucleus;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.48627 0.09509 0.126687467 62.75064874 840.37721 5.67705 PARD6A 0.854734700838115 0.144774428828502 0.000490870333383182 par-6 family cell polarity regulator alpha FUNCTION: Adapter protein involved in asymmetrical cell division and cell polarization processes. Probably involved in the formation of epithelial tight junctions. Association with PARD3 may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. {ECO:0000269|PubMed:10873802}.; . TISSUE SPECIFICITY: Expressed in pancreas, skeletal muscle, brain and heart. Weakly expressed in kidney and placenta.; unclassifiable (Anatomical System);medulla oblongata;lymph node;ovary;islets of Langerhans;hypothalamus;colon;parathyroid;retina;prostate;lung;placenta;visual apparatus;testis;kidney;brain;stomach;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;globus pallidus;testis;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.38490 0.25905 0.038710339 56.92380278 134.39747 2.52069 PARD6B 0.807577374871722 0.187482559378755 0.00494006574952279 par-6 family cell polarity regulator beta FUNCTION: Adapter protein involved in asymmetrical cell division and cell polarization processes. Probably involved in formation of epithelial tight junctions. Association with PARD3 may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins.; . TISSUE SPECIFICITY: Expressed in pancreas and in both adult and fetal kidney. Weakly expressed in placenta and lung. Not expressed in other tissues.; . . 0.13789 0.08773 0.21689899 68.12927577 212.81026 3.14883 PARD6G 0.111935410098095 0.85954815092149 0.0285164389804156 par-6 family cell polarity regulator gamma FUNCTION: Adapter protein involved in asymmetrical cell division and cell polarization processes. May play a role in the formation of epithelial tight junctions. The PARD6-PARD3 complex links GTP- bound Rho small GTPases to atypical protein kinase C proteins (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed, with a higher expression in fetal and adult kidney.; unclassifiable (Anatomical System);cartilage;heart;ovary;tongue;islets of Langerhans;parathyroid;blood;lens;skin;bone marrow;uterus;prostate;lung;bone;placenta;liver;head and neck;kidney;brain;mammary gland;stomach; atrioventricular node; 0.32605 0.11121 -0.516085732 21.20193442 21.10113 0.71400 PARD6G-AS1 . . . PARD6G antisense RNA 1 . . . . . . . . . . . PARG . . . poly(ADP-ribose) glycohydrolase FUNCTION: Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. PARG acts both as an endo- and exoglycosidase, releasing PAR of different length as well as ADP-ribose monomers. Required for retinoid acid-dependent gene transactivation, probably by dePARsylating histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters. {ECO:0000269|PubMed:23102699}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:14527731}.; . . 0.16017 0.13522 . . 87.98386 2.00608 PARGP1 . . . poly(ADP-ribose) glycohydrolase pseudogene 1 . . . . . . . . . . . PARK2 0.0218088318211922 0.974830477334406 0.00336069084440179 parkin RBR E3 ubiquitin protein ligase FUNCTION: Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPT5, TOMM20, USP30, ZNF746 and AIMP2 (PubMed:10973942, PubMed:10888878, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:16135753, PubMed:21376232, PubMed:23754282, PubMed:23620051, PubMed:24660806, PubMed:24751536). Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context (PubMed:19229105, PubMed:20889974, PubMed:25621951). Participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such as PARK7: 'Lys-63'- linked polyubiquitinated misfolded proteins are then recognized by HDAC6, leading to their recruitment to aggresomes, followed by degradation (PubMed:17846173, PubMed:19229105). Mediates 'Lys-63'- linked polyubiquitination of a 22 kDa O-linked glycosylated isoform of SNCAIP, possibly playing a role in Lewy-body formation (PubMed:11590439, PubMed:11431533, PubMed:19229105, PubMed:11590439, PubMed:15728840). Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy (PubMed:20889974). Promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins such as TOMM20, RHOT1/MIRO1 and USP30 (PubMed:19029340, PubMed:19966284, PubMed:23620051, PubMed:24896179, PubMed:25527291). Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains following mitochondrial damage, leading to mitophagy (PubMed:25621951). Mediates 'Lys-48'-linked polyubiquitination of ZNF746, followed by degradation of ZNF746 by the proteasome; possibly playing a role in the regulation of neuron death (PubMed:21376232). Limits the production of reactive oxygen species (ROS). Regulates cyclin-E during neuronal apoptosis. In collaboration with CHPF isoform 2, may enhance cell viability and protect cells from oxidative stress (PubMed:22082830). Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53 (PubMed:19801972). May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity (PubMed:11439185). May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene. {ECO:0000269|PubMed:10888878, ECO:0000269|PubMed:10973942, ECO:0000269|PubMed:11431533, ECO:0000269|PubMed:11590439, ECO:0000269|PubMed:12628165, ECO:0000269|PubMed:12719539, ECO:0000269|PubMed:15105460, ECO:0000269|PubMed:15728840, ECO:0000269|PubMed:16135753, ECO:0000269|PubMed:17846173, ECO:0000269|PubMed:18541373, ECO:0000269|PubMed:19029340, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:19801972, ECO:0000269|PubMed:19966284, ECO:0000269|PubMed:20889974, ECO:0000269|PubMed:21376232, ECO:0000269|PubMed:21532592, ECO:0000269|PubMed:22082830, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23754282, ECO:0000269|PubMed:23933751, ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:24896179, ECO:0000269|PubMed:25527291, ECO:0000269|PubMed:25621951}.; DISEASE: Parkinson disease (PARK) [MIM:168600]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features. {ECO:0000269|PubMed:12629236, ECO:0000269|PubMed:12730996}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry. Heterozygous mutations act as susceptibility alleles for late-onset Parkinson disease (PubMed:12730996 and PubMed:12629236).; DISEASE: Parkinson disease 2 (PARK2) [MIM:600116]: A neurodegenerative disorder characterized by bradykinesia, rigidity, postural instability, tremor, and onset usually before 40. It differs from classic Parkinson disease by early DOPA- induced dyskinesia, diurnal fluctuation of the symptoms, sleep benefit, dystonia and hyper-reflexia. Dementia is absent. Pathologically, patients show loss of dopaminergic neurons in the substantia nigra, similar to that seen in Parkinson disease; however, Lewy bodies (intraneuronal accumulations of aggregated proteins) are absent. {ECO:0000269|PubMed:10072423, ECO:0000269|PubMed:10824074, ECO:0000269|PubMed:10939576, ECO:0000269|PubMed:11163284, ECO:0000269|PubMed:11179010, ECO:0000269|PubMed:11487568, ECO:0000269|PubMed:11971093, ECO:0000269|PubMed:12056932, ECO:0000269|PubMed:12112109, ECO:0000269|PubMed:12114481, ECO:0000269|PubMed:12116199, ECO:0000269|PubMed:12362318, ECO:0000269|PubMed:12397156, ECO:0000269|PubMed:12629236, ECO:0000269|PubMed:12730996, ECO:0000269|PubMed:15584030, ECO:0000269|PubMed:22956510, ECO:0000269|PubMed:9560156, ECO:0000269|PubMed:9731209}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in PARK2 may be involved in the development and/or progression of ovarian cancer.; TISSUE SPECIFICITY: Highly expressed in the brain including the substantia nigra. Expressed in heart, testis and skeletal muscle. Expression is down-regulated or absent in tumor biopsies, and absent in the brain of PARK2 patients. Overexpression protects dopamine neurons from kainate-mediated apoptosis. Found in serum (at protein level). {ECO:0000269|PubMed:19501131}.; unclassifiable (Anatomical System);placenta; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.18426 0.47840 1.311772884 94.03750885 1930.72965 8.08308 PARK3 . . . Parkinson disease 3 (autosomal dominant, Lewy body) . . . . . . . . . . . PARK7 0.903949397411231 0.0952433791083466 0.000807223480422047 Parkinsonism associated deglycase FUNCTION: Protein deglycase that repairs methylglyoxal- and glyoxal-glycated amino acids and proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteines, arginines and lysines residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) (PubMed:25416785). Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease; functions probably related to its primary function (PubMed:17015834, PubMed:20304780, PubMed:18711745, PubMed:12796482, PubMed:19229105, PubMed:25416785). It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway (PubMed:12612053, PubMed:15502874, PubMed:14749723, PubMed:17015834, PubMed:21097510, PubMed:18711745). Its involvement in protein repair could also explain other unrelated functions. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death (PubMed:16390825). Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria (PubMed:19229105, PubMed:16632486). Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking (PubMed:18711745). Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (PubMed:23847046). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress (PubMed:18626009). Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity (PubMed:23792957). {ECO:0000250|UniProtKB:Q99LX0, ECO:0000269|PubMed:11477070, ECO:0000269|PubMed:12612053, ECO:0000269|PubMed:12855764, ECO:0000269|PubMed:12939276, ECO:0000269|PubMed:14749723, ECO:0000269|PubMed:15181200, ECO:0000269|PubMed:15502874, ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:16390825, ECO:0000269|PubMed:17015834, ECO:0000269|PubMed:18626009, ECO:0000269|PubMed:18711745, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:20186336, ECO:0000269|PubMed:20304780, ECO:0000269|PubMed:21097510, ECO:0000269|PubMed:22523093, ECO:0000269|PubMed:23792957, ECO:0000269|PubMed:23847046, ECO:0000269|PubMed:25416785, ECO:0000269|PubMed:9070310}.; DISEASE: Parkinson disease 7 (PARK7) [MIM:606324]: A neurodegenerative disorder characterized by resting tremor, postural tremor, bradykinesia, muscular rigidity, anxiety and psychotic episodes. PARK7 has onset before 40 years, slow progression and initial good response to levodopa. Some patients may show traits reminiscent of amyotrophic lateral sclerosis- parkinsonism/dementia complex (Guam disease). {ECO:0000269|PubMed:12446870, ECO:0000269|PubMed:12953260, ECO:0000269|PubMed:15254937, ECO:0000269|PubMed:15365989}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in pancreas, kidney, skeletal muscle, liver, testis and heart. Detected at slightly lower levels in placenta and brain (at protein level). Detected in astrocytes, Sertoli cells, spermatogonia, spermatids and spermatozoa. {ECO:0000269|PubMed:14579415, ECO:0000269|PubMed:14662519, ECO:0000269|PubMed:14705119, ECO:0000269|PubMed:9070310}.; lymphoreticular;medulla oblongata;ovary;umbilical cord;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;tongue;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; medulla oblongata;thalamus;olfactory bulb;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;adrenal gland;prefrontal cortex;kidney;parietal lobe;cingulate cortex; 0.19540 0.54065 0.082802743 60.09082331 67.74927 1.70290 PARK10 . . . Parkinson disease 10 (susceptibility) . . . . . . . . . . . PARK11 . . . Parkinson disease 11 (autosomal recessive, early onset) . . . . . . . . . . . PARK12 . . . Parkinson disease 12 (susceptibility) . . . . . . . . . . . PARK16 . . . Parkinson disease 16 (susceptibility) . . . . . . . . . . . PARL 1.07316888361272e-05 0.802746608935264 0.1972426593759 presenilin associated, rhomboid-like FUNCTION: Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptoptic signals (By similarity). Promotes changes in mitochondria morphology regulated by phosphorylation of P-beta domain. {ECO:0000250, ECO:0000269|PubMed:14732705, ECO:0000269|PubMed:17116872}.; . . umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;atrium;whole body;endometrium;bone;thyroid;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; . 0.14411 0.11702 0.17280645 65.75843359 3394.67529 11.16103 PARM1 0.00606336268651226 0.734832341779148 0.25910429553434 prostate androgen-regulated mucin-like protein 1 FUNCTION: May regulate TLP1 expression and telomerase activity, thus enabling certain prostatic cells to resist apoptosis. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in heart, kidney and placenta. {ECO:0000269|PubMed:18027867}.; . . . . 0.597144447 82.7435716 314.14041 3.76876 PARN 0.387183623172132 0.612798935499351 1.74413285165144e-05 poly(A)-specific ribonuclease FUNCTION: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization. {ECO:0000269|PubMed:10882133, ECO:0000269|PubMed:11359775, ECO:0000269|PubMed:12748283, ECO:0000269|PubMed:15175153, ECO:0000269|PubMed:9736620}.; DISEASE: Dyskeratosis congenita, autosomal recessive, 6 (DKCB6) [MIM:616353]: A form of dyskeratosis congenita, a rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy. {ECO:0000269|PubMed:25893599}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pulmonary fibrosis, and/or bone marrow failure, telomere- related, 4 (PFBMFT4) [MIM:616371]: A disease associated with shortened telomeres. Pulmonary fibrosis is the most common manifestation. Other manifestations include aplastic anemia due to bone marrow failure, hepatic fibrosis, and increased cancer risk, particularly myelodysplastic syndrome and acute myeloid leukemia. Phenotype, age at onset, and severity are determined by telomere length. {ECO:0000269|PubMed:25848748}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10640832, ECO:0000269|PubMed:9736620}.; unclassifiable (Anatomical System);heart;colon;skin;skeletal muscle;retina;breast;uterus;bile duct;prostate;whole body;lung;larynx;bone;thyroid;placenta;hypopharynx;liver;testis;head and neck;spleen;germinal center;brain;stomach; superior cervical ganglion;medulla oblongata;testis;ciliary ganglion;atrioventricular node;pons;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.15803 0.10321 -0.556537043 19.72753008 70.81127 1.75182 PARP1 0.00699693078764991 0.992996969322828 6.09988952242332e-06 poly(ADP-ribose) polymerase 1 FUNCTION: Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP- ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. {ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:19344625, ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:23230272}.; . . . . 0.90777 0.66498 -0.968173992 8.982071243 3117.80668 10.61131 PARP1P1 . . . poly(ADP-ribose) polymerase 1 pseudogene 1 . . . . . . . . . . . PARP1P2 . . . poly(ADP-ribose) polymerase 1 pseudogene 2 . . . . . . . . . . . PARP2 2.09998835678433e-07 0.969897607385351 0.0301021826158137 poly(ADP-ribose) polymerase 2 FUNCTION: Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks.; . TISSUE SPECIFICITY: Widely expressed, mainly in actively dividing tissues. The highest levels are in the brain, heart, pancreas, skeletal muscle and testis; also detected in kidney, liver, lung, placenta, ovary and spleen; levels are low in leukocytes, colon, small intestine, prostate and thymus.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;thyroid;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;occipital lobe;pons;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.09059 0.12032 -0.067881249 48.69072895 419.3216 4.27883 PARP3 1.48672469453256e-08 0.36862189227515 0.631378092857603 poly(ADP-ribose) polymerase family member 3 FUNCTION: Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing. {ECO:0000269|PubMed:16924674}.; . TISSUE SPECIFICITY: Widely expressed; the highest levels are in the kidney, skeletal muscle, liver, heart and spleen; also detected in pancreas, lung, placenta, brain, leukocytes, colon, small intestine, ovary, testis, prostate and thymus.; . . 0.03236 0.08533 0.802845857 87.69167256 495.98891 4.57731 PARP4 2.13341699280147e-20 0.71186119209566 0.28813880790434 poly(ADP-ribose) polymerase family member 4 . . TISSUE SPECIFICITY: Widely expressed; the highest levels are in the kidney; also detected in heart, placenta, lung, liver, skeletal muscle, spleen, leukocytes and pancreas.; . . 0.10511 . 4.627272075 99.76409531 3089.60625 10.56301 PARP4P1 . . . poly(ADP-ribose) polymerase family member 4 pseudogene 1 . . . . . . . . . . . PARP4P2 . . . poly(ADP-ribose) polymerase family member 4 pseudogene 2 . . . . . . . . . . . PARP4P3 . . . poly(ADP-ribose) polymerase family member 4 pseudogene 3 . . . . . . . . . . . PARP6 0.997418877545242 0.00258112156984246 8.84915460948825e-10 poly(ADP-ribose) polymerase family member 6 . . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;placenta;macula lutea;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;fetal brain;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.19132 0.07832 -0.514264485 21.41424864 22.30333 0.74868 PARP8 0.119242934394393 0.880756987949444 7.7656163073708e-08 poly(ADP-ribose) polymerase family member 8 . . . unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;blood;lens;skin;bone marrow;breast;uterus;prostate;pancreas;whole body;lung;frontal lobe;endometrium;larynx;thyroid;placenta;liver;testis;head and neck;spleen;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.35408 . -0.911109353 9.961075725 112.79172 2.31004 PARP9 5.1404381489417e-06 0.963727363518485 0.0362674960433658 poly(ADP-ribose) polymerase family member 9 FUNCTION: In concert with DTX3L plays a role in PARP1-dependent DNA damage repair. PARP1-dependent PARP9/BAL1-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. Involved in inducing the expression of IFN-gamma-responsive genes. {ECO:0000269|PubMed:16809771, ECO:0000269|PubMed:23230272}.; DISEASE: Note=Overexpressed at significantly higher levels in fatal high-risk diffuse large B-cell lymphomas (DLB-CL) compared to cured low-risk tumors. Overexpression in B-cell lymphoma transfectants may promote malignant B-cell migration. May therefore be involved in promoting B-cell migration and dissemination of high-risk DLB-CL tumors (PubMed:11110709). {ECO:0000269|PubMed:11110709}.; TISSUE SPECIFICITY: Expressed in lymphocyte-rich tissues, spleen, lymph nodes, peripheral blood lymphocytes and colonic mucosa. Also expressed in nonhematopoietic tissues such as heart and skeletal muscle. Isoform 2 is the predominant form. Most abundantly expressed in lymphomas with a brisk host inflammatory response. In diffuse large B-cell lymphomas tumors, expressed specifically by malignant B-cells. {ECO:0000269|PubMed:11110709, ECO:0000269|PubMed:16809771}.; ovary;salivary gland;intestine;colon;skin;retina;uterus;prostate;whole body;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; . 0.06342 0.08152 -0.394936437 27.02878037 529.88765 4.69811 PARP10 0.00291131564961967 0.996559365256894 0.000529319093486536 poly(ADP-ribose) polymerase family member 10 FUNCTION: May play a role in cell proliferation. May be required for the maintenance of cell cycle progression. {ECO:0000269|PubMed:15674325, ECO:0000269|PubMed:16455663}.; . TISSUE SPECIFICITY: Highly expressed in spleen and thymus. Intermediate levels in liver, kidney, pancreas, prostate, testis, ovary, intestine, and leukocytes. Low expression in heart, brain, placenta, lung, skeletal muscle, and colon. {ECO:0000269|PubMed:15674325}.; ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;testis;germinal center;brain;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;urinary;blood;pancreas;lung;placenta;visual apparatus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.06723 0.10296 0.433520496 77.34725171 2030.03083 8.29076 PARP11 0.00015946555998602 0.876096276653702 0.123744257786311 poly(ADP-ribose) polymerase family member 11 . . . unclassifiable (Anatomical System);uterus;lung;heart;visual apparatus;testis;colon;germinal center;skin; superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.56909 0.10884 -0.317668748 31.45789101 8.14301 0.29943 PARP12 7.92982223351822e-06 0.979732601374049 0.0202594688037176 poly(ADP-ribose) polymerase family member 12 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;blood;lens;breast;lung;placenta;macula lutea;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion; 0.14634 0.10401 -0.661316159 16.02382637 1281.17409 6.74010 PARP14 0.0129606904086898 0.987036829015945 2.48057536515332e-06 poly(ADP-ribose) polymerase family member 14 FUNCTION: Enhances STAT6-dependent transcription (By similarity). Has ADP-ribosyltransferase activity. {ECO:0000250, ECO:0000269|PubMed:16061477}.; . . unclassifiable (Anatomical System);smooth muscle;ovary;lacrimal gland;blood;skeletal muscle;uterus;breast;lung;placenta;bone;testis;germinal center;brain; ciliary ganglion;atrioventricular node; 0.10533 0.08512 -0.545632343 20.02241095 850.89316 5.69926 PARP15 2.70928333439315e-07 0.499472822062342 0.500526907009324 poly(ADP-ribose) polymerase family member 15 FUNCTION: Transcriptional repressor. Has ADP-ribosyltransferase activity. {ECO:0000269|PubMed:16061477}.; . . lung;testis;germinal center; . 0.04518 0.07911 2.622047925 98.78509082 3325.23246 11.02677 PARP16 1.92817785078927e-08 0.131875426262067 0.868124554456154 poly(ADP-ribose) polymerase family member 16 FUNCTION: Intracellular mono-ADP-ribosyltransferase that may play a role in different processes through the mono-ADP-ribosylation of proteins involved in those processes (PubMed:23103912, PubMed:22701565). May play a role in the unfolded protein response (UPR), by ADP-ribosylating and activating EIF2AK3 and ERN1, two important UPR effectors (PubMed:23103912). May also mediate mono- ADP-ribosylation of karyopherin KPNB1 a nuclear import factor (PubMed:22701565). May not modify proteins on arginine, cysteine or glutamate residues compared to other mono-ADP- ribosyltransferases (PubMed:22701565). {ECO:0000269|PubMed:22701565, ECO:0000269|PubMed:23103912}.; . . ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;synovium;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;blood;lens;breast;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.23398 0.10664 -0.159704656 41.90846898 53.79102 1.46128 PARPBP 9.66662310636925e-13 0.0107946923485658 0.989205307650467 PARP1 binding protein FUNCTION: Required to suppress inappropriate homologous recombination, thereby playing a central role DNA repair and in the maintenance of genomic stability. Antagonizes homologous recombination by interfering with the formation of the RAD51-DNA homologous recombination structure. Binds single-strand DNA and poly(A) homopolymers. Positively regulate the poly(ADP- ribosyl)ation activity of PARP1; however such function may be indirect. {ECO:0000269|PubMed:20931645, ECO:0000269|PubMed:22153967}.; . TISSUE SPECIFICITY: Restricted to testis. Overexpressed in multiple cancer cells. {ECO:0000269|PubMed:20931645}.; . . 0.32602 0.08484 0.064394823 58.84642604 611.04628 4.99564 PARS2 0.701898000015829 0.294431214511099 0.00367078547307177 prolyl-tRNA synthetase 2, mitochondrial (putative) . . . . . 0.14829 0.14856 -0.268115223 34.70747818 1072.64738 6.28001 PART1 . . . prostate androgen-regulated transcript 1 (non-protein coding) . . . . . . . . . . . PARTICL . . . promoter of MAT2A antisense radiation-induced circulating long non-coding RNA . . . . . . . . . . . PARVA 0.343764020273313 0.655640245359789 0.000595734366898581 parvin alpha FUNCTION: Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development (By similarity). Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. {ECO:0000250, ECO:0000269|PubMed:11134073, ECO:0000269|PubMed:11331308, ECO:0000269|PubMed:15284246, ECO:0000269|PubMed:20393563}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in heart, skeletal muscle, kidney and liver. {ECO:0000269|PubMed:11134073, ECO:0000269|PubMed:11331308, ECO:0000269|PubMed:11722847}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;urinary;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;mesenchyma;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; uterus;superior cervical ganglion;subthalamic nucleus;prostate;smooth muscle;adipose tissue;trachea;placenta;globus pallidus; 0.24069 0.17061 -0.405853867 26.23260203 31.71128 0.99845 PARVB 1.17140003331479e-12 0.0231749948413737 0.976825005157455 parvin beta FUNCTION: Adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange factors, such as ARHGEF6. Is involved in the reorganization of the actin cytoskeleton and formation of lamellipodia. Plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. {ECO:0000269|PubMed:11402068, ECO:0000269|PubMed:15005707, ECO:0000269|PubMed:15159419, ECO:0000269|PubMed:15284246, ECO:0000269|PubMed:18325335}.; . TISSUE SPECIFICITY: Expressed predominantly in heart and skeletal muscle. {ECO:0000269|PubMed:11402068, ECO:0000269|PubMed:11722847}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;gum;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;heart;trigeminal ganglion;skeletal muscle; 0.09248 0.20562 0.400544645 76.40953055 224.97702 3.24292 PARVG 0.012022450286735 0.979972647728749 0.00800490198451565 parvin gamma FUNCTION: Probably plays a role in the regulation of cell adhesion and cytoskeleton organization. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed predominantly in lymphoid organs, including spleen, thymus, lymph node, bone marrow and peripheral blood leukocytes and moderately in the digestive tract, including stomach, duodenum, jejunum, ileum, ileocecum and appendix, as well as in lung and liver. Also expressed in tumors, but at a lower level than in the corresponding normal tissues. {ECO:0000269|PubMed:11722847}.; unclassifiable (Anatomical System);smooth muscle;lymph node;small intestine;tongue;islets of Langerhans;blood;skeletal muscle;bone marrow;uterus;lung;endometrium;larynx;placenta;liver;testis;head and neck;kidney;brain;stomach;thymus; . 0.09080 0.14556 0.330767508 73.53739089 120.62002 2.39401 PASD1 0.89707670883228 0.102915125741341 8.16542637860132e-06 PAS domain containing 1 FUNCTION: Functions as a suppressor of the biological clock that drives the daily circadian rhythms of cells throughout the body (PubMed:25936801). Acts as a nuclear repressor of the CLOCK- ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock components (PubMed:25936801). Inhibits circadian clock function in cancer cells, when overexpressed (PubMed:25936801). {ECO:0000269|PubMed:25936801}.; . TISSUE SPECIFICITY: Testis-specific (PubMed:25936801). Expressed in a broad range of cancer cells, including melanoma, lung cancer, and breast cancer (at protein level). Testis-specific (PubMed:15162151). Found in histologically normal tissues from patients with uterus, lung and small intestine cancers. Widespread expression seen in solid tumors and diffuse large B-cell lymphoma (DLBCL)-derived cell lines. Isoform 2 is expressed in all DLBCL- derived cell lines, while isoform 1 is preferentially expressed in cell lines derived from non-germinal center DLBCL (PubMed:15162151). {ECO:0000269|PubMed:15162151, ECO:0000269|PubMed:25936801}.; . . 0.05538 0.06535 0.380318343 75.63104506 296.86261 3.67666 PASK 9.06471768179714e-20 0.0278883050833469 0.972111694916653 PAS domain containing serine/threonine kinase FUNCTION: Serine/threonine-protein kinase involved in energy homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1 and RPS6. Probably plays a role under changing environmental conditions (oxygen, glucose, nutrition), rather than under standard conditions. Acts as a sensor involved in energy homeostasis: regulates glycogen synthase synthesis by mediating phosphorylation of GYS1, leading to GYS1 inactivation. May be involved in glucose-stimulated insulin production in pancreas and regulation of glucagon secretion by glucose in alpha cells; however such data require additional evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate to respiratory regulation. {ECO:0000269|PubMed:16275910, ECO:0000269|PubMed:17052199, ECO:0000269|PubMed:17595531, ECO:0000269|PubMed:20943661, ECO:0000269|PubMed:21181396, ECO:0000269|PubMed:21418524}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with slightly higher expression in brain, prostate and testis. Reduced expression was found in placenta. Present in germ cells of testis and in the midpiece of sperm tails (at protein level).; ovary;salivary gland;intestine;colon;skin;prostate;endometrium;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;tongue;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;visual apparatus;liver;kidney;mammary gland;stomach;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;pons;trigeminal ganglion; 0.49938 0.10342 0.315838028 72.76480302 3295.07987 10.95978 PATE1 7.59081522526465e-08 0.0430252181335285 0.956974705958319 prostate and testis expressed 1 . . TISSUE SPECIFICITY: Expressed specifically in prostate cancer, normal prostate, and testis. Expressed in the epithelial cells of the prostate cancer and normal prostate tissues. {ECO:0000269|PubMed:11880645}.; prostate;lung;testis; . . 0.04784 0.657836546 84.27105449 3308.53588 10.98200 PATE2 3.37327473997107e-05 0.202887588340365 0.797078678912235 prostate and testis expressed 2 . . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in prostate and testis. Isoform 2 is expressed in male and female brain at equivalent levels, in particular in cerebellum, cerebral cortex, corpus callosum, occipital, parrietal and temporal lobes, and pons, but not in amygdala, cerebral peduncle, hippocampus and thalamus. {ECO:0000269|PubMed:18387948}.; prostate;lung;testis; . 0.13593 . -0.119252484 44.53880632 5.12795 0.18995 PATE3 . . . prostate and testis expressed 3 . . TISSUE SPECIFICITY: Specifically expressed in prostate and testis. {ECO:0000269|PubMed:18387948}.; . . . . 0.3455435 73.78509082 9.69627 0.35618 PATE4 . . . prostate and testis expressed 4 FUNCTION: May modulate the function of nicotinic acetylcholine receptors. May enhance sperm motility. {ECO:0000269|PubMed:18387948}.; . TISSUE SPECIFICITY: Specifically expressed in prostate, testis and spinal cord. Present in the acrosomal region of sperm cells. Present in apical epithelial cells of prostatic duct. {ECO:0000269|PubMed:18387948}.; . . . . 0.834220813 88.15758434 4744.77058 13.92051 PATJ . . . PATJ, crumbs cell polarity complex component FUNCTION: Scaffolding protein that may bring different proteins into adjacent positions at the cell membrane. May regulate protein targeting, cell polarity and integrity of tight junctions. May regulate the surface expression and/or function of ASIC3 in sensory neurons. May recruit ARHGEF18 to apical cell-cell boundaries (PubMed:22006950). {ECO:0000269|PubMed:11927608, ECO:0000269|PubMed:22006950}.; . TISSUE SPECIFICITY: Expressed in bladder, testis, ovary, small intestine, colon, heart, skeletal muscle, pancreas and cerebellum in the brain. {ECO:0000269|PubMed:11964389, ECO:0000269|PubMed:9280290}.; . . 0.17513 . 2.269245313 98.23661241 . . PATL1 0.991973625774226 0.0080263600850029 1.41407709919239e-08 protein associated with topoisomerase II homolog 1 (yeast) FUNCTION: RNA-binding protein involved in deadenylation-dependent decapping of mRNAs, leading to the degradation of mRNAs. Acts as a scaffold protein that connects deadenylation and decapping machinery. Required for cytoplasmic mRNA processing body (P-body) assembly. In case of infection, required for translation and replication of hepatitis C virus (HCV). {ECO:0000269|PubMed:17936923, ECO:0000269|PubMed:19628699, ECO:0000269|PubMed:20543818, ECO:0000269|PubMed:20584987, ECO:0000269|PubMed:20852261}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17936923}.; lymphoreticular;myocardium;smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;small intestine;tongue;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.66597 0.09722 0.066214104 58.95848077 111.84998 2.30211 PATL2 0.0677100893702347 0.516921895382463 0.415368015247302 protein associated with topoisomerase II homolog 2 (yeast) FUNCTION: RNA-binding protein that acts as a translational repressor. {ECO:0000250}.; . . . . . . 1.412946638 94.82189196 73.14264 1.78686 PATZ1 0.992716044132751 0.00728261042898731 1.34543826209723e-06 POZ/BTB and AT hook containing zinc finger 1 FUNCTION: Transcriptional repressor. {ECO:0000269|PubMed:10713105}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;whole body;optic nerve;cochlea;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;cerebrum;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;skin; 0.69272 0.12045 -0.800872469 12.33191791 948.34369 5.96456 PAUPAR . . . PAX6 upstream antisense RNA . . . . . . . . . . . PAWR 0.442459924660124 0.550912175330629 0.00662790000924739 pro-apoptotic WT1 regulator FUNCTION: Pro-apoptopic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down- regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Seems also to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1. {ECO:0000269|PubMed:11585763}.; . TISSUE SPECIFICITY: Widely expressed. Expression is elevated in various neurodegenerative diseases such as amyotrophic lateral sclerosis, Alzheimer, Parkinson and Huntington diseases and stroke. Down-regulated in several cancers. {ECO:0000269|PubMed:8943350}.; ovary;colon;parathyroid;skin;retina;uterus;prostate;endometrium;larynx;thyroid;pituitary gland;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;spinal cord;adrenal cortex;blood;breast;lung;trabecular meshwork;placenta;visual apparatus;head and neck;cervix;kidney;aorta;thymus; testis - interstitial;superior cervical ganglion;testis;trigeminal ganglion; 0.84910 0.29055 . . 2501.12098 9.32058 PAWRP1 . . . pro-apoptotic WT1 regulator pseudogene 1 . . . . . . . . . . . PAWRP2 . . . pro-apoptotic WT1 regulator pseudogene 2 . . . . . . . . . . . PAX1 0.616084025991163 0.382224632293948 0.00169134171488848 paired box 1 FUNCTION: This protein is a transcriptional activator. It may play a role in the formation of segmented structures of the embryo. May play an important role in the normal development of the vertebral column (By similarity). {ECO:0000250}.; DISEASE: Otofaciocervical syndrome 2 (OFC2) [MIM:615560]: A disorder characterized by facial dysmorphism, cup-shaped low-set ears, preauricular fistulas, hearing loss, branchial defects, skeletal anomalies including vertebral defects, low-set clavicles, winged scapulae, sloping shoulders, and mild intellectual disability. {ECO:0000269|PubMed:23851939}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.80187 0.30248 0.350995466 74.37485256 224.51285 3.24104 PAX2 0.120234372467327 0.878654059594261 0.00111156793841259 paired box 2 FUNCTION: Transcription factor that may have a role in kidney cell differentiation (PubMed:24676634). Has a critical role in the development of the urogenital tract, the eyes, and the CNS. {ECO:0000269|PubMed:24676634}.; DISEASE: Papillorenal syndrome (PAPRS) [MIM:120330]: An autosomal dominant disorder characterized by both ocular and renal anomalies, but may also include vesicoureteral reflux, high frequency hearing loss, central nervous system anomalies, and/or genital anomalies. Eye anomalies in this disorder consist of a wide and sometimes excavated dysplastic optic disk with the emergence of the retinal vessels from the periphery of the disk, designated optic nerve coloboma or 'morning glory' anomaly. Associated findings may include a small corneal diameter, retinal coloboma, scleral staphyloma, optic nerve cyst, microphthalmia, and pigmentary macular dysplasia. The kidneys are small and abnormally formed (renal hypodysplasia), and have fewer than the normal number of glomeruli, which are enlarged (oligomeganephronia). These ocular and renal anomalies result in decreased visual acuity and retinal detachment, as well as hypertension, proteinuria, and renal insufficiency that frequently progresses to end-stage renal disease. {ECO:0000269|PubMed:15652857, ECO:0000269|PubMed:19954729, ECO:0000269|PubMed:22213154, ECO:0000269|PubMed:9760197}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in PAX2 can be responsible for isolated renal hypodysplasia and oligomeganephronia (OMN). This is a rare congenital and usually sporadic anomaly characterized by bilateral renal hypoplasia, with a reduced number of enlarged nephrons and without urinary tract abnormalities. {ECO:0000269|PubMed:11168927}.; DISEASE: Focal segmental glomerulosclerosis 7 (FSGS7) [MIM:616002]: A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation. {ECO:0000269|PubMed:24676634}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in primitive cells of the kidney, ureter, eye, ear and central nervous system.; unclassifiable (Anatomical System);optic nerve;lung;ovary;placenta;macula lutea;visual apparatus;testis;parathyroid;fovea centralis;choroid;kidney;lens;retina; dorsal root ganglion;superior cervical ganglion;appendix;kidney;trigeminal ganglion; 0.83757 0.55278 -0.337894035 30.37272942 28.99207 0.92667 PAX3 0.900856133271901 0.099136457290853 7.40943724576781e-06 paired box 3 FUNCTION: Transcription factor that may regulate cell proliferation, migration and apoptosis. Involved in neural development and myogenesis. {ECO:0000269|PubMed:16951170}.; DISEASE: Waardenburg syndrome 1 (WS1) [MIM:193500]: WS1 is an autosomal dominant disorder characterized by non-progressive sensorineural deafness, pigmentary disturbances such as frontal white blaze of hair, heterochromia of irides, white eyelashes, leukoderma, and wide bridge of nose owing to lateral displacement of the inner canthus of each eye (dystopia canthorum). WS1 shows variable clinical expression and some affected individuals do not manifest hearing impairment or iris pigmentation disturbances. Dystopia canthorum is the most consistent sign and is found in 98% of the patients. {ECO:0000269|PubMed:10779847, ECO:0000269|PubMed:12949970, ECO:0000269|PubMed:1303193, ECO:0000269|PubMed:1347148, ECO:0000269|PubMed:1347149, ECO:0000269|PubMed:7825605, ECO:0000269|PubMed:7833953, ECO:0000269|PubMed:7981674, ECO:0000269|PubMed:8447316, ECO:0000269|PubMed:8490648, ECO:0000269|PubMed:8533800, ECO:0000269|PubMed:8589691, ECO:0000269|PubMed:8845842, ECO:0000269|PubMed:9067759, ECO:0000269|PubMed:9452070, ECO:0000269|PubMed:9541113, ECO:0000269|Ref.34}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Waardenburg syndrome 3 (WS3) [MIM:148820]: WS3 is an autosomal dominant disorder characterized by sensorineural deafness, pigmentary disturbances, dystopia canthorum and limb anomalies such as hypoplasia of the musculoskeletal system, flexion contractures, fusion of the carpal bones, syndactylies. {ECO:0000269|PubMed:12949970, ECO:0000269|PubMed:7726174, ECO:0000269|Ref.35}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Craniofacial-deafness-hand syndrome (CDHS) [MIM:122880]: Thought to be an autosomal dominant disease which comprises absence or hypoplasia of the nasal bones, hypoplastic maxilla, small and short nose with thin nares, limited movement of the wrist, short palpebral fissures, ulnar deviation of the fingers, hypertelorism and profound sensory-neural deafness. {ECO:0000269|PubMed:8664898}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Rhabdomyosarcoma 2 (RMS2) [MIM:268220]: A form of rhabdomyosarcoma, a highly malignant tumor of striated muscle derived from primitive mesenchymal cells and exhibiting differentiation along rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most frequently occurring soft tissue sarcomas and the most common in children. It occurs in four forms: alveolar, pleomorphic, embryonal and botryoidal rhabdomyosarcomas. {ECO:0000269|PubMed:8275086}. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving PAX3 is found in rhabdomyosarcoma. Translocation (2;13)(q35;q14) with FOXO1. The resulting protein is a transcriptional activator. {ECO:0000269|PubMed:8275086}.; DISEASE: Note=A chromosomal aberration involving PAX3 is a cause of rhabdomyosarcoma. Translocation t(2;2)(q35;p23) with NCOA1 generates the NCOA1-PAX3 oncogene consisting of the N-terminus part of PAX3 and the C-terminus part of NCOA1. The fusion protein acts as a transcriptional activator. Rhabdomyosarcoma is the most common soft tissue carcinoma in childhood, representing 5-8% of all malignancies in children. {ECO:0000269|PubMed:15313887}.; . unclassifiable (Anatomical System);uterus;heart;thyroid;testis;head and neck;brain;skin;retina; superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;skin; 0.99336 0.67982 -0.001743238 53.85114414 209.24476 3.12323 PAX4 0.00337035582414097 0.950489987720829 0.04613965645503 paired box 4 FUNCTION: Plays an important role in the differentiation and development of pancreatic islet beta cells. Transcriptional repressor that binds to a common element in the glucagon, insulin and somatostatin promoters. Competes with PAX6 for this same promoter binding site. Isoform 2 appears to be a dominant negative form antagonizing PAX4 transcriptional activity.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:11723072}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, insulin-dependent (IDDM) [MIM:222100]: A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:15834548}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, ketosis-prone (KPD) [MIM:612227]: An atypical form of diabetes mellitus characterized by an acute initial presentation with severe hyperglycemia and ketosis, as seen in classic type 1 diabetes, but after initiation of insulin therapy, prolonged remission is often possible with cessation of insulin therapy and maintenance of appropriate metabolic control. Metabolic studies show a markedly blunted insulin secretory response to glucose, partially reversible with the improvement of blood glucose control. Variable levels of insulin resistance are observed, especially in obese patients. Pancreatic beta-cell autoimmunity is a rare finding. {ECO:0000269|PubMed:15509590}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Maturity-onset diabetes of the young 9 (MODY9) [MIM:612225]: A form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease. {ECO:0000269|PubMed:17426099}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.06731 0.21490 0.486911049 79.46449634 579.48535 4.87867 PAX5 0.984243988730267 0.0157470987557515 8.91251398138048e-06 paired box 5 FUNCTION: May play an important role in B-cell differentiation as well as neural development and spermatogenesis. Involved in the regulation of the CD19 gene, a B-lymphoid-specific target gene.; DISEASE: Note=A chromosomal aberration involving PAX5 is a cause of acute lymphoblastic leukemia. Translocation t(9;18)(p13;q11.2) with ZNF521. Translocation t(9;3)(p13;p14.1) with FOXP1. Translocation t(9;12)(p13;p13) with ETV6. {ECO:0000269|PubMed:17344859}.; DISEASE: Leukemia, acute lymphoblastic, 3 (ALL3) [MIM:613065]: A subtype of acute leukemia, a cancer of the white blood cells. Acute lymphoblastic anemia is a malignant disease of bone marrow and the most common malignancy diagnosed in children. The malignant cells are lymphoid precursor cells (lymphoblasts) that are arrested in an early stage of development. The lymphoblasts replace the normal marrow elements, resulting in a marked decrease in the production of normal blood cells. Consequently, anemia, thrombocytopenia, and neutropenia occur to varying degrees. The lymphoblasts also proliferate in organs other than the marrow, particularly the liver, spleen, and lymphonodes. {ECO:0000269|PubMed:24013638}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . breast;lymphoreticular;lymph node;trabecular meshwork;testis;germinal center;tonsil; occipital lobe;tonsil;skeletal muscle; 0.43685 0.08086 -0.003562597 53.72729417 148.49912 2.65773 PAX6 0.998807897358069 0.00119209935613574 3.28579531032483e-09 paired box 6 FUNCTION: Transcription factor with important functions in the development of the eye, nose, central nervous system and pancreas. Required for the differentiation of pancreatic islet alpha cells (By similarity). Competes with PAX4 in binding to a common element in the glucagon, insulin and somatostatin promoters. Regulates specification of the ventral neuron subtypes by establishing the correct progenitor domains (By similarity). Isoform 5a appears to function as a molecular switch that specifies target genes. {ECO:0000250}.; DISEASE: Aniridia (AN) [MIM:106210]: A congenital, bilateral, panocular disorder characterized by complete absence of the iris or extreme iris hypoplasia. Aniridia is not just an isolated defect in iris development but it is associated with macular and optic nerve hypoplasia, cataract, corneal changes, nystagmus. Visual acuity is generally low but is unrelated to the degree of iris hypoplasia. Glaucoma is a secondary problem causing additional visual loss over time. {ECO:0000269|PubMed:10234503, ECO:0000269|PubMed:10737978, ECO:0000269|PubMed:11309364, ECO:0000269|PubMed:11553050, ECO:0000269|PubMed:11826019, ECO:0000269|PubMed:12552561, ECO:0000269|PubMed:12634864, ECO:0000269|PubMed:21850189, ECO:0000269|PubMed:8364574, ECO:0000269|PubMed:9147640, ECO:0000269|PubMed:9281415, ECO:0000269|PubMed:9792406, ECO:0000269|PubMed:9856761, ECO:0000269|PubMed:9931324, ECO:0000269|Ref.26, ECO:0000269|Ref.27}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peters anomaly (PETAN) [MIM:604229]: Consists of a central corneal leukoma, absence of the posterior corneal stroma and Descemet membrane, and a variable degree of iris and lenticular attachments to the central aspect of the posterior cornea. {ECO:0000269|PubMed:10441571, ECO:0000269|PubMed:12721955, ECO:0000269|PubMed:8162071}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Foveal hypoplasia 1 (FVH1) [MIM:136520]: An isolated form of foveal hypoplasia, a developmental defect of the eye defined as the lack of foveal depression with continuity of all neurosensory retinal layers in the presumed foveal area. Clinical features include absence of foveal pit on optical coherence tomography, absence of foveal hyperpigmentation, absence of foveal avascularity, absence of foveal and macular reflexes, decreased visual acuity, and nystagmus. Anterior segment anomalies and cataract are observed in some FVH1 patients. {ECO:0000269|PubMed:8640214, ECO:0000269|PubMed:9931324}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Keratitis hereditary (KERH) [MIM:148190]: An ocular disorder characterized by corneal opacification, recurrent stromal keratitis and vascularization. {ECO:0000269|PubMed:7668281}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Coloboma, ocular, autosomal dominant (COAD) [MIM:120200]: A set of malformations resulting from abnormal morphogenesis of the optic cup and stalk, and the fusion of the fetal fissure (optic fissure). The clinical presentation is variable. Some individuals may present with minimal defects in the anterior iris leaf without other ocular defects. More complex malformations create a combination of iris, uveoretinal and/or optic nerve defects without or with microphthalmia or even anophthalmia. {ECO:0000269|PubMed:12721955}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Coloboma of optic nerve (COLON) [MIM:120430]: An ocular defect that is due to malclosure of the fetal intraocular fissure affecting the optic nerve head. In some affected individuals, it appears as enlargement of the physiologic cup with severely affected eyes showing huge cavities at the site of the disk. {ECO:0000269|PubMed:12721955}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bilateral optic nerve hypoplasia (BONH) [MIM:165550]: A congenital anomaly in which the optic disk appears abnormally small. It may be an isolated finding or part of a spectrum of anatomic and functional abnormalities that includes partial or complete agenesis of the septum pellucidum, other midline brain defects, cerebral anomalies, pituitary dysfunction, and structural abnormalities of the pituitary. {ECO:0000269|PubMed:12721955}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Aniridia, cerebellar ataxia and mental deficiency (ACAMD) [MIM:206700]: A rare condition consisting of partial rudimentary iris, cerebellar impairment of the ability to perform coordinated voluntary movements, and mental retardation. {ECO:0000269|PubMed:17595013}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Fetal eye, brain, spinal cord and olfactory epithelium. Isoform 5a is less abundant than the PAX6 shorter form.; unclassifiable (Anatomical System);lung;lacrimal gland;endometrium;islets of Langerhans;visual apparatus;duodenum;lens;brain;skeletal muscle;retina; amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;beta cell islets;prefrontal cortex;globus pallidus;parietal lobe;cerebellum; 0.99522 0.82896 -0.361761279 28.6329323 4.65084 0.16659 PAX7 0.629829299867052 0.369864651997233 0.000306048135715208 paired box 7 FUNCTION: Transcription factor playing a role in myogenesis through regulation of muscle precursor cells proliferation. {ECO:0000250|UniProtKB:P47239}.; DISEASE: Rhabdomyosarcoma 2 (RMS2) [MIM:268220]: A form of rhabdomyosarcoma, a highly malignant tumor of striated muscle derived from primitive mesenchymal cells and exhibiting differentiation along rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most frequently occurring soft tissue sarcomas and the most common in children. It occurs in four forms: alveolar, pleomorphic, embryonal and botryoidal rhabdomyosarcomas. {ECO:0000269|PubMed:8187070}. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving PAX7 is found in rhabdomyosarcoma. Translocation t(1;13)(p36;q14) with FOXO1. The resulting protein is a transcriptional activator. {ECO:0000269|PubMed:8187070}.; . . . 0.89869 0.34974 -1.109541557 6.782259967 76.81981 1.83979 PAX8 0.90212384293593 0.0978407654978292 3.53915662403427e-05 paired box 8 FUNCTION: Transcription factor for the thyroid-specific expression of the genes exclusively expressed in the thyroid cell type, maintaining the functional differentiation of such cells.; DISEASE: Hypothyroidism, congenital, non-goitrous, 2 (CHNG2) [MIM:218700]: A disease characterized by thyroid dysgenesis, the most frequent cause of congenital hypothyroidism, accounting for 85% of case. The thyroid gland can be completely absent (athyreosis), ectopically located and/or severely hypoplastic. Ectopic thyroid gland is the most frequent malformation, with thyroid tissue being found most often at the base of the tongue. {ECO:0000269|PubMed:11232006, ECO:0000269|PubMed:11502839, ECO:0000269|PubMed:9590296}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the excretory system, thyroid gland and Wilms tumors.; unclassifiable (Anatomical System);lymph node;heart;ovary;colon;parathyroid;lens;skin;uterus;optic nerve;lung;endometrium;larynx;thyroid;placenta;visual apparatus;head and neck;germinal center;kidney;brain;bladder; dorsal root ganglion;superior cervical ganglion;thyroid;ciliary ganglion;kidney;atrioventricular node;fetal thyroid;trigeminal ganglion;cingulate cortex;skeletal muscle;cerebellum; 0.75501 0.56994 -0.468351206 23.42533616 56.15755 1.50565 PAX8-AS1 . . . PAX8 antisense RNA 1 . . . . . . . . . . . PAX9 0.0880945051453336 0.870432975580824 0.0414725192738426 paired box 9 FUNCTION: Transcription factor required for normal development of thymus, parathyroid glands, ultimobranchial bodies, teeth, skeletal elements of skull and larynx as well as distal limbs. {ECO:0000250, ECO:0000269|PubMed:12657635}.; DISEASE: Tooth agenesis selective 3 (STHAG3) [MIM:604625]: A form of selective tooth agenesis, a common anomaly characterized by the congenital absence of one or more teeth. Selective tooth agenesis without associated systemic disorders has sometimes been divided into 2 types: oligodontia, defined as agenesis of 6 or more permanent teeth, and hypodontia, defined as agenesis of less than 6 teeth. The number in both cases does not include absence of third molars (wisdom teeth). {ECO:0000269|PubMed:12786960}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;placenta;hypopharynx;parathyroid;head and neck;skeletal muscle;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.57606 0.24049 0.060756528 58.52795471 1992.89402 8.22534 PAXBP1 0.999970426365576 2.95736344072236e-05 1.6504379444176e-14 PAX3 and PAX7 binding protein 1 FUNCTION: Adapter protein linking the transcription factors PAX3 and PAX7 to the histone methylation machinery and involved in myogenesis. Associates with an histone methyltransferase complex that specifically mediates dimethylation and trimethylation of 'Lys-4' of histone H3. Mediates the recruitment of that complex to the transcription factors PAX3 and PAX7 on chromatin to regulate the expression of genes involved in muscle progenitor cells proliferation including ID3 and CDC20 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11707072}.; . . 0.47050 0.10286 -0.867014353 10.72776598 98.61481 2.14684 PAXBP1-AS1 . . . PAXBP1 antisense RNA 1 . . . . . . . . . . . PAXBP1P1 . . . PAX3 and PAX7 binding protein 1 pseudogene 1 . . . . . . . . . . . PAXIP1 0.999932438035634 6.75619613504703e-05 3.01584971438676e-12 PAX interacting protein 1 FUNCTION: Involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. Plays a role in early development. In DNA damage response is required for cell survival after ionizing radiation. In vitro shown to be involved in the homologous recombination mechanism for the repair of double-strand breaks (DSBs). Its localization to DNA damage foci requires RNF8 and UBE2N. Recruits TP53BP1 to DNA damage foci and, at least in particular repair processes, effective DNA damage response appears to require the association with TP53BP1 phosphorylated by ATM at 'Ser-25'. Together with TP53BP1 regulates ATM association. Recruits PAGR1 to sites of DNA damage and the PAGR1:PAXIP1 complex is required for cell survival in response to DNA damage; the function is probbaly independent of MLL-containing histone methyltransferase (HMT) complexes. Promotes ubiquitination of PCNA following UV irradiation and may regulate recruitment of polymerase eta and RAD51 to chromatin after DNA damage. Proposed to be involved in transcriptional regulation by linking MLL-containing histone methyltransferase (HMT) complexes to gene promoters by interacting with promoter-bound transcription factors such as PAX2. Associates with gene promoters that are known to be regulated by KMT2D/MLL2. During immunoglobulin class switching in activated B-cells is involved in trimethylation of histone H3 at 'Lys-4' and in transcription initiation of downstream switch regions at the immunoglobulin heavy-chain (Igh) locus; this function appears to involve the recruitment of MLL- containing HMT complexes. {ECO:0000269|PubMed:14576432, ECO:0000269|PubMed:15456759, ECO:0000269|PubMed:17690115, ECO:0000269|PubMed:17925232, ECO:0000269|PubMed:18353733, ECO:0000269|PubMed:20088963}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;bone;iris;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;testis;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.89940 0.11903 -0.486758915 22.69992923 2235.41871 8.71534 PAXIP1-AS1 . . . PAXIP1 antisense RNA 1 (head to head) . . . . . . . . . . . PAXIP1-AS2 0.0916808795062666 0.568880086184377 0.339439034309356 PAXIP1 antisense RNA 2 . . . . . . . . . 12.66462 0.46207 PBCRA1 . . . progressive bifocal chorioretinal atrophy 1 . . . . . . . . . . . PBDC1 0.84546441452731 0.151771167194111 0.00276441827857881 polysaccharide biosynthesis domain containing 1 . . . . . 0.05536 0.07658 -0.053113545 49.38664779 6.77226 0.24999 PBG1 . . . pancreatic beta cell glycoprotein 1 . . . . . . . . . . . PBK 4.09216216235921e-05 0.621688691312491 0.378270387065885 PDZ binding kinase FUNCTION: Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization and attenuation of G2/M checkpoint during doxorubicin-induced DNA damage. {ECO:0000269|PubMed:10781613, ECO:0000269|PubMed:17482142}.; . TISSUE SPECIFICITY: Expressed in the testis and placenta. In the testis, restrictedly expressed in outer cell layer of seminiferous tubules. {ECO:0000269|PubMed:10781613, ECO:0000269|PubMed:11378444}.; medulla oblongata;ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;pharynx;blood;bile duct;lung;cornea;mesenchyma;placenta;visual apparatus;liver;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;tumor;trigeminal ganglion; 0.48675 0.33362 0.305084559 72.22811984 1130.41159 6.41600 PBLD 2.81748273900393e-05 0.775703461561123 0.224268363611487 phenazine biosynthesis-like protein domain containing . . . unclassifiable (Anatomical System);cartilage;heart;small intestine;islets of Langerhans;colon;skin;skeletal muscle;uterus;lung;endometrium;larynx;nasopharynx;visual apparatus;liver;head and neck;spleen;kidney;brain;stomach; superior cervical ganglion;fetal liver;spinal cord;ciliary ganglion;pons;atrioventricular node;kidney;trigeminal ganglion; 0.13089 0.11164 0.106667882 61.73036093 328.38565 3.85205 PBOV1 0.00757239690458909 0.544339298466433 0.448088304628978 prostate and breast cancer overexpressed 1 . . TISSUE SPECIFICITY: Expressed in colon, prostate, small intestine, testis and spleen, with lower expression in thymus, ovary, and peripheral blood leukocytes. Up-regulated expression in prostate, breast, and bladder cancer, but not in lung and colon cancer. {ECO:0000269|PubMed:11156405}.; . . 0.11244 . 0.613741468 83.06794055 1247.40878 6.66939 PBRM1 0.999999987154091 1.28459092409921e-08 5.27098909489088e-22 polybromo 1 FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Acts as a negative regulator of cell proliferation. {ECO:0000269|PubMed:21248752}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12487023}.; ovary;salivary gland;intestine;colon;skin;retina;uterus;prostate;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;mesenchyma;nasopharynx;placenta;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.90442 0.24122 -2.147798897 1.480301958 257.97598 3.45511 PBX1 0.910582151189653 0.0893898255556753 2.80232546711569e-05 pre-B-cell leukemia homeobox 1 FUNCTION: Binds the sequence 5'-ATCAATCAA-3'. Acts as a transcriptional activator of PF4 in complex with MEIS1. Converted into a potent transcriptional activator by the (1;19) translocation. May have a role in steroidogenesis and, subsequently, sexual development and differentiation. Isoform PBX1b as part of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells is involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element. Probably in complex with MEIS2, is involved in transcriptional regulation by KLF4. Acts as a transcriptional activator of NKX2-5 and a transcriptional repressor of CDKN2B. Together with NKX2-5, it is required for spleen development through a mechanism that involves CDKN2B repression (By similarity). {ECO:0000250, ECO:0000269|PubMed:12609849, ECO:0000269|PubMed:21746878}.; . TISSUE SPECIFICITY: Expressed in all tissues except in cells of the B and T lineage.; unclassifiable (Anatomical System);heart;ovary;cartilage;fovea centralis;choroid;lens;skin;retina;uterus;breast;optic nerve;macula lutea;liver;spleen;kidney;brain; uterus;superior cervical ganglion;uterus corpus;fetal brain;heart;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.84048 0.09570 0.014844891 54.94810097 1981.92783 8.20620 PBX2 0.889707316038439 0.110244399504448 4.82844571124284e-05 pre-B-cell leukemia homeobox 2 FUNCTION: Transcriptional activator that binds the sequence 5'- ATCAATCAA-3'. Activates transcription of PF4 in complex with MEIS1. {ECO:0000269|PubMed:12609849}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; . . 0.49641 0.12614 -0.161524709 41.6430762 61.31213 1.59513 PBX2P1 . . . pre-B-cell leukemia homeobox 2 pseudogene 1 FUNCTION: Transcriptional activator that binds the sequence 5'- ATCAATCAA-3'. Activates transcription of PF4 in complex with MEIS1. {ECO:0000269|PubMed:12609849}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; . . 0.49641 0.12614 -0.161524709 41.6430762 . . PBX3 0.592665483652486 0.406913109794788 0.000421406552726901 pre-B-cell leukemia homeobox 3 FUNCTION: Transcriptional activator that binds the sequence 5'- ATCAATCAA-3'.; . TISSUE SPECIFICITY: Ubiquitously expressed.; unclassifiable (Anatomical System);ovary;hypothalamus;colon;blood;lens;breast;lung;larynx;visual apparatus;pituitary gland;liver;testis;head and neck;spleen;germinal center;kidney;brain;mammary gland;stomach; superior cervical ganglion;ovary;adrenal gland;adrenal cortex;trigeminal ganglion; 0.25255 0.07264 -0.161524709 41.6430762 53.96564 1.46470 PBX4 0.006772126187306 0.916590918723337 0.0766369550893573 pre-B-cell leukemia homeobox 4 . . . unclassifiable (Anatomical System);cartilage;fovea centralis;choroid;lens;skin;retina;optic nerve;whole body;lung;placenta;macula lutea;liver;testis;spleen;brain;thymus; trigeminal ganglion; 0.22535 . -0.468351206 23.42533616 60.9961 1.58873 PBXIP1 5.79843921369484e-07 0.869086852720171 0.130912567435907 pre-B-cell leukemia homeobox interacting protein 1 FUNCTION: Regulator of pre-B-cell leukemia transcription factors (BPXs) function. Inhibits the binding of PBX1-HOX complex to DNA and blocks the transcriptional activity of E2A-PBX1. Tethers estrogen receptor-alpha (ESR1) to microtubules and allows them to influence estrogen receptors-alpha signaling. {ECO:0000269|PubMed:10825160, ECO:0000269|PubMed:12360403, ECO:0000269|PubMed:17043237}.; . TISSUE SPECIFICITY: Expressed in early hematopoietic precursors. {ECO:0000269|PubMed:10825160}.; ovary;colon;retina;bone marrow;uterus;frontal lobe;larynx;synovium;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;blood;skeletal muscle;pancreas;lung;mesenchyma;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; thyroid; 0.07912 0.09055 -0.018331246 52.2764803 236.03126 3.31997 PC 0.716435670079512 0.283564106696938 2.23223549868594e-07 pyruvate carboxylase FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate.; DISEASE: Pyruvate carboxylase deficiency (PC deficiency) [MIM:266150]: Leads to lactic acidosis, mental retardation and death. It occurs in three forms: mild or type A, severe neonatal or type B, and a very mild lacticacidemia. Note=The disease is caused by mutations affecting the gene represented in this entry.; . sympathetic chain;colon;choroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;hypothalamus;lens;lung;visual apparatus;macula lutea;liver;cervix;spleen;kidney;mammary gland; whole brain;spinal cord;liver;caudate nucleus;pons;cingulate cortex; 0.19381 0.81784 -1.74358502 2.394432649 138.12153 2.55935 PCA3 . . . prostate cancer associated 3 (non-protein coding) . . . . . . . . . . . PCAP . . . predisposing for prostate cancer . . . . . . . . . . . PCAT1 . . . prostate cancer associated transcript 1 (non-protein coding) . . . . . . . . . . . PCAT2 . . . prostate cancer associated transcript 2 (non-protein coding) . . . . . . . . . . . PCAT4 . . . prostate cancer associated transcript 4 (non-protein coding) . . . . . . . . . . . PCAT5 . . . prostate cancer associated transcript 5 (non-protein coding) . . . . . . . . . . . PCAT6 . . . prostate cancer associated transcript 6 (non-protein coding) . . . . . . . . . . . PCAT7 . . . prostate cancer associated transcript 7 (non-protein coding) . . . . . . . . . . . PCAT14 . . . prostate cancer associated transcript 14 (non-protein coding) . . . . . . . . . . . PCAT18 . . . prostate cancer associated transcript 18 (non-protein coding) . . . . . . . . . . . PCAT19 . . . prostate cancer associated transcript 19 (non-protein coding) . . . . . . . . . . . PCAT29 . . . prostate cancer associated transcript 29 (non-protein coding) . . . . . . . . . . . PCBD1 0.00109441294418619 0.382356703615421 0.616548883440393 pterin-4 alpha-carbinolamine dehydratase 1 FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity.; DISEASE: Hyperphenylalaninemia, BH4-deficient, D (HPABH4D) [MIM:264070]: An autosomal recessive disease characterized by primapterinuria, a variant form of hyperphenylalaninemia defined by increased excretion of 7-substituted pterins in the urine. Patients with primapterinuria show an increased ratio of neopterin to biopterin in the urine, excretion of subnormal levels of biopterins, and normal levels of biogenic amines in cerebrospinal fluid. Neurologic signs are mild, present in the neonatal period only, and include hypotonia, delayed motor development and tremor. {ECO:0000269|PubMed:8352282, ECO:0000269|PubMed:9760199}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;myocardium;ovary;colon;parathyroid;choroid;vein;skin;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;lens;breast;pancreas;lung;placenta;visual apparatus;amnion;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; liver;kidney; 0.30026 0.23021 0.013025609 54.62962963 11.8495 0.42934 PCBD2 0.00306259643722676 0.590830337983089 0.406107065579684 pterin-4 alpha-carbinolamine dehydratase 2 FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2 (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;skin;prostate;lung;cornea;visual apparatus;hypopharynx;liver;head and neck;kidney;brain;mammary gland; globus pallidus;atrioventricular node;trigeminal ganglion; 0.13867 0.09870 0.079165051 59.43029016 5.18322 0.19297 PCBP1 0.727131612150662 0.26011695754195 0.012751430307388 poly(rC) binding protein 1 FUNCTION: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. In case of infection by poliovirus, plays a role in initiation of viral RNA replication in concert with the viral protein 3CD (PubMed:12414943). {ECO:0000269|PubMed:12414943}.; . TISSUE SPECIFICITY: Abundantly expressed in skeletal muscle, thymus and peripheral blood leukocytes while a lower expression is observed in prostate, spleen, testis, ovary, small intestine, heart, liver, adrenal and thyroid glands.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;bladder;brain;heart;cartilage;tongue;nervous;pineal body;adrenal cortex;blood;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;colon;choroid;vein;uterus;whole body;larynx;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;muscle;bile duct;pancreas;pia mater;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;thymus;cerebellum; placenta;ciliary ganglion;skeletal muscle; 0.44964 . -0.317668748 31.45789101 7.63828 0.28233 PCBP1-AS1 . . . PCBP1 antisense RNA 1 . . . . . 0.18328 . . . . . PCBP2 0.987030330209409 0.0129685504399508 1.11935063976235e-06 poly(rC) binding protein 2 FUNCTION: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. Major cellular poly(rC)-binding protein. Binds also poly(rU). Negatively regulates cellular antiviral responses mediated by MAVS signaling (PubMed:19881509). It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation (PubMed:19881509). In case of infection by poliovirus, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation (PubMed:12414943). Also plays a role in initiation of viral RNA replication in concert with the viral protein 3CD (PubMed:12414943). {ECO:0000269|PubMed:12414943, ECO:0000269|PubMed:19881509}.; . TISSUE SPECIFICITY: Detected in all tissues examined.; myocardium;lymphoreticular;smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;uterus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;bile duct;pancreas;lung;cornea;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus; fetal liver;superior cervical ganglion;adrenal gland;placenta;liver;testis;pons;kidney;trigeminal ganglion;thymus;cerebellum;bone marrow; 0.33122 . -0.185391282 39.67916962 . . PCBP2-OT1 . . . PCBP2 overlapping transcript 1 . . . . . . . . . . . PCBP2P1 . . . poly(rC) binding protein 2 pseudogene 1 . . . . . . . . . . . PCBP2P2 . . . poly(rC) binding protein 2 pseudogene 2 . . . . . . . . . . . PCBP2P3 . . . poly(rC) binding protein 2 pseudogene 3 . . . . . . . . . . . PCBP3 0.980315404815837 0.019681472610711 3.12257345180957e-06 poly(rC) binding protein 3 FUNCTION: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;colon;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;adrenal gland;bone;macula lutea;visual apparatus;testis;mammary gland;pineal gland;brain; superior cervical ganglion;trigeminal ganglion; 0.33025 0.11809 -0.670411825 15.61689078 60.98898 1.58841 PCBP3-OT1 . . . PCBP3 overlapping transcript 1 . . . . . 0.08265 . . . . . PCBP4 0.233370935826447 0.765115749984483 0.00151331418907054 poly(rC) binding protein 4 FUNCTION: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. {ECO:0000250}.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;oesophagus;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;stomach; dorsal root ganglion;occipital lobe;medulla oblongata;superior cervical ganglion;olfactory bulb;cerebellum peduncles;spinal cord;caudate nucleus;pons;atrioventricular node;skeletal muscle;prefrontal cortex;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.28196 0.10133 -0.135838822 43.77211607 331.95472 3.87367 PCCA 2.13324738593485e-10 0.852149109450278 0.147850890336397 propionyl-CoA carboxylase alpha subunit . DISEASE: Propionic acidemia type I (PA-1) [MIM:606054]: Life- threatening disease characterized by episodic vomiting, lethargy and ketosis, neutropenia, periodic thrombocytopenia, hypogammaglobulinemia, developmental retardation, and intolerance to protein. {ECO:0000269|PubMed:10101253, ECO:0000269|PubMed:10329019, ECO:0000269|PubMed:12559849, ECO:0000269|PubMed:15059621}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.67467 0.42741 0.090079492 60.64519934 317.99589 3.78624 PCCA-AS1 . . . PCCA antisense RNA 1 . . . . . . . . . . . PCCB 0.000735839433891269 0.995460688827364 0.00380347173874471 propionyl-CoA carboxylase beta subunit . DISEASE: Propionic acidemia type II (PA-2) [MIM:606054]: Life- threatening disease characterized by episodic vomiting, lethargy and ketosis, neutropenia, periodic thrombocytopenia, hypogammaglobulinemia, developmental retardation, and intolerance to protein. {ECO:0000269|PubMed:10447268, ECO:0000269|PubMed:12189489, ECO:0000269|PubMed:12559849, ECO:0000269|PubMed:15059621, ECO:0000269|PubMed:2154743, ECO:0000269|PubMed:8411997, ECO:0000269|PubMed:9683601}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;kidney; 0.16646 0.54212 0.110306132 62.00165133 142.91455 2.60563 PCDH1 0.87319543986175 0.126790450754263 1.410938398711e-05 protocadherin 1 FUNCTION: May be involved in cell-cell interaction processes and in cell adhesion.; . TISSUE SPECIFICITY: Highly expressed in the brain and neuro-glial cells.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;thyroid;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;epididymis;placenta;macula lutea;liver;amnion;spleen;cervix;stomach; dorsal root ganglion;superior cervical ganglion;placenta;globus pallidus;atrioventricular node;trigeminal ganglion; 0.86166 0.14254 -1.076610636 7.324840764 2337.77215 8.95649 PCDH7 . . . protocadherin 7 . . TISSUE SPECIFICITY: Expressed predominantly in brain and heart and at lower levels in various other tissues.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;iris;testis;bladder;brain;unclassifiable (Anatomical System);heart;tongue;pharynx;blood;lens;skeletal muscle;pancreas;lung;macula lutea;visual apparatus;liver;head and neck;kidney;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;medulla oblongata;subthalamic nucleus;prefrontal cortex;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex;parietal lobe; 0.93303 0.11453 -1.501002093 3.597546591 126.59456 2.45142 PCDH8 . . . protocadherin 8 FUNCTION: Calcium-dependent cell-adhesion protein (By similarity). May play a role in activity-induced synaptic reorganization underlying long term memory (By similarity). Could be involved in CDH2 internalization through TAOK2/p38 MAPK pathway. In hippocampal neurons, may play a role in the down-regulation of dendritic spines, maybe through its action on CDH2 endocytosis (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);whole body;hypothalamus;bone;hippocampus;brain;retina; whole brain;amygdala;occipital lobe;temporal lobe;prefrontal cortex;globus pallidus;pons;caudate nucleus;trigeminal ganglion;cingulate cortex; 0.91453 0.17256 . . 2030.33558 8.29226 PCDH8P1 . . . protocadherin 8 pseudogene 1 . . . . . . . . . . . PCDH9 0.97301427734079 0.026984345112414 1.37754679608414e-06 protocadherin 9 FUNCTION: Potential calcium-dependent cell-adhesion protein.; . . unclassifiable (Anatomical System);blood;choroid;fovea centralis;lens;skin;retina;optic nerve;whole body;frontal lobe;macula lutea;duodenum;liver;brain; whole brain;dorsal root ganglion;amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;thalamus;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;fetal brain;testis - seminiferous tubule;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.31737 0.11467 -0.126743121 44.0905874 396.92243 4.18586 PCDH9-AS1 . . . PCDH9 antisense RNA 1 . . . . . . . . . . . PCDH9-AS2 . . . PCDH9 antisense RNA 2 . . . . . . . . . . . PCDH9-AS3 . . . PCDH9 antisense RNA 3 . . . . . . . . . . . PCDH9-AS4 . . . PCDH9 antisense RNA 4 . . . . . . . . . . . PCDH10 0.894430213447045 0.105568021181273 1.76537168218335e-06 protocadherin 10 FUNCTION: Potential calcium-dependent cell-adhesion protein.; . TISSUE SPECIFICITY: Moderately expressed in all regions of the brain examined, as well as in testis and ovary, and low expression in all other tissues tested. {ECO:0000269|PubMed:11549318}.; unclassifiable (Anatomical System);smooth muscle;spinal cord;choroid;fovea centralis;lens;retina;breast;optic nerve;placenta;macula lutea;kidney;brain; amygdala;whole brain;subthalamic nucleus;occipital lobe;medulla oblongata;heart;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.58985 0.10504 -1.240018202 5.461193678 95.22371 2.10590 PCDH11X 0.925742124901504 0.0742404658858661 1.74092126300213e-05 protocadherin 11 X-linked FUNCTION: Potential calcium-dependent cell-adhesion protein.; . TISSUE SPECIFICITY: Expressed strongly in fetal brain and brain (cortex, amygdala, thalamus, substantia nigra, hippocampus, caudate nucleus and corpus callosum). Expressed at low level in testis. {ECO:0000269|PubMed:10644456, ECO:0000269|PubMed:11003707}.; unclassifiable (Anatomical System);bone;placenta;visual apparatus;brain;skeletal muscle; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.10751 0.08512 -0.220384297 37.6032083 228.18944 3.26311 PCDH11Y 0.0363686431008104 0.630636905279183 0.332994451620007 protocadherin 11 Y-linked FUNCTION: Potential calcium-dependent cell-adhesion protein.; . TISSUE SPECIFICITY: Expressed strongly in fetal brain and brain (cortex, amygdala, thalamus, substantia nigra, hippocampus, caudate nucleus and corpus callosum). Expressed at low level in testis. Expressed in apoptosis-resistant cells. {ECO:0000269|PubMed:11003707, ECO:0000269|PubMed:12420223, ECO:0000269|PubMed:14727141, ECO:0000269|PubMed:16331680}.; unclassifiable (Anatomical System);frontal lobe;bone;placenta;visual apparatus;brain;skeletal muscle; . 0.07229 0.08386 . . . . PCDH12 1.29394215809467e-10 0.319804620938402 0.680195378932204 protocadherin 12 FUNCTION: Cellular adhesion molecule that may play an important role in cell-cell interactions at interendothelial junctions. Promotes homotypic calcium-dependent aggregation and adhesion and clusters at intercellular junctions. Unable to bind to catenins, weakly associates with the cytoskeleton (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in highly vascularized tissues including the heart and placenta, but most tissues contain a low level of expression. Prominent expression in the spleen.; unclassifiable (Anatomical System);cartilage;heart;colon;vein;skin;skeletal muscle;uterus;pancreas;lung;bone;placenta;visual apparatus;testis;head and neck;spleen;kidney;brain;mammary gland;aorta; uterus corpus;superior cervical ganglion;heart;placenta;fetal lung;fetal thyroid;trigeminal ganglion;skeletal muscle; 0.60079 0.11198 0.747656234 86.41778721 545.62472 4.75149 PCDH15 7.23123612897865e-11 0.99999709993382 2.89999386729683e-06 protocadherin-related 15 FUNCTION: Calcium-dependent cell-adhesion protein. Essential for maintenance of normal retinal and cochlear function.; DISEASE: Usher syndrome 1F (USH1F) [MIM:602083]: USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa with sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). USH1 is characterized by profound congenital sensorineural deafness, absent vestibular function and prepubertal onset of progressive retinitis pigmentosa leading to blindness. {ECO:0000269|PubMed:15660226, ECO:0000269|PubMed:22815625}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Usher syndrome 1D/F (USH1DF) [MIM:601067]: USH1DF patients are heterozygous for mutations in CDH23 and PCDH15, indicating a digenic inheritance pattern. {ECO:0000269|PubMed:15537665, ECO:0000269|PubMed:18719945}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry.; DISEASE: Deafness, autosomal recessive, 23 (DFNB23) [MIM:609533]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:14570705, ECO:0000269|PubMed:18719945}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, lung, kidney, spleen and testis. Found also in the inner and outer synaptic layers, and the nerve fiber layer in adult and fetal retinas. Found in the supporting cells, outer sulcus cells and spiral ganglion of fetal cochlea. Expressed in cytotoxic tumor-derived T- and NK-cell lines as well as biopsies of nasal NK/T-cell lymphomas. Not detected in normal or in vitro activated peripheral blood cells, CD4 or CD8 lymphocytes or NK cells. Isoform 3 is expressed in brain, heart, cerebellum and kidney. CD1 isoforms, such as isoform 1, have a limited pattern of expression and is detected in testis, retina and cochlea. CD2 isoforms, such as isoforms 4 and 5, are expressed in heart, kidney, thymus, spleen, testis, retina and cochlea. CD3 isoforms, such as isoform 6, are widely expressed. {ECO:0000269|PubMed:11487575, ECO:0000269|PubMed:16369489, ECO:0000269|PubMed:18719945}.; unclassifiable (Anatomical System);placenta;brain; dorsal root ganglion;superior cervical ganglion;temporal lobe;atrioventricular node;skin; 0.25215 0.17842 0.742113909 86.35291342 10008.9347 21.80735 PCDH17 0.960498313002076 0.039498137039813 3.5499581109128e-06 protocadherin 17 FUNCTION: Potential calcium-dependent cell-adhesion protein.; . . . . 0.58994 0.11602 -1.238203625 5.490681765 82.14492 1.92300 PCDH18 0.000442524633771551 0.991735604272324 0.00782187109390451 protocadherin 18 FUNCTION: Potential calcium-dependent cell-adhesion protein.; . TISSUE SPECIFICITY: Expressed in all tissues, with highest expression in lung and ovary. {ECO:0000269|PubMed:11549318}.; unclassifiable (Anatomical System);heart;adrenal cortex;colon;skin;skeletal muscle;uterus;pancreas;prostate;whole body;lung;cochlea;endometrium;trabecular meshwork;bone;thyroid;placenta;visual apparatus;duodenum;liver;testis;spleen;kidney;brain;stomach;peripheral nerve; superior cervical ganglion;adipose tissue;atrioventricular node;trigeminal ganglion; 0.17987 0.11500 -1.258440978 5.307855626 180.60012 2.92063 PCDH19 0.977158512715513 0.0228369808559822 4.50642850530325e-06 protocadherin 19 FUNCTION: Potential calcium-dependent cell-adhesion protein.; DISEASE: Epileptic encephalopathy, early infantile, 9 (EIEE9) [MIM:300088]: A condition characterized by seizure with onset in infancy or early childhood, cognitive impairment, and delayed development of variable severity in some patients. Additional features include autistic signs and psychosis. The disorder is sex-limited, with the phenotype being restricted to females. {ECO:0000269|PubMed:18469813, ECO:0000269|PubMed:19214208, ECO:0000269|PubMed:19752159, ECO:0000269|PubMed:20713952, ECO:0000269|PubMed:20830798, ECO:0000269|PubMed:21053371, ECO:0000269|PubMed:21480887, ECO:0000269|PubMed:21519002, ECO:0000269|PubMed:22050978, ECO:0000269|PubMed:22267240}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Moderately expressed in all regions of the brain examined, with lowest levels found in the cerebellum. Moderate expression is also found in ovary, and low expression in all other tissues tested. Also detected in primary skin fibroblast. {ECO:0000269|PubMed:11549318, ECO:0000269|PubMed:18469813}.; unclassifiable (Anatomical System);uterus;optic nerve;heart;macula lutea;testis;fovea centralis;choroid;lens;brain;skin;retina; dorsal root ganglion;amygdala;superior cervical ganglion;subthalamic nucleus;fetal brain;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.38000 0.11070 -0.887242605 10.43288511 164.63901 2.80219 PCDH20 0.88114907262702 0.118792201164629 5.87262083502567e-05 protocadherin 20 FUNCTION: Potential calcium-dependent cell-adhesion protein.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;colon;skin;retina;uterus;whole body;lung;hippocampus;liver;spleen;brain;aorta; amygdala;superior cervical ganglion;globus pallidus; 0.30296 0.10451 -0.951568548 9.271054494 954.1195 5.97861 PCDHA1 0.000559474715442591 0.973083018282284 0.026357507002273 protocadherin alpha 1 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.08763 . 0.213053688 67.54541165 435.99793 4.35381 PCDHA2 1.98580542965182e-09 0.23464142234878 0.765358575665415 protocadherin alpha 2 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.12252 0.09470 0.010992521 54.17551309 187.00457 2.96875 PCDHA3 1.46196613178525e-13 0.0131516023316774 0.986848397668176 protocadherin alpha 3 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.09532 . -0.676105878 15.40457655 903.22009 5.85119 PCDHA4 2.8753730977395e-15 0.00251189083333639 0.997488109166661 protocadherin alpha 4 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;pituitary gland;testis;bladder;pineal gland;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;lens;lung;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;kidney;peripheral nerve; . 0.15891 0.20297 0.832189686 88.12809625 14979.10043 26.47872 PCDHA5 0.00353824820282254 0.986919755951384 0.00954199584579351 protocadherin alpha 5 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.09837 . 0.100999032 60.76315169 773.98299 5.50488 PCDHA6 6.16174888872113e-08 0.425463274961789 0.574536663420722 protocadherin alpha 6 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.06660 0.45200 -0.764300099 13.18117481 231.91909 3.29050 PCDHA7 0.000137151933946153 0.960924234863968 0.0389386132020857 protocadherin alpha 7 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.05263 . 0.075312176 59.17669262 540.85008 4.73693 PCDHA8 3.70119875231036e-10 0.173358702577393 0.826641297052487 protocadherin alpha 8 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.08811 . 1.879504852 97.23401746 2622.33234 9.60100 PCDHA9 7.8893945081967e-14 0.00915768373231229 0.990842316267609 protocadherin alpha 9 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.10584 . 1.502801682 95.39396084 6303.25237 16.59881 PCDHA10 4.18271816069149e-11 0.0507518069286533 0.94924819302952 protocadherin alpha 10 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;pituitary gland;testis;bladder;pineal gland;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;lens;lung;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;kidney;peripheral nerve; occipital lobe;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; . 0.10821 1.611214866 95.93064402 3823.87742 12.16143 PCDHA11 3.59325181225576e-10 0.305605932301612 0.694394067339063 protocadherin alpha 11 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.13159 . 1.078370636 91.75513093 796.12128 5.56045 PCDHA12 3.51762607400118e-10 0.090786698362961 0.909213301285276 protocadherin alpha 12 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.13030 . 1.234540528 93.27671621 295.25165 3.66735 PCDHA13 4.28546861491057e-11 0.0971847639222502 0.902815236034895 protocadherin alpha 13 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;pituitary gland;testis;bladder;pineal gland;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;lens;lung;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;kidney;peripheral nerve; . . 0.10821 -0.521770079 20.94243925 133.21741 2.50801 PCDHA14 . . . protocadherin alpha 14 pseudogene . . . . . . . . . . . PCDHA@ . . . protocadherin alpha cluster, complex locus FUNCTION: Involved in cannabinoid-induced CNS effects. Acts by inhibiting adenylate cyclase. Could be a receptor for anandamide. Inhibits L-type Ca(2+) channel current. Isoform 2 and isoform 3 have altered ligand binding. {ECO:0000269|PubMed:15620723}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15620723}.; . . 0.44350 0.20297 -0.957024976 9.088228356 . . PCDHAC1 4.57699170322582e-09 0.357296118793664 0.642703876629344 protocadherin alpha subfamily C, 1 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . medulla oblongata;ovary;sympathetic chain;adrenal medulla;colon;parathyroid;fovea centralis;choroid;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;pituitary gland;testis;bladder;pineal gland;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;lens;lung;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;kidney;peripheral nerve; occipital lobe;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; . 0.10821 1.232708491 93.27081859 382.82701 4.12573 PCDHAC2 0.916966111870881 0.083029198187929 4.68994118968274e-06 protocadherin alpha subfamily C, 2 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;pituitary gland;testis;bladder;pineal gland;brain;unclassifiable (Anatomical System);amygdala;cartilage;islets of Langerhans;lens;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;duodenum;kidney;peripheral nerve; . . 0.10821 -0.751322189 13.71196037 47.10982 1.32811 PCDHACT . . . protocadherin alpha constant . . . . . . . . . . . PCDHB1 2.81493692972867e-08 0.162419823703065 0.837580148147565 protocadherin beta 1 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . unclassifiable (Anatomical System);testis; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.21679 . 0.556689353 81.63481953 585.58728 4.90814 PCDHB2 . . . protocadherin beta 2 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . unclassifiable (Anatomical System);uterus;myocardium;cartilage;heart;endometrium;bone;thyroid;duodenum;testis;kidney;brain; . 0.14118 . 1.647992642 96.20783204 740.81523 5.40353 PCDHB3 . . . protocadherin beta 3 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . unclassifiable (Anatomical System);breast;uterus;myocardium;lung;duodenum;testis;brain;retina; . 0.12451 0.10391 0.802845857 87.69167256 1630.0502 7.46513 PCDHB4 . . . protocadherin beta 4 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . unclassifiable (Anatomical System);uterus;lung;islets of Langerhans;macula lutea;colon;fovea centralis;brain;retina; . 0.19735 . 0.804668134 87.71526303 4546.2128 13.53305 PCDHB5 9.45268553121999e-07 0.318857035757919 0.681142018973528 protocadherin beta 5 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . unclassifiable (Anatomical System);uterus;prostate;pancreas;lung;ovary;cochlea;muscle;testis;brain;pineal gland;stomach; . 0.07466 . 0.273728691 70.74781788 486.05983 4.53925 PCDHB6 0.00172664093496475 0.894344715098226 0.103928643966809 protocadherin beta 6 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . unclassifiable (Anatomical System);myocardium;cartilage;ovary;salivary gland;intestine;pharynx;colon;parathyroid;blood;uterus;prostate;lung;trabecular meshwork;placenta;visual apparatus;duodenum;liver;kidney;brain;bladder; medulla oblongata;superior cervical ganglion;uterus corpus; 0.07333 . 2.629367354 98.80278368 5415.09796 15.17538 PCDHB7 1.30423838331795e-15 0.000818545998901424 0.999181454001097 protocadherin beta 7 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . unclassifiable (Anatomical System);uterus;optic nerve;lung;cartilage;bone;duodenum;testis;colon;brain; . 0.10741 . 1.63326524 96.08398207 4489.23646 13.44872 PCDHB8 4.79968959397036e-08 0.117922549258552 0.882077402744552 protocadherin beta 8 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . unclassifiable (Anatomical System);uterus;whole body;frontal lobe;placenta;duodenum; . 0.03421 . 2.739661384 98.96201934 8920.76586 20.40904 PCDHB9 . . . protocadherin beta 9 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . . 0.10723 . . . . PCDHB10 1.17632278967153e-06 0.354752435817838 0.645246387859372 protocadherin beta 10 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . unclassifiable (Anatomical System);testis;brain;aorta;retina; . . 0.10723 2.20846126 98.13635291 1545.52179 7.28913 PCDHB11 3.09017538885927e-07 0.178174534031931 0.82182515695053 protocadherin beta 11 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . unclassifiable (Anatomical System);uterus;myocardium;frontal lobe;islets of Langerhans;internal ear;duodenum;retina; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.03029 0.14795 1.006742856 90.79971691 3913.17129 12.36711 PCDHB12 0.000155401804648917 0.669826242216561 0.33001835597879 protocadherin beta 12 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . unclassifiable (Anatomical System);uterus;bone;duodenum;testis;brain; . 0.04439 . 2.476806522 98.62585515 2834.29925 10.05542 PCDHB13 1.69139790303478e-09 0.0328413683593338 0.967158629949268 protocadherin beta 13 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . unclassifiable (Anatomical System);uterus;prostate;ovary;larynx;thyroid;placenta;duodenum;parathyroid;head and neck;brain;skin; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.02590 0.09006 0.205769367 67.49823071 1261.54022 6.69733 PCDHB14 9.0591236628607e-09 0.08628018460249 0.913719806338386 protocadherin beta 14 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . unclassifiable (Anatomical System);myocardium;cartilage;bile duct;uterus;pancreas;lung;endometrium;duodenum;liver;testis;cervix;brain;mammary gland;peripheral nerve;thymus; . 0.03309 . 1.030617021 91.10639302 666.24151 5.16589 PCDHB15 0.00680082460641515 0.975270939975868 0.0179282354177168 protocadherin beta 15 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . unclassifiable (Anatomical System);uterus;myocardium;lung;ovary;bone;sympathetic chain;duodenum;brain;stomach; . 0.19381 . 1.583668045 95.79499882 3037.87669 10.47047 PCDHB16 0.00177081504936022 0.897216857349261 0.101012327601379 protocadherin beta 16 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;hypothalamus;skin;uterus;whole body;lung;testis;mammary gland;brain;stomach; . 0.07988 0.19766 1.072886248 91.70794999 8831.34731 20.28873 PCDHB17P . . . protocadherin beta 17 pseudogene . . . . . . . . . . . PCDHB18P . . . protocadherin beta 18 pseudogene FUNCTION: Potential calcium-dependent cell-adhesion protein. {ECO:0000250}.; . . . . 0.06840 . . . . . PCDHB19P . . . protocadherin beta 19 pseudogene . . . . . . . . . . . PCDHB@ . . . protocadherin beta cluster . . . . . . . . . . . PCDHG@ . . . protocadherin gamma cluster . . . . . . . . . . . PCDHGA1 0.000268173566278005 0.931597313397073 0.068134513036649 protocadherin gamma subfamily A, 1 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.13396 . 0.117584698 62.19037509 538.94641 4.73099 PCDHGA2 8.23180823080115e-07 0.737637807157109 0.262361369662068 protocadherin gamma subfamily A, 2 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.04836 . 0.279193852 70.77730597 2085.52059 8.41538 PCDHGA3 0.000592397328401253 0.975010286999392 0.0243973156722072 protocadherin gamma subfamily A, 3 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;amygdala;heart;cartilage;tongue;pineal body;adrenal cortex;lens;skeletal muscle;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;medulla oblongata;superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.18107 . 0.473967469 78.86293937 1285.44842 6.74849 PCDHGA4 5.9646129412289e-07 0.43406798253468 0.565931421004026 protocadherin gamma subfamily A, 4 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . . . . . 1872.58361 7.96058 PCDHGA5 0.000468775328634083 0.966140624563636 0.0333906001077295 protocadherin gamma subfamily A, 5 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.21938 0.18427 -1.344833561 4.641424864 312.51879 3.76189 PCDHGA6 8.20064599747487e-07 0.736871867015814 0.263127312919587 protocadherin gamma subfamily A, 6 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.20048 . -0.079012906 47.25760793 336.38673 3.89594 PCDHGA7 5.27648432399162e-06 0.660312893485593 0.339681830030083 protocadherin gamma subfamily A, 7 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . . . 0.143271594 63.67067705 862.76559 5.72657 PCDHGA8 9.44701125840242e-09 0.295195591280539 0.70480439927245 protocadherin gamma subfamily A, 8 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.15642 . 0.677860057 84.76645435 2844.63517 10.08476 PCDHGA9 3.67577801365825e-05 0.949301404135125 0.0506618380847384 protocadherin gamma subfamily A, 9 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . . . . . 174.89737 2.87562 PCDHGA10 5.44479549104987e-06 0.871007606205674 0.128986948998835 protocadherin gamma subfamily A, 10 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . . . 0.181903047 66.2361406 245.83917 3.38242 PCDHGA11 4.54527989298976e-05 0.96143212326376 0.0385224239373097 protocadherin gamma subfamily A, 11 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.32539 . 0.051446096 57.53715499 956.94641 5.98918 PCDHGA12 0.00072767906356036 0.980847696101729 0.0184246248347109 protocadherin gamma subfamily A, 12 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;amygdala;heart;cartilage;tongue;pineal body;spinal cord;adrenal cortex;lens;skeletal muscle;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; . . 0.10087 0.229636184 68.56569946 327.25947 3.84666 PCDHGB1 0.168083945130884 0.831315655941262 0.00060039892785429 protocadherin gamma subfamily B, 1 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . . . -0.859744935 10.92238736 375.58723 4.08515 PCDHGB2 3.5428979703809e-07 0.556630464805988 0.443369180904215 protocadherin gamma subfamily B, 2 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . . . 0.672386703 84.73696627 1879.44566 7.97448 PCDHGB3 0.000624134619793241 0.976647233793812 0.0227286315863951 protocadherin gamma subfamily B, 3 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.10150 . . . 533.05301 4.70992 PCDHGB4 0.00256131629310045 0.982431468299879 0.015007215407021 protocadherin gamma subfamily B, 4 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.41102 0.09740 -0.881793075 10.53904223 377.4072 4.09655 PCDHGB5 . . . protocadherin gamma subfamily B, 5 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . . . . . . . PCDHGB6 6.46505596680808e-05 0.975849562486984 0.0240857869533475 protocadherin gamma subfamily B, 6 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . . . 0.141451114 63.65298419 543.79565 4.74619 PCDHGB7 0.0160706258502221 0.982853945742388 0.00107542840739028 protocadherin gamma subfamily B, 7 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . . . 0.10028 . -0.058785319 48.90894079 722.72522 5.33701 PCDHGB8P . . . protocadherin gamma subfamily B, 8 pseudogene . . . . . . . . . . . PCDHGB9P . . . protocadherin gamma subfamily B, 9 pseudogene . . . . . . . . . . . PCDHGC3 0.705736988755585 0.294232886815231 3.01244291843249e-05 protocadherin gamma subfamily C, 3 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;optic nerve;frontal lobe;endometrium;thyroid;iris;bladder;brain;amygdala;heart;cartilage;tongue;pineal body;adrenal cortex;lens;skeletal muscle;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle;cerebellum; . 0.10087 -1.550537744 3.249587167 65.56975 1.66755 PCDHGC4 0.93614957487166 0.0638480242569922 2.40087134820827e-06 protocadherin gamma subfamily C, 4 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;optic nerve;frontal lobe;endometrium;thyroid;iris;brain;amygdala;heart;cartilage;tongue;pineal body;adrenal cortex;lens;skeletal muscle;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; . . 0.10087 -0.530852121 20.82448691 451.81165 4.42089 PCDHGC5 2.85043689391107e-05 0.930461784942138 0.0695097106889232 protocadherin gamma subfamily C, 5 FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.; . . myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;amygdala;heart;cartilage;tongue;pineal body;adrenal cortex;lens;skeletal muscle;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;medulla oblongata;superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; . 0.10087 -1.458708104 3.821656051 1287.70265 6.75795 PCDHGCT . . . protocadherin gamma constant . . . . . . . . . . . PCED1A 0.0160267066093378 0.959127396814959 0.0248458965757033 PC-esterase domain containing 1A . . . . . 0.25747 0.10588 0.064394823 58.84642604 164.8719 2.80601 PCED1B 0.00826612737821006 0.792275925299044 0.199457947322746 PC-esterase domain containing 1B . . . . . 0.09515 0.09636 -0.53631094 20.53550366 8.44364 0.30919 PCED1B-AS1 . . . PCED1B antisense RNA 1 . . . . . . . . . . . PCED1CP . . . PC-esterase domain containing 1C, pseudogene . . . . . . . . . . . PCF11 0.999999873982097 1.26017902649751e-07 6.78161234025717e-19 PCF11 cleavage and polyadenylation factor subunit FUNCTION: Component of pre-mRNA cleavage complex II.; . . umbilical cord;ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;thyroid;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;breast;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; testis - interstitial;superior cervical ganglion;subthalamic nucleus;medulla oblongata;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle;parietal lobe; 0.61805 0.11422 -0.213110737 37.75064874 1020.60249 6.14722 PCF11-AS1 . . . PCF11 anstisense RNA 1 . . . . . . . . . . . PCGEM1 . . . PCGEM1, prostate-specific transcript (non-protein coding) . . . . . . . . . . . PCGF1 0.987060430814222 0.0129340732744579 5.49591132011558e-06 polycomb group ring finger 1 FUNCTION: Component of the Polycomb group (PcG) multiprotein BCOR complex, a complex required to maintain the transcriptionally repressive state of some genes, such as BCL6 and the cyclin- dependent kinase inhibitor, CDKN1A. Transcriptional repressor that may be targeted to the DNA by BCL6; this transcription repressor activity may be related to PKC signaling pathway. Represses CDKN1A expression by binding to its promoter, and this repression is dependent on the retinoic acid response element (RARE element). Promotes cell cycle progression and enhances cell proliferation as well. May have a positive role in tumor cell growth by down- regulating CDKN1A. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. {ECO:0000269|PubMed:15620699, ECO:0000269|PubMed:16943429, ECO:0000269|PubMed:17088287}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11287196}.; ovary;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lens;pancreas;lung;placenta;visual apparatus;macula lutea;liver;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion; 0.38807 0.10625 0.369407109 74.95281906 20.98541 0.71033 PCGF2 0.553826743472709 0.443344574103849 0.00282868242344261 polycomb group ring finger 2 FUNCTION: Transcriptional repressor. Binds specifically to the DNA sequence 5'-GACTNGACT-3'. Has tumor suppressor activity. May play a role in control of cell proliferation and/or neural cell development. Regulates proliferation of early T progenitor cells by maintaining expression of HES1. Also plays a role in antero- posterior specification of the axial skeleton and negative regulation of the self-renewal activity of hematopoietic stem cells. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Is not functionally redundant with BMI1; unlike BMI1 does not stimulate the E3 ubiquitin-protein ligase activity in a reconstituted PRC1-like complex (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in all tissues examined with high expression found in placenta lung and kidney and low expression, in liver, pancreas and skeletal muscle.; myocardium;smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;larynx;bone;thyroid;iris;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;cerebellum peduncles;ciliary ganglion;pons;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle;cerebellum; 0.28674 0.10781 -0.427900189 25.14744043 27.13463 0.87503 PCGF3 0.943399926818786 0.0563883098887852 0.000211763292428646 polycomb group ring finger 3 FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.; . . medulla oblongata;smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve;cerebellum; amygdala;dorsal root ganglion;superior cervical ganglion;fetal brain;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.19677 0.11262 -0.295622497 32.61972163 14.68699 0.52952 PCGF5 0.996021945517005 0.00397799237079229 6.21122026125939e-08 polycomb group ring finger 5 FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.; . . unclassifiable (Anatomical System);ovary;heart;colon;parathyroid;blood;skin;skeletal muscle;bone marrow;breast;uterus;pancreas;lung;frontal lobe;trabecular meshwork;bone;placenta;duodenum;liver;testis;germinal center;mammary gland;aorta;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;fetal liver;ciliary ganglion;atrioventricular node; 0.29980 0.07163 -0.163345027 41.24793583 4.94441 0.18393 PCGF6 0.000251716409020373 0.926180189607256 0.073568093983724 polycomb group ring finger 6 FUNCTION: Transcriptional repressor. May modulate the levels of histone H3K4Me3 by activating KDM5D histone demethylase. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. {ECO:0000269|PubMed:12167161, ECO:0000269|PubMed:17320162}.; . TISSUE SPECIFICITY: Ubiquitous.; unclassifiable (Anatomical System);smooth muscle;lymph node;ovary;heart;salivary gland;intestine;pharynx;colon;blood;skin;bone marrow;uterus;prostate;lung;endometrium;placenta;visual apparatus;liver;testis;kidney;brain;mammary gland;bladder;artery;aorta; . 0.54171 0.10678 -0.317668748 31.45789101 4680.61806 13.78571 PCGF7P . . . polycomb group ring finger 7 pseudogene . . . . . . . . . . . PCID2 6.36502716196613e-09 0.650895804353619 0.349104189281354 PCI domain containing 2 FUNCTION: Required for B-cell survival through the regulation of the expression of cell-cycle checkpoint MAD2L1 protein during B cell differentiation (By similarity). Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, DSS1, and either centrin CETN2 or CETN3 (PubMed:22307388). The TREX-2 complex functions in docking export- competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. Binds and stabilizes BRCA2 and is thus involved in the control of R-loop- associated DNA damage and transcription-associated genomic instability. R-loop accumulation does not increase in PCID2- depleted cells. {ECO:0000250, ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:24896180}.; . . umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;amnion;spleen;head and neck;cervix;kidney;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.51736 0.10556 -0.60427181 17.74593064 23.1122 0.77090 PCIF1 0.999961615698865 3.83842973745966e-05 3.75998132068589e-12 PDX1 C-terminal inhibiting factor 1 FUNCTION: May play a role in transcription elongation or in coupling transcription to pre-mRNA processing through its association with the phosphorylated C-terminal domain (CTD) of RNAPII largest subunit.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12565871}.; . . 0.11563 0.10007 -0.843147538 11.2762444 86.58113 1.98779 PCK1 3.93284883371259e-08 0.344653335688221 0.65534662498329 phosphoenolpyruvate carboxykinase 1 FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.; DISEASE: Cytosolic phosphoenolpyruvate carboxykinase deficiency (C-PEPCKD) [MIM:261680]: Metabolic disorder resulting from impaired gluconeogenesis. It is a rare disease with less than 10 cases reported in the literature. Clinical characteristics include hypotonia, hepatomegaly, failure to thrive, lactic acidosis and hypoglycemia. Autopsy reveals fatty infiltration of both the liver and kidneys. The disorder is transmitted as an autosomal recessive trait. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Major sites of expression are liver, kidney and adipocytes.; unclassifiable (Anatomical System);medulla oblongata;ovary;tongue;islets of Langerhans;colon;skeletal muscle;uterus;prostate;endometrium;trabecular meshwork;liver;head and neck;kidney;stomach; superior cervical ganglion;adipose tissue;liver;ciliary ganglion;fetal lung;kidney;pituitary; 0.53157 0.50154 0.277371677 70.75961312 642.29542 5.09210 PCK2 2.18697220904741e-17 0.0037598813373015 0.996240118662699 phosphoenolpyruvate carboxykinase 2, mitochondrial FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. {ECO:0000250}.; DISEASE: Mitochondrial phosphoenolpyruvate carboxykinase deficiency (M-PEPCKD) [MIM:261650]: Metabolic disorder resulting from impaired gluconeogenesis. It is a rare disease with less than 10 cases reported in the literature. Clinical characteristics include hypotonia, hepatomegaly, failure to thrive, lactic acidosis and hypoglycemia. Autopsy reveals fatty infiltration of both the liver and kidneys. The disorder is transmitted as an autosomal recessive trait. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;skeletal muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;liver;testis;kidney; 0.21081 0.81831 0.273728691 70.74781788 824.02605 5.62971 PCLO 0.999999999988929 1.10713112197768e-11 1.02791232186385e-35 piccolo presynaptic cytomatrix protein FUNCTION: May act as a scaffolding protein involved in the organization of synaptic active zones and in synaptic vesicle trafficking. {ECO:0000250|UniProtKB:Q9QYX7}.; DISEASE: Pontocerebellar hypoplasia 3 (PCH3) [MIM:608027]: A form of pontocerebellar hypoplasia, a disorder characterized by structural defects of the pons and cerebellum. Brain MRI shows an abnormally small cerebellum and brainstem, decreased cerebral white matter, and a thin corpus callosum. PCH3 features include seizures, short stature, optic atrophy, progressive microcephaly, severe developmental delay. {ECO:0000269|PubMed:25832664}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Moderately expressed in the developing cerebral cortex. {ECO:0000269|PubMed:25832664}.; breast;frontal lobe;thyroid;kidney;brain;stomach;retina; dorsal root ganglion;amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;cerebellum peduncles;temporal lobe;atrioventricular node;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.20691 0.08509 -0.175308288 40.56970984 9296.23295 20.89927 PCM1 . . . pericentriolar material 1 FUNCTION: Required for centrosome assembly and function. Essential for the correct localization of several centrosomal proteins including CEP250, CETN3, PCNT and NEK2. Required to anchor microtubules to the centrosome. Involved in the biogenesis of cilia. {ECO:0000269|PubMed:12403812, ECO:0000269|PubMed:15659651, ECO:0000269|PubMed:16943179, ECO:0000269|PubMed:20551181, ECO:0000269|PubMed:24121310}.; DISEASE: Note=A chromosomal aberration involving PCM1 is found in papillary thyroid carcinomas (PTCs). Translocation t(8;10)(p21.3;q11.2) with RET links the protein kinase domain of RET to the major portion of PCM1. {ECO:0000269|PubMed:10980597}.; DISEASE: Note=A chromosomal aberration involving PCM1 is found in a variety of hematological malignancies including atypical chronic myeloid leukemia (atypical CML) and T-cell lymphoma. Translocation t(8;9)(p22;p24) with JAK2 links the protein kinase domain of JAK2 to the major portion of PCM1.; TISSUE SPECIFICITY: Expressed in blood, bone marrow, breast, lymph node, ovary and thyroid. {ECO:0000269|PubMed:10980597, ECO:0000269|PubMed:15184884, ECO:0000269|PubMed:16270321, ECO:0000269|PubMed:16424865}.; myocardium;lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;cochlea;thyroid;amniotic fluid;germinal center;brain;amygdala;heart;cartilage;tongue;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus;cerebellum; testis - interstitial;superior cervical ganglion;occipital lobe;testis - seminiferous tubule;prefrontal cortex;testis;caudate nucleus;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.52458 0.13544 -0.323627113 30.93300307 3402.14478 11.17265 PCMT1 0.446383565895946 0.547179505232261 0.00643692887179311 protein-L-isoaspartate (D-aspartate) O-methyltransferase FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin carboxyl-terminal hydrolase isozyme L1, phosphatidylethanolamine- binding protein 1, stathmin, beta-synuclein and alpha-synuclein. {ECO:0000250|UniProtKB:P23506}.; . . . . 0.40253 0.17705 0.03689118 56.64071715 36.69422 1.10081 PCMTD1 2.55691827695449e-06 0.503470629415061 0.496526813666662 protein-L-isoaspartate (D-aspartate) O-methyltransferase domain containing 1 . . . unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;skin;skeletal muscle;breast;uterus;pancreas;whole body;lung;frontal lobe;nasopharynx;bone;placenta;liver;testis;head and neck;germinal center;kidney;brain;stomach; . . 0.10723 0.169169615 65.33380514 3481.72932 11.35685 PCMTD1P1 . . . protein-L-isoaspartate (D-aspartate) O-methyltransferase domain containing 1 pseudogene 1 . . . . . . . . . . . PCMTD1P2 . . . protein-L-isoaspartate (D-aspartate) O-methyltransferase domain containing 1 pseudogene 2 . . . . . . . . . . . PCMTD1P3 . . . protein-L-isoaspartate (D-aspartate) O-methyltransferase domain containing 1 pseudogene 3 . . . . . . . . . . . PCMTD1P4 . . . protein-L-isoaspartate (D-aspartate) O-methyltransferase domain containing 1 pseudogene 4 . . . . . . . . . . . PCMTD1P5 . . . protein-L-isoaspartate (D-aspartate) O-methyltransferase domain containing 1 pseudogene 5 . . . . . . . . . . . PCMTD1P6 . . . protein-L-isoaspartate (D-aspartate) O-methyltransferase domain containing 1 pseudogene 6 . . . . . . . . . . . PCMTD1P7 . . . protein-L-isoaspartate (D-aspartate) O-methyltransferase domain containing 1 pseudogene 7 . . . . . . . . . . . PCMTD1P8 . . . protein-L-isoaspartate (D-aspartate) O-methyltransferase domain containing 1 pseudogene 8 . . . . . . . . . . . PCMTD2 0.0123297627205191 0.952106421267062 0.0355638160124194 protein-L-isoaspartate (D-aspartate) O-methyltransferase domain containing 2 . . . ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;dura mater;brain;gall bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pia mater;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18192 . -0.249709319 35.74545883 47.62165 1.33989 PCNA 0.937503505123045 0.0622248803985591 0.000271614478396175 proliferating cell nuclear antigen FUNCTION: Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'- 5' exonuclease and 3'-phosphodiesterase, but not apurinic- apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways (PubMed:24939902). Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion. {ECO:0000269|PubMed:18719106, ECO:0000269|PubMed:19443450, ECO:0000269|PubMed:24939902}.; DISEASE: Ataxia-telangiectasia-like disorder 2 (ATLD2) [MIM:615919]: A neurodegenerative disorder due to defects in DNA excision repair. ATLD2 is characterized by developmental delay, ataxia, sensorineural hearing loss, short stature, cutaneous and ocular telangiectasia, and photosensitivity. {ECO:0000269|PubMed:24911150}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.99999 0.96597 -0.207437529 38.2814343 5.75658 0.21601 PCNA-AS1 . . . PCNA antisense RNA 1 . . . . . . . . . . . PCNAP1 . . . proliferating cell nuclear antigen pseudogene 1 . . . . . . . . . . . PCNAP2 . . . proliferating cell nuclear antigen pseudogene 2 . . . . . . . . . . . PCNAP3 . . . proliferating cell nuclear antigen pseudogene 3 . . . . . . . . . . . PCNAP4 . . . proliferating cell nuclear antigen pseudogene 4 . . . . . . . . . . . PCNP 0.872423409746757 0.125900362187447 0.00167622806579603 PEST proteolytic signal containing nuclear protein FUNCTION: May be involved in cell cycle regulation.; . . myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;substantia nigra;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;mesenchyma;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; amygdala;occipital lobe;prefrontal cortex;parietal lobe; 0.74558 0.10643 0.501689326 79.7888653 72.04666 1.76780 PCNPP1 . . . PEST containing nuclear protein pseudogene 1 . . . . . . . . . . . PCNPP2 . . . PEST containing nuclear protein pseudogene 2 . . . . . . . . . . . PCNPP3 . . . PEST containing nuclear protein pseudogene 3 . . . . . . . . . . . PCNPP4 . . . PEST containing nuclear protein pseudogene 4 . . . . . . . . . . . PCNPP5 . . . PEST containing nuclear protein pseudogene 5 . . . . . . . . . . . PCNT 4.17814442415305e-38 0.557429948071703 0.442570051928298 pericentrin FUNCTION: Integral component of the filamentous matrix of the centrosome involved in the initial establishment of organized microtubule arrays in both mitosis and meiosis. Plays a role, together with DISC1, in the microtubule network formation. Is an integral component of the pericentriolar material (PCM). May play an important role in preventing premature centrosome splitting during interphase by inhibiting NEK2 kinase activity at the centrosome. {ECO:0000269|PubMed:10823944, ECO:0000269|PubMed:11171385, ECO:0000269|PubMed:18955030, ECO:0000269|PubMed:20599736}.; DISEASE: Microcephalic osteodysplastic primordial dwarfism 2 (MOPD2) [MIM:210720]: Adults with this rare inherited condition have an average height of 100 centimeters and a brain size comparable to that of a 3-month-old baby, but are of near-normal intelligence. {ECO:0000269|PubMed:18157127, ECO:0000269|PubMed:18174396}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues tested, including placenta, liver, kidney and thymus. {ECO:0000269|PubMed:10823944}.; ovary;adrenal medulla;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; medulla oblongata;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;caudate nucleus;skeletal muscle; 0.12195 0.21397 3.571342941 99.52229299 12581.30373 24.04834 PCNX1 . . . pecanex homolog 1 (Drosophila) . . . . . 0.12609 0.10474 -1.951619288 1.869544704 . . PCNX2 . . . pecanex homolog 2 (Drosophila) FUNCTION: May play a role in tumorigenesis of colorectal carcinomas with high microsatellite instability (MSI-H). {ECO:0000269|PubMed:12140758, ECO:0000269|PubMed:14507650}.; . . . . 0.09947 . 0.389303812 75.70181647 . . PCNX3 . . . pecanex homolog 3 (Drosophila) . . . . . 0.64163 0.10751 -1.41686601 4.116536919 . . PCNX4 . . . pecanex homolog 4 (Drosophila) . . . . . 0.06273 0.08601 . . . . PCOLCE 0.500664877958131 0.498454986953343 0.000880135088525612 procollagen C-endopeptidase enhancer FUNCTION: Binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity.; . . medulla oblongata;smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;oesophagus;endometrium;synovium;bone;thyroid;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;spinal cord;adrenal cortex;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach; uterus;adipose tissue;smooth muscle;olfactory bulb;liver;fetal lung;trigeminal ganglion; 0.75819 0.14881 -0.134019284 43.90776126 423.68346 4.29790 PCOLCE-AS1 . . . PCOLCE antisense RNA 1 . . . . . . . . . . . PCOLCE2 6.87765105520563e-07 0.700523664739919 0.299475647494976 procollagen C-endopeptidase enhancer 2 FUNCTION: Binds to the C-terminal propeptide of types I and II procollagens and may enhance the cleavage of that propeptide by BMP1. {ECO:0000269|PubMed:12393877}.; . TISSUE SPECIFICITY: Highly expressed in the heart, trabecular meshwork, pituitary gland, bladder, mammary gland, trachea and placenta and weakly expressed in the brain. Expressed in cartilage. {ECO:0000269|PubMed:10873381, ECO:0000269|PubMed:11597177, ECO:0000269|PubMed:12393877}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;hypothalamus;colon;parathyroid;skin;uterus;prostate;whole body;lung;bone;placenta;pituitary gland;alveolus;liver;testis;spleen;kidney;brain; superior cervical ganglion;adipose tissue;trachea;ciliary ganglion;trigeminal ganglion; 0.14001 0.08463 0.066214104 58.95848077 517.122 4.64926 PCOS1 . . . polycystic ovary syndrome 1 . . . . . . . . . . . PCP2 1.2765672414005e-05 0.218680570767598 0.781306663559988 Purkinje cell protein 2 FUNCTION: May function as a cell-type specific modulator for G protein-mediated cell signaling. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;testis;brain;unclassifiable (Anatomical System);heart;hypothalamus;pharynx;blood;lens;bile duct;lung;cornea;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; . 0.19587 0.16205 0.128714042 63.19886766 245.23731 3.37903 PCP4 0.0751039149902311 0.747204481416701 0.177691603593068 Purkinje cell protein 4 FUNCTION: Probable regulator of calmodulin signaling. {ECO:0000269|PubMed:19106096}.; . . smooth muscle;ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;whole body;optic nerve;endometrium;thyroid;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;adrenal cortex;lens;trabecular meshwork;placenta;hippocampus;macula lutea;mammary gland; amygdala;whole brain;thalamus;medulla oblongata;subthalamic nucleus;hypothalamus;globus pallidus;pons;caudate nucleus;parietal lobe;cingulate cortex;cerebellum; 0.22284 . 0.079165051 59.43029016 . . PCP4L1 0.223985830023401 0.647154077834447 0.128860092142152 Purkinje cell protein 4 like 1 . . . . . 0.11646 . 0.323496558 72.93583392 40.40862 1.18576 PCSK1 0.0896398214145992 0.910344874744069 1.53038413319795e-05 proprotein convertase subtilisin/kexin type 1 FUNCTION: Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Substrates include POMC, renin, enkephalin, dynorphin, somatostatin, insulin and AGRP. {ECO:0000250|UniProtKB:P63239}.; DISEASE: Proprotein convertase 1 deficiency (PC1 deficiency) [MIM:600955]: Characterized by obesity, hypogonadism, hypoadrenalism, reactive hypoglycemia as well as marked small- intestinal absorptive dysfunction It is due to impaired processing of prohormones. {ECO:0000269|PubMed:14617756, ECO:0000269|PubMed:17595246, ECO:0000269|PubMed:9207799}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;cartilage;islets of Langerhans;hypothalamus;fovea centralis;retina;breast;lung;bone;macula lutea;hippocampus;pituitary gland;testis;brain;stomach; amygdala;whole brain;occipital lobe;medulla oblongata;subthalamic nucleus;hypothalamus;beta cell islets;prefrontal cortex;globus pallidus;ciliary ganglion;pons;parietal lobe;pituitary; 0.35142 0.33991 -0.420619508 25.72540694 2006.75712 8.25050 PCSK1N 0.444049066588872 0.454924430591728 0.101026502819399 proprotein convertase subtilisin/kexin type 1 inhibitor FUNCTION: May function in the control of the neuroendocrine secretory pathway. Proposed be a specific endogenous inhibitor of PCSK1. ProSAAS and Big PEN-LEN, both containing the C-terminal inhibitory domain, but not the further processed peptides reduce PCSK1 activity in the endoplasmic reticulum and Golgi. It reduces the activity of the 84 kDa form but not the autocatalytically derived 66 kDa form of PCSK1. Subsequent processing of proSAAS may eliminate the inhibition. Slows down convertase-mediated processing of proopiomelanocortin and proenkephalin. May control the intracellular timing of PCSK1 rather than its total level of activity. The function of the processed secreted peptides is not known (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain and pancreas. {ECO:0000269|PubMed:10632593}.; fovea centralis;choroid;retina;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;pituitary gland;iris;testis;pineal gland;brain;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pineal body;lens;pancreas;lung;placenta;macula lutea;hippocampus;visual apparatus;liver;spleen;kidney; whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;pituitary;cerebellum; 0.13475 0.11176 . . 2.39995 0.08317 PCSK2 0.994186021657942 0.00581394658351392 3.17585437215564e-08 proprotein convertase subtilisin/kexin type 2 FUNCTION: Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Responsible for the release of glucagon from proglucagon in pancreatic A cells. {ECO:0000269|PubMed:9287128}.; . . ovary;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;bone;pituitary gland;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pineal body;lens;skeletal muscle;lung;adrenal gland;placenta;hippocampus;visual apparatus;kidney; whole brain;amygdala;dorsal root ganglion;thalamus;medulla oblongata;occipital lobe;temporal lobe;pons;fetal thyroid;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.65844 0.26773 -1.111360919 6.717386176 40.76858 1.19481 PCSK4 6.59246485167205e-13 0.113546768860938 0.886453231138403 proprotein convertase subtilisin/kexin type 4 FUNCTION: Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Plays a role in transcriptional coactivation. May be involved in stabilizing the multiprotein transcription complex. {ECO:0000269|PubMed:16040806}.; . TISSUE SPECIFICITY: Placenta. {ECO:0000269|PubMed:16040806}.; unclassifiable (Anatomical System);medulla oblongata;optic nerve;lung;endometrium;bone;macula lutea;testis;fovea centralis;choroid;lens;brain;retina; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.09952 0.12910 0.606246644 82.93229535 734.41331 5.37512 PCSK5 0.000207778974917015 0.999792220475152 5.49931147551462e-10 proprotein convertase subtilisin/kexin type 5 FUNCTION: Likely to represent a widespread endoprotease activity within the constitutive and regulated secretory pathway. Capable of cleavage at the RX(K/R)R consensus motif. Plays an essential role in pregnancy establishment by proteolytic activation of a number of important factors such as BMP2, CALD1 and alpha- integrins. {ECO:0000269|PubMed:19764806, ECO:0000269|PubMed:20555025, ECO:0000269|PubMed:22740495}.; . TISSUE SPECIFICITY: Expressed in T-lymphocytes.; . . 0.12161 0.24178 2.837134915 99.10356216 13178.92317 24.65250 PCSK6 0.0104695863094061 0.989513656095092 1.67575955015096e-05 proprotein convertase subtilisin/kexin type 6 FUNCTION: Likely to represent an endoprotease activity within the constitutive secretory pathway, with unique restricted distribution in both neuroendocrine and non-neuroendocrine tissues and capable of cleavage at the RX(K/R)R consensus motif.; . TISSUE SPECIFICITY: Each PACE4 isoform exhibits a unique restricted distribution. Isoform PACE4A-I is expressed in heart, brain, placenta, lung, skeletal muscle, kidney, pancreas, but at comparatively higher levels in the liver. Isoform PACE4A-II is at least expressed in placenta. Isoform PACE4B was only found in the embryonic kidney cell line from which it was isolated. Isoform PACE4C and isoform PACE4D are expressed in placenta. Isoform PACE4E-I is expressed in cerebellum, placenta and pituitary. Isoform PACE4E-II is at least present in cerebellum.; unclassifiable (Anatomical System);medulla oblongata;ovary;cartilage;heart;islets of Langerhans;colon;parathyroid;choroid;skin;skeletal muscle;breast;uterus;prostate;whole body;lung;frontal lobe;placenta;iris;liver;testis;spleen;cervix;kidney;brain; dorsal root ganglion;whole brain;occipital lobe;superior cervical ganglion;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;atrioventricular node;caudate nucleus;pons;skeletal muscle;fetal liver;liver;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;cerebellum; 0.26934 0.24150 . . 1722.43766 7.65632 PCSK6-AS1 . . . PCSK6 antisense RNA 1 . . . . . . . . . . . PCSK7 0.191369613352617 0.808536146716536 9.42399308470885e-05 proprotein convertase subtilisin/kexin type 7 FUNCTION: Likely to represent a ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RXXX[KR]R consensus motif.; . TISSUE SPECIFICITY: Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocyte.; ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;nervous;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;parotid gland;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hypopharynx;amnion;head and neck;kidney;stomach;aorta; hypothalamus;bone marrow; 0.42938 0.10463 -0.753139731 13.67067705 311.97029 3.75925 PCSK9 1.02507611210468e-10 0.0848035964994896 0.915196403398003 proprotein convertase subtilisin/kexin type 9 FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments (PubMed:18039658). Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation (PubMed:18799458, PubMed:17461796, PubMed:18197702, PubMed:22074827). Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non- acetylated intermediates of BACE1 in the early secretory pathway (PubMed:18660751). Inhibits epithelial Na(+) channel (ENaC)- mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways. {ECO:0000269|PubMed:17461796, ECO:0000269|PubMed:18039658, ECO:0000269|PubMed:18197702, ECO:0000269|PubMed:18660751, ECO:0000269|PubMed:18799458, ECO:0000269|PubMed:22074827, ECO:0000269|PubMed:22493497, ECO:0000269|PubMed:22580899}.; DISEASE: Hypercholesterolemia, autosomal dominant, 3 (HCHOLA3) [MIM:603776]: A familial condition characterized by elevated circulating cholesterol contained in either low-density lipoproteins alone or also in very-low-density lipoproteins. {ECO:0000269|PubMed:12730697, ECO:0000269|PubMed:18799458, ECO:0000269|PubMed:24808179}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in neuro-epithelioma, colon carcinoma, hepatic and pancreatic cell lines, and in Schwann cells.; unclassifiable (Anatomical System);cartilage;heart;ovary;colon;blood;skin;uterus;pancreas;lung;endometrium;bone;liver;testis;spleen;cervix;brain;mammary gland;stomach;cerebellum; . 0.34184 0.19640 0.942426495 89.89148384 736.36615 5.38585 PCTP 1.63044512468483e-05 0.428209285661142 0.571774409887611 phosphatidylcholine transfer protein FUNCTION: Catalyzes the transfer of phosphatidylcholine between membranes. Binds a single lipid molecule. {ECO:0000269|PubMed:12055623}.; . TISSUE SPECIFICITY: Highest expression in liver, placenta, testis, kidney and heart. Low levels in brain and lung. No expression detected in thymus. {ECO:0000269|PubMed:10542325}.; unclassifiable (Anatomical System);medulla oblongata;lymph node;ovary;heart;colon;parathyroid;skin;skeletal muscle;uterus;prostate;lung;bone;placenta;hippocampus;liver;testis;cervix;spleen;germinal center;kidney;brain;mammary gland;bladder;aorta;tonsil;stomach; placenta;globus pallidus;ciliary ganglion;kidney;bone marrow; 0.04262 0.13913 0.12689526 63.00424628 3657.86041 11.75381 PCYOX1 6.73322799744091e-12 0.0175388447606905 0.982461155232576 prenylcysteine oxidase 1 FUNCTION: Involved in the degradation of prenylated proteins. Cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;cerebral cortex;endometrium;larynx;bone;pituitary gland;testis;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;skeletal muscle;bile duct;pancreas;pia mater;lung;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;stomach;cerebellum; . 0.09348 0.13312 -0.200157416 39.11299835 633.74076 5.06992 PCYOX1L 1.26712222774021e-05 0.608667728754868 0.391319600022855 prenylcysteine oxidase 1 like FUNCTION: Probable oxidoreductase. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;cartilage;ovary;heart;adrenal cortex;colon;parathyroid;blood;fovea centralis;skin;bone marrow;uterus;prostate;whole body;lung;frontal lobe;larynx;nasopharynx;bone;placenta;macula lutea;liver;testis;head and neck;spleen;kidney;germinal center;brain;stomach; superior cervical ganglion;medulla oblongata;prefrontal cortex;testis; 0.21268 . 0.597144447 82.7435716 882.03672 5.78591 PCYT1A 0.0983000755796718 0.900125669501523 0.0015742549188052 phosphate cytidylyltransferase 1, choline, alpha FUNCTION: Controls phosphatidylcholine synthesis.; DISEASE: Spondylometaphyseal dysplasia with cone-rod dystrophy (SMDCRD) [MIM:608940]: A disorder characterized by postnatal growth deficiency resulting in profound short stature, rhizomelia with bowing of the lower extremities, platyspondyly with anterior vertebral protrusions, progressive metaphyseal irregularity and cupping with shortened tubular bones, and early-onset progressive visual impairment associated with a pigmentary maculopathy and electroretinographic evidence of cone-rod dysfunction. {ECO:0000269|PubMed:24387990, ECO:0000269|PubMed:24387991}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;ovary;heart;islets of Langerhans;colon;blood;skin;breast;uterus;prostate;lung;endometrium;larynx;thyroid;placenta;visual apparatus;alveolus;hypopharynx;liver;testis;head and neck;germinal center;kidney;brain;bladder; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.75481 . -0.846787714 11.05803255 78.82184 1.87555 PCYT1B 0.944740314394971 0.0550602729312996 0.000199412673729447 phosphate cytidylyltransferase 1, choline, beta FUNCTION: Controls phosphatidylcholine synthesis.; . TISSUE SPECIFICITY: Highly expressed in testis, placenta, brain, ovary and fetus.; unclassifiable (Anatomical System);blood;choroid;fovea centralis;lens;skeletal muscle;retina;optic nerve;lung;frontal lobe;macula lutea;liver;testis;spleen; superior cervical ganglion;trachea;testis;trigeminal ganglion; 0.19436 0.13353 -0.05129383 49.75819769 9.71937 0.35666 PCYT1B-AS1 . . . PCYT1B antisense RNA 1 . . . . . . . . . . . PCYT2 0.248194491721239 0.750483905163942 0.00132160311481909 phosphate cytidylyltransferase 2, ethanolamine FUNCTION: Plays an important role in the biosynthesis of the phospholipid phosphatidylethanolamine. Catalyzes the formation of CDP-ethanolamine.; . TISSUE SPECIFICITY: Strongest expression in liver, heart, and skeletal muscle.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;muscle;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;liver;testis; 0.31484 0.11275 -0.448125345 24.19202642 31.9275 1.00433 PDAP1 0.00558937831758173 0.898293654871684 0.0961169668107342 PDGFA associated protein 1 FUNCTION: Enhances PDGFA-stimulated cell growth in fibroblasts, but inhibits the mitogenic effect of PDGFB. {ECO:0000250}.; . . medulla oblongata;ovary;sympathetic chain;skin;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;heart;ciliary ganglion;atrioventricular node;skeletal muscle; 0.42994 0.12514 -0.317668748 31.45789101 22.91664 0.76348 PDB1 . . . Paget disease of bone 1 . . . . . . . . . . . PDB4 . . . Paget disease of bone 4 . . . . . . . . . . . PDB5 . . . Paget disease of bone 5 . . . . . . . . . . . PDB6 . . . Paget disease of bone 6 . . . . . . . . . . . PDC 2.22523081961224e-06 0.155372187488462 0.844625587280718 phosducin FUNCTION: May participate in the regulation of visual phototransduction or in the integration of photoreceptor metabolism. Inhibits the transcriptional activation activity of the cone-rod homeobox CRX. {ECO:0000269|PubMed:10866677}.; . . optic nerve;macula lutea;fovea centralis;choroid;lens;retina; superior cervical ganglion;ciliary ganglion; 0.16828 0.47841 -0.073340031 48.11866006 61.5524 1.59898 PDCD1 0.0179540479322239 0.894121847643326 0.0879241044244502 programmed cell death 1 FUNCTION: Inhibitory cell surface receptor involved in the regulation of T-cell function during immunity and tolerance. Upon ligand binding, inhibits T-cell effector functions in an antigen- specific manner. Possible cell death inducer, in association with other factors. {ECO:0000269|PubMed:21276005}.; DISEASE: Systemic lupus erythematosus 2 (SLEB2) [MIM:605218]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:12402038}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . kidney; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.14221 0.27803 -0.314027422 31.9297004 885.9353 5.79855 PDCD1LG2 0.000429826390067904 0.649050165852396 0.350520007757536 programmed cell death 1 ligand 2 FUNCTION: Involved in the costimulatory signal, essential for T- cell proliferation and IFNG production in a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in heart, placenta, pancreas, lung and liver and weakly expressed in spleen, lymph nodes and thymus. {ECO:0000269|PubMed:11224527}.; . . 0.05765 0.16231 0.373041938 75.29488087 1508.33894 7.21599 PDCD2 0.000192308695614694 0.714949567156454 0.284858124147931 programmed cell death 2 FUNCTION: May be a DNA-binding protein with a regulatory function. May play an important role in cell death and/or in regulation of cell proliferation.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;bile duct;lung;cornea;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;testis;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.25318 0.18895 0.305084559 72.22811984 201.83282 3.06662 PDCD2L 4.99044178798444e-05 0.664889710992678 0.335060384589442 programmed cell death 2-like FUNCTION: Over-expression suppresses AP1, CREB, NFAT, and NF-kB transcriptional activation, and delays cell cycle progression at S phase. {ECO:0000269|PubMed:17393540}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;blood;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;cervix;kidney;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.46508 0.09553 -0.227663163 37.11370606 42.40247 1.23269 PDCD4 0.000577683801357511 0.974180271647249 0.0252420445513932 programmed cell death 4 (neoplastic transformation inhibitor) FUNCTION: Inhibits translation initiation and cap-dependent translation. May excert its function by hindering the interaction between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A. Modulates the activation of JUN kinase. Down-regulates the expression of MAP4K1, thus inhibiting events important in driving invasion, namely, MAPK85 activation and consequent JUN-dependent transcription. May play a role in apoptosis. Tumor suppressor. Inhibits tumor promoter-induced neoplastic transformation. Binds RNA (By similarity). {ECO:0000250, ECO:0000269|PubMed:16357133, ECO:0000269|PubMed:16449643, ECO:0000269|PubMed:17053147, ECO:0000269|PubMed:18296639, ECO:0000269|PubMed:19153607, ECO:0000269|PubMed:19204291}.; . TISSUE SPECIFICITY: Up-regulated in proliferative cells. Highly expressed in epithelial cells of the mammary gland. Reduced expression in lung cancer and colon carcinoma. {ECO:0000269|PubMed:10632927, ECO:0000269|PubMed:12898601, ECO:0000269|PubMed:16449643}.; ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;adrenal gland;placenta;hypopharynx;amnion;head and neck;kidney;stomach;aorta;thymus; pancreas;fetal liver;superior cervical ganglion;trachea;salivary gland;placenta;beta cell islets;ciliary ganglion;white blood cells;pituitary; 0.61290 0.14649 -0.157884861 42.05590941 43.18368 1.24776 PDCD4-AS1 . . . PDCD4 antisense RNA 1 . . . . . . . . . . . PDCD5 0.00712094198898545 0.76558449463798 0.227294563373034 programmed cell death 5 FUNCTION: May function in the process of apoptosis.; . TISSUE SPECIFICITY: Widely expressed. Highest levels in heart, testis, kidney, pituitary gland, adrenal gland and placenta.; myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; . 0.51978 0.14229 0.080983847 59.76055674 44.97515 1.28790 PDCD5P1 . . . programmed cell death 5 pseudogene 1 . . . . . . . . . . . PDCD5P2 . . . programmed cell death 5 pseudogene 2 . . . . . . . . . . . PDCD6 0.714212208927811 0.282549335805922 0.00323845526626791 programmed cell death 6 FUNCTION: Calcium-binding protein required for T-cell receptor-, Fas-, and glucocorticoid-induced cell death. May mediate Ca(2+)- regulated signals along the death pathway (By similarity). Calcium-dependent adapter necessary for the association between PDCD6IP and TSG101. Interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity. May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphoprylation of the Akt signaling pathway. Seems to play a role in the regulation of the distribution and function of MCOLN1 in the endosomal pathway. Isoform 2 has a lower Ca(2+) affinity than isoform 1. Isoform 1 and, to a lesser extend, isoform 2, can stabilize SHISA5. {ECO:0000250, ECO:0000269|PubMed:16132846, ECO:0000269|PubMed:17889823, ECO:0000269|PubMed:19520058, ECO:0000269|PubMed:19864416, ECO:0000269|PubMed:21893193}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;placenta;hippocampus;duodenum;hypopharynx;amnion;head and neck;kidney;stomach;thymus; whole brain;amygdala;subthalamic nucleus;superior cervical ganglion;skeletal muscle;skin;cerebellum; . 0.16352 -0.361761279 28.6329323 959.5815 5.99889 PDCD6IP 0.751958921876168 0.248040335310253 7.42813578630688e-07 programmed cell death 6 interacting protein FUNCTION: Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). Appears to be an adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis. Involved in HIV-1 virus budding. Can replace TSG101 it its role of supporting HIV-1 release; this function implies the interaction with CHMP4B. May play a role in the regulation of both apoptosis and cell proliferation. {ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14739459, ECO:0000269|PubMed:17428861, ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;iris;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;bile duct;pancreas;pia mater;lung;mesenchyma;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.26577 0.12495 -0.306750577 32.23047889 8447.59531 19.81694 PDCD6IPP1 . . . PDCD6IP pseudogene 1 . . . . . . . . . . . PDCD6IPP2 . . . PDCD6IP pseudogene 2 . . . . . . . . . . . PDCD7 0.045374793576378 0.92912236520865 0.0255028412149719 programmed cell death 7 FUNCTION: Promotes apoptosis when overexpressed. {ECO:0000250}.; . . ovary;salivary gland;skin;retina;bone marrow;prostate;whole body;frontal lobe;thyroid;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;spinal cord;blood;breast;lung;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;thymus; . 0.24992 0.10633 . . 401.45029 4.20219 PDCD10 0.985734930905909 0.0142580871490468 6.98194504464679e-06 programmed cell death 10 FUNCTION: Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity and STK26 activity. Important for cell migration, and for normal structure and assembly of the Golgi complex. Important for KDR/VEGFR2 signaling. Increases the stability of KDR/VEGFR2 and prevents its breakdown. Required for normal cardiovascular development. Required for normal angiogenesis, vasculogenesis and hematopoiesis during embryonic development (By similarity). {ECO:0000250, ECO:0000269|PubMed:15543491, ECO:0000269|PubMed:17360971, ECO:0000269|PubMed:20332113}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15543491}.; . . 0.76070 0.12390 -0.031067188 51.03798066 31.98829 1.00545 PDCD11 0.468448697895289 0.531551302099376 5.33489187132011e-12 programmed cell death 11 FUNCTION: Essential for the generation of mature 18S rRNA, specifically necessary for cleavages at sites A0, 1 and 2 of the 47S precursor. Directly interacts with U3 snoRNA. {ECO:0000269|PubMed:17654514}.; . . . . 0.04969 0.10522 -0.242676135 36.1759849 7424.65781 18.50415 PDCL 0.3120279698914 0.670323797794298 0.0176482323143027 phosducin like FUNCTION: Isoform 1: Functions as a co-chaperone for CCT in the assembly of heterotrimeric G protein complexes, facilitates the assembly of both Gbeta-Ggamma and RGS-Gbeta5 heterodimers.; . . fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;lens;lung;mesenchyma;nasopharynx;placenta;macula lutea;liver;alveolus;amnion;spleen;cervix;kidney; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.10008 0.12308 -0.271755481 34.31823543 24.59469 0.80819 PDCL2 0.0413602868128142 0.844538804752243 0.114100908434942 phosducin like 2 FUNCTION: May play a role in germ cell maturation. {ECO:0000250}.; . . unclassifiable (Anatomical System);blood; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;appendix;atrioventricular node;skin;skeletal muscle; 0.24036 0.09920 0.014844891 54.94810097 75.77943 1.82320 PDCL2P1 . . . phosducin-like 2 pseudogene 1 . . . . . . . . . . . PDCL2P2 . . . phosducin-like 2 pseudogene 2 . . . . . . . . . . . PDCL3 0.000392970999859276 0.629523819103467 0.370083209896674 phosducin like 3 FUNCTION: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, controlling its abundance and inhibiting its ubiquitination and degradation. Modulates the activation of caspases during apoptosis. Is a substrate for Orgyia pseudotsugata multicapsid polyhedrosis virus (OpMNPV) IAP-mediated ubiquitination. {ECO:0000269|PubMed:15371430, ECO:0000269|PubMed:23792958}.; . TISSUE SPECIFICITY: Expressed in all tissues examined including spleen, thymus, prostate, testis, ovary, small intestine and colon. {ECO:0000269|PubMed:15371430}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;pharynx;blood;lens;skeletal muscle;breast;pancreas;pia mater;lung;cornea;nasopharynx;trabecular meshwork;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach;aorta; . 0.09987 0.09248 0.016664174 55.21939137 47.08303 1.32751 PDCL3P1 . . . phosducin-like 3 pseudogene 1 . . . . . . . . . . . PDCL3P2 . . . phosducin-like 3 pseudogene 2 . . . . . . . . . . . PDCL3P3 . . . phosducin-like 3 pseudogene 3 . . . . . . . . . . . PDCL3P4 . . . phosducin-like 3 pseudogene 4 . . . . . . . . . . . PDCL3P5 . . . phosducin-like 3 pseudogene 5 . . . . . . . . . . . PDCL3P6 . . . phosducin-like 3 pseudogene 6 . . . . . . . . . . . PDCL3P7 . . . phosducin-like 3 pseudogene 7 . . . . . . . . . . . PDDC1 0.617289947810584 0.374765451032814 0.00794460115660213 Parkinson disease 7 domain containing 1 . . . unclassifiable (Anatomical System);cartilage;umbilical cord;heart;muscle;colon;blood;fovea centralis;skin;retina;uterus;pancreas;prostate;optic nerve;whole body;lung;endometrium;placenta;macula lutea;hippocampus;liver;testis;kidney;brain;stomach; ciliary ganglion;trigeminal ganglion; 0.11916 . -0.602450568 17.91106393 37.10182 1.10854 PDE1A 0.730656355381448 0.269320540377807 2.31042407455387e-05 phosphodiesterase 1A FUNCTION: Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a higher affinity for cGMP than for cAMP.; . TISSUE SPECIFICITY: Several tissues, including brain, kidney, testes and heart.; unclassifiable (Anatomical System);medulla oblongata;ovary;retina;prostate;lung;frontal lobe;cochlea;thyroid;liver;alveolus;testis;cervix;kidney;spinal ganglion;brain;stomach; testis - interstitial;superior cervical ganglion;testis;trigeminal ganglion; 0.22469 0.20059 -0.734731259 14.01863647 40.97898 1.20066 PDE1B 0.94673728390002 0.0532611970669243 1.51903305520338e-06 phosphodiesterase 1B FUNCTION: Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a preference for cGMP as a substrate. {ECO:0000269|PubMed:15260978}.; . . unclassifiable (Anatomical System);uterus;lung;islets of Langerhans;colon;brain;skin;skeletal muscle;retina;cerebellum; subthalamic nucleus;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;pons;caudate nucleus;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.38354 0.15734 -0.157884861 42.05590941 30.45684 0.97060 PDE1C 0.000270703875847391 0.999595512437577 0.000133783686575639 phosphodiesterase 1C FUNCTION: Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a high affinity for both cAMP and cGMP.; . TISSUE SPECIFICITY: Expressed in several tissues, including brain and heart.; unclassifiable (Anatomical System);lung;mesenchyma;hypothalamus;bone;placenta;iris;brain;mammary gland; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.24291 0.17371 0.047806932 57.51946214 247.32468 3.39210 PDE2A 0.988417592612146 0.0115824071001366 2.87717120482479e-10 phosphodiesterase 2A FUNCTION: Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes.; . TISSUE SPECIFICITY: Expressed in brain and to a lesser extent in heart, placenta, lung, skeletal muscle, kidney and pancreas.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);amygdala;heart;lacrimal gland;adrenal cortex;lens;lung;macula lutea;hippocampus;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; . 0.31412 0.18339 -1.085675268 7.147912243 357.59713 4.00736 PDE3A 0.106612095996096 0.893376507531194 1.13964727101701e-05 phosphodiesterase 3A FUNCTION: Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. {ECO:0000250|UniProtKB:Q9Z0X4}.; DISEASE: Hypertension and brachydactyly syndrome (HTNB) [MIM:112410]: A syndrome characterized by brachydactyly type E, severe salt-independent but age-dependent hypertension, an increased fibroblast growth rate, neurovascular contact at the rostral-ventrolateral medulla, and altered baroreflex blood pressure regulation. It results in death from stroke before age 50 years when untreated. Brachydactyly type E is characterized by shortening of the fingers mainly in the metacarpals and metatarsals. {ECO:0000269|PubMed:25961942}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;lung;placenta;thyroid;bone;macula lutea;liver;testis;head and neck;kidney; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.09476 0.14669 -1.104093597 6.894314697 1899.16799 8.01225 PDE3B 0.0036164696577972 0.996367665052451 1.58652897514079e-05 phosphodiesterase 3B FUNCTION: Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. May play a role in fat metabolism. Regulates cAMP binding of RAPGEF3. Through simultaneous binding to RAPGEF3 and PIK3R6 assembles a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis. {ECO:0000269|PubMed:15147193, ECO:0000269|PubMed:21393242}.; . TISSUE SPECIFICITY: Abundant in adipose tissues.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;skin;skeletal muscle;bone marrow;breast;pancreas;prostate;lung;cerebral cortex;visual apparatus;pituitary gland;liver;testis;spleen;kidney;brain;mammary gland;bladder;aorta;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.18608 0.39801 0.07167258 59.15899976 220.4717 3.20931 PDE4A 0.976417636472092 0.023582323111838 4.04160701323524e-08 phosphodiesterase 4A FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. {ECO:0000269|PubMed:11566027, ECO:0000269|PubMed:17727341}.; . TISSUE SPECIFICITY: Isoform 1 is widely expressed. Isoform 2 is abundant in liver, stomach, testis, thyroid and adrenal glands. It is also found in placenta, kidney, pancreas, ovary, uterus, skin, monocytes, mast cells, macrophages, as well as in bronchial smooth muscle. Isoform 6 is expressed at high levels in the heart and small intestine. It is also found in the brain, kidney, spleen, colon, salivary gland, ovary and peripheral blood lymphocytes. Isoform 7 is expressed predominantly in skeletal muscle and brain and at lower levels in the testis. Isoform 7 is expressed in the brain. Found in specific neuronal subpopulations in cortex, spinal cord and cerebellum (at protein level). {ECO:0000269|PubMed:11306681, ECO:0000269|PubMed:15738310, ECO:0000269|PubMed:18095939}.; ovary;salivary gland;colon;parathyroid;fovea centralis;skin;uterus;prostate;endometrium;bone;thyroid;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;nervous;islets of Langerhans;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;cerebellum; dorsal root ganglion;superior cervical ganglion;medulla oblongata;cerebellum peduncles;temporal lobe;pons;atrioventricular node;skeletal muscle;fetal liver;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.08521 0.11239 -1.105907904 6.86482661 973.10156 6.03083 PDE4B 0.709078616910536 0.290915493708856 5.88938060772235e-06 phosphodiesterase 4B FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in mediating central nervous system effects of therapeutic agents ranging from antidepressants to antiasthmatic and anti-inflammatory agents. {ECO:0000269|PubMed:10846163, ECO:0000269|PubMed:15003452}.; . TISSUE SPECIFICITY: Expressed in brain, heart, lung and skeletal muscle.; smooth muscle;umbilical cord;ovary;salivary gland;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.84740 0.40738 -0.686998355 15.26893135 150.61725 2.67949 PDE4C 4.88574724786651e-05 0.992360867201174 0.00759027532634714 phosphodiesterase 4C FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. {ECO:0000269|PubMed:17727341}.; . TISSUE SPECIFICITY: Expressed in various tissues but not in cells of the immune system.; unclassifiable (Anatomical System);lung;frontal lobe;ovary;placenta;testis;colon;brain; dorsal root ganglion;superior cervical ganglion;tongue;adrenal cortex;pons;atrioventricular node;skin;skeletal muscle;prostate;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.15384 0.17413 0.424410872 77.25878745 2015.82594 8.26686 PDE4D 0.983199686418857 0.0168002270009629 8.65801803613267e-08 phosphodiesterase 4D FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. {ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036}.; DISEASE: Note=Genetic variations in PDE4D might be associated with susceptibility to stroke. PubMed:17006457 states that association with stroke has to be considered with caution. {ECO:0000269|PubMed:17006457}.; DISEASE: Acrodysostosis 2, with or without hormone resistance (ACRDYS2) [MIM:614613]: A pleiotropic disorder characterized by skeletal, endocrine, and neurological abnormalities. Skeletal features include brachycephaly, midface hypoplasia with a small upturned nose, brachydactyly, and lumbar spinal stenosis. Endocrine abnormalities include hypothyroidism and hypogonadism in males and irregular menses in females. Developmental disability is a common finding but is variable in severity and can be associated with significant behavioral problems. {ECO:0000269|PubMed:22464250, ECO:0000269|PubMed:22464252, ECO:0000269|PubMed:23033274, ECO:0000269|PubMed:23043190}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in colonic epithelial cells (at protein level). Widespread; most abundant in skeletal muscle. Isoform 6 is detected in brain. Isoform 8 is detected in brain, placenta, lung and kidney. Isoform 7 is detected in heart and skeletal muscle. {ECO:0000269|PubMed:12834813, ECO:0000269|PubMed:17244609}.; unclassifiable (Anatomical System);ovary;cartilage;heart;colon;blood;skin;skeletal muscle;uterus;prostate;whole body;lung;endometrium;larynx;pituitary gland;liver;testis;spleen;head and neck;kidney;germinal center;brain;stomach;thymus; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.24539 0.34543 -1.375949569 4.393724935 15.63977 0.55771 PDE4DIP . . . phosphodiesterase 4D interacting protein FUNCTION: May function as an anchor sequestering components of the cAMP-dependent pathway to Golgi and/or centrosomes. {ECO:0000250}.; DISEASE: Note=A chromosomal aberration involving PDE4DIP may be the cause of a myeloproliferative disorder (MBD) associated with eosinophilia. Translocation t(1;5)(q23;q33) that forms a PDE4DIP- PDGFRB fusion protein. {ECO:0000269|PubMed:12907457}.; TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle and to a lower extent in brain and placenta. {ECO:0000269|PubMed:11374908}.; myocardium;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;spinal cord;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;cerebellum; occipital lobe;thalamus;superior cervical ganglion;fetal brain;placenta;spinal cord;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . . 7.985992467 99.94692144 8042.34707 19.35299 PDE4DIPP1 . . . phosphodiesterase 4D interacting protein pseudogene 1 . . . . . . . . . . . PDE5A 0.00339090594474959 0.996591682216308 1.74118389419238e-05 phosphodiesterase 5A FUNCTION: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'- GMP (PubMed:9714779, PubMed:15489334). Specifically regulates nitric-oxide-generated cGMP (PubMed:15489334). {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9714779}.; . TISSUE SPECIFICITY: Expressed in aortic smooth muscle cells, heart, placenta, skeletal muscle and pancreas and, to a much lesser extent, in brain, liver and lung.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;skeletal muscle;retina;prostate;whole body;lung;thyroid;placenta;visual apparatus;hippocampus;testis;cervix;kidney;spinal ganglion;brain;artery;aorta; superior cervical ganglion;pons;skeletal muscle; 0.17795 0.23802 1.047190339 91.34229771 426.62286 4.31406 PDE6A 6.60508610952056e-12 0.830863454392201 0.169136545601194 phosphodiesterase 6A FUNCTION: This protein participates in processes of transmission and amplification of the visual signal.; DISEASE: Retinitis pigmentosa 43 (RP43) [MIM:613810]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:10393062, ECO:0000269|PubMed:7493036}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);optic nerve;bone;macula lutea;colon;fovea centralis;choroid;lens;skeletal muscle;retina; superior cervical ganglion;temporal lobe;pons;parietal lobe; 0.38982 0.20248 -0.189246284 39.30761972 881.28278 5.78422 PDE6B 1.62565147164988e-13 0.529057744345711 0.470942255654126 phosphodiesterase 6B FUNCTION: This protein participates in processes of transmission and amplification of the visual signal. Necessary for the formation of a functional phosphodiesterase holoenzyme.; DISEASE: Retinitis pigmentosa 40 (RP40) [MIM:613801]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:22334370, ECO:0000269|PubMed:8394174, ECO:0000269|PubMed:8557257, ECO:0000269|PubMed:8595886, ECO:0000269|PubMed:8698075, ECO:0000269|PubMed:8956055, ECO:0000269|PubMed:9543643}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Night blindness, congenital stationary, autosomal dominant 2 (CSNBAD2) [MIM:163500]: A non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia. {ECO:0000269|PubMed:8075643}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;salivary gland;pharynx;colon;blood;skeletal muscle;retina;breast;uterus;prostate;lung;visual apparatus;liver;testis;kidney;brain;pineal gland;bladder; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.61184 0.55597 -0.538378753 20.05189903 482.88245 4.52475 PDE6C 7.4249966167879e-08 0.998807997782114 0.00119192796792033 phosphodiesterase 6C . DISEASE: Cone dystrophy 4 (COD4) [MIM:613093]: An early-onset cone dystrophy. Cone dystrophies are retinal dystrophies characterized by progressive degeneration of the cone photoreceptors with preservation of rod function, as indicated by electroretinogram. However, some rod involvement may be present in some cone dystrophies, particularly at late stage. Affected individuals suffer from photophobia, loss of visual acuity, color vision and central visual field. Another sign is the absence of macular lesions for many years. Cone dystrophies are distinguished from the cone-rod dystrophies in which some loss of peripheral vision also occurs. {ECO:0000269|PubMed:19615668}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.34895 0.13306 0.115764778 62.17268224 3123.84709 10.63181 PDE6D 0.0844960932718429 0.871358036211534 0.0441458705166231 phosphodiesterase 6D FUNCTION: Promotes the release of prenylated target proteins from cellular membranes (PubMed:9712853). Modulates the activity of prenylated or palmitoylated Ras family members by regulating their subcellular location (PubMed:22002721, PubMed:23698361). Required for normal ciliary targeting of farnesylated target proteins, such as INPP5E (PubMed:24166846). Modulates the subcellular location of target proteins by acting as a GTP specific dissociation inhibitor (GDI) (By similarity). Increases the affinity of ARL3 for GTP by several orders of magnitude. Stabilizes ARL3-GTP by decreasing the nucleotide dissociation rate (By similarity). {ECO:0000250|UniProtKB:O55057, ECO:0000269|PubMed:10518933, ECO:0000269|PubMed:22002721, ECO:0000269|PubMed:23559067, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:24166846, ECO:0000269|PubMed:9712853}.; . TISSUE SPECIFICITY: Widely expressed. Detected in various tissues including spleen, prostate gland, testis, ovary, small intestine, colon, retina, and peripheral blood. {ECO:0000269|PubMed:9712853}.; lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;stomach; whole brain;amygdala; 0.39233 0.19140 0.479642105 78.95140363 36.22935 1.08568 PDE6G 0.014216424092894 0.677118685905428 0.308664890001678 phosphodiesterase 6G FUNCTION: Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones.; DISEASE: Retinitis pigmentosa 57 (RP57) [MIM:613582]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:20655036}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;cartilage;pineal body;blood;parathyroid;fovea centralis;choroid;skeletal muscle;retina;uterus;lung;placenta;macula lutea;visual apparatus;liver;spleen;pineal gland;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.20666 0.13449 0.191216164 66.57230479 533.29397 4.71123 PDE6H 0.00652871284753312 0.513187596360356 0.48028369079211 phosphodiesterase 6H FUNCTION: Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones.; DISEASE: Cone dystrophy, retinal 3A (RCD3A) [MIM:610024]: A rare form of cone dystrophy associated with supernormal rod responses. The disorder is characterized by reduced visual acuity, photoaversion, night blindness, and abnormal color vision. At an early age, the retina shows subtle depigmentation at the macula and, later, more obvious areas of atrophy. {ECO:0000269|PubMed:15629837}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);optic nerve;pineal body;macula lutea;fovea centralis;choroid;pineal gland;retina; superior cervical ganglion;appendix;trigeminal ganglion;skeletal muscle; 0.32724 0.12944 0.101211609 60.95777306 11.63033 0.42151 PDE7A 0.19205771415361 0.807480412061557 0.000461873784832841 phosphodiesterase 7A FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May have a role in muscle signal transduction. {ECO:0000269|PubMed:19350606}.; . TISSUE SPECIFICITY: PDE7A1 is found at high levels in skeletal muscle and at low levels in a variety of tissues including brain and heart. It is expressed as well in two T-cell lines. PDE7A2 is found abundantly in skeletal muscle and at low levels in heart.; . . 0.63645 0.14596 -0.159704656 41.90846898 474.4538 4.50090 PDE7B 0.946452268895357 0.0535461915311974 1.53957344586715e-06 phosphodiesterase 7B FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in the control of cAMP-mediated neural activity and cAMP metabolism in the brain.; . . unclassifiable (Anatomical System);colon;skeletal muscle;skin;breast;prostate;optic nerve;lung;larynx;placenta;bone;testis;head and neck;brain;stomach; superior cervical ganglion;pons; 0.48259 0.13650 -0.291981272 33.20358575 81.71899 1.91609 PDE8A 0.713477056622093 0.286522713074327 2.30303579823865e-07 phosphodiesterase 8A FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development. {ECO:0000269|PubMed:18983167}.; . TISSUE SPECIFICITY: Expressed in most tissues except thymus and peripheral blood leukocytes. Highest levels in testis, ovary, small intestine and colon.; smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;testis - interstitial;thalamus;hypothalamus;atrioventricular node;caudate nucleus;globus pallidus;testis;ciliary ganglion;parietal lobe;cingulate cortex; 0.43995 0.13223 -0.200157416 39.11299835 317.57217 3.78359 PDE8B 0.986862335777411 0.0131376546495197 9.57306907025439e-09 phosphodiesterase 8B FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in specific signaling in the thyroid gland.; DISEASE: Striatal degeneration autosomal dominant (ADSD) [MIM:609161]: A movement disorder affecting the striatal part of the basal ganglia and characterized by bradykinesia, dysarthria and muscle rigidity. These symptoms resemble idiopathic Parkinson disease, but tremor is not present. {ECO:0000269|PubMed:20085714}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Primary pigmented nodular adrenocortical disease 3 (PPNAD3) [MIM:614190]: A rare bilateral adrenal defect causing ACTH-independent Cushing syndrome. Macroscopic appearance of the adrenals is characteristic with small pigmented micronodules observed in the cortex. Adrenal glands show overall normal size and weight, and multiple small yellow-to-dark brown nodules surrounded by a cortex with a uniform appearance. Microscopically, there are moderate diffuse cortical hyperplasia with mostly nonpigmented nodules, multiple capsular deficits and massive circumscribed and infiltrating extra-adrenal cortical excrescences with micronodules. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes. {ECO:0000269|PubMed:18431404}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Abundantly expressed in the thyroid. Also very weakly expressed in brain, spinal cord and placenta. In the thyroid isoform 1 predominates, and isoforms 2 and 6 are also highly expressed. In the placenta isoforms 1 and 2 are expressed equally. In the brain isoform 2 predominates. {ECO:0000269|PubMed:12372422, ECO:0000269|PubMed:12681444}.; unclassifiable (Anatomical System);cartilage;heart;ovary;tongue;islets of Langerhans;parathyroid;skin;uterus;prostate;lung;frontal lobe;bone;thyroid;placenta;hippocampus;liver;testis;head and neck;cervix;germinal center;kidney;mammary gland;brain; whole brain;occipital lobe;temporal lobe;caudate nucleus;pons;fetal thyroid;skeletal muscle;subthalamic nucleus;thyroid;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe; 0.47483 . -0.688817379 15.20405756 135.71543 2.53301 PDE9A 0.0020173637864315 0.99780072452504 0.000181911688528475 phosphodiesterase 9A FUNCTION: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP (PubMed:9624146, PubMed:18757755, PubMed:21483814). Specifically regulates natriuretic-peptide- dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart (PubMed:25799991). Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein (Probable). In brain, involved in cognitive function, such as learning and long-term memory (By similarity). {ECO:0000250|UniProtKB:Q8QZV1, ECO:0000269|PubMed:18757755, ECO:0000269|PubMed:21483814, ECO:0000269|PubMed:25799991, ECO:0000269|PubMed:9624146, ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in all tissues examined (testis, brain, small intestine, skeletal muscle, heart, lung, thymus, spleen, placenta, kidney, liver, pancreas, ovary and prostate) except blood (PubMed:9624146). Highest levels in brain, heart, kidney, spleen, prostate and colon. Isoform PDE9A12 is found in prostate (PubMed:12565835). In brain, present in the cortex, cerebellum, and subiculum (at protein level) (PubMed:22328573). In heart, primarily localizes to myocytes (PubMed:25799991). {ECO:0000269|PubMed:12565835, ECO:0000269|PubMed:22328573, ECO:0000269|PubMed:25799991, ECO:0000269|PubMed:9624146}.; unclassifiable (Anatomical System);cartilage;tongue;colon;fovea centralis;pancreas;prostate;whole body;lung;larynx;bone;thyroid;placenta;macula lutea;visual apparatus;iris;liver;testis;head and neck;spleen;kidney;brain; superior cervical ganglion;prostate;olfactory bulb;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.45473 0.12560 -0.462894052 23.62585515 56.76888 1.51603 PDE10A 0.998485350613982 0.00151464914483312 2.41184691946948e-10 phosphodiesterase 10A FUNCTION: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate. {ECO:0000269|PubMed:17389385}.; . TISSUE SPECIFICITY: Abundant in the putamen and caudate nucleus regions of brain and testis, moderately expressed in the thyroid gland, pituitary gland, thalamus and cerebellum.; unclassifiable (Anatomical System);lymph node;salivary gland;colon;fovea centralis;choroid;lens;skeletal muscle;retina;pancreas;optic nerve;lung;placenta;macula lutea;testis;head and neck;kidney; superior cervical ganglion;medulla oblongata;ciliary ganglion;pons;caudate nucleus;atrioventricular node;skeletal muscle; 0.32956 0.14947 -0.977252525 8.799245105 48.90667 1.36535 PDE11A 4.16725018760818e-31 4.13230761598233e-06 0.999995867692384 phosphodiesterase 11A FUNCTION: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'- GMP, respectively. {ECO:0000269|PubMed:10725373, ECO:0000269|PubMed:10906126, ECO:0000269|PubMed:11050148}.; DISEASE: Primary pigmented nodular adrenocortical disease 2 (PPNAD2) [MIM:610475]: A rare bilateral adrenal defect causing ACTH-independent Cushing syndrome. Macroscopic appearance of the adrenals is characteristic with small pigmented micronodules observed in the cortex. Adrenal glands show overall normal size and weight, and multiple small yellow-to-dark brown nodules surrounded by a cortex with a uniform appearance. Microscopically, there are moderate diffuse cortical hyperplasia with mostly nonpigmented nodules, multiple capsular deficits and massive circumscribed and infiltrating extra-adrenal cortical excrescences with micronodules. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes. {ECO:0000269|PubMed:16767104}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is present in prostate, pituitary, heart and liver. It is however not present in testis nor in penis, suggesting that weak inhibition by Tadalafil (Cialis) is not relevant (at protein level). Isoform 2 may be expressed in testis. Isoform 4 is expressed in adrenal cortex. {ECO:0000269|PubMed:10725373, ECO:0000269|PubMed:11121118, ECO:0000269|PubMed:15800651, ECO:0000269|PubMed:16079899, ECO:0000269|PubMed:16767104}.; unclassifiable (Anatomical System); superior cervical ganglion;skeletal muscle; 0.23385 0.14082 0.764222299 86.86010852 1086.94608 6.31598 PDE12 0.0235724225080969 0.962043605404927 0.0143839720869763 phosphodiesterase 12 FUNCTION: Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. This enzyme degraded triphosphorylated 2-5A to produce AMP and ATP. Also cleaves 3',5'-phosphodiester bond of oligoadenylates. Plays a role as a negative regulator of the The 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferons (IFNs). Suppression of this enzyme induces reduction of viral replication in Hela cells, thus counteracting the antiviral pathway probably by inhibiting the 2-5A system. {ECO:0000269|PubMed:15231837, ECO:0000269|PubMed:21245038, ECO:0000269|PubMed:21666256, ECO:0000269|PubMed:22285541}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15231837}.; unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;colon;parathyroid;blood;skin;retina;breast;uterus;prostate;pancreas;whole body;lung;cochlea;thyroid;liver;testis;head and neck;spleen;germinal center;kidney;brain;pineal gland;mammary gland; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.08441 0.10854 -0.179930907 40.35739561 2499.5168 9.31489 PDF 0.0503154180966918 0.689768042718933 0.259916539184375 peptide deformylase (mitochondrial) FUNCTION: Removes the formyl group from the N-terminal Met of newly synthesized proteins. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous.; unclassifiable (Anatomical System);lymph node;islets of Langerhans;adrenal cortex;colon;blood;uterus;pancreas;lung;liver;testis;germinal center;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.06879 . . . 585.09669 4.90401 PDGFA 0.858461737106681 0.139341905922522 0.00219635697079692 platelet derived growth factor subunit A FUNCTION: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFB (By similarity). {ECO:0000250}.; . . . . 0.13928 . -0.161524709 41.6430762 20.13502 0.68842 PDGFB 0.966288095427289 0.0336537081173494 5.81964553612486e-05 platelet derived growth factor subunit B FUNCTION: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFA (By similarity). {ECO:0000250}.; DISEASE: Note=A chromosomal aberration involving PDGFB is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGFB. {ECO:0000269|PubMed:12660034}.; TISSUE SPECIFICITY: Expressed at high levels in the heart, brain (sustantia nigra), placenta and fetal kidney. Expressed at moderate levels in the brain (hippocampus), skeletal muscle, kidney and lung. {ECO:0000269|PubMed:11331882}.; unclassifiable (Anatomical System);heart;ovary;hypothalamus;colon;parathyroid;uterus;pancreas;lung;endometrium;larynx;placenta;thyroid;head and neck;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21222 0.91443 -0.003562597 53.72729417 54.47502 1.47529 PDGFC 0.969061048929965 0.0308919047723497 4.7046297685146e-05 platelet derived growth factor C FUNCTION: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function. {ECO:0000269|PubMed:10806482, ECO:0000269|PubMed:10858496, ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11854040, ECO:0000269|PubMed:12032822, ECO:0000269|PubMed:15061151, ECO:0000269|PubMed:15372073, ECO:0000269|PubMed:15389578, ECO:0000269|PubMed:15728360, ECO:0000269|PubMed:15911618, ECO:0000269|PubMed:16439802, ECO:0000269|PubMed:18055825}.; . TISSUE SPECIFICITY: Expressed in the fallopian tube, vascular smooth muscle cells in kidney, breast and colon and in visceral smooth muscle of the gastrointestinal tract. Highly expressed in retinal pigment epithelia. Expressed in medulloblastoma. In the kidney, constitutively expressed in parietal epithelial cells of Bowman's capsule, tubular epithelial cells and in arterial endothelial cells (at protein level). Highly expressed in the platelets, prostate, testis and uterus. Higher expression is observed in uterine leiomyomata. Weaker expression in the spleen, thymus, heart, pancreas, liver, ovary cells and small intestine, and negligible expression in the colon and peripheral blood leukocytes. {ECO:0000269|PubMed:10806482, ECO:0000269|PubMed:11004490, ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11342471, ECO:0000269|PubMed:11854040, ECO:0000269|PubMed:12176024, ECO:0000269|PubMed:15061151, ECO:0000269|PubMed:17482170, ECO:0000269|PubMed:18055825}.; ovary;colon;parathyroid;skin;retina;uterus;prostate;cochlea;endometrium;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;hypothalamus;blood;bile duct;breast;pancreas;lung;mesenchyma;placenta;liver;hypopharynx;head and neck;cervix;kidney;stomach;thymus; dorsal root ganglion;uterus;superior cervical ganglion;fetal brain;pons;atrioventricular node;caudate nucleus;trigeminal ganglion; 0.32526 0.19184 0.038710339 56.92380278 16.87911 0.59422 PDGFD 0.0159483357606564 0.978732926555265 0.00531873768407828 platelet derived growth factor D FUNCTION: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Plays an important role in wound healing. Induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. Can initiate events that lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix (By similarity). {ECO:0000250, ECO:0000269|PubMed:11331881, ECO:0000269|PubMed:15271796}.; . TISSUE SPECIFICITY: Expressed at high levels in the heart, pancreas, adrenal gland and ovary and at low levels in placenta, liver, kidney, prostate, testis, small intestine, spleen and colon. In the kidney, expressed by the visceral epithelial cells of the glomeruli. A widespread expression is also seen in the medial smooth muscle cells of arteries and arterioles, as well as in smooth muscle cells of vasa rectae in the medullary area. Expressed in the adventitial connective tissue surrounding the suprarenal artery. In chronic obstructive nephropathy, a persistent expression is seen in glomerular visceral epithelial cells and vascular smooth muscle cells, as well as de novo expression by periglomerular interstitial cells and by some neointimal cells of atherosclerotic vessels. Expression in normal prostate is seen preferentially in the mesenchyme of the gland while expression is increased and more profuse in prostate carcinoma. Expressed in many ovarian, lung, renal and brain cancer-derived cell lines. {ECO:0000269|PubMed:11331881, ECO:0000269|PubMed:11331882, ECO:0000269|PubMed:11342471, ECO:0000269|PubMed:11980634, ECO:0000269|PubMed:12427128, ECO:0000269|PubMed:14514732, ECO:0000269|PubMed:15988036}.; unclassifiable (Anatomical System);cartilage;heart;ovary;adrenal cortex;parathyroid;skin;breast;uterus;pancreas;prostate;whole body;lung;endometrium;bone;placenta;visual apparatus;iris;testis;germinal center;kidney;brain;aorta; dorsal root ganglion;superior cervical ganglion;adipose tissue;adrenal gland;liver;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.22657 0.17212 -0.53631094 20.53550366 276.69433 3.56120 PDGFRA 0.999876729754594 0.000123270244871733 5.34267076338947e-13 platelet derived growth factor receptor alpha FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. {ECO:0000269|PubMed:10734113, ECO:0000269|PubMed:10947961, ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:12522257, ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:17141222, ECO:0000269|PubMed:20972453, ECO:0000269|PubMed:21224473, ECO:0000269|PubMed:21596750, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664, ECO:0000269|PubMed:8760137, ECO:0000269|PubMed:8943348}.; DISEASE: Note=A chromosomal aberration involving PDGFRA is found in some cases of hypereosinophilic syndrome. Interstitial chromosomal deletion del(4)(q12q12) causes the fusion of FIP1L1 and PDGFRA (FIP1L1-PDGFRA). Mutations that cause overexpression and/or constitutive activation of PDGFRA may be a cause of hypereosinophilic syndrome. {ECO:0000269|PubMed:12808148}.; DISEASE: Gastrointestinal stromal tumor (GIST) [MIM:606764]: Common mesenchymal neoplasms arising in the gastrointestinal tract, most often in the stomach. They are histologically, immunohistochemically, and genetically different from typical leiomyomas, leiomyosarcomas, and schwannomas. Most GISTs are composed of a fairly uniform population of spindle-shaped cells. Some tumors are dominated by epithelioid cells or contain a mixture of spindle and epithelioid morphologies. Primary GISTs in the gastrointestinal tract commonly metastasize in the omentum and mesenteries, often as multiple nodules. However, primary tumors may also occur outside of the gastrointestinal tract, in other intra-abdominal locations, especially in the omentum and mesentery. {ECO:0000269|PubMed:12522257, ECO:0000269|PubMed:15928335}. Note=The gene represented in this entry may be involved in disease pathogenesis. Mutations causing PDGFRA constitutive activation have been found in gastrointestinal stromal tumors lacking KIT mutations (PubMed:12522257). {ECO:0000269|PubMed:12522257}.; TISSUE SPECIFICITY: Detected in platelets (at protein level). Widely expressed. Detected in brain, fibroblasts, smooth muscle, heart, and embryo. Expressed in primary and metastatic colon tumors and in normal colon tissue. {ECO:0000269|PubMed:2536956, ECO:0000269|PubMed:7896447, ECO:0000269|PubMed:8188664}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;synovium;bone;iris;testis;brain;gall bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;spinal cord;blood;lens;skeletal muscle;pancreas;lung;mesenchyma;internal ear;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;peripheral nerve; uterus;adipose tissue; 0.96377 0.11670 -0.635637306 16.76102854 599.71226 4.95653 PDGFRB 0.998643465625158 0.00135653436729406 7.54749982205031e-12 platelet derived growth factor receptor beta FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5- trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. {ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11331881, ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:1653029, ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:1846866, ECO:0000269|PubMed:20494825, ECO:0000269|PubMed:20529858, ECO:0000269|PubMed:21098708, ECO:0000269|PubMed:21679854, ECO:0000269|PubMed:21733313, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:2835772, ECO:0000269|PubMed:2850496, ECO:0000269|PubMed:7685273, ECO:0000269|PubMed:7691811, ECO:0000269|PubMed:7692233, ECO:0000269|PubMed:8195171}.; DISEASE: Note=A chromosomal aberration involving PDGFRB is found in a form of chronic myelomonocytic leukemia (CMML). Translocation t(5;12)(q33;p13) with EVT6/TEL. It is characterized by abnormal clonal myeloid proliferation and by progression to acute myelogenous leukemia (AML).; DISEASE: Myeloproliferative disorder chronic with eosinophilia (MPE) [MIM:131440]: A hematologic disorder characterized by malignant eosinophils proliferation. Note=The gene represented in this entry may be involved in disease pathogenesis. Chromosomal aberrations involving PDGFRB have been found in many instances of chronic myeloproliferative disorder with eosinophilia. Translocation t(5;12) with ETV6 on chromosome 12 creating an PDGFRB-ETV6 fusion protein (PubMed:12181402). Translocation t(5;15)(q33;q22) with TP53BP1 creating a PDGFRB-TP53BP1 fusion protein (PubMed:15492236). Translocation t(1;5)(q23;q33) that forms a PDE4DIP-PDGFRB fusion protein (PubMed:12907457). Translocation t(5;6)(q33-34;q23) with CEP85L that fuses the 5'-end of CEP85L (isoform 4) to the 3'-end of PDGFRB (PubMed:21938754). {ECO:0000269|PubMed:12181402, ECO:0000269|PubMed:12907457, ECO:0000269|PubMed:15492236, ECO:0000269|PubMed:21938754}.; DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. Note=The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving PDGFRB has been found in a patient with AML. Translocation t(5;14)(q33;q32) with TRIP11 (PubMed:9373237). {ECO:0000269|PubMed:9373237}.; DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages. Note=The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving PDGFRB has been found in a patient with JMML. Translocation t(5;17)(q33;p11.2) with SPECC1 (PubMed:15087372). {ECO:0000269|PubMed:15087372}.; DISEASE: Basal ganglia calcification, idiopathic, 4 (IBGC4) [MIM:615007]: A form of basal ganglia calcification, an autosomal dominant condition characterized by symmetric calcification in the basal ganglia and other brain regions. Affected individuals can either be asymptomatic or show a wide spectrum of neuropsychiatric symptoms, including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis, seizures, and chronic headache. Serum levels of calcium, phosphate, alkaline phosphatase and parathyroid hormone are normal. The neuropathological hallmark of the disease is vascular and pericapillary calcification, mainly of calcium phosphate, in the affected brain areas. {ECO:0000269|PubMed:23255827}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myofibromatosis, infantile 1 (IMF1) [MIM:228550]: A rare mesenchymal disorder characterized by the development of benign tumors in the skin, striated muscles, bones, and, more rarely, visceral organs. Subcutaneous or soft tissue nodules commonly involve the skin of the head, neck, and trunk. Skeletal and muscular lesions occur in about half of the patients. Lesions may be solitary or multicentric, and they may be present at birth or become apparent in early infancy or occasionally in adult life. Visceral lesions are associated with high morbidity and mortality. {ECO:0000269|PubMed:23731537, ECO:0000269|PubMed:23731542}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;colon;substantia nigra;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;spinal cord;urinary;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; adipose tissue;atrioventricular node;trigeminal ganglion; 0.82978 0.81478 -0.716581425 14.29582449 403.35243 4.21096 PDGFRL 4.16904903414803e-10 0.0277786960684581 0.972221303514637 platelet derived growth factor receptor like . DISEASE: Note=A polymorphism in PDGFRL has been reported to be associated with susceptibility to Behcet disease (PubMed:22926996). Behcet disease is a complex multiple-system disorder characterized by recurrent oral ulcerations, recurrent genital ulcerations, typical skin lesions, and uveitis. Behcet disease also involves joints, blood vessels, musculoskeletal, neurological systems, and the gastrointestinal tract. {ECO:0000269|PubMed:22926996}.; TISSUE SPECIFICITY: Expressed in colon, lung and liver. {ECO:0000269|PubMed:7898930}.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;substantia nigra;skin;uterus;pancreas;whole body;lung;cerebral cortex;bone;thyroid;placenta;visual apparatus;testis;brain;mammary gland;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.28303 0.12624 0.181903047 66.2361406 239.47255 3.34436 PDHA1 0.99209013913194 0.00790821483430736 1.64603375247879e-06 pyruvate dehydrogenase (lipoamide) alpha 1 FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle. {ECO:0000269|PubMed:19081061, ECO:0000269|PubMed:7782287}.; DISEASE: Pyruvate dehydrogenase E1-alpha deficiency (PDHAD) [MIM:312170]: An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis. {ECO:0000269|PubMed:1293379, ECO:0000269|PubMed:1338114, ECO:0000269|PubMed:1551669, ECO:0000269|PubMed:1909401, ECO:0000269|PubMed:7545958, ECO:0000269|PubMed:7573035, ECO:0000269|PubMed:7757088, ECO:0000269|PubMed:7887409, ECO:0000269|PubMed:7967473, ECO:0000269|PubMed:8032855, ECO:0000269|PubMed:8504306, ECO:0000269|PubMed:8664900, ECO:0000269|PubMed:8844217, ECO:0000269|PubMed:9671272}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;adrenal cortex;parathyroid;skin;bile duct;prostate;whole body;lung;endometrium;bone;placenta;iris;liver;testis;spleen;cervix;kidney;brain;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;subthalamic nucleus;prefrontal cortex;globus pallidus;kidney;cingulate cortex;skeletal muscle; 0.27813 0.55950 0.170987912 65.5579146 381.13932 4.11483 PDHA1P1 . . . pyruvate dehydrogenase (lipoamide) alpha 1 pseudogene 1 . . . . . . . . . . . PDHA2 4.51589978063264e-11 0.00755750874841905 0.992442491206422 pyruvate dehydrogenase (lipoamide) alpha 2 FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle. {ECO:0000269|PubMed:16436377}.; . TISSUE SPECIFICITY: Testis. Expressed in postmeiotic spermatogenic cells. {ECO:0000269|PubMed:22750801}.; medulla oblongata;lung;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.25770 0.27498 0.332586472 73.61405992 293.71497 3.66167 PDHB 0.357305589322301 0.640067535520234 0.00262687515746472 pyruvate dehydrogenase (lipoamide) beta FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle. {ECO:0000269|PubMed:17474719, ECO:0000269|PubMed:19081061}.; DISEASE: Pyruvate dehydrogenase E1-beta deficiency (PDHBD) [MIM:614111]: An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis. {ECO:0000269|PubMed:15138885}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;umbilical cord;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach; amygdala;whole brain;thalamus;occipital lobe;subthalamic nucleus;medulla oblongata;adipose tissue;hypothalamus;prefrontal cortex;cingulate cortex;parietal lobe; 0.39283 0.44729 -0.405853867 26.23260203 16.80356 0.59065 PDHX 0.00137028838511485 0.991015255959772 0.00761445565511289 pyruvate dehydrogenase complex component X FUNCTION: Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.; DISEASE: Pyruvate dehydrogenase E3-binding protein deficiency (PDHXD) [MIM:245349]: A metabolic disorder characterized by decreased activity of the pyruvate dehydrogenase complex without observable reduction in the activities of enzymes E1, E2, or E3. Clinical features include hypotonia and psychomotor retardation. {ECO:0000269|PubMed:9399911}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;pharynx;blood;skeletal muscle;pancreas;lung;cornea;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;kidney;mammary gland;stomach;peripheral nerve; amygdala;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe; 0.04798 0.41933 0.246221394 69.56829441 2168.1326 8.57075 PDIA2 2.52932710736602e-21 1.79980515304132e-05 0.99998200194847 protein disulfide isomerase family A member 2 FUNCTION: Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins. {ECO:0000269|PubMed:19150607, ECO:0000269|PubMed:19429457}.; . TISSUE SPECIFICITY: Highly expressed in pancreas (at protein level). {ECO:0000269|PubMed:19429457, ECO:0000269|PubMed:8561901, ECO:0000269|PubMed:9115635}.; unclassifiable (Anatomical System);uterus;pancreas;optic nerve;lung;heart;islets of Langerhans;testis;spleen;brain;skin;cerebellum; pancreas;globus pallidus; 0.14665 0.10678 2.702925512 98.90304317 3052.49003 10.50276 PDIA3 0.959251419181895 0.0407447445871969 3.83623090825561e-06 protein disulfide isomerase family A member 3 . . TISSUE SPECIFICITY: Detected in the flagellum and head region of spermatozoa (at protein level). {ECO:0000269|PubMed:20400973}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;prostate;thyroid;iris;germinal center;brain;gall bladder;heart;tongue;urinary;adrenal cortex;breast;trabecular meshwork;visual apparatus;liver;spleen;mammary gland;colon;parathyroid;uterus;larynx;synovium;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;pia mater;mesenchyma;adrenal gland;nasopharynx;placenta;duodenum;amnion;head and neck;kidney;stomach; prostate;smooth muscle;lung;trachea;placenta;thyroid;beta cell islets;pituitary; 0.41087 0.44392 -0.514264485 21.41424864 58.08675 1.54160 PDIA3P1 . . . protein disulfide isomerase family A member 3 pseudogene 1 . . . . . . . . . . . PDIA3P2 . . . protein disulfide isomerase family A member 3 pseudogene 2 . . . . . . . . . . . PDIA4 0.014774296571888 0.979281641947716 0.00594406148039625 protein disulfide isomerase family A member 4 . . . smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;duodenum;head and neck;kidney;aorta;stomach;thymus; dorsal root ganglion;superior cervical ganglion;prostate;smooth muscle;lung;thyroid;placenta;liver;ciliary ganglion; 0.22699 . -0.192882212 39.25454117 447.88492 4.40188 PDIA5 1.00405592105616e-06 0.983714806765696 0.0162841891783829 protein disulfide isomerase family A member 5 . . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;aorta; fetal liver;superior cervical ganglion;liver;testis;trigeminal ganglion; 0.23723 0.13390 -0.953385901 9.206180703 310.15723 3.74607 PDIA6 0.120591091840199 0.878303134834707 0.00110577332509467 protein disulfide isomerase family A member 6 FUNCTION: May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin. {ECO:0000269|PubMed:12204115, ECO:0000269|PubMed:15466936}.; . TISSUE SPECIFICITY: Expressed in platelets (at protein level). {ECO:0000269|PubMed:15466936}.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;bile duct;pancreas;lung;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;cerebellum; adrenal gland;thyroid;placenta; 0.19770 0.09728 -0.690637458 15.12149092 2224.5543 8.69063 PDIK1L 0.381253877249055 0.60829796744857 0.0104481553023751 PDLIM1 interacting kinase 1 like . . TISSUE SPECIFICITY: Expressed in liver, kidney, pancreas, spleen, thymus and prostate. {ECO:0000269|PubMed:14631099}.; . . 0.71557 0.12534 -0.141298762 42.87567823 5.23044 0.19506 PDILT 9.26418194186399e-06 0.929534924127769 0.0704558116902896 protein disulfide isomerase-like, testis expressed FUNCTION: Probable redox-inactive chaperone involved in spermatogenesis. {ECO:0000269|PubMed:17507649}.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:15475357, ECO:0000269|PubMed:17507649}.; . . . . 0.786269343 87.29063458 2182.56553 8.61088 PDK1 0.00465668929433836 0.988879930810521 0.00646337989514047 pyruvate dehydrogenase kinase 1 FUNCTION: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Plays an important role in cellular responses to hypoxia and is important for cell proliferation under hypoxia. Protects cells against apoptosis in response to hypoxia and oxidative stress. {ECO:0000269|PubMed:17683942, ECO:0000269|PubMed:18541534, ECO:0000269|PubMed:22195962, ECO:0000269|PubMed:7499431}.; . TISSUE SPECIFICITY: Expressed predominantly in the heart. Detected at lower levels in liver, skeletal muscle and pancreas. {ECO:0000269|PubMed:7499431}.; ovary;salivary gland;intestine;colon;vein;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;skeletal muscle;breast;lung;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion; 0.28158 0.08277 -0.314027422 31.9297004 49.87193 1.38516 PDK1P1 . . . pyruvate dehydrogenase kinase 1 pseudogene 1 . . . . . . . . . . . PDK2 0.168975524516492 0.828107323159392 0.00291715232411587 pyruvate dehydrogenase kinase 2 FUNCTION: Kinase that plays a key role in the regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism. Mediates cellular responses to insulin. Plays an important role in maintaining normal blood glucose levels and in metabolic adaptation to nutrient availability. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. Plays a role in the regulation of cell proliferation and in resistance to apoptosis under oxidative stress. Plays a role in p53/TP53-mediated apoptosis. {ECO:0000269|PubMed:17222789, ECO:0000269|PubMed:19833728, ECO:0000269|PubMed:21283817, ECO:0000269|PubMed:22123926, ECO:0000269|PubMed:7499431, ECO:0000269|PubMed:9787110}.; . TISSUE SPECIFICITY: Expressed in many tissues, with the highest level in heart and skeletal muscle, intermediate levels in brain, kidney, pancreas and liver, and low levels in placenta and lung. {ECO:0000269|PubMed:7499431}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;spinal cord;muscle;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;placenta;macula lutea;hippocampus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve;cerebellum; whole brain;superior cervical ganglion;cerebellum peduncles;ciliary ganglion;pons;kidney;skeletal muscle;cerebellum; 0.09469 0.17179 -0.227663163 37.11370606 35.04029 1.06349 PDK3 0.879275520248217 0.12042352834953 0.000300951402253122 pyruvate dehydrogenase kinase 3 FUNCTION: Inhibits pyruvate dehydrogenase activity by phosphorylation of the E1 subunit PDHA1, and thereby regulates glucose metabolism and aerobic respiration. Can also phosphorylate PDHA2. Decreases glucose utilization and increases fat metabolism in response to prolonged fasting, and as adaptation to a high-fat diet. Plays a role in glucose homeostasis and in maintaining normal blood glucose levels in function of nutrient levels and under starvation. Plays a role in the generation of reactive oxygen species. {ECO:0000269|PubMed:10748134, ECO:0000269|PubMed:11486000, ECO:0000269|PubMed:15861126, ECO:0000269|PubMed:16436377, ECO:0000269|PubMed:17683942, ECO:0000269|PubMed:18718909, ECO:0000269|PubMed:22865452}.; DISEASE: Charcot-Marie-Tooth disease, X-linked dominant, 6 (CMTX6) [MIM:300905]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies characterized by severely reduced motor nerve conduction velocities (NCVs) (less than 38m/s) and segmental demyelination and remyelination, and primary peripheral axonal neuropathies characterized by normal or mildly reduced NCVs and chronic axonal degeneration and regeneration on nerve biopsy. {ECO:0000269|PubMed:23297365}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, spinal cord, as well as fetal and adult brain. {ECO:0000269|PubMed:23297365}.; . . 0.07241 0.12403 0.125076652 62.7388535 62.61684 1.61860 PDK4 4.55196606471685e-06 0.845039218713939 0.154956229319997 pyruvate dehydrogenase kinase 4 FUNCTION: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism in response to prolonged fasting and starvation. Plays an important role in maintaining normal blood glucose levels under starvation, and is involved in the insulin signaling cascade. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. In the fed state, mediates cellular responses to glucose levels and to a high-fat diet. Regulates both fatty acid oxidation and de novo fatty acid biosynthesis. Plays a role in the generation of reactive oxygen species. Protects detached epithelial cells against anoikis. Plays a role in cell proliferation via its role in regulating carbohydrate and fatty acid metabolism. {ECO:0000269|PubMed:15955060, ECO:0000269|PubMed:18658136, ECO:0000269|PubMed:21816445, ECO:0000269|PubMed:21852536}.; . TISSUE SPECIFICITY: Ubiquitous; highest levels of expression in heart and skeletal muscle. {ECO:0000269|PubMed:14966024, ECO:0000269|PubMed:21816445}.; smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;endometrium;synovium;thyroid;pituitary gland;testis;dura mater;brain;artery;bladder;gall bladder;unclassifiable (Anatomical System);amygdala;meninges;cartilage;small intestine;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;atrioventricular node;skeletal muscle; 0.21453 0.35436 0.038710339 56.92380278 125.8487 2.44283 PDLIM1 1.38008290255861e-05 0.627357723290329 0.372628475880645 PDZ and LIM domain 1 FUNCTION: Cytoskeletal protein that may act as an adapter that brings other proteins (like kinases) to the cytoskeleton.; . TISSUE SPECIFICITY: Strongly expressed in the heart and skeletal muscle, moderately expressed in the spleen, small intestine, colon, placenta, and lung. A lower level expression is seen in liver, thymus, kidney, prostate and pancreas and is not found in the brain, testis, ovary, and peripheral blood leukocytes.; . . 0.18947 0.17815 -0.315847836 31.68789809 34.82053 1.06037 PDLIM1P1 . . . PDZ and LIM domain 1 pseudogene 1 . . . . . . . . . . . PDLIM1P2 . . . PDZ and LIM domain 1 pseudogene 2 . . . . . . . . . . . PDLIM1P3 . . . PDZ and LIM domain 1 pseudogene 3 . . . . . . . . . . . PDLIM1P4 . . . PDZ and LIM domain 1 pseudogene 4 . . . . . . . . . . . PDLIM2 0.0497493108362985 0.927972251097916 0.0222784380657858 PDZ and LIM domain 2 FUNCTION: Probable adapter protein located at the actin cytoskeleton that promotes cell attachment. Necessary for the migratory capacity of epithelial cells. Overexpression enhances cell adhesion to collagen and fibronectin and suppresses anchorage independent growth. May contribute to tumor cell migratory capacity. {ECO:0000269|PubMed:15659642}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;mammary gland;stomach;cerebellum;thymus; superior cervical ganglion;placenta;skeletal muscle; 0.09001 0.18093 . . 893.46436 5.82564 PDLIM3 9.36781115533718e-08 0.170539683444839 0.829460222877049 PDZ and LIM domain 3 FUNCTION: May play a role in the organization of actin filament arrays within muscle cells. {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is highly expressed in differentiated skeletal muscle. Isoform 2 is heart-specific. {ECO:0000269|PubMed:9334352}.; myocardium;medulla oblongata;smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;atrium;optic nerve;whole body;endometrium;bone;testis;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;lens;skeletal muscle;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;macula lutea;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; uterus;superior cervical ganglion;heart;tongue;thyroid;pons;trigeminal ganglion;skeletal muscle; 0.23163 0.11095 -0.534490515 20.70063694 286.14323 3.62161 PDLIM4 0.924088701530717 0.0754676342036655 0.000443664265617348 PDZ and LIM domain 4 . . TISSUE SPECIFICITY: Isoform 2 is found in brain.; smooth muscle;ovary;foreskin;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;epidermis;islets of Langerhans;urinary;muscle;lens;lung;placenta;macula lutea;visual apparatus;mammary gland; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.24988 0.31228 0.52918614 80.81505072 1184.23756 6.52935 PDLIM5 0.0122782806115329 0.986126064153229 0.00159565523523851 PDZ and LIM domain 5 FUNCTION: May play an important role in the heart development by scaffolding PKC to the Z-disk region. May play a role in the regulation of cardiomyocyte expansion. Overexpression promotes the development of heart hypertrophy. Contributes to the regulation of dendritic spine morphogenesis in neurons. May restrain postsynaptic growth of excitatory synapses (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Heart and skeletal muscle specific. Expression is commonly increased in the brain of patients with bipolar disorder, schizophrenia, and major depression. {ECO:0000269|PubMed:10429367, ECO:0000269|PubMed:16044170, ECO:0000269|PubMed:16213469}.; myocardium;lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;amnion;head and neck;kidney;aorta;stomach; uterus;prostate;superior cervical ganglion;smooth muscle;heart;tongue;placenta;thyroid;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21242 0.85159 1.335644081 94.24982307 220.34888 3.20885 PDLIM7 0.903030194388649 0.0969352564480298 3.45491633207601e-05 PDZ and LIM domain 7 FUNCTION: May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation (e.g. embryonic flat bones mandible and cranium), and endochondral bone formation (e.g. embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway (By similarity). {ECO:0000250, ECO:0000269|PubMed:11874232, ECO:0000269|PubMed:7929196}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed ubiquitously, however, isoform 2 predominates in skeletal muscle, isoform 1 is more abundant in lung, spleen, leukocytes and fetal liver. {ECO:0000269|PubMed:11874232}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lacrimal gland;tongue;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;hippocampus;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus; uterus;superior cervical ganglion;uterus corpus;heart;skeletal muscle; 0.10514 0.12972 -0.661316159 16.02382637 560.6723 4.80957 PDP1 0.340047357623312 0.656947623190316 0.00300501918637209 pyruvate dehyrogenase phosphatase catalytic subunit 1 FUNCTION: Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex. {ECO:0000250}.; DISEASE: Pyruvate dehydrogenase phosphatase deficiency (PDP deficiency) [MIM:608782]: Results in lactic acidosis leading to neurological dysfunction. {ECO:0000269|PubMed:15855260}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;atrium;whole body;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;tongue;lens;skeletal muscle;bile duct;breast;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach;aorta; medulla oblongata;subthalamic nucleus;superior cervical ganglion;occipital lobe;temporal lobe;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;caudate nucleus;trigeminal ganglion; 0.12032 0.47482 -0.758599262 13.32861524 23.67152 0.78338 PDP2 1.86119178038611e-05 0.45419908042718 0.545782307655016 pyruvate dehyrogenase phosphatase catalytic subunit 2 FUNCTION: Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex. {ECO:0000250}.; . . unclassifiable (Anatomical System);pancreas;oesophagus;liver;kidney;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe;cerebellum; . . -0.933156985 9.54824251 36.00648 1.08197 PDPK1 0.952237847594102 0.0477339771847456 2.81752211525426e-05 3-phosphoinositide dependent protein kinase 1 FUNCTION: Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF- kappa-B activation in macrophages. Isoform 3 is catalytically inactive. {ECO:0000269|PubMed:10226025, ECO:0000269|PubMed:10480933, ECO:0000269|PubMed:10995762, ECO:0000269|PubMed:12167717, ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:14604990, ECO:0000269|PubMed:16207722, ECO:0000269|PubMed:16251192, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:17371830, ECO:0000269|PubMed:18835241, ECO:0000269|PubMed:9094314, ECO:0000269|PubMed:9445476, ECO:0000269|PubMed:9707564, ECO:0000269|PubMed:9768361}.; . TISSUE SPECIFICITY: Appears to be expressed ubiquitously. The Tyr- 9 phosphorylated form is markedly increased in diseased tissue compared with normal tissue from lung, liver, colon and breast. {ECO:0000269|PubMed:18024423}.; colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;larynx;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;hippocampus;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;medulla oblongata;cerebellum peduncles;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex;parietal lobe; 0.48981 0.25609 -0.314027422 31.9297004 11.8633 0.42959 PDPK2P . . . 3-phosphoinositide dependent protein kinase 2, pseudogene FUNCTION: Phosphorylates and activates not only PKB/AKT, but also PKA, PKC-zeta, RPS6KA1 and RPS6KB1. May play a general role in signaling processes and in development (By similarity). {ECO:0000250}.; . . . . . . . . . . PDPN 0.000983708235301868 0.813788362004386 0.185227929760312 podoplanin FUNCTION: May be involved in cell migration and/or actin cytoskeleton organization. When expressed in keratinocytes, induces changes in cell morphology with transfected cells showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion. Required for normal lung cell proliferation and alveolus formation at birth. Induces platelet aggregation. Does not have any effect on folic acid or amino acid transport. Does not function as a water channel or as a regulator of aquaporin-type water channels. {ECO:0000250|UniProtKB:Q62011, ECO:0000269|PubMed:14522983, ECO:0000269|PubMed:15231832, ECO:0000269|PubMed:15515019, ECO:0000269|PubMed:9651190}.; . TISSUE SPECIFICITY: Highly expressed in placenta, lung, skeletal muscle and brain. Weakly expressed in brain, kidney and liver. In placenta, expressed on the apical plasma membrane of endothelium. In lung, expressed in alveolar epithelium. Up-regulated in colorectal tumors and expressed in 25% of early oral squamous cell carcinomas. {ECO:0000269|PubMed:10393083, ECO:0000269|PubMed:14522983, ECO:0000269|PubMed:15515019}.; ovary;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;cochlea;cerebral cortex;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;tongue;adrenal cortex;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;appendix;pons;trigeminal ganglion;cingulate cortex; 0.55795 0.18627 0.020302773 55.60863411 25.8691 0.84202 PDPR 4.85026223543158e-08 0.989391132687971 0.0106088188094062 pyruvate dehydrogenase phosphatase regulatory subunit FUNCTION: Decreases the sensitivity of PDP1 to magnesium ions, and this inhibition is reversed by the polyamine spermine. {ECO:0000250}.; . . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;cochlea;bone;thyroid;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;skeletal muscle;breast;lung;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.11815 0.874458024 88.88888889 1513.23821 7.22888 PDR . . . pigment disorder, reticulate . . . . . . . . . . . PDRG1 0.00108693899519325 0.608381418071819 0.390531642932988 p53 and DNA damage regulated 1 FUNCTION: May play a role in chaperone-mediated protein folding. {ECO:0000305}.; . TISSUE SPECIFICITY: Predominantly expressed in normal testis and exhibits reduced but detectable expression in other organs. {ECO:0000269|PubMed:14562055}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; . 0.09986 0.11262 -0.007201372 53.19061099 6.36805 0.23871 PDS5A 0.999852920422859 0.000147079577107329 3.36333109371049e-14 PDS5 cohesin associated factor A FUNCTION: Probable regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. {ECO:0000269|PubMed:15855230, ECO:0000269|PubMed:19907496}.; . TISSUE SPECIFICITY: Highest level in colon. Low levels in lung, ovary, breast and kidney. Reduced level in renal tumor tissue. Isoform 2 is expressed in kidney. {ECO:0000269|PubMed:15019998}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;pharynx;blood;skeletal muscle;breast;bile duct;lung;epididymis;placenta;visual apparatus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.68436 0.10157 -0.688817379 15.20405756 46.97579 1.32510 PDS5B 0.99991240409457 8.75959054294456e-05 7.88456882724395e-17 PDS5 cohesin associated factor B FUNCTION: Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Plays a role in androgen-induced proliferative arrest in prostate cells. {ECO:0000269|PubMed:10963680, ECO:0000269|PubMed:15855230, ECO:0000269|PubMed:19696148}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9459187}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;testis;germinal center;brain;artery;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;small intestine;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;cerebellum peduncles;pons;atrioventricular node;skin;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.54427 0.14500 -1.484384569 3.638829913 70.24529 1.74119 PDSS1 0.263151860027171 0.736613194566945 0.000234945405884931 prenyl (decaprenyl) diphosphate synthase, subunit 1 FUNCTION: Supplies decaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone-10. {ECO:0000269|PubMed:16262699}.; DISEASE: Coenzyme Q10 deficiency, primary, 2 (COQ10D2) [MIM:614651]: An autosomal recessive multisystem disorder characterized by early-onset deafness, optic atrophy, mild mental retardation, peripheral neuropathy, obesity, livedo reticularis, and cardiac valvulopathy. {ECO:0000269|PubMed:17332895}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.51328 0.28985 0.060756528 58.52795471 205.7419 3.09959 PDSS1P1 . . . prenyl (decaprenyl) diphosphate synthase, subunit 1 pseudogene 1 . . . . . . . . . . . PDSS1P2 . . . prenyl (decaprenyl) diphosphate synthase, subunit 1 pseudogene 2 . . . . . . . . . . . PDSS2 1.89564464414184e-05 0.695884938159045 0.304096105394514 prenyl (decaprenyl) diphosphate synthase, subunit 2 FUNCTION: Supplies decaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone-10. {ECO:0000269|PubMed:16262699}.; DISEASE: Coenzyme Q10 deficiency, primary, 3 (COQ10D3) [MIM:614652]: A fatal encephalomyopathic form of coenzyme Q10 deficiency with nephrotic syndrome. Coenzyme Q10 deficiency is an autosomal recessive disorder with variable manifestations consistent with 5 major phenotypes. The phenotypes include an encephalomyopathic form with seizures and ataxia; a multisystem infantile form with encephalopathy, cardiomyopathy and renal failure; a predominantly cerebellar form with ataxia and cerebellar atrophy; Leigh syndrome with growth retardation; and an isolated myopathic form. {ECO:0000269|PubMed:17186472}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.07675 0.11464 -0.069700724 48.54328851 310.44253 3.74923 PDX1 0.522915815715109 0.460437615264296 0.0166465690205947 pancreatic and duodenal homeobox 1 FUNCTION: Activates insulin, somatostatin, glucokinase, islet amyloid polypeptide and glucose transporter type 2 gene transcription. Particularly involved in glucose-dependent regulation of insulin gene transcription. As part of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells is involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element. Binds preferentially the DNA motif 5'-[CT]TAAT[TG]-3'. During development, specifies the early pancreatic epithelium, permitting its proliferation, branching and subsequent differentiation. At adult stage, required for maintaining the hormone-producing phenotype of the beta-cell.; DISEASE: Pancreatic agenesis 1 (PAGEN1) [MIM:260370]: A disease characterized by isolated hypoplasia or agenesis of the pancreas, pancreatic beta-cell failure resulting in neonatal insulin- dependent diabetes mellitus, and exocrine pancreatic insufficiency. {ECO:0000269|PubMed:8988180}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Maturity-onset diabetes of the young 4 (MODY4) [MIM:606392]: A form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease. {ECO:0000269|PubMed:10545530, ECO:0000269|PubMed:10545531}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Duodenum and pancreas (Langerhans islet beta cells and small subsets of endocrine non-beta-cells, at low levels in acinar cells).; . . 0.18722 0.60328 . . 268.91295 3.51705 PDX1-AS1 . . . PDX1 antisense RNA 1 . . . . . . . . . . . PDXDC1 2.30260183441473e-07 0.994329920191892 0.00566984954792482 pyridoxal-dependent decarboxylase domain containing 1 . . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;testis - seminiferous tubule;testis;kidney;trigeminal ganglion; 0.32416 0.09959 1.383392355 94.62727058 619.91149 5.02449 PDXDC2P . . . pyridoxal-dependent decarboxylase domain containing 2, pseudogene . . . . . 0.17431 0.08962 . . . . PDXK 0.984648172841486 0.0153434658323419 8.36132617237517e-06 pyridoxal (pyridoxine, vitamin B6) kinase FUNCTION: Required for synthesis of pyridoxal-5-phosphate from vitamin B6.; . TISSUE SPECIFICITY: Ubiquitous. Isoform 3 is detected in adult testis and spermatozoa.; medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;synovium;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; whole brain;amygdala;occipital lobe;medulla oblongata;testis - interstitial;thalamus;temporal lobe;caudate nucleus;pons;atrioventricular node;subthalamic nucleus;lung;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.09550 0.17323 -0.314027422 31.9297004 56.05121 1.50408 PDXP 0.0427153489302202 0.66094454529997 0.29634010576981 pyridoxal phosphatase FUNCTION: Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho- tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP. {ECO:0000269|PubMed:14522954, ECO:0000269|PubMed:15580268}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in all the regions of central nerve system except the spinal cord. Also expressed at high level in liver and testis. In fetus, it is weakly expressed in all organs except brain. {ECO:0000269|PubMed:14522954, ECO:0000269|PubMed:15580268}.; lymphoreticular;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach;aorta;cerebellum;thymus; . . . . . 72.06175 1.76814 PDYN 0.000256778020981015 0.32525198594801 0.674491236031009 prodynorphin FUNCTION: Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity). {ECO:0000250}.; FUNCTION: Leumorphin has a typical opiod activity and may have anti-apoptotic effect. {ECO:0000250}.; DISEASE: Spinocerebellar ataxia 23 (SCA23) [MIM:610245]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA23 is an adult-onset autosomal dominant form characterized by slowly progressive gait and limb ataxia, with variable additional features, including peripheral neuropathy and dysarthria. {ECO:0000269|PubMed:21035104, ECO:0000269|PubMed:21712028, ECO:0000269|PubMed:23108490, ECO:0000269|PubMed:23471613}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;whole body;hippocampus;testis;brain; amygdala;medulla oblongata;caudate nucleus;pons;trigeminal ganglion; 0.12036 0.18651 0.573279816 82.08303845 66.64714 1.68355 PDZD2 0.999645170986495 0.000354829013504673 9.74943212086724e-17 PDZ domain containing 2 . . TISSUE SPECIFICITY: Isoform 2 is expressed (at protein level) in prostate and many prostate tumors. {ECO:0000269|PubMed:11289102}.; sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;bone;testis;dura mater;brain;unclassifiable (Anatomical System);amygdala;meninges;hypothalamus;lens;skeletal muscle;pia mater;lung;trabecular meshwork;placenta;macula lutea;liver;alveolus;spleen;head and neck;kidney;thymus; amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;olfactory bulb;tongue;atrioventricular node;caudate nucleus;skeletal muscle;skin;subthalamic nucleus;fetal brain;placenta;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.11498 0.16206 0.251405031 69.6685539 1979.49164 8.19886 PDZD3 3.35725944256501e-07 0.545007796968533 0.454991867305523 PDZ domain containing 3 FUNCTION: Acts as a regulatory protein that associates with GUCY2C and negatively modulates its heat-stable enterotoxin-mediated activation. Stimulates SLC9A3 activity in the presence of elevated calcium ions. {ECO:0000269|PubMed:11950846, ECO:0000269|PubMed:19088451}.; . TISSUE SPECIFICITY: Expressed in kidney and the gastrointestinal tract. Not detected in brain, heart, skeletal muscle or cells of hematopoietic origin. {ECO:0000269|PubMed:11950846}.; unclassifiable (Anatomical System);colon;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;caudate nucleus;kidney;pons;skeletal muscle; 0.13951 0.12811 -0.044015879 50.44821892 279.37841 3.58242 PDZD4 0.930873831930578 0.0690546132712939 7.15547981276119e-05 PDZ domain containing 4 . . TISSUE SPECIFICITY: Brain-specific. Expressed in fetal and adult brain. Up-regulated in synovial carcinomas. {ECO:0000269|PubMed:15077175}.; unclassifiable (Anatomical System);sympathetic chain;colon;choroid;fovea centralis;lens;retina;prostate;optic nerve;whole body;lung;frontal lobe;macula lutea;testis;brain; amygdala;whole brain;medulla oblongata;occipital lobe;cerebellum peduncles;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.46760 0.11257 -0.380166007 27.88393489 54.5917 1.47872 PDZD7 0.722769807735439 0.277105879951598 0.000124312312963372 PDZ domain containing 7 . DISEASE: Usher syndrome 2C (USH2C) [MIM:605472]: USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa with sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). USH2 is characterized by congenital mild hearing impairment with normal vestibular responses. {ECO:0000269|PubMed:20440071}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. PDZD7 mutations have been found in combination with mutations in USH2A and GPR98 in patients affected by Usher syndrome, suggesting a role as contributor to digenic Usher syndrome or a modifier of retinal disease expression. {ECO:0000269|PubMed:20440071}.; TISSUE SPECIFICITY: Weakly expressed in the inner ear. Expressed in the retinal pigment epithelium. {ECO:0000269|PubMed:19028668, ECO:0000269|PubMed:20440071}.; . . 0.24004 0.11039 -0.356299879 29.31115829 127.88087 2.46471 PDZD8 0.997263557407283 0.00273641766842631 2.49242908977427e-08 PDZ domain containing 8 FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. May inhibit herpes simplex virus 1 infection at an early stage. May promote retroviral infection. {ECO:0000269|PubMed:20573829, ECO:0000269|PubMed:21549406, ECO:0000269|PubMed:21834987}.; . . unclassifiable (Anatomical System);colon;blood;fovea centralis;choroid;lens;skin;skeletal muscle;retina;bone marrow;uterus;breast;optic nerve;lung;bone;macula lutea;liver;testis;spleen;cervix;kidney;brain;stomach; amygdala;pons; 0.51514 0.10008 0.292133603 71.59707478 403.87456 4.21682 PDZD9 0.545260624608038 0.440653844899897 0.0140855304920651 PDZ domain containing 9 . . . testis; . 0.13157 . 0.03689118 56.64071715 41.83528 1.21797 PDZD11 0.813638005471866 0.181826103197985 0.00453589133014951 PDZ domain containing 11 . . TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:12763866}.; myocardium;ovary;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;atrium;whole body;ganglion;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;brain;artery;bladder;gall bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;spinal cord;blood;lens;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; . 0.09765 0.10897 0.101211609 60.95777306 3.64814 0.13440 PDZK1 0.000134102441018778 0.637855055548786 0.362010842010195 PDZ domain containing 1 FUNCTION: A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. May be involved in the coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex with SLC9A3R1, may cluster proteins that are functionally dependent in a mutual fashion and modulate the trafficking and the activity of the associated membrane proteins. May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1. May potentiate the CFTR chloride channel activity. Required for normal cell-surface expression of SCARB1. Plays a role in maintaining normal plasma cholesterol levels via its effects on SCARB1. Plays a role in the normal localization and function of the chloride-anion exchanger SLC26A6 to the plasma membrane in the brush border of the proximal tubule of the kidney. May be involved in the regulation of proximal tubular Na(+)-dependent inorganic phosphate cotransport therefore playing an important role in tubule function (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expression is limited to epithelial cells. Expressed in the kidney (brush border of proximal tubule), pancreas, liver, and small intestine. Expressed at a lower level in the adrenal cortex, testis and stomach. Overexpressed in breast, renal and lung carcinomas. {ECO:0000269|PubMed:10496535, ECO:0000269|PubMed:11051556, ECO:0000269|PubMed:9461128}.; unclassifiable (Anatomical System);heart;ovary;colon;skin;uterus;breast;lung;endometrium;liver;testis;spleen;kidney;ciliary body; . 0.33894 0.20586 . . 244.48027 3.37323 PDZK1IP1 0.000484064755406402 0.438280407830993 0.5612355274136 PDZK1 interacting protein 1 FUNCTION: May play an important role in tumor biology.; . TISSUE SPECIFICITY: Expressed at significant levels only in a single epithelial cell population, the proximal tubular epithelial cells of the kidney. Diffusely expressed in various carcinomas originating from kidney, colon, lung and breast.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;stomach; kidney;bone marrow; 0.54064 0.25493 0.03689118 56.64071715 73.80685 1.79558 PDZK1P1 . . . PDZ domain containing 1 pseudogene 1 . . . . . . 0.07278 . . . . PDZPH1P . . . PDZ and pleckstrin homology domains 1, pseudogene . . . . . . . . . . . PDZRN3 0.908376144076894 0.0916178141294346 6.04179367107513e-06 PDZ domain containing ring finger 3 FUNCTION: E3 ubiquitin-protein ligase. Plays an important role in regulating the surface level of MUSK on myotubes. Mediates the ubiquitination of MUSK, promoting its endocytosis and lysosomal degradation. Might contribute to terminal myogenic differentiation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed, including in the heart, skeletal muscle and liver and, at lower levels, in the brain, colon, small intestine, placenta and lung. Down-regulated in ovarian serous papillary tumors. {ECO:0000269|PubMed:10470851, ECO:0000269|PubMed:15305371, ECO:0000269|PubMed:17118964}.; smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;skin;retina;uterus;prostate;whole body;endometrium;larynx;thyroid;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pineal body;pharynx;blood;skeletal muscle;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; uterus;superior cervical ganglion;adrenal gland;appendix;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.47220 0.13321 -0.990222991 8.634111819 1513.34426 7.23005 PDZRN3-AS1 . . . PDZRN3 antisense RNA 1 . . . . . . . . . . . PDZRN4 0.0708527732027404 0.929124681135585 2.25456616750135e-05 PDZ domain containing ring finger 4 . . . unclassifiable (Anatomical System);prostate;whole body;ovary;cerebral cortex;placenta;parathyroid;brain; atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12529 0.12138 1.405441678 94.77471102 4314.79074 13.07247 PEA15 0.698679171533243 0.284520680663559 0.0168001478031978 phosphoprotein enriched in astrocytes 15 FUNCTION: Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm (By similarity). Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface. {ECO:0000250, ECO:0000269|PubMed:10442631, ECO:0000269|PubMed:9670003}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Most abundant in tissues such as heart, brain, muscle and adipose tissue which utilize glucose as an energy source. Lower expression in glucose- producing tissues. Higher levels of expression are found in tissues from individuals with type 2 diabetes than in controls. {ECO:0000269|PubMed:9670003}.; lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;frontal lobe;endometrium;iris;brain;heart;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;uterus;cerebral cortex;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach; amygdala;whole brain;superior cervical ganglion;thalamus;medulla oblongata;occipital lobe;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.31714 0.24974 0.013025609 54.62962963 0.76525 0.01357 PEAK1 0.760544632953527 0.23945533958523 2.74612430347253e-08 pseudopodium enriched atypical kinase 1 FUNCTION: Tyrosine kinase that may play a role in cell spreading and migration on fibronectin. May directly or indirectly affect phosphorylation levels of cytoskeleton-associated proteins MAPK1/ERK and PXN. {ECO:0000269|PubMed:20534451}.; . . . . . . -1.293511806 5.001179523 2923.00247 10.26035 PEAR1 1.18896498529681e-14 0.685992153691757 0.314007846308231 platelet endothelial aggregation receptor 1 FUNCTION: When overexpressed, reduces the number of both early and late non-adherent myeloid progenitor cells. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in umbilical vein endothelial cells and platelets (at protein level). Expressed in heart, kidney, skeletal muscle, pancreas, ovary, breast, lung, brain cortex, hypothalamus, spinal cord, dorsal root ganglion, endothelial cells of umbilical cord artery and vein, megakaryocytes, osteoblasts, coronary muscle and erythroid cells. Weakly expressed in peripheral blood leukocytes and macrophages.; ovary;developmental;parathyroid;fovea centralis;choroid;vein;retina;uterus;optic nerve;whole body;synovium;bone;testis;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.13841 0.10328 0.677860057 84.76645435 3632.03803 11.69109 PEBP1 0.148864265050852 0.777775383071951 0.0733603518771979 phosphatidylethanolamine binding protein 1 FUNCTION: Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation. {ECO:0000250, ECO:0000269|PubMed:18294816}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;skin;retina;uterus;prostate;frontal lobe;cerebral cortex;endometrium;iris;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;islets of Langerhans;hypothalamus;spinal cord;pharynx;blood;lens;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;adrenal cortex;caudate nucleus;pons;subthalamic nucleus;adrenal gland;thyroid;prefrontal cortex;liver;globus pallidus;kidney;cingulate cortex;parietal lobe;cerebellum; 0.06882 0.28392 0.347360312 73.97381458 95.97254 2.11673 PEBP1P1 . . . phosphatidylethanolamine binding protein 1 pseudogene 1 . . . . . . . . . . . PEBP1P2 . . . phosphatidylethanolamine binding protein 1 pseudogene 2 . . . . . . . . . . . PEBP1P3 . . . phosphatidylethanolamine binding protein 1 pseudogene 3 . . . . . . . . . . . PEBP4 0.0388985351374596 0.929274715681557 0.0318267491809832 phosphatidylethanolamine binding protein 4 FUNCTION: Seems to promote cellular resistance to TNF-induced apoptosis by inhibiting activation of the Raf-1/MEK/ERK pathway, JNK and phosphatidylethanolamine externalization. {ECO:0000269|PubMed:15302887}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in tumor cells. {ECO:0000269|PubMed:15302887}.; unclassifiable (Anatomical System);myocardium;heart;cartilage;muscle;parathyroid;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;prostate;optic nerve;lung;macula lutea;testis;stomach; . . . 0.973768544 90.33970276 4637.38853 13.69638 PECAM1 . . . platelet/endothelial cell adhesion molecule 1 FUNCTION: Induces susceptibility to atherosclerosis (By similarity). Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-690 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Isoform Delta15 is unable to protect against apoptosis. Modulates BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in human umbilical cord vein cells (HUVEC). {ECO:0000250, ECO:0000269|PubMed:12110892, ECO:0000269|PubMed:19342684}.; . TISSUE SPECIFICITY: Expressed on platelets and leukocytes and is primarily concentrated at the borders between endothelial cells. Isoform Long predominates in all tissues examined. Isoform Delta12 is detected only in trachea. Isoform Delta14-15 is only detected in lung. Isoform Delta14 is detected in all tissues examined with the strongest expression in heart. Isoform Delta15 is expressed in brain, testis, ovary, cell surface of platelets, human umbilical vein endothelial cells (HUVECs), Jurkat T-cell leukemia, human erythroleukemia (HEL) and U-937 histiocytic lymphoma cell lines (at protein level). {ECO:0000269|PubMed:12433657, ECO:0000269|PubMed:19342684}.; . . 0.19477 . . . . . PECR 0.000786066276789855 0.927996690634778 0.0712172430884317 peroxisomal trans-2-enoyl-CoA reductase FUNCTION: Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity.; . . unclassifiable (Anatomical System);ovary;cartilage;islets of Langerhans;parathyroid;skin;skeletal muscle;bone marrow;lung;endometrium;placenta;visual apparatus;iris;liver;spleen;kidney;brain; dorsal root ganglion;fetal liver;superior cervical ganglion;ciliary ganglion;parietal lobe; 0.09810 0.05986 0.352813824 74.49280491 1049.47375 6.22101 PEE1 . . . preeclampsia/eclampsia 1 . . . . . . . . . . . PEF1 0.323496548949568 0.660347567158293 0.0161558838921385 penta-EF-hand domain containing 1 . . . . . 0.23919 0.13141 -0.271755481 34.31823543 67.67144 1.70192 PEG3 0.00190815720491937 0.998051947441998 3.98953530829218e-05 paternally expressed 3 FUNCTION: Induces apoptosis in cooperation with SIAH1A. Acts as a mediator between p53/TP53 and BAX in a neuronal death pathway that is activated by DNA damage. Acts synergistically with TRAF2 and inhibits TNF induced apoptosis through activation of NF-kappa-B (By similarity). Possesses a tumor suppressing activity in glioma cells. {ECO:0000250, ECO:0000269|PubMed:11260267}.; . TISSUE SPECIFICITY: Brain, glial cells, astrocytes, embryo, placenta, testis, ovary and uterus. In the placenta it is found in the layer of villous cytotrophoblast cells while in the ovary it is found in the cells of the ovarian stroma including the thecal layers around the follicles. Expression is highly repressed in glioma cell lines. {ECO:0000269|PubMed:11260267, ECO:0000269|PubMed:11331620, ECO:0000269|PubMed:9149948}.; . . . 0.20319 1.512021779 95.45293701 1640.78919 7.48748 PEG3-AS1 . . . PEG3 antisense RNA 1 . . . . . . . . . . . PEG10 0.894178858164044 0.104786510231459 0.00103463160449785 paternally expressed 10 FUNCTION: Prevents apoptosis in hepatocellular carcinoma (HCC) cells through interaction with SIAH1, a mediator of apoptosis. May also have a role in cell growth promotion and hepatoma formation. Inhibits the TGF-beta signaling by interacting with the TGF-beta receptor ALK1. When overexpressed, induces the formation of cellular extension, such as filipodia in association with ALK1. Involved at the immediate early stage of adipocyte differentiation (By similarity). May bind to the 5'-GCCTGTCTTT-3' DNA sequence of the MB1 domain in the myelin basic protein (MBP) promoter (By similarity). {ECO:0000250, ECO:0000269|PubMed:12810624, ECO:0000269|PubMed:15611116, ECO:0000269|PubMed:16423995, ECO:0000269|PubMed:17369855}.; . TISSUE SPECIFICITY: Expressed in the cytotrophoblast layer but not in the overlying syncytiotrophoblast of the placenta. Expressed in prostate and breast carcinomas but not in normal breast and prostate epithelial cells. Expressed in the Hep-G2 cell line (at protein level). Expressed in brain, liver, spleen, kidney, thymus, lung, ovary, testis, reactive lymph node, skeletal muscle, adipose tissue and placenta. Expressed in pancreatic and hepatocellular carcinomas (HCC). {ECO:0000269|PubMed:11318613, ECO:0000269|PubMed:12810624, ECO:0000269|PubMed:15611116, ECO:0000269|PubMed:16423995, ECO:0000269|PubMed:17621626}.; . . 0.70725 0.10969 -0.273576253 33.97027601 11.52995 0.41710 PEG13 . . . paternally expressed 13 . . . . . . . . . . . PELI1 0.909074231450461 0.090781621820873 0.000144146728666362 pellino E3 ubiquitin protein ligase 1 FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6. Mediates 'Lys-63'-linked polyubiquitination of IRAK1 allowing subsequent NF-kappa-B activation. {ECO:0000269|PubMed:12496252, ECO:0000269|PubMed:17675297}.; . . ovary;salivary gland;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; fetal brain;whole blood; 0.86398 0.12828 -0.494039303 22.09247464 12.44792 0.45195 PELI2 0.948506494774501 0.051459478856085 3.40263694141319e-05 pellino E3 ubiquitin protein ligase family member 2 FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6. Mediates IL1B-induced IRAK1 'Lys-63'-linked polyubiquitination and possibly 'Lys-48'-linked ubiquitination. May be important for LPS- and IL1B-induced MAP3K7- dependent, but not MAP3K3-dependent, NF-kappa-B activation. Can activate the MAP (mitogen activated protein) kinase pathway leading to activation of ELK1. {ECO:0000269|PubMed:12804775, ECO:0000269|PubMed:12860405, ECO:0000269|PubMed:17675297, ECO:0000269|PubMed:17997719, ECO:0000269|PubMed:22669975}.; . . ovary;sympathetic chain;colon;skin;bone marrow;retina;uterus;prostate;endometrium;cerebral cortex;cochlea;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;skeletal muscle;breast;lung;visual apparatus;liver;kidney;mammary gland;peripheral nerve; . 0.35205 0.11262 -0.600630256 18.06440198 97.86457 2.13884 PELI3 0.027343381963134 0.961061840763228 0.011594777273638 pellino E3 ubiquitin protein ligase family member 3 FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6. Mediates 'Lys-63'-linked polyubiquitination of IRAK1. Can activate AP1/JUN and ELK1. Not required for NF-kappa-B activation. {ECO:0000269|PubMed:12874243, ECO:0000269|PubMed:17675297}.; . TISSUE SPECIFICITY: Highly expressed in brain, heart and testis, and at lower level in kidney, liver, lung, placenta, small intestine, spleen and stomach. Isoform 1 is not expressed in lung. {ECO:0000269|PubMed:12874243}.; unclassifiable (Anatomical System);ovary;epidermis;colon;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;cerebral cortex;placenta;macula lutea;pituitary gland;testis;cervix;germinal center;kidney;brain;mammary gland;peripheral nerve;cerebellum; medulla oblongata;ciliary ganglion;atrioventricular node;parietal lobe; 0.32238 0.10913 -0.003562597 53.72729417 60.06361 1.57307 PELO 0.590624888783281 0.399485458895137 0.00988965232158178 pelota homolog (Drosophila) FUNCTION: Required for normal chromosome segregation during cell division and genomic stability (By similarity). May function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. May have ribonuclease activity (Potential). {ECO:0000250, ECO:0000305}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11060452}.; lymphoreticular;ovary;salivary gland;intestine;colon;vein;skin;uterus;prostate;whole body;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;stomach; superior cervical ganglion; 0.36580 . -0.249709319 35.74545883 38.40194 1.13932 PELP1 0.999794752493233 0.000205247283474312 2.23292833276024e-10 proline, glutamate and leucine rich protein 1 FUNCTION: Coactivator of estrogen receptor-mediated transcription and a corepressor of other nuclear hormone receptors and sequence- specific transcription factors. Plays a role in estrogen receptor (ER) genomic activity when present in the nuclear compartment by activating the ER target genes in a hormonal stimulation dependent manner. Can facilitate ER non-genomic signaling via SRC and PI3K interaction in the cytosol. Plays a role in E2-mediated cell cycle progression by interacting with RB1. May have important functional implications in ER/growth factor cross-talk. Interacts with several growth factor signaling components including EGFR and HRS. Involved in nuclear receptor signaling via its interaction with AR and NR3C1. May promote tumorigenesis via its interaction with and modulation of several oncogenes including SRC, PI3K, STAT3 and EGFR. Plays a role in cancer cell metastasis via its ability to modulate E2-mediated cytoskeleton changes and cell migration via its interaction with SRC and PI3K. Functions as the key stabilizing component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. {ECO:0000269|PubMed:11481323, ECO:0000269|PubMed:12415108, ECO:0000269|PubMed:12682072, ECO:0000269|PubMed:14963108, ECO:0000269|PubMed:15374949, ECO:0000269|PubMed:15456770, ECO:0000269|PubMed:15579769, ECO:0000269|PubMed:15994929, ECO:0000269|PubMed:16140940, ECO:0000269|PubMed:16352611, ECO:0000269|PubMed:16574651, ECO:0000269|PubMed:22872859}.; . TISSUE SPECIFICITY: Isoform 2 is expressed in breast cancer cell lines. Isoform 1 is widely expressed. {ECO:0000269|PubMed:11481323}.; . . 0.09116 0.08680 . . 780.43591 5.52623 PEMT 0.367752727517099 0.620689976471683 0.0115572960112175 phosphatidylethanolamine N-methyltransferase FUNCTION: Catalyzes three sequential methylation reactions of phosphatidylethanolamine (PE) by AdoMet, thereby producing phosphatidylcholine (PC).; . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;whole body;bone;testis;brain;unclassifiable (Anatomical System);cartilage;hypothalamus;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland; dorsal root ganglion;testis - interstitial;superior cervical ganglion;thyroid;liver;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17046 0.21736 0.839664339 88.29912715 1834.19835 7.89307 PENK 2.75735812375646e-05 0.324368396790407 0.675604029628356 proenkephalin FUNCTION: Met- and Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress. PENK(114-133) and PENK(237-258) increase glutamate release in the striatum. PENK(114-133) decreases GABA concentration in the striatum.; . . unclassifiable (Anatomical System);medulla oblongata;ovary;hypothalamus;skin;prostate;whole body;lung;frontal lobe;cochlea;larynx;thyroid;bone;visual apparatus;hippocampus;pituitary gland;testis;head and neck;brain; whole brain;medulla oblongata;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;adrenal gland;testis;caudate nucleus;pons; 0.18221 0.37518 0.308721233 72.59966973 131.78936 2.49932 PEPB . . . peptidase B . . . . . . . . . . . PEPC . . . peptidase C . . . . . . . . . . . PEPD 0.014507135033171 0.979389366665658 0.00610349830117136 peptidase D FUNCTION: Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.; DISEASE: Prolidase deficiency (PD) [MIM:170100]: A multisystem disorder associated with massive iminodipeptiduria and lack of or reduced prolidase activity in erythrocytes, leukocytes, or cultured fibroblasts. Clinical features include skin ulcers, developmental delay, recurrent infections, and a characteristic facies. {ECO:0000269|PubMed:12384772, ECO:0000269|PubMed:2365824, ECO:0000269|PubMed:8198124, ECO:0000269|PubMed:8900231}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;cerebellum; liver;kidney; 0.16621 0.49845 -0.150608082 42.28001887 2621.65254 9.59897 PEPE . . . peptidase E . . . . . . . . . . . PER1 0.875748961589664 0.124251033873624 4.53671231999872e-09 period circadian clock 1 FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time- keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. Regulates circadian target genes expression at post-transcriptional levels, but may not be required for the repression at transcriptional level. Controls PER2 protein decay. Represses CRY2 preventing its repression on CLOCK/ARNTL target genes such as FXYD5 and SCNN1A in kidney and PPARA in liver. Besides its involvement in the maintenance of the circadian clock, has an important function in the regulation of several processes. Participates in the repression of glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) by ARNTL:CLOCK. Plays a role in the modulation of the neuroinflammatory state via the regulation of inflammatory mediators release, such as CCL2 and IL6. In spinal astrocytes, negatively regulates the MAPK14/p38 and MAPK8/JNK MAPK cascades as well as the subsequent activation of NFkappaB. Coordinately regulates the expression of multiple genes that are involved in the regulation of renal sodium reabsorption. Can act as gene expression activator in a gene and tissue specific manner, in kidney enhances WNK1 and SLC12A3 expression in collaboration with CLOCK. Modulates hair follicle cycling. Represses the CLOCK- ARNTL/BMAL1 induced transcription of BHLHE40/DEC1. {ECO:0000269|PubMed:24005054}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in hair follicles (at protein level).Found in heart, brain, placenta, lung, liver, skeletal muscle, pancreas, kidney, spleen, thymus, prostate, testis, ovary and small intestine. Highest level in skeletal muscle. {ECO:0000269|PubMed:14750904, ECO:0000269|PubMed:24005054, ECO:0000269|PubMed:9333243, ECO:0000269|PubMed:9427249}.; myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;olfactory bulb;thyroid;adrenal cortex;ciliary ganglion;fetal lung;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.81937 0.22945 -1.889004548 1.981599434 289.79879 3.64159 PER2 0.933004687040542 0.0669953084123656 4.54709288216099e-09 period circadian clock 2 FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time- keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndrome and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock-controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK- ARTNL/BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK-ARTNL/BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like ARNTL or G6PC. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby inhibiting transcriptional activation. Required for fatty acid and lipid metabolism, is involved as well in the regulation of circulating insulin levels. Plays an important role in the maintenance of cardiovascular functions through the regulation of NO and vasodilatatory prostaglandins production in aortas. Controls circadian glutamate uptake in synaptic vesicles through the regulation of VGLUT1 expression. May also be involved in the regulation of inflammatory processes. Represses the CLOCK- ARNTL/BMAL1 induced transcription of BHLHE40/DEC1 and ATF4. Negatively regulates the formation of the TIMELESS-CRY1 complex by competing with TIMELESS for binding to CRY1. {ECO:0000250|UniProtKB:O54943}.; DISEASE: Advanced sleep phase syndrome, familial, 1 (FASPS1) [MIM:604348]: A disorder characterized by very early sleep onset and offset. Individuals are 'morning larks' with a 4 hours advance of the sleep, temperature and melatonin rhythms. {ECO:0000269|PubMed:11232563}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Found in heart, brain, placenta, lung, liver, skeleatal muscle, kidney and pancreas. High levels in skeletal muscle and pancreas. Low levels in lung. Isoform 2 is expressed in keratinocytes (at protein level). {ECO:0000269|PubMed:9427249}.; ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;prostate;optic nerve;frontal lobe;larynx;bone;testis;brain;gall bladder;unclassifiable (Anatomical System);cartilage;hypothalamus;blood;lens;skeletal muscle;breast;lung;epididymis;placenta;macula lutea;liver;head and neck;kidney;stomach;aorta; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.79725 0.24438 -1.17964842 5.921207832 855.54157 5.71082 PER3 2.19067741322434e-10 0.991571710420348 0.0084282893605847 period circadian clock 3 FUNCTION: Originally described as a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1, NR1D2, RORA, RORB and RORG, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. Has a redundant role with the other PER proteins PER1 and PER2 and is not essential for the circadian rhythms maintenance. In contrast, plays an important role in sleep-wake timing and sleep homeostasis probably through the transcriptional regulation of sleep homeostasis-related genes, without influencing circadian parameters. Can bind heme. {ECO:0000269|PubMed:17346965, ECO:0000269|PubMed:19716732, ECO:0000269|PubMed:24439663, ECO:0000269|PubMed:24577121}.; . . ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;artery;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pineal body;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.17974 . 1.352134556 94.35598018 722.42393 5.33625 PERM1 . . . PPARGC1 and ESRR induced regulator, muscle 1 FUNCTION: Regulates the expression of selective PPARGC1A/B and ESRRA/B/G target genes with roles in glucose and lipid metabolism, energy transfer, contractile function, muscle mitochondrial biogenesis and oxidative capacity. Required for the efficient induction of MT-CO2, MT-CO3, COX4I1, TFB1M, TFB2M, POLRMT and SIRT3 by PPARGC1A. Positively regulates the PPARGC1A/ESRRG-induced expression of CKMT2, TNNI3 and SLC2A4 and negatively regulates the PPARGC1A/ESRRG-induced expression of PDK4. {ECO:0000250|UniProtKB:Q149B8}.; . TISSUE SPECIFICITY: Muscle-specific expression is increased by endurance exercise. {ECO:0000269|PubMed:23836911}.; . . 0.06703 . . . . . PERP 0.141632278773961 0.779214092475848 0.0791536287501917 PERP, TP53 apoptosis effector FUNCTION: Component of intercellular desmosome junctions. Plays a role in stratified epithelial integrity and cell-cell adhesion by promoting desmosome assembly. Plays a role as an effector in the TP53-dependent apoptotic pathway (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in skin, heart, placental, liver, pancreas, keratinocytes and dermal fibroblasts. {ECO:0000269|PubMed:12752121}.; myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;amniotic fluid;bladder;brain;tonsil;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;oral cavity;bile duct;pancreas;lung;pia mater;placenta;hypopharynx;head and neck;kidney;stomach; prostate;lung;trachea;tongue;placenta;skin; 0.21969 0.15126 0.571462851 81.99457419 89.9839 2.04182 PES1 0.655113488767418 0.344876524343148 9.9868894335893e-06 pescadillo ribosomal biogenesis factor 1 FUNCTION: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. {ECO:0000255|HAMAP-Rule:MF_03028, ECO:0000269|PubMed:16738141, ECO:0000269|PubMed:17189298, ECO:0000269|PubMed:17353269}.; . TISSUE SPECIFICITY: Significant levels are detected in a variety of cancer cell lines, including glioblastoma, breast carcinoma, colon carcinoma and cervical carcinoma cells. Levels are abnormally elevated in malignant tumors of astrocytic origin.; lymphoreticular;ovary;salivary gland;sympathetic chain;intestine;colon;skin;bone marrow;retina;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;synovium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;mesenchyma;adrenal gland;placenta;visual apparatus;liver;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach; whole brain;lung;tumor;testis;ciliary ganglion;white blood cells; 0.58292 0.87725 -0.130380821 44.03161123 879.96424 5.77582 PES1P1 . . . pescadillo ribosomal biogenesis factor 1 pseudogene 1 . . . . . . . . . . . PES1P2 . . . pescadillo ribosomal biogenesis factor 1 pseudogene 2 . . . . . . . . . . . PET100 . . . PET100 homolog . . . . . . . 0.633974434 83.58693088 178.29168 2.90283 PET117 . . . PET117 homolog . . . . . . . 0.167351552 65.04482189 34.46737 1.05273 PEX1 3.96976240276807e-05 0.999959587322532 7.15053440067359e-07 peroxisomal biogenesis factor 1 FUNCTION: Required for stability of PEX5 and protein import into the peroxisome matrix. Anchored by PEX26 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes.; DISEASE: Peroxisome biogenesis disorder complementation group 1 (PBD-CG1) [MIM:214100]: A peroxisomal disorder arising from a failure of protein import into the peroxisomal membrane or matrix. The peroxisome biogenesis disorders (PBD group) are genetically heterogeneous with at least 14 distinct genetic groups as concluded from complementation studies. Include disorders are: Zellweger syndrome (ZWS), neonatal adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and IRD are distinct from RCDP and constitute a clinical continuum of overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS). {ECO:0000269|PubMed:19105186, ECO:0000269|PubMed:26387595}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 1A (PBD1A) [MIM:214100]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum. PBD1A is an autosomal recessive systemic disorder characterized clinically by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life. {ECO:0000269|PubMed:9398847, ECO:0000269|PubMed:9398848, ECO:0000269|PubMed:9539740}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 1B (PBD1B) [MIM:601539]: A peroxisome biogenesis disorder that includes neonatal adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two milder manifestations of the Zellweger disease spectrum. The clinical course of patients with the NALD and IRD presentation is variable and may include developmental delay, hypotonia, liver dysfunction, sensorineural hearing loss, retinal dystrophy and vision impairment. Children with the NALD presentation may reach their teens, while patients with the IRD presentation may reach adulthood. The clinical conditions are often slowly progressive in particular with respect to loss of hearing and vision. The biochemical abnormalities include accumulation of phytanic acid, very long chain fatty acids (VLCFA), di- and trihydroxycholestanoic acid and pipecolic acid. {ECO:0000269|PubMed:11439091, ECO:0000269|PubMed:9398847, ECO:0000269|PubMed:9539740}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;skin;uterus;prostate;whole body;endometrium;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;urinary;skeletal muscle;breast;lung;adrenal gland;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion; 0.57125 . -0.189246284 39.30761972 268.3796 3.51356 PEX2 0.0555564811475487 0.865216285217355 0.0792272336350965 peroxisomal biogenesis factor 2 FUNCTION: Somewhat implicated in the biogenesis of peroxisomes.; DISEASE: Peroxisome biogenesis disorder complementation group 5 (PBD-CG5) [MIM:614866]: A peroxisomal disorder arising from a failure of protein import into the peroxisomal membrane or matrix. The peroxisome biogenesis disorders (PBD group) are genetically heterogeneous with at least 14 distinct genetic groups as concluded from complementation studies. Include disorders are: Zellweger syndrome (ZWS), neonatal adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and IRD are distinct from RCDP and constitute a clinical continuum of overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS). Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 5A (PBD5A) [MIM:614866]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and clinically characterized by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life. {ECO:0000269|PubMed:1546315}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 5B (PBD5B) [MIM:614867]: A peroxisome biogenesis disorder that includes neonatal adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two milder manifestations of the Zellweger disease spectrum. The clinical course of patients with the NALD and IRD presentation is variable and may include developmental delay, hypotonia, liver dysfunction, sensorineural hearing loss, retinal dystrophy and vision impairment. Children with the NALD presentation may reach their teens, while patients with the IRD presentation may reach adulthood. The clinical conditions are often slowly progressive in particular with respect to loss of hearing and vision. The biochemical abnormalities include accumulation of phytanic acid, very long chain fatty acids (VLCFA), di- and trihydroxycholestanoic acid and pipecolic acid. {ECO:0000269|PubMed:10528859}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;developmental;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;kidney;mammary gland;stomach; superior cervical ganglion;pons;parietal lobe; 0.13400 0.24586 0.395088462 76.15003539 221.16802 3.21676 PEX3 0.00276137425966162 0.994431014623115 0.00280761111722353 peroxisomal biogenesis factor 3 FUNCTION: Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes. {ECO:0000269|PubMed:10848631, ECO:0000269|PubMed:15007061}.; DISEASE: Peroxisome biogenesis disorder 10A (PBD10A) [MIM:614882]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and clinically characterized by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life. {ECO:0000269|PubMed:10848631, ECO:0000269|PubMed:10958759}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in all examined tissues.; lymphoreticular;parathyroid;skin;uterus;prostate;endometrium;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;pineal body;blood;skeletal muscle;breast;pancreas;lung;visual apparatus;liver;spleen;kidney;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.33128 0.24909 -0.073340031 48.11866006 227.25778 3.25746 PEX5 0.401174868136947 0.598809463847609 1.56680154442132e-05 peroxisomal biogenesis factor 5 FUNCTION: Binds to the C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) and plays an essential role in peroxisomal protein import. {ECO:0000269|PubMed:7706321, ECO:0000269|PubMed:7719337, ECO:0000269|PubMed:7790377}.; DISEASE: Peroxisome biogenesis disorder 2A (PBD2A) [MIM:214110]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and characterized clinically by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life. {ECO:0000269|PubMed:7719337}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 2B (PBD2B) [MIM:202370]: A peroxisome biogenesis disorder that includes neonatal adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two milder manifestations of the Zellweger disease spectrum. The clinical course of patients with the NALD and IRD presentation is variable and may include developmental delay, hypotonia, liver dysfunction, sensorineural hearing loss, retinal dystrophy and vision impairment. Children with the NALD presentation may reach their teens, while patients with the IRD presentation may reach adulthood. The clinical conditions are often slowly progressive in particular with respect to loss of hearing and vision. The biochemical abnormalities include accumulation of phytanic acid, very long chain fatty acids (VLCFA), di- and trihydroxycholestanoic acid and pipecolic acid. {ECO:0000269|PubMed:10462504, ECO:0000269|PubMed:7719337}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:7706321, ECO:0000269|PubMed:7719337, ECO:0000269|PubMed:7790377}.; myocardium;medulla oblongata;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;larynx;thyroid;bone;iris;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;skeletal muscle;lung;hippocampus;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus; testis - interstitial;temporal lobe;testis;atrioventricular node;pons;parietal lobe; 0.51929 0.32146 -0.841329384 11.36470866 232.4519 3.29714 PEX5L 0.664004906251205 0.335985902061358 9.19168743696048e-06 peroxisomal biogenesis factor 5-like FUNCTION: Accessory subunit of hyperpolarization-activated cyclic nucleotide-gated (HCN) channels, regulating their cell-surface expression and cyclic nucleotide dependence. {ECO:0000250}.; . TISSUE SPECIFICITY: Mainly expressed in brain. Also expressed in pancreas, testis and pituitary. {ECO:0000269|PubMed:11463335}.; unclassifiable (Anatomical System);ovary;cerebellum cortex;islets of Langerhans;parathyroid;lens;skeletal muscle;whole body;lung;frontal lobe;cochlea;placenta;visual apparatus;testis;brain; superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15812 0.14485 -0.977252525 8.799245105 84.62819 1.95911 PEX5L-AS1 . . . PEX5L antisense RNA 1 . . . . . . . . . . . PEX5L-AS2 . . . PEX5L antisense RNA 2 . . . . . . . . . . . PEX6 0.00284958751998099 0.996604492304388 0.000545920175630553 peroxisomal biogenesis factor 6 FUNCTION: Involved in peroxisome biosynthesis. Required for stability of the PTS1 receptor. Anchored by PEX26 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes.; DISEASE: Peroxisome biogenesis disorder complementation group 4 (PBD-CG4) [MIM:614862]: A peroxisomal disorder arising from a failure of protein import into the peroxisomal membrane or matrix. The peroxisome biogenesis disorders (PBD group) are genetically heterogeneous with at least 14 distinct genetic groups as concluded from complementation studies. Include disorders are: Zellweger syndrome (ZWS), neonatal adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and IRD are distinct from RCDP and constitute a clinical continuum of overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS). {ECO:0000269|PubMed:19105186, ECO:0000269|PubMed:26387595}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 4A (PBD4A) [MIM:614862]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and clinically characterized by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life. {ECO:0000269|PubMed:10408779, ECO:0000269|PubMed:8670792}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 4B (PBD4B) [MIM:614863]: A peroxisome biogenesis disorder that includes neonatal adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two milder manifestations of the Zellweger disease spectrum. The clinical course of patients with the NALD and IRD presentation is variable and may include developmental delay, hypotonia, liver dysfunction, sensorineural hearing loss, retinal dystrophy and vision impairment. Children with the NALD presentation may reach their teens, while patients with the IRD presentation may reach adulthood. The clinical conditions are often slowly progressive in particular with respect to loss of hearing and vision. The biochemical abnormalities include accumulation of phytanic acid, very long chain fatty acids (VLCFA), di- and trihydroxycholestanoic acid and pipecolic acid. {ECO:0000269|PubMed:11355018}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;cerebellum; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.36559 0.20606 1.139030387 92.34489266 3202.08558 10.78604 PEX7 6.86128307466037e-08 0.260872575902808 0.739127355484362 peroxisomal biogenesis factor 7 FUNCTION: Binds to the N-terminal PTS2-type peroxisomal targeting signal and plays an essential role in peroxisomal protein import.; DISEASE: Rhizomelic chondrodysplasia punctata 1 (RCDP1) [MIM:215100]: A peroxisome biogenesis disorder. It is characterized by rhizomelic shortening of femur and humerus, vertebral disorders, cataract, cutaneous lesions and severe mental retardation. {ECO:0000269|PubMed:9090381}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 9B (PBD9B) [MIM:614879]: A peroxisome biogenesis disorder with unusually mild clinical and biochemical manifestations. Affected individuals manifest a variable phenotype similar to, and in some cases indistinguishable from, classic Refsum disease. Variable features include ocular abnormalities, sensorimotor neuropathy, ichthyosis, deafness, chondrodysplasia punctata without rhizomelia or growth failure. {ECO:0000269|PubMed:12522768}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Highest expression in pancreas, skeletal muscle and heart.; unclassifiable (Anatomical System);heart;tongue;hypothalamus;colon;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;endometrium;bone;placenta;macula lutea;liver;testis;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;testis;pons;atrioventricular node;trigeminal ganglion;parietal lobe; 0.11254 0.19973 0.014844891 54.94810097 28.2424 0.90611 PEX10 0.010463632475946 0.945302377621403 0.0442339899026509 peroxisomal biogenesis factor 10 FUNCTION: Somewhat implicated in the biogenesis of peroxisomes.; DISEASE: Peroxisome biogenesis disorder complementation group 7 (PBD-CG7) [MIM:614870]: A peroxisomal disorder arising from a failure of protein import into the peroxisomal membrane or matrix. The peroxisome biogenesis disorders (PBD group) are genetically heterogeneous with at least 14 distinct genetic groups as concluded from complementation studies. Include disorders are: Zellweger syndrome (ZWS), neonatal adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and IRD are distinct from RCDP and constitute a clinical continuum of overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS). {ECO:0000269|PubMed:19105186}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 6A (PBD6A) [MIM:614870]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and clinically characterized by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life. {ECO:0000269|PubMed:9700193}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 6B (PBD6B) [MIM:614871]: A peroxisome biogenesis disorder that includes neonatal adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two milder manifestations of the Zellweger disease spectrum. The clinical course of patients with the NALD and IRD presentation is variable and may include developmental delay, hypotonia, liver dysfunction, sensorineural hearing loss, retinal dystrophy and vision impairment. Children with the NALD presentation may reach their teens, while patients with the IRD presentation may reach adulthood. The clinical conditions are often slowly progressive in particular with respect to loss of hearing and vision. The biochemical abnormalities include accumulation of phytanic acid, very long chain fatty acids (VLCFA), di- and trihydroxycholestanoic acid and pipecolic acid. {ECO:0000269|PubMed:9683594}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pineal body;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; . 0.10434 0.16529 -0.26629572 34.81953291 144.47811 2.61859 PEX11A 5.93762026210222e-07 0.138534341151217 0.861465065086756 peroxisomal biogenesis factor 11 alpha FUNCTION: May be involved in peroxisomal proliferation and may regulate peroxisomes division (PubMed:9792670). May mediate binding of coatomer proteins to the peroxisomal membrane (By similarity). Promotes membrane protrusion and elongation on the peroxisomal surface (PubMed:20826455). {ECO:0000250|UniProtKB:O70597, ECO:0000269|PubMed:20826455, ECO:0000269|PubMed:9792670}.; . . unclassifiable (Anatomical System);heart;ovary;colon;skin;breast;uterus;whole body;lung;placenta;liver;testis;spleen;cervix;kidney;brain;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07097 0.13030 -0.449946534 24.00330267 23.39176 0.78019 PEX11B 0.000510737313623795 0.882472219910926 0.11701704277545 peroxisomal biogenesis factor 11 beta FUNCTION: Involved in peroxisomal proliferation (PubMed:9792670). May regulate peroxisome division by recruiting the dynamin-related GTPase DNM1L to the peroxisomal membrane (PubMed:12618434). Promotes membrane protrusion and elongation on the peroxisomal surface (PubMed:20826455). {ECO:0000269|PubMed:12618434, ECO:0000269|PubMed:20826455, ECO:0000269|PubMed:9792670}.; DISEASE: Peroxisome biogenesis disorder 14B (PBD14B) [MIM:614920]: An autosomal recessive peroxisome biogenesis disorder characterized clinically by mild intellectual disability, congenital cataracts, progressive hearing loss, and polyneuropathy. Additionally, recurrent migraine-like episodes following mental stress or physical exertion, not a common feature in peroxisome disorders, are observed. {ECO:0000269|PubMed:22581968}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.35026 0.19130 -0.273576253 33.97027601 30.48442 0.97143 PEX11G 0.000252773182205477 0.533586328056842 0.466160898760953 peroxisomal biogenesis factor 11 gamma FUNCTION: Promotes membrane protrusion and elongation on the peroxisomal surface. {ECO:0000269|PubMed:20826455}.; . . unclassifiable (Anatomical System);pancreas;lung;placenta;liver;colon;spleen;brain;stomach; liver;ciliary ganglion; 0.05996 0.10651 0.327131069 73.27199811 231.16822 3.28671 PEX12 3.69624709128407e-12 0.00642094319241608 0.993579056803888 peroxisomal biogenesis factor 12 FUNCTION: Required for protein import into peroxisomes. {ECO:0000269|PubMed:9632816}.; DISEASE: Peroxisome biogenesis disorder complementation group 3 (PBD-CG3) [MIM:614859]: A peroxisomal disorder arising from a failure of protein import into the peroxisomal membrane or matrix. The peroxisome biogenesis disorders (PBD group) are genetically heterogeneous with at least 14 distinct genetic groups as concluded from complementation studies. Include disorders are: Zellweger syndrome (ZWS), neonatal adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and IRD are distinct from RCDP and constitute a clinical continuum of overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS). {ECO:0000269|PubMed:19105186}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 3A (PBD3A) [MIM:614859]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and clinically characterized by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life. {ECO:0000269|PubMed:9090384}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 3B (PBD3B) [MIM:266510]: A peroxisome biogenesis disorder that includes neonatal adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two milder manifestations of the Zellweger disease spectrum. The clinical course of patients with the NALD and IRD presentation is variable and may include developmental delay, hypotonia, liver dysfunction, sensorineural hearing loss, retinal dystrophy and vision impairment. Children with the NALD presentation may reach their teens, while patients with the IRD presentation may reach adulthood. The clinical conditions are often slowly progressive in particular with respect to loss of hearing and vision. The biochemical abnormalities include accumulation of phytanic acid, very long chain fatty acids (VLCFA), di- and trihydroxycholestanoic acid and pipecolic acid. Note=The disease is caused by mutations affecting the gene represented in this entry. {ECO:0000269|PubMed:10562279, ECO:0000269|PubMed:19105186}.; . unclassifiable (Anatomical System);lymph node;ovary;adrenal cortex;parathyroid;skin;skeletal muscle;prostate;lung;frontal lobe;cochlea;mesenchyma;bone;thyroid;placenta;hypopharynx;liver;testis;head and neck;cervix;kidney;brain;mammary gland;aorta; superior cervical ganglion;spinal cord;trigeminal ganglion;skeletal muscle; 0.25086 0.17732 0.527368849 80.73248408 203.40006 3.07833 PEX12P1 . . . peroxisomal biogenesis factor 12 pseudogene 1 . . . . . . . . . . . PEX13 0.0231397187071568 0.912652714853822 0.0642075664390212 peroxisomal biogenesis factor 13 FUNCTION: Component of the peroxisomal translocation machinery with PEX14 and PEX17. Functions as a docking factor for the predominantly cytoplasmic PTS1 receptor (PAS10/PEX5). Involved in the import of PTS1 and PTS2 proteins.; DISEASE: Peroxisome biogenesis disorder complementation group 13 (PBD-CG13) [MIM:614883]: A peroxisomal disorder arising from a failure of protein import into the peroxisomal membrane or matrix. The peroxisome biogenesis disorders (PBD group) are genetically heterogeneous with at least 14 distinct genetic groups as concluded from complementation studies. Include disorders are: Zellweger syndrome (ZWS), neonatal adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and IRD are distinct from RCDP and constitute a clinical continuum of overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS). {ECO:0000269|PubMed:10332040, ECO:0000269|PubMed:19449432}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 11A (PBD11A) [MIM:614883]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and clinically characterized by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life. {ECO:0000269|PubMed:10332040, ECO:0000269|PubMed:19449432}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 11B (PBD11B) [MIM:614885]: A peroxisome biogenesis disorder that includes neonatal adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two milder manifestations of the Zellweger disease spectrum. The clinical course of patients with the NALD and IRD presentation is variable and may include developmental delay, hypotonia, liver dysfunction, sensorineural hearing loss, retinal dystrophy and vision impairment. Children with the NALD presentation may reach their teens, while patients with the IRD presentation may reach adulthood. The clinical conditions are often slowly progressive in particular with respect to loss of hearing and vision. The biochemical abnormalities include accumulation of phytanic acid, very long chain fatty acids (VLCFA), di- and trihydroxycholestanoic acid and pipecolic acid. {ECO:0000269|PubMed:10332040, ECO:0000269|PubMed:10441568}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;heart;vein;skin;skeletal muscle;breast;uterus;bile duct;pancreas;lung;endometrium;bone;placenta;visual apparatus;hippocampus;duodenum;liver;testis;spleen;germinal center;kidney;bladder;aorta;stomach; superior cervical ganglion;testis - interstitial;testis;skeletal muscle; 0.20714 0.21613 0.373041938 75.29488087 139.19176 2.57218 PEX14 0.634568377657546 0.365138188765138 0.000293433577315348 peroxisomal biogenesis factor 14 FUNCTION: Peroxisome membrane protein that is an essential component of the peroxisomal import machinery. Functions as a docking factor for the predominantly cytoplasmic PTS1 receptor (PEX5). Plays a key role for peroxisome movement through a direct interaction with tubulin. {ECO:0000269|PubMed:21525035, ECO:0000269|PubMed:9653144}.; DISEASE: Peroxisome biogenesis disorder complementation group K (PBD-CGK) [MIM:614887]: A peroxisomal disorder arising from a failure of protein import into the peroxisomal membrane or matrix. The peroxisome biogenesis disorders (PBD group) are genetically heterogeneous with at least 14 distinct genetic groups as concluded from complementation studies. Include disorders are: Zellweger syndrome (ZWS), neonatal adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and IRD are distinct from RCDP and constitute a clinical continuum of overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS). {ECO:0000269|PubMed:15146459}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 13A (PBD13A) [MIM:614887]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and clinically characterized by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life. {ECO:0000269|PubMed:15146459}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.23292 0.21670 -0.488577883 22.64685067 405.18413 4.22034 PEX16 0.00174660780249164 0.972862496625636 0.0253908955718727 peroxisomal biogenesis factor 16 FUNCTION: Required for peroxisome membrane biogenesis. May play a role in early stages of peroxisome assembly. Can recruit other peroxisomal proteins, such as PEX3 and PMP34, to de novo peroxisomes derived from the endoplasmic reticulum (ER). May function as receptor for PEX3. {ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:12223482, ECO:0000269|PubMed:16717127}.; DISEASE: Peroxisome biogenesis disorder complementation group 9 (PBD-CG9) [MIM:614876]: A peroxisomal disorder arising from a failure of protein import into the peroxisomal membrane or matrix. The peroxisome biogenesis disorders (PBD group) are genetically heterogeneous with at least 14 distinct genetic groups as concluded from complementation studies. Include disorders are: Zellweger syndrome (ZWS), neonatal adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and IRD are distinct from RCDP and constitute a clinical continuum of overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS). {ECO:0000269|PubMed:9837814}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 8A (PBD8A) [MIM:614876]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and clinically characterized by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life. {ECO:0000269|PubMed:9837814}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 8B (PBD8B) [MIM:614877]: A relatively mild peroxisome biogenesis disorder. Affected individuals manifest lower limb spasticity and ataxia resulting in wheelchair dependence. Other features include optic atrophy, cataracts, dysarthria, dysphagia, constipation, and a peripheral demyelinating motor and sensory neuropathy. Cognition is relatively preserved. Biochemical abnormalities are mild and include increased very-long-chain fatty acids (VLCFA), increased bile acid intermediates, and increased branched chain fatty acids. Phytanic acid alpha-oxidation, pristanic acid beta-oxidation, and red cell plasmalogen are normal. {ECO:0000269|PubMed:20647552}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);medulla oblongata;ovary;islets of Langerhans;colon;fovea centralis;choroid;lens;skin;retina;pancreas;prostate;optic nerve;lung;placenta;macula lutea;liver;spleen;kidney;brain;mammary gland;stomach;thymus; dorsal root ganglion;whole brain;superior cervical ganglion;liver;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe; 0.07692 0.19429 0.262810045 70.43524416 256.14052 3.44234 PEX19 0.0429221720976364 0.929434239787813 0.0276435881145506 peroxisomal biogenesis factor 19 FUNCTION: Necessary for early peroxisomal biogenesis. Acts both as a cytosolic chaperone and as an import receptor for peroxisomal membrane proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the cytoplasm by interacting with their hydrophobic membrane-spanning domains, and targets them to the peroxisome membrane by binding to the integral membrane protein PEX3. Excludes CDKN2A from the nucleus and prevents its interaction with MDM2, which results in active degradation of TP53. {ECO:0000269|PubMed:10051604, ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:11259404, ECO:0000269|PubMed:11883941, ECO:0000269|PubMed:14709540, ECO:0000269|PubMed:15007061}.; DISEASE: Peroxisome biogenesis disorder 12A (PBD12A) [MIM:614886]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and clinically characterized by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life. {ECO:0000269|PubMed:10051604}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 1 is strongly predominant in all tissues except in utero where isoform 2 is the main form. {ECO:0000269|PubMed:9339377}.; . . 0.33324 0.25510 -0.247889024 35.98726115 13.3395 0.48485 PEX26 0.43597330189852 0.557070917355256 0.00695578074622399 peroxisomal biogenesis factor 26 FUNCTION: Probably required for protein import into peroxisomes. Anchors PEX1 and PEX6 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes. Involved in the import of catalase and proteins containing a PTS2 target sequence, but not in import of proteins with a PTS1 target sequence. {ECO:0000269|PubMed:12717447, ECO:0000269|PubMed:12851857}.; DISEASE: Peroxisome biogenesis disorder 7A (PBD7A) [MIM:614872]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and clinically characterized by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life. {ECO:0000269|PubMed:12851857}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peroxisome biogenesis disorder 7B (PBD7B) [MIM:614873]: A peroxisome biogenesis disorder that includes neonatal adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two milder manifestations of the Zellweger disease spectrum. The clinical course of patients with the NALD and IRD presentation is variable and may include developmental delay, hypotonia, liver dysfunction, sensorineural hearing loss, retinal dystrophy and vision impairment. Children with the NALD presentation may reach their teens, while patients with the IRD presentation may reach adulthood. The clinical conditions are often slowly progressive in particular with respect to loss of hearing and vision. The biochemical abnormalities include accumulation of phytanic acid, very long chain fatty acids (VLCFA), di- and trihydroxycholestanoic acid and pipecolic acid. {ECO:0000269|PubMed:12717447, ECO:0000269|PubMed:12851857}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney, liver, brain and skeletal muscles. Expressed at intermediate level in pancreas, placenta and heart. Weakly expressed in lung. {ECO:0000269|PubMed:12851857}.; unclassifiable (Anatomical System);heart;islets of Langerhans;colon;blood;skin;skeletal muscle;bone marrow;breast;uterus;prostate;whole body;lung;bone;visual apparatus;hypopharynx;liver;testis;cervix;head and neck;spleen;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;temporal lobe;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex; 0.04881 . 1.126294249 92.16206653 66.90477 1.68945 PF4 0.0332968172086843 0.613399998245726 0.35330318454559 platelet factor 4 FUNCTION: Released during platelet aggregation. Neutralizes the anticoagulant effect of heparin because it binds more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Chemotactic for neutrophils and monocytes. Inhibits endothelial cell proliferation, the short form is a more potent inhibitor than the longer form. {ECO:0000269|PubMed:7644496}.; . . lung;whole body;ovary;heart;bone;placenta;liver;colon;parathyroid;spleen;bone marrow; fetal liver;whole blood;bone marrow; 0.05528 0.31251 -0.009020804 52.8544468 13.35188 0.48559 PF4V1 0.00689209434338382 0.524507475980311 0.468600429676305 platelet factor 4 variant 1 FUNCTION: Inhibitor of angiogenesis. Inhibitor of endothelial cell chemotaxis (in vitro). {ECO:0000269|PubMed:15459074}.; . . unclassifiable (Anatomical System); . 0.03389 0.10810 0.147123112 64.11299835 8.09501 0.29657 PFAS 2.79097135483484e-08 0.999959618205718 4.0353884568516e-05 phosphoribosylformylglycinamidine synthase FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (By similarity). {ECO:0000250}.; . . smooth muscle;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;duodenum;cervix;kidney;stomach;thymus; superior cervical ganglion;cerebellum; 0.78567 . -0.514518236 21.21962727 4348.06052 13.14058 PFDN1 0.805475103411555 0.189439301452789 0.00508559513565612 prefoldin subunit 1 FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.; . . medulla oblongata;smooth muscle;ovary;skin;prostate;frontal lobe;endometrium;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;salivary gland;colon;parathyroid;fovea centralis;vein;uterus;whole body;atrium;cerebral cortex;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus; thalamus;cerebellum peduncles;cingulate cortex;parietal lobe; 0.08376 0.11614 -0.009020804 52.8544468 2.49433 0.09224 PFDN2 0.219933484264837 0.742639510621318 0.0374270051138445 prefoldin subunit 2 FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. {ECO:0000269|PubMed:9630229}.; . . . . 0.71187 0.14229 -0.09720619 46.20193442 11.43886 0.41319 PFDN4 0.100179293326146 0.772428177394327 0.127392529279527 prefoldin subunit 4 FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. {ECO:0000269|PubMed:9630229}.; . . . . 0.54660 0.22085 0.301449681 71.80938901 17.8354 0.62334 PFDN5 0.0433855614772836 0.848776090952086 0.10783834757063 prefoldin subunit 5 FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Represses the transcriptional activity of MYC. {ECO:0000269|PubMed:9630229}.; . TISSUE SPECIFICITY: Highly expressed in pancreas and skeletal muscle and moderately in other tissues.; myocardium;lymphoreticular;smooth muscle;umbilical cord;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;cochlea;thyroid;iris;germinal center;bladder;brain;tonsil;gall bladder;cartilage;heart;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;trophoblast;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; testis; 0.45940 0.50622 -0.207437529 38.2814343 4.8462 0.17860 PFDN6 0.859422179892135 0.13842015232993 0.00215766777793527 prefoldin subunit 6 FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. {ECO:0000269|PubMed:9630229}.; . . . . 0.33266 0.14896 0.323496558 72.93583392 5.58824 0.20879 PFKFB1 0.000222069886004765 0.979361305701712 0.0204166244122835 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1 FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.; . TISSUE SPECIFICITY: Liver.; . . 0.42009 0.23453 -0.580403979 18.58928993 47.39908 1.33566 PFKFB2 0.0010886274208406 0.996737136280916 0.00217423629824336 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.; . TISSUE SPECIFICITY: Heart.; . . 0.22972 0.17259 -0.66859065 15.76433121 34.72563 1.05839 PFKFB3 0.0489318118268948 0.950078940846756 0.000989247326349137 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;amniotic fluid;germinal center;brain;bladder;ciliary body;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;uterus;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; amygdala;hypothalamus;spinal cord;ciliary ganglion;skeletal muscle; 0.20730 0.34793 -1.397999468 4.193205945 52.51588 1.43463 PFKFB4 0.000321134414442041 0.987414875931419 0.012263989654139 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4 FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.; . . unclassifiable (Anatomical System);medulla oblongata;ovary;tongue;colon;blood;skin;skeletal muscle;bone marrow;uterus;optic nerve;lung;larynx;placenta;visual apparatus;liver;testis;head and neck;spleen;kidney;brain; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.11735 0.14627 -0.934977358 9.465675867 55.24789 1.49154 PFKL 3.68287250532775e-10 0.753100795274505 0.246899204357208 phosphofructokinase, liver type FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:22923583}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;oesophagus;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;small intestine;lacrimal gland;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach; subthalamic nucleus;superior cervical ganglion;liver;ciliary ganglion;kidney;atrioventricular node;cingulate cortex;skeletal muscle; 0.18705 0.43522 -1.300731691 4.948100967 827.5826 5.64027 PFKM 6.03263003776653e-07 0.99970780233128 0.000291594405716478 phosphofructokinase, muscle FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.; DISEASE: Glycogen storage disease 7 (GSD7) [MIM:232800]: A metabolic disorder characterized by exercise intolerance with associated nausea and vomiting, muscle cramping, exertional myopathy and compensated hemolysis. Short bursts of intense activity are particularly difficult. Severe muscle cramps and myoglobinuria develop after vigorous exercise. {ECO:0000269|PubMed:22133655, ECO:0000269|PubMed:24427140, ECO:0000269|PubMed:7513946, ECO:0000269|PubMed:7825568, ECO:0000269|PubMed:8889589}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;lymphoreticular;ovary;sympathetic chain;skin;retina;prostate;optic nerve;ganglion;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;greater omentum;epididymis;visual apparatus;macula lutea;alveolus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;small intestine;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; whole brain;superior cervical ganglion;thalamus;occipital lobe;subthalamic nucleus;cerebellum peduncles;hypothalamus;globus pallidus;pons;skeletal muscle;cingulate cortex;parietal lobe;cerebellum; 0.25899 0.78377 -0.464712395 23.5727766 3843.53437 12.20917 PFKP 7.08342752970718e-15 0.199871474596296 0.800128525403697 phosphofructokinase, platelet FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.; . . . . 0.21987 0.31299 -2.627729218 0.790280727 140.15983 2.58263 PFM3 . . . parietal foramina 3 . . . . . . . . . . . PFN1 0.688581661711059 0.292992404281759 0.0184259340071818 profilin 1 FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR. {ECO:0000269|PubMed:18573880}.; DISEASE: Amyotrophic lateral sclerosis 18 (ALS18) [MIM:614808]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. {ECO:0000269|PubMed:22801503}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in epididymis (at protein level). {ECO:0000269|PubMed:20736409}.; smooth muscle;ovary;colon;parathyroid;choroid;vein;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; adipose tissue;smooth muscle;heart;tumor;white blood cells;bone marrow;lung;placenta;liver;fetal lung;whole blood;tonsil;thymus; 0.89845 0.25991 -0.075159878 47.78839349 474.77356 4.50278 PFN1P1 . . . profilin 1 pseudogene 1 . . . . . . . . . . . PFN1P2 . . . profilin 1 pseudogene 2 . . . . . . . . . . . PFN1P3 . . . profilin 1 pseudogene 3 . . . . . . . . . . . PFN1P4 . . . profilin 1 pseudogene 4 . . . . . . . . . . . PFN1P6 . . . profilin 1 pseudogene 6 . . . . . . . . . . . PFN1P8 . . . profilin 1 pseudogene 8 . . . . . . . . . . . PFN1P9 . . . profilin 1 pseudogene 9 . . . . . . . . . . . PFN1P10 . . . profilin 1 pseudogene 10 . . . . . . . . . . . PFN1P11 . . . profilin 1 pseudogene 11 . . . . . . . . . . . PFN1P12 . . . profilin 1 pseudogene 12 . . . . . . . . . . . PFN2 0.638693741946579 0.333223486710412 0.028082771343009 profilin 2 FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.; . TISSUE SPECIFICITY: Highly expressed in brain, skeletal muscle and kidney and less strongly in heart, placenta, lung and liver.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;brain;heart;cartilage;tongue;pineal body;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;placenta;hippocampus;amnion;head and neck;kidney;aorta;stomach;cerebellum; . 0.63497 0.23021 0.035072054 56.2514744 263.94455 3.48622 PFN3 0.519957351463764 0.415469029437309 0.0645736190989269 profilin 3 FUNCTION: Binds to actin and affects the structure of the cytoskeleton. Slightly reduces actin polymerization. Binds to poly-L-proline, phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 4-phosphate (PtdIns(4)P). May be involved in spermatogenesis. {ECO:0000269|PubMed:19419568}.; . TISSUE SPECIFICITY: Testis specific.; lung;testis; . 0.11262 . . . 33.36759 1.03015 PFN4 0.00113106337284472 0.617066884887737 0.381802051739419 profilin family member 4 FUNCTION: Binds to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidic acid (PA). Does not bind to actin (PubMed:19419568), contrary to other family members. {ECO:0000269|PubMed:19419568}.; . TISSUE SPECIFICITY: Detected in testis (at protein level). {ECO:0000269|PubMed:15591451}.; unclassifiable (Anatomical System);prostate;optic nerve;lung;macula lutea;testis;fovea centralis;choroid;lens;brain;retina; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.10800 0.11388 0.03689118 56.64071715 14.292 0.51700 PGA3 0.645340633938956 0.328029701887939 0.0266296641731055 pepsinogen 3, group I (pepsinogen A) FUNCTION: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.; . . hypothalamus;colon;skin;retina;oesophagus;cerebral cortex;liver;pituitary gland;spleen;kidney;mammary gland;stomach;peripheral nerve; . 0.08037 0.10431 . . 14.68958 0.52977 PGA4 . . . pepsinogen 4, group I (pepsinogen A) FUNCTION: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.; . . . . 0.15599 0.20707 . . 1.96546 0.06398 PGA5 0.00127358049246854 0.642905853966507 0.355820565541025 pepsinogen 5, group I (pepsinogen A) FUNCTION: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.; . . unclassifiable (Anatomical System);colon;skin;retina;lung;oesophagus;cerebral cortex;liver;pituitary gland;testis;spleen;kidney;stomach;peripheral nerve; . 0.19220 0.10469 . . 102.03931 2.18450 PGAM1 0.623538729209142 0.368924685124327 0.00753658566653093 phosphoglycerate mutase 1 FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.; . TISSUE SPECIFICITY: In mammalian tissues there are two types of phosphoglycerate mutase isozymes: type-M in muscles and type-B in other tissues.; . . 0.20024 0.30319 -0.029247611 51.40363293 43.96465 1.26347 PGAM1P1 . . . phosphoglycerate mutase 1 pseudogene 1 . . . . . . . . . . . PGAM1P2 . . . phosphoglycerate mutase 1 pseudogene 2 . . . . . . . . . . . PGAM1P3 . . . phosphoglycerate mutase 1 pseudogene 3 . . . . . . . . . . . PGAM1P4 . . . phosphoglycerate mutase 1 pseudogene 4 . . . unclassifiable (Anatomical System);lymph node;ovary;heart;tongue;salivary gland;skin;uterus;prostate;pancreas;whole body;lung;frontal lobe;endometrium;larynx;placenta;liver;cervix;head and neck;kidney;germinal center;brain;mammary gland;stomach; . . . . . . . PGAM1P5 . . . phosphoglycerate mutase 1 pseudogene 5 . . . . . . . . . . . PGAM1P6 . . . phosphoglycerate mutase 1 pseudogene 6 . . . . . . . . . . . PGAM1P7 . . . phosphoglycerate mutase 1 pseudogene 7 . . . . . . . . . . . PGAM1P8 . . . phosphoglycerate mutase 1 pseudogene 8 . . . . . . . . . . . PGAM1P9 . . . phosphoglycerate mutase 1 pseudogene 9 . . . . . . . . . . . PGAM1P10 . . . phosphoglycerate mutase 1 pseudogene 10 . . . . . . . . . . . PGAM1P11 . . . phosphoglycerate mutase 1 pseudogene 11 . . . . . . . . . . . PGAM1P12 . . . phosphoglycerate mutase 1 pseudogene 12 . . . . . . . . . . . PGAM1P13 . . . phosphoglycerate mutase 1 pseudogene 13 . . . . . . . . . . . PGAM2 0.000842261527216773 0.552920125785142 0.446237612687641 phosphoglycerate mutase 2 FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.; . TISSUE SPECIFICITY: In mammalian tissues there are two types of phosphoglycerate mutase isozymes: type-M in muscles and type-B in other tissues.; unclassifiable (Anatomical System);myocardium;medulla oblongata;heart;muscle;blood;lens;skeletal muscle;greater omentum;whole body;lung;placenta;bone;testis;brain;cerebellum; testis - interstitial;testis - seminiferous tubule;heart;tongue;testis;ciliary ganglion;skeletal muscle; 0.70253 0.21529 -0.512444034 21.55579146 485.14997 4.53547 PGAM3P . . . phosphoglycerate mutase 3, pseudogene . . . . . . . . . . . PGAM4 0.28327008535875 0.630432290902981 0.0862976237382694 phosphoglycerate mutase family member 4 . . . . . 0.14150 0.15572 0.415317661 76.81056853 387.32597 4.14472 PGAM4P1 . . . phosphoglycerate mutase family member 4 pseudogene 1 . . . . . . . . . . . PGAM4P2 . . . phosphoglycerate mutase family member 4 pseudogene 2 . . . . . . . . . . . PGAM5 0.03521668839589 0.827864050443202 0.136919261160908 PGAM family member 5, mitochondrial serine/threonine protein phosphatase FUNCTION: Displays phosphatase activity for serine/threonine residues, and, dephosphorylates and activates MAP3K5 kinase. Has apparently no phosphoglycerate mutase activity. May be regulator of mitochondrial dynamics. Substrate for a KEAP1-dependent ubiquitin ligase complex. Contributes to the repression of NFE2L2- dependent gene expression. Acts as a central mediator for programmed necrosis induced by TNF, by reactive oxygen species and by calcium ionophore. {ECO:0000269|PubMed:18387606, ECO:0000269|PubMed:19590015, ECO:0000269|PubMed:22265414}.; . . unclassifiable (Anatomical System);uterus;prostate;testis;cervix;blood;mammary gland;stomach; liver;kidney; 0.36385 0.11172 0.17280645 65.75843359 175.44559 2.88079 PGAM5P1 . . . PGAM family member 5, mitochondrial serine/threonine protein phosphatase pseudogene 1 . . . . . . . . . . . PGAP1 0.00878588184543819 0.991209738451216 4.37970334580232e-06 post-GPI attachment to proteins 1 FUNCTION: Involved in inositol deacylation of GPI-anchored proteins. GPI inositol deacylation may important for efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi (By similarity). {ECO:0000250}.; DISEASE: Mental retardation, autosomal recessive 42 (MRT42) [MIM:615802]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:24784135}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;skin;prostate;frontal lobe;cochlea;bone;testis;dura mater;brain;unclassifiable (Anatomical System);amygdala;meninges;islets of Langerhans;hypothalamus;skeletal muscle;breast;lung;pia mater;adrenal gland;placenta;liver;kidney;mammary gland;stomach;aorta; amygdala;superior cervical ganglion;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.24265 . -0.666770504 15.86459071 57.58899 1.53274 PGAP2 0.15222416020635 0.830890196409736 0.0168856433839145 post-GPI attachment to proteins 2 FUNCTION: Involved in the lipid remodeling steps of GPI-anchor maturation. Required for stable expression of GPI-anchored proteins at the cell surface (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in testis and pancreas. {ECO:0000269|PubMed:10585768}.; lymphoreticular;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;cochlea;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pineal body;blood;lens;bile duct;pancreas;lung;placenta;liver;spleen;kidney;mammary gland;stomach; testis; . . -0.291981272 33.20358575 . . PGAP3 0.0909847298785156 0.869522022351678 0.0394932477698062 post-GPI attachment to proteins 3 FUNCTION: Involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchors proteins. Required for phospholipase A2 activity that removes an acyl-chain at the sn-2 position of GPI-anchors during the remodeling of GPI (Probable). {ECO:0000305|PubMed:17021251}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in thyroid and placenta. {ECO:0000269|PubMed:12460457}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;adrenal cortex;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;placenta;liver;ciliary ganglion;pons;trigeminal ganglion; 0.32480 0.13182 0.328949044 73.41354093 79.17976 1.87863 PGBD1 1.46735073363618e-05 0.960551754807593 0.039433571685071 piggyBac transposable element derived 1 . . . unclassifiable (Anatomical System);heart;muscle;fovea centralis;choroid;lens;skin;retina;uterus;breast;optic nerve;lung;oesophagus;bone;macula lutea;liver;cervix;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.03039 0.10231 1.137205722 92.32719981 2687.18695 9.75354 PGBD2 3.892421473741e-07 0.35592234568248 0.644077265075373 piggyBac transposable element derived 2 . . . ovary;islets of Langerhans;skin;skeletal muscle;uterus;pancreas;prostate;lung;endometrium;thyroid;placenta;liver;testis;head and neck;spleen;brain;aorta; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.15772 . -0.821100135 11.88369899 352.4208 3.97674 PGBD3 3.01621817097075e-06 0.538529813516502 0.461467170265327 piggyBac transposable element derived 3 . . . . . . . -0.488577883 22.64685067 . . PGBD3P1 . . . piggyBac transposable element derived 3 pseudogene 1 . . . . . . . . . . . PGBD3P2 . . . piggyBac transposable element derived 3 pseudogene 2 . . . . . . . . . . . PGBD3P3 . . . piggyBac transposable element derived 3 pseudogene 3 . . . . . . . . . . . PGBD3P4 . . . piggyBac transposable element derived 3 pseudogene 4 . . . . . . . . . . . PGBD4 5.90742356728259e-05 0.700899633771394 0.299041291992934 piggyBac transposable element derived 4 . . . . . 0.04376 . -0.314027422 31.9297004 109.53855 2.27391 PGBD4P1 . . . piggyBac transposable element derived 4 pseudogene 1 . . . . . . . . . . . PGBD4P2 . . . piggyBac transposable element derived 4 pseudogene 2 . . . . . . . . . . . PGBD4P3 . . . piggyBac transposable element derived 4 pseudogene 3 . . . . . . . . . . . PGBD4P4 . . . piggyBac transposable element derived 4 pseudogene 4 . . . . . . . . . . . PGBD4P5 . . . piggyBac transposable element derived 4 pseudogene 5 . . . . . . . . . . . PGBD4P6 . . . piggyBac transposable element derived 4 pseudogene 6 . . . . . . . . . . . PGBD4P7 . . . piggyBac transposable element derived 4 pseudogene 7 . . . . . . . . . . . PGBD4P8 . . . piggyBac transposable element derived 4 pseudogene 8 . . . . . . . . . . . PGBD5 0.0280632434924286 0.96077475393942 0.0111620025681518 piggyBac transposable element derived 5 . . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);amygdala;heart;lens;breast;lung;placenta;macula lutea;hippocampus;liver;cervix;head and neck;kidney;cerebellum; amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.27400 . . . 1053.33568 6.23218 PGC 3.30129659251128e-06 0.558007879997902 0.441988818705505 progastricsin (pepsinogen C) FUNCTION: Hydrolyzes a variety of proteins.; . . unclassifiable (Anatomical System);prostate;pancreas;lung;cerebral cortex;oesophagus;stomach; prostate;superior cervical ganglion;fetal lung;skeletal muscle; 0.09000 . 0.264628794 70.5178108 34.21948 1.04735 PGCP1 . . . progastricsin (pepsinogen C) pseudogene 1 . . . . . . . . . . . PGD 0.968660462332331 0.0313375418661925 1.99580147591939e-06 phosphogluconate dehydrogenase FUNCTION: Catalyzes the oxidative decarboxylation of 6- phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. {ECO:0000250}.; . . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;tonsil;heart;urinary;pharynx;blood;lens;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;cerebellum; adipose tissue;tumor;bone marrow; 0.25674 0.83834 -0.66859065 15.76433121 359.50529 4.01463 PGDP1 . . . phosphogluconate dehydrogenase pseudogene 1 . . . . . . . . . . . PGDP2 . . . phosphogluconate dehydrogenase pseudogene 2 . . . . . . . . . . . PGF 0.898304164411566 0.100761547711561 0.000934287876872748 placental growth factor FUNCTION: Growth factor active in angiogenesis and endothelial cell growth, stimulating their proliferation and migration. It binds to the receptor FLT1/VEGFR-1. Isoform PlGF-2 binds NRP1/neuropilin-1 and NRP2/neuropilin-2 in a heparin-dependent manner. Also promotes cell tumor growth. {ECO:0000269|PubMed:21215706}.; . TISSUE SPECIFICITY: While the three isoforms are present in most placental tissues, PlGF-2 is specific to early (8 week) placenta and only PlGF-1 is found in the colon and mammary carcinomas.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;cerebral cortex;larynx;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;muscle;lens;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;subthalamic nucleus;thyroid;placenta;temporal lobe;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe; 0.34071 0.08473 -0.383807564 27.41802312 11.67075 0.42322 PGGT1B 0.625204501483712 0.374476715557221 0.000318782959066927 protein geranylgeranyltransferase type I subunit beta FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. Known substrates include RAC1, RAC2, RAP1A and RAP1B. {ECO:0000269|PubMed:8106351}.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;colon;blood;skeletal muscle;prostate;lung;larynx;testis;head and neck;germinal center;kidney;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;globus pallidus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.55968 0.15588 -0.0274281 51.65723048 134.97765 2.52744 PGGT1BP1 . . . protein geranylgeranyltransferase type I, beta subunit pseudogene 1 . . . . . . . . . . . PGGT1BP2 . . . protein geranylgeranyltransferase type I, beta subunit pseudogene 2 . . . . . . . . . . . PGK1 0.971138951857199 0.028821438527794 3.96096150065934e-05 phosphoglycerate kinase 1 FUNCTION: In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein).; DISEASE: Phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:300653]: A condition with a highly variable clinical phenotype that includes hemolytic anemia, rhabdomyolysis, myopathy and neurologic involvement. Patients can express one or more of these manifestations. {ECO:0000269|PubMed:1547346, ECO:0000269|PubMed:1586722, ECO:0000269|PubMed:2001457, ECO:0000269|PubMed:6933565, ECO:0000269|PubMed:6941312, ECO:0000269|PubMed:8043870, ECO:0000269|PubMed:8615693, ECO:0000269|PubMed:8673469, ECO:0000269|PubMed:9744480}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.80126 0.97337 -0.449946534 24.00330267 30.18239 0.96311 PGK1P1 . . . phosphoglycerate kinase 1, pseudogene 1 . . . . . . . . . . . PGK1P2 . . . phosphoglycerate kinase 1, pseudogene 2 . . . . . . . . . . . PGK2 9.50692786238878e-06 0.186843818303922 0.813146674768215 phosphoglycerate kinase 2 . . TISSUE SPECIFICITY: Testis specific.; medulla oblongata;testis;skeletal muscle; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;pons; 0.50448 0.50327 0.418953042 77.06416608 198.96137 3.04777 PGLS 0.0420579993703126 0.846059763351711 0.111882237277977 6-phosphogluconolactonase FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- phosphogluconate.; . . lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;pancreas;lung;cornea;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; lung;heart;thyroid;liver;whole blood; 0.45580 0.21955 . . 83.41566 1.94137 PGLYRP1 0.167200721076412 0.771853707001391 0.0609455719221967 peptidoglycan recognition protein 1 FUNCTION: Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram- negative bacteria, and has bacteriostatic activity towards Gram- negative bacteria. Plays a role in innate immunity. {ECO:0000269|PubMed:11461926, ECO:0000269|PubMed:16354652}.; . TISSUE SPECIFICITY: Highly expressed in bone marrow. Weak expression found in kidney, liver, small intestine, spleen, thymus, peripheral leukocyte, lung, fetal spleen and neutrophils. {ECO:0000269|PubMed:11461926, ECO:0000269|PubMed:9707603}.; unclassifiable (Anatomical System);frontal lobe;blood;bone marrow; superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle;bone marrow; 0.02479 0.06784 0.459411326 78.28497287 44.55885 1.27805 PGLYRP2 1.33294125207149e-08 0.197891064390294 0.802108922280293 peptidoglycan recognition protein 2 FUNCTION: May play a scavenger role by digesting biologically active peptidoglycan (PGN) into biologically inactive fragments. Has no direct bacteriolytic activity. {ECO:0000269|PubMed:14506276}.; . TISSUE SPECIFICITY: Strongly expressed in liver and fetal liver, and secreted into serum. Expressed to a much lesser extent in transverse colon, lymph nodes, heart, thymus, pancreas, descending colon, stomach and testis. Isoform 2 is not detected in the liver or serum. {ECO:0000269|PubMed:11461926, ECO:0000269|PubMed:16054449}.; unclassifiable (Anatomical System);medulla oblongata;liver; fetal liver;liver;atrioventricular node; 0.10496 0.14582 1.46612072 95.25241802 1454.60989 7.11541 PGLYRP3 9.00246757206822e-05 0.784807931014809 0.21510204430947 peptidoglycan recognition protein 3 FUNCTION: Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram- negative bacteria, and has bacteriostatic activity towards Gram- negative bacteria. Plays a role in innate immunity. {ECO:0000269|PubMed:16354652}.; . TISSUE SPECIFICITY: Detected in skin epidermis, eccrine sweat glands and ducts, ciliary body epithelial cells of the eye, in small intestine, colon, stomach and in mature epithelial cells of the tongue (at protein level). Highly expressed in skin and esophagus, expressed also in tonsils and thymus and to a much lesser extent in the stomach, descending colon, rectum and brain. {ECO:0000269|PubMed:11461926, ECO:0000269|PubMed:16354652}.; . . 0.10919 0.10500 1.199707453 92.98183534 5533.08243 15.36976 PGLYRP4 2.63028984617915e-08 0.156503973726313 0.843495999970788 peptidoglycan recognition protein 4 FUNCTION: Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram- negative bacteria, and has bacteriostatic activity towards Gram- negative bacteria. Plays a role in innate immunity. {ECO:0000269|PubMed:16354652}.; . TISSUE SPECIFICITY: Detected in skin epidermis, eccrine sweat glands and ducts, mucous cells in the submandibular salivary gland, mucous cells in the throat, ciliary body epithelial cells of the eye, small intestine, colon, stomach and in mature epithelial cells of the tongue (at protein level). High expression in skin and esophagus. Expressed also to a much lesser extent in the tonsils and thymus. {ECO:0000269|PubMed:11461926, ECO:0000269|PubMed:16354652}.; unclassifiable (Anatomical System);skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.08537 0.09092 1.264035907 93.58339231 368.64618 4.05737 PGM1 9.96139807231456e-06 0.935507180397983 0.0644828582039446 phosphoglucomutase 1 FUNCTION: This enzyme participates in both the breakdown and synthesis of glucose.; DISEASE: Congenital disorder of glycosylation 1T (CDG1T) [MIM:614921]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:19625727, ECO:0000269|PubMed:22492991, ECO:0000269|PubMed:22976764, ECO:0000269|PubMed:24499211, ECO:0000269|PubMed:25288802}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.87620 0.63061 -0.21856543 37.66218448 7693.9811 18.88204 PGM2 1.05928155018637e-12 0.147762519564678 0.852237480434263 phosphoglucomutase 2 FUNCTION: Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. May also catalyze the interconversion of glucose-1-phosphate and glucose-6-phosphate. Has low glucose 1,6-bisphosphate synthase activity. {ECO:0000269|PubMed:17804405}.; . . . . 0.13924 0.40444 0.090079492 60.64519934 383.06081 4.12803 PGM2L1 0.390476072570689 0.609439905342525 8.40220867858722e-05 phosphoglucomutase 2-like 1 FUNCTION: Glucose 1,6-bisphosphate synthase using 1,3- bisphosphoglycerate as a phosphate donor and a series of 1- phosphate sugars as acceptors, including glucose 1-phosphate, mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1- phosphate. 5 or 6-phosphosugars are bad substrates, with the exception of glucose 6-phosphate. Also synthesizes ribose 1,5- bisphosphate. Has only low phosphopentomutase and phosphoglucomutase activities. {ECO:0000269|PubMed:17804405, ECO:0000269|PubMed:18927083}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;brain;pineal gland;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;hypothalamus;pineal body;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland; amygdala;subthalamic nucleus;occipital lobe;fetal brain;temporal lobe;globus pallidus;ciliary ganglion;pons;cingulate cortex;parietal lobe; 0.44485 0.20386 0.50895761 80.20169851 2037.212 8.31781 PGM3 0.0235635730698108 0.975826407476604 0.000610019453584914 phosphoglucomutase 3 FUNCTION: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation. {ECO:0000303|PubMed:24589341, ECO:0000303|PubMed:24698316, ECO:0000303|PubMed:24931394}.; . TISSUE SPECIFICITY: Found in many tissues except lung. Relatively high expression in pancreas, heart, liver, and placenta, and relatively low expression in brain, skeletal muscle and kidney. {ECO:0000269|PubMed:10721701}.; ovary;colon;skin;retina;bone marrow;uterus;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;spinal cord;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;smooth muscle; 0.64376 0.67064 -0.26993514 34.59542345 1952.13289 8.13047 PGM5 0.961611244474183 0.0383854497566297 3.30576918695738e-06 phosphoglucomutase 5 FUNCTION: Component of adherens-type cell-cell and cell-matrix junctions. Lacks phosphoglucomutase activity.; . TISSUE SPECIFICITY: Detected in smooth and cardiac muscle at high levels and in skeletal muscle at low level. Present in other tissues due to vascular or other smooth muscle component. Low levels are present in liver, kidney, skin and brain (at protein level). {ECO:0000269|PubMed:8175905, ECO:0000269|PubMed:8631316}.; . . 0.47663 0.11828 -0.422438699 25.64284029 133.77721 2.51514 PGM5-AS1 . . . PGM5 antisense RNA 1 . . . . . . . . . . . PGM5P1 . . . phosphoglucomutase 5 pseudogene 1 . . . . . . . . . . . PGM5P2 . . . phosphoglucomutase 5 pseudogene 2 . . . unclassifiable (Anatomical System);pancreas; . . . . . . . PGM5P3 . . . phosphoglucomutase 5 pseudogene 3 . . . . . . . . . . . PGM5P3-AS1 . . . PGM5P3 antisense RNA 1 . . . . . . . . . . . PGM5P4 . . . phosphoglucomutase 5 pseudogene 4 . . . . . . . . . . . PGM5P4-AS1 . . . PGM5P4 antisense RNA 1 . . . . . . . . . . . PGP 0.757807855144398 0.233001720710039 0.00919042414556356 phosphoglycolate phosphatase FUNCTION: Phosphatase with broad substrate specificity. Has high phosphatase activity toward ADP, ATP, GDP, GTP and p- nitrophenylphosphate. Has tyrosine-protein phosphatase activity (in vitro). Has very low activity with pyridoxal 5'-phosphate (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in all tissues including red cells, lymphocytes and cultured fibroblasts (at protein level). The highest activities occur in skeletal muscle and cardiac muscle. {ECO:0000269|PubMed:215071}.; lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; trigeminal ganglion; 0.19531 0.18996 . . 171.46821 2.85586 PGPEP1 0.000353365407990264 0.606298564755972 0.393348069836038 pyroglutamyl-peptidase I FUNCTION: Removes 5-oxoproline from various penultimate amino acid residues except L-proline. {ECO:0000269|PubMed:12651114}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;skin;skeletal muscle;retina;uterus;prostate;optic nerve;lung;frontal lobe;cerebral cortex;endometrium;bone;placenta;liver;testis;spleen;germinal center;kidney;brain;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;prefrontal cortex;liver;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skin; 0.26680 0.21873 -0.205617011 38.57631517 140.56428 2.58665 PGPEP1L 6.97508611499858e-06 0.157918915692151 0.842074109221734 pyroglutamyl-peptidase I-like . . . . . . . 1.284269037 93.76621845 6405.86915 16.74324 PGR 0.884782623229294 0.115206413675528 1.09630951780876e-05 progesterone receptor FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Progesterone receptor isoform B (PRB) is involved activation of c-SRC/MAPK signaling on hormone stimulation.; FUNCTION: Isoform 4: Increases mitochondrial membrane potential and cellular respiration upon stimulation by progesterone.; . . medulla oblongata;kidney;skeletal muscle; uterus;uterus corpus;superior cervical ganglion;testis - interstitial;testis;pons;trigeminal ganglion;skeletal muscle; 0.13858 0.53017 . . 1363.72417 6.92862 PGRMC1 0.622396927421126 0.34572338587346 0.0318796867054134 progesterone receptor membrane component 1 FUNCTION: Receptor for progesterone. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in liver and kidney.; smooth muscle;ovary;salivary gland;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;ciliary body;brain;artery;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pineal body;adrenal cortex;blood;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;adrenal gland;hypothalamus;spinal cord;globus pallidus;caudate nucleus;kidney;parietal lobe; 0.23483 0.22862 0.125076652 62.7388535 15.64346 0.55821 PGRMC2 0.403432082267 0.557987568986232 0.0385803487467675 progesterone receptor membrane component 2 FUNCTION: Receptor for steroids. {ECO:0000305}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;atrium;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;fetal liver;placenta;thyroid; 0.24502 0.15979 . . 86.09241 1.98113 PGS1 0.000957081939012816 0.986438172330095 0.0126047457308917 phosphatidylglycerophosphate synthase 1 FUNCTION: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin. {ECO:0000250}.; . . colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;cochlea;endometrium;larynx;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;mammary gland;stomach; . 0.39549 0.12955 -0.336073593 30.55555556 123.91425 2.42300 PHACTR1 0.664117315162539 0.313073279913672 0.0228094049237885 phosphatase and actin regulator 1 FUNCTION: Binds actin monomers (G actin) and plays a role in the reorganization of the actin cytoskeleton and in formation of actin stress fibers. Plays a role in cell motility. Plays a role in the formation of tubules by endothelial cells. Regulates PPP1CA activity. Required for normal cell survival. {ECO:0000269|PubMed:21798305, ECO:0000269|PubMed:21939755}.; . TISSUE SPECIFICITY: Detected in umbilical vein endothelial cells. {ECO:0000269|PubMed:21939755}.; unclassifiable (Anatomical System);pancreas;lung;frontal lobe;pineal body;macula lutea;hippocampus;testis;fovea centralis;kidney;germinal center;brain;skin; amygdala;dorsal root ganglion;medulla oblongata;superior cervical ganglion;temporal lobe;atrioventricular node;pons;skeletal muscle;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.55676 0.11136 . . 15.56557 0.55544 PHACTR2 0.00738942305798489 0.99247299937875 0.000137577563264728 phosphatase and actin regulator 2 . . . unclassifiable (Anatomical System);heart;colon;skin;skeletal muscle;retina;uterus;lung;endometrium;nasopharynx;placenta;thyroid;iris;liver;kidney;thymus; superior cervical ganglion;testis - interstitial;placenta;trigeminal ganglion; 0.72710 0.09166 -0.045835247 50.34206181 1505.57685 7.21249 PHACTR2-AS1 . . . PHACTR2 antisense RNA 1 . . . . . . . . . . . PHACTR2P1 . . . phosphatase and actin regulator 2 pseudogene 1 . . . . . . . . . . . PHACTR3 0.971713289002321 0.0282863977534459 3.13244232881268e-07 phosphatase and actin regulator 3 . . TISSUE SPECIFICITY: Abundantly expressed in brain. Also found in several tumors such as lung carcinomas, nervous tumors and HL-60 leukemia cells. Isoform 3 is the major form in U-937, GOTO and HL- 60 leukemia cells.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;skin;uterus;pancreas;optic nerve;whole body;lung;frontal lobe;larynx;placenta;head and neck;kidney;brain; subthalamic nucleus;medulla oblongata;occipital lobe;temporal lobe;prefrontal cortex;globus pallidus;pons;cingulate cortex;parietal lobe; 0.42756 0.10156 -0.220384297 37.6032083 240.61752 3.35156 PHACTR4 0.00427377620221426 0.995422048015992 0.000304175781794249 phosphatase and actin regulator 4 FUNCTION: Regulator of protein phosphatase 1 (PP1) required for neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. Acts as an activator of PP1 by interacting with PPP1CA and preventing phosphorylation of PPP1CA at 'Thr-320'. During neural tube closure, localizes to the ventral neural tube and activates PP1, leading to down-regulate cell proliferation within cranial neural tissue and the neural retina. Also acts as a regulator of migration of enteric neural crest cells (ENCCs) by activating PP1, leading to dephosphorylation and subsequent activation of cofilin (COF1 or COF2) and repression of the integrin signaling through the RHO/ROCK pathway (By similarity). {ECO:0000250}.; . . . . 0.04060 0.06618 -0.442665927 24.53408823 1515.44842 7.23828 PHAX 0.00269319619944417 0.983312838187735 0.0139939656128211 phosphorylated adaptor for RNA export FUNCTION: A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation- independent manner (By similarity). Plays also a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Binds also to telomerase RNA. {ECO:0000250, ECO:0000269|PubMed:15574332, ECO:0000269|PubMed:15574333}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;cerebellum cortex;islets of Langerhans;adrenal cortex;pharynx;blood;lens;breast;bile duct;lung;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; . 0.17782 0.12170 -0.268115223 34.70747818 1174.52587 6.51141 PHB 0.821632149771825 0.177514222898353 0.000853627329821836 prohibitin FUNCTION: Prohibitin inhibits DNA synthesis. It has a role in regulating proliferation. As yet it is unclear if the protein or the mRNA exhibits this effect. May play a role in regulating mitochondrial respiration activity and in aging. {ECO:0000269|PubMed:11302691}.; . TISSUE SPECIFICITY: Widely expressed in different tissues.; lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;duodenum;kidney;stomach;thymus; heart;liver;tumor;appendix;kidney;trigeminal ganglion;skeletal muscle; 0.87417 0.68456 0.03689118 56.64071715 11.35938 0.40904 PHB2 0.0758353620381498 0.921743756734798 0.00242088122705258 prohibitin 2 FUNCTION: Acts as a mediator of transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases (By similarity). Functions as an estrogen receptor (ER)-selective coregulator that potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. Competes with NCOA1 for modulation of ER transcriptional activity. Probably involved in regulating mitochondrial respiration activity and in aging. {ECO:0000250|UniProtKB:O35129, ECO:0000269|PubMed:10359819, ECO:0000303|PubMed:11302691}.; . . . . 0.40876 . -0.405853867 26.23260203 38.54782 1.14308 PHB2P1 . . . prohibitin 2 pseudogene 1 . . . . . . . . . . . PHBP1 . . . prohibitin pseudogene 1 . . . . . . . . . . . PHBP2 . . . prohibitin pseudogene 2 . . . . . . . . . . . PHBP3 . . . prohibitin pseudogene 3 . . . . . . . . . . . PHBP4 . . . prohibitin pseudogene 4 . . . . . . . . . . . PHBP5 . . . prohibitin pseudogene 5 . . . . . . . . . . . PHBP6 . . . prohibitin pseudogene 6 . . . . . . . . . . . PHBP7 . . . prohibitin pseudogene 7 . . . . . . . . . . . PHBP8 . . . prohibitin pseudogene 8 . . . . . . . . . . . PHBP9 . . . prohibitin pseudogene 9 . . . . . . . . . . . PHBP10 . . . prohibitin pseudogene 10 . . . . . . . . . . . PHBP11 . . . prohibitin pseudogene 11 . . . . . . . . . . . PHBP12 . . . prohibitin pseudogene 12 . . . . . . . . . . . PHBP13 . . . prohibitin pseudogene 13 . . . . . . . . . . . PHBP14 . . . prohibitin pseudogene 14 . . . . . . . . . . . PHBP15 . . . prohibitin pseudogene 15 . . . . . . . . . . . PHBP16 . . . prohibitin pseudogene 16 . . . . . . . . . . . PHBP17 . . . prohibitin pseudogene 17 . . . . . . . . . . . PHBP18 . . . prohibitin pseudogene 18 . . . . . . . . . . . PHBP19 . . . prohibitin pseudogene 19 . . . . . . . . . . . PHBP20 . . . prohibitin pseudogene 20 . . . . . . . . . . . PHBP21 . . . prohibitin pseudogene 21 . . . . . . . . . . . PHC1 0.997152365464677 0.00284762897722825 5.55809508901463e-09 polyhomeotic homolog 1 FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Required for proper control of cellular levels of GMNN expression. {ECO:0000269|PubMed:23418308}.; DISEASE: Microcephaly 11, primary, autosomal recessive (MCPH11) [MIM:615414]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age- related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. {ECO:0000269|PubMed:23418308}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;aorta;thymus;cerebellum; . 0.48903 0.14669 0.04598748 57.47817882 1289.55749 6.76111 PHC1P1 . . . polyhomeotic homolog 1 pseudogene 1 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;cerebellum cortex;islets of Langerhans;colon;skin;retina;breast;uterus;whole body;lung;frontal lobe;epididymis;bone;placenta;liver;testis;spleen;kidney;brain;mammary gland; . . 0.10248 . . . . PHC2 0.205656047583874 0.794262576335213 8.13760809126222e-05 polyhomeotic homolog 2 FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.; . . myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;cerebral cortex;endometrium;oesophagus;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;nervous;islets of Langerhans;muscle;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; superior cervical ganglion; 0.68569 0.12463 -0.483123186 22.78249587 2175.91762 8.58997 PHC3 0.99995554091245 4.44590864616091e-05 1.0881871002281e-12 polyhomeotic homolog 3 FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. {ECO:0000269|PubMed:12167701}.; . . . . 0.79651 0.14981 -0.462894052 23.62585515 182.37895 2.93240 PHEX 0.999645685351575 0.000354314477572401 1.70852787210745e-10 phosphate regulating endopeptidase homolog, X-linked FUNCTION: Probably involved in bone and dentin mineralization and renal phosphate reabsorption.; . TISSUE SPECIFICITY: Lymphocytes and fetal brain; not in adult brain, placenta, skeletal muscle and pancreas; not in adult and fetal heart, lung, liver and kidney.; . . 0.61810 0.61623 -1.133409319 6.434300543 35.78853 1.07656 PHEX-AS1 . . . PHEX antisense RNA 1 . . . . . . . . . . . PHF1 0.999558759279796 0.000441239279138518 1.44106506437176e-09 PHD finger protein 1 FUNCTION: Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Involved in DNA damage response and is recruited at double-strand breaks (DSBs). Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex: it is however unclear whether recruitment of the PRC2 complex to H3K36me3 leads to enhance or inhibit H3K27me3 methylation mediated by the PRC2 complex. According to some reports, PRC2 recruitment by PHF1 promotes H3K27me3 and subsequent gene silencing by inducing spreading of PRC2 and H3K27me3 into H3K36me3 loci (PubMed:18285464 and PubMed:23273982). According to another report, PHF1 recruits the PRC2 complex at double-strand breaks (DSBs) and inhibits the activity of PRC2 (PubMed:23142980). Regulates p53/TP53 stability and prolonges its turnover: may act by specifically binding to a methylated from of p53/TP53. {ECO:0000269|PubMed:18086877, ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:18385154, ECO:0000269|PubMed:23142980, ECO:0000269|PubMed:23150668, ECO:0000269|PubMed:23273982}.; DISEASE: Note=A chromosomal aberration involving PHF1 may be a cause of endometrial stromal tumors. Translocation t(6;7)(p21;p22) with JAZF1. Translocation t(1;6)(p34;p21) with MEAF6. {ECO:0000269|PubMed:16397222, ECO:0000269|PubMed:22761769}.; TISSUE SPECIFICITY: Highest levels in heart, skeletal muscle, and pancreas, lower levels in brain, placenta, lung, liver and kidney.; . . 0.66215 0.14538 -0.334253673 30.70299599 126.42068 2.44907 PHF2 0.994132137165918 0.00586786150411262 1.32996985077728e-09 PHD finger protein 2 FUNCTION: Lysine demethylase that demethylates both histones and non-histone proteins. Enzymatically inactive by itself, and becomes active following phosphorylation by PKA: forms a complex with ARID5B and mediates demethylation of methylated ARID5B. Demethylation of ARID5B leads to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. PHF2 is recruited to trimethylated 'Lys-4' of histone H3 (H3K4me3) at rDNA promoters and promotes expression of rDNA. {ECO:0000269|PubMed:20129925, ECO:0000269|PubMed:21167174, ECO:0000269|PubMed:21532585}.; . TISSUE SPECIFICITY: Widely expressed, including in liver (at protein level). {ECO:0000269|PubMed:21532585}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;placenta;skeletal muscle;cerebellum; 0.45313 0.11119 -1.03432138 7.855626327 5090.05392 14.60736 PHF2P1 . . . PHD finger protein 2 pseudogene 1 . . . . . . . . . . . PHF2P2 . . . PHD finger protein 2 pseudogene 2 . . . . . . . . . . . PHF3 0.999469419864182 0.000530580135786283 3.13640359144942e-14 PHD finger protein 3 . . TISSUE SPECIFICITY: Ubiquitous. Expression is significantly reduced or lost in glioblastomas, glioblastoma cell lines, anaplastic astrocytomas, and astrocytomas. {ECO:0000269|PubMed:11856869}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;appendix;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.69088 0.09214 -0.802972206 12.09601321 757.35043 5.45391 PHF5A 0.849500693094142 0.147920334841389 0.00257897206446871 PHD finger protein 5A FUNCTION: Acts as a transcriptional regulator by binding to the GJA1/Cx43 promoter and enhancing its up-regulation by ESR1/ER- alpha. Also involved in pre-mRNA splicing. {ECO:0000269|PubMed:12234937}.; . . umbilical cord;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lung;trabecular meshwork;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;cerebellum; 0.25826 0.14896 0.145304857 63.81221986 . . PHF5CP . . . PHD finger protein 5C pseudogene . . . . . . . . . . . PHF5DP . . . PHD finger protein 5D pseudogene . . . . . . . . . . . PHF5EP . . . PHD finger protein 5E pseudogene . . . . . . . . . . . PHF5FP . . . PHD finger protein 5F pseudogene . . . . . . . . . . . PHF5GP . . . PHD finger protein 5G pseudogene . . . . . . . . . . . PHF5HP . . . PHD finger protein 5H pseudogene . . . . . . . . . . . PHF6 0.972400781120067 0.0275920249380131 7.19394191961717e-06 PHD finger protein 6 FUNCTION: Transcriptional regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription. {ECO:0000269|PubMed:23229552}.; DISEASE: Boerjeson-Forssman-Lehmann syndrome (BFLS) [MIM:301900]: A X-linked recessive disorder characterized by moderate to severe mental retardation, epilepsy, hypogonadism, hypometabolism, obesity with marked gynecomastia, swelling of subcutaneous tissue of the face, narrow palpebral fissure and large but not deformed ears. {ECO:0000269|PubMed:12415272}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12415272}.; sympathetic chain;colon;skin;bone marrow;uterus;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;blood;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;liver;duodenum;alveolus;cervix;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;medulla oblongata;fetal brain;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.75003 0.16306 -0.031067188 51.03798066 7.47388 0.27807 PHF7 0.0649138823166041 0.931977116291995 0.00310900139140052 PHD finger protein 7 FUNCTION: May play a role in spermatogenesis.; . TISSUE SPECIFICITY: Highly expressed in Sertoli cells, but not in germ cells in adult testis. Expression in embryonic testis is 30- times lower. Highly expressed in colon, spleen, white blood cells, pancreas, lung, liver, placenta and brain. Detected at lower levels in thymus, small intestine, ovary and kidney. {ECO:0000269|PubMed:11829468}.; unclassifiable (Anatomical System);medulla oblongata;heart;ovary;islets of Langerhans;colon;parathyroid;skin;retina;uterus;whole body;lung;placenta;visual apparatus;hippocampus;liver;testis;spleen;germinal center;kidney;brain;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09418 0.09987 0.238945317 69.20853975 124.2357 2.42533 PHF8 0.998239852588149 0.00176014569268908 1.71916235676486e-09 PHD finger protein 8 FUNCTION: Histone lysine demethylase with selectivity for the di- and monomethyl states that plays a key role cell cycle progression, rDNA transcription and brain development. Demethylates mono- and dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks. Involved in cell cycle progression by being required to control G1-S transition. Acts as a coactivator of rDNA transcription, by activating polymerase I (pol I) mediated transcription of rRNA genes. Required for brain development, probably by regulating expression of neuron-specific genes. Only has activity toward H4K20Me1 when nucleosome is used as a substrate and when not histone octamer is used as substrate. May also have weak activity toward dimethylated H3 'Lys-36' (H3K36Me2), however, the relevance of this result remains unsure in vivo. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: has weak activity toward H3K9Me2 in absence of H3K4me3, while it has high activity toward H3K9me2 when binding H3K4me3. {ECO:0000269|PubMed:19843542, ECO:0000269|PubMed:20023638, ECO:0000269|PubMed:20101266, ECO:0000269|PubMed:20208542, ECO:0000269|PubMed:20346720, ECO:0000269|PubMed:20421419, ECO:0000269|PubMed:20531378, ECO:0000269|PubMed:20548336, ECO:0000269|PubMed:20622853, ECO:0000269|PubMed:20622854}.; DISEASE: Mental retardation, X-linked, syndromic, Siderius type (MRXSSD) [MIM:300263]: A syndrome characterized by mild to borderline mental retardation with or without cleft lip/cleft palate. {ECO:0000269|PubMed:16199551, ECO:0000269|PubMed:17661819}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;lung;epididymis;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.48090 0.10114 -0.025608647 51.91672564 31.44976 0.99147 PHF10 0.0838841643103564 0.915698771279546 0.000417064410097765 PHD finger protein 10 FUNCTION: Involved in transcription activity regulation by chromatin remodeling. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron- specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;fovea centralis;skin;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;adrenal cortex;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.25781 0.10739 -0.427900189 25.14744043 8.44037 0.30895 PHF10P1 . . . PHD finger protein 10 pseudogene 1 . . . . . . . . . . . PHF11 1.76757700990619e-05 0.681003614592953 0.318978709636948 PHD finger protein 11 FUNCTION: Positive regulator of Th1-type cytokine gene expression. {ECO:0000269|PubMed:18405956}.; . TISSUE SPECIFICITY: Highly expressed in T and B-cells, as well as natural killer and mature dendritic cells. Expressed at higher levels in Th1 as compared to Th2 cells. Expressed at low levels in all normal tissues tested, including lung, testis, small intestine, breast, liver and placenta. {ECO:0000269|PubMed:18405956}.; smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;breast;pancreas;lung;adrenal gland;placenta;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;white blood cells; 0.09893 0.12660 -0.05129383 49.75819769 74.21424 1.79927 PHF12 0.999959675213551 4.03247855907325e-05 8.57926220836708e-13 PHD finger protein 12 FUNCTION: Acts as a transcriptional repressor. Involved in recruitment of functional SIN3A complexes to DNA. Represses transcription at least in part through the activity of an associated histone deacetylase (HDAC). May also repress transcription in a SIN3A-independent manner through recruitment of functional AES complexes to DNA. {ECO:0000269|PubMed:11390640, ECO:0000303|PubMed:11390640}.; . . unclassifiable (Anatomical System);lymph node;ovary;heart;tongue;muscle;colon;parathyroid;skin;skeletal muscle;retina;breast;uterus;bile duct;prostate;pancreas;lung;endometrium;thyroid;placenta;visual apparatus;alveolus;testis;head and neck;germinal center;brain;bladder;stomach; superior cervical ganglion; 0.76398 0.19435 -1.127956862 6.522764803 117.37226 2.35526 PHF13 0.931111283002542 0.0685415808989105 0.000347136098547826 PHD finger protein 13 FUNCTION: Modulates chromatin structure. Required for normal chromosome condensation during the early stages of mitosis. Required for normal chromosome separation during mitosis. {ECO:0000269|PubMed:19638409}.; . . . . 0.16824 0.12096 -0.426079032 25.36565228 53.89196 1.46408 PHF14 0.206539239599482 0.793444436435816 1.63239647020127e-05 PHD finger protein 14 . . . . . 0.53698 0.10653 -0.532670911 20.78320359 132.45351 2.50445 PHF19 0.995642238517627 0.00435774578019745 1.5702175485032e-08 PHD finger protein 19 FUNCTION: Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Probably involved in the transition from an active state to a repressed state in embryonic stem cells: acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting H3K36me3 histone demethylases NO66 or KDM2B, leading to demethylation of H3K36 and recruitment of the PRC2 complex that mediates H3K27me3 methylation, followed by de novo silencing. Recruits the PRC2 complex to CpG islands and contributes to embryonic stem cell self-renewal. Also binds dimethylated at 'Lys- 36' (H3K36me2). Isoform 1 and isoform 2 inhibit transcription from an HSV-tk promoter. {ECO:0000269|PubMed:15563832, ECO:0000269|PubMed:21143197, ECO:0000269|PubMed:23104054, ECO:0000269|PubMed:23160351}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in thymus, heart, lung and kidney. Isoform 2 is predominantly expressed in placenta, skeletal muscle and kidney, whereas isoform 1 is predominantly expressed in liver and peripheral blood leukocytes. Overexpressed in many types of cancers, including colon, skin, lung, rectal, cervical, uterus, liver cancers, in cell lines derived from different stages of melanoma and in glioma cell lines. {ECO:0000269|PubMed:15563832}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;oesophagus;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.43279 0.12253 0.020302773 55.60863411 63.74199 1.63734 PHF20 0.975739227580779 0.0242607636475354 8.77168547107780e-09 PHD finger protein 20 FUNCTION: Methyllysine-binding protein, component of the MOF histone acetyltransferase protein complex. Not required for maintaining the global histone H4 'Lys-16' acetylation (H4K16ac) levels or locus specific histone acetylation, but instead works downstream in transcriptional regulation of MOF target genes (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Contributes to methyllysine-dependent p53/TP53 stabilization and up-regulation after DNA damage. {ECO:0000250, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:22864287}.; . TISSUE SPECIFICITY: Expressed in heart, kidney, liver, lung, pancreas, placenta, spleen and testis. Not expressed in brain, skeletal muscle, colon, ovary, prostate, small intestine and thymus. Expressed in colon and ovary cancer cell lines while it is not expressed in the respective normal tissues. {ECO:0000269|PubMed:12097419}.; unclassifiable (Anatomical System);hypothalamus;skeletal muscle;uterus;breast;lung;nasopharynx;placenta;bone;visual apparatus;liver;testis;head and neck;germinal center;brain;stomach;thymus; amygdala;dorsal root ganglion;superior cervical ganglion;testis - interstitial;olfactory bulb;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.59735 0.13175 -0.552898813 19.86317528 939.79395 5.94357 PHF20L1 0.99991198433104 8.80156687250837e-05 2.35168357400863e-13 PHD finger protein 20-like 1 . . . lymphoreticular;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;thyroid;testis;dura mater;germinal center;bladder;pineal gland;brain;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;blood;lens;skeletal muscle;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;liver;head and neck;cervix;spleen;kidney;mammary gland;stomach;aorta; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.27164 0.10265 -1.374132436 4.429110639 91.22132 2.05428 PHF21A 0.999675486100741 0.000324513761327527 1.37931204208582e-10 PHD finger protein 21A FUNCTION: Component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it may act as a scaffold. Inhibits KDM1A-mediated demethylation of 'Lys-4' of histone H3 in vitro, suggesting a role in demethylation regulation. {ECO:0000269|PubMed:16140033}.; . TISSUE SPECIFICITY: Highly expressed in brain. Expressed at much lower level in other tissues. {ECO:0000269|PubMed:12032298}.; developmental;colon;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;lung;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;testis;white blood cells;whole blood;skeletal muscle; 0.45911 0.13081 -0.622676946 17.30950696 1807.75543 7.84684 PHF21B 0.914020956210128 0.0859537099016955 2.53338881765177e-05 PHD finger protein 21B . . . unclassifiable (Anatomical System);lung;visual apparatus;brain;pineal gland;retina;bone marrow; occipital lobe;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;skeletal muscle; 0.10851 . 0.88921411 89.24274593 708.32146 5.28646 PHF23 0.991271958267002 0.0087259473975497 2.09433544844594e-06 PHD finger protein 23 FUNCTION: Acts as a negative regulator of autophagy, through promoting ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that promotes autophagy in response to starvation or infecting bacteria. {ECO:0000269|PubMed:25484098}.; DISEASE: Note=A chromosomal aberration involving PHF23 is found in a patient with acute myeloid leukemia (AML). Translocation t(11;17)(p15;p13) with NUP98.; TISSUE SPECIFICITY: Widely expressed in human tissues and various cell lines. {ECO:0000269|PubMed:25484098}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;synovium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;cingulate cortex;cerebellum; 0.33406 0.10842 -0.359940251 28.93371078 26.5875 0.86066 PHF24 . . . PHD finger protein 24 . . . . . 0.19938 . -0.336073593 30.55555556 . . PHGDH 0.000436998677210205 0.962929912902011 0.0366330884207786 phosphoglycerate dehydrogenase . DISEASE: Phosphoglycerate dehydrogenase deficiency (PHGDHD) [MIM:601815]: An autosomal recessive inborn error of L-serine biosynthesis, clinically characterized by congenital microcephaly, psychomotor retardation, and seizures. {ECO:0000269|PubMed:11055895, ECO:0000269|PubMed:19235232}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Neu-Laxova syndrome 1 (NLS1) [MIM:256520]: A lethal, autosomal recessive multiple malformation syndrome characterized by ichthyosis, marked intrauterine growth restriction, microcephaly, short neck, limb deformities, hypoplastic lungs, edema, and central nervous system anomalies including lissencephaly, cerebellar hypoplasia and/or abnormal/agenesis of the corpus callosum. Abnormal facial features include severe proptosis with ectropion, hypertelorism, micrognathia, flattened nose, and malformed ears. {ECO:0000269|PubMed:24836451}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.24903 0.56183 -0.620857637 17.3566879 86.11185 1.98148 PHGR1 . . . proline/histidine/glycine-rich 1 . . . . . . . . . 76.21378 1.82996 PHIP 0.999999947701654 5.22983462395004e-08 1.10565889843483e-24 pleckstrin homology domain interacting protein FUNCTION: Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti- apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:12242307, ECO:0000269|PubMed:21834987}.; . TISSUE SPECIFICITY: Expressed in myeloma and epidermoid carcinoma cell lines. {ECO:0000269|PubMed:11018022}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;lung;nasopharynx;placenta;duodenum;kidney;stomach;aorta; superior cervical ganglion;skeletal muscle; 0.94541 0.10571 -1.238203625 5.490681765 2589.70314 9.52072 PHKA1 0.881287038362445 0.118712957614311 4.02324325814692e-09 phosphorylase kinase, alpha 1 (muscle) FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin.; DISEASE: Glycogen storage disease 9D (GSD9D) [MIM:300559]: A metabolic disorder characterized by slowly progressive, predominantly distal muscle weakness and atrophy. Clinical features include exercise intolerance with early fatigability, pain, cramps and occasionally myoglobinuria. {ECO:0000269|PubMed:12825073}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Muscle specific. Isoform 1 is predominant in vastus lateralis muscle. Isoform 2 predominates slightly in heart, and it predominates clearly in the other tissues tested.; unclassifiable (Anatomical System);lymphoreticular;ovary;heart;islets of Langerhans;colon;parathyroid;skeletal muscle;breast;pancreas;prostate;whole body;lung;bone;thyroid;placenta;hypopharynx;liver;head and neck;kidney;brain;stomach; . . 0.19048 -0.799052816 12.45576787 889.14986 5.81038 PHKA1-AS1 . . . PHKA1 antisense RNA 1 . . . . . . . . . . . PHKA1P1 . . . phosphorylase kinase, alpha 1 pseudogene 1 . . . . . . . . . . . PHKA2 0.908082279776674 0.0919177100094641 1.0213862316323e-08 phosphorylase kinase, alpha 2 (liver) FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin.; DISEASE: Glycogen storage disease 9A (GSD9A) [MIM:306000]: A metabolic disorder resulting in a mild liver glycogenosis with clinical symptoms that include hepatomegaly, growth retardation, muscle weakness, elevation of glutamate-pyruvate transaminase and glutamate-oxaloacetate transaminase, hypercholesterolemia, hypertriglyceridemia, and fasting hyperketosis. Two subtypes are known: type 1 or classic type with no phosphorylase kinase activity in liver or erythrocytes, and type 2 or variant type with no phosphorylase kinase activity in liver, but normal activity in erythrocytes. Unlike other glycogenosis diseases, glycogen storage disease type 9A is generally a benign condition. Patients improve with age and are often asymptomatic as adults. Accurate diagnosis is therefore also of prognostic interest. {ECO:0000269|PubMed:10330341, ECO:0000269|PubMed:17689125, ECO:0000269|PubMed:7549948, ECO:0000269|PubMed:7847371, ECO:0000269|PubMed:8733133, ECO:0000269|PubMed:8733134, ECO:0000269|PubMed:9600238}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in liver and other non-muscle tissues.; . . 0.11897 0.39190 -0.565865532 19.04930408 196.81218 3.03346 PHKA2-AS1 . . . PHKA2 antisense RNA 1 . . . . . . . . . . . PHKB 3.16119097774812e-10 0.999792045303077 0.00020795438080384 phosphorylase kinase, beta FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The beta chain acts as a regulatory unit and modulates the activity of the holoenzyme in response to phosphorylation.; DISEASE: Glycogen storage disease 9B (GSD9B) [MIM:261750]: A metabolic disorder characterized by hepatomegaly, only slightly elevated transaminases and plasma lipids, clinical improvement with increasing age, and remarkably no clinical muscle involvement. Biochemical observations suggest that this mild phenotype is caused by an incomplete holoenzyme that lacks the beta subunit, but that may possess residual activity. {ECO:0000269|PubMed:9402963}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;amygdala;heart;cartilage;urinary;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;placenta;hippocampus;head and neck;kidney;stomach;thymus; amygdala;dorsal root ganglion;subthalamic nucleus;medulla oblongata;testis - interstitial;superior cervical ganglion;thyroid;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.34561 0.21599 0.367380537 74.74050484 834.92029 5.65576 PHKBP1 . . . phosphorylase kinase, beta pseudogene 1 . . . . . . . . . . . PHKBP2 . . . phosphorylase kinase, beta pseudogene 2 . . . . . . . . . . . PHKG1 3.5805417364897e-10 0.170265637990262 0.829734361651684 phosphorylase kinase, gamma 1 (muscle) FUNCTION: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3 (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);amygdala;lymph node;ovary;cartilage;islets of Langerhans;colon;choroid;skin;skeletal muscle;greater omentum;lung;endometrium;placenta;visual apparatus;kidney;brain;mammary gland;stomach; parietal lobe;skeletal muscle; 0.17418 0.18710 -1.418232832 4.110639302 78.27585 1.86564 PHKG1P1 . . . phosphorylase kinase, gamma 1 pseudogene 1 . . . . . . . . . . . PHKG1P2 . . . phosphorylase kinase, gamma 1 pseudogene 2 . . . . . . . . . . . PHKG1P3 . . . phosphorylase kinase, gamma 1 pseudogene 3 . . . . . . . . . . . PHKG1P4 . . . phosphorylase kinase, gamma 1 pseudogene 4 . . . . . . . . . . . PHKG2 0.0216344941814238 0.974964721884212 0.00340078393436437 phosphorylase kinase, gamma 2 (testis) FUNCTION: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. May regulate glycogeneolysis in the testis. In vitro, phosphorylates PYGM (By similarity). {ECO:0000250, ECO:0000269|PubMed:10487978}.; DISEASE: Glycogen storage disease 9C (GSD9C) [MIM:613027]: A metabolic disorder manifesting in infancy with hepatomegaly, growth retardation, hypotonia, liver dysfunction, and elevated plasma aminotransferases and lipids. These symptoms improve with age in most cases; however, some patients may develop hepatic fibrosis or cirrhosis. {ECO:0000269|PubMed:12930917, ECO:0000269|PubMed:8896567, ECO:0000269|PubMed:9245685}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;amnion;cervix;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;parietal lobe;cerebellum; 0.18565 0.19614 -0.712684326 14.49634348 43.71616 1.25872 PHLDA1 0.166867882714649 0.771986339457612 0.0611457778277385 pleckstrin homology like domain family A member 1 FUNCTION: Seems to be involved in regulation of apoptosis. May be involved in detachment-mediated programmed cell death. May mediate apoptosis during neuronal development. May be involved in regulation of anti-apoptotic effects of IGF1. May be involved in translational regulation. {ECO:0000269|PubMed:11369516, ECO:0000269|PubMed:12738777}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in pancreas. Strongly expressed by benign melanocytic nevi, and progressively reduced expressed in primary and metastatic melanomas (at protein level). {ECO:0000269|PubMed:12384558, ECO:0000269|PubMed:12738777}.; lymphoreticular;ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;thyroid;bone;pituitary gland;bladder;brain;unclassifiable (Anatomical System);amygdala;cartilage;lacrimal gland;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;cervix;kidney; superior cervical ganglion;lung;trachea;ciliary ganglion;atrioventricular node; 0.33321 0.13380 . . 709.5326 5.29171 PHLDA2 0.0242596618306058 0.549645739020471 0.426094599148923 pleckstrin homology like domain family A member 2 FUNCTION: Plays a role in regulating placenta growth. May act via its PH domain that competes with other PH domain-containing proteins, thereby preventing their binding to membrane lipids (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in placenta and adult prostate gland. In placenta, it is present in all cells of the villous cytotrophoblast. The protein is absent in cells from hydatidiform moles. Hydatidiform mole is a gestation characterized by abnormal development of both fetus and trophoblast. The majority of hydatidiform moles are associated with an excess of paternal to maternal genomes and are likely to result from the abnormal expression of imprinted genes (at protein level). Expressed at low levels in adult liver and lung, and fetal liver. Expressed in adult brain and neuroblastoma, medullablastoma and glioblastoma cell lines. {ECO:0000269|PubMed:10594239, ECO:0000269|PubMed:10749982, ECO:0000269|PubMed:13129680, ECO:0000269|PubMed:15457853, ECO:0000269|PubMed:9328465}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; prostate;lung;placenta; 0.10016 . -0.09720619 46.20193442 386.39459 4.14011 PHLDA3 0.527854532202414 0.410704931295282 0.0614405365023038 pleckstrin homology like domain family A member 3 FUNCTION: p53/TP53-regulated repressor of Akt/AKT1 signaling. Represses AKT1 by preventing AKT1-binding to membrane lipids, thereby inhibiting AKT1 translocation to the cellular membrane and activation. Contributes to p53/TP53-dependent apoptosis by repressing AKT1 activity. Its direct transcription regulation by p53/TP53 may explain how p53/TP53 can negatively regulate AKT1. May act as a tumor suppressor. {ECO:0000269|PubMed:19203586}.; . TISSUE SPECIFICITY: Widely expressed with lowest expression in liver and spleen. {ECO:0000269|PubMed:10594239}.; . . 0.09384 0.11255 0.169169615 65.33380514 174.48823 2.87347 PHLDB1 0.81858015218857 0.181419845268456 2.54297438077426e-09 pleckstrin homology like domain family B member 1 . . . myocardium;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;brain;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;cerebral cortex;synovium;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;pancreas;lung;cornea;placenta;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;subthalamic nucleus;occipital lobe;thalamus;caudate nucleus; 0.17453 0.12156 -1.848467831 2.046473225 737.36936 5.39045 PHLDB2 0.0112157669847478 0.988781166895348 3.06611990395417e-06 pleckstrin homology like domain family B member 2 FUNCTION: Seems to be involved in the assembly of the postsynaptic apparatus. May play a role in acetyl-choline receptor (AChR) aggregation in the postsynaptic membrane (By similarity). {ECO:0000250, ECO:0000269|PubMed:12376540}.; . . myocardium;medulla oblongata;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;larynx;thyroid;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;breast;pancreas;lung;trabecular meshwork;placenta;liver;hypopharynx;amnion;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.12035 0.479438135 78.88063222 1475.77426 7.15675 PHLDB3 9.97221793547354e-17 0.00247786148345841 0.997522138516541 pleckstrin homology like domain family B member 3 . . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;parathyroid;skin;uterus;lung;bone;placenta;visual apparatus;testis;kidney;brain;bladder;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.21122 . 0.047806932 57.51946214 1046.89102 6.21079 PHLPP1 0.918153757180465 0.0818462053693984 3.74501366799313e-08 PH domain and leucine rich repeat protein phosphatase 1 FUNCTION: Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on 'Ser-473' of AKT2 and AKT3, 'Ser-660' of PRKCB and 'Ser-657' of PRKCA (PubMed:15808505, PubMed:17386267, PubMed:18162466). Isoform 2 seems to have a major role in regulating Akt signaling in hippocampal neurons (By similarity). Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of Akt triggers apoptosis and suppression of tumor growth. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation (PubMed:18162466). Dephosphorylates STK4 on 'Thr-387' leading to STK4 activation and apoptosis (PubMed:20513427). Dephosphorylates RPS6KB1 and is involved in regulation of cap-dependent translation (PubMed:21986499). Inhibits cancer cell proliferation and may act as a tumor suppressor (PubMed:19079341). Dephosphorylates RAF1 inhibiting its kinase activity (PubMed:24530606). May act as a negative regulator of K-Ras signaling in membrane rafts (By similarity). Involved in the hippocampus-dependent long-term memory formation (By similarity). Involved in circadian control by regulating the consolidation of circadian periodicity after resetting (By similarity). Involved in development and function of regulatory T cells (By similarity). {ECO:0000250|UniProtKB:Q8CHE4, ECO:0000250|UniProtKB:Q9WTR8, ECO:0000269|PubMed:15808505, ECO:0000269|PubMed:17386267, ECO:0000269|PubMed:18162466, ECO:0000269|PubMed:19079341, ECO:0000269|PubMed:21986499, ECO:0000269|PubMed:24530606}.; . TISSUE SPECIFICITY: In colorectal cancer tissue, expression is highest in the surface epithelium of normal colonic mucosa adjacent to the cancer tissue but is largely excluded from the crypt bases. Expression is lost or significantly decreased in 78% of tested tumors (at protein level). Ubiquitously expressed in non-cancerous tissues. {ECO:0000269|PubMed:15808505, ECO:0000269|PubMed:19079341}.; parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bone;testis;amniotic fluid;germinal center;ciliary body;brain;unclassifiable (Anatomical System);lymph node;heart;pineal body;spinal cord;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;cerebellum; whole brain;amygdala;thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;prefrontal cortex;caudate nucleus;pons;cingulate cortex;parietal lobe;cerebellum; 0.54156 0.14173 . . 564.11137 4.82169 PHLPP2 0.0157973198741475 0.984202304993629 3.75132223179812e-07 PH domain and leucine rich repeat protein phosphatase 2 FUNCTION: Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on 'Ser-473' of AKT1, 'Ser-660' of PRKCB isoform beta-II and 'Ser-657' of PRKCA. Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser- 473' of Akt triggers apoptosis and decreases cell proliferation. Also controls the phosphorylation of AKT3. Dephosphorylates STK4 on 'Thr-387' leading to STK4 activation and apoptosis (PubMed:20513427). Dephosphorylates RPS6KB1 and is involved in regulation of cap-dependent translation (PubMed:21986499). Inhibits cancer cell proliferation and may act as a tumor suppressor. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Dephosphorylates RAF1 inhibiting its kinase activity (PubMed:24530606). {ECO:0000269|PubMed:17386267, ECO:0000269|PubMed:18162466, ECO:0000269|PubMed:19079341, ECO:0000269|PubMed:20513427, ECO:0000269|PubMed:21986499, ECO:0000269|PubMed:24530606}.; . TISSUE SPECIFICITY: In colorectal cancer tissue, expression is highest in the surface epithelium of normal colonic mucosa adjacent to the cancer tissue but is largely excluded from the crypt bases. Expression is lost or significantly decreased in 80% of tested tumors (at protein level). {ECO:0000269|PubMed:19079341}.; ovary;adrenal medulla;colon;parathyroid;skin;retina;uterus;prostate;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;cerebellum; 0.51852 0.11202 -1.229158719 5.555555556 1578.91263 7.35263 PHOSPHO1 0.631109187622191 0.339083034101074 0.0298077782767352 phosphatase, orphan 1 FUNCTION: Phosphatase that has a high activity toward phosphoethanolamine (PEA) and phosphocholine (PCho). Involved in the generation of inorganic phosphate for bone mineralization.; . TISSUE SPECIFICITY: Expressed at sites of mineralization in bone and cartilage. Highly expressed in osteoblast cell line SaOS-2 which produces a mineralized matrix, but not in MG-63 cell line, which do not mineralize. {ECO:0000269|PubMed:15050893}.; unclassifiable (Anatomical System);uterus;lung;ovary;heart;placenta;liver;testis;spleen;skin; . 0.25438 0.11510 . . 66.98513 1.69174 PHOSPHO2 0.0155246829335628 0.69481663463707 0.289658682429367 phosphatase, orphan 2 FUNCTION: Phosphatase that has high activity toward pyridoxal 5'- phosphate (PLP). Also active at much lower level toward pyrophosphate, phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine, fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate.; . . unclassifiable (Anatomical System);uterus;prostate;lung;heart;bone;hippocampus;testis;kidney;skin; amygdala;superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion; 0.08974 . -0.007201372 53.19061099 28.2377 0.90556 PHOX2A 0.65257572600188 0.322315604788846 0.0251086692092736 paired like homeobox 2a FUNCTION: May be involved in regulating the specificity of expression of the catecholamine biosynthetic genes. Acts as a transcription activator/factor. Could maintain the noradrenergic phenotype.; DISEASE: Fibrosis of extraocular muscles, congenital, 2 (CFEOM2) [MIM:602078]: A congenital ocular motility disorder marked by restrictive ophthalmoplegia affecting extraocular muscles innervated by the oculomotor and/or trochlear nerves. It is clinically characterized by anchoring of the eyes in downward gaze, ptosis, and backward tilt of the head. Congenital fibrosis of extraocular muscles type 2 may result from the defective development of the oculomotor (nIII), trochlear (nIV) and abducens (nVI) cranial nerve nuclei. {ECO:0000269|PubMed:11600883}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;oesophagus;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;urinary;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;trigeminal ganglion; 0.33886 0.15644 . . 127.89938 2.46550 PHOX2B 0.850787952870986 0.146690481597983 0.00252156553103034 paired like homeobox 2b FUNCTION: Involved in the development of several major noradrenergic neuron populations, including the locus coeruleus. Transcription factor which could determine a neurotransmitter phenotype in vertebrates. Enhances second-messenger-mediated activation of the dopamine beta-hydrolase and c-fos promoters, and of several enhancers including cAMP-response element and serum- response element.; DISEASE: Neuroblastoma 2 (NBLST2) [MIM:613013]: A common neoplasm of early childhood arising from embryonic cells that form the primitive neural crest and give rise to the adrenal medulla and the sympathetic nervous system. {ECO:0000305|PubMed:15024693}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in neuroblastoma, brain and adrenal gland.; unclassifiable (Anatomical System);prostate;lung;whole body; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; 0.62870 0.28104 0.125076652 62.7388535 26.58296 0.86039 PHPT1 0.0043396321806158 0.666022988593417 0.329637379225967 phosphohistidine phosphatase 1 FUNCTION: Exhibits phosphohistidine phosphatase activity.; . TISSUE SPECIFICITY: Expressed abundantly in heart and skeletal muscle.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;cartilage;heart;spinal cord;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;amnion;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; heart;liver;skeletal muscle; 0.10189 . 0.128714042 63.19886766 118.18877 2.36443 PHRF1 0.948919011202068 0.0510809883340859 4.63846374226161e-10 PHD and ring finger domains 1 . . . lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;aorta; . . 0.11017 -1.584446832 3.125737202 1335.14975 6.86343 PHTF1 5.47464863886936e-18 0.0227349929040665 0.977265007095933 putative homeodomain transcription factor 1 FUNCTION: May play a role in transcription regulation.; . TISSUE SPECIFICITY: Widely expressed with highest levels in testis. {ECO:0000269|PubMed:10729229}.; unclassifiable (Anatomical System);islets of Langerhans;sympathetic chain;blood;skin;skeletal muscle;retina;bone marrow;pancreas;endometrium;thyroid;visual apparatus;liver;testis;spleen;germinal center;kidney;brain; dorsal root ganglion;testis - interstitial;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.16071 0.10954 -0.398573136 26.92852088 111.41413 2.29834 PHTF2 0.0249464272569149 0.974940094590668 0.000113478152417403 putative homeodomain transcription factor 2 FUNCTION: May play a role in transcription regulation.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;thyroid;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;cervix;head and neck;kidney;stomach;thymus; superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.17439 0.09950 -0.135838822 43.77211607 52.39692 1.43185 PHYH 1.80976025439547e-05 0.686039880960885 0.313942021436571 phytanoyl-CoA 2-hydroxylase FUNCTION: Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.; . TISSUE SPECIFICITY: Expressed in liver, kidney, and T-cells, but not in spleen, brain, heart, lung and skeletal muscle.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;stomach;peripheral nerve; superior cervical ganglion;fetal liver;thyroid;liver;ciliary ganglion;kidney;trigeminal ganglion;skeletal muscle; 0.06009 0.22937 0.619191319 83.36282142 487.77985 4.54684 PHYHD1 5.93053456347448e-10 0.0648452696880844 0.935154729718862 phytanoyl-CoA dioxygenase domain containing 1 FUNCTION: Isoform 1 has alpha-ketoglutarate-dependent dioxygenase activity. Does not show detectable activity towards fatty acid CoA thioesters. Is not expected to be active with phytanoyl CoA. Isoform 2 and isoform 3 probably lack enzyme activity. {ECO:0000269|PubMed:21530488}.; . . medulla oblongata;ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;blood;lens;pancreas;lung;nasopharynx;placenta;liver;spleen;kidney;mammary gland;stomach; atrioventricular node;kidney; 0.04063 0.05848 -0.047654689 50.22410946 2863.14914 10.12342 PHYHIP 0.873268767669363 0.125083659783314 0.0016475725473234 phytanoyl-CoA 2-hydroxylase interacting protein FUNCTION: Its interaction with PHYH suggests a role in the development of the central system.; . TISSUE SPECIFICITY: Highly expressed in the brain. {ECO:0000269|PubMed:10686344}.; unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;fovea centralis;choroid;lens;retina;uterus;optic nerve;whole body;lung;frontal lobe;placenta;macula lutea;hippocampus;testis;kidney;brain;stomach;cerebellum; whole brain;amygdala;occipital lobe;medulla oblongata;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.33731 0.14229 -0.60427181 17.74593064 78.14056 1.86428 PHYHIPL 0.402880316525568 0.588224860815252 0.00889482265918044 phytanoyl-CoA 2-hydroxylase interacting protein like FUNCTION: May play a role in the development of the central system. {ECO:0000250}.; . . . . 0.23151 0.11520 -0.161524709 41.6430762 11.01835 0.39881 PHYKPL 1.72748794347931e-10 0.0605085352636102 0.939491464563641 5-phosphohydroxy-L-lysine phospho-lyase FUNCTION: Catalyzes the pyridoxal-phosphate-dependent breakdown of 5-phosphohydroxy-L-lysine, converting it to ammonia, inorganic phosphate and 2-aminoadipate semialdehyde. {ECO:0000269|PubMed:22241472}.; DISEASE: Phosphohydroxylysinuria (PHLU) [MIM:615011]: A condition characterized by elevated phosphohydroxylysine in the urine. There is no clinical phenotype associated with this finding other than the urinary metabolites. {ECO:0000269|PubMed:23242558}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.13209 0.12187 0.088260113 60.56853031 393.90857 4.17249 PI3 0.00564031437143875 0.483049901785031 0.51130978384353 peptidase inhibitor 3 FUNCTION: Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;oesophagus;larynx;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);tongue;oral cavity;pharynx;blood;skeletal muscle;lung;visual apparatus;hypopharynx;liver;head and neck;cervix;kidney;stomach; superior cervical ganglion;trachea;tongue;ciliary ganglion;atrioventricular node;pons;whole blood;trigeminal ganglion;skin;tonsil;skeletal muscle;thymus; 0.35150 0.39584 0.571462851 81.99457419 362.69261 4.03370 PI4K2A 0.980219633327766 0.0197772065291233 3.16014311114584e-06 phosphatidylinositol 4-kinase type 2 alpha FUNCTION: Membrane-bound phosphatidylinositol-4 kinase (PI4- kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking and is required for prolonged survival of neurons. Besides, phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3). {ECO:0000269|PubMed:11279162, ECO:0000269|PubMed:16443754, ECO:0000269|PubMed:20388919, ECO:0000269|PubMed:23146885, ECO:0000269|PubMed:24675427, ECO:0000269|PubMed:25168678, ECO:0000305}.; . TISSUE SPECIFICITY: Widely expressed. Highest expression is observed in kidney, brain, heart, skeletal muscle, and placenta and lowest expression is observed in colon, thymus, and small intestine. {ECO:0000269|PubMed:11279162}.; . . 0.53922 . 0.549415813 81.38122199 145.91651 2.63201 PI4K2B 0.0426563496873728 0.951370045259079 0.00597360505354853 phosphatidylinositol 4-kinase type 2 beta FUNCTION: Together with PI4K2A and the type III PI4Ks (PIK4CA and PIK4CB) it contributes to the overall PI4-kinase activity of the cell. This contribution may be especially significant in plasma membrane, endosomal and Golgi compartments. The phosphorylation of phosphatidylinositol (PI) to PI4P is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3). Contributes to the production of InsP3 in stimulated cells and is likely to be involved in the regulation of vesicular trafficking. {ECO:0000269|PubMed:11923287}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11923287}.; ovary;colon;parathyroid;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;urinary;blood;skeletal muscle;bile duct;pancreas;lung;placenta;liver;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.14603 . -0.538132194 20.26421326 739.15628 5.39814 PI4KA 0.000804073363471932 0.999195926635876 6.51812988959285e-13 phosphatidylinositol 4-kinase alpha FUNCTION: Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol- 1,4,5,-trisphosphate. {ECO:0000269|PubMed:10101268, ECO:0000269|PubMed:23229899}.; . TISSUE SPECIFICITY: Expressed ubiquitously. Highest levels in placenta and brain. Little or no expression in lung, liver, pancreas, testis or leukocytes. {ECO:0000269|PubMed:10101268, ECO:0000269|PubMed:7961848}.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;iris;germinal center;brain;heart;cartilage;tongue;adrenal cortex;blood;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;muscle;bile duct;lung;adrenal gland;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus; whole brain;amygdala;medulla oblongata;subthalamic nucleus;occipital lobe;temporal lobe;prefrontal cortex;globus pallidus;caudate nucleus;pons;cingulate cortex;parietal lobe; 0.22216 0.18153 -4.02197819 0.182826138 222.15357 3.22375 PI4KAP1 . . . phosphatidylinositol 4-kinase alpha pseudogene 1 . . . . . . . . . . . PI4KAP2 . . . phosphatidylinositol 4-kinase alpha pseudogene 2 . . . ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;frontal lobe;thyroid;testis;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);heart;cerebellum cortex;tongue;islets of Langerhans;adrenal cortex;blood;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.20196 . . . . . PI4KB 0.998716210797651 0.00128378904118526 1.61164095867305e-10 phosphatidylinositol 4-kinase beta FUNCTION: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol- 1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation. Involved in Golgi-to-plasma membrane trafficking (By similarity). {ECO:0000250, ECO:0000269|PubMed:10559940, ECO:0000269|PubMed:12749687, ECO:0000269|PubMed:9405935}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in heart, skeletal muscle, pancreas, testis and ovary. Weakly expressed in liver. {ECO:0000269|PubMed:9020160, ECO:0000269|PubMed:9405935, ECO:0000269|PubMed:9405938}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.55384 0.15273 -0.822919685 11.76574664 68.21585 1.70981 PI15 0.00430939169683863 0.867452856234556 0.128237752068606 peptidase inhibitor 15 FUNCTION: Serine protease inhibitor which displays weak inhibitory activity against trypsin. {ECO:0000269|PubMed:8882727}.; . TISSUE SPECIFICITY: Weakly expressed. Expressed at low level in prostate, mammary gland, salivary gland and thyroid gland. {ECO:0000269|PubMed:11287197, ECO:0000269|PubMed:9473672}.; . . 0.85811 0.11009 0.238945317 69.20853975 46.37241 1.31246 PI16 4.4012998949913e-07 0.215344443847671 0.784655116022339 peptidase inhibitor 16 FUNCTION: Putative serine protease inhibitor. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in prostate, testis, ovary and intestine. Concentrates in prostate cancer patient's sera. {ECO:0000269|PubMed:15344909, ECO:0000269|PubMed:17062675}.; . . 0.19249 0.09759 0.420771676 77.15852795 1043.98291 6.20244 PIANP 0.619509239955918 0.378848699445235 0.00164206059884783 PILR alpha associated neural protein FUNCTION: Acts as a ligand for PILRA in neural tissues, where it may be involved in immune regulation. {ECO:0000269|PubMed:21241660}.; . TISSUE SPECIFICITY: Mainly expressed in adult brain and cerebellum. Weaker expression in fetal brain and virtually no expression in spleen, heart, kidney, liver and dorsal ganglion relative to brain. {ECO:0000269|PubMed:21241660}.; . . 0.26201 . 0.080983847 59.76055674 21.24177 0.71819 PIAS1 0.997024481652262 0.00297548777196083 3.05757771483391e-08 protein inhibitor of activated STAT 1 FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Together with PRMT1, may repress STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation (By similarity). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (By similarity). {ECO:0000250|UniProtKB:O88907, ECO:0000269|PubMed:14500712, ECO:0000269|PubMed:19136629, ECO:0000269|PubMed:21965678}.; . TISSUE SPECIFICITY: Expressed in numerous tissues with highest level in testis. {ECO:0000269|PubMed:11439351, ECO:0000269|PubMed:9177271}.; ovary;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pineal body;adrenal cortex;blood;lens;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;testis;ciliary ganglion;parietal lobe; 0.97113 0.31462 -0.514264485 21.41424864 13.97584 0.50700 PIAS2 0.997942260674644 0.00205772689006408 1.24352918704376e-08 protein inhibitor of activated STAT 2 FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulator in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and the PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity. Isoform PIAS2-beta, but not isoform PIAS2-alpha, promotes MDM2 sumoylation. Isoform PIAS2-alpha promotes PARK7 sumoylation. Isoform PIAS2-beta promotes NCOA2 sumoylation more efficiently than isoform PIAS2- alpha. Isoform PIAS2-alpha sumoylates PML at'Lys-65' and 'Lys- 160'. {ECO:0000269|PubMed:15920481, ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:22406621}.; . TISSUE SPECIFICITY: Mainly expressed in testis. Isoform 3 is expressed predominantly in adult testis, weakly in pancreas, embryonic testis and sperm, and at very low levels in other organs. {ECO:0000269|PubMed:11439351, ECO:0000269|PubMed:15301740, ECO:0000269|PubMed:9920921}.; unclassifiable (Anatomical System);medulla oblongata;ovary;hypothalamus;parathyroid;skin;retina;uterus;breast;pancreas;whole body;lung;frontal lobe;larynx;thyroid;hippocampus;pituitary gland;liver;testis;head and neck;spleen;brain;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;appendix;globus pallidus;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.98247 0.28737 -0.426079032 25.36565228 52.72409 1.43865 PIAS3 0.998174980398239 0.00182501032173213 9.280028649437e-09 protein inhibitor of activated STAT 3 FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway and the steroid hormone signaling pathway. Involved in regulating STAT3 signaling via inhibiting STAT3 DNA-binding and suppressing cell growth. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation (PubMed:21965678, PubMed:9388184). Sumoylates CCAR2 which promotes its interaction with SIRT1 (PubMed:25406032). Diminishes the sumoylation of ZFHX3 by preventing the colocalization of ZFHX3 with SUMO1 in the nucleus (PubMed:24651376). {ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24651376, ECO:0000269|PubMed:25406032, ECO:0000269|PubMed:9388184}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in most tissues except thymus and small intestine. Isoform 3 is expressed only in brain, heart, thymus, muscle, lung, testis, lactating breast and embryonic stem cells. {ECO:0000269|PubMed:9388184}.; . . 0.74798 0.22475 -0.664951379 15.91177164 362.00764 4.02752 PIAS4 0.994350817581458 0.00564845960405867 7.22814483457747e-07 protein inhibitor of activated STAT 4 FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53/TP53 pathway, the Wnt pathway and the steroid hormone signaling pathway. Involved in gene silencing. Mediates sumoylation of CEBPA, PARK7, HERC2, MYB, TCF4 and RNF168. In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. {ECO:0000269|PubMed:12511558, ECO:0000269|PubMed:12631292, ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:15831457, ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:22508508}.; . TISSUE SPECIFICITY: Highly expressed in testis and, at lower levels, in spleen, prostate, ovary, colon and peripheral blood leukocytes. {ECO:0000269|PubMed:11439351}.; medulla oblongata;ovary;colon;parathyroid;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;pancreas;lung;placenta;visual apparatus;hippocampus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;testis - interstitial;pons;atrioventricular node;skeletal muscle;prostate;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;cerebellum; 0.66120 0.16696 -0.686998355 15.26893135 43.31623 1.25042 PIBF1 4.97647085898113e-08 0.999570750212515 0.000429200022776239 progesterone immunomodulatory binding factor 1 FUNCTION: Isoform 1: Pericentriolar protein required to maintain mitotic spindle pole integrity (PubMed:21224392). Required for the centrosomal accumulation of PCM1 and the recruitment of centriolar satellite proteins such as BBS4. Via association with PCM1 may be involved in primary cilia formation (PubMed:23110211). Required for CEP63 centrosomal localization and its interaction with WDR62. Together with CEP63 promotes centriole duplication. Promotes the centrosomal localization of CDK2 (PubMed:26297806). {ECO:0000269|PubMed:21224392, ECO:0000269|PubMed:23110211, ECO:0000269|PubMed:26297806}.; DISEASE: Note=May be associated with microcephaly. {ECO:0000305|PubMed:26297806}.; TISSUE SPECIFICITY: Expressed at highest levels in testis. Moderate expression is detected in spleen, thymus, prostate, ovary, small intestine, and colon (PubMed:11935316). Expressed in the first trimester pregnancy decidua (PubMed:12516630). Localized to extravillous cytotrophoblast (at protein level). Also found in syncytiotrophoblast and part of the villous cytotrophoblast. Isoform 1 is expressed in first trimester and term villous trophoblast; trophoblast cells can additionally express other isoforms (PubMed:18817979). Overexpresed in solid tumors from stomach and uterus and in cells from ovary, cervical, breast, lymphoma and leukemia cancer (PubMed:25218441). {ECO:0000269|PubMed:11935316, ECO:0000269|PubMed:12516630, ECO:0000269|PubMed:18817979, ECO:0000305|PubMed:25218441}.; ovary;parathyroid;uterus;prostate;whole body;endometrium;cochlea;bone;thyroid;testis;germinal center;artery;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;skeletal muscle;lung;placenta;liver;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;pons; 0.34324 0.08500 0.42623145 77.29417315 637.11347 5.07850 PICALM 0.972083090436883 0.0279166063660434 3.03197073409767e-07 phosphatidylinositol binding clathrin assembly protein FUNCTION: Assembly protein recruiting clathrin and adapter protein complex 2 (AP2) to cell membranes at sites of coated-pit formation and clathrin-vesicle assembly. May be required to determine the amount of membrane to be recycled, possibly by regulating the size of the clathrin cage. Involved in AP2-dependent clathrin-mediated endocytosis at the neuromuscular junction. {ECO:0000269|PubMed:10436022}.; . TISSUE SPECIFICITY: Expressed in all tissues examined. {ECO:0000269|PubMed:8643484}.; myocardium;lymphoreticular;smooth muscle;ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;urinary;spinal cord;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;thymus; fetal liver;testis - interstitial;occipital lobe;adipose tissue;placenta;whole blood;parietal lobe; 0.97843 0.13037 -0.490397599 22.50530786 39.60281 1.16712 PICK1 0.555069205475041 0.444357085943587 0.000573708581371709 protein interacting with PRKCA 1 FUNCTION: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competetive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function. {ECO:0000269|PubMed:20403402}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;amniotic fluid;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);cartilage;lacrimal gland;islets of Langerhans;lens;breast;lung;placenta;macula lutea;hippocampus;liver;cervix;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;pons;atrioventricular node;trigeminal ganglion;parietal lobe; 0.23761 0.27035 -0.80269335 12.23755603 14.64711 0.52802 PID1 0.403719374100703 0.557775380726846 0.0385052451724512 phosphotyrosine interaction domain containing 1 FUNCTION: Increases proliferation of preadipocytes without affecting adipocytic differentiation. {ECO:0000269|PubMed:16815647}.; . TISSUE SPECIFICITY: Expressed in subcutaneous fat, heart, skeletal muscle, brain, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocyte. {ECO:0000269|PubMed:16815647}.; unclassifiable (Anatomical System);lung;larynx;bone;placenta;visual apparatus;liver;testis;colon;spleen;head and neck;brain; ciliary ganglion; 0.21329 0.10901 -0.337894035 30.37272942 30.57301 0.97227 PIDD1 . . . p53-induced death domain protein 1 FUNCTION: Promotes apoptosis downstream of the tumor suppressor as component of the DNA damage/stress response pathway that connects p53/TP53 to apoptosis. Associates with NEMO/IKBKG and RIP1 and enhances sumoylation and ubiquitination of NEMO/IKBKG which is important for activation of the transcription factor NF-kappa-B. Associates with CASP2/caspase-2 and CRADD/RAIDD, and induces activation of CASP2 which an important regulator in apoptotic pathways. {ECO:0000269|PubMed:10973264, ECO:0000269|PubMed:15073321, ECO:0000269|PubMed:16360037}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10825539}.; . . 0.12054 0.10590 -1.383523256 4.358339231 . . PIEZO1 0.535969010144802 0.405692826785737 0.0583381630694615 piezo type mechanosensitive ion channel component 1 FUNCTION: Pore-forming subunit of a mechanosensitive non-specific cation channel (PubMed:23479567, PubMed:23695678). Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium. Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling (PubMed:20016066). In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing. Acts as shear-stress sensor that promotes endothelial cell organization and alignment in the direction of blood flow through calpain activation (PubMed:25119035). Plays a key role in blood vessel formation and vascular structure in both development and adult physiology (By similarity). {ECO:0000250|UniProtKB:E2JF22, ECO:0000269|PubMed:20016066, ECO:0000269|PubMed:23479567, ECO:0000269|PubMed:23695678, ECO:0000269|PubMed:25119035}.; DISEASE: Dehydrated hereditary stomatocytosis with or without pseudohyperkalemia and/or perinatal edema (DHS) [MIM:194380]: An autosomal dominant hemolytic anemia characterized by primary erythrocyte dehydration. DHS erythrocytes exhibit decreased total cation and potassium content that are not accompanied by a proportional net gain of sodium and water. DHS patients typically exhibit mild to moderate compensated hemolytic anemia, with an increased erythrocyte mean corpuscular hemoglobin concentration and a decreased osmotic fragility, both of which reflect cellular dehydration. Patients may also show perinatal edema and pseudohyperkalemia due to loss of potassium from red cells stored at room temperature. A minor proportion of red cells appear as stomatocytes on blood films. Complications such as splenomegaly and cholelithiasis, resulting from increased red cell trapping in the spleen and elevated bilirubin levels, respectively, may occur. The course of DHS is frequently associated with iron overload, which may lead to hepatosiderosis. {ECO:0000269|PubMed:22529292, ECO:0000269|PubMed:23479567, ECO:0000269|PubMed:23487776, ECO:0000269|PubMed:23581886, ECO:0000269|PubMed:23695678, ECO:0000269|PubMed:23973043}. Note=The disease is caused by mutations affecting the gene represented in this entry. All disease-causing mutations characterized so far produce a gain-of- function phenotype, mutated channels exhibiting increased cation transport in erythroid cells, that could be due to slower channel inactivation rate compared to the wild-type protein.; TISSUE SPECIFICITY: Expressed in numerous tissues. In normal brain, expressed exclusively in neurons, not in astrocytes. In Alzheimer disease brains, expressed in about half of the activated astrocytes located around classical senile plaques. In Parkinson disease substantia nigra, not detected in melanin-containing neurons nor in activated astrocytes. Expressed in erythrocytes (at protein level). {ECO:0000269|PubMed:16854388, ECO:0000269|PubMed:22529292, ECO:0000269|PubMed:23479567}.; smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;blood;cerebrum;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; prostate;tumor;white blood cells; 0.27550 . 3.747372954 99.59896202 9550.40686 21.12347 PIEZO1P1 . . . piezo type mechanosensitive ion channel component 1 pseudogene 1 . . . . . . . . . . . PIEZO1P2 . . . piezo type mechanosensitive ion channel component 1 pseudogene 2 . . . . . . . . . . . PIEZO2 0.603955312622787 0.396028967982347 1.57193948657719e-05 piezo type mechanosensitive ion channel component 2 FUNCTION: Component of a mechanosensitive channel required for rapidly adapting mechanically activated (MA) currents. Required for Merkel-cell mechanotransduction. Plays a major role in light- touch mechanosensation. {ECO:0000250|UniProtKB:Q8CD54}.; DISEASE: Arthrogryposis, distal, 5 (DA5) [MIM:108145]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA5 features include ocular abnormalities, typically ptosis, ophthalmoplegia and/or strabismus, in addition to contractures of the skeletal muscles. Some patients have pulmonary hypertension as a result of restrictive lung disease. {ECO:0000269|PubMed:23487782}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Arthrogryposis, distal, 3 (DA3) [MIM:114300]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA3 features include short stature and cleft palate. {ECO:0000269|PubMed:24726473}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Marden-Walker syndrome (MWKS) [MIM:248700]: A syndrome characterized by a mask-like face with blepharophimosis, micrognathia, cleft or high-arched palate, low-set ears, congenital joint contractures, kyphoscoliosis, pectus excavatum or carinatum, and arachnodactyly. Additional features include decreased muscular mass, failure to thrive, renal anomalies, hypoplastic corpus callosum, cerebellar vermis hypoplasia, enlarged cisterna magna, and psychomotor retardation. {ECO:0000269|PubMed:24726473}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;cartilage;colon;blood;lens;skin;uterus;prostate;whole body;lung;frontal lobe;cerebral cortex;visual apparatus;hippocampus;liver;testis;spleen;brain; dorsal root ganglion;medulla oblongata;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.48817 0.10601 . . 9123.18224 20.76481 PIF1 7.57989172819851e-12 0.0683297944852686 0.931670205507152 PIF1 5'-to-3' DNA helicase FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Possesses an intrinsic strand annealing activity. {ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:16522649, ECO:0000269|PubMed:17172855, ECO:0000269|PubMed:17827721, ECO:0000269|PubMed:18835853, ECO:0000269|PubMed:19700773, ECO:0000269|PubMed:20524933, ECO:0000269|PubMed:23657261}.; . TISSUE SPECIFICITY: Weak ubiquitous expression.; unclassifiable (Anatomical System);heart;ovary;colon;blood;skin;uterus;prostate;lung;placenta;trabecular meshwork;liver;testis;spleen;cervix;kidney;germinal center; dorsal root ganglion;testis - interstitial;superior cervical ganglion;temporal lobe;adrenal cortex;atrioventricular node;pons;skin;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.36580 0.11532 0.558509856 81.67020524 812.20188 5.60542 PIFO 7.54735435611498e-05 0.513249739367118 0.486674787089321 primary cilia formation FUNCTION: During primary cilia disassembly, involved in cilia disassembly. Required specifically to control cilia retraction as well as the liberation and duplication of the basal body/centrosome. May act by stimulating AURKA activity at the basal body in a cell cycle-dependent manner. {ECO:0000269|PubMed:20643351}.; . . . . 0.05344 . 0.3032669 72.009908 286.96298 3.62929 PIGA 0.916789461610083 0.0826505509846934 0.000559987405223248 phosphatidylinositol glycan anchor biosynthesis class A FUNCTION: Necessary for the synthesis of N-acetylglucosaminyl- phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis.; DISEASE: Paroxysmal nocturnal hemoglobinuria 1 (PNH1) [MIM:300818]: A disorder characterized by hemolytic anemia with hemoglobinuria, thromboses in large vessels, and a deficiency in hematopoiesis. Red blood cell breakdown with release of hemoglobin into the urine is manifested most prominently by dark-colored urine in the morning. {ECO:0000269|PubMed:10087994, ECO:0000269|PubMed:12037021, ECO:0000269|PubMed:8167330, ECO:0000269|PubMed:8306954, ECO:0000269|PubMed:8500164}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Multiple congenital anomalies-hypotonia-seizures syndrome 2 (MCAHS2) [MIM:300868]: An X-linked recessive developmental disorder characterized by dysmorphic features, neonatal hypotonia, myoclonic seizures, and variable congenital anomalies involving the central nervous, cardiac, and urinary systems. Most affected individuals die in infancy. {ECO:0000269|PubMed:22305531, ECO:0000269|PubMed:24259184, ECO:0000269|PubMed:24259288, ECO:0000269|PubMed:24706016}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.12345 0.22579 0.237127192 68.98443029 78.77931 1.87487 PIGAP1 . . . phosphatidylinositol glycan anchor biosynthesis class A pseudogene 1 . . . . . . . . . . . PIGB 0.000232191988748325 0.980559747674234 0.0192080603370175 phosphatidylinositol glycan anchor biosynthesis class B FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-GlcN-acyl-PI during GPI precursor assembly. {ECO:0000269|PubMed:8861954}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;lens;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.04829 0.09848 . . 2022.03602 8.27282 PIGBOS1 . . . PIGB opposite strand 1 . . . . . . . . . . . PIGC 0.000110183266434322 0.370070689812847 0.629819126920719 phosphatidylinositol glycan anchor biosynthesis class C FUNCTION: Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.; . . ovary;salivary gland;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;breast;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;ciliary ganglion; 0.31329 0.15726 0.016664174 55.21939137 4111.48839 12.73457 PIGCP1 . . . phosphatidylinositol glycan anchor biosynthesis class C pseudogene 1 . . . . . . . . . . . PIGCP2 . . . phosphatidylinositol glycan anchor biosynthesis class C pseudogene 2 . . . . . . . . . . . PIGF 0.000909040072288399 0.569434375128209 0.429656584799503 phosphatidylinositol glycan anchor biosynthesis class F FUNCTION: Involved in GPI-anchor biosynthesis through the transfer of ethanolamine phosphate to the third mannose of GPI. {ECO:0000250}.; . . myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;endometrium;cochlea;bone;iris;pituitary gland;testis;dura mater;germinal center;spinal ganglion;brain;artery;unclassifiable (Anatomical System);amygdala;meninges;cartilage;heart;lacrimal gland;islets of Langerhans;blood;skeletal muscle;bile duct;breast;pancreas;pia mater;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; testis - interstitial;superior cervical ganglion;spinal cord;testis;ciliary ganglion; 0.64749 0.14763 0.327131069 73.27199811 67.3964 1.69962 PIGFP1 . . . phosphatidylinositol glycan anchor biosynthesis class F pseudogene 1 . . . . . . . . . . . PIGFP2 . . . phosphatidylinositol glycan anchor biosynthesis class F pseudogene 2 . . . . . . . . . . . PIGFP3 . . . phosphatidylinositol glycan anchor biosynthesis class F pseudogene 3 . . . . . . . . . . . PIGG 8.77510701005957e-07 0.980401606179858 0.0195975163094412 phosphatidylinositol glycan anchor biosynthesis class G FUNCTION: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose. {ECO:0000269|PubMed:15632136}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; amygdala; 0.20218 0.12223 1.787621418 96.8742628 4105.76864 12.71793 PIGH 0.0698815809187974 0.738560814727904 0.191557604353298 phosphatidylinositol glycan anchor biosynthesis class H FUNCTION: Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach;peripheral nerve;thymus; . 0.25154 0.12528 -0.229483771 36.86010852 10.136 0.36970 PIGHP1 . . . phosphatidylinositol glycan anchor biosynthesis class H pseudogene 1 . . . . . . . . . . . PIGK 0.000544787618840002 0.972136318385087 0.0273188939960728 phosphatidylinositol glycan anchor biosynthesis class K FUNCTION: Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein.; . . unclassifiable (Anatomical System);lymph node;hypothalamus;blood;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;pancreas;prostate;optic nerve;lung;endometrium;placenta;macula lutea;visual apparatus;testis;cervix;spinal ganglion;brain;stomach;peripheral nerve; amygdala;dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12589 0.11980 -0.315847836 31.68789809 835.51754 5.65985 PIGL 3.55118862990776e-05 0.590656061368443 0.409308426745258 phosphatidylinositol glycan anchor biosynthesis class L FUNCTION: Involved in the second step of GPI biosynthesis. De-N- acetylation of N-acetylglucosaminyl-phosphatidylinositol.; DISEASE: Coloboma, congenital heart disease, ichthyosiform dermatosis, mental retardation and ear anomalies syndrome (CHIME) [MIM:280000]: An extremely rare autosomal recessive multisystem disorder clinically characterized by colobomas, congenital heart defects, migratory ichthyosiform dermatosis, mental retardation, and ear anomalies including conductive hearing loss. Other clinical features include distinctive facial features, abnormal growth, genitourinary abnormalities, seizures, and feeding difficulties. {ECO:0000269|PubMed:22444671}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;ovary;sympathetic chain;colon;parathyroid;skin;uterus;pancreas;prostate;optic nerve;lung;bone;thyroid;placenta;liver;testis;spleen;kidney;brain;stomach;cerebellum; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07224 0.07185 -0.005381972 53.50908233 40.09032 1.17818 PIGM 0.000916857647096851 0.571293607727458 0.427789534625445 phosphatidylinositol glycan anchor biosynthesis class M FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly. {ECO:0000269|PubMed:11226175}.; DISEASE: Glycosylphosphatidylinositol deficiency (GPID) [MIM:610293]: Autosomal recessive trait that results in a propensity to venous thrombosis and seizures. Deficiency is due to a point mutation in the regulatory sequences of PIGM that disrupts binding of the transcription factor SP1 to its cognate promoter motif, leading to a strong reduction of expression. {ECO:0000269|PubMed:16767100}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.09949 0.10244 -0.26993514 34.59542345 715.74684 5.31053 PIGN 9.02060283775279e-16 0.0332679436507233 0.966732056349276 phosphatidylinositol glycan anchor biosynthesis class N FUNCTION: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor (By similarity). May act as suppressor of replication stress and chromosome missegregation. {ECO:0000250, ECO:0000269|PubMed:23446422}.; DISEASE: Multiple congenital anomalies-hypotonia-seizures syndrome 1 (MCAHS1) [MIM:614080]: An autosomal recessive disorder characterized by neonatal hypotonia, lack of psychomotor development, seizures, dysmorphic features, and variable congenital anomalies involving the cardiac, urinary, and gastrointestinal systems. Most affected individuals die before 3 years of age. {ECO:0000269|PubMed:21493957}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;bone;thyroid;testis;brain;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;pineal body;oral cavity;adrenal cortex;blood;lens;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;mammary gland;stomach; spinal cord;parietal lobe; 0.21776 0.10642 -0.571310997 19.01391838 388.69127 4.15280 PIGO 1.12529315374815e-06 0.986091838835348 0.0139070358714979 phosphatidylinositol glycan anchor biosynthesis class O FUNCTION: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI third mannose which links the GPI-anchor to the C-terminus of the proteins by an amide bond (By similarity). {ECO:0000250}.; DISEASE: Hyperphosphatasia with mental retardation syndrome 2 (HPMRS2) [MIM:614749]: An autosomal recessive form of intellectual disability characterized by facial dysmorphism, brachytelephalangy, and persistent elevated serum alkaline phosphatase (hyperphosphatasia). Some patients may have additional features, such as cardiac septal defects or seizures. {ECO:0000269|PubMed:22683086}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;urinary;lens;pancreas;lung;visual apparatus;duodenum;spleen;kidney;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.33692 0.09145 -1.348453925 4.60603916 113.47021 2.31875 PIGP 0.000394928585804372 0.399554219154112 0.600050852260083 phosphatidylinositol glycan anchor biosynthesis class P FUNCTION: Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;umbilical cord;colon;parathyroid;skin;uterus;prostate;whole body;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;urinary;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;liver;alveolus;spleen;stomach; dorsal root ganglion;testis - interstitial;adrenal gland;testis;ciliary ganglion; 0.12461 0.12410 0.549415813 81.38122199 990.34759 6.06659 PIGPP1 . . . phosphatidylinositol glycan anchor biosynthesis class P pseudogene 1 . . . . . . . . . . . PIGPP2 . . . phosphatidylinositol glycan anchor biosynthesis class P pseudogene 2 . . . . . . . . . . . PIGPP3 . . . phosphatidylinositol glycan anchor biosynthesis class P pseudogene 3 . . . . . . . . . . . PIGPP4 . . . phosphatidylinositol glycan anchor biosynthesis class P pseudogene 4 . . . . . . . . . . . PIGQ 3.38787210295676e-10 0.165214870006706 0.834785129654507 phosphatidylinositol glycan anchor biosynthesis class Q FUNCTION: Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.; . . ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12183 0.14652 0.07895234 59.21207832 128.11911 2.46745 PIGQP1 . . . phosphatidylinositol glycan anchor biosynthesis class Q pseudogene 1 . . . . . . . . . . . PIGR 0.650095686646365 0.34985263744906 5.16759045747435e-05 polymeric immunoglobulin receptor FUNCTION: This receptor binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment.; . . unclassifiable (Anatomical System);breast;lung;lacrimal gland;larynx;liver;colon;head and neck;mammary gland;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;trachea;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09106 0.19677 -0.416983034 25.82566643 2492.75607 9.31299 PIGS 0.0799524483019955 0.917826790583454 0.00222076111455028 phosphatidylinositol glycan anchor biosynthesis class S FUNCTION: Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates. {ECO:0000269|PubMed:11483512}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;larynx;bone;thyroid;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.20475 0.12205 0.088260113 60.56853031 442.39756 4.37809 PIGT 4.65840286191537e-12 0.0975391572094262 0.902460842785915 phosphatidylinositol glycan anchor biosynthesis class T FUNCTION: Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates. {ECO:0000269|PubMed:11483512}.; DISEASE: Multiple congenital anomalies-hypotonia-seizures syndrome 3 (MCAHS3) [MIM:615398]: An autosomal recessive syndrome characterized by distinct facial features, intellectual disability, hypotonia and seizures, in combination with abnormal skeletal, endocrine, and ophthalmologic findings including impaired vision, as well as abnormal motility of the eyes. {ECO:0000269|PubMed:23636107}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Paroxysmal nocturnal hemoglobinuria 2 (PNH2) [MIM:615399]: A disorder characterized by hemolytic anemia with hemoglobinuria, thromboses in large vessels, and a deficiency in hematopoiesis. Red blood cell breakdown with release of hemoglobin into the urine is manifested most prominently by dark-colored urine in the morning. {ECO:0000269|PubMed:23733340}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . medulla oblongata;ovary;adrenal medulla;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;cerebellum; testis; 0.17487 0.11427 -0.154246007 42.22694032 479.40953 4.51909 PIGU 0.813069113456619 0.186732528996757 0.000198357546624254 phosphatidylinositol glycan anchor biosynthesis class U FUNCTION: Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI. {ECO:0000269|PubMed:12802054}.; . . ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;retina;uterus;prostate;frontal lobe;cerebral cortex;endometrium;synovium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;lung;cornea;placenta;visual apparatus;liver;amnion;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;cerebellum; 0.17799 0.11142 -0.402212257 26.7338995 75.12131 1.81375 PIGUP1 . . . phosphatidylinositol glycan anchor biosynthesis class U pseudogene 1 . . . . . . . . . . . PIGV 7.2042376998992e-06 0.487458523629169 0.512534272133131 phosphatidylinositol glycan anchor biosynthesis class V FUNCTION: Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly. {ECO:0000269|PubMed:15623507, ECO:0000269|PubMed:15720390}.; DISEASE: Hyperphosphatasia with mental retardation syndrome 1 (HPMRS1) [MIM:239300]: A severe syndrome characterized by elevated serum alkaline phosphatase, severe mental retardation, seizures, hypotonia, facial dysmorphism, and hypoplastic terminal phalanges. {ECO:0000269|PubMed:20802478}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;lung;placenta;macula lutea;alveolus;spleen;cervix;kidney;stomach; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.35504 . -0.402212257 26.7338995 53.65386 1.45879 PIGW 5.93368987083235e-07 0.251838076749406 0.748161329881607 phosphatidylinositol glycan anchor biosynthesis class W FUNCTION: Required for the transport of GPI-anchored proteins to the plasma membrane (PubMed:24367057). Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually removed soon after the attachment of GPIs to proteins (By similarity). {ECO:0000250|UniProtKB:Q7TSN4, ECO:0000269|PubMed:24367057}.; DISEASE: Hyperphosphatasia with mental retardation syndrome 5 (HPMRS5) [MIM:616025]: An autosomal recessive neurologic disorder characterized by developmental delay, mental retardation, tonic seizures associated with hypsarrhythmia, dysmorphic facial features, and elevated serum alkaline phosphatase. {ECO:0000269|PubMed:24367057}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);prostate;pancreas;lung;islets of Langerhans;liver;testis;colon;spleen;brain;skin;stomach; . 0.34399 0.08193 -0.025608647 51.91672564 428.81227 4.32487 PIGX . . . phosphatidylinositol glycan anchor biosynthesis class X FUNCTION: Essential component of glycosylphosphatidylinositol- mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the mannosyltransferase PIGM (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;whole body;optic nerve;testis;germinal center;brain;amygdala;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;blood;lens;lung;placenta;macula lutea;liver;spleen;kidney;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;trigeminal ganglion; 0.02329 0.07615 0.503505267 79.88912479 283.28756 3.60375 PIGY 0.106390613184656 0.591792553766322 0.301816833049022 phosphatidylinositol glycan anchor biosynthesis class Y FUNCTION: Component of the GPI-GlcNAc transferase (GPI-GnT) complex in the endoplasmic reticulum, a complex that catalyzes transfer of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the first step in the production of GPI- anchors for cell surface proteins. May act by regulating the catalytic subunit PIGA. {ECO:0000269|PubMed:16162815}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;amnion;kidney;stomach; . . . 0.191216164 66.57230479 16.03874 0.56731 PIGZ 0.000159853219090366 0.675896021628682 0.323944125152228 phosphatidylinositol glycan anchor biosynthesis class Z FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to some trimannosyl-GPIs during GPI precursor assembly. The presence of a fourth mannose in GPI is facultative and only scarcely detected, suggesting that it only exists in some tissues. {ECO:0000269|PubMed:15208306}.; . TISSUE SPECIFICITY: Widely expressed at low level, with highest level in brain and colon. {ECO:0000269|PubMed:15208306}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;optic nerve;lung;placenta;thyroid;macula lutea;pituitary gland;head and neck;brain;stomach; . 0.05154 0.09731 0.293954043 71.62066525 1400.69033 6.99703 PIH1D1 0.087951252701366 0.902853730148272 0.00919501715036258 PIH1 domain containing 1 FUNCTION: Involved in the assembly of C/D box small nucleolar ribonucleoprotein (snoRNP) particles (PubMed:17636026). Recruits the SWI/SNF complex to the core promoter of rRNA genes and enhances pre-rRNA transcription (PubMed:22368283, PubMed:24036451). Mediates interaction of TELO2 with the R2TP complex which is necessary for the stability of MTOR and SMG1 (PubMed:20864032). Positively regulates the assembly and activity of the mTORC1 complex (PubMed:24036451). {ECO:0000269|PubMed:17636026, ECO:0000269|PubMed:20864032, ECO:0000269|PubMed:22368283, ECO:0000269|PubMed:24036451}.; . TISSUE SPECIFICITY: Expressed at low levels in normal mammary epithelial cells (at protein level) (PubMed:24036451). Highest expression in lung, leukocyte and placenta. Expressed at lower levels in brain, prostate, colon, heart, small intestine, liver, ovary, pancreas, skeletal muscle, spleen, testis and thymus (PubMed:21078300). {ECO:0000269|PubMed:21078300, ECO:0000269|PubMed:24036451}.; myocardium;smooth muscle;ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;frontal lobe;endometrium;bone;pituitary gland;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;thymus; whole brain;skeletal muscle;cingulate cortex;cerebellum; 0.13435 0.10440 0.861712133 88.6883699 999.78308 6.08999 PIH1D2 0.000130201269552391 0.631410854977673 0.368458943752775 PIH1 domain containing 2 . . . unclassifiable (Anatomical System);medulla oblongata;colon;blood;vein;bone marrow;breast;bile duct;uterus;lung;nasopharynx;placenta;testis;spleen;kidney; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; 0.10684 . 0.637604436 83.77565464 388.63584 4.15222 PIH1D3 0.814438563515254 0.181077251036234 0.00448418544851178 PIH1 domain containing 3 FUNCTION: Plays a role in cytoplasmic pre-assembly of axonemal dynein. {ECO:0000250|UniProtKB:Q3KNI6}.; . TISSUE SPECIFICITY: Expressed in testis, small intestine, prostate, adrenal gland, spleen, lung, bladder, breast and ovary. {ECO:0000269|PubMed:12601173}.; . . . . 0.301449681 71.80938901 6.16983 0.23285 PIK3AP1 0.999656618843573 0.000343380998135597 1.58291351515805e-10 phosphoinositide-3-kinase adaptor protein 1 FUNCTION: Signaling adapter that contributes to B-cell development by linking B-cell receptor (BCR) signaling to the phosphoinositide 3-kinase (PI3K)-Akt signaling pathway. Has a complementary role to the BCR coreceptor CD19, coupling BCR and PI3K activation by providing a docking site for the PI3K subunit PIK3R1. Alternatively, links Toll-like receptor (TLR) signaling to PI3K activation, a process preventing excessive inflammatory cytokine production. Also involved in the activation of PI3K in natural killer cells. May be involved in the survival of mature B-cells via activation of REL. {ECO:0000269|PubMed:15893754}.; . TISSUE SPECIFICITY: Expressed in natural killer (NK) cells. {ECO:0000269|PubMed:18337558}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;frontal lobe;bone;thyroid;testis;germinal center;spinal ganglion;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;breast;pancreas;lung;adrenal gland;placenta;macula lutea;liver;spleen;kidney;stomach;thymus; . 0.18465 0.10694 0.04598748 57.47817882 4023.54992 12.56295 PIK3C2A 0.14870309003261 0.851296909949731 1.76589635278487e-11 phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 alpha FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. Has a role in several intracellular trafficking events. Functions in insulin signaling and secretion. Required for translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane and glucose uptake in response to insulin- mediated RHOQ activation. Regulates insulin secretion through two different mechanisms: involved in glucose-induced insulin secretion downstream of insulin receptor in a pathway that involves AKT1 activation and TBC1D4/AS160 phosphorylation, and participates in the late step of insulin granule exocytosis probably in insulin granule fusion. Synthesizes PtdIns3P in response to insulin signaling. Functions in clathrin-coated endocytic vesicle formation and distribution. Regulates dynamin- independent endocytosis, probably by recruiting EEA1 to internalizing vesicles. In neurosecretory cells synthesizes PtdIns3P on large dense core vesicles. Participates in calcium induced contraction of vascular smooth muscle by regulating myosin light chain (MLC) phosphorylation through a mechanism involving Rho kinase-dependent phosphorylation of the MLCP-regulatory subunit MYPT1. May play a role in the EGF signaling cascade. May be involved in mitosis and UV-induced damage response. Required for maintenance of normal renal structure and function by supporting normal podocyte function. {ECO:0000269|PubMed:10766823, ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11239472, ECO:0000269|PubMed:12719431, ECO:0000269|PubMed:16215232, ECO:0000269|PubMed:21081650, ECO:0000269|PubMed:9337861}.; . TISSUE SPECIFICITY: Expressed in columnar and transitional epithelia, mononuclear cells, smooth muscle cells, and endothelial cells lining capillaries and small venules (at protein level). Ubiquitously expressed, with highest levels in heart, placenta and ovary, and lowest levels in the kidney. Detected at low levels in islets of Langerhans from type 2 diabetes mellitus individuals. {ECO:0000269|PubMed:14563213, ECO:0000269|PubMed:21127054, ECO:0000269|PubMed:9337861}.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;larynx;bone;thyroid;iris;testis;amniotic fluid;germinal center;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;skeletal muscle;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach;aorta;cerebellum; dorsal root ganglion;amygdala;occipital lobe;superior cervical ganglion;thyroid;spinal cord;ciliary ganglion;atrioventricular node;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.60598 0.63552 -1.475338529 3.715498938 815.51268 5.61269 PIK3C2B 0.976238394768661 0.0237616052307672 5.71899416994419e-13 phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 beta FUNCTION: Phosphorylates PtdIns and PtdIns4P with a preference for PtdIns. Does not phosphorylate PtdIns(4,5)P2. May be involved in EGF and PDGF signaling cascades. {ECO:0000269|PubMed:10805725}.; . TISSUE SPECIFICITY: Expressed in columnar and transitional epithelia, mononuclear cells, and ganglion cells (at protein level). Widely expressed, with highest levels in thymus and placenta and lowest in peripheral blood, skeletal muscle and kidney. {ECO:0000269|PubMed:14563213, ECO:0000269|PubMed:9144573}.; . . 0.28929 0.24538 0.446303541 77.92521821 529.07187 4.69353 PIK3C2G 9.18857248003686e-32 1.21276559342563e-05 0.999987872344066 phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 gamma FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. May play a role in SDF1A-stimulated chemotaxis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in liver, prostate and testis. Lower levels in small intestine, kidney and pancreas. {ECO:0000269|PubMed:9878262}.; unclassifiable (Anatomical System);lung;testis;kidney;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.15501 0.19874 0.639248104 83.78744987 8233.84263 19.60911 PIK3C3 0.0803177256175585 0.919681522324062 7.52058379686815e-07 phosphatidylinositol 3-kinase catalytic subunit type 3 FUNCTION: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20643123, PubMed:20208530). Involved in the transport of lysosomal enzyme precursors to lysosomes. Required for transport from early to late endosomes (By similarity). {ECO:0000250|UniProtKB:O88763, ECO:0000269|PubMed:14617358, ECO:0000269|PubMed:20208530, ECO:0000269|PubMed:20643123, ECO:0000269|PubMed:7628435, ECO:0000305}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with a highest expression in skeletal muscle. {ECO:0000269|PubMed:7628435}.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;spinal cord;blood;lens;skeletal muscle;pancreas;lung;mesenchyma;nasopharynx;placenta;macula lutea;liver;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule; 0.68247 0.48656 -1.353899809 4.558858221 57.00174 1.51949 PIK3CA 0.99999851122751 1.48877249045211e-06 1.13681499478358e-17 phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha FUNCTION: Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4- phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5- bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Participates in cellular signaling in response to various growth factors. Involved in the activation of AKT1 upon stimulation by receptor tyrosine kinases ligands such as EGF, insulin, IGF1, VEGFA and PDGF. Involved in signaling via insulin-receptor substrate (IRS) proteins. Essential in endothelial cell migration during vascular development through VEGFA signaling, possibly by regulating RhoA activity. Required for lymphatic vasculature development, possibly by binding to RAS and by activation by EGF and FGF2, but not by PDGF. Regulates invadopodia formation in breast cancer cells through the PDPK1- AKT1 pathway. Participates in cardiomyogenesis in embryonic stem cells through a AKT1 pathway. Participates in vasculogenesis in embryonic stem cells through PDK1 and protein kinase C pathway. Has also serine-protein kinase activity: phosphorylates PIK3R1 (p85alpha regulatory subunit), EIF4EBP1 and HRAS. {ECO:0000269|PubMed:21708979}.; DISEASE: Note=PIK3CA mutations are involved in various type of cancer. Most of the cancer-associated mutations are missense mutations and map to one of the three hotspots: Glu-542; Glu-545 and His-1047. Mutated isoforms participate in cellular transformation and tumorigenesis induced by oncogenic receptor tyrosine kinases (RTKs) and HRAS/KRAS. Interaction with HRAS/KRAS is required for Ras-driven tumor formation. Mutations increasing the lipid kinase activity are required for oncogenic signaling. The protein kinase activity may not be required for tumorigenesis. {ECO:0000269|PubMed:15016963, ECO:0000269|PubMed:15289301, ECO:0000269|PubMed:15520168, ECO:0000269|PubMed:15712344, ECO:0000269|PubMed:15784156, ECO:0000269|PubMed:15924253, ECO:0000269|PubMed:15930273, ECO:0000269|PubMed:15994075, ECO:0000269|PubMed:16114017, ECO:0000269|PubMed:16322209, ECO:0000269|PubMed:16353168, ECO:0000269|PubMed:16432179, ECO:0000269|PubMed:16533766, ECO:0000269|PubMed:17673550, ECO:0000269|PubMed:19805105, ECO:0000269|PubMed:21708979, ECO:0000269|PubMed:22658544, ECO:0000269|PubMed:22729224}.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:15930273, ECO:0000269|PubMed:15994075}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:16353168}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease. {ECO:0000269|PubMed:15520168}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Hepatocellular carcinoma (HCC) [MIM:114550]: A primary malignant neoplasm of epithelial liver cells. The major risk factors for HCC are chronic hepatitis B virus (HBV) infection, chronic hepatitis C virus (HCV) infection, prolonged dietary aflatoxin exposure, alcoholic cirrhosis, and cirrhosis due to other causes. {ECO:0000269|PubMed:15608678}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Keratosis, seborrheic (KERSEB) [MIM:182000]: A common benign skin tumor. Seborrheic keratoses usually begin with the appearance of one or more sharply defined, light brown, flat macules. The lesions may be sparse or numerous. As they initially grow, they develop a velvety to finely verrucous surface, followed by an uneven warty surface with multiple plugged follicles and a dull or lackluster appearance. {ECO:0000269|PubMed:17673550}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Megalencephaly-capillary malformation-polymicrogyria syndrome (MCAP) [MIM:602501]: A syndrome characterized by a spectrum of anomalies including primary megalencephaly, prenatal overgrowth, brain and body asymmetry, cutaneous vascular malformations, digital anomalies consisting of syndactyly with or without postaxial polydactyly, connective tissue dysplasia involving the skin, subcutaneous tissue, and joints, and cortical brain malformations, most distinctively polymicrogyria. {ECO:0000269|PubMed:22729224}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Congenital lipomatous overgrowth, vascular malformations, and epidermal nevi (CLOVE) [MIM:612918]: A sporadically occurring, non-hereditary disorder characterized by asymmetric somatic hypertrophy and anomalies in multiple organs. It is defined by four main clinical findings: congenital lipomatous overgrowth, vascular malformations, epidermal nevi, and skeletal/spinal abnormalities. The presence of truncal overgrowth and characteristic patterned macrodactyly at birth differentiates CLOVE from other syndromic forms of overgrowth. {ECO:0000269|PubMed:22658544}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cowden syndrome 5 (CWS5) [MIM:615108]: A form of Cowden syndrome, a hamartomatous polyposis syndrome with age-related penetrance. Cowden syndrome is characterized by hamartomatous lesions affecting derivatives of ectodermal, mesodermal and endodermal layers, macrocephaly, facial trichilemmomas (benign tumors of the hair follicle infundibulum), acral keratoses, papillomatous papules, and elevated risk for development of several types of malignancy, particularly breast carcinoma in women and thyroid carcinoma in both men and women. Colon cancer and renal cell carcinoma have also been reported. Hamartomas can be found in virtually every organ, but most commonly in the skin, gastrointestinal tract, breast and thyroid. {ECO:0000269|PubMed:23246288}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;lens;skeletal muscle;breast;lung;mesenchyma;placenta;macula lutea;liver;alveolus;kidney;aorta;thymus; prefrontal cortex;parietal lobe; 0.95444 0.85056 -0.448125345 24.19202642 410.49414 4.24624 PIK3CB 0.999979002310697 2.09976893018265e-05 1.45009533000363e-15 phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta FUNCTION: Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4- phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5- bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Involved in the activation of AKT1 upon stimulation by G-protein coupled receptors (GPCRs) ligands such as CXCL12, sphingosine 1-phosphate, and lysophosphatidic acid. May also act downstream receptor tyrosine kinases. Required in different signaling pathways for stable platelet adhesion and aggregation. Plays a role in platelet activation signaling triggered by GPCRs, alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) and ITAM (immunoreceptor tyrosine-based activation motif)-bearing receptors such as GP6. Regulates the strength of adhesion of ITGA2B/ ITGB3 activated receptors necessary for the cellular transmission of contractile forces. Required for platelet aggregation induced by F2 (thrombin) and thromboxane A2 (TXA2). Has a role in cell survival. May have a role in cell migration. Involved in the early stage of autophagosome formation. Modulates the intracellular level of PtdIns3P (Phosphatidylinositol 3-phosphate) and activates PIK3C3 kinase activity. May act as a scaffold, independently of its lipid kinase activity to positively regulate autophagy. May have a role in insulin signaling as scaffolding protein in which the lipid kinase activity is not required. May have a kinase-independent function in regulating cell proliferation and in clathrin-mediated endocytosis. Mediator of oncogenic signal in cell lines lacking PTEN. The lipid kinase activity is necessary for its role in oncogenic transformation. Required for the growth of ERBB2 and RAS driven tumors. {ECO:0000269|PubMed:18594509, ECO:0000269|PubMed:18755892, ECO:0000269|PubMed:21030680, ECO:0000269|PubMed:21383062}.; . TISSUE SPECIFICITY: Expressed ubiquitously.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;small intestine;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;pia mater;lung;nasopharynx;placenta;hippocampus;liver;cervix;head and neck;kidney;mammary gland;nose;aorta;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;temporal lobe;prefrontal cortex;globus pallidus;appendix;ciliary ganglion;pons;parietal lobe;cingulate cortex;skeletal muscle; 0.99777 0.36218 -1.42004951 4.104741684 42.08334 1.22591 PIK3CD 0.999984294919708 1.57050802056651e-05 8.62749945816415e-14 phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta FUNCTION: Phosphoinositide-3-kinase (PI3K) that phosphorylates PftdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Mediates immune responses. Plays a role in B-cell development, proliferation, migration, and function. Required for B-cell receptor (BCR) signaling. Mediates B-cell proliferation response to anti-IgM, anti-CD40 and IL4 stimulation. Promotes cytokine production in response to TLR4 and TLR9. Required for antibody class switch mediated by TLR9. Involved in the antigen presentation function of B-cells. Involved in B-cell chemotaxis in response to CXCL13 and sphingosine 1-phosphate (S1P). Required for proliferation, signaling and cytokine production of naive, effector and memory T-cells. Required for T-cell receptor (TCR) signaling. Mediates TCR signaling events at the immune synapse. Activation by TCR leads to antigen-dependent memory T-cell migration and retention to antigenic tissues. Together with PIK3CG participates in T-cell development. Contributes to T-helper cell expansion and differentiation. Required for T-cell migration mediated by homing receptors SELL/CD62L, CCR7 and S1PR1 and antigen dependent recruitment of T-cells. Together with PIK3CG is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in NK cell receptor activation. Have a role in NK cell maturation and cytokine production. Together with PIK3CG is involved in neutrophil chemotaxis and extravasation. Together with PIK3CG participates in neutrophil respiratory burst. Have important roles in mast-cell development and mast cell mediated allergic response. Involved in stem cell factor (SCF)-mediated proliferation, adhesion and migration. Required for allergen-IgE-induced degranulation and cytokine release. The lipid kinase activity is required for its biological function. Isoform 2 may be involved in stabilizing total RAS levels, resulting in increased ERK phosphorylation and increased PI3K activity. {ECO:0000269|PubMed:20081091, ECO:0000269|PubMed:22020336}.; DISEASE: Activated PI3K-delta syndrome (APDS) [MIM:615513]: A disorder characterized by recurrent respiratory infections, progressive airway damage, lymphopenia, increased circulating transitional B cells, increased immunoglobulin M, reduced immunoglobulin G2 levels in serum, and impaired vaccine responses. {ECO:0000269|PubMed:24136356}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 2 is expressed in normal thymus, lung and spleen tissues, and is detected at low levels in normal lysates from colon and ovarian biopsies, at elevated levels in lysates from colorectal tumors and is abundantly expressed in some ovarian tumors (at protein level). Both isoform 1 and isoform 2 are widely expressed. Isoform 1 is expressed predominantly in leukocytes. {ECO:0000269|PubMed:22020336}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;blood;skeletal muscle;skin;bone marrow;uterus;breast;prostate;lung;endometrium;visual apparatus;liver;testis;spleen;germinal center; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;white blood cells;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;whole blood;bone marrow; 0.61351 0.31361 -1.658985203 2.724699222 274.89339 3.55263 PIK3CD-AS1 . . . PIK3CD antisense RNA 1 . . . . . . . . . . . PIK3CD-AS2 . . . PIK3CD antisense RNA 2 . . . . . . . . . . . PIK3CG 0.56396387141262 0.436031692050704 4.43653667588277e-06 phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma FUNCTION: Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Links G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses. Modulates leukocyte chemotaxis to inflammatory sites and in response to chemoattractant agents. May control leukocyte polarization and migration by regulating the spatial accumulation of PIP3 and by regulating the organization of F-actin formation and integrin- based adhesion at the leading edge. Controls motility of dendritic cells. Together with PIK3CD is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in T-lymphocyte migration. Regulates T-lymphocyte proliferation and cytokine production. Together with PIK3CD participates in T-lymphocyte development. Required for B- lymphocyte development and signaling. Together with PIK3CD participates in neutrophil respiratory burst. Together with PIK3CD is involved in neutrophil chemotaxis and extravasation. Together with PIK3CB promotes platelet aggregation and thrombosis. Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) adhesive function in platelets downstream of P2Y12 through a lipid kinase activity-independent mechanism. May have also a lipid kinase activity-dependent function in platelet aggregation. Involved in endothelial progenitor cell migration. Negative regulator of cardiac contractility. Modulates cardiac contractility by anchoring protein kinase A (PKA) and PDE3B activation, reducing cAMP levels. Regulates cardiac contractility also by promoting beta-adrenergic receptor internalization by binding to ADRBK1 and by non-muscle tropomyosin phosphorylation. Also has serine/threonine protein kinase activity: both lipid and protein kinase activities are required for beta-adrenergic receptor endocytosis. May also have a scaffolding role in modulating cardiac contractility. Contributes to cardiac hypertrophy under pathological stress. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis. {ECO:0000269|PubMed:12163475, ECO:0000269|PubMed:15294162, ECO:0000269|PubMed:16094730, ECO:0000269|PubMed:21393242, ECO:0000269|PubMed:7624799}.; . TISSUE SPECIFICITY: Pancreas, skeletal muscle, liver and heart. {ECO:0000269|PubMed:7624799}.; unclassifiable (Anatomical System);lung;ovary;testis;blood;germinal center;brain;skeletal muscle; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.96004 0.76043 -0.813834387 12.05472989 1875.79638 7.96613 PIK3IP1 0.0597509759336671 0.868268802630864 0.0719802214354688 phosphoinositide-3-kinase interacting protein 1 FUNCTION: Negative regulator of hepatic phosphatidylinositol 3- kinase (PI3K) activity. {ECO:0000250}.; . . lymphoreticular;medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;muscle;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; superior cervical ganglion;trigeminal ganglion; 0.35052 0.10184 0.349177632 74.18023119 85.412 1.97063 PIK3IP1-AS1 . . . PIK3IP1 antisense RNA 1 (head to head) . . . . . . . . . . . PIK3R1 0.998240487886569 0.00175951204310482 7.03263733080152e-11 phosphoinositide-3-kinase regulatory subunit 1 FUNCTION: Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling (PubMed:17626883, PubMed:19805105, PubMed:7518429). Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (PubMed:20348923). {ECO:0000269|PubMed:17626883, ECO:0000269|PubMed:19805105, ECO:0000269|PubMed:20348923, ECO:0000269|PubMed:7518429}.; DISEASE: Agammaglobulinemia 7, autosomal recessive (AGM7) [MIM:615214]: A primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life. {ECO:0000269|PubMed:22351933}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: SHORT syndrome (SHORTS) [MIM:269880]: A rare, multisystem disease characterized by short stature, anomalies of the anterior chamber of the eye, characteristic facial features such as triangular facies, lack of facial fat, and hypoplastic nasal alae with overhanging columella, partial lipodystrophy, hernias, hyperextensibility, and delayed dentition. The clinical phenotype can include insulin resistance, nephrocalcinosis, and hearing deficits. Developmental milestones and cognition are normal. {ECO:0000269|PubMed:23810378, ECO:0000269|PubMed:23810379, ECO:0000269|PubMed:23810382}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Immunodeficiency 36 (IMD36) [MIM:616005]: A primary immunodeficiency characterized by impaired B-cell function, hypogammaglobulinemia and recurrent infections. {ECO:0000269|PubMed:25133428}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 2 is expressed in skeletal muscle and brain, and at lower levels in kidney and cardiac muscle. Isoform 2 and isoform 4 are present in skeletal muscle (at protein level). {ECO:0000269|PubMed:8628286}.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;germinal center;brain;gall bladder;cartilage;heart;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;pineal gland;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;lung;adrenal gland;placenta;head and neck;kidney;stomach;thymus; amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.88821 0.86719 -0.756778259 13.44656759 2135.01489 8.50101 PIK3R2 0.939626884464957 0.0603710319062914 2.08362875153338e-06 phosphoinositide-3-kinase regulatory subunit 2 FUNCTION: Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5- trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy (PubMed:23604317). Promotes nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin- dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (By similarity). {ECO:0000250|UniProtKB:O08908, ECO:0000269|PubMed:23604317}.; DISEASE: Megalencephaly-polymicrogyria-polydactyly-hydrocephalus syndrome 1 (MPPH1) [MIM:603387]: A syndrome characterized by megalencephaly, hydrocephalus, and polymicrogyria; polydactyly may also be seen. There is considerable phenotypic similarity between this disorder and the megalencephaly-capillary malformation syndrome. {ECO:0000269|PubMed:22729224}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;salivary gland;colon;parathyroid;skin;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;testis;brain;unclassifiable (Anatomical System);islets of Langerhans;urinary;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;liver;duodenum;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.47036 0.41833 -0.534490515 20.70063694 216.25734 3.17643 PIK3R3 1.40585793273596e-06 0.953944193803834 0.0460544003382331 phosphoinositide-3-kinase regulatory subunit 3 FUNCTION: Binds to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulates their kinase activity. During insulin stimulation, it also binds to IRS-1.; . TISSUE SPECIFICITY: Highest levels in brain and testis. Lower levels in adipose tissue, kidney, heart, lung and skeletal muscle.; ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);heart;lacrimal gland;tongue;pineal body;spinal cord;blood;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;cerebellum peduncles;testis;ciliary ganglion;cerebellum; 0.43963 0.34171 -0.093566408 46.7386176 76.83464 1.84013 PIK3R4 0.707146275693906 0.29285371423304 1.00730540686671e-08 phosphoinositide-3-kinase regulatory subunit 4 FUNCTION: Regulatory subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20643123). {ECO:0000269|PubMed:20643123}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:8999962}.; medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;spinal cord;urinary;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;medulla oblongata;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.86092 . -1.126142808 6.564048125 271.967 3.53406 PIK3R5 0.817693684157708 0.182304778396085 1.53744620697518e-06 phosphoinositide-3-kinase regulatory subunit 5 FUNCTION: Regulatory subunit of the PI3K gamma complex. Required for recruitment of the catalytic subunit to the plasma membrane via interaction with beta-gamma G protein dimers. Required for G protein-mediated activation of PIK3CG (By similarity). {ECO:0000250}.; DISEASE: Ataxia-oculomotor apraxia 3 (AOA3) [MIM:615217]: An autosomal recessive disease characterized by cerebellar ataxia, oculomotor apraxia, areflexia and peripheral neuropathy. {ECO:0000269|PubMed:22065524}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed with high expression in fetal brain compared to adult brain. Abundant expression is observed in cerebellum, cerebral cortex, cerebral meninges, and vermis cerebelli. {ECO:0000269|PubMed:15797027, ECO:0000269|PubMed:22065524}.; unclassifiable (Anatomical System);lung;nasopharynx;placenta;testis;blood;kidney;thymus;bone marrow; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.09170 0.10099 -0.461076406 23.66124086 168.04756 2.82980 PIK3R6 1.37502587799544e-15 0.011591614582004 0.988408385417995 phosphoinositide-3-kinase regulatory subunit 6 FUNCTION: Regulatory subunit of the PI3K gamma complex. Acts as an adapter to drive activation of PIK3CG by beta-gamma G protein dimers. The PIK3CG:PIK3R6 heterodimer is much less sensitive to beta-gamma G protein dimers than PIK3CG:PIK3R5 and its membrane recruitment and beta-gamma G protein dimer-dependent activation requires HRAS bound to PIK3CG. Recruits of the PI3K gamma complex to a PDE3B:RAPGEF3 signaling complex involved in angiogenesis; signaling seems to involve RRAS. {ECO:0000269|PubMed:21393242}.; . . unclassifiable (Anatomical System);prostate;lung;spleen;germinal center;brain;bone marrow; . 0.08757 0.09704 . . 360.70604 4.01967 PIKFYVE 0.97980274888433 0.0201972511156696 5.31810488318644e-18 phosphoinositide kinase, FYVE-type zinc finger containing FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo- inositol ring, to form phosphatidylinositol 3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. Plays a role in the biogenesis of endosome carrier vesicles (ECV)/ multivesicular bodies (MVB) transport intermediates from early endosomes. {ECO:0000269|PubMed:17556371}.; DISEASE: Corneal dystrophy, fleck (CFD) [MIM:121850]: A form of stromal corneal dystrophy characterized by numerous small white flecks scattered in all levels of the stroma, with configurations varying from semicircular to wreath-like, curvilinear, or punctate. Although CFD may occasionally cause mild photophobia, patients are typically asymptomatic and have normal vision. {ECO:0000269|PubMed:15902656}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;prostate;whole body;endometrium;larynx;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.40145 0.43176 -1.400183431 4.163717858 374.82497 4.08231 PILRA 2.14141882603506e-08 0.1397620907056 0.860237887880211 paired immunoglobin-like type 2 receptor alpha FUNCTION: Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRA is thought to act as a cellular signaling inhibitory receptor by recruiting cytoplasmic phosphatases like PTPN6/SHP-1 and PTPN11/SHP-2 via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. Receptor for PIANP. {ECO:0000269|PubMed:10903717, ECO:0000269|PubMed:18358807, ECO:0000269|PubMed:21241660}.; . TISSUE SPECIFICITY: Predominantly detected in hemopoietic tissues and is expressed by monocytes, macrophages, and granulocytes, but not by lymphocytes. Also strongly expressed by dendritic cells (DC); preferentially by CD14+/CD1a- DC derived from CD34+ progenitors. Also expressed by CD11c+ blood and tonsil DC, but not by CD11c- DC precursors. {ECO:0000269|PubMed:10903717}.; unclassifiable (Anatomical System);smooth muscle;blood;retina;bone marrow;uterus;breast;prostate;lung;thyroid;placenta;alveolus;testis;head and neck;kidney;brain;mammary gland; whole blood;skeletal muscle; 0.05578 . 0.685332364 85.09672092 24.52952 0.80605 PILRB 3.36639654254602e-06 0.194490182453813 0.805506451149644 paired immunoglobin-like type 2 receptor beta FUNCTION: Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRB is thought to act as a cellular signaling activating receptor that associates with ITAM-bearing adapter molecules on the cell surface.; . . unclassifiable (Anatomical System);lymphoreticular;lymph node;ovary;heart;islets of Langerhans;retina;breast;prostate;pancreas;lung;endometrium;larynx;epididymis;thyroid;testis;head and neck;spleen;spinal ganglion;brain;bladder;stomach;peripheral nerve; testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.06992 0.07324 -0.139478553 43.29440906 1309.19829 6.80664 PIM1 0.886575782773823 0.11316858915061 0.000255628075567746 Pim-1 proto-oncogene, serine/threonine kinase FUNCTION: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl- X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post- translational levels. Phosphorylation of CDKN1B,induces 14-3-3- proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis. {ECO:0000269|PubMed:10664448, ECO:0000269|PubMed:12431783, ECO:0000269|PubMed:15528381, ECO:0000269|PubMed:16356754, ECO:0000269|PubMed:1825810, ECO:0000269|PubMed:18593906, ECO:0000269|PubMed:19749799}.; . TISSUE SPECIFICITY: Expressed primarily in cells of the hematopoietic and germline lineages. Isoform 1 and isoform 2 are both expressed in prostate cancer cell lines. {ECO:0000269|PubMed:16186805}.; . . 0.63553 0.26358 0.283038099 71.26680821 69.31582 1.72630 PIM2 0.894760123149801 0.104219774988351 0.00102010186184734 Pim-2 proto-oncogene, serine/threonine kinase FUNCTION: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression, the regulation of cap-dependent protein translation and through survival signaling by phosphorylation of a pro-apoptotic protein, BAD. Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase transcriptional activity. The stabilization of MYC exerted by PIM2 might explain partly the strong synergism between these 2 oncogenes in tumorigenesis. Regulates cap-dependent protein translation in a mammalian target of rapamycin complex 1 (mTORC1)-independent manner and in parallel to the PI3K-Akt pathway. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti- apoptotic protein Bcl-X(L)/BCL2L1. Promotes cell survival in response to a variety of proliferative signals via positive regulation of the I-kappa-B kinase/NF-kappa-B cascade; this process requires phosphorylation of MAP3K8/COT. Isoform 1 is less active in this respect. Promotes growth factor-independent proliferation by phosphorylation of cell cycle factors such as CDKN1A and CDKN1B. Involved in the positive regulation of chondrocyte survival and autophagy in the epiphyseal growth plate. {ECO:0000269|PubMed:18593906, ECO:0000269|PubMed:18675992, ECO:0000269|PubMed:20307683}.; . TISSUE SPECIFICITY: Highly expressed in hematopoietic tissues, in leukemic and lymphoma cell lines, testis, small intestine, colon and colorectal adenocarcinoma cells. Weakly expressed in normal liver, but highly expressed in hepatocellular carcinoma tissues. {ECO:0000269|PubMed:18675992}.; . . 0.77719 0.25793 -0.185391282 39.67916962 4.12142 0.15069 PIM3 0.937120654328565 0.0626035259256684 0.000275819745767069 Pim-3 proto-oncogene, serine/threonine kinase FUNCTION: Proto-oncogene with serine/threonine kinase activity that can prevent apoptosis, promote cell survival and protein translation. May contribute to tumorigenesis through: the delivery of survival signaling through phosphorylation of BAD which induces release of the anti-apoptotic protein Bcl-X(L), the regulation of cell cycle progression, protein synthesis and by regulation of MYC transcriptional activity. Additionally to this role on tumorigenesis, can also negatively regulate insulin secretion by inhibiting the activation of MAPK1/3 (ERK1/2), through SOCS6. Involved also in the control of energy metabolism and regulation of AMPK activity in modulating MYC and PPARGC1A protein levels and cell growth. {ECO:0000269|PubMed:15540201, ECO:0000269|PubMed:16818649, ECO:0000269|PubMed:17270021, ECO:0000269|PubMed:17876606, ECO:0000269|PubMed:18593906}.; . TISSUE SPECIFICITY: Detected in various tissues, including the heart, brain, lung, kidney, spleen, placenta, skeletal muscle, and peripheral blood leukocytes. Not found or barely expressed in the normal adult endoderm-derived organs such as colon, thymus, liver, or small intestine. However, expression is augmented in premalignant and malignant lesions of these organs. {ECO:0000269|PubMed:15540201, ECO:0000269|PubMed:16818649, ECO:0000269|PubMed:17270021}.; unclassifiable (Anatomical System);lymph node;lung;endometrium;synovium;islets of Langerhans;testis;kidney;skin;stomach;retina; placenta;atrioventricular node;trigeminal ganglion; 0.23182 0.15417 . . 44.13907 1.26704 PIN1 0.340906808984076 0.600368759659988 0.0587244313559353 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 FUNCTION: Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr- Pro) motifs in a subset of proteins, resulting in conformational changes in the proteins (PubMed:21497122, PubMed:22033920). Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK (PubMed:16644721). Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation (PubMed:15664191). Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner (PubMed:17828269). Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN (PubMed:22608923). {ECO:0000269|PubMed:15664191, ECO:0000269|PubMed:16644721, ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:21497122, ECO:0000269|PubMed:22033920, ECO:0000269|PubMed:22608923}.; . TISSUE SPECIFICITY: The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells. {ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:21497122}.; medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;blood;lens;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;kidney;mammary gland;stomach;thymus; amygdala;whole brain;occipital lobe;medulla oblongata;hypothalamus;temporal lobe;prefrontal cortex;globus pallidus;testis;pons;cingulate cortex; 0.95345 0.40044 -0.029247611 51.40363293 4.27739 0.15553 PIN1P1 . . . peptidylprolyl cis/trans isomerase, NIMA-interacting 1 pseudogene 1 . . . . . . . . . . . PIN4 0.646369632596627 0.327220848516233 0.0264095188871402 peptidylprolyl cis/trans isomerase, NIMA-interacting 4 FUNCTION: Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA. {ECO:0000269|PubMed:19369196}.; . TISSUE SPECIFICITY: Isoform 2 is much more stable than isoform 1 (at protein level). Ubiquitous. Isoform 1 and isoform 2 are expressed in kidney, liver, blood vessel, brain, mammary gland, skeletal muscle, small intestine and submandibularis. Isoform 1 transcripts are much more abundant than isoform 2 in each tissue analyzed. {ECO:0000269|PubMed:10100858, ECO:0000269|PubMed:10364457, ECO:0000269|PubMed:16522211}.; ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;frontal lobe;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;lung;cornea;adrenal gland;visual apparatus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22953 0.22076 0.547599505 81.2160887 55.16442 1.48904 PIN4P1 . . . protein (peptidylprolyl cis/trans isomerase) NIMA-interacting, 4 pseudogene 1 . . . . . . . . . . . PINK1 4.0835436809341e-07 0.587542005349238 0.412457586296394 PTEN induced putative kinase 1 FUNCTION: Protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins. Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) by mediating activation and translocation of PARK2. Targets PARK2 to dysfunctional depolarized mitochondria through the phosphorylation of MFN2. Activates PARK2 in 2 steps: (1) by mediating phosphorylation at 'Ser-65' of PARK2 and (2) mediating phosphorylation of ubiquitin, converting PARK2 to its fully-active form (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25527291). {ECO:0000269|PubMed:14607334, ECO:0000269|PubMed:15087508, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:19966284, ECO:0000269|PubMed:20404107, ECO:0000269|PubMed:20798600, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23754282, ECO:0000269|PubMed:23933751, ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:24896179, ECO:0000269|PubMed:25527291}.; DISEASE: Parkinson disease 6 (PARK6) [MIM:605909]: A neurodegenerative disorder characterized by parkinsonian signs such as rigidity, resting tremor and bradykinesia. A subset of patients manifest additional symptoms including hyperreflexia, autonomic instability, dementia and psychiatric disturbances. Symptoms show diurnal fluctuation and can improve after sleep. {ECO:0000269|PubMed:15087508, ECO:0000269|PubMed:15349860, ECO:0000269|PubMed:15349870, ECO:0000269|PubMed:15505171, ECO:0000269|PubMed:15596610, ECO:0000269|PubMed:15955953, ECO:0000269|PubMed:15970950, ECO:0000269|PubMed:16009891, ECO:0000269|PubMed:16207217, ECO:0000269|PubMed:16257123, ECO:0000269|PubMed:16401616, ECO:0000269|PubMed:16482571, ECO:0000269|PubMed:16632486, ECO:0000269|PubMed:16966503, ECO:0000269|PubMed:17030667, ECO:0000269|PubMed:18286320, ECO:0000269|PubMed:22956510}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and testis, and at lower levels in brain, placenta, liver, kidney, pancreas, prostate, ovary and small intestine. Present in the embryonic testis from an early stage of development. {ECO:0000269|PubMed:11494141}.; . . 0.14291 0.17629 -0.462894052 23.62585515 2907.56994 10.22981 PINK1-AS . . . PINK1 antisense RNA . . . . . 0.19607 . . . . . PINLYP . . . phospholipase A2 inhibitor and LY6/PLAUR domain containing . . . . . . . . . 23.3479 0.77913 PINX1 4.9427916851122e-09 0.0610481045172872 0.938951890539921 PIN2/TERF1 interacting, telomerase inhibitor 1 FUNCTION: Microtubule-binding protein essential for faithful chromosome segregation. Mediates TRF1 and TERT accumulation in nucleolus and enhances TRF1 binding to telomeres. Inhibits telomerase activity. May inhibit cell proliferation and act as tumor suppressor. {ECO:0000269|PubMed:15381700, ECO:0000269|PubMed:17198684, ECO:0000269|PubMed:19117989, ECO:0000269|PubMed:19265708, ECO:0000269|PubMed:19393617, ECO:0000269|PubMed:19553660}.; . TISSUE SPECIFICITY: Ubiquitous; expressed at low levels. Not detectable in a number of hepatocarcinoma cell lines.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;oesophagus;testis;brain;bladder;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;bile duct;breast;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach; ciliary ganglion;atrioventricular node; . . 0.887394731 89.18966737 1328.2156 6.85051 PIP 0.0055055964537849 0.715549428855712 0.278944974690503 prolactin-induced protein . . TISSUE SPECIFICITY: Expressed in pathological conditions of the mammary gland and in several exocrine tissues, such as the lacrimal, salivary, and sweat glands.; ovary;salivary gland;intestine;colon;parathyroid;skin;prostate;thyroid;dura mater;bladder;pineal gland;brain;unclassifiable (Anatomical System);meninges;lacrimal gland;adrenal cortex;pharynx;blood;breast;pia mater;lung;adrenal gland;nasopharynx;visual apparatus;liver;head and neck;kidney;mammary gland; prostate;trachea;salivary gland;pons;skin; 0.00701 . 1.060147109 91.46614768 76.18252 1.82895 PIP4K2A 0.788196366835575 0.211522643330594 0.000280989833830552 phosphatidylinositol-5-phosphate 4-kinase, type II, alpha FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 5- phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2. May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation. May negatively regulate insulin- stimulated glucose uptake by lowering the levels of PtdIns5P. May be involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size. {ECO:0000269|PubMed:18364242}.; . TISSUE SPECIFICITY: Expressed ubiquitously, with high levels in the brain. Present in most tissues, except notably skeletal muscle and small intestine. {ECO:0000269|PubMed:7639683, ECO:0000269|PubMed:7852364}.; colon;parathyroid;fovea centralis;choroid;retina;uterus;optic nerve;frontal lobe;cerebral cortex;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;macula lutea;hippocampus;visual apparatus;liver;spleen;kidney;thymus; whole brain;amygdala;medulla oblongata;thalamus;occipital lobe;superior cervical ganglion;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;bone marrow;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.14038 0.21177 -0.0274281 51.65723048 1626.97809 7.45770 PIP4K2B 0.989205103584798 0.0107913719982909 3.52441691124382e-06 phosphatidylinositol-5-phosphate 4-kinase, type II, beta FUNCTION: Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. {ECO:0000269|PubMed:9038203}.; . TISSUE SPECIFICITY: Highly expressed in brain, heart, pancreas, skeletal muscle and kidney. Detected at lower levels in placenta, lung and liver. {ECO:0000269|PubMed:9038203}.; colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;mesenchyma;macula lutea;visual apparatus;head and neck;kidney;mammary gland;stomach;cerebellum; whole brain;amygdala;medulla oblongata;superior cervical ganglion;occipital lobe;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.18019 0.12112 -0.049474214 50.01179523 29.81132 0.95121 PIP4K2C 0.0133787346006026 0.979758941969208 0.00686232343018903 phosphatidylinositol-5-phosphate 4-kinase, type II, gamma FUNCTION: May play an important role in the production of Phosphatidylinositol bisphosphate (PIP2), in the endoplasmic reticulum. {ECO:0000250}.; . . ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;frontal lobe;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;heart;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach; whole brain;superior cervical ganglion;thalamus;occipital lobe;temporal lobe;prefrontal cortex;testis;ciliary ganglion;kidney;trigeminal ganglion;cingulate cortex;cerebellum; 0.15235 . -0.448125345 24.19202642 311.75433 3.75766 PIP5K1A 0.0145862989024307 0.985162173867752 0.000251527229817272 phosphatidylinositol-4-phosphate 5-kinase, type I, alpha FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as actin cytoskeleton organization, cell adhesion, migration and phagocytosis. Required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of RAC1 to the plasma membrane. Together with PIP5K1C is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle ingestion by activating WAS that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup. Together with PIP5K1B is required after stimulation of G-protein coupled receptors for stable platelet adhesion. Plays a role during calcium-induced keratinocyte differentiation. Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, diacylglycerol and inositol 1,4,5-trisphosphate that mobilize internal calcium and drive keratinocyte differentiation. Together with PIP5K1C have a role during embryogenesis. Functions also in the nucleus where acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs. {ECO:0000269|PubMed:18288197, ECO:0000269|PubMed:19158393, ECO:0000269|PubMed:20660631}.; . TISSUE SPECIFICITY: Highly expressed in heart, placenta, skeletal muscle, kidney and pancreas. Detected at lower levels in brain, lung and liver.; smooth muscle;ovary;colon;parathyroid;skin;retina;uterus;prostate;endometrium;larynx;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;placenta;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.12043 0.12792 -0.514264485 21.41424864 69.18119 1.72333 PIP5K1B 0.00744304703893292 0.991885028322177 0.000671924638890335 phosphatidylinositol-4-phosphate 5-kinase, type I, beta FUNCTION: Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. Mediates RAC1-dependent reorganization of actin filaments. Contributes to the activation of PLD2. Together with PIP5K1A is required after stimulation of G-protein coupled receptors for stable platelet adhesion (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in heart, pancreas, brain, kidney, skeletal muscle and lung. {ECO:0000269|PubMed:8955136}.; unclassifiable (Anatomical System);myocardium;lymph node;cartilage;heart;colon;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;lung;endometrium;placenta;macula lutea;hippocampus;iris;liver;testis;spleen;kidney;brain;aorta; superior cervical ganglion;testis; 0.21303 0.09348 0.196671391 67.19155461 204.50096 3.08963 PIP5K1C 0.859389818234551 0.140606423813985 3.75795146389358e-06 phosphatidylinositol-4-phosphate 5-kinase, type I, gamma FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as vesicle mediated transport, cell adhesion, cell polarization and cell migration. Together with PIP5K1A is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle attachment by generating the pool of PtdIns(4,5)P2 that induces controlled actin depolymerization to facilitate Fc-gamma-R clustering. Mediates RAC1-dependent reorganization of actin filaments. Required for synaptic vesicle transport. Controls the plasma membrane pool of PtdIns(4,5)P2 implicated in synaptic vesicle endocytosis and exocytosis. Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2). Required for clathrin-coated pits assembly at the synapse. Participates in cell junction assembly. Modulates adherens junctions formation by facilitating CDH1 trafficking. Required for focal adhesion dynamics. Modulates the targeting of talins (TLN1 and TLN2) to the plasma membrane and their efficient assembly into focal adhesions. Regulates the interaction between talins (TLN1 and TLN2) and beta-integrins. Required for uropodium formation and retraction of the cell rear during directed migration. Has a role in growth factor- stimulated directional cell migration and adhesion. Required for talin assembly into nascent adhesions forming at the leading edge toward the direction of the growth factor. Negative regulator of T-cell activation and adhesion. Negatively regulates integrin alpha-L/beta-2 (LFA-1) polarization and adhesion induced by T-cell receptor. Together with PIP5K1A have a role during embryogenesis and together with PIP5K1B may have a role immediately after birth. {ECO:0000269|PubMed:12422219, ECO:0000269|PubMed:12847086, ECO:0000269|PubMed:17261850, ECO:0000269|PubMed:17635937}.; DISEASE: Lethal congenital contracture syndrome 3 (LCCS3) [MIM:611369]: A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy, and congenital non-progressive joint contractures (arthrogryposis). The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth. LCCS3 patients present at birth with severe multiple joint contractures and severe muscle wasting and atrophy, mainly in the legs. Death occurs minutes to hours after birth due to respiratory insufficiency. The phenotype can be distinguished from that of LCCS1 by the absence of hydrops, fractures and multiple pterygia, and from LCCS2 by the absence of neurogenic bladder defect. {ECO:0000269|PubMed:17701898}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is strongly expressed in brain and also detected in heart and lung. Isoform 2 is strongly expressed in pancreas and liver and in lesser quantities in brain, heart, lung and kidney. Isoform 3 is detected in large amounts in heart and large intestine, is also present in lung, pancreas and thyroid, and to a lesser extent in brain, stomach and kidney. {ECO:0000269|PubMed:19548880}.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;cerebellum cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;kidney;mammary gland;stomach;cerebellum; . 0.11686 0.16692 -0.306750577 32.23047889 603.76401 4.97464 PIP5K1P1 . . . phosphatidylinositol-4-phosphate 5-kinase, type I, pseudogene 1 . . . . . . . . . . . PIP5K1P2 . . . phosphatidylinositol-4-phosphate 5-kinase, type I, pseudogene 2 . . . . . . . . . . . PIP5KL1 4.90216675296999e-06 0.411242567755845 0.588752530077402 phosphatidylinositol-4-phosphate 5-kinase-like 1 FUNCTION: May act as a scaffold to localize and regulate type I PI(4)P 5-kinases to specific compartments within the cell, where they generate PI(4,5)P2 for actin nucleation, signaling and scaffold protein recruitment and conversion to PI(3,4,5)P3. {ECO:0000250}.; . . medulla oblongata;optic nerve;lung;cartilage;macula lutea;cervix;fovea centralis;choroid;lens;skin;stomach;retina; . 0.08105 . 0.194852702 67.03231894 39.04921 1.15755 PIPOX 9.88251817300836e-11 0.0830592691458845 0.91694073075529 pipecolic acid oxidase FUNCTION: Metabolizes sarcosine, L-pipecolic acid and L-proline.; . . unclassifiable (Anatomical System);lymph node;endometrium;adrenal gland;islets of Langerhans;hypothalamus;placenta;visual apparatus;hippocampus;muscle;liver;spleen;brain;retina; liver;kidney;trigeminal ganglion;skeletal muscle; 0.93235 0.15237 -0.556537043 19.72753008 129.20874 2.47766 PIPSL . . . PIP5K1A and PSMD4-like, pseudogene FUNCTION: Has negligeable PIP5 kinase activity. Binds to ubiquitinated proteins.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:17623810}.; . . . . . . . . PIR 1.15732341465005e-05 0.365215781734669 0.634772645031184 pirin FUNCTION: Transcriptional coregulator of NF-kappa-B which facilitates binding of NF-kappa-B proteins to target kappa-B genes in a redox-state-dependent manner. May be required for efficient terminal myeloid maturation of hematopoietic cells. Has quercetin 2,3-dioxygenase activity (in vitro). {ECO:0000269|PubMed:17288615, ECO:0000269|PubMed:20010624, ECO:0000269|PubMed:20711196, ECO:0000269|PubMed:23716661}.; . TISSUE SPECIFICITY: Highly expressed in a subset of melanomas. Detected at very low levels in most tissues (at protein level). Expressed in all tissues, with highest level of expression in heart and liver. {ECO:0000269|PubMed:20089166, ECO:0000269|PubMed:9079676}.; . . 0.14392 0.28917 0.483275131 79.25218212 255.65341 3.43891 PIRC1 . . . piwi-interacting RNA cluster 1 . . . . . . . . . . . PIRC2 . . . piwi-interacting RNA cluster 2 . . . . . . . . . . . PIRC3 . . . piwi-interacting RNA cluster 3 . . . . . . . . . . . PIRC4 . . . piwi-interacting RNA cluster 4 . . . . . . . . . . . PIRC5 . . . piwi-interacting RNA cluster 5 . . . . . . . . . . . PIRC6 . . . piwi-interacting RNA cluster 6 . . . . . . . . . . . PIRC7 . . . piwi-interacting RNA cluster 7 . . . . . . . . . . . PIRC8 . . . piwi-interacting RNA cluster 8 . . . . . . . . . . . PIRC9 . . . piwi-interacting RNA cluster 9 . . . . . . . . . . . PIRC10 . . . piwi-interacting RNA cluster 10 . . . . . . . . . . . PIRC11 . . . piwi-interacting RNA cluster 11 . . . . . . . . . . . PIRC12 . . . piwi-interacting RNA cluster 12 . . . . . . . . . . . PIRC13 . . . piwi-interacting RNA cluster 13 . . . . . . . . . . . PIRC14 . . . piwi-interacting RNA cluster 14 . . . . . . . . . . . PIRC15 . . . piwi-interacting RNA cluster 15 . . . . . . . . . . . PIRC16 . . . piwi-interacting RNA cluster 16 . . . . . . . . . . . PIRC17 . . . piwi-interacting RNA cluster 17 . . . . . . . . . . . PIRC18 . . . piwi-interacting RNA cluster 18 . . . . . . . . . . . PIRC19 . . . piwi-interacting RNA cluster 19 . . . . . . . . . . . PIRC20 . . . piwi-interacting RNA cluster 20 . . . . . . . . . . . PIRC21 . . . piwi-interacting RNA cluster 21 . . . . . . . . . . . PIRC22 . . . piwi-interacting RNA cluster 22 . . . . . . . . . . . PIRC23 . . . piwi-interacting RNA cluster 23 . . . . . . . . . . . PIRC24 . . . piwi-interacting RNA cluster 24 . . . . . . . . . . . PIRC25 . . . piwi-interacting RNA cluster 25 . . . . . . . . . . . PIRC26 . . . piwi-interacting RNA cluster 26 . . . . . . . . . . . PIRC27 . . . piwi-interacting RNA cluster 27 . . . . . . . . . . . PIRC28 . . . piwi-interacting RNA cluster 28 . . . . . . . . . . . PIRC29 . . . piwi-interacting RNA cluster 29 . . . . . . . . . . . PIRC30 . . . piwi-interacting RNA cluster 30 . . . . . . . . . . . PIRC31 . . . piwi-interacting RNA cluster 31 . . . . . . . . . . . PIRC32 . . . piwi-interacting RNA cluster 32 . . . . . . . . . . . PIRC33 . . . piwi-interacting RNA cluster 33 . . . . . . . . . . . PIRC34 . . . piwi-interacting RNA cluster 34 . . . . . . . . . . . PIRC35 . . . piwi-interacting RNA cluster 35 . . . . . . . . . . . PIRC36 . . . piwi-interacting RNA cluster 36 . . . . . . . . . . . PIRC37 . . . piwi-interacting RNA cluster 37 . . . . . . . . . . . PIRC38 . . . piwi-interacting RNA cluster 38 . . . . . . . . . . . PIRC39 . . . piwi-interacting RNA cluster 39 . . . . . . . . . . . PIRC40 . . . piwi-interacting RNA cluster 40 . . . . . . . . . . . PIRC41 . . . piwi-interacting RNA cluster 41 . . . . . . . . . . . PIRC42 . . . piwi-interacting RNA cluster 42 . . . . . . . . . . . PIRC43 . . . piwi-interacting RNA cluster 43 . . . . . . . . . . . PIRC44 . . . piwi-interacting RNA cluster 44 . . . . . . . . . . . PIRC45 . . . piwi-interacting RNA cluster 45 . . . . . . . . . . . PIRC46 . . . piwi-interacting RNA cluster 46 . . . . . . . . . . . PIRC47 . . . piwi-interacting RNA cluster 47 . . . . . . . . . . . PIRC48 . . . piwi-interacting RNA cluster 48 . . . . . . . . . . . PIRC49 . . . piwi-interacting RNA cluster 49 . . . . . . . . . . . PIRC50 . . . piwi-interacting RNA cluster 50 . . . . . . . . . . . PIRC51 . . . piwi-interacting RNA cluster 51 . . . . . . . . . . . PIRC52 . . . piwi-interacting RNA cluster 52 . . . . . . . . . . . PIRC53 . . . piwi-interacting RNA cluster 53 . . . . . . . . . . . PIRC54 . . . piwi-interacting RNA cluster 54 . . . . . . . . . . . PIRC55 . . . piwi-interacting RNA cluster 55 . . . . . . . . . . . PIRC56 . . . piwi-interacting RNA cluster 56 . . . . . . . . . . . PIRC57 . . . piwi-interacting RNA cluster 57 . . . . . . . . . . . PIRC58 . . . piwi-interacting RNA cluster 58 . . . . . . . . . . . PIRC59 . . . piwi-interacting RNA cluster 59 . . . . . . . . . . . PIRC60 . . . piwi-interacting RNA cluster 60 . . . . . . . . . . . PIRC61 . . . piwi-interacting RNA cluster 61 . . . . . . . . . . . PIRC62 . . . piwi-interacting RNA cluster 62 . . . . . . . . . . . PIRC63 . . . piwi-interacting RNA cluster 63 . . . . . . . . . . . PIRC64 . . . piwi-interacting RNA cluster 64 . . . . . . . . . . . PIRC65 . . . piwi-interacting RNA cluster 65 . . . . . . . . . . . PIRC66 . . . piwi-interacting RNA cluster 66 . . . . . . . . . . . PIRC67 . . . piwi-interacting RNA cluster 67 . . . . . . . . . . . PIRC68 . . . piwi-interacting RNA cluster 68 . . . . . . . . . . . PIRC69 . . . piwi-interacting RNA cluster 69 . . . . . . . . . . . PIRC70 . . . piwi-interacting RNA cluster 70 . . . . . . . . . . . PIRC71 . . . piwi-interacting RNA cluster 71 . . . . . . . . . . . PIRC72 . . . piwi-interacting RNA cluster 72 . . . . . . . . . . . PIRC73 . . . piwi-interacting RNA cluster 73 . . . . . . . . . . . PIRC74 . . . piwi-interacting RNA cluster 74 . . . . . . . . . . . PIRC75 . . . piwi-interacting RNA cluster 75 . . . . . . . . . . . PIRC76 . . . piwi-interacting RNA cluster 76 . . . . . . . . . . . PIRC77 . . . piwi-interacting RNA cluster 77 . . . . . . . . . . . PIRC78 . . . piwi-interacting RNA cluster 78 . . . . . . . . . . . PIRC79 . . . piwi-interacting RNA cluster 79 . . . . . . . . . . . PIRC80 . . . piwi-interacting RNA cluster 80 . . . . . . . . . . . PIRC81 . . . piwi-interacting RNA cluster 81 . . . . . . . . . . . PIRC82 . . . piwi-interacting RNA cluster 82 . . . . . . . . . . . PIRC83 . . . piwi-interacting RNA cluster 83 . . . . . . . . . . . PIRC84 . . . piwi-interacting RNA cluster 84 . . . . . . . . . . . PIRC85 . . . piwi-interacting RNA cluster 85 . . . . . . . . . . . PIRC86 . . . piwi-interacting RNA cluster 86 . . . . . . . . . . . PIRC87 . . . piwi-interacting RNA cluster 87 . . . . . . . . . . . PIRC88 . . . piwi-interacting RNA cluster 88 . . . . . . . . . . . PIRC89 . . . piwi-interacting RNA cluster 89 . . . . . . . . . . . PIRC90 . . . piwi-interacting RNA cluster 90 . . . . . . . . . . . PIRC91 . . . piwi-interacting RNA cluster 91 . . . . . . . . . . . PIRC92 . . . piwi-interacting RNA cluster 92 . . . . . . . . . . . PIRC93 . . . piwi-interacting RNA cluster 93 . . . . . . . . . . . PIRC94 . . . piwi-interacting RNA cluster 94 . . . . . . . . . . . PIRC95 . . . piwi-interacting RNA cluster 95 . . . . . . . . . . . PIRC96 . . . piwi-interacting RNA cluster 96 . . . . . . . . . . . PIRC97 . . . piwi-interacting RNA cluster 97 . . . . . . . . . . . PIRC98 . . . piwi-interacting RNA cluster 98 . . . . . . . . . . . PIRC99 . . . piwi-interacting RNA cluster 99 . . . . . . . . . . . PIRC100 . . . piwi-interacting RNA cluster 100 . . . . . . . . . . . PIRC101 . . . piwi-interacting RNA cluster 101 . . . . . . . . . . . PIRC102 . . . piwi-interacting RNA cluster 102 . . . . . . . . . . . PIRC103 . . . piwi-interacting RNA cluster 103 . . . . . . . . . . . PIRC104 . . . piwi-interacting RNA cluster 104 . . . . . . . . . . . PIRC105 . . . piwi-interacting RNA cluster 105 . . . . . . . . . . . PIRC106 . . . piwi-interacting RNA cluster 106 . . . . . . . . . . . PIRC107 . . . piwi-interacting RNA cluster 107 . . . . . . . . . . . PIRC108 . . . piwi-interacting RNA cluster 108 . . . . . . . . . . . PIRC109 . . . piwi-interacting RNA cluster 109 . . . . . . . . . . . PIRC110 . . . piwi-interacting RNA cluster 110 . . . . . . . . . . . PIRC111 . . . piwi-interacting RNA cluster 111 . . . . . . . . . . . PIRC112 . . . piwi-interacting RNA cluster 112 . . . . . . . . . . . PIRC113 . . . piwi-interacting RNA cluster 113 . . . . . . . . . . . PIRC114 . . . piwi-interacting RNA cluster 114 . . . . . . . . . . . PIRT 0.150384795626214 0.63314739304709 0.216467811326695 phosphoinositide-interacting regulator of transient receptor potential channels FUNCTION: Regulatory subunit of TRPV1, a molecular sensor of noxious heat and capsaicin. Positively regulates TRPV1 channel activity via phosphatidylinositol 4,5-bisphosphate (PIP2). Binds various phosphoinositide, including phosphatidylinositol 4,5- bisphosphate (PIP2), but not phosphatidylinositol (PI) (By similarity). {ECO:0000250}.; . . . . . . 0.080983847 59.76055674 56.44774 1.51036 PISD 0.840252300973845 0.159114506768725 0.00063319225743057 phosphatidylserine decarboxylase FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. {ECO:0000255|HAMAP-Rule:MF_03208}.; . . ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;placenta;head and neck;kidney;stomach;thymus;cerebellum; . 0.90525 0.19510 -0.268115223 34.70747818 193.29214 3.01608 PISRT1 . . . polled intersex syndrome regulated transcript 1 (non-protein coding RNA) . . . . . . . . . . . PITHD1 0.102416722752494 0.864709705843151 0.0328735714043548 PITH (C-terminal proteasome-interacting domain of thioredoxin-like) domain containing 1 . . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; whole brain;amygdala;occipital lobe;globus pallidus;cerebellum;bone marrow; 0.24078 0.11809 . . 3.63195 0.13349 PITPNA 0.929437924643375 0.0705467888488552 1.52865077694877e-05 phosphatidylinositol transfer protein alpha FUNCTION: Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.; . TISSUE SPECIFICITY: Expressed in a wide range of tissues.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; whole brain;thalamus;subthalamic nucleus;occipital lobe;cerebellum peduncles;hypothalamus;globus pallidus;parietal lobe;cerebellum; 0.54955 0.14909 -0.295622497 32.61972163 3.74906 0.13944 PITPNA-AS1 . . . PITPNA antisense RNA 1 . . . . . . . . . . . PITPNB 0.974445019359892 0.0255256569328158 2.93237072925079e-05 phosphatidylinositol transfer protein beta FUNCTION: Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.; . TISSUE SPECIFICITY: Widely expressed in various tissues including brain.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;breast;bile duct;pancreas;lung;adrenal gland;mesenchyma;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.32024 0.13151 0.12325821 62.38499646 1.23583 0.04329 PITPNC1 0.967498710994397 0.0324904996360517 1.07893695508084e-05 phosphatidylinositol transfer protein, cytoplasmic 1 FUNCTION: Phosphatidylinositol transfer proteins mediate the monomeric transport of lipids by shielding a lipid from the aqueous environment and binding the lipid in a hydrophobic cavity. Able to transfer phosphatidylinositol in vitro. {ECO:0000269|PubMed:10531358}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10531358}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;breast;lung;nasopharynx;placenta;macula lutea;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.62678 0.09598 . . 10.9347 0.39565 PITPNM1 0.722090613819786 0.277909343657616 4.25225978983881e-08 phosphatidylinositol transfer protein membrane associated 1 FUNCTION: Regulates RHOA activity, and plays a role in cytoskeleton remodeling. Necessary for normal completion of cytokinesis. Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus. Binds phosphatidyl inositol phosphates (in vitro). May catalyze the transfer of phosphatidylinositol and phosphatidylcholine between membranes (By similarity). Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus. Required for protein export from the endoplasmic reticulum and the Golgi. Binds calcium ions. {ECO:0000250, ECO:0000269|PubMed:10022914, ECO:0000269|PubMed:11909959, ECO:0000269|PubMed:15545272, ECO:0000269|PubMed:15723057}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10022914}.; ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;endometrium;larynx;thyroid;bone;iris;germinal center;brain;unclassifiable (Anatomical System);amygdala;cartilage;islets of Langerhans;hypothalamus;pharynx;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; thalamus;subthalamic nucleus;medulla oblongata;cerebellum peduncles;temporal lobe;caudate nucleus;atrioventricular node;pons;skeletal muscle;parietal lobe;cingulate cortex;cerebellum; 0.12917 0.15037 -1.010461444 8.197688134 187.24709 2.97183 PITPNM2 0.999993632310422 6.36768956869587e-06 9.56956614426428e-15 phosphatidylinositol transfer protein membrane associated 2 FUNCTION: Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes (in vitro). Binds calcium ions. {ECO:0000269|PubMed:10022914}.; . TISSUE SPECIFICITY: Highly expressed in brain, heart, ovary, testis and thymus. Detected in small intestine, prostate, pancreas, skeletal muscle, liver, colon and placenta. {ECO:0000269|PubMed:10022914}.; ovary;choroid;fovea centralis;skin;retina;uterus;optic nerve;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pineal body;lens;pancreas;lung;placenta;visual apparatus;macula lutea;hypopharynx;spleen;head and neck;mammary gland;stomach;thymus; superior cervical ganglion;appendix;globus pallidus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.15763 0.12037 -1.899770452 1.963906582 750.7814 5.43369 PITPNM3 0.999503783305149 0.000496216616305776 7.85454097319955e-11 PITPNM family member 3 FUNCTION: Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes (in vitro) (By similarity). Binds calcium ions. {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in brain and spleen, and at low levels in ovary. {ECO:0000269|PubMed:10022914}.; unclassifiable (Anatomical System);pancreas;lung;ovary;muscle;testis;cervix;brain; superior cervical ganglion;medulla oblongata;subthalamic nucleus;globus pallidus;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.53739 0.11060 -1.3889361 4.311158292 950.06926 5.96807 PITRM1 7.16194900224229e-16 0.192931146419485 0.807068853580514 pitrilysin metallopeptidase 1 FUNCTION: ATP-independent protease that degrades mitochondrial transit peptides after their cleavage. Also degrades other unstructured peptides. Specific for peptides in the range of 10 to 65 residues. Able to degrade amyloid beta A4 (APP) protein when it accumulates in mitochondrion, suggesting a link with Alzheimer disease. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. {ECO:0000269|PubMed:16849325}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in muscle and heart compared to brain, pancreas, liver, lung and placenta. {ECO:0000269|PubMed:10360838}.; ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;cerebellum; whole brain;thalamus;testis - interstitial;heart;prefrontal cortex;testis;pons;skeletal muscle; 0.09989 0.17270 3.215903205 99.35715971 3783.48611 12.04965 PITRM1-AS1 . . . PITRM1 antisense RNA 1 . . . . . . . . . . . PITX1 0.273516400735677 0.702574918865353 0.0239086803989692 paired like homeodomain 1 FUNCTION: May play a role in the development of anterior structures, and in particular, the brain and facies and in specifying the identity or structure of hindlimb.; DISEASE: Clubfoot, congenital, with or without deficiency of long bones and/or mirror-image polydactyly (CCF) [MIM:119800]: A congenital limb deformity defined as fixation of the foot in cavus, adductus, varus, and equinus (i.e., inclined inwards, axially rotated outwards, and pointing downwards) with concomitant soft tissue abnormalities. Clubfoot may occur in isolation or as part of a syndrome. Some patients present tibial hemimelia, bilateral patellar hypoplasia, and preaxial mirror-image polydactyly. {ECO:0000269|PubMed:18950742, ECO:0000269|PubMed:22258522}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Liebenberg syndrome (LBNBG) [MIM:186550]: An upper limb- malformation syndrome characterized by the combination of dysplastic elbow joints and the fusion of wrist bones with consequent radial deviation. {ECO:0000269|PubMed:23022097}. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving the PITX1 locus results in LBNBG. Translocation t(5;18)(q31.1;q12.3). Additionally, two chromosome 5 deletions located 5'of PITX1 have been found in LBNBG patients. These structural variations cause altered expression of PITX1 in the forelimb via the activation of ectopic enhancers (PubMed:23022097). {ECO:0000269|PubMed:23022097}.; . ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;uterus;prostate;optic nerve;whole body;oesophagus;bone;pituitary gland;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;tongue;tumor;pituitary;tonsil;skeletal muscle; 0.62778 0.27322 -0.139478553 43.29440906 3127.07289 10.63695 PITX2 0.672788795640444 0.322347166287391 0.00486403807216532 paired like homeodomain 2 FUNCTION: Controls cell proliferation in a tissue-specific manner and is involved in morphogenesis. During embryonic development, exerts a role in the expansion of muscle progenitors. May play a role in the proper localization of asymmetric organs such as the heart and stomach. Isoform PTX2C is involved in left-right asymmetry the developing embryo (By similarity). {ECO:0000250}.; DISEASE: Axenfeld-Rieger syndrome 1 (RIEG1) [MIM:180500]: An autosomal dominant disorder of morphogenesis that results in abnormal development of the anterior segment of the eye, and results in blindness from glaucoma in approximately 50% of affected individuals. Additional features include aniridia, maxillary hypoplasia, hypodontia, anal stenosis, redundant periumbilical skin. {ECO:0000269|PubMed:10937553, ECO:0000269|PubMed:11487566, ECO:0000269|PubMed:12381896, ECO:0000269|PubMed:16936096, ECO:0000269|PubMed:8944018}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Iridogoniodysgenesis 2 (IRID2) [MIM:137600]: Autosomal dominant inherited disease. {ECO:0000269|PubMed:9437321, ECO:0000269|PubMed:9618168}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peters anomaly (PETAN) [MIM:604229]: Consists of a central corneal leukoma, absence of the posterior corneal stroma and Descemet membrane, and a variable degree of iris and lenticular attachments to the central aspect of the posterior cornea. {ECO:0000269|PubMed:10051017}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ring dermoid of cornea (RDC) [MIM:180550]: An ocular disorder characterized by bilateral annular limbal dermoids (growths with a skin-like structure) with corneal and conjunctival extension. {ECO:0000269|PubMed:15591271, ECO:0000269|PubMed:22224469}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;developmental;intestine;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;bone;pituitary gland;testis;bladder;brain;unclassifiable (Anatomical System);heart;tongue;muscle;pharynx;blood;lens;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney; superior cervical ganglion; 0.98807 0.63460 -0.337894035 30.37272942 16.74042 0.58887 PITX3 0.768360298132641 0.223498966160521 0.00814073570683795 paired like homeodomain 3 FUNCTION: Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. In addition to its importance during development, it also has roles in the long-term survival and maintenance of the mdDA neurons. Activates NR4A2/NURR1- mediated transcription of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons. Acts by decreasing the interaction of NR4A2/NURR1 with the corepressor NCOR2/SMRT which acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in a repressed deacetylated state. Essential for the normal lens development and differentiation. Plays a critical role in the maintenance of mitotic activity of lens epithelial cells, fiber cell differentiation and in the control of the temporal and spatial activation of fiber cell-specific crystallins. Positively regulates FOXE3 expression and negatively regulates PROX1 in the anterior lens epithelium, preventing activation of CDKN1B/P27Kip1 and CDKN1C/P57Kip2 and thus maintains lens epithelial cells in cell cycle (By similarity). {ECO:0000250}.; DISEASE: Cataract 11, multiple types (CTRCT11) [MIM:610623]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT11 includes posterior polar cataract, among others. Posterior polar cataract is a subcapsular opacity, usually disk-shaped, located at the back of the lens. Some CTRCT11 patients can present a severe phenotype including microphthalmia and neurological dysfunction. {ECO:0000269|PubMed:15286169, ECO:0000269|PubMed:9620774}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in developing eye lens.; . . 0.44533 0.19268 . . 13.31894 0.48386 PIWIL1 2.12575606834247e-07 0.999735959290859 0.000263828133534283 piwi-like RNA-mediated gene silencing 1 FUNCTION: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Directly binds methylated piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation. Probable component of some RISC complex, which mediates RNA cleavage and translational silencing. Also plays a role in the formation of chromatoid bodies and is required for some miRNAs stability (By similarity). Isoform 3 may be a negative developmental regulator. {ECO:0000250, ECO:0000269|PubMed:12037681, ECO:0000269|PubMed:14749716, ECO:0000269|PubMed:16287078}.; . TISSUE SPECIFICITY: Expressed in spermatocytes and spermatids. Also detected in prostate cancer (at protein level). Detected in most fetal and adult tissues. Expressed in testes, specifically in germline cells; detected in spermatocytes and spermatids during spermatogenesis. Increased expression in testicular tumors originating from embryonic germ cells with retention of germ cells phenotype. No expression in testicular tumors of somatic origin, such as Sertoli cell and Leydig cell tumors. Overexpressed in gastric cancer cells. Isoform 3 is ubiquitously expressed, and specifically in CD34+ hematopoietic progenitor cells but not in more differentiated cells. {ECO:0000269|PubMed:11154219, ECO:0000269|PubMed:12037681, ECO:0000269|PubMed:12906857, ECO:0000269|PubMed:23436708}.; unclassifiable (Anatomical System);uterus;lung;macula lutea;testis;colon;fovea centralis;skeletal muscle;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;pons;trigeminal ganglion;skeletal muscle; 0.27576 0.09921 -0.464712395 23.5727766 772.66548 5.50094 PIWIL2 0.0024831521594482 0.997511324559317 5.52328123490218e-06 piwi-like RNA-mediated gene silencing 2 FUNCTION: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiation and in self-renewal of spermatogonial stem cells. Its presence in oocytes suggests that it may participate in similar functions during oogenesis in females. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer- independent mechanism and are primarily derived from transposons and other repeated sequence elements. Associates with primary piRNAs in the cytoplasm and is required for PIWIL4/MIWI2 nuclear localization and association with secondary piRNAs antisense. The piRNA process acts upstream of known mediators of DNA methylation. Participates in a piRNA amplification loop. Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation. Indirectly modulate expression of genes such as PDGFRB, SLC2A1, ITGA6, GJA7, THY1, CD9 and STRA8. Inhibits tumor cell growth when repressed. When overexpressed, acts as an oncogene by inhibition of apoptosis and promotion of proliferation in tumors (By similarity). {ECO:0000250, ECO:0000269|PubMed:16377660}.; . TISSUE SPECIFICITY: Expressed in adult testis and in most tumors. {ECO:0000269|PubMed:16377660}.; unclassifiable (Anatomical System);testis;brain;skeletal muscle; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06667 0.08666 -0.345391639 29.61193678 286.91946 3.62877 PIWIL3 9.86575487560156e-26 0.000441109599358054 0.999558890400642 piwi-like RNA-mediated gene silencing 3 FUNCTION: May play a role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:12906857}.; unclassifiable (Anatomical System); superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.09051 0.08540 2.434539058 98.54328851 652.20821 5.12305 PIWIL4 7.41292866543896e-06 0.99903433222626 0.00095825484507411 piwi-like RNA-mediated gene silencing 4 FUNCTION: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer- independent mechanism and are primarily derived from transposons and other repeated sequence elements. Associates with secondary piRNAs antisense and PIWIL2/MILI is required for such association. The piRNA process acts upstream of known mediators of DNA methylation. Participates in a piRNA amplification loop. Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation (By similarity). May be involved in the chromatin-modifying pathway by inducing 'Lys-9' methylation of histone H3 at some loci. {ECO:0000250, ECO:0000269|PubMed:12906857}.; . TISSUE SPECIFICITY: Expressed in testis. According to PubMed:17544373, it is ubiquitously expressed. {ECO:0000269|PubMed:17544373}.; unclassifiable (Anatomical System);ovary;colon;blood;fovea centralis;choroid;lens;bone marrow;retina;pancreas;optic nerve;whole body;lung;macula lutea;testis;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.09531 0.09236 1.269496963 93.63057325 1802.50922 7.83469 PJA1 0.894042634793692 0.105743279709589 0.000214085496719036 praja ring finger ubiquitin ligase 1 FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome (By similarity). May be involved in protein sorting. {ECO:0000250, ECO:0000269|PubMed:12036302}.; . TISSUE SPECIFICITY: Expressed in various regions of the brain including the cerebellum, cerebral cortex, medulla, occipital pole, frontal lobe, temporal lobe and putamen. Highest levels in the cerebral cortex. {ECO:0000269|PubMed:12036302}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;iris;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;skeletal muscle;bile duct;greater omentum;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; amygdala;whole brain;subthalamic nucleus;medulla oblongata;superior cervical ganglion;fetal brain;prefrontal cortex;globus pallidus;testis;pons;parietal lobe; 0.06013 0.13121 0.442818085 77.8544468 424.16395 4.30208 PJA2 0.466603861583053 0.53316397895478 0.000232159462167508 praja ring finger ubiquitin ligase 2 FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity. Responsible for ubiquitination of cAMP-dependent protein kinase type I and type II-alpha/beta regulatory subunits and for targeting them for proteasomal degradation. Essential for PKA- mediated long-term memory processes. {ECO:0000269|PubMed:12036302, ECO:0000269|PubMed:21423175}.; . . ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;parotid gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;pia mater;lung;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta;thymus; amygdala;subthalamic nucleus;occipital lobe;medulla oblongata;hypothalamus;temporal lobe;prefrontal cortex;globus pallidus;caudate nucleus;pons;cingulate cortex;parietal lobe; 0.32444 0.09509 -0.132199953 43.97853267 2997.44585 10.38957 PKD1 0.999905331991465 9.46680085346985e-05 7.89207256034668e-19 polycystin 1, transient receptor potential channel interacting FUNCTION: Involved in renal tubulogenesis (PubMed:12482949). Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (By similarity). Acts as a regulator of cilium length, together with PKD2 (By similarity). The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling (By similarity). The cilium length response creates a negative feedback loop whereby fluid shear- mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling (By similarity). May be an ion-channel regulator. Involved in adhesive protein-protein and protein- carbohydrate interactions. {ECO:0000250|UniProtKB:O08852, ECO:0000269|PubMed:12482949}.; DISEASE: Polycystic kidney disease 1 (PKD1) [MIM:173900]: A disorder characterized by renal cysts, liver cysts and intracranial aneurysm. Clinical variability is due to differences in the rate of loss of glomerular filtration, the age of reaching end-stage renal disease and the occurrence of hypertension, symptomatic extrarenal cysts, and subarachnoid hemorrhage from intracranial 'berry' aneurysm. {ECO:0000269|PubMed:10200984, ECO:0000269|PubMed:10364515, ECO:0000269|PubMed:10577909, ECO:0000269|PubMed:10647901, ECO:0000269|PubMed:10729710, ECO:0000269|PubMed:10854095, ECO:0000269|PubMed:10923040, ECO:0000269|PubMed:10987650, ECO:0000269|PubMed:11012875, ECO:0000269|PubMed:11058904, ECO:0000269|PubMed:11115377, ECO:0000269|PubMed:11216660, ECO:0000269|PubMed:11316854, ECO:0000269|PubMed:11558899, ECO:0000269|PubMed:11571556, ECO:0000269|PubMed:11691639, ECO:0000269|PubMed:11773467, ECO:0000269|PubMed:11857740, ECO:0000269|PubMed:11967008, ECO:0000269|PubMed:12007219, ECO:0000269|PubMed:12070253, ECO:0000269|PubMed:12220456, ECO:0000269|PubMed:12842373, ECO:0000269|PubMed:15772804, ECO:0000269|PubMed:18837007, ECO:0000269|PubMed:21115670, ECO:0000269|PubMed:22508176, ECO:0000269|PubMed:8554072, ECO:0000269|PubMed:9199561, ECO:0000269|PubMed:9259200, ECO:0000269|PubMed:9285784, ECO:0000269|PubMed:9521593, ECO:0000269|PubMed:9921908}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;urinary;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;placenta;hypopharynx;amnion;head and neck;kidney;stomach;thymus;cerebellum; amygdala;medulla oblongata;subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;prefrontal cortex;globus pallidus;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.71863 . . . 3055.5228 10.50526 PKD1L1 1.72329201787273e-23 0.999996492252223 3.50774777683693e-06 polycystin 1 like 1, transient receptor potential channel interacting FUNCTION: Component of a ciliary calcium channel that controls calcium concentration within primary cilia without affecting cytoplasmic calcium concentration. Forms a heterodimer with PKD2L1 in primary cilia and forms a calcium-permeant ciliary channel that regulates sonic hedgehog/SHH signaling and GLI2 transcription. Does not constitute the pore-forming subunit. Also involved in left/right axis specification downstream of nodal flow: forms a complex with PKD2 in cilia to facilitate flow detection in left/right patterning. {ECO:0000269|PubMed:24336289}.; . TISSUE SPECIFICITY: Detected in testis and in fetal and adult heart.; unclassifiable (Anatomical System);lung;endometrium;placenta;testis;brain;retina; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;thyroid;temporal lobe;liver;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07124 . 2.171086137 98.04788865 3392.60955 11.14655 PKD1L2 2.36605828568027e-09 0.020877048832658 0.979122948801284 polycystin 1 like 2 (gene/pseudogene) FUNCTION: May function as an ion-channel regulator. May function as a G-protein-coupled receptor. {ECO:0000269|PubMed:15203210}.; . TISSUE SPECIFICITY: Expressed in all tissues tested including brain, placenta, mammary gland, testis, lung and liver. Highest expression in skeletal muscle. Isoform 2 is expressed in heart and kidney. {ECO:0000269|PubMed:12782129}.; unclassifiable (Anatomical System);lymph node;lung;testis;mammary gland;skin; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skin;skeletal muscle; 0.09644 0.07722 6.86111443 99.88794527 . . PKD1L3 . . . polycystin 1 like 3, transient receptor potential channel interacting FUNCTION: Component of a calcium channel. May act as a sour taste receptor by forming a calcium channel with PKD1L3 in gustatory cells; however, its contribution to sour taste perception is unclear in vivo and may be indirect. {ECO:0000269|PubMed:12782129, ECO:0000269|PubMed:19812697, ECO:0000269|PubMed:23212381}.; . TISSUE SPECIFICITY: Highly expressed in placenta, weakly in heart and lung. {ECO:0000269|PubMed:12782129}.; placenta;colon;retina; . . 0.11058 . . . . PKD1P1 . . . polycystin 1, transient receptor potential channel interacting pseudogene 1 . . . . . . . . . . . PKD1P2 . . . polycystin 1, transient receptor potential channel interacting pseudogene 2 . . . . . . . . . . . PKD1P3 . . . polycystin 1, transient receptor potential channel interacting pseudogene 3 . . . . . . . . . . . PKD1P4 . . . polycystin 1, transient receptor potential channel interacting pseudogene 4 . . . . . . . . . . . PKD1P5 . . . polycystin 1, transient receptor potential channel interacting pseudogene 5 . . . . . . . . . . . PKD1P6 . . . polycystin 1, transient receptor potential channel interacting pseudogene 6 . . . smooth muscle;ovary;colon;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;larynx;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;blood;skeletal muscle;breast;pancreas;pia mater;lung;placenta;visual apparatus;hypopharynx;amnion;spleen;head and neck;mammary gland;cerebellum; . . . . . . . PKD2 0.995277859575451 0.0047221402662727 1.5827648643677e-10 polycystin 2, transient receptor potential cation channel FUNCTION: Functions as a calcium permeable cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium. Together with TRPV4, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). PKD1 and PKD2 may function through a common signaling pathway that is necessary for normal tubulogenesis. Acts as a regulator of cilium length, together with PKD1. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. Also involved in left/right axis specification downstream of nodal flow: forms a complex with PKD1L1 in cilia to facilitate flow detection in left/right patterning (By similarity). {ECO:0000250|UniProtKB:O35245, ECO:0000269|PubMed:18695040}.; DISEASE: Polycystic kidney disease 2 (PKD2) [MIM:613095]: A disorder characterized by progressive formation and enlargement of cysts in both kidneys, typically leading to end-stage renal disease in adult life. Cysts also occurs in the liver and other organs. It represents approximately 15% of the cases of autosomal dominant polycystic kidney disease. PKD2 is clinically milder than PKD1 but it has a deleterious impact on overall life expectancy. {ECO:0000269|PubMed:10411676, ECO:0000269|PubMed:10541293, ECO:0000269|PubMed:10835625, ECO:0000269|PubMed:11968093, ECO:0000269|PubMed:12707387, ECO:0000269|PubMed:14993477, ECO:0000269|PubMed:15772804, ECO:0000269|PubMed:21115670, ECO:0000269|PubMed:9326320}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Strongly expressed in ovary, fetal and adult kidney, testis, and small intestine. Not detected in peripheral leukocytes. {ECO:0000269|PubMed:8650545}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach; uterus;trigeminal ganglion; 0.86513 0.31355 -0.707227564 14.71455532 1814.9201 7.85632 PKD2L1 6.57113540225805e-17 0.0504529024640373 0.949547097535963 polycystin 2 like 1, transient receptor potential cation channel FUNCTION: Pore-forming subunit of a ciliary calcium channel that controls calcium concentration within primary cilia without affecting cytoplasmic calcium concentration. Forms a heterodimer with PKD1L1 in primary cilia and forms a calcium-permeant ciliary channel that regulates sonic hedgehog/SHH signaling and GLI2 transcription. May act as a sour taste receptor by forming a calcium channel with PKD1L3 in gustatory cells; however, its contribution to sour taste perception is unclear in vivo and may be indirect. {ECO:0000269|PubMed:10517637, ECO:0000269|PubMed:19812697, ECO:0000269|PubMed:23212381, ECO:0000269|PubMed:24336289}.; . TISSUE SPECIFICITY: Expressed in adult heart, skeletal muscle, brain, spleen, testis, retina and liver. According to PubMed:9748274, expressed at high levels in fetal tissues, including kidney and liver, and down-regulated in adult tissues. According to PubMed:10602361, expressed in fetal brain, but not expressed in fetal lung, liver or kidney. Isoform 4 appears to be expressed only in transformed lymphoblasts. {ECO:0000269|PubMed:10602361, ECO:0000269|PubMed:9748274}.; unclassifiable (Anatomical System);alveolus;testis;retina; skeletal muscle; 0.45343 0.12014 1.006742856 90.79971691 3481.90583 11.35988 PKD2L2 3.49693117527093e-07 0.984971039989192 0.0150286103176909 polycystin 2 like 2, transient receptor potential cation channel FUNCTION: May function as a subunit of a cation channel and play a role in fertilization.; . TISSUE SPECIFICITY: According to PubMed:10602361, expressed only in testis. According to PubMed:10756092, expressed also in brain and kidney. Isoform 2 is found only in transformed lymphoblasts. Isoform 3 is found in all tissues tested.; unclassifiable (Anatomical System);lymph node;ovary;blood;parathyroid;skin;bone marrow;breast;lung;whole body;placenta;hippocampus;testis;amniotic fluid; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.37181 0.10351 -0.222203495 37.54423213 91.43805 2.05606 PKD3 . . . polycystic kidney disease 3 (autosomal dominant) . . . . . . . . . . . PKDCC 5.4125797267683e-05 0.682338064967538 0.317607809235195 protein kinase domain containing, cytoplasmic FUNCTION: Secreted tyrosine-protein kinase that mediates phosphorylation of extracellular proteins and endogenous proteins in the secretory pathway, which is essential for patterning at organogenesis stages. Mediates phosphorylation of MMP1, MMP13, MMP14, MMP19 and ERP29 (PubMed:25171405). Probably plays a role in platelets: rapidly and quantitatively secreted from platelets in response to stimulation of platelet degranulation (PubMed:25171405). May also have serine/threonine protein kinase activity. Required for longitudinal bone growth through regulation of chondrocyte differentiation. May be indirectly involved in protein transport from the Golgi apparatus to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q5RJI4, ECO:0000269|PubMed:25171405}.; . TISSUE SPECIFICITY: Highly expressed in platelets. {ECO:0000269|PubMed:25171405}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;synovium;testis;spinal ganglion;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion; . . . . 1359.0485 6.91987 PKDREJ 4.71093052032008e-20 0.00991424492259733 0.990085755077403 polycystin (PKD) family receptor for egg jelly FUNCTION: May have a central role in fertilization. May generate a Ca(2+) transporting channel directly involved in initiating the acrosome reaction of the sperm.; . TISSUE SPECIFICITY: Exclusively expressed in testis.; unclassifiable (Anatomical System);pancreas;islets of Langerhans; superior cervical ganglion;testis - interstitial;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07180 0.21527 -0.593676906 18.21774003 3291.07659 10.95148 PKHD1 2.88608936958615e-23 0.999999999976766 2.32335774448585e-11 polycystic kidney and hepatic disease 1 (autosomal recessive) FUNCTION: May be required for correct bipolar cell division through the regulation of centrosome duplication and mitotic spindle assembly. May be a receptor protein that acts in collecting-duct and biliary differentiation. {ECO:0000269|PubMed:20554582}.; . TISSUE SPECIFICITY: Predominantly expressed in fetal and adult kidney. In the kidney, it is found in the cortical and medullary collecting ducts. Also present in the adult pancreas, but at much lower levels. Detectable in fetal and adult liver. Rather indistinct signal in fetal brain. {ECO:0000269|PubMed:14978161, ECO:0000269|PubMed:15458427}.; unclassifiable (Anatomical System);liver;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.08201 0.25544 0.37824847 75.51309271 3737.47294 11.94762 PKHD1L1 9.12623254733104e-65 1.01673899193968e-07 0.999999898326101 polycystic kidney and hepatic disease 1 (autosomal recessive)-like 1 . . TISSUE SPECIFICITY: Ubiquitous. Expressed in spleen and thymus as well as in activated T-cells and B-lymphoblasts. {ECO:0000269|PubMed:12620974}.; . . 0.38442 0.10513 5.453048233 99.84666195 12241.38174 23.72246 PKIA 0.254973075890028 0.640645047718286 0.104381876391687 protein kinase (cAMP-dependent, catalytic) inhibitor alpha FUNCTION: Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.; . . ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;hippocampus;visual apparatus;liver; amygdala;superior cervical ganglion;occipital lobe;fetal brain;hypothalamus;prefrontal cortex;caudate nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21448 0.15588 0.189398298 66.31870724 0.64652 0.00956 PKIA-AS1 . . . PKIA antisense RNA 1 . . . . . . . . . . . PKIB 0.219496928302588 0.64761304933395 0.132890022363462 protein kinase (cAMP-dependent, catalytic) inhibitor beta FUNCTION: Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;colon;parathyroid;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;placenta;macula lutea;visual apparatus;liver;testis;spleen;brain;stomach;cerebellum; superior cervical ganglion;cerebellum peduncles;placenta;cerebellum; 0.01927 0.06773 0.013025609 54.62962963 8.34226 0.30538 PKIG 0.564580331450696 0.387119525026612 0.0483001435226923 protein kinase (cAMP-dependent, catalytic) inhibitor gamma FUNCTION: Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains. {ECO:0000250}.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;ganglion;endometrium;germinal center;bladder;brain;tonsil;heart;cartilage;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus; testis; 0.15103 0.11114 0.035072054 56.2514744 3.50135 0.12708 PKLR 1.00020289233933e-05 0.935829158886984 0.0641608390840923 pyruvate kinase, liver and RBC FUNCTION: Plays a key role in glycolysis. {ECO:0000250}.; DISEASE: Pyruvate kinase hyperactivity (PKHYP) [MIM:102900]: Autosomal dominant phenotype characterized by increase of red blood cell ATP. {ECO:0000269|PubMed:9090535}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pyruvate kinase deficiency of red cells (PKRD) [MIM:266200]: A frequent cause of hereditary non-spherocytic hemolytic anemia. Clinically, pyruvate kinase-deficient patients suffer from a highly variable degree of chronic hemolysis, ranging from severe neonatal jaundice and fatal anemia at birth, severe transfusion-dependent chronic hemolysis, moderate hemolysis with exacerbation during infection, to a fully compensated hemolysis without apparent anemia. {ECO:0000269|PubMed:11328279, ECO:0000269|PubMed:1536957, ECO:0000269|PubMed:1896471, ECO:0000269|PubMed:19085939, ECO:0000269|PubMed:2018831, ECO:0000269|PubMed:21794208, ECO:0000269|PubMed:7706479, ECO:0000269|PubMed:8161798, ECO:0000269|PubMed:8180378, ECO:0000269|PubMed:8476433, ECO:0000269|PubMed:8481523, ECO:0000269|PubMed:8483951, ECO:0000269|PubMed:9482576, ECO:0000269|PubMed:9827908, ECO:0000269|PubMed:9886305, ECO:0000269|Ref.24}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;ovary;salivary gland;intestine;pharynx;colon;blood;skin;pancreas;prostate;bone;visual apparatus;liver;spleen;kidney;brain;mammary gland;bladder; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.82714 0.75620 7.61E-05 53.98089172 81.73871 1.91644 PKM 0.994197406281851 0.00580243752357597 1.56194572774482e-07 pyruvate kinase, muscle FUNCTION: Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival. {ECO:0000269|PubMed:17308100, ECO:0000269|PubMed:18191611, ECO:0000269|PubMed:21620138}.; . TISSUE SPECIFICITY: Specifically expressed in proliferating cells, such as embryonic stem cells, embryonic carcinoma cells, as well as cancer cells. {ECO:0000269|PubMed:18191611}.; . . 0.77694 0.18070 -0.424258538 25.56027365 25.96104 0.84391 PKMP1 . . . pyruvate kinase, muscle pseudogene 1 . . . . . . . . . . . PKMP2 . . . pyruvate kinase, muscle pseudogene 2 . . . . . . . . . . . PKMP3 . . . pyruvate kinase, muscle pseudogene 3 . . . . . . . . . . . PKMP4 . . . pyruvate kinase, muscle pseudogene 4 . . . . . . . . . . . PKMP5 . . . pyruvate kinase, muscle pseudogene 5 . . . . . . . . . . . PKMYT1 0.667410731013562 0.331523198622377 0.00106607036406124 protein kinase, membrane associated tyrosine/threonine 1 FUNCTION: Acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylation of the CDK1 kinase specifically when CDK1 is complexed to cyclins. Mediates phosphorylation of CDK1 predominantly on 'Thr-14'. Also involved in Golgi fragmentation. May be involved in phosphorylation of CDK1 on 'Tyr-15' to a lesser degree, however tyrosine kinase activity is unclear and may be indirect. May be a downstream target of Notch signaling pathway during eye development. {ECO:0000269|PubMed:10373560, ECO:0000269|PubMed:9001210}.; . . lymphoreticular;medulla oblongata;ovary;developmental;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;ganglion;frontal lobe;oesophagus;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.36147 0.12042 -0.466531444 23.51380042 459.77368 4.44925 PKN1 0.8546946397822 0.145305192212195 1.68005605004026e-07 protein kinase N1 FUNCTION: PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser- 159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro. {ECO:0000269|PubMed:11104762, ECO:0000269|PubMed:12514133, ECO:0000269|PubMed:17332740, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:20188095, ECO:0000269|PubMed:21754995, ECO:0000269|PubMed:24248594, ECO:0000269|PubMed:8557118, ECO:0000269|PubMed:8621664, ECO:0000269|PubMed:9175763}.; . TISSUE SPECIFICITY: Found ubiquitously. Expressed in heart, brain, placenta, lung, skeletal muscle, kidney and pancreas. Expressed in numerous tumor cell lines, especially in breast tumor cells. {ECO:0000269|PubMed:21754995}.; lymphoreticular;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;tongue;muscle;blood;lens;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; tumor;white blood cells; 0.31787 0.49001 -0.96998676 8.958480774 3121.00071 10.61643 PKN2 0.999995222562088 4.77743790683195e-06 4.75260683899946e-15 protein kinase N2 FUNCTION: PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c- fos serum response factor (SRF). Phosphorylates HCV NS5B leading to stimulation of HCV RNA replication. {ECO:0000269|PubMed:10226025, ECO:0000269|PubMed:10926925, ECO:0000269|PubMed:11777936, ECO:0000269|PubMed:11781095, ECO:0000269|PubMed:15364941, ECO:0000269|PubMed:17332740, ECO:0000269|PubMed:20188095, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:21754995, ECO:0000269|PubMed:9121475}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in numerous tumor cell lines, especially in bladder tumor cells. {ECO:0000269|PubMed:10026169, ECO:0000269|PubMed:21754995}.; unclassifiable (Anatomical System);lung;islets of Langerhans;liver;testis;colon;skeletal muscle; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.52957 0.18687 -1.065444789 7.425100259 146.59854 2.63771 PKN2-AS1 . . . PKN2 antisense RNA 1 . . . . . . . . . . . PKN3 1.47314472009515e-09 0.986814952280164 0.0131850462466914 protein kinase N3 FUNCTION: Contributes to invasiveness in malignant prostate cancer. {ECO:0000269|PubMed:15282551}.; . TISSUE SPECIFICITY: Expressed in prostate tumors and various cancer cell lines. Not expressed in adult tissues. {ECO:0000269|PubMed:10441506}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;lens;pancreas;lung;placenta;macula lutea;visual apparatus;head and neck;cervix;kidney;stomach; atrioventricular node; 0.08003 0.30179 -0.745876353 13.76503892 284.23956 3.60885 PKNOX1 0.98655084446177 0.0134479318586535 1.22367957612483e-06 PBX/knotted 1 homeobox 1 . . TISSUE SPECIFICITY: Ubiquitous. Isoform 2 is expressed in all examined tissues except in bone marrow. {ECO:0000269|PubMed:15468914, ECO:0000269|PubMed:9143494}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;thyroid;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17665 0.14084 -0.47017169 23.25430526 35.42901 1.06945 PKNOX2 0.91736894679552 0.0826081748735715 2.28783309086602e-05 PBX/knotted 1 homeobox 2 . . . unclassifiable (Anatomical System);heart;ovary;cartilage;muscle;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;frontal lobe;thyroid;macula lutea;visual apparatus;liver;testis;head and neck;spleen;brain;mammary gland; dorsal root ganglion;whole brain;amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;fetal brain;thyroid;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.60016 0.12225 -0.800872469 12.33191791 399.25549 4.19460 PKNOX2-AS1 . . . PKNOX2 antisense RNA 1 (head to head) . . . . . . . . . . . PKP1 0.00480236370151161 0.993930765786682 0.00126687051180638 plakophilin 1 FUNCTION: Seems to play a role in junctional plaques. Contributes to epidermal morphogenesis. {ECO:0000269|PubMed:9326952}.; . TISSUE SPECIFICITY: Isoform 2 is widely expressed. Isoform 1 is expressed in stratified squamous, complex, glandular duct and bladder epithelia.; unclassifiable (Anatomical System);heart;tongue;colon;skin;skeletal muscle;breast;larynx;placenta;thyroid;hypopharynx;head and neck;brain;bladder;thymus; dorsal root ganglion;superior cervical ganglion;prostate;tongue;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.88271 0.16541 1.028790575 91.09459778 933.41524 5.92528 PKP2 6.1431013754488e-10 0.843776967833594 0.156223031552096 plakophilin 2 FUNCTION: May play a role in junctional plaques. {ECO:0000269|PubMed:22781308}.; . TISSUE SPECIFICITY: Detected in heart right ventricle (at protein level). Widely expressed. Found at desmosomal plaques in simple and stratified epithelia and in non-epithelial tissues such as myocardium and lymph node follicles. In most stratified epithelia found in the desmosomes of the basal cell layer and seems to be absent from suprabasal strata. {ECO:0000269|PubMed:10374264, ECO:0000269|PubMed:22781308}.; myocardium;ovary;colon;skin;retina;bone marrow;uterus;prostate;atrium;whole body;cerebral cortex;endometrium;gum;bone;testis;amniotic fluid;bladder;brain;unclassifiable (Anatomical System);heart;lacrimal gland;blood;skeletal muscle;lung;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;trigeminal ganglion; 0.68004 0.12345 0.652163325 84.17669262 1040.61604 6.19227 PKP2P1 . . . plakophilin 2 pseudogene 1 . . . . . . . . . . . PKP3 0.194350414769518 0.805198633657617 0.000450951572864384 plakophilin 3 FUNCTION: May play a role in junctional plaques.; . TISSUE SPECIFICITY: Isoform PKP3a is found in desmosomes of most simple and stratified epithelia. Not found in foreskin fibroblasts and various sarcoma-derived cell lines. Beside dendritic reticular cells of lymphatic follicles not found in non-epithelial desmosome-bearing tissues. Isoform PKP3b is abundant in the desmosomes of stratified epithelial cell but absent in simple epithelial cells, it is also expressed in the colon and its tumors. {ECO:0000269|PubMed:24178805}.; unclassifiable (Anatomical System);cartilage;ovary;heart;tongue;islets of Langerhans;colon;parathyroid;blood;skin;uterus;pancreas;prostate;whole body;lung;bone;placenta;hypopharynx;testis;cervix;head and neck;brain;mammary gland;stomach; superior cervical ganglion;tongue;placenta;trigeminal ganglion;skeletal muscle; 0.50658 0.11351 . . 238.13226 3.33382 PKP4 1.59819832523135e-05 0.999983483698908 5.34317839647399e-07 plakophilin 4 FUNCTION: Plays a role as a regulator of Rho activity during cytokinesis. May play a role in junctional plaques. {ECO:0000269|PubMed:17115030}.; . . . . 0.75315 0.12659 -1.076610636 7.324840764 273.10622 3.54308 PKP4P1 . . . plakophilin 4 pseudogene 1 . . . . . . . . . . . PLA1A 0.00169014777230665 0.97176534658149 0.0265445056462034 phospholipase A1 member A FUNCTION: Hydrolyzes the ester bond at the sn-1 position of glycerophospholipids and produces 2-acyl lysophospholipids. Hydrolyzes phosphatidylserine (PS) in the form of liposomes and 1- acyl-2 lysophosphatidylserine (lyso-PS), but not triolein, phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidic acid (PA) or phosphatidylinositol (PI). Isoform 2 hydrolyzes lyso-PS but not PS. Hydrolysis of lyso-PS in peritoneal mast cells activated by receptors for IgE leads to stimulate histamine production. {ECO:0000269|PubMed:10196188}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in placenta, prostate and liver. Weakly or not expressed in skin, leukocytes, platelets, colon, spleen, lung, muscle and kidney. {ECO:0000269|PubMed:9074642}.; unclassifiable (Anatomical System);meninges;heart;ovary;colon;parathyroid;skin;retina;uterus;prostate;pia mater;lung;nasopharynx;placenta;liver;testis;spleen;dura mater;kidney;brain;tonsil;stomach; . 0.08348 0.15694 0.88921411 89.24274593 447.79251 4.40127 PLA2G1B 3.64893028626161e-11 0.00346469475977781 0.996535305203733 phospholipase A2 group IB FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides, this releases glycerophospholipids and arachidonic acid that serve as the precursors of signal molecules. {ECO:0000269|PubMed:19297324}.; . . unclassifiable (Anatomical System);pancreas;lung;islets of Langerhans;testis;kidney; pancreas;beta cell islets; 0.38318 0.63165 -0.161524709 41.6430762 22.08097 0.74183 PLA2G2A 0.398124558137518 0.561882538323356 0.0399929035391259 phospholipase A2 group IIA FUNCTION: Thought to participate in the regulation of the phospholipid metabolism in biomembranes including eicosanoid biosynthesis. Catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides.; . . . . 0.27968 0.19538 0.014844891 54.94810097 36.92717 1.10511 PLA2G2C 0.000569562808573398 0.470707140977461 0.528723296213965 phospholipase A2 group IIC FUNCTION: Inactive phospholipase. {ECO:0000305}.; . . . . 0.06763 0.06776 . . 2653.24615 9.68279 PLA2G2D 0.000177682796600803 0.460287323735001 0.539534993468398 phospholipase A2 group IID FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. L-alpha-1-palmitoyl-2- linoleoyl phosphatidylethanolamine is more efficiently hydrolyzed than the other phospholipids examined.; . TISSUE SPECIFICITY: Broadly expressed.; . . 0.05776 0.08330 1.104245073 91.95564992 199.72449 3.05315 PLA2G2E 0.000343166465007747 0.374130934523008 0.625525899011984 phospholipase A2 group IIE FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids.; . TISSUE SPECIFICITY: Restricted to the brain, heart, lung, and placenta.; . . 0.17260 0.11760 0.12689526 63.00424628 304.59362 3.71619 PLA2G2F 2.09867850599463e-06 0.150458918355327 0.849538982966167 phospholipase A2 group IIF FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference. {ECO:0000269|PubMed:11112443}.; . TISSUE SPECIFICITY: Expressed at high levels in placenta, testis, thymus and at lower levels in heart, kidney, liver and prostate. {ECO:0000269|PubMed:11112443}.; . . 0.11590 0.10624 0.193034296 66.82000472 54.35042 1.47342 PLA2G3 1.13934377005578e-08 0.535369146491176 0.464630842115386 phospholipase A2 group III FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Shows an 11-fold preference for phosphatidylglycerol over phosphatidylcholine (PC). Preferential cleavage: 1-palmitoyl-2-linoleoyl- phosphatidylethanolamine (PE) > 1-palmitoyl-2-linoleoyl-PC > 1- palmitoyl-2-arachidonoyl-PC > 1-palmitoyl-2-arachidonoyl-PE. Plays a role in ciliogenesis. {ECO:0000269|PubMed:12522102, ECO:0000269|PubMed:20393563}.; . TISSUE SPECIFICITY: Expressed in kidney, heart, liver, and skeletal muscle. Also present in placenta and peripheral blood leukocytes. Not detected in brain, colon, thymus, spleen and small intestine. In lung, expressed in bronchial epithelial cells and alveolar macrophages, but scarcely detected in alveolar epithelium, arterial walls and interstitial fibroblasts (at protein level). In joints of osteoarthritis and rheumatoid arthritis, expressed in endothelial cells (at protein level). In normal heart, detected in some vessels. In myocardial tissues with acute infarction, expressed in vascular endothelial cells adjacent to cardiomyocytes and those in lesions with granulation. Expression in cardiomyocytes is scarce (at protein level). In uterus, breast and colon cancers, detected in tumor cells and neighboring microvascular endothelium, but not in normal glandular tissues (at protein level). {ECO:0000269|PubMed:15863501}.; unclassifiable (Anatomical System);adrenal cortex;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.35026 0.09817 1.291545885 93.87827318 5106.25546 14.67199 PLA2G4A 0.00110001839424313 0.99846473128963 0.000435250316127279 phospholipase A2 group IVA FUNCTION: Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response.; DISEASE: Note=PLA2G4A mutations resulting in phospholipase A2 deficiency have been found in a patient affected by recurrent episodes of multiple complicated ulcers of the small intestine, not due to cyclooxygenase inhibitors use. Disease features also include platelet dysfunction, and globally decreased eicosanoid synthesis (PubMed:18451993). {ECO:0000269|PubMed:18451993}.; TISSUE SPECIFICITY: Expressed in various tissues such as macrophages, platelets, neutrophils, fibroblasts and lung endothelium.; . . 0.13461 0.44794 -0.247889024 35.98726115 80.59595 1.89715 PLA2G4B 9.15662350167561e-25 0.000441734513603934 0.999558265486396 phospholipase A2 group IVB FUNCTION: Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position with a preference for arachidonoyl phospholipids. Has a much weaker activity than PLA2G4A. Isoform 3 has calcium-dependent activity against palmitoyl-arachidonyl-phosphatidylethanolamine and low level lysophospholipase activity but no activity against phosphatidylcholine. Isoform 5 does have activity against phosphatidylcholine. {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:16617059}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in brain, heart, liver, cerebellum and pancreas. Isoform 3 is widely expressed. {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:16617059}.; . . 0.17884 0.10269 0.058725693 58.00896438 936.51427 5.93398 PLA2G4C 4.41932214366148e-08 0.946243910574495 0.0537560452322842 phospholipase A2 group IVC FUNCTION: Has a preference for arachidonic acid at the sn-2 position of phosphatidylcholine as compared with palmitic acid. {ECO:0000269|PubMed:10085124}.; . TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle. {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:9705332}.; ovary;salivary gland;colon;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;testis;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; occipital lobe;hypothalamus;caudate nucleus;parietal lobe;skeletal muscle;cerebellum; 0.06112 0.06901 2.447407799 98.56687898 2845.06491 10.08702 PLA2G4C-AS1 . . . PLA2G4C antisense RNA 1 . . . . . . . . . . . PLA2G4D 6.29227608353161e-10 0.847458209777238 0.152541789593535 phospholipase A2 group IVD FUNCTION: Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position. Not arachidonic acid-specific but has linoleic acid-specific activity. May play a role in inflammation in psoriatic lesions. {ECO:0000269|PubMed:14709560}.; . TISSUE SPECIFICITY: Expressed in stratified squamous epithelia, such as those in skin and cervix, but not in other tissues. Strongly expressed in the upper spinous layer of the psoriatic epidermis, expressed weakly and discontinuously in atopic dermatitis and mycosis fungoides, and not detected in the epidermis of normal skin. {ECO:0000269|PubMed:14709560}.; unclassifiable (Anatomical System);medulla oblongata; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.11377 0.09817 1.611214866 95.93064402 5840.10645 15.84607 PLA2G4E 2.28331485083454e-06 0.994852999118172 0.00514471756697729 phospholipase A2 group IVE FUNCTION: Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position. {ECO:0000250}.; . . . . 0.09527 . 0.316000233 72.80018872 1519.70123 7.24651 PLA2G4E-AS1 . . . PLA2G4E antisense RNA 1 . . . . . . . . . . . PLA2G4F 1.39975398074621e-09 0.985845066644852 0.0141549319553937 phospholipase A2 group IVF FUNCTION: Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position. Has higher enzyme activity for phosphatidylethanolamine than phosphatidylcholine (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;pineal body;colon;skeletal muscle;bile duct;prostate;lung;thyroid;hypopharynx;pituitary gland;testis;head and neck;kidney;brain; . 0.06296 0.09823 1.32640619 94.10238264 1110.4377 6.37148 PLA2G5 0.000190274829493542 0.474147037399319 0.525662687771188 phospholipase A2 group V FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. This isozyme hydrolyzes more efficiently L-alpha-1-palmitoyl-2-oleoyl phosphatidylcholine than L-alpha-1-palmitoyl-2-arachidonyl phosphatidylcholine, L- alpha-1-palmitoyl-2-arachidonyl phosphatidylethanolamine, or L- alpha-1-stearoyl-2-arachidonyl phosphatidylinositol. May be involved in the production of lung surfactant, the remodeling or regulation of cardiac muscle.; DISEASE: Fleck retina, familial benign (FRFB) [MIM:228980]: An autosomal recessive condition associated with a distinctive retinal appearance and no apparent visual or electrophysiologic deficits. Affected individuals are asymptomatic, but fundus examination reveals a striking pattern of diffuse, yellow-white, fleck-like lesions extending to the far periphery of the retina but sparing the foveal region. {ECO:0000269|PubMed:22137173}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Heart, placenta and less abundantly, in lung. Detected in the outer and inner plexiform layers of the retina (at protein level). {ECO:0000269|PubMed:22137173}.; . . 0.11251 . -0.317668748 31.45789101 25.27033 0.82614 PLA2G6 2.66040412130891e-08 0.901102431785441 0.0988975416105176 phospholipase A2 group VI FUNCTION: Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F- actin polymerization at the pseudopods.; DISEASE: Neurodegeneration with brain iron accumulation 2A (NBIA2A) [MIM:256600]: A neurodegenerative disease characterized by pathologic axonal swelling and spheroid bodies in the central nervous system. Onset is within the first 2 years of life with death by age 10 years. {ECO:0000269|PubMed:16783378, ECO:0000269|PubMed:17033970, ECO:0000269|PubMed:23749988}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Parkinson disease 14 (PARK14) [MIM:612953]: An adult- onset progressive neurodegenerative disorder characterized by parkinsonism, dystonia, severe cognitive decline, cerebral and cerebellar atrophy and absent iron in the basal ganglia on magnetic resonance imaging. {ECO:0000269|PubMed:18570303}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Four different transcripts were found to be expressed in a distinct tissue distribution.; unclassifiable (Anatomical System);amygdala;lymph node;urinary;colon;skin;retina;uterus;prostate;optic nerve;lung;frontal lobe;endometrium;synovium;bone;placenta;visual apparatus;iris;testis;kidney;brain;mammary gland;bladder;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.16881 0.17642 -1.591018721 3.084453881 148.63297 2.65978 PLA2G7 8.02276784444073e-11 0.0737590758595616 0.926240924060211 phospholipase A2 group VII FUNCTION: Modulates the action of platelet-activating factor (PAF) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. Has a specificity for substrates with a short residue at the sn-2 position. It is inactive against long-chain phospholipids.; DISEASE: Asthma (ASTHMA) [MIM:600807]: The most common chronic disease affecting children and young adults. It is a complex genetic disorder with a heterogeneous phenotype, largely attributed to the interactions among many genes and between these genes and the environment. It is characterized by recurrent attacks of paroxysmal dyspnea, with wheezing due to spasmodic contraction of the bronchi. {ECO:0000269|PubMed:10733466}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Atopic hypersensitivity (ATOPY) [MIM:147050]: A condition characterized by predisposition to develop hypersensitivity reactions. Atopic individuals can develop eczema, allergic rhinitis and allergic asthma. {ECO:0000269|PubMed:10733466}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma.; unclassifiable (Anatomical System);ovary;tongue;islets of Langerhans;colon;parathyroid;prostate;lung;bone;placenta;thyroid;spleen;kidney;brain;mammary gland;stomach; . 0.06089 0.30401 0.576916344 82.25406936 347.33592 3.95129 PLA2G10 0.0217477326167779 0.527424852301324 0.450827415081898 phospholipase A2 group X FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. Prefers phosphatidylethanolamine and phosphatidylcholine liposomes to those of phosphatidylserine.; . TISSUE SPECIFICITY: Found in spleen, thymus, peripheral blood leukocytes, pancreas, lung, and colon.; lung;colon;germinal center; superior cervical ganglion;testis - seminiferous tubule;appendix;atrioventricular node;trigeminal ganglion;tonsil;skin;skeletal muscle; 0.13753 0.12253 . . 1.2578 0.04442 PLA2G12A 0.00188156069840513 0.725443857448546 0.272674581853049 phospholipase A2 group XIIA FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Does not exhibit detectable activity toward sn-2-arachidonoyl- or linoleoyl- phosphatidylcholine or -phosphatidylethanolamine. {ECO:0000269|PubMed:12522102}.; . TISSUE SPECIFICITY: Abundantly expressed in heart, skeletal muscle, kidney, liver and pancreas.; unclassifiable (Anatomical System);lymph node;ovary;heart;islets of Langerhans;hypothalamus;colon;parathyroid;skin;skeletal muscle;retina;bone marrow;uterus;prostate;lung;endometrium;nasopharynx;bone;placenta;liver;testis;spleen;kidney;brain;stomach; superior cervical ganglion;pons;trigeminal ganglion; 0.10613 0.11203 0.215080721 67.91696155 71.68404 1.76213 PLA2G12AP1 . . . phospholipase A2 group XIIA pseudogene 1 . . . . . . . . . . . PLA2G12AP2 . . . phospholipase A2 group XIIA pseudogene 2 . . . . . . . . . . . PLA2G12B 0.0598690316011939 0.86834010022917 0.0717908681696356 phospholipase A2 group XIIB FUNCTION: Not known; does not seem to have catalytic activity.; . TISSUE SPECIFICITY: Strong expression in liver, small intestine and kidney. {ECO:0000269|PubMed:14516201}.; . . 0.48254 0.12842 -0.185391282 39.67916962 12.46963 0.45343 PLA2G15 0.658429999883026 0.34041063721628 0.0011593629006936 phospholipase A2 group XV FUNCTION: Has transacylase and calcium-independent phospholipase A2 activity (PubMed:20410020, PubMed:23958596). Catalyzes the formation of 1-O-acyl-N-acetylsphingosine and the concomitant release of a lyso-phospholipid (PubMed:11790796, PubMed:25727495). Has high activity with 1-palmitoyl-2-oleoyl-sn-glycero-3- phosphocholine (POPC) and 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), catalyzing the transfer of oleic acid to N-acetyl- sphingosine. Required for normal phospholipid degradation in alveolar and peritoneal macrophages and in spleen (By similarity). May have weak lysophospholipase activity (PubMed:10092508). {ECO:0000250|UniProtKB:Q8VEB4, ECO:0000269|PubMed:10092508, ECO:0000269|PubMed:11790796, ECO:0000269|PubMed:20410020, ECO:0000269|PubMed:23958596, ECO:0000269|PubMed:25727495}.; . TISSUE SPECIFICITY: Detected in blood plasma (at protein level) (PubMed:10092508, PubMed:20410020). Ubiquitous. Highly expressed in heart, placenta, skeletal muscle, kidney and pancreas. Detected at lower levels in spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes (PubMed:10092508). {ECO:0000269|PubMed:10092508, ECO:0000269|PubMed:20410020}.; lymphoreticular;ovary;salivary gland;colon;parathyroid;choroid;skin;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;lens;skeletal muscle;pancreas;lung;placenta;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;stomach;thymus; ciliary ganglion;atrioventricular node;skeletal muscle; 0.09316 0.15898 -0.336073593 30.55555556 25.15947 0.82265 PLA2G16 1.19316734661233e-05 0.210989443079991 0.788998625246543 phospholipase A2 group XVI FUNCTION: Exhibits PLA1/2 activity, catalyzing the calcium- independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. Specifically catalyzes the release of fatty acids from phospholipids in adipose tissue (By similarity). N- and O- acylation activity is hardly detectable. Might decrease protein phosphatase 2A (PP2A) activity. {ECO:0000250, ECO:0000269|PubMed:17374643, ECO:0000269|PubMed:19615464}.; . TISSUE SPECIFICITY: Widely expressed. low expression, if any, in hematopoietic cells and thymus. In testis, confined to round spermatids. Expressed in normal ovarian epithelial cells. Down- regulated in some ovarian carcinomas and testicular germ cell tumors. {ECO:0000269|PubMed:11526504, ECO:0000269|PubMed:11973642, ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:9771974}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;iris;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);heart;hypothalamus;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; medulla oblongata;occipital lobe;thalamus;adipose tissue;olfactory bulb;hypothalamus;spinal cord;testis;parietal lobe; 0.47760 0.08731 -0.029247611 51.40363293 34.28041 1.04933 PLA2R1 5.17711186126812e-15 0.995695799803685 0.00430420019630991 phospholipase A2 receptor 1 FUNCTION: Receptor for secretory phospholipase A2 (sPLA2). Acts as a receptor for phosholipase sPLA2-IB/PLA2G1B but not sPLA2- IIA/PLA2G2A. Also able to bind to snake PA2-like toxins. Although its precise function remains unclear, binding of sPLA2 to its receptor participates in both positive and negative regulation of sPLA2 functions as well as clearance of sPLA2. Binding of sPLA2- IB/PLA2G1B induces various effects depending on the cell type, such as activation of the mitogen-activated protein kinase (MAPK) cascade to induce cell proliferation, the production of lipid mediators, selective release of arachidonic acid in bone marrow- derived mast cells. In neutrophils, binding of sPLA2-IB/PLA2G1B can activate p38 MAPK to stimulate elastase release and cell adhesion. May be involved in responses in proinflammatory cytokine productions during endotoxic shock. Also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. The soluble secretory phospholipase A2 receptor form is circulating and acts as a negative regulator of sPLA2 functions by blocking the biological functions of sPLA2-IB/PLA2G1B. {ECO:0000269|PubMed:15611272, ECO:0000269|PubMed:7721806}.; . TISSUE SPECIFICITY: Present in lung macrophage (at protein level). Highly expressed in kidney. Also expressed in pancreas, amnion, choriodecidua and placenta. Isoform 2 is expressed at much lower level. {ECO:0000269|PubMed:15611272, ECO:0000269|PubMed:7721806, ECO:0000269|PubMed:7925459, ECO:0000269|PubMed:9481783}.; unclassifiable (Anatomical System);heart;colon;parathyroid;skin;skeletal muscle;retina;breast;bile duct;uterus;lung;larynx;thyroid;placenta;iris;liver;testis;head and neck;spleen;kidney;brain;bladder; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.14885 0.11815 0.861555086 88.63529134 2482.68849 9.29219 PLAA 0.648657498456697 0.351331903542663 1.05980006394608e-05 phospholipase A2 activating protein FUNCTION: Involved in the maintenance of ubiquitin levels. {ECO:0000250}.; . . . . 0.15097 0.12067 -0.933156985 9.54824251 55.2675 1.49217 PLAC1 0.181581258657982 0.645392957950274 0.173025783391743 placenta specific 1 FUNCTION: May play a role in placental development. {ECO:0000269|PubMed:10995572}.; . TISSUE SPECIFICITY: Expressed in placenta. Localizes primarily to differentiated syncytiotrophoblast throughout gestation as well as to a small population of villous cytotrophoblasts. Also detected in maternal blood and rapidly disappears following delivery, but is not detected in other adult or fetal tissues examined. {ECO:0000269|PubMed:10995572, ECO:0000269|PubMed:12412044, ECO:0000269|PubMed:15608456, ECO:0000269|PubMed:15803460}.; unclassifiable (Anatomical System);ovary;placenta;liver;parathyroid;spleen; dorsal root ganglion;superior cervical ganglion;placenta;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11717 0.12344 -0.075159878 47.78839349 6.87232 0.25516 PLAC4 . . . placenta specific 4 . . TISSUE SPECIFICITY: Expressed in placental syncytiotrophoblast and choriocarcinoma cells. {ECO:0000269|PubMed:8406465}.; . . . . . . . . PLAC8 0.372859441505333 0.579723578149066 0.0474169803456007 placenta specific 8 . . TISSUE SPECIFICITY: Expressed at high levels in plasmacytoid dendritic cells. High expression in spleen, lymph nodes, peripheral blood leukocytes, and bone marrow, with lower expression in thymus, appendix, and fetal liver.; ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;trachea;white blood cells;whole blood;tonsil;bone marrow; 0.15661 0.11120 -0.031067188 51.03798066 3.91096 0.14564 PLAC8L1 0.13237785518608 0.780148731684932 0.0874734131289878 PLAC8-like 1 . . . unclassifiable (Anatomical System);medulla oblongata;lung;bone;testis; . 0.12198 . 0.327131069 73.27199811 255.27107 3.43695 PLAC9 0.010238569080354 0.608531059863899 0.381230371055747 placenta specific 9 . . . . . 0.11945 0.10135 0.325313577 73.11276244 234.97725 3.31282 PLAG1 0.829917236319924 0.169332703484022 0.000750060196053341 PLAG1 zinc finger FUNCTION: Transcription factor whose activation results in up- regulation of target genes, such as IGFII, leading to uncontrolled cell proliferation: when overexpressed in cultured cells, higher proliferation rate and transformation are observed. Other target genes such as CRLF1, CRABP2, CRIP2, PIGF are strongly induced in cells with PLAG1 induction. Proto-oncogene whose ectopic expression can trigger the development of pleomorphic adenomas of the salivary gland and lipoblastomas. Overexpression is associated with up-regulation of IGFII, is frequently observed in hepatoblastoma, common primary liver tumor in childhood. Cooperates with CBFB-MYH11, a fusion gene important for myeloid leukemia. {ECO:0000269|PubMed:11888928, ECO:0000269|PubMed:14695992, ECO:0000269|PubMed:14712223}.; DISEASE: Note=A chromosomal aberration involving PLAG1 is found in salivary gland pleiomorphic adenomas, the most common benign epithelial tumors of the salivary gland. Translocation t(3;8)(p21;q12) with constituvely expressed beta-catenin/CTNNB1. Fusion occurs in the 5'-regulatory regions, leading to promoter swapping between the 2 genes and activation of PLAG1 expression in adenomas. The chimeric transcript is formed by fusion of CTNNB1 exon 1 to PLAG1 exon 3. Reciprocal fusion transcript consisting of PLAG1 exon 1 and CTNNB1 exon 2-16 is also revealed in some adenomas (PubMed:9020842, PubMed:10029085). Translocation t(3;8)(p21;q12) with transcription elongation factor SII/TCEA1. The fusion transcript is composed of 5'-non-coding sequences as well as 63 nucleotides of the coding region of TCEA1 fused to the acceptor splice site of PLAG1 exon 3. The fusion transcript encodes a truncated TCEA1-PLAG1 protein of 90 AA as well as an apparently normal PLAG1 protein. Reciprocal fusion transcript PLAG1-TCEA1 is also present in one adenoma (PubMed:10029085, PubMed:16736500). Translocation t(5;8)(p13;q12) with leukemia inhibitory factor receptor LIFR. This fusion occured in the 5'- non-coding sequences of both genes, exchanging regulatory control element while preserving the coding sequences (PubMed:9525740). Translocation t(6;8)(p21.3-22;q13) with Coiled-coil-helix-coiled- coil-helix domain-containing protein 7/CHCHD7. Fusion occurs in the 5' regulatory regions, leading to promoter swapping and up- regulation of PLAG1 expression (PubMed:16736500). Ectopic expression of PLAG1 under the control of promoters of distinct translocation partner genes is a general pathogenetic mechanism for pleiomorphic adenomas with 8q aberrations. These fusion genes are likely to be found in adenomas with normal karyotype as this subgroup of tumors also exhibit PLAG1 activation (PubMed:9020842, PubMed:10029085, PubMed:9525740, PubMed:16736500). {ECO:0000269|PubMed:10029085, ECO:0000269|PubMed:16736500, ECO:0000269|PubMed:9020842, ECO:0000269|PubMed:9525740}.; DISEASE: Note=A chromosomal aberration involving PLAG1 may be a cause of lipoblastomas, which are benign tumors resulting from transformation of adipocytes, usually diagnosed in children. 8q12.1 to 8q24.1 intrachromosomal rearrangement with hyaluronic acid synthase 2/HAS2 results in promoter swapping and activation of PLAG1 expression. The breakpoint of HAS2 gene is in PLAG1 intron 1, whereas its coding sequence starts at exon 2 or exon 3. Translocation t(7;8)(p22;q13) with collagen 1A2/COL1A2. Fusion transcript COL1A2-PLAG1 as well as HAS2-PLAG1 encode a full-length PLAG1 protein. {ECO:0000269|PubMed:10987300, ECO:0000269|PubMed:15642402}.; TISSUE SPECIFICITY: Expressed in fetal tissues such as lung, liver and kidney. Not detected or weak detection in normal adult tissues, but highly expressed in salivary gland with benign or malignant pleiomorphic adenomas with or without 8q12 aberrations, with preferential occurrence in benign tumors. {ECO:0000269|PubMed:10029085, ECO:0000269|PubMed:14695992, ECO:0000269|PubMed:9020842, ECO:0000269|PubMed:9722527}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;parathyroid;skin;bone marrow;uterus;pancreas;whole body;lung;endometrium;nasopharynx;bone;thyroid;placenta;visual apparatus;pituitary gland;liver;testis;spleen;germinal center;kidney;brain; ciliary ganglion; 0.85037 0.19761 -0.227663163 37.11370606 581.1771 4.88619 PLAGL1 0.881694431277305 0.116926711939216 0.0013788567834793 PLAG1 like zinc finger 1 FUNCTION: Shows weak transcriptional activatory activity. Transcriptional regulator of the type 1 receptor for pituitary adenylate cyclase-activating polypeptide. {ECO:0000269|PubMed:18299245}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;endometrium;cochlea;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;amnion;spleen;head and neck;kidney;stomach;aorta; superior cervical ganglion;placenta;atrioventricular node;trigeminal ganglion; 0.15161 0.19461 -0.157884861 42.05590941 82.23267 1.92439 PLAGL2 0.86979563793487 0.128437036835281 0.0017673252298489 PLAG1 like zinc finger 2 FUNCTION: Shows weak transcriptional activatory activity.; . . medulla oblongata;umbilical cord;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.87257 0.12846 -0.137658575 43.57159707 26.9787 0.87150 PLAT 0.000197179503033642 0.994713517594786 0.00508930290218083 plasminogen activator, tissue type FUNCTION: Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. Plays a direct role in facilitating neuronal migration.; DISEASE: Note=Increased activity of TPA results in increased fibrinolysis of fibrin blood clots that is associated with excessive bleeding. Defective release of TPA results in hypofibrinolysis that can lead to thrombosis or embolism. {ECO:0000269|PubMed:1762144}.; TISSUE SPECIFICITY: Synthesized in numerous tissues (including tumors) and secreted into most extracellular body fluids, such as plasma, uterine fluid, saliva, gingival crevicular fluid, tears, seminal fluid, and milk.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;iris;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion; 0.21477 0.84232 -0.440847477 24.59896202 155.28813 2.72250 PLAU 0.00055026957460409 0.972496454206855 0.0269532762185409 plasminogen activator, urokinase FUNCTION: Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.; DISEASE: Quebec platelet disorder (QPD) [MIM:601709]: An autosomal dominant bleeding disorder due to a gain-of-function defect in fibrinolysis. Although affected individuals do not exhibit systemic fibrinolysis, they show delayed onset bleeding after challenge, such as surgery. The hallmark of the disorder is markedly increased PLAU levels within platelets, which causes intraplatelet plasmin generation and secondary degradation of alpha-granule proteins. {ECO:0000269|PubMed:20007542}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the prostate gland and prostate cancers. {ECO:0000269|PubMed:15988036}.; . . 0.08249 0.90261 0.308721233 72.59966973 135.07501 2.52903 PLAUR 0.3065849263056 0.68949230790105 0.00392276579335003 plasminogen activator, urokinase receptor FUNCTION: Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. It is subject to negative-feedback regulation by U-PA which cleaves it into an inactive form.; . TISSUE SPECIFICITY: Expressed in neurons of the rolandic area of the brain (at protein level). Expressed in the brain.; lymphoreticular;ovary;colon;vein;skin;bone marrow;prostate;endometrium;bone;iris;testis;amniotic fluid;bladder;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;alveolus;cervix;kidney;mammary gland;stomach; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.19887 0.55831 1.396334339 94.70393961 2238.41906 8.73023 PLB1 1.9931529274349e-56 1.21860216302548e-09 0.999999998781398 phospholipase B1 FUNCTION: Membrane-associated phospholipase. Exhibits a calcium- independent broad substrate specificity including phospholipase A2/lysophospholipase activity. Preferential hydrolysis at the sn-2 position of diacylphospholipids and diacyglycerol, whereas it shows no positional specificity toward triacylglycerol. Exhibits also esterase activity toward p-nitrophenyl. May act on the brush border membrane to facilitate the absorption of digested lipids (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the epidermis (at protein level). {ECO:0000269|PubMed:12150957}.; unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;prostate;optic nerve;lung;bone;placenta;macula lutea;testis;mammary gland;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12087 0.11509 1.208866406 93.05850436 3555.80975 11.53022 PLBD1 9.67351257348209e-13 0.0396161518948598 0.960383848104173 phospholipase B domain containing 1 FUNCTION: In view of the small size of the putative binding pocket, it has been proposed that it may act as an amidase or a peptidase (By similarity). Exhibits a weak phospholipase activity, acting on various phospholipids, including phosphatidylcholine, phosphatidylinositol, phosphatidylethanolamine and lysophospholipids. {ECO:0000250, ECO:0000269|PubMed:19019078}.; . TISSUE SPECIFICITY: Expressed in neutrophils and monocytes. {ECO:0000269|PubMed:19019078}.; myocardium;sympathetic chain;colon;choroid;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;larynx;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;urinary;blood;bile duct;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;head and neck;kidney;mammary gland;stomach; whole blood;bone marrow; . . 0.531004228 80.87992451 1398.05611 6.99148 PLBD1-AS1 . . . PLBD1 antisense RNA 1 . . . . . . . . . . . PLBD2 7.18473138561366e-08 0.693484922724931 0.306515005427756 phospholipase B domain containing 2 FUNCTION: Putative phospholipase. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in heart, brain and liver. {ECO:0000269|PubMed:17105447}.; unclassifiable (Anatomical System);medulla oblongata;cartilage;heart;islets of Langerhans;salivary gland;colon;skin;retina;uterus;pancreas;lung;oesophagus;bone;placenta;testis;kidney;brain;mammary gland;bladder;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . -0.268115223 34.70747818 475.55206 4.50466 PLCB1 0.979044816094075 0.0209551838956828 1.02420993612307e-11 phospholipase C beta 1 FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.; DISEASE: Epileptic encephalopathy, early infantile, 12 (EIEE12) [MIM:613722]: A form of epilepsy characterized by frequent tonic seizures or spasms beginning in infancy with a specific EEG finding of suppression-burst patterns, characterized by high- voltage bursts alternating with almost flat suppression phases. Patients may progress to West syndrome, which is characterized by tonic spasms with clustering, arrest of psychomotor development, and hypsarrhythmia on EEG. {ECO:0000269|PubMed:20833646}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;cartilage;islets of Langerhans;sympathetic chain;colon;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;lung;frontal lobe;cochlea;endometrium;placenta;macula lutea;visual apparatus;liver;spleen;kidney;brain;cerebellum; amygdala;whole brain;dorsal root ganglion;occipital lobe;superior cervical ganglion;medulla oblongata;temporal lobe;caudate nucleus;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.46510 0.19048 -0.835882558 11.47676339 220.50497 3.21024 PLCB1-IT1 . . . PLCB1 intronic transcript 1 . . . . . . . . . . . PLCB2 3.01690271048763e-12 0.993330677440369 0.00666932255661422 phospholipase C beta 2 FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.; . . unclassifiable (Anatomical System);lymphoreticular;cartilage;ovary;urinary;colon;blood;skin;skeletal muscle;bone marrow;optic nerve;lung;frontal lobe;bone;placenta;visual apparatus;liver;testis;spleen;germinal center;kidney;brain;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.26816 0.18478 -0.701780438 14.81481481 1421.20643 7.04287 PLCB2-AS1 . . . PLCB2 antisense RNA 1 . . . . . . . . . . . PLCB3 0.968376699687946 0.03162330017195 1.40104017650364e-10 phospholipase C beta 3 FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.; . . unclassifiable (Anatomical System);lymph node;cartilage;colon;skin;uterus;pancreas;prostate;lung;frontal lobe;endometrium;bone;thyroid;placenta;visual apparatus;testis;cervix;kidney;brain;stomach; trigeminal ganglion; 0.57222 0.17315 -0.637452658 16.73743808 1078.42089 6.29701 PLCB4 0.272263498048569 0.727736501340987 6.10444485614922e-10 phospholipase C beta 4 FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This form has a role in retina signal transduction.; . TISSUE SPECIFICITY: Preferentially expressed in the retina.; ovary;sympathetic chain;colon;parathyroid;skin;retina;uterus;prostate;whole body;cochlea;endometrium;thyroid;bone;testis;amniotic fluid;dura mater;spinal ganglion;ciliary body;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;blood;skeletal muscle;bile duct;pia mater;lung;trabecular meshwork;placenta;liver;spleen;kidney;mammary gland;stomach; thalamus;superior cervical ganglion;cerebellum peduncles; 0.12302 0.14602 -0.907472583 10.07313046 4614.82682 13.64468 PLCD1 2.55415564522998e-09 0.887228912627395 0.11277108481845 phospholipase C delta 1 FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Essential for trophoblast and placental development.; DISEASE: Nail disorder, non-syndromic congenital, 3 (NDNC3) [MIM:151600]: A nail disorder characterized by a white appearance of the nail plate (true leukonychia), the nail bed (pseudoleukonychia), or neither (apparent leukonychia). Leukonychia may involve all of the nail (leukonychia totalis) or only part of the nail (leukonychia partialis), or can appear as one or more transverse bands (leukonychia striata) or white spots (leukonychia punctata). {ECO:0000269|PubMed:21665001}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;cerebral cortex;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;urinary;lens;skeletal muscle;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;spleen;mammary gland; testis;trigeminal ganglion; 0.98535 0.15071 -0.854306498 10.96367068 1032.09996 6.17198 PLCD3 0.000143297256551118 0.963091934853409 0.0367647678900395 phospholipase C delta 3 FUNCTION: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow.; . TISSUE SPECIFICITY: Present in corneal epithelial cells (at protein level). {ECO:0000269|PubMed:15505048}.; unclassifiable (Anatomical System);ovary;muscle;colon;choroid;skin;skeletal muscle;pancreas;prostate;optic nerve;whole body;lung;frontal lobe;endometrium;bone;thyroid;visual apparatus;cervix;brain;bladder;aorta;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;skin; 0.14556 0.11570 . . 81.7627 1.91678 PLCD4 8.11639260444202e-09 0.892497689091611 0.107502302791996 phospholipase C delta 4 FUNCTION: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Required for acrosome reaction in sperm during fertilization, probably by acting as an important enzyme for intracellular Ca(2+) mobilization in the zona pellucida- induced acrosome reaction. May play a role in cell growth. Modulates the liver regeneration in cooperation with nuclear PKC. Overexpression up-regulates the Erk signaling pathway and proliferation. {ECO:0000269|PubMed:15140260}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle and kidney tissues, and at moderate level in intestinal tissue. Expressed in corneal epithelial cells. {ECO:0000269|PubMed:15140260, ECO:0000269|PubMed:15505048}.; unclassifiable (Anatomical System);tongue;spinal cord;colon;skeletal muscle;retina;breast;lung;placenta;thyroid;liver;head and neck;spleen;brain;stomach; . 0.36073 0.11602 -0.929520514 9.683887709 151.66317 2.69391 PLCE1 0.204555596267865 0.795444403732056 7.8451702113972e-14 phospholipase C epsilon 1 FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. PLCE1 is a bifunctional enzyme which also regulates small GTPases of the Ras superfamily through its Ras guanine- exchange factor (RasGEF) activity. As an effector of heterotrimeric and small G-protein, it may play a role in cell survival, cell growth, actin organization and T-cell activation. {ECO:0000269|PubMed:11022047, ECO:0000269|PubMed:11395506, ECO:0000269|PubMed:11715024, ECO:0000269|PubMed:11877431, ECO:0000269|PubMed:12721365, ECO:0000269|PubMed:16537651, ECO:0000269|PubMed:17086182}.; DISEASE: Nephrotic syndrome 3 (NPHS3) [MIM:610725]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. Most patients with NPHS3 show diffuse mesangial sclerosis on renal biopsy, which is a pathologic entity characterized by mesangial matrix expansion with no mesangial hypercellularity, hypertrophy of the podocytes, vacuolized podocytes, thickened basement membranes, and diminished patency of the capillary lumen. {ECO:0000269|PubMed:17086182}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Isoform 1 is broadly expressed and only absent in peripheral blood leukocytes. Isoform 2 is specifically expressed in placenta, lung and spleen. {ECO:0000269|PubMed:11022047, ECO:0000269|PubMed:11022048, ECO:0000269|PubMed:15558028}.; colon;parathyroid;skin;retina;uterus;prostate;cochlea;larynx;thyroid;bone;iris;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;lens;skeletal muscle;lung;adrenal gland;placenta;visual apparatus;liver;head and neck;kidney;stomach; pons;atrioventricular node;trigeminal ganglion; 0.08183 0.11603 0.356282176 74.58716678 11765.49279 23.41934 PLCE1-AS1 . . . PLCE1 antisense RNA 1 . . . . . . . . . . . PLCE1-AS2 . . . PLCE1 antisense RNA 2 . . . . . . . . . . . PLCE1P1 . . . phospholipase C epsilon 1 pseudogene 1 . . . . . . . . . . . PLCG1 0.76335235197211 0.236647648018886 9.00330178801274e-12 phospholipase C gamma 1 FUNCTION: Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand- mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration. {ECO:0000269|PubMed:17229814}.; . . ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;iris;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;blood;lens;skeletal muscle;lung;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; . 0.70856 0.63289 -1.967739992 1.816466148 548.82479 4.76411 PLCG1-AS1 . . . PLCG1 antisense RNA 1 . . . . . . . . . . . PLCG2 0.999993046683293 6.9533167074959e-06 4.02181887312522e-18 phospholipase C gamma 2 FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling.; DISEASE: Familial cold autoinflammatory syndrome 3 (FCAS3) [MIM:614468]: An autosomal dominant immune disorder characterized by the development of cutaneous urticaria, erythema, and pruritis in response to cold exposure. Affected individuals have variable additional immunologic defects, including antibody deficiency, decreased numbers of B-cells, defective B-cells, increased susceptibility to infection, and increased risk of autoimmune disorders. {ECO:0000269|PubMed:22236196}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Autoinflammation, antibody deficiency, and immune dysregulation PLCG2-associated (APLAID) [MIM:614878]: An autosomal dominant systemic disorder characterized by recurrent blistering skin lesions with a dense inflammatory infiltrate and variable involvement of other tissues, including joints, the eye, and the gastrointestinal tract. Affected individuals have a mild humoral immune deficiency associated with recurrent sinopulmonary infections, but no evidence of circulating autoantibodies. {ECO:0000269|PubMed:23000145}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;smooth muscle;choroid;bone marrow;uterus;whole body;larynx;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.74559 0.34638 -0.600905864 17.91696155 692.66245 5.24986 PLCH1 0.425540924509534 0.574459074597413 8.93052079563095e-10 phospholipase C eta 1 FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by calcium-activated phosphatidylinositol-specific phospholipase C enzymes. {ECO:0000269|PubMed:15702972}.; . TISSUE SPECIFICITY: Expressed in brain and to a lower extent in lung. In brain, it is found in cerebrum, cerebellum and spinal cord. {ECO:0000269|PubMed:15702972}.; unclassifiable (Anatomical System);medulla oblongata;colon;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;lung;frontal lobe;endometrium;macula lutea;visual apparatus;testis;brain; superior cervical ganglion;atrioventricular node;parietal lobe;skeletal muscle; 0.10745 0.09748 -1.074802575 7.336635999 322.80077 3.81661 PLCH1-AS1 . . . PLCH1 antisense RNA 1 . . . . . . . . . . . PLCH1-AS2 . . . PLCH1 antisense RNA 2 . . . . . . . . . . . PLCH2 1.70518647543863e-08 0.841467315531918 0.158532667416217 phospholipase C eta 2 FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This phospholipase activity is very sensitive to calcium. May be important for formation and maintenance of the neuronal network in the postnatal brain (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in retina and kidney. {ECO:0000269|PubMed:16107206}.; unclassifiable (Anatomical System);amygdala;lymph node;islets of Langerhans;colon;substantia nigra;fovea centralis;choroid;lens;retina;pancreas;whole body;optic nerve;lung;macula lutea;visual apparatus;germinal center;kidney;mammary gland;pineal gland;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;temporal lobe;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle;cerebellum; 0.16736 0.10113 . . 562.69013 4.81563 PLCL1 0.0110523707623017 0.988569847993791 0.00037778124390733 phospholipase C like 1 FUNCTION: Involved in an inositol phospholipid-based intracellular signaling cascade. Shows no PLC activity to phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol. Component in the phospho-dependent endocytosis process of GABA A receptor (By similarity). Regulates the turnover of receptors and thus contributes to the maintenance of GABA-mediated synaptic inhibition. Its aberrant expression could contribute to the genesis and progression of lung carcinoma. Acts as a inhibitor of PPP1C. {ECO:0000250, ECO:0000269|PubMed:17254016}.; . TISSUE SPECIFICITY: Expressed in a variety of fetal and adult organs including brain, lung and kidney. Its expression was greatly reduced in small and non-small cell lung carcinoma. Isoform 1 is predominantly expressed in brain. {ECO:0000269|PubMed:16952428, ECO:0000269|PubMed:7633416}.; . . 0.41180 0.11540 -0.24061166 36.28214201 4644.52791 13.71723 PLCL2 0.999118779774419 0.00088121245064469 7.77493660005578e-09 phospholipase C like 2 FUNCTION: May play an role in the regulation of Ins(1,4,5)P3 around the endoplasmic reticulum. {ECO:0000250}.; . . ovary;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;testis;germinal center;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;adrenal cortex;blood;lung;pia mater;trabecular meshwork;visual apparatus;liver;spleen;head and neck;kidney; amygdala;dorsal root ganglion;medulla oblongata;superior cervical ganglion;occipital lobe;atrioventricular node;skeletal muscle;skin;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;cerebellum; 0.57453 0.11025 -0.622676946 17.30950696 76.96403 1.84148 PLCL2-AS1 . . . PLCL2 antisense RNA 1 . . . . . . . . . . . PLCXD1 1.56642202426473e-12 0.00745601075626396 0.99254398924217 phosphatidylinositol specific phospholipase C X domain containing 1 . . . . . 0.10945 . -0.016511957 52.31776362 153.78841 2.71129 PLCXD2 5.16800987455644e-05 0.436127422575893 0.563820897325362 phosphatidylinositol specific phospholipase C X domain containing 2 . . . . . . 0.12035 -0.337894035 30.37272942 178.1315 2.90110 PLCXD2-AS1 . . . PLCXD2 antisense RNA 1 . . . . . . . . . . . PLCXD3 0.0484887392356897 0.857317654453857 0.0941936063104531 phosphatidylinositol specific phospholipase C X domain containing 3 . . . unclassifiable (Anatomical System);amygdala;heart;cerebellum cortex;islets of Langerhans;substantia nigra;blood;skeletal muscle;whole body;lung;adrenal gland;iris;liver;testis;kidney;brain; . 0.34360 0.11262 -0.317668748 31.45789101 29.21209 0.93383 PLCZ1 6.45114192499903e-10 0.404982029394134 0.595017969960751 phospholipase C zeta 1 FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)- dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg- activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function. {ECO:0000250|UniProtKB:Q8K4D7, ECO:0000269|PubMed:12416999, ECO:0000269|PubMed:14697805, ECO:0000269|PubMed:15579586, ECO:0000305}.; . TISSUE SPECIFICITY: Expressed specifically in testis. Weakly expressed in pancreatic-duct cells. Up-regulated in pancreatic- duct cells from patients with cystic fibrosis. {ECO:0000269|PubMed:12416999, ECO:0000269|PubMed:14697805}.; unclassifiable (Anatomical System);lung;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node; 0.09239 0.09255 -0.466531444 23.51380042 117.49888 2.35640 PLD1 7.20704885136773e-16 0.792829778294758 0.207170221705241 phospholipase D1 FUNCTION: Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed abundantly in the pancreas and heart and at high levels in brain, placenta, spleen, uterus and small intestine. {ECO:0000269|PubMed:9582313}.; ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;whole body;frontal lobe;oesophagus;larynx;thyroid;bone;testis;brain;gall bladder;unclassifiable (Anatomical System);cartilage;small intestine;heart;hypothalamus;spinal cord;adrenal cortex;blood;lens;breast;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;kidney; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.78722 0.22586 -0.011054102 52.36494456 496.81397 4.58114 PLD2 8.12711920535035e-14 0.839394898118896 0.160605101881023 phospholipase D2 FUNCTION: May have a role in signal-induced cytoskeletal regulation and/or endocytosis. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;colon;skin;uterus;prostate;optic nerve;thyroid;bone;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;tongue;islets of Langerhans;urinary;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; trigeminal ganglion; 0.33611 0.25303 0.411473843 76.55697098 4758.80464 13.96455 PLD3 0.015972164288732 0.978720649655941 0.00530718605532692 phospholipase D family member 3 FUNCTION: Probably involved in APP processing. {ECO:0000269|PubMed:24336208}.; DISEASE: Alzheimer disease 19 (AD19) [MIM:615711]: A late-onset form of Alzheimer disease, a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C- terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. {ECO:0000269|PubMed:24336208, ECO:0000269|PubMed:25832409, ECO:0000269|PubMed:25832410}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry. Disease association is, however, under debate. Some studies support PLD3 involvement in Alzheimer disease (PubMed:24336208, PubMed:25832410 and PubMed:25832409), while others do not (Ref.8, Ref.11 and Ref.12). {ECO:0000269|PubMed:24336208, ECO:0000269|PubMed:25832408, ECO:0000269|PubMed:25832409, ECO:0000269|PubMed:25832410, ECO:0000269|PubMed:25832411, ECO:0000269|PubMed:25832413}.; TISSUE SPECIFICITY: Widely expressed. In the brain, high levels of expression are detected in the frontal, temporal and occipital cortices and hippocampus. Expressed at low level in corpus callosum. {ECO:0000269|PubMed:15794758, ECO:0000269|PubMed:24336208}.; myocardium;ovary;salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;synovium;larynx;bone;thyroid;iris;pituitary gland;testis;amniotic fluid;brain;pineal gland;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; amygdala;whole brain;temporal lobe;pituitary; 0.29450 0.12854 -0.512444034 21.55579146 50.17338 1.39128 PLD4 1.23030186248079e-13 0.00618289209607334 0.993817107903804 phospholipase D family member 4 . . . . . 0.09210 0.09997 0.108486928 61.90728946 1007.43945 6.11442 PLD5 0.124197736898067 0.874752709165018 0.00104955393691477 phospholipase D family member 5 . . . amygdala;pancreas;optic nerve;macula lutea;visual apparatus;fovea centralis;choroid;lens;retina; superior cervical ganglion;olfactory bulb;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.21114 0.08983 -0.181750739 40.15687662 20.81668 0.70563 PLD6 0.0754626037619383 0.747745706523787 0.176791689714275 phospholipase D family member 6 FUNCTION: Regulates mitochondrial shape through facilitating mitochondrial fusion (PubMed:17028579, PubMed:). During spermatogenesis, plays a critical role in PIWI-interacting RNA (piRNA) biogenesis (By similarity). piRNAs provide essential protection against the activity of mobile genetic elements. piRNA- mediated transposon silencing is thus critical for maintaining genome stability, in particular in germline cells when transposons are mobilized as a consequence of wide-spread genomic demethylation. Has been shown to be a backbone-non-specific, single strand-specific nuclease, cleaving either RNA or DNA substrates with similar affinity (By similarity). Produces 5' phosphate and 3' hydroxyl termini, suggesting it could directly participate in the processing of primary piRNA transcripts (By similarity). Has been proposed to act as a cardiolipin hydrolase to generate phosphatidic acid at mitochondrial surface. Although it cannot be excluded that it can act as a phospholipase in some circumstances, it should be noted that cardiolipin hydrolase activity is either undetectable in vitro, or very low (PubMed:21397848). In addition, cardiolipin is almost exclusively found on the inner mitochondrial membrane, while PLD6 localizes to the outer mitochondrial membrane, facing the cytosol (PubMed:21397848). {ECO:0000250|UniProtKB:Q5SWZ9, ECO:0000269|PubMed:17028579, ECO:0000269|PubMed:21397848, ECO:0000269|PubMed:26711011}.; . TISSUE SPECIFICITY: Widely expressed. Expression is not limited to testis and ovary. {ECO:0000269|PubMed:17028579, ECO:0000269|PubMed:21397847}.; unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;colon;skin;skeletal muscle;uterus;prostate;lung;frontal lobe;visual apparatus;hippocampus;iris;duodenum;pituitary gland;testis;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; . 0.09965 . . 9.7742 0.35738 PLEC 0.024936270552365 0.975063729447634 8.96935734504024e-16 plectin FUNCTION: Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity. {ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:21109228}.; DISEASE: Epidermolysis bullosa simplex with pyloric atresia (EBS- PA) [MIM:612138]: Autosomal recessive genodermatosis characterized by severe skin blistering at birth and congenital pyloric atresia. Death usually occurs in infancy. This disorder is allelic to MD- EBS. {ECO:0000269|PubMed:14675180, ECO:0000269|PubMed:20665883}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa simplex, with muscular dystrophy (MD-EBS) [MIM:226670]: A form of epidermolysis bullosa characterized by the association of blister formation at the level of the hemidesmosome with late-onset muscular dystrophy. {ECO:0000269|PubMed:11159198, ECO:0000269|PubMed:21263134, ECO:0000269|PubMed:8894687}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa simplex, Ogna type (O-EBS) [MIM:131950]: A form of intraepidermal epidermolysis bullosa characterized by generalized skin bruising, skin fragility with non-scarring blistering and small hemorrhagic blisters on hands. At the ultrastructural level, it is differentiated from classical cases of K-EBS, WC-EBS and DM-EBS, by the occurrence of blisters originating in basal cells above hemidesmosomes, and abnormal hemidesmosome intracellular attachment plates. {ECO:0000269|PubMed:11851880}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Limb-girdle muscular dystrophy 2Q (LGMD2Q) [MIM:613723]: A form of limb-girdle muscular dystrophy characterized by early childhood onset of proximal muscle weakness. Limb-girdle muscular dystrophies are characterized by proximal weakness, weakness of the hip and shoulder girdles and prominent asymmetrical quadriceps femoris and biceps brachii atrophy. {ECO:0000269|PubMed:21109228}. Note=The disease is caused by mutations affecting the gene represented in this entry. A 9 bp deletion containing the initiation codon in exon 1f of PLEC have been found in limb-girdle muscular dystrophy patients. The mutation results in deficient expression of isoform 9 and disorganization of the myofibers, without any effect on the skin.; DISEASE: Epidermolysis bullosa simplex with nail dystrophy (EBSND) [MIM:616487]: A form of epidermolysis bullosa, a dermatologic disorder characterized by skin blistering. EBSND patients also manifest nail dystrophy. {ECO:0000269|PubMed:25712130}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed with highest levels in muscle, heart, placenta and spinal cord.; myocardium;smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;colon;choroid;fovea centralis;vein;uterus;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach; lung;placenta;prefrontal cortex;ciliary ganglion;atrioventricular node;skeletal muscle; 0.27288 0.29936 -6.570947902 0.029488087 16481.80337 27.47256 PLEK 0.140273936864108 0.855599477896883 0.00412658523900931 pleckstrin FUNCTION: Major protein kinase C substrate of platelets.; . . lymphoreticular;umbilical cord;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;aorta; superior cervical ganglion;white blood cells;trigeminal ganglion;whole blood;bone marrow; 0.34825 0.35190 0.551232944 81.48148148 4966.91179 14.36411 PLEK2 2.21898388320313e-08 0.258724280904676 0.741275696905485 pleckstrin 2 FUNCTION: May help orchestrate cytoskeletal arrangement. Contribute to lamellipodia formation.; . . unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;blood;skin;uterus;pancreas;prostate;lung;placenta;iris;liver;testis;amniotic fluid;cervix;spleen;kidney;stomach; superior cervical ganglion;lung;adrenal gland;thyroid;adrenal cortex;fetal thyroid;bone marrow; 0.14972 0.10903 -0.336073593 30.55555556 193.25839 3.01519 PLEKHA1 0.0177773375494199 0.977683534174853 0.00453912827572677 pleckstrin homology domain containing A1 FUNCTION: Binds specifically to phosphatidylinositol 3,4- diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane. {ECO:0000269|PubMed:11001876, ECO:0000269|PubMed:11513726, ECO:0000269|PubMed:14516276}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle, thymus, pancreas, placenta and lung. Detected at low levels in brain, heart, peripheral blood leukocytes, testis, ovary, spinal cord, thyroid, kidney, liver, small intestine and colon. {ECO:0000269|PubMed:11001876, ECO:0000269|PubMed:12101241}.; . . 0.31891 0.16525 -0.468351206 23.42533616 38.82145 1.14944 PLEKHA2 0.363909173512548 0.635581880626566 0.00050894586088633 pleckstrin homology domain containing A2 FUNCTION: Binds specifically to phosphatidylinositol 3,4- diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in heart, kidney, spleen and peripheral blood leukocytes. Detected at lower levels in brain, skeletal muscle, colon, thymus, liver, small intestine, placenta and lung.; . . 0.10334 0.09618 . . 105.05066 2.21730 PLEKHA3 0.0229786985598172 0.962098629904002 0.0149226715361807 pleckstrin homology domain containing A3 FUNCTION: Involved in Golgi to cell surface membrane traffic. Induces membrane tubulation. Binds preferentially to phosphatidylinositol 4-phosphate (PtdIns4P). {ECO:0000269|PubMed:15107860}.; . TISSUE SPECIFICITY: Widely expressed.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;blood;lens;lung;placenta;macula lutea;hippocampus;liver;head and neck;kidney;stomach;aorta; dorsal root ganglion;amygdala;trigeminal ganglion;parietal lobe; 0.34323 0.12662 -0.117432389 44.89266336 32.59321 1.01385 PLEKHA3P1 . . . pleckstrin homology domain containing A3 pseudogene 1 . . . . . . . . . . . PLEKHA4 4.7425343910477e-09 0.997474285477484 0.00252570977998181 pleckstrin homology domain containing A4 FUNCTION: Binds specifically to phosphatidylinositol 3-phosphate (PtdIns3P), but not to other phosphoinositides. {ECO:0000269|PubMed:11001876}.; . TISSUE SPECIFICITY: Highly expressed in melanoma. Detected at low levels in heart, skeletal muscle, kidney, liver and small intestine. {ECO:0000269|PubMed:11001876}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;oesophagus;endometrium;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;greater omentum;pancreas;lung;nasopharynx;placenta;macula lutea;spleen;kidney; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;olfactory bulb;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08565 0.08349 0.029399861 55.83274357 3929.34724 12.39401 PLEKHA5 0.999999407945124 5.92054875554991e-07 1.20287826475609e-18 pleckstrin homology domain containing A5 . . TISSUE SPECIFICITY: Highly expressed in heart and kidney. {ECO:0000269|PubMed:11001876}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;thyroid;pituitary gland;testis;brain;pineal gland;unclassifiable (Anatomical System);trophoblast;cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;liver;spleen;kidney;stomach; superior cervical ganglion;prefrontal cortex; 0.15553 0.09677 -0.418800956 25.79028073 470.79608 4.49027 PLEKHA6 0.981969069730327 0.0180309260510664 4.21860689557298e-09 pleckstrin homology domain containing A6 . . TISSUE SPECIFICITY: Highly expressed in heart, kidney and throughout the brain.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;frontal lobe;thyroid;bone;testis;dura mater;spinal ganglion;brain;unclassifiable (Anatomical System);meninges;heart;islets of Langerhans;pineal body;lens;breast;pancreas;lung;pia mater;placenta;macula lutea;liver;spleen;kidney;stomach; subthalamic nucleus;superior cervical ganglion;placenta;globus pallidus;trigeminal ganglion;skeletal muscle; 0.21929 0.11756 -1.207107349 5.726586459 192.56504 3.00941 PLEKHA7 0.000173040691290598 0.999826872980552 8.63281575791625e-08 pleckstrin homology domain containing A7 FUNCTION: Required for zonula adherens biogenesis and maintenance. Acts via its interaction with KIAA1543/Nezha, which anchors microtubules at their minus-ends to zonula adherens, leading to the recruitment of KIFC3 kinesin to the junctional site. {ECO:0000269|PubMed:19041755}.; . . colon;choroid;fovea centralis;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;amniotic fluid;brain;unclassifiable (Anatomical System);heart;lacrimal gland;lens;breast;lung;placenta;visual apparatus;macula lutea;liver;spleen;kidney;mammary gland;stomach; . 0.51293 0.10618 -1.385325458 4.334748762 980.5933 6.04599 PLEKHA8 2.06117242932264e-06 0.8892582644555 0.110739674372071 pleckstrin homology domain containing A8 FUNCTION: Cargo transport protein that is required for apical transport from the Golgi complex. Transports AQP2 from the trans- Golgi network (TGN) to sites of AQP2 phosphorylation. Mediates the non-vesicular transport of glucosylceramide (GlcCer) from the trans-Golgi network (TGN) to the plasma membrane and plays a pivotal role in the synthesis of complex glycosphingolipids. Binding of both phosphatidylinositol 4-phosphate (PIP) and ARF1 are essential for the GlcCer transfer ability. Also required for primary cilium formation, possibly by being involved in the transport of raft lipids to the apical membrane, and for membrane tubulation. {ECO:0000269|PubMed:15107860, ECO:0000269|PubMed:16103222, ECO:0000269|PubMed:17687330}.; . TISSUE SPECIFICITY: Expressed in kidney cell lines. {ECO:0000269|PubMed:15107860}.; unclassifiable (Anatomical System);optic nerve;whole body;islets of Langerhans;placenta;macula lutea;adrenal cortex;fovea centralis;choroid;lens;retina; . 0.08799 . 0.238945317 69.20853975 53.39698 1.45196 PLEKHA8P1 . . . pleckstrin homology domain containing A8 pseudogene 1 . . . unclassifiable (Anatomical System);islets of Langerhans;choroid;fovea centralis;lens;retina;whole body;optic nerve;placenta;macula lutea;liver;brain;peripheral nerve; . 0.20956 . . . . . PLEKHB1 0.000703306678862264 0.751941199643314 0.247355493677824 pleckstrin homology domain containing B1 FUNCTION: Required for proper localization of retinogeniculate projections but not for eye-specific segregation. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in retina and brain. Levels are very low or not detectable in all other tissues tested. {ECO:0000269|PubMed:10585447}.; myocardium;ovary;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;cerebral cortex;thyroid;pituitary gland;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;cerebellum cortex;islets of Langerhans;hypothalamus;pineal body;pharynx;blood;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;kidney;mammary gland;cerebellum; whole brain;amygdala;medulla oblongata;occipital lobe;thalamus;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.20802 0.13202 -0.538132194 20.26421326 50.1215 1.39067 PLEKHB2 3.5372142088758e-06 0.573002701184583 0.426993761601208 pleckstrin homology domain containing B2 FUNCTION: Involved in retrograde transport of recycling endosomes. {ECO:0000269|PubMed:21911378, ECO:0000269|PubMed:22281740}.; . . ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;synovium;thyroid;testis;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach;cerebellum; amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;superior cervical ganglion;hypothalamus;spinal cord;pons;caudate nucleus;prefrontal cortex;globus pallidus;kidney;cingulate cortex;parietal lobe;cerebellum; 0.16785 . -0.427900189 25.14744043 21.94762 0.73814 PLEKHD1 . . . pleckstrin homology and coiled-coil domain containing D1 . . . . . . . 0.349177632 74.18023119 83.12271 1.93789 PLEKHF1 0.0990669966135396 0.771755985096265 0.129177018290195 pleckstrin homology and FYVE domain containing 1 FUNCTION: May induce apoptosis through the lysosomal-mitochondrial pathway. Translocates to the lysosome initiating the permeabilization of lysosomal membrane (LMP) and resulting in the release of CTSD and CTSL to the cytoplasm. Triggers the caspase- independent apoptosis by altering mitochondrial membrane permeabilization (MMP) resulting in the release of PDCD8. {ECO:0000269|PubMed:16188880}.; . TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle. Weakly expressed in brain, thymus, spleen, kidney, liver, small intestine, placenta and lung. {ECO:0000269|PubMed:16188880}.; . . 0.04688 0.13491 -0.560178693 19.30879925 38.96945 1.15523 PLEKHF2 0.749566016857493 0.240363271254735 0.0100707118877721 pleckstrin homology and FYVE domain containing 2 FUNCTION: May play a role in early endosome fusion upstream of RAB5, hence regulating receptor trafficking and fluid-phase transport. Enhances cellular sensitivity to TNF-induced apoptosis (PubMed:18288467). {ECO:0000269|PubMed:18288467, ECO:0000269|PubMed:19995552, ECO:0000269|PubMed:22816767}.; . TISSUE SPECIFICITY: Expressed in placenta, ovary and small intestine, as well as in heart and pancreas. Also expressed in peripheral blood mononuclear cells and dendritic cells. {ECO:0000269|PubMed:18288467}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;atrium;whole body;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;kidney;mammary gland;stomach;aorta; superior cervical ganglion;atrioventricular node;trigeminal ganglion;tonsil; 0.29519 0.11565 -0.119252484 44.53880632 1.97572 0.06465 PLEKHG1 0.000178677408303547 0.999772148022059 4.917456963777e-05 pleckstrin homology and RhoGEF domain containing G1 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;blood;skin;uterus;pancreas;lung;cochlea;endometrium;thyroid;placenta;liver;testis;head and neck;spleen;germinal center;kidney;brain;pineal gland;stomach;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.15894 . 0.040318672 56.9297004 721.7254 5.33170 PLEKHG2 3.5925547959503e-08 0.999315130730636 0.000684833343816219 pleckstrin homology and RhoGEF domain containing G2 FUNCTION: May be a transforming oncogene with exchange activity for CDC42 (By similarity). May be a guanine-nucleotide exchange factor (GEF) for RAC1 and CDC42. Activated by the binding to subunits beta and gamma of the heterotrimeric guanine nucleotide- binding protein (G protein). {ECO:0000250, ECO:0000269|PubMed:18045877}.; . . lymphoreticular;ovary;colon;skin;uterus;optic nerve;endometrium;thyroid;bone;testis;germinal center;spinal ganglion;bladder;brain;unclassifiable (Anatomical System);cartilage;blood;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;medulla oblongata;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13369 0.09791 0.50696326 80.01297476 1308.42829 6.80345 PLEKHG3 1.16377189060086e-08 0.929295844855607 0.0707041435066745 pleckstrin homology and RhoGEF domain containing G3 . . . colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;testis;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;hippocampus;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;occipital lobe;thalamus;placenta;globus pallidus;caudate nucleus;trigeminal ganglion; 0.15905 0.09134 -0.205841949 38.28733192 619.10841 5.01885 PLEKHG4 1.46441415776125e-09 0.999438411065502 0.00056158747008416 pleckstrin homology and RhoGEF domain containing G4 FUNCTION: Possible role in intracellular signaling and cytoskeleton dynamics at the Golgi.; . TISSUE SPECIFICITY: Expressed in kidney, Leydig cells in the testis, epithelial cells in the prostate gland and Langerhans islet in the pancreas. Isoform 1 and isoform 3 are strongly expressed in Purkinje cells and to a lower extent in other neurons (at protein level). Widely expressed at low levels. More strongly expressed in testis and pancreas. {ECO:0000269|PubMed:16001362}.; unclassifiable (Anatomical System);heart;ovary;urinary;colon;parathyroid;skin;skeletal muscle;bone marrow;optic nerve;whole body;lung;bone;placenta;visual apparatus;liver;testis;cervix;spleen;kidney;tonsil; . 0.20106 0.16566 0.567625503 81.74687426 6305.5423 16.60897 PLEKHG4B 7.81216708928923e-20 0.0255727375566116 0.974427262443388 pleckstrin homology and RhoGEF domain containing G4B . . . unclassifiable (Anatomical System);pancreas;lymph node;lung;endometrium;visual apparatus;hypopharynx;testis;head and neck;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.10939 . -0.104929179 45.61217268 7254.54405 18.33443 PLEKHG5 4.02821229083025e-05 0.999542447593328 0.000417270283763282 pleckstrin homology and RhoGEF domain containing G5 FUNCTION: Guanine nucleotide exchange factor that activates RHOA and maybe the NF-kappa-B signaling pathway. Involved in the control of neuronal cell differentiation. Plays a role in angiogenesis through regulation of endothelial cells chemotaxis. {ECO:0000269|PubMed:11704860, ECO:0000269|PubMed:12761501}.; DISEASE: Charcot-Marie-Tooth disease, recessive, intermediate type, C (CMTRIC) [MIM:615376]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Recessive intermediate forms of Charcot-Marie-Tooth disease are characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. {ECO:0000269|PubMed:23777631, ECO:0000269|PubMed:23844677}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in the peripheral nervous system and brain. Highest expression is observed in heart, lung, kidney, testis and moderate expression is present in spleen, pancreas, skeletal muscle, ovary and liver. Weakly expressed in glioblastoma (GBM) cell lines. {ECO:0000269|PubMed:11704860, ECO:0000269|PubMed:16467373, ECO:0000269|PubMed:9872452}.; colon;fovea centralis;choroid;retina;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;head and neck;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;kidney;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.11331 0.50568 1.146346745 92.3920736 2745.09927 9.87912 PLEKHG6 1.17026398871661e-10 0.979856497986193 0.020143501896781 pleckstrin homology and RhoGEF domain containing G6 FUNCTION: Guanine nucleotide exchange factor activating the small GTPase RHOA, which, in turn, induces myosin filament formation. Also activates RHOG. Does not activate RAC1, or to a much lower extent than RHOA and RHOG. Part of a functional unit, involving PLEKHG6, MYH10 and RHOA, at the cleavage furrow to advance furrow ingression during cytokinesis. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with EZR, required for normal macropinocytosis. {ECO:0000269|PubMed:16721066, ECO:0000269|PubMed:17881735}.; . TISSUE SPECIFICITY: Highest expression in the placenta. Low levels in small intestine, lung, liver, kidney, thymus and heart.; lung;larynx;placenta;liver;colon;spleen;head and neck;brain;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.06909 0.08573 -0.788160233 12.62679877 740.31473 5.40276 PLEKHG7 3.6750124896981e-11 0.0890940045439959 0.910905995419254 pleckstrin homology and RhoGEF domain containing G7 . . . unclassifiable (Anatomical System);lung;kidney;germinal center; . 0.19160 . 0.463046108 78.58575136 319.25993 3.79421 PLEKHH1 0.000660284566746353 0.99933819380756 1.52162569363147e-06 pleckstrin homology, MyTH4 and FERM domain containing H1 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;amniotic fluid;brain;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;spinal cord;lens;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach;peripheral nerve; . 0.14941 0.08380 1.256589163 93.48903043 7095.83143 18.11317 PLEKHH2 1.78874098604568e-26 0.0302702587581157 0.969729741241884 pleckstrin homology, MyTH4 and FERM domain containing H2 FUNCTION: In the kidney glomerulus may play a role in linking podocyte foot processes to the glomerular basement membrane. May be involved in stabilization of F-actin by attenuating its depolymerization. Can recruit TGFB1I1 from focal adhesions to podocyte lamellipodia.; . TISSUE SPECIFICITY: Kidney. Reduced expression in patients with focal segmental glomerulosclerosis. {ECO:0000269|PubMed:22832517}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;brain;artery;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;hippocampus;kidney;mammary gland;stomach;aorta; globus pallidus;atrioventricular node; 0.12448 0.09100 -0.823216783 11.68318 2775.67326 9.94659 PLEKHH3 0.00376066186801617 0.99443738678073 0.00180195135125407 pleckstrin homology, MyTH4 and FERM domain containing H3 . . . smooth muscle;ovary;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;endometrium;cerebral cortex;thyroid;bone;testis;spinal ganglion;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;lens;pancreas;lung;placenta;macula lutea;hippocampus;head and neck;kidney;stomach; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.57588 0.09682 -0.955204708 9.170794999 149.26629 2.66346 PLEKHJ1 0.463248129638187 0.511195378859832 0.025556491501981 pleckstrin homology domain containing J1 . . TISSUE SPECIFICITY: Expressed in testis and liver. {ECO:0000269|PubMed:11602354}.; myocardium;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach;cerebellum;thymus; dorsal root ganglion;testis - interstitial;fetal thyroid; 0.13621 0.11480 . . 220.49058 3.20978 PLEKHM1 0.840543209831517 0.159451519909843 5.27025863998621e-06 pleckstrin homology and RUN domain containing M1 FUNCTION: Proposed to act as a multivalent adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways. Required for late stages of endolysosomal maturation, facilitating both endocytosis-mediated degradation of growth factor receptors and autophagosome clearance. Seems to be involved in the terminal maturation of autophagosomes and to mediate autophagosome-lysosome fusion (PubMed:25498145). Involved in vesicular transport in the osteoclast (By similarity). May be involved in negative regulation of endocytic transport from early endosome to late endosome/lysosome implicating its association with Rab7 (PubMed:20943950). May have a role in sialyl-lex-mediated transduction of apoptotic signals (PubMed:12820725). In case of infection contributes to Salmonella typhimurium pathogenesis by supporting the integrity of the Salmonella-containing vacuole (SCV) probably in concert with the HOPS complex and Rab7 (PubMed:25500191). {ECO:0000250|UniProtKB:Q5PQS0, ECO:0000269|PubMed:12820725, ECO:0000269|PubMed:20943950, ECO:0000269|PubMed:25498145, ECO:0000269|PubMed:25500191, ECO:0000305}.; DISEASE: Osteopetrosis, autosomal recessive 6 (OPTB6) [MIM:611497]: A rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Recessive osteopetrosis commonly manifests in early infancy with macrocephaly, feeding difficulties, evolving blindness and deafness, bone marrow failure, severe anemia, and hepatosplenomegaly. Deafness and blindness are generally thought to represent effects of pressure on nerves. {ECO:0000269|PubMed:17404618}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in placenta, liver, prostate, thymus, spleen, ovary, colon, colon carcinoma and peripheral blood lymphocytes (PBL). Weakly expressed in brain, lung, kidney, and testis. No expression in heart, skeletal muscle, pancreas and small intestine. Predominantly expressed in the breast carcinoma cell line MCF-7. {ECO:0000269|PubMed:12820725, ECO:0000269|PubMed:9205841}.; . . 0.11340 . -1.52667341 3.408822836 93.29293 2.07893 PLEKHM1P1 . . . pleckstrin homology and RUN domain containing M1 pseudogene 1 . . . . . . 0.09794 . . . . PLEKHM2 0.00506557458482561 0.994696541629096 0.000237883786078504 pleckstrin homology and RUN domain containing M2 FUNCTION: May play a role in the regulation of conventional kinesin activity. Required for maintenance of the Golgi apparatus organization. May play a role in membrane tubulation. {ECO:0000269|PubMed:15905402}.; . . . . 0.21876 0.10940 -0.571310997 19.01391838 2855.41812 10.11202 PLEKHM3 0.76624837589687 0.23374853188346 3.09221966953743e-06 pleckstrin homology domain containing M3 . . . . . 0.33952 . 0.020302773 55.60863411 227.97013 3.26076 PLEKHN1 2.01974835522321e-08 0.659994782009553 0.340005197792964 pleckstrin homology domain containing N1 . . . . . 0.19904 0.09620 0.900159287 89.32531257 709.4528 5.29021 PLEKHO1 0.949230797050779 0.0507363655357069 3.28374135142243e-05 pleckstrin homology domain containing O1 FUNCTION: Plays a role in the regulation of the actin cytoskeleton through its interactions with actin capping protein (CP). May function to target CK2 to the plasma membrane thereby serving as an adapter to facilitate the phosphorylation of CP by protein kinase 2 (CK2). Appears to target ATM to the plasma membrane. Appears to also inhibit tumor cell growth by inhibiting AKT- mediated cell-survival. Also implicated in PI3K-regulated muscle differentiation, the regulation of AP-1 activity (plasma membrane bound AP-1 regulator that translocates to the nucleus) and the promotion of apoptosis induced by tumor necrosis factor TNF. When bound to PKB, it inhibits it probably by decreasing PKB level of phosphorylation. {ECO:0000269|PubMed:14729969, ECO:0000269|PubMed:15706351, ECO:0000269|PubMed:15831458, ECO:0000269|PubMed:16325375, ECO:0000269|PubMed:16987810, ECO:0000269|PubMed:17197158, ECO:0000269|PubMed:17942896}.; . TISSUE SPECIFICITY: Abundantly expressed in skeletal muscle and heart, moderately in kidney, liver, brain and placenta and sparingly in the pancreas and lung. Easily detectable in cell lines such as MOLT-4, HEK293 and Jurkat. {ECO:0000269|PubMed:17197158}.; lymphoreticular;ovary;salivary gland;developmental;intestine;colon;skin;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;pharynx;blood;skeletal muscle;pancreas;lung;cornea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; . 0.09694 0.08726 -0.468351206 23.42533616 202.67074 3.07247 PLEKHO2 0.0047538423246732 0.965958577118467 0.0292875805568602 pleckstrin homology domain containing O2 . . . unclassifiable (Anatomical System);cartilage;ovary;heart;lacrimal gland;colon;blood;skin;skeletal muscle;retina;pancreas;optic nerve;lung;frontal lobe;bone;thyroid;placenta;liver;testis;spleen;germinal center;kidney;brain;bladder;stomach; trigeminal ganglion; 0.36813 0.09414 0.023941474 55.75607455 1234.77161 6.63959 PLEKHS1 1.17132107467687e-15 0.00285046059579109 0.997149539404208 pleckstrin homology domain containing S1 . . . . . 0.11876 . 1.330184494 94.17315405 1013.95545 6.12897 PLET1 . . . placenta expressed transcript 1 FUNCTION: Modulates leading keratinocyte migration and cellular adhesion to matrix proteins during a wound-healing response and promotes wound repair. May play a role during trichilemmal differentiation of the hair follicle (By similarity). {ECO:0000250}.; . . . . 0.03469 . . . 134.29607 2.52029 PLG 0.00243511733948206 0.997536808056632 2.80746038859423e-05 plasminogen FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells. {ECO:0000269|PubMed:14699093}.; DISEASE: Plasminogen deficiency (PLGD) [MIM:217090]: A disorder characterized by decreased serum plasminogen activity. Two forms of the disorder are distinguished: type 1 deficiency is additionally characterized by decreased plasminogen antigen levels and clinical symptoms, whereas type 2 deficiency, also known as dysplasminogenemia, is characterized by normal, or slightly reduced antigen levels, and absence of clinical manifestations. Plasminogen deficiency type 1 results in markedly impaired extracellular fibrinolysis and chronic mucosal pseudomembranous lesions due to subepithelial fibrin deposition and inflammation. The most common clinical manifestation of type 1 deficiency is ligneous conjunctivitis in which pseudomembranes formation on the palpebral surfaces of the eye progresses to white, yellow-white, or red thick masses with a wood-like consistency that replace the normal mucosa. {ECO:0000269|PubMed:10233898, ECO:0000269|PubMed:1427790, ECO:0000269|PubMed:1986355, ECO:0000269|PubMed:6216475, ECO:0000269|PubMed:6238949, ECO:0000269|PubMed:8392398, ECO:0000269|PubMed:9242524, ECO:0000269|PubMed:9858247}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Present in plasma and many other extracellular fluids. It is synthesized in the liver.; unclassifiable (Anatomical System);lung;frontal lobe;adrenal medulla;adrenal cortex;liver;testis;spleen;kidney; fetal liver;superior cervical ganglion;liver;fetal lung;kidney;trigeminal ganglion;skeletal muscle; 0.23308 0.77395 0.628293289 83.56923803 327.60602 3.84774 PLGLA . . . plasminogen-like A (pseudogene) FUNCTION: May bind non-covalently to lysine binding sites present in the kringle structures of plasminogen. This may interfere with the binding of fibrin or alpha-2-antiplasmin to plasminogen and may result in the localization of activity at sites necessary for extracellular matrix destruction (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:10092845}.; unclassifiable (Anatomical System);islets of Langerhans;uterus;prostate;lung;endometrium;bone;thyroid;visual apparatus;liver;testis;head and neck;spleen;germinal center;brain;stomach; . 0.04989 . . . . . PLGLB1 . . . plasminogen-like B1 FUNCTION: May bind noncovalently to lysine binding sites present in the kringle structures of plasminogen. This may interfere with the binding of fibrin or alpha-2-antiplasmin to plasminogen and may result in the localization of activity at sites necessary for extracellular matrix destruction.; . . unclassifiable (Anatomical System);islets of Langerhans;uterus;prostate;lung;endometrium;bone;thyroid;visual apparatus;liver;testis;head and neck;spleen;germinal center;brain;stomach; . . . . . 46.38158 1.31276 PLGLB2 . . . plasminogen-like B2 FUNCTION: May bind noncovalently to lysine binding sites present in the kringle structures of plasminogen. This may interfere with the binding of fibrin or alpha-2-antiplasmin to plasminogen and may result in the localization of activity at sites necessary for extracellular matrix destruction.; . . unclassifiable (Anatomical System);islets of Langerhans;uterus;prostate;lung;endometrium;bone;thyroid;visual apparatus;liver;testis;head and neck;spleen;germinal center;brain;stomach; . . . . . 24.22249 0.79537 PLGRKT 8.35916111034872e-08 0.0454931474226257 0.954506768985763 plasminogen receptor, C-terminal lysine transmembrane protein FUNCTION: Receptor for plasminogen. Regulates urokinase plasminogen activator-dependent and stimulates tissue-type plasminogen activator-dependent cell surface plasminogen activation. Proposed to be part of a local catecholaminergic cell plasminogen activation system that regulates neuroendocrine prohormone processing. Involved in regulation of inflammatory response; regulates monocyte chemotactic migration and matrix metallproteinase activation, such as of MMP2 and MMP9. {ECO:0000269|PubMed:21940822}.; . TISSUE SPECIFICITY: Expressed in peripheral blood cells and monocytes. Expressed in adrenal medulla. {ECO:0000269|PubMed:21795689, ECO:0000269|PubMed:21940822}.; . . 0.16089 0.10340 0.215080721 67.91696155 191.96386 3.00409 PLIN1 3.5584340242688e-07 0.340817787800349 0.659181856356248 perilipin 1 FUNCTION: Modulator of adipocyte lipid metabolism. Coats lipid storage droplets to protect them from breakdown by hormone- sensitive lipase (HSL). Its absence may result in leanness. Plays a role in unilocular lipid droplet formation by activating CIDEC. Their interaction promotes lipid droplet enlargement and directional net neutral lipid transfer. May modulate lipolysis and triglyceride levels. {ECO:0000269|PubMed:23399566}.; DISEASE: Lipodystrophy, familial partial, 4 (FPLD4) [MIM:613877]: A form of lipodystrophy characterized by loss of subcutaneous adipose tissue primarily affecting the lower limbs, insulin- resistant diabetes mellitus, hypertriglyceridemia, and hypertension. {ECO:0000269|PubMed:21345103}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Adipocytes. {ECO:0000269|PubMed:9521880}.; unclassifiable (Anatomical System);amygdala;heart;cartilage;muscle;skin;skeletal muscle;breast;lung;bone;hippocampus;liver;testis;spleen;kidney;mammary gland; testis - interstitial;adipose tissue;trachea;adrenal gland;ciliary ganglion;fetal thyroid;thymus; 0.14339 0.29048 0.756930627 86.79523473 355.36912 3.98896 PLIN2 1.19940435129965e-05 0.596644629245569 0.403343376710918 perilipin 2 FUNCTION: May be involved in development and maintenance of adipose tissue. {ECO:0000250}.; . TISSUE SPECIFICITY: Milk lipid globules.; lymphoreticular;ovary;skin;retina;prostate;optic nerve;endometrium;cochlea;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;bile duct;pancreas;lung;pia mater;mesenchyma;nasopharynx;placenta;kidney;stomach; adipose tissue;placenta;liver;skeletal muscle; 0.22429 0.48822 0.042348793 57.31304553 314.02328 3.76717 PLIN3 1.2373923055107e-08 0.10291097247641 0.897089015149667 perilipin 3 FUNCTION: Required for the transport of mannose 6-phosphate receptors (MPR) from endosomes to the trans-Golgi network. {ECO:0000269|PubMed:9590177}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;cornea;mesenchyma;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;head and neck;kidney;mammary gland;aorta;stomach; testis - interstitial;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.09274 0.13630 -0.216746887 37.69757018 119.09857 2.37440 PLIN4 1.65846988023811e-12 0.0077104331342539 0.992289566864088 perilipin 4 FUNCTION: May play a role in triacylglycerol packaging into adipocytes. May function as a coat protein involved in the biogenesis of lipid droplets (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;ovary;lacrimal gland;cerebral cortex;testis;colon;brain; . 0.16259 0.10200 5.994578529 99.85845718 9818.87991 21.57786 PLIN5 1.3236836849853e-07 0.205432119870623 0.794567747761008 perilipin 5 FUNCTION: Lipid droplet-associated protein that maintains the balance between lipogenesis and lipolysis and also regulates fatty acid oxidation in oxidative tissues. Recruits mitochondria to the surface of lipid droplets and is involved in lipid droplet homeostasis by regulating both the storage of fatty acids in the form of triglycerides and the release of fatty acids for mitochondrial fatty acid oxidation. In lipid droplet triacylglycerol hydrolysis, plays a role as a scaffolding protein for three major key lipolytic players: ABHD5, PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets. Phosphorylation by PKA enables lipolysis probably by promoting release of ABHD5 from the perilipin scaffold and by facilitating interaction of ABHD5 with PNPLA2. Also increases lipolysis through interaction with LIPE and upon PKA-mediated phosphorylation of LIPE (By similarity). {ECO:0000250, ECO:0000269|PubMed:17234449}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, liver, heart and kidney. {ECO:0000269|PubMed:17234449}.; . . . . . . 727.10313 5.35602 PLK1 0.994120613063786 0.00587922564086286 1.61295351282845e-07 polo like kinase 1 FUNCTION: Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGOL1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1 and WEE1. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ, NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1. Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains. Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase. Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGOL1: required for spindle pole localization of isoform 3 of SGOL1 and plays a role in regulating its centriole cohesion function. Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome. Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53. Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis. Phosphorylates MISP, leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning (PubMed:8991084, PubMed:11202906, PubMed:12207013, PubMed:12447691, PubMed:12524548, PubMed:12738781, PubMed:12852856, PubMed:12939256, PubMed:14532005, PubMed:14734534, PubMed:15070733, PubMed:15148369, PubMed:15469984, PubMed:16198290, PubMed:16247472, PubMed:16980960, PubMed:17081991, PubMed:17351640, PubMed:17376779, PubMed:17617734, PubMed:18174154, PubMed:18331714, PubMed:18418051, PubMed:18477460, PubMed:18521620, PubMed:18615013, PubMed:19160488, PubMed:19351716, PubMed:19468300, PubMed:19468302, PubMed:19473992, PubMed:19509060, PubMed:19597481, PubMed:23455478, PubMed:23509069). Together with MEIKIN, acts as a regulator of kinetochore function during meiosis I: required both for mono- orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage (By similarity). Phosphorylates CEP68 and is required for its degradation (PubMed:25503564). {ECO:0000250|UniProtKB:Q5F2C3, ECO:0000269|PubMed:11202906, ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:12447691, ECO:0000269|PubMed:12524548, ECO:0000269|PubMed:12738781, ECO:0000269|PubMed:12852856, ECO:0000269|PubMed:12939256, ECO:0000269|PubMed:14532005, ECO:0000269|PubMed:14734534, ECO:0000269|PubMed:15070733, ECO:0000269|PubMed:15148369, ECO:0000269|PubMed:15469984, ECO:0000269|PubMed:16198290, ECO:0000269|PubMed:16247472, ECO:0000269|PubMed:16980960, ECO:0000269|PubMed:17081991, ECO:0000269|PubMed:17351640, ECO:0000269|PubMed:17376779, ECO:0000269|PubMed:17617734, ECO:0000269|PubMed:18174154, ECO:0000269|PubMed:18331714, ECO:0000269|PubMed:18418051, ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:18521620, ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:19160488, ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302, ECO:0000269|PubMed:19473992, ECO:0000269|PubMed:19509060, ECO:0000269|PubMed:19597481, ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:23509069, ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:8991084}.; DISEASE: Note=Defects in PLK1 are associated with some cancers, such as gastric, thyroid or B-cell lymphomas. Expression is cancer increased in tumor tissues with a poor prognosis, suggesting a role in malignant transformations and carcinogenesis.; TISSUE SPECIFICITY: Placenta and colon.; lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;thyroid;germinal center;bladder;brain;tonsil;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;muscle;bile duct;pancreas;lung;cornea;placenta;duodenum;head and neck;kidney;stomach; dorsal root ganglion;fetal liver;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.99699 0.63475 -0.290161348 33.33923095 97.38524 2.13194 PLK2 0.998863614916352 0.0011363821596999 2.9239476803442e-09 polo like kinase 2 FUNCTION: Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress. {ECO:0000269|PubMed:15242618, ECO:0000269|PubMed:19001868, ECO:0000269|PubMed:20352051, ECO:0000269|PubMed:20531387}.; . TISSUE SPECIFICITY: Expressed at higher level in the fetal lung, kidney, spleen and heart. {ECO:0000269|PubMed:11696980}.; ovary;salivary gland;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;amniotic fluid;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;amnion;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;smooth muscle;prefrontal cortex;testis;caudate nucleus; 0.34084 0.11005 -0.380166007 27.88393489 52.84148 1.44174 PLK3 6.24924446856326e-05 0.994577897868844 0.00535960968647044 polo like kinase 3 FUNCTION: Serine/threonine-protein kinase involved in cell cycle regulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2, HIF1A, JUN, p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in cell cycle regulation: required for entry into S phase and cytokinesis. Phosphorylates BCL2L1, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Plays a key role in response to stress: rapidly activated upon stress stimulation, such as ionizing radiation, reactive oxygen species (ROS), hyperosmotic stress, UV irradiation and hypoxia. Involved in DNA damage response and G1/S transition checkpoint by phosphorylating CDC25A, p53/TP53 and p73/TP73. Phosphorylates p53/TP53 in response to reactive oxygen species (ROS), thereby promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in response to DNA damage, promoting the G2/M transition checkpoint. Phosphorylates the transcription factor p73/TP73 in response to DNA damage, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates HIF1A and JUN is response to hypoxia. Phosphorylates ATF2 following hyperosmotic stress in corneal epithelium. Also involved in Golgi disassembly during the cell cycle: part of a MEK1/MAP2K1-dependent pathway that induces Golgi fragmentation during mitosis by mediating phosphorylation of VRK1. May participate in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation, via its interaction with CIB1. {ECO:0000269|PubMed:10557092, ECO:0000269|PubMed:11156373, ECO:0000269|PubMed:11447225, ECO:0000269|PubMed:11551930, ECO:0000269|PubMed:11971976, ECO:0000269|PubMed:12242661, ECO:0000269|PubMed:14968113, ECO:0000269|PubMed:14980500, ECO:0000269|PubMed:15021912, ECO:0000269|PubMed:16478733, ECO:0000269|PubMed:16481012, ECO:0000269|PubMed:17264206, ECO:0000269|PubMed:17804415, ECO:0000269|PubMed:18062778, ECO:0000269|PubMed:18650425, ECO:0000269|PubMed:19103756, ECO:0000269|PubMed:19490146, ECO:0000269|PubMed:20889502, ECO:0000269|PubMed:20940307, ECO:0000269|PubMed:20951827, ECO:0000269|PubMed:21098032, ECO:0000269|PubMed:21264284, ECO:0000269|PubMed:21376736, ECO:0000269|PubMed:21840391, ECO:0000269|PubMed:9353331}.; . TISSUE SPECIFICITY: Transcripts are highly detected in placenta, lung, followed by skeletal muscle, heart, pancreas, ovaries and kidney and weakly detected in liver and brain. May have a short half-live. In cells of hematopoietic origin, strongly and exclusively detected in terminally differentiated macrophages. Transcript expression appears to be down-regulated in primary lung tumor.; . . 0.29709 0.18462 -1.109541557 6.782259967 54.52333 1.47654 PLK4 0.77798174923305 0.222017710737834 5.40029116157912e-07 polo like kinase 4 FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. {ECO:0000269|PubMed:16244668, ECO:0000269|PubMed:16326102, ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:18239451, ECO:0000269|PubMed:19164942, ECO:0000269|PubMed:21725316}.; DISEASE: Microcephaly and chorioretinopathy, autosomal recessive, 2 (MCCRP2) [MIM:616171]: A severe disorder characterized by microcephaly, delayed psychomotor development, growth retardation with dwarfism, and ocular abnormalities. {ECO:0000269|PubMed:25344692}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;tumor;atrioventricular node;skeletal muscle; 0.54171 0.24559 -0.306750577 32.23047889 93.45235 2.08037 PLK5 0.0716254602582295 0.526917476616289 0.401457063125482 polo like kinase 5 FUNCTION: Inactive serine/threonine-protein kinase that plays a role in cell cycle progression and neuronal differentiation. {ECO:0000269|PubMed:21245385}.; . TISSUE SPECIFICITY: Expressed in the brain, neurons and glial cells. Also expressed in highly differentiated cells, such as the serous acini in the parotid gland, distal and proximal tubules of the kidney, tubules of the seminal gland, Kupffer cells and some hepatocytes in the liver, and some cells in the germinal center of lymph nodes (at protein level). {ECO:0000269|PubMed:21245385}.; unclassifiable (Anatomical System);frontal lobe;testis;brain; globus pallidus;ciliary ganglion;atrioventricular node; . . . . 13099.05253 24.52475 PLLP 0.519581851885049 0.463357320160693 0.0170608279542581 plasmolipin FUNCTION: Appears to be involved in myelination. Could also participate in ion transport events as addition of plasmolipin to lipid bilayers induces the formation of ion channels, which are voltage-dependent and K(+)-selective (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;hypothalamus;sympathetic chain;colon;parathyroid;retina;breast;pancreas;prostate;lung;endometrium;placenta;hippocampus;liver;testis;spleen;cervix;kidney;brain;stomach; amygdala;whole brain;dorsal root ganglion;medulla oblongata;occipital lobe;thalamus;olfactory bulb;hypothalamus;spinal cord;caudate nucleus;pons;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.17595 0.12499 -0.117432389 44.89266336 21.02809 0.71216 PLN 0.111194228566321 0.598109980252846 0.290695791180833 phospholamban FUNCTION: Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN. ATP2A2 inhibition is alleviated by PLN phosphorylation. {ECO:0000269|PubMed:22427649, ECO:0000269|PubMed:22707725}.; DISEASE: Cardiomyopathy, dilated 1P (CMD1P) [MIM:609909]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:12610310, ECO:0000269|PubMed:16432188, ECO:0000269|PubMed:22137083}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, familial hypertrophic 18 (CMH18) [MIM:613874]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:12705874}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Heart muscle (at protein level). {ECO:0000269|PubMed:17241641}.; myocardium;smooth muscle;colon;skin;uterus;prostate;whole body;bone;testis;dura mater;artery;brain;spinal ganglion;unclassifiable (Anatomical System);meninges;heart;tongue;skeletal muscle;lung;pia mater;spleen;head and neck;kidney;stomach;aorta; uterus;testis - interstitial;superior cervical ganglion;trachea;heart;appendix;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.60443 . 0.12325821 62.38499646 2.24501 0.07526 PLOD1 2.70207303676794e-07 0.995480791834555 0.00451893795814163 procollagen-lysine, 2-oxoglutarate 5-dioxygenase 1 FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.; DISEASE: Ehlers-Danlos syndrome 6 (EDS6) [MIM:225400]: A connective tissue disorder characterized by generalized joint hypermobility, hyperextensible skin, atrophic cutaneous scars due to tissue fragility, progressive kyphoscoliosis already present at birth, ocular manifestations, arterial rupture, easy bruising, severe neonatal muscle hypotonia and delayed motor development. {ECO:0000269|PubMed:10686424, ECO:0000269|PubMed:15666309, ECO:0000269|PubMed:15854030, ECO:0000269|PubMed:15979919, ECO:0000269|PubMed:8163671, ECO:0000269|PubMed:9617436}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;brain;bladder;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; smooth muscle;heart;trigeminal ganglion;skeletal muscle; 0.25274 . -0.657684922 16.09459778 3458.35803 11.29956 PLOD2 0.00117484049993417 0.998744974564834 8.01849352316496e-05 procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2 FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.; DISEASE: Note=PLOD2 mutations give rise to a broad variety of phenotypes with variable degrees of severity of bone fragility and joint contractures. Disease-associated mutations have been found in patients with autosomal recessive osteogenesis imperfecta (AR- OI) (PubMed:22689593). {ECO:0000269|PubMed:22689593}.; TISSUE SPECIFICITY: Highly expressed in pancreas and muscle. Isoform 1 and isoform 2 are expressed in the majority of the examined cell types. Isoform 2 is specifically expressed in skin, lung, dura and aorta. {ECO:0000269|PubMed:10372558}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;gum;thyroid;bladder;brain;gall bladder;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);small intestine;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;smooth muscle;thyroid;fetal thyroid; 0.65048 0.12778 0.112125503 62.09601321 137.52121 2.55175 PLOD3 3.88014355176489e-08 0.98552291925712 0.014477041941444 procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3 FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.; DISEASE: Lysyl hydroxylase 3 deficiency (LH3 deficiency) [MIM:612394]: Connective tissue disorder. The syndrome is characterized by congenital malformations severely affecting many tissues and organs and revealing features of several collagen disorders, most of them involving COL2A1 (type II collagen). The findings suggest that the failure of lysyl hydroxylation and hydroxylysyl carbohydrate addition, which affects many collagens, is the molecular basis of this syndrome. {ECO:0000269|PubMed:18834968}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;myocardium;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;mesenchyma;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;placenta;atrioventricular node;trigeminal ganglion; 0.18416 0.34242 -1.122519798 6.581740977 585.12553 4.90470 PLP1 0.90295851162582 0.0962128011644449 0.000828687209735362 proteolipid protein 1 FUNCTION: This is the major myelin protein from the central nervous system. It plays an important role in the formation or maintenance of the multilamellar structure of myelin.; DISEASE: Leukodystrophy, hypomyelinating, 1 (HLD1) [MIM:312080]: A X-linked recessive disorder of the central nervous system in which myelin is not formed properly. Clinically characterized by nystagmus, spastic quadriplegia, ataxia, and developmental delay. {ECO:0000269|PubMed:10417279, ECO:0000269|PubMed:10425042, ECO:0000269|PubMed:11093273, ECO:0000269|PubMed:11786921, ECO:0000269|PubMed:1376966, ECO:0000269|PubMed:1384324, ECO:0000269|PubMed:15712223, ECO:0000269|PubMed:1707231, ECO:0000269|PubMed:1708672, ECO:0000269|PubMed:1715570, ECO:0000269|PubMed:2479017, ECO:0000269|PubMed:2480601, ECO:0000269|PubMed:2773936, ECO:0000269|PubMed:7531827, ECO:0000269|PubMed:7539213, ECO:0000269|PubMed:7541731, ECO:0000269|PubMed:7573159, ECO:0000269|PubMed:7679906, ECO:0000269|PubMed:7683951, ECO:0000269|PubMed:7684886, ECO:0000269|PubMed:8037216, ECO:0000269|PubMed:8909455, ECO:0000269|PubMed:9008538, ECO:0000269|PubMed:9143933, ECO:0000269|PubMed:9482656, ECO:0000269|PubMed:9633722, ECO:0000269|PubMed:9747038, ECO:0000269|PubMed:9788732, ECO:0000269|PubMed:9894878, ECO:0000269|PubMed:9934976}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spastic paraplegia 2, X-linked (SPG2) [MIM:312920]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG2 is characterized by spastic gait and hyperreflexia. In some patients, complicating features include nystagmus, dysarthria, sensory disturbance, mental retardation, optic atrophy. {ECO:0000269|PubMed:10319897, ECO:0000269|PubMed:11093273, ECO:0000269|PubMed:15450775, ECO:0000269|PubMed:17438221, ECO:0000269|PubMed:24103481, ECO:0000269|PubMed:7522741, ECO:0000269|PubMed:8012387, ECO:0000269|PubMed:8780101, ECO:0000269|PubMed:8956049, ECO:0000269|PubMed:9489796}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;sympathetic chain;parathyroid;skin;retina;bone marrow;subthalamic nucleus;whole body;ganglion;frontal lobe;endometrium;cochlea;cerebral cortex;bone;iris;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;heart;cerebellum cortex;hypothalamus;spinal cord;blood;cerebrum;skeletal muscle;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;mammary gland;cerebellum; whole brain;amygdala;dorsal root ganglion;thalamus;superior cervical ganglion;occipital lobe;medulla oblongata;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;atrioventricular node;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.95448 0.36844 0.013025609 54.62962963 5.34269 0.19831 PLP2 0.112369204580837 0.777772256915139 0.109858538504024 proteolipid protein 2 (colonic epithelium-enriched) FUNCTION: May play a role in cell differentiation in the intestinal epithelium.; . TISSUE SPECIFICITY: Enriched in colonic mucosa. The expression of A4 follows a gradient along the crypto-villus axis with the most abundant message occurring in the lower half of the crypt.; . . 0.34377 0.13160 -0.007201372 53.19061099 28.22389 0.90474 PLPP1 . . . phospholipid phosphatase 1 FUNCTION: Broad-specificity phosphohydrolase that dephosphorylates exogenous bioactive glycerolipids and sphingolipids. Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). Pivotal regulator of lysophosphatidic acid (LPA) signaling in the cardiovascular system. Major enzyme responsible of dephosphorylating LPA in platelets, which terminates signaling actions of LPA. May control circulating, and possibly also regulate localized, LPA levels resulting from platelet activation. It has little activity towards ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA > PA > S-1-P > C-1-P. It's down-regulation may contribute to the development of colon adenocarcinoma. {ECO:0000269|PubMed:12909631}.; . TISSUE SPECIFICITY: Ubiquitously expressed with highest expression found in prostate. Isoform 1 is predominant in kidney, lung, placenta and liver. Isoform 2 is predominant in heart and pancreas. Found to be down-regulated in colon adenocarcinomas.; . . 0.65495 . -0.249709319 35.74545883 . . PLPP2 . . . phospholipid phosphatase 2 FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1- phosphate (S-1-P). The relative catalytic efficiency is PA > C-1-P > LPA > S-1-P.; . TISSUE SPECIFICITY: Found mainly in brain, pancreas and placenta.; . . 0.45362 . 0.464864541 78.69190847 . . PLPP3 . . . phospholipid phosphatase 3 FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1- phosphate (S-1-P). The relative catalytic efficiency is LPA = PA > C-1-P > S-1-P. May be involved in cell adhesion and in cell-cell interactions.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in heart and placenta.; . . 0.27664 0.17892 -0.405853867 26.23260203 . . PLPP4 . . . phospholipid phosphatase 4 FUNCTION: Displays magnesium-independent phosphatidate phosphatase activity in vitro. Catalyzes the conversion of phosphatidic acid to diacylglycerol. {ECO:0000269|PubMed:17590538}.; . TISSUE SPECIFICITY: Expressed mainly to the brain, kidney and testis, and to a lesser extent the bone marrow, thymus, prostate, liver and uterus. {ECO:0000269|PubMed:17590538}.; . . 0.18611 0.10773 -0.249709319 35.74545883 . . PLPP5 . . . phospholipid phosphatase 5 FUNCTION: Displays magnesium-independent phosphatidate phosphatase activity in vitro. Catalyzes the conversion of phosphatidic acid to diacylglycerol. May be a metastatic suppressor for hepatocellular carcinoma. {ECO:0000269|PubMed:16261160, ECO:0000269|PubMed:17590538}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17590538}.; . . 0.10046 0.10138 0.215080721 67.91696155 . . PLPP6 . . . phospholipid phosphatase 6 FUNCTION: Phosphatase that dephosphorylates presqualene diphosphate (PSDP) into presqualene monophosphate (PSMP), suggesting that it may be indirectly involved in innate immunity. PSDP is a bioactive lipid that rapidly remodels to presqualene monophosphate PSMP upon cell activation. Displays diphosphate phosphatase activity with a substrate preference for PSDP > FDP > phosphatidic acid. {ECO:0000269|PubMed:16464866}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in most organs, in particular gastrointestinal organs, spleen, placenta, kidney, thymus and brain. {ECO:0000269|PubMed:16464866}.; . . 0.16577 . 0.194852702 67.03231894 . . PLPP7 . . . phospholipid phosphatase 7 (inactive) FUNCTION: Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity (By similarity). {ECO:0000250}.; . . . . 0.13175 . -0.291981272 33.20358575 . . PLPPR1 . . . phospholipid phosphatase related 1 . . . . . . . -0.492218069 22.35786742 . . PLPPR2 . . . phospholipid phosphatase related 2 . . . . . . . -0.358119787 29.16371786 . . PLPPR3 . . . phospholipid phosphatase related 3 . . . . . 0.25063 0.10322 -0.113792788 45.25831564 . . PLPPR4 . . . phospholipid phosphatase related 4 FUNCTION: Hydrolyzes lysophosphatidic acid (LPA). Facilitates axonal outgrowth during development and regenerative sprouting. In the outgrowing axons acts as an ecto-enzyme and attenuates phospholipid-induced axon collapse in neurons and facilitates outgrowth in the hippocampus. {ECO:0000269|PubMed:12730698}.; . TISSUE SPECIFICITY: Specifically expressed in neurons. {ECO:0000269|PubMed:12730698}.; . . . . -0.381986487 27.68931352 . . PLPPR5 . . . phospholipid phosphatase related 5 FUNCTION: Induces filopodia formation and promotes neurite growth in a CDC42-independent manner; impedes neurite growth inhibitory- mediated axonal retraction. {ECO:0000250|UniProtKB:Q8BJ52}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in brain, lung, kidney and colon. Isoform 2 is expressed in placenta, skeletal muscle and kidney. {ECO:0000269|PubMed:16010976}.; . . . . -0.383807564 27.41802312 . . PLRG1 0.998224783427136 0.00177521481759137 1.75527217613752e-09 pleiotropic regulator 1 FUNCTION: Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. {ECO:0000250, ECO:0000269|PubMed:11544257}.; . . ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; . 0.55468 0.15289 -0.291981272 33.20358575 28.74018 0.91926 PLS1 0.000310388416470486 0.99702159220127 0.00266801938225919 plastin 1 FUNCTION: Actin-bundling protein in the absence of calcium.; . TISSUE SPECIFICITY: In small intestine, colon, and kidney; relatively lower levels of expression are detected in the lung and stomach. {ECO:0000269|PubMed:8139549}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;salivary gland;intestine;pharynx;colon;parathyroid;blood;skin;skeletal muscle;retina;uterus;bile duct;pancreas;lung;cornea;bone;placenta;visual apparatus;pituitary gland;liver;kidney;brain;mammary gland;artery;aorta;stomach; testis - interstitial;superior cervical ganglion;fetal liver;subthalamic nucleus;trachea;pituitary;skin; 0.71025 0.16320 -0.398573136 26.92852088 444.4767 4.38601 PLS1-AS1 . . . PLS1 antisense RNA 1 . . . . . . . . . . . PLS3 0.987821982614245 0.0121770583195047 9.59066250281615e-07 plastin 3 FUNCTION: Actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. May play a role in the regulation of bone development.; DISEASE: Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal disorder characterized by decreased bone mass and deterioration of bone microarchitecture without alteration in the composition of bone. The result is fragile bones and an increased risk of fractures, even after minimal trauma. Osteoporosis is a chronic condition of multifactorial etiology and is usually clinically silent until a fracture occurs. {ECO:0000269|PubMed:24088043}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in a variety of organs, including muscle, brain, uterus and esophagus.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;prostate;endometrium;cochlea;gum;thyroid;iris;amniotic fluid;bladder;brain;gall bladder;amygdala;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;larynx;bone;testis;artery;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; . 0.97698 0.64888 -0.404032746 26.53338051 17.22072 0.60492 PLS3-AS1 . . . PLS3 antisense RNA 1 . . . . . . . . . . . PLSCR1 0.00293164530943767 0.941928844874749 0.0551395098158129 phospholipid scramblase 1 FUNCTION: May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system.; . TISSUE SPECIFICITY: Expressed in platelets, erythrocyte membranes, lymphocytes, spleen, thymus, prostate, testis, uterus, intestine, colon, heart, placenta, lung, liver, kidney and pancreas. Not detected in brain and skeletal muscle.; smooth muscle;ovary;salivary gland;intestine;colon;vein;skin;bone marrow;uterus;prostate;endometrium;oesophagus;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;alveolus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; . 0.20396 0.13592 0.393270925 76.04977589 348.51271 3.95681 PLSCR2 2.19480995516763e-05 0.487705637550566 0.512272414349883 phospholipid scramblase 2 FUNCTION: May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system.; . TISSUE SPECIFICITY: Expression of isoform 1 seems restricted to testis. {ECO:0000269|PubMed:10930526}.; lung;testis; testis - interstitial;superior cervical ganglion;testis;atrioventricular node;skeletal muscle; 0.14987 0.09621 0.61555716 83.13871196 150.06208 2.67126 PLSCR3 . . . phospholipid scramblase 3 FUNCTION: May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system. Seems to play a role in apoptosis, through translocation of cardiolipin from the inner to the outer mitochondrial membrane which promotes BID recruitment and enhances tBid-induced mitochondrial damages. {ECO:0000269|PubMed:17226776}.; . TISSUE SPECIFICITY: Expressed in heart, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, uterus, small intestine and peripheral blood lymphocytes. Not detected in testis, brain and liver.; lymphoreticular;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;bone;iris;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach;aorta;peripheral nerve;thymus; superior cervical ganglion;liver;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.40072 0.10827 . . . . PLSCR4 0.00169240896275056 0.892022589878029 0.106285001159221 phospholipid scramblase 4 FUNCTION: May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, kidney, pancreas, spleen, thymus, prostate, testis, uterus, small intestine and colon. Not detected in peripheral blood lymphocytes.; ovary;colon;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;cerebral cortex;endometrium;thyroid;pituitary gland;testis;brain;artery;bladder;gall bladder;unclassifiable (Anatomical System);hypothalamus;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.10244 0.09740 1.063778722 91.58410002 214.89583 3.16260 PLSCR5 1.16765638368877e-09 0.0264685192248521 0.973531479607492 phospholipid scramblase family member 5 . . . . . . . -0.293801652 32.93819297 193.23628 3.01385 PLSCR5-AS1 . . . PLSCR5 antisense RNA 1 . . . . . . . . . . . PLTP 0.000142042024392603 0.962665908642356 0.0371920493332514 phospholipid transfer protein FUNCTION: Facilitates the transfer of a spectrum of different lipid molecules, including diacylglycerol, phosphatidic acid, sphingomyelin, phosphatidylcholine, phosphatidylglycerol, cerebroside and phosphatidyl ethanolamine. Essential for the transfer of excess surface lipids from triglyceride-rich lipoproteins to HDL, thereby facilitating the formation of smaller lipoprotein remnants, contributing to the formation of LDL, and assisting in the maturation of HDL particles. PLTP also plays a key role in the uptake of cholesterol from peripheral cells and tissues that is subsequently transported to the liver for degradation and excretion. Two distinct forms of PLTP exist in plasma: an active form that can transfer PC from phospholipid vesicles to high-density lipoproteins (HDL), and an inactive form that lacks this capability.; . TISSUE SPECIFICITY: Wide tissue distribution. Placenta > pancreas > lung > kidney > heart > liver > skeletal muscle > brain.; myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;pancreas;lung;cornea;placenta;visual apparatus;alveolus;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;stomach;thymus; placenta;thymus; 0.36337 0.21599 -0.440847477 24.59896202 193.00501 3.01119 PLVAP 0.000801226857051978 0.929613882243065 0.0695848908998829 plasmalemma vesicle associated protein FUNCTION: Involved in the formation of stomatal and fenestral diaphragms of caveolae. May function in microvascular permeability. {ECO:0000269|PubMed:15155804}.; . TISSUE SPECIFICITY: Expressed in lung, kidney, heart, aorta, placenta, muscle, pituitary gland, adrenals, mammary gland, bladder, lymph node, bone marrow, trachea, digestive tract, liver and tumor-associated endothelium. {ECO:0000269|PubMed:11401446, ECO:0000269|PubMed:15971170}.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cerebral cortex;oesophagus;endometrium;larynx;bone;thyroid;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;thyroid;atrioventricular node;fetal thyroid; 0.13829 0.13045 -0.574945567 18.90186365 52.74155 1.43895 PLXDC1 0.000149406289070405 0.96505289280328 0.0347977009076492 plexin domain containing 1 FUNCTION: Plays a critical role in endothelial cell capillary morphogenesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in endothelial cells from colorectal cancer, and in endothelial cells from primary cancers of the lung, liver, pancreas, breast and brain. Not detectable in endothelial cells from normal tissue. Expressed in fibrovascular membrane with increased expression in individuals with proliferative diabetic retinopathy. {ECO:0000269|PubMed:10947988, ECO:0000269|PubMed:11559528, ECO:0000269|PubMed:17560052, ECO:0000269|PubMed:18316703}.; ovary;fovea centralis;choroid;skin;retina;uterus;optic nerve;thyroid;bone;pituitary gland;testis;pineal gland;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;head and neck;mammary gland;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.15764 0.12678 -0.021969881 52.14673272 691.27313 5.24466 PLXDC2 0.613047816780497 0.386937643693519 1.45395259832139e-05 plexin domain containing 2 FUNCTION: May play a role in tumor angiogenesis. {ECO:0000269|PubMed:11559528}.; . TISSUE SPECIFICITY: Expressed in the endothelial cells of the stroma but not in the endothelial cells of normal colonic tissue. {ECO:0000269|PubMed:11559528}.; . . 0.46149 0.10853 0.531004228 80.87992451 87.18855 1.99411 PLXNA1 0.999998424887592 1.57511240792151e-06 5.33960829928919e-19 plexin A1 FUNCTION: Coreceptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down- stream signaling events in the cytoplasm (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in fetal brain, lung, liver and kidney. {ECO:0000269|PubMed:8570614}.; smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;cerebellum; amygdala;dorsal root ganglion;whole brain;superior cervical ganglion;occipital lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.06749 0.17760 -4.392380749 0.08846426 184.48733 2.94857 PLXNA2 0.993981181863515 0.00601881813638796 9.71303342916005e-14 plexin A2 FUNCTION: Coreceptor for SEMA3A and SEMA6A. Necessary for signaling by SEMA6A and class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down- stream signaling events in the cytoplasm (By similarity). {ECO:0000250, ECO:0000269|PubMed:10520995}.; . TISSUE SPECIFICITY: Detected in fetal brain. {ECO:0000269|PubMed:8570614}.; . . 0.40081 0.15418 -1.483036981 3.64472753 5451.97785 15.21209 PLXNA3 0.983112793293949 0.0168872065590562 1.46994673261165e-10 plexin A3 FUNCTION: Coreceptor for SEMA3A and SEMA3F. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. Regulates the migration of sympathetic neurons, but not of neural crest precursors. Required for normal dendrite spine morphology in pyramidal neurons. May play a role in regulating semaphorin-mediated programmed cell death in the developing nervous system. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm.; . . . . 0.13437 0.14072 -2.494487417 0.937721161 2064.44297 8.37090 PLXNA4 0.9999997021004 2.97899599857824e-07 4.56798255394237e-20 plexin A4 FUNCTION: Coreceptor for SEMA3A. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm (By similarity). {ECO:0000250}.; . . frontal lobe;ovary;heart;cerebral cortex;testis;brain;skeletal muscle; . 0.16772 0.11298 -0.194946553 39.21325784 462.81286 4.45854 PLXNB1 0.85019510818446 0.149804891803025 1.25148406569713e-11 plexin B1 FUNCTION: Receptor for SEMA4D. Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. {ECO:0000269|PubMed:12196628, ECO:0000269|PubMed:12198496, ECO:0000269|PubMed:15210733, ECO:0000269|PubMed:19843518, ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:21912513}.; . TISSUE SPECIFICITY: Highly expressed in fetal kidney, and at slightly lower levels in fetal brain, lung and liver. {ECO:0000269|PubMed:8570614}.; myocardium;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; whole brain;amygdala;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;thyroid;prefrontal cortex;ciliary ganglion;kidney;cingulate cortex;parietal lobe;cerebellum; 0.15815 0.11899 -2.508520205 0.931823543 368.55714 4.05681 PLXNB2 0.992862470603308 0.00713752939654439 1.47366173040222e-13 plexin B2 FUNCTION: Cell surface receptor for SEMA4C, SEMA4D and SEMA4G that plays an important role in cell-cell signaling. Binding to class 4 semaphorins promotes downstream activation of RHOA and phosphorylation of ERBB2 at 'Tyr-1248'. Required for normal differentiation and migration of neuronal cells during brain corticogenesis and for normal embryonic brain development. Regulates the migration of cerebellar granule cells in the developing brain. Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. May modulate the activity of RAC1 and CDC42. Down-regulates macrophage migration in wound- healing assays (in vitro) (By similarity). {ECO:0000250, ECO:0000269|PubMed:12183458, ECO:0000269|PubMed:12533544, ECO:0000269|PubMed:15184888}.; . . lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;uterus;oesophagus;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; . 0.21876 0.12373 -3.297942414 0.418730833 992.83256 6.07108 PLXNB3 0.103343014352593 0.89665455256753 2.43307987695212e-06 plexin B3 FUNCTION: Receptor for SEMA5A that plays a role in axon guidance, invasive growth and cell migration. Stimulates neurite outgrowth and mediates Ca(2+)/Mg(2+)-dependent cell aggregation. In glioma cells, SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin stress fibers, disruption of focal adhesions and cellular collapse as well as inhibition of cell migration and invasion through ARHGDIA-mediated inactivation of RAC1. {ECO:0000269|PubMed:15218527, ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:21706053}.; . TISSUE SPECIFICITY: Expression detected in Purkinje and granular cells in cerebellum, and in brain neocortex but not in corpus callosum. Expressed in glioma cells and embryonic kidney cells (at protein level). Expressed in brain, liver, pancreas and placenta, with weak expression detected also in lung and kidney. Expressed in several glioma cell lines. {ECO:0000269|PubMed:16122393, ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:21706053}.; unclassifiable (Anatomical System);colon;fovea centralis;choroid;lens;retina;optic nerve;lung;frontal lobe;adrenal gland;bone;visual apparatus;macula lutea;testis;brain; . 0.18305 0.12743 -0.705742265 14.72045294 728.62676 5.35754 PLXNC1 0.999714839774068 0.000285160225897808 3.41457735092793e-14 plexin C1 FUNCTION: Receptor for SEMA7A, for smallpox semaphorin A39R, vaccinia virus semaphorin A39R and for herpesvirus Sema protein. Binding of semaphorins triggers cellular responses leading to the rearrangement of the cytoskeleton and to secretion of IL6 and IL8 (By similarity). {ECO:0000250, ECO:0000269|PubMed:20727575}.; . TISSUE SPECIFICITY: Detected in heart, brain, lung, spleen and placenta. {ECO:0000269|PubMed:9586637}.; unclassifiable (Anatomical System);medulla oblongata;heart;islets of Langerhans;hypothalamus;spinal cord;colon;skin;skeletal muscle;retina;bone marrow;uterus;whole body;lung;placenta;liver;testis;spleen;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;white blood cells;trigeminal ganglion;whole blood;skeletal muscle; 0.69608 0.10916 -0.325161626 30.92120783 2196.06093 8.62704 PLXND1 0.999989724505468 1.02754945324598e-05 5.14607321368707e-17 plexin D1 FUNCTION: Cell surface receptor for SEMA4A and for class 3 semaphorins, such as SEMA3A, SEMA3C and SEMA3E. Plays an important role in cell-cell signaling, and in regulating the migration of a wide spectrum of cell types. Regulates the migration of thymocytes in the medulla. Regulates endothelial cell migration. Plays an important role in ensuring the specificity of synapse formation. Required for normal development of the heart and vasculature (By similarity). Mediates anti-angiogenic signaling in response to SEMA3E. {ECO:0000250, ECO:0000269|PubMed:20385769}.; . TISSUE SPECIFICITY: Detected at low levels in heart, placenta, lung, skeletal muscle, kidney, thymus and liver. Detected at very low levels in brain, colon, spleen, small intestine and peripheral blood leukocytes. {ECO:0000269|PubMed:12412018}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;hypopharynx;alveolus;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; placenta; 0.15642 0.12590 -1.306585655 4.883227176 2739.76702 9.86834 PM20D1 1.26770298960659e-09 0.328828489265977 0.67117150946632 peptidase M20 domain containing 1 . . . . . 0.04303 0.06695 1.333822178 94.22033498 8308.67037 19.73261 PM20D2 0.00116674345055796 0.84152454110507 0.157308715444372 peptidase M20 domain containing 2 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.11411 0.10228 . . 210.24582 3.12916 PMAIP1 0.461950506283966 0.446730311449308 0.0913191822667261 phorbol-12-myristate-13-acetate-induced protein 1 FUNCTION: Promotes activation of caspases and apoptosis. Promotes mitochondrial membrane changes and efflux of apoptogenic proteins from the mitochondria. Contributes to p53/TP53-dependent apoptosis after radiation exposure. Promotes proteasomal degradation of MCL1. Competes with BAK1 for binding to MCL1 and can displace BAK1 from its binding site on MCL1 (By similarity). Competes with BIM/BCL2L11 for binding to MCL1 and can displace BIM/BCL2L11 from its binding site on MCL1. {ECO:0000250, ECO:0000269|PubMed:10807576, ECO:0000269|PubMed:15694340, ECO:0000269|PubMed:15705586, ECO:0000269|PubMed:17374615, ECO:0000269|PubMed:17389404}.; . TISSUE SPECIFICITY: Highly expressed in adult T-cell leukemia cell line.; smooth muscle;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;skeletal muscle;bile duct;breast;lung;placenta;visual apparatus;liver;alveolus;kidney;stomach; uterus corpus;tumor;white blood cells;trigeminal ganglion; 0.83339 . . . 424.86703 4.30567 PMCH 0.115285755884675 0.778562028910186 0.106152215205139 pro-melanin concentrating hormone FUNCTION: MCH may act as a neurotransmitter or neuromodulator in a broad array of neuronal functions directed toward the regulation of goal-directed behavior, such as food intake, and general arousal. May also have a role in spermatocyte differentiation.; . TISSUE SPECIFICITY: Predominantly expressed in lateral hypothalamus, also detected in pallidum, neocortex and cerebellum. Also found in thymus, brown adipose tissue, duodenum and testis (spermatogonia, early spermatocytes and Sertoli cells). No expression in peripheral blood. In brain exclusively mature MCH and NEI peptides are present. In peripheral tissues a large product, encompassing the NEI and MCH domains of the precursor, is found predominantly. {ECO:0000269|PubMed:9191099}.; unclassifiable (Anatomical System);heart;ovary;cartilage;hypothalamus;colon;skin;uterus;whole body;lung;adrenal gland;testis;germinal center;kidney;brain; superior cervical ganglion;hypothalamus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15338 . -0.075159878 47.78839349 6.88198 0.25587 PMCHL1 . . . pro-melanin concentrating hormone like 1 (pseudogene) . . TISSUE SPECIFICITY: Expressed in testis and brain. {ECO:0000269|PubMed:11070051, ECO:0000269|PubMed:9729295}.; . . 0.11790 . . . . . PMCHL2 . . . pro-melanin concentrating hormone like 2 (pseudogene) . . TISSUE SPECIFICITY: Expressed in testis but not in brain.; . . 0.31871 . . . . . PMEL 1.12363431292712e-07 0.783130649484692 0.216869238151877 premelanosome protein FUNCTION: Plays a central role in the biogenesis of melanosomes. Involved in the maturation of melanosomes from stage I to II. The transition from stage I melanosomes to stage II melanosomes involves an elongation of the vesicle, and the appearance within of distinct fibrillar structures. Release of the soluble form, ME20-S, could protect tumor cells from antibody mediated immunity. {ECO:0000269|PubMed:11694580, ECO:0000269|PubMed:21962903}.; . TISSUE SPECIFICITY: Preferentially expressed in melanomas. Some expression was found in dysplastic nevi. Not found in normal tissues nor in carcinomas. Normally expressed at low levels in quiescent adult melanocytes but overexpressed by proliferating neonatal melanocytes and during tumor growth.; ovary;salivary gland;intestine;colon;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;iris;bladder;brain;unclassifiable (Anatomical System);heart;pharynx;blood;lung;cornea;placenta;visual apparatus;liver;spleen;kidney;mammary gland; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.53002 0.31897 -0.040377332 50.50719509 571.82843 4.85212 PMEPA1 0.416594874357437 0.548128491662804 0.0352766339797592 prostate transmembrane protein, androgen induced 1 FUNCTION: Functions as a negative regulator of TGF-beta signaling and thereby probably plays a role in cell proliferation, differentiation, apoptosis, motility, extracellular matrix production and immunosuppression. In the canonical TGF-beta pathway, ZFYVE9/SARA recruits the intracellular signal transducer and transcriptional modulators SMAD2 and SMAD3 to the TGF-beta receptor. Phosphorylated by the receptor, SMAD2 and SMAD3 then form a heteromeric complex with SMAD4 that translocates to the nucleus to regulate transcription. Through interaction with SMAD2 and SMAD3, LDLRAD4 may compete with ZFYVE9 and SMAD4 and prevent propagation of the intracellular signal (PubMed:20129061, PubMed:24627487). Also involved in down-regulation of the androgen receptor (AR), enhancing ubiquitination and proteasome-mediated degradation of AR, probably by recruiting NEDD4 (PubMed:18703514). {ECO:0000269|PubMed:18703514, ECO:0000269|PubMed:20129061, ECO:0000269|PubMed:24627487}.; . TISSUE SPECIFICITY: Highest expression in prostate. Also expressed in ovary.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;spinal ganglion;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;oral cavity;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;prostate;ciliary ganglion;caudate nucleus; 0.22259 0.16670 0.17280645 65.75843359 506.91232 4.61956 PMF1 1.71367442696473e-05 0.437883633871675 0.562099229384056 polyamine-modulated factor 1 FUNCTION: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. May act as a cotranscription partner of NFE2L2 involved in regulation of polyamine-induced transcription of SSAT. {ECO:0000269|PubMed:10419538, ECO:0000269|PubMed:11256947, ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}.; . TISSUE SPECIFICITY: Highest levels of expression in heart and skeletal muscle, with significant levels expressed in kidney and liver. {ECO:0000269|PubMed:10419538}.; . . . 0.26210 0.883760026 89.07171503 92.05391 2.06391 PMF1-BGLAP 1.71367442696473e-05 0.437883633871675 0.562099229384056 PMF1-BGLAP readthrough FUNCTION: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. May act as a cotranscription partner of NFE2L2 involved in regulation of polyamine-induced transcription of SSAT. {ECO:0000269|PubMed:10419538, ECO:0000269|PubMed:11256947, ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}.; . TISSUE SPECIFICITY: Highest levels of expression in heart and skeletal muscle, with significant levels expressed in kidney and liver. {ECO:0000269|PubMed:10419538}.; . . . . 0.773521534 87.06062751 . . PMFBP1 4.06292657665862e-25 0.00101576080079476 0.998984239199205 polyamine modulated factor 1 binding protein 1 FUNCTION: May play a role in sperm morphology especially the sperm tail and consequently affect fertility. May also be involved in the general organization of cellular cytoskeleton. {ECO:0000269|PubMed:1770140}.; . . lung;testis; superior cervical ganglion;testis - interstitial;ciliary ganglion;trigeminal ganglion; 0.12957 . -0.655870776 16.12408587 7002.95481 17.83469 PML 0.937511028933986 0.0624866977302175 2.27333579642892e-06 promyelocytic leukemia FUNCTION: Functions via its association with PML-nuclear bodies (PML-NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Isoform PML-4 has a multifaceted role in the regulation of apoptosis and growth suppression: activates RB1 and inhibits AKT1 via interactions with PP1 and PP2A phosphatases respectively, negatively affects the PI3K pathway by inhibiting MTOR and activating PTEN, and positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Isoform PML-4 also: acts as a transcriptional repressor of TBX2 during cellular senescence and the repression is dependent on a functional RBL2/E2F4 repressor complex, regulates double-strand break repair in gamma- irradiation-induced DNA damage responses via its interaction with WRN, acts as a negative regulator of telomerase by interacting with TERT, and regulates PER2 nuclear localization and circadian function. Isoform PML-6 inhibits specifically the activity of the tetrameric form of PKM. The nuclear isoforms (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5) in concert with SATB1 are involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Isoform PML-2 is required for efficient IFN-gamma induced MHC II gene transcription via regulation of CIITA. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. PML also regulates transcription activity of ELF4 and can act as an important mediator for TNF-alpha- and IFN-alpha-mediated inhibition of endothelial cell network formation and migration.; DISEASE: Note=A chromosomal aberration involving PML may be a cause of acute promyelocytic leukemia (APL). Translocation t(15;17)(q21;q21) with RARA. The PML breakpoints (type A and type B) lie on either side of an alternatively spliced exon. {ECO:0000269|PubMed:1652369, ECO:0000269|PubMed:1720570}.; . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;amnion;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13603 0.57235 0.148734569 64.11889597 74.41273 1.80230 PMM1 0.000159924654790979 0.876475556848965 0.123364518496244 phosphomannomutase 1 FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain. {ECO:0000269|PubMed:16540464}.; . TISSUE SPECIFICITY: Strong expression in liver, heart, brain, and pancreas; lower expression in skeletal muscle.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;lens;bile duct;breast;lung;adrenal gland;nasopharynx;placenta;macula lutea;duodenum;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; amygdala;whole brain;thalamus;occipital lobe;subthalamic nucleus;hypothalamus;temporal lobe;prefrontal cortex;testis;globus pallidus;pons;cingulate cortex; 0.12855 0.23304 -0.404032746 26.53338051 44.86456 1.28521 PMM2 4.03082648601013e-10 0.0272382688417074 0.97276173075521 phosphomannomutase 2 FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. {ECO:0000250}.; DISEASE: Congenital disorder of glycosylation 1A (CDG1A) [MIM:212065]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. Congenital disorder of glycosylation type 1A is an autosomal recessive disorder characterized by a severe encephalopathy with axial hypotonia, abnormal eye movement, and pronounced psychomotor retardation, as well as peripheral neuropathy, cerebellar hypoplasia, and retinitis pigmentosa. Patients show a peculiar distribution of subcutaneous fat, nipple retraction, and hypogonadism. {ECO:0000269|PubMed:10066032, ECO:0000269|PubMed:10571956, ECO:0000269|PubMed:10602363, ECO:0000269|PubMed:10801058, ECO:0000269|PubMed:11058895, ECO:0000269|PubMed:11058896, ECO:0000269|PubMed:11350185, ECO:0000269|PubMed:12357336, ECO:0000269|PubMed:15844218, ECO:0000269|PubMed:17307006, ECO:0000269|PubMed:9140401, ECO:0000269|PubMed:9497260, ECO:0000269|PubMed:9781039}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;endometrium;synovium;larynx;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;placenta; 0.30521 0.36067 -0.556537043 19.72753008 146.87617 2.63975 PMM2P1 . . . phosphomannomutase 2 pseudogene 1 . . . . . . . . . . . PMM2P2 . . . phosphomannomutase 2 pseudogene 2 . . . . . . . . . . . PMP2 0.0339817010706723 0.823670091888165 0.142348207041162 peripheral myelin protein 2 FUNCTION: May play a role in lipid transport protein in Schwann cells. May bind cholesterol. {ECO:0000269|PubMed:20421974}.; . . unclassifiable (Anatomical System);amygdala;hypothalamus;sympathetic chain;fovea centralis;choroid;lens;skeletal muscle;skin;retina;optic nerve;whole body;cochlea;hippocampus;macula lutea;testis;brain; dorsal root ganglion;amygdala;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;olfactory bulb;hypothalamus;spinal cord;temporal lobe;atrioventricular node;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.14646 0.36445 0.547599505 81.2160887 145.44199 2.62672 PMP22 0.833150051663147 0.163467068502481 0.00338287983437137 peripheral myelin protein 22 FUNCTION: Might be involved in growth regulation, and in myelinization in the peripheral nervous system.; DISEASE: Charcot-Marie-Tooth disease 1A (CMT1A) [MIM:118220]: A dominant demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot- Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. {ECO:0000269|PubMed:10489052, ECO:0000269|PubMed:10737979, ECO:0000269|PubMed:11140841, ECO:0000269|PubMed:11835375, ECO:0000269|PubMed:12402337, ECO:0000269|PubMed:12497641, ECO:0000269|PubMed:1303281, ECO:0000269|PubMed:15205993, ECO:0000269|PubMed:8252046, ECO:0000269|PubMed:8510709, ECO:0000269|PubMed:8615087, ECO:0000269|PubMed:8655153, ECO:0000269|PubMed:8777804, ECO:0000269|PubMed:9040744}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dejerine-Sottas syndrome (DSS) [MIM:145900]: A severe degenerating neuropathy of the demyelinating Charcot-Marie-Tooth disease category, with onset by age 2 years. Characterized by motor and sensory neuropathy with very slow nerve conduction velocities, increased cerebrospinal fluid protein concentrations, hypertrophic nerve changes, delayed age of walking as well as areflexia. There are both autosomal dominant and autosomal recessive forms of Dejerine-Sottas syndrome. {ECO:0000269|PubMed:10211478, ECO:0000269|PubMed:10663978, ECO:0000269|PubMed:11438991, ECO:0000269|PubMed:12090401, ECO:0000269|PubMed:7675244, ECO:0000269|PubMed:7728152, ECO:0000269|PubMed:8252046, ECO:0000269|PubMed:8275092, ECO:0000269|PubMed:8995589, ECO:0000269|PubMed:9004143, ECO:0000269|PubMed:9055797, ECO:0000269|PubMed:9187667, ECO:0000269|PubMed:9452053, ECO:0000269|PubMed:9544841, ECO:0000269|PubMed:9585367, ECO:0000269|PubMed:9633821}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hereditary neuropathy with liability to pressure palsies (HNPP) [MIM:162500]: A neurologic disorder characterized by transient episodes of decreased perception or peripheral nerve palsies after slight traction, compression or minor traumas. {ECO:0000269|PubMed:12796555, ECO:0000269|PubMed:9748013}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease 1E (CMT1E) [MIM:118300]: An autosomal dominant form of Charcot-Marie-Tooth disease characterized by the association of sensorineural hearing loss with peripheral demyelinating neuropathy. {ECO:0000269|PubMed:10330345, ECO:0000269|PubMed:11835375, ECO:0000269|PubMed:12578939, ECO:0000269|PubMed:15099592}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Inflammatory demyelinating polyneuropathy (IDP) [MIM:139393]: Putative autoimmune disorder presenting in an acute (AIDP) or chronic form (CIDP). The acute form is also known as Guillain-Barre syndrome. {ECO:0000269|PubMed:12439896}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;cochlea;thyroid;iris;brain;heart;cartilage;tongue;adrenal cortex;lens;skeletal muscle;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;olfactory bulb;spinal cord;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.88492 0.41726 0.281220278 71.07808445 304.01033 3.71462 PMPCA 0.000186050485171578 0.994287672345526 0.00552627716930208 peptidase (mitochondrial processing) alpha FUNCTION: Cleaves presequences (transit peptides) from mitochondrial protein precursors. {ECO:0000250}.; . . . . 0.29624 0.10670 -1.175687564 5.974286388 64.34553 1.64544 PMPCAP1 . . . peptidase (mitochondrial processing) alpha pseudogene 1 . . . . . . . . . . . PMPCB 5.37977878966889e-06 0.965839532676668 0.034155087544542 peptidase (mitochondrial processing) beta FUNCTION: Cleaves presequences (transit peptides) from mitochondrial protein precursors. {ECO:0000250}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;cerebral cortex;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; uterus;amygdala;testis - interstitial;prefrontal cortex;tumor;testis;globus pallidus;white blood cells; 0.23715 0.10617 -0.420619508 25.72540694 649.88824 5.11439 PMS1 6.56457792406353e-14 0.108490835627294 0.89150916437264 PMS1 homolog 1, mismatch repair system component FUNCTION: Probably involved in the repair of mismatches in DNA. {ECO:0000269|PubMed:10748105}.; . . skin;retina;bone marrow;atrium;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;muscle;skeletal muscle;bile duct;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;cerebellum;thymus; superior cervical ganglion;medulla oblongata;testis - interstitial;testis - seminiferous tubule;temporal lobe;testis;globus pallidus;appendix;pons;atrioventricular node;trigeminal ganglion; 0.12287 0.09187 0.582377763 82.32484076 375.69909 4.08743 PMS2 1.13903542422692e-13 0.266962097134397 0.733037902865489 PMS1 homolog 2, mismatch repair system component FUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MLH1 to form MutL alpha. DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2- MSH6) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. {ECO:0000269|PubMed:16873062, ECO:0000269|PubMed:18206974, ECO:0000269|PubMed:23709753}.; DISEASE: Hereditary non-polyposis colorectal cancer 4 (HNPCC4) [MIM:614337]: An autosomal dominant disease associated with marked increase in cancer susceptibility. It is characterized by a familial predisposition to early-onset colorectal carcinoma (CRC) and extra-colonic tumors of the gastrointestinal, urological and female reproductive tracts. HNPCC is reported to be the most common form of inherited colorectal cancer in the Western world. Clinically, HNPCC is often divided into two subgroups. Type I is characterized by hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon. Type II is characterized by increased risk for cancers in certain tissues such as the uterus, ovary, breast, stomach, small intestine, skin, and larynx in addition to the colon. Diagnosis of classical HNPCC is based on the Amsterdam criteria: 3 or more relatives affected by colorectal cancer, one a first degree relative of the other two; 2 or more generation affected; 1 or more colorectal cancers presenting before 50 years of age; exclusion of hereditary polyposis syndromes. The term 'suspected HNPCC' or 'incomplete HNPCC' can be used to describe families who do not or only partially fulfill the Amsterdam criteria, but in whom a genetic basis for colon cancer is strongly suspected. {ECO:0000269|PubMed:15887124, ECO:0000269|PubMed:18178629, ECO:0000269|PubMed:23709753}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mismatch repair cancer syndrome (MMRCS) [MIM:276300]: An autosomal recessive, rare, childhood cancer predisposition syndrome encompassing a broad tumor spectrum. This includes hematological malignancies, central nervous system tumors, Lynch syndrome-associated malignancies such as colorectal tumors as well as multiple intestinal polyps, embryonic tumors and rhabdomyosarcoma. Multiple cafe-au-lait macules, a feature reminiscent of neurofibromatosis type 1, are often found as first manifestation of the underlying cancer. Areas of skin hypopigmentation have also been reported in MMRCS patients. {ECO:0000269|PubMed:15077197, ECO:0000269|PubMed:17557300, ECO:0000269|PubMed:7661930, ECO:0000269|PubMed:9419979}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;bone marrow;uterus;whole body;frontal lobe;endometrium;bone;thyroid;testis;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;kidney; . 0.77820 . 1.477080431 95.28780373 788.03656 5.54211 PMS2CL . . . PMS2 C-terminal like pseudogene . . . lymphoreticular;ovary;salivary gland;intestine;colon;skin;retina;prostate;frontal lobe;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;tongue;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; . 0.04300 0.05861 . . . . PMS2P1 . . . PMS1 homolog 2, mismatch repair system component pseudogene 1 . . TISSUE SPECIFICITY: Highly expressed in kidney, spleen, adrenal gland, ovary and cerebellum and to a lower extent in liver, esophagus, stomach, duodenum, colon, bladder, uterus, lung, pancreas and cerebrum. Not expressed in heart. {ECO:0000269|PubMed:10101297}.; . . . . . . . . PMS2P2 . . . PMS1 homolog 2, mismatch repair system component pseudogene 2 . . TISSUE SPECIFICITY: Highly expressed in kidney, spleen, adrenal gland, esophagus, duodenum, colon, bladder, ovary, cerebrum and cerebellum and to a lower extent in lung, liver, stomach, uterus and pancreas. Not expressed in heart. {ECO:0000269|PubMed:10101297}.; lung;frontal lobe;larynx;thyroid;placenta;testis;colon;parathyroid;cervix;head and neck;germinal center;brain;retina; . 0.07625 . . . . . PMS2P3 . . . PMS1 homolog 2, mismatch repair system component pseudogene 3 . . . unclassifiable (Anatomical System);lymph node;cartilage;tongue;colon;blood;skeletal muscle;bone marrow;uterus;lung;frontal lobe;placenta;visual apparatus;liver;hypopharynx;iris;testis;cervix;head and neck;germinal center;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.17911 . . . . . PMS2P4 . . . PMS1 homolog 2, mismatch repair system component pseudogene 4 . . . unclassifiable (Anatomical System);lung;heart;endometrium;testis;blood;germinal center;brain;stomach; . 0.06540 . . . . . PMS2P5 . . . PMS1 homolog 2, mismatch repair system component pseudogene 5 . . . medulla oblongata;ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;hypothalamus;skeletal muscle;breast;pancreas;lung;placenta;duodenum;liver;cervix;head and neck;kidney;stomach; . 0.02219 . . . . . PMS2P6 . . . PMS1 homolog 2, mismatch repair system component pseudogene 6 . . . . . . . . . . . PMS2P7 . . . PMS1 homolog 2, mismatch repair system component pseudogene 7 . . . . . . . . . . . PMS2P8 . . . PMS1 homolog 2, mismatch repair system component pseudogene 8 . . . . . . . . . . . PMS2P9 . . . PMS1 homolog 2, mismatch repair system component pseudogene 9 . . . . . . . . . . . PMS2P10 . . . PMS1 homolog 2, mismatch repair system component pseudogene 10 . . . unclassifiable (Anatomical System);colon;parathyroid;breast;lung;frontal lobe;larynx;placenta;thyroid;testis;head and neck;cervix;germinal center;brain; . . . . . . . PMS2P11 . . . PMS1 homolog 2, mismatch repair system component pseudogene 11 . . . . . . . . . . . PMS2P12 . . . PMS1 homolog 2, mismatch repair system component pseudogene 12 . . . . . . . . . . . PMVK 0.000305454915643329 0.574481042108404 0.425213502975953 phosphomevalonate kinase . DISEASE: Porokeratosis 1, multiple types (POROK1) [MIM:175800]: A form of porokeratosis, a disorder of faulty keratinization characterized by one or more atrophic patches surrounded by a distinctive hyperkeratotic ridgelike border called the cornoid lamella. The keratotic lesions can progress to overt cutaneous neoplasms, typically squamous cell carcinomas. Multiple clinical variants of porokeratosis are recognized, including porokeratosis of Mibelli, linear porokeratosis, disseminated superficial actinic porokeratosis, palmoplantar porokeratosis, and punctate porokeratosis. Different clinical presentations can be observed among members of the same family. Individuals expressing more than one variant have also been reported. {ECO:0000269|PubMed:26202976}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Heart, liver, skeletal muscle, kidney, and pancreas. Lower level in brain, placenta and lung. {ECO:0000269|PubMed:8663599}.; . . 0.13429 0.15898 0.593509966 82.51356452 281.80779 3.59562 PNCK 0.000479189687504524 0.874195491672904 0.125325318639591 pregnancy up-regulated nonubiquitous CaM kinase FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. In vitro phosphorylates CREB1 and SYN1/synapsin I. Phosphorylates and activates CAMK1 (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;prostate;lung;placenta;hippocampus;colon;kidney;brain; . 0.13631 0.11128 -0.494039303 22.09247464 30.66195 0.97560 PNISR 0.999085487307753 0.000914512621740111 7.05067232963529e-11 PNN-interacting serine/arginine-rich protein . . TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, thymus, spleen, kidney, liver, placenta and leukocytes. {ECO:0000269|PubMed:14578391}.; . . 0.95992 0.10958 0.068033485 59.0351498 139.81381 2.57901 PNKD 1.89916080841465e-08 0.130770233902539 0.869229747105853 paroxysmal nonkinesigenic dyskinesia FUNCTION: Probable hydrolase that plays an aggravative role in the development of cardiac hypertrophy via activation of the NF-kappa- B signaling pathway. {ECO:0000250}.; DISEASE: Dystonia 8 (DYT8) [MIM:118800]: A paroxysmal non- kinesigenic dystonia/dyskinesia. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. Dystonia type 8 is characterized by attacks of involuntary movements brought on by stress, alcohol, fatigue or caffeine. The attacks generally last between a few seconds and four hours or longer. The attacks may begin in one limb and spread throughout the body, including the face. {ECO:0000269|PubMed:15262732, ECO:0000269|PubMed:15824259, ECO:0000269|PubMed:16632198, ECO:0000269|PubMed:16717228, ECO:0000269|PubMed:16972263}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is only expressed in the brain. Isoform 2 is ubiquitously detected with highest expression in skeletal muscle and detected in myocardial myofibrils. Variant Val-7 and Val-9 are detected in the brain only. {ECO:0000269|PubMed:15188056, ECO:0000269|PubMed:15262732, ECO:0000269|PubMed:15496428}.; myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;lung;adrenal gland;placenta;hippocampus;macula lutea;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach; superior cervical ganglion;medulla oblongata;liver;globus pallidus;atrioventricular node; 0.51179 0.25823 -0.356299879 29.31115829 188.08639 2.97800 PNKDP1 . . . PNKD pseudogene 1 . . . . . . . . . . . PNKP 2.8844490761323e-07 0.750458365018527 0.249541346536566 polynucleotide kinase 3'-phosphatase FUNCTION: Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone. {ECO:0000269|PubMed:10446192}.; DISEASE: Microcephaly, seizures, and developmental delay (MCSZ) [MIM:613402]: A disease characterized by infantile-onset seizures, microcephaly, severe intellectual disability and delayed motor milestones with absent speech or only achieving a few words. Most patients also have behavioral problems with hyperactivity. Microcephaly is progressive and without neuronal migration or structural abnormalities, consistent with primary microcephaly. {ECO:0000269|PubMed:20118933}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ataxia-oculomotor apraxia 4 (AOA4) [MIM:616267]: An autosomal recessive disease characterized by cerebellar ataxia, oculomotor apraxia, areflexia and peripheral neuropathy. {ECO:0000269|PubMed:25728773}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in many tissues with highest expression in spleen and testis, and lowest expression in small intestine (PubMed:10446192). Expressed in higher amount in pancreas, heart and kidney and at lower levels in brain, lung and liver (PubMed:10446193). {ECO:0000269|PubMed:10446192, ECO:0000269|PubMed:10446193}.; lymphoreticular;medulla oblongata;ovary;colon;fovea centralis;choroid;bone marrow;uterus;prostate;endometrium;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);heart;tongue;hypothalamus;blood;pancreas;lung;placenta;macula lutea;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;heart; 0.34050 0.18160 -0.529034136 20.85987261 306.43839 3.72560 PNLDC1 2.5447781123909e-08 0.974206869416237 0.0257931051359817 PARN like, ribonuclease domain containing 1 . . . unclassifiable (Anatomical System);optic nerve;frontal lobe;tongue;islets of Langerhans;thyroid;placenta;head and neck; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.10720 . -0.997481928 8.47487615 56.73144 1.51508 PNLIP 0.00935447108842685 0.988275031150122 0.00237049776145135 pancreatic lipase . . . . . 0.11418 0.20090 -0.690637458 15.12149092 67.11451 1.69436 PNLIPP1 . . . pancreatic lipase pseudogene 1 . . . . . . . . . . . PNLIPRP1 6.28353313986005e-10 0.230026923602866 0.769973075768781 pancreatic lipase related protein 1 FUNCTION: May function as inhibitor of dietary triglyceride digestion. Lacks detectable lipase activity towards triglycerides, diglycerides, phosphatidylcholine, galactolipids or cholesterol esters (in vitro) (By similarity). {ECO:0000250, ECO:0000269|PubMed:19824014}.; . TISSUE SPECIFICITY: Pancreas. {ECO:0000269|PubMed:1379598}.; unclassifiable (Anatomical System);pancreas;islets of Langerhans;liver;spleen; dorsal root ganglion;superior cervical ganglion;pancreas;beta cell islets; 0.35499 0.12052 0.154398214 64.73814579 2480.12036 9.28465 PNLIPRP2 2.8556336614904e-05 0.778237802738904 0.221733640924481 pancreatic lipase related protein 2 (gene/pseudogene) FUNCTION: Lipase with broad substrate specificity. Can hydrolyze both phospholipids and galactolipids. Acts preferentially on monoglycerides, phospholipids and galactolipids. Contributes to milk fat hydrolysis. {ECO:0000269|PubMed:18702514, ECO:0000269|PubMed:19824014, ECO:0000269|PubMed:20083229}.; . TISSUE SPECIFICITY: Pancreas.; unclassifiable (Anatomical System);pancreas;islets of Langerhans;liver; . 0.08616 . . . . . PNLIPRP3 2.75274000877155e-09 0.277759316761505 0.722240680485755 pancreatic lipase related protein 3 . . TISSUE SPECIFICITY: Overexpressed in hepatocellular carcinoma. {ECO:0000269|PubMed:19640199}.; . . 0.04846 0.06540 1.308134829 94.01391838 2278.93844 8.83424 PNMA1 0.0593103724771047 0.867996045741142 0.0726935817817536 paraneoplastic Ma antigen 1 . . TISSUE SPECIFICITY: Testis- and brain-specific. In some cancer patients, specifically expressed by paraneoplastic tumor cells. {ECO:0000269|PubMed:10050892, ECO:0000269|PubMed:19366867}.; unclassifiable (Anatomical System);islets of Langerhans;colon;lens;retina;breast;uterus;bile duct;prostate;pancreas;whole body;lung;frontal lobe;larynx;bone;thyroid;visual apparatus;pituitary gland;liver;testis;cervix;head and neck;spleen;kidney;brain;stomach;cerebellum; . 0.44425 0.15283 0.038710339 56.92380278 107.66796 2.25297 PNMA2 0.101076994690922 0.865360552963635 0.0335624523454428 paraneoplastic Ma antigen 2 . . TISSUE SPECIFICITY: Brain-specific. In some cancer patients, specifically expressed by testicular tumor cells. {ECO:0000269|PubMed:10362822, ECO:0000269|PubMed:19366867}.; . . 0.06289 . -0.247889024 35.98726115 1256.33703 6.68489 PNMA3 0.00533780802091748 0.893346747500114 0.101315444478968 paraneoplastic Ma antigen 3 . . TISSUE SPECIFICITY: Expressed at high levels in the brain and testis. Expressed at lower levels in the heart, trachea and kidney. {ECO:0000269|PubMed:11558790, ECO:0000269|PubMed:16214224, ECO:0000269|PubMed:19366867}.; . . 0.19503 0.11749 0.41713504 76.95800896 15.88676 0.56377 PNMA5 0.00609707539882633 0.735922952110145 0.257979972491029 paraneoplastic Ma antigen family member 5 . . TISSUE SPECIFICITY: Expressed in the brain. {ECO:0000269|PubMed:19366867}.; thyroid;testis;head and neck; . 0.07335 . -0.025608647 51.91672564 17.29518 0.60722 PNMA6A . . . paraneoplastic Ma antigen family member 6A . . TISSUE SPECIFICITY: Expressed in the brain. {ECO:0000269|PubMed:19366867}.; . . 0.11242 . . . . . PNMA6B . . . paraneoplastic Ma antigen family member 6B (pseudogene) . . . . . 0.06739 . . . . . PNMAL1 0.0444369604042834 0.850771557372359 0.104791482223358 paraneoplastic Ma antigen family-like 1 . . . myocardium;ovary;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;spinal cord;urinary;muscle;skeletal muscle;lung;adrenal gland;placenta;macula lutea;alveolus;head and neck;kidney;cerebellum; dorsal root ganglion;whole brain;amygdala;occipital lobe;superior cervical ganglion;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;atrioventricular node;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.08193 0.09277 0.020302773 55.60863411 635.1646 5.07207 PNMAL2 . . . paraneoplastic Ma antigen family-like 2 . . . . . . . . . 3122.16834 10.62411 PNMT 0.000753820376516649 0.529125367058527 0.470120812564956 phenylethanolamine N-methyltransferase FUNCTION: Converts noradrenaline to adrenaline.; . . unclassifiable (Anatomical System);lung;adrenal gland;hypothalamus;thyroid;testis;choroid;brain;retina; adrenal gland;adrenal cortex;atrioventricular node;skeletal muscle; 0.44382 0.33284 0.062575634 58.74026893 41.86312 1.21944 PNN 0.163641787377565 0.836230136497912 0.000128076124522895 pinin, desmosome associated protein FUNCTION: Transcriptional activator binding to the E-box 1 core sequence of the E-cadherin promoter gene; the core-binding sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription repression. Auxiliary component of the splicing- dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Participates in the regulation of alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt upstream of the 5'-splice sites. Component of the PSAP complex which binds RNA in a sequence-independent manner and is proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. Involved in the establishment and maintenance of epithelia cell- cell adhesion. Potential tumor suppressor for renal cell carcinoma. {ECO:0000269|PubMed:12051732, ECO:0000269|PubMed:14517304, ECO:0000269|PubMed:15542832, ECO:0000269|PubMed:15735603, ECO:0000269|PubMed:22388736}.; . TISSUE SPECIFICITY: Expressed in placenta, lung, liver, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon, heart, epidermis, esophagus, brain and smooth and skeletal muscle. Expressed strongly in melanoma metastasis lesions and advanced primary tumors. {ECO:0000269|PubMed:10095061, ECO:0000269|PubMed:8922384, ECO:0000269|PubMed:9447706}.; lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;pia mater;cornea;nasopharynx;placenta;head and neck;kidney;stomach;thymus; testis - interstitial;tumor;white blood cells;trigeminal ganglion; 0.71163 0.25915 -0.066061882 48.77919321 995.57913 6.08097 PNO1 0.256534456542778 0.737496113226219 0.00596943023100336 partner of NOB1 homolog . . TISSUE SPECIFICITY: Expressed in liver, lung, spleen and kidney. Weakly expressed in thymus, testis and ovary. Weakly or not expressed in heart, brain, skeletal muscle, placenta, pancreas, prostate, small intestine, colon and peripheral blood leukocytes. {ECO:0000269|PubMed:15497447}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;tongue;atrioventricular node;pons;skeletal muscle;skin;subthalamic nucleus;testis - seminiferous tubule;appendix;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.88436 0.12382 0.260991686 70.25831564 310.23831 3.74660 PNOC 0.151495123138375 0.777114714421955 0.0713901624396704 prepronociceptin FUNCTION: Nociceptin: Ligand of the opioid receptor-like receptor OPRL1. It may act as a transmitter in the brain by modulating nociceptive and locomotor behavior. May be involved in neuronal differentiation and development. {ECO:0000250|UniProtKB:P55791}.; FUNCTION: Orphanin FQ2: Has potent analgesic activity. {ECO:0000250|UniProtKB:Q64387}.; . TISSUE SPECIFICITY: Predominantly expressed in the brain and spinal cord. Also expressed and secreted by peripheral blood neutrophils following degranulation. {ECO:0000269|PubMed:12950177}.; unclassifiable (Anatomical System);lung;cartilage;ovary;endometrium;tongue;placenta;testis;parathyroid;spleen;head and neck;germinal center;brain; superior cervical ganglion; 0.34991 0.17702 -0.295622497 32.61972163 226.51596 3.25230 PNP 0.0656268007332897 0.919727111603043 0.0146460876636677 purine nucleoside phosphorylase FUNCTION: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. {ECO:0000269|PubMed:2104852}.; . TISSUE SPECIFICITY: Expressed in red blood cells; overexpressed in red blood cells (cytoplasm) of patients with hereditary non- spherocytic hemolytic anemia of unknown etiology. {ECO:0000269|PubMed:22509282}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;thyroid;iris;testis;germinal center;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;urinary;blood;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;fetal liver;placenta;kidney;trigeminal ganglion;bone marrow; 0.42282 0.35175 0.593509966 82.51356452 1906.33719 8.03621 PNPLA1 0.000465200350864785 0.96580380970625 0.0337309899428853 patatin like phospholipase domain containing 1 FUNCTION: Lipid hydrolase. Important in the formation of the epidermal lipid barrier. Plays a role in glycerophospholipid metabolism. {ECO:0000269|PubMed:22246504}.; . TISSUE SPECIFICITY: Expressed in the digestive system. Expressed in the epidermis of skin keratinocytes. Strongly expressed in the granular layer. Expressed in the upper epidermis and eccrine sweat glands of the dermis and in the region of keratin filament bundles, which is more pronounced in upper epidermal layers and in the lower cornified layers. {ECO:0000269|PubMed:16799181, ECO:0000269|PubMed:22246504}.; . . 0.13177 . 1.269496963 93.63057325 2449.55631 9.20996 PNPLA2 0.0011411925640916 0.838081872593134 0.160776934842774 patatin like phospholipase domain containing 2 FUNCTION: Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets (PubMed:15550674). Also has acylglycerol transacylase activity. May act coordinately with LIPE/HLS within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes (PubMed:16239926). May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion. {ECO:0000269|PubMed:15364929, ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16239926}.; DISEASE: Note=Genetic variations in PNPLA2 may be associated with risk of diabetes mellitus type 2. {ECO:0000269|PubMed:16644682}.; DISEASE: Neutral lipid storage disease with myopathy (NLSDM) [MIM:610717]: Neutral lipid storage disorder (NLSD) with myopathy but without ichthyosis. NLSDs are characterized by the presence of triglyceride-containing cytoplasmic droplets in leukocytes and in other tissues, including bone marrow, skin, and muscle. Individuals with NLSDM did not show obesity, in spite of a defect in triglyceride degradation in fibroblasts and in marked triglyceride storage in liver, muscles, and other visceral cells. {ECO:0000269|PubMed:17187067}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest expression in adipose tissue. Also detected in heart, skeletal muscle, and portions of the gastrointestinal tract. Detected in normal retina and retinoblastoma cells. Detected in retinal pigment epithelium and, at lower intensity, in the inner segments of photoreceptors and in the ganglion cell layer of the neural retina (at protein level). {ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16249444, ECO:0000269|PubMed:17032652}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;duodenum;spleen;kidney;mammary gland;stomach;thymus; adipose tissue;testis;ciliary ganglion; 0.40021 0.21702 0.042348793 57.31304553 136.13585 2.53500 PNPLA3 0.000103859216104925 0.944270823348064 0.0556253174358311 patatin like phospholipase domain containing 3 FUNCTION: Multifunctional enzyme which has both triacylglycerol lipase and acylglycerol O-acyltransferase activities. {ECO:0000269|PubMed:15364929}.; DISEASE: Non-alcoholic fatty liver disease 1 (NAFLD1) [MIM:613282]: A condition characterized by accumulation of triglycerides in the liver. It is associated with adverse metabolic consequences, including insulin resistance and dyslipidemia. In a subset of individuals, hepatic steatosis promotes an inflammatory response in the liver, referred to as steatohepatitis, which can progress to cirrhosis and liver cancer. NAFLD is the most common form of liver disease in Western countries. {ECO:0000269|PubMed:18820647, ECO:0000269|PubMed:19224197, ECO:0000269|PubMed:19738004}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymphoreticular;islets of Langerhans;colon;fovea centralis;choroid;lens;skeletal muscle;skin;retina;optic nerve;macula lutea;liver;spleen;amniotic fluid;kidney;brain; . 0.13715 0.15992 0.846940207 88.47605567 2656.01989 9.68898 PNPLA4 0.0110685080808277 0.83839045375627 0.150541038162903 patatin like phospholipase domain containing 4 FUNCTION: Lipid hydrolase.; . TISSUE SPECIFICITY: Expressed in all tissues examined, including heart, brain, placenta, lung, liver, muscle, kidney, pancreas and spleen. {ECO:0000269|PubMed:7806223}.; . . 0.14625 0.10702 -0.427900189 25.14744043 25.2993 0.82749 PNPLA4P1 . . . patatin like phospholipase domain containing 4 pseudogene 1 . . . . . . . . . . . PNPLA5 9.38341355316044e-07 0.317699046668585 0.68230001499006 patatin like phospholipase domain containing 5 FUNCTION: Lipid hydrolase. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain and pituitary gland. {ECO:0000269|PubMed:16799181}.; unclassifiable (Anatomical System);blood;brain;skin; trigeminal ganglion; 0.17953 0.09445 0.576916344 82.25406936 1541.98025 7.28556 PNPLA6 1.58991551414988e-08 0.999981665607253 1.83184935918993e-05 patatin like phospholipase domain containing 6 FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. {ECO:0000269|PubMed:15044461, ECO:0000269|PubMed:1666291}.; DISEASE: Spastic paraplegia 39, autosomal recessive (SPG39) [MIM:612020]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG39 is associated with a motor axonopathy affecting upper and lower limbs and resulting in progressive wasting of distal upper and lower extremity muscles. {ECO:0000269|PubMed:18313024, ECO:0000269|PubMed:24355708}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Boucher-Neuhauser syndrome (BNHS) [MIM:215470]: An autosomal recessive disorder characterized by spinocerebellar ataxia, hypogonadotropic hypogonadism, and visual impairment due to chorioretinal dystrophy. The age at onset is variable, but most patients develop 1 or more symptoms in the first decade of life. Chorioretinal dystrophy may not always be present. {ECO:0000269|PubMed:24355708, ECO:0000269|PubMed:25033069}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Laurence-Moon syndrome (LNMS) [MIM:245800]: An autosomal recessive syndrome characterized by progressive spinocerebellar degeneration, spastic paraplegia, mental retardation, hypogonadism, dwarfism, and chorioretinopathy. Trichomegaly is absent. {ECO:0000269|PubMed:25480986}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Oliver-McFarlane syndrome (OMCS) [MIM:275400]: A rare autosomal recessive, congenital syndrome characterized by trichomegaly, severe chorioretinal atrophy and multiple pituitary hormone deficiencies. It results in intellectual impairment and dwarfism, if untreated. Clinical features include hypogonadotropic hypogonadism during puberty, pigmentary retinal degeneration, ataxia, spastic paraplegia, and peripheral neuropathy. {ECO:0000269|PubMed:25480986}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, placenta, kidney, neuron and skeletal muscle. Expressed in the developing eye, pituitary and brain. {ECO:0000269|PubMed:25480986, ECO:0000269|PubMed:9576844}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; prefrontal cortex;pons;parietal lobe; 0.10350 0.15862 -1.142761145 6.375324369 1325.61906 6.84406 PNPLA7 6.22823670158545e-27 0.00229814683804157 0.997701853161958 patatin like phospholipase domain containing 7 FUNCTION: Serine hydrolase, whose specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;retina;uterus;pancreas;prostate;lung;endometrium;bone;alveolus;testis;germinal center;kidney;brain;stomach;thymus; superior cervical ganglion;ciliary ganglion;caudate nucleus;trigeminal ganglion;skeletal muscle;skin;parietal lobe; 0.10273 0.09780 0.163315215 64.96815287 2633.02271 9.62537 PNPLA8 0.00813185680534786 0.991277288849844 0.000590854344808329 patatin like phospholipase domain containing 8 FUNCTION: Calcium-independent phospholipase A2, which catalyzes the hydrolysis of the sn-2 position of glycerophospholipids, PtdSer and to a lower extent PtdCho. Cleaves membrane phospholipids. {ECO:0000269|PubMed:10744668, ECO:0000269|PubMed:15695510}.; . TISSUE SPECIFICITY: Expressed in parenchymal tissues including heart, skeletal muscle, placenta, brain, liver and pancreas. Also expressed in bronchial epithelial cells and kidney. Highest expression is observed in skeletal muscle and heart. {ECO:0000269|PubMed:10744668, ECO:0000269|PubMed:10833412, ECO:0000269|PubMed:15629460, ECO:0000269|PubMed:15695510}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;endometrium;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;blood;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach;aorta; amygdala;prefrontal cortex;globus pallidus; 0.22103 0.10543 -0.418800956 25.79028073 79.80436 1.88754 PNPLA10P . . . patatin like phospholipase domain containing 10 pseudogene . . . . . . . . . . . PNPO 3.71896087830709e-05 0.600754755705319 0.399208054685898 pyridoxamine 5'-phosphate oxidase FUNCTION: Catalyzes the oxidation of either pyridoxine 5'- phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). {ECO:0000269|PubMed:12824491}.; DISEASE: Pyridoxine-5'-phosphate oxidase deficiency (PNPO deficiency) [MIM:610090]: The main feature of neonatal epileptic encephalopathy is the onset within hours of birth of a severe seizure disorder that does not respond to anticonvulsant drugs and can be fatal. Seizures can cease with the administration of PLP, being resistant to treatment with pyridoxine,. {ECO:0000269|PubMed:15772097}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.34035 0.23576 -0.117432389 44.89266336 255.03471 3.43499 PNPT1 0.90826684333985 0.0917331546041246 2.05602518664884e-09 polyribonucleotide nucleotidyltransferase 1 FUNCTION: RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double- stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Plays also a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA. {ECO:0000269|PubMed:12473748, ECO:0000269|PubMed:12721301, ECO:0000269|PubMed:12798676, ECO:0000269|PubMed:16055741, ECO:0000269|PubMed:16410805, ECO:0000269|PubMed:16934922, ECO:0000269|PubMed:18083836, ECO:0000269|PubMed:18083837, ECO:0000269|PubMed:18501193, ECO:0000269|PubMed:19509288, ECO:0000269|PubMed:20547861, ECO:0000269|PubMed:20691904}.; DISEASE: Combined oxidative phosphorylation deficiency 13 (COXPD13) [MIM:614932]: A mitochondrial disorder characterized by early onset severe encephalomyopathy, dystonia, choreoathetosis, bucofacial dyskinesias and combined mitochondrial respiratory chain deficiency. Nerve conductions velocities are decreased. Levels of plasma and cerebrospinal fluid lactate are increased. {ECO:0000269|PubMed:23084291}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal recessive, 70 (DFNB70) [MIM:614934]: A form of non-syndromic deafness characterized by severe, bilateral hearing impairment with prelingual onset, resulting in inability to acquire normal speech. {ECO:0000269|PubMed:23084290}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;uterus;prostate;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;placenta;visual apparatus;hippocampus;liver;duodenum;head and neck;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;medulla oblongata;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;parietal lobe;skeletal muscle; 0.23060 0.09520 0.135991087 63.61759849 3768.17005 12.01066 PNPT1P1 . . . polyribonucleotide nucleotidyltransferase 1 pseudogene 1 . . . . . . . . . . . PNPT1P2 . . . polyribonucleotide nucleotidyltransferase 1 pseudogene 2 . . . . . . . . . . . PNRC1 0.836159280405651 0.160616473547101 0.00322424604724802 proline rich nuclear receptor coactivator 1 FUNCTION: Nuclear receptor coactivator. May play a role in signal transduction. {ECO:0000269|PubMed:10894149}.; . TISSUE SPECIFICITY: Expressed in liver, lung, fat and NK/T cells. {ECO:0000269|PubMed:11574675}.; myocardium;medulla oblongata;smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;peripheral nerve;colon;fovea centralis;choroid;vein;uterus;whole body;atrium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; . 0.26405 0.15524 . . 119.16386 2.37555 PNRC2 . . . proline rich nuclear receptor coactivator 2 FUNCTION: Involved in nonsense-mediated mRNA decay (NMD) by acting as a bridge between the mRNA decapping complex and the NMD machinery. May act by targeting the NMD machinery to the P-body and recruiting the decapping machinery to aberrant mRNAs. Required for UPF1/RENT1 localization to the P-body. Also acts as a nuclear receptor coactivator. May play a role in controlling the energy balance between energy storage and energy expenditure. {ECO:0000269|PubMed:11574675, ECO:0000269|PubMed:19150429}.; . TISSUE SPECIFICITY: Expressed in heart, lung, muscle and brain. {ECO:0000269|PubMed:11574675}.; myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;bladder;gall bladder;amygdala;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;thymus; uterus corpus;trigeminal ganglion; 0.62114 0.11200 . . 3.31894 0.12137 PNRC2P1 . . . proline rich nuclear receptor coactivator 2 pseudogene 1 . . . . . . . . . . . POC1A 1.1532167339453e-05 0.815268037817113 0.184720430015547 POC1 centriolar protein A FUNCTION: Plays an important role in centriole assembly and/or stability and ciliogenesis. Involved in early steps of centriole duplication, as well as in the later steps of centriole length control. Acts in concert with POC1B to ensure centriole integrity and proper mitotic spindle formation. {ECO:0000269|PubMed:19109428, ECO:0000269|PubMed:23015594}.; DISEASE: Short stature, onychodysplasia, facial dysmorphism, and hypotrichosis (SOFT) [MIM:614813]: A syndrome characterized by severely short long bones, peculiar facies associated with paucity of hair, and nail anomalies. Growth retardation is evident on prenatal ultrasound as early as the second trimester of pregnancy, and affected individuals reach a final stature consistent with a height age of 6 years to 8 years. Relative macrocephaly is present during early childhood but head circumference is markedly low by adulthood. Psychomotor development is normal. Facial dysmorphism includes a long, triangular face with prominent nose and small ears, and affected individuals have an unusual high-pitched voice. Clinodactyly, brachydactyly, and hypoplastic distal phalanges and fingernails are present in association with postpubertal sparse and short hair. Typical skeletal findings include short and thick long bones with mild irregular metaphyseal changes, short femoral necks, and hypoplastic pelvis and sacrum. All long bones of the hand are short, with major delay of carpal ossification and cone- shaped epiphyses. Vertebral body ossification is also delayed. {ECO:0000269|PubMed:22840363, ECO:0000269|PubMed:22840364}. Note=The disease is caused by mutations affecting the gene represented in this entry. Cells derived from affected individuals have abnormal mitotic mechanics with multipolar spindles, in addition to clearly impaired ciliogenesis.; . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;optic nerve;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;trophoblast;heart;islets of Langerhans;muscle;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;mammary gland;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17644 0.10847 0.463046108 78.58575136 276.51537 3.55968 POC1B 5.89427992774507e-05 0.972655724053716 0.0272853331470062 POC1 centriolar protein B FUNCTION: Plays an important role in centriole assembly and/or stability and ciliogenesis (PubMed:20008567). Involved in early steps of centriole duplication, as well as in the later steps of centriole length control (PubMed:19109428). Acts in concert with POC1A to ensure centriole integrity and proper mitotic spindle formation. Required for primary cilia formation, ciliary length and also cell proliferation (PubMed:23015594). Required for retinal integrity (PubMed:25044745). {ECO:0000269|PubMed:19109428, ECO:0000269|PubMed:20008567, ECO:0000269|PubMed:23015594, ECO:0000269|PubMed:25044745}.; DISEASE: Cone-rod dystrophy 20 (CORD20) [MIM:615973]: A form of cone-rod dystrophy, an inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. {ECO:0000269|PubMed:24945461, ECO:0000269|PubMed:25018096, ECO:0000269|PubMed:25044745}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the retina. {ECO:0000269|PubMed:25044745}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;testis;brain;unclassifiable (Anatomical System);heart;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; testis - interstitial;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.17596 0.11319 -0.22584292 37.32012267 77.34053 1.84794 POC1B-GALNT4 0.0375964932909429 0.955172613925976 0.00723089278308099 POC1B-GALNT4 readthrough FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of SELPLG.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in mucous cells. {ECO:0000269|PubMed:9804815}.; . . . . 0.400544645 76.40953055 . . POC5 0.00213816175598754 0.978597030184052 0.0192648080599601 POC5 centriolar protein FUNCTION: Essential for the assembly of the distal half of centrioles, required for centriole elongation. {ECO:0000269|PubMed:19349582}.; . . unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;optic nerve;lung;frontal lobe;cochlea;endometrium;bone;macula lutea;hypopharynx;liver;testis;head and neck;spleen;kidney;brain;tonsil; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.04280 0.07405 0.621009802 83.41589998 1016.49099 6.13444 PODN 5.1967645599773e-07 0.853425189478631 0.146574290844913 podocan FUNCTION: Negatively regulates cell proliferation and cell migration. {ECO:0000269|PubMed:15063725}.; . TISSUE SPECIFICITY: Kidney, heart, liver, pancreas and vascular smooth muscle cells. Also detected in aortic intima (at protein level). {ECO:0000269|PubMed:12796502, ECO:0000269|PubMed:15063725, ECO:0000269|PubMed:20551380}.; smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;cerebral cortex;endometrium;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;greater omentum;breast;pancreas;placenta;visual apparatus;hypopharynx;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;adipose tissue;globus pallidus;appendix;trigeminal ganglion;cingulate cortex; 0.21830 0.10789 0.027580343 55.8091531 1753.94189 7.72811 PODNL1 2.50976901279169e-14 0.00125963667632452 0.99874036332365 podocan-like 1 . . . unclassifiable (Anatomical System);pancreas;lung;whole body;endometrium; occipital lobe;trigeminal ganglion;cingulate cortex; 0.11162 . . . 466.1971 4.47220 PODXL 0.251078485785218 0.747633645294978 0.0012878689198038 podocalyxin like FUNCTION: Involved in the regulation of both adhesion and cell morphology and cancer progression. Function as an anti-adhesive molecule that maintains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Acts as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell- cell contacts in an integrin-dependent manner. Induces the formation of apical actin-dependent microvilli. Involved in the formation of a preapical plasma membrane subdomain to set up inital epithelial polarization and the apical lumen formation during renal tubulogenesis. Plays a role in cancer development and aggressiveness by inducing cell migration and invasion through its interaction with the actin-binding protein EZR. Affects EZR- dependent signaling events, leading to increased activities of the MAPK and PI3K pathways in cancer cells. {ECO:0000269|PubMed:17616675, ECO:0000269|PubMed:18456258}.; . TISSUE SPECIFICITY: Glomerular epithelium cell (podocyte).; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;oesophagus;endometrium;larynx;bone;thyroid;pituitary gland;brain;unclassifiable (Anatomical System);heart;small intestine;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; superior cervical ganglion;kidney; 0.26340 0.09007 1.379742765 94.60368011 241.13538 3.35396 PODXL2 0.977986099041167 0.0219936051522606 2.02958065727509e-05 podocalyxin like 2 FUNCTION: Acts as a ligand for vascular selectins. Mediates rapid rolling of leukocytes over vascular surfaces through high affinity divalent cation-dependent interactions with E-, P- and L- selectins. {ECO:0000269|PubMed:18606703}.; . TISSUE SPECIFICITY: Expressed in T-cells, B-cells and monocytes. Expression is higher on memory and germinal center cells than on naive B-cells (at protein level). Highly expressed in brain. Moderately expressed in pancreas, kidney and lymphoid node. Weakly expressed in liver. Detected in both endothelial cells and CD34+ bone marrow cells. {ECO:0000269|PubMed:10722749, ECO:0000269|PubMed:18606703}.; unclassifiable (Anatomical System);medulla oblongata;ovary;islets of Langerhans;colon;fovea centralis;choroid;lens;skin;retina;pancreas;prostate;optic nerve;lung;frontal lobe;larynx;placenta;macula lutea;visual apparatus;duodenum;cervix;brain;stomach;peripheral nerve;thymus; amygdala;subthalamic nucleus;fetal brain;hypothalamus;prefrontal cortex;globus pallidus;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.10089 0.08403 0.064394823 58.84642604 181.93063 2.92978 POF1B 0.000181225035292492 0.972919213687286 0.026899561277422 premature ovarian failure, 1B FUNCTION: Plays a key role in the organization of epithelial monolayers by regulating the actin cytoskeleton. May be involved in ovary development. {ECO:0000269|PubMed:16773570, ECO:0000269|PubMed:21940798}.; DISEASE: Premature ovarian failure 2B (POF2B) [MIM:300604]: An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol. {ECO:0000269|PubMed:16773570}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . bile duct;unclassifiable (Anatomical System);lung;gum;muscle;liver;colon;spleen;bladder;skeletal muscle;stomach; superior cervical ganglion;tongue;trigeminal ganglion;skin;skeletal muscle; 0.14231 0.41445 0.92967242 89.79122435 227.93995 3.26029 POFUT1 0.987586067238811 0.0124089683962887 4.96436490023218e-06 protein O-fucosyltransferase 1 FUNCTION: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DLL1 or JAGGED1. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs). {ECO:0000269|PubMed:11524432, ECO:0000269|PubMed:8358148}.; DISEASE: Dowling-Degos disease 2 (DDD2) [MIM:615327]: An autosomal dominant genodermatosis. Affected individuals develop a postpubertal reticulate hyperpigmentation that is progressive and disfiguring, and small hyperkeratotic dark brown papules that affect mainly the flexures and great skin folds. Patients usually show no abnormalities of the hair or nails. {ECO:0000269|PubMed:23684010}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:11524432}.; . . 0.71785 0.13159 -0.091746757 46.91554612 211.56956 3.13647 POFUT2 0.0108408721953063 0.979874592272795 0.00928453553189821 protein O-fucosyltransferase 2 FUNCTION: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X(2,3)-S/T-C2-X(2)-G of thrombospondin type 1 repeats where C1 and C2 are the first and second cysteines, respectively. O-fucosylates members of several protein families including the ADAMTS family, the thrombosporin (TSP) and spondin families. The O-fucosylation of TSRs is also required for restricting epithelial to mesenchymal transition (EMT), maintaining the correct patterning of mesoderm and localization of the definite endoderm (By similarity). Required for the proper secretion of ADAMTS family members such as ADAMSL1 and ADAMST13. {ECO:0000250, ECO:0000269|PubMed:11067851, ECO:0000269|PubMed:16464858, ECO:0000269|PubMed:17395588, ECO:0000269|PubMed:17395589, ECO:0000269|PubMed:22588082}.; . TISSUE SPECIFICITY: Isoform A is expressed in fetal liver and peripheral blood lymphocytes. Isoform B is expressed in spleen, lung, testis, bone marrow, thymus, pancreas, prostate, fetal brain, fetal liver and fetal kidney. Isoform C is expressed in brain, heart, spleen, liver, lung, stomach, testis, placenta, skin, thymus, pancreas, mammary gland, prostate, fetal brain, fetal liver and fetal heart. {ECO:0000269|PubMed:15233996}.; myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;hypothalamus;blood;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;alveolus;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.15762 0.15072 -0.110153916 45.48832272 206.7967 3.10821 POGK 0.917279174747958 0.082697883133037 2.29421190051082e-05 pogo transposable element with KRAB domain . . . . . 0.18371 0.10748 0.707379532 85.62750649 48.82744 1.36292 POGLUT1 0.000114466389873238 0.988930599337464 0.010954934272663 protein O-glucosyltransferase 1 FUNCTION: Dual specificity glycosyltransferase. Catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to EGF repeats, such as those found in F7, F9 and NOTCH2, on the consensus sequence C-X-S-X-P-C. Positively regulates Notch signaling without affecting Notch ligand binding. {ECO:0000269|PubMed:21081508, ECO:0000269|PubMed:21490058, ECO:0000269|PubMed:21949356}.; . TISSUE SPECIFICITY: Expressed in most adult tissues at different intensities. Abundantly expressed in liver. Expressed also in brain, heart, skeletal muscle, spleen, kidney, placenta, lung and peripheral blood leukocyte. Not detectable in colon, thymus and small intestine. Expressed in the epidermis, especially in the upper parts, stratum spinosum and stratum granulosum (at protein level). {ECO:0000269|PubMed:16524674, ECO:0000269|PubMed:24387993}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;larynx;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;blood;lens;skeletal muscle;bile duct;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;temporal lobe;white blood cells;skeletal muscle; 0.12827 0.10695 0.038710339 56.92380278 59.17806 1.56001 POGZ 0.999999128125461 8.71874539445422e-07 1.52606829415895e-17 pogo transposable element with ZNF domain FUNCTION: Plays a role in mitotic cell cycle progression and is involved in kinetochore assembly and mitotic sister chromatid cohesion. Probably through its association with CBX5 plays a role in mitotic chromosome segregation by regulating aurora kinase B/AURKB activation and AURKB and CBX5 dissociation from chromosome arms. {ECO:0000269|PubMed:20562864}.; DISEASE: Note=Defects in POGZ may be associated with neuropsychiatric disorders such as autism spectrum disorders (ASD), bipolar affective disorders and early dementia onset. ASD are characterized by impairments in reciprocal social interaction and communication as well as restricted and stereotyped patterns of interest and activities. ASD include forms with moderate to severe cognitive impairment and milder forms with higher cognitive ability (Asperger syndrome). {ECO:0000269|PubMed:25694107}.; DISEASE: Mental retardation, autosomal dominant 37 (MRD37) [MIM:616364]: A form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:25533962}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;thymus;cerebellum; thalamus;occipital lobe;medulla oblongata;olfactory bulb;cerebellum peduncles;spinal cord;caudate nucleus;fetal brain;testis - seminiferous tubule;prefrontal cortex;testis;trigeminal ganglion;pituitary;cingulate cortex;parietal lobe;cerebellum; 0.23887 0.10792 -1.52667341 3.408822836 225.33539 3.24573 POLA1 0.999999524777767 4.75222233227771e-07 1.71989550975195e-17 polymerase (DNA) alpha 1, catalytic subunit FUNCTION: Plays an essential role in the initiation of DNA replication. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1/p180, a regulatory subunit POLA2/p70 and two primase subunits PRIM1/p49 and PRIM2/p58) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes. {ECO:0000269|PubMed:9518481}.; . . . . 0.99571 0.30271 -0.795417163 12.5324369 61.5917 1.59962 POLA2 0.000215959060480748 0.999598988532352 0.000185052407167741 polymerase (DNA) alpha 2, accessory subunit FUNCTION: May play an essential role at the early stage of chromosomal DNA replication by coupling the polymerase alpha/primase complex to the cellular replication machinery. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; globus pallidus; 0.51750 0.26908 -0.777005578 12.9747582 995.15873 6.07917 POLB 0.000157163663858776 0.967300602466269 0.032542233869872 polymerase (DNA) beta FUNCTION: Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. {ECO:0000269|PubMed:11805079, ECO:0000269|PubMed:21362556, ECO:0000269|PubMed:9207062, ECO:0000269|PubMed:9572863}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;cerebellum peduncles;testis;skeletal muscle;cerebellum; 0.29471 0.31265 -0.073340031 48.11866006 68.83369 1.71904 POLD1 0.00180701093302935 0.998149838325852 4.31507411190911e-05 polymerase (DNA) delta 1, catalytic subunit FUNCTION: Possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction. Required with its accessory proteins (proliferating cell nuclear antigen (PCNA) and replication factor C (RFC) or activator 1) for leading strand synthesis. Also involved in completing Okazaki fragments initiated by the DNA polymerase alpha/primase complex.; DISEASE: Colorectal cancer 10 (CRCS10) [MIM:612591]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:23263490, ECO:0000269|PubMed:24501277}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Mandibular hypoplasia, deafness, progeroid features, and lipodystrophy syndrome (MDPL) [MIM:615381]: An autosomal dominant systemic disorder characterized by prominent loss of subcutaneous fat, metabolic abnormalities including insulin resistance and diabetes mellitus, sclerodermatous skin, and a facial appearance characterized by mandibular hypoplasia. Sensorineural deafness occurs late in the first or second decades of life. {ECO:0000269|PubMed:23770608}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed across a panel of tissues, with high levels of expression in heart and lung. {ECO:0000269|PubMed:23770608}.; . . 0.96379 0.45610 -0.828637633 11.54163718 551.71434 4.77810 POLD2 0.0443243929840342 0.950041327501568 0.00563427951439766 polymerase (DNA) delta 2, accessory subunit FUNCTION: The function of the small subunit is not yet clear.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;liver;tumor;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.33576 0.22449 -0.912929826 9.902099552 20.23202 0.69259 POLD2P1 . . . polymerase (DNA) delta 2, accessory subunit pseudogene 1 . . . . . . . . . . . POLD3 0.99139424670152 0.00860567041479412 8.28836862211709e-08 polymerase (DNA) delta 3, accessory subunit FUNCTION: Required for optimal DNA polymerase delta activity. {ECO:0000269|PubMed:10219083, ECO:0000269|PubMed:10852724, ECO:0000269|PubMed:16510448}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;vein;skin;bone marrow;uterus;prostate;whole body;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;cerebellum cortex;spinal cord;pharynx;blood;breast;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach;peripheral nerve; testis;atrioventricular node;trigeminal ganglion; 0.60979 0.21476 0.575097644 82.1656051 193.7509 3.02008 POLD4 0.745036468604439 0.24438570373472 0.0105778276608417 polymerase (DNA) delta 4, accessory subunit FUNCTION: Required for optimal DNA polymerase delta activity. May contribute to PCNA-dependent activity of DNA polymerase delta. {ECO:0000269|PubMed:16510448}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;dura mater;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);meninges;trophoblast;lymph node;cartilage;heart;small intestine;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;pia mater;lung;cornea;placenta;visual apparatus;alveolus;liver;cervix;spleen;kidney;mammary gland;stomach; white blood cells; 0.27096 0.08980 0.191216164 66.57230479 10.91365 0.39492 POLDIP2 0.0492454565267766 0.945961244559532 0.00479329891369184 polymerase (DNA) delta interacting protein 2 . . . myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;colon;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;cerebellum; . 0.18686 0.12361 . . 56.57898 1.51257 POLDIP3 0.832319946565907 0.167650205625638 2.98478084551022e-05 polymerase (DNA) delta interacting protein 3 FUNCTION: Is involved in regulation of translation. Is preferentially associated with CBC-bound spliced mRNA-protein complexes during the pioneer round of mRNA translation. Contributes to enhanced translational efficiency of spliced over nonspliced mRNAs. Recruits activated ribosomal protein S6 kinase beta-1 I/RPS6KB1 to newly synthesized mRNA. Involved in nuclear mRNA export; probably mediated by assoociation with the TREX complex. {ECO:0000269|PubMed:18423201, ECO:0000269|PubMed:22928037}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;medulla oblongata;appendix;atrioventricular node;pons;cingulate cortex; 0.12164 . 0.264628794 70.5178108 852.50931 5.70421 POLE 1.00660603240353e-14 0.999999976747601 2.32523887287532e-08 polymerase (DNA) epsilon, catalytic subunit FUNCTION: Participates in DNA repair and in chromosomal DNA replication.; DISEASE: Colorectal cancer 12 (CRCS12) [MIM:615083]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. CRCS12 is characterized by a high-penetrance predisposition to the development of colorectal adenomas and carcinomas, with a variable tendency to develop multiple and large tumors. Onset is usually before age 40 years. The histologic features of the tumors are unremarkable. {ECO:0000269|PubMed:23263490, ECO:0000269|PubMed:24501277}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Facial dysmorphism, immunodeficiency, livedo, and short stature (FILS) [MIM:615139]: A syndrome characterized by mild facial dysmorphism, mainly malar hypoplasia, livedo on the skin since birth, and immunodeficiency resulting in recurrent infections. Growth impairment is observed during early childhood and results in variable short stature in adulthood. {ECO:0000269|PubMed:23230001}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;smooth muscle;ovary;developmental;colon;parathyroid;choroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;tongue;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;pons;trigeminal ganglion; 0.60007 . -0.805223789 12.09011559 2352.98038 8.98803 POLE2 0.000153355971239164 0.998356071956697 0.00149057207206426 polymerase (DNA) epsilon 2, accessory subunit FUNCTION: Participates in DNA repair and in chromosomal DNA replication.; . . unclassifiable (Anatomical System);lymph node;islets of Langerhans;colon;uterus;breast;prostate;whole body;liver;spleen;germinal center;kidney;brain;pineal gland;stomach; superior cervical ganglion;trigeminal ganglion; 0.96205 0.08955 0.15257911 64.60839821 232.72069 3.29856 POLE3 0.0777453985625654 0.751043147179803 0.171211454257632 polymerase (DNA) epsilon 3, accessory subunit FUNCTION: Forms a complex with DNA polymerase epsilon subunit CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1.; . TISSUE SPECIFICITY: Expressed in all tissues tested, including, heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; . . 0.34686 0.24974 -0.119252484 44.53880632 8.01565 0.29467 POLE4 0.000410965033929284 0.406956056924078 0.592632978041993 polymerase (DNA) epsilon 4, accessory subunit FUNCTION: May play a role in allowing polymerase epsilon to carry out its replication and/or repair function.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;larynx;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland; . 0.36019 0.10012 -0.009020804 52.8544468 2526.55661 9.37793 POLG 4.12449812767026e-05 0.999955410000115 3.34501860828531e-06 polymerase (DNA) gamma, catalytic subunit FUNCTION: Involved in the replication of mitochondrial DNA. Associates with mitochondrial DNA.; DISEASE: Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal dominant, 1 (PEOA1) [MIM:157640]: A disorder characterized by progressive weakness of ocular muscles and levator muscle of the upper eyelid. In a minority of cases, it is associated with skeletal myopathy, which predominantly involves axial or proximal muscles and which causes abnormal fatigability and even permanent muscle weakness. Ragged-red fibers and atrophy are found on muscle biopsy. A large proportion of chronic ophthalmoplegias are associated with other symptoms, leading to a multisystemic pattern of this disease. Additional symptoms are variable, and may include cataracts, hearing loss, sensory axonal neuropathy, ataxia, depression, hypogonadism, and parkinsonism. {ECO:0000269|PubMed:12210792, ECO:0000269|PubMed:15351195, ECO:0000269|PubMed:15534189, ECO:0000269|PubMed:17420318, ECO:0000269|PubMed:18575922}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal recessive, 1 (PEOB1) [MIM:258450]: A severe form of progressive external ophthalmoplegia, a disorder characterized by progressive weakness of ocular muscles and levator muscle of the upper eyelid. It is clinically more heterogeneous than the autosomal dominant forms. {ECO:0000269|PubMed:11431686, ECO:0000269|PubMed:12565911, ECO:0000269|PubMed:12707443, ECO:0000269|PubMed:12872260, ECO:0000269|PubMed:12975295, ECO:0000269|PubMed:14635118, ECO:0000269|PubMed:15349879, ECO:0000269|PubMed:15351195, ECO:0000269|PubMed:15477547, ECO:0000269|PubMed:15917273, ECO:0000269|PubMed:16401742, ECO:0000269|PubMed:16621917, ECO:0000269|PubMed:16634032, ECO:0000269|PubMed:16639411}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Sensory ataxic neuropathy dysarthria and ophthalmoparesis (SANDO) [MIM:607459]: A systemic disorder resulting from mitochondrial dysfunction associated with mitochondrial depletion in skeletal muscle and peripheral nerve tissue. The clinical triad of symptoms consists of sensory ataxic neuropathy, dysarthria, and ophthalmoparesis. However, the phenotype varies widely, even within the same family, and can also include myopathy, seizures, and hearing loss. An atypical form of the disease is characterized by headaches and/or seizures manifesting in childhood or adolescence, followed by development of cerebellar and sensory ataxia, dysarthria, progressive external ophthalmoplegia, and myoclonus in early adulthood. {ECO:0000269|PubMed:12565911, ECO:0000269|PubMed:14745080, ECO:0000269|PubMed:15477547, ECO:0000269|PubMed:15824347, ECO:0000269|PubMed:15917273, ECO:0000269|PubMed:16080118, ECO:0000269|PubMed:16621917, ECO:0000269|PubMed:16639411, ECO:0000269|PubMed:16919951}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial DNA depletion syndrome 4A (MTDPS4A) [MIM:203700]: An autosomal recessive hepatocerebral syndrome due to mitochondrial dysfunction. The typical course of the disease includes severe developmental delay, intractable seizures, liver failure, and death in childhood. Refractory seizures, cortical blindness, progressive liver dysfunction, and acute liver failure after exposure to valproic acid are considered diagnostic features. The neuropathological hallmarks are neuronal loss, spongiform degeneration, and astrocytosis of the visual cortex. Liver biopsy results show steatosis, often progressing to cirrhosis. {ECO:0000269|PubMed:15122711, ECO:0000269|PubMed:15689359, ECO:0000269|PubMed:15929042, ECO:0000269|PubMed:16621917, ECO:0000269|PubMed:16639411, ECO:0000269|PubMed:18828154}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial DNA depletion syndrome 4B (MTDPS4B) [MIM:613662]: An autosomal recessive progressive multisystem disorder due to mitochondrial dysfunction. It is clinically characterized by chronic gastrointestinal dysmotility and pseudo- obstruction, cachexia, progressive external ophthalmoplegia, axonal sensory ataxic neuropathy, and muscle weakness. {ECO:0000269|PubMed:12825077, ECO:0000269|PubMed:19307547}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. {ECO:0000269|PubMed:18828154}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;iris;germinal center;bladder;brain;tonsil;heart;cartilage;spinal cord;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;pancreas;lung;placenta;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;liver;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.23758 0.34185 -0.031281682 50.5779665 540.1607 4.73561 POLG2 2.159642523574e-06 0.89484373281182 0.105154107545656 polymerase (DNA) gamma 2, accessory subunit FUNCTION: Mitochondrial polymerase processivity subunit. Stimulates the polymerase and exonuclease activities, and increases the processivity of the enzyme. Binds to ss-DNA.; DISEASE: Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal dominant, 4 (PEOA4) [MIM:610131]: A disorder characterized by progressive weakness of ocular muscles and levator muscle of the upper eyelid. In a minority of cases, it is associated with skeletal myopathy, which predominantly involves axial or proximal muscles and which causes abnormal fatigability and even permanent muscle weakness. Ragged-red fibers and atrophy are found on muscle biopsy. A large proportion of chronic ophthalmoplegias are associated with other symptoms, leading to a multisystemic pattern of this disease. Additional symptoms are variable, and may include cataracts, hearing loss, sensory axonal neuropathy, ataxia, depression, hypogonadism, and parkinsonism. {ECO:0000269|PubMed:16685652}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.24797 0.12363 0.086440867 60.47416844 2981.32808 10.35811 POLH 0.00359087143137192 0.994483373411589 0.001925755157039 polymerase (DNA) eta FUNCTION: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Targets POLI to replication foci. {ECO:0000269|PubMed:10385124, ECO:0000269|PubMed:11376341, ECO:0000269|PubMed:11743006, ECO:0000269|PubMed:14630940, ECO:0000269|PubMed:14734526}.; DISEASE: Xeroderma pigmentosum variant type (XPV) [MIM:278750]: An autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. XPV shows normal nucleotide excision repair, but an exaggerated delay in recovery of replicative DNA synthesis. Most patients with the variant type of xeroderma pigmentosum do not develop clinical symptoms and skin neoplasias until a later age. Clinical manifestations are limited to photo-induced deterioration of the skin and eyes. {ECO:0000269|PubMed:10385124, ECO:0000269|PubMed:10398605, ECO:0000269|PubMed:11032022, ECO:0000269|PubMed:11121129, ECO:0000269|PubMed:11773631, ECO:0000269|PubMed:24130121}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.10607 0.16289 0.666922772 84.64260439 1309.71 6.80984 POLHP1 . . . polymerase (DNA) eta pseudogene 1 . . . . . . . . . . . POLI 4.26967456461878e-09 0.195191700431888 0.804808295298438 polymerase (DNA) iota FUNCTION: Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunogobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity. {ECO:0000269|PubMed:11013228, ECO:0000269|PubMed:11251121, ECO:0000269|PubMed:11387224, ECO:0000269|PubMed:12410315, ECO:0000269|PubMed:14630940, ECO:0000269|PubMed:15199127, ECO:0000269|PubMed:15254543}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in testis. {ECO:0000269|PubMed:10458907, ECO:0000269|PubMed:11387224}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;duodenum;kidney;stomach;thymus; testis - interstitial;testis - seminiferous tubule;testis; 0.13601 0.19952 0.202129237 67.42745931 300.18735 3.69482 POLK 5.99896012883471e-07 0.99293787489156 0.00706152521242663 polymerase (DNA) kappa FUNCTION: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. {ECO:0000269|PubMed:10620008, ECO:0000269|PubMed:11024016, ECO:0000269|PubMed:12145297, ECO:0000269|PubMed:12444249, ECO:0000269|PubMed:12952891, ECO:0000269|PubMed:14630940, ECO:0000269|PubMed:15533436}.; . TISSUE SPECIFICITY: Detected at low levels in testis, spleen, prostate and ovary. Detected at very low levels in kidney, colon, brain, heart, liver, lung, placenta, pancreas and peripheral blood leukocytes. {ECO:0000269|PubMed:10518552, ECO:0000269|PubMed:10620008}.; ovary;developmental;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);amygdala;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;breast;lung;adrenal gland;liver;spleen;kidney;mammary gland; skin; 0.13919 0.08642 -0.574945567 18.90186365 155.6478 2.72624 POLL 2.24671352271532e-11 0.12627556091423 0.873724439063303 polymerase (DNA) lambda FUNCTION: Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity. {ECO:0000269|PubMed:11457865, ECO:0000269|PubMed:15537631}.; . TISSUE SPECIFICITY: Expressed in a number of tissues. Abundant in testis.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;prostate;optic nerve;endometrium;larynx;thyroid;bone;testis;amniotic fluid;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;heart;lens;skeletal muscle;breast;pia mater;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;atrioventricular node;parietal lobe;skeletal muscle; 0.62976 0.09332 -0.132199953 43.97853267 807.19813 5.59655 POLM 2.42618818804445e-08 0.461040028932302 0.538959946805816 polymerase (DNA) mu FUNCTION: Gap-filling polymerase involved in repair of DNA double- strand breaks by non-homologous end joining (NHEJ). Participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination. {ECO:0000269|PubMed:12640116, ECO:0000269|PubMed:12888504, ECO:0000269|PubMed:17483519, ECO:0000269|PubMed:17915942}.; . TISSUE SPECIFICITY: Expressed in a number of tissues. Abundant in thymus.; smooth muscle;colon;bone marrow;retina;uterus;prostate;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;adrenal cortex;blood;skeletal muscle;lung;placenta;liver;duodenum;alveolus;cervix;spleen;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion; 0.04343 . -0.023789244 52.09365416 411.97542 4.25155 POLN 2.99655974305971e-32 1.6872524535886e-06 0.999998312747546 polymerase (DNA) nu . . TISSUE SPECIFICITY: Highly expressed in testis and heart. Weakly expressed in skeletal muscle. {ECO:0000269|PubMed:12794064}.; prostate;parathyroid;stomach; . 0.06562 . 0.653987697 84.18259023 4366.19692 13.18659 POLQ 9.94639217152803e-47 1.73243468659873e-06 0.999998267565313 polymerase (DNA) theta FUNCTION: DNA polymerase that promotes microhomology-mediated end- joining (MMEJ), an alternative non-homologous end-joining (NHEJ) machinery triggered in response to double-strand breaks in DNA (PubMed:25642963, PubMed:25643323). MMEJ is an error-prone repair pathway that produces deletions of sequences from the strand being repaired and promotes genomic rearrangements, such as telomere fusions, some of them leading to cellular transformation (PubMed:25642963, PubMed:25643323). POLQ acts as an inhibitor of homology-recombination repair (HR) pathway by limiting RAD51 accumulation at resected ends (PubMed:25642963). POLQ-mediated MMEJ may be required to promote the survival of cells with a compromised HR repair pathway, thereby preventing genomic havoc by resolving unrepaired lesions (By similarity). The polymerase acts by binding directly the 2 ends of resected double-strand breaks, allowing microhomologous sequences in the overhangs to form base pairs. It then extends each strand from the base-paired region using the opposing overhang as a template. Requires partially resected DNA containing 2 to 6 base pairs of microhomology to perform MMEJ (PubMed:25643323). The polymerase activity is highly promiscuous: unlike most polymerases, promotes extension of ssDNA and partial ssDNA (pssDNA) substrates (PubMed:18503084, PubMed:21050863, PubMed:22135286). Also exhibits low-fidelity DNA synthesis, translesion synthesis and lyase activity, and it is implicated in interstrand-cross-link repair, base excision repair and DNA end-joining (PubMed:14576298, PubMed:18503084, PubMed:19188258, PubMed:24648516). Involved in somatic hypermutation of immunoglobulin genes, a process that requires the activity of DNA polymerases to ultimately introduce mutations at both A/T and C/G base pairs (By similarity). {ECO:0000250|UniProtKB:Q8CGS6, ECO:0000269|PubMed:14576298, ECO:0000269|PubMed:18503084, ECO:0000269|PubMed:19188258, ECO:0000269|PubMed:21050863, ECO:0000269|PubMed:22135286, ECO:0000269|PubMed:24648516, ECO:0000269|PubMed:25642963, ECO:0000269|PubMed:25643323}.; DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:20624954, ECO:0000269|PubMed:20700469, ECO:0000269|PubMed:25409685}. Note=The gene represented in this entry may be involved in disease pathogenesis.; TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:14576298}.; unclassifiable (Anatomical System);lymph node;ovary;colon;parathyroid;blood;bone marrow;breast;uterus;whole body;lung;cochlea;bone;placenta;visual apparatus;liver;testis;spleen;germinal center;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17652 0.09393 2.324634612 98.37225761 4712.21542 13.85529 POLR1A 0.999861745940553 0.000138254059447401 9.81203397792753e-18 polymerase (RNA) I subunit A FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity). {ECO:0000250|UniProtKB:P10964}.; DISEASE: Acrofacial dysostosis, Cincinnati type (AFDCIN) [MIM:616462]: A form of acrofacial dysostosis, a group of disorders which are characterized by malformation of the craniofacial skeleton and, in some patients, the limbs. {ECO:0000269|PubMed:25913037}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;colon;parathyroid;skin;retina;uterus;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;spinal cord;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;epididymis;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; skeletal muscle; 0.23443 0.21983 0.086234637 60.326728 1702.42047 7.60869 POLR1B 0.91220791018127 0.0877920449760233 4.48427069632025e-08 polymerase (RNA) I subunit B FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity). {ECO:0000250}.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;muscle;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.40671 0.19997 -0.747690508 13.75324369 3437.70062 11.26080 POLR1C 0.000291622651225996 0.938244891392675 0.0614634859560986 polymerase (RNA) I subunit C FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively. RPAC1 is part of the Pol core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity). {ECO:0000250|UniProtKB:P07703, ECO:0000305|PubMed:26151409}.; DISEASE: Treacher Collins syndrome 3 (TCS3) [MIM:248390]: A form of Treacher Collins syndrome, a disorder of craniofacial development. Treacher Collins syndrome is characterized by a combination of bilateral downward slanting of the palpebral fissures, colobomas of the lower eyelids with a paucity of eyelashes medial to the defect, hypoplasia of the facial bones, cleft palate, malformation of the external ears, atresia of the external auditory canals, and bilateral conductive hearing loss. {ECO:0000269|PubMed:21131976}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leukodystrophy, hypomyelinating, 11 (HLD11) [MIM:616494]: An autosomal recessive neurologic disorder characterized by brain hypomyelination, delayed psychomotor development, intellectual disability, tremor and other neurologic symptoms. Some patients may additionally manifest non-neurologic features, particularly dental abnormalities and hypogonadotropic hypogonadism. {ECO:0000269|PubMed:26151409}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;thyroid;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;testis - interstitial;medulla oblongata;superior cervical ganglion;thalamus;temporal lobe;atrioventricular node;pons;skeletal muscle;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.50635 0.17650 -0.093566408 46.7386176 182.78241 2.93589 POLR1D 0.257868790684444 0.639769692566009 0.102361516749547 polymerase (RNA) I subunit D FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common core component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively.; DISEASE: Treacher Collins syndrome 2 (TCS2) [MIM:613717]: A form of Treacher Collins syndrome, a disorder of craniofacial development. Treacher Collins syndrome is characterized by a combination of bilateral downward slanting of the palpebral fissures, colobomas of the lower eyelids with a paucity of eyelashes medial to the defect, hypoplasia of the facial bones, cleft palate, malformation of the external ears, atresia of the external auditory canals, and bilateral conductive hearing loss. {ECO:0000269|PubMed:21131976}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . umbilical cord;ovary;salivary gland;intestine;colon;choroid;vein;skin;bone marrow;uterus;prostate;whole body;endometrium;synovium;bone;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;breast;lung;cornea;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach; lung;tumor;testis;kidney;cerebellum; 0.20581 0.16306 -0.315847836 31.68789809 5.74204 0.21531 POLR1E 1.02878653124634e-05 0.938020770778911 0.0619689413557764 polymerase (RNA) I subunit E FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Appears to be involved in the formation of the initiation complex at the promoter by mediating the interaction between Pol I and UBTF/UBF (By similarity). {ECO:0000250}.; . . . . 0.65474 0.10817 0.420771676 77.15852795 1791.85043 7.81316 POLR2A 0.999999942102154 5.78978458037217e-08 4.17605305401341e-21 polymerase (RNA) II subunit A FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Acts as an RNA- dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome. {ECO:0000269|PubMed:18032511, ECO:0000269|PubMed:20231364, ECO:0000269|PubMed:23748380, ECO:0000269|PubMed:9852112}.; . . lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; subthalamic nucleus;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion; 0.99710 0.57200 -3.515858098 0.318471338 28.22828 0.90501 POLR2B 0.988161838424889 0.0118381615626829 1.24283822618506e-11 polymerase (RNA) II subunit B FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB2 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template (By similarity). {ECO:0000250, ECO:0000269|PubMed:9852112}.; . . smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;small intestine;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; testis - interstitial;subthalamic nucleus;testis;pons;parietal lobe;cingulate cortex; 0.35804 0.49283 -1.001120478 8.321538099 27.50599 0.88564 POLR2C 0.0470077256392426 0.94784311599018 0.00514915837057704 polymerase (RNA) II subunit C FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB3 is part of the core element with the central large cleft and the clamp element that moves to open and close the cleft (By similarity). {ECO:0000250, ECO:0000269|PubMed:9852112}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;medulla oblongata;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle; 0.44839 0.23984 -0.183570861 39.95046001 3.62115 0.13257 POLR2CP1 . . . polymerase (RNA) II subunit C pseudogene 1 . . . . . . . . . . . POLR2D 0.470737784692657 0.505016466932955 0.0242457483743878 polymerase (RNA) II subunit D FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB4 is part of a subcomplex with RPB7 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA (By similarity). {ECO:0000250, ECO:0000269|PubMed:9852112}.; . . medulla oblongata;smooth muscle;ovary;salivary gland;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;oesophagus;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach;aorta; . 0.47550 0.20833 -0.119252484 44.53880632 1.79817 0.05677 POLR2E 4.40648501422082e-08 0.112415255295516 0.887584700639634 polymerase (RNA) II subunit E FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2E/RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process (By similarity). {ECO:0000250, ECO:0000269|PubMed:9852112}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;visual apparatus;duodenum;liver;spleen;kidney;mammary gland;stomach; amygdala;whole brain;heart;liver; 0.44115 0.32227 -0.426079032 25.36565228 16.48084 0.58328 POLR2F 0.652869046375363 0.345910661803254 0.00122029182138325 polymerase (RNA) II subunit F FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II, and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2F/RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds (By similarity). {ECO:0000250, ECO:0000269|PubMed:9852112}.; . . unclassifiable (Anatomical System);substantia nigra;skin;retina; whole brain;heart;liver;trigeminal ganglion;skeletal muscle; 0.16247 0.16465 -0.031067188 51.03798066 433.09933 4.34354 POLR2G 0.00646539515591118 0.912509375121526 0.0810252297225628 polymerase (RNA) II subunit G FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB7 is part of a subcomplex with RPB4 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA (By similarity). Binds RNA. {ECO:0000250, ECO:0000269|PubMed:9852112}.; . . medulla oblongata;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.28446 0.28104 -0.009020804 52.8544468 4.36266 0.15852 POLR2H 0.902767280232976 0.096399849560583 0.000832870206440684 polymerase (RNA) II subunit H FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. {ECO:0000269|PubMed:9852112}.; . . lymphoreticular;ovary;salivary gland;sympathetic chain;intestine;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);trophoblast;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;atrioventricular node;kidney;cerebellum; 0.10147 0.21641 -0.031067188 51.03798066 21.98231 0.73919 POLR2I 0.0541602779086594 0.863955031593032 0.0818846904983082 polymerase (RNA) II subunit I FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB9 is part of the upper jaw surrounding the central large cleft and thought to grab the incoming DNA template (By similarity). {ECO:0000250, ECO:0000269|PubMed:9852112}.; . . ovary;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;testis;artery;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;placenta;hippocampus;kidney;stomach;aorta; whole brain;testis - interstitial;testis - seminiferous tubule;heart;cerebellum peduncles;liver;testis;skeletal muscle; 0.19255 0.23021 -0.053113545 49.38664779 4.6843 0.16797 POLR2J 0.444173138750063 0.526638707263758 0.0291881539861797 polymerase (RNA) II subunit J FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB11 is part of the core element with the central large cleft (By similarity). {ECO:0000250, ECO:0000269|PubMed:9852112}.; . TISSUE SPECIFICITY: Ubiquitously expressed. High expression was found in heart and skeletal muscle. {ECO:0000269|PubMed:11747469}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;synovium;testis;unclassifiable (Anatomical System);trophoblast;small intestine;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;duodenum;hypopharynx;head and neck;kidney;stomach; . 0.12191 0.18866 0.079165051 59.43029016 3.698 0.13761 POLR2J2 0.0923409063648301 0.57003478351103 0.33762431012414 polymerase (RNA) II subunit J2 FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB11 is part of the core element with the central large cleft (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11747469}.; ovary;colon;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;germinal center;bladder;pineal gland;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;lung;placenta;visual apparatus;hypopharynx;head and neck;cervix;mammary gland;stomach;thymus; . . 0.14943 . . 21.19593 0.71557 POLR2J3 . . . polymerase (RNA) II subunit J3 FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB11 is part of the core element with the central large cleft (By similarity). {ECO:0000250}.; . . . . . 0.09141 . . 170.88018 2.85115 POLR2J4 . . . polymerase (RNA) II subunit J4, pseudogene . . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;synovium;testis;unclassifiable (Anatomical System);trophoblast;small intestine;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; . . . . . . . POLR2K 0.0117782524449014 0.638167983557482 0.350053763997616 polymerase (RNA) II subunit K FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively.; . . myocardium;medulla oblongata;ovary;skin;retina;prostate;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;tongue;urinary;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; superior cervical ganglion;subthalamic nucleus;occipital lobe;globus pallidus;ciliary ganglion;cingulate cortex; 0.11693 0.23984 0.057118534 57.99716914 2.52887 0.09360 POLR2KP1 . . . polymerase (RNA) II subunit K pseudogene 1 . . . . . . . . . . . POLR2KP2 . . . polymerase (RNA) II subunit K pseudogene 2 . . . . . . . . . . . POLR2L 0.53288051090857 0.407614286143349 0.0595052029480806 polymerase (RNA) II subunit L FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2L/RBP10 is part of the core element with the central large cleft (By similarity). {ECO:0000250, ECO:0000269|PubMed:9852112}.; . . ovary;umbilical cord;skin;retina;prostate;optic nerve;frontal lobe;thyroid;bladder;brain;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);trophoblast;lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;placenta;hippocampus;kidney;aorta;stomach; superior cervical ganglion;adipose tissue;smooth muscle;lung;heart;liver;appendix;trigeminal ganglion; 0.46128 0.36254 -0.053113545 49.38664779 2.77442 0.09905 POLR2LP1 . . . polymerase (RNA) II subunit L pseudogene 1 . . . . . . . . . . . POLR2M 0.169086388609866 0.816977408270344 0.0139362031197901 polymerase (RNA) II subunit M FUNCTION: Isoform 1 appears to be a stable component of the Pol II(G) complex form of RNA polymerase II (Pol II). Pol II synthesizes mRNA precursors and many functional non-coding RNAs and is the central component of the basal RNA polymerase II transcription machinery. Isoform 1 may play a role in the Mediator complex-dependent regulation of transcription activation. Isoform 1 acts in vitro as a negative regulator of transcriptional activation; this repression is relieved by the Mediator complex, which restores Pol II(G) activator-dependent transcription to a level equivalent to that of Pol II. {ECO:0000269|PubMed:16769904}.; . TISSUE SPECIFICITY: Detected in adult an fetal brain. Detected in heart, kidney, skeletal muscle, small intestine, lung, prostate and testis. {ECO:0000269|PubMed:15233991}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; amygdala;uterus;occipital lobe;subthalamic nucleus;superior cervical ganglion;prefrontal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; . 0.10192 0.308721233 72.59966973 2.26659 0.07616 POLR3A 7.38505099463942e-14 0.997674684874812 0.00232531512511417 polymerase (RNA) III subunit A FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity). Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway. {ECO:0000250, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}.; . TISSUE SPECIFICITY: Expressed in the brain, in the cortex and the white matter (at protein level). {ECO:0000269|PubMed:21855841}.; . . 0.49417 0.12225 -1.920024747 1.928520878 227.15204 3.25699 POLR3B 2.72991445717276e-09 0.999990582407644 9.41486244116852e-06 polymerase (RNA) III subunit B FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity). Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway. {ECO:0000250, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}.; DISEASE: Leukodystrophy, hypomyelinating, 8, with or without oligodontia and/or hypogonadotropic hypogonadism (HLD8) [MIM:614381]: An autosomal recessive neurodegenerative disorder characterized by early childhood onset of cerebellar ataxia and mild intellectual disabilities associated with diffuse hypomyelination apparent on brain MRI. Variable features include oligodontia and/or hypogonadotropic hypogonadism. {ECO:0000269|PubMed:22036171, ECO:0000269|PubMed:22036172, ECO:0000269|PubMed:23355746}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);colon;fovea centralis;skin;skeletal muscle;bone marrow;breast;bile duct;pancreas;prostate;lung;larynx;bone;thyroid;placenta;macula lutea;hippocampus;pituitary gland;hypopharynx;liver;cervix;head and neck;spleen;brain;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.58449 0.12971 -1.482570877 3.662420382 318.88375 3.79262 POLR3C 8.6570108559178e-06 0.982027806170719 0.0179635368184254 polymerase (RNA) III subunit C FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with other members of the subcomplex RNA Pol III binding to the TFIIIB- DNA complex via the interactions between TFIIIB and POLR3F. May be involved either in the recruitment and stabilization of the subcomplex within RNA polymerase III, or in stimulating catalytic functions of other subunits during initiation. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway. {ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}.; . . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;blood;skeletal muscle;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.31777 0.11458 0.575097644 82.1656051 157.06069 2.73790 POLR3D 5.65731890104614e-11 0.113611090969852 0.886388908973575 polymerase (RNA) III subunit D FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). {ECO:0000250, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis;ciliary ganglion;trigeminal ganglion; 0.45378 0.12429 -0.381986487 27.68931352 104.84774 2.21287 POLR3DP1 . . . polymerase (RNA) III subunit D pseudogene 1 . . . . . . . . . . . POLR3E 0.0194658182232362 0.980500938005545 3.32437712182833e-05 polymerase (RNA) III subunit E FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Essential for efficient transcription from both the type 2 VAI and type 3 U6 RNA polymerase III promoters. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). {ECO:0000250, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;liver;amnion;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; atrioventricular node;trigeminal ganglion; 0.35218 0.14468 -0.685180376 15.32200991 520.28326 4.65833 POLR3F 0.00386617468438894 0.957556956499073 0.0385768688165378 polymerase (RNA) III subunit F FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct RNA Pol III binding to the TFIIIB-DNA complex. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway. {ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}.; . . . . 0.20176 0.11682 -0.273576253 33.97027601 61.74337 1.60123 POLR3G 6.42759125510305e-05 0.47980883423665 0.520126889850799 polymerase (RNA) III subunit G FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with other members of the RPC3/POLR3C-RPC6/POLR3F- RPC7/POLR3G subcomplex RNA Pol III binding to the TFIIIB-DNA complex via the interactions between TFIIIB and POLR3F. May be involved either in the recruitment and stabilization of the subcomplex within RNA polymerase III, or in stimulating catalytic functions of other subunits during initiation. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway. {ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}.; . . . . 0.33235 . -0.163345027 41.24793583 20.55251 0.69832 POLR3GL 0.0024402126746499 0.928303266644487 0.0692565206808634 polymerase (RNA) III subunit G like . . . . . 0.15289 0.11495 -0.095386216 46.48502005 23.8527 0.78684 POLR3GP1 . . . polymerase (RNA) III subunit G pseudogene 1 . . . . . . . . . . . POLR3GP2 . . . polymerase (RNA) III subunit G pseudogene 2 . . . . . . . . . . . POLR3H 0.00200710591580713 0.738464311957058 0.259528582127135 polymerase (RNA) III subunit H FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). {ECO:0000250, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}.; . . myocardium;lymphoreticular;ovary;skin;bone marrow;retina;prostate;subthalamic nucleus;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;urinary;blood;lens;skeletal muscle;breast;bronchus;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;ileum;whole body;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;cerebellum; 0.14890 0.12200 -0.538132194 20.26421326 30.82453 0.97727 POLR3K 0.324223634570766 0.610135083836841 0.0656412815923928 polymerase (RNA) III subunit K FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). {ECO:0000250, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}.; . . lymphoreticular;ovary;umbilical cord;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;globus pallidus;pons;trigeminal ganglion;skeletal muscle; 0.72345 0.11149 -0.185391282 39.67916962 10.37777 0.37793 POLR3KP1 . . . polymerase (RNA) III subunit K pseudogene 1 . . . . . . . . . . . POLR3KP2 . . . polymerase (RNA) III subunit K pseudogene 2 . . . . . . . . . . . POLRMT 2.5979329788051e-13 0.399829310432495 0.600170689567245 polymerase (RNA) mitochondrial FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of mitochondrial DNA into RNA using the four ribonucleoside triphosphates as substrates. {ECO:0000269|PubMed:21278163}.; . . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;cerebral cortex;endometrium;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;liver;testis;skeletal muscle; 0.11466 0.11307 -0.024005347 51.92262326 2312.79995 8.90614 POLRMTP1 . . . polymerase (RNA) mitochondrial pseudogene 1 . . . . . . . . . . . POM121 . . . POM121 transmembrane nucleoporin FUNCTION: Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269|PubMed:17900573}.; . . medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;cartilage;heart;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;thymus;cerebellum; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.22550 0.08649 -0.33061537 30.82094834 663.23352 5.16151 POM121B . . . POM121 transmembrane nucleoporin B (pseudogene) FUNCTION: Putative component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane (By similarity). {ECO:0000250}.; . . . . . 0.08403 . . . . POM121C . . . POM121 transmembrane nucleoporin C FUNCTION: Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269|PubMed:17900573}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;thymus; . 0.08931 0.08403 . . 2897.33208 10.19948 POM121L1P . . . POM121 transmembrane nucleoporin like 1, pseudogene . . . . . . . . . . . POM121L2 . . . POM121 transmembrane nucleoporin like 2 . . . . . 0.03374 . . . 4148.61055 12.78909 POM121L3P . . . POM121 transmembrane nucleoporin like 3, pseudogene . . . . . . . . . . . POM121L4P . . . POM121 transmembrane nucleoporin like 4, pseudogene . . . . . . . . . . . POM121L6P . . . POM121 transmembrane nucleoporin like 6, pseudogene . . . . . . . . . . . POM121L7 . . . POM121 transmembrane nucleoporin like 7 . . . testis;retina; . . . . . . . POM121L8P . . . POM121 transmembrane nucleoporin like 8, pseudogene . . . . . . . . . . . POM121L9P . . . POM121 transmembrane nucleoporin like 9, pseudogene . . . . . . . . . . . POM121L10P . . . POM121 transmembrane nucleoporin like 10, pseudogene . . . . . . . . . . . POM121L11P . . . POM121 transmembrane nucleoporin like 11, pseudogene . . . . . . . . . . . POM121L12 8.97051067778844e-05 0.335171861835943 0.664738433057279 POM121 transmembrane nucleoporin like 12 . . . . . . . 1.46612072 95.25241802 3046.32091 10.49032 POM121L13P . . . POM121 transmembrane nucleoporin like 13, pseudogene . . . . . . . . . . . POM121L14P . . . POM121 transmembrane nucleoporin like 14, pseudogene . . . . . . . . . . . POMC 0.000689013181047222 0.510089563328766 0.489221423490186 proopiomelanocortin FUNCTION: ACTH stimulates the adrenal glands to release cortisol.; FUNCTION: Beta-endorphin and Met-enkephalin are endogenous opiates.; DISEASE: Obesity (OBESITY) [MIM:601665]: A condition characterized by an increase of body weight beyond the limitation of skeletal and physical requirements, as the result of excessive accumulation of body fat. {ECO:0000269|PubMed:12165561}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; DISEASE: Pro-opiomelanocortinin deficiency (POMCD) [MIM:609734]: Affected individuals present early-onset obesity, adrenal insufficiency and red hair. {ECO:0000269|PubMed:9620771}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: ACTH and MSH are produced by the pituitary gland.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;choroid;skin;uterus;whole body;lung;cerebral cortex;placenta;pituitary gland;testis;brain; superior cervical ganglion;testis - seminiferous tubule;testis;pituitary;skeletal muscle; 0.42236 0.98077 . . 780.95479 5.52940 POMGNT1 1.68023697303463e-09 0.989024463126871 0.010975535192892 protein O-linked mannose N-acetylglucosaminyltransferase 1 (beta 1,2-) FUNCTION: Participates in O-mannosyl glycosylation. May be responsible for the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O- Ser/Thr moiety on alpha-dystroglycan and other O-mannosylated proteins. Is specific for alpha linked terminal mannose and does not have MGAT3, MGAT4, MGAT5, MGAT7 or MGAT8 activity. {ECO:0000269|PubMed:11709191}.; DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A3 (MDDGA3) [MIM:253280]: An autosomal recessive disorder characterized by congenital muscular dystrophy, ocular abnormalities, cobblestone lissencephaly, and cerebellar and pontine hypoplasia. Patients present severe congenital myopia, congenital glaucoma, pallor of the optic disks, retinal hypoplasia, mental retardation, hydrocephalus, abnormal electroencephalograms, generalized muscle weakness and myoclonic jerks. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease. {ECO:0000269|PubMed:11709191, ECO:0000269|PubMed:12588800, ECO:0000269|PubMed:15236414, ECO:0000269|PubMed:15466003, ECO:0000269|PubMed:17030669, ECO:0000269|PubMed:19067344}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Muscular dystrophy-dystroglycanopathy congenital with mental retardation B3 (MDDGB3) [MIM:613151]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with mental retardation and mild structural brain abnormalities. Clinical features include mental retardation, white matter changes, cerebellar cysts, pontine hypoplasia, myopia, optic atrophy, decreased alpha-dystroglycan on muscle biopsy and increased serum creatine kinase. {ECO:0000269|PubMed:17030669, ECO:0000269|PubMed:19067344, ECO:0000269|PubMed:19299310}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C3 (MDDGC3) [MIM:613157]: A rare form of limb-girdle muscular dystrophy with normal cognition. Muscle biopsy shows dystrophic changes with variable staining for glycosylated alpha- dystroglycan. {ECO:0000269|PubMed:18195152}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Constitutively expressed. An additional weaker band is also detected in spinal cord, lymph node, and trachea. Expressed especially in astrocytes. Also expressed in immature and mature neurons. {ECO:0000269|PubMed:11709191, ECO:0000269|PubMed:11742540}.; . . 0.52912 0.30087 -0.286522835 33.47487615 150.18197 2.67332 POMGNT2 0.00772677154516411 0.927075062393216 0.0651981660616201 protein O-linked mannose N-acetylglucosaminyltransferase 2 (beta 1,4-) FUNCTION: O-linked mannose beta-1,4-N- acetylglucosaminyltransferase that tranfers UDP-N-acetyl-D- glucosamine to the 4-position of the mannose to generate N-acetyl- D-glucosamine-beta-1,4-O-D-mannosylprotein. Involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N- acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate- 6-)mannose), a carbohydrate structure present in alpha- dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. {ECO:0000269|PubMed:23929950}.; . TISSUE SPECIFICITY: Highly expressed in the brain, muscle, heart, and kidney in both fetus and adult. In the brain, highest expression in the cortex and cerebellum. Highly expressed in the pancreas. {ECO:0000269|PubMed:22958903}.; . . 0.21810 . -0.881793075 10.53904223 382.89913 4.12688 POMK 0.000523312395933512 0.69133099922303 0.308145688381036 protein-O-mannose kinase FUNCTION: Protein O-mannose kinase that specifically mediates phosphorylation at the 6-position of an O-mannose of the trisaccharide (N-acetylgalactosamine (GalNAc)-beta-1,3-N- acetylglucosamine (GlcNAc)-beta-1,4-mannose) to generate phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine- beta-1,3-N-acetylglucosamine-beta-1,4-(phosphate-6-)mannose). Phosphorylated O-mannosyl trisaccharide is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Only shows kinase activity when the GalNAc-beta-3-GlcNAc-beta-terminus is linked to the 4-position of O-mannose, suggesting that this disaccharide serves as the substrate recognition motif. {ECO:0000269|PubMed:23519211, ECO:0000269|PubMed:23929950}.; DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C12 (MDDGC12) [MIM:616094]: An autosomal recessive limb-girdle congenital muscular dystrophy, characterized by muscle weakness and delayed motor development in association with cognitive impairment. {ECO:0000269|PubMed:24925318}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest expression is observed in brain, skeletal muscle, kidney and heart in fetal and adult tissues. {ECO:0000269|PubMed:24925318}.; . . . . . . 177.14114 2.89158 POMP 0.861423055957475 0.136498467010391 0.00207847703213413 proteasome maturation protein FUNCTION: Molecular chaperone essential for the assembly of standard proteasomes and immunoproteasomes. Degraded after completion of proteasome maturation. Mediates the association of 20S preproteasome with the endoplasmic reticulum. {ECO:0000269|PubMed:15944226, ECO:0000269|PubMed:16251969, ECO:0000269|PubMed:17948026}.; DISEASE: Keratosis linearis with ichthyosis congenita and sclerosing keratoderma (KLICK) [MIM:601952]: A keratinizing disorder characterized by ichthyosis, palmoplantar keratoderma with constricting bands around fingers, flexural deformities of fingers and keratotic papules in a linear distribution on the flexural side of large joints. Histological examination of the skin of affected individuals shows hypertrophy and hyperplasia of the spinous, granular and horny epidermal layer. {ECO:0000269|PubMed:20226437}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Strongly expressed from the basal layer to the granular layer of healthy epidermis, whereas in KLICK patients there is a gradual decrease of expression toward the granular layer. {ECO:0000269|PubMed:20226437}.; . . 0.27467 0.10208 -0.185391282 39.67916962 5.50459 0.20506 POMT1 4.99835474252924e-10 0.987387787093966 0.0126122124061988 protein O-mannosyltransferase 1 FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. {ECO:0000269|PubMed:12369018, ECO:0000269|PubMed:14699049}.; DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A1 (MDDGA1) [MIM:236670]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with cobblestone lissencephaly and other brain anomalies, eye malformations, profound mental retardation, and death usually in the first years of life. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease. {ECO:0000269|PubMed:12369018, ECO:0000269|PubMed:15037715, ECO:0000269|PubMed:15637732, ECO:0000269|PubMed:16575835}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C1 (MDDGC1) [MIM:609308]: An autosomal recessive degenerative myopathy associated with mild mental retardation without any obvious structural brain abnormality. An abnormal alpha- dystroglycan pattern in observed in the muscle. {ECO:0000269|PubMed:15792865}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis, heart and pancreas. Detected at lower levels in kidney, skeletal muscle, brain, placenta, lung and liver.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;kidney;stomach;thymus; testis - interstitial;testis - seminiferous tubule;testis; 0.15432 0.23758 -0.301297762 32.25996697 1203.9994 6.57452 POMT2 0.000130414429321649 0.999487914322117 0.000381671248561716 protein O-mannosyltransferase 2 FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. {ECO:0000269|PubMed:14699049}.; DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A2 (MDDGA2) [MIM:613150]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with cobblestone lissencephaly and other brain anomalies, eye malformations, profound mental retardation, and death usually in the first years of life. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease. {ECO:0000269|PubMed:15894594, ECO:0000269|PubMed:16701995, ECO:0000269|PubMed:17878207, ECO:0000269|PubMed:19138766, ECO:0000269|PubMed:22958903}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Muscular dystrophy-dystroglycanopathy congenital with mental retardation B2 (MDDGB2) [MIM:613156]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with mental retardation and mild structural brain abnormalities. {ECO:0000269|PubMed:17634419, ECO:0000269|PubMed:19299310}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C2 (MDDGC2) [MIM:613158]: An autosomal recessive muscular dystrophy with onset after ambulation is achieved. MDDGC2 is characterized by increased serum creatine kinase and mild muscle weakness. Muscle biopsy shows dystrophic changes, inflammatory changes, and severely decreased alpha-dystroglycan. Cognition is normal. {ECO:0000269|PubMed:17878207, ECO:0000269|PubMed:17923109}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in testis; detected at low levels in most tissues.; medulla oblongata;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;synovium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.34060 0.19007 -0.929520514 9.683887709 230.84082 3.28529 POMZP3 0.879121225424826 0.119421063584434 0.00145771099074044 POM121 and ZP3 fusion . . TISSUE SPECIFICITY: Expressed in spleen, thymus, pancreas, testis, ovary, small intestine, colon and lymphocytes. {ECO:0000269|PubMed:7789967}.; unclassifiable (Anatomical System);smooth muscle;hypothalamus;salivary gland;colon;blood;lens;bone marrow;uterus;prostate;whole body;lung;frontal lobe;larynx;placenta;duodenum;liver;testis;amniotic fluid;head and neck;spleen;kidney;brain; . 0.18133 0.08649 0.415317661 76.81056853 109.91563 2.27728 PON1 0.00220884417330799 0.979369891810069 0.0184212640166233 paraoxonase 1 FUNCTION: Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation. {ECO:0000269|PubMed:10479665, ECO:0000269|PubMed:15772423}.; DISEASE: Microvascular complications of diabetes 5 (MVCD5) [MIM:612633]: Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end- stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Homozygosity for the Leu-55 allele is strongly associated with the development of retinal disease in diabetic patients.; TISSUE SPECIFICITY: Plasma, associated with HDL (at protein level). Expressed in liver, but not in heart, brain, placenta, lung, skeletal muscle, kidney or pancreas. {ECO:0000269|PubMed:8292612, ECO:0000269|PubMed:8382160}.; unclassifiable (Anatomical System);lung;islets of Langerhans;bone;liver;testis;spleen;brain; fetal liver;superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.12885 0.61089 0.751474114 86.64779429 1431.12238 7.06089 PON2 0.0014042483858281 0.86842781384635 0.130167937767822 paraoxonase 2 FUNCTION: Capable of hydrolyzing lactones and a number of aromatic carboxylic acid esters. Has antioxidant activity. Is not associated with high density lipoprotein. Prevents LDL lipid peroxidation, reverses the oxidation of mildly oxidized LDL, and inhibits the ability of MM-LDL to induce monocyte chemotaxis. {ECO:0000269|PubMed:11579088, ECO:0000269|PubMed:15772423}.; . TISSUE SPECIFICITY: Widely expressed with highest expression in liver, lung, placenta, testis and heart. {ECO:0000269|PubMed:11579088}.; ovary;substantia nigra;skin;prostate;endometrium;cochlea;thyroid;bladder;brain;gall bladder;amygdala;heart;cartilage;tongue;adrenal cortex;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;vein;uterus;whole body;bone;pituitary gland;testis;artery;pineal gland;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;aorta;stomach; amygdala;occipital lobe;hypothalamus;spinal cord;caudate nucleus;parietal lobe; 0.13185 0.51629 0.395088462 76.15003539 4349.96524 13.14974 PON3 0.00253678311281302 0.931423060704039 0.066040156183148 paraoxonase 3 FUNCTION: Has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters. Rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents. {ECO:0000269|PubMed:15772423}.; . . unclassifiable (Anatomical System);medulla oblongata;heart;islets of Langerhans;colon;skin;uterus;prostate;whole body;lung;liver;testis;spleen;kidney;brain;stomach; superior cervical ganglion;fetal liver;liver; 0.10846 0.11133 0.64123826 83.97617363 216.51685 3.17966 POP1 2.42370810234407e-08 0.998796459407076 0.00120351635584252 POP1 homolog, ribonuclease P/MRP subunit FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP.; DISEASE: Note=Defects in POP1 may be the cause of a severe skeletal dysplasia reminiscent of anauxetic dysplasia. Affected individuals show severe growth retardation of prenatal onset, a bone dysplasia affecting the epiphyses and metaphyses of the long bones particularly in the lower limbs, and abnormalities of the spine including irregularly shaped vertebral bodies and marked cervical spine instability. {ECO:0000269|PubMed:21455487}.; . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;lung;bone;visual apparatus;liver;cervix;spleen;germinal center;kidney;brain;bladder;stomach; . 0.10212 0.08921 -1.232771118 5.537862703 1547.92913 7.29865 POP4 0.14347717043933 0.837766893886478 0.0187559356741927 POP4 homolog, ribonuclease P/MRP subunit FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. May function with RPP38 to coordinate the nucleolar targeting and/or assembly of RNase P.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;amnion;alveolus;liver;spleen;kidney;mammary gland;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.25519 0.12490 -0.0274281 51.65723048 108.29586 2.25819 POP5 1.28002317887135e-05 0.383056626697781 0.61693057307043 POP5 homolog, ribonuclease P/MRP subunit FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP. {ECO:0000269|PubMed:11413139}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;hypothalamus;adrenal cortex;pharynx;blood;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;spleen;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.10882 0.14229 -0.163345027 41.24793583 51.42928 1.41551 POP7 0.285660408621197 0.629412476120972 0.0849271152578303 POP7 homolog, ribonuclease P/MRP subunit FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP complex, which cleaves pre-rRNA sequences.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;lymph node;heart;tongue;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; whole brain;superior cervical ganglion;liver;globus pallidus;parietal lobe;skeletal muscle; 0.08870 0.14499 0.147123112 64.11299835 16.44643 0.58227 POPDC2 0.000116007752087542 0.606160616194082 0.39372337605383 popeye domain containing 2 FUNCTION: May play an important role in heart development.; . TISSUE SPECIFICITY: Expressed predominantly in the heart, and is also detected in the skeletal muscle. {ECO:0000269|PubMed:10882522}.; unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;colon;parathyroid;blood;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;uterus;optic nerve;lung;endometrium;nasopharynx;placenta;macula lutea;testis;kidney;brain;stomach; heart;skeletal muscle; 0.09514 0.09106 -0.492218069 22.35786742 2085.49252 8.41383 POPDC3 1.70813560977159e-05 0.437250777631815 0.562732141012087 popeye domain containing 3 FUNCTION: May play an important role in heart development.; . TISSUE SPECIFICITY: Expressed predominantly in skeletal muscle and detected in heart. {ECO:0000269|PubMed:10882522}.; unclassifiable (Anatomical System);lung;whole body;frontal lobe;cartilage;heart;islets of Langerhans;visual apparatus;liver;alveolus;testis;skin; dorsal root ganglion;testis - interstitial;superior cervical ganglion;atrioventricular node;skeletal muscle; 0.18460 0.11737 0.238945317 69.20853975 257.74271 3.45364 POR 4.33906087150102e-05 0.990986712395589 0.00896989699569618 P450 (cytochrome) oxidoreductase FUNCTION: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. {ECO:0000255|HAMAP- Rule:MF_03212}.; DISEASE: Antley-Bixler syndrome, with genital anomalies and disordered steroidogenesis (ABS1) [MIM:201750]: A disease characterized by the association of Antley-Bixler syndrome with steroidogenesis defects and abnormal genitalia. Antley-Bixler syndrome is characterized by craniosynostosis, radiohumeral synostosis present from the perinatal period, midface hypoplasia, choanal stenosis or atresia, femoral bowing and multiple joint contractures. {ECO:0000269|PubMed:14758361, ECO:0000269|PubMed:15264278, ECO:0000269|PubMed:15483095}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Disordered steroidogenesis due to cytochrome P450 oxidoreductase deficiency (DISPORD) [MIM:613571]: A disorder resulting in a rare variant of congenital adrenal hyperplasia, with apparent combined P450C17 and P450C21 deficiency and accumulation of steroid metabolites. Affected girls are born with ambiguous genitalia, but their circulating androgens are low and virilization does not progress. Conversely, affected boys are sometimes born undermasculinized. Boys and girls can present with bone malformations, in some cases resembling the pattern seen in patients with Antley-Bixler syndrome. {ECO:0000269|PubMed:14758361, ECO:0000269|PubMed:15220035}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.16542 0.54222 -1.52305413 3.426515688 . . PORCN 0.995196052430872 0.00480346107934362 4.86489784313105e-07 porcupine homolog (Drosophila) FUNCTION: Protein-serine O-palmitoleoyltransferase that acts as a key regulator of the Wnt signaling pathway by mediating the attachment of palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1), to Wnt proteins. Serine palmitoleylation of WNT proteins is required for efficient binding to frizzled receptors. {ECO:0000250|UniProtKB:Q9JJJ7, ECO:0000269|PubMed:12034504, ECO:0000269|PubMed:20826466, ECO:0000269|PubMed:24292069}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in fetal brain, brain, amygdala, caudate nucleus, cerebellum, hippocampus, pituitary, thalamus, heart, skeletal muscle and testis. Isoform 4 is expressed in amygdala, corpus callosum, hippocampus, spinal cord, kidney, liver, lung, spleen, uterus, testis. Isoform 2 and isoform 3 are expressed in substantia negra, spinal cord, heart and lung. {ECO:0000269|PubMed:12034504}.; unclassifiable (Anatomical System);smooth muscle;cartilage;heart;tongue;adrenal cortex;colon;skeletal muscle;pancreas;prostate;lung;cerebral cortex;endometrium;bone;visual apparatus;duodenum;hypopharynx;liver;testis;head and neck;spleen;cervix;brain; . 0.30314 0.29038 -0.516085732 21.20193442 22.82678 0.76189 POSTN 5.5233906383619e-05 0.999891058588061 5.37075055549912e-05 periostin, osteoblast specific factor FUNCTION: Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX (By similarity). Induces cell attachment and spreading and plays a role in cell adhesion. May play a role in extracellular matrix mineralization. {ECO:0000250, ECO:0000269|PubMed:12235007, ECO:0000269|PubMed:18450759}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in aorta, stomach, lower gastrointestinal tract, placenta, uterus, thyroid tissue and breast. Up-regulated in epithelial ovarian tumors. Not expressed in normal ovaries. Also highly expressed at the tumor periphery of lung carcinoma tissue but not within the tumor. Overexpressed in breast cancers. {ECO:0000269|PubMed:11550156, ECO:0000269|PubMed:12235007, ECO:0000269|PubMed:15082792, ECO:0000269|PubMed:23946676}.; . . 0.93326 0.74372 0.266447942 70.5826846 1031.00738 6.16739 POT1 0.522727216703268 0.477242315835056 3.04674616760716e-05 protection of telomeres 1 FUNCTION: Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. Is a component of the double-stranded telomeric DNA- binding TRF1 complex which is involved in the regulation of telomere length by cis-inhibition of telomerase. Also acts as a single-stranded telomeric DNA-binding protein and thus may act as a downstream effector of the TRF1 complex and may transduce information about telomere maintenance and/or length to the telomere terminus. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Binds to two or more telomeric single-stranded 5'-TTAGGG-3' repeats (G-strand) and with high specificity to a minimal telomeric single-stranded 5'- TAGGGTTAG-3' sequence. Binds telomeric single-stranded sequences internally or at proximity of a 3'-end. Its activity is TERT dependent but it does not increase TERT activity by itself. In contrast, the ACD-POT1 heterodimer enhances telomere elongation by increasing telomerase processivity. {ECO:0000269|PubMed:12768206, ECO:0000269|PubMed:12781132, ECO:0000269|PubMed:16166375, ECO:0000269|PubMed:17237768, ECO:0000269|PubMed:20231318}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11349150, ECO:0000269|PubMed:12391173}.; unclassifiable (Anatomical System);cartilage;heart;ovary;lacrimal gland;islets of Langerhans;parathyroid;skin;skeletal muscle;retina;bone marrow;breast;uterus;prostate;lung;thyroid;placenta;visual apparatus;pituitary gland;liver;testis;cervix;kidney;brain;stomach;peripheral nerve; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.16916 0.16160 0.040529541 57.15380986 83.7068 1.94692 POT1-AS1 . . . POT1 antisense RNA 1 . . . . . . . . . . . POTEA . . . POTE ankyrin domain family member A . . . . . 0.04444 . . . . . POTEB . . . POTE ankyrin domain family member B . . . . . 0.10352 0.06565 . . 5.77658 0.21695 POTEB2 0.571892791435193 0.382158007721478 0.0459492008433289 POTE ankyrin domain family member B2 . . . . . . . . . 6798.26439 17.54766 POTEB3 . . . POTE ankyrin domain family member B3 . . . . . . . . . . . POTEC 0.161704413964799 0.835123743732973 0.00317184230222766 POTE ankyrin domain family member C . . TISSUE SPECIFICITY: Expressed in prostate and testis. {ECO:0000269|PubMed:12475935}.; . . 0.10352 0.06565 . . 920.22285 5.89584 POTED 0.736659832423479 0.251779619019395 0.0115605485571263 POTE ankyrin domain family member D . . TISSUE SPECIFICITY: Expressed in prostate, ovary, testis, placenta and prostate cancer cell lines. Localizes to basal and terminal prostate epithelial cells. {ECO:0000269|PubMed:12475935}.; testis;skeletal muscle; . . . . . 180.64544 2.92107 POTEE . . . POTE ankyrin domain family member E . . . . . . . . . 513.98926 4.63955 POTEF . . . POTE ankyrin domain family member F . . TISSUE SPECIFICITY: Expressed in breast cancer cell lines (at protein level). {ECO:0000269|PubMed:17101985}.; prostate;testis;stomach; . . . . . 1056.59425 6.24058 POTEG . . . POTE ankyrin domain family member G . . . . . . . . . 2124.0826 8.48688 POTEH . . . POTE ankyrin domain family member H . . . prostate;testis;stomach; . 0.04666 0.08864 . . 531.82086 4.70466 POTEH-AS1 . . . POTEH antisense RNA 1 . . . . . . . . . . . POTEI . . . POTE ankyrin domain family member I . . . . . . . . . 1959.75641 8.14928 POTEJ . . . POTE ankyrin domain family member J . . . . . . . . . 1579.22659 7.35384 POTEKP . . . POTE ankyrin domain family member K, pseudogene . . TISSUE SPECIFICITY: Expressed in some hepatocellular carcinomas. {ECO:0000269|PubMed:16824795}.; . . . 0.43916 . . . . POTEM 0.784476802333841 0.208826123517634 0.00669707414852418 POTE ankyrin domain family member M . . . . . . . . . 1603.8493 7.40974 POU1F1 0.618818418545953 0.379529677762643 0.00165190369140443 POU class 1 homeobox 1 FUNCTION: Transcription factor involved in the specification of the lactotrope, somatotrope, and thyrotrope phenotypes in the developing anterior pituitary. Activates growth hormone and prolactin genes. Specifically binds to the consensus sequence 5'- TAAAT-3'.; DISEASE: Pituitary hormone deficiency, combined, 1 (CPHD1) [MIM:613038]: Combined pituitary hormone deficiency is defined as the impaired production of growth hormone and one or more of the other five anterior pituitary hormones. CPHD1 is characterized by pleiotropic deficiencies of growth hormone, prolactin and thyroid- stimulating hormone, while the production of adrenocorticotropic hormone, luteinizing hormone, and follicle-stimulating hormone are preserved. In infancy severe growth deficiency from birth as well as distinctive facial features with prominent forehead, marked midfacial hypoplasia with depressed nasal bridge, deep-set eyes, and a short nose with anteverted nostrils and hypoplastic pituitary gland by MRI examination can be seen. Some cases present with severe mental retardation along with short stature. {ECO:0000269|PubMed:11297581, ECO:0000269|PubMed:1472057, ECO:0000269|PubMed:1509262, ECO:0000269|PubMed:1509263, ECO:0000269|PubMed:15928241, ECO:0000269|PubMed:16968807, ECO:0000269|PubMed:7852536, ECO:0000269|PubMed:8768831, ECO:0000269|PubMed:9485179, ECO:0000269|PubMed:9626142}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;placenta;pituitary gland;parathyroid; superior cervical ganglion;pituitary; 0.19992 0.28828 0.038710339 56.92380278 38.64856 1.14539 POU2AF1 0.752817874787067 0.245059269787957 0.00212285542497592 POU class 2 associating factor 1 FUNCTION: Transcriptional coactivator that specifically associates with either OCT1 or OCT2. It boosts the OCT1 mediated promoter activity and to a lesser extent, that of OCT2. It has no intrinsic DNA-binding activity. It recognizes the POU domains of OCT1 and OCT2. It is essential for the response of B-cells to antigens and required for the formation of germinal centers.; DISEASE: Note=A chromosomal aberration involving POU2AF1/OBF1 may be a cause of a form of B-cell leukemia. Translocation t(3;11)(q27;q23) with BCL6. {ECO:0000269|PubMed:8574789}.; TISSUE SPECIFICITY: B-cell specific.; . . 0.17216 0.27607 -0.315847836 31.68789809 69.5327 1.73060 POU2F1 0.913950638110934 0.0860483217384416 1.04015062475828e-06 POU class 2 homeobox 1 FUNCTION: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR (By similarity). In case of human herpes simplex virus (HSV) infection, POU2F1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and HCFC1 thereby enabling the transcription of the viral immediate early genes. {ECO:0000250, ECO:0000269|PubMed:1684878}.; . TISSUE SPECIFICITY: Ubiquitous. Isoform 2 is lymphocyte-specific.; colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;germinal center;brain;unclassifiable (Anatomical System);adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;pons;parietal lobe;skeletal muscle;cingulate cortex; 0.97789 0.41629 -0.334253673 30.70299599 100.87731 2.17460 POU2F2 0.97379427998087 0.0261993917286916 6.32829043840938e-06 POU class 2 homeobox 2 FUNCTION: Transcription factor that specifically binds to the octamer motif (5'-ATTTGCAT-3'). Regulates transcription in a number of tissues in addition to activating immunoglobulin gene expression. Modulates transcription transactivation by NR3C1, AR and PGR. Isoform 5 activates the U2 small nuclear RNA (snRNA) promoter. {ECO:0000269|PubMed:1739980, ECO:0000269|PubMed:2328728, ECO:0000269|PubMed:2901913, ECO:0000269|PubMed:2904654}.; . TISSUE SPECIFICITY: Isoform 3 is B-cell specific. Isoform 5 is expressed in B-cells and the immunoglobulin-expressing T-cell line MOLT-4, but not in the T-cell line BW5147. {ECO:0000269|PubMed:2904654, ECO:0000269|PubMed:3072196}.; unclassifiable (Anatomical System);lymph node;blood;skin;pancreas;lung;placenta;bone;liver;testis;spleen;germinal center;brain;tonsil; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.49246 0.27788 -0.538132194 20.26421326 113.2753 2.31761 POU2F3 0.00288839549557629 0.994479249041517 0.0026323554629064 POU class 2 homeobox 3 FUNCTION: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). Regulated the expression of a number of genes such as SPRR2A or placental lactogen.; . TISSUE SPECIFICITY: Specifically expressed in epidermis and cultured keratinocytes.; unclassifiable (Anatomical System);breast;uterus;thyroid;placenta;stomach; superior cervical ganglion;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.65857 0.26294 0.352813824 74.49280491 2078.72663 8.39999 POU3F1 . . . POU class 3 homeobox 1 FUNCTION: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). Thought to be involved in early embryogenesis and neurogenesis.; . TISSUE SPECIFICITY: Expressed in embryonal stem cells and in the developing brain.; . . 0.73401 . . . 26.59057 0.86120 POU3F2 . . . POU class 3 homeobox 2 FUNCTION: Transcription factor that binds preferentially to the recognition sequence which consists of two distinct half-sites, ('GCAT') and ('TAAT'), separated by a nonconserved spacer region of 0, 2, or 3 nucleotides. Positively regulates the genes under the control of corticotropin-releasing hormone (CRH) and CRH II promoters (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed specifically in the neuroectodermal cell lineage.; unclassifiable (Anatomical System);amygdala;hippocampus;duodenum;brain;skin;skeletal muscle;aorta; skeletal muscle; 0.67393 . . . 70.8118 1.75215 POU3F3 . . . POU class 3 homeobox 3 FUNCTION: Transcription factor that acts synergistically with SOX11 and SOX4. Plays a role in neuronal development. Is implicated in an enhancer activity at the embryonic met- mesencephalic junction; the enhancer element contains the octamer motif (5'-ATTTGCAT-3') (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Brain.; testis; superior cervical ganglion;medulla oblongata;temporal lobe;appendix;pons;trigeminal ganglion; 0.48694 . . . 40.99512 1.20183 POU3F4 0.720490939213332 0.265880116304996 0.0136289444816723 POU class 3 homeobox 4 FUNCTION: Probable transcription factor which exert its primary action widely during early neural development and in a very limited set of neurons in the mature brain.; . TISSUE SPECIFICITY: Brain specific.; . . 0.78270 0.10989 0.125076652 62.7388535 11.43093 0.41295 POU4F1 . . . POU class 4 homeobox 1 FUNCTION: Probable transcription factor which may play a role in the regulation of specific gene expression within a subset of neuronal lineages. May play a role in determining or maintaining the identities of a small subset of visual system neurons.; . TISSUE SPECIFICITY: Brain. Seems to be specific to the retina. Present in the developing brain, spinal cord and eye.; . . 0.77936 . . . 382.15337 4.12114 POU4F2 0.180133325514263 0.766094067120925 0.0537726073648121 POU class 4 homeobox 2 FUNCTION: Transcription factor. May play a role in determining or maintaining the identities of a small subset of visual system neurons.; . TISSUE SPECIFICITY: Brain. Seems to be specific to the retina.; macula lutea;visual apparatus;fovea centralis; dorsal root ganglion;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;skin; 0.63798 0.19967 -0.600630256 18.06440198 973.71567 6.03528 POU4F3 0.721115139448867 0.275871589268524 0.00301327128260892 POU class 4 homeobox 3 FUNCTION: May play a role in determining or maintaining the identities of a small subset of visual system neurons.; . TISSUE SPECIFICITY: Brain. Seems to be specific to the retina. {ECO:0000269|PubMed:7623109, ECO:0000269|PubMed:9506947}.; . . 0.89518 0.15588 -0.53631094 20.53550366 20.59903 0.70015 POU5F1 0.889691089140015 0.110071191766588 0.000237719093397371 POU class 5 homeobox 1 FUNCTION: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). Forms a trimeric complex with SOX2 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. Critical for early embryogenesis and for embryonic stem cell pluripotency. {ECO:0000269|PubMed:18035408}.; . TISSUE SPECIFICITY: Expressed in developing brain. Highest levels found in specific cell layers of the cortex, the olfactory bulb, the hippocampus and the cerebellum. Low levels of expression in adult tissues. {ECO:0000269|PubMed:1408763, ECO:0000269|PubMed:7908264}.; unclassifiable (Anatomical System);uterus;lung;ovary;liver;spleen;brain;mammary gland;stomach; . 0.89483 . -0.119252484 44.53880632 103.67823 2.19958 POU5F1B 7.27271426587485e-07 0.154902824147389 0.845096448581185 POU class 5 homeobox 1B FUNCTION: Shows weak transcriptional activator activity. {ECO:0000269|PubMed:18949397}.; . TISSUE SPECIFICITY: Detected at the mRNA level in several cancer tissues (breast, uterine cervix, lung, thyroid gland, esophagus, colon, urinary bladder, and glioma), but absent in normal tissues. {ECO:0000269|PubMed:16229821, ECO:0000269|PubMed:21341266}.; . . 0.06534 . . . 6077.10056 16.28567 POU5F1P2 . . . POU class 5 homeobox 1 pseudogene 2 . . . . . . . . . . . POU5F1P3 . . . POU class 5 homeobox 1 pseudogene 3 . . . . . . . . . . . POU5F1P4 . . . POU class 5 homeobox 1 pseudogene 4 . . . . . 0.49402 . . . . . POU5F1P5 . . . POU class 5 homeobox 1 pseudogene 5 . . . . . . . . . . . POU5F1P6 . . . POU class 5 homeobox 1 pseudogene 6 . . . . . . . . . . . POU5F1P7 . . . POU class 5 homeobox 1 pseudogene 7 . . . . . . . . . . . POU5F2 0.00100875260505586 0.818045298345106 0.180945949049838 POU domain class 5, transcription factor 2 FUNCTION: Transcription factor that binds preferentially to the octamer motif (5'-ATGTTAAT-3'). May exert a regulatory function in meiotic events that are required for terminal differentiation of male germ cell (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in skeletal and cardiac muscles, brain, heart and lung. Little or no detectable expression found in pancreas, kidney, liver or placenta. {ECO:0000269|PubMed:7908264}.; . . . . . . 24.90286 0.81783 POU6F1 0.907559367268063 0.0917086493702029 0.0007319833617337 POU class 6 homeobox 1 FUNCTION: Transcription factor that binds preferentially to a variant of the octamer motif (5'-ATGATAAT-3'). {ECO:0000250}.; . TISSUE SPECIFICITY: In the embryo, expressed exclusively in the developing brain, whereas in the adult its expression is restricted to brain, heart, skeletal muscle and lung. In the brain, the highest expression levels are found in specific cell layers of the cortex, the olfactory bulb, the hippocampus and the cerebellum.; unclassifiable (Anatomical System);heart;ovary;cartilage;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;prostate;optic nerve;lung;frontal lobe;macula lutea;cervix;kidney;mammary gland;brain; subthalamic nucleus;prefrontal cortex;globus pallidus;skin;cingulate cortex; 0.15868 . -0.207437529 38.2814343 65.38487 1.66494 POU6F2 0.00036907554163621 0.98953523186452 0.010095692593844 POU class 6 homeobox 2 FUNCTION: Probable transcription factor likely to be involved in early steps in the differentiation of amacrine and ganglion cells. Recognizes and binds to the DNA sequence 5'-ATGCAAAT-3'. Isoform 1 does not bind DNA.; . TISSUE SPECIFICITY: Expressed only within the CNS, where its expression is restricted to the medical habenulla, to a dispersed population of neurons in the dorsal hypothalamus, and to subsets of ganglion and amacrine cells in the retina. {ECO:0000269|PubMed:8601806}.; . . 0.81776 0.13521 -0.551080959 19.93394669 2623.72865 9.60505 POU6F2-AS1 . . . POU6F2 antisense RNA 1 . . . . . . . . . . . POU6F2-AS2 . . . POU6F2 antisense RNA 2 . . . . . . . . . . . PP1P . . . pyrophosphatase (inorganic) 1 pseudogene . . . . . . . . . . . PP2D1 . . . protein phosphatase 2C like domain containing 1 . . . testis; dorsal root ganglion;testis - interstitial;testis;atrioventricular node; 0.06757 . . . 1574.50949 7.34299 PPA1 0.00255640189205126 0.932026761408781 0.0654168366991678 pyrophosphatase (inorganic) 1 . . TISSUE SPECIFICITY: Expressed ubiquitously. {ECO:0000269|PubMed:10542310}.; . . 0.60042 0.69332 -0.273576253 33.97027601 15.17107 0.54586 PPA2 9.23378955160168e-06 0.775192031703746 0.224798734506702 pyrophosphatase (inorganic) 2 . . TISSUE SPECIFICITY: Detected in brain, gastric carcinoma, lung, ovary, skeletal muscle, umbilical cord blood and a cell line derived from kidney proximal tubule epithelium. {ECO:0000269|PubMed:15210126}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;kidney;stomach; subthalamic nucleus;ciliary ganglion;atrioventricular node; 0.04350 0.14527 -0.003562597 53.72729417 3367.76337 11.11199 PPAN 1.16703694174413e-08 0.775802522620842 0.224197465708789 peter pan homolog (Drosophila) FUNCTION: May have a role in cell growth.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10944437, ECO:0000269|PubMed:11278528}.; medulla oblongata;ovary;colon;skin;bone marrow;uterus;frontal lobe;cerebral cortex;oesophagus;endometrium;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;blood;skeletal muscle;lung;epididymis;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; . 0.18260 -0.863377021 10.84571833 1585.22106 7.36472 PPAN-P2RY11 1.16703694174413e-08 0.775802522620842 0.224197465708789 PPAN-P2RY11 readthrough FUNCTION: May have a role in cell growth.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10944437, ECO:0000269|PubMed:11278528}.; . . . . -0.622955869 17.16796414 . . PPARA 0.463829864293015 0.535003174941547 0.00116696076543773 peroxisome proliferator activated receptor alpha FUNCTION: Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl- 2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2. {ECO:0000269|PubMed:10195690, ECO:0000269|PubMed:24043310, ECO:0000269|PubMed:7629123, ECO:0000269|PubMed:7684926, ECO:0000269|PubMed:9556573}.; . TISSUE SPECIFICITY: Skeletal muscle, liver, heart and kidney. {ECO:0000269|PubMed:7981125, ECO:0000269|PubMed:8993548}.; colon;parathyroid;fovea centralis;choroid;peritoneum;skin;retina;bone marrow;uterus;optic nerve;whole body;thyroid;testis;amniotic fluid;brain;gall bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;adrenal cortex;lens;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;trigeminal ganglion; 0.32121 0.92276 -0.356299879 29.31115829 2065.11731 8.37395 PPARD 0.966868134632325 0.0330761199877497 5.57453799250923e-05 peroxisome proliferator activated receptor delta FUNCTION: Ligand-activated transcription factor. Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Has a preference for poly-unsaturated fatty acids, such as gamma-linoleic acid and eicosapentanoic acid. Once activated by a ligand, the receptor binds to promoter elements of target genes. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the acyl-CoA oxidase gene. Decreases expression of NPC1L1 once activated by a ligand. {ECO:0000269|PubMed:1333051, ECO:0000269|PubMed:15604518}.; . TISSUE SPECIFICITY: Ubiquitous with maximal levels in placenta and skeletal muscle.; smooth muscle;ovary;colon;choroid;skin;uterus;prostate;frontal lobe;endometrium;larynx;bone;brain;spinal ganglion;unclassifiable (Anatomical System);cartilage;heart;breast;pancreas;lung;nasopharynx;placenta;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;thyroid;placenta;prefrontal cortex;globus pallidus;ciliary ganglion;cerebellum; 0.67546 0.61005 -0.582225231 18.44184949 9.44199 0.34799 PPARG 0.668218173785609 0.33072384451043 0.00105798170396124 peroxisome proliferator activated receptor gamma FUNCTION: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated proinflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of ARNTL/BMAL1 in the blood vessels (By similarity). {ECO:0000250|UniProtKB:P37238, ECO:0000269|PubMed:16150867, ECO:0000269|PubMed:20829347, ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:9065481}.; DISEASE: Note=Defects in PPARG can lead to type 2 insulin- resistant diabetes and hyptertension. PPARG mutations may be associated with colon cancer. {ECO:0000269|PubMed:10394368}.; DISEASE: Obesity (OBESITY) [MIM:601665]: A condition characterized by an increase of body weight beyond the limitation of skeletal and physical requirements, as the result of excessive accumulation of body fat. {ECO:0000269|PubMed:9753710}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; DISEASE: Lipodystrophy, familial partial, 3 (FPLD3) [MIM:604367]: A form of lipodystrophy characterized by marked loss of subcutaneous fat from the extremities. Facial adipose tissue may be increased, decreased or normal. Affected individuals show an increased preponderance of insulin resistance, diabetes mellitus and dyslipidemia. {ECO:0000269|PubMed:11788685, ECO:0000269|PubMed:12453919}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Glioma 1 (GLM1) [MIM:137800]: Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes. {ECO:0000269|PubMed:10851250}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry. Polymorphic PPARG alleles have been found to be significantly over-represented among a cohort of American patients with sporadic glioblastoma multiforme suggesting a possible contribution to disease susceptibility.; TISSUE SPECIFICITY: Highest expression in adipose tissue. Lower in skeletal muscle, spleen, heart and liver. Also detectable in placenta, lung and ovary. {ECO:0000269|PubMed:9065481}.; unclassifiable (Anatomical System);cartilage;heart;urinary;colon;skin;uterus;pancreas;lung;bone;placenta;hypopharynx;liver;testis;cervix;head and neck;kidney;brain;bladder;stomach; superior cervical ganglion;adipose tissue;placenta;ciliary ganglion; 0.38871 0.97350 -0.314027422 31.9297004 580.36578 4.88414 PPARGC1A 0.999660628733418 0.000339371112756326 1.53825587313632e-10 PPARG coactivator 1 alpha FUNCTION: Transcriptional coactivator for steroid receptors and nuclear receptors. Greatly increases the transcriptional activity of PPARG and thyroid hormone receptor on the uncoupling protein promoter. Can regulate key mitochondrial genes that contribute to the program of adaptive thermogenesis. Plays an essential role in metabolic reprogramming in response to dietary availability through coordination of the expression of a wide array of genes involved in glucose and fatty acid metabolism. Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner. Also involved in the integration of the circadian rhythms and energy metabolism. Required for oscillatory expression of clock genes, such as ARNTL/BMAL1 and NR1D1, through the coactivation of RORA and RORC, and metabolic genes, such as PDK4 and PEPCK. {ECO:0000269|PubMed:10713165, ECO:0000269|PubMed:20005308, ECO:0000269|PubMed:21376232, ECO:0000269|PubMed:23836911}.; . TISSUE SPECIFICITY: Heart, skeletal muscle, liver and kidney. Expressed at lower levels in brain and pancreas and at very low levels in the intestine and white adipose tissue. In skeletal muscle, levels were lower in obese than in lean subjects and fasting induced a 2-fold increase in levels in the skeletal muscle in obese subjects. {ECO:0000269|PubMed:10585775, ECO:0000269|PubMed:10643692, ECO:0000269|PubMed:10713165}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;thyroid;pituitary gland;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;adrenal cortex;lens;skeletal muscle;pancreas;pia mater;lung;placenta;macula lutea;liver;head and neck;cervix;kidney;stomach; subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node; 0.98641 0.83983 -0.108334733 45.57088936 3482.86438 11.36596 PPARGC1B 0.934054614318936 0.065945278987448 1.06693615849487e-07 PPARG coactivator 1 beta FUNCTION: Plays a role of stimulator of transcription factors and nuclear receptors activities. Activates transcritional activity of estrogen receptor alpha, nuclear respiratory factor 1 (NRF1) and glucocorticoid receptor in the presence of glucocorticoids. May play a role in constitutive non-adrenergic-mediated mitochondrial biogenesis as suggested by increased basal oxygen consumption and mitochondrial number when overexpressed. May be involved in fat oxidation and non-oxidative glucose metabolism and in the regulation of energy expenditure. Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner. {ECO:0000269|PubMed:11854298, ECO:0000269|PubMed:12678921, ECO:0000269|PubMed:15546003, ECO:0000269|PubMed:23836911}.; . TISSUE SPECIFICITY: Ubiquitous with higher expression in heart, brain and skeletal muscle. {ECO:0000269|PubMed:11854298, ECO:0000269|PubMed:12678921}.; unclassifiable (Anatomical System);pancreas;optic nerve;heart;placenta;macula lutea;cervix;fovea centralis;choroid;lens;brain;retina;bone marrow; superior cervical ganglion;trigeminal ganglion; 0.23449 0.21407 1.061821821 91.47204529 2264.36762 8.79368 PPAT 0.994564413329382 0.00543545352713563 1.33143482159687e-07 phosphoribosyl pyrophosphate amidotransferase . . TISSUE SPECIFICITY: Ubiquitously expressed.; ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;globus pallidus; 0.89076 0.37887 -0.005381972 53.50908233 29.7895 0.95010 PPATP1 . . . phosphoribosyl pyrophosphate amidotransferase pseudogene 1 . . . . . . . . . . . PPATP2 . . . phosphoribosyl pyrophosphate amidotransferase pseudogene 2 . . . . . . . . . . . PPBP 0.267236204496095 0.636661394349437 0.0961024011544679 pro-platelet basic protein FUNCTION: LA-PF4 stimulates DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by human synovial cells. NAP-2 is a ligand for CXCR1 and CXCR2, and NAP-2, NAP-2(73), NAP-2(74), NAP-2(1-66), and most potent NAP-2(1-63) are chemoattractants and activators for neutrophils. TC-1 and TC-2 are antibacterial proteins, in vitro released from activated platelet alpha-granules. CTAP-III(1-81) is more potent than CTAP-III desensitize chemokine-induced neutrophil activation. {ECO:0000269|PubMed:10877842, ECO:0000269|PubMed:7890771, ECO:0000269|PubMed:8950790, ECO:0000269|PubMed:9794434}.; . . unclassifiable (Anatomical System);lung;cartilage;ovary;heart;placenta;liver;testis;colon;parathyroid;spleen;blood; fetal liver;white blood cells;whole blood;bone marrow; 0.34794 0.38595 -0.141298762 42.87567823 2.0088 0.06555 PPBPP1 . . . pro-platelet basic protein pseudogene 1 . . . . . . . . . . . PPBPP2 . . . pro-platelet basic protein pseudogene 2 . . . . . . . . . . . PPCDC 0.00087960119376272 0.56229676518169 0.436823633624548 phosphopantothenoylcysteine decarboxylase FUNCTION: Necessary for the biosynthesis of coenzyme A. Catalyzes the decarboxylation of 4-phosphopantothenoylcysteine to form 4'- phosphopantotheine. {ECO:0000269|PubMed:11923312, ECO:0000269|PubMed:15581364}.; . . colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;bone;pituitary gland;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;muscle;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;kidney;stomach;aorta; superior cervical ganglion; 0.22213 0.13571 -0.115612493 45.12856806 24.77535 0.81327 PPCS 0.00353633641897521 0.839288741075529 0.157174922505496 phosphopantothenoylcysteine synthetase FUNCTION: Catalyzes the first step in the biosynthesis of coenzyme A from vitamin B5, where cysteine is conjugated to 4'- phosphopantothenate to form 4-phosphopantothenoylcysteine. {ECO:0000269|PubMed:11923312, ECO:0000269|PubMed:12906824}.; . . . . 0.11978 0.15942 -0.029247611 51.40363293 18.42775 0.63875 PPDPF 0.000225837231011149 0.305198131483981 0.694576031285008 pancreatic progenitor cell differentiation and proliferation factor FUNCTION: Probable regulator of exocrine pancreas development. {ECO:0000250}.; . . . . 0.07933 . -0.163345027 41.24793583 9.03805 0.33142 PPEF1 0.984407235920156 0.0155924079272197 3.56152624239044e-07 protein phosphatase with EF-hand domain 1 FUNCTION: May have a role in the recovery or adaptation response of photoreceptors. May have a role in development.; . TISSUE SPECIFICITY: Detected in retina and retinal derived Y-79 retinoblastoma cells. Also found in fetal brain.; unclassifiable (Anatomical System);lung;whole body;ovary;adrenal gland;placenta;testis;parathyroid;brain;skeletal muscle; dorsal root ganglion;testis - interstitial;testis;ciliary ganglion;atrioventricular node; 0.18642 0.09748 -0.159704656 41.90846898 75.066 1.81341 PPEF1-AS1 . . . PPEF1 antisense RNA 1 . . . . . . . . . . . PPEF2 7.34246082496395e-10 0.86978763825233 0.130212361013424 protein phosphatase with EF-hand domain 2 FUNCTION: May play a role in phototransduction. May dephosphorylate photoactivated rhodopsin. May function as a calcium sensing regulator of ionic currents, energy production or synaptic transmission.; . TISSUE SPECIFICITY: Retinal specific.; optic nerve;macula lutea;fovea centralis;choroid;lens;pineal gland;skeletal muscle;retina; superior cervical ganglion;appendix;globus pallidus;atrioventricular node;trigeminal ganglion; 0.37944 0.08962 1.164733225 92.65746638 2139.83122 8.51045 PPFIA1 0.999999874338716 1.25661284309287e-07 1.36278193584083e-19 PTPRF interacting protein alpha 1 FUNCTION: May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000269|PubMed:7796809}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7796809, ECO:0000269|PubMed:9624153}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;pancreas;lung;placenta;hypopharynx;amnion;head and neck;kidney;stomach;thymus; dorsal root ganglion;amygdala;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.12784 0.11244 -1.675620402 2.689313517 2105.88312 8.44787 PPFIA2 0.999975971595094 2.40284049051194e-05 4.07489016520552e-16 PTPRF interacting protein alpha 2 FUNCTION: Alters PTPRF cellular localization and induces PTPRF clustering. May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000269|PubMed:9624153}.; . TISSUE SPECIFICITY: Expressed only in brain. {ECO:0000269|PubMed:9624153}.; unclassifiable (Anatomical System);smooth muscle;choroid;fovea centralis;lens;skeletal muscle;retina;optic nerve;frontal lobe;macula lutea;testis;kidney;brain;cerebellum; amygdala;subthalamic nucleus;superior cervical ganglion;medulla oblongata;occipital lobe;prefrontal cortex;globus pallidus;pons;skeletal muscle;parietal lobe; 0.37736 0.11686 -1.041578376 7.773059684 234.39142 3.30901 PPFIA3 0.99999959495107 4.05048929535138e-07 1.16541780930966e-17 PTPRF interacting protein alpha 3 FUNCTION: May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000269|PubMed:9624153}.; . TISSUE SPECIFICITY: Expressed only in brain. {ECO:0000269|PubMed:9624153}.; unclassifiable (Anatomical System);amygdala;medulla oblongata;heart;tongue;islets of Langerhans;colon;skin;skeletal muscle;retina;uterus;pancreas;prostate;lung;frontal lobe;bone;placenta;testis;head and neck;spleen;kidney;brain;stomach;peripheral nerve; amygdala;whole brain;superior cervical ganglion;cerebellum peduncles;temporal lobe;globus pallidus;trigeminal ganglion;cingulate cortex; 0.15973 0.11130 -1.063626766 7.484076433 3166.8692 10.72789 PPFIA4 0.00151553282447576 0.997131098365531 0.00135336880999314 PTPRF interacting protein alpha 4 FUNCTION: May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed only in the heart, brain, and skeletal muscle. {ECO:0000269|PubMed:9624153}.; unclassifiable (Anatomical System);heart;ovary;cartilage;cerebellum cortex;pineal body;blood;skeletal muscle;retina;bone marrow;uterus;frontal lobe;synovium;brain;cerebellum; whole brain;amygdala;medulla oblongata;occipital lobe;thalamus;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.17878 0.11375 -0.44448505 24.46331682 1473.79951 7.15098 PPFIBP1 2.09888083812757e-12 0.988893075069901 0.0111069249280005 PPFIA binding protein 1 FUNCTION: May regulate the disassembly of focal adhesions. Did not bind receptor-like tyrosine phosphatases type 2A. {ECO:0000269|PubMed:9624153}.; . TISSUE SPECIFICITY: Widely expressed. Absent in liver. {ECO:0000269|PubMed:9624153}.; lymphoreticular;ovary;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;cerebral cortex;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;spinal cord;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.66160 0.11133 -0.50335344 21.80938901 412.52002 4.25274 PPFIBP2 1.42290838281706e-18 0.0719720797265466 0.928027920273453 PPFIA binding protein 2 FUNCTION: May regulate the disassembly of focal adhesions. Did not bind receptor-like tyrosine phosphatases type 2A. {ECO:0000269|PubMed:9624153}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9624153}.; ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;prostate;optic nerve;whole body;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;blood;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland; testis - interstitial;thyroid;testis; 0.12626 0.10279 -0.279250919 33.56923803 1831.97955 7.88761 PPH2 . . . primary pulmonary hypertension 2 . . . . . . . . . . . PPHLN1 7.58102542315877e-05 0.995850209673841 0.00407398007192771 periphilin 1 FUNCTION: Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. In the HUSH complex, contributes to the maintenance of the complex at chromatin (PubMed:26022416). Acts as a transcriptional corepressor and regulates the cell cycle, probably via the HUSH complex (PubMed:15474462, PubMed:17963697). May be involved in epithelial differentiation by contributing to epidermal integrity and barrier formation (Probable). {ECO:0000269|PubMed:15474462, ECO:0000269|PubMed:17963697, ECO:0000269|PubMed:26022416, ECO:0000305|PubMed:12853457}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12853457}.; lymphoreticular;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;adrenal cortex;blood;lens;skeletal muscle;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach;thymus; dorsal root ganglion;medulla oblongata;subthalamic nucleus;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;pons;trigeminal ganglion; 0.10139 0.10008 -0.246069119 36.06982779 79.76425 1.88719 PPIA 0.808049495342876 0.187042740323256 0.00490776433386844 peptidylprolyl isomerase A FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.; . . ovary;salivary gland;parotid gland;intestine;colon;choroid;vein;skin;bone marrow;uterus;prostate;synovium;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;heart;tongue;islets of Langerhans;hypothalamus;pineal body;muscle;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; . 0.16409 0.41273 0.057118534 57.99716914 3.89638 0.14495 PPIAL4A 0.377823123108992 0.478268793952724 0.143908082938283 peptidylprolyl isomerase A like 4A FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in brain, ovary and mammary gland. Moderately expressed in lung, salivary gland, kidney, skin, adipose tissue, intestine and spleen. Weakly expressed in skeletal muscle, liver and stomach. Expressed in pleiomorphic and undifferentiated liposarcomas, osteosarcomas and breast carcinomas. {ECO:0000269|PubMed:11948409}.; . . . . . . 726.86038 5.35450 PPIAL4C . . . peptidylprolyl isomerase A like 4C FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}.; . . . . . . . . . . PPIAL4D . . . peptidylprolyl isomerase A like 4D FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}.; . . . . . . . . . . PPIAL4E . . . peptidylprolyl isomerase A like 4E FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}.; . . . . . . . . . . PPIAL4F . . . peptidylprolyl isomerase A like 4F FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}.; . . . . . . . . . . PPIAL4G 0.606751613079552 0.357396124053854 0.0358522628665933 peptidylprolyl isomerase A like 4G FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}.; . . . . . . 1.324743148 94.0905874 4146.83798 12.78066 PPIAP1 . . . peptidylprolyl isomerase A pseudogene 1 . . . . . . . . . . . PPIAP2 . . . peptidylprolyl isomerase A pseudogene 2 . . . . . . . . . . . PPIAP3 . . . peptidylprolyl isomerase A pseudogene 3 . . . . . . . . . . . PPIAP4 . . . peptidylprolyl isomerase A pseudogene 4 . . . . . . . . . . . PPIAP5 . . . peptidylprolyl isomerase A pseudogene 5 . . . . . . . . . . . PPIAP6 . . . peptidylprolyl isomerase A pseudogene 6 . . . . . . . . . . . PPIAP7 . . . peptidylprolyl isomerase A pseudogene 7 . . . . . . . . . . . PPIAP8 . . . peptidylprolyl isomerase A pseudogene 8 . . . . . . . . . . . PPIAP9 . . . peptidylprolyl isomerase A pseudogene 9 . . . . . . . . . . . PPIAP10 . . . peptidylprolyl isomerase A pseudogene 10 FUNCTION: Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells.; . TISSUE SPECIFICITY: Found in plasma.; . . 0.04842 0.44343 -0.117432389 44.89266336 . . PPIAP11 . . . peptidylprolyl isomerase A pseudogene 11 . . . . . . . . . . . PPIAP13 . . . peptidylprolyl isomerase A pseudogene 13 . . . . . . . . . . . PPIAP14 . . . peptidylprolyl isomerase A pseudogene 14 . . . . . . . . . . . PPIAP15 . . . peptidylprolyl isomerase A pseudogene 15 . . . . . . . . . . . PPIAP16 . . . peptidylprolyl isomerase A pseudogene 16 . . . . . . . . . . . PPIAP17 . . . peptidylprolyl isomerase A pseudogene 17 . . . . . . . . . . . PPIAP18 . . . peptidylprolyl isomerase A pseudogene 18 . . . . . . . . . . . PPIAP19 . . . peptidylprolyl isomerase A pseudogene 19 . . . . . . . . . . . PPIAP20 . . . peptidylprolyl isomerase A pseudogene 20 . . . . . . . . . . . PPIAP21 . . . peptidylprolyl isomerase A pseudogene 21 . . . . . . . . . . . PPIAP22 . . . peptidylprolyl isomerase A pseudogene 22 . . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;cervix;kidney;mammary gland;stomach;aorta;thymus; . . . . . . . PPIAP23 . . . peptidylprolyl isomerase A pseudogene 23 . . . . . . . . . . . PPIAP24 . . . peptidylprolyl isomerase A pseudogene 24 . . . . . . . . . . . PPIAP25 . . . peptidylprolyl isomerase A pseudogene 25 . . . . . . . . . . . PPIAP26 . . . peptidylprolyl isomerase A pseudogene 26 . . . . . . . . . . . PPIAP27 . . . peptidylprolyl isomerase A pseudogene 27 . . . . . . . . . . . PPIAP28 . . . peptidylprolyl isomerase A pseudogene 28 . . . . . . . . . . . PPIAP29 . . . peptidylprolyl isomerase A pseudogene 29 . . . . . . . . . . . PPIAP30 . . . peptidylprolyl isomerase A pseudogene 30 . . . . . . . . . . . PPIAP31 . . . peptidylprolyl isomerase A pseudogene 31 . . . . . . . . . . . PPIAP32 . . . peptidylprolyl isomerase A pseudogene 32 . . . . . . . . . . . PPIAP33 . . . peptidylprolyl isomerase A pseudogene 33 . . . . . . . . . . . PPIB 0.0106515280164213 0.832831133317211 0.156517338666368 peptidylprolyl isomerase B FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.; DISEASE: Osteogenesis imperfecta 9 (OI9) [MIM:259440]: A form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI9 is a severe autosomal recessive form of the disorder. {ECO:0000269|PubMed:19781681, ECO:0000269|PubMed:20089953}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;larynx;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);trophoblast;cartilage;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; uterus;prostate;smooth muscle;lung;adipose tissue;heart;adrenal gland;thyroid;placenta;liver;fetal lung;fetal thyroid; 0.37101 0.40044 -0.339715008 30.06605331 18.15303 0.63258 PPIC 0.000967993093039106 0.583098619552836 0.415933387354125 peptidylprolyl isomerase C FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.; . . medulla oblongata;ovary;colon;skin;uterus;prostate;cochlea;larynx;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;adrenal cortex;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;heart;thyroid;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.13967 0.15696 0.793752871 87.40268931 1495.2395 7.19383 PPID 1.70586248866827e-06 0.656762804631939 0.343235489505572 peptidylprolyl isomerase D FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA- binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. Promotes cell viability in anaplastic lymphoma kinase-positive anaplastic large- cell lymphoma (ALK+ ALCL) cell lines. May be involved in hepatitis C virus (HCV) replication and release. {ECO:0000269|PubMed:11350175, ECO:0000269|PubMed:18708059, ECO:0000269|PubMed:19932913, ECO:0000269|PubMed:21711559, ECO:0000269|PubMed:22681779, ECO:0000269|PubMed:23220213, ECO:0000269|PubMed:9659917}.; . TISSUE SPECIFICITY: Widely expressed.; ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;pituitary gland;testis;amniotic fluid;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach;thymus; amygdala;dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.24497 0.12019 0.77170517 87.00754895 2584.6918 9.51079 PPIE 0.980809839859493 0.0191756868981854 1.44732423219626e-05 peptidylprolyl isomerase E FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing.; . TISSUE SPECIFICITY: Found in all the examined tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;bladder;brain;tonsil;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle; 0.23480 0.10992 -0.427900189 25.14744043 25.82775 0.84067 PPIEL . . . peptidylprolyl isomerase E like pseudogene . . . . . . . . . . . PPIF 0.00518621282700724 0.703347204663335 0.291466582509658 peptidylprolyl isomerase F FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress- induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis. {ECO:0000269|PubMed:19228691, ECO:0000269|PubMed:22726440}.; . . lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; adrenal gland;liver;tumor; 0.24475 0.19897 . . 29.21967 0.93465 PPIG 0.984147328507764 0.0158526563044576 1.51877785244416e-08 peptidylprolyl isomerase G FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;spinal cord;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;medulla oblongata;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex;parietal lobe; 0.64108 0.51829 0.022122107 55.69120075 3812.30735 12.13957 PPIGP1 . . . peptidylprolyl isomerase G pseudogene 1 . . . . . . . . . . . PPIH 0.00475502689084187 0.879955203569871 0.115289769539288 peptidylprolyl isomerase H FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone. {ECO:0000269|PubMed:11823439, ECO:0000269|PubMed:12875835, ECO:0000269|PubMed:9570313}.; . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;heart;islets of Langerhans;hypothalamus;pharynx;blood;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;temporal lobe;white blood cells;skeletal muscle; 0.18461 0.12378 -0.09720619 46.20193442 22.99044 0.76640 PPIHP1 . . . peptidylprolyl isomerase H pseudogene 1 . . . . . . . . . . . PPIHP2 . . . peptidylprolyl isomerase H pseudogene 2 . . . . . . . . . . . PPIL1 0.013003975971324 0.859936241809546 0.12705978221913 peptidylprolyl isomerase like 1 FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing. {ECO:0000269|PubMed:16595688}.; . TISSUE SPECIFICITY: Ubiquitous, with the most abundant expression in heart and skeletal muscle.; . . 0.09855 . 0.103030231 61.2762444 83.62383 1.94484 PPIL1P1 . . . peptidylprolyl isomerase like 1 pseudogene 1 . . . . . . . . . . . PPIL2 0.0274929870468308 0.972408939657616 9.80732955533668e-05 peptidylprolyl isomerase like 2 FUNCTION: May catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins (By similarity). May also function as a chaperone, playing a role in transport to the cell membrane of BSG for instance (PubMed:15946952). May also have a protein ubiquitin ligase activity acting as an E3 ubiquitin protein ligase or as an ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. By mediating 'Lys-48'-linked polyubiquitination of proteins could target them for proteasomal degradation (PubMed:11435423). {ECO:0000250|UniProtKB:Q08752, ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:15946952, ECO:0000303|PubMed:8660300}.; . TISSUE SPECIFICITY: Highest expression in thymus, pancreas and testis. Also detected in heart, placenta, lung, liver, skeletal muscle, kidney, spleen, prostate, ovary, small intestine and colon. Poorly detected in brain and leukocytes. Strong protein expression in lymph node (cortical, paracortical and medullar regions), thyroid (follicular epithelial cells), testis (developing spermatozoa), stomach (cells lining the gastric pit), pancreas, kidney (proximal and distal-tubule cells and collecting duct cells but not in glomeruli), endometrium and colon (goblet cells). Moderate protein expression in spleen, prostate (epithelium and squamous cell carcinomas), placenta and adrenal gland. Weak protein expression in liver, heart, breast, ovary, and lung. No protein expression in brain and bladder. High protein expression in most lymphomas and melanomas. {ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:8660300}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;oesophagus;larynx;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;pineal body;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;heart;fetal brain;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.24149 0.11289 -0.596992387 18.18825195 85.07728 1.96609 PPIL3 0.549646605195737 0.436729126727232 0.0136242680770307 peptidylprolyl isomerase like 3 FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing.; . TISSUE SPECIFICITY: Ubiquitous. Detected at low levels. {ECO:0000269|PubMed:11435694}.; cartilage;heart;ovary;islets of Langerhans;colon;blood;skin;skeletal muscle;bone marrow;uterus;pancreas;prostate;whole body;lung;bone;placenta;testis;germinal center;kidney; . 0.10261 0.09330 0.281220278 71.07808445 1031.16024 6.16831 PPIL4 1.68093009893407e-05 0.992867370689602 0.00711582000940872 peptidylprolyl isomerase like 4 FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Abundantly expressed in kidney but has a ubiquitously low expression pattern in other adult tissues. {ECO:0000269|PubMed:11978968}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;kidney;stomach; uterus;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.28458 0.11780 -0.159704656 41.90846898 84.52811 1.95737 PPIL6 6.30258336517342e-08 0.137211733497767 0.862788203476399 peptidylprolyl isomerase like 6 FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.; . . . . 0.14477 0.10138 -0.249709319 35.74545883 263.88766 3.48573 PPIP5K1 0.102604913232572 0.890272897021375 0.00712218974605327 diphosphoinositol pentakisphosphate kinase 1 FUNCTION: Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis- diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation. Phosphorylates inositol hexakisphosphate (InsP6) at positions 1 or 3 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates at position 1 or 3 PP-InsP5, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Activated when cells are exposed to hyperosmotic stress. {ECO:0000269|PubMed:17412958, ECO:0000269|PubMed:17690096, ECO:0000269|PubMed:17702752}.; . TISSUE SPECIFICITY: Widely expressed, with a higher expression in skeletal muscle, heart and brain. {ECO:0000269|PubMed:17690096}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;bone;thyroid;testis;dura mater;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);meninges;cartilage;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pia mater;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;hypothalamus;temporal lobe;pons;cerebellum; 0.26681 0.09455 . . 99.78494 2.16471 PPIP5K1P1 . . . diphosphoinositol pentakisphosphate kinase 1 pseudogene 1 . . . . . . . . . . . PPIP5K2 4.05311854851164e-10 0.999970537276912 2.94623177756096e-05 diphosphoinositol pentakisphosphate kinase 2 FUNCTION: Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis- diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation. Phosphorylates inositol hexakisphosphate (InsP6) at positions 1 or 3 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates at position 1 or 3 PP-InsP5, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. {ECO:0000269|PubMed:17690096, ECO:0000269|PubMed:17702752}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;spinal cord;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;choroid;fovea centralis;vein;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;trigeminal ganglion; 0.10164 0.11409 -0.194700582 39.24274593 448.80643 4.40617 PPL 1.07536873356769e-25 0.0122705686982477 0.987729431301752 periplakin FUNCTION: Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments. May act as a localization signal in PKB/AKT-mediated signaling. {ECO:0000269|PubMed:9412476}.; . TISSUE SPECIFICITY: Expressed in stratified squamous epithelia and in some other epithelia. {ECO:0000269|PubMed:9412476, ECO:0000269|PubMed:9521878}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;oesophagus;endometrium;larynx;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;cerebellum cortex;islets of Langerhans;oral cavity;lens;breast;pancreas;lung;macula lutea;visual apparatus;liver;hypopharynx;head and neck;cervix;kidney;stomach; adipose tissue;lung;trachea;tongue;placenta;tonsil;skin; 0.21134 0.30050 -0.349655072 29.54706299 9764.33401 21.51445 PPM1A 0.985449561262778 0.0145431088829789 7.3298542433586e-06 protein phosphatase, Mg2+/Mn2+ dependent 1A FUNCTION: Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling. Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. {ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:18930133}.; . . sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;bile duct;breast;lung;adrenal gland;mesenchyma;trabecular meshwork;visual apparatus;liver;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;testis;ciliary ganglion; 0.99375 0.23984 -0.361761279 28.6329323 15.56407 0.55518 PPM1AP1 . . . protein phosphatase, Mg2+/Mn2+ dependent 1A pseudogene 1 . . . . . . . . . . . PPM1B 0.109620710824446 0.884012723751412 0.00636656542414197 protein phosphatase, Mg2+/Mn2+ dependent 1B FUNCTION: Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser- 172'. Plays an important role in the termination of TNF-alpha- mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. {ECO:0000269|PubMed:18930133, ECO:0000269|PubMed:22750291}.; . TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle.; ovary;colon;parathyroid;skin;retina;prostate;whole body;cochlea;endometrium;bone;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;spinal cord;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; amygdala;subthalamic nucleus;superior cervical ganglion;medulla oblongata;prefrontal cortex;trigeminal ganglion;skeletal muscle;cerebellum; 0.99971 0.21173 -0.490397599 22.50530786 53.58105 1.45600 PPM1D 0.00116800419611814 0.996866114376143 0.00196588142773894 protein phosphatase, Mg2+/Mn2+ dependent 1D FUNCTION: Required for the relief of p53-dependent checkpoint mediated cell cycle arrest. Binds to and dephosphorylates 'Ser-15' of TP53 and 'Ser-345' of CHEK1 which contributes to the functional inactivation of these proteins. Mediates MAPK14 dephosphorylation and inactivation (PubMed:21283629). {ECO:0000269|PubMed:15870257, ECO:0000269|PubMed:16311512, ECO:0000269|PubMed:21283629}.; . . ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;optic nerve;whole body;thyroid;iris;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;blood;lens;breast;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach;cerebellum; testis - interstitial;superior cervical ganglion;trigeminal ganglion; 0.61887 0.27303 -0.337894035 30.37272942 108.83575 2.26492 PPM1E 0.973416928914191 0.0265765149665628 6.55611924574725e-06 protein phosphatase, Mg2+/Mn2+ dependent 1E FUNCTION: Protein phosphatase that inactivates multifunctional CaM kinases such as CAMK4 and CAMK2 (By similarity). Dephosphorylates and inactivates PAK. May play a role in the inhibition of actin fiber stress breakdown and in morphological changes driven by TNK2/CDC42. Dephosphorylates PRKAA2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:11864573}.; . . unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;skeletal muscle;skin;uterus;whole body;lung;endometrium;visual apparatus;liver;testis;kidney;brain; . 0.99648 0.09036 -0.291981272 33.20358575 4159.81862 12.80177 PPM1F 0.000267470134913572 0.780259479585635 0.219473050279451 protein phosphatase, Mg2+/Mn2+ dependent 1F FUNCTION: Dephosphorylates and concomitantly deactivates CaM- kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase. Promotes apoptosis.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;kidney;mammary gland;stomach;cerebellum; . 0.94672 0.10663 -0.021969881 52.14673272 1107.57715 6.36090 PPM1G 0.996010385533881 0.00398955191231278 6.25538057998515e-08 protein phosphatase, Mg2+/Mn2+ dependent 1G . . TISSUE SPECIFICITY: Widely expressed. Most abundant in testis, skeletal muscle, and heart.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;larynx;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hypopharynx;amnion;head and neck;kidney;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.99862 0.12794 -0.271755481 34.31823543 16.83702 0.59244 PPM1H 0.855024040523664 0.144876512242805 9.94472335302057e-05 protein phosphatase, Mg2+/Mn2+ dependent 1H FUNCTION: Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal for proteasomal degradation. {ECO:0000269|PubMed:22586611}.; . . unclassifiable (Anatomical System);lung;ovary;bone;blood;skeletal muscle;stomach;bone marrow; subthalamic nucleus;cerebellum peduncles;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.44654 0.10907 0.062575634 58.74026893 63.58305 1.63345 PPM1J 2.30817311285829e-07 0.704933088403571 0.295066680779118 protein phosphatase, Mg2+/Mn2+ dependent 1J . . . unclassifiable (Anatomical System);myocardium;ovary;cartilage;parathyroid;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;frontal lobe;endometrium;placenta;thyroid;macula lutea;testis;kidney; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.39989 0.08381 0.663285274 84.55414013 533.33407 4.71189 PPM1K 0.0454661266650863 0.929105671092171 0.025428202242743 protein phosphatase, Mg2+/Mn2+ dependent 1K FUNCTION: Regulates the mitochondrial permeability transition pore and is essential for cellular survival and development. {ECO:0000269|PubMed:17374715}.; DISEASE: Maple syrup urine disease, mild variant (MSUDMV) [MIM:615135]: A mild form of maple syrup urine disease, a metabolic disorder due to an enzyme defect in the catabolic pathway of the branched-chain amino acids leucine, isoleucine, and valine. Accumulation of these 3 amino acids and their corresponding keto acids leads to encephalopathy and progressive neurodegeneration. Clinical features include mental and physical retardation, feeding problems, and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine. If untreated, maple syrup urine disease can lead to seizures, coma, and death. The disease is often classified by its pattern of signs and symptoms. The most common and severe form of the disease is the classic type, which becomes apparent soon after birth. Variant forms of the disorder become apparent later in infancy or childhood and are typically milder, but they still involve developmental delay and other medical problems if not treated. MSUDMV is characterized by increased plasma levels of branched-chain amino acids (BCAA) apparent at birth. Treatment with a low-protein diet free of BCAA can result in normal psychomotor development and lack of metabolic episodes. {ECO:0000269|PubMed:23086801}. Note=The gene represented in this entry is involved in disease pathogenesis.; . unclassifiable (Anatomical System);myocardium;heart;islets of Langerhans;hypothalamus;spinal cord;adrenal cortex;blood;skin;skeletal muscle;retina;pancreas;frontal lobe;placenta;liver;testis;germinal center;brain;pineal gland;aorta;stomach; amygdala;superior cervical ganglion; 0.99820 0.11400 -0.157884861 42.05590941 158.4555 2.75002 PPM1L 0.570549299339256 0.426977599347905 0.00247310131283952 protein phosphatase, Mg2+/Mn2+ dependent 1L FUNCTION: Acts as a suppressor of the SAPK signaling pathways by associating with and dephosphorylating MAP3K7/TAK1 and MAP3K5, and by attenuating the association between MAP3K7/TAK1 and MAP2K4 or MAP2K6. {ECO:0000269|PubMed:17456047}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, placenta, lung, liver, kidney and pancreas. {ECO:0000269|PubMed:15560375}.; unclassifiable (Anatomical System);lung;tongue;liver;head and neck;brain;skin;skeletal muscle;retina;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.99937 0.16738 0.016664174 55.21939137 45.9557 1.30496 PPM1M 0.0923289257222666 0.869051693642922 0.038619380634811 protein phosphatase, Mg2+/Mn2+ dependent 1M . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;urinary;blood;lens;breast;lung;placenta;macula lutea;liver;alveolus;spleen;kidney;mammary gland;aorta; superior cervical ganglion;white blood cells;whole blood; 0.10570 . 0.196671391 67.19155461 73.26126 1.78820 PPM1N 0.000104897385207125 0.584144980031075 0.415750122583718 protein phosphatase, Mg2+/Mn2+ dependent 1N (putative) . . . unclassifiable (Anatomical System);lung;ovary;placenta;testis;blood;kidney;germinal center;brain; . . . . . 65.29334 1.66266 PPME1 0.92489377029294 0.0750883086570456 1.79210500143955e-05 protein phosphatase methylesterase 1 FUNCTION: Demethylates proteins that have been reversibly carboxymethylated. Demethylates PPP2CB (in vitro) and PPP2CA. Binding to PPP2CA displaces the manganese ion and inactivates the enzyme. {ECO:0000269|PubMed:10318862}.; . . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;mammary gland;stomach; whole brain;amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;prefrontal cortex;globus pallidus;pons;parietal lobe;cingulate cortex;cerebellum; 0.24805 . -0.095386216 46.48502005 36.0072 1.08226 PPOX 0.328331759509175 0.670994980354593 0.000673260136232203 protoporphyrinogen oxidase FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. {ECO:0000269|PubMed:21048046, ECO:0000269|PubMed:23467411, ECO:0000269|PubMed:7713909}.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; unclassifiable (Anatomical System);ovary;islets of Langerhans;parathyroid;uterus;pancreas;lung;endometrium;bone;placenta;visual apparatus;liver;pituitary gland;testis;kidney;brain;mammary gland; fetal liver;superior cervical ganglion;trigeminal ganglion; 0.18959 0.29718 -0.247889024 35.98726115 272.26655 3.53606 PPP1CA 0.941508635503383 0.0584444743956206 4.68901009965072e-05 protein phosphatase 1 catalytic subunit alpha FUNCTION: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). {ECO:0000269|PubMed:17283141, ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:23396208}.; . . lymphoreticular;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; prostate;lung;heart;placenta;thyroid;liver;white blood cells;whole blood;thymus; 0.99591 0.45874 -0.361761279 28.6329323 4.17755 0.15276 PPP1CB 0.997194974203565 0.00280489496229002 1.30834144578399e-07 protein phosphatase 1 catalytic subunit beta FUNCTION: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T- cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). {ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:23396208}.; . . ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; globus pallidus; 0.75832 . -0.09720619 46.20193442 2.60658 0.09519 PPP1CC 0.944905081326266 0.0550545888697244 4.03298040099137e-05 protein phosphatase 1 catalytic subunit gamma FUNCTION: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density- associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T- cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). {ECO:0000269|PubMed:17936702, ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:23396208}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;synovium;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;placenta;head and neck;kidney;stomach;aorta; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.99939 0.29199 -0.031067188 51.03798066 4.80302 0.17490 PPP1R1A 0.00857614104493053 0.798560167357269 0.1928636915978 protein phosphatase 1 regulatory inhibitor subunit 1A FUNCTION: Inhibitor of protein-phosphatase 1. This protein may be important in hormonal control of glycogen metabolism. Hormones that elevate intracellular cAMP increase I-1 activity in many tissues. I-1 activation may impose cAMP control over proteins that are not directly phosphorylated by PKA. Following a rise in intracellular calcium, I-1 is inactivated by calcineurin (or PP2B). Does not inhibit type-2 phosphatases.; . . ovary;sympathetic chain;colon;parathyroid;choroid;fovea centralis;retina;prostate;optic nerve;whole body;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;lung;placenta;hippocampus;visual apparatus;macula lutea;liver;kidney;mammary gland;stomach; amygdala;whole brain;thalamus;medulla oblongata;adipose tissue;tongue;hypothalamus;spinal cord;caudate nucleus;pons;skeletal muscle;fetal brain;thyroid;liver;prefrontal cortex;ciliary ganglion;kidney;cingulate cortex; 0.45369 0.11527 0.613741468 83.06794055 99.3089 2.15704 PPP1R1AP1 . . . protein phosphatase 1 regulatory inhibitor subunit 1A pseudogene 1 . . . . . . . . . . . PPP1R1AP2 . . . protein phosphatase 1 regulatory inhibitor subunit 1A pseudogene 2 . . . . . . . . . . . PPP1R1B 0.082106282395609 0.871830497717204 0.0460632198871866 protein phosphatase 1 regulatory inhibitor subunit 1B FUNCTION: Inhibitor of protein-phosphatase 1.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;iris;pituitary gland;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;mammary gland;stomach;aorta; amygdala;medulla oblongata;prefrontal cortex;caudate nucleus;pons;cingulate cortex;cerebellum; 0.20457 0.47708 0.12689526 63.00424628 217.77532 3.19075 PPP1R1C 0.00253358869301562 0.549871683885073 0.447594727421912 protein phosphatase 1 regulatory inhibitor subunit 1C FUNCTION: Inhibitor of protein-phosphatase 1. Promotes cell growth and cell cycle progress at the G1/S transition. May increase cell susceptibility to TNF-induced apoptosis. {ECO:0000269|PubMed:18310074, ECO:0000269|PubMed:19874272}.; . TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, liver and testis (at protein level).; unclassifiable (Anatomical System);lung;whole body;islets of Langerhans;larynx;thyroid;liver;testis;spleen;head and neck;kidney;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.42339 0.06588 0.035072054 56.2514744 20.49327 0.69754 PPP1R2 0.04270925654256 0.929448060944492 0.0278426825129478 protein phosphatase 1 regulatory inhibitor subunit 2 FUNCTION: Inhibitor of protein-phosphatase 1.; . . ovary;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;thymus; . . 0.13322 0.25917371 70.05779665 27.84526 0.89491 PPP1R2P1 . . . protein phosphatase 1 regulatory inhibitor subunit 2 pseudogene 1 FUNCTION: Inhibitor of protein-phosphatase 1. {ECO:0000250}.; . . . . . . . . . . PPP1R2P2 . . . protein phosphatase 1 regulatory inhibitor subunit 2 pseudogene 2 . . . . . . . . . . . PPP1R2P3 . . . protein phosphatase 1 regulatory inhibitor subunit 2 pseudogene 3 FUNCTION: Inhibitor of protein-phosphatase 1. {ECO:0000269|PubMed:23506001}.; . TISSUE SPECIFICITY: Only detected in spermatozoa, both heads and tails. {ECO:0000269|PubMed:23506001}.; . . . 0.13322 . . . . PPP1R2P4 . . . protein phosphatase 1 regulatory inhibitor subunit 2 pseudogene 4 . . . . . . . . . . . PPP1R2P5 . . . protein phosphatase 1 regulatory inhibitor subunit 2 pseudogene 5 . . . . . . . . . . . PPP1R2P6 . . . protein phosphatase 1 regulatory inhibitor subunit 2 pseudogene 6 . . . . . . . . . . . PPP1R2P8 . . . protein phosphatase 1 regulatory inhibitor subunit 2 pseudogene 8 . . . . . . . . . . . PPP1R2P9 . . . protein phosphatase 1 regulatory inhibitor subunit 2 pseudogene 9 FUNCTION: Functions as a protein phosphatase inhibitor. It inhibits activity of the catalytic subunit of PP1 and weakly inhibits the activity of myosin-associated phosphates. {ECO:0000269|PubMed:11076525}.; . . . . 0.03872 . . . . . PPP1R2P10 . . . protein phosphatase 1 regulatory inhibitor subunit 2 pseudogene 10 . . . . . . . . . . . PPP1R3A 6.58740989250831e-07 0.971097301661024 0.0289020395979871 protein phosphatase 1 regulatory subunit 3A FUNCTION: Seems to act as a glycogen-targeting subunit for PP1. PP1 is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Plays an important role in glycogen synthesis but is not essential for insulin activation of glycogen synthase (By similarity). {ECO:0000250}.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:7926294}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Skeletal muscle and heart. {ECO:0000269|PubMed:9726244}.; unclassifiable (Anatomical System);lung;liver;testis;skeletal muscle; globus pallidus;skeletal muscle; 0.05505 0.18357 2.673484248 98.85586223 3733.96842 11.94067 PPP1R3B 0.0229191412335762 0.766665853179301 0.210415005587123 protein phosphatase 1 regulatory subunit 3B FUNCTION: Acts as a glycogen-targeting subunit for phosphatase PP1. Facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. Suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by PYGL, resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in the liver and, at lower levels, in skeletal muscle, including in vastus lateralis, gastrocnemius and soleus (at protein level). Highest mRNA levels are observed in skeletal muscle, and only moderate levels in liver and heart. Weak expression in placenta and lung. {ECO:0000269|PubMed:11872655, ECO:0000269|PubMed:17555403}.; unclassifiable (Anatomical System);tongue;colon;blood;skin;skeletal muscle;breast;whole body;lung;nasopharynx;placenta;visual apparatus;liver;testis;head and neck;cervix;germinal center;brain;bladder; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.17870 0.13270 0.038710339 56.92380278 558.87707 4.80152 PPP1R3C 0.0368811778240755 0.92880522812113 0.0343135940547942 protein phosphatase 1 regulatory subunit 3C FUNCTION: Acts as a glycogen-targeting subunit for PP1 and regulates its activity. Activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in a variety of cell types. {ECO:0000250|UniProtKB:Q7TMB3, ECO:0000269|PubMed:8985175}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;testis;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;macula lutea;hippocampus;liver;spleen;kidney;mammary gland;aorta; trachea;tongue;skeletal muscle; 0.34460 0.15898 0.084621747 60.31493277 94.15749 2.08719 PPP1R3D 0.0677652743829041 0.734620920262571 0.197613805354525 protein phosphatase 1 regulatory subunit 3D FUNCTION: Seems to act as a glycogen-targeting subunit for PP1. PP1 is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis.; . TISSUE SPECIFICITY: Expressed in all tissues tested. High expression in skeletal muscle and heart.; . . 0.12598 0.10493 . . 31.36039 0.98841 PPP1R3E . . . protein phosphatase 1 regulatory subunit 3E FUNCTION: Acts as a glycogen-targeting subunit for PP1. PP1 is involved in glycogen metabolism and contributes to the activation of glycogen synthase leading to an increase in glycogen synthesis. {ECO:0000269|PubMed:15752363}.; . . . . 0.20502 . . . 138.11018 2.55895 PPP1R3F 0.00474942926878046 0.685075984355342 0.310174586375877 protein phosphatase 1 regulatory subunit 3F FUNCTION: Glycogen-targeting subunit for protein phosphatase 1 (PP1). {ECO:0000269|PubMed:21668450}.; . TISSUE SPECIFICITY: Expressed in brain, skeletal muscle and heart. {ECO:0000269|PubMed:21668450}.; unclassifiable (Anatomical System);heart;islets of Langerhans;fovea centralis;choroid;lens;skin;retina;uterus;breast;pancreas;prostate;optic nerve;lung;placenta;macula lutea;hippocampus;testis;kidney;brain;cerebellum; . 0.38005 . . . 328.52445 3.85421 PPP1R3G . . . protein phosphatase 1 regulatory subunit 3G FUNCTION: Glycogen-targeting subunit for protein phosphatase 1 (PP1). Involved in the regulation of hepatic glycogenesis in a manner coupled to the fasting-feeding cycle and distinct from other glycogen-targeting subunits (By similarity). {ECO:0000250}.; . . . . . . . . 120.56899 2.39246 PPP1R7 0.840144247050338 0.159726402641458 0.000129350308204155 protein phosphatase 1 regulatory subunit 7 FUNCTION: Regulatory subunit of protein phosphatase 1. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:7498485}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;foreskin;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;pineal body;adrenal cortex;lens;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; whole brain;medulla oblongata;occipital lobe;superior cervical ganglion;testis - interstitial;temporal lobe;caudate nucleus;pons;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;parietal lobe;cingulate cortex; 0.08333 0.10006 -0.093566408 46.7386176 26.00104 0.84499 PPP1R8 0.954054369869303 0.0458199416716304 0.000125688459066311 protein phosphatase 1 regulatory subunit 8 FUNCTION: Inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. May also be involved in pre-mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in heart and skeletal muscle, followed by brain, placenta, lung, liver and pancreas. Less abundant in kidney. The concentration and ratio between isoforms is cell-type dependent. Isoform Alpha (>90%) and isoform Beta were found in brain, heart and kidney. Isoform Gamma is mainly found in B-cells and T-lymphocytes, and has been found in 293 embryonic kidney cells. {ECO:0000269|PubMed:10103062, ECO:0000269|PubMed:7499293}.; medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; thalamus;placenta;spinal cord;white blood cells; 0.75742 0.16306 -0.117432389 44.89266336 71.50893 1.76014 PPP1R8P1 . . . protein phosphatase 1 regulatory subunit 8 pseudogene 1 . . . . . . . . . . . PPP1R9A 0.0513404120249266 0.948659275930537 3.12044536234036e-07 protein phosphatase 1 regulatory subunit 9A FUNCTION: Binds to actin filaments (F-actin) and shows cross- linking activity. Binds along the sides of the F-actin. May be involved in neurite formation. Inhibits protein phosphatase 1- alpha activity (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;breast;prostate;optic nerve;lung;frontal lobe;placenta;thyroid;macula lutea;liver;testis;brain; dorsal root ganglion;superior cervical ganglion;prefrontal cortex;atrioventricular node;trigeminal ganglion; 0.43691 0.12794 0.029399861 55.83274357 1975.69062 8.18861 PPP1R9B 0.997286913740502 0.00271306185103834 2.44084593874214e-08 protein phosphatase 1 regulatory subunit 9B FUNCTION: Seems to act as a scaffold protein in multiple signaling pathways. Modulates excitatory synaptic transmission and dendritic spine morphology. Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction. Believed to target protein phosphatase 1/PP1 to dendritic spines, which are rich in F-actin, and regulates its specificity toward ion channels and other substrates, such as AMPA-type and NMDA-type glutamate receptors. Plays a role in regulation of G-protein coupled receptor signaling, including dopamine D2 receptors and alpha- adrenergic receptors. May establish a signaling complex for dopaminergic neurotransmission through D2 receptors by linking receptors downstream signaling molecules and the actin cytoskeleton. Binds to ADRA1B and RGS2 and mediates regulation of ADRA1B signaling. May confer to Rac signaling specificity by binding to both, RacGEFs and Rac effector proteins. Probably regulates p70 S6 kinase activity by forming a complex with TIAM1 (By similarity). Required for hepatocyte growth factor (HGF)- induced cell migration. {ECO:0000250, ECO:0000269|PubMed:19151759}.; . . unclassifiable (Anatomical System);ovary;muscle;blood;parathyroid;skin;retina;bone marrow;lung;frontal lobe;placenta;testis;kidney;brain;cerebellum;thymus; dorsal root ganglion;superior cervical ganglion;skeletal muscle; 0.44393 0.25079 . . 36.43125 1.09138 PPP1R10 0.999999767757527 2.32242472875332e-07 1.48585755843978e-17 protein phosphatase 1 regulatory subunit 10 FUNCTION: Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers (By similarity). {ECO:0000250, ECO:0000269|PubMed:9450550}.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:9450550, ECO:0000269|PubMed:9784381}.; . . 0.43779 0.11047 -0.777005578 12.9747582 89.09354 2.02657 PPP1R10P1 . . . protein phosphatase 1 regulatory subunit 10 pseudogene 1 . . . . . . . . . . . PPP1R11 0.783087010418086 0.2100987398256 0.00681424975631326 protein phosphatase 1 regulatory inhibitor subunit 11 FUNCTION: Inhibitor of protein phosphatase 1. {ECO:0000269|PubMed:9843442}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8781118}.; . . 0.09762 . 0.013025609 54.62962963 22.07553 0.74104 PPP1R11P1 . . . protein phosphatase 1 regulatory inhibitor subunit 11 pseudogene 1 . . . . . . . . . . . PPP1R11P2 . . . protein phosphatase 1 regulatory inhibitor subunit 11 pseudogene 2 . . . . . . . . . . . PPP1R12A 0.999179084030694 0.000820915958339768 1.09659172345228e-11 protein phosphatase 1 regulatory subunit 12A FUNCTION: Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN- dependent suppression of HIF1A activity. {ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:19245366, ECO:0000269|PubMed:20354225}.; . TISSUE SPECIFICITY: Expressed in striated muscles, specifically in type 2a fibers (at protein level). {ECO:0000269|PubMed:20634291}.; myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;thyroid;germinal center;bladder;brain;ciliary body;cartilage;heart;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;developmental;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;testis;artery;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; uterus;occipital lobe;prefrontal cortex;ciliary ganglion;white blood cells;whole blood; 0.98344 0.41772 -0.863377021 10.84571833 112.98192 2.31307 PPP1R12B 0.124454641728848 0.875545286289443 7.19817090427169e-08 protein phosphatase 1 regulatory subunit 12B FUNCTION: Regulates myosin phosphatase activity. Augments Ca(2+) sensitivity of the contractile apparatus. {ECO:0000269|PubMed:11067852, ECO:0000269|PubMed:9570949}.; . TISSUE SPECIFICITY: Detected in skeletal muscle, fetal and adult heart, brain, placenta, kidney, spleen, thymus, pancreas and lung. Isoform 3 and isoform 4 are heart specific. {ECO:0000269|PubMed:11067852, ECO:0000269|PubMed:9570949}.; myocardium;medulla oblongata;smooth muscle;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;oesophagus;larynx;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;artery;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;spinal cord;lens;skeletal muscle;breast;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;pons;atrioventricular node;skin;skeletal muscle;uterus;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.39842 0.10794 -0.857930839 10.95187544 214.85888 3.16168 PPP1R12BP1 . . . protein phosphatase 1 regulatory subunit 12B pseudogene 1 . . . . . . . . . . . PPP1R12BP2 . . . protein phosphatase 1 regulatory subunit 12B pseudogene 2 . . . . . . . . . . . PPP1R12C 0.462120927069352 0.537869226385547 9.84654510128381e-06 protein phosphatase 1 regulatory subunit 12C FUNCTION: Regulates myosin phosphatase activity. {ECO:0000269|PubMed:11399775}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in heart. {ECO:0000269|PubMed:11399775}.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; testis;caudate nucleus;cingulate cortex; 0.29098 0.10482 -1.03794674 7.832035858 344.728 3.93807 PPP1R13B 0.976929374224392 0.0230706242081239 1.56748449091463e-09 protein phosphatase 1 regulatory subunit 13B FUNCTION: Regulator that plays a central role in regulation of apoptosis via its interaction with p53/TP53. Regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes in vivo. {ECO:0000269|PubMed:11684014}.; . TISSUE SPECIFICITY: Reduced expression in breast carcinomas expressing a wild-type TP53 protein. {ECO:0000269|PubMed:11684014}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion; 0.15897 0.10945 -1.789497337 2.241094598 150.56241 2.67866 PPP1R13L 0.00265401837731973 0.994374291527501 0.00297169009517937 protein phosphatase 1 regulatory subunit 13 like FUNCTION: Regulator that plays a central role in regulation of apoptosis and transcription via its interaction with NF-kappa-B and p53/TP53 proteins. Blocks transcription of HIV-1 virus by inhibiting the action of both NF-kappa-B and SP1. Also inhibits p53/TP53 function, possibly by preventing the association between p53/TP53 and ASPP1 or ASPP2, and therefore suppressing the subsequent activation of apoptosis. {ECO:0000269|PubMed:10336463, ECO:0000269|PubMed:12134007, ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:15489900}.; . TISSUE SPECIFICITY: Highly expressed in heart, placenta and prostate. Weakly expressed in brain, liver, skeletal muscle, testis and peripheral blood leukocyte. {ECO:0000269|PubMed:10336463}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;retina;uterus;prostate;endometrium;thyroid;bone;testis;bladder;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.22456 . . . 75.78272 1.82354 PPP1R14A 0.287406516614265 0.628653340718103 0.0839401426676318 protein phosphatase 1 regulatory inhibitor subunit 14A FUNCTION: Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction.; . TISSUE SPECIFICITY: Isoform 1 is detected in aorta and testis. Isoform 2 is detected in aorta. {ECO:0000269|PubMed:11467857}.; myocardium;ovary;colon;parathyroid;choroid;skin;uterus;prostate;frontal lobe;larynx;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;pancreas;lung;placenta;liver;head and neck;spleen;kidney;stomach; medulla oblongata;hypothalamus;testis;parietal lobe; 0.20554 0.18210 . . 44.84943 1.28402 PPP1R14B 0.709204424376776 0.275582303379463 0.0152132722437611 protein phosphatase 1 regulatory inhibitor subunit 14B FUNCTION: Inhibitor of PPP1CA. Has over 50-fold higher inhibitory activity when phosphorylated (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed at low levels. {ECO:0000269|PubMed:8838322}.; ovary;salivary gland;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;larynx;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;blood;skeletal muscle;breast;greater omentum;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; . 0.39527 0.22050 0.057118534 57.99716914 2.32056 0.07933 PPP1R14BP1 . . . protein phosphatase 1 regulatory inhibitor subunit 14B pseudogene 1 . . . . . . . . . . . PPP1R14BP2 . . . protein phosphatase 1 regulatory inhibitor subunit 14B pseudogene 2 . . . . . . . . . . . PPP1R14BP3 . . . protein phosphatase 1 regulatory inhibitor subunit 14B pseudogene 3 . . . . . . . . . . . PPP1R14BP4 . . . protein phosphatase 1 regulatory inhibitor subunit 14B pseudogene 4 . . . . . . . . . . . PPP1R14BP5 . . . protein phosphatase 1 regulatory inhibitor subunit 14B pseudogene 5 . . . . . . . . . . . PPP1R14C 0.00467814206611273 0.681902775209178 0.313419082724709 protein phosphatase 1 regulatory inhibitor subunit 14C FUNCTION: Inhibitor of the PP1 regulatory subunit PPP1CA.; . TISSUE SPECIFICITY: Detected in breast cancer. {ECO:0000269|PubMed:12747765}.; unclassifiable (Anatomical System);cartilage;heart;ovary;tongue;islets of Langerhans;colon;parathyroid;skin;uterus;whole body;lung;thyroid;placenta;hypopharynx;testis;cervix;head and neck;germinal center;kidney;brain;mammary gland;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.14443 0.09724 0.035072054 56.2514744 18.34053 0.63618 PPP1R14D 0.0303416533365849 0.80922708018653 0.160431266476885 protein phosphatase 1 regulatory inhibitor subunit 14D FUNCTION: Inhibitor of PPP1CA. Has inhibitory activity only when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction. {ECO:0000269|PubMed:12974676}.; . TISSUE SPECIFICITY: Detected in colon, intestine, kidney and brain cortex. {ECO:0000269|PubMed:12974676}.; unclassifiable (Anatomical System);placenta;colon;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.19138 . 0.169169615 65.33380514 25.20403 0.82400 PPP1R15A 3.34188774969249e-09 0.171009119026881 0.828990877631231 protein phosphatase 1 regulatory subunit 15A FUNCTION: Recruits the serine/threonine-protein phosphatase PP1 to dephosphorylate the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing TP53 phosphorylation on 'Ser-15'. {ECO:0000269|PubMed:11564868, ECO:0000269|PubMed:12556489, ECO:0000269|PubMed:14635196, ECO:0000269|PubMed:14718519, ECO:0000269|PubMed:8139541}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;white blood cells;trigeminal ganglion; 0.02920 0.19494 2.561357218 98.73790988 6865.2358 17.66280 PPP1R15B 0.161223927951919 0.835586348481864 0.00318972356621702 protein phosphatase 1 regulatory subunit 15B FUNCTION: Maintains low levels of EIF2S1 phosphorylation in unstressed cells by promoting its dephosphorylation by PP1. {ECO:0000250}.; . . . . 0.20190 0.08179 0.734883636 86.29983487 244.79842 3.37420 PPP1R16A 0.0476703373113261 0.947290127203996 0.00503953548467822 protein phosphatase 1 regulatory subunit 16A FUNCTION: Inhibits protein phosphatase 1 activity toward phosphorylase, myosin light chain and myosin substrates. {ECO:0000250}.; . . myocardium;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;cervix;kidney;mammary gland;stomach; thyroid;liver; 0.16096 0.11053 -0.778825328 12.88039632 88.81106 2.02338 PPP1R16B 0.998536940448375 0.00146303279909153 2.67525336459111e-08 protein phosphatase 1 regulatory subunit 16B FUNCTION: Regulator of protein phosphatase 1 (PP1) that acts as a positive regulator of pulmonary endothelial cell (EC) barrier function. Involved in PKA-mediated moesin dephosphorylation which is important in EC barrier protection against thrombin stimulation. Promotes the interaction of PPP1CA with RPSA/LAMR1 and in turn facilitates the dephosphorylation of RPSA/LAMR1. Involved in the regulation of endothelial cell filopodia extension. May be a downstream target for TGF-beta1 signaling cascade in endothelial cells. {ECO:0000269|PubMed:16263087, ECO:0000269|PubMed:18586956}.; . TISSUE SPECIFICITY: Highly expressed in vascular endothelium, CNS, lung, spleen, kidney and testis.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;cerebellum;thymus; whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;kidney;parietal lobe;cingulate cortex;cerebellum; 0.63134 . -0.380166007 27.88393489 45.56998 1.29717 PPP1R17 0.000392906114832172 0.398605741109067 0.601001352776101 protein phosphatase 1 regulatory subunit 17 FUNCTION: Inhibits phosphatase activities of protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) complexes. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in cerebellum.; unclassifiable (Anatomical System);optic nerve;lung;cerebellum cortex;macula lutea;testis;blood;fovea centralis;choroid;lens;brain;retina; superior cervical ganglion;thalamus;cerebellum; 0.68865 0.19414 -0.0274281 51.65723048 1820.69582 7.86990 PPP1R18 0.12120153280798 0.877702509386013 0.00109595780600717 protein phosphatase 1 regulatory subunit 18 FUNCTION: Isoform 1: May target protein phosphatase 1 to F-actin cytoskeleton. {ECO:0000269|PubMed:24434620}.; . TISSUE SPECIFICITY: Isoform 4 is predominantly expressed in leukocytes and spleen. {ECO:0000269|PubMed:17374523}.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;whole blood;bone marrow; 0.15524 . 0.795569043 87.49115357 377.13358 4.09540 PPP1R21 0.000402100492101584 0.999582562249152 1.53372587459815e-05 protein phosphatase 1 regulatory subunit 21 . . . ovary;sympathetic chain;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;oesophagus;larynx;bone;iris;testis;brain;unclassifiable (Anatomical System);lymph node;heart;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;macula lutea;visual apparatus;spleen;head and neck;kidney;stomach;cerebellum; amygdala;whole brain;subthalamic nucleus;superior cervical ganglion;occipital lobe;hypothalamus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.21032 . -1.014084315 8.16230243 189.88472 2.98992 PPP1R26 0.985547303285213 0.0144524011876488 2.95527138300662e-07 protein phosphatase 1 regulatory subunit 26 FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. May positively regulate cell proliferation. {ECO:0000269|PubMed:16053918, ECO:0000269|PubMed:19389623}.; . TISSUE SPECIFICITY: Ubiquitous in normal tissues. Expressed in numerous adenocarcinoma cell lines. {ECO:0000269|PubMed:16053918}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);pharynx;blood;lens;pancreas;lung;cornea;macula lutea;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;aorta; subthalamic nucleus;thalamus;prefrontal cortex;globus pallidus;pons;cingulate cortex; 0.10340 0.10038 0.48857149 79.4821892 2978.84256 10.35088 PPP1R26-AS1 . . . PPP1R26 antisense RNA 1 . . . . . . . . . . . PPP1R26P1 . . . protein phosphatase 1 regulatory subunit 26 pseudogene 1 . . . . . . . . . . . PPP1R26P2 . . . protein phosphatase 1 regulatory subunit 26 pseudogene 2 . . . . . . . . . . . PPP1R26P3 . . . protein phosphatase 1 regulatory subunit 26 pseudogene 3 . . . . . . . . . . . PPP1R26P4 . . . protein phosphatase 1 regulatory subunit 26 pseudogene 4 . . . . . . . . . . . PPP1R26P5 . . . protein phosphatase 1 regulatory subunit 26 pseudogene 5 . . . . . . . . . . . PPP1R27 0.00195516228605964 0.495108336186232 0.502936501527708 protein phosphatase 1 regulatory subunit 27 FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. {ECO:0000269|PubMed:19389623}.; . . prostate;heart;larynx;head and neck; . 0.21329 0.10468 -0.317668748 31.45789101 22.15401 0.74341 PPP1R32 2.68242098295629e-07 0.735922316573548 0.264077415184354 protein phosphatase 1 regulatory subunit 32 . . . medulla oblongata;cartilage;ovary;tongue;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;breast;prostate;lung;bone;hippocampus;liver;testis;spleen;kidney;brain;bladder; testis - interstitial;testis - seminiferous tubule;testis;cerebellum; 0.25583 . 0.736704836 86.32932295 738.23042 5.39199 PPP1R35 0.00198348749453857 0.736096351130777 0.261920161374685 protein phosphatase 1 regulatory subunit 35 FUNCTION: Inhibits PPP1CA phosphatase activity. {ECO:0000269|PubMed:19389623}.; . . unclassifiable (Anatomical System);medulla oblongata;lymph node;heart;ovary;islets of Langerhans;pineal body;colon;parathyroid;blood;skin;retina;uterus;pancreas;lung;bone;thyroid;placenta;visual apparatus;alveolus;testis;cervix;kidney;brain;stomach;thymus; . 0.07875 . . . 40.97399 1.20037 PPP1R36 2.76562693347729e-07 0.742075909022556 0.257923814414751 protein phosphatase 1 regulatory subunit 36 FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. {ECO:0000269|PubMed:19389623}.; . . unclassifiable (Anatomical System);lung;frontal lobe;islets of Langerhans;testis;skeletal muscle; . 0.08312 . 1.10969368 92.05590941 877.30462 5.76659 PPP1R37 . . . protein phosphatase 1 regulatory subunit 37 FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. {ECO:0000269|PubMed:19389623}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;endometrium;larynx;thyroid;pituitary gland;testis;dura mater;germinal center;bladder;brain;unclassifiable (Anatomical System);meninges;heart;islets of Langerhans;lens;pancreas;pia mater;lung;placenta;macula lutea;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;skeletal muscle; . 0.09515 . . 397.32662 4.18702 PPP1R42 0.0127465309535919 0.857422082861175 0.129831386185233 protein phosphatase 1 regulatory subunit 42 FUNCTION: Regulates phosphatase activity of protein phosphatase 1 (PP1) complexes in the testis. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;islets of Langerhans;testis;kidney; superior cervical ganglion;globus pallidus; . . 0.369407109 74.95281906 26.40836 0.85498 PPP2CA 0.985509347938547 0.0144833959316858 7.25612976759733e-06 protein phosphatase 2 catalytic subunit alpha FUNCTION: PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGOL2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at 'Ser-259'. {ECO:0000250, ECO:0000269|PubMed:10801873, ECO:0000269|PubMed:22613722, ECO:0000269|PubMed:9920888}.; . . myocardium;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;placenta;hippocampus;hypopharynx;amnion;head and neck;kidney;stomach;aorta;thymus;cerebellum; . 0.88889 0.29199 -0.251530012 35.42108988 . . PPP2CB 0.622505955129438 0.375894127218171 0.00159991765239104 protein phosphatase 2 catalytic subunit beta FUNCTION: PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. {ECO:0000269|PubMed:2555176}.; . . smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;blood;lens;skeletal muscle;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;aorta;stomach;cerebellum; whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;testis - seminiferous tubule;thyroid;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.71703 0.17050 -0.185391282 39.67916962 5.52078 0.20599 PPP2CBP1 . . . protein phosphatase 2 catalytic subunit beta pseudogene 1 . . . . . . . . . . . PPP2R1A 0.719603752889923 0.280370201658822 2.60454512557187e-05 protein phosphatase 2 regulatory subunit A, alpha FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Required for proper chromosome segregation and for centromeric localization of SGOL1 in mitosis. {ECO:0000269|PubMed:16580887}.; DISEASE: Mental retardation, autosomal dominant 36 (MRD36) [MIM:616362]: A form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:25533962, ECO:0000269|PubMed:26168268}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;myocardium;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;bone;thyroid;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;subthalamic nucleus;heart;cerebellum peduncles;adrenal gland;temporal lobe;globus pallidus;caudate nucleus;parietal lobe;cerebellum; 0.64430 0.28104 -0.183570861 39.95046001 14.15057 0.51225 PPP2R1B 2.18828630617287e-07 0.971511040212911 0.0284887409584586 protein phosphatase 2 regulatory subunit A, beta FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;uterus;prostate;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;pineal gland;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;bile duct;breast;lung;adrenal gland;mesenchyma;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve;thymus; medulla oblongata;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.89057 0.10757 0.088260113 60.56853031 326.84773 3.84397 PPP2R2A 0.959642692100134 0.0403535629585633 3.74494130307269e-06 protein phosphatase 2 regulatory subunit B, alpha FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.; . TISSUE SPECIFICITY: Expressed in all tissues examined. {ECO:0000269|PubMed:1849734}.; lymphoreticular;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; medulla oblongata;superior cervical ganglion;occipital lobe;globus pallidus;atrioventricular node;pons;trigeminal ganglion;parietal lobe; . . -0.339715008 30.06605331 8.43281 0.30800 PPP2R2B 0.900682516546481 0.0992807254055077 3.67580480118039e-05 protein phosphatase 2 regulatory subunit B, beta FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. Within the PP2A holoenzyme complex, isoform 2 is required to promote proapoptotic activity (By similarity). Isoform 2 regulates neuronal survival through the mitochondrial fission and fusion balance (By similarity). {ECO:0000250}.; DISEASE: Spinocerebellar ataxia 12 (SCA12) [MIM:604326]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA12 is an autosomal dominant cerebellar ataxia (ADCA). {ECO:0000269|PubMed:10581021}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Brain.; unclassifiable (Anatomical System);smooth muscle;islets of Langerhans;hypothalamus;sympathetic chain;parathyroid;fovea centralis;retina;lung;frontal lobe;cochlea;placenta;hippocampus;macula lutea;visual apparatus;testis;kidney;brain; whole brain;dorsal root ganglion;amygdala;medulla oblongata;superior cervical ganglion;thalamus;occipital lobe;hypothalamus;atrioventricular node;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.92830 0.24608 -0.736552314 13.93606983 20.01727 0.68270 PPP2R2B-IT1 . . . PPP2R2B intronic transcript 1 . . . . . . . . . . . PPP2R2C 0.564450094959733 0.435018077603676 0.000531827436590723 protein phosphatase 2 regulatory subunit B, gamma FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;lung;trabecular meshwork;placenta;macula lutea;hippocampus;visual apparatus;liver;hypopharynx;spleen;cervix;head and neck;kidney;mammary gland;stomach;thymus; amygdala;whole brain;superior cervical ganglion;occipital lobe;medulla oblongata;thalamus;hypothalamus;temporal lobe;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.71511 0.13746 -0.670411825 15.61689078 11.87458 0.43032 PPP2R2D . . . protein phosphatase 2 regulatory subunit B, delta FUNCTION: B regulatory subunit of protein phosphatase 2A (PP2A) that plays a key role in cell cycle by controlling mitosis entry and exit. The activity of PP2A complexes containing PPP2R2D (PR55- delta) fluctuate during the cell cycle: the activity is high in interphase and low in mitosis. During mitosis, activity of PP2A is inhibited via interaction with phosphorylated ENSA and ARPP19 inhibitors. Within the PP2A complexes, the B regulatory subunits modulate substrate selectivity and catalytic activity, and also may direct the localization of the catalytic enzyme to a particular subcellular compartment (By similarity). {ECO:0000250}.; . . . . 0.68154 0.13376 . . 1391.45075 6.97817 PPP2R2DP1 . . . protein phosphatase 2 regulatory subunit B, delta pseudogene 1 . . . . . . . . . . . PPP2R3A 0.920487875254504 0.0795119528874266 1.71858069647523e-07 protein phosphatase 2 regulatory subunit B'', alpha FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, muscle and kidney.; ovary;colon;parathyroid;skin;uterus;prostate;atrium;whole body;cochlea;endometrium;larynx;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;oral cavity;spinal cord;pharynx;skeletal muscle;bile duct;breast;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;appendix;testis;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.15330 0.13168 0.369203982 74.77589054 3497.45303 11.39036 PPP2R3B 1.71421301526223e-09 0.380205267912545 0.619794730373242 protein phosphatase 2 regulatory subunit B'', beta FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.; . . . . 0.07081 . 0.343511191 73.73790988 2210.9456 8.65627 PPP2R3C 8.05791672286188e-07 0.733315456839694 0.266683737368634 protein phosphatase 2 regulatory subunit B'', gamma FUNCTION: May regulate MCM3AP phosphorylation through phosphatase recruitment. May act as a negative regulator of ABCB1 expression and function through the dephosphorylation of ABCB1 by TFPI2/PPP2R3C complex. May play a role in the activation-induced cell death of B-cells. {ECO:0000250|UniProtKB:Q9JK24, ECO:0000269|PubMed:24333728}.; . TISSUE SPECIFICITY: Ubiquitously expressed in brain and other tissues. {ECO:0000269|PubMed:12167160, ECO:0000269|PubMed:15820313}.; medulla oblongata;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;iris;testis;dura mater;germinal center;artery;brain;unclassifiable (Anatomical System);meninges;lymph node;heart;cartilage;islets of Langerhans;lens;pia mater;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion; 0.17698 0.13240 -0.47017169 23.25430526 14.30653 0.51750 PPP2R4 0.983923153384693 0.0160674815599191 9.36505538751834e-06 protein phosphatase 2A regulatory subunit 4 FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine- protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+) (By similarity). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A. {ECO:0000250, ECO:0000269|PubMed:16916641, ECO:0000269|PubMed:17333320}.; . TISSUE SPECIFICITY: Widely expressed.; medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus;cerebellum; amygdala;whole brain;thalamus;testis - interstitial;temporal lobe;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;parietal lobe;cingulate cortex; 0.09410 0.35334 -0.005381972 53.50908233 46.59488 1.31847 PPP2R5A 0.899520424028407 0.100471904729729 7.67124186473082e-06 protein phosphatase 2 regulatory subunit B', alpha FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.; . TISSUE SPECIFICITY: Widely expressed with the highest expression in heart and skeletal muscle.; umbilical cord;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;aorta;stomach;thymus; uterus corpus;superior cervical ganglion;testis - interstitial;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.72235 0.14785 -0.273576253 33.97027601 91.71546 2.05998 PPP2R5B 0.932458812261463 0.0675275100548528 1.36776836841869e-05 protein phosphatase 2 regulatory subunit B', beta FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The phosphorylated form mediates the interaction between AKT1 and PP2A phosphatase leading to dephosphorylation of AKT1 on the 'Thr-308' and 'Ser-373' residues. {ECO:0000269|PubMed:21329884}.; . TISSUE SPECIFICITY: Highest expression in brain.; medulla oblongata;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;endometrium;thyroid;testis;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pineal body;adrenal cortex;lens;lung;adrenal gland;placenta;macula lutea;liver;alveolus;spleen;kidney;cerebellum; medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;cerebellum peduncles;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.16145 0.10681 -0.538132194 20.26421326 15.72909 0.56074 PPP2R5C 0.997672663482247 0.00232731972723326 1.67905196981771e-08 protein phosphatase 2 regulatory subunit B', gamma FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage- induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation. {ECO:0000269|PubMed:16456541, ECO:0000269|PubMed:17245430}.; . TISSUE SPECIFICITY: Highest levels in heart, skeletal muscle and brain. Lower levels in pancreas, kidney, lung and placenta. Very low levels in liver.; lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;kidney;stomach;aorta;thymus; amygdala;superior cervical ganglion;testis - interstitial;occipital lobe;prefrontal cortex;tumor;ciliary ganglion; 0.16008 0.12741 0.018483465 55.44939844 1821.40468 7.87398 PPP2R5CP . . . protein phosphatase 2 regulatory subunit B', gamma pseudogene . . . . . . . . . . . PPP2R5D 0.997520078948917 0.00247991708434318 3.96673959341833e-09 protein phosphatase 2 regulatory subunit B', delta FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.; DISEASE: Mental retardation, autosomal dominant 35 (MRD35) [MIM:616355]: A form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:25533962, ECO:0000269|PubMed:26168268}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform Delta-2 is widely expressed. Isoform Delta-1 is highly expressed in brain.; lymphoreticular;medulla oblongata;umbilical cord;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;prefrontal cortex;pons;caudate nucleus;trigeminal ganglion;parietal lobe;skeletal muscle;cingulate cortex;cerebellum; 0.85153 0.13082 -0.648365105 16.35999056 13.97572 0.50675 PPP2R5E 0.999433463999183 0.000566533351254608 2.64956261693488e-09 protein phosphatase 2 regulatory subunit B', epsilon FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;meninges;cartilage;small intestine;heart;islets of Langerhans;adrenal cortex;blood;lens;breast;pia mater;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;thymus; . 0.55655 0.14896 -0.405853867 26.23260203 8.32866 0.30490 PPP3CA 0.998148788702111 0.00185120168974258 9.60814601723999e-09 protein phosphatase 3 catalytic subunit alpha FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase. Many of the substrates contain a PxIxIT motif. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1. {ECO:0000269|PubMed:15671020, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:18838687}.; . . ovary;sympathetic chain;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;amygdala;heart;cartilage;pineal body;pharynx;blood;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;cornea;placenta;hippocampus;kidney;aorta;stomach;thymus; whole brain;amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;cerebellum peduncles;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.91458 0.30319 -0.427900189 25.14744043 6.37885 0.23918 PPP3CB 0.9997036494233 0.000296350030296658 5.4640346016076e-10 protein phosphatase 3 catalytic subunit beta FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.; . . medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;gall bladder;heart;cartilage;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;alveolus;liver;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;aorta;stomach;thymus; dorsal root ganglion;amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.76042 0.18519 -0.141298762 42.87567823 21.40368 0.72159 PPP3CB-AS1 . . . PPP3CB antisense RNA 1 (head to head) . . . . . . . . . . . PPP3CC 0.0166246432473754 0.983167924655561 0.000207432097063908 protein phosphatase 3 catalytic subunit gamma FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.; . TISSUE SPECIFICITY: Testis.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;spleen;kidney;aorta;thymus; testis - interstitial;testis - seminiferous tubule;testis;white blood cells;skeletal muscle; 0.16547 0.16092 0.52918614 80.81505072 161.32852 2.77392 PPP3R1 0.889820219565523 0.109032029436134 0.00114775099834318 protein phosphatase 3 regulatory subunit B, alpha FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.; . . unclassifiable (Anatomical System);amygdala;heart;ovary;colon;skin;retina;breast;uterus;pancreas;prostate;whole body;lung;frontal lobe;placenta;hippocampus;testis;germinal center;kidney;brain;stomach; amygdala;dorsal root ganglion;occipital lobe;superior cervical ganglion;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cerebellum; . . 0.079165051 59.43029016 . . PPP3R2 0.0476655036055107 0.68051379155538 0.27182070483911 protein phosphatase 3 regulatory subunit B, beta FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:15865209}.; . . 0.17967 . -0.007201372 53.19061099 29.43246 0.94127 PPP4C 0.759585900442172 0.240011001371988 0.000403098185839583 protein phosphatase 4 catalytic subunit FUNCTION: Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of histone acetylation, DNA damage checkpoint signaling, NF-kappa-B activation and cell migration. The PPP4C- PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on Ser-140 (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair. Dephosphorylates NDEL1 at CDK1 phosphorylation sites and negatively regulates CDK1 activity in interphase (By similarity). In response to DNA damage, catalyzes RPA2 dephosphorylation, an essential step for DNA repair since it allows the efficient RPA2-mediated recruitment of RAD51 to chromatin. {ECO:0000250, ECO:0000269|PubMed:11698396, ECO:0000269|PubMed:12668731, ECO:0000269|PubMed:12934076, ECO:0000269|PubMed:1336397, ECO:0000269|PubMed:15805470, ECO:0000269|PubMed:18347064, ECO:0000269|PubMed:18487071, ECO:0000269|PubMed:18614045, ECO:0000269|PubMed:18758438, ECO:0000269|PubMed:20154705}.; . . myocardium;medulla oblongata;smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;amniotic fluid;germinal center;brain;tonsil;heart;cartilage;urinary;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;duodenum;hypopharynx;head and neck;kidney;stomach; lung;placenta;liver;white blood cells;whole blood;thymus; 0.67715 0.19444 -0.119252484 44.53880632 2.17485 0.07232 PPP4R1 0.998557751833321 0.00144224812336986 4.33092572727025e-11 protein phosphatase 4 regulatory subunit 1 FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4. May play a role in regulation of cell division in renal glomeruli. The PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. {ECO:0000269|PubMed:15805470}.; . TISSUE SPECIFICITY: Widely expressed with high expression in cultured mesangial cells. Isoform 1 and isoform 2 are expressed in renal tissues. {ECO:0000269|PubMed:11729228}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;placenta;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;testis; 0.21720 0.10891 0.091899012 60.68058504 824.4267 5.63052 PPP4R1-AS1 . . . PPP4R1 antisense RNA 1 . . . . . . . . . . . PPP4R1L . . . protein phosphatase 4 regulatory subunit 1 like (pseudogene) FUNCTION: May be a regulatory subunit of serine/threonine-protein phosphatase 4.; . . unclassifiable (Anatomical System);lymph node;lung;ovary;bone;liver;testis;colon;cervix;kidney;skin;stomach; dorsal root ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . . . 1076.00834 6.28755 PPP4R2 0.98805629012284 0.011939194014327 4.51586283295439e-06 protein phosphatase 4 regulatory subunit 2 FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers. Its interaction with the SMN complex leads to enhance the temporal localization of snRNPs, suggesting a role of PPP4C in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair. Mediates RPA2 dephosphorylation by recruiting PPP4C to RPA2 in a DNA damage-dependent manner. RPA2 dephosphorylation is required for the efficient RPA2-mediated recruitment of RAD51 to chromatin following double strand breaks, an essential step for DNA repair. {ECO:0000269|PubMed:10769191, ECO:0000269|PubMed:12668731, ECO:0000269|PubMed:18614045, ECO:0000269|PubMed:20154705}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12668731}.; ovary;salivary gland;intestine;colon;skin;retina;uterus;prostate;whole body;frontal lobe;larynx;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.29004 0.09559 0.218717575 68.27081859 267.16019 3.50459 PPP4R3A . . . protein phosphatase 4 regulatory subunit 3A FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4. May regulate the activity of PPP4C at centrosomal microtubule organizing centers. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX) generated during DNA replication and required for DNA DSB repair. {ECO:0000269|PubMed:18614045}.; . . . . 0.84274 . -0.648365105 16.35999056 . . PPP4R3B . . . protein phosphatase 4 regulatory subunit 3B FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers.; . TISSUE SPECIFICITY: Moderately expressed in tissues and specific brain regions examined. {ECO:0000269|PubMed:10718198}.; . . 0.85781 0.10544 -0.50880549 21.72682236 . . PPP4R3CP . . . protein phosphatase 4 regulatory subunit 3C, pseudogene . . . . . . . . . . . PPP4R4 0.00567425479283036 0.994325406692499 3.3851467021294e-07 protein phosphatase 4, regulatory subunit 4 FUNCTION: Putative regulatory subunit of serine/threonine-protein phosphatase 4.; . . unclassifiable (Anatomical System);breast;uterus;lung;heart;endometrium;iris;testis;skin; thalamus;superior cervical ganglion;testis - interstitial;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.10634 0.08878 -1.085675268 7.147912243 115.24346 2.33468 PPP5C 0.999092990117994 0.000907001540825106 8.34118119645574e-09 protein phosphatase 5 catalytic subunit FUNCTION: Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT. Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses. Participates in the control of DNA damage response mechanisms such as checkpoint activation and DNA damage repair through, for instance, the regulation ATM/ATR-signaling and dephosphorylation of PRKDC and TP53BP1. Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress. Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function. Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1. Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E. May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels. Dephosphorylates and may play a role in the regulation of TAU/MAPT. Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2. {ECO:0000269|PubMed:14734805, ECO:0000269|PubMed:14764652, ECO:0000269|PubMed:14871926, ECO:0000269|PubMed:15383005, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16260606, ECO:0000269|PubMed:16790549, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:19948726, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:22399290, ECO:0000269|PubMed:22781750, ECO:0000269|PubMed:23102700, ECO:0000269|PubMed:9000529}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15546861}.; lymphoreticular;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;brain;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;blood;lens;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach; superior cervical ganglion;trigeminal ganglion; 0.58582 0.16834 -0.66859065 15.76433121 22.72261 0.76031 PPP5D1 0.0393450229909042 0.645664407825672 0.314990569183424 PPP5 tetratricopeptide repeat domain containing 1 . . . . . . . . . 36.38344 1.09052 PPP6C 0.988609353693385 0.0113866259687912 4.02033782394649e-06 protein phosphatase 6 catalytic subunit FUNCTION: Catalytic subunit of protein phosphatase 6 (PP6). PP6 is a component of a signaling pathway regulating cell cycle progression in response to IL2 receptor stimulation. N-terminal domain restricts G1 to S phase progression in cancer cells, in part through control of cyclin D1. Downregulates MAP3K7 kinase activation of the IL1 signaling pathway by dephosphorylation of MAP3K7. {ECO:0000269|PubMed:10227379, ECO:0000269|PubMed:17079228, ECO:0000269|PubMed:17568194, ECO:0000269|PubMed:9013334}.; . TISSUE SPECIFICITY: Ubiquitously expressed in all tissues tested with highest expression levels in testis, heart, kidney, brain, stomach, liver and skeletal muscle and lowest in placenta, lung colon and spleen. {ECO:0000269|PubMed:16769727, ECO:0000269|PubMed:9013334}.; . . 0.57043 0.33817 -0.249709319 35.74545883 19.59249 0.67232 PPP6CP . . . protein phosphatase 6 catalytic subunit pseudogene . . . . . . . . . . . PPP6R1 0.997854505544281 0.00214549166968823 2.78603055508342e-09 protein phosphatase 6 regulatory subunit 1 FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. Involved in the PP6- mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. {ECO:0000269|PubMed:16769727}.; . TISSUE SPECIFICITY: Ubiquitous with higher expression in testis. {ECO:0000269|PubMed:16769727}.; . . 0.16523 0.11824 0.121225147 62.22576079 190.13458 2.99301 PPP6R2 0.718789474101901 0.281209449972184 1.07592591445501e-06 protein phosphatase 6 regulatory subunit 2 FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. Involved in the PP6- mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. {ECO:0000269|PubMed:16769727}.; . TISSUE SPECIFICITY: Ubiquitously expressed with strongest expression in the testis followed by liver, heart, kidney, brain and placenta. {ECO:0000269|PubMed:16769727}.; medulla oblongata;smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;brain;tonsil;cartilage;heart;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;thymus; occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;testis;trigeminal ganglion;cingulate cortex;cerebellum; 0.16066 0.08929 0.701733761 85.31493277 303.35039 3.71149 PPP6R2P1 . . . protein phosphatase 6 regulatory subunit 2 pseudogene 1 . . . . . . . . . . . PPP6R3 0.995714713640604 0.00428528623452791 1.24867821003816e-10 protein phosphatase 6 regulatory subunit 3 FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. May have an important role in maintaining immune self-tolerance. {ECO:0000269|PubMed:11401438, ECO:0000269|PubMed:16769727}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, placenta, heart, pancreas, testis, brain, lung, liver, kidney, spleen, thymus, prostate, small intestine, colon and leukocytes. {ECO:0000269|PubMed:11401438, ECO:0000269|PubMed:16769727}.; smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;gall bladder;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;oesophagus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;cerebellum;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.62710 0.09663 0.044168103 57.40740741 208.85481 3.11913 PPRC1 0.999999327553735 6.72446265385889e-07 4.00617375263138e-17 peroxisome proliferator-activated receptor gamma, coactivator-related 1 FUNCTION: Acts as a coactivator during transcriptional activation of nuclear genes related to mitochondrial biogenesis and cell growth. Involved in the transcription coactivation of CREB and NRF1 target genes. {ECO:0000269|PubMed:11340167, ECO:0000269|PubMed:16908542}.; . TISSUE SPECIFICITY: Strongly expressed in heart and skeletal muscle, moderately in lung, placenta, intestine, liver, kidney, spleen, thymus, colon and brain. Also expressed in several oncocytic thyroid tumors. {ECO:0000269|PubMed:11340167, ECO:0000269|PubMed:14550271}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;pons; 0.43087 0.68462 0.437169176 77.45930644 513.19932 4.63632 PPT1 3.75207213169725e-05 0.826491751841536 0.173470727437148 palmitoyl-protein thioesterase 1 FUNCTION: Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.; DISEASE: Ceroid lipofuscinosis, neuronal, 1 (CLN1) [MIM:256730]: A form of neuronal ceroid lipofuscinosis with variable age at onset. Infantile, late-infantile, juvenile, and adult onset have been reported. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment pattern seen most often in CLN1 is referred to as granular osmiophilic deposits (GROD). {ECO:0000269|PubMed:11506414, ECO:0000269|PubMed:19201763, ECO:0000269|PubMed:21990111, ECO:0000269|PubMed:7637805, ECO:0000269|PubMed:9425237, ECO:0000269|PubMed:9664077}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.33940 0.58260 -0.159704656 41.90846898 659.10425 5.14769 PPT2 0.772683334522566 0.22697337143605 0.000343294041384009 palmitoyl-protein thioesterase 2 FUNCTION: Removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA. Has the highest S- thioesterase activity for the acyl groups palmitic and myristic acid followed by other short- and long-chain acyl substrates. However, because of structural constraints, is unable to remove palmitate from peptides or proteins. {ECO:0000269|PubMed:10417332, ECO:0000269|PubMed:12855696, ECO:0000269|PubMed:9341199}.; . TISSUE SPECIFICITY: Broadly expressed, with highest levels in skeletal muscle. {ECO:0000269|PubMed:9341199}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;bile duct;pancreas;lung;placenta;visual apparatus;macula lutea;hippocampus;liver;spleen;kidney;mammary gland;stomach; . . . 0.25917371 70.05779665 1203.89127 6.57351 PPT2-EGFL8 . . . PPT2-EGFL8 readthrough (NMD candidate) . . . . . . . . . 416.9395 4.27288 PPTC7 0.354852283261299 0.632415015337095 0.0127327014016057 PTC7 protein phosphatase homolog . . . myocardium;ovary;colon;skin;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;larynx;thyroid;bone;testis;dura mater;germinal center;gall bladder;unclassifiable (Anatomical System);meninges;heart;islets of Langerhans;skeletal muscle;bile duct;breast;pia mater;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; . 0.84262 0.10997 -0.207437529 38.2814343 526.26611 4.68242 PPWD1 0.0317857747802877 0.968135444738663 7.87804810496098e-05 peptidylprolyl isomerase domain and WD repeat containing 1 FUNCTION: Putative peptidylprolyl isomerase (PPIase). PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;pineal body;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;skeletal muscle; 0.42123 0.10787 -0.690637458 15.12149092 57.12138 1.52264 PPY 0.563418203683469 0.387900228897128 0.0486815674194027 pancreatic polypeptide FUNCTION: Pancreatic hormone is synthesized in pancreatic islets of Langerhans and acts as a regulator of pancreatic and gastrointestinal functions.; . . unclassifiable (Anatomical System);pancreas;islets of Langerhans;spleen; beta cell islets;trigeminal ganglion; 0.17859 0.28615 0.369407109 74.95281906 67.73292 1.70257 PPY2P . . . pancreatic polypeptide 2, pseudogene . . . . . 0.16873 . . . . . PQBP1 0.59284411367679 0.397441487907889 0.00971439841532104 polyglutamine binding protein 1 FUNCTION: Probably functions as scaffold protein that is part of numerous complexes and thereby plays a role in pre-mRNA splicing, transcription regulation and neuron development. Required for normal alternative splicing of target pre-mRNA species (PubMed:23512658). May suppress the ability of POU3F2 to transactivate the DRD1 gene in a POU3F2 dependent manner. Can activate transcription directly or via association with the transcription machinery. May be involved in ATXN1 mutant-induced cell death. The interaction with ATXN1 mutant reduces levels of phosphorylated RNA polymerase II large subunit. {ECO:0000269|PubMed:10198427, ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:12062018, ECO:0000269|PubMed:20410308, ECO:0000269|PubMed:23512658}.; DISEASE: Renpenning syndrome 1 (RENS1) [MIM:309500]: A X-linked mental retardation syndrome characterized by mental retardation, microcephaly, short stature, and small testes. The craniofacies tends to be narrow and tall with upslanting palpebral fissures, abnormal nasal configuration, cupped ears, and short philtrum. The nose may appear long or bulbous, with overhanging columella. Less consistent manifestations include ocular colobomas, cardiac malformations, cleft palate, and anal anomalies. {ECO:0000269|PubMed:14634649, ECO:0000269|PubMed:16740914}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed with high level in heart, skeletal muscle, pancreas, spleen, thymus, prostate, ovary, small intestine and peripheral blood leukocytes. {ECO:0000269|PubMed:10198427, ECO:0000269|PubMed:10332029}.; lymphoreticular;ovary;umbilical cord;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;placenta;head and neck;kidney;stomach;cerebellum; subthalamic nucleus;superior cervical ganglion;temporal lobe;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12360 0.15801 -0.031067188 51.03798066 17.51809 0.61463 PQBP4 . . . polyglutamine binding protein 4 . . . . . . . . . . . PQLC1 0.000252469088329691 0.533328868682219 0.466418662229452 PQ loop repeat containing 1 . . . myocardium;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;bile duct;pancreas;lung;epididymis;placenta;hippocampus;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;subthalamic nucleus;testis - interstitial;liver;testis;globus pallidus;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.26065 . -0.314027422 31.9297004 85.63008 1.97413 PQLC1P1 . . . PQ loop repeat containing 1 pseudogene 1 . . . . . . . . . . . PQLC1P2 . . . PQ loop repeat containing 1 pseudogene 2 . . . . . . . . . . . PQLC2 0.000146809008866195 0.864831955576048 0.135021235415086 PQ loop repeat containing 2 FUNCTION: Amino acid transporter that specifically mediates the pH-dependent export of the cationic amino acids arginine, histidine and lysine from lysosomes. {ECO:0000269|PubMed:22822152, ECO:0000269|PubMed:23169667}.; . . . . 0.12488 . 0.174625237 65.9648502 497.56252 4.58305 PQLC2L . . . PQ loop repeat containing 2-like . . . . . 0.10534 . 0.347360312 73.97381458 . . PQLC3 6.74909232375959e-07 0.148675565500962 0.851323759589805 PQ loop repeat containing 3 . . . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;heart;cartilage;hypothalamus;bile duct;pancreas;lung;placenta;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion; 0.18968 . -0.05129383 49.75819769 78.38843 1.86837 PR@ . . . proline-rich protein gene cluster . . . . . . . . . . . PRAC1 0.00177992300773383 0.281200116641063 0.717019960351204 prostate cancer susceptibility candidate 1 . . TISSUE SPECIFICITY: Highly expressed in prostate, rectum, and distal colon, and weakly expressed in bladder. Expressed in prostate cancer cell lines. {ECO:0000269|PubMed:11340635}.; . . 0.03945 . 0.457594962 78.16112291 29.86582 0.95314 PRAC2 . . . prostate cancer susceptibility candidate 2 . . TISSUE SPECIFICITY: Highly expressed in prostate and testis. Also detected in placenta, muscle, colon, peripheral blood leukocytes and skin. {ECO:0000269|PubMed:12746837}.; . . . . . . . . PRADC1 3.3061098634495e-07 0.0998816427353329 0.900118026653681 protease-associated domain containing 1 . . TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart and liver. Expressed at intermediate level in kidney. {ECO:0000269|PubMed:15498570}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; . 0.43379 0.12378 0.03689118 56.64071715 147.70571 2.64832 PRADC1P1 . . . protease-associated domain containing 1 pseudogene 1 . . . . . . . . . . . PRAF2 0.65127647545626 0.32334631235136 0.0253772121923799 PRA1 domain family member 2 FUNCTION: May be involved in ER/Golgi transport and vesicular traffic. Plays a proapoptic role in cerulenin-induced neuroblastoma apoptosis. {ECO:0000269|PubMed:17975142, ECO:0000269|PubMed:18395978}.; . TISSUE SPECIFICITY: Strong expression in the brain, small intestine, lung, spleen, and pancreas as well as in tumor tissues of the breast, colon, lung and ovary, with a weaker expression in normal tissues of the same patient. High expression in neuroblastic tumors. Strongly expressed in Purkinje cells and more moderately in cells of the molecular and the granular layers in the cerebellum. Detected in neuronal cells, but not in non- neuronal cells in the cerebral cortex, hippocampus, and lateral ventricles. {ECO:0000269|PubMed:16481131, ECO:0000269|PubMed:17975142, ECO:0000269|PubMed:18395978}.; . . 0.17118 0.10424 . . 13.4772 0.48982 PRAM1 0.00762489575795408 0.977092730820432 0.0152823734216138 PML-RARA regulated adaptor molecule 1 FUNCTION: May be involved in myeloid differentiation. May be involved in integrin signaling in neutrophils. Binds to PtdIns(4)P.; . TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes and bone marrow. Expressed in monocytes, and to a lesser extent in granulocytes and lymphocytes. Not expressed in non hematopoietic tissues except in lung. {ECO:0000269|PubMed:11301322}.; unclassifiable (Anatomical System);lung;spleen;blood;thymus;bone marrow; bone marrow; 0.07212 0.09413 0.780798785 87.24345364 1485.44258 7.17177 PRAME 0.000838035154210176 0.933292454639504 0.0658695102062857 preferentially expressed antigen in melanoma FUNCTION: Functions as a transcriptional repressor, inhibiting the signaling of retinoic acid through the retinoic acid receptors RARA, RARB and RARG. Prevents retinoic acid-induced cell proliferation arrest, differentiation and apoptosis. {ECO:0000269|PubMed:16179254}.; . TISSUE SPECIFICITY: Expressed in testis. Detected in samples of kidney, brain and skin. {ECO:0000269|PubMed:9047241}.; . . 0.03338 0.14058 0.268267497 70.64166077 198.16197 3.04150 PRAMEF1 0.0981051636001553 0.866728021575149 0.0351668148246952 PRAME family member 1 . . . testis; . 0.09477 . 1.668219306 96.30219391 173.2434 2.86530 PRAMEF2 0.000567609686510291 0.708417519070975 0.291014871242514 PRAME family member 2 . . . testis; . 0.07552 . 5.208541975 99.84076433 3268.27865 10.91295 PRAMEF4 0.0746095246056682 0.872447590549004 0.0529428848453282 PRAME family member 4 . . . unclassifiable (Anatomical System); . 0.14569 . 3.532159363 99.48100967 1356.98129 6.91114 PRAMEF5 . . . PRAME family member 5 . . . . . 0.11414 . . . 0.18894 0.00378 PRAMEF6 0.691325858232332 0.290700296556954 0.0179738452107144 PRAME family member 6 . . . unclassifiable (Anatomical System); . 0.11108 . . . 121.69407 2.40249 PRAMEF7 0.17686296313217 0.644231740077447 0.178905296790383 PRAME family member 7 . . . . . 0.07230 . . . 223.95325 3.23589 PRAMEF8 . . . PRAME family member 8 . . . . . . . . . . . PRAMEF9 . . . PRAME family member 9 . . . . . . . . . . . PRAMEF10 0.875594718751663 0.122834937336318 0.00157034391201928 PRAME family member 10 . . . . . 0.03923 . . . 578.96094 4.87594 PRAMEF11 0.285437974687136 0.692826457822496 0.0217355674903683 PRAME family member 11 . . . unclassifiable (Anatomical System); . . . . . 565.11976 4.82776 PRAMEF12 3.89692512946575e-06 0.369464079984044 0.630532023090827 PRAME family member 12 . . . . . 0.05788 . 1.161078613 92.64567115 451.59604 4.41782 PRAMEF13 0.529422081197501 0.409745836630707 0.0608320821717919 PRAME family member 13 . . . . . . . . . 357.16307 4.00457 PRAMEF14 0.55964161278638 0.390422321517745 0.0499360656958752 PRAME family member 14 . . . . . 0.07609 . . . 11.01906 0.39930 PRAMEF15 . . . PRAME family member 15 . . . unclassifiable (Anatomical System); . . . . . . . PRAMEF17 0.790929575854879 0.202899904823131 0.00617051932199048 PRAME family member 17 . . . . . 0.02646 . . . 23.20446 0.77488 PRAMEF18 . . . PRAME family member 18 . . . . . . . . . 287.00244 3.62980 PRAMEF19 0.583094142263464 0.374397128999757 0.0425087287367788 PRAME family member 19 . . . . . 0.05953 . . . 3.64274 0.13394 PRAMEF20 . . . PRAME family member 20 . . . . . 0.06893 . . . 9.32078 0.34198 PRAMEF22 0.617146896404532 0.349677012309516 0.0331760912859517 PRAME family member 22 . . . . . . . . . 216.18972 3.17550 PRAMEF25 . . . PRAME family member 25 . . . . . . . . . . . PRAMEF26 . . . PRAME family member 26 . . . . . . . . . . . PRAMEF27 . . . PRAME family member 27 . . . . . . . . . . . PRAMEF28 . . . PRAME family member 28 . . . . . . . . . . . PRAMEF29P . . . PRAME family member 29, pseudogene . . . . . . . . . . . PRAMEF30P . . . PRAME family member 30, pseudogene . . . . . . . . . . . PRAMEF31P . . . PRAME family member 31, pseudogene . . . . . . . . . . . PRAMEF32P . . . PRAME family member 32, pseudogene . . . . . . . . . . . PRAMEF33P . . . PRAME family member 33, pseudogene . . . . . . . . . . . PRAMEF34P . . . PRAME family member 34, pseudogene . . . . . . . . . . . PRAMEF35P . . . PRAME family member 35, pseudogene . . . . . . . . . . . PRAMEF36P . . . PRAME family member 36, pseudogene . . . . . . . . . . . PRAMENP . . . PRAME N-terminal-like, pseudogene . . . . . . . . . . . PRAP1 0.000246548833965658 0.528261857223324 0.47149159394271 proline-rich acidic protein 1 FUNCTION: May play an important role in maintaining normal growth homeostasis in epithelial cells. {ECO:0000269|PubMed:14583459}.; . TISSUE SPECIFICITY: Abundantly expressed in the epithelial cells of the liver, kidney, gastrointestinal tract and cervix. Significantly down-regulated in hepatocellular carcinoma and right colon adenocarcinoma compared with the respective adjacent normal tissues. Expressed in epididymis (at protein level). {ECO:0000269|PubMed:14583459, ECO:0000269|PubMed:20736409}.; . . 0.08788 0.07389 0.483275131 79.25218212 . . PRB1 2.09216771553037e-05 0.477852485540648 0.522126592782197 proline-rich protein BstNI subfamily 1 . . . unclassifiable (Anatomical System);lung;salivary gland;skeletal muscle; . . . 0.305084559 72.22811984 318.00442 3.78677 PRB2 2.87656217860537e-14 0.00973359357594469 0.990266406424027 proline-rich protein BstNI subfamily 2 . . . . . . . 1.932845308 97.48171739 718.49848 5.32110 PRB3 2.57026606514489e-07 0.290048959411042 0.709950783562351 proline-rich protein BstNI subfamily 3 FUNCTION: Acts as a receptor for the Gram-negative bacterium F.nucleatum. {ECO:0000269|PubMed:1894623}.; . . larynx;salivary gland;thyroid;head and neck;skeletal muscle; thalamus;trachea;salivary gland;thymus; 0.11739 . . . 228.06158 3.26170 PRB4 8.85269506815037e-08 0.165369217593938 0.834630693879111 proline-rich protein BstNI subfamily 4 . . . . . . . 1.352234299 94.36777542 885.28057 5.79602 PRC1 0.015975839505285 0.984015149072859 9.01142185616785e-06 protein regulator of cytokinesis 1 FUNCTION: Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression (PubMed:17409436). {ECO:0000269|PubMed:12082078, ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:17409436, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:20691902, ECO:0000269|PubMed:9885575}.; . TISSUE SPECIFICITY: Overexpressed in bladder cancer cells (PubMed:17409436). {ECO:0000269|PubMed:17409436}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;gum;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;muscle;bile duct;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;thymus; testis - interstitial;fetal liver;testis - seminiferous tubule;tumor;testis; 0.68082 0.15466 -0.200157416 39.11299835 294.41154 3.66477 PRC1-AS1 . . . PRC1 antisense RNA 1 . . . . . . . . . . . PRCC 0.921293121521907 0.0786073025189582 9.95759591352894e-05 papillary renal cell carcinoma (translocation-associated) FUNCTION: May regulate cell cycle progression through interaction with MAD2L2. {ECO:0000269|PubMed:11717438}.; . TISSUE SPECIFICITY: Ubiquitous in fetal and adult tissues.; myocardium;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;oesophagus;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach; superior cervical ganglion;heart; 0.33188 0.17027 -0.47017169 23.25430526 1285.96464 6.75164 PRCD 0.00310509622416 0.593819876859408 0.403075026916432 progressive rod-cone degeneration FUNCTION: Involved in vision.; DISEASE: Retinitis pigmentosa 36 (RP36) [MIM:610599]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:16938425}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.10855 . 0.057118534 57.99716914 35.03699 1.06321 PRCP 3.33652772106359e-08 0.527180223518365 0.472819743116358 prolylcarboxypeptidase FUNCTION: Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH.; . TISSUE SPECIFICITY: Highest levels in placenta, lung and liver. Also present in heart, brain, pancreas and kidney.; smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;gall bladder;tonsil;heart;cartilage;pineal body;adrenal cortex;blood;skeletal muscle;breast;epididymis;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; kidney; 0.42214 0.21008 0.198490371 67.30360934 1597.81081 7.39874 PRD . . . primary retinal dysplasia . . . . . . . . . . . PRDM1 0.980264413149198 0.0197324443076129 3.1425431894302e-06 PR domain 1 FUNCTION: Transcriptional repressor that binds specifically to the PRDI element in the promoter of the beta-interferon gene (PubMed:1851123). Drives the maturation of B-lymphocytes into Ig secreting cells (PubMed:12626569). {ECO:0000269|PubMed:12626569, ECO:0000269|PubMed:1851123}.; . . . . 0.75728 0.34838 0.824892996 88.06912008 1937.8398 8.09882 PRDM2 0.995040619056877 0.00495938076471239 1.78410483761285e-10 PR domain 2 FUNCTION: S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3. May function as a DNA-binding transcription factor. Binds to the macrophage-specific TPA-responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and may act as a transcriptional activator of this gene. {ECO:0000269|PubMed:14633678}.; . TISSUE SPECIFICITY: Highly expressed in retinoblastoma cell lines and in brain tumors. Also expressed in a number of other cell lines and in brain, heart, skeletal muscle, liver and spleen. Isoform 1 is expressed in testis at much higher level than isoform 3. {ECO:0000269|PubMed:8654390, ECO:0000269|PubMed:9006946}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;optic nerve;frontal lobe;cerebral cortex;thyroid;bone;testis;germinal center;brain;bladder;pineal gland;amygdala;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;urinary;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;head and neck;spleen;kidney;mammary gland;stomach;thymus; whole brain;dorsal root ganglion;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.28355 0.21546 -0.553188106 19.81009672 615.77007 5.01180 PRDM4 0.833196847904435 0.166773727482029 2.94246135365691e-05 PR domain 4 FUNCTION: May function as a transcription factor involved in cell differentiation.; . TISSUE SPECIFICITY: Expressed in many tissues. Highly expressed in ovary, testis, pancreas, brain, heart and prostate.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;thalamus;medulla oblongata;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.27262 0.11630 -1.353899809 4.558858221 42.47269 1.23328 PRDM5 0.742419320671244 0.257576580509626 4.09881913001754e-06 PR domain 5 FUNCTION: Sequence-specific DNA-binding transcription factor. Represses transcription at least in part by recruitment of the histone methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1. Regulates hematopoiesis-associated protein-coding and microRNA (miRNA) genes. May regulate the expression of proteins involved in extracellular matrix development and maintenance, including fibrillar collagens, such as COL4A1 and COL11A1, connective tissue components, such as HAPLN1, and molecules regulating cell migration and adhesion, including EDIL3 and TGFB2. May caused G2/M arrest and apoptosis in cancer cells. {ECO:0000269|PubMed:15077163, ECO:0000269|PubMed:17636019, ECO:0000269|PubMed:21664999}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in colon and ovary. Tends to be silenced in breast, colorectal, gastric and liver cancer tissues. {ECO:0000269|PubMed:15077163, ECO:0000269|PubMed:17699856}.; unclassifiable (Anatomical System);pancreas;lung;whole body;thyroid;liver;testis;head and neck;skeletal muscle; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.43634 0.09811 -0.620857637 17.3566879 226.2631 3.25042 PRDM6 . . . PR domain 6 FUNCTION: Putative histone methyltransferase that acts as a transcriptional repressor of smooth muscle gene expression. Promotes the transition from differentiated to proliferative smooth muscle by suppressing differentiation and maintaining the proliferative potential of vascular smooth muscle cells. Also plays a role in endothelial cells by inhibiting endothelial cell proliferation, survival and differentiation. It is unclear whether it has histone methyltransferase activity in vivo. According to some authors, it does not act as a histone methyltransferase by itself and represses transcription by recruiting EHMT2/G9a. According to others, it possesses histone methyltransferase activity when associated with other proteins and specifically methylates 'Lys-20' of histone H4 in vitro. 'Lys-20' methylation represents a specific tag for epigenetic transcriptional repression (By similarity). {ECO:0000250}.; . . . . 0.32166 0.09864 . . 3796.30099 12.08898 PRDM7 3.13626272886712e-10 0.285399595236047 0.714600404450326 PR domain 7 FUNCTION: Probable histone methyltransferase. {ECO:0000250}.; . . . . 0.05898 0.05973 1.910792163 97.4168436 4300.105 13.05001 PRDM8 . . . PR domain 8 FUNCTION: Probable histone methyltransferase, preferentially acting on 'Lys-9' of histone H3 (By similarity). Involved in the control of steroidogenesis through transcriptional repression of steroidogenesis marker genes such as CYP17A1 and LHCGR (By similarity). Forms with BHLHE22 a transcriptional repressor complex controlling genes involved in neural development and neuronal differentiation (By similarity). In the retina, it is required for rod bipolar and type 2 OFF-cone bipolar cell survival (By similarity). {ECO:0000250|UniProtKB:Q8BZ97}.; . TISSUE SPECIFICITY: Expressed in brain, heart, skeletal muscle, testes, prostate. {ECO:0000269|PubMed:22961547}.; unclassifiable (Anatomical System);ovary;colon;blood;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;frontal lobe;placenta;macula lutea;hippocampus;testis;brain; dorsal root ganglion;uterus corpus;superior cervical ganglion;subthalamic nucleus;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.27752 0.10475 . . 95.49877 2.10987 PRDM9 1.9533397375621e-22 0.000203625113481485 0.999796374886519 PR domain 9 FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-4' of histone H3 during meiotic prophase and is essential for proper meiotic progression. Does not have the ability to mono- and dimethylate 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes during early meiotic prophase (By similarity). {ECO:0000250}.; . . skeletal muscle; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06754 . 1.317245065 94.06699693 268.62721 3.51556 PRDM10 0.998059991340664 0.00194000865568205 3.65359646382705e-12 PR domain 10 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);colon;fovea centralis;choroid;skeletal muscle;bone marrow;uterus;breast;prostate;whole body;lung;endometrium;bone;placenta;macula lutea;visual apparatus;liver;germinal center;brain;mammary gland;stomach;cerebellum;thymus; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;parietal lobe;skeletal muscle; 0.34103 . -0.012873393 52.35904695 2398.16123 9.08767 PRDM11 0.942263570754501 0.0576910501913327 4.53790541659587e-05 PR domain 11 FUNCTION: May be involved in transcription regulation. {ECO:0000269|PubMed:25499759}.; . TISSUE SPECIFICITY: Highly expressed in lung, including bronchial epithelial cells and airway smooth muscle cells, as well as in peripheral blood mononuclear cells. In tonsils, expressed in B- cell types, including naive B-cells, centroblasts, centrocytes and memory B-cells (at protein level). In benign hyperplastic lymph nodes, expressed in germinal center cells in both the dark and light zones, as well as in scattered cells in the mantle zone and the interfollicular area (at protein level). {ECO:0000269|PubMed:24929828, ECO:0000269|PubMed:25499759}.; breast;prostate;lung;brain; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.19739 . . . 338.03141 3.90302 PRDM12 0.297870330270587 0.682424386394444 0.0197052833349689 PR domain 12 FUNCTION: Involved in the positive regulation of histone H3-K9 dimethylation. {ECO:0000269|PubMed:26005867}.; DISEASE: Neuropathy, hereditary sensory and autonomic, 8 (HSAN8) [MIM:616488]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by sensory and/or autonomic abnormalities. HSAN8 patients manifest congenital insensitivity to pain resulting in ulceration to the fingers, tongue, lips, and other distal appendages. Some patients may also have decreased sweating and tear production. {ECO:0000269|PubMed:26005867}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Not found in adult tissues except in dorsal root ganglia. {ECO:0000269|PubMed:26005867}.; lung;muscle;testis; heart;skeletal muscle; 0.40567 . . . 22.66512 0.75872 PRDM13 . . . PR domain 13 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.85202 . . . 3105.10566 10.60110 PRDM14 0.968775953486552 0.0312142790347202 9.767478727713e-06 PR domain 14 FUNCTION: Transcription factor that has both positive and negative roles on transcription. Required for the maintenance of emryonic stem cell identity and the reacquisition of pluripotency in somatic cells. May play an essential role in germ cell development at 2 levels: the reacquisition of potential pluripotency, including SOX2 up-regulation, and successful epigenetic reprogramming, characterized by EHMT1 repression (By similarity). Directly up-regulates the expression of pluripotency gene POU5F1 through its proximal enhancer. Binds to the DNA consensus sequence 5'-GGTC[TC]CTAA-3'. {ECO:0000250, ECO:0000269|PubMed:17942894, ECO:0000269|PubMed:20953172}.; . TISSUE SPECIFICITY: Expressed in embryonic stem cells. Tends to be overexpressed in breast cancer (at protein level). {ECO:0000269|PubMed:17942894, ECO:0000269|PubMed:20953172}.; unclassifiable (Anatomical System);ovary;epididymis;nasopharynx;brain; . 0.39311 0.10057 0.018483465 55.44939844 1782.52817 7.79575 PRDM15 0.753744615224627 0.24625538355603 1.21934292903256e-09 PR domain 15 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Detected in all tissues examined. {ECO:0000269|PubMed:15904895}.; unclassifiable (Anatomical System);lymph node;lung;ovary;islets of Langerhans;visual apparatus;testis;blood;germinal center;brain;stomach; superior cervical ganglion;testis - seminiferous tubule;adrenal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle;skin; 0.07470 0.10154 -2.001084103 1.733899505 875.44322 5.75655 PRDM16 0.999843194473124 0.000156805522131504 4.74503772018985e-12 PR domain 16 FUNCTION: Binds DNA and functions as a transcriptional regulator. Functions in the differentiation of brown adipose tissue (BAT) which is specialized in dissipating chemical energy in the form of heat in response to cold or excess feeding while white adipose tissue (WAT) is specialized in the storage of excess energy and the control of systemic metabolism. Together with CEBPB, regulates the differentiation of myoblastic precursors into brown adipose cells. Functions also as a repressor of TGF-beta signaling. Isoform 4 may regulate granulocytes differentiation. {ECO:0000269|PubMed:12816872, ECO:0000269|PubMed:14656887, ECO:0000269|PubMed:19049980}.; DISEASE: Cardiomyopathy, dilated 1LL (CMD1LL) [MIM:615373]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:23768516}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving PRDM16 is found in myelodysplastic syndrome (MDS) and acute myeloid leukemia (AML). Reciprocal translocation t(1;3)(p36;q21). Isoform 4 is specifically expressed in adult T-cell leukemia. {ECO:0000269|PubMed:11050005, ECO:0000269|PubMed:12557231}.; TISSUE SPECIFICITY: Expressed in uterus and kidney. Expressed in both cardiomyocytes and interstitial cells. {ECO:0000269|PubMed:11050005, ECO:0000269|PubMed:12816872, ECO:0000269|PubMed:23768516}.; unclassifiable (Anatomical System);lymph node;lung;whole body;liver;testis;colon;brain; trigeminal ganglion; 0.35627 0.19070 -1.424032938 4.063458363 1261.89174 6.69837 PRDX1 1.43818422373501e-07 0.0621881601170892 0.937811696064488 peroxiredoxin 1 FUNCTION: Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;thymus; hypothalamus;spinal cord;kidney;fetal thyroid; 0.84286 0.73165 -0.251530012 35.42108988 22.33675 0.75000 PRDX1P1 . . . peroxiredoxin 1 pseudogene 1 . . . . . . . . . . . PRDX2 0.496065280846928 0.483689953987275 0.0202447651657976 peroxiredoxin 2 FUNCTION: Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2).; . . lymphoreticular;medulla oblongata;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;synovium;thyroid;pituitary gland;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;hippocampus;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;fetal liver;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.92575 0.59865 -0.405853867 26.23260203 11.87102 0.43008 PRDX2P1 . . . peroxiredoxin 2 pseudogene 1 . . . . . . . . . . . PRDX2P2 . . . peroxiredoxin 2 pseudogene 2 . . . . . . . . . . . PRDX2P3 . . . peroxiredoxin 2 pseudogene 3 . . . . . . . . . . . PRDX2P4 . . . peroxiredoxin 2 pseudogene 4 . . . . . . . . . . . PRDX3 0.221688705653951 0.770130926286014 0.00818036806003524 peroxiredoxin 3 FUNCTION: Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical- generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol. {ECO:0000269|PubMed:12492477}.; . . ovary;umbilical cord;sympathetic chain;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;gum;thyroid;germinal center;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;fetal liver;adrenal gland;appendix;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.41360 0.33828 0.349177632 74.18023119 110.77356 2.29307 PRDX3P1 . . . peroxiredoxin 3 pseudogene 1 . . . . . . . . . . . PRDX3P2 . . . peroxiredoxin 3 pseudogene 2 . . . . . . . . . . . PRDX3P3 . . . peroxiredoxin 3 pseudogene 3 . . . . . . . . . . . PRDX3P4 . . . peroxiredoxin 3 pseudogene 4 . . . . . . . . . . . PRDX4 0.281507844531997 0.696066166498937 0.0224259889690655 peroxiredoxin 4 FUNCTION: Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation. {ECO:0000269|PubMed:9388242}.; . . . . 0.20687 0.30181 0.103030231 61.2762444 71.43955 1.75914 PRDX4P1 . . . peroxiredoxin 4 pseudogene 1 . . . . . . . . . . . PRDX4P2 . . . peroxiredoxin 4 pseudogene 2 . . . . . . . . . . . PRDX5 0.00314038121761632 0.820478548917196 0.176381069865188 peroxiredoxin 5 FUNCTION: Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10521424}.; myocardium;smooth muscle;ovary;umbilical cord;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;oesophagus;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; whole brain;cerebellum peduncles;liver;cerebellum; 0.41018 0.55078 0.415317661 76.81056853 39.59544 1.16683 PRDX6 0.00998976782458624 0.823191731136947 0.166818501038467 peroxiredoxin 6 FUNCTION: Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.; . . . . 0.42340 0.51939 -0.273576253 33.97027601 10.90502 0.39467 PREB 0.0018983627682706 0.97542854064702 0.0226730965847091 prolactin regulatory element binding FUNCTION: Was first identified based on its probable role in the regulation of pituitary gene transcription. Binds to the prolactin gene (PRL) promoter and seems to activate transcription (By similarity). Guanine nucleotide exchange factor that activates SARA2. Required for the formation of COPII transport vesicles from the ER. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10920239, ECO:0000269|PubMed:12735795}.; lymphoreticular;medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.29365 0.27544 -0.356299879 29.31115829 105.39495 2.22397 PRELID1 0.865363911946567 0.13423494353315 0.000401144520283104 PRELI domain containing 1 FUNCTION: Involved in the modulation of the mitochondrial apoptotic pathway by ensuring the accumulation of cardiolipin (CL) in mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space to provide PA for CL synthesis in the inner membrane. Regulates the mitochondrial apoptotic pathway in primary Th cells. Regulates Th cell differentiation by down-regulating STAT6 thereby reducing IL-4-induced Th2 cell number. May be important for the development of vital and immunocompetent organs. {ECO:0000269|PubMed:18945965, ECO:0000269|PubMed:21364629, ECO:0000269|PubMed:23931759}.; . TISSUE SPECIFICITY: Highly expressed in fetal liver; less expressed in fetal brain, lung, and kidney. At the adult stage, expression is drastically reduced in the liver but highly expressed in the spleen, brain, lung, lymph nodes and peripheral blood leukocytes.; lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;iris;germinal center;bladder;brain;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;vein;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;kidney;stomach;aorta; . 0.32555 0.11110 -0.163345027 41.24793583 4.31085 0.15691 PRELID1P1 . . . PRELI domain containing 1 pseudogene 1 . . . . . . . . . . . PRELID1P2 . . . PRELI domain containing 1 pseudogene 2 . . . . . . . . . . . PRELID1P3 . . . PRELI domain containing 1 pseudogene 3 . . . . . . . . . . . PRELID1P4 . . . PRELI domain containing 1 pseudogene 4 . . . . . . . . . . . PRELID2 1.73073934677441e-05 0.43982389368785 0.560158798918682 PRELI domain containing 2 . . . uterus;prostate;lymph node;heart;endometrium;tongue;islets of Langerhans;testis;colon;kidney;brain;skin;retina; superior cervical ganglion; 0.18128 0.09482 -0.029247611 51.40363293 232.01926 3.29239 PRELID2P1 . . . PRELI domain containing 2 pseudogene 1 . . . . . . . . . . . PRELID3A . . . PRELI domain containing 3A . . . . . 0.23791 0.10785 -0.185391282 39.67916962 . . PRELID3B . . . PRELI domain containing 3B . . . . . 0.48576 . 0.281220278 71.07808445 . . PRELID3BP1 . . . PRELI domain containing 3B pseudogene 1 . . . . . . . . . . . PRELID3BP2 . . . PRELI domain containing 3B pseudogene 2 . . . . . . . . . . . PRELID3BP3 . . . PRELI domain containing 3B pseudogene 3 . . . . . . . . . . . PRELID3BP4 . . . PRELI domain containing 3B pseudogene 4 . . . . . . . . . . . PRELID3BP5 . . . PRELI domain containing 3B pseudogene 5 . . . . . . . . . . . PRELID3BP6 . . . PRELI domain containing 3B pseudogene 6 . . . . . . . . . . . PRELID3BP7 . . . PRELI domain containing 3B pseudogene 7 . . . . . . . . . . . PRELID3BP8 . . . PRELI domain containing 3B pseudogene 8 . . . . . . . . . . . PRELID3BP9 . . . PRELI domain containing 3B pseudogene 9 . . . . . . . . . . . PRELID3BP10 . . . PRELI domain containing 3B pseudogene 10 . . . . . . . . . . . PRELID3BP11 . . . PRELI domain containing 3B pseudogene 11 . . . . . . . . . . . PRELP 0.00373648581113307 0.847534565275165 0.148728948913702 proline/arginine-rich end leucine-rich repeat protein FUNCTION: May anchor basement membranes to the underlying connective tissue. {ECO:0000250}.; . TISSUE SPECIFICITY: Connective tissue.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;oesophagus;endometrium;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.72446 0.12933 0.354632714 74.58126917 147.10767 2.64260 PREP 0.991043730072313 0.0089562514340649 1.84936217710684e-08 prolyl endopeptidase FUNCTION: Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.; . . . . 0.09260 0.38934 -0.997481928 8.47487615 3956.75021 12.44439 PREPL 2.42946176486827e-11 0.240558654074955 0.75944134590075 prolyl endopeptidase-like FUNCTION: Probable serine peptidase whose precise substrate specificity remains unclear. Does not cleave peptides after a arginine or lysine residue. {ECO:0000269|PubMed:16143824, ECO:0000269|PubMed:16385448}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in brain, skeletal muscle, heart and kidney. {ECO:0000269|PubMed:15913950}.; lymphoreticular;ovary;sympathetic chain;skin;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;aorta;cerebellum; whole brain;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.37424 0.10892 -0.835882558 11.47676339 281.52127 3.59257 PREX1 0.999999621898147 3.78101853037118e-07 8.16446054885829e-20 phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 1 FUNCTION: Functions as a RAC guanine nucleotide exchange factor (GEF), which activates the Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol 3,4,5-trisphosphate and the beta gamma subunits of heterotrimeric G protein. May function downstream of heterotrimeric G proteins in neutrophils.; . TISSUE SPECIFICITY: Mainly expressed in peripheral blood leukocytes and brain. Expressed at intermediate level in spleen and lymph nodes, and weakly expressed in other tissues.; . . . 0.10475 0.067828261 58.96437839 4483.27013 13.43401 PREX2 1.00807254029751e-10 0.999991105039047 8.89486014627865e-06 phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 2 FUNCTION: Functions as a RAC1 guanine nucleotide exchange factor (GEF), activating Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol 3,4,5-trisphosphate and the beta gamma subunits of heterotrimeric G protein. Mediates the activation of RAC1 in a PI3K-dependent manner. May be an important mediator of Rac signaling, acting directly downstream of both G protein- coupled receptors and phosphoinositide 3-kinase. {ECO:0000269|PubMed:15304342, ECO:0000269|PubMed:15304343, ECO:0000269|PubMed:15897194}.; . TISSUE SPECIFICITY: Isoform 1 is highly expressed in skeletal muscle, heart and placenta, absent from peripheral blood leukocytes. Isoform 2 is expressed in skeletal muscle, kidney, small intestine, and placenta. Isoform 3 is expressed in the heart. {ECO:0000269|PubMed:15304343}.; unclassifiable (Anatomical System);lung;hypothalamus;thyroid;spinal cord;liver;head and neck;kidney;brain;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;temporal lobe;skeletal muscle; 0.34721 0.10286 -0.672483109 15.41637179 1511.01196 7.21951 PRF1 1.39812349386747e-07 0.115080298844417 0.884919561343233 perforin 1 FUNCTION: Plays a key role in secretory granule-dependent cell death, and in defense against virus-infected or neoplastic cells. Plays an important role in killing other cells that are recognized as non-self by the immune system, e.g. in transplant rejection or some forms of autoimmune disease. Can insert into the membrane of target cells in its calcium-bound form, oligomerize and form large pores. Promotes cytolysis and apoptosis of target cells by facilitating the uptake of cytotoxic granzymes. {ECO:0000269|PubMed:20038786, ECO:0000269|PubMed:20225066, ECO:0000269|PubMed:20889983, ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:9058810, ECO:0000269|PubMed:9164947}.; DISEASE: Familial hemophagocytic lymphohistiocytosis 2 (FHL2) [MIM:603553]: A rare disorder characterized by immune dysregulation with hypercytokinemia, defective function of natural killer cell, and massive infiltration of several organs by activated lymphocytes and macrophages. The clinical features of the disease include fever, hepatosplenomegaly, cytopenia, and less frequently neurological abnormalities ranging from irritability and hypotonia to seizures, cranial nerve deficits and ataxia. {ECO:0000269|PubMed:10583959, ECO:0000269|PubMed:11179007}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);pancreas;smooth muscle;lung;liver;spleen;blood;kidney;skeletal muscle; whole blood; 0.05432 0.57371 -0.617221851 17.44515216 262.93472 3.47879 PRG2 1.36694535208987e-05 0.394999589984969 0.60498674056151 proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein) FUNCTION: Cytotoxin and helminthotoxin. Also induces non-cytolytic histamine release from human basophils. Involved in antiparasitic defense mechanisms and immune hypersensitivity reactions. The proform acts as a proteinase inhibitor, reducing the activity of PAPPA. {ECO:0000269|PubMed:10913121}.; . TISSUE SPECIFICITY: High levels of the proform in placenta and pregnancy serum; in placenta, localized to X cells of septa and anchoring villi. Lower levels in a variety of other tissues including kidney, myometrium, endometrium, ovaries, breast, prostate, bone marrow and colon. {ECO:0000269|PubMed:10491647, ECO:0000269|PubMed:7526035}.; unclassifiable (Anatomical System);heart;ovary;cartilage;blood;parathyroid;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;optic nerve;placenta;macula lutea;liver;spleen; fetal liver;prostate;placenta;bone marrow; 0.25063 0.10322 -0.113792788 45.25831564 10.45731 0.38011 PRG3 0.000177440765062925 0.698111215506483 0.301711343728454 proteoglycan 3 FUNCTION: Possesses similar cytotoxic and cytostimulatory activities to PRG2/MBP. In vitro, stimulates neutrophil superoxide production and IL8 release, and histamine and leukotriene C4 release from basophils. {ECO:0000269|PubMed:10318872}.; . TISSUE SPECIFICITY: Expressed in bone marrow. Not detected in placenta. {ECO:0000269|PubMed:10318872}.; liver;spleen; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;bone marrow; 0.05220 0.10300 0.837848571 88.22835574 283.05119 3.60223 PRG4 0.469279559391241 0.530674376695604 4.60639131552124e-05 proteoglycan 4 FUNCTION: Plays a role in boundary lubrication within articulating joints. Prevents protein deposition onto cartilage from synovial fluid by controlling adhesion-dependent synovial growth and inhibiting the adhesion of synovial cells to the cartilage surface.; DISEASE: Camptodactyly-arthropathy-coxa vara-pericarditis syndrome (CACP) [MIM:208250]: An autosomal recessive disorder characterized by the association of congenital or early-onset camptodactyly and non-inflammatory arthropathy with synovial hyperplasia. Individuals with CACP have normal appearing joints at birth but with advancing age develop joint failure, non-inflammatory synoviocyte hyperplasia and subintimal fibrosis of the synovial capsule. Some patients also manifest progressive coxa vara deformity and/or non-inflammatory pericardial or pleural effusions. {ECO:0000269|PubMed:10545950}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in synovial tissue, cartilage and liver and weakly in heart and lung. Isoform B is expressed in kidney, lung, liver, heart and brain. Isoform C and isoform D are widely expressed. {ECO:0000269|PubMed:10545950, ECO:0000269|PubMed:11124536}.; . . 0.14452 . 1.502801682 95.39396084 3294.98507 10.95701 PRH1 0.284195071358163 0.693853668720195 0.0219512599216417 proline-rich protein HaeIII subfamily 1 FUNCTION: PRP's act as highly potent inhibitors of crystal growth of calcium phosphates. They provide a protective and reparative environment for dental enamel which is important for the integrity of the teeth.; . . . . . . . . 72.38013 1.77281 PRH2 0.595625943201393 0.394875766545268 0.00949829025333887 proline-rich protein HaeIII subfamily 2 FUNCTION: PRP's act as highly potent inhibitors of crystal growth of calcium phosphates. They provide a protective and reparative environment for dental enamel which is important for the integrity of the teeth.; . . medulla oblongata;salivary gland;adrenal cortex;parotid gland;colon;parathyroid;skeletal muscle;prostate;larynx;adrenal gland;thyroid;liver;head and neck;kidney;brain;pineal gland; . . . 0.747842143 86.47676339 51.88257 1.42290 PRICKLE1 0.991966858696436 0.0080330712758113 7.00277528085005e-08 prickle planar cell polarity protein 1 FUNCTION: Involved in the planar cell polarity pathway that controls convergent extension during gastrulation and neural tube closure. Convergent extension is a complex morphogenetic process during which cells elongate, move mediolaterally, and intercalate between neighboring cells, leading to convergence toward the mediolateral axis and extension along the anteroposterior axis. Necessary for nuclear localization of REST. May serve as nuclear receptor. {ECO:0000269|PubMed:21901791}.; DISEASE: Neural tube defects (NTD) [MIM:182940]: Congenital malformations of the central nervous system and adjacent structures related to defective neural tube closure during the first trimester of pregnancy. Failure of neural tube closure can occur at any level of the embryonic axis. Common NTD forms include anencephaly, myelomeningocele and spina bifida, which result from the failure of fusion in the cranial and spinal region of the neural tube. NTDs have a multifactorial etiology encompassing both genetic and environmental components. {ECO:0000269|PubMed:21901791}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at highest levels in placenta and at lower levels in lung, liver, kidney and pancreas. Expressed in thalamus, hippocampus, cerebral cortex, and cerebellum (in neurons rather than glia). {ECO:0000269|PubMed:12525887, ECO:0000269|PubMed:14645515, ECO:0000269|PubMed:18976727}.; lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex; 0.82156 0.14621 -0.286522835 33.47487615 582.56048 4.89304 PRICKLE2 0.987837185730764 0.0121627751148814 3.91543547578885e-08 prickle planar cell polarity protein 2 . . TISSUE SPECIFICITY: Expressed in brain, eye and testis. Additionally in fetal brain, adult cartilage, pancreatic islet, gastric cancer and uterus tumors. {ECO:0000269|PubMed:12525887}.; ovary;developmental;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;thyroid;bone;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;tongue;islets of Langerhans;pineal body;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.19738 0.13472 -1.109541557 6.782259967 94.65407 2.09581 PRICKLE2-AS1 . . . PRICKLE2 antisense RNA 1 . . . . . . . . . . . PRICKLE2-AS2 . . . PRICKLE2 antisense RNA 2 . . . . . . . . . . . PRICKLE2-AS3 . . . PRICKLE2 antisense RNA 3 . . . . . . . . . . . PRICKLE3 0.15265646111407 0.830543593736699 0.0167999451492309 prickle planar cell polarity protein 3 . . TISSUE SPECIFICITY: Widely expressed.; . . 0.18351 0.11213 -0.358119787 29.16371786 . . PRICKLE4 7.00664679526374e-06 0.720454946764274 0.279538046588931 prickle planar cell polarity protein 4 . . TISSUE SPECIFICITY: Expressed in a broad range of normal tissues as well as in hepatocellular carcinoma, breast cancer and prostate cancer tissues. {ECO:0000269|PubMed:15702247}.; lymphoreticular;medulla oblongata;ovary;adrenal medulla;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta; . 0.17414 0.08679 0.619191319 83.36282142 203.54887 3.07879 PRIM1 0.0268979390191366 0.961225661242737 0.0118763997381262 primase (DNA) subunit 1 FUNCTION: DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.; . . unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;colon;blood;lens;breast;lung;endometrium;nasopharynx;thyroid;liver;testis;head and neck;spleen;germinal center;kidney;brain;bladder;stomach; subthalamic nucleus;superior cervical ganglion;occipital lobe;adrenal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.95810 . 0.038710339 56.92380278 1513.73456 7.23358 PRIM2 5.14707916843554e-08 0.39171956986701 0.608280378662199 primase (DNA) subunit 2 FUNCTION: DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.; . . unclassifiable (Anatomical System);uterus;prostate;lymph node;lung;heart;placenta;visual apparatus;cervix;spleen;skin;stomach; dorsal root ganglion;superior cervical ganglion;uterus corpus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.89222 0.08308 . . 55.84911 1.50063 PRIMA1 0.367086765780191 0.58362351363537 0.0492897205844383 proline rich membrane anchor 1 FUNCTION: Required to anchor acetylcholinesterase (ACHE) to the basal lamina of the neuromuscular junction and to the membrane of neuronal synapses in brain. Also able to organize ACHE into tetramers (By similarity). {ECO:0000250}.; . . ovary;skeletal muscle;retina; . 0.17164 0.15948 -0.163345027 41.24793583 5.69887 0.21345 PRIMPOL 2.78745619908396e-13 0.0367075975918715 0.96329240240785 primase and DNA directed polymerase FUNCTION: DNA primase and DNA polymerase able to initiate de novo DNA synthesis using dNTPs. Shows a high capacity to tolerate DNA damage lesions such as 8oxoG and abasic sites in DNA. Involved in translesion synthesis via its primase activity by mediating uninterrupted fork progression after programmed or damage-induced fork arrest and by reinitiating DNA synthesis after dNTP depletion. Required for mitochondrial DNA (mtDNA) synthesis, suggesting it may be involved in DNA tolerance during the replication of mitochondrial DNA. Has non-overlapping function with POLH. {ECO:0000269|PubMed:24126761, ECO:0000269|PubMed:24207056, ECO:0000269|PubMed:24240614, ECO:0000269|PubMed:24267451}.; DISEASE: Myopia 22, autosomal dominant (MYP22) [MIM:615420]: A refractive error of the eye, in which parallel rays from a distant object come to focus in front of the retina, vision being better for near objects than for far. {ECO:0000269|PubMed:23579484}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.14884 . 0.510776592 80.23708422 1081.70511 6.30838 PRINS . . . psoriasis associated non-protein coding RNA induced by stress . . . . . . . . . . . PRKAA1 0.0351010343853684 0.963250729908533 0.0016482357060989 protein kinase AMP-activated catalytic subunit alpha 1 FUNCTION: Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1. {ECO:0000269|PubMed:11518699, ECO:0000269|PubMed:11554766, ECO:0000269|PubMed:12519745, ECO:0000269|PubMed:14651849, ECO:0000269|PubMed:15866171, ECO:0000269|PubMed:17486097, ECO:0000269|PubMed:17711846, ECO:0000269|PubMed:18184930, ECO:0000269|PubMed:18439900, ECO:0000269|PubMed:20074060, ECO:0000269|PubMed:20160076, ECO:0000269|PubMed:21205641}.; . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.90852 0.13068 -0.494039303 22.09247464 21.33891 0.72054 PRKAA2 1.44261719898224e-05 0.959668129273646 0.0403174445543647 protein kinase AMP-activated catalytic subunit alpha 2 FUNCTION: Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. Involved in insulin receptor/INSR internalization (PubMed:25687571). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1. Plays an important role in the differential regulation of pro-autophagy (composed of PIK3C3, BECN1, PIK3R4 and UVRAG or ATG14) and non-autophagy (composed of PIK3C3, BECN1 and PIK3R4) complexes, in response to glucose starvation. Can inhibit the non-autophagy complex by phosphorylating PIK3C3 and can activate the pro-autophagy complex by phosphorylating BECN1 (By similarity). {ECO:0000250|UniProtKB:Q8BRK8, ECO:0000269|PubMed:11518699, ECO:0000269|PubMed:11554766, ECO:0000269|PubMed:12519745, ECO:0000269|PubMed:14651849, ECO:0000269|PubMed:15866171, ECO:0000269|PubMed:17486097, ECO:0000269|PubMed:17711846, ECO:0000269|PubMed:18184930, ECO:0000269|PubMed:20074060, ECO:0000269|PubMed:20160076, ECO:0000269|PubMed:21205641, ECO:0000269|PubMed:25687571, ECO:0000269|PubMed:7959015}.; . . . . 0.96381 0.23021 -0.670411825 15.61689078 54.24264 1.47062 PRKAB1 0.0518791329975909 0.927187020697611 0.0209338463047977 protein kinase AMP-activated non-catalytic subunit beta 1 FUNCTION: Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).; . . medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;synovium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;small intestine;heart;lacrimal gland;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;pons;kidney;atrioventricular node;skeletal muscle; 0.21058 0.23021 0.016664174 55.21939137 112.79322 2.31042 PRKAB2 0.767108491529973 0.231100275820708 0.00179123264931932 protein kinase AMP-activated non-catalytic subunit beta 2 FUNCTION: Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).; . . ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;pia mater;lung;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.67503 0.17428 0.191216164 66.57230479 26.51097 0.85741 PRKACA 0.959056420321561 0.0409244108895993 1.91687888398227e-05 protein kinase cAMP-activated catalytic subunit alpha FUNCTION: Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose- mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B- alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha- difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT). Phosphorylates APOBEC3G and AICDA. Isoform 2 phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation. {ECO:0000269|PubMed:15642694, ECO:0000269|PubMed:15905176, ECO:0000269|PubMed:16387847, ECO:0000269|PubMed:17333334, ECO:0000269|PubMed:17565987, ECO:0000269|PubMed:17693412, ECO:0000269|PubMed:18836454, ECO:0000269|PubMed:19949837, ECO:0000269|PubMed:20356841, ECO:0000269|PubMed:21423175, ECO:0000269|PubMed:21514275, ECO:0000269|PubMed:21812984}.; DISEASE: Primary pigmented nodular adrenocortical disease 4 (PPNAD4) [MIM:615830]: A rare bilateral adrenal defect causing ACTH-independent Cushing syndrome. Macroscopic appearance of the adrenals is characteristic with small pigmented micronodules observed in the cortex. Adrenal glands show overall normal size and weight, and multiple small yellow-to-dark brown nodules surrounded by a cortex with a uniform appearance. Microscopically, there are moderate diffuse cortical hyperplasia with mostly nonpigmented nodules, multiple capsular deficits and massive circumscribed and infiltrating extra-adrenal cortical excrescences with micronodules. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes. {ECO:0000269|PubMed:24571724, ECO:0000269|PubMed:24700472, ECO:0000269|PubMed:24747643, ECO:0000269|PubMed:24855271}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is ubiquitous. Isoform 2 is sperm- specific and is enriched in pachytene spermatocytes but is not detected in round spermatids. {ECO:0000269|PubMed:10906071, ECO:0000269|PubMed:21812984}.; lymphoreticular;myocardium;smooth muscle;ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;synovium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;adrenal gland;adrenal cortex;trigeminal ganglion;cerebellum; 0.43829 0.53490 -0.471992905 23.03609342 6.6082 0.24435 PRKACB 0.612478408550855 0.387165493213666 0.000356098235478502 protein kinase cAMP-activated catalytic subunit beta FUNCTION: Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. {ECO:0000269|PubMed:12420224, ECO:0000269|PubMed:21423175}.; . TISSUE SPECIFICITY: Isoform 1 is most abundant in the brain, with low level expression in kidney. Isoform 2 is predominantly expressed in thymus, spleen and kidney. Isoform 3 and isoform 4 are only expressed in the brain. {ECO:0000269|PubMed:11589697}.; . . 0.92308 0.34147 -0.427900189 25.14744043 21.38815 0.72133 PRKACG 0.00505819149155764 0.698191288813528 0.296750519694915 protein kinase cAMP-activated catalytic subunit gamma FUNCTION: Phosphorylates a large number of substrates in the cytoplasm and the nucleus.; . TISSUE SPECIFICITY: Testis specific. But important tissues such as brain and ovary have not been analyzed for the content of transcript.; . . 0.65424 0.27675 -0.093566408 46.7386176 1237.26738 6.64266 PRKAG1 0.00163708742661498 0.992444148143943 0.00591876442944228 protein kinase AMP-activated non-catalytic subunit gamma 1 FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive. {ECO:0000269|PubMed:21680840}.; . . ovary;skin;retina;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;urinary;pharynx;blood;lens;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;small intestine;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;adrenal gland;testis;kidney;parietal lobe; 0.62200 0.15707 0.193034296 66.82000472 67.09894 1.69404 PRKAG2 0.977557428638321 0.022442394626663 1.76735016195424e-07 protein kinase AMP-activated non-catalytic subunit gamma 2 FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive. {ECO:0000269|PubMed:14722619}.; DISEASE: Wolff-Parkinson-White syndrome (WPWS) [MIM:194200]: A supernormal conduction disorder characterized by the presence of one or several accessory atrioventricular connections, which can lead to episodes of sporadic tachycardia. {ECO:0000269|PubMed:11407343, ECO:0000269|PubMed:11748095}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, familial hypertrophic 6 (CMH6) [MIM:600858]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. CMH6 patients present Wolff-Parkinson-White ventricular preexcitation, enlarged myocytes without myofiber disarray, and glycogen- containing cytosolic vacuoles within cardiomyocytes. {ECO:0000269|PubMed:11371514, ECO:0000269|PubMed:11827995}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Glycogen storage disease of heart lethal congenital (GSDH) [MIM:261740]: Rare disease which leads to death within a few weeks to a few months after birth, through heart failure and respiratory compromise. {ECO:0000269|PubMed:15877279}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform B is ubiquitously expressed except in liver and thymus. The highest level is detected in heart with abundant expression in placenta and testis.; ovary;colon;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;larynx;iris;pituitary gland;amniotic fluid;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;skeletal muscle;bile duct;breast;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.75824 0.19412 -0.867014353 10.72776598 322.64102 3.81555 PRKAG2-AS1 . . . PRKAG2 antisense RNA 1 . . . . . . . . . . . PRKAG3 9.66992545866806e-05 0.939090480565648 0.0608128201797649 protein kinase AMP-activated non-catalytic subunit gamma 3 FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive. {ECO:0000269|PubMed:14722619}.; . TISSUE SPECIFICITY: Skeletal muscle, with weak expression in heart and pancreas.; unclassifiable (Anatomical System);uterus;heart;liver;spleen;skin;skeletal muscle; . 0.21868 0.15227 0.268267497 70.64166077 1227.80308 6.62527 PRKAR1A 0.999223269468243 0.000776724815451227 5.71630608410178e-09 protein kinase cAMP-dependent type I regulatory subunit alpha FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. {ECO:0000269|PubMed:16491121, ECO:0000269|PubMed:20215566}.; DISEASE: Carney complex 1 (CNC1) [MIM:160980]: CNC is a multiple neoplasia syndrome characterized by spotty skin pigmentation, cardiac and other myxomas, endocrine tumors, and psammomatous melanotic schwannomas. {ECO:0000269|PubMed:15371594, ECO:0000269|PubMed:18241045, ECO:0000269|PubMed:22785148, ECO:0000269|PubMed:23323113}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Intracardiac myxoma (INTMYX) [MIM:255960]: Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Primary pigmented nodular adrenocortical disease 1 (PPNAD1) [MIM:610489]: A rare bilateral adrenal defect causing ACTH-independent Cushing syndrome. Macroscopic appearance of the adrenals is characteristic with small pigmented micronodules observed in the cortex. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes. PPNAD1 is most often diagnosed in patients with Carney complex, a multiple neoplasia syndrome. However it can also be observed in patients without other manifestations. {ECO:0000269|PubMed:12213893}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Acrodysostosis 1, with or without hormone resistance (ACRDYS1) [MIM:101800]: A form of skeletal dysplasia characterized by short stature, severe brachydactyly, facial dysostosis, and nasal hypoplasia. Affected individuals often have advanced bone age and obesity. Laboratory studies show resistance to multiple hormones, including parathyroid, thyrotropin, calcitonin, growth hormone-releasing hormone, and gonadotropin. However, not all patients show endocrine abnormalities. {ECO:0000269|PubMed:21651393, ECO:0000269|PubMed:22464250, ECO:0000269|PubMed:22464252, ECO:0000269|PubMed:22723333, ECO:0000269|PubMed:23043190, ECO:0000269|PubMed:23425300}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Four types of regulatory chains are found: I- alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.; myocardium;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;oesophagus;larynx;bone;pituitary gland;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;lung;pia mater;mesenchyma;placenta;head and neck;kidney;stomach;aorta; amygdala;whole brain;testis - interstitial;thalamus;occipital lobe;caudate nucleus;subthalamic nucleus;testis - seminiferous tubule;thyroid;prefrontal cortex;globus pallidus;testis;cingulate cortex;parietal lobe; 0.93386 0.72660 -0.339715008 30.06605331 5.79493 0.21858 PRKAR1AP1 . . . protein kinase cAMP-dependent type I regulatory subunit alpha pseudogene 1 . . . . . . . . . . . PRKAR1B 0.0247577995630588 0.961843449188185 0.0133987512487564 protein kinase cAMP-dependent type I regulatory subunit beta FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. {ECO:0000269|PubMed:20819953}.; . TISSUE SPECIFICITY: Four types of regulatory chains are found: I- alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.; unclassifiable (Anatomical System); whole brain;dorsal root ganglion;amygdala;occipital lobe;superior cervical ganglion;thalamus;medulla oblongata;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; . . -1.109541557 6.782259967 79.27334 1.88171 PRKAR2A 0.983250575891508 0.0167473258099448 2.09829854684244e-06 protein kinase cAMP-dependent type II regulatory subunit alpha FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.; . TISSUE SPECIFICITY: Four types of regulatory chains are found: I- alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.; medulla oblongata;ovary;colon;fovea centralis;skin;uterus;frontal lobe;larynx;testis;brain;amygdala;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pancreas;lung;placenta;visual apparatus;hippocampus;macula lutea;liver;head and neck;cervix;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;occipital lobe;atrioventricular node;pons;skin;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.79848 0.32089 -0.161524709 41.6430762 138.8496 2.56816 PRKAR2A-AS1 . . . PRKAR2A antisense RNA 1 . . . . . . . . . . . PRKAR2B 0.995321215882976 0.00467832800458495 4.56112438593304e-07 protein kinase cAMP-dependent type II regulatory subunit beta FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.; . TISSUE SPECIFICITY: Four types of regulatory chains are found: I- alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.; myocardium;ovary;sympathetic chain;parathyroid;vein;skin;bone marrow;prostate;whole body;larynx;bone;testis;dura mater;germinal center;brain;artery;unclassifiable (Anatomical System);amygdala;meninges;heart;adrenal cortex;blood;lens;pancreas;pia mater;lung;adrenal gland;trabecular meshwork;placenta;visual apparatus;hippocampus;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; fetal brain; 0.66244 0.54697 -0.185391282 39.67916962 14.0537 0.51025 PRKCA 0.952135908118796 0.0478640443282032 4.75530012841676e-08 protein kinase C alpha FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)- dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B- ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF- kappa-B-induced genes, through IL1A-dependent induction of NF- kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O- tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. {ECO:0000269|PubMed:10848585, ECO:0000269|PubMed:11909826, ECO:0000269|PubMed:12724315, ECO:0000269|PubMed:12832403, ECO:0000269|PubMed:15016832, ECO:0000269|PubMed:15504744, ECO:0000269|PubMed:15526160, ECO:0000269|PubMed:18056764, ECO:0000269|PubMed:19176525, ECO:0000269|PubMed:21576361, ECO:0000269|PubMed:23990668, ECO:0000269|PubMed:9738012, ECO:0000269|PubMed:9830023, ECO:0000269|PubMed:9873035, ECO:0000269|PubMed:9927633}.; . . ovary;salivary gland;sympathetic chain;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;small intestine;heart;spinal cord;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach; whole brain;amygdala;dorsal root ganglion;medulla oblongata;superior cervical ganglion;occipital lobe;olfactory bulb;spinal cord;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cerebellum; 0.81012 0.85579 -0.334253673 30.70299599 22.99218 0.76666 PRKCA-AS1 . . . PRKCA antisense RNA 1 . . . . . . . . . . . PRKCB 0.999908070013039 9.1929955400824e-05 3.15600284485897e-11 protein kinase C beta FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1- MAPK/ERK signaling cascade. May participate in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. Under high glucose in pancreatic beta-cells, is probably involved in the inhibition of the insulin gene transcription, via regulation of MYC expression. In endothelial cells, activation of PRKCB induces increased phosphorylation of RB1, increased VEGFA-induced cell proliferation, and inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS) regulation by insulin, which causes endothelial dysfunction. Also involved in triglyceride homeostasis (By similarity). Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. {ECO:0000250, ECO:0000269|PubMed:11598012, ECO:0000269|PubMed:19176525, ECO:0000269|PubMed:20228790}.; . . colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;optic nerve;frontal lobe;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;blood;lens;breast;lung;placenta;macula lutea;hippocampus;visual apparatus;liver;spleen;kidney; whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;temporal lobe;white blood cells;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.97714 0.68326 -0.80269335 12.23755603 26.08929 0.84687 PRKCD 0.997593706576692 0.00240628973773969 3.68556872381128e-09 protein kinase C delta FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor- initiated cell death, is involved in tumor suppression as well as survival of several cancers, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Negatively regulates B cell proliferation and also has an important function in self- antigen induced B cell tolerance induction. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)- induced inhibition of cell cycle progression at G1/S phase by up- regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Is highly expressed in a number of cancer cells and promotes cell survival and resistance against chemotherapeutic drugs by inducing cyclin D1 (CCND1) and hyperphosphorylation of RB1, and via several pro- survival pathways, including NF-kappa-B, AKT1 and MAPK1/3 (ERK1/2). Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl- phenylalanine (fMLP)-treated cells, is required for NCF1 (p47- phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C- terminal and regulates the interaction between MUC1 and beta- catenin. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion (By similarity). {ECO:0000250, ECO:0000269|PubMed:11748588, ECO:0000269|PubMed:11877440, ECO:0000269|PubMed:15774464, ECO:0000269|PubMed:16940418, ECO:0000269|PubMed:19587372, ECO:0000269|PubMed:19801500}.; DISEASE: Autoimmune lymphoproliferative syndrome 3 (ALPS3) [MIM:615559]: A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low. CVID9 patients have B-cell deficiency and severe autoimmunity. {ECO:0000269|PubMed:23319571}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;breast;lung;placenta;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; whole blood; 0.50726 0.64101 -1.041578376 7.773059684 38.38258 1.13875 PRKCDBP 4.93189420887156e-05 0.247824628810563 0.752126052247348 protein kinase C delta binding protein FUNCTION: Plays a role in the regulation of the circadian clock. Modulates the period length and phase of circadian gene expression and also regulates expression and interaction of the core clock components PER1/2 and CRY1/2. Seems to have an immune potentiation function. {ECO:0000250|UniProtKB:Q91VJ2, ECO:0000250|UniProtKB:Q9Z1H9}.; . TISSUE SPECIFICITY: Strongly expressed in mammary and epithelial cells. {ECO:0000269|PubMed:11691816}.; medulla oblongata;smooth muscle;ovary;salivary gland;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;larynx;bone;iris;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion; 0.10213 0.22954 . . 387.79965 4.14818 PRKCE 0.999891646235438 0.000108353717460902 4.71013739556987e-11 protein kinase C epsilon FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin-dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell-cell detachment prior to migration. In HeLa cells, contributes to hepatocyte growth factor (HGF)-induced cell migration, and in human corneal epithelial cells, plays a critical role in wound healing after activation by HGF. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F- actin via interaction with COPB1. During endothelin-induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma-aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2). In prostate cancer cells, interacts with and phosphorylates STAT3, which increases DNA-binding and transcriptional activity of STAT3 and seems to be essential for prostate cancer cell invasion. Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL- mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1. {ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:1374067, ECO:0000269|PubMed:15355962, ECO:0000269|PubMed:16757566, ECO:0000269|PubMed:17603037, ECO:0000269|PubMed:17875639, ECO:0000269|PubMed:17875724}.; . . smooth muscle;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.88093 0.77765 -0.023789244 52.09365416 156.41768 2.73373 PRKCG 0.999823679633206 0.000176320335587395 3.12064387772058e-11 protein kinase C gamma FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress (By similarity). Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component ARNTL/BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock (By similarity). {ECO:0000250|UniProtKB:P63318, ECO:0000250|UniProtKB:P63319, ECO:0000269|PubMed:16377624}.; DISEASE: Spinocerebellar ataxia 14 (SCA14) [MIM:605361]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA14 is an autosomal dominant cerebellar ataxia (ADCA). {ECO:0000269|PubMed:12644968}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in Purkinje cells of the cerebellar cortex. {ECO:0000269|PubMed:12644968}.; amygdala;choroid;fovea centralis;lens;retina;optic nerve;lung;hippocampus;macula lutea;testis;kidney;brain;thymus; amygdala;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.37267 0.71487 -0.712684326 14.49634348 107.94314 2.25670 PRKCH 0.99439017871354 0.00560982009492727 1.19153273456406e-09 protein kinase C eta FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in the regulation of cell differentiation in keratinocytes and pre-B cell receptor, mediates regulation of epithelial tight junction integrity and foam cell formation, and is required for glioblastoma proliferation and apoptosis prevention in MCF-7 cells. In keratinocytes, binds and activates the tyrosine kinase FYN, which in turn blocks epidermal growth factor receptor (EGFR) signaling and leads to keratinocyte growth arrest and differentiation. Associates with the cyclin CCNE1-CDK2-CDKN1B complex and inhibits CDK2 kinase activity, leading to RB1 dephosphorylation and thereby G1 arrest in keratinocytes. In association with RALA activates actin depolymerization, which is necessary for keratinocyte differentiation. In the pre-B cell receptor signaling, functions downstream of BLNK by up-regulating IRF4, which in turn activates L chain gene rearrangement. Regulates epithelial tight junctions (TJs) by phosphorylating occludin (OCLN) on threonine residues, which is necessary for the assembly and maintenance of TJs. In association with PLD2 and via TLR4 signaling, is involved in lipopolysaccharide (LPS)-induced RGS2 down-regulation and foam cell formation. Upon PMA stimulation, mediates glioblastoma cell proliferation by activating the mTOR pathway, the PI3K/AKT pathway and the ERK1- dependent phosphorylation of ELK1. Involved in the protection of glioblastoma cells from irradiation-induced apoptosis by preventing caspase-9 activation. In camptothecin-treated MCF-7 cells, regulates NF-kappa-B upstream signaling by activating IKBKB, and confers protection against DNA damage-induced apoptosis. Promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria. Phosphorylates ATF2 which promotes its nuclear retention and transcriptional activity and negatively regulates its mitochondrial localization. {ECO:0000269|PubMed:10806212, ECO:0000269|PubMed:11112424, ECO:0000269|PubMed:11772428, ECO:0000269|PubMed:15489897, ECO:0000269|PubMed:17146445, ECO:0000269|PubMed:18780722, ECO:0000269|PubMed:19114660, ECO:0000269|PubMed:20558593, ECO:0000269|PubMed:21820409, ECO:0000269|PubMed:22304920}.; DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. {ECO:0000269|PubMed:17206144}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Most abundant in lung, less in heart and skin. {ECO:0000269|PubMed:1986216}.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;islets of Langerhans;blood;breast;lung;nasopharynx;placenta;macula lutea;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.45961 0.29090 -0.44448505 24.46331682 401.95149 4.20569 PRKCI 0.253553082477709 0.746436438168861 1.04793534304081e-05 protein kinase C iota FUNCTION: Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI(3)K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non- small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis. {ECO:0000269|PubMed:10356400, ECO:0000269|PubMed:10467349, ECO:0000269|PubMed:10906326, ECO:0000269|PubMed:11042363, ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:12871960, ECO:0000269|PubMed:14684752, ECO:0000269|PubMed:15994303, ECO:0000269|PubMed:18270268, ECO:0000269|PubMed:19327373, ECO:0000269|PubMed:21189248, ECO:0000269|PubMed:21419810, ECO:0000269|PubMed:8226978, ECO:0000269|PubMed:9346882}.; . TISSUE SPECIFICITY: Predominantly expressed in lung and brain, but also expressed at lower levels in many tissues including pancreatic islets. Highly expressed in non-small cell lung cancers. {ECO:0000269|PubMed:15994303, ECO:0000269|PubMed:7607695, ECO:0000269|PubMed:8226978}.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;spinal cord;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;duodenum;kidney;mammary gland;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;subthalamic nucleus;prefrontal cortex;appendix;globus pallidus;atrioventricular node;parietal lobe; 0.74881 . -0.890882376 10.30313753 31.41088 0.99036 PRKCQ 0.967595405937699 0.0324045760943864 1.7967915009927e-08 protein kinase C theta FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that mediates non- redundant functions in T-cell receptor (TCR) signaling, including T-cells activation, proliferation, differentiation and survival, by mediating activation of multiple transcription factors such as NF-kappa-B, JUN, NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells, is required for the activation of NF-kappa-B and JUN, which in turn are essential for IL2 production, and participates to the calcium-dependent NFATC1 and NFATC2 transactivation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on several serine residues, inducing CARD11 association with lipid rafts and recruitment of the BCL10-MALT1 complex, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. May also play an indirect role in activation of the non- canonical NF-kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN activation, acts by phosphorylating the mediator STK39/SPAK and may not act through MAP kinases signaling. Plays a critical role in TCR/CD28-induced NFATC1 and NFATC2 transactivation by participating in the regulation of reduced inositol 1,4,5-trisphosphate generation and intracellular calcium mobilization. After costimulation of T-cells through CD28 can phosphorylate CBLB and is required for the ubiquitination and subsequent degradation of CBLB, which is a prerequisite for the activation of TCR. During T-cells differentiation, plays an important role in the development of T-helper 2 (Th2) cells following immune and inflammatory responses, and, in the development of inflammatory autoimmune diseases, is necessary for the activation of IL17-producing Th17 cells. May play a minor role in Th1 response. Upon TCR stimulation, mediates T-cell protective survival signal by phosphorylating BAD, thus protecting T-cells from BAD-induced apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-kappa-B and JUN pathways. In platelets, regulates signal transduction downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors, playing a positive role in 'outside-in' signaling and granule secretion signal transduction. May relay signals from the activated ITGA2B receptor by regulating the uncoupling of WASP and WIPF1, thereby permitting the regulation of actin filament nucleation and branching activity of the Arp2/3 complex. May mediate inhibitory effects of free fatty acids on insulin signaling by phosphorylating IRS1, which in turn blocks IRS1 tyrosine phosphorylation and downstream activation of the PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at 'Ser-504' and 'Ser-532' and negatively regulates its ability to phosphorylate PKB/AKT1. {ECO:0000269|PubMed:11342610, ECO:0000269|PubMed:14988727, ECO:0000269|PubMed:15364919, ECO:0000269|PubMed:16252004, ECO:0000269|PubMed:16356855, ECO:0000269|PubMed:16709830, ECO:0000269|PubMed:19549985, ECO:0000269|PubMed:8657160}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, T-cells, megakaryoblastic cells and platelets. {ECO:0000269|PubMed:7686153}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;colon;skin;skeletal muscle;uterus;prostate;lung;epididymis;thyroid;liver;testis;stomach;thymus; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.67010 0.45889 -0.378346116 28.01368247 672.23761 5.18050 PRKCQ-AS1 . . . PRKCQ antisense RNA 1 . . . . . . . . . . . PRKCSH 0.140789247885124 0.859041031928231 0.000169720186644113 protein kinase C substrate 80K-H FUNCTION: Regulatory subunit of glucosidase II. {ECO:0000269|PubMed:10929008}.; DISEASE: Polycystic liver disease (PCLD) [MIM:174050]: A hepatobiliary disease characterized by overgrowth of biliary epithelium and supportive connective tissue, resulting in multiple liver cysts. {ECO:0000269|PubMed:12529853, ECO:0000269|PubMed:12577059}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;synovium;thyroid;iris;pituitary gland;testis;amniotic fluid;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; prostate;medulla oblongata;superior cervical ganglion;trachea;thyroid;placenta;liver;prefrontal cortex;kidney;parietal lobe; 0.16464 0.13839 -0.885424753 10.4623732 5083.65004 14.60095 PRKCZ 0.266923656763182 0.732849004761263 0.000227338475555452 protein kinase C zeta FUNCTION: Calcium- and diacylglycerol-independent serine/threonine-protein kinase that functions in phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated protein (MAP) kinase cascade, and is involved in NF-kappa-B activation, mitogenic signaling, cell proliferation, cell polarity, inflammatory response and maintenance of long-term potentiation (LTP). Upon lipopolysaccharide (LPS) treatment in macrophages, or following mitogenic stimuli, functions downstream of PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade independently of RAF1 activation. Required for insulin-dependent activation of AKT3, but may function as an adapter rather than a direct activator. Upon insulin treatment may act as a downstream effector of PI3K and contribute to the activation of translocation of the glucose transporter SLC2A4/GLUT4 and subsequent glucose transport in adipocytes. In EGF-induced cells, binds and activates MAP2K5/MEK5-MAPK7/ERK5 independently of its kinase activity and can activate JUN promoter through MEF2C. Through binding with SQSTM1/p62, functions in interleukin-1 signaling and activation of NF-kappa-B with the specific adapters RIPK1 and TRAF6. Participates in TNF-dependent transactivation of NF-kappa-B by phosphorylating and activating IKBKB kinase, which in turn leads to the degradation of NF-kappa-B inhibitors. In migrating astrocytes, forms a cytoplasmic complex with PARD6A and is recruited by CDC42 to function in the establishment of cell polarity along with the microtubule motor and dynein. In association with FEZ1, stimulates neuronal differentiation in PC12 cells. In the inflammatory response, is required for the T-helper 2 (Th2) differentiation process, including interleukin production, efficient activation of JAK1 and the subsequent phosphorylation and nuclear translocation of STAT6. May be involved in development of allergic airway inflammation (asthma), a process dependent on Th2 immune response. In the NF-kappa-B-mediated inflammatory response, can relieve SETD6-dependent repression of NF-kappa-B target genes by phosphorylating the RELA subunit at 'Ser-311'. Necessary and sufficient for LTP maintenance in hippocampal CA1 pyramidal cells. In vein endothelial cells treated with the oxidant peroxynitrite, phosphorylates STK11 leading to nuclear export of STK11, subsequent inhibition of PI3K/Akt signaling, and increased apoptosis. Phosphorylates VAMP2 in vitro (PubMed:17313651). {ECO:0000269|PubMed:11035106, ECO:0000269|PubMed:12162751, ECO:0000269|PubMed:15084291, ECO:0000269|PubMed:15324659, ECO:0000269|PubMed:17313651, ECO:0000269|PubMed:18321849, ECO:0000269|PubMed:9447975}.; . TISSUE SPECIFICITY: Expressed in brain, and to a lesser extent in lung, kidney and testis.; . . 0.19321 0.44770 -0.975433863 8.852323661 63.44396 1.63119 PRKD1 2.12624005070963e-05 0.998935897044072 0.00104284055542056 protein kinase D1 FUNCTION: Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. Phosphorylates the epidermal growth factor receptor (EGFR) on dual threonine residues, which leads to the suppression of epidermal growth factor (EGF)-induced MAPK8/JNK1 activation and subsequent JUN phosphorylation. Phosphorylates RIN1, inducing RIN1 binding to 14-3-3 proteins YWHAB, YWHAE and YWHAZ and increased competition with RAF1 for binding to GTP-bound form of Ras proteins (NRAS, HRAS and KRAS). Acts downstream of the heterotrimeric G-protein beta/gamma-subunit complex to maintain the structural integrity of the Golgi membranes, and is required for protein transport along the secretory pathway. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane. May act by activating the lipid kinase phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the local synthesis of phosphorylated inositol lipids, which induces a sequential production of DAG, phosphatidic acid (PA) and lyso-PA (LPA) that are necessary for membrane fission and generation of specific transport carriers to the cell surface. Under oxidative stress, is phosphorylated at Tyr-463 via SRC-ABL1 and contributes to cell survival by activating IKK complex and subsequent nuclear translocation and activation of NFKB1. Involved in cell migration by regulating integrin alpha-5/beta-3 recycling and promoting its recruitment in newly forming focal adhesion. In osteoblast differentiation, mediates the bone morphogenic protein 2 (BMP2)- induced nuclear export of HDAC7, which results in the inhibition of HDAC7 transcriptional repression of RUNX2. In neurons, plays an important role in neuronal polarity by regulating the biogenesis of TGN-derived dendritic vesicles, and is involved in the maintenance of dendritic arborization and Golgi structure in hippocampal cells. May potentiate mitogenesis induced by the neuropeptide bombesin or vasopressin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. Plays an important role in the proliferative response induced by low calcium in keratinocytes, through sustained activation of MAPK1/3 (ERK1/2) pathway. Downstream of novel PKC signaling, plays a role in cardiac hypertrophy by phosphorylating HDAC5, which in turn triggers XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A transcriptional activation and induction of downstream target genes that promote myocyte hypertrophy and pathological cardiac remodeling. Mediates cardiac troponin I (TNNI3) phosphorylation at the PKA sites, which results in reduced myofilament calcium sensitivity, and accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway is also involved in angiogenesis by mediating VEGFA-induced specific subset of gene expression, cell migration, and tube formation. In response to VEGFA, is necessary and required for HDAC7 phosphorylation which induces HDAC7 nuclear export and endothelial cell proliferation and migration. During apoptosis induced by cytarabine and other genotoxic agents, PRKD1 is cleaved by caspase-3 at Asp-378, resulting in activation of its kinase function and increased sensitivity of cells to the cytotoxic effects of genotoxic agents. In epithelial cells, is required for transducing flagellin-stimulated inflammatory responses by binding and phosphorylating TLR5, which contributes to MAPK14/p38 activation and production of inflammatory cytokines. May play a role in inflammatory response by mediating activation of NF-kappa- B. May be involved in pain transmission by directly modulating TRPV1 receptor. {ECO:0000269|PubMed:10523301, ECO:0000269|PubMed:10764790, ECO:0000269|PubMed:12505989, ECO:0000269|PubMed:12637538, ECO:0000269|PubMed:15471852, ECO:0000269|PubMed:17442957, ECO:0000269|PubMed:18332134, ECO:0000269|PubMed:18509061, ECO:0000269|PubMed:19135240, ECO:0000269|PubMed:19211839}.; . . unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;frontal lobe;thyroid;bone;macula lutea;liver;amnion;testis;brain;stomach; dorsal root ganglion;superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion; 0.26789 0.67432 -0.949752638 9.32413305 568.0914 4.83722 PRKD2 0.9996964074254 0.000303592457339082 1.17260401134187e-10 protein kinase D2 FUNCTION: Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress- induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. In response to oxidative stress, is phosphorylated at Tyr-438 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B. In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77. Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation. During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens. In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF- kappa-B-dependent pathway. During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane. Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis. In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN. Downstream of PRKCA, plays important roles in angiotensin-2- induced monocyte adhesion to endothelial cells. Plays a regulatory role in angiogenesis and tumor growth by phosphorylating a downstream mediator CIB1 isoform 2, resulting in vascular endothelial growth factor A (VEGFA) secretion. {ECO:0000269|PubMed:14743217, ECO:0000269|PubMed:15604256, ECO:0000269|PubMed:16928771, ECO:0000269|PubMed:17077180, ECO:0000269|PubMed:17951978, ECO:0000269|PubMed:17962809, ECO:0000269|PubMed:18262756, ECO:0000269|PubMed:19001381, ECO:0000269|PubMed:19192391, ECO:0000269|PubMed:23503467}.; . TISSUE SPECIFICITY: Widely expressed.; lymphoreticular;umbilical cord;ovary;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;bone;thyroid;iris;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;bile duct;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; prostate;superior cervical ganglion;lung;heart;thyroid;ciliary ganglion;trigeminal ganglion;whole blood;thymus; 0.09498 0.26572 -0.731092527 14.13658882 199.04525 3.04956 PRKD3 0.00807565614889671 0.991899872844524 2.44710065797706e-05 protein kinase D3 FUNCTION: Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;alveolus;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;adrenal cortex;testis;white blood cells;ciliary ganglion;trigeminal ganglion;tonsil; 0.19522 0.30524 0.135991087 63.61759849 843.24858 5.68444 PRKDC 1 1.81599980515305e-17 1.21320819340433e-45 protein kinase, DNA-activated, catalytic polypeptide FUNCTION: Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Required to protect and align broken ends of DNA. May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, SRF, XRCC1, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D. Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein stability, most likely through an indirect machanism. Interacts with CRY1 and CRY2; negatively regulates CRY1 phosphorylation. {ECO:0000269|PubMed:12649176, ECO:0000269|PubMed:14734805, ECO:0000269|PubMed:15574326, ECO:0000269|PubMed:9679063}.; DISEASE: Immunodeficiency 26 with or without neurologic abnormalities (IMD26) [MIM:615966]: A form of severe combined immunodeficiency characterized by reduced or absent T and B cells, recurrent candidiasis, and lower respiratory tract infections. Some patients show dysmorphic features, severe growth failure, microcephaly, seizures, and impaired neurological functions. {ECO:0000269|PubMed:19075392, ECO:0000269|PubMed:23722905}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;gum;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;urinary;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;amnion;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;tumor;ciliary ganglion;trigeminal ganglion; 0.74641 0.66512 . . 1205.70001 6.57755 PRKG1 0.999743687068331 0.000256312854037606 7.76315587775674e-11 protein kinase, cGMP-dependent, type I FUNCTION: Serine/threonine protein kinase that acts as key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates MRVI1/IRAG and inhibits IP3- induced Ca(2+) release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca(2+) levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle. {ECO:0000269|PubMed:10567269, ECO:0000269|PubMed:11162591, ECO:0000269|PubMed:11723116, ECO:0000269|PubMed:12082086, ECO:0000269|PubMed:14608379, ECO:0000269|PubMed:15194681, ECO:0000269|PubMed:16990611, ECO:0000269|PubMed:8182057}.; DISEASE: Aortic aneurysm, familial thoracic 8 (AAT8) [MIM:615436]: A disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance. {ECO:0000269|PubMed:23910461}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Primarily expressed in lung and placenta. {ECO:0000269|PubMed:9192852}.; unclassifiable (Anatomical System);uterus;whole body;heart;artery;skin;aorta; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;caudate nucleus;pons;atrioventricular node;trigeminal ganglion;cerebellum; 0.98705 0.70722 -0.799052816 12.45576787 316.60592 3.77988 PRKG1-AS1 . . . PRKG1 antisense RNA 1 . . . . . . . . . . . PRKG2 0.449903081101253 0.550094731846985 2.18705176245959e-06 protein kinase, cGMP-dependent, type II . . TISSUE SPECIFICITY: Highly concentrated in brain, lung and intestinal mucosa.; uterus;lung;heart;testis;skin;skeletal muscle; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.27705 0.22346 -0.844966979 11.1759849 29.92466 0.95563 PRKRA 0.15454198723567 0.829025006366981 0.0164330063973493 protein activator of interferon induced protein kinase EIF2AK2 FUNCTION: Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by DICER1 and for subsequent siRNA-mediated post- transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by DICER1. Promotes UBC9-p53/TP53 association and sumoylation and phosphorylation of p53/TP53 at 'Lys-386' at 'Ser-392' respectively and enhances its activity in a EIF2AK2/PKR-dependent manner (By similarity). {ECO:0000250, ECO:0000269|PubMed:10336432, ECO:0000269|PubMed:11238927, ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:16982605, ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:9687506}.; DISEASE: Dystonia 16 (DYT16) [MIM:612067]: An early-onset dystonia-parkinsonism disorder. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. DYT16 patients have progressive, generalized dystonia with axial muscle involvement, oro-mandibular (sardonic smile) and laryngeal dystonia and, in some cases, parkinsonian features. {ECO:0000269|PubMed:18243799, ECO:0000269|PubMed:18420150}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;hypopharynx;liver;spleen;head and neck;cervix;kidney;stomach; . 0.40361 0.17821 0.325313577 73.11276244 2234.66098 8.71369 PRKRAP1 . . . protein activator of interferon induced protein kinase EIF2AK2 pseudogene 1 . . . . . . . . . . . PRKRIP1 0.000394800445184658 0.846551843353932 0.153053356200884 PRKR interacting protein 1 (IL11 inducible) FUNCTION: Binds double-stranded RNA. Inhibits EIF2AK2 kinase activity (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; testis;skeletal muscle; 0.12987 . 0.170987912 65.5579146 322.92264 3.81768 PRKX 0.221428117908246 0.741629719599076 0.0369421624926784 protein kinase, X-linked FUNCTION: Serine/threonine protein kinase regulated by and mediating cAMP signaling in cells. Acts through phosphorylation of downstream targets that may include CREB, SMAD6 and PKD1 and has multiple functions in cellular differentiation and epithelial morphogenesis. Regulates myeloid cell differentiation through SMAD6 phosphorylation. Involved in nephrogenesis by stimulating renal epithelial cell migration and tubulogenesis. Also involved in angiogenesis through stimulation of endothelial cell proliferation, migration and vascular-like structure formation. {ECO:0000269|PubMed:12082174, ECO:0000269|PubMed:16236808, ECO:0000269|PubMed:16491121, ECO:0000269|PubMed:17980165, ECO:0000269|PubMed:19367327, ECO:0000269|PubMed:21684272, ECO:0000269|PubMed:9860982}.; DISEASE: Note=A chromosomal aberration involving PRKX is a cause of sex reversal disorder. Translocation t(X;Y)(p22;p11) with PRKY. Chromosomal translocations proximal to PRKY account for about 30% of the cases of sex reversal disorder in XX males and XY females.; TISSUE SPECIFICITY: Widely expressed (at protein level). Specifically expressed in blood by macrophages and granulocytes according to PubMed:9860982. {ECO:0000269|PubMed:15879576, ECO:0000269|PubMed:16236808, ECO:0000269|PubMed:7633447, ECO:0000269|PubMed:9860982}.; unclassifiable (Anatomical System);lymphoreticular;ovary;lacrimal gland;salivary gland;intestine;pharynx;colon;parathyroid;blood;skin;skeletal muscle;breast;uterus;prostate;whole body;lung;placenta;liver;testis;kidney;brain;bladder; superior cervical ganglion;thyroid;testis;trigeminal ganglion; . 0.10088 -0.471992905 23.03609342 12.00432 0.43572 PRKX-AS1 . . . PRKX antisense RNA 1 . . . . . . . . . . . PRKXP1 . . . protein kinase, X-linked, pseudogene 1 . . . . . . . . . . . PRKXP2 . . . protein kinase, X-linked, pseudogene 2 . . . . . . . . . . . PRKY . . . protein kinase, Y-linked, pseudogene . . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12815422}.; . . 0.12841 0.11541 . . . . PRL 0.00264110170025645 0.934524788521353 0.0628341097783905 prolactin FUNCTION: Prolactin acts primarily on the mammary gland by promoting lactation.; . . unclassifiable (Anatomical System);smooth muscle;fovea centralis;choroid;lens;retina;uterus;optic nerve;lung;cerebral cortex;placenta;macula lutea;alveolus;liver;pituitary gland;testis;spleen;brain; uterus corpus;superior cervical ganglion;placenta;atrioventricular node;trigeminal ganglion;pituitary; 0.19259 0.85447 -0.161524709 41.6430762 24.58098 0.80792 PRLH 0.0401709303704193 0.649570461543791 0.31025860808579 prolactin releasing hormone FUNCTION: Stimulates prolactin (PRL) release and regulates the expression of prolactin through its receptor GPR10. May stimulate lactotrophs directly to secrete PRL.; . TISSUE SPECIFICITY: Medulla oblongata and hypothalamus. {ECO:0000269|PubMed:10498338}.; . . 0.09604 0.13752 -0.295622497 32.61972163 26.46551 0.85660 PRLHR 0.000426453630646031 0.413912411336615 0.585661135032739 prolactin releasing hormone receptor FUNCTION: Receptor for prolactin-releasing peptide (PrRP). Implicated in lactation, regulation of food intake and pain-signal processing.; . TISSUE SPECIFICITY: Only detected in the pituitary gland and in all cell types of pituitary adenomas. {ECO:0000269|PubMed:10498338, ECO:0000269|PubMed:11923475}.; unclassifiable (Anatomical System); . 0.19460 0.14591 0.461228372 78.46190139 251.29074 3.41495 PRLR 0.916128016014322 0.0838482139324899 2.37700531879014e-05 prolactin receptor FUNCTION: This is a receptor for the anterior pituitary hormone prolactin (PRL). Acts as a prosurvival factor for spermatozoa by inhibiting sperm capacitation through suppression of SRC kinase activation and stimulation of AKT. Isoform 4 is unable to transduce prolactin signaling. Isoform 6 is unable to transduce prolactin signaling. {ECO:0000269|PubMed:12580759, ECO:0000269|PubMed:20032052}.; DISEASE: Multiple fibroadenomas of the breast (MFAB) [MIM:615554]: A benign breast disease marked by lobuloalveolar growth with abnormally high proliferation of the epithelium, and characterized by the presence of more than 3 fibroadenomas in one breast. Fibroadenomas are adenomas containing fibrous tissue. {ECO:0000269|PubMed:18779591}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hyperprolactinemia (HPRL) [MIM:615555]: A disorder characterized by increased levels of prolactin in the blood not associated with gestation or the puerperium. HPRL may result in infertility, hypogonadism, and galactorrhea. {ECO:0000269|PubMed:24195502}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in breast, placenta, kidney, liver and pancreas. {ECO:0000269|PubMed:11518703, ECO:0000269|PubMed:12580759}.; unclassifiable (Anatomical System);ovary;colon;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;breast;optic nerve;placenta;macula lutea;liver;spleen;kidney; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07595 0.38344 0.020302773 55.60863411 347.86975 3.95295 PRM1 0.371061724240126 0.580945573627771 0.0479927021321035 protamine 1 FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.; . TISSUE SPECIFICITY: Testis.; unclassifiable (Anatomical System);medulla oblongata;placenta;testis; testis - interstitial;testis - seminiferous tubule;testis; 0.00810 0.03676 0.347360312 73.97381458 15.15519 0.54510 PRM2 0.108047166399074 0.776274403285227 0.115678430315699 protamine 2 FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.; . TISSUE SPECIFICITY: Testis.; unclassifiable (Anatomical System);medulla oblongata;lung;epididymis;placenta;hippocampus;testis;kidney;brain; superior cervical ganglion;uterus corpus;testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.04646 0.08130 -0.251530012 35.42108988 7.00767 0.26200 PRM3 . . . protamine 3 FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex (By similarity). {ECO:0000250}.; . . . . 0.18725 0.10186 . . 12.87986 0.46948 PRMT1 0.993587786937211 0.0064112279104797 9.85152309287171e-07 protein arginine methyltransferase 1 FUNCTION: Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, PIAS1, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15 and EWS. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. Together with dimethylated PIAS1, represses STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway. Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity. Methylates CHTOP and this methylation is critical for its 5-hydroxymethylcytosine (5hmC)-binding activity (PubMed:25284789). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (PubMed:25284789). {ECO:0000269|PubMed:11387442, ECO:0000269|PubMed:11448779, ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:18320585, ECO:0000269|PubMed:18657504, ECO:0000269|PubMed:18773938, ECO:0000269|PubMed:19124016, ECO:0000269|PubMed:19136629, ECO:0000269|PubMed:19405910, ECO:0000269|PubMed:20442406, ECO:0000269|PubMed:25284789}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11097842}.; . . 0.91947 0.45920 -0.560178693 19.30879925 19.62667 0.67361 PRMT1P1 . . . protein arginine methyltransferase 1 pseudogene 1 . . . . . . . . . . . PRMT2 0.751420208347907 0.248489641325407 9.01503266864357e-05 protein arginine methyltransferase 2 FUNCTION: Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as STAT3, FBL, histone H4. Acts as a coactivator (with NCOA2) of the androgen receptor (AR)-mediated transactivation. Acts as a coactivator (with estrogen) of estrogen receptor (ER)-mediated transactivation. Enhances PGR, PPARG, RARA-mediated transactivation. May inhibit NF-kappa-B transcription and promote apoptosis. Represses E2F1 transcriptional activity (in a RB1- dependent manner). May be involved in growth regulation. {ECO:0000269|PubMed:12039952, ECO:0000269|PubMed:16648481, ECO:0000269|PubMed:17587566, ECO:0000269|PubMed:19405910}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in androgen target organs such as heart, prostate, skeletal muscle, ovary and spinal cord. {ECO:0000269|PubMed:17587566}.; lymphoreticular;myocardium;medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;ganglion;frontal lobe;endometrium;iris;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;synovium;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17325 0.23530 -0.023789244 52.09365416 19.90658 0.67777 PRMT3 6.29172115448445e-12 0.115489076198462 0.884510923795246 protein arginine methyltransferase 3 FUNCTION: Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;prostate;whole body;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;hypothalamus;pharynx;blood;skeletal muscle;breast;lung;cornea;placenta;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach;aorta; superior cervical ganglion; 0.23154 0.15949 -0.378346116 28.01368247 700.70181 5.26775 PRMT5 0.994806432825256 0.00519356229728782 4.87745644622573e-09 protein arginine methyltransferase 5 FUNCTION: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA (PubMed:10531356, PubMed:11152681, PubMed:11747828, PubMed:12411503, PubMed:15737618, PubMed:17709427, PubMed:20159986, PubMed:20810653, PubMed:21258366, PubMed:21917714, PubMed:22269951). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles (PubMed:12411503, PubMed:11747828, PubMed:17709427). Methylates SUPT5H (PubMed:12718890). Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (By similarity). Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation (PubMed:21917714, PubMed:21258366). Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity (PubMed:21917714). Required for induction of E- selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9 (PubMed:22269951). Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (PubMed:20810653). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (By similarity). Methylates GM130/GOLGA2, regulating Golgi ribbon formation (PubMed:20421892). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (PubMed:25284789). {ECO:0000250|UniProtKB:Q8CIG8, ECO:0000269|PubMed:10531356, ECO:0000269|PubMed:11152681, ECO:0000269|PubMed:11747828, ECO:0000269|PubMed:12411503, ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:15737618, ECO:0000269|PubMed:17709427, ECO:0000269|PubMed:20159986, ECO:0000269|PubMed:20421892, ECO:0000269|PubMed:20810653, ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:22269951, ECO:0000269|PubMed:25284789}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9556550}.; lymphoreticular;medulla oblongata;ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;synovium;larynx;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;muscle;blood;lens;breast;bile duct;pancreas;lung;placenta;visual apparatus;amnion;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; whole brain;tumor; 0.56106 0.31456 -0.558357437 19.54470394 11.30815 0.40685 PRMT5-AS1 . . . PRMT5 antisense RNA 1 . . . . . . . . . . . PRMT5P1 . . . protein arginine methyltransferase 5 pseudogene 1 . . . . . . . . . . . PRMT6 0.0241276210660794 0.915022469304837 0.060849909629084 protein arginine methyltransferase 6 FUNCTION: Arginine methyltransferase that can catalyze the formation of both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA. Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates. Specifically mediates the asymmetric dimethylation of histone H3 'Arg-2' to form H3R2me2a. H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3). Acts as a transcriptional repressor of various genes such as HOXA2, THBS1 and TP53. Repression of TP53 blocks cellular senescence (By similarity). Also methylates histone H2A and H4 'Arg-3' (H2AR3me and H4R3me, respectively). Acts as a regulator of DNA base excision during DNA repair by mediating the methylation of DNA polymerase beta (POLB), leading to the stimulation of its polymerase activity by enhancing DNA binding and processivity. Methylates HMGA1. Regulates alternative splicing events. Acts as a transcriptional coactivator of a number of steroid hormone receptors including ESR1, ESR2, PGR and NR3C1. Promotes fasting- induced transcriptional activation of the gluconeogenic program through methylation of the CRTC2 transcription coactivator. May play a role in innate immunity against HIV-1 in case of infection by methylating and impairing the function of various HIV-1 proteins such as Tat, Rev and Nucleocapsid protein p7 (NC). {ECO:0000250, ECO:0000269|PubMed:11724789, ECO:0000269|PubMed:16157300, ECO:0000269|PubMed:16159886, ECO:0000269|PubMed:16600869, ECO:0000269|PubMed:17267505, ECO:0000269|PubMed:17898714, ECO:0000269|PubMed:18077460, ECO:0000269|PubMed:18079182, ECO:0000269|PubMed:19405910, ECO:0000269|PubMed:19509293, ECO:0000269|PubMed:20047962}.; . TISSUE SPECIFICITY: Highly expressed in kidney and testis. {ECO:0000269|PubMed:11724789}.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland; . 0.27476 0.20163 -0.404032746 26.53338051 1147.42125 6.45509 PRMT7 8.30563679212495e-09 0.895222115412009 0.104777876282354 protein arginine methyltransferase 7 FUNCTION: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo. {ECO:0000269|PubMed:15044439, ECO:0000269|PubMed:15494416, ECO:0000269|PubMed:17709427, ECO:0000269|PubMed:19110445}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;brain;tonsil;unclassifiable (Anatomical System);heart;pharynx;blood;lens;skeletal muscle;bile duct;lung;cornea;placenta;macula lutea;visual apparatus;duodenum;liver;head and neck;cervix;kidney;mammary gland;stomach; globus pallidus;skeletal muscle; 0.04723 0.11983 -1.903381992 1.94621373 52.71496 1.43803 PRMT8 0.95875274427484 0.0412277301503571 1.95255748025898e-05 protein arginine methyltransferase 8 FUNCTION: Membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS. {ECO:0000269|PubMed:16051612, ECO:0000269|PubMed:17925405, ECO:0000269|PubMed:18320585}.; . TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:16051612}.; unclassifiable (Anatomical System);lung;testis;kidney;brain; superior cervical ganglion;medulla oblongata;globus pallidus;pons;trigeminal ganglion;parietal lobe; 0.25910 0.12839 -0.405853867 26.23260203 7.75661 0.28589 PRMT9 . . . protein arginine methyltransferase 9 . . . . . . . -0.837696902 11.45317292 . . PRNCR1 . . . prostate cancer associated non-coding RNA 1 . . . . . . . . . . . PRND 0.0677966552935181 0.734681312586782 0.1975220321197 prion protein 2 (dublet) . . TISSUE SPECIFICITY: Expressed in testis.; unclassifiable (Anatomical System);heart;choroid;fovea centralis;lens;skin;retina;uterus;prostate;optic nerve;lung;macula lutea;testis;brain; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion; 0.15208 0.17393 0.305084559 72.22811984 2560.16195 9.44580 PRNP 0.0291390272600768 0.803668524007551 0.167192448732373 prion protein . . TISSUE SPECIFICITY: Detected in brain homogenate, primary neurons, and peripheral blood mononuclear cells (at protein level). {ECO:0000269|PubMed:21478263}.; . . 0.31838 0.66436 0.371224249 75.12384996 2023.08584 8.27581 PRNT 0.105498859424942 0.590560887112804 0.303940253462254 prion protein (testis specific) . . TISSUE SPECIFICITY: Specifically expressed in adult testis. {ECO:0000269|PubMed:12514748}.; lung;testis; . 0.05630 . . . 6.95921 0.25941 PROB1 . . . proline-rich basic protein 1 . . . . . . . . . 4358.91898 13.17274 PROC 0.0324754428971477 0.958525310004276 0.00899924709857677 protein C, inactivator of coagulation factors Va and VIIIa FUNCTION: Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids (PubMed:25618265). Exerts a protective effect on the endothelial cell barrier function (PubMed:25651845). {ECO:0000269|PubMed:25618265, ECO:0000269|PubMed:25651845}.; DISEASE: Thrombophilia due to protein C deficiency, autosomal dominant (THPH3) [MIM:176860]: A hemostatic disorder characterized by impaired regulation of blood coagulation and a tendency to recurrent venous thrombosis. Individuals with decreased amounts of protein C are classically referred to as having type I protein C deficiency and those with normal amounts of a functionally defective protein as having type II deficiency. {ECO:0000269|PubMed:1301959, ECO:0000269|PubMed:1347706, ECO:0000269|PubMed:1511989, ECO:0000269|PubMed:1868249, ECO:0000269|PubMed:2437584, ECO:0000269|PubMed:25618265, ECO:0000269|PubMed:25748729, ECO:0000269|PubMed:2602169, ECO:0000269|PubMed:7792728, ECO:0000269|PubMed:7865674, ECO:0000269|PubMed:8292730, ECO:0000269|PubMed:8398832, ECO:0000269|PubMed:8499568, ECO:0000269|PubMed:8560401, ECO:0000269|PubMed:8829639, ECO:0000269|PubMed:9798967}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Thrombophilia due to protein C deficiency, autosomal recessive (THPH4) [MIM:612304]: A hemostatic disorder characterized by impaired regulation of blood coagulation and a tendency to recurrent venous thrombosis. It results in a thrombotic condition that can manifest as a severe neonatal disorder or as a milder disorder with late-onset thrombophilia. The severe form leads to neonatal death through massive neonatal venous thrombosis. Often associated with ecchymotic skin lesions which can turn necrotic called purpura fulminans, this disorder is very rare. {ECO:0000269|PubMed:1511988, ECO:0000269|PubMed:1593215, ECO:0000269|PubMed:1611081, ECO:0000269|PubMed:25618265, ECO:0000269|PubMed:7841323, ECO:0000269|PubMed:7841324, ECO:0000269|PubMed:7878626}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma; synthesized in the liver.; unclassifiable (Anatomical System);lung;liver;colon;spleen;kidney;stomach; superior cervical ganglion;fetal liver;liver;fetal lung;atrioventricular node;kidney; 0.52932 0.65749 -0.602450568 17.91106393 81.15217 1.90713 PROCA1 0.00087615119311804 0.793462519586145 0.205661329220737 protein interacting with cyclin A1 . . . unclassifiable (Anatomical System);uterus;prostate;lung;ovary;testis;colon; . . . -0.159704656 41.90846898 80.87009 1.90024 PROCR 0.0101308888898987 0.825337126419437 0.164531984690664 protein C receptor FUNCTION: Binds activated protein C. Enhances protein C activation by the thrombin-thrombomodulin complex; plays a role in the protein C pathway controlling blood coagulation.; . TISSUE SPECIFICITY: Expressed strongly in the endothelial cells of arteries and veins in heart and lung, less intensely in capillaries in the lung and skin, and not at all in the endothelium of small vessels of the liver and kidney.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;oesophagus;bone;thyroid;dura mater;brain;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;muscle;lens;bile duct;breast;pancreas;pia mater;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; placenta;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05249 0.17609 -0.049474214 50.01179523 670.55985 5.17684 PRODH 4.75363149716848e-06 0.85161466673164 0.148380579636863 proline dehydrogenase (oxidase) 1 FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.; DISEASE: Hyperprolinemia 1 (HYRPRO1) [MIM:239500]: An inborn error of proline metabolism resulting in elevated levels of proline in the plasma and urine. The disorder is generally benign and most affected individuals are clinically asymptomatic. Some patients, however, have neurologic manifestations, including epilepsy and mental retardation. Association with certain forms of schizophrenia have been reported. {ECO:0000269|PubMed:12217952, ECO:0000269|PubMed:15662599, ECO:0000269|PubMed:17135275}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Schizophrenia 4 (SCZD4) [MIM:600850]: A complex, multifactorial psychotic disorder or group of disorders characterized by disturbances in the form and content of thought (e.g. delusions, hallucinations), in mood (e.g. inappropriate affect), in sense of self and relationship to the external world (e.g. loss of ego boundaries, withdrawal), and in behavior (e.g bizarre or apparently purposeless behavior). Although it affects emotions, it is distinguished from mood disorders in which such disturbances are primary. Similarly, there may be mild impairment of cognitive function, and it is distinguished from the dementias in which disturbed cognitive function is considered primary. Some patients manifest schizophrenic as well as bipolar disorder symptoms and are often given the diagnosis of schizoaffective disorder. {ECO:0000269|PubMed:11891283, ECO:0000269|PubMed:15662599}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in lung, skeletal muscle and brain, to a lesser extent in heart and kidney, and weakly in liver, placenta and pancreas.; choroid;fovea centralis;skin;retina;uterus;optic nerve;endometrium;thyroid;iris;testis;pineal gland;brain;unclassifiable (Anatomical System);small intestine;heart;cartilage;hypothalamus;lens;skeletal muscle;pancreas;lung;macula lutea;liver;mammary gland;stomach;cerebellum; amygdala;prefrontal cortex;pons; 0.66122 . 1.73619725 96.62656287 2500.61703 9.31868 PRODH2 7.20821354097691e-12 0.0663910639362009 0.933608936056591 proline dehydrogenase (oxidase) 2 FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate. {ECO:0000305}.; . . unclassifiable (Anatomical System);liver;spleen;kidney; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;pons;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; . . 0.271907863 70.73012503 587.70874 4.91708 PROK1 0.0206691663843015 0.748849298875198 0.230481534740501 prokineticin 1 FUNCTION: Potently contracts gastrointestinal (GI) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types. Induces proliferation and differentiation, but not migration, of enteric neural crest cells. Directly influences neuroblastoma progression by promoting the proliferation and migration of neuroblastoma cells. Positively regulates PTGS2 expression and prostaglandin synthesis. May play a role in placentation. May play a role in normal and pathological testis angiogenesis. {ECO:0000269|PubMed:11259612, ECO:0000269|PubMed:11528470, ECO:0000269|PubMed:15292351, ECO:0000269|PubMed:17289879, ECO:0000269|PubMed:18339712}.; . TISSUE SPECIFICITY: Localizes to glandular epithelium, stroma and vascular epithelial cells of first trimester decidua (at protein level). Up-regulated in first trimester decidua when compared with non-pregnant endometrium. Expressed in the steroidogenic glands, ovary, testis, adrenal and placenta. {ECO:0000269|PubMed:11528470, ECO:0000269|PubMed:15292351, ECO:0000269|PubMed:18339712}.; unclassifiable (Anatomical System);uterus;medulla oblongata;lung;ovary;placenta;iris;liver;testis;spleen;brain; superior cervical ganglion;testis - interstitial;ovary;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19484 0.12037 0.525552348 80.57914603 1701.02209 7.60357 PROK2 0.270454067222245 0.635500167847042 0.0940457649307127 prokineticin 2 FUNCTION: May function as an output molecule from the suprachiasmatic nucleus (SCN) that transmits behavioral circadian rhythm. May also function locally within the SCN to synchronize output. Potently contracts gastrointestinal (GI) smooth muscle.; DISEASE: Hypogonadotropic hypogonadism 4 with or without anosmia (HH4) [MIM:610628]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:17054399, ECO:0000269|PubMed:18559922, ECO:0000269|PubMed:23643382, ECO:0000269|PubMed:25077900}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. The genetics of hypogonadotropic hypogonadism involves various modes of transmission. Oligogenic inheritance has been reported in some patients carrying mutations in PROK2 as well as in other HH- associated genes including PROKR2 (PubMed:23643382). {ECO:0000269|PubMed:23643382}.; TISSUE SPECIFICITY: Expressed in the testis and, at low levels, in the small intestine.; unclassifiable (Anatomical System);placenta;colon;aorta;bone marrow; superior cervical ganglion;atrioventricular node;whole blood; 0.33111 0.12165 0.147123112 64.11299835 67.78822 1.70356 PROKR1 5.42251256340407e-10 0.00880443531975726 0.991195564137992 prokineticin receptor 1 FUNCTION: Receptor for prokineticin 1. Exclusively coupled to the G(q) subclass of heteromeric G proteins. Activation leads to mobilization of calcium, stimulation of phosphoinositide turnover and activation of p44/p42 mitogen-activated protein kinase. May play a role during early pregnancy. {ECO:0000269|PubMed:18339712}.; . TISSUE SPECIFICITY: Localizes to glandular epithelium, stroma and vascular endothelial cells of first trimester decidua (at protein level). Up-regulated in first trimester decidua when compared with non-pregnant endometrium. Expressed in the stomach, throughout the small intestine, colon, rectum, thyroid gland, pituitary gland, salivary gland, adrenal gland, testis, ovary, brain, spleen, prostate and pancreas. {ECO:0000269|PubMed:18339712}.; unclassifiable (Anatomical System); superior cervical ganglion;globus pallidus; 0.11983 0.12964 -0.488577883 22.64685067 219.45642 3.20513 PROKR2 0.000669053120174497 0.503920664373336 0.495410282506489 prokineticin receptor 2 FUNCTION: Receptor for prokineticin 2. Exclusively coupled to the G(q) subclass of heteromeric G proteins. Activation leads to mobilization of calcium, stimulation of phosphoinositide turnover and activation of p44/p42 mitogen-activated protein kinase.; . TISSUE SPECIFICITY: Expressed in the ileocecum, thyroid gland, pituitary gland, salivary gland, adrenal gland, testis, ovary and brain.; . . 0.16785 0.13372 -0.222203495 37.54423213 340.77102 3.91723 PROM1 7.17058540967505e-17 0.0278327981178301 0.97216720188217 prominin 1 FUNCTION: May play a role in cell differentiation, proliferation and apoptosis (PubMed:24556617). Binds cholesterol in cholesterol- containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenesis. Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner (PubMed:20818439). {ECO:0000269|PubMed:20818439, ECO:0000269|PubMed:24556617}.; DISEASE: Retinitis pigmentosa 41 (RP41) [MIM:612095]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:10587575, ECO:0000269|PubMed:17605048}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cone-rod dystrophy 12 (CORD12) [MIM:612657]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. {ECO:0000269|PubMed:18654668}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Stargardt disease 4 (STGD4) [MIM:603786]: A common hereditary macular degeneration. It is characterized by decreased central vision, atrophy of the macula and underlying retinal pigment epithelium, and frequent presence of prominent flecks in the posterior pole of the retina. {ECO:0000269|PubMed:18654668}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Retinal macular dystrophy 2 (MCDR2) [MIM:608051]: A bull's-eye macular dystrophy characterized by bilateral annular atrophy of retinal pigment epithelium at the macula. {ECO:0000269|PubMed:18654668}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is selectively expressed on CD34 hematopoietic stem and progenitor cells in adult and fetal bone marrow, fetal liver, cord blood and adult peripheral blood. Isoform 1 is not detected on other blood cells. Isoform 1 is also expressed in a number of non-lymphoid tissues including retina, pancreas, placenta, kidney, liver, lung, brain and heart. Found in saliva within small membrane particles. Isoform 2 is predominantly expressed in fetal liver, skeletal muscle, kidney, and heart as well as adult pancreas, kidney, liver, lung, and placenta. Isoform 2 is highly expressed in fetal liver, low in bone marrow, and barely detectable in peripheral blood. Isoform 2 is expressed on hematopoietic stem cells and in epidermal basal cells (at protein level). Expressed in adult retina by rod and cone photoreceptor cells (at protein level). {ECO:0000269|PubMed:12042327, ECO:0000269|PubMed:17874118}.; . . 0.31674 0.31496 -1.368693559 4.482189196 96.86296 2.12686 PROM2 7.89703407792325e-08 0.994662578021275 0.00533734300838434 prominin 2 . . TISSUE SPECIFICITY: Present in saliva within small membrane particles (at protein level). Expressed in kidney, prostate, trachea, esophagus, salivary gland, thyroid gland, mammary gland adrenal gland, placenta, stomach, spinal cord and liver. In submucosal tumor, expressed in spindle-shaped or stellate stromal cells. Expressed in prostate cancer cell lines. {ECO:0000269|PubMed:12446606, ECO:0000269|PubMed:12514187, ECO:0000269|PubMed:16673119, ECO:0000269|PubMed:17874118}.; unclassifiable (Anatomical System);lacrimal gland;colon;uterus;prostate;lung;frontal lobe;oesophagus;endometrium;larynx;thyroid;hypopharynx;testis;head and neck;kidney;brain;stomach; ciliary ganglion;skeletal muscle; 0.12478 0.09270 -0.369255208 28.25548478 1092.43407 6.32455 PROP1 0.299126611004975 0.681361078944099 0.019512310050926 PROP paired-like homeobox 1 FUNCTION: Possibly involved in the ontogenesis of pituitary gonadotropes, as well as somatotropes, lactotropes and caudomedial thyrotropes.; . TISSUE SPECIFICITY: Expressed specifically in embryonic pituitary.; . . 0.09956 . 0.283038099 71.26680821 14.54926 0.52401 PRORSD1P . . . prolyl-tRNA synthetase associated domain containing 1, pseudogene . . . lung;whole body;ovary;placenta;parathyroid; . . . . . . . PRORY . . . proline rich, Y-linked . . . . . . . . . . . PROS1 0.000209233911903675 0.995112544121315 0.00467822196678099 protein S (alpha) FUNCTION: Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis.; DISEASE: Thrombophilia due to protein S deficiency, autosomal dominant (THPH5) [MIM:612336]: A hemostatic disorder characterized by impaired regulation of blood coagulation and a tendency to recurrent venous thrombosis. Based on the plasma levels of total and free PROS1 as well as the serine protease-activated protein C cofactor activity, three types of THPH5 have been described: type I, characterized by reduced total and free PROS1 levels together with reduced anticoagulant activity; type III, in which only free PROS1 antigen and PROS1 activity levels are reduced; and the rare type II which is characterized by normal concentrations of both total and free PROS1 antigen, but low cofactor activity. {ECO:0000269|PubMed:10447256, ECO:0000269|PubMed:10613647, ECO:0000269|PubMed:10706858, ECO:0000269|PubMed:10790208, ECO:0000269|PubMed:11372770, ECO:0000269|PubMed:11776305, ECO:0000269|PubMed:11858485, ECO:0000269|PubMed:11927129, ECO:0000269|PubMed:12351389, ECO:0000269|PubMed:12632031, ECO:0000269|PubMed:15238143, ECO:0000269|PubMed:15712227, ECO:0000269|PubMed:7482398, ECO:0000269|PubMed:7545463, ECO:0000269|PubMed:7579449, ECO:0000269|PubMed:7803790, ECO:0000269|PubMed:8298131, ECO:0000269|PubMed:8639833, ECO:0000269|PubMed:8701404, ECO:0000269|PubMed:8765219, ECO:0000269|PubMed:8781426, ECO:0000269|PubMed:8943854, ECO:0000269|PubMed:8977443, ECO:0000269|PubMed:9031443, ECO:0000269|PubMed:9241758, ECO:0000269|Ref.15}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Thrombophilia due to protein S deficiency, autosomal recessive (THPH6) [MIM:614514]: A very rare and severe hematologic disorder resulting in thrombosis and secondary hemorrhage usually beginning in early infancy. Some affected individuals develop neonatal purpura fulminans, multifocal thrombosis, or intracranial hemorrhage. {ECO:0000269|PubMed:20484936}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;thyroid;bone;iris;testis;dura mater;brain;gall bladder;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;urinary;lens;pancreas;pia mater;lung;placenta;macula lutea;hippocampus;liver;duodenum;spleen;cervix;kidney;stomach; . 0.11674 0.42750 -0.220384297 37.6032083 170.86942 2.85072 PROS2P . . . protein S (beta) pseudogene . . . . . . . . . . . PROSC 0.297119448410396 0.698643189940077 0.00423736164952761 proline synthetase co-transcribed homolog (bacterial) . . TISSUE SPECIFICITY: Ubiquitous.; myocardium;ovary;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;dura mater;germinal center;brain;artery;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;adrenal cortex;blood;skeletal muscle;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;subthalamic nucleus;medulla oblongata;occipital lobe;superior cervical ganglion;globus pallidus;caudate nucleus;kidney;atrioventricular node;parietal lobe; 0.07369 0.19166 -0.159704656 41.90846898 70.64743 1.74916 PROSER1 0.736135591768488 0.263842666481055 2.17417504575854e-05 proline and serine rich 1 . . . ovary;salivary gland;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);heart;pharynx;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;placenta;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10421 0.09566 -0.170835809 40.65227648 338.0786 3.90357 PROSER2 0.00546315143684282 0.713979704667376 0.280557143895781 proline and serine rich 2 . . . . . 0.09537 . . . 802.73118 5.58207 PROSER2-AS1 . . . PROSER2 antisense RNA 1 . . . . . . . . . . . PROSER3 . . . proline and serine rich 3 . . . . . 0.16961 . . . . . PROX1 0.993426962817253 0.0065728253324507 2.11850296365884e-07 prospero homeobox 1 FUNCTION: Transcription factor involved in developmental processes such as cell fate determination, gene transcriptional regulation and progenitor cell regulation in a number of organs. Plays a critical role in embryonic development and functions as a key regulatory protein in neurogenesis and the development of the heart, eye lens, liver, pancreas and the lymphatic system. Involved in the regulation of the circadian rhythm. Represses: transcription of the retinoid-related orphan receptor RORG, transcriptional activator activity of RORA and RORG and the expression of RORA/G-target genes including core clock components: ARNTL/BMAL1, NPAS2 and CRY1 and metabolic genes: AVPR1A and ELOVL3. {ECO:0000269|PubMed:23723244, ECO:0000303|PubMed:22733308}.; . TISSUE SPECIFICITY: Most actively expressed in the developing lens. Detected also in embryonic brain, lung, liver and kidney. In adult, it is more abundant in heart and liver than in brain, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:8812486}.; unclassifiable (Anatomical System);breast;lung;cartilage;hypothalamus;liver;testis;germinal center;brain;retina; superior cervical ganglion;testis - interstitial;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.49987 0.14219 -0.670411825 15.61689078 16.90934 0.59575 PROX1-AS1 . . . PROX1 antisense RNA 1 . . . . . . . . . . . PROX2 7.88534780140081e-07 0.16191193732827 0.83808727413695 prospero homeobox 2 FUNCTION: Transcription regulator. Does not seem to be essential for embryonic development and postnatal survival (By similarity). {ECO:0000250}.; . . . . 0.14572 . -0.110153916 45.48832272 258.61029 3.45610 PROZ 3.84163746031333e-09 0.0996644065356725 0.90033558962269 protein Z, vitamin K-dependent plasma glycoprotein FUNCTION: Appears to assist hemostasis by binding thrombin and promoting its association with phospholipid vesicles. Inhibits activity of the coagulation protease factor Xa in the presence of SERPINA10, calcium and phospholipids.; . TISSUE SPECIFICITY: Plasma.; unclassifiable (Anatomical System);lung;bone;liver;testis;spleen;kidney; superior cervical ganglion;liver;kidney; 0.10867 0.25685 -0.244249595 36.17008728 175.78502 2.88511 PRPF3 0.999998843810724 1.15618927554709e-06 7.41247264467359e-16 pre-mRNA processing factor 3 FUNCTION: Participates in pre-mRNA splicing. Part of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. {ECO:0000269|PubMed:9328476, ECO:0000269|PubMed:9404889, ECO:0000303|PubMed:20595234}.; DISEASE: Retinitis pigmentosa 18 (RP18) [MIM:601414]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:11773002, ECO:0000269|PubMed:12714658}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in retina, liver, kidney and blood. Detected at lower levels in heart and brain. {ECO:0000269|PubMed:11773002}.; unclassifiable (Anatomical System);uterus;heart;cervix;brain;stomach;retina; testis;white blood cells; 0.83102 0.16844 -0.560178693 19.30879925 16.61976 0.58582 PRPF4 0.999643089192096 0.000356910633985495 1.73918868325752e-10 pre-mRNA processing factor 4 FUNCTION: Participates in pre-mRNA splicing. Part of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. {ECO:0000269|PubMed:25383878}.; DISEASE: Retinitis pigmentosa 70 (RP70) [MIM:615922]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:24419317, ECO:0000269|PubMed:25383878}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.33136 0.12719 -0.381986487 27.68931352 64.16192 1.64220 PRPF4B 0.999999729158495 2.70841504546864e-07 4.37237603636487e-18 pre-mRNA processing factor 4B FUNCTION: Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;medulla oblongata;superior cervical ganglion;occipital lobe;hypothalamus;thyroid;prefrontal cortex;testis;white blood cells;trigeminal ganglion;parietal lobe;pituitary; 0.90822 0.13321 -0.731092527 14.13658882 68.41343 1.71211 PRPF6 0.280831794647215 0.719167866953401 3.3839938384699e-07 pre-mRNA processing factor 6 FUNCTION: Involved in pre-mRNA splicing as component of the U4/U6- U5 tri-snRNP complex, one of the building blocks of the spliceosome. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation. {ECO:0000269|PubMed:12039962}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12039962}.; lymphoreticular;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;breast;bile duct;pancreas;lung;adrenal gland;epididymis;placenta;visual apparatus;duodenum;liver;cervix;spleen;kidney;mammary gland;stomach; amygdala;placenta;liver;pons;cingulate cortex;cerebellum; 0.09508 0.35707 -1.375949569 4.393724935 23.08084 0.77011 PRPF8 0.999999999219228 7.80771924814832e-10 3.94353645718941e-29 pre-mRNA processing factor 8 FUNCTION: Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for the assembly of the U4/U6-U5 tri-snRNP complex. Functions as scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site. {ECO:0000269|PubMed:20595234, ECO:0000303|PubMed:15840809}.; DISEASE: Retinitis pigmentosa 13 (RP13) [MIM:600059]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:11468273, ECO:0000269|PubMed:11910553, ECO:0000269|PubMed:12714658, ECO:0000269|Ref.33}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10411133}.; myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;thymus; testis - interstitial;testis - seminiferous tubule;testis;cerebellum; 0.82448 0.21033 -3.03027298 0.501297476 22.76309 0.76084 PRPF18 0.099443258781573 0.893050443747055 0.0075062974713714 pre-mRNA processing factor 18 FUNCTION: Participates in the second step of pre-mRNA splicing. {ECO:0000269|PubMed:9000057}.; . . unclassifiable (Anatomical System);smooth muscle;ovary;colon;parathyroid;blood;fovea centralis;choroid;lens;skin;retina;optic nerve;lung;endometrium;nasopharynx;bone;macula lutea;visual apparatus;hypopharynx;liver;testis;head and neck;spleen;kidney;brain; atrioventricular node;trigeminal ganglion; 0.10502 0.11262 0.082802743 60.09082331 57.85386 1.53717 PRPF19 0.998566695864226 0.00143327869030732 2.54454664631393e-08 pre-mRNA processing factor 19 FUNCTION: Ubiquitin-protein ligase which is a core component of several complexes mainly involved pre-mRNA splicing and DNA repair. Core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome and participates in its assembly, its remodeling and is required for its activity. During assembly of the spliceosome, mediates 'Lys-63'-linked polyubiquitination of the U4 spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its recognition by the U5 component PRPF8 and stabilizes the U4/U5/U6 tri-snRNP spliceosomal complex (PubMed:20595234). Recruited to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA, it may also couple the transcriptional and spliceosomal machineries (PubMed:21536736). The XAB2 complex, which contains PRPF19, is also involved in pre- mRNA splicing, transcription and transcription-coupled repair (PubMed:17981804). Beside its role in pre-mRNA splicing PRPF19, as part of the PRP19-CDC5L complex, plays a role in the DNA damage response/DDR. It is recruited to the sites of DNA damage by the RPA complex where PRPF19 directly ubiquitinates RPA1 and RPA2. 'Lys-63'-linked polyubiquitination of the RPA complex allows the recruitment of the ATR-ATRIP complex and the activation of ATR, a master regulator of the DNA damage response (PubMed:24332808). May also play a role in DNA double-strand break (DSB) repair by recruiting the repair factor SETMAR to altered DNA (PubMed:18263876). As part of the PSO4 complex may also be involved in the DNA interstrand cross-links/ICLs repair process (PubMed:16223718). In addition, may also mediate 'Lys-48'-linked polyubiquitination of substrates and play a role in proteasomal degradation (PubMed:11435423). May play a role in the biogenesis of lipid droplets (By similarity). May play a role in neural differentiation possibly through its function as part of the spliceosome (By similarity). {ECO:0000250|UniProtKB:Q99KP6, ECO:0000250|UniProtKB:Q9JMJ4, ECO:0000269|PubMed:11082287, ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:12960389, ECO:0000269|PubMed:15660529, ECO:0000269|PubMed:16223718, ECO:0000269|PubMed:16332694, ECO:0000269|PubMed:16388800, ECO:0000269|PubMed:17349974, ECO:0000269|PubMed:18263876, ECO:0000269|PubMed:21536736, ECO:0000269|PubMed:24332808, ECO:0000303|PubMed:17981804, ECO:0000303|PubMed:20595234}.; . TISSUE SPECIFICITY: Ubiquitous. Weakly expressed in senescent cells of different tissue origins. Highly expressed in tumor cell lines. {ECO:0000269|PubMed:10404385, ECO:0000269|PubMed:11082287, ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:12960389, ECO:0000269|PubMed:16388800}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; amygdala;whole brain;thalamus;medulla oblongata;cerebellum peduncles;temporal lobe;pons;subthalamic nucleus;prefrontal cortex;parietal lobe;cingulate cortex;thymus;cerebellum; 0.60527 0.17956 -0.560178693 19.30879925 12.11009 0.43916 PRPF19P1 . . . PRPF19 pseudogene 1 . . . . . . . . . . . PRPF31 0.968045446613026 0.0319442089768862 1.03444100873709e-05 pre-mRNA processing factor 31 FUNCTION: Involved in pre-mRNA splicing. Required for the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. {ECO:0000269|PubMed:11867543}.; DISEASE: Retinitis pigmentosa 11 (RP11) [MIM:600138]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:11545739, ECO:0000269|PubMed:12923864, ECO:0000269|PubMed:8808602}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11545739}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;heart;trigeminal ganglion;skeletal muscle; 0.22180 0.31462 -1.089312628 7.047652748 11.58931 0.41906 PRPF38A 0.996467618668032 0.00353233485860139 4.64733671624405e-08 pre-mRNA processing factor 38A FUNCTION: May be required for pre-mRNA splicing. {ECO:0000305}.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;fovea centralis;choroid;lens;skin;retina;bone marrow;breast;uterus;pancreas;optic nerve;lung;nasopharynx;placenta;macula lutea;duodenum;liver;testis;cervix;germinal center;brain;mammary gland; superior cervical ganglion;testis;trigeminal ganglion;skeletal muscle; 0.04390 0.10543 -0.207437529 38.2814343 7.72909 0.28518 PRPF38AP1 . . . PRP38 domain containing A pseudogene 1 . . . . . . . . . . . PRPF38AP2 . . . PRP38 domain containing A pseudogene 2 . . . . . . . . . . . PRPF38B 0.990908108110014 0.00909188800759528 3.8823906106752e-09 pre-mRNA processing factor 38B FUNCTION: May be required for pre-mRNA splicing. {ECO:0000305}.; . . . . 0.61332 0.10040 0.084621747 60.31493277 103.45472 2.19700 PRPF39 0.995121732276915 0.00487816550278528 1.02220300136461e-07 pre-mRNA processing factor 39 FUNCTION: Involved in pre-mRNA splicing. {ECO:0000250}.; . . ovary;colon;skin;retina;uterus;prostate;whole body;cochlea;endometrium;thyroid;bone;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;islets of Langerhans;skeletal muscle;bile duct;breast;pancreas;pia mater;lung;placenta;hippocampus;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;caudate nucleus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10868 0.08609 0.150760231 64.51403633 82.09744 1.92162 PRPF40A 0.966325783136999 0.0336742128629604 4.00004091531282e-09 pre-mRNA processing factor 40 homolog A FUNCTION: Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing. {ECO:0000250, ECO:0000269|PubMed:21834987}.; . TISSUE SPECIFICITY: Expressed in the brain cortex (at protein level). Widely expressed. {ECO:0000269|PubMed:16391387, ECO:0000269|PubMed:9700202}.; lymphoreticular;ovary;salivary gland;intestine;colon;vein;skin;bone marrow;prostate;whole body;frontal lobe;endometrium;oesophagus;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;small intestine;islets of Langerhans;pharynx;blood;bile duct;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;fetal liver;testis - interstitial;testis - seminiferous tubule;testis;white blood cells;ciliary ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.46081 0.17847 -1.111360919 6.717386176 22.59417 0.75608 PRPF40B 0.98865339397477 0.0113466057516663 2.73563430659706e-10 pre-mRNA processing factor 40 homolog B FUNCTION: May be involved in pre-mRNA splicing. {ECO:0000269|PubMed:9700202}.; . TISSUE SPECIFICITY: Expressed in the striatum and cortex of the brain (at protein level). Highly expressed in testis, fetal kidney and fetal brain. Moderately expressed in pancreas, skeletal muscle, placenta, brain and heart. Weakly expressed in colon, ileum, ovary, prostate, spleen, kidney and fetal lung. {ECO:0000269|PubMed:10958656, ECO:0000269|PubMed:9700202}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;nervous;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; . 0.46946 0.08281 -1.460519861 3.809860816 70.83292 1.75248 PRPH 5.04583995510316e-10 0.111255536391632 0.888744463103784 peripherin FUNCTION: Class-III neuronal intermediate filament protein.; . . unclassifiable (Anatomical System);lung;whole body;islets of Langerhans;sympathetic chain;visual apparatus;testis;colon;spinal ganglion;brain;stomach;retina; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;trigeminal ganglion; 0.18752 0.41233 0.018483465 55.44939844 322.45963 3.81287 PRPH2 0.388059586223376 0.602008964872671 0.00993144890395311 peripherin 2 (retinal degeneration, slow) FUNCTION: May function as an adhesion molecule involved in stabilization and compaction of outer segment disks or in the maintenance of the curvature of the rim. It is essential for disk morphogenesis.; DISEASE: Retinitis punctata albescens (RPA) [MIM:136880]: Rare form of stationary night blindness characterized by a delay in the regeneration of cone and rod photopigments. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Macular dystrophy, vitelliform, 3 (VMD3) [MIM:608161]: A form of vitelliform macular dystrophy, a retinal disease characterized by yellow, lipofuscin-containing deposits, usually localized at the center of the macula. Patients usually become symptomatic in the fourth or fifth decade of life with a protracted disease of decreased visual acuity. {ECO:0000269|PubMed:17653047, ECO:0000269|PubMed:9338584}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Macular dystrophy, patterned, 1 (MDPT1) [MIM:169150]: A form of retinal patterned dystrophy, a heterogeneous group of macular disorders that includes reticular (fishnet-like) dystrophy, macroreticular (spider-shaped) dystrophy and butterfly- shaped pigment dystrophy. {ECO:0000269|PubMed:16024869, ECO:0000269|PubMed:8485574, ECO:0000269|PubMed:9443872}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Choroidal dystrophy, central areolar 2 (CACD2) [MIM:613105]: A disease of the macula leading to a well-demarcated circumscribed area of atrophy of the pigment epithelium and choriocapillaris. {ECO:0000269|PubMed:16832026}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in PRPH2 are found in different retinal diseases including cone-rod dystrophy, retinitis pigmentosa, macular degeneration. The mutations underlying autosomal dominant retinitis pigmentosa and severe macular degeneration are largely missense or small in-frame deletions in a large intradiscal loop between the third and fourth transmembrane domains. In contrast, those associated with the milder pattern phenotypes or with digenic RP are scattered more evenly through the gene and are often nonsense mutations. This observation correlates with the hypothesis that the large loop is an important site of interaction between PRPH2 molecules and other protein components in the disk.; TISSUE SPECIFICITY: Retina (photoreceptor). In rim region of ROS (rod outer segment) disks.; unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;prostate;optic nerve;whole body;lung;bone;macula lutea;visual apparatus;kidney;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.36677 0.21357 0.463046108 78.58575136 95.39465 2.10770 PRPS1 0.871770724918057 0.126530706849299 0.00169856823264422 phosphoribosyl pyrophosphate synthetase 1 FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.; DISEASE: Note=Phosphoribosyl pyrophosphate synthetase I deficiency is a rare condition caused by mutations in PRPS1 that lead to variable disease phenotypes including optic atrophy, retinitis pigmentosa, ataxia, peripheral neuropathy and hearing loss. {ECO:0000269|PubMed:25491489}.; DISEASE: Phosphoribosylpyrophosphate synthetase superactivity (PRPS1 superactivity) [MIM:300661]: Familial disorder characterized by excessive purine production, gout and uric acid urolithiasis. {ECO:0000269|PubMed:7593598, ECO:0000269|Ref.12}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease, X-linked recessive, 5 (CMTX5) [MIM:311070]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot- Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies characterized by severely reduced motor nerve conduction velocities (NCVs) (less than 38m/s) and segmental demyelination and remyelination, and primary peripheral axonal neuropathies characterized by normal or mildly reduced NCVs and chronic axonal degeneration and regeneration on nerve biopsy. {ECO:0000269|PubMed:17701900}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: ARTS syndrome (ARTS) [MIM:301835]: A disorder characterized by mental retardation, early-onset hypotonia, ataxia, delayed motor development, hearing impairment, and optic atrophy. Susceptibility to infections, especially of the upper respiratory tract, can result in early death. {ECO:0000269|PubMed:17701896}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, X-linked, 1 (DFNX1) [MIM:304500]: A form of deafness characterized by progressive, severe-to-profound sensorineural hearing loss in males. Females manifest mild to moderate hearing loss. {ECO:0000269|PubMed:20021999}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . 0.29199 0.035072054 56.2514744 . . PRPS1L1 . . . phosphoribosyl pyrophosphate synthetase 1-like 1 FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.; . TISSUE SPECIFICITY: Testis.; . . . 0.30319 0.396906589 76.30927105 1511.43454 7.22068 PRPS1P1 . . . phosphoribosyl pyrophosphate synthetase 1 pseudogene 1 . . . . . . . . . . . PRPS1P2 . . . phosphoribosyl pyrophosphate synthetase 1 pseudogene 2 . . . . . . . . . . . PRPS2 0.922707345456536 0.0768282570025002 0.000464397540963397 phosphoribosyl pyrophosphate synthetase 2 FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.; . . . . 0.14178 0.22474 -0.273576253 33.97027601 3.02051 0.10951 PRPSAP1 1.9694174251285e-10 0.0343082686917712 0.965691731111287 phosphoribosyl pyrophosphate synthetase-associated protein 1 FUNCTION: Seems to play a negative regulatory role in 5- phosphoribose 1-diphosphate synthesis.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;oesophagus;larynx;bone;testis;artery;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;medulla oblongata;superior cervical ganglion;testis;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.06530 0.12366 -0.449946534 24.00330267 22.31598 0.74921 PRPSAP2 0.0720452015966568 0.915295015941816 0.0126597824615276 phosphoribosyl pyrophosphate synthetase-associated protein 2 FUNCTION: Seems to play a negative regulatory role in 5- phosphoribose 1-diphosphate synthesis.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;aorta;stomach;thymus; amygdala;superior cervical ganglion;testis;parietal lobe; 0.07357 0.08744 -0.227663163 37.11370606 9.95953 0.36462 PRR3 0.114320038533931 0.858125135218518 0.0275548262475509 proline rich 3 . . . . . 0.24059 . 0.058937498 58.26256192 299.93696 3.69274 PRR4 1.03390158107127e-05 0.345948803051807 0.654040857932382 proline rich 4 (lacrimal) . . TISSUE SPECIFICITY: Abundantly expressed in lacrimal gland where it is found in the acinar cells but not in the intralobular ducts. Also found in the submandibular gland, the parotid and sublingual glands. {ECO:0000269|PubMed:7544782}.; unclassifiable (Anatomical System);smooth muscle;cartilage;lacrimal gland;adrenal cortex;parathyroid;prostate;lung;adrenal gland;larynx;nasopharynx;thyroid;visual apparatus;liver;testis;head and neck;cervix;kidney;pineal gland;stomach; superior cervical ganglion;trachea;salivary gland;thyroid;globus pallidus;ciliary ganglion;thymus; 0.03800 0.03335 0.569646743 81.88841708 14.67536 0.52927 PRR5 0.972989444687975 0.0269769313435773 3.36239684475337e-05 proline rich 5 FUNCTION: Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient- insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. PRR5 plays an important role in regulation of PDGFRB expression and in modulation of platelet-derived growth factor signaling. May act as a tumor suppressor in breast cancer. {ECO:0000269|PubMed:15718101, ECO:0000269|PubMed:17599906}.; . TISSUE SPECIFICITY: Most abundant in kidney and liver. Also highly expressed in brain, spleen, testis and placenta. Overexpressed in several colorectal tumors. {ECO:0000269|PubMed:15718101, ECO:0000269|PubMed:17599906}.; ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;cerebral cortex;bone;pituitary gland;iris;testis;brain;unclassifiable (Anatomical System);lymph node;heart;urinary;lens;lung;placenta;macula lutea;hippocampus;liver;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion; . 0.13931 0.444637294 77.91342298 483.20854 4.52538 PRR5-ARHGAP8 . . . PRR5-ARHGAP8 readthrough . . . unclassifiable (Anatomical System);ovary;colon;parathyroid;blood;skin;breast;prostate;lung;endometrium;larynx;placenta;hippocampus;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion; . . 2.282000943 98.27789573 986.91926 6.05583 PRR5L 0.0787688609861764 0.910242770993758 0.010988368020066 proline rich 5 like FUNCTION: Associates with the mTORC2 complex that regulates cellular processes including survival and organization of the cytoskeleton. Regulates the activity of the mTORC2 complex in a substrate-specific manner preventing for instance the specific phosphorylation of PKCs and thereby controlling cell migration. {ECO:0000269|PubMed:17461779, ECO:0000269|PubMed:22609986}.; . . unclassifiable (Anatomical System);lung;endometrium;hypothalamus;testis;colon;cervix;brain;stomach; . . . 0.176444282 66.07100731 625.83265 5.04502 PRR7 0.72498912624669 0.261980663405521 0.0130302103477883 proline rich 7 (synaptic) . . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;salivary gland;colon;parathyroid;skin;retina;uterus;pancreas;lung;frontal lobe;endometrium;bone;thyroid;placenta;duodenum;testis;brain;mammary gland;stomach; amygdala;medulla oblongata;subthalamic nucleus;temporal lobe;atrioventricular node; 0.62667 0.11479 . . . . PRR7-AS1 . . . PRR7 antisense RNA 1 . . . . . . . . . . . PRR9 . . . proline rich 9 . . . . . 0.16362 . . . 19.24749 0.66351 PRR11 3.71709922242414e-06 0.811940555735221 0.188055727165557 proline rich 11 FUNCTION: Plays a critical role in cell cycle progression. {ECO:0000269|PubMed:23246489}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:23246489}.; unclassifiable (Anatomical System);lymph node;lung;placenta;visual apparatus;liver;testis;cervix;spleen;germinal center;mammary gland;skin;skeletal muscle; . 0.56487 . 0.108486928 61.90728946 81.25525 1.90885 PRR12 0.999969576883676 3.04231141892776e-05 2.13444011114465e-12 proline rich 12 . . . unclassifiable (Anatomical System);ovary;colon;fovea centralis;choroid;lens;skin;retina;pancreas;prostate;optic nerve;lung;placenta;thyroid;macula lutea;visual apparatus;germinal center;bladder;brain;cerebellum; superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion; 0.39076 0.11358 . . 335.02137 3.88941 PRR13 0.634332002252778 0.336602033699086 0.0290659640481365 proline rich 13 FUNCTION: Negatively regulates TSP1 expression at the level of transcription. This down-regulation was shown to reduce taxane- induced apoptosis. {ECO:0000269|PubMed:16847352}.; . . . . 0.04455 0.09483 0.079165051 59.43029016 28.34564 0.90748 PRR13P1 . . . proline rich 13 pseudogene 1 . . . . . . . . . . . PRR13P2 . . . proline rich 13 pseudogene 2 . . . . . . . . . . . PRR13P3 . . . proline rich 13 pseudogene 3 . . . . . . . . . . . PRR13P4 . . . proline rich 13 pseudogene 4 . . . . . . . . . . . PRR13P5 . . . proline rich 13 pseudogene 5 . . . . . . . . . . . PRR13P6 . . . proline rich 13 pseudogene 6 . . . . . . . . . . . PRR13P7 . . . proline rich 13 pseudogene 7 . . . . . . . . . . . PRR14 0.258591291316777 0.741359191738238 4.95169449845559e-05 proline rich 14 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; subthalamic nucleus;cerebellum peduncles;thyroid;placenta;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle;cerebellum; 0.29172 0.08143 -0.242430445 36.22906346 3607.63844 11.62925 PRR14L 0.984999166925525 0.0149992329986783 1.60007579698315e-06 proline rich 14 like . . . unclassifiable (Anatomical System);heart;islets of Langerhans;colon;blood;skeletal muscle;skin;bone marrow;breast;uterus;larynx;placenta;liver;testis;head and neck;spleen;cervix;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06431 . 3.804330582 99.62255249 2648.35146 9.65604 PRR15 0.446963256775024 0.453641018480694 0.0993957247442825 proline rich 15 FUNCTION: May have a role in proliferation and/or differentiation. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;blood;skin;retina;breast;uterus;pancreas;prostate;lung;endometrium;thyroid;placenta;spleen;germinal center;kidney;brain;stomach; . 0.58745 0.10844 . . 2657.67063 9.69312 PRR15L 0.481246950810061 0.437097791181413 0.0816552580085263 proline rich 15 like . . . unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;skeletal muscle;uterus;pancreas;prostate;whole body;lung;endometrium;thyroid;liver;testis;spleen;cervix;kidney;brain;stomach; superior cervical ganglion;atrioventricular node; 0.08990 0.10869 0.080983847 59.76055674 24.52195 0.80551 PRR16 0.52619928151234 0.457553662362122 0.016247056125538 proline rich 16 FUNCTION: Regulator of cell size that promotes cell size increase independently of mTOR and Hippo signaling pathways. Acts by stimulating the translation of specific mRNAs, including those encoding proteins affecting mitochondrial functions. Increases mitochondrial mass and respiration. {ECO:0000269|PubMed:24656129}.; . . . . 0.18106 . 0.549415813 81.38122199 963.05189 6.00685 PRR18 0.488137895604996 0.433466289011268 0.0783958153837362 proline rich 18 . . . lung;hippocampus;testis;brain; prefrontal cortex;trigeminal ganglion; 0.15862 . . . 11.11575 0.40222 PRR19 0.196398788206015 0.757406853574422 0.0461943582195635 proline rich 19 . . . umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;uterus;prostate;optic nerve;frontal lobe;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pharynx;blood;bile duct;breast;pancreas;lung;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;testis;ciliary ganglion;pons;atrioventricular node;skeletal muscle;skin; 0.13738 . -0.003562597 53.72729417 62.41705 1.61409 PRR20A . . . proline rich 20A . . . . . . . . . . . PRR20B . . . proline rich 20B . . . . . . . . . . . PRR20C . . . proline rich 20C . . . . . . . . . . . PRR20D . . . proline rich 20D . . . . . . . . . . . PRR20E . . . proline rich 20E . . . . . . . . . . . PRR20FP . . . proline rich 20F, pseudogene . . . . . . . . . . . PRR21 0.00365275248209853 0.398658652040877 0.597688595477024 proline rich 21 . . . . . . . . . 2739.14281 9.86619 PRR22 0.0206405591402269 0.748603616581055 0.230755824278718 proline rich 22 . . . . . . . -0.047654689 50.22410946 2628.60865 9.61723 PRR23A 0.0180799350653936 0.724346192219317 0.25757387271529 proline rich 23A . . . . . . . 0.523736627 80.45529606 20.515 0.69780 PRR23B 0.0025340200634616 0.549908221008258 0.44755775892828 proline rich 23B . . . . . . . 0.791937896 87.33781552 19.51791 0.66947 PRR23C 0.000636017536157745 0.493366059442436 0.505997923021406 proline rich 23C . . . . . . . 0.657836546 84.27105449 19.23022 0.66274 PRR23D1 . . . proline rich 23 domain containing 1 . . . . . . . . . 0.29746 0.00622 PRR23D2 . . . proline rich 23 domain containing 2 . . . . . . . . . . . PRR25 3.12896569287399e-06 0.186993085867386 0.813003785166921 proline rich 25 . . . optic nerve;macula lutea;fovea centralis;choroid;lens;retina; . . . . . 3429.21292 11.24303 PRR26 . . . proline rich 26 . . . . . 0.08153 . . . 66.6905 1.68519 PRR27 . . . proline rich 27 . . . . . 0.01155 0.03940 0.793752871 87.40268931 . . PRR29 . . . proline rich 29 . . . . . . . 0.257356108 69.83368719 . . PRR29-AS1 . . . PRR29 antisense RNA 1 . . . . . . . . . . . PRR30 . . . proline rich 30 . . . . . 0.14896 . 0.598963042 82.7789573 . . PRR31 . . . proline rich 31 . . . . . 0.10900 . . . . . PRR32 . . . proline rich 32 . . . . . . . 1.012423333 90.829205 . . PRR33 . . . proline rich 33 . . . . . . . . . . . PRR34 . . . proline rich 34 . . . . . 0.07675 . . . . . PRR34-AS1 . . . PRR34 antisense RNA 1 . . . . . . . . . . . PRR35 . . . proline rich 35 . . . . . . . . . . . PRR36 . . . proline rich 36 . . . . . . . . . . . PRRC1 2.13078587199281e-05 0.720328173841593 0.279650518299687 proline rich coiled-coil 1 . . TISSUE SPECIFICITY: Isoform 4 is specifically expressed in liver. Ubiquitously expressed with higher expression in kidney, liver and placenta. {ECO:0000269|PubMed:15541471}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;oesophagus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; superior cervical ganglion;placenta;liver;pons;trigeminal ganglion;skeletal muscle; 0.11923 0.08564 -0.911109353 9.961075725 104.99985 2.21582 PRRC2A 0.999999999990663 9.337194749059e-12 9.89006493913549e-32 proline rich coiled-coil 2A FUNCTION: May play a role in the regulation of pre-mRNA splicing. {ECO:0000269|PubMed:14667819}.; . TISSUE SPECIFICITY: Limited to cell-lines of leukemic origin.; . . 0.55673 0.09596 2.15710641 98.01840057 9600.77696 21.21063 PRRC2B 0.99999910432668 8.95673320439201e-07 1.11843420595551e-21 proline rich coiled-coil 2B . . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;colon;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;cerebellum cortex;islets of Langerhans;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;thymus;cerebellum; dorsal root ganglion;whole brain;amygdala;occipital lobe;thalamus;superior cervical ganglion;cerebellum peduncles;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.14736 0.09076 -0.476189544 22.82967681 1856.75011 7.94257 PRRC2C 0.999999999976013 2.3987025343037e-11 9.84700883284565e-31 proline rich coiled-coil 2C . . TISSUE SPECIFICITY: Overexpressed in bladder cancer. {ECO:0000269|PubMed:12443540}.; myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;oral cavity;muscle;bile duct;pancreas;lung;nasopharynx;placenta;amnion;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;medulla oblongata;testis - interstitial;olfactory bulb;temporal lobe;adrenal cortex;white blood cells;atrioventricular node;pons;subthalamic nucleus;testis - seminiferous tubule;placenta;prefrontal cortex;globus pallidus;testis;trigeminal ganglion;cingulate cortex;parietal lobe; 0.75906 0.09702 -0.681886476 15.36919085 1981.07714 8.20033 PRRC2CP1 . . . proline rich coiled-coil 2C pseudogene 1 . . . . . . . . . . . PRRG1 0.335254587436665 0.603762594190878 0.060982818372458 proline rich Gla (G-carboxyglutamic acid) 1 . . TISSUE SPECIFICITY: Highly expressed in the spinal cord.; . . 0.23610 0.12113 0.080983847 59.76055674 17.72103 0.61924 PRRG2 5.96505604158473e-05 0.464608512898346 0.535331836541239 proline rich Gla (G-carboxyglutamic acid) 2 . . TISSUE SPECIFICITY: Highly expressed in the thyroid.; unclassifiable (Anatomical System);lymph node;heart;ovary;colon;parathyroid;skin;uterus;prostate;lung;thyroid;placenta;liver;testis;spleen;kidney;mammary gland;stomach; trigeminal ganglion;skeletal muscle; 0.12082 . 0.659651797 84.35362114 1074.92802 6.28378 PRRG3 2.0741935360123e-05 0.281303027208376 0.718676230856264 proline rich Gla (G-carboxyglutamic acid) 3 (transmembrane) . . TISSUE SPECIFICITY: Expressed in brain, lung, kidney and heart. {ECO:0000269|PubMed:11171957}.; . . 0.27731 0.10508 0.617373774 83.25076669 65.98373 1.67342 PRRG4 0.18140174334153 0.765470219667309 0.0531280369911616 proline rich Gla (G-carboxyglutamic acid) 4 (transmembrane) . . TISSUE SPECIFICITY: Expressed in lung, liver, kidney, pancreas and placenta. {ECO:0000269|PubMed:11171957}.; unclassifiable (Anatomical System);uterus;lung;placenta;testis;colon;skin; superior cervical ganglion; 0.05189 0.07841 1.082196027 91.79641425 738.98528 5.39584 PRRT1 0.407945729723328 0.554638123364392 0.0374161469122806 proline rich transmembrane protein 1 . . . unclassifiable (Anatomical System);heart;ovary;cartilage;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;frontal lobe;placenta;macula lutea;hippocampus;cervix;brain;stomach;cerebellum; . 0.00984 0.03221 . . 10.54497 0.38253 PRRT2 0.301735693046838 0.679146035182821 0.0191182717703409 proline rich transmembrane protein 2 . DISEASE: Episodic kinesigenic dyskinesia 1 (EKD1) [MIM:128200]: An autosomal dominant neurologic condition characterized by recurrent and brief attacks of abnormal involuntary movements, triggered by sudden voluntary movement. These attacks usually have onset during childhood or early adulthood and can involve dystonic postures, chorea, or athetosis. {ECO:0000269|PubMed:22101681, ECO:0000269|PubMed:22120146, ECO:0000269|PubMed:22131361, ECO:0000269|PubMed:22209761}. Note=The disease is caused by mutations affecting the gene represented in this entry. Disease- causing mutations that produce truncation of the C-terminus of the protein alter subcellular location, from plasma membrane to cytosplasm (PubMed:22101681). {ECO:0000269|PubMed:22101681}.; DISEASE: Convulsions, familial infantile, with paroxysmal choreoathetosis (ICCA) [MIM:602066]: A syndrome characterized by clinical features of benign familial infantile seizures and episodic kinesigenic dyskinesia. Benign familial infantile seizures is a disorder characterized by afebrile seizures occurring during the first year of life, without neurologic sequelae. Paroxysmal choreoathetosis is a disorder of involuntary movements characterized by attacks that occur spontaneously or are induced by a variety of stimuli. {ECO:0000269|PubMed:22243967}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Seizures, benign familial infantile 2 (BFIS2) [MIM:605751]: An autosomal dominant disorder in which afebrile seizures occur in clusters during the first year of life, without neurologic sequelae. {ECO:0000269|PubMed:22243967, ECO:0000269|PubMed:22399141, ECO:0000269|PubMed:22623405}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;parathyroid;choroid;fovea centralis;skin;retina;prostate;optic nerve;frontal lobe;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;hypothalamus;lens;skeletal muscle;lung;pia mater;placenta;hippocampus;macula lutea;duodenum;spleen;stomach;cerebellum; dorsal root ganglion;occipital lobe;subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;caudate nucleus;atrioventricular node;pons;cingulate cortex;cerebellum; 0.30697 0.08082 0.549415813 81.38122199 216.41438 3.17873 PRRT3 0.658018522445195 0.341744428981392 0.000237048573413057 proline rich transmembrane protein 3 . . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;hypothalamus;skin;bone marrow;uterus;lung;liver;pituitary gland;spleen;germinal center;kidney;brain; . 0.10702 0.08913 . . 3828.2537 12.17240 PRRT3-AS1 . . . PRRT3 antisense RNA 1 . . . . . . . . . . . PRRT4 . . . proline rich transmembrane protein 4 . . . . . . . . . 3421.37755 11.22532 PRRX1 0.752904237310255 0.244975033594116 0.00212072909562811 paired related homeobox 1 FUNCTION: Acts as a transcriptional regulator of muscle creatine kinase (MCK) and so has a role in the establishment of diverse mesodermal muscle types. The protein binds to an A/T-rich element in the muscle creatine enhancer (By similarity). {ECO:0000250}.; DISEASE: Agnathia-otocephaly complex (AGOTC) [MIM:202650]: A rare condition characterized by mandibular hypoplasia or agnathia, ventromedial auricular malposition (melotia) and/or auricular fusion (synotia), and microstomia with oroglossal hypoplasia or aglossia. Holoprosencephaly is the most commonly identified association, but skeletal, genitourinary, and cardiovascular anomalies, and situs inversus have been reported. The disorder is almost always lethal. {ECO:0000269|PubMed:21294718}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;heart;ovary;tongue;sympathetic chain;colon;skin;retina;uterus;prostate;whole body;lung;larynx;nasopharynx;placenta;visual apparatus;testis;head and neck;brain;stomach; dorsal root ganglion;superior cervical ganglion;adipose tissue;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; 0.85592 0.20297 0.283038099 71.26680821 144.53857 2.61900 PRRX2 0.305924077055442 0.619908185697086 0.0741677372474728 paired related homeobox 2 FUNCTION: May play a role in the scarless healing of cutaneous wounds during the first two trimesters of development. {ECO:0000269|PubMed:9665387}.; . TISSUE SPECIFICITY: In fetal skin, highest expression found in cells of mesodermal origin within the dermal papilla of the developing hair shaft. Not detected in epidermis or dermis. In adult skin, weakly expressed within the basal layers of the epidermis. Not expressed in dermis. {ECO:0000269|PubMed:9665387}.; . . 0.41929 0.15588 . . 31.30599 0.98729 PRRX2-AS1 . . . PRRX2 antisense RNA 1 . . . . . . . . . . . PRS . . . Prieto X-linked mental retardation syndrome . . . . . . . . . . . PRSM2 . . . protease, metallo, 2 . . . . . . . . . . . PRSS1 0.00122029540045484 0.848354592654671 0.150425111944874 protease, serine 1 FUNCTION: Has activity against the synthetic substrates Boc-Phe- Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val- Pro-Arg-Mec. The single-chain form is more active than the two- chain form against all of these substrates. {ECO:0000269|PubMed:7945238}.; DISEASE: Pancreatitis, hereditary (PCTT) [MIM:167800]: A disease characterized by pancreas inflammation, permanent destruction of the pancreatic parenchyma, maldigestion, and severe abdominal pain attacks. {ECO:0000269|PubMed:10204851, ECO:0000269|PubMed:10381903, ECO:0000269|PubMed:10930381, ECO:0000269|PubMed:11073545, ECO:0000269|PubMed:11788572, ECO:0000269|PubMed:11866271, ECO:0000269|PubMed:14695529, ECO:0000269|PubMed:15776435, ECO:0000269|PubMed:8841182, ECO:0000269|PubMed:9322498, ECO:0000269|PubMed:9633818}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . pancreas;islets of Langerhans;liver;colon;spleen; superior cervical ganglion;pancreas;beta cell islets;ciliary ganglion;bone marrow; 0.47806 0.78094 -0.117432389 44.89266336 35.65715 1.07286 PRSS2 . . . protease, serine 2 FUNCTION: In the ileum, may be involved in defensin processing, including DEFA5. {ECO:0000269|PubMed:12021776}.; . TISSUE SPECIFICITY: Expressed in Paneth cells, at the base of small intestinal crypts. {ECO:0000269|PubMed:12021776}.; . . 0.23451 0.73904 . . . . PRSS3 4.79797626819515e-10 0.0157398256921942 0.984260173828008 protease, serine 3 FUNCTION: Digestive protease specialized for the degradation of trypsin inhibitors. In the ileum, may be involved in defensin processing, including DEFA5. {ECO:0000269|PubMed:12021776, ECO:0000269|PubMed:14507909}.; . TISSUE SPECIFICITY: Expressed in pancreas and brain. Also expressed in Paneth cells, at the base of small intestinal crypts. {ECO:0000269|PubMed:12021776}.; unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;salivary gland;intestine;colon;pharynx;blood;uterus;prostate;pancreas;lung;bone;visual apparatus;liver;testis;spleen;kidney;brain;bladder;stomach; whole brain;pancreas;subthalamic nucleus;superior cervical ganglion;tongue;cerebellum peduncles;beta cell islets;trigeminal ganglion;skeletal muscle;cerebellum; 0.28887 0.85050 -0.139478553 43.29440906 1149.53078 6.46000 PRSS3P1 . . . protease, serine 3 pseudogene 1 . . . . . . . . . . . PRSS3P2 . . . protease, serine 3 pseudogene 2 FUNCTION: May regulate cell migration. {ECO:0000269|PubMed:15313892}.; . TISSUE SPECIFICITY: Overexpressed in metastasing in non small cell lung tumors, leading to an enhanced cell migration. {ECO:0000269|PubMed:15313892}.; . . . . . . . . PRSS3P3 . . . protease, serine 3 pseudogene 3 . . . . . . . . . . . PRSS3P4 . . . protease, serine 3 pseudogene 4 . . . . . 0.23451 . . . . . PRSS8 0.00338430962613161 0.832489220331792 0.164126470042077 protease, serine 8 FUNCTION: Possesses a trypsin-like cleavage specificity with a preference for poly-basic substrates. Stimulates epithelial sodium channel (ENaC) activity through activating cleavage of the gamma subunits (SCNN1G). {ECO:0000269|PubMed:15246975, ECO:0000269|PubMed:15474520}.; . TISSUE SPECIFICITY: Found in prostate, liver, salivary gland, kidney, lung, pancreas, colon, bronchus and renal proximal tubular cells. In the prostate gland it may be synthesized in epithelial cells, secreted into the ducts, and excreted into the seminal fluid.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;testis;bladder;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;prostate;lung;trachea;thyroid;placenta;liver;kidney; 0.24615 0.19892 -0.139478553 43.29440906 12.41809 0.45023 PRSS12 4.55000945509139e-18 0.020406075676599 0.979593924323401 protease, serine 12 FUNCTION: Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations. {ECO:0000250}.; . TISSUE SPECIFICITY: Brain and Leydig cells of the testis.; ovary;salivary gland;intestine;colon;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;testis;bladder;brain;unclassifiable (Anatomical System);pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;fetal brain;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.20626 0.13614 0.07167258 59.15899976 3342.41847 11.06917 PRSS16 2.23791834002529e-06 0.975077477919405 0.0249202841622546 protease, serine 16 FUNCTION: Protease that may play a role in T-cell development.; . TISSUE SPECIFICITY: Expressed predominantly in cortical thymic epithelial cells.; unclassifiable (Anatomical System);medulla oblongata;lymph node;ovary;colon;parathyroid;retina;uterus;whole body;lung;placenta;thyroid;cervix;stomach;thymus; superior cervical ganglion;trigeminal ganglion;thymus; 0.29795 0.10774 -0.380166007 27.88393489 1620.43255 7.44535 PRSS21 3.27226707337438e-07 0.183773976560701 0.816225696212592 protease, serine 21 FUNCTION: Could regulate proteolytic events associated with testicular germ cell maturation.; . TISSUE SPECIFICITY: Expressed predominantly in premeiotic testicular germ cells, mostly late pachytene and diplotene spermatocytes.; unclassifiable (Anatomical System);uterus;bile duct;pancreas;lung;ovary;heart;testis;colon;cervix;brain;skin; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.16715 0.09440 0.218717575 68.27081859 189.03039 2.98550 PRSS22 0.0154763640761076 0.879877943107297 0.104645692816596 protease, serine 22 FUNCTION: Preferentially cleaves the synthetic substrate H-D-Leu- Thr-Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA. {ECO:0000269|PubMed:11602603}.; . TISSUE SPECIFICITY: Expressed abundantly in the epithelial cells of the airways, including trachea, esophagus and fetal lung. Scarce in adult lung. Expressed at low levels in placenta, pancreas, prostate and thyroid gland. {ECO:0000269|PubMed:11602603}.; unclassifiable (Anatomical System);islets of Langerhans;urinary;colon;uterus;pancreas;lung;endometrium;larynx;placenta;testis;head and neck;kidney;stomach; superior cervical ganglion; . . -0.714505427 14.4019816 43.42765 1.25428 PRSS23 1.26863442289862e-06 0.367807947552427 0.63219078381315 protease, serine 23 . . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;endometrium;bone;thyroid;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;hypothalamus;urinary;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;aorta; . 0.28081 0.12895 0.042348793 57.31304553 51.00422 1.40691 PRSS27 8.68860972407141e-07 0.170699854431437 0.82929927670759 protease, serine 27 . . TISSUE SPECIFICITY: Expressed predominantly in the pancreas. {ECO:0000269|PubMed:12441343}.; unclassifiable (Anatomical System);uterus;placenta;hypopharynx;cervix;head and neck;lens;brain;skin;stomach; . 0.14438 0.18092 0.198490371 67.30360934 155.30094 2.72291 PRSS29P . . . protease, serine 29, pseudogene . . . . . . . . . . . PRSS30P . . . protease, serine, 30 pseudogene . . . . . . . . . . . PRSS33 0.000160243696997293 0.439783391510292 0.560056364792711 protease, serine 33 FUNCTION: Serine protease that has amidolytic activity, cleaving its substrates before Arg residues. {ECO:0000269|PubMed:12795636}.; . TISSUE SPECIFICITY: Predominantly expressed in macrophages. Present in the spleen, small and large intestine, lung and brain (at protein level). Highly expressed in peripheral leukocytes, ovary, retina, spleen and stomach. Moderately expressed in thymus, uterus and platelets, as well as some brain tissues, such as thalamus and fetal brain. {ECO:0000269|PubMed:12795636}.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;lung;cornea;endometrium;visual apparatus;liver;kidney;brain;mammary gland; dorsal root ganglion;ciliary ganglion;atrioventricular node; 0.05419 . . . 451.00798 4.41353 PRSS35 1.33594366817905e-06 0.215062459878191 0.784936204178141 protease, serine 35 . . . . . 0.21613 0.10211 -0.446304853 24.33356924 74.11501 1.79894 PRSS36 4.42359099895437e-13 0.168465104431352 0.831534895568206 protease, serine 36 FUNCTION: Serine protease. Hydrolyzes the peptides N-t-Boc-Gln- Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC and, to a lesser extent, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Val-Leu-Lys-AMC. Has a preference for substrates with an Arg instead of a Lys residue in position P1.; . TISSUE SPECIFICITY: Expressed in fetal kidney, skeletal muscle, liver, placenta and heart. Also expressed in tumor cell lines derived from lung and colon adenocarcinomas. {ECO:0000269|PubMed:15536082}.; unclassifiable (Anatomical System);optic nerve;heart;macula lutea;cervix;fovea centralis;choroid;lens;brain;retina;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node; 0.21065 0.11595 0.801024817 87.65628686 374.85449 4.08288 PRSS37 0.001727084840966 0.894374262640334 0.1038986525187 protease, serine 37 . . . unclassifiable (Anatomical System);lung;testis; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skin; . . 0.68351529 85.03774475 70.93988 1.75415 PRSS38 0.0302666135927824 0.924653770873147 0.0450796155340703 protease, serine 38 . . . . . . . 1.422020658 94.93394669 1792.01767 7.81450 PRSS41 . . . protease, serine 41 . . . . . . . . . . . PRSS42 4.68320795534589e-05 0.651123630433156 0.348829537487291 protease, serine 42 . . . . . . . 0.014844891 54.94810097 15.17186 0.54611 PRSS43 . . . protease, serine 43 . . . . . . . . . . . PRSS44 . . . protease, serine 44 . . . . . . . . . . . PRSS45 8.77664623875441e-05 0.331610062091875 0.668302171445738 protease, serine 45 . . . . . . . 0.927856124 89.70276008 1621.56642 7.44782 PRSS46 . . . protease, serine 46 . . . . . . . . . 1557.00367 7.31059 PRSS47 . . . protease, serine 47 . . . . . . . . . . . PRSS48 0.000223313869312723 0.745379374864798 0.254397311265889 protease, serine 48 . . . . . . . 1.172206761 92.69874971 5908.27685 15.96719 PRSS50 2.62070748435681e-05 0.524934563344488 0.475039229580668 protease, serine 50 FUNCTION: May be involved in proteolysis through its threonine endopeptidase activity. {ECO:0000269|PubMed:17283160}.; . TISSUE SPECIFICITY: Testis specific. Differentially expressed in some breast cancer tissues.; unclassifiable (Anatomical System);uterus;lung;islets of Langerhans;testis;retina; ciliary ganglion; . . 0.466683681 78.73908941 817.65642 5.61836 PRSS51 . . . protease, serine 51 . . . . . . . . . . . PRSS52P . . . protease, serine 52, pseudogene . . . . . . . . . . . PRSS53 7.27161895996479e-11 0.0697305784264563 0.930269421500828 protease, serine 53 FUNCTION: In vitro can degrade the fibrinogen alpha chain of as well as pro-urokinase-type plasminogen activator. {ECO:0000269|PubMed:16566820}.; . TISSUE SPECIFICITY: Predominantly detected in testis, liver, heart and ovary, as well as in several tumor cell lines. {ECO:0000269|PubMed:16566820}.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;fovea centralis;choroid;lens;skin;skeletal muscle;retina;bone marrow;uterus;pancreas;prostate;optic nerve;whole body;lung;bone;placenta;macula lutea;testis;kidney;brain;mammary gland; superior cervical ganglion;skeletal muscle; . . -0.688817379 15.20405756 4417.39604 13.30378 PRSS54 4.49967790564216e-05 0.642424333147847 0.357530670073096 protease, serine 54 . . . unclassifiable (Anatomical System);lung;hippocampus;testis;cervix;stomach; . . . 0.707379532 85.62750649 274.33348 3.54811 PRSS55 1.2335690846368e-08 0.0544715809870709 0.945528406677238 protease, serine 55 FUNCTION: Probable serine protease. {ECO:0000250}.; . TISSUE SPECIFICITY: Only detected in testis. Expressed in spermatogonia, spermatocytes, spermatids, Leydig and Sertoli cells. Expressed in prostate cancer and ovarian cancer (at protein level). {ECO:0000269|PubMed:18844450, ECO:0000269|PubMed:23436708}.; unclassifiable (Anatomical System);medulla oblongata;testis; testis - seminiferous tubule;testis; . . 0.979225112 90.42816702 1741.38701 7.70317 PRSS56 . . . protease, serine 56 FUNCTION: Serine protease required during eye development. {ECO:0000269|PubMed:21397065}.; DISEASE: Microphthalmia, isolated, 6 (MCOP6) [MIM:613517]: A developmental ocular disorder characterized by small malformed eyes. Clinical features are extreme hyperopia due to short axial length with essentially normal anterior segment, steep corneal curvatures, shallow anterior chamber, thick lenses, and thickened scleral wall. Palpebral fissures appear narrow because of relatively deep-set eyes, visual acuity is mildly to moderately reduced, and anisometropic or strabismic amblyopia is common. The fundus of the eye shows crowded optical disks, tortuous vessels, and an abnormal foveal avascular zone. {ECO:0000269|PubMed:21397065, ECO:0000269|PubMed:21532570, ECO:0000269|PubMed:21850159}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . . . . 277.94055 3.57129 PRSS57 1.72723245472858e-07 0.0690682534624233 0.930931573814331 protease, serine 57 . . . blood;bone marrow; . 0.13383 0.12006 -0.376526807 28.10804435 393.37562 4.17133 PRSS58 6.15774870353692e-05 0.471050071833893 0.528888350679072 protease, serine 58 . . . . . . . 0.240763792 69.36777542 65.98033 1.67310 PRTFDC1 5.27828246084182e-09 0.119117953916043 0.880882040805675 phosphoribosyl transferase domain containing 1 FUNCTION: Has low, barely detectable phosphoribosyltransferase activity (in vitro). Binds GMP, IMP and alpha-D-5-phosphoribosyl 1-pyrophosphate (PRPP). Is not expected to contribute to purine metabolism or GMP salvage.; . . ovary;colon;parathyroid;retina;bone marrow;uterus;whole body;cerebral cortex;thyroid;bone;testis;spinal ganglion;artery;brain;unclassifiable (Anatomical System);lymph node;cartilage;hypothalamus;skeletal muscle;lung;placenta;visual apparatus;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.40914 0.15602 0.082802743 60.09082331 45.12589 1.29029 PRTG 0.0195291074116393 0.980469537914038 1.35467432293479e-06 protogenin FUNCTION: May play a role in anteroposterior axis elongation. {ECO:0000250|UniProtKB:Q2EY15}.; . . . . 0.30925 0.10335 -0.056966364 48.91483841 1611.959 7.42935 PRTN3 0.000831488795975963 0.550144536080008 0.449023975124016 proteinase 3 FUNCTION: Polymorphonuclear leukocyte serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro) and causes emphysema when administered by tracheal insufflation to hamsters.; . . unclassifiable (Anatomical System);uterus;heart;blood;skin;bone marrow; superior cervical ganglion;bone marrow; 0.14638 . 0.461228372 78.46190139 1592.43538 7.38170 PRUNE 0.0107617657791834 0.979855983862065 0.00938225035875183 prune exopolyphosphatase FUNCTION: Phosphodiesterase (PDE) that has higher activity toward cAMP than cGMP, as substrate. Plays a role in cell proliferation, is able to induce cell motility and acts as a negative regulator of NME1. {ECO:0000269|PubMed:10602478, ECO:0000269|PubMed:11687967, ECO:0000269|PubMed:14998490, ECO:0000269|PubMed:16428445, ECO:0000269|PubMed:17906697}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Seems to be overexpressed in aggressive sarcoma subtypes, such as leiomyosarcomas and malignant fibrous histiocytomas (MFH) as well as in the less malignant liposarcomas. {ECO:0000269|PubMed:10602478, ECO:0000269|PubMed:11687967, ECO:0000269|PubMed:15671547}.; smooth muscle;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;larynx;bone;testis;amniotic fluid;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pineal body;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.17527 0.13941 0.707379532 85.62750649 875.83536 5.75906 PRUNE2 3.68321629803942e-12 0.999991467435259 8.53256105754938e-06 prune homolog 2 (Drosophila) FUNCTION: May play an important role in regulating differentiation, survival and aggressiveness of the tumor cells. {ECO:0000269|PubMed:16288218}.; . TISSUE SPECIFICITY: A high level of expression seen in the nervous system (brain, cerebellum and spinal cord) as well as adrenal gland. Expressed at high levels in noneuroblastoma, rhabdomyosarcoma, melanoma and some osteosarcoma cell lines, whereas at only low levels in cancer cell lines of liver, breast, thyroid and colon. Expression is significantly higher in favorable tumors than aggressive ones. {ECO:0000269|PubMed:16288218}.; unclassifiable (Anatomical System);amygdala;breast;uterus;heart;islets of Langerhans;placenta;liver;spleen;vein;skin;skeletal muscle; dorsal root ganglion;amygdala;occipital lobe;superior cervical ganglion;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;caudate nucleus;pons;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.07279 0.07799 2.779178029 99.02689314 10480.06134 22.38246 PRUNEP1 . . . prune exopolyphosphatase pseudogene 1 . . . . . . . . . . . PRX 3.70050570170033e-11 0.500268564902025 0.49973143506097 periaxin FUNCTION: Scaffolding protein that functions as part of a dystroglycan complex in Schwann cells, and as part of EZR and AHNAK-containing complexes in eye lens fiber cells. Required for the maintenance of the peripheral myelin sheath that is essential for normal transmission of nerve impulses and normal perception of sensory stimuli. Required for normal transport of MBP mRNA from the perinuclear to the paranodal regions. Required for normal remyelination after nerve injury. Required for normal elongation of Schwann cells and normal length of the internodes between the nodes of Ranvier. The demyelinated nodes of Ranvier permit saltatory transmission of nerve impulses; shorter internodes cause slower transmission of nerve impulses. Required for the formation of appositions between the abaxonal surface of the myelin sheath and the Schwann cell plasma membrane; the Schwann cell cytoplasm is restricted to regions between these appositions. Required for the formation of Cajal bands and of Schmidt-Lanterman incisures that correspond to short, cytoplasm-filled regions on myelinated nerves. Recruits DRP2 to the Schwann cell plasma membrane. Required for normal protein composition of the eye lens fiber cell plasma membrane and normal eye lens fiber cell morphology. {ECO:0000250|UniProtKB:O55103}.; DISEASE: Dejerine-Sottas syndrome (DSS) [MIM:145900]: A severe degenerating neuropathy of the demyelinating Charcot-Marie-Tooth disease category, with onset by age 2 years. Characterized by motor and sensory neuropathy with very slow nerve conduction velocities, increased cerebrospinal fluid protein concentrations, hypertrophic nerve changes, delayed age of walking as well as areflexia. There are both autosomal dominant and autosomal recessive forms of Dejerine-Sottas syndrome. {ECO:0000269|PubMed:11133365}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease 4F (CMT4F) [MIM:614895]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot- Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie-Tooth disease are designated CMT4. CMT4F is characterized by distal sensory impairment and distal muscle weakness and atrophy affecting the lower more than the upper limbs. The age at onset is variable and can range from childhood to adult years. When the onset is in infancy, the phenotype is characterized as Dejerine-Sottas syndrome. {ECO:0000269|PubMed:22847150}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in spinal cord (PubMed:11133365). Isoform 1 and isoform 2 are found in sciatic nerve and Schwann cells (PubMed:11157804). {ECO:0000269|PubMed:11133365, ECO:0000269|PubMed:11157804}.; unclassifiable (Anatomical System);lymph node;frontal lobe;ovary;cerebral cortex;sympathetic chain;colon;spinal ganglion;lens;brain;skeletal muscle;peripheral nerve;retina; dorsal root ganglion;superior cervical ganglion;olfactory bulb;spinal cord;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.11130 0.16968 -0.180160811 40.17456947 849.04764 5.69431 PRY . . . PTPN13-like, Y-linked . . TISSUE SPECIFICITY: Expressed in testis. Detected in spermatocytes, spermatids and spermatozoa (at protein level). {ECO:0000269|PubMed:11420382, ECO:0000269|PubMed:14665702}.; . . . . . . . . PRY2 . . . PTPN13-like, Y-linked 2 . . TISSUE SPECIFICITY: Expressed in testis. Detected in spermatocytes, spermatids and spermatozoa (at protein level). {ECO:0000269|PubMed:11420382, ECO:0000269|PubMed:14665702}.; . . . . . . . . PRYP1 . . . PTPN13-like, Y-linked pseudogene 1 . . . . . . . . . . . PRYP2 . . . PTPN13-like, Y-linked pseudogene 2 . . . . . . . . . . . PRYP3 . . . PTPN13-like, Y-linked pseudogene 3 . . TISSUE SPECIFICITY: Expressed in testis. Detected in spermatocytes, spermatids and spermatozoa (at protein level). {ECO:0000269|PubMed:11420382, ECO:0000269|PubMed:14665702}.; . . . . . . . . PRYP4 . . . PTPN13-like, Y-linked pseudogene 4 . . TISSUE SPECIFICITY: Expressed in testis. Detected in spermatocytes, spermatids and spermatozoa (at protein level). {ECO:0000269|PubMed:11420382, ECO:0000269|PubMed:14665702}.; . . . . . . . . PRYP5 . . . PTPN13-like, Y-linked pseudogene 5 . . . . . . . . . . . PRYP6 . . . PTPN13-like, Y-linked pseudogene 6 . . . . . . . . . . . PSAP 0.950037220630023 0.0499563887691487 6.39060082810222e-06 prosaposin FUNCTION: Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate.; FUNCTION: Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).; FUNCTION: Saposins are specific low-molecular mass non-enzymic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases.; DISEASE: Combined saposin deficiency (CSAPD) [MIM:611721]: Due to absence of all saposins, leading to a fatal storage disorder with hepatosplenomegaly and severe neurological involvement. {ECO:0000269|PubMed:11309366, ECO:0000269|PubMed:1371116}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leukodystrophy metachromatic due to saposin-B deficiency (MLD-SAPB) [MIM:249900]: An atypical form of metachromatic leukodystrophy. It is characterized by tissue accumulation of cerebroside-3-sulfate, demyelination, periventricular white matter abnormalities, peripheral neuropathy. Additional neurological features include dysarthria, ataxic gait, psychomotor regression, seizures, cognitive decline and spastic quadriparesis. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Gaucher disease, atypical, due to saposin C deficiency (AGD) [MIM:610539]: A disease characterized by marked glucosylceramide accumulation in the spleen without having a deficiency of glucosylceramide-beta glucosidase characteristic of classic Gaucher disease. Gaucher disease is a lysosomal storage disorder characterized by skeletal deterioration, hepatosplenomegaly, and organ dysfunction. There are several subtypes based on the presence and severity of neurological involvement. {ECO:0000269|PubMed:17919309, ECO:0000269|PubMed:2060627}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Krabbe disease, atypical, due to saposin A deficiency (AKRD) [MIM:611722]: A disorder of galactosylceramide metabolism. Clinical features include neurologic regression around age 3 months, loss of spontaneous movements, hyporeflexia, generalized brain atrophy, and diffuse white matter dysmyelination. {ECO:0000269|PubMed:15773042}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in PSAP saposin-D region are found in a variant of Tay-Sachs disease (GM2-gangliosidosis).; . myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;oesophagus;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; . 0.20076 0.40600 -0.997481928 8.47487615 73.16131 1.78719 PSAPL1 3.33502575049141e-11 0.00632412285533319 0.993675877111316 prosaposin-like 1 (gene/pseudogene) FUNCTION: May activate the lysosomal degradation of sphingolipids. {ECO:0000250}.; . . uterus;frontal lobe;heart;skin; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.13719 . 0.916727815 89.56711489 1876.7913 7.97031 PSAT1 2.11054344459797e-09 0.0709267371357893 0.929073260753667 phosphoserine aminotransferase 1 FUNCTION: Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. {ECO:0000250|UniProtKB:P10658}.; DISEASE: Neu-Laxova syndrome 2 (NLS2) [MIM:616038]: A form of Neu- Laxova syndrome, a lethal, autosomal recessive multiple malformation syndrome characterized by ichthyosis, marked intrauterine growth restriction, microcephaly, short neck, limb deformities, hypoplastic lungs, edema, and central nervous system anomalies. These include lissencephaly, cerebellar hypoplasia and/or abnormal/agenesis of the corpus callosum. Abnormal facial features include severe proptosis with ectropion, hypertelorism, micrognathia, flattened nose, and malformed ears. {ECO:0000269|PubMed:25152457}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at high levels in the brain, liver, kidney and pancreas, and very weakly expressed in the thymus, prostate, testis and colon.; ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;larynx;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;mesenchyma;epididymis;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;stomach;thymus; . . 0.48406 -0.291981272 33.20358575 33.55043 1.03606 PSAT1P1 . . . phosphoserine aminotransferase 1 pseudogene 1 . . . . . . . . . . . PSAT1P2 . . . phosphoserine aminotransferase 1 pseudogene 2 . . . . . . . . . . . PSAT1P3 . . . phosphoserine aminotransferase 1 pseudogene 3 . . . . . . . . . . . PSAT1P4 . . . phosphoserine aminotransferase 1 pseudogene 4 . . . . . . . . . . . PSBP1 . . . prostatic steroid binding protein 1 . . . . . . . . . . . PSCA 0.00894842686480651 0.579834097145547 0.411217475989646 prostate stem cell antigen FUNCTION: May be involved in the regulation of cell proliferation. Has a cell-proliferation inhibition activity in vitro. {ECO:0000269|PubMed:18488030}.; . TISSUE SPECIFICITY: Highly expressed in prostate (basal, secretory and neuroendocrine epithelium cells). Also found in bladder (transitional epithelium), placenta (trophoblasts), stomach (neuroendocrine cells), colon (neuroendocrine cells) and kidney (collecting ducts). Overexpressed in prostate cancers and expression is correlated with tumor stage, grade and androgen- independence. Highly expressed in prostate cancer bone metastases. Expressed in gastric epithelial cells, mainly in the isthmus (at protein level). Not detected in normal intestinal epithelium (at protein level). {ECO:0000269|PubMed:10713670, ECO:0000269|PubMed:18488030}.; unclassifiable (Anatomical System);cartilage;heart;colon;blood;skin;breast;pancreas;prostate;whole body;lung;bone;placenta;visual apparatus;liver;testis;cervix;spleen;kidney;brain;stomach; . 0.10617 0.15182 . . 117.96949 2.36214 PSD 0.987334022305881 0.012665968942797 8.75132194777027e-09 pleckstrin and Sec7 domain containing FUNCTION: Guanine nucleotide exchange factor for ARF6. Induces cytoskeletal remodeling (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 2 is expressed in the brain. {ECO:0000269|PubMed:9417912}.; ovary;colon;choroid;fovea centralis;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;pituitary gland;testis;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;hypothalamus;lens;lung;placenta;visual apparatus;macula lutea;aorta;peripheral nerve; whole brain;amygdala;superior cervical ganglion;medulla oblongata;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.11541 0.10253 -1.322782544 4.759377212 234.01091 3.30663 PSD2 0.180222827298736 0.819670972257887 0.000106200443376728 pleckstrin and Sec7 domain containing 2 . . . unclassifiable (Anatomical System);fovea centralis;skeletal muscle;uterus;optic nerve;whole body;lung;frontal lobe;larynx;macula lutea;testis;head and neck;brain;cerebellum; subthalamic nucleus;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;prefrontal cortex;globus pallidus;caudate nucleus;pons;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.16987 0.10571 0.007353605 54.12243454 152.91807 2.70508 PSD3 0.851705649436322 0.148294173125023 1.7743865529105e-07 pleckstrin and Sec7 domain containing 3 FUNCTION: Guanine nucleotide exchange factor for ARF6. {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 2 is expressed in epididymis (at protein level). {ECO:0000269|PubMed:20736409}.; lymphoreticular;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;larynx;bone;thyroid;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;spinal cord;muscle;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;alveolus;spleen;head and neck;mammary gland;stomach; whole brain;amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;adrenal gland;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.62203 . 0.102819578 60.96956829 622.28445 5.02944 PSD4 0.805496070283155 0.194503557512148 3.72204697214165e-07 pleckstrin and Sec7 domain containing 4 FUNCTION: Guanine nucleotide exchange factor for ARF6 and ARL14/ARF7. Through ARL14 activation, controls the movement of MHC class II-containing vesicles along the actin cytoskeleton in dendritic cells. Involved in membrane recycling. Interacts with several phosphatidylinositol phosphate species, including phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 3,5- bisphosphate and phosphatidylinositol 4,5-bisphosphate. {ECO:0000269|PubMed:12082148, ECO:0000269|PubMed:21458045}.; . TISSUE SPECIFICITY: Widely expressed. Highest levels of expression are found in placenta, pancreas, spleen, thymus and peripheral blood. {ECO:0000269|PubMed:12082148}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;thyroid;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;peripheral nerve;thymus; superior cervical ganglion;liver;white blood cells;thymus; 0.07411 0.07779 1.407269618 94.78650625 353.71179 3.98118 PSEN1 0.997601160543998 0.00239875012598488 8.93300174152101e-08 presenilin 1 FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. Stimulates cell-cell adhesion though its association with the E-cadherin/catenin complex. Under conditions of apoptosis or calcium influx, cleaves E-cadherin promoting the disassembly of the E-cadherin/catenin complex and increasing the pool of cytoplasmic beta-catenin, thus negatively regulating Wnt signaling. May also play a role in hematopoiesis. {ECO:0000269|PubMed:10206644, ECO:0000269|PubMed:10545183, ECO:0000269|PubMed:10593990, ECO:0000269|PubMed:10811883, ECO:0000269|PubMed:10899933, ECO:0000269|PubMed:11226248, ECO:0000269|PubMed:15341515, ECO:0000269|PubMed:16305624}.; DISEASE: Alzheimer disease 3 (AD3) [MIM:607822]: A familial early- onset form of Alzheimer disease. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. {ECO:0000269|PubMed:10025789, ECO:0000269|PubMed:10090481, ECO:0000269|PubMed:10200054, ECO:0000269|PubMed:10208579, ECO:0000269|PubMed:10439444, ECO:0000269|PubMed:10441572, ECO:0000269|PubMed:10447269, ECO:0000269|PubMed:10533070, ECO:0000269|PubMed:10631141, ECO:0000269|PubMed:10644793, ECO:0000269|PubMed:11027672, ECO:0000269|PubMed:11710891, ECO:0000269|PubMed:11920851, ECO:0000269|PubMed:12048239, ECO:0000269|PubMed:12484344, ECO:0000269|PubMed:12493737, ECO:0000269|PubMed:22503161, ECO:0000269|PubMed:7550356, ECO:0000269|PubMed:7596406, ECO:0000269|PubMed:7651536, ECO:0000269|PubMed:8634711, ECO:0000269|PubMed:8634712, ECO:0000269|PubMed:8733303, ECO:0000269|PubMed:9172170, ECO:0000269|PubMed:9225696, ECO:0000269|PubMed:9298817, ECO:0000269|PubMed:9384602, ECO:0000269|PubMed:9507958, ECO:0000269|PubMed:9521423, ECO:0000269|PubMed:9719376, ECO:0000269|PubMed:9831473, ECO:0000269|PubMed:9833068, ECO:0000269|Ref.78}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Frontotemporal dementia (FTD) [MIM:600274]: A form of dementia characterized by pathologic finding of frontotemporal lobar degeneration, presenile dementia with behavioral changes, deterioration of cognitive capacities and loss of memory. In some cases, parkinsonian symptoms are prominent. Neuropathological changes include frontotemporal atrophy often associated with atrophy of the basal ganglia, substantia nigra, amygdala. In most cases, protein tau deposits are found in glial cells and/or neurons. {ECO:0000269|PubMed:11094121}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1U (CMD1U) [MIM:613694]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:17186461}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Acne inversa, familial, 3 (ACNINV3) [MIM:613737]: A chronic relapsing inflammatory disease of the hair follicles characterized by recurrent draining sinuses, painful skin abscesses, and disfiguring scars. Manifestations typically appear after puberty. {ECO:0000269|PubMed:20929727}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in a wide range of tissues including various regions of the brain, liver, spleen and lymph nodes. {ECO:0000269|PubMed:11987239, ECO:0000269|PubMed:8574969}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;muscle;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;medulla oblongata;thalamus;occipital lobe;spinal cord;testis;pons;caudate nucleus;trigeminal ganglion;parietal lobe; 0.94871 0.87580 -0.337894035 30.37272942 60.74439 1.58457 PSEN2 0.0270141824537153 0.961183973490347 0.0118018440559376 presenilin 2 FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. May function in the cytoplasmic partitioning of proteins. {ECO:0000269|PubMed:10497236, ECO:0000269|PubMed:10652302}.; DISEASE: Alzheimer disease 4 (AD4) [MIM:606889]: A familial early- onset form of Alzheimer disease. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. {ECO:0000269|PubMed:10631141, ECO:0000269|PubMed:10732806, ECO:0000269|PubMed:22503161, ECO:0000269|PubMed:7638622, ECO:0000269|PubMed:7651536, ECO:0000269|PubMed:9384602}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1V (CMD1V) [MIM:613697]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:17186461}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is seen in the placenta, skeletal muscle and heart while isoform 2 is seen in the heart, brain, placenta, liver, skeletal muscle and kidney. {ECO:0000269|PubMed:8574969}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;aorta; superior cervical ganglion;skeletal muscle; 0.64189 0.66407 -1.019530098 8.038452465 211.70746 3.13692 PSENEN 0.535694860133088 0.449167649611101 0.0151374902558117 presenilin enhancer gamma secretase subunit FUNCTION: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta- amyloid precursor protein). Probably represents the last step of maturation of gamma-secretase, facilitating endoproteolysis of presenilin and conferring gamma-secretase activity. {ECO:0000269|PubMed:12522139, ECO:0000269|PubMed:12763021}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in leukocytes, lung, placenta, small intestine, liver, kidney, spleen thymus, skeletal muscle, heart and brain. {ECO:0000269|PubMed:12110170, ECO:0000269|PubMed:12740439}.; ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;lung;adrenal gland;nasopharynx;placenta;hippocampus;liver;spleen;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.25672 . 0.101211609 60.95777306 12.82133 0.46726 PSG1 3.44125355062010e-12 0.0227041263875489 0.97729587360901 pregnancy specific beta-1-glycoprotein 1 . . . uterus;bile duct;unclassifiable (Anatomical System);whole body;heart;frontal lobe;placenta;liver;spleen;skin;stomach;aorta; dorsal root ganglion;superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; . . 1.851941967 97.1455532 1073.11648 6.28095 PSG2 6.18608797738968e-07 0.441195774287073 0.558803607104129 pregnancy specific beta-1-glycoprotein 2 . . . placenta;liver;spleen;blood;stomach;bone marrow; . 0.07772 . 1.401792296 94.75112055 126.24057 2.44595 PSG3 2.30575719944982e-12 0.0343817552681336 0.965618244729561 pregnancy specific beta-1-glycoprotein 3 . . . unclassifiable (Anatomical System);frontal lobe;epididymis;placenta;liver;colon;spleen;skin;stomach; superior cervical ganglion;placenta;ciliary ganglion;trigeminal ganglion; . . 1.183126933 92.82849729 375.80846 4.08857 PSG4 7.89516459070488e-10 0.142725512980173 0.85727448623031 pregnancy specific beta-1-glycoprotein 4 . . . unclassifiable (Anatomical System);epididymis;placenta;colon;skin; . . . 2.180909934 98.08327436 470.5539 4.48902 PSG5 1.20871976273802e-10 0.0492627703993902 0.950737229479738 pregnancy specific beta-1-glycoprotein 5 . . TISSUE SPECIFICITY: Synthesized by syncytiotrophoblast of the placenta.; unclassifiable (Anatomical System);uterus;bile duct;whole body;placenta;liver;spleen;skin;stomach; . . . 2.734169767 98.95612173 2276.49664 8.82406 PSG6 2.97106013168008e-09 0.160390480337806 0.839609516691134 pregnancy specific beta-1-glycoprotein 6 . . . unclassifiable (Anatomical System);lung;whole body;ovary;epididymis;placenta;visual apparatus;liver;parathyroid;spleen;skin; . 0.26273 . 2.166192036 98.0301958 170.30147 2.84730 PSG7 . . . pregnancy specific beta-1-glycoprotein 7 (gene/pseudogene) . . . . . . . . . . . PSG8 1.92926054362959e-10 0.0644679117538643 0.93553208805321 pregnancy specific beta-1-glycoprotein 8 . . . unclassifiable (Anatomical System);frontal lobe;placenta;liver;spleen;stomach; . . . 1.072886248 91.70794999 898.91198 5.83925 PSG9 2.7470177840116e-14 0.00492566057880838 0.995074339421164 pregnancy specific beta-1-glycoprotein 9 . . . unclassifiable (Anatomical System);ovary;colon;parathyroid;skin;breast;whole body;lung;frontal lobe;placenta;visual apparatus;liver;testis;spleen;stomach; dorsal root ganglion;superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.24972 . 1.607548084 95.91884879 1896.34765 8.00804 PSG10P . . . pregnancy specific beta-1-glycoprotein 10, pseudogene . . . . . . . . . . . PSG11 7.20270893081861e-09 0.141564498457536 0.858435494339755 pregnancy specific beta-1-glycoprotein 11 . . . unclassifiable (Anatomical System);epididymis;placenta;liver;spleen;aorta; . . . 0.802845857 87.69167256 34.03895 1.04368 PSIP1 0.946350057562085 0.0536496293973396 3.1304057564564e-07 PC4 and SFRS1 interacting protein 1 FUNCTION: Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stress-induced apoptosis. Isoform 2 is a more general and stronger transcriptional coactivator. Isoform 2 may also act as an adapter to coordinate pre-mRNA splicing. Cellular cofactor for lentiviral integration. {ECO:0000269|PubMed:15642333}.; DISEASE: Note=A chromosomal aberration involving PSIP1 is associated with pediatric acute myeloid leukemia (AML) with intermediate characteristics between M2-M3 French-American-British (FAB) subtypes. Translocation t(9;11)(p22;p15) with NUP98. The chimeric transcript is an in-frame fusion of NUP98 exon 8 to PSIP1 exon 4. {ECO:0000269|PubMed:15725483}.; TISSUE SPECIFICITY: Widely expressed. Expressed at high level in the thymus. Expressed in fetal and adult brain. Expressed in neurons, but not astrocytes. Markedly elevated in fetal as compared to adult brain. In the adult brain, expressed in the subventricular zone (SVZ), in hippocampus, and undetectable elsewhere. In the fetal brain, expressed in the germinal neuroepithelium and cortical plate regions. {ECO:0000269|PubMed:15642333, ECO:0000269|PubMed:9822615}.; . . 0.99037 0.15245 -0.047654689 50.22410946 197.3359 3.03703 PSIP1P1 . . . PC4 and SFRS1 interacting protein 1 pseudogene 1 . . . . . . . . . . . PSIP1P2 . . . PC4 and SFRS1 interacting protein 1 pseudogene 2 . . . . . . . . . . . PSKH1 0.0178742052133664 0.893731330773748 0.0883944640128854 protein serine kinase H1 FUNCTION: May be a SFC-associated serine kinase (splicing factor compartment-associated serine kinase) with a role in intranuclear SR protein (non-snRNP splicing factors containing a serine/arginine-rich domain) trafficking and pre-mRNA processing. {ECO:0000269|PubMed:12466556}.; . TISSUE SPECIFICITY: Expressed in all tissues and cell lines tested with the highest level of abundance in testis. {ECO:0000269|PubMed:11087665}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;synovium;thyroid;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;appendix;testis;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.46757 0.14122 -0.736552314 13.93606983 20.26929 0.69311 PSKH2 1.74383885343745e-07 0.130166845985621 0.869832979630494 protein serine kinase H2 . . . . . 0.10219 0.09736 1.131742211 92.26232602 1099.91572 6.34747 PSMA1 0.947988404934487 0.0519767022560348 3.48928094784292e-05 proteasome subunit alpha 1 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Mediates the lipopolysaccharide-induced signal transduction in the macrophage proteasome (By similarity). Might be involved in the anti-inflammatory response of macrophages during the interaction with C.albicans heat-inactivated cells (By similarity). {ECO:0000250}.; . . . . 0.94257 0.50622 -0.229483771 36.86010852 24.18661 0.79430 PSMA2 0.937474829201216 0.0624696805192404 5.54902795436633e-05 proteasome subunit alpha 2 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation.; . . medulla oblongata;ovary;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.98914 0.19444 -0.053113545 49.38664779 2.40691 0.08453 PSMA2P1 . . . proteasome (prosome, macropain) subunit, alpha type, 2 pseudogene 1 . . . . . . . . . . . PSMA2P2 . . . proteasome (prosome, macropain) subunit, alpha type, 2 pseudogene 2 . . . . . . . . . . . PSMA2P3 . . . proteasome (prosome, macropain) subunit, alpha type, 2 pseudogene 3 . . . . . . . . . . . PSMA3 0.99028192222966 0.00971535324383934 2.72452650085325e-06 proteasome subunit alpha 3 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2. {ECO:0000269|PubMed:11350925, ECO:0000269|PubMed:17499743}.; . . myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; tumor; 0.99440 0.40044 -0.317668748 31.45789101 3.37723 0.12251 PSMA3-AS1 . . . PSMA3 antisense RNA 1 . . . . . . . . . . . PSMA3P . . . proteasome (prosome, macropain) subunit, alpha type, 3 pseudogene . . . . . . . . . . . PSMA4 0.620423590120457 0.377947303197172 0.00162910668237076 proteasome subunit alpha 4 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.; . . lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;iris;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;spleen;kidney;stomach; testis - interstitial; 0.96879 0.38765 -0.09720619 46.20193442 6.98921 0.26082 PSMA5 0.974255885097096 0.0257142523316313 2.98625712727678e-05 proteasome subunit alpha 5 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.; . TISSUE SPECIFICITY: Expressed in fetal brain (at protein level). {ECO:0000269|PubMed:11771738}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;umbilical cord;sympathetic chain;skin;retina;prostate;optic nerve;endometrium;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;testis;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach;thymus; superior cervical ganglion;testis;tumor; 0.97837 0.53296 -0.075159878 47.78839349 4.78683 0.17421 PSMA6 0.943987639676727 0.0558060682861092 0.000206292037163698 proteasome subunit alpha 6 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.; . . ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;bladder;brain;gall bladder;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; . 0.98841 0.38765 -0.007201372 53.19061099 1.69455 0.05520 PSMA6P1 . . . proteasome (prosome, macropain) subunit, alpha type, 6 pseudogene 1 . . . . . . . . . . . PSMA6P2 . . . proteasome (prosome, macropain) subunit, alpha type, 6 pseudogene 2 . . . . . . . . . . . PSMA6P3 . . . proteasome (prosome, macropain) subunit, alpha type, 6 pseudogene 3 . . . . . . . . . . . PSMA6P4 . . . proteasome (prosome, macropain) subunit, alpha type, 6 pseudogene 4 . . . . . . . . . . . PSMA7 0.965751461122936 0.0341880178297002 6.05210473642826e-05 proteasome subunit alpha 7 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Plays an important role in the regulation of cell proliferation or cell cycle control, transcriptional regulation, immune and stress response, cell differentiation, and apoptosis. Interacts with some important proteins involved in transcription factor regulation, cell cycle transition, viral replication and even tumor initiation and progression. Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response. {ECO:0000269|PubMed:11389899, ECO:0000269|PubMed:11713272, ECO:0000269|PubMed:12119296, ECO:0000269|PubMed:19442227, ECO:0000269|PubMed:19734229}.; . . . . 0.93228 0.54054 -0.141298762 42.87567823 5.77064 0.21648 PSMA7P . . . proteasome (prosome, macropain) subunit, alpha type, 7 pseudogene . . . . . . . . . . . PSMA8 0.00397964772969195 0.958887576171115 0.037132776099193 proteasome subunit alpha 8 FUNCTION: Component of the spermatoproteasome, a form of the proteasome specifically found in testis that promotes degradation of histones, thereby participating actively to the exchange of histones during spermatogenesis. The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;nasopharynx;testis; subthalamic nucleus;superior cervical ganglion;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.06247 0.14184 -0.139478553 43.29440906 38.9722 1.15552 PSMB1 0.718811352095635 0.278101550742073 0.00308709716229158 proteasome subunit beta 1 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.; . . myocardium;lymphoreticular;ovary;skin;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;tonsil;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;oesophagus;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;placenta;kidney;stomach; testis - interstitial;testis - seminiferous tubule;placenta;testis;skeletal muscle; 0.92196 0.33472 0.170987912 65.5579146 1798.99636 7.82122 PSMB2 0.972351383142869 0.0276129954567253 3.56214004062827e-05 proteasome subunit beta 2 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit has a trypsin-like activity.; . . . . 0.97348 0.13730 0.12689526 63.00424628 84.86683 1.96295 PSMB3 0.697590277224645 0.298578009846882 0.00383171292847286 proteasome subunit beta 3 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.; . . ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;endometrium;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta; heart;liver; 0.84491 0.30945 0.3032669 72.009908 1438.05221 7.07559 PSMB3P . . . proteasome (prosome, macropain) subunit, beta type, 3 pseudogene . . . . . . . . . . . PSMB3P2 . . . proteasome (prosome, macropain) subunit, beta type, 3 pseudogene 2 . . . . . . . . . . . PSMB4 0.398813284714522 0.599275783632883 0.00191093165259489 proteasome subunit beta 4 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Mediates the lipopolysaccharide-induced signal macrophage proteasome (By similarity). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. {ECO:0000250, ECO:0000269|PubMed:12097147}.; . . lymphoreticular;medulla oblongata;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;kidney;mammary gland;stomach;cerebellum; thalamus;smooth muscle;heart;cerebellum peduncles;globus pallidus;parietal lobe;cerebellum; 0.86588 0.29568 -0.05129383 49.75819769 1699.46831 7.60101 PSMB5 0.758964107014505 0.239060593805921 0.00197529917957396 proteasome subunit beta 5 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib. May catalyze basal processing of intracellular antigens. Plays a role in the protection against oxidative damage through the Nrf2-ARE pathway (By similarity). {ECO:0000250, ECO:0000269|PubMed:18502982, ECO:0000269|PubMed:18565852}.; . . myocardium;lymphoreticular;medulla oblongata;smooth muscle;umbilical cord;ovary;skin;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;spinal cord;urinary;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;kidney;stomach;thymus; thalamus;parietal lobe; 0.86174 0.35390 0.03689118 56.64071715 307.27727 3.73032 PSMB6 0.143186390069862 0.837990716695511 0.0188228932346273 proteasome subunit beta 6 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This unit is responsible of the peptidyl glutamyl-like activity. May catalyze basal processing of intracellular antigens.; . . medulla oblongata;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;vein;uterus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; whole brain;thalamus;parietal lobe; 0.84031 0.16749 -0.139478553 43.29440906 296.75779 3.67614 PSMB7 0.941261762860495 0.0585058226349532 0.00023241450455211 proteasome subunit beta 7 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This unit is responsible of the trypsin-like activity.; . TISSUE SPECIFICITY: Expressed at a low level in colonic mucosa. Up-regulated in colorectal cancer tissues. {ECO:0000269|PubMed:18549262}.; myocardium;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;pancreas;lung;placenta;kidney;stomach;aorta;thymus; testis - interstitial;testis - seminiferous tubule;testis; 0.50835 0.16348 0.104848986 61.49445624 3929.05465 12.39015 PSMB7P1 . . . PSMB7 pseudogene 1 . . . . . . . . . . . PSMB8 0.0120031719912635 0.951127903658414 0.0368689243503228 proteasome subunit beta 8 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB5 by PSMB8 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. Acts as a major component of interferon gamma-induced sensitivity. Plays a key role in apoptosis via the degradation of the apoptotic inhibitor MCL1. May be involved in the inflammatory response pathway. In cancer cells, substitution of isoform 1 (E2) by isoform 2 (E1) results in immunoproteasome deficiency. Required for the differentiation of preadipocytes into adipocytes. {ECO:0000269|PubMed:16423992, ECO:0000269|PubMed:19443843, ECO:0000269|PubMed:21881205, ECO:0000269|PubMed:8163024}.; DISEASE: Nakajo syndrome (NKJO) [MIM:256040]: An autosomal recessive autoinflammatory disorder characterized by early childhood onset of recurrent fever, joint stiffness and severe contractures of the hands and feet, and erythematous skin lesions with subsequent development of lipodystrophy and laboratory evidence of immune dysregulation. Accompanying features may include muscle weakness and atrophy, hepatosplenomegaly, and microcytic anemia. {ECO:0000269|PubMed:21129723, ECO:0000269|PubMed:21852578, ECO:0000269|PubMed:21881205}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Mutation Met-75 has been found in chronic atypical neutrophilic dermatosis with lipodystrophy and elevated temperature syndrome (CANDLE syndrome). CANDLE patients have some overlapping features with NKJO patients, including a cutaneous eruption and lipodystrophy. They show a characteristic neutrophilic dermatosis with a mononuclear interstitial infiltrate in the dermis that seems pathognomonic for CANDLE syndrome (PubMed:21953331). {ECO:0000269|PubMed:21953331}.; . . . 0.40872 . 0.040529541 57.15380986 1719.52867 7.64727 PSMB8-AS1 . . . PSMB8 antisense RNA 1 (head to head) . . . . . 0.67676 . . . . . PSMB9 0.225647028212841 0.766469888301112 0.00788308348604729 proteasome subunit beta 9 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB6 by PSMB9 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. {ECO:0000269|PubMed:8163024}.; . . . . 0.67676 . 0.637604436 83.77565464 1708.23884 7.62151 PSMB10 2.33997900720924e-05 0.501022297321912 0.498954302888016 proteasome subunit beta 10 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides.; . . myocardium;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;larynx;bone;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; tumor;white blood cells;whole blood;thymus; 0.67811 0.19056 -0.405853867 26.23260203 38.03927 1.13010 PSMB11 0.0171391308148329 0.714168521793852 0.268692347391316 proteasome (prosome, macropain) subunit, beta type, 11 FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Incorporated instead of PSMB5 or PSMB8, this unit reduces the chymotrypsin-like activity of the proteasome (By similarity). Plays a pivotal role in development of CD8-positive T cells (By similarity). {ECO:0000250}.; . . . . 0.36564 . 0.110306132 62.00165133 138.67322 2.56576 PSMC1 0.995728890599096 0.00427074431995713 3.65080946532943e-07 proteasome 26S subunit, ATPase 1 FUNCTION: The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.; . . ovary;skin;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;spinal cord;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;cerebral cortex;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;cerebellum; subthalamic nucleus;testis - interstitial;testis; 0.85830 . -0.295622497 32.61972163 3.30599 0.12023 PSMC1P1 . . . proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 1 . . . . . . . . . . . PSMC1P2 . . . proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 2 . . . . . . . . . . . PSMC1P3 . . . proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 3 . . . . . . . . . . . PSMC1P4 . . . proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 4 . . . . . . . . . . . PSMC1P5 . . . proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 5 . . . . . . . . . . . PSMC1P6 . . . proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 6 . . . . . . . . . . . PSMC1P7 . . . proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 7 . . . . . . . . . . . PSMC1P8 . . . proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 8 . . . . . . . . . . . PSMC1P9 . . . proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 9 . . . . . . . . . . . PSMC1P10 . . . proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 10 . . . . . . . . . . . PSMC1P11 . . . proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 11 . . . . . . . . . . . PSMC1P12 . . . proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 12 . . . . . . . . . . . PSMC1P13 . . . proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 13 . . . . . . . . . . . PSMC2 0.999210832748991 0.000789161309085552 5.94192349064721e-09 proteasome 26S subunit, ATPase 2 FUNCTION: The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex. In case of HIV-1 infection, positive modulator of Tat-mediated transactivation. {ECO:0000269|PubMed:9295362}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; medulla oblongata;superior cervical ganglion;prefrontal cortex;globus pallidus;trigeminal ganglion;skeletal muscle; 0.86027 . -0.273576253 33.97027601 6.07663 0.23004 PSMC3 0.979199713289554 0.0207967096252852 3.57708516053218e-06 proteasome 26S subunit, ATPase 3 FUNCTION: The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). In case of HIV-1 infection, suppresses Tat-mediated transactivation. {ECO:0000250}.; . . lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus; globus pallidus;caudate nucleus; 0.99215 0.39888 -0.471992905 23.03609342 0.9687 0.02427 PSMC3IP 0.00019254510299238 0.715204416126028 0.284603038770979 PSMC3 interacting protein FUNCTION: Plays an important role in meiotic recombination. Stimulates DMC1-mediated strand exchange required for pairing homologous chromosomes during meiosis. The complex PSMC3IP/MND1 binds DNA, stimulates the recombinase activity of DMC1 as well as DMC1 D-loop formation from double-strand DNA. This complex stabilizes presynaptic RAD51 and DMC1 filaments formed on single strand DNA to capture double-strand DNA. This complex stimulates both synaptic and presynaptic critical steps in RAD51 and DMC1- promoted homologous pairing. May inhibit HIV-1 viral protein TAT activity and modulate the activity of proteasomes through association with PSMC3. Acts as a tissue specific coactivator of hormone-dependent transcription mediated by nuclear receptors. {ECO:0000269|PubMed:10806355, ECO:0000269|PubMed:16407260, ECO:0000269|PubMed:21963259}.; DISEASE: Ovarian dysgenesis 3 (ODG3) [MIM:614324]: A disorder characterized by lack of spontaneous pubertal development, primary amenorrhea, uterine hypoplasia, and hypergonadotropic hypogonadism as a result of streak gonads. {ECO:0000269|PubMed:21963259}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in testis and colon. {ECO:0000269|PubMed:11739747, ECO:0000269|PubMed:7490091}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;tumor;testis;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; 0.06995 0.10859 -0.293801652 32.93819297 546.06968 4.75216 PSMC3P . . . proteasome (prosome, macropain) 26S subunit, ATPase, 3 pseudogene . . . . . . . . . . . PSMC4 0.605976545511019 0.393646934764955 0.000376519724025465 proteasome 26S subunit, ATPase 4 FUNCTION: The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex. {ECO:0000269|PubMed:8060531}.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;hypothalamus;muscle;adrenal cortex;pharynx;blood;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; testis - interstitial;placenta; 0.43079 0.38765 -0.560178693 19.30879925 5.5116 0.20576 PSMC5 0.969571425390585 0.0304194127561526 9.16185326239998e-06 proteasome 26S subunit, ATPase 5 FUNCTION: The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.; . . lymphoreticular;ovary;skin;retina;prostate;frontal lobe;endometrium;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; testis - interstitial;medulla oblongata;thalamus;hypothalamus;temporal lobe;pons;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;cingulate cortex;parietal lobe; 0.57059 0.20700 -0.317668748 31.45789101 7.15596 0.26814 PSMC6 0.995511977073858 0.00448793954027741 8.33858643247666e-08 proteasome 26S subunit, ATPase 6 FUNCTION: The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.; . . . . 0.99909 . -0.117432389 44.89266336 10.42634 0.37865 PSMC6P1 . . . proteasome 26S subunit, ATPase, 6 pseudogene 1 . . . . . . . . . . . PSMC6P2 . . . proteasome 26S subunit, ATPase, 6 pseudogene 2 . . . . . . . . . . . PSMC6P3 . . . proteasome 26S subunit, ATPase, 6 pseudogene 3 . . . . . . . . . . . PSMD1 0.999999202638138 7.97361861585727e-07 2.99836640659835e-16 proteasome 26S subunit, non-ATPase 1 FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.; . . ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;dura mater;brain;bladder;tonsil;unclassifiable (Anatomical System);meninges;trophoblast;cartilage;heart;tongue;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;pia mater;lung;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;globus pallidus;caudate nucleus;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.94807 0.14977 -0.380166007 27.88393489 75.57454 1.81948 PSMD2 0.999997115740613 2.88425937963702e-06 6.87070564265885e-15 proteasome 26S subunit, non-ATPase 2 FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.; . TISSUE SPECIFICITY: Found in skeletal muscle, liver, heart, brain, kidney, pancreas, lung and placenta.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;bladder;brain;heart;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;developmental;intestine;colon;uterus;oesophagus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;mesenchyma;placenta;hippocampus;amnion;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle;cingulate cortex; 0.94859 0.75045 -0.664951379 15.91177164 603.90861 4.97534 PSMD2P1 . . . proteasome 26S subunit, non-ATPase, 2 pseudogene 1 . . . . . . . . . . . PSMD3 0.999288334519646 0.000711660861569041 4.61878503560812e-09 proteasome 26S subunit, non-ATPase 3 FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.; . . lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;amnion;alveolus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;cerebellum; 0.94656 0.29934 -0.291981272 33.20358575 125.83219 2.44205 PSMD4 0.984312091842397 0.0156790899878506 8.81816975277427e-06 proteasome 26S subunit, non-ATPase 4 FUNCTION: Binds and presumably selects ubiquitin-conjugates for destruction. Displays selectivity for longer polyubiquitin chains. Modulates intestinal fluid secretion.; . . . . 0.96505 . -0.405853867 26.23260203 10.11657 0.36873 PSMD4P1 . . . proteasome (prosome, macropain) 26S subunit, non-ATPase, 4 pseudogene 1 . . . . . . . . . . . PSMD5 1.26579691239429e-05 0.830792821455133 0.169194520575743 proteasome 26S subunit, non-ATPase 5 FUNCTION: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD5:PSMC2:PSMC1:PSMD2 module which probably assembles with a PSMD10:PSMC4:PSMC5:PAAF1 module followed by dissociation of PSMD5. {ECO:0000269|PubMed:19412159, ECO:0000269|PubMed:19490896}.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;atrium;whole body;frontal lobe;endometrium;bone;thyroid;testis;dura mater;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;lacrimal gland;oral cavity;muscle;blood;skeletal muscle;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach; testis; 0.69426 0.13242 -0.201976964 38.98325077 605.54211 4.98093 PSMD5-AS1 . . . PSMD5 antisense RNA 1 (head to head) . . . . . . . . . . . PSMD6 0.962085714874074 0.0378984592866939 1.58258392323443e-05 proteasome 26S subunit, non-ATPase 6 FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.; . . lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;gall bladder;tonsil;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.96157 0.15874 -0.602450568 17.91106393 51.42896 1.41521 PSMD6-AS2 . . . PSMD6 antisense RNA 2 . . . . . . . . . . . PSMD7 0.0193323505913806 0.961568701705436 0.0190989477031833 proteasome 26S subunit, non-ATPase 7 FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.; . . myocardium;lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach; amygdala;whole brain;dorsal root ganglion;subthalamic nucleus;placenta;globus pallidus;caudate nucleus;fetal thyroid;parietal lobe; 0.79861 0.19185 -0.383807564 27.41802312 16.82569 0.59167 PSMD7P1 . . . proteasome 26S subunit, non-ATPase 7 pseudogene 1 . . . . . . . . . . . PSMD8 0.176154540930518 0.810940345605003 0.0129051134644784 proteasome 26S subunit, non-ATPase 8 FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Necessary for activation of the CDC28 kinase.; . . smooth muscle;ovary;skin;retina;prostate;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;adrenal cortex;pharynx;blood;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;cerebral cortex;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; amygdala;whole brain;testis - interstitial;heart;testis - seminiferous tubule;placenta;testis; 0.94051 . -0.361761279 28.6329323 59.1848 1.56033 PSMD8P1 . . . proteasome 26S subunit, non-ATPase, 8 pseudogene 1 . . . . . . . . . . . PSMD9 3.77628232193741e-05 0.377512915453283 0.622449321723498 proteasome 26S subunit, non-ATPase 9 FUNCTION: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex assembly is part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as modulator trimer complex; PSMD9 is released during the further base assembly process. {ECO:0000269|PubMed:19490896}.; . TISSUE SPECIFICITY: Expressed in all tissues tested, highly expressed in liver and kidney.; myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;aorta;stomach;thymus; dorsal root ganglion;superior cervical ganglion;prefrontal cortex;white blood cells;ciliary ganglion;trigeminal ganglion; 0.47748 0.14490 0.483275131 79.25218212 2377.62302 9.04825 PSMD10 0.403603163193442 0.557861228459509 0.0385356083470484 proteasome 26S subunit, non-ATPase 10 FUNCTION: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pahway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis.; . TISSUE SPECIFICITY: Tends to be up-regulated in cancer cells with RAS mutations, including lung cancers and adenocarconimas (at protein level). {ECO:0000269|PubMed:10613832, ECO:0000269|PubMed:20628200}.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; occipital lobe;subthalamic nucleus;hypothalamus;pons;cingulate cortex;parietal lobe; 0.97830 0.12517 -0.09720619 46.20193442 31.2092 0.98478 PSMD10P1 . . . proteasome 26S subunit, non-ATPase, 10 pseudogene 1 . . . . . . . . . . . PSMD10P2 . . . proteasome 26S subunit, non-ATPase, 10 pseudogene 2 . . . . . . . . . . . PSMD10P3 . . . proteasome 26S subunit, non-ATPase, 10 pseudogene 3 . . . . . . . . . . . PSMD11 0.999745808833033 0.000254190790999343 3.75968042057183e-10 proteasome 26S subunit, non-ATPase 11 FUNCTION: Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, PSMD11 is required for proteasome assembly. Plays a key role in increased proteasome activity in embryonic stem cells (ESCs): its high expression in ESCs promotes enhanced assembly of the 26S proteasome, followed by higher proteasome activity. {ECO:0000269|PubMed:22972301}.; . TISSUE SPECIFICITY: Highly expressed in embryonic stem cells (ESCs). Expression decreases as ESCs differentiate. {ECO:0000269|PubMed:22972301}.; myocardium;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;amnion;liver;cervix;spleen;head and neck;kidney;stomach;peripheral nerve;cerebellum; whole brain;medulla oblongata;thalamus;superior cervical ganglion;testis - interstitial;occipital lobe;hypothalamus;pons;caudate nucleus;subthalamic nucleus;testis - seminiferous tubule;fetal brain;prefrontal cortex;globus pallidus;parietal lobe; 0.99338 0.14229 -0.405853867 26.23260203 5.14301 0.19111 PSMD12 0.997267742152841 0.00273223301575805 2.48314007375381e-08 proteasome 26S subunit, non-ATPase 12 FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.; . . medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;gum;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; amygdala;dorsal root ganglion;superior cervical ganglion;occipital lobe;testis - interstitial;cerebellum peduncles;pons;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.95993 0.15588 -0.315847836 31.68789809 22.17927 0.74446 PSMD12P . . . proteasome 26S subunit, non-ATPase, 12 pseudogene . . . . . . . . . . . PSMD13 0.993513212124208 0.00648658275829275 2.05117499385169e-07 proteasome 26S subunit, non-ATPase 13 FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.; . . myocardium;lymphoreticular;medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;salivary gland;intestine;colon;uterus;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;amnion;head and neck;kidney;stomach; superior cervical ganglion;globus pallidus;testis;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.93270 . 1.107875794 92.03821656 53.7399 1.46066 PSMD14 0.790099057421391 0.20856375192313 0.00133719065547889 proteasome 26S subunit, non-ATPase 14 FUNCTION: Metalloprotease component of the 26S proteasome that specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading. {ECO:0000269|PubMed:22909820, ECO:0000269|PubMed:9374539}.; . TISSUE SPECIFICITY: Widely expressed. Highest levels in heart and skeletal muscle. {ECO:0000269|PubMed:9374539}.; . . 0.96651 0.28104 0.013025609 54.62962963 3.66433 0.13578 PSME1 0.0508808333116453 0.927571331249409 0.0215478354389458 proteasome activator subunit 1 FUNCTION: Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome.; . . lymphoreticular;smooth muscle;ovary;umbilical cord;skin;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;thymus; adrenal gland;liver;white blood cells;whole blood; 0.39132 0.11179 0.283038099 71.26680821 19.18514 0.66093 PSME2 0.108796041514697 0.884754819988735 0.00644913849656801 proteasome activator subunit 2 FUNCTION: Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;developmental;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;urinary;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; . 0.83039 0.17270 0.103030231 61.2762444 24.05418 0.79084 PSME2P1 . . . proteasome activator subunit 2 pseudogene 1 . . . . . . . . . . . PSME2P2 . . . proteasome activator subunit 2 pseudogene 2 . . . . . . . . . . . PSME2P3 . . . proteasome activator subunit 2 pseudogene 3 . . . . . . . . . . . PSME2P4 . . . proteasome activator subunit 2 pseudogene 4 . . . . . . . . . . . PSME2P5 . . . proteasome activator subunit 2 pseudogene 5 . . . . . . . . . . . PSME2P6 . . . proteasome activator subunit 2 pseudogene 6 . . . . . . . . . . . PSME3 0.988103823358922 0.0118917047153203 4.4719257577775e-06 proteasome activator subunit 3 FUNCTION: Subunit of the 11S REG-gamma (also called PA28-gamma) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates the trypsin-like catalytic subunit of the proteasome but inhibits the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53 interaction which promotes ubiquitination- and MDM2-dependent proteasomal degradation of p53/TP53, limiting its accumulation and resulting in inhibited apoptosis after DNA damage. May also be involved in cell cycle regulation. Mediates CCAR2 and CHEK2-dependent SIRT1 inhibition (PubMed:25361978). {ECO:0000269|PubMed:10835274, ECO:0000269|PubMed:11185562, ECO:0000269|PubMed:11432824, ECO:0000269|PubMed:15111123, ECO:0000269|PubMed:18309296, ECO:0000269|PubMed:25361978, ECO:0000269|PubMed:9325261}.; . . lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;choroid;uterus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;mesenchyma;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;cerebellum; amygdala;testis - interstitial;superior cervical ganglion;medulla oblongata;cerebellum peduncles;temporal lobe;subthalamic nucleus;testis - seminiferous tubule;testis;ciliary ganglion;kidney;trigeminal ganglion;cerebellum; 0.97581 0.24361 -0.053113545 49.38664779 2.42898 0.08725 PSME4 0.999999996860777 3.13922277635551e-09 5.77777921257196e-27 proteasome activator subunit 4 FUNCTION: Associated component of the proteasome that specifically recognizes acetylated histones and promotes ATP- and ubiquitin- independent degradation of core histones during spermatogenesis and DNA damage response. Recognizes and binds acetylated histones via its bromodomain-like (BRDL) region and activates the proteasome by opening the gated channel for substrate entry. Binds to the core proteasome via its C-terminus, which occupies the same binding sites as the proteasomal ATPases, opening the closed structure of the proteasome via an active gating mechanism. Component of the spermatoproteasome, a form of the proteasome specifically found in testis: binds to acetylated histones and promotes degradation of histones, thereby participating actively to the exchange of histones during spermatogenesis. Also involved in DNA damage response in somatic cells, by promoting degradation of histones following DNA double-strand breaks. {ECO:0000269|PubMed:12093752, ECO:0000269|PubMed:18845680, ECO:0000269|PubMed:22550082, ECO:0000269|PubMed:23706739}.; . . . . 0.73539 0.21928 -1.054560763 7.60202878 4060.31194 12.63567 PSMF1 0.000147581676028268 0.658676832693833 0.341175585630139 proteasome inhibitor subunit 1 FUNCTION: Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28. {ECO:0000269|PubMed:10764772}.; . . medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;amnion;head and neck;kidney;stomach;aorta; testis - interstitial;testis - seminiferous tubule;liver;testis; 0.73878 0.09163 0.418953042 77.06416608 305.30152 3.72089 PSMG1 0.0129744173088997 0.953825634202487 0.0331999484886132 proteasome (prosome, macropain) assembly chaperone 1 FUNCTION: Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization. {ECO:0000269|PubMed:16251969, ECO:0000269|PubMed:17707236}.; . TISSUE SPECIFICITY: In the adult, detected in brain, colon, leukocytes, breast and testis. Widely expressed in the fetus. Also expressed in a variety of proliferating cell lines. {ECO:0000269|PubMed:10872820, ECO:0000269|PubMed:9784380}.; myocardium;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.09671 0.11625 0.439181676 77.69521113 67.45208 1.69994 PSMG2 0.00355676049077914 0.840165604798957 0.156277634710263 proteasome (prosome, macropain) assembly chaperone 2 FUNCTION: Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG1. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization. {ECO:0000269|PubMed:16251969, ECO:0000269|PubMed:17707236}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in lung, brain and colon. Moderately expressed in muscle, stomach, spleen and heart. Weakly expressed in small intestine, pancreas and liver. Highly expressed in hepatocellular carcinomas with low levels in surrounding liver tissue. {ECO:0000269|PubMed:11854909}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.24257 0.10989 0.461228372 78.46190139 124.81121 2.42960 PSMG3 0.194253225381003 0.647463862643659 0.158282911975338 proteasome (prosome, macropain) assembly chaperone 3 FUNCTION: Chaperone protein which promotes assembly of the 20S proteasome. May cooperate with PSMG1-PSMG2 heterodimers to orchestrate the correct assembly of proteasomes. {ECO:0000269|PubMed:17189198}.; . . ovary;colon;parathyroid;fovea centralis;choroid;vein;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;blood;lens;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; thalamus;temporal lobe;tumor;globus pallidus;white blood cells; 0.34797 . 0.125076652 62.7388535 17.49134 0.61361 PSMG3-AS1 . . . PSMG3 antisense RNA 1 (head to head) . . . . . . . . . . . PSMG4 . . . proteasome (prosome, macropain) assembly chaperone 4 FUNCTION: Chaperone protein which promotes assembly of the 20S proteasome.; . . unclassifiable (Anatomical System);prostate;lung;heart;placenta;liver;spleen;brain;stomach; . . . 0.72397987 85.91648974 21.5692 0.72553 PSORS1C1 0.00085535591737133 0.556250844965368 0.442893799117261 psoriasis susceptibility 1 candidate 1 . . TISSUE SPECIFICITY: Expressed in skin. Also found in heart, placenta, liver, skeletal muscle and pancreas. {ECO:0000269|PubMed:12930300}.; uterus;lung;ovary;heart;testis;mammary gland;skin; . 0.09872 . 1.879670682 97.24581269 827.20904 5.63783 PSORS1C2 0.104502852669113 0.774730973681622 0.120766173649265 psoriasis susceptibility 1 candidate 2 . . TISSUE SPECIFICITY: Expressed in skin. Also expressed in heart and skeletal muscle. {ECO:0000269|PubMed:12930300}.; unclassifiable (Anatomical System);heart; . 0.11336 . 1.324743148 94.0905874 1053.17602 6.23125 PSORS1C3 . . . psoriasis susceptibility 1 candidate 3 (non-protein coding) . . . . . 0.06556 . . . . . PSORS3 . . . psoriasis susceptibility 3 . . . . . . . . . . . PSORS4 . . . psoriasis susceptibility 4 . . . . . . . . . . . PSORS5 . . . psoriasis susceptibility 5 . . . . . . . . . . . PSORS6 . . . psoriasis susceptibility 6 . . . . . . . . . . . PSORS7 . . . psoriasis susceptibility 7 . . . . . . . . . . . PSORS8 . . . psoriasis susceptibility 8 . . . . . . . . . . . PSORS9 . . . psoriasis susceptibility 9 . . . . . . . . . . . PSORS10 . . . psoriasis susceptibility 10 . . . . . . . . . . . PSPC1 0.9926070201195 0.0073926974607393 2.82419760527011e-07 paraspeckle component 1 FUNCTION: Regulates, cooperatively with NONO and SFPQ, androgen receptor-mediated gene transcription activity in Sertoli cell line (By similarity). Binds to poly(A), poly(G) and poly(U) RNA homopolymers. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer (By similarity). Together with NONO, required for the formation of nuclear paraspeckles. {ECO:0000250, ECO:0000269|PubMed:22416126}.; . TISSUE SPECIFICITY: Expressed in pancreas, kidney, skeletal muscle, liver, lung, placenta, brain and heart. {ECO:0000269|PubMed:11790299}.; unclassifiable (Anatomical System);lymphoreticular;medulla oblongata;heart;muscle;colon;lens;skin;skeletal muscle;retina;prostate;optic nerve;lung;bone;placenta;visual apparatus;liver;testis;cervix;germinal center;kidney;brain;mammary gland;stomach; superior cervical ganglion;skeletal muscle; 0.15131 0.11430 -0.405853867 26.23260203 58.28959 1.54636 PSPC1P1 . . . paraspeckle component 1 pseudogene 1 . . . . . . . . . . . PSPC1P2 . . . paraspeckle component 1 pseudogene 2 . . . . . . . . . . . PSPH 0.709723367299492 0.286885226936162 0.0033914057643462 phosphoserine phosphatase FUNCTION: Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates. {ECO:0000269|PubMed:12777757}.; DISEASE: Phosphoserine phosphatase deficiency (PSPHD) [MIM:614023]: A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome. {ECO:0000269|PubMed:14673469}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);islets of Langerhans;colon;skin;skeletal muscle;uterus;prostate;whole body;lung;bone;visual apparatus;hippocampus;liver;testis;cervix;spleen;germinal center;kidney;brain;aorta;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; . . 0.415317661 76.81056853 48.29094 1.35472 PSPHP1 . . . phosphoserine phosphatase pseudogene 1 . . TISSUE SPECIFICITY: Highly expressed in FA (Fanconi's anemia) B- cells of complementation group A and Raji cells. Not expressed in B-cells of other FA complementation groups. {ECO:0000269|PubMed:9573387}.; . . . . . . . . PSPN 0.00774141151421535 0.549013588915589 0.443244999570196 persephin FUNCTION: Exhibits neurotrophic activity on mesencephalic dopaminergic and motor neurons.; . . unclassifiable (Anatomical System);lung; pons;skeletal muscle; 0.14522 0.14782 . . 105.01373 2.21656 PSRC1 1.74717788563073e-06 0.661945450501836 0.338052802320279 proline/serine-rich coiled-coil 1 FUNCTION: Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate, and for normal rate of chromosomal segregation during anaphase. Plays a role in the regulation of mitotic spindle dynamics. Increases the rate of turnover of microtubules on metaphase spindles, and contributes to the generation of normal tension across sister kinetochores. Recruits KIF2A to the mitotic spindle and spindle poles. May participate in p53/TP53-regulated growth suppression. {ECO:0000269|PubMed:18411309, ECO:0000269|PubMed:19738423}.; . TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues, with highest expression in the adult brain and fetal thymus. Not detected in adult skeletal muscle. {ECO:0000269|PubMed:12427559}.; . . . 0.08672 0.711016566 85.72776598 144.36618 2.61657 PSTK 0.00411002353042562 0.960308594057246 0.0355813824123287 phosphoseryl-tRNA kinase FUNCTION: Specifically phosphorylates seryl-tRNA(Sec) to O- phosphoseryl-tRNA(Sec), an activated intermediate for selenocysteine biosynthesis. {ECO:0000250}.; . . . . 0.25378 0.09590 0.527368849 80.73248408 . . PSTPIP1 0.000726150105344361 0.980795875695822 0.0184779741988336 proline-serine-threonine phosphatase interacting protein 1 FUNCTION: Involved in regulation of the actin cytoskeleton. May regulate WAS actin-bundling activity. Bridges the interaction between ABL1 and PTPN18 leading to ABL1 dephosphorylation. May play a role as a scaffold protein between PTPN12 and WAS and allow PTPN12 to dephosphorylate WAS. Has the potential to physically couple CD2 and CD2AP to WAS. Acts downstream of CD2 and CD2AP to recruit WAS to the T-cell:APC contact site so as to promote the actin polymerization required for synapse induction during T-cell activation (By similarity). Down-regulates CD2-stimulated adhesion through the coupling of PTPN12 to CD2. Also has a role in innate immunity and the inflammatory response. Recruited to inflammasomes by MEFV. Induces formation of pyroptosomes, large supramolecular structures composed of oligomerized PYCARD dimers which form prior to inflammatory apoptosis. Binding to MEFV allows MEFV to bind to PYCARD and facilitates pyroptosome formation. Regulates endocytosis and cell migration in neutrophils. {ECO:0000250, ECO:0000269|PubMed:17964261, ECO:0000269|PubMed:18480402, ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923, ECO:0000269|PubMed:9857189}.; DISEASE: PAPA syndrome (PAPAS) [MIM:604416]: Characterized by autosomal dominant inheritance of early-onset, primarily affecting skin and joint tissues. Recurring inflammatory episodes lead to accumulation of sterile, pyogenic, neutrophil-rich material within the affected joints, ultimately resulting in significant destruction. {ECO:0000269|PubMed:11971877, ECO:0000269|PubMed:22161697}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in the peripheral blood leukocytes, granulocytes and monocytes, namely in T-cells and natural killer cells, and in spleen. Weakly expressed in the thymus, small intestine, lung and placenta. {ECO:0000269|PubMed:14595024, ECO:0000269|PubMed:9857189}.; unclassifiable (Anatomical System);lymph node;ovary;cartilage;blood;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;optic nerve;lung;endometrium;bone;macula lutea;liver;spleen;germinal center;brain; superior cervical ganglion;white blood cells;whole blood; 0.18907 0.17191 0.312359769 72.71172446 220.82961 3.21350 PSTPIP2 0.107611557288659 0.892114743158107 0.000273699553234439 proline-serine-threonine phosphatase interacting protein 2 FUNCTION: Binds to F-actin. May be involved in regulation of the actin cytoskeleton (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;colon;blood;vein;skin;bone marrow;uterus;endometrium;visual apparatus;alveolus;liver;spleen;kidney;brain; superior cervical ganglion; 0.08446 0.08464 0.060756528 58.52795471 1683.83562 7.56284 PTAFR 0.118775353428594 0.779289831874374 0.101934814697032 platelet activating factor receptor FUNCTION: Receptor for platelet activating factor, a chemotactic phospholipid mediator that possesses potent inflammatory, smooth- muscle contractile and hypotensive activity. Seems to mediate its action via a G protein that activates a phosphatidylinositol- calcium second messenger system. {ECO:0000269|PubMed:1281995, ECO:0000269|PubMed:1374385, ECO:0000269|PubMed:1656963, ECO:0000269|PubMed:1657923}.; . TISSUE SPECIFICITY: Expressed in the placenta, lung, left and right heart ventricles, heart atrium, leukocytes and differentiated HL-60 granulocytes. {ECO:0000269|PubMed:1281995, ECO:0000269|PubMed:1656963, ECO:0000269|PubMed:1657923}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;islets of Langerhans;blood;retina;bone marrow;uterus;lung;adrenal gland;nasopharynx;placenta;testis;germinal center;brain; superior cervical ganglion;trigeminal ganglion; 0.12053 0.24156 0.661468037 84.4420854 263.96257 3.48672 PTAR1 0.73155829105821 0.267885691039082 0.000556017902707458 protein prenyltransferase alpha subunit repeat containing 1 . . . unclassifiable (Anatomical System);visual apparatus;amniotic fluid;germinal center;mammary gland;skin; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skin; 0.23913 . -0.0274281 51.65723048 179.24101 2.90804 PTBP1 0.998739199526157 0.00126078185941441 1.8614428457564e-08 polypyrimidine tract binding protein 1 FUNCTION: Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. Represses the splicing of MAPT/Tau exon 10 (PubMed:15009664). In case of infection by picornaviruses, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation (PubMed:21518806). {ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:16179478, ECO:0000269|PubMed:16260624, ECO:0000269|PubMed:21518792, ECO:0000269|PubMed:21518806}.; . . lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;iris;germinal center;bladder;brain;tonsil;heart;cartilage;blood;lens;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);trophoblast;lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;hypopharynx;duodenum;head and neck;kidney;stomach;thymus; tumor;white blood cells;atrioventricular node;bone marrow;prostate;lung;testis - seminiferous tubule;placenta;thyroid;testis;fetal lung;kidney;trigeminal ganglion;thymus; 0.88766 0.24759 -1.217968826 5.638122199 29.53361 0.94402 PTBP1P . . . polypyrimidine tract binding protein 1 pseudogene . . . . . . . . . . . PTBP2 0.992693429228573 0.0073065152414733 5.55299540916183e-08 polypyrimidine tract binding protein 2 FUNCTION: RNA-binding protein which binds to intronic polypyrimidine tracts and mediates negative regulation of exons splicing. May antagonize in a tissue-specific manner the ability of NOVA1 to activate exon selection. In addition to its function in pre-mRNA splicing, plays also a role in the regulation of translation. Isoform 5 has a reduced affinity for RNA. {ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:12667457}.; . TISSUE SPECIFICITY: Mainly expressed in brain although also detected in other tissues like heart and skeletal muscle. Isoform 1 and isoform 2 are specifically expressed in neuronal tissues. Isoform 3 and isoform 4 are expressed in non-neuronal tissues. Isoform 5 and isoform 6 are truncated forms expressed in non- neuronal tissues. {ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:12213192}.; ovary;sympathetic chain;parathyroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;hypothalamus;pineal body;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;kidney;aorta; amygdala;occipital lobe;testis - interstitial;superior cervical ganglion;hypothalamus;pons;caudate nucleus;uterus;testis - seminiferous tubule;fetal brain;prefrontal cortex;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.84828 0.12378 -0.516085732 21.20193442 6.8231 0.25305 PTBP3 0.978776733356337 0.0212231126680931 1.53975569630188e-07 polypyrimidine tract binding protein 3 FUNCTION: RNA-binding protein that mediates pre-mRNA alternative splicing regulation. Plays a role in the regulation of cell proliferation, differentiation and migration. Positive regulator of EPO-dependent erythropoiesis. Participates in cell differentiation regulation by repressing tissue-specific exons. Promotes FAS exon 6 skipping. Binds RNA, preferentially to both poly(G) and poly(U). {ECO:0000269|PubMed:10207106, ECO:0000269|PubMed:18335065, ECO:0000269|PubMed:19441079, ECO:0000269|PubMed:20937273}.; . TISSUE SPECIFICITY: Expressed in several hematopoietic cell lines examined. {ECO:0000269|PubMed:10207106}.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;bladder;cartilage;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;nasopharynx;placenta;hypopharynx;head and neck;kidney;aorta;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.95978 0.09493 -0.624497208 17.16206653 51.95286 1.42383 PTCD1 1.77777327849927e-09 0.386760912200586 0.613239086021641 pentatricopeptide repeat domain 1 FUNCTION: Mitochondrial protein implicated in negative regulation of leucine tRNA levels, as well as negative regulation of mitochondria-encoded proteins and COX activity. Affects also the 3'-processing of mitochondrial tRNAs. {ECO:0000269|PubMed:21857155}.; . TISSUE SPECIFICITY: Abundant in testes, skeletal muscle and heart. {ECO:0000269|PubMed:19651879}.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;cervix;head and neck;kidney;mammary gland;stomach; superior cervical ganglion; 0.09741 0.11013 0.475790265 78.87473461 . . PTCD2 3.49480168983275e-08 0.325335683834527 0.674664281217456 pentatricopeptide repeat domain 2 FUNCTION: Involved in mitochondrial RNA maturation and mitochondrial respiratory chain function. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymphoreticular;lymph node;heart;islets of Langerhans;colon;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;uterus;optic nerve;lung;bone;macula lutea;hippocampus;testis;germinal center;kidney;brain;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.02760 . -0.648365105 16.35999056 14.78572 0.53278 PTCD2P1 . . . pentatricopeptide repeat domain 2 pseudogene 1 . . . . . . . . . . . PTCD2P2 . . . pentatricopeptide repeat domain 2 pseudogene 2 . . . . . . . . . . . PTCD3 1.02555530600256e-06 0.999326935296503 0.000672039148191502 pentatricopeptide repeat domain 3 FUNCTION: Mitochondrial RNA-binding protein that has a role in mitochondrial translation. {ECO:0000269|PubMed:19427859}.; . TISSUE SPECIFICITY: Abundant in testes, skeletal muscle and heart tissue. {ECO:0000269|PubMed:19427859}.; lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;germinal center;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach;thymus; testis - seminiferous tubule;prefrontal cortex;testis; 0.04896 0.08346 -0.571310997 19.01391838 724.4006 5.34308 PTCH1 0.999998857309533 1.14269046642715e-06 1.45757486268782e-16 patched 1 FUNCTION: Acts as a receptor for sonic hedgehog (SHH), indian hedgehog (IHH) and desert hedgehog (DHH). Associates with the smoothened protein (SMO) to transduce the hedgehog's proteins signal. Seems to have a tumor suppressor function, as inactivation of this protein is probably a necessary, if not sufficient step for tumorigenesis. {ECO:0000269|PubMed:21537345}.; DISEASE: Basal cell nevus syndrome (BCNS) [MIM:109400]: An autosomal dominant disease characterized by nevoid basal cell carcinomas and developmental abnormalities such as rib and craniofacial alterations, polydactyly, syndactyly, and spina bifida. In addition, the patients suffer from a multitude of tumors like basal cell carcinomas, fibromas of the ovaries and heart, cysts of the skin, jaws and mesentery, as well as medulloblastomas and meningiomas. {ECO:0000269|PubMed:11231326, ECO:0000269|PubMed:15459969, ECO:0000269|PubMed:8840969, ECO:0000269|PubMed:8981943, ECO:0000269|PubMed:9620294}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Basal cell carcinoma (BCC) [MIM:605462]: A common malignant skin neoplasm that typically appears on hair-bearing skin, most commonly on sun-exposed areas. BCC is slow growing and rarely metastasizes, but has potentialities for local invasion and destruction. It usually develops as a flat, firm, pale area that is small, raised, pink or red, translucent, shiny, and waxy, and the area may bleed following minor injury. Tumor size can vary from a few millimeters to several centimeters in diameter. {ECO:0000269|PubMed:8658145, ECO:0000269|PubMed:9620294}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Holoprosencephaly 7 (HPE7) [MIM:610828]: A structural anomaly of the brain, in which the developing forebrain fails to correctly separate into right and left hemispheres. Holoprosencephaly is genetically heterogeneous and associated with several distinct facies and phenotypic variability. {ECO:0000269|PubMed:11941477, ECO:0000269|PubMed:17001668, ECO:0000269|PubMed:17096318}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In the adult, expressed in brain, lung, liver, heart, placenta, skeletal muscle, pancreas and kidney. Expressed in tumor cells but not in normal skin.; ovary;colon;skin;uterus;prostate;whole body;endometrium;cochlea;testis;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;tongue;islets of Langerhans;pharynx;lens;skeletal muscle;lung;placenta;hippocampus;duodenum;kidney; dorsal root ganglion;superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.54020 0.78677 -2.730960138 0.707714084 6145.45731 16.38112 PTCH2 6.1101240485129e-10 0.956738167648157 0.0432618317408304 patched 2 FUNCTION: May have a role in epidermal development. May act as a receptor for Sonic hedgehog (SHH).; DISEASE: Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. {ECO:0000269|PubMed:9931336}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Basal cell carcinoma (BCC) [MIM:605462]: A common malignant skin neoplasm that typically appears on hair-bearing skin, most commonly on sun-exposed areas. BCC is slow growing and rarely metastasizes, but has potentialities for local invasion and destruction. It usually develops as a flat, firm, pale area that is small, raised, pink or red, translucent, shiny, and waxy, and the area may bleed following minor injury. Tumor size can vary from a few millimeters to several centimeters in diameter. {ECO:0000269|PubMed:9931336}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.68495 0.19766 -1.517642441 3.467799009 494.343 4.57158 PTCHD1 0.947053078709569 0.0527677620961688 0.000179159194262459 patched domain containing 1 . . TISSUE SPECIFICITY: Widely expressed, including in various regions of the brain with highest expression in the gray and white cerebellum, followed by the cerebellar vermis and the pituitary gland. {ECO:0000269|PubMed:20844286}.; . . 0.53174 0.11439 -1.001120478 8.321538099 18.27813 0.63515 PTCHD1-AS . . . PTCHD1 antisense RNA (head to head) . . . . . . . . . . . PTCHD3 6.38190348669616e-11 0.0647100414101764 0.935289958526004 patched domain containing 3 FUNCTION: May play a role in sperm development or sperm function. {ECO:0000269|PubMed:17904097}.; . TISSUE SPECIFICITY: Expressed in germ cells of the testis (at protein level). {ECO:0000269|PubMed:17904097}.; . . 0.08160 0.11960 3.16435382 99.30997877 5927.22826 15.99359 PTCHD3P1 . . . patched domain containing 3 pseudogene 1 . . . . . . . . . . . PTCHD3P2 . . . patched domain containing 3 pseudogene 2 . . . . . . . . . . . PTCHD3P3 . . . patched domain containing 3 pseudogene 3 . . . . . . . . . . . PTCHD4 0.00276059838903919 0.983719779778393 0.013519621832568 patched domain containing 4 . . . . . 0.76784 . -0.707227564 14.71455532 97.49459 2.13448 PTCRA 0.0113951526484819 0.842493630782548 0.14611121656897 pre T-cell antigen receptor alpha FUNCTION: The pre-T-cell receptor complex (composed of PTCRA, TCRB and the CD3 complex) regulates early T-cell development. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in immature but not mature T-cells. Also found in CD34+ cells from peripheral blood, CD34+ precursors from umbilical cord blood and adult bone marrow. {ECO:0000269|PubMed:8618853, ECO:0000269|PubMed:8760805}.; unclassifiable (Anatomical System);alveolus;spleen;kidney; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17443 0.19181 1.082196027 91.79641425 2800.35213 9.99068 PTCSC1 . . . papillary thyroid carcinoma susceptibility candidate 1 (non-protein coding) . . . . . . . . . . . PTCSC2 . . . papillary thyroid carcinoma susceptibility candidate 2 (non-protein coding) . . . . . . . . . . . PTCSC3 . . . papillary thyroid carcinoma susceptibility candidate 3 (non-protein coding) . . . . . . . . . . . PTDSS1 0.857749191896846 0.142246931834879 3.87626827541444e-06 phosphatidylserine synthase 1 FUNCTION: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. In membranes, PTDSS1 catalyzes mainly the conversion of phosphatidylcholine. Also converts, in vitro and to a lesser extent, phosphatidylethanolamine.; DISEASE: Lenz-Majewski hyperostotic dwarfism (LMHD) [MIM:151050]: A syndrome of intellectual disability and multiple congenital anomalies that features generalized craniotubular hyperostosis. LMHD is characterized by the combination of sclerosing bone dysplasia, intellectual disability and distinct craniofacial, dental, cutaneous and distal limb anomalies. The progressive generalized hyperostosis associated with this syndrome affects the cranium, the vertebrae and the diaphyses of tubular bones, leading to severe growth restriction. {ECO:0000269|PubMed:24241535}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;superior cervical ganglion;globus pallidus;trigeminal ganglion;bone marrow;cerebellum; 0.26928 0.12774 -0.359940251 28.93371078 145.442 2.62713 PTDSS2 0.000109482996794452 0.988232643047095 0.0116578739561105 phosphatidylserine synthase 2 FUNCTION: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. PTDSS2 is specific for phosphatatidylethanolamine and does not act on phosphatidylcholine.; . . medulla oblongata;smooth muscle;ovary;salivary gland;colon;parathyroid;skin;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;urinary;lens;breast;pancreas;lung;placenta;visual apparatus;duodenum;kidney;stomach; testis; 0.17051 0.10256 -0.201976964 38.98325077 959.51491 5.99801 PTEN 0.975506865848027 0.0244877796497562 5.35450221699976e-06 phosphatase and tensin homolog FUNCTION: Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine- phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3- phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K- AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement.; DISEASE: Cowden syndrome 1 (CWS1) [MIM:158350]: An autosomal dominant hamartomatous polyposis syndrome with age-related penetrance. Cowden syndrome is characterized by hamartomatous lesions affecting derivatives of ectodermal, mesodermal and endodermal layers, macrocephaly, facial trichilemmomas (benign tumors of the hair follicle infundibulum), acral keratoses, papillomatous papules, and elevated risk for development of several types of malignancy, particularly breast carcinoma in women and thyroid carcinoma in both men and women. Colon cancer and renal cell carcinoma have also been reported. Hamartomas can be found in virtually every organ, but most commonly in the skin, gastrointestinal tract, breast and thyroid. {ECO:0000269|PubMed:10051160, ECO:0000269|PubMed:10234502, ECO:0000269|PubMed:11494117, ECO:0000269|PubMed:9140396, ECO:0000269|PubMed:9259288, ECO:0000269|PubMed:9345101, ECO:0000269|PubMed:9399897, ECO:0000269|PubMed:9425889, ECO:0000269|PubMed:9600246, ECO:0000269|PubMed:9735393, ECO:0000269|PubMed:9797362, ECO:0000269|PubMed:9832031, ECO:0000269|PubMed:9915974}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Lhermitte-Duclos disease (LDD) [MIM:158350]: A rare disease characterized by the occurrence of a slowly enlarging mass within the cerebellar cortex corresponding histologically to a cerebellar hamartoma. It manifests, most commonly in the third and fourth decades of life, with increased intracranial pressure, headache, nausea, cerebellar dysfunction, occlusive hydrocephalus, ataxia, visual disturbances and other cranial nerve palsies. Various associated abnormalities may be present such as megalencephaly, microgyria, hydromyelia, polydactyly, partial gigantism, macroglossia. LDD is part of the PTEN hamartoma tumor syndromes spectrum that also includes Cowden syndrome. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bannayan-Riley-Ruvalcaba syndrome (BRRS) [MIM:153480]: A rare hamartomatous disorder characterized by macrocephaly and multiple hemangiomas as well as subcutaneous and visceral lipomas. It belongs to the family of hamartomatous polyposis syndromes that includes Peutz Jeghers syndrome, juvenile polyposis, and Cowden syndrome. {ECO:0000269|PubMed:10400993, ECO:0000269|PubMed:11494117, ECO:0000269|PubMed:9241266, ECO:0000269|PubMed:9467011}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Squamous cell carcinoma of the head and neck (HNSCC) [MIM:275355]: A non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes. {ECO:0000269|PubMed:11801303}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of endometrium, the mucous lining of the uterus. Most endometrial cancers are adenocarcinomas, cancers that begin in cells that make and release mucus and other fluids. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=PTEN mutations are found in a subset of patients with Proteus syndrome, a genetically heterogeneous condition. The molecular diagnosis of PTEN mutation positive cases classifies Proteus syndrome patients as part of the PTEN hamartoma syndrome spectrum. As such, patients surviving the early years of Proteus syndrome are likely at a greater risk of developing malignancies.; DISEASE: Glioma 2 (GLM2) [MIM:613028]: Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: VACTERL association with hydrocephalus (VACTERL-H) [MIM:276950]: VACTERL is an acronym for vertebral anomalies, anal atresia, congenital cardiac disease, tracheoesophageal fistula, renal anomalies, radial dysplasia, and other limb defects. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Prostate cancer (PC) [MIM:176807]: A malignancy originating in tissues of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma. {ECO:0000269|PubMed:9072974}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Macrocephaly/autism syndrome (MCEPHAS) [MIM:605309]: Patients have autism spectrum disorders and macrocephaly, with head circumferences ranging from +2.5 to +8 SD for age and sex (average head circumference +4.0 SD). {ECO:0000269|PubMed:15805158}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A microdeletion of chromosome 10q23 involving BMPR1A and PTEN is a cause of chromosome 10q23 deletion syndrome, which shows overlapping features of the following three disorders: Bannayan-Zonana syndrome, Cowden disease and juvenile polyposis syndrome.; TISSUE SPECIFICITY: Expressed at a relatively high level in all adult tissues, including heart, brain, placenta, lung, liver, muscle, kidney and pancreas. {ECO:0000269|PubMed:9090379}.; . . 0.21037 0.94603 -0.229483771 36.86010852 3.61036 0.13188 PTENP1 . . . phosphatase and tensin homolog pseudogene 1 FUNCTION: Plays a role as a potent and selective agonist of PTH2R resulting in adenyl cyclase activation and intracellular calcium levels elevation. Induces protein kinase C beta activation, recruitment of beta-arrestin and PTH2R internalization. May inhibit cell proliferation via its action on PTH2R activation. Neuropeptide which may also have a role in spermatogenesis. May activate nociceptors and nociceptive circuits. {ECO:0000269|PubMed:11861531, ECO:0000269|PubMed:12559132, ECO:0000269|PubMed:12754053, ECO:0000269|PubMed:14988434}.; . TISSUE SPECIFICITY: Highly expressed in fetal and adult brain, cerebellum and trachea. Weakly expressed in spinal cord, fetal liver, kidney and heart. {ECO:0000269|PubMed:12098667}.; . . 0.14996 0.94603 0.635788962 83.63411182 . . PTENP1-AS . . . PTENP1 antisense RNA . . . . . . . . . . . PTER 2.38597256347762e-10 0.0200564277369114 0.979943572024491 phosphotriesterase related . . . ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;cerebellum cortex;blood;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;liver;head and neck;cervix;kidney;mammary gland;stomach; kidney;atrioventricular node;skin; 0.13381 0.81046 0.196671391 67.19155461 147.13198 2.64301 PTF1A . . . pancreas specific transcription factor, 1a FUNCTION: Transcription factor implicated in the cell fate determination in various organs. Binds to the E-box consensus sequence 5'-CANNTG-3'. Plays a role in early and late pancreas development and differentiation. Important for determining whether cells allocated to the pancreatic buds continue towards pancreatic organogenesis or revert back to duodenal fates. May be involved in the maintenance of exocrine pancreas-specific gene expression including ELA1 and amylase. Required for the formation of pancreatic acinar and ductal cells. Plays an important role in cerebellar development. Directly regulated by FOXN4 and RORC during retinal development, FOXN4-PTF1A pathway plays a central role in directing the differentiation of retinal progenitors towards horizontal and amacrine fates. {ECO:0000269|PubMed:10768861, ECO:0000269|PubMed:15543146}.; DISEASE: Pancreatic agenesis 2 (PAGEN2) [MIM:615935]: A disease characterized by isolated hypoplasia or agenesis of the pancreas, pancreatic beta-cell failure resulting in neonatal insulin- dependent diabetes mellitus, and exocrine pancreatic insufficiency. {ECO:0000269|PubMed:24212882}. Note=The disease is caused by mutations affecting the gene represented in this entry. In some families with pancreatic agenesis, disease causing mutations affect the sequence and activity of an enhancer region of 400-bp located 25 kb downstream of PTF1A (PubMed:24212882). {ECO:0000269|PubMed:24212882}.; TISSUE SPECIFICITY: Pancreas-specific (at protein level). Loss of expression is seen in ductal type pancreas cancers. {ECO:0000269|PubMed:10768861}.; . . 0.19266 . . . 96.69148 2.12505 PTGDR 4.02092917428872e-05 0.388808516841608 0.611151273866649 prostaglandin D2 receptor (DP) FUNCTION: Receptor for prostaglandin D2 (PGD2). The activity of this receptor is mainly mediated by G(s) proteins that stimulate adenylate cyclase, resulting in an elevation of intracellular cAMP. A mobilization of calcium is also observed, but without formation of inositol 1,4,5-trisphosphate (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in retinal choroid, ciliary epithelium, longitudinal and circular ciliary muscles, iris, small intestine and platelet membranes. {ECO:0000269|PubMed:11082108, ECO:0000269|PubMed:6302737}.; liver;colon;brain; superior cervical ganglion;skeletal muscle; 0.13242 0.23869 1.15197334 92.52182118 208.36817 3.11549 PTGDR2 0.184110369283718 0.64592532602258 0.169964304693702 prostaglandin D2 receptor 2 FUNCTION: Receptor for prostaglandin D2 (PGD2). Coupled to the G(i)-protein. Receptor activation may result in pertussis toxin- sensitive decreases in cAMP levels and Ca(2+) mobilization. PI3K signaling is also implicated in mediating PTGDR2 effects. PGD2 induced receptor internalization. CRTH2 internalization can be regulated by diverse kinases such as, PKC, PKA, ADRBK1/GRK2, GPRK5/GRK5 and GRK6. Receptor activation is responsible, at least in part, in immune regulation and allergic/inflammation responses. {ECO:0000269|PubMed:11208866, ECO:0000269|PubMed:11535533, ECO:0000269|PubMed:17196174}.; . TISSUE SPECIFICITY: Widespread expression. High expression in stomach, small intestine, heart and thymus. Intermediate expression in colon, spinal cord and peripheral blood and low expression in brain, skeletal muscle and spleen. Expressed also on Th2- and Tc2- type cells, eosinophils and basophils. {ECO:0000269|PubMed:11168006, ECO:0000269|PubMed:11208866, ECO:0000269|PubMed:12466225, ECO:0000269|PubMed:9973380}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.10628 0.19677 . . 165.3637 2.81279 PTGDS 0.00887038851736075 0.936341482528596 0.0547881289540435 prostaglandin D2 synthase FUNCTION: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophopic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system. {ECO:0000269|PubMed:20667974, ECO:0000269|PubMed:9475419}.; . TISSUE SPECIFICITY: Abundant in the brain and CNS, where it is expressed in tissues of the blood-brain barrier and secreted into the cerebro-spinal fluid. Abundantly expressed in the heart. In the male reproductive system, it is expressed in the testis, epididymis and prostate, and is secreted into the seminal fluid. Expressed in the eye and secreted into the aqueous humor. Lower levels detected in various tissue fluids such as serum, normal urine, ascitic fluid and tear fluid. Also found in a number of other organs including ovary, fimbriae of the fallopian tubes, kidney, leukocytes. {ECO:0000269|PubMed:10462696, ECO:0000269|PubMed:11882588, ECO:0000269|PubMed:7692978, ECO:0000269|PubMed:8599604, ECO:0000269|PubMed:8761996, ECO:0000269|PubMed:9065498, ECO:0000269|PubMed:9405674, ECO:0000269|PubMed:9475419, ECO:0000269|PubMed:9844724}.; myocardium;medulla oblongata;sympathetic chain;choroid;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;cerebral cortex;bone;iris;testis;ciliary body;brain;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;hypothalamus;pineal body;spinal cord;lens;pancreas;lung;epididymis;placenta;hippocampus;visual apparatus;spleen;kidney;peripheral nerve;cerebellum; superior cervical ganglion;testis - interstitial;testis;atrioventricular node;trigeminal ganglion; 0.11100 0.09797 -0.141298762 42.87567823 17.99728 0.62847 PTGER1 0.255749329233531 0.640414479158652 0.103836191607817 prostaglandin E receptor 1 FUNCTION: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(q) proteins which activate a phosphatidylinositol-calcium second messenger system. May play a role as an important modulator of renal function. Implicated the smooth muscle contractile response to PGE2 in various tissues.; . TISSUE SPECIFICITY: Abundant in kidney. Lower level expression in lung, skeletal muscle and spleen, lowest expression in testis and not detected in liver brain and heart.; unclassifiable (Anatomical System);lung;islets of Langerhans;visual apparatus;testis;colon;kidney;stomach; superior cervical ganglion;ciliary ganglion;kidney;trigeminal ganglion;skeletal muscle;parietal lobe; 0.01963 . . . 692.19279 5.24689 PTGER2 0.105022888329559 0.863386532567052 0.0315905791033897 prostaglandin E receptor 2 FUNCTION: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. The subsequent raise in intracellular cAMP is responsible for the relaxing effect of this receptor on smooth muscle.; . TISSUE SPECIFICITY: Placenta and lung.; unclassifiable (Anatomical System);heart;cartilage;blood;skin;bone marrow;bile duct;uterus;lung;visual apparatus;liver;kidney;stomach; pons;trigeminal ganglion; 0.09331 0.17677 -0.159704656 41.90846898 40.90294 1.19803 PTGER3 0.787642828876607 0.210975835730959 0.00138133539243424 prostaglandin E receptor 3 FUNCTION: Receptor for prostaglandin E2 (PGE2); the EP3 receptor may be involved in inhibition of gastric acid secretion, modulation of neurotransmitter release in central and peripheral neurons, inhibition of sodium and water reabsorption in kidney tubulus and contraction in uterine smooth muscle. The activity of this receptor can couple to both the inhibition of adenylate cyclase mediated by G-I proteins, and to an elevation of intracellular calcium. The various isoforms have identical ligand binding properties but can interact with different second messenger systems (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in small intestine, heart, pancreas, gastric fundic mucosa, mammary artery and pulmonary vessels. {ECO:0000269|PubMed:18023986}.; unclassifiable (Anatomical System);uterus;prostate;heart;cornea;testis;colon;head and neck;kidney;mammary gland;skin;skeletal muscle;stomach; superior cervical ganglion;adipose tissue;temporal lobe;atrioventricular node;pons;skeletal muscle;skin;uterus;testis - seminiferous tubule;appendix;ciliary ganglion;kidney;trigeminal ganglion; 0.32291 0.24187 0.128714042 63.19886766 53.0037 1.44545 PTGER4 0.896912956538018 0.102887688059149 0.000199355402832241 prostaglandin E receptor 4 FUNCTION: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. Has a relaxing effect on smooth muscle. May play an important role in regulating renal hemodynamics, intestinal epithelial transport, adrenal aldosterone secretion, and uterine function.; . TISSUE SPECIFICITY: High in intestine and in peripheral blood mononuclear cells; low in lung, kidney, thymus, uterus, vasculature and brain. Not found in liver, heart, retina oe skeletal muscle.; smooth muscle;ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;whole body;thyroid;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;blood;pia mater;lung;adrenal gland;placenta;liver;alveolus;kidney;stomach;thymus; pons;trigeminal ganglion;whole blood;skeletal muscle;cingulate cortex; 0.14036 . -0.404032746 26.53338051 31.85447 1.00237 PTGER4P1 . . . prostaglandin E receptor 4 pseudogene 1 . . . . . . . . . . . PTGER4P2 . . . prostaglandin E receptor 4 pseudogene 2 . . . . . . . . . . . PTGER4P2-CDK2AP2P2 . . . PTGER4P2-CDK2AP2P2 readthrough, transcribed pseudogene . . . . . . . . . . . PTGER4P3 . . . prostaglandin E receptor 4 pseudogene 3 . . . . . . . . . . . PTGES 0.624659346812814 0.344008450213196 0.0313322029739891 prostaglandin E synthase FUNCTION: Catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). {ECO:0000269|PubMed:18682561}.; . . unclassifiable (Anatomical System);heart;tongue;colon;skin;breast;uterus;pancreas;prostate;optic nerve;lung;cerebral cortex;endometrium;bone;placenta;head and neck;spleen;cervix;brain;mammary gland;bladder;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12421 0.33694 0.371224249 75.12384996 48.12052 1.35109 PTGES2 2.07241974496747e-05 0.714577908279099 0.285401367523452 prostaglandin E synthase 2 FUNCTION: Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2). {ECO:0000269|PubMed:12804604, ECO:0000269|PubMed:18198127}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in the heart, including apex, inter-ventricular septum, both atria and ventricles, but not in the aorta. Also expressed in fetal heart. Detected in various regions of the brain: cerebellum; occipital, frontal and parietal lobes. Also expressed in the lymph nodes, skeletal muscle, kidney and trachea, but not in the thymus or lung. Overexpressed in colorectal cancer. {ECO:0000269|PubMed:11866447}.; medulla oblongata;ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;placenta;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; whole brain;subthalamic nucleus;heart;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.13661 0.35880 0.17280645 65.75843359 523.91409 4.66938 PTGES2-AS1 . . . PTGES2 antisense RNA 1 (head to head) . . . . . . . . . . . PTGES3 0.871365849855667 0.128278537812585 0.000355612331748242 prostaglandin E synthase 3 FUNCTION: Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) (PubMed:10922363). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes (PubMed:11274138, PubMed:12077419). Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway (PubMed:24711448). {ECO:0000269|PubMed:10922363, ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:12077419, ECO:0000269|PubMed:24711448}.; . . lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;larynx;bone;testis;dura mater;spinal ganglion;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;pia mater;lung;cornea;adrenal gland;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;nose;stomach;aorta; amygdala;testis; 0.96620 0.28104 0.191216164 66.57230479 30.97993 0.97977 PTGES3L 0.0247440738776789 0.779178249074335 0.196077677047986 prostaglandin E synthase 3 (cytosolic)-like . . . . . . . . . 327.16293 3.84559 PTGES3L-AARSD1 2.56865193172703e-08 0.711192620677244 0.288807353636236 PTGES3L-AARSD1 readthrough FUNCTION: Functions in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala). {ECO:0000250}.; . . . . 0.15995 . . . 3016.49921 10.43106 PTGES3P1 . . . prostaglandin E synthase 3 (cytosolic) pseudogene 1 . . . . . . . . . . . PTGES3P2 . . . prostaglandin E synthase 3 (cytosolic) pseudogene 2 . . . . . . . . . . . PTGES3P3 . . . prostaglandin E synthase 3 (cytosolic) pseudogene 3 . . . . . . . . . . . PTGES3P4 . . . prostaglandin E synthase 3 (cytosolic) pseudogene 4 . . . . . . . . . . . PTGES3P5 . . . prostaglandin E synthase 3 (cytosolic) pseudogene 5 . . . . . . . . . . . PTGFR 0.760040674562793 0.238009095833548 0.0019502296036587 prostaglandin F receptor FUNCTION: Receptor for prostaglandin F2-alpha (PGF2-alpha). The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. Initiates luteolysis in the corpus luteum (By similarity). Isoforms 2 to 7 do not bind PGF2-alpha but are proposed to modulate signaling by participating in variant receptor complexes; heterodimers between isoform 1 and isoform 5 are proposed to be a receptor for prostamides including the synthetic analog bimatoprost. {ECO:0000250, ECO:0000269|PubMed:18587449}.; . TISSUE SPECIFICITY: Eye. {ECO:0000269|PubMed:18587449}.; . . 0.36718 0.19921 0.284856336 71.40835103 104.34598 2.20806 PTGFRN 0.6388592328477 0.361129184417152 1.15827351479566e-05 prostaglandin F2 receptor inhibitor FUNCTION: Inhibits the binding of prostaglandin F2-alpha (PGF2- alpha) to its specific FP receptor, by decreasing the receptor number rather than the affinity constant. Functional coupling with the prostaglandin F2-alpha receptor seems to occur (By similarity). {ECO:0000250}.; . . . . 0.29268 0.16012 -0.24061166 36.28214201 4444.58555 13.36118 PTGIR 0.00136020164797244 0.657148653311377 0.341491145040651 prostaglandin I2 (prostacyclin) receptor (IP) FUNCTION: Receptor for prostacyclin (prostaglandin I2 or PGI2). The activity of this receptor is mediated by G(s) proteins which activate adenylate cyclase.; . . unclassifiable (Anatomical System);ovary;cartilage;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;placenta;macula lutea;testis;spleen; atrioventricular node;trigeminal ganglion; 0.16048 0.22469 . . 374.53887 4.08117 PTGIS 2.42325399858621e-05 0.91559389773133 0.0843818697286842 prostaglandin I2 (prostacyclin) synthase FUNCTION: Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2).; . TISSUE SPECIFICITY: Widely expressed; particularly abundant in ovary, heart, skeletal muscle, lung and prostate.; unclassifiable (Anatomical System);cartilage;ovary;colon;parathyroid;skeletal muscle;uterus;breast;pancreas;prostate;lung;bone;placenta;thyroid;visual apparatus;hypopharynx;testis;head and neck;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.36541 0.27749 -0.352661697 29.48808681 184.44683 2.94813 PTGR1 0.0442771156840298 0.929295384928337 0.0264274993876337 prostaglandin reductase 1 FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity towards PGE1, PGE2 and PGE2-alpha (By similarity). Catalyzes the conversion of leukotriene B4 into its biologically less active metabolite, 12-oxo-leukotriene B4. This is an initial and key step of metabolic inactivation of leukotriene B4. {ECO:0000250}.; . TISSUE SPECIFICITY: High expression in the kidney, liver, and intestine but not in leukocytes. {ECO:0000269|PubMed:8576264}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;testis;brain;gall bladder;unclassifiable (Anatomical System);heart;muscle;pharynx;blood;lens;skeletal muscle;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.08999 0.09890 0.106667882 61.73036093 70.21342 1.74020 PTGR2 7.20253305877724e-07 0.471622242851422 0.528377036895272 prostaglandin reductase 2 FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto- PGE2-alpha with highest activity towards 15-keto-PGE2. Overexpression represses transcriptional activity of PPARG and inhibits adipocyte differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:19000823}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15004468}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;hypothalamus;skeletal muscle;uterus;pancreas;whole body;lung;larynx;bone;liver;testis;head and neck;kidney;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.16841 0.11143 -0.161524709 41.6430762 38.21322 1.13499 PTGS1 6.4126306324781e-06 0.97297114656351 0.0270224408058573 prostaglandin-endoperoxide synthase 1 (prostaglandin G/H synthase and cyclooxygenase) FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;testis;germinal center;brain;pineal gland;tonsil;gall bladder;unclassifiable (Anatomical System);cartilage;heart;nervous;tongue;spinal cord;muscle;lens;skeletal muscle;pancreas;lung;adrenal gland;mesenchyma;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;smooth muscle;heart;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17138 0.48780 0.868987491 88.84760557 550.09831 4.77010 PTGS2 0.999033115984394 0.000966874268216037 9.7473902254036e-09 prostaglandin-endoperoxide synthase 2 FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Constitutively expressed in some tissues in physiological conditions, such as the endothelium, kidney and brain, and in pathological conditions, such as in cancer. PTGS2 is responsible for production of inflammatory prostaglandins. Up-regulation of PTGS2 is also associated with increased cell adhesion, phenotypic changes, resistance to apoptosis and tumor angiogenesis. In cancer cells, PTGS2 is a key step in the production of prostaglandin E2 (PGE2), which plays important roles in modulating motility, proliferation and resistance to apoptosis. {ECO:0000269|PubMed:16373578}.; . . . . 0.81176 0.94573 -0.359940251 28.93371078 119.93994 2.38630 PTH 0.270149119024624 0.63561219686482 0.0942386841105556 parathyroid hormone FUNCTION: PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Stimulates [1-14C]-2- deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells. {ECO:0000269|PubMed:21076856}.; DISEASE: Hypoparathyroidism, familial isolated (FIH) [MIM:146200]: A disorder characterized by hypocalcemia and hyperphosphatemia due to inadequate secretion of parathyroid hormone. Clinical features include seizures, tetany and cramps. {ECO:0000269|PubMed:10523031, ECO:0000269|PubMed:2212001}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . whole body;ovary;placenta;parathyroid; superior cervical ganglion;thyroid;fetal thyroid; 0.14367 0.95422 -0.075159878 47.78839349 2.4877 0.09133 PTH1R 0.742389488872585 0.257590250698223 2.02604291916912e-05 parathyroid hormone 1 receptor FUNCTION: This is a receptor for parathyroid hormone and for parathyroid hormone-related peptide. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase and also a phosphatidylinositol-calcium second messenger system. {ECO:0000269|PubMed:18611381, ECO:0000269|PubMed:20172855}.; DISEASE: Chondrodysplasia Blomstrand type (BOCD) [MIM:215045]: Severe skeletal dysplasia. {ECO:0000269|PubMed:9745456}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Enchondromatosis multiple (ENCHOM) [MIM:166000]: A condition characterized by multiple formation of enchondromas, benign neoplasms derived from mesodermal cells that form cartilage. Enchondromas remain within the substance of a cartilage or bone. Clinical problems caused by enchondromas include skeletal deformity and the potential for malignant change to osteosarcoma. {ECO:0000269|PubMed:11850620}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Eiken skeletal dysplasia (EISD) [MIM:600002]: A rare skeletal dysplasia characterized by severely retarded ossification, principally of the epiphyses, pelvis, hands and feet, as well as by abnormal modeling of the bones in hands and feet, abnormal persistence of cartilage in the pelvis and mild growth retardation. {ECO:0000269|PubMed:15525660}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Primary failure of tooth eruption (PFE) [MIM:125350]: Rare condition that has high penetrance and variable expressivity and in which tooth retention occurs without evidence of any obvious mechanical interference. Instead, malfunction of the eruptive mechanism itself appears to cause nonankylosed permanent teeth to fail to erupt, although the eruption pathway has been cleared by bone resorption. {ECO:0000269|PubMed:19061984}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in most tissues. Most abundant in kidney, bone and liver.; unclassifiable (Anatomical System);heart;cartilage;colon;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;whole body;lung;placenta;bone;macula lutea;visual apparatus;liver;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;kidney;atrioventricular node;skeletal muscle; 0.46022 . 0.066214104 58.95848077 98.9665 2.15303 PTH2 0.522952191907171 0.413675744818935 0.0633720632738943 parathyroid hormone 2 FUNCTION: Plays a role as a potent and selective agonist of PTH2R resulting in adenyl cyclase activation and intracellular calcium levels elevation. Induces protein kinase C beta activation, recruitment of beta-arrestin and PTH2R internalization. May inhibit cell proliferation via its action on PTH2R activation. Neuropeptide which may also have a role in spermatogenesis. May activate nociceptors and nociceptive circuits. {ECO:0000269|PubMed:11861531, ECO:0000269|PubMed:12559132, ECO:0000269|PubMed:12754053, ECO:0000269|PubMed:14988434}.; . TISSUE SPECIFICITY: Highly expressed in fetal and adult brain, cerebellum and trachea. Weakly expressed in spinal cord, fetal liver, kidney and heart. {ECO:0000269|PubMed:12098667}.; . . 0.14996 0.13539 0.635788962 83.63411182 76.35716 1.83199 PTH2R 1.3161518374435e-15 0.0112978100132928 0.988702189986706 parathyroid hormone 2 receptor FUNCTION: This is a specific receptor for parathyroid hormone. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. PTH2R may be responsible for PTH effects in a number of physiological systems. It may play a significant role in pancreatic function. PTH2R presence in neurons indicates that it may function as a neurotransmitter receptor (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed abundantly in brain and pancreas. Also expressed in the testis. {ECO:0000269|PubMed:7797535}.; unclassifiable (Anatomical System);lymphoreticular;lung;macula lutea;fovea centralis;skin; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.18266 0.17802 -0.664951379 15.91177164 215.52876 3.16905 PTHLH 0.921296517827875 0.0782172996805235 0.000486182491601128 parathyroid hormone-like hormone FUNCTION: Neuroendocrine peptide which is a critical regulator of cellular and organ growth, development, migration, differentiation and survival and of epithelial calcium ion transport. Regulates endochondral bone development and epithelial-mesenchymal interactions during the formation of the mammary glands and teeth. Required for skeletal homeostasis. Promotes mammary mesenchyme differentiation and bud outgrowth by modulating mesenchymal cell responsiveness to BMPs. Upregulates BMPR1A expression in the mammary mesenchyme and this increases the sensitivity of these cells to BMPs and allows them to respond to BMP4 in a paracrine and/or autocrine fashion. BMP4 signaling in the mesenchyme, in turn, triggers epithelial outgrowth and augments MSX2 expression, which causes the mammary mesenchyme to inhibit hair follicle formation within the nipple sheath (By similarity). Promotes colon cancer cell migration and invasion in an integrin alpha-6/beta-1- dependent manner through activation of Rac1. {ECO:0000250, ECO:0000269|PubMed:20637541}.; DISEASE: Brachydactyly E2 (BDE2) [MIM:613382]: A form of brachydactyly. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. Brachydactyly type E is characterized by shortening of the fingers mainly in the metacarpals and metatarsals. Wide variability in the number of digits affected occurs from person to person, even in the same family. Some individuals are moderately short of stature. In brachydactyly type E2 variable combinations of metacarpals are involved, with shortening also of the first and third distal and the second and fifth middle phalanges. {ECO:0000269|PubMed:20170896}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Also expressed in the mammary gland.; ovary;islets of Langerhans;colon;parathyroid;skin;breast;prostate;pancreas;lung;larynx;gum;placenta;thyroid;testis;head and neck;kidney;brain; superior cervical ganglion;lung;appendix;pons;trigeminal ganglion; 0.78463 0.48903 0.057118534 57.99716914 15.65277 0.55872 PTK2 0.999992957786805 7.04221319458345e-06 1.01316176294646e-16 protein tyrosine kinase 2 FUNCTION: Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription. {ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:11331870, ECO:0000269|PubMed:11980671, ECO:0000269|PubMed:15166238, ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:15895076, ECO:0000269|PubMed:16919435, ECO:0000269|PubMed:16927379, ECO:0000269|PubMed:17395594, ECO:0000269|PubMed:17431114, ECO:0000269|PubMed:17968709, ECO:0000269|PubMed:18006843, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:18256281, ECO:0000269|PubMed:18292575, ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:18677107, ECO:0000269|PubMed:19138410, ECO:0000269|PubMed:19147981, ECO:0000269|PubMed:19224453, ECO:0000269|PubMed:20332118, ECO:0000269|PubMed:20495381, ECO:0000269|PubMed:21454698}.; DISEASE: Note=Aberrant PTK2/FAK1 expression may play a role in cancer cell proliferation, migration and invasion, in tumor formation and metastasis. PTK2/FAK1 overexpression is seen in many types of cancer.; TISSUE SPECIFICITY: Detected in B and T-lymphocytes. Isoform 1 and isoform 6 are detected in lung fibroblasts (at protein level). Ubiquitous. {ECO:0000269|PubMed:20109444, ECO:0000269|PubMed:7692878, ECO:0000269|PubMed:8247543, ECO:0000269|PubMed:8422239}.; myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;bladder;amygdala;heart;cartilage;tongue;pineal body;spinal cord;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;hypothalamus;pancreas;lung;mesenchyma;adrenal gland;placenta;amnion;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;occipital lobe;medulla oblongata;superior cervical ganglion;thalamus;hypothalamus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.86876 . -1.506435464 3.544468035 55.1779 1.48998 PTK2B 0.984520870569303 0.0154791294066865 2.40103565257946e-11 protein tyrosine kinase 2 beta FUNCTION: Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T- cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376'. Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2. {ECO:0000269|PubMed:10022920, ECO:0000269|PubMed:12771146, ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:15050747, ECO:0000269|PubMed:15166227, ECO:0000269|PubMed:17634955, ECO:0000269|PubMed:18086875, ECO:0000269|PubMed:18339875, ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:18765415, ECO:0000269|PubMed:19086031, ECO:0000269|PubMed:19207108, ECO:0000269|PubMed:19244237, ECO:0000269|PubMed:19428251, ECO:0000269|PubMed:19648005, ECO:0000269|PubMed:19880522, ECO:0000269|PubMed:20001213, ECO:0000269|PubMed:20381867, ECO:0000269|PubMed:20521079, ECO:0000269|PubMed:21357692, ECO:0000269|PubMed:21533080, ECO:0000269|PubMed:7544443, ECO:0000269|PubMed:8670418, ECO:0000269|PubMed:8849729}.; DISEASE: Note=Aberrant PTK2B/PYK2 expression may play a role in cancer cell proliferation, migration and invasion, in tumor formation and metastasis. Elevated PTK2B/PYK2 expression is seen in gliomas, hepatocellular carcinoma, lung cancer and breast cancer.; TISSUE SPECIFICITY: Most abundant in the brain, with highest levels in amygdala and hippocampus. Low levels in kidney (at protein level). Also expressed in spleen and lymphocytes. {ECO:0000269|PubMed:7544443, ECO:0000269|PubMed:9545257}.; lymphoreticular;ovary;colon;skin;bone marrow;prostate;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;lacrimal gland;nervous;blood;lens;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;stomach;cerebellum;thymus; amygdala;superior cervical ganglion;subthalamic nucleus;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;temporal lobe;prefrontal cortex;globus pallidus;pons;parietal lobe;cingulate cortex;cerebellum; 0.34869 0.74272 -1.275066404 5.189903279 2387.00343 9.06613 PTK6 1.17663250084696e-07 0.341835054065898 0.658164828270852 protein tyrosine kinase 6 FUNCTION: Non-receptor tyrosine-protein kinase implicated in the regulation of a variety of signaling pathways that control the differentiation and maintenance of normal epithelia, as well as tumor growth. Function seems to be context dependent and differ depending on cell type, as well as its intracellular localization. A number of potential nuclear and cytoplasmic substrates have been identified. These include the RNA-binding proteins: KHDRBS1/SAM68, KHDRBS2/SLM1, KHDRBS3/SLM2 and SFPQ/PSF; transcription factors: STAT3 and STAT5A/B and a variety of signaling molecules: ARHGAP35/p190RhoGAP, PXN/paxillin, BTK/ATK, STAP2/BKS. Associates also with a variety of proteins that are likely upstream of PTK6 in various signaling pathways, or for which PTK6 may play an adapter-like role. These proteins include ADAM15, EGFR, ERBB2, ERBB3 and IRS4. In normal or non-tumorigenic tissues, PTK6 promotes cellular differentiation and apoptosis. In tumors PTK6 contributes to cancer progression by sensitizing cells to mitogenic signals and enhancing proliferation, anchorage- independent survival and migration/invasion. Association with EGFR, ERBB2, ERBB3 may contribute to mammary tumor development and growth through enhancement of EGF-induced signaling via BTK/AKT and PI3 kinase. Contributes to migration and proliferation by contributing to EGF-mediated phosphorylation of ARHGAP35/p190RhoGAP, which promotes association with RASA1/p120RasGAP, inactivating RhoA while activating RAS. EGF stimulation resulted in phosphorylation of PNX/Paxillin by PTK6 and activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion. PTK6 activates STAT3 and STAT5B to promote proliferation. Nuclear PTK6 may be important for regulating growth in normal epithelia, while cytoplasmic PTK6 might activate oncogenic signaling pathways.; . TISSUE SPECIFICITY: Epithelia-specific. Very high level in colon and high levels in small intestine and prostate, and low levels in some fetal tissues. Not expressed in breast or ovarian tissue but expressed in high percentage of breast and ovarian cancers. Also overexpressed in some metastatic melanomas, lymphomas, colon cancers, squamous cell carcinomas and prostate cancers. Also found in melanocytes. Not expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Isoform 2 is present in prostate epithelial cell lines derived from normal prostate and prostate adenocarcinomas, as well as in a variety of cell lines. {ECO:0000269|PubMed:12833144, ECO:0000269|PubMed:15509496, ECO:0000269|PubMed:16651629, ECO:0000269|PubMed:9185712}.; unclassifiable (Anatomical System);bile duct;pancreas;lymph node;cartilage;colon;cervix;kidney;mammary gland;skin;stomach; superior cervical ganglion;tongue;pons;trigeminal ganglion;skeletal muscle; 0.21520 0.17447 -1.041578376 7.773059684 88.26186 2.01278 PTK7 0.975879481016201 0.0241205103369059 8.64689268589339e-09 protein tyrosine kinase 7 (inactive) FUNCTION: Inactive tyrosine kinase involved in Wnt signaling pathway. Component of both the non-canonical (also known as the Wnt/planar cell polarity signaling) and the canonical Wnt signaling pathway. Functions in cell adhesion, cell migration, cell polarity, proliferation, actin cytoskeleton reorganization and apoptosis. Has a role in embryogenesis, epithelial tissue organization and angiogenesis. {ECO:0000269|PubMed:18471990, ECO:0000269|PubMed:20558616, ECO:0000269|PubMed:20837484, ECO:0000269|PubMed:21103379, ECO:0000269|PubMed:21132015}.; . TISSUE SPECIFICITY: Highly expressed in lung, liver, pancreas, kidney, placenta and melanocytes. Weakly expressed in thyroid gland, ovary, brain, heart and skeletal muscle. Also expressed in erythroleukemia cells. But not expressed in colon.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;oesophagus;endometrium;larynx;bone;thyroid;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; ciliary ganglion; 0.64562 0.13964 -0.766111714 13.17527719 636.95125 5.07778 PTLAH . . . patella aplasia-hypoplasia . . . . . . . . . . . PTMA 0.377491925621091 0.576544202434321 0.0459638719445889 prothymosin, alpha FUNCTION: Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.; . . lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;tonsil;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;synovium;bone;testis;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; . . . -0.009020804 52.8544468 . . PTMAP1 . . . prothymosin, alpha pseudogene 1 . . . . . . . . . . . PTMAP2 . . . prothymosin, alpha pseudogene 2 . . . . . 0.28434 . . . . . PTMAP3 . . . prothymosin, alpha pseudogene 3 . . . . . . . . . . . PTMAP4 . . . prothymosin, alpha pseudogene 4 . . . . . 0.28434 . . . . . PTMAP5 . . . prothymosin, alpha pseudogene 5 . . . . . . . . . . . PTMAP6 . . . prothymosin, alpha pseudogene 6 . . . . . . . . . . . PTMAP7 . . . prothymosin, alpha pseudogene 7 . . . . . . . . . . . PTMAP8 . . . prothymosin, alpha pseudogene 8 . . . . . . . . . . . PTMS 0.778967638261344 0.213862815534181 0.00716954620447516 parathymosin FUNCTION: Parathymosin may mediate immune function by blocking the effect of prothymosin alpha which confers resistance to certain opportunistic infections.; . . myocardium;ovary;salivary gland;colon;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lens;bile duct;lung;visual apparatus;duodenum;spleen;head and neck;kidney;mammary gland;thymus; . 0.21897 0.21690 0.079165051 59.43029016 1.69941 0.05565 PTN 0.289147235393633 0.689746714239957 0.0211060503664102 pleiotrophin FUNCTION: Secreted growth factor that induces neurite outgrowth and which is mitogenic for fibroblasts, epithelial, and endothelial cells. Binds anaplastic lymphoma kinase (ALK) which induces MAPK pathway activation, an important step in the anti- apoptotic signaling of PTN and regulation of cell proliferation. {ECO:0000269|PubMed:11278720, ECO:0000269|PubMed:1768439}.; . TISSUE SPECIFICITY: Osteoblast and brain.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;larynx;bone;iris;pituitary gland;testis;brain;bladder;pineal gland;unclassifiable (Anatomical System);heart;tongue;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;stomach; dorsal root ganglion;whole brain;superior cervical ganglion;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;pons;caudate nucleus;subthalamic nucleus;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;pituitary;cingulate cortex;amygdala;hypothalamus;spinal cord;temporal lobe;atrioventricular node;skeletal muscle;fetal brain;prefrontal cortex;parietal lobe;cerebellum; 0.28928 0.37007 0.279402865 70.86577023 18.3676 0.63669 PTOS1 . . . ptosis, congenital 1 (autosomal dominant) . . . . . . . . . . . PTOV1 0.358456527279287 0.641012483198515 0.000530989522198395 prostate tumor overexpressed 1 FUNCTION: May activate transcription. Required for nuclear translocation of FLOT1. Promotes cell proliferation. {ECO:0000269|PubMed:12598323, ECO:0000269|PubMed:15713644, ECO:0000269|PubMed:17641689}.; . TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, placenta, skeletal muscle and small intestine. {ECO:0000269|PubMed:11313889}.; medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;larynx;thyroid;iris;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;pancreas;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; whole brain;superior cervical ganglion;testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;fetal brain;cerebellum peduncles;prefrontal cortex;testis;caudate nucleus;cingulate cortex; 0.36920 0.11188 -0.821100135 11.88369899 836.58972 5.66639 PTOV1-AS1 . . . PTOV1 antisense RNA 1 . . . . . . . . . . . PTOV1-AS2 . . . PTOV1 antisense RNA 2 . . . . . . . . . . . PTP4A1 0.889900786451036 0.108953620944541 0.00114559260442328 protein tyrosine phosphatase type IVA, member 1 FUNCTION: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. {ECO:0000269|PubMed:12235145, ECO:0000269|PubMed:12782572, ECO:0000269|PubMed:14643450}.; . TISSUE SPECIFICITY: Expressed in bone marrow, lymph nodes, T lymphocytes, spleen, thymus and tonsil. Overexpressed in tumor cell lines. {ECO:0000269|PubMed:10940933, ECO:0000269|PubMed:12235145}.; . . 0.21134 . -0.075159878 47.78839349 6.0286 0.22793 PTP4A1P1 . . . protein tyrosine phosphatase type IVA, member 1 pseudogene 1 . . . . . . . . . . . PTP4A1P2 . . . protein tyrosine phosphatase type IVA, member 1 pseudogene 2 . . . . . . . . . . . PTP4A1P3 . . . protein tyrosine phosphatase type IVA, member 1 pseudogene 3 . . . . . . . . . . . PTP4A1P4 . . . protein tyrosine phosphatase type IVA, member 1 pseudogene 4 . . . . . . . . . . . PTP4A1P5 . . . protein tyrosine phosphatase type IVA, member 1 pseudogene 5 . . . . . . . . . . . PTP4A1P6 . . . protein tyrosine phosphatase type IVA, member 1 pseudogene 6 . . . . . . . . . . . PTP4A1P7 . . . protein tyrosine phosphatase type IVA, member 1 pseudogene 7 . . . . . . . . . . . PTP4A2 0.760772901354061 0.237293789925906 0.00193330872003268 protein tyrosine phosphatase type IVA, member 2 FUNCTION: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Promotes tumors. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB. {ECO:0000269|PubMed:14643450}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in skeletal muscle, heart and thymus. Overexpressed in prostate tumor tissue. {ECO:0000269|PubMed:10940933, ECO:0000269|PubMed:11734337, ECO:0000269|PubMed:8661118}.; myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pineal body;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;oesophagus;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach;thymus; amygdala;testis - interstitial;medulla oblongata;occipital lobe;thalamus;adipose tissue;hypothalamus;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;whole blood;parietal lobe;cingulate cortex;thymus; 0.08994 0.08609 -0.009020804 52.8544468 2.35834 0.08001 PTP4A2P1 . . . protein tyrosine phosphatase type IVA, member 2 pseudogene 1 . . . . . . . . . . . PTP4A2P2 . . . protein tyrosine phosphatase type IVA, member 2 pseudogene 2 . . . . . . . . . . . PTP4A3 0.127669884218514 0.780179392280861 0.092150723500625 protein tyrosine phosphatase type IVA, member 3 FUNCTION: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II. {ECO:0000269|PubMed:11355880, ECO:0000269|PubMed:12782572}.; . TISSUE SPECIFICITY: Mainly expressed in cardiomyocytes and skeletal muscle; also found in pancreas. Consistently overexpressed in colon cancer metastasis. {ECO:0000269|PubMed:11355880}.; ovary;sympathetic chain;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;iris;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;skeletal muscle;greater omentum;pancreas;lung;placenta;visual apparatus;spleen;cervix;kidney;stomach; superior cervical ganglion;heart;trigeminal ganglion;skeletal muscle; 0.21928 0.22085 -0.317668748 31.45789101 12.49227 0.45442 PTPDC1 0.00209572239053366 0.997054675192194 0.000849602417272359 protein tyrosine phosphatase domain containing 1 FUNCTION: May play roles in cilia formation and/or maintenance. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;substantia nigra;parathyroid;skin;uterus;whole body;lung;bone;placenta;liver;testis;spleen;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.10832 . -0.216746887 37.69757018 159.73174 2.75923 PTPMT1 0.459152455272006 0.514547681633407 0.0262998630945869 protein tyrosine phosphatase, mitochondrial 1 FUNCTION: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production. Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues. Probably involved in regulation of insulin secretion in pancreatic beta cells (By similarity). {ECO:0000250}.; . . ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;oesophagus;cerebral cortex;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach; . 0.20141 0.12378 . . 21.79044 0.73393 PTPN1 0.69764496881077 0.302322312066641 3.2719122589578e-05 protein tyrosine phosphatase, non-receptor type 1 FUNCTION: Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET. {ECO:0000269|PubMed:18819921, ECO:0000269|PubMed:21135139, ECO:0000269|PubMed:22169477}.; . . . . 0.49216 0.42468 -0.358119787 29.16371786 23.44227 0.78126 PTPN2 0.995606482600094 0.00439343823728612 7.91626201607083e-08 protein tyrosine phosphatase, non-receptor type 2 FUNCTION: Non-receptor type tyrosine-specific phosphatase that dephosphorylates receptor protein tyrosine kinases including INSR, EGFR, CSF1R, PDGFR. Also dephosphorylates non-receptor protein tyrosine kinases like JAK1, JAK2, JAK3, Src family kinases, STAT1, STAT3, STAT5A, STAT5B and STAT6 either in the nucleus or the cytoplasm. Negatively regulates numerous signaling pathways and biological processes like hematopoiesis, inflammatory response, cell proliferation and differentiation, and glucose homeostasis. Plays a multifaceted and important role in the development of the immune system. Functions in T-cell receptor signaling through dephosphorylation of FYN and LCK to control T-cells differentiation and activation. Dephosphorylates CSF1R, negatively regulating its downstream signaling and macrophage differentiation. Negatively regulates cytokine (IL2/interleukin-2 and interferon)-mediated signaling through dephosphorylation of the cytoplasmic kinases JAK1, JAK3 and their substrate STAT1, that propagate signaling downstream of the cytokine receptors. Also regulates the IL6/interleukin-6 and IL4/interleukin-4 cytokine signaling through dephosphorylation of STAT3 and STAT6 respectively. In addition to the immune system, it is involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. Activated by the integrin ITGA1/ITGB1, it dephosphorylates EGFR and negatively regulates EGF signaling. Dephosphorylates PDGFRB and negatively regulates platelet-derived growth factor receptor-beta signaling pathway and therefore cell proliferation. Negatively regulates tumor necrosis factor-mediated signaling downstream via MAPK through SRC dephosphorylation. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of the hepatocyte growth factor receptor MET. Plays also an important role in glucose homeostasis. For instance, negatively regulates the insulin receptor signaling pathway through the dephosphorylation of INSR and control gluconeogenesis and liver glucose production through negative regulation of the IL6 signaling pathways. Finally, it negatively regulates prolactin-mediated signaling pathway through dephosphorylation of STAT5A and STAT5B. May also bind DNA. {ECO:0000269|PubMed:10734133, ECO:0000269|PubMed:11909529, ECO:0000269|PubMed:12138178, ECO:0000269|PubMed:12612081, ECO:0000269|PubMed:14966296, ECO:0000269|PubMed:15592458, ECO:0000269|PubMed:18819921, ECO:0000269|PubMed:22080863, ECO:0000269|PubMed:9488479}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 2 is probably the major isoform. Isoform 1 is expressed in T-cells and in placenta. {ECO:0000269|PubMed:1731319, ECO:0000269|PubMed:2546150}.; medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;endometrium;bone;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; white blood cells;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.94655 . 0.749657564 86.56522765 198.1961 3.04195 PTPN2P1 . . . protein tyrosine phosphatase, non-receptor type 2 pseudogene 1 . . . . . . . . . . . PTPN2P2 . . . protein tyrosine phosphatase, non-receptor type 2 pseudogene 2 . . . . . . . . . . . PTPN3 0.000188227651000982 0.999811394266552 3.78082446688931e-07 protein tyrosine phosphatase, non-receptor type 3 FUNCTION: May act at junctions between the membrane and the cytoskeleton. Possesses tyrosine phosphatase activity.; . . medulla oblongata;smooth muscle;colon;parathyroid;skin;uterus;endometrium;thyroid;testis;dura mater;bladder;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;muscle;adrenal cortex;skeletal muscle;pia mater;lung;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.33179 0.60913 -1.16661987 6.074545883 3579.8361 11.56829 PTPN4 0.999997516004175 2.48399582483888e-06 3.95576099045768e-17 protein tyrosine phosphatase, non-receptor type 4 FUNCTION: May act at junctions between the membrane and the cytoskeleton.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;skin;skeletal muscle;retina;breast;uterus;prostate;lung;endometrium;larynx;bone;testis;head and neck;kidney;brain;tonsil; superior cervical ganglion;subthalamic nucleus; 0.18506 0.12354 -0.021969881 52.14673272 429.77615 4.32968 PTPN5 0.000777688142490709 0.995707112579371 0.00351519927813854 protein tyrosine phosphatase, non-receptor type 5 FUNCTION: May regulate the activity of several effector molecules involved in synaptic plasticity and neuronal cell survival, including MAPKs, Src family kinases and NMDA receptors. {ECO:0000269|PubMed:21777200}.; . . unclassifiable (Anatomical System);ovary;heart;hypothalamus;hippocampus;brain; . 0.41089 0.18970 -0.598810865 18.13517339 2288.45061 8.85295 PTPN6 0.999911914896819 8.80850747409063e-05 2.84406069216917e-11 protein tyrosine phosphatase, non-receptor type 6 FUNCTION: Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis. {ECO:0000269|PubMed:11266449}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in hematopoietic cells. Isoform 2 is expressed in non-hematopoietic cells.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;alveolus;liver;spleen;kidney;mammary gland;stomach;thymus; white blood cells;whole blood; 0.77351 0.54281 -0.622676946 17.30950696 38.84867 1.15059 PTPN7 2.56582220393352e-07 0.726876183550953 0.273123559866827 protein tyrosine phosphatase, non-receptor type 7 FUNCTION: Protein phosphatase that acts preferentially on tyrosine-phosphorylated MAPK1. Plays a role in the regulation of T and B-lymphocyte development and signal transduction. {ECO:0000269|PubMed:10206983, ECO:0000269|PubMed:10559944, ECO:0000269|PubMed:10702794, ECO:0000269|PubMed:1510684, ECO:0000269|PubMed:1530918, ECO:0000269|PubMed:9624114}.; . TISSUE SPECIFICITY: Expressed exclusively in thymus and spleen. {ECO:0000269|PubMed:1510684, ECO:0000269|PubMed:1530918}.; unclassifiable (Anatomical System);lymph node;cartilage;colon;blood;skeletal muscle;bone marrow;breast;uterus;pancreas;lung;endometrium;epididymis;liver;testis;spleen;germinal center;kidney;brain;tonsil; dorsal root ganglion;superior cervical ganglion;testis;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.24586 0.14992 7.61E-05 53.98089172 3744.17727 11.96155 PTPN9 0.9862836143924 0.0137161257008741 2.5990672598145e-07 protein tyrosine phosphatase, non-receptor type 9 FUNCTION: Protein-tyrosine phosphatase that could participate in the transfer of hydrophobic ligands or in functions of the Golgi apparatus. {ECO:0000269|PubMed:19167335}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;blood;lens;skeletal muscle;pancreas;pia mater;lung;epididymis;placenta;macula lutea;duodenum;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;caudate nucleus;atrioventricular node;trigeminal ganglion;parietal lobe;cerebellum; 0.35974 0.11224 -0.558357437 19.54470394 31.40712 0.99008 PTPN11 0.999877230878678 0.000122769057470549 6.38519788034449e-11 protein tyrosine phosphatase, non-receptor type 11 FUNCTION: Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Dephosphorylates ROCK2 at Tyr-722 resulting in stimulatation of its RhoA binding activity. {ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:18559669, ECO:0000269|PubMed:18829466}.; DISEASE: LEOPARD syndrome 1 (LPRD1) [MIM:151100]: A disorder characterized by lentigines, electrocardiographic conduction abnormalities, ocular hypertelorism, pulmonic stenosis, abnormalities of genitalia, retardation of growth, and sensorineural deafness. {ECO:0000269|PubMed:12058348, ECO:0000269|PubMed:14961557, ECO:0000269|PubMed:15121796, ECO:0000269|PubMed:15389709, ECO:0000269|PubMed:15520399, ECO:0000269|PubMed:15690106, ECO:0000269|PubMed:16679933, ECO:0000269|PubMed:24891296}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Noonan syndrome 1 (NS1) [MIM:163950]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. Some patients with NS1 develop multiple giant cell lesions of the jaw or other bony or soft tissues, which are classified as pigmented villonodular synovitis (PVNS) when occurring in the jaw or joints. {ECO:0000269|PubMed:11704759, ECO:0000269|PubMed:11992261, ECO:0000269|PubMed:12161469, ECO:0000269|PubMed:12325025, ECO:0000269|PubMed:12529711, ECO:0000269|PubMed:12634870, ECO:0000269|PubMed:12717436, ECO:0000269|PubMed:12739139, ECO:0000269|PubMed:12960218, ECO:0000269|PubMed:15384080, ECO:0000269|PubMed:15948193, ECO:0000269|PubMed:19020799, ECO:0000269|PubMed:24891296}. Note=The disease is caused by mutations affecting the gene represented in this entry. Mutations in PTPN11 account for more than 50% of the cases.; DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages. {ECO:0000269|PubMed:12717436}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Metachondromatosis (MC) [MIM:156250]: A skeletal disorder with radiologic features of both multiple exostoses and Ollier disease, characterized by the presence of exostoses, commonly of the bones of the hands and feet, and enchondromas of the metaphyses of long bones and iliac crest. {ECO:0000269|PubMed:20577567}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, with highest levels in heart, brain, and skeletal muscle. {ECO:0000269|PubMed:1280823, ECO:0000269|PubMed:7681589, ECO:0000269|PubMed:8216283}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;oesophagus;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;cornea;adrenal gland;placenta;visual apparatus;hippocampus;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;aorta;stomach; amygdala;testis - interstitial;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;hypothalamus;spinal cord;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.26245 0.72890 -0.427900189 25.14744043 19.44641 0.66817 PTPN12 0.999459858785815 0.000540141117607977 9.65771199018582e-11 protein tyrosine phosphatase, non-receptor type 12 FUNCTION: Dephosphorylates cellular tyrosine kinases, including PTK2B/PYK2, and thereby regulates signaling via PTK2B/PYK2. {ECO:0000269|PubMed:17329398}.; . . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;cochlea;gum;thyroid;amniotic fluid;brain;amygdala;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;head and neck;kidney;stomach; trigeminal ganglion; 0.37635 0.16791 -0.488577883 22.64685067 1762.97619 7.75318 PTPN13 5.05692716523618e-10 0.999999992220275 7.2740322066444e-09 protein tyrosine phosphatase, non-receptor type 13 FUNCTION: Tyrosine phosphatase which regulates negatively FAS- induced apoptosis and NGFR-mediated pro-apoptotic signaling (PubMed:15611135). May regulate phosphoinositide 3-kinase (PI3K) signaling through dephosphorylation of PIK3R2 (PubMed:23604317). {ECO:0000269|PubMed:15611135, ECO:0000269|PubMed:23604317}.; . TISSUE SPECIFICITY: Present in most tissues with the exception of the liver and skeletal muscle. Most abundant in lung, kidney and fetal brain.; colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;thyroid;bone;pituitary gland;testis;amniotic fluid;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;lens;skeletal muscle;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;stomach; superior cervical ganglion;atrioventricular node; 0.53061 0.17583 1.295217909 93.89006841 2553.22705 9.43799 PTPN14 0.991959026069808 0.00804097390638161 2.38106829675703e-11 protein tyrosine phosphatase, non-receptor type 14 FUNCTION: Protein tyrosine phosphatase which may play a role in the regulation of lymphangiogenesis, cell-cell adhesion, cell- matrix adhesion, cell migration, cell growth and also regulates TGF-beta gene expression, thereby modulating epithelial- mesenchymal transition. Mediates beta-catenin dephosphorylation at adhesion junctions. Acts as a negative regulator of the oncogenic property of YAP, a downstream target of the hippo pathway, in a cell density-dependent manner. May function as a tumor suppressor. {ECO:0000269|PubMed:10934049, ECO:0000269|PubMed:12808048, ECO:0000269|PubMed:17893246, ECO:0000269|PubMed:20826270, ECO:0000269|PubMed:22233626, ECO:0000269|PubMed:22525271, ECO:0000269|PubMed:22948661}.; DISEASE: Choanal atresia and lymphedema (CHATLY) [MIM:613611]: A disease characterized by posterior choanal atresia and lymphedema. Additional features are a high-arched palate, hypoplastic nipples, and mild pectus excavatum. {ECO:0000269|PubMed:20826270}. Note=The disease is caused by mutations affecting the gene represented in this entry. A homozygous deletion in PTPN14 predicted to result in frameshift and premature truncation, has been shown to be the cause of choanal atresia and lymphedema in one family.; DISEASE: Note=Influence clinical severity of hereditary haemorragic telagiectasia (HHT). {ECO:0000269|PubMed:22233626}.; TISSUE SPECIFICITY: Ubiquitous.; . . 0.25116 0.28275 -0.295848828 32.27765983 873.89149 5.75238 PTPN18 6.51922683029034e-07 0.884512832612319 0.115486515464998 protein tyrosine phosphatase, non-receptor type 18 FUNCTION: Differentially dephosphorylate autophosphorylated tyrosine kinases which are known to be overexpressed in tumor tissues.; . TISSUE SPECIFICITY: Expressed in brain, colon and several tumor- derived cell lines. {ECO:0000269|PubMed:8950995}.; lymphoreticular;ovary;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pineal body;blood;breast;pancreas;lung;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion; 0.07611 0.11551 -0.224023033 37.4321774 2867.52409 10.13944 PTPN20 . . . protein tyrosine phosphatase, non-receptor type 20 FUNCTION: Tyrosine-protein phosphatase targeted to sites of actin polymerization in response of varied extracellular stimuli. Has tyrosine phosphatase activity towards various tyrosyl phosphorylated substrates.; . TISSUE SPECIFICITY: Present in many cell lines (at protein level). Widely expressed. {ECO:0000269|PubMed:15790311}.; . . 0.54478 0.08314 . . . . PTPN20CP . . . protein tyrosine phosphatase, non-receptor type 20C, pseudogene . . . . . . . . . . . PTPN21 2.36179668693425e-07 0.999953845730635 4.59180896960917e-05 protein tyrosine phosphatase, non-receptor type 21 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;atrium;thyroid;testis;brain;unclassifiable (Anatomical System);heart;cartilage;muscle;blood;lens;bile duct;breast;lung;placenta;macula lutea;liver;spleen;kidney;aorta; superior cervical ganglion;uterus corpus;testis - interstitial;testis - seminiferous tubule;adrenal gland;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15764 0.14576 0.435344483 77.36494456 3246.49545 10.85309 PTPN22 3.0777571006681e-16 0.0340006356983055 0.965999364301694 protein tyrosine phosphatase, non-receptor type 22 FUNCTION: Acts as negative regulator of T-cell receptor (TCR) signaling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signaling molecules (PubMed:16461343, PubMed:18056643). Associates with and probably dephosphorylates CBL. Dephosphorylates LCK at its activating 'Tyr-394' residue (PubMed:21719704). Dephosphorylates ZAP70 at its activating 'Tyr- 493' residue (PubMed:16461343). Dephosphorylates the immune system activator SKAP2 (PubMed:21719704). Positively regulates toll-like receptor (TLR)-induced type 1 interferon production (PubMed:23871208). Promotes host antiviral responses mediated by type 1 interferon (By similarity). Regulates NOD2-induced pro- inflammatory cytokine secretion and autophagy (PubMed:23991106). {ECO:0000250|UniProtKB:P29352, ECO:0000269|PubMed:16461343, ECO:0000269|PubMed:18056643, ECO:0000269|PubMed:19167335, ECO:0000269|PubMed:21719704, ECO:0000269|PubMed:23871208, ECO:0000269|PubMed:23991106}.; DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:15273934}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, insulin-dependent (IDDM) [MIM:222100]: A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:15004560}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Rheumatoid arthritis (RA) [MIM:180300]: An inflammatory disease with autoimmune features and a complex genetic component. It primarily affects the joints and is characterized by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures. {ECO:0000269|PubMed:15208781}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Vitiligo (VTLG) [MIM:193200]: A pigmentary disorder of the skin and mucous membranes. It is characterized by circumscribed depigmented macules and patches, commonly on extensor aspects of extremities, on the face or neck and in skin folds. Vitiligo is a progressive disorder in which some or all of the melanocytes in the affected skin are selectively destroyed. It is a multifactorial disorder with a complex etiology probably including autoimmune mechanisms, and is associated with an elevated risk of other autoimmune diseases. {ECO:0000269|PubMed:16015369}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in bone marrow, B and T-cells, PBMCs, natural killer cells, monocytes, dendritic cells and neutrophils (PubMed:15208781). Both isoform 1 and 4 are predominantly expressed in lymphoid tissues and cells. Isoform 1 is expressed in thymocytes and both mature B and T-cells. {ECO:0000269|PubMed:15208781}.; unclassifiable (Anatomical System);lymph node;lung;adrenal gland;nasopharynx;thyroid;testis;colon;germinal center;skeletal muscle;bone marrow; superior cervical ganglion;temporal lobe;globus pallidus;atrioventricular node;pons;trigeminal ganglion; 0.15785 0.35538 0.268267497 70.64166077 275.51599 3.55515 PTPN23 0.647596781106679 0.352403215263194 3.63012739111467e-09 protein tyrosine phosphatase, non-receptor type 23 FUNCTION: Plays a role in sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) via its interaction with the ESCRT-I complex (endosomal sorting complex required for transport I), and possibly also other ESCRT complexes. May act as a negative regulator of Ras-mediated mitogenic activity. Plays a role in ciliogenesis. {ECO:0000269|PubMed:18434552, ECO:0000269|PubMed:20393563, ECO:0000269|PubMed:21757351}.; . . lymphoreticular;myocardium;smooth muscle;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;synovium;thyroid;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;urinary;blood;lens;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; . 0.09755 0.12139 -1.3304325 4.676810569 1113.07486 6.37437 PTPRA 0.999976743548953 2.32564508220361e-05 2.2449488999606e-13 protein tyrosine phosphatase, receptor type A . . . ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;brain;amygdala;heart;cartilage;nervous;pineal body;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;amnion;head and neck;kidney;stomach;aorta;cerebellum; whole brain;amygdala;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;hypothalamus;spinal cord;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.34398 0.10195 -1.085675268 7.147912243 2221.73247 8.68079 PTPRB 0.943502941208234 0.0564970587917245 4.10297784152416e-14 protein tyrosine phosphatase, receptor type B FUNCTION: Plays an important role in blood vessel remodeling and angiogenesis. Not necessary for the initial formation of blood vessels, but is essential for their maintenance and remodeling. Can induce dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2. Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a negative regulator of TIE2, and controls TIE2 driven endothelial cell proliferation, which in turn affects blood vessel remodeling during embryonic development and determines blood vessel size during perinatal growth. Essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells and this requires the presence of plakoglobin (By similarity). {ECO:0000250, ECO:0000269|PubMed:19116766, ECO:0000269|PubMed:19136612}.; . . unclassifiable (Anatomical System);cartilage;heart;parathyroid;fovea centralis;choroid;lens;skin;skeletal muscle;retina;bile duct;uterus;optic nerve;lung;frontal lobe;endometrium;placenta;macula lutea;testis;spleen;cervix;kidney;spinal ganglion;brain; superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.28326 0.13944 0.337887267 73.68483133 6004.94186 16.17382 PTPRC 0.999941156148536 5.88438514605854e-05 3.61091241046845e-15 protein tyrosine phosphatase, receptor type C FUNCTION: Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:11909961, ECO:0000269|PubMed:2845400}.; DISEASE: Severe combined immunodeficiency autosomal recessive T- cell-negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+) SCID) [MIM:608971]: A form of severe combined immunodeficiency (SCID), a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development. {ECO:0000269|PubMed:11145714}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multiple sclerosis (MS) [MIM:126200]: A multifactorial, inflammatory, demyelinating disease of the central nervous system. Sclerotic lesions are characterized by perivascular infiltration of monocytes and lymphocytes and appear as indurated areas in pathologic specimens (sclerosis in plaques). The pathological mechanism is regarded as an autoimmune attack of the myelin sheath, mediated by both cellular and humoral immunity. Clinical manifestations include visual loss, extra-ocular movement disorders, paresthesias, loss of sensation, weakness, dysarthria, spasticity, ataxia and bladder dysfunction. Genetic and environmental factors influence susceptibility to the disease. {ECO:0000269|PubMed:11101853}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; . ovary;colon;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;liver;spleen;head and neck;kidney;stomach;aorta;thymus; lymph node;white blood cells;whole blood;tonsil;thymus; 0.17677 0.67006 0.231457213 68.57159707 71.3304 1.75714 PTPRCAP 0.770195971803083 0.221837278523578 0.00796674967333956 protein tyrosine phosphatase, receptor type C associated protein . . . unclassifiable (Anatomical System);lymphoreticular;lymph node;cartilage;heart;colon;fovea centralis;choroid;lens;retina;prostate;pancreas;optic nerve;lung;macula lutea;testis;spleen;germinal center;kidney;brain;mammary gland;aorta;tonsil;stomach; white blood cells;thymus; 0.10618 0.11094 . . 54.82654 1.48341 PTPRD 0.999999982037603 1.79623970237779e-08 4.88348739117673e-23 protein tyrosine phosphatase, receptor type D . . . unclassifiable (Anatomical System);smooth muscle;ovary;developmental;colon;parathyroid;skeletal muscle;retina;breast;pancreas;prostate;whole body;lung;frontal lobe;thyroid;placenta;pituitary gland;testis;head and neck;kidney;brain;mammary gland;cerebellum; amygdala;whole brain;thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.89661 0.17382 -3.078871465 0.483604624 1565.5627 7.32256 PTPRD-AS1 . . . PTPRD antisense RNA 1 . . . . . . . . . . . PTPRD-AS2 . . . PTPRD antisense RNA 2 (head to head) . . . . . . . . . . . PTPRE 0.0100100422146958 0.989986337042143 3.62074316106757e-06 protein tyrosine phosphatase, receptor type E FUNCTION: Isoform 1 plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function (By similarity). {ECO:0000250}.; FUNCTION: Isoform 1 and isoform 2 act as a negative regulator of FceRI-mediated signal transduction leading to cytokine production and degranulation, most likely by acting at the level of SYK to affect downstream events such as phosphorylation of SLP76 and LAT and mobilization of Ca(2+). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in giant cell tumor (osteoclastoma rich in multinucleated osteoclastic cells). {ECO:0000269|PubMed:8610169}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;spinal cord;urinary;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;mammary gland;aorta; amygdala;superior cervical ganglion;whole blood; 0.14178 0.12565 -1.284117362 5.113234253 184.75202 2.95076 PTPRF 0.999998378977356 1.62102264375303e-06 5.72667521434645e-19 protein tyrosine phosphatase, receptor type F FUNCTION: Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity.; DISEASE: Aplasia or hypoplasia of the breasts and/or nipples 2 (BNAH2) [MIM:616001]: A group of congenital deformities encompassing total absence of breasts and nipple (amastia), absence of the nipple (athelia), and absence of the mammary gland (amazia). {ECO:0000269|PubMed:24781087}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;bladder;brain;gall bladder;amygdala;heart;urinary;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;mammary gland;peripheral nerve;colon;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;cerebellum; amygdala;prostate;lung;placenta; 0.30877 0.14232 -3.924965486 0.20051899 258.69725 3.45757 PTPRG 0.00417657315674374 0.995823405243676 2.15995798279799e-08 protein tyrosine phosphatase, receptor type G FUNCTION: Possesses tyrosine phosphatase activity. {ECO:0000269|PubMed:19167335}.; . TISSUE SPECIFICITY: Found in a variety of tissues.; unclassifiable (Anatomical System);medulla oblongata;ovary;hypothalamus;colon;parathyroid;skeletal muscle;bile duct;lung;placenta;thyroid;bone;visual apparatus;kidney;ciliary body;stomach; amygdala;superior cervical ganglion;adipose tissue; 0.72801 0.18321 -1.738187109 2.429818353 1119.45815 6.38788 PTPRG-AS1 . . . PTPRG antisense RNA 1 . . . . . . . . . . . PTPRH 5.09931564319084e-29 7.02714197685245e-05 0.999929728580232 protein tyrosine phosphatase, receptor type H FUNCTION: May contribute to contact inhibition of cell growth and motility by mediating the dephosphorylation of focal adhesion- associated substrates and thus negatively regulating integrin- promoted signaling processes. Induces apoptotic cell death by at least two distinct mechanisms: inhibition of cell survival signaling mediated by PI 3-kinase, Akt, and ILK and activation of a caspase-dependent proapoptotic pathway. Inhibits the basal activity of LCK and its activation in response to TCR stimulation and TCR-induced activation of MAP kinase and surface expression of CD69. Inhibits TCR-induced tyrosine phosphorylation of LAT and ZAP70. Inhibits both basal activity of DOK1 and its CD2-induced tyrosine phosphorylation. Induces dephosphorylation of p130cas, focal adhesion kinase and c-Src. Reduces migratory activity of Jurkat cells. {ECO:0000269|PubMed:11278335, ECO:0000269|PubMed:12101188, ECO:0000269|PubMed:12837766, ECO:0000269|PubMed:15850787}.; . TISSUE SPECIFICITY: Expressed at high levels in the brain, spleen and liver and at lower levels in the heart and stomach. Expressed in pancreatic and colorectal cancer cells, but not in normal pancreas or colon. Expression in hepatocellular carcinoma is related to the differentiation status of the tumor and expression is inversely related to tumor aggressiveness. {ECO:0000269|PubMed:12837766, ECO:0000269|PubMed:12879010, ECO:0000269|PubMed:8294459}.; unclassifiable (Anatomical System);pancreas;lung;colon;spleen;skeletal muscle; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.07710 . 1.111434312 92.06770465 5182.51875 14.81765 PTPRJ 2.38654353395849e-05 0.999968796726082 7.33783857825722e-06 protein tyrosine phosphatase, receptor type J FUNCTION: Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET (variant MEN2A), KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2. Plays a role in cell adhesion, migration, proliferation and differentiation. Involved in vascular development. Regulator of macrophage adhesion and spreading. Positively affects cell-matrix adhesion. Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation. Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR. Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation. Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation. Enhances the barrier function of epithelial junctions during reassembly. Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling. {ECO:0000269|PubMed:10821867, ECO:0000269|PubMed:11259588, ECO:0000269|PubMed:12062403, ECO:0000269|PubMed:12370829, ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:12913111, ECO:0000269|PubMed:14709717, ECO:0000269|PubMed:16682945, ECO:0000269|PubMed:16778204, ECO:0000269|PubMed:18348712, ECO:0000269|PubMed:18936167, ECO:0000269|PubMed:19332538, ECO:0000269|PubMed:19494114, ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:19922411, ECO:0000269|PubMed:21091576, ECO:0000269|PubMed:21262971, ECO:0000269|PubMed:9531590, ECO:0000269|PubMed:9780142}.; . TISSUE SPECIFICITY: Expressed in the promyelocytic cell line HL- 60, the granulocyte-macrophage colony-stimulating factor-dependent leukemic cell line F-36P, and the IL3 and erythropoietin-dependent leukemic cell line F-36E. Expressed predominantly in epithelial cells and lymphocytes. Enhanced expression at high cell density. {ECO:0000269|PubMed:12370829, ECO:0000269|PubMed:8483328, ECO:0000269|PubMed:9531590}.; smooth muscle;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;optic nerve;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);blood;lens;breast;pancreas;lung;placenta;macula lutea;liver;head and neck;kidney;stomach; superior cervical ganglion;globus pallidus;atrioventricular node; 0.08384 0.14681 0.747656234 86.41778721 563.07811 4.81765 PTPRJ-AS1 . . . PTPRJ antisense RNA 1 . . . . . . . . . . . PTPRK 0.980388546226756 0.0196114537728881 3.56130428132296e-13 protein tyrosine phosphatase, receptor type K FUNCTION: Regulation of processes involving cell contact and adhesion such as growth control, tumor invasion, and metastasis. Negative regulator of EGFR signaling pathway. Forms complexes with beta-catenin and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the catalytic activity of PTPRK/PTP-kappa. {ECO:0000269|PubMed:19836242}.; . TISSUE SPECIFICITY: High levels in lung, brain and colon; less in liver, pancreas, stomach, kidney, placenta and mammary carcinoma.; . . 0.39459 . -1.723336008 2.465204058 177.34828 2.89418 PTPRM 0.999958213992023 4.17860079773411e-05 1.29940659921597e-17 protein tyrosine phosphatase, receptor type M FUNCTION: Involved in cell-cell adhesion through homophilic interactions. May play a key role in signal transduction and growth control. {ECO:0000269|PubMed:16456543}.; . . smooth muscle;ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;nervous;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;pancreas;lung;cornea;placenta;amnion;kidney;stomach;cerebellum; thalamus; 0.20617 0.12992 -2.02851154 1.704411418 316.58577 3.77934 PTPRN 0.021748200630743 0.978223608122257 2.81912469998811e-05 protein tyrosine phosphatase, receptor type N FUNCTION: Plays a role in vesicle-mediated secretory processes (PubMed:24843546). Required for normal accumulation of secretory vesicles in hippocampus, pituitary and pancreatic islets (By similarity). Required for the accumulation of normal levels of insulin-containing vesicles and preventing their degradation (PubMed:24843546). Plays a role in insulin secretion in response to glucose stimuli (PubMed:24843546). Required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain (By similarity). In females, but not in males, required for normal accumulation and secretion of pituitary hormones, such as luteinizing hormone (LH) and follicle- stimulating hormone (FSH) (By similarity). Seems to lack intrinsic enzyme activity (By similarity). {ECO:0000250|UniProtKB:Q60673, ECO:0000269|PubMed:24843546}.; DISEASE: Note=Autoantigen in insulin-dependent diabetes mellitus (IDDM). {ECO:0000269|PubMed:8144912, ECO:0000269|PubMed:8641276}.; TISSUE SPECIFICITY: Expression is restricted to neuroendocrine cells. Found in pancreas, brain and pituitary. {ECO:0000269|PubMed:8024693}.; unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;hypothalamus;pineal body;fovea centralis;choroid;breast;pancreas;lung;frontal lobe;macula lutea;visual apparatus;pituitary gland;brain;cerebellum; amygdala;whole brain;superior cervical ganglion;medulla oblongata;subthalamic nucleus;globus pallidus;caudate nucleus;pons;skeletal muscle; 0.50430 0.32250 -1.392555112 4.269874971 262.5746 3.47632 PTPRN2 0.0165571526676371 0.983434298991953 8.54834040962044e-06 protein tyrosine phosphatase, receptor type N2 FUNCTION: Plays a role in vesicle-mediated secretory processes. Required for normal accumulation of secretory vesicles in hippocampus, pituitary and pancreatic islets. Required for the accumulation of normal levels of insulin-containing vesicles and preventing their degradation. Plays a role in insulin secretion in response to glucose stimuli. Required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain. In females, but not in males, required for normal accumulation and secretion of pituitary hormones, such as luteinizing hormone (LH) and follicle-stimulating hormone (FSH). {ECO:0000250|UniProtKB:P80560}.; DISEASE: Note=Autoantigen in insulin-dependent diabetes mellitus (IDDM). {ECO:0000269|PubMed:8637868, ECO:0000269|PubMed:8798755, ECO:0000269|PubMed:8878534}.; TISSUE SPECIFICITY: Highest levels in brain and pancreas (PubMed:8954911, PubMed:8798755). Lower levels in trachea, prostate, stomach and spinal chord (PubMed:8798755). {ECO:0000269|PubMed:8798755, ECO:0000269|PubMed:8954911}.; . . 0.18753 0.09983 0.889106693 89.19556499 4454.24566 13.37565 PTPRO 0.304626089545522 0.695373854322015 5.61324622015615e-08 protein tyrosine phosphatase, receptor type O FUNCTION: Possesses tyrosine phosphatase activity. Plays a role in regulating the glomerular pressure/filtration rate relationship through an effect on podocyte structure and function (By similarity). {ECO:0000250, ECO:0000269|PubMed:19167335}.; DISEASE: Nephrotic syndrome 6 (NPHS6) [MIM:614196]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. {ECO:0000269|PubMed:21722858}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Glomerulus of kidney. Also detected in brain, lung and placenta. {ECO:0000269|PubMed:10498613}.; unclassifiable (Anatomical System);lymph node;heart;hypothalamus;colon;blood;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;breast;prostate;optic nerve;lung;frontal lobe;macula lutea;visual apparatus;testis;kidney;brain;peripheral nerve; dorsal root ganglion;superior cervical ganglion;fetal brain;globus pallidus; 0.57353 . -1.965936983 1.828261382 172.96294 2.86316 PTPRQ . . . protein tyrosine phosphatase, receptor type Q FUNCTION: Phosphatidylinositol phosphatase required for auditory function. May act by regulating the level of phosphatidylinositol 4,5-bisphosphate (PIP2) level in the basal region of hair bundles. Can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates. Phosphate can be hydrolyzed from the D3 and D5 positions in the inositol ring. Has low tyrosine-protein phosphatase activity; however, the relevance of such activity in vivo is unclear. Plays an important role in adipogenesis of mesenchymal stem cells (MSCs). Regulates the phosphorylation state of AKT1 by suppressing the phosphatidylinositol 3,4,5-trisphosphate (PIP3) level in MSCs and preadipocyte cells. {ECO:0000269|PubMed:19351528}.; DISEASE: Deafness, autosomal recessive, 84A (DFNB84A) [MIM:613391]: A form of non-syndromic deafness characterized by progressive, sensorineural hearing loss and vestibular dysfunction. {ECO:0000269|PubMed:20346435, ECO:0000269|PubMed:20472657}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In developing kidney, it localizes to the basal membrane of podocytes, beginning when podocyte progenitors can first be identified in the embryonic kidney (at protein level). Expressed in lung and kidney. {ECO:0000269|PubMed:12837292, ECO:0000269|PubMed:20346435}.; . . 0.39566 0.10497 . . 17963.04124 28.76351 PTPRR 0.000430475916164989 0.99789778580012 0.00167173828371489 protein tyrosine phosphatase, receptor type R FUNCTION: Sequesters mitogen-activated protein kinases (MAPKs) such as MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs bind to a dephosphorylated kinase interacting motif, phosphorylation of which by the protein kinase A complex releases the MAPKs for activation and translocation into the nucleus (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, placenta, small intestine, stomach, uterus and weakly in the prostate. Isoform alpha has been observed only in the brain. Isoform gamma is expressed in brain, placenta and uterus. Isoform delta is expressed in brain, kidney, placenta, prostate, small intestine and uterus. {ECO:0000269|PubMed:10705342}.; unclassifiable (Anatomical System);amygdala;hypothalamus;sympathetic chain;colon;pancreas;whole body;lung;placenta;bone;visual apparatus;testis;cervix;kidney;bladder;brain; amygdala;superior cervical ganglion;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.45107 0.12979 0.53464283 81.00967209 679.59853 5.21209 PTPRS 0.760915060454347 0.23908493953638 9.27332519607152e-12 protein tyrosine phosphatase, receptor type S FUNCTION: Interacts with LAR-interacting protein LIP.1.; . TISSUE SPECIFICITY: Detected in all tissues tested except for placenta and liver.; unclassifiable (Anatomical System);ovary;islets of Langerhans;urinary;colon;blood;retina;bone marrow;breast;prostate;lung;frontal lobe;larynx;thyroid;hippocampus;head and neck;germinal center;kidney;brain;bladder;stomach; superior cervical ganglion;pons; 0.30785 0.15922 -4.366877839 0.100259495 388.5902 4.15164 PTPRT 0.999998893194682 1.10680531830769e-06 2.26069473100473e-19 protein tyrosine phosphatase, receptor type T FUNCTION: May be involved in both signal transduction and cellular adhesion in the CNS.; . TISSUE SPECIFICITY: Expressed in colon, lung, heart and testis, as well as in fetal and adult brain. Not detected in muscle and peripheral blood leukocytes. {ECO:0000269|PubMed:15155950}.; unclassifiable (Anatomical System);blood;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;breast;prostate;optic nerve;whole body;frontal lobe;placenta;macula lutea;hippocampus;visual apparatus;alveolus;brain; subthalamic nucleus;superior cervical ganglion;medulla oblongata;occipital lobe;prefrontal cortex;pons;cingulate cortex;parietal lobe; 0.39705 0.11014 -1.027089224 7.873319179 360.34688 4.01687 PTPRU 0.990698955783316 0.00930104421529149 1.39234750480718e-12 protein tyrosine phosphatase, receptor type U FUNCTION: Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis. {ECO:0000269|PubMed:10397721, ECO:0000269|PubMed:12501215, ECO:0000269|PubMed:16574648}.; . TISSUE SPECIFICITY: High levels in brain, pancreas, and skeletal muscle; less in colon, kidney, liver, stomach, and uterus; not expressed in placenta and spleen. Also detected in heart, prostate, lung, thymus, testis and ovary. Ubiquitously expressed in brain. Expressed by hematopoietic stem cells. {ECO:0000269|PubMed:8700514, ECO:0000269|PubMed:8870675, ECO:0000269|PubMed:9070223, ECO:0000269|PubMed:9434160}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;ganglion;endometrium;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.34585 0.13375 -1.780505741 2.282377919 2370.71205 9.03935 PTPRVP . . . protein tyrosine phosphatase, receptor type V, pseudogene . . . . . . . . . . . PTPRZ1 0.994707963074545 0.00529203692538452 7.09193319062453e-14 protein tyrosine phosphatase, receptor type Z1 FUNCTION: Protein tyrosine phosphatase that negatively regulates oligodendrocyte precursor proliferation in the embryonic spinal cord. Required for normal differentiation of the precursor cells into mature, fully myelinating oligodendrocytes. May play a role in protecting oligondendrocytes against apoptosis. May play a role in the establishment of contextual memory, probably via the dephosphorylation of proteins that are part of important signaling cascades (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in the central nervous system, where it is localized in the Purkinje cell layer of the cerebellum, the dentate gyrus, and the subependymal layer of the anterior horn of the lateral ventricle. Developmentally regulated in the brain. {ECO:0000269|PubMed:9653645}.; . . 0.41776 0.27352 -2.216367922 1.350554376 7148.28548 18.18568 PTPRZ2 . . . protein tyrosine phosphatase, receptor type, Z2 FUNCTION: Protein tyrosine phosphatase that negatively regulates oligodendrocyte precursor proliferation in the embryonic spinal cord. Required for normal differentiation of the precursor cells into mature, fully myelinating oligodendrocytes. May play a role in protecting oligondendrocytes against apoptosis. May play a role in the establishment of contextual memory, probably via the dephosphorylation of proteins that are part of important signaling cascades (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in the central nervous system, where it is localized in the Purkinje cell layer of the cerebellum, the dentate gyrus, and the subependymal layer of the anterior horn of the lateral ventricle. Developmentally regulated in the brain. {ECO:0000269|PubMed:9653645}.; . . . . . . . . PTRF 0.0208810466767636 0.750653038140711 0.228465915182526 polymerase I and transcript release factor FUNCTION: Plays an important role in caveolae formation and organization. Required for the sequestration of mobile caveolin into immobile caveolae. Termination of transcription by RNA polymerase I involves pausing of transcription by TTF1, and the dissociation of the transcription complex, releasing pre-rRNA and RNA polymerase I from the template. PTRF is required for dissociation of the ternary transcription complex. {ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19726876}.; DISEASE: Congenital generalized lipodystrophy 4 (CGL4) [MIM:613327]: A disorder characterized by the association of congenital generalized lipodystrophy with muscular dystrophy and cardiac anomalies. Congenital generalized lipodystrophy is characterized by a near complete absence of adipose tissue, extreme insulin resistance, hypertriglyceridemia, hepatic steatosis and early onset of diabetes. {ECO:0000269|PubMed:19726876, ECO:0000269|PubMed:20684003}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;oesophagus;larynx;bone;thyroid;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;oral cavity;pharynx;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;olfactory bulb;lung;heart;placenta;appendix;ciliary ganglion;atrioventricular node; 0.59345 0.26484 -0.0274281 51.65723048 53.17912 1.44824 PTRH1 0.00158633515439893 0.690017465619195 0.308396199226406 peptidyl-tRNA hydrolase 1 homolog . . . . . 0.14787 0.32573 . . 39.14924 1.16074 PTRH2 0.336972394236785 0.602740081917032 0.0602875238461821 peptidyl-tRNA hydrolase 2 FUNCTION: The natural substrate for this enzyme may be peptidyl- tRNAs which drop off the ribosome during protein synthesis. {ECO:0000250}.; DISEASE: Neurologic, endocrine, and pancreatic disease, multisystem, infantile-onset (IMNEPD) [MIM:616263]: A progressive multisystem disease characterized by a variety of neurologic, endocrine, and, in some patients, pancreatic features. Variable clinical symptoms include global developmental delay, hypotonia, hearing loss, ataxia, hyporeflexia, facial dysmorphism, hypothyroidism, and pancreatic insufficiency. {ECO:0000269|PubMed:25558065, ECO:0000269|PubMed:25574476}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.44220 0.09030 0.103030231 61.2762444 21.21498 0.71688 PTRHD1 9.18016740847292e-06 0.183353335263583 0.816637484569008 peptidyl-tRNA hydrolase domain containing 1 . . . unclassifiable (Anatomical System);medulla oblongata;lymph node;cartilage;heart;islets of Langerhans;colon;blood;lens;skeletal muscle;prostate;pancreas;whole body;lung;adrenal gland;bone;thyroid;placenta;liver;testis;spleen;kidney;brain;mammary gland;stomach; . . . -0.361761279 28.6329323 36.54909 1.09538 PTS 0.00115618802233995 0.621859694436221 0.376984117541439 6-pyruvoyltetrahydropterin synthase FUNCTION: Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6- pyruvoyl tetrahydropterin. {ECO:0000269|PubMed:1282802}.; DISEASE: Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]: An autosomal recessive disorder characterized by hyperphenylalaninemia, depletion of the neurotransmitters dopamine and serotonin, and progressive cognitive and motor deficits. Neurological symptoms are unresponsive to the classic phenylalanine-low diet. {ECO:0000269|PubMed:10220141, ECO:0000269|PubMed:10585341, ECO:0000269|PubMed:10874306, ECO:0000269|PubMed:11388593, ECO:0000269|PubMed:7698774, ECO:0000269|PubMed:8178819, ECO:0000269|PubMed:8707300, ECO:0000269|PubMed:9159737, ECO:0000269|PubMed:9222757, ECO:0000269|PubMed:9450907}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;cochlea;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;stomach; amygdala;whole brain;occipital lobe;subthalamic nucleus;medulla oblongata;adrenal gland;hypothalamus;globus pallidus;pons;trigeminal ganglion;cingulate cortex; 0.11306 0.61718 -0.119252484 44.53880632 5.732 0.21461 PTTG1 0.169726364244784 0.770820331490602 0.0594533042646145 pituitary tumor-transforming 1 FUNCTION: Regulatory protein, which plays a central role in chromosome stability, in the p53/TP53 pathway, and DNA repair. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESPL1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of ESPL1. Its function is however not limited to a blocking activity, since it is required to activate ESPL1. Negatively regulates the transcriptional activity and related apoptosis activity of TP53. The negative regulation of TP53 may explain the strong transforming capability of the protein when it is overexpressed. May also play a role in DNA repair via its interaction with Ku, possibly by connecting DNA damage-response pathways with sister chromatid separation. {ECO:0000269|PubMed:10411507, ECO:0000269|PubMed:11238996, ECO:0000269|PubMed:11371342, ECO:0000269|PubMed:12355087}.; . TISSUE SPECIFICITY: Expressed at low level in most tissues, except in adult testis, where it is highly expressed. Overexpressed in many patients suffering from pituitary adenomas, primary epithelial neoplasias, and esophageal cancer. {ECO:0000269|PubMed:9811450}.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;vein;skin;bone marrow;uterus;prostate;whole body;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;cornea;adrenal gland;nasopharynx;visual apparatus;duodenum;liver;cervix;spleen;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;bone marrow; . 0.31652 -0.141298762 42.87567823 1.21964 0.04038 PTTG1IP 0.266254067406983 0.708391264307941 0.0253546682850764 pituitary tumor-transforming 1 interacting protein FUNCTION: May facilitate PTTG1 nuclear translocation.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;smooth muscle;ovary;sympathetic chain;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;gum;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;adrenal cortex;blood;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; placenta; 0.06526 0.10670 0.237127192 68.98443029 22.57024 0.75475 PTTG2 0.00173161102598497 0.470222031019484 0.528046357954531 pituitary tumor-transforming 2 . . TISSUE SPECIFICITY: Expressed at low levels in the pituitary, liver, spleen, prostate, testis, ovary, small intestine and colon. Also expressed in various pituitary, testicular, liver and ovarian tumors. {ECO:0000269|PubMed:10084610, ECO:0000269|PubMed:10806349}.; . . . 0.31652 0.349177632 74.18023119 95.95724 2.11601 PTTG3P . . . pituitary tumor-transforming 3, pseudogene . . TISSUE SPECIFICITY: Expressed in ovarian tumor and tumor cell lines (SK-OV-3 and PA1). {ECO:0000269|PubMed:10806349}.; . . 0.11255 . . . . . PTTG4P . . . pituitary tumor-transforming 4 pseudogene . . . . . . . . . . . PTX3 0.0129819003080692 0.859724390106914 0.127293709585017 pentraxin 3 FUNCTION: Plays a role in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self- components and female fertility. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;ovary;heart;islets of Langerhans;vein;skin;skeletal muscle;bone marrow;uterus;pancreas;lung;frontal lobe;cochlea;mesenchyma;bone;placenta;visual apparatus;alveolus;liver;spleen;kidney;brain;bladder;aorta;gall bladder; smooth muscle;adipose tissue;heart;fetal lung;trigeminal ganglion; 0.51617 0.13376 1.038098315 91.20665251 453.81025 4.43135 PTX4 1.77530402250970e-12 0.00802508728483687 0.991974912713388 pentraxin 4 . . TISSUE SPECIFICITY: Widely expressed at low levels with highest levels in small intestine, testis and brain. Very low expression in endothelial cells, monocytes, neutrophils and lymphocytes. Isoform 1 is not expressed in small intestine. {ECO:0000269|PubMed:20357257}.; . . . . 2.65326545 98.83816938 10364.69216 22.23139 PUDP . . . pseudouridine 5'-phosphatase FUNCTION: Dephosphorylates pseudouridine 5'-phosphate, a potential intermediate in rRNA degradation. Pseudouridine is then excreted intact in urine. {ECO:0000269|PubMed:20722631}.; . . . . 0.07182 0.15289 -0.095386216 46.48502005 . . PUDPP1 . . . pseudouridine 5'-phosphatase pseudogene 1 . . . . . . . . . . . PUDPP2 . . . pseudouridine 5'-phosphatase pseudogene 2 . . . . . . . . . . . PUDPP3 . . . pseudouridine 5'-phosphatase pseudogene 3 . . . . . . . . . . . PUF60 0.849324854511446 0.150564863677616 0.000110281810938077 poly(U) binding splicing factor 60KDa FUNCTION: DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation. In association with FUBP1 regulates MYC transcription at the P2 promoter through the core-TFIIH basal transcription factor. Acts as a transcriptional repressor through the core-TFIIH basal transcription factor. Represses FUBP1-induced transcriptional activation but not basal transcription. Decreases ERCC3 helicase activity. Does not repress TFIIH-mediated transcription in xeroderma pigmentosum complementation group B (XPB) cells. Is also involved in pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice site and pyrimidine tract in a cooperative manner with U2AF2. Involved in apoptosis induction when overexpressed in HeLa cells. Isoform 6 failed to repress MYC transcription and inhibited FIR-induced apoptosis in colorectal cancer. Isoform 6 may contribute to tumor progression by enabling increased MYC expression and greater resistance to apoptosis in tumors than in normal cells. Modulates alternative splicing of several mRNAs. Binds to relaxed DNA of active promoter regions. Binds to the pyrimidine tract and 3'-splice site regions of pre-mRNA; binding is enhanced in presence of U2AF2. Binds to Y5 RNA in association with TROVE2. Binds to poly(U) RNA. {ECO:0000269|PubMed:10606266, ECO:0000269|PubMed:10882074, ECO:0000269|PubMed:11239393, ECO:0000269|PubMed:16452196, ECO:0000269|PubMed:16628215, ECO:0000269|PubMed:17579712}.; DISEASE: Verheij syndrome (VRJS) [MIM:615583]: A syndrome characterized by growth retardation, delayed psychomotor development, dysmorphic facial features, and skeletal, mainly vertebral, abnormalities. Additional variable features may include coloboma, renal defects, and cardiac defects. {ECO:0000269|PubMed:24140112}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 2 is expressed in colonic epithelium and colorectal epithelium cancer (at protein level). Isoform 6 is expressed in colorectal epithelial cancer but below detection level in colonic epithelium. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes. {ECO:0000269|PubMed:10668799, ECO:0000269|PubMed:16452196}.; lymphoreticular;medulla oblongata;ovary;skin;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;placenta;hippocampus;duodenum;head and neck;kidney;stomach; whole brain;thalamus;temporal lobe;liver;pons;caudate nucleus;parietal lobe; 0.24714 0.14229 -0.714505427 14.4019816 8.28818 0.30419 PUM1 0.999998854510137 1.14548986255303e-06 1.46628805129605e-16 pumilio RNA binding family member 1 FUNCTION: Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE) (PubMed:21572425, PubMed:18328718, PubMed:21653694, PubMed:21397187). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (PubMed:22955276). Also mediates deadenylation-independent repression by promoting accessibility of miRNAs (PubMed:18776931, PubMed:20818387, PubMed:20860814, PubMed:22345517). Following growth factor stimulation, phosphorylated and binds to the 3'-UTR of CDKN1B/p27 mRNA, inducing a local conformational change that exposes miRNA- binding sites, promoting association of miR-221 and miR-222, efficient suppression of CDKN1B/p27 expression, and rapid entry to the cell cycle (PubMed:20818387). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (PubMed:22345517). Involved in neuronal functions by regulating ATXN1 mRNA levels: acts by binding to the 3'-UTR of ATXN1 transcripts, leading to their down-regulation independently of the miRNA machinery (PubMed:25768905). Plays a role in cytoplasmic sensing of viral infection (PubMed:25340845). In testis, acts as a post-transcriptional regulator of spermatogenesis by binding to the 3'-UTR of mRNAs coding for regulators of p53/TP53. Involved in embryonic stem cell renewal by facilitating the exit from the ground state: acts by targeting mRNAs coding for naive pluripotency transcription factors and accelerates their down-regulation at the onset of differentiation (By similarity). {ECO:0000250|UniProtKB:Q80U78, ECO:0000269|PubMed:18328718, ECO:0000269|PubMed:18776931, ECO:0000269|PubMed:20818387, ECO:0000269|PubMed:20860814, ECO:0000269|PubMed:21397187, ECO:0000269|PubMed:21572425, ECO:0000269|PubMed:21653694, ECO:0000269|PubMed:22345517, ECO:0000269|PubMed:22955276, ECO:0000269|PubMed:25340845, ECO:0000269|PubMed:25768905}.; . TISSUE SPECIFICITY: Expressed in brain, heart, kidney, muscle, intestine and stomach. Not expressed in cerebellum, corpus callosum, caudate nucleus, hippocampus, medulla oblongata and putamen. Expressed in all fetal tissues tested. {ECO:0000269|PubMed:12459267}.; ovary;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;oral cavity;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;amnion;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;subthalamic nucleus;superior cervical ganglion;placenta;prefrontal cortex;globus pallidus;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.36215 0.16306 -1.017713296 8.103326256 75.49142 1.81780 PUM2 0.999922863782349 7.71362174803649e-05 1.7052775576572e-13 pumilio RNA binding family member 2 FUNCTION: Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE) (, PubMed:21397187). Mediates post- transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (PubMed:22955276). Also mediates deadenylation- independent repression by promoting accessibility of miRNAs (PubMed:18776931, PubMed:22345517). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (PubMed:22345517). Plays a role in cytoplasmic sensing of viral infection (PubMed:25340845). May regulate DCUN1D3 mRNA levels (PubMed:25349211). May support proliferation and self- renewal of stem cells. {ECO:0000269|PubMed:18776931, ECO:0000269|PubMed:21397187, ECO:0000269|PubMed:22345517, ECO:0000269|PubMed:22955276, ECO:0000269|PubMed:25340845, ECO:0000269|PubMed:25349211}.; . TISSUE SPECIFICITY: Expressed in male germ cells of adult testis (at protein level). Highly expressed in testis and ovary. Predominantly expressed in stem cells and germ cells. Expressed at lower level in brain, heart, kidney, liver, muscle, placenta, intestine and stomach Expressed in cerebellum, corpus callosum, caudate nucleus, hippocampus, medulla oblongata and putamen. Expressed in all fetal tissues tested. {ECO:0000269|PubMed:12459267, ECO:0000269|PubMed:12511597, ECO:0000269|PubMed:19168546}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;spinal cord;adrenal cortex;blood;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;oral cavity;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.76937 0.09464 -0.844966979 11.1759849 35.7553 1.07514 PUM3 . . . pumilio RNA binding family member 3 FUNCTION: Inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress (PubMed:21266351). Binds to double-stranded RNA or DNA without sequence specificity (PubMed:25512524). Involved in development of the eye and of primordial germ cells (By similarity). {ECO:0000250|UniProtKB:X1WGX5, ECO:0000269|PubMed:21266351, ECO:0000269|PubMed:25512524}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:7584026}.; . . 0.65344 0.11829 0.472145421 78.85114414 . . PURA 0.845099483885208 0.152118919923745 0.00278159619104648 purine-rich element binding protein A FUNCTION: This is a probable transcription activator that specifically binds the purine-rich single strand of the PUR element located upstream of the MYC gene. May play a role in the initiation of DNA replication and in recombination.; DISEASE: Mental retardation, autosomal dominant 31 (MRD31) [MIM:616158]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD31 patients manifest neonatal hypotonia, encephalopathy with or without epilepsy, and severe developmental delay. {ECO:0000269|PubMed:25342064, ECO:0000269|PubMed:25439098}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;medulla oblongata;occipital lobe;superior cervical ganglion;olfactory bulb;cerebellum peduncles;temporal lobe;pons;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;pituitary;cerebellum; 0.66003 0.19986 -0.119252484 44.53880632 2.10685 0.06871 PURB 0.605935032790202 0.38533387714003 0.0087310900697682 purine-rich element binding protein B FUNCTION: Has capacity to bind repeated elements in single- stranded DNA such as the purine-rich single strand of the PUR element located upstream of the MYC gene. Plays a role in the control of vascular smooth muscle (VSM) alpha-actin gene transcription as repressor in myoblasts and fibroblasts. Participates in transcriptional and translational regulation of alpha-MHC expression in cardiac myocytes by binding to the purine- rich negative regulatory (PNR) element. Modulates constitutive liver galectin-3 gene transcription by binding to its promoter. May play a role in the dendritic transport of a subset of mRNAs (By similarity). {ECO:0000250, ECO:0000269|PubMed:1448097}.; . TISSUE SPECIFICITY: Expressed in myocardium of heart failure patients. {ECO:0000269|PubMed:12933792}.; . . 0.72666 . . . 11.13168 0.40295 PURG 0.934741136588781 0.0649560089181463 0.000302854493073012 purine-rich element binding protein G . . TISSUE SPECIFICITY: Isoform 1 is expressed in testis and glioblastoma. Isoform 2 is expressed in fetal lung. {ECO:0000269|PubMed:12034829}.; unclassifiable (Anatomical System);prostate;lung;whole body;ovary;hippocampus;testis;brain;skeletal muscle;cerebellum; superior cervical ganglion;ciliary ganglion;atrioventricular node;parietal lobe; 0.26554 . -0.117432389 44.89266336 164.41181 2.80008 PUS1 0.0199884225458712 0.902842564291872 0.0771690131622572 pseudouridylate synthase 1 FUNCTION: Converts specific uridines to PSI in a number of tRNA substrates. Acts on positions 27/28 in the anticodon stem and also positions 34 and 36 in the anticodon of an intron containing tRNA. Involved in regulation of nuclear receptor activity possibly through pseudouridylation of SRA1 RNA (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. High levels of expression found in brain and skeletal muscle. {ECO:0000269|PubMed:15108122}.; medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;bone;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; skeletal muscle; 0.48675 0.13402 -0.754958418 13.57631517 283.00448 3.60121 PUS3 1.0865601617407e-05 0.804937062890329 0.195052071508054 pseudouridylate synthase 3 FUNCTION: Formation of pseudouridine at position 39 in the anticodon stem and loop of transfer RNAs. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;muscle;pharynx;colon;skeletal muscle;uterus;pancreas;lung;endometrium;nasopharynx;bone;placenta;pituitary gland;alveolus;testis;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22575 0.11019 0.244401822 69.50931824 2056.00354 8.35566 PUS7 2.16505288475568e-05 0.995004700916779 0.00497364855437355 pseudouridylate synthase 7 (putative) . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;gum;bone;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;oral cavity;urinary;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;macula lutea;visual apparatus;hypopharynx;duodenum;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.83216 0.10907 -0.578583623 18.71903751 94.66396 2.09617 PUS7L 1.56980935543342e-06 0.638681277504257 0.361317152686388 pseudouridylate synthase 7 like . . . unclassifiable (Anatomical System);ovary;heart;salivary gland;pharynx;colon;blood;skin;skeletal muscle;bone marrow;breast;uterus;prostate;lung;placenta;visual apparatus;hippocampus;liver;testis;germinal center;kidney;brain;pineal gland;bladder; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.21355 . 0.646696306 84.12361406 1681.76546 7.56030 PUS7P1 . . . pseudouridylate synthase 7 pseudogene 1 . . . . . . . . . . . PUS10 5.26981477460816e-10 0.592799587286489 0.40720041218653 pseudouridylate synthase 10 FUNCTION: Pseudouridylate synthases catalyze pseudouridination of structural RNAs, including transfer, ribosomal, and splicing RNAs. PUS10 catalyzes the formation of the universal psi55 in the GC loop of transfer RNAs (Probable). Modulator of TRAIL-induced cell death via activation of procaspase 8 and BID cleavage. Required for the progression of the apoptotic signal through intrinsic mitochondrial cell death. {ECO:0000269|PubMed:14527409, ECO:0000269|PubMed:19712588, ECO:0000305}.; . . unclassifiable (Anatomical System);colon;skeletal muscle;uterus;lung;endometrium;placenta;liver;testis;spleen;germinal center;kidney;brain;stomach; . 0.26322 0.10019 -0.490397599 22.50530786 145.53333 2.62835 PUSL1 6.58681964674524e-12 0.00468747091109371 0.995312529082319 pseudouridylate synthase-like 1 . . . . . 0.17782 0.14233 . . 736.17658 5.38431 PVALB 0.0678701921991012 0.734822596885443 0.197307210915456 parvalbumin FUNCTION: In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.; . . unclassifiable (Anatomical System);ovary;hypothalamus;placenta;liver;parathyroid;spleen;blood;kidney;brain;retina; dorsal root ganglion;whole brain;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;subthalamic nucleus;globus pallidus;ciliary ganglion;kidney;cingulate cortex;parietal lobe;cerebellum; 0.40074 0.36296 0.25917371 70.05779665 115.60983 2.33849 PVR 5.51101308161619e-07 0.418836433455441 0.581163015443251 poliovirus receptor FUNCTION: Mediates NK cell adhesion and triggers NK cell effector functions. Binds two different NK cell receptors: CD96 and CD226. These interactions accumulates at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytoxicity of activated NK cells. May also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Plays a role in mediating tumor cell invasion and migration. {ECO:0000269|PubMed:15471548, ECO:0000269|PubMed:15607800}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;bone;iris;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;mesenchyma;epididymis;placenta;macula lutea;visual apparatus;hippocampus;alveolus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.08465 0.15428 0.799205007 87.58551545 138.8255 2.56696 PVRIG 0.0010018919897152 0.816895436372789 0.182102671637496 poliovirus receptor related immunoglobulin domain containing . . . unclassifiable (Anatomical System);lymphoreticular;lymph node;heart;muscle;blood;bone marrow;breast;prostate;pancreas;lung;epididymis;larynx;placenta;testis;head and neck;spleen;brain;mammary gland;stomach;cerebellum;thymus; . 0.06433 . 0.819433854 87.98655343 229.23449 3.27253 PVRIG2P . . . poliovirus receptor related immunoglobulin domain containing 2, pseudogene . . . . . . . . . . . PVRL3-AS1 . . . PVRL3 antisense RNA 1 . . . . . . . . . . . PVT1 . . . Pvt1 oncogene (non-protein coding) . . . . . . . . . . . PWAR1 . . . Prader Willi/Angelman region RNA 1 . . . . . . . . . . . PWAR4 . . . Prader Willi/Angelman region RNA 4 . . . . . . . . . . . PWAR5 . . . Prader Willi/Angelman region RNA 5 . . . . . . . . . . . PWAR6 . . . Prader Willi/Angelman region RNA 6 . . . . . . . . . . . PWARSN . . . Prader Willi/Angelman region RNA, SNRPN neighbor . . . . . . . . . . . PWP1 1.8549631577177e-05 0.993790248797399 0.00619120157102439 PWP1 homolog, endonuclein FUNCTION: May play an important role in cell growth and/or transcription.; . TISSUE SPECIFICITY: High levels seen in the placenta, skeletal muscle, kidney and pancreas while lower levels were seen in the heart, brain and lung.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.50261 . -0.044015879 50.44821892 685.05733 5.22612 PWP2 0.875422848057892 0.124577040368151 1.11573956858731e-07 PWP2 periodic tryptophan protein homolog (yeast) . . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;oesophagus;endometrium;larynx;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; amygdala; 0.75950 0.11568 -0.562239385 19.06699693 373.23568 4.07549 PWRN1 . . . Prader-Willi region non-protein coding RNA 1 . . . . . . . . . . . PWRN2 . . . Prader-Willi region non-protein coding RNA 2 . . . . . . . . . . . PWRN3 . . . Prader-Willi region non-protein coding RNA 3 . . . . . . . . . . . PWRN4 . . . Prader-Willi region non-protein coding RNA 4 . . . . . . . . . . . PWWP2A 0.920215651464739 0.0796812531599757 0.000103095375284973 PWWP domain containing 2A . . . unclassifiable (Anatomical System);meninges;heart;colon;skin;uterus;breast;prostate;pia mater;lung;visual apparatus;hippocampus;liver;testis;spleen;dura mater;germinal center;brain; superior cervical ganglion;temporal lobe;ciliary ganglion;atrioventricular node;skeletal muscle; 0.15294 . -0.003562597 53.72729417 395.64117 4.17888 PWWP2AP1 . . . PWWP domain containing 2A pseudogene 1 . . . . . . . . . . . PWWP2B 0.71615388692527 0.28067221102082 0.00317390205391006 PWWP domain containing 2B . . . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;blood;choroid;skin;skeletal muscle;uterus;pancreas;prostate;lung;endometrium;bone;placenta;visual apparatus;testis;cervix;kidney;brain;pineal gland;mammary gland; superior cervical ganglion;liver; 0.25140 . . . 62.38763 1.61280 PXDC1 0.550017216808143 0.436396901582905 0.0135858816089522 PX domain containing 1 . . . . . 0.32678 . -0.029247611 51.40363293 34.62039 1.05641 PXDN 2.03602830062533e-05 0.999934089382599 4.55503343943967e-05 peroxidasin FUNCTION: Displays low peroxidase activity and is likely to participate in H(2)O(2) metabolism and peroxidative reactions in the cardiovascular system. Plays a role in extracellular matrix formation. {ECO:0000269|PubMed:18929642, ECO:0000269|PubMed:19590037}.; DISEASE: Corneal opacification with other ocular anomalies (COPOA) [MIM:269400]: An ocular disease characterized by sclerocornea associated with other ocular anomalies, such as cataract, microcornea, microphthalmia, and anterior segment dysgenesis. Sclerocornea is a primary anomaly in which scleralization of a peripheral part of the cornea, or the entire corneal tissue, occurs. In the peripheral type of sclerocornea, the affected area is vascularized with regular arcades of superficial scleral vessels. In total sclerocornea, the entire cornea is opaque and vascularized. {ECO:0000269|PubMed:21907015}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at higher levels in heart, lung, ovary, spleen, intestine and placenta, and at lower levels in liver, colon, pancreas, kidney, thymus, skeletal muscle and prostate. Expressed in tumors such as melanoma, breast cancer, ovarian cancer and glioblastoma. A shorter form probably lacking the signal sequence is found in testis and in EB1 cells undergoing p53/TP53-dependent apoptosis. {ECO:0000269|PubMed:10441517, ECO:0000269|PubMed:11103812, ECO:0000269|PubMed:18929642, ECO:0000269|PubMed:19590037}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;larynx;gum;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;uterus corpus;superior cervical ganglion;adipose tissue;smooth muscle;lung;placenta;ciliary ganglion;fetal lung;atrioventricular node;trigeminal ganglion; 0.44329 0.10322 -1.512251235 3.479594244 529.85594 4.69745 PXDNL 1.93677107008286e-27 0.000599485814575364 0.999400514185425 peroxidasin like FUNCTION: Isoform PMR1: Endonuclease selectively degrading some target mRNAs while they are engaged by translating ribosomes, among which albumin and beta-globin mRNAs. {ECO:0000269|PubMed:22543864}.; . TISSUE SPECIFICITY: the 57 kDa isoform PMR1 is the only form detected at protein levels in human cell lines. {ECO:0000269|PubMed:22543864}.; unclassifiable (Anatomical System);lung;heart;testis; dorsal root ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . . 2.732433216 98.95022411 6585.72871 17.14983 PXK 0.932144255708936 0.0678556295748875 1.14716176845592e-07 PX domain containing serine/threonine kinase like FUNCTION: Binds to and modulates brain Na,K-ATPase subunits ATP1B1 and ATP1B3 and may thereby participate in the regulation of electrical excitability and synaptic transmission. May not display kinase activity. {ECO:0000250|UniProtKB:Q8BX57, ECO:0000303|PubMed:16142408}.; . TISSUE SPECIFICITY: Widely expressed in all tissues examined except in heart. Isoform 1 is expressed in high levels in the brain, skeletal muscle, spleen and testis. Isoform 7 expression has yet to be demonstrated. {ECO:0000269|PubMed:16142408}.; colon;choroid;skin;bone marrow;uterus;prostate;whole body;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;prefrontal cortex;globus pallidus;atrioventricular node;pons;parietal lobe;cerebellum; 0.13995 0.09839 0.266447942 70.5826846 2672.1939 9.71802 PXMP2 0.0288943082845666 0.802483496925054 0.168622194790379 peroxisomal membrane protein 2 FUNCTION: Seems to be involved in pore-forming activity and may contribute to the unspecific permeability of the peroxisomal membrane.; . . ovary;salivary gland;intestine;colon;fovea centralis;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;aorta; liver;kidney; 0.16468 0.11275 -0.427900189 25.14744043 50.72259 1.40323 PXMP4 0.604956427154611 0.386241880079323 0.00880169276606649 peroxisomal membrane protein 4 . . TISSUE SPECIFICITY: Expressed in normal prostate epithelial cells, and androgen-sensitive prostate adenocarcinoma cells. Not expressed in androgen-insensitive prostate adenocarcinoma cells. {ECO:0000269|PubMed:14712230}.; ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;prostate;thyroid;germinal center;brain;bladder;unclassifiable (Anatomical System);lacrimal gland;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;hippocampus;visual apparatus;alveolus;liver;kidney; dorsal root ganglion;superior cervical ganglion;testis;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.10380 0.10278 0.527368849 80.73248408 67.7056 1.70224 PXN 0.00656841085846847 0.97461633472968 0.0188152544118515 paxillin FUNCTION: Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion).; . . smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;larynx;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;placenta;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.19830 0.61852 -0.398573136 26.92852088 77.44992 1.85032 PXN-AS1 . . . PXN antisense RNA 1 . . . . . . . . . . . PXT1 1.3167645760551e-05 0.121287572051031 0.878699260303208 peroxisomal, testis specific 1 . . . . . 0.32904 . 0.257356108 69.83368719 1721.89347 7.65502 PXYLP1 . . . 2-phosphoxylose phosphatase 1 FUNCTION: Responsible for the 2-O-dephosphorylation of xylose in the glycosaminoglycan-protein linkage region of proteoglycans thereby regulating the amount of mature glycosaminoglycan (GAG) chains. Sulfated glycosaminoglycans (GAGs), including heparan sulfate and chondroitin sulfate, are synthesized on the so-called common GAG-protein linkage region (GlcUAbeta1-3Galbeta1-3Galbeta1- 4Xylbeta1-O-Ser) of core proteins, which is formed by the stepwise addition of monosaccharide residues by the respective specific glycosyltransferases. Xylose 2-O-dephosphorylation during completion of linkage region formation is a prerequisite for the initiation and efficient elongation of the repeating disaccharide region of GAG chains. {ECO:0000269|PubMed:24425863}.; . TISSUE SPECIFICITY: Widely expressed. Strongly expressed in spleen, fetal liver, moderately in placenta, pancreas, kidney, thymus and colon. {ECO:0000269|PubMed:24425863}.; . . 0.18199 . -0.378346116 28.01368247 . . PYCARD 0.0165035542141555 0.706850816569356 0.276645629216489 PYD and CARD domain containing FUNCTION: Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. Isoform 2 may have a regulating effect on the function as inflammasome adapter. Isoform 3 seems to inhibit inflammasome- mediated maturation of interleukin-1 beta. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. {ECO:0000269|PubMed:11103777, ECO:0000269|PubMed:12486103, ECO:0000269|PubMed:12646168, ECO:0000269|PubMed:14499617, ECO:0000269|PubMed:14730312, ECO:0000269|PubMed:15030775, ECO:0000269|PubMed:16585594, ECO:0000269|PubMed:16964285, ECO:0000269|PubMed:16982856, ECO:0000269|PubMed:17349957, ECO:0000269|PubMed:17599095, ECO:0000269|PubMed:19158675, ECO:0000269|PubMed:19158676, ECO:0000269|PubMed:19234215, ECO:0000269|PubMed:19494289, ECO:0000269|PubMed:21487011, ECO:0000269|PubMed:22732093}.; . TISSUE SPECIFICITY: Widely expressed at low levels. Detected in peripheral blood leukocytes, lung, small intestine, spleen, thymus, colon and at lower levels in placenta, liver and kidney. Very low expression in skeletal muscle, heart and brain. Detected in the leukemia cell lines HL-60 and U-937, but not in Jurkat T- cell lymphoma and Daudi Burkitt's lymphoma. Detected in the melanoma cell line WM35, but not in WM793. Not detected in HeLa cervical carcinoma cells and MOLT-4 lymphocytic leukemia cells.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;thymus; lung;white blood cells;whole blood; 0.44086 0.17300 0.125076652 62.7388535 7.12018 0.26554 PYCARD-AS1 . . . PYCARD antisense RNA 1 . . . . . . . . . . . PYCR1 0.000359028805830681 0.609776662397893 0.389864308796276 pyrroline-5-carboxylate reductase 1 FUNCTION: Housekeeping enzyme that catalyzes the last step in proline biosynthesis. Can utilize both NAD and NADP, but has higher affinity for NAD. Involved in the cellular response to oxidative stress. {ECO:0000269|PubMed:16730026, ECO:0000269|PubMed:19648921}.; DISEASE: Cutis laxa, autosomal recessive, 2B (ARCL2B) [MIM:612940]: A disorder characterized by an excessive congenital skin wrinkling, a large fontanelle with delayed closure, a typical facial appearance with downslanting palpebral fissures, a general connective tissue weakness, and varying degrees of growth and developmental delay and neurological abnormalities. Patients do not manifest metabolic abnormalities. {ECO:0000269|PubMed:19576563, ECO:0000269|PubMed:19648921}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cutis laxa, autosomal recessive, 3B (ARCL3B) [MIM:614438]: A disorder characterized by an aged appearance with distinctive facial features, sparse hair, ophthalmologic abnormalities, intrauterine growth retardation, and cutis laxa. {ECO:0000269|PubMed:19648921, ECO:0000269|PubMed:22052856}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;endometrium;gum;bone;iris;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; tumor;skeletal muscle; 0.13959 0.26255 -0.534490515 20.70063694 33.50339 1.03437 PYCR2 0.00506294198593209 0.88739642885157 0.107540629162498 pyrroline-5-carboxylate reductase family member 2 FUNCTION: Housekeeping enzyme that catalyzes the last step in proline biosynthesis. In some cell types, such as erythrocytes, its primary function may be the generation of NADP(+). Can utilize both NAD and NADP. Has higher affinity for NADP, but higher catalytic efficiency with NADH (PubMed:2722838, PubMed:6894153). Involved in cellular response to oxidative stress (PubMed:25865492). {ECO:0000269|PubMed:25865492, ECO:0000269|PubMed:2722838, ECO:0000269|PubMed:6894153}.; . TISSUE SPECIFICITY: Detected in erythrocytes (at protein level) (PubMed:2722838, PubMed:6894153). Expressed in fetal brain (PubMed:25865492). {ECO:0000269|PubMed:25865492, ECO:0000269|PubMed:2722838, ECO:0000269|PubMed:6894153}.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;thyroid;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;hippocampus;macula lutea;visual apparatus;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;atrioventricular node; 0.20134 0.16159 -0.714505427 14.4019816 11.30253 0.40661 PYCRL 0.0171284135571899 0.889881785127401 0.0929898013154091 pyrroline-5-carboxylate reductase-like . . . medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;pancreas;lung;mesenchyma;macula lutea;hippocampus;cervix;kidney;mammary gland; superior cervical ganglion;trigeminal ganglion;skeletal muscle;cingulate cortex;parietal lobe; 0.09359 0.12576 -0.023789244 52.09365416 3746.12345 11.97203 PYDC1 0.465269917823027 0.445131040781027 0.0895990413959461 PYD (pyrin domain) containing 1 FUNCTION: Associates with PYCARD/ASC and modulates its ability to collaborate with MEFV/pyrin and NLRP3/cryopyrin in NF-kappa-B and pro-caspase-1 activation. Suppresses kinase activity of NF-kappa-B inhibitor kinase (IKK) complex, expression of NF-kappa-B inducible genes and inhibits NF-kappa-B activation by cytokines and LPS. {ECO:0000269|PubMed:12656673, ECO:0000269|PubMed:24871464}.; . TISSUE SPECIFICITY: Predominantly expressed in monocytes, macrophages and granulocytes. {ECO:0000269|PubMed:12656673}.; unclassifiable (Anatomical System);heart; cerebellum; 0.05659 0.10484 0.235309407 68.71903751 6.0693 0.22957 PYDC2 0.0221705221528128 0.53133444259196 0.446495035255227 pyrin domain containing 2 FUNCTION: May play a role in innate immunity by disrupting the interaction between PYCARD and NLRP3, thereby regulating the NLRP3 inflammasome (PubMed:17339483, PubMed:17178784). May also inhibit NF-kappa-B signaling distally by affecting the nuclear accumulation of RELA (PubMed:17339483, PubMed:24871464). {ECO:0000269|PubMed:17178784, ECO:0000269|PubMed:17339483, ECO:0000269|PubMed:24871464}.; . TISSUE SPECIFICITY: Predominantly expressed in peripheral blood. Weakly expressed in testis. {ECO:0000269|PubMed:17339483}.; . . . 0.08591 . . 6.81187 0.25187 PYGB 4.76485243414978e-07 0.997985913777979 0.00201360973677787 phosphorylase, glycogen; brain FUNCTION: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.; . . myocardium;adrenal medulla;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;iris;testis;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;muscle;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;head and neck;cervix;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;cerebellum peduncles; 0.08143 0.44857 -1.455091209 3.886529842 3164.71877 10.72002 PYGL 1.31337485605572e-09 0.98453943941942 0.0154605592672049 phosphorylase, glycogen, liver FUNCTION: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.; DISEASE: Glycogen storage disease 6 (GSD6) [MIM:232700]: A metabolic disorder characterized by mild to moderate hypoglycemia, mild ketosis, growth retardation, and prominent hepatomegaly. Heart and skeletal muscle are not affected. {ECO:0000269|PubMed:9529348}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;skeletal muscle; 0.24234 0.42342 0.205769367 67.49823071 1159.70276 6.48168 PYGM 2.61594230276409e-08 0.994722305217651 0.00527766862292549 phosphorylase, glycogen, muscle FUNCTION: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.; DISEASE: Glycogen storage disease 5 (GSD5) [MIM:232600]: A metabolic disorder resulting in myopathy characterized by exercise intolerance, cramps, muscle weakness and recurrent myoglobinuria. {ECO:0000269|PubMed:10382911, ECO:0000269|PubMed:10382912, ECO:0000269|PubMed:10417800, ECO:0000269|PubMed:10590419, ECO:0000269|PubMed:10681080, ECO:0000269|PubMed:10714589, ECO:0000269|PubMed:10899452, ECO:0000269|PubMed:11706962, ECO:0000269|PubMed:12031624, ECO:0000269|PubMed:7603523, ECO:0000269|PubMed:8316268, ECO:0000269|PubMed:8535454, ECO:0000269|PubMed:9506549}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;retina;prostate;whole body;larynx;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;muscle;skeletal muscle;greater omentum;pancreas;lung;placenta;hippocampus;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; tongue;thyroid;skeletal muscle; 0.50808 0.12819 -0.187428709 39.31351734 839.0753 5.67294 PYGO1 0.956651521929469 0.0432397635850281 0.000108714485503129 pygopus family PHD finger 1 FUNCTION: Involved in signal transduction through the Wnt pathway.; . . cervix; superior cervical ganglion;testis - interstitial;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08925 0.11665 0.196671391 67.19155461 345.47846 3.94247 PYGO2 0.923104365059159 0.0764372565526476 0.000458378388193136 pygopus family PHD finger 2 FUNCTION: Involved in signal transduction through the Wnt pathway.; . . . . 0.14273 0.11620 -0.337894035 30.37272942 73.78634 1.79491 PYHIN1 0.000917067605008323 0.940164858068146 0.0589180743268459 pyrin and HIN domain family member 1 FUNCTION: Major mediator of the tumor suppressor activity of IFN in breast cancer cells. Promotes ubiquitination and subsequent degradation of MDM2, which leads to p53/TP53 stabilization. Promotes ubiquitination and subsequent degradation of HDAC1, which in turn enhances maspin expression, and impairs invasive activity of cancer cells. {ECO:0000269|PubMed:16479015, ECO:0000269|PubMed:18247378}.; . TISSUE SPECIFICITY: Expressed in spleen, lymph node and peripheral blood leukocytes, and at lower levels in thymus, bone marrow and fetal liver. Down-regulated in breast tumors. {ECO:0000269|PubMed:15122330}.; . . 0.03651 0.06141 7.61E-05 53.98089172 326.8894 3.84451 PYHIN5P . . . pyrin and HIN domain family member 5, pseudogene . . . . . . . . . . . PYM1 . . . PYM homolog 1, exon junction complex associated factor FUNCTION: Key regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon-exon junction on mRNAs and serves as a positional landmarks for the intron exon structure of genes and directs post- transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Acts as a EJC disassembly factor, allowing translation-dependent EJC removal and recycling by disrupting mature EJC from spliced mRNAs. Its association with the 40S ribosomal subunit probably prevents a translation-independent disassembly of the EJC from spliced mRNAs, by restricting its activity to mRNAs that have been translated. Interferes with NMD and enhances translation of spliced mRNAs, probably by antagonizing EJC functions. May bind RNA; the relevance of RNA-binding remains unclear in vivo, RNA-binding was detected by PubMed:14968132, while PubMed:19410547 did not detect RNA-binding activity independently of the EJC. {ECO:0000269|PubMed:18026120, ECO:0000269|PubMed:19410547}.; . . . . 0.15471 0.12127 -0.163345027 41.24793583 . . PYROXD1 3.50579116851114e-07 0.787764597944416 0.212235051476468 pyridine nucleotide-disulphide oxidoreductase domain 1 . . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;atrium;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;alveolus;hypopharynx;liver;cervix;head and neck;kidney;mammary gland;aorta;stomach; . 0.08320 0.09323 -0.534490515 20.70063694 40.64742 1.19130 PYROXD2 8.99028044954632e-08 0.912323472695686 0.087676437401509 pyridine nucleotide-disulphide oxidoreductase domain 2 FUNCTION: Probable oxidoreductase. {ECO:0000250}.; . . . . 0.11303 0.10253 0.892856963 89.28992687 4275.74581 13.00098 PYURF . . . PIGY upstream reading frame . . . . . . . . . 9.96946 0.36511 PYY 0.0544166347481236 0.702632110470612 0.242951254781264 peptide YY FUNCTION: This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility.; . . unclassifiable (Anatomical System); . 0.12649 . 0.523736627 80.45529606 109.27527 2.27016 PYY2 . . . peptide YY, 2 (pseudogene) . . TISSUE SPECIFICITY: Expressed mainly in the testis and prostate. {ECO:0000269|PubMed:10756099}.; . . 0.16799 . . . . . PYY3 . . . peptide YY, 3 (pseudogene) . . . . . 0.16674 0.09533 . . . . PZP 1.35183771709263e-21 0.596764545179065 0.403235454820935 pregnancy-zone protein FUNCTION: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase.; . TISSUE SPECIFICITY: Plasma. Prominent constituent of late- pregnancy sera.; lymphoreticular;lung;endometrium;hippocampus;liver;testis;cervix; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13604 . 0.262615756 70.26421326 6488.1693 16.89264 QARS 8.78969829865226e-08 0.999063845605078 0.000936066497938853 glutaminyl-tRNA synthetase FUNCTION: Plays a critical role in brain development. {ECO:0000269|PubMed:24656866}.; . TISSUE SPECIFICITY: Highly expressed in fetal cerebral cortex, particularly in the ventricular zone, inner subventricular zone, outer subventricular zone, and cortical plate. {ECO:0000269|PubMed:24656866}.; lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;heart;liver;kidney; 0.24405 0.18932 -0.641086234 16.6784619 211.23017 3.13464 QDPR 0.0658164274641498 0.919602835387295 0.0145807371485548 quinoid dihydropteridine reductase FUNCTION: The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases.; DISEASE: Hyperphenylalaninemia, BH4-deficient, C (HPABH4C) [MIM:261630]: Rare autosomal recessive disorder characterized by hyperphenylalaninemia and severe neurologic symptoms (malignant hyperphenylalaninemia) including axial hypotonia and truncal hypertonia, abnormal thermogenesis, and microcephaly. These signs are attributable to depletion of the neurotransmitters dopamine and serotonin, whose syntheses are controlled by tryptophan and tyrosine hydroxylases that use BH-4 as cofactor. Patients do not respond to phenylalanine-restricted diet. HPABH4C is lethal if untreated. {ECO:0000269|PubMed:10408783, ECO:0000269|PubMed:11153907, ECO:0000269|PubMed:2116088, ECO:0000269|PubMed:8326489, ECO:0000269|PubMed:9744478}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;thyroid;bladder;brain;heart;cartilage;spinal cord;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;liver;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.16310 0.40344 -0.383807564 27.41802312 13.56109 0.49280 QKI 0.963163356453829 0.036821914188707 1.47293574644315e-05 QKI, KH domain containing, RNA binding FUNCTION: RNA-binding protein that plays a central role in myelinization (PubMed:16641098). Binds to the 5'-NACUAAY-N(1,20)- UAAY-3' RNA core sequence. Regulates target mRNA stability (PubMed:23630077). In addition, acts by regulating pre-mRNA splicing, mRNA export and protein translation. Required to protect and promote stability of mRNAs such as MBP and CDKN1B. Regulator of oligodendrocyte differentiation and maturation in the brain that may play a role in myelin and oligodendrocyte dysfunction in schizophrenia (PubMed:16641098). Participates in mRNA transport by regulating the nuclear export of MBP mRNA. Also involved in regulation of mRNA splicing of MAG pre-mRNA. Acts as a translational repressor (By similarity). {ECO:0000250|UniProtKB:Q9QYS9, ECO:0000269|PubMed:16641098, ECO:0000269|PubMed:23630077}.; . TISSUE SPECIFICITY: Expressed in the frontal cortex of brain. Down-regulated in the brain of schizophrenic patients. {ECO:0000269|PubMed:16342280}.; lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;amygdala;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;atrium;larynx;bone;testis;dura mater;pineal gland;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;whole brain;medulla oblongata;superior cervical ganglion;occipital lobe;thalamus;olfactory bulb;pons;caudate nucleus;subthalamic nucleus;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;amygdala;testis - interstitial;hypothalamus;spinal cord;atrioventricular node;skeletal muscle;fetal brain;prefrontal cortex;appendix;parietal lobe; 0.28593 0.19768 -0.229483771 36.86010852 6.7048 0.24740 QPCT 1.87382648510695e-08 0.23697958575002 0.763020395511715 glutaminyl-peptide cyclotransferase FUNCTION: Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides. {ECO:0000269|PubMed:15063747, ECO:0000269|PubMed:18486145, ECO:0000269|PubMed:21288892}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;endometrium;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; adrenal gland; 0.34618 0.26744 0.308721233 72.59966973 2893.94032 10.19019 QPCTL 0.000261539862441849 0.776051134035613 0.223687326101945 glutaminyl-peptide cyclotransferase-like FUNCTION: Responsible for the biosynthesis of pyroglutamyl peptides. {ECO:0000269|PubMed:18486145, ECO:0000269|PubMed:21288892}.; . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;prostate;frontal lobe;larynx;placenta;visual apparatus;liver;cervix;head and neck;kidney;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node; 0.25441 0.10687 0.286674996 71.49681529 373.82761 4.07890 QPRT 0.593365505826568 0.39696090168364 0.00967359248979238 quinolinate phosphoribosyltransferase FUNCTION: Involved in the catabolism of quinolinic acid (QA). {ECO:0000269|PubMed:17868694}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;testis;bladder;brain;unclassifiable (Anatomical System);adrenal cortex;pharynx;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; adrenal gland;liver;kidney; 0.17965 0.17866 0.527368849 80.73248408 560.73473 4.81025 QRFP 0.00762334929561819 0.545758519930189 0.446618130774193 pyroglutamylated RFamide peptide FUNCTION: Stimulates feeding behavior, metabolic rate and locomotor activity and increases blood pressure. May have orexigenic activity. May promote aldosterone secretion by the adrenal gland (By similarity). {ECO:0000250, ECO:0000269|PubMed:12960173, ECO:0000269|PubMed:14657341}.; . TISSUE SPECIFICITY: Expressed widely in the brain with highest expression levels in the cerebellum, medulla, pituitary, retina, vestibular nucleus, and white matter. Also expressed in the bladder, colon, coronary artery, parathyroid gland, prostate, testis, and thyroid. {ECO:0000269|PubMed:12714592}.; cartilage; . 0.09694 0.08182 0.861712133 88.6883699 120.58026 2.39285 QRFPR 1.86675403550802e-12 0.0158769623319894 0.984123037666144 pyroglutamylated RFamide peptide receptor FUNCTION: Receptor for the orexigenic neuropeptide QRFP. The activity of this receptor is mediated by G proteins that modulate adenylate cyclase activity and intracellular calcium levels. {ECO:0000269|PubMed:12960173}.; . TISSUE SPECIFICITY: Expressed widely in the brain with high levels in the hypothalamus, trigeminal ganglia and vestibular neurons, and moderate levels in the amygdala, cortex, pituitary, hippocampus, thalamus, caudate nucleus and medulla oblongata. In peripheral tissues, expressed at high levels in the retina and at moderate levels in the heart, kidney, testis and thyroid. {ECO:0000269|PubMed:11574155, ECO:0000269|PubMed:12714592}.; lung;testis;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04574 0.07907 1.618658506 95.99551781 4171.15062 12.82724 QRICH1 0.996069748046578 0.00393023975053419 1.2202888187802e-08 glutamine rich 1 . . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;iris;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; testis - interstitial;testis - seminiferous tubule;testis;cerebellum; 0.30629 0.07512 -0.47017169 23.25430526 223.53402 3.23309 QRICH2 1.21935180720808e-18 0.394563967910032 0.605436032089968 glutamine rich 2 . . . unclassifiable (Anatomical System);lung;frontal lobe;cerebral cortex;placenta;liver;testis;colon;spleen;brain; trigeminal ganglion; 0.12708 0.06942 1.670085733 96.31988677 13082.37783 24.46226 QRSL1 8.77942908077522e-05 0.984069782805781 0.0158424229034116 glutaminyl-tRNA synthase (glutamine-hydrolyzing)-like 1 FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_03150, ECO:0000269|PubMed:19805282}.; . . . . 0.09904 0.19316 0.420771676 77.15852795 836.41184 5.66312 QRSL1P1 . . . glutaminyl-tRNA synthase (glutamine-hydrolyzing)-like 1 pseudogene 1 . . . . . . . . . . . QRSL1P2 . . . glutaminyl-tRNA synthase (glutamine-hydrolyzing)-like 1 pseudogene 2 . . . . . . . . . . . QRSL1P3 . . . glutaminyl-tRNA synthase (glutamine-hydrolyzing)-like 1 pseudogene 3 . . . . . . . . . . . QSER1 0.999935658653166 6.43413467238554e-05 1.09627942007305e-13 glutamine and serine rich 1 . . . unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;colon;blood;skin;skeletal muscle;retina;uterus;lung;bone;liver;testis;spleen;germinal center;kidney;brain;mammary gland;peripheral nerve;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.56585 0.09696 -0.231522913 36.36470866 711.28789 5.29998 QSOX1 6.78457250016221e-05 0.995162326201129 0.0047698280738698 quiescin sulfhydryl oxidase 1 FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins. In fibroblasts, it may have tumor- suppressing capabilities being involved in growth regulation. {ECO:0000269|PubMed:10542195, ECO:0000269|PubMed:10708601, ECO:0000269|PubMed:12176051, ECO:0000269|PubMed:16806532, ECO:0000269|PubMed:17331072, ECO:0000269|PubMed:18393449}.; . TISSUE SPECIFICITY: Expressed in heart, placenta, lung, liver, skeletal muscle, pancreas and very weakly in brain and kidney. {ECO:0000269|PubMed:10708601, ECO:0000269|Ref.9}.; . . 0.11463 0.13137 -0.08265057 47.20452937 1198.21501 6.56746 QSOX2 0.00783061284578592 0.99154521375907 0.000624173395144352 quiescin sulfhydryl oxidase 2 FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins. Also seems to play a role in regulating the sensitization of neuroblastoma cells for interferon-gamma-induced apoptosis. {ECO:0000269|PubMed:14633699}.; . TISSUE SPECIFICITY: Expressed in pancreas, brain, placenta, kidney, heart and fetal tissues. Weakly expressed in lung, liver and skeletal muscles. {ECO:0000269|PubMed:14633699}.; unclassifiable (Anatomical System);lymph node;spleen;blood;germinal center;cerebellum; trigeminal ganglion; 0.22600 0.11440 -0.06060434 48.88535032 405.23545 4.22151 QTRT1 0.000223249642879381 0.914936004325219 0.0848407460319013 queuine tRNA-ribosyltransferase catalytic subunit 1 FUNCTION: Interacts with QTRTD1 to form an active queuine tRNA- ribosyltransferase. This enzyme exchanges queuine for the guanine at the wobble position of tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), thereby forming the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1- yl)amino)methyl)-7-deazaguanosine) (By similarity). {ECO:0000250}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;synovium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;islets of Langerhans;hypothalamus;urinary;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;alveolus;spleen;cervix;kidney;stomach; medulla oblongata;thyroid;skeletal muscle;cingulate cortex;cerebellum; 0.15678 0.10798 -0.514264485 21.41424864 34.35451 1.05075 QTRT1P1 . . . queuine tRNA-ribosyltransferase catalytic subunit 1 pseudogene 1 . . . . . . . . . . . QTRT2 . . . queuine tRNA-ribosyltransferase accessory subunit 2 FUNCTION: Interacts with QTRT1 to form an active queuine tRNA- ribosyltransferase. This enzyme exchanges queuine for the guanine at the wobble position of tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), thereby forming the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1- yl)amino)methyl)-7-deazaguanosine). {ECO:0000255|HAMAP- Rule:MF_03043}.; . . . . 0.03624 0.13210 0.016664174 55.21939137 . . R3HCC1 . . . R3H domain and coiled-coil containing 1 . . . medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;spleen;kidney;mammary gland;stomach;aorta;thymus; whole brain;thalamus;superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.14185 . 0.3032669 72.009908 1213.05414 6.59171 R3HCC1L 2.88113627340706e-05 0.931361172936905 0.068610015700361 R3H domain and coiled-coil containing 1 like . . TISSUE SPECIFICITY: Expressed in placenta.; . . 0.08159 0.07005 3.293062599 99.41023826 1062.07159 6.25556 R3HDM1 0.00602513988409452 0.993973326571785 1.53354412021804e-06 R3H domain containing 1 . . . lymphoreticular;medulla oblongata;smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;artery;unclassifiable (Anatomical System);amygdala;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;placenta;visual apparatus;liver;head and neck;kidney;stomach;aorta; amygdala;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.50034 0.07527 -0.086288664 47.11606511 4224.86385 12.93501 R3HDM2 0.995928589389731 0.0040713973094398 1.33008294677221e-08 R3H domain containing 2 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;atrium;frontal lobe;cochlea;cerebral cortex;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;cerebellum; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;fetal brain;cerebellum peduncles;prefrontal cortex;globus pallidus;caudate nucleus;parietal lobe;cingulate cortex;cerebellum; 0.38749 0.10760 -0.600630256 18.06440198 457.89203 4.44246 R3HDM2P1 . . . R3H domain containing 2 pseudogene 1 . . . . . . . . . . . R3HDM2P2 . . . R3H domain containing 2 pseudogene 2 . . . . . . . . . . . R3HDM4 0.0193453111593238 0.900324135917696 0.0803305529229805 R3H domain containing 4 . . . medulla oblongata;ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;thyroid;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;lens;pancreas;lung;epididymis;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;whole blood;bone marrow; 0.14605 0.10939 0.262810045 70.43524416 922.19623 5.89756 R3HDML 0.00299617468807422 0.812658046057099 0.184345779254827 R3H domain containing-like FUNCTION: Putative serine protease inhibitor. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary; dorsal root ganglion;superior cervical ganglion;globus pallidus;trigeminal ganglion; 0.37482 0.10077 0.707379532 85.62750649 569.91074 4.84195 RAB1A 0.602945640832257 0.388106151815091 0.00894820735265287 RAB1A, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB1A regulates vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment and on to the cell surface, and plays a role in IL-8 and growth hormone secretion. Regulates the level of CASR present at the cell membrane. Plays a role in cell adhesion and cell migration, via its role in protein trafficking. Plays a role in autophagosome assembly and cellular defense reactions against pathogenic bacteria. Plays a role in microtubule-dependent protein transport by early endosomes and in anterograde melanosome transport. {ECO:0000269|PubMed:20639577, ECO:0000269|PubMed:20861236, ECO:0000269|PubMed:21303926, ECO:0000269|PubMed:22939626}.; . . lymphoreticular;ovary;colon;substantia nigra;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;atrium;whole body;cochlea;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;subthalamic nucleus;thyroid;placenta;caudate nucleus; 0.66808 0.24770 0.301449681 71.80938901 27.05157 0.87367 RAB1B 0.751684324915879 0.246164768598745 0.00215090648537612 RAB1B, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB1B regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum. {ECO:0000269|PubMed:20545908, ECO:0000269|PubMed:9437002}.; . . myocardium;medulla oblongata;smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus;cerebellum; prostate;trigeminal ganglion; 0.34483 . -0.229483771 36.86010852 7.65837 0.28304 RAB1C . . . RAB1C, member RAS oncogene family pseudogene FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}.; . . . . . . . . . . RAB2A 0.970735512688083 0.0292234938261008 4.0993485816471e-05 RAB2A, member RAS oncogene family FUNCTION: Required for protein transport from the endoplasmic reticulum to the Golgi complex.; . . lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; dorsal root ganglion;whole brain;amygdala;medulla oblongata;superior cervical ganglion;thalamus;occipital lobe;hypothalamus;caudate nucleus;pons;atrioventricular node;subthalamic nucleus;fetal brain;placenta;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.66027 0.23984 0.013025609 54.62962963 2.87372 0.10200 RAB2B 0.000147821571275719 0.659028489257192 0.340823689171532 RAB2B, member RAS oncogene family FUNCTION: Required for protein transport from the endoplasmic reticulum to the Golgi complex. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in kidney, prostate, lung, liver, thymus, colon, pancreas, and skeletal muscle, and low levels in placenta. Not detected in heart, brain, spleen, testis, ovary, small intestine and leukocyte.; ovary;salivary gland;colon;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;hypopharynx;spleen;head and neck;cervix;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.37953 0.11262 0.014844891 54.94810097 24.84507 0.81541 RAB3A 0.870967555184365 0.127306126338372 0.00172631847726322 RAB3A, member RAS oncogene family FUNCTION: Involved in exocytosis by regulating a late step in synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal.; . TISSUE SPECIFICITY: Specifically expressed in brain.; unclassifiable (Anatomical System);ovary;hypothalamus;pineal body;colon;substantia nigra;fovea centralis;retina;prostate;whole body;lung;frontal lobe;bone;macula lutea;visual apparatus;hippocampus;testis;kidney;mammary gland;brain;stomach;cerebellum; amygdala;whole brain;occipital lobe;medulla oblongata;thalamus;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.44092 0.35026 -0.229483771 36.86010852 6.76255 0.24952 RAB3B 0.156443019931872 0.775690257570023 0.0678667224981051 RAB3B, member RAS oncogene family FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}.; . . . . 0.61008 0.17538 -0.007201372 53.19061099 21.78565 0.73367 RAB3C 0.015496264062785 0.880012133928957 0.104491602008258 RAB3C, member RAS oncogene family FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, placenta and lung. {ECO:0000269|PubMed:12296628}.; unclassifiable (Anatomical System);lung;frontal lobe;islets of Langerhans;hypothalamus;placenta;brain;skeletal muscle;retina; globus pallidus;ciliary ganglion;trigeminal ganglion; 0.57323 0.14229 -0.295622497 32.61972163 8.00432 0.29420 RAB3D 0.00142628412727186 0.667359738493865 0.331213977378863 RAB3D, member RAS oncogene family FUNCTION: Protein transport. Probably involved in regulated exocytosis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in granulocytes of peripheral blood. Constitutively expressed at low levels in all hematopoietic cell lines investigated.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;fovea centralis;choroid;lens;skin;skeletal muscle;retina;bone marrow;uterus;optic nerve;lung;cornea;placenta;macula lutea;visual apparatus;liver;kidney;brain;mammary gland; superior cervical ganglion;ciliary ganglion; 0.13045 0.21474 0.106667882 61.73036093 314.113 3.76823 RAB3GAP1 3.66101381631237e-05 0.999959420366715 3.96949512155187e-06 RAB3 GTPase activating protein catalytic subunit 1 FUNCTION: Probable catalytic subunit of a GTPase activating protein that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. Specifically converts active Rab3-GTP to the inactive form Rab3-GDP. Required for normal eye and brain development. May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters. {ECO:0000269|PubMed:10859313, ECO:0000269|PubMed:9030515}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9030515}.; lymphoreticular;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;iris;testis;germinal center;brain;artery;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;cerebellum; amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;hypothalamus;temporal lobe;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;placenta;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.42054 0.14874 0.202129237 67.42745931 2290.07687 8.85637 RAB3GAP2 0.99873648274446 0.00126351725552891 1.06405941098825e-14 RAB3 GTPase activating non-catalytic protein subunit 2 FUNCTION: Regulatory subunit of a GTPase activating protein that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. Rab3 GTPase-activating complex specifically converts active Rab3-GTP to the inactive form Rab3- GDP. Required for normal eye and brain development. May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non- synaptic vesicular release of neurotransmitters. {ECO:0000269|PubMed:9733780}.; DISEASE: Warburg micro syndrome 2 (WARBM2) [MIM:614225]: A rare syndrome characterized by microcephaly, microphthalmia, microcornia, congenital cataracts, optic atrophy, cortical dysplasia, in particular corpus callosum hypoplasia, severe mental retardation, spastic diplegia, and hypogonadism. {ECO:0000269|PubMed:20967465}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9733780}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;pineal gland;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; subthalamic nucleus;fetal liver;occipital lobe;superior cervical ganglion;medulla oblongata;prefrontal cortex;globus pallidus;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle;parietal lobe; 0.63992 0.12109 -1.080231599 7.277659825 2000.41869 8.24160 RAB3IL1 0.000894540821499919 0.938334548644554 0.0607709105339456 RAB3A interacting protein (rabin3)-like 1 FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB3A, a GTPase that regulates synaptic vesicle exocytosis. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. May also activate RAB8A and RAB8B. {ECO:0000269|PubMed:20937701}.; . . unclassifiable (Anatomical System);medulla oblongata;ovary;colon;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;endometrium;placenta;bone;macula lutea;liver;testis;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.37659 0.13982 -0.402212257 26.7338995 995.04891 6.07827 RAB3IP 0.0167529426994785 0.982235508103603 0.00101154919691877 RAB3A interacting protein FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB8A and RAB8B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP- bound form. Mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. Modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. Together with RAB11A, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. {ECO:0000269|PubMed:12221131, ECO:0000269|PubMed:20890297, ECO:0000269|PubMed:20937701}.; . TISSUE SPECIFICITY: Expressed in brain, kidney, heart, pancreas and placenta. Not detected in skeletal muscle or liver. {ECO:0000269|PubMed:12007189, ECO:0000269|PubMed:12221131}.; ovary;developmental;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.05975 0.11040 -0.492218069 22.35786742 110.62696 2.29081 RAB4A 0.081107904343709 0.908407522465016 0.0104845731912754 RAB4A, member RAS oncogene family FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}.; . . . . 0.22443 0.10657 -0.119252484 44.53880632 18.10086 0.63181 RAB4B 0.940202326280457 0.0595545873230046 0.000243086396538658 RAB4B, member RAS oncogene family FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;optic nerve;frontal lobe;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;epididymis;placenta;visual apparatus;macula lutea;liver;spleen;kidney;mammary gland;stomach;thymus; amygdala;dorsal root ganglion;whole brain;occipital lobe;medulla oblongata;olfactory bulb;hypothalamus;temporal lobe;spinal cord;white blood cells;atrioventricular node;placenta;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.37331 0.11262 -0.538132194 20.26421326 2.81543 0.10018 RAB4B-EGLN2 . . . RAB4B-EGLN2 readthrough (NMD candidate) . . . . . 0.42712 . . . . . RAB5A 0.774403049424523 0.22395994654642 0.00163700402905651 RAB5A, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB5A is required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension. {ECO:0000269|PubMed:10818110, ECO:0000269|PubMed:14617813, ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:15378032, ECO:0000269|PubMed:16410077}.; . . lymphoreticular;umbilical cord;ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;dura mater;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;hippocampus;hypopharynx;liver;head and neck;kidney;mammary gland;stomach; amygdala;occipital lobe;thalamus;superior cervical ganglion;cerebellum peduncles;hypothalamus;spinal cord;pons;skeletal muscle;subthalamic nucleus;placenta;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.75413 0.45954 -0.317668748 31.45789101 14.15943 0.51275 RAB5B 0.215698853711726 0.775643530134182 0.00865761615409166 RAB5B, member RAS oncogene family FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;oral cavity;pancreas;lung;adrenal gland;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;prefrontal cortex;ciliary ganglion;pons;atrioventricular node;parietal lobe;cerebellum; 0.71956 0.12519 -0.119252484 44.53880632 36.49398 1.09395 RAB5C 0.826569532430599 0.17263964910922 0.000790818460181114 RAB5C, member RAS oncogene family FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;lens;breast;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;temporal lobe;kidney;pons;atrioventricular node;trigeminal ganglion;whole blood; 0.57797 0.12971 0.215080721 67.91696155 28.22907 0.90529 RAB5CP1 . . . RAB5C, member RAS oncogene family pseudogene 1 . . . . . . . . . . . RAB5CP2 . . . RAB5C, member RAS oncogene family pseudogene 2 . . . . . . . . . . . RAB6A 0.877760860434295 0.121928177611187 0.000310961954517776 RAB6A, member RAS oncogene family FUNCTION: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Has a low GTPase activity.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11071909}.; myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;subthalamic nucleus;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;amygdala;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; occipital lobe;subthalamic nucleus;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex; . . 0.103030231 61.2762444 10.60644 0.38568 RAB6B 0.893311148938933 0.10647090353423 0.000217947526837134 RAB6B, member RAS oncogene family FUNCTION: Seems to have a role in retrograde membrane traffic at the level of the Golgi complex. May function in retrograde transport in neuronal cells. {ECO:0000269|PubMed:17707369}.; . TISSUE SPECIFICITY: Predominantly expressed in brain.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;stomach;cerebellum; whole brain;dorsal root ganglion;amygdala;superior cervical ganglion;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;atrioventricular node;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.70633 0.14229 0.014844891 54.94810097 3.08689 0.11110 RAB6C 0.377324685045267 0.576659735726666 0.046015579228067 RAB6C, member RAS oncogene family FUNCTION: May be involved in the regulation of centrosome duplication and cell cycle progression. {ECO:0000269|PubMed:17426708, ECO:0000269|PubMed:18992151, ECO:0000269|PubMed:20064528}.; . TISSUE SPECIFICITY: Highest levels are found in fetal and adult brain, prostate, testis and spinal cord. Undetectable expression in adrenal gland, skeletal muscle, bone marrow, fetal, and adult liver, heart, salivary gland, and trachea. Detected in the HEK293, HEK293T, LNCaP, MCF-7, T-47D and EVSA-T cell lines (at protein level). {ECO:0000269|PubMed:20064528}.; . . . 0.02889 1.659136225 96.23142251 547.7083 4.75946 RAB6C-AS1 . . . RAB6C antisense RNA 1 . . . . . . . . . . . RAB7A 0.922269115879691 0.0772597860292752 0.000471098091034338 RAB7A, member RAS oncogene family FUNCTION: Key regulator in endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades. Plays a central role, not only in endosomal traffic, but also in many other cellular and physiological events, such as growth-factor-mediated cell signaling, nutrient- transportor mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism. Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes. Plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses. Microbial pathogens possess survival strategies governed by RAB7A, sometimes by employing RAB7A function (e.g. Salmonella) and sometimes by excluding RAB7A function (e.g. Mycobacterium). In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA (PubMed:11179213, PubMed:12944476, PubMed:14617358, PubMed:20028791, PubMed:21255211). Regulates the endocytic trafficking of the EGF- EGFR complex by regulating its lysosomal degradation. Involved in the ADRB2-stimulated lipolysis through lipophagy, a cytosolic lipase-independent autophagic pathway (By similarity). {ECO:0000250|UniProtKB:P51150, ECO:0000269|PubMed:11179213, ECO:0000269|PubMed:12944476, ECO:0000269|PubMed:14617358, ECO:0000269|PubMed:20028791, ECO:0000269|PubMed:21255211}.; . TISSUE SPECIFICITY: Widely expressed; high expression found in skeletal muscle. {ECO:0000269|PubMed:12545426}.; lymphoreticular;myocardium;smooth muscle;ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;muscle;blood;breast;pancreas;lung;mesenchyma;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; whole brain;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;thalamus;placenta;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.50311 . -0.229483771 36.86010852 4.25742 0.15507 RAB7B . . . RAB7B, member RAS oncogene family FUNCTION: Controls vesicular trafficking from endosomes to the trans-Golgi network (TGN). Acts as a negative regulator of TLR9 signaling and can suppress TLR9-triggered TNFA, IL6, and IFNB production in macrophages by promoting TLR9 lysosomal degradation. Also negatively regulates TLR4 signaling in macrophages by promoting lysosomal degradation of TLR4. Promotes megakaryocytic differentiation by increasing NF-kappa-B-dependent IL6 production and subsequently enhancing the association of STAT3 with GATA1. Not involved in the regulation of the EGF- and EGFR degradation pathway. {ECO:0000269|PubMed:20375062, ECO:0000269|PubMed:20953574}.; . TISSUE SPECIFICITY: Expressed in heart, placenta, lung, skeletal muscle and peripheral blood leukocyte. {ECO:0000269|PubMed:15144907}.; . . . . . . . . RAB8A 0.962128955227462 0.0377933646663601 7.76801061780308e-05 RAB8A, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in polarized vesicular trafficking and neurotransmitter release. Together with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B and RAB11A participates in epithelial cell polarization. Plays an important role in ciliogenesis. Together with MICALL2, may also regulate adherens junction assembly. May play a role in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore play a role in glucose homeostasis. {ECO:0000269|PubMed:20890297, ECO:0000269|PubMed:21282656, ECO:0000269|PubMed:21844891}.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;thymus;cerebellum; superior cervical ganglion;placenta;liver;kidney; 0.20304 0.31462 -0.251530012 35.42108988 1.07555 0.02762 RAB8B 0.0495152480226271 0.928050349755284 0.0224344022220888 RAB8B, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab may be involved in polarized vesicular trafficking and neurotransmitter release. May participate in cell junction dynamics in Sertoli cells (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;dura mater;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;small intestine;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pia mater;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;aorta; testis - interstitial;testis;skeletal muscle; 0.09665 0.13588 -0.053113545 49.38664779 6.15812 0.23191 RAB9A 0.779010976914761 0.213823277514625 0.00716574557061431 RAB9A, member RAS oncogene family FUNCTION: Involved in the transport of proteins between the endosomes and the trans Golgi network.; . . ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hypopharynx;amnion;head and neck;kidney;mammary gland;stomach; . 0.12355 0.10970 0.035072054 56.2514744 1.10631 0.02919 RAB9AP1 . . . RAB9A, member RAS oncogene family pseudogene 1 . . . . . . . . . . . RAB9AP2 . . . RAB9A, member RAS oncogene family pseudogene 2 . . . . . . . . . . . RAB9AP3 . . . RAB9A, member RAS oncogene family pseudogene 3 . . . . . . . . . . . RAB9AP4 . . . RAB9A, member RAS oncogene family pseudogene 4 . . . . . . . . . . . RAB9AP5 . . . RAB9A, member RAS oncogene family pseudogene 5 . . . . . . . . . . . RAB9B 0.618182540762696 0.348899995456805 0.0329174637804987 RAB9B, member RAS oncogene family FUNCTION: Involved in the transport of proteins between the endosomes and the trans Golgi network. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11043518}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;parathyroid;fovea centralis;skin;skeletal muscle;uterus;prostate;whole body;lung;endometrium;placenta;macula lutea;hippocampus;liver;spleen;kidney;brain;mammary gland;stomach; . 0.39937 0.10468 -0.075159878 47.78839349 7.12466 0.26601 RAB9BP1 . . . RAB9B, member RAS oncogene family pseudogene 1 . . . . . . . . . . . RAB10 0.944404791408518 0.0553927469122775 0.000202461679204639 RAB10, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane. Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane. In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response. Plays also a specific role in asymmetric protein transport to the plasma membrane within the polarized neuron and epithelial cells. In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane while in epithelial cells, it regulates transport from the Golgi to the basolateral membrane. Moreover, may play a role in the basolateral recycling pathway and in phagosome maturation. According to PubMed:23263280, may play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion. {ECO:0000250, ECO:0000269|PubMed:16641372, ECO:0000269|PubMed:21248164, ECO:0000269|PubMed:23263280}.; . . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; amygdala;superior cervical ganglion; 0.49391 . 0.013025609 54.62962963 1.2898 0.04599 RAB11A 0.983220856534547 0.0167687407515434 1.0402713909889e-05 RAB11A, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes. May also play a role in melanosome transport and release from melanocytes. {ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:15689490, ECO:0000269|PubMed:17462998, ECO:0000269|PubMed:19542231, ECO:0000269|PubMed:20890297, ECO:0000269|PubMed:21282656}.; . . myocardium;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;alveolus;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; amygdala;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;atrioventricular node;parietal lobe; 0.47787 0.25991 -0.053113545 49.38664779 1.39773 0.04980 RAB11AP1 . . . RAB11A, member RAS oncogene family pseudogene 1 . . . . . . . . . . . RAB11AP2 . . . RAB11A, member RAS oncogene family pseudogene 2 . . . . . . . . . . . RAB11B 0.664363642569307 0.330377564709756 0.00525879272093717 RAB11B, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage- gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis. {ECO:0000269|PubMed:14627637, ECO:0000269|PubMed:19029296, ECO:0000269|PubMed:19244346, ECO:0000269|PubMed:20717956, ECO:0000269|PubMed:21248079, ECO:0000269|PubMed:22129970}.; . . lymphoreticular;ovary;salivary gland;sympathetic chain;colon;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;urinary;blood;lens;breast;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; thyroid;prefrontal cortex; 0.33496 0.11262 -0.273576253 33.97027601 5.54668 0.20692 RAB11B-AS1 . . . RAB11B antisense RNA 1 . . . . . . . . . . . RAB11FIP1 2.10564412942988e-05 0.975595538234517 0.0243834053241888 RAB11 family interacting protein 1 (class I) FUNCTION: A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and in phagocytosis. {ECO:0000269|PubMed:11786538, ECO:0000269|PubMed:15181150, ECO:0000269|PubMed:15355514, ECO:0000269|PubMed:16920206}.; . TISSUE SPECIFICITY: Isoform 2 is expressed in brain, heart, testis, lung, spleen, ovary and small intestine. {ECO:0000269|PubMed:11786538}.; ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;endometrium;bone;testis;amniotic fluid;germinal center;ciliary body;brain;unclassifiable (Anatomical System);lymph node;cartilage;small intestine;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;trachea;placenta;ciliary ganglion;whole blood;trigeminal ganglion;bone marrow; 0.15235 0.09985 1.416442137 94.85138004 2710.66697 9.80207 RAB11FIP1P1 . . . RAB11 family interacting protein 1 (class I) pseudogene 1 . . . . . . . . . . . RAB11FIP2 0.910707841389083 0.0891545791684454 0.000137579442471925 RAB11 family interacting protein 2 (class I) FUNCTION: A Rab11 effector binding preferentially phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA) and acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Involved in insulin granule exocytosis. Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles. Required in a complex with MYO5B and RAB11 for the transport of NPC1L1 to the plasma membrane. Also acts as a regulator of cell polarity. {ECO:0000269|PubMed:12364336, ECO:0000269|PubMed:15304524, ECO:0000269|PubMed:16251358, ECO:0000269|PubMed:16775013, ECO:0000269|PubMed:19542231}.; . . lymphoreticular;smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;islets of Langerhans;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;kidney; superior cervical ganglion;prefrontal cortex;globus pallidus;pons;parietal lobe;skeletal muscle; 0.32279 0.13177 0.086440867 60.47416844 470.93745 4.49152 RAB11FIP3 0.99624251258264 0.00375743337965377 5.40377060087588e-08 RAB11 family interacting protein 3 (class II) FUNCTION: Acts as a regulator of endocytic traffic by participating in membrane delivery. Required for the abcission step in cytokinesis, possibly by acting as an 'address tag' delivering recycling endosome membranes to the cleavage furrow during late cytokinesis. Also required for the structural integrity of the endosomal recycling compartment during interphase. May play a role in breast cancer cell motility by regulating actin cytoskeleton. {ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:17394487, ECO:0000269|PubMed:19327867}.; . . ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; amygdala;uterus corpus;superior cervical ganglion;testis - interstitial;pons;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.15672 0.10902 . . 175.66911 2.88381 RAB11FIP4 0.993663613309385 0.00633619300687827 1.93683736937849e-07 RAB11 family interacting protein 4 (class II) FUNCTION: Acts as a regulator of endocytic traffic by participating in membrane delivery. Required for the abcission step in cytokinesis, possibly by acting as an 'address tag' delivering recycling endosome membranes to the cleavage furrow during late cytokinesis. In case of infection by HCMV (human cytomegalovirus), may participate in egress of the virus out of nucleus; this function is independent of ARF6. {ECO:0000269|PubMed:12470645}.; . TISSUE SPECIFICITY: Present at high level in testis (at protein level). Weakly expressed in other tissues. {ECO:0000269|PubMed:12857874}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach; whole brain;amygdala;superior cervical ganglion;medulla oblongata;thalamus;occipital lobe;hypothalamus;temporal lobe;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.16205 0.12251 -0.865195027 10.79853739 78.6509 1.87111 RAB11FIP5 0.00267591631179698 0.935503066570636 0.0618210171175671 RAB11 family interacting protein 5 (class I) FUNCTION: Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis. {ECO:0000269|PubMed:11163216, ECO:0000269|PubMed:20717956}.; . TISSUE SPECIFICITY: Detected at low levels in heart, brain, placenta, lung, liver, adipocytes, kidney, spleen, skeletal muscle and pancreas. {ECO:0000269|PubMed:10545525, ECO:0000269|PubMed:11278501}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach; . 0.29184 0.23310 -0.887242605 10.43288511 94.5108 2.09293 RAB12 0.718356946973086 0.27854123851097 0.00310181451594455 RAB12, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab may play a role in protein transport from recycling endosomes to lysosomes regulating, for instance, the degradation of the transferrin receptor. Involved in autophagy (By similarity). {ECO:0000250}.; . . urinary;colon;skin;skeletal muscle;retina;uterus;breast;lung;cerebral cortex;larynx;placenta;liver;testis;spleen;brain;mammary gland; . 0.15870 . -0.207437529 38.2814343 18.24236 0.63386 RAB13 0.57012570509712 0.427392688204975 0.00248160669790474 RAB13, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in endocytic recycling and regulates the transport to the plasma membrane of transmembrane proteins like the tight junction protein OCLN/occludin. Thereby, it regulates the assembly and the activity of tight junctions. Moreover, it may also regulate tight junction assembly by activating the PKA signaling pathway and by reorganizing the actin cytoskeleton through the activation of the downstream effectors PRKACA and MICALL2 respectively. Through its role in tight junction assembly, may play a role in the establishment of Sertoli cell barrier. Plays also a role in angiogenesis through regulation of endothelial cells chemotaxis. Also involved in neurite outgrowth. Has also been proposed to play a role in post-Golgi membrane trafficking from the TGN to the recycling endosome. Finally, it has been involved in insulin- induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore may play a role in glucose homeostasis. {ECO:0000269|PubMed:12058051, ECO:0000269|PubMed:15096524, ECO:0000269|PubMed:15528189, ECO:0000269|PubMed:16525024, ECO:0000269|PubMed:18779367, ECO:0000269|PubMed:20008558}.; . TISSUE SPECIFICITY: Detected in several types of epithelia, including intestine, kidney, liver and in endothelial cells.; . . 0.07521 0.14896 0.215080721 67.91696155 106.31372 2.23696 RAB14 0.973482565196718 0.0264853073159995 3.21274872828671e-05 RAB14, member RAS oncogene family FUNCTION: Involved in membrane trafficking between the Golgi complex and endosomes during early embryonic development. Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. May act by modulating the kinesin KIF16B-cargo association to endosomes (By similarity). Regulates, together with its guanine nucleotide exchange factor DENND6A, the specific endocytic transport of ADAM10, N- cadherin/CDH2 shedding and cell-cell adhesion. {ECO:0000250, ECO:0000269|PubMed:22595670}.; . . . . 0.13111 0.16306 -0.009020804 52.8544468 0.89908 0.01914 RAB15 5.20750293834997e-06 0.422722563564016 0.577272228933045 RAB15, member RAS oncogene family FUNCTION: May act in concert with RAB3A in regulating aspects of synaptic vesicle membrane flow within the nerve terminal. {ECO:0000250}.; . . ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;head and neck;kidney;stomach; whole brain;amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;pons;subthalamic nucleus;fetal brain;placenta;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.14088 . 0.014844891 54.94810097 2.38532 0.08114 RAB17 0.00739028017956446 0.772406620157847 0.220203099662589 RAB17, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in transcytosis, the directed movement of endocytosed material through the cell and its exocytosis from the plasma membrane at the opposite side. Mainly observed in epithelial cells, transcytosis mediates for instance, the transcellular transport of immunoglobulins from the basolateral surface to the apical surface. Most probably controls membrane trafficking through apical recycling endosomes in a post- endocytic step of transcytosis. Required for melanosome transport and release from melanocytes, it also regulates dendrite and dendritic spine development (By similarity). May also play a role in cell migration. {ECO:0000250, ECO:0000269|PubMed:22328529}.; . TISSUE SPECIFICITY: Expressed in melanocytes (at protein level). {ECO:0000269|PubMed:21291502}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;blood;lens;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach;thymus; thyroid;liver;kidney; 0.07748 0.11591 0.485092724 79.37603208 446.76368 4.39821 RAB18 0.955008594637843 0.0448721274883378 0.000119277873819447 RAB18, member RAS oncogene family FUNCTION: Plays a role in apical endocytosis/recycling. May be implicated in transport between the plasma membrane and early endosomes. Plays a key role in eye and brain development and neurodegeneration. {ECO:0000269|PubMed:21473985}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;mesenchyma;nasopharynx;trabecular meshwork;placenta;visual apparatus;alveolus;liver;head and neck;kidney;mammary gland;stomach; . 0.19227 0.10960 0.103030231 61.2762444 . . RAB19 4.08401148578637e-05 0.22453812550211 0.775421034383032 RAB19, member RAS oncogene family . . . breast; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.21169 0.10029 -0.337894035 30.37272942 403.70536 4.21389 RAB20 0.697708787502414 0.285339286912482 0.0169519255851046 RAB20, member RAS oncogene family FUNCTION: Plays a role in apical endocytosis/recycling. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes. {ECO:0000269|PubMed:21255211}.; . TISSUE SPECIFICITY: Low or absent expression in normal pancreas and stronger expression in 15 of 18 exocrine pancreatic adenocarcinomas (at protein level). {ECO:0000269|PubMed:16613320}.; unclassifiable (Anatomical System);cartilage;ovary;adrenal cortex;colon;blood;parathyroid;fovea centralis;choroid;lens;retina;bone marrow;optic nerve;lung;placenta;macula lutea;testis;kidney;brain;mammary gland;stomach; adrenal gland;adrenal cortex; 0.13957 0.13052 -0.161524709 41.6430762 2.61806 0.09541 RAB21 0.882341696062871 0.117376972238926 0.00028133169820354 RAB21, member RAS oncogene family FUNCTION: Regulates integrin internalization and recycling, but does not influence the traffic of endosomally translocated receptors in general. As a result, may regulate cell adhesion and migration (By similarity). During the mitosis of adherent cells, controls the endosomal trafficking of integrins which is required for the successful completion of cytokinesis. Involved in neurite growth (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q6AXT5, ECO:0000269|PubMed:18804435}.; . TISSUE SPECIFICITY: Widely expressed. In jejunal tissue, predominantly expressed in the apical region of the epithelial cell layer of the villi, weak expression, if any, in the crypt epithelium. Capillary endothelium and some cell types in the lamina propria also show expression. {ECO:0000269|PubMed:10887961}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;trabecular meshwork;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; amygdala;occipital lobe;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.19701 0.12522 0.325313577 73.11276244 90.63641 2.04893 RAB22A 0.685129847877273 0.313970859305597 0.00089929281712969 RAB22A, member RAS oncogene family FUNCTION: Plays a role in endocytosis and intracellular protein transport. Mediates trafficking of TF from early endosomes to recycling endosomes. Required for NGF-mediated endocytosis of NTRK1, and subsequent neurite outgrowth. Binds GTP and GDP and has low GTPase activity. Alternates between a GTP-bound active form and a GDP-bound inactive form. {ECO:0000269|PubMed:16537905, ECO:0000269|PubMed:21849477}.; . . ovary;skin;retina;prostate;optic nerve;endometrium;cochlea;iris;germinal center;bladder;brain;heart;cartilage;urinary;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);cerebellum cortex;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;placenta;head and neck;kidney;stomach; amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;adrenal gland;prefrontal cortex;ciliary ganglion;atrioventricular node;pons;parietal lobe; 0.13239 0.12253 -0.207437529 38.2814343 9.37183 0.34486 RAB23 0.038517374000133 0.929208305293009 0.0322743207068576 RAB23, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Together with SUFU, prevents nuclear import of GLI1, and thereby inhibits GLI1 transcription factor activity. Regulates GLI1 in differentiating chondrocytes. Likewise, regulates GLI3 proteolytic processing and modulates GLI2 and GLI3 transcription factor activity. Plays a role in autophagic vacuole assembly, and mediates defense against pathogens, such as S.aureus, by promoting their capture by autophagosomes that then merge with lysosomes. {ECO:0000269|PubMed:22365972, ECO:0000269|PubMed:22452336}.; DISEASE: Carpenter syndrome 1 (CRPT1) [MIM:201000]: A rare autosomal recessive disorder characterized by acrocephaly with variable synostosis of the sagittal, lambdoid, and coronal sutures; peculiar facies; brachydactyly of the hands with syndactyly; preaxial polydactyly and syndactyly of the feet; congenital heart defects; growth retardation; mental retardation; hypogenitalism; and obesity. In addition, cerebral malformations, oral and dental abnormalities, coxa valga, genu valgum, hydronephrosis, precocious puberty, and hearing loss may be observed. {ECO:0000269|PubMed:17503333, ECO:0000269|PubMed:21412941}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;endometrium;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; uterus;trigeminal ganglion; 0.21235 0.14490 0.12689526 63.00424628 1138.91644 6.43550 RAB24 0.725032093168432 0.274370897289113 0.000597009542455695 RAB24, member RAS oncogene family FUNCTION: May be involved in autophagy-related processes. {ECO:0000250}.; . . medulla oblongata;ovary;colon;fovea centralis;skin;bone marrow;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;cervix;kidney;stomach;aorta; . 0.10222 . -0.207437529 38.2814343 3.30707 0.12045 RAB25 9.31079417686485e-06 0.541615555018813 0.45837513418701 RAB25, member RAS oncogene family FUNCTION: Involved in the regulation of cell survival. Promotes invasive migration of cells in which it functions to localize and maintain integrin alpha-V/beta-1 at the tips of extending pseudopodia (PubMed:17925226). Involved in the regulation of epithelial morphogenesis through the control of CLDN4 expression and localization at tight junctions (By similarity). May selectively regulate the apical recycling pathway. Together with MYO5B regulates transcytosis (By similarity). {ECO:0000250|UniProtKB:E2RQ15, ECO:0000250|UniProtKB:P46629, ECO:0000250|UniProtKB:Q9WTL2, ECO:0000269|PubMed:17925226}.; . TISSUE SPECIFICITY: Expressed in ovarian epithelium (NOE) and breast tissue. Expressed in ovarian cancer; expression is increased relative to NOE cells. Expression in ovarian cancer is stage dependent, with stage III and stage IV showing higher levels than early stage cancers. Expressed in breast cancer; expression is increased relative to normal breast tissue. {ECO:0000269|PubMed:15502842}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;oesophagus;larynx;thyroid;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;urinary;pharynx;blood;breast;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach; prostate;lung;trachea;tongue;placenta;thyroid;skin; 0.21353 0.09246 0.349177632 74.18023119 101.42575 2.18009 RAB26 3.5573777860374e-06 0.353701327260753 0.646295115361461 RAB26, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Mediates transport of ADRA2A and ADRA2B from the Golgi to the cell membrane. Plays a role in the maturation of zymogenic granules and in pepsinogen secretion in the stomach. Plays a role in the secretion of amylase from acinar granules in the parotid gland. {ECO:0000269|PubMed:20038531, ECO:0000269|PubMed:23105096}.; . TISSUE SPECIFICITY: Predominantly expressed in brain.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;retina;pancreas;optic nerve;lung;frontal lobe;endometrium;bone;hippocampus;liver;spleen;kidney;brain;stomach;thymus; whole brain;dorsal root ganglion;amygdala;medulla oblongata;superior cervical ganglion;cerebellum peduncles;temporal lobe;pons;atrioventricular node;caudate nucleus;subthalamic nucleus;liver;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.23803 0.10974 -0.271755481 34.31823543 28.74683 0.91981 RAB27A 8.23365144303053e-05 0.53174095590289 0.468176707582679 RAB27A, member RAS oncogene family FUNCTION: Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. {ECO:0000269|PubMed:18812475}.; . TISSUE SPECIFICITY: Found in all the examined tissues except in brain. Low expression was found in thymus, kidney, muscle and placenta. Detected in melanocytes, and in most tumor cell lines examined. Expressed in cytotoxic T-lymphocytes (CTL) and mast cells. {ECO:0000269|PubMed:15548590}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;prostate;white blood cells;atrioventricular node;whole blood;trigeminal ganglion;skeletal muscle;pituitary;bone marrow; 0.72181 0.39000 -0.560178693 19.30879925 38.08593 1.13154 RAB27B 0.687300099985693 0.308462367133436 0.00423753288087063 RAB27B, member RAS oncogene family FUNCTION: May be involved in targeting uroplakins to urothelial apical membranes. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed primarily in testis.; unclassifiable (Anatomical System);breast;prostate;lung;frontal lobe;bone;thyroid;testis;colon;head and neck;skeletal muscle; testis - interstitial;superior cervical ganglion;temporal lobe;trigeminal ganglion; 0.27810 0.15268 0.237127192 68.98443029 33.41117 1.03127 RAB28 0.000997907226518685 0.816221995562062 0.18278009721142 RAB28, member RAS oncogene family . . TISSUE SPECIFICITY: Isoform S is detected in most tissues investigated: cortex, liver, kidney, skeletal muscle, adipose tissue, testis, urothelium, lung, bone marrow and retinal pigment epithelium (RPE). Isoform L 2 is widely and abundantly expressed all tissues. Isoform 3 is highly expressed in heart, lung, bone marrow, retina, brain, and RPE. {ECO:0000269|PubMed:23746546}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;atrium;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;stomach;aorta;thymus; amygdala;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.16428 0.10804 -0.229483771 36.86010852 34.07388 1.04509 RAB28P1 . . . RAB28, member RAS oncogene family pseudogene 1 . . . . . . . . . . . RAB28P2 . . . RAB28, member RAS oncogene family pseudogene 2 . . . . . . . . . . . RAB28P3 . . . RAB28, member RAS oncogene family pseudogene 3 . . . . . . . . . . . RAB28P4 . . . RAB28, member RAS oncogene family pseudogene 4 . . . . . . . . . . . RAB28P5 . . . RAB28, member RAS oncogene family pseudogene 5 . . . . . . . . . . . RAB29 . . . RAB29, member RAS oncogene family FUNCTION: Rab GTPase key regulator in vesicle trafficking. Essential for maintaining the integrity of the endosome-trans- Golgi network structure. Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner. Regulates neuronal process morphology in the intact central nervous system (CNS). May play a role in the formation of typhoid toxin transport intermediates during Salmonella enterica serovar Typhi (S.Typhi) epithelial cell infection. {ECO:0000269|PubMed:22042847, ECO:0000269|PubMed:24788816}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:24788816}.; . . 0.17037 0.11880 0.125076652 62.7388535 . . RAB30 0.959123959685969 0.0407821166913199 9.39236227105464e-05 RAB30, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Required for maintaining the structural integrity of the Golgi apparatus, possibly by mediating interactions with cytoplasmic scaffolding proteins. {ECO:0000250, ECO:0000269|PubMed:22188167}.; . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skeletal muscle;breast;prostate;visual apparatus;liver;germinal center;kidney;brain;bladder;tonsil; superior cervical ganglion;globus pallidus;skeletal muscle; 0.42262 0.11262 -0.09720619 46.20193442 8.96111 0.32903 RAB30-AS1 . . . RAB30 antisense RNA 1 (head to head) . . . . . . . . . . . RAB31 0.0540334843531379 0.86383385804301 0.0821326576038518 RAB31, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Required for the integrity and for normal function of the Golgi apparatus and the trans-Golgi network. Plays a role in insulin-stimulated translocation of GLUT4 to the cell membrane. Plays a role in M6PR transport from the trans-Golgi network to endosomes. Plays a role in the internalization of EGFR from the cell membrane into endosomes. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. {ECO:0000269|PubMed:17189207, ECO:0000269|PubMed:17678623, ECO:0000269|PubMed:19725050, ECO:0000269|PubMed:21255211, ECO:0000269|PubMed:21586568}.; . TISSUE SPECIFICITY: Highest expression in placenta and brain with lower levels in heart and lung. Not detected in liver, skeletal muscle, kidney or pancreas. {ECO:0000269|PubMed:11784320}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;oral cavity;pancreas;lung;adrenal gland;nasopharynx;internal ear;placenta;hippocampus;head and neck;kidney;stomach;thymus; . 0.06168 0.10905 -0.141298762 42.87567823 10.46141 0.38035 RAB32 0.00877092275554058 0.80233036457503 0.188898712669429 RAB32, member RAS oncogene family FUNCTION: Acts as an A-kinase anchoring protein by binding to the type II regulatory subunit of protein kinase A and anchoring it to the mitochondrion. Also involved in synchronization of mitochondrial fission. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. {ECO:0000269|PubMed:12186851, ECO:0000269|PubMed:21255211}.; . TISSUE SPECIFICITY: Widely expressed with high levels in heart, liver, kidney, bone marrow, testis, colon and fetal lung. {ECO:0000269|PubMed:11784320, ECO:0000269|PubMed:12186851}.; . . 0.09777 0.12197 -0.339715008 30.06605331 18.86073 0.65111 RAB33A 0.713538246843134 0.271870918403836 0.0145908347530296 RAB33A, member RAS oncogene family . . TISSUE SPECIFICITY: Expressed only in lymphoid cell lines.; unclassifiable (Anatomical System);lymphoreticular;heart;hypothalamus;colon;blood;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;placenta;macula lutea;germinal center;kidney;brain; whole brain;superior cervical ganglion;trigeminal ganglion;skeletal muscle;parietal lobe;cerebellum; 0.11534 0.12281 0.125076652 62.7388535 65.05267 1.65908 RAB33B 0.902062769310016 0.0970888358598501 0.000848394830133949 RAB33B, member RAS oncogene family FUNCTION: Protein transport. Acts, in coordination with RAB6A, to regulate intra-Golgi retrograde trafficking. It is involved in autophagy, acting as a modulator of autophagosome formation. {ECO:0000269|PubMed:20163571}.; DISEASE: Smith-McCort dysplasia 2 (SMC2) [MIM:615222]: A rare autosomal recessive osteochondrodysplasia with skeletal features identical to those of Dyggve-Melchior-Clausen syndrome, but with normal intelligence and no microcephaly. It is characterized by short limbs and trunk with barrel-shaped chest. The radiographic phenotype includes platyspondyly, generalized abnormalities of the epiphyses and metaphyses, and a distinctive lacy appearance of the iliac crest. {ECO:0000269|PubMed:22652534, ECO:0000269|PubMed:23042644}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . sympathetic chain;fovea centralis;choroid;vein;retina;optic nerve;atrium;endometrium;bone;pituitary gland;germinal center;artery;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;adrenal cortex;lens;skeletal muscle;pancreas;mesenchyma;placenta;macula lutea;hypopharynx;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;trigeminal ganglion; 0.15308 0.10819 0.082802743 60.09082331 20.92026 0.70824 RAB34 4.67974818241862e-06 0.849259751633369 0.150735568618448 RAB34, member RAS oncogene family . . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;bone;testis;brain;unclassifiable (Anatomical System);trophoblast;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;amnion;spleen;cervix;kidney;mammary gland;stomach; uterus corpus;lung;heart;thyroid; 0.49492 0.14267 -0.60427181 17.74593064 14.52455 0.52200 RAB35 0.979782361188921 0.0202011825128796 1.64562981995094e-05 RAB35, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. {ECO:0000269|PubMed:16950109, ECO:0000269|PubMed:21951725}.; . . ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;testis;brain;unclassifiable (Anatomical System);cartilage;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;pons;cerebellum; 0.56862 . -0.163345027 41.24793583 343.3934 3.92819 RAB36 1.44185655300034e-05 0.851130616435579 0.148854964998891 RAB36, member RAS oncogene family FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously present in all tissues examined.; unclassifiable (Anatomical System);ovary;cartilage;islets of Langerhans;parathyroid;choroid;retina;uterus;prostate;lung;frontal lobe;placenta;thyroid;iris;kidney;brain;stomach; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion; 0.05027 0.10981 0.621009802 83.41589998 182.68124 2.93545 RAB37 8.22692114813263e-05 0.767820210308877 0.232097520479641 RAB37, member RAS oncogene family . . . unclassifiable (Anatomical System);pancreas;lung;lens;brain; superior cervical ganglion;cerebellum peduncles;ciliary ganglion;whole blood;cerebellum; 0.08186 0.11813 0.040529541 57.15380986 48.09219 1.35018 RAB38 0.00471761819647518 0.683666984221141 0.311615397582384 RAB38, member RAS oncogene family FUNCTION: May be involved in melanosomal transport and docking. Involved in the proper sorting of TYRP1. Involved in peripheral melanosomal distribution of TYRP1 in melanocytes; the function, which probably is implicating vesicle-trafficking, includes cooperation with ANKRD27 and VAMP7 (By similarity). Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. {ECO:0000250|UniProtKB:Q8QZZ8, ECO:0000269|PubMed:21255211}.; . TISSUE SPECIFICITY: Expressed in melanocytes.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;heart;salivary gland;urinary;intestine;pharynx;colon;blood;skin;lung;cornea;placenta;visual apparatus;pituitary gland;liver;testis;kidney;brain;mammary gland;bladder;stomach; superior cervical ganglion;lung;tongue;adrenal gland;adrenal cortex;skin; 0.25026 0.14628 0.305084559 72.22811984 55.92063 1.50157 RAB39A 0.00185648965406038 0.722710509313596 0.275433001032344 RAB39A, member RAS oncogene family FUNCTION: Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in vesicular trafficking. Plays a role in the fusion of phagosomes with lysosomes. Negatively regulates LPS-induced autophagosome formation in macrophages possibly by implicating PI3K (PubMed:24349490). May be involved in multiple neurite formation (By similarity). {ECO:0000250|UniProtKB:Q8BHD0, ECO:0000269|PubMed:21255211, ECO:0000269|PubMed:24349490}.; . . unclassifiable (Anatomical System);optic nerve;macula lutea;fovea centralis;choroid;lens;brain;retina; globus pallidus;ciliary ganglion; 0.67342 0.11262 -0.031067188 51.03798066 10.38316 0.37817 RAB39B 0.715196297042307 0.270446326984042 0.0143573759736508 RAB39B, member RAS oncogene family FUNCTION: May be involved in vesicular trafficking. Plays a role in synapse formation. May regulate the homeostasis of SNCA/alpha- synuclein. Together with PICK1 proposed to ensure selectively GRIA2 exit from the endoplasmic reticulum to the Golgi and to regulate AMPAR compostion at the post-synapses and thus synaptic transmission (By similarity). {ECO:0000250|UniProtKB:Q8BHC1}.; DISEASE: Waisman syndrome (WSMN) [MIM:311510]: A neurologic disorder characterized by delayed psychomotor development, intellectual disability, and early-onset Parkinson disease. {ECO:0000269|PubMed:25434005}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in the brain. {ECO:0000269|PubMed:20159109}.; . . 0.51604 0.11262 0.013025609 54.62962963 . . RAB40A 0.0666088196899615 0.732352632191396 0.201038548118643 RAB40A, member RAS oncogene family FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;visual apparatus;liver;spleen;kidney;brain;mammary gland; ciliary ganglion; 0.10174 0.10148 0.659651797 84.35362114 1182.64671 6.52735 RAB40AL 0.306490452326046 0.61962174925786 0.0738877984160946 RAB40A, member RAS oncogene family-like FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}.; DISEASE: Mental retardation, X-linked, syndromic, Martin-Probst type (MRXSMP) [MIM:300519]: A rare neurodevelopmental disorder characterized by mental retardation, sensorineural hearing loss, short stature and craniofacial dysmorphisms. Patients also exhibit abnormal teeth, widely spaced nipples, abnormal dermatoglyphics, renal insufficiency, and impaired haematopoiesis. Mental retardation is defined as significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:22581972}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, lung, heart, skeletal muscle, kidney and liver. Highest expression in brain. Expressed in fetal brain and kidney. {ECO:0000269|PubMed:12145744, ECO:0000269|PubMed:22581972}.; unclassifiable (Anatomical System);lung;visual apparatus;liver;spleen;kidney;brain; . 0.11505 . 0.463046108 78.58575136 1643.8774 7.49246 RAB40B 0.00383601041524839 0.851363070593067 0.144800918991684 RAB40B, member RAS oncogene family FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland; whole brain;amygdala;medulla oblongata;subthalamic nucleus;occipital lobe;spinal cord;prefrontal cortex;caudate nucleus;cingulate cortex;parietal lobe;skeletal muscle; 0.09938 0.11179 -0.404032746 26.53338051 1287.59417 6.75585 RAB40C 0.113249055305225 0.858770040796227 0.0279809038985488 RAB40C, member RAS oncogene family FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000269|PubMed:15601820}.; . . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;globus pallidus;pons;trigeminal ganglion;skeletal muscle; 0.14042 0.11809 -0.560178693 19.30879925 3.81543 0.14105 RAB41 0.0121821534238742 0.851559856996434 0.136257989579692 RAB41, member RAS oncogene family FUNCTION: Required for normal Golgi ribbon organization and ER-to- Golgi trafficking. {ECO:0000269|PubMed:23936529}.; . TISSUE SPECIFICITY: Widely expressed in brain, testis, lung, heart, ovary, colon, kidney, uterus and spleen but not in liver. {ECO:0000269|PubMed:15018353}.; unclassifiable (Anatomical System);optic nerve;macula lutea;testis;fovea centralis;choroid;lens;retina; . 0.05559 0.08459 -0.317668748 31.45789101 7.84351 0.28850 RAB42 0.00255498366167514 0.336531544490134 0.660913471848191 RAB42, member RAS oncogene family . . . . . 0.09250 . 0.72397987 85.91648974 52.83031 1.44143 RAB42P1 . . . RAB42, member RAS oncogene family, pseudogene 1 . . . . . 0.09250 . 0.72397987 85.91648974 . . RAB43 0.341400602766556 0.600068296742659 0.0585311004907849 RAB43, member RAS oncogene family FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. The low intrinsic GTPase activity of RAB43 is activated by USP6NL. Involved in retrograde transport from the endocytic pathway to the Golgi apparatus. Involved in the transport of Shiga toxin from early and recycling endosomes to the trans-Golgi network. Required for the structural integrity of the Golgi complex. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. {ECO:0000269|PubMed:17562788, ECO:0000269|PubMed:17684057, ECO:0000269|PubMed:18664496, ECO:0000269|PubMed:21255211}.; . TISSUE SPECIFICITY: Widely expressed in brain, testis, lung, heart, ovary, colon, kidney, uterus and spleen but not in liver. {ECO:0000269|PubMed:15018353}.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;globus pallidus;trigeminal ganglion; 0.05559 0.08459 0.169169615 65.33380514 20.97908 0.70955 RAB43P1 . . . RAB43 pseudogene 1 . . . . . . . . . . . RAB44 . . . RAB44, member RAS oncogene family . . . . . 0.16928 0.09949 . . . . RABAC1 0.0765470703257406 0.872426510641271 0.0510264190329881 Rab acceptor 1 FUNCTION: General Rab protein regulator required for vesicle formation from the Golgi complex. May control vesicle docking and fusion by mediating the action of Rab GTPases to the SNARE complexes. In addition it inhibits the removal of Rab GTPases from the membrane by GDI. {ECO:0000250|UniProtKB:O35394}.; . TISSUE SPECIFICITY: Ubiquitous. Strongest expression found in placenta, pituitary gland, kidney, lung and stomach. {ECO:0000269|PubMed:11520070}.; lymphoreticular;medulla oblongata;ovary;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;oesophagus;larynx;bone;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;spleen;head and neck;kidney;mammary gland;aorta;stomach; whole brain; 0.17452 0.13766 -0.185391282 39.67916962 8.12844 0.29871 RABEP1 0.982815073240194 0.0171849230118432 3.74796247733052e-09 rabaptin, RAB GTPase binding effector protein 1 FUNCTION: Rab effector protein acting as linker between gamma- adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Involved in KCNH1 channels trafficking to and from the cell membrane (PubMed:22841712). Stimulates RABGEF1 mediated nucleotide exchange on RAB5A. {ECO:0000269|PubMed:10698684, ECO:0000269|PubMed:11452015, ECO:0000269|PubMed:12773381, ECO:0000269|PubMed:22841712, ECO:0000269|PubMed:8521472}.; . . ovary;salivary gland;intestine;colon;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;larynx;pituitary gland;testis;amniotic fluid;germinal center;bladder;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; temporal lobe;parietal lobe; 0.62580 0.16461 -1.195919584 5.832743572 184.90445 2.95163 RABEP2 0.00273664449583801 0.994419325710312 0.00284402979384951 rabaptin, RAB GTPase binding effector protein 2 FUNCTION: Plays a role in membrane trafficking and in homotypic early endosome fusion. {ECO:0000269|PubMed:9524116}.; . . lymphoreticular;colon;fovea centralis;choroid;skin;retina;corpus callosum;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;dura mater;brain;tonsil;unclassifiable (Anatomical System);meninges;heart;lacrimal gland;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;pia mater;lung;placenta;hippocampus;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;prostate;globus pallidus;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.24554 0.23889 -0.690637458 15.12149092 569.98335 4.84331 RABEPK 4.19209227321727e-06 0.610129772583598 0.389866035324129 Rab9 effector protein with kelch motifs FUNCTION: Rab9 effector required for endosome to trans-Golgi network (TGN) transport. {ECO:0000269|PubMed:9230071}.; . . unclassifiable (Anatomical System);ovary;heart;salivary gland;colon;parathyroid;blood;choroid;skin;uterus;prostate;pancreas;lung;endometrium;oesophagus;nasopharynx;bone;placenta;visual apparatus;alveolus;liver;kidney;germinal center;brain;stomach; caudate nucleus;pons;trigeminal ganglion; 0.07847 0.08513 -0.023789244 52.09365416 1197.77924 6.56646 RABEPKP1 . . . Rab9 effector protein with kelch motifs pseudogene 1 . . . . . . . . . . . RABGAP1 0.999999799770328 2.00229672312506e-07 1.0353271421152e-17 RAB GTPase activating protein 1 FUNCTION: May act as a GTPase-activating protein of RAB6A. May play a role in microtubule nucleation by centrosome. May participate in a RAB6A-mediated pathway involved in the metaphase- anaphase transition. {ECO:0000269|PubMed:10202141, ECO:0000269|PubMed:16395330}.; . . unclassifiable (Anatomical System);prostate;cartilage;spinal cord;colon;germinal center;mammary gland;skeletal muscle; dorsal root ganglion;amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;olfactory bulb;hypothalamus;temporal lobe;pons;caudate nucleus;atrioventricular node;fetal thyroid;skeletal muscle;subthalamic nucleus;fetal brain;thyroid;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.29209 0.11542 -1.50825116 3.503184713 121.41418 2.40018 RABGAP1L 0.0891727139857161 0.910824162047058 3.12396722596501e-06 RAB GTPase activating protein 1-like . . . medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;bladder;tonsil;amygdala;heart;cartilage;blood;lens;skeletal muscle;macula lutea;liver;spleen;peripheral nerve;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; amygdala;dorsal root ganglion;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;ciliary ganglion;whole blood;trigeminal ganglion;cingulate cortex;parietal lobe; 0.37939 . -1.087493118 7.106628922 552.4126 4.78010 RABGAP1L-IT1 . . . RABGAP1L intronic transcript 1 . . . . . . . . . . . RABGEF1 0.496529665997915 0.503285825882055 0.000184508120030639 RAB guanine nucleotide exchange factor (GEF) 1 FUNCTION: Rab effector protein acting as linker between gamma- adaptin, RAB4A or RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates nucleotide exchange on RAB5A. Can act as a ubiquitin ligase (By similarity). {ECO:0000250, ECO:0000269|PubMed:11452015, ECO:0000269|PubMed:15339665, ECO:0000269|PubMed:9323142}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.16465 0.08403 -0.426079032 25.36565228 0.7197 0.01178 RABGGTA 0.00133984157846634 0.998332353809828 0.00032780461170556 Rab geranylgeranyltransferase alpha subunit FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A. {ECO:0000269|PubMed:7991565}.; . . medulla oblongata;colon;fovea centralis;skin;uterus;prostate;frontal lobe;endometrium;larynx;bone;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;trophoblast;heart;islets of Langerhans;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;spleen;kidney;stomach;cerebellum; superior cervical ganglion;subthalamic nucleus; 0.30950 0.13502 -0.753139731 13.67067705 49.34187 1.37449 RABGGTB 0.449469061672224 0.549229479552181 0.00130145877559531 Rab geranylgeranyltransferase beta subunit FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.; . . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;ciliary body;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;trabecular meshwork;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;uterus;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;kidney;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.60703 0.12378 -0.251530012 35.42108988 13.30383 0.48286 RABIF 0.0252902573574674 0.782627790221629 0.192081952420904 RAB interacting factor FUNCTION: Guanine-nucleotide-releasing protein that acts on members of the SEC4/YPT1/RAB subfamily. Stimulates GDP release from both YPT1 and RAB3A, but is less active on these proteins than on the SEC4 protein. Might play a general role in vesicular transport.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.15556 0.12841 -0.007201372 53.19061099 12.8667 0.46924 RABL2A 0.940339177673539 0.0594191310086908 0.000241691317770159 RAB, member of RAS oncogene family-like 2A FUNCTION: Plays an essential role in male fertility, sperm intra- flagellar transport, and tail assembly. Binds, in a GTP-regulated manner, to a specific set of effector proteins including key proteins involved in cilia development and function and delivers them into the growing sperm tail (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the testis. {ECO:0000269|PubMed:23055941}.; . . . 0.09824 0.283038099 71.26680821 604.99814 4.97813 RABL2B 0.765589454248129 0.232585948723316 0.00182459702855535 RAB, member of RAS oncogene family-like 2B . . TISSUE SPECIFICITY: Expressed in the testis. {ECO:0000269|PubMed:23055941}.; medulla oblongata;ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;skeletal muscle;pancreas;lung;placenta;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach; . 0.09613 0.10109 0.371224249 75.12384996 37.72239 1.12261 RABL3 0.136652214705715 0.842929085334455 0.0204186999598307 RAB, member of RAS oncogene family-like 3 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.10894 -0.205617011 38.57631517 19.54182 0.67076 RABL6 0.970513087651376 0.0294851965289995 1.71581962487366e-06 RAB, member RAS oncogene family-like 6 FUNCTION: May enhance cellular proliferation. May reduce growth inhibitory activity of CDKN2A. {ECO:0000269|PubMed:16582619}.; . . . . 0.10622 0.11255 -0.282886048 33.53385232 162.54419 2.78361 RAC1 0.572395052728126 0.42516861526108 0.00243633201079408 ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1) FUNCTION: Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In glioma cells, promotes cell migration and invasion. In podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. Required for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3.; . TISSUE SPECIFICITY: Isoform B is predominantly identified in skin and epithelial tissues from the intestinal tract. Its expression is elevated in colorectal tumors at various stages of neoplastic progression, as compared to their respective adjacent tissues.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;cerebral cortex;oesophagus;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;thymus; whole brain;amygdala;subthalamic nucleus;occipital lobe;thalamus;hypothalamus;spinal cord;prefrontal cortex;globus pallidus;caudate nucleus;cingulate cortex;parietal lobe; 0.98840 0.47945 -0.163345027 41.24793583 4.72747 0.17143 RAC1P1 . . . ras-related C3 botulinum toxin substrate 1 pseudogene 1 . . . . . . . . . . . RAC1P2 . . . ras-related C3 botulinum toxin substrate 1 pseudogene 2 . . . . . . . . . . . RAC1P3 . . . ras-related C3 botulinum toxin substrate 1 pseudogene 3 . . . . . . . . . . . RAC1P4 . . . ras-related C3 botulinum toxin substrate 1 pseudogene 4 . . . . . . . . . . . RAC1P5 . . . ras-related C3 botulinum toxin substrate 1 pseudogene 5 . . . . . . . . . . . RAC1P6 . . . ras-related C3 botulinum toxin substrate 1 pseudogene 6 . . . . . . . . . . . RAC1P7 . . . ras-related C3 botulinum toxin substrate 1 pseudogene 7 . . . . . . . . . . . RAC1P8 . . . ras-related C3 botulinum toxin substrate 1 pseudogene 8 . . . . . . . . . . . RAC1P9 . . . ras-related C3 botulinum toxin substrate 1 pseudogene 9 . . . . . . . . . . . RAC2 0.873092320404228 0.125254151905792 0.00165352768997987 ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2) FUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the production of reactive oxygen species (ROS) by NADPH oxidase. {ECO:0000269|PubMed:1660188}.; DISEASE: Neutrophil immunodeficiency syndrome (NEUID) [MIM:608203]: An immunodeficiency syndrome due to defective neutrophils. Affected individuals present with leukocytosis, neutrophilia, severe recurrent bacterial infections and poor wound healing. {ECO:0000269|PubMed:10758162}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Hematopoietic specific.; lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; lymph node;lung;heart;tumor;white blood cells;whole blood;tonsil;thymus;bone marrow; 0.94057 0.55950 -0.295622497 32.61972163 4.56287 0.16451 RAC3 0.0354422485411882 0.82859566662111 0.135962084837702 ras-related C3 botulinum toxin substrate 3 (rho family, small GTP binding protein Rac3) FUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as cell spreading and the formation of actin-based protusions including lamellipodia and membrane ruffles. Promotes cell adhesion and spreading on fibrinogen in a CIB1 and alpha-IIb/beta3 integrin-mediated manner. {ECO:0000269|PubMed:11756406, ECO:0000269|PubMed:11956649}.; . TISSUE SPECIFICITY: Highest levels in brain, also detected in heart, placenta and pancreas.; unclassifiable (Anatomical System);bile duct;lung;whole body;adrenal gland;testis;colon;choroid;brain;stomach;peripheral nerve; whole brain;atrioventricular node; 0.92514 0.19444 -0.05129383 49.75819769 6.90502 0.25681 RACGAP1 0.786373400640943 0.213626115222736 4.84136321556091e-07 Rac GTPase activating protein 1 FUNCTION: Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells. {ECO:0000269|PubMed:10979956, ECO:0000269|PubMed:11085985, ECO:0000269|PubMed:11278976, ECO:0000269|PubMed:11782313, ECO:0000269|PubMed:14729465, ECO:0000269|PubMed:15642749, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16129829, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302, ECO:0000269|PubMed:23235882, ECO:0000269|PubMed:9497316}.; . TISSUE SPECIFICITY: Highly expressed in testis, thymus and placenta. Expressed at lower levels in spleen and peripheral blood lymphocytes. In testis, expression is restricted to germ cells with the highest levels of expression found in spermatocytes. Expression is regulated in a cell cycle-dependent manner and peaks during G2/M phase. {ECO:0000269|PubMed:10979956, ECO:0000269|PubMed:11278976, ECO:0000269|PubMed:12590651, ECO:0000269|PubMed:9497316}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);heart;urinary;pharynx;blood;lens;bile duct;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;tumor;testis;skeletal muscle; 0.33109 0.15859 -0.402212257 26.7338995 52.39059 1.43154 RACGAP1P . . . Rac GTPase activating protein 1 pseudogene . . . . . . . . . . . RACK1 . . . receptor for activated C kinase 1 FUNCTION: Involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression. Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand- independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (PubMed:19674157). Binds to Y.pseudotuberculosis yopK which leads to inhibition of phagocytosis and survival of bacteria following infection of host cells. Enhances phosphorylation of HIV-1 Nef by PKCs. Promotes migration of breast carcinoma cells by binding to and activating RHOA. {ECO:0000269|PubMed:11312657, ECO:0000269|PubMed:11884618, ECO:0000269|PubMed:12589061, ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:17108144, ECO:0000269|PubMed:17244529, ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:18088317, ECO:0000269|PubMed:18258429, ECO:0000269|PubMed:18621736, ECO:0000269|PubMed:19423701, ECO:0000269|PubMed:19674157, ECO:0000269|PubMed:19785988, ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20541605, ECO:0000269|PubMed:20573744, ECO:0000269|PubMed:20976005, ECO:0000269|PubMed:21212275, ECO:0000269|PubMed:21347310, ECO:0000269|PubMed:9584165}.; . TISSUE SPECIFICITY: In the liver, expressed at higher levels in activated hepatic stellate cells than in hepatocytes or Kupffer cells. Up-regulated in hepatocellular carcinomas and in the adjacent non-tumor liver tissue. {ECO:0000269|PubMed:18621736}.; . . 0.15130 0.16557 -0.09720619 46.20193442 . . RAD1 0.000186646011793966 0.708728116276915 0.291085237711291 RAD1 checkpoint DNA exonuclease FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity. {ECO:0000269|PubMed:21659603, ECO:0000269|PubMed:9660799}.; . TISSUE SPECIFICITY: Expressed in testis, uterus, bladder, spleen, ovaries, lung, brain and muscle (at protein level). {ECO:0000269|PubMed:9716408}.; ovary;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.38309 0.14896 0.194852702 67.03231894 437.32146 4.35926 RAD1P1 . . . RAD1 pseudogene 1 . . . . . . . . . . . RAD1P2 . . . RAD1 pseudogene 2 . . . . . . . . . . . RAD9A 0.00232537793665103 0.924243245197476 0.073431376865873 RAD9 checkpoint clamp component A FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex. {ECO:0000269|PubMed:10713044, ECO:0000269|PubMed:21659603}.; . . lymphoreticular;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;synovium;larynx;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.51119 0.19706 -0.334253673 30.70299599 139.60424 2.57579 RAD9B 3.62698610369545e-05 0.820851507510509 0.179112222628454 RAD9 checkpoint clamp component B . . TISSUE SPECIFICITY: Expressed in testis and skeletal muscle. {ECO:0000269|PubMed:14500360, ECO:0000269|PubMed:14611806}.; lung;visual apparatus;testis;skin; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.27072 0.09522 0.639420866 83.8995046 316.72218 3.78094 RAD17 0.00769743491101139 0.992172918057604 0.000129647031385176 RAD17 checkpoint clamp loader component FUNCTION: Essential for sustained cell growth, maintenance of chromosomal stability, and ATR-dependent checkpoint activation upon DNA damage. Has a weak ATPase activity required for binding to chromatin. Participates in the recruitment of the RAD1-RAD9- HUS1 complex and RHNO1 onto chromatin, and in CHEK1 activation. May also serve as a sensor of DNA replication progression, and may be involved in homologous recombination. {ECO:0000269|PubMed:10208430, ECO:0000269|PubMed:11418864, ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:12578958, ECO:0000269|PubMed:12672690, ECO:0000269|PubMed:14500819, ECO:0000269|PubMed:14624239, ECO:0000269|PubMed:15235112, ECO:0000269|PubMed:15538388, ECO:0000269|PubMed:21659603}.; . TISSUE SPECIFICITY: Overexpressed in various cancer cell lines and in colon carcinoma (at protein level). Isoform 2 and isoform 3 are the most abundant isoforms in non irradiated cells (at protein level). Ubiquitous at low levels. Highly expressed in testis, where it is expressed within the germinal epithelium of the seminiferous tubuli. Weakly expressed in seminomas (testicular tumors). {ECO:0000269|PubMed:10208430, ECO:0000269|PubMed:10232579, ECO:0000269|PubMed:10480350, ECO:0000269|PubMed:11602352, ECO:0000269|PubMed:9660800}.; lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.37653 0.20695 -0.066061882 48.77919321 3538.4722 11.47373 RAD17P1 . . . RAD17 checkpoint clamp loader component pseudogene 1 . . . . . . . . . . . RAD17P2 . . . RAD17 checkpoint clamp loader component pseudogene 2 . . . . . . . . . . . RAD18 5.20372835528497e-05 0.967718892783347 0.0322290699331004 RAD18, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap- filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono- ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity. {ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:21659603}.; . . ovary;salivary gland;intestine;colon;skin;uterus;whole body;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;skeletal muscle;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.25223 0.07995 0.042348793 57.31304553 206.45514 3.10413 RAD21 0.999544949425601 0.000455049020963184 1.55343606052114e-09 RAD21 cohesin complex component FUNCTION: Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle, in DNA repair, and in apoptosis. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by separase/ESPL1 and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Also plays a role in apoptosis, via its cleavage by caspase-3/CASP3 or caspase-7/CASP7 during early steps of apoptosis: the C-terminal 64 kDa cleavage product may act as a nuclear signal to initiate cytoplasmic events involved in the apoptotic pathway. {ECO:0000269|PubMed:11875078, ECO:0000269|PubMed:12417729}.; DISEASE: Cornelia de Lange syndrome 4 (CDLS4) [MIM:614701]: A form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. It is characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies. {ECO:0000269|PubMed:22633399}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; amygdala;occipital lobe;medulla oblongata;fetal brain;thyroid;prefrontal cortex;globus pallidus;testis; 0.97015 0.19298 -0.514264485 21.41424864 75.51422 1.81847 RAD21-AS1 . . . RAD21 antisense RNA 1 . . . . . . . . . . . RAD21L1 . . . RAD21 cohesin complex component like 1 FUNCTION: Meiosis-specific component of some cohesin complex required during the initial steps of prophase I in male meiosis. Probably required during early meiosis in males for separation of sister chromatids and homologous chromosomes. Replaces RAD21 in premeiotic S phase (during early stages of prophase I), while RAD21 reappears in later stages of prophase I. Involved in synaptonemal complex assembly, synapsis initiation and crossover recombination between homologous chromosomes during prophase I (By similarity). {ECO:0000250}.; . . . . . . 0.769889969 86.95447039 4420.50458 13.31330 RAD23A 0.0392565362650634 0.953968381568931 0.00677508216600568 RAD23 homolog A, nucleotide excision repair protein FUNCTION: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome.; FUNCTION: Involved in vpr-dependent replication of HIV-1 in non- proliferating cells and primary macrophages. Required for the association of HIV-1 vpr with the host proteasome.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;iris;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;greater omentum;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;duodenum;kidney;stomach; fetal liver;skeletal muscle;bone marrow; 0.75777 0.19913 0.373041938 75.29488087 343.62896 3.93038 RAD23B 0.973409007097557 0.0265844319482735 6.56095416961768e-06 RAD23 homolog B, nucleotide excision repair protein FUNCTION: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum- associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome.; FUNCTION: The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pineal body;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;oral cavity;pancreas;lung;cornea;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta;thymus; amygdala;superior cervical ganglion;placenta;skeletal muscle;cerebellum; 0.62349 0.24261 -0.137658575 43.57159707 1593.76636 7.38535 RAD23BLP . . . RAD23 homolog B-like (S. cerevisiae) pseudogene . . . . . . . . . . . RAD23BP1 . . . RAD23 homolog B, nucleotide excision repair protein pseudogene 1 . . . . . . . . . . . RAD23BP2 . . . RAD23 homolog B, nucleotide excision repair protein pseudogene 2 . . . . . . . . . . . RAD50 3.45027967852237e-15 0.992354993202805 0.00764500679719119 RAD50 double strand break repair protein FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand- specific 3'-5' exonuclease activity, which are provided by MRE11A. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11A to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation. {ECO:0000269|PubMed:10888888, ECO:0000269|PubMed:11741547, ECO:0000269|PubMed:15064416, ECO:0000269|PubMed:9590181, ECO:0000269|PubMed:9651580, ECO:0000269|PubMed:9705271}.; DISEASE: Nijmegen breakage syndrome-like disorder (NBSLD) [MIM:613078]: A disorder similar to Nijmegen breakage syndrome and characterized by chromosomal instability, radiation sensitivity, microcephaly, growth retardation, short stature and bird-like face. Immunodeficiency is absent. {ECO:0000269|PubMed:19409520}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at very low level in most tissues, except in testis where it is expressed at higher level. Expressed in fibroblasts. {ECO:0000269|PubMed:8756642}.; ovary;sympathetic chain;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;artery;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;trigeminal ganglion;skeletal muscle; 0.75384 0.58646 -0.501537595 21.83887709 175.25604 2.87907 RAD51 0.99041808754591 0.00957928046474953 2.63198934082282e-06 RAD51 recombinase FUNCTION: Participates in a common DNA damage response pathway associated with the activation of homologous recombination and double-strand break repair. Binds to single and double-stranded DNA and exhibits DNA-dependent ATPase activity. Underwinds duplex DNA and forms helical nucleoprotein filaments. Part of a PALB2- scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. {ECO:0000269|PubMed:12205100, ECO:0000269|PubMed:12442171, ECO:0000269|PubMed:18417535, ECO:0000269|PubMed:20231364, ECO:0000269|PubMed:20348101, ECO:0000269|PubMed:20413593, ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:23754376}.; DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:10807537}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Mirror movements 2 (MRMV2) [MIM:614508]: A disorder characterized by contralateral involuntary movements that mirror voluntary ones. While mirror movements are occasionally found in young children, persistence beyond the age of 10 is abnormal. Mirror movements occur more commonly in the upper extremities. {ECO:0000269|PubMed:22305526}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in testis and thymus, followed by small intestine, placenta, colon, pancreas and ovary. Weakly expressed in breast.; unclassifiable (Anatomical System);medulla oblongata;heart;ovary;adrenal cortex;colon;skin;skeletal muscle;bone marrow;breast;uterus;prostate;lung;endometrium;bone;placenta;visual apparatus;hypopharynx;duodenum;liver;head and neck;kidney;brain;stomach; superior cervical ganglion;temporal lobe;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.99998 0.95880 -0.139478553 43.29440906 27.3455 0.88074 RAD51-AS1 . . . RAD51 antisense RNA 1 (head to head) . . . . . . . . . . . RAD51AP1 0.0223532839828689 0.962120083487802 0.015526632529329 RAD51 associated protein 1 FUNCTION: May participate in a common DNA damage response pathway associated with the activation of homologous recombination and double-strand break repair. Functionally cooperates with PALB2 in promoting of D-loop formation by RAD51. Binds to single and double stranded DNA, and is capable of aggregating DNA. Also binds RNA. {ECO:0000269|PubMed:20871616, ECO:0000269|PubMed:9396801}.; . TISSUE SPECIFICITY: Highly expressed in testis and thymus. Lower levels in colon and small intestine. Little or no expression in spleen, prostate, ovary and peripheral blood leukocytes. {ECO:0000269|PubMed:9396801}.; ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);pharynx;blood;bile duct;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;tumor;trigeminal ganglion; 0.34314 0.08519 0.907624513 89.46685539 370.58875 4.06586 RAD51AP1P1 . . . RAD51 associated protein 1 pseudogene 1 . . . . . . . . . . . RAD51AP2 1.70293206079099e-18 0.000835972243891466 0.999164027756108 RAD51 associated protein 2 . . TISSUE SPECIFICITY: Specifically expressed in meiotic tissues. Highly expressed in testis. {ECO:0000269|PubMed:16990250}.; . . . . 1.298854499 93.91365888 328.78223 3.85529 RAD51B 1.45736567534375e-09 0.108047608527258 0.891952390015376 RAD51 paralog B FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. May promote the assembly of presynaptic RAD51 nucleoprotein filaments. Binds single-stranded DNA and double-stranded DNA and has DNA-dependent ATPase activity. Part of the RAD21 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity suggesting an involvement in early stages of the HR pathway. {ECO:0000269|PubMed:11751635, ECO:0000269|PubMed:11751636, ECO:0000269|PubMed:11842113, ECO:0000269|PubMed:12441335, ECO:0000269|PubMed:23108668, ECO:0000269|PubMed:23149936}.; DISEASE: Note=A chromosomal aberration involving RAD51B is found in pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23- 24) with HMGA1. {ECO:0000269|PubMed:11978964}.; DISEASE: Note=A chromosomal aberration involving RAD51B is found in uterine leiomyoma. Translocation t(12;14)(q15;q23-24) with HMGA2. {ECO:0000269|PubMed:12649198, ECO:0000269|PubMed:9892177}.; TISSUE SPECIFICITY: Expressed in a wide range of tissues.; unclassifiable (Anatomical System);lung;mesenchyma;testis;spleen; dorsal root ganglion;superior cervical ganglion;uterus corpus;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex;cerebellum; 0.17794 0.10218 0.92967242 89.79122435 349.16909 3.95957 RAD51C 4.27808774468152e-09 0.195397780599171 0.804602215122741 RAD51 paralog C FUNCTION: Essential for the homologous recombination (HR) pathway of DNA repair. Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Part of the RAD21 paralog protein complexes BCDX2 and CX3 which act at different stages of the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 seems to act downstream of BRCA2 recruitment and upstream of RAD51 recruitment; CX3 seems to act downstream of RAD51 recruitment; both complexes bind predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity suggesting an involvement in early stages of the HR pathway. Involved in RAD51 foci formation in response to DNA damage suggesting an involvement in early stages of HR probably in the invasion step. Has an early function in DNA repair in facilitating phosphorylation of the checkpoint kinase CHEK2 and thereby transduction of the damage signal, leading to cell cycle arrest and HR activation. Participates in branch migration and HJ resolution and thus is important for processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex. Part of a PALB2-scaffolded HR complex containing BRCA2 and which is thought to play a role in DNA repair by HR. Protects RAD51 from ubiquitin-mediated degradation that is enhanced following DNA damage. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and XRCC3. Contributes to DNA cross-link resistance, sister chromatid cohesion and genomic stability. Involved in maintaining centrosome number in mitosis. {ECO:0000269|PubMed:14716019, ECO:0000269|PubMed:16215984, ECO:0000269|PubMed:16395335, ECO:0000269|PubMed:19451272, ECO:0000269|PubMed:19783859, ECO:0000269|PubMed:20413593, ECO:0000269|PubMed:23108668, ECO:0000269|PubMed:23149936}.; DISEASE: Fanconi anemia complementation group O (FANCO) [MIM:613390]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:20400963}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Breast-ovarian cancer, familial, 3 (BROVCA3) [MIM:613399]: A condition associated with familial predisposition to cancer of the breast and ovaries. Characteristic features in affected families are an early age of onset of breast cancer (often before age 50), increased chance of bilateral cancers (cancer that develop in both breasts, or both ovaries, independently), frequent occurrence of breast cancer among men, increased incidence of tumors of other specific organs, such as the prostate. {ECO:0000269|PubMed:20400964, ECO:0000269|PubMed:21990120}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in a variety of tissues, with highest expression in testis, heart muscle, spleen and prostate.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;breast;lung;cornea;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; whole brain;amygdala;subthalamic nucleus;occipital lobe;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;cingulate cortex; 0.85079 0.16604 0.106667882 61.73036093 60.56289 1.58201 RAD51D 6.18804564528162e-07 0.678061937816514 0.321937443378921 RAD51 paralog D FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Bind to single- stranded DNA (ssDNA) and has DNA-dependent ATPase activity. Part of the Rad21 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single- stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. Involved in telomere maintenance. The BCDX2 subcomplex XRCC2:RAD51D can stimulate Holliday junction resolution by BLM. {ECO:0000269|PubMed:10871607, ECO:0000269|PubMed:11751635, ECO:0000269|PubMed:11834724, ECO:0000269|PubMed:11842113, ECO:0000269|PubMed:12975363, ECO:0000269|PubMed:15109494, ECO:0000269|PubMed:23149936}.; . TISSUE SPECIFICITY: Expressed in colon, prostate, spleen, testis, ovary, thymus and small intestine. Weakly expressed in leukocytes.; unclassifiable (Anatomical System);heart;islets of Langerhans;urinary;colon;skin;uterus;pancreas;prostate;lung;frontal lobe;endometrium;thyroid;bone;placenta;liver;testis;cervix;spleen;germinal center;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;appendix;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.45766 . 0.532823122 80.96249115 21.07912 0.71347 RAD52 2.38441629175774e-07 0.711727582547236 0.288272179011135 RAD52 homolog, DNA repair protein FUNCTION: Involved in double-stranded break repair. Plays a central role in genetic recombination and DNA repair by promoting the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase. {ECO:0000269|PubMed:12379650, ECO:0000269|PubMed:8702565}.; . . unclassifiable (Anatomical System);cartilage;heart;tongue;colon;fovea centralis;breast;uterus;whole body;lung;macula lutea;liver;testis;head and neck;spleen;germinal center;kidney;brain;mammary gland; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.72190 0.41509 0.507139401 80.10143902 186.7787 2.96787 RAD54B 8.51438445753387e-10 0.888980166368406 0.111019832780156 RAD54 homolog B (S. cerevisiae) FUNCTION: Involved in DNA repair and mitotic recombination. May play an active role in recombination processes in concert with other members of the RAD52 epistasis group. {ECO:0000269|PubMed:11782437, ECO:0000269|PubMed:11884632}.; . TISSUE SPECIFICITY: Abundantly expressed in testis and spleen. Relatively low levels observed in thymus, prostate, ovary and colon. {ECO:0000269|PubMed:10362364}.; ovary;colon;parathyroid;choroid;fovea centralis;skin;bone marrow;retina;optic nerve;cochlea;thyroid;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;blood;lens;lung;placenta;macula lutea;liver;head and neck;cervix;kidney;stomach; superior cervical ganglion;testis - seminiferous tubule; 0.48615 0.14369 0.402364592 76.45081387 199.85362 3.05404 RAD54L 2.73718135268854e-13 0.409566683951366 0.59043331604836 RAD54-like (S. cerevisiae) FUNCTION: Involved in DNA repair and mitotic recombination. Functions in the recombinational DNA repair (RAD52) pathway. Dissociates RAD51 from nucleoprotein filaments formed on dsDNA. Could be involved in the turnover of RAD51 protein-dsDNA filaments (By similarity). May play also an essential role in telomere length maintenance and telomere capping in mammalian cells. {ECO:0000250, ECO:0000269|PubMed:11459989, ECO:0000269|PubMed:12205100, ECO:0000269|PubMed:9774452}.; . . . . 0.83074 0.14769 -0.372889896 28.20240623 175.69413 2.88424 RAD54L2 0.999999053426257 9.46573742818498e-07 4.55356560179519e-16 RAD54-like 2 (S. cerevisiae) FUNCTION: DNA helicase that modulates androgen receptor (AR)- dependent transactivation in a promoter-dependent manner. Not able to remodel mononucleosomes in vitro (By similarity). {ECO:0000250}.; . . ovary;parathyroid;vein;skin;bone marrow;uterus;prostate;cochlea;endometrium;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;muscle;blood;skeletal muscle;lung;epididymis;placenta;visual apparatus;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.99916 0.09309 -1.390744555 4.305260675 250.4185 3.40911 RADIL 1.30554853556863e-12 0.0891378366300764 0.910862163368618 Ras association and DIL domains FUNCTION: Downstream effector of Rap required for cell adhesion and migration of neural crest precursors during development. {ECO:0000269|PubMed:17704304}.; . . unclassifiable (Anatomical System);ovary;spinal cord;skin;whole body;lung;endometrium;visual apparatus;testis;head and neck;kidney;mammary gland;brain;thymus; skeletal muscle; . . 0.236922632 68.73083274 3259.52862 10.87748 RAE1 0.991169300003019 0.00883026370859505 4.36288386448728e-07 ribonucleic acid export 1 FUNCTION: Binds mRNA. May function in nucleocytoplasmic transport and in directly or indirectly attaching cytoplasmic mRNPs to the cytoskeleton.; . . . . 0.49719 0.19444 -0.205617011 38.57631517 49.11228 1.36992 RAET1E 1.85957575867062e-05 0.45402575853045 0.545955645711964 retinoic acid early transcript 1E FUNCTION: Ligand for the KLRK1 receptor. Delivers activating signals to NK cells and promotes tumor immune surveillance by inducing the expansion of anti-tumor cytotoxic lymphocytes.; . TISSUE SPECIFICITY: Predominantly expressed in the skin, but also expressed in testis and trachea. Up-regulated in tumor cells of different origins. Expression progressively decreased after treatment of tumor cells with retinoic acid. {ECO:0000269|PubMed:12732206, ECO:0000269|PubMed:14508119}.; optic nerve;macula lutea;fovea centralis;choroid;lens;retina; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.03332 0.12047 2.149758993 97.97711724 1343.90882 6.88288 RAET1E-AS1 . . . RAET1E antisense RNA 1 . . . . . . . . . . . RAET1F . . . retinoic acid early transcript 1F pseudogene . . . . . . . . . . . RAET1G 0.00147072916271158 0.673933352093366 0.324595918743922 retinoic acid early transcript 1G FUNCTION: Acts as a ligand for the KLRK1 receptor and mediates NK cell cytotoxicity via the receptor. {ECO:0000269|PubMed:15240696}.; . TISSUE SPECIFICITY: Isoform 1 is highly expressed in colon and in a number of tumor cell lines and highly restricted in normal tissues. Both isoforms are frequently expressed in cell lines derived from epithelial cancers, and in primary breast cancers. {ECO:0000269|PubMed:15240696, ECO:0000269|PubMed:19223974}.; . . 0.07649 0.05401 1.907156687 97.38145789 66.79305 1.68650 RAET1K . . . retinoic acid early transcript 1K pseudogene . . . . . . . . . . . RAET1L 0.00020020961846237 0.484579283127827 0.51522050725371 retinoic acid early transcript 1L . . TISSUE SPECIFICITY: Widely expressed in non-hemopoietic and non- intestinal tissues. {ECO:0000269|PubMed:11827464}.; unclassifiable (Anatomical System);lung;tongue;bone;hypopharynx;head and neck;skeletal muscle; . 0.09005 0.07059 2.839026422 99.10945978 1696.76749 7.59590 RAET1M . . . retinoic acid early transcript 1M pseudogene . . . . . . . . . . . RAF1 0.999776866110749 0.000223133833869176 5.53819998824154e-11 Raf-1 proto-oncogene, serine/threonine kinase FUNCTION: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2- antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation. {ECO:0000269|PubMed:11427728, ECO:0000269|PubMed:11719507, ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:15618521, ECO:0000269|PubMed:15849194, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:16924233, ECO:0000269|PubMed:9360956}.; DISEASE: Noonan syndrome 5 (NS5) [MIM:611553]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. {ECO:0000269|PubMed:17603482, ECO:0000269|PubMed:17603483, ECO:0000269|PubMed:20683980}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: LEOPARD syndrome 2 (LPRD2) [MIM:611554]: A disorder characterized by lentigines, electrocardiographic conduction abnormalities, ocular hypertelorism, pulmonic stenosis, abnormalities of genitalia, retardation of growth, and sensorineural deafness. {ECO:0000269|PubMed:17603483}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1NN (CMD1NN) [MIM:615916]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:24777450}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In skeletal muscle, isoform 1 is more abundant than isoform 2. {ECO:0000269|PubMed:1886707}.; ovary;umbilical cord;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;trachea;placenta;amnion;kidney;stomach;aorta;thymus; superior cervical ganglion;ciliary ganglion;whole blood;skeletal muscle; 0.99869 0.93060 -0.646543901 16.44255721 87.82499 2.00185 RAF1P1 . . . RAF1 pseudogene 1 . . . . . . . . . . . RAG1 0.00189800110752859 0.975423011927332 0.0226789869651396 recombination activating gene 1 FUNCTION: Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T- lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. In the RAG complex, RAG1 mediates the DNA-binding to the conserved recombination signal sequences (RSS) and catalyzes the DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. RAG2 is not a catalytic component but is required for all known catalytic activities. DNA cleavage occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'- hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'- phosphorylated ends. The chromatin structure plays an essential role in the V(D)J recombination reactions and the presence of histone H3 trimethylated at 'Lys-4' (H3K4me3) stimulates both the nicking and haipinning steps. The RAG complex also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. The introduction of DNA breaks by the RAG complex on one immunoglobulin allele induces ATM-dependent repositioning of the other allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. In addition to its endonuclease activity, RAG1 also acts as a E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3. Histone H3 monoubiquitination is required for the joining step of V(D)J recombination. Mediates polyubiquitination of KPNA1 (By similarity). {ECO:0000250}.; DISEASE: Combined cellular and humoral immune defects with granulomas (CHIDG) [MIM:233650]: Immunodeficiency disease with granulomas in the skin, mucous membranes, and internal organs. Other characteristics include hypogammaglobulinemia, a diminished number of T and B-cells, and sparse thymic tissue on ultrasonography. {ECO:0000269|PubMed:18463379}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Severe combined immunodeficiency autosomal recessive T- cell-negative/B-cell-negative/NK-cell-positive (T(-)B(-)NK(+) SCID) [MIM:601457]: A form of severe combined immunodeficiency (SCID), a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development. {ECO:0000269|PubMed:19912631, ECO:0000269|PubMed:8810255}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Omenn syndrome (OS) [MIM:603554]: Severe immunodeficiency characterized by the presence of activated, anergic, oligoclonal T-cells, hypereosinophilia, and high IgE levels. {ECO:0000269|PubMed:10606976, ECO:0000269|PubMed:11133745, ECO:0000269|PubMed:19912631, ECO:0000269|PubMed:21624848, ECO:0000269|PubMed:21771083, ECO:0000269|PubMed:9630231}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Alpha/beta T-cell lymphopenia, with gamma/delta T-cell expansion, severe cytomegalovirus infection and autoimmunity (T- CMVA) [MIM:609889]: An immunological disorder characterized by oligoclonal expansion of TCR gamma/delta T-cells, TCR alpha/beta T-cell lymphopenia, severe, disseminated cytomegalovirus infection and autoimmune cytopenia. {ECO:0000269|PubMed:16276422}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Maturing lymphoid cells.; unclassifiable (Anatomical System);pancreas;lung;testis;thymus;bone marrow; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;thymus; 0.26882 0.57182 -0.367438677 28.29087049 2251.23465 8.76351 RAG2 0.0105193118193894 0.830988437071249 0.158492251109362 recombination activating gene 2 FUNCTION: Core component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T- lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. DNA cleavage by the RAG complex occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. The chromatin structure plays an essential role in the V(D)J recombination reactions and the presence of histone H3 trimethylated at 'Lys-4' (H3K4me3) stimulates both the nicking and haipinning steps. The RAG complex also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B- cell antigen receptor (BCR) expressed on individual B-lymphocytes. The introduction of DNA breaks by the RAG complex on one immunoglobulin allele induces ATM-dependent repositioning of the other allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. In the RAG complex, RAG2 is not the catalytic component but is required for all known catalytic activities mediated by RAG1. It probably acts as a sensor of chromatin state that recruits the RAG complex to H3K4me3 (By similarity). {ECO:0000250}.; DISEASE: Combined cellular and humoral immune defects with granulomas (CHIDG) [MIM:233650]: Immunodeficiency disease with granulomas in the skin, mucous membranes, and internal organs. Other characteristics include hypogammaglobulinemia, a diminished number of T and B-cells, and sparse thymic tissue on ultrasonography. {ECO:0000269|PubMed:18463379}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Severe combined immunodeficiency autosomal recessive T- cell-negative/B-cell-negative/NK-cell-positive (T(-)B(-)NK(+) SCID) [MIM:601457]: A form of severe combined immunodeficiency (SCID), a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development. {ECO:0000269|PubMed:8810255}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Omenn syndrome (OS) [MIM:603554]: Severe immunodeficiency characterized by the presence of activated, anergic, oligoclonal T-cells, hypereosinophilia, and high IgE levels. {ECO:0000269|PubMed:9630231}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Cells of the B- and T-lymphocyte lineages.; lymph node;lung;testis;thymus; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.08579 0.60680 0.020302773 55.60863411 272.86413 3.54108 RAI1 0.999136111876994 0.000863888061636037 6.13699051698234e-11 retinoic acid induced 1 FUNCTION: Transcriptional regulator of the circadian clock components: CLOCK, ARNTL/BMAL1, ARNTL2/BMAL2, PER1/3, CRY1/2, NR1D1/2 and RORA/C. Positively regulates the transcriptional activity of CLOCK a core component of the circadian clock. Regulates transcription through chromatin remodeling by interacting with other proteins in chromatin as well as proteins in the basic transcriptional machinery. May be important for embryonic and postnatal development. May be involved in neuronal differentiation. {ECO:0000269|PubMed:22578325}.; DISEASE: Smith-Magenis syndrome (SMS) [MIM:182290]: Characterized by congenital mental retardation associated with development and growth delays. Affected persons have characteristic behavioral abnormalities, including self-injurious behaviors and sleep disturbance, and distinct craniofacial and skeletal anomalies. {ECO:0000269|PubMed:11404004, ECO:0000269|PubMed:12652298}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues examined with higher expression in the heart and brain. No expression was seen in the corpus callosum of the brain. {ECO:0000269|PubMed:12837267}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;larynx;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;lens;breast;pancreas;lung;placenta;macula lutea;duodenum;liver;spleen;head and neck;cervix;kidney;stomach;thymus; superior cervical ganglion;globus pallidus;pons;trigeminal ganglion;skeletal muscle; 0.13693 0.11743 -3.683732498 0.253597547 223.68182 3.23449 RAI1-AS1 . . . RAI1 antisense RNA 1 . . . . . . . . . . . RAI2 0.298853666814438 0.623392024539448 0.0777543086461141 retinoic acid induced 2 . . . unclassifiable (Anatomical System);lymph node;heart;ovary;islets of Langerhans;parathyroid;lens;retina;uterus;pancreas;prostate;optic nerve;lung;cerebral cortex;endometrium;thyroid;placenta;kidney;brain;gall bladder;thymus; . 0.78262 0.09964 -0.424258538 25.56027365 30.16691 0.96255 RAI14 0.487656416164767 0.512341945511274 1.63832395930888e-06 retinoic acid induced 14 . . TISSUE SPECIFICITY: Highly expressed in placenta, muscle, kidney and testis. Moderately expressed in heart, brain, lung, liver and intestine. Isoform 2 is widely expressed and expressed in fetal and adult testes, and spermatozoa. {ECO:0000269|PubMed:11042181, ECO:0000269|PubMed:11168586, ECO:0000269|PubMed:16110356}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;oesophagus;larynx;bone;thyroid;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;lens;skeletal muscle;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;uterus;uterus corpus;olfactory bulb;smooth muscle;placenta;trigeminal ganglion; 0.24420 0.11401 -0.216746887 37.69757018 3767.60269 12.00361 RALA 0.950372431421878 0.0494751983576456 0.000152370220475982 v-ral simian leukemia viral oncogene homolog A (ras related) FUNCTION: Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Plays a role in the early stages of cytokinesis and is required to tether the exocyst to the cytokinetic furrow. The RALA-exocyst complex regulates integrin- dependent membrane raft exocytosis and growth signaling. Key regulator of LPAR1 signaling and competes with ADRBK1 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage-independent proliferation of transformed cells. {ECO:0000269|PubMed:18756269, ECO:0000269|PubMed:19306925, ECO:0000269|PubMed:20005108}.; . . smooth muscle;ovary;skin;retina;prostate;optic nerve;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;adrenal gland;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; superior cervical ganglion;smooth muscle;tongue;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.35244 0.31462 0.323496558 72.93583392 4.62331 0.16589 RALB 0.193989190711601 0.758782119811383 0.0472286894770158 v-ral simian leukemia viral oncogene homolog B FUNCTION: Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells. Plays a role in the late stages of cytokinesis and is required for the abscission of the bridge joining the sister cells emerging from mitosis. Required for suppression of apoptosis. {ECO:0000269|PubMed:18756269}.; . . myocardium;ovary;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;hypothalamus;adrenal cortex;blood;lens;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;trigeminal ganglion; 0.37582 0.13315 -0.141298762 42.87567823 15.56303 0.55493 RALBP1 0.670181325366825 0.329775840024964 4.28346082114271e-05 ralA binding protein 1 FUNCTION: Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin. {ECO:0000269|PubMed:11437348, ECO:0000269|PubMed:12775724, ECO:0000269|PubMed:7673236}.; . TISSUE SPECIFICITY: Expressed ubiquitously but at low levels. Shows a strong expression in the erythrocytes. {ECO:0000269|PubMed:11437348}.; sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;tongue;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;placenta;head and neck;kidney;stomach;thymus; amygdala;occipital lobe;subthalamic nucleus;prostate;superior cervical ganglion;olfactory bulb;tongue;placenta;globus pallidus;pons;atrioventricular node;cingulate cortex; 0.13198 0.17103 -0.380166007 27.88393489 78.91347 1.87623 RALGAPA1 0.999999978076686 2.19233143663562e-08 3.24873289122752e-24 Ral GTPase activating protein catalytic alpha subunit 1 FUNCTION: Catalytic subunit of the heterodimeric RalGAP1 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15498464}.; colon;skin;bone marrow;retina;uterus;cochlea;endometrium;larynx;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;spleen;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;amygdala;superior cervical ganglion;thalamus;medulla oblongata;occipital lobe;hypothalamus;spinal cord;caudate nucleus;atrioventricular node;skeletal muscle;uterus corpus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.75239 0.12918 -1.210720546 5.708893607 2267.65022 8.80210 RALGAPA1P1 . . . Ral GTPase activating protein catalytic alpha subunit 1 pseudogene 1 . . . . . . . . . . . RALGAPA2 8.48775696516084e-06 0.999991501260514 1.09825211894721e-08 Ral GTPase activating protein catalytic alpha subunit 2 FUNCTION: Catalytic subunit of the heterodimeric RalGAP2 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;whole body;islets of Langerhans;placenta;testis;colon;blood;kidney;skeletal muscle;stomach;retina;bone marrow; dorsal root ganglion;skin; 0.21358 0.10195 -2.30816515 1.203113942 547.52089 4.75813 RALGAPB 0.999999955632558 4.43674418742452e-08 5.3334274089996e-20 Ral GTPase activating protein non-catalytic beta subunit FUNCTION: Non-catalytic subunit of the heterodimeric RalGAP1 and RalGAP2 complexes which act as GTPase activators for the Ras-like small GTPases RALA and RALB. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in brain, mostly in amygdala.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;spleen;cervix;mammary gland;stomach;aorta; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.64391 0.10552 -0.949752638 9.32413305 208.99718 3.12049 RALGDS 0.296706347503849 0.703257908626603 3.57438695481003e-05 ral guanine nucleotide dissociation stimulator FUNCTION: Stimulates the dissociation of GDP from the Ras-related RalA and RalB GTPases which allows GTP binding and activation of the GTPases. Interacts and acts as an effector molecule for R-Ras, H-Ras, K-Ras, and Rap.; . . . . 0.48158 0.16125 -1.344833561 4.641424864 2512.28764 9.33580 RALGPS1 0.999856880539416 0.000143119441811166 1.87727641835729e-11 Ral GEF with PH domain and SH3 binding motif 1 FUNCTION: Guanine nucleotide exchange factor (GEF) for the small GTPase RALA. May be involved in cytoskeletal organization (By similarity). Guanine nucleotide exchange factor for. {ECO:0000250, ECO:0000269|PubMed:10747847, ECO:0000269|PubMed:10889189}.; . TISSUE SPECIFICITY: Widely expressed (at protein level). Isoform 2 is expressed in brain, colon, kidney, pancreas, prostate, skeletal muscle, small intestine, testis, thymus and uterus. Isoform 1 is expressed at high levels in heart and testis and at lower levels in brain, pancreas, skeletal muscle, small intestine and thymus. {ECO:0000269|PubMed:10747847, ECO:0000269|PubMed:10889189}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;spinal cord;blood;lens;pancreas;lung;placenta;macula lutea;head and neck;kidney;mammary gland;stomach; amygdala;whole brain;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;skeletal muscle;subthalamic nucleus;fetal brain;testis - seminiferous tubule;prefrontal cortex;liver;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.76983 0.12378 -0.293801652 32.93819297 294.12779 3.66270 RALGPS2 0.922194824062516 0.0778050133611385 1.62576345066946e-07 Ral GEF with PH domain and SH3 binding motif 2 FUNCTION: Guanine nucleotide exchange factor for the small GTPase RALA. May be involved in cytoskeletal organization. May also be involved in the stimulation of transcription in a Ras-independent fashion (By similarity). {ECO:0000250}.; DISEASE: Note=RALGPS2 is a potential candidate gene for susceptibility to Alzheimer disease linked to 1q24. {ECO:0000269|PubMed:17564960}.; . ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland; superior cervical ganglion; 0.14220 0.09694 -0.26993514 34.59542345 77.93867 1.86189 RALY 0.554573839722822 0.442614262427277 0.00281189784990063 RALY heterogeneous nuclear ribonucleoprotein FUNCTION: Probable-RNA binding protein. Could be a heterogeneous nuclear ribonucleoprotein (hnRNP). May be involved in pre-mRNA splicing (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in heart, brain, lung, liver, skeletal muscle, kidney and pancreas. Weakly expressed in placenta.; medulla oblongata;ovary;salivary gland;colon;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;amniotic fluid;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;epididymis;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; heart;testis - seminiferous tubule;thyroid;testis; 0.18001 0.13451 -0.093566408 46.7386176 666.56385 5.16662 RALY-AS1 . . . RALY antisense RNA 1 . . . . . . . . . . . RALYL 0.0296900360975372 0.924042635451041 0.0462673284514215 RALY RNA binding protein-like . . TISSUE SPECIFICITY: Widely expressed, with highest levels in brain. {ECO:0000269|PubMed:12688537}.; . . 0.21161 0.11262 -0.271755481 34.31823543 33.66101 1.03832 RAMP1 0.0577928242238866 0.712036947245301 0.230170228530812 receptor (G protein-coupled) activity modifying protein 1 FUNCTION: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL. {ECO:0000269|PubMed:9620797}.; . TISSUE SPECIFICITY: Expressed in many tissues including the uterus, bladder, brain, pancreas and gastro-intestinal tract. {ECO:0000269|PubMed:9620797}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;islets of Langerhans;hypothalamus;muscle;colon;skeletal muscle;greater omentum;uterus;prostate;lung;bone;placenta;testis;kidney;brain;pineal gland;stomach; uterus;pons; 0.12203 0.15981 -0.471992905 23.03609342 9.25483 0.33910 RAMP2 0.00389299156111896 0.64277663097747 0.353330377461411 receptor (G protein-coupled) activity modifying protein 2 FUNCTION: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for adrenomedullin (AM) together with CALCRL. {ECO:0000269|PubMed:22102369, ECO:0000269|PubMed:9620797}.; . TISSUE SPECIFICITY: Strongly expressed in lung, breast, immune system and fetal tissues. {ECO:0000269|PubMed:9620797}.; unclassifiable (Anatomical System);cartilage;heart;colon;fovea centralis;choroid;lens;retina;uterus;pancreas;prostate;optic nerve;lung;endometrium;placenta;thyroid;macula lutea;testis;spleen;kidney;brain; adipose tissue;adrenal gland;thyroid;placenta;fetal lung; 0.53313 0.14072 -0.053113545 49.38664779 26.34746 0.85417 RAMP2-AS1 . . . RAMP2 antisense RNA 1 . . . . . . . . . . . RAMP3 0.00952875139018002 0.593231283985663 0.397239964624157 receptor (G protein-coupled) activity modifying protein 3 FUNCTION: Plays a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a GPER1-dependent manner. Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) and GPER1 to the plasma membrane. Acts as a receptor for adrenomedullin (AM) together with CALCRL. {ECO:0000269|PubMed:23674134, ECO:0000269|PubMed:9620797}.; . TISSUE SPECIFICITY: Strongly expressed in lung, breast, immune system and fetal tissues. {ECO:0000269|PubMed:9620797}.; smooth muscle;ovary;colon;parathyroid;choroid;retina;uterus;prostate;endometrium;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;pancreas;lung;placenta;hippocampus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;atrioventricular node;kidney; 0.12881 0.15128 0.659651797 84.35362114 552.76542 4.78211 RAN 0.95593796807508 0.0439488026420061 0.00011322928291402 RAN, member RAS oncogene family FUNCTION: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. {ECO:0000250, ECO:0000269|PubMed:10400640, ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:8692944}.; . TISSUE SPECIFICITY: Expressed in a variety of tissues. {ECO:0000269|PubMed:2108320}.; lymphoreticular;medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;bone;pituitary gland;testis;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;whole brain;thalamus;occipital lobe;hypothalamus;temporal lobe;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; . 0.25991 -0.075159878 47.78839349 34.77273 1.06009 RANBP1 0.336215103625086 0.649124351384162 0.0146605449907526 RAN binding protein 1 FUNCTION: Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.; . . ovary;salivary gland;intestine;colon;vein;skin;retina;uterus;prostate;whole body;cochlea;gum;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;pharynx;blood;breast;bile duct;pancreas;lung;adrenal gland;epididymis;placenta;visual apparatus;liver;cervix;spleen;kidney;aorta;stomach; subthalamic nucleus;globus pallidus;pons;trigeminal ganglion; 0.76363 0.16306 -0.251530012 35.42108988 4.25575 0.15484 RANBP2 0.999999998507193 1.49280670948305e-09 4.67023637848024e-27 RAN binding protein 2 FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Binds single- stranded RNA (in vitro). May bind DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB. {ECO:0000269|PubMed:11792325, ECO:0000269|PubMed:12032081, ECO:0000269|PubMed:15378033, ECO:0000269|PubMed:15931224, ECO:0000269|PubMed:22194619}.; DISEASE: Encephalopathy, acute, infection-induced, 3 (IIAE3) [MIM:608033]: A rapidly progressive encephalopathy manifesting in susceptible individuals with seizures and coma. It can occur within days in otherwise healthy children after common viral infections such as influenza and parainfluenza, without evidence of viral infection of the brain or inflammatory cell infiltration. Brain T2-weighted magnetic resonance imaging reveals characteristic symmetric lesions present in the thalami, pons and brainstem. {ECO:0000269|PubMed:19118815}. Note=The disease is caused by mutations affecting the gene represented in this entry. Mutations in the RANBP2 gene predispose to IIAE3, but by themselves are insufficient to make the phenotype fully penetrant; additional genetic and environmental factors are required (PubMed:19118815). {ECO:0000269|PubMed:19118815}.; . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;small intestine;lacrimal gland;cerebellum cortex;islets of Langerhans;bile duct;pancreas;lung;pia mater;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;thymus; superior cervical ganglion;adrenal cortex;atrioventricular node;trigeminal ganglion;parietal lobe; 0.93164 0.52169 -1.538551197 3.33215381 1024.97017 6.15454 RANBP3 0.999905044102182 9.49558636678633e-05 3.41506182214028e-11 RAN binding protein 3 FUNCTION: Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF- beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export. {ECO:0000269|PubMed:11425870, ECO:0000269|PubMed:11571268, ECO:0000269|PubMed:11932251, ECO:0000269|PubMed:19289081, ECO:0000269|PubMed:9637251}.; . TISSUE SPECIFICITY: Widely expressed with high levels in testis and heart. {ECO:0000269|PubMed:9637251}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;cerebral cortex;larynx;bone;iris;testis;germinal center;dura mater;brain;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;pia mater;placenta;macula lutea;hippocampus;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;stomach;peripheral nerve;cerebellum; subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.65153 0.13971 -0.732911333 14.07761264 207.36577 3.11094 RANBP3L 1.13183444081718e-10 0.299186693383906 0.70081330650291 RAN binding protein 3 like . . . amygdala;prostate;hippocampus;liver;testis;kidney;brain; . 0.14945 . 0.108486928 61.90728946 976.85822 6.03974 RANBP6 0.0417425099168488 0.956992563038172 0.00126492704497931 RAN binding protein 6 FUNCTION: May function in nuclear protein import as nuclear transport receptor.; . . unclassifiable (Anatomical System);lymph node;heart;blood;parathyroid;skin;skeletal muscle;bone marrow;breast;lung;nasopharynx;bone;placenta;germinal center;brain;bladder;stomach; subthalamic nucleus;medulla oblongata;thalamus;occipital lobe;hypothalamus;prefrontal cortex;ciliary ganglion;parietal lobe;cingulate cortex; 0.91864 0.10241 -0.995664936 8.539749941 97.1035 2.13013 RANBP9 0.999958495559594 4.15044358576723e-05 4.54843409081256e-12 RAN binding protein 9 FUNCTION: May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. May be involved in signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation. Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity. Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA (By similarity). {ECO:0000250, ECO:0000269|PubMed:12147692, ECO:0000269|PubMed:12361945, ECO:0000269|PubMed:14500717, ECO:0000269|PubMed:14722085, ECO:0000269|PubMed:15381419, ECO:0000269|PubMed:15558019, ECO:0000269|PubMed:18222118}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in testes, placenta, heart, and muscle, and lowest levels in lung. Within the brain, expressed predominantly by neurons in the gray matter of cortex, the granular layer of cerebellum and the Purkinje cells. {ECO:0000269|PubMed:12147692, ECO:0000269|PubMed:12361945, ECO:0000269|PubMed:15381419}.; myocardium;smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;lung;mesenchyma;epididymis;trabecular meshwork;placenta;visual apparatus;hypopharynx;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;testis - interstitial;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;trigeminal ganglion;parietal lobe; 0.77088 0.20645 -0.756778259 13.44656759 118.2155 2.36558 RANBP10 0.951824229348564 0.0481745902198399 1.18043159588843e-06 RAN binding protein 10 FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase (By similarity). May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen- induced transactivation. In contrast to RANBP9, does not interact with Sos and does not activate the Ras pathway. {ECO:0000250, ECO:0000269|PubMed:18222118}.; . TISSUE SPECIFICITY: Broadly expressed, with highest levels in skeletal muscle. {ECO:0000269|PubMed:14684163}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;bone marrow; 0.58610 0.11289 -0.843147538 11.2762444 72.21908 1.77081 RANBP17 8.61017652515499e-36 7.05975319978102e-07 0.99999929402468 RAN binding protein 17 FUNCTION: May function as a nuclear transport receptor. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in testis, moderately in pancreas and weakly in other tissues studied. {ECO:0000269|PubMed:11071879}.; . . 0.18512 . 0.121225147 62.22576079 494.71509 4.57222 RANBP20P . . . RAN binding protein 20 pseudogene . . . . . . . . . . . RANGAP1 0.132718719795843 0.866349282894871 0.000931997309286542 Ran GTPase activating protein 1 FUNCTION: GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state.; . TISSUE SPECIFICITY: Highly expressed in brain, thymus and testis. {ECO:0000269|PubMed:8973340}.; lymphoreticular;medulla oblongata;ovary;colon;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; amygdala;superior cervical ganglion;testis - interstitial;subthalamic nucleus;temporal lobe;prefrontal cortex;globus pallidus;testis;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe; 0.27430 0.20477 -0.376526807 28.10804435 116.60029 2.34877 RANGRF 0.0207633298112848 0.90562022486601 0.0736164453227054 RAN guanine nucleotide release factor FUNCTION: May regulate the intracellular trafficking of RAN. In cardiac cells seems to regulate the cell surface localization of SCN5A. {ECO:0000269|PubMed:11290418, ECO:0000269|PubMed:18184654}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are ubiquitously expressed. {ECO:0000269|PubMed:11290418}.; lymphoreticular;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;breast;lung;adrenal gland;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;aorta;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11351 0.10667 -0.205617011 38.57631517 14.86914 0.53529 RANP1 . . . RAN, member RAS oncogene family pseudogene 1 . . . . . . . . . . . RANP2 . . . RAN, member RAS oncogene family pseudogene 2 . . . . . . . . . . . RANP3 . . . RAN, member RAS oncogene family pseudogene 3 . . . . . . . . . . . RANP4 . . . RAN, member RAS oncogene family pseudogene 4 . . . . . . . . . . . RANP5 . . . RAN, member RAS oncogene family pseudogene 5 . . . . . . . . . . . RANP6 . . . RAN, member RAS oncogene family pseudogene 6 . . . . . . . . . . . RANP7 . . . RAN, member RAS oncogene family pseudogene 7 . . . . . . . . . . . RANP8 . . . RAN, member RAS oncogene family pseudogene 8 . . . . . . . . . . . RANP9 . . . RAN, member RAS oncogene family pseudogene 9 . . . . . . . . . . . RAP1A 0.934189797815675 0.0655008605875022 0.000309341596823083 RAP1A, member of RAS oncogene family FUNCTION: Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes. Plays a role in nerve growth factor (NGF)-induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions. {ECO:0000269|PubMed:17916086, ECO:0000269|PubMed:21840392}.; . . smooth muscle;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;pancreas;pia mater;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;spinal cord;whole blood; 0.55238 0.28104 -0.075159878 47.78839349 2.39611 0.08204 RAP1AP . . . RAP1A, member of RAS oncogene family pseudogene . . . . . . . . . . . RAP1B 0.936825076137946 0.0628958302506959 0.00027909361135797 RAP1B, member of RAS oncogene family FUNCTION: GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays a role in the establishment of basal endothelial barrier function. {ECO:0000269|PubMed:18660803, ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:21840392}.; . . myocardium;ovary;skin;retina;bone marrow;prostate;cochlea;endometrium;gum;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;blood;lens;breast;macula lutea;visual apparatus;liver;cervix;mammary gland;colon;parathyroid;fovea centralis;vein;uterus;whole body;oesophagus;larynx;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus;cerebellum; . 0.66833 . -0.09720619 46.20193442 1.27901 0.04486 RAP1BP1 . . . RAP1B, member of RAS oncogene family pseudogene 1 . . . . . . . . . . . RAP1BP2 . . . RAP1B, member of RAS oncogene family pseudogene 2 . . . . . . . . . . . RAP1BP3 . . . RAP1B, member of RAS oncogene family pseudogene 3 . . . . . . . . . . . RAP1GAP 0.974156915163255 0.0258430341562822 5.0680462784698e-08 RAP1 GTPase activating protein FUNCTION: GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state. {ECO:0000269|PubMed:15141215}.; . TISSUE SPECIFICITY: Significant expression seen in the brain, kidney and pancreas. Abundant in the cerebral cortex and expressed at much lower levels in the spinal cord. Not detected in the lymphoid tissues. {ECO:0000269|PubMed:9346962}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;hypothalamus;sympathetic chain;skin;prostate;lung;frontal lobe;placenta;thyroid;hippocampus;testis;kidney;brain;stomach;cerebellum; amygdala;whole brain;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;adrenal cortex;caudate nucleus;pons;fetal thyroid;skeletal muscle;subthalamic nucleus;uterus corpus;adrenal gland;thyroid;prefrontal cortex;globus pallidus;kidney;trigeminal ganglion;cingulate cortex;parietal lobe; 0.37356 0.15820 -0.725642751 14.24274593 2918.53299 10.24858 RAP1GAP2 0.95593855271305 0.0440612562897605 1.9099718916618e-07 RAP1 GTPase activating protein 2 FUNCTION: GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state. {ECO:0000269|PubMed:15632203}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in platelets with isoform 2 being the predominant form. Expressed in lymphocytes, heart, testis and pancreas. {ECO:0000269|PubMed:15632203}.; unclassifiable (Anatomical System);cartilage;heart;tongue;sympathetic chain;colon;blood;skeletal muscle;bone marrow;uterus;pancreas;prostate;lung;bone;placenta;testis;head and neck;germinal center;kidney;brain;mammary gland; amygdala;whole brain;occipital lobe;temporal lobe;prefrontal cortex;cingulate cortex;cerebellum; 0.47188 0.10037 -1.129772626 6.505071951 3045.8448 10.48783 RAP1GDS1 0.824878144875972 0.175115052309811 6.80281421713226e-06 Rap1 GTPase-GDP dissociation stimulator 1 FUNCTION: Stimulates GDP/GTP exchange reaction of a group of small GTP-binding proteins (G proteins) including Rap1a/Rap1b, RhoA, RhoB and KRas, by stimulating the dissociation of GDP from and the subsequent binding of GTP to each small G protein.; . . ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;kidney;stomach; amygdala;dorsal root ganglion;medulla oblongata;testis - interstitial;occipital lobe;thalamus;hypothalamus;spinal cord;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.23278 0.11027 -0.025608647 51.91672564 40.57822 1.18926 RAP2A 0.71733965665019 0.268600965216812 0.014059378132998 RAP2A, member of RAS oncogene family FUNCTION: Small GTP-binding protein which cycles between a GDP- bound inactive and a GTP-bound active form. In its active form interacts with and regulates several effectors including MAP4K4, MINK1 and TNIK. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it is part of several signaling cascades and may regulate cytoskeletal rearrangements, cell migration, cell adhesion and cell spreading. {ECO:0000269|PubMed:14966141, ECO:0000269|PubMed:15342639, ECO:0000269|PubMed:16246175, ECO:0000269|PubMed:16540189, ECO:0000269|PubMed:18930710, ECO:0000269|PubMed:20159449}.; . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;aorta;stomach; amygdala;whole brain;occipital lobe;superior cervical ganglion;medulla oblongata;temporal lobe;atrioventricular node;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.15000 0.18963 0.013025609 54.62962963 2.30275 0.07820 RAP2B 0.275476507802157 0.633596656159974 0.0909268360378691 RAP2B, member of RAS oncogene family FUNCTION: Small GTP-binding protein which cycles between a GDP- bound inactive and a GTP-bound active form. Involved in EGFR and CHRM3 signaling pathways through stimulation of PLCE1. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May regulate membrane vesiculation in red blood cells. {ECO:0000269|PubMed:11877431, ECO:0000269|PubMed:15143162, ECO:0000269|PubMed:16540189}.; . TISSUE SPECIFICITY: Expressed in red blood cells (at protein level). {ECO:0000269|PubMed:16540189}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;bone;testis;amniotic fluid;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;stomach;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node;whole blood;bone marrow; 0.36167 0.15588 -0.031067188 51.03798066 4.83001 0.17768 RAP2C 0.212765647011738 0.648042037841048 0.139192315147214 RAP2C, member of RAS oncogene family FUNCTION: Small GTP-binding protein which cycles between a GDP- bound inactive and a GTP-bound active form. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May play a role in SRE-mediated gene transcription. {ECO:0000269|PubMed:17447155}.; . TISSUE SPECIFICITY: Expressed in liver, skeletal muscle, prostate, uterus, rectum, stomach, and bladder and to a lower extent in brain, kidney, pancreas, and bone marrow. Expressed in mononuclear leukocytes and megakaryocytes. {ECO:0000269|PubMed:16213650, ECO:0000269|PubMed:17447155}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;gum;testis;germinal center;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;hypothalamus;blood;pancreas;lung;adrenal gland;epididymis;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; uterus;fetal liver;superior cervical ganglion;trigeminal ganglion; 0.61236 0.13588 -0.009020804 52.8544468 1.19806 0.03500 RAP2C-AS1 . . . RAP2C antisense RNA 1 . . . . . . . . . . . RAP2CP1 . . . RAP2C pseudogene 1 . . . . . . . . . . . RAPGEF1 0.999914749689066 8.5250310716412e-05 2.17573889204483e-13 Rap guanine nucleotide exchange factor 1 FUNCTION: Guanine nucleotide-releasing protein that binds to SH3 domain of CRK and GRB2/ASH. Transduces signals from CRK to activate RAS. Plays a role in the establishment of basal endothelial barrier function. Plays a role in nerve growth factor (NGF)-induced sustained activation of Rap1 and neurite outgrowth. {ECO:0000269|PubMed:17724123, ECO:0000269|PubMed:21840392, ECO:0000269|PubMed:7806500}.; . TISSUE SPECIFICITY: Ubiquitously expressed in adult and fetus. Expression is high in adult skeletal muscle and placenta and in fetal brain and heart. Low levels of expression in adult and fetal liver.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;cerebellum; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17146 0.19882 -1.767443354 2.317763623 77.63729 1.85508 RAPGEF2 0.999996666741051 3.33325894869825e-06 1.6384060605414e-17 Rap guanine nucleotide exchange factor 2 FUNCTION: Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Acts also as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP (PubMed:23800469, PubMed:10801446) or not (PubMed:10608844, PubMed:10548487, PubMed:11359771). Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP- induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Provides also inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain- derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions. {ECO:0000269|PubMed:10548487, ECO:0000269|PubMed:10608844, ECO:0000269|PubMed:10608883, ECO:0000269|PubMed:10801446, ECO:0000269|PubMed:10934204, ECO:0000269|PubMed:11359771, ECO:0000269|PubMed:12391161, ECO:0000269|PubMed:16272156, ECO:0000269|PubMed:17724123, ECO:0000269|PubMed:21840392, ECO:0000269|PubMed:23800469}.; . TISSUE SPECIFICITY: Expressed in primary neuronal and endocrine cells (at protein level). Highest expression levels in brain. Lower expression levels in heart, kidney, lung, placenta and blood leukocytes. {ECO:0000269|PubMed:10934204, ECO:0000269|PubMed:11168587, ECO:0000269|PubMed:23800469}.; lymphoreticular;ovary;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;spinal cord;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;liver;alveolus;spleen;kidney;mammary gland;stomach; amygdala;whole brain;subthalamic nucleus;superior cervical ganglion;medulla oblongata;occipital lobe;prefrontal cortex;pons;trigeminal ganglion;parietal lobe;skeletal muscle;cingulate cortex; 0.57738 0.13300 -1.658985203 2.724699222 98.637 2.14720 RAPGEF3 2.0974108088557e-15 0.784649455559428 0.215350544440569 Rap guanine nucleotide exchange factor 3 FUNCTION: Guanine nucleotide exchange factor (GEF) for RAP1A and RAP2A small GTPases that is activated by binding cAMP. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which it activates the PI3K gamma complex and which is involved in angiogenesis. Plays a role in the modulation of the cAMP-induced dynamic control of endothelial barrier function through a pathway that is independent on Rho- mediated signaling. Required for the actin rearrangement at cell- cell junctions, such as stress fibers and junctional actin. {ECO:0000269|PubMed:10777494, ECO:0000269|PubMed:21840392, ECO:0000269|PubMed:9853756}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in adult kidney, heart, thyroid and brain, and fetal kidney. {ECO:0000269|PubMed:9856955}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;colon;uterus;optic nerve;lung;cerebral cortex;endometrium;bone;thyroid;placenta;pituitary gland;testis;spleen;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;thyroid;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10753 0.21068 -0.275617382 33.58693088 3668.6445 11.77047 RAPGEF4 0.957225849602447 0.0427741503853806 1.21723159428543e-11 Rap guanine nucleotide exchange factor 4 FUNCTION: Guanine nucleotide exchange factor (GEF) for RAP1A, RAP1B and RAP2A small GTPases that is activated by binding cAMP. Seems not to activate RAB3A. Involved in cAMP-dependent, PKA- independent exocytosis through interaction with RIMS2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:10777494, ECO:0000269|PubMed:9856955}.; . TISSUE SPECIFICITY: Predominantly expressed in brain and adrenal gland. Isoform 2 is expressed in liver. Isoform 1 is expressed in liver at very low levels.; unclassifiable (Anatomical System);amygdala;lymph node;cartilage;colon;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;frontal lobe;macula lutea;hippocampus;pituitary gland;brain;tonsil;stomach; amygdala;occipital lobe;subthalamic nucleus;superior cervical ganglion;temporal lobe;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex; 0.14543 0.12306 -0.771553417 13.15168672 157.86292 2.74458 RAPGEF4-AS1 . . . RAPGEF4 antisense RNA 1 . . . . . . . . . . . RAPGEF5 0.997815952976676 0.00218404643455787 5.88765700109186e-10 Rap guanine nucleotide exchange factor 5 FUNCTION: Guanine nucleotide exchange factor (GEF) for RAP1A, RAP2A and MRAS/M-Ras-GTP. Its association with MRAS inhibits Rap1 activation. {ECO:0000269|PubMed:10777494, ECO:0000269|PubMed:10934204}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in brain.; unclassifiable (Anatomical System);ovary;heart;colon;parathyroid;skin;uterus;whole body;lung;frontal lobe;cochlea;adrenal gland;gum;placenta;hypopharynx;liver;testis;head and neck;spleen;germinal center;kidney;brain; amygdala;whole brain;dorsal root ganglion;thalamus;superior cervical ganglion;occipital lobe;medulla oblongata;hypothalamus;spinal cord;pons;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.11243 0.08091 -0.977252525 8.799245105 330.13033 3.86176 RAPGEF6 0.998026273148455 0.00197372685138884 1.56010025272144e-13 Rap guanine nucleotide exchange factor 6 FUNCTION: Guanine nucleotide exchange factor (GEF) for Rap1A, Rap2A and M-Ras GTPases. Does not interact with cAMP. {ECO:0000269|PubMed:11524421, ECO:0000269|PubMed:12581858}.; . TISSUE SPECIFICITY: Isoform 3 has highest expression levels in the brain, heart, liver, lung and placenta and is barely detectable in skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:11524421}.; unclassifiable (Anatomical System);lymphoreticular;smooth muscle;cartilage;heart;islets of Langerhans;hypothalamus;colon;blood;skin;retina;bone marrow;breast;uterus;prostate;lung;nasopharynx;placenta;liver;testis;spleen;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cingulate cortex; 0.69007 0.09893 -1.673819661 2.695211135 0.86508 0.01735 RAPGEFL1 0.874145903651903 0.125840264761311 1.38315867855447e-05 Rap guanine nucleotide exchange factor like 1 FUNCTION: Probable guanine nucleotide exchange factor (GEF).; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);amygdala;heart;lens;skeletal muscle;lung;macula lutea;visual apparatus;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; whole brain;amygdala;superior cervical ganglion;occipital lobe;tongue;temporal lobe;pons;atrioventricular node;skeletal muscle;skin;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.42544 . -0.758599262 13.32861524 28.15111 0.90201 RAPH1 0.957851233210029 0.0421487322017924 3.45881787672742e-08 Ras association (RalGDS/AF-6) and pleckstrin homology domains 1 FUNCTION: Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion.; . TISSUE SPECIFICITY: Isoform RMO1-RAPH1 is ubiquitously expressed with highest levels in brain, heart, ovary and developing embryo. Isoform RMO1 is widely expressed with highest levels in liver. Low expression in B-cells. {ECO:0000269|PubMed:15469845, ECO:0000269|PubMed:15609301}.; smooth muscle;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;lens;skeletal muscle;bile duct;breast;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;peripheral nerve; superior cervical ganglion;testis - interstitial;pons;atrioventricular node; 0.25984 0.27016 -2.607452819 0.807973579 124.99766 2.43194 RAPSN 0.0326445463388561 0.926696833446204 0.0406586202149398 receptor associated protein of the synapse FUNCTION: Postsynaptic protein required for clustering of nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction. It may link the receptor to the underlying postsynaptic cytoskeleton, possibly by direct association with actin or spectrin.; DISEASE: Myasthenic syndrome, congenital, 11, associated with acetylcholine receptor deficiency (CMS11) [MIM:616326]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS11 is an autosomal recessive disorder of postsynaptic neuromuscular transmission, due to deficiency of AChR at the endplate that results in low amplitude of the miniature endplate potential and current. {ECO:0000269|PubMed:11791205, ECO:0000269|PubMed:12730725, ECO:0000269|PubMed:12796535, ECO:0000269|PubMed:12929188, ECO:0000269|PubMed:14504330, ECO:0000269|PubMed:15036330, ECO:0000269|PubMed:15328566, ECO:0000269|PubMed:16931511, ECO:0000269|PubMed:17594401}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Fetal akinesia deformation sequence (FADS) [MIM:208150]: A clinically and genetically heterogeneous group of disorders with congenital malformations related to impaired fetal movement. Clinical features include fetal akinesia, intrauterine growth retardation, polyhydramnios, arthrogryposis, pulmonary hypoplasia, craniofacial abnormalities, and cryptorchidism. {ECO:0000269|PubMed:18179903, ECO:0000269|PubMed:18252226}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);optic nerve;lung;whole body;bone;macula lutea;muscle;testis;fovea centralis;choroid;lens;skeletal muscle;retina; uterus corpus;ciliary ganglion;trigeminal ganglion;skeletal muscle;skin; 0.57380 . 0.220536484 68.38287332 876.73715 5.76157 RARA 0.934197317282478 0.0657395328752509 6.31498422709868e-05 retinoic acid receptor alpha FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis. Has a role in the survival of early spermatocytes at the beginning prophase of meiosis. In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (By similarity). Regulates expression of target genes in a ligand- dependent manner by recruiting chromatin complexes containing KMT2E/MLL5. Mediates retinoic acid-induced granulopoiesis. {ECO:0000250, ECO:0000269|PubMed:16417524, ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:19850744, ECO:0000269|PubMed:20215566}.; DISEASE: Note=Chromosomal aberrations involving RARA are commonly found in acute promyelocytic leukemia. Translocation t(11;17)(q32;q21) with ZBTB16/PLZF; translocation t(15;17)(q21;q21) with PML; translocation t(5;17)(q32;q11) with NPM. The PML-RARA oncoprotein requires both the PML ring structure and coiled-coil domain for both interaction with UBE2I, nuclear microspeckle location and sumoylation. In addition, the coiled- coil domain functions in blocking RA-mediated transactivation and cell differentiation. {ECO:0000269|PubMed:12691149, ECO:0000269|PubMed:8302850, ECO:0000269|PubMed:8562957}.; . medulla oblongata;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;testis;pons;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle; 0.97252 0.88590 -0.47017169 23.25430526 30.08447 0.95978 RARA-AS1 . . . RARA antisense RNA 1 . . . . . . . . . . . RARB 0.999317519370488 0.000682476458773119 4.17073887494665e-09 retinoic acid receptor beta FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence or presence of hormone ligand, acts mainly as an activator of gene expression due to weak binding to corepressors. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function. {ECO:0000269|PubMed:12554770}.; DISEASE: Microphthalmia, syndromic, 12 (MCOPS12) [MIM:615524]: A form of microphthalmia, a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. MCOPS12 patients manifest variable features, including diaphragmatic hernia, pulmonary hypoplasia, and cardiac abnormalities. {ECO:0000269|PubMed:24075189}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lens;breast;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.56320 0.28442 -0.494039303 22.09247464 18.39283 0.63721 RARG 0.970063074313349 0.0299281264956047 8.79919104589393e-06 retinoic acid receptor gamma FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, acts mainly as an activator of gene expression due to weak binding to corepressors. Required for limb bud development. In concert with RARA or RARB, required for skeletal growth, matrix homeostasis and growth plate function (By similarity). {ECO:0000250}.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;bone;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;head and neck;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;tongue;kidney;trigeminal ganglion;skeletal muscle; 0.54662 0.22085 -0.271755481 34.31823543 676.40224 5.19517 RARRES1 8.40651968753382e-07 0.167662377408507 0.832336781939524 retinoic acid receptor responder (tazarotene induced) 1 FUNCTION: Inhibitor of the cytoplasmic carboxypeptidase AGBL2, may regulate the alpha-tubulin tyrosination cycle. {ECO:0000269|PubMed:21303978}.; . . ovary;parathyroid;choroid;skin;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;larynx;bone;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;urinary;breast;pancreas;lung;trabecular meshwork;placenta;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;prostate;trachea;ovary;salivary gland;fetal lung;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.09751 0.08176 . . 1105.62229 6.35418 RARRES2 0.00295445312501597 0.583036393789479 0.414009153085505 retinoic acid receptor responder (tazarotene induced) 2 FUNCTION: Adipocyte-secreted protein (adipokine) that regulates adipogenesis, metabolism and inflammation through activation of the chemokine-like receptor 1 (CMKLR1). Its other ligands include G protein-coupled receptor 1 (GPR1) and chemokine receptor-like 2 (CCRL2). Positively regulates adipocyte differentiation, modulates the expression of adipocyte genes involved in lipid and glucose metabolism and might play a role in angiogenesis, a process essential for the expansion of white adipose tissue. Also acts as a proinflammatory adipokine, causing an increase in secretion of proinflammatory and prodiabetic adipokines, which further impair adipose tissue metabolic function and have negative systemic effects including impaired insulin sensitivity, altered glucose and lipid metabolism, and a decrease in vascular function in other tissues. Can have both pro- and anti-inflammatory properties depending on the modality of enzymatic cleavage by different classes of proteases. Acts as a chemotactic factor for leukocyte populations expressing CMKLR1, particularly immature plasmacytoid dendritic cells, but also immature myeloid DCs, macrophages and natural killer cells. Exerts an anti-inflammatory role by preventing TNF/TNFA-induced VCAM1 expression and monocytes adhesion in vascular endothelial cells. The effect is mediated via inhibiting activation of NF-kappa-B and CRK/p38 through stimulation of AKT1/NOS3 signaling and nitric oxide production. Its dual role in inflammation and metabolism might provide a link between chronic inflammation and obesity, as well as obesity- related disorders such as type 2 diabetes and cardiovascular disease. Exhibits an antimicrobial function in the skin. {ECO:0000269|PubMed:14675762, ECO:0000269|PubMed:17635925, ECO:0000269|PubMed:17767914, ECO:0000269|PubMed:18242188, ECO:0000269|PubMed:20237162, ECO:0000269|PubMed:22634313, ECO:0000269|PubMed:23527010}.; . TISSUE SPECIFICITY: Expressed at the highest levels in placenta, liver, and white adipose tissue (WAT), and to a lesser extent in many other tissues such as lung, brown adipose tissue, heart, ovary, kidney, skeletal muscle and pancreas. Within WAT, expression is enriched in adipocytes as compared to the stromal vascular fraction. Expression and secretion increases dramatically with adipogenesis. Highly expressed in skin (basal and suprabasal layers of the epidermis, hair follicles and endothelial cells). Expression is elevated in numerous metabolic and inflammatory diseases including psoriasis, obesity, type 2 diabetes, metabolic syndrome and cardiovascular disease. {ECO:0000269|PubMed:17635925, ECO:0000269|PubMed:17767914, ECO:0000269|PubMed:23527010}.; ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;testis;brain;unclassifiable (Anatomical System);trophoblast;heart;cartilage;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;pancreas;lung;cornea;epididymis;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland; adrenal gland;adrenal cortex;liver;appendix; 0.30470 0.11929 -0.007201372 53.19061099 42.34707 1.23210 RARRES2P1 . . . retinoic acid receptor responder (tazarotene induced) 2 pseudogene 1 . . . . . . . . . . . RARRES2P2 . . . retinoic acid receptor responder (tazarotene induced) 2 pseudogene 2 . . . . . . . . . . . RARRES2P3 . . . retinoic acid receptor responder (tazarotene induced) 2 pseudogene 3 . . . . . . . . . . . RARRES2P4 . . . retinoic acid receptor responder (tazarotene induced) 2 pseudogene 4 . . . . . . . . . . . RARRES2P5 . . . retinoic acid receptor responder (tazarotene induced) 2 pseudogene 5 . . . . . . . . . . . RARRES2P6 . . . retinoic acid receptor responder (tazarotene induced) 2 pseudogene 6 . . . . . . . . . . . RARRES2P7 . . . retinoic acid receptor responder (tazarotene induced) 2 pseudogene 7 . . . . . . . . . . . RARRES2P8 . . . retinoic acid receptor responder (tazarotene induced) 2 pseudogene 8 . . . . . . . . . . . RARRES2P9 . . . retinoic acid receptor responder (tazarotene induced) 2 pseudogene 9 . . . . . . . . . . . RARRES2P10 . . . retinoic acid receptor responder (tazarotene induced) 2 pseudogene 10 . . . . . . . . . . . RARRES2P11 . . . retinoic acid receptor responder (tazarotene induced) 2 pseudogene 11 . . . . . . . . . . . RARRES3 0.000504117067056656 0.446256503536614 0.55323937939633 retinoic acid receptor responder (tazarotene induced) 3 FUNCTION: Exhibits PLA1/2 activity, catalyzing the calcium- independent hydrolysis of acyl groups in various phosphotidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. N- and O-acylation activity is hardly detectable. {ECO:0000269|PubMed:19615464}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10687848, ECO:0000269|PubMed:19615464}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;iris;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;pharynx;blood;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; . 0.00106 . -0.405853867 26.23260203 6.92072 0.25799 RARS 0.000533649935549474 0.998237342828153 0.00122900723629715 arginyl-tRNA synthetase FUNCTION: Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1. {ECO:0000269|PubMed:17443684}.; DISEASE: Leukodystrophy, hypomyelinating, 9 (HLD9) [MIM:616140]: An autosomal recessive neurodegenerative disorder characterized by delayed psychomotor development, severe spasticity, nystagmus, and ataxia associated with diffuse hypomyelination apparent on brain MRI. {ECO:0000269|PubMed:24777941}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; . 0.52278 0.41207 -0.422438699 25.64284029 168.3653 2.83236 RARS2 3.49435482374605e-06 0.997187850171314 0.00280865547386206 arginyl-tRNA synthetase 2, mitochondrial . DISEASE: Pontocerebellar hypoplasia 6 (PCH6) [MIM:611523]: A disorder characterized by an abnormally small cerebellum and brainstem, infantile encephalopathy, generalized hypotonia, lethargy and poor feeding. Recurrent apnea, intractable seizures occur early in the course of this condition. {ECO:0000269|PubMed:17847012}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.50388 0.12295 -0.134019284 43.90776126 1187.41612 6.53435 RARSP1 . . . arginyl-tRNA synthetase pseudogene 1 . . . . . . . . . . . RASA1 0.999998285566451 1.71443354917204e-06 7.92311990278951e-17 RAS p21 protein activator 1 FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. Stimulates the GTPase of normal but not oncogenic Ras p21; this stimulation may be further increased in the presence of NCK1. {ECO:0000269|PubMed:11389730, ECO:0000269|PubMed:8360177}.; DISEASE: Note=Mutations in the SH2 domain of RASA seem to be oncogenic and cause basal cell carcinomas.; DISEASE: Capillary malformation-arteriovenous malformation (CMAVM) [MIM:608354]: A disorder characterized by atypical capillary malformations that are multiple, small, round to oval in shape and pinkish red in color. These capillary malformations are associated with either arteriovenous malformation, arteriovenous fistula, or Parkes Weber syndrome. {ECO:0000269|PubMed:14639529, ECO:0000269|PubMed:24038909}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Parkes Weber syndrome (PKWS) [MIM:608355]: Disorder characterized by a cutaneous flush with underlying multiple micro- arteriovenous fistulas, in association with soft tissue and skeletal hypertrophy of the affected limb. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In placental villi, detected only in the trophoblast layer (cytotrophoblast and syncytiotrophoblast). Not detected in stromal, endothelial or Hofbauer cells (at protein level). {ECO:0000269|PubMed:8360177}.; lymphoreticular;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;blood;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve; dorsal root ganglion;amygdala;occipital lobe;testis - interstitial;superior cervical ganglion;medulla oblongata;temporal lobe;pons;atrioventricular node;subthalamic nucleus;testis - seminiferous tubule;fetal brain;placenta;prefrontal cortex;testis;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.71615 0.13530 -0.821100135 11.88369899 144.431 2.61738 RASA2 5.3166662616203e-17 0.157432660070488 0.842567339929512 RAS p21 protein activator 2 FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4).; . . unclassifiable (Anatomical System);lymphoreticular;heart;cartilage;lacrimal gland;epidermis;islets of Langerhans;skin;skeletal muscle;uterus;breast;whole body;lung;endometrium;adrenal gland;liver;germinal center; . 0.27536 0.11453 -0.688817379 15.20405756 370.15424 4.06246 RASA2-IT1 . . . RASA2 intronic transcript 1 . . . . . . . . . . . RASA3 0.000433958644882729 0.999498117645572 6.79237095450996e-05 RAS p21 protein activator 3 FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4) with high affinity. Might be a specific IP4 receptor.; . . ovary;umbilical cord;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; medulla oblongata;superior cervical ganglion;globus pallidus;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.20897 0.10415 -1.657176494 2.736494456 205.03169 3.09370 RASA3-IT1 . . . RASA3 intronic transcript 1 . . . . . . . . . . . RASA4 0.661336761566351 0.315313914011893 0.0233493244217555 RAS p21 protein activator 4 FUNCTION: Ca(2+)-dependent Ras GTPase-activating protein, that switches off the Ras-MAPK pathway following a stimulus that elevates intracellular calcium. Functions as an adaptor for Cdc42 and Rac1 during FcR-mediated phagocytosis. {ECO:0000269|PubMed:11448776}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11448776}.; ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;peripheral nerve; . . . . . 11.40367 0.41148 RASA4B 0.57564632650937 0.379578765655781 0.0447749078348483 RAS p21 protein activator 4B FUNCTION: Ca(2+)-dependent Ras GTPase-activating protein, that may play a role in the Ras-MAPK pathway. {ECO:0000250|UniProtKB:O43374}.; . . ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;lens;skeletal muscle;breast;lung;epididymis;adrenal gland;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland; . . . . . 3312.1037 10.99594 RASA4CP . . . RAS p21 protein activator 4C, pseudogene . . . . . . . . . . . RASA4DP . . . RAS p21 protein activator 4CD, pseudogene . . . . . . . . . . . RASAL1 4.85979006124582e-08 0.989420225948445 0.0105797254536538 RAS protein activator like 1 FUNCTION: Probable inhibitory regulator of the Ras-cyclic AMP pathway (PubMed:9751798). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000269|PubMed:23999003, ECO:0000269|PubMed:9751798}.; . TISSUE SPECIFICITY: Highly expressed in thyroid and adrenal medulla, lower expression in brain, spinal cord and trachea (PubMed:9751798). Expressed in melanocytes (PubMed:23999003). {ECO:0000269|PubMed:23999003, ECO:0000269|PubMed:9751798}.; unclassifiable (Anatomical System);lymph node;ovary;lacrimal gland;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;adrenal gland;placenta;macula lutea;hypopharynx;testis;head and neck;germinal center;brain;stomach; amygdala;medulla oblongata;globus pallidus;skeletal muscle;parietal lobe; 0.12465 0.09534 0.472145421 78.85114414 490.44457 4.55761 RASAL2 0.226449659060918 0.773549790440042 5.50499040056328e-07 RAS protein activator like 2 FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway.; . . . . 0.77034 0.10960 -2.103686554 1.533380514 121.37364 2.39979 RASAL2-AS1 . . . RASAL2 antisense RNA 1 . . . . . . . . . . . RASAL3 8.34612284891441e-07 0.979011935722998 0.020987229664717 RAS protein activator like 3 FUNCTION: Functions as a Ras GTPase-activating protein. Plays an important role in the expansion and functions of natural killer T (NKT) cells in the liver by negatively regulating RAS activity and the down-stream ERK signaling pathway. {ECO:0000250|UniProtKB:Q8C2K5}.; . TISSUE SPECIFICITY: Predominantly expressed in cells of hematopoietic lineages. {ECO:0000269|PubMed:25652366}.; myocardium;ovary;salivary gland;colon;skin;bone marrow;uterus;prostate;endometrium;testis;germinal center;bladder;brain;tonsil;unclassifiable (Anatomical System);heart;urinary;pharynx;blood;breast;lung;placenta;visual apparatus;liver;kidney; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . -0.462894052 23.62585515 793.6358 5.55486 RASD1 0.0607160204631021 0.71940879766628 0.219875181870618 RAS, dexamethasone-induced 1 FUNCTION: Small GTPase. Negatively regulates the transcription regulation activity of the APBB1/FE65-APP complex via its interaction with APBB1/FE65 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in a variety of tissues including heart, cardiovascular tissues, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, gastrointestinal and reproductive tissues. {ECO:0000269|PubMed:10673050, ECO:0000269|PubMed:12818426}.; medulla oblongata;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;lens;pancreas;lung;macula lutea;hippocampus;kidney;mammary gland;stomach; . 0.19359 0.96027 -0.317668748 31.45789101 39.44379 1.16509 RASD2 0.716620456976745 0.26922064738411 0.0141588956391456 RASD family member 2 FUNCTION: GTPase signaling protein that binds to and hydrolyzes GTP. Regulates signaling pathways involving G-proteins-coupled receptor and heterotrimeric proteins such as GNB1, GNB2 and GNB3. May be involved in selected striatal competencies, mainly locomotor activity and motor coordination. {ECO:0000269|PubMed:11976265, ECO:0000269|PubMed:19255495}.; . TISSUE SPECIFICITY: Pancreatic endocrine cells (islets of Langerhans). {ECO:0000269|PubMed:11976265}.; unclassifiable (Anatomical System);cartilage;ovary;adrenal cortex;colon;parathyroid;skin;retina;breast;prostate;lung;endometrium;placenta;hippocampus;hypopharynx;head and neck;brain;stomach; . 0.28400 0.15339 -0.139478553 43.29440906 59.03847 1.55842 RASEF 3.27123151464191e-05 0.999404852749947 0.000562434934906286 RAS and EF-hand domain containing FUNCTION: Binds predominantly GDP, and also GTP. {ECO:0000269|PubMed:17448446}.; . TISSUE SPECIFICITY: Down-regulated in cutaneous melanoma cells but not in breast cancer cells. {ECO:0000269|PubMed:16174859}.; lung;islets of Langerhans;muscle;mammary gland; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;atrioventricular node;kidney; 0.09812 . 0.42259095 77.22929936 665.99098 5.16516 RASGEF1A 0.910096302244158 0.0898752805837558 2.8417172086285e-05 RasGEF domain family member 1A FUNCTION: Guanine nucleotide exchange factor (GEF) with specificity for RAP2A, KRAS, HRAS, and NRAS (in vitro). Plays a role in cell migration. {ECO:0000269|PubMed:17121879, ECO:0000269|PubMed:19645719}.; . TISSUE SPECIFICITY: Detected in brain and spinal cord. Highly expressed in a number of intrahepatic cholangiocarcinoma tissue biopsies. {ECO:0000269|PubMed:17121879}.; . . 0.28193 0.10809 0.084621747 60.31493277 52.5675 1.43524 RASGEF1B 0.48852966231346 0.511430598577081 3.97391094591406e-05 RasGEF domain family member 1B FUNCTION: Guanine nucleotide exchange factor (GEF) with specificity for RAP2A, it doesn't seems to activate other Ras family proteins (in vitro). {ECO:0000269|PubMed:19645719, ECO:0000269|PubMed:23894443}.; . . unclassifiable (Anatomical System);heart;cartilage;colon;skin;retina;uterus;lung;oesophagus;adrenal gland;visual apparatus;liver;testis;germinal center;spinal ganglion;mammary gland;brain; superior cervical ganglion; 0.62004 0.10842 -0.514264485 21.41424864 73.40783 1.79055 RASGEF1C 0.00331810036135796 0.986235576053216 0.0104463235854256 RasGEF domain family member 1C FUNCTION: Guanine nucleotide exchange factor (GEF). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;visual apparatus;testis;spinal ganglion;brain;mammary gland; dorsal root ganglion;subthalamic nucleus;ciliary ganglion;trigeminal ganglion; 0.11301 0.10716 -0.890882376 10.30313753 662.31636 5.15641 RASGRF1 0.999614037089254 0.000385962910393003 3.52788450764291e-13 Ras protein specific guanine nucleotide releasing factor 1 FUNCTION: Promotes the exchange of Ras-bound GDP by GTP. {ECO:0000269|PubMed:11389730}.; . . . . 0.23126 0.16717 -1.410987626 4.140127389 88.98612 2.02551 RASGRF2 0.998743353862856 0.00125664613709219 5.1892166340433e-14 Ras protein specific guanine nucleotide releasing factor 2 FUNCTION: Functions as a calcium-regulated nucleotide exchange factor activating both Ras and RAC1 through the exchange of bound GDP for GTP. Preferentially activates HRAS in vivo compared to RRAS based on their different types of prenylation. Functions in synaptic plasticity by contributing to the induction of long term potentiation. {ECO:0000269|PubMed:15128856}.; . TISSUE SPECIFICITY: Widely expressed with higher expression in brain, followed by heart, lung, pancreas and kidney. Detected in placenta. Expressed in brain and lung (at protein level). {ECO:0000269|PubMed:10373510, ECO:0000269|PubMed:11856323}.; unclassifiable (Anatomical System);spinal cord;colon;fovea centralis;choroid;lens;retina;uterus;prostate;optic nerve;frontal lobe;macula lutea;liver;spleen;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19695 . -1.256630467 5.343241331 592.56723 4.93365 RASGRF2-AS1 . . . RASGRF2 antisense RNA 1 . . . . . . . . . . . RASGRP1 0.189676970174086 0.810303613090179 1.94167357358935e-05 RAS guanyl releasing protein 1 FUNCTION: Functions as a calcium- and diacylglycerol (DAG)- regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP (PubMed:15899849, PubMed:23908768). Activates the Erk/MAP kinase cascade (PubMed:15899849). Regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B- lymphocyte antigen receptors to Ras (PubMed:10807788, PubMed:12839994). Regulates NK cell cytotoxicity and ITAM- dependent cytokine production by activation of Ras-mediated ERK and JNK pathways (PubMed:19933860). Functions in mast cell degranulation and cytokine secretion, regulating FcERI-evoked allergic responses (By similarity). May also function in differentiation of other cell types (PubMed:12845332). {ECO:0000250|UniProtKB:Q9Z1S3, ECO:0000269|PubMed:10807788, ECO:0000269|PubMed:12782630, ECO:0000269|PubMed:12839994, ECO:0000269|PubMed:12845332, ECO:0000269|PubMed:15060167, ECO:0000269|PubMed:15184873, ECO:0000269|PubMed:15899849, ECO:0000269|PubMed:19933860, ECO:0000269|PubMed:23908768}.; DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:17878389}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Aberrantly spliced isoforms and/or diminished levels of RASGRP1 are found in a cohort of SLE patients raising the possibility that dysregulation of this signaling protein contributes to the development of autoimmunity in a subset of SLE patients.; TISSUE SPECIFICITY: Expressed in brain with higher expression in cerebellum, cerebral cortex and amygdala. Expressed in the hematopoietic system. Expressed in T-cells (at protein level). Expressed in NK cells (at protein level) (PubMed:19933860). {ECO:0000269|PubMed:10807788, ECO:0000269|PubMed:17878389, ECO:0000269|PubMed:19933860, ECO:0000269|PubMed:9789079}.; unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;parathyroid;fovea centralis;skeletal muscle;retina;uterus;pancreas;lung;endometrium;adrenal gland;placenta;macula lutea;testis;germinal center;kidney;brain;stomach;thymus; . 0.36307 0.16981 -0.822919685 11.76574664 1592.55154 7.38291 RASGRP2 0.995280465479902 0.00471944023469103 9.428540651576e-08 RAS guanyl releasing protein 2 FUNCTION: Functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. May also activates other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. Functions in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation. May function in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. {ECO:0000269|PubMed:10918068, ECO:0000269|PubMed:14702343, ECO:0000269|PubMed:17576779, ECO:0000269|PubMed:17702895, ECO:0000269|PubMed:24958846}.; DISEASE: Bleeding disorder, platelet-type 18 (BDPLT18) [MIM:615888]: A disorder characterized by increased bleeding tendency due to platelet dysfunction. Clinical features include epistaxis, hematomas, bleeding after tooth extraction, and menorrhagia. {ECO:0000269|PubMed:24958846}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in platelets, neutrophils and T lymphocytes (at protein level). Expressed in brain where it is enriched in the striatum. Also expressed in the hematopoietic system. Detected in heart, brain, lung, placenta, liver, skeletal muscle and kidney. {ECO:0000269|PubMed:10918068, ECO:0000269|PubMed:17576779, ECO:0000269|PubMed:17702895, ECO:0000269|PubMed:9341881, ECO:0000269|PubMed:9789079}.; unclassifiable (Anatomical System);lymph node;cartilage;colon;blood;skeletal muscle;bone marrow;pancreas;prostate;cerebral cortex;bone;placenta;liver;testis;spleen;germinal center;brain;thymus; superior cervical ganglion;lymph node;white blood cells;pons;caudate nucleus;atrioventricular node;skeletal muscle;bone marrow;fetal brain;testis;whole blood;trigeminal ganglion;tonsil; 0.39977 0.15177 -0.799052816 12.45576787 62.29282 1.61055 RASGRP3 0.110282852347241 0.889454831512268 0.000262316140491388 RAS guanyl releasing protein 3 FUNCTION: Guanine nucleotide exchange factor (GEF) for Ras and Rap1. {ECO:0000269|PubMed:10934204}.; . . . . 0.57564 . 0.378498378 75.58386412 567.50125 4.83654 RASGRP4 0.0501177515861943 0.949689038705229 0.000193209708577043 RAS guanyl releasing protein 4 FUNCTION: Functions as a cation- and diacylglycerol (DAG)- regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. May function in mast cells differentiation. {ECO:0000269|PubMed:11880369, ECO:0000269|PubMed:11956218, ECO:0000269|PubMed:12493770, ECO:0000269|PubMed:18024961}.; . TISSUE SPECIFICITY: Expressed by mast cells and their progenitors (at protein level). Specifically expressed in mononuclear leukocytes. Highly expressed in myeloid cells compared to lymphoid cells. Also detected in heart, skeletal muscle, spleen, liver, placenta and lung. Not detected in brain. Isoform 1 is the major isoform in normal individuals. Isoform 2 is more significantly expressed in a patient with asthma. Isoform 3 is more significantly expressed in a patient with asthma and a mastocytosis patient. {ECO:0000269|PubMed:11880369, ECO:0000269|PubMed:11956218}.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;blood;skeletal muscle;bone marrow;pancreas;prostate;whole body;lung;bone;testis;kidney;brain;mammary gland; . 0.10484 0.10255 -0.042196577 50.49539986 636.51465 5.07492 RASIP1 0.975494281851725 0.0245046328571197 1.08529115523719e-06 Ras interacting protein 1 FUNCTION: Required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. Acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Regulates the activity of Rho GTPases in part by recruiting ARHGAP29 and suppressing RhoA signaling and dampening ROCK and MYH9 activities in endothelial cells (By similarity). May act as effector for Golgi-bound HRAS and other Ras-like proteins. May promote HRAS- mediated transformation. Negative regulator of amino acid starvation-induced autophagy. {ECO:0000250, ECO:0000269|PubMed:15031288, ECO:0000269|PubMed:22354037}.; . TISSUE SPECIFICITY: Highly expressed in heart. Detected at lower levels in placenta and pancreas. {ECO:0000269|PubMed:15031288}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;parathyroid;choroid;skin;uterus;prostate;lung;thyroid;placenta;liver;testis;cervix;spleen;kidney;brain;mammary gland;aorta;stomach; superior cervical ganglion;trigeminal ganglion; 0.15092 0.09074 . . 1592.61427 7.38413 RASL10A 0.678377624022204 0.301446544539358 0.0201758314384377 RAS like family 10 member A FUNCTION: Potent inhibitor of cellular proliferation. {ECO:0000269|PubMed:15833841}.; . TISSUE SPECIFICITY: Expression appears to be strictly limited to the central nervous system. {ECO:0000269|PubMed:8975699}.; unclassifiable (Anatomical System);lung;whole body;ovary;hypothalamus;testis;brain; amygdala;whole brain;temporal lobe;globus pallidus; 0.09460 . . . 3.61576 0.13234 RASL10B 0.0367926151825494 0.832766797189275 0.130440587628176 RAS like family 10 member B FUNCTION: May facilitate the release of atrial natriuretic peptide by cardiomyocytes and hence play a role in the regulation of arterial pressure. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at high levels in skeletal muscle and, at much lower levels, in heart, brain and pancreas. {ECO:0000269|PubMed:17984325}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;parathyroid;choroid;skeletal muscle;uterus;lung;optic nerve;liver;pituitary gland;testis;brain; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.19256 0.11192 0.170987912 65.5579146 48.9651 1.36687 RASL11A 0.00768974207631144 0.779578825865423 0.212731432058265 RAS like family 11 member A FUNCTION: Regulator of rDNA transcription. Acts in cooperation UBF/UBTF and positively regulates RNA polymerase I transcription (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Down-regulated in prostate tumors compared to normal prostate tissue. High levels found in colon tumor and normal colon tissue followed by small intestine, liver, jejunum, ileum, bladder and aorta. Lowest levels observed in endothelial cells. {ECO:0000269|PubMed:15033445, ECO:0000269|PubMed:17628721}.; unclassifiable (Anatomical System);choroid;fovea centralis;lens;retina;prostate;optic nerve;lung;oesophagus;bone;macula lutea;kidney;mammary gland;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.16091 0.11571 -0.139478553 43.29440906 29.53125 0.94375 RASL11B 0.290784777820631 0.68838048826318 0.0208347339161884 RAS like family 11 member B . . TISSUE SPECIFICITY: Widely expressed with highest levels in placenta and primary macrophages. {ECO:0000269|PubMed:17628721}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;muscle;lens;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;atrioventricular node;cerebellum; 0.49003 0.10864 -0.095386216 46.48502005 63.84681 1.63863 RASL12 0.00696822152010853 0.761549457701035 0.231482320778856 RAS like family 12 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;prostate;optic nerve;whole body;lung;cerebral cortex;placenta;macula lutea;iris;liver;testis;kidney;spinal ganglion;brain; ciliary ganglion; 0.12306 0.14980 -0.60427181 17.74593064 28.94334 0.92475 RASSF1 4.85820372401728e-08 0.118723573683744 0.881276377734219 Ras association domain family member 1 FUNCTION: Potential tumor suppressor. Required for death receptor- dependent apoptosis. Mediates activation of STK3/MST2 and STK4/MST1 during Fas-induced apoptosis by preventing their dephosphorylation. When associated with MOAP1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF10 stimulation. Isoform A interacts with CDC20, an activator of the anaphase-promoting complex, APC, resulting in the inhibition of APC activity and mitotic progression. Inhibits proliferation by negatively regulating cell cycle progression at the level of G1/S-phase transition by regulating accumulation of cyclin D1 protein. Isoform C has been shown not to perform these roles, no function has been identified for this isoform. Isoform A disrupts interactions among MDM2, DAXX and USP7, thus contributing to the efficient activation of TP53 by promoting MDM2 self-ubiquitination in cell-cycle checkpoint control in response to DNA damage. {ECO:0000269|PubMed:10888881, ECO:0000269|PubMed:11333291, ECO:0000269|PubMed:12024041, ECO:0000269|PubMed:14743218, ECO:0000269|PubMed:15109305, ECO:0000269|PubMed:15949439, ECO:0000269|PubMed:16510573, ECO:0000269|PubMed:18566590, ECO:0000269|PubMed:21199877}.; . TISSUE SPECIFICITY: Isoform A and isoform C are ubiquitously expressed in all tissues tested, however isoform A is absent in many corresponding cancer cell lines. Isoform B is mainly expressed in hematopoietic cells. {ECO:0000269|PubMed:10888881, ECO:0000269|PubMed:11333291}.; ovary;adrenal medulla;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;gum;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; testis;white blood cells; 0.33770 0.42420 0.663285274 84.55414013 2290.51824 8.85978 RASSF1-AS1 . . . RASSF1 antisense RNA 1 . . . . . . . . . . . RASSF2 0.000156231740850229 0.967043687129933 0.032800081129217 Ras association domain family member 2 FUNCTION: Potential tumor suppressor. Acts as a KRAS-specific effector protein. May promote apoptosis and cell cycle arrest. Stabilizes STK3/MST2 by protecting it from proteasomal degradation. {ECO:0000269|PubMed:12732644, ECO:0000269|PubMed:16012945, ECO:0000269|PubMed:19525978}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in brain, placenta, peripheral blood and lung. Frequently down-regulated in lung tumor cell lines. {ECO:0000269|PubMed:12732644}.; . . 0.10467 0.12812 -0.203796826 38.81811748 121.9418 2.40404 RASSF3 0.00159786199358572 0.691545895947598 0.306856242058816 Ras association domain family member 3 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11965544}.; unclassifiable (Anatomical System);whole body;colon;blood;skin;bone marrow; . 0.09178 0.09111 -0.029247611 51.40363293 115.55515 2.33696 RASSF4 2.04594734373322e-11 0.017524440298382 0.982475559681159 Ras association domain family member 4 FUNCTION: Potential tumor suppressor. May act as a KRAS effector protein. May promote apoptosis and cell cycle arrest. {ECO:0000269|PubMed:15574778}.; . TISSUE SPECIFICITY: Widely expressed. Frequently down-regulated in tumor cell lines. {ECO:0000269|PubMed:15574778}.; myocardium;ovary;adrenal medulla;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; . 0.09920 0.09317 0.733063566 86.27034678 1210.23369 6.58766 RASSF5 0.248711065765209 0.74489445807152 0.00639447616327127 Ras association domain family member 5 FUNCTION: Potential tumor suppressor. Seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. Isoform 2 stimulates lymphocyte polarization and the patch-like distribution of ITGAL/LFA-1, resulting in an enhanced adhesion to ICAM1. Together with RAP1A may participate in regulation of microtubule growth. The association of isoform 2 with activated RAP1A is required for directional movement of endothelial cells during wound healing. May be involved in regulation of Ras apoptotic function. The RASSF5-STK4/MST1 complex may mediate HRAS and KRAS induced apoptosis. {ECO:0000269|PubMed:12676952, ECO:0000269|PubMed:12845325, ECO:0000269|PubMed:15569673}.; . TISSUE SPECIFICITY: Widely expressed. Frequently down-regulated in lung tumor cell lines and primary lung tumors. {ECO:0000269|PubMed:11965544, ECO:0000269|PubMed:12676952}.; lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;thyroid;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;pharynx;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach;thymus; white blood cells;whole blood;bone marrow; 0.15676 . . . 253.21721 3.42374 RASSF6 1.00445854817251e-17 0.000332639012674195 0.999667360987326 Ras association domain family member 6 FUNCTION: Involved in the induction of apoptosis, through both caspase-dependent and caspase-independent pathways. May act as a Ras effector protein. May suppress the serum-induced basal levels of NF-kappa-B (By similarity). {ECO:0000250, ECO:0000269|PubMed:17367779}.; . TISSUE SPECIFICITY: Highest expression in thymus, kidney and placenta. Also detected in colon, small intestine and lung. Tends to be down-regulated in 30-60% of tumors derived from breast, colon, kidney liver, rectum, pancreas, stomach and the thyroid gland compared to the normal counterpart. {ECO:0000269|PubMed:17404571}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;salivary gland;intestine;pharynx;colon;parathyroid;blood;skin;breast;prostate;lung;placenta;liver;testis;germinal center;kidney;brain;bladder;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.08711 0.09740 1.330184494 94.17315405 2569.48259 9.47129 RASSF7 3.45003416366976e-06 0.348512736895499 0.651483813070338 Ras association domain family member 7 FUNCTION: Negatively regulates stress-induced JNK activation and apoptosis by promoting MAP2K7 phosphorylation and inhibiting its ability to activate JNK. Following prolonged stress, anti- apoptotic effect stops because of degradation of RASSF7 protein via the ubiquitin-proteasome pathway. Required for the activation of AURKB and chromosomal congression during mitosis where it stimulates microtubule polymerization. {ECO:0000269|PubMed:20629633, ECO:0000269|PubMed:21278800}.; . . unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;blood;lens;skin;uterus;prostate;lung;endometrium;placenta;testis;spleen;kidney;brain;stomach; subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;cerebellum; 0.10244 0.10107 0.488730112 79.52347252 1527.39187 7.26067 RASSF8 0.841236340481478 0.158636685315272 0.000126974203250015 Ras association domain family member 8 . . TISSUE SPECIFICITY: Widely expressed as a 6.2 kb transcript. A 2.2 kb alternatively spliced transcript is expressed exclusively in testis. {ECO:0000269|PubMed:10951517}.; unclassifiable (Anatomical System);medulla oblongata;heart;placenta;kidney; testis - interstitial;superior cervical ganglion;testis; 0.29739 0.12378 -0.314027422 31.9297004 106.48295 2.23919 RASSF8-AS1 . . . RASSF8 atnisense RNA 1 . . . . . . . . . . . RASSF9 7.70404622377727e-05 0.755070432188619 0.244852527349144 Ras association domain family member 9 FUNCTION: May play a role in regulating vesicuar trafficking in cells. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;colon;skin;skeletal muscle;uterus;pancreas;lung;bone;spleen;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.22794 0.10688 0.376678994 75.50719509 331.1863 3.87150 RASSF10 . . . Ras association domain family member 10 . . TISSUE SPECIFICITY: Expressed in brain. Tends to be down-regulated in astrocytic gliomas due to promoter methylation. Methylation occurs early in gliomagenesis and the extent of methylation parallels with higher glioma grades, so that methylation is observed in close to 70% WHO grade IV primary glioblastomas, but not in grade I astrocytomas. {ECO:0000269|PubMed:20956940}.; . . . 0.10655 . . . . RAVER1 0.982340267394972 0.0176573424839899 2.39012103801208e-06 ribonucleoprotein, PTB-binding 1 FUNCTION: Cooperates with PTBP1 to modulate regulated alternative splicing events. Promotes exon skipping. Cooperates with PTBP1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA (By similarity). {ECO:0000250}.; . . lymphoreticular;smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum;thymus; superior cervical ganglion;ciliary ganglion; 0.21648 0.10722 -0.222203495 37.54423213 120.73412 2.39439 RAVER2 1.85996394365043e-06 0.9680629530284 0.031935187007656 ribonucleoprotein, PTB-binding 2 FUNCTION: May bind single-stranded nucleic acids. {ECO:0000305}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;iris;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;liver;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;pons; 0.16139 0.09116 -0.113792788 45.25831564 48.72242 1.36171 RAX 0.841214635572597 0.155816610762897 0.00296875366450603 retina and anterior neural fold homeobox FUNCTION: Plays a critical role in eye formation by regulating the initial specification of retinal cells and/or their subsequent proliferation. Binds to the photoreceptor conserved element-I (PCE-1/Ret 1) in the photoreceptor cell-specific arrestin promoter.; . TISSUE SPECIFICITY: Expressed in the developing eye and weakly expressed in the adult retina.; uterus;optic nerve;heart;macula lutea;visual apparatus;fovea centralis;choroid;lens;skin;retina; dorsal root ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;skeletal muscle; 0.25010 0.11043 . . 1947.25801 8.12037 RAX2 0.510132428611179 0.421234913104978 0.0686326582838427 retina and anterior neural fold homeobox 2 FUNCTION: May be involved in modulating the expression of photoreceptor specific genes. Binds to the Ret-1 and Bat-1 element within the rhodopsin promoter. {ECO:0000269|PubMed:15028672}.; DISEASE: Macular degeneration, age-related, 6 (ARMD6) [MIM:613757]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. {ECO:0000269|PubMed:15028672}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Cone-rod dystrophy 11 (CORD11) [MIM:610381]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. {ECO:0000269|PubMed:15028672}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.20867 0.17499 . . 63.15058 1.62602 RB1 0.999999833394892 1.66605108380864e-07 1.3387269714778e-18 retinoblastoma 1 FUNCTION: Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity). In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity. {ECO:0000250, ECO:0000269|PubMed:15084261}.; DISEASE: Childhood cancer retinoblastoma (RB) [MIM:180200]: Congenital malignant tumor that arises from the nuclear layers of the retina. It occurs in about 1:20'000 live births and represents about 2% of childhood malignancies. It is bilateral in about 30% of cases. Although most RB appear sporadically, about 20% are transmitted as an autosomal dominant trait with incomplete penetrance. The diagnosis is usually made before the age of 2 years when strabismus or a gray to yellow reflex from pupil ('cat eye') is investigated. {ECO:0000269|PubMed:10671068, ECO:0000269|PubMed:11524739, ECO:0000269|PubMed:1352883, ECO:0000269|PubMed:2594029, ECO:0000269|PubMed:7704558, ECO:0000269|PubMed:7795591, ECO:0000269|PubMed:7927327, ECO:0000269|PubMed:8346255, ECO:0000269|PubMed:8605116, ECO:0000269|PubMed:8776589, ECO:0000269|PubMed:9140452, ECO:0000269|PubMed:9311732, ECO:0000269|PubMed:9973307}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bladder cancer (BLC) [MIM:109800]: A malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas that begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Osteogenic sarcoma (OSRC) [MIM:259500]: A sarcoma originating in bone-forming cells, affecting the ends of long bones. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the retina.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; amygdala;subthalamic nucleus;prefrontal cortex; 0.99984 0.96982 -0.690637458 15.12149092 183.73881 2.94113 RB1CC1 0.999999798846797 2.01153202805607e-07 4.28675107823123e-19 RB1 inducible coiled-coil 1 FUNCTION: Plays a role as a modulator of TGF-beta-signaling by restricting substrate specificity of RNF111. Involved in autophagy. Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1. Required for the formation of the autophagosome-like double- membrane structure that surrounds the Salmonella-containing vacuole (SCV) duting S.typhimurium infection and subsequent xenophagy. Autophagy positively regulates repair of DNA damage induced by ionizing radiation and negatively regulates apoptosis. Plays an indispensible role in fetal hematopoiesis and in the regulation of neuronal homeostasis (By similarity). Implicated in the regulation of RB1 expression. Functions as a DNA-binding transcription factor. Is a potent regulator of the RB1 pathway and a mediator that plays a crucial role in muscular differentiation. Expression is, thus, a prerequisite for myogenic differentiation. Inhibits PTK2/FAK1 and PTK2B/PYK2 activity and activation of downstream signaling pathways. {ECO:0000250, ECO:0000269|PubMed:10769033, ECO:0000269|PubMed:12095676, ECO:0000269|PubMed:12163359, ECO:0000269|PubMed:12221124, ECO:0000269|PubMed:14533007, ECO:0000269|PubMed:21775823, ECO:0000269|PubMed:23262492}.; . TISSUE SPECIFICITY: Expression levels correlated closely with those of RB1 in cancer cell lines as well as in various normal human tissues. Abundantly expressed in human musculoskeletal and cultured osteosarcoma cells. {ECO:0000269|PubMed:11850849, ECO:0000269|PubMed:12163359}.; smooth muscle;ovary;colon;parathyroid;skin;retina;uterus;prostate;atrium;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);heart;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;mesenchyma;placenta;liver;spleen;kidney;stomach;peripheral nerve; amygdala;occipital lobe;subthalamic nucleus;medulla oblongata;testis - interstitial;superior cervical ganglion;temporal lobe;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.82038 0.21518 -1.587406381 3.113941967 234.10831 3.30711 RBAK 0.0096768994616337 0.979406650411382 0.0109164501269846 RB associated KRAB zinc finger FUNCTION: May repress E2F-dependent transcription. May promote AR- dependent transcription. {ECO:0000269|PubMed:10702291, ECO:0000269|PubMed:14664718}.; . TISSUE SPECIFICITY: Expressed in bone, brain, heart, kidney, liver, lung, pancreas and placenta. {ECO:0000269|PubMed:10702291}.; unclassifiable (Anatomical System);lacrimal gland;adrenal gland;bone;thyroid;placenta;liver;colon;germinal center;skin;skeletal muscle;stomach;retina; . 0.54015 0.13176 0.001895464 54.03397028 184.71939 2.94988 RBAK-RBAKDN 0.724663171287708 0.262263845385863 0.013072983326429 RBAK-RBAKDN readthrough . . . . . . . . . 1634.64779 7.47256 RBAKDN . . . RBAK downstream neighbor (non-protein coding) . . . . . . . . . . . RBBP4 0.989804589203081 0.0101947904425842 6.20354334374114e-07 retinoblastoma binding protein 4 FUNCTION: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex. {ECO:0000269|PubMed:10866654}.; . . . . 0.62179 0.35026 -0.229483771 36.86010852 29.97102 0.95729 RBBP4P1 . . . retinoblastoma binding protein 4 pseudogene 1 . . . . . . . . . . . RBBP4P2 . . . retinoblastoma binding protein 4 pseudogene 2 . . . . . . . . . . . RBBP4P3 . . . retinoblastoma binding protein 4 pseudogene 3 . . . . . . . . . . . RBBP4P4 . . . retinoblastoma binding protein 4 pseudogene 4 . . . . . . . . . . . RBBP4P5 . . . retinoblastoma binding protein 4 pseudogene 5 . . . . . . . . . . . RBBP4P6 . . . retinoblastoma binding protein 4 pseudogene 6 . . . . . . . . . . . RBBP5 0.995054147429424 0.00494583117895029 2.13916256216786e-08 retinoblastoma binding protein 5 FUNCTION: In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid (By similarity). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. {ECO:0000250, ECO:0000269|PubMed:19556245}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;cerebral cortex;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;liver;kidney;mammary gland;stomach; . 0.42612 0.10608 -0.471992905 23.03609342 7.88991 0.28945 RBBP6 0.999999002580924 9.97419075570974e-07 8.67095125900412e-19 retinoblastoma binding protein 6 FUNCTION: E3 ubiquitin-protein ligase which promotes ubiquitination of YBX1, leading to its degradation by the proteasome (PubMed:18851979). May play a role as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in increase of MDM2-mediated ubiquitination and degradation of p53/TP53; may function as negative regulator of p53/TP53, leading to both apoptosis and cell growth (By similarity). Regulates DNA-replication and the stability of chromosomal common fragile sites (CFSs) in a ZBTB38- and MCM10- dependent manner. Controls ZBTB38 protein stability and abundance via ubiquitination and proteasomal degradation, and ZBTB38 in turn negatively regulates the expression of MCM10 which plays an important role in DNA-replication (PubMed:24726359). {ECO:0000250|UniProtKB:P97868, ECO:0000269|PubMed:18851979, ECO:0000269|PubMed:24726359}.; . TISSUE SPECIFICITY: Highly expressed in the placenta and testis. Expressed at lower levels in the brain, heart, kidney, liver and lung. Overexpressed in esophageal cancer. {ECO:0000269|PubMed:15475430}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;cornea;placenta;head and neck;kidney;stomach;thymus; subthalamic nucleus;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;white blood cells;pons;trigeminal ganglion;cingulate cortex; 0.75696 0.12691 -2.116743963 1.527482897 388.06228 4.14933 RBBP6P1 . . . retinoblastoma binding protein 6 pseudogene 1 . . . . . . . . . . . RBBP7 0.983294257742315 0.0166954510476466 1.02912100382442e-05 retinoblastoma binding protein 7 FUNCTION: Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex. {ECO:0000269|PubMed:10866654}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;lung;pia mater;cornea;adrenal gland;placenta;head and neck;kidney;stomach;aorta; . 0.97005 0.31407 -0.141298762 42.87567823 1069.29067 6.26776 RBBP8 0.000108378971563585 0.999790808592162 0.000100812436275003 retinoblastoma binding protein 8 FUNCTION: Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in processing meiotic and mitotic double-strand breaks (DSBs) by ensuring both resection and intrachromosomal association of the broken ends. Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA. Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage. Promotes microhomology-mediated alternative end joining (A-NHEJ) during class-switch recombination and plays an essential role in chromosomal translocations. {ECO:0000269|PubMed:10764811, ECO:0000269|PubMed:10910365, ECO:0000269|PubMed:15485915, ECO:0000269|PubMed:16581787, ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17965729, ECO:0000269|PubMed:19202191, ECO:0000269|PubMed:19759395, ECO:0000269|PubMed:20064462, ECO:0000269|PubMed:20829486}.; DISEASE: Seckel syndrome 2 (SCKL2) [MIM:606744]: A rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and mental retardation. {ECO:0000269|PubMed:21998596}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Jawad syndrome (JWDS) [MIM:251255]: A syndrome characterized by congenital microcephaly, moderately severe mental retardation, and symmetrical digital anomalies. Digital malformations of variable degree include hallux valgus, syndactyly of toes 4 and 5, short fifth fingers, single flexion crease of fifth fingers, polydactyly and synpolydactyly. {ECO:0000269|PubMed:21998596}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Genetic variability in RBBP8 is noted as a factor in BRCA1-associated breast cancer risk (PubMed:21799032). Exhibits sensitivity to tamoxifen in certain breast cancer cell lines (PubMed:18171986). {ECO:0000269|PubMed:18171986, ECO:0000269|PubMed:21799032}.; . ovary;salivary gland;intestine;colon;skin;retina;uterus;frontal lobe;endometrium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;pharynx;blood;skeletal muscle;breast;lung;cornea;nasopharynx;placenta;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.82222 . -0.641086234 16.6784619 66.92298 1.69043 RBBP8NL 0.00748846457322915 0.976837773017523 0.0156737624092478 RBBP8 N-terminal like . . . . . 0.05961 . . . 2614.50579 9.57273 RBBP8P1 . . . retinoblastoma binding protein 8 pseudogene 1 . . . . . . . . . . . RBBP8P2 . . . retinoblastoma binding protein 8 pseudogene 2 . . . . . . . . . . . RBBP9 0.10391013399072 0.863960454291193 0.0321294117180873 retinoblastoma binding protein 9 FUNCTION: May play a role in the transformation process due to its capacity to confer resistance to the growth-inhibitory effects of TGF-beta1 through interaction with retinoblastoma and the subsequent displacement of E2F-1.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher levels in tumor tissues than in normal tissues.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;pharynx;blood;lens;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.27549 0.15710 -0.095386216 46.48502005 24.18644 0.79403 RBCK1 0.212094447600287 0.787528696036451 0.000376856363261886 RANBP2-type and C3HC4-type zinc finger containing 1 FUNCTION: E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF- kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF- RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types. {ECO:0000269|PubMed:12629548, ECO:0000269|PubMed:17006537, ECO:0000269|PubMed:17449468, ECO:0000269|PubMed:18711448, ECO:0000269|PubMed:19136968, ECO:0000269|PubMed:20005846, ECO:0000269|PubMed:21455173, ECO:0000269|PubMed:21455180, ECO:0000269|PubMed:21455181}.; DISEASE: Polyglucosan body myopathy 1 with or without immunodeficiency (PGBM1) [MIM:615895]: A disease characterized by polyglucosan storage myopathy associated with early-onset progressive muscle weakness and progressive dilated cardiomyopathy, which may necessitate cardiac transplant in severe cases. Some patients present with severe immunodeficiency, invasive bacterial infections and chronic autoinflammation. {ECO:0000269|PubMed:23104095, ECO:0000269|PubMed:23798481}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;myocardium;medulla oblongata;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;muscle;urinary;adrenal cortex;blood;lens;breast;pancreas;lung;placenta;macula lutea;liver;cervix;head and neck;spleen;kidney;mammary gland;stomach;thymus; lung;placenta;prefrontal cortex;liver;tumor;testis;trigeminal ganglion; 0.19753 0.11590 -0.912929826 9.902099552 17.52607 0.61540 RBFA 0.000358068013612274 0.831218399363685 0.168423532622703 ribosome binding factor A (putative) . . . unclassifiable (Anatomical System);lymph node;cartilage;ovary;colon;skin;skeletal muscle;breast;prostate;pancreas;lung;endometrium;larynx;placenta;visual apparatus;pituitary gland;duodenum;liver;cervix;head and neck;germinal center;kidney;bladder;tonsil;stomach; superior cervical ganglion;atrioventricular node; 0.07773 . 1.552504757 95.63576315 2649.40245 9.65809 RBFADN . . . RBFA downstream neighbor (non-protein coding) . . . . . . . . . . . RBFOX1 0.935961018293749 0.064036562829719 2.41887653191339e-06 RNA binding protein, fox-1 homolog (C. elegans) 1 FUNCTION: RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Regulates alternative splicing of tissue-specific exons and of differentially spliced exons during erythropoiesis. {ECO:0000269|PubMed:16537540}.; . TISSUE SPECIFICITY: Predominantly expressed in muscle and brain.; unclassifiable (Anatomical System);amygdala;heart;ovary;hypothalamus;muscle;parathyroid;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;prostate;optic nerve;whole body;lung;placenta;macula lutea;visual apparatus;kidney;brain;cerebellum; whole brain;amygdala;dorsal root ganglion;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;cerebellum peduncles;temporal lobe;atrioventricular node;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex; . . -0.466531444 23.51380042 64.21028 1.64414 RBFOX2 0.993206874904073 0.00679289547761925 2.29618308063389e-07 RNA binding protein, fox-1 homolog (C. elegans) 2 FUNCTION: RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2 to the 3'-splice site. Regulates alternative splicing of tissue-specific exons and of differentially spliced exons during erythropoiesis (By similarity). RNA-binding protein that seems to act as a coregulatory factor of ER-alpha. {ECO:0000250, ECO:0000269|PubMed:11875103}.; . . ovary;developmental;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;frontal lobe;endometrium;cochlea;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;urinary;pharynx;lung;nasopharynx;placenta;macula lutea;liver;cervix;spleen;kidney;stomach;aorta; superior cervical ganglion;cerebellum peduncles;temporal lobe;atrioventricular node;pons;skeletal muscle;uterus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;cerebellum; 0.46697 0.09220 -0.427900189 25.14744043 30.95685 0.97922 RBFOX3 . . . RNA binding protein, fox-1 homolog (C. elegans) 3 FUNCTION: RNA-binding protein that regulates alternative splicing events. {ECO:0000250}.; . . unclassifiable (Anatomical System);prostate;visual apparatus;brain; superior cervical ganglion;globus pallidus;atrioventricular node; . . -0.141298762 42.87567823 36.57701 1.09709 RBKS 1.93197572918752e-05 0.461679771642971 0.538300908599737 ribokinase . . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;iris;testis;brain;unclassifiable (Anatomical System);cartilage;lens;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;spleen;kidney;stomach; . 0.10745 . 0.15257911 64.60839821 150.62936 2.67990 RBL1 1.76076225583568e-05 0.999971037080589 1.13552968531571e-05 retinoblastoma-like 1 FUNCTION: Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation. Forms a complex with adenovirus E1A and with SV40 large T antigen. May bind and modulate functionally certain cellular proteins with which T and E1A compete for pocket binding. May act as a tumor suppressor.; . . unclassifiable (Anatomical System);myocardium;blood;skin;retina;uterus;breast;pancreas;lung;larynx;liver;testis;head and neck;germinal center; superior cervical ganglion;testis - interstitial; 0.83315 0.20766 -0.817464788 11.97806086 173.54974 2.86831 RBL2 0.957797035589511 0.0422029573892403 7.02124914199613e-09 retinoblastoma-like 2 FUNCTION: Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation, associates preferentially with E2F5. Binds to cyclins A and E. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. May act as a tumor suppressor.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;white blood cells; 0.84365 . -0.729274834 14.15428167 1350.04388 6.90134 RBM3 0.700968680872873 0.282585571984742 0.0164457471423843 RNA binding motif (RNP1, RRM) protein 3 FUNCTION: Cold-inducible mRNA binding protein that enhances global protein synthesis at both physiological and mild hypothermic temperatures. Reduces the relative abundance of microRNAs, when overexpressed. Enhances phosphorylation of translation initiation factors and active polysome formation (By similarity). {ECO:0000250}.; . . ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;prostate;optic nerve;endometrium;bone;thyroid;germinal center;brain;bladder;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;epididymis;nasopharynx;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; white blood cells; 0.34752 . -0.09720619 46.20193442 10.09763 0.36825 RBM4 0.943908956686511 0.0558840238649025 0.000207019448587092 RNA binding motif protein 4 FUNCTION: RNA-binding factor involved in multiple aspects of cellular processes like alternative splicing of pre-mRNA and translation regulation. Modulates alternative 5'-splice site and exon selection. Acts as a muscle cell differentiation-promoting factor. Activates exon skipping of the PTB pre-mRNA during muscle cell differentiation. Antagonizes the activity of the splicing factor PTBP1 to modulate muscle cell-specific exon selection of alpha tropomyosin. Binds to intronic pyrimidine-rich sequence of the TPM1 and MAPT pre-mRNAs. Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA. Exerts a suppressive activity on Cap-dependent translation via binding to CU-rich responsive elements within the 3'UTR of mRNAs, a process increased under stress conditions or during myocytes differentiation. Recruits EIF4A1 to stimulate IRES-dependent translation initiation in respons to cellular stress. Associates to internal ribosome entry segment (IRES) in target mRNA species under stress conditions. Plays a role for miRNA-guided RNA cleavage and translation suppression by promoting association of AGO2- containing miRNPs with their cognate target mRNAs. Associates with miRNAs during muscle cell differentiation. Binds preferentially to 5'-CGCGCG[GCA]-3' motif in vitro. {ECO:0000269|PubMed:12628928, ECO:0000269|PubMed:16260624, ECO:0000269|PubMed:16777844, ECO:0000269|PubMed:16934801, ECO:0000269|PubMed:17284590, ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:19801630, ECO:0000269|PubMed:21343338, ECO:0000269|PubMed:21518792}.; . TISSUE SPECIFICITY: Expressed in the cerebellum. Expressed in neurons and glial cells, including layers II neurons in the frontal cortex and CA1 pyramidal neurons in the hippocampus. Expressed in heart, liver, pancreas, skeletal muscle, placenta, primary fibroblasts and peripheral blood monocytes (at protein level). Ubiquitously expressed. Highly expressed in heart, placenta and skeletal muscle. Weakly expressed in pancreas, kidney, liver, lung and brain. {ECO:0000269|PubMed:12628928, ECO:0000269|PubMed:16260624, ECO:0000269|PubMed:16777844, ECO:0000269|PubMed:18708123}.; lymphoreticular;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;pineal body;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; subthalamic nucleus;testis - seminiferous tubule;testis;white blood cells;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle;cerebellum; 0.61704 0.14710 -0.516085732 21.20193442 1.11171 0.02963 RBM4B 0.442246701889638 0.55111486391099 0.00663843419937172 RNA binding motif protein 4B FUNCTION: Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in liver and kidney (at protein level). Ubiquitously expressed. {ECO:0000269|PubMed:12628928, ECO:0000269|PubMed:18708123}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;pons;caudate nucleus;atrioventricular node;cerebellum; 0.35126 0.12378 -0.53631094 20.53550366 30.06102 0.95951 RBM5 0.999999469802352 5.30197648320326e-07 2.24545290162496e-17 RNA binding motif protein 5 FUNCTION: Component of the spliceosome A complex. Regulates alternative splicing of a number of mRNAs. May modulate splice site pairing after recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of the intron. May both positively and negatively regulate aopotosis by regulating the alternative splicing of several genes involved in this process, including FAS and CASP2/caspase-2. In the case of FAS, promotes exclusion of exon 6 thereby producing a soluble form of FAS that inhibits apoptosis. In the case of CASP2/caspase-2, promotes exclusion of exon 9 thereby producing a catalytically active form of CASP2/Caspase-2 that induces apoptosis. {ECO:0000269|PubMed:10949932, ECO:0000269|PubMed:12207175, ECO:0000269|PubMed:12581154, ECO:0000269|PubMed:15192330, ECO:0000269|PubMed:16585163, ECO:0000269|PubMed:18840686, ECO:0000269|PubMed:18851835}.; . TISSUE SPECIFICITY: Isoform 5 is widely expressed in normal tissues and is expressed at increased levels in T-leukemic cell lines.; myocardium;ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;cochlea;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;tongue;blood;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;uterus;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus; subthalamic nucleus;testis;pons;parietal lobe; 0.49937 0.11696 -1.111360919 6.717386176 14.39881 0.51975 RBM5-AS1 . . . RBM5 antisense RNA 1 . . . . . . . . . . . RBM6 0.999999963583324 3.64166764082978e-08 3.29685431274461e-20 RNA binding motif protein 6 FUNCTION: Specifically binds poly(G) RNA homopolymers in vitro.; . TISSUE SPECIFICITY: Ubiquitous in adults.; myocardium;smooth muscle;ovary;skin;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;gall bladder;amygdala;heart;cartilage;tongue;adrenal cortex;blood;skeletal muscle;breast;epididymis;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;vein;uterus;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;amnion;head and neck;kidney;stomach;thymus;cerebellum; superior cervical ganglion;olfactory bulb;testis - seminiferous tubule;fetal brain;adrenal cortex;testis;parietal lobe; 0.28469 0.08669 -0.547447733 19.99882048 222.7519 3.22748 RBM7 0.769935289328386 0.22833441162116 0.00173029905045399 RNA binding motif protein 7 FUNCTION: Possible involved in germ cell RNA processing and meiosis.; . . . . 0.24926 0.10196 -0.229483771 36.86010852 13.13146 0.47790 RBM8A 0.962186022966541 0.0377365874711994 7.73895622590703e-05 RNA binding motif protein 8A FUNCTION: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP- bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Its removal from cytoplasmic mRNAs requires translation initiation from EJC-bearing spliced mRNAs. Associates preferentially with mRNAs produced by splicing. Does not interact with pre-mRNAs, introns, or mRNAs produced from intronless cDNAs. Associates with both nuclear mRNAs and newly exported cytoplasmic mRNAs. The MAGOH-RBM8A heterodimer is a component of the nonsense mediated decay (NMD) pathway. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly. {ECO:0000269|PubMed:12121612, ECO:0000269|PubMed:12718880, ECO:0000269|PubMed:12730685, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:19409878, ECO:0000269|PubMed:22203037}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach;aorta; amygdala;occipital lobe;medulla oblongata;subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;pons;caudate nucleus;cingulate cortex;parietal lobe;cerebellum; 0.36480 0.14896 -0.075159878 47.78839349 2.40691 0.08431 RBM8B . . . RNA binding motif protein 8B pseudogene . . . . . . . . . . . RBM10 0.999912181208767 8.7818763001365e-05 2.82316037841841e-11 RNA binding motif protein 10 FUNCTION: May be involved in post-transcriptional processing, most probably in mRNA splicing. Binds to RNA homopolymers, with a preference for poly(G) and poly(U) and little for poly(A) (By similarity). {ECO:0000250, ECO:0000269|PubMed:18315527}.; DISEASE: TARP syndrome (TARPS) [MIM:311900]: A disorder characterized by the Robin sequence (micrognathia, glossoptosis and cleft palate), talipes equinovarus and cardiac defects. {ECO:0000269|PubMed:20451169}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;myocardium;medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;urinary;adrenal cortex;blood;breast;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; fetal brain;cerebellum peduncles;placenta;prefrontal cortex;tumor;white blood cells;skeletal muscle;thymus; 0.17567 0.15702 -0.66859065 15.76433121 77.16708 1.84454 RBM11 2.91015515635607e-05 0.547383659108136 0.4525872393403 RNA binding motif protein 11 FUNCTION: Tissue-specific splicing factor with potential implication in the regulation of alternative splicing during neuron and germ cell differentiation. Antagonizes SRSF1-mediated BCL-X splicing. May affect the choice of alternative 5' splice sites by binding to specific sequences in exons and antagonizing the SR protein SRSF1. {ECO:0000269|PubMed:21984414}.; . TISSUE SPECIFICITY: Expressed in brain, hippocampus, prefrontal cortex, cerebellum, spinal cord, testis, mammary gland, spleen and kidney. Also expressed in fetal brain. {ECO:0000269|PubMed:12036298, ECO:0000269|PubMed:12909339, ECO:0000269|PubMed:21984414}.; . . 0.13652 0.08447 1.616843854 95.96013211 756.11384 5.45080 RBM11P1 . . . RNA binding motif protein 11 pseudogene 1 . . . . . . . . . . . RBM12 0.474673920574839 0.520117688512431 0.00520839091272947 RNA binding motif protein 12 . . . umbilical cord;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;synovium;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;placenta;hypopharynx;amnion;head and neck;kidney;aorta;stomach;cerebellum; superior cervical ganglion; . 0.18648 -0.997481928 8.47487615 238.09276 3.33191 RBM12B 0.120424618919486 0.879350537947157 0.000224843133357538 RNA binding motif protein 12B . . . . . 0.12957 . -0.527216948 20.8893607 359.53554 4.01519 RBM12B-AS1 . . . RBM12B antisense RNA 1 . . . . . 0.14311 . . . 2801.07042 9.99512 RBM14 0.987907650264068 0.0120876948263522 4.65490958001672e-06 RNA binding motif protein 14 FUNCTION: Isoform 1 may function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1. Isoform 2, functions as a transcriptional repressor, modulating transcriptional activities of coactivators including isoform 1, NCOA6 and CITED1.; . TISSUE SPECIFICITY: Expressed in all tissues tested, including brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood lymphocytes.; lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;hypothalamus;muscle;blood;lens;skeletal muscle;bile duct;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;white blood cells;ciliary ganglion;atrioventricular node;thymus;cerebellum; 0.84616 0.14710 -0.710864321 14.5730125 53.61813 1.45786 RBM14-RBM4 0.918848169112948 0.0806263597749429 0.00052547111210922 RBM14-RBM4 readthrough FUNCTION: Isoform 1 may function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1. Isoform 2, functions as a transcriptional repressor, modulating transcriptional activities of coactivators including isoform 1, NCOA6 and CITED1.; . TISSUE SPECIFICITY: Expressed in all tissues tested, including brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood lymphocytes.; . . . . -0.494039303 22.09247464 12.96816 0.47245 RBM15 0.999853092554739 0.000146907425254997 2.00062339094927e-11 RNA binding motif protein 15 FUNCTION: May function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing. High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing. May be implicated in HOX gene regulation. {ECO:0000269|PubMed:17001072, ECO:0000269|PubMed:19786495}.; DISEASE: Note=A chromosomal aberration involving RBM15 may be a cause of acute megakaryoblastic leukemia. Translocation t(1;22)(p13;q13) with MKL1. Although both reciprocal fusion transcripts are detected in acute megakaryoblastic leukemia (AMKL, FAB-M7), the RBM15-MKL1 chimeric protein has all the putative functional domains encoded by each gene and is the candidate oncogene. {ECO:0000269|PubMed:11344311, ECO:0000269|PubMed:11431691}.; . . . 0.41164 0.42963 -0.949752638 9.32413305 173.34726 2.86702 RBM15B 0.998677123640892 0.00132285543099135 2.09281163258801e-08 RNA binding motif protein 15B FUNCTION: May function in the regulation of alternative or illicit splicing. {ECO:0000269|PubMed:16129689}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:16129689}.; ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;placenta;amnion;head and neck;kidney;stomach;thymus; testis - interstitial;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;cerebellum; 0.37868 0.10964 -1.177506449 5.944798301 37.12899 1.10912 RBM17 0.998602405364789 0.00139757070761332 2.39275975367245e-08 RNA binding motif protein 17 FUNCTION: Splice factor that binds to the single-stranded 3'AG at the exon/intron border and promotes its utilization in the second catalytic step. Involved in the regulation of alternative splicing and the utilization of cryptic splice sites. Promotes the utilization of a cryptic splice site created by the beta-110 mutation in the HBB gene. The resulting frameshift leads to sickle cell anemia. {ECO:0000269|PubMed:12015979, ECO:0000269|PubMed:17589525}.; . . . . 0.46979 0.17050 -0.427900189 25.14744043 1.23583 0.04307 RBM17P1 . . . RNA binding motif protein 17 pseudogene 1 . . . . . . . . . . . RBM17P2 . . . RNA binding motif protein 17 pseudogene 2 . . . . . . . . . . . RBM17P3 . . . RNA binding motif protein 17 pseudogene 3 . . . . . . . . . . . RBM17P4 . . . RNA binding motif protein 17 pseudogene 4 . . . . . . . . . . . RBM18 0.0380098730683964 0.929104253581353 0.0328858733502506 RNA binding motif protein 18 . . . . . 0.32921 0.11262 -0.163345027 41.24793583 9.3578 0.34414 RBM19 1.62207368798361e-05 0.999920652624935 6.31266381855323e-05 RNA binding motif protein 19 FUNCTION: Plays a role in embryo pre-implantation development. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the crypts of Lieberkuhn of the intestine and in intestinal neoplasia (at protein level). {ECO:0000269|PubMed:16027046}.; lymphoreticular;ovary;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;blood;lens;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skeletal muscle; 0.23300 0.16815 0.036678689 56.26916726 6590.56227 17.16137 RBM20 . . . RNA binding motif protein 20 FUNCTION: RNA-binding protein that acts as a regulator of mRNA splicing of a subset of genes involved in cardiac development. Regulates splicing of TTN (Titin). {ECO:0000269|PubMed:22466703}.; . TISSUE SPECIFICITY: Expressed in the heart. {ECO:0000269|PubMed:19712804}.; . . 0.35928 . 1.019682101 90.97664544 689.38658 5.23723 RBM22 0.995946455694191 0.00405322297518012 3.21330629256564e-07 RNA binding motif protein 22 FUNCTION: Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle. Involved in both translocations of the nuclear SLU7 to the cytoplasm and the cytosolic calcium-binding protein PDCD6 to the nucleus upon cellular stress responses. {ECO:0000269|PubMed:17045351, ECO:0000269|PubMed:21122810, ECO:0000269|PubMed:22246180}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;placenta;head and neck;kidney;stomach;thymus; superior cervical ganglion;placenta;atrioventricular node;caudate nucleus; 0.39026 0.11262 -0.405853867 26.23260203 9.17971 0.33502 RBM22P1 . . . RNA binding motif protein 22 pseudogene 1 . . . . . . . . . . . RBM22P2 . . . RNA binding motif protein 22 pseudogene 2 . . . . . . . . . . . RBM22P3 . . . RNA binding motif protein 22 pseudogene 3 . . . . . . . . . . . RBM22P4 . . . RNA binding motif protein 22 pseudogene 4 . . . . . . . . . . . RBM22P5 . . . RNA binding motif protein 22 pseudogene 5 . . . . . . . . . . . RBM22P6 . . . RNA binding motif protein 22 pseudogene 6 . . . . . . . . . . . RBM22P7 . . . RNA binding motif protein 22 pseudogene 7 . . . . . . . . . . . RBM22P11 . . . RNA binding motif protein 22 pseudogene 11 . . . . . . . . . . . RBM22P12 . . . RNA binding motif protein 22 pseudogene 12 . . . . . . . . . . . RBM22P13 . . . RNA binding motif protein 22 pseudogene 13 . . . . . . . . . . . RBM23 4.62938214208565e-08 0.823057021776457 0.176942931929722 RNA binding motif protein 23 FUNCTION: Probable RNA-binding protein. May be involved in pre- mRNA splicing process.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;caudate nucleus; 0.12722 0.10253 -0.134019284 43.90776126 2374.33734 9.04113 RBM24 0.196222354193918 0.757508513812541 0.0462691319935416 RNA binding motif protein 24 FUNCTION: Plays a role in myogenic differentiation by regulating MYOG levels. Binds to the 3'-UTR of MYOG mRNA and regulates its stability. {ECO:0000269|PubMed:20977548}.; . . unclassifiable (Anatomical System);heart;cartilage;skeletal muscle;skin;bile duct;uterus;prostate;lung;larynx;trabecular meshwork;liver;testis;head and neck;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.25596 0.07720 0.058937498 58.26256192 202.43727 3.07067 RBM25 0.99999996714713 3.285286971731e-08 2.56538438140027e-20 RNA binding motif protein 25 FUNCTION: RNA-binding protein that acts as a regulator of alternative pre-mRNA splicing. Involved in apoptotic cell death through the regulation of the apoptotic factor BCL2L1 isoform expression. Modulates the ratio of proapoptotic BCL2L1 isoform S to antiapoptotic BCL2L1 isoform L mRNA expression. When overexpressed, stimulates proapoptotic BCL2L1 isoform S 5'-splice site (5'-ss) selection, whereas its depletion caused the accumulation of antiapoptotic BCL2L1 isoform L. Promotes BCL2L1 isoform S 5'-ss usage through the 5'-CGGGCA-3' RNA sequence. Its association with LUC7L3 promotes U1 snRNP binding to a weak 5' ss in a 5'-CGGGCA-3'-dependent manner. Binds to the exonic splicing enhancer 5'-CGGGCA-3' RNA sequence located within exon 2 of the BCL2L1 pre-mRNA. Also involved in the generation of an abnormal and truncated splice form of SCN5A in heart failure. {ECO:0000269|PubMed:18663000, ECO:0000269|PubMed:21859973}.; . . myocardium;lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;gall bladder;heart;tongue;blood;lens;skeletal muscle;macula lutea;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;oesophagus;larynx;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; amygdala;dorsal root ganglion;superior cervical ganglion;occipital lobe;testis - interstitial;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;cingulate cortex;parietal lobe; 0.77196 0.14089 -0.80269335 12.23755603 19.8014 0.67569 RBM26 0.999996998269038 3.00173096204026e-06 3.10038127103154e-16 RNA binding motif protein 26 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; amygdala;subthalamic nucleus;superior cervical ganglion;thyroid;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.49934 0.11069 -1.42004951 4.104741684 557.60054 4.79682 RBM26-AS1 . . . RBM26 antisense RNA 1 . . . . . . . . . . . RBM27 0.999999942051571 5.79484287759644e-08 1.0221324934969e-19 RNA binding motif protein 27 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;blood;retina;bone marrow;uterus;lung;endometrium;larynx;bone;thyroid;placenta;duodenum;testis;cervix;head and neck;germinal center;kidney;mammary gland; medulla oblongata;testis - interstitial;testis - seminiferous tubule;testis; 0.38890 0.10831 -0.841329384 11.36470866 58.70328 1.55270 RBM28 2.04684238620984e-09 0.96182622848746 0.0381737694656975 RNA binding motif protein 28 FUNCTION: Nucleolar component of the spliceosomal ribonucleoprotein complexes. {ECO:0000269|PubMed:17081119}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:18439547}.; ovary;salivary gland;sympathetic chain;intestine;colon;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;gum;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; testis - interstitial;subthalamic nucleus;superior cervical ganglion;trigeminal ganglion;parietal lobe;skeletal muscle; 0.70174 0.09620 1.003094668 90.77022883 692.202 5.24763 RBM33 0.999967324739204 3.26752602816209e-05 5.13954731525536e-13 RNA binding motif protein 33 . . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;larynx;bone;thyroid;pituitary gland;testis;germinal center;pineal gland;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; ciliary ganglion;trigeminal ganglion; 0.15099 . -1.144569759 6.363529134 1720.69538 7.64985 RBM34 7.9464873955861e-09 0.2703934941062 0.729606497947313 RNA binding motif protein 34 . . . . . 0.58870 . -0.844966979 11.1759849 50.60593 1.40016 RBM38 0.859282996288302 0.138553756557534 0.00216324715416447 RNA binding motif protein 38 FUNCTION: RNA-binding protein that specifically bind the 3'-UTR of CDKN1A transcripts, leading to maintain the stability of CDKN1A transcripts, thereby acting as a mediator of the p53/TP53 family to regulate CDKN1A. CDKN1A is a cyclin-dependent kinase inhibitor transcriptionally regulated by the p53/TP53 family to induce cell cycle arrest. Isoform 1, but not isoform 2, has the ability to induce cell cycle arrest in G1 and maintain the stability of CDKN1A transcripts induced by p53/TP53. Also acts as a mRNA splicing factor. Specifically regulates the expression of FGFR2- IIIb, an epithelial cell-specific isoform of FGFR2. Plays a role in myogenic differentiation. {ECO:0000269|PubMed:17050675, ECO:0000269|PubMed:19285943}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;urinary;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; fetal liver;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;bone marrow; 0.16014 0.11106 0.43736446 77.56546355 461.24812 4.45359 RBM39 0.9999969154952 3.08450479210585e-06 8.09112006310456e-15 RNA binding motif protein 39 FUNCTION: Transcriptional coactivator for steroid nuclear receptors ESR1/ER-alpha and ESR2/ER-beta, and JUN/AP-1 (By similarity). May be involved in pre-mRNA splicing process. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in pancreas, skeletal muscle, lung and brain. Expressed at intermediate level in kidney, liver and heart.; lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;cerebral cortex;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; . 0.85822 0.14229 -0.207437529 38.2814343 7.60928 0.28162 RBM41 0.229027554978131 0.763332601494168 0.00763984352770068 RNA binding motif protein 41 FUNCTION: May bind RNA. {ECO:0000305}.; . . unclassifiable (Anatomical System);lung;placenta;pituitary gland;spleen; medulla oblongata;temporal lobe;prefrontal cortex;globus pallidus;pons; 0.12978 0.09592 -0.249709319 35.74545883 29.33957 0.93851 RBM42 0.759889530892988 0.239708836487642 0.000401632619369686 RNA binding motif protein 42 FUNCTION: Binds (via the RRM domain) to the 3'-untranslated region (UTR) of CDKN1A mRNA. {ECO:0000250}.; . . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;gum;germinal center;brain;tonsil;cartilage;tongue;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;oesophagus;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.20400 0.11141 -0.293801652 32.93819297 28.6708 0.91789 RBM43 0.0518667699188216 0.861581766625594 0.0865514634555843 RNA binding motif protein 43 . . . unclassifiable (Anatomical System);lung;ovary;placenta;visual apparatus;lens; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.04235 . 0.148941568 64.31941496 75.64131 1.82117 RBM43P1 . . . RNA binding motif protein 43 pseudogene 1 . . . . . . . . . . . RBM44 0.0141498802590379 0.984553591602209 0.00129652813875333 RNA binding motif protein 44 FUNCTION: Component of intercellular bridges during meiosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells. Not required for fertility (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;endometrium;testis;aorta; . 0.08424 . 0.336225928 73.67893371 522.71902 4.66548 RBM45 0.000125349305556292 0.990228316854008 0.00964633384043575 RNA binding motif protein 45 FUNCTION: RNA-binding protein with binding specificity for poly(C). May play an important role in neural development. {ECO:0000250|UniProtKB:Q8CFD1, ECO:0000269|PubMed:12220514}.; . . unclassifiable (Anatomical System);medulla oblongata;lymph node;heart;ovary;colon;fovea centralis;retina;whole body;lung;frontal lobe;macula lutea;liver;testis;spleen;kidney;brain;mammary gland;stomach; . 0.10040 0.11409 -0.271755481 34.31823543 44.33184 1.27150 RBM46 0.0203628577683536 0.96189583976909 0.0177413024625567 RNA binding motif protein 46 . . . unclassifiable (Anatomical System);lung;testis; subthalamic nucleus;superior cervical ganglion;testis - interstitial;ciliary ganglion;trigeminal ganglion;parietal lobe;skeletal muscle; 0.31238 0.14393 -0.426079032 25.36565228 336.91349 3.89921 RBM47 0.958532355471074 0.0414478575071131 1.97870218133624e-05 RNA binding motif protein 47 . . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;gum;bone;thyroid;testis;amniotic fluid;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;islets of Langerhans;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;trachea;thyroid;adrenal cortex;kidney;fetal thyroid; 0.55945 0.14851 -0.490397599 22.50530786 96.03904 2.11745 RBM48 5.12365921814138e-05 0.670570341841775 0.329378421566044 RNA binding motif protein 48 . . . unclassifiable (Anatomical System);cartilage;umbilical cord;ovary;epidermis;islets of Langerhans;hypothalamus;blood;skeletal muscle;bone marrow;bile duct;lung;nasopharynx;thyroid;placenta;pituitary gland;liver;testis;cervix;head and neck;spleen;germinal center;brain;mammary gland;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;cerebellum; . 0.09861 -0.26993514 34.59542345 49.92944 1.38639 RBM48P1 . . . RNA binding motif protein 48 pseudogene 1 . . . . . . . . . . . RBMS1 0.996886207084215 0.00311375875600332 3.4159781290761e-08 RNA binding motif, single stranded interacting protein 1 FUNCTION: Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication.; . TISSUE SPECIFICITY: Highest amounts are found in placenta, lung and heart.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;iris;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.93381 0.15337 -0.427900189 25.14744043 16.05936 0.56807 RBMS1P1 . . . RNA binding motif, single stranded interacting protein 1 pseudogene 1 . . . . . . . . . . . RBMS2 0.00291479790209536 0.994486965775292 0.0025982363226122 RNA binding motif, single stranded interacting protein 2 . . . unclassifiable (Anatomical System);muscle;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;pancreas;prostate;optic nerve;lung;placenta;macula lutea;hypopharynx;liver;head and neck;spleen;kidney;brain;stomach;peripheral nerve; . . 0.11870 -0.736552314 13.93606983 24.83639 0.81515 RBMS2P1 . . . RNA binding motif, single stranded interacting protein 2 pseudogene 1 . . . . . . . . . . . RBMS3 0.741403241313464 0.25857626975889 2.0488927646316e-05 RNA binding motif, single stranded interacting protein 3 FUNCTION: Binds poly(A) and poly(U) oligoribonucleotides. {ECO:0000269|PubMed:10675610}.; . TISSUE SPECIFICITY: Expressed in fetal brain, fetal lung, fetal liver, heart, brain, placenta, lung, liver, muscle, kidney and pancreas. {ECO:0000269|PubMed:10675610}.; unclassifiable (Anatomical System);breast;meninges;pia mater;ovary;placenta;liver;spleen;head and neck;dura mater;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.60992 0.10820 -0.60427181 17.74593064 25.43983 0.83071 RBMS3-AS1 . . . RBMS3 antisense RNA 1 . . . . . . . . . . . RBMS3-AS2 . . . RBMS3 antisense RNA 2 . . . . . . . . . . . RBMS3-AS3 . . . RBMS3 antisense RNA 3 . . . . . . . . . . . RBMX 0.948299697362106 0.0516659320305191 3.43706073748005e-05 RNA binding motif protein, X-linked FUNCTION: RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single- stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Plays also a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1- beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment. {ECO:0000269|PubMed:12165565, ECO:0000269|PubMed:12761049, ECO:0000269|PubMed:16707624, ECO:0000269|PubMed:18445477, ECO:0000269|PubMed:18541147, ECO:0000269|PubMed:19282290, ECO:0000269|PubMed:21327109}.; DISEASE: Mental retardation, X-linked, syndromic, 11 (MRXS11) [MIM:300238]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXS11 patients manifest moderate intellectual disability and craniofacial dysmorphism. {ECO:0000269|PubMed:25256757}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed strongly in oral keratinocytes, but only weakly detected in oral squamous cell carcinomas (at protein level). {ECO:0000269|PubMed:16707624}.; . . 0.26116 . 0.325313577 73.11276244 16.97983 0.59829 RBMX2 0.772803906392487 0.225526115583186 0.00166997802432709 RNA binding motif protein, X-linked 2 . . . . . 0.06060 0.39625 0.170987912 65.5579146 19.54878 0.67128 RBMX2P1 . . . RNA binding motif protein, X-linked 2 pseudogene 1 . . . . . . . . . . . RBMX2P2 . . . RNA binding motif protein, X-linked 2 pseudogene 2 . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;thymus; . . . . . . . RBMX2P3 . . . RNA binding motif protein, X-linked 2 pseudogene 3 . . . . . . . . . . . RBMX2P4 . . . RNA binding motif protein, X-linked 2 pseudogene 4 . . . . . . . . . . . RBMX2P5 . . . RNA binding motif protein, X-linked 2 pseudogene 5 . . . . . . . . . . . RBMXL1 0.119596956167504 0.874924569809645 0.0054784740228511 RNA binding motif protein, X-linked-like 1 FUNCTION: RNA-binding protein which may be involved in pre-mRNA splicing. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;pharynx;blood;lens;pancreas;pia mater;lung;cornea;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.20063 . 0.72761005 86.08162302 80.60629 1.89749 RBMXL2 0.677816820678495 0.317543675586747 0.00463950373475764 RNA binding motif protein, X-linked-like 2 . . TISSUE SPECIFICITY: Expressed predominantly in spermatocytes and less in round spermatids (at protein level). Expressed in germ cells. {ECO:0000269|PubMed:10958650}.; unclassifiable (Anatomical System);medulla oblongata;lung;hippocampus;testis;kidney; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;appendix;testis;trigeminal ganglion; 0.13906 . . . 1116.15696 6.38015 RBMXL3 . . . RNA binding motif protein, X-linked-like 3 . . . . . 0.09471 . 4.932394334 99.80537863 785.37004 5.53655 RBMXP1 . . . RNA binding motif protein, X-linked pseudogene 1 . . . . . . . . . . . RBMXP2 . . . RNA binding motif protein, X-linked pseudogene 2 . . . . . . . . . . . RBMXP3 . . . RNA binding motif protein, X-linked pseudogene 3 . . . . . . . . . . . RBMXP4 . . . RNA binding motif protein, X-linked pseudogene 4 . . . . . . . . . . . RBMY1A1 . . . RNA binding motif protein, Y-linked, family 1, member A1 FUNCTION: RNA-binding protein involved in pre-mRNA splicing. Required for sperm development. Acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN. Binds non-specifically to mRNAs. {ECO:0000269|PubMed:12165565, ECO:0000269|PubMed:8269511}.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:8269511}.; lung;testis; . . . . . . . RBMY1A3P . . . RNA binding motif protein, Y-linked, family 1, member A3 pseudogene . . . . . . . . . . . RBMY1B . . . RNA binding motif protein, Y-linked, family 1, member B FUNCTION: RNA-binding protein which may be involved in spermatogenesis. Required for sperm development, possibly by participating in pre-mRNA splicing in the testis.; . TISSUE SPECIFICITY: Testis-specific.; . . . . . . . . RBMY1C . . . RNA binding motif protein, Y-linked, family 1, member C FUNCTION: RNA-binding protein involved in pre-mRNA splicing. Required for sperm development. Acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN. Binds non-specifically to mRNAs.; . TISSUE SPECIFICITY: Testis-specific.; . . . . . . . . RBMY1D . . . RNA binding motif protein, Y-linked, family 1, member D FUNCTION: RNA-binding protein which may be involved in spermatogenesis. Required for sperm development, possibly by participating in pre-mRNA splicing in the testis.; . TISSUE SPECIFICITY: Testis-specific.; . . . . . . . . RBMY1E . . . RNA binding motif protein, Y-linked, family 1, member E FUNCTION: RNA-binding protein which may be involved in spermatogenesis. Required for sperm development, possibly by participating in pre-mRNA splicing in the testis.; . TISSUE SPECIFICITY: Testis-specific.; . . . . . . . . RBMY1F . . . RNA binding motif protein, Y-linked, family 1, member F FUNCTION: RNA-binding protein which may be involved in spermatogenesis. Required for sperm development, possibly by participating in pre-mRNA splicing in the testis. {ECO:0000269|PubMed:8269511}.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:8269511}.; unclassifiable (Anatomical System);lung;liver;testis;skin; . 0.13204 . . . . . RBMY1GP . . . RNA binding motif protein, Y-linked, family 1, member G, pseudogene . . . . . . . . . . . RBMY1HP . . . RNA binding motif protein, Y-linked, family 1, member H, pseudogene . . . . . 0.18403 . . . . . RBMY1J . . . RNA binding motif protein, Y-linked, family 1, member J FUNCTION: RNA-binding protein which may be involved in spermatogenesis. Required for sperm development, possibly by participating in pre-mRNA splicing in the testis. {ECO:0000269|PubMed:8269511}.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:8269511}.; unclassifiable (Anatomical System);lung;liver;testis;skin; . . . . . . . RBMY1KP . . . RNA binding motif protein, Y-linked, family 1, member K, pseudogene . . . . . . . . . . . RBMY2AP . . . RNA binding motif protein, Y-linked, family 2, member A pseudogene . . . . . . . . . . . RBMY2BP . . . RNA binding motif protein, Y-linked, family 2, member B pseudogene . . . . . . . . . . . RBMY2CP . . . RNA binding motif protein, Y-linked, family 2, member C pseudogene . . . . . . . . . . . RBMY2DP . . . RNA binding motif protein, Y-linked, family 2, member D pseudogene . . . . . . . . . . . RBMY2EP . . . RNA binding motif protein, Y-linked, family 2, member E pseudogene . . . . . . . . . . . RBMY2FP . . . RNA binding motif protein, Y-linked, family 2, member F pseudogene . . . testis; . . . . . . . RBMY2GP . . . RNA binding motif protein, Y-linked, family 2, member G pseudogene . . . . . . . . . . . RBMY2HP . . . RNA binding motif protein, Y-linked, family 2, member H pseudogene . . . . . . . . . . . RBMY2JP . . . RNA binding motif protein, Y-linked, family 2, member J pseudogene . . . . . . . . . . . RBMY2KP . . . RNA binding motif protein, Y-linked, family 2, member K pseudogene . . . . . . . . . . . RBMY2MP . . . RNA binding motif protein, Y-linked, family 2, member M pseudogene . . . . . . . . . . . RBMY2NP . . . RNA binding motif protein, Y-linked, family 2, member N pseudogene . . . . . . . . . . . RBMY2OP . . . RNA binding motif protein, Y-linked, family 2, member O pseudogene . . . . . . . . . . . RBMY2QP . . . RNA binding motif protein, Y-linked, family 2, member Q pseudogene . . . . . . . . . . . RBMY2SP . . . RNA binding motif protein, Y-linked, family 2, member S pseudogene . . . . . . . . . . . RBMY2TP . . . RNA binding motif protein, Y-linked, family 2, member T pseudogene . . . . . . . . . . . RBMY2UP . . . RNA binding motif protein, Y-linked, family 2, member U pseudogene . . . . . . . . . . . RBMY2VP . . . RNA binding motif protein, Y-linked, family 2, member V pseudogene . . . . . . . . . . . RBMY2WP . . . RNA binding motif protein, Y-linked, family 2, member W pseudogene . . . . . . . . . . . RBMY2XP . . . RNA binding motif protein, Y-linked, family 2, member X pseudogene . . . . . . . . . . . RBMY2YP . . . RNA binding motif protein, Y-linked, family 2, member Y pseudogene . . . . . . . . . . . RBMY3AP . . . RNA binding motif protein, Y-linked, family 3, member A pseudogene . . . . . . . . . . . RBP1 0.000490535137623092 0.440880812185617 0.55862865267676 retinol binding protein 1 FUNCTION: Intracellular transport of retinol.; . TISSUE SPECIFICITY: Detected in nearly all the tissues with higher expression in adult ovary, pancreas, pituitary gland and adrenal gland, and fetal liver. {ECO:0000269|PubMed:11274389}.; ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;larynx;bone;pituitary gland;testis;amniotic fluid;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;pineal body;oral cavity;pharynx;blood;lens;breast;pancreas;lung;placenta;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland; . 0.20182 0.32213 0.080983847 59.76055674 1333.97386 6.86019 RBP2 0.433554514449151 0.535037959760065 0.0314075257907842 retinol binding protein 2 FUNCTION: Intracellular transport of retinol.; . TISSUE SPECIFICITY: Higher expression in adult small intestine and to a much lesser extent in fetal kidney. {ECO:0000269|PubMed:11274389}.; unclassifiable (Anatomical System);lung;liver;spleen;kidney; . 0.04863 0.12149 -0.163345027 41.24793583 11.96816 0.43400 RBP3 0.0166541508510061 0.978352482275446 0.00499336687354805 retinol binding protein 3 FUNCTION: IRBP shuttles 11-cis and all trans retinoids between the retinol isomerase in the pigment epithelium and the visual pigments in the photoreceptor cells of the retina.; DISEASE: Retinitis pigmentosa 66 (RP66) [MIM:615233]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:19074801}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . optic nerve;pineal body;macula lutea;visual apparatus;colon;fovea centralis;choroid;lens;pineal gland;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.37163 0.25552 -0.957327604 9.017456947 262.94799 3.47929 RBP4 0.57861895575558 0.419065266766176 0.00231577747824379 retinol binding protein 4 FUNCTION: Delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli.; DISEASE: Retinal dystrophy, iris coloboma, and comedogenic acne syndrome (RDCCAS) [MIM:615147]: A disease characterized by retinal degeneration, ocular colobomas involving both the anterior and posterior segment, impaired night vision and loss of visual acuity. Additional characteristic features include developmental abnormalities and severe acne. {ECO:0000269|PubMed:23189188, ECO:0000269|PubMed:9888420}. Note=The disease is caused by mutations affecting the gene represented in this entry. Loss of functional RBP4 protein results in serum retinol deficiency. Lack of normal levels of retinol impairs the visual cycle leading to night blindness at early stages; prolonged deficiency may lead to retinal degeneration. Additionally, retinol deficiency may result in dry skin, increased susceptibility to infection and acne (PubMed:23189188). {ECO:0000269|PubMed:23189188}.; DISEASE: Microphthalmia, isolated, with coloboma, 10 (MCOPCB10) [MIM:616428]: A disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues. Ocular abnormalities like opacities of the cornea and lens, scaring of the retina and choroid, and other abnormalities may also be present. Ocular colobomas are a set of malformations resulting from abnormal morphogenesis of the optic cup and stalk, and the fusion of the fetal fissure (optic fissure). {ECO:0000269|PubMed:25910211}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.51372 . -0.471992905 23.03609342 11.42202 0.41246 RBP5 0.00181920990078845 0.718559024324784 0.279621765774427 retinol binding protein 5 FUNCTION: Intracellular transport of retinol. {ECO:0000269|PubMed:11274389}.; . TISSUE SPECIFICITY: Higher expression in adult kidney and liver and to a lesser extent in adult and fetal spleen, adult lymph nodes and appendix, and fetal liver and kidney. Strongly decreased in hepatocellular carcinoma tissues (at protein level). {ECO:0000269|PubMed:11274389, ECO:0000269|PubMed:17497168}.; unclassifiable (Anatomical System);trophoblast;cartilage;colon;uterus;pancreas;lung;nasopharynx;liver;testis;spleen;kidney;stomach; superior cervical ganglion;lymph node;liver;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.12065 0.11560 1.058333711 91.42486435 4608.64717 13.62417 RBP7 0.408810205691644 0.553992825495652 0.0371969688127033 retinol binding protein 7 FUNCTION: Intracellular transport of retinol. {ECO:0000269|PubMed:12177003}.; . TISSUE SPECIFICITY: Expressed primarily in kidney, heart and transverse colon. Detected in adult lymph node, appendix, ascending colon, and in fetal heart and spleen. {ECO:0000269|PubMed:12177003}.; unclassifiable (Anatomical System);pancreas;lung;spleen;kidney;skeletal muscle;tonsil; . 0.02827 . 0.191216164 66.57230479 13.98489 0.50750 RBPJ 0.999929168569422 7.08314138546287e-05 1.67229369036493e-11 recombination signal binding protein for immunoglobulin kappa J region FUNCTION: Transcriptional regulator that plays a central role in Notch signaling, a signaling pathway involved in cell-cell communication that regulates a broad spectrum of cell-fate determinations. Acts as a transcriptional repressor when it is not associated with Notch proteins. When associated with some NICD product of Notch proteins (Notch intracellular domain), it acts as a transcriptional activator that activates transcription of Notch target genes. Probably represses or activates transcription via the recruitment of chromatin remodeling complexes containing histone deacetylase or histone acetylase proteins, respectively. Specifically binds to the immunoglobulin kappa-type J segment recombination signal sequence. Binds specifically to methylated DNA. Binds to the oxygen responsive element of COX4I2 and activates its transcription under hypoxia conditions (4% oxygen) (PubMed:23303788). {ECO:0000269|PubMed:21991380, ECO:0000269|PubMed:23303788}.; DISEASE: Adams-Oliver syndrome 3 (AOS3) [MIM:614814]: An autosomal dominant form of Adams-Oliver syndrome, a disorder characterized by the congenital absence of skin (aplasia cutis congenita) in combination with transverse limb defects. Aplasia cutis congenita can be located anywhere on the body, but in the vast majority of the cases, it is present on the posterior parietal region where it is often associated with an underlying defect of the parietal bones. Limb abnormalities are typically limb truncation defects affecting the distal phalanges or entire digits (true ectrodactyly). Only rarely, metatarsals/metacarpals or more proximal limb structures are also affected. Apart from transverse limb defects, syndactyly, most commonly of second and third toes, can also be observed. The clinical features are highly variable and can also include cardiovascular malformations, brain abnormalities and vascular defects such as cutis marmorata and dilated scalp veins. AOS3 patients manifest characteristic vertex scalp defects and terminal limb defects, but without congenital heart defects, other associated defects, or immune defects. {ECO:0000269|PubMed:22883147}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;peripheral nerve;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;lung;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; medulla oblongata;superior cervical ganglion;subthalamic nucleus;testis - interstitial;occipital lobe;olfactory bulb;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;cingulate cortex; 0.92815 0.36448 -0.516085732 21.20193442 32.41043 1.01189 RBPJL 1.89367601104857e-11 0.0610269573374025 0.938973042643661 recombination signal binding protein for immunoglobulin kappa J region-like FUNCTION: Putative transcription factor, which cooperates with EBNA2 to activate transcription. {ECO:0000250}.; . . unclassifiable (Anatomical System);pancreas;islets of Langerhans;spleen; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.18921 0.14266 0.99945266 90.6935598 539.89234 4.73495 RBPJP1 . . . RBPJ pseudogene 1 . . . . . . . . . . . RBPJP2 . . . RBPJ pseudogene 2 . . . . . . . . . . . RBPJP3 . . . RBPJ pseudogene 3 . . . . . . . . . . . RBPJP4 . . . RBPJ pseudogene 4 . . . . . . . . . . . RBPJP5 . . . RBPJ pseudogene 5 . . . . . . . . . . . RBPJP6 . . . RBPJ pseudogene 6 . . . . . . . . . . . RBPJP7 . . . RBPJ pseudogene 7 . . . . . . . . . . . RBPMS 0.783171944383471 0.215363772853765 0.00146428276276389 RNA binding protein with multiple splicing FUNCTION: Acts as a coactivator of transcriptional activity. Required to increase TGFB1/Smad-mediated transactivation. Acts through SMAD2, SMAD3 and SMAD4 to increase transcriptional activity. Increases phosphorylation of SMAD2 and SMAD3 on their C- terminal SSXS motif, possibly through recruitment of TGFBR1. Promotes the nuclear accumulation of SMAD2, SMAD3 and SMAD4 proteins. Binds to poly(A) RNA. {ECO:0000269|PubMed:17099224}.; . TISSUE SPECIFICITY: Ubiquitously expressed, at various levels depending on the isoform and the tissue.; smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;pharynx;blood;lens;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis - interstitial;adipose tissue;heart;ovary;atrioventricular node;pons;fetal thyroid;skeletal muscle;uterus;subthalamic nucleus;uterus corpus;prostate;trachea;testis - seminiferous tubule;adrenal gland;thyroid;placenta;liver;testis;globus pallidus;fetal lung;ciliary ganglion;kidney;trigeminal ganglion;parietal lobe; 0.39545 0.18619 0.12689526 63.00424628 38.26492 1.13615 RBPMS-AS1 . . . RBPMS antisense RNA 1 . . . . . . . . . . . RBPMS2 0.323534851132986 0.660314010500989 0.0161511383660255 RNA binding protein with multiple splicing 2 . . . unclassifiable (Anatomical System);myocardium;heart;cartilage;colon;uterus;pancreas;prostate;lung;placenta;bone;visual apparatus;testis;kidney; dorsal root ganglion; 0.76988 0.09913 0.305084559 72.22811984 48.43389 1.35746 RBPMS2P1 . . . RBPMS2 pseudogene 1 . . . . . . . . . . . RBPMSLP . . . RNA binding protein with multiple splicing-like pseudogene . . . . . . . . . . . RBSN . . . rabenosyn, RAB effector FUNCTION: Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3) (PubMed:11062261, PubMed:11788822, PubMed:15020713). Plays a role in the recycling of transferrin receptor to the plasma membrane (PubMed:22308388). {ECO:0000269|PubMed:11062261, ECO:0000269|PubMed:11788822, ECO:0000269|PubMed:15020713, ECO:0000269|PubMed:22308388}.; . . . . 0.22882 0.12517 -0.420619508 25.72540694 . . RBX1 0.940246880165137 0.0595104881666374 0.00024263166822607 ring-box 1, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin ligase component of multiple cullin-RING- based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. In concert with ATF2 and CUL3, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. {ECO:0000269|PubMed:10579999, ECO:0000269|PubMed:11027288, ECO:0000269|PubMed:15983046, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:16751180, ECO:0000269|PubMed:18397884, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:19679664}.; . TISSUE SPECIFICITY: Widely expressed.; ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;frontal lobe;endometrium;bone;testis;dura mater;germinal center;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);meninges;trophoblast;heart;cerebellum cortex;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pia mater;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; pons;parietal lobe;cingulate cortex; 0.80957 0.17367 0.079165051 59.43029016 . . RC3H1 0.999539902744329 0.000460097255649019 2.21618947984746e-14 ring finger and CCCH-type domains 1 FUNCTION: Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF and in many more mRNAs (By similarity). Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs (By similarity). In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity (By similarity). In resting or LPS- stimulated macrophages, controls inflammation by suppressing TNF expression (By similarity). Also recognizes CDE in its own mRNA and in that of paralogous RC3H2, possibly leading to feedback loop regulation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in cerebellum, spleen, ovary and liver. {ECO:0000269|Ref.3}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;ovary;tongue;developmental;colon;blood;lens;skin;skeletal muscle;bone marrow;breast;lung;frontal lobe;placenta;liver;testis;head and neck;spleen;kidney;germinal center;brain;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin;cerebellum; 0.37680 . -0.108334733 45.57088936 258.69631 3.45708 RC3H1-IT1 . . . RC3H1 intronic transcript 1 . . . . . . . . . . . RC3H2 0.999999562144921 4.37855078972274e-07 1.40886206256999e-17 ring finger and CCCH-type domains 2 FUNCTION: Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF and in many more mRNAs. Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs. In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity. In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression. Also recognizes CDE in its own mRNA and in that of paralogous RC3H2, possibly leading to feedback loop regulation (By similarity). May act as a ubiquitin E3 ligase. Involved in the ubiquitination of MAP3K5 (PubMed:24448648). {ECO:0000250|UniProtKB:P0C090, ECO:0000269|PubMed:24448648}.; . TISSUE SPECIFICITY: Expressed in spleen, testis, ovary and small intestine. {ECO:0000269|PubMed:10938276}.; ovary;colon;parathyroid;skin;retina;uterus;prostate;frontal lobe;cerebral cortex;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;skeletal muscle;breast;lung;nasopharynx;placenta;liver;hypopharynx;spleen;head and neck;cervix;stomach;aorta;peripheral nerve; subthalamic nucleus;superior cervical ganglion;prefrontal cortex;atrioventricular node;pons;trigeminal ganglion;pituitary;cingulate cortex;parietal lobe; 0.46539 . -1.330032624 4.688605803 187.34179 2.97315 RCA1 . . . renal carcinoma associated 1 . . . . . . . . . . . RCAN1 0.557669158298526 0.429517478096945 0.0128133636045299 regulator of calcineurin 1 FUNCTION: Inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. Could play a role during central nervous system development.; . TISSUE SPECIFICITY: Highly expressed heart, brain and skeletal muscle. Also expressed in all other tissues.; smooth muscle;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;pituitary gland;testis;dura mater;germinal center;brain;artery;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;lens;breast;pia mater;lung;placenta;alveolus;cervix;kidney;mammary gland;stomach;aorta;cerebellum;thymus; superior cervical ganglion;medulla oblongata;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.16149 0.23419 -0.05129383 49.75819769 16.20147 0.57466 RCAN2 0.430936968293151 0.537085140403774 0.0319778913030755 regulator of calcineurin 2 FUNCTION: Inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. Could play a role during central nervous system development.; . TISSUE SPECIFICITY: Expressed in fibroblasts, heart, brain, liver, and skeletal muscle but not in placenta, lung, kidney and pancreas.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;iris;testis;spinal ganglion;ciliary body;artery;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;lens;skeletal muscle;breast;lung;placenta;macula lutea;hippocampus;visual apparatus;liver;kidney;stomach;aorta; whole brain;amygdala;superior cervical ganglion;thalamus;occipital lobe;medulla oblongata;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.50192 0.12352 0.257356108 69.83368719 30.29372 0.96616 RCAN3 0.00320642195331169 0.823874218371016 0.172919359675673 RCAN family member 3 FUNCTION: Inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. Could play a role during central nervous system development (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highest expression in heart, skeletal muscle kidney, liver and peripheral blood leukocytes. Lower expression in all other tissues.; . . 0.14079 0.09206 -0.139478553 43.29440906 123.07433 2.41603 RCAN3AS . . . RCAN3 antisense . . . . . . . . . . . RCBTB1 0.000217673997703456 0.978800399268245 0.0209819267340518 RCC1 and BTB domain containing protein 1 FUNCTION: May be involved in cell cycle regulation by chromatin remodeling. {ECO:0000269|PubMed:11306461}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11306461}.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;head and neck;kidney;mammary gland;stomach; amygdala;dorsal root ganglion;subthalamic nucleus;thyroid;prefrontal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.22413 0.12033 -0.576764155 18.7839113 37.96124 1.12750 RCBTB2 7.21687231446053e-09 0.441221509374757 0.55877848340837 RCC1 and BTB domain containing protein 2 . . . ovary;salivary gland;developmental;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;thyroid;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;aorta; . 0.16449 0.08898 -0.865195027 10.79853739 41.44076 1.21033 RCBTB2P1 . . . RCC1 and BTB domain containing protein 2 pseudogene 1 . . . . . . . . . . . RCC1 0.19394393095681 0.803829969984209 0.00222609905898098 regulator of chromosome condensation 1 FUNCTION: Guanine-nucleotide releasing factor that promotes the exchange of Ran-bound GDP by GTP. Involved in the regulation of onset of chromosome condensation in the S phase. Binds both to the nucleosomes and double-stranded DNA. RCC1-Ran complex (together with other proteins) acts as a component of a signal transmission pathway that detects unreplicated DNA. Plays a key role in nucleo- cytoplasmic transport, mitosis and nuclear-envelope assembly. {ECO:0000269|PubMed:1944575}.; . . . . . 0.37148 -0.558357437 19.54470394 44.69525 1.28193 RCC2 0.787633127226415 0.212355245582008 1.1627191577202e-05 regulator of chromosome condensation 2 FUNCTION: Required for completion of mitosis and cytokinesis. May function as a guanine nucleotide exchange factor for the small GTPase RAC1. {ECO:0000269|PubMed:12919680}.; . . . . 0.50342 . -0.670411825 15.61689078 160.69226 2.76762 RCC2P1 . . . regulator of chromosome condensation 2 pseudogene 1 . . . . . . . . . . . RCC2P2 . . . regulator of chromosome condensation 2 pseudogene 2 . . . . . . . . . . . RCC2P3 . . . regulator of chromosome condensation 2 pseudogene 3 . . . . . . . . . . . RCC2P4 . . . regulator of chromosome condensation 2 pseudogene 4 . . . . . . . . . . . RCC2P5 . . . regulator of chromosome condensation 2 pseudogene 5 . . . . . . . . . . . RCC2P6 . . . regulator of chromosome condensation 2 pseudogene 6 . . . . . . . . . . . RCC2P7 . . . regulator of chromosome condensation 2 pseudogene 7 . . . . . . . . . . . RCC2P8 . . . regulator of chromosome condensation 2 pseudogene 8 . . . . . . . . . . . RCCD1 1.62554312815351e-05 0.662984416717945 0.336999327850774 RCC1 domain containing 1 . . . . . 0.03250 0.09502 . . 642.93986 5.09354 RCD1 . . . retinal cone dystrophy 1 . . . . . . . . . . . RCE1 0.559303286832047 0.43798906869048 0.00270764447747236 Ras converting CAAX endopeptidase 1 FUNCTION: Proteolytically removes the C-terminal three residues of farnesylated and geranylated proteins. Seems to be able to process K-Ras, N-Ras, H-Ras, RAP1B and G-gamma-1 (PubMed:10085068). {ECO:0000269|PubMed:10085068, ECO:0000269|PubMed:11038283, ECO:0000269|PubMed:19188362}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10085068}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;blood;lens;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;globus pallidus;pons;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.41891 0.14036 -0.405853867 26.23260203 237.7423 3.32952 RCHY1 0.823377800911552 0.176452495904166 0.000169703184281505 ring finger and CHY zinc finger domain containing 1 FUNCTION: Mediates E3-dependent ubiquitination and proteasomal degradation of target proteins, including p53/TP53, P73, HDAC1 and CDKN1B. Preferentially acts on tetrameric p53/TP53. Monoubiquitinates the translesion DNA polymerase POLH. Contributes to the regulation of the cell cycle progression. Increases AR transcription factor activity. {ECO:0000269|PubMed:16914734, ECO:0000269|PubMed:17721809, ECO:0000269|PubMed:18006823, ECO:0000269|PubMed:19043414, ECO:0000269|PubMed:19483087, ECO:0000269|PubMed:21791603, ECO:0000269|PubMed:21994467}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;pharynx;blood;lens;skeletal muscle;bile duct;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach;aorta;peripheral nerve;cerebellum; amygdala;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;trigeminal ganglion;skeletal muscle;cerebellum; 0.34901 0.19444 -0.295622497 32.61972163 11.59795 0.41955 RCL1 0.948080583071813 0.0519123788084141 7.03811977274707e-06 RNA terminal phosphate cyclase-like 1 FUNCTION: Does not have cyclase activity. Plays a role in 40S- ribosomal-subunit biogenesis in the early pre-rRNA processing steps at sites A0, A1 and A2 that are required for proper maturation of the 18S RNA (By similarity). {ECO:0000250}.; . . . . 0.51781 0.11461 0.396906589 76.30927105 198.5706 3.04508 RCN1 0.0163385637096446 0.885373262165658 0.098288174124697 reticulocalbin 1 FUNCTION: May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment.; . . medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;pia mater;lung;mesenchyma;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; . 0.17487 0.16720 0.415317661 76.81056853 75.39205 1.81712 RCN1P1 . . . reticulocalbin 1 pseudogene 1 . . . . . . . . . . . RCN1P2 . . . reticulocalbin 1 pseudogene 2 . . . . . . . . . . . RCN2 0.449457626519201 0.544251327396903 0.00629104608389637 reticulocalbin 2 FUNCTION: Not known. Binds calcium.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;bladder;brain;gall bladder;amygdala;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;placenta;hippocampus;head and neck;kidney;stomach; whole brain;amygdala;testis - interstitial;occipital lobe;testis - seminiferous tubule;hypothalamus;placenta;prefrontal cortex;globus pallidus;testis; 0.52998 0.12576 -0.141298762 42.87567823 34.49672 1.05358 RCN3 1.77726445447237e-09 0.0338003731758572 0.966199625046878 reticulocalbin 3 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;hypothalamus;lens;breast;lung;epididymis;placenta;macula lutea;visual apparatus;hypopharynx;spleen;head and neck;mammary gland;stomach; superior cervical ganglion;adipose tissue;smooth muscle;heart;trigeminal ganglion; 0.18175 . 0.863528995 88.74144845 1267.2461 6.70876 RCOR1 0.994042794940819 0.00595703849564759 1.66563533441062e-07 REST corepressor 1 FUNCTION: Essential component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it serves as a molecular beacon for the recruitment of molecular machinery, including MeCP2 and SUV39H1, that imposes silencing across a chromosomal interval. Plays a central role in demethylation of Lys-4 of histone H3 by promoting demethylase activity of KDM1A on core histones and nucleosomal substrates. It also protects KDM1A from the proteasome. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation. {ECO:0000269|PubMed:11171972, ECO:0000269|PubMed:11516394, ECO:0000269|PubMed:12032298, ECO:0000269|PubMed:12399542, ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:16079794, ECO:0000269|PubMed:16140033}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10449787}.; unclassifiable (Anatomical System);lymphoreticular;ovary;colon;blood;skin;bone marrow;breast;lung;bone;testis;germinal center;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;placenta;testis;trigeminal ganglion; 0.15896 0.16064 -0.251530012 35.42108988 30.15903 0.96200 RCOR2 0.115753696587521 0.883058054980653 0.00118824843182577 REST corepressor 2 FUNCTION: May act as a component of a corepressor complex that represses transcription. {ECO:0000305}.; . . unclassifiable (Anatomical System);ovary;colon;fovea centralis;choroid;lens;retina;optic nerve;whole body;frontal lobe;visual apparatus;macula lutea;mammary gland;brain;stomach; dorsal root ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.15407 0.11192 -0.514264485 21.41424864 38.78816 1.14828 RCOR3 0.672007745805069 0.327784476432618 0.00020777776231328 REST corepressor 3 FUNCTION: May act as a component of a corepressor complex that represses transcription. {ECO:0000305}.; . . . . 0.60500 0.10748 -0.405853867 26.23260203 15.27523 0.54964 RCSD1 0.108221839863747 0.885270602551433 0.00650755758481976 RCSD domain containing 1 FUNCTION: Stress-induced phosphorylation of CAPZIP may regulate the ability of F-actin-capping protein to remodel actin filament assembly. {ECO:0000269|PubMed:15850461}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle and more weakly in cardiac muscle. Also expressed in several lymphoid organs, including spleen, thymus, peripheral blood leukocytes, lymph node and bone marrow. {ECO:0000269|PubMed:15850461}.; smooth muscle;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;tongue;blood;lens;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion;whole blood;bone marrow;thymus; 0.31501 0.09640 0.001895464 54.03397028 64.91396 1.65550 RCVRN 2.96020215900158e-07 0.0938397172862697 0.906159986693514 recoverin FUNCTION: Seems to be implicated in the pathway from retinal rod guanylate cyclase to rhodopsin. May be involved in the inhibition of the phosphorylation of rhodopsin in a calcium-dependent manner. The calcium-bound recoverin prolongs the photoresponse.; . . unclassifiable (Anatomical System);ovary;pineal body;blood;choroid;fovea centralis;skeletal muscle;retina;lung;optic nerve;visual apparatus;macula lutea;spinal ganglion;pineal gland; superior cervical ganglion;uterus corpus;subthalamic nucleus;atrioventricular node;skeletal muscle; 0.16262 0.32133 0.3032669 72.009908 75.32498 1.81611 RD3 0.0975162265688966 0.770761404233961 0.131722369197142 retinal degeneration 3 . . TISSUE SPECIFICITY: Preferentially expressed in retina. {ECO:0000269|PubMed:12914764}.; . . 0.24953 . 1.128108522 92.19155461 286.75487 3.62724 RD3L . . . retinal degeneration 3-like . . . . . . . . . 666.70282 5.16734 RDH5 3.1134515694943e-06 0.545351738894043 0.454645147654388 retinol dehydrogenase 5 FUNCTION: Stereospecific 11-cis retinol dehydrogenase, which catalyzes the final step in the biosynthesis of 11-cis retinaldehyde, the universal chromophore of visual pigments. Also able to oxidize 9-cis-retinol and 13-cis-retinol, but not all- trans-retinol. Active in the presence of NAD as cofactor but not in the presence of NADP. {ECO:0000269|PubMed:10588954, ECO:0000269|PubMed:9115228}.; . TISSUE SPECIFICITY: Abundant in the retinal pigment epithelium. Expressed at high levels in mammary tissue, kidney and testis, and at lower levels in liver, heart, adrenal gland, lung, pancreas and skeletal muscle. {ECO:0000269|PubMed:9115228}.; unclassifiable (Anatomical System);cartilage;heart;colon;blood;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;optic nerve;lung;frontal lobe;thyroid;bone;macula lutea;visual apparatus;liver;testis;spleen;kidney;brain;stomach; adipose tissue;liver;skeletal muscle; 0.40981 0.21807 0.084621747 60.31493277 152.66364 2.70259 RDH8 3.72790127743868e-05 0.6012803137558 0.398682407231426 retinol dehydrogenase 8 (all-trans) FUNCTION: Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinal to all-trans-retinol. May play a role in the regeneration of visual pigment at high light intensity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in photoreceptor outer segments in the retina (at protein level). {ECO:0000269|PubMed:10753906}.; visual apparatus;skeletal muscle;retina; superior cervical ganglion;skeletal muscle; 0.34140 0.13575 0.687150476 85.17928757 2128.1685 8.49472 RDH10 0.934320138948288 0.0653720607048301 0.000307800346882246 retinol dehydrogenase 10 (all-trans) FUNCTION: Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinol to all-trans-retinal. Has no detectable activity towards 11-cis-retinol, 9-cis-retinol and 13-cis-retinol. {ECO:0000269|PubMed:12407145}.; . TISSUE SPECIFICITY: Detected in retina, kidney, liver, small intestine, placenta, lung, heart and skeletal muscle. {ECO:0000269|PubMed:12407145, ECO:0000269|PubMed:14596915}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;spinal cord;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;duodenum;kidney;stomach; testis - interstitial;trachea;testis;ciliary ganglion;trigeminal ganglion; 0.29445 0.14229 0.389637587 75.75489502 28.58653 0.91542 RDH10-AS1 . . . RDH10 antisense RNA 1 . . . . . . . . . . . RDH11 0.00966533141048819 0.941274818256231 0.049059850333281 retinol dehydrogenase 11 (all-trans/9-cis/11-cis) FUNCTION: Exhibits an oxidoreductive catalytic activity towards retinoids. Most efficient as an NADPH-dependent retinal reductase. Displays high activity towards 9-cis and all-trans-retinol. Also involved in the metabolism of short-chain aldehydes. No steroid dehydrogenase activity detected.; DISEASE: Retinal dystrophy, juvenile cataracts, and short stature syndrome (RDJCSS) [MIM:616108]: A disorder characterized by retinal dystrophy resulting in progressive decrease in visual acuity and difficulties with night vision in the first decade of life, development of juvenile cataracts, facial dysmorphism, psychomotor developmental delays, learning disabilities and short stature. Ophthalmological findings include salt-and-pepper retinopathy, attenuation of the arterioles, generalized rod-cone dysfunction, mottled macula at an early age, and peripapillary sparing of the retinal pigment epithelium. {ECO:0000269|PubMed:24916380}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in the epithelial cells of prostate, in both basal and luminal secretory cell populations. Expressed at low levels in spleen, thymus, testis, ovary, small intestine, colon, peripherical blood leukocytes, kidney, adrenal gland and fetal liver. Not detected in prostatic fibromuscular stromal cells, endothelial cells, or infiltrating lymphocytes.; . . 0.33489 . 0.082802743 60.09082331 126.64573 2.45298 RDH12 4.71469945442482e-06 0.635828800188586 0.364166485111959 retinol dehydrogenase 12 (all-trans/9-cis/11-cis) FUNCTION: Exhibits an oxidoreductive catalytic activity towards retinoids. Most efficient as an NADPH-dependent retinal reductase. Displays high activity toward 9-cis and all-trans-retinol. Also involved in the metabolism of short-chain aldehydes. No steroid dehydrogenase activity detected. Might be the key enzyme in the formation of 11-cis-retinal from 11-cis-retinol during regeneration of the cone visual pigments. {ECO:0000269|PubMed:12226107}.; DISEASE: Retinitis pigmentosa 53 (RP53) [MIM:612712]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:19140180, ECO:0000269|PubMed:19956407}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, mostly in eye, kidney, brain, skeletal muscle and stomach.; unclassifiable (Anatomical System);optic nerve;macula lutea;liver;fovea centralis;choroid;kidney;lens;brain;skin;skeletal muscle;stomach;retina; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.31938 0.18182 -0.646543901 16.44255721 671.60152 5.17904 RDH13 5.35333781778222e-12 0.00798254573034287 0.992017454264304 retinol dehydrogenase 13 (all-trans/9-cis) FUNCTION: Does not exhibit retinol dehydrogenase (RDH) activity in vitro.; . TISSUE SPECIFICITY: Expressed mostly in eye, pancreas, placenta and lung. In the retina, detected in the inner segment of the photoreceptor cells. Weak signals were observed in a small population of inner nuclear neurons and the inner plexiform layer. {ECO:0000269|PubMed:12226107}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;muscle;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;kidney;mammary gland;stomach;thymus; . 0.20628 . -0.044015879 50.44821892 924.21716 5.90448 RDH14 0.232943493348579 0.645848769245518 0.121207737405903 retinol dehydrogenase 14 (all-trans/9-cis/11-cis) FUNCTION: Exhibits an oxidoreductive catalytic activity towards retinoids. Most efficient as an NADPH-dependent retinal reductase. Displays high activity toward 9-cis and all-trans-retinol. No steroid dehydrogenase activity detected. {ECO:0000269|PubMed:12226107}.; . . . . 0.73763 0.15553 -0.617221851 17.44515216 165.64634 2.81576 RDH16 8.59884923667545e-05 0.541042054195573 0.45887195731206 retinol dehydrogenase 16 (all-trans) FUNCTION: Oxidoreductase with a preference for NAD. Oxidizes all- trans-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol. Oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction. {ECO:0000269|PubMed:10329026, ECO:0000269|PubMed:12534290, ECO:0000269|PubMed:9677409}.; . TISSUE SPECIFICITY: Highly expressed in adult liver (at protein level). Detected in endometrium, liver and foreskin. Detected in the spineous layers of adult skin, and at lower levels in basal and granular skin layers. Detected in fetal liver and lung. {ECO:0000269|PubMed:10329026, ECO:0000269|PubMed:11967490, ECO:0000269|PubMed:9677409}.; . . 0.14185 . -0.358119787 29.16371786 130.002 2.48395 RDM1 0.00503096531248961 0.886663749413041 0.108305285274469 RAD52 motif containing 1 FUNCTION: May confer resistance to the antitumor agent cisplatin. Binds to DNA and RNA. {ECO:0000269|PubMed:15611051}.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:15611051}.; unclassifiable (Anatomical System);medulla oblongata;trophoblast;whole body;endometrium;placenta;testis;colon;germinal center;mammary gland;skin;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;trigeminal ganglion; 0.07347 0.08817 0.062575634 58.74026893 2784.65952 9.96858 RDX 0.998954589256721 0.00104541026051449 4.82764589373757e-10 radixin FUNCTION: Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.; DISEASE: Deafness, autosomal recessive, 24 (DFNB24) [MIM:611022]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:17226784}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;artery;unclassifiable (Anatomical System);trophoblast;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;lung;placenta;internal ear;hippocampus;head and neck;kidney;aorta;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.50562 0.26811 -0.558357437 19.54470394 63.11771 1.62538 RDXP1 . . . radixin pseudogene 1 . . . . . . . . . . . RDXP2 . . . radixin pseudogene 2 . . . . . . . . . . . REC8 0.526977585048225 0.473016451896153 5.96305562186395e-06 REC8 meiotic recombination protein FUNCTION: Required during meiosis for separation of sister chromatids and homologous chromosomes. Proteolytic cleavage of REC8 on chromosome arms by separin during anaphase I allows for homologous chromosome separation in meiosis I and cleavage of REC8 on centromeres during anaphase II allows for sister chromatid separation in meiosis II (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis and thymus. Expressed in the B-cell lines WI-L2-NS and Namalwa (at protein level). {ECO:0000269|PubMed:10207075}.; medulla oblongata;smooth muscle;ovary;umbilical cord;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;oesophagus;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;thymus; superior cervical ganglion;testis - interstitial; 0.08130 0.09210 -0.312207497 32.05944798 56.77631 1.51666 REC114 . . . REC114 meiotic recombination protein FUNCTION: May play a role in meiotic DNA double-strand break formation. {ECO:0000250}.; . . . . . 0.08390 -0.005381972 53.50908233 . . RECK 0.000196797881487026 0.999760397167875 4.28049506374343e-05 reversion inducing cysteine rich protein with kazal motifs FUNCTION: Negatively regulates matrix metalloproteinase-9 (MMP-9) by suppressing MMP-9 secretion and by direct inhibition of its enzymatic activity. RECK down-regulation by oncogenic signals may facilitate tumor invasion and metastasis. Appears to also regulate MMP-2 and MT1-MMP, which are involved in cancer progression.; . TISSUE SPECIFICITY: Expressed in various tissues and untransformed cells. It is undetectable in tumor-derived cell lines and oncogenically transformed cells.; . . 0.37337 0.19959 -0.951568548 9.271054494 1398.34528 6.99259 RECQL 7.14017324493182e-13 0.063180525191969 0.936819474807317 RecQ like helicase FUNCTION: DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction. {ECO:0000269|PubMed:15886194, ECO:0000269|PubMed:7961977, ECO:0000269|PubMed:8056767}.; . TISSUE SPECIFICITY: High expression in heart, lung, skeletal muscle and kidney, low expression in brain. {ECO:0000269|PubMed:7961977}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;atrium;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;blood;skeletal muscle;bile duct;pancreas;lung;placenta;liver;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.96604 0.29029 -0.973616687 8.8995046 602.74519 4.96976 RECQL4 . . . RecQ like helicase 4 FUNCTION: DNA-dependent ATPase. May modulate chromosome segregation. {ECO:0000269|PubMed:15317757}.; DISEASE: Rothmund-Thomson syndrome (RTS) [MIM:268400]: Characterized by dermatological features such as atrophy, pigmentation, and telangiectasia and frequently accompanied by juvenile cataract, saddle nose, congenital bone defects, disturbances of hair growth, and hypogonadism. {ECO:0000269|PubMed:10552928}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: RAPADILINO syndrome (RAPADILINOS) [MIM:266280]: Disease characterized by radial and patellar aplasia or hypoplasia. {ECO:0000269|PubMed:12952869}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Baller-Gerold syndrome (BGS) [MIM:218600]: An autosomal recessive syndrome characterized by short stature, craniosynostosis, absent or hypoplastic radii, short and curved ulna, fused carpal bones and absent carpals, metacarpals and phalanges. Some patients manifest poikiloderma. Cases reported as Baller-Gerold syndrome have phenotypic overlap with several other disorders, including Saethre-Chotzen syndrome. {ECO:0000269|PubMed:15964893}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in thymus and testis. {ECO:0000269|PubMed:9878247}.; unclassifiable (Anatomical System);ovary;muscle;colon;skin;uterus;lung;endometrium;visual apparatus;testis;spleen;germinal center;brain;stomach; skeletal muscle; 0.06646 0.17226 . . 7865.46795 19.16576 RECQL5 3.00939600505428e-07 0.996122246447281 0.00387745261311825 RecQ like helicase 5 FUNCTION: Isoform beta is a DNA helicase that plays an important role in DNA replication, transcription and repair. Inhibits elongation of stalled transcripts at DNA damage sites by binding to the RNA polymerase II subunit POLR2A and blocking the TCEA1 binding site. Required for mitotic chromosome separation after cross-over events and cell cycle progress. Required for efficient DNA repair, including repair of inter-strand cross-links. Stimulates DNA decatenation mediated by TOP2A. Prevents sister chromatid exchange and homologous recombination. {ECO:0000269|PubMed:20231364, ECO:0000269|PubMed:20348101, ECO:0000269|PubMed:20643585, ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:22973052, ECO:0000269|PubMed:23715498, ECO:0000269|PubMed:23748380}.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland;cerebellum;thymus; dorsal root ganglion;superior cervical ganglion;placenta;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14432 0.22579 0.145092325 63.67657466 2799.73965 9.98847 REEP1 0.938706616254476 0.0610347270423685 0.000258656703154883 receptor accessory protein 1 FUNCTION: Required for endoplasmic reticulum (ER) network formation, shaping and remodeling; it links ER tubules to the cytoskeleton. May also enhance the cell surface expression of odorant receptors (PubMed:20200447). May play a role in long-term axonal maintenance (PubMed:24478229). {ECO:0000269|PubMed:20200447, ECO:0000269|PubMed:24478229}.; DISEASE: Neuronopathy, distal hereditary motor, 5B (HMN5B) [MIM:614751]: A disorder characterized by distal muscular atrophy mainly affecting the upper extremities, in contrast to other distal motor neuronopathies. These constitute a heterogeneous group of neuromuscular diseases caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. HMN5B is characterized by onset in the first or second decade of distal muscle weakness and atrophy, primarily affecting the intrinsic hand muscles, but also affecting the lower legs, resulting in abnormal gait and pes cavus. {ECO:0000269|PubMed:22703882}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in circumvallate papillae and testis. {ECO:0000269|PubMed:16720576}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;larynx;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;head and neck;kidney; dorsal root ganglion;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;pons;caudate nucleus;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;pituitary;amygdala;testis - interstitial;hypothalamus;temporal lobe;atrioventricular node;skeletal muscle;fetal brain;prefrontal cortex;parietal lobe; 0.44204 0.11211 0.170987912 65.5579146 12.43022 0.45097 REEP2 0.876388829269941 0.123290956363917 0.000320214366141685 receptor accessory protein 2 FUNCTION: Required for endoplasmic reticulum (ER) network formation, shaping and remodeling. May enhance the cell surface expression of odorant receptors (By similarity). {ECO:0000250, ECO:0000269|PubMed:24388663}.; . TISSUE SPECIFICITY: Detected in brain, heart and skeletal muscle, and at low levels in placenta, kidney and pancreas (PubMed:11161817). Expressed in circumvallate papillae (PubMed:16720576). {ECO:0000269|PubMed:11161817, ECO:0000269|PubMed:16720576}.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;whole body;bone;macula lutea;visual apparatus;brain;stomach; whole brain;amygdala;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.35140 0.10539 -0.073340031 48.11866006 18.82305 0.65008 REEP3 0.0129812993547476 0.953842585133132 0.0331761155121202 receptor accessory protein 3 FUNCTION: Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering the endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes. {ECO:0000269|PubMed:23911198}.; . TISSUE SPECIFICITY: Expressed in circumvallate papillae. {ECO:0000269|PubMed:16720576}.; medulla oblongata;ovary;salivary gland;intestine;colon;skin;uterus;prostate;bone;testis;bladder;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;kidney;stomach; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; 0.15078 0.09193 0.148941568 64.31941496 42.88893 1.24155 REEP4 0.175027611415095 0.811909842729548 0.0130625458553569 receptor accessory protein 4 FUNCTION: Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering the endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes. {ECO:0000269|PubMed:23911198}.; . TISSUE SPECIFICITY: Expressed in circumvallate papillae and testis. {ECO:0000269|PubMed:16720576}.; medulla oblongata;ovary;salivary gland;colon;skin;bone marrow;uterus;prostate;optic nerve;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;small intestine;heart;tongue;islets of Langerhans;blood;skeletal muscle;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis;skeletal muscle; 0.20116 0.10008 0.018483465 55.44939844 188.41583 2.98197 REEP5 0.0628875963888091 0.869920163784811 0.0671922398263796 receptor accessory protein 5 FUNCTION: May promote functional cell surface expression of olfactory receptors.; . TISSUE SPECIFICITY: Expressed in circumvallate papillae and testis. {ECO:0000269|PubMed:16720576}.; myocardium;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;placenta;kidney;stomach;aorta;cerebellum; dorsal root ganglion;amygdala;occipital lobe;medulla oblongata;thalamus;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;thyroid;placenta;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.28221 0.11262 -0.095386216 46.48502005 99.58363 2.16033 REEP6 0.000463081508958989 0.665179660155568 0.334357258335473 receptor accessory protein 6 FUNCTION: May play a role in intracellular protein transport from the endoplasmic reticulum to the cell surface. May play a role in retinal development (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in circumvallate papillae and testis. {ECO:0000269|PubMed:16720576}.; unclassifiable (Anatomical System);medulla oblongata;ovary;colon;retina;bone marrow;uterus;pancreas;prostate;optic nerve;lung;bone;placenta;visual apparatus;hippocampus;liver;testis;spleen;kidney;spinal ganglion;brain;mammary gland;stomach; prostate;superior cervical ganglion;testis - interstitial;fetal liver;testis - seminiferous tubule;adrenal gland;adrenal cortex;liver;testis;kidney;trigeminal ganglion; 0.06456 0.03846 -0.427900189 25.14744043 125.42377 2.43777 REG1A 0.00852762762703895 0.797600205456041 0.19387216691692 regenerating family member 1 alpha FUNCTION: Might act as an inhibitor of spontaneous calcium carbonate precipitation. May be associated with neuronal sprouting in brain, and with brain and pancreas regeneration.; . TISSUE SPECIFICITY: In pancreatic acinar cells and, in lower levels, in brain. Enhanced expression of PSP-related transcripts and intraneuronal accumulation of PSP-like proteins is found in brain from Alzheimer disease and Down syndrome patients. {ECO:0000269|PubMed:2394826}.; unclassifiable (Anatomical System);prostate;pancreas;ovary;small intestine;islets of Langerhans;colon;kidney;stomach; pancreas;beta cell islets; . 0.21173 -0.163345027 41.24793583 6.00345 0.22559 REG1B 0.00195416709048902 0.733105349571956 0.264940483337555 regenerating family member 1 beta FUNCTION: Might act as an inhibitor of spontaneous calcium carbonate precipitation. May be associated with neuronal sprouting in brain, and with brain and pancreas regeneration.; . . unclassifiable (Anatomical System);pancreas;lung;islets of Langerhans;testis;colon;spleen;stomach; pancreas;superior cervical ganglion;beta cell islets;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.10180 0.11840 0.393270925 76.04977589 118.46214 2.36826 REG1CP . . . regenerating family member 1 gamma, pseudogene . . . . . . 0.21173 . . . . REG3A 0.00142860711460032 0.667709016640866 0.330862376244533 regenerating family member 3 alpha FUNCTION: Bactericidal C-type lectin which acts exclusively against Gram-positive bacteria and mediates bacterial killing by binding to surface-exposed carbohydrate moieties of peptidoglycan. Regulates keratinocyte proliferation and differentiation after skin injury via activation of EXTL3-PI3K-AKT signaling pathway. {ECO:0000269|PubMed:16931762}.; . TISSUE SPECIFICITY: Highly expressed in epidermal keratinocytes of psoriasis patients (at protein level). Constitutively expressed in intestine. Low expression is found in healthy pancreas. Overexpressed during the acute phase of pancreatitis and in some patients with chronic pancreatitis. {ECO:0000269|PubMed:1469087, ECO:0000269|PubMed:22727489}.; unclassifiable (Anatomical System);pancreas;small intestine;islets of Langerhans;colon;spleen;stomach; superior cervical ganglion;pancreas;beta cell islets;trigeminal ganglion; 0.19485 0.12276 -0.073340031 48.11866006 12.35762 0.44826 REG3G 2.17515516666175e-05 0.288158993815648 0.711819254632685 regenerating family member 3 gamma FUNCTION: Bactericidal C-type lectin which acts exclusively against Gram-positive bacteria and mediates bacterial killing by binding to surface-exposed carbohydrate moieties of peptidoglycan. Restricts bacterial colonization of the intestinal epithelial surface and consequently limits activation of adaptive immune responses by the microbiota. The uncleaved form has bacteriostatic activity, whereas the cleaved form has bactericidal activity against L.monocytogenes and methicillin-resistant S.aureus. Regulates keratinocyte proliferation and differentiation after skin injury. {ECO:0000269|PubMed:19095652}.; . TISSUE SPECIFICITY: Predominantly expressed in pancreas, where it may be restricted to exocrine pancreas. Moderate expression levels in testis and weak in heart, kidney and placenta. {ECO:0000269|PubMed:15556304, ECO:0000269|PubMed:15777617}.; unclassifiable (Anatomical System);pancreas;islets of Langerhans;testis;colon; beta cell islets; 0.07577 0.09128 0.549415813 81.38122199 461.00787 4.45235 REG4 5.62414830360332e-05 0.452805170209753 0.547138588307211 regenerating family member 4 FUNCTION: Calcium-independent lectin displaying mannose-binding specificity and able to maintain carbohydrate recognition activity in an acidic environment. May be involved in inflammatory and metaplastic responses of the gastrointestinal epithelium. {ECO:0000269|PubMed:12819006, ECO:0000269|PubMed:20692269}.; . TISSUE SPECIFICITY: Highly expressed in the gastrointestinal tract including the duodenum, jejunum, ileum, ileocecum, appendix, descending colon, pancreas and small intestine. Weakly expressed in normal colon and stomach. Strongly expressed in most colorectal tumors than in normal colon. Preferentially expressed in mucinous tumors and in some cases neuro-endocrine tumors. Expressed in mucus-secreting cells and enterocyte-like cells. In small intestine expressed at the basal perinuclear zone of goblet cells. {ECO:0000269|PubMed:11311942, ECO:0000269|PubMed:12455032, ECO:0000269|PubMed:12819006}.; unclassifiable (Anatomical System);breast;prostate;pancreas;lung;ovary;testis;colon;stomach; pancreas; 0.08299 . 0.883760026 89.07171503 14.70508 0.53027 REL 0.969516332676901 0.0304818040454348 1.8632776644159e-06 v-rel avian reticuloendotheliosis viral oncogene homolog FUNCTION: Proto-oncogene that may play a role in differentiation and lymphopoiesis. NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF- kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF- kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The NF-kappa-B heterodimer RELA/p65-c-Rel is a transcriptional activator.; . . unclassifiable (Anatomical System);ovary;colon;parathyroid;blood;bone marrow;breast;pancreas;lung;larynx;placenta;testis;head and neck;germinal center;kidney;brain; superior cervical ganglion; 0.85286 0.36170 -0.690637458 15.12149092 77.12377 1.84420 RELA 0.998828467638028 0.00117151679830584 1.55636660772339e-08 v-rel avian reticuloendotheliosis viral oncogene homolog A FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells (PubMed:15790681). {ECO:0000269|PubMed:10928981, ECO:0000269|PubMed:12748188, ECO:0000269|PubMed:15790681, ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:17620405, ECO:0000269|PubMed:19058135, ECO:0000269|PubMed:19103749, ECO:0000269|PubMed:20547752}.; DISEASE: Note=A chromosomal aberration involving C11orf95 is found in more than two-thirds of supratentorial ependymomas. Translocation with C11orf95 produces a C11orf95-RELA fusion protein. C11orf95-RELA translocations are potent oncogenes that probably transform neural stem cells by driving an aberrant NF- kappa-B transcription program (PubMed:24553141). {ECO:0000269|PubMed:24553141}.; . ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;muscle;urinary;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle;cerebellum; 0.99684 0.75429 -0.690637458 15.12149092 33.48367 1.03296 RELB 0.973562746007932 0.0264307864864085 6.46750565966656e-06 v-rel avian reticuloendotheliosis viral oncogene homolog B FUNCTION: NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF- kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF- kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric RelB-p50 and RelB-p52 complexes are transcriptional activators. RELB neither associates with DNA nor with RELA/p65 or REL. Stimulates promoter activity in the presence of NFKB2/p49. As a member of the NUPR1/RELB/IER3 survival pathway, may provide pancreatic ductal adenocarcinoma with remarkable resistance to cell stress, such as starvation or gemcitabine treatment. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer in a CRY1/CRY2 independent manner. Increased repression of the heterodimer is seen in the presence of NFKB2/p52. {ECO:0000269|PubMed:1732739, ECO:0000269|PubMed:22565310, ECO:0000269|PubMed:7925301, ECO:0000269|PubMed:8441398}.; . . unclassifiable (Anatomical System);cartilage;ovary;colon;blood;fovea centralis;choroid;lens;retina;bone marrow;uterus;pancreas;prostate;optic nerve;lung;larynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;germinal center;kidney;brain; atrioventricular node; 0.65798 0.48682 -1.001120478 8.321538099 16.82547 0.59142 RELL1 0.883550395447861 0.115125906908446 0.00132369764369262 RELT like 1 . . TISSUE SPECIFICITY: Widely expressed. Expressed at highest levels in the placenta, skeletal muscle, spleen and testis. {ECO:0000269|PubMed:16389068}.; unclassifiable (Anatomical System);pancreas;lung;endometrium;placenta;liver;testis;colon;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06403 0.10656 0.371224249 75.12384996 182.18905 2.93152 RELL2 0.800132420991145 0.198700566917202 0.0011670120916531 RELT like 2 . . TISSUE SPECIFICITY: Primarily expressed in spleen, thymus, testis, peripheral blood leukocytes, brain and placenta. Not detected in prostate, ovary, small intestine, colon, heart, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:16389068}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;tongue;islets of Langerhans;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; . 0.09419 0.08720 0.196671391 67.19155461 3792.11049 12.08180 RELN 0.999999999999998 2.43713313930997e-15 3.09861954987044e-43 reelin FUNCTION: Extracellular matrix serine protease that plays a role in layering of neurons in the cerebral cortex and cerebellum. Regulates microtubule function in neurons and neuronal migration. Affects migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration. Enzymatic activity is important for the modulation of cell adhesion. Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of TAU phosphorylation (By similarity). {ECO:0000250}.; DISEASE: Lissencephaly 2 (LIS2) [MIM:257320]: A classic type lissencephaly associated with ataxia, mental retardation, seizures and abnormalities of the cerebellum, hippocampus and brainstem. {ECO:0000269|PubMed:10973257}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epilepsy, familial temporal lobe, 7 (ETL7) [MIM:616436]: A focal form of epilepsy characterized by recurrent seizures that arise from foci within the temporal lobe. Seizures are usually accompanied by sensory symptoms, most often auditory in nature. {ECO:0000269|PubMed:26046367}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Abundantly produced during brain ontogenesis by the Cajal-Retzius cells and other pioneer neurons located in the telencephalic marginal zone and by granule cells of the external granular layer of the cerebellum. In adult brain, preferentially expressed in GABAergic interneurons of prefrontal cortices, temporal cortex, hippocampus and glutamatergic granule cells of cerebellum. Expression is reduced to about 50% in patients with schizophrenia. Also expressed in fetal and adult liver. {ECO:0000269|PubMed:9861036}.; unclassifiable (Anatomical System);amygdala;heart;cartilage;colon;fovea centralis;skin;skeletal muscle;retina;uterus;breast;prostate;lung;cochlea;endometrium;macula lutea;visual apparatus;hippocampus;liver;testis;spleen;spinal ganglion;brain; dorsal root ganglion;amygdala;fetal liver;superior cervical ganglion;olfactory bulb;cerebellum peduncles;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.25073 . -2.151227095 1.462609106 2605.03558 9.54865 RELT 1.50780432907826e-05 0.857734961773748 0.142249960182961 RELT tumor necrosis factor receptor FUNCTION: Mediates activation of NF-kappa-B. May play a role in T- cell activation.; . TISSUE SPECIFICITY: Highest levels are in spleen, lymph node, thymus, peripheral blood leukocytes, bone marrow and fetal liver. Very low levels in skeletal muscle, testis and colon. Not detected in brain, kidney and pancreas. {ECO:0000269|PubMed:16389068}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;blood;choroid;skin;bone marrow;optic nerve;lung;endometrium;bone;visual apparatus;hippocampus;liver;testis;cervix;spleen;germinal center;kidney;brain;mammary gland;tonsil;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons; 0.14220 0.11697 0.001895464 54.03397028 220.84228 3.21396 REM1 1.6783884226419e-05 0.43382554017968 0.566157675936094 RAS (RAD and GEM)-like GTP-binding 1 FUNCTION: Promotes endothelial cell sprouting and actin cytoskeletal reorganization. May be involved in angiogenesis. May function in Ca(2+) signaling.; . TISSUE SPECIFICITY: Most highly expressed in the endothelial lining of the blood vessels in uterus and heart. Lower levels found in spleen, lymph node, kidney and testis. Also found in cells with secretory function such as the islets of Langerhans, lobule/duct epithelium in the breast, bile duct epithelium in the liver, surface epithelium in the endometrial glands of the uterus, colon mucosa and acinar cells in the pancreas and the prostate.; unclassifiable (Anatomical System);uterus;pancreas;lung;heart;bone;placenta;testis;spinal ganglion;skin; dorsal root ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.22406 0.12413 -0.159704656 41.90846898 3498.71835 11.39342 REM2 0.00050240605135054 0.682663346359705 0.316834247588944 RAS (RAD and GEM)-like GTP binding 2 FUNCTION: Binds GTP saturably and exhibits a low intrinsic rate of GTP hydrolysis. {ECO:0000250|UniProtKB:Q9WTY2}.; . . unclassifiable (Anatomical System);lung;endometrium;testis;colon;spleen;brain; . 0.41667 0.10679 -0.071520315 48.34866714 982.67944 6.05046 REN 0.00660413891460337 0.98947639941704 0.00391946166835694 renin FUNCTION: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.; DISEASE: Renal tubular dysgenesis (RTD) [MIM:267430]: Autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype). {ECO:0000269|PubMed:16116425}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Familial juvenile hyperuricemic nephropathy 2 (HNFJ2) [MIM:613092]: A renal disease characterized by juvenile onset of hyperuricemia, slowly progressive renal failure and anemia. {ECO:0000269|PubMed:19664745}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;lung;ovary;heart;placenta;colon;parathyroid;kidney;skin;stomach; superior cervical ganglion;ovary;kidney; 0.09012 0.89087 -0.402212257 26.7338995 42.28384 1.23092 RENBP 0.962622292028919 0.0373624340665686 1.5273904512898e-05 renin binding protein FUNCTION: Catalyzes the interconversion of N-acetylglucosamine to N-acetylmannosamine. Binds to renin forming a protein complex called high molecular weight (HMW) renin and inhibits renin activity. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway: although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded. {ECO:0000269|PubMed:9990133}.; . . . . 0.08751 0.18638 0.995816767 90.62278839 538.78318 4.73033 RENS2 . . . Renpenning syndrome 2 . . . . . . . . . . . REP15 0.00139895184971886 0.428049642707761 0.57055140544252 RAB15 effector protein FUNCTION: Regulates transferrin receptor recycling from the endocytic recycling compartment. {ECO:0000269|PubMed:16195351}.; . . unclassifiable (Anatomical System);pancreas;lung;testis;brain;mammary gland; . . . 0.193034296 66.82000472 413.64113 4.26043 REPIN1 0.961996440962356 0.0379876402124018 1.59188252417494e-05 replication initiator 1 FUNCTION: Sequence-specific double-stranded DNA-binding protein required for initiation of chromosomal DNA replication. Binds on 5'-ATT-3' reiterated sequences downstream of the origin of bidirectional replication (OBR) and a second, homologous ATT sequence of opposite orientation situated within the OBR zone. Facilitates DNA bending.; . . . . 0.62124 . 0.92967242 89.79122435 7732.69315 18.93384 REPS1 0.999363610065212 0.00063638979077368 1.44013832425528e-10 RALBP1 associated Eps domain containing 1 FUNCTION: May coordinate the cellular actions of activated EGF receptors and Ral-GTPases. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in heart and testis. {ECO:0000269|PubMed:11750063}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lacrimal gland;tongue;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;hippocampus;spleen;head and neck;kidney;mammary gland;stomach;thymus; subthalamic nucleus;testis - interstitial;superior cervical ganglion;occipital lobe;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;atrioventricular node;cingulate cortex; 0.28171 0.12183 -0.132199953 43.97853267 1155.54118 6.47576 REPS2 0.968427757558824 0.0315702096519267 2.03278924965246e-06 RALBP1 associated Eps domain containing 2 FUNCTION: Involved in growth factor signaling through its influence on the Ral signaling pathway.; . TISSUE SPECIFICITY: Expressed at high levels in the cerebrum, cerebellum, lung, kidney, and testis. Weakly expressed in the kidney. Relatively highly expressed in androgen-dependent as compared to androgen-independent prostate cancer cell lines and xenografts. Isoform 2 is down-regulated during progression of prostate cancer.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;pancreas;optic nerve;cochlea;epididymis;macula lutea;liver;spleen;kidney;brain;mammary gland;stomach; superior cervical ganglion;whole blood; 0.35957 0.11476 -0.181750739 40.15687662 36.43736 1.09224 RER1 0.969239732851388 0.0307138907614624 4.63763871498707e-05 retention in endoplasmic reticulum sorting receptor 1 FUNCTION: Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment. {ECO:0000250}.; . . lymphoreticular;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pineal body;pharynx;blood;skeletal muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;alveolus;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;stomach; testis - interstitial;superior cervical ganglion;prostate;testis - seminiferous tubule;thyroid;placenta;liver;testis;globus pallidus; 0.41698 0.10577 -0.09720619 46.20193442 4.91581 0.18231 RERE 0.999995655258253 4.34474174647455e-06 1.54412472616823e-16 arginine-glutamic acid dipeptide (RE) repeats FUNCTION: Plays a role as a transcriptional repressor during development. May play a role in the control of cell survival. Overexpression of RERE recruits BAX to the nucleus particularly to POD and triggers caspase-3 activation, leading to cell death. {ECO:0000269|PubMed:11331249}.; DISEASE: Note=A chromosomal aberration involving RERE is found in the neuroblastoma cell line NGP. Translocation t(1;15)(p36.2;q24).; TISSUE SPECIFICITY: Widely expressed. Expressed in tumor cell lines. {ECO:0000269|PubMed:10729226, ECO:0000269|PubMed:10814707, ECO:0000269|PubMed:11331249}.; ovary;salivary gland;sympathetic chain;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve;cerebellum; dorsal root ganglion;testis - interstitial;superior cervical ganglion;temporal lobe;spinal cord;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cerebellum; 0.87038 0.13942 -2.629516077 0.784383109 607.52718 4.98583 REREP1Y . . . arginine-glutamic acid dipeptide (RE) repeats pseudogene 1, Y-linked . . . . . . . . . . . REREP2Y . . . arginine-glutamic acid dipeptide (RE) repeats pseudogene 2, Y-linked . . . . . . . . . . . REREP3 . . . arginine-glutamic acid dipeptide (RE) repeats pseudogene 3 . . . . . . . . . . . RERG 0.00116495678097805 0.84128781032491 0.157547232894112 RAS like estrogen regulated growth inhibitor FUNCTION: Binds GDP/GTP and possesses intrinsic GTPase activity. Has higher affinity for GDP than for GTP. In cell lines overexpression leads to a reduction in the rate of proliferation, colony formation and in tumorigenic potential. {ECO:0000269|PubMed:11533059}.; . TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung, liver, skin, kidney and pancreas. Detected in estrogen receptor- positive breast-derived cell lines, but not in estrogen receptor- negative cell lines. Expression is decreased or lost in a significant proportion of primary breast tumors with poor clinical prognosis. {ECO:0000269|PubMed:11533059}.; ovary;salivary gland;intestine;colon;retina;uterus;prostate;endometrium;bone;testis;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;kidney;stomach;aorta;peripheral nerve; uterus;superior cervical ganglion;atrioventricular node; 0.20476 0.11262 -0.273576253 33.97027601 8.136 0.29895 RERG-AS1 . . . RERG antisense RNA 1 . . . . . . . . . . . RERG-IT1 . . . RERG intronic transcript 1 . . . . . . . . . . . RERGL 5.31614636600088e-09 0.0636529290099171 0.936347065673937 RERG like FUNCTION: Binds GDP/GTP and may possess intrinsic GTPase activity. {ECO:0000250}.; . . uterus;frontal lobe;heart;islets of Langerhans;kidney;brain;skin;skeletal muscle;peripheral nerve; trigeminal ganglion; 0.07575 . 0.284856336 71.40835103 402.70211 4.20921 RESP18 . . . regulated endocrine specific protein 18 FUNCTION: May play an important regulatory role in corticotrophs. {ECO:0000250}.; . TISSUE SPECIFICITY: Pancreas. Found in alpha, beta and delta cells in the pancreatic islets. {ECO:0000269|PubMed:17951542}.; lung;testis; . . . 1.547065406 95.59447983 4828.78806 14.08800 REST 0.972672070524831 0.0273265082751779 1.42119999111935e-06 RE1 silencing transcription factor FUNCTION: Transcriptional repressor which binds neuron-restrictive silencer element (NRSE) and represses neuronal gene transcription in non-neuronal cells. Restricts the expression of neuronal genes by associating with two distinct corepressors, mSin3 and CoREST, which in turn recruit histone deacetylase to the promoters of REST-regulated genes. Mediates repression by recruiting the BHC complex at RE1/NRSE sites which acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. Transcriptional repression by REST-CDYL via the recruitment of histone methyltransferase EHMT2 may be important in transformation suppression. {ECO:0000269|PubMed:12399542, ECO:0000269|PubMed:19061646, ECO:0000269|PubMed:7697725, ECO:0000269|PubMed:7871435, ECO:0000269|PubMed:8568247}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed at higher levels in the tissues of the lymphocytic compartment, including spleen, thymus, peripheral blood lymphocytes and ovary. {ECO:0000269|PubMed:8568247}.; unclassifiable (Anatomical System);cartilage;ovary;heart;parathyroid;blood;lens;skin;skeletal muscle;bone marrow;breast;uterus;lung;endometrium;nasopharynx;bone;thyroid;placenta;liver;head and neck;spleen;germinal center;kidney;bladder;stomach; dorsal root ganglion;superior cervical ganglion;temporal lobe;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.17428 0.39640 2.072468822 97.80608634 656.30434 5.13680 RET 0.999889043907306 0.000110956090650627 2.04326509935969e-12 ret proto-oncogene FUNCTION: Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. Phosphorylates PTK2/FAK1. Regulates both cell death/survival balance and positional information. Required for the molecular mechanisms orchestration during intestine organogenesis; involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut- associated lymphoid tissue. Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e.g. ITGB1 and ITGB3)-dependent manner. Involved in the development of the neural crest. Active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage. Acts as a dependence receptor; in the presence of the ligand GDNF in somatotrophs (within pituitary), promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF. Regulates nociceptor survival and size. Triggers the differentiation of rapidly adapting (RA) mechanoreceptors. Mediator of several diseases such as neuroendocrine cancers; these diseases are characterized by aberrant integrins-regulated cell migration. {ECO:0000269|PubMed:20064382, ECO:0000269|PubMed:20616503, ECO:0000269|PubMed:20702524, ECO:0000269|PubMed:21357690, ECO:0000269|PubMed:21454698}.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Hirschsprung disease 1 (HSCR1) [MIM:142623]: A disorder of neural crest development characterized by absence of enteric ganglia along a variable length of the intestine. It is the most common cause of congenital intestinal obstruction. Early symptoms range from complete acute neonatal obstruction, characterized by vomiting, abdominal distention and failure to pass stool, to chronic constipation in the older child. {ECO:0000269|PubMed:10090908, ECO:0000269|PubMed:10484767, ECO:0000269|PubMed:10618407, ECO:0000269|PubMed:22174939, ECO:0000269|PubMed:7581377, ECO:0000269|PubMed:7633441, ECO:0000269|PubMed:7704557, ECO:0000269|PubMed:7881414, ECO:0000269|PubMed:8114938, ECO:0000269|PubMed:8114939, ECO:0000269|PubMed:9043870, ECO:0000269|PubMed:9090527, ECO:0000269|PubMed:9094028, ECO:0000269|PubMed:9259198, ECO:0000269|PubMed:9384613, ECO:0000269|Ref.56}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Medullary thyroid carcinoma (MTC) [MIM:155240]: Rare tumor derived from the C cells of the thyroid. Three hereditary forms are known, that are transmitted in an autosomal dominant fashion: (a) multiple neoplasia type 2A (MEN2A), (b) multiple neoplasia type IIB (MEN2B) and (c) familial MTC (FMTC), which occurs in 25-30% of MTC cases and where MTC is the only clinical manifestation. {ECO:0000269|PubMed:10323403, ECO:0000269|PubMed:10826520, ECO:0000269|PubMed:11692159, ECO:0000269|PubMed:7784092, ECO:0000269|PubMed:7845675, ECO:0000269|PubMed:7849720, ECO:0000269|PubMed:7874109, ECO:0000269|PubMed:7881414, ECO:0000269|PubMed:7915165, ECO:0000269|PubMed:8103403, ECO:0000269|PubMed:8557249, ECO:0000269|PubMed:8625130, ECO:0000269|PubMed:8807338, ECO:0000269|PubMed:9223675, ECO:0000269|PubMed:9259198, ECO:0000269|PubMed:9398735, ECO:0000269|PubMed:9452077, ECO:0000269|PubMed:9506724, ECO:0000269|PubMed:9621513, ECO:0000269|PubMed:9677065}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multiple neoplasia 2B (MEN2B) [MIM:162300]: Uncommon inherited cancer syndrome characterized by predisposition to MTC and phaeochromocytoma which is associated with marfanoid habitus, mucosal neuromas, skeletal and ophthalmic abnormalities, and ganglioneuromas of the intestine tract. Then the disease progresses rapidly with the development of metastatic MTC and a pheochromocytome in 50% of cases. {ECO:0000269|PubMed:7906417, ECO:0000269|PubMed:7906866, ECO:0000269|PubMed:7911697, ECO:0000269|PubMed:8595427, ECO:0000269|PubMed:8807338, ECO:0000269|PubMed:9294615, ECO:0000269|PubMed:9360560}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pheochromocytoma (PCC) [MIM:171300]: A catecholamine- producing tumor of chromaffin tissue of the adrenal medulla or sympathetic paraganglia. The cardinal symptom, reflecting the increased secretion of epinephrine and norepinephrine, is hypertension, which may be persistent or intermittent. {ECO:0000269|PubMed:12000816}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Multiple neoplasia 2A (MEN2A) [MIM:171400]: The most frequent form of medullary thyroid cancer (MTC). It is an inherited cancer syndrome characterized by MTC, phaeochromocytoma and/or hyperparathyroidism. {ECO:0000269|PubMed:10522989, ECO:0000269|PubMed:7860065, ECO:0000269|PubMed:7874109, ECO:0000269|PubMed:7881414, ECO:0000269|PubMed:8099202, ECO:0000269|PubMed:8626834, ECO:0000269|PubMed:8807338, ECO:0000269|PubMed:9097963, ECO:0000269|PubMed:9384613, ECO:0000269|PubMed:9452064}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Various chromosomal aberrations involving RET are known. Some of them have been found in papillary thyroid carcinomas (PTCs) (PubMed:12787916, PubMed:2406025, PubMed:10980597, PubMed:10439047). Inversion inv(10)(q11.2;q21) generates the RET/CCDC6 (PTC1) oncogene (PubMed:2406025). Inversion inv(10)(q11.2;q11.2) generates the RET/NCOA4 (PTC3) oncogene. Translocation t(10;14)(q11;q32) with GOLGA5 generates the RET/GOLGA5 (PTC5) oncogene (PubMed:2734021). Translocation t(8;10)(p21.3;q11.2) with PCM1 generates the PCM1/RET fusion (PubMed:10980597). Translocation t(6;10)(p21.3;q11.2) with TRIM27/RFP generates the Delta RFP/RET oncogene (PubMed:12787916). Translocation t(1;10)(p13;q11) with TRIM33 generates the TRIM33/RET (PTC7) oncogene (PubMed:10439047). Translocation t(7;10)(q32;q11) with TRIM24/TIF1 generates the TRIM24/RET (PTC6) oncogene (PubMed:10439047). Translocation t(6;10)(p21.3;q11.2) with TRIM27/RFP generates the TRIM27/RET oncogene (PubMed:3037315). {ECO:0000269|PubMed:10439047, ECO:0000269|PubMed:10980597, ECO:0000269|PubMed:12787916, ECO:0000269|PubMed:2406025, ECO:0000269|PubMed:2734021, ECO:0000269|PubMed:3037315}.; DISEASE: Note=Mutations in RET have been detected in patients with renal agenesis suggesting a possible involvement of this gene in disease pathogenesis.; DISEASE: Congenital central hypoventilation syndrome (CCHS) [MIM:209880]: Rare disorder characterized by abnormal control of respiration in the absence of neuromuscular or lung disease, or an identifiable brain stem lesion. A deficiency in autonomic control of respiration results in inadequate or negligible ventilatory and arousal responses to hypercapnia and hypoxemia. {ECO:0000269|PubMed:12086152, ECO:0000269|PubMed:14566559, ECO:0000269|PubMed:9497256}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);breast;pancreas;sympathetic chain;macula lutea;liver;blood;fovea centralis;kidney;brain; dorsal root ganglion;superior cervical ganglion;medulla oblongata;uterus corpus;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe; 0.90316 0.68126 -1.609459583 3.001887238 1155.10498 6.47477 RETN 0.0740027903756986 0.745502455689905 0.180494753934396 resistin FUNCTION: Hormone that seems to suppress insulin ability to stimulate glucose uptake into adipose cells. Potentially links obesity to diabetes.; . TISSUE SPECIFICITY: Expressed only in fatty tissues.; unclassifiable (Anatomical System);optic nerve;placenta;macula lutea;colon;fovea centralis;choroid;lens;retina; bone marrow; 0.07151 . 0.013025609 54.62962963 2.42893 0.08702 RETNLB 0.0099474568203867 0.602393214700219 0.387659328479394 resistin like beta FUNCTION: Probable hormone.; . TISSUE SPECIFICITY: Expressed only in the gastrointestinal tract, particularly the colon.; colon; . 0.04459 0.14328 0.369407109 74.95281906 2044.02241 8.33594 RETSAT 2.04966693109555e-10 0.398709533271399 0.601290466523635 retinol saturase (all-trans-retinol 13,14-reductase) FUNCTION: Retinol saturase carrying out the saturation of the 13- 14 double bond of all-trans-retinol to produce all-trans-13,14- dihydroretinol. Has activity toward all-trans-retinol as substrate. Does not use all-trans-retinoic acid nor 9-cis, 11-cis or 13-cis-retinol isomers as substrates. May play a role in the metabolism of vitamin A (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;oesophagus;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;adipose tissue;thyroid;liver;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.11067 0.09350 0.07167258 59.15899976 314.14546 3.76928 REV1 0.997023540664416 0.00297645932520449 1.03795855083552e-11 REV1, DNA directed polymerase FUNCTION: Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. {ECO:0000269|PubMed:10536157, ECO:0000269|PubMed:10760286, ECO:0000269|PubMed:11278384, ECO:0000269|PubMed:11485998, ECO:0000269|PubMed:22266823}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10536157, ECO:0000269|PubMed:11278384, ECO:0000269|PubMed:11485998}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; 0.22100 . 0.055085661 57.54895022 2444.8046 9.19887 REV3L 0.999999999999932 6.81431913866016e-14 7.44836248900986e-35 REV3 like, DNA directed polymerase zeta catalytic subunit FUNCTION: Interacts with MAD2L2 to form the error prone DNA polymerase zeta involved in translesion DNA synthesis.; . TISSUE SPECIFICITY: Ubiquitously expressed.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;thyroid;testis;germinal center;spinal ganglion;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;lung;adrenal gland;mesenchyma;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach;aorta;thymus; uterus;amygdala;adipose tissue;fetal brain;prefrontal cortex;globus pallidus;skin; 0.85968 0.19470 -2.097226344 1.551073366 1709.50934 7.62408 REV3L-IT1 . . . REV3L intronic transcript 1 . . . . . . . . . . . REXO1 0.567927564385063 0.432051208842801 2.12267721360225e-05 REX1, RNA exonuclease 1 homolog FUNCTION: Seems to have no detectable effect on transcription elongation in vitro. {ECO:0000269|PubMed:12943681}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12943681}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;muscle;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.22306 0.10566 -1.357871407 4.535267752 6405.25153 16.73276 REXO1L1P . . . REX1, RNA exonuclease 1 homolog-like 1, pseudogene . . . . . . . . . 6.57396 0.24294 REXO1L2P . . . REX1, RNA exonuclease 1 homolog-like 2, pseudogene . . . . . . . . . . . REXO1L3P . . . REX1, RNA exonuclease 1 homolog-like 3, pseudogene . . . . . . . . . . . REXO1L4P . . . REX1, RNA exonuclease 1 homolog-like 4, pseudogene . . . . . . . . . . . REXO1L5P . . . REX1, RNA exonuclease 1 homolog-like 5, pseudogene . . . . . . . . . . . REXO1L6P . . . REX1, RNA exonuclease 1 homolog-like 6, pseudogene . . . . . . . . . . . REXO1L8P . . . REX1, RNA exonuclease 1 homolog-like 8, pseudogene . . . . . . . . . . . REXO1L9P . . . REX1, RNA exonuclease 1 homolog-like 9, pseudogene . . . . . . . . . . . REXO1L10P . . . REX1, RNA exonuclease 1 homolog-like 10, pseudogene . . . . . . . . . . . REXO1L11P . . . REX1, RNA exonuclease 1 homolog-like 11, pseudogene . . . . . . . . . . . REXO1L12P . . . REX1, RNA exonuclease 1 homolog-like 12, pseudogene . . . . . . . . . . . REXO2 0.888428672321779 0.11132645223662 0.000244875441600266 RNA exonuclease 2 FUNCTION: 3'-to-5' exoribonuclease specific for small oligoribonucleotides. Active on small (primarily G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G-protein.; . TISSUE SPECIFICITY: Highest expression in lung. Placenta, liver and heart also express high levels of GAIP.; lymphoreticular;ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;frontal lobe;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;whole blood;bone marrow; 0.16521 0.15257 -0.073340031 48.11866006 17.51167 0.61438 RGS20 0.0162152582585256 0.959339455642005 0.0244452860994696 regulator of G-protein signaling 20 FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is inhibited by the phosphorylation and palmitoylation of the G- protein. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:12379657}.; . TISSUE SPECIFICITY: Isoform 5 is expressed in brain at high levels in the caudate nucleus and temporal lobe.; unclassifiable (Anatomical System);heart;ovary;cartilage;parathyroid;skin;bile duct;uterus;whole body;lung;cochlea;placenta;bone;brain; amygdala;medulla oblongata;subthalamic nucleus;occipital lobe;prefrontal cortex;globus pallidus;caudate nucleus;parietal lobe;cingulate cortex; 0.06935 0.09192 -0.205617011 38.57631517 44.51825 1.27626 RGS21 0.00740545430462791 0.772780236973426 0.219814308721946 regulator of G-protein signaling 21 FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. {ECO:0000250}.; . . . . 0.30684 . 0.147123112 64.11299835 58.67041 1.55175 RGS22 1.18909888570947e-20 0.111898503203558 0.888101496796442 regulator of G-protein signaling 22 FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. {ECO:0000250}.; . TISSUE SPECIFICITY: Testis-specific. Expressed in Leydig cells and spermatogenic cells from the spermatogonia to spermatid stages (at protein level). {ECO:0000269|PubMed:18703424}.; unclassifiable (Anatomical System);uterus;optic nerve;lung;endometrium;macula lutea;testis;fovea centralis;choroid;lens;skeletal muscle;retina; testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.14708 0.08423 1.140856814 92.36848313 603.44916 4.97255 RGSL1 . . . regulator of G-protein signaling like 1 . . . testis; dorsal root ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15666 . . . 3949.09836 12.43660 RHAG 0.340299251263077 0.659088513060885 0.000612235676037155 Rh-associated glycoprotein FUNCTION: Associated with rhesus blood group antigen expression. May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. {ECO:0000269|PubMed:11062476, ECO:0000269|PubMed:11861637}.; . TISSUE SPECIFICITY: Erythrocytes. {ECO:0000269|PubMed:9473510}.; unclassifiable (Anatomical System);lung;heart;bone;liver;spleen;blood;skeletal muscle; fetal liver;superior cervical ganglion;temporal lobe;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;bone marrow; 0.98991 0.07602 -0.047654689 50.22410946 738.81446 5.39430 RHBDD1 4.74167775070528e-09 0.0596089128138642 0.940391082444458 rhomboid domain containing 1 FUNCTION: Intramembrane-cleaving serine protease that cleaves single transmembrane or multi-pass membrane proteins in the hydrophobic plane of the membrane, luminal loops and juxtamembrane regions. Involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded membrane proteins. Required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Functions in BIK, MPZ, PKD1, PTCRA, RHO, STEAP3 and TRAC processing. Involved in the regulation of exosomal secretion; inhibits the TSAP6-mediated secretion pathway. Involved in the regulation of apoptosis; modulates BIK-mediated apoptotic activity. Also plays a role in the regulation of spermatogenesis; inhibits apoptotic activity in spermatogonia. {ECO:0000269|PubMed:18953687, ECO:0000269|PubMed:22624035}.; . TISSUE SPECIFICITY: Expressed strongly in testis.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pancreas;nasopharynx;placenta;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04305 0.06354 0.773521534 87.06062751 355.6199 3.99174 RHBDD2 0.646226806703523 0.347580993094682 0.00619220020179593 rhomboid domain containing 2 . . . ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;pancreas;lung;adrenal gland;placenta;hippocampus;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; whole brain;amygdala;subthalamic nucleus;medulla oblongata;occipital lobe;adrenal gland;hypothalamus;temporal lobe;caudate nucleus;parietal lobe; 0.10681 . -0.492218069 22.35786742 34.93225 1.06207 RHBDD3 2.03589668904127e-05 0.278650879174532 0.721328761858577 rhomboid domain containing 3 . . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.26598 0.08681 -0.157884861 42.05590941 99.57906 2.15997 RHBDF1 3.65345577837932e-06 0.997360517640931 0.00263582890329086 rhomboid 5 homolog 1 (Drosophila) FUNCTION: Rhomboid protease-like protein which has no protease activity but regulates the secretion of several ligands of the epidermal growth factor receptor. Indirectly activates the epidermal growth factor receptor signaling pathway and may thereby regulate sleep, cell survival, proliferation and migration. {ECO:0000269|PubMed:15965977, ECO:0000269|PubMed:18524845, ECO:0000269|PubMed:18832597, ECO:0000269|PubMed:21439629}.; . TISSUE SPECIFICITY: Highly expressed in cerebellum, cerebrum, heart, skeletal muscle, placenta, pancreatic islet and testis. Detected at lower levels in colon, kidney, small intestine and lung. {ECO:0000269|PubMed:15965977, ECO:0000269|PubMed:8318735}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;urinary;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;olfactory bulb;placenta;ciliary ganglion;trigeminal ganglion; 0.22495 . -0.791786324 12.59731069 281.70325 3.59511 RHBDF1P1 . . . RHBDF1 pseudogene 1 . . . . . . . . . . . RHBDF2 0.000966720943739994 0.998509275066769 0.000524003989491445 rhomboid 5 homolog 2 (Drosophila) FUNCTION: Rhomboid protease-like protein which has no protease activity but regulates the secretion of several ligands of the epidermal growth factor receptor. Indirectly activates the epidermal growth factor receptor signaling pathway and may thereby regulate sleep, cell survival, proliferation and migration (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Found in the epidermis and esophageal epithelium. {ECO:0000269|PubMed:22265016}.; lymphoreticular;smooth muscle;sympathetic chain;colon;skin;uterus;prostate;oesophagus;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;urinary;blood;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;mammary gland;stomach;aorta; white blood cells; 0.22785 0.10899 -0.367438677 28.29087049 609.30799 4.99073 RHBDL1 0.494734021596252 0.500790555081153 0.00447542332259449 rhomboid, veinlet-like 1 (Drosophila) FUNCTION: May be involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in heart, brain, skeletal muscle and kidney.; unclassifiable (Anatomical System);optic nerve;hypothalamus;macula lutea;hippocampus;colon;fovea centralis;choroid;lens;retina; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.33778 0.17310 -0.093566408 46.7386176 31.87192 1.00265 RHBDL2 2.70127816729767e-06 0.309075741548158 0.690921557173675 rhomboid, veinlet-like 2 (Drosophila) FUNCTION: Involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. Known substrate: EFNB3. {ECO:0000269|PubMed:11672525, ECO:0000269|PubMed:15047175}.; . . lung;whole body;endometrium;liver;testis;colon;spleen;brain;skeletal muscle; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.07442 0.08555 0.593509966 82.51356452 2851.93253 10.10291 RHBDL3 0.00152311404141233 0.967948765690525 0.0305281202680622 rhomboid, veinlet-like 3 (Drosophila) FUNCTION: May be involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. {ECO:0000250}.; . . unclassifiable (Anatomical System);brain; dorsal root ganglion;superior cervical ganglion;occipital lobe;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.15890 0.10761 -0.249709319 35.74545883 2655.56199 9.68692 RHBG 3.72564357556274e-10 0.09378664716053 0.906213352466906 Rh family B glycoprotein (gene/pseudogene) FUNCTION: Functions as a specific ammonium transporter. {ECO:0000269|PubMed:15284342, ECO:0000269|PubMed:15929723}.; . TISSUE SPECIFICITY: Specifically expressed in kidney. Also detected in liver and ovary. {ECO:0000269|PubMed:11024028}.; liver;spleen;kidney; superior cervical ganglion;testis - seminiferous tubule;cerebellum peduncles;testis;ciliary ganglion;kidney;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.04516 0.11744 . . 6525.59053 16.96932 RHCE 0.861454126246099 0.138457772500318 8.81012535834144e-05 Rh blood group CcEe antigens FUNCTION: May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane.; . TISSUE SPECIFICITY: Restricted to tissues or cell lines expressing erythroid characters. Isoform 4g and isoform RhPI-Alpha are expressed in immature erythroblasts but not in mature erythroblasts. {ECO:0000269|PubMed:8117271}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;subthalamic nucleus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;islets of Langerhans;urinary;blood;lens;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;aorta; superior cervical ganglion;fetal liver;trigeminal ganglion;skeletal muscle;bone marrow; 0.18894 0.11913 1.686630123 96.38476056 2200.98585 8.63676 RHCG 4.90789526315851e-06 0.856341185318143 0.143653906786594 Rh family C glycoprotein FUNCTION: Functions as an electroneutral and bidirectional ammonium transporter. May regulate transepithelial ammonia secretion. {ECO:0000269|PubMed:11062476, ECO:0000269|PubMed:14761968, ECO:0000269|PubMed:15929723, ECO:0000269|PubMed:16477434}.; . TISSUE SPECIFICITY: Expressed in brain, testis, placenta, pancreas, esophagus and prostate. Expressed in squamous epithelial tissues (at protein level). According to PubMed:11062476, specifically expressed in kidney. {ECO:0000269|PubMed:10852913, ECO:0000269|PubMed:11062476, ECO:0000269|PubMed:12204676}.; medulla oblongata;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;oesophagus;larynx;bladder;unclassifiable (Anatomical System);tongue;oral cavity;lens;skeletal muscle;breast;lung;adrenal gland;nasopharynx;macula lutea;hypopharynx;alveolus;head and neck;cervix;kidney;stomach; superior cervical ganglion;tongue;pons;kidney;trigeminal ganglion;cingulate cortex;tonsil; 0.08768 0.13769 -0.44448505 24.46331682 838.56048 5.67212 RHD 0.00606009991775824 0.972907919580733 0.0210319805015084 Rh blood group D antigen FUNCTION: May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane.; . TISSUE SPECIFICITY: Restricted to tissues or cell lines expressing erythroid characters.; unclassifiable (Anatomical System);cochlea;pituitary gland;liver;colon;spleen;blood;germinal center;skeletal muscle; superior cervical ganglion;fetal liver;atrioventricular node;bone marrow; 0.40369 . 3.311471185 99.41613588 1433.80387 7.06993 RHEB 0.954420413456341 0.0454563813456059 0.000123205198053297 Ras homolog enriched in brain FUNCTION: Activates the protein kinase activity of mTORC1, and thereby plays a role in the regulation of apoptosis. Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Has low intrinsic GTPase activity. {ECO:0000269|PubMed:12271141, ECO:0000269|PubMed:12869586, ECO:0000269|PubMed:15340059, ECO:0000269|PubMed:15854902, ECO:0000269|PubMed:16098514, ECO:0000269|PubMed:20381137}.; . TISSUE SPECIFICITY: Ubiquitous. Highest levels observed in skeletal and cardiac muscle. {ECO:0000269|PubMed:8543055}.; smooth muscle;ovary;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; subthalamic nucleus;temporal lobe;atrioventricular node;trigeminal ganglion; 0.78345 0.17050 0.013025609 54.62962963 4.50081 0.16313 RHEBL1 3.29298900292704e-06 0.340729340671589 0.659267366339408 Ras homolog enriched in brain like 1 FUNCTION: Binds GTP and exhibits intrinsic GTPase activity. May activate NF-kappa-B-mediated gene transcription. Promotes signal transduction through MTOR, activates RPS6KB1, and is a downstream target of the small GTPase-activating proteins TSC1 and TSC2. {ECO:0000269|PubMed:12869548, ECO:0000269|PubMed:16098514, ECO:0000269|PubMed:16328882, ECO:0000269|PubMed:17162089}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Expression increased at least 2-fold in several tumor cell lines. {ECO:0000269|PubMed:16006564, ECO:0000269|PubMed:16328882}.; unclassifiable (Anatomical System);myocardium;ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;lung;visual apparatus;liver;kidney;brain;bladder; subthalamic nucleus;globus pallidus; 0.17457 0.09581 0.058937498 58.26256192 7.12898 0.26625 RHEBP1 . . . Ras-homolog enriched in brain pseudogene 1 FUNCTION: Activates the protein kinase activity of mTORC1, and thereby plays a role in the regulation of apoptosis. Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Has low intrinsic GTPase activity. {ECO:0000269|PubMed:12271141, ECO:0000269|PubMed:12869586, ECO:0000269|PubMed:15340059, ECO:0000269|PubMed:15854902, ECO:0000269|PubMed:16098514, ECO:0000269|PubMed:20381137}.; . TISSUE SPECIFICITY: Ubiquitous. Highest levels observed in skeletal and cardiac muscle. {ECO:0000269|PubMed:8543055}.; . . 0.78345 0.17050 0.013025609 54.62962963 . . RHEBP2 . . . Ras-homolog enriched in brain pseudogene 2 . . . . . . . . . . . RHEBP3 . . . Ras-homolog enriched in brain pseudogene 3 . . . . . . . . . . . RHNO1 0.000558184641145266 0.704918916530285 0.29452289882857 RAD9-HUS1-RAD1 interacting nuclear orphan 1 FUNCTION: Plays a role in DNA damage response (DDR) signaling upon genotoxic stresses such as ionizing radiation (IR) during the S phase. Recruited to sites of DNA damage through interaction with the 9-1-1 cell-cycle checkpoint response complex and TOPBP1 in a ATR-dependent manner. Required for the progression of the G1 to S phase transition. Plays a role in the stimulation of CHEK1 phosphorylation. {ECO:0000269|PubMed:21659603}.; . TISSUE SPECIFICITY: Weakly expressed in testis, prostate, ovary, thymus and small intestine. Expressed strongly in breast cancer cells. {ECO:0000269|PubMed:20811708}.; . . 0.10242 . . . 34.24976 1.04792 RHO 0.000556528415833613 0.704296749384065 0.295146722200102 rhodopsin FUNCTION: Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal.; DISEASE: Retinitis pigmentosa 4 (RP4) [MIM:613731]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:1302614, ECO:0000269|PubMed:1391967, ECO:0000269|PubMed:1833777, ECO:0000269|PubMed:1840561, ECO:0000269|PubMed:1862076, ECO:0000269|PubMed:1897520, ECO:0000269|PubMed:1985460, ECO:0000269|PubMed:19960070, ECO:0000269|PubMed:2137202, ECO:0000269|PubMed:2215617, ECO:0000269|PubMed:22334370, ECO:0000269|PubMed:2239971, ECO:0000269|PubMed:7633434, ECO:0000269|PubMed:7981701, ECO:0000269|PubMed:7987326, ECO:0000269|PubMed:7987331, ECO:0000269|PubMed:8045708, ECO:0000269|PubMed:8076945, ECO:0000269|PubMed:8081400, ECO:0000269|PubMed:8088850, ECO:0000269|PubMed:8317502, ECO:0000269|PubMed:8353500, ECO:0000269|PubMed:8554077, ECO:0000269|PubMed:9452035}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Night blindness, congenital stationary, autosomal dominant 1 (CSNBAD1) [MIM:610445]: A non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia. {ECO:0000269|PubMed:7846071, ECO:0000269|PubMed:8358437, ECO:0000269|PubMed:9888392}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediates vision in dim light.; unclassifiable (Anatomical System);optic nerve;macula lutea;fovea centralis;choroid;lens;skeletal muscle;retina; superior cervical ganglion;appendix;ciliary ganglion;caudate nucleus;pons;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.49556 0.83261 -0.88906181 10.36801132 69.29687 1.72465 RHOA 0.804697934205436 0.190161965914856 0.00514009987970765 ras homolog family member A FUNCTION: Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis (PubMed:9635436, PubMed:19403695). {ECO:0000250, ECO:0000269|PubMed:12900402, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:19934221, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:8910519, ECO:0000269|PubMed:9121475, ECO:0000269|PubMed:9635436}.; . . myocardium;ovary;sympathetic chain;skin;bone marrow;retina;prostate;endometrium;cochlea;thyroid;germinal center;brain;heart;cartilage;urinary;blood;lens;skeletal muscle;epididymis;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; . 0.87445 0.10389 -0.009020804 52.8544468 . . RHOA-IT1 . . . RHOA intronic transcript 1 . . . . . . . . . . . RHOB 0.245030976539202 0.643323695689937 0.111645327770861 ras homolog family member B FUNCTION: Mediates apoptosis in neoplastically transformed cells after DNA damage. Not essential for development but affects cell adhesion and growth factor signaling in transformed cells. Plays a negative role in tumorigenesis as deletion causes tumor formation. Involved in intracellular protein trafficking of a number of proteins. Targets PKN1 to endosomes and is involved in trafficking of the EGF receptor from late endosomes to lysosomes. Also required for stability and nuclear trafficking of AKT1/AKT which promotes endothelial cell survival during vascular development. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Required for genotoxic stress-induced cell death in breast cancer cells. {ECO:0000269|PubMed:10508588, ECO:0000269|PubMed:15226397, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:21373644, ECO:0000269|PubMed:9478917}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;pancreas;lung;placenta;macula lutea;hippocampus;spleen;kidney;mammary gland;stomach; adrenal gland; 0.39292 . 0.080983847 59.76055674 5.09228 0.18856 RHOBTB1 0.00183822701018375 0.997136002075529 0.00102577091428758 Rho related BTB domain containing 1 . . TISSUE SPECIFICITY: Ubiquitous, with highest levels in skeletal muscle, placenta, testis, stomach, and kidney, followed by uterus and adrenal gland. Expressed in a variety of fetal tissues. {ECO:0000269|PubMed:12426103}.; medulla oblongata;smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;whole body;endometrium;bone;iris;testis;amniotic fluid;brain;unclassifiable (Anatomical System);cartilage;heart;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;macula lutea;liver;spleen;kidney;mammary gland;aorta;stomach;peripheral nerve; placenta;testis;kidney;skeletal muscle; 0.35476 0.13749 -0.709045403 14.673272 58.8089 1.55588 RHOBTB2 0.508425067947333 0.491540862662824 3.40693898420527e-05 Rho related BTB domain containing 2 . . TISSUE SPECIFICITY: Ubiquitous, with highest levels in neural tissues. Expression is also detected in fetal lung, heart, and brain. {ECO:0000269|PubMed:12426103}.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; whole brain;superior cervical ganglion;medulla oblongata;prefrontal cortex;globus pallidus;cingulate cortex; 0.17478 0.15010 -0.973616687 8.8995046 94.82717 2.09905 RHOBTB3 0.000533732466857457 0.993464262364813 0.0060020051683293 Rho related BTB domain containing 3 FUNCTION: Rab9-regulated ATPase required for endosome to Golgi transport. Involved in transport vesicle docking at the Golgi complex, possibly by participating in release M6PRBP1/TIP47 from vesicles to permit their efficient docking and fusion at the Golgi. Specifically binds Rab9, but not other Rab proteins. Has low intrinsic ATPase activity due to autoinhibition, which is relieved by Rab9. {ECO:0000269|PubMed:19490898}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in neural and cardiac tissues, pancreas, placenta and testis. {ECO:0000269|PubMed:12426103}.; . . 0.23100 . -0.201976964 38.98325077 1484.64442 7.16946 RHOC 0.586036085485523 0.403703701316197 0.0102602131982801 ras homolog family member C FUNCTION: Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells. {ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:20974804}.; . . medulla oblongata;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);trophoblast;cartilage;heart;small intestine;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; heart; 0.39470 0.18829 -0.251530012 35.42108988 43.85151 1.26139 RHOD 0.203235060329607 0.753355947675822 0.0434089919945703 ras homolog family member D FUNCTION: Involved in endosome dynamics. May coordinate membrane transport with the function of the cytoskeleton. Involved in the internalization and trafficking of activated tyrosine kinase receptors such as PDGFRB. Participates in the reorganization of actin cytoskeleton; the function seems to involve WHAMM and includes regulation of filopodia formation and actin filament bundling. Can modulate the effect of DAPK3 in reorganization of actin cytoskeleton and focal adhesion dissolution. {ECO:0000269|PubMed:23087206, ECO:0000269|PubMed:23454120, ECO:0000269|PubMed:24102721}.; . TISSUE SPECIFICITY: Heart, placenta, liver, skeletal muscle, and pancreas and, with weaker intensity, in several other tissues.; unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;lens;skin;skeletal muscle;breast;uterus;pancreas;prostate;lung;bone;placenta;visual apparatus;liver;cervix;spleen;kidney;stomach; superior cervical ganglion;lung;heart;tongue;thyroid;placenta;liver;atrioventricular node;skeletal muscle; 0.05527 0.20676 0.148941568 64.31941496 83.71945 1.94727 RHOF 0.00520736033592633 0.704183818427707 0.290608821236367 ras homolog family member F (in filopodia) FUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. Causes the formation of thin, actin-rich surface projections called filopodia. Functions cooperatively with CDC42 and Rac to generate additional structures, increasing the diversity of actin- based morphology.; . . ovary;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;pancreas;lung;epididymis;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;globus pallidus;ciliary ganglion;pons; 0.15808 0.14548 0.349177632 74.18023119 200.17138 3.05808 RHOG 0.600682842297036 0.361833743076238 0.0374834146267267 ras homolog family member G FUNCTION: Required for the formation of membrane ruffles during macropinocytosis. Plays a role in cell migration and is required for the formation of cup-like structures during trans-endothelial migration of leukocytes. In case of Salmonella enterica infection, activated by SopB and ARHGEF26/SGEF, which induces cytoskeleton rearrangements and promotes bacterial entry. {ECO:0000269|PubMed:15133129, ECO:0000269|PubMed:17074883, ECO:0000269|PubMed:17875742, ECO:0000269|PubMed:20679435}.; . . lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;choroid;skin;bone marrow;uterus;prostate;whole body;synovium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;trigeminal ganglion;whole blood;bone marrow; 0.58922 0.21763 0.03689118 56.64071715 9.54344 0.35136 RHOH 0.123279462609065 0.779904501947178 0.0968160354437564 ras homolog family member H FUNCTION: Negative regulator of hematopoietic progenitor cell proliferation, survival and migration. Critical regulator of thymocyte development and T-cell antigen receptor (TCR) signaling by mediating recruitment and activation of ZAP70. Required for phosphorylation of CD3Z, membrane translocation of ZAP70 and subsequent activation of the ZAP70-mediated pathways. Essential for efficient beta-selection and positive selection by promoting the ZAP70-dependent phosphorylation of the LAT signalosome during pre-TCR and TCR signaling. Crucial for thymocyte maturation during DN3 to DN4 transition and during positive selection. Plays critical roles in mast cell function by facilitating phosphorylation of SYK in Fc epsilon RI-mediated signal transduction. Essential for the phosphorylation of LAT, LCP2, PLCG1 and PLCG2 and for Ca(2+) mobilization in mast cells (By similarity). Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins. Inhibits the activation of NF-kappa-B by TNF and IKKB and the activation of CRK/p38 by TNF. Inhibits activities of RAC1, RHOA and CDC42. Negatively regulates leukotriene production in neutrophils. {ECO:0000250, ECO:0000269|PubMed:11809807, ECO:0000269|PubMed:19414807}.; DISEASE: Note=A chromosomal aberration involving RHOH is found in a non-Hodgkin lymphoma cell line. Translocation t(3;4)(q27;p11) with BCL6.; TISSUE SPECIFICITY: Expressed only in hematopoietic cells. Present at very high levels in the thymus, less abundant in the spleen, and least abundant in the bone marrow. Expressed at a higher level in the TH1 subtype of T-helper cells than in the TH2 subpopulation. Expressed in neutrophils under inflammatory conditions, such as cystic fibrosis, ulcerative colitis and appendicitis. {ECO:0000269|PubMed:11809807, ECO:0000269|PubMed:19414807}.; . . 0.29443 0.31047 -0.273576253 33.97027601 20.03305 0.68348 RHOJ 0.229657760958795 0.735937658923278 0.0344045801179274 ras homolog family member J FUNCTION: GTP-binding protein with GTPase activity. Elicits the formation of F-actin-rich structures in fibroblasts and is involved in the regulation of cell morphology (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;optic nerve;whole body;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;pancreas;lung;nasopharynx;placenta;macula lutea;kidney;mammary gland;stomach; . 0.51746 0.35847 -0.183570861 39.95046001 8.84889 0.32544 RHOQ 0.304654917043609 0.676657169256661 0.0186879136997301 ras homolog family member Q FUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. May play a role in CFTR trafficking to the plasma membrane. Causes the formation of thin, actin-rich surface projections called filopodia. {ECO:0000269|PubMed:15546864}.; . . myocardium;lymphoreticular;ovary;sympathetic chain;skin;retina;prostate;optic nerve;cochlea;endometrium;iris;germinal center;bladder;brain;amygdala;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;cerebral cortex;bone;testis;dura mater;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta; amygdala;adipose tissue;spinal cord;ciliary ganglion;skeletal muscle; 0.10960 0.19444 -0.163345027 41.24793583 18.62886 0.64415 RHOQP1 . . . ras homolog family member Q pseudogene 1 . . . . . . . . . . . RHOQP2 . . . ras homolog family member Q pseudogene 2 . . . . . . . . . . . RHOQP3 . . . ras homolog family member Q pseudogene 3 . . . . . . . . . . . RHOT1 0.955425773125559 0.0445742188245725 8.04986814161319e-09 ras homolog family member T1 FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution. {ECO:0000269|PubMed:12482879, ECO:0000269|PubMed:16630562}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at high level in heart and skeletal muscle. {ECO:0000269|PubMed:12482879}.; myocardium;medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; amygdala;superior cervical ganglion;occipital lobe;subthalamic nucleus;medulla oblongata;temporal lobe;prefrontal cortex;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;parietal lobe;skeletal muscle;cingulate cortex; 0.20400 0.15424 -0.426079032 25.36565228 33.45778 1.03156 RHOT1P1 . . . ras homolog family member T1 pseudogene 1 . . . . . . . . . . . RHOT1P2 . . . ras homolog family member T1 pseudogene 2 . . . . . . . . . . . RHOT1P3 . . . ras homolog family member T1 pseudogene 3 . . . . . . . . . . . RHOT2 9.27430835542939e-12 0.445128678203373 0.554871321787352 ras homolog family member T2 FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution (By similarity). {ECO:0000250, ECO:0000269|PubMed:16630562}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in heart, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:12482879, ECO:0000269|PubMed:15218247}.; lymphoreticular;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;tongue;blood;breast;pancreas;lung;cornea;placenta;visual apparatus;hypopharynx;alveolus;duodenum;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; amygdala;thyroid;testis;cerebellum; 0.12445 0.11379 -1.120710825 6.605331446 4054.23791 12.61941 RHOU 0.531957244266069 0.45247649791998 0.0155662578139511 ras homolog family member U FUNCTION: Acts upstream of PAK1 to regulate the actin cytoskeleton, adhesion turnover and increase cell migration. Stimulates quiescent cells to reenter the cell cycle. Has no detectable GTPase activity but its high intrinsic guanine nucleotide exchange activity suggests it is constitutively GTP- bound. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. {ECO:0000269|PubMed:11459829, ECO:0000269|PubMed:16472646, ECO:0000269|PubMed:17620058, ECO:0000269|PubMed:18086875, ECO:0000269|PubMed:21834987}.; . TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined. Expressed at high levels in the stomach, small intestine, brain, skeletal muscle and placenta. {ECO:0000269|PubMed:11459829, ECO:0000269|PubMed:14731133}.; . . 0.48420 0.16093 -0.229483771 36.86010852 8.43821 0.30848 RHOV 0.590311998511154 0.399773434271556 0.00991456721729023 ras homolog family member V FUNCTION: Plays a role in the control of the actin cytoskeleton via activation of the JNK pathway. {ECO:0000250|UniProtKB:Q9Z1Y0}.; . TISSUE SPECIFICITY: Highly expressed in pancreas, placenta, and fetal brain. {ECO:0000269|PubMed:11956592}.; breast;uterus;prostate;lung;larynx;placenta;cervix;head and neck;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.25604 0.15703 0.013025609 54.62962963 4.63573 0.16613 RHOXF1 0.826599973903155 0.16965451720295 0.0037455088938948 Rhox homeobox family member 1 FUNCTION: May be a transcription factor involved in reproductive processes.; . TISSUE SPECIFICITY: Ovary, testis and epididymis. Also detected in the prostate and the mammary gland. Expressed in many tumor cell lines derived from acute lymphocytic leukemia, prostate, endometrial adenocarcinoma, melanoma, bladder carcinoma, colon carcinoma, erythroleukemia and breast carcinoma. Not expressed in placenta. {ECO:0000269|PubMed:12490318}.; unclassifiable (Anatomical System);lung;testis;blood; dorsal root ganglion;testis;atrioventricular node;trigeminal ganglion; 0.00918 0.04116 -0.029247611 51.40363293 5.33831 0.19808 RHOXF1-AS1 . . . RHOXF1 antisense RNA 1 . . . . . . . . . . . RHOXF1P1 . . . Rhox homeobox family member 1 pseudogene 1 . . . . . . . . . . . RHOXF1P2 . . . Rhox homeobox family member 1 pseudogene 2 . . . . . . . . . . . RHOXF1P3 . . . Rhox homeobox family member 1 pseudogene 3 . . . . . . . . . . . RHOXF2 0.592958781555666 0.367406338299744 0.0396348801445894 Rhox homeobox family member 2 . . TISSUE SPECIFICITY: Testis. Not detected in epididymis nor placenta. {ECO:0000269|PubMed:12490318}.; . . 0.02124 0.05186 . . 37.98883 1.12837 RHOXF2B 0.576875870835534 0.378729160937553 0.0443949682269134 Rhox homeobox family member 2B . . . . . 0.04537 . . . 1.91614 0.05970 RHPN1 1.30045250011161e-06 0.822567715881233 0.177430983666267 rhophilin, Rho GTPase binding protein 1 FUNCTION: Has no enzymatic activity. May serve as a target for Rho, and interact with some cytoskeletal component upon Rho binding or relay a Rho signal to other molecules (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;colon;fovea centralis;choroid;lens;retina;uterus;optic nerve;lung;frontal lobe;endometrium;bone;placenta;macula lutea;visual apparatus;pituitary gland;testis;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.10052 0.10074 -0.529034136 20.85987261 149.9984 2.67044 RHPN1-AS1 . . . RHPN1 antisense RNA 1 (head to head) . . . . . . . . . . . RHPN2 0.000336630552508902 0.997287291273552 0.00237607817393924 rhophilin, Rho GTPase binding protein 2 FUNCTION: Binds specifically to GTP-Rho. May function in a Rho pathway to limit stress fiber formation and/or increase the turnover of F-actin structures in the absence of high levels of RhoA activity. {ECO:0000269|PubMed:12221077}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in prostate, trachea, stomach, colon, thyroid and pancreas. Expressed at lower level in brain, spinal cord, kidney, placenta and liver. {ECO:0000269|PubMed:12221077, ECO:0000269|PubMed:12473120}.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;thyroid;bone;testis;amniotic fluid;brain;unclassifiable (Anatomical System);heart;urinary;blood;breast;pancreas;lung;placenta;visual apparatus;hippocampus;head and neck;kidney;stomach; . 0.19070 0.10228 0.003714825 54.06935598 5254.99892 14.95444 RHPN2P1 . . . rhophilin, Rho GTPase binding protein 2 pseudogene 1 . . . . . . . . . . . RIBC1 0.966259507412859 0.0336821736785913 5.83189085495388e-05 RIB43A domain with coiled-coils 1 . . . optic nerve;placenta;macula lutea;testis;fovea centralis;choroid;lens;stomach;retina; . 0.08274 0.08605 -0.405853867 26.23260203 6.16945 0.23262 RIBC2 3.91231648417033e-07 0.202269737283932 0.79772987148442 RIB43A domain with coiled-coils 2 . . . unclassifiable (Anatomical System);medulla oblongata;pancreas;lung;bone;pituitary gland;testis;colon;cervix; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;skeletal muscle; 0.17779 0.10546 . . 1604.9577 7.41463 RIC1 . . . RIC1 homolog, RAB6A GEF complex partner 1 FUNCTION: The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates RAB6A by exchanging bound GDP for free GTP and may thereby required for efficient fusion of endosome-derived vesicles with the Golgi compartment. The RIC1- RGP1 complex participates in the recycling of mannose-6-phosphate receptors. Required for phosphorylation and localization of GJA1. {ECO:0000269|PubMed:16112082, ECO:0000269|PubMed:23091056}.; . TISSUE SPECIFICITY: Present in kidney and various cell lines (at protein level). Widely expressed at low level. {ECO:0000269|PubMed:10718198, ECO:0000269|PubMed:16112082}.; . . 0.18954 0.11055 -1.697674421 2.583156405 . . RIC3 0.0122613505184732 0.95190779277218 0.0358308567093465 RIC3 acetylcholine receptor chaperone FUNCTION: Promotes functional expression of homomeric alpha-7 and alpha-8 nicotinic acetylcholine receptors at the cell surface. May also promote functional expression of homomeric serotoninergic 5- HT3 receptors, and of heteromeric acetylcholine receptors alpha- 3/beta-2, alpha-3/beta-4, alpha-4/beta-2 and alpha-4/beta-4. {ECO:0000269|PubMed:12821669, ECO:0000269|PubMed:15504725, ECO:0000269|PubMed:15809299, ECO:0000269|PubMed:15927954, ECO:0000269|PubMed:16120769, ECO:0000269|PubMed:17609200, ECO:0000269|PubMed:18691158}.; . TISSUE SPECIFICITY: Broadly expressed, with high levels in muscle, brain, heart, pancreas and testis. In the central nervous system, highest levels are detected in the cerebellum and pituitary gland. Over-expressed in brains from patients with bipolar disease or schizophrenia. Isoform 5 is predominantly expressed in the brain. {ECO:0000269|PubMed:12821669, ECO:0000269|PubMed:17640815, ECO:0000269|PubMed:18691158}.; myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;retina;prostate;optic nerve;frontal lobe;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;blood;lens;pancreas;lung;adrenal gland;placenta;macula lutea;hippocampus;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.09742 0.10257 1.618658506 95.99551781 1290.68459 6.76322 RIC8A 0.000378552821267232 0.955448939404384 0.0441725077743492 RIC8 guanine nucleotide exchange factor A FUNCTION: Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex (By similarity). Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation. {ECO:0000250, ECO:0000269|PubMed:16629901}.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;iris;germinal center;brain;heart;cartilage;pineal body;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;adrenal gland;placenta;hippocampus;amnion;kidney;stomach;thymus;cerebellum; whole brain;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;cingulate cortex; 0.17800 0.10121 -0.110153916 45.48832272 4557.94196 13.55314 RIC8B 0.997486826763253 0.00251307316265735 1.00074089180052e-07 RIC8 guanine nucleotide exchange factor B FUNCTION: Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins by exchanging bound GDP for free GTP. Able to potentiate G(olf)-alpha-dependent cAMP accumulation suggesting that it may be an important component for odorant signal transduction. {ECO:0000250}.; . . colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;lung;macula lutea;liver;alveolus;spleen;head and neck;kidney;stomach; caudate nucleus; 0.53798 0.10163 -0.26993514 34.59542345 85.92104 1.97938 RICTOR 0.999999999869293 1.30706909396292e-10 3.0252953193937e-28 RPTOR independent companion of MTOR, complex 2 FUNCTION: Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient- insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Plays an essential role in embryonic growth and development. {ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15718470}.; . . ovary;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;kidney; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; . . -0.28106828 33.55744279 3691.63911 11.84114 RIDA . . . reactive intermediate imine deaminase A homolog FUNCTION: Endoribonuclease responsible for the inhibition of the translation by cleaving mRNA. Inhibits cell-free protein synthesis. Cleaves phosphodiester bonds only in single-stranded RNA (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Hepatocytes and renal distal tubular epithelial cells. Only weak expression in other tissues.; . . 0.16025 0.16668 -0.053113545 49.38664779 . . RIEG2 . . . Rieger syndrome 2 . . . . . . . . . . . RIF1 0.999999997436204 2.56379585387591e-09 2.10470909762426e-24 replication timing regulatory factor 1 FUNCTION: Required for checkpoint mediated arrest of cell cycle progression in response to DNA damage during S-phase (the intra-S- phase checkpoint). This checkpoint requires activation of at least 2 parallel pathways by the ATM kinase: one involves the MRN (MRE11A-RAD50-NBS1) complex, while the second requires CHEK2. RIF1 seems to act independently of both these pathways. Seems to play no role in either the G1/S or G2/M DNA damage checkpoints. {ECO:0000269|PubMed:15342490}.; . TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:15583028}.; unclassifiable (Anatomical System);smooth muscle;ovary;islets of Langerhans;colon;lens;skeletal muscle;uterus;prostate;lung;thyroid;placenta;duodenum;liver;testis;germinal center;kidney;brain;mammary gland;stomach; superior cervical ganglion;appendix;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.63638 0.09482 -1.812152875 2.182118424 452.97512 4.42889 RIIAD1 . . . regulatory subunit of type II PKA R-subunit (RIIa) domain containing 1 . . . optic nerve;macula lutea;pituitary gland;fovea centralis;choroid;lens;retina; . . . 0.367590509 74.75819769 68.0159 1.70586 RILP 0.000670859753110892 0.742575739893672 0.256753400353218 Rab interacting lysosomal protein FUNCTION: Rab effector playing a role in late endocytic transport to degradative compartments. Involved in the regulation of lysosomal morphology and distribution. Induces recruitment of dynein-dynactin motor complexes to Rab7A-containing late endosome and lysosome compartments. Promotes centripetal migration of phagosomes and the fusion of phagosomes with the late endosomes and lysosomes. {ECO:0000269|PubMed:11179213, ECO:0000269|PubMed:11696325, ECO:0000269|PubMed:12944476, ECO:0000269|PubMed:14668488}.; . TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in fetal heart, heart, stomach, spleen, adrenal gland, thyroid gland, salivary gland, fetal liver, liver and lung. Poorly expressed in brain. {ECO:0000269|PubMed:11179213, ECO:0000269|PubMed:11520070, ECO:0000269|PubMed:14668488}.; unclassifiable (Anatomical System);ovary;urinary;colon;parathyroid;skin;skeletal muscle;prostate;optic nerve;lung;endometrium;placenta;liver;spleen;cervix;kidney;brain;tonsil;stomach; . 0.09211 0.08973 . . 1278.83336 6.73381 RILPL1 0.0660195664772473 0.930954028370191 0.0030264051525613 Rab interacting lysosomal protein-like 1 FUNCTION: Plays a role in the regulation of cell shape and polarity. Plays a role in cellular protein transport, including protein transport away from primary cilia. Neuroprotective protein, which acts by sequestring GAPDH in the cytosol and prevent the apoptotic function of GAPDH in the nucleus. Competes with SIAH1 for binding GAPDH (By similarity). Does not regulate lysosomal morphology and distribution. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at lower level in liver and kidney. {ECO:0000269|PubMed:14668488}.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach; whole brain;amygdala;thyroid; 0.13509 . 0.016664174 55.21939137 55.40101 1.49373 RILPL2 0.0608721865653384 0.868916205483671 0.070211607950991 Rab interacting lysosomal protein like 2 FUNCTION: Involved in cell shape and neuronal morphogenesis, positively regulating the establishment and maintenance of dendritic spines. Plays a role in cellular protein transport, including protein transport away from primary cilia. May function via activation of RAC1 and PAK1 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in lung. {ECO:0000269|PubMed:14668488}.; unclassifiable (Anatomical System);umbilical cord;islets of Langerhans;colon;blood;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;prostate;optic nerve;lung;endometrium;bone;macula lutea;alveolus;duodenum;liver;spleen;kidney;brain;stomach; superior cervical ganglion;thyroid;white blood cells;whole blood;bone marrow; 0.07683 0.07466 -0.185391282 39.67916962 29.91633 0.95480 RIMBP2 0.292582176020545 0.707410337991669 7.48598778544702e-06 RIMS binding protein 2 FUNCTION: Plays a role in the synaptic transmission as bifunctional linker that interacts simultaneously with RIMS1, RIMS2, CACNA1D and CACNA1B. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;whole body;islets of Langerhans;brain; amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;fetal brain;temporal lobe;prefrontal cortex;globus pallidus;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe; 0.12630 0.10358 -2.070835943 1.615947157 308.7902 3.74029 RIMBP3 . . . RIMS binding protein 3 . . . unclassifiable (Anatomical System);uterus;optic nerve;lung;ovary;macula lutea;testis;fovea centralis;choroid;lens;retina; . . 0.08391 . . 1804.88297 7.84008 RIMBP3B . . . RIMS binding protein 3B . . . unclassifiable (Anatomical System);uterus;optic nerve;lung;ovary;macula lutea;testis;fovea centralis;choroid;lens;retina; . . . . . 40.17247 1.18080 RIMBP3C . . . RIMS binding protein 3C . . . unclassifiable (Anatomical System);uterus;optic nerve;lung;ovary;macula lutea;testis;fovea centralis;choroid;lens;retina; . . 0.08271 . . 0.02742 0.00111 RIMKLA 0.0873953268287957 0.87063161212178 0.0419730610494242 ribosomal modification protein rimK-like family member A FUNCTION: Catalyzes the synthesis of N-acetyl-L-aspartyl-L- glutamate (NAAG) and N-acetyl-L-aspartyl-L-glutamyl-L-glutamate. {ECO:0000250|UniProtKB:Q6PFX8}.; . . . . 0.17920 0.12023 -0.249709319 35.74545883 67.08644 1.69371 RIMKLB 0.911252633654497 0.088611934068572 0.000135432276930562 ribosomal modification protein rimK-like family member B FUNCTION: Catalyzes the synthesis of beta-citryl-L-glutamate and N-acetyl-L-aspartyl-L-glutamate. Beta-citryl-L-glutamate is synthesized more efficiently than N-acetyl-L-aspartyl-L-glutamate. {ECO:0000250|UniProtKB:Q80WS1}.; . . myocardium;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;lacrimal gland;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.19661 0.08631 -0.049474214 50.01179523 154.47629 2.71710 RIMKLBP1 . . . ribosomal modification protein rimK-like family member B pseudogene 1 . . . lymphoreticular;cervix;skeletal muscle; . . . . . . . RIMKLBP2 . . . ribosomal modification protein rimK-like family member B pseudogene 2 . . . . . . . . . . . RIMS1 0.0292114494347639 0.970788550514326 5.0909783156634e-11 regulating synaptic membrane exocytosis 1 FUNCTION: Rab effector involved in exocytosis (By similarity). May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short- term synaptic plasticity (By similarity). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000250|UniProtKB:Q99NE5, ECO:0000269|PubMed:23999003}.; DISEASE: Cone-rod dystrophy 7 (CORD7) [MIM:603649]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. {ECO:0000269|PubMed:12659814}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in melanocytes (PubMed:23999003). Detected in brain and retina (PubMed:23999003). {ECO:0000269|PubMed:23999003}.; unclassifiable (Anatomical System);frontal lobe;cerebellum cortex;liver;brain;skeletal muscle; superior cervical ganglion;subthalamic nucleus;cerebellum peduncles;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skin;skeletal muscle;cerebellum; 0.52106 0.15134 -1.543300564 3.320358575 440.01281 4.37079 RIMS2 0.999998398615947 1.60138405288881e-06 1.12486289878965e-19 regulating synaptic membrane exocytosis 2 FUNCTION: Rab effector involved in exocytosis. May act as scaffold protein. Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000269|PubMed:23999003}.; . TISSUE SPECIFICITY: Expressed in melanocytes (PubMed:23999003). {ECO:0000269|PubMed:23999003}.; unclassifiable (Anatomical System);whole body;adrenal gland;islets of Langerhans;hypothalamus;visual apparatus;pituitary gland;brain;mammary gland;skin;skeletal muscle;retina; dorsal root ganglion;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;prefrontal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.85345 0.13067 -0.5879134 18.28261382 2152.14667 8.53415 RIMS3 0.00725110831997781 0.922229096508002 0.0705197951720197 regulating synaptic membrane exocytosis 3 FUNCTION: Regulates synaptic membrane exocytosis. {ECO:0000250}.; . . . . 0.38445 0.11690 0.062575634 58.74026893 144.35552 2.61616 RIMS4 0.952765434512064 0.047099891405226 0.000134674082710595 regulating synaptic membrane exocytosis 4 FUNCTION: Regulates synaptic membrane exocytosis. {ECO:0000250}.; . . . . 0.27845 0.11729 -0.339715008 30.06605331 3.85321 0.14380 RIN1 0.000202046521763345 0.976576187521509 0.0232217659567273 Ras and Rab interactor 1 FUNCTION: Ras effector protein, which may serve as an inhibitory modulator of neuronal plasticity in aversive memory formation. Can affect Ras signaling at different levels. First, by competing with RAF1 protein for binding to activated Ras. Second, by enhancing signaling from ABL1 and ABL2, which regulate cytoskeletal remodeling. Third, by activating RAB5A, possibly by functioning as a guanine nucleotide exchange factor (GEF) for RAB5A, by exchanging bound GDP for free GTP, and facilitating Ras-activated receptor endocytosis. {ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:9144171, ECO:0000269|PubMed:9208849}.; . TISSUE SPECIFICITY: Expressed in all tissues examined with high levels in brain, placenta and pancreas. {ECO:0000269|PubMed:9144171}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;oesophagus;bone;testis;germinal center;brain;unclassifiable (Anatomical System);tongue;islets of Langerhans;lens;lung;placenta;macula lutea;visual apparatus;liver;stomach;cerebellum; ciliary ganglion;caudate nucleus;pons;atrioventricular node;trigeminal ganglion; 0.07712 0.14099 0.270087468 70.69473933 837.95353 5.66967 RIN2 0.0082955850905875 0.988883428713083 0.00282098619632961 Ras and Rab interactor 2 FUNCTION: Ras effector protein. May function as an upstream activator and/or downstream effector for RAB5B in endocytic pathway. May function as a guanine nucleotide exchange (GEF) of RAB5B, required for activating the RAB5 proteins by exchanging bound GDP for free GTP. {ECO:0000269|PubMed:11733506}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in heart, kidney, lung placenta. Expressed at low level in skeletal muscle, spleen and peripheral blood. {ECO:0000269|PubMed:11733506}.; smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;cartilage;lacrimal gland;islets of Langerhans;adrenal cortex;lens;skeletal muscle;breast;pancreas;pia mater;lung;nasopharynx;placenta;macula lutea;liver;hypopharynx;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.19645 0.13267 0.521707177 80.39631989 1572.99065 7.34058 RIN3 0.000276829502107209 0.984648822991065 0.0150743475068276 Ras and Rab interactor 3 FUNCTION: Ras effector protein that functions as a guanine nucleotide exchange (GEF) for RAB5B and RAB31, by exchanging bound GDP for free GTP. Required for normal RAB31 function. {ECO:0000269|PubMed:12972505, ECO:0000269|PubMed:21586568}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12972505}.; ovary;colon;parathyroid;skin;bone marrow;uterus;optic nerve;endometrium;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;blood;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;liver;testis;white blood cells;trigeminal ganglion;whole blood;skeletal muscle; 0.21300 0.09535 0.167138932 64.99174334 4974.51737 14.37018 RING1 0.915792421657898 0.0840892187190906 0.000118359623011538 ring finger protein 1 FUNCTION: Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. Compared to RNF2/RING2, it does not have the main E3 ubiquitin ligase activity on histone H2A, and it may rather act as a modulator of RNF2/RING2 activity. {ECO:0000269|PubMed:16359901}.; . . . . 0.38612 0.15278 -0.361761279 28.6329323 155.84978 2.72790 RINL 0.0301105358577335 0.959825075151946 0.0100643889903202 Ras and Rab interactor like FUNCTION: Guanine nucleotide exchange factor (GEF) for RAB5A and RAB22A that activates RAB5A and RAB22A by exchanging bound GDP for free GTP. Plays a role in endocytosis via its role in activating Rab family members (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;pancreas;whole body;islets of Langerhans;testis;blood;peripheral nerve; superior cervical ganglion;ciliary ganglion; . . 0.350995466 74.37485256 3406.55874 11.17847 RINT1 1.92725153213016e-06 0.998657756649387 0.00134031609908112 RAD50 interactor 1 FUNCTION: Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the NRZ complex which is believed to play a role in SNARE assembly at the ER. May play a role in cell cycle checkpoint control (PubMed:11096100). Essential for telomere length control (PubMed:16600870). {ECO:0000269|PubMed:11096100, ECO:0000269|PubMed:16600870, ECO:0000305}.; . . skin;retina;bone marrow;uterus;prostate;whole body;endometrium;gum;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;bile duct;breast;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;appendix;ciliary ganglion;trigeminal ganglion; 0.21749 0.11191 -0.310388054 32.14791224 802.75923 5.58288 RIOK1 8.13737884500142e-07 0.9099849009477 0.0900142853144157 RIO kinase 1 . . . colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;muscle;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;amnion;spleen;cervix;kidney;mammary gland;stomach; . 0.07427 0.09451 0.778977686 87.21396556 153.59995 2.71046 RIOK2 0.00114011174991567 0.988993674079408 0.00986621417067679 RIO kinase 2 . . . smooth muscle;ovary;salivary gland;intestine;colon;skin;bone marrow;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;liver;kidney;stomach;thymus; . 0.64042 0.09168 1.065596954 91.61358811 3638.14552 11.71409 RIOK3 0.000146775088539085 0.992126591094082 0.00772663381737934 RIO kinase 3 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9602165}.; lymphoreticular;medulla oblongata;ovary;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;oral cavity;blood;skeletal muscle;pancreas;lung;adrenal gland;epididymis;nasopharynx;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion; 0.52836 0.12785 -0.22584292 37.32012267 71.1293 1.75581 RIOK3P1 . . . RIO kinase 3 pseudogene 1 . . . . . . . . . . . RIPK1 0.418177400187703 0.581486943910012 0.000335655902285289 receptor interacting serine/threonine kinase 1 FUNCTION: Serine-threonine kinase which transduces inflammatory and cell-death signals (programmed necrosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage. Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor. Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade. Ubiquitination by TRAF2 via 'Lys-63'-link chains acts as a critical enhancer of communication with downstream signal transducers in the mitogen-activated protein kinase pathway and the NF-kappa-B pathway, which in turn mediate downstream events including the activation of genes encoding inflammatory molecules. Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory subunit of the IKK complex, a critical event for NF-kappa-B activation. Interaction with other cellular RHIM-containing adapters initiates gene activation and cell death. RIPK1 and RIPK3 association, in particular, forms a necrosis-inducing complex. {ECO:0000269|PubMed:11101870, ECO:0000269|PubMed:17389591, ECO:0000269|PubMed:19524512, ECO:0000269|PubMed:19524513}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);small intestine;heart;nervous;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13016 0.31423 -1.352082458 4.582448691 58.71209 1.55302 RIPK2 0.554263285932167 0.445619578169749 0.000117135898084473 receptor interacting serine/threonine kinase 2 FUNCTION: Serine/threonine/tyrosine kinase that plays an essential role in modulation of innate and adaptive immune responses. Upon stimulation by bacterial peptidoglycans, NOD1 and NOD2 are activated, oligomerize and recruit RIPK2 through CARD-CARD domains. Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3. The polyubiquitinated protein mediates the recruitment of MAP3K7/TAK1 to IKBKG/NEMO and induces 'Lys-63'-linked polyubiquitination of IKBKG/NEMO and subsequent activation of IKBKB/IKKB. In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Plays also a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation. {ECO:0000269|PubMed:14638696, ECO:0000269|PubMed:17054981, ECO:0000269|PubMed:18079694, ECO:0000269|PubMed:21123652, ECO:0000269|PubMed:21887730}.; . TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung, peripheral blood leukocytes, spleen, kidney, testis, prostate, pancreas and lymph node.; smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;blood;breast;bile duct;pancreas;lung;placenta;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; subthalamic nucleus;superior cervical ganglion;atrioventricular node; 0.21726 0.23214 0.41713504 76.95800896 641.53178 5.08995 RIPK3 2.24111545145836e-06 0.899123177793338 0.10087458109121 receptor interacting serine/threonine kinase 3 FUNCTION: Essential for necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members. Upon induction of necrosis, RIPK3 interacts with, and phosphorylates RIPK1 and MLKL to form a necrosis-inducing complex. RIPK3 binds to and enhances the activity of three metabolic enzymes: GLUL, GLUD1, and PYGL. These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production. {ECO:0000269|PubMed:19498109, ECO:0000269|PubMed:19524512, ECO:0000269|PubMed:19524513, ECO:0000269|PubMed:22265413, ECO:0000269|PubMed:22265414, ECO:0000269|PubMed:22421439}.; . TISSUE SPECIFICITY: Highly expressed in the pancreas. Detected at lower levels in heart, placenta, lung and kidney. Isoform 3 is significantly increased in colon and lung cancers. {ECO:0000269|PubMed:15896315}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;colon;blood;skin;skeletal muscle;bone marrow;uterus;lung;placenta;hypopharynx;liver;testis;cervix;head and neck;spleen;brain;mammary gland; superior cervical ganglion;trigeminal ganglion;bone marrow; 0.04916 0.14944 -0.044015879 50.44821892 324.74909 3.83108 RIPK4 0.00120659621680067 0.989682841555841 0.00911056222735777 receptor interacting serine/threonine kinase 4 FUNCTION: Involved in stratified epithelial development. It is a direct transcriptional target of TP63. Plays a role in NF-kappa-B activation. {ECO:0000269|PubMed:12446564, ECO:0000269|PubMed:22197488}.; DISEASE: Popliteal pterygium syndrome, lethal type (PPS-L) [MIM:263650]: An autosomal recessive disorder characterized by multiple popliteal pterygia leading to severe arthrogryposis, ankyloblepharon filiforme adnatum, filiform bands between the jaws, synostosis of the carpal/tarsal and phalangeal bones in the hands and feet, digital hypoplasia/aplasia, complete soft-tissue syndactyly, lack of nails, lack of scalp hair, eyebrows and eyelashes, blepharophimosis, cleft lip and/or palate, and hypoplastic external genitalia. Early lethality is common, although survival into childhood and beyond has been reported. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;breast;prostate;optic nerve;lung;endometrium;larynx;macula lutea;liver;head and neck;kidney;mammary gland;stomach; prostate;trachea;tongue;thyroid;liver;kidney;skin; 0.21725 0.17243 -1.655370293 2.754187308 1306.90402 6.79920 RIPPLY1 0.00780581933403429 0.550769978551815 0.441424202114151 ripply transcriptional repressor 1 FUNCTION: Plays a role in somitogenesis. Essential for transcriptional repression of the segmental patterning genes, thus terminating the segmentation program in the presomitic mesoderm, and also required for the maintenance of rostrocaudal polarity in somites (By similarity). {ECO:0000250|UniProtKB:Q2WG80}.; . . unclassifiable (Anatomical System);kidney;brain; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion; 0.36054 . 0.103030231 61.2762444 15.67518 0.55922 RIPPLY2 0.078765747544666 0.752437444310381 0.168796808144953 ripply transcriptional repressor 2 FUNCTION: Plays a role in somitogenesis. Required for somite segregation and establishment of rostrocaudal polarity in somites (By similarity). {ECO:0000250|UniProtKB:Q2WG76}.; . . . . . . -0.031067188 51.03798066 5.74042 0.21508 RIPPLY3 2.12280673958272e-06 0.151406772398082 0.848591104795178 ripply transcriptional repressor 3 FUNCTION: Acts as a transcriptional corepressor. Negative regulator of the transcriptional activity of TBX1. Plays a role in the development of the pharyngeal apparatus and derivatives (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at a low level in fetal kidney and fetal brain. {ECO:0000269|PubMed:10814524}.; . . 0.13922 . 0.948089677 89.95635763 105.18106 2.21915 RIPPLY3P1 . . . RIPPLY3 pseudogene 1 . . . . . . . . . . . RIT1 0.666809792340233 0.332118085847131 0.00107212181263634 Ras-like without CAAX 1 FUNCTION: Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF- dependent neuronal differentiation. Involved in ELK1 transactivation through the Ras-MAPK signaling cascade that mediates a wide variety of cellular functions, including cell proliferation, survival, and differentiation. {ECO:0000269|PubMed:15632082, ECO:0000269|PubMed:23791108}.; . TISSUE SPECIFICITY: Expressed in many tissues.; . . 0.12175 0.21177 -0.185391282 39.67916962 1.96708 0.06420 RIT2 0.0600485284509002 0.86844707465163 0.0715043968974697 Ras-like without CAAX 2 FUNCTION: Binds and exchanges GTP and GDP. {ECO:0000250}.; . TISSUE SPECIFICITY: Neuron-specific.; unclassifiable (Anatomical System);frontal lobe;hypothalamus;macula lutea;hippocampus;fovea centralis;brain; amygdala;whole brain;medulla oblongata;superior cervical ganglion;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;ciliary ganglion;trigeminal ganglion;cingulate cortex;cerebellum; 0.93403 0.28682 0.191216164 66.57230479 32.62699 1.01441 RITA1 . . . RBPJ interacting and tubulin associated 1 FUNCTION: Tubulin-binding protein that acts as a negative regulator of Notch signaling pathway. Shuttles between the cytoplasm and the nucleus and mediates the nuclear export of RBPJ/RBPSUH, thereby preventing the interaction between RBPJ/RBPSUH and NICD product of Notch proteins (Notch intracellular domain), leading to down-regulate Notch-mediated transcription. May play a role in neurogenesis. {ECO:0000269|PubMed:21102556}.; . . . . 0.04663 . 0.485092724 79.37603208 119.53598 2.37900 RLBP1 5.41120505102986e-05 0.682283784080852 0.317662103868638 retinaldehyde binding protein 1 FUNCTION: Soluble retinoid carrier essential the proper function of both rod and cone photoreceptors. Participates in the regeneration of active 11-cis-retinol and 11-cis-retinaldehyde, from the inactive 11-trans products of the rhodopsin photocycle and in the de novo synthesis of these retinoids from 11-trans metabolic precursors. The cycling of retinoids between photoreceptor and adjacent pigment epithelium cells is known as the 'visual cycle'. {ECO:0000269|PubMed:19846785}.; DISEASE: Bothnia retinal dystrophy (BRD) [MIM:607475]: A type of retinitis punctata albescens. Affected individuals show night blindness from early childhood with features consistent with retinitis punctata albescens and macular degeneration. {ECO:0000269|PubMed:10102298}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Rod-cone dystrophy Newfoundland (NFRCD) [MIM:607476]: A rod-cone dystrophy reminiscent of retinitis punctata albescens but with a substantially lower age at onset and more-rapid and distinctive progression. Rod-cone dystrophies results from initial loss of rod photoreceptors, later followed by cone photoreceptors loss. {ECO:0000269|PubMed:11868161}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Retinitis punctata albescens (RPA) [MIM:136880]: Rare form of stationary night blindness characterized by a delay in the regeneration of cone and rod photopigments. {ECO:0000269|PubMed:10102299}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Retina and pineal gland. Not present in photoreceptor cells but is expressed abundantly in the adjacent retinal pigment epithelium (RPE) and in the Mueller glial cells of the retina. {ECO:0000269|PubMed:19846785}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;endometrium;testis;bladder;brain;unclassifiable (Anatomical System);hypothalamus;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;hippocampus;visual apparatus;liver;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.25744 0.21620 0.174625237 65.9648502 62.19255 1.60830 RLF 0.999999867034835 1.32965165414839e-07 3.81953225070365e-18 rearranged L-myc fusion FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues.; . . 0.53725 0.11314 0.077132183 59.19438547 1040.82453 6.19411 RLFP1 . . . rearranged L-myc fusion pseudogene 1 . . . . . . . . . . . RLIM 0.99177291457597 0.00822527315648283 1.81226754728072e-06 ring finger protein, LIM domain interacting FUNCTION: E3 ubiquitin-protein ligase. Acts as a negative coregulator for LIM homeodomain transcription factors by mediating the ubiquitination and subsequent degradation of LIM cofactors LDB1 and LDB2 and by mediating the recruitment the SIN3a/histone deacetylase corepressor complex. Ubiquitination and degradation of LIM cofactors LDB1 and LDB2 allows DNA-bound LIM homeodomain transcription factors to interact with other protein partners such as RLIM. Plays a role in telomere length-mediated growth suppression by mediating the ubiquitination and degradation of TERF1. By targeting ZFP42 for degradation, acts as an activator of random inactivation of X chromosome in the embryo, a stochastic process in which one X chromosome is inactivated to minimize sex- related dosage differences of X-encoded genes in somatic cells of female placental mammals. {ECO:0000269|PubMed:19164295, ECO:0000269|PubMed:19945382}.; . TISSUE SPECIFICITY: Expressed in many tissues.; colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;breast;pancreas;lung;visual apparatus;macula lutea;liver;spleen;kidney;stomach; . 0.77898 0.12708 -0.249709319 35.74545883 16.45426 0.58252 RLIMP1 . . . ring finger protein, LIM domain interacting pseudogene 1 . . . unclassifiable (Anatomical System);islets of Langerhans;urinary;muscle;uterus;placenta;bone;testis;amniotic fluid;germinal center;kidney;brain;cerebellum; . . . . . . . RLIMP2 . . . ring finger protein, LIM domain interacting pseudogene 2 . . . . . . . . . . . RLIMP3 . . . ring finger protein, LIM domain interacting pseudogene 3 . . . . . . . . . . . RLN1 0.000528756556393035 0.455734364969682 0.543736878473925 relaxin 1 FUNCTION: Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. May be involved in remodeling of connective tissues during pregnancy, promoting growth of pubic ligaments and ripening of the cervix.; . TISSUE SPECIFICITY: Prostate. Not expressed in placenta, decidua or ovary. {ECO:0000269|PubMed:8735594}.; unclassifiable (Anatomical System);prostate;testis;germinal center;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.16418 . -0.093566408 46.7386176 12.15146 0.43990 RLN2 5.04438325121297e-05 0.250740768949187 0.749208787218301 relaxin 2 FUNCTION: Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. May be involved in remodeling of connective tissues during pregnancy, promoting growth of pubic ligaments and ripening of the cervix.; . TISSUE SPECIFICITY: Isoform 1 is expressed in the ovary during pregnancy. Also expressed in placenta, decidua and prostate. Isoform 2 is relatively abundant in placenta. It is in much lower abundance in the prostate gland. Not detected in the ovary. {ECO:0000269|PubMed:6548702, ECO:0000269|PubMed:8735594}.; unclassifiable (Anatomical System);lung;pituitary gland;parathyroid; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.21448 . 0.350995466 74.37485256 74.50878 1.80499 RLN3 9.7759868484547e-05 0.568788307802611 0.431113932328905 relaxin 3 FUNCTION: May play a role in neuropeptide signaling processes. Ligand for LGR7, relaxin-3 receptor-1 (GPCR135) and relaxin-3 receptor-2 (GPCR142).; . . . . 0.14245 0.11087 0.571462851 81.99457419 135.08949 2.52943 RLTPR 0.0223533069911047 0.977646683829081 9.17981461658794e-09 RGD motif, leucine rich repeats, tropomodulin domain and proline-rich containing . . TISSUE SPECIFICITY: Expressed in all tissues tested, including thymus, spleen, colon, leukocytes, peripheral blood, skin, skin keratinocytes and skin fibroblasts. {ECO:0000269|PubMed:15588584}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;thymus; . 0.22811 0.09224 -1.120710825 6.605331446 593.87232 4.93780 RMD1 . . . rippling muscle disease 1 . . . . . . . . . . . RMDN1 8.90570887997982e-07 0.515704062672411 0.484295046756701 regulator of microtubule dynamics 1 . . . . . 0.15975 0.10356 -0.093566408 46.7386176 1303.49301 6.79283 RMDN2 5.20509387294093e-16 0.00340451494470965 0.99659548505529 regulator of microtubule dynamics 2 . . . . . 0.11955 0.07480 0.852410773 88.49964614 334.47186 3.88560 RMDN2-AS1 . . . RMDN2 antisense RNA 1 . . . . . . . . . . . RMDN3 0.023779597676249 0.975618636222755 0.000601766100996401 regulator of microtubule dynamics 3 FUNCTION: Involved in cellular calcium homeostasis regulation. May participate in differentiation and apoptosis of keratinocytes. Overexpression induces apoptosis. {ECO:0000269|PubMed:16820967, ECO:0000269|PubMed:22131369}.; . TISSUE SPECIFICITY: Present at high level in epidermis and seminiferous epithelium: while basal cells in the epidermis and spermatogonia show no perceptible amount, keratinocytes of suprabasal layers and differentiating first-order spermatocytes up to spermatids exhibit high expression. In skeletal muscle, its presence is restricted to fibers of the fast twitch type. In surface epithelia containing ciliated cells, it is associated with the microtubular structures responsible for ciliary movement. Also present in specific structures of the central nervous system such as neurons of the hippocampal region, ganglion cells of the autonomic nervous system, and axons of the peripheral nervous system (at protein level). Widely expressed. {ECO:0000269|PubMed:15609043, ECO:0000269|PubMed:16820967}.; . . 0.17026 0.11024 -0.426079032 25.36565228 175.66734 2.88338 RMI1 0.00309709763513186 0.945474570833966 0.0514283315309022 RecQ mediated genome instability 1 FUNCTION: Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability. {ECO:0000269|PubMed:15775963, ECO:0000269|PubMed:16537486, ECO:0000269|PubMed:16595695}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;fovea centralis;skin;skeletal muscle;retina;uterus;pancreas;whole body;lung;endometrium;bone;macula lutea;liver;testis;germinal center;kidney;brain; testis;parietal lobe; 0.71412 0.09672 0.665103516 84.6131163 98.05269 2.14066 RMI2 0.0246041881131188 0.552514142306321 0.422881669580561 RecQ mediated genome instability 2 FUNCTION: Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. The complex is therefore essential for the stability, localization, and function of complexes containing BLM. In the RMI complex, it is required to target BLM to chromatin and stress- induced nuclear foci and mitotic phosphorylation of BLM. {ECO:0000269|PubMed:18923082, ECO:0000269|PubMed:18923083}.; . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;larynx;bone;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.40169 0.11447 . . 12.16777 0.44063 RMND1 7.66495450662999e-07 0.723096379180243 0.276902854324306 required for meiotic nuclear division 1 homolog FUNCTION: Required for mitochondrial translation, possibly by coordinating the assembly or maintenance of the mitochondrial ribosome (PubMed:23022098, PubMed:25604853). {ECO:0000269|PubMed:23022098, ECO:0000269|PubMed:25604853}.; DISEASE: Combined oxidative phosphorylation deficiency 11 (COXPD11) [MIM:614922]: A severe, multisystemic, autosomal recessive, disorder characterized by deficiencies of multiple mitochondrial respiratory enzymes leading to neonatal hypotonia and lactic acidosis. Affected individuals may have respiratory insufficiency, foot deformities, or seizures. {ECO:0000269|PubMed:23022098, ECO:0000269|PubMed:23022099, ECO:0000269|PubMed:25604853, ECO:0000269|PubMed:26238252}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;ovary;endometrium;oesophagus;bone;placenta;colon;germinal center;tonsil; dorsal root ganglion;subthalamic nucleus;ciliary ganglion;trigeminal ganglion; 0.12512 0.10129 0.15257911 64.60839821 1207.14793 6.58058 RMND5A 0.964712069198993 0.0352746943812311 1.32364197760619e-05 required for meiotic nuclear division 5 homolog A . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;muscle;lens;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;cerebellum peduncles;atrioventricular node;skeletal muscle;fetal liver;subthalamic nucleus;uterus corpus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.34932 0.08856 0.080983847 59.76055674 8.76956 0.32304 RMND5B 6.92213346694124e-08 0.448184547058829 0.551815383719837 required for meiotic nuclear division 5 homolog B . . . lymphoreticular;medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.16299 0.10454 -0.777005578 12.9747582 74.64616 1.80600 RMRP . . . RNA component of mitochondrial RNA processing endoribonuclease FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein- coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair. {ECO:0000269|PubMed:12628186, ECO:0000269|PubMed:16818237, ECO:0000269|PubMed:8810265}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in heart, brain, placenta, lung, liver, skeletal muscle, pancreas, spleen and thymus. Expressed in lung carcinoma cell lines but not in normal lung tissues. Isoform 2 is ubiquitously expressed and its expression is also related to tumor differentiation. Isoform 3 is ubiquitously expressed. {ECO:0000269|PubMed:10512675, ECO:0000269|PubMed:12601555, ECO:0000269|PubMed:16442775}.; . . . 0.46077 -0.119252484 44.53880632 . . RMRPP5 . . . RNA component of mitochondrial RNA processing endoribonuclease pseudogene 5 . . . . . . . . . . . RMST . . . rhabdomyosarcoma 2 associated transcript (non-protein coding) . . . . . . . . . . . RN5S1@ . . . RNA, 5S ribosomal 1q42 cluster . . . . . . . . . . . RN7SK . . . RNA, 7SK small nuclear . . . . . . . . . . . RN7SKP1 . . . RNA, 7SK small nuclear pseudogene 1 . . . . . . . . . . . RN7SKP2 . . . RNA, 7SK small nuclear pseudogene 2 . . . . . . . . . . . RN7SKP3 . . . RNA, 7SK small nuclear pseudogene 3 . . . . . . . . . . . RN7SKP4 . . . RNA, 7SK small nuclear pseudogene 4 . . . . . . . . . . . RN7SKP5 . . . RNA, 7SK small nuclear pseudogene 5 . . . . . . . . . . . RN7SKP6 . . . RNA, 7SK small nuclear pseudogene 6 . . . . . . . . . . . RN7SKP7 . . . RNA, 7SK small nuclear pseudogene 7 . . . . . . . . . . . RN7SKP8 . . . RNA, 7SK small nuclear pseudogene 8 . . . . . . . . . . . RN7SKP9 . . . RNA, 7SK small nuclear pseudogene 9 . . . . . . . . . . . RN7SKP10 . . . RNA, 7SK small nuclear pseudogene 10 . . . . . . . . . . . RN7SKP11 . . . RNA, 7SK small nuclear pseudogene 11 . . . . . . . . . . . RN7SKP12 . . . RNA, 7SK small nuclear pseudogene 12 . . . . . . . . . . . RN7SKP13 . . . RNA, 7SK small nuclear pseudogene 13 . . . . . . . . . . . RN7SKP14 . . . RNA, 7SK small nuclear pseudogene 14 . . . . . . . . . . . RN7SKP15 . . . RNA, 7SK small nuclear pseudogene 15 . . . . . . . . . . . RN7SKP16 . . . RNA, 7SK small nuclear pseudogene 16 . . . . . . . . . . . RN7SKP17 . . . RNA, 7SK small nuclear pseudogene 17 . . . . . . . . . . . RN7SKP18 . . . RNA, 7SK small nuclear pseudogene 18 . . . . . . . . . . . RN7SKP19 . . . RNA, 7SK small nuclear pseudogene 19 . . . . . . . . . . . RN7SKP20 . . . RNA, 7SK small nuclear pseudogene 20 . . . . . . . . . . . RN7SKP21 . . . RNA, 7SK small nuclear pseudogene 21 . . . . . . . . . . . RN7SKP22 . . . RNA, 7SK small nuclear pseudogene 22 . . . . . . . . . . . RN7SKP23 . . . RNA, 7SK small nuclear pseudogene 23 . . . . . . . . . . . RN7SKP24 . . . RNA, 7SK small nuclear pseudogene 24 . . . . . . . . . . . RN7SKP25 . . . RNA, 7SK small nuclear pseudogene 25 . . . . . . . . . . . RN7SKP26 . . . RNA, 7SK small nuclear pseudogene 26 . . . . . . . . . . . RN7SKP27 . . . RNA, 7SK small nuclear pseudogene 27 . . . . . . . . . . . RN7SKP28 . . . RNA, 7SK small nuclear pseudogene 28 . . . . . . . . . . . RN7SKP29 . . . RNA, 7SK small nuclear pseudogene 29 . . . . . . . . . . . RN7SKP30 . . . RNA, 7SK small nuclear pseudogene 30 . . . . . . . . . . . RN7SKP31 . . . RNA, 7SK small nuclear pseudogene 31 . . . . . . . . . . . RN7SKP32 . . . RNA, 7SK small nuclear pseudogene 32 . . . . . . . . . . . RN7SKP33 . . . RNA, 7SK small nuclear pseudogene 33 . . . . . . . . . . . RN7SKP34 . . . RNA, 7SK small nuclear pseudogene 34 . . . . . . . . . . . RN7SKP35 . . . RNA, 7SK small nuclear pseudogene 35 . . . . . . . . . . . RN7SKP36 . . . RNA, 7SK small nuclear pseudogene 36 . . . . . . . . . . . RN7SKP37 . . . RNA, 7SK small nuclear pseudogene 37 . . . . . . . . . . . RN7SKP38 . . . RNA, 7SK small nuclear pseudogene 38 . . . . . . . . . . . RN7SKP39 . . . RNA, 7SK small nuclear pseudogene 39 . . . . . . . . . . . RN7SKP40 . . . RNA, 7SK small nuclear pseudogene 40 . . . . . . . . . . . RN7SKP42 . . . RNA, 7SK small nuclear pseudogene 42 . . . . . . . . . . . RN7SKP43 . . . RNA, 7SK small nuclear pseudogene 43 . . . . . . . . . . . RN7SKP44 . . . RNA, 7SK small nuclear pseudogene 44 . . . . . . . . . . . RN7SKP45 . . . RNA, 7SK small nuclear pseudogene 45 . . . . . . . . . . . RN7SKP46 . . . RNA, 7SK small nuclear pseudogene 46 . . . . . . . . . . . RN7SKP47 . . . RNA, 7SK small nuclear pseudogene 47 . . . . . . . . . . . RN7SKP48 . . . RNA, 7SK small nuclear pseudogene 48 . . . . . . . . . . . RN7SKP49 . . . RNA, 7SK small nuclear pseudogene 49 . . . . . . . . . . . RN7SKP50 . . . RNA, 7SK small nuclear pseudogene 50 . . . . . . . . . . . RN7SKP51 . . . RNA, 7SK small nuclear pseudogene 51 . . . . . . . . . . . RN7SKP52 . . . RNA, 7SK small nuclear pseudogene 52 . . . . . . . . . . . RN7SKP53 . . . RNA, 7SK small nuclear pseudogene 53 . . . . . . . . . . . RN7SKP54 . . . RNA, 7SK small nuclear pseudogene 54 . . . . . . . . . . . RN7SKP55 . . . RNA, 7SK small nuclear pseudogene 55 . . . . . . . . . . . RN7SKP56 . . . RNA, 7SK small nuclear pseudogene 56 . . . . . . . . . . . RN7SKP57 . . . RNA, 7SK small nuclear pseudogene 57 . . . . . . . . . . . RN7SKP58 . . . RNA, 7SK small nuclear pseudogene 58 . . . . . . . . . . . RN7SKP59 . . . RNA, 7SK small nuclear pseudogene 59 . . . . . . . . . . . RN7SKP60 . . . RNA, 7SK small nuclear pseudogene 60 . . . . . . . . . . . RN7SKP61 . . . RNA, 7SK small nuclear pseudogene 61 . . . . . . . . . . . RN7SKP62 . . . RNA, 7SK small nuclear pseudogene 62 . . . . . . . . . . . RN7SKP63 . . . RNA, 7SK small nuclear pseudogene 63 . . . . . . . . . . . RN7SKP64 . . . RNA, 7SK small nuclear pseudogene 64 . . . . . . . . . . . RN7SKP65 . . . RNA, 7SK small nuclear pseudogene 65 . . . . . . . . . . . RN7SKP66 . . . RNA, 7SK small nuclear pseudogene 66 . . . . . . . . . . . RN7SKP67 . . . RNA, 7SK small nuclear pseudogene 67 . . . . . . . . . . . RN7SKP68 . . . RNA, 7SK small nuclear pseudogene 68 . . . . . . . . . . . RN7SKP69 . . . RNA, 7SK small nuclear pseudogene 69 . . . . . . . . . . . RN7SKP70 . . . RNA, 7SK small nuclear pseudogene 70 . . . . . . . . . . . RN7SKP71 . . . RNA, 7SK small nuclear pseudogene 71 . . . . . . . . . . . RN7SKP72 . . . RNA, 7SK small nuclear pseudogene 72 . . . . . . . . . . . RN7SKP73 . . . RNA, 7SK small nuclear pseudogene 73 . . . . . . . . . . . RN7SKP74 . . . RNA, 7SK small nuclear pseudogene 74 . . . . . . . . . . . RN7SKP75 . . . RNA, 7SK small nuclear pseudogene 75 . . . . . . . . . . . RN7SKP76 . . . RNA, 7SK small nuclear pseudogene 76 . . . . . . . . . . . RN7SKP77 . . . RNA, 7SK small nuclear pseudogene 77 . . . . . . . . . . . RN7SKP78 . . . RNA, 7SK small nuclear pseudogene 78 . . . . . . . . . . . RN7SKP79 . . . RNA, 7SK small nuclear pseudogene 79 . . . . . . . . . . . RN7SKP80 . . . RNA, 7SK small nuclear pseudogene 80 . . . . . . . . . . . RN7SKP81 . . . RNA, 7SK small nuclear pseudogene 81 . . . . . . . . . . . RN7SKP82 . . . RNA, 7SK small nuclear pseudogene 82 . . . . . . . . . . . RN7SKP83 . . . RNA, 7SK small nuclear pseudogene 83 . . . . . . . . . . . RN7SKP85 . . . RNA, 7SK small nuclear pseudogene 85 . . . . . . . . . . . RN7SKP86 . . . RNA, 7SK small nuclear pseudogene 86 . . . . . . . . . . . RN7SKP87 . . . RNA, 7SK small nuclear pseudogene 87 . . . . . . . . . . . RN7SKP88 . . . RNA, 7SK small nuclear pseudogene 88 . . . . . . . . . . . RN7SKP89 . . . RNA, 7SK small nuclear pseudogene 89 . . . . . . . . . . . RN7SKP90 . . . RNA, 7SK small nuclear pseudogene 90 . . . . . . . . . . . RN7SKP91 . . . RNA, 7SK small nuclear pseudogene 91 . . . . . . . . . . . RN7SKP92 . . . RNA, 7SK small nuclear pseudogene 92 . . . . . . . . . . . RN7SKP93 . . . RNA, 7SK small nuclear pseudogene 93 . . . . . . . . . . . RN7SKP94 . . . RNA, 7SK small nuclear pseudogene 94 . . . . . . . . . . . RN7SKP95 . . . RNA, 7SK small nuclear pseudogene 95 . . . . . . . . . . . RN7SKP96 . . . RNA, 7SK small nuclear pseudogene 96 . . . . . . . . . . . RN7SKP97 . . . RNA, 7SK small nuclear pseudogene 97 . . . . . . . . . . . RN7SKP98 . . . RNA, 7SK small nuclear pseudogene 98 . . . . . . . . . . . RN7SKP99 . . . RNA, 7SK small nuclear pseudogene 99 . . . . . . . . . . . RN7SKP100 . . . RNA, 7SK small nuclear pseudogene 100 . . . . . . . . . . . RN7SKP101 . . . RNA, 7SK small nuclear pseudogene 101 . . . . . . . . . . . RN7SKP102 . . . RNA, 7SK small nuclear pseudogene 102 . . . . . . . . . . . RN7SKP103 . . . RNA, 7SK small nuclear pseudogene 103 . . . . . . . . . . . RN7SKP104 . . . RNA, 7SK small nuclear pseudogene 104 . . . . . . . . . . . RN7SKP105 . . . RNA, 7SK small nuclear pseudogene 105 . . . . . . . . . . . RN7SKP106 . . . RNA, 7SK small nuclear pseudogene 106 . . . . . . . . . . . RN7SKP107 . . . RNA, 7SK small nuclear pseudogene 107 . . . . . . . . . . . RN7SKP108 . . . RNA, 7SK small nuclear pseudogene 108 . . . . . . . . . . . RN7SKP109 . . . RNA, 7SK small nuclear pseudogene 109 . . . . . . . . . . . RN7SKP110 . . . RNA, 7SK small nuclear pseudogene 110 . . . . . . . . . . . RN7SKP111 . . . RNA, 7SK small nuclear pseudogene 111 . . . . . . . . . . . RN7SKP112 . . . RNA, 7SK small nuclear pseudogene 112 . . . . . . . . . . . RN7SKP113 . . . RNA, 7SK small nuclear pseudogene 113 . . . . . . . . . . . RN7SKP114 . . . RNA, 7SK small nuclear pseudogene 114 . . . . . . . . . . . RN7SKP115 . . . RNA, 7SK small nuclear pseudogene 115 . . . . . . . . . . . RN7SKP116 . . . RNA, 7SK small nuclear pseudogene 116 . . . . . . . . . . . RN7SKP117 . . . RNA, 7SK small nuclear pseudogene 117 . . . . . . . . . . . RN7SKP118 . . . RNA, 7SK small nuclear pseudogene 118 . . . . . . . . . . . RN7SKP119 . . . RNA, 7SK small nuclear pseudogene 119 . . . . . . . . . . . RN7SKP120 . . . RNA, 7SK small nuclear pseudogene 120 . . . . . . . . . . . RN7SKP121 . . . RNA, 7SK small nuclear pseudogene 121 . . . . . . . . . . . RN7SKP122 . . . RNA, 7SK small nuclear pseudogene 122 . . . . . . . . . . . RN7SKP123 . . . RNA, 7SK small nuclear pseudogene 123 . . . . . . . . . . . RN7SKP124 . . . RNA, 7SK small nuclear pseudogene 124 . . . . . . . . . . . RN7SKP125 . . . RNA, 7SK small nuclear pseudogene 125 . . . . . . . . . . . RN7SKP126 . . . RNA, 7SK small nuclear pseudogene 126 . . . . . . . . . . . RN7SKP127 . . . RNA, 7SK small nuclear pseudogene 127 . . . . . . . . . . . RN7SKP128 . . . RNA, 7SK small nuclear pseudogene 128 . . . . . . . . . . . RN7SKP129 . . . RNA, 7SK small nuclear pseudogene 129 . . . . . . . . . . . RN7SKP130 . . . RNA, 7SK small nuclear pseudogene 130 . . . . . . . . . . . RN7SKP131 . . . RNA, 7SK small nuclear pseudogene 131 . . . . . . . . . . . RN7SKP132 . . . RNA, 7SK small nuclear pseudogene 132 . . . . . . . . . . . RN7SKP133 . . . RNA, 7SK small nuclear pseudogene 133 . . . . . . . . . . . RN7SKP134 . . . RNA, 7SK small nuclear pseudogene 134 . . . . . . . . . . . RN7SKP135 . . . RNA, 7SK small nuclear pseudogene 135 . . . . . . . . . . . RN7SKP136 . . . RNA, 7SK small nuclear pseudogene 136 . . . . . . . . . . . RN7SKP137 . . . RNA, 7SK small nuclear pseudogene 137 . . . . . . . . . . . RN7SKP139 . . . RNA, 7SK small nuclear pseudogene 139 . . . . . . . . . . . RN7SKP140 . . . RNA, 7SK small nuclear pseudogene 140 . . . . . . . . . . . RN7SKP141 . . . RNA, 7SK small nuclear pseudogene 141 . . . . . . . . . . . RN7SKP142 . . . RNA, 7SK small nuclear pseudogene 142 . . . . . . . . . . . RN7SKP143 . . . RNA, 7SK small nuclear pseudogene 143 . . . . . . . . . . . RN7SKP144 . . . RNA, 7SK small nuclear pseudogene 144 . . . . . . . . . . . RN7SKP145 . . . RNA, 7SK small nuclear pseudogene 145 . . . . . . . . . . . RN7SKP146 . . . RNA, 7SK small nuclear pseudogene 146 . . . . . . . . . . . RN7SKP147 . . . RNA, 7SK small nuclear pseudogene 147 . . . . . . . . . . . RN7SKP148 . . . RNA, 7SK small nuclear pseudogene 148 . . . . . . . . . . . RN7SKP149 . . . RNA, 7SK small nuclear pseudogene 149 . . . . . . . . . . . RN7SKP150 . . . RNA, 7SK small nuclear pseudogene 150 . . . . . . . . . . . RN7SKP151 . . . RNA, 7SK small nuclear pseudogene 151 . . . . . . . . . . . RN7SKP152 . . . RNA, 7SK small nuclear pseudogene 152 . . . . . . . . . . . RN7SKP153 . . . RNA, 7SK small nuclear pseudogene 153 . . . . . . . . . . . RN7SKP154 . . . RNA, 7SK small nuclear pseudogene 154 . . . . . . . . . . . RN7SKP155 . . . RNA, 7SK small nuclear pseudogene 155 . . . . . . . . . . . RN7SKP156 . . . RNA, 7SK small nuclear pseudogene 156 . . . . . . . . . . . RN7SKP157 . . . RNA, 7SK small nuclear pseudogene 157 . . . . . . . . . . . RN7SKP158 . . . RNA, 7SK small nuclear pseudogene 158 . . . . . . . . . . . RN7SKP159 . . . RNA, 7SK small nuclear pseudogene 159 . . . . . . . . . . . RN7SKP160 . . . RNA, 7SK small nuclear pseudogene 160 . . . . . . . . . . . RN7SKP161 . . . RNA, 7SK small nuclear pseudogene 161 . . . . . . . . . . . RN7SKP162 . . . RNA, 7SK small nuclear pseudogene 162 . . . . . . . . . . . RN7SKP163 . . . RNA, 7SK small nuclear pseudogene 163 . . . . . . . . . . . RN7SKP164 . . . RNA, 7SK small nuclear pseudogene 164 . . . . . . . . . . . RN7SKP165 . . . RNA, 7SK small nuclear pseudogene 165 . . . . . . . . . . . RN7SKP166 . . . RNA, 7SK small nuclear pseudogene 166 . . . . . . . . . . . RN7SKP167 . . . RNA, 7SK small nuclear pseudogene 167 . . . . . . . . . . . RN7SKP168 . . . RNA, 7SK small nuclear pseudogene 168 . . . . . . . . . . . RN7SKP169 . . . RNA, 7SK small nuclear pseudogene 169 . . . . . . . . . . . RN7SKP170 . . . RNA, 7SK small nuclear pseudogene 170 . . . . . . . . . . . RN7SKP171 . . . RNA, 7SK small nuclear pseudogene 171 . . . . . . . . . . . RN7SKP172 . . . RNA, 7SK small nuclear pseudogene 172 . . . . . . . . . . . RN7SKP173 . . . RNA, 7SK small nuclear pseudogene 173 . . . . . . . . . . . RN7SKP174 . . . RNA, 7SK small nuclear pseudogene 174 . . . . . . . . . . . RN7SKP175 . . . RNA, 7SK small nuclear pseudogene 175 . . . . . . . . . . . RN7SKP176 . . . RNA, 7SK small nuclear pseudogene 176 . . . . . . . . . . . RN7SKP177 . . . RNA, 7SK small nuclear pseudogene 177 . . . . . . . . . . . RN7SKP178 . . . RNA, 7SK small nuclear pseudogene 178 . . . . . . . . . . . RN7SKP179 . . . RNA, 7SK small nuclear pseudogene 179 . . . . . . . . . . . RN7SKP180 . . . RNA, 7SK small nuclear pseudogene 180 . . . . . . . . . . . RN7SKP181 . . . RNA, 7SK small nuclear pseudogene 181 . . . . . . . . . . . RN7SKP182 . . . RNA, 7SK small nuclear pseudogene 182 . . . . . . . . . . . RN7SKP183 . . . RNA, 7SK small nuclear pseudogene 183 . . . . . . . . . . . RN7SKP184 . . . RNA, 7SK small nuclear pseudogene 184 . . . . . . . . . . . RN7SKP185 . . . RNA, 7SK small nuclear pseudogene 185 . . . . . . . . . . . RN7SKP186 . . . RNA, 7SK small nuclear pseudogene 186 . . . . . . . . . . . RN7SKP187 . . . RNA, 7SK small nuclear pseudogene 187 . . . . . . . . . . . RN7SKP188 . . . RNA, 7SK small nuclear pseudogene 188 . . . . . . . . . . . RN7SKP189 . . . RNA, 7SK small nuclear pseudogene 189 . . . . . . . . . . . RN7SKP190 . . . RNA, 7SK small nuclear pseudogene 190 . . . . . . . . . . . RN7SKP191 . . . RNA, 7SK small nuclear pseudogene 191 . . . . . . . . . . . RN7SKP192 . . . RNA, 7SK small nuclear pseudogene 192 . . . . . . . . . . . RN7SKP193 . . . RNA, 7SK small nuclear pseudogene 193 . . . . . . . . . . . RN7SKP194 . . . RNA, 7SK small nuclear pseudogene 194 . . . . . . . . . . . RN7SKP195 . . . RNA, 7SK small nuclear pseudogene 195 . . . . . . . . . . . RN7SKP196 . . . RNA, 7SK small nuclear pseudogene 196 . . . . . . . . . . . RN7SKP197 . . . RNA, 7SK small nuclear pseudogene 197 . . . . . . . . . . . RN7SKP198 . . . RNA, 7SK small nuclear pseudogene 198 . . . . . . . . . . . RN7SKP199 . . . RNA, 7SK small nuclear pseudogene 199 . . . . . . . . . . . RN7SKP200 . . . RNA, 7SK small nuclear pseudogene 200 . . . . . . . . . . . RN7SKP202 . . . RNA, 7SK small nuclear pseudogene 202 . . . . . . . . . . . RN7SKP203 . . . RNA, 7SK small nuclear pseudogene 203 . . . . . . . . . . . RN7SKP204 . . . RNA, 7SK small nuclear pseudogene 204 . . . . . . . . . . . RN7SKP205 . . . RNA, 7SK small nuclear pseudogene 205 . . . . . . . . . . . RN7SKP206 . . . RNA, 7SK small nuclear pseudogene 206 . . . . . . . . . . . RN7SKP207 . . . RNA, 7SK small nuclear pseudogene 207 . . . . . . . . . . . RN7SKP208 . . . RNA, 7SK small nuclear pseudogene 208 . . . . . . . . . . . RN7SKP209 . . . RNA, 7SK small nuclear pseudogene 209 . . . . . . . . . . . RN7SKP210 . . . RNA, 7SK small nuclear pseudogene 210 . . . . . . . . . . . RN7SKP211 . . . RNA, 7SK small nuclear pseudogene 211 . . . . . . . . . . . RN7SKP212 . . . RNA, 7SK small nuclear pseudogene 212 . . . . . . . . . . . RN7SKP213 . . . RNA, 7SK small nuclear pseudogene 213 . . . . . . . . . . . RN7SKP214 . . . RNA, 7SK small nuclear pseudogene 214 . . . . . . . . . . . RN7SKP216 . . . RNA, 7SK small nuclear pseudogene 216 . . . . . . . . . . . RN7SKP217 . . . RNA, 7SK small nuclear pseudogene 217 . . . . . . . . . . . RN7SKP218 . . . RNA, 7SK small nuclear pseudogene 218 . . . . . . . . . . . RN7SKP219 . . . RNA, 7SK small nuclear pseudogene 219 . . . . . . . . . . . RN7SKP220 . . . RNA, 7SK small nuclear pseudogene 220 . . . . . . . . . . . RN7SKP221 . . . RNA, 7SK small nuclear pseudogene 221 . . . . . . . . . . . RN7SKP222 . . . RNA, 7SK small nuclear pseudogene 222 . . . . . . . . . . . RN7SKP223 . . . RNA, 7SK small nuclear pseudogene 223 . . . . . . . . . . . RN7SKP224 . . . RNA, 7SK small nuclear pseudogene 224 . . . . . . . . . . . RN7SKP225 . . . RNA, 7SK small nuclear pseudogene 225 . . . . . . . . . . . RN7SKP226 . . . RNA, 7SK small nuclear pseudogene 226 . . . . . . . . . . . RN7SKP227 . . . RNA, 7SK small nuclear pseudogene 227 . . . . . . . . . . . RN7SKP228 . . . RNA, 7SK small nuclear pseudogene 228 . . . . . . . . . . . RN7SKP229 . . . RNA, 7SK small nuclear pseudogene 229 . . . . . . . . . . . RN7SKP230 . . . RNA, 7SK small nuclear pseudogene 230 . . . . . . . . . . . RN7SKP231 . . . RNA, 7SK small nuclear pseudogene 231 . . . . . . . . . . . RN7SKP232 . . . RNA, 7SK small nuclear pseudogene 232 . . . . . . . . . . . RN7SKP233 . . . RNA, 7SK small nuclear pseudogene 233 . . . . . . . . . . . RN7SKP234 . . . RNA, 7SK small nuclear pseudogene 234 . . . . . . . . . . . RN7SKP235 . . . RNA, 7SK small nuclear pseudogene 235 . . . . . . . . . . . RN7SKP236 . . . RNA, 7SK small nuclear pseudogene 236 . . . . . . . . . . . RN7SKP237 . . . RNA, 7SK small nuclear pseudogene 237 . . . . . . . . . . . RN7SKP238 . . . RNA, 7SK small nuclear pseudogene 238 . . . . . . . . . . . RN7SKP239 . . . RNA, 7SK small nuclear pseudogene 239 . . . . . . . . . . . RN7SKP240 . . . RNA, 7SK small nuclear pseudogene 240 . . . . . . . . . . . RN7SKP241 . . . RNA, 7SK small nuclear pseudogene 241 . . . . . . . . . . . RN7SKP242 . . . RNA, 7SK small nuclear pseudogene 242 . . . . . . . . . . . RN7SKP243 . . . RNA, 7SK small nuclear pseudogene 243 . . . . . . . . . . . RN7SKP244 . . . RNA, 7SK small nuclear pseudogene 244 . . . . . . . . . . . RN7SKP245 . . . RNA, 7SK small nuclear pseudogene 245 . . . . . . . . . . . RN7SKP246 . . . RNA, 7SK small nuclear pseudogene 246 . . . . . . . . . . . RN7SKP247 . . . RNA, 7SK small nuclear pseudogene 247 . . . . . . . . . . . RN7SKP248 . . . RNA, 7SK small nuclear pseudogene 248 . . . . . . . . . . . RN7SKP249 . . . RNA, 7SK small nuclear pseudogene 249 . . . . . . . . . . . RN7SKP250 . . . RNA, 7SK small nuclear pseudogene 250 . . . . . . . . . . . RN7SKP251 . . . RNA, 7SK small nuclear pseudogene 251 . . . . . . . . . . . RN7SKP252 . . . RNA, 7SK small nuclear pseudogene 252 . . . . . . . . . . . RN7SKP253 . . . RNA, 7SK small nuclear pseudogene 253 . . . . . . . . . . . RN7SKP254 . . . RNA, 7SK small nuclear pseudogene 254 . . . . . . . . . . . RN7SKP255 . . . RNA, 7SK small nuclear pseudogene 255 . . . . . . . . . . . RN7SKP256 . . . RNA, 7SK small nuclear pseudogene 256 . . . . . . . . . . . RN7SKP257 . . . RNA, 7SK small nuclear pseudogene 257 . . . . . . . . . . . RN7SKP258 . . . RNA, 7SK small nuclear pseudogene 258 . . . . . . . . . . . RN7SKP259 . . . RNA, 7SK small nuclear pseudogene 259 . . . . . . . . . . . RN7SKP260 . . . RNA, 7SK small nuclear pseudogene 260 . . . . . . . . . . . RN7SKP261 . . . RNA, 7SK small nuclear pseudogene 261 . . . . . . . . . . . RN7SKP262 . . . RNA, 7SK small nuclear pseudogene 262 . . . . . . . . . . . RN7SKP263 . . . RNA, 7SK small nuclear pseudogene 263 . . . . . . . . . . . RN7SKP264 . . . RNA, 7SK small nuclear pseudogene 264 . . . . . . . . . . . RN7SKP265 . . . RNA, 7SK small nuclear pseudogene 265 . . . . . . . . . . . RN7SKP266 . . . RNA, 7SK small nuclear pseudogene 266 . . . . . . . . . . . RN7SKP267 . . . RNA, 7SK small nuclear pseudogene 267 . . . . . . . . . . . RN7SKP268 . . . RNA, 7SK small nuclear pseudogene 268 . . . . . . . . . . . RN7SKP269 . . . RNA, 7SK small nuclear pseudogene 269 . . . . . . . . . . . RN7SKP270 . . . RNA, 7SK small nuclear pseudogene 270 . . . . . . . . . . . RN7SKP271 . . . RNA, 7SK small nuclear pseudogene 271 . . . . . . . . . . . RN7SKP272 . . . RNA, 7SK small nuclear pseudogene 272 . . . . . . . . . . . RN7SKP273 . . . RNA, 7SK small nuclear pseudogene 273 . . . . . . . . . . . RN7SKP275 . . . RNA, 7SK small nuclear pseudogene 275 . . . . . . . . . . . RN7SKP276 . . . RNA, 7SK small nuclear pseudogene 276 . . . . . . . . . . . RN7SKP277 . . . RNA, 7SK small nuclear pseudogene 277 . . . . . . . . . . . RN7SKP278 . . . RNA, 7SK small nuclear pseudogene 278 . . . . . . . . . . . RN7SKP279 . . . RNA, 7SK small nuclear pseudogene 279 . . . . . . . . . . . RN7SKP280 . . . RNA, 7SK small nuclear pseudogene 280 . . . . . . . . . . . RN7SKP281 . . . RNA, 7SK small nuclear pseudogene 281 . . . . . . . . . . . RN7SKP282 . . . RNA, 7SK small nuclear pseudogene 282 . . . . . . . . . . . RN7SKP283 . . . RNA, 7SK small nuclear pseudogene 283 . . . . . . . . . . . RN7SKP284 . . . RNA, 7SK small nuclear pseudogene 284 . . . . . . . . . . . RN7SKP285 . . . RNA, 7SK small nuclear pseudogene 285 . . . . . . . . . . . RN7SKP286 . . . RNA, 7SK small nuclear pseudogene 286 . . . . . . . . . . . RN7SKP287 . . . RNA, 7SK small nuclear pseudogene 287 . . . . . . . . . . . RN7SKP288 . . . RNA, 7SK small nuclear pseudogene 288 . . . . . . . . . . . RN7SKP289 . . . RNA, 7SK small nuclear pseudogene 289 . . . . . . . . . . . RN7SKP290 . . . RNA, 7SK small nuclear pseudogene 290 . . . . . . . . . . . RN7SKP291 . . . RNA, 7SK small nuclear pseudogene 291 . . . . . . . . . . . RN7SKP292 . . . RNA, 7SK small nuclear pseudogene 292 . . . . . . . . . . . RN7SKP293 . . . RNA, 7SK small nuclear pseudogene 293 . . . . . . . . . . . RN7SKP294 . . . RNA, 7SK small nuclear pseudogene 294 . . . . . . . . . . . RN7SKP295 . . . RNA, 7SK small nuclear pseudogene 295 . . . . . . . . . . . RN7SKP296 . . . RNA, 7SK small nuclear pseudogene 296 . . . . . . . . . . . RN7SKP297 . . . RNA, 7SK small nuclear pseudogene 297 . . . . . . . . . . . RN7SKP298 . . . RNA, 7SK small nuclear pseudogene 298 . . . . . . . . . . . RN7SKP299 . . . RNA, 7SK small nuclear pseudogene 299 . . . . . . . . . . . RN7SL1 . . . RNA, 7SL, cytoplasmic 1 . . . . . . . . . . . RN7SL2 . . . RNA, 7SL, cytoplasmic 2 . . . . . . . . . . . RN7SL3 . . . RNA, 7SL, cytoplasmic 3 . . . . . . . . . . . RN7SL4P . . . RNA, 7SL, cytoplasmic 4, pseudogene . . . . . . . . . . . RN7SL5P . . . RNA, 7SL, cytoplasmic 5, pseudogene . . . . . . . . . . . RN7SL6P . . . RNA, 7SL, cytoplasmic 6, pseudogene . . . . . . . . . . . RN7SL7P . . . RNA, 7SL, cytoplasmic 7, pseudogene . . . . . . . . . . . RN7SL8P . . . RNA, 7SL, cytoplasmic 8, pseudogene . . . . . . . . . . . RN7SL11P . . . RNA, 7SL, cytoplasmic 11, pseudogene . . . . . . . . . . . RN7SL12P . . . RNA, 7SL, cytoplasmic 12, pseudogene . . . . . . . . . . . RN7SL14P . . . RNA, 7SL, cytoplasmic 14, pseudogene . . . . . . . . . . . RN7SL15P . . . RNA, 7SL, cytoplasmic 15, pseudogene . . . . . . . . . . . RN7SL16P . . . RNA, 7SL, cytoplasmic 16, pseudogene . . . . . . . . . . . RN7SL18P . . . RNA, 7SL, cytoplasmic 18, pseudogene . . . . . . . . . . . RN7SL19P . . . RNA, 7SL, cytoplasmic 19, pseudogene . . . . . . . . . . . RN7SL20P . . . RNA, 7SL, cytoplasmic 20, pseudogene . . . . . . . . . . . RN7SL22P . . . RNA, 7SL, cytoplasmic 22, pseudogene . . . . . . . . . . . RN7SL23P . . . RNA, 7SL, cytoplasmic 23, pseudogene . . . . . . . . . . . RN7SL25P . . . RNA, 7SL, cytoplasmic 25, pseudogene . . . . . . . . . . . RN7SL26P . . . RNA, 7SL, cytoplasmic 26, pseudogene . . . . . . . . . . . RN7SL28P . . . RNA, 7SL, cytoplasmic 28, pseudogene . . . . . . . . . . . RN7SL30P . . . RNA, 7SL, cytoplasmic 30, pseudogene . . . . . . . . . . . RN7SL32P . . . RNA, 7SL, cytoplasmic 32, pseudogene . . . . . . . . . . . RN7SL33P . . . RNA, 7SL, cytoplasmic 33, pseudogene . . . . . . . . . . . RN7SL34P . . . RNA, 7SL, cytoplasmic 34, pseudogene . . . . . . . . . . . RN7SL35P . . . RNA, 7SL, cytoplasmic 35, pseudogene . . . . . . . . . . . RN7SL36P . . . RNA, 7SL, cytoplasmic 36, pseudogene . . . . . . . . . . . RN7SL37P . . . RNA, 7SL, cytoplasmic 37, pseudogene . . . . . . . . . . . RN7SL38P . . . RNA, 7SL, cytoplasmic 38, pseudogene . . . . . . . . . . . RN7SL39P . . . RNA, 7SL, cytoplasmic 39, pseudogene . . . . . . . . . . . RN7SL40P . . . RNA, 7SL, cytoplasmic 40, pseudogene . . . . . . . . . . . RN7SL41P . . . RNA, 7SL, cytoplasmic 41, pseudogene . . . . . . . . . . . RN7SL42P . . . RNA, 7SL, cytoplasmic 42, pseudogene . . . . . . . . . . . RN7SL43P . . . RNA, 7SL, cytoplasmic 43, pseudogene . . . . . . . . . . . RN7SL44P . . . RNA, 7SL, cytoplasmic 44, pseudogene . . . . . . . . . . . RN7SL45P . . . RNA, 7SL, cytoplasmic 45, pseudogene . . . . . . . . . . . RN7SL47P . . . RNA, 7SL, cytoplasmic 47, pseudogene . . . . . . . . . . . RN7SL48P . . . RNA, 7SL, cytoplasmic 48, pseudogene . . . . . . . . . . . RN7SL49P . . . RNA, 7SL, cytoplasmic 49, pseudogene . . . . . . . . . . . RN7SL50P . . . RNA, 7SL, cytoplasmic 50, pseudogene . . . . . . . . . . . RN7SL51P . . . RNA, 7SL, cytoplasmic 51, pseudogene . . . . . . . . . . . RN7SL52P . . . RNA, 7SL, cytoplasmic 52, pseudogene . . . . . . . . . . . RN7SL55P . . . RNA, 7SL, cytoplasmic 55, pseudogene . . . . . . . . . . . RN7SL57P . . . RNA, 7SL, cytoplasmic 57, pseudogene . . . . . . . . . . . RN7SL58P . . . RNA, 7SL, cytoplasmic 58, pseudogene . . . . . . . . . . . RN7SL60P . . . RNA, 7SL, cytoplasmic 60, pseudogene . . . . . . . . . . . RN7SL62P . . . RNA, 7SL, cytoplasmic 62, pseudogene . . . . . . . . . . . RN7SL63P . . . RNA, 7SL, cytoplasmic 63, pseudogene . . . . . . . . . . . RN7SL65P . . . RNA, 7SL, cytoplasmic 65, pseudogene . . . . . . . . . . . RN7SL66P . . . RNA, 7SL, cytoplasmic 66, pseudogene . . . . . . . . . . . RN7SL67P . . . RNA, 7SL, cytoplasmic 67, pseudogene . . . . . . . . . . . RN7SL68P . . . RNA, 7SL, cytoplasmic 68, pseudogene . . . . . . . . . . . RN7SL69P . . . RNA, 7SL, cytoplasmic 69, pseudogene . . . . . . . . . . . RN7SL70P . . . RNA, 7SL, cytoplasmic 70, pseudogene . . . . . . . . . . . RN7SL72P . . . RNA, 7SL, cytoplasmic 72, pseudogene . . . . . . . . . . . RN7SL73P . . . RNA, 7SL, cytoplasmic 73, pseudogene . . . . . . . . . . . RN7SL74P . . . RNA, 7SL, cytoplasmic 74, pseudogene . . . . . . . . . . . RN7SL75P . . . RNA, 7SL, cytoplasmic 75, pseudogene . . . . . . . . . . . RN7SL76P . . . RNA, 7SL, cytoplasmic 76, pseudogene . . . . . . . . . . . RN7SL77P . . . RNA, 7SL, cytoplasmic 77, pseudogene . . . . . . . . . . . RN7SL78P . . . RNA, 7SL, cytoplasmic 78, pseudogene . . . . . . . . . . . RN7SL79P . . . RNA, 7SL, cytoplasmic 79, pseudogene . . . . . . . . . . . RN7SL81P . . . RNA, 7SL, cytoplasmic 81, pseudogene . . . . . . . . . . . RN7SL82P . . . RNA, 7SL, cytoplasmic 82, pseudogene . . . . . . . . . . . RN7SL83P . . . RNA, 7SL, cytoplasmic 83, pseudogene . . . . . . . . . . . RN7SL87P . . . RNA, 7SL, cytoplasmic 87, pseudogene . . . . . . . . . . . RN7SL88P . . . RNA, 7SL, cytoplasmic 88, pseudogene . . . . . . . . . . . RN7SL89P . . . RNA, 7SL, cytoplasmic 89, pseudogene . . . . . . . . . . . RN7SL91P . . . RNA, 7SL, cytoplasmic 91, pseudogene . . . . . . . . . . . RN7SL92P . . . RNA, 7SL, cytoplasmic 92, pseudogene . . . . . . . . . . . RN7SL93P . . . RNA, 7SL, cytoplasmic 93, pseudogene . . . . . . . . . . . RN7SL96P . . . RNA, 7SL, cytoplasmic 96, pseudogene . . . . . . . . . . . RN7SL97P . . . RNA, 7SL, cytoplasmic 97, pseudogene . . . . . . . . . . . RN7SL98P . . . RNA, 7SL, cytoplasmic 98, pseudogene . . . . . . . . . . . RN7SL100P . . . RNA, 7SL, cytoplasmic 100, pseudogene . . . . . . . . . . . RN7SL101P . . . RNA, 7SL, cytoplasmic 101, pseudogene . . . . . . . . . . . RN7SL104P . . . RNA, 7SL, cytoplasmic 104, pseudogene . . . . . . . . . . . RN7SL105P . . . RNA, 7SL, cytoplasmic 105, pseudogene . . . . . . . . . . . RN7SL106P . . . RNA, 7SL, cytoplasmic 106, pseudogene . . . . . . . . . . . RN7SL107P . . . RNA, 7SL, cytoplasmic 107, pseudogene . . . . . . . . . . . RN7SL108P . . . RNA, 7SL, cytoplasmic 108, pseudogene . . . . . . . . . . . RN7SL110P . . . RNA, 7SL, cytoplasmic 110, pseudogene . . . . . . . . . . . RN7SL111P . . . RNA, 7SL, cytoplasmic 111, pseudogene . . . . . . . . . . . RN7SL113P . . . RNA, 7SL, cytoplasmic 113, pseudogene . . . . . . . . . . . RN7SL116P . . . RNA, 7SL, cytoplasmic 116, pseudogene . . . . . . . . . . . RN7SL117P . . . RNA, 7SL, cytoplasmic 117, pseudogene . . . . . . . . . . . RN7SL118P . . . RNA, 7SL, cytoplasmic 118, pseudogene . . . . . . . . . . . RN7SL120P . . . RNA, 7SL, cytoplasmic 120, pseudogene . . . . . . . . . . . RN7SL121P . . . RNA, 7SL, cytoplasmic 121, pseudogene . . . . . . . . . . . RN7SL122P . . . RNA, 7SL, cytoplasmic 122, pseudogene . . . . . . . . . . . RN7SL123P . . . RNA, 7SL, cytoplasmic 123, pseudogene . . . . . . . . . . . RN7SL124P . . . RNA, 7SL, cytoplasmic 124, pseudogene . . . . . . . . . . . RN7SL125P . . . RNA, 7SL, cytoplasmic 125, pseudogene . . . . . . . . . . . RN7SL126P . . . RNA, 7SL, cytoplasmic 126, pseudogene . . . . . . . . . . . RN7SL127P . . . RNA, 7SL, cytoplasmic 127, pseudogene . . . . . . . . . . . RN7SL128P . . . RNA, 7SL, cytoplasmic 128, pseudogene . . . . . . . . . . . RN7SL130P . . . RNA, 7SL, cytoplasmic 130, pseudogene . . . . . . . . . . . RN7SL131P . . . RNA, 7SL, cytoplasmic 131, pseudogene . . . . . . . . . . . RN7SL132P . . . RNA, 7SL, cytoplasmic 132, pseudogene . . . . . . . . . . . RN7SL134P . . . RNA, 7SL, cytoplasmic 134, pseudogene . . . . . . . . . . . RN7SL135P . . . RNA, 7SL, cytoplasmic 135, pseudogene . . . . . . . . . . . RN7SL138P . . . RNA, 7SL, cytoplasmic 138, pseudogene . . . . . . . . . . . RN7SL140P . . . RNA, 7SL, cytoplasmic 140, pseudogene . . . . . . . . . . . RN7SL141P . . . RNA, 7SL, cytoplasmic 141, pseudogene . . . . . . . . . . . RN7SL143P . . . RNA, 7SL, cytoplasmic 143, pseudogene . . . . . . . . . . . RN7SL144P . . . RNA, 7SL, cytoplasmic 144, pseudogene . . . . . . . . . . . RN7SL145P . . . RNA, 7SL, cytoplasmic 145, pseudogene . . . . . . . . . . . RN7SL146P . . . RNA, 7SL, cytoplasmic 146, pseudogene . . . . . . . . . . . RN7SL147P . . . RNA, 7SL, cytoplasmic 147, pseudogene . . . . . . . . . . . RN7SL148P . . . RNA, 7SL, cytoplasmic 148, pseudogene . . . . . . . . . . . RN7SL149P . . . RNA, 7SL, cytoplasmic 149, pseudogene . . . . . . . . . . . RN7SL150P . . . RNA, 7SL, cytoplasmic 150, pseudogene . . . . . . . . . . . RN7SL151P . . . RNA, 7SL, cytoplasmic 151, pseudogene . . . . . . . . . . . RN7SL152P . . . RNA, 7SL, cytoplasmic 152, pseudogene . . . . . . . . . . . RN7SL153P . . . RNA, 7SL, cytoplasmic 153, pseudogene . . . . . . . . . . . RN7SL154P . . . RNA, 7SL, cytoplasmic 154, pseudogene . . . . . . . . . . . RN7SL155P . . . RNA, 7SL, cytoplasmic 155, pseudogene . . . . . . . . . . . RN7SL156P . . . RNA, 7SL, cytoplasmic 156, pseudogene . . . . . . . . . . . RN7SL159P . . . RNA, 7SL, cytoplasmic 159, pseudogene . . . . . . . . . . . RN7SL160P . . . RNA, 7SL, cytoplasmic 160, pseudogene . . . . . . . . . . . RN7SL162P . . . RNA, 7SL, cytoplasmic 162, pseudogene . . . . . . . . . . . RN7SL163P . . . RNA, 7SL, cytoplasmic 163, pseudogene . . . . . . . . . . . RN7SL164P . . . RNA, 7SL, cytoplasmic 164, pseudogene . . . . . . . . . . . RN7SL165P . . . RNA, 7SL, cytoplasmic 165, pseudogene . . . . . . . . . . . RN7SL166P . . . RNA, 7SL, cytoplasmic 166, pseudogene . . . . . . . . . . . RN7SL167P . . . RNA, 7SL, cytoplasmic 167, pseudogene . . . . . . . . . . . RN7SL168P . . . RNA, 7SL, cytoplasmic 168, pseudogene . . . . . . . . . . . RN7SL169P . . . RNA, 7SL, cytoplasmic 169, pseudogene . . . . . . . . . . . RN7SL170P . . . RNA, 7SL, cytoplasmic 170, pseudogene . . . . . . . . . . . RN7SL172P . . . RNA, 7SL, cytoplasmic 172, pseudogene . . . . . . . . . . . RN7SL173P . . . RNA, 7SL, cytoplasmic 173, pseudogene . . . . . . . . . . . RN7SL174P . . . RNA, 7SL, cytoplasmic 174, pseudogene . . . . . . . . . . . RN7SL176P . . . RNA, 7SL, cytoplasmic 176, pseudogene . . . . . . . . . . . RN7SL177P . . . RNA, 7SL, cytoplasmic 177, pseudogene . . . . . . . . . . . RN7SL178P . . . RNA, 7SL, cytoplasmic 178, pseudogene . . . . . . . . . . . RN7SL180P . . . RNA, 7SL, cytoplasmic 180, pseudogene . . . . . . . . . . . RN7SL181P . . . RNA, 7SL, cytoplasmic 181, pseudogene . . . . . . . . . . . RN7SL182P . . . RNA, 7SL, cytoplasmic 182, pseudogene . . . . . . . . . . . RN7SL183P . . . RNA, 7SL, cytoplasmic 183, pseudogene . . . . . . . . . . . RN7SL184P . . . RNA, 7SL, cytoplasmic 184, pseudogene . . . . . . . . . . . RN7SL185P . . . RNA, 7SL, cytoplasmic 185, pseudogene . . . . . . . . . . . RN7SL186P . . . RNA, 7SL, cytoplasmic 186, pseudogene . . . . . . . . . . . RN7SL187P . . . RNA, 7SL, cytoplasmic 187, pseudogene . . . . . . . . . . . RN7SL188P . . . RNA, 7SL, cytoplasmic 188, pseudogene . . . . . . . . . . . RN7SL189P . . . RNA, 7SL, cytoplasmic 189, pseudogene . . . . . . . . . . . RN7SL190P . . . RNA, 7SL, cytoplasmic 190, pseudogene . . . . . . . . . . . RN7SL191P . . . RNA, 7SL, cytoplasmic 191, pseudogene . . . . . . . . . . . RN7SL192P . . . RNA, 7SL, cytoplasmic 192, pseudogene . . . . . . . . . . . RN7SL193P . . . RNA, 7SL, cytoplasmic 193, pseudogene . . . . . . . . . . . RN7SL196P . . . RNA, 7SL, cytoplasmic 196, pseudogene . . . . . . . . . . . RN7SL197P . . . RNA, 7SL, cytoplasmic 197, pseudogene . . . . . . . . . . . RN7SL198P . . . RNA, 7SL, cytoplasmic 198, pseudogene . . . . . . . . . . . RN7SL199P . . . RNA, 7SL, cytoplasmic 199, pseudogene . . . . . . . . . . . RN7SL200P . . . RNA, 7SL, cytoplasmic 200, pseudogene . . . . . . . . . . . RN7SL201P . . . RNA, 7SL, cytoplasmic 201, pseudogene . . . . . . . . . . . RN7SL202P . . . RNA, 7SL, cytoplasmic 202, pseudogene . . . . . . . . . . . RN7SL203P . . . RNA, 7SL, cytoplasmic 203, pseudogene . . . . . . . . . . . RN7SL204P . . . RNA, 7SL, cytoplasmic 204, pseudogene . . . . . . . . . . . RN7SL205P . . . RNA, 7SL, cytoplasmic 205, pseudogene . . . . . . . . . . . RN7SL208P . . . RNA, 7SL, cytoplasmic 208, pseudogene . . . . . . . . . . . RN7SL209P . . . RNA, 7SL, cytoplasmic 209, pseudogene . . . . . . . . . . . RN7SL210P . . . RNA, 7SL, cytoplasmic 210, pseudogene . . . . . . . . . . . RN7SL211P . . . RNA, 7SL, cytoplasmic 211, pseudogene . . . . . . . . . . . RN7SL213P . . . RNA, 7SL, cytoplasmic 213, pseudogene . . . . . . . . . . . RN7SL214P . . . RNA, 7SL, cytoplasmic 214, pseudogene . . . . . . . . . . . RN7SL215P . . . RNA, 7SL, cytoplasmic 215, pseudogene . . . . . . . . . . . RN7SL216P . . . RNA, 7SL, cytoplasmic 216, pseudogene . . . . . . . . . . . RN7SL217P . . . RNA, 7SL, cytoplasmic 217, pseudogene . . . . . . . . . . . RN7SL218P . . . RNA, 7SL, cytoplasmic 218, pseudogene . . . . . . . . . . . RN7SL219P . . . RNA, 7SL, cytoplasmic 219, pseudogene . . . . . . . . . . . RN7SL220P . . . RNA, 7SL, cytoplasmic 220, pseudogene . . . . . . . . . . . RN7SL221P . . . RNA, 7SL, cytoplasmic 221, pseudogene . . . . . . . . . . . RN7SL222P . . . RNA, 7SL, cytoplasmic 222, pseudogene . . . . . . . . . . . RN7SL223P . . . RNA, 7SL, cytoplasmic 223, pseudogene . . . . . . . . . . . RN7SL225P . . . RNA, 7SL, cytoplasmic 225, pseudogene . . . . . . . . . . . RN7SL228P . . . RNA, 7SL, cytoplasmic 228, pseudogene . . . . . . . . . . . RN7SL229P . . . RNA, 7SL, cytoplasmic 229, pseudogene . . . . . . . . . . . RN7SL230P . . . RNA, 7SL, cytoplasmic 230, pseudogene . . . . . . . . . . . RN7SL231P . . . RNA, 7SL, cytoplasmic 231, pseudogene . . . . . . . . . . . RN7SL233P . . . RNA, 7SL, cytoplasmic 233, pseudogene . . . . . . . . . . . RN7SL234P . . . RNA, 7SL, cytoplasmic 234, pseudogene . . . . . . . . . . . RN7SL236P . . . RNA, 7SL, cytoplasmic 236, pseudogene . . . . . . . . . . . RN7SL237P . . . RNA, 7SL, cytoplasmic 237, pseudogene . . . . . . . . . . . RN7SL238P . . . RNA, 7SL, cytoplasmic 238, pseudogene . . . . . . . . . . . RN7SL239P . . . RNA, 7SL, cytoplasmic 239, pseudogene . . . . . . . . . . . RN7SL240P . . . RNA, 7SL, cytoplasmic 240, pseudogene . . . . . . . . . . . RN7SL241P . . . RNA, 7SL, cytoplasmic 241, pseudogene . . . . . . . . . . . RN7SL242P . . . RNA, 7SL, cytoplasmic 242, pseudogene . . . . . . . . . . . RN7SL244P . . . RNA, 7SL, cytoplasmic 244, pseudogene . . . . . . . . . . . RN7SL246P . . . RNA, 7SL, cytoplasmic 246, pseudogene . . . . . . . . . . . RN7SL248P . . . RNA, 7SL, cytoplasmic 248, pseudogene . . . . . . . . . . . RN7SL250P . . . RNA, 7SL, cytoplasmic 250, pseudogene . . . . . . . . . . . RN7SL251P . . . RNA, 7SL, cytoplasmic 251, pseudogene . . . . . . . . . . . RN7SL252P . . . RNA, 7SL, cytoplasmic 252, pseudogene . . . . . . . . . . . RN7SL253P . . . RNA, 7SL, cytoplasmic 253, pseudogene . . . . . . . . . . . RN7SL254P . . . RNA, 7SL, cytoplasmic 254, pseudogene . . . . . . . . . . . RN7SL255P . . . RNA, 7SL, cytoplasmic 255, pseudogene . . . . . . . . . . . RN7SL257P . . . RNA, 7SL, cytoplasmic 257, pseudogene . . . . . . . . . . . RN7SL258P . . . RNA, 7SL, cytoplasmic 258, pseudogene . . . . . . . . . . . RN7SL259P . . . RNA, 7SL, cytoplasmic 259, pseudogene . . . . . . . . . . . RN7SL260P . . . RNA, 7SL, cytoplasmic 260, pseudogene . . . . . . . . . . . RN7SL261P . . . RNA, 7SL, cytoplasmic 261, pseudogene . . . . . . . . . . . RN7SL262P . . . RNA, 7SL, cytoplasmic 262, pseudogene . . . . . . . . . . . RN7SL263P . . . RNA, 7SL, cytoplasmic 263, pseudogene . . . . . . . . . . . RN7SL265P . . . RNA, 7SL, cytoplasmic 265, pseudogene . . . . . . . . . . . RN7SL266P . . . RNA, 7SL, cytoplasmic 266, pseudogene . . . . . . . . . . . RN7SL267P . . . RNA, 7SL, cytoplasmic 267, pseudogene . . . . . . . . . . . RN7SL268P . . . RNA, 7SL, cytoplasmic 268, pseudogene . . . . . . . . . . . RN7SL269P . . . RNA, 7SL, cytoplasmic 269, pseudogene . . . . . . . . . . . RN7SL270P . . . RNA, 7SL, cytoplasmic 270, pseudogene . . . . . . . . . . . RN7SL271P . . . RNA, 7SL, cytoplasmic 271, pseudogene . . . . . . . . . . . RN7SL272P . . . RNA, 7SL, cytoplasmic 272, pseudogene . . . . . . . . . . . RN7SL273P . . . RNA, 7SL, cytoplasmic 273, pseudogene . . . . . . . . . . . RN7SL274P . . . RNA, 7SL, cytoplasmic 274, pseudogene . . . . . . . . . . . RN7SL275P . . . RNA, 7SL, cytoplasmic 275, pseudogene . . . . . . . . . . . RN7SL277P . . . RNA, 7SL, cytoplasmic 277, pseudogene . . . . . . . . . . . RN7SL278P . . . RNA, 7SL, cytoplasmic 278, pseudogene . . . . . . . . . . . RN7SL279P . . . RNA, 7SL, cytoplasmic 279, pseudogene . . . . . . . . . . . RN7SL280P . . . RNA, 7SL, cytoplasmic 280, pseudogene . . . . . . . . . . . RN7SL282P . . . RNA, 7SL, cytoplasmic 282, pseudogene . . . . . . . . . . . RN7SL283P . . . RNA, 7SL, cytoplasmic 283, pseudogene . . . . . . . . . . . RN7SL284P . . . RNA, 7SL, cytoplasmic 284, pseudogene . . . . . . . . . . . RN7SL285P . . . RNA, 7SL, cytoplasmic 285, pseudogene . . . . . . . . . . . RN7SL286P . . . RNA, 7SL, cytoplasmic 286, pseudogene . . . . . . . . . . . RN7SL288P . . . RNA, 7SL, cytoplasmic 288, pseudogene . . . . . . . . . . . RN7SL290P . . . RNA, 7SL, cytoplasmic 290, pseudogene . . . . . . . . . . . RN7SL291P . . . RNA, 7SL, cytoplasmic 291, pseudogene . . . . . . . . . . . RN7SL292P . . . RNA, 7SL, cytoplasmic 292, pseudogene . . . . . . . . . . . RN7SL293P . . . RNA, 7SL, cytoplasmic 293, pseudogene . . . . . . . . . . . RN7SL294P . . . RNA, 7SL, cytoplasmic 294, pseudogene . . . . . . . . . . . RN7SL296P . . . RNA, 7SL, cytoplasmic 296, pseudogene . . . . . . . . . . . RN7SL297P . . . RNA, 7SL, cytoplasmic 297, pseudogene . . . . . . . . . . . RN7SL299P . . . RNA, 7SL, cytoplasmic 299, pseudogene . . . . . . . . . . . RN7SL300P . . . RNA, 7SL, cytoplasmic 300, pseudogene . . . . . . . . . . . RN7SL301P . . . RNA, 7SL, cytoplasmic 301, pseudogene . . . . . . . . . . . RN7SL302P . . . RNA, 7SL, cytoplasmic 302, pseudogene . . . . . . . . . . . RN7SL303P . . . RNA, 7SL, cytoplasmic 303, pseudogene . . . . . . . . . . . RN7SL304P . . . RNA, 7SL, cytoplasmic 304, pseudogene . . . . . . . . . . . RN7SL305P . . . RNA, 7SL, cytoplasmic 305, pseudogene . . . . . . . . . . . RN7SL306P . . . RNA, 7SL, cytoplasmic 306, pseudogene . . . . . . . . . . . RN7SL307P . . . RNA, 7SL, cytoplasmic 307, pseudogene . . . . . . . . . . . RN7SL308P . . . RNA, 7SL, cytoplasmic 308, pseudogene . . . . . . . . . . . RN7SL309P . . . RNA, 7SL, cytoplasmic 309, pseudogene . . . . . . . . . . . RN7SL310P . . . RNA, 7SL, cytoplasmic 310, pseudogene . . . . . . . . . . . RN7SL311P . . . RNA, 7SL, cytoplasmic 311, pseudogene . . . . . . . . . . . RN7SL313P . . . RNA, 7SL, cytoplasmic 313, pseudogene . . . . . . . . . . . RN7SL314P . . . RNA, 7SL, cytoplasmic 314, pseudogene . . . . . . . . . . . RN7SL316P . . . RNA, 7SL, cytoplasmic 316, pseudogene . . . . . . . . . . . RN7SL317P . . . RNA, 7SL, cytoplasmic 317, pseudogene . . . . . . . . . . . RN7SL318P . . . RNA, 7SL, cytoplasmic 318, pseudogene . . . . . . . . . . . RN7SL319P . . . RNA, 7SL, cytoplasmic 319, pseudogene . . . . . . . . . . . RN7SL320P . . . RNA, 7SL, cytoplasmic 320, pseudogene . . . . . . . . . . . RN7SL321P . . . RNA, 7SL, cytoplasmic 321, pseudogene . . . . . . . . . . . RN7SL322P . . . RNA, 7SL, cytoplasmic 322, pseudogene . . . . . . . . . . . RN7SL323P . . . RNA, 7SL, cytoplasmic 323, pseudogene . . . . . . . . . . . RN7SL325P . . . RNA, 7SL, cytoplasmic 325, pseudogene . . . . . . . . . . . RN7SL326P . . . RNA, 7SL, cytoplasmic 326, pseudogene . . . . . . . . . . . RN7SL327P . . . RNA, 7SL, cytoplasmic 327, pseudogene . . . . . . . . . . . RN7SL328P . . . RNA, 7SL, cytoplasmic 328, pseudogene . . . . . . . . . . . RN7SL329P . . . RNA, 7SL, cytoplasmic 329, pseudogene . . . . . . . . . . . RN7SL330P . . . RNA, 7SL, cytoplasmic 330, pseudogene . . . . . . . . . . . RN7SL331P . . . RNA, 7SL, cytoplasmic 331, pseudogene . . . . . . . . . . . RN7SL332P . . . RNA, 7SL, cytoplasmic 332, pseudogene . . . . . . . . . . . RN7SL333P . . . RNA, 7SL, cytoplasmic 333, pseudogene . . . . . . . . . . . RN7SL334P . . . RNA, 7SL, cytoplasmic 334, pseudogene . . . . . . . . . . . RN7SL335P . . . RNA, 7SL, cytoplasmic 335, pseudogene . . . . . . . . . . . RN7SL336P . . . RNA, 7SL, cytoplasmic 336, pseudogene . . . . . . . . . . . RN7SL337P . . . RNA, 7SL, cytoplasmic 337, pseudogene . . . . . . . . . . . RN7SL338P . . . RNA, 7SL, cytoplasmic 338, pseudogene . . . . . . . . . . . RN7SL339P . . . RNA, 7SL, cytoplasmic 339, pseudogene . . . . . . . . . . . RN7SL340P . . . RNA, 7SL, cytoplasmic 340, pseudogene . . . . . . . . . . . RN7SL341P . . . RNA, 7SL, cytoplasmic 341, pseudogene . . . . . . . . . . . RN7SL342P . . . RNA, 7SL, cytoplasmic 342, pseudogene . . . . . . . . . . . RN7SL343P . . . RNA, 7SL, cytoplasmic 343, pseudogene . . . . . . . . . . . RN7SL344P . . . RNA, 7SL, cytoplasmic 344, pseudogene . . . . . . . . . . . RN7SL346P . . . RNA, 7SL, cytoplasmic 346, pseudogene . . . . . . . . . . . RN7SL350P . . . RNA, 7SL, cytoplasmic 350, pseudogene . . . . . . . . . . . RN7SL351P . . . RNA, 7SL, cytoplasmic 351, pseudogene . . . . . . . . . . . RN7SL352P . . . RNA, 7SL, cytoplasmic 352, pseudogene . . . . . . . . . . . RN7SL353P . . . RNA, 7SL, cytoplasmic 353, pseudogene . . . . . . . . . . . RN7SL354P . . . RNA, 7SL, cytoplasmic 354, pseudogene . . . . . . . . . . . RN7SL356P . . . RNA, 7SL, cytoplasmic 356, pseudogene . . . . . . . . . . . RN7SL357P . . . RNA, 7SL, cytoplasmic 357, pseudogene . . . . . . . . . . . RN7SL359P . . . RNA, 7SL, cytoplasmic 359, pseudogene . . . . . . . . . . . RN7SL361P . . . RNA, 7SL, cytoplasmic 361, pseudogene . . . . . . . . . . . RN7SL362P . . . RNA, 7SL, cytoplasmic 362, pseudogene . . . . . . . . . . . RN7SL363P . . . RNA, 7SL, cytoplasmic 363, pseudogene . . . . . . . . . . . RN7SL364P . . . RNA, 7SL, cytoplasmic 364, pseudogene . . . . . . . . . . . RN7SL366P . . . RNA, 7SL, cytoplasmic 366, pseudogene . . . . . . . . . . . RN7SL368P . . . RNA, 7SL, cytoplasmic 368, pseudogene . . . . . . . . . . . RN7SL369P . . . RNA, 7SL, cytoplasmic 369, pseudogene . . . . . . . . . . . RN7SL370P . . . RNA, 7SL, cytoplasmic 370, pseudogene . . . . . . . . . . . RN7SL371P . . . RNA, 7SL, cytoplasmic 371, pseudogene . . . . . . . . . . . RN7SL372P . . . RNA, 7SL, cytoplasmic 372, pseudogene . . . . . . . . . . . RN7SL375P . . . RNA, 7SL, cytoplasmic 375, pseudogene . . . . . . . . . . . RN7SL376P . . . RNA, 7SL, cytoplasmic 376, pseudogene . . . . . . . . . . . RN7SL377P . . . RNA, 7SL, cytoplasmic 377, pseudogene . . . . . . . . . . . RN7SL378P . . . RNA, 7SL, cytoplasmic 378, pseudogene . . . . . . . . . . . RN7SL379P . . . RNA, 7SL, cytoplasmic 379, pseudogene . . . . . . . . . . . RN7SL380P . . . RNA, 7SL, cytoplasmic 380, pseudogene . . . . . . . . . . . RN7SL381P . . . RNA, 7SL, cytoplasmic 381, pseudogene . . . . . . . . . . . RN7SL382P . . . RNA, 7SL, cytoplasmic 382, pseudogene . . . . . . . . . . . RN7SL383P . . . RNA, 7SL, cytoplasmic 383, pseudogene . . . . . . . . . . . RN7SL384P . . . RNA, 7SL, cytoplasmic 384, pseudogene . . . . . . . . . . . RN7SL385P . . . RNA, 7SL, cytoplasmic 385, pseudogene . . . . . . . . . . . RN7SL386P . . . RNA, 7SL, cytoplasmic 386, pseudogene . . . . . . . . . . . RN7SL387P . . . RNA, 7SL, cytoplasmic 387, pseudogene . . . . . . . . . . . RN7SL388P . . . RNA, 7SL, cytoplasmic 388, pseudogene . . . . . . . . . . . RN7SL390P . . . RNA, 7SL, cytoplasmic 390, pseudogene . . . . . . . . . . . RN7SL391P . . . RNA, 7SL, cytoplasmic 391, pseudogene . . . . . . . . . . . RN7SL392P . . . RNA, 7SL, cytoplasmic 392, pseudogene . . . . . . . . . . . RN7SL393P . . . RNA, 7SL, cytoplasmic 393, pseudogene . . . . . . . . . . . RN7SL394P . . . RNA, 7SL, cytoplasmic 394, pseudogene . . . . . . . . . . . RN7SL395P . . . RNA, 7SL, cytoplasmic 395, pseudogene . . . . . . . . . . . RN7SL396P . . . RNA, 7SL, cytoplasmic 396, pseudogene . . . . . . . . . . . RN7SL397P . . . RNA, 7SL, cytoplasmic 397, pseudogene . . . . . . . . . . . RN7SL398P . . . RNA, 7SL, cytoplasmic 398, pseudogene . . . . . . . . . . . RN7SL399P . . . RNA, 7SL, cytoplasmic 399, pseudogene . . . . . . . . . . . RN7SL400P . . . RNA, 7SL, cytoplasmic 400, pseudogene . . . . . . . . . . . RN7SL401P . . . RNA, 7SL, cytoplasmic 401, pseudogene . . . . . . . . . . . RN7SL402P . . . RNA, 7SL, cytoplasmic 402, pseudogene . . . . . . . . . . . RN7SL403P . . . RNA, 7SL, cytoplasmic 403, pseudogene . . . . . . . . . . . RN7SL404P . . . RNA, 7SL, cytoplasmic 404, pseudogene . . . . . . . . . . . RN7SL405P . . . RNA, 7SL, cytoplasmic 405, pseudogene . . . . . . . . . . . RN7SL408P . . . RNA, 7SL, cytoplasmic 408, pseudogene . . . . . . . . . . . RN7SL411P . . . RNA, 7SL, cytoplasmic 411, pseudogene . . . . . . . . . . . RN7SL413P . . . RNA, 7SL, cytoplasmic 413, pseudogene . . . . . . . . . . . RN7SL414P . . . RNA, 7SL, cytoplasmic 414, pseudogene . . . . . . . . . . . RN7SL415P . . . RNA, 7SL, cytoplasmic 415, pseudogene . . . . . . . . . . . RN7SL416P . . . RNA, 7SL, cytoplasmic 416, pseudogene . . . . . . . . . . . RN7SL417P . . . RNA, 7SL, cytoplasmic 417, pseudogene . . . . . . . . . . . RN7SL418P . . . RNA, 7SL, cytoplasmic 418, pseudogene . . . . . . . . . . . RN7SL419P . . . RNA, 7SL, cytoplasmic 419, pseudogene . . . . . . . . . . . RN7SL420P . . . RNA, 7SL, cytoplasmic 420, pseudogene . . . . . . . . . . . RN7SL422P . . . RNA, 7SL, cytoplasmic 422, pseudogene . . . . . . . . . . . RN7SL423P . . . RNA, 7SL, cytoplasmic 423, pseudogene . . . . . . . . . . . RN7SL424P . . . RNA, 7SL, cytoplasmic 424, pseudogene . . . . . . . . . . . RN7SL425P . . . RNA, 7SL, cytoplasmic 425, pseudogene . . . . . . . . . . . RN7SL426P . . . RNA, 7SL, cytoplasmic 426, pseudogene . . . . . . . . . . . RN7SL428P . . . RNA, 7SL, cytoplasmic 428, pseudogene . . . . . . . . . . . RN7SL429P . . . RNA, 7SL, cytoplasmic 429, pseudogene . . . . . . . . . . . RN7SL430P . . . RNA, 7SL, cytoplasmic 430, pseudogene . . . . . . . . . . . RN7SL431P . . . RNA, 7SL, cytoplasmic 431, pseudogene . . . . . . . . . . . RN7SL432P . . . RNA, 7SL, cytoplasmic 432, pseudogene . . . . . . . . . . . RN7SL434P . . . RNA, 7SL, cytoplasmic 434, pseudogene . . . . . . . . . . . RN7SL435P . . . RNA, 7SL, cytoplasmic 435, pseudogene . . . . . . . . . . . RN7SL438P . . . RNA, 7SL, cytoplasmic 438, pseudogene . . . . . . . . . . . RN7SL440P . . . RNA, 7SL, cytoplasmic 440, pseudogene . . . . . . . . . . . RN7SL441P . . . RNA, 7SL, cytoplasmic 441, pseudogene . . . . . . . . . . . RN7SL442P . . . RNA, 7SL, cytoplasmic 442, pseudogene . . . . . . . . . . . RN7SL443P . . . RNA, 7SL, cytoplasmic 443, pseudogene . . . . . . . . . . . RN7SL444P . . . RNA, 7SL, cytoplasmic 444, pseudogene . . . . . . . . . . . RN7SL445P . . . RNA, 7SL, cytoplasmic 445, pseudogene . . . . . . . . . . . RN7SL446P . . . RNA, 7SL, cytoplasmic 446, pseudogene . . . . . . . . . . . RN7SL447P . . . RNA, 7SL, cytoplasmic 447, pseudogene . . . . . . . . . . . RN7SL448P . . . RNA, 7SL, cytoplasmic 448, pseudogene . . . . . . . . . . . RN7SL449P . . . RNA, 7SL, cytoplasmic 449, pseudogene . . . . . . . . . . . RN7SL451P . . . RNA, 7SL, cytoplasmic 451, pseudogene . . . . . . . . . . . RN7SL452P . . . RNA, 7SL, cytoplasmic 452, pseudogene . . . . . . . . . . . RN7SL453P . . . RNA, 7SL, cytoplasmic 453, pseudogene . . . . . . . . . . . RN7SL454P . . . RNA, 7SL, cytoplasmic 454, pseudogene . . . . . . . . . . . RN7SL455P . . . RNA, 7SL, cytoplasmic 455, pseudogene . . . . . . . . . . . RN7SL456P . . . RNA, 7SL, cytoplasmic 456, pseudogene . . . . . . . . . . . RN7SL457P . . . RNA, 7SL, cytoplasmic 457, pseudogene . . . . . . . . . . . RN7SL459P . . . RNA, 7SL, cytoplasmic 459, pseudogene . . . . . . . . . . . RN7SL460P . . . RNA, 7SL, cytoplasmic 460, pseudogene . . . . . . . . . . . RN7SL461P . . . RNA, 7SL, cytoplasmic 461, pseudogene . . . . . . . . . . . RN7SL462P . . . RNA, 7SL, cytoplasmic 462, pseudogene . . . . . . . . . . . RN7SL464P . . . RNA, 7SL, cytoplasmic 464, pseudogene . . . . . . . . . . . RN7SL465P . . . RNA, 7SL, cytoplasmic 465, pseudogene . . . . . . . . . . . RN7SL466P . . . RNA, 7SL, cytoplasmic 466, pseudogene . . . . . . . . . . . RN7SL468P . . . RNA, 7SL, cytoplasmic 468, pseudogene . . . . . . . . . . . RN7SL469P . . . RNA, 7SL, cytoplasmic 469, pseudogene . . . . . . . . . . . RN7SL470P . . . RNA, 7SL, cytoplasmic 470, pseudogene . . . . . . . . . . . RN7SL471P . . . RNA, 7SL, cytoplasmic 471, pseudogene . . . . . . . . . . . RN7SL472P . . . RNA, 7SL, cytoplasmic 472, pseudogene . . . . . . . . . . . RN7SL473P . . . RNA, 7SL, cytoplasmic 473, pseudogene . . . . . . . . . . . RN7SL474P . . . RNA, 7SL, cytoplasmic 474, pseudogene . . . . . . . . . . . RN7SL475P . . . RNA, 7SL, cytoplasmic 475, pseudogene . . . . . . . . . . . RN7SL477P . . . RNA, 7SL, cytoplasmic 477, pseudogene . . . . . . . . . . . RN7SL478P . . . RNA, 7SL, cytoplasmic 478, pseudogene . . . . . . . . . . . RN7SL479P . . . RNA, 7SL, cytoplasmic 479, pseudogene . . . . . . . . . . . RN7SL480P . . . RNA, 7SL, cytoplasmic 480, pseudogene . . . . . . . . . . . RN7SL481P . . . RNA, 7SL, cytoplasmic 481, pseudogene . . . . . . . . . . . RN7SL482P . . . RNA, 7SL, cytoplasmic 482, pseudogene . . . . . . . . . . . RN7SL483P . . . RNA, 7SL, cytoplasmic 483, pseudogene . . . . . . . . . . . RN7SL484P . . . RNA, 7SL, cytoplasmic 484, pseudogene . . . . . . . . . . . RN7SL487P . . . RNA, 7SL, cytoplasmic 487, pseudogene . . . . . . . . . . . RN7SL488P . . . RNA, 7SL, cytoplasmic 488, pseudogene . . . . . . . . . . . RN7SL489P . . . RNA, 7SL, cytoplasmic 489, pseudogene . . . . . . . . . . . RN7SL491P . . . RNA, 7SL, cytoplasmic 491, pseudogene . . . . . . . . . . . RN7SL492P . . . RNA, 7SL, cytoplasmic 492, pseudogene . . . . . . . . . . . RN7SL493P . . . RNA, 7SL, cytoplasmic 493, pseudogene . . . . . . . . . . . RN7SL494P . . . RNA, 7SL, cytoplasmic 494, pseudogene . . . . . . . . . . . RN7SL495P . . . RNA, 7SL, cytoplasmic 495, pseudogene . . . . . . . . . . . RN7SL496P . . . RNA, 7SL, cytoplasmic 496, pseudogene . . . . . . . . . . . RN7SL497P . . . RNA, 7SL, cytoplasmic 497, pseudogene . . . . . . . . . . . RN7SL498P . . . RNA, 7SL, cytoplasmic 498, pseudogene . . . . . . . . . . . RN7SL499P . . . RNA, 7SL, cytoplasmic 499, pseudogene . . . . . . . . . . . RN7SL500P . . . RNA, 7SL, cytoplasmic 500, pseudogene . . . . . . . . . . . RN7SL502P . . . RNA, 7SL, cytoplasmic 502, pseudogene . . . . . . . . . . . RN7SL503P . . . RNA, 7SL, cytoplasmic 503, pseudogene . . . . . . . . . . . RN7SL504P . . . RNA, 7SL, cytoplasmic 504, pseudogene . . . . . . . . . . . RN7SL505P . . . RNA, 7SL, cytoplasmic 505, pseudogene . . . . . . . . . . . RN7SL507P . . . RNA, 7SL, cytoplasmic 507, pseudogene . . . . . . . . . . . RN7SL508P . . . RNA, 7SL, cytoplasmic 508, pseudogene . . . . . . . . . . . RN7SL509P . . . RNA, 7SL, cytoplasmic 509, pseudogene . . . . . . . . . . . RN7SL510P . . . RNA, 7SL, cytoplasmic 510, pseudogene . . . . . . . . . . . RN7SL513P . . . RNA, 7SL, cytoplasmic 513, pseudogene . . . . . . . . . . . RN7SL515P . . . RNA, 7SL, cytoplasmic 515, pseudogene . . . . . . . . . . . RN7SL516P . . . RNA, 7SL, cytoplasmic 516, pseudogene . . . . . . . . . . . RN7SL517P . . . RNA, 7SL, cytoplasmic 517, pseudogene . . . . . . . . . . . RN7SL518P . . . RNA, 7SL, cytoplasmic 518, pseudogene . . . . . . . . . . . RN7SL519P . . . RNA, 7SL, cytoplasmic 519, pseudogene . . . . . . . . . . . RN7SL520P . . . RNA, 7SL, cytoplasmic 520, pseudogene . . . . . . . . . . . RN7SL521P . . . RNA, 7SL, cytoplasmic 521, pseudogene . . . . . . . . . . . RN7SL523P . . . RNA, 7SL, cytoplasmic 523, pseudogene . . . . . . . . . . . RN7SL524P . . . RNA, 7SL, cytoplasmic 524, pseudogene . . . . . . . . . . . RN7SL525P . . . RNA, 7SL, cytoplasmic 525, pseudogene . . . . . . . . . . . RN7SL526P . . . RNA, 7SL, cytoplasmic 526, pseudogene . . . . . . . . . . . RN7SL530P . . . RNA, 7SL, cytoplasmic 530, pseudogene . . . . . . . . . . . RN7SL531P . . . RNA, 7SL, cytoplasmic 531, pseudogene . . . . . . . . . . . RN7SL535P . . . RNA, 7SL, cytoplasmic 535, pseudogene . . . . . . . . . . . RN7SL536P . . . RNA, 7SL, cytoplasmic 536, pseudogene . . . . . . . . . . . RN7SL538P . . . RNA, 7SL, cytoplasmic 538, pseudogene . . . . . . . . . . . RN7SL539P . . . RNA, 7SL, cytoplasmic 539, pseudogene . . . . . . . . . . . RN7SL541P . . . RNA, 7SL, cytoplasmic 541, pseudogene . . . . . . . . . . . RN7SL542P . . . RNA, 7SL, cytoplasmic 542, pseudogene . . . . . . . . . . . RN7SL543P . . . RNA, 7SL, cytoplasmic 543, pseudogene . . . . . . . . . . . RN7SL544P . . . RNA, 7SL, cytoplasmic 544, pseudogene . . . . . . . . . . . RN7SL545P . . . RNA, 7SL, cytoplasmic 545, pseudogene . . . . . . . . . . . RN7SL546P . . . RNA, 7SL, cytoplasmic 546, pseudogene . . . . . . . . . . . RN7SL547P . . . RNA, 7SL, cytoplasmic 547, pseudogene . . . . . . . . . . . RN7SL549P . . . RNA, 7SL, cytoplasmic 549, pseudogene . . . . . . . . . . . RN7SL551P . . . RNA, 7SL, cytoplasmic 551, pseudogene . . . . . . . . . . . RN7SL552P . . . RNA, 7SL, cytoplasmic 552, pseudogene . . . . . . . . . . . RN7SL553P . . . RNA, 7SL, cytoplasmic 553, pseudogene . . . . . . . . . . . RN7SL554P . . . RNA, 7SL, cytoplasmic 554, pseudogene . . . . . . . . . . . RN7SL555P . . . RNA, 7SL, cytoplasmic 555, pseudogene . . . . . . . . . . . RN7SL556P . . . RNA, 7SL, cytoplasmic 556, pseudogene . . . . . . . . . . . RN7SL557P . . . RNA, 7SL, cytoplasmic 557, pseudogene . . . . . . . . . . . RN7SL558P . . . RNA, 7SL, cytoplasmic 558, pseudogene . . . . . . . . . . . RN7SL559P . . . RNA, 7SL, cytoplasmic 559, pseudogene . . . . . . . . . . . RN7SL560P . . . RNA, 7SL, cytoplasmic 560, pseudogene . . . . . . . . . . . RN7SL561P . . . RNA, 7SL, cytoplasmic 561, pseudogene . . . . . . . . . . . RN7SL563P . . . RNA, 7SL, cytoplasmic 563, pseudogene . . . . . . . . . . . RN7SL564P . . . RNA, 7SL, cytoplasmic 564, pseudogene . . . . . . . . . . . RN7SL565P . . . RNA, 7SL, cytoplasmic 565, pseudogene . . . . . . . . . . . RN7SL566P . . . RNA, 7SL, cytoplasmic 566, pseudogene . . . . . . . . . . . RN7SL567P . . . RNA, 7SL, cytoplasmic 567, pseudogene . . . . . . . . . . . RN7SL568P . . . RNA, 7SL, cytoplasmic 568, pseudogene . . . . . . . . . . . RN7SL569P . . . RNA, 7SL, cytoplasmic 569, pseudogene . . . . . . . . . . . RN7SL570P . . . RNA, 7SL, cytoplasmic 570, pseudogene . . . . . . . . . . . RN7SL571P . . . RNA, 7SL, cytoplasmic 571, pseudogene . . . . . . . . . . . RN7SL573P . . . RNA, 7SL, cytoplasmic 573, pseudogene . . . . . . . . . . . RN7SL574P . . . RNA, 7SL, cytoplasmic 574, pseudogene . . . . . . . . . . . RN7SL575P . . . RNA, 7SL, cytoplasmic 575, pseudogene . . . . . . . . . . . RN7SL577P . . . RNA, 7SL, cytoplasmic 577, pseudogene . . . . . . . . . . . RN7SL578P . . . RNA, 7SL, cytoplasmic 578, pseudogene . . . . . . . . . . . RN7SL579P . . . RNA, 7SL, cytoplasmic 579, pseudogene . . . . . . . . . . . RN7SL580P . . . RNA, 7SL, cytoplasmic 580, pseudogene . . . . . . . . . . . RN7SL581P . . . RNA, 7SL, cytoplasmic 581, pseudogene . . . . . . . . . . . RN7SL582P . . . RNA, 7SL, cytoplasmic 582, pseudogene . . . . . . . . . . . RN7SL583P . . . RNA, 7SL, cytoplasmic 583, pseudogene . . . . . . . . . . . RN7SL584P . . . RNA, 7SL, cytoplasmic 584, pseudogene . . . . . . . . . . . RN7SL585P . . . RNA, 7SL, cytoplasmic 585, pseudogene . . . . . . . . . . . RN7SL586P . . . RNA, 7SL, cytoplasmic 586, pseudogene . . . . . . . . . . . RN7SL587P . . . RNA, 7SL, cytoplasmic 587, pseudogene . . . . . . . . . . . RN7SL589P . . . RNA, 7SL, cytoplasmic 589, pseudogene . . . . . . . . . . . RN7SL591P . . . RNA, 7SL, cytoplasmic 591, pseudogene . . . . . . . . . . . RN7SL592P . . . RNA, 7SL, cytoplasmic 592, pseudogene . . . . . . . . . . . RN7SL594P . . . RNA, 7SL, cytoplasmic 594, pseudogene . . . . . . . . . . . RN7SL596P . . . RNA, 7SL, cytoplasmic 596, pseudogene . . . . . . . . . . . RN7SL597P . . . RNA, 7SL, cytoplasmic 597, pseudogene . . . . . . . . . . . RN7SL598P . . . RNA, 7SL, cytoplasmic 598, pseudogene . . . . . . . . . . . RN7SL600P . . . RNA, 7SL, cytoplasmic 600, pseudogene . . . . . . . . . . . RN7SL601P . . . RNA, 7SL, cytoplasmic 601, pseudogene . . . . . . . . . . . RN7SL602P . . . RNA, 7SL, cytoplasmic 602, pseudogene . . . . . . . . . . . RN7SL604P . . . RNA, 7SL, cytoplasmic 604, pseudogene . . . . . . . . . . . RN7SL605P . . . RNA, 7SL, cytoplasmic 605, pseudogene . . . . . . . . . . . RN7SL606P . . . RNA, 7SL, cytoplasmic 606, pseudogene . . . . . . . . . . . RN7SL607P . . . RNA, 7SL, cytoplasmic 607, pseudogene . . . . . . . . . . . RN7SL608P . . . RNA, 7SL, cytoplasmic 608, pseudogene . . . . . . . . . . . RN7SL610P . . . RNA, 7SL, cytoplasmic 610, pseudogene . . . . . . . . . . . RN7SL612P . . . RNA, 7SL, cytoplasmic 612, pseudogene . . . . . . . . . . . RN7SL614P . . . RNA, 7SL, cytoplasmic 614, pseudogene . . . . . . . . . . . RN7SL615P . . . RNA, 7SL, cytoplasmic 615, pseudogene . . . . . . . . . . . RN7SL616P . . . RNA, 7SL, cytoplasmic 616, pseudogene . . . . . . . . . . . RN7SL617P . . . RNA, 7SL, cytoplasmic 617, pseudogene . . . . . . . . . . . RN7SL618P . . . RNA, 7SL, cytoplasmic 618, pseudogene . . . . . . . . . . . RN7SL619P . . . RNA, 7SL, cytoplasmic 619, pseudogene . . . . . . . . . . . RN7SL620P . . . RNA, 7SL, cytoplasmic 620, pseudogene . . . . . . . . . . . RN7SL621P . . . RNA, 7SL, cytoplasmic 621, pseudogene . . . . . . . . . . . RN7SL622P . . . RNA, 7SL, cytoplasmic 622, pseudogene . . . . . . . . . . . RN7SL623P . . . RNA, 7SL, cytoplasmic 623, pseudogene . . . . . . . . . . . RN7SL624P . . . RNA, 7SL, cytoplasmic 624, pseudogene . . . . . . . . . . . RN7SL625P . . . RNA, 7SL, cytoplasmic 625, pseudogene . . . . . . . . . . . RN7SL627P . . . RNA, 7SL, cytoplasmic 627, pseudogene . . . . . . . . . . . RN7SL628P . . . RNA, 7SL, cytoplasmic 628, pseudogene . . . . . . . . . . . RN7SL629P . . . RNA, 7SL, cytoplasmic 629, pseudogene . . . . . . . . . . . RN7SL630P . . . RNA, 7SL, cytoplasmic 630, pseudogene . . . . . . . . . . . RN7SL632P . . . RNA, 7SL, cytoplasmic 632, pseudogene . . . . . . . . . . . RN7SL633P . . . RNA, 7SL, cytoplasmic 633, pseudogene . . . . . . . . . . . RN7SL634P . . . RNA, 7SL, cytoplasmic 634, pseudogene . . . . . . . . . . . RN7SL635P . . . RNA, 7SL, cytoplasmic 635, pseudogene . . . . . . . . . . . RN7SL636P . . . RNA, 7SL, cytoplasmic 636, pseudogene . . . . . . . . . . . RN7SL638P . . . RNA, 7SL, cytoplasmic 638, pseudogene . . . . . . . . . . . RN7SL640P . . . RNA, 7SL, cytoplasmic 640, pseudogene . . . . . . . . . . . RN7SL643P . . . RNA, 7SL, cytoplasmic 643, pseudogene . . . . . . . . . . . RN7SL644P . . . RNA, 7SL, cytoplasmic 644, pseudogene . . . . . . . . . . . RN7SL645P . . . RNA, 7SL, cytoplasmic 645, pseudogene . . . . . . . . . . . RN7SL646P . . . RNA, 7SL, cytoplasmic 646, pseudogene . . . . . . . . . . . RN7SL647P . . . RNA, 7SL, cytoplasmic 647, pseudogene . . . . . . . . . . . RN7SL648P . . . RNA, 7SL, cytoplasmic 648, pseudogene . . . . . . . . . . . RN7SL649P . . . RNA, 7SL, cytoplasmic 649, pseudogene . . . . . . . . . . . RN7SL650P . . . RNA, 7SL, cytoplasmic 650, pseudogene . . . . . . . . . . . RN7SL652P . . . RNA, 7SL, cytoplasmic 652, pseudogene . . . . . . . . . . . RN7SL653P . . . RNA, 7SL, cytoplasmic 653, pseudogene . . . . . . . . . . . RN7SL654P . . . RNA, 7SL, cytoplasmic 654, pseudogene . . . . . . . . . . . RN7SL655P . . . RNA, 7SL, cytoplasmic 655, pseudogene . . . . . . . . . . . RN7SL656P . . . RNA, 7SL, cytoplasmic 656, pseudogene . . . . . . . . . . . RN7SL657P . . . RNA, 7SL, cytoplasmic 657, pseudogene . . . . . . . . . . . RN7SL658P . . . RNA, 7SL, cytoplasmic 658, pseudogene . . . . . . . . . . . RN7SL659P . . . RNA, 7SL, cytoplasmic 659, pseudogene . . . . . . . . . . . RN7SL660P . . . RNA, 7SL, cytoplasmic 660, pseudogene . . . . . . . . . . . RN7SL663P . . . RNA, 7SL, cytoplasmic 663, pseudogene . . . . . . . . . . . RN7SL664P . . . RNA, 7SL, cytoplasmic 664, pseudogene . . . . . . . . . . . RN7SL665P . . . RNA, 7SL, cytoplasmic 665, pseudogene . . . . . . . . . . . RN7SL666P . . . RNA, 7SL, cytoplasmic 666, pseudogene . . . . . . . . . . . RN7SL667P . . . RNA, 7SL, cytoplasmic 667, pseudogene . . . . . . . . . . . RN7SL668P . . . RNA, 7SL, cytoplasmic 668, pseudogene . . . . . . . . . . . RN7SL670P . . . RNA, 7SL, cytoplasmic 670, pseudogene . . . . . . . . . . . RN7SL671P . . . RNA, 7SL, cytoplasmic 671, pseudogene . . . . . . . . . . . RN7SL672P . . . RNA, 7SL, cytoplasmic 672, pseudogene . . . . . . . . . . . RN7SL673P . . . RNA, 7SL, cytoplasmic 673, pseudogene . . . . . . . . . . . RN7SL674P . . . RNA, 7SL, cytoplasmic 674, pseudogene . . . . . . . . . . . RN7SL675P . . . RNA, 7SL, cytoplasmic 675, pseudogene . . . . . . . . . . . RN7SL676P . . . RNA, 7SL, cytoplasmic 676, pseudogene . . . . . . . . . . . RN7SL677P . . . RNA, 7SL, cytoplasmic 677, pseudogene . . . . . . . . . . . RN7SL678P . . . RNA, 7SL, cytoplasmic 678, pseudogene . . . . . . . . . . . RN7SL679P . . . RNA, 7SL, cytoplasmic 679, pseudogene . . . . . . . . . . . RN7SL680P . . . RNA, 7SL, cytoplasmic 680, pseudogene . . . . . . . . . . . RN7SL681P . . . RNA, 7SL, cytoplasmic 681, pseudogene . . . . . . . . . . . RN7SL683P . . . RNA, 7SL, cytoplasmic 683, pseudogene . . . . . . . . . . . RN7SL684P . . . RNA, 7SL, cytoplasmic 684, pseudogene . . . . . . . . . . . RN7SL685P . . . RNA, 7SL, cytoplasmic 685, pseudogene . . . . . . . . . . . RN7SL687P . . . RNA, 7SL, cytoplasmic 687, pseudogene . . . . . . . . . . . RN7SL688P . . . RNA, 7SL, cytoplasmic 688, pseudogene . . . . . . . . . . . RN7SL689P . . . RNA, 7SL, cytoplasmic 689, pseudogene . . . . . . . . . . . RN7SL690P . . . RNA, 7SL, cytoplasmic 690, pseudogene . . . . . . . . . . . RN7SL691P . . . RNA, 7SL, cytoplasmic 691, pseudogene . . . . . . . . . . . RN7SL692P . . . RNA, 7SL, cytoplasmic 692, pseudogene . . . . . . . . . . . RN7SL693P . . . RNA, 7SL, cytoplasmic 693, pseudogene . . . . . . . . . . . RN7SL697P . . . RNA, 7SL, cytoplasmic 697, pseudogene . . . . . . . . . . . RN7SL698P . . . RNA, 7SL, cytoplasmic 698, pseudogene . . . . . . . . . . . RN7SL700P . . . RNA, 7SL, cytoplasmic 700, pseudogene . . . . . . . . . . . RN7SL702P . . . RNA, 7SL, cytoplasmic 702, pseudogene . . . . . . . . . . . RN7SL703P . . . RNA, 7SL, cytoplasmic 703, pseudogene . . . . . . . . . . . RN7SL704P . . . RNA, 7SL, cytoplasmic 704, pseudogene . . . . . . . . . . . RN7SL705P . . . RNA, 7SL, cytoplasmic 705, pseudogene . . . . . . . . . . . RN7SL706P . . . RNA, 7SL, cytoplasmic 706, pseudogene . . . . . . . . . . . RN7SL708P . . . RNA, 7SL, cytoplasmic 708, pseudogene . . . . . . . . . . . RN7SL709P . . . RNA, 7SL, cytoplasmic 709, pseudogene . . . . . . . . . . . RN7SL711P . . . RNA, 7SL, cytoplasmic 711, pseudogene . . . . . . . . . . . RN7SL712P . . . RNA, 7SL, cytoplasmic 712, pseudogene . . . . . . . . . . . RN7SL713P . . . RNA, 7SL, cytoplasmic 713, pseudogene . . . . . . . . . . . RN7SL714P . . . RNA, 7SL, cytoplasmic 714, pseudogene . . . . . . . . . . . RN7SL715P . . . RNA, 7SL, cytoplasmic 715, pseudogene . . . . . . . . . . . RN7SL716P . . . RNA, 7SL, cytoplasmic 716, pseudogene . . . . . . . . . . . RN7SL717P . . . RNA, 7SL, cytoplasmic 717, pseudogene . . . . . . . . . . . RN7SL718P . . . RNA, 7SL, cytoplasmic 718, pseudogene . . . . . . . . . . . RN7SL719P . . . RNA, 7SL, cytoplasmic 719, pseudogene . . . . . . . . . . . RN7SL720P . . . RNA, 7SL, cytoplasmic 720, pseudogene . . . . . . . . . . . RN7SL722P . . . RNA, 7SL, cytoplasmic 722, pseudogene . . . . . . . . . . . RN7SL724P . . . RNA, 7SL, cytoplasmic 724, pseudogene . . . . . . . . . . . RN7SL725P . . . RNA, 7SL, cytoplasmic 725, pseudogene . . . . . . . . . . . RN7SL726P . . . RNA, 7SL, cytoplasmic 726, pseudogene . . . . . . . . . . . RN7SL727P . . . RNA, 7SL, cytoplasmic 727, pseudogene . . . . . . . . . . . RN7SL728P . . . RNA, 7SL, cytoplasmic 728, pseudogene . . . . . . . . . . . RN7SL731P . . . RNA, 7SL, cytoplasmic 731, pseudogene . . . . . . . . . . . RN7SL732P . . . RNA, 7SL, cytoplasmic 732, pseudogene . . . . . . . . . . . RN7SL733P . . . RNA, 7SL, cytoplasmic 733, pseudogene . . . . . . . . . . . RN7SL734P . . . RNA, 7SL, cytoplasmic 734, pseudogene . . . . . . . . . . . RN7SL735P . . . RNA, 7SL, cytoplasmic 735, pseudogene . . . . . . . . . . . RN7SL736P . . . RNA, 7SL, cytoplasmic 736, pseudogene . . . . . . . . . . . RN7SL737P . . . RNA, 7SL, cytoplasmic 737, pseudogene . . . . . . . . . . . RN7SL738P . . . RNA, 7SL, cytoplasmic 738, pseudogene . . . . . . . . . . . RN7SL740P . . . RNA, 7SL, cytoplasmic 740, pseudogene . . . . . . . . . . . RN7SL741P . . . RNA, 7SL, cytoplasmic 741, pseudogene . . . . . . . . . . . RN7SL743P . . . RNA, 7SL, cytoplasmic 743, pseudogene . . . . . . . . . . . RN7SL744P . . . RNA, 7SL, cytoplasmic 744, pseudogene . . . . . . . . . . . RN7SL745P . . . RNA, 7SL, cytoplasmic 745, pseudogene . . . . . . . . . . . RN7SL748P . . . RNA, 7SL, cytoplasmic 748, pseudogene . . . . . . . . . . . RN7SL749P . . . RNA, 7SL, cytoplasmic 749, pseudogene . . . . . . . . . . . RN7SL750P . . . RNA, 7SL, cytoplasmic 750, pseudogene . . . . . . . . . . . RN7SL751P . . . RNA, 7SL, cytoplasmic 751, pseudogene . . . . . . . . . . . RN7SL752P . . . RNA, 7SL, cytoplasmic 752, pseudogene . . . . . . . . . . . RN7SL753P . . . RNA, 7SL, cytoplasmic 753, pseudogene . . . . . . . . . . . RN7SL754P . . . RNA, 7SL, cytoplasmic 754, pseudogene . . . . . . . . . . . RN7SL756P . . . RNA, 7SL, cytoplasmic 756, pseudogene . . . . . . . . . . . RN7SL757P . . . RNA, 7SL, cytoplasmic 757, pseudogene . . . . . . . . . . . RN7SL759P . . . RNA, 7SL, cytoplasmic 759, pseudogene . . . . . . . . . . . RN7SL760P . . . RNA, 7SL, cytoplasmic 760, pseudogene . . . . . . . . . . . RN7SL761P . . . RNA, 7SL, cytoplasmic 761, pseudogene . . . . . . . . . . . RN7SL762P . . . RNA, 7SL, cytoplasmic 762, pseudogene . . . . . . . . . . . RN7SL763P . . . RNA, 7SL, cytoplasmic 763, pseudogene . . . . . . . . . . . RN7SL764P . . . RNA, 7SL, cytoplasmic 764, pseudogene . . . . . . . . . . . RN7SL766P . . . RNA, 7SL, cytoplasmic 766, pseudogene . . . . . . . . . . . RN7SL767P . . . RNA, 7SL, cytoplasmic 767, pseudogene . . . . . . . . . . . RN7SL769P . . . RNA, 7SL, cytoplasmic 769, pseudogene . . . . . . . . . . . RN7SL771P . . . RNA, 7SL, cytoplasmic 771, pseudogene . . . . . . . . . . . RN7SL774P . . . RNA, 7SL, cytoplasmic 774, pseudogene . . . . . . . . . . . RN7SL775P . . . RNA, 7SL, cytoplasmic 775, pseudogene . . . . . . . . . . . RN7SL776P . . . RNA, 7SL, cytoplasmic 776, pseudogene . . . . . . . . . . . RN7SL778P . . . RNA, 7SL, cytoplasmic 778, pseudogene . . . . . . . . . . . RN7SL782P . . . RNA, 7SL, cytoplasmic 782, pseudogene . . . . . . . . . . . RN7SL783P . . . RNA, 7SL, cytoplasmic 783, pseudogene . . . . . . . . . . . RN7SL784P . . . RNA, 7SL, cytoplasmic 784, pseudogene . . . . . . . . . . . RN7SL785P . . . RNA, 7SL, cytoplasmic 785, pseudogene . . . . . . . . . . . RN7SL786P . . . RNA, 7SL, cytoplasmic 786, pseudogene . . . . . . . . . . . RN7SL787P . . . RNA, 7SL, cytoplasmic 787, pseudogene . . . . . . . . . . . RN7SL788P . . . RNA, 7SL, cytoplasmic 788, pseudogene . . . . . . . . . . . RN7SL789P . . . RNA, 7SL, cytoplasmic 789, pseudogene . . . . . . . . . . . RN7SL790P . . . RNA, 7SL, cytoplasmic 790, pseudogene . . . . . . . . . . . RN7SL791P . . . RNA, 7SL, cytoplasmic 791, pseudogene . . . . . . . . . . . RN7SL792P . . . RNA, 7SL, cytoplasmic 792, pseudogene . . . . . . . . . . . RN7SL793P . . . RNA, 7SL, cytoplasmic 793, pseudogene . . . . . . . . . . . RN7SL794P . . . RNA, 7SL, cytoplasmic 794, pseudogene . . . . . . . . . . . RN7SL795P . . . RNA, 7SL, cytoplasmic 795, pseudogene . . . . . . . . . . . RN7SL796P . . . RNA, 7SL, cytoplasmic 796, pseudogene . . . . . . . . . . . RN7SL797P . . . RNA, 7SL, cytoplasmic 797, pseudogene . . . . . . . . . . . RN7SL798P . . . RNA, 7SL, cytoplasmic 798, pseudogene . . . . . . . . . . . RN7SL799P . . . RNA, 7SL, cytoplasmic 799, pseudogene . . . . . . . . . . . RN7SL800P . . . RNA, 7SL, cytoplasmic 800, pseudogene . . . . . . . . . . . RN7SL801P . . . RNA, 7SL, cytoplasmic 801, pseudogene . . . . . . . . . . . RN7SL802P . . . RNA, 7SL, cytoplasmic 802, pseudogene . . . . . . . . . . . RN7SL803P . . . RNA, 7SL, cytoplasmic 803, pseudogene . . . . . . . . . . . RN7SL804P . . . RNA, 7SL, cytoplasmic 804, pseudogene . . . . . . . . . . . RN7SL806P . . . RNA, 7SL, cytoplasmic 806, pseudogene . . . . . . . . . . . RN7SL807P . . . RNA, 7SL, cytoplasmic 807, pseudogene . . . . . . . . . . . RN7SL808P . . . RNA, 7SL, cytoplasmic 808, pseudogene . . . . . . . . . . . RN7SL809P . . . RNA, 7SL, cytoplasmic 809, pseudogene . . . . . . . . . . . RN7SL810P . . . RNA, 7SL, cytoplasmic 810, pseudogene . . . . . . . . . . . RN7SL811P . . . RNA, 7SL, cytoplasmic 811, pseudogene . . . . . . . . . . . RN7SL812P . . . RNA, 7SL, cytoplasmic 812, pseudogene . . . . . . . . . . . RN7SL813P . . . RNA, 7SL, cytoplasmic 813, pseudogene . . . . . . . . . . . RN7SL814P . . . RNA, 7SL, cytoplasmic 814, pseudogene . . . . . . . . . . . RN7SL815P . . . RNA, 7SL, cytoplasmic 815, pseudogene . . . . . . . . . . . RN7SL817P . . . RNA, 7SL, cytoplasmic 817, pseudogene . . . . . . . . . . . RN7SL818P . . . RNA, 7SL, cytoplasmic 818, pseudogene . . . . . . . . . . . RN7SL819P . . . RNA, 7SL, cytoplasmic 819, pseudogene . . . . . . . . . . . RN7SL820P . . . RNA, 7SL, cytoplasmic 820, pseudogene . . . . . . . . . . . RN7SL822P . . . RNA, 7SL, cytoplasmic 822, pseudogene . . . . . . . . . . . RN7SL823P . . . RNA, 7SL, cytoplasmic 823, pseudogene . . . . . . . . . . . RN7SL824P . . . RNA, 7SL, cytoplasmic 824, pseudogene . . . . . . . . . . . RN7SL825P . . . RNA, 7SL, cytoplasmic 825, pseudogene . . . . . . . . . . . RN7SL826P . . . RNA, 7SL, cytoplasmic 826, pseudogene . . . . . . . . . . . RN7SL827P . . . RNA, 7SL, cytoplasmic 827, pseudogene . . . . . . . . . . . RN7SL828P . . . RNA, 7SL, cytoplasmic 828, pseudogene . . . . . . . . . . . RN7SL831P . . . RNA, 7SL, cytoplasmic 831, pseudogene . . . . . . . . . . . RN7SL832P . . . RNA, 7SL, cytoplasmic 832, pseudogene . . . . . . . . . . . RN7SL833P . . . RNA, 7SL, cytoplasmic 833, pseudogene . . . . . . . . . . . RN7SL834P . . . RNA, 7SL, cytoplasmic 834, pseudogene . . . . . . . . . . . RN7SL835P . . . RNA, 7SL, cytoplasmic 835, pseudogene . . . . . . . . . . . RN7SL836P . . . RNA, 7SL, cytoplasmic 836, pseudogene . . . . . . . . . . . RN7SL837P . . . RNA, 7SL, cytoplasmic 837, pseudogene . . . . . . . . . . . RN7SL838P . . . RNA, 7SL, cytoplasmic 838, pseudogene . . . . . . . . . . . RN7SL840P . . . RNA, 7SL, cytoplasmic 840, pseudogene . . . . . . . . . . . RN7SL841P . . . RNA, 7SL, cytoplasmic 841, pseudogene . . . . . . . . . . . RN7SL842P . . . RNA, 7SL, cytoplasmic 842, pseudogene . . . . . . . . . . . RN7SL843P . . . RNA, 7SL, cytoplasmic 843, pseudogene . . . . . . . . . . . RN7SL845P . . . RNA, 7SL, cytoplasmic 845, pseudogene . . . . . . . . . . . RN7SL846P . . . RNA, 7SL, cytoplasmic 846, pseudogene . . . . . . . . . . . RN7SL847P . . . RNA, 7SL, cytoplasmic 847, pseudogene . . . . . . . . . . . RN7SL849P . . . RNA, 7SL, cytoplasmic 849, pseudogene . . . . . . . . . . . RN7SL850P . . . RNA, 7SL, cytoplasmic 850, pseudogene . . . . . . . . . . . RN7SL851P . . . RNA, 7SL, cytoplasmic 851, pseudogene . . . . . . . . . . . RN7SL853P . . . RNA, 7SL, cytoplasmic 853, pseudogene . . . . . . . . . . . RN7SL854P . . . RNA, 7SL, cytoplasmic 854, pseudogene . . . . . . . . . . . RN7SL856P . . . RNA, 7SL, cytoplasmic 856, pseudogene . . . . . . . . . . . RN7SL860P . . . RNA, 7SL, cytoplasmic 860, pseudogene . . . . . . . . . . . RN7SL861P . . . RNA, 7SL, cytoplasmic 861, pseudogene . . . . . . . . . . . RN7SL862P . . . RNA, 7SL, cytoplasmic 862, pseudogene . . . . . . . . . . . RN7SL863P . . . RNA, 7SL, cytoplasmic 863, pseudogene . . . . . . . . . . . RN7SL864P . . . RNA, 7SL, cytoplasmic 864, pseudogene . . . . . . . . . . . RN7SL865P . . . RNA, 7SL, cytoplasmic 865, pseudogene . . . . . . . . . . . RN7SL868P . . . RNA, 7SL, cytoplasmic 868, pseudogene . . . . . . . . . . . RN7SL869P . . . RNA, 7SL, cytoplasmic 869, pseudogene . . . . . . . . . . . RN7SL870P . . . RNA, 7SL, cytoplasmic 870, pseudogene . . . . . . . . . . . RNA5-8S1 . . . RNA, 5.8S ribosomal 1 . . . . . . . . . . . RNA5-8S2 . . . RNA, 5.8S ribosomal 2 . . . . . . . . . . . RNA5-8S3 . . . RNA, 5.8S ribosomal 3 . . . . . . . . . . . RNA5-8S4 . . . RNA, 5.8S ribosomal 4 . . . . . . . . . . . RNA5-8S5 . . . RNA, 5.8S ribosomal 5 . . . . . . . . . . . RNA5-8SP2 . . . RNA, 5.8S ribosomal pseudogene 2 . . . . . . . . . . . RNA5-8SP3 . . . RNA, 5.8S ribosomal pseudogene 3 . . . . . . . . . . . RNA5-8SP4 . . . RNA, 5.8S ribosomal pseudogene 4 . . . . . . . . . . . RNA5-8SP5 . . . RNA, 5.8S ribosomal pseudogene 5 . . . . . . . . . . . RNA5-8SP6 . . . RNA, 5.8S ribosomal pseudogene 6 . . . . . . . . . . . RNA5-8SP7 . . . RNA, 5.8S ribosomal pseudogene 7 . . . . . . . . . . . RNA5S1 . . . RNA, 5S ribosomal 1 . . . . . . . . . . . RNA5S2 . . . RNA, 5S ribosomal 2 . . . . . . . . . . . RNA5S3 . . . RNA, 5S ribosomal 3 . . . . . . . . . . . RNA5S4 . . . RNA, 5S ribosomal 4 . . . . . . . . . . . RNA5S5 . . . RNA, 5S ribosomal 5 . . . . . . . . . . . RNA5S6 . . . RNA, 5S ribosomal 6 . . . . . . . . . . . RNA5S7 . . . RNA, 5S ribosomal 7 . . . . . . . . . . . RNA5S8 . . . RNA, 5S ribosomal 8 . . . . . . . . . . . RNA5S9 . . . RNA, 5S ribosomal 9 . . . . . . . . . . . RNA5S10 . . . RNA, 5S ribosomal 10 . . . . . . . . . . . RNA5S11 . . . RNA, 5S ribosomal 11 . . . . . . . . . . . RNA5S12 . . . RNA, 5S ribosomal 12 . . . . . . . . . . . RNA5S13 . . . RNA, 5S ribosomal 13 . . . . . . . . . . . RNA5S14 . . . RNA, 5S ribosomal 14 . . . . . . . . . . . RNA5S15 . . . RNA, 5S ribosomal 15 . . . . . . . . . . . RNA5S16 . . . RNA, 5S ribosomal 16 . . . . . . . . . . . RNA5S17 . . . RNA, 5S ribosomal 17 . . . . . . . . . . . RNA5SP18 . . . RNA, 5S ribosomal pseudogene 18 . . . . . . . . . . . RNA5SP19 . . . RNA, 5S ribosomal pseudogene 19 . . . . . . . . . . . RNA5SP20 . . . RNA, 5S ribosomal pseudogene 20 . . . . . . . . . . . RNA5SP21 . . . RNA, 5S ribosomal pseudogene 21 . . . . . . . . . . . RNA5SP22 . . . RNA, 5S ribosomal pseudogene 22 . . . . . . . . . . . RNA5SP23 . . . RNA, 5S ribosomal pseudogene 23 . . . . . . . . . . . RNA5SP24 . . . RNA, 5S ribosomal pseudogene 24 . . . . . . . . . . . RNA5SP25 . . . RNA, 5S ribosomal pseudogene 25 . . . . . . . . . . . RNA5SP26 . . . RNA, 5S ribosomal pseudogene 26 . . . . . . . . . . . RNA5SP27 . . . RNA, 5S ribosomal pseudogene 27 . . . . . . . . . . . RNA5SP28 . . . RNA, 5S ribosomal pseudogene 28 . . . . . . . . . . . RNA5SP29 . . . RNA, 5S ribosomal pseudogene 29 . . . . . . . . . . . RNA5SP30 . . . RNA, 5S ribosomal pseudogene 30 . . . . . . . . . . . RNA5SP31 . . . RNA, 5S ribosomal pseudogene 31 . . . . . . . . . . . RNA5SP32 . . . RNA, 5S ribosomal pseudogene 32 . . . . . . . . . . . RNA5SP33 . . . RNA, 5S ribosomal pseudogene 33 . . . . . . . . . . . RNA5SP34 . . . RNA, 5S ribosomal pseudogene 34 . . . . . . . . . . . RNA5SP35 . . . RNA, 5S ribosomal pseudogene 35 . . . . . . . . . . . RNA5SP36 . . . RNA, 5S ribosomal pseudogene 36 . . . . . . . . . . . RNA5SP37 . . . RNA, 5S ribosomal pseudogene 37 . . . . . . . . . . . RNA5SP38 . . . RNA, 5S ribosomal pseudogene 38 . . . . . . . . . . . RNA5SP39 . . . RNA, 5S ribosomal pseudogene 39 . . . . . . . . . . . RNA5SP40 . . . RNA, 5S ribosomal pseudogene 40 . . . . . . . . . . . RNA5SP41 . . . RNA, 5S ribosomal pseudogene 41 . . . . . . . . . . . RNA5SP42 . . . RNA, 5S ribosomal pseudogene 42 . . . . . . . . . . . RNA5SP43 . . . RNA, 5S ribosomal pseudogene 43 . . . . . . . . . . . RNA5SP44 . . . RNA, 5S ribosomal pseudogene 44 . . . . . . . . . . . RNA5SP45 . . . RNA, 5S ribosomal pseudogene 45 . . . . . . . . . . . RNA5SP46 . . . RNA, 5S ribosomal pseudogene 46 . . . . . . . . . . . RNA5SP47 . . . RNA, 5S ribosomal pseudogene 47 . . . . . . . . . . . RNA5SP48 . . . RNA, 5S ribosomal pseudogene 48 . . . . . . . . . . . RNA5SP49 . . . RNA, 5S ribosomal pseudogene 49 . . . . . . . . . . . RNA5SP50 . . . RNA, 5S ribosomal pseudogene 50 . . . . . . . . . . . RNA5SP51 . . . RNA, 5S ribosomal pseudogene 51 . . . . . . . . . . . RNA5SP52 . . . RNA, 5S ribosomal pseudogene 52 . . . . . . . . . . . RNA5SP53 . . . RNA, 5S ribosomal pseudogene 53 . . . . . . . . . . . RNA5SP54 . . . RNA, 5S ribosomal pseudogene 54 . . . . . . . . . . . RNA5SP55 . . . RNA, 5S ribosomal pseudogene 55 . . . . . . . . . . . RNA5SP56 . . . RNA, 5S ribosomal pseudogene 56 . . . . . . . . . . . RNA5SP57 . . . RNA, 5S ribosomal pseudogene 57 . . . . . . . . . . . RNA5SP59 . . . RNA, 5S ribosomal pseudogene 59 . . . . . . . . . . . RNA5SP60 . . . RNA, 5S ribosomal pseudogene 60 . . . . . . . . . . . RNA5SP61 . . . RNA, 5S ribosomal pseudogene 61 . . . . . . . . . . . RNA5SP62 . . . RNA, 5S ribosomal pseudogene 62 . . . . . . . . . . . RNA5SP63 . . . RNA, 5S ribosomal pseudogene 63 . . . . . . . . . . . RNA5SP64 . . . RNA, 5S ribosomal pseudogene 64 . . . . . . . . . . . RNA5SP65 . . . RNA, 5S ribosomal pseudogene 65 . . . . . . . . . . . RNA5SP66 . . . RNA, 5S ribosomal pseudogene 66 . . . . . . . . . . . RNA5SP67 . . . RNA, 5S ribosomal pseudogene 67 . . . . . . . . . . . RNA5SP68 . . . RNA, 5S ribosomal pseudogene 68 . . . . . . . . . . . RNA5SP69 . . . RNA, 5S ribosomal pseudogene 69 . . . . . . . . . . . RNA5SP70 . . . RNA, 5S ribosomal pseudogene 70 . . . . . . . . . . . RNA5SP71 . . . RNA, 5S ribosomal pseudogene 71 . . . . . . . . . . . RNA5SP72 . . . RNA, 5S ribosomal pseudogene 72 . . . . . . . . . . . RNA5SP73 . . . RNA, 5S ribosomal pseudogene 73 . . . . . . . . . . . RNA5SP74 . . . RNA, 5S ribosomal pseudogene 74 . . . . . . . . . . . RNA5SP75 . . . RNA, 5S ribosomal pseudogene 75 . . . . . . . . . . . RNA5SP76 . . . RNA, 5S ribosomal pseudogene 76 . . . . . . . . . . . RNA5SP77 . . . RNA, 5S ribosomal pseudogene 77 . . . . . . . . . . . RNA5SP78 . . . RNA, 5S ribosomal pseudogene 78 . . . . . . . . . . . RNA5SP79 . . . RNA, 5S ribosomal pseudogene 79 . . . . . . . . . . . RNA5SP80 . . . RNA, 5S ribosomal pseudogene 80 . . . . . . . . . . . RNA5SP81 . . . RNA, 5S ribosomal pseudogene 81 . . . . . . . . . . . RNA5SP82 . . . RNA, 5S ribosomal pseudogene 82 . . . . . . . . . . . RNA5SP84 . . . RNA, 5S ribosomal pseudogene 84 . . . . . . . . . . . RNA5SP85 . . . RNA, 5S ribosomal pseudogene 85 . . . . . . . . . . . RNA5SP86 . . . RNA, 5S ribosomal pseudogene 86 . . . . . . . . . . . RNA5SP87 . . . RNA, 5S ribosomal pseudogene 87 . . . . . . . . . . . RNA5SP88 . . . RNA, 5S ribosomal pseudogene 88 . . . . . . . . . . . RNA5SP89 . . . RNA, 5S ribosomal pseudogene 89 . . . . . . . . . . . RNA5SP90 . . . RNA, 5S ribosomal pseudogene 90 . . . . . . . . . . . RNA5SP91 . . . RNA, 5S ribosomal pseudogene 91 . . . . . . . . . . . RNA5SP92 . . . RNA, 5S ribosomal pseudogene 92 . . . . . . . . . . . RNA5SP93 . . . RNA, 5S ribosomal pseudogene 93 . . . . . . . . . . . RNA5SP94 . . . RNA, 5S ribosomal pseudogene 94 . . . . . . . . . . . RNA5SP95 . . . RNA, 5S ribosomal pseudogene 95 . . . . . . . . . . . RNA5SP96 . . . RNA, 5S ribosomal pseudogene 96 . . . . . . . . . . . RNA5SP97 . . . RNA, 5S ribosomal pseudogene 97 . . . . . . . . . . . RNA5SP98 . . . RNA, 5S ribosomal pseudogene 98 . . . . . . . . . . . RNA5SP99 . . . RNA, 5S ribosomal pseudogene 99 . . . . . . . . . . . RNA5SP100 . . . RNA, 5S ribosomal pseudogene 100 . . . . . . . . . . . RNA5SP101 . . . RNA, 5S ribosomal pseudogene 101 . . . . . . . . . . . RNA5SP102 . . . RNA, 5S ribosomal pseudogene 102 . . . . . . . . . . . RNA5SP103 . . . RNA, 5S ribosomal pseudogene 103 . . . . . . . . . . . RNA5SP104 . . . RNA, 5S ribosomal pseudogene 104 . . . . . . . . . . . RNA5SP105 . . . RNA, 5S ribosomal pseudogene 105 . . . . . . . . . . . RNA5SP106 . . . RNA, 5S ribosomal pseudogene 106 . . . . . . . . . . . RNA5SP107 . . . RNA, 5S ribosomal pseudogene 107 . . . . . . . . . . . RNA5SP108 . . . RNA, 5S ribosomal pseudogene 108 . . . . . . . . . . . RNA5SP109 . . . RNA, 5S ribosomal pseudogene 109 . . . . . . . . . . . RNA5SP110 . . . RNA, 5S ribosomal pseudogene 110 . . . . . . . . . . . RNA5SP111 . . . RNA, 5S ribosomal pseudogene 111 . . . . . . . . . . . RNA5SP112 . . . RNA, 5S ribosomal pseudogene 112 . . . . . . . . . . . RNA5SP113 . . . RNA, 5S ribosomal pseudogene 113 . . . . . . . . . . . RNA5SP114 . . . RNA, 5S ribosomal pseudogene 114 . . . . . . . . . . . RNA5SP115 . . . RNA, 5S ribosomal pseudogene 115 . . . . . . . . . . . RNA5SP116 . . . RNA, 5S ribosomal pseudogene 116 . . . . . . . . . . . RNA5SP117 . . . RNA, 5S ribosomal pseudogene 117 . . . . . . . . . . . RNA5SP118 . . . RNA, 5S ribosomal pseudogene 118 . . . . . . . . . . . RNA5SP119 . . . RNA, 5S ribosomal pseudogene 119 . . . . . . . . . . . RNA5SP120 . . . RNA, 5S ribosomal pseudogene 120 . . . . . . . . . . . RNA5SP121 . . . RNA, 5S ribosomal pseudogene 121 . . . . . . . . . . . RNA5SP122 . . . RNA, 5S ribosomal pseudogene 122 . . . . . . . . . . . RNA5SP123 . . . RNA, 5S ribosomal pseudogene 123 . . . . . . . . . . . RNA5SP124 . . . RNA, 5S ribosomal pseudogene 124 . . . . . . . . . . . RNA5SP125 . . . RNA, 5S ribosomal pseudogene 125 . . . . . . . . . . . RNA5SP126 . . . RNA, 5S ribosomal pseudogene 126 . . . . . . . . . . . RNA5SP127 . . . RNA, 5S ribosomal pseudogene 127 . . . . . . . . . . . RNA5SP128 . . . RNA, 5S ribosomal pseudogene 128 . . . . . . . . . . . RNA5SP129 . . . RNA, 5S ribosomal pseudogene 129 . . . . . . . . . . . RNA5SP130 . . . RNA, 5S ribosomal pseudogene 130 . . . . . . . . . . . RNA5SP131 . . . RNA, 5S ribosomal pseudogene 131 . . . . . . . . . . . RNA5SP132 . . . RNA, 5S ribosomal pseudogene 132 . . . . . . . . . . . RNA5SP133 . . . RNA, 5S ribosomal pseudogene 133 . . . . . . . . . . . RNA5SP134 . . . RNA, 5S ribosomal pseudogene 134 . . . . . . . . . . . RNA5SP135 . . . RNA, 5S ribosomal pseudogene 135 . . . . . . . . . . . RNA5SP136 . . . RNA, 5S ribosomal pseudogene 136 . . . . . . . . . . . RNA5SP137 . . . RNA, 5S ribosomal pseudogene 137 . . . . . . . . . . . RNA5SP138 . . . RNA, 5S ribosomal pseudogene 138 . . . . . . . . . . . RNA5SP139 . . . RNA, 5S ribosomal pseudogene 139 . . . . . . . . . . . RNA5SP140 . . . RNA, 5S ribosomal pseudogene 140 . . . . . . . . . . . RNA5SP141 . . . RNA, 5S ribosomal pseudogene 141 . . . . . . . . . . . RNA5SP142 . . . RNA, 5S ribosomal pseudogene 142 . . . . . . . . . . . RNA5SP143 . . . RNA, 5S ribosomal pseudogene 143 . . . . . . . . . . . RNA5SP144 . . . RNA, 5S ribosomal pseudogene 144 . . . . . . . . . . . RNA5SP145 . . . RNA, 5S ribosomal pseudogene 145 . . . . . . . . . . . RNA5SP146 . . . RNA, 5S ribosomal pseudogene 146 . . . . . . . . . . . RNA5SP147 . . . RNA, 5S ribosomal pseudogene 147 . . . . . . . . . . . RNA5SP148 . . . RNA, 5S ribosomal pseudogene 148 . . . . . . . . . . . RNA5SP149 . . . RNA, 5S ribosomal pseudogene 149 . . . . . . . . . . . RNA5SP150 . . . RNA, 5S ribosomal pseudogene 150 . . . . . . . . . . . RNA5SP151 . . . RNA, 5S ribosomal pseudogene 151 . . . . . . . . . . . RNA5SP152 . . . RNA, 5S ribosomal pseudogene 152 . . . . . . . . . . . RNA5SP153 . . . RNA, 5S ribosomal pseudogene 153 . . . . . . . . . . . RNA5SP154 . . . RNA, 5S ribosomal pseudogene 154 . . . . . . . . . . . RNA5SP155 . . . RNA, 5S ribosomal pseudogene 155 . . . . . . . . . . . RNA5SP156 . . . RNA, 5S ribosomal pseudogene 156 . . . . . . . . . . . RNA5SP157 . . . RNA, 5S ribosomal pseudogene 157 . . . . . . . . . . . RNA5SP158 . . . RNA, 5S ribosomal pseudogene 158 . . . . . . . . . . . RNA5SP159 . . . RNA, 5S ribosomal pseudogene 159 . . . . . . . . . . . RNA5SP160 . . . RNA, 5S ribosomal pseudogene 160 . . . . . . . . . . . RNA5SP161 . . . RNA, 5S ribosomal pseudogene 161 . . . . . . . . . . . RNA5SP162 . . . RNA, 5S ribosomal pseudogene 162 . . . . . . . . . . . RNA5SP163 . . . RNA, 5S ribosomal pseudogene 163 . . . . . . . . . . . RNA5SP164 . . . RNA, 5S ribosomal pseudogene 164 . . . . . . . . . . . RNA5SP165 . . . RNA, 5S ribosomal pseudogene 165 . . . . . . . . . . . RNA5SP166 . . . RNA, 5S ribosomal pseudogene 166 . . . . . . . . . . . RNA5SP167 . . . RNA, 5S ribosomal pseudogene 167 . . . . . . . . . . . RNA5SP168 . . . RNA, 5S ribosomal pseudogene 168 . . . . . . . . . . . RNA5SP169 . . . RNA, 5S ribosomal pseudogene 169 . . . . . . . . . . . RNA5SP170 . . . RNA, 5S ribosomal pseudogene 170 . . . . . . . . . . . RNA5SP171 . . . RNA, 5S ribosomal pseudogene 171 . . . . . . . . . . . RNA5SP172 . . . RNA, 5S ribosomal pseudogene 172 . . . . . . . . . . . RNA5SP173 . . . RNA, 5S ribosomal pseudogene 173 . . . . . . . . . . . RNA5SP174 . . . RNA, 5S ribosomal pseudogene 174 . . . . . . . . . . . RNA5SP175 . . . RNA, 5S ribosomal pseudogene 175 . . . . . . . . . . . RNA5SP176 . . . RNA, 5S ribosomal pseudogene 176 . . . . . . . . . . . RNA5SP177 . . . RNA, 5S ribosomal pseudogene 177 . . . . . . . . . . . RNA5SP178 . . . RNA, 5S ribosomal pseudogene 178 . . . . . . . . . . . RNA5SP179 . . . RNA, 5S ribosomal pseudogene 179 . . . . . . . . . . . RNA5SP180 . . . RNA, 5S ribosomal pseudogene 180 . . . . . . . . . . . RNA5SP181 . . . RNA, 5S ribosomal pseudogene 181 . . . . . . . . . . . RNA5SP182 . . . RNA, 5S ribosomal pseudogene 182 . . . . . . . . . . . RNA5SP183 . . . RNA, 5S ribosomal pseudogene 183 . . . . . . . . . . . RNA5SP184 . . . RNA, 5S ribosomal pseudogene 184 . . . . . . . . . . . RNA5SP185 . . . RNA, 5S ribosomal pseudogene 185 . . . . . . . . . . . RNA5SP186 . . . RNA, 5S ribosomal pseudogene 186 . . . . . . . . . . . RNA5SP187 . . . RNA, 5S ribosomal pseudogene 187 . . . . . . . . . . . RNA5SP188 . . . RNA, 5S ribosomal pseudogene 188 . . . . . . . . . . . RNA5SP189 . . . RNA, 5S ribosomal pseudogene 189 . . . . . . . . . . . RNA5SP190 . . . RNA, 5S ribosomal pseudogene 190 . . . . . . . . . . . RNA5SP191 . . . RNA, 5S ribosomal pseudogene 191 . . . . . . . . . . . RNA5SP192 . . . RNA, 5S ribosomal pseudogene 192 . . . . . . . . . . . RNA5SP193 . . . RNA, 5S ribosomal pseudogene 193 . . . . . . . . . . . RNA5SP194 . . . RNA, 5S ribosomal pseudogene 194 . . . . . . . . . . . RNA5SP195 . . . RNA, 5S ribosomal pseudogene 195 . . . . . . . . . . . RNA5SP196 . . . RNA, 5S ribosomal pseudogene 196 . . . . . . . . . . . RNA5SP197 . . . RNA, 5S ribosomal pseudogene 197 . . . . . . . . . . . RNA5SP198 . . . RNA, 5S ribosomal pseudogene 198 . . . . . . . . . . . RNA5SP199 . . . RNA, 5S ribosomal pseudogene 199 . . . . . . . . . . . RNA5SP200 . . . RNA, 5S ribosomal pseudogene 200 . . . . . . . . . . . RNA5SP201 . . . RNA, 5S ribosomal pseudogene 201 . . . . . . . . . . . RNA5SP202 . . . RNA, 5S ribosomal pseudogene 202 . . . . . . . . . . . RNA5SP203 . . . RNA, 5S ribosomal pseudogene 203 . . . . . . . . . . . RNA5SP204 . . . RNA, 5S ribosomal pseudogene 204 . . . . . . . . . . . RNA5SP205 . . . RNA, 5S ribosomal pseudogene 205 . . . . . . . . . . . RNA5SP206 . . . RNA, 5S ribosomal pseudogene 206 . . . . . . . . . . . RNA5SP207 . . . RNA, 5S ribosomal pseudogene 207 . . . . . . . . . . . RNA5SP208 . . . RNA, 5S ribosomal pseudogene 208 . . . . . . . . . . . RNA5SP209 . . . RNA, 5S ribosomal pseudogene 209 . . . . . . . . . . . RNA5SP210 . . . RNA, 5S ribosomal pseudogene 210 . . . . . . . . . . . RNA5SP211 . . . RNA, 5S ribosomal pseudogene 211 . . . . . . . . . . . RNA5SP212 . . . RNA, 5S ribosomal pseudogene 212 . . . . . . . . . . . RNA5SP213 . . . RNA, 5S ribosomal pseudogene 213 . . . . . . . . . . . RNA5SP214 . . . RNA, 5S ribosomal pseudogene 214 . . . . . . . . . . . RNA5SP215 . . . RNA, 5S ribosomal pseudogene 215 . . . . . . . . . . . RNA5SP216 . . . RNA, 5S ribosomal pseudogene 216 . . . . . . . . . . . RNA5SP217 . . . RNA, 5S ribosomal pseudogene 217 . . . . . . . . . . . RNA5SP218 . . . RNA, 5S ribosomal pseudogene 218 . . . . . . . . . . . RNA5SP219 . . . RNA, 5S ribosomal pseudogene 219 . . . . . . . . . . . RNA5SP220 . . . RNA, 5S ribosomal pseudogene 220 . . . . . . . . . . . RNA5SP221 . . . RNA, 5S ribosomal pseudogene 221 . . . . . . . . . . . RNA5SP222 . . . RNA, 5S ribosomal pseudogene 222 . . . . . . . . . . . RNA5SP223 . . . RNA, 5S ribosomal pseudogene 223 . . . . . . . . . . . RNA5SP224 . . . RNA, 5S ribosomal pseudogene 224 . . . . . . . . . . . RNA5SP225 . . . RNA, 5S ribosomal pseudogene 225 . . . . . . . . . . . RNA5SP226 . . . RNA, 5S ribosomal pseudogene 226 . . . . . . . . . . . RNA5SP227 . . . RNA, 5S ribosomal pseudogene 227 . . . . . . . . . . . RNA5SP228 . . . RNA, 5S ribosomal pseudogene 228 . . . . . . . . . . . RNA5SP229 . . . RNA, 5S ribosomal pseudogene 229 . . . . . . . . . . . RNA5SP230 . . . RNA, 5S ribosomal pseudogene 230 . . . . . . . . . . . RNA5SP231 . . . RNA, 5S ribosomal pseudogene 231 . . . . . . . . . . . RNA5SP232 . . . RNA, 5S ribosomal pseudogene 232 . . . . . . . . . . . RNA5SP233 . . . RNA, 5S ribosomal pseudogene 233 . . . . . . . . . . . RNA5SP234 . . . RNA, 5S ribosomal pseudogene 234 . . . . . . . . . . . RNA5SP235 . . . RNA, 5S ribosomal pseudogene 235 . . . . . . . . . . . RNA5SP236 . . . RNA, 5S ribosomal pseudogene 236 . . . . . . . . . . . RNA5SP237 . . . RNA, 5S ribosomal pseudogene 237 . . . . . . . . . . . RNA5SP238 . . . RNA, 5S ribosomal pseudogene 238 . . . . . . . . . . . RNA5SP239 . . . RNA, 5S ribosomal pseudogene 239 . . . . . . . . . . . RNA5SP240 . . . RNA, 5S ribosomal pseudogene 240 . . . . . . . . . . . RNA5SP241 . . . RNA, 5S ribosomal pseudogene 241 . . . . . . . . . . . RNA5SP242 . . . RNA, 5S ribosomal pseudogene 242 . . . . . . . . . . . RNA5SP243 . . . RNA, 5S ribosomal pseudogene 243 . . . . . . . . . . . RNA5SP244 . . . RNA, 5S ribosomal pseudogene 244 . . . . . . . . . . . RNA5SP245 . . . RNA, 5S ribosomal pseudogene 245 . . . . . . . . . . . RNA5SP246 . . . RNA, 5S ribosomal pseudogene 246 . . . . . . . . . . . RNA5SP247 . . . RNA, 5S ribosomal pseudogene 247 . . . . . . . . . . . RNA5SP248 . . . RNA, 5S ribosomal pseudogene 248 . . . . . . . . . . . RNA5SP249 . . . RNA, 5S ribosomal pseudogene 249 . . . . . . . . . . . RNA5SP250 . . . RNA, 5S ribosomal pseudogene 250 . . . . . . . . . . . RNA5SP251 . . . RNA, 5S ribosomal pseudogene 251 . . . . . . . . . . . RNA5SP252 . . . RNA, 5S ribosomal pseudogene 252 . . . . . . . . . . . RNA5SP253 . . . RNA, 5S ribosomal pseudogene 253 . . . . . . . . . . . RNA5SP254 . . . RNA, 5S ribosomal pseudogene 254 . . . . . . . . . . . RNA5SP255 . . . RNA, 5S ribosomal pseudogene 255 . . . . . . . . . . . RNA5SP256 . . . RNA, 5S ribosomal pseudogene 256 . . . . . . . . . . . RNA5SP257 . . . RNA, 5S ribosomal pseudogene 257 . . . . . . . . . . . RNA5SP258 . . . RNA, 5S ribosomal pseudogene 258 . . . . . . . . . . . RNA5SP259 . . . RNA, 5S ribosomal pseudogene 259 . . . . . . . . . . . RNA5SP260 . . . RNA, 5S ribosomal pseudogene 260 . . . . . . . . . . . RNA5SP261 . . . RNA, 5S ribosomal pseudogene 261 . . . . . . . . . . . RNA5SP262 . . . RNA, 5S ribosomal pseudogene 262 . . . . . . . . . . . RNA5SP263 . . . RNA, 5S ribosomal pseudogene 263 . . . . . . . . . . . RNA5SP264 . . . RNA, 5S ribosomal pseudogene 264 . . . . . . . . . . . RNA5SP265 . . . RNA, 5S ribosomal pseudogene 265 . . . . . . . . . . . RNA5SP266 . . . RNA, 5S ribosomal pseudogene 266 . . . . . . . . . . . RNA5SP267 . . . RNA, 5S ribosomal pseudogene 267 . . . . . . . . . . . RNA5SP268 . . . RNA, 5S ribosomal pseudogene 268 . . . . . . . . . . . RNA5SP269 . . . RNA, 5S ribosomal pseudogene 269 . . . . . . . . . . . RNA5SP270 . . . RNA, 5S ribosomal pseudogene 270 . . . . . . . . . . . RNA5SP271 . . . RNA, 5S ribosomal pseudogene 271 . . . . . . . . . . . RNA5SP272 . . . RNA, 5S ribosomal pseudogene 272 . . . . . . . . . . . RNA5SP273 . . . RNA, 5S ribosomal pseudogene 273 . . . . . . . . . . . RNA5SP274 . . . RNA, 5S ribosomal pseudogene 274 . . . . . . . . . . . RNA5SP275 . . . RNA, 5S ribosomal pseudogene 275 . . . . . . . . . . . RNA5SP276 . . . RNA, 5S ribosomal pseudogene 276 . . . . . . . . . . . RNA5SP277 . . . RNA, 5S ribosomal pseudogene 277 . . . . . . . . . . . RNA5SP278 . . . RNA, 5S ribosomal pseudogene 278 . . . . . . . . . . . RNA5SP279 . . . RNA, 5S ribosomal pseudogene 279 . . . . . . . . . . . RNA5SP280 . . . RNA, 5S ribosomal pseudogene 280 . . . . . . . . . . . RNA5SP281 . . . RNA, 5S ribosomal pseudogene 281 . . . . . . . . . . . RNA5SP282 . . . RNA, 5S ribosomal pseudogene 282 . . . . . . . . . . . RNA5SP283 . . . RNA, 5S ribosomal pseudogene 283 . . . . . . . . . . . RNA5SP284 . . . RNA, 5S ribosomal pseudogene 284 . . . . . . . . . . . RNA5SP285 . . . RNA, 5S ribosomal pseudogene 285 . . . . . . . . . . . RNA5SP286 . . . RNA, 5S ribosomal pseudogene 286 . . . . . . . . . . . RNA5SP287 . . . RNA, 5S ribosomal pseudogene 287 . . . . . . . . . . . RNA5SP288 . . . RNA, 5S ribosomal pseudogene 288 . . . . . . . . . . . RNA5SP289 . . . RNA, 5S ribosomal pseudogene 289 . . . . . . . . . . . RNA5SP290 . . . RNA, 5S ribosomal pseudogene 290 . . . . . . . . . . . RNA5SP291 . . . RNA, 5S ribosomal pseudogene 291 . . . . . . . . . . . RNA5SP292 . . . RNA, 5S ribosomal pseudogene 292 . . . . . . . . . . . RNA5SP293 . . . RNA, 5S ribosomal pseudogene 293 . . . . . . . . . . . RNA5SP294 . . . RNA, 5S ribosomal pseudogene 294 . . . . . . . . . . . RNA5SP295 . . . RNA, 5S ribosomal pseudogene 295 . . . . . . . . . . . RNA5SP296 . . . RNA, 5S ribosomal pseudogene 296 . . . . . . . . . . . RNA5SP297 . . . RNA, 5S ribosomal pseudogene 297 . . . . . . . . . . . RNA5SP298 . . . RNA, 5S ribosomal pseudogene 298 . . . . . . . . . . . RNA5SP299 . . . RNA, 5S ribosomal pseudogene 299 . . . . . . . . . . . RNA5SP300 . . . RNA, 5S ribosomal pseudogene 300 . . . . . . . . . . . RNA5SP301 . . . RNA, 5S ribosomal pseudogene 301 . . . . . . . . . . . RNA5SP302 . . . RNA, 5S ribosomal pseudogene 302 . . . . . . . . . . . RNA5SP303 . . . RNA, 5S ribosomal pseudogene 303 . . . . . . . . . . . RNA5SP304 . . . RNA, 5S ribosomal pseudogene 304 . . . . . . . . . . . RNA5SP305 . . . RNA, 5S ribosomal pseudogene 305 . . . . . . . . . . . RNA5SP306 . . . RNA, 5S ribosomal pseudogene 306 . . . . . . . . . . . RNA5SP307 . . . RNA, 5S ribosomal pseudogene 307 . . . . . . . . . . . RNA5SP308 . . . RNA, 5S ribosomal pseudogene 308 . . . . . . . . . . . RNA5SP309 . . . RNA, 5S ribosomal pseudogene 309 . . . . . . . . . . . RNA5SP310 . . . RNA, 5S ribosomal pseudogene 310 . . . . . . . . . . . RNA5SP311 . . . RNA, 5S ribosomal pseudogene 311 . . . . . . . . . . . RNA5SP312 . . . RNA, 5S ribosomal pseudogene 312 . . . . . . . . . . . RNA5SP315 . . . RNA, 5S ribosomal pseudogene 315 . . . . . . . . . . . RNA5SP317 . . . RNA, 5S ribosomal pseudogene 317 . . . . . . . . . . . RNA5SP318 . . . RNA, 5S ribosomal pseudogene 318 . . . . . . . . . . . RNA5SP319 . . . RNA, 5S ribosomal pseudogene 319 . . . . . . . . . . . RNA5SP320 . . . RNA, 5S ribosomal pseudogene 320 . . . . . . . . . . . RNA5SP321 . . . RNA, 5S ribosomal pseudogene 321 . . . . . . . . . . . RNA5SP322 . . . RNA, 5S ribosomal pseudogene 322 . . . . . . . . . . . RNA5SP323 . . . RNA, 5S ribosomal pseudogene 323 . . . . . . . . . . . RNA5SP324 . . . RNA, 5S ribosomal pseudogene 324 . . . . . . . . . . . RNA5SP325 . . . RNA, 5S ribosomal pseudogene 325 . . . . . . . . . . . RNA5SP326 . . . RNA, 5S ribosomal pseudogene 326 . . . . . . . . . . . RNA5SP327 . . . RNA, 5S ribosomal pseudogene 327 . . . . . . . . . . . RNA5SP328 . . . RNA, 5S ribosomal pseudogene 328 . . . . . . . . . . . RNA5SP329 . . . RNA, 5S ribosomal pseudogene 329 . . . . . . . . . . . RNA5SP330 . . . RNA, 5S ribosomal pseudogene 330 . . . . . . . . . . . RNA5SP331 . . . RNA, 5S ribosomal pseudogene 331 . . . . . . . . . . . RNA5SP332 . . . RNA, 5S ribosomal pseudogene 332 . . . . . . . . . . . RNA5SP333 . . . RNA, 5S ribosomal pseudogene 333 . . . . . . . . . . . RNA5SP334 . . . RNA, 5S ribosomal pseudogene 334 . . . . . . . . . . . RNA5SP335 . . . RNA, 5S ribosomal pseudogene 335 . . . . . . . . . . . RNA5SP336 . . . RNA, 5S ribosomal pseudogene 336 . . . . . . . . . . . RNA5SP337 . . . RNA, 5S ribosomal pseudogene 337 . . . . . . . . . . . RNA5SP338 . . . RNA, 5S ribosomal pseudogene 338 . . . . . . . . . . . RNA5SP339 . . . RNA, 5S ribosomal pseudogene 339 . . . . . . . . . . . RNA5SP340 . . . RNA, 5S ribosomal pseudogene 340 . . . . . . . . . . . RNA5SP341 . . . RNA, 5S ribosomal pseudogene 341 . . . . . . . . . . . RNA5SP342 . . . RNA, 5S ribosomal pseudogene 342 . . . . . . . . . . . RNA5SP343 . . . RNA, 5S ribosomal pseudogene 343 . . . . . . . . . . . RNA5SP344 . . . RNA, 5S ribosomal pseudogene 344 . . . . . . . . . . . RNA5SP345 . . . RNA, 5S ribosomal pseudogene 345 . . . . . . . . . . . RNA5SP346 . . . RNA, 5S ribosomal pseudogene 346 . . . . . . . . . . . RNA5SP347 . . . RNA, 5S ribosomal pseudogene 347 . . . . . . . . . . . RNA5SP348 . . . RNA, 5S ribosomal pseudogene 348 . . . . . . . . . . . RNA5SP349 . . . RNA, 5S ribosomal pseudogene 349 . . . . . . . . . . . RNA5SP350 . . . RNA, 5S ribosomal pseudogene 350 . . . . . . . . . . . RNA5SP351 . . . RNA, 5S ribosomal pseudogene 351 . . . . . . . . . . . RNA5SP352 . . . RNA, 5S ribosomal pseudogene 352 . . . . . . . . . . . RNA5SP353 . . . RNA, 5S ribosomal pseudogene 353 . . . . . . . . . . . RNA5SP354 . . . RNA, 5S ribosomal pseudogene 354 . . . . . . . . . . . RNA5SP355 . . . RNA, 5S ribosomal pseudogene 355 . . . . . . . . . . . RNA5SP356 . . . RNA, 5S ribosomal pseudogene 356 . . . . . . . . . . . RNA5SP357 . . . RNA, 5S ribosomal pseudogene 357 . . . . . . . . . . . RNA5SP358 . . . RNA, 5S ribosomal pseudogene 358 . . . . . . . . . . . RNA5SP359 . . . RNA, 5S ribosomal pseudogene 359 . . . . . . . . . . . RNA5SP360 . . . RNA, 5S ribosomal pseudogene 360 . . . . . . . . . . . RNA5SP361 . . . RNA, 5S ribosomal pseudogene 361 . . . . . . . . . . . RNA5SP362 . . . RNA, 5S ribosomal pseudogene 362 . . . . . . . . . . . RNA5SP363 . . . RNA, 5S ribosomal pseudogene 363 . . . . . . . . . . . RNA5SP364 . . . RNA, 5S ribosomal pseudogene 364 . . . . . . . . . . . RNA5SP365 . . . RNA, 5S ribosomal pseudogene 365 . . . . . . . . . . . RNA5SP366 . . . RNA, 5S ribosomal pseudogene 366 . . . . . . . . . . . RNA5SP367 . . . RNA, 5S ribosomal pseudogene 367 . . . . . . . . . . . RNA5SP368 . . . RNA, 5S ribosomal pseudogene 368 . . . . . . . . . . . RNA5SP369 . . . RNA, 5S ribosomal pseudogene 369 . . . . . . . . . . . RNA5SP370 . . . RNA, 5S ribosomal pseudogene 370 . . . . . . . . . . . RNA5SP371 . . . RNA, 5S ribosomal pseudogene 371 . . . . . . . . . . . RNA5SP372 . . . RNA, 5S ribosomal pseudogene 372 . . . . . . . . . . . RNA5SP373 . . . RNA, 5S ribosomal pseudogene 373 . . . . . . . . . . . RNA5SP374 . . . RNA, 5S ribosomal pseudogene 374 . . . . . . . . . . . RNA5SP375 . . . RNA, 5S ribosomal pseudogene 375 . . . . . . . . . . . RNA5SP376 . . . RNA, 5S ribosomal pseudogene 376 . . . . . . . . . . . RNA5SP377 . . . RNA, 5S ribosomal pseudogene 377 . . . . . . . . . . . RNA5SP378 . . . RNA, 5S ribosomal pseudogene 378 . . . . . . . . . . . RNA5SP379 . . . RNA, 5S ribosomal pseudogene 379 . . . . . . . . . . . RNA5SP380 . . . RNA, 5S ribosomal pseudogene 380 . . . . . . . . . . . RNA5SP382 . . . RNA, 5S ribosomal pseudogene 382 . . . . . . . . . . . RNA5SP383 . . . RNA, 5S ribosomal pseudogene 383 . . . . . . . . . . . RNA5SP384 . . . RNA, 5S ribosomal pseudogene 384 . . . . . . . . . . . RNA5SP385 . . . RNA, 5S ribosomal pseudogene 385 . . . . . . . . . . . RNA5SP386 . . . RNA, 5S ribosomal pseudogene 386 . . . . . . . . . . . RNA5SP387 . . . RNA, 5S ribosomal pseudogene 387 . . . . . . . . . . . RNA5SP388 . . . RNA, 5S ribosomal pseudogene 388 . . . . . . . . . . . RNA5SP389 . . . RNA, 5S ribosomal pseudogene 389 . . . . . . . . . . . RNA5SP390 . . . RNA, 5S ribosomal pseudogene 390 . . . . . . . . . . . RNA5SP391 . . . RNA, 5S ribosomal pseudogene 391 . . . . . . . . . . . RNA5SP392 . . . RNA, 5S ribosomal pseudogene 392 . . . . . . . . . . . RNA5SP393 . . . RNA, 5S ribosomal pseudogene 393 . . . . . . . . . . . RNA5SP394 . . . RNA, 5S ribosomal pseudogene 394 . . . . . . . . . . . RNA5SP395 . . . RNA, 5S ribosomal pseudogene 395 . . . . . . . . . . . RNA5SP396 . . . RNA, 5S ribosomal pseudogene 396 . . . . . . . . . . . RNA5SP397 . . . RNA, 5S ribosomal pseudogene 397 . . . . . . . . . . . RNA5SP398 . . . RNA, 5S ribosomal pseudogene 398 . . . . . . . . . . . RNA5SP399 . . . RNA, 5S ribosomal pseudogene 399 . . . . . . . . . . . RNA5SP400 . . . RNA, 5S ribosomal pseudogene 400 . . . . . . . . . . . RNA5SP401 . . . RNA, 5S ribosomal pseudogene 401 . . . . . . . . . . . RNA5SP402 . . . RNA, 5S ribosomal pseudogene 402 . . . . . . . . . . . RNA5SP403 . . . RNA, 5S ribosomal pseudogene 403 . . . . . . . . . . . RNA5SP404 . . . RNA, 5S ribosomal pseudogene 404 . . . . . . . . . . . RNA5SP405 . . . RNA, 5S ribosomal pseudogene 405 . . . . . . . . . . . RNA5SP406 . . . RNA, 5S ribosomal pseudogene 406 . . . . . . . . . . . RNA5SP407 . . . RNA, 5S ribosomal pseudogene 407 . . . . . . . . . . . RNA5SP408 . . . RNA, 5S ribosomal pseudogene 408 . . . . . . . . . . . RNA5SP409 . . . RNA, 5S ribosomal pseudogene 409 . . . . . . . . . . . RNA5SP410 . . . RNA, 5S ribosomal pseudogene 410 . . . . . . . . . . . RNA5SP411 . . . RNA, 5S ribosomal pseudogene 411 . . . . . . . . . . . RNA5SP412 . . . RNA, 5S ribosomal pseudogene 412 . . . . . . . . . . . RNA5SP413 . . . RNA, 5S ribosomal pseudogene 413 . . . . . . . . . . . RNA5SP414 . . . RNA, 5S ribosomal pseudogene 414 . . . . . . . . . . . RNA5SP415 . . . RNA, 5S ribosomal pseudogene 415 . . . . . . . . . . . RNA5SP416 . . . RNA, 5S ribosomal pseudogene 416 . . . . . . . . . . . RNA5SP417 . . . RNA, 5S ribosomal pseudogene 417 . . . . . . . . . . . RNA5SP418 . . . RNA, 5S ribosomal pseudogene 418 . . . . . . . . . . . RNA5SP419 . . . RNA, 5S ribosomal pseudogene 419 . . . . . . . . . . . RNA5SP420 . . . RNA, 5S ribosomal pseudogene 420 . . . . . . . . . . . RNA5SP421 . . . RNA, 5S ribosomal pseudogene 421 . . . . . . . . . . . RNA5SP422 . . . RNA, 5S ribosomal pseudogene 422 . . . . . . . . . . . RNA5SP423 . . . RNA, 5S ribosomal pseudogene 423 . . . . . . . . . . . RNA5SP424 . . . RNA, 5S ribosomal pseudogene 424 . . . . . . . . . . . RNA5SP425 . . . RNA, 5S ribosomal pseudogene 425 . . . . . . . . . . . RNA5SP426 . . . RNA, 5S ribosomal pseudogene 426 . . . . . . . . . . . RNA5SP427 . . . RNA, 5S ribosomal pseudogene 427 . . . . . . . . . . . RNA5SP428 . . . RNA, 5S ribosomal pseudogene 428 . . . . . . . . . . . RNA5SP429 . . . RNA, 5S ribosomal pseudogene 429 . . . . . . . . . . . RNA5SP430 . . . RNA, 5S ribosomal pseudogene 430 . . . . . . . . . . . RNA5SP431 . . . RNA, 5S ribosomal pseudogene 431 . . . . . . . . . . . RNA5SP432 . . . RNA, 5S ribosomal pseudogene 432 . . . . . . . . . . . RNA5SP433 . . . RNA, 5S ribosomal pseudogene 433 . . . . . . . . . . . RNA5SP434 . . . RNA, 5S ribosomal pseudogene 434 . . . . . . . . . . . RNA5SP435 . . . RNA, 5S ribosomal pseudogene 435 . . . . . . . . . . . RNA5SP436 . . . RNA, 5S ribosomal pseudogene 436 . . . . . . . . . . . RNA5SP437 . . . RNA, 5S ribosomal pseudogene 437 . . . . . . . . . . . RNA5SP438 . . . RNA, 5S ribosomal pseudogene 438 . . . . . . . . . . . RNA5SP439 . . . RNA, 5S ribosomal pseudogene 439 . . . . . . . . . . . RNA5SP440 . . . RNA, 5S ribosomal pseudogene 440 . . . . . . . . . . . RNA5SP441 . . . RNA, 5S ribosomal pseudogene 441 . . . . . . . . . . . RNA5SP442 . . . RNA, 5S ribosomal pseudogene 442 . . . . . . . . . . . RNA5SP443 . . . RNA, 5S ribosomal pseudogene 443 . . . . . . . . . . . RNA5SP444 . . . RNA, 5S ribosomal pseudogene 444 . . . . . . . . . . . RNA5SP445 . . . RNA, 5S ribosomal pseudogene 445 . . . . . . . . . . . RNA5SP446 . . . RNA, 5S ribosomal pseudogene 446 . . . . . . . . . . . RNA5SP447 . . . RNA, 5S ribosomal pseudogene 447 . . . . . . . . . . . RNA5SP448 . . . RNA, 5S ribosomal pseudogene 448 . . . . . . . . . . . RNA5SP449 . . . RNA, 5S ribosomal pseudogene 449 . . . . . . . . . . . RNA5SP450 . . . RNA, 5S ribosomal pseudogene 450 . . . . . . . . . . . RNA5SP451 . . . RNA, 5S ribosomal pseudogene 451 . . . . . . . . . . . RNA5SP452 . . . RNA, 5S ribosomal pseudogene 452 . . . . . . . . . . . RNA5SP453 . . . RNA, 5S ribosomal pseudogene 453 . . . . . . . . . . . RNA5SP454 . . . RNA, 5S ribosomal pseudogene 454 . . . . . . . . . . . RNA5SP455 . . . RNA, 5S ribosomal pseudogene 455 . . . . . . . . . . . RNA5SP456 . . . RNA, 5S ribosomal pseudogene 456 . . . . . . . . . . . RNA5SP457 . . . RNA, 5S ribosomal pseudogene 457 . . . . . . . . . . . RNA5SP458 . . . RNA, 5S ribosomal pseudogene 458 . . . . . . . . . . . RNA5SP459 . . . RNA, 5S ribosomal pseudogene 459 . . . . . . . . . . . RNA5SP460 . . . RNA, 5S ribosomal pseudogene 460 . . . . . . . . . . . RNA5SP461 . . . RNA, 5S ribosomal pseudogene 461 . . . . . . . . . . . RNA5SP462 . . . RNA, 5S ribosomal pseudogene 462 . . . . . . . . . . . RNA5SP463 . . . RNA, 5S ribosomal pseudogene 463 . . . . . . . . . . . RNA5SP464 . . . RNA, 5S ribosomal pseudogene 464 . . . . . . . . . . . RNA5SP465 . . . RNA, 5S ribosomal pseudogene 465 . . . . . . . . . . . RNA5SP466 . . . RNA, 5S ribosomal pseudogene 466 . . . . . . . . . . . RNA5SP467 . . . RNA, 5S ribosomal pseudogene 467 . . . . . . . . . . . RNA5SP468 . . . RNA, 5S ribosomal pseudogene 468 . . . . . . . . . . . RNA5SP469 . . . RNA, 5S ribosomal pseudogene 469 . . . . . . . . . . . RNA5SP470 . . . RNA, 5S ribosomal pseudogene 470 . . . . . . . . . . . RNA5SP471 . . . RNA, 5S ribosomal pseudogene 471 . . . . . . . . . . . RNA5SP472 . . . RNA, 5S ribosomal pseudogene 472 . . . . . . . . . . . RNA5SP473 . . . RNA, 5S ribosomal pseudogene 473 . . . . . . . . . . . RNA5SP474 . . . RNA, 5S ribosomal pseudogene 474 . . . . . . . . . . . RNA5SP475 . . . RNA, 5S ribosomal pseudogene 475 . . . . . . . . . . . RNA5SP476 . . . RNA, 5S ribosomal pseudogene 476 . . . . . . . . . . . RNA5SP477 . . . RNA, 5S ribosomal pseudogene 477 . . . . . . . . . . . RNA5SP478 . . . RNA, 5S ribosomal pseudogene 478 . . . . . . . . . . . RNA5SP479 . . . RNA, 5S ribosomal pseudogene 479 . . . . . . . . . . . RNA5SP480 . . . RNA, 5S ribosomal pseudogene 480 . . . . . . . . . . . RNA5SP481 . . . RNA, 5S ribosomal pseudogene 481 . . . . . . . . . . . RNA5SP482 . . . RNA, 5S ribosomal pseudogene 482 . . . . . . . . . . . RNA5SP483 . . . RNA, 5S ribosomal pseudogene 483 . . . . . . . . . . . RNA5SP484 . . . RNA, 5S ribosomal pseudogene 484 . . . . . . . . . . . RNA5SP485 . . . RNA, 5S ribosomal pseudogene 485 . . . . . . . . . . . RNA5SP486 . . . RNA, 5S ribosomal pseudogene 486 . . . . . . . . . . . RNA5SP487 . . . RNA, 5S ribosomal pseudogene 487 . . . . . . . . . . . RNA5SP488 . . . RNA, 5S ribosomal pseudogene 488 . . . . . . . . . . . RNA5SP489 . . . RNA, 5S ribosomal pseudogene 489 . . . . . . . . . . . RNA5SP490 . . . RNA, 5S ribosomal pseudogene 490 . . . . . . . . . . . RNA5SP491 . . . RNA, 5S ribosomal pseudogene 491 . . . . . . . . . . . RNA5SP492 . . . RNA, 5S ribosomal pseudogene 492 . . . . . . . . . . . RNA5SP493 . . . RNA, 5S ribosomal pseudogene 493 . . . . . . . . . . . RNA5SP494 . . . RNA, 5S ribosomal pseudogene 494 . . . . . . . . . . . RNA5SP495 . . . RNA, 5S ribosomal pseudogene 495 . . . . . . . . . . . RNA5SP496 . . . RNA, 5S ribosomal pseudogene 496 . . . . . . . . . . . RNA5SP497 . . . RNA, 5S ribosomal pseudogene 497 . . . . . . . . . . . RNA5SP498 . . . RNA, 5S ribosomal pseudogene 498 . . . . . . . . . . . RNA5SP499 . . . RNA, 5S ribosomal pseudogene 499 . . . . . . . . . . . RNA5SP500 . . . RNA, 5S ribosomal pseudogene 500 . . . . . . . . . . . RNA5SP501 . . . RNA, 5S ribosomal pseudogene 501 . . . . . . . . . . . RNA5SP502 . . . RNA, 5S ribosomal pseudogene 502 . . . . . . . . . . . RNA5SP503 . . . RNA, 5S ribosomal pseudogene 503 . . . . . . . . . . . RNA5SP504 . . . RNA, 5S ribosomal pseudogene 504 . . . . . . . . . . . RNA5SP505 . . . RNA, 5S ribosomal pseudogene 505 . . . . . . . . . . . RNA5SP506 . . . RNA, 5S ribosomal pseudogene 506 . . . . . . . . . . . RNA5SP507 . . . RNA, 5S ribosomal pseudogene 507 . . . . . . . . . . . RNA5SP508 . . . RNA, 5S ribosomal pseudogene 508 . . . . . . . . . . . RNA5SP509 . . . RNA, 5S ribosomal pseudogene 509 . . . . . . . . . . . RNA5SP510 . . . RNA, 5S ribosomal pseudogene 510 . . . . . . . . . . . RNA5SP511 . . . RNA, 5S ribosomal pseudogene 511 . . . . . . . . . . . RNA5SP512 . . . RNA, 5S ribosomal pseudogene 512 . . . . . . . . . . . RNA5SP513 . . . RNA, 5S ribosomal pseudogene 513 . . . . . . . . . . . RNA5SP514 . . . RNA, 5S ribosomal pseudogene 514 . . . . . . . . . . . RNA5SP515 . . . RNA, 5S ribosomal pseudogene 515 . . . . . . . . . . . RNA5SP516 . . . RNA, 5S ribosomal pseudogene 516 . . . . . . . . . . . RNA5SP517 . . . RNA, 5S ribosomal pseudogene 517 . . . . . . . . . . . RNA5SP518 . . . RNA, 5S ribosomal pseudogene 518 . . . . . . . . . . . RNA5SP519 . . . RNA, 5S ribosomal pseudogene 519 . . . . . . . . . . . RNA5SP520 . . . RNA, 5S ribosomal pseudogene 520 . . . . . . . . . . . RNA5SP521 . . . RNA, 5S ribosomal pseudogene 521 . . . . . . . . . . . RNA5SP522 . . . RNA, 5S ribosomal pseudogene 522 . . . . . . . . . . . RNA5SP523 . . . RNA, 5S ribosomal pseudogene 523 . . . . . . . . . . . RNA18S1 . . . RNA, 18S ribosomal 1 . . . . . . . . . . . RNA18S2 . . . RNA, 18S ribosomal 2 . . . . . . . . . . . RNA18S3 . . . RNA, 18S ribosomal 3 . . . . . . . . . . . RNA18S4 . . . RNA, 18S ribosomal 4 . . . . . . . . . . . RNA18S5 . . . RNA, 18S ribosomal 5 . . . . . . . . . . . RNA18SP2 . . . RNA, 18S ribosomal pseudogene 2 . . . . . . . . . . . RNA28S1 . . . RNA, 28S ribosomal 1 . . . . . . . . . . . RNA28S2 . . . RNA, 28S ribosomal 2 . . . . . . . . . . . RNA28S3 . . . RNA, 28S ribosomal 3 . . . . . . . . . . . RNA28S4 . . . RNA, 28S ribosomal 4 . . . . . . . . . . . RNA28S5 . . . RNA, 28S ribosomal 5 . . . . . . . . . . . RNA45S1 . . . RNA, 45S pre-ribosomal 1 . . . . . . . . . . . RNA45S2 . . . RNA, 45S pre-ribosomal 2 . . . . . . . . . . . RNA45S3 . . . RNA, 45S pre-ribosomal 3 . . . . . . . . . . . RNA45S4 . . . RNA, 45S pre-ribosomal 4 . . . . . . . . . . . RNA45S5 . . . RNA, 45S pre-ribosomal 5 . . . . . . . . . . . RNASE1 0.161588976975498 0.638851606171356 0.199559416853146 ribonuclease A family member 1, pancreatic FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA. {ECO:0000269|PubMed:17350650}.; . TISSUE SPECIFICITY: Pancreas and other tissues and body fluids (indicating it may have other physiological functions besides its role in digestion).; myocardium;medulla oblongata;ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pineal body;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;hippocampus;liver;alveolus;spleen;kidney;mammary gland;stomach;aorta; medulla oblongata;superior cervical ganglion;pancreas;testis - seminiferous tubule;placenta;testis;caudate nucleus;parietal lobe; 0.09615 0.22238 0.703746784 85.42108988 47.26898 1.33294 RNASE2 0.0380227485132804 0.836273074798468 0.125704176688251 ribonuclease A family member 2 FUNCTION: This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Selectively chemotactic for dendritic cells. Possesses a wide variety of biological activities. {ECO:0000269|PubMed:12578357, ECO:0000269|PubMed:3458170}.; . TISSUE SPECIFICITY: Liver, lung, spleen, leukocytes and body fluids.; liver;spleen;blood;head and neck;kidney;bone marrow; bone marrow; 0.21236 . 0.148941568 64.31941496 34.12214 1.04622 RNASE3 0.000178635535037144 0.271091931293323 0.728729433171639 ribonuclease A family member 3 FUNCTION: Cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. Possesses a wide variety of biological activities. Exhibits antibacterial activity, including cytoplasmic membrane depolarization of preferentially Gram-negative, but also Gram-positive strains. Promotes E.coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content. {ECO:0000269|PubMed:19450231, ECO:0000269|PubMed:2501794}.; . . optic nerve;larynx;placenta;macula lutea;blood;fovea centralis;choroid;lens;brain;retina;bone marrow; superior cervical ganglion;trigeminal ganglion;bone marrow; 0.15750 0.17049 0.393270925 76.04977589 12.00594 0.43597 RNASE4 0.00701713412897145 0.528281003035226 0.464701862835803 ribonuclease A family member 4 FUNCTION: This RNase has marked specificity towards the 3' side of uridine nucleotides.; . . ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;testis;brain;artery;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; dorsal root ganglion;fetal liver;superior cervical ganglion;trachea;liver;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05472 . 0.926041233 89.65557915 850.93401 5.70009 RNASE6 5.43170259087741e-08 0.0185214663363765 0.981478479346597 ribonuclease A family member k6 FUNCTION: May have a role in host defense.; . TISSUE SPECIFICITY: Strong expression in lung, followed by heart, placenta, kidney, pancreas, liver, brain and skeletal muscle. Also expressed in monocytes and neutrophils.; unclassifiable (Anatomical System);cartilage;ovary;heart;islets of Langerhans;colon;blood;choroid;skin;breast;uterus;pancreas;whole body;lung;nasopharynx;bone;placenta;liver;testis;spleen;kidney;germinal center;brain;artery;aorta;tonsil; white blood cells;whole blood; 0.48448 0.08665 0.347360312 73.97381458 28.07143 0.90064 RNASE7 0.28044916605996 0.631606441992512 0.0879443919475286 ribonuclease A family member 7 FUNCTION: Exhibits a potent RNase activity. Has broad-spectrum antimicrobial activity against many pathogenic microorganisms and remarkably potent activity (lethal dose of 90% < 30 nM) against a vancomycin resistant Enterococcus faecium. {ECO:0000269|PubMed:12244054, ECO:0000269|PubMed:12527768, ECO:0000269|PubMed:17150966}.; . TISSUE SPECIFICITY: Expressed in various epithelial tissues including skin, respiratory tract, genito-urinary tract and, at a low level, in the gut. Expressed in liver, kidney, skeletal muscle and heart. {ECO:0000269|PubMed:12244054, ECO:0000269|PubMed:12527768}.; unclassifiable (Anatomical System);lung;heart;skin; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.11703 0.09364 1.148343558 92.42745931 59.5198 1.56542 RNASE8 0.0051691020998071 0.46543261600753 0.529398281892662 ribonuclease A family member 8 FUNCTION: Has a low ribonuclease activity.; . TISSUE SPECIFICITY: Expressed prominently in the placenta and is not detected in any other tissues examined.; . . 0.10599 . 0.503505267 79.88912479 22.36247 0.75053 RNASE9 1.66649163366409e-05 0.138242240332203 0.86174109475146 ribonuclease A family member 9 (inactive) FUNCTION: Does not exhibit any ribonuclease activity. {ECO:0000269|PubMed:18992174, ECO:0000269|PubMed:19137000}.; . TISSUE SPECIFICITY: At the mRNA level, widely expressed (PubMed:18992174). At protein level, restricted to epididymis (PubMed:19137000). Expressed in spermatozoa (sperm head and neck), with higher levels on ejaculated and epididymal sperm than on testicular sperm (at protein level). Expressed in the epithelial cells of the epididymal tubule (at protein level). Not detected in muscle. {ECO:0000269|PubMed:18992174, ECO:0000269|PubMed:19137000}.; . . 0.05030 0.05793 1.727105015 96.51450814 249.33593 3.40376 RNASE10 0.013059518657014 0.659706831459872 0.327233649883114 ribonuclease A family member 10 (inactive) FUNCTION: Secreted proximal epididymal protein required for post- testicular sperm maturation and male fertility. May be involved in sperm adhesion to the egg zona pellucida. Does not have ribonuclease activity (By similarity). {ECO:0000250}.; . . uterus;parathyroid; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09246 0.07203 0.549415813 81.38122199 45.32143 1.29298 RNASE11 0.000992587146927763 0.365104531369424 0.633902881483649 ribonuclease A family member 11 (inactive) . . . unclassifiable (Anatomical System);medulla oblongata;lung;placenta;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; 0.02844 . 0.483275131 79.25218212 190.02401 2.99169 RNASE12 0.00683829902185725 0.522865275723072 0.470296425255071 ribonuclease A family member 12 (inactive) FUNCTION: Does not exhibit any ribonuclease activity. {ECO:0000305}.; . . . . 0.15145 0.11743 -0.251530012 35.42108988 8.76227 0.32256 RNASE13 0.00115691527116493 0.392407931853419 0.606435152875417 ribonuclease A family member 13 (inactive) FUNCTION: Does not exhibit any ribonuclease activity. {ECO:0000305}.; . . . . 0.03937 . 0.281220278 71.07808445 80.71587 1.89784 RNASEH1 0.0164156541621668 0.959553349185446 0.024030996652387 ribonuclease H1 FUNCTION: Endonuclease that specifically degrades the RNA of RNA- DNA hybrids (PubMed:10497183). Plays a role in RNA polymerase II (RNAp II) transcription termination by degrading R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site and behind the elongating RNAp II (PubMed:21700224). {ECO:0000269|PubMed:10497183, ECO:0000269|PubMed:21700224}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;alveolus;liver;head and neck;cervix;kidney;mammary gland;stomach; . 0.10739 0.11742 -0.736552314 13.93606983 13.14635 0.47890 RNASEH1-AS1 . . . RNASEH1 antisense RNA 1 . . . . . . . . . . . RNASEH1P1 . . . ribonuclease H1 pseudogene 1 FUNCTION: Endonuclease that specifically degrades the RNA of RNA- DNA hybrids (PubMed:10497183). Plays a role in RNA polymerase II (RNAp II) transcription termination by degrading R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site and behind the elongating RNAp II (PubMed:21700224). {ECO:0000269|PubMed:10497183, ECO:0000269|PubMed:21700224}.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.10739 0.11742 -0.736552314 13.93606983 . . RNASEH1P2 . . . ribonuclease H1 pseudogene 2 . . . . . . . . . . . RNASEH1P3 . . . ribonuclease H1 pseudogene 3 . . . . . . . . . . . RNASEH2A 0.0500791342521709 0.927859339492098 0.0220615262557316 ribonuclease H2 subunit A FUNCTION: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging- strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes. {ECO:0000269|PubMed:16845400, ECO:0000269|PubMed:21177858}.; DISEASE: Aicardi-Goutieres syndrome 4 (AGS4) [MIM:610333]: A form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood. {ECO:0000269|PubMed:16845400, ECO:0000269|PubMed:17846997, ECO:0000269|PubMed:20131292}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;dura mater;germinal center;brain;tonsil;unclassifiable (Anatomical System);meninges;lymph node;heart;muscle;urinary;adrenal cortex;blood;lens;pia mater;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;alveolus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.81511 0.48447 -0.049474214 50.01179523 234.74484 3.31139 RNASEH2B 1.29919624387268e-09 0.0536879346944041 0.9463120640064 ribonuclease H2 subunit B FUNCTION: Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging- strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes. {ECO:0000269|PubMed:16845400, ECO:0000269|PubMed:21177858}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16845400}.; smooth muscle;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;cochlea;cerebral cortex;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;pineal body;blood;lens;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.11956 . 0.038710339 56.92380278 253.09297 3.42276 RNASEH2B-AS1 . . . RNASEH2B antisense RNA 1 . . . . . . . . . . . RNASEH2C 0.511931591971642 0.470023276894282 0.0180451311340759 ribonuclease H2 subunit C FUNCTION: Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging- strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes. {ECO:0000269|PubMed:16845400, ECO:0000269|PubMed:21177858}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16845400}.; myocardium;lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;pancreas;lung;cornea;adrenal gland;placenta;duodenum;kidney;stomach;thymus; . 0.08239 0.11400 -0.053113545 49.38664779 166.76046 2.82129 RNASEH2CP1 . . . ribonuclease H2 subunit C pseudogene 1 . . . . . . . . . . . RNASEK 0.339227905981652 0.601385612543773 0.0593864814745744 ribonuclease K FUNCTION: Endoribonuclease which preferentially cleaves ApU and ApG phosphodiester bonds. Hydrolyzes UpU bonds at a lower rate. {ECO:0000269|PubMed:17881363}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17881363}.; . . 0.07007 . -0.031067188 51.03798066 12.8253 0.46775 RNASEK-C17orf49 . . . RNASEK-C17orf49 readthrough . . . . . 0.41661 . . . . . RNASEL 8.98220456476748e-09 0.287779651188804 0.712220339828991 ribonuclease L FUNCTION: Endoribonuclease that functions in the interferon (IFN) antiviral response. In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress- response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. Therefore, activation of RNASEL could lead to elimination of virus infected cells under some circumstances. In the crosstalk between autophagy and apoptosis proposed to induce autophagy as an early stress response to small double-stranded RNA and at later stages of prolonged stress to activate caspase-dependent proteolytic cleavage of BECN1 to terminate autophagy and promote apoptosis (PubMed:26263979). Might play a central role in the regulation of mRNA turnover (PubMed:11585831). {ECO:0000269|PubMed:11585831, ECO:0000269|PubMed:26263979}.; DISEASE: Prostate cancer, hereditary, 1 (HPC1) [MIM:601518]: A condition associated with familial predisposition to cancer of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. {ECO:0000305|PubMed:11799394, ECO:0000305|PubMed:11941539, ECO:0000305|PubMed:12415269, ECO:0000305|PubMed:17344846}.; TISSUE SPECIFICITY: Highly expressed in spleen and thymus followed by prostate, testis, uterus, small intestine, colon and peripheral blood leukocytes.; . . 0.06110 0.12135 -0.172654315 40.63458363 2257.84547 8.78025 RNASET2 0.00948040570721487 0.940217750490896 0.0503018438018894 ribonuclease T2 FUNCTION: Has ribonuclease activity, with higher activity at acidic pH. Probably is involved in lysosomal degradation of ribosomal RNA (By similarity). Probably plays a role in cellular RNA catabolism. {ECO:0000250, ECO:0000269|PubMed:16620762, ECO:0000269|PubMed:19525954, ECO:0000269|PubMed:22735700}.; . TISSUE SPECIFICITY: Ubiquitous. Higher expression levels observed in the temporal lobe and fetal brain. {ECO:0000269|PubMed:19525954}.; medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;blood;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle; 0.07919 0.10217 0.549415813 81.38122199 203.22207 3.07698 RND1 0.965631677734805 0.0343072748211002 6.10474440947777e-05 Rho family GTPase 1 FUNCTION: Lacks intrinsic GTPase activity. Has a low affinity for GDP, and constitutively binds GTP. Controls rearrangements of the actin cytoskeleton. Induces the Rac-dependent neuritic process formation in part by disruption of the cortical actin filaments. Causes the formation of many neuritic processes from the cell body with disruption of the cortical actin filaments. {ECO:0000269|PubMed:11095956}.; . TISSUE SPECIFICITY: Mostly expressed in brain and liver.; unclassifiable (Anatomical System);lymph node;heart;hypothalamus;colon;fovea centralis;choroid;lens;retina;bone marrow;optic nerve;lung;frontal lobe;bone;macula lutea;visual apparatus;hippocampus;testis;kidney;mammary gland;brain;stomach; subthalamic nucleus;globus pallidus;pons; 0.22708 0.16524 0.080983847 59.76055674 26.32366 0.85363 RND2 0.000138854210054274 0.645442074392143 0.354419071397803 Rho family GTPase 2 FUNCTION: May be specifically involved in neuronal and hepatic functions. Is a C3 toxin-insensitive member of the Rho subfamily (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in testis.; unclassifiable (Anatomical System);ovary;hypothalamus;blood;parathyroid;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;epididymis;placenta;macula lutea;testis;brain; dorsal root ganglion;amygdala;thalamus;testis - interstitial;superior cervical ganglion;hypothalamus;spinal cord;temporal lobe;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;cerebellum; 0.25979 0.14540 -0.295622497 32.61972163 21.864 0.73577 RND3 0.940812851099585 0.0589502482973435 0.00023690060307142 Rho family GTPase 3 FUNCTION: Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;nasopharynx;trabecular meshwork;placenta;visual apparatus;amnion;alveolus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; uterus corpus;ciliary ganglion; 0.45299 0.16306 -0.229483771 36.86010852 13.34323 0.48510 RNF2 0.944004162174101 0.0559538271086445 4.20107172550238e-05 ring finger protein 2 FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes. {ECO:0000269|PubMed:11513855, ECO:0000269|PubMed:15386022, ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16714294, ECO:0000269|PubMed:20696397}.; . . . . 0.63393 0.44984 -0.09720619 46.20193442 13.41293 0.48808 RNF2P1 . . . ring finger protein 2 pseudogene 1 . . . . . . . . . . . RNF4 0.628950995184494 0.36385220350281 0.00719680131269572 ring finger protein 4 FUNCTION: E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor- mediated transcriptional activation. {ECO:0000269|PubMed:12885770, ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:19307308, ECO:0000269|PubMed:20026589, ECO:0000269|PubMed:20212317, ECO:0000269|PubMed:20943951}.; . TISSUE SPECIFICITY: Widely expressed at low levels in many tissues; highly expressed in testis. {ECO:0000269|PubMed:9479498}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta;cerebellum; testis - seminiferous tubule;testis;cingulate cortex;cerebellum; 0.15544 0.12342 0.547599505 81.2160887 26.29011 0.85255 RNF5 0.00299042376639745 0.812334033525094 0.184675542708509 ring finger protein 5, E3 ubiquitin protein ligase FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity. May function together with E2 ubiquitin-conjugating enzymes UBE2D1/UBCH5A and UBE2D2/UBC4. Mediates ubiquitination of PXN/paxillin and Salmonella type III secreted protein sopA. May be involved in regulation of cell motility and localization of PXN/paxillin. Mediates the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD; the ubiquitination appears to involve E2 ubiquitin-conjugating enzyme UBE2N. Mediates the 'Lys-48'-linked polyubiquitination of TMEM173 at 'Lys-150' leading to its proteasomal degradation; the ubiquitination occurrs in mitochondria after viral transfection and regulates antiviral responses. {ECO:0000269|PubMed:11329381, ECO:0000269|PubMed:12861019, ECO:0000269|PubMed:16176924, ECO:0000269|PubMed:19269966, ECO:0000269|PubMed:19285439}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9533025}.; . . 0.17404 . -0.053113545 49.38664779 34.56414 1.05556 RNF5P1 . . . ring finger protein 5, E3 ubiquitin protein ligase pseudogene 1 . . . . . . . . . . . RNF6 0.170343293261201 0.829632709974642 2.39967641565198e-05 ring finger protein (C3H2C3 type) 6 FUNCTION: E3 ubiquitin-protein ligase mediating 'Lys-48'-linked polyubiquitination of LIMK1 and its subsequent targeting to the proteasome for degradation. Negatively regulates axonal outgrowth through regulation of the LIMK1 turnover. Mediates 'Lys-6' and 'Lys-27'-linked polyubiquitination of AR/androgen receptor thereby modulating its transcriptional activity. May also bind DNA and function as a transcriptional regulator. {ECO:0000269|PubMed:19345326}.; DISEASE: Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the esophagus. The most common types are esophageal squamous cell carcinoma and adenocarcinoma. Cancer of the esophagus remains a devastating disease because it is usually not detected until it has progressed to an advanced incurable stage. {ECO:0000269|PubMed:12154016}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Weakly expressed in peripheral blood, spleen, prostate, testis and ovary. According to PubMed:18368307, it is preferentially expressed in testis and ovary and hardly detected in other tissues. {ECO:0000269|PubMed:18368307, ECO:0000269|PubMed:19345326}.; ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;urinary;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;artery;unclassifiable (Anatomical System);islets of Langerhans;lung;mesenchyma;adrenal gland;placenta;hippocampus;kidney;aorta;stomach;cerebellum; amygdala;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis; 0.11802 0.09304 0.158037129 64.85020052 81.50721 1.91195 RNF6P1 . . . ring finger protein (C3H2C3 type) 6 pseudogene 1 . . . . . . . . . . . RNF7 0.0145273267605025 0.681504863257215 0.303967809982283 ring finger protein 7 FUNCTION: Probable component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme to the complex and brings it into close proximity to the substrate. Promotes the neddylation of CUL5 via its interaction with UBE2F. May play a role in protecting cells from apoptosis induced by redox agents. {ECO:0000269|PubMed:10851089}.; . TISSUE SPECIFICITY: Expressed in heart, liver, skeletal muscle and pancreas. At very low levels expressed in brain, placenta and lung. {ECO:0000269|PubMed:10512750}.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;skeletal muscle; 0.14955 0.12378 0.035072054 56.2514744 . . RNF7P1 . . . ring finger protein 7 pseudogene 1 . . . . . . . . . . . RNF8 0.995892884804807 0.00410704804727656 6.71479168032459e-08 ring finger protein 8 FUNCTION: E3 ubiquitin-protein ligase that plays a key role in DNA damage signaling via 2 distinct roles: by mediating the 'Lys-63'- linked ubiquitination of histones H2A and H2AX and promoting the recruitment of DNA repair proteins at double-strand breaks (DSBs) sites, and by catalyzing 'Lys-48'-linked ubiquitination to remove target proteins from DNA damage sites. Following DNA DSBs, it is recruited to the sites of damage by ATM-phosphorylated MDC1 and catalyzes the 'Lys-63'-linked ubiquitination of histones H2A and H2AX, thereby promoting the formation of TP53BP1 and BRCA1 ionizing radiation-induced foci (IRIF). Also controls the recruitment of UIMC1-BRCC3 (RAP80-BRCC36) and PAXIP1/PTIP to DNA damage sites. Also recruited at DNA interstrand cross-links (ICLs) sites and catalyzes 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Promotes the formation of 'Lys-63'-linked polyubiquitin chains via interactions with the specific ubiquitin-conjugating UBE2N/UBC13 and ubiquitinates non-histone substrates such as PCNA. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation. Also catalyzes the formation of 'Lys-48'-linked polyubiquitin chains via interaction with the ubiquitin- conjugating UBE2L6/UBCH8, leading to degradation of substrate proteins such as CHEK2, JMJD2A/KDM4A and KU80/XRCC5: it is still unclear how the preference toward 'Lys-48'- versus 'Lys-63'-linked ubiquitination is regulated but it could be due to RNF8 ability to interact with specific E2 specific ligases. For instance, interaction with phosphorylated HERC2 promotes the association between RNF8 and UBE2N/UBC13 and favors the specific formation of 'Lys-63'-linked ubiquitin chains. Promotes non-homologous end joining (NHEJ) by promoting the 'Lys-48'-linked ubiquitination and degradation the of KU80/XRCC5. Following DNA damage, mediates the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF168, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. In addition to its function in damage signaling, also plays a role in higher-order chromatin structure by mediating extensive chromatin decondensation. Involved in the activation of ATM by promoting histone H2B ubiquitination, which indirectly triggers histone H4 'Lys-16' acetylation (H4K16ac), establishing a chromatin environment that promotes efficient activation of ATM kinase. Required in the testis, where it plays a role in the replacement of histones during spermatogenesis. At uncapped telomeres, promotes the joining of deprotected chromosome ends by inducing H2A ubiquitination and TP53BP1 recruitment, suggesting that it may enhance cancer development by aggravating telomere-induced genome instability in case of telomeric crisis. Promotes the assembly of RAD51 at DNA DSBs in the absence of BRCA1 and TP53BP1 Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. May be required for proper exit from mitosis after spindle checkpoint activation and may regulate cytokinesis. May play a role in the regulation of RXRA-mediated transcriptional activity. Not involved in RXRA ubiquitination by UBE2E2. {ECO:0000269|PubMed:11322894, ECO:0000269|PubMed:14981089, ECO:0000269|PubMed:17724460, ECO:0000269|PubMed:18001824, ECO:0000269|PubMed:18001825, ECO:0000269|PubMed:18006705, ECO:0000269|PubMed:18077395, ECO:0000269|PubMed:18337245, ECO:0000269|PubMed:18948756, ECO:0000269|PubMed:19015238, ECO:0000269|PubMed:19124460, ECO:0000269|PubMed:19202061, ECO:0000269|PubMed:19203578, ECO:0000269|PubMed:19203579, ECO:0000269|PubMed:20550933, ECO:0000269|PubMed:21558560, ECO:0000269|PubMed:21857671, ECO:0000269|PubMed:21911360, ECO:0000269|PubMed:22266820, ECO:0000269|PubMed:22373579, ECO:0000269|PubMed:22531782, ECO:0000269|PubMed:22705371, ECO:0000269|PubMed:22865450, ECO:0000269|PubMed:22980979}.; . TISSUE SPECIFICITY: Ubiquitous. In fetal tissues, highest expression in brain, thymus and liver. In adult tissues, highest levels in brain and testis, lowest levels in peripheral blood cells. {ECO:0000269|PubMed:16215985, ECO:0000269|PubMed:9852682}.; smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;medulla oblongata;superior cervical ganglion;testis - interstitial;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;testis;appendix;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.10535 0.10940 -0.538132194 20.26421326 24.76726 0.81274 RNF10 0.502963048424231 0.497029758106525 7.19346924390258e-06 ring finger protein 10 FUNCTION: Transcriptional factor involved in the regulation of MAG (Myelin-associated glycoprotein) expression. Acts as a regulator of Schwann cell differentiation and myelination. {ECO:0000250|UniProtKB:Q5XI59}.; . . ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;skeletal muscle;greater omentum;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;hypothalamus;muscle;bile duct;lung;mesenchyma;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;testis;atrioventricular node;pons;kidney;trigeminal ganglion;skeletal muscle;cingulate cortex;bone marrow; 0.30910 0.11298 -0.598810865 18.13517339 106.93114 2.24365 RNF10P1 . . . ring finger protein 10 pseudogene 1 . . . . . . . . . . . RNF11 0.420327239136286 0.545283676542564 0.0343890843211501 ring finger protein 11 FUNCTION: Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, leading to its degradation by the 26S proteasome. {ECO:0000269|PubMed:14755250}.; . TISSUE SPECIFICITY: Expressed at low levels in the lung, liver, kidney, pancreas, spleen, prostate, thymus, ovary, small intestine, colon, and peripheral blood lymphocytes, and, at intermediate levels, in the testis, heart, brain and placenta. Highest expression in the skeletal muscle. In the brain, expressed at different levels in several regions: high levels in the amygdala, moderate in the hippocampus and thalamus, low in the caudate and extremely low levels in the corpus callosum (at protein level). Restricted to neurons, enriched in somatodendritic compartments and excluded from white matter (at protein level). In substantia nigra, present in cell bodies and processes of dopaminergic and nondopaminergic cells (at protein level). In Parkinson disease, sequestered in Lewy bodies and neurites. Overexpressed in breast cancer cells, but not detected in the surrounding stroma and weakly, if at all, in normal breast epithelial cells (at protein level). Also expressed in several tumor cell lines. {ECO:0000269|PubMed:14559117, ECO:0000269|PubMed:14562029, ECO:0000269|PubMed:17917589}.; smooth muscle;ovary;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;amygdala;heart;cartilage;urinary;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;uterus;whole body;atrium;cerebral cortex;larynx;bone;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;placenta;amnion;head and neck;kidney;stomach;aorta;thymus;cerebellum; whole brain;amygdala;subthalamic nucleus;occipital lobe;temporal lobe;globus pallidus;parietal lobe; 0.20344 0.17050 0.057118534 57.99716914 1.34377 0.04778 RNF11P1 . . . ring finger protein 11 pseudogene 1 . . . . . . . . . . . RNF11P2 . . . ring finger protein 11 pseudogene 2 . . . . . . . . . . . RNF13 0.00198548907909874 0.909435455987473 0.0885790549334284 ring finger protein 13 FUNCTION: E3 ubiquitin-protein ligase that may play a role in controlling cell proliferation. {ECO:0000269|PubMed:18794910}.; . TISSUE SPECIFICITY: Widely expressed (at protein level). In normal pancreas, expressed in islets, but not in ducts, nor in acini (at protein level). {ECO:0000269|PubMed:18794910}.; smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;urinary;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;alveolus;spleen;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;occipital lobe;medulla oblongata;thalamus;superior cervical ganglion;hypothalamus;spinal cord;caudate nucleus;pons;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex; 0.39712 0.08746 -0.005381972 53.50908233 181.15242 2.92542 RNF14 0.00753476991397154 0.976926162586813 0.0155390674992161 ring finger protein 14 FUNCTION: Might act as an E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates, which could be nuclear proteins. Could play a role as a coactivator for androgen- and, to a lesser extent, progesterone-dependent transcription. {ECO:0000269|PubMed:19345326}.; . TISSUE SPECIFICITY: Widely expressed.; lymphoreticular;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;atrium;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18256 0.13499 -0.181750739 40.15687662 41.93057 1.22150 RNF17 0.99999998654341 1.34565899833615e-08 5.9023261215599e-22 ring finger protein 17 FUNCTION: Seems to be involved in regulation of transcriptional activity of MYC. In vitro, inhibits DNA-binding activity of Mad- MAX heterodimers. Can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. May be involved in spermiogenesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis specific.; unclassifiable (Anatomical System);lung;placenta;testis;retina; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;appendix;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.26489 0.10549 0.168960133 65.05071951 2686.91297 9.74935 RNF19A 0.0270760961169109 0.972823551033239 0.00010035284985036 ring finger protein 19A, RBR E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as SNCAIP or CASR. Specifically ubiquitinates pathogenic SOD1 variants, which leads to their proteasomal degradation and to neuronal protection. {ECO:0000269|PubMed:11237715, ECO:0000269|PubMed:12145308, ECO:0000269|PubMed:12750386, ECO:0000269|PubMed:15456787, ECO:0000269|PubMed:16513638}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in heart. Ubiquitously expressed in the central nervous system. {ECO:0000269|PubMed:11237715}.; ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;placenta;hippocampus;amnion;head and neck;kidney;stomach;thymus;cerebellum; testis - interstitial;subthalamic nucleus;skeletal muscle; 0.31889 0.14417 -0.822919685 11.76574664 40.29628 1.18401 RNF19B 0.625353364992841 0.37432826862197 0.000318366385188837 ring finger protein 19B FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1. Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells. {ECO:0000269|PubMed:10438909, ECO:0000269|PubMed:16709802}.; . TISSUE SPECIFICITY: Expressed specifically in natural killer cells, activated macrophages and cytotoxic T-cells. Present in natural killer cells (at protein level). {ECO:0000269|PubMed:10438909, ECO:0000269|PubMed:10912506}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;hypothalamus;blood;lens;breast;pancreas;lung;placenta;macula lutea;liver;duodenum;head and neck;kidney;stomach; whole brain;amygdala;testis - interstitial;superior cervical ganglion;adrenal cortex;pons;skeletal muscle;fetal liver;lung;testis - seminiferous tubule;adrenal gland;thyroid;liver;testis;kidney;whole blood;trigeminal ganglion;parietal lobe;cerebellum; 0.49195 0.09301 -0.780646273 12.77423921 65.38152 1.66462 RNF19BPX . . . ring finger protein 19B pseudogene, X-linked . . . . . . . . . . . RNF19BPY . . . ring finger protein 19B pseudogene, Y-linked . . . . . . . . . . . RNF20 0.000923364699321696 0.99907644519072 1.90109958646652e-07 ring finger protein 20 FUNCTION: Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role inb histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. Recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator. Mediates the polyubiquitination of isoform 2 of PA2G4 in cancer cells leading to its proteasome-mediated degradation. {ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16337599, ECO:0000269|PubMed:19037095, ECO:0000269|PubMed:19410543}.; . TISSUE SPECIFICITY: Expressed in the normal brain and also in malignant gliomas (at protein level). {ECO:0000269|PubMed:19037095}.; . . 0.15368 0.12971 -0.598810865 18.13517339 121.63796 2.40133 RNF24 0.898356865489774 0.100710087076674 0.00093304743355182 ring finger protein 24 FUNCTION: May play a role in TRPCs intracellular trafficking. {ECO:0000269|PubMed:17850865}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;testis;brain;unclassifiable (Anatomical System);trophoblast;heart;cartilage;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;stomach; dorsal root ganglion;superior cervical ganglion;adipose tissue;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.08974 0.08061 -0.053113545 49.38664779 6.23907 0.23519 RNF25 0.829695265718338 0.170298431200755 6.30308090707427e-06 ring finger protein 25 FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NKD2 (By similarity). Stimulates transcription mediated by NF-kappa-B. {ECO:0000250, ECO:0000269|PubMed:12748188}.; . . lymphoreticular;medulla oblongata;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;cerebral cortex;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;muscle;blood;lens;breast;lung;mesenchyma;placenta;macula lutea;visual apparatus;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.40063 0.10679 0.86534717 88.80042463 179.8543 2.91411 RNF26 0.677950757165205 0.317415610198363 0.00463363263643193 ring finger protein 26 . . TISSUE SPECIFICITY: Ubiquitous. Up-regulated in several cancer cell lines.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;duodenum;head and neck;cervix;kidney;mammary gland;stomach; . 0.21330 0.13705 -0.558357437 19.54470394 61.29925 1.59481 RNF31 0.999718687079344 0.000281312920492428 1.63257683390858e-13 ring finger protein 31 FUNCTION: E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF- induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types. {ECO:0000269|PubMed:17006537, ECO:0000269|PubMed:19136968, ECO:0000269|PubMed:20005846, ECO:0000269|PubMed:21455173, ECO:0000269|PubMed:21455180, ECO:0000269|PubMed:21455181, ECO:0000269|PubMed:22863777, ECO:0000269|PubMed:23708998}.; . TISSUE SPECIFICITY: Expressed in both normal and transformed breast epithelial cell lines. {ECO:0000269|PubMed:15093743}.; smooth muscle;ovary;foreskin;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;endometrium;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;epidermis;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.16776 0.38741 -0.571310997 19.01391838 363.8652 4.03763 RNF32 1.59862356818775e-08 0.217987463152416 0.782012520861349 ring finger protein 32 FUNCTION: May play a role in sperm formation. {ECO:0000269|PubMed:11890671}.; . TISSUE SPECIFICITY: Highly expressed in testis, less abundant in ovary. {ECO:0000269|PubMed:11890671}.; unclassifiable (Anatomical System);medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;lens;retina;uterus;optic nerve;lung;placenta;macula lutea;visual apparatus;liver;testis;spleen;germinal center;brain; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion; 0.21289 0.10790 0.775339069 87.13729653 2407.60192 9.11294 RNF34 0.190893161577717 0.798048153688446 0.0110586847338372 ring finger protein 34 FUNCTION: E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis (PubMed:15069192). May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway (Ref.13). Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation (PubMed:17121812). Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN (PubMed:18382127). Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells (PubMed:22064484). Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent proteasomal degradation (PubMed:25012219). {ECO:0000269|PubMed:12118383, ECO:0000269|PubMed:15069192, ECO:0000269|PubMed:15897238, ECO:0000269|PubMed:17121812, ECO:0000269|PubMed:22064484, ECO:0000269|PubMed:25012219, ECO:0000269|Ref.13, ECO:0000303|PubMed:18382127}.; . TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, colon and leukocytes. {ECO:0000269|PubMed:12118383, ECO:0000269|PubMed:15069192}.; ovary;salivary gland;intestine;colon;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;duodenum;liver;cervix;spleen;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;thalamus;occipital lobe;medulla oblongata;subthalamic nucleus;prefrontal cortex;testis;pons;atrioventricular node;cingulate cortex;parietal lobe; 0.31619 0.16005 -0.337894035 30.37272942 425.5126 4.31046 RNF38 0.999390256892047 0.000609742466674754 6.41278174464174e-10 ring finger protein 38 FUNCTION: Acts as an E3 ubiquitin-protein ligase able to ubiquitinate p53/TP53 which promotes its relocalization to discrete foci associated with PML nuclear bodies. Exhibits preference for UBE2D2 as a E2 enzyme. {ECO:0000269|PubMed:23973461}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in testis. {ECO:0000269|PubMed:12074600}.; medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;brain;amygdala;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;liver;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;vein;uterus;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.55680 0.11262 -0.471992905 23.03609342 10.65785 0.38690 RNF39 0.00666120713219206 0.915160829309268 0.0781779635585401 ring finger protein 39 FUNCTION: May play a role in prolonged long term-potentiation (LTP) maintenance. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:11130983}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; . 0.32207 0.09952 . . 3842.46168 12.19811 RNF40 0.999994909279865 5.09072013392981e-06 1.12257073491532e-15 ring finger protein 40, E3 ubiquitin protein ligase FUNCTION: Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role in histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. {ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:19410543}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at higher level in testis, heart and pancreas, while it is only weakly expressed in lung, skeletal muscle and small intestine. {ECO:0000269|PubMed:10944455}.; lymphoreticular;medulla oblongata;ovary;salivary gland;colon;parathyroid;choroid;vein;skin;retina;uterus;prostate;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;skeletal muscle;bile duct;pancreas;lung;adrenal gland;epididymis;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;testis - seminiferous tubule;testis; 0.31961 0.17571 -1.993409678 1.757489974 37.70308 1.12232 RNF41 0.856083577085887 0.143437605498702 0.000478817415410745 ring finger protein 41 FUNCTION: Acts as E3 ubiquitin-protein ligase and regulates the degradation of target proteins. Polyubiquitinates MYD88. Negatively regulates MYD88-dependent production of proinflammatory cytokines. Can promote TRIF-dependent production of type I interferon and inhibits infection with vesicular stomatitis virus (By similarity). Promotes also activation of TBK1 and IRF3. Involved in the ubiquitination of erythropoietin (EPO) and interleukin-3 (IL-3) receptors. Thus, through maintaining basal levels of cytokine receptors, RNF41 is involved in the control of hematopoietic progenitor cell differentiation into myeloerythroid lineages (By similarity). Contributes to the maintenance of steady-state ERBB3 levels by mediating its growth factor- independent degradation. Involved in the degradation of the inhibitor of apoptosis BIRC6 and thus is an important regulator of cell death by promoting apoptosis. Acts also as a PARK2 modifier that accelerates its degradation, resulting in a reduction of PARK2 activity, influencing the balance of intracellular redox state. The RNF41-PARK2 pathway regulates autophagosome-lysosome fusion during late mitophagy. Mitophagy is a selective form of autophagy necessary for mitochondrial quality control (PubMed:24949970). {ECO:0000250, ECO:0000250|UniProtKB:Q8BH75, ECO:0000269|PubMed:12411582, ECO:0000269|PubMed:14765125, ECO:0000269|PubMed:15632191, ECO:0000269|PubMed:17210635, ECO:0000269|PubMed:18541373, ECO:0000269|PubMed:19483718, ECO:0000269|PubMed:24949970}.; . TISSUE SPECIFICITY: Detected in ovary, testis and prostate. {ECO:0000269|PubMed:12411582}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;spinal ganglion;brain;pineal gland;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach; whole brain;amygdala;thalamus;superior cervical ganglion;occipital lobe;medulla oblongata;testis - interstitial;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.76957 0.13588 -0.161524709 41.6430762 26.86984 0.86825 RNF43 0.324237751943356 0.675733696194151 2.85518624921115e-05 ring finger protein 43 FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination, endocytosis and subsequent degradation of Wnt receptor complex components Frizzled. Acts on both canonical and non-canonical Wnt signaling pathway. Acts as a tumor suppressor in the intestinal stem cell zone by inhibiting the Wnt signaling pathway, thereby resticting the size of the intestinal stem cell zone. {ECO:0000269|PubMed:18313049, ECO:0000269|PubMed:22575959, ECO:0000269|PubMed:22895187}.; . TISSUE SPECIFICITY: Expressed in fetal kidney, fetal lung, in colon cancer tissues, hepatocellular carcinomas and lung adenocarcinomas. Overexpressed in colorectal cancer cell lines. {ECO:0000269|PubMed:15492824, ECO:0000269|PubMed:18313049}.; . . 0.05291 0.08973 0.736704836 86.32932295 8830.17403 20.26507 RNF44 0.56792965822815 0.431553355097856 0.000516986673993518 ring finger protein 44 . . . lymphoreticular;ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;pancreas;lung;placenta;visual apparatus;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.35919 . -0.179930907 40.35739561 104.3157 2.20769 RNF103 0.832672501332977 0.167297821495983 2.96771710399462e-05 ring finger protein 103 FUNCTION: Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway. {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:18675248}.; . TISSUE SPECIFICITY: Highly expressed in the normal cerebellum but not in the cerebral cortex. {ECO:0000269|PubMed:9070305}.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;head and neck;kidney;stomach;cerebellum; . 0.91528 0.10828 -0.154246007 42.22694032 204.06871 3.08465 RNF103-CHMP3 0.036245866120423 0.928593238160349 0.0351608957192276 RNF103-CHMP3 readthrough FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor. Isoform 2 prevents stress- mediated cell death and accumulation of reactive oxygen species when expressed in yeast cells. {ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:15707591, ECO:0000269|PubMed:16740483, ECO:0000269|PubMed:17331679, ECO:0000269|PubMed:18076377}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:15632132}.; . . . . -0.383807564 27.41802312 . . RNF111 0.999889183334039 0.000110816655893481 1.00670701801258e-11 ring finger protein 111 FUNCTION: Acts in the NODAL pathway of mesoderm patterning during embryonic development. Acts downstream AXIN1 as an E3 ubiquitin- protein ligase which promotes the ubiquitination of inhibitory SMADs such as SMAD7, induces their proteasomal degradation and thereby enhances the transcriptional activity of TGF-beta and BMP. Activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation. Associates with UBE2D2 as an E2 enzyme. {ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17591695, ECO:0000269|PubMed:22411132}.; . TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:14657019}.; smooth muscle;ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; . 0.32094 0.17516 -0.925889687 9.754659118 2481.10145 9.28842 RNF112 0.0036567395135091 0.987234978404795 0.00910828208169547 ring finger protein 112 . . TISSUE SPECIFICITY: Predominantly expressed in brain. {ECO:0000269|PubMed:10574464}.; . . 0.32157 0.24246 . . 57.58728 1.53211 RNF113A 0.822115117314938 0.173877043851382 0.00400783883368003 ring finger protein 113A . . TISSUE SPECIFICITY: Ubiquitous.; . . 0.15510 0.09276 0.547599505 81.2160887 24.78016 0.81407 RNF113B 0.135168377219133 0.779983269075274 0.0848483537055926 ring finger protein 113B . . . medulla oblongata;lung;testis; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;skeletal muscle;parietal lobe; 0.11894 0.09436 0.260991686 70.25831564 200.46799 3.06033 RNF114 0.0170045996254868 0.889205689240938 0.0937897111335751 ring finger protein 114 FUNCTION: E3 ubiquitin-protein ligase promoting the ubiquitination and degradation of the CDK inhibitor CDKN1A and probably also CDKN1B and CDKN1C. These activities stimulate cell cycle's G1-to-S phase transition and suppress cellular senescence. May play a role in spermatogenesis. {ECO:0000269|PubMed:23645206}.; . TISSUE SPECIFICITY: Expressed in numerous tissues, including skin, CD4 lymphocytes and dendritic cells. Highest levels in testis. {ECO:0000269|PubMed:18364390}.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;spinal cord;adrenal cortex;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;placenta;testis;trigeminal ganglion;skeletal muscle; 0.48391 0.11053 0.481458261 79.03986789 58.10862 1.54224 RNF115 0.0806347440374519 0.908781624351597 0.0105836316109508 ring finger protein 115 FUNCTION: E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys-48'- and/or 'Lys-63'-linked polyubiquitination of substrates and may play a role in diverse biological processes. Through their polyubiquitination, may play a role in the endosomal trafficking and degradation of membrane receptors including EGFR, FLT3, MET and CXCR4. {ECO:0000269|PubMed:16288031, ECO:0000269|PubMed:18819927, ECO:0000303|PubMed:23418353}.; . TISSUE SPECIFICITY: Expressed at extremely low levels in normal breast, prostate, lung, colon. Higher levels of expression are detected in heart, skeletal muscle, testis as well as in breast and prostate cancer cells. {ECO:0000269|PubMed:16288031}.; . . 0.49389 0.10488 -0.095386216 46.48502005 43.35188 1.25190 RNF121 0.972894709447048 0.0270984110987502 6.87945420164408e-06 ring finger protein 121 . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;iris;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;pharynx;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach;aorta;cerebellum; superior cervical ganglion; 0.86556 0.11614 -0.494039303 22.09247464 18.40799 0.63772 RNF122 0.0763862528356865 0.872432197993905 0.0511815491704085 ring finger protein 122 FUNCTION: May induce necrosis and apoptosis. May play a role in cell viability. {ECO:0000269|PubMed:16751333}.; . TISSUE SPECIFICITY: Widely expressed in several tissues and cell lines. {ECO:0000269|PubMed:16778963}.; unclassifiable (Anatomical System);uterus;lung;heart;thyroid;blood;brain;bone marrow; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion; 0.17231 0.10898 -0.007201372 53.19061099 23.53634 0.78179 RNF123 0.969714693858756 0.0302853061157792 2.54652347520169e-11 ring finger protein 123 FUNCTION: Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle. {ECO:0000269|PubMed:15531880, ECO:0000269|PubMed:16227581}.; . . smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skeletal muscle; 0.22658 0.10326 -1.120710825 6.605331446 831.63203 5.65005 RNF125 0.0806248454194983 0.872061320716893 0.0473138338636083 ring finger protein 125, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase that acts as a positive regulator of T-cell activation. E3 ligase proteins mediate ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000269|PubMed:15843525}.; . TISSUE SPECIFICITY: Predominantly expressed in lymphoid tissues, including bone marrow, spleen and thymus. Also weakly expressed in other tissues. Predominant in the CD4+ and CD8+ T-cells, suggesting that it is preferentially confined to T-cells. {ECO:0000269|PubMed:12974981, ECO:0000269|PubMed:15843525}.; unclassifiable (Anatomical System);hypothalamus;cervix;skin; superior cervical ganglion; 0.59986 0.10246 0.549415813 81.38122199 606.65521 4.98373 RNF126 0.774554603279982 0.223811493682736 0.00163390303728249 ring finger protein 126 FUNCTION: E3 ubiquitin-protein ligase that regulates several biological processes through ubiquitination of various target proteins. Depending on the associated E2 ligase, mediates 'Lys- 48'- and 'Lys-63'-linked polyubiquitination of substrates. Through their polyubiquitination, may play a role in the endosomal sorting and degradation of several membrane receptors including EGFR, FLT3, MET and CXCR4. May also be part of a BAG6-dependent quality control process ensuring that proteins of the secretory pathway that are mislocalized to the cytosol are degraded by the proteasome. May provide the ubiquitin ligase activity associated with the BAG6 complex and be responsible for ubiquitination of the mislocalized proteins and their targeting to the proteasome (PubMed:24981174). May also play a role in the endosomal recycling of IGF2R, the cation-independent mannose-6-phosphate receptor (PubMed:24275455). By ubiquitinating CDKN1A/p21 and targeting it for degradation, may also promote cell proliferation (PubMed:23026136). May monoubiquitinate AICDA (PubMed:23277564). {ECO:0000250|UniProtKB:Q91YL2, ECO:0000269|PubMed:23277564, ECO:0000269|PubMed:24275455, ECO:0000269|PubMed:24981174, ECO:0000303|PubMed:23026136}.; . TISSUE SPECIFICITY: Highly expressed in liver and testis. {ECO:0000269|PubMed:23026136}.; lymphoreticular;medulla oblongata;ovary;colon;skin;retina;uterus;prostate;endometrium;bone;iris;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;testis;ciliary ganglion;white blood cells;atrioventricular node;parietal lobe; 0.14462 0.11239 -0.468351206 23.42533616 439.52593 4.36897 RNF126P1 . . . ring finger protein 126 pseudogene 1 . . . . . . . . . . . RNF128 0.768185327415573 0.230046828098966 0.00176784448546095 ring finger protein 128, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains formation. Functions as an inhibitor of cytokine gene transcription. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys- 48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down-regulation of these cytosleletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse. Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals. {ECO:0000269|PubMed:12705856, ECO:0000269|PubMed:22016387}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;prostate;cochlea;pituitary gland;bladder;brain;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;kidney;stomach;aorta; superior cervical ganglion;fetal liver;adrenal gland;thyroid; 0.59848 0.16080 0.062575634 58.74026893 28.42924 0.91076 RNF130 0.864935169465201 0.134982497123099 8.23334117005402e-05 ring finger protein 130 FUNCTION: May have a role during the programmed cell death of hematopoietic cells (By similarity). Acts as an E3 ubiquitin- protein ligase. {ECO:0000250, ECO:0000269|PubMed:16549277}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in leukocytes. Not expressed in erythroblasts. {ECO:0000269|PubMed:16549277}.; smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;pineal body;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;hippocampus;duodenum;kidney;aorta;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.81645 0.30035 -0.159704656 41.90846898 50.37508 1.39526 RNF133 0.015150794090117 0.877629919501432 0.107219286408451 ring finger protein 133 FUNCTION: Has E3 ubiquitin-protein ligase activity. {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; dorsal root ganglion;testis - interstitial;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion; 0.26591 . 0.751474114 86.64779429 178.62505 2.90457 RNF135 0.00307516615505143 0.817012897286652 0.179911936558296 ring finger protein 135 FUNCTION: Acts as an E2-dependent E3 ubiquitin-protein ligase, involved in innate immune defense against viruses. Ubiquitinates DDX58 and is required for full activation of the DDX58 signaling resulting in interferon beta production. {ECO:0000269|PubMed:19017631, ECO:0000269|PubMed:19484123}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, spleen, kidney, placenta, prostate, stomach, thyroid and tongue. Also weakly expressed in heart, thymus, liver and lung. {ECO:0000269|PubMed:19017631}.; unclassifiable (Anatomical System);cartilage;ovary;heart;salivary gland;colon;parathyroid;skin;bile duct;prostate;lung;frontal lobe;endometrium;nasopharynx;bone;placenta;liver;germinal center;kidney;brain;mammary gland;tonsil;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.42836 . . . 1918.05923 8.06171 RNF138 0.738927914381854 0.258586814127361 0.00248527149078526 ring finger protein 138, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase involved in DNA damage response by promoting DNA resection and homologous recombination (PubMed:26502055, PubMed:26502057). Recruited to sites of double- strand breaks following DNA damage and specifically promotes double-strand break repair via homologous recombination (PubMed:26502055, PubMed:26502057). Two different, non-exclusive, mechanisms have been proposed. According to a report, regulates the choice of double-strand break repair by favoring homologous recombination over non-homologous end joining (NHEJ): acts by mediating ubiquitination of XRCC5/Ku80, leading to remove the Ku complex from DNA breaks, thereby promoting homologous recombination (PubMed:26502055). According to another report, cooperates with UBE2Ds E2 ubiquitin ligases (UBE2D1, UBE2D2, UBE2D3 or UBE2D4) to promote homologous recombination by mediating ubiquitination of RBBP8/CtIP (PubMed:26502057). Together with NLK, involved in the ubiquitination and degradation of TCF/LEF (PubMed:16714285). Also exhibits auto-ubiquitination activity in combination with UBE2K (PubMed:16714285). May act as a negative regulator in the Wnt/beta-catenin-mediated signaling pathway (PubMed:16714285). {ECO:0000269|PubMed:16714285, ECO:0000269|PubMed:26502055, ECO:0000269|PubMed:26502057}.; . . medulla oblongata;developmental;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;gum;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;white blood cells;trigeminal ganglion; 0.36764 0.11417 0.479642105 78.95140363 136.92005 2.54336 RNF138P1 . . . ring finger protein 138, E3 ubiquitin protein ligase pseudogene 1 . . . . . . . . . . . RNF138P2 . . . ring finger protein 138, E3 ubiquitin protein ligase pseudogene 2 . . . . . . . . . . . RNF139 0.0608738334958745 0.935683545305876 0.00344262119824933 ring finger protein 139 FUNCTION: E3-ubiquitin ligase; acts as a negative regulator of the cell proliferation through mechanisms involving G2/M arrest and cell death. Required for MHC class I ubiquitination in cells expressing the cytomegalovirus protein US2 before dislocation from the endoplasmic reticulum (ER). Affects SREBP processing by hindering the SREBP/SCAP complex translocation from the ER to the Golgi, thereby reducing SREBF2 target gene expression. Required for INSIG1 ubiquitination. May be required for EIF3 complex ubiquitination. May function as a signaling receptor. {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:12032852, ECO:0000269|PubMed:17016439, ECO:0000269|PubMed:19706601, ECO:0000269|PubMed:19720873, ECO:0000269|PubMed:20068067}.; DISEASE: Renal cell carcinoma (RCC) [MIM:144700]: Renal cell carcinoma is a heterogeneous group of sporadic or hereditary carcinoma derived from cells of the proximal renal tubular epithelium. It is subclassified into clear cell renal carcinoma (non-papillary carcinoma), papillary renal cell carcinoma, chromophobe renal cell carcinoma, collecting duct carcinoma with medullary carcinoma of the kidney, and unclassified renal cell carcinoma. Clear cell renal cell carcinoma is the most common subtype. Note=The disease may be caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving RNF139 has been found in a lymphoblastoid cell line established from a family with renal cell carcinoma and thyroid carcinoma. Translocation (3;8)(q14.2;q24.1) with FHIT. RNF139 is found to be fused to FHIT and disrupted within the sterol-sensing domain. In contrast, the FHIT coding region is maintained and expressed. Sporadic cases of renal carcinoma, where an acquired mutation in RNF139 results in the duplication of 12 nucleotides in the 5'-UTR, has also been identified.; TISSUE SPECIFICITY: Highly expressed in testis, placenta and adrenal gland. Moderate expression in heart, brain, liver, skeletal muscle and pancreas, and low expression in lung and kidney. {ECO:0000269|PubMed:9689122}.; myocardium;smooth muscle;ovary;colon;fovea centralis;skin;retina;uterus;prostate;frontal lobe;cochlea;endometrium;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.30669 0.11489 -0.712684326 14.49634348 50.09283 1.38944 RNF139-AS1 . . . RNF139 antisense RNA 1 (head to head) . . . . . . . . . . . RNF141 0.00070215316465317 0.751618101588766 0.247679745246581 ring finger protein 141 FUNCTION: May be involved in spermatogenesis. {ECO:0000269|PubMed:11672448}.; . TISSUE SPECIFICITY: Isoform 1 is testis-specific. Isoform 2 is expressed in heart, brain, skeletal muscle, kidney and pancreas. Isoform 1 is not expressed in fetus or in azoospermic patients. {ECO:0000269|PubMed:11672448}.; ovary;salivary gland;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion;parietal lobe; 0.24632 0.11809 0.25917371 70.05779665 62.11544 1.60637 RNF144A 0.988258456955496 0.0117372122901381 4.33075436583974e-06 ring finger protein 144A FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates the ubiquitination and degradation of the DNA damage kinase PRKDC. {ECO:0000250, ECO:0000269|PubMed:24979766}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland; medulla oblongata;cerebellum peduncles;prefrontal cortex;parietal lobe;cerebellum; 0.15192 0.10676 -0.161524709 41.6430762 17.81597 0.62257 RNF144A-AS1 . . . RNF144A antisense RNA 1 . . . . . . . . . . . RNF144B 0.0276377158382251 0.960947695296661 0.0114145888651133 ring finger protein 144B FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se. {ECO:0000269|PubMed:12853982, ECO:0000269|PubMed:20300062}.; . TISSUE SPECIFICITY: Broadly expressed, with lowest levels in brain and thymus, and highest levels detectable in heart, ovary and testis. {ECO:0000269|PubMed:16427630, ECO:0000269|PubMed:20300062}.; colon;skin;bone marrow;uterus;atrium;frontal lobe;cochlea;endometrium;larynx;thyroid;bone;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;lung;placenta;liver;spleen;head and neck;mammary gland;stomach;aorta; . 0.24190 0.11712 0.060756528 58.52795471 48.42165 1.35715 RNF145 0.663621979090798 0.336332443022211 4.55778869912241e-05 ring finger protein 145 . . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;head and neck;kidney;stomach;peripheral nerve; amygdala;placenta;fetal lung; 0.33859 . -0.736552314 13.93606983 26.28405 0.85227 RNF146 0.44521331275852 0.548293366097874 0.006493321143606 ring finger protein 146 FUNCTION: E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated (PARsylated) proteins and mediates their ubiquitination and subsequent degradation. May regulate many important biological processes, such as cell survival and DNA damage response. Acts as an activator of the Wnt signaling pathway by mediating the ubiquitination of PARsylated AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex. Acts in cooperation with tankyrase proteins (TNKS and TNKS2), which mediate PARsylation of target proteins AXIN1, AXIN2, BLZF1, CASC3, TNKS and TNKS2. Recognizes and binds tankyrase-dependent PARsylated proteins via its WWE domain and mediates their ubiquitination, leading to their degradation. Different ubiquitin linkage types have been observed: TNKS2 undergoes ubiquitination at 'Lys-48' and 'Lys-63', while AXIN1 is only ubiquitinated at 'Lys-48'. May regulate TNKS and TNKS2 subcellular location, preventing aggregation at a centrosomal location. Neuroprotective protein. Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos. Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner. Does not affect PARP1 activation (By similarity). Protects against cell death induced by DNA damaging agents, such as N- methyl-N-nitro-N-nitrosoguanidine (MNNG) and rescues cells from G1 arrest. Promotes cell survival after gamma-irradiation. Facilitates DNA repair. {ECO:0000250, ECO:0000269|PubMed:21478859, ECO:0000269|PubMed:21602803, ECO:0000269|PubMed:21799911, ECO:0000269|PubMed:21825151, ECO:0000269|PubMed:22267412}.; DISEASE: Note=Defects in RNF146 are a cause of susceptibility to breast cancer.; TISSUE SPECIFICITY: Ubiquitously expressed. Up-regulated in brains from patients with Alzheimer disease.; smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;whole body;frontal lobe;cochlea;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;cervix;kidney;stomach;aorta; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle;parietal lobe;cerebellum; 0.05708 0.07309 0.150760231 64.51403633 60.67885 1.58393 RNF148 0.000117583776346138 0.381615205292661 0.618267210930993 ring finger protein 148 . . TISSUE SPECIFICITY: Abundantly expressed in testis and slightly in pancreas. Mainly present in the interstitial cells of testicular tissues. {ECO:0000269|PubMed:24089095}.; . . . . -0.824740496 11.67728238 49.78057 1.38364 RNF149 0.000502223698926861 0.880329737733442 0.119168038567631 ring finger protein 149 FUNCTION: E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation. {ECO:0000269|PubMed:22628551}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;alveolus;liver;spleen;head and neck;cervix;mammary gland;stomach;aorta; superior cervical ganglion;placenta;testis;white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion;whole blood;bone marrow; 0.09149 0.10429 -0.137658575 43.57159707 1814.81969 7.85496 RNF150 0.0136897522513468 0.955445249280842 0.0308649984678109 ring finger protein 150 . . . ovary;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;lens;skeletal muscle;lung;nasopharynx;macula lutea;liver;cervix;spleen;mammary gland; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16117 0.10539 -0.446304853 24.33356924 279.18793 3.58141 RNF151 3.79966413724101e-07 0.0573407326746276 0.942658887358959 ring finger protein 151 FUNCTION: May be involved in acrosome formation of spermatids.; . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.25195 0.09584 . . 395.07081 4.17597 RNF152 0.00705384647515106 0.52937754511006 0.463568608414788 ring finger protein 152 FUNCTION: E3 ubiquitin-protein ligase mediating 'Lys-63'-linked polyubiquitination of RRAGA in response to amino acid starvation. Thereby, regulates mTORC1 signaling and plays a role in the cellular response to amino acid availability (PubMed:25936802). Also mediates 'Lys-48'-linked polyubiquitination of target proteins and their subsequent targeting to the proteasome for degradation. Induces apoptosis when overexpressed (PubMed:21203937). {ECO:0000269|PubMed:21203937, ECO:0000269|PubMed:25936802}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:21203937}.; unclassifiable (Anatomical System);breast;heart;tongue;larynx;sympathetic chain;colon;head and neck;kidney;stomach; . 0.70790 0.11103 -0.093566408 46.7386176 95.66838 2.11348 RNF152P1 . . . ring finger protein 152 pseudogene 1 . . . . . . . . . . . RNF157 0.000108022535284771 0.999391879837104 0.000500097627611183 ring finger protein 157 . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;macula lutea;visual apparatus;liver;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe; 0.11128 0.09618 0.293954043 71.62066525 274.86653 3.55163 RNF157-AS1 . . . RNF157 antisense RNA 1 . . . . . . . . . . . RNF165 0.971099075288373 0.028892860984961 8.06372666568723e-06 ring finger protein 165 . . . unclassifiable (Anatomical System);adrenal cortex;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;frontal lobe;endometrium;adrenal gland;placenta;thyroid;macula lutea;pineal gland;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14451 0.08796 -0.359940251 28.93371078 63.64355 1.63475 RNF166 0.551620567355592 0.434958574078657 0.013420858565751 ring finger protein 166 . . . unclassifiable (Anatomical System);medulla oblongata;lymph node;heart;ovary;islets of Langerhans;adrenal cortex;skin;skeletal muscle;uterus;prostate;lung;oesophagus;endometrium;visual apparatus;testis;spleen;germinal center;brain;stomach; . 0.11689 0.09913 -0.494039303 22.09247464 11.26606 0.40587 RNF167 0.129414191753804 0.865817151003725 0.00476865724247069 ring finger protein 167 FUNCTION: May act as an E3 ubiquitin-protein ligase, or as part of the E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2E1, and then transfers it to substrates, such as SLC22A18. May play a role in growth regulation involved in G1/S transition. {ECO:0000269|PubMed:16314844}.; . TISSUE SPECIFICITY: Strongly expressed in the kidney and liver (at protein level). {ECO:0000269|PubMed:16314844}.; medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus;cerebellum; adrenal gland;kidney; 0.61394 0.11410 -0.358119787 29.16371786 68.48487 1.71277 RNF168 1.37259354976502e-10 0.10003620385757 0.899963796005171 ring finger protein 168, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and H2AX and amplifies the RNF8- dependent H2A ubiquitination, promoting the formation of 'Lys-63'- linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of TP53BP1 and BRCA1. Also recruited at DNA interstrand cross-links (ICLs) sites and promotes accumulation of 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. Following DNA damage, promotes the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF8, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. Not able to initiate 'Lys-63'-linked ubiquitination in vitro; possibly due to partial occlusion of the UBE2N/UBC13-binding region. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively). {ECO:0000269|PubMed:19203578, ECO:0000269|PubMed:19203579, ECO:0000269|PubMed:20550933, ECO:0000269|PubMed:22373579, ECO:0000269|PubMed:22705371, ECO:0000269|PubMed:22713238, ECO:0000269|PubMed:22742833, ECO:0000269|PubMed:22980979}.; DISEASE: Riddle syndrome (RIDDLES) [MIM:611943]: Characterized by increased radiosensitivity, immunodeficiency, mild motor control and learning difficulties, facial dysmorphism, and short stature. Defects are probably due to impaired localization of TP53BP1 and BRCA1 at DNA lesions. {ECO:0000269|PubMed:19203578}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);medulla oblongata;lung;bone;developmental;liver;testis;cervix;kidney;germinal center;brain;mammary gland;skeletal muscle;tonsil;retina; . 0.08332 0.09046 0.424410872 77.25878745 1531.33954 7.27250 RNF169 0.0841392817954343 0.913818772883285 0.00204194532128116 ring finger protein 169 FUNCTION: Probable E3 ubiquitin-protein ligase that acts as a negative regulator of double-strand breaks (DSBs) repair following DNA damage. Recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168 and competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby acting as a negative regulator of DSBs repair. E3 ubiquitin- protein ligase activity is not required for regulation of DSBs repair. {ECO:0000269|PubMed:22492721, ECO:0000269|PubMed:22733822, ECO:0000269|PubMed:22742833}.; . . ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;synovium;bone;pituitary gland;testis;germinal center;brain;artery;gall bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.42105 . -0.556537043 19.72753008 311.37838 3.75555 RNF170 0.648136150929931 0.3505897174546 0.00127413161546842 ring finger protein 170 FUNCTION: E3 ubiquitin-protein ligase that plays an essential role in stimulus-induced inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ubiquitination and degradation via the endoplasmic reticulum-associated degradation (ERAD) pathway. Also involved in ITPR1 turnover in resting cells. {ECO:0000269|PubMed:21610068}.; . TISSUE SPECIFICITY: Expressed in the spinal chord. {ECO:0000269|PubMed:21115467}.; unclassifiable (Anatomical System);ovary;hypothalamus;parathyroid;skeletal muscle;breast;lung;endometrium;nasopharynx;bone;placenta;duodenum;liver;spleen;kidney;brain;stomach; . 0.16835 0.09282 0.170987912 65.5579146 38.11665 1.13269 RNF175 6.78625718663534e-10 0.0700468869248908 0.929953112396483 ring finger protein 175 . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;iris;testis;bladder;brain;unclassifiable (Anatomical System);cartilage;pharynx;blood;lens;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach;aorta;cerebellum; dorsal root ganglion;amygdala;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.07351 . 1.929210393 97.45812692 3089.76696 10.56554 RNF180 5.17341244679766e-05 0.672649595875842 0.32729866999969 ring finger protein 180 FUNCTION: E3 ubiquitin-protein ligase which promotes polyubiquitination and degradation by the proteasome pathway of ZIC2. {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;visual apparatus;brain; superior cervical ganglion;trigeminal ganglion; 0.41298 0.07689 0.108486928 61.90728946 571.53785 4.85009 RNF181 3.13991934782278e-09 0.047007038834599 0.952992958025482 ring finger protein 181 FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000269|PubMed:18331836}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in liver and heart and lowest levels in brain and skeletal muscle. Expressed in platelets (at protein level). {ECO:0000269|PubMed:18331836}.; lymphoreticular;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;bone marrow;uterus;prostate;whole body;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; . 0.23842 0.10146 0.281220278 71.07808445 . . RNF182 0.0120687768208081 0.643279775440699 0.344651447738493 ring finger protein 182 FUNCTION: E3 ubiquitin-protein ligase that mediates the ubiquitination of ATP6V0C and targets it to degradation via the ubiquitin-proteasome pathway. {ECO:0000269|PubMed:18298843}.; . TISSUE SPECIFICITY: Up-regulated in neuronal cells subjected to cell death-inducing injuries, such as oxygen and glucose deprivation (at protein level). Could be up-regulated in Alzheimer disease brains. {ECO:0000269|PubMed:18298843}.; . . 0.23625 0.11046 -0.227663163 37.11370606 24.03513 0.79057 RNF183 0.0375935013159203 0.637008099631668 0.325398399052411 ring finger protein 183 . . . unclassifiable (Anatomical System);lung;cochlea;endometrium;testis;kidney;stomach; . 0.09212 0.10624 0.483275131 79.25218212 5476.86247 15.26401 RNF185 0.679395060761065 0.316034259297232 0.00457067994170311 ring finger protein 185 FUNCTION: E3 ubiquitin-protein ligase that regulates selective mitochondrial autophagy by mediating 'Lys-63'-linked polyubiquitination of BNIP1. Responsible for the cotranslational ubiquitination and degradation of CFTR in the ERAD pathway. Preferentially associates with the E2 enzymes UBE2J1 and UBE2J2. {ECO:0000269|PubMed:21931693, ECO:0000269|PubMed:24019521}.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.38095 . -0.007201372 53.19061099 7.94172 0.29111 RNF185-AS1 . . . RNF185 antisense RNA 1 . . . . . . . . . . . RNF186 0.0154783237731939 0.694222283048139 0.290299393178667 ring finger protein 186 . . . . . 0.08453 0.09834 0.685332364 85.09672092 662.35865 5.15787 RNF187 . . . ring finger protein 187 FUNCTION: E3 ubiquitin-protein ligase that acts as a coactivator of JUN-mediated gene activation in response to growth factor signaling via the MAP3K1 pathway, independently from MAPK8. {ECO:0000269|PubMed:20852630}.; . . myocardium;lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; amygdala;whole brain;superior cervical ganglion;occipital lobe;thalamus;medulla oblongata;hypothalamus;temporal lobe;pons;subthalamic nucleus;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.23355 . . . 5.88068 0.22185 RNF207 5.19011202351337e-06 0.964183419360546 0.0358113905274303 ring finger protein 207 . . . . . 0.09840 . 0.913082291 89.54352442 2247.13325 8.75350 RNF208 0.603529096049194 0.359758913999892 0.0367119899509136 ring finger protein 208 . . . . . 0.41496 0.11032 -0.05129383 49.75819769 20.18316 0.69024 RNF212 0.125225584495356 0.869720007694598 0.00505440781004613 ring finger protein 212 FUNCTION: SUMO E3 ligase that acts as a regulator of crossing-over during meiosis: required to couple chromosome synapsis to the formation of crossover-specific recombination complexes. Localizes to recombination sites and stabilizes meiosis-specific recombination factors, such as MutS-gamma complex proteins (MSH4 and MSH5) and TEX11. May mediate sumoylation of target proteins MSH4 and/or MSH5, leading to enhance their binding to recombination sites. Acts as a limiting factor for crossover designation and/or reinforcement and plays an antagonist role with CCNB1IP1/HEI10 in the regulation of meiotic recombination (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);testis; . 0.13995 . . . 166.87321 2.82299 RNF212B . . . ring finger protein 212B . . . . . . . . . . . RNF213 1.67778352788526e-29 0.99999994137761 5.86223897809217e-08 ring finger protein 213 FUNCTION: Probable E3 ubiquitin-protein ligase that may play a role in angiogenesis. May also have an ATPase activity.; DISEASE: Moyamoya disease 2 (MYMY2) [MIM:607151]: A progressive cerebral angiopathy characterized by bilateral intracranial carotid artery stenosis and telangiectatic vessels in the region of the basal ganglia. The abnormal vessels resemble a 'puff of smoke' (moyamoya) on cerebral angiogram. Affected individuals can develop transient ischemic attacks and/or cerebral infarction, and rupture of the collateral vessels can cause intracranial hemorrhage. Hemiplegia of sudden onset and epileptic seizures constitute the prevailing presentation in childhood, while subarachnoid bleeding occurs more frequently in adults. {ECO:0000269|PubMed:21048783, ECO:0000269|PubMed:21799892}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving ALO17 is associated with anaplastic large-cell lymphoma (ALCL). Translocation t(2;17)(p23;q25) with ALK.; TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:21799892}.; smooth muscle;ovary;colon;parathyroid;choroid;fovea centralis;vein;skin;bone marrow;retina;uterus;prostate;whole body;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;small intestine;heart;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;macula lutea;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; uterus;dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.27678 . 1.993454751 97.65274829 3964.07552 12.45610 RNF214 0.830018244677536 0.169975484822182 6.27050028247705e-06 ring finger protein 214 . . . medulla oblongata;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;breast;pancreas;lung;placenta;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;trigeminal ganglion; 0.16541 . -0.490397599 22.50530786 72.66565 1.77882 RNF215 0.000386646001224259 0.843352092750958 0.156261261247818 ring finger protein 215 . . . prostate;lymph node; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.16964 . 0.218717575 68.27081859 199.73835 3.05359 RNF216 0.409334345064788 0.590665052161564 6.02773648186951e-07 ring finger protein 216 FUNCTION: Isoform 1 acts as an E3 ubiquitin ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Promotes degradation of TRAF3, TLR4 and TLR9. Contributes to the regulation of antiviral responses. Down- regulates activation of NF-kappa-B, IRF3 activation and IFNB production. Isoform 3/ZIN inhibits TNF and IL-1 mediated activation of NF-kappa-B. Promotes TNF and RIP mediated apoptosis. {ECO:0000269|PubMed:15107846, ECO:0000269|PubMed:19893624}.; DISEASE: Gordon Holmes syndrome (GDHS) [MIM:212840]: A disease characterized by cerebellar symptoms and signs of sex steroid deficiency. Clinical features include cerebellar and brain stem atrophy, cerebellar ataxia, hypothalamic LHRH deficiency, hypogonadotrophic hypogonadism, lack of secondary sexual characteristics, and infertility. {ECO:0000269|PubMed:23656588}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous, with the highest levels of expression in testis and peripheral blood leukocytes.; . . 0.12144 0.08992 -1.188670131 5.891719745 131.90997 2.50090 RNF216-IT1 . . . RNF216 intronic transcript 1 . . . . . . . . . . . RNF216P1 . . . ring finger protein 216 pseudogene 1 . . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;lens;skeletal muscle;bile duct;breast;pancreas;lung;macula lutea;cervix;kidney; . . . . . . . RNF217 0.0299836634081045 0.959889099325529 0.0101272372663666 ring finger protein 217 FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;cartilage;adrenal cortex;colon;blood;parathyroid;skin;bone marrow;frontal lobe;endometrium;adrenal gland;placenta;thyroid;testis;pineal gland;stomach; superior cervical ganglion;atrioventricular node; 0.02856 . 0.328949044 73.41354093 336.83992 3.89812 RNF217-AS1 . . . RNF217 antisense RNA 1 (head to head) . . . . . . . . . . . RNF219 2.48629783293926e-05 0.91810416155842 0.0818709754632507 ring finger protein 219 . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;pharynx;blood;lens;skeletal muscle;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion; 0.70616 0.09323 -0.111973265 45.35857514 81.05634 1.90575 RNF219-AS1 . . . RNF219 antisense RNA 1 . . . . . . . . . . . RNF220 0.999277879441591 0.00072211958999983 9.68409647645081e-10 ring finger protein 220 FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of SIN3B (By similarity). Independently of its E3 ligase activity, acts as a CTNNB1 stabilizer through USP7-mediated deubiquitination of CTNNB1 promoting Wnt signaling (PubMed:25266658). {ECO:0000250|UniProtKB:Q6PDX6, ECO:0000269|PubMed:25266658}.; . . myocardium;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;synovium;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;cerebellum; whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;spinal cord;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.74271 0.10951 -0.646543901 16.44255721 77.57306 1.85372 RNF222 . . . ring finger protein 222 . . . . . . . . . 273.95976 3.54610 RNF223 . . . ring finger protein 223 . . . . . . . . . 350.3187 3.96842 RNF224 . . . ring finger protein 224 . . . . . . . . . 860.70297 5.72242 RNF225 . . . ring finger protein 225 . . . . . . . . . . . RNFT1 0.011205655064819 0.979939258817182 0.00885508611799933 ring finger protein, transmembrane 1 . . TISSUE SPECIFICITY: Expressed at highest levels in testis, lower levels in heart, liver, lung, and kidney. Not detected in brain, ovary, and uterus. Down-regulated in testis from patients with maturation arrest (MA) or Sertoli cell-only syndrome (SCOS). {ECO:0000269|PubMed:17074343}.; medulla oblongata;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;skin;bone marrow;prostate;atrium;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion; 0.08208 0.09419 -0.003562597 53.72729417 79.51704 1.88411 RNFT1P1 . . . ring finger protein, transmembrane 1 pseudogene 1 . . . . . . . . . . . RNFT1P2 . . . ring finger protein, transmembrane 1 pseudogene 2 . . . . . . . . . . . RNFT1P3 . . . ring finger protein, transmembrane 1 pseudogene 3 . . . . . . . . . . . RNFT2 0.790709970439595 0.209018319446117 0.000271710114287776 ring finger protein, transmembrane 2 . . . medulla oblongata;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;frontal lobe;bone;testis;germinal center;brain;amygdala;unclassifiable (Anatomical System);lymph node;muscle;pharynx;blood;lung;cornea;visual apparatus;liver;cervix;spleen;kidney;mammary gland;cerebellum; amygdala;dorsal root ganglion;whole brain;superior cervical ganglion;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.17258 . -0.80269335 12.23755603 55.40984 1.49436 RNGTT 0.763456431133887 0.236540369185524 3.19968058895243e-06 RNA guanylyltransferase and 5'-phosphatase FUNCTION: Bifunctional mRNA-capping enzyme exhibiting RNA 5'- triphosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the gmp moiety of GTP to the 5'-diphosphate terminus. {ECO:0000269|PubMed:21636784, ECO:0000269|PubMed:9473487, ECO:0000269|PubMed:9512541}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 4 (at a lesser extent) are expressed in cerebrum, cerebellum, thyroid, lung, heart, liver, kidney, spleen, large intestine, testis, skin and muscle.; ovary;colon;fovea centralis;choroid;skin;bone marrow;retina;optic nerve;whole body;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;hippocampus;macula lutea;liver;spleen;head and neck; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.84113 0.19698 -0.558357437 19.54470394 54.7413 1.48185 RNGTTP1 . . . RNA guanylyltransferase and 5'-phosphatase pseudogene 1 . . . . . . . . . . . RNH1 0.000213431930050961 0.910380353182292 0.0894062148876569 ribonuclease/angiogenin inhibitor 1 FUNCTION: Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis. {ECO:0000269|PubMed:12578357, ECO:0000269|PubMed:14515218, ECO:0000269|PubMed:17292889}.; . . myocardium;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;placenta;head and neck;kidney;stomach; heart;thyroid; 0.10917 0.40837 -0.154246007 42.22694032 903.41886 5.85204 RNLS 1.04360345149786e-06 0.334750790837887 0.665248165558662 renalase, FAD-dependent amine oxidase FUNCTION: Catalyzes the oxidation of the less abundant 1,2- dihydro-beta-NAD(P) and 1,6-dihydro-beta-NAD(P) to form beta- NAD(P)(+). The enzyme hormone is secreted by the kidney, and circulates in blood and modulates cardiac function and systemic blood pressure. Lowers blood pressure in vivo by decreasing cardiac contractility and heart rate and preventing a compensatory increase in peripheral vascular tone, suggesting a causal link to the increased plasma catecholamine and heightened cardiovascular risk. High concentrations of catecholamines activate plasma renalase and promotes its secretion and synthesis. {ECO:0000269|PubMed:15841207, ECO:0000269|PubMed:17385068, ECO:0000269|PubMed:25531177}.; . TISSUE SPECIFICITY: Secreted into the blood by the kidney. Highly expressed in the kidney, expressed at lower level in heart, skeletal muscle and small intestine. Its plasma concentration is markedly reduced in patients with end-stage renal disease, as compared with healthy subjects. {ECO:0000269|PubMed:15841207}.; unclassifiable (Anatomical System);uterus;lung;cartilage;heart;placenta;testis;parathyroid;kidney;brain;skin;retina; atrioventricular node;trigeminal ganglion; 0.07858 0.11546 0.839664339 88.29912715 2865.38231 10.13028 RNMT 0.0809328060183284 0.916890374570406 0.002176819411266 RNA (guanine-7-) methyltransferase FUNCTION: mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC. {ECO:0000269|PubMed:10347220, ECO:0000269|PubMed:22099306, ECO:0000269|PubMed:9705270, ECO:0000269|PubMed:9790902}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9705270, ECO:0000269|PubMed:9790902}.; ovary;salivary gland;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;synovium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;medulla oblongata;superior cervical ganglion;thalamus;caudate nucleus;atrioventricular node;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;testis;trigeminal ganglion;cingulate cortex; 0.40794 0.11054 0.082802743 60.09082331 61.26292 1.59385 RNMTL1 1.81967911622819e-07 0.242948716362633 0.757051101669456 RNA methyltransferase like 1 FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O- methylguanosine at position 1370 (Gm1370) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a conserved modification in the peptidyl transferase domain of the mtLSU rRNA. {ECO:0000269|PubMed:24036117, ECO:0000269|PubMed:25009282, ECO:0000269|PubMed:25074936}.; . TISSUE SPECIFICITY: Expressed at same level in normal liver and hepatocarcinoma. {ECO:0000269|PubMed:12296377}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;adrenal cortex;pharynx;blood;lens;breast;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;trigeminal ganglion; 0.08761 . 0.20030965 67.3566879 2382.57907 9.05897 RNMTL1P1 . . . RNA methyltransferase like 1 pseudogene 1 . . . . . . . . . . . RNMTL1P2 . . . RNA methyltransferase like 1 pseudogene 2 . . . . . . . . . . . RNPC3 0.525297994226153 0.412259632615535 0.0624423731583122 RNA binding region (RNP1, RRM) containing 3 FUNCTION: Participates in pre-mRNA U12-dependent splicing, performed by the minor spliceosome which removes U12-type introns. U12-type introns comprises less than 1% of all non-coding sequences. Binds to the 3'-stem-loop of m(7)G-capped U12 snRNA. {ECO:0000269|PubMed:16096647, ECO:0000269|PubMed:19447915}.; . TISSUE SPECIFICITY: Highly expressed in pancreas and kidney. Detected at lower levels in heart, brain, placenta, lung, liver, spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocytes. {ECO:0000269|PubMed:14974681}.; . . 0.09040 . -0.009020804 52.8544468 38.2065 1.13384 RNPC3P1 . . . RNA binding region (RNP1, RRM) containing 3 pseudogene 1 . . . . . . . . . . . RNPEP 4.80666222710557e-11 0.103679485417392 0.896320514534542 arginyl aminopeptidase FUNCTION: Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(- 1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pineal body;muscle;urinary;blood;skeletal muscle;breast;bile duct;pancreas;lung;trachea;adrenal gland;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; . 0.18495 0.22579 -0.598810865 18.13517339 2186.42242 8.61411 RNPEPL1 0.0279016170372594 0.960841519664889 0.0112568632978515 arginyl aminopeptidase (aminopeptidase B)-like 1 . . TISSUE SPECIFICITY: Ubiquitous. Expressed at relatively higher levels in heart and skeletal muscle. {ECO:0000269|PubMed:11017071}.; salivary gland;sympathetic chain;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion; 0.20691 0.11110 . . 27.51822 0.88645 RNPS1 0.94850298717449 0.0513298810345398 0.000167131790970557 RNA binding protein S1, serine-rich domain FUNCTION: Part of pre- and post-splicing multiprotein mRNP complexes. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Enhances the formation of the ATP-dependent A complex of the spliceosome. Involved in both constitutive splicing and, in association with SRP54 and TRA2B/SFRS10, in distinctive modulation of alternative splicing in a substrate-dependent manner. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Participates in mRNA 3'-end cleavage. Involved in UPF2- dependent nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Also mediates increase of mRNA abundance and translational efficiency. Binds spliced mRNA 20-25 nt upstream of exon-exon junctions. {ECO:0000269|PubMed:10449421, ECO:0000269|PubMed:11546874, ECO:0000269|PubMed:12665594, ECO:0000269|PubMed:12944400, ECO:0000269|PubMed:14729963, ECO:0000269|PubMed:14752011, ECO:0000269|PubMed:15684395, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:17586820, ECO:0000269|PubMed:22203037}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8543184}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;tonsil;heart;pineal body;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;colon;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;aorta; whole brain;amygdala;prostate;cerebellum peduncles;prefrontal cortex;testis;globus pallidus;cingulate cortex;cerebellum; 0.40433 0.14229 -0.183570861 39.95046001 38.82288 1.14973 RNPS1P1 . . . RNA binding protein S1, serine-rich domain pseudogene 1 . . . . . . . . . . . RNR1 . . . RNA, ribosomal cluster 1 . . . . . . . . . . . RNR2 . . . RNA, ribosomal cluster 2 . . . . . . . . . . . RNR3 . . . RNA, ribosomal cluster 3 . . . . . . . . . . . RNR4 . . . RNA, ribosomal cluster 4 . . . . . . . . . . . RNR5 . . . RNA, ribosomal cluster 5 . . . . . . . . . . . RNU1-1 . . . RNA, U1 small nuclear 1 . . . . . . . . . . . RNU1-2 . . . RNA, U1 small nuclear 2 . . . . . . . . . . . RNU1-3 . . . RNA, U1 small nuclear 3 . . . . . . . . . . . RNU1-4 . . . RNA, U1 small nuclear 4 . . . . . . . . . . . RNU1-5P . . . RNA, U1 small nuclear 5, pseudogene . . . . . . . . . . . RNU1-6P . . . RNA, U1 small nuclear 6, pseudogene . . . . . . . . . . . RNU1-7P . . . RNA, U1 small nuclear 7, pseudogene . . . . . . . . . . . RNU1-8P . . . RNA, U1 small nuclear 8, pseudogene . . . . . . . . . . . RNU1-11P . . . RNA, U1 small nuclear 11, pseudogene . . . . . . . . . . . RNU1-13P . . . RNA, U1 small nuclear 13, pseudogene . . . . . . . . . . . RNU1-14P . . . RNA, U1 small nuclear 14, pseudogene . . . . . . . . . . . RNU1-15P . . . RNA, U1 small nuclear 15, pseudogene . . . . . . . . . . . RNU1-16P . . . RNA, U1 small nuclear 16, pseudogene . . . . . . . . . . . RNU1-17P . . . RNA, U1 small nuclear 17, pseudogene . . . . . . . . . . . RNU1-18P . . . RNA, U1 small nuclear 18, pseudogene . . . . . . . . . . . RNU1-19P . . . RNA, U1 small nuclear 19, pseudogene . . . . . . . . . . . RNU1-20P . . . RNA, U1 small nuclear 20, pseudogene . . . . . . . . . . . RNU1-21P . . . RNA, U1 small nuclear 21, pseudogene . . . . . . . . . . . RNU1-22P . . . RNA, U1 small nuclear 22, pseudogene . . . . . . . . . . . RNU1-23P . . . RNA, U1 small nuclear 23, pseudogene . . . . . . . . . . . RNU1-24P . . . RNA, U1 small nuclear 24, pseudogene . . . . . . . . . . . RNU1-27P . . . RNA, U1 small nuclear 27, pseudogene . . . . . . . . . . . RNU1-28P . . . RNA, U1 small nuclear 28, pseudogene . . . . . . . . . . . RNU1-29P . . . RNA, U1 small nuclear 29, pseudogene . . . . . . . . . . . RNU1-30P . . . RNA, U1 small nuclear 30, pseudogene . . . . . . . . . . . RNU1-31P . . . RNA, U1 small nuclear 31, pseudogene . . . . . . . . . . . RNU1-32P . . . RNA, U1 small nuclear 32, pseudogene . . . . . . . . . . . RNU1-33P . . . RNA, U1 small nuclear 33, pseudogene . . . . . . . . . . . RNU1-34P . . . RNA, U1 small nuclear 34, pseudogene . . . . . . . . . . . RNU1-35P . . . RNA, U1 small nuclear 35, pseudogene . . . . . . . . . . . RNU1-36P . . . RNA, U1 small nuclear 36, pseudogene . . . . . . . . . . . RNU1-38P . . . RNA, U1 small nuclear 38, pseudogene . . . . . . . . . . . RNU1-39P . . . RNA, U1 small nuclear 39, pseudogene . . . . . . . . . . . RNU1-40P . . . RNA, U1 small nuclear 40, pseudogene . . . . . . . . . . . RNU1-41P . . . RNA, U1 small nuclear 41, pseudogene . . . . . . . . . . . RNU1-42P . . . RNA, U1 small nuclear 42, pseudogene . . . . . . . . . . . RNU1-43P . . . RNA, U1 small nuclear 43, pseudogene . . . . . . . . . . . RNU1-44P . . . RNA, U1 small nuclear 44, pseudogene . . . . . . . . . . . RNU1-45P . . . RNA, U1 small nuclear 45, pseudogene . . . . . . . . . . . RNU1-46P . . . RNA, U1 small nuclear 46, pseudogene . . . . . . . . . . . RNU1-47P . . . RNA, U1 small nuclear 47, pseudogene . . . . . . . . . . . RNU1-48P . . . RNA, U1 small nuclear 48, pseudogene . . . . . . . . . . . RNU1-49P . . . RNA, U1 small nuclear 49, pseudogene . . . . . . . . . . . RNU1-51P . . . RNA, U1 small nuclear 51, pseudogene . . . . . . . . . . . RNU1-52P . . . RNA, U1 small nuclear 52, pseudogene . . . . . . . . . . . RNU1-54P . . . RNA, U1 small nuclear 54, pseudogene . . . . . . . . . . . RNU1-55P . . . RNA, U1 small nuclear 55, pseudogene . . . . . . . . . . . RNU1-56P . . . RNA, U1 small nuclear 56, pseudogene . . . . . . . . . . . RNU1-57P . . . RNA, U1 small nuclear 57, pseudogene . . . . . . . . . . . RNU1-58P . . . RNA, U1 small nuclear 58, pseudogene . . . . . . . . . . . RNU1-59P . . . RNA, U1 small nuclear 59, pseudogene . . . . . . . . . . . RNU1-61P . . . RNA, U1 small nuclear 61, pseudogene . . . . . . . . . . . RNU1-62P . . . RNA, U1 small nuclear 62, pseudogene . . . . . . . . . . . RNU1-63P . . . RNA, U1 small nuclear 63, pseudogene . . . . . . . . . . . RNU1-64P . . . RNA, U1 small nuclear 64, pseudogene . . . . . . . . . . . RNU1-65P . . . RNA, U1 small nuclear 65, pseudogene . . . . . . . . . . . RNU1-67P . . . RNA, U1 small nuclear 67, pseudogene . . . . . . . . . . . RNU1-68P . . . RNA, U1 small nuclear 68, pseudogene . . . . . . . . . . . RNU1-69P . . . RNA, U1 small nuclear 69, pseudogene . . . . . . . . . . . RNU1-70P . . . RNA, U1 small nuclear 70, pseudogene . . . . . . . . . . . RNU1-72P . . . RNA, U1 small nuclear 72, pseudogene . . . . . . . . . . . RNU1-73P . . . RNA, U1 small nuclear 73, pseudogene . . . . . . . . . . . RNU1-74P . . . RNA, U1 small nuclear 74, pseudogene . . . . . . . . . . . RNU1-75P . . . RNA, U1 small nuclear 75, pseudogene . . . . . . . . . . . RNU1-76P . . . RNA, U1 small nuclear 76, pseudogene . . . . . . . . . . . RNU1-77P . . . RNA, U1 small nuclear 77, pseudogene . . . . . . . . . . . RNU1-78P . . . RNA, U1 small nuclear 78, pseudogene . . . . . . . . . . . RNU1-79P . . . RNA, U1 small nuclear 79, pseudogene . . . . . . . . . . . RNU1-80P . . . RNA, U1 small nuclear 80, pseudogene . . . . . . . . . . . RNU1-82P . . . RNA, U1 small nuclear 82, pseudogene . . . . . . . . . . . RNU1-83P . . . RNA, U1 small nuclear 83, pseudogene . . . . . . . . . . . RNU1-84P . . . RNA, U1 small nuclear 84, pseudogene . . . . . . . . . . . RNU1-85P . . . RNA, U1 small nuclear 85, pseudogene . . . . . . . . . . . RNU1-86P . . . RNA, U1 small nuclear 86, pseudogene . . . . . . . . . . . RNU1-87P . . . RNA, U1 small nuclear 87, pseudogene . . . . . . . . . . . RNU1-88P . . . RNA, U1 small nuclear 88, pseudogene . . . . . . . . . . . RNU1-89P . . . RNA, U1 small nuclear 89, pseudogene . . . . . . . . . . . RNU1-91P . . . RNA, U1 small nuclear 91, pseudogene . . . . . . . . . . . RNU1-92P . . . RNA, U1 small nuclear 92, pseudogene . . . . . . . . . . . RNU1-93P . . . RNA, U1 small nuclear 93, pseudogene . . . . . . . . . . . RNU1-94P . . . RNA, U1 small nuclear 94, pseudogene . . . . . . . . . . . RNU1-95P . . . RNA, U1 small nuclear 95, pseudogene . . . . . . . . . . . RNU1-96P . . . RNA, U1 small nuclear 96, pseudogene . . . . . . . . . . . RNU1-97P . . . RNA, U1 small nuclear 97, pseudogene . . . . . . . . . . . RNU1-98P . . . RNA, U1 small nuclear 98, pseudogene . . . . . . . . . . . RNU1-100P . . . RNA, U1 small nuclear 100, pseudogene . . . . . . . . . . . RNU1-101P . . . RNA, U1 small nuclear 101, pseudogene . . . . . . . . . . . RNU1-103P . . . RNA, U1 small nuclear 103, pseudogene . . . . . . . . . . . RNU1-104P . . . RNA, U1 small nuclear 104, pseudogene . . . . . . . . . . . RNU1-105P . . . RNA, U1 small nuclear 105, pseudogene . . . . . . . . . . . RNU1-106P . . . RNA, U1 small nuclear 106, pseudogene . . . . . . . . . . . RNU1-107P . . . RNA, U1 small nuclear 107, pseudogene . . . . . . . . . . . RNU1-108P . . . RNA, U1 small nuclear 108, pseudogene . . . . . . . . . . . RNU1-109P . . . RNA, U1 small nuclear 109, pseudogene . . . . . . . . . . . RNU1-112P . . . RNA, U1 small nuclear 112, pseudogene . . . . . . . . . . . RNU1-114P . . . RNA, U1 small nuclear 114, pseudogene . . . . . . . . . . . RNU1-115P . . . RNA, U1 small nuclear 115, pseudogene . . . . . . . . . . . RNU1-116P . . . RNA, U1 small nuclear 116, pseudogene . . . . . . . . . . . RNU1-117P . . . RNA, U1 small nuclear 117, pseudogene . . . . . . . . . . . RNU1-119P . . . RNA, U1 small nuclear 119, pseudogene . . . . . . . . . . . RNU1-120P . . . RNA, U1 small nuclear 120, pseudogene . . . . . . . . . . . RNU1-122P . . . RNA, U1 small nuclear 122, pseudogene . . . . . . . . . . . RNU1-123P . . . RNA, U1 small nuclear 123, pseudogene . . . . . . . . . . . RNU1-124P . . . RNA, U1 small nuclear 124, pseudogene . . . . . . . . . . . RNU1-125P . . . RNA, U1 small nuclear 125, pseudogene . . . . . . . . . . . RNU1-128P . . . RNA, U1 small nuclear 128, pseudogene . . . . . . . . . . . RNU1-129P . . . RNA, U1 small nuclear 129, pseudogene . . . . . . . . . . . RNU1-130P . . . RNA, U1 small nuclear 130, pseudogene . . . . . . . . . . . RNU1-131P . . . RNA, U1 small nuclear 131, pseudogene . . . . . . . . . . . RNU1-132P . . . RNA, U1 small nuclear 132, pseudogene . . . . . . . . . . . RNU1-133P . . . RNA, U1 small nuclear 133, pseudogene . . . . . . . . . . . RNU1-134P . . . RNA, U1 small nuclear 134, pseudogene . . . . . . . . . . . RNU1-136P . . . RNA, U1 small nuclear 136, pseudogene . . . . . . . . . . . RNU1-138P . . . RNA, U1 small nuclear 138, pseudogene . . . . . . . . . . . RNU1-139P . . . RNA, U1 small nuclear 139, pseudogene . . . . . . . . . . . RNU1-140P . . . RNA, U1 small nuclear 140, pseudogene . . . . . . . . . . . RNU1-141P . . . RNA, U1 small nuclear 141, pseudogene . . . . . . . . . . . RNU1-142P . . . RNA, U1 small nuclear 142, pseudogene . . . . . . . . . . . RNU1-143P . . . RNA, U1 small nuclear 143, pseudogene . . . . . . . . . . . RNU1-146P . . . RNA, U1 small nuclear 146, pseudogene . . . . . . . . . . . RNU1-148P . . . RNA, U1 small nuclear 148, pseudogene . . . . . . . . . . . RNU1-149P . . . RNA, U1 small nuclear 149, pseudogene . . . . . . . . . . . RNU1-150P . . . RNA, U1 small nuclear 150, pseudogene . . . . . . . . . . . RNU2-1 . . . RNA, U2 small nuclear 1 . . . . . . . . . . . RNU2-2P . . . RNA, U2 small nuclear 2, pseudogene . . . . . . . . . . . RNU2-3P . . . RNA, U2 small nuclear 3, pseudogene . . . . . . . . . . . RNU2-4P . . . RNA, U2 small nuclear 4, pseudogene . . . . . . . . . . . RNU2-5P . . . RNA, U2 small nuclear 5, pseudogene . . . . . . . . . . . RNU2-6P . . . RNA, U2 small nuclear 6, pseudogene . . . . . . . . . . . RNU2-7P . . . RNA, U2 small nuclear 7, pseudogene . . . . . . . . . . . RNU2-8P . . . RNA, U2 small nuclear 8, pseudogene . . . . . . . . . . . RNU2-9P . . . RNA, U2 small nuclear 9, pseudogene . . . . . . . . . . . RNU2-10P . . . RNA, U2 small nuclear 10, pseudogene . . . . . . . . . . . RNU2-11P . . . RNA, U2 small nuclear 11, pseudogene . . . . . . . . . . . RNU2-12P . . . RNA, U2 small nuclear 12, pseudogene . . . . . . . . . . . RNU2-13P . . . RNA, U2 small nuclear 13, pseudogene . . . . . . . . . . . RNU2-14P . . . RNA, U2 small nuclear 14, pseudogene . . . . . . . . . . . RNU2-15P . . . RNA, U2 small nuclear 15, pseudogene . . . . . . . . . . . RNU2-16P . . . RNA, U2 small nuclear 16, pseudogene . . . . . . . . . . . RNU2-17P . . . RNA, U2 small nuclear 17, pseudogene . . . . . . . . . . . RNU2-18P . . . RNA, U2 small nuclear 18, pseudogene . . . . . . . . . . . RNU2-19P . . . RNA, U2 small nuclear 19, pseudogene . . . . . . . . . . . RNU2-20P . . . RNA, U2 small nuclear 20, pseudogene . . . . . . . . . . . RNU2-21P . . . RNA, U2 small nuclear 21, pseudogene . . . . . . . . . . . RNU2-22P . . . RNA, U2 small nuclear 22, pseudogene . . . . . . . . . . . RNU2-23P . . . RNA, U2 small nuclear 23, pseudogene . . . . . . . . . . . RNU2-24P . . . RNA, U2 small nuclear 24, pseudogene . . . . . . . . . . . RNU2-25P . . . RNA, U2 small nuclear 25, pseudogene . . . . . . . . . . . RNU2-26P . . . RNA, U2 small nuclear 26, pseudogene . . . . . . . . . . . RNU2-27P . . . RNA, U2 small nuclear 27, pseudogene . . . . . . . . . . . RNU2-28P . . . RNA, U2 small nuclear 28, pseudogene . . . . . . . . . . . RNU2-29P . . . RNA, U2 small nuclear 29, pseudogene . . . . . . . . . . . RNU2-30P . . . RNA, U2 small nuclear 30, pseudogene . . . . . . . . . . . RNU2-31P . . . RNA, U2 small nuclear 31, pseudogene . . . . . . . . . . . RNU2-32P . . . RNA, U2 small nuclear 32, pseudogene . . . . . . . . . . . RNU2-33P . . . RNA, U2 small nuclear 33, pseudogene . . . . . . . . . . . RNU2-34P . . . RNA, U2 small nuclear 34, pseudogene . . . . . . . . . . . RNU2-35P . . . RNA, U2 small nuclear 35, pseudogene . . . . . . . . . . . RNU2-36P . . . RNA, U2 small nuclear 36, pseudogene . . . . . . . . . . . RNU2-37P . . . RNA, U2 small nuclear 37, pseudogene . . . . . . . . . . . RNU2-38P . . . RNA, U2 small nuclear 38, pseudogene . . . . . . . . . . . RNU2-39P . . . RNA, U2 small nuclear 39, pseudogene . . . . . . . . . . . RNU2-40P . . . RNA, U2 small nuclear 40, pseudogene . . . . . . . . . . . RNU2-41P . . . RNA, U2 small nuclear 41, pseudogene . . . . . . . . . . . RNU2-42P . . . RNA, U2 small nuclear 42, pseudogene . . . . . . . . . . . RNU2-43P . . . RNA, U2 small nuclear 43, pseudogene . . . . . . . . . . . RNU2-44P . . . RNA, U2 small nuclear 44, pseudogene . . . . . . . . . . . RNU2-45P . . . RNA, U2 small nuclear 45, pseudogene . . . . . . . . . . . RNU2-46P . . . RNA, U2 small nuclear 46, pseudogene . . . . . . . . . . . RNU2-47P . . . RNA, U2 small nuclear 47, pseudogene . . . . . . . . . . . RNU2-48P . . . RNA, U2 small nuclear 48, pseudogene . . . . . . . . . . . RNU2-49P . . . RNA, U2 small nuclear 49, pseudogene . . . . . . . . . . . RNU2-50P . . . RNA, U2 small nuclear 50, pseudogene . . . . . . . . . . . RNU2-51P . . . RNA, U2 small nuclear 51, pseudogene . . . . . . . . . . . RNU2-52P . . . RNA, U2 small nuclear 52, pseudogene . . . . . . . . . . . RNU2-53P . . . RNA, U2 small nuclear 53, pseudogene . . . . . . . . . . . RNU2-54P . . . RNA, U2 small nuclear 54, pseudogene . . . . . . . . . . . RNU2-55P . . . RNA, U2 small nuclear 55, pseudogene . . . . . . . . . . . RNU2-56P . . . RNA, U2 small nuclear 56, pseudogene . . . . . . . . . . . RNU2-57P . . . RNA, U2 small nuclear 57, pseudogene . . . . . . . . . . . RNU2-58P . . . RNA, U2 small nuclear 58, pseudogene . . . . . . . . . . . RNU2-59P . . . RNA, U2 small nuclear 59, pseudogene . . . . . . . . . . . RNU2-60P . . . RNA, U2 small nuclear 60, pseudogene . . . . . . . . . . . RNU2-61P . . . RNA, U2 small nuclear 61, pseudogene . . . . . . . . . . . RNU2-62P . . . RNA, U2 small nuclear 62, pseudogene . . . . . . . . . . . RNU2-63P . . . RNA, U2 small nuclear 63, pseudogene . . . . . . . . . . . RNU2-64P . . . RNA, U2 small nuclear 64, pseudogene . . . . . . . . . . . RNU2-65P . . . RNA, U2 small nuclear 65, pseudogene . . . . . . . . . . . RNU2-66P . . . RNA, U2 small nuclear 66, pseudogene . . . . . . . . . . . RNU2-68P . . . RNA, U2 small nuclear 68, pseudogene . . . . . . . . . . . RNU2-69P . . . RNA, U2 small nuclear 69, pseudogene . . . . . . . . . . . RNU2-70P . . . RNA, U2 small nuclear 70, pseudogene . . . . . . . . . . . RNU2-71P . . . RNA, U2 small nuclear 71, pseudogene . . . . . . . . . . . RNU2-72P . . . RNA, U2 small nuclear 72, pseudogene . . . . . . . . . . . RNU3P1 . . . RNA, U3 small nucleolar pseudogene 1 . . . . . . . . . . . RNU3P2 . . . RNA, U3 small nucleolar pseudogene 2 . . . . . . . . . . . RNU3P3 . . . RNA, U3 small nucleolar pseudogene 3 . . . . . . . . . . . RNU3P4 . . . RNA, U3 small nucleolar pseudogene 4 . . . . . . . . . . . RNU4-1 . . . RNA, U4 small nuclear 1 . . . . . . . . . . . RNU4-2 . . . RNA, U4 small nuclear 2 . . . . . . . . . . . RNU4-3P . . . RNA, U4 small nuclear 3, pseudogene . . . . . . . . . . . RNU4-4P . . . RNA, U4 small nuclear 4, pseudogene . . . . . . . . . . . RNU4-5P . . . RNA, U4 small nuclear 5, pseudogene . . . . . . . . . . . RNU4-6P . . . RNA, U4 small nuclear 6, pseudogene . . . . . . . . . . . RNU4-7P . . . RNA, U4 small nuclear 7, pseudogene . . . . . . . . . . . RNU4-8P . . . RNA, U4 small nuclear 8, pseudogene . . . . . . . . . . . RNU4-9P . . . RNA, U4 small nuclear 9, pseudogene . . . . . . . . . . . RNU4-10P . . . RNA, U4 small nuclear 10, pseudogene . . . . . . . . . . . RNU4-11P . . . RNA, U4 small nuclear 11, pseudogene . . . . . . . . . . . RNU4-12P . . . RNA, U4 small nuclear 12, pseudogene . . . . . . . . . . . RNU4-13P . . . RNA, U4 small nuclear 13, pseudogene . . . . . . . . . . . RNU4-14P . . . RNA, U4 small nuclear 14, pseudogene . . . . . . . . . . . RNU4-15P . . . RNA, U4 small nuclear 15, pseudogene . . . . . . . . . . . RNU4-16P . . . RNA, U4 small nuclear 16, pseudogene . . . . . . . . . . . RNU4-17P . . . RNA, U4 small nuclear 17, pseudogene . . . . . . . . . . . RNU4-18P . . . RNA, U4 small nuclear 18, pseudogene . . . . . . . . . . . RNU4-20P . . . RNA, U4 small nuclear 20, pseudogene . . . . . . . . . . . RNU4-21P . . . RNA, U4 small nuclear 21, pseudogene . . . . . . . . . . . RNU4-22P . . . RNA, U4 small nuclear 22, pseudogene . . . . . . . . . . . RNU4-23P . . . RNA, U4 small nuclear 23, pseudogene . . . . . . . . . . . RNU4-24P . . . RNA, U4 small nuclear 24, pseudogene . . . . . . . . . . . RNU4-25P . . . RNA, U4 small nuclear 25, pseudogene . . . . . . . . . . . RNU4-26P . . . RNA, U4 small nuclear 26, pseudogene . . . . . . . . . . . RNU4-27P . . . RNA, U4 small nuclear 27, pseudogene . . . . . . . . . . . RNU4-28P . . . RNA, U4 small nuclear 28, pseudogene . . . . . . . . . . . RNU4-29P . . . RNA, U4 small nuclear 29, pseudogene . . . . . . . . . . . RNU4-30P . . . RNA, U4 small nuclear 30, pseudogene . . . . . . . . . . . RNU4-31P . . . RNA, U4 small nuclear 31, pseudogene . . . . . . . . . . . RNU4-32P . . . RNA, U4 small nuclear 32, pseudogene . . . . . . . . . . . RNU4-33P . . . RNA, U4 small nuclear 33, pseudogene . . . . . . . . . . . RNU4-34P . . . RNA, U4 small nuclear 34, pseudogene . . . . . . . . . . . RNU4-35P . . . RNA, U4 small nuclear 35, pseudogene . . . . . . . . . . . RNU4-36P . . . RNA, U4 small nuclear 36, pseudogene . . . . . . . . . . . RNU4-37P . . . RNA, U4 small nuclear 37, pseudogene . . . . . . . . . . . RNU4-38P . . . RNA, U4 small nuclear 38, pseudogene . . . . . . . . . . . RNU4-39P . . . RNA, U4 small nuclear 39, pseudogene . . . . . . . . . . . RNU4-40P . . . RNA, U4 small nuclear 40, pseudogene . . . . . . . . . . . RNU4-41P . . . RNA, U4 small nuclear 41, pseudogene . . . . . . . . . . . RNU4-42P . . . RNA, U4 small nuclear 42, pseudogene . . . . . . . . . . . RNU4-43P . . . RNA, U4 small nuclear 43, pseudogene . . . . . . . . . . . RNU4-44P . . . RNA, U4 small nuclear 44, pseudogene . . . . . . . . . . . RNU4-45P . . . RNA, U4 small nuclear 45, pseudogene . . . . . . . . . . . RNU4-46P . . . RNA, U4 small nuclear 46, pseudogene . . . . . . . . . . . RNU4-47P . . . RNA, U4 small nuclear 47, pseudogene . . . . . . . . . . . RNU4-48P . . . RNA, U4 small nuclear 48, pseudogene . . . . . . . . . . . RNU4-49P . . . RNA, U4 small nuclear 49, pseudogene . . . . . . . . . . . RNU4-50P . . . RNA, U4 small nuclear 50, pseudogene . . . . . . . . . . . RNU4-51P . . . RNA, U4 small nuclear 51, pseudogene . . . . . . . . . . . RNU4-52P . . . RNA, U4 small nuclear 52, pseudogene . . . . . . . . . . . RNU4-53P . . . RNA, U4 small nuclear 53, pseudogene . . . . . . . . . . . RNU4-54P . . . RNA, U4 small nuclear 54, pseudogene . . . . . . . . . . . RNU4-55P . . . RNA, U4 small nuclear 55, pseudogene . . . . . . . . . . . RNU4-56P . . . RNA, U4 small nuclear 56, pseudogene . . . . . . . . . . . RNU4-57P . . . RNA, U4 small nuclear 57, pseudogene . . . . . . . . . . . RNU4-58P . . . RNA, U4 small nuclear 58, pseudogene . . . . . . . . . . . RNU4-59P . . . RNA, U4 small nuclear 59, pseudogene . . . . . . . . . . . RNU4-60P . . . RNA, U4 small nuclear 60, pseudogene . . . . . . . . . . . RNU4-61P . . . RNA, U4 small nuclear 61, pseudogene . . . . . . . . . . . RNU4-62P . . . RNA, U4 small nuclear 62, pseudogene . . . . . . . . . . . RNU4-63P . . . RNA, U4 small nuclear 63, pseudogene . . . . . . . . . . . RNU4-64P . . . RNA, U4 small nuclear 64, pseudogene . . . . . . . . . . . RNU4-65P . . . RNA, U4 small nuclear 65, pseudogene . . . . . . . . . . . RNU4-66P . . . RNA, U4 small nuclear 66, pseudogene . . . . . . . . . . . RNU4-67P . . . RNA, U4 small nuclear 67, pseudogene . . . . . . . . . . . RNU4-68P . . . RNA, U4 small nuclear 68, pseudogene . . . . . . . . . . . RNU4-69P . . . RNA, U4 small nuclear 69, pseudogene . . . . . . . . . . . RNU4-70P . . . RNA, U4 small nuclear 70, pseudogene . . . . . . . . . . . RNU4-71P . . . RNA, U4 small nuclear 71, pseudogene . . . . . . . . . . . RNU4-72P . . . RNA, U4 small nuclear 72, pseudogene . . . . . . . . . . . RNU4-73P . . . RNA, U4 small nuclear 73, pseudogene . . . . . . . . . . . RNU4-74P . . . RNA, U4 small nuclear 74, pseudogene . . . . . . . . . . . RNU4-75P . . . RNA, U4 small nuclear 75, pseudogene . . . . . . . . . . . RNU4-76P . . . RNA, U4 small nuclear 76, pseudogene . . . . . . . . . . . RNU4-77P . . . RNA, U4 small nuclear 77, pseudogene . . . . . . . . . . . RNU4-78P . . . RNA, U4 small nuclear 78, pseudogene . . . . . . . . . . . RNU4-79P . . . RNA, U4 small nuclear 79, pseudogene . . . . . . . . . . . RNU4-80P . . . RNA, U4 small nuclear 80, pseudogene . . . . . . . . . . . RNU4-81P . . . RNA, U4 small nuclear 81, pseudogene . . . . . . . . . . . RNU4-82P . . . RNA, U4 small nuclear 82, pseudogene . . . . . . . . . . . RNU4-83P . . . RNA, U4 small nuclear 83, pseudogene . . . . . . . . . . . RNU4-84P . . . RNA, U4 small nuclear 84, pseudogene . . . . . . . . . . . RNU4-85P . . . RNA, U4 small nuclear 85, pseudogene . . . . . . . . . . . RNU4-86P . . . RNA, U4 small nuclear 86, pseudogene . . . . . . . . . . . RNU4-87P . . . RNA, U4 small nuclear 87, pseudogene . . . . . . . . . . . RNU4-88P . . . RNA, U4 small nuclear 88, pseudogene . . . . . . . . . . . RNU4-89P . . . RNA, U4 small nuclear 89, pseudogene . . . . . . . . . . . RNU4-90P . . . RNA, U4 small nuclear 90, pseudogene . . . . . . . . . . . RNU4-91P . . . RNA, U4 small nuclear 91, pseudogene . . . . . . . . . . . RNU4-92P . . . RNA, U4 small nuclear 92, pseudogene . . . . . . . . . . . RNU4ATAC . . . RNA, U4atac small nuclear (U12-dependent splicing) . . . . . . . . . . . RNU4ATAC2P . . . RNA, U4atac small nuclear 2, pseudogene . . . . . . . . . . . RNU4ATAC3P . . . RNA, U4atac small nuclear 3, pseudogene . . . . . . . . . . . RNU4ATAC4P . . . RNA, U4atac small nuclear 4, pseudogene . . . . . . . . . . . RNU4ATAC5P . . . RNA, U4atac small nuclear 5, pseudogene . . . . . . . . . . . RNU4ATAC6P . . . RNA, U4atac small nuclear 6, pseudogene . . . . . . . . . . . RNU4ATAC7P . . . RNA, U4atac small nuclear 7, pseudogene . . . . . . . . . . . RNU4ATAC8P . . . RNA, U4atac small nuclear 8, pseudogene . . . . . . . . . . . RNU4ATAC9P . . . RNA, U4atac small nuclear 9, pseudogene . . . . . . . . . . . RNU4ATAC10P . . . RNA, U4atac small nuclear 10, pseudogene . . . . . . . . . . . RNU4ATAC11P . . . RNA, U4atac small nuclear 11, pseudogene . . . . . . . . . . . RNU4ATAC12P . . . RNA, U4atac small nuclear 12, pseudogene . . . . . . . . . . . RNU4ATAC13P . . . RNA, U4atac small nuclear 13, pseudogene . . . . . . . . . . . RNU4ATAC14P . . . RNA, U4atac small nuclear 14, pseudogene . . . . . . . . . . . RNU4ATAC15P . . . RNA, U4atac small nuclear 15, pseudogene . . . . . . . . . . . RNU4ATAC16P . . . RNA, U4atac small nuclear 16, pseudogene . . . . . . . . . . . RNU4ATAC17P . . . RNA, U4atac small nuclear 17, pseudogene . . . . . . . . . . . RNU4ATAC18P . . . RNA, U4atac small nuclear 18, pseudogene . . . . . . . . . . . RNU5A-1 . . . RNA, U5A small nuclear 1 . . . . . . . . . . . RNU5A-2P . . . RNA, U5A small nuclear 2, pseudogene . . . . . . . . . . . RNU5A-3P . . . RNA, U5A small nuclear 3, pseudogene . . . . . . . . . . . RNU5A-4P . . . RNA, U5A small nuclear 4, pseudogene . . . . . . . . . . . RNU5A-5P . . . RNA, U5A small nuclear 5, pseudogene . . . . . . . . . . . RNU5A-6P . . . RNA, U5A small nuclear 6, pseudogene . . . . . . . . . . . RNU5A-7P . . . RNA, U5A small nuclear 7, pseudogene . . . . . . . . . . . RNU5A-8P . . . RNA, U5A small nuclear 8, pseudogene . . . . . . . . . . . RNU5B-1 . . . RNA, U5B small nuclear 1 . . . . . . . . . . . RNU5B-2P . . . RNA, U5B small nuclear 2, pseudogene . . . . . . . . . . . RNU5B-3P . . . RNA, U5B small nuclear 3, pseudogene . . . . . . . . . . . RNU5B-4P . . . RNA, U5B small nuclear 4, pseudogene . . . . . . . . . . . RNU5B-5P . . . RNA, U5B small nuclear 5, pseudogene . . . . . . . . . . . RNU5B-6P . . . RNA, U5B small nuclear 6, pseudogene . . . . . . . . . . . RNU5D-1 . . . RNA, U5D small nuclear 1 . . . . . . . . . . . RNU5D-2P . . . RNA, U5D small nuclear 2, pseudogene . . . . . . . . . . . RNU5E-1 . . . RNA, U5E small nuclear 1 . . . . . . . . . . . RNU5E-2P . . . RNA, U5E small nuclear 2, pseudogene . . . . . . . . . . . RNU5E-3P . . . RNA, U5E small nuclear 3, pseudogene . . . . . . . . . . . RNU5E-4P . . . RNA, U5E small nuclear 4, pseudogene . . . . . . . . . . . RNU5E-5P . . . RNA, U5E small nuclear 5, pseudogene . . . . . . . . . . . RNU5E-6P . . . RNA, U5E small nuclear 6, pseudogene . . . . . . . . . . . RNU5E-7P . . . RNA, U5E small nuclear 7, pseudogene . . . . . . . . . . . RNU5E-8P . . . RNA, U5E small nuclear 8, pseudogene . . . . . . . . . . . RNU5E-9P . . . RNA, U5E small nuclear 9, pseudogene . . . . . . . . . . . RNU5E-10P . . . RNA, U5E small nuclear 10, pseudogene . . . . . . . . . . . RNU5F-1 . . . RNA, U5F small nuclear 1 . . . . . . . . . . . RNU5F-2P . . . RNA, U5F small nuclear 2, pseudogene . . . . . . . . . . . RNU5F-3P . . . RNA, U5F small nuclear 3, pseudogene . . . . . . . . . . . RNU5F-4P . . . RNA, U5F small nuclear 4, pseudogene . . . . . . . . . . . RNU5F-5P . . . RNA, U5F small nuclear 5, pseudogene . . . . . . . . . . . RNU5F-6P . . . RNA, U5F small nuclear 6, pseudogene . . . . . . . . . . . RNU5F-7P . . . RNA, U5F small nuclear 7, pseudogene . . . . . . . . . . . RNU5F-8P . . . RNA, U5F small nuclear 8, pseudogene . . . . . . . . . . . RNU6-1 . . . RNA, U6 small nuclear 1 . . . . . . . . . . . RNU6-2 . . . RNA, U6 small nuclear 2 . . . . . . . . . . . RNU6-3P . . . RNA, U6 small nuclear 3, pseudogene . . . . . . . . . . . RNU6-4P . . . RNA, U6 small nuclear 4, pseudogene . . . . . . . . . . . RNU6-5P . . . RNA, U6 small nuclear 5, pseudogene . . . . . . . . . . . RNU6-6P . . . RNA, U6 small nuclear 6, pseudogene . . . . . . . . . . . RNU6-7 . . . RNA, U6 small nuclear 7 . . . . . . . . . . . RNU6-8 . . . RNA, U6 small nuclear 8 . . . . . . . . . . . RNU6-9 . . . RNA, U6 small nuclear 9 . . . . . . . . . . . RNU6-10P . . . RNA, U6 small nuclear 10, pseudogene . . . . . . . . . . . RNU6-11P . . . RNA, U6 small nuclear 11, pseudogene . . . . . . . . . . . RNU6-12P . . . RNA, U6 small nuclear 12, pseudogene . . . . . . . . . . . RNU6-13P . . . RNA, U6 small nuclear 13, pseudogene . . . . . . . . . . . RNU6-14P . . . RNA, U6 small nuclear 14, pseudogene . . . . . . . . . . . RNU6-15P . . . RNA, U6 small nuclear 15, pseudogene . . . . . . . . . . . RNU6-16P . . . RNA, U6 small nuclear 16, pseudogene . . . . . . . . . . . RNU6-17P . . . RNA, U6 small nuclear 17, pseudogene . . . . . . . . . . . RNU6-18P . . . RNA, U6 small nuclear 18, pseudogene . . . . . . . . . . . RNU6-19P . . . RNA, U6 small nuclear 19, pseudogene . . . . . . . . . . . RNU6-20P . . . RNA, U6 small nuclear 20, pseudogene . . . . . . . . . . . RNU6-21P . . . RNA, U6 small nuclear 21, pseudogene . . . . . . . . . . . RNU6-22P . . . RNA, U6 small nuclear 22, pseudogene . . . . . . . . . . . RNU6-23P . . . RNA, U6 small nuclear 23, pseudogene . . . . . . . . . . . RNU6-24P . . . RNA, U6 small nuclear 24, pseudogene . . . . . . . . . . . RNU6-25P . . . RNA, U6 small nuclear 25, pseudogene . . . . . . . . . . . RNU6-26P . . . RNA, U6 small nuclear 26, pseudogene . . . . . . . . . . . RNU6-27P . . . RNA, U6 small nuclear 27, pseudogene . . . . . . . . . . . RNU6-28P . . . RNA, U6 small nuclear 28, pseudogene . . . . . . . . . . . RNU6-29P . . . RNA, U6 small nuclear 29, pseudogene . . . . . . . . . . . RNU6-30P . . . RNA, U6 small nuclear 30, pseudogene . . . . . . . . . . . RNU6-31P . . . RNA, U6 small nuclear 31, pseudogene . . . . . . . . . . . RNU6-32P . . . RNA, U6 small nuclear 32, pseudogene . . . . . . . . . . . RNU6-33P . . . RNA, U6 small nuclear 33, pseudogene . . . . . . . . . . . RNU6-34P . . . RNA, U6 small nuclear 34, pseudogene . . . . . . . . . . . RNU6-35P . . . RNA, U6 small nuclear 35, pseudogene . . . . . . . . . . . RNU6-36P . . . RNA, U6 small nuclear 36, pseudogene . . . . . . . . . . . RNU6-37P . . . RNA, U6 small nuclear 37, pseudogene . . . . . . . . . . . RNU6-38P . . . RNA, U6 small nuclear 38, pseudogene . . . . . . . . . . . RNU6-39P . . . RNA, U6 small nuclear 39, pseudogene . . . . . . . . . . . RNU6-40P . . . RNA, U6 small nuclear 40, pseudogene . . . . . . . . . . . RNU6-41P . . . RNA, U6 small nuclear 41, pseudogene . . . . . . . . . . . RNU6-42P . . . RNA, U6 small nuclear 42, pseudogene . . . . . . . . . . . RNU6-43P . . . RNA, U6 small nuclear 43, pseudogene . . . . . . . . . . . RNU6-44P . . . RNA, U6 small nuclear 44, pseudogene . . . . . . . . . . . RNU6-45P . . . RNA, U6 small nuclear 45, pseudogene . . . . . . . . . . . RNU6-46P . . . RNA, U6 small nuclear 46, pseudogene . . . . . . . . . . . RNU6-47P . . . RNA, U6 small nuclear 47, pseudogene . . . . . . . . . . . RNU6-48P . . . RNA, U6 small nuclear 48, pseudogene . . . . . . . . . . . RNU6-49P . . . RNA, U6 small nuclear 49, pseudogene . . . . . . . . . . . RNU6-50P . . . RNA, U6 small nuclear 50, pseudogene . . . . . . . . . . . RNU6-52P . . . RNA, U6 small nuclear 52, pseudogene . . . . . . . . . . . RNU6-53P . . . RNA, U6 small nuclear 53, pseudogene . . . . . . . . . . . RNU6-54P . . . RNA, U6 small nuclear 54, pseudogene . . . . . . . . . . . RNU6-55P . . . RNA, U6 small nuclear 55, pseudogene . . . . . . . . . . . RNU6-56P . . . RNA, U6 small nuclear 56, pseudogene . . . . . . . . . . . RNU6-57P . . . RNA, U6 small nuclear 57, pseudogene . . . . . . . . . . . RNU6-58P . . . RNA, U6 small nuclear 58, pseudogene . . . . . . . . . . . RNU6-59P . . . RNA, U6 small nuclear 59, pseudogene . . . . . . . . . . . RNU6-60P . . . RNA, U6 small nuclear 60, pseudogene . . . . . . . . . . . RNU6-61P . . . RNA, U6 small nuclear 61, pseudogene . . . . . . . . . . . RNU6-62P . . . RNA, U6 small nuclear 62, pseudogene . . . . . . . . . . . RNU6-63P . . . RNA, U6 small nuclear 63, pseudogene . . . . . . . . . . . RNU6-64P . . . RNA, U6 small nuclear 64, pseudogene . . . . . . . . . . . RNU6-65P . . . RNA, U6 small nuclear 65, pseudogene . . . . . . . . . . . RNU6-66P . . . RNA, U6 small nuclear 66, pseudogene . . . . . . . . . . . RNU6-67P . . . RNA, U6 small nuclear 67, pseudogene . . . . . . . . . . . RNU6-68P . . . RNA, U6 small nuclear 68, pseudogene . . . . . . . . . . . RNU6-69P . . . RNA, U6 small nuclear 69, pseudogene . . . . . . . . . . . RNU6-70P . . . RNA, U6 small nuclear 70, pseudogene . . . . . . . . . . . RNU6-71P . . . RNA, U6 small nuclear 71, pseudogene . . . . . . . . . . . RNU6-72P . . . RNA, U6 small nuclear 72, pseudogene . . . . . . . . . . . RNU6-73P . . . RNA, U6 small nuclear 73, pseudogene . . . . . . . . . . . RNU6-74P . . . RNA, U6 small nuclear 74, pseudogene . . . . . . . . . . . RNU6-75P . . . RNA, U6 small nuclear 75, pseudogene . . . . . . . . . . . RNU6-76P . . . RNA, U6 small nuclear 76, pseudogene . . . . . . . . . . . RNU6-77P . . . RNA, U6 small nuclear 77, pseudogene . . . . . . . . . . . RNU6-78P . . . RNA, U6 small nuclear 78, pseudogene . . . . . . . . . . . RNU6-79P . . . RNA, U6 small nuclear 79, pseudogene . . . . . . . . . . . RNU6-80P . . . RNA, U6 small nuclear 80, pseudogene . . . . . . . . . . . RNU6-81P . . . RNA, U6 small nuclear 81, pseudogene . . . . . . . . . . . RNU6-82P . . . RNA, U6 small nuclear 82, pseudogene . . . . . . . . . . . RNU6-83P . . . RNA, U6 small nuclear 83, pseudogene . . . . . . . . . . . RNU6-84P . . . RNA, U6 small nuclear 84, pseudogene . . . . . . . . . . . RNU6-85P . . . RNA, U6 small nuclear 85, pseudogene . . . . . . . . . . . RNU6-86P . . . RNA, U6 small nuclear 86, pseudogene . . . . . . . . . . . RNU6-87P . . . RNA, U6 small nuclear 87, pseudogene . . . . . . . . . . . RNU6-88P . . . RNA, U6 small nuclear 88, pseudogene . . . . . . . . . . . RNU6-89P . . . RNA, U6 small nuclear 89, pseudogene . . . . . . . . . . . RNU6-90P . . . RNA, U6 small nuclear 90, pseudogene . . . . . . . . . . . RNU6-91P . . . RNA, U6 small nuclear 91, pseudogene . . . . . . . . . . . RNU6-92P . . . RNA, U6 small nuclear 92, pseudogene . . . . . . . . . . . RNU6-94P . . . RNA, U6 small nuclear 94, pseudogene . . . . . . . . . . . RNU6-95P . . . RNA, U6 small nuclear 95, pseudogene . . . . . . . . . . . RNU6-96P . . . RNA, U6 small nuclear 96, pseudogene . . . . . . . . . . . RNU6-97P . . . RNA, U6 small nuclear 97, pseudogene . . . . . . . . . . . RNU6-98P . . . RNA, U6 small nuclear 98, pseudogene . . . . . . . . . . . RNU6-99P . . . RNA, U6 small nuclear 99, pseudogene . . . . . . . . . . . RNU6-100P . . . RNA, U6 small nuclear 100, pseudogene . . . . . . . . . . . RNU6-101P . . . RNA, U6 small nuclear 101, pseudogene . . . . . . . . . . . RNU6-102P . . . RNA, U6 small nuclear 102, pseudogene . . . . . . . . . . . RNU6-103P . . . RNA, U6 small nuclear 103, pseudogene . . . . . . . . . . . RNU6-104P . . . RNA, U6 small nuclear 104, pseudogene . . . . . . . . . . . RNU6-105P . . . RNA, U6 small nuclear 105, pseudogene . . . . . . . . . . . RNU6-106P . . . RNA, U6 small nuclear 106, pseudogene . . . . . . . . . . . RNU6-107P . . . RNA, U6 small nuclear 107, pseudogene . . . . . . . . . . . RNU6-108P . . . RNA, U6 small nuclear 108, pseudogene . . . . . . . . . . . RNU6-109P . . . RNA, U6 small nuclear 109, pseudogene . . . . . . . . . . . RNU6-110P . . . RNA, U6 small nuclear 110, pseudogene . . . . . . . . . . . RNU6-111P . . . RNA, U6 small nuclear 111, pseudogene . . . . . . . . . . . RNU6-112P . . . RNA, U6 small nuclear 112, pseudogene . . . . . . . . . . . RNU6-113P . . . RNA, U6 small nuclear 113, pseudogene . . . . . . . . . . . RNU6-114P . . . RNA, U6 small nuclear 114, pseudogene . . . . . . . . . . . RNU6-115P . . . RNA, U6 small nuclear 115, pseudogene . . . . . . . . . . . RNU6-116P . . . RNA, U6 small nuclear 116, pseudogene . . . . . . . . . . . RNU6-117P . . . RNA, U6 small nuclear 117, pseudogene . . . . . . . . . . . RNU6-118P . . . RNA, U6 small nuclear 118, pseudogene . . . . . . . . . . . RNU6-119P . . . RNA, U6 small nuclear 119, pseudogene . . . . . . . . . . . RNU6-120P . . . RNA, U6 small nuclear 120, pseudogene . . . . . . . . . . . RNU6-121P . . . RNA, U6 small nuclear 121, pseudogene . . . . . . . . . . . RNU6-122P . . . RNA, U6 small nuclear 122, pseudogene . . . . . . . . . . . RNU6-123P . . . RNA, U6 small nuclear 123, pseudogene . . . . . . . . . . . RNU6-124P . . . RNA, U6 small nuclear 124, pseudogene . . . . . . . . . . . RNU6-125P . . . RNA, U6 small nuclear 125, pseudogene . . . . . . . . . . . RNU6-126P . . . RNA, U6 small nuclear 126, pseudogene . . . . . . . . . . . RNU6-127P . . . RNA, U6 small nuclear 127, pseudogene . . . . . . . . . . . RNU6-128P . . . RNA, U6 small nuclear 128, pseudogene . . . . . . . . . . . RNU6-129P . . . RNA, U6 small nuclear 129, pseudogene . . . . . . . . . . . RNU6-130P . . . RNA, U6 small nuclear 130, pseudogene . . . . . . . . . . . RNU6-131P . . . RNA, U6 small nuclear 131, pseudogene . . . . . . . . . . . RNU6-132P . . . RNA, U6 small nuclear 132, pseudogene . . . . . . . . . . . RNU6-133P . . . RNA, U6 small nuclear 133, pseudogene . . . . . . . . . . . RNU6-135P . . . RNA, U6 small nuclear 135, pseudogene . . . . . . . . . . . RNU6-136P . . . RNA, U6 small nuclear 136, pseudogene . . . . . . . . . . . RNU6-137P . . . RNA, U6 small nuclear 137, pseudogene . . . . . . . . . . . RNU6-138P . . . RNA, U6 small nuclear 138, pseudogene . . . . . . . . . . . RNU6-139P . . . RNA, U6 small nuclear 139, pseudogene . . . . . . . . . . . RNU6-140P . . . RNA, U6 small nuclear 140, pseudogene . . . . . . . . . . . RNU6-141P . . . RNA, U6 small nuclear 141, pseudogene . . . . . . . . . . . RNU6-142P . . . RNA, U6 small nuclear 142, pseudogene . . . . . . . . . . . RNU6-143P . . . RNA, U6 small nuclear 143, pseudogene . . . . . . . . . . . RNU6-144P . . . RNA, U6 small nuclear 144, pseudogene . . . . . . . . . . . RNU6-145P . . . RNA, U6 small nuclear 145, pseudogene . . . . . . . . . . . RNU6-146P . . . RNA, U6 small nuclear 146, pseudogene . . . . . . . . . . . RNU6-147P . . . RNA, U6 small nuclear 147, pseudogene . . . . . . . . . . . RNU6-148P . . . RNA, U6 small nuclear 148, pseudogene . . . . . . . . . . . RNU6-150P . . . RNA, U6 small nuclear 150, pseudogene . . . . . . . . . . . RNU6-151P . . . RNA, U6 small nuclear 151, pseudogene . . . . . . . . . . . RNU6-152P . . . RNA, U6 small nuclear 152, pseudogene . . . . . . . . . . . RNU6-153P . . . RNA, U6 small nuclear 153, pseudogene . . . . . . . . . . . RNU6-154P . . . RNA, U6 small nuclear 154, pseudogene . . . . . . . . . . . RNU6-155P . . . RNA, U6 small nuclear 155, pseudogene . . . . . . . . . . . RNU6-156P . . . RNA, U6 small nuclear 156, pseudogene . . . . . . . . . . . RNU6-157P . . . RNA, U6 small nuclear 157, pseudogene . . . . . . . . . . . RNU6-158P . . . RNA, U6 small nuclear 158, pseudogene . . . . . . . . . . . RNU6-159P . . . RNA, U6 small nuclear 159, pseudogene . . . . . . . . . . . RNU6-160P . . . RNA, U6 small nuclear 160, pseudogene . . . . . . . . . . . RNU6-161P . . . RNA, U6 small nuclear 161, pseudogene . . . . . . . . . . . RNU6-162P . . . RNA, U6 small nuclear 162, pseudogene . . . . . . . . . . . RNU6-163P . . . RNA, U6 small nuclear 163, pseudogene . . . . . . . . . . . RNU6-164P . . . RNA, U6 small nuclear 164, pseudogene . . . . . . . . . . . RNU6-165P . . . RNA, U6 small nuclear 165, pseudogene . . . . . . . . . . . RNU6-166P . . . RNA, U6 small nuclear 166, pseudogene . . . . . . . . . . . RNU6-167P . . . RNA, U6 small nuclear 167, pseudogene . . . . . . . . . . . RNU6-168P . . . RNA, U6 small nuclear 168, pseudogene . . . . . . . . . . . RNU6-169P . . . RNA, U6 small nuclear 169, pseudogene . . . . . . . . . . . RNU6-170P . . . RNA, U6 small nuclear 170, pseudogene . . . . . . . . . . . RNU6-171P . . . RNA, U6 small nuclear 171, pseudogene . . . . . . . . . . . RNU6-172P . . . RNA, U6 small nuclear 172, pseudogene . . . . . . . . . . . RNU6-173P . . . RNA, U6 small nuclear 173, pseudogene . . . . . . . . . . . RNU6-174P . . . RNA, U6 small nuclear 174, pseudogene . . . . . . . . . . . RNU6-175P . . . RNA, U6 small nuclear 175, pseudogene . . . . . . . . . . . RNU6-176P . . . RNA, U6 small nuclear 176, pseudogene . . . . . . . . . . . RNU6-177P . . . RNA, U6 small nuclear 177, pseudogene . . . . . . . . . . . RNU6-178P . . . RNA, U6 small nuclear 178, pseudogene . . . . . . . . . . . RNU6-179P . . . RNA, U6 small nuclear 179, pseudogene . . . . . . . . . . . RNU6-180P . . . RNA, U6 small nuclear 180, pseudogene . . . . . . . . . . . RNU6-181P . . . RNA, U6 small nuclear 181, pseudogene . . . . . . . . . . . RNU6-182P . . . RNA, U6 small nuclear 182, pseudogene . . . . . . . . . . . RNU6-183P . . . RNA, U6 small nuclear 183, pseudogene . . . . . . . . . . . RNU6-184P . . . RNA, U6 small nuclear 184, pseudogene . . . . . . . . . . . RNU6-185P . . . RNA, U6 small nuclear 185, pseudogene . . . . . . . . . . . RNU6-187P . . . RNA, U6 small nuclear 187, pseudogene . . . . . . . . . . . RNU6-188P . . . RNA, U6 small nuclear 188, pseudogene . . . . . . . . . . . RNU6-189P . . . RNA, U6 small nuclear 189, pseudogene . . . . . . . . . . . RNU6-190P . . . RNA, U6 small nuclear 190, pseudogene . . . . . . . . . . . RNU6-191P . . . RNA, U6 small nuclear 191, pseudogene . . . . . . . . . . . RNU6-192P . . . RNA, U6 small nuclear 192, pseudogene . . . . . . . . . . . RNU6-193P . . . RNA, U6 small nuclear 193, pseudogene . . . . . . . . . . . RNU6-194P . . . RNA, U6 small nuclear 194, pseudogene . . . . . . . . . . . RNU6-195P . . . RNA, U6 small nuclear 195, pseudogene . . . . . . . . . . . RNU6-196P . . . RNA, U6 small nuclear 196, pseudogene . . . . . . . . . . . RNU6-197P . . . RNA, U6 small nuclear 197, pseudogene . . . . . . . . . . . RNU6-198P . . . RNA, U6 small nuclear 198, pseudogene . . . . . . . . . . . RNU6-199P . . . RNA, U6 small nuclear 199, pseudogene . . . . . . . . . . . RNU6-200P . . . RNA, U6 small nuclear 200, pseudogene . . . . . . . . . . . RNU6-201P . . . RNA, U6 small nuclear 201, pseudogene . . . . . . . . . . . RNU6-202P . . . RNA, U6 small nuclear 202, pseudogene . . . . . . . . . . . RNU6-203P . . . RNA, U6 small nuclear 203, pseudogene . . . . . . . . . . . RNU6-204P . . . RNA, U6 small nuclear 204, pseudogene . . . . . . . . . . . RNU6-205P . . . RNA, U6 small nuclear 205, pseudogene . . . . . . . . . . . RNU6-206P . . . RNA, U6 small nuclear 206, pseudogene . . . . . . . . . . . RNU6-207P . . . RNA, U6 small nuclear 207, pseudogene . . . . . . . . . . . RNU6-208P . . . RNA, U6 small nuclear 208, pseudogene . . . . . . . . . . . RNU6-209P . . . RNA, U6 small nuclear 209, pseudogene . . . . . . . . . . . RNU6-210P . . . RNA, U6 small nuclear 210, pseudogene . . . . . . . . . . . RNU6-211P . . . RNA, U6 small nuclear 211, pseudogene . . . . . . . . . . . RNU6-212P . . . RNA, U6 small nuclear 212, pseudogene . . . . . . . . . . . RNU6-213P . . . RNA, U6 small nuclear 213, pseudogene . . . . . . . . . . . RNU6-214P . . . RNA, U6 small nuclear 214, pseudogene . . . . . . . . . . . RNU6-215P . . . RNA, U6 small nuclear 215, pseudogene . . . . . . . . . . . RNU6-216P . . . RNA, U6 small nuclear 216, pseudogene . . . . . . . . . . . RNU6-217P . . . RNA, U6 small nuclear 217, pseudogene . . . . . . . . . . . RNU6-218P . . . RNA, U6 small nuclear 218, pseudogene . . . . . . . . . . . RNU6-219P . . . RNA, U6 small nuclear 219, pseudogene . . . . . . . . . . . RNU6-220P . . . RNA, U6 small nuclear 220, pseudogene . . . . . . . . . . . RNU6-221P . . . RNA, U6 small nuclear 221, pseudogene . . . . . . . . . . . RNU6-222P . . . RNA, U6 small nuclear 222, pseudogene . . . . . . . . . . . RNU6-223P . . . RNA, U6 small nuclear 223, pseudogene . . . . . . . . . . . RNU6-224P . . . RNA, U6 small nuclear 224, pseudogene . . . . . . . . . . . RNU6-225P . . . RNA, U6 small nuclear 225, pseudogene . . . . . . . . . . . RNU6-226P . . . RNA, U6 small nuclear 226, pseudogene . . . . . . . . . . . RNU6-227P . . . RNA, U6 small nuclear 227, pseudogene . . . . . . . . . . . RNU6-228P . . . RNA, U6 small nuclear 228, pseudogene . . . . . . . . . . . RNU6-229P . . . RNA, U6 small nuclear 229, pseudogene . . . . . . . . . . . RNU6-230P . . . RNA, U6 small nuclear 230, pseudogene . . . . . . . . . . . RNU6-231P . . . RNA, U6 small nuclear 231, pseudogene . . . . . . . . . . . RNU6-232P . . . RNA, U6 small nuclear 232, pseudogene . . . . . . . . . . . RNU6-233P . . . RNA, U6 small nuclear 233, pseudogene . . . . . . . . . . . RNU6-234P . . . RNA, U6 small nuclear 234, pseudogene . . . . . . . . . . . RNU6-235P . . . RNA, U6 small nuclear 235, pseudogene . . . . . . . . . . . RNU6-236P . . . RNA, U6 small nuclear 236, pseudogene . . . . . . . . . . . RNU6-237P . . . RNA, U6 small nuclear 237, pseudogene . . . . . . . . . . . RNU6-238P . . . RNA, U6 small nuclear 238, pseudogene . . . . . . . . . . . RNU6-239P . . . RNA, U6 small nuclear 239, pseudogene . . . . . . . . . . . RNU6-240P . . . RNA, U6 small nuclear 240, pseudogene . . . . . . . . . . . RNU6-241P . . . RNA, U6 small nuclear 241, pseudogene . . . . . . . . . . . RNU6-242P . . . RNA, U6 small nuclear 242, pseudogene . . . . . . . . . . . RNU6-243P . . . RNA, U6 small nuclear 243, pseudogene . . . . . . . . . . . RNU6-244P . . . RNA, U6 small nuclear 244, pseudogene . . . . . . . . . . . RNU6-245P . . . RNA, U6 small nuclear 245, pseudogene . . . . . . . . . . . RNU6-246P . . . RNA, U6 small nuclear 246, pseudogene . . . . . . . . . . . RNU6-247P . . . RNA, U6 small nuclear 247, pseudogene . . . . . . . . . . . RNU6-248P . . . RNA, U6 small nuclear 248, pseudogene . . . . . . . . . . . RNU6-249P . . . RNA, U6 small nuclear 249, pseudogene . . . . . . . . . . . RNU6-250P . . . RNA, U6 small nuclear 250, pseudogene . . . . . . . . . . . RNU6-251P . . . RNA, U6 small nuclear 251, pseudogene . . . . . . . . . . . RNU6-252P . . . RNA, U6 small nuclear 252, pseudogene . . . . . . . . . . . RNU6-253P . . . RNA, U6 small nuclear 253, pseudogene . . . . . . . . . . . RNU6-254P . . . RNA, U6 small nuclear 254, pseudogene . . . . . . . . . . . RNU6-255P . . . RNA, U6 small nuclear 255, pseudogene . . . . . . . . . . . RNU6-256P . . . RNA, U6 small nuclear 256, pseudogene . . . . . . . . . . . RNU6-257P . . . RNA, U6 small nuclear 257, pseudogene . . . . . . . . . . . RNU6-258P . . . RNA, U6 small nuclear 258, pseudogene . . . . . . . . . . . RNU6-259P . . . RNA, U6 small nuclear 259, pseudogene . . . . . . . . . . . RNU6-260P . . . RNA, U6 small nuclear 260, pseudogene . . . . . . . . . . . RNU6-261P . . . RNA, U6 small nuclear 261, pseudogene . . . . . . . . . . . RNU6-262P . . . RNA, U6 small nuclear 262, pseudogene . . . . . . . . . . . RNU6-263P . . . RNA, U6 small nuclear 263, pseudogene . . . . . . . . . . . RNU6-264P . . . RNA, U6 small nuclear 264, pseudogene . . . . . . . . . . . RNU6-266P . . . RNA, U6 small nuclear 266, pseudogene . . . . . . . . . . . RNU6-267P . . . RNA, U6 small nuclear 267, pseudogene . . . . . . . . . . . RNU6-268P . . . RNA, U6 small nuclear 268, pseudogene . . . . . . . . . . . RNU6-269P . . . RNA, U6 small nuclear 269, pseudogene . . . . . . . . . . . RNU6-270P . . . RNA, U6 small nuclear 270, pseudogene . . . . . . . . . . . RNU6-271P . . . RNA, U6 small nuclear 271, pseudogene . . . . . . . . . . . RNU6-272P . . . RNA, U6 small nuclear 272, pseudogene . . . . . . . . . . . RNU6-273P . . . RNA, U6 small nuclear 273, pseudogene . . . . . . . . . . . RNU6-274P . . . RNA, U6 small nuclear 274, pseudogene . . . . . . . . . . . RNU6-275P . . . RNA, U6 small nuclear 275, pseudogene . . . . . . . . . . . RNU6-276P . . . RNA, U6 small nuclear 276, pseudogene . . . . . . . . . . . RNU6-277P . . . RNA, U6 small nuclear 277, pseudogene . . . . . . . . . . . RNU6-278P . . . RNA, U6 small nuclear 278, pseudogene . . . . . . . . . . . RNU6-279P . . . RNA, U6 small nuclear 279, pseudogene . . . . . . . . . . . RNU6-280P . . . RNA, U6 small nuclear 280, pseudogene . . . . . . . . . . . RNU6-281P . . . RNA, U6 small nuclear 281, pseudogene . . . . . . . . . . . RNU6-282P . . . RNA, U6 small nuclear 282, pseudogene . . . . . . . . . . . RNU6-283P . . . RNA, U6 small nuclear 283, pseudogene . . . . . . . . . . . RNU6-284P . . . RNA, U6 small nuclear 284, pseudogene . . . . . . . . . . . RNU6-285P . . . RNA, U6 small nuclear 285, pseudogene . . . . . . . . . . . RNU6-286P . . . RNA, U6 small nuclear 286, pseudogene . . . . . . . . . . . RNU6-287P . . . RNA, U6 small nuclear 287, pseudogene . . . . . . . . . . . RNU6-288P . . . RNA, U6 small nuclear 288, pseudogene . . . . . . . . . . . RNU6-289P . . . RNA, U6 small nuclear 289, pseudogene . . . . . . . . . . . RNU6-290P . . . RNA, U6 small nuclear 290, pseudogene . . . . . . . . . . . RNU6-291P . . . RNA, U6 small nuclear 291, pseudogene . . . . . . . . . . . RNU6-293P . . . RNA, U6 small nuclear 293, pseudogene . . . . . . . . . . . RNU6-294P . . . RNA, U6 small nuclear 294, pseudogene . . . . . . . . . . . RNU6-295P . . . RNA, U6 small nuclear 295, pseudogene . . . . . . . . . . . RNU6-296P . . . RNA, U6 small nuclear 296, pseudogene . . . . . . . . . . . RNU6-297P . . . RNA, U6 small nuclear 297, pseudogene . . . . . . . . . . . RNU6-298P . . . RNA, U6 small nuclear 298, pseudogene . . . . . . . . . . . RNU6-299P . . . RNA, U6 small nuclear 299, pseudogene . . . . . . . . . . . RNU6-300P . . . RNA, U6 small nuclear 300, pseudogene . . . . . . . . . . . RNU6-301P . . . RNA, U6 small nuclear 301, pseudogene . . . . . . . . . . . RNU6-302P . . . RNA, U6 small nuclear 302, pseudogene . . . . . . . . . . . RNU6-303P . . . RNA, U6 small nuclear 303, pseudogene . . . . . . . . . . . RNU6-304P . . . RNA, U6 small nuclear 304, pseudogene . . . . . . . . . . . RNU6-306P . . . RNA, U6 small nuclear 306, pseudogene . . . . . . . . . . . RNU6-307P . . . RNA, U6 small nuclear 307, pseudogene . . . . . . . . . . . RNU6-308P . . . RNA, U6 small nuclear 308, pseudogene . . . . . . . . . . . RNU6-309P . . . RNA, U6 small nuclear 309, pseudogene . . . . . . . . . . . RNU6-310P . . . RNA, U6 small nuclear 310, pseudogene . . . . . . . . . . . RNU6-311P . . . RNA, U6 small nuclear 311, pseudogene . . . . . . . . . . . RNU6-312P . . . RNA, U6 small nuclear 312, pseudogene . . . . . . . . . . . RNU6-313P . . . RNA, U6 small nuclear 313, pseudogene . . . . . . . . . . . RNU6-314P . . . RNA, U6 small nuclear 314, pseudogene . . . . . . . . . . . RNU6-315P . . . RNA, U6 small nuclear 315, pseudogene . . . . . . . . . . . RNU6-316P . . . RNA, U6 small nuclear 316, pseudogene . . . . . . . . . . . RNU6-317P . . . RNA, U6 small nuclear 317, pseudogene . . . . . . . . . . . RNU6-318P . . . RNA, U6 small nuclear 318, pseudogene . . . . . . . . . . . RNU6-319P . . . RNA, U6 small nuclear 319, pseudogene . . . . . . . . . . . RNU6-320P . . . RNA, U6 small nuclear 320, pseudogene . . . . . . . . . . . RNU6-321P . . . RNA, U6 small nuclear 321, pseudogene . . . . . . . . . . . RNU6-322P . . . RNA, U6 small nuclear 322, pseudogene . . . . . . . . . . . RNU6-323P . . . RNA, U6 small nuclear 323, pseudogene . . . . . . . . . . . RNU6-324P . . . RNA, U6 small nuclear 324, pseudogene . . . . . . . . . . . RNU6-325P . . . RNA, U6 small nuclear 325, pseudogene . . . . . . . . . . . RNU6-326P . . . RNA, U6 small nuclear 326, pseudogene . . . . . . . . . . . RNU6-327P . . . RNA, U6 small nuclear 327, pseudogene . . . . . . . . . . . RNU6-328P . . . RNA, U6 small nuclear 328, pseudogene . . . . . . . . . . . RNU6-329P . . . RNA, U6 small nuclear 329, pseudogene . . . . . . . . . . . RNU6-330P . . . RNA, U6 small nuclear 330, pseudogene . . . . . . . . . . . RNU6-331P . . . RNA, U6 small nuclear 331, pseudogene . . . . . . . . . . . RNU6-332P . . . RNA, U6 small nuclear 332, pseudogene . . . . . . . . . . . RNU6-333P . . . RNA, U6 small nuclear 333, pseudogene . . . . . . . . . . . RNU6-334P . . . RNA, U6 small nuclear 334, pseudogene . . . . . . . . . . . RNU6-335P . . . RNA, U6 small nuclear 335, pseudogene . . . . . . . . . . . RNU6-336P . . . RNA, U6 small nuclear 336, pseudogene . . . . . . . . . . . RNU6-337P . . . RNA, U6 small nuclear 337, pseudogene . . . . . . . . . . . RNU6-338P . . . RNA, U6 small nuclear 338, pseudogene . . . . . . . . . . . RNU6-339P . . . RNA, U6 small nuclear 339, pseudogene . . . . . . . . . . . RNU6-340P . . . RNA, U6 small nuclear 340, pseudogene . . . . . . . . . . . RNU6-341P . . . RNA, U6 small nuclear 341, pseudogene . . . . . . . . . . . RNU6-342P . . . RNA, U6 small nuclear 342, pseudogene . . . . . . . . . . . RNU6-343P . . . RNA, U6 small nuclear 343, pseudogene . . . . . . . . . . . RNU6-344P . . . RNA, U6 small nuclear 344, pseudogene . . . . . . . . . . . RNU6-345P . . . RNA, U6 small nuclear 345, pseudogene . . . . . . . . . . . RNU6-346P . . . RNA, U6 small nuclear 346, pseudogene . . . . . . . . . . . RNU6-347P . . . RNA, U6 small nuclear 347, pseudogene . . . . . . . . . . . RNU6-348P . . . RNA, U6 small nuclear 348, pseudogene . . . . . . . . . . . RNU6-349P . . . RNA, U6 small nuclear 349, pseudogene . . . . . . . . . . . RNU6-351P . . . RNA, U6 small nuclear 351, pseudogene . . . . . . . . . . . RNU6-352P . . . RNA, U6 small nuclear 352, pseudogene . . . . . . . . . . . RNU6-353P . . . RNA, U6 small nuclear 353, pseudogene . . . . . . . . . . . RNU6-354P . . . RNA, U6 small nuclear 354, pseudogene . . . . . . . . . . . RNU6-355P . . . RNA, U6 small nuclear 355, pseudogene . . . . . . . . . . . RNU6-356P . . . RNA, U6 small nuclear 356, pseudogene . . . . . . . . . . . RNU6-358P . . . RNA, U6 small nuclear 358, pseudogene . . . . . . . . . . . RNU6-359P . . . RNA, U6 small nuclear 359, pseudogene . . . . . . . . . . . RNU6-360P . . . RNA, U6 small nuclear 360, pseudogene . . . . . . . . . . . RNU6-361P . . . RNA, U6 small nuclear 361, pseudogene . . . . . . . . . . . RNU6-362P . . . RNA, U6 small nuclear 362, pseudogene . . . . . . . . . . . RNU6-363P . . . RNA, U6 small nuclear 363, pseudogene . . . . . . . . . . . RNU6-364P . . . RNA, U6 small nuclear 364, pseudogene . . . . . . . . . . . RNU6-365P . . . RNA, U6 small nuclear 365, pseudogene . . . . . . . . . . . RNU6-366P . . . RNA, U6 small nuclear 366, pseudogene . . . . . . . . . . . RNU6-367P . . . RNA, U6 small nuclear 367, pseudogene . . . . . . . . . . . RNU6-368P . . . RNA, U6 small nuclear 368, pseudogene . . . . . . . . . . . RNU6-369P . . . RNA, U6 small nuclear 369, pseudogene . . . . . . . . . . . RNU6-370P . . . RNA, U6 small nuclear 370, pseudogene . . . . . . . . . . . RNU6-371P . . . RNA, U6 small nuclear 371, pseudogene . . . . . . . . . . . RNU6-373P . . . RNA, U6 small nuclear 373, pseudogene . . . . . . . . . . . RNU6-374P . . . RNA, U6 small nuclear 374, pseudogene . . . . . . . . . . . RNU6-375P . . . RNA, U6 small nuclear 375, pseudogene . . . . . . . . . . . RNU6-376P . . . RNA, U6 small nuclear 376, pseudogene . . . . . . . . . . . RNU6-377P . . . RNA, U6 small nuclear 377, pseudogene . . . . . . . . . . . RNU6-378P . . . RNA, U6 small nuclear 378, pseudogene . . . . . . . . . . . RNU6-379P . . . RNA, U6 small nuclear 379, pseudogene . . . . . . . . . . . RNU6-380P . . . RNA, U6 small nuclear 380, pseudogene . . . . . . . . . . . RNU6-381P . . . RNA, U6 small nuclear 381, pseudogene . . . . . . . . . . . RNU6-382P . . . RNA, U6 small nuclear 382, pseudogene . . . . . . . . . . . RNU6-383P . . . RNA, U6 small nuclear 383, pseudogene . . . . . . . . . . . RNU6-384P . . . RNA, U6 small nuclear 384, pseudogene . . . . . . . . . . . RNU6-386P . . . RNA, U6 small nuclear 386, pseudogene . . . . . . . . . . . RNU6-387P . . . RNA, U6 small nuclear 387, pseudogene . . . . . . . . . . . RNU6-388P . . . RNA, U6 small nuclear 388, pseudogene . . . . . . . . . . . RNU6-389P . . . RNA, U6 small nuclear 389, pseudogene . . . . . . . . . . . RNU6-390P . . . RNA, U6 small nuclear 390, pseudogene . . . . . . . . . . . RNU6-391P . . . RNA, U6 small nuclear 391, pseudogene . . . . . . . . . . . RNU6-392P . . . RNA, U6 small nuclear 392, pseudogene . . . . . . . . . . . RNU6-393P . . . RNA, U6 small nuclear 393, pseudogene . . . . . . . . . . . RNU6-394P . . . RNA, U6 small nuclear 394, pseudogene . . . . . . . . . . . RNU6-395P . . . RNA, U6 small nuclear 395, pseudogene . . . . . . . . . . . RNU6-396P . . . RNA, U6 small nuclear 396, pseudogene . . . . . . . . . . . RNU6-397P . . . RNA, U6 small nuclear 397, pseudogene . . . . . . . . . . . RNU6-398P . . . RNA, U6 small nuclear 398, pseudogene . . . . . . . . . . . RNU6-399P . . . RNA, U6 small nuclear 399, pseudogene . . . . . . . . . . . RNU6-400P . . . RNA, U6 small nuclear 400, pseudogene . . . . . . . . . . . RNU6-401P . . . RNA, U6 small nuclear 401, pseudogene . . . . . . . . . . . RNU6-402P . . . RNA, U6 small nuclear 402, pseudogene . . . . . . . . . . . RNU6-403P . . . RNA, U6 small nuclear 403, pseudogene . . . . . . . . . . . RNU6-405P . . . RNA, U6 small nuclear 405, pseudogene . . . . . . . . . . . RNU6-406P . . . RNA, U6 small nuclear 406, pseudogene . . . . . . . . . . . RNU6-407P . . . RNA, U6 small nuclear 407, pseudogene . . . . . . . . . . . RNU6-408P . . . RNA, U6 small nuclear 408, pseudogene . . . . . . . . . . . RNU6-409P . . . RNA, U6 small nuclear 409, pseudogene . . . . . . . . . . . RNU6-410P . . . RNA, U6 small nuclear 410, pseudogene . . . . . . . . . . . RNU6-411P . . . RNA, U6 small nuclear 411, pseudogene . . . . . . . . . . . RNU6-412P . . . RNA, U6 small nuclear 412, pseudogene . . . . . . . . . . . RNU6-413P . . . RNA, U6 small nuclear 413, pseudogene . . . . . . . . . . . RNU6-414P . . . RNA, U6 small nuclear 414, pseudogene . . . . . . . . . . . RNU6-415P . . . RNA, U6 small nuclear 415, pseudogene . . . . . . . . . . . RNU6-416P . . . RNA, U6 small nuclear 416, pseudogene . . . . . . . . . . . RNU6-417P . . . RNA, U6 small nuclear 417, pseudogene . . . . . . . . . . . RNU6-418P . . . RNA, U6 small nuclear 418, pseudogene . . . . . . . . . . . RNU6-419P . . . RNA, U6 small nuclear 419, pseudogene . . . . . . . . . . . RNU6-420P . . . RNA, U6 small nuclear 420, pseudogene . . . . . . . . . . . RNU6-421P . . . RNA, U6 small nuclear 421, pseudogene . . . . . . . . . . . RNU6-422P . . . RNA, U6 small nuclear 422, pseudogene . . . . . . . . . . . RNU6-423P . . . RNA, U6 small nuclear 423, pseudogene . . . . . . . . . . . RNU6-424P . . . RNA, U6 small nuclear 424, pseudogene . . . . . . . . . . . RNU6-425P . . . RNA, U6 small nuclear 425, pseudogene . . . . . . . . . . . RNU6-426P . . . RNA, U6 small nuclear 426, pseudogene . . . . . . . . . . . RNU6-427P . . . RNA, U6 small nuclear 427, pseudogene . . . . . . . . . . . RNU6-428P . . . RNA, U6 small nuclear 428, pseudogene . . . . . . . . . . . RNU6-429P . . . RNA, U6 small nuclear 429, pseudogene . . . . . . . . . . . RNU6-430P . . . RNA, U6 small nuclear 430, pseudogene . . . . . . . . . . . RNU6-431P . . . RNA, U6 small nuclear 431, pseudogene . . . . . . . . . . . RNU6-432P . . . RNA, U6 small nuclear 432, pseudogene . . . . . . . . . . . RNU6-433P . . . RNA, U6 small nuclear 433, pseudogene . . . . . . . . . . . RNU6-434P . . . RNA, U6 small nuclear 434, pseudogene . . . . . . . . . . . RNU6-435P . . . RNA, U6 small nuclear 435, pseudogene . . . . . . . . . . . RNU6-436P . . . RNA, U6 small nuclear 436, pseudogene . . . . . . . . . . . RNU6-437P . . . RNA, U6 small nuclear 437, pseudogene . . . . . . . . . . . RNU6-438P . . . RNA, U6 small nuclear 438, pseudogene . . . . . . . . . . . RNU6-439P . . . RNA, U6 small nuclear 439, pseudogene . . . . . . . . . . . RNU6-440P . . . RNA, U6 small nuclear 440, pseudogene . . . . . . . . . . . RNU6-441P . . . RNA, U6 small nuclear 441, pseudogene . . . . . . . . . . . RNU6-442P . . . RNA, U6 small nuclear 442, pseudogene . . . . . . . . . . . RNU6-443P . . . RNA, U6 small nuclear 443, pseudogene . . . . . . . . . . . RNU6-444P . . . RNA, U6 small nuclear 444, pseudogene . . . . . . . . . . . RNU6-445P . . . RNA, U6 small nuclear 445, pseudogene . . . . . . . . . . . RNU6-446P . . . RNA, U6 small nuclear 446, pseudogene . . . . . . . . . . . RNU6-447P . . . RNA, U6 small nuclear 447, pseudogene . . . . . . . . . . . RNU6-448P . . . RNA, U6 small nuclear 448, pseudogene . . . . . . . . . . . RNU6-449P . . . RNA, U6 small nuclear 449, pseudogene . . . . . . . . . . . RNU6-450P . . . RNA, U6 small nuclear 450, pseudogene . . . . . . . . . . . RNU6-451P . . . RNA, U6 small nuclear 451, pseudogene . . . . . . . . . . . RNU6-452P . . . RNA, U6 small nuclear 452, pseudogene . . . . . . . . . . . RNU6-453P . . . RNA, U6 small nuclear 453, pseudogene . . . . . . . . . . . RNU6-454P . . . RNA, U6 small nuclear 454, pseudogene . . . . . . . . . . . RNU6-455P . . . RNA, U6 small nuclear 455, pseudogene . . . . . . . . . . . RNU6-456P . . . RNA, U6 small nuclear 456, pseudogene . . . . . . . . . . . RNU6-457P . . . RNA, U6 small nuclear 457, pseudogene . . . . . . . . . . . RNU6-458P . . . RNA, U6 small nuclear 458, pseudogene . . . . . . . . . . . RNU6-460P . . . RNA, U6 small nuclear 460, pseudogene . . . . . . . . . . . RNU6-461P . . . RNA, U6 small nuclear 461, pseudogene . . . . . . . . . . . RNU6-462P . . . RNA, U6 small nuclear 462, pseudogene . . . . . . . . . . . RNU6-463P . . . RNA, U6 small nuclear 463, pseudogene . . . . . . . . . . . RNU6-464P . . . RNA, U6 small nuclear 464, pseudogene . . . . . . . . . . . RNU6-465P . . . RNA, U6 small nuclear 465, pseudogene . . . . . . . . . . . RNU6-466P . . . RNA, U6 small nuclear 466, pseudogene . . . . . . . . . . . RNU6-467P . . . RNA, U6 small nuclear 467, pseudogene . . . . . . . . . . . RNU6-468P . . . RNA, U6 small nuclear 468, pseudogene . . . . . . . . . . . RNU6-469P . . . RNA, U6 small nuclear 469, pseudogene . . . . . . . . . . . RNU6-470P . . . RNA, U6 small nuclear 470, pseudogene . . . . . . . . . . . RNU6-471P . . . RNA, U6 small nuclear 471, pseudogene . . . . . . . . . . . RNU6-472P . . . RNA, U6 small nuclear 472, pseudogene . . . . . . . . . . . RNU6-473P . . . RNA, U6 small nuclear 473, pseudogene . . . . . . . . . . . RNU6-474P . . . RNA, U6 small nuclear 474, pseudogene . . . . . . . . . . . RNU6-475P . . . RNA, U6 small nuclear 475, pseudogene . . . . . . . . . . . RNU6-476P . . . RNA, U6 small nuclear 476, pseudogene . . . . . . . . . . . RNU6-477P . . . RNA, U6 small nuclear 477, pseudogene . . . . . . . . . . . RNU6-478P . . . RNA, U6 small nuclear 478, pseudogene . . . . . . . . . . . RNU6-479P . . . RNA, U6 small nuclear 479, pseudogene . . . . . . . . . . . RNU6-480P . . . RNA, U6 small nuclear 480, pseudogene . . . . . . . . . . . RNU6-481P . . . RNA, U6 small nuclear 481, pseudogene . . . . . . . . . . . RNU6-482P . . . RNA, U6 small nuclear 482, pseudogene . . . . . . . . . . . RNU6-483P . . . RNA, U6 small nuclear 483, pseudogene . . . . . . . . . . . RNU6-484P . . . RNA, U6 small nuclear 484, pseudogene . . . . . . . . . . . RNU6-485P . . . RNA, U6 small nuclear 485, pseudogene . . . . . . . . . . . RNU6-486P . . . RNA, U6 small nuclear 486, pseudogene . . . . . . . . . . . RNU6-487P . . . RNA, U6 small nuclear 487, pseudogene . . . . . . . . . . . RNU6-488P . . . RNA, U6 small nuclear 488, pseudogene . . . . . . . . . . . RNU6-489P . . . RNA, U6 small nuclear 489, pseudogene . . . . . . . . . . . RNU6-490P . . . RNA, U6 small nuclear 490, pseudogene . . . . . . . . . . . RNU6-491P . . . RNA, U6 small nuclear 491, pseudogene . . . . . . . . . . . RNU6-492P . . . RNA, U6 small nuclear 492, pseudogene . . . . . . . . . . . RNU6-493P . . . RNA, U6 small nuclear 493, pseudogene . . . . . . . . . . . RNU6-494P . . . RNA, U6 small nuclear 494, pseudogene . . . . . . . . . . . RNU6-495P . . . RNA, U6 small nuclear 495, pseudogene . . . . . . . . . . . RNU6-496P . . . RNA, U6 small nuclear 496, pseudogene . . . . . . . . . . . RNU6-497P . . . RNA, U6 small nuclear 497, pseudogene . . . . . . . . . . . RNU6-498P . . . RNA, U6 small nuclear 498, pseudogene . . . . . . . . . . . RNU6-499P . . . RNA, U6 small nuclear 499, pseudogene . . . . . . . . . . . RNU6-500P . . . RNA, U6 small nuclear 500, pseudogene . . . . . . . . . . . RNU6-501P . . . RNA, U6 small nuclear 501, pseudogene . . . . . . . . . . . RNU6-502P . . . RNA, U6 small nuclear 502, pseudogene . . . . . . . . . . . RNU6-503P . . . RNA, U6 small nuclear 503, pseudogene . . . . . . . . . . . RNU6-504P . . . RNA, U6 small nuclear 504, pseudogene . . . . . . . . . . . RNU6-505P . . . RNA, U6 small nuclear 505, pseudogene . . . . . . . . . . . RNU6-506P . . . RNA, U6 small nuclear 506, pseudogene . . . . . . . . . . . RNU6-507P . . . RNA, U6 small nuclear 507, pseudogene . . . . . . . . . . . RNU6-508P . . . RNA, U6 small nuclear 508, pseudogene . . . . . . . . . . . RNU6-509P . . . RNA, U6 small nuclear 509, pseudogene . . . . . . . . . . . RNU6-510P . . . RNA, U6 small nuclear 510, pseudogene . . . . . . . . . . . RNU6-511P . . . RNA, U6 small nuclear 511, pseudogene . . . . . . . . . . . RNU6-512P . . . RNA, U6 small nuclear 512, pseudogene . . . . . . . . . . . RNU6-513P . . . RNA, U6 small nuclear 513, pseudogene . . . . . . . . . . . RNU6-514P . . . RNA, U6 small nuclear 514, pseudogene . . . . . . . . . . . RNU6-516P . . . RNA, U6 small nuclear 516, pseudogene . . . . . . . . . . . RNU6-517P . . . RNA, U6 small nuclear 517, pseudogene . . . . . . . . . . . RNU6-518P . . . RNA, U6 small nuclear 518, pseudogene . . . . . . . . . . . RNU6-519P . . . RNA, U6 small nuclear 519, pseudogene . . . . . . . . . . . RNU6-520P . . . RNA, U6 small nuclear 520, pseudogene . . . . . . . . . . . RNU6-521P . . . RNA, U6 small nuclear 521, pseudogene . . . . . . . . . . . RNU6-522P . . . RNA, U6 small nuclear 522, pseudogene . . . . . . . . . . . RNU6-523P . . . RNA, U6 small nuclear 523, pseudogene . . . . . . . . . . . RNU6-524P . . . RNA, U6 small nuclear 524, pseudogene . . . . . . . . . . . RNU6-525P . . . RNA, U6 small nuclear 525, pseudogene . . . . . . . . . . . RNU6-526P . . . RNA, U6 small nuclear 526, pseudogene . . . . . . . . . . . RNU6-527P . . . RNA, U6 small nuclear 527, pseudogene . . . . . . . . . . . RNU6-528P . . . RNA, U6 small nuclear 528, pseudogene . . . . . . . . . . . RNU6-529P . . . RNA, U6 small nuclear 529, pseudogene . . . . . . . . . . . RNU6-530P . . . RNA, U6 small nuclear 530, pseudogene . . . . . . . . . . . RNU6-531P . . . RNA, U6 small nuclear 531, pseudogene . . . . . . . . . . . RNU6-532P . . . RNA, U6 small nuclear 532, pseudogene . . . . . . . . . . . RNU6-533P . . . RNA, U6 small nuclear 533, pseudogene . . . . . . . . . . . RNU6-534P . . . RNA, U6 small nuclear 534, pseudogene . . . . . . . . . . . RNU6-535P . . . RNA, U6 small nuclear 535, pseudogene . . . . . . . . . . . RNU6-536P . . . RNA, U6 small nuclear 536, pseudogene . . . . . . . . . . . RNU6-537P . . . RNA, U6 small nuclear 537, pseudogene . . . . . . . . . . . RNU6-538P . . . RNA, U6 small nuclear 538, pseudogene . . . . . . . . . . . RNU6-539P . . . RNA, U6 small nuclear 539, pseudogene . . . . . . . . . . . RNU6-540P . . . RNA, U6 small nuclear 540, pseudogene . . . . . . . . . . . RNU6-541P . . . RNA, U6 small nuclear 541, pseudogene . . . . . . . . . . . RNU6-542P . . . RNA, U6 small nuclear 542, pseudogene . . . . . . . . . . . RNU6-543P . . . RNA, U6 small nuclear 543, pseudogene . . . . . . . . . . . RNU6-544P . . . RNA, U6 small nuclear 544, pseudogene . . . . . . . . . . . RNU6-545P . . . RNA, U6 small nuclear 545, pseudogene . . . . . . . . . . . RNU6-546P . . . RNA, U6 small nuclear 546, pseudogene . . . . . . . . . . . RNU6-547P . . . RNA, U6 small nuclear 547, pseudogene . . . . . . . . . . . RNU6-548P . . . RNA, U6 small nuclear 548, pseudogene . . . . . . . . . . . RNU6-549P . . . RNA, U6 small nuclear 549, pseudogene . . . . . . . . . . . RNU6-550P . . . RNA, U6 small nuclear 550, pseudogene . . . . . . . . . . . RNU6-551P . . . RNA, U6 small nuclear 551, pseudogene . . . . . . . . . . . RNU6-552P . . . RNA, U6 small nuclear 552, pseudogene . . . . . . . . . . . RNU6-553P . . . RNA, U6 small nuclear 553, pseudogene . . . . . . . . . . . RNU6-554P . . . RNA, U6 small nuclear 554, pseudogene . . . . . . . . . . . RNU6-555P . . . RNA, U6 small nuclear 555, pseudogene . . . . . . . . . . . RNU6-556P . . . RNA, U6 small nuclear 556, pseudogene . . . . . . . . . . . RNU6-557P . . . RNA, U6 small nuclear 557, pseudogene . . . . . . . . . . . RNU6-558P . . . RNA, U6 small nuclear 558, pseudogene . . . . . . . . . . . RNU6-559P . . . RNA, U6 small nuclear 559, pseudogene . . . . . . . . . . . RNU6-560P . . . RNA, U6 small nuclear 560, pseudogene . . . . . . . . . . . RNU6-561P . . . RNA, U6 small nuclear 561, pseudogene . . . . . . . . . . . RNU6-562P . . . RNA, U6 small nuclear 562, pseudogene . . . . . . . . . . . RNU6-563P . . . RNA, U6 small nuclear 563, pseudogene . . . . . . . . . . . RNU6-564P . . . RNA, U6 small nuclear 564, pseudogene . . . . . . . . . . . RNU6-565P . . . RNA, U6 small nuclear 565, pseudogene . . . . . . . . . . . RNU6-566P . . . RNA, U6 small nuclear 566, pseudogene . . . . . . . . . . . RNU6-567P . . . RNA, U6 small nuclear 567, pseudogene . . . . . . . . . . . RNU6-570P . . . RNA, U6 small nuclear 570, pseudogene . . . . . . . . . . . RNU6-571P . . . RNA, U6 small nuclear 571, pseudogene . . . . . . . . . . . RNU6-572P . . . RNA, U6 small nuclear 572, pseudogene . . . . . . . . . . . RNU6-573P . . . RNA, U6 small nuclear 573, pseudogene . . . . . . . . . . . RNU6-574P . . . RNA, U6 small nuclear 574, pseudogene . . . . . . . . . . . RNU6-575P . . . RNA, U6 small nuclear 575, pseudogene . . . . . . . . . . . RNU6-576P . . . RNA, U6 small nuclear 576, pseudogene . . . . . . . . . . . RNU6-577P . . . RNA, U6 small nuclear 577, pseudogene . . . . . . . . . . . RNU6-578P . . . RNA, U6 small nuclear 578, pseudogene . . . . . . . . . . . RNU6-579P . . . RNA, U6 small nuclear 579, pseudogene . . . . . . . . . . . RNU6-580P . . . RNA, U6 small nuclear 580, pseudogene . . . . . . . . . . . RNU6-581P . . . RNA, U6 small nuclear 581, pseudogene . . . . . . . . . . . RNU6-582P . . . RNA, U6 small nuclear 582, pseudogene . . . . . . . . . . . RNU6-583P . . . RNA, U6 small nuclear 583, pseudogene . . . . . . . . . . . RNU6-584P . . . RNA, U6 small nuclear 584, pseudogene . . . . . . . . . . . RNU6-586P . . . RNA, U6 small nuclear 586, pseudogene . . . . . . . . . . . RNU6-587P . . . RNA, U6 small nuclear 587, pseudogene . . . . . . . . . . . RNU6-588P . . . RNA, U6 small nuclear 588, pseudogene . . . . . . . . . . . RNU6-589P . . . RNA, U6 small nuclear 589, pseudogene . . . . . . . . . . . RNU6-590P . . . RNA, U6 small nuclear 590, pseudogene . . . . . . . . . . . RNU6-591P . . . RNA, U6 small nuclear 591, pseudogene . . . . . . . . . . . RNU6-592P . . . RNA, U6 small nuclear 592, pseudogene . . . . . . . . . . . RNU6-593P . . . RNA, U6 small nuclear 593, pseudogene . . . . . . . . . . . RNU6-595P . . . RNA, U6 small nuclear 595, pseudogene . . . . . . . . . . . RNU6-596P . . . RNA, U6 small nuclear 596, pseudogene . . . . . . . . . . . RNU6-597P . . . RNA, U6 small nuclear 597, pseudogene . . . . . . . . . . . RNU6-598P . . . RNA, U6 small nuclear 598, pseudogene . . . . . . . . . . . RNU6-599P . . . RNA, U6 small nuclear 599, pseudogene . . . . . . . . . . . RNU6-600P . . . RNA, U6 small nuclear 600, pseudogene . . . . . . . . . . . RNU6-601P . . . RNA, U6 small nuclear 601, pseudogene . . . . . . . . . . . RNU6-602P . . . RNA, U6 small nuclear 602, pseudogene . . . . . . . . . . . RNU6-603P . . . RNA, U6 small nuclear 603, pseudogene . . . . . . . . . . . RNU6-604P . . . RNA, U6 small nuclear 604, pseudogene . . . . . . . . . . . RNU6-605P . . . RNA, U6 small nuclear 605, pseudogene . . . . . . . . . . . RNU6-606P . . . RNA, U6 small nuclear 606, pseudogene . . . . . . . . . . . RNU6-607P . . . RNA, U6 small nuclear 607, pseudogene . . . . . . . . . . . RNU6-608P . . . RNA, U6 small nuclear 608, pseudogene . . . . . . . . . . . RNU6-609P . . . RNA, U6 small nuclear 609, pseudogene . . . . . . . . . . . RNU6-610P . . . RNA, U6 small nuclear 610, pseudogene . . . . . . . . . . . RNU6-611P . . . RNA, U6 small nuclear 611, pseudogene . . . . . . . . . . . RNU6-612P . . . RNA, U6 small nuclear 612, pseudogene . . . . . . . . . . . RNU6-613P . . . RNA, U6 small nuclear 613, pseudogene . . . . . . . . . . . RNU6-614P . . . RNA, U6 small nuclear 614, pseudogene . . . . . . . . . . . RNU6-615P . . . RNA, U6 small nuclear 615, pseudogene . . . . . . . . . . . RNU6-616P . . . RNA, U6 small nuclear 616, pseudogene . . . . . . . . . . . RNU6-617P . . . RNA, U6 small nuclear 617, pseudogene . . . . . . . . . . . RNU6-618P . . . RNA, U6 small nuclear 618, pseudogene . . . . . . . . . . . RNU6-619P . . . RNA, U6 small nuclear 619, pseudogene . . . . . . . . . . . RNU6-620P . . . RNA, U6 small nuclear 620, pseudogene . . . . . . . . . . . RNU6-621P . . . RNA, U6 small nuclear 621, pseudogene . . . . . . . . . . . RNU6-622P . . . RNA, U6 small nuclear 622, pseudogene . . . . . . . . . . . RNU6-623P . . . RNA, U6 small nuclear 623, pseudogene . . . . . . . . . . . RNU6-624P . . . RNA, U6 small nuclear 624, pseudogene . . . . . . . . . . . RNU6-625P . . . RNA, U6 small nuclear 625, pseudogene . . . . . . . . . . . RNU6-626P . . . RNA, U6 small nuclear 626, pseudogene . . . . . . . . . . . RNU6-627P . . . RNA, U6 small nuclear 627, pseudogene . . . . . . . . . . . RNU6-628P . . . RNA, U6 small nuclear 628, pseudogene . . . . . . . . . . . RNU6-629P . . . RNA, U6 small nuclear 629, pseudogene . . . . . . . . . . . RNU6-630P . . . RNA, U6 small nuclear 630, pseudogene . . . . . . . . . . . RNU6-631P . . . RNA, U6 small nuclear 631, pseudogene . . . . . . . . . . . RNU6-632P . . . RNA, U6 small nuclear 632, pseudogene . . . . . . . . . . . RNU6-633P . . . RNA, U6 small nuclear 633, pseudogene . . . . . . . . . . . RNU6-634P . . . RNA, U6 small nuclear 634, pseudogene . . . . . . . . . . . RNU6-635P . . . RNA, U6 small nuclear 635, pseudogene . . . . . . . . . . . RNU6-636P . . . RNA, U6 small nuclear 636, pseudogene . . . . . . . . . . . RNU6-637P . . . RNA, U6 small nuclear 637, pseudogene . . . . . . . . . . . RNU6-638P . . . RNA, U6 small nuclear 638, pseudogene . . . . . . . . . . . RNU6-639P . . . RNA, U6 small nuclear 639, pseudogene . . . . . . . . . . . RNU6-640P . . . RNA, U6 small nuclear 640, pseudogene . . . . . . . . . . . RNU6-641P . . . RNA, U6 small nuclear 641, pseudogene . . . . . . . . . . . RNU6-642P . . . RNA, U6 small nuclear 642, pseudogene . . . . . . . . . . . RNU6-643P . . . RNA, U6 small nuclear 643, pseudogene . . . . . . . . . . . RNU6-644P . . . RNA, U6 small nuclear 644, pseudogene . . . . . . . . . . . RNU6-645P . . . RNA, U6 small nuclear 645, pseudogene . . . . . . . . . . . RNU6-646P . . . RNA, U6 small nuclear 646, pseudogene . . . . . . . . . . . RNU6-647P . . . RNA, U6 small nuclear 647, pseudogene . . . . . . . . . . . RNU6-648P . . . RNA, U6 small nuclear 648, pseudogene . . . . . . . . . . . RNU6-649P . . . RNA, U6 small nuclear 649, pseudogene . . . . . . . . . . . RNU6-650P . . . RNA, U6 small nuclear 650, pseudogene . . . . . . . . . . . RNU6-651P . . . RNA, U6 small nuclear 651, pseudogene . . . . . . . . . . . RNU6-652P . . . RNA, U6 small nuclear 652, pseudogene . . . . . . . . . . . RNU6-653P . . . RNA, U6 small nuclear 653, pseudogene . . . . . . . . . . . RNU6-654P . . . RNA, U6 small nuclear 654, pseudogene . . . . . . . . . . . RNU6-655P . . . RNA, U6 small nuclear 655, pseudogene . . . . . . . . . . . RNU6-656P . . . RNA, U6 small nuclear 656, pseudogene . . . . . . . . . . . RNU6-657P . . . RNA, U6 small nuclear 657, pseudogene . . . . . . . . . . . RNU6-658P . . . RNA, U6 small nuclear 658, pseudogene . . . . . . . . . . . RNU6-659P . . . RNA, U6 small nuclear 659, pseudogene . . . . . . . . . . . RNU6-660P . . . RNA, U6 small nuclear 660, pseudogene . . . . . . . . . . . RNU6-661P . . . RNA, U6 small nuclear 661, pseudogene . . . . . . . . . . . RNU6-662P . . . RNA, U6 small nuclear 662, pseudogene . . . . . . . . . . . RNU6-663P . . . RNA, U6 small nuclear 663, pseudogene . . . . . . . . . . . RNU6-664P . . . RNA, U6 small nuclear 664, pseudogene . . . . . . . . . . . RNU6-665P . . . RNA, U6 small nuclear 665, pseudogene . . . . . . . . . . . RNU6-666P . . . RNA, U6 small nuclear 666, pseudogene . . . . . . . . . . . RNU6-667P . . . RNA, U6 small nuclear 667, pseudogene . . . . . . . . . . . RNU6-668P . . . RNA, U6 small nuclear 668, pseudogene . . . . . . . . . . . RNU6-669P . . . RNA, U6 small nuclear 669, pseudogene . . . . . . . . . . . RNU6-670P . . . RNA, U6 small nuclear 670, pseudogene . . . . . . . . . . . RNU6-672P . . . RNA, U6 small nuclear 672, pseudogene . . . . . . . . . . . RNU6-673P . . . RNA, U6 small nuclear 673, pseudogene . . . . . . . . . . . RNU6-674P . . . RNA, U6 small nuclear 674, pseudogene . . . . . . . . . . . RNU6-675P . . . RNA, U6 small nuclear 675, pseudogene . . . . . . . . . . . RNU6-677P . . . RNA, U6 small nuclear 677, pseudogene . . . . . . . . . . . RNU6-678P . . . RNA, U6 small nuclear 678, pseudogene . . . . . . . . . . . RNU6-679P . . . RNA, U6 small nuclear 679, pseudogene . . . . . . . . . . . RNU6-680P . . . RNA, U6 small nuclear 680, pseudogene . . . . . . . . . . . RNU6-681P . . . RNA, U6 small nuclear 681, pseudogene . . . . . . . . . . . RNU6-682P . . . RNA, U6 small nuclear 682, pseudogene . . . . . . . . . . . RNU6-684P . . . RNA, U6 small nuclear 684, pseudogene . . . . . . . . . . . RNU6-685P . . . RNA, U6 small nuclear 685, pseudogene . . . . . . . . . . . RNU6-686P . . . RNA, U6 small nuclear 686, pseudogene . . . . . . . . . . . RNU6-687P . . . RNA, U6 small nuclear 687, pseudogene . . . . . . . . . . . RNU6-689P . . . RNA, U6 small nuclear 689, pseudogene . . . . . . . . . . . RNU6-690P . . . RNA, U6 small nuclear 690, pseudogene . . . . . . . . . . . RNU6-692P . . . RNA, U6 small nuclear 692, pseudogene . . . . . . . . . . . RNU6-693P . . . RNA, U6 small nuclear 693, pseudogene . . . . . . . . . . . RNU6-694P . . . RNA, U6 small nuclear 694, pseudogene . . . . . . . . . . . RNU6-695P . . . RNA, U6 small nuclear 695, pseudogene . . . . . . . . . . . RNU6-696P . . . RNA, U6 small nuclear 696, pseudogene . . . . . . . . . . . RNU6-697P . . . RNA, U6 small nuclear 697, pseudogene . . . . . . . . . . . RNU6-698P . . . RNA, U6 small nuclear 698, pseudogene . . . . . . . . . . . RNU6-699P . . . RNA, U6 small nuclear 699, pseudogene . . . . . . . . . . . RNU6-700P . . . RNA, U6 small nuclear 700, pseudogene . . . . . . . . . . . RNU6-701P . . . RNA, U6 small nuclear 701, pseudogene . . . . . . . . . . . RNU6-702P . . . RNA, U6 small nuclear 702, pseudogene . . . . . . . . . . . RNU6-703P . . . RNA, U6 small nuclear 703, pseudogene . . . . . . . . . . . RNU6-704P . . . RNA, U6 small nuclear 704, pseudogene . . . . . . . . . . . RNU6-705P . . . RNA, U6 small nuclear 705, pseudogene . . . . . . . . . . . RNU6-706P . . . RNA, U6 small nuclear 706, pseudogene . . . . . . . . . . . RNU6-707P . . . RNA, U6 small nuclear 707, pseudogene . . . . . . . . . . . RNU6-708P . . . RNA, U6 small nuclear 708, pseudogene . . . . . . . . . . . RNU6-709P . . . RNA, U6 small nuclear 709, pseudogene . . . . . . . . . . . RNU6-710P . . . RNA, U6 small nuclear 710, pseudogene . . . . . . . . . . . RNU6-711P . . . RNA, U6 small nuclear 711, pseudogene . . . . . . . . . . . RNU6-712P . . . RNA, U6 small nuclear 712, pseudogene . . . . . . . . . . . RNU6-713P . . . RNA, U6 small nuclear 713, pseudogene . . . . . . . . . . . RNU6-714P . . . RNA, U6 small nuclear 714, pseudogene . . . . . . . . . . . RNU6-715P . . . RNA, U6 small nuclear 715, pseudogene . . . . . . . . . . . RNU6-716P . . . RNA, U6 small nuclear 716, pseudogene . . . . . . . . . . . RNU6-717P . . . RNA, U6 small nuclear 717, pseudogene . . . . . . . . . . . RNU6-718P . . . RNA, U6 small nuclear 718, pseudogene . . . . . . . . . . . RNU6-719P . . . RNA, U6 small nuclear 719, pseudogene . . . . . . . . . . . RNU6-720P . . . RNA, U6 small nuclear 720, pseudogene . . . . . . . . . . . RNU6-721P . . . RNA, U6 small nuclear 721, pseudogene . . . . . . . . . . . RNU6-722P . . . RNA, U6 small nuclear 722, pseudogene . . . . . . . . . . . RNU6-723P . . . RNA, U6 small nuclear 723, pseudogene . . . . . . . . . . . RNU6-724P . . . RNA, U6 small nuclear 724, pseudogene . . . . . . . . . . . RNU6-725P . . . RNA, U6 small nuclear 725, pseudogene . . . . . . . . . . . RNU6-726P . . . RNA, U6 small nuclear 726, pseudogene . . . . . . . . . . . RNU6-727P . . . RNA, U6 small nuclear 727, pseudogene . . . . . . . . . . . RNU6-728P . . . RNA, U6 small nuclear 728, pseudogene . . . . . . . . . . . RNU6-729P . . . RNA, U6 small nuclear 729, pseudogene . . . . . . . . . . . RNU6-730P . . . RNA, U6 small nuclear 730, pseudogene . . . . . . . . . . . RNU6-731P . . . RNA, U6 small nuclear 731, pseudogene . . . . . . . . . . . RNU6-732P . . . RNA, U6 small nuclear 732, pseudogene . . . . . . . . . . . RNU6-733P . . . RNA, U6 small nuclear 733, pseudogene . . . . . . . . . . . RNU6-735P . . . RNA, U6 small nuclear 735, pseudogene . . . . . . . . . . . RNU6-737P . . . RNA, U6 small nuclear 737, pseudogene . . . . . . . . . . . RNU6-738P . . . RNA, U6 small nuclear 738, pseudogene . . . . . . . . . . . RNU6-739P . . . RNA, U6 small nuclear 739, pseudogene . . . . . . . . . . . RNU6-740P . . . RNA, U6 small nuclear 740, pseudogene . . . . . . . . . . . RNU6-741P . . . RNA, U6 small nuclear 741, pseudogene . . . . . . . . . . . RNU6-742P . . . RNA, U6 small nuclear 742, pseudogene . . . . . . . . . . . RNU6-743P . . . RNA, U6 small nuclear 743, pseudogene . . . . . . . . . . . RNU6-744P . . . RNA, U6 small nuclear 744, pseudogene . . . . . . . . . . . RNU6-745P . . . RNA, U6 small nuclear 745, pseudogene . . . . . . . . . . . RNU6-746P . . . RNA, U6 small nuclear 746, pseudogene . . . . . . . . . . . RNU6-747P . . . RNA, U6 small nuclear 747, pseudogene . . . . . . . . . . . RNU6-748P . . . RNA, U6 small nuclear 748, pseudogene . . . . . . . . . . . RNU6-749P . . . RNA, U6 small nuclear 749, pseudogene . . . . . . . . . . . RNU6-750P . . . RNA, U6 small nuclear 750, pseudogene . . . . . . . . . . . RNU6-751P . . . RNA, U6 small nuclear 751, pseudogene . . . . . . . . . . . RNU6-752P . . . RNA, U6 small nuclear 752, pseudogene . . . . . . . . . . . RNU6-753P . . . RNA, U6 small nuclear 753, pseudogene . . . . . . . . . . . RNU6-754P . . . RNA, U6 small nuclear 754, pseudogene . . . . . . . . . . . RNU6-755P . . . RNA, U6 small nuclear 755, pseudogene . . . . . . . . . . . RNU6-756P . . . RNA, U6 small nuclear 756, pseudogene . . . . . . . . . . . RNU6-757P . . . RNA, U6 small nuclear 757, pseudogene . . . . . . . . . . . RNU6-758P . . . RNA, U6 small nuclear 758, pseudogene . . . . . . . . . . . RNU6-759P . . . RNA, U6 small nuclear 759, pseudogene . . . . . . . . . . . RNU6-760P . . . RNA, U6 small nuclear 760, pseudogene . . . . . . . . . . . RNU6-761P . . . RNA, U6 small nuclear 761, pseudogene . . . . . . . . . . . RNU6-762P . . . RNA, U6 small nuclear 762, pseudogene . . . . . . . . . . . RNU6-763P . . . RNA, U6 small nuclear 763, pseudogene . . . . . . . . . . . RNU6-764P . . . RNA, U6 small nuclear 764, pseudogene . . . . . . . . . . . RNU6-765P . . . RNA, U6 small nuclear 765, pseudogene . . . . . . . . . . . RNU6-766P . . . RNA, U6 small nuclear 766, pseudogene . . . . . . . . . . . RNU6-767P . . . RNA, U6 small nuclear 767, pseudogene . . . . . . . . . . . RNU6-768P . . . RNA, U6 small nuclear 768, pseudogene . . . . . . . . . . . RNU6-769P . . . RNA, U6 small nuclear 769, pseudogene . . . . . . . . . . . RNU6-770P . . . RNA, U6 small nuclear 770, pseudogene . . . . . . . . . . . RNU6-771P . . . RNA, U6 small nuclear 771, pseudogene . . . . . . . . . . . RNU6-772P . . . RNA, U6 small nuclear 772, pseudogene . . . . . . . . . . . RNU6-773P . . . RNA, U6 small nuclear 773, pseudogene . . . . . . . . . . . RNU6-774P . . . RNA, U6 small nuclear 774, pseudogene . . . . . . . . . . . RNU6-775P . . . RNA, U6 small nuclear 775, pseudogene . . . . . . . . . . . RNU6-776P . . . RNA, U6 small nuclear 776, pseudogene . . . . . . . . . . . RNU6-777P . . . RNA, U6 small nuclear 777, pseudogene . . . . . . . . . . . RNU6-778P . . . RNA, U6 small nuclear 778, pseudogene . . . . . . . . . . . RNU6-780P . . . RNA, U6 small nuclear 780, pseudogene . . . . . . . . . . . RNU6-781P . . . RNA, U6 small nuclear 781, pseudogene . . . . . . . . . . . RNU6-782P . . . RNA, U6 small nuclear 782, pseudogene . . . . . . . . . . . RNU6-783P . . . RNA, U6 small nuclear 783, pseudogene . . . . . . . . . . . RNU6-784P . . . RNA, U6 small nuclear 784, pseudogene . . . . . . . . . . . RNU6-785P . . . RNA, U6 small nuclear 785, pseudogene . . . . . . . . . . . RNU6-786P . . . RNA, U6 small nuclear 786, pseudogene . . . . . . . . . . . RNU6-787P . . . RNA, U6 small nuclear 787, pseudogene . . . . . . . . . . . RNU6-788P . . . RNA, U6 small nuclear 788, pseudogene . . . . . . . . . . . RNU6-789P . . . RNA, U6 small nuclear 789, pseudogene . . . . . . . . . . . RNU6-790P . . . RNA, U6 small nuclear 790, pseudogene . . . . . . . . . . . RNU6-791P . . . RNA, U6 small nuclear 791, pseudogene . . . . . . . . . . . RNU6-792P . . . RNA, U6 small nuclear 792, pseudogene . . . . . . . . . . . RNU6-793P . . . RNA, U6 small nuclear 793, pseudogene . . . . . . . . . . . RNU6-794P . . . RNA, U6 small nuclear 794, pseudogene . . . . . . . . . . . RNU6-795P . . . RNA, U6 small nuclear 795, pseudogene . . . . . . . . . . . RNU6-796P . . . RNA, U6 small nuclear 796, pseudogene . . . . . . . . . . . RNU6-797P . . . RNA, U6 small nuclear 797, pseudogene . . . . . . . . . . . RNU6-798P . . . RNA, U6 small nuclear 798, pseudogene . . . . . . . . . . . RNU6-799P . . . RNA, U6 small nuclear 799, pseudogene . . . . . . . . . . . RNU6-800P . . . RNA, U6 small nuclear 800, pseudogene . . . . . . . . . . . RNU6-801P . . . RNA, U6 small nuclear 801, pseudogene . . . . . . . . . . . RNU6-803P . . . RNA, U6 small nuclear 803, pseudogene . . . . . . . . . . . RNU6-804P . . . RNA, U6 small nuclear 804, pseudogene . . . . . . . . . . . RNU6-805P . . . RNA, U6 small nuclear 805, pseudogene . . . . . . . . . . . RNU6-806P . . . RNA, U6 small nuclear 806, pseudogene . . . . . . . . . . . RNU6-807P . . . RNA, U6 small nuclear 807, pseudogene . . . . . . . . . . . RNU6-808P . . . RNA, U6 small nuclear 808, pseudogene . . . . . . . . . . . RNU6-809P . . . RNA, U6 small nuclear 809, pseudogene . . . . . . . . . . . RNU6-810P . . . RNA, U6 small nuclear 810, pseudogene . . . . . . . . . . . RNU6-811P . . . RNA, U6 small nuclear 811, pseudogene . . . . . . . . . . . RNU6-812P . . . RNA, U6 small nuclear 812, pseudogene . . . . . . . . . . . RNU6-813P . . . RNA, U6 small nuclear 813, pseudogene . . . . . . . . . . . RNU6-815P . . . RNA, U6 small nuclear 815, pseudogene . . . . . . . . . . . RNU6-816P . . . RNA, U6 small nuclear 816, pseudogene . . . . . . . . . . . RNU6-817P . . . RNA, U6 small nuclear 817, pseudogene . . . . . . . . . . . RNU6-818P . . . RNA, U6 small nuclear 818, pseudogene . . . . . . . . . . . RNU6-819P . . . RNA, U6 small nuclear 819, pseudogene . . . . . . . . . . . RNU6-820P . . . RNA, U6 small nuclear 820, pseudogene . . . . . . . . . . . RNU6-821P . . . RNA, U6 small nuclear 821, pseudogene . . . . . . . . . . . RNU6-822P . . . RNA, U6 small nuclear 822, pseudogene . . . . . . . . . . . RNU6-823P . . . RNA, U6 small nuclear 823, pseudogene . . . . . . . . . . . RNU6-824P . . . RNA, U6 small nuclear 824, pseudogene . . . . . . . . . . . RNU6-826P . . . RNA, U6 small nuclear 826, pseudogene . . . . . . . . . . . RNU6-827P . . . RNA, U6 small nuclear 827, pseudogene . . . . . . . . . . . RNU6-828P . . . RNA, U6 small nuclear 828, pseudogene . . . . . . . . . . . RNU6-829P . . . RNA, U6 small nuclear 829, pseudogene . . . . . . . . . . . RNU6-830P . . . RNA, U6 small nuclear 830, pseudogene . . . . . . . . . . . RNU6-831P . . . RNA, U6 small nuclear 831, pseudogene . . . . . . . . . . . RNU6-832P . . . RNA, U6 small nuclear 832, pseudogene . . . . . . . . . . . RNU6-833P . . . RNA, U6 small nuclear 833, pseudogene . . . . . . . . . . . RNU6-834P . . . RNA, U6 small nuclear 834, pseudogene . . . . . . . . . . . RNU6-835P . . . RNA, U6 small nuclear 835, pseudogene . . . . . . . . . . . RNU6-836P . . . RNA, U6 small nuclear 836, pseudogene . . . . . . . . . . . RNU6-837P . . . RNA, U6 small nuclear 837, pseudogene . . . . . . . . . . . RNU6-838P . . . RNA, U6 small nuclear 838, pseudogene . . . . . . . . . . . RNU6-839P . . . RNA, U6 small nuclear 839, pseudogene . . . . . . . . . . . RNU6-840P . . . RNA, U6 small nuclear 840, pseudogene . . . . . . . . . . . RNU6-841P . . . RNA, U6 small nuclear 841, pseudogene . . . . . . . . . . . RNU6-842P . . . RNA, U6 small nuclear 842, pseudogene . . . . . . . . . . . RNU6-843P . . . RNA, U6 small nuclear 843, pseudogene . . . . . . . . . . . RNU6-844P . . . RNA, U6 small nuclear 844, pseudogene . . . . . . . . . . . RNU6-845P . . . RNA, U6 small nuclear 845, pseudogene . . . . . . . . . . . RNU6-847P . . . RNA, U6 small nuclear 847, pseudogene . . . . . . . . . . . RNU6-848P . . . RNA, U6 small nuclear 848, pseudogene . . . . . . . . . . . RNU6-849P . . . RNA, U6 small nuclear 849, pseudogene . . . . . . . . . . . RNU6-850P . . . RNA, U6 small nuclear 850, pseudogene . . . . . . . . . . . RNU6-851P . . . RNA, U6 small nuclear 851, pseudogene . . . . . . . . . . . RNU6-853P . . . RNA, U6 small nuclear 853, pseudogene . . . . . . . . . . . RNU6-854P . . . RNA, U6 small nuclear 854, pseudogene . . . . . . . . . . . RNU6-855P . . . RNA, U6 small nuclear 855, pseudogene . . . . . . . . . . . RNU6-856P . . . RNA, U6 small nuclear 856, pseudogene . . . . . . . . . . . RNU6-857P . . . RNA, U6 small nuclear 857, pseudogene . . . . . . . . . . . RNU6-858P . . . RNA, U6 small nuclear 858, pseudogene . . . . . . . . . . . RNU6-859P . . . RNA, U6 small nuclear 859, pseudogene . . . . . . . . . . . RNU6-860P . . . RNA, U6 small nuclear 860, pseudogene . . . . . . . . . . . RNU6-861P . . . RNA, U6 small nuclear 861, pseudogene . . . . . . . . . . . RNU6-862P . . . RNA, U6 small nuclear 862, pseudogene . . . . . . . . . . . RNU6-863P . . . RNA, U6 small nuclear 863, pseudogene . . . . . . . . . . . RNU6-864P . . . RNA, U6 small nuclear 864, pseudogene . . . . . . . . . . . RNU6-865P . . . RNA, U6 small nuclear 865, pseudogene . . . . . . . . . . . RNU6-866P . . . RNA, U6 small nuclear 866, pseudogene . . . . . . . . . . . RNU6-867P . . . RNA, U6 small nuclear 867, pseudogene . . . . . . . . . . . RNU6-869P . . . RNA, U6 small nuclear 869, pseudogene . . . . . . . . . . . RNU6-871P . . . RNA, U6 small nuclear 871, pseudogene . . . . . . . . . . . RNU6-873P . . . RNA, U6 small nuclear 873, pseudogene . . . . . . . . . . . RNU6-874P . . . RNA, U6 small nuclear 874, pseudogene . . . . . . . . . . . RNU6-875P . . . RNA, U6 small nuclear 875, pseudogene . . . . . . . . . . . RNU6-876P . . . RNA, U6 small nuclear 876, pseudogene . . . . . . . . . . . RNU6-877P . . . RNA, U6 small nuclear 877, pseudogene . . . . . . . . . . . RNU6-878P . . . RNA, U6 small nuclear 878, pseudogene . . . . . . . . . . . RNU6-879P . . . RNA, U6 small nuclear 879, pseudogene . . . . . . . . . . . RNU6-880P . . . RNA, U6 small nuclear 880, pseudogene . . . . . . . . . . . RNU6-881P . . . RNA, U6 small nuclear 881, pseudogene . . . . . . . . . . . RNU6-882P . . . RNA, U6 small nuclear 882, pseudogene . . . . . . . . . . . RNU6-883P . . . RNA, U6 small nuclear 883, pseudogene . . . . . . . . . . . RNU6-884P . . . RNA, U6 small nuclear 884, pseudogene . . . . . . . . . . . RNU6-885P . . . RNA, U6 small nuclear 885, pseudogene . . . . . . . . . . . RNU6-886P . . . RNA, U6 small nuclear 886, pseudogene . . . . . . . . . . . RNU6-887P . . . RNA, U6 small nuclear 887, pseudogene . . . . . . . . . . . RNU6-888P . . . RNA, U6 small nuclear 888, pseudogene . . . . . . . . . . . RNU6-889P . . . RNA, U6 small nuclear 889, pseudogene . . . . . . . . . . . RNU6-890P . . . RNA, U6 small nuclear 890, pseudogene . . . . . . . . . . . RNU6-891P . . . RNA, U6 small nuclear 891, pseudogene . . . . . . . . . . . RNU6-892P . . . RNA, U6 small nuclear 892, pseudogene . . . . . . . . . . . RNU6-893P . . . RNA, U6 small nuclear 893, pseudogene . . . . . . . . . . . RNU6-894P . . . RNA, U6 small nuclear 894, pseudogene . . . . . . . . . . . RNU6-895P . . . RNA, U6 small nuclear 895, pseudogene . . . . . . . . . . . RNU6-896P . . . RNA, U6 small nuclear 896, pseudogene . . . . . . . . . . . RNU6-897P . . . RNA, U6 small nuclear 897, pseudogene . . . . . . . . . . . RNU6-898P . . . RNA, U6 small nuclear 898, pseudogene . . . . . . . . . . . RNU6-899P . . . RNA, U6 small nuclear 899, pseudogene . . . . . . . . . . . RNU6-900P . . . RNA, U6 small nuclear 900, pseudogene . . . . . . . . . . . RNU6-901P . . . RNA, U6 small nuclear 901, pseudogene . . . . . . . . . . . RNU6-902P . . . RNA, U6 small nuclear 902, pseudogene . . . . . . . . . . . RNU6-903P . . . RNA, U6 small nuclear 903, pseudogene . . . . . . . . . . . RNU6-904P . . . RNA, U6 small nuclear 904, pseudogene . . . . . . . . . . . RNU6-905P . . . RNA, U6 small nuclear 905, pseudogene . . . . . . . . . . . RNU6-906P . . . RNA, U6 small nuclear 906, pseudogene . . . . . . . . . . . RNU6-907P . . . RNA, U6 small nuclear 907, pseudogene . . . . . . . . . . . RNU6-908P . . . RNA, U6 small nuclear 908, pseudogene . . . . . . . . . . . RNU6-909P . . . RNA, U6 small nuclear 909, pseudogene . . . . . . . . . . . RNU6-910P . . . RNA, U6 small nuclear 910, pseudogene . . . . . . . . . . . RNU6-911P . . . RNA, U6 small nuclear 911, pseudogene . . . . . . . . . . . RNU6-912P . . . RNA, U6 small nuclear 912, pseudogene . . . . . . . . . . . RNU6-913P . . . RNA, U6 small nuclear 913, pseudogene . . . . . . . . . . . RNU6-914P . . . RNA, U6 small nuclear 914, pseudogene . . . . . . . . . . . RNU6-915P . . . RNA, U6 small nuclear 915, pseudogene . . . . . . . . . . . RNU6-916P . . . RNA, U6 small nuclear 916, pseudogene . . . . . . . . . . . RNU6-917P . . . RNA, U6 small nuclear 917, pseudogene . . . . . . . . . . . RNU6-918P . . . RNA, U6 small nuclear 918, pseudogene . . . . . . . . . . . RNU6-919P . . . RNA, U6 small nuclear 919, pseudogene . . . . . . . . . . . RNU6-920P . . . RNA, U6 small nuclear 920, pseudogene . . . . . . . . . . . RNU6-921P . . . RNA, U6 small nuclear 921, pseudogene . . . . . . . . . . . RNU6-922P . . . RNA, U6 small nuclear 922, pseudogene . . . . . . . . . . . RNU6-923P . . . RNA, U6 small nuclear 923, pseudogene . . . . . . . . . . . RNU6-924P . . . RNA, U6 small nuclear 924, pseudogene . . . . . . . . . . . RNU6-925P . . . RNA, U6 small nuclear 925, pseudogene . . . . . . . . . . . RNU6-926P . . . RNA, U6 small nuclear 926, pseudogene . . . . . . . . . . . RNU6-927P . . . RNA, U6 small nuclear 927, pseudogene . . . . . . . . . . . RNU6-928P . . . RNA, U6 small nuclear 928, pseudogene . . . . . . . . . . . RNU6-929P . . . RNA, U6 small nuclear 929, pseudogene . . . . . . . . . . . RNU6-930P . . . RNA, U6 small nuclear 930, pseudogene . . . . . . . . . . . RNU6-931P . . . RNA, U6 small nuclear 931, pseudogene . . . . . . . . . . . RNU6-932P . . . RNA, U6 small nuclear 932, pseudogene . . . . . . . . . . . RNU6-933P . . . RNA, U6 small nuclear 933, pseudogene . . . . . . . . . . . RNU6-934P . . . RNA, U6 small nuclear 934, pseudogene . . . . . . . . . . . RNU6-935P . . . RNA, U6 small nuclear 935, pseudogene . . . . . . . . . . . RNU6-936P . . . RNA, U6 small nuclear 936, pseudogene . . . . . . . . . . . RNU6-937P . . . RNA, U6 small nuclear 937, pseudogene . . . . . . . . . . . RNU6-938P . . . RNA, U6 small nuclear 938, pseudogene . . . . . . . . . . . RNU6-939P . . . RNA, U6 small nuclear 939, pseudogene . . . . . . . . . . . RNU6-940P . . . RNA, U6 small nuclear 940, pseudogene . . . . . . . . . . . RNU6-941P . . . RNA, U6 small nuclear 941, pseudogene . . . . . . . . . . . RNU6-942P . . . RNA, U6 small nuclear 942, pseudogene . . . . . . . . . . . RNU6-943P . . . RNA, U6 small nuclear 943, pseudogene . . . . . . . . . . . RNU6-944P . . . RNA, U6 small nuclear 944, pseudogene . . . . . . . . . . . RNU6-945P . . . RNA, U6 small nuclear 945, pseudogene . . . . . . . . . . . RNU6-946P . . . RNA, U6 small nuclear 946, pseudogene . . . . . . . . . . . RNU6-947P . . . RNA, U6 small nuclear 947, pseudogene . . . . . . . . . . . RNU6-948P . . . RNA, U6 small nuclear 948, pseudogene . . . . . . . . . . . RNU6-949P . . . RNA, U6 small nuclear 949, pseudogene . . . . . . . . . . . RNU6-950P . . . RNA, U6 small nuclear 950, pseudogene . . . . . . . . . . . RNU6-951P . . . RNA, U6 small nuclear 951, pseudogene . . . . . . . . . . . RNU6-952P . . . RNA, U6 small nuclear 952, pseudogene . . . . . . . . . . . RNU6-953P . . . RNA, U6 small nuclear 953, pseudogene . . . . . . . . . . . RNU6-954P . . . RNA, U6 small nuclear 954, pseudogene . . . . . . . . . . . RNU6-955P . . . RNA, U6 small nuclear 955, pseudogene . . . . . . . . . . . RNU6-956P . . . RNA, U6 small nuclear 956, pseudogene . . . . . . . . . . . RNU6-957P . . . RNA, U6 small nuclear 957, pseudogene . . . . . . . . . . . RNU6-958P . . . RNA, U6 small nuclear 958, pseudogene . . . . . . . . . . . RNU6-959P . . . RNA, U6 small nuclear 959, pseudogene . . . . . . . . . . . RNU6-960P . . . RNA, U6 small nuclear 960, pseudogene . . . . . . . . . . . RNU6-961P . . . RNA, U6 small nuclear 961, pseudogene . . . . . . . . . . . RNU6-964P . . . RNA, U6 small nuclear 964, pseudogene . . . . . . . . . . . RNU6-965P . . . RNA, U6 small nuclear 965, pseudogene . . . . . . . . . . . RNU6-966P . . . RNA, U6 small nuclear 966, pseudogene . . . . . . . . . . . RNU6-967P . . . RNA, U6 small nuclear 967, pseudogene . . . . . . . . . . . RNU6-968P . . . RNA, U6 small nuclear 968, pseudogene . . . . . . . . . . . RNU6-969P . . . RNA, U6 small nuclear 969, pseudogene . . . . . . . . . . . RNU6-970P . . . RNA, U6 small nuclear 970, pseudogene . . . . . . . . . . . RNU6-971P . . . RNA, U6 small nuclear 971, pseudogene . . . . . . . . . . . RNU6-972P . . . RNA, U6 small nuclear 972, pseudogene . . . . . . . . . . . RNU6-973P . . . RNA, U6 small nuclear 973, pseudogene . . . . . . . . . . . RNU6-974P . . . RNA, U6 small nuclear 974, pseudogene . . . . . . . . . . . RNU6-975P . . . RNA, U6 small nuclear 975, pseudogene . . . . . . . . . . . RNU6-976P . . . RNA, U6 small nuclear 976, pseudogene . . . . . . . . . . . RNU6-977P . . . RNA, U6 small nuclear 977, pseudogene . . . . . . . . . . . RNU6-978P . . . RNA, U6 small nuclear 978, pseudogene . . . . . . . . . . . RNU6-979P . . . RNA, U6 small nuclear 979, pseudogene . . . . . . . . . . . RNU6-980P . . . RNA, U6 small nuclear 980, pseudogene . . . . . . . . . . . RNU6-981P . . . RNA, U6 small nuclear 981, pseudogene . . . . . . . . . . . RNU6-982P . . . RNA, U6 small nuclear 982, pseudogene . . . . . . . . . . . RNU6-983P . . . RNA, U6 small nuclear 983, pseudogene . . . . . . . . . . . RNU6-984P . . . RNA, U6 small nuclear 984, pseudogene . . . . . . . . . . . RNU6-985P . . . RNA, U6 small nuclear 985, pseudogene . . . . . . . . . . . RNU6-986P . . . RNA, U6 small nuclear 986, pseudogene . . . . . . . . . . . RNU6-987P . . . RNA, U6 small nuclear 987, pseudogene . . . . . . . . . . . RNU6-988P . . . RNA, U6 small nuclear 988, pseudogene . . . . . . . . . . . RNU6-989P . . . RNA, U6 small nuclear 989, pseudogene . . . . . . . . . . . RNU6-990P . . . RNA, U6 small nuclear 990, pseudogene . . . . . . . . . . . RNU6-991P . . . RNA, U6 small nuclear 991, pseudogene . . . . . . . . . . . RNU6-992P . . . RNA, U6 small nuclear 992, pseudogene . . . . . . . . . . . RNU6-993P . . . RNA, U6 small nuclear 993, pseudogene . . . . . . . . . . . RNU6-994P . . . RNA, U6 small nuclear 994, pseudogene . . . . . . . . . . . RNU6-995P . . . RNA, U6 small nuclear 995, pseudogene . . . . . . . . . . . RNU6-996P . . . RNA, U6 small nuclear 996, pseudogene . . . . . . . . . . . RNU6-997P . . . RNA, U6 small nuclear 997, pseudogene . . . . . . . . . . . RNU6-998P . . . RNA, U6 small nuclear 998, pseudogene . . . . . . . . . . . RNU6-999P . . . RNA, U6 small nuclear 999, pseudogene . . . . . . . . . . . RNU6-1000P . . . RNA, U6 small nuclear 1000, pseudogene . . . . . . . . . . . RNU6-1001P . . . RNA, U6 small nuclear 1001, pseudogene . . . . . . . . . . . RNU6-1003P . . . RNA, U6 small nuclear 1003, pseudogene . . . . . . . . . . . RNU6-1004P . . . RNA, U6 small nuclear 1004, pseudogene . . . . . . . . . . . RNU6-1005P . . . RNA, U6 small nuclear 1005, pseudogene . . . . . . . . . . . RNU6-1006P . . . RNA, U6 small nuclear 1006, pseudogene . . . . . . . . . . . RNU6-1007P . . . RNA, U6 small nuclear 1007, pseudogene . . . . . . . . . . . RNU6-1008P . . . RNA, U6 small nuclear 1008, pseudogene . . . . . . . . . . . RNU6-1009P . . . RNA, U6 small nuclear 1009, pseudogene . . . . . . . . . . . RNU6-1010P . . . RNA, U6 small nuclear 1010, pseudogene . . . . . . . . . . . RNU6-1011P . . . RNA, U6 small nuclear 1011, pseudogene . . . . . . . . . . . RNU6-1012P . . . RNA, U6 small nuclear 1012, pseudogene . . . . . . . . . . . RNU6-1013P . . . RNA, U6 small nuclear 1013, pseudogene . . . . . . . . . . . RNU6-1014P . . . RNA, U6 small nuclear 1014, pseudogene . . . . . . . . . . . RNU6-1015P . . . RNA, U6 small nuclear 1015, pseudogene . . . . . . . . . . . RNU6-1016P . . . RNA, U6 small nuclear 1016, pseudogene . . . . . . . . . . . RNU6-1017P . . . RNA, U6 small nuclear 1017, pseudogene . . . . . . . . . . . RNU6-1018P . . . RNA, U6 small nuclear 1018, pseudogene . . . . . . . . . . . RNU6-1019P . . . RNA, U6 small nuclear 1019, pseudogene . . . . . . . . . . . RNU6-1020P . . . RNA, U6 small nuclear 1020, pseudogene . . . . . . . . . . . RNU6-1021P . . . RNA, U6 small nuclear 1021, pseudogene . . . . . . . . . . . RNU6-1022P . . . RNA, U6 small nuclear 1022, pseudogene . . . . . . . . . . . RNU6-1023P . . . RNA, U6 small nuclear 1023, pseudogene . . . . . . . . . . . RNU6-1024P . . . RNA, U6 small nuclear 1024, pseudogene . . . . . . . . . . . RNU6-1025P . . . RNA, U6 small nuclear 1025, pseudogene . . . . . . . . . . . RNU6-1026P . . . RNA, U6 small nuclear 1026, pseudogene . . . . . . . . . . . RNU6-1027P . . . RNA, U6 small nuclear 1027, pseudogene . . . . . . . . . . . RNU6-1028P . . . RNA, U6 small nuclear 1028, pseudogene . . . . . . . . . . . RNU6-1029P . . . RNA, U6 small nuclear 1029, pseudogene . . . . . . . . . . . RNU6-1031P . . . RNA, U6 small nuclear 1031, pseudogene . . . . . . . . . . . RNU6-1032P . . . RNA, U6 small nuclear 1032, pseudogene . . . . . . . . . . . RNU6-1034P . . . RNA, U6 small nuclear 1034, pseudogene . . . . . . . . . . . RNU6-1035P . . . RNA, U6 small nuclear 1035, pseudogene . . . . . . . . . . . RNU6-1036P . . . RNA, U6 small nuclear 1036, pseudogene . . . . . . . . . . . RNU6-1037P . . . RNA, U6 small nuclear 1037, pseudogene . . . . . . . . . . . RNU6-1038P . . . RNA, U6 small nuclear 1038, pseudogene . . . . . . . . . . . RNU6-1039P . . . RNA, U6 small nuclear 1039, pseudogene . . . . . . . . . . . RNU6-1040P . . . RNA, U6 small nuclear 1040, pseudogene . . . . . . . . . . . RNU6-1041P . . . RNA, U6 small nuclear 1041, pseudogene . . . . . . . . . . . RNU6-1042P . . . RNA, U6 small nuclear 1042, pseudogene . . . . . . . . . . . RNU6-1043P . . . RNA, U6 small nuclear 1043, pseudogene . . . . . . . . . . . RNU6-1044P . . . RNA, U6 small nuclear 1044, pseudogene . . . . . . . . . . . RNU6-1045P . . . RNA, U6 small nuclear 1045, pseudogene . . . . . . . . . . . RNU6-1046P . . . RNA, U6 small nuclear 1046, pseudogene . . . . . . . . . . . RNU6-1047P . . . RNA, U6 small nuclear 1047, pseudogene . . . . . . . . . . . RNU6-1048P . . . RNA, U6 small nuclear 1048, pseudogene . . . . . . . . . . . RNU6-1049P . . . RNA, U6 small nuclear 1049, pseudogene . . . . . . . . . . . RNU6-1050P . . . RNA, U6 small nuclear 1050, pseudogene . . . . . . . . . . . RNU6-1051P . . . RNA, U6 small nuclear 1051, pseudogene . . . . . . . . . . . RNU6-1052P . . . RNA, U6 small nuclear 1052, pseudogene . . . . . . . . . . . RNU6-1053P . . . RNA, U6 small nuclear 1053, pseudogene . . . . . . . . . . . RNU6-1054P . . . RNA, U6 small nuclear 1054, pseudogene . . . . . . . . . . . RNU6-1055P . . . RNA, U6 small nuclear 1055, pseudogene . . . . . . . . . . . RNU6-1056P . . . RNA, U6 small nuclear 1056, pseudogene . . . . . . . . . . . RNU6-1057P . . . RNA, U6 small nuclear 1057, pseudogene . . . . . . . . . . . RNU6-1059P . . . RNA, U6 small nuclear 1059, pseudogene . . . . . . . . . . . RNU6-1060P . . . RNA, U6 small nuclear 1060, pseudogene . . . . . . . . . . . RNU6-1061P . . . RNA, U6 small nuclear 1061, pseudogene . . . . . . . . . . . RNU6-1062P . . . RNA, U6 small nuclear 1062, pseudogene . . . . . . . . . . . RNU6-1064P . . . RNA, U6 small nuclear 1064, pseudogene . . . . . . . . . . . RNU6-1065P . . . RNA, U6 small nuclear 1065, pseudogene . . . . . . . . . . . RNU6-1066P . . . RNA, U6 small nuclear 1066, pseudogene . . . . . . . . . . . RNU6-1067P . . . RNA, U6 small nuclear 1067, pseudogene . . . . . . . . . . . RNU6-1068P . . . RNA, U6 small nuclear 1068, pseudogene . . . . . . . . . . . RNU6-1069P . . . RNA, U6 small nuclear 1069, pseudogene . . . . . . . . . . . RNU6-1071P . . . RNA, U6 small nuclear 1071, pseudogene . . . . . . . . . . . RNU6-1072P . . . RNA, U6 small nuclear 1072, pseudogene . . . . . . . . . . . RNU6-1073P . . . RNA, U6 small nuclear 1073, pseudogene . . . . . . . . . . . RNU6-1074P . . . RNA, U6 small nuclear 1074, pseudogene . . . . . . . . . . . RNU6-1075P . . . RNA, U6 small nuclear 1075, pseudogene . . . . . . . . . . . RNU6-1076P . . . RNA, U6 small nuclear 1076, pseudogene . . . . . . . . . . . RNU6-1077P . . . RNA, U6 small nuclear 1077, pseudogene . . . . . . . . . . . RNU6-1078P . . . RNA, U6 small nuclear 1078, pseudogene . . . . . . . . . . . RNU6-1079P . . . RNA, U6 small nuclear 1079, pseudogene . . . . . . . . . . . RNU6-1080P . . . RNA, U6 small nuclear 1080, pseudogene . . . . . . . . . . . RNU6-1081P . . . RNA, U6 small nuclear 1081, pseudogene . . . . . . . . . . . RNU6-1082P . . . RNA, U6 small nuclear 1082, pseudogene . . . . . . . . . . . RNU6-1083P . . . RNA, U6 small nuclear 1083, pseudogene . . . . . . . . . . . RNU6-1084P . . . RNA, U6 small nuclear 1084, pseudogene . . . . . . . . . . . RNU6-1085P . . . RNA, U6 small nuclear 1085, pseudogene . . . . . . . . . . . RNU6-1086P . . . RNA, U6 small nuclear 1086, pseudogene . . . . . . . . . . . RNU6-1087P . . . RNA, U6 small nuclear 1087, pseudogene . . . . . . . . . . . RNU6-1088P . . . RNA, U6 small nuclear 1088, pseudogene . . . . . . . . . . . RNU6-1089P . . . RNA, U6 small nuclear 1089, pseudogene . . . . . . . . . . . RNU6-1090P . . . RNA, U6 small nuclear 1090, pseudogene . . . . . . . . . . . RNU6-1091P . . . RNA, U6 small nuclear 1091, pseudogene . . . . . . . . . . . RNU6-1092P . . . RNA, U6 small nuclear 1092, pseudogene . . . . . . . . . . . RNU6-1093P . . . RNA, U6 small nuclear 1093, pseudogene . . . . . . . . . . . RNU6-1094P . . . RNA, U6 small nuclear 1094, pseudogene . . . . . . . . . . . RNU6-1095P . . . RNA, U6 small nuclear 1095, pseudogene . . . . . . . . . . . RNU6-1096P . . . RNA, U6 small nuclear 1096, pseudogene . . . . . . . . . . . RNU6-1097P . . . RNA, U6 small nuclear 1097, pseudogene . . . . . . . . . . . RNU6-1098P . . . RNA, U6 small nuclear 1098, pseudogene . . . . . . . . . . . RNU6-1099P . . . RNA, U6 small nuclear 1099, pseudogene . . . . . . . . . . . RNU6-1100P . . . RNA, U6 small nuclear 1100, pseudogene . . . . . . . . . . . RNU6-1101P . . . RNA, U6 small nuclear 1101, pseudogene . . . . . . . . . . . RNU6-1102P . . . RNA, U6 small nuclear 1102, pseudogene . . . . . . . . . . . RNU6-1103P . . . RNA, U6 small nuclear 1103, pseudogene . . . . . . . . . . . RNU6-1104P . . . RNA, U6 small nuclear 1104, pseudogene . . . . . . . . . . . RNU6-1105P . . . RNA, U6 small nuclear 1105, pseudogene . . . . . . . . . . . RNU6-1106P . . . RNA, U6 small nuclear 1106, pseudogene . . . . . . . . . . . RNU6-1107P . . . RNA, U6 small nuclear 1107, pseudogene . . . . . . . . . . . RNU6-1108P . . . RNA, U6 small nuclear 1108, pseudogene . . . . . . . . . . . RNU6-1109P . . . RNA, U6 small nuclear 1109, pseudogene . . . . . . . . . . . RNU6-1110P . . . RNA, U6 small nuclear 1110, pseudogene . . . . . . . . . . . RNU6-1111P . . . RNA, U6 small nuclear 1111, pseudogene . . . . . . . . . . . RNU6-1112P . . . RNA, U6 small nuclear 1112, pseudogene . . . . . . . . . . . RNU6-1113P . . . RNA, U6 small nuclear 1113, pseudogene . . . . . . . . . . . RNU6-1114P . . . RNA, U6 small nuclear 1114, pseudogene . . . . . . . . . . . RNU6-1115P . . . RNA, U6 small nuclear 1115, pseudogene . . . . . . . . . . . RNU6-1116P . . . RNA, U6 small nuclear 1116, pseudogene . . . . . . . . . . . RNU6-1117P . . . RNA, U6 small nuclear 1117, pseudogene . . . . . . . . . . . RNU6-1118P . . . RNA, U6 small nuclear 1118, pseudogene . . . . . . . . . . . RNU6-1119P . . . RNA, U6 small nuclear 1119, pseudogene . . . . . . . . . . . RNU6-1120P . . . RNA, U6 small nuclear 1120, pseudogene . . . . . . . . . . . RNU6-1121P . . . RNA, U6 small nuclear 1121, pseudogene . . . . . . . . . . . RNU6-1122P . . . RNA, U6 small nuclear 1122, pseudogene . . . . . . . . . . . RNU6-1123P . . . RNA, U6 small nuclear 1123, pseudogene . . . . . . . . . . . RNU6-1124P . . . RNA, U6 small nuclear 1124, pseudogene . . . . . . . . . . . RNU6-1125P . . . RNA, U6 small nuclear 1125, pseudogene . . . . . . . . . . . RNU6-1126P . . . RNA, U6 small nuclear 1126, pseudogene . . . . . . . . . . . RNU6-1127P . . . RNA, U6 small nuclear 1127, pseudogene . . . . . . . . . . . RNU6-1128P . . . RNA, U6 small nuclear 1128, pseudogene . . . . . . . . . . . RNU6-1129P . . . RNA, U6 small nuclear 1129, pseudogene . . . . . . . . . . . RNU6-1130P . . . RNA, U6 small nuclear 1130, pseudogene . . . . . . . . . . . RNU6-1131P . . . RNA, U6 small nuclear 1131, pseudogene . . . . . . . . . . . RNU6-1132P . . . RNA, U6 small nuclear 1132, pseudogene . . . . . . . . . . . RNU6-1133P . . . RNA, U6 small nuclear 1133, pseudogene . . . . . . . . . . . RNU6-1134P . . . RNA, U6 small nuclear 1134, pseudogene . . . . . . . . . . . RNU6-1135P . . . RNA, U6 small nuclear 1135, pseudogene . . . . . . . . . . . RNU6-1136P . . . RNA, U6 small nuclear 1136, pseudogene . . . . . . . . . . . RNU6-1137P . . . RNA, U6 small nuclear 1137, pseudogene . . . . . . . . . . . RNU6-1138P . . . RNA, U6 small nuclear 1138, pseudogene . . . . . . . . . . . RNU6-1139P . . . RNA, U6 small nuclear 1139, pseudogene . . . . . . . . . . . RNU6-1140P . . . RNA, U6 small nuclear 1140, pseudogene . . . . . . . . . . . RNU6-1141P . . . RNA, U6 small nuclear 1141, pseudogene . . . . . . . . . . . RNU6-1143P . . . RNA, U6 small nuclear 1143, pseudogene . . . . . . . . . . . RNU6-1144P . . . RNA, U6 small nuclear 1144, pseudogene . . . . . . . . . . . RNU6-1145P . . . RNA, U6 small nuclear 1145, pseudogene . . . . . . . . . . . RNU6-1146P . . . RNA, U6 small nuclear 1146, pseudogene . . . . . . . . . . . RNU6-1147P . . . RNA, U6 small nuclear 1147, pseudogene . . . . . . . . . . . RNU6-1148P . . . RNA, U6 small nuclear 1148, pseudogene . . . . . . . . . . . RNU6-1149P . . . RNA, U6 small nuclear 1149, pseudogene . . . . . . . . . . . RNU6-1150P . . . RNA, U6 small nuclear 1150, pseudogene . . . . . . . . . . . RNU6-1151P . . . RNA, U6 small nuclear 1151, pseudogene . . . . . . . . . . . RNU6-1152P . . . RNA, U6 small nuclear 1152, pseudogene . . . . . . . . . . . RNU6-1153P . . . RNA, U6 small nuclear 1153, pseudogene . . . . . . . . . . . RNU6-1154P . . . RNA, U6 small nuclear 1154, pseudogene . . . . . . . . . . . RNU6-1155P . . . RNA, U6 small nuclear 1155, pseudogene . . . . . . . . . . . RNU6-1156P . . . RNA, U6 small nuclear 1156, pseudogene . . . . . . . . . . . RNU6-1157P . . . RNA, U6 small nuclear 1157, pseudogene . . . . . . . . . . . RNU6-1158P . . . RNA, U6 small nuclear 1158, pseudogene . . . . . . . . . . . RNU6-1159P . . . RNA, U6 small nuclear 1159, pseudogene . . . . . . . . . . . RNU6-1160P . . . RNA, U6 small nuclear 1160, pseudogene . . . . . . . . . . . RNU6-1161P . . . RNA, U6 small nuclear 1161, pseudogene . . . . . . . . . . . RNU6-1162P . . . RNA, U6 small nuclear 1162, pseudogene . . . . . . . . . . . RNU6-1163P . . . RNA, U6 small nuclear 1163, pseudogene . . . . . . . . . . . RNU6-1164P . . . RNA, U6 small nuclear 1164, pseudogene . . . . . . . . . . . RNU6-1165P . . . RNA, U6 small nuclear 1165, pseudogene . . . . . . . . . . . RNU6-1167P . . . RNA, U6 small nuclear 1167, pseudogene . . . . . . . . . . . RNU6-1168P . . . RNA, U6 small nuclear 1168, pseudogene . . . . . . . . . . . RNU6-1169P . . . RNA, U6 small nuclear 1169, pseudogene . . . . . . . . . . . RNU6-1170P . . . RNA, U6 small nuclear 1170, pseudogene . . . . . . . . . . . RNU6-1171P . . . RNA, U6 small nuclear 1171, pseudogene . . . . . . . . . . . RNU6-1172P . . . RNA, U6 small nuclear 1172, pseudogene . . . . . . . . . . . RNU6-1174P . . . RNA, U6 small nuclear 1174, pseudogene . . . . . . . . . . . RNU6-1175P . . . RNA, U6 small nuclear 1175, pseudogene . . . . . . . . . . . RNU6-1176P . . . RNA, U6 small nuclear 1176, pseudogene . . . . . . . . . . . RNU6-1177P . . . RNA, U6 small nuclear 1177, pseudogene . . . . . . . . . . . RNU6-1178P . . . RNA, U6 small nuclear 1178, pseudogene . . . . . . . . . . . RNU6-1179P . . . RNA, U6 small nuclear 1179, pseudogene . . . . . . . . . . . RNU6-1180P . . . RNA, U6 small nuclear 1180, pseudogene . . . . . . . . . . . RNU6-1181P . . . RNA, U6 small nuclear 1181, pseudogene . . . . . . . . . . . RNU6-1183P . . . RNA, U6 small nuclear 1183, pseudogene . . . . . . . . . . . RNU6-1184P . . . RNA, U6 small nuclear 1184, pseudogene . . . . . . . . . . . RNU6-1186P . . . RNA, U6 small nuclear 1186, pseudogene . . . . . . . . . . . RNU6-1187P . . . RNA, U6 small nuclear 1187, pseudogene . . . . . . . . . . . RNU6-1188P . . . RNA, U6 small nuclear 1188, pseudogene . . . . . . . . . . . RNU6-1189P . . . RNA, U6 small nuclear 1189, pseudogene . . . . . . . . . . . RNU6-1190P . . . RNA, U6 small nuclear 1190, pseudogene . . . . . . . . . . . RNU6-1191P . . . RNA, U6 small nuclear 1191, pseudogene . . . . . . . . . . . RNU6-1192P . . . RNA, U6 small nuclear 1192, pseudogene . . . . . . . . . . . RNU6-1193P . . . RNA, U6 small nuclear 1193, pseudogene . . . . . . . . . . . RNU6-1194P . . . RNA, U6 small nuclear 1194, pseudogene . . . . . . . . . . . RNU6-1195P . . . RNA, U6 small nuclear 1195, pseudogene . . . . . . . . . . . RNU6-1196P . . . RNA, U6 small nuclear 1196, pseudogene . . . . . . . . . . . RNU6-1197P . . . RNA, U6 small nuclear 1197, pseudogene . . . . . . . . . . . RNU6-1198P . . . RNA, U6 small nuclear 1198, pseudogene . . . . . . . . . . . RNU6-1199P . . . RNA, U6 small nuclear 1199, pseudogene . . . . . . . . . . . RNU6-1200P . . . RNA, U6 small nuclear 1200, pseudogene . . . . . . . . . . . RNU6-1201P . . . RNA, U6 small nuclear 1201, pseudogene . . . . . . . . . . . RNU6-1203P . . . RNA, U6 small nuclear 1203, pseudogene . . . . . . . . . . . RNU6-1204P . . . RNA, U6 small nuclear 1204, pseudogene . . . . . . . . . . . RNU6-1205P . . . RNA, U6 small nuclear 1205, pseudogene . . . . . . . . . . . RNU6-1206P . . . RNA, U6 small nuclear 1206, pseudogene . . . . . . . . . . . RNU6-1207P . . . RNA, U6 small nuclear 1207, pseudogene . . . . . . . . . . . RNU6-1208P . . . RNA, U6 small nuclear 1208, pseudogene . . . . . . . . . . . RNU6-1209P . . . RNA, U6 small nuclear 1209, pseudogene . . . . . . . . . . . RNU6-1210P . . . RNA, U6 small nuclear 1210, pseudogene . . . . . . . . . . . RNU6-1211P . . . RNA, U6 small nuclear 1211, pseudogene . . . . . . . . . . . RNU6-1212P . . . RNA, U6 small nuclear 1212, pseudogene . . . . . . . . . . . RNU6-1213P . . . RNA, U6 small nuclear 1213, pseudogene . . . . . . . . . . . RNU6-1214P . . . RNA, U6 small nuclear 1214, pseudogene . . . . . . . . . . . RNU6-1215P . . . RNA, U6 small nuclear 1215, pseudogene . . . . . . . . . . . RNU6-1216P . . . RNA, U6 small nuclear 1216, pseudogene . . . . . . . . . . . RNU6-1217P . . . RNA, U6 small nuclear 1217, pseudogene . . . . . . . . . . . RNU6-1218P . . . RNA, U6 small nuclear 1218, pseudogene . . . . . . . . . . . RNU6-1219P . . . RNA, U6 small nuclear 1219, pseudogene . . . . . . . . . . . RNU6-1220P . . . RNA, U6 small nuclear 1220, pseudogene . . . . . . . . . . . RNU6-1222P . . . RNA, U6 small nuclear 1222, pseudogene . . . . . . . . . . . RNU6-1223P . . . RNA, U6 small nuclear 1223, pseudogene . . . . . . . . . . . RNU6-1224P . . . RNA, U6 small nuclear 1224, pseudogene . . . . . . . . . . . RNU6-1225P . . . RNA, U6 small nuclear 1225, pseudogene . . . . . . . . . . . RNU6-1226P . . . RNA, U6 small nuclear 1226, pseudogene . . . . . . . . . . . RNU6-1227P . . . RNA, U6 small nuclear 1227, pseudogene . . . . . . . . . . . RNU6-1228P . . . RNA, U6 small nuclear 1228, pseudogene . . . . . . . . . . . RNU6-1229P . . . RNA, U6 small nuclear 1229, pseudogene . . . . . . . . . . . RNU6-1230P . . . RNA, U6 small nuclear 1230, pseudogene . . . . . . . . . . . RNU6-1231P . . . RNA, U6 small nuclear 1231, pseudogene . . . . . . . . . . . RNU6-1232P . . . RNA, U6 small nuclear 1232, pseudogene . . . . . . . . . . . RNU6-1233P . . . RNA, U6 small nuclear 1233, pseudogene . . . . . . . . . . . RNU6-1234P . . . RNA, U6 small nuclear 1234, pseudogene . . . . . . . . . . . RNU6-1235P . . . RNA, U6 small nuclear 1235, pseudogene . . . . . . . . . . . RNU6-1236P . . . RNA, U6 small nuclear 1236, pseudogene . . . . . . . . . . . RNU6-1237P . . . RNA, U6 small nuclear 1237, pseudogene . . . . . . . . . . . RNU6-1238P . . . RNA, U6 small nuclear 1238, pseudogene . . . . . . . . . . . RNU6-1239P . . . RNA, U6 small nuclear 1239, pseudogene . . . . . . . . . . . RNU6-1240P . . . RNA, U6 small nuclear 1240, pseudogene . . . . . . . . . . . RNU6-1241P . . . RNA, U6 small nuclear 1241, pseudogene . . . . . . . . . . . RNU6-1242P . . . RNA, U6 small nuclear 1242, pseudogene . . . . . . . . . . . RNU6-1243P . . . RNA, U6 small nuclear 1243, pseudogene . . . . . . . . . . . RNU6-1244P . . . RNA, U6 small nuclear 1244, pseudogene . . . . . . . . . . . RNU6-1245P . . . RNA, U6 small nuclear 1245, pseudogene . . . . . . . . . . . RNU6-1246P . . . RNA, U6 small nuclear 1246, pseudogene . . . . . . . . . . . RNU6-1247P . . . RNA, U6 small nuclear 1247, pseudogene . . . . . . . . . . . RNU6-1248P . . . RNA, U6 small nuclear 1248, pseudogene . . . . . . . . . . . RNU6-1249P . . . RNA, U6 small nuclear 1249, pseudogene . . . . . . . . . . . RNU6-1250P . . . RNA, U6 small nuclear 1250, pseudogene . . . . . . . . . . . RNU6-1251P . . . RNA, U6 small nuclear 1251, pseudogene . . . . . . . . . . . RNU6-1252P . . . RNA, U6 small nuclear 1252, pseudogene . . . . . . . . . . . RNU6-1254P . . . RNA, U6 small nuclear 1254, pseudogene . . . . . . . . . . . RNU6-1255P . . . RNA, U6 small nuclear 1255, pseudogene . . . . . . . . . . . RNU6-1256P . . . RNA, U6 small nuclear 1256, pseudogene . . . . . . . . . . . RNU6-1257P . . . RNA, U6 small nuclear 1257, pseudogene . . . . . . . . . . . RNU6-1258P . . . RNA, U6 small nuclear 1258, pseudogene . . . . . . . . . . . RNU6-1260P . . . RNA, U6 small nuclear 1260, pseudogene . . . . . . . . . . . RNU6-1261P . . . RNA, U6 small nuclear 1261, pseudogene . . . . . . . . . . . RNU6-1262P . . . RNA, U6 small nuclear 1262, pseudogene . . . . . . . . . . . RNU6-1263P . . . RNA, U6 small nuclear 1263, pseudogene . . . . . . . . . . . RNU6-1264P . . . RNA, U6 small nuclear 1264, pseudogene . . . . . . . . . . . RNU6-1265P . . . RNA, U6 small nuclear 1265, pseudogene . . . . . . . . . . . RNU6-1266P . . . RNA, U6 small nuclear 1266, pseudogene . . . . . . . . . . . RNU6-1267P . . . RNA, U6 small nuclear 1267, pseudogene . . . . . . . . . . . RNU6-1268P . . . RNA, U6 small nuclear 1268, pseudogene . . . . . . . . . . . RNU6-1269P . . . RNA, U6 small nuclear 1269, pseudogene . . . . . . . . . . . RNU6-1270P . . . RNA, U6 small nuclear 1270, pseudogene . . . . . . . . . . . RNU6-1271P . . . RNA, U6 small nuclear 1271, pseudogene . . . . . . . . . . . RNU6-1272P . . . RNA, U6 small nuclear 1272, pseudogene . . . . . . . . . . . RNU6-1273P . . . RNA, U6 small nuclear 1273, pseudogene . . . . . . . . . . . RNU6-1274P . . . RNA, U6 small nuclear 1274, pseudogene . . . . . . . . . . . RNU6-1275P . . . RNA, U6 small nuclear 1275, pseudogene . . . . . . . . . . . RNU6-1276P . . . RNA, U6 small nuclear 1276, pseudogene . . . . . . . . . . . RNU6-1277P . . . RNA, U6 small nuclear 1277, pseudogene . . . . . . . . . . . RNU6-1278P . . . RNA, U6 small nuclear 1278, pseudogene . . . . . . . . . . . RNU6-1279P . . . RNA, U6 small nuclear 1279, pseudogene . . . . . . . . . . . RNU6-1280P . . . RNA, U6 small nuclear 1280, pseudogene . . . . . . . . . . . RNU6-1281P . . . RNA, U6 small nuclear 1281, pseudogene . . . . . . . . . . . RNU6-1282P . . . RNA, U6 small nuclear 1282, pseudogene . . . . . . . . . . . RNU6-1283P . . . RNA, U6 small nuclear 1283, pseudogene . . . . . . . . . . . RNU6-1284P . . . RNA, U6 small nuclear 1284, pseudogene . . . . . . . . . . . RNU6-1285P . . . RNA, U6 small nuclear 1285, pseudogene . . . . . . . . . . . RNU6-1286P . . . RNA, U6 small nuclear 1286, pseudogene . . . . . . . . . . . RNU6-1287P . . . RNA, U6 small nuclear 1287, pseudogene . . . . . . . . . . . RNU6-1288P . . . RNA, U6 small nuclear 1288, pseudogene . . . . . . . . . . . RNU6-1289P . . . RNA, U6 small nuclear 1289, pseudogene . . . . . . . . . . . RNU6-1290P . . . RNA, U6 small nuclear 1290, pseudogene . . . . . . . . . . . RNU6-1291P . . . RNA, U6 small nuclear 1291, pseudogene . . . . . . . . . . . RNU6-1292P . . . RNA, U6 small nuclear 1292, pseudogene . . . . . . . . . . . RNU6-1293P . . . RNA, U6 small nuclear 1293, pseudogene . . . . . . . . . . . RNU6-1294P . . . RNA, U6 small nuclear 1294, pseudogene . . . . . . . . . . . RNU6-1296P . . . RNA, U6 small nuclear 1296, pseudogene . . . . . . . . . . . RNU6-1297P . . . RNA, U6 small nuclear 1297, pseudogene . . . . . . . . . . . RNU6-1298P . . . RNA, U6 small nuclear 1298, pseudogene . . . . . . . . . . . RNU6-1299P . . . RNA, U6 small nuclear 1299, pseudogene . . . . . . . . . . . RNU6-1300P . . . RNA, U6 small nuclear 1300, pseudogene . . . . . . . . . . . RNU6-1301P . . . RNA, U6 small nuclear 1301, pseudogene . . . . . . . . . . . RNU6-1303P . . . RNA, U6 small nuclear 1303, pseudogene . . . . . . . . . . . RNU6-1304P . . . RNA, U6 small nuclear 1304, pseudogene . . . . . . . . . . . RNU6-1305P . . . RNA, U6 small nuclear 1305, pseudogene . . . . . . . . . . . RNU6-1306P . . . RNA, U6 small nuclear 1306, pseudogene . . . . . . . . . . . RNU6-1307P . . . RNA, U6 small nuclear 1307, pseudogene . . . . . . . . . . . RNU6-1308P . . . RNA, U6 small nuclear 1308, pseudogene . . . . . . . . . . . RNU6-1309P . . . RNA, U6 small nuclear 1309, pseudogene . . . . . . . . . . . RNU6-1310P . . . RNA, U6 small nuclear 1310, pseudogene . . . . . . . . . . . RNU6-1311P . . . RNA, U6 small nuclear 1311, pseudogene . . . . . . . . . . . RNU6-1312P . . . RNA, U6 small nuclear 1312, pseudogene . . . . . . . . . . . RNU6-1313P . . . RNA, U6 small nuclear 1313, pseudogene . . . . . . . . . . . RNU6-1314P . . . RNA, U6 small nuclear 1314, pseudogene . . . . . . . . . . . RNU6-1315P . . . RNA, U6 small nuclear 1315, pseudogene . . . . . . . . . . . RNU6-1316P . . . RNA, U6 small nuclear 1316, pseudogene . . . . . . . . . . . RNU6-1317P . . . RNA, U6 small nuclear 1317, pseudogene . . . . . . . . . . . RNU6-1318P . . . RNA, U6 small nuclear 1318, pseudogene . . . . . . . . . . . RNU6-1319P . . . RNA, U6 small nuclear 1319, pseudogene . . . . . . . . . . . RNU6-1320P . . . RNA, U6 small nuclear 1320, pseudogene . . . . . . . . . . . RNU6-1321P . . . RNA, U6 small nuclear 1321, pseudogene . . . . . . . . . . . RNU6-1322P . . . RNA, U6 small nuclear 1322, pseudogene . . . . . . . . . . . RNU6-1323P . . . RNA, U6 small nuclear 1323, pseudogene . . . . . . . . . . . RNU6-1324P . . . RNA, U6 small nuclear 1324, pseudogene . . . . . . . . . . . RNU6-1325P . . . RNA, U6 small nuclear 1325, pseudogene . . . . . . . . . . . RNU6-1326P . . . RNA, U6 small nuclear 1326, pseudogene . . . . . . . . . . . RNU6-1327P . . . RNA, U6 small nuclear 1327, pseudogene . . . . . . . . . . . RNU6-1328P . . . RNA, U6 small nuclear 1328, pseudogene . . . . . . . . . . . RNU6-1329P . . . RNA, U6 small nuclear 1329, pseudogene . . . . . . . . . . . RNU6-1330P . . . RNA, U6 small nuclear 1330, pseudogene . . . . . . . . . . . RNU6-1331P . . . RNA, U6 small nuclear 1331, pseudogene . . . . . . . . . . . RNU6-1332P . . . RNA, U6 small nuclear 1332, pseudogene . . . . . . . . . . . RNU6-1333P . . . RNA, U6 small nuclear 1333, pseudogene . . . . . . . . . . . RNU6-1334P . . . RNA, U6 small nuclear 1334, pseudogene . . . . . . . . . . . RNU6-1335P . . . RNA, U6 small nuclear 1335, pseudogene . . . . . . . . . . . RNU6-1336P . . . RNA, U6 small nuclear 1336, pseudogene . . . . . . . . . . . RNU6-1337P . . . RNA, U6 small nuclear 1337, pseudogene . . . . . . . . . . . RNU6-1338P . . . RNA, U6 small nuclear 1338, pseudogene . . . . . . . . . . . RNU6-1339P . . . RNA, U6 small nuclear 1339, pseudogene . . . . . . . . . . . RNU6-1340P . . . RNA, U6 small nuclear 1340, pseudogene . . . . . . . . . . . RNU6ATAC . . . RNA, U6atac small nuclear (U12-dependent splicing) . . . . . . . . . . . RNU6ATAC2P . . . RNA, U6atac small nuclear 2, pseudogene . . . . . . . . . . . RNU6ATAC3P . . . RNA, U6atac small nuclear 3, pseudogene . . . . . . . . . . . RNU6ATAC4P . . . RNA, U6atac small nuclear 4, pseudogene . . . . . . . . . . . RNU6ATAC5P . . . RNA, U6atac small nuclear 5, pseudogene . . . . . . . . . . . RNU6ATAC6P . . . RNA, U6atac small nuclear 6, pseudogene . . . . . . . . . . . RNU6ATAC7P . . . RNA, U6atac small nuclear 7, pseudogene . . . . . . . . . . . RNU6ATAC8P . . . RNA, U6atac small nuclear 8, pseudogene . . . . . . . . . . . RNU6ATAC9P . . . RNA, U6atac small nuclear 9, pseudogene . . . . . . . . . . . RNU6ATAC10P . . . RNA, U6atac small nuclear 10, pseudogene . . . . . . . . . . . RNU6ATAC11P . . . RNA, U6atac small nuclear 11, pseudogene . . . . . . . . . . . RNU6ATAC12P . . . RNA, U6atac small nuclear 12, pseudogene . . . . . . . . . . . RNU6ATAC13P . . . RNA, U6atac small nuclear 13, pseudogene . . . . . . . . . . . RNU6ATAC14P . . . RNA, U6atac small nuclear 14, pseudogene . . . . . . . . . . . RNU6ATAC15P . . . RNA, U6atac small nuclear 15, pseudogene . . . . . . . . . . . RNU6ATAC16P . . . RNA, U6atac small nuclear 16, pseudogene . . . . . . . . . . . RNU6ATAC17P . . . RNA, U6atac small nuclear 17, pseudogene . . . . . . . . . . . RNU6ATAC18P . . . RNA, U6atac small nuclear 18, pseudogene . . . . . . . . . . . RNU6ATAC19P . . . RNA, U6atac small nuclear 19, pseudogene . . . . . . . . . . . RNU6ATAC20P . . . RNA, U6atac small nuclear 20, pseudogene . . . . . . . . . . . RNU6ATAC21P . . . RNA, U6atac small nuclear 21, pseudogene . . . . . . . . . . . RNU6ATAC22P . . . RNA, U6atac small nuclear 22, pseudogene . . . . . . . . . . . RNU6ATAC23P . . . RNA, U6atac small nuclear 23, pseudogene . . . . . . . . . . . RNU6ATAC24P . . . RNA, U6atac small nuclear 24, pseudogene . . . . . . . . . . . RNU6ATAC25P . . . RNA, U6atac small nuclear 25, pseudogene . . . . . . . . . . . RNU6ATAC26P . . . RNA, U6atac small nuclear 26, pseudogene . . . . . . . . . . . RNU6ATAC27P . . . RNA, U6atac small nuclear 27, pseudogene . . . . . . . . . . . RNU6ATAC28P . . . RNA, U6atac small nuclear 28, pseudogene . . . . . . . . . . . RNU6ATAC29P . . . RNA, U6atac small nuclear 29, pseudogene . . . . . . . . . . . RNU6ATAC30P . . . RNA, U6atac small nuclear 30, pseudogene . . . . . . . . . . . RNU6ATAC31P . . . RNA, U6atac small nuclear 31, pseudogene . . . . . . . . . . . RNU6ATAC32P . . . RNA, U6atac small nuclear 32, pseudogene . . . . . . . . . . . RNU6ATAC33P . . . RNA, U6atac small nuclear 33, pseudogene . . . . . . . . . . . RNU6ATAC34P . . . RNA, U6atac small nuclear 34, pseudogene . . . . . . . . . . . RNU6ATAC35P . . . RNA, U6atac small nuclear 35, pseudogene . . . . . . . . . . . RNU6ATAC36P . . . RNA, U6atac small nuclear 36, pseudogene . . . . . . . . . . . RNU6ATAC37P . . . RNA, U6atac small nuclear 37, pseudogene . . . . . . . . . . . RNU6ATAC38P . . . RNA, U6atac small nuclear 38, pseudogene . . . . . . . . . . . RNU6ATAC39P . . . RNA, U6atac small nuclear 39, pseudogene . . . . . . . . . . . RNU6ATAC40P . . . RNA, U6atac small nuclear 40, pseudogene . . . . . . . . . . . RNU6ATAC41P . . . RNA, U6atac small nuclear 41, pseudogene . . . . . . . . . . . RNU6ATAC42P . . . RNA, U6atac small nuclear 42, pseudogene . . . . . . . . . . . RNU6V . . . RNA, U6 small nuclear variant sequence with SNRPE pseudogene sequence . . . . . . . . . . . RNU7-1 . . . RNA, U7 small nuclear 1 . . . . . . . . . . . RNU7-2P . . . RNA, U7 small nuclear 2 pseudogene . . . . . . . . . . . RNU7-3P . . . RNA, U7 small nuclear 3 pseudogene . . . . . . . . . . . RNU7-4P . . . RNA, U7 small nuclear 4 pseudogene . . . . . . . . . . . RNU7-5P . . . RNA, U7 small nuclear 5 pseudogene . . . . . . . . . . . RNU7-6P . . . RNA, U7 small nuclear 6 pseudogene . . . . . . . . . . . RNU7-7P . . . RNA, U7 small nuclear 7 pseudogene . . . . . . . . . . . RNU7-8P . . . RNA, U7 small nuclear 8 pseudogene . . . . . . . . . . . RNU7-9P . . . RNA, U7 small nuclear 9 pseudogene . . . . . . . . . . . RNU7-10P . . . RNA, U7 small nuclear 10 pseudogene . . . . . . . . . . . RNU7-11P . . . RNA, U7 small nuclear 11 pseudogene . . . . . . . . . . . RNU7-12P . . . RNA, U7 small nuclear 12 pseudogene . . . . . . . . . . . RNU7-13P . . . RNA, U7 small nuclear 13 pseudogene . . . . . . . . . . . RNU7-14P . . . RNA, U7 small nuclear 14 pseudogene . . . . . . . . . . . RNU7-15P . . . RNA, U7 small nuclear 15 pseudogene . . . . . . . . . . . RNU7-16P . . . RNA, U7 small nuclear 16 pseudogene . . . . . . . . . . . RNU7-17P . . . RNA, U7 small nuclear 17 pseudogene . . . . . . . . . . . RNU7-18P . . . RNA, U7 small nuclear 18 pseudogene . . . . . . . . . . . RNU7-19P . . . RNA, U7 small nuclear 19 pseudogene . . . . . . . . . . . RNU7-20P . . . RNA, U7 small nuclear 20 pseudogene . . . . . . . . . . . RNU7-21P . . . RNA, U7 small nuclear 21 pseudogene . . . . . . . . . . . RNU7-22P . . . RNA, U7 small nuclear 22 pseudogene . . . . . . . . . . . RNU7-23P . . . RNA, U7 small nuclear 23 pseudogene . . . . . . . . . . . RNU7-24P . . . RNA, U7 small nuclear 24 pseudogene . . . . . . . . . . . RNU7-25P . . . RNA, U7 small nuclear 25 pseudogene . . . . . . . . . . . RNU7-26P . . . RNA, U7 small nuclear 26 pseudogene . . . . . . . . . . . RNU7-27P . . . RNA, U7 small nuclear 27 pseudogene . . . . . . . . . . . RNU7-28P . . . RNA, U7 small nuclear 28 pseudogene . . . . . . . . . . . RNU7-29P . . . RNA, U7 small nuclear 29 pseudogene . . . . . . . . . . . RNU7-30P . . . RNA, U7 small nuclear 30 pseudogene . . . . . . . . . . . RNU7-31P . . . RNA, U7 small nuclear 31 pseudogene . . . . . . . . . . . RNU7-32P . . . RNA, U7 small nuclear 32 pseudogene . . . . . . . . . . . RNU7-33P . . . RNA, U7 small nuclear 33 pseudogene . . . . . . . . . . . RNU7-34P . . . RNA, U7 small nuclear 34 pseudogene . . . . . . . . . . . RNU7-35P . . . RNA, U7 small nuclear 35 pseudogene . . . . . . . . . . . RNU7-36P . . . RNA, U7 small nuclear 36 pseudogene . . . . . . . . . . . RNU7-37P . . . RNA, U7 small nuclear 37 pseudogene . . . . . . . . . . . RNU7-38P . . . RNA, U7 small nuclear 38 pseudogene . . . . . . . . . . . RNU7-39P . . . RNA, U7 small nuclear 39 pseudogene . . . . . . . . . . . RNU7-40P . . . RNA, U7 small nuclear 40 pseudogene . . . . . . . . . . . RNU7-41P . . . RNA, U7 small nuclear 41 pseudogene . . . . . . . . . . . RNU7-42P . . . RNA, U7 small nuclear 42 pseudogene . . . . . . . . . . . RNU7-43P . . . RNA, U7 small nuclear 43 pseudogene . . . . . . . . . . . RNU7-44P . . . RNA, U7 small nuclear 44 pseudogene . . . . . . . . . . . RNU7-45P . . . RNA, U7 small nuclear 45 pseudogene . . . . . . . . . . . RNU7-46P . . . RNA, U7 small nuclear 46 pseudogene . . . . . . . . . . . RNU7-47P . . . RNA, U7 small nuclear 47 pseudogene . . . . . . . . . . . RNU7-48P . . . RNA, U7 small nuclear 48 pseudogene . . . . . . . . . . . RNU7-49P . . . RNA, U7 small nuclear 49 pseudogene . . . . . . . . . . . RNU7-50P . . . RNA, U7 small nuclear 50 pseudogene . . . . . . . . . . . RNU7-51P . . . RNA, U7 small nuclear 51 pseudogene . . . . . . . . . . . RNU7-52P . . . RNA, U7 small nuclear 52 pseudogene . . . . . . . . . . . RNU7-53P . . . RNA, U7 small nuclear 53 pseudogene . . . . . . . . . . . RNU7-54P . . . RNA, U7 small nuclear 54 pseudogene . . . . . . . . . . . RNU7-55P . . . RNA, U7 small nuclear 55 pseudogene . . . . . . . . . . . RNU7-56P . . . RNA, U7 small nuclear 56 pseudogene . . . . . . . . . . . RNU7-57P . . . RNA, U7 small nuclear 57 pseudogene . . . . . . . . . . . RNU7-58P . . . RNA, U7 small nuclear 58 pseudogene . . . . . . . . . . . RNU7-59P . . . RNA, U7 small nuclear 59 pseudogene . . . . . . . . . . . RNU7-60P . . . RNA, U7 small nuclear 60 pseudogene . . . . . . . . . . . RNU7-61P . . . RNA, U7 small nuclear 61 pseudogene . . . . . . . . . . . RNU7-62P . . . RNA, U7 small nuclear 62 pseudogene . . . . . . . . . . . RNU7-63P . . . RNA, U7 small nuclear 63 pseudogene . . . . . . . . . . . RNU7-64P . . . RNA, U7 small nuclear 64 pseudogene . . . . . . . . . . . RNU7-65P . . . RNA, U7 small nuclear 65 pseudogene . . . . . . . . . . . RNU7-66P . . . RNA, U7 small nuclear 66 pseudogene . . . . . . . . . . . RNU7-67P . . . RNA, U7 small nuclear 67 pseudogene . . . . . . . . . . . RNU7-68P . . . RNA, U7 small nuclear 68 pseudogene . . . . . . . . . . . RNU7-69P . . . RNA, U7 small nuclear 69 pseudogene . . . . . . . . . . . RNU7-70P . . . RNA, U7 small nuclear 70 pseudogene . . . . . . . . . . . RNU7-71P . . . RNA, U7 small nuclear 71 pseudogene . . . . . . . . . . . RNU7-72P . . . RNA, U7 small nuclear 72 pseudogene . . . . . . . . . . . RNU7-73P . . . RNA, U7 small nuclear 73 pseudogene . . . . . . . . . . . RNU7-74P . . . RNA, U7 small nuclear 74 pseudogene . . . . . . . . . . . RNU7-75P . . . RNA, U7 small nuclear 75 pseudogene . . . . . . . . . . . RNU7-76P . . . RNA, U7 small nuclear 76 pseudogene . . . . . . . . . . . RNU7-77P . . . RNA, U7 small nuclear 77 pseudogene . . . . . . . . . . . RNU7-78P . . . RNA, U7 small nuclear 78 pseudogene . . . . . . . . . . . RNU7-79P . . . RNA, U7 small nuclear 79 pseudogene . . . . . . . . . . . RNU7-80P . . . RNA, U7 small nuclear 80 pseudogene . . . . . . . . . . . RNU7-81P . . . RNA, U7 small nuclear 81 pseudogene . . . . . . . . . . . RNU7-82P . . . RNA, U7 small nuclear 82 pseudogene . . . . . . . . . . . RNU7-83P . . . RNA, U7 small nuclear 83 pseudogene . . . . . . . . . . . RNU7-84P . . . RNA, U7 small nuclear 84 pseudogene . . . . . . . . . . . RNU7-85P . . . RNA, U7 small nuclear 85 pseudogene . . . . . . . . . . . RNU7-86P . . . RNA, U7 small nuclear 86 pseudogene . . . . . . . . . . . RNU7-87P . . . RNA, U7 small nuclear 87 pseudogene . . . . . . . . . . . RNU7-88P . . . RNA, U7 small nuclear 88 pseudogene . . . . . . . . . . . RNU7-89P . . . RNA, U7 small nuclear 89 pseudogene . . . . . . . . . . . RNU7-90P . . . RNA, U7 small nuclear 90 pseudogene . . . . . . . . . . . RNU7-92P . . . RNA, U7 small nuclear 92 pseudogene . . . . . . . . . . . RNU7-93P . . . RNA, U7 small nuclear 93 pseudogene . . . . . . . . . . . RNU7-94P . . . RNA, U7 small nuclear 94 pseudogene . . . . . . . . . . . RNU7-95P . . . RNA, U7 small nuclear 95 pseudogene . . . . . . . . . . . RNU7-96P . . . RNA, U7 small nuclear 96 pseudogene . . . . . . . . . . . RNU7-97P . . . RNA, U7 small nuclear 97 pseudogene . . . . . . . . . . . RNU7-99P . . . RNA, U7 small nuclear 99 pseudogene . . . . . . . . . . . RNU7-102P . . . RNA, U7 small nuclear 102 pseudogene . . . . . . . . . . . RNU7-103P . . . RNA, U7 small nuclear 103 pseudogene . . . . . . . . . . . RNU7-104P . . . RNA, U7 small nuclear 104 pseudogene . . . . . . . . . . . RNU7-105P . . . RNA, U7 small nuclear 105 pseudogene . . . . . . . . . . . RNU7-106P . . . RNA, U7 small nuclear 106 pseudogene . . . . . . . . . . . RNU7-107P . . . RNA, U7 small nuclear 107 pseudogene . . . . . . . . . . . RNU7-110P . . . RNA, U7 small nuclear 110 pseudogene . . . . . . . . . . . RNU7-111P . . . RNA, U7 small nuclear 111 pseudogene . . . . . . . . . . . RNU7-113P . . . RNA, U7 small nuclear 113 pseudogene . . . . . . . . . . . RNU7-115P . . . RNA, U7 small nuclear 115 pseudogene . . . . . . . . . . . RNU7-116P . . . RNA, U7 small nuclear 116 pseudogene . . . . . . . . . . . RNU7-119P . . . RNA, U7 small nuclear 119 pseudogene . . . . . . . . . . . RNU7-120P . . . RNA, U7 small nuclear 120 pseudogene . . . . . . . . . . . RNU7-121P . . . RNA, U7 small nuclear 121 pseudogene . . . . . . . . . . . RNU7-123P . . . RNA, U7 small nuclear 123 pseudogene . . . . . . . . . . . RNU7-124P . . . RNA, U7 small nuclear 124 pseudogene . . . . . . . . . . . RNU7-125P . . . RNA, U7 small nuclear 125 pseudogene . . . . . . . . . . . RNU7-126P . . . RNA, U7 small nuclear 126 pseudogene . . . . . . . . . . . RNU7-127P . . . RNA, U7 small nuclear 127 pseudogene . . . . . . . . . . . RNU7-128P . . . RNA, U7 small nuclear 128 pseudogene . . . . . . . . . . . RNU7-129P . . . RNA, U7 small nuclear 129 pseudogene . . . . . . . . . . . RNU7-130P . . . RNA, U7 small nuclear 130 pseudogene . . . . . . . . . . . RNU7-133P . . . RNA, U7 small nuclear 133 pseudogene . . . . . . . . . . . RNU7-134P . . . RNA, U7 small nuclear 134 pseudogene . . . . . . . . . . . RNU7-136P . . . RNA, U7 small nuclear 136 pseudogene . . . . . . . . . . . RNU7-137P . . . RNA, U7 small nuclear 137 pseudogene . . . . . . . . . . . RNU7-138P . . . RNA, U7 small nuclear 138 pseudogene . . . . . . . . . . . RNU7-140P . . . RNA, U7 small nuclear 140 pseudogene . . . . . . . . . . . RNU7-141P . . . RNA, U7 small nuclear 141 pseudogene . . . . . . . . . . . RNU7-143P . . . RNA, U7 small nuclear 143 pseudogene . . . . . . . . . . . RNU7-144P . . . RNA, U7 small nuclear 144 pseudogene . . . . . . . . . . . RNU7-147P . . . RNA, U7 small nuclear 147 pseudogene . . . . . . . . . . . RNU7-148P . . . RNA, U7 small nuclear 148 pseudogene . . . . . . . . . . . RNU7-149P . . . RNA, U7 small nuclear 149 pseudogene . . . . . . . . . . . RNU7-151P . . . RNA, U7 small nuclear 151 pseudogene . . . . . . . . . . . RNU7-152P . . . RNA, U7 small nuclear 152 pseudogene . . . . . . . . . . . RNU7-153P . . . RNA, U7 small nuclear 153 pseudogene . . . . . . . . . . . RNU7-154P . . . RNA, U7 small nuclear 154 pseudogene . . . . . . . . . . . RNU7-155P . . . RNA, U7 small nuclear 155 pseudogene . . . . . . . . . . . RNU7-156P . . . RNA, U7 small nuclear 156 pseudogene . . . . . . . . . . . RNU7-157P . . . RNA, U7 small nuclear 157 pseudogene . . . . . . . . . . . RNU7-158P . . . RNA, U7 small nuclear 158 pseudogene . . . . . . . . . . . RNU7-159P . . . RNA, U7 small nuclear 159 pseudogene . . . . . . . . . . . RNU7-160P . . . RNA, U7 small nuclear 160 pseudogene . . . . . . . . . . . RNU7-161P . . . RNA, U7 small nuclear 161 pseudogene . . . . . . . . . . . RNU7-164P . . . RNA, U7 small nuclear 164 pseudogene . . . . . . . . . . . RNU7-165P . . . RNA, U7 small nuclear 165 pseudogene . . . . . . . . . . . RNU7-167P . . . RNA, U7 small nuclear 167 pseudogene . . . . . . . . . . . RNU7-169P . . . RNA, U7 small nuclear 169 pseudogene . . . . . . . . . . . RNU7-170P . . . RNA, U7 small nuclear 170 pseudogene . . . . . . . . . . . RNU7-171P . . . RNA, U7 small nuclear 171 pseudogene . . . . . . . . . . . RNU7-172P . . . RNA, U7 small nuclear 172 pseudogene . . . . . . . . . . . RNU7-173P . . . RNA, U7 small nuclear 173 pseudogene . . . . . . . . . . . RNU7-174P . . . RNA, U7 small nuclear 174 pseudogene . . . . . . . . . . . RNU7-175P . . . RNA, U7 small nuclear 175 pseudogene . . . . . . . . . . . RNU7-176P . . . RNA, U7 small nuclear 176 pseudogene . . . . . . . . . . . RNU7-179P . . . RNA, U7 small nuclear 179 pseudogene . . . . . . . . . . . RNU7-180P . . . RNA, U7 small nuclear 180 pseudogene . . . . . . . . . . . RNU7-181P . . . RNA, U7 small nuclear 181 pseudogene . . . . . . . . . . . RNU7-182P . . . RNA, U7 small nuclear 182 pseudogene . . . . . . . . . . . RNU7-183P . . . RNA, U7 small nuclear 183 pseudogene . . . . . . . . . . . RNU7-185P . . . RNA, U7 small nuclear 185 pseudogene . . . . . . . . . . . RNU7-186P . . . RNA, U7 small nuclear 186 pseudogene . . . . . . . . . . . RNU7-187P . . . RNA, U7 small nuclear 187 pseudogene . . . . . . . . . . . RNU7-188P . . . RNA, U7 small nuclear 188 pseudogene . . . . . . . . . . . RNU7-190P . . . RNA, U7 small nuclear 190 pseudogene . . . . . . . . . . . RNU7-192P . . . RNA, U7 small nuclear 192 pseudogene . . . . . . . . . . . RNU7-193P . . . RNA, U7 small nuclear 193 pseudogene . . . . . . . . . . . RNU7-194P . . . RNA, U7 small nuclear 194 pseudogene . . . . . . . . . . . RNU7-195P . . . RNA, U7 small nuclear 195 pseudogene . . . . . . . . . . . RNU7-196P . . . RNA, U7 small nuclear 196 pseudogene . . . . . . . . . . . RNU7-197P . . . RNA, U7 small nuclear 197 pseudogene . . . . . . . . . . . RNU7-200P . . . RNA, U7 small nuclear 200 pseudogene . . . . . . . . . . . RNU11 . . . RNA, U11 small nuclear . . . . . . . . . . . RNU11-2P . . . RNA, U11 small nuclear 2, pseudogene . . . . . . . . . . . RNU11-3P . . . RNA, U11 small nuclear 3, pseudogene . . . . . . . . . . . RNU11-4P . . . RNA, U11 small nuclear 4, pseudogene . . . . . . . . . . . RNU11-5P . . . RNA, U11 small nuclear 5, pseudogene . . . . . . . . . . . RNU11-6P . . . RNA, U11 small nuclear 6, pseudogene . . . . . . . . . . . RNU12 . . . RNA, U12 small nuclear . . . . . . . . . . . RNU12-2P . . . RNA, U12 small nuclear 2, pseudogene . . . . . . . . . . . RNU105B . . . RNA, U105B small nucleolar . . . . . . . . . . . RNU105C . . . RNA, U105C small nucleolar . . . . . . . . . . . RNVU1-1 . . . RNA, variant U1 small nuclear 1 . . . . . . . . . . . RNVU1-2 . . . RNA, variant U1 small nuclear 2 . . . . . . . . . . . RNVU1-3 . . . RNA, variant U1 small nuclear 3 . . . . . . . . . . . RNVU1-4 . . . RNA, variant U1 small nuclear 4 . . . . . . . . . . . RNVU1-6 . . . RNA, variant U1 small nuclear 6 . . . . . . . . . . . RNVU1-7 . . . RNA, variant U1 small nuclear 7 . . . . . . . . . . . RNVU1-8 . . . RNA, variant U1 small nuclear 8 . . . . . . . . . . . RNVU1-11 . . . RNA, variant U1 small nuclear 11 . . . . . . . . . . . RNVU1-14 . . . RNA, variant U1 small nuclear 14 . . . . . . . . . . . RNVU1-15 . . . RNA, variant U1 small nuclear 15 . . . . . . . . . . . RNVU1-17 . . . RNA, variant U1 small nuclear 17 . . . . . . . . . . . RNVU1-18 . . . RNA, variant U1 small nuclear 18 . . . . . . . . . . . RNVU1-19 . . . RNA, variant U1 small nuclear 19 . . . . . . . . . . . RNVU1-20 . . . RNA, variant U1 small nuclear 20 . . . . . . . . . . . RNY1 . . . RNA, Ro-associated Y1 . . . . . . . . . . . RNY1P1 . . . RNA, Ro-associated Y1 pseudogene 1 . . . . . . . . . . . RNY1P2 . . . RNA, Ro-associated Y1 pseudogene 2 . . . . . . . . . . . RNY1P3 . . . RNA, Ro-associated Y1 pseudogene 3 . . . . . . . . . . . RNY1P4 . . . RNA, Ro-associated Y1 pseudogene 4 . . . . . . . . . . . RNY1P5 . . . RNA, Ro-associated Y1 pseudogene 5 . . . . . . . . . . . RNY1P6 . . . RNA, Ro-associated Y1 pseudogene 6 . . . . . . . . . . . RNY1P7 . . . RNA, Ro-associated Y1 pseudogene 7 . . . . . . . . . . . RNY1P8 . . . RNA, Ro-associated Y1 pseudogene 8 . . . . . . . . . . . RNY1P9 . . . RNA, Ro-associated Y1 pseudogene 9 . . . . . . . . . . . RNY1P10 . . . RNA, Ro-associated Y1 pseudogene 10 . . . . . . . . . . . RNY1P11 . . . RNA, Ro-associated Y1 pseudogene 11 . . . . . . . . . . . RNY1P12 . . . RNA, Ro-associated Y1 pseudogene 12 . . . . . . . . . . . RNY1P13 . . . RNA, Ro-associated Y1 pseudogene 13 . . . . . . . . . . . RNY1P14 . . . RNA, Ro-associated Y1 pseudogene 14 . . . . . . . . . . . RNY1P15 . . . RNA, Ro-associated Y1 pseudogene 15 . . . . . . . . . . . RNY1P16 . . . RNA, Ro-associated Y1 pseudogene 16 . . . . . . . . . . . RNY3 . . . RNA, Ro-associated Y3 . . . . . . . . . . . RNY3P1 . . . RNA, Ro-associated Y3 pseudogene 1 . . . . . . . . . . . RNY3P2 . . . RNA, Ro-associated Y3 pseudogene 2 . . . . . . . . . . . RNY3P3 . . . RNA, Ro-associated Y3 pseudogene 3 . . . . . . . . . . . RNY3P4 . . . RNA, Ro-associated Y3 pseudogene 4 . . . . . . . . . . . RNY3P5 . . . RNA, Ro-associated Y3 pseudogene 5 . . . . . . . . . . . RNY3P6 . . . RNA, Ro-associated Y3 pseudogene 6 . . . . . . . . . . . RNY3P7 . . . RNA, Ro-associated Y3 pseudogene 7 . . . . . . . . . . . RNY3P8 . . . RNA, Ro-associated Y3 pseudogene 8 . . . . . . . . . . . RNY3P9 . . . RNA, Ro-associated Y3 pseudogene 9 . . . . . . . . . . . RNY3P10 . . . RNA, Ro-associated Y3 pseudogene 10 . . . . . . . . . . . RNY3P11 . . . RNA, Ro-associated Y3 pseudogene 11 . . . . . . . . . . . RNY3P12 . . . RNA, Ro-associated Y3 pseudogene 12 . . . . . . . . . . . RNY3P13 . . . RNA, Ro-associated Y3 pseudogene 13 . . . . . . . . . . . RNY3P14 . . . RNA, Ro-associated Y3 pseudogene 14 . . . . . . . . . . . RNY3P15 . . . RNA, Ro-associated Y3 pseudogene 15 . . . . . . . . . . . RNY3P16 . . . RNA, Ro-associated Y3 pseudogene 16 . . . . . . . . . . . RNY4 . . . RNA, Ro-associated Y4 . . . . . . . . . . . RNY4P1 . . . RNA, Ro-associated Y4 pseudogene 1 . . . . . . . . . . . RNY4P2 . . . RNA, Ro-associated Y4 pseudogene 2 . . . . . . . . . . . RNY4P3 . . . RNA, Ro-associated Y4 pseudogene 3 . . . . . . . . . . . RNY4P4 . . . RNA, Ro-associated Y4 pseudogene 4 . . . . . . . . . . . RNY4P5 . . . RNA, Ro-associated Y4 pseudogene 5 . . . . . . . . . . . RNY4P6 . . . RNA, Ro-associated Y4 pseudogene 6 . . . . . . . . . . . RNY4P7 . . . RNA, Ro-associated Y4 pseudogene 7 . . . . . . . . . . . RNY4P8 . . . RNA, Ro-associated Y4 pseudogene 8 . . . . . . . . . . . RNY4P9 . . . RNA, Ro-associated Y4 pseudogene 9 . . . . . . . . . . . RNY4P10 . . . RNA, Ro-associated Y4 pseudogene 10 . . . . . . . . . . . RNY4P11 . . . RNA, Ro-associated Y4 pseudogene 11 . . . . . . . . . . . RNY4P13 . . . RNA, Ro-associated Y4 pseudogene 13 . . . . . . . . . . . RNY4P14 . . . RNA, Ro-associated Y4 pseudogene 14 . . . . . . . . . . . RNY4P15 . . . RNA, Ro-associated Y4 pseudogene 15 . . . . . . . . . . . RNY4P16 . . . RNA, Ro-associated Y4 pseudogene 16 . . . . . . . . . . . RNY4P17 . . . RNA, Ro-associated Y4 pseudogene 17 . . . . . . . . . . . RNY4P18 . . . RNA, Ro-associated Y4 pseudogene 18 . . . . . . . . . . . RNY4P19 . . . RNA, Ro-associated Y4 pseudogene 19 . . . . . . . . . . . RNY4P20 . . . RNA, Ro-associated Y4 pseudogene 20 . . . . . . . . . . . RNY4P21 . . . RNA, Ro-associated Y4 pseudogene 21 . . . . . . . . . . . RNY4P22 . . . RNA, Ro-associated Y4 pseudogene 22 . . . . . . . . . . . RNY4P23 . . . RNA, Ro-associated Y4 pseudogene 23 . . . . . . . . . . . RNY4P24 . . . RNA, Ro-associated Y4 pseudogene 24 . . . . . . . . . . . RNY4P25 . . . RNA, Ro-associated Y4 pseudogene 25 . . . . . . . . . . . RNY4P26 . . . RNA, Ro-associated Y4 pseudogene 26 . . . . . . . . . . . RNY4P27 . . . RNA, Ro-associated Y4 pseudogene 27 . . . . . . . . . . . RNY4P28 . . . RNA, Ro-associated Y4 pseudogene 28 . . . . . . . . . . . RNY4P29 . . . RNA, Ro-associated Y4 pseudogene 29 . . . . . . . . . . . RNY4P30 . . . RNA, Ro-associated Y4 pseudogene 30 . . . . . . . . . . . RNY4P31 . . . RNA, Ro-associated Y4 pseudogene 31 . . . . . . . . . . . RNY4P34 . . . RNA, Ro-associated Y4 pseudogene 34 . . . . . . . . . . . RNY4P36 . . . RNA, Ro-associated Y4 pseudogene 36 . . . . . . . . . . . RNY4P37 . . . RNA, Ro-associated Y4 pseudogene 37 . . . . . . . . . . . RNY5 . . . RNA, Ro-associated Y5 . . . . . . . . . . . RNY5P1 . . . RNA, Ro-associated Y5 pseudogene 1 . . . . . . . . . . . RNY5P2 . . . RNA, Ro-associated Y5 pseudogene 2 . . . . . . . . . . . RNY5P3 . . . RNA, Ro-associated Y5 pseudogene 3 . . . . . . . . . . . RNY5P4 . . . RNA, Ro-associated Y5 pseudogene 4 . . . . . . . . . . . RNY5P5 . . . RNA, Ro-associated Y5 pseudogene 5 . . . . . . . . . . . RNY5P6 . . . RNA, Ro-associated Y5 pseudogene 6 . . . . . . . . . . . RNY5P7 . . . RNA, Ro-associated Y5 pseudogene 7 . . . . . . . . . . . RNY5P8 . . . RNA, Ro-associated Y5 pseudogene 8 . . . . . . . . . . . RNY5P9 . . . RNA, Ro-associated Y5 pseudogene 9 . . . . . . . . . . . RNY5P10 . . . RNA, Ro-associated Y5 pseudogene 10 . . . . . . . . . . . ROBO1 3.04028778350882e-08 0.999999909764394 5.98327276758773e-08 roundabout guidance receptor 1 FUNCTION: Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development (PubMed:10102268, PubMed:24560577). Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (PubMed:24560577). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex. May be required for lung development (By similarity). {ECO:0000250|UniProtKB:O89026, ECO:0000269|PubMed:10102268, ECO:0000269|PubMed:24560577, ECO:0000305}.; . TISSUE SPECIFICITY: Widely expressed, with exception of kidney. {ECO:0000269|PubMed:9608531}.; . . 0.94674 0.12413 -1.960545765 1.845954234 484.42539 4.53042 ROBO2 0.99999613022592 3.86977408007182e-06 4.76864766346636e-18 roundabout guidance receptor 2 FUNCTION: Receptor for SLIT2, and probably SLIT1, which are thought to act as molecular guidance cue in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development.; DISEASE: Vesicoureteral reflux 2 (VUR2) [MIM:610878]: A disease belonging to the group of congenital anomalies of the kidney and urinary tract. It is characterized by the reflux of urine from the bladder into the ureters and sometimes into the kidneys, and is a risk factor for urinary tract infections. Primary disease results from a developmental defect of the ureterovesical junction. In combination with intrarenal reflux, the resulting inflammatory reaction may result in renal injury or scarring, also called reflux nephropathy. Extensive renal scarring impairs renal function and may predispose patients to hypertension, proteinuria, renal insufficiency and end-stage renal disease. {ECO:0000269|PubMed:17357069}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving ROBO2 is a cause of multiple congenital abnormalities, including severe bilateral VUR with ureterovesical junction defects. Translocation t(Y;3)(p11;p12) with PCDH11Y. This translocation disrupts ROBO2 and produces dominant-negative ROBO2 proteins that abrogate SLIT- ROBO signaling in vitro.; . ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;cornea;placenta;hippocampus;duodenum;head and neck;kidney;stomach; fetal brain;trigeminal ganglion;cingulate cortex; 0.33863 0.12605 -1.501002093 3.597546591 322.63201 3.81501 ROBO2P1 . . . roundabout guidance receptor 2 pseudogene 1 . . . . . . . . . . . ROBO3 0.0286120107539813 0.97138783439047 1.54855548524781e-07 roundabout guidance receptor 3 FUNCTION: Thought to be involved during neural development in axonal navigation at the ventral midline of the neural tube. In spinal chord development plays a role in guiding commissural axons probably by preventing premature sensitivity to Slit proteins thus inhibiting Slit signaling through ROBO1 (By similarity). Required for hindbrain axon midline crossing. {ECO:0000250, ECO:0000269|PubMed:15105459}.; DISEASE: Familial horizontal gaze palsy with progressive scoliosis (HGPPS) [MIM:607313]: Patients show a medulla where motor and sensory projections appear uncrossed. {ECO:0000269|PubMed:15105459}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.46236 0.13154 0.652163325 84.17669262 6788.99215 17.52248 ROBO4 1.66866223576903e-09 0.950296356573798 0.04970364175754 roundabout guidance receptor 4 FUNCTION: Receptor for Slit proteins, at least for SLIT2, and seems to be involved in angiogenesis and vascular patterning. May mediate the inhibition of primary endothelial cell migration by Slit proteins (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in endothelial cells. Expressed at sites of angiogenesis in different tumor types. {ECO:0000269|PubMed:11944987}.; ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;cochlea;thyroid;iris;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09052 0.12945 0.657639543 84.20028309 3167.49955 10.73314 ROCK1 0.999996548070552 3.45192944804221e-06 1.47809639026709e-19 Rho associated coiled-coil containing protein kinase 1 FUNCTION: Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles. Promotes keratinocyte terminal differentiation. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. {ECO:0000269|PubMed:10436159, ECO:0000269|PubMed:10652353, ECO:0000269|PubMed:11018042, ECO:0000269|PubMed:11283607, ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:18573880, ECO:0000269|PubMed:18694941, ECO:0000269|PubMed:19036714, ECO:0000269|PubMed:19131646, ECO:0000269|PubMed:19181962, ECO:0000269|PubMed:19997641, ECO:0000269|PubMed:21072057, ECO:0000269|PubMed:8617235, ECO:0000269|PubMed:9722579}.; . TISSUE SPECIFICITY: Detected in blood platelets. {ECO:0000269|PubMed:8617235}.; . . . 0.55483 -0.574945567 18.90186365 77.81309 1.85951 ROCK1P1 . . . Rho associated coiled-coil containing protein kinase 1 pseudogene 1 . . . . . . . . . . . ROCK2 0.999999990311408 9.68859250002217e-09 5.36517953105583e-23 Rho associated coiled-coil containing protein kinase 2 FUNCTION: Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca(2+) sensitivity and vascular contractility by modulating the myosin light chain phosphorylation. {ECO:0000269|PubMed:10579722, ECO:0000269|PubMed:15699075, ECO:0000269|PubMed:16574662, ECO:0000269|PubMed:17015463, ECO:0000269|PubMed:19131646, ECO:0000269|PubMed:19997641, ECO:0000269|PubMed:21084279, ECO:0000269|PubMed:21147781}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;urinary;spinal cord;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;placenta;head and neck;kidney;stomach; amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;pons;atrioventricular node;caudate nucleus;skin;skeletal muscle;subthalamic nucleus;prefrontal cortex;appendix;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.74930 0.31215 -1.019530098 8.038452465 2623.84779 9.60708 ROGDI 3.12930827517025e-12 0.00582211374839778 0.994177886248473 rogdi homolog FUNCTION: May act as a positive regulator of cell proliferation. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in spinal cord, brain, heart and bone marrow. Also expressed in fetal brain and liver. {ECO:0000269|PubMed:22482807}.; colon;choroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;blood;lens;skeletal muscle;lung;placenta;visual apparatus;hippocampus;liver;alveolus;cervix;kidney;stomach; whole brain;amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;testis - interstitial;cerebellum peduncles;spinal cord;temporal lobe;atrioventricular node;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.16981 0.11213 -0.135838822 43.77211607 115.29391 2.33544 ROM1 0.00326883045590689 0.826982382724083 0.16974878682001 retinal outer segment membrane protein 1 FUNCTION: May function as an adhesion molecule involved in stabilization and compaction of outer segment disks or in the maintenance of the curvature of the rim. It is essential for disk morphogenesis.; . TISSUE SPECIFICITY: Retina (photoreceptor). In rim region of ROS (rod outer segment) disks.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;bone;testis;brain;unclassifiable (Anatomical System);cartilage;tongue;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.41130 0.23030 -0.224023033 37.4321774 133.6058 2.51197 ROMO1 0.726806954057013 0.260399634282707 0.0127934116602803 reactive oxygen species modulator 1 FUNCTION: Induces production of reactive oxygen species (ROS) which are necessary for cell proliferation. May play a role in inducing oxidative DNA damage and replicative senescence. May play a role in the coordination of mitochondrial morphology and cell proliferation.; . TISSUE SPECIFICITY: Up-regulated in a number of cancer cell lines when compared to a normal lung fibroblast cell line. Highly expressed in brain tumors. {ECO:0000269|PubMed:16842742, ECO:0000269|PubMed:19535734}.; myocardium;medulla oblongata;ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;thyroid;bladder;brain;heart;pineal body;adrenal cortex;pharynx;blood;cerebrum;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;trophoblast;lymph node;islets of Langerhans;muscle;pancreas;lung;pia mater;cornea;adrenal gland;placenta;kidney;stomach;cerebellum; heart;liver; 0.25715 0.11262 0.545784012 81.11582921 37.28469 1.11170 ROPN1 0.00818535249401917 0.790578539228473 0.201236108277507 rhophilin associated tail protein 1 . . TISSUE SPECIFICITY: Testis specific in adult. Overexpressed in hematologic tumor cells. {ECO:0000269|PubMed:17551920}.; unclassifiable (Anatomical System);uterus;medulla oblongata;heart;testis;brain;skin; . 0.37282 0.07943 0.12689526 63.00424628 144.61905 2.61941 ROPN1B 5.67126033394535e-05 0.45446857911899 0.545474708277671 rhophilin associated tail protein 1B . . . medulla oblongata;hippocampus;testis;brain;skin; . 0.15207 0.09824 0.03689118 56.64071715 200.09979 3.05584 ROPN1L 0.00163543636221054 0.696439013284787 0.301925550353003 rhophilin associated tail protein 1 like . . . unclassifiable (Anatomical System);medulla oblongata;colon;fovea centralis;skin;retina;uterus;lung;frontal lobe;endometrium;nasopharynx;placenta;macula lutea;hippocampus;testis;kidney;brain; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis; 0.08679 0.08716 0.461228372 78.46190139 95.66573 2.11312 ROPN1L-AS1 . . . ROPN1L antisense RNA 1 . . . . . . . . . . . ROR1 0.906688532334116 0.0933051343535336 6.3333123503398e-06 receptor tyrosine kinase-like orphan receptor 1 FUNCTION: Has very low kinase activity in vitro and is unlikely to function as a tyrosine kinase in vivo. May act as a receptor for wnt ligand WNT5A which may result in the inhibition of WNT3A- mediated signaling. {ECO:0000269|PubMed:25029443}.; . TISSUE SPECIFICITY: Expressed strongly in human heart, lung and kidney, but weakly in the CNS. Isoform Short is strongly expressed in fetal and adult CNS and in a variety of human cancers, including those originating from CNS or PNS neuroectoderm.; . . 0.88787 0.11603 -1.594640695 3.054965794 2681.58701 9.73470 ROR1-AS1 . . . ROR1 antisense RNA 1 . . . . . . . . . . . ROR2 0.46471860623842 0.53527174064803 9.65311355009042e-06 receptor tyrosine kinase-like orphan receptor 2 FUNCTION: Tyrosine-protein kinase receptor which may be involved in the early formation of the chondrocytes. It seems to be required for cartilage and growth plate development (By similarity). Phosphorylates YWHAB, leading to induction of osteogenesis and bone formation (PubMed:17717073). In contrast, has also been shown to have very little tyrosine kinase activity in vitro. May act as a receptor for wnt ligand WNT5A which may result in the inhibition of WNT3A-mediated signaling (PubMed:25029443). {ECO:0000250|UniProtKB:Q9Z138, ECO:0000269|PubMed:17717073, ECO:0000269|PubMed:25029443}.; DISEASE: Brachydactyly B1 (BDB1) [MIM:113000]: A form of brachydactyly. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. In brachydactyly type B1 the middle phalanges are short but in addition the terminal phalanges are rudimentary or absent. Both fingers and toes are affected. The thumbs and big toes are usually deformed. Symphalangism is also a feature. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Robinow syndrome autosomal recessive (RRS) [MIM:268310]: A recessive form of Robinow syndrome, a disease characterized by short-limb dwarfism, costovertebral segmentation defects and abnormalities of the head, face and external genitalia. The clinical signs are generally far more severe in recessive cases, particularly skeletal abnormalities. All patients with the recessive form suffer from vertebral segmentation abnormalities, resulting in scoliosis and chest deformities. Rib fusions are considered to be characteristic of the autosomal recessive form. Patients can also present brachydactyly, with extensive aplasia/hypoplasia of the phalanges and metacarpals/metatarsals, and brachy-syn-polydactyly of the hands and oligodactyly of the feet. {ECO:0000269|PubMed:10932186, ECO:0000269|PubMed:10932187}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.18774 0.10982 -1.072996117 7.348431234 585.21299 4.90539 RORA 0.953196549708048 0.0468032281231729 2.2216877867586e-07 RAR related orphan receptor A FUNCTION: Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Key regulator of embryonic development, cellular differentiation, immunity, circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism. Considered to have intrinsic transcriptional activity, have some natural ligands like oxysterols that act as agonists (25-hydroxycholesterol) or inverse agonists (7-oxygenated sterols), enhancing or repressing the transcriptional activity, respectively. Recruits distinct combinations of cofactors to target genes regulatory regions to modulate their transcriptional expression, depending on the tissue, time and promoter contexts. Regulates genes involved in photoreceptor development including OPN1SW, OPN1SM and ARR3 and skeletal muscle development with MYOD1. Required for proper cerebellum development, regulates SHH gene expression, among others, to induce granule cells proliferation as well as expression of genes involved in calcium- mediated signal transduction. Regulates the circadian expression of several clock genes, including CLOCK, ARNTL/BMAL1, NPAS2 and CRY1. Competes with NR1D1 for binding to their shared DNA response element on some clock genes such as ARNTL/BMAL1, CRY1 and NR1D1 itself, resulting in NR1D1-mediated repression or RORA-mediated activation of clock genes expression, leading to the circadian pattern of clock genes expression. Therefore influences the period length and stability of the clock. Regulates genes involved in lipid metabolism such as apolipoproteins APOA1, APOA5, APOC3 and PPARG. In liver, has specific and redundant functions with RORC as positive or negative modulator of expression of genes encoding phase I and phase II proteins involved in the metabolism of lipids, steroids and xenobiotics, such as CYP7B1 and SULT2A1. Induces a rhythmic expression of some of these genes. In addition, interplays functionally with NR1H2 and NR1H3 for the regulation of genes involved in cholesterol metabolism. Also involved in the regulation of hepatic glucose metabolism through the modulation of G6PC and PCK1. In adipose tissue, plays a role as negative regulator of adipocyte differentiation, probably acting through dual mechanisms. May suppress CEBPB-dependent adipogenesis through direct interaction and PPARG-dependent adipogenesis through competition for DNA-binding. Downstream of IL6 and TGFB and synergistically with RORC isoform 2, is implicated in the lineage specification of uncommitted CD4(+) T-helper (T(H)) cells into T(H)17 cells, antagonizing the T(H)1 program. Probably regulates IL17 and IL17F expression on T(H) by binding to the essential enhancer conserved non-coding sequence 2 (CNS2) in the IL17-IL17F locus. Involved in hypoxia signaling by interacting with and activating the transcriptional activity of HIF1A. May inhibit cell growth in response to cellular stress. May exert an anti- inflammatory role by inducing CHUK expression and inhibiting NF- kappa-B signaling. {ECO:0000269|PubMed:10478845, ECO:0000269|PubMed:11053433, ECO:0000269|PubMed:11252722, ECO:0000269|PubMed:11554739, ECO:0000269|PubMed:12467577, ECO:0000269|PubMed:14570920, ECO:0000269|PubMed:15781255, ECO:0000269|PubMed:15790933, ECO:0000269|PubMed:16462772, ECO:0000269|PubMed:17512500, ECO:0000269|PubMed:18005000, ECO:0000269|PubMed:18354202, ECO:0000269|PubMed:18658046, ECO:0000269|PubMed:19965867, ECO:0000269|PubMed:21499262, ECO:0000269|PubMed:7926749, ECO:0000269|PubMed:9328355, ECO:0000269|PubMed:9862959}.; . TISSUE SPECIFICITY: Widely expressed in a number of tissues. Expressed in both regulatory T-cells (Treg) and effector T-cells (Teff). {ECO:0000269|PubMed:18354202, ECO:0000269|PubMed:7916608}.; unclassifiable (Anatomical System);ovary;tongue;nasopharynx;bone;liver;duodenum;testis;spleen;head and neck;skin;skeletal muscle; superior cervical ganglion; 0.82886 0.17831 -0.957024976 9.088228356 20.08791 0.68686 RORA-AS1 . . . RORA antisense RNA 1 . . . . . . . . . . . RORA-AS2 . . . RORA antisense RNA 2 . . . . . . . . . . . RORB 0.998551700707594 0.00144827319307621 2.60993299382551e-08 RAR related orphan receptor B FUNCTION: Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Considered to have intrinsic transcriptional activity, have some natural ligands such as all-trans retinoic acid (ATRA) and other retinoids which act as inverse agonists repressing the transcriptional activity. Required for normal postnatal development of rod and cone photoreceptor cells. Modulates rod photoreceptors differentiation at least by inducing the transcription factor NRL-mediated pathway. In cone photoreceptor cells, regulates transcription of OPN1SW. Involved in the regulation of the period length and stability of the circadian rhythm. May control cytoarchitectural patterning of neocortical neurons during development. May act in a dose-dependent manner to regulate barrel formation upon innervation of layer IV neurons by thalamocortical axons. May play a role in the suppression of osteoblastic differentiation through the inhibition of RUNX2 transcriptional activity (By similarity). {ECO:0000250}.; . . . . 0.80674 0.17821 -0.405853867 26.23260203 11.04155 0.40003 RORB-AS1 . . . RORB antisense RNA 1 . . . . . . . . . . . RORC 0.997845135319209 0.00215485076509212 1.39156989882322e-08 RAR related orphan receptor C FUNCTION: Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Key regulator of cellular differentiation, immunity, peripheral circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism (PubMed:19381306, PubMed:19965867, PubMed:22789990, PubMed:26160376, PubMed:20203100). Considered to have intrinsic transcriptional activity, have some natural ligands like oxysterols that act as agonists (25-hydroxycholesterol) or inverse agonists (7-oxygenated sterols), enhancing or repressing the transcriptional activity, respectively (PubMed:19965867, PubMed:22789990). Recruits distinct combinations of cofactors to target gene regulatory regions to modulate their transcriptional expression, depending on the tissue, time and promoter contexts. Regulates the circadian expression of clock genes such as CRY1, ARNTL/BMAL1 and NR1D1 in peripheral tissues and in a tissue- selective manner. Competes with NR1D1 for binding to their shared DNA response element on some clock genes such as ARNTL/BMAL1, CRY1 and NR1D1 itself, resulting in NR1D1-mediated repression or RORC- mediated activation of the expression, leading to the circadian pattern of clock genes expression. Therefore influences the period length and stability of the clock. Involved in the regulation of the rhythmic expression of genes involved in glucose and lipid metabolism, including PLIN2 and AVPR1A (PubMed:19965867). Negative regulator of adipocyte differentiation through the regulation of early phase genes expression, such as MMP3. Controls adipogenesis as well as adipocyte size and modulates insulin sensitivity in obesity. In liver, has specific and redundant functions with RORA as positive or negative modulator of expression of genes encoding phase I and Phase II proteins involved in the metabolism of lipids, steroids and xenobiotics, such as SULT1E1. Also plays also a role in the regulation of hepatocyte glucose metabolism through the regulation of G6PC and PCK1 (PubMed:19965867). Regulates the rhythmic expression of PROX1 and promotes its nuclear localization (PubMed:19381306, PubMed:19965867, PubMed:22789990, PubMed:26160376, PubMed:20203100). Plays an indispensable role in the induction of IFN-gamma dependent anti-mycobacterial systemic immunity (PubMed:26160376). {ECO:0000250|UniProtKB:P51450, ECO:0000269|PubMed:19381306, ECO:0000269|PubMed:19965867, ECO:0000269|PubMed:20203100, ECO:0000269|PubMed:22789990, ECO:0000269|PubMed:26160376}.; DISEASE: Note=Biallelic RORC mutations are a cause of immunodeficiency resulting in concomitant candidiasis and mycobacteriosis. Candidiasis is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida. Mycobacteriosis is characterized by infections caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. {ECO:0000269|PubMed:26160376}.; TISSUE SPECIFICITY: Isoform 1 is widely expressed in many tissues, including liver and adipose, and highly expressed in skeletal muscle. Isoform 2 is primarily expressed in immature thymocytes.; unclassifiable (Anatomical System);medulla oblongata;cartilage;islets of Langerhans;muscle;colon;skeletal muscle;lung;endometrium;bone;thyroid;liver;pituitary gland;testis;spleen;cervix;germinal center;kidney;stomach; superior cervical ganglion;liver;kidney;pons; 0.67495 0.09487 0.040529541 57.15380986 501.17397 4.59391 ROS1 1.78016845315113e-44 5.15188928587586e-06 0.999994848110714 ROS proto-oncogene 1 , receptor tyrosine kinase FUNCTION: Orphan receptor tyrosine kinase (RTK) that plays a role in epithelial cell differentiation and regionalization of the proximal epididymal epithelium. May activate several downstream signaling pathways related to cell differentiation, proliferation, growth and survival including the PI3 kinase-mTOR signaling pathway. Mediates the phosphorylation of PTPN11, an activator of this pathway. May also phosphorylate and activate the transcription factor STAT3 to control anchorage-independent cell growth. Mediates the phosphorylation and the activation of VAV3, a guanine nucleotide exchange factor regulating cell morphology. May activate other downstream signaling proteins including AKT1, MAPK1, MAPK3, IRS1 and PLCG2. {ECO:0000269|PubMed:11094073, ECO:0000269|PubMed:16885344}.; DISEASE: Note=A chromosomal aberration involving ROS1 is found in a glioblastoma multiforme sample. An intra-chromosomal deletion del(6)(q21q21) is responsible for the formation of GOPC-ROS1 chimeric protein which is localized to the Golgi and has a constitutive receptor tyrosine kinase activity. A SLC34A2-ROS1 chimeric protein produced in non-small cell lung cancer cells also retains a constitutive kinase activity. A third type of chimeric protein CD74-ROS1 was also identified in those cells. {ECO:0000269|PubMed:12661006}.; TISSUE SPECIFICITY: Expressed in brain. Expression is increased in primary gliomas. {ECO:0000269|PubMed:8143271}.; . . 0.60171 0.24685 -0.02786522 51.40953055 6571.55365 17.08126 RP1 3.68445777366637e-10 0.91892853733132 0.0810714623002344 retinitis pigmentosa 1 (autosomal dominant) FUNCTION: Microtubule-associated protein regulating the stability and length of the microtubule-based axoneme of photoreceptors. Required for the differentiation of photoreceptor cells, it plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme (By similarity). {ECO:0000250}.; DISEASE: Retinitis pigmentosa 1 (RP1) [MIM:180100]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:10391211, ECO:0000269|PubMed:10484783, ECO:0000269|PubMed:11095597, ECO:0000269|PubMed:15863674, ECO:0000269|PubMed:15933747, ECO:0000269|PubMed:19956407, ECO:0000269|PubMed:20664799, ECO:0000269|PubMed:22052604, ECO:0000269|PubMed:22334370}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in retina. Not expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, spleen and pancreas.; unclassifiable (Anatomical System);breast;macula lutea;fovea centralis;skeletal muscle;retina; superior cervical ganglion;ciliary ganglion; 0.33806 0.10246 0.845009452 88.3816938 6989.07147 17.80779 RP1L1 . . . retinitis pigmentosa 1-like 1 FUNCTION: Required for the differentiation of photoreceptor cells. Plays a role in the organization of outer segment of rod and cone photoreceptors (By similarity). {ECO:0000250}.; DISEASE: Occult macular dystrophy (OCMD) [MIM:613587]: An inherited macular dystrophy characterized by progressive loss of macular function but normal ophthalmoscopic appearance. It is typically characterized by a central cone dysfunction leading to a loss of vision despite normal ophthalmoscopic appearance, normal fluorescein angiography, and normal full-field electroretinogram (ERGs), but the amplitudes of the focal macular ERGs and multifocal ERGs are significantly reduced at the central retina. {ECO:0000269|PubMed:20826268, ECO:0000269|PubMed:22605915}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Retinal-specific; expressed in photoreceptor.; retina; . 0.09178 . 7.246646544 99.8997405 19576.13196 29.90294 RP2 0.851505576518184 0.146004500504604 0.00248992297721158 retinitis pigmentosa 2 (X-linked recessive) FUNCTION: Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins. {ECO:0000269|PubMed:11847227, ECO:0000269|PubMed:18376416, ECO:0000269|PubMed:20106869, ECO:0000269|PubMed:22085962}.; DISEASE: Retinitis pigmentosa 2 (RP2) [MIM:312600]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:10090907, ECO:0000269|PubMed:10520237, ECO:0000269|PubMed:10634633, ECO:0000269|PubMed:10937588, ECO:0000269|PubMed:11462235, ECO:0000269|PubMed:11992260, ECO:0000269|PubMed:12657579, ECO:0000269|PubMed:14564670, ECO:0000269|PubMed:22334370, ECO:0000269|PubMed:9697692}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Expressed in the rod and cone photoreceptors, extending from the tips of the outer segment (OS) through the inner segment (IS) and outer nuclear layer (ONL) and into the synaptic terminals of the outer plexiform layer (ONL). Also detected in the bipolar, horizontal and amacrine cells in the inner nuclear layer (INL), extending to the inner plexiform layer (IPL) and though the ganglion cell layer (GCL) and into the nerve fiber layer (NFL) (at protein level). {ECO:0000269|PubMed:10942419, ECO:0000269|PubMed:12417528, ECO:0000269|PubMed:18376416}.; unclassifiable (Anatomical System);lymph node;cartilage;colon;blood;skin;bone marrow;uterus;pancreas;prostate;lung;cochlea;endometrium;bone;placenta;liver;testis;spleen;germinal center;brain;stomach; . 0.15579 0.28800 0.349177632 74.18023119 65.67823 1.66983 RP6 . . . retinitis pigmentosa 6 (X-linked recessive) . . . . . . . . . . . RP9 0.174162977653973 0.812651954063466 0.0131850682825613 retinitis pigmentosa 9 (autosomal dominant) FUNCTION: Is thought to be a target protein for the PIM1 kinase. May play some roles in B-cell proliferation in association with PIM1 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Appears to be expressed in a wide range of tissues.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;blood;lens;skeletal muscle;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;tumor;ciliary ganglion;white blood cells;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.12730 0.19511 0.169169615 65.33380514 1702.05652 7.60613 RP9P . . . retinitis pigmentosa 9 pseudogene . . . . . . . . . . . RP22 . . . retinitis pigmentosa 22 (autosomal recessive) . . . . . . . . . . . RP24 . . . retinitis pigmentosa 24 (X-linked recessive) . . . . . . . . . . . RP29 . . . retinitis pigmentosa 29 (autosomal recessive) . . . . . . . . . . . RP32 . . . retinitis pigmentosa 32 (autosomal recessive) . . . . . . . . . . . RP34 . . . retinitis pigmentosa 34 (X-linked recessive) . . . . . . . . . . . RP35 . . . retinitis pigmentosa 35 (autosomal dominant) . . . . . . . . . . . RP52 . . . retinitis pigmentosa 52 (autosomal dominant) . . . . . . . . . . . RP63 . . . retinitis pigmentosa 63 (autosomal dominant) . . . . . . . . . . . RPA1 0.308711195767143 0.691282251981208 6.55225164906987e-06 replication protein A1 FUNCTION: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (PubMed:9430682). In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response (PubMed:24332808). It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage (PubMed:17765923). Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair (PubMed:7697716). Plays also a role in base excision repair (BER) probably through interaction with UNG (PubMed:9765279). Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance (PubMed:17959650). As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2- containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange (PubMed:19996105). {ECO:0000269|PubMed:12791985, ECO:0000269|PubMed:17765923, ECO:0000269|PubMed:17959650, ECO:0000269|PubMed:19116208, ECO:0000269|PubMed:19996105, ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:7697716, ECO:0000269|PubMed:7700386, ECO:0000269|PubMed:9430682, ECO:0000269|PubMed:9765279}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.99838 0.15950 -1.109541557 6.782259967 213.87685 3.15525 RPA2 0.888461678653319 0.111293634752697 0.000244686593983416 replication protein A2 FUNCTION: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. {ECO:0000269|PubMed:15205463, ECO:0000269|PubMed:17765923, ECO:0000269|PubMed:17959650, ECO:0000269|PubMed:19116208, ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21504906, ECO:0000269|PubMed:2406247, ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:7697716, ECO:0000269|PubMed:7700386, ECO:0000269|PubMed:8702565, ECO:0000269|PubMed:9430682, ECO:0000269|PubMed:9765279}.; . . . . 0.88914 0.39065 0.25917371 70.05779665 155.28434 2.72208 RPA2P1 . . . replication protein A2 pseudogene 1 . . . . . . . . . . . RPA2P2 . . . replication protein A2 pseudogene 2 . . . . . . . . . . . RPA2P3 . . . replication protein A2 pseudogene 3 . . . . . . . . . . . RPA3 7.56338766676384e-05 0.308110220409232 0.691814145714101 replication protein A3 FUNCTION: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (PubMed:9430682). In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response (PubMed:24332808). It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin, in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair (PubMed:7697716). Plays also a role in base excision repair (BER), probably through interaction with UNG (PubMed:9765279). Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA (PubMed:19010961). As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange (PubMed:19996105). {ECO:0000269|PubMed:19010961, ECO:0000269|PubMed:19116208, ECO:0000269|PubMed:19996105, ECO:0000269|PubMed:7697716, ECO:0000269|PubMed:9430682, ECO:0000269|PubMed:9765279, ECO:0000303|PubMed:24332808}.; . . ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;spleen;kidney;mammary gland;stomach; fetal liver;testis;tumor;ciliary ganglion;bone marrow; 0.92190 0.22362 0.035072054 56.2514744 1.27572 0.04464 RPA4 0.273955521172468 0.634184620810257 0.0918598580172749 replication protein A4 FUNCTION: As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange. {ECO:0000269|PubMed:19116208, ECO:0000269|PubMed:19942684, ECO:0000269|PubMed:19996105, ECO:0000269|PubMed:20545304}.; . TISSUE SPECIFICITY: Preferentially expressed in placental and colon mucosa. Widely expressed at intermediate or lower levels. {ECO:0000269|PubMed:19996105}.; . . 0.17222 . -0.007201372 53.19061099 444.24515 4.38357 RPAIN 6.3595199382132e-06 0.271529764619891 0.72846387586017 RPA interacting protein FUNCTION: Mediates the import of RPA complex into the nucleus, possibly via some interaction with importin beta. Isoform 2 is sumoylated and mediates the localization of RPA complex into the PML body of the nucleus, thereby participating in RPA function in DNA metabolism. {ECO:0000269|PubMed:16135809}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in pancreas, kidney, muscle, liver, lung, placenta, brain, heart, leukocytes, colon, intestine, ovary, testis, prostate, thymus and spleen. {ECO:0000269|PubMed:16008515}.; unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;colon;blood;retina;optic nerve;whole body;lung;nasopharynx;placenta;liver;cervix;spleen;germinal center;aorta;stomach; superior cervical ganglion;testis - seminiferous tubule;skeletal muscle; 0.19849 . -0.005381972 53.50908233 771.71707 5.49858 RPAP1 5.01588405270387e-15 0.911329764095814 0.0886702359041805 RNA polymerase II associated protein 1 FUNCTION: Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. Required for interaction of the RNA polymerase II complex with acetylated histone H3. {ECO:0000269|PubMed:17643375}.; . . lymphoreticular;ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;duodenum;alveolus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;pons; 0.07096 0.09965 1.173901604 92.70464732 1746.73127 7.71234 RPAP2 0.00208553433642619 0.993720548783195 0.00419391688037918 RNA polymerase II associated protein 2 FUNCTION: Protein phosphatase that displays CTD phosphatase activity and regulates transcription of snRNA genes. Recognizes and binds phosphorylated 'Ser-7' of the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and mediates dephosphorylation of 'Ser-5' of the CTD, thereby promoting transcription of snRNA genes. {ECO:0000269|PubMed:17643375, ECO:0000269|PubMed:22137580}.; . . . . 0.08868 0.10640 -0.602450568 17.91106393 137.76888 2.55615 RPAP2P1 . . . RNA polymerase II associated protein 2 pseudogene 1 . . . . . . . . . . . RPAP3 0.140309540099749 0.859655889053249 3.45708470016437e-05 RNA polymerase II associated protein 3 FUNCTION: Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. {ECO:0000269|PubMed:17643375}.; . . colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;blood;skeletal muscle;pancreas;lung;placenta;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; pons;trigeminal ganglion; 0.42719 0.09626 -0.600630256 18.06440198 60.90578 1.58713 RPARP-AS1 . . . RPARP antisense RNA 1 . . . . . . . . . . . RPE 0.316665036809444 0.666307679480289 0.0170272837102672 ribulose-5-phosphate-3-epimerase FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5- phosphate to D-xylulose 5-phosphate. {ECO:0000269|PubMed:20923965}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;macula lutea;liver;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;skeletal muscle;parietal lobe; 0.71757 0.32628 -0.05129383 49.75819769 13.02698 0.47468 RPE65 1.45840005679569e-07 0.828788531950487 0.171211322209507 retinal pigment epithelium-specific protein 65kDa FUNCTION: Plays important roles in the production of 11-cis retinal and in visual pigment regeneration. The soluble form binds vitamin A (all-trans-retinol), making it available for LRAT processing to all-trans-retinyl ester. The membrane form, palmitoylated by LRAT, binds all-trans-retinyl esters, making them available for IMH (isomerohydrolase) processing to all-cis- retinol. The soluble form is regenerated by transferring its palmitoyl groups onto 11-cis-retinol, a reaction catalyzed by LRAT. The enzymatic activity is linearly dependent of the expression levels and membrane association. {ECO:0000269|PubMed:16116091, ECO:0000269|PubMed:21654732}.; DISEASE: Leber congenital amaurosis 2 (LCA2) [MIM:204100]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:10090910, ECO:0000269|PubMed:10766140, ECO:0000269|PubMed:11462243, ECO:0000269|PubMed:14611946, ECO:0000269|PubMed:14962443, ECO:0000269|PubMed:15024725, ECO:0000269|PubMed:16205573, ECO:0000269|PubMed:17297704, ECO:0000269|PubMed:17724218, ECO:0000269|PubMed:18682808, ECO:0000269|PubMed:9326941, ECO:0000269|PubMed:9801879}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa 20 (RP20) [MIM:613794]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:11095629, ECO:0000269|PubMed:12960219, ECO:0000269|PubMed:15557452, ECO:0000269|PubMed:22334370, ECO:0000269|PubMed:23878505, ECO:0000269|PubMed:9501220}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in RPE65 are a cause of autosomal dominant retinitis pigmentosa with choroidal involvement (PubMed:21654732). Affected individuals show reduction of central vision, constriction of visual fields, night blindness and chorioretinal atrophy. {ECO:0000269|PubMed:21654732}.; TISSUE SPECIFICITY: Retinal pigment epithelium specific. {ECO:0000269|PubMed:21493626}.; unclassifiable (Anatomical System);optic nerve;macula lutea;visual apparatus;fovea centralis;choroid;lens;brain;retina; superior cervical ganglion;trigeminal ganglion;skin; 0.13937 0.25571 -0.378346116 28.01368247 347.53959 3.95184 RPEL1 . . . ribulose-5-phosphate-3-epimerase-like 1 FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5- phosphate to D-xylulose 5-phosphate. {ECO:0000250}.; . . . . . . . . 78.34471 1.86735 RPEP1 . . . ribulose-5-phosphate-3-epimerase pseudogene 1 . . . . . . . . . . . RPEP2 . . . ribulose-5-phosphate-3-epimerase pseudogene 2 . . . . . . . . . . . RPEP3 . . . ribulose-5-phosphate-3-epimerase pseudogene 3 . . . . . . . . . . . RPEP4 . . . ribulose-5-phosphate-3-epimerase pseudogene 4 . . . . . . . . . . . RPEP5 . . . ribulose-5-phosphate-3-epimerase pseudogene 5 . . . . . . . . . . . RPEP6 . . . ribulose-5-phosphate-3-epimerase pseudogene 6 . . . . . . . . . . . RPF1 9.47682922183822e-07 0.528911426224003 0.471087626093075 ribosome production factor 1 homolog FUNCTION: May be required for ribosome biogenesis. {ECO:0000269|PubMed:11864606}.; . . . . 0.17412 0.10595 0.997633954 90.65227648 2647.98942 9.65398 RPF2 0.393258891668275 0.604747654284578 0.00199345404714779 ribosome production factor 2 homolog . . . . . 0.67549 0.12730 0.150760231 64.51403633 339.23234 3.90575 RPF2P1 . . . ribosome production factor 2 homolog pseudogene 1 . . . . . . . . . . . RPF2P2 . . . ribosome production factor 2 homolog pseudogene 2 . . . . . . . . . . . RPGR 0.997857546203891 0.00214244007507096 1.37210376804215e-08 retinitis pigmentosa GTPase regulator FUNCTION: Could be a guanine-nucleotide releasing factor. Plays a role in ciliogenesis. Probably regulates cilia formation by regulating actin stress filaments and cell contractility. Plays an important role in photoreceptor integrity. May play a critical role in spermatogenesis and in intraflagellar transport processes (By similarity). May be involved in microtubule organization and regulation of transport in primary cilia. {ECO:0000250, ECO:0000269|PubMed:21933838}.; DISEASE: Retinitis pigmentosa 3 (RP3) [MIM:300029]: A X-linked retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. In RP3, affected males have a severe phenotype, and carrier females show a wide spectrum of clinical features ranging from completely asymptomatic to severe retinitis pigmentosa. Heterozygous women can manifest a form of choroidoretinal degeneration which is distinguished from other types by the absence of visual defects in the presence of a brilliant, scintillating, golden-hued, patchy appearance most striking around the macula, called a tapetal-like retinal reflex. {ECO:0000269|PubMed:10482958, ECO:0000269|PubMed:10737996, ECO:0000269|PubMed:10932196, ECO:0000269|PubMed:10937588, ECO:0000269|PubMed:10970770, ECO:0000269|PubMed:11180598, ECO:0000269|PubMed:11992260, ECO:0000269|PubMed:12657579, ECO:0000269|PubMed:14564670, ECO:0000269|PubMed:8673101, ECO:0000269|PubMed:8817343, ECO:0000269|PubMed:9399904, ECO:0000269|PubMed:9855162}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa and sinorespiratory infections with or without deafness (RPDSI) [MIM:300455]: A disease characterized by the association primary ciliary dyskinesia features with retinitis pigmentosa. Some patients also manifest deafness. {ECO:0000269|PubMed:12920075, ECO:0000269|PubMed:14627685}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cone-rod dystrophy, X-linked 1 (CORDX1) [MIM:304020]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. In cone-rod dystrophy X-linked type 1 the degree of rod-photoreceptor involvement can be variable, with degeneration increasing as the disease progresses. Affected individuals (essentially all of whom are males) present with decreased visual acuity, myopia, photophobia, abnormal color vision, full peripheral visual fields, decreased photopic electroretinographic responses, and granularity of the macular retinal pigment epithelium. Although penetrance appears to be nearly 100%, there is variable expressivity with respect to age at onset and severity of symptoms. {ECO:0000269|PubMed:11857109}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Macular degeneration, X-linked, atrophic (MDXLA) [MIM:300834]: An ocular disorder characterized by macular atrophy causing progressive loss of visual acuity with minimal peripheral visual impairment. Some patients manifest extensive macular degeneration plus peripheral loss of retinal pigment epithelium and choriocapillaries. Full-field electroretinograms (ERGs) show normal cone and rod responses in some affected males despite advanced macular degeneration. {ECO:0000269|PubMed:12160730}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, muscle, kidney, retina, pancreas and fetal retinal pigment epithelium. Isoform 3 is found only in the retina. Colocalizes with RPGRIP1 in the outer segment of rod photoreceptors and cone outer segments. {ECO:0000269|PubMed:12140192}.; unclassifiable (Anatomical System);myocardium;lymph node;cartilage;colon;fovea centralis;bone marrow;uterus;lung;larynx;placenta;macula lutea;pituitary gland;testis;head and neck;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.54230 . 2.802177104 99.03868837 2307.37975 8.90096 RPGRIP1 2.57325929287003e-21 0.0467319125629642 0.953268087437036 retinitis pigmentosa GTPase regulator interacting protein 1 FUNCTION: May function as scaffolding protein. Required for normal location of RPGR at the connecting cilium of photoreceptor cells. Required for normal disk morphogenesis and disk organization in the outer segment of photoreceptor cells and for survival of photoreceptor cells. {ECO:0000250|UniProtKB:Q9EPQ2, ECO:0000305|PubMed:10958648}.; DISEASE: Leber congenital amaurosis 6 (LCA6) [MIM:613826]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:11528500, ECO:0000269|PubMed:18682808}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cone-rod dystrophy 13 (CORD13) [MIM:608194]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. {ECO:0000269|PubMed:10958648, ECO:0000269|PubMed:12920076}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Heterozygous non-synonymous variants of RPGRIP1 may cause or increase the susceptibility to various forms of glaucoma, a genetically heterogeneous disorder. It is the second cause of blindness worldwide owing to the progressive degeneration of retinal ganglion neurons (PubMed:21224891). {ECO:0000269|PubMed:21224891}.; TISSUE SPECIFICITY: Strong expression in retina, with weaker expression in testis. Expressed in other neurons such as amacrine cells. Colocalizes with RGPR in the outer segment of rod photoreceptors and cone outer segments. {ECO:0000269|PubMed:10958647, ECO:0000269|PubMed:10958648, ECO:0000269|PubMed:12140192}.; unclassifiable (Anatomical System);uterus;medulla oblongata;optic nerve;lung;whole body;cartilage;testis;skeletal muscle;retina; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;appendix;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.08190 0.18230 1.298854499 93.91365888 2951.663 10.29586 RPGRIP1L 1.19937665171712e-18 0.621134911252416 0.378865088747584 RPGRIP1-like FUNCTION: Negatively regulates signaling through the G-protein coupled thromboxane A2 receptor (TBXA2R). May be involved in mechanisms like programmed cell death, craniofacial development, patterning of the limbs, and formation of the left-right axis (By similarity). Involved in the organization of apical junctions in kidney cells together with NPHP1 and NPHP4 (By similarity). Does not seem to be strictly required for ciliogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:19464661}.; DISEASE: Joubert syndrome 7 (JBTS7) [MIM:611560]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. {ECO:0000269|PubMed:17558407, ECO:0000269|PubMed:17558409, ECO:0000269|PubMed:22693042}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Meckel syndrome 5 (MKS5) [MIM:611561]: A disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly. {ECO:0000269|PubMed:17558409, ECO:0000269|PubMed:19430481}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: COACH syndrome (COACHS) [MIM:216360]: A disorder characterized by mental retardation, ataxia due to cerebellar hypoplasia, and hepatic fibrosis. Patients present the molar tooth sign, a midbrain-hindbrain malformation pathognomonic for Joubert syndrome and related disorders. Other features, such as coloboma and renal cysts, may be variable. {ECO:0000269|PubMed:19574260}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed with relatively high level of expression in hypothalamus and islet. During early development, expressed in multiple organs including brain, eye, forelimb and kidney. {ECO:0000269|PubMed:17434869, ECO:0000269|PubMed:17558407, ECO:0000269|PubMed:17558409, ECO:0000269|PubMed:19464661}.; unclassifiable (Anatomical System);ovary;cartilage;colon;parathyroid;skeletal muscle;retina;uterus;lung;placenta;visual apparatus;liver;testis;spleen;kidney;brain;thymus; superior cervical ganglion;testis;skeletal muscle; 0.29293 0.22948 1.078370636 91.75513093 2689.08075 9.76194 RPH3A 0.738603478065915 0.261396346696508 1.75237577216936e-07 rabphilin 3A FUNCTION: Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal (By similarity). {ECO:0000250}.; . . . . 0.30185 0.13029 -1.482570877 3.662420382 623.39047 5.03439 RPH3AL 5.10573723225223e-10 0.111993915374282 0.888006084115145 rabphilin 3A-like (without C2 domains) FUNCTION: Rab GTPase effector involved in the late steps of regulated exocytosis, both in endocrine and exocrine cells (By similarity). Acts as a potential RAB3B effector protein in epithelial cells. {ECO:0000250, ECO:0000269|PubMed:15003533}.; . TISSUE SPECIFICITY: Moderate to high levels of expression in thyroid, ovary, stomach, heart, pancreas, skeletal muscle, kidney and liver. Also detected in epithelial cells. {ECO:0000269|PubMed:10395805, ECO:0000269|PubMed:15003533}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;muscle;colon;parathyroid;fovea centralis;choroid;lens;retina;uterus;pancreas;prostate;optic nerve;lung;synovium;placenta;macula lutea;testis;kidney;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.18553 . -0.156065314 42.16206653 298.79923 3.68651 RPIA 0.00590911291307371 0.972315356073343 0.0217755310135831 ribose 5-phosphate isomerase A . DISEASE: Ribose 5-phosphate isomerase deficiency (RPID) [MIM:608611]: A patient has been described with a deficiency of ribose 5-phosphate isomerase who presented with leukoencephalopathy and peripheral neuropathy. Proton magnetic resonance spectroscopy of the brain revealed a highly elevated level of the polyols ribitol and D-arabitol, which were subsequently also found in high concentrations in body fluids. Deficient activity of RPIA, one of the pentose phosphate pathway enzymes, has been demonstrated in fibroblasts. {ECO:0000269|PubMed:14988808}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;placenta;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;placenta;atrioventricular node;bone marrow; 0.58590 0.46106 -0.163345027 41.24793583 35.03561 1.06293 RPIAP1 . . . ribose 5-phosphate isomerase A pseudogene 1 . . . . . . . . . . . RPL3 0.994251970706247 0.0057472751825113 7.54111241398196e-07 ribosomal protein L3 FUNCTION: The L3 protein is a component of the large subunit of cytoplasmic ribosomes.; . . ovary;salivary gland;foreskin;intestine;colon;vein;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;oesophagus;pituitary gland;testis;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pineal body;urinary;adrenal cortex;pharynx;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;alveolus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach;thymus; . 0.30356 0.27325 -0.758599262 13.32861524 54.58196 1.47841 RPL3L 2.13545692074586e-08 0.253648075112042 0.746351903533389 ribosomal protein L3 like . . . unclassifiable (Anatomical System);prostate;heart;muscle;liver;skeletal muscle;peripheral nerve; tongue;skeletal muscle; 0.84611 0.15162 0.762397607 86.8542109 432.11942 4.33932 RPL3P1 . . . ribosomal protein L3 pseudogene 1 . . . . . . . . . . . RPL3P2 . . . ribosomal protein L3 pseudogene 2 . . . . . . . . . . . RPL3P3 . . . ribosomal protein L3 pseudogene 3 . . . . . . . . . . . RPL3P4 . . . ribosomal protein L3 pseudogene 4 . . . . . . . . . . . RPL3P5 . . . ribosomal protein L3 pseudogene 5 . . . . . . . . . . . RPL3P6 . . . ribosomal protein L3 pseudogene 6 . . . . . . . . . . . RPL3P7 . . . ribosomal protein L3 pseudogene 7 . . . . . . . . . . . RPL3P8 . . . ribosomal protein L3 pseudogene 8 . . . . . . . . . . . RPL3P9 . . . ribosomal protein L3 pseudogene 9 . . . . . . . . . . . RPL3P10 . . . ribosomal protein L3 pseudogene 10 . . . . . . . . . . . RPL3P11 . . . ribosomal protein L3 pseudogene 11 . . . . . . . . . . . RPL3P12 . . . ribosomal protein L3 pseudogene 12 . . . . . . . . . . . RPL3P13 . . . ribosomal protein L3 pseudogene 13 . . . . . . . . . . . RPL4 0.999281603608024 0.000718391666014969 4.72596079152717e-09 ribosomal protein L4 . . . ovary;salivary gland;intestine;colon;parathyroid;vein;skin;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;gum;bone;pituitary gland;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;oral cavity;muscle;urinary;adrenal cortex;pharynx;blood;cerebrum;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; . 0.99240 0.37896 0.018483465 55.44939844 47.4392 1.33656 RPL4P1 . . . ribosomal protein L4 pseudogene 1 . . . . . . . . . . . RPL4P2 . . . ribosomal protein L4 pseudogene 2 . . . . . . . . . . . RPL4P3 . . . ribosomal protein L4 pseudogene 3 . . . . . . . . . . . RPL4P4 . . . ribosomal protein L4 pseudogene 4 . . . . . . . . . . . RPL4P5 . . . ribosomal protein L4 pseudogene 5 . . . . . . . . . . . RPL4P6 . . . ribosomal protein L4 pseudogene 6 . . . . . . . . . . . RPL5 0.994762228681169 0.00523717043219018 6.00886640808227e-07 ribosomal protein L5 FUNCTION: Required for rRNA maturation and formation of the 60S ribosomal subunits. This protein binds 5S RNA. {ECO:0000269|PubMed:19061985}.; DISEASE: Diamond-Blackfan anemia 6 (DBA6) [MIM:612561]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. {ECO:0000269|PubMed:19061985, ECO:0000269|PubMed:19191325}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.26327 0.20634 -0.029247611 51.40363293 22.85333 0.76269 RPL5P1 . . . ribosomal protein L5 pseudogene 1 . . . . . . . . . . . RPL5P2 . . . ribosomal protein L5 pseudogene 2 . . . . . . . . . . . RPL5P3 . . . ribosomal protein L5 pseudogene 3 . . . . . . . . . . . RPL5P4 . . . ribosomal protein L5 pseudogene 4 . . . . . . . . . . . RPL5P5 . . . ribosomal protein L5 pseudogene 5 . . . . . . . . . . . RPL5P6 . . . ribosomal protein L5 pseudogene 6 . . . . . . . . . . . RPL5P7 . . . ribosomal protein L5 pseudogene 7 . . . . . . . . . . . RPL5P8 . . . ribosomal protein L5 pseudogene 8 . . . . . . . . . . . RPL5P9 . . . ribosomal protein L5 pseudogene 9 . . . . . . . . . . . RPL5P10 . . . ribosomal protein L5 pseudogene 10 . . . . . . . . . . . RPL5P11 . . . ribosomal protein L5 pseudogene 11 . . . . . . . . . . . RPL5P12 . . . ribosomal protein L5 pseudogene 12 . . . . . . . . . . . RPL5P13 . . . ribosomal protein L5 pseudogene 13 . . . . . . . . . . . RPL5P14 . . . ribosomal protein L5 pseudogene 14 . . . . . . . . . . . RPL5P15 . . . ribosomal protein L5 pseudogene 15 . . . . . . . . . . . RPL5P16 . . . ribosomal protein L5 pseudogene 16 . . . . . . . . . . . RPL5P17 . . . ribosomal protein L5 pseudogene 17 . . . . . . . . . . . RPL5P18 . . . ribosomal protein L5 pseudogene 18 . . . . . . . . . . . RPL5P19 . . . ribosomal protein L5 pseudogene 19 . . . . . . . . . . . RPL5P20 . . . ribosomal protein L5 pseudogene 20 . . . . . . . . . . . RPL5P21 . . . ribosomal protein L5 pseudogene 21 . . . . . . . . . . . RPL5P22 . . . ribosomal protein L5 pseudogene 22 . . . . . . . . . . . RPL5P23 . . . ribosomal protein L5 pseudogene 23 . . . . . . . . . . . RPL5P24 . . . ribosomal protein L5 pseudogene 24 . . . . . . . . . . . RPL5P25 . . . ribosomal protein L5 pseudogene 25 . . . . . . . . . . . RPL5P26 . . . ribosomal protein L5 pseudogene 26 . . . . . . . . . . . RPL5P27 . . . ribosomal protein L5 pseudogene 27 . . . . . . . . . . . RPL5P28 . . . ribosomal protein L5 pseudogene 28 . . . . . . . . . . . RPL5P29 . . . ribosomal protein L5 pseudogene 29 . . . . . . . . . . . RPL5P30 . . . ribosomal protein L5 pseudogene 30 . . . . . . . . . . . RPL5P31 . . . ribosomal protein L5 pseudogene 31 . . . . . . . . . . . RPL5P32 . . . ribosomal protein L5 pseudogene 32 . . . . . . . . . . . RPL5P33 . . . ribosomal protein L5 pseudogene 33 . . . . . . . . . . . RPL5P34 . . . ribosomal protein L5 pseudogene 34 . . . . . . . . . . . RPL5P35 . . . ribosomal protein L5 pseudogene 35 . . . . . . . . . . . RPL6 0.98828827107104 0.0117074250839146 4.30384504550909e-06 ribosomal protein L6 FUNCTION: Specifically binds to domain C of the Tax-responsive enhancer element in the long terminal repeat of HTLV-I.; . . ovary;skin;prostate;frontal lobe;cochlea;endometrium;bladder;brain;gall bladder;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;epidermis;islets of Langerhans;pancreas;lung;pia mater;cornea;placenta;kidney;stomach;aorta;thymus; . 0.65012 0.21208 -0.139478553 43.29440906 24.38571 0.80204 RPL6P1 . . . ribosomal protein L6 pseudogene 1 . . . . . . . . . . . RPL6P2 . . . ribosomal protein L6 pseudogene 2 . . . . . . . . . . . RPL6P3 . . . ribosomal protein L6 pseudogene 3 . . . . . . . . . . . RPL6P4 . . . ribosomal protein L6 pseudogene 4 . . . . . . . . . . . RPL6P5 . . . ribosomal protein L6 pseudogene 5 . . . . . . . . . . . RPL6P6 . . . ribosomal protein L6 pseudogene 6 . . . . . . . . . . . RPL6P7 . . . ribosomal protein L6 pseudogene 7 . . . . . . . . . . . RPL6P8 . . . ribosomal protein L6 pseudogene 8 . . . . . . . . . . . RPL6P9 . . . ribosomal protein L6 pseudogene 9 . . . . . . . . . . . RPL6P10 . . . ribosomal protein L6 pseudogene 10 . . . . . . . . . . . RPL6P12 . . . ribosomal protein L6 pseudogene 12 . . . . . . . . . . . RPL6P13 . . . ribosomal protein L6 pseudogene 13 . . . . . . . . . . . RPL6P14 . . . ribosomal protein L6 pseudogene 14 . . . . . . . . . . . RPL6P15 . . . ribosomal protein L6 pseudogene 15 . . . . . . . . . . . RPL6P16 . . . ribosomal protein L6 pseudogene 16 . . . . . . . . . . . RPL6P17 . . . ribosomal protein L6 pseudogene 17 . . . . . . . . . . . RPL6P18 . . . ribosomal protein L6 pseudogene 18 . . . . . . . . . . . RPL6P19 . . . ribosomal protein L6 pseudogene 19 . . . . . . . . . . . RPL6P20 . . . ribosomal protein L6 pseudogene 20 . . . . . . . . . . . RPL6P21 . . . ribosomal protein L6 pseudogene 21 . . . . . . . . . . . RPL6P22 . . . ribosomal protein L6 pseudogene 22 . . . . . . . . . . . RPL6P24 . . . ribosomal protein L6 pseudogene 24 . . . . . . . . . . . RPL6P25 . . . ribosomal protein L6 pseudogene 25 . . . . . . . . . . . RPL6P26 . . . ribosomal protein L6 pseudogene 26 . . . . . . . . . . . RPL6P27 . . . ribosomal protein L6 pseudogene 27 . . . . . . . . . . . RPL6P28 . . . ribosomal protein L6 pseudogene 28 . . . . . . . . . . . RPL6P29 . . . ribosomal protein L6 pseudogene 29 . . . . . . . . . . . RPL6P30 . . . ribosomal protein L6 pseudogene 30 . . . . . . . . . . . RPL7 0.991153031565654 0.00884480355837766 2.1648759678843e-06 ribosomal protein L7 FUNCTION: Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs.; . . myocardium;ovary;sympathetic chain;skin;retina;prostate;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;tongue;pineal body;urinary;adrenal cortex;pharynx;blood;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;oesophagus;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; . 0.95682 0.22744 -0.295622497 32.61972163 12.46643 0.45294 RPL7A 0.979405408797334 0.0205773689274648 1.72222752007552e-05 ribosomal protein L7a . DISEASE: Note=Chromosomal recombination involving RPL7A activates the receptor kinase domain of the TRK oncogene.; . . . 0.18834 . -0.161524709 41.6430762 10.143 0.36994 RPL7AP2 . . . ribosomal protein L7a pseudogene 2 . . . . . . . . . . . RPL7AP3 . . . ribosomal protein L7a pseudogene 3 . . . . . . . . . . . RPL7AP4 . . . ribosomal protein L7a pseudogene 4 . . . . . . . . . . . RPL7AP5 . . . ribosomal protein L7a pseudogene 5 . . . . . . . . . . . RPL7AP6 . . . ribosomal protein L7a pseudogene 6 . . . . . . . . . . . RPL7AP7 . . . ribosomal protein L7a pseudogene 7 . . . . . . . . . . . RPL7AP8 . . . ribosomal protein L7a pseudogene 8 . . . . . . . . . . . RPL7AP9 . . . ribosomal protein L7a pseudogene 9 . . . . . . . . . . . RPL7AP10 . . . ribosomal protein L7a pseudogene 10 . . . . . . . . . . . RPL7AP11 . . . ribosomal protein L7a pseudogene 11 . . . . . . . . . . . RPL7AP12 . . . ribosomal protein L7a pseudogene 12 . . . . . . . . . . . RPL7AP13 . . . ribosomal protein L7a pseudogene 13 . . . . . . . . . . . RPL7AP14 . . . ribosomal protein L7a pseudogene 14 . . . . . . . . . . . RPL7AP15 . . . ribosomal protein L7a pseudogene 15 . . . . . . . . . . . RPL7AP16 . . . ribosomal protein L7a pseudogene 16 . . . . . . . . . . . RPL7AP17 . . . ribosomal protein L7a pseudogene 17 . . . . . . . . . . . RPL7AP18 . . . ribosomal protein L7a pseudogene 18 . . . . . . . . . . . RPL7AP19 . . . ribosomal protein L7a pseudogene 19 . . . . . . . . . . . RPL7AP20 . . . ribosomal protein L7a pseudogene 20 . . . . . . . . . . . RPL7AP21 . . . ribosomal protein L7a pseudogene 21 . . . . . . . . . . . RPL7AP22 . . . ribosomal protein L7a pseudogene 22 . . . . . . . . . . . RPL7AP23 . . . ribosomal protein L7a pseudogene 23 . . . . . . . . . . . RPL7AP24 . . . ribosomal protein L7a pseudogene 24 . . . . . . . . . . . RPL7AP25 . . . ribosomal protein L7a pseudogene 25 . . . . . . . . . . . RPL7AP26 . . . ribosomal protein L7a pseudogene 26 . . . . . . . . . . . RPL7AP27 . . . ribosomal protein L7a pseudogene 27 . . . . . . . . . . . RPL7AP28 . . . ribosomal protein L7a pseudogene 28 . . . . . . . . . . . RPL7AP29 . . . ribosomal protein L7a pseudogene 29 . . . . . . . . . . . RPL7AP30 . . . ribosomal protein L7a pseudogene 30 . . . . . . . . . . . RPL7AP31 . . . ribosomal protein L7a pseudogene 31 . . . . . . . . . . . RPL7AP32 . . . ribosomal protein L7a pseudogene 32 . . . . . . . . . . . RPL7AP33 . . . ribosomal protein L7a pseudogene 33 . . . . . . . . . . . RPL7AP34 . . . ribosomal protein L7a pseudogene 34 . . . . . . . . . . . RPL7AP35 . . . ribosomal protein L7a pseudogene 35 . . . . . . . . . . . RPL7AP36 . . . ribosomal protein L7a pseudogene 36 . . . . . . . . . . . RPL7AP37 . . . ribosomal protein L7a pseudogene 37 . . . . . . . . . . . RPL7AP38 . . . ribosomal protein L7a pseudogene 38 . . . . . . . . . . . RPL7AP39 . . . ribosomal protein L7a pseudogene 39 . . . . . . . . . . . RPL7AP40 . . . ribosomal protein L7a pseudogene 40 . . . . . . . . . . . RPL7AP41 . . . ribosomal protein L7a pseudogene 41 . . . . . . . . . . . RPL7AP42 . . . ribosomal protein L7a pseudogene 42 . . . . . . . . . . . RPL7AP43 . . . ribosomal protein L7a pseudogene 43 . . . . . . . . . . . RPL7AP44 . . . ribosomal protein L7a pseudogene 44 . . . . . . . . . . . RPL7AP45 . . . ribosomal protein L7a pseudogene 45 . . . . . . . . . . . RPL7AP46 . . . ribosomal protein L7a pseudogene 46 . . . . . . . . . . . RPL7AP47 . . . ribosomal protein L7a pseudogene 47 . . . . . . . . . . . RPL7AP48 . . . ribosomal protein L7a pseudogene 48 . . . . . . . . . . . RPL7AP49 . . . ribosomal protein L7a pseudogene 49 . . . . . . . . . . . RPL7AP50 . . . ribosomal protein L7a pseudogene 50 . . . . . . . . . . . RPL7AP51 . . . ribosomal protein L7a pseudogene 51 . . . . . . . . . . . RPL7AP52 . . . ribosomal protein L7a pseudogene 52 . . . . . . . . . . . RPL7AP53 . . . ribosomal protein L7a pseudogene 53 . . . . . . . . . . . RPL7AP54 . . . ribosomal protein L7a pseudogene 54 . . . . . . . . . . . RPL7AP55 . . . ribosomal protein L7a pseudogene 55 . . . . . . . . . . . RPL7AP56 . . . ribosomal protein L7a pseudogene 56 . . . . . . . . . . . RPL7AP57 . . . ribosomal protein L7a pseudogene 57 . . . . . . . . . . . RPL7AP58 . . . ribosomal protein L7a pseudogene 58 . . . . . . . . . . . RPL7AP60 . . . ribosomal protein L7a pseudogene 60 . . . . . . . . . . . RPL7AP61 . . . ribosomal protein L7a pseudogene 61 . . . . . . . . . . . RPL7AP62 . . . ribosomal protein L7a pseudogene 62 . . . . . . . . . . . RPL7AP63 . . . ribosomal protein L7a pseudogene 63 . . . . . . . . . . . RPL7AP64 . . . ribosomal protein L7a pseudogene 64 . . . . . . . . . . . RPL7AP65 . . . ribosomal protein L7a pseudogene 65 . . . . . . . . . . . RPL7AP66 . . . ribosomal protein L7a pseudogene 66 . . . . . . . . . . . RPL7AP67 . . . ribosomal protein L7a pseudogene 67 . . . . . . . . . . . RPL7AP69 . . . ribosomal protein L7a pseudogene 69 . . . . . . . . . . . RPL7AP70 . . . ribosomal protein L7a pseudogene 70 . . . . . . . . . . . RPL7AP71 . . . ribosomal protein L7a pseudogene 71 . . . . . . . . . . . RPL7AP72 . . . ribosomal protein L7a pseudogene 72 . . . . . . . . . . . RPL7AP73 . . . ribosomal protein L7a pseudogene 73 . . . . . . . . . . . RPL7L1 0.201503933112919 0.788557685409801 0.00993838147728024 ribosomal protein L7 like 1 . . . lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cerebellum; 0.10974 0.10449 -0.538132194 20.26421326 92.5444 2.06820 RPL7L1P1 . . . ribosomal protein L7 like 1 pseudogene 1 . . . . . . . . . . . RPL7L1P2 . . . ribosomal protein L7 like 1 pseudogene 2 . . . . . . . . . . . RPL7L1P3 . . . ribosomal protein L7 like 1 pseudogene 3 . . . . . . . . . . . RPL7L1P4 . . . ribosomal protein L7 like 1 pseudogene 4 . . . . . . . . . . . RPL7L1P5 . . . ribosomal protein L7 like 1 pseudogene 5 . . . . . . . . . . . RPL7L1P6 . . . ribosomal protein L7 like 1 pseudogene 6 . . . . . . . . . . . RPL7L1P7 . . . ribosomal protein L7 like 1 pseudogene 7 . . . . . . . . . . . RPL7L1P8 . . . ribosomal protein L7 like 1 pseudogene 8 . . . . . . . . . . . RPL7L1P9 . . . ribosomal protein L7 like 1 pseudogene 9 . . . . . . . . . . . RPL7L1P10 . . . ribosomal protein L7 like 1 pseudogene 10 . . . . . . . . . . . RPL7L1P11 . . . ribosomal protein L7 like 1 pseudogene 11 . . . . . . . . . . . RPL7L1P12 . . . ribosomal protein L7 like 1 pseudogene 12 . . . . . . . . . . . RPL7L1P13 . . . ribosomal protein L7 like 1 pseudogene 13 . . . . . . . . . . . RPL7P1 . . . ribosomal protein L7 pseudogene 1 . . . . . . . . . . . RPL7P2 . . . ribosomal protein L7 pseudogene 2 . . . . . . . . . . . RPL7P3 . . . ribosomal protein L7 pseudogene 3 . . . . . . . . . . . RPL7P4 . . . ribosomal protein L7 pseudogene 4 . . . . . . . . . . . RPL7P5 . . . ribosomal protein L7 pseudogene 5 . . . . . . . . . . . RPL7P6 . . . ribosomal protein L7 pseudogene 6 . . . . . . . . . . . RPL7P7 . . . ribosomal protein L7 pseudogene 7 . . . . . . . . . . . RPL7P8 . . . ribosomal protein L7 pseudogene 8 . . . . . . . . . . . RPL7P9 . . . ribosomal protein L7 pseudogene 9 . . . . . . . . . . . RPL7P10 . . . ribosomal protein L7 pseudogene 10 . . . . . . . . . . . RPL7P11 . . . ribosomal protein L7 pseudogene 11 . . . . . . . . . . . RPL7P12 . . . ribosomal protein L7 pseudogene 12 . . . . . . . . . . . RPL7P13 . . . ribosomal protein L7 pseudogene 13 . . . . . . . . . . . RPL7P14 . . . ribosomal protein L7 pseudogene 14 . . . . . . . . . . . RPL7P15 . . . ribosomal protein L7 pseudogene 15 . . . . . . . . . . . RPL7P16 . . . ribosomal protein L7 pseudogene 16 . . . . . . . . . . . RPL7P17 . . . ribosomal protein L7 pseudogene 17 . . . . . . . . . . . RPL7P18 . . . ribosomal protein L7 pseudogene 18 . . . . . . . . . . . RPL7P19 . . . ribosomal protein L7 pseudogene 19 . . . . . . . . . . . RPL7P20 . . . ribosomal protein L7 pseudogene 20 . . . . . . . . . . . RPL7P21 . . . ribosomal protein L7 pseudogene 21 . . . . . . . . . . . RPL7P22 . . . ribosomal protein L7 pseudogene 22 . . . . . . . . . . . RPL7P23 . . . ribosomal protein L7 pseudogene 23 . . . . . . . . . . . RPL7P24 . . . ribosomal protein L7 pseudogene 24 . . . . . . . . . . . RPL7P25 . . . ribosomal protein L7 pseudogene 25 . . . . . . . . . . . RPL7P26 . . . ribosomal protein L7 pseudogene 26 . . . . . . . . . . . RPL7P27 . . . ribosomal protein L7 pseudogene 27 . . . . . . . . . . . RPL7P28 . . . ribosomal protein L7 pseudogene 28 . . . . . . . . . . . RPL7P29 . . . ribosomal protein L7 pseudogene 29 . . . . . . . . . . . RPL7P30 . . . ribosomal protein L7 pseudogene 30 . . . . . . . . . . . RPL7P31 . . . ribosomal protein L7 pseudogene 31 . . . . . . . . . . . RPL7P32 . . . ribosomal protein L7 pseudogene 32 . . . . . . . . . . . RPL7P33 . . . ribosomal protein L7 pseudogene 33 . . . . . . . . . . . RPL7P34 . . . ribosomal protein L7 pseudogene 34 . . . . . . . . . . . RPL7P35 . . . ribosomal protein L7 pseudogene 35 . . . . . . . . . . . RPL7P36 . . . ribosomal protein L7 pseudogene 36 . . . . . . . . . . . RPL7P37 . . . ribosomal protein L7 pseudogene 37 . . . . . . . . . . . RPL7P38 . . . ribosomal protein L7 pseudogene 38 . . . . . . . . . . . RPL7P39 . . . ribosomal protein L7 pseudogene 39 . . . . . . . . . . . RPL7P40 . . . ribosomal protein L7 pseudogene 40 . . . . . . . . . . . RPL7P41 . . . ribosomal protein L7 pseudogene 41 . . . . . . . . . . . RPL7P42 . . . ribosomal protein L7 pseudogene 42 . . . . . . . . . . . RPL7P43 . . . ribosomal protein L7 pseudogene 43 . . . . . . . . . . . RPL7P44 . . . ribosomal protein L7 pseudogene 44 . . . . . . . . . . . RPL7P45 . . . ribosomal protein L7 pseudogene 45 . . . . . . . . . . . RPL7P46 . . . ribosomal protein L7 pseudogene 46 . . . . . . . . . . . RPL7P47 . . . ribosomal protein L7 pseudogene 47 . . . . . . . . . . . RPL7P48 . . . ribosomal protein L7 pseudogene 48 . . . . . . . . . . . RPL7P49 . . . ribosomal protein L7 pseudogene 49 . . . . . . . . . . . RPL7P50 . . . ribosomal protein L7 pseudogene 50 . . . . . . . . . . . RPL7P51 . . . ribosomal protein L7 pseudogene 51 . . . . . . . . . . . RPL7P52 . . . ribosomal protein L7 pseudogene 52 . . . . . . . . . . . RPL7P53 . . . ribosomal protein L7 pseudogene 53 . . . . . . . . . . . RPL7P54 . . . ribosomal protein L7 pseudogene 54 . . . . . . . . . . . RPL7P55 . . . ribosomal protein L7 pseudogene 55 . . . . . . . . . . . RPL7P56 . . . ribosomal protein L7 pseudogene 56 . . . . . . . . . . . RPL7P57 . . . ribosomal protein L7 pseudogene 57 . . . . . . . . . . . RPL7P58 . . . ribosomal protein L7 pseudogene 58 . . . . . . . . . . . RPL7P59 . . . ribosomal protein L7 pseudogene 59 . . . . . . . . . . . RPL7P60 . . . ribosomal protein L7 pseudogene 60 . . . . . . . . . . . RPL7P61 . . . ribosomal protein L7 pseudogene 61 . . . . . . . . . . . RPL8 0.93269341315758 0.0669792096038094 0.000327377238610403 ribosomal protein L8 . . . lymphoreticular;myocardium;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;endometrium;bone;pituitary gland;testis;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;epididymis;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; uterus;pancreas;prostate;lung;heart;thyroid;liver;tumor;white blood cells; 0.93269 . -0.205617011 38.57631517 51.82189 1.42167 RPL8P1 . . . ribosomal protein L8 pseudogene 1 . . . . . . . . . . . RPL8P2 . . . ribosomal protein L8 pseudogene 2 . . . . . . . . . . . RPL8P3 . . . ribosomal protein L8 pseudogene 3 . . . . . . . . . . . RPL8P4 . . . ribosomal protein L8 pseudogene 4 . . . . . . . . . . . RPL8P5 . . . ribosomal protein L8 pseudogene 5 . . . . . . . . . . . RPL9 0.918456437508184 0.0810116285875558 0.000531933904259829 ribosomal protein L9 . . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;oesophagus;bone;thyroid;pituitary gland;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;trabecular meshwork;placenta;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; . 0.99267 0.10690 -0.163345027 41.24793583 8.97949 0.32975 RPL9P2 . . . ribosomal protein L9 pseudogene 2 . . . . . . . . . . . RPL9P3 . . . ribosomal protein L9 pseudogene 3 . . . . . . . . . . . RPL9P4 . . . ribosomal protein L9 pseudogene 4 . . . . . . . . . . . RPL9P5 . . . ribosomal protein L9 pseudogene 5 . . . . . . . . . . . RPL9P6 . . . ribosomal protein L9 pseudogene 6 . . . . . . . . . . . RPL9P7 . . . ribosomal protein L9 pseudogene 7 . . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;retina;uterus;prostate;frontal lobe;endometrium;oesophagus;bone;thyroid;pituitary gland;testis;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;aorta; . . . . . . . RPL9P8 . . . ribosomal protein L9 pseudogene 8 . . . . . . . . . . . RPL9P9 . . . ribosomal protein L9 pseudogene 9 . . . . . . . . . . . RPL9P10 . . . ribosomal protein L9 pseudogene 10 . . . . . . . . . . . RPL9P11 . . . ribosomal protein L9 pseudogene 11 . . . . . . . . . . . RPL9P12 . . . ribosomal protein L9 pseudogene 12 . . . . . . . . . . . RPL9P13 . . . ribosomal protein L9 pseudogene 13 . . . . . . . . . . . RPL9P14 . . . ribosomal protein L9 pseudogene 14 . . . . . . . . . . . RPL9P15 . . . ribosomal protein L9 pseudogene 15 . . . . . . . . . . . RPL9P16 . . . ribosomal protein L9 pseudogene 16 . . . . . . . . . . . RPL9P17 . . . ribosomal protein L9 pseudogene 17 . . . . . . . . . . . RPL9P18 . . . ribosomal protein L9 pseudogene 18 . . . . . . . . . . . RPL9P19 . . . ribosomal protein L9 pseudogene 19 . . . . . . . . . . . RPL9P20 . . . ribosomal protein L9 pseudogene 20 . . . . . . . . . . . RPL9P21 . . . ribosomal protein L9 pseudogene 21 . . . . . . . . . . . RPL9P22 . . . ribosomal protein L9 pseudogene 22 . . . . . . . . . . . RPL9P23 . . . ribosomal protein L9 pseudogene 23 . . . . . . . . . . . RPL9P24 . . . ribosomal protein L9 pseudogene 24 . . . . . . . . . . . RPL9P25 . . . ribosomal protein L9 pseudogene 25 . . . . . . . . . . . RPL9P26 . . . ribosomal protein L9 pseudogene 26 . . . . . . . . . . . RPL9P27 . . . ribosomal protein L9 pseudogene 27 . . . . . . . . . . . RPL9P28 . . . ribosomal protein L9 pseudogene 28 . . . . . . . . . . . RPL9P29 . . . ribosomal protein L9 pseudogene 29 . . . . . . . . . . . RPL9P30 . . . ribosomal protein L9 pseudogene 30 . . . . . . . . . . . RPL9P31 . . . ribosomal protein L9 pseudogene 31 . . . . . . . . . . . RPL9P32 . . . ribosomal protein L9 pseudogene 32 . . . . . . . . . . . RPL9P33 . . . ribosomal protein L9 pseudogene 33 . . . . . . . . . . . RPL10 0.90119329809699 0.0979388987849578 0.00086780311805227 ribosomal protein L10 . DISEASE: Autism, X-linked 5 (AUTSX5) [MIM:300847]: A complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation. {ECO:0000269|PubMed:16940977, ECO:0000269|PubMed:21567917}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. RPL10 is involved in autism only in rare cases. Two hypomorphic variants affecting the translation process have been found in families with autism spectrum disorders, suggesting that aberrant translation may play a role in disease mechanisms.; . umbilical cord;ovary;salivary gland;intestine;colon;skin;bone marrow;prostate;endometrium;bone;testis;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;spinal cord;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;pia mater;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;skeletal muscle; 0.28076 0.38095 0.035072054 56.2514744 2.20183 0.07345 RPL10A 0.30237883059711 0.6785986534763 0.0190225159265897 ribosomal protein L10a . . . . . 0.89137 . -0.185391282 39.67916962 2.4123 0.08544 RPL10AP1 . . . ribosomal protein L10a pseudogene 1 . . . . . . . . . . . RPL10AP2 . . . ribosomal protein L10a pseudogene 2 . . . . . . . . . . . RPL10AP3 . . . ribosomal protein L10a pseudogene 3 . . . . . . . . . . . RPL10AP4 . . . ribosomal protein L10a pseudogene 4 . . . . . . . . . . . RPL10AP5 . . . ribosomal protein L10a pseudogene 5 . . . . . . . . . . . RPL10AP6 . . . ribosomal protein L10a pseudogene 6 . . . . . . . . . . . RPL10AP7 . . . ribosomal protein L10a pseudogene 7 . . . . . . . . . . . RPL10AP8 . . . ribosomal protein L10a pseudogene 8 . . . . . . . . . . . RPL10AP9 . . . ribosomal protein L10a pseudogene 9 . . . . . . . . . . . RPL10AP10 . . . ribosomal protein L10a pseudogene 10 . . . . . . . . . . . RPL10AP11 . . . ribosomal protein L10a pseudogene 11 . . . . . . . . . . . RPL10AP12 . . . ribosomal protein L10a pseudogene 12 . . . . . . . . . . . RPL10AP13 . . . ribosomal protein L10a pseudogene 13 . . . . . . . . . . . RPL10L 0.0260549200341443 0.787247685760333 0.186697394205523 ribosomal protein L10 like FUNCTION: May play a role in compensating for the inactivated X- linked gene during spermatogenesis. {ECO:0000269|PubMed:12490704}.; . . unclassifiable (Anatomical System);medulla oblongata;testis; testis - interstitial;testis - seminiferous tubule;heart;liver;testis; 0.97891 0.12334 0.17280645 65.75843359 88.18617 2.01137 RPL10P1 . . . ribosomal protein L10 pseudogene 1 . . . . . . . . . . . RPL10P2 . . . ribosomal protein L10 pseudogene 2 . . . . . . . . . . . RPL10P3 . . . ribosomal protein L10 pseudogene 3 . . . . . . . . . . . RPL10P5 . . . ribosomal protein L10 pseudogene 5 . . . . . . . . . . . RPL10P7 . . . ribosomal protein L10 pseudogene 7 . . . . . . . . . . . RPL10P9 . . . ribosomal protein L10 pseudogene 9 . . . . . . . . . . . RPL10P10 . . . ribosomal protein L10 pseudogene 10 . . . . . . . . . . . RPL10P11 . . . ribosomal protein L10 pseudogene 11 . . . . . . . . . . . RPL10P14 . . . ribosomal protein L10 pseudogene 14 . . . . . . . . . . . RPL10P16 . . . ribosomal protein L10 pseudogene 16 . . . . . . . . . . . RPL11 0.725843320629066 0.271290851951151 0.00286582741978335 ribosomal protein L11 FUNCTION: Binds to 5S ribosomal RNA (By similarity). Required for rRNA maturation and formation of the 60S ribosomal subunits. Promotes nucleolar location of PML (By similarity). {ECO:0000250, ECO:0000269|PubMed:19061985}.; DISEASE: Diamond-Blackfan anemia 7 (DBA7) [MIM:612562]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. {ECO:0000269|PubMed:19061985, ECO:0000269|PubMed:19191325}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.91293 . -0.053113545 49.38664779 5.48246 0.20413 RPL11P1 . . . ribosomal protein L11 pseudogene 1 . . . . . . . . . . . RPL11P2 . . . ribosomal protein L11 pseudogene 2 . . . . . . . . . . . RPL11P3 . . . ribosomal protein L11 pseudogene 3 . . . . . . . . . . . RPL11P4 . . . ribosomal protein L11 pseudogene 4 . . . . . . . . . . . RPL11P5 . . . ribosomal protein L11 pseudogene 5 . . . . . . . . . . . RPL12 0.164356184673043 0.820955364798705 0.0146884505282513 ribosomal protein L12 FUNCTION: Binds directly to 26S ribosomal RNA. {ECO:0000250}.; . . lymphoreticular;ovary;skin;retina;prostate;frontal lobe;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;oesophagus;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;duodenum;kidney;stomach;aorta;cerebellum; . . . 0.103030231 61.2762444 8.46195 0.30991 RPL12P1 . . . ribosomal protein L12 pseudogene 1 . . . . . . . . . . . RPL12P2 . . . ribosomal protein L12 pseudogene 2 . . . . . . . . . . . RPL12P3 . . . ribosomal protein L12 pseudogene 3 . . . . . . . . . . . RPL12P4 . . . ribosomal protein L12 pseudogene 4 . . . . . . . . . . . RPL12P5 . . . ribosomal protein L12 pseudogene 5 . . . . . . . . . . . RPL12P6 . . . ribosomal protein L12 pseudogene 6 . . . . . . . . . . . RPL12P7 . . . ribosomal protein L12 pseudogene 7 . . . . . . . . . . . RPL12P8 . . . ribosomal protein L12 pseudogene 8 . . . . . . . . . . . RPL12P9 . . . ribosomal protein L12 pseudogene 9 . . . . . . . . . . . RPL12P10 . . . ribosomal protein L12 pseudogene 10 . . . . . . . . . . . RPL12P11 . . . ribosomal protein L12 pseudogene 11 . . . . . . . . . . . RPL12P12 . . . ribosomal protein L12 pseudogene 12 . . . . . . . . . . . RPL12P13 . . . ribosomal protein L12 pseudogene 13 . . . . . . . . . . . RPL12P14 . . . ribosomal protein L12 pseudogene 14 . . . . . . . . . . . RPL12P15 . . . ribosomal protein L12 pseudogene 15 . . . . . . . . . . . RPL12P16 . . . ribosomal protein L12 pseudogene 16 . . . . . . . . . . . RPL12P17 . . . ribosomal protein L12 pseudogene 17 . . . . . . . . . . . RPL12P18 . . . ribosomal protein L12 pseudogene 18 . . . . . . . . . . . RPL12P19 . . . ribosomal protein L12 pseudogene 19 . . . . . . . . . . . RPL12P20 . . . ribosomal protein L12 pseudogene 20 . . . . . . . . . . . RPL12P21 . . . ribosomal protein L12 pseudogene 21 . . . . . . . . . . . RPL12P22 . . . ribosomal protein L12 pseudogene 22 . . . . . . . . . . . RPL12P23 . . . ribosomal protein L12 pseudogene 23 . . . . . . . . . . . RPL12P24 . . . ribosomal protein L12 pseudogene 24 . . . . . . . . . . . RPL12P25 . . . ribosomal protein L12 pseudogene 25 . . . . . . . . . . . RPL12P26 . . . ribosomal protein L12 pseudogene 26 . . . . . . . . . . . RPL12P27 . . . ribosomal protein L12 pseudogene 27 . . . . . . . . . . . RPL12P28 . . . ribosomal protein L12 pseudogene 28 . . . . . . . . . . . RPL12P29 . . . ribosomal protein L12 pseudogene 29 . . . . . . . . . . . RPL12P30 . . . ribosomal protein L12 pseudogene 30 . . . . . . . . . . . RPL12P31 . . . ribosomal protein L12 pseudogene 31 . . . . . . . . . . . RPL12P32 . . . ribosomal protein L12 pseudogene 32 . . . . . . . . . . . RPL12P33 . . . ribosomal protein L12 pseudogene 33 . . . . . . . . . . . RPL12P34 . . . ribosomal protein L12 pseudogene 34 . . . . . . . . . . . RPL12P35 . . . ribosomal protein L12 pseudogene 35 . . . . . . . . . . . RPL12P36 . . . ribosomal protein L12 pseudogene 36 . . . . . . . . . . . RPL12P37 . . . ribosomal protein L12 pseudogene 37 . . . . . . . . . . . RPL12P38 . . . ribosomal protein L12 pseudogene 38 . . . . . . . . . . . RPL12P39 . . . ribosomal protein L12 pseudogene 39 . . . . . . . . . . . RPL12P40 . . . ribosomal protein L12 pseudogene 40 . . . . . . . . . . . RPL12P41 . . . ribosomal protein L12 pseudogene 41 . . . . . . . . . . . RPL12P42 . . . ribosomal protein L12 pseudogene 42 . . . . . . . . . . . RPL12P43 . . . ribosomal protein L12 pseudogene 43 . . . . . . . . . . . RPL12P44 . . . ribosomal protein L12 pseudogene 44 . . . . . . . . . . . RPL12P45 . . . ribosomal protein L12 pseudogene 45 . . . . . . . . . . . RPL12P46 . . . ribosomal protein L12 pseudogene 46 . . . . . . . . . . . RPL12P47 . . . ribosomal protein L12 pseudogene 47 . . . . . . . . . . . RPL12P48 . . . ribosomal protein L12 pseudogene 48 . . . . . . . . . . . RPL12P49 . . . ribosomal protein L12 pseudogene 49 . . . . . . . . . . . RPL12P50 . . . ribosomal protein L12 pseudogene 50 . . . . . . . . . . . RPL13 0.914867444922444 0.084539101198125 0.000593453879431306 ribosomal protein L13 . . TISSUE SPECIFICITY: Higher levels of expression in benign breast lesions than in carcinomas.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;skin;uterus;prostate;frontal lobe;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;urinary;pharynx;blood;breast;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;prostate;liver;atrioventricular node;pons;trigeminal ganglion; 0.76022 0.19477 0.060756528 58.52795471 770.99247 5.49543 RPL13A 0.633828368843267 0.364723050451334 0.00144858070539883 ribosomal protein L13a FUNCTION: Associated with ribosomes but is not required for canonical ribosome function and has extra-ribosomal functions. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the ribosome and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. In the GAIT complex interacts with m7G cap-bound eIF4G at or near the eIF3-binding site and blocks the recruitment of the 43S ribosomal complex. Involved in methylation of rRNA. {ECO:0000269|PubMed:14567916, ECO:0000269|PubMed:17218275, ECO:0000269|PubMed:17921318, ECO:0000269|PubMed:23071094}.; . . . . 0.75208 0.26526 -0.427900189 25.14744043 . . RPL13AP . . . ribosomal protein L13a pseudogene . . . . . . . . . . . RPL13AP2 . . . ribosomal protein L13a pseudogene 2 . . . . . . . . . . . RPL13AP3 . . . ribosomal protein L13a pseudogene 3 . . . . . . . . . . . RPL13AP5 . . . ribosomal protein L13a pseudogene 5 . . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;visual apparatus;liver;cervix;kidney;mammary gland;stomach;peripheral nerve; . . . . . . . RPL13AP6 . . . ribosomal protein L13a pseudogene 6 . . . . . . . . . . . RPL13AP7 . . . ribosomal protein L13a pseudogene 7 . . . . . . . . . . . RPL13AP8 . . . ribosomal protein L13a pseudogene 8 . . . . . . . . . . . RPL13AP9 . . . ribosomal protein L13a pseudogene 9 . . . . . . . . . . . RPL13AP10 . . . ribosomal protein L13a pseudogene 10 . . . . . . . . . . . RPL13AP11 . . . ribosomal protein L13a pseudogene 11 . . . . . . . . . . . RPL13AP12 . . . ribosomal protein L13a pseudogene 12 . . . . . . . . . . . RPL13AP13 . . . ribosomal protein L13a pseudogene 13 . . . . . . . . . . . RPL13AP14 . . . ribosomal protein L13a pseudogene 14 . . . . . . . . . . . RPL13AP15 . . . ribosomal protein L13a pseudogene 15 . . . . . . . . . . . RPL13AP16 . . . ribosomal protein L13a pseudogene 16 . . . . . . . . . . . RPL13AP17 . . . ribosomal protein L13a pseudogene 17 . . . . . . . . . . . RPL13AP18 . . . ribosomal protein L13a pseudogene 18 . . . . . . . . . . . RPL13AP19 . . . ribosomal protein L13a pseudogene 19 . . . . . . . . . . . RPL13AP20 . . . ribosomal protein L13a pseudogene 20 . . . . . . . . . . . RPL13AP21 . . . ribosomal protein L13a pseudogene 21 . . . . . . . . . . . RPL13AP22 . . . ribosomal protein L13a pseudogene 22 . . . . . . . . . . . RPL13AP23 . . . ribosomal protein L13a pseudogene 23 . . . . . . . . . . . RPL13AP24 . . . ribosomal protein L13a pseudogene 24 . . . . . . . . . . . RPL13AP25 . . . ribosomal protein L13a pseudogene 25 . . . . . . . . . . . RPL13AP26 . . . ribosomal protein L13a pseudogene 26 . . . . . . . . . . . RPL13P . . . ribosomal protein L13 pseudogene . . . . . . . . . . . RPL13P2 . . . ribosomal protein L13 pseudogene 2 . . . . . . . . . . . RPL13P4 . . . ribosomal protein L13 pseudogene 4 . . . . . . . . . . . RPL13P5 . . . ribosomal protein L13 pseudogene 5 . . . unclassifiable (Anatomical System);lung;visual apparatus;testis;spinal ganglion;brain;mammary gland; . . . . . . . RPL13P6 . . . ribosomal protein L13 pseudogene 6 . . . . . . . . . . . RPL13P7 . . . ribosomal protein L13 pseudogene 7 . . . . . . . . . . . RPL13P8 . . . ribosomal protein L13 pseudogene 8 . . . . . . . . . . . RPL13P9 . . . ribosomal protein L13 pseudogene 9 . . . . . . . . . . . RPL13P10 . . . ribosomal protein L13 pseudogene 10 . . . . . . . . . . . RPL13P11 . . . ribosomal protein L13 pseudogene 11 . . . . . . . . . . . RPL13P12 . . . ribosomal protein L13 pseudogene 12 . . . . . . . . . . . RPL13P13 . . . ribosomal protein L13 pseudogene 13 . . . . . . . . . . . RPL13P14 . . . ribosomal protein L13 pseudogene 14 . . . . . . . . . . . RPL14 0.936435427719195 0.0632811265156858 0.000283445765119322 ribosomal protein L14 . . . . . 0.97593 0.19170 0.25917371 70.05779665 380.83848 4.11312 RPL14P1 . . . ribosomal protein L14 pseudogene 1 . . . lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;bladder;brain;tonsil;heart;spinal cord;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;synovium;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;muscle;pancreas;pia mater;lung;cornea;adrenal gland;placenta;duodenum;amnion;kidney;stomach;aorta;thymus; . 0.19709 0.09860 . . . . RPL14P2 . . . ribosomal protein L14 pseudogene 2 . . . . . . . . . . . RPL14P3 . . . ribosomal protein L14 pseudogene 3 . . . . . . . . . . . RPL14P4 . . . ribosomal protein L14 pseudogene 4 . . . . . . . . . . . RPL14P5 . . . ribosomal protein L14 pseudogene 5 . . . . . . . . . . . RPL15 0.956294173685839 0.0435948647651595 0.000110961549001325 ribosomal protein L15 . DISEASE: Diamond-Blackfan anemia 12 (DBA12) [MIM:615550]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. {ECO:0000269|PubMed:23812780}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;umbilical cord;sympathetic chain;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;bone;pituitary gland;testis;pineal gland;spinal ganglion;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; amygdala;occipital lobe;thalamus;subthalamic nucleus;medulla oblongata;fetal brain;cerebellum peduncles;hypothalamus;temporal lobe;globus pallidus;pons;parietal lobe; 0.48147 0.17050 -0.075159878 47.78839349 17.7554 0.62078 RPL15P1 . . . ribosomal protein L15 pseudogene 1 . . . . . . . . . . . RPL15P2 . . . ribosomal protein L15 pseudogene 2 . . . . . . . . . . . RPL15P3 . . . ribosomal protein L15 pseudogene 3 . . . . . . . . . . . RPL15P4 . . . ribosomal protein L15 pseudogene 4 . . . . . . . . . . . RPL15P5 . . . ribosomal protein L15 pseudogene 5 . . . . . . . . . . . RPL15P6 . . . ribosomal protein L15 pseudogene 6 . . . . . . . . . . . RPL15P7 . . . ribosomal protein L15 pseudogene 7 . . . . . . . . . . . RPL15P8 . . . ribosomal protein L15 pseudogene 8 . . . . . . . . . . . RPL15P9 . . . ribosomal protein L15 pseudogene 9 . . . . . . . . . . . RPL15P11 . . . ribosomal protein L15 pseudogene 11 . . . . . . . . . . . RPL15P12 . . . ribosomal protein L15 pseudogene 12 . . . . . . . . . . . RPL15P13 . . . ribosomal protein L15 pseudogene 13 . . . . . . . . . . . RPL15P14 . . . ribosomal protein L15 pseudogene 14 . . . . . . . . . . . RPL15P15 . . . ribosomal protein L15 pseudogene 15 . . . . . . . . . . . RPL15P16 . . . ribosomal protein L15 pseudogene 16 . . . . . . . . . . . RPL15P17 . . . ribosomal protein L15 pseudogene 17 . . . . . . . . . . . RPL15P18 . . . ribosomal protein L15 pseudogene 18 . . . . . . . . . . . RPL15P20 . . . ribosomal protein L15 pseudogene 20 . . . . . . . . . . . RPL15P21 . . . ribosomal protein L15 pseudogene 21 . . . . . . . . . . . RPL15P22 . . . ribosomal protein L15 pseudogene 22 . . . . . . . . . . . RPL17 0.494059426420399 0.501442148400947 0.0044984251786533 ribosomal protein L17 . . TISSUE SPECIFICITY: Expressed in pancreas, lung, colon, cystic duct, gall bladder, kidney and liver. Expressed at high levels in the well differentiated pancreatic tumor cell lines HPAF, COLO 357 and Capan-1, the moderately differentiated pancreatic tumor cell lines T3M-4, AsPc-1 and BxPc-3, the poorly differentiated pancreatic tumor cell line MIA PaCa-2, and the pancreatic tumor cell lines of undefined differentiation status such as SW979. Expressed at lower levels in the poorly differentiated pancreatic tumor cell lines HCG-25 and PANC-1. {ECO:0000269|PubMed:1793733}.; . . 0.33905 0.08190 -0.09720619 46.20193442 . . RPL17-C18orf32 0.605942171595584 0.392213355703088 0.00184447270132857 RPL17-C18orf32 readthrough . . TISSUE SPECIFICITY: Expressed in pancreas, lung, colon, cystic duct, gall bladder, kidney and liver. Expressed at high levels in the well differentiated pancreatic tumor cell lines HPAF, COLO 357 and Capan-1, the moderately differentiated pancreatic tumor cell lines T3M-4, AsPc-1 and BxPc-3, the poorly differentiated pancreatic tumor cell line MIA PaCa-2, and the pancreatic tumor cell lines of undefined differentiation status such as SW979. Expressed at lower levels in the poorly differentiated pancreatic tumor cell lines HCG-25 and PANC-1. {ECO:0000269|PubMed:1793733}.; . . . . . . 101.37142 2.17973 RPL17P1 . . . ribosomal protein L17 pseudogene 1 . . . . . . . . . . . RPL17P2 . . . ribosomal protein L17 pseudogene 2 . . . . . . . . . . . RPL17P3 . . . ribosomal protein L17 pseudogene 3 . . . . . . . . . . . RPL17P4 . . . ribosomal protein L17 pseudogene 4 . . . . . . . . . . . RPL17P5 . . . ribosomal protein L17 pseudogene 5 . . . . . . . . . . . RPL17P6 . . . ribosomal protein L17 pseudogene 6 . . . . . . . . . . . RPL17P7 . . . ribosomal protein L17 pseudogene 7 . . . . . . . . . . . RPL17P8 . . . ribosomal protein L17 pseudogene 8 . . . . . . . . . . . RPL17P9 . . . ribosomal protein L17 pseudogene 9 . . . . . . . . . . . RPL17P10 . . . ribosomal protein L17 pseudogene 10 . . . . . . . . . . . RPL17P11 . . . ribosomal protein L17 pseudogene 11 . . . . . . . . . . . RPL17P12 . . . ribosomal protein L17 pseudogene 12 . . . . . . . . . . . RPL17P13 . . . ribosomal protein L17 pseudogene 13 . . . . . . . . . . . RPL17P14 . . . ribosomal protein L17 pseudogene 14 . . . . . . . . . . . RPL17P15 . . . ribosomal protein L17 pseudogene 15 . . . . . . . . . . . RPL17P16 . . . ribosomal protein L17 pseudogene 16 . . . . . . . . . . . RPL17P17 . . . ribosomal protein L17 pseudogene 17 . . . . . . . . . . . RPL17P18 . . . ribosomal protein L17 pseudogene 18 . . . . . . . . . . . RPL17P19 . . . ribosomal protein L17 pseudogene 19 . . . . . . . . . . . RPL17P20 . . . ribosomal protein L17 pseudogene 20 . . . . . . . . . . . RPL17P21 . . . ribosomal protein L17 pseudogene 21 . . . . . . . . . . . RPL17P22 . . . ribosomal protein L17 pseudogene 22 . . . . . . . . . . . RPL17P23 . . . ribosomal protein L17 pseudogene 23 . . . . . . . . . . . RPL17P24 . . . ribosomal protein L17 pseudogene 24 . . . . . . . . . . . RPL17P25 . . . ribosomal protein L17 pseudogene 25 . . . . . . . . . . . RPL17P26 . . . ribosomal protein L17 pseudogene 26 . . . . . . . . . . . RPL17P27 . . . ribosomal protein L17 pseudogene 27 . . . . . . . . . . . RPL17P28 . . . ribosomal protein L17 pseudogene 28 . . . . . . . . . . . RPL17P29 . . . ribosomal protein L17 pseudogene 29 . . . . . . . . . . . RPL17P30 . . . ribosomal protein L17 pseudogene 30 . . . . . . . . . . . RPL17P31 . . . ribosomal protein L17 pseudogene 31 . . . . . . . . . . . RPL17P32 . . . ribosomal protein L17 pseudogene 32 . . . . . . . . . . . RPL17P33 . . . ribosomal protein L17 pseudogene 33 . . . . . . . . . . . RPL17P34 . . . ribosomal protein L17 pseudogene 34 . . . . . . . . . . . RPL17P35 . . . ribosomal protein L17 pseudogene 35 . . . . . . . . . . . RPL17P36 . . . ribosomal protein L17 pseudogene 36 . . . . . . . . . . . RPL17P37 . . . ribosomal protein L17 pseudogene 37 . . . . . . . . . . . RPL17P38 . . . ribosomal protein L17 pseudogene 38 . . . . . . . . . . . RPL17P39 . . . ribosomal protein L17 pseudogene 39 . . . . . . . . . . . RPL17P40 . . . ribosomal protein L17 pseudogene 40 . . . . . . . . . . . RPL17P41 . . . ribosomal protein L17 pseudogene 41 . . . . . . . . . . . RPL17P42 . . . ribosomal protein L17 pseudogene 42 . . . . . . . . . . . RPL17P43 . . . ribosomal protein L17 pseudogene 43 . . . . . . . . . . . RPL17P44 . . . ribosomal protein L17 pseudogene 44 . . . . . . . . . . . RPL17P45 . . . ribosomal protein L17 pseudogene 45 . . . . . . . . . . . RPL17P46 . . . ribosomal protein L17 pseudogene 46 . . . . . . . . . . . RPL17P47 . . . ribosomal protein L17 pseudogene 47 . . . . . . . . . . . RPL17P48 . . . ribosomal protein L17 pseudogene 48 . . . . . . . . . . . RPL17P49 . . . ribosomal protein L17 pseudogene 49 . . . . . . . . . . . RPL17P50 . . . ribosomal protein L17 pseudogene 50 . . . . . . . . . . . RPL17P51 . . . ribosomal protein L17 pseudogene 51 . . . . . . . . . . . RPL18 0.554781180671353 0.442411564243936 0.00280725508471075 ribosomal protein L18 . . . lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;kidney;stomach;aorta;thymus; subthalamic nucleus;prostate;superior cervical ganglion;lung;ovary;heart;thyroid;liver;adrenal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.86855 0.20297 -0.251530012 35.42108988 . . RPL18A 0.963491173324846 0.036437903201023 7.09234741307386e-05 ribosomal protein L18a . . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;frontal lobe;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;muscle;pharynx;blood;bile duct;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.64483 0.12930 -0.317668748 31.45789101 11.44037 0.41344 RPL18AP1 . . . ribosomal protein L18a pseudogene 1 . . . . . . . . . . . RPL18AP2 . . . ribosomal protein L18a pseudogene 2 . . . . . . . . . . . RPL18AP3 . . . ribosomal protein L18a pseudogene 3 . . . . . . . . . . . RPL18AP4 . . . ribosomal protein L18a pseudogene 4 . . . . . . . . . . . RPL18AP5 . . . ribosomal protein L18a pseudogene 5 . . . . . . . . . . . RPL18AP6 . . . ribosomal protein L18a pseudogene 6 . . . . . . . . . . . RPL18AP7 . . . ribosomal protein L18a pseudogene 7 . . . . . . . . . . . RPL18AP8 . . . ribosomal protein L18a pseudogene 8 . . . . . . . . . . . RPL18AP10 . . . ribosomal protein L18a pseudogene 10 . . . . . . . . . . . RPL18AP11 . . . ribosomal protein L18a pseudogene 11 . . . . . . . . . . . RPL18AP12 . . . ribosomal protein L18a pseudogene 12 . . . . . . . . . . . RPL18AP13 . . . ribosomal protein L18a pseudogene 13 . . . . . . . . . . . RPL18AP14 . . . ribosomal protein L18a pseudogene 14 . . . . . . . . . . . RPL18AP15 . . . ribosomal protein L18a pseudogene 15 . . . . . . . . . . . RPL18AP16 . . . ribosomal protein L18a pseudogene 16 . . . . . . . . . . . RPL18AP17 . . . ribosomal protein L18a pseudogene 17 . . . . . . . . . . . RPL18P1 . . . ribosomal protein L18 pseudogene 1 . . . . . . . . . . . RPL18P2 . . . ribosomal protein L18 pseudogene 2 . . . . . . . . . . . RPL18P3 . . . ribosomal protein L18 pseudogene 3 . . . . . . . . . . . RPL18P4 . . . ribosomal protein L18 pseudogene 4 . . . . . . . . . . . RPL18P5 . . . ribosomal protein L18 pseudogene 5 . . . . . . . . . . . RPL18P6 . . . ribosomal protein L18 pseudogene 6 . . . . . . . . . . . RPL18P7 . . . ribosomal protein L18 pseudogene 7 . . . . . . . . . . . RPL18P8 . . . ribosomal protein L18 pseudogene 8 . . . . . . . . . . . RPL18P9 . . . ribosomal protein L18 pseudogene 9 . . . . . . . . . . . RPL18P10 . . . ribosomal protein L18 pseudogene 10 . . . . . . . . . . . RPL18P11 . . . ribosomal protein L18 pseudogene 11 . . . . . . . . . . . RPL18P12 . . . ribosomal protein L18 pseudogene 12 . . . . . . . . . . . RPL18P13 . . . ribosomal protein L18 pseudogene 13 . . . . . . . . . . . RPL19 0.974448375215553 0.0255223105851913 2.93141992559808e-05 ribosomal protein L19 . . . lymphoreticular;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;synovium;thyroid;testis;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;heart;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach; . 0.25391 0.22085 0.013025609 54.62962963 1.18187 0.03411 RPL19P1 . . . ribosomal protein L19 pseudogene 1 . . . . . . . . . . . RPL19P2 . . . ribosomal protein L19 pseudogene 2 . . . . . . . . . . . RPL19P3 . . . ribosomal protein L19 pseudogene 3 . . . . . . . . . . . RPL19P4 . . . ribosomal protein L19 pseudogene 4 . . . . . . . . . . . RPL19P5 . . . ribosomal protein L19 pseudogene 5 . . . . . . . . . . . RPL19P6 . . . ribosomal protein L19 pseudogene 6 . . . . . . . . . . . RPL19P7 . . . ribosomal protein L19 pseudogene 7 . . . . . . . . . . . RPL19P8 . . . ribosomal protein L19 pseudogene 8 . . . . . . . . . . . RPL19P9 . . . ribosomal protein L19 pseudogene 9 . . . . . . . . . . . RPL19P10 . . . ribosomal protein L19 pseudogene 10 . . . . . . . . . . . RPL19P11 . . . ribosomal protein L19 pseudogene 11 . . . . . . . . . . . RPL19P12 . . . ribosomal protein L19 pseudogene 12 . . . . . . . . . . . RPL19P13 . . . ribosomal protein L19 pseudogene 13 . . . . . . . . . . . RPL19P14 . . . ribosomal protein L19 pseudogene 14 . . . . . . . . . . . RPL19P15 . . . ribosomal protein L19 pseudogene 15 . . . . . . . . . . . RPL19P16 . . . ribosomal protein L19 pseudogene 16 . . . . . . . . . . . RPL19P17 . . . ribosomal protein L19 pseudogene 17 . . . . . . . . . . . RPL19P18 . . . ribosomal protein L19 pseudogene 18 . . . . . . . . . . . RPL19P19 . . . ribosomal protein L19 pseudogene 19 . . . . . . . . . . . RPL19P20 . . . ribosomal protein L19 pseudogene 20 . . . . . . . . . . . RPL19P21 . . . ribosomal protein L19 pseudogene 21 . . . . . . . . . . . RPL21 0.920443069002851 0.0790572682099256 0.000499662787222928 ribosomal protein L21 . DISEASE: Hypotrichosis 12 (HYPT12) [MIM:615885]: A form of hypotrichosis, a condition characterized by the presence of less than the normal amount of hair and abnormal hair follicles and shafts, which are thin and atrophic. The extent of scalp and body hair involvement can be very variable, within as well as between families. HYPT12 patients have normal scalp hair density at birth. Hair loss begins during the first 6 months of life and gradually progresses to nearly complete loss of scalp hair. The remaining hairs grow slowly and are thin, sparse, dry, and fragile. Body hair, axillary and pubic hair, eyebrows and eyelashes are also sparse or absent. {ECO:0000269|PubMed:21412954}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.30374 0.20650 0.057118534 57.99716914 1.21425 0.03881 RPL21P1 . . . ribosomal protein L21 pseudogene 1 . . . . . . . . . . . RPL21P2 . . . ribosomal protein L21 pseudogene 2 . . . . . . . . . . . RPL21P3 . . . ribosomal protein L21 pseudogene 3 . . . . . . . . . . . RPL21P4 . . . ribosomal protein L21 pseudogene 4 . . . . . . . . . . . RPL21P5 . . . ribosomal protein L21 pseudogene 5 . . . . . . . . . . . RPL21P6 . . . ribosomal protein L21 pseudogene 6 . . . . . . . . . . . RPL21P7 . . . ribosomal protein L21 pseudogene 7 . . . . . . . . . . . RPL21P8 . . . ribosomal protein L21 pseudogene 8 . . . . . . . . . . . RPL21P9 . . . ribosomal protein L21 pseudogene 9 . . . . . . . . . . . RPL21P10 . . . ribosomal protein L21 pseudogene 10 . . . . . . . . . . . RPL21P11 . . . ribosomal protein L21 pseudogene 11 . . . . . . . . . . . RPL21P12 . . . ribosomal protein L21 pseudogene 12 . . . . . . . . . . . RPL21P13 . . . ribosomal protein L21 pseudogene 13 . . . . . . . . . . . RPL21P14 . . . ribosomal protein L21 pseudogene 14 . . . . . . . . . . . RPL21P15 . . . ribosomal protein L21 pseudogene 15 . . . . . . . . . . . RPL21P16 . . . ribosomal protein L21 pseudogene 16 . . . . . . . . . . . RPL21P17 . . . ribosomal protein L21 pseudogene 17 . . . . . . . . . . . RPL21P18 . . . ribosomal protein L21 pseudogene 18 . . . . . . . . . . . RPL21P19 . . . ribosomal protein L21 pseudogene 19 . . . . . . . . . . . RPL21P20 . . . ribosomal protein L21 pseudogene 20 . . . . . . . . . . . RPL21P21 . . . ribosomal protein L21 pseudogene 21 . . . . . . . . . . . RPL21P22 . . . ribosomal protein L21 pseudogene 22 . . . . . . . . . . . RPL21P23 . . . ribosomal protein L21 pseudogene 23 . . . . . . . . . . . RPL21P24 . . . ribosomal protein L21 pseudogene 24 . . . . . . . . . . . RPL21P25 . . . ribosomal protein L21 pseudogene 25 . . . . . . . . . . . RPL21P26 . . . ribosomal protein L21 pseudogene 26 . . . . . . . . . . . RPL21P27 . . . ribosomal protein L21 pseudogene 27 . . . . . . . . . . . RPL21P28 . . . ribosomal protein L21 pseudogene 28 . . . . . . . . . . . RPL21P29 . . . ribosomal protein L21 pseudogene 29 . . . . . . . . . . . RPL21P30 . . . ribosomal protein L21 pseudogene 30 . . . . . . . . . . . RPL21P31 . . . ribosomal protein L21 pseudogene 31 . . . . . . . . . . . RPL21P32 . . . ribosomal protein L21 pseudogene 32 . . . . . . . . . . . RPL21P33 . . . ribosomal protein L21 pseudogene 33 . . . . . . . . . . . RPL21P34 . . . ribosomal protein L21 pseudogene 34 . . . . . . . . . . . RPL21P35 . . . ribosomal protein L21 pseudogene 35 . . . . . . . . . . . RPL21P36 . . . ribosomal protein L21 pseudogene 36 . . . . . . . . . . . RPL21P37 . . . ribosomal protein L21 pseudogene 37 . . . . . . . . . . . RPL21P38 . . . ribosomal protein L21 pseudogene 38 . . . . . . . . . . . RPL21P39 . . . ribosomal protein L21 pseudogene 39 . . . . . . . . . . . RPL21P40 . . . ribosomal protein L21 pseudogene 40 . . . . . . . . . . . RPL21P41 . . . ribosomal protein L21 pseudogene 41 . . . . . . . . . . . RPL21P42 . . . ribosomal protein L21 pseudogene 42 . . . . . . . . . . . RPL21P43 . . . ribosomal protein L21 pseudogene 43 . . . . . . . . . . . RPL21P44 . . . ribosomal protein L21 pseudogene 44 . . . . . . . . . . . RPL21P45 . . . ribosomal protein L21 pseudogene 45 . . . . . . . . . . . RPL21P46 . . . ribosomal protein L21 pseudogene 46 . . . . . . . . . . . RPL21P47 . . . ribosomal protein L21 pseudogene 47 . . . . . . . . . . . RPL21P48 . . . ribosomal protein L21 pseudogene 48 . . . . . . . . . . . RPL21P49 . . . ribosomal protein L21 pseudogene 49 . . . . . . . . . . . RPL21P50 . . . ribosomal protein L21 pseudogene 50 . . . . . . . . . . . RPL21P51 . . . ribosomal protein L21 pseudogene 51 . . . . . . . . . . . RPL21P52 . . . ribosomal protein L21 pseudogene 52 . . . . . . . . . . . RPL21P53 . . . ribosomal protein L21 pseudogene 53 . . . . . . . . . . . RPL21P54 . . . ribosomal protein L21 pseudogene 54 . . . . . . . . . . . RPL21P55 . . . ribosomal protein L21 pseudogene 55 . . . . . . . . . . . RPL21P56 . . . ribosomal protein L21 pseudogene 56 . . . . . . . . . . . RPL21P57 . . . ribosomal protein L21 pseudogene 57 . . . . . . . . . . . RPL21P58 . . . ribosomal protein L21 pseudogene 58 . . . . . . . . . . . RPL21P59 . . . ribosomal protein L21 pseudogene 59 . . . . . . . . . . . RPL21P60 . . . ribosomal protein L21 pseudogene 60 . . . . . . . . . . . RPL21P61 . . . ribosomal protein L21 pseudogene 61 . . . . . . . . . . . RPL21P62 . . . ribosomal protein L21 pseudogene 62 . . . . . . . . . . . RPL21P63 . . . ribosomal protein L21 pseudogene 63 . . . . . . . . . . . RPL21P64 . . . ribosomal protein L21 pseudogene 64 . . . . . . . . . . . RPL21P65 . . . ribosomal protein L21 pseudogene 65 . . . . . . . . . . . RPL21P66 . . . ribosomal protein L21 pseudogene 66 . . . . . . . . . . . RPL21P67 . . . ribosomal protein L21 pseudogene 67 . . . . . . . . . . . RPL21P68 . . . ribosomal protein L21 pseudogene 68 . . . . . . . . . . . RPL21P69 . . . ribosomal protein L21 pseudogene 69 . . . . . . . . . . . RPL21P70 . . . ribosomal protein L21 pseudogene 70 . . . . . . . . . . . RPL21P71 . . . ribosomal protein L21 pseudogene 71 . . . . . . . . . . . RPL21P72 . . . ribosomal protein L21 pseudogene 72 . . . . . . . . . . . RPL21P73 . . . ribosomal protein L21 pseudogene 73 . . . . . . . . . . . RPL21P74 . . . ribosomal protein L21 pseudogene 74 . . . . . . . . . . . RPL21P75 . . . ribosomal protein L21 pseudogene 75 . . . . . . . . . . . RPL21P76 . . . ribosomal protein L21 pseudogene 76 . . . . . . . . . . . RPL21P77 . . . ribosomal protein L21 pseudogene 77 . . . . . . . . . . . RPL21P78 . . . ribosomal protein L21 pseudogene 78 . . . . . . . . . . . RPL21P79 . . . ribosomal protein L21 pseudogene 79 . . . . . . . . . . . RPL21P80 . . . ribosomal protein L21 pseudogene 80 . . . . . . . . . . . RPL21P81 . . . ribosomal protein L21 pseudogene 81 . . . . . . . . . . . RPL21P82 . . . ribosomal protein L21 pseudogene 82 . . . . . . . . . . . RPL21P83 . . . ribosomal protein L21 pseudogene 83 . . . . . . . . . . . RPL21P84 . . . ribosomal protein L21 pseudogene 84 . . . . . . . . . . . RPL21P85 . . . ribosomal protein L21 pseudogene 85 . . . . . . . . . . . RPL21P86 . . . ribosomal protein L21 pseudogene 86 . . . . . . . . . . . RPL21P87 . . . ribosomal protein L21 pseudogene 87 . . . . . . . . . . . RPL21P88 . . . ribosomal protein L21 pseudogene 88 . . . . . . . . . . . RPL21P89 . . . ribosomal protein L21 pseudogene 89 . . . . . . . . . . . RPL21P90 . . . ribosomal protein L21 pseudogene 90 . . . . . . . . . . . RPL21P91 . . . ribosomal protein L21 pseudogene 91 . . . . . . . . . . . RPL21P92 . . . ribosomal protein L21 pseudogene 92 . . . . . . . . . . . RPL21P93 . . . ribosomal protein L21 pseudogene 93 . . . . . . . . . . . RPL21P94 . . . ribosomal protein L21 pseudogene 94 . . . . . . . . . . . RPL21P95 . . . ribosomal protein L21 pseudogene 95 . . . . . . . . . . . RPL21P96 . . . ribosomal protein L21 pseudogene 96 . . . . . . . . . . . RPL21P97 . . . ribosomal protein L21 pseudogene 97 . . . . . . . . . . . RPL21P98 . . . ribosomal protein L21 pseudogene 98 . . . . . . . . . . . RPL21P99 . . . ribosomal protein L21 pseudogene 99 . . . . . . . . . . . RPL21P100 . . . ribosomal protein L21 pseudogene 100 . . . . . . . . . . . RPL21P101 . . . ribosomal protein L21 pseudogene 101 . . . . . . . . . . . RPL21P102 . . . ribosomal protein L21 pseudogene 102 . . . . . . . . . . . RPL21P103 . . . ribosomal protein L21 pseudogene 103 . . . . . . . . . . . RPL21P104 . . . ribosomal protein L21 pseudogene 104 . . . . . . . . . . . RPL21P105 . . . ribosomal protein L21 pseudogene 105 . . . . . . . . . . . RPL21P106 . . . ribosomal protein L21 pseudogene 106 . . . . . . . . . . . RPL21P107 . . . ribosomal protein L21 pseudogene 107 . . . . . . . . . . . RPL21P108 . . . ribosomal protein L21 pseudogene 108 . . . . . . . . . . . RPL21P109 . . . ribosomal protein L21 pseudogene 109 . . . . . . . . . . . RPL21P110 . . . ribosomal protein L21 pseudogene 110 . . . . . . . . . . . RPL21P111 . . . ribosomal protein L21 pseudogene 111 . . . . . . . . . . . RPL21P112 . . . ribosomal protein L21 pseudogene 112 . . . . . . . . . . . RPL21P113 . . . ribosomal protein L21 pseudogene 113 . . . . . . . . . . . RPL21P114 . . . ribosomal protein L21 pseudogene 114 . . . . . . . . . . . RPL21P115 . . . ribosomal protein L21 pseudogene 115 . . . . . . . . . . . RPL21P116 . . . ribosomal protein L21 pseudogene 116 . . . . . . . . . . . RPL21P117 . . . ribosomal protein L21 pseudogene 117 . . . . . . . . . . . RPL21P118 . . . ribosomal protein L21 pseudogene 118 . . . . . . . . . . . RPL21P119 . . . ribosomal protein L21 pseudogene 119 . . . . . . . . . . . RPL21P120 . . . ribosomal protein L21 pseudogene 120 . . . . . . . . . . . RPL21P121 . . . ribosomal protein L21 pseudogene 121 . . . . . . . . . . . RPL21P122 . . . ribosomal protein L21 pseudogene 122 . . . . . . . . . . . RPL21P123 . . . ribosomal protein L21 pseudogene 123 . . . . . . . . . . . RPL21P124 . . . ribosomal protein L21 pseudogene 124 . . . . . . . . . . . RPL21P125 . . . ribosomal protein L21 pseudogene 125 . . . . . . . . . . . RPL21P126 . . . ribosomal protein L21 pseudogene 126 . . . . . . . . . . . RPL21P127 . . . ribosomal protein L21 pseudogene 127 . . . . . . . . . . . RPL21P128 . . . ribosomal protein L21 pseudogene 128 . . . . . . . . . . . RPL21P129 . . . ribosomal protein L21 pseudogene 129 . . . . . . . . . . . RPL21P130 . . . ribosomal protein L21 pseudogene 130 . . . . . . . . . . . RPL21P131 . . . ribosomal protein L21 pseudogene 131 . . . . . . . . . . . RPL21P132 . . . ribosomal protein L21 pseudogene 132 . . . . . . . . . . . RPL21P133 . . . ribosomal protein L21 pseudogene 133 . . . . . . . . . . . RPL21P134 . . . ribosomal protein L21 pseudogene 134 . . . . . . . . . . . RPL21P135 . . . ribosomal protein L21 pseudogene 135 . . . . . . . . . . . RPL21P136 . . . ribosomal protein L21 pseudogene 136 . . . . . . . . . . . RPL22 0.348492156430072 0.595685116069832 0.0558227275000964 ribosomal protein L22 . . . ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;fetal brain;caudate nucleus; 0.35206 0.28031 0.013025609 54.62962963 0.9034 0.01958 RPL22L1 0.0939593928074091 0.768215348251189 0.137825258941402 ribosomal protein L22 like 1 . . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;oesophagus;bone;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;breast;lung;cornea;placenta;visual apparatus;alveolus;duodenum;liver;kidney;mammary gland;aorta;stomach; . 0.15435 0.10591 0.191216164 66.57230479 68.22834 1.71014 RPL22P1 . . . ribosomal protein L22 pseudogene 1 . . . . . . . . . . . RPL22P2 . . . ribosomal protein L22 pseudogene 2 . . . . . . . . . . . RPL22P3 . . . ribosomal protein L22 pseudogene 3 . . . . . . . . . . . RPL22P4 . . . ribosomal protein L22 pseudogene 4 . . . . . . . . . . . RPL22P5 . . . ribosomal protein L22 pseudogene 5 . . . . . . . . . . . RPL22P6 . . . ribosomal protein L22 pseudogene 6 . . . . . . . . . . . RPL22P7 . . . ribosomal protein L22 pseudogene 7 . . . . . . . . . . . RPL22P8 . . . ribosomal protein L22 pseudogene 8 . . . . . . . . . . . RPL22P10 . . . ribosomal protein L22 pseudogene 10 . . . . . . . . . . . RPL22P11 . . . ribosomal protein L22 pseudogene 11 . . . . . . . . . . . RPL22P12 . . . ribosomal protein L22 pseudogene 12 . . . . . . . . . . . RPL22P13 . . . ribosomal protein L22 pseudogene 13 . . . . . . . . . . . RPL22P14 . . . ribosomal protein L22 pseudogene 14 . . . . . . . . . . . RPL22P16 . . . ribosomal protein L22 pseudogene 16 . . . . . . . . . . . RPL22P17 . . . ribosomal protein L22 pseudogene 17 . . . . . . . . . . . RPL22P18 . . . ribosomal protein L22 pseudogene 18 . . . . . . . . . . . RPL22P19 . . . ribosomal protein L22 pseudogene 19 . . . . . . . . . . . RPL22P20 . . . ribosomal protein L22 pseudogene 20 . . . . . . . . . . . RPL22P21 . . . ribosomal protein L22 pseudogene 21 . . . . . . . . . . . RPL22P22 . . . ribosomal protein L22 pseudogene 22 . . . . . . . . . . . RPL23 0.93162442983743 0.0680349209362947 0.000340649226275044 ribosomal protein L23 . . . myocardium;ovary;salivary gland;developmental;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;testis;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;epididymis;trabecular meshwork;placenta;visual apparatus;alveolus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; . 0.89138 0.36254 0.013025609 54.62962963 2.43929 0.08793 RPL23A 0.876904381937284 0.12156772580507 0.00152789225764633 ribosomal protein L23a FUNCTION: This protein binds to a specific region on the 26S rRNA. {ECO:0000250}.; . . ovary;umbilical cord;salivary gland;intestine;colon;parathyroid;skin;bone marrow;prostate;frontal lobe;thyroid;pituitary gland;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;adrenal cortex;pharynx;blood;skeletal muscle;bile duct;breast;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; . 0.26337 0.16167 -0.09720619 46.20193442 44.38616 1.27329 RPL23AP1 . . . ribosomal protein L23a pseudogene 1 . . . . . . . . . . . RPL23AP2 . . . ribosomal protein L23a pseudogene 2 . . . . . . . . . . . RPL23AP3 . . . ribosomal protein L23a pseudogene 3 . . . . . . . . . . . RPL23AP4 . . . ribosomal protein L23a pseudogene 4 . . . . . . . . . . . RPL23AP5 . . . ribosomal protein L23a pseudogene 5 . . . . . . . . . . . RPL23AP6 . . . ribosomal protein L23a pseudogene 6 . . . . . . . . . . . RPL23AP7 . . . ribosomal protein L23a pseudogene 7 . . . . . . . . . . . RPL23AP8 . . . ribosomal protein L23a pseudogene 8 . . . . . . . . . . . RPL23AP10 . . . ribosomal protein L23a pseudogene 10 . . . . . . . . . . . RPL23AP11 . . . ribosomal protein L23a pseudogene 11 . . . . . . . . . . . RPL23AP12 . . . ribosomal protein L23a pseudogene 12 . . . . . . . . . . . RPL23AP14 . . . ribosomal protein L23a pseudogene 14 . . . . . . . . . . . RPL23AP15 . . . ribosomal protein L23a pseudogene 15 . . . . . . . . . . . RPL23AP16 . . . ribosomal protein L23a pseudogene 16 . . . . . . . . . . . RPL23AP17 . . . ribosomal protein L23a pseudogene 17 . . . . . . . . . . . RPL23AP18 . . . ribosomal protein L23a pseudogene 18 . . . . . . . . . . . RPL23AP19 . . . ribosomal protein L23a pseudogene 19 . . . . . . . . . . . RPL23AP20 . . . ribosomal protein L23a pseudogene 20 . . . . . . . . . . . RPL23AP21 . . . ribosomal protein L23a pseudogene 21 . . . . . . . . . . . RPL23AP22 . . . ribosomal protein L23a pseudogene 22 . . . . . . . . . . . RPL23AP23 . . . ribosomal protein L23a pseudogene 23 . . . . . . . . . . . RPL23AP24 . . . ribosomal protein L23a pseudogene 24 . . . . . . . . . . . RPL23AP25 . . . ribosomal protein L23a pseudogene 25 . . . . . . . . . . . RPL23AP26 . . . ribosomal protein L23a pseudogene 26 . . . . . . . . . . . RPL23AP27 . . . ribosomal protein L23a pseudogene 27 . . . . . . . . . . . RPL23AP28 . . . ribosomal protein L23a pseudogene 28 . . . . . . . . . . . RPL23AP29 . . . ribosomal protein L23a pseudogene 29 . . . . . . . . . . . RPL23AP30 . . . ribosomal protein L23a pseudogene 30 . . . . . . . . . . . RPL23AP31 . . . ribosomal protein L23a pseudogene 31 . . . . . . . . . . . RPL23AP32 . . . ribosomal protein L23a pseudogene 32 . . . . . . . . . . . RPL23AP33 . . . ribosomal protein L23a pseudogene 33 . . . . . . . . . . . RPL23AP34 . . . ribosomal protein L23a pseudogene 34 . . . . . . . . . . . RPL23AP35 . . . ribosomal protein L23a pseudogene 35 . . . . . . . . . . . RPL23AP36 . . . ribosomal protein L23a pseudogene 36 . . . . . . . . . . . RPL23AP37 . . . ribosomal protein L23a pseudogene 37 . . . . . . . . . . . RPL23AP38 . . . ribosomal protein L23a pseudogene 38 . . . . . . . . . . . RPL23AP39 . . . ribosomal protein L23a pseudogene 39 . . . . . . . . . . . RPL23AP40 . . . ribosomal protein L23a pseudogene 40 . . . . . . . . . . . RPL23AP41 . . . ribosomal protein L23a pseudogene 41 . . . . . . . . . . . RPL23AP42 . . . ribosomal protein L23a pseudogene 42 . . . . . . . . . . . RPL23AP43 . . . ribosomal protein L23a pseudogene 43 . . . . . . . . . . . RPL23AP44 . . . ribosomal protein L23a pseudogene 44 . . . . . . . . . . . RPL23AP45 . . . ribosomal protein L23a pseudogene 45 . . . . . . . . . . . RPL23AP46 . . . ribosomal protein L23a pseudogene 46 . . . . . . . . . . . RPL23AP47 . . . ribosomal protein L23a pseudogene 47 . . . . . . . . . . . RPL23AP48 . . . ribosomal protein L23a pseudogene 48 . . . . . . . . . . . RPL23AP49 . . . ribosomal protein L23a pseudogene 49 . . . . . . . . . . . RPL23AP50 . . . ribosomal protein L23a pseudogene 50 . . . . . . . . . . . RPL23AP51 . . . ribosomal protein L23a pseudogene 51 . . . . . . . . . . . RPL23AP52 . . . ribosomal protein L23a pseudogene 52 . . . . . . . . . . . RPL23AP53 . . . ribosomal protein L23a pseudogene 53 . . . . . . . . . . . RPL23AP54 . . . ribosomal protein L23a pseudogene 54 . . . . . . . . . . . RPL23AP55 . . . ribosomal protein L23a pseudogene 55 . . . . . . . . . . . RPL23AP56 . . . ribosomal protein L23a pseudogene 56 . . . . . . . . . . . RPL23AP57 . . . ribosomal protein L23a pseudogene 57 . . . . . . . . . . . RPL23AP58 . . . ribosomal protein L23a pseudogene 58 . . . . . . . . . . . RPL23AP59 . . . ribosomal protein L23a pseudogene 59 . . . . . . . . . . . RPL23AP60 . . . ribosomal protein L23a pseudogene 60 . . . . . . . . . . . RPL23AP61 . . . ribosomal protein L23a pseudogene 61 . . . . . . . . . . . RPL23AP62 . . . ribosomal protein L23a pseudogene 62 . . . . . . . . . . . RPL23AP63 . . . ribosomal protein L23a pseudogene 63 . . . . . . . . . . . RPL23AP64 . . . ribosomal protein L23a pseudogene 64 . . . . . . . . . . . RPL23AP65 . . . ribosomal protein L23a pseudogene 65 . . . . . . . . . . . RPL23AP66 . . . ribosomal protein L23a pseudogene 66 . . . . . . . . . . . RPL23AP67 . . . ribosomal protein L23a pseudogene 67 . . . . . . . . . . . RPL23AP68 . . . ribosomal protein L23a pseudogene 68 . . . . . . . . . . . RPL23AP69 . . . ribosomal protein L23a pseudogene 69 . . . . . . . . . . . RPL23AP70 . . . ribosomal protein L23a pseudogene 70 . . . . . . . . . . . RPL23AP71 . . . ribosomal protein L23a pseudogene 71 . . . . . . . . . . . RPL23AP72 . . . ribosomal protein L23a pseudogene 72 . . . . . . . . . . . RPL23AP73 . . . ribosomal protein L23a pseudogene 73 . . . . . . . . . . . RPL23AP74 . . . ribosomal protein L23a pseudogene 74 . . . . . . . . . . . RPL23AP75 . . . ribosomal protein L23a pseudogene 75 . . . . . . . . . . . RPL23AP76 . . . ribosomal protein L23a pseudogene 76 . . . . . . . . . . . RPL23AP77 . . . ribosomal protein L23a pseudogene 77 . . . . . . . . . . . RPL23AP78 . . . ribosomal protein L23a pseudogene 78 . . . . . . . . . . . RPL23AP79 . . . ribosomal protein L23a pseudogene 79 . . . . . . . . . . . RPL23AP80 . . . ribosomal protein L23a pseudogene 80 . . . . . . . . . . . RPL23AP81 . . . ribosomal protein L23a pseudogene 81 . . . . . . . . . . . RPL23AP82 . . . ribosomal protein L23a pseudogene 82 . . . . . . . . . . . RPL23AP83 . . . ribosomal protein L23a pseudogene 83 . . . . . . . . . . . RPL23AP84 . . . ribosomal protein L23a pseudogene 84 . . . . . . . . . . . RPL23AP85 . . . ribosomal protein L23a pseudogene 85 . . . . . . . . . . . RPL23AP86 . . . ribosomal protein L23a pseudogene 86 . . . . . . . . . . . RPL23AP87 . . . ribosomal protein L23a pseudogene 87 . . . . . . . . . . . RPL23AP88 . . . ribosomal protein L23a pseudogene 88 . . . . . . . . . . . RPL23AP89 . . . ribosomal protein L23a pseudogene 89 . . . . . . . . . . . RPL23AP90 . . . ribosomal protein L23a pseudogene 90 . . . . . . . . . . . RPL23AP91 . . . ribosomal protein L23a pseudogene 91 . . . . . . . . . . . RPL23AP92 . . . ribosomal protein L23a pseudogene 92 . . . . . . . . . . . RPL23AP93 . . . ribosomal protein L23a pseudogene 93 . . . . . . . . . . . RPL23AP94 . . . ribosomal protein L23a pseudogene 94 . . . . . . . . . . . RPL23AP95 . . . ribosomal protein L23a pseudogene 95 . . . . . . . . . . . RPL23AP96 . . . ribosomal protein L23a pseudogene 96 . . . . . . . . . . . RPL23AP97 . . . ribosomal protein L23a pseudogene 97 . . . . . . . . . . . RPL23P2 . . . ribosomal protein L23 pseudogene 2 . . . . . . . . . . . RPL23P3 . . . ribosomal protein L23 pseudogene 3 . . . . . . . . . . . RPL23P4 . . . ribosomal protein L23 pseudogene 4 . . . . . . . . . . . RPL23P5 . . . ribosomal protein L23 pseudogene 5 . . . . . . . . . . . RPL23P6 . . . ribosomal protein L23 pseudogene 6 . . . . . . . . . . . RPL23P7 . . . ribosomal protein L23 pseudogene 7 . . . . . . . . . . . RPL23P8 . . . ribosomal protein L23 pseudogene 8 . . . . . . . . . . . RPL23P9 . . . ribosomal protein L23 pseudogene 9 . . . . . . . . . . . RPL23P10 . . . ribosomal protein L23 pseudogene 10 . . . . . . . . . . . RPL23P11 . . . ribosomal protein L23 pseudogene 11 . . . . . . . . . . . RPL24 0.864299873369858 0.135290531935741 0.000409594694401177 ribosomal protein L24 . . . . . 0.98928 0.08861 -0.075159878 47.78839349 2.93038 0.10632 RPL24P2 . . . ribosomal protein L24 pseudogene 2 . . . . . . . . . . . RPL24P3 . . . ribosomal protein L24 pseudogene 3 . . . . . . . . . . . RPL24P4 . . . ribosomal protein L24 pseudogene 4 . . . . . . . . . . . RPL24P5 . . . ribosomal protein L24 pseudogene 5 . . . . . . . . . . . RPL24P6 . . . ribosomal protein L24 pseudogene 6 . . . . . . . . . . . RPL24P7 . . . ribosomal protein L24 pseudogene 7 . . . . . . . . . . . RPL24P8 . . . ribosomal protein L24 pseudogene 8 . . . . . . . . . . . RPL26 0.915888681432076 0.0835357971335168 0.0005755214344068 ribosomal protein L26 . DISEASE: Diamond-Blackfan anemia 11 (DBA11) [MIM:614900]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. {ECO:0000269|PubMed:22431104}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;lymphoreticular;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;bladder;brain;tonsil;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;larynx;bone;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;placenta;kidney;stomach;aorta; . . 0.18658 -0.009020804 52.8544468 5.90394 0.22232 RPL26L1 0.492260269694433 0.486933889406674 0.0208058408988934 ribosomal protein L26 like 1 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;frontal lobe;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; . 0.13563 0.12378 -0.163345027 41.24793583 53.07229 1.44607 RPL26P2 . . . ribosomal protein L26 pseudogene 2 . . . . . . . . . . . RPL26P3 . . . ribosomal protein L26 pseudogene 3 . . . . . . . . . . . RPL26P4 . . . ribosomal protein L26 pseudogene 4 . . . . . . . . . . . RPL26P5 . . . ribosomal protein L26 pseudogene 5 . . . . . . . . . . . RPL26P6 . . . ribosomal protein L26 pseudogene 6 . . . . . . 0.18658 . . . . RPL26P7 . . . ribosomal protein L26 pseudogene 7 . . . . . . . . . . . RPL26P8 . . . ribosomal protein L26 pseudogene 8 . . . . . . . . . . . RPL26P9 . . . ribosomal protein L26 pseudogene 9 . . . . . . . . . . . RPL26P10 . . . ribosomal protein L26 pseudogene 10 . . . . . . . . . . . RPL26P11 . . . ribosomal protein L26 pseudogene 11 . . . . . . . . . . . RPL26P12 . . . ribosomal protein L26 pseudogene 12 . . . . . . . . . . . RPL26P13 . . . ribosomal protein L26 pseudogene 13 . . . . . . . . . . . RPL26P14 . . . ribosomal protein L26 pseudogene 14 . . . . . . . . . . . RPL26P15 . . . ribosomal protein L26 pseudogene 15 . . . . . . . . . . . RPL26P16 . . . ribosomal protein L26 pseudogene 16 . . . . . . . . . . . RPL26P17 . . . ribosomal protein L26 pseudogene 17 . . . . . . . . . . . RPL26P18 . . . ribosomal protein L26 pseudogene 18 . . . . . . . . . . . RPL26P19 . . . ribosomal protein L26 pseudogene 19 . . . . . . . . . . . RPL26P20 . . . ribosomal protein L26 pseudogene 20 . . . . . . . . . . . RPL26P21 . . . ribosomal protein L26 pseudogene 21 . . . . . . . . . . . RPL26P22 . . . ribosomal protein L26 pseudogene 22 . . . . . . . . . . . RPL26P23 . . . ribosomal protein L26 pseudogene 23 . . . . . . . . . . . RPL26P24 . . . ribosomal protein L26 pseudogene 24 . . . . . . . . . . . RPL26P25 . . . ribosomal protein L26 pseudogene 25 . . . . . . . . . . . RPL26P26 . . . ribosomal protein L26 pseudogene 26 . . . . . . . . . . . RPL26P27 . . . ribosomal protein L26 pseudogene 27 . . . . . . . . . . . RPL26P28 . . . ribosomal protein L26 pseudogene 28 . . . . . . . . . . . RPL26P29 . . . ribosomal protein L26 pseudogene 29 . . . . . . . . . . . RPL26P30 . . . ribosomal protein L26 pseudogene 30 . . . . . . . . . . . RPL26P31 . . . ribosomal protein L26 pseudogene 31 . . . . . . . . . . . RPL26P32 . . . ribosomal protein L26 pseudogene 32 . . . . . . . . . . . RPL26P33 . . . ribosomal protein L26 pseudogene 33 . . . . . . . . . . . RPL26P34 . . . ribosomal protein L26 pseudogene 34 . . . . . . . . . . . RPL26P35 . . . ribosomal protein L26 pseudogene 35 . . . . . . . . . . . RPL26P36 . . . ribosomal protein L26 pseudogene 36 . . . . . . . . . . . RPL26P37 . . . ribosomal protein L26 pseudogene 37 . . . . . . . . . . . RPL27 0.822384681492307 0.17362357532384 0.00399174318385324 ribosomal protein L27 . . . myocardium;medulla oblongata;ovary;umbilical cord;skin;bone marrow;retina;prostate;endometrium;bladder;brain;tonsil;heart;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;lung;pia mater;cornea;nasopharynx;placenta;kidney;stomach;aorta; adipose tissue;tongue;adrenal cortex; 0.85713 0.16306 -0.207437529 38.2814343 . . RPL27A 0.867199853512814 0.130939791582702 0.00186035490448441 ribosomal protein L27a . . . lymphoreticular;myocardium;ovary;salivary gland;intestine;colon;vein;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;synovium;larynx;bone;testis;dura mater;brain;bladder;tonsil;unclassifiable (Anatomical System);meninges;trophoblast;lymph node;heart;islets of Langerhans;hypothalamus;pineal body;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;pia mater;lung;cornea;nasopharynx;placenta;visual apparatus;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;stomach; . 0.96704 0.16878 0.079165051 59.43029016 17.6401 0.61847 RPL27AP . . . ribosomal protein L27a pseudogene . . . lymphoreticular;myocardium;ovary;salivary gland;intestine;colon;vein;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;synovium;bone;testis;dura mater;brain;bladder;tonsil;unclassifiable (Anatomical System);meninges;trophoblast;lymph node;heart;islets of Langerhans;hypothalamus;pineal body;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;pia mater;lung;cornea;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; . . . . . . . RPL27AP2 . . . ribosomal protein L27a pseudogene 2 . . . . . . . . . . . RPL27AP3 . . . ribosomal protein L27a pseudogene 3 . . . . . . . . . . . RPL27AP4 . . . ribosomal protein L27a pseudogene 4 . . . . . . . . . . . RPL27AP5 . . . ribosomal protein L27a pseudogene 5 . . . . . . . . . . . RPL27AP6 . . . ribosomal protein L27a pseudogene 6 . . . . . . . . . . . RPL27AP7 . . . ribosomal protein L27a pseudogene 7 . . . . . . . . . . . RPL27AP8 . . . ribosomal protein L27a pseudogene 8 . . . . . . . . . . . RPL27P1 . . . ribosomal protein L27 pseudogene 1 . . . . . . . . . . . RPL27P2 . . . ribosomal protein L27 pseudogene 2 . . . . . . . . . . . RPL27P4 . . . ribosomal protein L27 pseudogene 4 . . . . . . . . . . . RPL27P5 . . . ribosomal protein L27 pseudogene 5 . . . . . . . . . . . RPL27P6 . . . ribosomal protein L27 pseudogene 6 . . . . . . . . . . . RPL27P7 . . . ribosomal protein L27 pseudogene 7 . . . . . . . . . . . RPL27P8 . . . ribosomal protein L27 pseudogene 8 . . . . . . . . . . . RPL27P9 . . . ribosomal protein L27 pseudogene 9 . . . . . . . . . . . RPL27P10 . . . ribosomal protein L27 pseudogene 10 . . . . . . . . . . . RPL27P11 . . . ribosomal protein L27 pseudogene 11 . . . . . . . . . . . RPL27P12 . . . ribosomal protein L27 pseudogene 12 . . . . . . . . . . . RPL28 0.671038473320397 0.307458289376164 0.0215032373034384 ribosomal protein L28 . . . myocardium;ovary;salivary gland;intestine;colon;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;pituitary gland;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;breast;bile duct;pancreas;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; dorsal root ganglion;prostate;superior cervical ganglion;lung;heart;liver;tumor;ciliary ganglion;skeletal muscle;thymus;bone marrow; 0.61762 0.22085 0.084621747 60.31493277 3157.21337 10.70171 RPL28P1 . . . ribosomal protein L28 pseudogene 1 . . . . . . . . . . . RPL28P2 . . . ribosomal protein L28 pseudogene 2 . . . . . . . . . . . RPL28P3 . . . ribosomal protein L28 pseudogene 3 . . . . . . . . . . . RPL28P4 . . . ribosomal protein L28 pseudogene 4 . . . . . . . . . . . RPL28P5 . . . ribosomal protein L28 pseudogene 5 . . . . . . . . . . . RPL29 0.597262029881945 0.393364946658997 0.00937302345905843 ribosomal protein L29 . . . medulla oblongata;ovary;umbilical cord;foreskin;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;brain;bladder;tonsil;heart;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;choroid;vein;uterus;whole body;oesophagus;larynx;synovium;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;epidermis;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;kidney;stomach;aorta;thymus; . 0.96052 0.24223 -0.09720619 46.20193442 1604.60298 7.41218 RPL29P1 . . . ribosomal protein L29 pseudogene 1 . . . . . . . . . . . RPL29P2 . . . ribosomal protein L29 pseudogene 2 . . . . . . . . . . . RPL29P3 . . . ribosomal protein L29 pseudogene 3 . . . . . . . . . . . RPL29P4 . . . ribosomal protein L29 pseudogene 4 . . . . . . . . . . . RPL29P5 . . . ribosomal protein L29 pseudogene 5 . . . . . . . . . . . RPL29P6 . . . ribosomal protein L29 pseudogene 6 . . . . . . . . . . . RPL29P7 . . . ribosomal protein L29 pseudogene 7 . . . . . . . . . . . RPL29P8 . . . ribosomal protein L29 pseudogene 8 . . . . . . . . . . . RPL29P9 . . . ribosomal protein L29 pseudogene 9 . . . . . . . . . . . RPL29P11 . . . ribosomal protein L29 pseudogene 11 . . . . . . . . . . . RPL29P12 . . . ribosomal protein L29 pseudogene 12 . . . . . . . . . . . RPL29P13 . . . ribosomal protein L29 pseudogene 13 . . . . . . . . . . . RPL29P14 . . . ribosomal protein L29 pseudogene 14 . . . . . . . . . . . RPL29P15 . . . ribosomal protein L29 pseudogene 15 . . . . . . . . . . . RPL29P16 . . . ribosomal protein L29 pseudogene 16 . . . . . . . . . . . RPL29P17 . . . ribosomal protein L29 pseudogene 17 . . . . . . . . . . . RPL29P18 . . . ribosomal protein L29 pseudogene 18 . . . . . . . . . . . RPL29P19 . . . ribosomal protein L29 pseudogene 19 . . . . . . . . . . . RPL29P20 . . . ribosomal protein L29 pseudogene 20 . . . . . . . . . . . RPL29P21 . . . ribosomal protein L29 pseudogene 21 . . . . . . . . . . . RPL29P22 . . . ribosomal protein L29 pseudogene 22 . . . . . . . . . . . RPL29P23 . . . ribosomal protein L29 pseudogene 23 . . . . . . . . . . . RPL29P24 . . . ribosomal protein L29 pseudogene 24 . . . . . . . . . . . RPL29P25 . . . ribosomal protein L29 pseudogene 25 . . . . . . . . . . . RPL29P26 . . . ribosomal protein L29 pseudogene 26 . . . . . . . . . . . RPL29P27 . . . ribosomal protein L29 pseudogene 27 . . . . . . . . . . . RPL29P28 . . . ribosomal protein L29 pseudogene 28 . . . . . . . . . . . RPL29P29 . . . ribosomal protein L29 pseudogene 29 . . . . . . . . . . . RPL29P30 . . . ribosomal protein L29 pseudogene 30 . . . . . . . . . . . RPL29P31 . . . ribosomal protein L29 pseudogene 31 . . . . . . . . . . . RPL29P32 . . . ribosomal protein L29 pseudogene 32 . . . . . . . . . . . RPL29P33 . . . ribosomal protein L29 pseudogene 33 . . . . . . . . . . . RPL30 0.77479016788703 0.21766760475546 0.00754222735751022 ribosomal protein L30 . . . myocardium;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;synovium;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; pancreas;ovary;salivary gland;whole blood; 0.81516 0.27983 0.035072054 56.2514744 . . RPL30P1 . . . ribosomal protein L30 pseudogene 1 . . . . . . . . . . . RPL30P2 . . . ribosomal protein L30 pseudogene 2 . . . . . . . . . . . RPL30P3 . . . ribosomal protein L30 pseudogene 3 . . . . . . . . . . . RPL30P4 . . . ribosomal protein L30 pseudogene 4 . . . . . . . . . . . RPL30P5 . . . ribosomal protein L30 pseudogene 5 . . . . . . . . . . . RPL30P6 . . . ribosomal protein L30 pseudogene 6 . . . . . . . . . . . RPL30P7 . . . ribosomal protein L30 pseudogene 7 . . . . . . . . . . . RPL30P8 . . . ribosomal protein L30 pseudogene 8 . . . . . . . . . . . RPL30P9 . . . ribosomal protein L30 pseudogene 9 . . . . . . . . . . . RPL30P10 . . . ribosomal protein L30 pseudogene 10 . . . . . . . . . . . RPL30P11 . . . ribosomal protein L30 pseudogene 11 . . . . . . . . . . . RPL30P12 . . . ribosomal protein L30 pseudogene 12 . . . . . . . . . . . RPL30P13 . . . ribosomal protein L30 pseudogene 13 . . . . . . . . . . . RPL30P14 . . . ribosomal protein L30 pseudogene 14 . . . . . . . . . . . RPL30P15 . . . ribosomal protein L30 pseudogene 15 . . . . . . . . . . . RPL30P16 . . . ribosomal protein L30 pseudogene 16 . . . . . . . . . . . RPL31 0.843001842538011 0.154116483441778 0.00288167402021105 ribosomal protein L31 . . . medulla oblongata;ovary;skin;retina;bone marrow;prostate;thyroid;bladder;brain;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;choroid;whole body;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;trachea;temporal lobe;appendix;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.23344 0.20160 0.235309407 68.71903751 3.69131 0.13692 RPL31P1 . . . ribosomal protein L31 pseudogene 1 . . . . . . . . . . . RPL31P2 . . . ribosomal protein L31 pseudogene 2 . . . . . . . . . . . RPL31P3 . . . ribosomal protein L31 pseudogene 3 . . . . . . . . . . . RPL31P4 . . . ribosomal protein L31 pseudogene 4 . . . . . . . . . . . RPL31P5 . . . ribosomal protein L31 pseudogene 5 . . . . . . . . . . . RPL31P6 . . . ribosomal protein L31 pseudogene 6 . . . . . . . . . . . RPL31P7 . . . ribosomal protein L31 pseudogene 7 . . . . . . . . . . . RPL31P8 . . . ribosomal protein L31 pseudogene 8 . . . . . . . . . . . RPL31P9 . . . ribosomal protein L31 pseudogene 9 . . . . . . . . . . . RPL31P10 . . . ribosomal protein L31 pseudogene 10 . . . . . . . . . . . RPL31P11 . . . ribosomal protein L31 pseudogene 11 . . . . . . . . . . . RPL31P12 . . . ribosomal protein L31 pseudogene 12 . . . . . . . . . . . RPL31P13 . . . ribosomal protein L31 pseudogene 13 . . . . . . . . . . . RPL31P14 . . . ribosomal protein L31 pseudogene 14 . . . . . . . . . . . RPL31P15 . . . ribosomal protein L31 pseudogene 15 . . . . . . . . . . . RPL31P16 . . . ribosomal protein L31 pseudogene 16 . . . . . . . . . . . RPL31P17 . . . ribosomal protein L31 pseudogene 17 . . . . . . . . . . . RPL31P18 . . . ribosomal protein L31 pseudogene 18 . . . . . . . . . . . RPL31P19 . . . ribosomal protein L31 pseudogene 19 . . . . . . . . . . . RPL31P20 . . . ribosomal protein L31 pseudogene 20 . . . . . . . . . . . RPL31P21 . . . ribosomal protein L31 pseudogene 21 . . . . . . . . . . . RPL31P22 . . . ribosomal protein L31 pseudogene 22 . . . . . . . . . . . RPL31P23 . . . ribosomal protein L31 pseudogene 23 . . . . . . . . . . . RPL31P24 . . . ribosomal protein L31 pseudogene 24 . . . . . . . . . . . RPL31P25 . . . ribosomal protein L31 pseudogene 25 . . . . . . . . . . . RPL31P26 . . . ribosomal protein L31 pseudogene 26 . . . . . . . . . . . RPL31P27 . . . ribosomal protein L31 pseudogene 27 . . . . . . . . . . . RPL31P28 . . . ribosomal protein L31 pseudogene 28 . . . . . . . . . . . RPL31P29 . . . ribosomal protein L31 pseudogene 29 . . . . . . . . . . . RPL31P30 . . . ribosomal protein L31 pseudogene 30 . . . . . . . . . . . RPL31P31 . . . ribosomal protein L31 pseudogene 31 . . . . . . . . . . . RPL31P32 . . . ribosomal protein L31 pseudogene 32 . . . . . . . . . . . RPL31P33 . . . ribosomal protein L31 pseudogene 33 . . . . . . . . . . . RPL31P34 . . . ribosomal protein L31 pseudogene 34 . . . . . . . . . . . RPL31P35 . . . ribosomal protein L31 pseudogene 35 . . . . . . . . . . . RPL31P36 . . . ribosomal protein L31 pseudogene 36 . . . . . . . . . . . RPL31P37 . . . ribosomal protein L31 pseudogene 37 . . . . . . . . . . . RPL31P38 . . . ribosomal protein L31 pseudogene 38 . . . . . . . . . . . RPL31P39 . . . ribosomal protein L31 pseudogene 39 . . . . . . . . . . . RPL31P40 . . . ribosomal protein L31 pseudogene 40 . . . . . . . . . . . RPL31P41 . . . ribosomal protein L31 pseudogene 41 . . . . . . . . . . . RPL31P42 . . . ribosomal protein L31 pseudogene 42 . . . . . . . . . . . RPL31P43 . . . ribosomal protein L31 pseudogene 43 . . . . . . . . . . . RPL31P44 . . . ribosomal protein L31 pseudogene 44 . . . . . . . . . . . RPL31P45 . . . ribosomal protein L31 pseudogene 45 . . . . . . . . . . . RPL31P46 . . . ribosomal protein L31 pseudogene 46 . . . . . . . . . . . RPL31P47 . . . ribosomal protein L31 pseudogene 47 . . . . . . . . . . . RPL31P48 . . . ribosomal protein L31 pseudogene 48 . . . . . . . . . . . RPL31P49 . . . ribosomal protein L31 pseudogene 49 . . . . . . . . . . . RPL31P50 . . . ribosomal protein L31 pseudogene 50 . . . . . . . . . . . RPL31P51 . . . ribosomal protein L31 pseudogene 51 . . . . . . . . . . . RPL31P52 . . . ribosomal protein L31 pseudogene 52 . . . . . . . . . . . RPL31P53 . . . ribosomal protein L31 pseudogene 53 . . . . . . . . . . . RPL31P54 . . . ribosomal protein L31 pseudogene 54 . . . . . . . . . . . RPL31P55 . . . ribosomal protein L31 pseudogene 55 . . . . . . . . . . . RPL31P56 . . . ribosomal protein L31 pseudogene 56 . . . . . . . . . . . RPL31P57 . . . ribosomal protein L31 pseudogene 57 . . . . . . . . . . . RPL31P58 . . . ribosomal protein L31 pseudogene 58 . . . . . . . . . . . RPL31P59 . . . ribosomal protein L31 pseudogene 59 . . . . . . . . . . . RPL31P60 . . . ribosomal protein L31 pseudogene 60 . . . . . . . . . . . RPL31P61 . . . ribosomal protein L31 pseudogene 61 . . . . . . . . . . . RPL31P62 . . . ribosomal protein L31 pseudogene 62 . . . . . . . . . . . RPL31P63 . . . ribosomal protein L31 pseudogene 63 . . . . . . . . . . . RPL32 0.755582037585297 0.234995125144788 0.00942283726991472 ribosomal protein L32 . . . myocardium;ovary;umbilical cord;skin;retina;bone marrow;prostate;endometrium;thyroid;germinal center;brain;bladder;heart;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;oesophagus;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;muscle;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; . 0.18153 0.19805 0.235309407 68.71903751 12.36999 0.44850 RPL32P1 . . . ribosomal protein L32 pseudogene 1 . . . . . . . . . . . RPL32P2 . . . ribosomal protein L32 pseudogene 2 . . . . . . . . . . . RPL32P3 . . . ribosomal protein L32 pseudogene 3 . . . colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;cochlea;bone;thyroid;pituitary gland;testis;germinal center;brain;artery;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; superior cervical ganglion;ciliary ganglion;white blood cells;atrioventricular node;pons; 0.11819 . . . . . RPL32P4 . . . ribosomal protein L32 pseudogene 4 . . . . . . . . . . . RPL32P5 . . . ribosomal protein L32 pseudogene 5 . . . . . . . . . . . RPL32P6 . . . ribosomal protein L32 pseudogene 6 . . . . . . . . . . . RPL32P7 . . . ribosomal protein L32 pseudogene 7 . . . . . . . . . . . RPL32P8 . . . ribosomal protein L32 pseudogene 8 . . . . . . . . . . . RPL32P9 . . . ribosomal protein L32 pseudogene 9 . . . . . . . . . . . RPL32P10 . . . ribosomal protein L32 pseudogene 10 . . . . . . . . . . . RPL32P11 . . . ribosomal protein L32 pseudogene 11 . . . . . . . . . . . RPL32P12 . . . ribosomal protein L32 pseudogene 12 . . . . . . . . . . . RPL32P13 . . . ribosomal protein L32 pseudogene 13 . . . . . . . . . . . RPL32P14 . . . ribosomal protein L32 pseudogene 14 . . . . . . . . . . . RPL32P15 . . . ribosomal protein L32 pseudogene 15 . . . . . . . . . . . RPL32P16 . . . ribosomal protein L32 pseudogene 16 . . . . . . . . . . . RPL32P17 . . . ribosomal protein L32 pseudogene 17 . . . . . . . . . . . RPL32P18 . . . ribosomal protein L32 pseudogene 18 . . . . . . . . . . . RPL32P19 . . . ribosomal protein L32 pseudogene 19 . . . . . . . . . . . RPL32P20 . . . ribosomal protein L32 pseudogene 20 . . . . . . . . . . . RPL32P21 . . . ribosomal protein L32 pseudogene 21 . . . . . . . . . . . RPL32P22 . . . ribosomal protein L32 pseudogene 22 . . . . . . . . . . . RPL32P23 . . . ribosomal protein L32 pseudogene 23 . . . . . . . . . . . RPL32P24 . . . ribosomal protein L32 pseudogene 24 . . . . . . . . . . . RPL32P25 . . . ribosomal protein L32 pseudogene 25 . . . . . . . . . . . RPL32P26 . . . ribosomal protein L32 pseudogene 26 . . . . . . . . . . . RPL32P27 . . . ribosomal protein L32 pseudogene 27 . . . . . . . . . . . RPL32P28 . . . ribosomal protein L32 pseudogene 28 . . . . . . . . . . . RPL32P29 . . . ribosomal protein L32 pseudogene 29 . . . . . . . . . . . RPL32P30 . . . ribosomal protein L32 pseudogene 30 . . . . . . . . . . . RPL32P31 . . . ribosomal protein L32 pseudogene 31 . . . . . . . . . . . RPL32P32 . . . ribosomal protein L32 pseudogene 32 . . . . . . . . . . . RPL32P33 . . . ribosomal protein L32 pseudogene 33 . . . . . . . . . . . RPL32P34 . . . ribosomal protein L32 pseudogene 34 . . . . . . . . . . . RPL32P35 . . . ribosomal protein L32 pseudogene 35 . . . . . . . . . . . RPL32P36 . . . ribosomal protein L32 pseudogene 36 . . . . . . . . . . . RPL34 0.891623097197441 0.107276839937136 0.00110006286542333 ribosomal protein L34 . . . . . 0.12997 0.12971 -0.075159878 47.78839349 2.43389 0.08770 RPL34-AS1 . . . RPL34 antisense RNA 1 (head to head) . . . . . . . . . . . RPL34P1 . . . ribosomal protein L34 pseudogene 1 . . . . . . . . . . . RPL34P2 . . . ribosomal protein L34 pseudogene 2 . . . . . . . . . . . RPL34P3 . . . ribosomal protein L34 pseudogene 3 . . . . . . . . . . . RPL34P4 . . . ribosomal protein L34 pseudogene 4 . . . . . . . . . . . RPL34P5 . . . ribosomal protein L34 pseudogene 5 . . . . . . . . . . . RPL34P6 . . . ribosomal protein L34 pseudogene 6 . . . . . . . . . . . RPL34P7 . . . ribosomal protein L34 pseudogene 7 . . . . . . . . . . . RPL34P8 . . . ribosomal protein L34 pseudogene 8 . . . . . . . . . . . RPL34P9 . . . ribosomal protein L34 pseudogene 9 . . . . . . . . . . . RPL34P10 . . . ribosomal protein L34 pseudogene 10 . . . . . . . . . . . RPL34P11 . . . ribosomal protein L34 pseudogene 11 . . . . . . . . . . . RPL34P12 . . . ribosomal protein L34 pseudogene 12 . . . . . . . . . . . RPL34P13 . . . ribosomal protein L34 pseudogene 13 . . . . . . . . . . . RPL34P14 . . . ribosomal protein L34 pseudogene 14 . . . . . . . . . . . RPL34P15 . . . ribosomal protein L34 pseudogene 15 . . . . . . . . . . . RPL34P16 . . . ribosomal protein L34 pseudogene 16 . . . . . . . . . . . RPL34P17 . . . ribosomal protein L34 pseudogene 17 . . . . . . . . . . . RPL34P18 . . . ribosomal protein L34 pseudogene 18 . . . . . . . . . . . RPL34P19 . . . ribosomal protein L34 pseudogene 19 . . . . . . . . . . . RPL34P20 . . . ribosomal protein L34 pseudogene 20 . . . . . . . . . . . RPL34P21 . . . ribosomal protein L34 pseudogene 21 . . . . . . . . . . . RPL34P22 . . . ribosomal protein L34 pseudogene 22 . . . . . . . . . . . RPL34P23 . . . ribosomal protein L34 pseudogene 23 . . . . . . . . . . . RPL34P24 . . . ribosomal protein L34 pseudogene 24 . . . . . . . . . . . RPL34P25 . . . ribosomal protein L34 pseudogene 25 . . . . . . . . . . . RPL34P26 . . . ribosomal protein L34 pseudogene 26 . . . . . . . . . . . RPL34P27 . . . ribosomal protein L34 pseudogene 27 . . . . . . . . . . . RPL34P28 . . . ribosomal protein L34 pseudogene 28 . . . . . . . . . . . RPL34P29 . . . ribosomal protein L34 pseudogene 29 . . . . . . . . . . . RPL34P30 . . . ribosomal protein L34 pseudogene 30 . . . . . . . . . . . RPL34P31 . . . ribosomal protein L34 pseudogene 31 . . . . . . . . . . . RPL34P32 . . . ribosomal protein L34 pseudogene 32 . . . . . . . . . . . RPL34P33 . . . ribosomal protein L34 pseudogene 33 . . . . . . . . . . . RPL34P34 . . . ribosomal protein L34 pseudogene 34 . . . . . . . . . . . RPL34P35 . . . ribosomal protein L34 pseudogene 35 . . . . . . . . . . . RPL35 0.527875068824637 0.456078588762101 0.0160463424132617 ribosomal protein L35 . . . myocardium;lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;thyroid;iris;bladder;brain;tonsil;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;vein;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;bile duct;pancreas;lung;cornea;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus; heart;liver;tumor; 0.92515 . 0.125076652 62.7388535 10.99298 0.39832 RPL35A 0.914385546016633 0.0850124189126302 0.000602035070736751 ribosomal protein L35a FUNCTION: Required for the proliferation and viability of hematopoietic cells. Plays a role in 60S ribosomal subunit formation. The protein was found to bind to both initiator and elongator tRNAs and consequently was assigned to the P site or P and A site. {ECO:0000269|PubMed:18535205}.; DISEASE: Diamond-Blackfan anemia 5 (DBA5) [MIM:612528]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. {ECO:0000269|PubMed:18535205}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;endometrium;amniotic fluid;bladder;brain;tonsil;heart;tongue;urinary;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; . 0.25369 0.21177 0.279402865 70.86577023 16.95178 0.59702 RPL35AP . . . ribosomal protein L35a pseudogene . . . . . . . . . . . RPL35AP2 . . . ribosomal protein L35a pseudogene 2 . . . . . . . . . . . RPL35AP3 . . . ribosomal protein L35a pseudogene 3 . . . . . . . . . . . RPL35AP4 . . . ribosomal protein L35a pseudogene 4 . . . . . . . . . . . RPL35AP5 . . . ribosomal protein L35a pseudogene 5 . . . . . . . . . . . RPL35AP6 . . . ribosomal protein L35a pseudogene 6 . . . . . . . . . . . RPL35AP7 . . . ribosomal protein L35a pseudogene 7 . . . . . . . . . . . RPL35AP8 . . . ribosomal protein L35a pseudogene 8 . . . . . . . . . . . RPL35AP9 . . . ribosomal protein L35a pseudogene 9 . . . . . . . . . . . RPL35AP10 . . . ribosomal protein L35a pseudogene 10 . . . . . . . . . . . RPL35AP11 . . . ribosomal protein L35a pseudogene 11 . . . . . . . . . . . RPL35AP12 . . . ribosomal protein L35a pseudogene 12 . . . . . . . . . . . RPL35AP13 . . . ribosomal protein L35a pseudogene 13 . . . . . . . . . . . RPL35AP14 . . . ribosomal protein L35a pseudogene 14 . . . . . . . . . . . RPL35AP15 . . . ribosomal protein L35a pseudogene 15 . . . . . . . . . . . RPL35AP16 . . . ribosomal protein L35a pseudogene 16 . . . . . . . . . . . RPL35AP17 . . . ribosomal protein L35a pseudogene 17 . . . . . . . . . . . RPL35AP18 . . . ribosomal protein L35a pseudogene 18 . . . . . . . . . . . RPL35AP19 . . . ribosomal protein L35a pseudogene 19 . . . . . . . . . . . RPL35AP20 . . . ribosomal protein L35a pseudogene 20 . . . . . . . . . . . RPL35AP21 . . . ribosomal protein L35a pseudogene 21 . . . . . . . . . . . RPL35AP22 . . . ribosomal protein L35a pseudogene 22 . . . . . . . . . . . RPL35AP23 . . . ribosomal protein L35a pseudogene 23 . . . . . . . . . . . RPL35AP24 . . . ribosomal protein L35a pseudogene 24 . . . . . . . . . . . RPL35AP25 . . . ribosomal protein L35a pseudogene 25 . . . . . . . . . . . RPL35AP26 . . . ribosomal protein L35a pseudogene 26 . . . . . . . . . . . RPL35AP27 . . . ribosomal protein L35a pseudogene 27 . . . . . . . . . . . RPL35AP28 . . . ribosomal protein L35a pseudogene 28 . . . . . . . . . . . RPL35AP29 . . . ribosomal protein L35a pseudogene 29 . . . . . . . . . . . RPL35AP30 . . . ribosomal protein L35a pseudogene 30 . . . . . . . . . . . RPL35AP31 . . . ribosomal protein L35a pseudogene 31 . . . . . . . . . . . RPL35AP32 . . . ribosomal protein L35a pseudogene 32 . . . . . . . . . . . RPL35AP33 . . . ribosomal protein L35a pseudogene 33 . . . . . . . . . . . RPL35AP34 . . . ribosomal protein L35a pseudogene 34 . . . . . . . . . . . RPL35AP35 . . . ribosomal protein L35a pseudogene 35 . . . . . . . . . . . RPL35AP36 . . . ribosomal protein L35a pseudogene 36 . . . . . . . . . . . RPL35AP37 . . . ribosomal protein L35a pseudogene 37 . . . . . . . . . . . RPL35P1 . . . ribosomal protein L35 pseudogene 1 . . . . . . . . . . . RPL35P2 . . . ribosomal protein L35 pseudogene 2 . . . . . . . . . . . RPL35P3 . . . ribosomal protein L35 pseudogene 3 . . . . . . . . . . . RPL35P4 . . . ribosomal protein L35 pseudogene 4 . . . . . . . . . . . RPL35P5 . . . ribosomal protein L35 pseudogene 5 . . . . . . . . . . . RPL35P6 . . . ribosomal protein L35 pseudogene 6 . . . . . . . . . . . RPL35P7 . . . ribosomal protein L35 pseudogene 7 . . . . . . . . . . . RPL35P8 . . . ribosomal protein L35 pseudogene 8 . . . . . . . . . . . RPL35P9 . . . ribosomal protein L35 pseudogene 9 . . . . . . . . . . . RPL36 0.623121945323737 0.345174543576371 0.0317035110998925 ribosomal protein L36 . . . myocardium;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;pituitary gland;testis;brain;artery;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;trabecular meshwork;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; adrenal cortex;tumor; 0.14862 0.15145 0.035072054 56.2514744 4.69498 0.16843 RPL36A 0.79320686438897 0.200801680350886 0.00599145526014416 ribosomal protein L36a . . . . . 0.28680 0.22085 0.257356108 69.83368719 6.95413 0.25870 RPL36A-HNRNPH2 . . . RPL36A-HNRNPH2 readthrough . . . . . . . . . . . RPL36AL 0.0418331992833221 0.657110156022564 0.301056644694114 ribosomal protein L36a like . . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12490704}.; myocardium;ovary;umbilical cord;foreskin;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;developmental;intestine;colon;choroid;vein;uterus;bone;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;muscle;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta; ovary;beta cell islets;white blood cells;whole blood; 0.41740 0.12214 -0.009020804 52.8544468 2.07933 0.06803 RPL36AP1 . . . ribosomal protein L36a pseudogene 1 . . . . . . . . . . . RPL36AP2 . . . ribosomal protein L36a pseudogene 2 . . . . . . . . . . . RPL36AP4 . . . ribosomal protein L36a pseudogene 4 . . . . . . . . . . . RPL36AP5 . . . ribosomal protein L36a pseudogene 5 . . . . . . . . . . . RPL36AP6 . . . ribosomal protein L36a pseudogene 6 . . . . . . . . . . . RPL36AP7 . . . ribosomal protein L36a pseudogene 7 . . . . . . . . . . . RPL36AP8 . . . ribosomal protein L36a pseudogene 8 . . . . . . . . . . . RPL36AP9 . . . ribosomal protein L36a pseudogene 9 . . . . . . . . . . . RPL36AP10 . . . ribosomal protein L36a pseudogene 10 . . . . . . . . . . . RPL36AP11 . . . ribosomal protein L36a pseudogene 11 . . . . . . . . . . . RPL36AP12 . . . ribosomal protein L36a pseudogene 12 . . . . . . . . . . . RPL36AP13 . . . ribosomal protein L36a pseudogene 13 . . . . . . . . . . . RPL36AP14 . . . ribosomal protein L36a pseudogene 14 . . . . . . . . . . . RPL36AP15 . . . ribosomal protein L36a pseudogene 15 . . . . . . . . . . . RPL36AP16 . . . ribosomal protein L36a pseudogene 16 . . . . . . . . . . . RPL36AP17 . . . ribosomal protein L36a pseudogene 17 . . . . . . . . . . . RPL36AP18 . . . ribosomal protein L36a pseudogene 18 . . . . . . . . . . . RPL36AP19 . . . ribosomal protein L36a pseudogene 19 . . . . . . . . . . . RPL36AP20 . . . ribosomal protein L36a pseudogene 20 . . . . . . . . . . . RPL36AP21 . . . ribosomal protein L36a pseudogene 21 . . . . . . . . . . . RPL36AP23 . . . ribosomal protein L36a pseudogene 23 . . . . . . . . . . . RPL36AP24 . . . ribosomal protein L36a pseudogene 24 . . . . . . . . . . . RPL36AP25 . . . ribosomal protein L36a pseudogene 25 . . . . . . . . . . . RPL36AP26 . . . ribosomal protein L36a pseudogene 26 . . . . . . . . . . . RPL36AP27 . . . ribosomal protein L36a pseudogene 27 . . . . . . . . . . . RPL36AP28 . . . ribosomal protein L36a pseudogene 28 . . . . . . . . . . . RPL36AP29 . . . ribosomal protein L36a pseudogene 29 . . . . . . . . . . . RPL36AP30 . . . ribosomal protein L36a pseudogene 30 . . . . . . . . . . . RPL36AP31 . . . ribosomal protein L36a pseudogene 31 . . . . . . . . . . . RPL36AP32 . . . ribosomal protein L36a pseudogene 32 . . . . . . . . . . . RPL36AP33 . . . ribosomal protein L36a pseudogene 33 . . . . . . . . . . . RPL36AP34 . . . ribosomal protein L36a pseudogene 34 . . . . . . . . . . . RPL36AP35 . . . ribosomal protein L36a pseudogene 35 . . . . . . . . . . . RPL36AP36 . . . ribosomal protein L36a pseudogene 36 . . . . . . . . . . . RPL36AP37 . . . ribosomal protein L36a pseudogene 37 . . . . . . . . . . . RPL36AP38 . . . ribosomal protein L36a pseudogene 38 . . . . . . . . . . . RPL36AP39 . . . ribosomal protein L36a pseudogene 39 . . . . . . . . . . . RPL36AP40 . . . ribosomal protein L36a pseudogene 40 . . . . . . . . . . . RPL36AP41 . . . ribosomal protein L36a pseudogene 41 . . . . . . . . . . . RPL36AP42 . . . ribosomal protein L36a pseudogene 42 . . . . . . . . . . . RPL36AP43 . . . ribosomal protein L36a pseudogene 43 . . . . . . . . . . . RPL36AP44 . . . ribosomal protein L36a pseudogene 44 . . . . . . . . . . . RPL36AP45 . . . ribosomal protein L36a pseudogene 45 . . . . . . . . . . . RPL36AP46 . . . ribosomal protein L36a pseudogene 46 . . . . . . . . . . . RPL36AP47 . . . ribosomal protein L36a pseudogene 47 . . . . . . . . . . . RPL36AP48 . . . ribosomal protein L36a pseudogene 48 . . . . . . . . . . . RPL36AP49 . . . ribosomal protein L36a pseudogene 49 . . . . . . . . . . . RPL36AP50 . . . ribosomal protein L36a pseudogene 50 . . . . . . . . . . . RPL36AP51 . . . ribosomal protein L36a pseudogene 51 . . . . . . . . . . . RPL36AP53 . . . ribosomal protein L36a pseudogene 53 . . . . . . . . . . . RPL36AP54 . . . ribosomal protein L36a pseudogene 54 . . . . . . . . . . . RPL36AP55 . . . ribosomal protein L36a pseudogene 55 . . . . . . . . . . . RPL36P1 . . . ribosomal protein L36 pseudogene 1 . . . . . . . . . . . RPL36P2 . . . ribosomal protein L36 pseudogene 2 . . . . . . . . . . . RPL36P3 . . . ribosomal protein L36 pseudogene 3 . . . . . . . . . . . RPL36P4 . . . ribosomal protein L36 pseudogene 4 . . . . . . . . . . . RPL36P5 . . . ribosomal protein L36 pseudogene 5 . . . . . . . . . . . RPL36P6 . . . ribosomal protein L36 pseudogene 6 . . . . . . . . . . . RPL36P7 . . . ribosomal protein L36 pseudogene 7 . . . . . . . . . . . RPL36P8 . . . ribosomal protein L36 pseudogene 8 . . . . . . . . . . . RPL36P9 . . . ribosomal protein L36 pseudogene 9 . . . . . . . . . . . RPL36P10 . . . ribosomal protein L36 pseudogene 10 . . . . . . . . . . . RPL36P11 . . . ribosomal protein L36 pseudogene 11 . . . . . . . . . . . RPL36P12 . . . ribosomal protein L36 pseudogene 12 . . . . . . . . . . . RPL36P13 . . . ribosomal protein L36 pseudogene 13 . . . . . . . . . . . RPL36P14 . . . ribosomal protein L36 pseudogene 14 . . . . . . . . . . . RPL36P15 . . . ribosomal protein L36 pseudogene 15 . . . . . . . . . . . RPL36P16 . . . ribosomal protein L36 pseudogene 16 . . . . . . . . . . . RPL36P17 . . . ribosomal protein L36 pseudogene 17 . . . . . . . . . . . RPL36P18 . . . ribosomal protein L36 pseudogene 18 . . . . . . . . . . . RPL36P19 . . . ribosomal protein L36 pseudogene 19 . . . . . . . . . . . RPL36P20 . . . ribosomal protein L36 pseudogene 20 . . . . . . . . . . . RPL37 0.577671288406045 0.411363789173122 0.0109649224208325 ribosomal protein L37 FUNCTION: Binds to the 23S rRNA. {ECO:0000250}.; . . lymphoreticular;ovary;foreskin;skin;bone marrow;prostate;frontal lobe;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;vein;uterus;cerebral cortex;bone;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;epidermis;islets of Langerhans;muscle;bile duct;pancreas;pia mater;lung;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;kidney;stomach;aorta; ovary;white blood cells;skin; 0.59796 0.11453 -0.009020804 52.8544468 4.87318 0.17976 RPL37A 0.00477076544447004 0.686014766378007 0.309214468177523 ribosomal protein L37a . . . myocardium;lymphoreticular;ovary;skin;bone marrow;prostate;frontal lobe;endometrium;thyroid;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;uterus;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; . 0.92832 0.16306 0.035072054 56.2514744 4.13006 0.15138 RPL37AP1 . . . ribosomal protein L37a pseudogene 1 . . . . . . . . . . . RPL37AP2 . . . ribosomal protein L37a pseudogene 2 . . . . . . . . . . . RPL37AP3 . . . ribosomal protein L37a pseudogene 3 . . . . . . . . . . . RPL37AP4 . . . ribosomal protein L37a pseudogene 4 . . . . . . . . . . . RPL37AP5 . . . ribosomal protein L37a pseudogene 5 . . . . . . . . . . . RPL37AP6 . . . ribosomal protein L37a pseudogene 6 . . . . . . . . . . . RPL37AP7 . . . ribosomal protein L37a pseudogene 7 . . . . . . . . . . . RPL37AP8 . . . ribosomal protein L37a pseudogene 8 . . . . . . . . . . . RPL37AP9 . . . ribosomal protein L37a pseudogene 9 . . . . . . . . . . . RPL37P1 . . . ribosomal protein L37 pseudogene 1 . . . . . . . . . . . RPL37P2 . . . ribosomal protein L37 pseudogene 2 . . . . . . . . . . . RPL37P3 . . . ribosomal protein L37 pseudogene 3 . . . . . . . . . . . RPL37P4 . . . ribosomal protein L37 pseudogene 4 . . . . . . . . . . . RPL37P5 . . . ribosomal protein L37 pseudogene 5 . . . . . . . . . . . RPL37P6 . . . ribosomal protein L37 pseudogene 6 . . . . . . . . . . . RPL37P7 . . . ribosomal protein L37 pseudogene 7 . . . . . . . . . . . RPL37P8 . . . ribosomal protein L37 pseudogene 8 . . . . . . . . . . . RPL37P9 . . . ribosomal protein L37 pseudogene 9 . . . . . . . . . . . RPL37P10 . . . ribosomal protein L37 pseudogene 10 . . . . . . . . . . . RPL37P11 . . . ribosomal protein L37 pseudogene 11 . . . . . . . . . . . RPL37P12 . . . ribosomal protein L37 pseudogene 12 . . . . . . . . . . . RPL37P13 . . . ribosomal protein L37 pseudogene 13 . . . . . . . . . . . RPL37P14 . . . ribosomal protein L37 pseudogene 14 . . . . . . . . . . . RPL37P15 . . . ribosomal protein L37 pseudogene 15 . . . . . . . . . . . RPL37P16 . . . ribosomal protein L37 pseudogene 16 . . . . . . . . . . . RPL37P17 . . . ribosomal protein L37 pseudogene 17 . . . . . . . . . . . RPL37P18 . . . ribosomal protein L37 pseudogene 18 . . . . . . . . . . . RPL37P19 . . . ribosomal protein L37 pseudogene 19 . . . . . . . . . . . RPL37P20 . . . ribosomal protein L37 pseudogene 20 . . . . . . . . . . . RPL37P21 . . . ribosomal protein L37 pseudogene 21 . . . . . . . . . . . RPL37P22 . . . ribosomal protein L37 pseudogene 22 . . . . . . . . . . . RPL37P23 . . . ribosomal protein L37 pseudogene 23 . . . . . . . . . . . RPL37P24 . . . ribosomal protein L37 pseudogene 24 . . . . . . . . . . . RPL37P25 . . . ribosomal protein L37 pseudogene 25 . . . . . . . . . . . RPL38 0.890753137672675 0.10812394748514 0.0011229148421852 ribosomal protein L38 . . . lymphoreticular;ovary;salivary gland;developmental;intestine;colon;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;oesophagus;bone;testis;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;trophoblast;lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;pia mater;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; liver;testis;cingulate cortex;skeletal muscle; 0.83967 0.24974 0.035072054 56.2514744 . . RPL38P1 . . . ribosomal protein L38 pseudogene 1 . . . . . . . . . . . RPL38P2 . . . ribosomal protein L38 pseudogene 2 . . . . . . . . . . . RPL38P3 . . . ribosomal protein L38 pseudogene 3 . . . . . . . . . . . RPL38P4 . . . ribosomal protein L38 pseudogene 4 . . . . . . . . . . . RPL39 0.620183578382466 0.347394631312881 0.032421790304653 ribosomal protein L39 . . . myocardium;lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;tongue;pharynx;blood;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;pancreas;lung;cornea;placenta;hypopharynx;head and neck;kidney;stomach;aorta; . 0.58801 0.12971 0.145304857 63.81221986 . . RPL39L 0.175781234610387 0.643933814252144 0.180284951137469 ribosomal protein L39 like . . TISSUE SPECIFICITY: Testis specific.; unclassifiable (Anatomical System);ovary;cartilage;skin;uterus;pancreas;prostate;lung;endometrium;bone;visual apparatus;testis;brain;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.68054 0.09208 0.3455435 73.78509082 73.11093 1.78619 RPL39P . . . ribosomal protein L39 pseudogene . . . . . . . . . . . RPL39P2 . . . ribosomal protein L39 pseudogene 2 . . . . . . . . . . . RPL39P3 . . . ribosomal protein L39 pseudogene 3 . . . . . . . . . . . RPL39P4 . . . ribosomal protein L39 pseudogene 4 . . . . . . . . . . . RPL39P5 . . . ribosomal protein L39 pseudogene 5 . . . . . . . . . . . RPL39P6 . . . ribosomal protein L39 pseudogene 6 . . . . . . . . . . . RPL39P7 . . . ribosomal protein L39 pseudogene 7 . . . . . . . . . . . RPL39P8 . . . ribosomal protein L39 pseudogene 8 . . . . . . . . . . . RPL39P9 . . . ribosomal protein L39 pseudogene 9 . . . . . . . . . . . RPL39P10 . . . ribosomal protein L39 pseudogene 10 . . . . . . . . . . . RPL39P11 . . . ribosomal protein L39 pseudogene 11 . . . . . . . . . . . RPL39P12 . . . ribosomal protein L39 pseudogene 12 . . . . . . . . . . . RPL39P13 . . . ribosomal protein L39 pseudogene 13 . . . . . . . . . . . RPL39P14 . . . ribosomal protein L39 pseudogene 14 . . . . . . . . . . . RPL39P15 . . . ribosomal protein L39 pseudogene 15 . . . . . . . . . . . RPL39P16 . . . ribosomal protein L39 pseudogene 16 . . . . . . . . . . . RPL39P17 . . . ribosomal protein L39 pseudogene 17 . . . . . . . . . . . RPL39P18 . . . ribosomal protein L39 pseudogene 18 . . . . . . . . . . . RPL39P19 . . . ribosomal protein L39 pseudogene 19 . . . . . . . . . . . RPL39P20 . . . ribosomal protein L39 pseudogene 20 . . . . . . . . . . . RPL39P21 . . . ribosomal protein L39 pseudogene 21 . . . . . . . . . . . RPL39P22 . . . ribosomal protein L39 pseudogene 22 . . . . . . . . . . . RPL39P23 . . . ribosomal protein L39 pseudogene 23 . . . . . . . . . . . RPL39P24 . . . ribosomal protein L39 pseudogene 24 . . . . . . . . . . . RPL39P25 . . . ribosomal protein L39 pseudogene 25 . . . . . . . . . . . RPL39P26 . . . ribosomal protein L39 pseudogene 26 . . . . . . . . . . . RPL39P27 . . . ribosomal protein L39 pseudogene 27 . . . . . . . . . . . RPL39P28 . . . ribosomal protein L39 pseudogene 28 . . . . . . . . . . . RPL39P29 . . . ribosomal protein L39 pseudogene 29 . . . . . . . . . . . RPL39P30 . . . ribosomal protein L39 pseudogene 30 . . . . . . . . . . . RPL39P31 . . . ribosomal protein L39 pseudogene 31 . . . . . . . . . . . RPL39P32 . . . ribosomal protein L39 pseudogene 32 . . . . . . . . . . . RPL39P33 . . . ribosomal protein L39 pseudogene 33 . . . . . . . . . . . RPL39P34 . . . ribosomal protein L39 pseudogene 34 . . . . . . . . . . . RPL39P35 . . . ribosomal protein L39 pseudogene 35 . . . . . . . . . . . RPL39P36 . . . ribosomal protein L39 pseudogene 36 . . . . . . . . . . . RPL39P37 . . . ribosomal protein L39 pseudogene 37 . . . . . . . . . . . RPL39P38 . . . ribosomal protein L39 pseudogene 38 . . . . . . . . . . . RPL39P39 . . . ribosomal protein L39 pseudogene 39 . . . . . . . . . . . RPL39P40 . . . ribosomal protein L39 pseudogene 40 . . . . . . . . . . . RPL39P41 . . . ribosomal protein L39 pseudogene 41 . . . . . . . . . . . RPL41 0.0415295991097929 0.655764243148309 0.302706157741898 ribosomal protein L41 FUNCTION: Interacts with the beta subunit of protein kinase CKII and stimulates phosphorylation of DNA topoisomerase II alpha by CKII.; . . myocardium;ovary;skin;bone marrow;prostate;thyroid;bladder;brain;gall bladder;heart;cartilage;tongue;pharynx;blood;skeletal muscle;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; . 0.42246 . 0.145304857 63.81221986 . . RPL41P1 . . . ribosomal protein L41 pseudogene 1 . . . . . . . . . . . RPL41P2 . . . ribosomal protein L41 pseudogene 2 . . . . . . . . . . . RPL41P3 . . . ribosomal protein L41 pseudogene 3 . . . . . . . . . . . RPL41P4 . . . ribosomal protein L41 pseudogene 4 . . . . . . . . . . . RPL41P5 . . . ribosomal protein L41 pseudogene 5 . . . . . . . . . . . RPL41P6 . . . ribosomal protein L41 pseudogene 6 . . . . . . . . . . . RPL41P7 . . . ribosomal protein L41 pseudogene 7 . . . . . . . . . . . RPLP0 0.978691782887372 0.0212894872200496 1.87298925781529e-05 ribosomal protein lateral stalk subunit P0 FUNCTION: Ribosomal protein P0 is the functional equivalent of E.coli protein L10.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;bladder;brain;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;vein;uterus;whole body;oesophagus;cerebral cortex;bone;testis;dura mater;unclassifiable (Anatomical System);lymph node;islets of Langerhans;oral cavity;pancreas;lung;cornea;placenta;duodenum;head and neck;kidney;stomach;aorta; . 0.99689 0.28104 -0.029247611 51.40363293 28.4761 0.91158 RPLP1 0.680907046710861 0.299361142088681 0.0197318112004584 ribosomal protein lateral stalk subunit P1 FUNCTION: Plays an important role in the elongation step of protein synthesis.; . . myocardium;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;thyroid;bladder;brain;gall bladder;heart;tongue;spinal cord;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;uterus;whole body;oesophagus;larynx;pituitary gland;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;amnion;head and neck;kidney;stomach; . 0.31003 0.21177 -0.053113545 49.38664779 6.91851 0.25752 RPLP1P1 . . . ribosomal protein lateral stalk subunit P1 pseudogene 1 . . . . . . . . . . . RPLP1P2 . . . ribosomal protein lateral stalk subunit P1 pseudogene 2 . . . . . . . . . . . RPLP1P3 . . . ribosomal protein lateral stalk subunit P1 pseudogene 3 . . . . . . . . . . . RPLP1P4 . . . ribosomal protein lateral stalk subunit P1 pseudogene 4 . . . . . . . . . . . RPLP1P5 . . . ribosomal protein lateral stalk subunit P1 pseudogene 5 . . . . . . . . . . . RPLP1P6 . . . ribosomal protein lateral stalk subunit P1 pseudogene 6 . . . . . . . . . . . RPLP1P7 . . . ribosomal protein lateral stalk subunit P1 pseudogene 7 . . . . . . . . . . . RPLP1P8 . . . ribosomal protein lateral stalk subunit P1 pseudogene 8 . . . . . . . . . . . RPLP1P9 . . . ribosomal protein lateral stalk subunit P1 pseudogene 9 . . . . . . . . . . . RPLP1P10 . . . ribosomal protein lateral stalk subunit P1 pseudogene 10 . . . . . . . . . . . RPLP1P11 . . . ribosomal protein lateral stalk subunit P1 pseudogene 11 . . . . . . . . . . . RPLP1P12 . . . ribosomal protein lateral stalk subunit P1 pseudogene 12 . . . . . . . . . . . RPLP1P13 . . . ribosomal protein lateral stalk subunit P1 pseudogene 13 . . . . . . . . . . . RPLP2 0.708517552606227 0.276168887211356 0.0153135601824168 ribosomal protein lateral stalk subunit P2 FUNCTION: Plays an important role in the elongation step of protein synthesis.; . . myocardium;lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;duodenum;kidney;stomach; prostate;lung;heart;liver;appendix;tumor;white blood cells;skin;thymus; 0.81054 0.28104 -0.185391282 39.67916962 49.14713 1.37083 RPLP2P1 . . . ribosomal protein lateral stalk subunit P2 pseudogene 1 . . . . . . . . . . . RPLP2P2 . . . ribosomal protein lateral stalk subunit P2 pseudogene 2 . . . . . . . . . . . RPLP2P3 . . . ribosomal protein lateral stalk subunit P2 pseudogene 3 . . . . . . . . . . . RPLP2P4 . . . ribosomal protein lateral stalk subunit P2 pseudogene 4 . . . . . . . . . . . RPLP2P5 . . . ribosomal protein lateral stalk subunit P2 pseudogene 5 . . . . . . . . . . . RPLP0P1 . . . ribosomal protein lateral stalk subunit P0 pseudogene 1 . . . . . . . . . . . RPLP0P2 . . . ribosomal protein lateral stalk subunit P0 pseudogene 2 . . . . . . . . . . . RPLP0P3 . . . ribosomal protein lateral stalk subunit P0 pseudogene 3 . . . . . . . . . . . RPLP0P4 . . . ribosomal protein lateral stalk subunit P0 pseudogene 4 . . . . . . . . . . . RPLP0P5 . . . ribosomal protein lateral stalk subunit P0 pseudogene 5 . . . . . . . . . . . RPLP0P6 . . . ribosomal protein lateral stalk subunit P0 pseudogene 6 FUNCTION: Ribosomal protein P0 is the functional equivalent of E.coli protein L10. {ECO:0000250}.; . . . . . . . . . . RPLP0P7 . . . ribosomal protein lateral stalk subunit P0 pseudogene 7 . . . . . . . . . . . RPLP0P8 . . . ribosomal protein lateral stalk subunit P0 pseudogene 8 . . . . . . . . . . . RPLP0P10 . . . ribosomal protein lateral stalk subunit P0 pseudogene 10 . . . . . . . . . . . RPLP0P11 . . . ribosomal protein lateral stalk subunit P0 pseudogene 11 . . . . . . . . . . . RPN1 0.664450734249708 0.335326055321061 0.000223210429231127 ribophorin I FUNCTION: Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains.; . TISSUE SPECIFICITY: Expressed in all tissues tested. {ECO:0000269|PubMed:12887896}.; ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;amniotic fluid;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta; prostate;lung;liver;testis; 0.23265 0.32102 -0.023789244 52.09365416 192.21644 3.00497 RPN2 0.0316773430272863 0.967931604166003 0.000391052806710438 ribophorin II FUNCTION: Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains.; . TISSUE SPECIFICITY: Expressed in all tissues tested.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; prostate;smooth muscle;testis - seminiferous tubule;placenta;thyroid;testis;white blood cells;fetal thyroid; 0.34633 0.47228 -0.352661697 29.48808681 334.67267 3.88778 RPP14 0.147340973271617 0.778125560468509 0.0745334662598742 ribonuclease P/MRP 14kDa subunit FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.; . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);islets of Langerhans;oral cavity;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;liver;amnion;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.10300 . 0.435547893 77.45340882 173.61913 2.87003 RPP21 0.0824539766931298 0.871769274546857 0.045776748760013 ribonuclease P/MRP 21kDa subunit FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.; . . . . 0.15015 0.10752 0.547599505 81.2160887 382.25131 4.12171 RPP25 0.00695757715935081 0.526491185218539 0.46655123762211 ribonuclease P/MRP 25kDa subunit FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP. This subunit binds to RNA.; . . unclassifiable (Anatomical System);lymphoreticular;lymph node;islets of Langerhans;colon;choroid;lens;skin;retina;pancreas;prostate;whole body;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;brain;mammary gland;stomach; . 0.12345 0.10020 . . 11.09115 0.40197 RPP25L 0.834923218511704 0.161787973637054 0.00328880785124145 ribonuclease P/MRP 25kDa subunit-like FUNCTION: May be a component of ribonuclease P or MRP.; . . . . 0.08468 . -0.163345027 41.24793583 3.34053 0.12205 RPP30 2.35352304647074e-05 0.91266574462602 0.087310720143515 ribonuclease P/MRP 30kDa subunit FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.; . . umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.25392 0.24934 0.106667882 61.73036093 95.28898 2.10698 RPP38 1.68152550937737e-05 0.138930430368587 0.861052754376319 ribonuclease P/MRP 38kDa subunit FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. RPP38 may associate transiently with RNase P RNA as a factor involved in the transport of H1 RNA to the putative site of its assembly in the cell, the nucleolus.; . . . . 0.02901 0.08485 0.92967242 89.79122435 2905.41106 10.22045 RPP40 0.00257720793912516 0.932656444259557 0.0647663478013176 ribonuclease P/MRP 40kDa subunit FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.; . . medulla oblongata;ovary;salivary gland;intestine;colon;skin;uterus;whole body;larynx;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;pharynx;blood;lung;cornea;nasopharynx;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland; superior cervical ganglion; 0.09601 0.09999 0.52918614 80.81505072 902.88839 5.84863 RPP40P1 . . . ribonuclease P/MRP 40kDa subunit pseudogene 1 . . . . . . . . . . . RPP40P2 . . . ribonuclease P/MRP 40kDa subunit pseudogene 2 . . . . . . . . . . . RPPH1 . . . ribonuclease P RNA component H1 . . . . . . . . . . . RPPH1-2P . . . ribonuclease P RNA component H1, 2 pseudogene . . . . . . . . . . . RPPH1-3P . . . ribonuclease P RNA component H1, 3 pseudogene . . . . . . . . . . . RPRD1A 0.25114910852473 0.742592710280219 0.00625818119505087 regulation of nuclear pre-mRNA domain containing 1A FUNCTION: Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD. May act as a negative regulator of cyclin-D1 (CCND1) and cyclin-E (CCNE1) in the cell cycle. {ECO:0000269|PubMed:22231121}.; . . medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;germinal center;brain;bladder;gall bladder;amygdala;cartilage;heart;tongue;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;developmental;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pia mater;lung;placenta;hippocampus;kidney;stomach;thymus; amygdala;superior cervical ganglion;subthalamic nucleus;occipital lobe;globus pallidus; . 0.10913 -0.273576253 33.97027601 1.55424 0.05138 RPRD1B 0.595211393438137 0.404376117738216 0.000412488823647304 regulation of nuclear pre-mRNA domain containing 1B FUNCTION: Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD. Transcriptional regulator which enhances expression of CCND1. Promotes binding of RNA polymerase II to the CCDN1 promoter and to the termination region before the poly-A site but decreases its binding after the poly-A site. Prevents RNA polymerase II from reading through the 3' end termination site and may allow it to be recruited back to the promoter through promotion of the formation of a chromatin loop. Also enhances the transcription of a number of other cell cycle-related genes including CDK2, CDK4, CDK6 and cyclin-E but not CDKN1A, CDKN1B or cyclin-A. Promotes cell proliferation. {ECO:0000269|PubMed:22231121, ECO:0000269|PubMed:22264791}.; . TISSUE SPECIFICITY: Preferentially expressed in a range of tumor tissues including colon, lung, liver, breast, prostate, stomach, uterine endometrium and cervical cancers with higher levels in tumors than in adjacent non-tumor tissue (at protein level). {ECO:0000269|PubMed:22264791}.; . . 0.30358 0.11809 -0.207437529 38.2814343 27.80674 0.89300 RPRD2 0.999977310558099 2.26894408560688e-05 1.04472882090676e-12 regulation of nuclear pre-mRNA domain containing 2 . . . . . 0.16389 0.09546 -0.795417163 12.5324369 369.12414 4.05963 RPRM 0.532566514880165 0.407808690589234 0.0596247945306016 reprimo, TP53 dependent G2 arrest mediator candidate FUNCTION: May be involved in the regulation of p53-dependent G2 arrest of the cell cycle. Seems to induce cell cycle arrest by inhibiting CDK1 activity and nuclear translocation of the CDC2 cyclin B1 complex (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;frontal lobe;visual apparatus;choroid;brain; . 0.62912 0.16306 0.035072054 56.2514744 2.27037 0.07684 RPRML 0.421294822682809 0.46423892303024 0.114466254286951 reprimo-like . . . unclassifiable (Anatomical System);medulla oblongata;brain; . 0.30486 . . . 586.94663 4.91364 RPS2 0.236872070471978 0.730777126265753 0.0323508032622693 ribosomal protein S2 . . . ovary;colon;vein;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;oesophagus;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;pineal body;urinary;adrenal cortex;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach;thymus; . 0.98312 . -0.560178693 19.30879925 9.93416 0.36390 RPS2P1 . . . ribosomal protein S2 pseudogene 1 . . . . . . . . . . . RPS2P2 . . . ribosomal protein S2 pseudogene 2 . . . . . . . . . . . RPS2P3 . . . ribosomal protein S2 pseudogene 3 . . . . . . . . . . . RPS2P4 . . . ribosomal protein S2 pseudogene 4 . . . . . . . . . . . RPS2P5 . . . ribosomal protein S2 pseudogene 5 . . . lymphoreticular;medulla oblongata;ovary;salivary gland;colon;skin;uterus;prostate;whole body;frontal lobe;cerebral cortex;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;adrenal cortex;lens;pancreas;lung;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach; . . . . . . . RPS2P6 . . . ribosomal protein S2 pseudogene 6 . . . . . . . . . . . RPS2P7 . . . ribosomal protein S2 pseudogene 7 . . . . . . . . . . . RPS2P8 . . . ribosomal protein S2 pseudogene 8 . . . . . . . . . . . RPS2P9 . . . ribosomal protein S2 pseudogene 9 . . . . . . . . . . . RPS2P10 . . . ribosomal protein S2 pseudogene 10 . . . . . . . . . . . RPS2P11 . . . ribosomal protein S2 pseudogene 11 . . . . . . . . . . . RPS2P12 . . . ribosomal protein S2 pseudogene 12 . . . . . . . . . . . RPS2P13 . . . ribosomal protein S2 pseudogene 13 . . . . . . . . . . . RPS2P14 . . . ribosomal protein S2 pseudogene 14 . . . . . . . . . . . RPS2P15 . . . ribosomal protein S2 pseudogene 15 . . . . . . . . . . . RPS2P16 . . . ribosomal protein S2 pseudogene 16 . . . . . . . . . . . RPS2P17 . . . ribosomal protein S2 pseudogene 17 . . . . . . . . . . . RPS2P18 . . . ribosomal protein S2 pseudogene 18 . . . . . . . . . . . RPS2P19 . . . ribosomal protein S2 pseudogene 19 . . . . . . . . . . . RPS2P20 . . . ribosomal protein S2 pseudogene 20 . . . . . . . . . . . RPS2P21 . . . ribosomal protein S2 pseudogene 21 . . . . . . . . . . . RPS2P22 . . . ribosomal protein S2 pseudogene 22 . . . . . . . . . . . RPS2P23 . . . ribosomal protein S2 pseudogene 23 . . . . . . . . . . . RPS2P24 . . . ribosomal protein S2 pseudogene 24 . . . . . . . . . . . RPS2P25 . . . ribosomal protein S2 pseudogene 25 . . . . . . . . . . . RPS2P26 . . . ribosomal protein S2 pseudogene 26 . . . . . . . . . . . RPS2P27 . . . ribosomal protein S2 pseudogene 27 . . . . . . . . . . . RPS2P28 . . . ribosomal protein S2 pseudogene 28 . . . . . . . . . . . RPS2P29 . . . ribosomal protein S2 pseudogene 29 . . . . . . . . . . . RPS2P30 . . . ribosomal protein S2 pseudogene 30 . . . . . . . . . . . RPS2P31 . . . ribosomal protein S2 pseudogene 31 . . . . . . . . . . . RPS2P32 . . . ribosomal protein S2 pseudogene 32 . . . . . . . . . . . RPS2P33 . . . ribosomal protein S2 pseudogene 33 . . . . . . . . . . . RPS2P34 . . . ribosomal protein S2 pseudogene 34 . . . . . . . . . . . RPS2P35 . . . ribosomal protein S2 pseudogene 35 . . . . . . . . . . . RPS2P36 . . . ribosomal protein S2 pseudogene 36 . . . . . . . . . . . RPS2P37 . . . ribosomal protein S2 pseudogene 37 . . . . . . . . . . . RPS2P38 . . . ribosomal protein S2 pseudogene 38 . . . . . . . . . . . RPS2P39 . . . ribosomal protein S2 pseudogene 39 . . . . . . . . . . . RPS2P40 . . . ribosomal protein S2 pseudogene 40 . . . . . . . . . . . RPS2P41 . . . ribosomal protein S2 pseudogene 41 . . . . . . . . . . . RPS2P42 . . . ribosomal protein S2 pseudogene 42 . . . . . . . . . . . RPS2P43 . . . ribosomal protein S2 pseudogene 43 . . . . . . . . . . . RPS2P44 . . . ribosomal protein S2 pseudogene 44 . . . . . . . . . . . RPS2P45 . . . ribosomal protein S2 pseudogene 45 . . . . . . . . . . . RPS2P46 . . . ribosomal protein S2 pseudogene 46 . . . . . . . . . . . RPS2P47 . . . ribosomal protein S2 pseudogene 47 . . . . . . . . . . . RPS2P48 . . . ribosomal protein S2 pseudogene 48 . . . . . . . . . . . RPS2P49 . . . ribosomal protein S2 pseudogene 49 . . . . . . . . . . . RPS2P50 . . . ribosomal protein S2 pseudogene 50 . . . . . . . . . . . RPS2P51 . . . ribosomal protein S2 pseudogene 51 . . . . . . . . . . . RPS2P52 . . . ribosomal protein S2 pseudogene 52 . . . . . . . . . . . RPS2P53 . . . ribosomal protein S2 pseudogene 53 . . . . . . . . . . . RPS2P54 . . . ribosomal protein S2 pseudogene 54 . . . . . . . . . . . RPS2P55 . . . ribosomal protein S2 pseudogene 55 . . . . . . . . . . . RPS3 0.957385985784031 0.0425098308232986 0.000104183392670803 ribosomal protein S3 FUNCTION: Involved in translation as a component of the 40S small ribosomal subunit (PubMed:8706699). Has endonuclease activity and plays a role in repair of damaged DNA (PubMed:7775413). Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (PubMed:15707971). Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (PubMed:14706345). Has also been shown to bind with similar affinity to intact and damaged DNA (PubMed:18610840). Stimulates the N-glycosylase activity of the base excision protein OGG1 (PubMed:15518571). Enhances the uracil excision activity of UNG1 (PubMed:18973764). Also stimulates the cleavage of the phosphodiester backbone by APEX1 (PubMed:18973764). When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (PubMed:23911537). Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (PubMed:17049931). Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes (PubMed:18045535). Represses its own translation by binding to its cognate mRNA (PubMed:20217897). Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (PubMed:19656744). Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (PubMed:23131551). Involved in induction of apoptosis through its role in activation of CASP8 (PubMed:14988002). Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787). Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (PubMed:22510408). {ECO:0000269|PubMed:14706345, ECO:0000269|PubMed:14988002, ECO:0000269|PubMed:15518571, ECO:0000269|PubMed:15707971, ECO:0000269|PubMed:17049931, ECO:0000269|PubMed:18045535, ECO:0000269|PubMed:18610840, ECO:0000269|PubMed:18973764, ECO:0000269|PubMed:19656744, ECO:0000269|PubMed:20217897, ECO:0000269|PubMed:20605787, ECO:0000269|PubMed:22510408, ECO:0000269|PubMed:23131551, ECO:0000269|PubMed:23911537, ECO:0000269|PubMed:7775413, ECO:0000269|PubMed:8706699}.; . . ovary;salivary gland;intestine;colon;skin;retina;bone marrow;prostate;frontal lobe;pituitary gland;testis;brain;bladder;lymph node;trophoblast;hypothalamus;pharynx;blood;bile duct;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;cervix;kidney;stomach; uterus corpus;lung;smooth muscle;ovary;heart;tumor;fetal lung;white blood cells;fetal thyroid;whole blood;bone marrow;thymus; 0.98620 0.45280 0.325313577 73.11276244 127.68923 2.46354 RPS3A 0.744269730691134 0.253389262853842 0.00234100645502421 ribosomal protein S3A FUNCTION: May play a role during erythropoiesis through regulation of transcription factor DDIT3. {ECO:0000255|HAMAP-Rule:MF_03122}.; . . lymphoreticular;umbilical cord;ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;thyroid;testis;dura mater;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);meninges;trophoblast;lymph node;cerebellum cortex;spinal cord;muscle;adrenal cortex;pharynx;blood;breast;bile duct;pia mater;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;head and neck;cervix;kidney;aorta;stomach; . 0.99653 0.30163 0.013025609 54.62962963 4.49164 0.16244 RPS3AP1 . . . ribosomal protein S3A pseudogene 1 . . . . . . . . . . . RPS3AP2 . . . ribosomal protein S3A pseudogene 2 . . . . . . . . . . . RPS3AP3 . . . ribosomal protein S3A pseudogene 3 . . . . . . . . . . . RPS3AP4 . . . ribosomal protein S3A pseudogene 4 . . . . . . . . . . . RPS3AP5 . . . ribosomal protein S3A pseudogene 5 . . . . . . . . . . . RPS3AP6 . . . ribosomal protein S3A pseudogene 6 . . . . . . . . . . . RPS3AP7 . . . ribosomal protein S3a pseudogene 7 . . . . . . . . . . . RPS3AP8 . . . ribosomal protein S3a pseudogene 8 . . . . . . . . . . . RPS3AP9 . . . ribosomal protein S3a pseudogene 9 . . . . . . . . . . . RPS3AP10 . . . ribosomal protein S3a pseudogene 10 . . . . . . . . . . . RPS3AP11 . . . ribosomal protein S3a pseudogene 11 . . . . . . . . . . . RPS3AP12 . . . ribosomal protein S3a pseudogene 12 . . . . . . . . . . . RPS3AP14 . . . ribosomal protein S3a pseudogene 14 . . . . . . . . . . . RPS3AP15 . . . ribosomal protein S3a pseudogene 15 . . . . . . . . . . . RPS3AP16 . . . ribosomal protein S3a pseudogene 16 . . . . . . . . . . . RPS3AP17 . . . ribosomal protein S3a pseudogene 17 . . . . . . . . . . . RPS3AP18 . . . ribosomal protein S3a pseudogene 18 . . . . . . . . . . . RPS3AP19 . . . ribosomal protein S3a pseudogene 19 . . . . . . . . . . . RPS3AP20 . . . ribosomal protein S3a pseudogene 20 . . . . . . . . . . . RPS3AP21 . . . ribosomal protein S3a pseudogene 21 . . . . . . . . . . . RPS3AP22 . . . ribosomal protein S3a pseudogene 22 . . . . . . . . . . . RPS3AP23 . . . ribosomal protein S3a pseudogene 23 . . . . . . . . . . . RPS3AP24 . . . ribosomal protein S3a pseudogene 24 . . . . . . . . . . . RPS3AP25 . . . ribosomal protein S3a pseudogene 25 . . . . . . . . . . . RPS3AP26 . . . ribosomal protein S3a pseudogene 26 . . . . . . . . . . . RPS3AP27 . . . ribosomal protein S3a pseudogene 27 . . . . . . . . . . . RPS3AP28 . . . ribosomal protein S3a pseudogene 28 . . . . . . . . . . . RPS3AP29 . . . ribosomal protein S3a pseudogene 29 . . . . . . . . . . . RPS3AP30 . . . ribosomal protein S3a pseudogene 30 . . . . . . . . . . . RPS3AP31 . . . ribosomal protein S3a pseudogene 31 . . . . . . . . . . . RPS3AP32 . . . ribosomal protein S3a pseudogene 32 . . . . . . . . . . . RPS3AP33 . . . ribosomal protein S3a pseudogene 33 . . . . . . . . . . . RPS3AP34 . . . ribosomal protein S3a pseudogene 34 . . . . . . . . . . . RPS3AP35 . . . ribosomal protein S3a pseudogene 35 . . . . . . . . . . . RPS3AP36 . . . ribosomal protein S3a pseudogene 36 . . . . . . . . . . . RPS3AP37 . . . ribosomal protein S3a pseudogene 37 . . . . . . . . . . . RPS3AP38 . . . ribosomal protein S3a pseudogene 38 . . . . . . . . . . . RPS3AP39 . . . ribosomal protein S3a pseudogene 39 . . . . . . . . . . . RPS3AP40 . . . ribosomal protein S3a pseudogene 40 . . . . . . . . . . . RPS3AP41 . . . ribosomal protein S3a pseudogene 41 . . . . . . . . . . . RPS3AP42 . . . ribosomal protein S3a pseudogene 42 . . . . . . . . . . . RPS3AP43 . . . ribosomal protein S3a pseudogene 43 . . . . . . . . . . . RPS3AP44 . . . ribosomal protein S3a pseudogene 44 . . . . . . . . . . . RPS3AP46 . . . ribosomal protein S3a pseudogene 46 . . . . . . . . . . . RPS3AP47 . . . ribosomal protein S3a pseudogene 47 . . . . . . . . . . . RPS3AP48 . . . ribosomal protein S3a pseudogene 48 . . . . . . . . . . . RPS3AP49 . . . ribosomal protein S3a pseudogene 49 . . . . . . . . . . . RPS3AP50 . . . ribosomal protein S3a pseudogene 50 . . . . . . . . . . . RPS3AP51 . . . ribosomal protein S3a pseudogene 51 . . . . . . . . . . . RPS3AP52 . . . ribosomal protein S3a pseudogene 52 . . . . . . . . . . . RPS3AP53 . . . ribosomal protein S3a pseudogene 53 . . . . . . . . . . . RPS3AP54 . . . ribosomal protein S3a pseudogene 54 . . . . . . . . . . . RPS3P1 . . . ribosomal protein S3 pseudogene 1 . . . . . . . . . . . RPS3P2 . . . ribosomal protein S3 pseudogene 2 . . . . . . . . . . . RPS3P3 . . . ribosomal protein S3 pseudogene 3 . . . . . . . . . . . RPS3P4 . . . ribosomal protein S3 pseudogene 4 . . . . . . . . . . . RPS3P5 . . . ribosomal protein S3 pseudogene 5 . . . . . . . . . . . RPS3P6 . . . ribosomal protein S3 pseudogene 6 . . . . . . . . . . . RPS3P7 . . . ribosomal protein S3 pseudogene 7 . . . . . . . . . . . RPS4X 0.886149633662523 0.112601537037442 0.00124882930003548 ribosomal protein S4, X-linked . . . . . 0.89002 . 0.057118534 57.99716914 . . RPS4XP1 . . . ribosomal protein S4X pseudogene 1 . . . . . . . . . . . RPS4XP2 . . . ribosomal protein S4X pseudogene 2 . . . . . . . . . . . RPS4XP3 . . . ribosomal protein S4X pseudogene 3 . . . . . . . . . . . RPS4XP4 . . . ribosomal protein S4X pseudogene 4 . . . . . . . . . . . RPS4XP5 . . . ribosomal protein S4X pseudogene 5 . . . . . . . . . . . RPS4XP6 . . . ribosomal protein S4X pseudogene 6 . . . . . . . . . . . RPS4XP7 . . . ribosomal protein S4X pseudogene 7 . . . . . . . . . . . RPS4XP8 . . . ribosomal protein S4X pseudogene 8 . . . . . . . . . . . RPS4XP9 . . . ribosomal protein S4X pseudogene 9 . . . . . . . . . . . RPS4XP10 . . . ribosomal protein S4X pseudogene 10 . . . . . . . . . . . RPS4XP11 . . . ribosomal protein S4X pseudogene 11 . . . . . . . . . . . RPS4XP12 . . . ribosomal protein S4X pseudogene 12 . . . . . . . . . . . RPS4XP13 . . . ribosomal protein S4X pseudogene 13 . . . . . . . . . . . RPS4XP14 . . . ribosomal protein S4X pseudogene 14 . . . . . . . . . . . RPS4XP15 . . . ribosomal protein S4X pseudogene 15 . . . . . . . . . . . RPS4XP16 . . . ribosomal protein S4X pseudogene 16 . . . . . . . . . . . RPS4XP17 . . . ribosomal protein S4X pseudogene 17 . . . . . . . . . . . RPS4XP18 . . . ribosomal protein S4X pseudogene 18 . . . . . . . . . . . RPS4XP19 . . . ribosomal protein S4X pseudogene 19 . . . . . . . . . . . RPS4XP20 . . . ribosomal protein S4X pseudogene 20 . . . . . . . . . . . RPS4XP21 . . . ribosomal protein S4X pseudogene 21 . . . . . . . . . . . RPS4XP22 . . . ribosomal protein S4X pseudogene 22 . . . . . . . . . . . RPS4XP23 . . . ribosomal protein S4X pseudogene 23 . . . . . . . . . . . RPS4Y1 0.502396329607095 0.425645678848258 0.0719579915446461 ribosomal protein S4, Y-linked 1 . . . lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;gum;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;whole body;larynx;bone;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;cerebellum cortex;hypothalamus;muscle;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; . 0.72771 . . . . . RPS4Y1P1 . . . ribosomal protein S4Y pseudogene 1 . . . . . . . . . . . RPS4Y2 0.00298794938170108 0.362854371246254 0.634157679372045 ribosomal protein S4, Y-linked 2 . . . stomach; . 0.07590 . . . 3.66805 0.13601 RPS5 0.903178121006896 0.0959979792442139 0.000823899748890414 ribosomal protein S5 . . . lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;germinal center;bladder;brain;tonsil;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;uterus;whole body;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; prostate;lung;heart;liver;tumor;thymus; 0.96285 0.31462 -0.251530012 35.42108988 6.77172 0.24975 RPS5P1 . . . ribosomal protein S5 pseudogene 1 . . . . . . . . . . . RPS5P2 . . . ribosomal protein S5 pseudogene 2 . . . . . . . . . . . RPS5P3 . . . ribosomal protein S5 pseudogene 3 . . . . . . . . . . . RPS5P4 . . . ribosomal protein S5 pseudogene 4 . . . . . . . . . . . RPS5P5 . . . ribosomal protein S5 pseudogene 5 . . . . . . . . . . . RPS5P6 . . . ribosomal protein S5 pseudogene 6 . . . . . . . . . . . RPS5P7 . . . ribosomal protein S5 pseudogene 7 . . . . . . . . . . . RPS5P8 . . . ribosomal protein S5 pseudogene 8 . . . . . . . . . . . RPS6 0.789114983445045 0.209530259471624 0.00135475708333129 ribosomal protein S6 FUNCTION: May play an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA.; . . . . . 0.58572 -0.339715008 30.06605331 7.16136 0.26861 RPS6KA1 0.725875552839744 0.274119520409998 4.92675025811703e-06 ribosomal protein S6 kinase A1 FUNCTION: Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin- derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the pre-initiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro- apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Mediates induction of hepatocyte prolifration by TGFA through phosphorylation of CEBPB (By similarity). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. {ECO:0000250|UniProtKB:P18653, ECO:0000250|UniProtKB:Q63531, ECO:0000269|PubMed:10679322, ECO:0000269|PubMed:11684016, ECO:0000269|PubMed:12213813, ECO:0000269|PubMed:15117958, ECO:0000269|PubMed:15342917, ECO:0000269|PubMed:16213824, ECO:0000269|PubMed:16223362, ECO:0000269|PubMed:16763566, ECO:0000269|PubMed:17360704, ECO:0000269|PubMed:18722121, ECO:0000269|PubMed:9430688}.; . . . . 0.80849 0.21975 -1.065444789 7.425100259 1576.33661 7.34660 RPS6KA2 0.0847008861629755 0.915295709994979 3.40384204577543e-06 ribosomal protein S6 kinase A2 FUNCTION: Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of transcription factors, regulates translation, and mediates cellular proliferation, survival, and differentiation. May function as tumor suppressor in epithelial ovarian cancer cells. {ECO:0000269|PubMed:16878154, ECO:0000269|PubMed:7623830}.; . TISSUE SPECIFICITY: Widely expressed with higher expression in lung, skeletal muscle, brain, uterus, ovary, thyroid and prostate. {ECO:0000269|PubMed:16878154, ECO:0000269|PubMed:7623830}.; ovary;salivary gland;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;cerebral cortex;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;head and neck;kidney;mammary gland;stomach; amygdala;superior cervical ganglion;spinal cord;prefrontal cortex;atrioventricular node;cingulate cortex;parietal lobe; 0.62299 0.12029 -1.015898037 8.144609578 29.0191 0.92777 RPS6KA2-AS1 . . . RPS6KA2 antisense RNA 1 . . . . . . . . . . . RPS6KA2-IT1 . . . RPS6KA2 intronic transcript 1 . . . . . . . . . . . RPS6KA3 0.999905699416843 9.43005495779085e-05 3.35793472027192e-11 ribosomal protein S6 kinase A3 FUNCTION: Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR- independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro- apoptotic proteins BAD and DAPK1 and suppressing their pro- apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3. Phosphorylates DAPK1. {ECO:0000269|PubMed:10436156, ECO:0000269|PubMed:16213824, ECO:0000269|PubMed:16223362, ECO:0000269|PubMed:17360704, ECO:0000269|PubMed:18722121, ECO:0000269|PubMed:8250835, ECO:0000269|PubMed:9770464}.; DISEASE: Coffin-Lowry syndrome (CLS) [MIM:303600]: A X-linked mental retardation associated with facial and digital dysmorphisms, progressive skeletal malformations, growth retardation, hearing deficit and paroxysmal movement disorders. {ECO:0000269|PubMed:10094187, ECO:0000269|PubMed:10528858, ECO:0000269|PubMed:14986828, ECO:0000269|PubMed:15214012, ECO:0000269|PubMed:8955270, ECO:0000269|PubMed:9837815}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mental retardation, X-linked 19 (MRX19) [MIM:300844]: A non-syndromic form of mild to moderate mental retardation. Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. In contrast to syndromic or specific X-linked mental retardation which also present with associated physical, neurological and/or psychiatric manifestations, intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation. {ECO:0000269|PubMed:10319851, ECO:0000269|PubMed:17100996}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in many tissues, highest levels in skeletal muscle.; . . 0.72327 0.64633 0.393270925 76.04977589 48.24612 1.35290 RPS6KA4 0.99947453973056 0.000525459823144884 4.46295442535628e-10 ribosomal protein S6 kinase A4 FUNCTION: Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factor RELA, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide- stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors. {ECO:0000269|PubMed:11035004, ECO:0000269|PubMed:12773393, ECO:0000269|PubMed:9792677}.; . . unclassifiable (Anatomical System);ovary;cartilage;heart;colon;skin;uterus;pancreas;prostate;whole body;lung;frontal lobe;endometrium;oesophagus;bone;thyroid;placenta;testis;spleen;cervix;kidney;brain;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;cingulate cortex;cerebellum; 0.47751 0.20620 -0.312207497 32.05944798 250.28243 3.40765 RPS6KA5 0.999801806584297 0.00019819337421089 4.14921205138138e-11 ribosomal protein S6 kinase A5 FUNCTION: Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factors RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF and upon glucocorticoid, associates in the cytoplasm with the glucocorticoid receptor NR3C1 and contributes to RELA inhibition and repression of inflammatory gene expression. In skeletal myoblasts is required for phosphorylation of RELA at 'Ser-276' during oxidative stress. In erythropoietin-stimulated cells, is necessary for the 'Ser-727' phosphorylation of STAT3 and regulation of its transcriptional potential. Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby regulates its ability to stimulate transcription, which may be important during development and breast tumor formation. Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto- oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro- inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti- inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors. Plays a role in neuronal cell death by mediating the downstream effects of excitotoxic injury. {ECO:0000269|PubMed:11909979, ECO:0000269|PubMed:12569367, ECO:0000269|PubMed:12628924, ECO:0000269|PubMed:12763138, ECO:0000269|PubMed:12773393, ECO:0000269|PubMed:15010469, ECO:0000269|PubMed:18511904, ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9873047}.; . TISSUE SPECIFICITY: Widely expressed with high levels in heart, brain and placenta. Less abundant in lung, kidney and liver. {ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9873047}.; ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;prostate;whole body;cochlea;endometrium;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);hypothalamus;blood;bile duct;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;olfactory bulb;placenta;prefrontal cortex;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.66327 0.31031 -0.178111357 40.44585987 117.20806 2.35411 RPS6KA6 0.744166833872825 0.255813312733482 1.98533936921947e-05 ribosomal protein S6 kinase A6 FUNCTION: Constitutively active serine/threonine-protein kinase that exhibits growth-factor-independent kinase activity and that may participate in p53/TP53-dependent cell growth arrest signaling and play an inhibitory role during embryogenesis. {ECO:0000269|PubMed:15042092, ECO:0000269|PubMed:15632195}.; . . unclassifiable (Anatomical System);optic nerve;macula lutea;liver;spleen;fovea centralis;choroid;lens;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.20172 0.16479 -0.093566408 46.7386176 450.65317 4.40985 RPS6KB1 0.998223240008685 0.00177675823231944 1.75899566191984e-09 ribosomal protein S6 kinase B1 FUNCTION: Serine/threonine-protein kinase that acts downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression. Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD. Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex. Upon mitogenic stimulation, phosphorylation by the mammalian target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation. The active form then phosphorylates and activates several substrates in the pre-initiation complex, including the EIF2B complex and the cap-binding complex component EIF4B. Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis. Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR. In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2. Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling. Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function. Phosphorylates mitochondrial URI1 leading to dissociation of a URI1-PPP1CC complex. The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative feedback mechanism for the RPS6KB1 anti- apoptotic function. Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1. In cells lacking functional TSC1- 2 complex, constitutively phosphorylates and inhibits GSK3B. May be involved in cytoskeletal rearrangement through binding to neurabin. Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR. {ECO:0000269|PubMed:11500364, ECO:0000269|PubMed:12801526, ECO:0000269|PubMed:14673156, ECO:0000269|PubMed:15071500, ECO:0000269|PubMed:15341740, ECO:0000269|PubMed:16286006, ECO:0000269|PubMed:17052453, ECO:0000269|PubMed:17053147, ECO:0000269|PubMed:17936702, ECO:0000269|PubMed:18952604, ECO:0000269|PubMed:19085255, ECO:0000269|PubMed:19720745, ECO:0000269|PubMed:19935711, ECO:0000269|PubMed:19995915, ECO:0000269|PubMed:23429703}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9804755}.; medulla oblongata;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;spinal cord;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.62174 0.62277 -0.494039303 22.09247464 6.4258 0.24035 RPS6KB2 3.2061006422526e-11 0.0824516940697308 0.917548305898208 ribosomal protein S6 kinase B2 FUNCTION: Phosphorylates specifically ribosomal protein S6.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;liver;amnion;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;liver;skeletal muscle; 0.24011 0.28559 -0.310388054 32.14791224 3788.54325 12.06748 RPS6KB3 . . . ribosomal protein S6 kinase B3 . . . . . . . . . . . RPS6KC1 0.0204400966055895 0.979528985722263 3.09176721477707e-05 ribosomal protein S6 kinase C1 FUNCTION: May be involved in transmitting sphingosine-1 phosphate (SPP)-mediated signaling into the cell.; . TISSUE SPECIFICITY: Highly expressed in testis, skeletal muscle, brain, heart, placenta, kidney and liver and weakly expressed in thymus, small intestine, lung and colon. {ECO:0000269|PubMed:12077123}.; . . 0.12108 0.12186 0.450099045 78.01958009 426.82545 4.31586 RPS6KL1 0.000674280963305879 0.978871199698235 0.0204545193384591 ribosomal protein S6 kinase like 1 . . . unclassifiable (Anatomical System);myocardium;heart;ovary;islets of Langerhans;hypothalamus;colon;blood;skeletal muscle;lung;frontal lobe;larynx;liver;testis;cervix;head and neck;spleen;brain;stomach; subthalamic nucleus;superior cervical ganglion;prefrontal cortex;globus pallidus;caudate nucleus;atrioventricular node;trigeminal ganglion; 0.10194 . 0.04598748 57.47817882 4892.98014 14.22680 RPS6P1 . . . ribosomal protein S6 pseudogene 1 . . . . . . . . . . . RPS6P2 . . . ribosomal protein S6 pseudogene 2 . . . . . . . . . . . RPS6P3 . . . ribosomal protein S6 pseudogene 3 . . . . . . . . . . . RPS6P4 . . . ribosomal protein S6 pseudogene 4 . . . . . . . . . . . RPS6P5 . . . ribosomal protein S6 pseudogene 5 . . . . . . . . . . . RPS6P7 . . . ribosomal protein S6 pseudogene 7 . . . . . . . . . . . RPS6P8 . . . ribosomal protein S6 pseudogene 8 . . . . . . . . . . . RPS6P9 . . . ribosomal protein S6 pseudogene 9 . . . . . . . . . . . RPS6P10 . . . ribosomal protein S6 pseudogene 10 . . . . . . . . . . . RPS6P11 . . . ribosomal protein S6 pseudogene 11 . . . . . . . . . . . RPS6P12 . . . ribosomal protein S6 pseudogene 12 . . . . . . . . . . . RPS6P13 . . . ribosomal protein S6 pseudogene 13 . . . . . . . . . . . RPS6P14 . . . ribosomal protein S6 pseudogene 14 . . . . . . . . . . . RPS6P15 . . . ribosomal protein S6 pseudogene 15 . . . . . . . . . . . RPS6P16 . . . ribosomal protein S6 pseudogene 16 . . . . . . . . . . . RPS6P17 . . . ribosomal protein S6 pseudogene 17 . . . . . . . . . . . RPS6P18 . . . ribosomal protein S6 pseudogene 18 . . . . . . . . . . . RPS6P19 . . . ribosomal protein S6 pseudogene 19 . . . . . . . . . . . RPS6P20 . . . ribosomal protein S6 pseudogene 20 . . . . . . . . . . . RPS6P21 . . . ribosomal protein S6 pseudogene 21 . . . . . . . . . . . RPS6P22 . . . ribosomal protein S6 pseudogene 22 . . . . . . . . . . . RPS6P23 . . . ribosomal protein S6 pseudogene 23 . . . . . . . . . . . RPS6P24 . . . ribosomal protein S6 pseudogene 24 . . . . . . . . . . . RPS6P25 . . . ribosomal protein S6 pseudogene 25 . . . . . . . . . . . RPS6P26 . . . ribosomal protein S6 pseudogene 26 . . . . . . . . . . . RPS7 0.907087093194304 0.0921713412341155 0.000741565571580941 ribosomal protein S7 FUNCTION: Required for rRNA maturation. {ECO:0000269|PubMed:19061985}.; DISEASE: Diamond-Blackfan anemia 8 (DBA8) [MIM:612563]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. {ECO:0000269|PubMed:19061985}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; trigeminal ganglion; 0.96899 0.29199 -0.09720619 46.20193442 31.08852 0.98200 RPS7P1 . . . ribosomal protein S7 pseudogene 1 . . . . . . . . . . . RPS7P2 . . . ribosomal protein S7 pseudogene 2 . . . . . . . . . . . RPS7P3 . . . ribosomal protein S7 pseudogene 3 . . . . . . . . . . . RPS7P4 . . . ribosomal protein S7 pseudogene 4 . . . . . . . . . . . RPS7P5 . . . ribosomal protein S7 pseudogene 5 . . . . . . . . . . . RPS7P6 . . . ribosomal protein S7 pseudogene 6 . . . . . . . . . . . RPS7P7 . . . ribosomal protein S7 pseudogene 7 . . . . . . . . . . . RPS7P8 . . . ribosomal protein S7 pseudogene 8 . . . . . . . . . . . RPS7P9 . . . ribosomal protein S7 pseudogene 9 . . . . . . . . . . . RPS7P10 . . . ribosomal protein S7 pseudogene 10 . . . . . . . . . . . RPS7P11 . . . ribosomal protein S7 pseudogene 11 . . . . . . . . . . . RPS7P12 . . . ribosomal protein S7 pseudogene 12 . . . . . . . . . . . RPS7P13 . . . ribosomal protein S7 pseudogene 13 . . . . . . . . . . . RPS7P14 . . . ribosomal protein S7 pseudogene 14 . . . . . . . . . . . RPS7P15 . . . ribosomal protein S7 pseudogene 15 . . . . . . . . . . . RPS8 0.965122842277358 0.0348138433892815 6.3314333361026e-05 ribosomal protein S8 . . . . . 0.26192 0.21177 -0.053113545 49.38664779 1.20885 0.03679 RPS8P1 . . . ribosomal protein S8 pseudogene 1 . . . . . . . . . . . RPS8P3 . . . ribosomal protein S8 pseudogene 3 . . . . . . . . . . . RPS8P4 . . . ribosomal protein S8 pseudogene 4 . . . . . . . . . . . RPS8P5 . . . ribosomal protein S8 pseudogene 5 . . . . . . . . . . . RPS8P6 . . . ribosomal protein S8 pseudogene 6 . . . . . . . . . . . RPS8P7 . . . ribosomal protein S8 pseudogene 7 . . . . . . . . . . . RPS8P8 . . . ribosomal protein S8 pseudogene 8 . . . . . . . . . . . RPS8P9 . . . ribosomal protein S8 pseudogene 9 . . . . . . . . . . . RPS8P10 . . . ribosomal protein S8 pseudogene 10 . . . . . . . . . . . RPS9 0.787131549437011 0.206391470445899 0.00647698011709077 ribosomal protein S9 . . . lymphoreticular;myocardium;medulla oblongata;ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;blood;lens;bile duct;pancreas;lung;adrenal gland;trabecular meshwork;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;kidney;mammary gland;stomach;thymus; . 0.93942 0.23984 -0.119252484 44.53880632 3.58338 0.13005 RPS9P1 . . . ribosomal protein S9 pseudogene 1 . . . . . . . . . . . RPS9P2 . . . ribosomal protein S9 pseudogene 2 . . . . . . . . . . . RPS9P3 . . . ribosomal protein S9 pseudogene 3 . . . . . . . . . . . RPS9P4 . . . ribosomal protein S9 pseudogene 4 . . . . . . . . . . . RPS10 0.946462997504496 0.0533528015531142 0.000184200942390105 ribosomal protein S10 FUNCTION: Component of the 40S ribosomal subunit.; DISEASE: Diamond-Blackfan anemia 9 (DBA9) [MIM:613308]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. {ECO:0000269|PubMed:20116044}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.24713 0.10516 -0.141298762 42.87567823 6.46651 0.24059 RPS10-NUDT3 . . . RPS10-NUDT3 readthrough . . . . . . . . . 6.67566 0.24622 RPS10P1 . . . ribosomal protein S10 pseudogene 1 . . . . . . . . . . . RPS10P2 . . . ribosomal protein S10 pseudogene 2 . . . . . . . . . . . RPS10P3 . . . ribosomal protein S10 pseudogene 3 . . . . . . . . . . . RPS10P4 . . . ribosomal protein S10 pseudogene 4 . . . . . . . . . . . RPS10P5 . . . ribosomal protein S10 pseudogene 5 . . . . . 0.25407 0.07578 . . . . RPS10P6 . . . ribosomal protein S10 pseudogene 6 . . . . . . . . . . . RPS10P7 . . . ribosomal protein S10 pseudogene 7 . . . . . . . . . . . RPS10P8 . . . ribosomal protein S10 pseudogene 8 . . . . . . . . . . . RPS10P9 . . . ribosomal protein S10 pseudogene 9 . . . . . . . . . . . RPS10P10 . . . ribosomal protein S10 pseudogene 10 . . . . . . . . . . . RPS10P11 . . . ribosomal protein S10 pseudogene 11 . . . . . . . . . . . RPS10P12 . . . ribosomal protein S10 pseudogene 12 . . . . . . . . . . . RPS10P13 . . . ribosomal protein S10 pseudogene 13 . . . . . . . . . . . RPS10P14 . . . ribosomal protein S10 pseudogene 14 . . . . . . . . . . . RPS10P15 . . . ribosomal protein S10 pseudogene 15 . . . . . . . . . . . RPS10P16 . . . ribosomal protein S10 pseudogene 16 . . . . . . . . . . . RPS10P17 . . . ribosomal protein S10 pseudogene 17 . . . . . . . . . . . RPS10P18 . . . ribosomal protein S10 pseudogene 18 . . . . . . . . . . . RPS10P19 . . . ribosomal protein S10 pseudogene 19 . . . . . . . . . . . RPS10P20 . . . ribosomal protein S10 pseudogene 20 . . . . . . . . . . . RPS10P21 . . . ribosomal protein S10 pseudogene 21 . . . . . . . . . . . RPS10P22 . . . ribosomal protein S10 pseudogene 22 . . . . . . . . . . . RPS10P23 . . . ribosomal protein S10 pseudogene 23 . . . . . . . . . . . RPS10P24 . . . ribosomal protein S10 pseudogene 24 . . . . . . . . . . . RPS10P25 . . . ribosomal protein S10 pseudogene 25 . . . . . . . . . . . RPS10P26 . . . ribosomal protein S10 pseudogene 26 . . . . . . . . . . . RPS10P27 . . . ribosomal protein S10 pseudogene 27 . . . . . . . . . . . RPS10P28 . . . ribosomal protein S10 pseudogene 28 . . . . . . . . . . . RPS10P29 . . . ribosomal protein S10 pseudogene 29 . . . . . . . . . . . RPS10P30 . . . ribosomal protein S10 pseudogene 30 . . . . . . . . . . . RPS10P31 . . . ribosomal protein S10 pseudogene 31 . . . . . . . . . . . RPS11 0.913344861476602 0.0860343092990953 0.000620829224303101 ribosomal protein S11 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;breast;bile duct;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;head and neck;cervix;kidney;mammary gland;stomach; atrioventricular node;fetal thyroid;skin; 0.97553 0.18619 -0.163345027 41.24793583 1.21425 0.03859 RPS11P1 . . . ribosomal protein S11 pseudogene 1 . . . . . . . . . . . RPS11P2 . . . ribosomal protein S11 pseudogene 2 . . . . . . . . . . . RPS11P3 . . . ribosomal protein S11 pseudogene 3 . . . . . . . . . . . RPS11P4 . . . ribosomal protein S11 pseudogene 4 . . . . . . . . . . . RPS11P5 . . . ribosomal protein S11 pseudogene 5 . . . . . . . . . . . RPS11P6 . . . ribosomal protein S11 pseudogene 6 . . . . . . . . . . . RPS11P7 . . . ribosomal protein S11 pseudogene 7 . . . . . . . . . . . RPS12 0.827435141809626 0.168866927813676 0.00369793037669759 ribosomal protein S12 . . . lymphoreticular;ovary;salivary gland;intestine;colon;vein;skin;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;bone;thyroid;iris;pituitary gland;testis;dura mater;brain;bladder;tonsil;unclassifiable (Anatomical System);meninges;trophoblast;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;breast;bile duct;pancreas;pia mater;lung;cornea;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; . 0.26171 0.19444 0.035072054 56.2514744 9.87588 0.36197 RPS12P1 . . . ribosomal protein S12 pseudogene 1 . . . . . . . . . . . RPS12P2 . . . ribosomal protein S12 pseudogene 2 . . . . . . . . . . . RPS12P3 . . . ribosomal protein S12 pseudogene 3 . . . . . . . . . . . RPS12P4 . . . ribosomal protein S12 pseudogene 4 . . . . . . . . . . . RPS12P5 . . . ribosomal protein S12 pseudogene 5 . . . . . . . . . . . RPS12P6 . . . ribosomal protein S12 pseudogene 6 . . . . . . . . . . . RPS12P7 . . . ribosomal protein S12 pseudogene 7 . . . . . . . . . . . RPS12P8 . . . ribosomal protein S12 pseudogene 8 . . . . . . . . . . . RPS12P9 . . . ribosomal protein S12 pseudogene 9 . . . . . . . . . . . RPS12P10 . . . ribosomal protein S12 pseudogene 10 . . . . . . . . . . . RPS12P11 . . . ribosomal protein S12 pseudogene 11 . . . . . . . . . . . RPS12P12 . . . ribosomal protein S12 pseudogene 12 . . . . . . . . . . . RPS12P13 . . . ribosomal protein S12 pseudogene 13 . . . . . . . . . . . RPS12P14 . . . ribosomal protein S12 pseudogene 14 . . . . . . . . . . . RPS12P15 . . . ribosomal protein S12 pseudogene 15 . . . . . . . . . . . RPS12P16 . . . ribosomal protein S12 pseudogene 16 . . . . . . . . . . . RPS12P17 . . . ribosomal protein S12 pseudogene 17 . . . . . . . . . . . RPS12P18 . . . ribosomal protein S12 pseudogene 18 . . . . . . . . . . . RPS12P20 . . . ribosomal protein S12 pseudogene 20 . . . . . . . . . . . RPS12P21 . . . ribosomal protein S12 pseudogene 21 . . . . . . . . . . . RPS12P22 . . . ribosomal protein S12 pseudogene 22 . . . . . . . . . . . RPS12P23 . . . ribosomal protein S12 pseudogene 23 . . . . . . . . . . . RPS12P24 . . . ribosomal protein S12 pseudogene 24 . . . . . . . . . . . RPS12P25 . . . ribosomal protein S12 pseudogene 25 . . . . . . . . . . . RPS12P26 . . . ribosomal protein S12 pseudogene 26 . . . . . . . . . . . RPS12P27 . . . ribosomal protein S12 pseudogene 27 . . . . . . . . . . . RPS12P28 . . . ribosomal protein S12 pseudogene 28 . . . . . . . . . . . RPS12P29 . . . ribosomal protein S12 pseudogene 29 . . . . . . . . . . . RPS12P30 . . . ribosomal protein S12 pseudogene 30 . . . . . . . . . . . RPS12P31 . . . ribosomal protein S12 pseudogene 31 . . . . . . . . . . . RPS12P32 . . . ribosomal protein S12 pseudogene 32 . . . . . . . . . . . RPS13 0.960207216837053 0.0397049307559158 8.78524070309978e-05 ribosomal protein S13 . . . myocardium;lymphoreticular;ovary;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;gum;thyroid;bladder;brain;gall bladder;heart;cartilage;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach;aorta; . . 0.27035 -0.031067188 51.03798066 1.18726 0.03433 RPS13P1 . . . ribosomal protein S13 pseudogene 1 . . . . . . . . . . . RPS13P2 . . . ribosomal protein S13 pseudogene 2 . . . . . . . . . . . RPS13P3 . . . ribosomal protein S13 pseudogene 3 . . . . . . . . . . . RPS13P4 . . . ribosomal protein S13 pseudogene 4 . . . . . . . . . . . RPS13P5 . . . ribosomal protein S13 pseudogene 5 . . . . . . . . . . . RPS13P6 . . . ribosomal protein S13 pseudogene 6 . . . . . . . . . . . RPS13P7 . . . ribosomal protein S13 pseudogene 7 . . . . . . . . . . . RPS13P8 . . . ribosomal protein S13 pseudogene 8 . . . . . . . . . . . RPS14 0.864815342185179 0.133236140535401 0.00194851727942047 ribosomal protein S14 . . . ovary;umbilical cord;skin;retina;prostate;ganglion;frontal lobe;endometrium;gum;bladder;brain;gall bladder;tonsil;heart;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;synovium;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;heart;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.90649 0.35430 -0.119252484 44.53880632 . . RPS14P1 . . . ribosomal protein S14 pseudogene 1 . . . . . . . . . . . RPS14P2 . . . ribosomal protein S14 pseudogene 2 . . . . . . . . . . . RPS14P3 . . . ribosomal protein S14 pseudogene 3 . . . . . . . . . . . RPS14P4 . . . ribosomal protein S14 pseudogene 4 . . . . . . . . . . . RPS14P5 . . . ribosomal protein S14 pseudogene 5 . . . . . . . . . . . RPS14P6 . . . ribosomal protein S14 pseudogene 6 . . . . . . . . . . . RPS14P7 . . . ribosomal protein S14 pseudogene 7 . . . . . . . . . . . RPS14P8 . . . ribosomal protein S14 pseudogene 8 . . . . . . . . . . . RPS14P9 . . . ribosomal protein S14 pseudogene 9 . . . . . . . . . . . RPS14P10 . . . ribosomal protein S14 pseudogene 10 . . . . . . . . . . . RPS15 0.697325164941198 0.28566264825412 0.0170121868046817 ribosomal protein S15 . . . myocardium;ovary;salivary gland;intestine;colon;vein;skin;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;larynx;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;trabecular meshwork;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;cerebellum; . 0.16134 0.18470 0.013025609 54.62962963 1.0599 0.02695 RPS15A 0.833355704516176 0.163272414574529 0.00337188090929453 ribosomal protein S15a . . . myocardium;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;oesophagus;larynx;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;stomach; . 0.37339 0.23021 0.057118534 57.99716914 1.2844 0.04554 RPS15AP1 . . . ribosomal protein S15a pseudogene 1 . . . . . . . . . . . RPS15AP2 . . . ribosomal protein S15a pseudogene 2 . . . . . . . . . . . RPS15AP3 . . . ribosomal protein S15a pseudogene 3 . . . . . . . . . . . RPS15AP4 . . . ribosomal protein S15a pseudogene 4 . . . . . . . . . . . RPS15AP5 . . . ribosomal protein S15a pseudogene 5 . . . . . . . . . . . RPS15AP6 . . . ribosomal protein S15a pseudogene 6 . . . . . . . . . . . RPS15AP7 . . . ribosomal protein S15a pseudogene 7 . . . . . . . . . . . RPS15AP8 . . . ribosomal protein S15a pseudogene 8 . . . . . . . . . . . RPS15AP9 . . . ribosomal protein S15a pseudogene 9 . . . . . . . . . . . RPS15AP10 . . . ribosomal protein S15a pseudogene 10 . . . . . . . . . . . RPS15AP11 . . . ribosomal protein S15a pseudogene 11 . . . . . . . . . . . RPS15AP12 . . . ribosomal protein S15a pseudogene 12 . . . . . . . . . . . RPS15AP13 . . . ribosomal protein S15a pseudogene 13 . . . . . . . . . . . RPS15AP14 . . . ribosomal protein S15a pseudogene 14 . . . . . . . . . . . RPS15AP15 . . . ribosomal protein S15a pseudogene 15 . . . . . . . . . . . RPS15AP16 . . . ribosomal protein S15a pseudogene 16 . . . . . . . . . . . RPS15AP17 . . . ribosomal protein S15a pseudogene 17 . . . . . . . . . . . RPS15AP18 . . . ribosomal protein S15a pseudogene 18 . . . . . . . . . . . RPS15AP19 . . . ribosomal protein S15a pseudogene 19 . . . . . . . . . . . RPS15AP20 . . . ribosomal protein S15a pseudogene 20 . . . . . . . . . . . RPS15AP21 . . . ribosomal protein S15a pseudogene 21 . . . . . . . . . . . RPS15AP22 . . . ribosomal protein S15a pseudogene 22 . . . . . . . . . . . RPS15AP23 . . . ribosomal protein S15a pseudogene 23 . . . . . . . . . . . RPS15AP24 . . . ribosomal protein S15a pseudogene 24 . . . . . . . . . . . RPS15AP25 . . . ribosomal protein S15a pseudogene 25 . . . . . . . . . . . RPS15AP26 . . . ribosomal protein S15a pseudogene 26 . . . . . . . . . . . RPS15AP27 . . . ribosomal protein S15a pseudogene 27 . . . . . . . . . . . RPS15AP28 . . . ribosomal protein S15a pseudogene 28 . . . . . . . . . . . RPS15AP29 . . . ribosomal protein S15a pseudogene 29 . . . . . . . . . . . RPS15AP30 . . . ribosomal protein S15a pseudogene 30 . . . . . . . . . . . RPS15AP31 . . . ribosomal protein S15a pseudogene 31 . . . . . . . . . . . RPS15AP32 . . . ribosomal protein S15a pseudogene 32 . . . . . . . . . . . RPS15AP33 . . . ribosomal protein S15a pseudogene 33 . . . . . . . . . . . RPS15AP34 . . . ribosomal protein S15a pseudogene 34 . . . . . . . . . . . RPS15AP35 . . . ribosomal protein S15a pseudogene 35 . . . . . . . . . . . RPS15AP36 . . . ribosomal protein S15a pseudogene 36 . . . . . . . . . . . RPS15AP37 . . . ribosomal protein S15a pseudogene 37 . . . . . . . . . . . RPS15AP38 . . . ribosomal protein S15a pseudogene 38 . . . . . . . . . . . RPS15AP39 . . . ribosomal protein S15a pseudogene 39 . . . . . . . . . . . RPS15AP40 . . . ribosomal protein S15a pseudogene 40 . . . . . . . . . . . RPS15P1 . . . ribosomal protein S15 pseudogene 1 . . . . . . . . . . . RPS15P2 . . . ribosomal protein S15 pseudogene 2 . . . . . . . . . . . RPS15P3 . . . ribosomal protein S15 pseudogene 3 . . . . . . . . . . . RPS15P4 . . . ribosomal protein S15 pseudogene 4 . . . . . . . . . . . RPS15P5 . . . ribosomal protein S15 pseudogene 5 . . . . . . . . . . . RPS15P6 . . . ribosomal protein S15 pseudogene 6 . . . . . . . . . . . RPS15P7 . . . ribosomal protein S15 pseudogene 7 . . . . . . . . . . . RPS15P8 . . . ribosomal protein S15 pseudogene 8 . . . . . . . . . . . RPS15P9 . . . ribosomal protein S15 pseudogene 9 . . . . . . . . . . . RPS16 0.28185910292269 0.6957776224598 0.0223632746175103 ribosomal protein S16 . . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;frontal lobe;endometrium;oesophagus;bone;pituitary gland;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;hypothalamus;muscle;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; lung;ovary;heart;liver;tumor;white blood cells;skeletal muscle;thymus; 0.87031 . -0.185391282 39.67916962 12.72637 0.46330 RPS16P1 . . . ribosomal protein S16 pseudogene 1 . . . . . . . . . . . RPS16P2 . . . ribosomal protein S16 pseudogene 2 . . . . . . . . . . . RPS16P3 . . . ribosomal protein S16 pseudogene 3 . . . . . . . . . . . RPS16P4 . . . ribosomal protein S16 pseudogene 4 . . . . . . . . . . . RPS16P5 . . . ribosomal protein S16 pseudogene 5 . . . . . . . . . . . RPS16P6 . . . ribosomal protein S16 pseudogene 6 . . . . . . . . . . . RPS16P7 . . . ribosomal protein S16 pseudogene 7 . . . . . . . . . . . RPS16P8 . . . ribosomal protein S16 pseudogene 8 . . . . . . . . . . . RPS16P9 . . . ribosomal protein S16 pseudogene 9 . . . . . . . . . . . RPS16P10 . . . ribosomal protein S16 pseudogene 10 . . . . . . . . . . . RPS17 . . . ribosomal protein S17 . DISEASE: Diamond-Blackfan anemia 4 (DBA4) [MIM:612527]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of developing leukemia. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. {ECO:0000269|PubMed:17647292, ECO:0000269|PubMed:19061985}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;intestine;colon;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;oesophagus;larynx;gum;bone;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;trabecular meshwork;placenta;visual apparatus;alveolus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; . 0.85268 0.21597 . . . . RPS17P1 . . . ribosomal protein S17 pseudogene 1 . . . . . . . . . . . RPS17P2 . . . ribosomal protein S17 pseudogene 2 . . . lymphoreticular;ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;pituitary gland;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;muscle;blood;lens;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach; . . . . . . . RPS17P3 . . . ribosomal protein S17 pseudogene 3 . . . . . . . . . . . RPS17P5 . . . ribosomal protein S17 pseudogene 5 . . . . . . . . . . . RPS17P6 . . . ribosomal protein S17 pseudogene 6 . . . . . . . . . . . RPS17P7 . . . ribosomal protein S17 pseudogene 7 . . . . . . . . . . . RPS17P8 . . . ribosomal protein S17 pseudogene 8 . . . . . . . . . . . RPS17P9 . . . ribosomal protein S17 pseudogene 9 . . . . . . . . . . . RPS17P10 . . . ribosomal protein S17 pseudogene 10 . . . . . . . . . . . RPS17P11 . . . ribosomal protein S17 pseudogene 11 . . . . . . . . . . . RPS17P12 . . . ribosomal protein S17 pseudogene 12 . . . . . . . . . . . RPS17P13 . . . ribosomal protein S17 pseudogene 13 . . . . . . . . . . . RPS17P14 . . . ribosomal protein S17 pseudogene 14 . . . . . . . . . . . RPS17P15 . . . ribosomal protein S17 pseudogene 15 . . . . . . . . . . . RPS17P16 . . . ribosomal protein S17 pseudogene 16 . . . . . . . . . . . RPS17P17 . . . ribosomal protein S17 pseudogene 17 . . . . . . . . . . . RPS18 0.962013320594563 0.0379084085571287 7.82708483082454e-05 ribosomal protein S18 FUNCTION: Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA. {ECO:0000250}.; . . . . 0.21960 . 0.057118534 57.99716914 1.20345 0.03567 RPS18P1 . . . ribosomal protein S18 pseudogene 1 . . . . . . . . . . . RPS18P2 . . . ribosomal protein S18 pseudogene 2 . . . . . . . . . . . RPS18P3 . . . ribosomal protein S18 pseudogene 3 . . . . . . . . . . . RPS18P4 . . . ribosomal protein S18 pseudogene 4 . . . . . . . . . . . RPS18P5 . . . ribosomal protein S18 pseudogene 5 . . . . . . . . . . . RPS18P6 . . . ribosomal protein S18 pseudogene 6 . . . . . . . . . . . RPS18P7 . . . ribosomal protein S18 pseudogene 7 . . . . . . . . . . . RPS18P8 . . . ribosomal protein S18 pseudogene 8 . . . . . . . . . . . RPS18P9 . . . ribosomal protein S18 pseudogene 9 . . . . . . . . . . . RPS18P10 . . . ribosomal protein S18 pseudogene 10 . . . . . . . . . . . RPS18P11 . . . ribosomal protein S18 pseudogene 11 . . . . . . . . . . . RPS18P12 . . . ribosomal protein S18 pseudogene 12 . . . . . . . . . . . RPS18P13 . . . ribosomal protein S18 pseudogene 13 . . . . . . . . . . . RPS18P14 . . . ribosomal protein S18 pseudogene 14 . . . . . . . . . . . RPS19 0.923992800087249 0.0755621151512098 0.000445084761540693 ribosomal protein S19 FUNCTION: Required for pre-rRNA processing and maturation of 40S ribosomal subunits. {ECO:0000269|PubMed:16990592}.; . TISSUE SPECIFICITY: Higher level expression is seen in the colon carcinoma tissue than normal colon tissue.; lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;bladder;brain;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;synovium;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus;cerebellum; prostate;uterus corpus;smooth muscle;lung;heart;tongue;liver;tumor;white blood cells; 0.67551 0.40044 -0.207437529 38.2814343 1.23583 0.04285 RPS19BP1 0.00589798441146116 0.729363733720814 0.264738281867725 ribosomal protein S19 binding protein 1 FUNCTION: Direct regulator of SIRT1. Enhances SIRT1-mediated deacetylation of p53/TP53, thereby participating in inhibition of p53/TP53-mediated transcriptional activity. {ECO:0000269|PubMed:17964266}.; . TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:17964266}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;adrenal gland;trabecular meshwork;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; whole brain;prostate;thyroid;liver; 0.12648 0.10910 0.21326276 67.71644256 26.23481 0.85011 RPS19P1 . . . ribosomal protein S19 pseudogene 1 . . . . . . . . . . . RPS19P2 . . . ribosomal protein S19 pseudogene 2 . . . . . . . . . . . RPS19P3 . . . ribosomal protein S19 pseudogene 3 . . . . . . . . . . . RPS19P4 . . . ribosomal protein S19 pseudogene 4 . . . . . . . . . . . RPS19P5 . . . ribosomal protein S19 pseudogene 5 . . . . . . . . . . . RPS19P6 . . . ribosomal protein S19 pseudogene 6 . . . . . . . . . . . RPS19P7 . . . ribosomal protein S19 pseudogene 7 . . . . . . . . . . . RPS20 0.686321059018356 0.309401177930167 0.00427776305147752 ribosomal protein S20 . . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;oesophagus;synovium;bone;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; testis - seminiferous tubule;ovary;testis;white blood cells;tonsil; 0.95484 . 0.21326276 67.71644256 29.08929 0.93025 RPS20P1 . . . ribosomal protein S20 pseudogene 1 . . . . . . . . . . . RPS20P2 . . . ribosomal protein S20 pseudogene 2 . . . . . . . . . . . RPS20P3 . . . ribosomal protein S20 pseudogene 3 . . . . . . . . . . . RPS20P4 . . . ribosomal protein S20 pseudogene 4 . . . . . . . . . . . RPS20P5 . . . ribosomal protein S20 pseudogene 5 . . . . . . . . . . . RPS20P6 . . . ribosomal protein S20 pseudogene 6 . . . . . . . . . . . RPS20P7 . . . ribosomal protein S20 pseudogene 7 . . . . . . . . . . . RPS20P8 . . . ribosomal protein S20 pseudogene 8 . . . . . . . . . . . RPS20P9 . . . ribosomal protein S20 pseudogene 9 . . . . . . . . . . . RPS20P10 . . . ribosomal protein S20 pseudogene 10 . . . . . . . . . . . RPS20P11 . . . ribosomal protein S20 pseudogene 11 . . . . . . . . . . . RPS20P12 . . . ribosomal protein S20 pseudogene 12 . . . . . . . . . . . RPS20P13 . . . ribosomal protein S20 pseudogene 13 . . . . . . . . . . . RPS20P14 . . . ribosomal protein S20 pseudogene 14 . . . . . . . . . . . RPS20P15 . . . ribosomal protein S20 pseudogene 15 . . . . . . . . . . . RPS20P16 . . . ribosomal protein S20 pseudogene 16 . . . . . . . . . . . RPS20P17 . . . ribosomal protein S20 pseudogene 17 . . . . . . . . . . . RPS20P18 . . . ribosomal protein S20 pseudogene 18 . . . . . . . . . . . RPS20P19 . . . ribosomal protein S20 pseudogene 19 . . . . . . . . . . . RPS20P20 . . . ribosomal protein S20 pseudogene 20 . . . . . . . . . . . RPS20P21 . . . ribosomal protein S20 pseudogene 21 . . . . . . . . . . . RPS20P22 . . . ribosomal protein S20 pseudogene 22 . . . . . . . . . . . RPS20P23 . . . ribosomal protein S20 pseudogene 23 . . . . . . . . . . . RPS20P24 . . . ribosomal protein S20 pseudogene 24 . . . . . . . . . . . RPS20P25 . . . ribosomal protein S20 pseudogene 25 . . . . . . . . . . . RPS20P26 . . . ribosomal protein S20 pseudogene 26 . . . . . . . . . . . RPS20P27 . . . ribosomal protein S20 pseudogene 27 . . . . . . . . . . . RPS20P28 . . . ribosomal protein S20 pseudogene 28 . . . . . . . . . . . RPS20P29 . . . ribosomal protein S20 pseudogene 29 . . . . . . . . . . . RPS20P30 . . . ribosomal protein S20 pseudogene 30 . . . . . . . . . . . RPS20P31 . . . ribosomal protein S20 pseudogene 31 . . . . . . . . . . . RPS20P32 . . . ribosomal protein S20 pseudogene 32 . . . . . . . . . . . RPS20P33 . . . ribosomal protein S20 pseudogene 33 . . . . . . . . . . . RPS20P34 . . . ribosomal protein S20 pseudogene 34 . . . . . . . . . . . RPS20P35 . . . ribosomal protein S20 pseudogene 35 . . . . . . . . . . . RPS21 0.46553481920164 0.509315455914578 0.0251497248837817 ribosomal protein S21 . . . lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;pia mater;lung;cornea;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta; prostate;lung;tumor;white blood cells;atrioventricular node; 0.66173 0.10783 0.013025609 54.62962963 236.5999 3.32140 RPS21P1 . . . ribosomal protein S21 pseudogene 1 . . . . . . . . . . . RPS21P2 . . . ribosomal protein S21 pseudogene 2 . . . . . . . . . . . RPS21P3 . . . ribosomal protein S21 pseudogene 3 . . . . . . . . . . . RPS21P4 . . . ribosomal protein S21 pseudogene 4 . . . . . . . . . . . RPS21P5 . . . ribosomal protein S21 pseudogene 5 . . . . . . . . . . . RPS21P6 . . . ribosomal protein S21 pseudogene 6 . . . . . . . . . . . RPS21P7 . . . ribosomal protein S21 pseudogene 7 . . . . . . . . . . . RPS21P8 . . . ribosomal protein S21 pseudogene 8 . . . . . . . . . . . RPS23 0.878578937888168 0.119946376737474 0.00147468537435857 ribosomal protein S23 . . . myocardium;ovary;umbilical cord;foreskin;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;bladder;brain;tonsil;heart;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;vein;uterus;oesophagus;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;epidermis;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; . 0.98321 0.27035 -0.009020804 52.8544468 0.90178 0.01936 RPS23P1 . . . ribosomal protein S23 pseudogene 1 . . . . . . . . . . . RPS23P2 . . . ribosomal protein S23 pseudogene 2 . . . . . . . . . . . RPS23P3 . . . ribosomal protein S23 pseudogene 3 . . . . . . . . . . . RPS23P4 . . . ribosomal protein S23 pseudogene 4 . . . . . . . . . . . RPS23P5 . . . ribosomal protein S23 pseudogene 5 . . . . . . . . . . . RPS23P6 . . . ribosomal protein S23 pseudogene 6 . . . . . . . . . . . RPS23P7 . . . ribosomal protein S23 pseudogene 7 . . . . . . . . . . . RPS23P8 . . . ribosomal protein S23 pseudogene 8 . . . . . . . . . . . RPS23P9 . . . ribosomal protein S23 pseudogene 9 . . . . . . . . . . . RPS23P10 . . . ribosomal protein S23 pseudogene 10 . . . . . . . . . . . RPS24 0.852844134621405 0.144724278702875 0.00243158667571974 ribosomal protein S24 FUNCTION: Required for processing of pre-rRNA and maturation of 40S ribosomal subunits. {ECO:0000269|PubMed:18230666}.; . TISSUE SPECIFICITY: Mature tissues, such as adult brain, skeletal muscle, heart, and kidney, express low levels, whereas tissues and organs with significant populations of proliferating cells, such as fetal brain, placenta, bone marrow, and various glandular organs, contain significantly higher levels. {ECO:0000269|PubMed:17186470}.; myocardium;lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;gall bladder;heart;tongue;urinary;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;vein;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;amnion;head and neck;kidney;stomach;aorta;cerebellum; . 0.95319 0.20297 0.03689118 56.64071715 5.61455 0.21042 RPS24P1 . . . ribosomal protein S24 pseudogene 1 . . . . . . . . . . . RPS24P2 . . . ribosomal protein S24 pseudogene 2 . . . . . . . . . . . RPS24P3 . . . ribosomal protein S24 pseudogene 3 . . . . . . . . . . . RPS24P4 . . . ribosomal protein S24 pseudogene 4 . . . . . . . . . . . RPS24P5 . . . ribosomal protein S24 pseudogene 5 . . . . . . . . . . . RPS24P6 . . . ribosomal protein S24 pseudogene 6 . . . . . . . . . . . RPS24P7 . . . ribosomal protein S24 pseudogene 7 . . . . . . . . . . . RPS24P8 . . . ribosomal protein S24 pseudogene 8 . . . . . . . . . . . RPS24P9 . . . ribosomal protein S24 pseudogene 9 . . . . . . . . . . . RPS24P10 . . . ribosomal protein S24 pseudogene 10 . . . . . . . . . . . RPS24P11 . . . ribosomal protein S24 pseudogene 11 . . . . . . . . . . . RPS24P12 . . . ribosomal protein S24 pseudogene 12 . . . . . . . . . . . RPS24P13 . . . ribosomal protein S24 pseudogene 13 . . . . . . . . . . . RPS24P14 . . . ribosomal protein S24 pseudogene 14 . . . . . . . . . . . RPS24P15 . . . ribosomal protein S24 pseudogene 15 . . . . . . . . . . . RPS24P16 . . . ribosomal protein S24 pseudogene 16 . . . . . . . . . . . RPS24P17 . . . ribosomal protein S24 pseudogene 17 . . . . . . . . . . . RPS24P18 . . . ribosomal protein S24 pseudogene 18 . . . . . . . . . . . RPS24P19 . . . ribosomal protein S24 pseudogene 19 . . . . . . . . . . . RPS25 0.809686936073412 0.185516253932608 0.00479680999398029 ribosomal protein S25 . . . . . 0.94325 0.17050 0.013025609 54.62962963 2.43389 0.08748 RPS25P1 . . . ribosomal protein S25 pseudogene 1 . . . . . . . . . . . RPS25P2 . . . ribosomal protein S25 pseudogene 2 . . . . . . . . . . . RPS25P3 . . . ribosomal protein S25 pseudogene 3 . . . . . . . . . . . RPS25P4 . . . ribosomal protein S25 pseudogene 4 . . . . . . . . . . . RPS25P5 . . . ribosomal protein S25 pseudogene 5 . . . . . . . . . . . RPS25P6 . . . ribosomal protein S25 pseudogene 6 . . . . . . . . . . . RPS25P7 . . . ribosomal protein S25 pseudogene 7 . . . . . . . . . . . RPS25P8 . . . ribosomal protein S25 pseudogene 8 . . . . . . . . . . . RPS25P9 . . . ribosomal protein S25 pseudogene 9 . . . . . . . . . . . RPS25P10 . . . ribosomal protein S25 pseudogene 10 . . . . . . . . . . . RPS26 0.753342825086325 0.244547220716038 0.00210995419763697 ribosomal protein S26 . DISEASE: Diamond-Blackfan anemia 10 (DBA10) [MIM:613309]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. {ECO:0000269|PubMed:20116044}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pineal body;pharynx;blood;skeletal muscle;greater omentum;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;larynx;synovium;bone;testis;artery;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta; . 0.12526 . -0.075159878 47.78839349 1.23583 0.04262 RPS26P1 . . . ribosomal protein S26 pseudogene 1 . . . . . . . . . . . RPS26P2 . . . ribosomal protein S26 pseudogene 2 . . . . . . . . . . . RPS26P3 . . . ribosomal protein S26 pseudogene 3 . . . . . . . . . . . RPS26P4 . . . ribosomal protein S26 pseudogene 4 . . . . . . . . . . . RPS26P5 . . . ribosomal protein S26 pseudogene 5 . . . . . . . . . . . RPS26P6 . . . ribosomal protein S26 pseudogene 6 . . . . . . . . . . . RPS26P7 . . . ribosomal protein S26 pseudogene 7 . . . . . . . . . . . RPS26P8 . . . ribosomal protein S26 pseudogene 8 . . . . . . . . . . . RPS26P9 . . . ribosomal protein S26 pseudogene 9 . . . . . . . . . . . RPS26P10 . . . ribosomal protein S26 pseudogene 10 . . . . . . . . . . . RPS26P11 . . . ribosomal protein S26 pseudogene 11 . . . . . 0.07804 . . . . . RPS26P12 . . . ribosomal protein S26 pseudogene 12 . . . . . . . . . . . RPS26P13 . . . ribosomal protein S26 pseudogene 13 . . . . . . . . . . . RPS26P14 . . . ribosomal protein S26 pseudogene 14 . . . . . . . . . . . RPS26P15 . . . ribosomal protein S26 pseudogene 15 . . . . . . . . . . . RPS26P16 . . . ribosomal protein S26 pseudogene 16 . . . . . . . . . . . RPS26P17 . . . ribosomal protein S26 pseudogene 17 . . . . . . . . . . . RPS26P18 . . . ribosomal protein S26 pseudogene 18 . . . . . . . . . . . RPS26P19 . . . ribosomal protein S26 pseudogene 19 . . . . . . . . . . . RPS26P20 . . . ribosomal protein S26 pseudogene 20 . . . . . . . . . . . RPS26P21 . . . ribosomal protein S26 pseudogene 21 . . . . . . . . . . . RPS26P22 . . . ribosomal protein S26 pseudogene 22 . . . . . . . . . . . RPS26P23 . . . ribosomal protein S26 pseudogene 23 . . . . . . . . . . . RPS26P24 . . . ribosomal protein S26 pseudogene 24 . . . . . . . . . . . RPS26P25 . . . ribosomal protein S26 pseudogene 25 . . . . . . . . . . . RPS26P26 . . . ribosomal protein S26 pseudogene 26 . . . . . . . . . . . RPS26P27 . . . ribosomal protein S26 pseudogene 27 . . . . . . . . . . . RPS26P28 . . . ribosomal protein S26 pseudogene 28 . . . . . . . . . . . RPS26P29 . . . ribosomal protein S26 pseudogene 29 . . . . . . . . . . . RPS26P30 . . . ribosomal protein S26 pseudogene 30 . . . . . . . . . . . RPS26P31 . . . ribosomal protein S26 pseudogene 31 . . . . . . . . . . . RPS26P32 . . . ribosomal protein S26 pseudogene 32 . . . . . . . . . . . RPS26P33 . . . ribosomal protein S26 pseudogene 33 . . . . . . . . . . . RPS26P34 . . . ribosomal protein S26 pseudogene 34 . . . . . . . . . . . RPS26P35 . . . ribosomal protein S26 pseudogene 35 . . . . . . . . . . . RPS26P36 . . . ribosomal protein S26 pseudogene 36 . . . . . . . . . . . RPS26P37 . . . ribosomal protein S26 pseudogene 37 . . . . . . . . . . . RPS26P38 . . . ribosomal protein S26 pseudogene 38 . . . . . . . . . . . RPS26P39 . . . ribosomal protein S26 pseudogene 39 . . . . . . . . . . . RPS26P40 . . . ribosomal protein S26 pseudogene 40 . . . . . . . . . . . RPS26P41 . . . ribosomal protein S26 pseudogene 41 . . . . . . . . . . . RPS26P42 . . . ribosomal protein S26 pseudogene 42 . . . . . . . . . . . RPS26P43 . . . ribosomal protein S26 pseudogene 43 . . . . . . . . . . . RPS26P44 . . . ribosomal protein S26 pseudogene 44 . . . . . . . . . . . RPS26P45 . . . ribosomal protein S26 pseudogene 45 . . . . . . . . . . . RPS26P46 . . . ribosomal protein S26 pseudogene 46 . . . . . . . . . . . RPS26P47 . . . ribosomal protein S26 pseudogene 47 . . . . . . . . . . . RPS26P48 . . . ribosomal protein S26 pseudogene 48 . . . . . . . . . . . RPS26P49 . . . ribosomal protein S26 pseudogene 49 . . . . . . . . . . . RPS26P50 . . . ribosomal protein S26 pseudogene 50 . . . . . . . . . . . RPS26P51 . . . ribosomal protein S26 pseudogene 51 . . . . . . . . . . . RPS26P52 . . . ribosomal protein S26 pseudogene 52 . . . . . . . . . . . RPS26P53 . . . ribosomal protein S26 pseudogene 53 . . . . . . . . . . . RPS26P54 . . . ribosomal protein S26 pseudogene 54 . . . . . . . . . . . RPS26P55 . . . ribosomal protein S26 pseudogene 55 . . . . . . . . . . . RPS26P56 . . . ribosomal protein S26 pseudogene 56 . . . . . . . . . . . RPS26P57 . . . ribosomal protein S26 pseudogene 57 . . . . . . . . . . . RPS26P58 . . . ribosomal protein S26 pseudogene 58 . . . . . . . . . . . RPS27 0.697777961357601 0.28528096358463 0.0169410750577699 ribosomal protein S27 . . TISSUE SPECIFICITY: Expressed in a wide variety of actively proliferating cells and tumor tissues.; . . 0.22658 0.20646 0.057118534 57.99716914 1.23044 0.04217 RPS27A 0.525112781965164 0.458508883284357 0.0163783347504787 ribosomal protein S27a FUNCTION: Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.; . . ovary;skin;retina;bone marrow;prostate;thyroid;germinal center;bladder;brain;tonsil;heart;tongue;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;uterus;bone;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;oral cavity;muscle;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; . 0.30803 0.37530 0.103030231 61.2762444 4.8462 0.17837 RPS27AP1 . . . ribosomal protein S27a pseudogene 1 . . . . . . . . . . . RPS27AP2 . . . ribosomal protein S27a pseudogene 2 . . . . . . . . . . . RPS27AP3 . . . ribosomal protein S27a pseudogene 3 . . . . . . . . . . . RPS27AP4 . . . ribosomal protein S27a pseudogene 4 . . . . . . . . . . . RPS27AP5 . . . ribosomal protein S27a pseudogene 5 . . . . . . . . . . . RPS27AP6 . . . ribosomal protein S27a pseudogene 6 . . . . . . . . . . . RPS27AP7 . . . ribosomal protein S27a pseudogene 7 . . . . . . . . . . . RPS27AP8 . . . ribosomal protein S27a pseudogene 8 . . . . . . . . . . . RPS27AP9 . . . ribosomal protein S27a pseudogene 9 . . . . . . . . . . . RPS27AP10 . . . ribosomal protein S27a pseudogene 10 . . . . . . . . . . . RPS27AP11 . . . ribosomal protein S27a pseudogene 11 . . . . . . . . . . . RPS27AP12 . . . ribosomal protein S27a pseudogene 12 . . . . . . . . . . . RPS27AP13 . . . ribosomal protein S27a pseudogene 13 . . . . . . . . . . . RPS27AP14 . . . ribosomal protein S27a pseudogene 14 . . . . . . . . . . . RPS27AP15 . . . ribosomal protein S27a pseudogene 15 . . . . . . . . . . . RPS27AP16 . . . ribosomal protein S27a pseudogene 16 . . . . . . . . . . . RPS27AP17 . . . ribosomal protein S27a pseudogene 17 . . . . . . . . . . . RPS27L 0.335851901877477 0.603407942439914 0.0607401556826095 ribosomal protein S27 like . . . myocardium;ovary;salivary gland;foreskin;developmental;intestine;colon;parathyroid;skin;uterus;prostate;testis;brain;artery;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;muscle;pharynx;blood;breast;lung;cornea;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; uterus corpus;adipose tissue;smooth muscle;adrenal gland;kidney;atrioventricular node; 0.35212 0.08617 0.101211609 60.95777306 22.08009 0.74130 RPS27P1 . . . ribosomal protein S27 pseudogene 1 . . . . . . . . . . . RPS27P2 . . . ribosomal protein S27 pseudogene 2 . . . . . . . . . . . RPS27P3 . . . ribosomal protein S27 pseudogene 3 . . . . . . . . . . . RPS27P4 . . . ribosomal protein S27 pseudogene 4 . . . . . . . . . . . RPS27P5 . . . ribosomal protein S27 pseudogene 5 . . . . . . . . . . . RPS27P6 . . . ribosomal protein S27 pseudogene 6 . . . . . . . . . . . RPS27P7 . . . ribosomal protein S27 pseudogene 7 . . . . . . . . . . . RPS27P8 . . . ribosomal protein S27 pseudogene 8 . . . . . . . . . . . RPS27P9 . . . ribosomal protein S27 pseudogene 9 . . . . . . . . . . . RPS27P10 . . . ribosomal protein S27 pseudogene 10 . . . . . . . . . . . RPS27P11 . . . ribosomal protein S27 pseudogene 11 . . . . . . . . . . . RPS27P12 . . . ribosomal protein S27 pseudogene 12 . . . . . . . . . . . RPS27P13 . . . ribosomal protein S27 pseudogene 13 . . . . . . . . . . . RPS27P14 . . . ribosomal protein S27 pseudogene 14 . . . . . . . . . . . RPS27P15 . . . ribosomal protein S27 pseudogene 15 . . . . . . . . . . . RPS27P16 . . . ribosomal protein S27 pseudogene 16 . . . . . . . . . . . RPS27P17 . . . ribosomal protein S27 pseudogene 17 . . . . . . . . . . . RPS27P18 . . . ribosomal protein S27 pseudogene 18 . . . . . . . . . . . RPS27P19 . . . ribosomal protein S27 pseudogene 19 . . . . . . . . . . . RPS27P20 . . . ribosomal protein S27 pseudogene 20 . . . . . . . . . . . RPS27P21 . . . ribosomal protein S27 pseudogene 21 . . . . . . . . . . . RPS27P22 . . . ribosomal protein S27 pseudogene 22 . . . . . . . . . . . RPS27P23 . . . ribosomal protein S27 pseudogene 23 . . . . . . . . . . . RPS27P24 . . . ribosomal protein S27 pseudogene 24 . . . . . . . . . . . RPS27P25 . . . ribosomal protein S27 pseudogene 25 . . . . . . . . . . . RPS27P26 . . . ribosomal protein S27 pseudogene 26 . . . . . . . . . . . RPS27P27 . . . ribosomal protein S27 pseudogene 27 . . . . . . . . . . . RPS27P28 . . . ribosomal protein S27 pseudogene 28 . . . . . . . . . . . RPS27P29 . . . ribosomal protein S27 pseudogene 29 . . . . . . . . . . . RPS28 0.688845091552417 0.292772708893651 0.0183821995539328 ribosomal protein S28 . DISEASE: Diamond-Blackfan anemia 15, with mandibulofacial dysostosis (DBA15) [MIM:606164]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. {ECO:0000269|PubMed:24942156}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . . 0.167351552 65.04482189 0.89854 0.01892 RPS28P1 . . . ribosomal protein S28 pseudogene 1 . . . . . . . . . . . RPS28P2 . . . ribosomal protein S28 pseudogene 2 . . . . . . . . . . . RPS28P3 . . . ribosomal protein S28 pseudogene 3 . . . . . . . . . . . RPS28P4 . . . ribosomal protein S28 pseudogene 4 . . . . . . . . . . . RPS28P5 . . . ribosomal protein S28 pseudogene 5 . . . . . . . . . . . RPS28P6 . . . ribosomal protein S28 pseudogene 6 . . . . . . . . . . . RPS28P7 . . . ribosomal protein S28 pseudogene 7 . . . . . . . . . . . RPS28P8 . . . ribosomal protein S28 pseudogene 8 . . . . . . . . . . . RPS28P9 . . . ribosomal protein S28 pseudogene 9 . . . . . . . . . . . RPS29 0.349407010133348 0.595110570499892 0.0554824193667603 ribosomal protein S29 . DISEASE: Diamond-Blackfan anemia 13 (DBA13) [MIM:615909]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. {ECO:0000269|PubMed:24829207}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;thyroid;bladder;brain;gall bladder;tonsil;heart;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;bile duct;pancreas;lung;pia mater;placenta;kidney;stomach;aorta;thymus; lymph node;salivary gland;white blood cells;skin;tonsil;thymus; . 0.08516 0.035072054 56.2514744 1.69692 0.05542 RPS29P1 . . . ribosomal protein S29 pseudogene 1 . . . . . . . . . . . RPS29P2 . . . ribosomal protein S29 pseudogene 2 . . . . . . . . . . . RPS29P3 . . . ribosomal protein S29 pseudogene 3 . . . . . . . . . . . RPS29P4 . . . ribosomal protein S29 pseudogene 4 . . . . . . . . . . . RPS29P5 . . . ribosomal protein S29 pseudogene 5 . . . . . . . . . . . RPS29P6 . . . ribosomal protein S29 pseudogene 6 . . . . . . . . . . . RPS29P7 . . . ribosomal protein S29 pseudogene 7 . . . . . . . . . . . RPS29P8 . . . ribosomal protein S29 pseudogene 8 . . . . . . . . . . . RPS29P9 . . . ribosomal protein S29 pseudogene 9 . . . . . . . . . . . RPS29P10 . . . ribosomal protein S29 pseudogene 10 . . . . . . . . . . . RPS29P11 . . . ribosomal protein S29 pseudogene 11 . . . . . . . . . . . RPS29P12 . . . ribosomal protein S29 pseudogene 12 . . . . . . . . . . . RPS29P13 . . . ribosomal protein S29 pseudogene 13 . . . . . . . . . . . RPS29P14 . . . ribosomal protein S29 pseudogene 14 . . . . . . . . . . . RPS29P15 . . . ribosomal protein S29 pseudogene 15 . . . . . . . . . . . RPS29P16 . . . ribosomal protein S29 pseudogene 16 . . . . . . . . . . . RPS29P17 . . . ribosomal protein S29 pseudogene 17 . . . . . . . . . . . RPS29P18 . . . ribosomal protein S29 pseudogene 18 . . . . . . . . . . . RPS29P19 . . . ribosomal protein S29 pseudogene 19 . . . . . . . . . . . RPS29P20 . . . ribosomal protein S29 pseudogene 20 . . . . . . . . . . . RPS29P21 . . . ribosomal protein S29 pseudogene 21 . . . . . . . . . . . RPS29P22 . . . ribosomal protein S29 pseudogene 22 . . . . . . . . . . . RPS29P23 . . . ribosomal protein S29 pseudogene 23 . . . . . . . . . . . RPS29P24 . . . ribosomal protein S29 pseudogene 24 . . . . . . . . . . . RPS29P25 . . . ribosomal protein S29 pseudogene 25 . . . . . . . . . . . RPS29P26 . . . ribosomal protein S29 pseudogene 26 . . . . . . . . . . . RPS29P27 . . . ribosomal protein S29 pseudogene 27 . . . . . . . . . . . RPS29P28 . . . ribosomal protein S29 pseudogene 28 . . . . . . . . . . . RPSA 0.751851425879316 0.24600181936317 0.00214675475751406 ribosomal protein SA FUNCTION: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA- precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Acts as a PPP1R16B-dependent substrate of PPP1CA. {ECO:0000255|HAMAP-Rule:MF_03016, ECO:0000269|PubMed:16263087, ECO:0000269|PubMed:6300843}.; DISEASE: Asplenia, isolated congenital (ICAS) [MIM:271400]: A rare primary immunodeficiency and life-threatening condition, often presenting with pneumococcal sepsis. Most affected individuals die of severe bacterial infections in early childhood. Isolated asplenia is distinct from asplenia associated with other complex visceral defects, notably heterotaxy syndromes such as Ivemark syndrome. {ECO:0000269|PubMed:23579497}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;synovium;bone;thyroid;testis;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;stomach;thymus; . . 0.28814 0.035072054 56.2514744 4.22412 0.15368 RPSAP1 . . . ribosomal protein SA pseudogene 1 . . . . . . . . . . . RPSAP2 . . . ribosomal protein SA pseudogene 2 . . . . . . . . . . . RPSAP3 . . . ribosomal protein SA pseudogene 3 . . . . . . . . . . . RPSAP4 . . . ribosomal protein SA pseudogene 4 . . . . . . . . . . . RPSAP5 . . . ribosomal protein SA pseudogene 5 . . . . . . . . . . . RPSAP6 . . . ribosomal protein SA pseudogene 6 . . . . . . . . . . . RPSAP7 . . . ribosomal protein SA pseudogene 7 . . . . . . . . . . . RPSAP8 . . . ribosomal protein SA pseudogene 8 . . . . . . . . . . . RPSAP9 . . . ribosomal protein SA pseudogene 9 . . . . . . . . . . . RPSAP10 . . . ribosomal protein SA pseudogene 10 . . . . . . . . . . . RPSAP11 . . . ribosomal protein SA pseudogene 11 . . . . . . . . . . . RPSAP12 . . . ribosomal protein SA pseudogene 12 . . . . . . . . . . . RPSAP13 . . . ribosomal protein SA pseudogene 13 . . . . . . . . . . . RPSAP14 . . . ribosomal protein SA pseudogene 14 . . . . . . . . . . . RPSAP15 . . . ribosomal protein SA pseudogene 15 . . . . . . 0.28814 . . . . RPSAP16 . . . ribosomal protein SA pseudogene 16 . . . . . . . . . . . RPSAP17 . . . ribosomal protein SA pseudogene 17 . . . . . . . . . . . RPSAP18 . . . ribosomal protein SA pseudogene 18 . . . . . . . . . . . RPSAP19 . . . ribosomal protein SA pseudogene 19 . . . . . . . . . . . RPSAP20 . . . ribosomal protein SA pseudogene 20 . . . . . . . . . . . RPSAP21 . . . ribosomal protein SA pseudogene 21 . . . . . . . . . . . RPSAP22 . . . ribosomal protein SA pseudogene 22 . . . . . . . . . . . RPSAP23 . . . ribosomal protein SA pseudogene 23 . . . . . . . . . . . RPSAP24 . . . ribosomal protein SA pseudogene 24 . . . . . . . . . . . RPSAP25 . . . ribosomal protein SA pseudogene 25 . . . . . . . . . . . RPSAP26 . . . ribosomal protein SA pseudogene 26 . . . . . . . . . . . RPSAP27 . . . ribosomal protein SA pseudogene 27 . . . . . . . . . . . RPSAP28 . . . ribosomal protein SA pseudogene 28 . . . . . . . . . . . RPSAP29 . . . ribosomal protein SA pseudogene 29 . . . . . . . . . . . RPSAP30 . . . ribosomal protein SA pseudogene 30 . . . . . . . . . . . RPSAP31 . . . ribosomal protein SA pseudogene 31 . . . . . . . . . . . RPSAP32 . . . ribosomal protein SA pseudogene 32 . . . . . . . . . . . RPSAP33 . . . ribosomal protein SA pseudogene 33 . . . . . . . . . . . RPSAP34 . . . ribosomal protein SA pseudogene 34 . . . . . . . . . . . RPSAP35 . . . ribosomal protein SA pseudogene 35 . . . . . . . . . . . RPSAP36 . . . ribosomal protein SA pseudogene 36 . . . . . . . . . . . RPSAP37 . . . ribosomal protein SA pseudogene 37 . . . . . . . . . . . RPSAP38 . . . ribosomal protein SA pseudogene 38 . . . . . . . . . . . RPSAP39 . . . ribosomal protein SA pseudogene 39 . . . . . . . . . . . RPSAP40 . . . ribosomal protein SA pseudogene 40 . . . . . . . . . . . RPSAP41 . . . ribosomal protein SA pseudogene 41 . . . . . . . . . . . RPSAP42 . . . ribosomal protein SA pseudogene 42 . . . . . . . . . . . RPSAP43 . . . ribosomal protein SA pseudogene 43 . . . . . . . . . . . RPSAP44 . . . ribosomal protein SA pseudogene 44 . . . . . . . . . . . RPSAP45 . . . ribosomal protein SA pseudogene 45 . . . . . . . . . . . RPSAP46 . . . ribosomal protein SA pseudogene 46 . . . . . . . . . . . RPSAP47 . . . ribosomal protein SA pseudogene 47 . . . . . . . . . . . RPSAP48 . . . ribosomal protein SA pseudogene 48 . . . . . . . . . . . RPSAP49 . . . ribosomal protein SA pseudogene 49 . . . . . . . . . . . RPSAP50 . . . ribosomal protein SA pseudogene 50 . . . . . . . . . . . RPSAP51 . . . ribosomal protein SA pseudogene 51 . . . . . . . . . . . RPSAP52 . . . ribosomal protein SA pseudogene 52 . . . . . . . . . . . RPSAP53 . . . ribosomal protein SA pseudogene 53 . . . . . . . . . . . RPSAP54 . . . ribosomal protein SA pseudogene 54 . . . . . . . . . . . RPSAP55 . . . ribosomal protein SA pseudogene 55 . . . . . . . . . . . RPSAP56 . . . ribosomal protein SA pseudogene 56 . . . . . . . . . . . RPSAP57 . . . ribosomal protein SA pseudogene 57 . . . . . . . . . . . RPSAP58 0.581630356470054 0.375422155763326 0.0429474877666195 ribosomal protein SA pseudogene 58 . . . lymphoreticular;ovary;colon;vein;skin;retina;uterus;prostate;endometrium;bone;testis;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;trophoblast;heart;islets of Langerhans;muscle;urinary;blood;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;cerebellum; . . . . . 3538.79624 11.47685 RPSAP59 . . . ribosomal protein SA pseudogene 59 . . . . . . . . . . . RPSAP60 . . . ribosomal protein SA pseudogene 60 . . . . . . . . . . . RPSAP61 . . . ribosomal protein SA pseudogene 61 . . . . . . . . . . . RPSAP62 . . . ribosomal protein SA pseudogene 62 . . . . . . . . . . . RPSAP63 . . . ribosomal protein SA pseudogene 63 . . . . . . . . . . . RPSAP64 . . . ribosomal protein SA pseudogene 64 . . . . . . . . . . . RPSAP65 . . . ribosomal protein SA pseudogene 65 . . . . . . . . . . . RPSAP66 . . . ribosomal protein SA pseudogene 66 . . . . . . . . . . . RPSAP67 . . . ribosomal protein SA pseudogene 67 . . . . . . . . . . . RPSAP68 . . . ribosomal protein SA pseudogene 68 . . . . . . . . . . . RPSAP69 . . . ribosomal protein SA pseudogene 69 . . . . . . . . . . . RPSAP70 . . . ribosomal protein SA pseudogene 70 . . . . . . . . . . . RPSAP71 . . . ribosomal protein SA pseudogene 71 . . . . . . . . . . . RPSAP72 . . . ribosomal protein SA pseudogene 72 . . . . . . . . . . . RPSAP73 . . . ribosomal protein SA pseudogene 73 . . . . . . . . . . . RPSAP74 . . . ribosomal protein SA pseudogene 74 . . . . . . . . . . . RPSAP75 . . . ribosomal protein SA pseudogene 75 . . . . . . . . . . . RPSAP76 . . . ribosomal protein SA pseudogene 76 . . . . . . . . . . . RPTN 3.17531967976647e-18 0.00447502569563581 0.995524974304364 repetin FUNCTION: Involved in the cornified cell envelope formation. Multifunctional epidermal matrix protein. Reversibly binds calcium.; . TISSUE SPECIFICITY: Expression is scattered in the normal epidermis but strong in the acrosyringium, the inner hair root sheath and in the filiform papilli of the tongue. {ECO:0000269|PubMed:15854042}.; oral cavity;head and neck; superior cervical ganglion;skeletal muscle; 0.09608 . 1.243805243 93.41825902 382.87927 4.12630 RPTOR 0.999999983261949 1.67380507155648e-08 4.96335172636628e-21 regulatory associated protein of MTOR, complex 1 FUNCTION: Involved in the control of the mammalian target of rapamycin complex 1 (mTORC1) activity which regulates cell growth and survival, and autophagy in response to nutrient and hormonal signals; functions as a scaffold for recruiting mTORC1 substrates. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1- mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Involved in ciliogenesis. {ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12150926, ECO:0000269|PubMed:23727834}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle, and in a lesser extent in brain, lung, small intestine, kidney and placenta. Isoform 3 is widely expressed, with highest levels in nasal mucosa and pituitary and lowest in spleen. {ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12408816}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . . -2.583601763 0.831564048 64.74857 1.65128 RPUSD1 3.05727308154375e-08 0.0483933179703621 0.951606651456907 RNA pseudouridylate synthase domain containing 1 . . . lymphoreticular;medulla oblongata;colon;skin;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;visual apparatus;alveolus;spleen;cervix;kidney;stomach; ciliary ganglion;trigeminal ganglion;cerebellum; 0.09645 0.13239 -0.244249595 36.17008728 572.27155 4.85688 RPUSD2 0.000105170590634246 0.812609108307562 0.187285721101804 RNA pseudouridylate synthase domain containing 2 . . . medulla oblongata;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;lens;lung;placenta;macula lutea;hippocampus;visual apparatus;liver;cervix;kidney;mammary gland;stomach; superior cervical ganglion; 0.03377 0.07364 -0.622676946 17.30950696 66.58895 1.68224 RPUSD3 0.0003227735750223 0.945536942009371 0.0541402844156061 RNA pseudouridylate synthase domain containing 3 . . . . . 0.10418 0.07402 0.064394823 58.84642604 121.65948 2.40211 RPUSD4 0.00672913845111168 0.975076594537374 0.018194267011514 RNA pseudouridylate synthase domain containing 4 . . . salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;germinal center;brain;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; . 0.06134 0.08207 0.997633954 90.65227648 2854.48141 10.10974 RQCD1 0.930277945404411 0.0696489232595629 7.31313360256311e-05 RCD1 required for cell differentiation1 homolog (S. pombe) FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Involved in down-regulation of MYB- and JUN-dependent transcription. May play a role in cell differentiation (By similarity). Can bind oligonucleotides, such as poly-G, poly-C or poly-T (in vitro), but the physiological relevance of this is not certain. Does not bind poly-A. Enhances ligand-dependent transcriptional activity of nuclear hormone receptors, including RARA, expect ESR1-mediated transcription that is not only slightly increased, if at all. {ECO:0000250, ECO:0000269|PubMed:17189474, ECO:0000269|PubMed:18180299}.; . TISSUE SPECIFICITY: Detected in spleen, thymus, prostate, testis, ovary and intestine. {ECO:0000269|PubMed:9447985}.; ovary;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;hypothalamus;oral cavity;muscle;blood;skeletal muscle;bile duct;breast;lung;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;cerebellum peduncles;testis;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.40373 0.15178 -0.119252484 44.53880632 4.04018 0.14863 RRAD 0.310768743276529 0.67141010502917 0.0178211516943015 Ras-related associated with diabetes FUNCTION: May play an important role in cardiac antiarrhythmia via the strong suppression of voltage-gated L-type Ca(2+) currents. Regulates voltage-dependent L-type calcium channel subunit alpha- 1C trafficking to the cell membrane (By similarity). Inhibits cardiac hypertrophy through the calmodulin-dependent kinase II (CaMKII) pathway. Inhibits phosphorylation and activation of CAMK2D. {ECO:0000250, ECO:0000269|PubMed:18056528}.; . TISSUE SPECIFICITY: Most abundantly expressed in the heart. Also found in the skeletal muscle and lung. Lesser amounts in placenta and kidney. Also detected in adipose tissue. Overexpressed in muscle of type II diabetic humans. {ECO:0000269|PubMed:18056528}.; myocardium;ovary;colon;skin;uterus;prostate;whole body;optic nerve;ganglion;larynx;gum;bone;testis;unclassifiable (Anatomical System);heart;cartilage;muscle;adrenal cortex;skeletal muscle;lung;nasopharynx;placenta;visual apparatus;alveolus;head and neck;kidney; lung;heart;tongue;placenta;fetal lung;skeletal muscle; 0.40283 0.34309 -0.361761279 28.6329323 271.87199 3.53255 RRAGA 0.291376609279646 0.687885741559797 0.0207376491605571 Ras related GTP binding A FUNCTION: Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade. Forms heterodimeric Rag complexes with RRAGC or RRAGD and cycles between an inactive GDP-bound and an active GTP-bound form. In its active form participates to the relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. Involved in the RCC1/Ran-GTPase pathway. May play a direct role in a TNF-alpha signaling pathway leading to induction of cell death. May alternatively act as a cellular target for adenovirus E3-14.7K, an inhibitor of TNF-alpha functions, thereby affecting cell death. {ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:25936802, ECO:0000269|PubMed:8995684, ECO:0000269|PubMed:9394008}.; . TISSUE SPECIFICITY: Ubiquitously expressed with highest levels of expression in skeletal muscle, heart, and brain. {ECO:0000269|PubMed:8995684}.; . . 0.05456 0.14896 -0.273576253 33.97027601 9.40907 0.34631 RRAGAP1 . . . Ras related GTP binding A pseudogene 1 . . . . . . . . . . . RRAGB 0.893169858978643 0.106611442414397 0.000218698606959937 Ras related GTP binding B FUNCTION: Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade. Forms heterodimeric Rag complexes with RRAGC or RRAGD and cycles between an inactive GDP-bound and an active GTP-bound form. In its active form participates to the relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. Involved in the RCC1/Ran-GTPase pathway. {ECO:0000269|PubMed:18497260, ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:9394008}.; . . unclassifiable (Anatomical System);ovary;heart;colon;skin;skeletal muscle;retina;uterus;pancreas;prostate;lung;adrenal gland;nasopharynx;trabecular meshwork;bone;thyroid;placenta;testis;spleen;germinal center;kidney;brain;tonsil;stomach; superior cervical ganglion; 0.20583 0.12684 -0.141298762 42.87567823 12.6163 0.46009 RRAGC 0.600078052257623 0.397983800062249 0.00193814768012778 Ras related GTP binding C FUNCTION: Guanine nucleotide-binding protein forming heterodimeric Rag complexes required for the amino acid-induced relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. This is a crucial step in the activation of the TOR signaling cascade by amino acids. {ECO:0000269|PubMed:20381137}.; . . . . 0.37240 0.11657 -0.229483771 36.86010852 8.10146 0.29705 RRAGD 0.812902090860283 0.186125075449519 0.000972833690197695 Ras related GTP binding D FUNCTION: Guanine nucleotide-binding protein forming heterodimeric Rag complexes required for the amino acid-induced relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. This is a crucial step in the activation of the TOR signaling cascade by amino acids. {ECO:0000269|PubMed:20381137}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;lung;placenta;macula lutea;liver;alveolus;spleen;kidney;stomach;cerebellum; tongue;kidney;skeletal muscle; 0.21118 0.10528 -0.05129383 49.75819769 34.1959 1.04707 RRAS 0.287257428796457 0.691318417605804 0.0214241535977389 related RAS viral (r-ras) oncogene homolog FUNCTION: Regulates the organization of the actin cytoskeleton (PubMed:16537651, PubMed:18270267). With OSPBL3, modulates integrin beta-1 (ITGB1) activity (PubMed:18270267). {ECO:0000269|PubMed:16537651, ECO:0000269|PubMed:18270267}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; lung;heart; 0.19254 0.19894 0.238945317 69.20853975 49.3267 1.37357 RRAS2 0.674254313651317 0.320947930157995 0.00479775619068778 related RAS viral (r-ras) oncogene homolog 2 FUNCTION: It is a plasma membrane-associated GTP-binding protein with GTPase activity. Might transduce growth inhibitory signals across the cell membrane, exerting its effect through an effector shared with the Ras proteins but in an antagonistic fashion.; DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease. {ECO:0000269|PubMed:8052619}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously present in all tissues examined, with the highest levels in heart, placenta, and skeletal muscle. Moderate levels in lung and liver; low levels in brain, kidney, and pancreas. {ECO:0000269|PubMed:8052619}.; unclassifiable (Anatomical System);heart;ovary;colon;fovea centralis;choroid;lens;skin;retina;breast;uterus;optic nerve;whole body;bone;thyroid;placenta;macula lutea;liver;amnion;testis;germinal center;kidney;spinal ganglion;brain;stomach; superior cervical ganglion; 0.84807 0.15588 0.035072054 56.2514744 9.67806 0.35570 RRBP1 0.000136331977393793 0.999791152624101 7.25153985048292e-05 ribosome binding protein 1 FUNCTION: Acts as a ribosome receptor and mediates interaction between the ribosome and the endoplasmic reticulum membrane. {ECO:0000250}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;pancreas;placenta;thyroid;liver;ciliary ganglion;trigeminal ganglion;fetal thyroid; 0.17093 0.23281 0.10828245 61.73625855 5646.91958 15.54928 RREB1 0.999967927968287 3.20720292861017e-05 2.42728600952417e-12 ras responsive element binding protein 1 FUNCTION: Transcription factor that binds specifically to the RAS- responsive elements (RRE) of gene promoters. May be involved in Ras/Raf-mediated cell differentiation by enhancing calcitonin expression. Represses the angiotensinogen gene. Negatively regulates the transcriptional activity of AR. Potentiates the transcriptional activity of NEUROD1. {ECO:0000269|PubMed:10390538, ECO:0000269|PubMed:12482979, ECO:0000269|PubMed:15067362, ECO:0000269|PubMed:17550981, ECO:0000269|PubMed:8816445, ECO:0000269|PubMed:9305772}.; . TISSUE SPECIFICITY: Expressed in heart, placenta, lung, liver, skeletal muscle, kidney and pancreas. Not found in the brain. {ECO:0000269|PubMed:8816445}.; medulla oblongata;ovary;colon;parathyroid;skin;bone marrow;prostate;frontal lobe;larynx;thyroid;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.22153 0.11322 -0.172896356 40.60509554 6473.92162 16.88180 RRH 5.10693280504954e-06 0.418996356854964 0.580998536212231 retinal pigment epithelium-derived rhodopsin homolog FUNCTION: May play a role in rpe physiology either by detecting light directly or by monitoring the concentration of retinoids or other photoreceptor-derived compounds.; . TISSUE SPECIFICITY: Found only in the eye, where it is localized to the retinal pigment epithelium (RPE). In the RPE, it is localized to the microvilli that surround the photoreceptor outer segments.; optic nerve;macula lutea;fovea centralis;choroid;lens;brain;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.22442 0.12931 0.507139401 80.10143902 85.38394 1.96958 RRM1 0.999994803572266 5.19642770538439e-06 2.88252150802573e-14 ribonucleotide reductase catalytic subunit M1 FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;pharynx;blood;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;tumor;ciliary ganglion; 0.99050 0.35194 -0.644723694 16.52512385 49.59769 1.37845 RRM1-AS1 . . . RRM1 antisense RNA 1 . . . . . . . . . . . RRM2 0.96827092119529 0.0317189146046616 1.01642000488142e-05 ribonucleotide reductase regulatory subunit M2 FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling.; . . lymphoreticular;ovary;salivary gland;intestine;colon;vein;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;visual apparatus;liver;duodenum;cervix;head and neck;spleen;kidney;mammary gland;stomach; fetal liver;superior cervical ganglion;tumor;bone marrow;thymus; 0.98364 0.21552 -0.249709319 35.74545883 20.12841 0.68790 RRM2B 0.157235868251287 0.839420527649236 0.00334360409947754 ribonucleotide reductase regulatory TP53 inducible subunit M2B FUNCTION: Plays a pivotal role in cell survival by repairing damaged DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free radical center required for catalysis. Forms an active ribonucleotide reductase (RNR) complex with RRM1 which is expressed both in resting and proliferating cells in response to DNA damage. {ECO:0000269|PubMed:10716435, ECO:0000269|PubMed:11517226, ECO:0000269|PubMed:11719458}.; DISEASE: Mitochondrial DNA depletion syndrome 8A (MTDPS8A) [MIM:612075]: A disorder due to mitochondrial dysfunction characterized by various combinations of neonatal hypotonia, neurological deterioration, respiratory distress, lactic acidosis, and renal tubulopathy. {ECO:0000269|PubMed:17486094, ECO:0000269|PubMed:18504129}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial DNA depletion syndrome 8B (MTDPS8B) [MIM:612075]: A disease due to mitochondrial dysfunction and characterized by ophthalmoplegia, ptosis, gastrointestinal dysmotility, cachexia, peripheral neuropathy. {ECO:0000269|PubMed:19667227}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal dominant, 5 (PEOA5) [MIM:613077]: A disorder characterized by progressive weakness of ocular muscles and levator muscle of the upper eyelid. In a minority of cases, it is associated with skeletal myopathy, which predominantly involves axial or proximal muscles and which causes abnormal fatigability and even permanent muscle weakness. Ragged-red fibers and atrophy are found on muscle biopsy. A large proportion of chronic ophthalmoplegias are associated with other symptoms, leading to a multisystemic pattern of this disease. Additional symptoms are variable, and may include cataracts, hearing loss, sensory axonal neuropathy, ataxia, depression, hypogonadism, and parkinsonism. {ECO:0000269|PubMed:19664747}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed at a high level in skeletal muscle and at a weak level in thymus. Expressed in epithelial dysplasias and squamous cell carcinoma. {ECO:0000269|PubMed:14583450}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);amygdala;heart;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;cornea;trabecular meshwork;placenta;visual apparatus;liver;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion; 0.44429 0.20468 -0.075159878 47.78839349 . . RRM2P2 . . . ribonucleotide reductase M2 polypeptide pseudogene 2 . . . . . . . . . . . RRM2P3 . . . ribonucleotide reductase M2 polypeptide pseudogene 3 . . . . . . . . . . . RRM2P4 . . . ribonucleotide reductase M2 polypeptide pseudogene 4 . . . . . . . . . . . RRN3 0.000474580439094432 0.998071536910588 0.00145388265031799 RRN3 homolog, RNA polymerase I transcription factor FUNCTION: Required for efficient transcription initiation by RNA polymerase I. Required for the formation of the competent preinitiation complex (PIC). Dissociates from pol I as a consequence of transcription. In vitro, cannot activate transcription in a subsequent transcription reaction (By similarity). {ECO:0000250, ECO:0000269|PubMed:10758157, ECO:0000269|PubMed:11250903, ECO:0000269|PubMed:11265758, ECO:0000269|PubMed:15805466}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; testis;atrioventricular node; 0.09916 0.13442 0.378498378 75.58386412 586.40473 4.91226 RRN3P1 . . . RRN3 homolog, RNA polymerase I transcription factor pseudogene 1 . . . . . . . . . . . RRN3P2 . . . RRN3 homolog, RNA polymerase I transcription factor pseudogene 2 . . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;parathyroid;skin;skeletal muscle;retina;uterus;prostate;lung;placenta;liver;testis;spleen;germinal center;brain;stomach; . . . . . . . RRN3P3 . . . RRN3 homolog, RNA polymerase I transcription factor pseudogene 3 . . . . . . . . . . . RRNAD1 2.11535175142641e-08 0.433908204817998 0.566091774028484 ribosomal RNA adenine dimethylase domain containing 1 . . . . . 0.14510 . -0.201976964 38.98325077 39.57821 1.16654 RRP1 0.00185041139129439 0.993176452003687 0.00497313660501849 ribosomal RNA processing 1 FUNCTION: Plays a critical role in the generation of 28S rRNA.; . TISSUE SPECIFICITY: Ubiquitously expressed in fetal and adult tissues. {ECO:0000269|PubMed:9192856}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;lens;skeletal muscle;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;alveolus;head and neck;cervix;kidney;mammary gland;stomach; . 0.10646 0.10690 0.841481379 88.35810333 2696.1066 9.77036 RRP1B 0.0368184350731871 0.963118575169199 6.29897576137654e-05 ribosomal RNA processing 1B . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;muscle;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney; tumor;testis; 0.43897 0.12441 -0.354480518 29.42911064 196.09453 3.03033 RRP7A 0.00237295900903576 0.92597460612801 0.0716524348629545 ribosomal RNA processing 7 homolog A . . . lymphoreticular;ovary;salivary gland;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;lung;tumor;ciliary ganglion;white blood cells;skeletal muscle; . . 1.306318795 93.99622552 1895.05295 8.00383 RRP7BP . . . ribosomal RNA processing 7 homolog B, pseudogene . . . . . . . . . . . RRP8 6.40182729629982e-06 0.701636824792975 0.298356773379729 ribosomal RNA processing 8, methyltransferase, homolog (yeast) FUNCTION: Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys- 9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and probably acts as a methyltransferase. Its substrates are however unknown. {ECO:0000269|PubMed:18485871}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;pons;skin; 0.16394 0.08512 0.512596355 80.29606039 465.12442 4.46785 RRP9 0.3420434837746 0.657834109116385 0.000122407109015722 ribosomal RNA processing 9, small subunit (SSU) processome component, homolog (yeast) FUNCTION: Component of a nucleolar small nuclear ribonucleoprotein particle (snoRNP) thought to participate in the processing and modification of pre-ribosomal RNA.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;endometrium;synovium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;blood;lens;lung;macula lutea;visual apparatus;liver;spleen;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion; 0.81384 0.12094 -0.157884861 42.05590941 109.70531 2.27541 RRP12 4.36448365338862e-06 0.999994938445879 6.97070467504461e-07 ribosomal RNA processing 12 homolog . . TISSUE SPECIFICITY: Weakly expressed. Expressed at intermediate level in testis and ovary. {ECO:0000269|PubMed:9734811}.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;urinary;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; atrioventricular node;trigeminal ganglion;skeletal muscle; 0.36713 0.09995 -0.981182694 8.657702288 7215.81402 18.30427 RRP15 0.00163197039115739 0.695993276398539 0.302374753210304 ribosomal RNA processing 15 homolog . . . . . 0.42620 0.09811 0.72761005 86.08162302 550.82989 4.77277 RRP36 9.22385848172131e-11 0.0798639890092927 0.920136010898469 ribosomal RNA processing 36 FUNCTION: Involved in the early processing steps of the pre-rRNA in the maturation pathway leading to the 18S rRNA. {ECO:0000269|PubMed:20038530}.; . . lymphoreticular;medulla oblongata;umbilical cord;ovary;salivary gland;intestine;colon;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;thyroid;pituitary gland;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;alveolus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.03981 0.09432 0.262810045 70.43524416 765.88948 5.48207 RRS1 0.551023834121811 0.43549408712052 0.013482078757669 ribosome biogenesis regulator homolog FUNCTION: Involved in ribosome biogenesis. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;skeletal muscle; 0.52765 0.20417 0.971952656 90.26893135 968.25079 6.01838 RRS1-AS1 . . . RRS1 antisense RNA 1 (head to head) . . . . . . . . . . . RS1 0.892912340131916 0.106020919610618 0.00106674025746627 retinoschisin 1 FUNCTION: May be active in cell adhesion processes during retinal development.; DISEASE: Retinoschisis juvenile X-linked 1 (XLRS1) [MIM:312700]: A vitreo-retinal dystrophy characterized by macular pathology and by splitting of the superficial layer of the retina. Macular changes are present in almost all cases. In the fundi, radially oriented intraretinal foveomacular cysts are seen in a spoke-wheel configuration, with the absence of foveal reflex in most cases. In addition, approximately half of cases have bilateral peripheral retinoschisis in the inferotemporal part of the retina. Aside from the typical fundus appearance, strabismus, nystagmus, axial hyperopia, defective color vision and foveal ectopy can be present. The most important complications are vitreous hemorrhage, retinal detachment, and neovascular glaucoma. {ECO:0000269|PubMed:10079181, ECO:0000269|PubMed:10220153, ECO:0000269|PubMed:10234514, ECO:0000269|PubMed:10450864, ECO:0000269|PubMed:10533068, ECO:0000269|PubMed:17304551, ECO:0000269|PubMed:17615541, ECO:0000269|PubMed:19093009, ECO:0000269|PubMed:9326935, ECO:0000269|PubMed:9760195, ECO:0000269|Ref.10}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Restricted to the retina (at protein level). At the mRNA level, detected only within the photoreceptor cell layer, most prominently within the inner segments of the photoreceptors. Undetectable in the inner plexiform layers and the inner nuclear layer. At the protein level, found in the inner segment of the photoreceptors, the inner nuclear layer, the inner plexiform layer and the ganglion cell layer. At the macula, expressed in both the outer and inner nuclear layers and in the inner plexiform layer (at protein level). {ECO:0000269|PubMed:10915776}.; . . 0.24530 0.23021 0.3032669 72.009908 117.21763 2.35449 RSAD1 5.75080843134765e-06 0.678855737836305 0.321138511355263 radical S-adenosyl methionine domain containing 1 FUNCTION: May be involved in porphyrin cofactor biosynthesis. {ECO:0000250}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;aorta;stomach; atrioventricular node;trigeminal ganglion; 0.15846 0.13877 0.264628794 70.5178108 589.54972 4.92329 RSAD2 4.58535841046995e-12 0.00728826278325863 0.992711737212156 radical S-adenosyl methionine domain containing 2 FUNCTION: Interferon-inducible iron-sulfur (4FE-4S) cluster- binding antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon. Can inhibit a wide range of DNA and RNA viruses, including human cytomegalovirus (HCMV), hepatitis C virus (HCV), west Nile virus (WNV), dengue virus, sindbis virus, influenza A virus, sendai virus, vesicular stomatitis virus (VSV), and human immunodeficiency virus (HIV-1). Displays antiviral activity against influenza A virus by inhibiting the budding of the virus from the plasma membrane by disturbing the lipid rafts. This is accomplished, at least in part, through binding and inhibition of the enzyme farnesyl diphospate synthase (FPPS), which is essential for the biosynthesis of isoprenoid-derived lipids. Promotes TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating Lys-63'-linked ubiquitination of IRAK1. Plays a role in CD4+ T-cells activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins. {ECO:0000269|PubMed:11752458, ECO:0000269|PubMed:16108059, ECO:0000269|PubMed:16982913, ECO:0000269|PubMed:17686841, ECO:0000269|PubMed:18005719, ECO:0000269|PubMed:19074433}.; . . . . 0.20262 . -0.047654689 50.22410946 74.4174 1.80264 RSBN1 0.805139687607845 0.194858463570593 1.84882156123654e-06 round spermatid basic protein 1 . . . ovary;colon;parathyroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;cerebellum peduncles;prefrontal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.58281 0.10748 -0.844966979 11.1759849 38.26495 1.13644 RSBN1L 0.500030091124699 0.499933546154535 3.63627207653917e-05 round spermatid basic protein 1-like . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;ganglion;endometrium;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;adrenal cortex;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.19477 . -0.821100135 11.88369899 271.24768 3.52955 RSC1A1 1.4572097447573e-08 0.0599496494939228 0.94005033593398 regulatory solute carrier protein, family 1, member 1 FUNCTION: Mediates transcriptional and post-transcriptional regulation of SLC5A1. Inhibits a dynamin and PKC-dependent exocytotic pathway of SLC5A1. Also involved in transcriptional regulation of SLC22A2. Exhibits glucose-dependent, short-term inhibition of SLC5A1 and SLC22A2 by inhibiting the release of vesicles from the trans-Golgi network. {ECO:0000269|PubMed:14724758, ECO:0000269|PubMed:16788146, ECO:0000269|PubMed:8836035}.; . TISSUE SPECIFICITY: Expressed in small intestine, kidney and brain. {ECO:0000269|PubMed:8836035}.; unclassifiable (Anatomical System);lymph node;sympathetic chain;colon;skeletal muscle;breast;frontal lobe;cochlea;larynx;nasopharynx;placenta;thyroid;liver;head and neck;spleen;kidney;brain;stomach; . 0.41597 0.23021 1.067416815 91.66666667 1729.18109 7.67578 RSF1 0.999999962570394 3.74296059174351e-08 1.74193208212563e-19 remodeling and spacing factor 1 FUNCTION: Required for assembly of regular nucleosome arrays by the RSF chromatin-remodeling complex. Facilitates transcription of hepatitis B virus (HBV) genes by the pX transcription activator. In case of infection by HBV, together with pX, it represses TNF- alpha induced NF-kappa-B transcription activation. Represses transcription when artificially recruited to chromatin by fusion to a heterogeneous DNA binding domain. {ECO:0000269|PubMed:11788598, ECO:0000269|PubMed:12972596}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;epidermis;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.82615 0.10928 0.387604191 75.69591885 216.63215 3.18104 RSF1-IT1 . . . RSF1 intronic transcript 1 . . . . . . . . . . . RSF1-IT2 . . . RSF1 intronic transcript 2 . . . . . . . . . . . RSG1 1.08197156167219e-06 0.104062182706987 0.895936735321451 REM2 and RAB like small GTPase 1 FUNCTION: Potential effector of the planar cell polarity signaling pathway. Plays a role in targeted membrane trafficking most probably at the level of vesicle fusion with membranes. Involved in cilium biogenesis by regulating the transport of cargo proteins to the basal body and to the apical tips of cilia. More generally involved in exocytosis in secretory cells (By similarity). {ECO:0000250}.; . . . . 0.08558 0.10190 -0.115612493 45.12856806 47.84625 1.34321 RSL1D1 0.000364294182041933 0.953224039579425 0.046411666238533 ribosomal L1 domain containing 1 FUNCTION: Regulates cellular senescence through inhibition of PTEN translation. Acts as a pro-apoptotic regulator in response to DNA damage. {ECO:0000269|PubMed:18678645, ECO:0000269|PubMed:22419112}.; . TISSUE SPECIFICITY: Expressed at high intensities in the heart, skeletal muscle, and placenta. {ECO:0000269|PubMed:18678645, ECO:0000269|PubMed:9859858}.; myocardium;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;brain;bladder;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta; superior cervical ganglion; 0.81838 0.09725 -0.110153916 45.48832272 96.88278 2.12759 RSL24D1 0.946909507265446 0.0529101147101083 0.000180378024445716 ribosomal L24 domain containing 1 FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. Ensures the docking of GTPBP4/NOG1 to pre-60S particles (By similarity). {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;aorta;peripheral nerve;thymus; tumor;trigeminal ganglion; 0.53977 0.11809 -0.119252484 44.53880632 22.31869 0.74947 RSL24D1P1 . . . ribosomal L24 domain containing 1 pseudogene 1 . . . . . . . . . . . RSL24D1P2 . . . ribosomal L24 domain containing 1 pseudogene 2 . . . . . . . . . . . RSL24D1P3 . . . ribosomal L24 domain containing 1 pseudogene 3 . . . . . . . . . . . RSL24D1P4 . . . ribosomal L24 domain containing 1 pseudogene 4 . . . . . . . . . . . RSL24D1P5 . . . ribosomal L24 domain containing 1 pseudogene 5 . . . . . . . . . . . RSL24D1P6 . . . ribosomal L24 domain containing 1 pseudogene 6 . . . . . . . . . . . RSL24D1P7 . . . ribosomal L24 domain containing 1 pseudogene 7 . . . . . . . . . . . RSL24D1P8 . . . ribosomal L24 domain containing 1 pseudogene 8 . . . . . . . . . . . RSL24D1P9 . . . ribosomal L24 domain containing 1 pseudogene 9 . . . . . . . . . . . RSL24D1P10 . . . ribosomal L24 domain containing 1 pseudogene 10 . . . . . . . . . . . RSL24D1P11 . . . ribosomal L24 domain containing 1 pseudogene 11 . . . . . . . . . . . RSPH1 0.000210570388617988 0.908975753128566 0.0908136764828157 radial spoke head 1 homolog (Chlamydomonas) FUNCTION: May play an important role in male meiosis (By similarity). It is necessary for proper building of the axonemal central pair and radial spokes. {ECO:0000250, ECO:0000269|PubMed:23993197}.; . TISSUE SPECIFICITY: Expressed in trachea, lungs, airway brushings, and testes. {ECO:0000269|PubMed:23993197}.; unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;skin;uterus;prostate;lung;endometrium;thyroid;placenta;visual apparatus;liver;testis;kidney;brain;bladder;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05122 0.09511 0.488730112 79.52347252 377.25887 4.09598 RSPH3 0.00139623159251261 0.997081503003038 0.00152226540444903 radial spoke 3 homolog (Chlamydomonas) FUNCTION: Functions as a protein kinase A-anchoring protein that scaffolds the cAMP-dependent protein kinase holoenzyme. May serve as a point of convergence for MAPK and PKA signaling in cilia. {ECO:0000269|PubMed:19684019}.; DISEASE: Ciliary dyskinesia, primary, 32 (CILD32) [MIM:616481]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia. {ECO:0000269|PubMed:26073779}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);medulla oblongata;lymph node;islets of Langerhans;colon;retina;uterus;lung;whole body;frontal lobe;cochlea;cerebral cortex;gum;bone;hippocampus;pituitary gland;testis;kidney;brain; testis - interstitial;testis - seminiferous tubule;testis; 0.06647 0.07243 1.159254003 92.6279783 5925.68431 15.98478 RSPH4A 1.84090351392863e-07 0.864278395289755 0.135721420619894 radial spoke head 4 homolog A (Chlamydomonas) FUNCTION: Probable component of the axonemal radial spoke head. Radial spokes are regularly spaced along cilia, sperm and flagella axonemes. They consist of a thin stalk which is attached to a subfiber of the outer doublet microtubule, and a bulbous head which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. {ECO:0000269|PubMed:19200523}.; . TISSUE SPECIFICITY: Expressed in trachea, lungs, and testes. Very strong expression is detected in nasal brushings. {ECO:0000269|PubMed:23993197}.; unclassifiable (Anatomical System);pancreas;lung;nasopharynx;pituitary gland;testis;spleen;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11012 . 0.824892996 88.06912008 3265.43988 10.91021 RSPH6A 2.54884442731765e-08 0.47101399617466 0.528985978336896 radial spoke head 6 homolog A (Chlamydomonas) . . . testis; testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.07190 . -1.056370776 7.578438311 752.26224 5.43990 RSPH9 0.00490037811031499 0.883577560608779 0.111522061280906 radial spoke head 9 homolog (Chlamydomonas) FUNCTION: Probable component of the axonemal radial spoke head. Radial spokes are regularly spaced along cilia, sperm and flagella axonemes. They consist of a thin stalk, which is attached to a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. {ECO:0000269|PubMed:19200523}.; DISEASE: Ciliary dyskinesia, primary, 12 (CILD12) [MIM:612650]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit situs inversus, due to dysfunction of monocilia at the embryonic node and randomization of left-right body asymmetry. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:19200523}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.19322 . -0.137658575 43.57159707 1276.17135 6.72440 RSPH10B . . . radial spoke head 10 homolog B (Chlamydomonas) . . . unclassifiable (Anatomical System);endometrium;thyroid;placenta;adrenal medulla;testis;retina; . 0.08378 . . . 685.80127 5.22908 RSPH10B2 . . . radial spoke head 10 homolog B2 (Chlamydomonas) . . . unclassifiable (Anatomical System);lung;endometrium;thyroid;placenta;adrenal medulla;testis;retina; . . . . . 967.79555 6.01483 RSPH14 . . . radial spoke head 14 homolog . . TISSUE SPECIFICITY: Expressed in adult cerebellum, spinal cord, spleen, skeletal muscle and some/5 out of 9 rhabdoid tumors. Detected in fetal brain, lung, liver and kidney. {ECO:0000269|PubMed:10607907}.; . . 0.07670 0.10678 0.887394731 89.18966737 . . RSPO1 0.00291051404723573 0.80773018363853 0.189359302314234 R-spondin 1 FUNCTION: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Acts as a ligand for frizzled FZD8 and LRP6. May negatively regulate the TGF-beta pathway. Has a essential roles in ovary determination. {ECO:0000269|PubMed:16109882, ECO:0000269|PubMed:21727895, ECO:0000269|PubMed:21909076, ECO:0000269|PubMed:22575959, ECO:0000269|PubMed:22615920, ECO:0000269|PubMed:22815884, ECO:0000269|PubMed:23756652, ECO:0000269|PubMed:23809763}.; DISEASE: Keratoderma, palmoplantar, with squamous cell carcinoma of skin and sex reversal (PKKSCC) [MIM:610644]: A recessive syndrome characterized by XX (female to male) SRY-independent sex reversal, palmoplantar hyperkeratosis and predisposition to squamous cell carcinoma of the skin. {ECO:0000269|PubMed:17041600}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Abundantly expressed in adrenal glands, ovary, testis, thyroid and trachea but not in bone marrow, spinal cord, stomach, leukocytes colon, small intestine, prostate, thymus and spleen. {ECO:0000269|PubMed:17041600}.; unclassifiable (Anatomical System);uterus;cartilage;ovary;heart;placenta;parathyroid;lens;skin; . 0.26089 0.17014 0.17280645 65.75843359 511.03533 4.62987 RSPO2 0.691140450045943 0.308011963429985 0.000847586524071722 R-spondin 2 FUNCTION: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Probably also acts as a ligand for frizzled and LRP receptors. {ECO:0000269|PubMed:21727895, ECO:0000269|PubMed:21909076, ECO:0000269|PubMed:22615920}.; . . unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;optic nerve;whole body;lung;frontal lobe;cochlea;macula lutea;pituitary gland;testis;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.29372 0.11139 -0.005381972 53.50908233 4896.56308 14.23857 RSPO3 0.043976319489366 0.950321169854479 0.00570251065615442 R-spondin 3 FUNCTION: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Acts as a ligand for frizzled FZD8 and LRP6. May negatively regulate the TGF-beta pathway. {ECO:0000269|PubMed:21727895, ECO:0000269|PubMed:21909076, ECO:0000269|PubMed:22615920}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at higher level in placenta, small intestine, fetal thymus and lymph node. {ECO:0000269|PubMed:12463421}.; unclassifiable (Anatomical System);smooth muscle;heart;ovary;developmental;colon;parathyroid;skin;uterus;prostate;lung;endometrium;placenta;hippocampus;liver;testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;cerebellum; 0.19799 0.11476 -0.139478553 43.29440906 16.02879 0.56706 RSPO4 0.000413043495572724 0.640387847314936 0.359199109189491 R-spondin 4 FUNCTION: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. {ECO:0000269|PubMed:21727895, ECO:0000269|PubMed:21909076}.; DISEASE: Nail disorder, non-syndromic congenital, 4 (NDNC4) [MIM:206800]: A nail disorder characterized by congenital anonychia or its milder phenotypic variant hyponychia. Anonychia/hyponychia is the absence or severe hypoplasia of all fingernails and toenails without significant bone anomalies. {ECO:0000269|PubMed:17041604}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . optic nerve;cartilage;ovary;macula lutea;visual apparatus;testis;fovea centralis;choroid;kidney;lens;retina; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.19936 0.13751 0.306902668 72.38145789 273.02646 3.54258 RSPRY1 0.999778005187676 0.000221994542014576 2.70309585235213e-10 ring finger and SPRY domain containing 1 . . . . . 0.39568 . -0.293801652 32.93819297 46.0784 1.30796 RSRC1 3.41025677860813e-05 0.944271149268061 0.0556947481641533 arginine/serine-rich coiled-coil 1 FUNCTION: Plays a role in pre-mRNA splicing. Involved in both constitutive and alternative pre-mRNA splicing. May have a role in the recognition of the 3' splice site during the second step of splicing. {ECO:0000269|PubMed:15798186}.; . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;frontal lobe;oesophagus;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;visual apparatus;liver;kidney;stomach; dorsal root ganglion;globus pallidus;trigeminal ganglion; 0.37921 0.10562 -0.337894035 30.37272942 49.35023 1.37479 RSRC2 0.992877361426345 0.00712258640124426 5.21724106633305e-08 arginine/serine-rich coiled-coil 2 . . . myocardium;lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;amnion;head and neck;kidney;stomach; amygdala;testis - interstitial;medulla oblongata;superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;parietal lobe; 0.32804 0.10857 -0.317668748 31.45789101 11.17377 0.40392 RSRP1 . . . arginine/serine-rich protein 1 . . . . . 0.07419 0.08336 0.905808022 89.4373673 . . RSS . . . Russell Silver syndrome . . . . . . . . . . . RSU1 0.0477656793520055 0.92857797200826 0.0236563486397348 Ras suppressor protein 1 FUNCTION: Potentially plays a role in the Ras signal transduction pathway. Capable of suppressing v-Ras transformation in vitro.; . . ovary;sympathetic chain;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;pineal gland;artery;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;adipose tissue;temporal lobe;pons;atrioventricular node;skeletal muscle;skin;subthalamic nucleus;testis - seminiferous tubule;placenta;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.19291 0.13264 -0.381986487 27.68931352 254.93131 3.43401 RSU1P1 . . . Ras suppressor protein 1 pseudogene 1 . . . . . . . . . . . RSU1P2 . . . Ras suppressor protein 1 pseudogene 2 . . . . . . . . . . . RSU1P3 . . . Ras suppressor protein 1 pseudogene 3 . . . . . . . . . . . RTBDN 3.27850963623921e-07 0.183963056482114 0.816036615666922 retbindin . . TISSUE SPECIFICITY: Expressed in retina.; unclassifiable (Anatomical System);choroid;fovea centralis;retina;bile duct;lung;optic nerve;bone;visual apparatus;macula lutea;liver;pineal gland;brain; superior cervical ganglion;pancreas;atrioventricular node;pons; 0.12374 0.09639 0.106667882 61.73036093 240.14561 3.34772 RTCA 0.00292097800955511 0.984585599429831 0.0124934225606142 RNA 3'-terminal phosphate cyclase FUNCTION: Catalyzes the conversion of 3'-phosphate to a 2',3'- cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA- N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'- phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.16113 0.26878 0.373041938 75.29488087 118.74232 2.37056 RTCA-AS1 . . . RTCA antisense RNA 1 . . . . . . . . . . . RTCB 0.0587292330087026 0.940528075422471 0.000742691568826797 RNA 2',3'-cyclic phosphate and 5'-OH ligase FUNCTION: Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'- phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs. {ECO:0000269|PubMed:21311021, ECO:0000269|PubMed:24870230}.; . . . . 0.13725 0.18224 -0.80269335 12.23755603 1426.79693 7.05638 RTEL1 0.777758475451746 0.22224152436455 1.83703998441753e-10 regulator of telomere elongation helicase 1 FUNCTION: ATP-dependent DNA helicase implicated in telomere-length regulation, DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates. Also disassembles T loops and prevents telomere fragility by counteracting telomeric G4-DNA structures, which together ensure the dynamics and stability of the telomere. {ECO:0000255|HAMAP- Rule:MF_03065, ECO:0000269|PubMed:18957201, ECO:0000269|PubMed:23453664, ECO:0000269|PubMed:24009516}.; DISEASE: Dyskeratosis congenita, autosomal recessive, 5 (DKCB5) [MIM:615190]: A form of dyskeratosis congenita, a rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy. DKCB5 is characterized by onset of bone marrow failure and immunodeficiency in early childhood. Most patients also have growth and developmental delay and cerebellar hypoplasia, consistent with a clinical diagnosis of Hoyeraal-Hreidarsson syndrome. {ECO:0000269|PubMed:23329068, ECO:0000269|PubMed:23453664, ECO:0000269|PubMed:23591994, ECO:0000269|PubMed:23959892, ECO:0000269|PubMed:24009516}. Note=The disease is caused by mutations affecting the gene represented in this entry. RTEL1 mutations have also been found in patients with a dyskeratosis congenita-like phenotype consisting of one feature of dyskeratosis congenita and short telomeres, in the absence of the typical DKC diagnostic triad (PubMed:23329068). {ECO:0000269|PubMed:23329068}.; DISEASE: Dyskeratosis congenita, autosomal dominant, 4 (DKCA4) [MIM:615190]: A rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy. {ECO:0000269|PubMed:23329068}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pulmonary fibrosis, and/or bone marrow failure, telomere- related, 3 (PFBMFT3) [MIM:616373]: A disease associated with shortened telomeres. Pulmonary fibrosis is the most common manifestation. Other manifestations include aplastic anemia due to bone marrow failure, hepatic fibrosis, and increased cancer risk, particularly myelodysplastic syndrome and acute myeloid leukemia. Phenotype, age at onset, and severity are determined by telomere length. {ECO:0000269|PubMed:25848748}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . 0.16864 -2.481161548 0.949516395 1308.22688 6.80132 RTEL1-TNFRSF6B . . . RTEL1-TNFRSF6B readthrough (NMD candidate) . . . . . . . . . . . RTEL1P1 . . . regulator of telomere elongation helicase 1 pseudogene 1 . . . . . . . . . . . RTF1 0.993637763534383 0.00636222845566554 8.00995132985629e-09 RTF1 homolog, Paf1/RNA polymerase II complex component FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non- phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Binds single-stranded DNA. Required for maximal induction of heat-shock genes. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of a SET1 complex (By similarity). {ECO:0000250, ECO:0000269|PubMed:19345177, ECO:0000269|PubMed:20178742}.; . . . . 0.65572 0.14229 -0.339715008 30.06605331 27.36211 0.88156 RTFDC1 0.00393227636872296 0.95834319336826 0.0377245302630173 replication termination factor 2 domain containing 1 . . . . . 0.09313 0.09233 -0.359940251 28.93371078 40.98664 1.20095 RTKN 0.000149538066738097 0.992324330747225 0.00752613118603737 rhotekin FUNCTION: Mediates Rho signaling to activate NF-kappa-B and may confer increased resistance to apoptosis to cells in gastric tumorigenesis. May play a novel role in the organization of septin structures. {ECO:0000269|PubMed:10940294, ECO:0000269|PubMed:15480428, ECO:0000269|PubMed:16007136}.; . TISSUE SPECIFICITY: Highly expressed in prostate, moderately in kidney, heart, brain, spleen, testis, placenta, small intestine, pancreas, skeletal muscle and peripheral blood leukocytes, and weakly in ovary, colon and thymus. Weakly expressed in all normal cell lines tested. Overexpressed in various cancer cell lines. {ECO:0000269|PubMed:10873388, ECO:0000269|PubMed:15480428}.; smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;liver;hypopharynx;cervix;spleen;head and neck;kidney;mammary gland;stomach; . 0.16440 0.10277 -0.841329384 11.36470866 111.05692 2.29721 RTKN2 1.30976541627025e-14 0.0818261365503177 0.918173863449669 rhotekin 2 FUNCTION: May play an important role in lymphopoiesis. {ECO:0000269|PubMed:15504364}.; . TISSUE SPECIFICITY: Expressed in lymphocytes, CD4 positive T-cells and bone marrow-derived cells. Also expressed in lung, colon, thymus and brain. {ECO:0000269|PubMed:15504364}.; unclassifiable (Anatomical System);placenta;testis; testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.10573 0.09109 -0.066061882 48.77919321 2418.31095 9.14018 RTL1 0.00816648413128806 0.98894781995481 0.0028856959139022 retrotransposon-like 1 FUNCTION: Plays an essential role in capillaries endothelial cells for the maintenance of feto-maternal interface and for development of the placenta. {ECO:0000250}.; . . . . 0.22864 0.13929 0.334405942 73.64944562 3311.20848 10.98757 RTN1 0.959599485657203 0.0403819736353317 1.85407074649683e-05 reticulon 1 FUNCTION: May be involved in neuroendocrine secretion or in membrane trafficking in neuroendocrine cells.; . TISSUE SPECIFICITY: Expressed in neural and neuroendocrine tissues and cell cultures derived therefrom. Expression of isoform RTN1-C is strongly correlated with neuronal differentiation. {ECO:0000269|PubMed:9560466}.; ovary;sympathetic chain;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;pituitary gland;testis;brain;gall bladder;amygdala;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;lens;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;mammary gland;cerebellum; whole brain;amygdala;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.50683 0.11839 0.134171522 63.57041755 571.10507 4.84873 RTN2 0.636179982447555 0.363808153026566 1.18645258788542e-05 reticulon 2 . . TISSUE SPECIFICITY: Isoform RTN2-C is highly expressed in skeletal muscle. {ECO:0000269|PubMed:9693037}.; lymphoreticular;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;whole body;optic nerve;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;macula lutea;kidney;mammary gland;stomach; amygdala;whole brain;medulla oblongata;occipital lobe;temporal lobe;prefrontal cortex;caudate nucleus;parietal lobe;cingulate cortex;skeletal muscle; 0.58971 . -0.200157416 39.11299835 92.63069 2.06891 RTN3 0.0400228226482246 0.958627886917488 0.0013492904342877 reticulon 3 FUNCTION: May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress. In case of enteroviruses infection, RTN3 may be involved in the viral replication or pathogenesis. {ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:16054885, ECO:0000269|PubMed:17031492, ECO:0000269|PubMed:17191123}.; . TISSUE SPECIFICITY: Isoform 3 is widely expressed, with highest levels in brain, where it is enriched in neuronal cell bodies from gray matter (at protein level). Three times more abundant in macula than in peripheral retina. Isoform 1 is expressed at high levels in brain and at low levels in skeletal muscle. Isoform 2 is only found in melanoma. {ECO:0000269|PubMed:10331947, ECO:0000269|PubMed:12811824, ECO:0000269|PubMed:14986927, ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:15946766}.; smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;germinal center;bladder;brain;amygdala;heart;tongue;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;cerebral cortex;larynx;bone;pituitary gland;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;pia mater;mesenchyma;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;cerebellum; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.36858 0.09681 -0.837696902 11.45317292 679.02923 5.21062 RTN3P1 . . . reticulon 3 pseudogene 1 . . . . . . . . . . . RTN4 0.0108353564169536 0.987249940600313 0.00191470298273314 reticulon 4 FUNCTION: Developmental neurite growth regulatory factor with a role as a negative regulator of axon-axon adhesion and growth, and as a facilitator of neurite branching. Regulates neurite fasciculation, branching and extension in the developing nervous system. Involved in down-regulation of growth, stabilization of wiring and restriction of plasticity in the adult CNS. Regulates the radial migration of cortical neurons via an RTN4R-LINGO1 containing receptor complex (By similarity). Isoform 2 reduces the anti-apoptotic activity of Bcl-xl and Bcl-2. This is likely consecutive to their change in subcellular location, from the mitochondria to the endoplasmic reticulum, after binding and sequestration. Isoform 2 and isoform 3 inhibit BACE1 activity and amyloid precursor protein processing. {ECO:0000250, ECO:0000269|PubMed:10667797, ECO:0000269|PubMed:11201742, ECO:0000269|PubMed:16965550}.; . TISSUE SPECIFICITY: Isoform 1 is specifically expressed in brain and testis and weakly in heart and skeletal muscle. Isoform 2 is widely expressed except for the liver. Isoform 3 is expressed in brain, skeletal muscle and adipocytes. Isoform 4 is testis- specific.; ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;whole body;ganglion;frontal lobe;cochlea;endometrium;larynx;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;alveolus;hypopharynx;liver;spleen;head and neck;cervix;kidney;aorta;stomach;peripheral nerve; amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;adipose tissue;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.40708 0.23501 1.850110669 97.13375796 1450.14696 7.10628 RTN4IP1 3.75201094361177e-06 0.813550445602158 0.186445802386898 reticulon 4 interacting protein 1 FUNCTION: Appears to be a potent inhibitor of regeneration following spinal cord injury.; . TISSUE SPECIFICITY: Widely expressed in mitochondria-enriched tissues. Found in heart, muscle, kidney, liver, brain and placenta. {ECO:0000269|PubMed:12067236}.; . . 0.05981 0.09264 -0.490397599 22.50530786 43.55625 1.25605 RTN4R 0.526443417823064 0.457338899987706 0.0162176821892297 reticulon 4 receptor FUNCTION: Receptor for RTN4, OMG and MAG. Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton. Mediates axonal growth inhibition and may play a role in regulating axonal regeneration and plasticity in the adult central nervous system. Acts in conjunction with RTN4 and LINGO1 in regulating neuronal precursor cell motility during cortical development. {ECO:0000250|UniProtKB:Q99PI8, ECO:0000269|PubMed:12037567, ECO:0000269|PubMed:14966521}.; . TISSUE SPECIFICITY: Widespread in the brain but highest levels in the gray matter. Low levels in heart and kidney not expressed in oligodendrocytes (white matter).; unclassifiable (Anatomical System);lymph node;ovary;colon;parathyroid;fovea centralis;choroid;lens;retina;uterus;optic nerve;whole body;lung;placenta;thyroid;macula lutea;visual apparatus;testis;cervix;kidney;brain;stomach; . 0.23327 0.21581 -1.089312628 7.047652748 . . RTN4RL1 0.787530525426807 0.206025151258865 0.00644432331432755 reticulon 4 receptor-like 1 FUNCTION: May play a role in regulating axonal regeneration and plasticity in the adult central nervous system. {ECO:0000303|PubMed:14664809}.; . TISSUE SPECIFICITY: Predominantly expressed in brain. Expressed at lower levels in kidney, lung, mammary gland, placenta, salivary gland, skeletal muscle and spleen. {ECO:0000269|PubMed:12694398, ECO:0000269|PubMed:14664809}.; brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.54411 0.11622 0.398725314 76.35645199 152.13717 2.69763 RTN4RL2 0.975814588290454 0.024159815985314 2.55957242323499e-05 reticulon 4 receptor-like 2 FUNCTION: May play a role in regulating axonal regeneration and plasticity in the adult central nervous system. {ECO:0000303|PubMed:14664809}.; . TISSUE SPECIFICITY: Highly expressed in brain and liver. Expressed at lower levels in kidney, mammary gland, placenta, skeletal muscle, spleen and thyroid. {ECO:0000269|PubMed:12694398, ECO:0000269|PubMed:14664809}.; unclassifiable (Anatomical System);frontal lobe;ovary;bone;placenta;hippocampus;colon;kidney;brain; superior cervical ganglion; 0.28156 0.11579 . . 40.58676 1.18984 RTP1 0.56382972565799 0.423951854337294 0.0122184200047157 receptor (chemosensory) transporter protein 1 FUNCTION: Specifically promotes functional cell surface expression of olfactory receptors, but not of other GPCRs. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:16720576}.; lung;hypothalamus;testis;brain; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;uterus corpus;temporal lobe;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.79035 0.11684 0.064394823 58.84642604 2341.27335 8.96348 RTP2 0.00338105493146928 0.612292667804584 0.384326277263946 receptor (chemosensory) transporter protein 2 FUNCTION: Specifically promotes functional cell surface expression of olfactory receptors, but not of other GPCRs. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in circumvallate papillae and testis. {ECO:0000269|PubMed:16720576}.; unclassifiable (Anatomical System);salivary gland;testis; . 0.18955 0.10985 0.238945317 69.20853975 3613.00534 11.63896 RTP3 0.181516461400941 0.765413316390433 0.0530702222086256 receptor (chemosensory) transporter protein 3 FUNCTION: Promotes functional cell surface expression of the bitter taste receptors TAS2R16 and TAS2R43. {ECO:0000269|PubMed:16720576}.; . TISSUE SPECIFICITY: Expressed predominantly in adult liver (PubMed:11896456, PubMed:17693185). Expressed in testis (PubMed:16720576, PubMed:17693185). Also expressed in kidney, lung and fetal liver (PubMed:17693185). Low levels in heart, thyroid, adrenal gland, pancreas, ovary, prostate, skin, plasma leukocytes, bone marrow and fetal brain (PubMed:17693185). Not detected in brain, spleen, colon, small intestine, skeletal muscle, stomach, placenta, salivary gland and uterus (PubMed:17693185). {ECO:0000269|PubMed:11896456, ECO:0000269|PubMed:16720576, ECO:0000269|PubMed:17693185}.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;liver; 0.04231 0.07119 -0.029247611 51.40363293 6 0.22513 RTP4 0.0108456456084385 0.835465726928449 0.153688627463112 receptor (chemosensory) transporter protein 4 FUNCTION: Probable chaperone protein which facilitates trafficking and functional cell surface expression of some G-protein coupled receptors (GPCRs). Promotes functional expression of the bitter taste receptor TAS2R16 (PubMed:16720576). Also promotes functional expression of the opioid receptor heterodimer OPRD1-OPRM1 (By similarity). {ECO:0000250|UniProtKB:Q9ER80, ECO:0000269|PubMed:16720576}.; . TISSUE SPECIFICITY: Expressed in circumvallate papillae and testis. {ECO:0000269|PubMed:16720576}.; unclassifiable (Anatomical System);lymph node;cartilage;spinal cord;colon;skin;breast;uterus;bile duct;prostate;pancreas;lung;endometrium;larynx;nasopharynx;bone;liver;testis;head and neck;spleen;kidney;bladder; . 0.05072 0.07309 1.350418743 94.35008257 2744.58435 9.87696 RTP5 . . . receptor (chemosensory) transporter protein 5 (putative) . . . . . . . 0.736704836 86.32932295 . . RTTN 2.40394270810394e-13 0.999999994034628 5.96513180225979e-09 rotatin FUNCTION: Involved in the genetic cascade that governs left-right specification. Plays a role in the maintenance of a normal ciliary structure. Required for correct asymmetric expression of NODAL, LEFTY and PITX2. {ECO:0000269|PubMed:22939636}.; DISEASE: Polymicrogyria with seizures (PMGYS) [MIM:614833]: A disease characterized by many irregular small gyri in the brain surface and fusion of the molecular layer over multiple small gyri, which gives a festooned appearance to the cortical surface, without abnormal neuronal migration. Polymicrogyria is a heterogeneous disorder, considered to be the result of postmigratory abnormal cortical organization. PMGYS patients have moderate to severe mental retardation, poor speech, dysarthria and seizures. {ECO:0000269|PubMed:22939636}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney; dorsal root ganglion;superior cervical ganglion;testis - interstitial;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.25498 0.10307 0.18719002 66.27742392 829.75241 5.64516 RUBCN . . . RUN and cysteine rich domain containing beclin 1 interacting protein FUNCTION: Inhibits PIK3C3 activity; under basal conditions negatively regulates PI3K complex II (PI3KC3-C2) function in autophagy. Negatively regulates endosome maturation and degradative endocytic trafficking and impairs autophagosome maturation process. Can sequester UVRAG from association with a class C Vps complex (possibly the HOPS complex) and negatively regulates Rab7 activation (PubMed:20974968, PubMed:21062745). {ECO:0000269|PubMed:20974968, ECO:0000269|PubMed:21062745}.; DISEASE: Spinocerebellar ataxia, autosomal recessive, 15 (SCAR15) [MIM:615705]: Spinocerebellar ataxia defines a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR15 patients manifest cerebellar ataxia in early childhood and delayed motor development with delayed walking. Additional features include dysarthria, upper limb involvement, abnormal eye movements, and hyporeflexia. {ECO:0000269|PubMed:20826435}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.18496 0.09999 0.431697208 77.32955886 . . RUFY1 0.0646702146609533 0.935303663176112 2.61221629343127e-05 RUN and FYVE domain containing 1 FUNCTION: Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in early endosomal trafficking. {ECO:0000269|PubMed:14617813}.; . TISSUE SPECIFICITY: Broadly expressed, with highest levels in lung, testis, kidney and brain. {ECO:0000269|PubMed:11877430}.; ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;cerebellum cortex;islets of Langerhans;muscle;adrenal cortex;blood;skeletal muscle;breast;lung;placenta;visual apparatus;hippocampus;liver;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;trigeminal ganglion; 0.24529 . -0.488577883 22.64685067 95.63276 2.11203 RUFY2 0.416574096064703 0.583423085032644 2.81890265256113e-06 RUN and FYVE domain containing 2 . . TISSUE SPECIFICITY: Expressed in brain, lung and testis. {ECO:0000269|PubMed:11877430}.; ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;head and neck;cervix;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13637 0.09918 -0.22584292 37.32012267 69.4068 1.72828 RUFY3 0.980976378677518 0.019023597532099 2.37903828229472e-08 RUN and FYVE domain containing 3 FUNCTION: Plays a role in the generation of neuronal polarity formation and axon growth (By similarity). Implicated in the formation of a single axon by developing neurons (By similarity). May inhibit the formation of additional axons by inhibition of PI3K in minor neuronal processes (By similarity). Plays a role in the formation of F-actin-enriched protrusive structures at the cell periphery (PubMed:25766321). Plays a role in cytoskeletal organization by regulating the subcellular localization of FSCN1 and DBN1 at axonal growth cones (By similarity). Promotes gastric cancer cell migration and invasion in a PAK1-dependent manner (PubMed:25766321). {ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000250|UniProtKB:Q9D394, ECO:0000269|PubMed:25766321}.; . TISSUE SPECIFICITY: Overexpressed in gastric cancer cells and tissues (at protein level) (PubMed:25766321). {ECO:0000269|PubMed:25766321}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;lacrimal gland;tongue;islets of Langerhans;spinal cord;lens;skeletal muscle;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach; amygdala;whole brain;superior cervical ganglion;testis - interstitial;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;skin;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;pituitary; 0.86149 0.08400 -0.844966979 11.1759849 66.52798 1.68028 RUFY4 4.87589210961602e-09 0.0605722835318576 0.93942771159225 RUN and FYVE domain containing 4 . . . unclassifiable (Anatomical System);uterus;ovary;brain; . 0.03108 . . . 405.4648 4.22210 RUNDC1 0.0189204905991752 0.961389732861583 0.0196897765392418 RUN domain containing 1 FUNCTION: May play a role as p53/TP53 inhibitor and thus may have oncogenic activity. {ECO:0000269|PubMed:16929179}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;pharynx;blood;breast;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;cerebellum; 0.18499 . -0.558357437 19.54470394 278.48435 3.57685 RUNDC3A 0.960334019427912 0.0395788228131567 8.71577589316135e-05 RUN domain containing 3A FUNCTION: May act as an effector of RAP2A in neuronal cells. {ECO:0000250}.; . . unclassifiable (Anatomical System);prostate;lung;islets of Langerhans;hypothalamus;hippocampus;urinary;pituitary gland;liver;testis;spleen;brain;cerebellum; amygdala;whole brain;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.33264 0.10493 -0.317668748 31.45789101 61.44446 1.59770 RUNDC3A-AS1 . . . RUNDC3A antisense RNA 1 . . . . . . . . . . . RUNDC3B 0.00149189416804701 0.991756450160592 0.0067516556713612 RUN domain containing 3B . . TISSUE SPECIFICITY: Isoform 2 is expressed at high levels in brain, thymus, ovary, testis, leukocyte, liver, small intestine and prostate. Isoform 1 is expressed in the brain, testis and adrenal gland. It is activated in tumorigenic breast cancer cell lines and in the primary tumor of breast cancer patients. Activation also correlates with metastatic lymph node invasion and can be detected in metastatic epithelial cells from the lymph nodes and in the bone marrow of patients. {ECO:0000269|PubMed:12645870, ECO:0000269|PubMed:15986426}.; unclassifiable (Anatomical System);prostate;endometrium;hypothalamus;colon;brain;retina; amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;cerebellum peduncles;temporal lobe;atrioventricular node;skeletal muscle;fetal brain;adrenal gland;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.14292 0.10936 -0.516085732 21.20193442 38.89024 1.15204 RUNX1 0.449323606506754 0.54937349793652 0.00130289555672611 runt related transcription factor 1 FUNCTION: CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL-3 and GM-CSF promoters. The alpha subunit binds DNA and appears to have a role in the development of normal hematopoiesis. Isoform AML-1L interferes with the transactivation activity of RUNX1. Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the mouse BLK promoter. Inhibits KAT6B- dependent transcriptional activation. Controls the anergy and suppressive function of regulatory T-cells (Treg) by associating with FOXP3. Activates the expression of IL2 and IFNG and down- regulates the expression of TNFRSF18, IL2RA and CTLA4, in conventional T-cells (PubMed:17377532). {ECO:0000269|PubMed:10207087, ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:14970218, ECO:0000269|PubMed:17377532, ECO:0000269|PubMed:17431401}.; DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a cause of M2 type acute myeloid leukemia (AML-M2). Translocation t(8;21)(q22;q22) with RUNX1T1.; DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a cause of therapy-related myelodysplastic syndrome (T-MDS). Translocation t(3;21)(q26;q22) with EAP or MECOM.; DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a cause of chronic myelogenous leukemia (CML). Translocation t(3;21)(q26;q22) with EAP or MECOM.; DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is found in childhood acute lymphoblastic leukemia (ALL). Translocation t(12;21)(p13;q22) with TEL. The translocation fuses the 3'-end of TEL to the alternate 5'-exon of AML-1H.; DISEASE: Note=A chromosomal aberration involving RUNX1 is found in acute leukemia. Translocation t(11,21)(q13;q22) that forms a MACROD1-RUNX1 fusion protein.; DISEASE: Familial platelet disorder with associated myeloid malignancy (FPDMM) [MIM:601399]: Autosomal dominant disease characterized by qualitative and quantitative platelet defects, and propensity to develop acute myelogenous leukemia. {ECO:0000269|PubMed:10508512}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is found in therapy-related myeloid malignancies. Translocation t(16;21)(q24;q22) that forms a RUNX1-CBFA2T3 fusion protein.; DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a cause of chronic myelomonocytic leukemia. Inversion inv(21)(q21;q22) with USP16.; TISSUE SPECIFICITY: Expressed in all tissues examined except brain and heart. Highest levels in thymus, bone marrow and peripheral blood.; myocardium;smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;alveolus;liver;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;medulla oblongata;cerebellum peduncles;atrioventricular node;pons;caudate nucleus;skeletal muscle;bone marrow;fetal liver;testis - seminiferous tubule;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.71814 0.72461 -0.227663163 37.11370606 85.67689 1.97553 RUNX1-IT1 . . . RUNX1 intronic transcript 1 . . . . . . . . . . . RUNX1T1 0.999121687972463 0.000878304314984079 7.71255270944827e-09 runt related transcription factor 1; translocated to, 1 (cyclin D related) FUNCTION: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes (PubMed:12559562, PubMed:15203199). Can repress the expression of MMP7 in a ZBTB33-dependent manner (PubMed:23251453). Can repress transactivation mediated by TCF12 (PubMed:16803958). {ECO:0000269|PubMed:10973986, ECO:0000269|PubMed:16803958, ECO:0000269|PubMed:23251453, ECO:0000303|PubMed:12559562, ECO:0000303|PubMed:15203199}.; DISEASE: Note=A chromosomal aberration involving RUNX1T1 is a cause of acute myeloid leukemia (AML-M2). Translocation t(8;21)(q22;q22) with RUNX1/AML1. {ECO:0000269|PubMed:1423235, ECO:0000269|PubMed:7541640, ECO:0000269|PubMed:8334990, ECO:0000269|PubMed:8353289}.; TISSUE SPECIFICITY: Most abundantly expressed in brain. Lower levels in lung, heart, testis and ovary.; unclassifiable (Anatomical System);smooth muscle;heart;ovary;islets of Langerhans;muscle;skin;uterus;pancreas;prostate;whole body;lung;frontal lobe;liver;testis;spleen;brain; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;fetal brain;cerebellum peduncles;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;cerebellum; 0.85092 0.58871 -1.001120478 8.321538099 35.00756 1.06236 RUNX2 0.995958899294884 0.00404078177740098 3.18927715060021e-07 runt related transcription factor 2 FUNCTION: Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis. Essential for the maturation of osteoblasts and both intramembranous and endochondral ossification. CBF binds to the core site, 5'- PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, osteocalcin, osteopontin, bone sialoprotein, alpha 1(I) collagen, LCK, IL-3 and GM-CSF promoters. In osteoblasts, supports transcription activation: synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE) (By similarity). Inhibits KAT6B-dependent transcriptional activation. {ECO:0000250, ECO:0000269|PubMed:11965546}.; DISEASE: Cleidocranial dysplasia (CLCD) [MIM:119600]: Autosomal dominant skeletal disorder with high penetrance and variable expressivity. It is due to defective endochondral and intramembranous bone formation. Typical features include hypoplasia/aplasia of clavicles, patent fontanelles, wormian bones (additional cranial plates caused by abnormal ossification of the calvaria), supernumerary teeth, short stature, and other skeletal changes. In some cases defects in RUNX2 are exclusively associated with dental anomalies. {ECO:0000269|PubMed:10521292, ECO:0000269|PubMed:10545612, ECO:0000269|PubMed:10689183, ECO:0000269|PubMed:10980549, ECO:0000269|PubMed:11857736, ECO:0000269|PubMed:12081718, ECO:0000269|PubMed:12196916, ECO:0000269|PubMed:12424590, ECO:0000269|PubMed:16270353, ECO:0000269|PubMed:19744171, ECO:0000269|PubMed:20082269, ECO:0000269|PubMed:20648631, ECO:0000269|PubMed:9182765, ECO:0000269|PubMed:9207800}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Metaphyseal dysplasia with maxillary hypoplasia with or without brachydactyly (MDMHB) [MIM:156510]: An autosomal dominant bone dysplasia characterized by metaphyseal flaring of long bones, enlargement of the medial halves of the clavicles, maxillary hypoplasia, variable brachydactyly, and dystrophic teeth. {ECO:0000269|PubMed:23290074}. Note=The disease is caused by mutations affecting the gene represented in this entry. Analysis for copy-number variations revealed that a 105 kb duplication within RUNX2 segregated with the MDMHB phenotype in a region with maximum linkage. Real-time PCR for copy-number variation in genomic DNA in eight samples, as well as sequence analysis of fibroblast cDNA from one subject with MDMHB confirmed that affected family members were heterozygous for the presence of an intragenic duplication encompassing exons 3 to 5 of RUNX2. These three exons code for the Q/A domain and the functionally essential DNA-binding Runt domain of RUNX2. The RUNX2 duplication found in individuals with MDMHB leads to a gain of function (PubMed:23290074). {ECO:0000269|PubMed:23290074}.; TISSUE SPECIFICITY: Specifically expressed in osteoblasts.; unclassifiable (Anatomical System);lung;ovary;heart;thyroid;testis;colon;skeletal muscle; testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cerebellum; 0.53349 0.87580 -0.446304853 24.33356924 87.92892 2.00467 RUNX3 0.673967691642928 0.325030542259053 0.00100176609801867 runt related transcription factor 3 FUNCTION: CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, lck, IL-3 and GM-CSF promoters. In association with ZFHX3, upregulates CDKN1A promoter activity following TGF-beta stimulation (PubMed:20599712). {ECO:0000269|PubMed:20599712}.; . TISSUE SPECIFICITY: Expressed in gastric cancer tissues (at protein level). {ECO:0000269|PubMed:20599712}.; unclassifiable (Anatomical System);heart;islets of Langerhans;colon;blood;skin;bone marrow;uterus;prostate;lung;cerebral cortex;placenta;testis;cervix;germinal center;spinal ganglion;stomach; . 0.48027 0.52799 -0.271755481 34.31823543 16.08365 0.56934 RUSC1 0.949429117518656 0.0505695491521111 1.33332923251912e-06 RUN and SH3 domain containing 1 FUNCTION: Putative signaling adapter which may play a role in neuronal differentiation. May be involved in regulation of NGF- dependent neurite outgrowth. Proposed to play a role in neuronal vesicular trafficking, specifically involving pre-synaptic membrane proteins. Seems to be involved in signaling pathways that are regulated by the prolonged activation of MAPK. Can regulate the polyubiquitination of IKBKG and thus may be involved in regulation of the NF-kappa-B pathway. {ECO:0000269|PubMed:19365808}.; . TISSUE SPECIFICITY: Predominantly expressed in brain.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;uterus;prostate;frontal lobe;cochlea;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;bile duct;pancreas;lung;cornea;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;amygdala;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.16506 0.10444 -0.398573136 26.92852088 572.82198 4.85892 RUSC1-AS1 . . . RUSC1 antisense RNA 1 . . . . . . . . . . . RUSC2 0.999977319884014 2.26801159434183e-05 4.27318152841765e-14 RUN and SH3 domain containing 2 . . TISSUE SPECIFICITY: Widely expressed, with highest levels in brain and testis. {ECO:0000269|PubMed:15796781}.; medulla oblongata;ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;nervous;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach; amygdala;whole brain;testis - interstitial;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;cerebellum peduncles;temporal lobe;pons;subthalamic nucleus;fetal brain;prefrontal cortex;testis;globus pallidus;cingulate cortex;cerebellum; 0.12331 0.09447 -2.09468547 1.556970984 476.30396 4.50842 RUVBL1 0.998897690232788 0.00110229635066796 1.3416543683851e-08 RuvB like AAA ATPase 1 FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP- dependent DNA helicase (3' to 5') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity.; FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.; FUNCTION: May be able to bind plasminogen at cell surface and enhance plasminogen activation.; . TISSUE SPECIFICITY: Ubiquitously expressed with high expression in heart, skeletal muscle and testis.; myocardium;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; superior cervical ganglion;tumor;testis;trigeminal ganglion; 0.86256 0.38765 -0.560178693 19.30879925 3.63734 0.13372 RUVBL1-AS1 . . . RUVBL1 antisense RNA 1 . . . . . . . . . . . RUVBL2 0.999110080217839 0.000889911818837068 7.96332396968843e-09 RuvB like AAA ATPase 2 FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP- dependent DNA helicase (5' to 3') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity.; FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.; FUNCTION: Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway where it negatively regulates expression of ER stress response genes. {ECO:0000269|PubMed:25652260}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in testis and thymus.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;pituitary gland;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;muscle;adrenal cortex;pharynx;blood;breast;pancreas;lung;adrenal gland;epididymis;placenta;visual apparatus;duodenum;liver;cervix;spleen;kidney;mammary gland;stomach; amygdala;whole brain;testis - interstitial;lung;testis - seminiferous tubule;liver;testis;tumor;thymus; 0.60957 0.54626 -1.023168368 7.944090587 19.53697 0.67025 RWDD1 0.372943967483844 0.615939047620118 0.0111169848960385 RWD domain containing 1 FUNCTION: Protects DRG2 from proteolytic degradation. {ECO:0000250}.; . . . . 0.24516 0.11809 -0.141298762 42.87567823 22.27519 0.74657 RWDD1P1 . . . RWD domain containing 1 pseudogene 1 . . . . . . . . . . . RWDD1P3 . . . RWD domain containing 1 pseudogene 3 . . . . . . . . . . . RWDD2A 0.000931281554491641 0.574685307176305 0.424383411269203 RWD domain containing 2A . . . . . 0.33139 . -0.09720619 46.20193442 12.45391 0.45245 RWDD2B 0.000174917032865459 0.695085304044542 0.304739778922593 RWD domain containing 2B . . TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;aorta;stomach; . 0.06753 0.08655 0.507139401 80.10143902 167.54874 2.82809 RWDD3 1.52122961502874e-06 0.125926127532792 0.874072351237593 RWD domain containing 3 FUNCTION: Enhancer of SUMO conjugation. Via its interaction with UBE2I/UBC9, increases SUMO conjugation to proteins by promoting the: binding of E1 and E2 enzymes, thioester linkage between SUMO and UBE2I/UBC9 and transfer of SUMO to specific target proteins which include HIF1A, PIAS, NFKBIA, NR3C1 and TOP1. Isoform 1 and isoform 2 positively regulate the NF-kappa-B signaling pathway by enhancing the sumoylation of NF-kappa-B inhibitor alpha (NFKBIA), promoting its stabilization which consequently leads to an increased inhibition of NF-kappa-B transcriptional activity. Isoform 1 and isoform 2 negatively regulate the hypoxia-inducible factor-1 alpha (HIF1A) signaling pathway by increasing the sumoylation of HIF1A, promoting its stabilization, transcriptional activity and the expression of its target gene VEGFA during hypoxia. Isoform 2 promotes the sumoylation and transcriptional activity of the glucocorticoid receptor NR3C1 and enhances the interaction of SUMO1 and NR3C1 with UBE2I/UBC9. Has no effect on ubiquitination. {ECO:0000269|PubMed:17956732, ECO:0000269|PubMed:22009797, ECO:0000269|PubMed:23469069, ECO:0000269|PubMed:23508108}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in glioma tumors (at protein level). Expressed in a wide number of tissues with highest expression in cerebellum, pituitary, heart, kidney, liver, stomach, pancreas, prostate and spleen. Low levels in thalamus, spinal cord, esophagus, thymus, lung and peripheral blood leukocytes. A higher level expression seen in pituitary tumors as compared to the pituitary gland. {ECO:0000269|PubMed:17956732, ECO:0000269|PubMed:22009797, ECO:0000269|PubMed:23469069}.; unclassifiable (Anatomical System);meninges;lymph node;cartilage;lacrimal gland;islets of Langerhans;urinary;colon;skin;bone marrow;uterus;prostate;pancreas;pia mater;whole body;lung;frontal lobe;endometrium;bone;liver;testis;spleen;dura mater;germinal center;kidney;brain; superior cervical ganglion; 0.03006 0.03970 0.349177632 74.18023119 80.90605 1.90265 RWDD4 0.482983522176144 0.512124348360686 0.00489212946316985 RWD domain containing 4 . . . sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;alveolus;head and neck;kidney;mammary gland;stomach; . 0.21504 0.10832 0.058937498 58.26256192 1037.77466 6.18857 RWDD4P1 . . . RWD domain containing 4 pseudogene 1 . . . . . . . . . . . RWDD4P2 . . . RWD domain containing 4 pseudogene 2 . . . . . . . . . . . RXFP1 3.06530424439522e-07 0.981975911583862 0.0180237818857141 relaxin/insulin-like family peptide receptor 1 FUNCTION: Receptor for relaxins. The activity of this receptor is mediated by G proteins leading to stimulation of adenylate cyclase and an increase of cAMP. Binding of the ligand may also activate a tyrosine kinase pathway that inhibits the activity of a phosphodiesterase that degrades cAMP.; . TISSUE SPECIFICITY: Expressed in the brain, kidney, testis, placenta, uterus, ovary, adrenal, prostate, skin and heart. Not detected in spleen. {ECO:0000269|PubMed:16051677}.; unclassifiable (Anatomical System);uterus;pancreas;lung;cartilage;heart;endometrium;testis;skeletal muscle;skin;tonsil; . 0.21846 0.16783 -0.312207497 32.05944798 98.63757 2.14757 RXFP2 2.94175840947603e-08 0.978811653140612 0.0211883174418038 relaxin/insulin-like family peptide receptor 2 FUNCTION: Receptor for relaxin. The activity of this receptor is mediated by G proteins leading to stimulation of adenylate cyclase and an increase of cAMP. May also be a receptor for Leydig insulin-like peptide (INSL3).; . TISSUE SPECIFICITY: Expressed mainly in the brain, kidney, muscle, testis, thyroid, uterus, peripheral blood cells and bone marrow.; unclassifiable (Anatomical System);bone marrow; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.16562 0.12616 -0.176292081 40.56381222 1150.99694 6.46394 RXFP3 2.31380740273664e-11 0.00510069797356808 0.994899302003294 relaxin/insulin-like family peptide receptor 3 FUNCTION: Receptor for RNL3/relaxin-3. Binding of the ligand inhibit cAMP accumulation. {ECO:0000269|PubMed:14522968}.; . TISSUE SPECIFICITY: Expressed predominantly in brain regions. Highest expression in substantia nigra and pituitary, followed by hippocampus, spinal cord, amygdala, caudate nucleus and corpus callosum, quite low level in cerebellum. In peripheral tissues, relatively high levels in adrenal glands, low levels in pancreas, salivary gland, placenta, mammary gland and testis.; unclassifiable (Anatomical System);uterus;heart;skin; superior cervical ganglion;uterus corpus;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05329 . -0.069700724 48.54328851 69.30431 1.72531 RXFP4 0.00549581832537321 0.715189171571439 0.279315010103188 relaxin/insulin-like family peptide receptor 4 FUNCTION: High affinity receptor for INSL5. Also acts as receptor for RLN3/relaxin-3, as well as bradykinin and kallidin. Binding of the ligand inhibit cAMP accumulation. {ECO:0000269|PubMed:14522967, ECO:0000269|PubMed:15525639}.; . TISSUE SPECIFICITY: Expressed in a broader range of tissues including brain, kidney, testis, thymus, placenta, prostate, salivary gland, thyroid and colon. {ECO:0000269|PubMed:14530218}.; . . 0.11063 0.10169 0.242582624 69.45623968 138.80451 2.56656 RXRA 0.943607122852813 0.0563501121736727 4.27649735146456e-05 retinoid X receptor alpha FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a common heterodimeric partner for a number of nuclear receptors. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes. {ECO:0000269|PubMed:10195690, ECO:0000269|PubMed:11162439, ECO:0000269|PubMed:11915042, ECO:0000269|PubMed:20215566}.; . TISSUE SPECIFICITY: Highly expressed in liver, also found in lung, kidney and heart.; salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland; . 0.72501 0.76250 -0.690637458 15.12149092 54.60468 1.47935 RXRB 0.99759435069672 0.00240555935345052 8.99498290507591e-08 retinoid X receptor beta FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (By similarity). Specifically binds 9-cis retinoic acid (9C-RA). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in a variety of tumor cell lines. {ECO:0000269|PubMed:8381386}.; . . 0.32177 . -0.119252484 44.53880632 88.56715 2.01843 RXRG 0.937024401992312 0.0629641442436644 1.14537640237653e-05 retinoid X receptor gamma FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skin;retina;optic nerve;whole body;lung;thyroid;macula lutea;visual apparatus;pituitary gland;iris;brain; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.64456 0.60631 -0.846787714 11.05803255 16.40534 0.58151 RYBP . . . RING1 and YY1 binding protein FUNCTION: Inhibits ubiquitination and subsequent degradation of TP53, and thereby plays a role in regulating transcription of TP53 target genes. May be implicated in the regulation of the transcription as a repressor of the transcriptional activity of E4TF1. May bind to DNA. Promotes apoptosis. {ECO:0000269|PubMed:11395500, ECO:0000269|PubMed:11953439, ECO:0000269|PubMed:14765135, ECO:0000269|PubMed:19098711}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in lymphoid tissues and placenta. {ECO:0000269|PubMed:11395500, ECO:0000269|PubMed:11953439, ECO:0000269|PubMed:14765135}.; . . 0.48997 0.14229 . . . . RYK . . . receptor-like tyrosine kinase FUNCTION: May be a coreceptor along with FZD8 of Wnt proteins, such as WNT1, WNT3, WNT3A and WNT5A. Involved in neuron differentiation, axon guidance, corpus callosum establishment and neurite outgrowth. In response to WNT3 stimulation, receptor C- terminal cleavage occurs in its transmembrane region and allows the C-terminal intracellular product to translocate from the cytoplasm to the nucleus where it plays a crucial role in neuronal development. {ECO:0000269|PubMed:15454084}.; . TISSUE SPECIFICITY: Observed in all the tissues examined.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;trabecular meshwork;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node; 0.28099 0.18932 . . 2354.37198 8.99508 RYKP1 . . . receptor-like tyrosine kinase pseudogene 1 . . . . . . . . . . . RYR1 1.60965844168568e-07 0.999999839034156 2.45437690799858e-26 ryanodine receptor 1 FUNCTION: Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm. Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:18268335}.; DISEASE: Malignant hyperthermia 1 (MHS1) [MIM:145600]: Autosomal dominant pharmacogenetic disorder of skeletal muscle and is one of the main causes of death due to anesthesia. In susceptible people, an MH episode can be triggered by all commonly used inhalational anesthetics such as halothane and by depolarizing muscle relaxants such as succinylcholine. The clinical features of the myopathy are hyperthermia, accelerated muscle metabolism, contractures, metabolic acidosis, tachycardia and death, if not treated with the postsynaptic muscle relaxant, dantrolene. Susceptibility to MH can be determined with the 'in vitro' contracture test (IVCT): observing the magnitude of contractures induced in strips of muscle tissue by caffeine alone and halothane alone. Patients with normal response are MH normal (MHN), those with abnormal response to caffeine alone or halothane alone are MH equivocal (MHE(C) and MHE(H) respectively). {ECO:0000269|PubMed:10051009, ECO:0000269|PubMed:10484775, ECO:0000269|PubMed:10612851, ECO:0000269|PubMed:10823104, ECO:0000269|PubMed:10888602, ECO:0000269|PubMed:11241852, ECO:0000269|PubMed:11389482, ECO:0000269|PubMed:11525881, ECO:0000269|PubMed:11575529, ECO:0000269|PubMed:11928716, ECO:0000269|PubMed:12059893, ECO:0000269|PubMed:12066726, ECO:0000269|PubMed:12123492, ECO:0000269|PubMed:12208234, ECO:0000269|PubMed:12411788, ECO:0000269|PubMed:12709367, ECO:0000269|PubMed:12883402, ECO:0000269|PubMed:1354642, ECO:0000269|PubMed:14732627, ECO:0000269|PubMed:14985404, ECO:0000269|PubMed:15221887, ECO:0000269|PubMed:15448513, ECO:0000269|PubMed:16163667, ECO:0000269|PubMed:1774074, ECO:0000269|PubMed:19191329, ECO:0000269|PubMed:20142353, ECO:0000269|PubMed:20681998, ECO:0000269|PubMed:23558838, ECO:0000269|PubMed:24013571, ECO:0000269|PubMed:7751854, ECO:0000269|PubMed:7849712, ECO:0000269|PubMed:7881417, ECO:0000269|PubMed:8012359, ECO:0000269|PubMed:9066328, ECO:0000269|PubMed:9138151, ECO:0000269|PubMed:9389851, ECO:0000269|PubMed:9450902, ECO:0000269|PubMed:9497245}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Central core disease of muscle (CCD) [MIM:117000]: Autosomal dominant congenital myopathy, but a severe autosomal recessive form also exists. Both clinical and histological variability is observed. Affected individuals typically display hypotonia and proximal muscle weakness in infancy, leading to the delay of motor milestones. The clinical course of the disorder is usually slow or nonprogressive in adulthood, and the severity of the symptoms may vary from normal to significant muscle weakness. Microscopic examination of CCD-affected skeletal muscle reveals a predominance of type I fibers containing amorphous-looking areas (cores) that do not stain with oxidative and phosphorylase histochemical techniques. {ECO:0000269|PubMed:10051009, ECO:0000269|PubMed:10097181, ECO:0000269|PubMed:11113224, ECO:0000269|PubMed:11709545, ECO:0000269|PubMed:11741831, ECO:0000269|PubMed:12112081, ECO:0000269|PubMed:12136074, ECO:0000269|PubMed:12565913, ECO:0000269|PubMed:12566385, ECO:0000269|PubMed:12937085, ECO:0000269|PubMed:14670767, ECO:0000269|PubMed:14985404, ECO:0000269|PubMed:17204054, ECO:0000269|PubMed:17226826, ECO:0000269|PubMed:18253926, ECO:0000269|PubMed:18312400, ECO:0000269|PubMed:20142353, ECO:0000269|PubMed:21674524, ECO:0000269|PubMed:23558838, ECO:0000269|PubMed:24561095, ECO:0000269|PubMed:7829078, ECO:0000269|PubMed:8220422, ECO:0000269|PubMed:8220423, ECO:0000269|PubMed:9497245}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multiminicore disease with external ophthalmoplegia (MMDO) [MIM:255320]: Clinically heterogeneous neuromuscular disorder. General features include neonatal hypotonia, delayed motor development, and generalized muscle weakness and amyotrophy, which may progress slowly or remain stable. Muscle biopsy shows multiple, poorly circumscribed, short areas of sarcomere disorganization and mitochondria depletion (areas termed minicores) in most muscle fibers. Typically, no dystrophic signs, such as muscle fiber necrosis or regeneration or significant endomysial fibrosis, are present in multiminicore disease. {ECO:0000269|PubMed:12719381, ECO:0000269|PubMed:16380615}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myopathy, congenital, with fiber-type disproportion (CFTD) [MIM:255310]: A genetically heterogeneous disorder in which there is relative hypotrophy of type 1 muscle fibers compared to type 2 fibers on skeletal muscle biopsy. However, these findings are not specific and can be found in many different myopathic and neuropathic conditions. {ECO:0000269|PubMed:20583297}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in RYR1 may be a cause of Samaritan myopathy, a congenital myopathy with benign course. Patients display severe hypotonia and respiratory distress at birth. Unlike other congenital myopathies, the health status constantly improves and patients are minimally affected at adulthood.; TISSUE SPECIFICITY: Skeletal muscle and brain (cerebellum and hippocampus). {ECO:0000269|PubMed:9607712}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;muscle;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;hippocampus;hypopharynx;head and neck;cervix;kidney; tongue;skeletal muscle; 0.22212 . -8.291678111 0.005897617 2142.38985 8.51518 RYR2 0.999999934433848 6.55661522248267e-08 1.2546840724792e-37 ryanodine receptor 2 FUNCTION: Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca(2+) levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity is modulated by formation of heterotetramers with RYR3. Required for cellular calcium ion homeostasis. Required for embryonic heart development. {ECO:0000269|PubMed:10830164, ECO:0000269|PubMed:20056922}.; DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 2 (ARVD2) [MIM:600996]: A congenital heart disease characterized by infiltration of adipose and fibrous tissue into the right ventricle and loss of myocardial cells, resulting in ventricular and supraventricular arrhythmias. {ECO:0000269|PubMed:11159936}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ventricular tachycardia, catecholaminergic polymorphic, 1, with or without atrial dysfunction and/or dilated cardiomyopathy (CPVT1) [MIM:604772]: An arrhythmogenic disorder characterized by stress-induced, bidirectional ventricular tachycardia that may degenerate into cardiac arrest and cause sudden death. Patients present with recurrent syncope, seizures, or sudden death after physical activity or emotional stress. {ECO:0000269|PubMed:11157710, ECO:0000269|PubMed:12093772, ECO:0000269|PubMed:12106942, ECO:0000269|PubMed:15046072, ECO:0000269|PubMed:15046073, ECO:0000269|PubMed:15466642, ECO:0000269|PubMed:15544015}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in heart muscle (at protein level). Heart muscle, brain (cerebellum and hippocampus) and placenta. {ECO:0000269|PubMed:10830164, ECO:0000269|PubMed:9607712}.; unclassifiable (Anatomical System);heart;hypothalamus;colon;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;atrium;lung;frontal lobe;placenta;bone;macula lutea;liver;head and neck;spleen;cervix;brain; amygdala;occipital lobe;subthalamic nucleus;medulla oblongata;temporal lobe;prefrontal cortex;globus pallidus;caudate nucleus;pons;cingulate cortex; 0.27314 0.27889 -5.869562633 0.053078556 1401.64962 6.99815 RYR3 0.999999945238815 5.47611850870598e-08 8.09162693365091e-38 ryanodine receptor 3 FUNCTION: Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. May regulate Ca(2+) release by other calcium channels. Calcium channel that mediates Ca(2+)-induced Ca(2+) release from the endoplasmic reticulum in non-muscle cells. Contributes to cellular calcium ion homeostasis (By similarity). Plays a role in cellular calcium signaling. {ECO:0000250, ECO:0000269|PubMed:12354756}.; . TISSUE SPECIFICITY: Brain, skeletal muscle, placenta and possibly liver and kidney. In brain, highest levels are found in the cerebellum, hippocampus, caudate nucleus and amygdala, with lower levels in the corpus callosum, substantia nigra and thalamus. {ECO:0000269|PubMed:9395096, ECO:0000269|PubMed:9607712}.; unclassifiable (Anatomical System);ovary;cartilage;islets of Langerhans;spinal cord;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;whole body;frontal lobe;placenta;macula lutea;spleen;germinal center;brain; amygdala;superior cervical ganglion;occipital lobe;caudate nucleus;trigeminal ganglion;parietal lobe;skeletal muscle; 0.32508 0.17005 -5.868890763 0.058976174 4624.36471 13.68080 S1PR1 0.484814894860016 0.493241676338834 0.02194342880115 sphingosine-1-phosphate receptor 1 FUNCTION: G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular maturation. Inhibits sprouting angiogenesis to prevent excessive sprouting during blood vessel development. Required for normal egress of mature T-cells from the thymus into the blood stream and into peripheral lymphoid organs. Plays a role in the migration of osteoclast precursor cells, the regulation of bone mineralization and bone homeostasis (By similarity). Plays a role in responses to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3- phosphocholine by pulmonary endothelial cells and in the protection against ventilator-induced lung injury. {ECO:0000250, ECO:0000269|PubMed:10982820, ECO:0000269|PubMed:11230698, ECO:0000269|PubMed:11583630, ECO:0000269|PubMed:11604399, ECO:0000269|PubMed:19286607, ECO:0000269|PubMed:22344443, ECO:0000269|PubMed:8626678, ECO:0000269|PubMed:9488656}.; . TISSUE SPECIFICITY: Endothelial cells, and to a lesser extent, in vascular smooth muscle cells, fibroblasts, melanocytes, and cells of epithelioid origin.; unclassifiable (Anatomical System);smooth muscle;lymph node;islets of Langerhans;hypothalamus;colon;skeletal muscle;retina;bone marrow;uterus;pancreas;prostate;lung;frontal lobe;trabecular meshwork;thyroid;placenta;hippocampus;spleen;kidney;spinal ganglion;brain;mammary gland;aorta;stomach; cerebellum; 0.30085 0.18374 0.060756528 58.52795471 167.09789 2.82469 S1PR2 0.127343395339276 0.780169359500039 0.0924872451606852 sphingosine-1-phosphate receptor 2 FUNCTION: Receptor for the lysosphingolipid sphingosine 1- phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferation and suppression of apoptosis.; . . unclassifiable (Anatomical System);uterus;lung;testis;germinal center; superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13555 0.16663 -0.402212257 26.7338995 52.79275 1.43988 S1PR3 0.0793338897465345 0.753193215386487 0.167472894866979 sphingosine-1-phosphate receptor 3 FUNCTION: Receptor for the lysosphingolipid sphingosine 1- phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferation and suppression of apoptosis. {ECO:0000269|PubMed:10617617}.; . TISSUE SPECIFICITY: Expressed in all tissues, but most abundantly in heart, placenta, kidney, and liver.; unclassifiable (Anatomical System);cartilage;heart;colon;skin;skeletal muscle;breast;uterus;pancreas;prostate;lung;endometrium;bone;placenta;amnion;testis;kidney;brain;artery;aorta;stomach; . 0.12400 0.13731 0.042348793 57.31304553 330.63286 3.86555 S1PR4 0.520047224467617 0.462950299057052 0.0170024764753317 sphingosine-1-phosphate receptor 4 FUNCTION: Receptor for the lysosphingolipid sphingosine 1- phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. May be involved in cell migration processes that are specific for lymphocytes. {ECO:0000269|PubMed:10679247, ECO:0000269|PubMed:10753843}.; . TISSUE SPECIFICITY: Specifically expressed in fetal and adult lymphoid and hematopoietic tissue as well as in lung. Considerable level of expression in adult and fetal spleen as well as adult peripheral leukocytes and lung. Lower expression in adult thymus, lymph node, bone marrow, and appendix as well as in fetal liver, thymus, and lung.; unclassifiable (Anatomical System);uterus;lymph node;lung;alveolus;colon;kidney;stomach;tonsil; whole blood;skeletal muscle; 0.14051 0.14623 -0.532670911 20.78320359 125.09601 2.43388 S1PR5 0.0574132950803294 0.711029029993166 0.231557674926505 sphingosine-1-phosphate receptor 5 FUNCTION: Receptor for the lysosphingolipid sphingosine 1- phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. Is coupled to both the G(i/0)alpha and G(12) subclass of heteromeric G-proteins (By similarity). May play a regulatory role in the transformation of radial glial cells into astrocytes and may affect proliferative activity of these cells. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed in the brain, most prominently in the corpus callosum, which is predominantly white matter. Detected in spleen, peripheral blood leukocytes, placenta, lung, aorta and fetal spleen. Low-level signal detected in many tissue extracts. Overexpressed in leukemic large granular lymphocytes. Isoform 1 is predominantly expressed in peripheral tissues. Isoform 2 is expressed in brain, spleen and peripheral blood leukocytes. {ECO:0000269|PubMed:11705398, ECO:0000269|PubMed:12234605, ECO:0000269|PubMed:12427546}.; unclassifiable (Anatomical System);pancreas;prostate;lung;hypothalamus;bone;placenta;hypopharynx;testis;spleen;head and neck;kidney;brain; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.09462 0.11955 0.617373774 83.25076669 237.86868 3.33047 S7 . . . surface antigen (chromosome 7) 2 . . . . . . . . . . . S11 . . . surface antigen (X-linked) 2 . . . . . . . . . . . S12 . . . surface antigen (X-linked) 3 . . . . . . . . . . . S100A1 0.00465602079501881 0.444733381712993 0.550610597491988 S100 calcium binding protein A1 FUNCTION: Weakly binds calcium but binds zinc very tightly- distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity. {ECO:0000269|PubMed:22399290}.; . TISSUE SPECIFICITY: Highly prevalent in heart. Also found in lesser quantities in skeletal muscle and brain.; myocardium;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;hypothalamus;muscle;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;head and neck;kidney;mammary gland;stomach; occipital lobe;thalamus;medulla oblongata;spinal cord;temporal lobe;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.23599 0.12583 -0.09720619 46.20193442 28.203 0.90365 S100A2 0.000135122428502476 0.234621122604333 0.765243754967165 S100 calcium binding protein A2 FUNCTION: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes. May also play a role in suppressing tumor cell growth. {ECO:0000269|PubMed:1372446, ECO:0000269|PubMed:22399290}.; . TISSUE SPECIFICITY: A subset of epithelial cells including normal human mammary epithelial cells and keratinocytes. {ECO:0000269|PubMed:1372446}.; . . 0.15299 0.20334 0.169169615 65.33380514 619.29393 5.01955 S100A3 0.000978354164779786 0.362599342467703 0.636422303367517 S100 calcium binding protein A3 FUNCTION: Binds both calcium and zinc. May be involved in calcium- dependent cuticle cell differentiation, hair shaft and hair cuticular barrier formation. {ECO:0000269|PubMed:18083705}.; . TISSUE SPECIFICITY: Skin specific, specifically expressed at the inner endocuticle of hair fibers. {ECO:0000269|PubMed:12470658}.; . . 0.09462 0.11807 0.613741468 83.06794055 452.55836 4.42520 S100A4 0.00465145853748136 0.444541538476662 0.550807002985857 S100 calcium binding protein A4 . . TISSUE SPECIFICITY: Ubiquitously expressed.; lymphoreticular;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;synovium;bone;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;amnion;alveolus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach; adipose tissue;white blood cells;whole blood;bone marrow; 0.26207 0.51960 -0.185391282 39.67916962 6.99406 0.26106 S100A5 4.81203056762956e-05 0.134287922668217 0.865663957026107 S100 calcium binding protein A5 FUNCTION: Binds calcium, zinc and copper. One subunit can simultaneously bind 2 calcium ions or 2 copper ions plus 1 zinc ion. Calcium and copper ions compete for the same binding sites. {ECO:0000269|PubMed:10882717}.; . . brain; appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06502 0.11669 0.391453969 75.87284737 919.49308 5.89325 S100A6 0.178917966295076 0.64476485958129 0.176317174123634 S100 calcium binding protein A6 FUNCTION: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative. {ECO:0000269|PubMed:22399290}.; . . . . 0.15229 0.58572 0.413500896 76.67492333 53.25108 1.44948 S100A7 0.547478872262447 0.398386227026542 0.0541349007110105 S100 calcium binding protein A7 . . TISSUE SPECIFICITY: Fetal ear, skin, and tongue and human cell lines. Highly up-regulated in psoriatic epidermis. Also highly expressed in the urine of bladder squamous cell carcinoma (SCC) bearing patients. {ECO:0000269|PubMed:8618345}.; . . 0.09588 . 0.369407109 74.95281906 4.583 0.16474 S100A7A 0.0315992767749722 0.603027656294107 0.365373066930921 S100 calcium binding protein A7A FUNCTION: May be involved in epidermal differentiation and inflammation and might therefore be important for the pathogenesis of psoriasis and other diseases.; . TISSUE SPECIFICITY: Overexpressed in psoriasis.; visual apparatus;hypopharynx;testis;head and neck; . 0.16781 . 0.749657564 86.56522765 14.28165 0.51600 S100A7L2 0.558124073655943 0.391429270913957 0.0504466554301009 S100 calcium binding protein A7 like 2 . . . . . . . . . 100.52228 2.17167 S100A7P1 . . . S100 calcium binding protein A7 pseudogene 1 . . . . . . . . . . . S100A7P2 . . . S100 calcium binding protein A7 pseudogene 2 . . . . . . . . . . . S100A8 0.186216605301329 0.646322176276722 0.167461218421949 S100 calcium binding protein A8 FUNCTION: S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH- oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinfammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF- kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread. The iNOS-S100A8/A9 transnitrosylase complex directs selective inflammatory stimulus-dependent S-nitrosylation of GAPDH and probably multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to contribute to S-nitrosylation site selectivity. {ECO:0000269|PubMed:12626582, ECO:0000269|PubMed:15331440, ECO:0000269|PubMed:15598812, ECO:0000269|PubMed:15642721, ECO:0000269|PubMed:16258195, ECO:0000269|PubMed:19087201, ECO:0000269|PubMed:19122197, ECO:0000269|PubMed:19935772, ECO:0000269|PubMed:21487906, ECO:0000269|PubMed:22363402, ECO:0000269|PubMed:22808130, ECO:0000269|PubMed:25417112}.; . TISSUE SPECIFICITY: Calprotectin (S100A8/9) is predominantly expressed in myeloid cells. Except for inflammatory conditions, the expression is restricted to a specific stage of myeloid differentiation since both proteins are expressed in circulating neutrophils and monocytes but are absent in normal tissue macrophages and lymphocytes. Under chronic inflammatory conditions, such as psoriasis and malignant disorders, also expressed in the epidermis. Found in high concentrations at local sites of inflammation or in the serum of patients with inflammatory diseases such as rheumatoid, cystic fibrosis, inflammatory bowel disease, Crohn's disease, giant cell arteritis, cystic fibrosis, Sjogren's syndrome, systemic lupus erythematosus, and progressive systemic sclerosis. Involved in the formation and deposition of amyloids in the aging prostate known as corpora amylacea inclusions. Strongly up-regulated in many tumors, including gastric, esophageal, colon, pancreatic, bladder, ovarian, thyroid, breast and skin cancers. {ECO:0000269|PubMed:15598812, ECO:0000269|PubMed:9083090}.; . . 0.29004 0.45465 0.035072054 56.2514744 1.98251 0.06488 S100A9 0.667440117616727 0.31038423415785 0.0221756482254237 S100 calcium binding protein A9 FUNCTION: S100A9 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis, adhesion, can increase the bactericidal activity of neutrophils by promoting phagocytosis via activation of SYK, PI3K/AKT, and ERK1/2 and can induce degranulation of neutrophils by a MAPK-dependent mechanism. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH- oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinfammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF- kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread. Has transnitrosylase activity; in oxidatively-modified low- densitity lipoprotein (LDL(ox))-induced S-nitrosylation of GAPDH on 'Cys-247' proposed to transfer the NO moiety from NOS2/iNOS to GAPDH via its own S-nitrosylated Cys-3. The iNOS-S100A8/A9 transnitrosylase complex is proposed to also direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C- x-x-[DE] motif. {ECO:0000269|PubMed:12626582, ECO:0000269|PubMed:15331440, ECO:0000269|PubMed:15598812, ECO:0000269|PubMed:15642721, ECO:0000269|PubMed:16258195, ECO:0000269|PubMed:19087201, ECO:0000269|PubMed:19122197, ECO:0000269|PubMed:19402754, ECO:0000269|PubMed:19534726, ECO:0000269|PubMed:19935772, ECO:0000269|PubMed:20103766, ECO:0000269|PubMed:21325622, ECO:0000269|PubMed:21487906, ECO:0000269|PubMed:22363402, ECO:0000269|PubMed:22804476, ECO:0000269|PubMed:22808130, ECO:0000269|PubMed:25417112, ECO:0000269|PubMed:8423249}.; . TISSUE SPECIFICITY: Calprotectin (S100A8/9) is predominantly expressed in myeloid cells. Except for inflammatory conditions, the expression is restricted to a specific stage of myeloid differentiation since both proteins are expressed in circulating neutrophils and monocytes but are absent in normal tissue macrophages and lymphocytes. Under chronic inflammatory conditions, such as psoriasis and malignant disorders, also expressed in the epidermis. Found in high concentrations at local sites of inflammation or in the serum of patients with inflammatory diseases such as rheumatoid, cystic fibrosis, inflammatory bowel disease, Crohn's disease, giant cell arteritis, cystic fibrosis, Sjogren's syndrome, systemic lupus erythematosus, and progressive systemic sclerosis. Involved in the formation and deposition of amyloids in the aging prostate known as corpora amylacea inclusions. Strongly up-regulated in many tumors, including gastric, esophageal, colon, pancreatic, bladder, ovarian, thyroid, breast and skin cancers. {ECO:0000269|PubMed:15598812, ECO:0000269|PubMed:3313057, ECO:0000269|PubMed:3405210, ECO:0000269|PubMed:8423249, ECO:0000269|PubMed:9083090}.; . . 0.43581 0.45083 0.103030231 61.2762444 11.02977 0.39954 S100A10 0.173245480827353 0.643187752902823 0.183566766269825 S100 calcium binding protein A10 FUNCTION: Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine- specific kinase.; . . . . 0.55179 0.29199 0.125076652 62.7388535 3.29196 0.11931 S100A11 0.0501061591847237 0.689065519073055 0.260828321742222 S100 calcium binding protein A11 FUNCTION: Facilitates the differentiation and the cornification of keratinocytes. {ECO:0000269|PubMed:18618420}.; . . ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;bone marrow;uterus;prostate;optic nerve;endometrium;gum;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;pineal body;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;alveolus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; adipose tissue;lung;heart;tongue;placenta;whole blood; 0.14282 0.19847 0.215080721 67.91696155 46.57347 1.31757 S100A11P1 . . . S100 calcium binding protein A11 pseudogene 1 FUNCTION: Modulates P53/TP53 protein levels, and thereby plays a role in the regulation of cell survival and apoptosis. Depending on the context, it can promote cell proliferation or apoptosis. Plays a role in the regulation of cell migration by modulating the levels of MMP2, a matrix protease that is under transcriptional control of P53/TP53. Does not bind calcium. {ECO:0000269|PubMed:21559403, ECO:0000269|PubMed:22032898, ECO:0000269|PubMed:22451655}.; . TISSUE SPECIFICITY: Expressed at highest levels in colon and at moderate levels in thymus, kidney, liver, small intestine, and lung. Low expression in heart and no expression is seen in brain, skeletal muscle, spleen, placenta and peripheral blood leukocytes. {ECO:0000269|PubMed:11944983}.; . . 0.17578 . -0.207437529 38.2814343 . . S100A11P2 . . . S100 calcium binding protein A11 pseudogene 2 . . . . . . . . . . . S100A11P3 . . . S100 calcium binding protein A11 pseudogene 3 . . . . . . . . . . . S100A11P4 . . . S100 calcium binding protein A11 pseudogene 4 . . . . . . . . . . . S100A12 0.0335297458461187 0.614774091966073 0.351696162187808 S100 calcium binding protein A12 FUNCTION: S100A12 is a calcium-, zinc- and copper-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. Its proinflammatory activity involves recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to receptor for advanced glycation endproducts (AGER). Binding to AGER activates the MAP-kinase and NF-kappa-B signaling pathways leading to production of proinflammatory cytokines and up-regulation of cell adhesion molecules ICAM1 and VCAM1. Acts as a monocyte and mast cell chemoattractant. Can stimulate mast cell degranulation and activation which generates chemokines, histamine and cytokines inducing further leukocyte recruitment to the sites of inflammation. Can inhibit the activity of matrix metalloproteinases; MMP2, MMP3 and MMP9 by chelating Zn(2+) from their active sites. Possesses filariacidal and filariastatic activity. Calcitermin possesses antifungal activity against C.albicans and is also active against E.coli and P.aeruginosa but not L.monocytogenes and S.aureus. {ECO:0000269|PubMed:11522286, ECO:0000269|PubMed:17208591, ECO:0000269|PubMed:18292089, ECO:0000269|PubMed:19386136}.; . TISSUE SPECIFICITY: Predominantly expressed by neutrophils, monocytes and activated macrophages. Expressed by eosinophils and macrophages in asthmatic airways in regions where mast cells accumulate. Found in high concentrations in the serum of patients suffering from various inflammatory disorders, such as rheumatoid arthritis, psoriatic arthritis, Crohn's disease, ulcerative colitis, and Kawasaki disease.; . . 0.01409 0.11307 -0.031067188 51.03798066 6.81069 0.25163 S100A13 0.0351531421862098 0.624039522066038 0.340807335747752 S100 calcium binding protein A13 FUNCTION: Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine (By similarity). {ECO:0000250, ECO:0000269|PubMed:12746488, ECO:0000269|PubMed:20863990}.; . TISSUE SPECIFICITY: Expressed in heart and skeletal muscle.; myocardium;ovary;salivary gland;developmental;colon;parathyroid;skin;uterus;prostate;whole body;cochlea;synovium;thyroid;bone;pituitary gland;testis;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;occipital lobe;subthalamic nucleus;appendix;ciliary ganglion;pons;trigeminal ganglion;parietal lobe;cingulate cortex;skeletal muscle; 0.11796 . 0.169169615 65.33380514 9.78198 0.35787 S100A14 0.0570469536230336 0.71004462361376 0.232908422763207 S100 calcium binding protein A14 FUNCTION: Modulates P53/TP53 protein levels, and thereby plays a role in the regulation of cell survival and apoptosis. Depending on the context, it can promote cell proliferation or apoptosis. Plays a role in the regulation of cell migration by modulating the levels of MMP2, a matrix protease that is under transcriptional control of P53/TP53. Does not bind calcium. {ECO:0000269|PubMed:21559403, ECO:0000269|PubMed:22032898, ECO:0000269|PubMed:22451655}.; . TISSUE SPECIFICITY: Expressed at highest levels in colon and at moderate levels in thymus, kidney, liver, small intestine, and lung. Low expression in heart and no expression is seen in brain, skeletal muscle, spleen, placenta and peripheral blood leukocytes. {ECO:0000269|PubMed:11944983}.; ovary;salivary gland;intestine;colon;skin;uterus;prostate;oesophagus;endometrium;larynx;thyroid;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;oral cavity;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;lung;tongue;trigeminal ganglion;skin; 0.17578 . -0.207437529 38.2814343 22.30319 0.74842 S100A16 0.00563845182351615 0.482982663019651 0.511378885156832 S100 calcium binding protein A16 FUNCTION: Calcium-binding protein. Binds one calcium ion per monomer. {ECO:0000269|PubMed:17030513}.; . . . . 0.11437 0.10879 -0.141298762 42.87567823 11.9844 0.43498 S100B 0.181611099130469 0.645399599943051 0.172989300926481 S100 calcium binding protein B FUNCTION: Weakly binds calcium but binds zinc very tightly- distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity. {ECO:0000269|PubMed:20351179, ECO:0000269|PubMed:22399290}.; . TISSUE SPECIFICITY: Although predominant among the water-soluble brain proteins, S100 is also found in a variety of other tissues.; ovary;sympathetic chain;colon;substantia nigra;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;cochlea;endometrium;cerebral cortex;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;lung;adrenal gland;trabecular meshwork;placenta;visual apparatus;hippocampus;kidney;mammary gland;stomach;cerebellum; whole brain;dorsal root ganglion;amygdala;occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;atrioventricular node;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.31883 . 0.057118534 57.99716914 2.73357 0.09791 S100G 0.141285757222525 0.627269994765971 0.231444248011503 S100 calcium binding protein G . . . . . 0.25854 0.18247 0.145304857 63.81221986 272.38672 3.53857 S100P 0.0486493649314778 0.684042023397536 0.267308611670986 S100 calcium binding protein P FUNCTION: May function as calcium sensor and contribute to cellular calcium signaling. In a calcium-dependent manner, functions by interacting with other proteins, such as EZR and PPP5C, and indirectly plays a role in physiological processes like the formation of microvilli in epithelial cells. May stimulate cell proliferation in an autocrine manner via activation of the receptor for activated glycation end products (RAGE). {ECO:0000269|PubMed:14617629, ECO:0000269|PubMed:19111582, ECO:0000269|PubMed:22399290}.; . TISSUE SPECIFICITY: Detected in all of the tissues except brain, testis and small intestine, expression level is higher in placenta, heart, lung, skeletal muscle, spleen and leukocyte. Up- regulated in various pancreatic ductal adenocarcinomas and pancreatic intraepithelial neoplasias. {ECO:0000269|PubMed:14672411, ECO:0000269|PubMed:15632002}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;brain;bladder;unclassifiable (Anatomical System);heart;pharynx;blood;lens;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; lung;trachea;placenta;fetal lung;whole blood;tonsil;skin;bone marrow; 0.22156 0.11262 -0.163345027 41.24793583 8.60207 0.31516 S100PBP 0.947039388875535 0.0529240963250425 3.65147994226735e-05 S100P binding protein . . TISSUE SPECIFICITY: Expressed in brain, spleen, and lung. Not detected in pancreas or liver. In pancreas, expressed predominantly in islet cells and to a lesser extent in acinar cells, but not expressed in ductal cells. Up-regulated in various pancreatic ductal adenocarcinomas and pancreatic intraepithelial neoplasias. Detected in pancreatic ductal adenocarcinoma cells (at protein level). Not detected in non-neoplastic ductal epithelium (at protein level). {ECO:0000269|PubMed:15632002, ECO:0000269|PubMed:18089492}.; unclassifiable (Anatomical System);pancreas;nasopharynx;placenta;liver;testis;germinal center;brain;skin;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node; 0.13106 . -0.291981272 33.20358575 94.69848 2.09689 S100Z 0.00959470303590954 0.594701458216036 0.395703838748054 S100 calcium binding protein Z . . TISSUE SPECIFICITY: Highest level of expression in spleen and leukocytes. {ECO:0000269|PubMed:11747429}.; ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;optic nerve;lung;bone;liver;kidney;brain;bladder; . 0.10917 . 0.457594962 78.16112291 12.56766 0.45836 SAA1 0.181814610902195 0.76526505590757 0.052920333190235 serum amyloid A1 FUNCTION: Major acute phase protein.; DISEASE: Note=Reactive, secondary amyloidosis is characterized by the extracellular accumulation in various tissues of the SAA1 protein. These deposits are highly insoluble and resistant to proteolysis; they disrupt tissue structure and compromise function. {ECO:0000269|PubMed:1463770}.; DISEASE: Note=Elevated serum SAA1 protein levels may be associated with lung cancer. {ECO:0000269|PubMed:1463770}.; TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma (at protein level). {ECO:0000269|PubMed:12973732, ECO:0000269|PubMed:4816450, ECO:0000269|PubMed:7115671}.; unclassifiable (Anatomical System);meninges;adrenal cortex;parathyroid;skin;skeletal muscle;uterus;pancreas;prostate;pia mater;lung;adrenal gland;nasopharynx;thyroid;liver;testis;dura mater;kidney;brain;mammary gland;pineal gland;stomach;gall bladder; . 0.07473 0.51812 0.103030231 61.2762444 286.88113 3.62775 SAA2 0.0286553987840972 0.801308264709636 0.170036336506267 serum amyloid A2 FUNCTION: Major acute phase reactant. Apolipoprotein of the HDL complex.; DISEASE: Note=Reactive, secondary amyloidosis is characterized by the extracellular accumulation in various tissues of the SAA2 protein. These deposits are highly insoluble and resistant to proteolysis; they disrupt tissue structure and compromise function. {ECO:0000269|PubMed:1463770}.; TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma.; unclassifiable (Anatomical System);skeletal muscle;uterus;pancreas;prostate;lung;larynx;nasopharynx;liver;testis;head and neck;brain;mammary gland;gall bladder; . 0.19499 0.19435 0.725794416 85.98136353 48.05648 1.34866 SAA2-SAA4 . . . SAA2-SAA4 readthrough . . . . . . . . . . . SAA3P . . . serum amyloid A3 pseudogene . . . . . 0.04749 0.20484 . . . . SAA4 0.0146359405828845 0.683009746800654 0.302354312616462 serum amyloid A4, constitutive FUNCTION: Major acute phase reactant. Apolipoprotein of the HDL complex.; . TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma.; uterus;lung;heart;epididymis;liver;kidney;skin; dorsal root ganglion;superior cervical ganglion;fetal liver;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.03127 0.19474 0.659651797 84.35362114 86.98323 1.99165 SAA@ . . . serum amyloid A1 cluster . . . . . . . . . . . SAAL1 0.000128876571862682 0.957645828874199 0.0422252945539381 serum amyloid A like 1 . . . lymphoreticular;colon;skin;uterus;prostate;whole body;endometrium;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node; 0.12547 0.09267 1.129924507 92.23283793 2068.28584 8.38006 SAC3D1 4.62359782878809e-05 0.239635499257974 0.760318264763739 SAC3 domain containing 1 FUNCTION: Involved in centrosome duplication and mitotic progression. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;endometrium;bone;pituitary gland;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);heart;lens;pancreas;lung;placenta;macula lutea;liver;head and neck;cervix;kidney; whole brain;testis - interstitial;testis - seminiferous tubule;testis;tumor;thymus; 0.10034 0.10906 . . 2899.79941 10.20413 SACM1L 0.721901742734862 0.278097216589975 1.04067516225642e-06 SAC1 suppressor of actin mutations 1-like (yeast) FUNCTION: Phosphoinositide phosphatase that hydrolyzes phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P) (PubMed:24209621). Has low activity towards PtdIns(3,5)P2 (By similarity). {ECO:0000250|UniProtKB:Q9ES21, ECO:0000269|PubMed:24209621}.; . TISSUE SPECIFICITY: Detected in heart, brain, lung, liver, kidney, pancreas and testis. {ECO:0000269|PubMed:10048485}.; . . 0.55456 0.10490 -0.424258538 25.56027365 29.43851 0.94154 SACS 6.1462947887645e-12 0.999999999713099 2.80755213698537e-10 sacsin molecular chaperone FUNCTION: Co-chaperone which acts as a regulator of the Hsp70 chaperone machinery and may be involved in the processing of other ataxia-linked proteins. {ECO:0000269|PubMed:19208651}.; DISEASE: Spastic ataxia Charlevoix-Saguenay type (SACS) [MIM:270550]: A neurodegenerative disease characterized by early- onset cerebellar ataxia, spasticity, retinal hypermyelination, pyramidal signs, and both axonal and demyelinating neuropathy with loss of sensory nerve conduction and reduced motor conduction velocities. Other features include dysarthria, distal muscle wasting, nystagmus, defect in conjugate pursuit ocular movements, retinal striation (from prominent retinal nerves) obscuring the retinal blood vessels in places, and the frequent presence of mitral valve prolapse. {ECO:0000269|PubMed:10655055, ECO:0000269|PubMed:12873855, ECO:0000269|PubMed:14718708, ECO:0000269|PubMed:15156359, ECO:0000269|PubMed:15985586, ECO:0000269|PubMed:16007637, ECO:0000269|PubMed:17290461, ECO:0000269|PubMed:17716690, ECO:0000269|PubMed:18398442, ECO:0000269|PubMed:18465152, ECO:0000269|PubMed:18484239, ECO:0000269|PubMed:19529988, ECO:0000269|PubMed:20876471}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in the central nervous system. Also found in skeletal muscle and at low levels in pancreas.; . . 0.66524 0.30950 -1.83176571 2.099551781 4882.3481 14.20336 SACS-AS1 . . . SACS antisense RNA 1 . . . . . . . . . . . SAE1 0.988952422396941 0.0110438475808783 3.73002218097608e-06 SUMO1 activating enzyme subunit 1 FUNCTION: The heterodimer acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2. {ECO:0000269|PubMed:10187858, ECO:0000269|PubMed:10217437, ECO:0000269|PubMed:11451954, ECO:0000269|PubMed:11481243, ECO:0000269|PubMed:15660128, ECO:0000269|PubMed:20164921, ECO:0000269|PubMed:9920803}.; . TISSUE SPECIFICITY: Expression level increases during S phase and drops in G2 phase (at protein level). {ECO:0000269|PubMed:11481243}.; lymphoreticular;medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;synovium;bone;thyroid;testis;germinal center;spinal ganglion;brain;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;hypothalamus;muscle;adrenal cortex;lens;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.63220 0.12546 -0.380166007 27.88393489 72.606 1.77749 SAFB 0.999685074218684 0.000314925755372867 2.59430682328154e-11 scaffold attachment factor B FUNCTION: Binds to scaffold/matrix attachment region (S/MAR) DNA and forms a molecular assembly point to allow the formation of a 'transcriptosomal' complex (consisting of SR proteins and RNA polymerase II) coupling transcription and RNA processing (By similarity). Can function as an estrogen receptor corepressor and can also bind to the HSP27 promoter and decrease its transcription. When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter (By similarity). Can inhibit cell proliferation. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the CNS and at low levels in the liver. Expressed in a wide number of breast cancer cell lines.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle;cingulate cortex;parietal lobe; 0.20672 0.15741 -1.618506764 2.925218212 44.85677 1.28461 SAFB2 0.999582500881394 0.000417499067041763 5.15639364665452e-11 scaffold attachment factor B2 FUNCTION: Binds to scaffold/matrix attachment region (S/MAR) DNA. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation.; . TISSUE SPECIFICITY: Expressed at high levels in the CNS and at low levels in the liver. Expressed in a wide number of breast cancer cell lines.; smooth muscle;ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;lacrimal gland;tongue;islets of Langerhans;hypothalamus;muscle;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach; amygdala;medulla oblongata;thalamus;subthalamic nucleus;testis - seminiferous tubule;thyroid;prefrontal cortex;globus pallidus;cingulate cortex; 0.17843 0.15468 -0.929520514 9.683887709 138.84431 2.56776 SAG 1.56803495288471e-08 0.378036644043591 0.621963340276059 S-antigen; retina and pineal gland (arrestin) FUNCTION: Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated- phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase.; DISEASE: Retinitis pigmentosa 47 (RP47) [MIM:613758]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:9565049}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Retina and pineal gland.; unclassifiable (Anatomical System);optic nerve;lung;macula lutea;visual apparatus;testis;fovea centralis;skeletal muscle;retina; uterus corpus;superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion; 0.24804 0.46299 0.290313621 71.56758669 968.22528 6.01749 SAGE1 1.63649424965499e-09 0.597251857414968 0.402748140948538 sarcoma antigen 1 . . TISSUE SPECIFICITY: Expressed mainly in bladder, lung, head and neck carcinomas. Not expressed in normal tissues except for testis. {ECO:0000269|PubMed:10919659}.; unclassifiable (Anatomical System);lung;testis; superior cervical ganglion;testis - interstitial;atrioventricular node;trigeminal ganglion; 0.43406 . 0.005534202 54.09884407 132.88467 2.50683 SAGE2P . . . sarcoma antigen 2, pseudogene . . . . . . . . . . . SAGE3P . . . sarcoma antigen 3, pseudogene . . . . . . . . . . . SAGE4P . . . sarcoma antigen 4, pseudogene . . . . . . . . . . . SAI1 . . . suppression of anchorage independence 1 . . . . . . . . . . . SALL1 0.994674178309957 0.0053256950208858 1.2666915764924e-07 spalt-like transcription factor 1 FUNCTION: Transcriptional repressor involved in organogenesis. {ECO:0000250}.; DISEASE: Townes-Brocks syndrome (TBS) [MIM:107480]: Rare, autosomal dominant malformation syndrome with a combination of imperforate anus, triphalangeal and supernumerary thumbs, malformed ears and sensorineural hearing loss. {ECO:0000269|PubMed:10533063, ECO:0000269|PubMed:9425907, ECO:0000269|PubMed:9973281}. Note=The disease is caused by mutations affecting the gene represented in this entry. Some individuals with SALL1 mutations manifest a phenotype overlapping with TBS and bronchio-oto-renal syndrome. Clinical features include dysplastic ears, hypoplastic kidneys with impaired renal function, gastroesophageal reflux, hypermetropia, hypospadias, and mild developmental delay. Affected individuals lack the characteristic anal or hand malformations of TBS. {ECO:0000269|PubMed:10928856}.; TISSUE SPECIFICITY: Highest levels in kidney. Lower levels in adult brain (enriched in corpus callosum, lower expression in substantia nigra) and liver.; unclassifiable (Anatomical System);lung;whole body;thyroid;testis;kidney;brain;skeletal muscle; amygdala;thyroid;spinal cord;globus pallidus; 0.93269 0.27771 -0.830447013 11.52984194 202.60205 3.07157 SALL1P1 . . . spalt-like transcription factor 1 pseudogene 1 . . . . . . . . . . . SALL2 1.78061422737665e-05 0.880550232198812 0.119431961658914 spalt-like transcription factor 2 FUNCTION: Probable transcription factor that plays a role in eye development before, during, and after optic fissure closure. {ECO:0000269|PubMed:24412933}.; DISEASE: Coloboma, ocular, autosomal recessive (COAR) [MIM:216820]: An ocular anomaly resulting from abnormal morphogenesis of the optic cup and stalk, and incomplete fusion of the fetal intra-ocular fissure during gestation. The clinical presentation is variable. Some individuals may present with minimal defects in the anterior iris leaf without other ocular defects. More complex malformations create a combination of iris, uveoretinal and/or optic nerve defects without or with microphthalmia or even anophthalmia. {ECO:0000269|PubMed:24412933}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest levels in adult brain (in different areas). Lower levels in heart; very low levels in kidney and pancreas. Expressed throughout the retina and lens vesicle as well as the periocular mesenchyme. {ECO:0000269|PubMed:24412933}.; unclassifiable (Anatomical System);lymph node;heart;ovary;islets of Langerhans;hypothalamus;sympathetic chain;choroid;skin;skeletal muscle;retina;uterus;whole body;lung;frontal lobe;thyroid;visual apparatus;hippocampus;testis;kidney;brain;bladder;peripheral nerve;cerebellum; superior cervical ganglion;cerebellum peduncles;hypothalamus;globus pallidus;pons;trigeminal ganglion;cerebellum; 0.93246 . 0.496013929 79.63552725 2698.83404 9.77668 SALL3 0.0901931288456932 0.900982929801891 0.008823941352416 spalt-like transcription factor 3 FUNCTION: Probable transcription factor.; . TISSUE SPECIFICITY: Widely expressed in adult with highest levels in heart. Expressed in fetal brain (in neurons of hippocampus, cortex, mediodorsal and ventrolateral thalamic nuclei, putamen, cerebellum and brainstem).; . . 0.53411 0.12093 . . 660.65433 5.15350 SALL4 0.999442034343346 0.000557963103696446 2.55295790033754e-09 spalt-like transcription factor 4 FUNCTION: Transcription factor with a key role in the maintenance and self-renewal of embryonic and hematopoietic stem cells. {ECO:0000269|PubMed:23012367}.; DISEASE: Duane-radial ray syndrome (DRRS) [MIM:607323]: Disorder characterized by the association of forearm malformations with Duane retraction syndrome. {ECO:0000269|PubMed:12393809, ECO:0000269|PubMed:12395297, ECO:0000269|PubMed:16402211}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Oculootoradial syndrome (OORS) [MIM:147750]: Autosomal dominant condition characterized by upper limbs anomalies (radial ray defects, carpal bones fusion), extraocular motor disturbances, congenital bilateral non-progressive mixed hearing loss. Other less consistent malformations include heart involvement, mild thrombocytopenia and leukocytosis (before age 50), shoulder girdle hypoplasia, imperforate anus, kidney malrotation or rectovaginal fistula. The IVIC syndrome is an allelic disorder of Duane-radial ray syndrome (DRRS) with a similar phenotype. {ECO:0000269|PubMed:17256792}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in testis. Constitutively expressed in acute myeloid leukemia (AML). {ECO:0000269|PubMed:16763212}.; unclassifiable (Anatomical System);heart;ovary;adrenal medulla;blood;skeletal muscle;skin;bone marrow;uterus;epididymis;thyroid;testis;brain; . 0.62203 0.15583 -1.473536006 3.727294173 3396.93268 11.16683 SALL4P1 . . . spalt-like transcription factor 4 pseudogene 1 . . . . . . . . . . . SALL4P2 . . . spalt-like transcription factor 4 pseudogene 2 . . . . . . . . . . . SALL4P3 . . . spalt-like transcription factor 4 pseudogene 3 . . . . . . . . . . . SALL4P4 . . . spalt-like transcription factor 4 pseudogene 4 . . . . . . . . . . . SALL4P5 . . . spalt-like transcription factor 4 pseudogene 5 . . . . . . . . . . . SALL4P6 . . . spalt-like transcription factor 4 pseudogene 6 . . . . . . . . . . . SALL4P7 . . . spalt-like transcription factor 4 pseudogene 7 . . . . . . . . . . . SALRNA1 . . . senescence associated long non-coding RNA 1 . . . . . . . . . . . SALRNA2 . . . senescence associated long non-coding RNA 2 . . . . . . . . . . . SALRNA3 . . . senescence associated long non-coding RNA 3 . . . . . . . . . . . SAMD1 0.204726948541933 0.752444072317747 0.0428289791403203 sterile alpha motif domain containing 1 FUNCTION: May play a role in atherogenesis by immobilizing LDL in the atherial wall. {ECO:0000269|PubMed:16159594}.; . TISSUE SPECIFICITY: Expressed in atherosclerotic lesions, not in normal intima. {ECO:0000269|PubMed:16159594}.; lymphoreticular;myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.41371 0.12640 . . 86.80726 1.98990 SAMD3 1.09707510090606e-06 0.937046699335671 0.0629522035892287 sterile alpha motif domain containing 3 . . . unclassifiable (Anatomical System);medulla oblongata;visual apparatus; . 0.10152 0.10086 -0.354480518 29.42911064 120.51258 2.39131 SAMD4A 0.999267731904104 0.000732267093988258 1.00190724445355e-09 sterile alpha motif domain containing 4A FUNCTION: Acts as a translational repressor of SRE-containing messengers. {ECO:0000269|PubMed:16221671}.; . . unclassifiable (Anatomical System);medulla oblongata;ovary;islets of Langerhans;parathyroid;skin;skeletal muscle;retina;uterus;lung;frontal lobe;larynx;epididymis;placenta;bone;testis;head and neck;germinal center;kidney;mammary gland; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;trigeminal ganglion;skeletal muscle; 0.89857 0.11324 -0.642904474 16.62538335 387.26704 4.14414 SAMD4B 0.998551353474612 0.00144864124106058 5.28432703152836e-09 sterile alpha motif domain containing 4B FUNCTION: Has transcriptional repressor activity. Overexpression inhibits the transcriptional activities of AP-1, p53/TP53 and CDKN1A. {ECO:0000269|PubMed:20510020}.; . TISSUE SPECIFICITY: Widely expressed in embryonic and adult tissues. {ECO:0000269|PubMed:20510020}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;skin;uterus;pancreas;optic nerve;lung;endometrium;adrenal gland;larynx;epididymis;thyroid;visual apparatus;testis;head and neck;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.18206 0.10727 -0.912929826 9.902099552 68.09244 1.70652 SAMD5 0.000898003812903688 0.347983594095382 0.651118402091714 sterile alpha motif domain containing 5 . . . . . 0.29958 0.09907 . . 563.80159 4.82034 SAMD7 6.78008462543362e-06 0.713646255728833 0.286346964186542 sterile alpha motif domain containing 7 . . . retina; . 0.39427 0.08733 0.086440867 60.47416844 1131.34051 6.41698 SAMD8 0.00435169659402061 0.962672556013937 0.0329757473920426 sterile alpha motif domain containing 8 FUNCTION: Sphingomyelin synthases synthesize sphingolipids through transfer of a phosphatidyl head group on to the primary hydroxyl of ceramide. SAMD8 is an endoplasmic reticulum (ER) transferase that has no sphingomyelin synthase activity but can convert phosphatidylethanolamine (PE) and ceramide to ceramide phosphoethanolamine (CPE) albeit with low product yield. Appears to operate as a ceramide sensor to control ceramide homeostasis in the endoplasmic reticulum rather than a converter of ceramides. Seems to be critical for the integrity of the early secretory pathway. {ECO:0000269|PubMed:19506037}.; . . . . 0.30405 0.11012 -0.161524709 41.6430762 31.66382 0.99650 SAMD9 1.28543048483051e-23 0.000152057386039016 0.999847942613961 sterile alpha motif domain containing 9 FUNCTION: May play a role in the inflammatory response to tissue injury and the control of extra-osseous calcification, acting as a downstream target of TNF-alpha signaling. Involved in the regulation of EGR1, in coordination with RGL2. {ECO:0000269|PubMed:16960814, ECO:0000269|PubMed:18094730, ECO:0000269|PubMed:21160498}.; DISEASE: Tumoral calcinosis, normophosphatemic, familial (NFTC) [MIM:610455]: An uncommon, life-threatening disorder characterized by progressive deposition of calcified masses in cutaneous and subcutaneous tissues. Serum phosphate levels are normal. Clinical features include painful calcified ulcerative lesions and massive calcium deposition in the mid- and lower dermis, severe skin and bone infections, erythematous papular skin eruption in infancy, conjunctivitis, and gingivitis. NFTC shows a striking resemblance to acquired dystrophic calcinosis, in which tissue calcification occurs as a consequence of tissue injury/inflammation. {ECO:0000269|PubMed:16960814, ECO:0000269|PubMed:18094730}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Very low levels are detected in skeletal muscle. Not detected in brain. Down-regulated in aggressive fibromatosis, as well as in breast and colon cancers. Up-regulated in fibroblasts from patients with normophosphatemic tumoral calcinosis (NFTC). {ECO:0000269|PubMed:16960814, ECO:0000269|PubMed:17407603}.; . . 0.11464 0.09279 1.122466798 92.11488559 1358.3785 6.91769 SAMD9L 3.79851707301836e-10 0.921807367375142 0.0781926322450065 sterile alpha motif domain containing 9-like . . TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues. Variable expression in tumors. Down-regulated in breast cancer. {ECO:0000269|PubMed:17407603}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;hypopharynx;liver;spleen;head and neck;kidney;stomach; . 0.12163 0.09050 -0.033100763 50.56027365 662.11912 5.15496 SAMD10 0.00605113928963302 0.734434922600312 0.259513938110055 sterile alpha motif domain containing 10 . . . . . 0.11059 . 0.283038099 71.26680821 53.52856 1.45414 SAMD11 1.35381157129201e-10 0.18370000637236 0.816299993492259 sterile alpha motif domain containing 11 FUNCTION: May play a role in photoreceptor development. {ECO:0000250}.; . . lymphoreticular;ovary;salivary gland;developmental;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;oesophagus;endometrium;larynx;gum;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; . 0.10109 . . . 835.24604 5.65821 SAMD11P1 . . . sterile alpha motif domain containing 11 pseudogene 1 . . . . . . . . . . . SAMD12 0.00131724341047217 0.859529580900545 0.139153175688983 sterile alpha motif domain containing 12 . . . breast;optic nerve;macula lutea;fovea centralis;choroid;lens;retina; . 0.10334 0.07307 0.327131069 73.27199811 40.81076 1.19540 SAMD12-AS1 . . . SAMD12 antisense RNA 1 . . . . . . . . . . . SAMD13 0.128562761436203 0.780198578076932 0.0912386604868656 sterile alpha motif domain containing 13 . . . . . 0.04451 . -0.119252484 44.53880632 2.78251 0.09950 SAMD14 0.0202644303517086 0.975990270820888 0.0037452988274037 sterile alpha motif domain containing 14 . . . ovary;colon;parathyroid;choroid;fovea centralis;retina;uterus;optic nerve;testis;brain;unclassifiable (Anatomical System);blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;macula lutea;liver;spleen;kidney;aorta;cerebellum; superior cervical ganglion;cerebellum peduncles;atrioventricular node;trigeminal ganglion; 0.19905 0.10658 -0.53631094 20.53550366 50.42659 1.39709 SAMD15 2.34405461457857e-06 0.485397044286949 0.514600611658436 sterile alpha motif domain containing 15 . . . unclassifiable (Anatomical System);lung;nasopharynx;bone;testis;colon;amniotic fluid;spleen; . 0.08195 . 0.846940207 88.47605567 728.5977 5.35678 SAMHD1 1.50497735378024e-05 0.999637778144474 0.000347172081988005 SAM domain and HD domain 1 FUNCTION: Host restriction nuclease that blocks early-stage virus replication in dendritic and other myeloid cells. Likewise, suppresses LINE-1 retrotransposon activity. May function by reducing the cellular dNTP levels to levels too low for retroviral reverse transcription to occur. May play a role in mediating proinflammatory responses to TNF-alpha signaling. {ECO:0000269|PubMed:18546154, ECO:0000269|PubMed:19525956, ECO:0000269|PubMed:22056990, ECO:0000269|PubMed:24336198}.; DISEASE: Aicardi-Goutieres syndrome 5 (AGS5) [MIM:612952]: A form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood. {ECO:0000269|PubMed:19525956, ECO:0000269|PubMed:20131292, ECO:0000269|PubMed:20842748}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Chilblain lupus 2 (CHBL2) [MIM:614415]: A rare cutaneous form of lupus erythematosus. Affected individuals present with painful bluish-red papular or nodular lesions of the skin in acral locations precipitated by cold and wet exposure at temperatures less than 10 degrees centigrade. {ECO:0000269|PubMed:21204240}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, spleen, liver, small intestine, placenta, lung and peripheral blood leukocytes. No expression is seen in brain and thymus. {ECO:0000269|PubMed:11064105}.; lymphoreticular;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;blood;breast;lung;cornea;nasopharynx;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach; olfactory bulb;white blood cells;ciliary ganglion;whole blood; 0.04441 0.13603 -0.734731259 14.01863647 16.13734 0.57187 SAMM50 0.000727114523857838 0.995404246992102 0.00386863848404024 SAMM50 sorting and assembly machinery component FUNCTION: Plays a crucial role in the maintenance of the structure of mitochondrial cristae and the proper assembly of the mitochondrial respiratory chain complexes (PubMed:22252321, PubMed:25781180). Required for the assembly of TOMM40 into the TOM complex (PubMed:15644312). {ECO:0000269|PubMed:15644312, ECO:0000269|PubMed:22252321, ECO:0000269|PubMed:25781180}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;brain;gall bladder;tonsil;heart;cartilage;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;developmental;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus; fetal liver;adrenal gland;testis;skeletal muscle; 0.10327 0.12103 -0.26629572 34.81953291 2520.91203 9.36256 SAMM50P1 . . . SAMM50 sorting and assembly machinery component pseudogene 1 . . . . . . . . . . . SAMSN1 0.0756023579713905 0.912666727097622 0.0117309149309877 SAM domain, SH3 domain and nuclear localization signals 1 FUNCTION: Negative regulator of B-cell activation. Down-regulates cell proliferation (in vitro). Promotes RAC1-dependent membrane ruffle formation and reorganization of the actin cytoskeleton. Regulates cell spreading and cell polarization. Stimulates HDAC1 activity. Regulates LYN activity by modulating its tyrosine phosphorylation (By similarity). {ECO:0000250, ECO:0000269|PubMed:15381729}.; . TISSUE SPECIFICITY: Detected in peripheral blood B-cells (at protein level). Detected in spleen, liver and peripheral blood. {ECO:0000269|PubMed:11594764, ECO:0000269|PubMed:15381729}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;cochlea;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;pharynx;blood;lens;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;alveolus;liver;kidney;mammary gland;stomach; white blood cells;trigeminal ganglion; 0.13816 0.20845 0.41713504 76.95800896 2089.70219 8.42155 SAMSN1-AS1 . . . SAMSN1 antisense RNA 1 . . . . . . . . . . . SAP18 0.0457562409111712 0.853093758328228 0.101150000760601 Sin3A associated protein 18kDa FUNCTION: Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit mRNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits the formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. {ECO:0000269|PubMed:12665594, ECO:0000269|PubMed:20966198, ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:9150135}.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.44812 0.14896 -0.119252484 44.53880632 5.43227 0.20157 SAP18P1 . . . SAP18 pseudogene 1 . . . . . . . . . . . SAP18P2 . . . SAP18 pseudogene 2 . . . . . . . . . . . SAP18P3 . . . SAP18 pseudogene 3 . . . . . . . . . . . SAP25 . . . Sin3A associated protein 25kDa FUNCTION: Involved in the transcriptional repression mediated by the mSIN3A but not the N-CoR corepressor complex. {ECO:0000250}.; . . . . . . 0.323496558 72.93583392 21.78248 0.73341 SAP30 0.228585001159406 0.736691827125022 0.0347231717155721 Sin3A associated protein 30kDa FUNCTION: Involved in the functional recruitment of the Sin3- histone deacetylase complex (HDAC) to a specific subset of N-CoR corepressor complexes. Capable of transcription repression by N- CoR. Active in deacetylating core histone octamers (when in a complex) but inactive in deacetylating nucleosomal histones. {ECO:0000250|UniProtKB:O88574, ECO:0000269|PubMed:9651585}.; . TISSUE SPECIFICITY: Expressed in all tissues tested with highest levels in pancreas, ovary, PBL, spleen and thymus; lowest levels in brain, placenta, lung and kidney. {ECO:0000269|PubMed:9702189}.; unclassifiable (Anatomical System);heart;ovary;adrenal cortex;colon;parathyroid;lens;skin;bone marrow;breast;uterus;prostate;lung;trabecular meshwork;bone;placenta;testis;cervix;kidney;brain;mammary gland;aorta;stomach;thymus; testis;trigeminal ganglion; 0.22916 0.11162 0.057118534 57.99716914 62.73133 1.61989 SAP30BP 1.57392044285554e-05 0.863886438144151 0.13609782265142 SAP30 binding protein FUNCTION: Induces cell death. May act as a transcriptional corepressor of a gene related to cell survival. May be involved in the regulation of beta-2-microglobulin genes. {ECO:0000250|UniProtKB:Q02614, ECO:0000269|PubMed:15496587}.; . . lymphoreticular;ovary;adrenal medulla;skin;retina;prostate;optic nerve;cochlea;thyroid;iris;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;uterus;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;nose;stomach;thymus;cerebellum; . 0.35411 0.11039 -0.117432389 44.89266336 . . SAP30L 0.857185856481165 0.142345029033083 0.000469114485752204 SAP30-like FUNCTION: Involved in the functional recruitment of the class 1 Sin3-histone deacetylase complex (HDAC) to the nucleolus. {ECO:0000269|PubMed:16820529}.; . TISSUE SPECIFICITY: Expressed in all tissues tested with highest levels in testis.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.31318 0.11262 -0.009020804 52.8544468 17.45657 0.61284 SAP30L-AS1 . . . SAP30L antisense RNA 1 (head to head) . . . . . . . . . . . SAP130 0.998572964181711 0.00142703577608458 4.22040324724674e-11 Sin3A associated protein 130kDa FUNCTION: Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the mSin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes. {ECO:0000269|PubMed:12724404}.; . TISSUE SPECIFICITY: Expressed in various cancer cell ines. {ECO:0000269|PubMed:12724404}.; lymphoreticular;medulla oblongata;ovary;adrenal medulla;developmental;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;pancreas;lung;adrenal gland;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;medulla oblongata;testis - seminiferous tubule;testis;pons;trigeminal ganglion;cerebellum; 0.12576 0.08486 -1.616692429 2.937013447 64.86596 1.65420 SAPCD1 2.31956261529551e-07 0.152378142576588 0.847621625467151 suppressor APC domain containing 1 . . . . . . . 1.436808095 95.04600142 699.03034 5.26327 SAPCD1-AS1 . . . SAPCD1 antisense RNA 1 . . . . . . . . . . . SAPCD2 0.00479900889045619 0.881072946357922 0.114128044751622 suppressor APC domain containing 2 . . TISSUE SPECIFICITY: Expressed in 5-month-old fetal tissues, including stomach, intestine, colon, liver, brain, lung, heart, spleen and kidney. Undetectable in non-cancerous adult tissues. Expressed in many primary gastric carcinoma, but almost not in adjacent normal mucosa. Expressed preferentially in M and G1 phases, compared to S and G2 phases. {ECO:0000269|PubMed:17525738}.; . . 0.24374 0.10812 . . 4196.50284 12.86573 SAPCD2P1 . . . suppressor APC domain containing 2 pseudogene 1 . . . . . . . . . . . SAPCD2P2 . . . suppressor APC domain containing 2 pseudogene 2 . . . . . . . . . . . SAPCD2P3 . . . suppressor APC domain containing 2 pseudogene 3 . . . . . . . . . . . SAPCD2P4 . . . suppressor APC domain containing 2 pseudogene 4 . . . . . . . . . . . SAR1A 0.630165514404675 0.362712239172765 0.00712224642256023 secretion associated Ras related GTPase 1A FUNCTION: Involved in transport from the endoplasmic reticulum to the Golgi apparatus (By similarity). Required to maintain SEC16A localization at discrete locations on the ER membrane perhaps by preventing its dissociation. SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining endoplasmic reticulum exit sites (ERES). {ECO:0000250, ECO:0000269|PubMed:17005010}.; . . . . 0.48549 0.10649 -0.031067188 51.03798066 4.83001 0.17744 SAR1AP1 . . . secretion associated Ras related GTPase 1A pseudogene 1 . . . . . . . . . . . SAR1AP2 . . . secretion associated Ras related GTPase 1A pseudogene 2 . . . . . . . . . . . SAR1AP3 . . . secretion associated Ras related GTPase 1A pseudogene 3 . . . . . . . . . . . SAR1AP4 . . . secretion associated Ras related GTPase 1A pseudogene 4 . . . . . . . . . . . SAR1B 0.00630041605283772 0.910141255140546 0.0835583288066165 secretion associated Ras related GTPase 1B FUNCTION: Involved in transport from the endoplasmic reticulum to the Golgi apparatus. Activated by the guanine nucleotide exchange factor PREB. Involved in the selection of the protein cargo and the assembly of the COPII coat complex.; . TISSUE SPECIFICITY: Expressed in many tissues including small intestine, liver, muscle and brain.; . . 0.45660 0.14201 -0.229483771 36.86010852 11.40907 0.41222 SARAF . . . store-operated calcium entry-associated regulatory factor FUNCTION: Negative regulator of store-operated Ca(2+) entry (SOCE) involved in protecting cells from Ca(2+) overfilling. In response to cytosolic Ca(2+) elevation after endoplasmic reticulum Ca(2+) refilling, promotes a slow inactivation of STIM (STIM1 or STIM2)- dependent SOCE activity: possibly act by facilitating the deoligomerization of STIM to efficiently turn off ORAI when the endoplasmic reticulum lumen is filled with the appropriate Ca(2+) levels, and thus preventing the overload of the cell with excessive Ca(2+) ions. {ECO:0000269|PubMed:22464749}.; . TISSUE SPECIFICITY: Highly expressed in macrophages. {ECO:0000269|Ref.2}.; . . 0.22248 0.12343 -0.404032746 26.53338051 . . SARDH 8.19688048123126e-10 0.970614815411718 0.029385183768594 sarcosine dehydrogenase . DISEASE: Sarcosinemia (SARCOS) [MIM:268900]: A metabolic disorder characterized by an increased concentration of sarcosine in plasma and an increased excretion of sarcosine in urine. Sarcosinemia is most probably a benign condition without significant clinical problems. Some reports have associated sarcosinemia with mental retardation and neurologic problems. {ECO:0000269|PubMed:10444331, ECO:0000269|PubMed:22825317}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . testis;skeletal muscle; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex;skin;parietal lobe; 0.36493 0.31675 1.410932035 94.81009672 3244.42381 10.84499 SARM1 9.18622777225885e-09 0.0869649487451614 0.913035042068611 sterile alpha and TIR motif containing 1 FUNCTION: Negative regulator of MYD88- and TRIF-dependent toll- like receptor signaling pathway which plays a pivotal role in activating axonal degeneration following injury. Promotes Wallerian degeneration an injury-induced axonal death pathway which involves degeneration of an axon distal to the injury site. Can activate neuronal death in response to stress. Regulates dendritic arborization through the MAPK4-JNK pathway. Involved in innate immune response. Inhibits both TICAM1/TRIF- and MYD88- dependent activation of JUN/AP-1, TRIF-dependent activation of NF- kappa-B and IRF3, and the phosphorylation of MAPK14/p38. {ECO:0000269|PubMed:15123841, ECO:0000269|PubMed:16964262, ECO:0000269|PubMed:16985498, ECO:0000269|PubMed:20306472}.; . TISSUE SPECIFICITY: Predominantly expressed in brain, kidney and liver. Expressed at lower level in placenta. {ECO:0000269|PubMed:11386760, ECO:0000269|PubMed:17724133}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;cingulate cortex;skeletal muscle; 0.19814 0.12474 . . 86.57687 1.98744 SARNP 0.989074046382946 0.0109223234244534 3.63019260025714e-06 SAP domain containing ribonucleoprotein FUNCTION: Binds both single-stranded and double-stranded DNA with higher affinity for the single-stranded form. Specifically binds to scaffold/matrix attachment region DNA. Also binds single- stranded RNA. Enhances RNA unwinding activity of DDX39A. May participate in important transcriptional or translational control of cell growth, metabolism and carcinogenesis. Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269|PubMed:15338056, ECO:0000269|PubMed:17196963, ECO:0000269|PubMed:20844015}.; . TISSUE SPECIFICITY: Low expression in spleen, liver, pancreas, testis, thymus, heart, and kidney. Increased levels are seen in hepatocellular carcinoma and pancreatic adenocarcinoma. {ECO:0000269|PubMed:11356193}.; medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;bladder;brain;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; . . -0.119252484 44.53880632 29.78252 0.94955 SARS 0.999150650957633 0.000849347604208611 1.4381586843451e-09 seryl-tRNA synthetase FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). {ECO:0000269|PubMed:9431993}.; . . ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;bladder;brain;gall bladder;heart;tongue;urinary;pharynx;blood;skeletal muscle;greater omentum;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;vein;uterus;whole body;cerebral cortex;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;muscle;bile duct;lung;cornea;nasopharynx;placenta;hippocampus;duodenum;amnion;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;whole brain;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;temporal lobe;pons;subthalamic nucleus;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.18998 0.26095 -0.315847836 31.68789809 60.23566 1.57658 SARS2 5.30599942085599e-05 0.993190974725199 0.00675596528059198 seryl-tRNA synthetase 2, mitochondrial FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (By similarity). {ECO:0000250}.; DISEASE: Hyperuricemia, pulmonary hypertension, renal failure, and alkalosis syndrome (HUPRAS) [MIM:613845]: A multisystem disorder characterized by onset in infancy of progressive renal failure leading to electrolyte imbalances, metabolic alkalosis, pulmonary hypertension, hypotonia, and delayed development. Affected individuals are born prematurely. {ECO:0000269|PubMed:21255763}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;head and neck;spleen;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.08678 0.15379 -0.709045403 14.673272 564.91468 4.82641 SART1 0.992556330388662 0.00744366723192751 2.37941072672014e-09 squamous cell carcinoma antigen recognized by T-cells 1 FUNCTION: Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA. {ECO:0000269|PubMed:11350945}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9449708}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;whole body;larynx;bone;thyroid;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;muscle;adrenal cortex;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; subthalamic nucleus;superior cervical ganglion;medulla oblongata;thalamus;globus pallidus;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.81659 0.10424 -0.949752638 9.32413305 2126.69388 8.49158 SART3 0.991709384753294 0.0082906151198877 1.26817934088647e-10 squamous cell carcinoma antigen recognized by T-cells 3 FUNCTION: U6 snRNP-binding protein that functions as a recycling factor of the splicing machinery. Promotes the initial reassembly of U4 and U6 snRNPs following their ejection from the spliceosome during its maturation (PubMed:12032085). Also binds U6atac snRNPs and may function as a recycling factor for U4atac/U6atac spliceosomal snRNP, an initial step in the assembly of U12-type spliceosomal complex. The U12-type spliceosomal complex plays a role in the splicing of introns with non-canonical splice sites (PubMed:14749385). May also function as a substrate-targeting factor for deubiquitinases like USP4 and USP15. Recruits USP4 to ubiquitinated PRPF3 within the U4/U5/U6 tri-snRNP complex, promoting PRPF3 deubiquitination and thereby regulating the spliceosome U4/U5/U6 tri-snRNP spliceosomal complex disassembly (PubMed:20595234). May also recruit the deubiquitinase USP15 to histone H2B and mediate histone deubiquitination, thereby regulating gene expression and/or DNA repair (PubMed:24526689). May play a role in hematopoiesis probably through transcription regulation of specific genes including MYC (By similarity). {ECO:0000250|UniProtKB:Q9JLI8, ECO:0000269|PubMed:12032085, ECO:0000269|PubMed:14749385, ECO:0000269|PubMed:20595234, ECO:0000269|PubMed:24526689}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11959860}.; medulla oblongata;ovary;skin;retina;prostate;optic nerve;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; amygdala;dorsal root ganglion;occipital lobe;superior cervical ganglion;placenta;globus pallidus;white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;thymus; 0.08156 0.15103 -1.03613328 7.843831092 1963.71024 8.16526 SASH1 0.00325444461467519 0.996741816786582 3.73859874266323e-06 SAM and SH3 domain containing 1 FUNCTION: May have a role in a signaling pathway. Could act as a tumor suppressor.; . . . . 0.36890 0.11167 -0.562239385 19.06699693 3939.62918 12.40945 SASH3 0.891377604908222 0.10839402447588 0.00022837061589782 SAM and SH3 domain containing 3 FUNCTION: May function as a signaling adapter protein in lymphocytes. {ECO:0000250}.; . . umbilical cord;ovary;salivary gland;intestine;colon;choroid;skin;bone marrow;uterus;prostate;whole body;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;breast;lung;placenta;liver;spleen;kidney;aorta;stomach;thymus; . 0.35910 0.26327 -0.448125345 24.19202642 28.8003 0.92063 SASS6 4.9987952418433e-05 0.998441505989101 0.00150850605848064 SAS-6 centriolar assembly protein FUNCTION: Central scaffolding component of the centrioles ensuring their 9-fold symmetry. Required for centrosome biogenesis and duplication: required both for mother-centriole-dependent centriole duplication and deuterosome-dependent centriole amplification in multiciliated cells. Overexpression results in excess foci-bearing centriolar markers. {ECO:0000269|PubMed:15665853, ECO:0000269|PubMed:16244668, ECO:0000269|PubMed:17681131}.; DISEASE: Microcephaly 14, primary, autosomal recessive (MCPH14) [MIM:616402]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. {ECO:0000269|PubMed:24951542}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;ovary;tongue;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;lung;endometrium;visual apparatus;liver;testis;cervix;head and neck;kidney;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10042 0.09296 -0.246069119 36.06982779 3028.03698 10.44826 SAT1 0.811595278666733 0.18373512869992 0.00466959263334768 spermidine/spermine N1-acetyltransferase 1 FUNCTION: Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)-acetylspermine > putrescine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. Also involved in the regulation of polyamine transport out of cells. Acts on 1,3-diaminopropane, 1,5-diaminopentane, putrescine, spermidine (forming N(1)- and N(8)-acetylspermidine), spermine, N(1)-acetylspermidine and N(8)-acetylspermidine. {ECO:0000269|PubMed:16455797, ECO:0000269|PubMed:17516632}.; DISEASE: Keratosis follicularis spinulosa decalvans X-linked (KFSDX) [MIM:308800]: A rare disorder affecting the skin and the eye. Affected men show thickening of the skin of the neck, ears, and extremities, especially the palms and soles, loss of eyebrows, eyelashes and beard, thickening of the eyelids with blepharitis and ectropion, and corneal degeneration. {ECO:0000269|PubMed:12215835, ECO:0000269|PubMed:9341865}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;oesophagus;bone;thyroid;testis;amniotic fluid;germinal center;brain;pineal gland;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;islets of Langerhans;urinary;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;cerebellum; lung;adipose tissue;trachea;placenta;thyroid;fetal lung;kidney; 0.06862 0.09447 -0.031067188 51.03798066 7.59056 0.28138 SAT2 0.0176163047684809 0.892442063120362 0.089941632111157 spermidine/spermine N1-acetyltransferase family member 2 FUNCTION: Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine > spermidine = spermine >> N(1)acetylspermine = putrescine.; . TISSUE SPECIFICITY: Widely expressed.; myocardium;ovary;colon;fovea centralis;uterus;prostate;whole body;frontal lobe;larynx;thyroid;bone;testis;brain;pineal gland;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;pineal body;blood;skeletal muscle;bile duct;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach; . 0.08268 0.09939 0.281220278 71.07808445 621.10583 5.02591 SATB1 0.856613872020163 0.143385326738389 8.01241448112956e-07 SATB homeobox 1 FUNCTION: Crucial silencing factor contributing to the initiation of X inactivation mediated by Xist RNA that occurs during embryogenesis and in lymphoma (By similarity). Binds to DNA at special AT-rich sequences, the consensus SATB1-binding sequence (CSBS), at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcriptional repressor controlling nuclear and viral gene expression in a phosphorylated and acetylated status-dependent manner, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes (e.g. PML at the MHC-I locus) and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Modulates genes that are essential in the maturation of the immune T-cell CD8SP from thymocytes. Required for the switching of fetal globin species, and beta- and gamma-globin genes regulation during erythroid differentiation. Plays a role in chromatin organization and nuclear architecture during apoptosis. Interacts with the unique region (UR) of cytomegalovirus (CMV). Alu-like motifs and SATB1- binding sites provide a unique chromatin context which seems preferentially targeted by the HIV-1 integration machinery. Moreover, HIV-1 Tat may overcome SATB1-mediated repression of IL2 and IL2RA (interleukin) in T-cells by binding to the same domain than HDAC1. Delineates specific epigenetic modifications at target gene loci, directly up-regulating metastasis-associated genes while down-regulating tumor-suppressor genes. Reprograms chromatin organization and the transcription profiles of breast tumors to promote growth and metastasis. {ECO:0000250, ECO:0000269|PubMed:10595394, ECO:0000269|PubMed:11463840, ECO:0000269|PubMed:12374985, ECO:0000269|PubMed:12692553, ECO:0000269|PubMed:1505028, ECO:0000269|PubMed:15618465, ECO:0000269|PubMed:15713622, ECO:0000269|PubMed:16377216, ECO:0000269|PubMed:16630892, ECO:0000269|PubMed:17173041, ECO:0000269|PubMed:17376900, ECO:0000269|PubMed:18337816, ECO:0000269|PubMed:19103759, ECO:0000269|PubMed:19247486, ECO:0000269|PubMed:19332023, ECO:0000269|PubMed:19430959, ECO:0000269|PubMed:9111059, ECO:0000269|PubMed:9548713}.; . TISSUE SPECIFICITY: Expressed predominantly in thymus. {ECO:0000269|PubMed:1505028}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;spinal cord;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;liver;kidney;thymus; . 0.15476 0.15778 -0.580403979 18.58928993 376.72704 4.09142 SATB1-AS1 . . . SATB1 antisense RNA 1 . . . . . . . . . . . SATB2 0.99956300698079 0.000436991611711889 1.40749824587054e-09 SATB homeobox 2 FUNCTION: Binds to DNA, at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcription factor controlling nuclear gene expression, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Required for the initiation of the upper- layer neurons (UL1) specific genetic program and for the inactivation of deep-layer neurons (DL) and UL2 specific genes, probably by modulating BCL11B expression. Repressor of Ctip2 and regulatory determinant of corticocortical connections in the developing cerebral cortex. May play an important role in palate formation. Acts as a molecular node in a transcriptional network regulating skeletal development and osteoblast differentiation. {ECO:0000269|PubMed:14701874}.; DISEASE: Note=Chromosomal aberrations involving SATB2 are found in isolated cleft palate. Translocation t(2;7); translocation t(2;11). {ECO:0000269|PubMed:12915443}.; DISEASE: Cleft palate isolated (CPI) [MIM:119540]: A congenital fissure of the soft and/or hard palate, due to faulty fusion. Isolated cleft palate is not associated with cleft lips. Some patients may manifest other craniofacial dysmorphic features, mental retardation, and osteoporosis. {ECO:0000269|PubMed:12915443, ECO:0000269|PubMed:17377962}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving SATB2 is found in a patient with classical features of Toriello-Carey syndrome. Translocation t(2;14)(q33;q22). {ECO:0000269|PubMed:19170718}.; TISSUE SPECIFICITY: High expression in adult brain, moderate expression in fetal brain, and weak expression in adult liver, kidney, and spinal cord and in select brain regions, including amygdala, corpus callosum, caudate nucleus, and hippocampus. {ECO:0000269|PubMed:14701874}.; colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;larynx;bone;testis;dura mater;brain;unclassifiable (Anatomical System);amygdala;meninges;lymph node;lens;skeletal muscle;pancreas;lung;pia mater;macula lutea;visual apparatus;liver;head and neck;kidney;aorta; whole brain;occipital lobe;subthalamic nucleus;medulla oblongata;fetal brain;temporal lobe;prefrontal cortex;globus pallidus;pons;trigeminal ganglion;cingulate cortex;skeletal muscle;parietal lobe; 0.90767 . -0.868835007 10.65109696 18.7762 0.64879 SATB2-AS1 . . . SATB2 antisense RNA 1 . . . . . . . . . . . SATL1 6.50493662540814e-12 0.017188353951113 0.982811646042382 spermidine/spermine N1-acetyl transferase-like 1 . . . unclassifiable (Anatomical System);myocardium;heart;hypothalamus;pineal body;skin;bone marrow;bile duct;uterus;prostate;lung;adrenal gland;placenta;liver;testis;spleen;cervix;kidney;brain; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05649 . 1.574555842 95.73602265 64.655 1.64966 SAV1 0.777230367391595 0.222703865292044 6.57673163606242e-05 salvador family WW domain containing protein 1 FUNCTION: Regulator of STK3/MST2 and STK4/MST1 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. SAV1 is required for STK3/MST2 and STK4/MST1 activation and promotes cell-cycle exit and terminal differentiation in developing epithelial tissues. Plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosomes, and its ability to phosphorylate CROCC and CEP250. In conjunction with STK3/MST2, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation. {ECO:0000269|PubMed:16930133, ECO:0000269|PubMed:19212654, ECO:0000269|PubMed:21076410, ECO:0000269|PubMed:21104395}.; . TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues with highest expression in the pancreas, aorta and interventricular septum and lowest expression in skeletal muscle. Expression was higher in fetal than in the adult heart. Expressed in various cell lines. {ECO:0000269|PubMed:19212654}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; ciliary ganglion;trigeminal ganglion; 0.64918 0.22769 -0.293801652 32.93819297 28.50729 0.91323 SAX1 . . . spastic ataxia 1 (autosomal dominant) . . . . . . . . . . . SAXO1 . . . stabilizer of axonemal microtubules 1 FUNCTION: May play a role in the regulation of cilium length. Stabilizes microtubules at low temperature. {ECO:0000269|PubMed:25673876}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in testis. Expressed in mature spermatozoa (at protein level). {ECO:0000269|PubMed:25673876}.; . . 0.17625 . 2.361012236 98.43123378 . . SAXO2 . . . stabilizer of axonemal microtubules 2 . . . . . 0.14180 . 0.887394731 89.18966737 . . SAYSD1 0.000747903956143336 0.527447181967854 0.471804914076002 SAYSVFN motif domain containing 1 . . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;lens;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12382 . 0.503505267 79.88912479 64.97566 1.65648 SBDS 0.119263624331666 0.855033544999036 0.0257028306692983 SBDS ribosome assembly guanine nucleotide exchange factor FUNCTION: Required for the assembly of mature ribosomes and ribosome biogenesis. Together with EFTUD1, triggers the GTP- dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Required for normal levels of protein synthesis. May play a role in cellular stress resistance. May play a role in cellular response to DNA damage. May play a role in cell proliferation. {ECO:0000269|PubMed:17643419, ECO:0000269|PubMed:19602484, ECO:0000269|PubMed:19759903, ECO:0000269|PubMed:21536732}.; . TISSUE SPECIFICITY: Widely expressed.; myocardium;ovary;skin;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;hypopharynx;amnion;head and neck;kidney;stomach;aorta; amygdala;occipital lobe;testis - interstitial; 0.65906 0.38797 0.237127192 68.98443029 176.04699 2.88683 SBDSP1 . . . Shwachman-Bodian-Diamond syndrome pseudogene 1 . . . . . . . . . . . SBF1 0.690538813887376 0.30946118609264 1.99846807104168e-11 SET binding factor 1 FUNCTION: Probable pseudophosphatase. Lacks several amino acids in the catalytic pocket which renders it catalytically inactive as a phosphatase. The pocket is however sufficiently preserved to bind phosphorylated substrates, and maybe protect them from phosphatases. Inhibits myoblast differentiation in vitro and induces oncogenic transformation in fibroblasts. According to PubMed:20937701, may function as a guanine nucleotide exchange factor (GEF) activating RAB28. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. {ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:9537414}.; DISEASE: Charcot-Marie-Tooth disease 4B3 (CMT4B3) [MIM:615284]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot- Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie-Tooth disease are designated CMT4. {ECO:0000269|PubMed:23749797}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; whole brain;amygdala;medulla oblongata;superior cervical ganglion;testis - interstitial;caudate nucleus;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.15406 0.14540 -4.050718657 0.171030904 715.45512 5.30977 SBF1P1 . . . SET binding factor 1 pseudogene 1 . . . . . . . . . . . SBF2 0.380054089955573 0.619945910042307 2.12006128591202e-12 SET binding factor 2 FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB28. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. {ECO:0000269|PubMed:20937701}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in spinal cord. {ECO:0000269|PubMed:12554688}.; ovary;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;cochlea;thyroid;bone;testis;brain;artery;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;aorta; dorsal root ganglion;fetal brain; 0.05823 0.16882 -2.004661068 1.728001887 987.04507 6.05762 SBF2-AS1 . . . SBF2 antisense RNA 1 . . . . . . . . . . . SBK1 0.437577104080955 0.531873692615778 0.0305492033032663 SH3 domain binding kinase 1 FUNCTION: May be involved in signal-transduction pathways related to the control of brain development. {ECO:0000250}.; . . colon; . 0.33787 0.12241 . . 14.59456 0.52601 SBK2 0.00147484843945607 0.674531170029247 0.323993981531297 SH3 domain binding kinase family member 2 . . . unclassifiable (Anatomical System); . . . . . 158.52563 2.75043 SBK3 . . . SH3 domain binding kinase family member 3 . . . . . . . . . 322.31624 3.81234 SBNO1 0.999999983699679 1.63003204980969e-08 9.41527595340657e-22 strawberry notch homolog 1 (Drosophila) . . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach; whole brain;superior cervical ganglion;testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;appendix;globus pallidus;testis;pons;trigeminal ganglion; 0.75860 0.10123 -0.815648973 12.01344657 1461.40904 7.12914 SBNO2 0.0244237651687452 0.975552528115315 2.37067159394856e-05 strawberry notch homolog 2 (Drosophila) FUNCTION: Acts as a transcriptional coregulator, that can have both coactivator and corepressor functions. Inhibits the DCSTAMP- repressive activity of TAL1, hence enhancing the access of the transcription factor MITF to the DC-STAMP promoter in osteoclast. Plays a role in bone homeostasis; required as a positive regulator in TNFSF11//RANKL-mediated osteoclast fusion via a DCSTAMP- dependent pathway. May also be required in the regulation of osteoblast differentiation (By similarity). Involved in the transcriptional corepression of NF-kappaB in macrophages (PubMed:18025162). Plays a role as a regulator in the proinflammatory cascade (PubMed:18025162). {ECO:0000250|UniProtKB:Q7TNB8, ECO:0000269|PubMed:18025162}.; . TISSUE SPECIFICITY: Detected in macrophages. IL10 regulates expression in a STAT3-dependent way. {ECO:0000269|PubMed:18025162}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; trigeminal ganglion;whole blood; 0.41647 0.11239 -2.2729502 1.250294881 880.95739 5.78170 SBSN 0.03514528123125 0.928145311969982 0.0367094067987683 suprabasin . . TISSUE SPECIFICITY: Detected in thymus, uterus and esophagus. {ECO:0000269|PubMed:12228223}.; . . 0.11115 0.09814 1.997187788 97.66454352 2531.0409 9.38563 SBSPON 5.95163270931251e-05 0.702468127918752 0.297472355754155 somatomedin B and thrombospondin type 1 domain containing . . TISSUE SPECIFICITY: Detected in aorta extracellular matrix (at protein level). {ECO:0000269|PubMed:20551380}.; . . . 0.09828 0.72761005 86.08162302 3482.82517 11.36292 SC4MOP . . . sterol-C4-methyl oxidase pseudogene . . . . . . . . . . . SC5D 0.103132834566042 0.864353489074067 0.0325136763598906 sterol-C5-desaturase FUNCTION: Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol.; DISEASE: Lathosterolosis (LATHST) [MIM:607330]: Autosomal recessive disorder characterized by a complex phenotype, including multiple congenital anomalies, mental retardation, and liver disease. {ECO:0000269|PubMed:12189593, ECO:0000269|PubMed:12812989}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.12835 0.15143 -0.249709319 35.74545883 15.07852 0.54133 SCA9 . . . spinocerebellar ataxia 9 . . . . . . . . . . . SCA18 . . . spinocerebellar ataxia 18 (sensory with neurogenic muscular atrophy) . . . . . . . . . . . SCA20 . . . spinocerebellar ataxia 20 . . . . . . . . . . . SCA25 . . . spinocerebellar ataxia 25 . . . . . . . . . . . SCA26 . . . spinocerebellar ataxia 26 . . . . . . . . . . . SCA30 . . . spinocerebellar ataxia 30 . . . . . . . . . . . SCA32 . . . spinocerebellar ataxia 32 . . . . . . . . . . . SCA37 . . . spinocerebellar ataxia 37 . . . . . . . . . . . SCAANT1 . . . SCA7/ATXN7 antisense RNA 1 . . . . . . . . . . . SCAF1 0.998787538768532 0.00121245780720822 3.42426007375842e-09 SR-related CTD associated factor 1 FUNCTION: May function in pre-mRNA splicing. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in fetal brain and liver, poorly expressed in salivary gland, heart, skin and ovary. Expressed in colorectal carcinomas and ovarian cancers. Overexpressed in colorectal carcinomas as compared to normal colonic mucosa. {ECO:0000269|PubMed:11461075, ECO:0000269|PubMed:15493872, ECO:0000269|PubMed:16631123, ECO:0000269|PubMed:17132108}.; lymphoreticular;medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland; . 0.19731 0.14899 . . 621.53803 5.02803 SCAF4 0.999999693301169 3.06698830689798e-07 5.9189509665223e-18 SR-related CTD associated factor 4 FUNCTION: May act to physically and functionally link transcription and pre-mRNA processing. {ECO:0000250}.; . . myocardium;ovary;colon;choroid;retina;uterus;prostate;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;urinary;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.76390 0.10408 -1.214341017 5.67940552 104.06406 2.20474 SCAF8 0.999999979124473 2.08755270838552e-08 4.20106177670743e-20 SR-related CTD associated factor 8 FUNCTION: May play a role in mRNA processing. {ECO:0000269|PubMed:11101529}.; . . . . 0.19849 . -0.947938165 9.341825902 330.90174 3.86879 SCAF11 0.999681330779109 0.000318669219798064 1.09321811246398e-12 SR-related CTD associated factor 11 FUNCTION: Plays a role in pre-mRNA alternative splicing by regulating spliceosome assembly. {ECO:0000269|PubMed:9447963}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9224939}.; myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;gum;thyroid;amniotic fluid;germinal center;bladder;brain;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;oesophagus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15562 0.10384 -0.20947578 37.78013682 1703.46208 7.61381 SCAI 0.999445289317284 0.000554710661865266 2.08512006316415e-11 suppressor of cancer cell invasion FUNCTION: Tumor suppressor which functions to suppress MKL1- induced SRF transcriptional activity. May function in the RHOA- DIAPH1 signal transduction pathway and regulate cell migration through transcriptional regulation of ITGB1. {ECO:0000269|PubMed:19350017}.; . . unclassifiable (Anatomical System);heart;pituitary gland;germinal center;brain; dorsal root ganglion;superior cervical ganglion;testis - interstitial;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.18559 0.09173 -0.492218069 22.35786742 2430.32407 9.15661 SCAMP1 0.842276280270073 0.157111881686367 0.000611838043559911 secretory carrier membrane protein 1 FUNCTION: Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in brain.; myocardium;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;meninges;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;pancreas;pia mater;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;head and neck;kidney;mammary gland;stomach; amygdala;dorsal root ganglion;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;hypothalamus;temporal lobe;pons;atrioventricular node;caudate nucleus;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;pituitary; 0.92895 0.10741 . . 145.44918 2.62753 SCAMP1-AS1 . . . SCAMP1 antisense RNA 1 . . . . . . . . . . . SCAMP2 0.383700654337713 0.614155078202478 0.00214426745980889 secretory carrier membrane protein 2 FUNCTION: Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface.; . TISSUE SPECIFICITY: Widely expressed.; myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;kidney;stomach; dorsal root ganglion;superior cervical ganglion;adrenal gland;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.22258 0.10471 -0.071520315 48.34866714 246.13705 3.38484 SCAMP3 0.0128944102681846 0.979868201497911 0.00723738823390423 secretory carrier membrane protein 3 FUNCTION: Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in heart and skeletal muscle.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; . 0.20650 0.11207 0.038710339 56.92380278 61.7518 1.60155 SCAMP4 0.0209517140380353 0.906256033169662 0.0727922527923031 secretory carrier membrane protein 4 FUNCTION: Probably involved in membrane protein trafficking. {ECO:0000250}.; . . ovary;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;spinal cord;lens;pancreas;lung;placenta;macula lutea;duodenum;cervix;spleen;kidney;mammary gland;stomach; superior cervical ganglion;skeletal muscle; . 0.10114 0.218717575 68.27081859 84.61618 1.95876 SCAMP5 0.345427472674241 0.640901302999504 0.0136712243262549 secretory carrier membrane protein 5 FUNCTION: Required for the calcium-dependent exocytosis of signal sequence-containing cytokines such as CCL5. Probably acts in cooperation with the SNARE machinery. May play a role in accumulation of expanded polyglutamine (polyQ) protein huntingtin (HTT) in case of endoplasmic reticulum stress by inhibiting the endocytosis pathway. {ECO:0000269|PubMed:19234194}.; . TISSUE SPECIFICITY: Expressed both by neuronal and non-neuronal tissues. Expressed in brain, stomach, thyroid, spinal cord, lymph node, trachea, adrenal gland, bone marrow and in the different parts of brain. In thyroid tissues, it is expressed by the follicular epithelial cells. In the adrenal gland tissues it is detected in the zona fasciculata of the cortex region (at protein level). {ECO:0000269|PubMed:19234194}.; ovary;colon;parathyroid;fovea centralis;choroid;retina;prostate;optic nerve;frontal lobe;testis;bladder;brain;unclassifiable (Anatomical System);cerebellum cortex;tongue;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;breast;lung;adrenal gland;placenta;macula lutea;hippocampus;liver;cervix;head and neck;mammary gland;stomach;cerebellum; amygdala;whole brain;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.43707 0.10923 -0.339715008 30.06605331 8.58338 0.31444 SCAND1 0.158311342081053 0.637347168481011 0.204341489437936 SCAN domain containing 1 FUNCTION: May regulate transcriptional activity.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;urinary;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; prostate;heart;liver; 0.13423 0.10407 . . 3.44037 0.12571 SCAND2P . . . SCAN domain containing 2 pseudogene . . . . . . . . . . . SCAND3P1 . . . SCAN domain containing 3 pseudogene 1 . . . . . . . . . . . SCAP 0.0225547504834219 0.977439846323477 5.40319310143232e-06 SREBF chaperone FUNCTION: Escort protein required for cholesterol as well as lipid homeostasis. Regulates export of the SCAP/SREBF complex from the ER upon low cholesterol. Formation of a ternary complex with INSIG at high sterol concentrations leads to masking of an ER-export signal in SCAP and retention of the complex in the ER. Low sterol concentrations trigger release of INSIG, a conformational change in the SSC domain of SCAP, unmasking of the ER export signal, recruitment into COPII-coated vesicles, transport to the Golgi complex, proteolytic cleavage of SREBF in the Golgi, release of the transcription factor fragment of SREBF from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway (By similarity). {ECO:0000250}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;bone;thyroid;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;muscle;urinary;adrenal cortex;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach; subthalamic nucleus;testis - seminiferous tubule;adrenal gland;cerebellum peduncles;adrenal cortex;liver;testis;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.05282 0.16079 -2.188305787 1.391837698 3410.40993 11.19013 SCAPER 0.0392828983920439 0.960717097692565 3.91539112023909e-09 S-phase cyclin A-associated protein in the ER FUNCTION: CCNA2/CDK2 regulatory protein that transiently maintains CCNA2 in the cytoplasm. {ECO:0000269|PubMed:17698606}.; . TISSUE SPECIFICITY: Widely expressed with highest expression in testis. {ECO:0000269|PubMed:17698606}.; smooth muscle;ovary;colon;parathyroid;choroid;fovea centralis;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;lens;skeletal muscle;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;macula lutea;liver;alveolus;spleen;kidney;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;fetal brain;globus pallidus;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.16013 0.10510 0.652163325 84.17669262 5691.45688 15.61350 SCAR2 . . . spinocerebellar ataxia, autosomal recessive 2 . . . . . . . . . . . SCAR3 . . . spinocerebellar ataxia, autosomal recessive 3 . . . . . . . . . . . SCAR6 . . . spinocerebellar ataxia, autosomal recessive 6 . . . . . . . . . . . SCARA3 1.62407014825429e-07 0.398384612515905 0.60161522507708 scavenger receptor class A member 3 FUNCTION: Seems to protect cells by scavenging oxidative molecules or harmful products of oxidation. {ECO:0000269|PubMed:9580669}.; . TISSUE SPECIFICITY: Expressed ubiquitously. {ECO:0000269|PubMed:9580669}.; smooth muscle;ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;whole body;optic nerve;larynx;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;spinal cord;lens;breast;lung;placenta;visual apparatus;macula lutea;liver;cervix;head and neck;spleen;kidney;aorta; occipital lobe;uterus corpus;pons;trigeminal ganglion; 0.17955 0.14273 -1.217968826 5.638122199 1127.00047 6.40337 SCARA5 0.0669917769697247 0.918822737046658 0.0141854859836173 scavenger receptor class A member 5 FUNCTION: Ferritin receptor that mediates non-transferrin- dependent delivery of iron. Mediates cellular uptake of ferritin- bound iron by stimulating ferritin endocytosis from the cell surface with consequent iron delivery within the cell. Delivery of iron to cells by ferritin is required for the development of specific cell types, suggesting the existence of cell type- specific mechanisms of iron traffic in organogenesis, which alternatively utilize transferrin or non-transferrin iron delivery pathways. Ferritin mediates iron uptake in capsule cells of the developing kidney. Binds preferrentially ferritin light chain (FTL) compared to heavy chain (FTH1) (By similarity). {ECO:0000250}.; . . uterus;lung;ovary;heart;cerebral cortex;placenta;alveolus;parathyroid;brain;skin;retina; . 0.18359 0.15428 0.621009802 83.41589998 1708.42502 7.62279 SCARB1 0.0772244034409674 0.920425202007706 0.00235039455132612 scavenger receptor class B member 1 FUNCTION: Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells. Probable receptor for HDL, located in particular region of the plasma membrane, called caveolae. Facilitates the flux of free and esterified cholesterol between the cell surface and extracellular donors and acceptors, such as HDL and to a lesser extent, apoB-containing lipoproteins and modified lipoproteins. Probably involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity. Receptor for hepatitis C virus glycoprotein E2. Binding between SCARB1 and E2 was found to be independent of the genotype of the viral isolate. Plays an important role in the uptake of HDL cholesteryl ester (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed.; medulla oblongata;ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;optic nerve;endometrium;bone;testis;germinal center;bladder;brain;spinal ganglion;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;urinary;adrenal cortex;lens;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach;thymus; superior cervical ganglion;adrenal gland;placenta;adrenal cortex;liver; 0.13741 0.09993 -0.156065314 42.16206653 1095.25197 6.33218 SCARB2 0.072442869057668 0.927026675026707 0.000530455915624696 scavenger receptor class B member 2 FUNCTION: Acts as a lysosomal receptor for glucosylceramidase (GBA) targeting. {ECO:0000269|PubMed:18022370}.; DISEASE: Epilepsy, progressive myoclonic 4, with or without renal failure (EPM4) [MIM:254900]: An autosomal recessive progressive myoclonic epilepsy associated with renal failure in some cases. Cognitive function is preserved. Myoclonus is a brief, involuntary twitching of a muscle or a group of muscles. {ECO:0000269|PubMed:18308289, ECO:0000269|PubMed:18424452, ECO:0000269|PubMed:19454373, ECO:0000269|PubMed:21670406}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Genetic variants in SCARB2 can act as modifier of the phenotypic expression and severity of Gaucher disease. {ECO:0000269|PubMed:21796727}.; . smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;brain;amygdala;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;atrium;oesophagus;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;bile duct;pancreas;lung;cornea;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.20980 0.44672 0.485092724 79.37603208 107.27576 2.24626 SCARF1 0.000660074291001061 0.994900347956307 0.00443957775269209 scavenger receptor class F member 1 FUNCTION: Mediates the binding and degradation of acetylated low density lipoprotein (Ac-LDL). Mediates heterophilic interactions, suggesting a function as adhesion protein. Plays a role in the regulation of neurite-like outgrowth (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Endothelial cells.; unclassifiable (Anatomical System);uterus;lung;bone;placenta;testis;stomach; superior cervical ganglion;ciliary ganglion; 0.10651 0.09834 2.337125365 98.40174569 1801.80436 7.82929 SCARF2 . . . scavenger receptor class F member 2 FUNCTION: Probable adhesion protein, which mediates homophilic and heterophilic interactions. In contrast to SCARF1, it poorly mediates the binding and degradation of acetylated low density lipoprotein (Ac-LDL) (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Predominantly expressed in endothelial cells. Expressed in heart, placenta, lung, kidney, spleen, small intestine and ovary. {ECO:0000269|PubMed:12154095}.; unclassifiable (Anatomical System);cartilage;heart;ovary;colon;blood;fovea centralis;choroid;lens;skin;skeletal muscle;retina;bone marrow;uterus;pancreas;optic nerve;whole body;lung;bone;macula lutea;visual apparatus;testis;kidney;brain;stomach; . 0.12308 0.14503 . . 3987.3511 12.48749 SCARNA1 . . . small Cajal body-specific RNA 1 . . . . . . . . . . . SCARNA2 . . . small Cajal body-specific RNA 2 . . . . . . . . . . . SCARNA3 . . . small Cajal body-specific RNA 3 . . . . . . . . . . . SCARNA4 . . . small Cajal body-specific RNA 4 . . . . . . . . . . . SCARNA5 . . . small Cajal body-specific RNA 5 . . . . . . . . . . . SCARNA6 . . . small Cajal body-specific RNA 6 . . . . . . . . . . . SCARNA7 . . . small Cajal body-specific RNA 7 . . . . . . . . . . . SCARNA8 . . . small Cajal body-specific RNA 8 . . . . . . . . . . . SCARNA9 . . . small Cajal body-specific RNA 9 . . . . . . . . . . . SCARNA9L . . . small Cajal body-specific RNA 9-like . . . . . . . . . . . SCARNA10 . . . small Cajal body-specific RNA 10 . . . . . . . . . . . SCARNA11 . . . small Cajal body-specific RNA 11 . . . . . . . . . . . SCARNA12 . . . small Cajal body-specific RNA 12 . . . . . . . . . . . SCARNA13 . . . small Cajal body-specific RNA 13 . . . . . . . . . . . SCARNA14 . . . small Cajal body-specific RNA 14 . . . . . . . . . . . SCARNA15 . . . small Cajal body-specific RNA 15 . . . . . . . . . . . SCARNA16 . . . small Cajal body-specific RNA 16 . . . . . . . . . . . SCARNA17 . . . small Cajal body-specific RNA 17 . . . . . . . . . . . SCARNA18 . . . small Cajal body-specific RNA 18 . . . . . . . . . . . SCARNA18B . . . small Cajal body-specific RNA 18B . . . . . . . . . . . SCARNA20 . . . small Cajal body-specific RNA 20 . . . . . . . . . . . SCARNA21 . . . small Cajal body-specific RNA 21 . . . . . . . . . . . SCARNA21B . . . small Cajal body-specific RNA 21B . . . . . . . . . . . SCARNA22 . . . small Cajal body-specific RNA 22 . . . . . . . . . . . SCARNA23 . . . small Cajal body-specific RNA 23 . . . . . . . . . . . SCARNA26A . . . small Cajal body-specific RNA 26A . . . . . . . . . . . SCARNA26B . . . small Cajal body-specific RNA 26B . . . . . . . . . . . SCARNA27 . . . small Cajal body-specific RNA 27 . . . . . . . . . . . SCARNA28 . . . small Cajal body-specific RNA 28 . . . . . . . . . . . SCASI . . . spinocerebellar ataxia with saccadic intrusions . . . . . . . . . . . SCAX2 . . . spinocerebellar ataxia, X-linked 2 . . . . . . . . . . . SCAX3 . . . spinocerebellar ataxia, X-linked 3 . . . . . . . . . . . SCAX4 . . . spinocerebellar ataxia, X-linked 4 . . . . . . . . . . . SCCPDH 0.0119007027684187 0.979976472933191 0.00812282429839009 saccharopine dehydrogenase (putative) . . . . . 0.35216 0.15876 0.262810045 70.43524416 266.21084 3.50062 SCD 0.887398175951616 0.112351005233195 0.000250818815189514 stearoyl-CoA desaturase (delta-9-desaturase) FUNCTION: Stearyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:15907797, PubMed:18765284). Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:15907797, PubMed:18765284). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:15610069). Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (By similarity). Plays an important role in body energy homeostasis (By similarity). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity). {ECO:0000250|UniProtKB:P13516, ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797, ECO:0000269|PubMed:18765284}.; . TISSUE SPECIFICITY: Detected in fetal liver, lung and brain. Highly expressed in adult adipose tissue, and at lower levels in adult brain and lung. {ECO:0000269|PubMed:15907797}.; . . 0.83098 0.57486 -0.095386216 46.48502005 303.58245 3.71253 SCD5 0.0050170857407118 0.886342962906167 0.108639951353122 stearoyl-CoA desaturase 5 FUNCTION: Stearyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:15907797, PubMed:15610069). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids. {ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797}.; . TISSUE SPECIFICITY: Detected in fetal brain, and at lower levels in fetal kidney. Detected in adult brain and pancreas, and at lower levels in kidney and lung. {ECO:0000269|PubMed:12727354, ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797}.; unclassifiable (Anatomical System);lymph node;frontal lobe;adrenal gland;islets of Langerhans;hypothalamus;thyroid;placenta;visual apparatus;hippocampus;testis;brain;bone marrow;retina; dorsal root ganglion;superior cervical ganglion;testis - interstitial;tongue;adrenal cortex;pons;atrioventricular node;skin;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;appendix;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.20616 0.29531 0.15257911 64.60839821 57.71886 1.53527 SCDP1 . . . stearoyl-CoA desaturase (delta-9-desaturase) pseudogene 1 . . . . . . . . . . . SCEL 5.00221967904975e-12 0.93244265304538 0.0675573469496178 sciellin FUNCTION: May function in the assembly or regulation of proteins in the cornified envelope. The LIM domain may be involved in homotypic or heterotypic associations and may function to localize sciellin to the cornified envelope.; . TISSUE SPECIFICITY: Highly expressed in esophagus. It is also expressed in keratinocytes, amniotic tissue, foreskin stratum spinosum and stratum granulosum, hair follicle and nail.; unclassifiable (Anatomical System);heart;tongue;skin;uterus;pancreas;prostate;whole body;lung;epididymis;thyroid;hypopharynx;head and neck;tonsil;stomach; tongue;tonsil;skeletal muscle;skin; 0.08151 0.10863 0.112125503 62.09601321 4220.39307 12.92629 SCEL-AS1 . . . SCEL antisense RNA 1 . . . . . . . . . . . SCFD1 0.991579193827834 0.00842080552105666 6.51109750810277e-10 sec1 family domain containing 1 FUNCTION: Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with COG4. Involved in vesicular transport between the endoplasmic reticulum and the Golgi (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pineal body;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; pons; 0.22735 0.11778 -0.179930907 40.35739561 171.75077 2.85758 SCFD2 1.8739349735319e-06 0.877188533187998 0.122809592877028 sec1 family domain containing 2 FUNCTION: May be involved in protein transport.; . . . . 0.06905 . -0.040377332 50.50719509 2760.73412 9.91817 SCG2 0.898323134283839 0.101484502576395 0.00019236313976627 secretogranin II FUNCTION: Secretogranin-2 is a neuroendocrine secretory granule protein, which is the precursor for biologically active peptides.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;prostate;whole body;frontal lobe;thyroid;pituitary gland;testis;ciliary body;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;islets of Langerhans;hypothalamus;pharynx;blood;bile duct;breast;pancreas;lung;mesenchyma;adrenal gland;placenta;hippocampus;liver;kidney;stomach; amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;subthalamic nucleus;hypothalamus;globus pallidus;caudate nucleus;pons;parietal lobe;cingulate cortex;pituitary; 0.83936 0.42313 -0.66859065 15.76433121 88.38054 2.01525 SCG3 0.267523893167639 0.731361730435435 0.00111437639692652 secretogranin III . . TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver and skeletal muscle. {ECO:0000269|PubMed:12098761}.; unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pineal body;spinal cord;blood;fovea centralis;skin;skeletal muscle;retina;bone marrow;uterus;optic nerve;whole body;lung;frontal lobe;adrenal gland;macula lutea;visual apparatus;liver;pituitary gland;testis;spinal ganglion;brain; whole brain;amygdala;occipital lobe;subthalamic nucleus;medulla oblongata;temporal lobe;prefrontal cortex;globus pallidus;pons;cingulate cortex;parietal lobe; 0.57631 0.13873 -0.314027422 31.9297004 852.61642 5.70504 SCG5 1.07115773193623e-05 0.351916724006038 0.648072564416643 secretogranin V FUNCTION: Acts as a molecular chaperone for PCSK2/PC2, preventing its premature activation in the regulated secretory pathway. Binds to inactive PCSK2 in the endoplasmic reticulum and facilitates its transport from there to later compartments of the secretory pathway where it is proteolytically matured and activated. Also required for cleavage of PCSK2 but does not appear to be involved in its folding. Plays a role in regulating pituitary hormone secretion. The C-terminal peptide inhibits PCSK2 in vitro. {ECO:0000269|PubMed:7913882}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;whole body;frontal lobe;thyroid;pituitary gland;testis;dura mater;pineal gland;brain;unclassifiable (Anatomical System);meninges;cartilage;cerebellum cortex;tongue;islets of Langerhans;hypothalamus;blood;pancreas;pia mater;lung;adrenal gland;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;mammary gland; whole brain;amygdala;occipital lobe;medulla oblongata;thalamus;superior cervical ganglion;cerebellum peduncles;hypothalamus;beta cell islets;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;pituitary;parietal lobe;cingulate cortex;cerebellum; 0.08270 0.16867 -0.207437529 38.2814343 28.24624 0.90638 SCGB1A1 0.00766133226097893 0.546810805004316 0.445527862734705 secretoglobin family 1A member 1 FUNCTION: Binds phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB) and weakly progesterone, potent inhibitor of phospholipase A2.; . TISSUE SPECIFICITY: Clara cells (nonciliated cells of the surface epithelium of the pulmonary airways).; prostate;lung;cartilage;nasopharynx;thyroid;testis;colon;brain;bone marrow; superior cervical ganglion;lung;trachea;fetal lung; 0.07297 0.25759 0.057118534 57.99716914 37.5233 1.11744 SCGB1B1P . . . secretoglobin family 1B member 1, pseudogene . . . . . . . . . . . SCGB1B2P . . . secretoglobin family 1B member 2, pseudogene . . . . . . . . . . . SCGB1B3P . . . secretoglobin family 1B member 3, pseudogene . . . . . . . . . . . SCGB1C1 3.34415917228498e-05 0.201950883252366 0.798015675155911 secretoglobin family 1C member 1 . . . kidney; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;parietal lobe;skeletal muscle; 0.10009 0.08616 0.637604436 83.77565464 3665.67427 11.76713 SCGB1C2 . . . secretoglobin family 1C member 2 . . . . . . . . . . . SCGB1D1 1.19495732132787e-05 0.114884604227347 0.885103446199439 secretoglobin family 1D member 1 FUNCTION: May bind androgens and other steroids, may also bind estramustine, a chemotherapeutic agent used for prostate cancer. May be under transcriptional regulation of steroid hormones.; . TISSUE SPECIFICITY: Expressed in lachrymal gland, thymus, kidney, testis, ovary and salivary gland.; lacrimal gland;adrenal gland;thyroid;adrenal cortex;parathyroid;pineal gland; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.00165 0.02412 0.525552348 80.57914603 8.46595 0.31038 SCGB1D2 0.0961136812474541 0.769802495252949 0.134083823499597 secretoglobin, family 1D member 2 FUNCTION: May bind androgens and other steroids, may also bind estramustine, a chemotherapeutic agent used for prostate cancer. May be under transcriptional regulation of steroid hormones.; . TISSUE SPECIFICITY: Highest expression was found in skeletal muscle. Expressed as well in thymus, trachea, kidney, steroid responsive tissues (prostate, testis, uterus, breast and ovary) and salivary gland.; unclassifiable (Anatomical System);uterus;lung;ovary;epididymis;testis;skeletal muscle; uterus;superior cervical ganglion;trigeminal ganglion;skin;skeletal muscle; 0.00801 . 0.080983847 59.76055674 416.60704 4.27169 SCGB1D4 0.00290219205998929 0.579170303468475 0.417927504471535 secretoglobin family 1D member 4 FUNCTION: Seems to be involved in the regulation of chemotactic cell migration and invasion.; . TISSUE SPECIFICITY: Expressed in all tissues; the highest level of expression is detectable in lymph nodes, tonsil, cultured lymphoblasts and ovary. {ECO:0000269|PubMed:15034037}.; endometrium;brain; . 0.01196 . 0.013025609 54.62962963 16.66822 0.58709 SCGB1D5P . . . secretoglobin family 1D member 5, pseudogene . . . . . . . . . . . SCGB2A1 0.0564012954624431 0.708281714087781 0.235316990449776 secretoglobin family 2A member 1 FUNCTION: May bind androgens and other steroids, may also bind estramustine, a chemotherapeutic agent used for prostate cancer. May be under transcriptional regulation of steroid hormones.; . TISSUE SPECIFICITY: Expressed in thymus, trachea, kidney, steroid responsive tissues (prostate, testis, uterus, breast and ovary) and salivary gland.; unclassifiable (Anatomical System);ovary;lacrimal gland;islets of Langerhans;adrenal cortex;parathyroid;skeletal muscle;uterus;prostate;endometrium;adrenal gland;thyroid;testis;kidney;pineal gland; uterus;uterus corpus;trachea;salivary gland;beta cell islets;testis; 0.27456 0.12204 -0.075159878 47.78839349 3.17887 0.11452 SCGB2A2 0.00892427737697349 0.579257967159164 0.411817755463862 secretoglobin family 2A member 2 . . TISSUE SPECIFICITY: Mammary gland specific. Over-expressed in breast cancer.; unclassifiable (Anatomical System);breast;lung;mammary gland; skin; 0.01525 . -0.229483771 36.86010852 12.79934 0.46553 SCGB2B1P . . . secretoglobin family 2B member 1, pseudogene . . . . . . . . . . . SCGB2B2 0.000675653451540748 0.302558352776053 0.696765993772406 secretoglobin family 2B member 2 . . . . . . . 0.369407109 74.95281906 6.80928 0.25116 SCGB2B3P . . . secretoglobin family 2B member 3, pseudogene . . . . . . . . . . . SCGB3A1 0.452637901767245 0.451084954113676 0.0962771441190791 secretoglobin family 3A member 1 FUNCTION: Potential growth inhibitory cytokine.; . TISSUE SPECIFICITY: Highly expressed in breast tissues. Absent in breast cancer cell lines.; unclassifiable (Anatomical System);prostate;lung;islets of Langerhans;testis;brain; . 0.06513 0.12353 0.035072054 56.2514744 15.03985 0.54032 SCGB3A2 0.0424274770547476 0.659705605136443 0.29786691780881 secretoglobin family 3A member 2 . . TISSUE SPECIFICITY: Highly expressed in lung.; unclassifiable (Anatomical System);uterus;lung;whole body;ovary;heart;larynx;placenta;parathyroid;spleen;head and neck;skin; . 0.02029 0.03000 -0.031067188 51.03798066 3.38036 0.12297 SCGN 0.0359460022848758 0.956319094418519 0.00773490329660551 secretagogin, EF-hand calcium binding protein . . TISSUE SPECIFICITY: Expressed at high levels in the pancreatic islets of Langerhans and to a much lesser extent in the gastrointestinal tract (stomach, small intestine and colon), the adrenal medulla and cortex and the thyroid C-cells. In the brain, the expression is restricted to distinct subtypes of neurons with highest expression in the molecular layer of the cerebellum (stellate and basket cells), in the anterior part of the pituitary gland, in the thalamus, in the hypothalamus and in a subgroup of neocortical neurons. {ECO:0000269|PubMed:11709487}.; unclassifiable (Anatomical System);prostate;pancreas;lung;islets of Langerhans;placenta;colon;substantia nigra;kidney;stomach; dorsal root ganglion;superior cervical ganglion;pancreas;cerebellum peduncles;hypothalamus;beta cell islets;atrioventricular node;pituitary;cerebellum; 0.06713 0.11112 0.373041938 75.29488087 235.09801 3.31377 SCHIP1 0.956602926491204 0.0432880550869552 0.000109018421840859 schwannomin interacting protein 1 . . TISSUE SPECIFICITY: Isoform 5 and isoform 6 are highly expressed in the brain. Both isoforms derive from naturally occurring readthrough transcripts which produce IQCJ-SCHIP1 fusion proteins. {ECO:0000269|PubMed:17045569}.; . . 0.29687 0.11322 -0.095386216 46.48502005 1.10092 0.02874 SCHLAP1 . . . SWI/SNF complex antagonist associated with prostate cancer 1 (non-protein coding) . . . . . . . . . . . SCIMP 0.0125753435020966 0.855696201900384 0.131728454597519 SLP adaptor and CSK interacting membrane protein FUNCTION: Lipid tetraspanin-associated transmembrane adapter/mediator involved in major histocompatibility complex (MHC) class II signaling transduction. Required in generating the calcium response and enhancing ERK activity upon MHC-II stimulation. {ECO:0000269|PubMed:21930792}.; . TISSUE SPECIFICITY: Expressed in antigen-presenting cells, like peripheral blood leukocytes and monocyte-derived dendritic cells (MDDC) (at protein level). Highly expressed in lymph nodes and spleen. Expressed in antigen-presenting cells. Faintly expressed in the majority of nonimmune system tissues. {ECO:0000269|PubMed:21930792}.; . . 0.13040 . -0.163345027 41.24793583 10.11893 0.36946 SCIN 4.08229993266863e-16 0.00153218745492042 0.998467812545079 scinderin FUNCTION: Ca(2+)-dependent actin filament-severing protein that is presumed to have a regulatory function in exocytosis by affecting the organization of the microfilament network underneath the plasma membrane. In vitro, also has barbed end capping and nucleating activities in the presence of Ca(2+). Regulates chondrocyte proliferation and differentiation. MAP kinases p38 and ERK1/2 mediate the adseverin-induced accelerated differentiation of non-hypertrophic chondrocytes (By similarity). {ECO:0000250}.; . . pancreas;lung;whole body;cartilage;bone;placenta;sympathetic chain;testis;cervix;kidney;skin;skeletal muscle;stomach; . 0.49689 0.12425 1.223576934 93.23543289 4912.87103 14.29790 SCKL3 . . . Seckel syndrome 3 . . . . . . . . . . . SCLT1 5.17317913653687e-12 0.78851849333812 0.211481506656707 sodium channel and clathrin linker 1 FUNCTION: Adapter protein that links SCN10A to clathrin. Regulates SCN10A channel activity, possibly by promoting channel internalization (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;ovary;tongue;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;breast;prostate;lung;frontal lobe;cochlea;endometrium;trabecular meshwork;liver;head and neck;kidney;brain;bladder;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.34487 0.09874 -0.064242613 48.844067 315.8929 3.77458 SCLY 1.52191274633036e-06 0.631915891763499 0.368082586323755 selenocysteine lyase FUNCTION: Catalyzes the decomposition of L-selenocysteine to L- alanine and elemental selenium. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;heart;skin;breast;pancreas;prostate;lung;placenta;testis;cervix;kidney;brain;stomach; superior cervical ganglion;testis - interstitial;appendix;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.39376 0.16550 0.224175308 68.48903043 1317.80679 6.82905 SCMH1 0.52410168415646 0.475868175482748 3.01403607927335e-05 sex comb on midleg homolog 1 (Drosophila) FUNCTION: Associates with Polycomb group (PcG) multiprotein complexes; the complex class is required to maintain the transcriptionally repressive state of some genes. {ECO:0000250}.; . TISSUE SPECIFICITY: Strongly expressed in heart, muscle and pancreas. Weakly expressed in brain, placenta, lung, liver and kidney. {ECO:0000269|PubMed:10524249}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion; 0.23981 0.10902 -0.731092527 14.13658882 85.71222 1.97588 SCML1 0.948610392136383 0.0512233467847535 0.000166261078863289 sex comb on midleg-like 1 (Drosophila) FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. May be involved in spermatogenesis during sexual maturation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in fetal and adult tissues. {ECO:0000269|PubMed:9570953}.; . . 0.02653 0.06729 -0.075159878 47.78839349 0.81944 0.01579 SCML2 0.998434048382124 0.00156592004428861 3.15735877897295e-08 sex comb on midleg-like 2 (Drosophila) FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in placenta, thymus and testis. Detected at lower levels in brain, liver, skeletal muscle, pancreas and ovary. {ECO:0000269|PubMed:10331946}.; unclassifiable (Anatomical System);cartilage;colon;skeletal muscle;uterus;lung;frontal lobe;cochlea;endometrium;larynx;placenta;liver;testis;head and neck;spleen;brain;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.12839 0.09503 -0.494039303 22.09247464 16.14895 0.57238 SCML2P1 . . . SCML2 pseudogene 1 . . . . . . . . . . . SCML2P2 . . . SCML2 pseudogene 2 . . . . . . . . . . . SCML4 0.268213054620722 0.706832050650507 0.0249548947287705 sex comb on midleg-like 4 (Drosophila) FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development (By similarity). {ECO:0000250}.; . . . . 0.42590 . -0.047654689 50.22410946 1266.26154 6.70668 SCN1A 0.999999999535395 4.64605137606285e-10 1.62257315008925e-25 sodium voltage-gated channel alpha subunit 1 FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient.; DISEASE: Generalized epilepsy with febrile seizures plus 2 (GEFS+2) [MIM:604403]: A rare autosomal dominant, familial condition with incomplete penetrance and large intrafamilial variability. Patients display febrile seizures persisting sometimes beyond the age of 6 years and/or a variety of afebrile seizure types. This disease combines febrile seizures, generalized seizures often precipitated by fever at age 6 years or more, and partial seizures, with a variable degree of severity. {ECO:0000269|PubMed:10742094, ECO:0000269|PubMed:11254444, ECO:0000269|PubMed:11254445, ECO:0000269|PubMed:11524484, ECO:0000269|PubMed:11756608, ECO:0000269|PubMed:12535936, ECO:0000269|PubMed:12576172, ECO:0000269|PubMed:12919402, ECO:0000269|PubMed:14672992, ECO:0000269|PubMed:15525788, ECO:0000269|PubMed:15694566, ECO:0000269|PubMed:15715999, ECO:0000269|PubMed:16525050, ECO:0000269|PubMed:17347258, ECO:0000269|PubMed:17507202, ECO:0000269|PubMed:17561957, ECO:0000269|PubMed:17927801, ECO:0000269|PubMed:18251839, ECO:0000269|PubMed:18413471, ECO:0000269|PubMed:18566737, ECO:0000269|PubMed:19339291, ECO:0000269|PubMed:19464195, ECO:0000269|PubMed:19522081, ECO:0000269|PubMed:20117752, ECO:0000269|PubMed:20550552, ECO:0000269|PubMed:20600615, ECO:0000269|PubMed:20729507, ECO:0000269|PubMed:21248271, ECO:0000269|PubMed:21864321}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epileptic encephalopathy, early infantile, 6 (EIEE6) [MIM:607208]: A severe form of epileptic encephalopathy characterized by generalized tonic, clonic, and tonic-clonic seizures that are initially induced by fever and begin during the first year of life. Later, patients also manifest other seizure types, including absence, myoclonic, and simple and complex partial seizures. Psychomotor development delay is observed around the second year of life. Some patients manifest a borderline disease phenotype and do not necessarily fulfill all diagnostic criteria for core EIEE6. EIEE6 is considered to be the most severe phenotype within the spectrum of generalized epilepsies with febrile seizures-plus. {ECO:0000269|PubMed:11359211, ECO:0000269|PubMed:12083760, ECO:0000269|PubMed:12566275, ECO:0000269|PubMed:12754708, ECO:0000269|PubMed:12821740, ECO:0000269|PubMed:14504318, ECO:0000269|PubMed:14738421, ECO:0000269|PubMed:15087100, ECO:0000269|PubMed:15944908, ECO:0000269|PubMed:16122630, ECO:0000269|PubMed:16458823, ECO:0000269|PubMed:16713920, ECO:0000269|PubMed:17054684, ECO:0000269|PubMed:17054685, ECO:0000269|PubMed:17129991, ECO:0000269|PubMed:17347258, ECO:0000269|PubMed:17561957, ECO:0000269|PubMed:18413471, ECO:0000269|PubMed:18639757, ECO:0000269|PubMed:18930999, ECO:0000269|PubMed:19522081, ECO:0000269|PubMed:19563458, ECO:0000269|PubMed:19589774, ECO:0000269|PubMed:19783390, ECO:0000269|PubMed:20110217, ECO:0000269|PubMed:20431604, ECO:0000269|PubMed:20452746, ECO:0000269|PubMed:20522430, ECO:0000269|PubMed:20729507, ECO:0000269|PubMed:21248271, ECO:0000269|PubMed:21864321, ECO:0000269|PubMed:22092154, ECO:0000269|PubMed:22612257, ECO:0000269|PubMed:23195492}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Intractable childhood epilepsy with generalized tonic- clonic seizures (ICEGTC) [MIM:607208]: A disorder characterized by generalized tonic-clonic seizures beginning usually in infancy and induced by fever. Seizures are associated with subsequent mental decline, as well as ataxia or hypotonia. ICEGTC is similar to SMEI, except for the absence of myoclonic seizures. {ECO:0000269|PubMed:12566275, ECO:0000269|PubMed:16210358, ECO:0000269|PubMed:17507202, ECO:0000269|PubMed:23195492}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Migraine, familial hemiplegic, 3 (FHM3) [MIM:609634]: A subtype of migraine associated with transient blindness in some families. Migraine is a disabling symptom complex of periodic headaches, usually temporal and unilateral. Headaches are often accompanied by irritability, nausea, vomiting and photophobia, preceded by constriction of the cranial arteries. The two major subtypes are common migraine (migraine without aura) and classic migraine (migraine with aura). Classic migraine is characterized by recurrent attacks of reversible neurological symptoms (aura) that precede or accompany the headache. Aura may include a combination of sensory disturbances, such as blurred vision, hallucinations, vertigo, numbness and difficulty in concentrating and speaking. {ECO:0000269|PubMed:16054936, ECO:0000269|PubMed:17397047, ECO:0000269|PubMed:18021921, ECO:0000269|PubMed:19332696}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Febrile seizures, familial, 3A (FEB3A) [MIM:604403]: Seizures associated with febrile episodes in childhood without any evidence of intracranial infection or defined pathologic or traumatic cause. It is a common condition, affecting 2-5% of children aged 3 months to 5 years. The majority are simple febrile seizures (generally defined as generalized onset, single seizures with a duration of less than 30 minutes). Complex febrile seizures are characterized by focal onset, duration greater than 30 minutes, and/or more than one seizure in a 24 hour period. The likelihood of developing epilepsy following simple febrile seizures is low. Complex febrile seizures are associated with a moderately increased incidence of epilepsy. {ECO:0000269|PubMed:16326807, ECO:0000269|PubMed:19522081}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=SCN1A mutations may be involved in Panayiotopoulos syndrome, a benign age-related focal seizure disorder occurring in early and mid-childhood. It is characterized by seizures, often prolonged, with predominantly autonomic symptoms, and by an electroencephalogram that shows shifting and/or multiple foci, often with occipital predominance. Autonomic seizures in Panayiotopoulos syndrome consist of episodes of disturbed autonomic function with emesis as the predominant symptom. Cardiorespiratory arrest is exceptional. {ECO:0000269|PubMed:17679682, ECO:0000269|PubMed:19339291, ECO:0000269|PubMed:19522081}.; . unclassifiable (Anatomical System);optic nerve;frontal lobe;hypothalamus;macula lutea;fovea centralis;choroid;lens;brain;skeletal muscle;retina; amygdala;occipital lobe;medulla oblongata;thalamus;subthalamic nucleus;temporal lobe;prefrontal cortex;globus pallidus;pons;cingulate cortex;parietal lobe; 0.25753 0.21408 -1.429430352 4.028072659 148.17021 2.65241 SCN1B 0.205166938448244 0.752173314342671 0.042659747209085 sodium voltage-gated channel beta subunit 1 FUNCTION: Crucial in the assembly, expression, and functional modulation of the heterotrimeric complex of the sodium channel. The subunit beta-1 can modulate multiple alpha subunit isoforms from brain, skeletal muscle, and heart. Its association with neurofascin may target the sodium channels to the nodes of Ranvier of developing axons and retain these channels at the nodes in mature myelinated axons. {ECO:0000269|PubMed:14622265}.; DISEASE: Brugada syndrome 5 (BRGDA5) [MIM:612838]: A tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs, the individual will faint and may die in a few minutes if the heart is not reset. {ECO:0000269|PubMed:18464934}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Atrial fibrillation, familial, 13 (ATFB13) [MIM:615377]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:19808477}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: The overall expression of isoforms 1 and 2 is very similar. Isoform 1 is abundantly expressed in skeletal muscle, heart and brain. Isoform 2 is highly expressed in brain and skeletal muscle and present at a very low level in heart, placenta, lung, liver, kidney and pancreas. In brain, isoform 2 is most abundant in the cerebellum, followed by the cerebral cortex and occipital lobe, while isoform 1 levels are higher in the cortex compared to the cerebellum. Isoform 2 is expressed in many regions of the brain, including cerebellar Purkinje cells, cortex pyramidal neurons and many of the neuronal fibers throughout the brain (at protein level). Also detected in dorsal root ganglion, in fibers of the spinal nerve and in cortical neurons and their processes (at protein level). {ECO:0000269|PubMed:14622265}.; unclassifiable (Anatomical System);heart;ovary;cartilage;islets of Langerhans;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;optic nerve;lung;frontal lobe;bone;macula lutea;hippocampus;testis;kidney;brain;mammary gland;thymus; . 0.17394 0.15823 0.617373774 83.25076669 1150.29546 6.46197 SCN2A 0.999999992314383 7.6856172010827e-09 1.50831673961379e-22 sodium voltage-gated channel alpha subunit 2 FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. {ECO:0000269|PubMed:1325650}.; DISEASE: Seizures, benign familial infantile 3 (BFIS3) [MIM:607745]: An autosomal dominant disorder in which afebrile seizures occur in clusters during the first year of life, without neurologic sequelae. {ECO:0000269|PubMed:11371648, ECO:0000269|PubMed:12243921, ECO:0000269|PubMed:15048894, ECO:0000269|PubMed:20371507, ECO:0000269|PubMed:22612257}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epileptic encephalopathy, early infantile, 11 (EIEE11) [MIM:613721]: An autosomal dominant seizure disorder characterized by neonatal or infantile onset of refractory seizures with resultant delayed neurologic development and persistent neurologic abnormalities. Patients may progress to West syndrome, which is characterized by tonic spasms with clustering, arrest of psychomotor development, and hypsarrhythmia on EEG. {ECO:0000269|PubMed:19783390, ECO:0000269|PubMed:19786696, ECO:0000269|PubMed:20956790, ECO:0000269|PubMed:23550958, ECO:0000269|PubMed:23935176}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);amygdala;cerebellum cortex;colon;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;lung;frontal lobe;bone;macula lutea;kidney;brain; amygdala;medulla oblongata;occipital lobe;cerebellum peduncles;temporal lobe;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.64580 0.34375 -1.98979551 1.769285209 693.6775 5.25209 SCN2B 0.133477243490071 0.780096154460408 0.0864266020495217 sodium voltage-gated channel beta subunit 2 FUNCTION: Crucial in the assembly, expression, and functional modulation of the heterotrimeric complex of the sodium channel. The subunit beta-2 causes an increase in the plasma membrane surface area and in its folding into microvilli. Interacts with TNR may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier (By similarity). {ECO:0000250}.; DISEASE: Note=Genetic variations in SCN2B may be involved in Brugada syndrome (PubMed:23559163). This tachyarrhythmia is characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs, the individual will faint and may die in a few minutes if the heart is not reset. {ECO:0000269|PubMed:23559163}.; TISSUE SPECIFICITY: Brain specific.; unclassifiable (Anatomical System);heart;placenta;brain;skeletal muscle;cerebellum; whole brain;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;globus pallidus;appendix;cingulate cortex;cerebellum; 0.21416 0.13285 -0.449946534 24.00330267 11.26886 0.40612 SCN3A 0.999999992847256 7.15274359517823e-09 1.26613451910626e-22 sodium voltage-gated channel alpha subunit 3 FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient.; . . unclassifiable (Anatomical System);lung;adrenal gland;thyroid;visual apparatus;kidney;brain;skin;skeletal muscle;peripheral nerve; amygdala;occipital lobe;medulla oblongata;subthalamic nucleus;fetal brain;hypothalamus;prefrontal cortex;caudate nucleus; 0.58721 0.10604 -2.475079584 0.973106865 555.03286 4.78678 SCN3B 0.347297034219147 0.639223622250792 0.0134793435300608 sodium voltage-gated channel beta subunit 3 FUNCTION: Modulates channel gating kinetics. Causes unique persistent sodium currents. Inactivates the sodium channel opening more slowly than the subunit beta-1. Its association with neurofascin may target the sodium channels to the nodes of Ranvier of developing axons and retain these channels at the nodes in mature myelinated axons (By similarity). {ECO:0000250}.; DISEASE: Atrial fibrillation, familial, 16 (ATFB16) [MIM:613120]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:20558140, ECO:0000269|PubMed:21051419}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the atrium. {ECO:0000269|PubMed:21051419}.; unclassifiable (Anatomical System);amygdala;heart;ovary;tongue;islets of Langerhans;sympathetic chain;parathyroid;skin;retina;uterus;lung;frontal lobe;adrenal gland;placenta;visual apparatus;pituitary gland;hypopharynx;liver;testis;head and neck;brain;aorta; whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.14484 0.14928 -0.273576253 33.97027601 12.44522 0.45171 SCN4A 0.0104419346692469 0.989557925956649 1.39374103691317e-07 sodium voltage-gated channel alpha subunit 4 FUNCTION: This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. This sodium channel may be present in both denervated and innervated skeletal muscle.; DISEASE: Paramyotonia congenita of von Eulenburg (PMC) [MIM:168300]: An autosomal dominant channelopathy characterized by myotonia, increased by exposure to cold, intermittent flaccid paresis, not necessarily dependent on cold or myotonia, lability of serum potassium, non-progressive nature and lack of atrophy or hypertrophy of muscles. In some patients, myotonia is not increased by cold exposure (paramyotonia without cold paralysis). Patients may have a combination phenotype of PMC and HYPP. {ECO:0000269|PubMed:10369308, ECO:0000269|PubMed:10727489, ECO:0000269|PubMed:1310898, ECO:0000269|PubMed:1316765, ECO:0000269|PubMed:1338909, ECO:0000269|PubMed:15318338, ECO:0000269|PubMed:15790667, ECO:0000269|PubMed:16786525, ECO:0000269|PubMed:18166706, ECO:0000269|PubMed:19077043, ECO:0000269|PubMed:20076800, ECO:0000269|PubMed:8242056, ECO:0000269|PubMed:8308722, ECO:0000269|PubMed:8388676, ECO:0000269|PubMed:8580427}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Periodic paralysis hypokalemic 2 (HOKPP2) [MIM:613345]: An autosomal dominant disorder manifested by episodic flaccid generalized muscle weakness associated with falls of serum potassium levels. {ECO:0000269|PubMed:10599760, ECO:0000269|PubMed:10851391, ECO:0000269|PubMed:10944223, ECO:0000269|PubMed:11558801, ECO:0000269|PubMed:11591859, ECO:0000269|PubMed:16890191, ECO:0000269|PubMed:17898326, ECO:0000269|PubMed:18162704, ECO:0000269|PubMed:19118277, ECO:0000269|PubMed:20522878, ECO:0000269|PubMed:21043388}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Periodic paralysis hyperkalemic (HYPP) [MIM:170500]: An autosomal dominant channelopathy characterized by episodic flaccid generalized muscle weakness associated with high levels of serum potassium. Concurrence of myotonia is found in HYPP patients. {ECO:0000269|PubMed:1659668, ECO:0000269|PubMed:1659948, ECO:0000269|PubMed:20076800, ECO:0000269|PubMed:7695243}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Periodic paralysis normokalemic (NKPP) [MIM:170500]: A disorder closely related to hyperkalemic periodic paralysis, but marked by a lack of alterations in potassium levels during attacks of muscle weakness. {ECO:0000269|PubMed:15596759, ECO:0000269|PubMed:18046642, ECO:0000269|PubMed:20522878}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myotonia SCN4A-related (MYOSCN4A) [MIM:608390]: A phenotypically highly variable myotonia aggravated by potassium loading, and sometimes by cold. Myotonia is characterized by sustained muscle tensing that prevents muscles from relaxing normally. It causes muscle stiffness that can interfere with movement. In some people the stiffness is very mild, while in other cases it may be severe enough to interfere with walking, running, and other activities of daily life. Myotonia SCN4A- related includes myotonia permanens and myotonia fluctuans. In myotonia permanens, the myotonia is generalized and there is a hypertrophy of the muscle, particularly in the neck and the shoulder. Attacks of severe muscle stiffness of the thoracic muscles may be life threatening due to impaired ventilation. In myotonia fluctuans, the muscle stiffness may fluctuate from day to day, provoked by exercise. {ECO:0000269|PubMed:10218481, ECO:0000269|PubMed:16786525, ECO:0000269|PubMed:16832098, ECO:0000269|PubMed:17212350, ECO:0000269|PubMed:17998485, ECO:0000269|PubMed:18203179, ECO:0000269|PubMed:18337100, ECO:0000269|PubMed:19015483, ECO:0000269|PubMed:19347921, ECO:0000269|PubMed:20076800, ECO:0000269|PubMed:8058156, ECO:0000269|PubMed:9392583}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myasthenic syndrome, congenital, 16 (CMS16) [MIM:614198]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness. CMS16 is characterized by fatigable generalized weakness and recurrent attacks of respiratory and bulbar paralysis since birth. The fatigable weakness involves lid-elevator, external ocular, facial, limb and truncal muscles and an decremental response of the compound muscle action potential on repetitive stimulation. {ECO:0000269|PubMed:12766226}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.13221 0.33815 -0.751649942 13.67657466 461.6219 4.45606 SCN4B 0.00153522738620452 0.683080229153547 0.315384543460249 sodium voltage-gated channel beta subunit 4 FUNCTION: Modulates channel gating kinetics. Causes negative shifts in the voltage dependence of activation of certain alpha sodium channels, but does not affect the voltage dependence of inactivation. Modulates the suceptibility of the sodium channel to inhibition by toxic peptides from spider, scorpion, wasp and sea anemone venom. {ECO:0000269|PubMed:24297919}.; DISEASE: Long QT syndrome 10 (LQT10) [MIM:611819]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. {ECO:0000269|PubMed:17592081}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Atrial fibrillation, familial, 17 (ATFB17) [MIM:611819]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:23604097}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at a high level in dorsal root ganglia, at a lower level in brain, spinal cord, skeletal muscle and heart. Expressed in the atrium. {ECO:0000269|PubMed:12930796, ECO:0000269|PubMed:21051419}.; unclassifiable (Anatomical System);prostate;pancreas;frontal lobe;cartilage;tongue;hippocampus;head and neck;brain;skeletal muscle;retina; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22248 0.12747 -0.383807564 27.41802312 17.78887 0.62155 SCN5A 0.995747526532478 0.00425247346731697 2.05430012390677e-13 sodium voltage-gated channel alpha subunit 5 FUNCTION: This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant Na(+) channel isoform. This channel is responsible for the initial upstroke of the action potential. Channel inactivation is regulated by intracellular calcium levels. {ECO:0000269|PubMed:19074138}.; DISEASE: Progressive familial heart block 1A (PFHB1A) [MIM:113900]: A cardiac bundle branch disorder characterized by progressive alteration of cardiac conduction through the His- Purkinje system, with a pattern of a right bundle-branch block and/or left anterior hemiblock occurring individually or together. It leads to complete atrio-ventricular block causing syncope and sudden death. {ECO:0000269|PubMed:12569159, ECO:0000269|PubMed:12574143, ECO:0000269|PubMed:19251209}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Long QT syndrome 3 (LQT3) [MIM:603830]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. {ECO:0000269|PubMed:10377081, ECO:0000269|PubMed:10508990, ECO:0000269|PubMed:10627139, ECO:0000269|PubMed:10911008, ECO:0000269|PubMed:10973849, ECO:0000269|PubMed:11304498, ECO:0000269|PubMed:11997281, ECO:0000269|PubMed:12209021, ECO:0000269|PubMed:12673799, ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:16414944, ECO:0000269|PubMed:16922724, ECO:0000269|PubMed:18060054, ECO:0000269|PubMed:18708744, ECO:0000269|PubMed:18848812, ECO:0000269|PubMed:18929331, ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:7651517, ECO:0000269|PubMed:7889574, ECO:0000269|PubMed:8541846, ECO:0000269|PubMed:9506831, ECO:0000269|PubMed:9686753, ECO:0000269|Ref.31}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Brugada syndrome 1 (BRGDA1) [MIM:601144]: A tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs, the individual will faint and may die in a few minutes if the heart is not reset. {ECO:0000269|PubMed:11748104, ECO:0000269|PubMed:11901046, ECO:0000269|PubMed:12051963, ECO:0000269|PubMed:12106943, ECO:0000269|PubMed:15023552, ECO:0000269|PubMed:15338453, ECO:0000269|PubMed:15579534, ECO:0000269|PubMed:15851320, ECO:0000269|PubMed:16266370, ECO:0000269|PubMed:16325048, ECO:0000269|PubMed:16616735, ECO:0000269|PubMed:17075016, ECO:0000269|PubMed:17081365, ECO:0000269|PubMed:17198989, ECO:0000269|PubMed:18252757, ECO:0000269|PubMed:18341814, ECO:0000269|PubMed:18451998, ECO:0000269|PubMed:18456723, ECO:0000269|PubMed:18616619, ECO:0000269|PubMed:19251209, ECO:0000269|PubMed:19272188, ECO:0000269|PubMed:20129283, ECO:0000269|PubMed:9521325}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Sick sinus syndrome 1 (SSS1) [MIM:608567]: The term 'sick sinus syndrome' encompasses a variety of conditions caused by sinus node dysfunction. The most common clinical manifestations are syncope, presyncope, dizziness, and fatigue. Electrocardiogram typically shows sinus bradycardia, sinus arrest, and/or sinoatrial block. Episodes of atrial tachycardias coexisting with sinus bradycardia ('tachycardia-bradycardia syndrome') are also common in this disorder. SSS occurs most often in the elderly associated with underlying heart disease or previous cardiac surgery, but can also occur in the fetus, infant, or child without heart disease or other contributing factors. SSS1 onset is in utero, infancy, or early childhood. {ECO:0000269|PubMed:14523039, ECO:0000269|PubMed:22795782}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Familial paroxysmal ventricular fibrillation 1 (VF1) [MIM:603829]: A cardiac arrhythmia marked by fibrillary contractions of the ventricular muscle due to rapid repetitive excitation of myocardial fibers without coordinated contraction of the ventricle and by absence of atrial activity. {ECO:0000269|PubMed:10940383}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Sudden infant death syndrome (SIDS) [MIM:272120]: SIDS is the sudden death of an infant younger than 1 year that remains unexplained after a thorough case investigation, including performance of a complete autopsy, examination of the death scene, and review of clinical history. Pathophysiologic mechanisms for SIDS may include respiratory dysfunction, cardiac dysrhythmias, cardiorespiratory instability, and inborn errors of metabolism, but definitive pathogenic mechanisms precipitating an infant sudden death remain elusive. {ECO:0000269|PubMed:18596570, ECO:0000269|PubMed:19302788}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Atrial standstill 1 (ATRST1) [MIM:108770]: A rare arrhythmia characterized by the absence of electrical and mechanical activity in the atria. Electrocardiographically, it is characterized by bradycardia, the absence of P waves, and a junctional narrow complex escape rhythm. {ECO:0000269|PubMed:12522116}. Note=The disease may be caused by mutations affecting distinct genetic loci, including the gene represented in this entry. A mutation in SCN5A has been detected in combination with a rare GJA5 genotype in a large family with atrial standstill.; DISEASE: Cardiomyopathy, dilated 1E (CMD1E) [MIM:601154]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:15466643}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Atrial fibrillation, familial, 10 (ATFB10) [MIM:614022]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:18088563, ECO:0000269|PubMed:18378609}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in jejunal circular smooth muscle cells (at protein level). Expressed in human atrial and ventricular cardiac muscle but not in adult skeletal muscle, brain, myometrium, liver, or spleen. Isoform 4 is expressed in brain. {ECO:0000269|PubMed:12358675}.; unclassifiable (Anatomical System);ovary;heart;endometrium; superior cervical ganglion;heart; 0.27349 0.25781 -1.881883902 1.987497051 1128.17048 6.40726 SCN7A 1.72076245416042e-15 0.304316363118635 0.695683636881363 sodium voltage-gated channel alpha subunit 7 FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient.; . TISSUE SPECIFICITY: Heart and uterus.; unclassifiable (Anatomical System);lung;islets of Langerhans;testis;skeletal muscle; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07774 0.09397 0.859723513 88.57041755 781.90454 5.53258 SCN8A 0.999998290292746 1.70970725378775e-06 3.22224477833524e-18 sodium voltage-gated channel alpha subunit 8 FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. In macrophages and melanoma cells, isoform 5 may participate in the control of podosome and invadopodia formation. {ECO:0000269|PubMed:19136557}.; DISEASE: Cognitive impairment with or without cerebellar ataxia (CIAT) [MIM:614306]: A disorder characterized by markedly delayed cognitive and motor development, attention deficit disorder, and cerebellar ataxia. Features include bilateral esophoria, strabismatic amblyopia, unsustained gaze evoked nystagmus on horizontal gaze, ataxic gait, dysmetria in the upper limbs and dysarthria, with normal strength, tone, and reflexes. {ECO:0000269|PubMed:16236810}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epileptic encephalopathy, early infantile, 13 (EIEE13) [MIM:614558]: A form of epilepsy characterized by frequent tonic seizures or spasms beginning in infancy with a specific EEG finding of suppression-burst patterns, characterized by high- voltage bursts alternating with almost flat suppression phases. Patients may progress to West syndrome, which is characterized by tonic spasms with clustering, arrest of psychomotor development, and hypsarrhythmia on EEG. EIEE13 is a severe form consisting of early-onset seizures, features of autism, intellectual disability, ataxia, and sudden unexplained death in epilepsy. {ECO:0000269|PubMed:22365152, ECO:0000269|PubMed:24352161, ECO:0000269|PubMed:24874546, ECO:0000269|PubMed:24888894, ECO:0000269|PubMed:25239001}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 5 is expressed in non-neuronal tissues, such as monocytes/macrophages. {ECO:0000269|PubMed:19136557}.; heart;fovea centralis;choroid;lens;retina;breast;optic nerve;lung;frontal lobe;macula lutea;alveolus;liver;bladder;brain; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.60310 0.25451 -1.749006627 2.341354093 100.07778 2.16874 SCN9A 9.30185484244833e-13 0.998502198437561 0.00149780156150877 sodium voltage-gated channel alpha subunit 9 FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-sensitive Na(+) channel isoform. Plays a role in pain mechanisms, especially in the development of inflammatory pain (By similarity). {ECO:0000250, ECO:0000269|PubMed:15178348, ECO:0000269|PubMed:7720699}.; DISEASE: Primary erythermalgia (PERYTHM) [MIM:133020]: Autosomal dominant disease characterized by recurrent episodes of severe pain associated with redness and warmth in the feet or hands. {ECO:0000269|PubMed:14985375, ECO:0000269|PubMed:15955112, ECO:0000269|PubMed:15958509, ECO:0000269|PubMed:16216943, ECO:0000269|PubMed:16392115, ECO:0000269|PubMed:18945915, ECO:0000269|PubMed:19369487, ECO:0000269|PubMed:24311784}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Indifference to pain, congenital, autosomal recessive (CIP) [MIM:243000]: A disorder characterized by congenital inability to perceive any form of pain, in any part of the body. All other sensory modalities are preserved and the peripheral and central nervous systems are apparently intact. Patients perceive the sensations of touch, warm and cold temperature, proprioception, tickle and pressure, but not painful stimuli. There is no evidence of a motor or sensory neuropathy, either axonal or demyelinating. {ECO:0000269|PubMed:20635406}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Paroxysmal extreme pain disorder (PEPD) [MIM:167400]: Autosomal dominant paroxysmal disorder of pain and autonomic dysfunction. The distinctive features are paroxysmal episodes of burning pain in the rectal, ocular, and mandibular areas accompanied by autonomic manifestations such as skin flushing. {ECO:0000269|PubMed:17145499, ECO:0000269|PubMed:18945915, ECO:0000269|PubMed:25285947}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Generalized epilepsy with febrile seizures plus 7 (GEFS+7) [MIM:613863]: A rare autosomal dominant, familial condition with incomplete penetrance and large intrafamilial variability. Patients display febrile seizures persisting sometimes beyond the age of 6 years and/or a variety of afebrile seizure types. This disease combines febrile seizures, generalized seizures often precipitated by fever at age 6 years or more, and partial seizures, with a variable degree of severity. {ECO:0000269|PubMed:19763161}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Febrile seizures, familial, 3B (FEB3B) [MIM:613863]: Seizures associated with febrile episodes in childhood without any evidence of intracranial infection or defined pathologic or traumatic cause. It is a common condition, affecting 2-5% of children aged 3 months to 5 years. The majority are simple febrile seizures (generally defined as generalized onset, single seizures with a duration of less than 30 minutes). Complex febrile seizures are characterized by focal onset, duration greater than 30 minutes, and/or more than one seizure in a 24 hour period. The likelihood of developing epilepsy following simple febrile seizures is low. Complex febrile seizures are associated with a moderately increased incidence of epilepsy. {ECO:0000269|PubMed:19763161}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed strongly in dorsal root ganglion, with only minor levels elsewhere in the body, smooth muscle cells, MTC cell line and C-cell carcinoma. Isoform 1 is expressed preferentially in the central and peripheral nervous system. Isoform 2 is expressed preferentially in the dorsal root ganglion. {ECO:0000269|PubMed:15178348, ECO:0000269|PubMed:15302875, ECO:0000269|PubMed:7720699, ECO:0000269|PubMed:9169448}.; unclassifiable (Anatomical System);lung;frontal lobe;cartilage;ovary;larynx;bone;placenta;liver;parathyroid;head and neck; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skin;skeletal muscle; 0.32351 0.19894 0.334233824 73.62585515 2905.67056 10.22513 SCN10A 6.14214934293813e-26 0.0324752357721617 0.967524764227838 sodium voltage-gated channel alpha subunit 10 FUNCTION: Tetrodotoxin-resistant channel that mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium- selective channel through which sodium ions may pass in accordance with their electrochemical gradient. Plays a role in neuropathic pain mechanisms. {ECO:0000269|PubMed:9839820}.; DISEASE: Episodic pain syndrome, familial, 2 (FEPS2) [MIM:615551]: An autosomal dominant neurologic disorder characterized by adult- onset of paroxysmal pain mainly affecting the distal lower extremities. {ECO:0000269|PubMed:23115331}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the dorsal root ganglia and sciatic nerve. {ECO:0000269|PubMed:9839820}.; . . 0.19023 0.09704 -1.323279302 4.735786742 1695.64989 7.59207 SCN11A 2.51866017251712e-19 0.922637770446685 0.0773622295533153 sodium voltage-gated channel alpha subunit 11 FUNCTION: This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which sodium ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant sodium channel isoform. Also involved, with the contribution of the receptor tyrosine kinase NTRK2, in rapid BDNF-evoked neuronal depolarization. {ECO:0000269|PubMed:10580103, ECO:0000269|PubMed:12384689}.; DISEASE: Neuropathy, hereditary sensory and autonomic, 7 (HSAN7) [MIM:615548]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by sensory and/or autonomic abnormalities. HSAN7 is characterized by congenital inability to experience pain resulting in self-mutilations, slow-healing wounds, and multiple painless fractures. mild muscle weakness, delayed motor development, slightly reduced motor and sensory nerve conduction velocities, hyperhidrosis and gastrointestinal dysfunction. {ECO:0000269|PubMed:24036948}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Episodic pain syndrome, familial, 3 (FEPS3) [MIM:615552]: An autosomal dominant neurologic disorder characterized by paroxysmal pain mainly affecting the distal lower extremities and occasionally the upper body, especially the joints of fingers and arms. The pain is exacerbated with fatigue. {ECO:0000269|PubMed:24207120}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the dorsal root ganglia and trigeminal ganglia, olfactory bulb, hippocampus, cerebellar cortex, spinal cord, spleen, small intestine and placenta. {ECO:0000269|PubMed:10623608, ECO:0000269|PubMed:15302875}.; lung;whole body;testis; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.04740 . -1.822830336 2.140835103 421.59129 4.28776 SCNM1 4.72848403910251e-05 0.862053613423874 0.137899101735735 sodium channel modifier 1 FUNCTION: Plays a role in RNA splicing, possibly contributing to the recognition of non-consensus donor sites. {ECO:0000250}.; . . . . 0.11055 0.11270 0.349177632 74.18023119 171.77934 2.85801 SCNN1A 9.40050560868697e-06 0.996643008254681 0.00334759123971021 sodium channel epithelial 1 alpha subunit FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception. {ECO:0000269|PubMed:24124190, ECO:0000269|PubMed:8278374}.; DISEASE: Pseudohypoaldosteronism 1, autosomal recessive (PHA1B) [MIM:264350]: A rare salt wasting disease resulting from target organ unresponsiveness to mineralocorticoids. PHA1B is a severe form involving multiple organ systems, and characterized by an often fulminant presentation in the neonatal period with dehydration, hyponatremia, hyperkalemia, metabolic acidosis, failure to thrive and weight loss. {ECO:0000269|PubMed:10586178, ECO:0000269|PubMed:15853823, ECO:0000269|PubMed:18634878}. Note=The disease is caused by mutations affecting the gene represented in this entry. The degree of channel function impairment differentially affects the renin-aldosterone system and urinary Na/K ratios, resulting in distinct genotype-phenotype relationships in PHA1 patients. Loss-of-function mutations are associated with a severe clinical course and age-dependent hyperactivation of the renin-aldosterone system. This feature is not observed in patients with missense mutations that reduce but do not eliminate channel function. Markedly reduced channel activity results in impaired linear growth and delayed puberty (PubMed:18634878). {ECO:0000269|PubMed:18634878}.; DISEASE: Bronchiectasis with or without elevated sweat chloride 2 (BESC2) [MIM:613021]: A debilitating respiratory disease characterized by chronic, abnormal dilatation of the bronchi and other cystic fibrosis-like symptoms in the absence of known causes of bronchiectasis (cystic fibrosis, autoimmune diseases, ciliary dyskinesia, common variable immunodeficiency, foreign body obstruction). Clinical features include sub-normal lung function, sinopulmonary infections, chronic productive cough, excessive sputum production, and elevated sweat chloride in some cases. {ECO:0000269|PubMed:19462466}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the female reproductive tract, from the fimbrial end of the fallopian tube to the endometrium (at protein level). Expressed in kidney (at protein level). In the respiratory tract, expressed in the bronchial epithelium (at protein level). Highly expressed in lung. Detected at intermediate levels in pancreas and liver, and at low levels in heart and placenta. Isoform 1 and isoform 2 predominate in all tissues. Expression of isoform 3, isoform 4 and isoform 5 is very low or not detectable, except in lung and heart. {ECO:0000269|PubMed:22207244, ECO:0000269|PubMed:9575806}.; ovary;colon;bone marrow;retina;uterus;prostate;oesophagus;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;blood;lens;breast;pancreas;lung;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;prostate;lung;trachea;tongue;thyroid;globus pallidus;pons;kidney;atrioventricular node;fetal thyroid; 0.97023 0.29005 0.268267497 70.64166077 2083.23781 8.40614 SCNN1B 0.000701536553027014 0.995227464356569 0.004070999090404 sodium channel epithelial 1 beta subunit FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception. {ECO:0000269|PubMed:7762608, ECO:0000303|PubMed:7490094}.; DISEASE: Pseudohypoaldosteronism 1, autosomal recessive (PHA1B) [MIM:264350]: A rare salt wasting disease resulting from target organ unresponsiveness to mineralocorticoids. PHA1B is a severe form involving multiple organ systems, and characterized by an often fulminant presentation in the neonatal period with dehydration, hyponatremia, hyperkalemia, metabolic acidosis, failure to thrive and weight loss. {ECO:0000269|PubMed:8589714}. Note=The disease is caused by mutations affecting the gene represented in this entry. The degree of channel function impairment differentially affects the renin-aldosterone system and urinary Na/K ratios, resulting in distinct genotype-phenotype relationships in PHA1 patients. Loss-of-function mutations are associated with a severe clinical course and age-dependent hyperactivation of the renin-aldosterone system. This feature is not observed in patients with missense mutations that reduce but do not eliminate channel function. Markedly reduced channel activity results in impaired linear growth and delayed puberty (PubMed:18634878). {ECO:0000269|PubMed:18634878}.; DISEASE: Liddle syndrome (LIDLS) [MIM:177200]: An autosomal dominant disorder characterized by hypertension, hypokalemic alkalosis, and suppression of plasma renin activity and aldosterone secretion. {ECO:0000269|PubMed:15483078, ECO:0000269|PubMed:7550319, ECO:0000269|PubMed:8524790, ECO:0000269|PubMed:8601645, ECO:0000269|PubMed:9626162, ECO:0000269|PubMed:9794716}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bronchiectasis with or without elevated sweat chloride 1 (BESC1) [MIM:211400]: A debilitating respiratory disease characterized by chronic, abnormal dilatation of the bronchi and other cystic fibrosis-like symptoms in the absence of known causes of bronchiectasis (cystic fibrosis, autoimmune diseases, ciliary dyskinesia, common variable immunodeficiency, foreign body obstruction). Clinical features include sub-normal lung function, sinopulmonary infections, chronic productive cough, excessive sputum production, and elevated sweat chloride in some cases. {ECO:0000269|PubMed:16207733, ECO:0000269|PubMed:18507830, ECO:0000269|PubMed:19017867}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in placenta, lung and kidney (PubMed:7762608). Expressed in kidney (at protein level) (PubMed:22207244). {ECO:0000269|PubMed:22207244, ECO:0000269|PubMed:7762608}.; unclassifiable (Anatomical System);lymph node;heart;ovary;islets of Langerhans;colon;parathyroid;choroid;skin;uterus;pancreas;prostate;optic nerve;lung;endometrium;placenta;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;placenta;globus pallidus;atrioventricular node;skeletal muscle; 0.67830 0.26884 0.159856957 64.91507431 204.40277 3.08872 SCNN1D 2.82187066585139e-15 0.00478257645975459 0.995217423540243 sodium channel epithelial 1 delta subunit FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception. {ECO:0000269|PubMed:16423824, ECO:0000269|PubMed:7499195}.; . . unclassifiable (Anatomical System);medulla oblongata;ovary;islets of Langerhans;blood;fovea centralis;choroid;lens;retina;optic nerve;lung;placenta;bone;macula lutea;testis;brain; superior cervical ganglion;medulla oblongata;temporal lobe;pons;trigeminal ganglion; 0.70009 0.14008 1.771089818 96.77990092 880.06096 5.77750 SCNN1G 0.368698568765529 0.631202052246918 9.93789875525946e-05 sodium channel epithelial 1 gamma subunit FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception. {ECO:0000269|PubMed:24124190, ECO:0000303|PubMed:7490094}.; DISEASE: Liddle syndrome (LIDLS) [MIM:177200]: An autosomal dominant disorder characterized by hypertension, hypokalemic alkalosis, and suppression of plasma renin activity and aldosterone secretion. {ECO:0000269|PubMed:7550319}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bronchiectasis with or without elevated sweat chloride 3 (BESC3) [MIM:613071]: A debilitating respiratory disease characterized by chronic, abnormal dilatation of the bronchi and other cystic fibrosis-like symptoms in the absence of known causes of bronchiectasis (cystic fibrosis, autoimmune diseases, ciliary dyskinesia, common variable immunodeficiency, foreign body obstruction). Clinical features include sub-normal lung function, sinopulmonary infections, chronic productive cough, excessive sputum production, and elevated sweat chloride in some cases. {ECO:0000269|PubMed:18507830, ECO:0000269|PubMed:19017867}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in kidney (at protein level). {ECO:0000269|PubMed:22207244}.; unclassifiable (Anatomical System);breast;endometrium;kidney;brain;peripheral nerve; . 0.69216 0.45347 -0.953385901 9.206180703 675.78693 5.19370 SCO1 0.507628824320746 0.488315131825301 0.00405604385395215 SCO1 cytochrome c oxidase assembly protein FUNCTION: Thought to play a role in cellular copper homeostasis, mitochondrial redox signaling or insertion of copper into the active site of COX. {ECO:0000269|PubMed:15659396, ECO:0000269|PubMed:16735468, ECO:0000269|PubMed:17189203}.; . TISSUE SPECIFICITY: Predominantly expressed in tissues characterized by high rates of oxidative phosphorylation (OxPhos), including muscle, heart, and brain. {ECO:0000269|PubMed:9878253}.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; atrioventricular node; 0.03959 0.14449 -0.183570861 39.95046001 235.95543 3.31949 SCO2 0.000101907145142781 0.356526143455592 0.643371949399265 SCO2 cytochrome c oxidase assembly protein FUNCTION: Acts as a copper chaperone, transporting copper to the Cu(A) site on the cytochrome c oxidase subunit II (COX2).; DISEASE: Myopia 6 (MYP6) [MIM:608908]: A refractive error of the eye, in which parallel rays from a distant object come to focus in front of the retina, vision being better for near objects than for far. {ECO:0000269|PubMed:23643385, ECO:0000269|PubMed:25525168}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;muscle;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; liver;trigeminal ganglion; 0.09780 0.26338 -0.622676946 17.30950696 54.66645 1.47997 SCOC 0.280616505811833 0.631537689330686 0.0878458048574815 short coiled-coil protein FUNCTION: Positive regulator of amino acid starvation-induced autophagy. {ECO:0000269|PubMed:22354037}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in brain, heart and skeletal muscle. {ECO:0000269|PubMed:11303027}.; ovary;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;blood;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; amygdala;whole brain;subthalamic nucleus;occipital lobe;thalamus;medulla oblongata;hypothalamus;temporal lobe;prefrontal cortex;globus pallidus;pons;cingulate cortex;parietal lobe; 0.30010 0.11229 0.701931997 85.34442085 698.26576 5.26029 SCOC-AS1 . . . SCOC antisense RNA 1 . . . . . . . . . . . SCOCP1 . . . short coiled-coil protein pseudogene 1 . . . . . . . . . . . SCP2 0.000139759628696758 0.991581767940407 0.00827847243089616 sterol carrier protein 2 FUNCTION: Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis. {ECO:0000269|PubMed:17157249, ECO:0000269|PubMed:8300590}.; DISEASE: Leukoencephalopathy, with dystonia and motor neuropathy (LDMN) [MIM:613724]: A syndrome characterized by leukoencephalopathy, dystonic head tremor, spasmodic torticollis and reduced tendon reflexes in lower extremities. Additional features include hyposmia, pathologic saccadic eye movements, a slight hypoacusis, accumulation of branched-chain pristanic acid in plasma, and the presence of abnormal bile alcohol glucuronides in urine. {ECO:0000269|PubMed:16685654}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver, fibroblasts, and placenta.; . . 0.28063 0.40063 -0.80269335 12.23755603 14.92337 0.53730 SCP2D1 0.0315534483185386 0.602738616950425 0.365707934731037 SCP2 sterol-binding domain containing 1 . . . . . 0.15488 . 0.547599505 81.2160887 819.78421 5.62403 SCPEP1 6.98627530887446e-08 0.687534419491352 0.312465510645895 serine carboxypeptidase 1 FUNCTION: May be involved in vascular wall and kidney homeostasis. {ECO:0000250}.; . . lymphoreticular;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;cerebellum cortex;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; adrenal gland; 0.15795 0.14822 -0.446304853 24.33356924 130.78776 2.49103 SCRG1 0.0345290274781524 0.62054062435156 0.344930348170287 stimulator of chondrogenesis 1 . . TISSUE SPECIFICITY: Expressed abundantly in the central nervous system of adult, but not at all in fetal brain. High levels of SCRG1 transcripts are also observed in testis and aorta.; smooth muscle;ovary;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;pineal body;lens;lung;placenta;macula lutea;mammary gland;aorta; dorsal root ganglion;whole brain;amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;testis - interstitial;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;atrioventricular node;pons;caudate nucleus;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; . . 0.013025609 54.62962963 31.63245 0.99566 SCRIB 0.91327318061127 0.0867268176094986 1.77923166421237e-09 scribbled planar cell polarity protein FUNCTION: Scaffold protein involved in different aspects of polarized cells differentiation regulating epithelial and neuronal morphogenesis. Most probably functions in the establishment of apico-basal cell polarity. May function in cell proliferation regulating progression from G1 to S phase and as a positive regulator of apoptosis for instance during acinar morphogenesis of the mammary epithelium. May also function in cell migration and adhesion and hence regulate cell invasion through MAPK signaling. May play a role in exocytosis and in the targeting synaptic vesicles to synapses. Functions as an activator of Rac GTPase activity. {ECO:0000269|PubMed:15182672, ECO:0000269|PubMed:15775968, ECO:0000269|PubMed:16344308, ECO:0000269|PubMed:16965391, ECO:0000269|PubMed:18641685, ECO:0000269|PubMed:18716323, ECO:0000269|PubMed:19041750}.; DISEASE: Neural tube defects (NTD) [MIM:182940]: Congenital malformations of the central nervous system and adjacent structures related to defective neural tube closure during the first trimester of pregnancy. Failure of neural tube closure can occur at any level of the embryonic axis. Common NTD forms include anencephaly, myelomeningocele and spina bifida, which result from the failure of fusion in the cranial and spinal region of the neural tube. NTDs have a multifactorial etiology encompassing both genetic and environmental components. {ECO:0000269|PubMed:22095531}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in kidney, skeletal muscles, liver, lung, breast, intestine, placenta and skin mainly in epithelial cells (at protein level). {ECO:0000269|PubMed:15806148}.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);muscle;pharynx;blood;skeletal muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach; . 0.42375 0.13468 -2.440554124 1.026185421 1336.78509 6.86559 SCRN1 0.065188552320723 0.920012594765453 0.0147988529138239 secernin 1 FUNCTION: Regulates exocytosis in mast cells. Increases both the extent of secretion and the sensitivity of mast cells to stimulation with calcium (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;gum;amniotic fluid;germinal center;bladder;brain;amygdala;heart;cartilage;pineal body;spinal cord;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;oral cavity;muscle;bile duct;pancreas;lung;cornea;mesenchyma;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; whole brain;amygdala;occipital lobe;medulla oblongata;thalamus;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.19043 0.07855 0.196671391 67.19155461 622.34945 5.03085 SCRN2 6.55878589036845e-07 0.452768958466524 0.547230385654887 secernin 2 . . . ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;hypothalamus;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; . 0.09983 0.09718 0.756930627 86.79523473 678.96406 5.20988 SCRN3 1.32015222635661e-06 0.374820031819472 0.625178648028302 secernin 3 . . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;optic nerve;whole body;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10934 0.09756 -0.001743238 53.85114414 2346.51971 8.97574 SCRT1 0.294251146505632 0.625565469505686 0.0801833839886812 scratch family zinc finger 1 FUNCTION: Transcriptional repressor that binds E-box motif CAGGTG. Can modulate the action of basic helix-loop-helix (bHLH) transcription factors, critical for neuronal differentiation. {ECO:0000269|PubMed:11274425}.; . TISSUE SPECIFICITY: Brain specific. {ECO:0000269|PubMed:11274425}.; brain;retina; superior cervical ganglion;subthalamic nucleus;medulla oblongata;occipital lobe;pons;cingulate cortex;parietal lobe;cerebellum; 0.21303 . . . 10.3722 0.37768 SCRT2 0.364922305004282 0.585067539195847 0.0500101557998714 scratch family zinc finger 2 FUNCTION: May be involved in transcriptional regulation.; . . medulla oblongata;optic nerve;islets of Langerhans;macula lutea;fovea centralis;choroid;lens;brain;retina; . 0.14914 0.16139 . . 52.58697 1.43617 SCT 0.406650722252906 0.46954063120825 0.123808646538844 secretin FUNCTION: Stimulates formation of NaHCO(3)-rich pancreatic juice and secretion of NaHCO(3)-rich bile and inhibits HCl production by the stomach.; . . . . 0.07398 . . . 12.04322 0.43670 SCTR 1.95522328385349e-09 0.232741371731084 0.767258626313692 secretin receptor FUNCTION: This is a receptor for secretin. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.; . . unclassifiable (Anatomical System);pancreas;lung;cartilage;testis;kidney;skeletal muscle; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.07290 0.17717 0.554869705 81.59943383 160.51374 2.76468 SCUBE1 0.960878305718201 0.0391216884713302 5.81046865129618e-09 signal peptide, CUB domain and EGF like domain containing 1 FUNCTION: Could function as an adhesive molecule and its matrix bound and soluble fragments may play a critical role in vascular biology. {ECO:0000269|PubMed:16753137}.; . TISSUE SPECIFICITY: Detected in endothelial cells. Highly expressed in platelets. Stored in platelet alpha granules, and transferred to the cell surface upon activation and aggregation. A smaller form, probably produced by limited proteolysis, after being released from the storage granules, is associated with thrombus and localized with the subendothelial matrices in atherosclerotic plaques. {ECO:0000269|PubMed:12270931, ECO:0000269|PubMed:16753137}.; unclassifiable (Anatomical System);lung;optic nerve;cartilage;iris;liver;choroid;brain; . 0.27203 0.10456 -1.447883661 3.927813163 3244.50733 10.84768 SCUBE2 1.4930424797099e-13 0.748934738093863 0.251065261905987 signal peptide, CUB domain and EGF like domain containing 2 . . TISSUE SPECIFICITY: Expressed in a broad spectrum of adult tissues. {ECO:0000269|PubMed:12270931}.; unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;urinary;parathyroid;blood;skin;retina;breast;uterus;prostate;pancreas;whole body;lung;nasopharynx;placenta;liver;testis;spleen;kidney;spinal ganglion;brain;mammary gland;stomach; superior cervical ganglion; 0.09477 0.10075 -0.701780438 14.81481481 3415.75515 11.21356 SCUBE3 0.9999837065276 1.62934723807016e-05 1.90934895654898e-14 signal peptide, CUB domain and EGF like domain containing 3 FUNCTION: Binds to TGFBR2 and activates TGFB signaling. In lung cancer cells, could serve as an endogenous autocrine and paracrine ligand of TGFBR2, which could regulate TGFBR2 signaling and hence modulate epithelial-mesenchymal transition and cancer progression. {ECO:0000269|PubMed:21441952}.; . TISSUE SPECIFICITY: Highly expressed in osteoblasts. In normal lung, mainly expressed in bronchial epithelial cells. Tends to be up-regulated in lung cancer cells. {ECO:0000269|PubMed:15234972, ECO:0000269|PubMed:21441952}.; unclassifiable (Anatomical System);ovary;colon;skin;breast;prostate;whole body;lung;adrenal gland;bone;placenta;thyroid;visual apparatus;testis;artery;aorta; dorsal root ganglion;uterus corpus;superior cervical ganglion;subthalamic nucleus;temporal lobe;liver;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.24617 0.09100 -0.21856543 37.66218448 216.97195 3.18474 SCX . . . scleraxis bHLH transcription factor FUNCTION: Plays an early essential role in mesoderm formation, as well as a later role in formation of somite-derived chondrogenic lineages. {ECO:0000250}.; . . . . . . . . . . SCYL1 0.00778440657043786 0.992088047683864 0.000127545745698251 SCY1 like pseudokinase 1 FUNCTION: Regulates COPI-mediated retrograde traffic. Has no detectable kinase activity in vitro. {ECO:0000269|PubMed:18556652}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12036289}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;urinary;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;duodenum;kidney;stomach;thymus; superior cervical ganglion; 0.27008 0.14727 0.470324112 78.82755367 191.64065 3.00231 SCYL2 0.931828671048131 0.0681712128753588 1.16076510463477e-07 SCY1 like pseudokinase 2 FUNCTION: Component of AP2-containing clathrin coated structures at the plasma membrane or of endocytic coated vesicles. According to PubMed:15809293, probable serine/threonine-protein kinase that phosphorylates, in vitro, the beta2-subunit of the plasma membrane adapter complex AP2 and other proteins in presence of poly-L- lysine. According to PubMed:16914521, has no detectable kinase activity in vitro. May regulate clathrin-dependent trafficking between the TGN and/or the endosomal system. {ECO:0000269|PubMed:15809293, ECO:0000269|PubMed:16914521}.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;urinary;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.24774 0.19298 0.044168103 57.40740741 586.02722 4.91089 SCYL3 0.547053807767411 0.452921065370908 2.51268616809106e-05 SCY1 like pseudokinase 3 FUNCTION: May play a role in regulating cell adhesion/migration complexes in migrating cells. {ECO:0000269|PubMed:12651155}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12651155}.; . . 0.19094 0.07496 0.312359769 72.71172446 582.74642 4.89441 SCZD1 . . . schizophrenia disorder 1 . . . . . . . . . . . SCZD2 . . . schizophrenia disorder 2 . . . . . . . . . . . SCZD3 . . . schizophrenia disorder 3 . . . . . . . . . . . SCZD4 . . . schizophrenia disorder 4 . . . . . . . . . . . SCZD5 . . . schizophrenia disorder 5 . . . . . . . . . . . SCZD6 . . . schizophrenia disorder 6 . . . . . . . . . . . SCZD7 . . . schizophrenia disorder 7 . . . . . . . . . . . SCZD8 . . . schizophrenia disorder 8 . . . . . . . . . . . SCZD10 . . . schizophrenia disorder 10 (periodic catatonia) . . . . . . . . . . . SDAD1 3.78400058799568e-09 0.996515321078907 0.00348467513709253 SDA1 domain containing 1 FUNCTION: Required for 60S pre-ribosomal subunits export to the cytoplasm. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in testis, kidney, spleen, brain and fetal tissues. Also expressed at lower level in heart, lung, liver, small intestine, ovary, uterus, mammary gland and placenta. {ECO:0000269|PubMed:14976432, ECO:0000269|PubMed:15607425}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.10012 0.11349 -0.042196577 50.49539986 3455.42024 11.28760 SDAD1P1 . . . SDA1 domain containing 1 pseudogene 1 . . . . . . . . . . . SDAD1P2 . . . SDA1 domain containing 1 pseudogene 2 . . . . . . . . . . . SDAD1P3 . . . SDA1 domain containing 1 pseudogene 3 . . . . . . . . . . . SDAD1P4 . . . SDA1 domain containing 1 pseudogene 4 . . . . . . . . . . . SDC1 0.290469547271798 0.688643798182838 0.0208866545453639 syndecan 1 FUNCTION: Cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;oesophagus;gum;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;urinary;pharynx;blood;lens;breast;bile duct;pancreas;lung;cornea;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; prostate;superior cervical ganglion;lung;tongue;placenta;liver;kidney;trigeminal ganglion;skin; 0.06732 0.51297 0.885576705 89.14248644 243.85141 3.36985 SDC2 0.579949600907069 0.409281236346809 0.0107691627461228 syndecan 2 FUNCTION: Cell surface proteoglycan that bears heparan sulfate. Regulates dendritic arbor morphogenesis (By similarity). {ECO:0000250}.; . . lymphoreticular;smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;amygdala;superior cervical ganglion;adipose tissue;thyroid;liver;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;pituitary;skeletal muscle; 0.55337 0.55515 0.104848986 61.49445624 3205.08824 10.79403 SDC3 0.527916180650144 0.456042374224655 0.0160414451252014 syndecan 3 FUNCTION: Cell surface proteoglycan that may bear heparan sulfate (By similarity). May have a role in the organization of cell shape by affecting the actin cytoskeleton, possibly by transferring signals from the cell surface in a sugar-dependent mechanism. {ECO:0000250, ECO:0000269|PubMed:11527150}.; . TISSUE SPECIFICITY: Expressed in the nervous system, the adrenal gland, and the spleen. {ECO:0000269|PubMed:11527150}.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;iris;germinal center;brain;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;oesophagus;cerebral cortex;larynx;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;mesenchyma;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus; amygdala;whole brain;occipital lobe;fetal brain;adrenal gland;hypothalamus;spinal cord;prefrontal cortex;parietal lobe;cingulate cortex; 0.20214 0.31827 -0.020150552 52.25288983 4069.42538 12.65200 SDC4 0.0118034906332036 0.847335333689781 0.140861175677016 syndecan 4 FUNCTION: Cell surface proteoglycan that bears heparan sulfate.; . TISSUE SPECIFICITY: Expressed in epithelial and fibroblastic cells. {ECO:0000269|PubMed:1500433}.; . . 0.26113 0.20685 -0.161524709 41.6430762 2463.14431 9.23969 SDC4P . . . syndecan 4 pseudogene . . . . . . . . . . . SDCBP 0.000811571828670198 0.77940736628676 0.21978106188457 syndecan binding protein FUNCTION: Seems to function as an adapter protein. In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway. {ECO:0000269|PubMed:10230395, ECO:0000269|PubMed:11179419, ECO:0000269|PubMed:11498591}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in fetal kidney, liver, lung and brain. In adult highest expression in heart and placenta.; smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;thyroid;amniotic fluid;bladder;brain;gall bladder;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;breast;epididymis;visual apparatus;liver;cervix;mammary gland;salivary gland;intestine;colon;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; superior cervical ganglion;whole blood; 0.13282 0.36375 -0.516085732 21.20193442 52.12947 1.42722 SDCBP2 0.410340821760316 0.581243947396935 0.00841523084274953 syndecan binding protein 2 . . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; . 0.11800 0.17985 1.330184494 94.17315405 4196.90857 12.87003 SDCBP2-AS1 . . . SDCBP2 antisense RNA 1 . . . . . . . . . . . SDCBP2P1 . . . syndecan binding protein (syntenin) 2 pseudogene 1 . . . . . . . . . . . SDCBPP1 . . . syndecan binding protein (syntenin) pseudogene 1 . . . . . . . . . . . SDCBPP2 . . . syndecan binding protein (syntenin) pseudogene 2 . . . . . . . . . . . SDCBPP3 . . . syndecan binding protein (syntenin) pseudogene 3 . . . . . . . . . . . SDCCAG3 1.37769738127372e-07 0.368767768467124 0.631232093763138 serologically defined colon cancer antigen 3 FUNCTION: May be involved in modulation of TNF response. May be involved in presentation of TNFRSF1A on the cell surface (By similarity). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1 (PubMed:25278552). Involved in the regulation of cytokinesis; the function may involve PTPN13 and GIT1 (PubMed:23108400). {ECO:0000250|UniProtKB:A2AIW0, ECO:0000269|PubMed:23108400, ECO:0000269|PubMed:25278552}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion; 0.13869 0.10313 0.468503535 78.79806558 1803.84196 7.83738 SDCCAG3P1 . . . serologically defined colon cancer antigen 3 pseudogene 1 . . . . . . . . . . . SDCCAG3P2 . . . serologically defined colon cancer antigen 3 pseudogene 2 . . . . . . . . . . . SDCCAG8 1.32893386487215e-07 0.98771789550758 0.0122819715990331 serologically defined colon cancer antigen 8 FUNCTION: Plays a role in the establishment of cell polarity and epithelial lumen formation (By similarity). May play a role in ciliogenesis. {ECO:0000250|UniProtKB:Q80UF4}.; DISEASE: Bardet-Biedl syndrome 16 (BBS16) [MIM:615993]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:20835237, ECO:0000269|PubMed:22626039}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in thymus, prostate, testis, ovary, small intestine, colon, mucosa, colon and renal cancer tumors. {ECO:0000269|PubMed:9610721}.; lymphoreticular;ovary;parathyroid;skin;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;thymus; . 0.13767 0.11503 -0.154246007 42.22694032 1944.53595 8.11749 SDE2 5.17001532782485e-07 0.639146769618251 0.360852713380216 SDE2 telomere maintenance homolog (S. pombe) . . . . . 0.11060 . 0.064394823 58.84642604 60.15244 1.57434 SDF2 0.682810040021872 0.312765544804366 0.0044244151737622 stromal cell derived factor 2 . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.24240 0.12959 0.325313577 73.11276244 85.6278 1.97343 SDF2L1 0.0542960896755155 0.702277406122135 0.243426504202349 stromal cell derived factor 2 like 1 . . TISSUE SPECIFICITY: Ubiquitously expressed with high expression in testis, moderate expression in the pancreas, spleen, prostate, small intestine and colon. Very low expression is seen in brain and skeletal muscle. {ECO:0000269|PubMed:11162531}.; medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;macula lutea;alveolus;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;thyroid;liver; 0.18970 0.12459 . . 179.50832 2.90977 SDF4 0.0013098271899439 0.858724276816432 0.139965895993624 stromal cell derived factor 4 FUNCTION: May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. Isoform 5 is expressed in pancreas. {ECO:0000269|PubMed:17442889}.; medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;oesophagus;endometrium;bone;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;trophoblast;heart;cartilage;islets of Langerhans;urinary;muscle;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; prostate;placenta;thyroid;liver;testis; 0.10366 0.35502 -0.598810865 18.13517339 109.15684 2.26829 SDHA 9.3872916167157e-06 0.996636308369499 0.00335430433888413 succinate dehydrogenase complex flavoprotein subunit A FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) (PubMed:24781757). Can act as a tumor suppressor (PubMed:20484225). {ECO:0000269|PubMed:20484225, ECO:0000305|PubMed:24781757}.; DISEASE: Mitochondrial complex II deficiency (MT-C2D) [MIM:252011]: A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations. Clinical features include psychomotor regression in infants, poor growth with lack of speech development, severe spastic quadriplegia, dystonia, progressive leukoencephalopathy, muscle weakness, exercise intolerance, cardiomyopathy. Some patients manifest Leigh syndrome or Kearns-Sayre syndrome. Note=The disease is caused by mutations affecting the gene represented in this entry. {ECO:0000269|PubMed:12794685}.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. {ECO:0000269|PubMed:10746566, ECO:0000269|PubMed:24781757, ECO:0000269|PubMed:7550341}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1GG (CMD1GG) [MIM:613642]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:20551992}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Paragangliomas 5 (PGL5) [MIM:614165]: A neural crest tumor usually derived from the chromoreceptor tissue of a paraganglion. Paragangliomas can develop at various body sites, including the head, neck, thorax and abdomen. Most commonly, they are located in the head and neck region, specifically at the carotid bifurcation, the jugular foramen, the vagal nerve, and in the middle ear. {ECO:0000269|PubMed:20484225}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;cerebellum; . 0.29640 . -0.857930839 10.95187544 1260.39498 6.69421 SDHAF1 0.106593833761682 0.592070599970024 0.301335566268294 succinate dehydrogenase complex assembly factor 1 FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit SDHB of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. May act together with SDHAF3. {ECO:0000269|PubMed:19465911, ECO:0000269|PubMed:24954417}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:19465911}.; . . . . . . 13.08923 0.47642 SDHAF2 6.97874038276147e-05 0.295950315711293 0.703979896884879 succinate dehydrogenase complex assembly factor 2 FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SDHA of the SDH catalytic dimer. {ECO:0000255|HAMAP-Rule:MF_03057, ECO:0000269|PubMed:19628817}.; DISEASE: Paragangliomas 2 (PGL2) [MIM:601650]: A neural crest tumor usually derived from the chromoreceptor tissue of a paraganglion. Paragangliomas can develop at various body sites, including the head, neck, thorax and abdomen. Most commonly, they are located in the head and neck region, specifically at the carotid bifurcation, the jugular foramen, the vagal nerve, and in the middle ear. {ECO:0000269|PubMed:19628817}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;iris;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;uterus;superior cervical ganglion;uterus corpus;smooth muscle;adipose tissue;placenta;ciliary ganglion;skeletal muscle; 0.12498 0.10652 0.014844891 54.94810097 3.62655 0.13326 SDHAF3 . . . succinate dehydrogenase complex assembly factor 3 FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit SDHB of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. May act together with SDHAF1. {ECO:0000250|UniProtKB:Q04401, ECO:0000250|UniProtKB:Q8SZ16}.; . . . . 0.14567 0.08794 0.3032669 72.009908 . . SDHAF4 . . . succinate dehydrogenase complex assembly factor 4 FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol (PubMed:24954416). Binds to the flavoprotein subunit SDHA in its FAD-bound form, blocking the generation of excess reactive oxigen species (ROS) and facilitating its assembly with the iron-sulfur protein subunit SDHB into the SDH catalytic dimer (By similarity). {ECO:0000250|UniProtKB:P38345, ECO:0000269|PubMed:24954416}.; . . . . 0.04425 0.09295 0.569646743 81.88841708 . . SDHAP1 . . . succinate dehydrogenase complex flavoprotein subunit A pseudogene 1 . . . unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;colon;blood;lens;skin;skeletal muscle;retina;breast;uterus;pancreas;lung;frontal lobe;endometrium;larynx;bone;thyroid;placenta;hippocampus;hypopharynx;duodenum;liver;testis;head and neck;germinal center;brain;stomach; . . . . . . . SDHAP2 . . . succinate dehydrogenase complex flavoprotein subunit A pseudogene 2 . . . . . . . . . . . SDHAP3 . . . succinate dehydrogenase complex flavoprotein subunit A pseudogene 3 . . . . . . . . . . . SDHB 0.0501027715702188 0.945230052931343 0.0046671754984379 succinate dehydrogenase complex iron sulfur subunit B FUNCTION: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).; DISEASE: Pheochromocytoma (PCC) [MIM:171300]: A catecholamine- producing tumor of chromaffin tissue of the adrenal medulla or sympathetic paraganglia. The cardinal symptom, reflecting the increased secretion of epinephrine and norepinephrine, is hypertension, which may be persistent or intermittent. {ECO:0000269|PubMed:11404820, ECO:0000269|PubMed:12000816, ECO:0000269|PubMed:12618761, ECO:0000269|PubMed:14500403, ECO:0000269|PubMed:14974914, ECO:0000269|PubMed:15328326, ECO:0000269|PubMed:17634472}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Paragangliomas 4 (PGL4) [MIM:115310]: A neural crest tumor usually derived from the chromoreceptor tissue of a paraganglion. Paragangliomas can develop at various body sites, including the head, neck, thorax and abdomen. Most commonly, they are located in the head and neck region, specifically at the carotid bifurcation, the jugular foramen, the vagal nerve, and in the middle ear. {ECO:0000269|PubMed:11404820, ECO:0000269|PubMed:11897817, ECO:0000269|PubMed:14715873, ECO:0000269|PubMed:14974914, ECO:0000269|PubMed:15328326}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Paraganglioma and gastric stromal sarcoma (PGGSS) [MIM:606864]: Gastrointestinal stromal tumors may be sporadic or inherited in an autosomal dominant manner, alone or as a component of a syndrome associated with other tumors, such as in the context of neurofibromatosis type 1 (NF1). Patients have both gastrointestinal stromal tumors and paragangliomas. Susceptibility to the tumors was inherited in an apparently autosomal dominant manner, with incomplete penetrance. {ECO:0000269|PubMed:17804857}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cowden syndrome 2 (CWS2) [MIM:612359]: A form of Cowden syndrome, a hamartomatous polyposis syndrome with age-related penetrance. Cowden syndrome is characterized by hamartomatous lesions affecting derivatives of ectodermal, mesodermal and endodermal layers, macrocephaly, facial trichilemmomas (benign tumors of the hair follicle infundibulum), acral keratoses, papillomatous papules, and elevated risk for development of several types of malignancy, particularly breast carcinoma in women and thyroid carcinoma in both men and women. Colon cancer and renal cell carcinoma have also been reported. Hamartomas can be found in virtually every organ, but most commonly in the skin, gastrointestinal tract, breast and thyroid. {ECO:0000269|PubMed:18678321}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . . . 0.40522 0.63579 0.527368849 80.73248408 150.23642 2.67455 SDHC 0.0954199560781008 0.867866430308991 0.0367136136129083 succinate dehydrogenase complex subunit C FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).; DISEASE: Paragangliomas 3 (PGL3) [MIM:605373]: A neural crest tumor usually derived from the chromoreceptor tissue of a paraganglion. Paragangliomas can develop at various body sites, including the head, neck, thorax and abdomen. Most commonly, they are located in the head and neck region, specifically at the carotid bifurcation, the jugular foramen, the vagal nerve, and in the middle ear. {ECO:0000269|PubMed:11062460}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Paraganglioma and gastric stromal sarcoma (PGGSS) [MIM:606864]: Gastrointestinal stromal tumors may be sporadic or inherited in an autosomal dominant manner, alone or as a component of a syndrome associated with other tumors, such as in the context of neurofibromatosis type 1 (NF1). Patients have both gastrointestinal stromal tumors and paragangliomas. Susceptibility to the tumors was inherited in an apparently autosomal dominant manner, with incomplete penetrance. {ECO:0000269|PubMed:17804857}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.21642 0.35425 0.391453969 75.87284737 5.31927 0.19645 SDHCP1 . . . succinate dehydrogenase complex subunit C pseudogene 1 . . . . . . . . . . . SDHCP2 . . . succinate dehydrogenase complex subunit C pseudogene 2 . . . . . . . . . . . SDHCP3 . . . succinate dehydrogenase complex subunit C pseudogene 3 . . . . . . . . . . . SDHCP4 . . . succinate dehydrogenase complex subunit C pseudogene 4 . . . . . . . . . . . SDHD 0.70544004830206 0.291017663656491 0.00354228804144933 succinate dehydrogenase complex subunit D FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). {ECO:0000250}.; DISEASE: Paragangliomas 1 (PGL1) [MIM:168000]: A neural crest tumor usually derived from the chromoreceptor tissue of a paraganglion. PGL1 is a rare autosomal dominant disorder which is characterized by the development of mostly benign, highly vascular, slowly growing tumors in the head and neck. In the head and neck region, the carotid body is the largest of all paraganglia and is also the most common site of the tumors. {ECO:0000269|PubMed:10657297, ECO:0000269|PubMed:11343322, ECO:0000269|PubMed:11391796, ECO:0000269|PubMed:11391798, ECO:0000269|PubMed:15328326}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pheochromocytoma (PCC) [MIM:171300]: A catecholamine- producing tumor of chromaffin tissue of the adrenal medulla or sympathetic paraganglia. The cardinal symptom, reflecting the increased secretion of epinephrine and norepinephrine, is hypertension, which may be persistent or intermittent. {ECO:0000269|PubMed:11156372, ECO:0000269|PubMed:12000816, ECO:0000269|PubMed:15328326}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Intestinal carcinoid tumor (ICT) [MIM:114900]: A yellow, well-differentiated, circumscribed tumor that arises from enterochromaffin cells in the small intestine or, less frequently, in other parts of the gastrointestinal tract. {ECO:0000269|PubMed:12007193}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Paraganglioma and gastric stromal sarcoma (PGGSS) [MIM:606864]: Gastrointestinal stromal tumors may be sporadic or inherited in an autosomal dominant manner, alone or as a component of a syndrome associated with other tumors, such as in the context of neurofibromatosis type 1 (NF1). Patients have both gastrointestinal stromal tumors and paragangliomas. Susceptibility to the tumors was inherited in an apparently autosomal dominant manner, with incomplete penetrance. {ECO:0000269|PubMed:17804857}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cowden syndrome 3 (CWS3) [MIM:615106]: A form of Cowden syndrome, a hamartomatous polyposis syndrome with age-related penetrance. Cowden syndrome is characterized by hamartomatous lesions affecting derivatives of ectodermal, mesodermal and endodermal layers, macrocephaly, facial trichilemmomas (benign tumors of the hair follicle infundibulum), acral keratoses, papillomatous papules, and elevated risk for development of several types of malignancy, particularly breast carcinoma in women and thyroid carcinoma in both men and women. Colon cancer and renal cell carcinoma have also been reported. Hamartomas can be found in virtually every organ, but most commonly in the skin, gastrointestinal tract, breast and thyroid. {ECO:0000269|PubMed:18678321}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial complex II deficiency (MT-C2D) [MIM:252011]: A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations. Clinical features include psychomotor regression in infants, poor growth with lack of speech development, severe spastic quadriplegia, dystonia, progressive leukoencephalopathy, muscle weakness, exercise intolerance, cardiomyopathy. Some patients manifest Leigh syndrome or Kearns-Sayre syndrome. {ECO:0000269|PubMed:24367056, ECO:0000269|PubMed:26008905}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.20501 0.61660 0.457594962 78.16112291 64.45608 1.64674 SDHDP1 . . . succinate dehydrogenase complex subunit D pseudogene 1 . . . . . . . . . . . SDHDP2 . . . succinate dehydrogenase complex subunit D pseudogene 2 . . . . . . . . . . . SDHDP3 . . . succinate dehydrogenase complex subunit D pseudogene 3 . . . . . . . . . . . SDHDP4 . . . succinate dehydrogenase complex subunit D pseudogene 4 . . . . . . . . . . . SDHDP5 . . . succinate dehydrogenase complex subunit D pseudogene 5 . . . . . . . . . . . SDHDP6 . . . succinate dehydrogenase complex subunit D pseudogene 6 . . . . . . . . . . . SDHDP7 . . . succinate dehydrogenase complex subunit D pseudogene 7 . . . . . . . . . . . SDIM1 . . . stress responsive DNAJB4 interacting membrane protein 1 FUNCTION: Promotes neuronal cells survival to stress conditions. {ECO:0000269|PubMed:21255413}.; . TISSUE SPECIFICITY: Expressed in brain with higher detection in neurons than astrocytes. Decreased expression in Alzheimer brains. Detected at protein level in brain and cervix. {ECO:0000269|PubMed:21255413}.; . . . . . . 22.28373 0.74763 SDK1 0.00501599676743558 0.994984003204786 2.77790079216421e-11 sidekick cell adhesion molecule 1 FUNCTION: Adhesion molecule that promotes lamina-specific synaptic connections in the retina. Expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions. {ECO:0000250|UniProtKB:Q8AV58}.; . TISSUE SPECIFICITY: Up-regulated in glomeruli in HIV-associated nephropathy. In diseased glomeruli, significantly overexpressed and the expression is no longer restricted to mesangial cells but includes podocytes and parietal epithelial cells (PubMed:15213259). {ECO:0000269|PubMed:15213259}.; . . 0.23874 0.11227 -4.629838752 0.076669026 1933.799 8.09023 SDK2 0.0290344313872634 0.970965567357858 1.25487877804611e-09 sidekick cell adhesion molecule 2 FUNCTION: Adhesion molecule that promotes lamina-specific synaptic connections in the retina and is specifically required for the formation of neuronal circuits that detect motion. Acts by promoting formation of synapses between two specific retinal cell types: the retinal ganglion cells W3B-RGCs and the excitatory amacrine cells VG3-ACs. Formation of synapses between these two cells plays a key role in detection of motion. Promotes synaptic connectivity via homophilic interactions. {ECO:0000250|UniProtKB:Q6V4S5}.; . . unclassifiable (Anatomical System);uterus;lymph node;lung;cartilage;visual apparatus;muscle;testis;kidney;germinal center;lens;brain; subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.41261 0.12096 -2.470675891 0.9849021 2484.07134 9.29974 SDPR 0.000704632748926169 0.752311760404387 0.246983606846687 serum deprivation response FUNCTION: May play a role in targeting PRKCA to caveolae. {ECO:0000250|UniProtKB:Q66H98}.; . TISSUE SPECIFICITY: Highly expressed in heart and lung, and expressed at lower levels in brain, kidney, liver, pancreas, placenta, and skeletal muscle. {ECO:0000269|PubMed:10191091}.; unclassifiable (Anatomical System);cartilage;lacrimal gland;islets of Langerhans;vein;prostate;atrium;lung;frontal lobe;endometrium;nasopharynx;bone;placenta;duodenum;liver;spleen;kidney;spinal ganglion;brain;stomach; ciliary ganglion; 0.25218 0.27228 0.220536484 68.38287332 388.92558 4.15338 SDR9C7 0.013528777168157 0.864775866156685 0.121695356675158 short chain dehydrogenase/reductase family 9C, member 7 FUNCTION: Displays weak conversion of all-trans-retinal to all- trans-retinol in the presence of NADH. Has apparently no steroid dehydrogenase activity. {ECO:0000269|PubMed:19703561}.; . TISSUE SPECIFICITY: Highly expressed in liver. {ECO:0000269|PubMed:12234675}.; . . . 0.09322 0.330767508 73.53739089 233.89891 3.30521 SDR16C5 0.00291744009323263 0.808136864683139 0.188945695223629 short chain dehydrogenase/reductase family 16C, member 5 FUNCTION: Oxidoreductase with strong preference for NAD. Active in both the oxidative and reductive directions. Oxidizes all-trans- retinol in all-trans-retinaldehyde. No activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD(+)/NADH or NADP(+)/NADPH. {ECO:0000269|PubMed:18926804}.; . TISSUE SPECIFICITY: Detected in adult lung. Detected at low levels in adult brain, heart, testis, placenta, cervix, pancreas, uterus, stomach, rectum, small intestine, colon, esophagus, thymus, skin, and skin keratinocyte. Expression is higher in psoriasis lesions relative to unaffected skin from psoriasis patients. Detected in fetal kidney, skin and lung. {ECO:0000269|PubMed:12372410}.; unclassifiable (Anatomical System);pancreas;lung;heart;oesophagus;islets of Langerhans;larynx;nasopharynx;hypopharynx;testis;colon;head and neck;brain;stomach; . . 0.08029 0.104848986 61.49445624 79.23879 1.88102 SDR16C6P . . . short chain dehydrogenase/reductase family 16C, member 6, pseudogene . . . . . . . . . . . SDR39U1 7.40935818071384e-08 0.150017491530789 0.849982434375629 short chain dehydrogenase/reductase family 39U member 1 FUNCTION: Putative NADP-dependent oxidoreductase. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in adrenal gland.; ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;iris;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;placenta;amnion;head and neck;kidney;stomach;aorta;cerebellum; . 0.09304 0.09694 1.462485515 95.2111347 381.94119 4.11942 SDR42E1 3.52616114391235e-07 0.103573559362965 0.896426088020921 short chain dehydrogenase/reductase family 42E, member 1 . . . unclassifiable (Anatomical System);heart;colon;skin;skeletal muscle;uterus;pancreas;prostate;lung;thyroid;bone;germinal center;kidney;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; . 0.07366 1.199707453 92.98183534 1763.37539 7.75451 SDR42E1P1 . . . short chain dehydrogenase/reductase family 42E, member 1 pseudogene 1 . . . . . . . . . . . SDR42E1P2 . . . short chain dehydrogenase/reductase family 42E, member 1 pseudogene 2 . . . . . . . . . . . SDR42E1P3 . . . short chain dehydrogenase/reductase family 42E, member 1 pseudogene 3 . . . . . . . . . . . SDR42E1P4 . . . short chain dehydrogenase/reductase family 42E, member 1 pseudogene 4 . . . . . . . . . . . SDR42E1P5 . . . short chain dehydrogenase/reductase family 42E, member 1 pseudogene 5 . . . . . . . . . . . SDR42E2 . . . short chain dehydrogenase/reductase family 42E, member 2 . . . . . . 0.10175 . . 1684.16831 7.56410 SDS 0.00548426197624614 0.89628082468137 0.0982349133423841 serine dehydratase . . . unclassifiable (Anatomical System);heart;ovary;urinary;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;lung;placenta;bone;macula lutea;hippocampus;iris;liver;kidney;brain;gall bladder; . 0.23479 0.38797 -0.424258538 25.56027365 101.72756 2.18266 SDSL 2.99135817651197e-09 0.0457085494426622 0.95429144756598 serine dehydratase like FUNCTION: Has low serine dehydratase and threonine dehydratase activity.; . . unclassifiable (Anatomical System);ovary;hypothalamus;colon;parathyroid;skin;prostate;lung;endometrium;placenta;bone;visual apparatus;hippocampus;liver;spleen;kidney;brain;aorta; superior cervical ganglion;thyroid;liver;kidney;atrioventricular node;trigeminal ganglion; 0.29804 0.12768 0.621009802 83.41589998 463.01333 4.45978 SEA . . . S13 erythroblastosis (avian) oncogene homolog . . . . . . . . . . . SEBOX . . . SEBOX homeobox FUNCTION: Probable transcription factor involved in the control of specification of mesoderm and endoderm. {ECO:0000250}.; . . . . 0.19600 . 0.815800671 87.8744987 . . SEC1P . . . secretory blood group 1, pseudogene . . . . . . . . . . . SEC11A 0.173327554548954 0.813367538953771 0.0133049064972743 SEC11 homolog A, signal peptidase complex subunit FUNCTION: Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. {ECO:0000250}.; . . smooth muscle;ovary;substantia nigra;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;gum;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;muscle;pancreas;lung;cornea;adrenal gland;placenta;head and neck;kidney;stomach;aorta; adipose tissue;testis; 0.39573 0.14229 -0.031067188 51.03798066 0.98813 0.02494 SEC11B . . . SEC11 homolog B, signal peptidase complex subunit (pseudogene) FUNCTION: Putative component of some signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. {ECO:0000250}.; . . . . . 0.14229 . . . . SEC11C 0.694287699372018 0.301753677443474 0.00395862318450763 SEC11 homolog C, signal peptidase complex subunit FUNCTION: Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;alveolus;kidney;mammary gland;stomach; amygdala;whole brain;prostate;pancreas;trachea;hypothalamus;beta cell islets; 0.32201 0.10713 -0.031067188 51.03798066 5.6503 0.21182 SEC13 0.584365053119917 0.415183318626518 0.000451628253564779 SEC13 homolog, nuclear pore and COPII coat complex component FUNCTION: Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles. As a component of the GATOR2 complex, inhibits GATOR1 complex, an inhibitor of the amino acid-sensing branch of the TORC1 pathway. {ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:8972206}.; . . lymphoreticular;medulla oblongata;umbilical cord;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;bladder;tonsil;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;choroid;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hypopharynx;amnion;head and neck;kidney;stomach;aorta;cerebellum; testis - interstitial;placenta;thyroid;liver;testis; 0.31003 0.17720 -0.426079032 25.36565228 39.29791 1.16335 SEC13P1 . . . SEC13 homolog, nuclear pore and COPII coat complex component pseudogene 1 . . . . . . . . . . . SEC14L1 0.179640443143628 0.820337924871133 2.16319852396033e-05 SEC14 like lipid binding 1 FUNCTION: May play a role in innate immunity by inhibiting the antiviral RIG-I signaling pathway. In this pathway, functions as a negative regulator of DDX58/RIG-I, the cytoplasmic sensor of viral nucleic acids. Prevents the interaction of DDX58 with MAVS/IPS1, an important step in signal propagation (PubMed:23843640). May also regulate the SLC18A3 and SLC5A7 cholinergic transporters (PubMed:17092608). {ECO:0000269|PubMed:17092608, ECO:0000269|PubMed:23843640}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8697811}.; . . 0.36588 0.11977 -0.619039275 17.39797122 87.35443 1.99622 SEC14L1P1 . . . SEC14 like 1 pseudogene 1 . . . . . . . . . . . SEC14L2 4.31488873660089e-05 0.958730605472038 0.0412262456405957 SEC14 like lipid binding 2 FUNCTION: Carrier protein. Binds to some hydrophobic molecules and promotes their transfer between the different cellular sites. Binds with high affinity to alpha-tocopherol. Also binds with a weaker affinity to other tocopherols and to tocotrienols. May have a transcriptional activatory activity via its association with alpha-tocopherol. Probably recognizes and binds some squalene structure, suggesting that it may regulate cholesterol biosynthesis by increasing the transfer of squalene to a metabolic active pool in the cell.; . TISSUE SPECIFICITY: Widely expressed. Strong expression in liver, brain and prostate. {ECO:0000269|PubMed:10829015}.; colon;fovea centralis;choroid;vein;skin;retina;prostate;optic nerve;whole body;frontal lobe;thyroid;bone;testis;bladder;brain;unclassifiable (Anatomical System);cartilage;cerebellum cortex;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; liver;trigeminal ganglion; 0.27976 0.12613 0.238945317 69.20853975 3585.08728 11.58105 SEC14L3 4.21057781805564e-18 0.000739736343451667 0.999260263656548 SEC14 like lipid binding 3 FUNCTION: Probable hydrophobic ligand-binding protein; may play a role in the transport of hydrophobic ligands like tocopherol, squalene and phospholipids.; . . unclassifiable (Anatomical System);optic nerve;lung;nasopharynx;macula lutea;liver;spleen;fovea centralis;choroid;lens;nose;retina; subthalamic nucleus;superior cervical ganglion;uterus corpus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.33148 0.11968 1.155610133 92.59259259 7730.11725 18.91651 SEC14L4 5.59567327026563e-05 0.970688619723097 0.0292554235442009 SEC14 like lipid binding 4 FUNCTION: Probable hydrophobic ligand-binding protein; may play a role in the transport of hydrophobic ligands like tocopherol, squalene and phospholipids.; . . unclassifiable (Anatomical System);medulla oblongata;lymph node;hypothalamus;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;lung;endometrium;thyroid;visual apparatus;testis;germinal center;kidney;brain;mammary gland;stomach; . 0.27910 0.10076 1.067416815 91.66666667 6436.78524 16.83869 SEC14L5 6.56646738092541e-10 0.408296631263094 0.591703368080259 SEC14 like lipid binding 5 . . . unclassifiable (Anatomical System);frontal lobe;cochlea;hypothalamus;pineal body;lens;brain;mammary gland; amygdala;medulla oblongata;superior cervical ganglion;hypothalamus;spinal cord;prefrontal cortex;pons;caudate nucleus;cingulate cortex;skeletal muscle;parietal lobe; 0.15183 . -1.703090605 2.535975466 83.7768 1.94866 SEC14L6 0.0459161840126631 0.853362181296358 0.100721634690978 SEC14 like lipid binding 6 . . . . . . . . . 241.84156 3.35877 SEC16A 0.687007221303222 0.312992778594494 1.02283900368824e-10 SEC16 homolog A, endoplasmic reticulum export factor FUNCTION: Defines endoplasmic reticulum exit sites (ERES) and is required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus. SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining an ERES. Required for normal transitional endoplasmic reticulum (tER) organization. {ECO:0000269|PubMed:17005010, ECO:0000269|PubMed:17192411}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed at higher levels in the pancreas. {ECO:0000269|PubMed:17192411}.; lymphoreticular;ovary;sympathetic chain;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;adrenal cortex;blood;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; prostate;liver;cerebellum; 0.19095 0.12594 -2.288876199 1.232602029 1838.95143 7.90814 SEC16B 4.43622376673842e-13 0.744192626037864 0.255807373961693 SEC16 homolog B, endoplasmic reticulum export factor FUNCTION: Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus and for normal transitional endoplasmic reticulum (tER) organization. {ECO:0000269|PubMed:17192411}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12244571, ECO:0000269|PubMed:17192411}.; unclassifiable (Anatomical System);heart;islets of Langerhans;adrenal cortex;colon;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;lung;endometrium;macula lutea;liver;testis;spleen;kidney;brain;mammary gland;stomach;peripheral nerve; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.43340 0.09454 3.611232357 99.53998585 4542.38133 13.52805 SEC22A 0.638909264916314 0.359706175477277 0.00138455960640861 SEC22 homolog A, vesicle trafficking protein FUNCTION: May be involved in vesicle transport between the ER and the Golgi complex. {ECO:0000250|UniProtKB:Q642F4}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.31225 0.10772 -0.163345027 41.24793583 25.01889 0.81997 SEC22B . . . SEC22 homolog B, vesicle trafficking protein (gene/pseudogene) FUNCTION: SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER. {ECO:0000269|PubMed:15272311}.; . . . . . . . . . . SEC22C 1.72380785269272e-06 0.424110011016537 0.57588826517561 SEC22 homolog C, vesicle trafficking protein FUNCTION: May be involved in vesicle transport between the ER and the Golgi complex. {ECO:0000269|PubMed:9501016}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9501016}.; medulla oblongata;ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;ciliary body;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;lens;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;spleen;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis;trigeminal ganglion;skin;cerebellum; 0.37853 0.08248 -0.183570861 39.95046001 51.21459 1.41121 SEC23A 0.000127975825136816 0.999792614446524 7.94097283387632e-05 Sec23 homolog A, COPII coat complex component FUNCTION: Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.; DISEASE: Craniolenticulosutural dysplasia (CLSD) [MIM:607812]: Autosomal recessive syndrome characterized by late-closing fontanels, sutural cataracts, facial dysmorphisms and skeletal defects. {ECO:0000269|PubMed:16980979}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;artery;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;smooth muscle;trigeminal ganglion;skeletal muscle; 0.68918 0.16819 -0.778825328 12.88039632 41.28269 1.20681 SEC23B 6.85928695809641e-14 0.811373806739475 0.188626193260456 Sec23 homolog B, COPII coat complex component FUNCTION: Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex (By similarity). {ECO:0000250}.; DISEASE: Anemia, congenital dyserythropoietic, 2 (CDAN2) [MIM:224100]: An autosomal recessive blood disorder characterized by morphological abnormalities of erythroblasts, ineffective erythropoiesis, normocytic anemia, iron overload, jaundice, and variable splenomegaly. Ultrastructural features include bi- or multinucleated erythroblasts in bone marrow, karyorrhexis, and the presence of Gaucher-like bone marrow histiocytes. The main biochemical feature of the disease is defective glycosylation of some red blood cells membrane proteins. {ECO:0000269|PubMed:19561605, ECO:0000269|PubMed:19621418}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10429 0.15151 0.492370491 79.60603916 2058.30581 8.36175 SEC23IP 0.373415107688289 0.626584098213591 7.94098120169822e-07 SEC23 interacting protein FUNCTION: Plays a role in the organization of endoplasmic reticulum exit sites. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P) and phosphatidylinositol 5-phosphate (PI(5)P). {ECO:0000269|PubMed:10400679, ECO:0000269|PubMed:15623529, ECO:0000269|PubMed:22922100}.; . TISSUE SPECIFICITY: Ubiquitously expressed with stronger levels detected in heart, liver and skeletal muscle. {ECO:0000269|PubMed:10400679}.; . . 0.64566 0.22552 0.161677043 64.96225525 282.64086 3.59867 SEC24A 1.31213682191576e-05 0.999969557220104 1.73214116770792e-05 SEC24 homolog A, COPII coat complex component FUNCTION: Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.; . TISSUE SPECIFICITY: Expressed in fibroblasts, hepatocytes, and lymphocytes.; unclassifiable (Anatomical System);muscle;colon;blood;choroid;skeletal muscle;retina;bone marrow;breast;whole body;lung;endometrium;placenta;visual apparatus;testis;brain; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion; 0.19793 0.09969 -1.058182374 7.554847841 248.85929 3.39890 SEC24B 0.999867447443696 0.000132552556174799 1.29019937925895e-13 SEC24 homolog B, COPII coat complex component FUNCTION: Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.; . TISSUE SPECIFICITY: Expressed in fibroblasts, hepatocytes, and lymphocytes.; ovary;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; prefrontal cortex;trigeminal ganglion; 0.15148 0.10884 -1.304353358 4.91861288 99.13633 2.15449 SEC24B-AS1 . . . SEC24B antisense RNA 1 . . . . . . . . . . . SEC24C 0.999992339582229 7.6604177564115e-06 1.50113043526113e-14 SEC24 homolog C, COPII coat complex component FUNCTION: Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex. {ECO:0000269|PubMed:10075675, ECO:0000269|PubMed:10214955, ECO:0000269|PubMed:10329445}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10329445}.; ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; testis - seminiferous tubule; 0.32022 0.09529 -0.968173992 8.982071243 215.09351 3.16444 SEC24D 0.00209421159390303 0.997898727921288 7.06048480884257e-06 SEC24 homolog D, COPII coat complex component FUNCTION: Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.; . TISSUE SPECIFICITY: Ubiquitously expressed, with higher amounts in placenta, pancreas, heart and liver.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;liver;cervix;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.69117 0.12413 1.18495331 92.84029252 374.7432 4.08174 SEC31A 0.00369934559039677 0.996300527199387 1.27210216226784e-07 SEC31 homolog A, COPII coat complex component FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity). {ECO:0000250, ECO:0000269|PubMed:10788476}.; DISEASE: Note=A chromosomal aberration involving SEC31A is associated with inflammatory myofibroblastic tumors (IMTs). Translocation t(2;4)(p23;q21) with ALK.; TISSUE SPECIFICITY: Abundantly and ubiquitously expressed. {ECO:0000269|PubMed:10574704, ECO:0000269|PubMed:10788476}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum;thymus; dorsal root ganglion;amygdala;superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion; 0.39013 0.13588 -0.990222991 8.634111819 387.14566 4.14299 SEC31B 1.30061598943069e-24 0.00104657734684148 0.998953422653158 SEC31 homolog B, COPII coat complex component FUNCTION: As a component of the coat protein complex II (COPII), may function in vesicle budding and cargo export from the endoplasmic reticulum. {ECO:0000269|PubMed:16495487}.; . TISSUE SPECIFICITY: Ubiquitously expressed at low levels with specific expression in thymus and testis. Expressed in testis by Sertoli cells, Leydig cells and spermatogonia and in cerebellum more prominently by Purkinje and granular cells (at protein level). {ECO:0000269|PubMed:10788476, ECO:0000269|PubMed:16495487}.; . . 0.06552 0.07762 2.081666378 97.82377919 8025.98175 19.31489 SEC61A1 0.995608071830047 0.00439184907724369 7.90927092716191e-08 Sec61 translocon alpha 1 subunit FUNCTION: Plays a crucial role in the insertion of secretory and membrane polypeptides into the ER. Required for assembly of membrane and secretory proteins. Tightly associated with membrane- bound ribosomes, either directly or through adapter proteins.; . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;cerebral cortex;oesophagus;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;blood;lens;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; prostate;pancreas;adipose tissue;smooth muscle;lung;thyroid;placenta;liver;adrenal cortex; 0.85984 0.40044 -0.538132194 20.26421326 4.38651 0.15944 SEC61A2 0.950042172255429 0.0499565346423954 1.29310217567767e-06 Sec61 translocon alpha 2 subunit FUNCTION: Appears to play a crucial role in the insertion of secretory and membrane polypeptides into the ER. It is required for assembly of membrane and secretory proteins. Found to be tightly associated with membrane-bound ribosomes, either directly or through adaptor proteins (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;lacrimal gland;hypothalamus;lens;skin;uterus;prostate;lung;frontal lobe;endometrium;larynx;placenta;bone;visual apparatus;hippocampus;liver;testis;head and neck;spleen;brain;mammary gland;cerebellum; amygdala;superior cervical ganglion;subthalamic nucleus;medulla oblongata;occipital lobe;globus pallidus;testis;pons;cingulate cortex; 0.87734 0.15588 -0.427900189 25.14744043 685.22003 5.22686 SEC61B 0.74284023328671 0.246329972713076 0.0108297940002139 Sec61 translocon beta subunit FUNCTION: Necessary for protein translocation in the endoplasmic reticulum.; . . lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;heart;islets of Langerhans;pineal body;muscle;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; . 0.09849 0.12971 -0.09720619 46.20193442 9.37075 0.34462 SEC61G 0.611529456532535 0.35386654575386 0.0346039977136054 Sec61 translocon gamma subunit FUNCTION: Necessary for protein translocation in the endoplasmic reticulum. {ECO:0000250}.; . . ovary;skin;bone marrow;prostate;cochlea;endometrium;thyroid;bladder;brain;heart;tongue;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);trophoblast;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; smooth muscle;heart; 0.21270 . 0.145304857 63.81221986 . . SEC62 0.967257862682972 0.0327311483266992 1.09889903283522e-05 SEC62 homolog, preprotein translocation factor FUNCTION: Required for preprotein translocation. {ECO:0000250}.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;amniotic fluid;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; medulla oblongata;occipital lobe;superior cervical ganglion;subthalamic nucleus;olfactory bulb;prefrontal cortex;globus pallidus;pons;parietal lobe;cingulate cortex; 0.73260 0.12221 0.371224249 75.12384996 150.4239 2.67702 SEC62-AS1 . . . SEC62 antisense RNA 1 . . . . . . . . . . . SEC63 1.24261908060209e-05 0.999895027797944 9.254601125033e-05 SEC63 homolog, protein translocation regulator FUNCTION: Required for integral membrane and secreted preprotein translocation across the endoplasmic reticulum membrane.; . TISSUE SPECIFICITY: Widely expressed, with high levels in the liver. {ECO:0000269|PubMed:15133510}.; . . 0.26756 0.15588 -0.578583623 18.71903751 221.36898 3.21909 SEC63P1 . . . SEC63 homolog, protein translocation regulator pseudogene 1 . . . . . . . . . . . SEC63P2 . . . SEC63 homolog, protein translocation regulator pseudogene 2 . . . . . . . . . . . SECISBP2 1.29314962997414e-09 0.931695282333941 0.0683047163729094 SECIS binding protein 2 FUNCTION: Binds to the SECIS element in the 3'-UTR of some mRNAs encoding selenoproteins. Binding is stimulated by SELB.; . TISSUE SPECIFICITY: Expressed at high levels in testis. {ECO:0000269|PubMed:12095701}.; . . 0.09040 0.09001 -0.530852121 20.82448691 318.59481 3.79049 SECISBP2L 0.10171305162342 0.898284448082132 2.50029444783592e-06 SECIS binding protein 2 like FUNCTION: Binds SECIS (Sec insertion sequence) elements present on selenocysteine (Sec) protein mRNAs, but does not promote Sec incorporation into selenoproteins in vitro.; . . ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;skeletal muscle;breast;pancreas;lung;placenta;hippocampus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;amygdala;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;olfactory bulb;temporal lobe;spinal cord;pons;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; . . -0.929520514 9.683887709 1626.14312 7.45523 SECTM1 0.172404202643393 0.769674220873956 0.0579215764826511 secreted and transmembrane 1 FUNCTION: May be involved in thymocyte signaling. {ECO:0000269|PubMed:15742156}.; . TISSUE SPECIFICITY: Detected at the highest levels in peripheral blood leukocytes and breast cancer cell lines. Found in leukocytes of the myeloid lineage, with the strongest expression observed in granulocytes and no detectable expression in lymphocytes. Expressed in thymic epithelial cells and fibroblasts. {ECO:0000269|PubMed:15742156, ECO:0000269|PubMed:9480746}.; smooth muscle;ovary;salivary gland;colon;parathyroid;uterus;prostate;endometrium;synovium;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;bile duct;pancreas;lung;placenta;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; whole blood; 0.09004 0.07829 0.907624513 89.46685539 155.45212 2.72416 SEH1L 0.745892347230499 0.254011530959634 9.6121809867136e-05 SEH1 like nucleoporin FUNCTION: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. As a component of the GATOR2 complex, inhibits GATOR1 complex, an inhibitor of the amino acid-sensing branch of the TORC1 pathway. {ECO:0000269|PubMed:15146057, ECO:0000269|PubMed:17363900, ECO:0000269|PubMed:23723238}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;whole brain;medulla oblongata;superior cervical ganglion;occipital lobe;temporal lobe;prefrontal cortex;pons;parietal lobe;cingulate cortex; 0.75475 0.13679 -0.115612493 45.12856806 70.573 1.74850 SEL1L 0.704308255469323 0.295691491200072 2.533306044389e-07 SEL1L ERAD E3 ligase adaptor subunit FUNCTION: May play a role in Notch signaling (By similarity). May be involved in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. {ECO:0000250, ECO:0000269|PubMed:16186509}.; . TISSUE SPECIFICITY: Highly expressed in pancreas.; myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;atrium;larynx;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;adrenal gland;placenta;head and neck;kidney;stomach;aorta; dorsal root ganglion;pancreas;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.36570 0.18583 0.154398214 64.73814579 162.19537 2.78150 SEL1L2 2.6912869713909e-11 0.435820280408388 0.564179719564699 SEL1L2 ERAD E3 ligase adaptor subunit . . . unclassifiable (Anatomical System); testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node; 0.14689 0.07440 0.42259095 77.22929936 615.74121 5.01110 SEL1L3 0.628820331551994 0.371179563493711 1.04954294923466e-07 SEL1L family member 3 . . . ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;small intestine;heart;islets of Langerhans;muscle;adrenal cortex;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;amnion;liver;cervix;kidney;mammary gland;stomach;aorta;cerebellum; . . . -0.126743121 44.0905874 627.79709 5.05070 SELE 1.6649159169351e-08 0.617878004307517 0.382121979043324 selectin E FUNCTION: Cell-surface glycoprotein having a role in immunoadhesion. Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with PSGL1/SELPLG. May have a role in capillary morphogenesis. {ECO:0000269|PubMed:1689848}.; . . unclassifiable (Anatomical System);smooth muscle;heart;cartilage;hypothalamus;parathyroid;vein;skeletal muscle;uterus;lung;thyroid;testis;mammary gland;tonsil; ciliary ganglion;trigeminal ganglion; 0.08178 0.53496 1.333822178 94.22033498 1648.8509 7.50245 SELENBP1 1.22411207379355e-06 0.81229888011219 0.187699895775736 selenium binding protein 1 FUNCTION: Selenium-binding protein which may be involved in the sensing of reactive xenobiotics in the cytoplasm. May be involved in intra-Golgi protein transport (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in liver, lung, colon, prostate, kidney and pancreas. In brain, present both in neurons and glia (at protein level). Down-regulated in lung adenocarcinoma, colorectal carcinoma and ovarian cancer. Two-fold up-regulated in brain and blood from schizophrenia patients. {ECO:0000269|PubMed:14991897, ECO:0000269|PubMed:16223876, ECO:0000269|PubMed:16380993, ECO:0000269|PubMed:16645984, ECO:0000269|PubMed:9679983}.; . . 0.25708 . -0.644723694 16.52512385 230.78602 3.28434 SELL 0.00173463089981873 0.894874381484417 0.103390987615765 selectin L FUNCTION: Cell surface adhesion protein. Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of leukocytes in endothelia. {ECO:0000269|PubMed:12403782}.; . TISSUE SPECIFICITY: Expressed in B-cell lines and T-lymphocytes. {ECO:0000269|PubMed:2473156}.; ovary;umbilical cord;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;pharynx;blood;breast;lung;nasopharynx;placenta;liver;spleen;kidney;stomach;aorta;thymus; superior cervical ganglion;lymph node;white blood cells;whole blood;tonsil;bone marrow; 0.25849 0.56432 0.793752871 87.40268931 3687.04461 11.82759 SELP 4.62464817320191e-20 0.00264898439763095 0.997351015602369 selectin P FUNCTION: Ca(2+)-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with PSGL1. {ECO:0000269|PubMed:7585950}.; . TISSUE SPECIFICITY: Stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. Upon cell activation by agonists, P-selectin is transported rapidly to the cell surface.; unclassifiable (Anatomical System);cartilage;fovea centralis;choroid;lens;skeletal muscle;retina;pancreas;prostate;optic nerve;lung;frontal lobe;oesophagus;larynx;nasopharynx;bone;thyroid;placenta;macula lutea;liver;testis;head and neck;spleen;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05857 0.53017 1.008569289 90.80561453 1329.25055 6.85373 SELPLG 0.00495442531161246 0.693893837723935 0.301151736964452 selectin P ligand FUNCTION: A SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E-, P- and L-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture. {ECO:0000269|PubMed:11566773, ECO:0000269|PubMed:12403782}.; . TISSUE SPECIFICITY: Expressed on neutrophils, monocytes and most lymphocytes.; unclassifiable (Anatomical System);uterus;lymph node;placenta;blood;brain;thymus;bone marrow; superior cervical ganglion;spinal cord;white blood cells;whole blood;skeletal muscle;bone marrow; 0.02498 0.13249 1.219937511 93.19414956 2358.88465 9.01273 SEMA3A 0.988432782312704 0.0115672162699479 1.41734788821873e-09 semaphorin 3A FUNCTION: Involved in the development of the olfactory system and in neuronal control of puberty. Induces the collapse and paralysis of neuronal growth cones. Could serve as a ligand that guides specific growth cones by a motility-inhibiting mechanism. Binds to the complex neuropilin-1/plexin-1. {ECO:0000269|PubMed:22416012}.; DISEASE: Hypogonadotropic hypogonadism 16 with or without anosmia (HH16) [MIM:614897]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:22416012, ECO:0000269|PubMed:22927827, ECO:0000269|PubMed:25077900}. Note=The disease may be caused by mutations affecting distinct genetic loci, including the gene represented in this entry.; . unclassifiable (Anatomical System);heart;ovary;cartilage;skeletal muscle;skin;retina;uterus;breast;lung;visual apparatus;liver;testis;brain; dorsal root ganglion;superior cervical ganglion;appendix;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.84810 0.41367 0.336225928 73.67893371 228.57596 3.26594 SEMA3B . . . semaphorin 3B FUNCTION: Inhibits axonal extension by providing local signals to specify territories inaccessible for growing axons. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed abundantly but differentially in a variety of neural and nonneural tissues.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;endometrium;bone;iris;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;breast;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;occipital lobe;thalamus;olfactory bulb;adrenal gland;placenta;spinal cord;adrenal cortex;prefrontal cortex;caudate nucleus;parietal lobe; 0.37836 0.14710 . . . . SEMA3B-AS1 . . . SEMA3B antisense RNA 1 (head to head) . . . . . . . . . . . SEMA3C 0.296856253558956 0.70313652214893 7.22429211477407e-06 semaphorin 3C FUNCTION: Binds to plexin family members and plays an important role in the regulation of developmental processes. Required for normal cardiovascular development during embryogenesis. Functions as attractant for growing axons, and thereby plays an important role in axon growth and axon guidance (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed intensely in the heart, skeletal muscle, colon, small intestine, ovary, testis, and prostate. Faint expression ubiquitously among other organs, including brain.; medulla oblongata;smooth muscle;sympathetic chain;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;testis;dura mater;brain;bladder;unclassifiable (Anatomical System);amygdala;meninges;heart;cartilage;hypothalamus;blood;skeletal muscle;bile duct;breast;pancreas;pia mater;lung;adrenal gland;visual apparatus;liver;duodenum;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;fetal brain;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.23302 0.18797 -0.619039275 17.39797122 657.84766 5.14333 SEMA3D 3.53080230466104e-05 0.999862590300224 0.000102101676729171 semaphorin 3D FUNCTION: Induces the collapse and paralysis of neuronal growth cones. Could potentially act as repulsive cues toward specific neuronal populations. Binds to neuropilin (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;cochlea;endometrium;bone;macula lutea;testis;spleen;amniotic fluid;artery;aorta;stomach; superior cervical ganglion;temporal lobe;globus pallidus;atrioventricular node;trigeminal ganglion; 0.63818 . -0.264476624 34.8844067 2380.10213 9.05539 SEMA3E 0.0304478723822677 0.969535111771292 1.70158464398353e-05 semaphorin 3E FUNCTION: Plays an important role in signaling via the cell surface receptor PLXND1. Mediates reorganization of the actin cytoskeleton, leading to the retraction of cell projections. Promotes focal adhesion disassembly and inhibits adhesion of endothelial cells to the extracellular matrix. Regulates angiogenesis, both during embryogenesis and after birth. Can down- regulate sprouting angiogenesis. Required for normal vascular patterning during embryogenesis. Plays an important role in ensuring the specificity of synapse formation (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);pancreas;lymph node;ovary;nasopharynx;trabecular meshwork;iris;testis;kidney;brain;skeletal muscle; amygdala; 0.09259 0.11165 -0.797234383 12.48525596 1048.49469 6.21822 SEMA3F 0.999917700468544 8.22995304693593e-05 9.86844713954074e-13 semaphorin 3F FUNCTION: May play a role in cell motility and cell adhesion.; . TISSUE SPECIFICITY: Expressed abundantly but differentially in a variety of neural and nonneural tissues. There is high expression in mammary gland, kidney, fetal brain, and lung and lower expression in heart and liver.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;synovium;thyroid;bone;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;cervix;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;thalamus;tongue;placenta;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.40000 0.14869 -0.264476624 34.8844067 403.76892 4.21565 SEMA3F-AS1 . . . SEMA3F antisense RNA 1 . . . . . . . . . . . SEMA3G 6.07682770496396e-10 0.842094453464701 0.157905545927616 semaphorin 3G FUNCTION: Has chemorepulsive activities for sympathetic axons. Ligand of NRP2 (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;lung;cerebral cortex;placenta;thyroid;bone;macula lutea;visual apparatus;kidney;spinal ganglion;brain;stomach; skeletal muscle; 0.14479 0.10790 -0.659500046 16.07100731 151.66127 2.69350 SEMA4A 0.615371620982326 0.384614128865517 1.42501521577794e-05 semaphorin 4A FUNCTION: Cell surface receptor for PLXNB1, PLXNB2, PLXNB3 and PLXND1 that plays an important role in cell-cell signaling. Plays a role in priming antigen-specific T-cells, promotes differentiation of Th1 T-helper cells, and thereby contributes to adaptive immunity. Promotes phosphorylation of TIMD2. Inhibits angiogenesis. Promotes axon growth cone collapse. Inhibits axonal extension by providing local signals to specify territories inaccessible for growing axons (By similarity). {ECO:0000250}.; DISEASE: Retinitis pigmentosa 35 (RP35) [MIM:610282]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:16199541}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cone-rod dystrophy 10 (CORD10) [MIM:610283]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. {ECO:0000269|PubMed:16199541}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;adrenal medulla;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;blood;breast;pancreas;lung;placenta;hypopharynx;liver;head and neck;mammary gland; superior cervical ganglion; 0.76767 0.12700 0.023941474 55.75607455 510.94958 4.62858 SEMA4B 0.00160800069630225 0.997148904463158 0.0012430948405394 semaphorin 4B FUNCTION: Inhibits axonal extension by providing local signals to specify territories inaccessible for growing axons. {ECO:0000250}.; . . colon;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;thyroid;iris;brain;unclassifiable (Anatomical System);lymph node;blood;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; . 0.13489 0.10113 -0.036738982 50.53668318 1432.54344 7.06541 SEMA4C 0.999373139159557 0.000626860154408693 6.86034706283716e-10 semaphorin 4C FUNCTION: Cell surface receptor for PLXNB2 that plays an important role in cell-cell signaling. PLXNB2 binding promotes downstream activation of RHOA and phosphorylation of ERBB2 at 'Tyr-1248'. Required for normal brain development, axon guidance and cell migration (By similarity). Probable signaling receptor which may play a role in myogenic differentiation through activation of the stress-activated MAPK cascade. {ECO:0000250, ECO:0000269|PubMed:17498836}.; . . smooth muscle;ovary;sympathetic chain;parathyroid;fovea centralis;choroid;retina;uterus;optic nerve;endometrium;cerebral cortex;thyroid;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; dorsal root ganglion;olfactory bulb;placenta;atrioventricular node;trigeminal ganglion; 0.61716 0.15612 -0.775187015 13.05142722 605.52004 4.98023 SEMA4D 0.995825192024996 0.00417479383422217 1.41407816190307e-08 semaphorin 4D FUNCTION: Cell surface receptor for PLXN1B and PLXNB2 that plays an important role in cell-cell signaling. Promotes reorganization of the actin cytoskeleton and plays a role in axonal growth cone guidance in the developing central nervous system. Regulates dendrite and axon branching and morphogenesis. Promotes the migration of cerebellar granule cells and of endothelial cells. Plays a role in the immune system; induces B-cells to aggregate and improves their viability (in vitro). Promotes signaling via SRC and PTK2B/PYK2, which then mediates activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Interaction with PLXNB1 mediates activation of RHOA. {ECO:0000269|PubMed:16055703, ECO:0000269|PubMed:19788569, ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:8876214}.; . TISSUE SPECIFICITY: Strongly expressed in skeletal muscle, peripheral blood lymphocytes, spleen, and thymus and also expressed at lower levels in testes, brain, kidney, small intestine, prostate, heart, placenta, lung and pancreas, but not in colon and liver. {ECO:0000269|PubMed:8876214}.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;pineal gland;brain;amygdala;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;spinal cord;urinary;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach;thymus; medulla oblongata;hypothalamus;white blood cells;caudate nucleus;whole blood; 0.23550 0.22400 0.123045693 62.23755603 3261.67374 10.88836 SEMA4F 6.7352998574131e-10 0.857591602583366 0.142408396743104 ssemaphorin 4F FUNCTION: Has growth cone collapse activity against retinal ganglion-cell axons. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;umbilical cord;heart;colon;blood;fovea centralis;choroid;lens;skin;retina;uterus;breast;prostate;optic nerve;lung;synovium;bone;placenta;macula lutea;liver;testis;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.08110 0.09449 -1.061810361 7.519462137 110.21044 2.28329 SEMA4G 0.000802235120632221 0.998512845058033 0.000684919821334581 semaphorin 4G FUNCTION: Cell surface receptor for PLXNB2. May play a role in axon guidance (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;cartilage;pineal body;colon;skeletal muscle;prostate;optic nerve;lung;frontal lobe;synovium;placenta;liver;testis;spleen;cervix;kidney;brain;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.16354 0.10894 -1.126142808 6.564048125 179.90491 2.91498 SEMA5A 0.000979594322677327 0.999016140899957 4.2647773658593e-06 semaphorin 5A FUNCTION: Bifunctional axonal guidance cue regulated by sulfated proteoglycans; attractive effects result from interactions with heparan sulfate proteoglycans (HSPGs), while the inhibitory effects depend on interactions with chondroitin sulfate proteoglycans (CSPGs) (By similarity). Ligand for receptor PLXNB3. In glioma cells, SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin stress fibers, disruption of focal adhesions and cellular collapse as well as inhibition of cell migration and invasion through ARHGDIA-mediated inactivation of RAC1. May promote angiogenesis by increasing endothelial cell proliferation and migration and inhibiting apoptosis. {ECO:0000250, ECO:0000269|PubMed:15218527, ECO:0000269|PubMed:19850054, ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:21706053}.; . . . . 0.23092 0.10687 -2.892521092 0.583864119 185.92785 2.96172 SEMA5B 0.00033149979824729 0.999648260065092 2.02401366607334e-05 semaphorin 5B FUNCTION: May act as positive axonal guidance cues. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;tongue;colon;parathyroid;fovea centralis;choroid;lens;retina;uterus;breast;optic nerve;lung;frontal lobe;placenta;macula lutea;visual apparatus;testis;head and neck;kidney;brain; . 0.71231 0.10725 -0.453812624 23.73201227 2905.53502 10.22279 SEMA6A 0.999546536591411 0.000453463096922415 3.11666709857472e-10 semaphorin 6A FUNCTION: Cell surface receptor for PLXNA2 that plays an important role in cell-cell signaling. Required for normal granule cell migration in the developing cerebellum. Promotes reorganization of the actin cytoskeleton and plays an important role in axon guidance in the developing central nervous system. Can act as repulsive axon guidance cue. Has repulsive action towards migrating granular neurons. May play a role in channeling sympathetic axons into the sympathetic chains and controlling the temporal sequence of sympathetic target innervation (By similarity). {ECO:0000250}.; . . ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;lens;skeletal muscle;breast;lung;epididymis;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;mammary gland;stomach;cerebellum; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;adrenal gland;adrenal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.56513 0.46987 -0.058785319 48.90894079 464.02903 4.46288 SEMA6A-AS1 . . . SEMA6A antisense RNA 1 . . . . . . . . . . . SEMA6B 0.742578966540981 0.257416942088222 4.09137079657213e-06 semaphorin 6B FUNCTION: May play a role in both peripheral and central nervous system development. {ECO:0000250}.; . . unclassifiable (Anatomical System);smooth muscle;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;optic nerve;frontal lobe;bone;macula lutea;hypopharynx;head and neck;mammary gland;brain;stomach; subthalamic nucleus;cingulate cortex; 0.25354 . . . 85.38111 1.96888 SEMA6C 5.65313335596491e-05 0.99867846861939 0.00126500004705063 semaphorin 6C FUNCTION: Shows growth cone collapsing activity on dorsal root ganglion (DRG) neurons in vitro. May be a stop signal for the DRG neurons in their target areas, and possibly also for other neurons. May also be involved in the maintenance and remodeling of neuronal connections. {ECO:0000269|PubMed:12110693}.; . TISSUE SPECIFICITY: In adult tissues, expressed only in skeletal muscle. {ECO:0000269|PubMed:12110693}.; unclassifiable (Anatomical System);urinary;muscle;colon;skeletal muscle;prostate;lung;frontal lobe;larynx;visual apparatus;iris;liver;testis;head and neck;kidney;brain;mammary gland; superior cervical ganglion;skeletal muscle; 0.15756 0.10044 . . 877.69789 5.76995 SEMA6D 0.999469975966626 0.00053002401471202 1.86619480007012e-11 semaphorin 6D FUNCTION: Shows growth cone collapsing activity on dorsal root ganglion (DRG) neurons in vitro. May be a stop signal for the DRG neurons in their target areas, and possibly also for other neurons. May also be involved in the maintenance and remodeling of neuronal connections.; . . ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;whole body;optic nerve;cerebral cortex;thyroid;spinal ganglion;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;lung;placenta;macula lutea;liver;head and neck;kidney;aorta; dorsal root ganglion;medulla oblongata;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.23915 0.15776 -0.725642751 14.24274593 1050.41264 6.22473 SEMA7A 0.0253934009542489 0.974061101369772 0.000545497675978764 semaphorin 7A (John Milton Hagen blood group) FUNCTION: Plays an important role in integrin-mediated signaling and functions both in regulating cell migration and immune responses. Promotes formation of focal adhesion complexes, activation of the protein kinase PTK2/FAK1 and subsequent phosphorylation of MAPK1 and MAPK3. Promotes production of proinflammatory cytokines by monocytes and macrophages. Plays an important role in modulating inflammation and T-cell-mediated immune responses. Promotes axon growth in the embryonic olfactory bulb. Promotes attachment, spreading and dendrite outgrowth in melanocytes. {ECO:0000269|PubMed:12879062, ECO:0000269|PubMed:17377534, ECO:0000269|PubMed:17671519}.; . TISSUE SPECIFICITY: Detected in skin keratinocytes and on endothelial cells from skin blood vessels (at protein level). Expressed in fibroblasts, keratinocytes, melanocytes, placenta, testis, ovary, spleen, brain, spinal chord, lung, heart, adrenal gland, lymph nodes, thymus, intestine and kidney. {ECO:0000269|PubMed:10201933, ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:9712866}.; unclassifiable (Anatomical System);ovary;colon;skin;bone marrow;uterus;breast;lung;frontal lobe;larynx;epididymis;bone;placenta;amnion;head and neck;germinal center;brain; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.30594 0.15579 -1.041578376 7.773059684 163.51267 2.79205 SEMG1 1.9424739088767e-14 0.00772893288160658 0.992271067118374 semenogelin I FUNCTION: Predominant protein in semen. It participates in the formation of a gel matrix entrapping the accessory gland secretions and ejaculated spermatozoa. Fragments of semenogelin and/or fragments of the related proteins may contribute to the activation of progressive sperm movements as the gel-forming proteins are fragmented by KLK3/PSA. {ECO:0000269|PubMed:19889947}.; . TISSUE SPECIFICITY: Seminal vesicle.; unclassifiable (Anatomical System);prostate;kidney;skeletal muscle; prostate;superior cervical ganglion; 0.03788 0.10996 0.88921411 89.24274593 246.22767 3.38629 SEMG2 6.77030449388864e-15 0.00215981772986247 0.997840182270131 semenogelin II FUNCTION: Participates in the formation of a gel matrix (sperm coagulum) entrapping the accessory gland secretions and ejaculated spermatozoa.; . TISSUE SPECIFICITY: Seminal vesicles, and to a much lesser extent, epididymis.; . . 0.15752 0.05654 1.069238311 91.68435952 924.18091 5.90361 SEN2 . . . senescence (cellular)-related 2 . . . . . . . . . . . SEN3 . . . senescence (cellular)-related 3 . . . . . . . . . . . SEN6 . . . senescence (cellular)-related 6 . . . . . . . . . . . SEN6A . . . senescence (cellular)-related 6A . . . . . . . . . . . SEN6B . . . senescence (cellular)-related 6B . . . . . . . . . . . SENCR . . . smooth muscle and endothelial cell enriched migration/differentiation-associated long non-coding RNA . . . . . . . . . . . SENP1 0.99389690234868 0.00610309041567082 7.23564961385748e-09 SUMO1/sentrin specific peptidase 1 FUNCTION: Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1 and BHLHE40/DEC1, which decreases its transcriptional repression activity. Deconjugates SUMO1 from CLOCK, which decreases its transcriptional activation activity. Deconjugates SUMO2 from MTA1. Desumoylates CCAR2 which decreases its interaction with SIRT1 (PubMed:25406032). {ECO:0000269|PubMed:10652325, ECO:0000269|PubMed:15199155, ECO:0000269|PubMed:16253240, ECO:0000269|PubMed:16553580, ECO:0000269|PubMed:21829689, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:23160374, ECO:0000269|PubMed:25406032}.; . TISSUE SPECIFICITY: Highly expressed in testis. Expressed at lower levels in thymus, pancreas, spleen, liver, ovary and small intestine. {ECO:0000269|PubMed:15487983}.; unclassifiable (Anatomical System);lymph node;heart;ovary;islets of Langerhans;parathyroid;skin;skeletal muscle;bone marrow;breast;uterus;bile duct;whole body;lung;placenta;visual apparatus;pituitary gland;liver;testis;germinal center;kidney;stomach;thymus; . 0.22807 0.13114 -0.049474214 50.01179523 80.87281 1.90059 SENP2 0.998304834433867 0.00169516524875663 3.17376312167552e-10 SUMO1/sentrin/SMT3 specific peptidase 2 FUNCTION: Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway. Deconjugates SUMO2 from MTA1. Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB (PubMed:20194620). {ECO:0000250|UniProtKB:Q91ZX6, ECO:0000250|UniProtKB:Q9EQE1, ECO:0000269|PubMed:11896061, ECO:0000269|PubMed:12192048, ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:21965678}.; . . medulla oblongata;ovary;colon;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;amnion;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;pons;trigeminal ganglion; 0.41070 0.10014 -0.137658575 43.57159707 2471.52197 9.26398 SENP3 0.995995419772783 0.00400451709895311 6.31282634233604e-08 SUMO1/sentrin/SMT3 specific peptidase 3 FUNCTION: Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates. Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability. Deconjugates SUMO2 and SUMO3 from CDCA8. Redox sensor that, when redistributed into nucleoplasm, can act as an effector to enhance HIF1A transcriptional activity by desumoylating EP300. Required for rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin, NPM1. Plays a role in the regulation of sumoylation status of ZNF148. Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. {ECO:0000269|PubMed:15743823, ECO:0000269|PubMed:16608850, ECO:0000269|PubMed:18259216, ECO:0000269|PubMed:18946085, ECO:0000269|PubMed:19015314, ECO:0000269|PubMed:19680224, ECO:0000269|PubMed:22872859}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;larynx;bone;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;adrenal cortex;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;head and neck;stomach; superior cervical ganglion;subthalamic nucleus;medulla oblongata;occipital lobe;globus pallidus;trigeminal ganglion; 0.73311 0.10866 . . 33.46733 1.03184 SENP3-EIF4A1 . . . SENP3-EIF4A1 readthrough (NMD candidate) . . . . . . . . . . . SENP5 0.996261182637231 0.00373876397817578 5.33845931462846e-08 SUMO1/sentrin specific peptidase 5 FUNCTION: Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO3 to its mature form and deconjugation of SUMO2 and SUMO3 from targeted proteins. Has weak proteolytic activity against full-length SUMO1 or SUMO1 conjugates. Required for cell division. {ECO:0000269|PubMed:16608850, ECO:0000269|PubMed:16738315}.; . . unclassifiable (Anatomical System);cartilage;ovary;colon;parathyroid;blood;vein;skin;skeletal muscle;bone marrow;breast;uterus;lung;larynx;bone;placenta;liver;testis;amniotic fluid;head and neck;spleen;kidney;stomach; dorsal root ganglion;testis - interstitial;medulla oblongata;occipital lobe;thalamus;superior cervical ganglion;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.10011 0.08014 0.376678994 75.50719509 224.33267 3.23870 SENP6 0.999876821596652 0.000123178403326144 2.18349664866213e-14 SUMO1/sentrin specific peptidase 6 FUNCTION: Protease that deconjugates SUMO1, SUMO2 and SUMO3 from targeted proteins. Processes preferentially poly-SUMO2 and poly- SUMO3 chains, but does not efficiently process SUMO1, SUMO2 and SUMO3 precursors. Deconjugates SUMO1 from RXRA, leading to transcriptional activation. Involved in chromosome alignment and spindle assembly, by regulating the kinetochore CENPH-CENPI-CENPK complex. Desumoylates PML and CENPI, protecting them from degradation by the ubiquitin ligase RNF4, which targets polysumoylated proteins for proteasomal degradation. Desumoylates also RPA1, thus preventing recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. {ECO:0000269|PubMed:16912044, ECO:0000269|PubMed:17000875, ECO:0000269|PubMed:18799455, ECO:0000269|PubMed:20212317, ECO:0000269|PubMed:20705237, ECO:0000269|PubMed:21148299}.; . TISSUE SPECIFICITY: Highly expressed in reproductive organs, such as testis, ovary and prostate.; myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;urinary;adrenal cortex;lens;skeletal muscle;breast;macula lutea;liver;mammary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;placenta;duodenum;head and neck;kidney;aorta;stomach;cerebellum; dorsal root ganglion;testis - interstitial;superior cervical ganglion;subthalamic nucleus;ciliary ganglion; 0.70503 0.08273 0.360092658 74.68152866 1761.80947 7.74789 SENP7 0.987260725175161 0.01273927480996 1.48795600813182e-11 SUMO1/sentrin specific peptidase 7 FUNCTION: Protease that deconjugates SUMO2 and SUMO3 from targeted proteins, but not SUMO1. Catalyzes the deconjugation of poly-SUMO2 and poly-SUMO3 chains. Has very low efficiency in processing full- length SUMO proteins to their mature forms. {ECO:0000269|PubMed:18799455}.; . . ovary;sympathetic chain;colon;parathyroid;skin;retina;uterus;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;spinal ganglion;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;skeletal muscle;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; subthalamic nucleus;cerebellum peduncles;globus pallidus;parietal lobe; 0.16333 0.08467 0.492370491 79.60603916 2875.14043 10.15092 SENP8 0.257288612865091 0.639948400017562 0.102762987117347 SUMO/sentrin peptidase family member, NEDD8 specific FUNCTION: Protease that catalyzes two essential functions in the NEDD8 pathway: processing of full-length NEDD8 to its mature form and deconjugation of NEDD8 from targeted proteins such as cullins or p53. {ECO:0000269|PubMed:12730221, ECO:0000269|PubMed:12759362, ECO:0000269|PubMed:12759363, ECO:0000269|PubMed:15242646, ECO:0000269|PubMed:15775960}.; . TISSUE SPECIFICITY: Broadly expressed, with highest levels in kidney and pancreas. {ECO:0000269|PubMed:12730221}.; unclassifiable (Anatomical System);heart;ovary;skin;uterus;lung;cerebral cortex;nasopharynx;placenta;liver;testis;spleen;cervix;kidney; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15874 0.13137 -0.029247611 51.40363293 5.41662 0.20041 SEPHS1 0.979964054551001 0.0200198509326306 1.60945163684159e-05 selenophosphate synthetase 1 FUNCTION: Synthesizes selenophosphate from selenide and ATP. {ECO:0000269|PubMed:7665581}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are gradually expressed during the cell cycle until G2/M phase and then decreased. Isoform 3 is gradually expressed during the cell cycle until S phase and then decreased. {ECO:0000269|PubMed:20471958}.; . . 0.69050 0.13588 -0.648365105 16.35999056 8.57528 0.31420 SEPHS1P1 . . . selenophosphate synthetase 1 pseudogene 1 . . . . . . . . . . . SEPHS1P2 . . . selenophosphate synthetase 1 pseudogene 2 . . . . . . . . . . . SEPHS1P3 . . . selenophosphate synthetase 1 pseudogene 3 . . . . . . . . . . . SEPHS1P4 . . . selenophosphate synthetase 1 pseudogene 4 . . . . . . . . . . . SEPHS1P6 . . . selenophosphate synthetase 1 pseudogene 6 . . . . . . . . . . . SEPHS1P7 . . . selenophosphate synthetase 1 pseudogene 7 . . . . . . . . . . . SEPHS2 0.00178605301440582 0.714776350162595 0.283437596822999 selenophosphate synthetase 2 FUNCTION: Synthesizes selenophosphate from selenide and ATP.; . . . . 0.11237 . 0.593509966 82.51356452 80.11336 1.89234 SEPHS2P1 . . . selenophosphate synthetase 2 pseudogene 1 . . . . . . . . . . . SEPN1 1.08497392205754e-07 0.54139889745718 0.458600994045428 selenoprotein N, 1 . DISEASE: Rigid spine muscular dystrophy 1 (RSMD1) [MIM:602771]: A neuromuscular disorder characterized by poor axial muscle strength, scoliosis and neck weakness, and a variable degree of spinal rigidity. Early ventilatory insufficiency can lead to death by respiratory failure. {ECO:0000269|PubMed:11528383, ECO:0000269|PubMed:12192640, ECO:0000269|PubMed:15122708, ECO:0000269|PubMed:19067361}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in skeletal muscle, brain, lung and placenta. Isoform 2 is also expressed in heart, diaphragm and stomach. {ECO:0000269|PubMed:11528383, ECO:0000269|PubMed:12700173}.; myocardium;ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;synovium;bone;thyroid;pituitary gland;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;adrenal cortex;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.14591 0.20188 0.621009802 83.41589998 291.70309 3.65394 SEPP1 3.00317467343857e-08 0.168253389778766 0.831746580189487 selenoprotein P, plasma, 1 FUNCTION: Might be responsible for some of the extracellular antioxidant defense properties of selenium or might be involved in the transport of selenium. May supply selenium to tissues such as brain and testis.; . TISSUE SPECIFICITY: Made in the liver and heart and secreted into the plasma. It is also found in the kidney.; . . 0.22046 . 0.573279816 82.08303845 972.64291 6.02905 SEPSECS 2.65169597190819e-06 0.916899223134043 0.0830981251699851 Sep (O-phosphoserine) tRNA:Sec (selenocysteine) tRNA synthase FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl- tRNA(Sec) required for selenoprotein biosynthesis. {ECO:0000269|PubMed:17142313}.; . TISSUE SPECIFICITY: Primarily expressed in liver, pancreas, kidney and lung. Overexpressed in PHA-stimulated T-cells.; ovary;colon;parathyroid;choroid;fovea centralis;retina;uterus;prostate;optic nerve;whole body;bone;pituitary gland;testis;germinal center;unclassifiable (Anatomical System);lymph node;muscle;blood;lens;skeletal muscle;lung;placenta;visual apparatus;macula lutea;liver;kidney;stomach; superior cervical ganglion;trigeminal ganglion; 0.22267 0.15573 -0.003562597 53.72729417 1010.18728 6.11987 SEPSECS-AS1 . . . SEPSECS antisense RNA 1 (head to head) . . . . . . . . . . . SEPT1 0.00293746552059533 0.984667172874706 0.0123953616046988 septin 1 FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}.; . TISSUE SPECIFICITY: Expressed at high levels in lymphoid and hematopoietic tissues. {ECO:0000269|PubMed:15915442}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;cartilage;heart;blood;choroid;skin;uterus;pancreas;lung;bone;placenta;visual apparatus;liver;testis;germinal center;kidney;brain;thymus; . 0.07045 0.12189 0.128714042 63.19886766 141.44381 2.59431 SEPT2 0.866554502924365 0.133365759546139 7.97375294961164e-05 septin 2 FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules, thus facilitating efficient vesicle transport, and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements. In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein. May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri. {ECO:0000269|PubMed:15774761, ECO:0000269|PubMed:17803907, ECO:0000269|PubMed:18209106, ECO:0000269|PubMed:19145258}.; . TISSUE SPECIFICITY: Widely expressed. Up-regulated in liver cancer. {ECO:0000269|PubMed:15915442, ECO:0000269|PubMed:19165576}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;nervous;spinal cord;pharynx;blood;lens;skeletal muscle;greater omentum;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;thymus; amygdala;occipital lobe;olfactory bulb;hypothalamus;thyroid;spinal cord;prefrontal cortex;testis;atrioventricular node;parietal lobe; 0.21998 0.20297 -0.007201372 53.19061099 11.01857 0.39905 SEPT2P1 . . . septin 2 pseudogene 1 . . . . . . . . . . . SEPT3 0.0692482029063671 0.927948089621432 0.00280370747220112 septin 3 FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}.; . TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:11322766, ECO:0000269|PubMed:15915442}.; ovary;salivary gland;colon;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cerebellum cortex;hypothalamus;spinal cord;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;head and neck;kidney;stomach;aorta;peripheral nerve; . 0.29233 0.11102 -0.295622497 32.61972163 52.36353 1.43092 SEPT4 0.0118368603873699 0.986479885390846 0.001683254221784 septin 4 FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in platelet secretion. Isoform ARTS, but not the other isoforms, is required for the induction of cell death mediated by TGF-beta and by other apoptotic stimuli. {ECO:0000250, ECO:0000269|PubMed:11146656, ECO:0000269|PubMed:15029247, ECO:0000269|PubMed:15116257, ECO:0000269|PubMed:15837787, ECO:0000269|PubMed:9889007, ECO:0000305}.; . TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues with highest expression in adult brain (at protein level), heart, liver and adrenal gland and fetal heart, kidney, liver and lung. Also expressed in colorectal cancers and malignant melanomas. Expressed in platelets. {ECO:0000269|PubMed:11146656, ECO:0000269|PubMed:11167005, ECO:0000269|PubMed:11511094, ECO:0000269|PubMed:15116257, ECO:0000269|PubMed:15915442, ECO:0000269|PubMed:9889007}.; sympathetic chain;colon;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cerebellum cortex;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; amygdala;whole brain;superior cervical ganglion;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;spinal cord;atrioventricular node;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.62368 0.20511 -0.800872469 12.33191791 2568.52414 9.46932 SEPT4-AS1 . . . SEPT4 antisense RNA 1 . . . . . . . . . . . SEPT5 0.914631982551485 0.0853431435519052 2.48738966095864e-05 septin 5 FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in platelet secretion (By similarity). {ECO:0000250, ECO:0000305}.; . TISSUE SPECIFICITY: Expressed at high levels in the CNS, as well as in heart and platelets (at protein level). {ECO:0000269|PubMed:12023038, ECO:0000269|PubMed:15915442}.; . . 0.28416 0.27805 -0.339715008 30.06605331 9.31247 0.34174 SEPT6 0.948998031817981 0.0509687515100205 3.32166719983479e-05 septin 6 FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Involved in cytokinesis. May play a role in HCV RNA replication. {ECO:0000269|PubMed:17229681, ECO:0000269|PubMed:17803907}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15915442}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;germinal center;bladder;brain;tonsil;cartilage;heart;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;atrium;whole body;oesophagus;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;hypothalamus;muscle;bile duct;pancreas;lung;pia mater;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; superior cervical ganglion;testis - interstitial;lymph node;adrenal cortex;tumor;white blood cells;atrioventricular node;bone marrow;testis - seminiferous tubule;adrenal gland;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;whole blood;tonsil;cingulate cortex;cerebellum;thymus; 0.46057 0.14570 -0.251530012 35.42108988 17.49919 0.61387 SEPT7 0.992377500380079 0.00762099605440174 1.50356551943386e-06 septin 7 FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements. {ECO:0000269|PubMed:17803907, ECO:0000269|PubMed:18460473}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15915442}.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;amygdala;heart;tongue;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;mammary gland;developmental;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;cerebral cortex;larynx;bone;pituitary gland;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; whole brain;dorsal root ganglion;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;thalamus;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;atrioventricular node;skin;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex; 0.73731 0.26107 . . 4.24738 0.15460 SEPT7-AS1 . . . SEPT7 antisense RNA 1 (head to head) . . . . . . . . . . . SEPT7P1 . . . septin 7 pseudogene 1 . . . . . . . . . . . SEPT7P2 . . . septin 7 pseudogene 2 . . . unclassifiable (Anatomical System);lung;islets of Langerhans;thyroid;testis; . . . . . . . SEPT7P3 . . . septin 7 pseudogene 3 . . . . . . . . . . . SEPT7P4 . . . septin 7 pseudogene 4 . . . . . . . . . . . SEPT7P5 . . . septin 7 pseudogene 5 . . . . . . . . . . . SEPT7P6 . . . septin 7 pseudogene 6 . . . . . . . . . . . SEPT7P7 . . . septin 7 pseudogene 7 . . . . . . . . . . . SEPT7P8 . . . septin 7 pseudogene 8 . . . . . . . . . . . SEPT7P9 . . . septin 7 pseudogene 9 . . . . . . . . . . . SEPT8 0.954285718069544 0.045689034982127 2.52469483294207e-05 septin 8 FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in platelet secretion. {ECO:0000250, ECO:0000269|PubMed:15116257, ECO:0000305}.; . TISSUE SPECIFICITY: Widely expressed, including in brain, heart and platelets; most abundant in aorta. Isoform 2 is expressed at low levels in specific brain areas, such as occipital pole, frontal lobe, temporal lobe and putamen. Isoform 1 and 3 are highly expressed in specific brain areas, such as occipital pole, frontal lobe, temporal lobe and putamen. Isoform 2 is highly expressed in prostate, testis and ovary. Isoform 1 and isoform 3 are expressed at low levels in prostate, testis and ovary. {ECO:0000269|PubMed:12023038, ECO:0000269|PubMed:12909369, ECO:0000269|PubMed:15116257, ECO:0000269|PubMed:15915442}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;endometrium;synovium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;oral cavity;spinal cord;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;stomach;cerebellum; amygdala;whole brain;superior cervical ganglion;thalamus;medulla oblongata;occipital lobe;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.93629 0.12092 -0.688817379 15.20405756 45.74838 1.30016 SEPT9 0.892006145895558 0.107948152489791 4.57016146507788e-05 septin 9 FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri. {ECO:0000250, ECO:0000305}.; DISEASE: Hereditary neuralgic amyotrophy (HNA) [MIM:162100]: Autosomal dominant form of recurrent focal neuropathy characterized clinically by acute, recurrent episodes of brachial plexus neuropathy with muscle weakness and atrophy preceded by severe pain in the affected arm. HNA is triggered by environmental factors such as infection or parturition. {ECO:0000269|PubMed:16186812, ECO:0000269|PubMed:17546647, ECO:0000269|PubMed:18492087, ECO:0000269|PubMed:19451530}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Isoforms are differentially expressed in testes, kidney, liver heart, spleen, brain, peripheral blood leukocytes, skeletal muscle and kidney. Specific isoforms appear to demonstrate tissue specificity. Isoform 5 is the most highly expressed in fetal tissue. Isoform 1 is detected in all tissues except the brain and thymus, while isoform 2, isoform 3, and isoform 4 are detected at low levels in approximately half of the fetal tissues. {ECO:0000269|PubMed:10339604, ECO:0000269|PubMed:10673329, ECO:0000269|PubMed:11593400, ECO:0000269|PubMed:15915442}.; lymphoreticular;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;urinary;pharynx;blood;cerebrum;breast;bile duct;pancreas;lung;cornea;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; prostate;heart;temporal lobe;white blood cells;whole blood;trigeminal ganglion;skeletal muscle;cerebellum;thymus; 0.33850 . -1.50462206 3.568058504 379.5764 4.10797 SEPT10 0.00288328636526247 0.984394153276616 0.0127225603581213 septin 10 FUNCTION: Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential). {ECO:0000305}.; . TISSUE SPECIFICITY: Widely expressed. Abundantly expressed in heart and kidney, placenta, skeletal muscles, liver and lung, as well as various tumor cell lines. {ECO:0000269|PubMed:12711328, ECO:0000269|PubMed:15915442}.; myocardium;medulla oblongata;ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;testis;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; testis - interstitial;superior cervical ganglion;testis;skeletal muscle; 0.50754 0.11337 -0.288341872 33.41589998 203.08148 3.07653 SEPT10P1 . . . septin 10 pseudogene 1 . . . . . . . . . . . SEPT11 0.68190156444561 0.317909581696648 0.000188853857741921 septin 11 FUNCTION: Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential). May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity (By similarity). During Listeria monocytogenes infection, not required for the bacterial entry process, but restricts its efficacy. {ECO:0000250, ECO:0000269|PubMed:15196925, ECO:0000269|PubMed:19234302, ECO:0000305}.; . TISSUE SPECIFICITY: Widely expressed, except in leukocytes. {ECO:0000269|PubMed:15196925, ECO:0000269|PubMed:15915442}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;bladder;brain;heart;cartilage;tongue;pineal body;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;lung;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta; whole brain;dorsal root ganglion;amygdala;medulla oblongata;superior cervical ganglion;occipital lobe;temporal lobe;caudate nucleus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.24971 0.12971 -0.317668748 31.45789101 20.19968 0.69128 SEPT12 4.59207575683259e-10 0.055985964268704 0.944014035272088 septin 12 FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15915442}.; unclassifiable (Anatomical System);medulla oblongata;lung;endometrium;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;cingulate cortex; 0.22113 0.10673 -0.378346116 28.01368247 184.01864 2.94463 SEPT14 4.96607463060426e-05 0.868917445373679 0.131032893880015 septin 14 FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:17922164}.; . . 0.22944 0.09039 0.841481379 88.35810333 262.69433 3.47731 SEPT14P1 . . . septin 14 pseudogene 1 . . . . . . . . . . . SEPT14P2 . . . septin 14 pseudogene 2 . . . . . . . . . . . SEPT14P3 . . . septin 14 pseudogene 3 . . . . . . . . . . . SEPT14P4 . . . septin 14 pseudogene 4 . . . . . . . . . . . SEPT14P5 . . . septin 14 pseudogene 5 . . . . . . . . . . . SEPT14P6 . . . septin 14 pseudogene 6 . . . . . . . . . . . SEPT14P7 . . . septin 14 pseudogene 7 . . . . . . . . . . . SEPT14P8 . . . septin 14 pseudogene 8 . . . . . . . . . . . SEPT14P10 . . . septin 14 pseudogene 10 . . . . . . . . . . . SEPT14P11 . . . septin 14 pseudogene 11 . . . . . . . . . . . SEPT14P12 . . . septin 14 pseudogene 12 . . . . . . . . . . . SEPT14P13 . . . septin 14 pseudogene 13 . . . . . . . . . . . SEPT14P14 . . . septin 14 pseudogene 14 . . . . . . . . . . . SEPT14P15 . . . septin 14 pseudogene 15 . . . . . . . . . . . SEPT14P16 . . . septin 14 pseudogene 16 . . . . . . . . . . . SEPT14P17 . . . septin 14 pseudogene 17 . . . . . . . . . . . SEPT14P18 . . . septin 14 pseudogene 18 . . . . . . . . . . . SEPT14P19 . . . septin 14 pseudogene 19 . . . . . . . . . . . SEPT14P20 . . . septin 14 pseudogene 20 . . . . . . . . . . . SEPT14P21 . . . septin 14 pseudogene 21 . . . . . . . . . . . SEPT14P22 . . . septin 14 pseudogene 22 . . . . . . . . . . . SEPT14P23 . . . septin 14 pseudogene 23 . . . . . . . . . . . SEPT14P24 . . . septin 14 pseudogene 24 . . . . . . . . . . . SEPW1 0.000743620933357238 0.526225105651844 0.473031273414799 selenoprotein W, 1 FUNCTION: Plays a role as a glutathione (GSH)-dependent antioxidant. May be involved in a redox-related process. May play a role in the myopathies of selenium deficiency (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in skeletal muscle and heart, moderate levels in brain, spinal cord, thyroid, spleen, prostate, ovary, small intestine and colon, and lowest levels in liver and lymph node. {ECO:0000269|PubMed:10718624, ECO:0000269|PubMed:12818432}.; . . 0.14471 . . . 164.93558 2.80812 SEPW1P . . . selenoprotein W, 1 pseudogene . . . myocardium;smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;frontal lobe;oesophagus;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;pineal body;muscle;urinary;pharynx;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;cerebellum; . . . . . . . SERAC1 0.0024009813989791 0.997457458331713 0.000141560269308011 serine active site containing 1 FUNCTION: Plays an important role in the phosphatidylglycerol remodeling that is essential for both mitochondrial function and intracellular cholesterol trafficking. May catalyze the remodeling of phosphatidylglycerol and be involved in the transacylation- acylation reaction to produce phosphatidylglycerol-36:1. May be involved in bis(monoacylglycerol)phosphate biosynthetic pathway. {ECO:0000269|PubMed:22683713}.; . TISSUE SPECIFICITY: Widely expressed, with predominant expression in fetal skeletal muscle and adult brain. In the brain, highest levels are found in the frontal and occipital cortices, cerebellum and hippocampus. {ECO:0000269|PubMed:22683713}.; . . 0.19774 0.09724 0.244401822 69.50931824 279.04465 3.58040 SERBP1 0.999863113808072 0.000136886108688978 8.32388184868044e-11 SERPINE1 mRNA binding protein 1 FUNCTION: May play a role in the regulation of mRNA stability. Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay.; . TISSUE SPECIFICITY: Expressed at high level in the heart, skeletal muscle and kidney, and at low levels in placenta, liver and brain. {ECO:0000269|PubMed:12505151}.; ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;tongue;pineal body;urinary;pharynx;blood;lens;skeletal muscle;breast;bronchus;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;synovium;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;bile duct;lung;pia mater;placenta;duodenum;head and neck;kidney;stomach;aorta; testis - interstitial;fetal liver;tumor;testis;white blood cells;skeletal muscle; 0.67038 0.17940 -0.339715008 30.06605331 17.23583 0.60518 SERBP1P1 . . . SERPINE1 mRNA binding protein 1 pseudogene 1 . . . . . . . . . . . SERBP1P2 . . . SERPINE1 mRNA binding protein 1 pseudogene 2 . . . . . . . . . . . SERBP1P3 . . . SERPINE1 mRNA binding protein 1 pseudogene 3 . . . . . . . . . . . SERBP1P4 . . . SERPINE1 mRNA binding protein 1 pseudogene 4 . . . . . . . . . . . SERBP1P5 . . . SERPINE1 mRNA binding protein 1 pseudogene 5 . . . . . . . . . . . SERBP1P6 . . . SERPINE1 mRNA binding protein 1 pseudogene 6 . . . . . . . . . . . SERF1A . . . small EDRK-rich factor 1A (telomeric) . . TISSUE SPECIFICITY: Isoform Long is predominantly expressed in heart, brain and skeletal muscle. Isoform Short and Isoform Long are expressed throughout the central nervous system, including spinal cord.; umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;bone;testis;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;cerebrum;skeletal muscle;breast;lung;cornea;placenta;visual apparatus;liver;kidney;mammary gland;stomach;cerebellum; . . . . . . . SERF1AP1 . . . small EDRK-rich factor 1A (telomeric) pseudogene 1 . . . . . . . . . . . SERF1B . . . small EDRK-rich factor 1B (centromeric) . . TISSUE SPECIFICITY: Isoform Long is predominantly expressed in heart, brain and skeletal muscle. Isoform Short and Isoform Long are expressed throughout the central nervous system, including spinal cord.; . . . . . . 0.96346 0.02405 SERF2 0.138975962472976 0.779592802372338 0.081431235154686 small EDRK-rich factor 2 . . . myocardium;lymphoreticular;ovary;umbilical cord;skin;bone marrow;retina;prostate;frontal lobe;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;cerebral cortex;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;duodenum;kidney;stomach; . 0.24204 0.11262 . . 2084.12462 8.40921 SERGEF 2.21836725525601e-10 0.130869793921616 0.869130205856547 secretion regulating guanine nucleotide exchange factor FUNCTION: Probable guanine nucleotide exchange factor (GEF), which may be involved in the secretion process.; . . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;lens;breast;lung;visual apparatus;macula lutea;head and neck;kidney;stomach; medulla oblongata;ciliary ganglion;skeletal muscle; 0.09569 0.09246 0.817616644 87.95116773 1281.17116 6.73905 SERHL . . . serine hydrolase-like (pseudogene) FUNCTION: Putative serine hydrolase.; . . ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;bile duct;pancreas;lung;epididymis;placenta;visual apparatus;duodenum;hypopharynx;head and neck;kidney;stomach; . 0.10684 . . . . . SERHL2 1.16697862264791e-11 0.00656171455440128 0.993438285433929 serine hydrolase-like 2 FUNCTION: Probable serine hydrolase. May be related to cell muscle hypertrophy.; . . colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;lung;epididymis;placenta;macula lutea;visual apparatus;hypopharynx;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;trigeminal ganglion; . . . . 426.8356 4.31646 SERINC1 0.0746214563362831 0.922893383314231 0.00248516034948546 serine incorporator 1 FUNCTION: Enhances the incorporation of serine into phosphatidylserine and sphingolipids. {ECO:0000250|UniProtKB:Q7TNK0}.; . . myocardium;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;pharynx;blood;skeletal muscle;breast;trabecular meshwork;macula lutea;liver;alveolus;spleen;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;aorta;thymus; amygdala;subthalamic nucleus;occipital lobe;thalamus;medulla oblongata;hypothalamus;spinal cord;prefrontal cortex;globus pallidus;pons;caudate nucleus;parietal lobe;cingulate cortex; 0.78071 0.11809 0.284856336 71.40835103 104.88692 2.21397 SERINC2 1.03374403745308e-06 0.547561581717533 0.452437384538429 serine incorporator 2 . . . . . 0.13954 . 0.180083178 66.16536919 226.68549 3.25418 SERINC3 0.590252231777824 0.409317758154851 0.000430010067325311 serine incorporator 3 FUNCTION: Restriction factor required to restrict infectivity of lentiviruses, such as HIV-1: acts by inhibiting an early step of viral infection. Impairs the penetration of the viral particle into the cytoplasm (PubMed:26416733, PubMed:26416734). {ECO:0000269|PubMed:26416733, ECO:0000269|PubMed:26416734}.; . TISSUE SPECIFICITY: Ubiquitous. Expression levels were increased fourfold to tenfold in lung tumor tissues compared with normal pulmonary tissues. {ECO:0000269|PubMed:10559794}.; medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;iris;germinal center;brain;gall bladder;amygdala;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;synovium;bone;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;pia mater;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;aorta;stomach; whole brain;amygdala;occipital lobe;superior cervical ganglion;testis - interstitial;temporal lobe;pons;subthalamic nucleus;placenta;prefrontal cortex;testis;globus pallidus;cingulate cortex;parietal lobe; 0.14485 0.16945 -0.157884861 42.05590941 228.06631 3.26217 SERINC4 0.0107594286376223 0.9465999072745 0.0426406640878775 serine incorporator 4 FUNCTION: Incorporates a polar amino acid serine into membranes and facilitates the synthesis of two serine-derived lipids, phosphatidylserine and sphingolipids. {ECO:0000269|PubMed:16120614}.; . . myocardium;ovary;colon;parathyroid;vein;skin;uterus;optic nerve;whole body;frontal lobe;cerebral cortex;pituitary gland;testis;germinal center;pineal gland;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;blood;lens;skeletal muscle;lung;epididymis;placenta;liver;spleen;cervix;kidney;stomach; . 0.36927 . . . 167.46472 2.82767 SERINC5 0.000839904080638089 0.98404523503193 0.0151148608874316 serine incorporator 5 FUNCTION: Restriction factor required to restrict infectivity of lentiviruses, such as HIV-1: acts by inhibiting an early step of viral infection. Impairs the penetration of the viral particle into the cytoplasm (PubMed:26416733, PubMed:26416734). Enhances the incorporation of serine into phosphatidylserine and sphingolipids. May play a role in providing serine molecules for the formation of myelin glycosphingolipids in oligodendrocytes (By similarity). {ECO:0000250|UniProtKB:Q63175, ECO:0000269|PubMed:26416733, ECO:0000269|PubMed:26416734}.; . TISSUE SPECIFICITY: Highly expressed in placenta, skeletal muscle, spleen, thymus, testis and peripheral leukocyte and is expressed weakly in the heart, liver and fetal brain. {ECO:0000269|PubMed:12688535}.; unclassifiable (Anatomical System);uterus;lung;heart;placenta;liver;colon;germinal center;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;placenta;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;cerebellum; 0.16090 0.13036 -0.203796826 38.81811748 323.28412 3.81982 SERP1 0.211802393028658 0.648077036042894 0.140120570928448 stress-associated endoplasmic reticulum protein 1 FUNCTION: Interacts with target proteins during their translocation into the lumen of the endoplasmic reticulum. Protects unfolded target proteins against degradation during ER stress. May facilitate glycosylation of target proteins after termination of ER stress. May modulate the use of N-glycosylation sites on target proteins (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;prostate;lung;trachea;adrenal gland;placenta;thyroid;liver;testis;white blood cells;trigeminal ganglion;whole blood;bone marrow; 0.22645 0.16306 0.035072054 56.2514744 1.87048 0.05880 SERP2 0.229121363041921 0.646467406467294 0.124411230490785 stress-associated endoplasmic reticulum protein family member 2 FUNCTION: May interact with target proteins during translocation into the lumen of the endoplasmic reticulum. May protect unfolded target proteins against degradation and facilitate correct glycosylation (Potential). {ECO:0000305}.; . . . . 0.26504 . 0.101211609 60.95777306 . . SERPINA1 3.65586459511635e-07 0.105699517598885 0.894300116814656 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1 FUNCTION: Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.; DISEASE: Alpha-1-antitrypsin deficiency (A1ATD) [MIM:613490]: A disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age. {ECO:0000269|PubMed:1905728, ECO:0000269|PubMed:2227940, ECO:0000269|PubMed:2390072}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Expressed in leukocytes and plasma. {ECO:0000269|PubMed:23826168}.; lymphoreticular;ovary;salivary gland;intestine;colon;choroid;skin;uterus;prostate;whole body;endometrium;bone;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;alveolus;liver;spleen;kidney;stomach;aorta; fetal liver;beta cell islets;liver;fetal lung;kidney;whole blood; 0.19452 0.79779 0.53464283 81.00967209 266.58272 3.50260 SERPINA2 . . . serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 2 (gene/pseudogene) FUNCTION: Putative serine protease inhibitor.; . TISSUE SPECIFICITY: Expressed in the liver, leukocytes and testis. Also detected in brain, colon, uterus, esophagus, spleen, trachea, kidney and lung. {ECO:0000269|PubMed:17135331, ECO:0000269|PubMed:23826168}.; . . 0.01880 0.14325 -1.639226005 2.789573013 . . SERPINA3 5.34007170592001e-12 0.00414304048508738 0.995856959509572 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3 FUNCTION: Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2. {ECO:0000269|PubMed:2404007}.; . TISSUE SPECIFICITY: Plasma. Synthesized in the liver. Like the related alpha-1-antitrypsin, its concentration increases in the acute phase of inflammation or infection. Found in the amyloid plaques from the hippocampus of Alzheimer disease brains. {ECO:0000269|PubMed:3257719, ECO:0000269|PubMed:9880565}.; . . 0.18315 0.38376 -0.420619508 25.72540694 1436.4047 7.07333 SERPINA4 1.58265231800216e-07 0.123329711336434 0.876670130398334 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 4 FUNCTION: Inhibits human amidolytic and kininogenase activities of tissue kallikrein. Inhibition is achieved by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and generation of a small C-terminal fragment of the inhibitor due to cleavage at the reactive site by tissue kallikrein. {ECO:0000269|PubMed:8227002}.; . TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; unclassifiable (Anatomical System);uterus;pancreas;lung;heart;islets of Langerhans;liver;colon;spleen;kidney;skin;stomach; dorsal root ganglion;superior cervical ganglion;fetal liver;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.11245 0.23924 -0.754958418 13.57631517 20.0632 0.68530 SERPINA5 0.0526385833218062 0.862424292560443 0.0849371241177506 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 5 FUNCTION: Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and proinflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant factor by inhibiting blood coagulation factors like prothrombin, factor XI, factor Xa, plasma kallikrein and fibrinolytic enzymes such as tissue- and urinary- type plasminogen activators. In seminal plasma, inactivates several serine proteases implicated in the reproductive system. Inhibits the serpin acrosin; indirectly protects component of the male genital tract from being degraded by excessive released acrosin. Inhibits tissue-and urinary-type plasminogen activator, prostate-specific antigen and kallikrein activities; has a control on the sperm motility and fertilization. Inhibits the activated protein C-catalyzed degradation of SEMG1 and SEMG2; regulates the degradation of semenogelin during the process of transfer of spermatozoa from the male reproductive tract into the female tract. In urine, inhibits urinary-type plasminogen activator and kallikrein activities. Inactivates membrane-anchored serine proteases activities such as MPRSS7 and TMPRSS11E. Inhibits urinary-type plasminogen activator-dependent tumor cell invasion and metastasis. May also play a non-inhibitory role in seminal plasma and urine as a hydrophobic hormone carrier by its binding to retinoic acid. {ECO:0000269|PubMed:10340997, ECO:0000269|PubMed:11722589, ECO:0000269|PubMed:14696115, ECO:0000269|PubMed:15140131, ECO:0000269|PubMed:15328353, ECO:0000269|PubMed:15853774, ECO:0000269|PubMed:1725227, ECO:0000269|PubMed:18467335, ECO:0000269|PubMed:2844223, ECO:0000269|PubMed:3501295, ECO:0000269|PubMed:6323392, ECO:0000269|PubMed:7521127, ECO:0000269|PubMed:7548057, ECO:0000269|PubMed:8536714, ECO:0000269|PubMed:8665956, ECO:0000269|PubMed:9473218, ECO:0000269|PubMed:9510955, ECO:0000269|PubMed:9556620}.; . TISSUE SPECIFICITY: Predominantly expressed in the epithelium of seminal vesicles. Expressed in the proximal tubular epithelium of the kidney. Expressed in the superficial and more differentiated epidermal keratinocytes of the skin. Expressed in megakaryocytes and platelets. Expressed poorly in kidney tumor cells compared to non tumor kidney tissues. Expressed in spermatozoa. Present in very high concentration in seminal plasma. Present in high concentration in plasma, synovial and Graaf follicle fluids. Present in low concentration in breast milk and in amniotic fluids. Present in very low concentration in urine, cerebrospinal fluids, saliva and tears (at protein level). Strongly expressed in liver. Expressed in kidney, spleen, pancreas, skeletal muscle, heart, testes, ovary, interstitial Leydig cells, epididymal glands, seminal vesicles and prostate. {ECO:0000269|PubMed:1372913, ECO:0000269|PubMed:14696115, ECO:0000269|PubMed:15140131, ECO:0000269|PubMed:17706750, ECO:0000269|PubMed:18467335, ECO:0000269|PubMed:9510955, ECO:0000269|PubMed:9556620}.; medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;endometrium;larynx;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;pancreas;fetal liver;testis - seminiferous tubule;adrenal gland;adrenal cortex;liver;testis;kidney;trigeminal ganglion; 0.23276 0.31401 0.624649618 83.53385232 1998.56973 8.23716 SERPINA6 5.27007649744634e-07 0.129673293982396 0.870326179009955 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 6 FUNCTION: Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species. {ECO:0000269|PubMed:18513745}.; DISEASE: Corticosteroid-binding globulin deficiency (CBG deficiency) [MIM:611489]: Extremely rare hereditary disorder characterized by reduced corticosteroid-binding capacity with normal or low plasma corticosteroid-binding globulin concentration, and normal or low basal cortisol levels associated with hypo/hypertension and muscle fatigue. {ECO:0000269|PubMed:10634411, ECO:0000269|PubMed:1504007, ECO:0000269|PubMed:17245537, ECO:0000269|PubMed:8212073}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma; synthesized in liver. Has also been identified in a number of glycocorticoid responsive cells.; unclassifiable (Anatomical System);lung;whole body;cartilage;heart;islets of Langerhans;visual apparatus;liver;testis;spleen;kidney; superior cervical ganglion;fetal liver;liver;kidney;trigeminal ganglion; 0.24452 0.21203 -0.490397599 22.50530786 53.95909 1.46439 SERPINA7 0.132498719622418 0.780143767171582 0.0873575132060006 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 7 FUNCTION: Major thyroid hormone transport protein in serum.; DISEASE: Thyroxine-binding globulin deficiency (TBG deficiency) [MIM:314200]: Mutations in the SERPINA7 gene can result as a whole spectrum of deficiencies, characterized by either reduced or increased TBG levels in the serum. Patients show, respectively, reduced or elevated protein-bound iodine but are euthyroid. {ECO:0000269|PubMed:1294376, ECO:0000269|PubMed:1515456, ECO:0000269|PubMed:1901689, ECO:0000269|PubMed:1906047, ECO:0000269|PubMed:2155256, ECO:0000269|PubMed:2501669}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;lung;visual apparatus;liver;spleen;kidney;brain;bladder; fetal liver;liver;trigeminal ganglion; 0.11134 0.13818 0.994001092 90.5579146 1584.88807 7.36351 SERPINA7P1 . . . serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 7 pseudogene 1 . . . . . . . . . . . SERPINA9 1.79474750647935e-09 0.0339931878082941 0.966006810396958 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 9 FUNCTION: Protease inhibitor that inhibits trypsin and trypsin- like serine proteases (in vitro). Inhibits plasmin and thrombin with lower efficiency (in vitro). {ECO:0000269|PubMed:17447896}.; . TISSUE SPECIFICITY: Highly expressed in normal germinal center (GC) B-cells and GC B-cell-derived malignancies. {ECO:0000269|PubMed:12819018, ECO:0000269|PubMed:17447896, ECO:0000269|PubMed:17898315, ECO:0000269|PubMed:18550480}.; germinal center;tonsil; dorsal root ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.04429 0.09455 2.778290809 99.02099552 5288.84851 15.03156 SERPINA10 1.21176106869289e-05 0.373281431474621 0.626706450914692 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 10 FUNCTION: Inhibits activity of the coagulation protease factor Xa in the presence of PROZ, calcium and phospholipids. Also inhibits factor XIa in the absence of cofactors. {ECO:0000269|PubMed:11049983}.; . TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; lung;liver;spleen; dorsal root ganglion;fetal liver;superior cervical ganglion;liver;ciliary ganglion;trigeminal ganglion;skeletal muscle;skin; 0.11936 0.14430 2.399644443 98.51380042 343.97285 3.93258 SERPINA11 1.4053679123183e-07 0.115413568276717 0.884586291186492 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 11 . . . unclassifiable (Anatomical System);whole body;endometrium;liver; fetal liver;superior cervical ganglion;liver;atrioventricular node;trigeminal ganglion; 0.06431 0.10024 0.020302773 55.60863411 1032.90536 6.17474 SERPINA12 7.46593117503427e-06 0.294546887643759 0.705445646425066 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 12 FUNCTION: Adipokine that modulates insulin action by specifically inhibiting its target protease KLK7 in white adipose tissues. {ECO:0000269|PubMed:16030142}.; . TISSUE SPECIFICITY: Expressed in visceral adipose tissues. {ECO:0000269|PubMed:16030142}.; uterus;heart;tongue;liver;head and neck;skin; . 0.03328 0.12166 1.420201535 94.92215145 125.40993 2.43738 SERPINA13P . . . serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 13, pseudogene . . . . . 0.05087 . . . . . SERPINA15P . . . serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 15, pseudogene . . . . . . . . . . . SERPINB1 0.0203430155859586 0.904146894992294 0.0755100894217471 serpin peptidase inhibitor, clade B (ovalbumin), member 1 FUNCTION: Regulates the activity of the neutrophil proteases elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and kallikrein-3. Also functions as a potent intracellular inhibitor of granzyme H. {ECO:0000269|PubMed:11747453}.; . . . . 0.12848 0.65153 0.020302773 55.60863411 207.99059 3.11412 SERPINB2 5.7582951955992e-05 0.69550390321213 0.304438513835914 serpin peptidase inhibitor, clade B (ovalbumin), member 2 FUNCTION: Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell- derived PAI-1.; . . unclassifiable (Anatomical System);lymphoreticular;cartilage;heart;islets of Langerhans;blood;skin;skeletal muscle;bone marrow;breast;uterus;whole body;lung;larynx;nasopharynx;thyroid;placenta;liver;alveolus;hypopharynx;testis;head and neck;spleen;stomach; superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node; 0.09511 0.37379 0.20030965 67.3566879 4701.43923 13.82304 SERPINB3 8.68913370901801e-14 0.00261772969296884 0.997382270306944 serpin peptidase inhibitor, clade B (ovalbumin), member 3 FUNCTION: May act as a papain-like cysteine protease inhibitor to modulate the host immune response against tumor cells. Also functions as an inhibitor of UV-induced apoptosis via suppression of the activity of c-Jun NH(2)-terminal kinase (JNK1). {ECO:0000269|PubMed:19166818}.; . TISSUE SPECIFICITY: Squamous cells. Expressed in some hepatocellular carcinoma (at protein level). {ECO:0000269|PubMed:14970861}.; unclassifiable (Anatomical System);tongue;skin;skeletal muscle;bone marrow;uterus;pancreas;lung;larynx;nasopharynx;thyroid;hypopharynx;head and neck;cervix;brain; dorsal root ganglion;superior cervical ganglion;trachea;tongue;atrioventricular node;trigeminal ganglion; 0.31680 0.31828 2.177262001 98.07147912 707.88934 5.28346 SERPINB4 1.27619533633833e-11 0.0132918143041207 0.986708185683117 serpin peptidase inhibitor, clade B (ovalbumin), member 4 FUNCTION: May act as a protease inhibitor to modulate the host immune response against tumor cells.; . TISSUE SPECIFICITY: Squamous cells.; unclassifiable (Anatomical System);tongue;skeletal muscle;uterus;pancreas;lung;oesophagus;larynx;nasopharynx;thyroid;hypopharynx;testis;head and neck;cervix;brain; dorsal root ganglion;superior cervical ganglion;trachea;tongue;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.07044 0.11679 -0.334253673 30.70299599 100.53866 2.17276 SERPINB5 0.450309366949428 0.543439438233888 0.00625119481668411 serpin peptidase inhibitor, clade B (ovalbumin), member 5 FUNCTION: Tumor suppressor. It blocks the growth, invasion, and metastatic properties of mammary tumors. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity.; . TISSUE SPECIFICITY: Normal mammary epithelial cells.; . . 0.09628 0.40321 0.420771676 77.15852795 4867.63996 14.18586 SERPINB6 0.0356687992106553 0.928371580180581 0.0359596206087639 serpin peptidase inhibitor, clade B (ovalbumin), member 6 FUNCTION: May be involved in the regulation of serine proteinases present in the brain or extravasated from the blood (By similarity). Inhibitor of cathepsin G, kallikrein-8 and thrombin. May play an important role in the inner ear in the protection against leakage of lysosomal content during stress and loss of this protection results in cell death and sensorineural hearing loss. {ECO:0000250, ECO:0000269|PubMed:10068683, ECO:0000269|PubMed:17761692, ECO:0000269|PubMed:20451170, ECO:0000269|PubMed:8136380, ECO:0000269|PubMed:8415716}.; . TISSUE SPECIFICITY: Expressed in keratinocytes (at protein level). Highest levels in skeletal muscle. Also found in placenta, cardiac muscle, lung, liver, kidney and pancreas. Expressed in the inner ear hair cells. Expressed abundantly by normal mast cells in different tissues and by mast cells in mastocytoma lesions. {ECO:0000269|PubMed:14670919, ECO:0000269|PubMed:17761692, ECO:0000269|PubMed:20451170}.; medulla oblongata;ovary;sympathetic chain;colon;parathyroid;choroid;vein;skin;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; testis - interstitial;testis - seminiferous tubule;testis; 0.58499 . -0.135838822 43.77211607 187.82392 2.97536 SERPINB7 7.67027798018844e-05 0.754207159847603 0.245716137372595 serpin peptidase inhibitor, clade B (ovalbumin), member 7 FUNCTION: Might function as an inhibitor of Lys-specific proteases. Might influence the maturation of megakaryocytes via its action as a serpin.; . TISSUE SPECIFICITY: Predominantly expressed in mesangial cells. Expressed in the epidermis of the whole body. {ECO:0000269|PubMed:24207119}.; unclassifiable (Anatomical System);lung;ovary;tongue;islets of Langerhans;nasopharynx;gum;placenta;liver;parathyroid;skin; superior cervical ganglion;skeletal muscle;skin;parietal lobe; 0.24932 0.14526 -0.358119787 29.16371786 1467.68906 7.13948 SERPINB8 6.74035819292039e-07 0.268926353253979 0.731072972710202 serpin peptidase inhibitor, clade B (ovalbumin), member 8 . . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;bone;testis;germinal center;artery;spinal ganglion;ciliary body;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;liver;cervix;head and neck;kidney;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11773 0.48758 0.354632714 74.58126917 1588.32892 7.37320 SERPINB8P1 . . . serpin peptidase inhibitor, clade B8 (ovalbumin) pseudogene 1 FUNCTION: Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. {ECO:0000269|PubMed:17562709}.; . TISSUE SPECIFICITY: Detected in a restricted number of tissues, including lung, placenta, prostate, and tonsil. {ECO:0000269|PubMed:17562709}.; . . 0.13544 . . . . . SERPINB9 0.00489853442133744 0.883532876342608 0.111568589236055 serpin peptidase inhibitor, clade B (ovalbumin), member 9 FUNCTION: Granzyme B inhibitor.; . . . . 0.44707 0.21847 -0.602450568 17.91106393 29.99819 0.95868 SERPINB9P1 . . . serpin peptidase inhibitor, clade B (ovalbumin), member 9, pseudogene 1 . . . . . . . . . . . SERPINB10 6.26724483578838e-05 0.713273104804852 0.28666422274679 serpin peptidase inhibitor, clade B (ovalbumin), member 10 FUNCTION: Protease inhibitor that may play a role in the regulation of protease activities during hematopoiesis and apoptosis induced by TNF. May regulate protease activities in the cytoplasm and in the nucleus. {ECO:0000269|PubMed:10871600, ECO:0000269|PubMed:7592909}.; . TISSUE SPECIFICITY: Expressed specifically in myeloid cells and the bone marrow. {ECO:0000269|PubMed:20433722, ECO:0000269|PubMed:7592909}.; larynx;blood;head and neck;bone marrow; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.19182 0.10917 1.355871599 94.40905874 11087.61292 22.91324 SERPINB11 5.09314823816963e-07 0.232568721069153 0.767430769616023 serpin peptidase inhibitor, clade B (ovalbumin), member 11 (gene/pseudogene) FUNCTION: Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. {ECO:0000269|PubMed:17562709}.; . TISSUE SPECIFICITY: Detected in a restricted number of tissues, including lung, placenta, prostate, and tonsil. {ECO:0000269|PubMed:17562709}.; . . 0.13544 . . . . . SERPINB12 7.75579414319893e-17 0.000298875117769565 0.999701124882231 serpin peptidase inhibitor, clade B (ovalbumin), member 12 FUNCTION: Inhibits trypsin and plasmin, but not thrombin, coagulation factor Xa, or urokinase-type plasminogen activator.; . TISSUE SPECIFICITY: Expressed in many tissues, including brain, bone marrow, lymph node, heart, lung, liver, pancreas, testis, ovary, and intestine.; . . 0.64256 0.12241 0.64123826 83.97617363 445.92863 4.39516 SERPINB13 0.000102298767913382 0.807809072738847 0.192088628493239 serpin peptidase inhibitor, clade B (ovalbumin), member 13 FUNCTION: May play a role in the proliferation or differentiation of keratinocytes.; . TISSUE SPECIFICITY: Skin specific.; larynx;oral cavity;hypopharynx;head and neck;skeletal muscle; dorsal root ganglion;superior cervical ganglion;trachea;tongue;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.11565 0.12738 -0.402212257 26.7338995 107.48158 2.25110 SERPINC1 0.993263587241958 0.00673530135356232 1.11140447976132e-06 serpin peptidase inhibitor, clade C (antithrombin), member 1 FUNCTION: Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin. {ECO:0000269|PubMed:15853774}.; DISEASE: Antithrombin III deficiency (AT3D) [MIM:613118]: An important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. Antithrombin-III deficiency is classified into 4 types. Type I: characterized by a 50% decrease in antigenic and functional levels. Type II: has defects affecting the thrombin-binding domain. Type III: alteration of the heparin-binding domain. Plasma AT-III antigen levels are normal in type II and III. Type IV: consists of miscellaneous group of unclassifiable mutations. {ECO:0000269|PubMed:10997988, ECO:0000269|PubMed:11713457, ECO:0000269|PubMed:11794707, ECO:0000269|PubMed:12353073, ECO:0000269|PubMed:12595305, ECO:0000269|PubMed:12894857, ECO:0000269|PubMed:15164384, ECO:0000269|PubMed:1547341, ECO:0000269|PubMed:1555650, ECO:0000269|PubMed:16908819, ECO:0000269|PubMed:1906811, ECO:0000269|PubMed:2229057, ECO:0000269|PubMed:2365065, ECO:0000269|PubMed:23910795, ECO:0000269|PubMed:2781509, ECO:0000269|PubMed:3080419, ECO:0000269|PubMed:3162733, ECO:0000269|PubMed:3179438, ECO:0000269|PubMed:3191114, ECO:0000269|PubMed:3805013, ECO:0000269|PubMed:6582486, ECO:0000269|PubMed:7734359, ECO:0000269|PubMed:7832187, ECO:0000269|PubMed:7878627, ECO:0000269|PubMed:7959685, ECO:0000269|PubMed:7981186, ECO:0000269|PubMed:7989582, ECO:0000269|PubMed:7994035, ECO:0000269|PubMed:8274732, ECO:0000269|PubMed:8443391, ECO:0000269|PubMed:8486379, ECO:0000269|PubMed:9031473, ECO:0000269|PubMed:9157604, ECO:0000269|PubMed:9759613, ECO:0000269|PubMed:9845533, ECO:0000269|Ref.3, ECO:0000269|Ref.55}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in plasma.; unclassifiable (Anatomical System);liver;spleen; superior cervical ganglion;fetal liver;liver;fetal lung;pons;skeletal muscle; 0.45194 0.56467 -0.047654689 50.22410946 54.14108 1.46750 SERPIND1 2.79554255070019e-05 0.538739940414859 0.461232104159634 serpin peptidase inhibitor, clade D (heparin cofactor), member 1 FUNCTION: Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT-III). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner. {ECO:0000269|PubMed:1939083}.; DISEASE: Thrombophilia due to heparin cofactor 2 deficiency (THPH10) [MIM:612356]: A hemostatic disorder characterized by a tendency to recurrent thrombosis. {ECO:0000269|PubMed:10391209, ECO:0000269|PubMed:11204559, ECO:0000269|PubMed:15337701, ECO:0000269|PubMed:2647747}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly in liver. Also present in plasma.; unclassifiable (Anatomical System);seminal vesicle;prostate;lung;whole body;liver;parathyroid;spleen;brain;skin;gall bladder;stomach; fetal liver;superior cervical ganglion;temporal lobe;liver;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.72393 0.26676 0.556689353 81.63481953 182.84551 2.93676 SERPINE1 0.219519976967254 0.77213078901791 0.00834923401483553 serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitor type 1), member 1 FUNCTION: Serine protease inhibitor. This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis. {ECO:0000269|PubMed:15853774}.; DISEASE: Plasminogen activator inhibitor-1 deficiency (PAI-1D) [MIM:613329]: A hematologic disorder characterized by increased bleeding after trauma, injury, or surgery. Affected females have menorrhagia. The bleeding defect is due to increased fibrinolysis of fibrin blood clots due to deficiency of plasminogen activator inhibitor-1, which inhibits tissue and urinary activators of plasminogen. {ECO:0000269|PubMed:9207454}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=High concentrations of SERPINE1 seem to contribute to the development of venous but not arterial occlusions.; TISSUE SPECIFICITY: Found in plasma and platelets and in endothelial, hepatoma and fibrosarcoma cells.; ovary;colon;vein;skin;uterus;larynx;bone;thyroid;testis;amniotic fluid;brain;gall bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;urinary;skeletal muscle;bile duct;pancreas;lung;epididymis;placenta;visual apparatus;liver;amnion;spleen;head and neck;cervix;stomach;aorta; adipose tissue;lung;smooth muscle;heart;placenta;fetal lung; 0.42306 0.86891 -0.268115223 34.70747818 478.10918 4.51469 SERPINE2 0.643023919378065 0.355641676920347 0.00133440370158827 serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitor type 1), member 2 FUNCTION: Serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin. Binds heparin.; . . lymphoreticular;ovary;foreskin;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;bladder;brain;heart;cartilage;pharynx;blood;lens;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; whole brain;amygdala;occipital lobe;smooth muscle;placenta;spinal cord;pons;parietal lobe;cerebellum; 0.26997 0.63944 -0.404032746 26.53338051 38.87264 1.15146 SERPINE3 0.00116717973839619 0.841582258663142 0.157250561598462 serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitor type 1), member 3 FUNCTION: Probable serine protease inhibitor. {ECO:0000250}.; . . . . . . 0.108486928 61.90728946 220.54536 3.21117 SERPINE4P . . . serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitor type 1), member 4 pseudogene . . . . . . . . . . . SERPINF1 8.28899615258178e-05 0.769260595225184 0.230656514813291 serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 1 FUNCTION: Neurotrophic protein; induces extensive neuronal differentiation in retinoblastoma cells. Potent inhibitor of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. {ECO:0000269|PubMed:7592790, ECO:0000269|PubMed:8226833}.; DISEASE: Osteogenesis imperfecta 6 (OI6) [MIM:613982]: A form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI6 is a severe, autosomal recessive form compatible with OI type III in the Sillence classification. {ECO:0000269|PubMed:21353196}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Retinal pigment epithelial cells and blood plasma. {ECO:0000269|PubMed:12737624}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;colon;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;synovium;bone;thyroid;iris;testis;ciliary body;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pineal body;muscle;blood;pancreas;lung;adrenal gland;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve;thymus; adipose tissue;liver;testis; 0.45778 . -0.596992387 18.18825195 199.0381 3.04911 SERPINF2 0.423433542043792 0.574981157039978 0.00158530091623056 serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2 FUNCTION: Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase-3/TMPRSS7 and chymotrypsin. {ECO:0000269|PubMed:15853774}.; DISEASE: Alpha-2-plasmin inhibitor deficiency (APLID) [MIM:262850]: An autosomal recessive disorder resulting in severe hemorrhagic diathesis. {ECO:0000269|PubMed:10583218, ECO:0000269|PubMed:2572590}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; unclassifiable (Anatomical System);colon;fovea centralis;choroid;lens;skeletal muscle;retina;pancreas;prostate;optic nerve;lung;macula lutea;liver;spleen;kidney;mammary gland;stomach;gall bladder; dorsal root ganglion;superior cervical ganglion;fetal liver;liver;ciliary ganglion;pons;kidney;atrioventricular node;trigeminal ganglion; 0.22228 0.53469 -0.775187015 13.05142722 4075.1537 12.66839 SERPING1 0.972837398501847 0.0271285078347259 3.40936634275837e-05 serpin peptidase inhibitor, clade G (C1 inhibitor), member 1 FUNCTION: Activation of the C1 complex is under control of the C1- inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein. {ECO:0000269|PubMed:8495195}.; DISEASE: Hereditary angioedema (HAE) [MIM:106100]: An autosomal dominant disorder characterized by episodic local swelling involving subcutaneous or submucous tissue of the upper respiratory and gastrointestinal tracts, face, extremities, and genitalia. Hereditary angioedema due to C1 esterase inhibitor deficiency is comprised of two clinically indistinguishable forms. In hereditary angioedema type 1, serum levels of C1 esterase inhibitor are decreased, while in type 2, the levels are normal or elevated, but the protein is non-functional. {ECO:0000269|PubMed:12773530, ECO:0000269|PubMed:1363816, ECO:0000269|PubMed:1451784, ECO:0000269|PubMed:14635117, ECO:0000269|PubMed:16409206, ECO:0000269|PubMed:2118657, ECO:0000269|PubMed:2296585, ECO:0000269|PubMed:22994404, ECO:0000269|PubMed:2365061, ECO:0000269|PubMed:24456027, ECO:0000269|PubMed:3178731, ECO:0000269|PubMed:7814636, ECO:0000269|PubMed:7883978, ECO:0000269|PubMed:8172583, ECO:0000269|PubMed:8529136, ECO:0000269|PubMed:8755917, ECO:0000269|Ref.41}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;iris;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;islets of Langerhans;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;liver;atrioventricular node; 0.10481 0.21468 -0.646543901 16.44255721 1555.3967 7.30820 SERPINH1 0.16655084953195 0.819116317442578 0.0143328330254725 serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1) FUNCTION: Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen.; DISEASE: Osteogenesis imperfecta 10 (OI10) [MIM:613848]: A form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI10 is an autosomal recessive form characterized by multiple bone deformities and fractures, generalized osteopenia, dentinogenesis imperfecta, and blue sclerae. {ECO:0000269|PubMed:20188343}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;salivary gland;colon;skin;retina;uterus;frontal lobe;cerebral cortex;larynx;bone;iris;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);trophoblast;heart;islets of Langerhans;muscle;urinary;pancreas;lung;mesenchyma;placenta;visual apparatus;hippocampus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; uterus;uterus corpus;adipose tissue;lung;smooth muscle;heart;placenta;fetal lung; 0.83973 0.39597 -0.602450568 17.91106393 54.13484 1.46719 SERPINH1P1 . . . serpin peptidase inhibitor, clade H1, pseudogene 1 . . . . . . . . . . . SERPINI1 0.930874238033153 0.0690542082358537 7.15537309934224e-05 serpin peptidase inhibitor, clade I (neuroserpin), member 1 FUNCTION: Serine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect neurons from cell damage by tissue-type plasminogen activator.; . TISSUE SPECIFICITY: Predominantly expressed in the brain.; ovary;colon;parathyroid;fovea centralis;skin;uterus;prostate;frontal lobe;thyroid;bone;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pineal body;adrenal cortex;skeletal muscle;breast;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;hippocampus;liver;kidney;stomach; amygdala;whole brain;occipital lobe;medulla oblongata;thalamus;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.65251 0.23170 1.150157577 92.46874263 796.93901 5.56525 SERPINI2 1.99904531615741e-10 0.0346071781075063 0.965392821692589 serpin peptidase inhibitor, clade I (pancpin), member 2 . . TISSUE SPECIFICITY: Expressed in pancreas and adipose tissues. {ECO:0000269|PubMed:9624529}.; unclassifiable (Anatomical System);pancreas;lung;endometrium;islets of Langerhans;liver;spleen; dorsal root ganglion;superior cervical ganglion;pancreas;ciliary ganglion;trigeminal ganglion; 0.07402 0.12086 0.218717575 68.27081859 4199.40981 12.87433 SERTAD1 0.0421844903041302 0.658650583198952 0.299164926496918 SERTA domain containing 1 FUNCTION: Acts at E2F-responsive promoters as coregulator to integrate signals provided by PHD- and/or bromodomain-containing transcription factors. Stimulates E2F1/TFDP1 transcriptional activity. Renders the activity of cyclin D1/CDK4 resistant to the inhibitory effects of CDKN2A/p16INK4A.; . . ovary;colon;skin;retina;bone marrow;uterus;prostate;endometrium;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; . 0.33949 0.11955 0.12689526 63.00424628 20.13556 0.68868 SERTAD2 0.736975237127184 0.251502290892314 0.0115224719805015 SERTA domain containing 2 FUNCTION: Acts at E2F-responsive promoters as coregulator to integrate signals provided by PHD- and/or bromodomain-containing transcription factors. May act as coactivator as well as corepressor of E2F1-TFDP1 and E2F4-TFDP1 complexes on E2F consensus binding sites, which would activate or inhibit E2F- target genes expression. Modulates fat storage by down-regulating the expression of key genes involved in adipocyte lipolysis, thermogenesis and oxidative metabolism. {ECO:0000269|PubMed:11331592}.; . TISSUE SPECIFICITY: Expressed in adipose tissue. {ECO:0000269|PubMed:23291629}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.79041 0.09606 -0.514264485 21.41424864 22.87026 0.76295 SERTAD3 0.0653917301176075 0.729873490836267 0.204734779046125 SERTA domain containing 3 FUNCTION: Strong transcriptional coactivator. {ECO:0000269|PubMed:10982866}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;pharynx;blood;lens;breast;lung;macula lutea;visual apparatus;liver;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion; 0.25447 0.14688 -0.317668748 31.45789101 9.84781 0.36052 SERTAD4 0.641278925379282 0.357365581971486 0.00135549264923204 SERTA domain containing 4 . . . . . 0.15119 0.08823 0.92967242 89.79122435 109.21905 2.26941 SERTAD4-AS1 . . . SERTAD4 antisense RNA 1 . . . . . 0.40743 . . . . . SERTM1 0.467667125905543 0.443960942561123 0.0883719315333343 serine rich and transmembrane domain containing 1 . . . unclassifiable (Anatomical System);lung;whole body;ovary;placenta;macula lutea;hippocampus;testis;parathyroid;fovea centralis;brain;retina; . . . 0.035072054 56.2514744 11.62368 0.42126 SESN1 0.000638247819798128 0.977314601080787 0.0220471510994145 sestrin 1 FUNCTION: Involved in the reduction of peroxiredoxins. May also be regulator of cellular growth. {ECO:0000269|PubMed:15105503}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12607115}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;urinary;adrenal cortex;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;alveolus;duodenum;liver;spleen;head and neck;kidney;stomach;aorta;peripheral nerve; superior cervical ganglion;prefrontal cortex;testis;atrioventricular node;skeletal muscle; 0.34167 0.13392 -0.844966979 11.1759849 684.84727 5.22390 SESN2 0.00076370931416015 0.981997661911777 0.0172386287740626 sestrin 2 FUNCTION: Involved in the reduction of peroxiredoxins. {ECO:0000269|PubMed:15105503}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12607115}.; myocardium;medulla oblongata;ovary;adrenal medulla;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;synovium;bone;iris;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach; liver; 0.61057 0.12065 -0.666770504 15.86459071 156.74305 2.73540 SESN3 0.994296082928102 0.00570376728964704 1.49782251461483e-07 sestrin 3 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12607115}.; unclassifiable (Anatomical System);breast;prostate;frontal lobe;ovary;heart;placenta;liver;parathyroid;bladder; . 0.34198 0.11130 -0.317668748 31.45789101 33.04464 1.02312 SESTD1 0.989112552502484 0.0108874414596034 6.03791211506074e-09 SEC14 and spectrin domain containing 1 FUNCTION: May act as the primary docking protein directing membrane turnover and assembly of the transient receptor potential channels TRPC4 and TRPC5. Binds phospholipids such as phosphatidylinositol monophosphates, phosphatidylinositol diphosphates (PIP2s) and phosphatidic acid, but not less polar lipids including phosphatidylcholine, phosphatidylserine, and phosphatidylinositol. The binding to PIP2s is calcium dependent. Might be involved in the plasma membrane localization of CTNNB1. {ECO:0000269|PubMed:20164195}.; . TISSUE SPECIFICITY: Broad expression. High expression in thalamus and brain. Significantly expressed in vasculature. {ECO:0000269|PubMed:20164195}.; ovary;colon;skin;retina;uterus;prostate;whole body;cochlea;endometrium;bone;testis;artery;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;muscle;breast;lung;trabecular meshwork;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;aorta; dorsal root ganglion;superior cervical ganglion;medulla oblongata;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.29030 0.11176 -0.468351206 23.42533616 68.01256 1.70553 SET 0.963364279903668 0.0365641828939204 7.15372024114534e-05 SET nuclear proto-oncogene FUNCTION: Multitasking protein, involved in apoptosis, transcription, nucleosome assembly and histone chaperoning. Isoform 2 anti-apoptotic activity is mediated by inhibition of the GZMA-activated DNase, NME1. In the course of cytotoxic T- lymphocyte (CTL)-induced apoptosis, GZMA cleaves SET, disrupting its binding to NME1 and releasing NME1 inhibition. Isoform 1 and isoform 2 are potent inhibitors of protein phosphatase 2A. Isoform 1 and isoform 2 inhibit EP300/CREBBP and PCAF-mediated acetylation of histones (HAT) and nucleosomes, most probably by masking the accessibility of lysines of histones to the acetylases. The predominant target for inhibition is histone H4. HAT inhibition leads to silencing of HAT-dependent transcription and prevents active demethylation of DNA. Both isoforms stimulate DNA replication of the adenovirus genome complexed with viral core proteins; however, isoform 2 specific activity is higher. {ECO:0000269|PubMed:11555662, ECO:0000269|PubMed:12628186}.; DISEASE: Note=A chromosomal aberration involving SET is found in some cases of acute undifferentiated leukemia (AUL). Translocation t(6;9)(q21;q34.1) with NUP214/CAN.; TISSUE SPECIFICITY: Widely expressed. Low levels in quiescent cells during serum starvation, contact inhibition or differentiation. Highly expressed in Wilms' tumor.; ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;thyroid;pituitary gland;brain;unclassifiable (Anatomical System);small intestine;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;lung;cornea;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; amygdala;subthalamic nucleus;occipital lobe;fetal brain;tumor;white blood cells;parietal lobe; 0.60962 0.29577 0.3032669 72.009908 21.10998 0.71452 SETBP1 0.999002929381036 0.00099707018881189 4.30152142314033e-10 SET binding protein 1 . DISEASE: Note=SETBP1 somatic mutations are frequently found in myeloid malignancies. They cause gain of function associated with myeloid leukemic transformation (PubMed:23832012). Myeloid malignancies are separated into three main categories: myeloproliferative neoplasms (MPN) characterized by cellular proliferation of one or more hematologic cell lines in the peripheral blood, myelodysplastic syndromes (MDS) and MDS/MPN. The MDS/MPN category shows overlapping characteristics of both MDS and MPN and includes chronic myelomonocytic leukemia (CMML), juvenile myelomonocytic leukemia, atypical chronic myeloid leukemia (ACML) and unclassified MDS/MPN (PubMed:23628959). {ECO:0000269|PubMed:23628959, ECO:0000269|PubMed:23832012}.; DISEASE: Myelodysplastic syndrome (MDS) [MIM:614286]: A heterogeneous group of closely related clonal hematopoietic disorders. All are characterized by a hypercellular or hypocellular bone marrow with impaired morphology and maturation, dysplasia of the myeloid, megakaryocytic and/or erythroid lineages, and peripheral blood cytopenias resulting from ineffective blood cell production. Included diseases are: refractory anemia (RA), refractory anemia with ringed sideroblasts (RARS), refractory anemia with excess blasts (RAEB), refractory cytopenia with multilineage dysplasia and ringed sideroblasts (RCMD-RS); chronic myelomonocytic leukemia (CMML) is a myelodysplastic/myeloproliferative disease. MDS is considered a premalignant condition in a subgroup of patients that often progresses to acute myeloid leukemia (AML). {ECO:0000269|PubMed:23648668, ECO:0000269|PubMed:23889083}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Mental retardation, autosomal dominant 29 (MRD29) [MIM:616078]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD29 patients manifest severe intellectual disability, behavioral difficulties, speech and motor delays, and dysmorphic facial features. {ECO:0000269|PubMed:25217958}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. {ECO:0000269|PubMed:23648668, ECO:0000269|PubMed:23889083}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Leukemia, chronic myeloid, atypical (ACML) [MIM:608232]: A myeloproliferative disorder that shares clinical and laboratory features with chronic myeloid leukemia but lacks the pathognomonic Philadelphia chromosome and the corresponding BCR/ABL1 fusion transcript. Features include myeloid predominance in the bone marrow, myeloid proliferation and low leukocyte alkaline phosphatase value, splenomegaly, hepatomegaly, elevated white blood cell count. Enlarged spleen may also be associated with a hypermetabolic state, fever, weight loss, and chronic fatigue. The enlarged liver may contribute to the patient's weight loss. {ECO:0000269|PubMed:23222956}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages. {ECO:0000269|PubMed:23832011}. Note=The gene represented in this entry is involved in disease pathogenesis.; TISSUE SPECIFICITY: Expressed in numerous tissues. Expressed at low levels in myeloid and monocytic cells as well as in CD34+ cells; expression levels are higher in myeloid malignancies. {ECO:0000269|PubMed:11231286, ECO:0000269|PubMed:23832012}.; unclassifiable (Anatomical System);ovary;colon;blood;prostate;lung;frontal lobe;cochlea;cerebral cortex;larynx;placenta;visual apparatus;hippocampus;testis;head and neck;spleen;germinal center;brain;stomach; . 0.75510 0.29962 -1.118903529 6.611229063 3394.47384 11.15813 SETD1A 0.999996231355084 3.76864491541725e-06 5.39645114823542e-16 SET domain containing 1A FUNCTION: Histone methyltransferase that specifically methylates 'Lys-4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys- 9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overalpping localization with SETD1B suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. {ECO:0000269|PubMed:12670868}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node; 0.31946 . -2.934884757 0.560273649 360.97151 4.02191 SETD1B 0.0224563158915498 0.533936805683567 0.443606878424883 SET domain containing 1B FUNCTION: Histone methyltransferase that specifically methylates 'Lys-4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys- 9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overalpping localization with SETD1A suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. Specifically tri-methylates 'Lys-4' of histone H3 in vitro.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pineal body;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;spleen;kidney;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.22155 0.10620 0.202129237 67.42745931 326.28837 3.84021 SETD2 0.999992944074178 7.0559258216066e-06 6.98690040764261e-21 SET domain containing 2 FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate. Represents the main enzyme generating H3K36me3, a specific tag for epigenetic transcriptional activation. Plays a role in chromatin structure modulation during elongation by coordinating recruitment of the FACT complex and by interacting with hyperphosphorylated POLR2A. Acts as a key regulator of DNA mismatch repair in G1 and early S phase by generating H3K36me3, a mark required to recruit MSH6 subunit of the MutS alpha complex: early recruitment of the MutS alpha complex to chromatin to be replicated allows a quick identification of mismatch DNA to initiate the mismatch repair reaction. H3K36me3 also plays an essential role in the maintenance of a heterochromatic state, by recruiting DNA methyltransferase DNMT3A. H3K36me3 is also enhanced in intron-containing genes, suggesting that SETD2 recruitment is enhanced by splicing and that splicing is coupled to recruitment of elongating RNA polymerase. Required during angiogenesis. Recruited to the promoters of adenovirus 12 E1A gene in case of infection, possibly leading to regulate its expression. {ECO:0000269|PubMed:16118227, ECO:0000269|PubMed:19141475, ECO:0000269|PubMed:21526191, ECO:0000269|PubMed:21792193, ECO:0000269|PubMed:23043551, ECO:0000269|PubMed:23325844, ECO:0000269|PubMed:23622243}.; DISEASE: Renal cell carcinoma (RCC) [MIM:144700]: Renal cell carcinoma is a heterogeneous group of sporadic or hereditary carcinoma derived from cells of the proximal renal tubular epithelium. It is subclassified into clear cell renal carcinoma (non-papillary carcinoma), papillary renal cell carcinoma, chromophobe renal cell carcinoma, collecting duct carcinoma with medullary carcinoma of the kidney, and unclassified renal cell carcinoma. Clear cell renal cell carcinoma is the most common subtype. {ECO:0000269|PubMed:20054297, ECO:0000269|PubMed:23622243, ECO:0000269|PubMed:23792563}. Note=The disease may be caused by mutations affecting the gene represented in this entry. Defects of SETD2 are associated with loss of DNA methylation at non-promoter regions (PubMed:23792563). {ECO:0000269|PubMed:23792563}.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11461154}.; ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;stomach;peripheral nerve;cerebellum;thymus; dorsal root ganglion;superior cervical ganglion;testis;trigeminal ganglion;parietal lobe;skeletal muscle; 0.50275 0.38957 -0.93708102 9.424392545 5284.19613 15.02449 SETD3 0.371891002606027 0.628089373725271 1.96236687021455e-05 SET domain containing 3 FUNCTION: Histone methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3 (H3K4me and H3K36me). Acts as a transcriptional activator. Plays an important role in the transcriptional regulation of muscle cell differentiation via interaction with MYOD1. {ECO:0000250|UniProtKB:Q91WC0}.; . . medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pineal body;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; testis - interstitial;medulla oblongata;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.29413 0.10715 -0.933156985 9.54824251 37.78471 1.12376 SETD4 2.5473165547071e-12 0.0364296628590639 0.963570337138389 SET domain containing 4 . . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;stomach; superior cervical ganglion;testis - interstitial;testis;kidney;pons;trigeminal ganglion;skeletal muscle; 0.13356 0.09963 -0.179930907 40.35739561 195.14433 3.02855 SETD5 0.999999563778174 4.36221826397394e-07 2.82492183592089e-18 SET domain containing 5 . DISEASE: Mental retardation, autosomal dominant 23 (MRD23) [MIM:615761]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD23 patients manifest moderate to severe intellectual disability with additional variable features of brachycephaly, a low hairline, depressed nasal bridge, prominent high nasal root, tubular nose, upslanting palpebral fissures, long and smooth philtrum, micrognathia, thin upper lip, and crowded teeth. Behavioral problems, including obsessive-compulsive disorder, hand flapping with ritualized behavior, and autism, are prominent features. {ECO:0000269|PubMed:24680889}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;muscle;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; testis - interstitial;testis - seminiferous tubule;adrenal cortex;prefrontal cortex;testis; 0.46735 0.10674 -0.791786324 12.59731069 500.45582 4.59199 SETD6 1.02142648154529e-09 0.0884112475359779 0.911588751442596 SET domain containing 6 FUNCTION: Protein-lysine N-methyltransferase. Monomethylates 'Lys- 310' of the RELA subunit of NF-kappa-B complex, leading to down- regulate NF-kappa-B transcription factor activity (PubMed:21131967). Monomethylates 'Lys-8' of H2AZ (H2AZK8me1) (PubMed:23324626). Required for the maintenance of embryonic stem cell self-renewal (By similarity). {ECO:0000250|UniProtKB:Q9CWY3, ECO:0000269|PubMed:21131967, ECO:0000269|PubMed:23324626}.; . . lymphoreticular;choroid;fovea centralis;skin;retina;prostate;optic nerve;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;lens;pancreas;lung;nasopharynx;macula lutea;liver;spleen;kidney;stomach;aorta; superior cervical ganglion;pons; 0.37690 . 0.132352165 63.48785091 65.5989 1.66820 SETD6P1 . . . SET domain containing 6 pseudogene 1 . . . . . . . . . . . SETD7 0.293260030580492 0.702366052238805 0.00437391718070303 SET domain containing lysine methyltransferase 7 FUNCTION: Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation. {ECO:0000269|PubMed:12540855, ECO:0000269|PubMed:12588998, ECO:0000269|PubMed:15099517, ECO:0000269|PubMed:15525938, ECO:0000269|PubMed:16141209, ECO:0000269|PubMed:17108971}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in pancreatic islets.; ovary;skin;bone marrow;retina;prostate;cochlea;endometrium;gum;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus;cerebellum; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.57760 0.15588 0.084621747 60.31493277 22.99717 0.76719 SETD8P1 . . . SET domain containing 8 pseudogene 1 . . . . . . . . . . . SETD9 0.000533497554716758 0.887897099373124 0.111569403072159 SET domain containing 9 . . . . . 0.23141 . -0.115612493 45.12856806 4792.86156 14.04270 SETDB1 0.999996683969478 3.31603052145588e-06 7.99554930965384e-17 SET domain bifurcated 1 FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins. {ECO:0000269|PubMed:12869583, ECO:0000269|PubMed:14536086, ECO:0000269|PubMed:15327775, ECO:0000269|PubMed:17952062}.; . TISSUE SPECIFICITY: Widely expressed. High expression in testis.; lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;skin;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;alveolus;liver;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13447 . -1.460519861 3.809860816 354.06408 3.98173 SETDB2 0.0437301091973815 0.956221541652222 4.83491503967077e-05 SET domain bifurcated 2 FUNCTION: Histone methyltransferase involved in left-right axis specification in early development and mitosis. Specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). H3K9me3 is a specific tag for epigenetic transcriptional repression that recruits HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Contributes to H3K9me3 in both the interspersed repetitive elements and centromere-associated repeats. Plays a role in chromosome condensation and segregation during mitosis. {ECO:0000269|PubMed:20404330}.; . TISSUE SPECIFICITY: Ubiquitous. Highest expression in heart, testis and ovary.; unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;colon;skin;skeletal muscle;breast;uterus;prostate;whole body;lung;endometrium;adrenal gland;placenta;liver;testis;germinal center; . 0.07671 0.09226 -0.067881249 48.69072895 152.91231 2.70466 SETMAR 0.00213127902514751 0.916365138807877 0.0815035821669753 SET domain and mariner transposase fusion gene FUNCTION: Protein derived from the fusion of a methylase with the transposase of an Hsmar1 transposon that plays a role in DNA double-strand break repair, stalled replication fork restart and DNA integration. DNA-binding protein, it is indirectly recruited to sites of DNA damage through protein-protein interactions. Has also kept a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity (PubMed:16332963, PubMed:16672366, PubMed:17877369, PubMed:17403897, PubMed:18263876, PubMed:22231448, PubMed:24573677, PubMed:20521842). In parallel, has a histone methyltransferase activity and methylates 'Lys-4' and 'Lys-36' of histone H3. Specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining (PubMed:16332963, PubMed:21187428, PubMed:22231448). Also regulates replication fork processing, promoting replication fork restart and regulating DNA decatenation through stimulation of the topoisomerase activity of TOP2A (PubMed:18790802, PubMed:20457750). {ECO:0000269|PubMed:16332963, ECO:0000269|PubMed:16672366, ECO:0000269|PubMed:17403897, ECO:0000269|PubMed:17877369, ECO:0000269|PubMed:18790802, ECO:0000269|PubMed:20457750, ECO:0000269|PubMed:20521842, ECO:0000269|PubMed:21187428, ECO:0000269|PubMed:22231448, ECO:0000269|PubMed:24573677, ECO:0000303|PubMed:18263876}.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in placenta and ovary and lowest expression in skeletal muscle. {ECO:0000269|PubMed:16332963}.; . . 0.07436 0.09300 0.308721233 72.59966973 1076.85119 6.28944 SETP1 . . . SET pseudogene 1 . . . . . . . . . . . SETP2 . . . SET pseudogene 2 . . . . . . . . . . . SETP3 . . . SET pseudogene 3 . . . . . . . . . . . SETP4 . . . SET pseudogene 4 . . . . . . . . . . . SETP5 . . . SET pseudogene 5 . . . . . . . . . . . SETP6 . . . SET pseudogene 6 . . . . . . . . . . . SETP7 . . . SET pseudogene 7 . . . . . . . . . . . SETP8 . . . SET pseudogene 8 . . . . . . . . . . . SETP9 . . . SET pseudogene 9 . . . . . . . . . . . SETP10 . . . SET pseudogene 10 . . . . . . . . . . . SETP11 . . . SET pseudogene 11 . . . . . . . . . . . SETP12 . . . SET pseudogene 12 . . . . . . . . . . . SETP14 . . . SET pseudogene 14 . . . . . . . . . . . SETP15 . . . SET pseudogene 15 . . . . . . . . . . . SETP16 . . . SET pseudogene 16 . . . . . . . . . . . SETP17 . . . SET pseudogene 17 . . . . . . . . . . . SETP20 . . . SET pseudogene 20 . . . . . . . . . . . SETP21 . . . SET pseudogene 21 . . . . . . . . . . . SETP22 . . . SET pseudogene 22 . . . . . . . . . . . SETSIP . . . SET-like protein FUNCTION: Plays a role as a transcriptional activator involved in the early stage of somatic cell reprogramming. Promotes the differentiation of protein-induced pluripotent stem (PiPS) cells into endothelial cells and the formation of vascular-like tubes (in vitro). Involved in the transcription induction of vascular endothelial-cadherin (VE-cadherin) expression. Associates to the VE-cadherin gene promoter. {ECO:0000269|PubMed:22869753}.; . TISSUE SPECIFICITY: Expressed in endothelial cell (EC) and protein-induced pluripotent stem (PiPS) endothelial cell (EC) (at protein level). {ECO:0000269|PubMed:22869753}.; . . . . . . . . SETX 0.200249583810895 0.799750416187103 2.00169354283551e-12 senataxin FUNCTION: Probable RNA/DNA helicase involved in diverse aspects of RNA metabolism and genomic integrity. Plays a role in transcription regulation by its ability to modulate RNA Polymerase II (Pol II) binding to chromatin and through its interaction with proteins involved in transcription (PubMed:19515850, PubMed:21700224). Contributes to the mRNA splicing efficiency and splice site selection (PubMed:19515850). Required for the resolution of R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site, allowing XRN2 recruitment and XRN2-mediated degradation of the downstream cleaved RNA and hence efficient RNA polymerase II (RNAp II) transcription termination (PubMed:19515850, PubMed:21700224). Required for the 3' transcriptional termination of PER1 and CRY2, thus playing an important role in the circadian rhythm regulation (By similarity). Involved in DNA double-strand breaks damage response generated by oxidative stress (PubMed:17562789). In association with RRP45, targets the RNA exosome complex to sites of transcription-induced DNA damage (PubMed:24105744). Plays a role in the development and maturation of germ cells: essential for male meiosis, acting at the interface of transcription and meiotic recombination, and in the process of gene silencing during meiotic sex chromosome inactivation (MSCI) (By similarity). May be involved in telomeric stability through the regulation of telomere repeat-containing RNA (TERRA) transcription (PubMed:21112256). Plays a role in neurite outgrowth in hippocampal cells through FGF8-activated signaling pathways. Inhibits retinoic acid-induced apoptosis (PubMed:21576111). {ECO:0000250|UniProtKB:A2AKX3, ECO:0000269|PubMed:17562789, ECO:0000269|PubMed:19515850, ECO:0000269|PubMed:21112256, ECO:0000269|PubMed:21576111, ECO:0000269|PubMed:21700224, ECO:0000269|PubMed:24105744}.; DISEASE: Spinocerebellar ataxia, autosomal recessive, 1 (SCAR1) [MIM:606002]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR1 is an autosomal recessive form associated with peripheral neuropathy and elevated serum alpha- fetoprotein, immunoglobulins and, less commonly, creatine kinase levels. Some SCAR1 patients manifest oculomotor apraxia. {ECO:0000269|PubMed:14770181, ECO:0000269|PubMed:16644229, ECO:0000269|PubMed:16717225, ECO:0000269|PubMed:17096168, ECO:0000269|PubMed:23566282, ECO:0000269|PubMed:23786967, ECO:0000269|PubMed:23941260, ECO:0000269|PubMed:24105744}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Amyotrophic lateral sclerosis 4 (ALS4) [MIM:602433]: A form of amyotrophic lateral sclerosis with childhood- or adolescent-onset, and characterized by slow disease progression and the sparing of bulbar and respiratory muscles. Amyotrophic lateral sclerosis is a neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. {ECO:0000269|PubMed:14770181, ECO:0000269|PubMed:15106121, ECO:0000269|PubMed:21190393, ECO:0000269|PubMed:24105744, ECO:0000269|PubMed:24244371}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Expressed in heart, fibroblast, placenta and liver. Weakly expressed in brain and lung. Expressed in the cortex of the kidney (highly expressed in tubular epithelial cells but low expression in the glomerulus). {ECO:0000269|PubMed:14770181, ECO:0000269|PubMed:15106121, ECO:0000269|PubMed:16644229, ECO:0000269|PubMed:17562789}.; lymphoreticular;ovary;colon;substantia nigra;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;small intestine;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion; 0.07422 0.41280 -0.13995117 42.88157584 1619.58256 7.44289 SEZ6 1.39340908360683e-05 0.998076956435264 0.00190910947389983 seizure related 6 homolog (mouse) FUNCTION: May play a role in cell-cell recognition and in neuronal membrane signaling. Seems to be important for the achievement of the necessary balance between dendrite elongation and branching during the elaboration of a complex dendritic arbor. Involved in the development of appropriate excitatory synaptic connectivity (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;lung;frontal lobe;placenta;thyroid;macula lutea;visual apparatus;head and neck;brain;cerebellum; dorsal root ganglion;superior cervical ganglion;fetal liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.36852 0.09030 1.249272484 93.46543996 4855.90823 14.16843 SEZ6L 0.928831047449245 0.07116882304884 1.2950191546436e-07 seizure related 6 homolog (mouse)-like FUNCTION: May contribute to specialized endoplasmic reticulum functions in neurons. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed, including adult and fetal brains and lungs. Not expressed in all lung cancer cell lines.; unclassifiable (Anatomical System);amygdala;islets of Langerhans;sympathetic chain;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;frontal lobe;macula lutea;hippocampus;testis;kidney;mammary gland;brain;aorta; amygdala;superior cervical ganglion;subthalamic nucleus;thalamus;fetal brain;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe;cerebellum; 0.30074 0.11342 -2.032105599 1.686718566 1299.61065 6.78117 SEZ6L2 0.130153160381108 0.869807213328335 3.96262905569382e-05 seizure related 6 homolog (mouse)-like 2 FUNCTION: May contribute to specialized endoplasmic reticulum functions in neurons. {ECO:0000250}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;bone;pituitary gland;testis;brain;pineal gland;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;pineal body;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; whole brain;amygdala;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;pituitary;cerebellum; 0.53499 0.10324 -1.124330456 6.575843359 637.27687 5.07921 SF1 0.998855016951352 0.00114496833072414 1.47179235116173e-08 splicing factor 1 FUNCTION: Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor. {ECO:0000269|PubMed:10449420, ECO:0000269|PubMed:8752089, ECO:0000269|PubMed:9660765}.; . TISSUE SPECIFICITY: Detected in lung, ovary, adrenal gland, colon, kidney, muscle, pancreas, thyroid, placenta, brain, liver and heart. {ECO:0000269|PubMed:7912130}.; lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;duodenum;kidney;stomach;aorta;thymus;cerebellum; dorsal root ganglion;amygdala;superior cervical ganglion;thyroid;testis;ciliary ganglion;trigeminal ganglion;cerebellum; 0.35435 0.08669 -0.868835007 10.65109696 20.81543 0.70537 SF3A1 0.994075395519488 0.00592459775128123 6.72923105452177e-09 splicing factor 3a subunit 1 FUNCTION: Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex.; . TISSUE SPECIFICITY: Ubiquitously expressed.; medulla oblongata;smooth muscle;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;duodenum;liver;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;cerebellum; 0.75785 0.12150 -0.780646273 12.77423921 60.44517 1.58073 SF3A2 0.774375362030151 0.223987066972354 0.0016375709974959 splicing factor 3a subunit 2 FUNCTION: Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex.; . . ovary;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;breast;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;placenta;testis;ciliary ganglion;trigeminal ganglion; 0.22891 0.13749 . . 41.27603 1.20652 SF3A3 0.999895351853046 0.000104648138197462 8.75611741232936e-12 splicing factor 3a subunit 3 FUNCTION: Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.35351 0.08994 -0.427900189 25.14744043 6.01727 0.22700 SF3A3P1 . . . splicing factor 3a, subunit 3 pseudogene 1 . . . . . . . . . . . SF3A3P2 . . . splicing factor 3a, subunit 3 pseudogene 2 . . . . . . . . . . . SF3B1 0.999999972774106 2.72258942237541e-08 1.62334318734556e-20 splicing factor 3b subunit 1 FUNCTION: Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron.; . . smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;lymph node;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.99595 0.23021 -1.133409319 6.434300543 10.78251 0.39127 SF3B2 0.999459845161211 0.000540154834834155 3.95442868271811e-12 splicing factor 3b subunit 2 FUNCTION: Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron.; . . lymphoreticular;ovary;umbilical cord;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;iris;amniotic fluid;germinal center;bladder;brain;tonsil;heart;urinary;spinal cord;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach; thalamus;testis - interstitial;testis - seminiferous tubule;placenta;testis;white blood cells; 0.14360 0.17713 -1.087493118 7.106628922 282.07854 3.59663 SF3B3 0.999962978336449 3.70216635494894e-05 1.1678970766182e-15 splicing factor 3b subunit 3 FUNCTION: Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron.; . . lymphoreticular;smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hypopharynx;duodenum;head and neck;kidney;stomach; fetal liver;superior cervical ganglion;temporal lobe;atrioventricular node;trigeminal ganglion;cingulate cortex;cerebellum; 0.62975 0.20297 -1.019530098 8.038452465 3037.56808 10.46553 SF3B4 0.918007232108898 0.0818822171343416 0.000110550756760738 splicing factor 3b subunit 4 FUNCTION: Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. SF3B4 has been found in complex 'B' and 'C' as well. Belongs also to the minor U12- dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron.; DISEASE: Acrofacial dysostosis 1, Nager type (AFD1) [MIM:154400]: A form of acrofacial dysostosis, a group of disorders which are characterized by malformation of the craniofacial skeleton and the limbs. The major facial features of AFD1 include downslanted palpebral fissures, midface retrusion, and micrognathia, the latter of which often requires the placement of a tracheostomy in early childhood. Limb defects typically involve the anterior (radial) elements of the upper limbs and manifest as small or absent thumbs, triphalangeal thumbs, radial hyoplasia or aplasia, and radioulnar synostosis. Phocomelia of the upper limbs and, occasionally, lower-limb defects have also been reported. {ECO:0000269|PubMed:22541558}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis; 0.23270 0.11262 -0.295622497 32.61972163 2.39611 0.08182 SF3B4P1 . . . splicing factor 3b, subunit 4 pseudogene 1 . . . . . . . . . . . SF3B5 0.600475506656737 0.361984438272733 0.0375400550705298 splicing factor 3b subunit 5 . . . . . 0.16826 0.11262 0.101211609 60.95777306 1.17647 0.03299 SF3B6 . . . splicing factor 3b subunit 6 FUNCTION: Necessary for the splicing of pre-mRNA. Directly contacts the pre-mRNA branch site adenosine for the first catalytic step of splicing. Enters the spliceosome and associates with the pre-mRNA branch site as part of the 17S U2 or, in the case of the minor spliceosome, as part of the 18S U11/U12 snRNP complex, and thus may facilitate the interaction of these snRNP with the branch sites of U2 and U12 respectively. {ECO:0000269|PubMed:16432215}.; . . . . . . . . . . SFI1 5.98724844744369e-25 0.219326979284339 0.780673020715661 SFI1 centrin binding protein FUNCTION: Plays a role in the dynamic structure of centrosome- associated contractile fibers via its interaction with CETN2. {ECO:0000269|PubMed:16956364}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;thymus; . 0.19999 0.09106 0.595153166 82.52535975 7567.61517 18.66443 SFMBT1 0.99589420844432 0.00410579099979879 5.55880986550487e-10 Scm-like with four mbt domains 1 FUNCTION: Histone-binding protein, which is part of various corepressor complexes. Mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. Plays a role during myogenesis: required for the maintenance of undifferentiated states of myogenic progenitor cells via interaction with MYOD1. Interaction with MYOD1 leads to the recruitment of associated corepressors and silencing of MYOD1 target genes. Part of the SLC complex in germ cells, where it may play a role during spermatogenesis. {ECO:0000269|PubMed:17599839, ECO:0000269|PubMed:23349461, ECO:0000269|PubMed:23592795}.; . TISSUE SPECIFICITY: Expressed in all cell lines and normal tissues tested, including the thymus. {ECO:0000269|PubMed:10661410}.; ovary;colon;parathyroid;skin;retina;uterus;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;lens;bile duct;breast;lung;nasopharynx;placenta;visual apparatus;liver;amnion;spleen;head and neck;cervix;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.80360 0.11437 -0.642904474 16.62538335 169.45987 2.84046 SFMBT2 0.996407769866383 0.00359223005244756 8.11696986356557e-11 Scm-like with four mbt domains 2 FUNCTION: Transcriptional repressor of HOXB13 gene. {ECO:0000269|PubMed:23385818}.; . . unclassifiable (Anatomical System);breast;liver;spleen;mammary gland; dorsal root ganglion;ciliary ganglion;atrioventricular node; 0.11952 0.11741 -0.615405356 17.47464025 675.97175 5.19443 SFN 0.490890062387915 0.488098730163916 0.0210112074481694 stratifin FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53. {ECO:0000269|PubMed:18382127}.; . TISSUE SPECIFICITY: Present mainly in tissues enriched in stratified squamous keratinizing epithelium.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;optic nerve;endometrium;oesophagus;larynx;gum;bone;thyroid;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;pharynx;blood;lens;breast;greater omentum;pancreas;lung;epididymis;placenta;visual apparatus;hypopharynx;liver;cervix;head and neck;kidney;stomach; superior cervical ganglion;prostate;lung;trachea;tongue;tonsil;skin; 0.59871 0.34719 -0.229483771 36.86010852 10.20993 0.37236 SFPQ 0.999527260233545 0.000472739421516008 3.44938690935979e-10 splicing factor proline/glutamine-rich FUNCTION: DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation. {ECO:0000269|PubMed:10847580, ECO:0000269|PubMed:10858305, ECO:0000269|PubMed:10931916, ECO:0000269|PubMed:11259580, ECO:0000269|PubMed:11525732, ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:15590677, ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:8045264, ECO:0000269|PubMed:8449401}.; DISEASE: Note=A chromosomal aberration involving SFPQ may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X;1)(p11.2;p34) with TFE3.; . ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;larynx;testis;artery;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta; superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;placenta;prefrontal cortex;globus pallidus;pons;cingulate cortex; 0.92237 0.11252 . . 50.11453 1.39006 SFPQP1 . . . splicing factor proline/glutamine-rich pseudogene 1 . . . . . . . . . . . SFR1 0.000222754704198165 0.506780782064184 0.492996463231618 SWI5 dependent homologous recombination repair protein 1 FUNCTION: Component of the SWI5-SFR1 complex, a complex required for double-strand break repair via homologous recombination (PubMed:21252223). Acts as a transcriptional modulator for ESR1 (PubMed:23874500). {ECO:0000269|PubMed:21252223, ECO:0000269|PubMed:23874500}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:21252223}.; unclassifiable (Anatomical System);medulla oblongata;cartilage;fovea centralis;choroid;lens;skin;retina;bone marrow;pancreas;prostate;optic nerve;lung;epididymis;nasopharynx;bone;macula lutea;hippocampus;liver;testis;spleen;germinal center;brain;stomach; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09030 0.09372 -0.117432389 44.89266336 1205.57949 6.57654 SFR1P1 . . . SFR1 pseudogene 1 . . . . . . . . . . . SFR1P2 . . . SFR1 pseudogene 2 . . . . . . . . . . . SFRP1 0.465845741756302 0.509059390388014 0.0250948678556839 secreted frizzled-related protein 1 FUNCTION: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP1 decreases intracellular beta-catenin levels (By similarity). Has antiproliferative effects on vascular cells, in vitro and in vivo, and can induce, in vivo, an angiogenic response. In vascular cell cycle, delays the G1 phase and entry into the S phase (By similarity). In kidney development, inhibits tubule formation and bud growth in metanephroi (By similarity). Inhibits WNT1/WNT4-mediated TCF-dependent transcription. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Absent from lung, liver and peripheral blood leukocytes. Highest levels in heart and fetal kidney. Also expressed in testis, ovary, fetal brain and lung, leiomyomal cells, myometrial cells and vascular smooth muscle cells. Expressed in foreskin fibroblasts and in keratinocytes. {ECO:0000269|PubMed:9391078}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;synovium;bone;testis;amniotic fluid;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;lens;skeletal muscle;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;hippocampus;liver;hypopharynx;amnion;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve;cerebellum; uterus;superior cervical ganglion;tongue;testis;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.87202 0.42207 -0.471992905 23.03609342 3273.82594 10.92118 SFRP2 0.0538845191822357 0.863690045450787 0.0824254353669777 secreted frizzled-related protein 2 FUNCTION: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP2 may be important for eye retinal development and for myogenesis.; . TISSUE SPECIFICITY: Expressed in adipose tissue, heart, brain, skeletal muscle, pancreas, thymus, prostate, testis, ovary, small intestine and colon. Highest levels in adipose tissue, small intestine and colon. {ECO:0000269|PubMed:9391078, ECO:0000269|PubMed:9642118}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;iris;testis;dura mater;spinal ganglion;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;urinary;lens;skeletal muscle;breast;pancreas;pia mater;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;olfactory bulb;trachea;tongue;thyroid;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.88914 0.35008 -0.139478553 43.29440906 1051.74266 6.22845 SFRP4 4.45782556410063e-05 0.640387454834675 0.359567966909684 secreted frizzled-related protein 4 FUNCTION: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP4 may act as a regulator of adult uterine morphology and function. Increases apoptosis during ovulation possibly through modulation of FZ1/FZ4/WNT4 signaling (By similarity). Has phosphaturic effects by specifically inhibiting sodium-dependent phosphate uptake. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in mesenchymal cells. Highly expressed in the stroma of proliferative endometrium. Expressed in cardiomyocytes. Shows moderate to strong expression in ovarian tumors with expression increasing as the tumor stage increases. In ovarian tumors, expression levels are inversely correlated with expression of CTNNB1 (at protein level). {ECO:0000269|PubMed:10728394, ECO:0000269|PubMed:19480240}.; . . 0.18761 0.25404 -0.247889024 35.98726115 624.7779 5.04218 SFRP5 1.17131762074183e-05 0.208927101849133 0.791061184974659 secreted frizzled-related protein 5 FUNCTION: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP5 may be involved in determining the polarity of photoreceptor, and perhaps, other cells in the retina.; . TISSUE SPECIFICITY: Highly expressed in the retinal pigment epithelium (RPE) and pancreas. Weak expression in heart, liver and muscle. {ECO:0000269|PubMed:10072424, ECO:0000269|PubMed:9391078, ECO:0000269|PubMed:9642118}.; optic nerve;islets of Langerhans;sympathetic chain;macula lutea;iris;fovea centralis;choroid;lens;retina; dorsal root ganglion;testis - interstitial;superior cervical ganglion;olfactory bulb;spinal cord;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.41154 0.19215 0.128714042 63.19886766 119.23207 2.37670 SFSWAP 0.999425434016638 0.000574565871094658 1.12267827347043e-10 splicing factor, suppressor of white-apricot homolog FUNCTION: Plays a role as an alternative splicing regulator. Regulate its own expression at the level of RNA processing. Also regulates the splicing of fibronectin and CD45 genes. May act, at least in part, by interaction with other R/S-containing splicing factors. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269|PubMed:8940107}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;subthalamic nucleus;medulla oblongata;testis - seminiferous tubule;prefrontal cortex;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;parietal lobe;cingulate cortex; 0.19131 0.10508 -0.964552806 8.999764095 214.00747 3.15663 SFT2D1 0.350193452291255 0.636618812697457 0.0131877350112879 SFT2 domain containing 1 FUNCTION: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex. {ECO:0000250|UniProtKB:P38166}.; . . ovary;salivary gland;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;cerebellum;thymus; whole brain; 0.10870 0.06515 0.103030231 61.2762444 21.42372 0.72317 SFT2D2 0.00394965055414437 0.855531758646833 0.140518590799023 SFT2 domain containing 2 FUNCTION: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex. {ECO:0000250|UniProtKB:P38166}.; . . unclassifiable (Anatomical System);lymphoreticular;heart;pharynx;blood;skin;skeletal muscle;uterus;lung;liver;testis;spleen;kidney;tonsil; superior cervical ganglion;testis - interstitial;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10989 . -0.229483771 36.86010852 10.43983 0.37986 SFT2D3 . . . SFT2 domain containing 3 FUNCTION: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex. {ECO:0000250|UniProtKB:P38166}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;synovium;larynx;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.19420 . . . 2566.91092 9.46736 SFTA1P . . . surfactant associated 1, pseudogene . . . . . . . . . . . SFTA2 0.594981142208541 0.36595555861232 0.0390632991791392 surfactant associated 2 . . . unclassifiable (Anatomical System);lung;colon;kidney;skin;stomach; . 0.19027 . 0.21326276 67.71644256 291.04933 3.64879 SFTA3 0.294636981931893 0.625386208421171 0.0799768096469358 surfactant associated 3 . . TISSUE SPECIFICITY: Found (at protein level) in lung alveolar cells type I and II, as well as alveolar macrophages. {ECO:0000269|PubMed:24743970}.; . . . . 0.147123112 64.11299835 70.96794 1.75448 SFTPA1 0.000541611929247931 0.698591229011399 0.300867159059353 surfactant protein A1 FUNCTION: In presence of calcium ions, it binds to surfactant phospholipids and contributes to lower the surface tension at the air-liquid interface in the alveoli of the mammalian lung and is essential for normal respiration.; DISEASE: Pulmonary fibrosis, idiopathic (IPF) [MIM:178500]: A lung disease characterized by shortness of breath, radiographically evident diffuse pulmonary infiltrates, and varying degrees of inflammation and fibrosis on biopsy. In some cases, the disorder can be rapidly progressive and characterized by sequential acute lung injury with subsequent scarring and end-stage lung disease. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Respiratory distress syndrome in premature infants (RDS) [MIM:267450]: A lung disease affecting usually premature newborn infants. It is characterized by deficient gas exchange, diffuse atelectasis, high-permeability lung edema and fibrin-rich alveolar deposits called 'hyaline membranes'. {ECO:0000269|PubMed:10762543}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry. The association between SFTPA1 alleles and respiratory distress syndrome in premature infants is dependent on a variation Ile to Thr at position 131 in SFTPB.; . . . 0.07078 0.40525 0.461228372 78.46190139 831.90165 5.65086 SFTPA2 0.0145995049228688 0.873585597580302 0.111814897496829 surfactant protein A2 FUNCTION: In presence of calcium ions, it binds to surfactant phospholipids and contributes to lower the surface tension at the air-liquid interface in the alveoli of the mammalian lung and is essential for normal respiration.; DISEASE: Pulmonary fibrosis, idiopathic (IPF) [MIM:178500]: A lung disease characterized by shortness of breath, radiographically evident diffuse pulmonary infiltrates, and varying degrees of inflammation and fibrosis on biopsy. In some cases, the disorder can be rapidly progressive and characterized by sequential acute lung injury with subsequent scarring and end-stage lung disease. {ECO:0000269|PubMed:19100526}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.08226 0.13740 0.617373774 83.25076669 138.31651 2.56015 SFTPA3P . . . surfactant protein A3, pseudogene . . . . . . . . . . . SFTPB 0.040741578571877 0.952853358735952 0.00640506269217135 surfactant protein B FUNCTION: Pulmonary surfactant-associated proteins promote alveolar stability by lowering the surface tension at the air- liquid interface in the peripheral air spaces. SP-B increases the collapse pressure of palmitic acid to nearly 70 millinewtons per meter.; DISEASE: Pulmonary surfactant metabolism dysfunction 1 (SMDP1) [MIM:265120]: A rare lung disorder due to impaired surfactant homeostasis. It is characterized by alveolar filling with floccular material that stains positive using the periodic acid- Schiff method and is derived from surfactant phospholipids and protein components. Excessive lipoproteins accumulation in the alveoli results in severe respiratory distress. {ECO:0000269|PubMed:7491219}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Respiratory distress syndrome in premature infants (RDS) [MIM:267450]: A lung disease affecting usually premature newborn infants. It is characterized by deficient gas exchange, diffuse atelectasis, high-permeability lung edema and fibrin-rich alveolar deposits called 'hyaline membranes'. {ECO:0000269|PubMed:11063734}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry. A variation Ile to Thr at position 131 influences the association between specific alleles of SFTPA1 and respiratory distress syndrome in premature infants.; . unclassifiable (Anatomical System);lung;cartilage;nasopharynx;thyroid;placenta;testis;colon;spleen;brain; superior cervical ganglion;lung;ciliary ganglion;fetal lung;atrioventricular node;trigeminal ganglion; 0.19235 0.23535 0.709197509 85.68058504 200.48489 3.06078 SFTPC 0.0684488020229368 0.871750903782917 0.0598002941941458 surfactant protein C FUNCTION: Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air- liquid interface in the peripheral air spaces.; DISEASE: Pulmonary surfactant metabolism dysfunction 2 (SMDP2) [MIM:610913]: A rare disease associated with progressive respiratory insufficiency and lung disease with a variable clinical course, due to impaired surfactant homeostasis. It is characterized by alveolar filling with floccular material that stains positive using the periodic acid-Schiff method and is derived from surfactant phospholipids and protein components. Excessive lipoproteins accumulation in the alveoli results in severe respiratory distress. {ECO:0000269|PubMed:11991887, ECO:0000269|PubMed:15039969, ECO:0000269|PubMed:15293602, ECO:0000269|PubMed:15557112, ECO:0000269|PubMed:15572558}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Respiratory distress syndrome in premature infants (RDS) [MIM:267450]: A lung disease affecting usually premature newborn infants. It is characterized by deficient gas exchange, diffuse atelectasis, high-permeability lung edema and fibrin-rich alveolar deposits called 'hyaline membranes'. {ECO:0000269|PubMed:14735158}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;cartilage;sympathetic chain;colon;skin;retina;uterus;lung;nasopharynx;testis;kidney;brain; lung;fetal lung; 0.25737 0.23432 0.21689899 68.12927577 3906.63118 12.35564 SFTPD 0.240356031009661 0.752754018058034 0.00688995093230567 surfactant protein D FUNCTION: Contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties. {ECO:0000269|PubMed:23478426}.; . TISSUE SPECIFICITY: Expressed in lung, brain, pancreas and adipose tissue (mainly mature adipocytes). {ECO:0000269|PubMed:23478426}.; . . 0.04988 0.25503 0.751474114 86.64779429 582.85445 4.89509 SFTPD-AS1 . . . SFTPD antisense RNA 1 . . . . . . . . . . . SFXN1 0.58517754975236 0.41437385959553 0.000448590652110729 sideroflexin 1 FUNCTION: Might be involved in the transport of a component required for iron utilization into or out of the mitochondria.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;spinal cord;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;mesenchyma;epididymis;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.23911 0.15578 0.174625237 65.9648502 64.03438 1.64025 SFXN2 0.00108457408549622 0.951266274165116 0.0476491517493879 sideroflexin 2 FUNCTION: Potential iron transporter.; . TISSUE SPECIFICITY: Widely expressed, highest levels in kidney, liver, and pancreas. {ECO:0000269|PubMed:12670026}.; . . 0.06626 0.10227 -0.424258538 25.56027365 71.28418 1.75647 SFXN3 1.26901089843385e-11 0.0253988231664989 0.974601176820811 sideroflexin 3 FUNCTION: Potential iron transporter.; . . ovary;salivary gland;sympathetic chain;colon;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;pineal body;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;head and neck;cervix;mammary gland;stomach;aorta;cerebellum; subthalamic nucleus;cerebellum peduncles;temporal lobe;prefrontal cortex;trigeminal ganglion;cerebellum; 0.07889 0.08835 0.328949044 73.41354093 228.6513 3.26641 SFXN4 0.000148320455391636 0.992238286228954 0.00761339331565392 sideroflexin 4 FUNCTION: Potential iron transporter. {ECO:0000250}.; DISEASE: Combined oxidative phosphorylation deficiency 18 (COXPD18) [MIM:615578]: An autosomal recessive disorder of mitochondrial dysfunction characterized by intrauterine growth retardation, hypotonia, visual impairment, speech delay, and lactic acidosis associated with decreased mitochondrial respiratory chain activity. Affected patients may also show hematologic abnormalities, mainly macrocytic anemia. {ECO:0000269|PubMed:24119684}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;epidermis;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;adrenal gland;nasopharynx;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;trigeminal ganglion; 0.04555 0.06327 -0.714505427 14.4019816 9.01689 0.33046 SFXN5 0.0140304509437934 0.979563346835213 0.0064062022209937 sideroflexin 5 FUNCTION: Transports citrate. Potential iron transporter (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Primarily expressed in the brain. {ECO:0000269|PubMed:12039050}.; unclassifiable (Anatomical System);islets of Langerhans;salivary gland;muscle;colon;blood;skin;skeletal muscle;retina;bone marrow;uterus;prostate;pancreas;lung;endometrium;placenta;hippocampus;liver;testis;spleen;kidney;brain;mammary gland;aorta;stomach; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.18230 0.11388 -0.778825328 12.88039632 22.52132 0.75343 SGCA 0.194446674101566 0.794887266821406 0.0106660590770288 sarcoglycan alpha FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.; . TISSUE SPECIFICITY: Most strongly expressed in skeletal muscle. Also expressed in cardiac muscle and, at much lower levels, in lung. In the fetus, most abundant in cardiac muscle and, at lower levels, in lung. Also detected in liver and kidney. Not expressed in brain.; unclassifiable (Anatomical System);cartilage;heart;ovary;muscle;choroid;skeletal muscle;uterus;whole body;lung;bone;visual apparatus;testis;brain; superior cervical ganglion;heart;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.13568 0.10299 -0.712684326 14.49634348 89.9263 2.04040 SGCB 0.00360015162466118 0.842001022146507 0.154398826228832 sarcoglycan beta FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.; DISEASE: Limb-girdle muscular dystrophy 2E (LGMD2E) [MIM:604286]: An autosomal recessive degenerative myopathy characterized by pelvic and shoulder muscle wasting, onset usually in childhood and variable progression rate. {ECO:0000269|PubMed:8968749, ECO:0000269|PubMed:9565988, ECO:0000269|PubMed:9631401}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest expression in heart and skeletal muscle. Low expression in brain, kidney, placenta, pancreas and lung. High expression in fetal brain. Also found in fetal lung, kidney and liver.; . . 0.19969 0.11630 -0.227663163 37.11370606 92.95891 2.07177 SGCD 0.00233910042363156 0.92474998969308 0.0729109098832882 sarcoglycan delta FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.; DISEASE: Limb-girdle muscular dystrophy 2F (LGMD2F) [MIM:601287]: An autosomal recessive degenerative myopathy initially affecting the proximal limb girdle musculature. Muscle from patients shows a complete loss of delta-sarcoglycan as well as of the others components of the sarcoglycan complex. {ECO:0000269|PubMed:9832045}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1L (CMD1L) [MIM:606685]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:10974018}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Most strongly expressed in skeletal and cardiac muscle. Also detected in smooth muscle. Weak expression in brain and lung.; myocardium;ovary;colon;parathyroid;choroid;skin;uterus;atrium;whole body;thyroid;bone;pituitary gland;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;adrenal cortex;skeletal muscle;lung;adrenal gland;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; occipital lobe;medulla oblongata;superior cervical ganglion;olfactory bulb;ciliary ganglion;trigeminal ganglion;parietal lobe;skeletal muscle;cingulate cortex; 0.14985 0.36776 -0.271755481 34.31823543 233.51927 3.30188 SGCE 0.00138632178574484 0.9911233587579 0.00749031945635514 sarcoglycan epsilon FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.; DISEASE: Dystonia 11, myoclonic (DYT11) [MIM:159900]: A myoclonic dystonia. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. DYT11 is characterized by involuntary lightning jerks and dystonic movements and postures alleviated by alcohol. Inheritance is autosomal dominant. The age of onset, pattern of body involvement, presence of myoclonus and response to alcohol are all variable. {ECO:0000269|PubMed:11528394, ECO:0000269|PubMed:12402271, ECO:0000269|PubMed:15079037, ECO:0000269|PubMed:15258227, ECO:0000269|PubMed:16227522, ECO:0000269|PubMed:17853490, ECO:0000269|PubMed:18175340, ECO:0000269|PubMed:18362280, ECO:0000269|PubMed:19066193}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; ovary;parathyroid;skin;uterus;whole body;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;hypothalamus;urinary;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;hippocampus;liver;spleen;kidney;stomach;aorta;peripheral nerve; . 0.42305 0.23123 -0.53631094 20.53550366 62.60337 1.61828 SGCG 0.00637038417637866 0.911161181229688 0.082468434593933 sarcoglycan gamma FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.; . TISSUE SPECIFICITY: Expressed in skeletal and heart muscle.; unclassifiable (Anatomical System);uterus;whole body;heart;skin; superior cervical ganglion;tongue;ciliary ganglion;skeletal muscle; 0.11128 0.36264 -0.135838822 43.77211607 253.60081 3.42667 SGCZ 0.00198581635801512 0.976693683856909 0.0213204997850763 sarcoglycan zeta FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix. May play a role in the maintenance of striated muscle membrane stability (By similarity). {ECO:0000250}.; . . . . 0.47775 0.10103 -0.426079032 25.36565228 132.20995 2.50287 SGF29 . . . SAGA complex associated factor 29 FUNCTION: Involved in transcriptional regulation, through association with histone acetyltransferase (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes. Specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3). In the SAGA- type complexes, required to recruit complexes to H3K4me. May be involved in MYC-mediated oncogenic transformation. {ECO:0000269|PubMed:19103755}.; . . . . 0.19776 0.11809 -0.273576253 33.97027601 . . SGIP1 0.999651092711271 0.000348907281990592 6.73802701508139e-12 SH3-domain GRB2-like (endophilin) interacting protein 1 FUNCTION: May function in clathrin-mediated endocytosis. Has both a membrane binding/tubulating activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a preference for membranes enriched in phosphatidylserine and phosphoinositides and is required for the endocytosis of the transferrin receptor. May also bind tubulin. May play a role in the regulation of energy homeostasis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in brain. {ECO:0000269|PubMed:15919751}.; unclassifiable (Anatomical System);amygdala;islets of Langerhans;hypothalamus;pineal body;sympathetic chain;fovea centralis;choroid;lens;skin;retina;whole body;optic nerve;lung;endometrium;macula lutea;pituitary gland;testis;kidney;spinal ganglion;brain;aorta; whole brain;amygdala;occipital lobe; 0.55441 0.08704 -1.083859071 7.195093182 3375.22155 11.12347 SGK1 0.986448162634836 0.0135515850482105 2.52316953736295e-07 serum/glucocorticoid regulated kinase 1 FUNCTION: Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cellular enzymes, transcription factors, neuronal excitability, cell growth, proliferation, survival, migration and apoptosis. Plays an important role in cellular stress response. Contributes to regulation of renal Na(+) retention, renal K(+) elimination, salt appetite, gastric acid secretion, intestinal Na(+)/H(+) exchange and nutrient transport, insulin-dependent salt sensitivity of blood pressure, salt sensitivity of peripheral glucose uptake, cardiac repolarization and memory consolidation. Up-regulates Na(+) channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2, K(+) channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2 and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2, SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT, SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes: GSK3A/B, PMM2 and Na(+)/K(+) ATPase, and transcription factors: CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport into epithelial cells by enhancing the stability and expression of SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L ubiquitin E3 ligase, promoting its interaction with 14-3-3 proteins, thereby preventing it from binding to SCNN1A/ENAC and targeting it for degradation. Regulates store-operated Ca(+2) entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1 directly via its phosphorylation or indirectly via increased interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and activates MDM2-dependent ubiquitination of p53/TP53. Phosphorylates MAPT/TAU and mediates microtubule depolymerization and neurite formation in hippocampal neurons. Phosphorylates SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates APBB1/FE65 and promotes its localization to the nucleus. Phosphorylates MAPK1/ERK2 and activates it by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Phosphorylates FBXW7 and plays an inhibitory role in the NOTCH1 signaling. Phosphorylates FOXO1 resulting in its relocalization from the nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit from the nucleus and interference with FOXO3-dependent transcription. Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits their activity. Phosphorylates SLC9A3/NHE3 in response to dexamethasone, resulting in its activation and increased localization at the cell membrane. Phosphorylates CREB1. Necessary for vascular remodeling during angiogenesis. Sustained high levels and activity may contribute to conditions such as hypertension and diabetic nephropathy. Isoform 2 exhibited a greater effect on cell plasma membrane expression of SCNN1A/ENAC and Na(+) transport than isoform 1. {ECO:0000269|PubMed:11154281, ECO:0000269|PubMed:11410590, ECO:0000269|PubMed:11696533, ECO:0000269|PubMed:12397388, ECO:0000269|PubMed:12590200, ECO:0000269|PubMed:12634932, ECO:0000269|PubMed:12650886, ECO:0000269|PubMed:12761204, ECO:0000269|PubMed:12911626, ECO:0000269|PubMed:14623317, ECO:0000269|PubMed:14706641, ECO:0000269|PubMed:15040001, ECO:0000269|PubMed:15044175, ECO:0000269|PubMed:15234985, ECO:0000269|PubMed:15319523, ECO:0000269|PubMed:15496163, ECO:0000269|PubMed:15733869, ECO:0000269|PubMed:15737648, ECO:0000269|PubMed:15845389, ECO:0000269|PubMed:15888551, ECO:0000269|PubMed:16036218, ECO:0000269|PubMed:16443776, ECO:0000269|PubMed:16982696, ECO:0000269|PubMed:17382906, ECO:0000269|PubMed:18005662, ECO:0000269|PubMed:18304449, ECO:0000269|PubMed:18753299, ECO:0000269|PubMed:19447520, ECO:0000269|PubMed:19756449, ECO:0000269|PubMed:20511718, ECO:0000269|PubMed:20730100, ECO:0000269|PubMed:21865597}.; . TISSUE SPECIFICITY: Expressed in most tissues with highest levels in the pancreas, followed by placenta, kidney and lung. Isoform 2 is strongly expressed in brain and pancreas, weaker in heart, placenta, lung, liver and skeletal muscle. {ECO:0000269|PubMed:10548550, ECO:0000269|PubMed:18753299}.; ovary;sympathetic chain;substantia nigra;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;small intestine;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;pia mater;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; adrenal gland;adrenal cortex; 0.67964 0.57708 -0.288341872 33.41589998 105.09569 2.21804 SGK2 2.93457296557479e-07 0.51626802632845 0.483731680214253 serum/glucocorticoid regulated kinase 2 FUNCTION: Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cell growth, survival and proliferation. Up- regulates Na(+) channels: SCNN1A/ENAC, K(+) channels: KCNA3/Kv1.3, KCNE1 and KCNQ1, amino acid transporter: SLC6A19, glutamate transporter: SLC1A6/EAAT4, glutamate receptors: GRIA1/GLUR1 and GRIK2/GLUR6, Na(+)/H(+) exchanger: SLC9A3/NHE3, and the Na(+)/K(+) ATPase. {ECO:0000269|PubMed:12397388, ECO:0000269|PubMed:12590200, ECO:0000269|PubMed:12632189, ECO:0000269|PubMed:12634932, ECO:0000269|PubMed:15040001, ECO:0000269|PubMed:20511718, ECO:0000269|PubMed:21865597}.; . TISSUE SPECIFICITY: Highly expressed in liver, kidney and pancreas, and at lower levels in brain. {ECO:0000269|PubMed:10548550}.; unclassifiable (Anatomical System);uterus;lung;ovary;liver;colon;kidney;brain;skin;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.57729 0.10831 -0.312207497 32.05944798 119.47337 2.37862 SGK3 0.136832560084944 0.862988643309599 0.000178796605456706 serum/glucocorticoid regulated kinase family member 3 FUNCTION: Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cell growth, proliferation, survival and migration. Up-regulates Na(+) channels: SCNN1A/ENAC and SCN5A, K(+) channels: KCNA3/KV1.3, KCNE1, KCNQ1 and KCNH2/HERG, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channel: BSND, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, amino acid transporters: SLC1A5/ASCT2 and SLC6A19, glutamate transporters: SLC1A3/EAAT1, SLC1A6/EAAT4 and SLC1A7/EAAT5, glutamate receptors: GRIA1/GLUR1 and GRIK2/GLUR6, Na(+)/H(+) exchanger: SLC9A3/NHE3, and the Na(+)/K(+) ATPase. Plays a role in the regulation of renal tubular phosphate transport and bone density. Phosphorylates NEDD4L and GSK3B. Positively regulates ER transcription activity through phosphorylation of FLII. Negatively regulates the function of ITCH/AIP4 via its phosphorylation and thereby prevents CXCR4 from being efficiently sorted to lysosomes. {ECO:0000269|PubMed:12054501, ECO:0000269|PubMed:12397388, ECO:0000269|PubMed:12590200, ECO:0000269|PubMed:12632189, ECO:0000269|PubMed:12634932, ECO:0000269|PubMed:12650886, ECO:0000269|PubMed:12911626, ECO:0000269|PubMed:14706641, ECO:0000269|PubMed:15040001, ECO:0000269|PubMed:15044175, ECO:0000269|PubMed:15319523, ECO:0000269|PubMed:15496163, ECO:0000269|PubMed:15737648, ECO:0000269|PubMed:15845389, ECO:0000269|PubMed:16036218, ECO:0000269|PubMed:16888620, ECO:0000269|PubMed:17167223, ECO:0000269|PubMed:18005662, ECO:0000269|PubMed:19293151, ECO:0000269|PubMed:20511718, ECO:0000269|PubMed:21865597}.; . TISSUE SPECIFICITY: Expressed in most tissues with highest levels in pancreas, kidney liver, heart and brain and lower levels in lung, placenta and skeletal muscle. Expression is higher in ER- positive breast tumors than ER-negative breast tumors. {ECO:0000269|PubMed:21084382}.; lymphoreticular;ovary;colon;parathyroid;skin;retina;uterus;prostate;cochlea;endometrium;thyroid;bone;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lung;nasopharynx;placenta;hippocampus;liver;spleen;kidney;mammary gland;stomach; . 0.25430 0.12929 -0.317668748 31.45789101 . . SGMS1 0.89086679790325 0.109086231825504 4.69702712467e-05 sphingomyelin synthase 1 FUNCTION: Sphingomyelin synthases synthesize the sphingolipid, sphingomyelin, through transfer of the phosphatidyl head group, phosphatidylcholine, on to the primary hydroxyl of ceramide. The reaction is bidirectional depending on the respective levels of the sphingolipid and ceramide. Golgi apparatus SMS1 directly and specifically recognizes the choline head group on the substrate, requiring two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Major form in macrophages. Required for cell growth in certain cell types such as HeLa cells. Suppresses BAX-mediated apoptosis and also prevents cell death in response to stimuli such as hydrogen peroxide, osmotic stress, elevated temperature and exogenously supplied sphingolipids. May protect against cell death by reversing the stress-inducible increase in levels of proapoptotic ceramide. {ECO:0000269|PubMed:14685263, ECO:0000269|PubMed:17449912}.; . TISSUE SPECIFICITY: Brain, heart, kidney, liver, muscle and stomach. {ECO:0000269|PubMed:11841947, ECO:0000269|PubMed:14685263, ECO:0000269|PubMed:15315829}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;spinal cord;blood;lens;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skin; 0.28358 0.38765 -0.449946534 24.00330267 11.40907 0.41197 SGMS1-AS1 . . . SGMS1 antisense RNA 1 . . . . . . . . . . . SGMS2 0.0371284039640799 0.955503242364057 0.00736835367186281 sphingomyelin synthase 2 FUNCTION: Sphingomyelin synthases synthesize the sphingolipid, sphingomyelin, through transfer of the phosphatidyl head group, phosphatidylcholine, on to the primary hydroxyl of ceramide. The reaction is bidirectional depending on the respective levels of the sphingolipid and ceramide. Plasma membrane SMS2 can also convert phosphatidylethanolamine (PE) to ceramide phosphatidylethanolamine (CPE). Major form in liver. Required for cell growth in certain cell types. Regulator of cell surface levels of ceramide, an important mediator of signal transduction and apoptosis. Regulation of sphingomyelin (SM) levels at the cell surface affects insulin sensitivity. {ECO:0000269|PubMed:14685263, ECO:0000269|PubMed:17449912}.; . TISSUE SPECIFICITY: Brain, heart, kidney, liver, muscle and stomach. Also expressed in a number of cell lines such as carcinoma HeLa cells, hepatoma Hep-G2 cells, and colon carcinoma Caco-2 cells. {ECO:0000269|PubMed:14685263}.; ovary;salivary gland;intestine;colon;skin;uterus;optic nerve;whole body;thyroid;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;lung;cornea;placenta;visual apparatus;liver;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion; 0.31654 0.13293 0.016664174 55.21939137 29.24177 0.93575 SGOL1 2.46285208677179e-07 0.718446651350239 0.281553102364552 shugoshin-like 1 (S. pombe) FUNCTION: Plays a central role in chromosome cohesion during mitosis by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. May act by preventing phosphorylation of the STAG2 subunit of cohesin complex at the centromere, ensuring cohesin persistence at centromere until cohesin cleavage by ESPL1/separase at anaphase. Essential for proper chromosome segregation during mitosis and this function requires interaction with PPP2R1A. Its phosphorylated form is necessary for chromosome congression and for the proper attachment of spindle microtubule to the kinetochore. Necessary for kinetochore localization of PLK1 and CENPF. May play a role in the tension sensing mechanism of the spindle-assembly checkpoint by regulating PLK1 kinetochore affinity. Isoform 3 plays a role in maintaining centriole cohesion involved in controlling spindle pole integrity. {ECO:0000269|PubMed:15604152, ECO:0000269|PubMed:15723797, ECO:0000269|PubMed:15737064, ECO:0000269|PubMed:16580887, ECO:0000269|PubMed:17617734, ECO:0000269|PubMed:17621308, ECO:0000269|PubMed:18331714}.; DISEASE: Chronic atrial and intestinal dysrhythmia (CAID) [MIM:616201]: A disease characterized by dysregulation of the cardiac sinus node resulting in sick sinus syndrome, in association with chronic intestinal pseudo-obstruction, a disorder of gastrointestinal motility in which intestinal obstruction occurs in the absence of a mechanical obstacle. {ECO:0000269|PubMed:25282101}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis. Expressed in lung, small intestine, breast, liver and placenta. Strongly overexpressed in 90% of breast cancers tested. {ECO:0000269|PubMed:12747765}.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;bone marrow;breast;whole body;lung;cornea;nasopharynx;visual apparatus;liver;testis;spleen;germinal center;kidney;brain;mammary gland; . 0.06750 0.07755 0.709197509 85.68058504 90.99924 2.05214 SGOL1-AS1 . . . SGOL1 antisense RNA 1 . . . . . . . . . . . SGOL1P1 . . . shugoshin-like 1 (S. pombe) pseudogene 1 . . . . . . . . . . . SGOL1P2 . . . shugoshin-like 1 (S. pombe) pseudogene 2 . . . . . . . . . . . SGOL2 6.60739694811965e-05 0.994981577019205 0.00495234901131388 shugoshin-like 2 (S. pombe) FUNCTION: Cooperates with PPP2CA to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I. Has a crucial role in protecting REC8 at centromeres from cleavage by separase. During meiosis, protects centromeric cohesion complexes until metaphase II/anaphase II transition, preventing premature release of meiosis-specific REC8 cohesin complexes from anaphase I centromeres. Is thus essential for an accurate gametogenesis. May act by targeting PPP2CA to centromeres, thus leading to cohesin dephosphorylation (By similarity). Essential for recruiting KIF2C to the inner centromere and for correcting defective kinetochore attachments. {ECO:0000250, ECO:0000269|PubMed:16541025, ECO:0000269|PubMed:17485487}.; . . unclassifiable (Anatomical System);cartilage;heart;tongue;colon;blood;skin;uterus;whole body;lung;nasopharynx;liver;testis;head and neck;spleen;germinal center;mammary gland;stomach;thymus; . 0.05233 0.09647 2.252570408 98.20712432 910.64653 5.86745 SGPL1 0.122514047712303 0.877267857815296 0.000218094472401326 sphingosine-1-phosphate lyase 1 FUNCTION: Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis. {ECO:0000269|PubMed:11018465, ECO:0000269|PubMed:14570870, ECO:0000269|PubMed:24809814}.; . TISSUE SPECIFICITY: Found in liver and kidney. {ECO:0000269|PubMed:11018465}.; smooth muscle;ovary;rectum;skin;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;atrium;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;bile duct;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;hypopharynx;amnion;head and neck;kidney;stomach; dorsal root ganglion;uterus corpus;superior cervical ganglion;temporal lobe;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.16544 0.43246 -0.290161348 33.33923095 406.33204 4.22621 SGPP1 0.500345892791711 0.495365867737628 0.00428823947066026 sphingosine-1-phosphate phosphatase 1 FUNCTION: Has enzymatic activity against both sphingosine 1- phosphate (S1P) and dihydro-S1P. Regulates intracellular and extracellular S1P levels. {ECO:0000269|PubMed:12815058}.; . TISSUE SPECIFICITY: Ubiquitous, with the strongest level in placenta and kidney. {ECO:0000269|PubMed:12815058}.; unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;blood;skin;skeletal muscle;prostate;whole body;lung;frontal lobe;adrenal gland;placenta;liver;head and neck;germinal center;kidney;brain;bladder;stomach;gall bladder;cerebellum;thymus; amygdala;superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.34123 0.13888 -0.359940251 28.93371078 25.10585 0.82158 SGPP2 0.0122737609427454 0.852545661567613 0.135180577489641 sphingosine-1-phosphate phosphatase 2 FUNCTION: Has specific phosphohydrolase activity towards sphingoid base 1-phosphates. Has high phosphohydrolase activity against dihydrosphingosine-1-phosphate and sphingosine-1-phosphate (S1P) in vitro. May play a role in attenuating intracellular sphingosine 1-phosphate (S1P) signaling. May play a role in pro-inflammatory signaling. {ECO:0000269|PubMed:12411432, ECO:0000269|PubMed:17113265}.; . TISSUE SPECIFICITY: Expressed strongly in kidney and heart, followed by brain, colon, small intestine and lung. Not detected in skeletal muscle, thymus, spleen, liver, placenta, and peripheral blood leukocytes. {ECO:0000269|PubMed:12411432}.; unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;skin;lung;cornea;visual apparatus;liver;kidney;brain;mammary gland;stomach; dorsal root ganglion;ciliary ganglion; 0.17475 0.12155 -0.602450568 17.91106393 61.12309 1.59129 SGSH 0.000105789945939708 0.813618449241641 0.186275760812419 N-sulfoglucosamine sulfohydrolase . DISEASE: Mucopolysaccharidosis 3A (MPS3A) [MIM:252900]: A severe form of mucopolysaccharidosis type 3, an autosomal recessive lysosomal storage disease due to impaired degradation of heparan sulfate. MPS3 is characterized by severe central nervous system degeneration, but only mild somatic disease. Onset of clinical features usually occurs between 2 and 6 years; severe neurologic degeneration occurs in most patients between 6 and 10 years of age, and death occurs typically during the second or third decade of life. MPS3A is characterized by earlier onset, rapid progression of symptoms and shorter survival. {ECO:0000269|PubMed:11182930, ECO:0000269|PubMed:11793481, ECO:0000269|PubMed:12000360, ECO:0000269|PubMed:12702166, ECO:0000269|PubMed:15146460, ECO:0000269|PubMed:15637719, ECO:0000269|PubMed:15902564, ECO:0000269|PubMed:16311287, ECO:0000269|PubMed:17128482, ECO:0000269|PubMed:18407553, ECO:0000269|PubMed:21671382, ECO:0000269|PubMed:9158154, ECO:0000269|PubMed:9285796, ECO:0000269|PubMed:9401012, ECO:0000269|PubMed:9554748, ECO:0000269|PubMed:9744479}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;salivary gland;colon;parathyroid;skin;retina;uterus;prostate;endometrium;larynx;thyroid;bone;testis;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;mammary gland;stomach; superior cervical ganglion;adrenal gland;thyroid;adrenal cortex; 0.11962 0.17483 0.338046437 73.70252418 1221.396 6.60693 SGSM1 0.977248922647981 0.0227510758376059 1.51441363672265e-09 small G protein signaling modulator 1 . . TISSUE SPECIFICITY: Mainly expressed in brain, heart and testis. {ECO:0000269|PubMed:17509819}.; . . 0.19919 0.10282 -0.698154263 14.82661005 858.83951 5.71662 SGSM2 5.55963371668394e-08 0.998196866222293 0.00180307818136986 small G protein signaling modulator 2 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17509819}.; myocardium;lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;gall bladder;amygdala;heart;cartilage;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;thymus;cerebellum; amygdala;superior cervical ganglion;subthalamic nucleus;medulla oblongata;temporal lobe;prefrontal cortex;globus pallidus;pons;atrioventricular node;caudate nucleus;trigeminal ganglion;cingulate cortex; 0.25708 0.09905 -0.738630771 13.80042463 708.63925 5.28721 SGSM3 1.00601271154805e-06 0.996607292555308 0.00339170143198032 small G protein signaling modulator 3 FUNCTION: May play a cooperative role in NF2-mediated growth suppression of cells. {ECO:0000269|PubMed:15541357}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17509819}.; lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;submandibular gland;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;urinary;blood;breast;visual apparatus;liver;spleen;mammary gland;peripheral nerve;colon;uterus;ileum;whole body;oesophagus;synovium;bone;pituitary gland;testis;myometrium;unclassifiable (Anatomical System);lymph node;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;nose;stomach;aorta;parietal lobe;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.12662 0.10486 -2.45481381 1.008492569 94.74018 2.09725 SGTA 0.470281213257638 0.528607769140511 0.00111101760185104 small glutamine rich tetratricopeptide repeat containing alpha FUNCTION: Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity. {ECO:0000269|PubMed:18759457}.; . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pineal body;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;uterus;whole body;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;cerebellum; subthalamic nucleus;cerebellum peduncles;globus pallidus;atrioventricular node; 0.19064 0.24906 -0.66859065 15.76433121 13.56039 0.49255 SGTB 0.991633522582233 0.00836458908911272 1.88832865438328e-06 small glutamine rich tetratricopeptide repeat containing beta FUNCTION: Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity. {ECO:0000250}.; . . . . 0.29302 0.17394 -0.029247611 51.40363293 24.32508 0.79884 SH2B1 0.956829709593037 0.0431658589731375 4.43143382528098e-06 SH2B adaptor protein 1 FUNCTION: Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways mediated by Janus kinase (JAK) and receptor tyrosine kinases, including the receptors of insulin (INS), insulin-like growth factor I (IGF1), nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), glial cell line-derived neurotrophic factor (GDNF), platelet-derived growth factor (PDGF) and fibroblast growth factors (FGFs). In growth hormone (GH) signaling, autophosphorylated ('Tyr-813') JAK2 recruits SH2B1, which in turn is phosphorylated by JAK2 on tyrosine residues. These phosphotyrosines form potential binding sites for other signaling proteins. GH also promotes serine/threonine phosphorylation of SH2B1 and these phosphorylated residues may serve to recruit other proteins to the GHR-JAK2-SH2B1 complexes, such as RAC1. In leptin (LEP) signaling, binds to and potentiates the activation of JAK2 by globally enhancing downstream pathways. In response to leptin, binds simultaneously to both, JAK2 and IRS1 or IRS2, thus mediating formation of a complex of JAK2, SH2B1 and IRS1 or IRS2. Mediates tyrosine phosphorylation of IRS1 and IRS2, resulting in activation of the PI 3-kinase pathway. Acts as positive regulator of NGF-mediated activation of the Akt/Forkhead pathway; prolongs NGF-induced phosphorylation of AKT1 on 'Ser-473' and AKT1 enzymatic activity. Enhances the kinase activity of the cytokine receptor-associated tyrosine kinase JAK2 and of other receptor tyrosine kinases, such as FGFR3 and NTRK1. For JAK2, the mechanism seems to involve dimerization of both, SH2B1 and JAK2. Enhances RET phosphorylation and kinase activity. Isoforms seem to be differentially involved in IGF-I and PDGF-induced mitogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:11827956, ECO:0000269|PubMed:14565960, ECO:0000269|PubMed:15767667, ECO:0000269|PubMed:16569669, ECO:0000269|PubMed:17471236, ECO:0000269|PubMed:9694882, ECO:0000269|PubMed:9742218}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in skeletal muscle and ovary. {ECO:0000269|PubMed:15767667}.; ovary;salivary gland;sympathetic chain;colon;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;muscle;blood;lens;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.50303 0.23508 -0.244249595 36.17008728 1577.15232 7.34901 SH2B2 0.0113599414609977 0.842061451953783 0.146578606585219 SH2B adaptor protein 2 FUNCTION: Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways. May be involved in coupling from immunoreceptor to Ras signaling. Acts as a negative regulator of cytokine signaling in collaboration with CBL. Binds to EPOR and suppresses EPO-induced STAT5 activation, possibly through a masking effect on STAT5 docking sites in EPOR. Suppresses PDGF-induced mitogenesis. May induce cytoskeletal reorganization via interaction with VAV3. {ECO:0000269|PubMed:10374881, ECO:0000269|PubMed:12400014, ECO:0000269|PubMed:15378031, ECO:0000269|PubMed:9989826}.; . TISSUE SPECIFICITY: Expressed in spleen, prostate, testis, uterus, small intestine and skeletal muscle. Among hematopoietic cell lines, expressed exclusively in B-cells. Not expressed in most tumor cell lines. {ECO:0000269|PubMed:9233773, ECO:0000269|PubMed:9989826}.; unclassifiable (Anatomical System);lymphoreticular;smooth muscle;lung;ovary;placenta;muscle;testis;colon;blood;germinal center;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.09897 . . . 681.01598 5.21726 SH2B3 0.00592218956138136 0.972368399236281 0.0217094112023377 SH2B adaptor protein 3 FUNCTION: Links T-cell receptor activation signal to phospholipase C-gamma-1, GRB2 and phosphatidylinositol 3-kinase. {ECO:0000250}.; DISEASE: Celiac disease 13 (CELIAC13) [MIM:612011]: A multifactorial, chronic disorder of the small intestine caused by intolerance to gluten. It is characterized by immune-mediated enteropathy associated with failed intestinal absorption, and malnutrition. In predisposed individuals, the ingestion of gluten- containing food such as wheat and rye induces a flat jejunal mucosa with infiltration of lymphocytes. {ECO:0000269|PubMed:18311140}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Diabetes mellitus, insulin-dependent (IDDM) [MIM:222100]: A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:17554260}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Preferentially expressed by lymphoid cell lines.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;aorta;peripheral nerve; superior cervical ganglion;atrioventricular node; 0.78211 0.35815 . . 1095.64678 6.33313 SH2D1A 0.0826088107933548 0.7572743647861 0.160116824420545 SH2 domain containing 1A FUNCTION: Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as SLAMF1, CD244, LY9, CD84, SLAMF6 and SLAMF7. In SLAM signaling seems to cooperate with SH2D1B/EAT-2. Initially it has been proposed that association with SLAMF1 prevents SLAMF1 binding to inhibitory effectors including INPP5D/SHIP1 and PTPN11/SHP-2 (PubMed:11806999). However, by simultaneous interactions, recruits FYN which subsequently phosphorylates and activates SLAMF1 (PubMed:12458214). Positively regulates CD244/2B4- and CD84- mediated natural killer (NK) cell functions. Can also promote CD48-, SLAMF6 -, LY9-, and SLAMF7-mediated NK cell activation. In the context of NK cell-mediated cytotoxicity enhances conjugate formation with target cells (By similarity). May also regulate the activity of the neurotrophin receptors NTRK1, NTRK2 and NTRK3. {ECO:0000250|UniProtKB:O88890, ECO:0000269|PubMed:11806999, ECO:0000269|PubMed:12458214, ECO:0000305|PubMed:21219180}.; . TISSUE SPECIFICITY: Expressed at a high level in thymus and lung, with a lower level of expression in spleen and liver. Expressed in peripheral blood leukocytes, including T-lymphocytes. Tends to be expressed at lower levels in peripheral blood leukocytes in patients with rheumatoid arthritis. {ECO:0000269|PubMed:11282995}.; unclassifiable (Anatomical System);uterus;heart;blood;skin; superior cervical ganglion;trigeminal ganglion;whole blood;thymus; 0.50353 0.45280 0.057118534 57.99716914 1.31797 0.04688 SH2D1B 0.0598833646548052 0.86834870550583 0.0717679298393651 SH2 domain containing 1B FUNCTION: Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as CD84, SLAMF1, LY9 and CD244 (PubMed:11689425). In SLAM signaling seems to cooperate with SH2D1A/SAP. Plays a role in regulation of effector functions of natural killer (NK) cells by controlling signal transduction through CD244/2B4 without effecting its tyrosine phosphorylation; downstream signaling involves PLCG1 and ERK activation (PubMed:24687958). Activation of SLAMF7-mediated NK cell function does not effect receptor tyrosine phosphorylation but distal signaling (By similarity). In the context of NK cell- mediated cytotoxicity does not enhance conjugate formation with target cells but stimulates polarization of the microtubule- organizing center and cytotoxic granules toward the NK cell synapse (PubMed:24687958). Negatively regulates CD40-induced cytokine procuction dendritic cells downstream of SLAM family receptors probably by inducing activation of the PI3K pathway to inhibit p38 MAPK and JNK activation (By similarity). {ECO:0000250|UniProtKB:O35324, ECO:0000269|PubMed:11689425, ECO:0000269|PubMed:24687958, ECO:0000305|PubMed:21219180}.; . . spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.13294 0.14684 0.369407109 74.95281906 657.65469 5.14260 SH2D2A 8.43213730306944e-05 0.772526141841637 0.227389536785333 SH2 domain containing 2A FUNCTION: Could be a T-cell-specific adapter protein involved in the control of T-cell activation. May play a role in the CD4-p56- LCK-dependent signal transduction pathway. Could also play an important role in normal and pathological angiogenesis. Could be an adapter protein that facilitates and regulates interaction of KDR with effector proteins important to endothelial cell survival and proliferation.; . TISSUE SPECIFICITY: Expression limited to tissues of the immune system and, in particular, activated T-cells. Expressed in peripheral blood leukocytes, thymus and spleen. Much lower expression or undetectable, in brain, placenta, skeletal muscle, prostate, testis, ovary, small intestine, and colon. Expressed at low levels in unstimulated T-cells, but not expressed in normal resting or activated B-cells. According to PubMed:10692392, expression is not restricted to activated T-cells, but strongly expressed in blood cell lineages, the endothelium and other cell and tissue types, such as heart, lung, and liver.; . . 0.21852 0.11790 0.52918614 80.81505072 62.22259 1.60959 SH2D3A 4.11388010763311e-06 0.828986236392526 0.171009649727366 SH2 domain containing 3A FUNCTION: May play a role in JNK activation.; . TISSUE SPECIFICITY: Weakly expressed in placenta, fetal kidney, fetal lung, adult pancreas, adult kidney and adult lung. {ECO:0000269|PubMed:10187783}.; unclassifiable (Anatomical System);lymph node;islets of Langerhans;oral cavity;colon;blood;uterus;bile duct;prostate;pancreas;whole body;lung;endometrium;placenta;testis;cervix;head and neck;brain;mammary gland;bladder;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.12796 0.11754 1.512041961 95.47062987 2116.4495 8.46811 SH2D3C 0.000941187334660319 0.996381627958924 0.00267718470641557 SH2 domain containing 3C FUNCTION: Eph receptor-binding protein which may be a positive regulator of TCR signaling. Binding to BCAR1 is required to induce membrane ruffling and promote EGF-dependent cell migration (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10187783}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.33676 0.12268 -0.639268965 16.70794999 510.40629 4.62665 SH2D4A 1.53114480649588e-18 0.00151260275867082 0.998487397241329 SH2 domain containing 4A FUNCTION: Inhibits estrogen-induced cell proliferation by competing with PLCG for binding to ESR1, blocking the effect of estrogen on PLCG and repressing estrogen-induced proliferation. May play a role in T-cell development and function. {ECO:0000269|PubMed:18641339, ECO:0000269|PubMed:19712589}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Aberrantly expressed in some cancers. {ECO:0000269|PubMed:12476414}.; unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;urinary;colon;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;prostate;optic nerve;whole body;lung;bone;placenta;macula lutea;liver;testis;cervix;kidney;stomach; superior cervical ganglion;skeletal muscle; 0.13779 0.09450 0.69078985 85.23826374 3397.3404 11.16974 SH2D4B 3.12418681330873e-07 0.529577524050189 0.47042216353113 SH2 domain containing 4B . . . lung;testis; . 0.34685 0.10182 1.332002318 94.20853975 3636.74731 11.69765 SH2D5 0.00265361571731959 0.934879567861457 0.0624668164212237 SH2 domain containing 5 FUNCTION: May be involved in synaptic plasticity regulation through the control of Rac-GTP levels. {ECO:0000250|UniProtKB:Q8JZW5}.; . . . . 0.23004 0.10952 -0.378346116 28.01368247 58.13047 1.54287 SH2D6 0.00369649800986005 0.631606601925408 0.364696900064732 SH2 domain containing 6 . . . unclassifiable (Anatomical System);testis;colon; . 0.05815 . 0.459411326 78.28497287 94.15331 2.08683 SH2D7 0.0014209813173193 0.870030300252699 0.128548718429982 SH2 domain containing 7 . . . placenta; . . . 0.330767508 73.53739089 233.23378 3.30141 SH3BGR 0.00035235304533994 0.605670981682243 0.393976665272417 SH3 domain binding glutamate rich protein . . TISSUE SPECIFICITY: Expressed in heart and skeletal muscle.; smooth muscle;ovary;sympathetic chain;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;alveolus;kidney;aorta; medulla oblongata;superior cervical ganglion;testis - interstitial;tongue;hypothalamus;caudate nucleus;skeletal muscle;cingulate cortex; 0.05491 0.05734 1.304504747 93.94904459 562.90492 4.81697 SH3BGRL 0.281416437305486 0.631207457664653 0.0873761050298612 SH3 domain binding glutamate rich protein like . . TISSUE SPECIFICITY: Ubiquitous.; . . 0.76391 0.14229 0.013025609 54.62962963 2.51484 0.09292 SH3BGRL2 7.16872263567788e-06 0.160301960201695 0.839690871075669 SH3 domain binding glutamate rich protein like 2 . . TISSUE SPECIFICITY: Highly expressed in brain, placenta, liver and kidney. Expressed in retina. {ECO:0000269|PubMed:12095696}.; . . 0.16852 . 0.147123112 64.11299835 18.93269 0.65369 SH3BGRL3 0.795103829065415 0.199051223613106 0.00584494732147843 SH3 domain binding glutamate rich protein like 3 FUNCTION: Could act as a modulator of glutaredoxin biological activity.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11444877}.; myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;gum;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;spinal cord;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;oral cavity;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; lung;adipose tissue;smooth muscle;heart;white blood cells;whole blood;bone marrow; 0.12662 0.08852 0.035072054 56.2514744 4.86239 0.17906 SH3BP1 0.152682967806694 0.846596532447131 0.000720499746174886 SH3-domain binding protein 1 FUNCTION: Binds differentially to the SH3 domains of certain proteins of signal transduction pathways. This protein binds preferentially to the ABL1 proto-oncogene, SRC and GRB2. Shows GAP activity for Rac-related proteins but not for Rho- or Ras-related proteins. It inhibits PDGF-induced membrane ruffling mediated by Rac (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;cartilage;colon;blood;skin;uterus;epididymis;placenta;bone;germinal center;kidney;spinal ganglion;bladder;brain;tonsil;stomach; . . 0.11139 0.466683681 78.73908941 678.37787 5.20399 SH3BP2 0.00310189992242549 0.985414006788582 0.0114840932889929 SH3-domain binding protein 2 FUNCTION: Binds differentially to the SH3 domains of certain proteins of signal transduction pathways. Binds to phosphatidylinositols; linking the hemopoietic tyrosine kinase fes to the cytoplasmic membrane in a phosphorylation dependent mechanism.; DISEASE: Cherubism (CRBM) [MIM:118400]: An autosomal dominant syndrome characterized by excessive bone degradation of the upper and lower jaws, which often begins around three years of age. It is followed by development of fibrous tissue masses, which causes a characteristic facial swelling. {ECO:0000269|PubMed:11381256, ECO:0000269|PubMed:12900899, ECO:0000269|PubMed:14577811}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in a variety of tissues including lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:9734812}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;bone;testis;corpus striatum;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13698 0.15124 -0.837696902 11.45317292 106.0391 2.23361 SH3BP4 0.0809644359581152 0.916860140306563 0.00217542373532201 SH3-domain binding protein 4 FUNCTION: May function in transferrin receptor internalization at the plasma membrane through a cargo-specific control of clathrin- mediated endocytosis. Alternatively, may act as a negative regulator of the amino acid-induced TOR signaling by inhibiting the formation of active Rag GTPase complexes. Preferentially binds inactive Rag GTPase complexes and prevents their interaction with the mTORC1 complex inhibiting its relocalization to lysosomes and its activation. Thereby, may indirectly regulate cell growth, proliferation and autophagy. {ECO:0000269|PubMed:16325581, ECO:0000269|PubMed:22575674}.; . TISSUE SPECIFICITY: Expressed in all tissues tested with higher expression in pancreas. Expressed by retinal pigment epithelial cells (at protein level). {ECO:0000269|PubMed:10644451, ECO:0000269|PubMed:15616480}.; ovary;sympathetic chain;colon;vein;skin;uterus;prostate;endometrium;synovium;larynx;gum;thyroid;iris;pituitary gland;testis;amniotic fluid;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;visual apparatus;liver;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; . 0.16796 0.10864 -0.72020276 14.27813163 283.16989 3.60324 SH3BP5 0.00902325002023801 0.978921719887121 0.012055030092641 SH3-domain binding protein 5 FUNCTION: Inhibits the auto- and transphosphorylation activity of BTK. Plays a negative regulatory role in BTK-related cytoplasmic signaling in B-cells. May be involved in BCR-induced apoptotic cell death. {ECO:0000269|PubMed:10339589, ECO:0000269|PubMed:9571151}.; . TISSUE SPECIFICITY: Highly expressed in testis and ovaries. It is also expressed in a variety of tissues including spleen, lymph node, thymus, bone marrow, fetal liver, colon, small intestine and prostate. {ECO:0000269|PubMed:9571151}.; medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;tonsil;heart;cartilage;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; superior cervical ganglion;adrenal gland;adrenal cortex; 0.33935 0.27067 0.308721233 72.59966973 195.08335 3.02765 SH3BP5-AS1 . . . SH3BP5 antisense RNA 1 . . . . . . . . . . . SH3BP5L 0.140999405772345 0.854912467276809 0.00408812695084498 SH3-binding domain protein 5 like . . . . . 0.16873 0.11080 -0.736552314 13.93606983 15.89801 0.56402 SH3D19 0.3750873860445 0.624908739914493 3.87404100680313e-06 SH3 domain containing 19 FUNCTION: May play a role in regulating A disintegrin and metalloproteases (ADAMs) in the signaling of EGFR-ligand shedding. May be involved in suppression of Ras-induced cellular transformation and Ras-mediated activation of ELK1. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:14551139, ECO:0000269|PubMed:15280379, ECO:0000269|PubMed:21834987}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in heart, skeletal muscle, kidney, liver, placenta, small intestine and lung. Expressed at low levels in colon, thymus, spleen and leukocytes. {ECO:0000269|PubMed:15280379}.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;ciliary ganglion; 0.30262 0.13522 -0.086288664 47.11606511 842.83393 5.68279 SH3D21 0.000722997736993469 0.520254217340407 0.479022784922599 SH3 domain containing 21 . . . colon;choroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;optic nerve;thyroid;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;liver;stomach; superior cervical ganglion; 0.03355 . 0.512596355 80.29606039 601.00137 4.96140 SH3GL1 0.0586367540123022 0.937711278483891 0.00365196750380682 SH3-domain GRB2-like 1 FUNCTION: Implicated in endocytosis. May recruit other proteins to membranes with high curvature (By similarity). {ECO:0000250}.; DISEASE: Note=In some cases of acute leukemia, a translocation results in the formation of a KMT2A/MLL1-EEN fusion gene. {ECO:0000269|PubMed:9122235}.; TISSUE SPECIFICITY: Ubiquitous. Higher expression in pancreas, placenta, prostate, testis and uterus.; lymphoreticular;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;iris;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;duodenum;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;stomach;peripheral nerve; prostate;tongue; 0.06869 . -1.021348453 7.997169144 56.65861 1.51351 SH3GL1P1 . . . SH3-domain GRB2-like 1 pseudogene 1 . . . . . . . . . . . SH3GL1P2 . . . SH3-domain GRB2-like 1 pseudogene 2 . . . . . . . . . . . SH3GL1P3 . . . SH3-domain GRB2-like 1 pseudogene 3 . . . . . . . . . . . SH3GL2 0.916295307104429 0.0836810443137059 2.36485818652189e-05 SH3-domain GRB2-like 2 FUNCTION: Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature.; . TISSUE SPECIFICITY: Brain, mostly in frontal cortex. Expressed at high level in fetal cerebellum.; . . 0.31500 0.20767 -0.492218069 22.35786742 28.23793 0.90583 SH3GL3 0.000359349545380338 0.952407934761839 0.0472327156927804 SH3-domain GRB2-like 3 FUNCTION: Implicated in endocytosis. May recruit other proteins to membranes with high curvature (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Brain and testis.; unclassifiable (Anatomical System);uterus;prostate;lung;frontal lobe;heart;testis;brain;skin; amygdala;dorsal root ganglion;occipital lobe;testis - interstitial;thalamus;superior cervical ganglion;medulla oblongata;hypothalamus;spinal cord;temporal lobe;atrioventricular node;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.08575 0.10874 0.283038099 71.26680821 13.53368 0.49156 SH3GLB1 0.730421396838354 0.269015599559335 0.000563003602310705 SH3-domain GRB2 like endophilin B1 FUNCTION: May be required for normal outer mitochondrial membrane dynamics (PubMed:15452144). Required for coatomer-mediated retrograde transport in certain cells (By similarity). May recruit other proteins to membranes with high curvature. May promote membrane fusion (PubMed:11604418). Involved in activation of caspase-dependent apoptosis by promoting BAX/BAK1 activation (PubMed:16227588). Isoform 1 acts proapoptotic in fibroblasts (By similarity). Involved in caspase-independent apoptosis during nutrition starvation and involved in the regulation of autophagy. Activates lipid kinase activity of PIK3C3 during autophagy probably by associating with the PI3K complex II (PI3KC3-C2) (PubMed:17891140). Associated with PI3KC3-C2 during autophagy may regulate the trafficking of ATG9A from the Golgi complex to the peripheral cytoplasm for the formation of autophagosomes by inducing Golgi membrane tubulation and fragmentation (PubMed:21068542). Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20643123). Isoform 2 acts antiapoptotic in neuronal cells; involved in maintenance of mitochondrial morphology and promotes neuronal viability (By similarity). {ECO:0000250|UniProtKB:Q9JK48, ECO:0000269|PubMed:11604418, ECO:0000269|PubMed:15452144, ECO:0000269|PubMed:17891140, ECO:0000269|PubMed:20643123, ECO:0000269|PubMed:21068542}.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, kidney and placenta. Detected at lower levels in brain, colon, thymus, spleen, liver, small intestine, lung and peripheral blood leukocytes. {ECO:0000269|PubMed:11161816, ECO:0000269|PubMed:11259440}.; myocardium;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;adipose tissue;testis - seminiferous tubule;fetal brain;testis;ciliary ganglion;atrioventricular node;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.10774 0.13117 -0.317668748 31.45789101 14.24771 0.51550 SH3GLB2 0.370053036389675 0.627566211221342 0.00238075238898238 SH3-domain GRB2-like endophilin B2 . . TISSUE SPECIFICITY: Detected in skeletal muscle, adipocyte, brain, lung, colon and mammary gland. {ECO:0000269|PubMed:11161816}.; . . 0.20329 0.10718 0.174625237 65.9648502 118.51167 2.36903 SH3KBP1 0.998643127661381 0.00135685007514528 2.22634739439498e-08 SH3-domain kinase binding protein 1 FUNCTION: Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through a association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit (By similarity). May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. {ECO:0000250, ECO:0000269|PubMed:11894095, ECO:0000269|PubMed:11894096, ECO:0000269|PubMed:12177062, ECO:0000269|PubMed:12734385, ECO:0000269|PubMed:12771190, ECO:0000269|PubMed:15090612, ECO:0000269|PubMed:15707590, ECO:0000269|PubMed:16177060, ECO:0000269|PubMed:16256071, ECO:0000269|PubMed:21834987}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Also expressed in some cancer cell lines.; . . 0.82888 0.14174 -0.422438699 25.64284029 50.91638 1.40629 SH3PXD2A 0.232738023334583 0.767249304749207 1.26719162097502e-05 SH3 and PX domains 2A FUNCTION: Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of beta-amyloid peptide. {ECO:0000269|PubMed:12615925, ECO:0000269|PubMed:15710328, ECO:0000269|PubMed:15710903, ECO:0000269|PubMed:19755710, ECO:0000269|PubMed:20609497}.; . TISSUE SPECIFICITY: Found in several cancer cell lines, particularly invasive breast carcinomas and melanomas. {ECO:0000269|PubMed:15710328}.; smooth muscle;ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;nervous;hypothalamus;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;macula lutea;liver;hypopharynx;cervix;head and neck;spleen;kidney;stomach; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.44247 0.12129 -1.830003058 2.117244633 780.89034 5.52782 SH3PXD2A-AS1 . . . SH3PXD2A antisense RNA 1 . . . . . . . . . . . SH3PXD2B 0.0185367927997724 0.981286619463668 0.000176587736559825 SH3 and PX domains 2B FUNCTION: Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. Plays a role in mitotic clonal expansion during the immediate early stage of adipocyte differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:12615925, ECO:0000269|PubMed:19755710, ECO:0000269|PubMed:20609497}.; DISEASE: Frank-Ter Haar syndrome (FTHS) [MIM:249420]: A syndrome characterized by brachycephaly, wide fontanels, prominent forehead, hypertelorism, prominent eyes, macrocornea with or without glaucoma, full cheeks, small chin, bowing of the long bones and flexion deformity of the fingers. {ECO:0000269|PubMed:20137777}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in fibroblasts. {ECO:0000269|PubMed:20137777}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;larynx;thyroid;bone;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;cervix;head and neck;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.26216 0.10532 -0.279250919 33.56923803 389.35486 4.15627 SH3RF1 0.0463955276236296 0.953386569918973 0.0002179024573979 SH3 domain containing ring finger 1 FUNCTION: Acts as a scaffold protein, contributes to Rac-induced signal transduction such as JNKs (MAPK8 and MAPK9) activation and induces apoptosis. Within a signaling complex, it probably recruits protein kinases such as MAP3K10 or MAP3K11 which are in turn activated leading to the sequential activation of MAP2K4, MAP2K7 and JNKs (MAPK8 and MAPK9) (By similarity). May be involved in targeting of HIV-1 GAG and GAG-POL polyproteins to the plasma membrane. {ECO:0000250, ECO:0000269|PubMed:15659549, ECO:0000269|PubMed:19710010}.; FUNCTION: Plays an essential role in the targeting of HIV-1 Gag to the plasma membrane, this function is dependent on it's RING domain, and hence it's E3 ligase activity.; . . ovary;colon;parathyroid;uterus;prostate;frontal lobe;endometrium;larynx;thyroid;bone;iris;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);tongue;islets of Langerhans;skeletal muscle;breast;lung;placenta;visual apparatus;liver;head and neck;cervix;kidney;stomach; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.66607 0.13805 -0.573127851 18.96083982 344.52462 3.93697 SH3RF2 1.79074374939974e-11 0.111247307853066 0.888752692129027 SH3 domain containing ring finger 2 FUNCTION: Inhibits PPP1CA phosphatase activity. May be a E3 ubiquitin-protein ligase (Potential). May play a role in cardiac function. {ECO:0000269|PubMed:19389623, ECO:0000269|PubMed:19945436, ECO:0000305}.; . TISSUE SPECIFICITY: Heart (at protein level). Heart and testis. In the heart, present in the apex, left atrium, right atrium, left ventricle and right ventricle, but not in the aorta. {ECO:0000269|PubMed:19945436}.; unclassifiable (Anatomical System);myocardium;cartilage;ovary;heart;colon;skin;breast;uterus;pancreas;prostate;lung;thyroid;visual apparatus;liver;testis;spleen;kidney;brain;bladder;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17894 0.09775 -0.146971018 42.31540458 238.18509 3.33526 SH3RF3 0.981100871728341 0.0188851892501809 1.39390214782535e-05 SH3 domain containing ring finger 3 . . . unclassifiable (Anatomical System);testis;skeletal muscle; . . . . . 1390.76659 6.97706 SH3RF3-AS1 . . . SH3RF3 antisense RNA 1 . . . . . . . . . . . SH3TC1 1.08196254711814e-27 1.60121271762727e-05 0.999983987872824 SH3 domain and tetratricopeptide repeats 1 . . . ovary;colon;parathyroid;substantia nigra;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;spleen;kidney;stomach;aorta; . 0.06743 . 1.017812819 90.87638594 4345.64439 13.13144 SH3TC2 1.73290380655384e-12 0.792013074743659 0.207986925254608 SH3 domain and tetratricopeptide repeats 2 . DISEASE: Mononeuropathy of the median nerve mild (MNMN) [MIM:613353]: A disease characterized by median nerve mononeuropathy at the wrist. The clinical presentation ranges from a mild phenotype, consistent with carpal tunnel syndrome, to a severe median nerve mononeuropathy at the wrist associated with evidence of a more widespread axonal polyneuropathy. The latter phenotype is similar to that of patients with hereditary neuropathy with liability to pressure palsies. {ECO:0000269|PubMed:20220177}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Strongly expressed in brain and spinal cord. Expressed at equal level in spinal cord and sciatic nerve. Weakly expressed in striated muscle. {ECO:0000269|PubMed:14574644}.; placenta;macula lutea;blood;fovea centralis;skin;skeletal muscle;bone marrow; dorsal root ganglion;superior cervical ganglion;placenta;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13415 0.13877 0.018271026 55.22528898 877.38282 5.76827 SH3YL1 1.00024009653743e-05 0.557077352177757 0.442912645421278 SH3 and SYLF domain containing 1 . . . . . 0.26980 0.18815 0.12689526 63.00424628 60.56048 1.58169 SHANK1 0.999999760947139 2.3905286068555e-07 6.52732228484513e-19 SH3 and multiple ankyrin repeat domains 1 FUNCTION: Seems to be an adapter protein in the postsynaptic density (PSD) of excitatory synapses that interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors via complexes with GKAP/PSD-95 and Homer, respectively, and the actin-based cytoskeleton. Plays a role in the structural and functional organization of the dendritic spine and synaptic junction.; . TISSUE SPECIFICITY: Expressed in brain particularly in the amygdala, hippocampus, substantia nigra and thalamus. Isoform 2 seems to be expressed ubiquitously.; breast;frontal lobe;nervous;epididymis;brain; whole brain;amygdala;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.15019 0.10342 . . 820.42694 5.62565 SHANK2 0.999920169615752 7.98303618694895e-05 2.23789879524929e-11 SH3 and multiple ankyrin repeat domains 2 FUNCTION: Seems to be an adapter protein in the postsynaptic density (PSD) of excitatory synapses that interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors, and the actin-based cytoskeleton. May play a role in the structural and functional organization of the dendritic spine and synaptic junction.; DISEASE: Autism 17 (AUTS17) [MIM:613436]: A complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation. {ECO:0000269|PubMed:20473310}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 3 is present in epithelial colonic cells (at protein level). {ECO:0000269|PubMed:16293618, ECO:0000269|PubMed:17244609}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;testis;dura mater;brain;unclassifiable (Anatomical System);amygdala;meninges;cartilage;lens;skeletal muscle;breast;lung;pia mater;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland; amygdala;whole brain;dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.35021 . . . 1233.68596 6.63651 SHANK2-AS1 . . . SHANK2 antisense RNA 1 . . . . . . . . . . . SHANK2-AS2 . . . SHANK2 antisense RNA 2 . . . . . . . . . . . SHANK2-AS3 . . . SHANK2 antisense RNA 3 . . . frontal lobe; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.17053 . . . . . SHANK3 0.999839619981909 0.000160379993317064 2.47739080225053e-11 SH3 and multiple ankyrin repeat domains 3 FUNCTION: Major scaffold postsynaptic density protein which interacts with multiple proteins and complexes to orchestrate the dendritic spine and synapse formation, maturation and maintenance. Interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors via complexes with GKAP/PSD-95 and HOMER, respectively, and the actin-based cytoskeleton. Plays a role in the structural and functional organization of the dendritic spine and synaptic junction through the interaction with Arp2/3 and WAVE1 complex as well as the promotion of the F-actin clusters. By way of this control of actin dynamics, participates in the regulation of developing neurons growth cone motility and the NMDA receptor-signaling. Also modulates GRIA1 exocytosis and GRM5/MGLUR5 expression and signaling to control the AMPA and metabotropic glutamate receptor- mediated synaptic transmission and plasticity. May be required at an early stage of synapse formation and be inhibited by IGF1 to promote synapse maturation. {ECO:0000269|PubMed:24132240}.; DISEASE: Note=A chromosomal aberration involving SHANK3 is found in patients with chromosome 22q13.3 deletion syndrome. Translocation t(12;22)(q24.1;q13.3) with APPL2/DIP13B. {ECO:0000269|PubMed:11431708}.; DISEASE: Note=Defects in SHANK3 are associated with neuropsychiatric disorders such as autism spectrum disorders (ASD), bipolar affective disorders and early dementia onset. ASD are characterized by impairments in reciprocal social interaction and communication as well as restricted and stereotyped patterns of interest and activities. ASD include forms with moderate to severe cognitive impairment and milder forms with higher cognitive ability (Asperger syndrome). Gene duplication is associated with hyperkinetic neuropsychiatric disorders (PubMed:24153177) such as hyperactivity, auditory overstimulation, epilepsy and bipolar affective disorders, among others. {ECO:0000269|PubMed:24153177}.; DISEASE: Phelan-McDermid syndrome (PHMDS) [MIM:606232]: A developmental disorder with variable features. Common features include neonatal hypotonia, global developmental delay, normal to accelerated growth, absent to severely delayed speech, autistic behavior, and minor dysmorphic features. {ECO:0000269|PubMed:22892527, ECO:0000269|PubMed:23758760, ECO:0000269|PubMed:24132240}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Schizophrenia 15 (SCZD15) [MIM:613950]: A complex, multifactorial psychotic disorder or group of disorders characterized by disturbances in the form and content of thought (e.g. delusions, hallucinations), in mood (e.g. inappropriate affect), in sense of self and relationship to the external world (e.g. loss of ego boundaries, withdrawal), and in behavior (e.g bizarre or apparently purposeless behavior). Although it affects emotions, it is distinguished from mood disorders in which such disturbances are primary. Similarly, there may be mild impairment of cognitive function, and it is distinguished from the dementias in which disturbed cognitive function is considered primary. Some patients manifest schizophrenic as well as bipolar disorder symptoms and are often given the diagnosis of schizoaffective disorder. {ECO:0000269|PubMed:20385823}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the cerebral cortex and the cerebellum.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;stomach; whole brain;amygdala;dorsal root ganglion;thalamus;superior cervical ganglion;cerebellum peduncles;temporal lobe;atrioventricular node;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cerebellum; 0.19798 0.11117 . . 3010.19231 10.41881 SHARPIN 0.0198873358156404 0.961765183182196 0.0183474810021634 SHANK associated RH domain interactor FUNCTION: Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. {ECO:0000269|PubMed:21455173, ECO:0000269|PubMed:21455180, ECO:0000269|PubMed:21455181}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle and placenta and at lower levels in brain, heart, colon without mucosa, thymus, spleen, kidney, liver, small intestine, lung and peripheral blood leukocytes. Up-regulated in various tumor tissues such as kidney, liver, ovary and pancreas tumors. {ECO:0000269|PubMed:20179993}.; unclassifiable (Anatomical System);meninges;medulla oblongata;lymph node;hypothalamus;muscle;colon;skin;retina;uterus;prostate;optic nerve;pia mater;lung;endometrium;thyroid;visual apparatus;testis;dura mater;germinal center;kidney;brain;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.06770 0.08336 0.108486928 61.90728946 575.56399 4.86640 SHB 0.744183629095086 0.25533369808822 0.000482672816693961 Src homology 2 domain containing adaptor protein B FUNCTION: Adapter protein which regulates several signal transduction cascades by linking activated receptors to downstream signaling components. May play a role in angiogenesis by regulating FGFR1, VEGFR2 and PDGFR signaling. May also play a role in T-cell antigen receptor/TCR signaling, interleukin-2 signaling, apoptosis and neuronal cells differentiation by mediating basic- FGF and NGF-induced signaling cascades. May also regulate IRS1 and IRS2 signaling in insulin-producing cells. {ECO:0000269|PubMed:10828022, ECO:0000269|PubMed:10837138, ECO:0000269|PubMed:12084069, ECO:0000269|PubMed:12464388, ECO:0000269|PubMed:12520086, ECO:0000269|PubMed:15026417, ECO:0000269|PubMed:15919073, ECO:0000269|PubMed:8806685, ECO:0000269|PubMed:9484780, ECO:0000269|PubMed:9751119}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9484780}.; . . 0.32011 0.12113 . . 230.15239 3.27914 SHBG 0.000188842387449784 0.897001377483344 0.102809780129207 sex hormone-binding globulin FUNCTION: Functions as an androgen transport protein, but may also be involved in receptor mediated processes. Each dimer binds one molecule of steroid. Specific for 5-alpha-dihydrotestosterone, testosterone, and 17-beta-estradiol. Regulates the plasma metabolic clearance rate of steroid hormones by controlling their plasma concentration.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are present in liver and testis.; optic nerve;lung;macula lutea;testis;fovea centralis;choroid;lens;retina; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;temporal lobe;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05349 0.08112 0.130533008 63.35810333 235.27173 3.31425 SHC1 0.341634863000658 0.657759321404084 0.000605815595258128 SHC (Src homology 2 domain containing) transforming protein 1 FUNCTION: Signaling adapter that couples activated growth factor receptors to signaling pathways. Participates in a signaling cascade initiated by activated KIT and KITLG/SCF. Isoform p46Shc and isoform p52Shc, once phosphorylated, couple activated receptor tyrosine kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p46Shc and isoform p52Shc may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span (By similarity). Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis. {ECO:0000250, ECO:0000269|PubMed:14665640}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in neural stem cells but absent in mature neurons.; . . 0.70620 0.83002 -0.179930907 40.35739561 940.76033 5.94706 SHC1P1 . . . SHC (Src homology 2 domain containing) transforming protein 1 pseudogene 1 . . . . . . . . . . . SHC1P2 . . . SHC (Src homology 2 domain containing) transforming protein 1 pseudogene 2 . . . . . . . . . . . SHC2 1.22486237905385e-05 0.82540469879717 0.17458305257904 SHC (Src homology 2 domain containing) transforming protein 2 FUNCTION: Signaling adapter that couples activated growth factor receptors to signaling pathway in neurons. Involved in the signal transduction pathways of neurotrophin-activated Trk receptors in cortical neurons (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain. Expressed at high level in the hypothalamus and at low level in the caudate nucleus. {ECO:0000269|PubMed:9507002}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;whole body;lung;placenta;macula lutea;testis;spleen;brain;mammary gland;stomach; trigeminal ganglion;cingulate cortex; 0.08532 0.24544 . . 370.25994 4.06359 SHC3 0.457668718698201 0.542082743300493 0.000248538001305868 SHC (Src homology 2 domain containing) transforming protein 3 FUNCTION: Signaling adapter that couples activated growth factor receptors to signaling pathway in neurons. Involved in the signal transduction pathways of neurotrophin-activated Trk receptors in cortical neurons.; . TISSUE SPECIFICITY: Mainly expressed in brain. Hardly detectable in other tissues, except in pancreas. Highly expressed in the cerebral cortex, frontal and temporal lobes, occipital pole, hippocampus, caudate nucleus and amygdala. Expressed at low level in the cerebellum, medulla and spinal cord. {ECO:0000269|PubMed:8808684}.; . . 0.46399 0.15334 0.086440867 60.47416844 110.12139 2.28104 SHC4 1.16969936608024e-05 0.988149866275175 0.0118384367311641 SHC (Src homology 2 domain containing) family member 4 FUNCTION: Activates both Ras-dependent and Ras-independent migratory pathways in melanomas. Contributes to the early phases of agrin-induced tyrosine phosphorylation of CHRNB1. {ECO:0000269|PubMed:17409413}.; . TISSUE SPECIFICITY: Only expressed in melanomas. Weakly expressed in normal melanocytes and benign nevi. Highly expressed at the transition from radial growth phase to vertical growth phase and metastatic melanomas, when tumor cells acquire migratory competence and invasive potential. {ECO:0000269|PubMed:17409413}.; unclassifiable (Anatomical System);cartilage;ovary;heart;hypothalamus;salivary gland;sympathetic chain;intestine;pharynx;colon;blood;skin;retina;uterus;whole body;lung;frontal lobe;cochlea;cornea;visual apparatus;liver;testis;kidney;brain;mammary gland;aorta; ciliary ganglion;atrioventricular node; 0.29902 0.12806 -0.709045403 14.673272 251.32202 3.41544 SHCBP1 5.5265911035503e-06 0.967035372952495 0.0329591004564015 SHC SH2-domain binding protein 1 FUNCTION: May play a role in signaling pathways governing cellular proliferation, cell growth and differentiation. May be a component of a novel signaling pathway downstream of Shc. Acts as a positive regulator of FGF signaling in neural progenitor cells (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;ovary;blood;skeletal muscle;greater omentum;uterus;whole body;lung;bone;liver;testis;cervix;germinal center;kidney;brain; superior cervical ganglion;atrioventricular node; 0.33129 0.09957 -0.488577883 22.64685067 50.3598 1.39495 SHCBP1L 7.09410137011176e-10 0.134527150046424 0.865472849244166 SHC SH2-domain binding protein 1-like . . TISSUE SPECIFICITY: Highly expressed in the testis. {ECO:0000269|PubMed:11318611}.; unclassifiable (Anatomical System);lung;hippocampus;testis; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion; 0.11475 . 0.354632714 74.58126917 747.67858 5.42516 SHD 5.1849696454898e-06 0.421892261457914 0.578102553572441 Src homology 2 domain containing transforming protein D FUNCTION: May function as an adapter protein. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;muscle;colon;parathyroid;fovea centralis;choroid;lens;retina;bile duct;optic nerve;lung;placenta;macula lutea;visual apparatus;testis;brain;stomach; superior cervical ganglion;pons;atrioventricular node; 0.23939 0.25284 0.154398214 64.73814579 4782.50684 14.02583 SHE 0.721620118578427 0.278254023405498 0.000125858016074387 Src homology 2 domain containing E . . . unclassifiable (Anatomical System);smooth muscle;heart;cartilage;skin;skeletal muscle;uterus;lung;endometrium;placenta;thyroid;bone;liver;testis;spleen; superior cervical ganglion; 0.06952 0.12569 -0.203796826 38.81811748 61.44239 1.59738 SHF 0.0280832658607613 0.960766392650513 0.0111503414887254 Src homology 2 domain containing F FUNCTION: Adapter protein which may play a role in the regulation of apoptosis in response to PDGF. {ECO:0000269|PubMed:11095946}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, brain, liver, prostate, testis, ovary, small intestine and colon. {ECO:0000269|PubMed:11095946}.; unclassifiable (Anatomical System);ovary;heart;salivary gland;sympathetic chain;intestine;pharynx;colon;blood;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;macula lutea;visual apparatus;liver;testis;kidney;brain;bladder;cerebellum; superior cervical ganglion;cerebellum peduncles;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.19355 0.14411 0.088260113 60.56853031 755.63117 5.45002 SHFM1 0.418592332178749 0.54660864111083 0.0347990267104209 split hand/foot malformation (ectrodactyly) type 1 FUNCTION: Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis (PubMed:15117943). Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, DSS1, and either centrin CETN2 or CETN3 (PubMed:22307388). The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. Binds and stabilizes BRCA2 and is thus involved in the control of R-loop-associated DNA damage and thus transcription- associated genomic instability. R-loop accumulation increases in DSS1-depleted cells. {ECO:0000269|PubMed:15117943, ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:24896180}.; . TISSUE SPECIFICITY: Expressed in limb bud, craniofacial primordia and skin.; myocardium;lymphoreticular;medulla oblongata;ovary;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;tongue;pharynx;blood;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.40146 0.23984 0.013025609 54.62962963 0.78872 0.01490 SHFM1P1 . . . split hand/foot malformation (ectrodactyly) type 1 pseudogene 1 . . . . . . . . . . . SHFM2 . . . split hand/foot malformation (ectrodactyly) type 2 . . . . . . . . . . . SHFM5 . . . split hand/foot malformation (ectrodactyly) type 5 . . . . . . . . . . . SHH 0.912961328200915 0.0864108251942839 0.000627846604800884 sonic hedgehog FUNCTION: Intercellular signal essential for a variety of patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior- posterior axis of the developing limb bud. Displays both floor plate- and motor neuron-inducing activity. The threshold concentration of N-product required for motor neuron induction is 5-fold lower than that required for floor plate induction. Activates the transcription of target genes by interacting with its receptor PTCH1 to prevent normal inhibition by PTCH1 on the constitutive signaling activity of SMO (By similarity). {ECO:0000250, ECO:0000269|PubMed:10753901}.; DISEASE: Microphthalmia, isolated, with coloboma, 5 (MCOPCB5) [MIM:611638]: A disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues. Ocular abnormalities like opacities of the cornea and lens, scaring of the retina and choroid, and other abnormalities may also be present. Ocular colobomas are a set of malformations resulting from abnormal morphogenesis of the optic cup and stalk, and the fusion of the fetal fissure (optic fissure). {ECO:0000269|PubMed:12503095}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Holoprosencephaly 3 (HPE3) [MIM:142945]: A structural anomaly of the brain, in which the developing forebrain fails to correctly separate into right and left hemispheres. Holoprosencephaly is genetically heterogeneous and associated with several distinct facies and phenotypic variability. The majority of holoprosencephaly type 3 cases are apparently sporadic, although clear examples of autosomal dominant inheritance have been described. {ECO:0000269|PubMed:10441331, ECO:0000269|PubMed:10556296, ECO:0000269|PubMed:11479728, ECO:0000269|PubMed:15107988, ECO:0000269|PubMed:15221788, ECO:0000269|PubMed:15942952, ECO:0000269|PubMed:15942953, ECO:0000269|PubMed:17001669, ECO:0000269|PubMed:19603532, ECO:0000269|PubMed:8896572, ECO:0000269|PubMed:9302262}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Solitary median maxillary central incisor (SMMCI) [MIM:147250]: Rare dental anomaly characterized by the congenital absence of one maxillary central incisor. {ECO:0000269|PubMed:11471164, ECO:0000269|PubMed:15103725}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Triphalangeal thumb-polysyndactyly syndrome (TPTPS) [MIM:174500]: Autosomal dominant syndrome. It is characterized by a wide spectrum of pre- and post-axial abnormalities due to altered SHH expression pattern during limb development. {ECO:0000269|PubMed:12837695, ECO:0000269|PubMed:18417549}. Note=The gene represented in this entry is involved in disease pathogenesis. Mutations located in intron 5 of LMBR1 disrupt a long-range, cis-regulatory element of SHH expression.; DISEASE: Preaxial polydactyly 2 (PPD2) [MIM:174500]: Polydactyly consists of duplication of the distal phalanx. The thumb in PPD2 is usually opposable and possesses a normal metacarpal. {ECO:0000269|PubMed:12837695}. Note=The gene represented in this entry is involved in disease pathogenesis. Mutations located in intron 5 of LMBR1 disrupt a long-range, cis-regulatory element of SHH and result in abnormal, ectopic SHH expression with pathological consequences (PubMed:12837695). {ECO:0000269|PubMed:12837695}.; DISEASE: Hypoplasia or aplasia of tibia with polydactyly (THYP) [MIM:188740]: An autosomal dominant disease characterized by hypoplastic or absent tibia, and polydactyly. {ECO:0000269|PubMed:19847792, ECO:0000269|PubMed:24965254}. Note=The gene represented in this entry is involved in disease pathogenesis. Mutations located in intron 5 of LMBR1 disrupt a long-range, cis-regulatory element of SHH and result in abnormal, ectopic SHH expression with pathological consequences. {ECO:0000303|PubMed:19847792, ECO:0000303|PubMed:24965254}.; DISEASE: Laurin-Sandrow syndrome (LSS) [MIM:135750]: A rare autosomal dominant disorder characterized by polysyndactyly of hands and/or feet, mirror image duplication of the feet, nasal defects, and loss of identity between fibula and tibia. Some patients do not have nasal abnormalities (segmental Laurin-Sandrow syndrome). {ECO:0000269|PubMed:24456159}. Note=The gene represented in this entry is involved in disease pathogenesis. Abnormal SHH limb expression with pathological consequences is caused by duplications (16-75 kb) involving the ZPA regulatory sequence (ZRS), a SHH long-range cis-regulatory element, located in LMBR1 intron 5 (PubMed:24456159).; TISSUE SPECIFICITY: Expressed in fetal intestine, liver, lung, and kidney. Not expressed in adult tissues.; brain; testis - interstitial;superior cervical ganglion;testis; 0.49106 0.89143 . . 20.18395 0.69050 SHISA2 0.404087524363213 0.557503271001836 0.0384092046349509 shisa family member 2 FUNCTION: Plays an essential role in the maturation of presomitic mesoderm cells by individual attenuation of both FGF and WNT signaling. {ECO:0000250}.; . . unclassifiable (Anatomical System);larynx; . 0.39780 0.10893 . . 1189.34167 6.54035 SHISA3 0.000449561639995539 0.423960007119064 0.57559043124094 shisa family member 3 FUNCTION: Plays an essential role in the maturation of presomitic mesoderm cells by individual attenuation of both FGF and WNT signaling. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;salivary gland;developmental;adrenal cortex;intestine;pharynx;colon;blood;uterus;prostate;whole body;lung;endometrium;visual apparatus;liver;testis;kidney;brain;bladder;aorta; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.17644 . -0.405853867 26.23260203 1584.1848 7.36230 SHISA4 0.00107148238892978 0.605254729041609 0.393673788569461 shisa family member 4 . . . ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;thyroid;bone;testis;pineal gland;bladder;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;hippocampus;kidney;stomach;peripheral nerve;cerebellum; amygdala;superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.18911 . 0.569646743 81.88841708 33.47745 1.03268 SHISA5 9.94272259623573e-08 0.0950029067979488 0.904996993774825 shisa family member 5 FUNCTION: Can induce apoptosis in a caspase-dependent manner and plays a role in p53/TP53-dependent apoptosis. {ECO:0000269|PubMed:12135983}.; . . lymphoreticular;smooth muscle;ovary;umbilical cord;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;urinary;pharynx;blood;lens;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;oesophagus;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;duodenum;kidney;stomach;aorta;thymus; . 0.13400 0.09610 -0.203796826 38.81811748 45.73833 1.29956 SHISA6 . . . shisa family member 6 . . TISSUE SPECIFICITY: Expressed in the developing ventral mesencephalon. {ECO:0000269|PubMed:16473350}.; . . . . 0.569646743 81.88841708 121.97942 2.40519 SHISA7 . . . shisa family member 7 . . . . . . . . . 18.53211 0.64106 SHISA8 . . . shisa family member 8 . . . . . . . . . . . SHISA9 . . . shisa family member 9 FUNCTION: Regulator of short-term neuronal synaptic plasticity in the dentate gyrus. Associates with AMPA receptors (ionotropic glutamate receptors) in synaptic spines and promotes AMPA receptor desensitization at excitatory synapses (By similarity). {ECO:0000250}.; . . . . . . . . 70.24125 1.74086 SHKBP1 0.000346950937358068 0.999190520321505 0.000462528741136495 SH3KBP1 binding protein 1 FUNCTION: Inhibits CBL-SH3KBP1 complex mediated down-regulation of EGFR signaling by sequestration of SH3KBP1. Binds to SH3KBP1 and prevents its interaction with CBL and inhibits translocation of SH3KBP1 to EGFR containing vesicles upon EGF stimulation. {ECO:0000250|UniProtKB:Q6P7W2}.; . . lymphoreticular;medulla oblongata;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; . 0.27389 0.11314 -1.172055164 6.027364945 112.33876 2.30551 SHMT1 1.86116477095909e-07 0.658960394030564 0.341039419852959 serine hydroxymethyltransferase 1 (soluble) FUNCTION: Interconversion of serine and glycine (PubMed:8505317, PubMed:24698160). {ECO:0000269|PubMed:24698160, ECO:0000269|PubMed:8505317}.; . . lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;pharynx;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;kidney;stomach; adipose tissue;liver;kidney; 0.82380 0.38836 0.220536484 68.38287332 986.92433 6.05672 SHMT1P1 . . . serine hydroxymethyltransferase 1 (soluble) pseudogene 1 . . . . . . . . . . . SHMT2 0.00748753462073037 0.991846328846509 0.000666136532760743 serine hydroxymethyltransferase 2 FUNCTION: Contributes to the de novo mitochondrial thymidylate biosynthesis pathway via its role in glycine and tetrahydrofolate metabolism. Thymidylate biosynthesis is required to prevent uracil accumulation in mtDNA (PubMed:21876188). Interconversion of serine and glycine (PubMed:25619277). Associates with mitochondrial DNA (PubMed:18063578). Plays a role in the deubiquitination of target proteins as component of the BRISC complex (PubMed:24075985). Required for IFNAR1 deubiquitination by the BRISC complex (PubMed:24075985). {ECO:0000269|PubMed:18063578, ECO:0000269|PubMed:21876188, ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:25619277}.; . . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;hypothalamus;muscle;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; lung;smooth muscle;heart;placenta;liver;tumor;white blood cells;kidney;trigeminal ganglion;skeletal muscle; 0.17922 0.39461 -0.113792788 45.25831564 257.84598 3.45462 SHOC2 0.991705191552454 0.00829295945769003 1.84898985615785e-06 SHOC2 leucine-rich repeat scaffold protein FUNCTION: Regulatory subunit of protein phosphatase 1 (PP1c) that acts as a M-Ras/MRAS effector and participates in MAPK pathway activation. Upon M-Ras/MRAS activation, targets PP1c to specifically dephosphorylate the 'Ser-259' inhibitory site of RAF1 kinase and stimulate RAF1 activity at specialized signaling complexes. {ECO:0000269|PubMed:10783161, ECO:0000269|PubMed:16630891, ECO:0000269|PubMed:25137548}.; DISEASE: Noonan syndrome-like disorder with loose anagen hair (NSLH) [MIM:607721]: A syndrome characterized by Noonan dysmorphic features such as macrocephaly, high forehead, hypertelorism, palpebral ptosis, low-set and posteriorly rotated ears, short and webbed neck, pectus anomalies, in association with pluckable, sparse, thin and slow-growing hair. {ECO:0000269|PubMed:19684605, ECO:0000269|PubMed:25137548}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;testis;trigeminal ganglion; 0.46401 0.24608 -0.183570861 39.95046001 30.58108 0.97282 SHOX 0.738457610429217 0.259044115978608 0.00249827359217486 short stature homeobox FUNCTION: Controls fundamental aspects of growth and development.; DISEASE: Leri-Weill dyschondrosteosis (LWD) [MIM:127300]: Dominantly inherited skeletal dysplasia characterized by moderate short stature predominantly because of short mesomelic limb segments. It is often associated with the Madelung deformity of the wrist, comprising bowing of the radius and dorsal dislocation of the distal ulna. {ECO:0000269|PubMed:11030412, ECO:0000269|PubMed:11403039}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Langer mesomelic dysplasia (LMD) [MIM:249700]: Autosomal recessive rare skeletal dysplasia characterized by severe short stature owing to shortening and maldevelopment of the mesomelic and rhizomelic segments of the limbs. Associated malformations are rarely reported and intellect is normal in all affected subjects reported to date. {ECO:0000269|PubMed:11889214}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Short stature, idiopathic, X-linked (ISS) [MIM:300582]: A condition defined by a standing height more than 2 standard deviations below the mean (or below the 2.5 percentile) for sex and chronological age, compared with a well-nourished, genetically relevant population, in the absence of specific causative disorders. {ECO:0000269|PubMed:9140395}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: SHOXA is expressed in skeletal muscle, placenta, pancreas, heart and bone marrow fibroblast and SHOXB is highly expressed in bone marrow fibroblast followed by kidney and skeletal muscle. SHOXB is not expressed in brain, kidney, liver and lung. Highly expressed in osteogenic cells.; . . 0.10149 . . . 12.63351 0.46157 SHOX2 0.0852112280919416 0.905107645063688 0.00968112684437028 short stature homeobox 2 FUNCTION: May be a growth regulator and have a role in specifying neural systems involved in processing somatosensory information, as well as in face and body structure formation.; . TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, liver, lung, bone marrow fibroblast, pancreas and placenta.; unclassifiable (Anatomical System);uterus;whole body;heart;testis;skin; superior cervical ganglion;testis - interstitial;thalamus;subthalamic nucleus;globus pallidus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.83131 0.12971 -0.405853867 26.23260203 17.09768 0.60161 SHPK 3.97287394987282e-06 0.823230279355171 0.176765747770879 sedoheptulokinase FUNCTION: Acts as a modulator of macrophage activation through control of glucose metabolism. {ECO:0000250}.; . TISSUE SPECIFICITY: Strongly expressed in liver, kidney and pancreas. Expressed at lower levels in placenta and heart. Very weakly expressed in lung and brain. {ECO:0000269|PubMed:10673275}.; unclassifiable (Anatomical System);lymph node;ovary;muscle;colon;choroid;skin;retina;bone marrow;bile duct;optic nerve;whole body;lung;epididymis;bone;placenta;visual apparatus;liver;testis;spleen;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;liver;prefrontal cortex;ciliary ganglion;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.10355 . -0.398573136 26.92852088 4213.22339 12.91324 SHPRH 0.491308215820232 0.508691784175292 4.4762503007662e-12 SNF2 histone linker PHD RING helicase FUNCTION: E3 ubiquitin-protein ligase involved in DNA repair. Upon genotoxic stress, accepts ubiquitin from the UBE2N-UBE2V2 E2 complex and transfers it to 'Lys-164' of PCNA which had been monoubiquitinated by UBE2A/B-RAD18, promoting the formation of non-canonical poly-ubiquitin chains linked through 'Lys-63'. {ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:17130289, ECO:0000269|PubMed:18719106}.; . TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:12837266}.; unclassifiable (Anatomical System);heart;islets of Langerhans;colon;skin;skeletal muscle;uterus;prostate;whole body;lung;adrenal gland;nasopharynx;liver;testis;cervix;kidney;brain;aorta;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin;cerebellum; 0.13185 0.10634 -1.056370776 7.578438311 331.48456 3.87204 SHQ1 1.16644798453142e-10 0.303733901295762 0.696266098587593 SHQ1, H/ACA ribonucleoprotein assembly factor FUNCTION: Required for the quantitative accumulation of H/ACA ribonucleoproteins (RNPs), including telomerase, probably through the stabilization of DKC1, from the time of its synthesis until its association with NOP10, NHP2, and NAF1 at the nascent H/ACA RNA. {ECO:0000269|PubMed:19383767}.; . . ovary;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;testis;bladder;brain;unclassifiable (Anatomical System);heart;urinary;blood;skeletal muscle;breast;pancreas;lung;placenta;head and neck;kidney;stomach; superior cervical ganglion;medulla oblongata;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.10835 . 0.887394731 89.18966737 436.29681 4.35563 SHQ1P1 . . . SHQ1, H/ACA ribonucleoprotein assembly factor pseudogene 1 . . . . . . . . . . . SHROOM1 0.00959554880204162 0.979356255967487 0.0110481952304713 shroom family member 1 FUNCTION: May be involved in the assembly of microtubule arrays during cell elongation. {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;prostate;islets of Langerhans;placenta;testis;colon;skin;stomach;cerebellum; . 0.09495 0.08873 -1.241834664 5.414012739 602.46739 4.96767 SHROOM2 0.00694500211668264 0.989409364331527 0.0036456335517901 shroom family member 2 FUNCTION: May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Abundant in retina and melanoma; also in brain, placenta, lung, kidney and pancreas.; . . 0.13460 0.13889 1.532223403 95.53550366 330.12615 3.86122 SHROOM2P1 . . . shroom family member 2 pseudogene 1 . . . . . . . . . . . SHROOM3 0.732358844454904 0.267641147852377 7.69271814559397e-09 shroom family member 3 FUNCTION: Controls cell shape changes in the neuroepithelium during neural tube closure. Induces apical constriction in epithelial cells by promoting the apical accumulation of F-actin and myosin II, and probably by bundling stress fibers. Induces apicobasal cell elongation by redistributing gamma-tubulin and directing the assembly of robust apicobasal microtubule arrays (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pineal body;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;liver;cervix;head and neck;spleen;kidney;mammary gland;stomach; . 0.25209 0.10029 1.401769777 94.7334277 6067.86635 16.25743 SHROOM4 0.997425924732999 0.00257405379788978 2.1469111364059e-08 shroom family member 4 FUNCTION: Probable regulator of cytoskeletal architecture that plays an important role in development. May regulate cellular and cytoskeletal architecture by modulating the spatial distribution of myosin II (By similarity). {ECO:0000250, ECO:0000269|PubMed:16684770}.; DISEASE: Note=A chromosomal aberration involving SHROOM4 is a cause of X-linked mental retardation (XLMR). Translocation t(X;8)(p11.22;p23.3) with FBXO25.; DISEASE: Note=A chromosomal aberration involving SHROOM4 is a cause of X-linked mental retardation (XLMR). Translocation t(X;19).; TISSUE SPECIFICITY: Expressed in all fetal and adult tissues investigated. Expressed in adult heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. In brain regions detected in cerebellum, cerebral cortex, medulla, spinal cord, occipital pole, frontal lobe, temporal lobe and putamen. The expression is strongest in the medulla and weakest in the cerebral cortex. {ECO:0000269|PubMed:16249884}.; lung;liver;colon;amniotic fluid;spleen;blood;brain;skeletal muscle;stomach;bone marrow; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14234 0.08265 1.074712704 91.71384761 709.91072 5.29321 SHTN1 . . . shootin 1 FUNCTION: Involved in the generation of internal asymmetric signals required for neuronal polarization and neurite outgrowth. Mediates netrin-1-induced F-actin-substrate coupling or 'clutch engagement' within the axon growth cone through activation of CDC42, RAC1 and PAK1-dependent signaling pathway, thereby converting the F-actin retrograde flow into traction forces, concomitantly with filopodium extension and axon outgrowth. Plays a role in cytoskeletal organization by regulating the subcellular localization of phosphoinositide 3-kinase (PI3K) activity at the axonal growth cone. Plays also a role in regenerative neurite outgrowth. In the developing cortex, cooperates with KIF20B to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. Involved in the accumulation of phosphatidylinositol 3,4,5- trisphosphate (PIP3) in the growth cone of primary hippocampal neurons. {ECO:0000250|UniProtKB:A0MZ67, ECO:0000250|UniProtKB:Q8K2Q9}.; . . . . 0.14058 0.08683 -0.449946534 24.00330267 . . SI 7.97067187590746e-26 0.864647709603944 0.135352290396056 sucrase-isomaltase (alpha-glucosidase) FUNCTION: Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides. {ECO:0000269|PubMed:20356844}.; DISEASE: Congenital sucrase-isomaltase deficiency (CSID) [MIM:222900]: Autosomal recessive intestinal disorder that is clinically characterized by fermentative diarrhea, abdominal pain, and cramps upon ingestion of sugar. The symptoms are the consequence of absent or drastically reduced enzymatic activities of sucrase and isomaltase. The prevalence of CSID is 0.02 % in individuals of European descent and appears to be much higher in Greenland, Alaskan, and Canadian native people. CSID arises due to post-translational perturbations in the intracellular transport, polarized sorting, aberrant processing, and defective function of SI. {ECO:0000269|PubMed:10903344, ECO:0000269|PubMed:11340066, ECO:0000269|PubMed:14724820, ECO:0000269|PubMed:16329100, ECO:0000269|PubMed:8609217}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the poorly differentiated crypt cells of the small intestine as well as in the mature villous cells. Expressed at very low levels in the colon. {ECO:0000269|PubMed:1677636}.; unclassifiable (Anatomical System);lung;small intestine;testis;colon;skeletal muscle; superior cervical ganglion;testis;trigeminal ganglion; 0.07211 0.17154 0.666787636 84.61901392 2753.13216 9.89427 SIAE 2.58571955397209e-09 0.269022542385991 0.730977455028289 sialic acid acetylesterase FUNCTION: Catalyzes the removal of O-acetyl ester groups from position 9 of the parent sialic acid, N-acetylneuraminic acid.; . TISSUE SPECIFICITY: Widely expressed with high expression in the testis, prostate, and colon. {ECO:0000269|PubMed:15292578}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;thyroid;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;lens;skeletal muscle;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;testis - seminiferous tubule;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14724 0.19452 0.378498378 75.58386412 1278.04735 6.73067 SIAH1 0.949054584763539 0.0507827257157662 0.000162689520694273 siah E3 ubiquitin protein ligase 1 FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (ELL2, MYB, POU2AF1, PML and RBBP8), a cell surface receptor (DCC), the cell-surface receptor-type tyrosine kinase FLT3, the cytoplasmic signal transduction molecules (KLF10/TIEG1 and NUMB), an antiapoptotic protein (BAG1), a microtubule motor protein (KIF22), a protein involved in synaptic vesicle function in neurons (SYP), a structural protein (CTNNB1) and SNCAIP. Confers constitutive instability to HIPK2 through proteasomal degradation. It is thereby involved in many cellular processes such as apoptosis, tumor suppression, cell cycle, axon guidance, transcription regulation, spermatogenesis and TNF-alpha signaling. Has some overlapping function with SIAH2. Induces apoptosis in cooperation with PEG3. Upon nitric oxid (NO) generation that follows apoptotic stimulation, interacts with S- nitrosylated GAPDH, mediating the translocation of GAPDH to the nucleus. GAPDH acts as a stabilizer of SIAH1, facilitating the degradation of nuclear proteins. {ECO:0000269|PubMed:10747903, ECO:0000269|PubMed:11146551, ECO:0000269|PubMed:11389839, ECO:0000269|PubMed:11389840, ECO:0000269|PubMed:11483517, ECO:0000269|PubMed:11483518, ECO:0000269|PubMed:11752454, ECO:0000269|PubMed:12072443, ECO:0000269|PubMed:14506261, ECO:0000269|PubMed:14645235, ECO:0000269|PubMed:14654780, ECO:0000269|PubMed:15064394, ECO:0000269|PubMed:16085652, ECO:0000269|PubMed:18536714, ECO:0000269|PubMed:19224863, ECO:0000269|PubMed:20508617, ECO:0000269|PubMed:22483617, ECO:0000269|PubMed:9334332, ECO:0000269|PubMed:9858595}.; . TISSUE SPECIFICITY: Widely expressed at a low level. Down- regulated in advanced hepatocellular carcinomas. {ECO:0000269|PubMed:12557228, ECO:0000269|PubMed:9403064}.; smooth muscle;ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;breast;pancreas;lung;epididymis;trabecular meshwork;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;stomach;aorta; superior cervical ganglion;fetal brain;placenta;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.92718 . 0.125076652 62.7388535 48.27472 1.35381 SIAH1P1 . . . siah E3 ubiquitin protein ligase 1 pseudogene 1 . . . . . . . . . . . SIAH2 0.360182186098013 0.588194102532641 0.0516237113693458 siah E3 ubiquitin protein ligase 2 FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (POU2AF1, PML, NCOR1), a cell surface receptor (DCC), an antiapoptotic protein (BAG1), and a protein involved in synaptic vesicle function in neurons (SYP). Mediates ubiquitination and proteasomal degradation of DYRK2 in response to hypoxia. It is thereby involved in apoptosis, tumor suppression, cell cycle, transcription and signaling processes. Has some overlapping function with SIAH1. Triggers the ubiquitin-mediated degradation of TRAF2, whereas SIAH1 can not. Promotes monoubiquitination of SNCA. {ECO:0000269|PubMed:11483518, ECO:0000269|PubMed:12411493, ECO:0000269|PubMed:19224863, ECO:0000269|PubMed:22878263, ECO:0000269|PubMed:9334332}.; . TISSUE SPECIFICITY: Widely expressed at low level. {ECO:0000269|PubMed:9403064}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;nervous;islets of Langerhans;blood;lens;breast;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;mammary gland;stomach;thymus; whole brain;fetal liver;adrenal gland;placenta;adrenal cortex;white blood cells;bone marrow; 0.38551 0.20297 -0.163345027 41.24793583 259.68398 3.46250 SIAH2-AS1 . . . SIAH2 antisense RNA 1 . . . . . . . . . . . SIAH3 0.00183208051769324 0.481709457596771 0.516458461885536 siah E3 ubiquitin protein ligase family member 3 FUNCTION: Negative regulator of PARK2 translocation to damaged mitochondria. Acts probably by destabilizing PINK1 protein, hence inhibiting PARK2 targeting to dysfunctional depolarized mitochondria. {ECO:0000269|PubMed:24270810}.; . . . . . . -0.383807564 27.41802312 33.52965 1.03550 SIDT1 5.02880784411406e-13 0.532578591972566 0.467421408026931 SID1 transmembrane family member 1 . . . lymph node;islets of Langerhans;hypothalamus;colon;blood;skeletal muscle;breast;prostate;whole body;endometrium;liver;spleen;germinal center;mammary gland;stomach; superior cervical ganglion;atrioventricular node; 0.21346 0.12002 -0.922264439 9.778249587 1760.28141 7.74525 SIDT1-AS1 . . . SIDT1 antisense RNA 1 . . . . . . . . . . . SIDT2 0.00257240105871232 0.997422349853205 5.24908808258801e-06 SID1 transmembrane family member 2 . . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; prostate; 0.45816 . -0.036738982 50.53668318 375.6269 4.08572 SIGIRR 0.00530888875886403 0.969475617648661 0.0252154935924748 single immunoglobulin and toll-interleukin 1 receptor (TIR) domain FUNCTION: Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Attenuates the recruitment of receptor-proximal signaling components to the TLR4 receptor, probably through an TIR-TIR domain interaction with TLR4. Through its extracellular domain interferes with the heterodimerization of Il1R1 and IL1RAP. {ECO:0000269|PubMed:12925853, ECO:0000269|PubMed:14715412, ECO:0000269|PubMed:15866876, ECO:0000269|PubMed:25963006}.; . TISSUE SPECIFICITY: Mainly expressed in epithelial tissues such as kidney, lung and gut. {ECO:0000269|PubMed:14715412, ECO:0000269|PubMed:21077278}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;bone;iris;testis;brain;unclassifiable (Anatomical System);urinary;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;aorta; superior cervical ganglion;liver;white blood cells;kidney;trigeminal ganglion; 0.11433 0.12086 0.064394823 58.84642604 125.38641 2.43699 SIGLEC1 1.62408118412598e-28 0.000268024937746567 0.999731975062253 sialic acid binding Ig like lectin 1 FUNCTION: Acts as an endocytic receptor mediating clathrin dependent endocytosis. Macrophage-restricted adhesion molecule that mediates sialic-acid dependent binding to lymphocytes, including granulocytes, monocytes, natural killer cells, B-cells and CD8 T-cells. Preferentially binds to alpha-2,3-linked sialic acid (By similarity). Binds to SPN/CD43 on T-cells (By similarity). May play a role in hemopoiesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed by macrophages in various tissues. High levels are found in spleen, lymph node, perivascular macrophages in brain and lower levels in bone marrow, liver Kupffer cells and lamina propria of colon and lung. Also expressed by inflammatory macrophages in rheumatoid arthritis.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;thyroid;bone;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;blood;lens;pancreas;lung;pia mater;placenta;macula lutea;liver;alveolus;spleen;cervix;kidney; superior cervical ganglion;lymph node;placenta;pons; 0.11347 0.20825 -1.81038272 2.188016042 766.76722 5.48599 SIGLEC5 7.61333709335823e-05 0.918669676637401 0.081254189991665 sialic acid binding Ig like lectin 5 FUNCTION: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.; . TISSUE SPECIFICITY: Expressed by monocytic/myeloid lineage cells. Found at high levels in peripheral blood leukocytes, spleen, bone marrow and at lower levels in lymph node, lung, appendix, placenta, pancreas and thymus. Expressed by monocytes and neutrophils but absent from leukemic cell lines representing early stages of myelomonocytic differentiation.; unclassifiable (Anatomical System);lung;blood;germinal center;brain;bone marrow; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;bone marrow; 0.02667 0.06874 0.554869705 81.59943383 1747.05185 7.71365 SIGLEC6 0.024724478649233 0.961850592369541 0.0134249289812257 sialic acid binding Ig like lectin 6 FUNCTION: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.; . TISSUE SPECIFICITY: Expressed at high levels in placenta (cyto- and syncytiotrophoblastic cells) and at lower levels in spleen, peripheral blood leukocytes (predominantly B-cells) and small intestine.; unclassifiable (Anatomical System);ovary;placenta;parathyroid;aorta; dorsal root ganglion;superior cervical ganglion;placenta;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle;cerebellum; 0.05124 0.07099 1.510221359 95.4470394 801.47957 5.57886 SIGLEC7 8.9311366832357e-06 0.768847672791926 0.231143396071391 sialic acid binding Ig like lectin 7 FUNCTION: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- and alpha-2,6-linked sialic acid. Also binds disialogangliosides (disialogalactosyl globoside, disialyl lactotetraosylceramide and disialyl GalNAc lactotetraoslylceramide). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Mediates inhibition of natural killer cells cytotoxicity. May play a role in hemopoiesis. Inhibits differentiation of CD34+ cell precursors towards myelomonocytic cell lineage and proliferation of leukemic myeloid cells (in vitro). {ECO:0000269|PubMed:10611343}.; . TISSUE SPECIFICITY: Predominantly expressed by resting and activated natural killer cells and at lower levels by granulocytes and monocytes. High expression found in placenta, liver, lung, spleen, and peripheral blood leukocytes.; unclassifiable (Anatomical System);lymph node;lung;endometrium;placenta;liver;testis;spleen;choroid;brain;gall bladder; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04525 . -0.600630256 18.06440198 41.04459 1.20242 SIGLEC8 0.000488762401895089 0.967922145689096 0.0315890919090088 sialic acid binding Ig like lectin 8 FUNCTION: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- linked sialic acid. Also binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.; . TISSUE SPECIFICITY: Expressed specifically on eosinophils.; lung;frontal lobe;nasopharynx;spleen;brain;skeletal muscle; . 0.20849 . 0.600782551 82.82613824 2588.50286 9.51476 SIGLEC9 0.0003283348922794 0.816853876486105 0.182817788621616 sialic acid binding Ig like lectin 9 FUNCTION: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- or alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.; . TISSUE SPECIFICITY: Expressed by peripheral blood leukocytes (neutrophils and monocytes but not eosinophils). Found in liver, fetal liver, bone marrow, placenta, spleen and in lower levels in skeletal muscle, fetal brain, stomach, lung, thymus, prostate, brain, mammary, adrenal gland, colon, trachea, cerebellum, testis, small intestine and spinal cordon.; unclassifiable (Anatomical System);pancreas;lung;nasopharynx;bone;testis;brain;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.06326 0.07947 1.089464986 91.87308327 502.15704 4.59711 SIGLEC10 4.05540868320963e-06 0.98900983089231 0.0109861136990066 sialic acid binding Ig like lectin 10 FUNCTION: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- or alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules.; . TISSUE SPECIFICITY: Expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation). Isoform 5 is found to be the most abundant isoform. Found in lymph node, lung, ovary and appendix. Isoform 1 is found at high levels and isoform 2 at lower levels in bone marrow, spleen and spinal chord. Isoform 2 is also found in brain. Isoform 4 is specifically found in natural killer cells.; unclassifiable (Anatomical System);ovary;tongue;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;skin;bone marrow;breast;prostate;lung;larynx;visual apparatus;liver;spleen;head and neck;kidney;brain;bladder;tonsil; atrioventricular node;pons;skeletal muscle; 0.08166 0.08125 -0.238793231 36.3116301 3256.10289 10.86662 SIGLEC11 2.64293930264503e-08 0.478412852452464 0.521587121118143 sialic acid binding Ig like lectin 11 FUNCTION: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,8- linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules.; . TISSUE SPECIFICITY: Expressed by macrophages in various tissues including Kupffer cells. Also found in brain microglia.; . . 0.07542 0.08273 0.846940207 88.47605567 1686.30736 7.57044 SIGLEC12 1.54311758491148e-10 0.197090501670817 0.802909498174871 sialic acid binding Ig like lectin 12 (gene/pseudogene) FUNCTION: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.; . TISSUE SPECIFICITY: Isoform Short is highly expressed in spleen, small intestine and adrenal gland; it is lower expressed in thyroid, placenta, brain, stomach, bone marrow, spinal chord and breast. Isoform Long is highly expressed in spleen, small intestine and bone marrow; it is lower expressed in thyroid, placenta, thymus, trachea, stomach, lung, adrenal gland, fetal brain and testis.; unclassifiable (Anatomical System);liver; superior cervical ganglion; 0.06344 . 2.337125365 98.40174569 3066.99793 10.53027 SIGLEC14 0.0356627411821091 0.928369101135508 0.0359681576823829 sialic acid binding Ig like lectin 14 FUNCTION: Putative adhesion molecule. Sialic acid-binding paired receptor which may activate associated receptors. {ECO:0000269|PubMed:17012248}.; . TISSUE SPECIFICITY: Mainly expressed in hematopoietic tissues including bone marrow, spleen and fetal liver. Also detected in lung and testis. {ECO:0000269|PubMed:17012248}.; unclassifiable (Anatomical System);lung;placenta;blood;bone marrow; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;bone marrow; 0.05859 . . . 53.12482 1.44638 SIGLEC15 1.08177312684363e-11 0.0032607982491434 0.996739201740039 sialic acid binding Ig like lectin 15 FUNCTION: Binds sialylated glycoproteins. {ECO:0000269|PubMed:17483134}.; . TISSUE SPECIFICITY: Expressed in macrophage and/or dendritic cells of spleen and lymph nodes.; . . 0.15667 . . . 2662.45225 9.70140 SIGLEC16 . . . sialic acid binding Ig like lectin 16 (gene/pseudogene) FUNCTION: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in bone marrow, fetal brain, fetal liver, lung and salivary gland. Detected in brain, macrophage, cancerous esophagus and lung at protein level. {ECO:0000269|PubMed:18629938}.; . . 0.05488 . . . . . SIGLEC17P . . . sialic acid binding Ig like lectin 17, pseudogene . . . . . 0.02249 . . . . . SIGLEC18P . . . sialic acid binding Ig like lectin 18, pseudogene . . . . . . . . . . . SIGLEC20P . . . sialic acid binding Ig like lectin 20, pseudogene . . . . . . . . . . . SIGLEC21P . . . sialic acid binding Ig like lectin 21, pseudogene . . . . . . . . . . . SIGLEC22P . . . sialic acid binding Ig like lectin 22, pseudogene . . . . . . . . . . . SIGLEC24P . . . sialic acid binding Ig like lectin 24, pseudogene . . . . . . . . . . . SIGLEC25P . . . sialic acid binding Ig like lectin 25, pseudogene . . . . . . . . . . . SIGLEC26P . . . sialic acid binding Ig like lectin 26, pseudogene . . . . . . . . . . . SIGLEC27P . . . sialic acid binding Ig like lectin 27, pseudogene . . . . . . . . . . . SIGLEC28P . . . sialic acid binding Ig like lectin 28, pseudogene . . . . . . . . . . . SIGLEC29P . . . sialic acid binding Ig like lectin 29, pseudogene . . . . . . . . . . . SIGLEC30P . . . sialic acid binding Ig like lectin 30, pseudogene . . . . . . . . . . . SIGLEC31P . . . sialic acid binding Ig like lectin 31, pseudogene . . . . . . . . . . . SIGLECL1 0.00033234714417744 0.592889555143791 0.406778097712031 SIGLEC family like 1 . . . . . . . 0.038710339 56.92380278 8.78383 0.32400 SIGMAR1 0.125068129498213 0.780053546129155 0.0948783243726317 sigma non-opioid intracellular receptor 1 FUNCTION: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (PubMed:16472803, PubMed:9341151). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000269|PubMed:16472803, ECO:0000269|PubMed:9341151}.; DISEASE: Distal spinal muscular atrophy, autosomal recessive, 2 (DSMA2) [MIM:605726]: An autosomal recessive neuromuscular disorder characterized by onset of distal muscle weakness and wasting affecting the lower and upper limbs in the first decade. There is no sensory involvement. {ECO:0000269|PubMed:26078401}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed with higher expression in liver, colon, prostate, placenta, small intestine, heart and pancreas. Expressed in the retina by retinal pigment epithelial cells. Expressed in alpha-motor neurons (PubMed:23314020). {ECO:0000269|PubMed:11687279, ECO:0000269|PubMed:23314020, ECO:0000269|PubMed:8954936, ECO:0000269|PubMed:9341151}.; lymphoreticular;myocardium;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;iris;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; subthalamic nucleus;superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.55678 0.22085 0.080983847 59.76055674 2236.60547 8.72030 SIK1 0.993830465042737 0.00616935350588741 1.81451375759768e-07 salt inducible kinase 1 FUNCTION: Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, gluconeogenesis and lipogenesis regulation, muscle growth and differentiation and tumor suppression. Phosphorylates HDAC4, HDAC5, PPME1, SREBF1, CRTC1/TORC1 and CRTC2/TORC2. Acts as a tumor suppressor and plays a key role in p53/TP53-dependent anoikis, a type of apoptosis triggered by cell detachment: required for phosphorylation of p53/TP53 in response to loss of adhesion and is able to suppress metastasis. Part of a sodium-sensing signaling network, probably by mediating phosphorylation of PPME1: following increases in intracellular sodium, SIK1 is activated by CaMK1 and phosphorylates PPME1 subunit of protein phosphatase 2A (PP2A), leading to dephosphorylation of sodium/potassium-transporting ATPase ATP1A1 and subsequent increase activity of ATP1A1. Acts as a regulator of muscle cells by phosphorylating and inhibiting class II histone deacetylases HDAC4 and HDAC5, leading to promote expression of MEF2 target genes in myocytes. Also required during cardiomyogenesis by regulating the exit of cardiomyoblasts from the cell cycle via down-regulation of CDKN1C/p57Kip2. Acts as a regulator of hepatic gluconeogenesis by phosphorylating and repressing the CREB-specific coactivators CRTC1/TORC1 and CRTC2/TORC2, leading to inhibit CREB activity. Also regulates hepatic lipogenesis by phosphorylating and inhibiting SREBF1. In concert with CRTC1/TORC1, regulates the light-induced entrainment of the circadian clock by attenuating PER1 induction; represses CREB-mediated transcription of PER1 by phosphorylating and deactivating CRTC1/TORC1 (By similarity). {ECO:0000250|UniProtKB:Q60670, ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:16306228, ECO:0000269|PubMed:18348280, ECO:0000269|PubMed:19622832}.; DISEASE: Epileptic encephalopathy, early infantile, 30 (EIEE30) [MIM:616341]: A form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. {ECO:0000269|PubMed:25839329}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in SIK1 may be associated with some cancers, such as breast cancers. Loss of SIK1 correlates with poor patient outcome in breast cancers (PubMed:19622832). {ECO:0000269|PubMed:19622832}.; . colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;gum;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;duodenum;hypopharynx;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;adrenal cortex;skin; 0.21011 0.20814 -0.262657925 34.93158764 1292.6128 6.76849 SIK2 0.99983680888605 0.000163191108720057 5.2296074003978e-12 salt inducible kinase 2 FUNCTION: Phosphorylates 'Ser-794' of IRS1 in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction. Inhibits CREB activity by phosphorylating and repressing TORCs, the CREB-specific coactivators. {ECO:0000269|PubMed:15454081}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;liver;duodenum;spleen;kidney;mammary gland;stomach; prefrontal cortex; 0.26605 0.17210 -0.418800956 25.79028073 43.02086 1.24421 SIK3 0.999882540750175 0.000117459249350113 4.74977381554428e-13 SIK family kinase 3 . . . ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;thymus;cerebellum; amygdala;whole brain;superior cervical ganglion;testis - interstitial;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;pons;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;cingulate cortex;parietal lobe;cerebellum; . . -0.992035476 8.604623732 . . SIK3-IT1 . . . SIK3 intronic transcript 1 . . . . . . . . . . . SIKE1 0.0729823085203998 0.872381771521014 0.0546359199585864 suppressor of IKBKE 1 FUNCTION: Physiological suppressor of IKK-epsilon and TBK1 that plays an inhibitory role in virus- and TLR3-triggered IRF3. Inhibits TLR3-mediated activation of interferon-stimulated response elements (ISRE) and the IFN-beta promoter. May act by disrupting the interactions of IKBKE or TBK1 with TICAM1/TRIF, IRF3 and DDX58/RIG-I. Does not inhibit NF-kappa-B activation pathways. {ECO:0000269|PubMed:16281057}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and leukocytes. Present in all cell lines tested (at protein level). {ECO:0000269|PubMed:16281057}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;heart;colon;parathyroid;blood;skin;skeletal muscle;retina;breast;uterus;prostate;whole body;lung;frontal lobe;bone;placenta;liver;testis;germinal center;kidney;brain;mammary gland;aorta;thymus; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . . -0.229483771 36.86010852 10.26874 0.37478 SIL1 0.000933875133307504 0.941470258953966 0.057595865912726 SIL1 nucleotide exchange factor FUNCTION: Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone HSPA5. {ECO:0000269|PubMed:12356756}.; DISEASE: Marinesco-Sjoegren syndrome (MSS) [MIM:248800]: Autosomal recessive multisystem disorder which is characterized by cerebellar ataxia due to cerebellar atrophy, with Purkinje and granule cell loss and myopathy featuring marked muscle replacement with fat and connective tissue. Other cardinal features include bilateral cataracts, hypergonadotrophic hypogonadism and mild to severe mental retardation. Skeletal abnormalities, short stature, dysarthria, strabismus and nystagmus are also frequent findings. Mutational inactivation of this protein may result in ER stress- induced cell death signaling or malfunctioning chaperone machineries that mishandle client proteins which are critical for the organs targeted in MSS. {ECO:0000269|PubMed:16282977, ECO:0000269|PubMed:16282978}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in tissues which produce large amounts of secreted proteins such as kidney, liver and placenta. Also expressed in colon, heart, lung, ovary, pancreas, peripheral leukocyte, prostate, spleen and thymus. Expressed at low levels throughout the brain. {ECO:0000269|PubMed:12356756, ECO:0000269|PubMed:16282978}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; prostate;testis - interstitial;lung;adrenal gland;placenta;thyroid;beta cell islets;liver;testis; 0.06865 0.50289 0.42259095 77.22929936 356.07352 3.99397 SIM1 0.99693618254279 0.00306381081261866 6.64459118091292e-09 single-minded family bHLH transcription factor 1 FUNCTION: Transcriptional factor that may have pleiotropic effects during embryogenesis and in the adult.; . . unclassifiable (Anatomical System);pancreas;islets of Langerhans;liver;kidney; uterus corpus;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;skeletal muscle; 0.86069 0.17145 -0.821100135 11.88369899 2822.33817 10.01958 SIM2 0.178825368644501 0.820642349089636 0.00053228226586248 single-minded family bHLH transcription factor 2 FUNCTION: Transcription factor that may be a master gene of CNS development in cooperation with Arnt. It may have pleiotropic effects in the tissues expressed during development.; . . unclassifiable (Anatomical System);uterus;lung;ovary;bone;testis;colon;cervix;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;tongue;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.36242 0.24747 -0.198338176 39.17197452 2208.64464 8.65301 SIMC1 0.000207486981163 0.907420865519901 0.0923716474989363 SUMO interacting motifs containing 1 . . . . . 0.11144 0.08199 -0.580403979 18.58928993 498.88864 4.58624 SIN3A 0.99999994122779 5.87722101743002e-08 5.22815417619428e-19 SIN3 transcription regulator family member A FUNCTION: Acts as a transcriptional repressor. Corepressor for REST. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Also interacts with MXD1-MAX heterodimers to repress transcription by tethering SIN3A to DNA. Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation. Involved in he control of the circadian rhythms. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation. {ECO:0000269|PubMed:12150998}.; . . ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;synovium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;tongue;muscle;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.92468 0.37170 -1.392555112 4.269874971 88.8785 2.02409 SIN3B 0.992239405222561 0.00776059214246463 2.63497394166178e-09 SIN3 transcription regulator family member B FUNCTION: Acts as a transcriptional repressor. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer then represses transcription by tethering SIN3B to DNA. Also forms a complex with FOXK1 which represses transcription (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum;thymus; amygdala;superior cervical ganglion;prefrontal cortex;globus pallidus;testis;trigeminal ganglion; 0.33817 0.11722 -1.366884746 4.505779665 113.01186 2.31383 SIPA1 0.0279051429893718 0.971621353159705 0.000473503850922689 signal-induced proliferation-associated 1 FUNCTION: GTPase activator for the nuclear Ras-related regulatory proteins Rap1 and Rap2 in vitro, converting it to the putatively inactive GDP-bound state. {ECO:0000269|PubMed:9346962}.; . TISSUE SPECIFICITY: Expressed in fetal as well as in adult tissues. Expressed abundantly in the lymphoid tissues such as thymus, spleen and peripheral blood lymphocytes and also shows a significant expression in the spinal cord.; . . 0.17185 0.10668 -0.08446956 47.15145081 1245.34692 6.66733 SIPA1L1 0.999999774320167 2.2567983352702e-07 1.14796258597314e-19 signal-induced proliferation-associated 1 like 1 FUNCTION: Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F- actin. Contributes to the regulation of dendritic spine morphogenesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9858596}.; ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;urinary;pharynx;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; amygdala;subthalamic nucleus;occipital lobe;prefrontal cortex;globus pallidus;caudate nucleus; 0.53561 0.11441 -2.73449852 0.701816466 229.73804 3.27537 SIPA1L2 0.999219705697118 0.000780294302865291 1.62442084657396e-14 signal-induced proliferation-associated 1 like 2 . . . lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;vein;skin;retina;uterus;optic nerve;frontal lobe;cochlea;endometrium;cerebral cortex;larynx;thyroid;bone;testis;amniotic fluid;spinal ganglion;pineal gland;bladder;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;hypothalamus;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;head and neck;kidney;stomach;peripheral nerve; dorsal root ganglion;occipital lobe;superior cervical ganglion;medulla oblongata;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.23513 . -1.308377521 4.865534324 2579.80412 9.49692 SIPA1L3 0.999676985877316 0.000323014122455094 2.28626679458788e-13 signal-induced proliferation-associated 1 like 3 FUNCTION: Plays a critical role in epithelial cell morphogenesis, polarity, adhesion and cytoskeletal organization in the lens (PubMed:26231217). {ECO:0000269|PubMed:26231217}.; DISEASE: Note=A chromosomal translocation involving SIPA1L3 is found in a patient with bilateral severe ocular abnormalities including congenital cataracts, corneal clouding, iridocorneal and lenticular adhesions and microphthalmia. Chromosomal translocation t(2;19)(q37.3;q13.1). In addition to translocation, missense variant has been found in patient with bilateral congenital cataracts (PubMed:26231217). {ECO:0000269|PubMed:26231217}.; . ovary;adrenal medulla;colon;parathyroid;skin;bone marrow;uterus;prostate;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;small intestine;islets of Langerhans;urinary;blood;lens;skeletal muscle;bile duct;breast;lung;liver;spleen;kidney;stomach; superior cervical ganglion;cerebellum; 0.48936 0.10963 -1.61360557 2.954706299 1728.944 7.67448 SIRPA 0.137720810094911 0.858013148191033 0.00426604171405659 signal regulatory protein alpha FUNCTION: Immunoglobulin-like cell surface receptor for CD47. Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular signaling during synaptogenesis and in synaptic function (By similarity). Involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin. Mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. {ECO:0000250, ECO:0000269|PubMed:10469599, ECO:0000269|PubMed:11509594}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain. Detected on myeloid cells, but not T-cells. Detected at lower levels in heart, placenta, lung, testis, ovary, colon, liver, small intestine, prostate, spleen, kidney, skeletal muscle and pancreas.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;bladder;brain;amygdala;heart;cartilage;nervous;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;oesophagus;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;pancreas;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;cerebellum; subthalamic nucleus;occipital lobe;medulla oblongata;prefrontal cortex;globus pallidus;pons;parietal lobe;cingulate cortex; 0.15954 . -0.775187015 13.05142722 9703.80737 21.35988 SIRPAP1 . . . signal regulatory protein alpha pseudogene 1 . . . . . . . . . . . SIRPB1 2.22163067811888e-09 0.0384757595029116 0.961524238275458 signal regulatory protein beta 1 FUNCTION: Immunoglobulin-like cell surface receptor involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. Participates also in the recruitment of tyrosine kinase SYK.; . TISSUE SPECIFICITY: Detected in monocytes and dendritic cells. {ECO:0000269|PubMed:10604985}.; unclassifiable (Anatomical System);amygdala;lung;cartilage;testis;blood;brain;stomach;retina;bone marrow; superior cervical ganglion;heart;ciliary ganglion;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle; 0.09596 0.09430 3.223205135 99.36305732 57.03185 1.52012 SIRPB2 0.0145880945141627 0.873498571987165 0.111913333498672 signal regulatory protein beta 2 . . . unclassifiable (Anatomical System);lung;endometrium;larynx;head and neck; superior cervical ganglion;globus pallidus;trigeminal ganglion; 0.14220 0.08706 1.0178651 90.91766926 302.20382 3.70263 SIRPB3P . . . signal regulatory protein beta 3, pseudogene . . . . . . . . . . . SIRPD 7.78200741287581e-05 0.312509299561532 0.687412880364339 signal regulatory protein delta . . . . . 0.07237 . 0.062575634 58.74026893 44.24105 1.26793 SIRPG 5.20922689402416e-08 0.123435578889256 0.876564369018475 signal regulatory protein gamma FUNCTION: Probable immunoglobulin-like cell surface receptor. On binding with CD47, mediates cell-cell adhesion. Engagement on T- cells by CD47 on antigen-presenting cells results in enhanced antigen-specific T-cell proliferation and costimulates T-cell activation. {ECO:0000269|PubMed:15383453}.; . TISSUE SPECIFICITY: Detected in liver, and at very low levels in brain, heart, lung, pancreas, kidney, placenta and skeletal muscle. Expressed on CD4+ T-cells, CD8+ T-cells, CD56-bright natural killer (NK) cells, CD20+ cells, and all activated NK cells. Mainly present in the paracortical T-cell area of lymph nodes, with only sparse positive cells in the mantle and in the germinal center of B-cell follicles. In the thymus, primarily expressed in the medulla on mature T-lymphocytes that have undergone thymic selection. {ECO:0000269|PubMed:11185750, ECO:0000269|PubMed:15383453}.; unclassifiable (Anatomical System);lung;ovary;nasopharynx;testis;kidney; superior cervical ganglion;skeletal muscle; 0.07604 0.08642 0.801024817 87.65628686 56.86072 1.51823 SIRPG-AS1 . . . SIRPG antisense RNA 1 . . . . . . . . . . . SIRT1 0.951787840736877 0.0482063158070068 5.84345611596061e-06 sirtuin 1 FUNCTION: NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metobolism, apoptosis and autophagy. Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression. Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively. Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction. Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Deacetylates 'Lys-266' of SUV39H1, leading to its activation. Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. Deacetylates H2A and 'Lys-26' of HIST1H1E. Deacetylates 'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression. Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting. Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1. Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2. This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response. Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence. Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability. Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation. Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis. Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing. Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha. Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1. Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver. Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation. Involved in HES1- and HEY2-mediated transcriptional repression. In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62'. Deacetylates MEF2D. Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3. Represses HNF1A- mediated transcription. Required for the repression of ESRRG by CREBZF. Modulates AP-1 transcription factor activity. Deacetylates NR1H3 AND NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteosomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed. Involved in lipid metabolism. Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2. Deacetylates ACSS2 leading to its activation, and HMGCS1. Involved in liver and muscle metabolism. Through deacteylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletel muscle under low-glucose conditions and is involved in glucose homeostasis. Involved in regulation of PPARA and fatty acid beta-oxidation in liver. Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2. Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression. Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and faciliting recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2. Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN. Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling. Transcriptional suppression of TP73 probably involves E2F4 and PCAF. Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage. Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1. Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8. Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation. Proposed to play role in regulation of STK11/LBK1- dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear. In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation. Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation. Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability. Deacteylates MECOM/EVI1. Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization. During the neurogenic transition, repress selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation. Regulates the circadian expression of several core clock genes, including ARNTL/BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling. Deacetylates ARNTL/BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator. Deacetylates PER2, facilitating its ubiquitination and degradation by the proteosome. Protects cardiomyocytes against palmitate-induced apoptosis (PubMed:11672523, PubMed:12006491, PubMed:14976264, PubMed:14980222, PubMed:15126506, PubMed:15152190, PubMed:15205477, PubMed:15469825, PubMed:15692560, PubMed:16079181, PubMed:16166628, PubMed:16892051, PubMed:16998810, PubMed:17283066, PubMed:17334224, PubMed:17505061, PubMed:17612497, PubMed:17620057, PubMed:17936707, PubMed:18203716, PubMed:18296641, PubMed:18662546, PubMed:18687677, PubMed:19188449, PubMed:19220062, PubMed:19364925, PubMed:19690166, PubMed:19934257, PubMed:20097625, PubMed:20100829, PubMed:20203304, PubMed:20375098, PubMed:20620956, PubMed:20670893, PubMed:20817729, PubMed:21149730, PubMed:21245319, PubMed:21471201, PubMed:21504832, PubMed:21555002, PubMed:21698133, PubMed:21701047, PubMed:21775285, PubMed:21807113, PubMed:21841822, PubMed:21890893, PubMed:21909281, PubMed:21947282, PubMed:22274616). Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity (PubMed:20955178). Involved in the CCAR2- mediated regulation of PCK1 and NR1D1 (PubMed:24415752). Deacetylates CTNB1 at 'Lys-49' (PubMed:24824780). In POMC (pro- opiomelanocortin) neurons, required for leptin-induced activation of PI3K signaling (By similarity). {ECO:0000250|UniProtKB:Q923E4, ECO:0000269|PubMed:11672523, ECO:0000269|PubMed:12006491, ECO:0000269|PubMed:14976264, ECO:0000269|PubMed:14980222, ECO:0000269|PubMed:15126506, ECO:0000269|PubMed:15152190, ECO:0000269|PubMed:15205477, ECO:0000269|PubMed:15469825, ECO:0000269|PubMed:15692560, ECO:0000269|PubMed:16079181, ECO:0000269|PubMed:16166628, ECO:0000269|PubMed:16892051, ECO:0000269|PubMed:16998810, ECO:0000269|PubMed:17283066, ECO:0000269|PubMed:17290224, ECO:0000269|PubMed:17334224, ECO:0000269|PubMed:17505061, ECO:0000269|PubMed:17612497, ECO:0000269|PubMed:17620057, ECO:0000269|PubMed:17936707, ECO:0000269|PubMed:18203716, ECO:0000269|PubMed:18296641, ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:18687677, ECO:0000269|PubMed:19188449, ECO:0000269|PubMed:19220062, ECO:0000269|PubMed:19364925, ECO:0000269|PubMed:19690166, ECO:0000269|PubMed:19934257, ECO:0000269|PubMed:20097625, ECO:0000269|PubMed:20100829, ECO:0000269|PubMed:20203304, ECO:0000269|PubMed:20375098, ECO:0000269|PubMed:20620956, ECO:0000269|PubMed:20670893, ECO:0000269|PubMed:20817729, ECO:0000269|PubMed:20955178, ECO:0000269|PubMed:21149730, ECO:0000269|PubMed:21245319, ECO:0000269|PubMed:21471201, ECO:0000269|PubMed:21504832, ECO:0000269|PubMed:21555002, ECO:0000269|PubMed:21698133, ECO:0000269|PubMed:21701047, ECO:0000269|PubMed:21775285, ECO:0000269|PubMed:21807113, ECO:0000269|PubMed:21841822, ECO:0000269|PubMed:21890893, ECO:0000269|PubMed:21909281, ECO:0000269|PubMed:21947282, ECO:0000269|PubMed:22274616, ECO:0000269|PubMed:24415752, ECO:0000269|PubMed:24824780}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, interacts with and deacetylates the viral Tat protein. The viral Tat protein inhibits SIRT1 deacetylation activity toward RELA/NF- kappa-B p65, thereby potentiates its transcriptional activity and SIRT1 is proposed to contribute to T-cell hyperactivation during infection. {ECO:0000269|PubMed:18329615}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10381378}.; medulla oblongata;ovary;salivary gland;colon;skin;uterus;prostate;whole body;cochlea;endometrium;bone;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;cervix;kidney;mammary gland;aorta;thymus; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion; 0.92235 0.62242 0.196671391 67.19155461 82.60166 1.93096 SIRT1-AS . . . SIRT1 antisense RNA . . . . . . . . . . . SIRT2 1.0819075859999e-05 0.941777740658523 0.0582114402656173 sirtuin 2 FUNCTION: NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors. Participates in the modulation of multiple and diverse biological processes such as cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metabolic networks, and autophagy. Plays a major role in the control of cell cycle progression and genomic stability. Functions in the antephase checkpoint preventing precocious mitotic entry in response to microtubule stress agents, and hence allowing proper inheritance of chromosomes. Positively regulates the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity by deacetylating CDC20 and FZR1, then allowing progression through mitosis. Associates both with chromatin at transcriptional start sites (TSSs) and enhancers of active genes. Plays a role in cell cycle and chromatin compaction through epigenetic modulation of the regulation of histone H4 'Lys-20' methylation (H4K20me1) during early mitosis. Specifically deacetylates histone H4 at 'Lys-16' (H4K16ac) between the G2/M transition and metaphase enabling H4K20me1 deposition by SETD8 leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle, and mitotic S-phase progression. Deacetylates SETD8 modulating SETD8 chromatin localization during the mitotic stress response. Deacetylates also histone H3 at 'Lys- 57' (H3K56ac) during the mitotic G2/M transition. Upon bacterium Listeria monocytogenes infection, deacetylates 'Lys-18' of histone H3 in a receptor tyrosine kinase MET- and PI3K/Akt-dependent manner, thereby inhibiting transcriptional activity and promoting late stages of listeria infection. During oocyte meiosis progression, may deacetylate histone H4 at 'Lys-16' (H4K16ac) and alpha-tubulin, regulating spindle assembly and chromosome alignment by influencing microtubule dynamics and kinetochore function. Deacetylates alpha-tubulin at 'Lys-40' and hence controls neuronal motility, oligodendroglial cell arbor projection processes and proliferation of non-neuronal cells. Phosphorylation at Ser-368 by a G1/S-specific cyclin E-CDK2 complex inactivates SIRT2-mediated alpha-tubulin deacetylation, negatively regulating cell adhesion, cell migration and neurite outgrowth during neuronal differentiation. Deacetylates PARD3 and participates in the regulation of Schwann cell peripheral myelination formation during early postnatal development and during postinjury remyelination. Involved in several cellular metabolic pathways. Plays a role in the regulation of blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in response to low nutrient availability. Acts as a key regulator in the pentose phosphate pathway (PPP) by deacetylating and activating the glucose-6-phosphate G6PD enzyme, and therefore, stimulates the production of cytosolic NADPH to counteract oxidative damage. Maintains energy homeostasis in response to nutrient deprivation as well as energy expenditure by inhibiting adipogenesis and promoting lipolysis. Attenuates adipocyte differentiation by deacetylating and promoting FOXO1 interaction to PPARG and subsequent repression of PPARG-dependent transcriptional activity. Plays a role in the regulation of lysosome-mediated degradation of protein aggregates by autophagy in neuronal cells. Deacetylates FOXO1 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1- mediated autophagy. Deacetylates a broad range of transcription factors and co-regulators regulating target gene expression. Deacetylates transcriptional factor FOXO3 stimulating the ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and degradation. Deacetylates HIF1A and therefore promotes HIF1A degradation and inhibition of HIF1A transcriptional activity in tumor cells in response to hypoxia. Deacetylates RELA in the cytoplasm inhibiting NF-kappaB-dependent transcription activation upon TNF-alpha stimulation. Inhibits transcriptional activation by deacetylating p53/TP53 and EP300. Deacetylates also EIF5A. Functions as a negative regulator on oxidative stress-tolerance in response to anoxia-reoxygenation conditions. Plays a role as tumor suppressor.; FUNCTION: Isoform 2: Deacetylates EP300, alpha-tubulin and histone H3 and H4.; . TISSUE SPECIFICITY: Isoform 1 is expressed in heart, liver and skeletal muscle, weakly expressed in the cortex. Isoform 2 is strongly expressed in the cortex, weakly expressed in heart and liver. Weakly expressed in several malignancies including breast, liver, brain, kidney and prostate cancers compared to normal tissues. Weakly expressed in glioma cell lines compared to normal brain tissues (at protein level). Widely expressed. Highly expressed in heart, brain and skeletal muscle, while it is weakly expressed in placenta and lung. Down-regulated in many gliomas suggesting that it may act as a tumor suppressor gene in human gliomas possibly through the regulation of microtubule network. {ECO:0000269|PubMed:10381378, ECO:0000269|PubMed:10393250, ECO:0000269|PubMed:12963026, ECO:0000269|PubMed:16909107, ECO:0000269|PubMed:21791548, ECO:0000269|PubMed:22014574}.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;iris;germinal center;brain;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;greater omentum;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;kidney;stomach;aorta;cerebellum; superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;spinal cord;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;globus pallidus;cingulate cortex;parietal lobe; 0.31120 0.33703 0.020302773 55.60863411 166.65453 2.82044 SIRT3 2.70051653943508e-05 0.531332953455666 0.468640041378939 sirtuin 3 FUNCTION: NAD-dependent protein deacetylase. Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues. Known targets include ACSS1, IDH, GDH, SOD2, PDHA1, LCAD, SDHA and the ATP synthase subunit ATP5O. Contributes to the regulation of the cellular energy metabolism. Important for regulating tissue-specific ATP levels. {ECO:0000269|PubMed:16788062, ECO:0000269|PubMed:18680753, ECO:0000269|PubMed:18794531, ECO:0000269|PubMed:19535340, ECO:0000269|PubMed:24121500, ECO:0000269|PubMed:24252090}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10381378, ECO:0000269|PubMed:12374852}.; . . 0.08093 0.13388 0.486911049 79.46449634 970.41965 6.02104 SIRT4 1.80676632025049e-07 0.0708692595517169 0.929130559771651 sirtuin 4 FUNCTION: Acts as NAD-dependent protein lipoamidase, ADP-ribosyl transferase and deacetylase. Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications. Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner (PubMed:25525879). Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity. Acts as a negative regulator of mitochondrial glutamine metabolism by mediating mono ADP- ribosylation of GLUD1: expressed in response to DNA damage and negatively regulates anaplerosis by inhibiting GLUD1, leading to block metabolism of glutamine into tricarboxylic acid cycle and promoting cell cycle arrest (PubMed:16959573, PubMed:17715127). In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation. Acts as a tumor suppressor (PubMed:23562301, PubMed:23663782). Also acts as a NAD- dependent protein deacetylase: mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity, thereby acting as a regulator of lipid homeostasis (By similarity). Controls fatty acid oxidation by inhibiting PPARA transcriptional activation. Impairs SIRT1:PPARA interaction probably through the regulation of NAD(+) levels (PubMed:24043310). Down-regulates insulin secretion. {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000269|PubMed:16959573, ECO:0000269|PubMed:17715127, ECO:0000269|PubMed:23562301, ECO:0000269|PubMed:23663782, ECO:0000269|PubMed:24043310, ECO:0000269|PubMed:25525879}.; . TISSUE SPECIFICITY: Detected in vascular smooth muscle and striated muscle. Detected in insulin-producing beta-cells in pancreas islets of Langerhans (at protein level). Widely expressed. Weakly expressed in leukocytes and fetal thymus. {ECO:0000269|PubMed:10381378}.; unclassifiable (Anatomical System);heart;colon;fovea centralis;choroid;lens;retina;uterus;optic nerve;lung;macula lutea;liver;testis;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.15011 . -0.091746757 46.91554612 110.65045 2.29119 SIRT5 1.87753474665446e-05 0.887241146625048 0.112740078027486 sirtuin 5 FUNCTION: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins (PubMed:21908771, PubMed:22076378, PubMed:24703693). Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting (PubMed:22076378, PubMed:24703693). Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species (PubMed:24140062). Modulates ketogenesis through the desuccinylation and activation of HMGCS2 (By similarity). Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX. {ECO:0000250|UniProtKB:Q8K2C6, ECO:0000269|PubMed:18680753, ECO:0000269|PubMed:21908771, ECO:0000269|PubMed:22076378, ECO:0000269|PubMed:24140062, ECO:0000269|PubMed:24703693}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10381378}.; unclassifiable (Anatomical System);cartilage;ovary;heart;lacrimal gland;colon;parathyroid;blood;uterus;prostate;lung;frontal lobe;endometrium;larynx;bone;thyroid;placenta;liver;testis;head and neck;spleen;germinal center;kidney;brain;stomach;thymus; superior cervical ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.13111 0.16246 0.332586472 73.61405992 466.72179 4.47531 SIRT6 0.0544711567553148 0.926067668054921 0.0194611751897637 sirtuin 6 FUNCTION: NAD-dependent protein deacetylase. Has deacetylase activity towards histone H3K9Ac and H3K56Ac. Modulates acetylation of histone H3 in telomeric chromatin during the S-phase of the cell cycle. Deacetylates histone H3K9Ac at NF-kappa-B target promoters and may down-regulate the expression of a subset of NF- kappa-B target genes. Acts as a corepressor of the transcription factor HIF1A to control the expression of multiple glycolytic genes to regulate glucose homeostasis. Required for genomic stability. Regulates the production of TNF protein. Has a role in the regulation of life span (By similarity). Deacetylation of nucleosomes interferes with RELA binding to target DNA. May be required for the association of WRN with telomeres during S-phase and for normal telomere maintenance. Required for genomic stability. Required for normal IGF1 serum levels and normal glucose homeostasis. Modulates cellular senescence and apoptosis. On DNA damage, promotes DNA end resection via deacetylation of RBBP8. Has very weak deacetylase activity and can bind NAD(+) in the absence of acetylated substrate. {ECO:0000250, ECO:0000269|PubMed:18337721, ECO:0000269|PubMed:19135889, ECO:0000269|PubMed:19625767, ECO:0000269|PubMed:20829486, ECO:0000269|PubMed:21362626}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;pharynx;blood;lens;lung;cornea;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;mammary gland;stomach; superior cervical ganglion;cerebellum; 0.19201 0.17526 0.327131069 73.27199811 119.41575 2.37785 SIRT7 0.567108371695204 0.430348704477411 0.00254292382738456 sirtuin 7 FUNCTION: NAD-dependent protein deacetylase that specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac). In contrast to other histone deacetylases, displays selectivity for a single histone mark, H3K18Ac, directly linked to control of gene expression. H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors. SIRT7 thereby acts as a transcription repressor. Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells. These data suggest that SIRT7 may play a key role in oncogenic transformation by suppresses expression of tumor suppressor genes by locus-specific deacetylation of H3K18Ac at promoter regions. Also required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis: promotes the association of RNA polymerase I with the rDNA promoter region and coding region. Stimulates transcription activity of the RNA polymerase I complex. May also deacetylate p53/TP53 and promotes cell survival, however such data need additional confirmation. {ECO:0000269|PubMed:16618798, ECO:0000269|PubMed:19174463, ECO:0000269|PubMed:22722849}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.17301 0.14089 -0.115612493 45.12856806 26.87247 0.86852 SIT1 0.0354131319355265 0.8285018036196 0.136085064444873 signaling threshold regulating transmembrane adaptor 1 FUNCTION: Negatively regulates TCR (T-cell antigen receptor)- mediated signaling in T-cells. Involved in positive selection of T-cells. {ECO:0000269|PubMed:10209036}.; . TISSUE SPECIFICITY: Specifically expressed in T- and B-cells. Present in plasma cells but not in germinal center B-cells (at protein level). Expressed in T- and B-cell lymphoma. {ECO:0000269|PubMed:10209036, ECO:0000269|PubMed:16160011}.; unclassifiable (Anatomical System);lymphoreticular;pancreas;lymph node;endometrium;colon;spleen;blood;kidney;germinal center; trigeminal ganglion;thymus; 0.14951 0.09976 0.305084559 72.22811984 56.37864 1.50911 SIVA1 0.313588965101933 0.668974586738414 0.0174364481596533 SIVA1 apoptosis inducing factor FUNCTION: Induces CD27-mediated apoptosis. Inhibits BCL2L1 isoform Bcl-x(L) anti-apoptotic activity. Inhibits activation of NF-kappa- B and promotes T-cell receptor-mediated apoptosis. {ECO:0000269|PubMed:12011449, ECO:0000269|PubMed:14739602, ECO:0000269|PubMed:15034012, ECO:0000269|PubMed:15958577, ECO:0000269|PubMed:16491128}.; . TISSUE SPECIFICITY: Ubiquitous. Mostly expressed in thymus, testis, ovary, prostate, small intestine and spleen and less in colon.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;hypothalamus;spinal cord;muscle;pharynx;blood;skeletal muscle;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;kidney;mammary gland;stomach;cerebellum; prostate;testis - interstitial;lung;testis - seminiferous tubule;heart;thyroid;liver;tumor;testis;trigeminal ganglion;skeletal muscle;thymus; 0.15757 0.15629 0.349177632 74.18023119 . . SIX1 0.92637706377143 0.0732123384605364 0.000410597768033478 SIX homeobox 1 FUNCTION: Transcription factor that is involved in the regulation of cell proliferation, apoptosis and embryonic development. Plays an important role in the development of several organs, including kidney, muscle and inner ear. Depending on context, functions as transcriptional repressor or activator. Lacks an activation domain, and requires interaction with EYA family members for transcription activation. Mediates nuclear translocation of EYA1 and EYA2. Binds the 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3 element in the MYOG promoter. Regulates the expression of numerous genes, including MYC, CCND1 and EZR. Acts as activator of the IGFBP5 promoter, probably coactivated by EYA2. Repression of precursor cell proliferation in myoblasts is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex. During myogenesis, seems to act together with EYA2 and DACH2 (By similarity). Regulates the expression of CCNA1. {ECO:0000250, ECO:0000269|PubMed:15123840, ECO:0000269|PubMed:15141091, ECO:0000269|PubMed:19497856, ECO:0000269|PubMed:23435380}.; DISEASE: Deafness, autosomal dominant, 23 (DFNA23) [MIM:605192]: A form of non-syndromic deafness characterized by prelingual, bilateral, symmetric hearing loss with a conductive component present in some but not all patients. {ECO:0000269|PubMed:15141091}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Branchiootic syndrome 3 (BOS3) [MIM:608389]: A syndrome characterized by usually bilateral branchial cleft fistulas or cysts, sensorineural and/or conductive hearing loss, pre-auricular pits, and structural defects of the outer, middle or inner ear. Otic defects include malformed and hypoplastic pinnae, a narrowed external ear canal, bulbous internal auditory canal, stapes fixation, malformed and hypoplastic cochlea. Branchial and otic anomalies overlap with those seen in individuals with the branchiootorenal syndrome. However renal anomalies are absent in branchiootic syndrome patients. {ECO:0000269|PubMed:15141091, ECO:0000269|PubMed:17637804, ECO:0000269|PubMed:18330911, ECO:0000269|PubMed:21280147}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in SIX1 could be a cause of branchiootorenal syndrome (BOR). BOR is an autosomal dominant disorder manifested by various combinations of preauricular pits, branchial fistulae or cysts, lacrimal duct stenosis, hearing loss, structural defects of the outer, middle, or inner ear, and renal dysplasia. Associated defects include asthenic habitus, long narrow facies, constricted palate, deep overbite, and myopia. Hearing loss may be due to mondini type cochlear defect and stapes fixation. Penetrance of BOR syndrome is high, although expressivity can be extremely variable. {ECO:0000305|PubMed:15141091, ECO:0000305|PubMed:19497856}.; TISSUE SPECIFICITY: Specifically expressed in skeletal muscle.; unclassifiable (Anatomical System);tongue;muscle;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;breast;prostate;optic nerve;whole body;lung;synovium;bone;macula lutea;kidney; dorsal root ganglion;testis - interstitial;prostate;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;pituitary;skeletal muscle; 0.82208 0.23521 -0.295622497 32.61972163 7.05882 0.26436 SIX2 0.870283341963573 0.12796647274495 0.00175018529147716 SIX homeobox 2 FUNCTION: Transcription factor that plays an important role in the development of several organs, including kidney, skull and stomach. During kidney development, maintains cap mesenchyme multipotent nephron progenitor cells in an undifferentiated state by opposing the inductive signals emanating from the ureteric bud and cooperates with WNT9B to promote renewing progenitor cells proliferation. Acts through its interaction with TCF7L2 and OSR1 in a canonical Wnt signaling independent manner preventing transcription of differentiation genes in cap mesenchyme such as WNT4. Also acts independently of OSR1 to activate expression of many cap mesenchyme genes, including itself, GDNF and OSR1. During craniofacial development plays a role in growth and elongation of the cranial base through regulation of chondrocyte differentiation. During stomach organogenesis, controls pyloric sphincter formation and mucosal growth through regulation of a gene network including NKX2-5, BMPR1B, BMP4, SOX9 and GREM1. During branchial arch development, acts to mediate HOXA2 control over the insulin-like growth factor pathway. Also may be involved in limb tendon and ligament development (By similarity). Plays a role in cell proliferation and migration. {ECO:0000250|UniProtKB:Q62232, ECO:0000269|PubMed:22995329}.; . TISSUE SPECIFICITY: Strongly expressed in skeletal muscle. Expressed in Wilms' tumor and in the cap mesenchyme of fetal kidney (at protein level). {ECO:0000269|PubMed:22703800}.; unclassifiable (Anatomical System);prostate;lung;endometrium;bone;muscle;cervix;kidney;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.89235 0.16296 0.060756528 58.52795471 37.06347 1.10769 SIX3 0.348879193568557 0.595442298319936 0.0556785081115071 SIX homeobox 3 FUNCTION: Transcriptional regulator which can act as both a transcriptional repressor and activator by binding a ATTA homeodomain core recognition sequence on these target genes. During forebrain development represses WNT1 expression allowing zona limitans intrathalamica formation and thereby ensuring proper anterio-posterior patterning of the diencephalon and formation of the rostral diencephalon. Acts as a direct upstream activator of SHH expression in the rostral diencephalon ventral midline and that in turn SHH maintains its expression. In addition, Six3 activity is required for the formation of the telencephalon. During postnatal stages of brain development is necessary for ependymal cell maturation by promoting the maturation of radial glia into ependymal cells through regulation of neuroblast proliferation and migration. Acts on the proliferation and differentiation of neural progenitor cells through activating transcription of CCND1 AND CCND2. During early lens formation plays a role in lens induction and specification by activating directly PAX6 in the presumptive lens ectoderm. In turn PAX6 activates SIX3 resulting in activation of PDGFRA and CCND1 promoting cell proliferation. Also is required for the neuroretina development by directly suppressing WNT8B expression in the anterior neural plate territory. Its action during retina development and lens morphogenesis is AES and TLE4-dependent manner. Furthermore, during eye development regulates several genes expression. Before and during early lens development represses the CRYGF promoter by binding a SIX repressor element. Directly activates RHO transcription, or cooperates with CRX or NRL. Six3 functions also in the formation of the proximodistal axis of the optic cup, and promotes the formation of optic vesicles-like structures. During pituitary development, acts in parallel or alternatively with HESX1 to control cell proliferation through Wnt/beta-catenin pathway (By similarity). Plays a role in eye development by suppressing WNT1 expression and in dorsal- ventral patterning by repressing BMP signaling pathway. {ECO:0000250|UniProtKB:Q62233, ECO:0000269|PubMed:18791198}.; DISEASE: Holoprosencephaly 2 (HPE2) [MIM:157170]: A structural anomaly of the brain, in which the developing forebrain fails to correctly separate into right and left hemispheres. Holoprosencephaly is genetically heterogeneous and associated with several distinct facies and phenotypic variability. {ECO:0000269|PubMed:10369266, ECO:0000269|PubMed:15221788, ECO:0000269|PubMed:15523651, ECO:0000269|PubMed:17001667, ECO:0000269|PubMed:18791198, ECO:0000269|PubMed:20531442}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Schizencephaly (SCHZC) [MIM:269160]: Extremely rare human congenital disorder characterized by a full-thickness cleft within the cerebral hemispheres. These clefts are lined with gray matter and most commonly involve the parasylvian regions. Large portions of the cerebral hemispheres may be absent and replaced by cerebro- spinal fluid. {ECO:0000269|PubMed:20157829}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);optic nerve;lung;macula lutea;visual apparatus;iris;duodenum;fovea centralis;choroid;kidney;lens;brain;retina; caudate nucleus;pons;skeletal muscle;pituitary; 0.87268 0.21837 0.058937498 58.26256192 39.09376 1.15929 SIX3-AS1 . . . SIX3 antisense RNA 1 . . . . . . . . . . . SIX4 0.685504308249748 0.313599689554923 0.000896002195329118 SIX homeobox 4 FUNCTION: Transcriptional regulator which can act as both a transcriptional repressor and activator by binding a DNA sequence on these target genes and is involved in processes like cell differentiation, cell migration and cell survival. Transactivates gene expression by binding a 5'-[CAT]A[CT][CT][CTG]GA[GAT]-3' motif present in the Trex site and a 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3 site of the muscle-specific genes enhancer. Acts cooperatively with EYA proteins to transactivate their target genes through interaction and nuclear translocation of EYA protein. Acts synergistically with SIX1 to regulate target genes involved in formation of various organs, including muscle, kidney, gonad, ganglia, olfactory epithelium and cranial skeleton. Plays a role in several important steps of muscle development. Controls the genesis of hypaxial myogenic progenitors in the dermomyotome by transactivating PAX3 and the delamination and migration of the hypaxial precursors from the ventral lip to the limb buds through the transactivation of PAX3, MET and LBX1. Controls myoblast determination by transactivating MYF5, MYOD1 and MYF6. Controls somitic differentiation in myocyte through MYOG transactivation. Plays a role in synaptogenesis and sarcomere organization by participating in myofiber specialization during embryogenesis by activating fast muscle program in the primary myotome resulting in an up-regulation of fast muscle genes, including ATP2A1, MYL1 and TNNT3. Simultaneously, is also able to activate inhibitors of slow muscle genes, such as SOX6, HRASLS, and HDAC4, thereby restricting the activation of the slow muscle genes. During muscle regeneration, negatively regulates differentiation of muscle satellite cells through down-regulation of MYOG expression. During kidney development regulates the early stages of metanephros development and ureteric bud formation through regulation of GDNF, SALL1, PAX8 and PAX2 expression. Plays a role in gonad development by regulating both testis determination and size determination. In gonadal sex determination, transactivates ZFPM2 by binding a MEF3 consensus sequence, resulting in SRY up-regulation. In gonadal size determination, transactivates NR5A1 by binding a MEF3 consensus sequence resulting in gonadal precursor cell formation regulation. During olfactory development mediates the specification and patterning of olfactory placode through fibroblast growth factor and BMP4 signaling pathways and also regulates epithelial cell proliferation during placode formation. Promotes survival of sensory neurons during early trigeminal gangliogenesis. In the developing dorsal root ganglia, up- regulates SLC12A2 transcription. Regulates early thymus/parathyroid organogenesis through regulation of GCM2 and FOXN1 expression. Forms gustatory papillae during development of the tongue. Also plays a role during embryonic cranial skeleton morphogenesis. {ECO:0000250|UniProtKB:Q61321}.; . . unclassifiable (Anatomical System);lung;colon; . 0.75035 0.12206 0.310540264 72.65864591 433.91108 4.34837 SIX5 0.310828642912358 0.671358473342735 0.0178128837449072 SIX homeobox 5 FUNCTION: Transcription factor that is thought to be involved in regulation of organogenesis. May be involved in determination and maintenance of retina formation. Binds a 5'-GGTGTCAG-3' motif present in the ARE regulatory element of ATP1A1. Binds a 5'- TCA[AG][AG]TTNC-3' motif present in the MEF3 element in the myogenin promoter, and in the IGFBP5 promoter (By similarity). Thought to be regulated by association with Dach and Eya proteins, and seems to be coactivated by EYA1, EYA2 and EYA3 (By similarity). {ECO:0000250}.; DISEASE: Branchiootorenal syndrome 2 (BOR2) [MIM:610896]: A syndrome characterized by branchial cleft fistulas or cysts, sensorineural and/or conductive hearing loss, pre-auricular pits, structural defects of the outer, middle or inner ear, and renal malformations. {ECO:0000269|PubMed:17357085}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in adult but not in fetal eyes. Found in corneal epithelium and endothelium, lens epithelium, ciliary body epithelia, cellular layers of the retina and the sclera. {ECO:0000269|PubMed:9949207}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;brain;unclassifiable (Anatomical System);islets of Langerhans;muscle;lens;pancreas;lung;placenta;visual apparatus;macula lutea;spleen;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17233 0.19078 . . 2249.68711 8.76017 SIX6 0.757754035338817 0.240242213489813 0.00200375117137035 SIX homeobox 6 FUNCTION: May be involved in eye development.; . TISSUE SPECIFICITY: Expressed in the developing and adult retina. Also expressed in the hypothalamic and the pituitary regions.; unclassifiable (Anatomical System);uterus;optic nerve;heart;macula lutea;visual apparatus;pituitary gland;fovea centralis;choroid;lens;skin;retina; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.31341 0.12485 0.681699246 84.93158764 3353.41856 11.09767 SKA1 1.32265949651803e-06 0.375156552360963 0.62484212497954 spindle and kinetochore associated complex subunit 1 FUNCTION: Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation (PubMed:17093495, PubMed:19289083, PubMed:23085020). Required for timely anaphase onset during mitosis, when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint (PubMed:17093495). The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies (PubMed:19289083). The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner (PubMed:19289083). Affinity for microtubules is synergistically enhanced in the presence of the ndc-80 complex and may allow the ndc-80 complex to track depolymerizing microtubules (PubMed:23085020). In the complex, it mediates the interaction with microtubules (PubMed:19289083, PubMed:23085020). {ECO:0000269|PubMed:17093495, ECO:0000269|PubMed:19289083, ECO:0000269|PubMed:23085020}.; . . unclassifiable (Anatomical System);lung;ovary;nasopharynx;placenta;testis; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07962 0.07802 0.260991686 70.25831564 49.22546 1.37144 SKA2 0.000501074471856632 0.445061841673288 0.554437083854856 spindle and kinetochore associated complex subunit 2 FUNCTION: Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation (PubMed:17093495, PubMed:19289083, PubMed:23085020). Required for timely anaphase onset during mitosis, when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint (PubMed:17093495). The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies (PubMed:19289083). The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner (PubMed:17093495, PubMed:19289083). In the complex, it is required for SKA1 localization (PubMed:19289083). Affinity for microtubules is synergistically enhanced in the presence of the ndc-80 complex and may allow the ndc-80 complex to track depolymerizing microtubules (PubMed:23085020). {ECO:0000269|PubMed:17093495, ECO:0000269|PubMed:19289083, ECO:0000269|PubMed:23085020}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;frontal lobe;endometrium;bone;thyroid;testis;brain;artery;bladder;unclassifiable (Anatomical System);heart;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; ciliary ganglion;atrioventricular node; 0.08771 0.08756 0.191216164 66.57230479 5.32056 0.19669 SKA2P1 . . . spindle and kinetochore associated complex subunit 2 pseudogene 1 . . . . . . . . . . . SKA3 2.99578704451869e-07 0.313173985869545 0.68682571455175 spindle and kinetochore associated complex subunit 3 FUNCTION: Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation (PubMed:19289083, PubMed:19360002, PubMed:23085020). The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies (PubMed:19289083, PubMed:19360002). The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner (PubMed:19289083). In the complex, it mediates the microtubule-stimulated oligomerization (PubMed:19289083). Affinity for microtubules is synergistically enhanced in the presence of the ndc-80 complex and may allow the ndc-80 complex to track depolymerizing microtubules (PubMed:23085020). {ECO:0000269|PubMed:19289083, ECO:0000269|PubMed:19360002, ECO:0000269|PubMed:23085020}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;adrenal cortex;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;kidney;mammary gland;stomach; superior cervical ganglion;atrioventricular node; 0.10563 0.07823 0.839664339 88.29912715 1222.59599 6.60998 SKAP1 0.000301840236150372 0.986328957742111 0.0133692020217385 src kinase associated phosphoprotein 1 FUNCTION: Positively regulates T-cell receptor signaling by enhancing the MAP kinase pathway. Required for optimal conjugation between T-cells and antigen-presenting cells by promoting the clustering of integrin ITGAL on the surface of T-cells. May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells. {ECO:0000269|PubMed:10856234, ECO:0000269|PubMed:11909961, ECO:0000269|PubMed:12652296, ECO:0000269|PubMed:15939789, ECO:0000269|PubMed:16980616}.; . TISSUE SPECIFICITY: Highly expressed in thymocytes and peripheral blood lymphocytes. Also expressed in spleen cells and testis. Present in T-cells (at protein level). {ECO:0000269|PubMed:9195899}.; unclassifiable (Anatomical System);breast;lung;liver;testis;colon;spleen;blood;kidney;spinal ganglion;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14374 0.10630 0.17280645 65.75843359 28.15835 0.90255 SKAP2 0.909797277702382 0.0901740609436501 2.86613539683708e-05 src kinase associated phosphoprotein 2 FUNCTION: May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway. {ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:9837776}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Present in platelets (at protein level). {ECO:0000269|PubMed:10942756, ECO:0000269|PubMed:9755858, ECO:0000269|PubMed:9837776}.; medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;spinal cord;urinary;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;white blood cells;atrioventricular node;trigeminal ganglion;whole blood; 0.82035 0.26241 0.17280645 65.75843359 1007.31849 6.11261 SKI 0.981402099833324 0.0185845014841333 1.33986825423255e-05 SKI proto-oncogene FUNCTION: May play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. Functions as a repressor of TGF-beta signaling. {ECO:0000269|PubMed:19049980}.; DISEASE: Shprintzen-Goldberg craniosynostosis syndrome (SGS) [MIM:182212]: A very rare syndrome characterized by a marfanoid habitus, craniosynostosis, characteristic dysmorphic facial features, skeletal and cardiovascular abnormalities, mental retardation, developmental delay and learning disabilities. {ECO:0000269|PubMed:23023332, ECO:0000269|PubMed:23103230, ECO:0000269|PubMed:24357594, ECO:0000269|PubMed:24736733}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.20786 0.15244 . . 335.72865 3.89213 SKIDA1 . . . SKI/DACH domain containing 1 . . . . . 0.89100 . . . 438.2434 4.36472 SKIL 0.459267762614766 0.54048671071434 0.000245526670893859 SKI-like proto-oncogene FUNCTION: May have regulatory role in cell division or differentiation in response to extracellular signals.; . TISSUE SPECIFICITY: Isoform SNON and isoform SNOA are widely expressed. Highest expression is found in skeletal muscle, followed by placenta and lung. Lowest expression in heart, brain and pancreas. Isoform SNOI expression is restricted to skeletal muscle. {ECO:0000269|PubMed:8233802}.; unclassifiable (Anatomical System);cartilage;ovary;parathyroid;skeletal muscle;breast;lung;larynx;placenta;bone;liver;testis;head and neck;germinal center;brain;stomach; subthalamic nucleus;ciliary ganglion; 0.79743 . -0.334253673 30.70299599 103.95442 2.20253 SKINT1L . . . Skint1 like (pseudogene) . . . . . . . . . . . SKIV2L 1.11011779473699e-15 0.963730660644036 0.0362693393559626 Ski2 like RNA helicase FUNCTION: Helicase; has ATPase activity. Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C).; DISEASE: Trichohepatoenteric syndrome 2 (THES2) [MIM:614602]: A syndrome characterized by intrauterine growth retardation, severe diarrhea in infancy requiring total parenteral nutrition, facial dysmorphism, immunodeficiency, and hair abnormalities, mostly trichorrhexis nodosa. Hepatic involvement contributes to the poor prognosis of affected patients. {ECO:0000269|PubMed:22444670}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.11827 . 0.165318022 64.9799481 2979.16369 10.35329 SKIV2L2 0.725400924600165 0.274599067097836 8.30199923198606e-09 Ski2 like RNA helicase 2 FUNCTION: May be involved in pre-mRNA splicing. Associated with the RNA exosome complex and involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA. {ECO:0000269|PubMed:17412707}.; . . ovary;skin;prostate;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;amygdala;heart;cartilage;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;choroid;uterus;whole body;oesophagus;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach; superior cervical ganglion;testis - interstitial;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.57998 0.15628 -1.153638777 6.233781552 85.82584 1.97798 SKOR1 . . . SKI family transcriptional corepressor 1 FUNCTION: Acts as a transcriptional corepressor of LBX1 (By similarity). Inhibits BMP signaling. {ECO:0000250}.; . TISSUE SPECIFICITY: Present specifically in cerebellar Purkinje cells (at protein level). {ECO:0000269|PubMed:17292623}.; germinal center; dorsal root ganglion;superior cervical ganglion;skeletal muscle; 0.08309 0.11270 . . 286.51918 3.62519 SKOR2 0.611171343025554 0.354132181866503 0.0346964751079431 SKI family transcriptional corepressor 2 FUNCTION: Exhibits transcriptional repressor activity (By similarity). Acts as a TGF-beta antagonist in the nervous system. {ECO:0000250, ECO:0000269|PubMed:16200078}.; . TISSUE SPECIFICITY: Expressed in cerebellum, spinal cord and testis. Isoform 2 is present in cerebellum (at protein level). {ECO:0000269|PubMed:16200078}.; . . . . . . 2129.889 8.49629 SKP1 0.224830619473668 0.739302878494732 0.0358665020315999 S-phase kinase-associated protein 1 FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5, CEP68 and probably NFKB2 (PubMed:25704143). SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) directs ubiquitination of TTI1 and TELO2. SCF(FBXO10) directs ubiquitination of BCL2. {ECO:0000269|PubMed:16209941, ECO:0000269|PubMed:20181953, ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:23431138, ECO:0000269|PubMed:25704143}.; . . myocardium;lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;bladder;tonsil;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;atrium;oesophagus;larynx;bone;pituitary gland;testis;artery;spinal ganglion;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;aorta;stomach;cerebellum;thymus; amygdala;whole brain;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.88062 . 0.057118534 57.99716914 . . SKP1P1 . . . S-phase kinase-associated protein 1 pseudogene 1 . . . . . . . . . . . SKP1P2 . . . S-phase kinase-associated protein 1 pseudogene 2 . . . . . . . . . . . SKP1P3 . . . S-phase kinase-associated protein 1 pseudogene 3 . . . . . . . . . . . SKP2 0.9942587612668 0.00574108654438025 1.5218881947319e-07 S-phase kinase-associated protein 2, E3 ubiquitin protein ligase FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. Degradation of CDKN1B/p27kip also requires CKS1. Recognizes target proteins ORC1, CDT1, RBL2, KMT2A/MLL1, CDK9, RAG2, FOXO1, UBP43, and probably MYC, TOB1 and TAL1. Degradation of TAL1 also requires STUB1. Recognizes CDKN1A in association with CCNE1 or CCNE2 and CDK2. Promotes ubiquitination and destruction of CDH1 in a CK1-Dependent Manner, thereby regulating cell migration. {ECO:0000269|PubMed:11931757, ECO:0000269|PubMed:12435635, ECO:0000269|PubMed:12769844, ECO:0000269|PubMed:12840033, ECO:0000269|PubMed:15342634, ECO:0000269|PubMed:15668399, ECO:0000269|PubMed:15949444, ECO:0000269|PubMed:16103164, ECO:0000269|PubMed:16262255, ECO:0000269|PubMed:16581786, ECO:0000269|PubMed:16951159, ECO:0000269|PubMed:17908926, ECO:0000269|PubMed:17962192, ECO:0000269|PubMed:22770219}.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;urinary;skeletal muscle;pancreas;lung;placenta;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach; fetal liver;superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.84521 0.22825 -0.692458599 14.96815287 7.13276 0.26672 SLA 0.722953169634171 0.276436302604009 0.000610527761819653 Src-like-adaptor FUNCTION: Adapter protein, which negatively regulates T-cell receptor (TCR) signaling. Inhibits T-cell antigen-receptor induced activation of nuclear factor of activated T-cells. Involved in the negative regulation of positive selection and mitosis of T-cells. May act by linking signaling proteins such as ZAP70 with CBL, leading to a CBL dependent degradation of signaling proteins. {ECO:0000269|PubMed:10449770, ECO:0000269|PubMed:11696592}.; . TISSUE SPECIFICITY: Expressed in lung and fetal brain. Weakly expressed in heart, adult brain, placenta, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:9660183}.; ovary;umbilical cord;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;cerebral cortex;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;lung;nasopharynx;placenta;macula lutea;liver;alveolus;spleen;kidney;mammary gland;thymus; fetal brain;white blood cells;whole blood;thymus;bone marrow; 0.64234 0.32933 -0.093566408 46.7386176 247.56148 3.39356 SLA2 0.384130951390547 0.605642627202347 0.0102264214071055 Src-like-adaptor 2 FUNCTION: Adapter protein, which negatively regulates T-cell receptor (TCR) signaling. Inhibits T-cell antigen-receptor induced activation of nuclear factor of activated T-cells. May act by linking signaling proteins such as ZAP70 with CBL, leading to a CBL dependent degradation of signaling proteins. {ECO:0000269|PubMed:11696592}.; . TISSUE SPECIFICITY: Predominantly expressed in immune system, with highest levels in peripheral blood leukocytes. Expressed in spleen, thymus and lymph nodes. Expressed in T-cells as well as in monocytes, and at low level in B-cells. Also detected in placenta, prostate, skin, retina and colon.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;endometrium;gum;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach;thymus; . 0.09791 0.23425 0.260991686 70.25831564 292.5164 3.65755 SLAIN1 0.959443821545465 0.0405374590160108 1.87194385239094e-05 SLAIN motif family member 1 . . TISSUE SPECIFICITY: Expressed in embryonic stem cells. {ECO:0000269|PubMed:16546155}.; unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;hypothalamus;parathyroid;fovea centralis;cerebrum;skin;retina;prostate;whole body;lung;endometrium;placenta;macula lutea;visual apparatus;hippocampus;liver;testis;germinal center;kidney;brain;artery;aorta; medulla oblongata;superior cervical ganglion;occipital lobe;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;pons;parietal lobe;cerebellum; 0.43441 0.11246 -0.315847836 31.68789809 2009.99237 8.25347 SLAIN2 0.883438470234681 0.11650572723282 5.58025324990583e-05 SLAIN motif family member 2 FUNCTION: Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Required for normal structure of the microtubule cytoskeleton during interphase. {ECO:0000269|PubMed:21646404}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in adult liver, testis and ovary, and lowest levels in adult pancreas and spleen and in fetal brain. {ECO:0000269|PubMed:10819331}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.72814 0.10961 -0.293801652 32.93819297 24.34614 0.80017 SLAMF1 0.135406431574352 0.84384952384424 0.0207440445814087 signaling lymphocytic activation molecule family member 1 FUNCTION: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. SLAMF1-induced signal- transduction events in T-lymphocytes are different from those in B-cells. Two modes of SLAMF1 signaling seem to exist: one depending on SH2D1A (and perhaps SH2D1B) and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction operates. Initially it has been proposed that association with SH2D1A prevents binding to inhibitory effectors including INPP5D/SHIP1 and PTPN11/SHP-2 (PubMed:11806999). However, signaling is also regulated by SH2D1A which can simultaneously interact with and recruit FYN which subsequently phosphorylates and activates SLAMF1 (PubMed:12458214). Mediates IL-2-independent proliferation of activated T-cells during immune responses and induces IFN-gamma production (By similarity). Downstreaming signaling involves INPP5D, DOK1 and DOK2 leading to inhibited IFN-gamma production in T-cells, and PRKCQ, BCL10 and NFKB1 leading to increased T-cell activation and Th2 cytokine production (By similarity). Promotes T-cell receptor-induced IL-4 secretion by CD4(+) cells (By similarity). Inhibits antigen receptor-mediated production of IFN-gamma, but not IL-2, in CD4(-)/CD8(-) T-cells (By similarity). Required for IL-4 production by germinal centers T follicular helper (T(Fh))cells (By similarity). May inhibit CD40-induced signal transduction in monocyte-derived dendritic cells (PubMed:16317102). May play a role in a allergic responses and may regulate allergen-induced Th2 cytokine and Th1 cytokine secretion (By similarity). In conjunction with SLAMF6 controls the transition between positive selection and the subsequent expansion and differentiation of the thymocytic natural killer T (NKT) cell lineage. Involved in the peripheral differentiation of indifferent natural killer T (iNKT) cells toward a regulatory NKT2 type (By similarity). In macrophages involved in down-regulation of IL-12, TNF-alpha and nitric oxide in response to lipopolysaccharide (LPS) (By similarity). In B-cells activates the ERK signaling pathway independently of SH2D1A but implicating both, SYK and INPP5D, and activates Akt signaling dependent on SYK and SH2D1A (By similarity). In B-cells also activates p38 MAPK and JNK1 and JNK2 (PubMed:20231852). In conjunction with CD84/SLAMF5 and SLAMF6 may be a negative regulator of the humoral immune response (By similarity). {ECO:0000250|UniProtKB:Q9QUM4, ECO:0000269|PubMed:16317102, ECO:0000269|PubMed:20231852, ECO:0000305|PubMed:11806999, ECO:0000305|PubMed:12458214}.; . TISSUE SPECIFICITY: Constitutively expressed on peripheral blood memory T-cells, T-cell clones, immature thymocytes and a proportion of B-cells, and is rapidly induced on naive T-cells after activation (PubMed:7617038). Activated B-cells express isoform 1, isoform 3 and a cytoplasmic isoform (PubMed:9091591). Isoform 4 is expressed in B-cells, primary T-cells, dendritic cells and macrophages. Isoform 4 is expressed in tumors of the central nervous system (PubMed:25710480). {ECO:0000269|PubMed:25710480, ECO:0000269|PubMed:7617038, ECO:0000269|PubMed:9091591}.; unclassifiable (Anatomical System);lymph node;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;optic nerve;lung;nasopharynx;bone;placenta;macula lutea;testis;germinal center; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09966 0.24625 0.729426781 86.17008728 607.90051 4.98723 SLAMF6 0.356879514961895 0.640484924013399 0.0026355610247057 SLAM family member 6 FUNCTION: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Triggers cytolytic activity only in natural killer cells (NK) expressing high surface densities of natural cytotoxicity receptors (PubMed:11489943, PubMed:16920955). Positive signaling in NK cells implicates phosphorylation of VAV1. NK cell activation seems to depend on SH2D1B and not on SH2D1A (PubMed:16920955). In conjunction with SLAMF1 controls the transition between positive selection and the subsequent expansion and differentiation of the thymocytic natural killer T (NKT) cell lineage (By similarity). Promotes T-cell differentiation into a helper T-cell Th17 phenotype leading to increased IL-17 secretion; the costimulatory activity requires SH2D1A (PubMed:22184727, PubMed:16920955). Promotes recruitment of RORC to the IL-17 promoter (PubMed:22989874). In conjunction with SLAMF1 and CD84/SLAMF5 may be a negative regulator of the humoral immune response. In the absence of SH2D1A/SAP can transmit negative signals to CD4(+) T-cells and NKT cells. Negatively regulates germinal center formation by inhibiting T-cell:B-cell adhesion; the function probably implicates increased association with PTPN6/SHP-1 via ITSMs in absence of SH2D1A/SAP. However, reported to be involved in maintaining B-cell tolerance in germinal centers and in preventing autoimmunity (By similarity). {ECO:0000250|UniProtKB:Q9ET39, ECO:0000269|PubMed:11489943, ECO:0000269|PubMed:16920955, ECO:0000269|PubMed:22184727, ECO:0000269|PubMed:22989874}.; . TISSUE SPECIFICITY: Expressed by all (resting and activated) natural killer cells (NK), T- and B-lymphocytes (PubMed:11489943). Increased surface expression on T-cells of systemic lupus erythematosus (SLE) patients (PubMed:22184727). {ECO:0000269|PubMed:11489943, ECO:0000269|PubMed:22184727}.; . . 0.02674 0.11186 -0.427900189 25.14744043 12.74982 0.46404 SLAMF6P1 . . . SLAM family member 6 pseudogene 1 . . . . . . . . . . . SLAMF7 0.00654462638539223 0.91360234991234 0.0798530237022677 SLAM family member 7 FUNCTION: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Isoform 1 mediates NK cell activation through a SH2D1A-independent extracellular signal- regulated ERK-mediated pathway (PubMed:11698418). Positively regulates NK cell functions by a mechanism dependent on phosphorylated SH2D1B. Downstream signaling implicates PLCG1, PLCG2 and PI3K (PubMed:16339536). In addition to heterotypic NK cells-target cells interactions also homotypic interactions between NK cells may contribute to activation. However, in the absence of SH2D1B, inhibits NK cell function. Acts also inhibitory in T-cells (By similarity). May play a role in lymphocyte adhesion (PubMed:11802771). In LPS-activated monocytes negatively regulates production of proinflammatory cytokines (PubMed:23695528). {ECO:0000250|UniProtKB:Q8BHK6, ECO:0000269|PubMed:11698418, ECO:0000269|PubMed:11802771, ECO:0000269|PubMed:16339536, ECO:0000269|PubMed:23695528, ECO:0000269|Ref.4}.; . TISSUE SPECIFICITY: Expressed in spleen, lymph node, peripheral blood leukocytes, bone marrow, small intestine, stomach, appendix, lung and trachea. Expression was detected in NK cells, activated B-cells, NK-cell line but not in promyelocytic, B-, or T-cell lines. Expressed in monocytes. Isoform 3 is expressed at much lower level than isoform 1. {ECO:0000269|PubMed:11220635, ECO:0000269|PubMed:11698418, ECO:0000269|PubMed:11802771, ECO:0000269|PubMed:12242590, ECO:0000269|PubMed:23695528}.; unclassifiable (Anatomical System);lymph node;heart;adrenal cortex;parathyroid;blood;skin;uterus;pancreas;prostate;lung;endometrium;oesophagus;adrenal gland;larynx;nasopharynx;bone;thyroid;head and neck;germinal center;pineal gland;mammary gland; skeletal muscle; 0.03543 0.21394 0.306902668 72.38145789 16.77883 0.58989 SLAMF8 1.70506204430406e-06 0.422014191221952 0.577984103716004 SLAM family member 8 FUNCTION: May play a role in B-lineage commitment and/or modulation of signaling through the B-cell receptor. {ECO:0000269|PubMed:11313408}.; . TISSUE SPECIFICITY: Expressed in lymph node, spleen, thymus and bone marrow. {ECO:0000269|PubMed:11313408}.; unclassifiable (Anatomical System);smooth muscle;cartilage;urinary;colon;blood;fovea centralis;choroid;lens;skin;retina;optic nerve;lung;nasopharynx;placenta;bone;macula lutea;alveolus;liver;spleen;brain;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14799 0.10599 -0.001743238 53.85114414 631.46276 5.06279 SLAMF9 0.00785783195511103 0.928295425162528 0.0638467428823608 SLAM family member 9 FUNCTION: May play a role in the immune response. {ECO:0000269|PubMed:11300479}.; . TISSUE SPECIFICITY: Expression is predominantly restricted in hematopoietic tissues. Expressed in heart, spleen, liver, intestine, muscle and testis. Expressed in immune cells, including monocytes, dendritic, B- and T-cells. No expression was seen in peripheral blood leukocytes. Expressed in the leukocyte cell line THP-1. {ECO:0000269|PubMed:11300479, ECO:0000269|PubMed:11685473}.; . . 0.02391 0.06354 0.817616644 87.95116773 678.60963 5.20693 SLBP 0.51565945835262 0.480527184232855 0.00381335741452537 stem-loop binding protein FUNCTION: RNA-binding protein involved in the histone pre-mRNA processing. Binds the stem-loop structure of replication-dependent histone pre-mRNAs and contributes to efficient 3'-end processing by stabilizing the complex between histone pre-mRNA and U7 small nuclear ribonucleoprotein (snRNP), via the histone downstream element (HDE). Plays an important role in targeting mature histone mRNA from the nucleus to the cytoplasm and to the translation machinery. Stabilizes mature histone mRNA and could be involved in cell-cycle regulation of histone gene expression. Involved in the mechanism by which growing oocytes accumulate histone proteins that support early embryogenesis. Binds to the 5' side of the stem-loop structure of histone pre-mRNAs. {ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:19155325}.; . TISSUE SPECIFICITY: Widely expressed.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; amygdala;testis - interstitial;testis - seminiferous tubule;testis; 0.15025 0.07916 0.058937498 58.26256192 18.41337 0.63798 SLC1A1 0.00127116672107192 0.990263239628326 0.00846559365060187 solute carrier family 1 member 1 FUNCTION: Transports L-glutamate, L- and D-aspartate and L-cystein (PubMed:21123949). Essential for terminating the postsynaptic action of glutamate by rapidly removing released glutamate from the synaptic cleft. Acts as a symport by cotransporting sodium. Negatively regulated by ARL6IP5 (By similarity). {ECO:0000250|UniProtKB:P51906, ECO:0000250|UniProtKB:P51907, ECO:0000269|PubMed:21123949}.; DISEASE: Dicarboxylic aminoaciduria (DCBXA) [MIM:222730]: An autosomal recessive disorder characterized by abnormal excretion of urinary glutamate and aspartate, resulting from the incomplete reabsorption of anionic amino acids from the glomerular filtrate in the kidney. It can be associated with mental retardation. {ECO:0000269|PubMed:21123949}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Schizophrenia 18 (SCZD18) [MIM:615232]: A complex, multifactorial psychotic disorder or group of disorders characterized by disturbances in the form and content of thought (e.g. delusions, hallucinations), in mood (e.g. inappropriate affect), in sense of self and relationship to the external world (e.g. loss of ego boundaries, withdrawal), and in behavior (e.g bizarre or apparently purposeless behavior). Although it affects emotions, it is distinguished from mood disorders in which such disturbances are primary. Similarly, there may be mild impairment of cognitive function, and it is distinguished from the dementias in which disturbed cognitive function is considered primary. Some patients manifest schizophrenic as well as bipolar disorder symptoms and are often given the diagnosis of schizoaffective disorder. {ECO:0000269|PubMed:21982423, ECO:0000269|PubMed:23341099}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. A deletion at the chromosome 9p24.2 locus, including SLC1A1, has been identified in patients with psychotic disorders (PubMed:21982423). This 84 kb deletion is immediately upstream of the SLC1A1 gene in a regulatory region that contains the full native promoter sequence, extends through exon 1 of the SLC1A1 mRNA, co-segregates with disease in an extended 5-generation pedigree and increases disease risk more than 18-fold for family members (PubMed:23341099). {ECO:0000269|PubMed:21982423, ECO:0000269|PubMed:23341099}.; TISSUE SPECIFICITY: Expressed in all tissues tested including liver, muscle, testis, ovary, retinoblastoma cell line, neurons and brain (in which there was dense expression in substantia nigra, red nucleus, hippocampus and in cerebral cortical layers). {ECO:0000269|PubMed:7521911, ECO:0000269|PubMed:7859077, ECO:0000269|PubMed:7914198}.; colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;thyroid;bone;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;cervix;kidney;stomach; amygdala;superior cervical ganglion;occipital lobe;thalamus;globus pallidus;kidney;parietal lobe; 0.33586 0.36670 -0.709045403 14.673272 180.84982 2.92281 SLC1A2 0.907792747494983 0.0921769197891323 3.03327158844873e-05 solute carrier family 1 member 2 FUNCTION: Transports L-glutamate and also L- and D-aspartate. Essential for terminating the postsynaptic action of glutamate by rapidly removing released glutamate from the synaptic cleft. Acts as a symport by cotransporting sodium.; . . bone marrow;retina;ganglion;frontal lobe;cerebral cortex;larynx;testis;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;lymph node;nervous;hypothalamus;spinal cord;blood;lens;skeletal muscle;breast;lung;adrenal gland;placenta;hippocampus;liver;head and neck;mammary gland;stomach; whole brain;amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.57019 0.38533 -1.287751345 5.03066761 31.32127 0.98813 SLC1A3 0.432519796435931 0.567179241911644 0.000300961652425531 solute carrier family 1 member 3 FUNCTION: Transports L-glutamate and also L- and D-aspartate. Essential for terminating the postsynaptic action of glutamate by rapidly removing released glutamate from the synaptic cleft. Acts as a symport by cotransporting sodium.; DISEASE: Episodic ataxia 6 (EA6) [MIM:612656]: A disorder characterized by episodic ataxia, seizures, migraine and alternating hemiplegia. {ECO:0000269|PubMed:16116111}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in cerebellum, but also found in frontal cortex, hippocampus and basal ganglia.; lymphoreticular;myocardium;ovary;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;pituitary gland;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;spinal cord;urinary;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;hypopharynx;spleen;head and neck;kidney;stomach;cerebellum; whole brain;amygdala;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.29842 0.53995 -0.66859065 15.76433121 187.70695 2.97492 SLC1A4 0.242897704080993 0.750367908245597 0.00673438767341002 solute carrier family 1 member 4 FUNCTION: Transporter for alanine, serine, cysteine, and threonine. Exhibits sodium dependence. {ECO:0000269|PubMed:26041762}.; . TISSUE SPECIFICITY: Expressed mostly in brain, muscle, and pancreas but detected in all tissues examined.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;urinary;pharynx;blood;cerebrum;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;amygdala;superior cervical ganglion;globus pallidus;ciliary ganglion;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.12708 0.17318 -0.111973265 45.35857514 749.9076 5.43136 SLC1A5 0.0518112085245823 0.927214039882222 0.0209747515931954 solute carrier family 1 member 5 FUNCTION: Sodium-dependent amino acids transporter that has a broad substrate specificity, with a preference for zwitterionic amino acids. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated, anionic, and cationic amino acids. May also be activated by insulin. Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development (PubMed:10708449, PubMed:23492904). Acts as a cell surface receptor for feline endogenous virus RD114, baboon M7 endogenous virus and type D simian retroviruses (PubMed:10051606, PubMed:10196349). {ECO:0000269|PubMed:10051606, ECO:0000269|PubMed:10196349, ECO:0000269|PubMed:10708449, ECO:0000269|PubMed:23492904}.; . TISSUE SPECIFICITY: Placenta, lung, skeletal muscle, kidney, pancreas, and intestine.; smooth muscle;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;greater omentum;pancreas;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion; 0.34584 0.23562 . . 1968.95604 8.17692 SLC1A6 0.92891102404997 0.0710121468367547 7.68291132750924e-05 solute carrier family 1 member 6 FUNCTION: Transports L-glutamate and also L- and D-aspartate. Seems to act as a symport by cotransporting sodium.; . TISSUE SPECIFICITY: Brain. Expressed densely and selectively in cell bodies of Purkinje cells.; unclassifiable (Anatomical System);medulla oblongata;brain;skin;stomach;cerebellum; amygdala;superior cervical ganglion;testis - interstitial;cerebellum peduncles;pons;caudate nucleus;skeletal muscle;fetal brain;testis - seminiferous tubule;testis;globus pallidus;parietal lobe;cerebellum; 0.26103 . -0.800872469 12.33191791 38.46571 1.14105 SLC1A7 1.86525618722239e-05 0.692462208986593 0.307519138451534 solute carrier family 1 member 7 FUNCTION: Transports L-glutamate; the L-glutamate uptake is sodium- and voltage-dependent and chloride-independent. Its associated chloride conductance may participate in visual processing.; . TISSUE SPECIFICITY: Expressed primarily in retina. Detectable in liver, heart, muscle and brain.; . . 0.16248 0.11957 -0.435396074 24.70511913 3881.59601 12.29872 SLC2A1 0.939808130156394 0.0601414632785394 5.04065650665899e-05 solute carrier family 2 member 1 FUNCTION: Facilitative glucose transporter. This isoform may be responsible for constitutive or basal glucose uptake. Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses. {ECO:0000269|PubMed:18245775, ECO:0000269|PubMed:19449892}.; DISEASE: GLUT1 deficiency syndrome 2 (GLUT1DS2) [MIM:612126]: A clinically variable disorder characterized primarily by onset in childhood of paroxysmal exercise-induced dyskinesia. The dyskinesia involves transient abnormal involuntary movements, such as dystonia and choreoathetosis, induced by exercise or exertion, and affecting the exercised limbs. Some patients may also have epilepsy, most commonly childhood absence epilepsy. Mild mental retardation may also occur. In some patients involuntary exertion- induced dystonic, choreoathetotic, and ballistic movements may be associated with macrocytic hemolytic anemia. {ECO:0000269|PubMed:14605501, ECO:0000269|PubMed:18451999, ECO:0000269|PubMed:19630075, ECO:0000269|PubMed:19798636, ECO:0000269|PubMed:20129935, ECO:0000269|PubMed:20574033, ECO:0000269|PubMed:20621801, ECO:0000269|PubMed:20830593, ECO:0000269|PubMed:21204808}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epilepsy, idiopathic generalized 12 (EIG12) [MIM:614847]: A disorder characterized by recurring generalized seizures in the absence of detectable brain lesions and/or metabolic abnormalities. Generalized seizures arise diffusely and simultaneously from both hemispheres of the brain. Seizure types include juvenile myoclonic seizures, absence seizures, and generalized tonic-clonic seizures. In some EIG12 patients seizures may remit with age. {ECO:0000269|PubMed:19798636, ECO:0000269|PubMed:22282645}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dystonia 9 (DYT9) [MIM:601042]: An autosomal dominant neurologic disorder characterized by childhood onset of paroxysmal choreoathetosis and progressive spastic paraplegia. Most patients show some degree of cognitive impairment. Other variable features may include seizures, migraine headaches, and ataxia. {ECO:0000269|PubMed:21832227}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in erythrocytes (at protein level). Expressed at variable levels in many human tissues. {ECO:0000269|PubMed:23219802}.; . . 0.38519 0.78861 -1.045216355 7.661004954 15.72909 0.56049 SLC2A1-AS1 . . . SLC2A1 antisense RNA 1 . . . . . . . . . . . SLC2A2 7.53167438901512e-05 0.980362440422839 0.0195622428332711 solute carrier family 2 member 2 FUNCTION: Facilitative glucose transporter. This isoform likely mediates the bidirectional transfer of glucose across the plasma membrane of hepatocytes and is responsible for uptake of glucose by the beta cells; may comprise part of the glucose-sensing mechanism of the beta cell. May also participate with the Na(+)/glucose cotransporter in the transcellular transport of glucose in the small intestine and kidney.; DISEASE: Fanconi-Bickel syndrome (FBS) [MIM:227810]: Rare, well- defined clinical entity, inherited in an autosomal recessive mode and characterized by hepatorenal glycogen accumulation, proximal renal tubular dysfunction, and impaired utilization of glucose and galactose. {ECO:0000269|PubMed:10987651, ECO:0000269|PubMed:11044475}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver, insulin-producing beta cell, small intestine and kidney.; unclassifiable (Anatomical System);lung;liver;testis;spleen;kidney;skeletal muscle; superior cervical ganglion;fetal liver;liver;ciliary ganglion;kidney;pons;trigeminal ganglion;skeletal muscle; 0.54341 0.73053 -0.224023033 37.4321774 1965.19505 8.16817 SLC2A3 0.519822945853932 0.479418579843023 0.000758474303045016 solute carrier family 2 member 3 FUNCTION: Facilitative glucose transporter that can also mediate the uptake of various other monosaccharides across the cell membrane (PubMed:9477959, PubMed:26176916). Mediates the uptake of glucose, 2-deoxyglucose, galactose, mannose, xylose and fucose, and probably also dehydroascorbate (PubMed:9477959, PubMed:26176916). Does not mediate fructose transport (PubMed:9477959, PubMed:26176916). {ECO:0000269|PubMed:26176916, ECO:0000269|PubMed:9477959}.; . TISSUE SPECIFICITY: Highly expressed in brain. Expressed in many tissues. {ECO:0000269|PubMed:3170580}.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;germinal center;bladder;brain;ciliary body;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;cerebellum; olfactory bulb;whole blood;bone marrow; 0.35764 0.14971 0.619191319 83.36282142 55.14143 1.48810 SLC2A3P1 . . . solute carrier family 2 member 3 pseudogene 1 . . . . . . . . . . . SLC2A3P2 . . . solute carrier family 2 member 3 pseudogene 2 . . . . . . . . . . . SLC2A3P4 . . . solute carrier family 2 member 3 pseudogene 4 . . . . . . . . . . . SLC2A4 0.135386792584163 0.86371416405545 0.000899043360387207 solute carrier family 2 member 4 FUNCTION: Insulin-regulated facilitative glucose transporter.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:1521731, ECO:0000269|PubMed:1756912, ECO:0000269|PubMed:1918382}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Skeletal and cardiac muscles; brown and white fat.; unclassifiable (Anatomical System);myocardium;heart;muscle;colon;skin;skeletal muscle;uterus;prostate;lung;larynx;bone;liver;testis;head and neck;spleen;kidney;stomach; dorsal root ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.32877 0.13952 -0.178111357 40.44585987 1219.29265 6.60287 SLC2A4RG 0.00794438690680656 0.785359603916919 0.206696009176275 SLC2A4 regulator FUNCTION: Transcription factor involved in SLC2A4 and HD gene transactivation. Binds to the consensus sequence 5'-GCCGGCG-3'. {ECO:0000269|PubMed:14625278, ECO:0000269|PubMed:14630949}.; . TISSUE SPECIFICITY: According to PubMed:14630949, expressed in heart, skeletal muscle, liver, kidney and pancreas; undetectable in lung, placenta or brain. According to PubMed:14625278, ubiquitously expressed, with lowest expression in brain and ileum. {ECO:0000269|PubMed:14625278, ECO:0000269|PubMed:14630949}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;urinary;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;liver;kidney; 0.09524 0.21330 . . 46.99331 1.32570 SLC2A5 5.67732629021242e-05 0.886434588035433 0.113508638701665 solute carrier family 2 member 5 FUNCTION: Cytochalasin B-sensitive carrier. Seems to function primarily as a fructose transporter.; . TISSUE SPECIFICITY: Expressed in small intestine, and at much lower levels in kidney, skeletal muscle, and adipose tissue.; . . 0.14495 0.37127 -0.198338176 39.17197452 161.01384 2.77098 SLC2A6 0.000366664150450035 0.83502725282833 0.16460608302122 solute carrier family 2 member 6 FUNCTION: Facilitative glucose transporter; binds cytochalasin B with low affinity.; . TISSUE SPECIFICITY: Highly expressed in brain, spleen and peripheral blood leukocytes.; . . 0.13365 0.11917 -0.220384297 37.6032083 266.02217 3.49813 SLC2A7 2.99498303352468e-17 0.000633281993701998 0.999366718006298 solute carrier family 2 member 7 FUNCTION: High-affinity transporter for glucose and fructose Does not transport galactose, 2-deoxy-d-glucose and xylose. {ECO:0000269|PubMed:15033637}.; . TISSUE SPECIFICITY: Expressed in small intestine and colon. Weakly expressed in testis and prostate. {ECO:0000269|PubMed:15033637}.; . . 0.08611 0.17345 1.692094639 96.42014626 924.8755 5.90621 SLC2A8 0.237274587723511 0.755640875698136 0.0070845365783523 solute carrier family 2 member 8 FUNCTION: Insulin-regulated facilitative glucose transporter. Binds cytochalasin B in a glucose-inhibitable manner. Seems to be a dual-specific sugar transporter as it is inhibitable by fructose (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in testis, but not in testicular carcinoma. Lower amounts present in most other tissues.; . . 0.13559 0.19460 . . 535.19959 4.71649 SLC2A9 1.40146196215314e-10 0.05365009043664 0.946349909423214 solute carrier family 2 member 9 FUNCTION: Transport urate and fructose. May have a role in the urate reabsorption by proximal tubules. Also transports glucose at low rate. {ECO:0000269|PubMed:14739288, ECO:0000269|PubMed:18327257}.; DISEASE: Hypouricemia renal 2 (RHUC2) [MIM:612076]: A disorder characterized by impaired uric acid reabsorption at the apical membrane of proximal renal tubule cells, and high urinary urate excretion. Patients often appear asymptomatic, but may be subject to exercise-induced acute renal failure, chronic renal dysfunction and nephrolithiasis. {ECO:0000269|PubMed:19026395, ECO:0000269|PubMed:19926891, ECO:0000269|PubMed:21810765}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Most strongly expressed in basolateral membranes of proximal renal tubular cells, liver and placenta. Also detected in lung, blood leukocytes, heart skeletal muscle and chondrocytes from articular cartilage. Isoform 2 is only detected in the apical membranes of polarized renal tubular cells and placenta. Isoform 1 and isoform 2 are detected in kidney membrane (at protein level). {ECO:0000269|PubMed:11991658, ECO:0000269|PubMed:24409316}.; unclassifiable (Anatomical System);lung;cartilage;endometrium;placenta;liver;testis;colon;spleen;kidney;brain;skeletal muscle;stomach;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;kidney;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.02777 . 1.225399457 93.24722812 5201.07444 14.85144 SLC2A10 0.00820173708336499 0.931287564159103 0.0605106987575319 solute carrier family 2 member 10 FUNCTION: Facilitative glucose transporter.; . TISSUE SPECIFICITY: Widely expressed; highest levels in liver and pancreas. {ECO:0000269|PubMed:11592815}.; unclassifiable (Anatomical System);heart;islets of Langerhans;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;breast;pancreas;optic nerve;whole body;lung;mesenchyma;placenta;macula lutea;liver;testis;brain;stomach; . 0.11613 0.17999 0.225995239 68.51851852 1026.34052 6.15729 SLC2A11 5.45933694484048e-12 0.0297141428608734 0.970285857133667 solute carrier family 2 member 11 FUNCTION: Facilitative glucose transporter. {ECO:0000269|PubMed:12175779}.; . TISSUE SPECIFICITY: Expressed in heart and skeletal muscle.; ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;whole body;optic nerve;frontal lobe;cerebral cortex;bone;thyroid;testis;brain;tonsil;unclassifiable (Anatomical System);islets of Langerhans;blood;lens;lung;placenta;hippocampus;macula lutea;liver;cervix;kidney;stomach;aorta; superior cervical ganglion;skeletal muscle; 0.12516 0.17895 0.756930627 86.79523473 2116.44908 8.46655 SLC2A12 0.0194084110413465 0.961598580402219 0.0189930085564348 solute carrier family 2 member 12 FUNCTION: Facilitative glucose transporter. {ECO:0000250}.; . TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle, heart and prostate, with lower levels in brain, placenta and kidney. {ECO:0000269|PubMed:11832379}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);amygdala;meninges;islets of Langerhans;hypothalamus;urinary;lens;skeletal muscle;pancreas;pia mater;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.51083 0.13755 -1.153638777 6.233781552 134.73204 2.52307 SLC2A13 0.956100908800451 0.0438944703004106 4.62089913874615e-06 solute carrier family 2 member 13 FUNCTION: H(+)-myo-inositol cotransporter. Can also transport related stereoisomers. {ECO:0000269|PubMed:11500374}.; . TISSUE SPECIFICITY: Predominantly expressed in the brain. {ECO:0000269|PubMed:11500374}.; unclassifiable (Anatomical System);amygdala;cartilage;liver;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.26791 0.18971 -0.626318434 17.03231894 187.0857 2.96919 SLC2A13P1 . . . SLC2A13 pseudogene 1 . . . . . . . . . . . SLC2A14 0.989967414117294 0.0100296403168352 2.94556587082895e-06 solute carrier family 2 member 14 FUNCTION: Facilitative glucose transporter (By similarity). May have a specific function related to spermatogenesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed mainly in testis. {ECO:0000269|PubMed:12504846}.; smooth muscle;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;cochlea;thyroid;testis;ciliary body;brain;bladder;unclassifiable (Anatomical System);heart;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;spleen;head and neck;kidney;cerebellum; . 0.10940 0.12793 -0.534490515 20.70063694 503.82321 4.60543 SLC2AXP1 . . . solute carrier family 2 pseudogene 1 . . . . . . . . . . . SLC3A1 7.54764121472888e-16 0.00423677370069255 0.995763226299307 solute carrier family 3 member 1 FUNCTION: Involved in the high-affinity, sodium-independent transport of cystine and neutral and dibasic amino acids (system B(0,+)-like activity). May function as an activator of SLC7A9 and be involved in the high-affinity reabsorption of cystine in the kidney tubule. {ECO:0000269|PubMed:11318953, ECO:0000269|PubMed:7686906, ECO:0000269|PubMed:8486766, ECO:0000269|PubMed:8663184}.; DISEASE: Hypotonia-cystinuria syndrome (HCS) [MIM:606407]: Characterized generalized hypotonia at birth, nephrolithiasis, growth hormone deficiency, minor facial dysmorphism, failure to thrive, followed by hyperphagia and rapid weight gain in late childhood. {ECO:0000269|PubMed:16385448}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the brush border membrane in the kidney (at protein level). Predominantly expressed in the kidney, small intestine and pancreas. Weakly expressed in liver. {ECO:0000269|PubMed:12167606, ECO:0000269|PubMed:7686906, ECO:0000269|PubMed:8486766}.; ovary;salivary gland;sympathetic chain;colon;skin;retina;uterus;prostate;frontal lobe;larynx;testis;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;pia mater;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney; superior cervical ganglion;kidney;parietal lobe; 0.14759 0.43231 -1.589211351 3.096249115 899.71507 5.84266 SLC3A2 0.923234161379885 0.0767468892122091 1.89494079054839e-05 solute carrier family 3 member 2 FUNCTION: Required for the function of light chain amino-acid transporters. Involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. Involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, is also involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. When associated with SLC7A5 or SLC7A8, involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L- nitrosocysteine (L-CNSO) across the transmembrane. Together with ICAM1, regulates the transport activity LAT2 in polarized intestinal cells, by generating and delivering intracellular signals. When associated with SLC7A5, plays an important role in transporting L-leucine from the circulating blood to the retina across the inner blood-retinal barrier. {ECO:0000269|PubMed:10903140, ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:11389679, ECO:0000269|PubMed:11557028, ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:11742812, ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:12716892, ECO:0000269|PubMed:14603368, ECO:0000269|PubMed:15769744, ECO:0000269|PubMed:15980244, ECO:0000269|PubMed:9751058, ECO:0000269|PubMed:9829974, ECO:0000269|PubMed:9878049}.; . TISSUE SPECIFICITY: Expressed ubiquitously in all tissues tested with highest levels detected in kidney, placenta and testis and weakest level in thymus. During gestation, expression in the placenta was significantly stronger at full-term than at the mid- trimester stage. Expressed in HUVECS and at low levels in resting peripheral blood T-lymphocytes and quiescent fibroblasts. Also expressed in fetal liver and in the astrocytic process of primary astrocytic gliomas. Expressed in retinal endothelial cells and in the intestinal epithelial cell line C2BBe1. {ECO:0000269|PubMed:11389679, ECO:0000269|PubMed:11557028, ECO:0000269|PubMed:11742812, ECO:0000269|PubMed:12716892, ECO:0000269|PubMed:14603368, ECO:0000269|PubMed:15980244, ECO:0000269|PubMed:16496379, ECO:0000269|PubMed:3265470, ECO:0000269|PubMed:3480538}.; lymphoreticular;medulla oblongata;ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;endometrium;bone;thyroid;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;skeletal muscle;bile duct;breast;pancreas;lung;mesenchyma;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; placenta;kidney; 0.27357 0.41835 -0.310388054 32.14791224 99.64846 2.16179 SLC4A1 0.909484294882695 0.0905154653539652 2.39763339543266e-07 solute carrier family 4 member 1 (Diego blood group) FUNCTION: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine. {ECO:0000269|PubMed:10926824, ECO:0000269|PubMed:14734552, ECO:0000269|PubMed:1538405, ECO:0000269|PubMed:20151848, ECO:0000269|PubMed:24121512}.; DISEASE: Ovalocytosis, Southeast Asian (SAO) [MIM:166900]: A hereditary hematologic disorder characterized by ovalocytic erythrocytes that are rigid and exhibit reduced expression of many erythrocyte antigens. Clinical manifestations include mild hemolysis, intermittent jaundice and gallstones. However, the disorder is most often asymptomatic. {ECO:0000269|PubMed:1538405, ECO:0000269|PubMed:1722314}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spherocytosis 4 (SPH4) [MIM:612653]: Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. {ECO:0000269|PubMed:10580570, ECO:0000269|PubMed:10745622, ECO:0000269|PubMed:10942416, ECO:0000269|PubMed:11380459, ECO:0000269|PubMed:1378323, ECO:0000269|PubMed:15813913, ECO:0000269|PubMed:16227998, ECO:0000269|PubMed:7530501, ECO:0000269|PubMed:8547122, ECO:0000269|PubMed:8640229, ECO:0000269|PubMed:8943874, ECO:0000269|PubMed:9012689, ECO:0000269|PubMed:9207478, ECO:0000269|PubMed:9233560, ECO:0000269|PubMed:9973643}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Renal tubular acidosis, distal, autosomal dominant (AD- dRTA) [MIM:179800]: An autosomal dominant disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. It is due to functional failure of alpha- intercalated cells of the cortical collecting duct of the distal nephron, where vectorial proton transport is required for urinary acidification. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Renal tubular acidosis, distal, with hemolytic anemia (dRTA-HA) [MIM:611590]: A disease characterized by the association of hemolytic anemia with distal renal tubular acidosis, the reduced ability to acidify urine resulting in variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. {ECO:0000269|PubMed:10926824, ECO:0000269|PubMed:15211439, ECO:0000269|PubMed:9854053}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Renal tubular acidosis, distal, with normal red cell morphology (dRTA-NRC) [MIM:611590]: A disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. It is due to functional failure of alpha- intercalated cells of the cortical collecting duct of the distal nephron, where vectorial proton transport is required for urinary acidification. {ECO:0000269|PubMed:15211439}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in erythrocytes (at protein level). Isoform 2 is expressed in kidney (at protein level) (PubMed:7506871). {ECO:0000269|PubMed:10926824, ECO:0000269|PubMed:1538405, ECO:0000269|PubMed:23219802, ECO:0000269|PubMed:7506871}.; unclassifiable (Anatomical System);heart;placenta;liver;spleen;brain; fetal liver;superior cervical ganglion;fetal lung;kidney;bone marrow; 0.10965 0.57746 -0.789972689 12.61500354 702.26691 5.26999 SLC4A1AP 7.73999085415032e-07 0.976744184846949 0.0232550411539654 solute carrier family 4 member 1 adaptor protein . . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15764369}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pia mater;lung;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.09992 0.09231 -0.442665927 24.53408823 1349.12013 6.89590 SLC4A1APP1 . . . solute carrier family 4 member 1 adaptor protein pseudogene 1 . . . . . . . . . . . SLC4A1APP2 . . . solute carrier family 4 member 1 adaptor protein pseudogene 2 . . . . . . . . . . . SLC4A2 0.999960115734587 3.98842652442939e-05 1.69013317951806e-13 solute carrier family 4 member 2 FUNCTION: Plasma membrane anion exchange protein of wide distribution.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;endometrium;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;cervix;kidney;mammary gland;stomach; placenta;skeletal muscle; 0.16300 . -1.767443354 2.317763623 743.50361 5.41356 SLC4A3 0.218420219942613 0.78157918550151 5.94555876417017e-07 solute carrier family 4 member 3 FUNCTION: Plasma membrane anion exchange protein of wide distribution. Mediates at least a part of the Cl(-)/HCO3(-) exchange in cardiac myocytes. Both BAE3 and CAE3 forms transport Cl(-).; . TISSUE SPECIFICITY: Both BAE3 and CAE3 are expressed in failing ventricle.; myocardium;ovary;salivary gland;sympathetic chain;choroid;fovea centralis;skin;retina;uterus;prostate;whole body;optic nerve;thyroid;iris;testis;brain;unclassifiable (Anatomical System);amygdala;islets of Langerhans;lens;skeletal muscle;lung;hippocampus;visual apparatus;macula lutea;liver;duodenum;spleen;mammary gland;aorta; fetal liver;superior cervical ganglion;thalamus;heart;hypothalamus;fetal lung;kidney;caudate nucleus;bone marrow; 0.13793 0.29645 -1.181449241 5.915310215 285.03266 3.61293 SLC4A4 0.999995794728427 4.20527155559051e-06 1.72144380674243e-14 solute carrier family 4 member 4 FUNCTION: Electrogenic sodium/bicarbonate cotransporter with a Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3. May regulate bicarbonate influx/efflux at the basolateral membrane of cells and regulate intracellular pH. {ECO:0000269|PubMed:10069984, ECO:0000269|PubMed:12907161, ECO:0000269|PubMed:16636648, ECO:0000269|PubMed:16769890, ECO:0000269|PubMed:17661077, ECO:0000269|PubMed:9235899, ECO:0000269|PubMed:9651366}.; DISEASE: Renal tubular acidosis, proximal, with ocular abnormalities and mental retardation (pRTA-OA) [MIM:604278]: An extremely rare autosomal recessive syndrome characterized by short stature, profound proximal renal tubular acidosis, mental retardation, bilateral glaucoma, cataracts and bandkeratopathy. pRTA is due to a failure of the proximal tubular cells to reabsorb filtered bicarbonate from the urine, leading to urinary bicarbonate wasting and subsequent acidemia. {ECO:0000269|PubMed:10545938, ECO:0000269|PubMed:15471865, ECO:0000269|PubMed:15713912, ECO:0000269|PubMed:15930088, ECO:0000269|PubMed:16636648, ECO:0000269|PubMed:17661077}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Loss of interaction with and stimulation by CA4 is the cause of retinitis pigmentosa type 17 (RP17).; TISSUE SPECIFICITY: Isoform 1 is expressed in pancreas and to a lower extent in heart, skeletal muscle, liver, parotid salivary glands, prostate, colon, stomach, thyroid, brain and spinal chord. Corneal endothelium cells express only isoform 1 (at protein level). Isoform 2 is specifically expressed in kidney at the level of proximal tubules. {ECO:0000269|PubMed:10069984, ECO:0000269|PubMed:11743927, ECO:0000269|PubMed:12907161, ECO:0000269|PubMed:14559244, ECO:0000269|PubMed:15329059, ECO:0000269|PubMed:9235899, ECO:0000269|PubMed:9651366}.; ovary;colon;parathyroid;fovea centralis;skin;bone marrow;prostate;whole body;frontal lobe;cerebral cortex;thyroid;testis;amniotic fluid;bladder;brain;amygdala;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;hippocampus;macula lutea;liver;spleen;kidney;stomach;cerebellum; dorsal root ganglion;amygdala;superior cervical ganglion;occipital lobe;cerebellum peduncles;spinal cord;caudate nucleus;atrioventricular node;pons;skin;skeletal muscle;prefrontal cortex;appendix;ciliary ganglion;kidney;trigeminal ganglion;parietal lobe;cerebellum; 0.06301 0.32138 -0.372889896 28.20240623 1787.71075 7.80377 SLC4A5 1.37460263086747e-07 0.999506764789814 0.000493097749923239 solute carrier family 4 member 5 FUNCTION: Mediates sodium- and bicarbonate-dependent electrogenic sodium bicarbonate cotransport, with a Na(+):HCO3(-) stoichiometry of 2:1. May have a housekeeping function in regulating the pH of tissues in which it is expressed. May play a role in mediating Na(+):HCO3(-) cotransport in hepatocytes and intrahepatic cholangiocytes. Also may be important in protecting the renal paranchyma from alterations in urine pH. {ECO:0000250|UniProtKB:Q6RI88, ECO:0000269|PubMed:11788353, ECO:0000269|PubMed:11997242, ECO:0000269|PubMed:12388414}.; . TISSUE SPECIFICITY: Highest expression observed in liver, spleen and testis; moderate expression in the choroid plexus, hippocampus, cerebrum and cerebellum of brain, and in kidney cortex and kidney medulla. Also observed in heart, pancreas, muscle, lung, placenta, stomach and small intestine. Weakest expression seen in peripheral blood lymphocytes, colon, duodenum, jejunum, ileum and skeletal muscle. {ECO:0000269|PubMed:10978526, ECO:0000269|PubMed:11087115, ECO:0000269|PubMed:11788353, ECO:0000269|PubMed:17715183}.; lymphoreticular;myocardium;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;aorta; superior cervical ganglion;globus pallidus;atrioventricular node; 0.64152 0.15239 -1.54510635 3.30856334 590.38757 4.92536 SLC4A7 0.69770797268161 0.302292016224193 1.10941972522967e-08 solute carrier family 4 member 7 FUNCTION: Electroneutral sodium- and bicarbonate-dependent cotransporter with a Na(+):HCO3(-) 1:1 stoichiometry. Regulates intracellular pH and may play a role in bicarbonate salvage in secretory epithelia. May also have an associated sodium channel activity. {ECO:0000269|PubMed:10347222, ECO:0000269|PubMed:12403779}.; . TISSUE SPECIFICITY: Highly expressed in testis and spleen. Also expressed in retina, colon, small intestine, ovary, thymus, prostate, muscle, heart and kidney. Isoform 1 is expressed in skeletal muscle and heart muscle. {ECO:0000269|PubMed:9610397}.; unclassifiable (Anatomical System);heart;ovary;spinal cord;colon;parathyroid;skin;skeletal muscle;breast;uterus;whole body;lung;endometrium;larynx;bone;placenta;liver;testis;cervix;head and neck;spleen;brain;stomach;thymus; dorsal root ganglion;whole brain;superior cervical ganglion;subthalamic nucleus;medulla oblongata;cerebellum peduncles;prefrontal cortex;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe; 0.32289 0.17102 -0.96998676 8.958480774 1426.46505 7.05525 SLC4A8 0.999867374132928 0.000132625866433072 6.38484664073607e-13 solute carrier family 4 member 8 FUNCTION: Mediates electroneutral sodium- and carbonate-dependent chloride-HCO3(-) exchange with a Na(+):HCO3(-) stoichiometry of 2:1. Plays a major role in pH regulation in neurons. May be involved in cell pH regulation by transporting HCO3(-) from blood to cell. Enhanced expression in severe acid stress could be important for cell survival by mediating the influx of HCO3(-) into the cells. Also mediates lithium-dependent HCO3(-) cotransport. May be regulated by osmolarity. {ECO:0000269|PubMed:10362779, ECO:0000269|PubMed:11133997}.; . TISSUE SPECIFICITY: Expressed in the pyramidal cells of the hippocampus (at protein level). Highly expressed in all major regions of the brain, spinal column and in testis, and moderate levels in trachea, thyroid and medulla region of kidney. Low expression levels observed in pancreas and kidney cortex. {ECO:0000269|PubMed:10362779, ECO:0000269|PubMed:11133997, ECO:0000269|PubMed:17715183}.; unclassifiable (Anatomical System);lung;frontal lobe;cerebral cortex;islets of Langerhans;bone;sympathetic chain;testis;germinal center;brain;skeletal muscle; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;prefrontal cortex; 0.07064 0.11699 -0.799052816 12.45576787 53.47821 1.45321 SLC4A9 5.6907011258673e-18 0.00327711043087832 0.996722889569122 solute carrier family 4 member 9 FUNCTION: Probable apical anion exchanger of the kidney cortex. {ECO:0000250}.; . TISSUE SPECIFICITY: Kidney specific. {ECO:0000269|PubMed:11305939, ECO:0000269|Ref.7}.; testis;kidney; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.16646 0.16629 -0.437212558 24.67563105 300.21036 3.69534 SLC4A10 0.00263554372615494 0.997359387585577 5.06868826788784e-06 solute carrier family 4 member 10 FUNCTION: Electrogenic sodium/bicarbonate cotransporter in exchange for intracellular chloride. Plays an important role in regulating intracellular pH (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);smooth muscle;cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;vein;skin;uterus;prostate;lung;frontal lobe;endometrium;thyroid;placenta;hippocampus;liver;testis;spleen;kidney;mammary gland;peripheral nerve; . 0.80523 0.11754 -0.843147538 11.2762444 69.94846 1.73490 SLC4A11 1.36725840636298e-08 0.986858917459332 0.0131410688680841 solute carrier family 4 member 11 FUNCTION: Transporter which plays an important role in sodium- mediated fluid transport in different organs. Prevents severe morphological changes of the cornea caused by increased sodium chloride concentrations in the stroma. In the inner ear, is involved in transport of potassium through the fibrocyte layer to the stria vascularis and is essential for the generation of the endocochlear potential but not for regulation of potassium concentrations in the endolymph. In the kidney, is essential for urinary concentration, mediates a sodium flux into the thin descending limb of Henle loop to allow countercurrent multiplication by osmotic equilibration (By similarity). Involved in borate homeostasis. In the absence of borate, it functions as a Na(+) and OH(-)(H(+)) channel. In the presence of borate functions as an electrogenic Na(+) coupled borate cotransporter. {ECO:0000250, ECO:0000269|PubMed:15525507}.; DISEASE: Corneal dystrophy and perceptive deafness (CDPD) [MIM:217400]: An ocular disease characterized by the association of corneal clouding with progressive perceptive hearing loss. {ECO:0000269|PubMed:17220209}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, endothelial 2, autosomal recessive (CHED2) [MIM:217700]: A congenital corneal dystrophy characterized by thickening and opacification of the cornea, altered morphology of the endothelium, and secretion of an abnormal collagenous layer at the Descemet membrane. {ECO:0000269|PubMed:16767101, ECO:0000269|PubMed:16825429, ECO:0000269|PubMed:17220209, ECO:0000269|PubMed:17397048, ECO:0000269|PubMed:17679935, ECO:0000269|PubMed:18474783, ECO:0000269|PubMed:19369245, ECO:0000269|PubMed:20108384, ECO:0000269|PubMed:21203343, ECO:0000269|PubMed:26286922}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, Fuchs endothelial, 4 (FECD4) [MIM:613268]: A corneal disease caused by loss of endothelium of the central cornea. It is characterized by focal wart-like guttata that arise from Descemet membrane and develop in the central cornea, epithelial blisters, reduced vision and pain. Descemet membrane is thickened by abnormal collagenous deposition. {ECO:0000269|PubMed:18024964, ECO:0000269|PubMed:20848555}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney, testis, salivary gland, thyroid, trachea and corneal endothelium. Not detected in retina and lymphocytes. {ECO:0000269|PubMed:11302728, ECO:0000269|PubMed:16767101}.; . . 0.46037 0.13430 -2.339131252 1.173625855 523.34294 4.66743 SLC5A1 0.00803119583011728 0.991367154811515 0.000601649358367285 solute carrier family 5 member 1 FUNCTION: Actively transports glucose into cells by Na(+) cotransport with a Na(+) to glucose coupling ratio of 2:1. Efficient substrate transport in mammalian kidney is provided by the concerted action of a low affinity high capacity and a high affinity low capacity Na(+)/glucose cotransporter arranged in series along kidney proximal tubules.; DISEASE: Congenital glucose/galactose malabsorption (GGM) [MIM:606824]: Intestinal monosaccharide transporter deficiency. It is an autosomal recessive disorder manifesting itself within the first weeks of life. It is characterized by severe diarrhea and dehydration which are usually fatal unless glucose and galactose are eliminated from the diet. {ECO:0000269|PubMed:10036327, ECO:0000269|PubMed:11406349, ECO:0000269|PubMed:2008213, ECO:0000269|PubMed:8195156}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed mainly in intestine and kidney.; seminal vesicle;lung;small intestine;heart;liver;testis;colon;kidney;skin;skeletal muscle; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16404 0.40470 0.332586472 73.61405992 415.36286 4.26635 SLC5A2 8.34847516316556e-11 0.256233353475595 0.74376664644092 solute carrier family 5 member 2 FUNCTION: Sodium-dependent glucose transporter. Has a Na(+) to glucose coupling ratio of 1:1.; DISEASE: Renal glucosuria (GLYS) [MIM:233100]: A disorder characterized by persistent isolated glucosuria, normal fasting serum glucose concentration, decreased renal tubular resorption of glucose from the urine, and absence of any other signs of tubular dysfunction. {ECO:0000269|PubMed:14614622}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;bone;testis;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;oral cavity;muscle;blood;lens;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;head and neck;kidney;mammary gland;stomach; kidney;skeletal muscle; 0.29148 0.19205 -0.861560326 10.89289927 83.6341 1.94519 SLC5A3 0.849464749953749 0.149995365371998 0.000539884674253199 solute carrier family 5 member 3 FUNCTION: Prevents intracellular accumulation of high concentrations of myo-inositol (an osmolyte) that result in impairment of cellular function.; . . . . 0.47678 0.38085 -0.666770504 15.86459071 50.54376 1.39893 SLC5A4 2.60144685908226e-13 0.125757351228254 0.874242648771486 solute carrier family 5 member 4 FUNCTION: Sodium-dependent glucose transporter. {ECO:0000250}.; . . unclassifiable (Anatomical System);liver;spleen; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skin; 0.08441 0.11240 0.736704836 86.32932295 914.47301 5.88119 SLC5A4P1 . . . solute carrier family 5 member 4 pseudogene 1 . . . . . . . . . . . SLC5A5 0.740011195140398 0.259967990187734 2.0814671867698e-05 solute carrier family 5 member 5 FUNCTION: Mediates iodide uptake in the thyroid gland.; . TISSUE SPECIFICITY: Expression is primarily in thyroid tissue, but also to a lower extent in mammary gland and ovary. Expression is reduced in tumors. {ECO:0000269|PubMed:8806637, ECO:0000269|PubMed:9329364}.; skeletal muscle; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06754 . -0.887242605 10.43288511 87.44126 1.99728 SLC5A6 0.571968337581082 0.428011126015068 2.05364038502662e-05 solute carrier family 5 member 6 FUNCTION: Transports pantothenate, biotin and lipoate in the presence of sodium.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; placenta;testis;ciliary ganglion; 0.28049 . -0.088107893 47.06298655 303.36532 3.71201 SLC5A7 0.101652706275807 0.896860271494859 0.00148702222933374 solute carrier family 5 member 7 FUNCTION: Imports choline from the extracellular space to the neuron with high affinity. Choline uptake is the rate-limiting step in acetylcholine synthesis. Sodium ion- and chloride ion- dependent. {ECO:0000269|PubMed:11027560}.; DISEASE: Neuronopathy, distal hereditary motor, 7A (HMN7A) [MIM:158580]: A neuromuscular disorder. Distal hereditary motor neuronopathies constitute a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. HMN7A is characterized by onset in the second decade of progressive distal muscle wasting and weakness affecting the upper and lower limbs and resulting in walking difficulties and hand grip. There is significant muscle atrophy of the hands and lower limbs. The disorder is associated with vocal cord paresis due to involvement of the tenth cranial nerve. {ECO:0000269|PubMed:23141292}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in putamen, spinal cord and medulla. Specific for cholinergic neurons.; adrenal gland;pineal body;sympathetic chain;spinal ganglion; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.30034 0.21418 0.240763792 69.36777542 401.3971 4.20160 SLC5A8 2.85808956199266e-11 0.144285014055644 0.855714985915775 solute carrier family 5 member 8 FUNCTION: Acts as an electrogenic sodium (Na(+)) and chloride (Cl-)-dependent sodium-coupled solute transporter, including transport of monocarboxylates (short-chain fatty acids including L-lactate, D-lactate, pyruvate, acetate, propionate, valerate and butyrate), lactate, mocarboxylate drugs (nicotinate, benzoate, salicylate and 5-aminosalicylate) and ketone bodies (beta-D- hydroxybutyrate, acetoacetate and alpha-ketoisocaproate), with a Na(+):substrate stoichiometry of between 4:1 and 2:1. Catalyzes passive carrier mediated diffusion of iodide. Mediates iodide transport from the thyrocyte into the colloid lumen through the apical membrane. May be responsible for the absorption of D- lactate and monocarboxylate drugs from the intestinal tract. Acts as a tumor suppressor, suppressing colony formation in colon cancer, prostate cancer and glioma cell lines. May play a critical role in the entry of L-lactate and ketone bodies into neurons by a process driven by an electrochemical Na(+) gradient and hence contribute to the maintenance of the energy status and function of neurons. {ECO:0000269|PubMed:12107270, ECO:0000269|PubMed:12829793, ECO:0000269|PubMed:14966140, ECO:0000269|PubMed:15090606, ECO:0000269|PubMed:15361710, ECO:0000269|PubMed:15867356, ECO:0000269|PubMed:16729224, ECO:0000269|PubMed:16805814, ECO:0000269|PubMed:17178845, ECO:0000269|PubMed:17245649, ECO:0000269|PubMed:18037591}.; . TISSUE SPECIFICITY: Expressed in normal thyroid, localized at the apical pole of thyroid cells facing the colloid lumen, but expression profoundly decreased in thyroid carcinomas. Expressed in normal colon but absent in colon aberrant crypt foci and colon cancers. Present in normal kidney cortex, brain, prostate, gastric mucosa and breast tissue but was significantly down-regulated in primary gliomas, gastric cancer, prostate tumors and breast tumors. {ECO:0000269|PubMed:12107270, ECO:0000269|PubMed:12829793, ECO:0000269|PubMed:14966140, ECO:0000269|PubMed:15001644, ECO:0000269|PubMed:15090606, ECO:0000269|PubMed:15361710, ECO:0000269|PubMed:15867356, ECO:0000269|PubMed:17178845, ECO:0000269|PubMed:17245649, ECO:0000269|PubMed:18037591}.; . . 0.10158 0.19628 0.402364592 76.45081387 4376.33259 13.20513 SLC5A9 6.41959687057975e-13 0.205889732699933 0.794110267299425 solute carrier family 5 member 9 FUNCTION: Involved in sodium-dependent transport of D-mannose, D- glucose and D-fructose. {ECO:0000269|PubMed:15607332}.; . TISSUE SPECIFICITY: Expressed in the small intestine, kidney and liver. {ECO:0000269|PubMed:15607332}.; lung;visual apparatus;liver;testis;spleen;kidney;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.15660 . 1.140856814 92.36848313 4675.1235 13.76981 SLC5A10 3.65971963018288e-12 0.158427677685009 0.841572322311331 solute carrier family 5 member 10 FUNCTION: High capacity transporter for mannose and fructose and, to a lesser extent, glucose, AMG, and galactose. {ECO:0000269|PubMed:22212718}.; . TISSUE SPECIFICITY: Seems to be exclusively expressed in kidney. {ECO:0000269|PubMed:22212718}.; unclassifiable (Anatomical System);cartilage;heart;ovary;pharynx;colon;skin;pancreas;lung;endometrium;liver;testis;cervix;spleen;germinal center;kidney;brain;stomach; . 0.13415 0.12866 -0.817464788 11.97806086 259.29549 3.46053 SLC5A11 1.49641187474707e-06 0.957508085377538 0.0424904182105876 solute carrier family 5 member 11 FUNCTION: Involved in the sodium-dependent cotransport of myo- inositol (MI) with a Na(+):MI stoichiometry of 2:1. Exclusively responsible for apical MI transport and absorption in intestine. Also can transport D-chiro-inositol (DCI) but not L-fructose. Exhibits stereospecific cotransport of both D-glucose and D- xylose. May induce apoptosis through the TNF-alpha, PDCD1 pathway. May play a role in the regulation of MI concentration in serum, involving reabsorption in at least the proximal tubule of the kidney. {ECO:0000269|PubMed:15172003}.; . TISSUE SPECIFICITY: Highest expression in heart, skeletal muscle, kidney, liver and placenta. Weaker expression in brain, colon, spleen, lung and peripheral blood leukocytes. {ECO:0000269|PubMed:12039040}.; unclassifiable (Anatomical System);frontal lobe;kidney; hypothalamus;parietal lobe; 0.15471 0.14812 0.07167258 59.15899976 1301.03449 6.78647 SLC5A12 2.14726778576519e-05 0.994946342112692 0.00503218520945024 solute carrier family 5 member 12 FUNCTION: Acts as an electroneutral and low-affinity sodium (Na(+))-dependent sodium-coupled solute transporter. Catalyzes the transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, nicotinate, propionate, butyrate and beta-D- hydroxybutyrate. May be responsible for the first step of reabsorption of monocarboxylates from the lumen of the proximal tubule of the kidney and the small intestine. May play also a role in monocarboxylates transport in the retina (By similarity). Mediates electroneutral uptake of lactate, with a stoichiometry of 2 Na(+) for each lactate (By similarity). {ECO:0000250, ECO:0000269|PubMed:17692818}.; . . unclassifiable (Anatomical System);colon;kidney;stomach; fetal liver;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;kidney;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07079 0.08633 -0.067881249 48.69072895 817.0844 5.61431 SLC6A1 0.999301879165817 0.000698116426688977 4.40749428704483e-09 solute carrier family 6 member 1 FUNCTION: Terminates the action of GABA by its high affinity sodium-dependent reuptake into presynaptic terminals.; DISEASE: Myoclonic-atonic epilepsy (MAE) [MIM:616421]: A form of epilepsy characterized by myoclonic-atonic and absence seizures, appearing in early childhood. Patients have delayed development before the onset of seizures and show varying degrees of intellectual disability following seizure onset. {ECO:0000269|PubMed:25865495}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);amygdala;hypothalamus;colon;parathyroid;pancreas;frontal lobe;bone;hippocampus;liver;spleen;brain;stomach; whole brain;amygdala;superior cervical ganglion;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.18869 0.23984 -0.358119787 29.16371786 65.10574 1.66104 SLC6A1-AS1 . . . SLC6A1 antisense RNA 1 . . . . . . . . . . . SLC6A2 0.277118300003759 0.722673486422211 0.000208213574029789 solute carrier family 6 member 2 FUNCTION: Amine transporter. Terminates the action of noradrenaline by its high affinity sodium-dependent reuptake into presynaptic terminals. {ECO:0000269|PubMed:2008212}.; DISEASE: Orthostatic intolerance (OI) [MIM:604715]: Syndrome characterized by lightheadedness, fatigue, altered mentation and syncope. It is associated with postural tachycardia. Plasma norepinephrine concentration is abnormally high. {ECO:0000269|PubMed:10684912}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);larynx;placenta;liver;spleen;head and neck;brain;skeletal muscle; dorsal root ganglion;thalamus;superior cervical ganglion;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;adrenal gland;placenta;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.20984 0.25220 -0.44448505 24.46331682 192.60631 3.00986 SLC6A3 0.99703690247797 0.00296306725675279 3.02652776186517e-08 solute carrier family 6 member 3 FUNCTION: Amine transporter. Terminates the action of dopamine by its high affinity sodium-dependent reuptake into presynaptic terminals. {ECO:0000269|PubMed:1406597, ECO:0000269|PubMed:15505207, ECO:0000269|PubMed:8302271}.; . TISSUE SPECIFICITY: Highly expressed in substantia nigra. {ECO:0000269|PubMed:7637582}.; unclassifiable (Anatomical System);uterus;lung;ganglion;heart;kidney;brain;skin; . 0.23027 0.37171 -1.528486521 3.385232366 27.97415 0.89791 SLC6A4 0.85488009451934 0.145115816394683 4.08908597668397e-06 solute carrier family 6 member 4 FUNCTION: Serotonin transporter whose primary function in the central nervous system involves the regulation of serotonergic signaling via transport of serotonin molecules from the synaptic cleft back into the pre-synaptic terminal for re-utilization. Plays a key role in mediating regulation of the availability of serotonin to other receptors of serotonergic systems. Terminates the action of serotonin and recycles it in a sodium-dependent manner. {ECO:0000269|PubMed:17506858, ECO:0000269|PubMed:18227069, ECO:0000269|PubMed:19270731}.; . TISSUE SPECIFICITY: Expressed in platelets (at protein level). {ECO:0000269|PubMed:17506858}.; lung;cartilage;bone;placenta;liver;spleen; superior cervical ganglion;pons;trigeminal ganglion; 0.12724 0.55872 -0.600630256 18.06440198 115.61782 2.33887 SLC6A5 1.84554624033866e-12 0.352780378349569 0.647219621648586 solute carrier family 6 member 5 FUNCTION: Terminates the action of glycine by its high affinity sodium-dependent reuptake into presynaptic terminals. May be responsible for the termination of neurotransmission at strychnine-sensitive glycinergic synapses. {ECO:0000269|PubMed:10381548, ECO:0000269|PubMed:10606742, ECO:0000269|PubMed:9845349}.; . TISSUE SPECIFICITY: Expressed in medulla, and to a lesser extent in spinal cord and cerebellum.; testis; superior cervical ganglion;globus pallidus;trigeminal ganglion; 0.28678 0.12247 0.784444605 87.2611465 4374.32344 13.20049 SLC6A6 0.98227564953919 0.0177238623369894 4.88123820498594e-07 solute carrier family 6 member 6 FUNCTION: Sodium-dependent taurine and beta-alanine transporter. Chloride ions are necessary for optimal uptake. {ECO:0000269|PubMed:8382624}.; . TISSUE SPECIFICITY: Expressed abundantly in placenta and skeletal muscle, at intermediate levels in heart, brain, lung, kidney and pancreas and at low levels in liver. {ECO:0000269|PubMed:8382624}.; unclassifiable (Anatomical System);fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;breast;prostate;optic nerve;placenta;macula lutea;visual apparatus;liver;spleen;brain;stomach; superior cervical ganglion;subthalamic nucleus;tongue;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.32797 . -0.291981272 33.20358575 72.45796 1.77348 SLC6A6P1 . . . solute carrier family 6 member 6 pseudogene 1 . . . . . . . . . . . SLC6A7 7.14638706508392e-06 0.976649657622941 0.0233431959899939 solute carrier family 6 member 7 FUNCTION: Terminates the action of proline by its high affinity sodium-dependent reuptake into presynaptic terminals.; . TISSUE SPECIFICITY: Brain.; unclassifiable (Anatomical System);optic nerve;macula lutea;colon;fovea centralis;choroid;lens;brain;tonsil;retina;cerebellum; superior cervical ganglion;temporal lobe;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.21530 0.51251 -1.285933373 5.083746167 154.49049 2.71751 SLC6A8 0.991889602732559 0.00810864725099276 1.75001644841976e-06 solute carrier family 6 member 8 FUNCTION: Required for the uptake of creatine in muscles and brain.; . TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and kidney. Also found in brain, heart, colon, testis and prostate. {ECO:0000269|PubMed:7945388, ECO:0000269|PubMed:7953292}.; medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;bladder;brain;amygdala;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);hypothalamus;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;cerebellum; amygdala;whole brain;occipital lobe;thalamus;prefrontal cortex;kidney;caudate nucleus;parietal lobe;cingulate cortex;skeletal muscle;cerebellum; 0.46879 0.09301 -0.736552314 13.93606983 16.24131 0.57643 SLC6A9 0.0442530405880805 0.955512482401763 0.000234477010156261 solute carrier family 6 member 9 FUNCTION: Terminates the action of glycine by its high affinity sodium-dependent reuptake into presynaptic terminals. May play a role in regulation of glycine levels in NMDA receptor-mediated neurotransmission.; . TISSUE SPECIFICITY: Isoform GlyT-1A and isoform GlyT-1B can be found in brain, kidney, pancreas, lung, placenta and liver but isoform GlyT-1C is only found in brain.; unclassifiable (Anatomical System);breast;placenta;colon;brain; superior cervical ganglion;skeletal muscle; 0.33742 0.18430 -0.709045403 14.673272 90.55117 2.04822 SLC6A10P . . . solute carrier family 6 member 10, pseudogene . . . medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;testis;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.09544 . . . . . SLC6A11 0.364943330068891 0.634954352797094 0.000102317134014636 solute carrier family 6 member 11 FUNCTION: Terminates the action of GABA by its high affinity sodium-dependent reuptake into presynaptic terminals.; . TISSUE SPECIFICITY: Widespread distribution in the brain.; unclassifiable (Anatomical System);frontal lobe;thyroid;head and neck;brain;skeletal muscle; superior cervical ganglion; 0.20827 0.14310 -0.442665927 24.53408823 180.38702 2.91889 SLC6A12 7.90050068276314e-07 0.906866608353463 0.0931326015964687 solute carrier family 6 member 12 FUNCTION: Transports betaine and GABA. May have a role in regulation of GABAergic transmission in the brain through the reuptake of GABA into presynaptic terminals, as well as in osmotic regulation.; . TISSUE SPECIFICITY: Liver, heart, skeletal muscle, placenta, and a widespread distribution in the brain.; unclassifiable (Anatomical System);uterus;lung;endometrium;placenta;liver;testis;spleen;kidney;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion; 0.09170 0.13124 -0.396754488 26.97570182 130.44718 2.48749 SLC6A13 1.85726644531532e-08 0.641770503703225 0.35822947772411 solute carrier family 6 member 13 FUNCTION: Sodium-dependent GABA and taurine transporter. In presynaptic terminals, regulates GABA signaling termination through GABA uptake. May also be involved in beta-alanine transport. {ECO:0000269|PubMed:17502375, ECO:0000269|PubMed:22932902}.; . TISSUE SPECIFICITY: Expressed in brain, kidney, lung, liver and testis. {ECO:0000269|PubMed:11824941, ECO:0000269|PubMed:17502375}.; unclassifiable (Anatomical System);optic nerve;lung;macula lutea;colon;fovea centralis;choroid;kidney;lens;brain;stomach;retina; superior cervical ganglion;globus pallidus;kidney;trigeminal ganglion;skeletal muscle; 0.08446 0.14271 -0.527216948 20.8893607 398.80138 4.19401 SLC6A14 0.986093843050961 0.0139048286347103 1.32831432879299e-06 solute carrier family 6 member 14 FUNCTION: Mediates the uptake of a broad range of neutral and cationic amino acids (with the exception of proline) in a Na(+)/Cl(-)-dependent manner. {ECO:0000269|PubMed:10446133}.; . TISSUE SPECIFICITY: Levels are highest in adult and fetal lung, in trachea and salivary gland. Lower levels detected in mammary gland, stomach and pituitary gland, and very low levels in colon, uterus, prostate and testis. {ECO:0000269|PubMed:10446133}.; . . 0.31634 0.11942 -0.227663163 37.11370606 33.30111 1.02846 SLC6A15 0.00226259561522053 0.994003973708605 0.00373343067617463 solute carrier family 6 member 15 FUNCTION: Functions as a sodium-dependent neutral amino acid transporter. Exhibits preference for the branched-chain amino acids, particularly leucine, valine and isoleucine and methionine. Mediates the saturable, pH-sensitive and electrogenic cotransport of proline and sodium ions with a stoichiometry of 1:1. May have a role as transporter for neurotransmitter precursors into neurons. In contrast to other members of the neurotransmitter transporter family, does not appear to be chloride-dependent. {ECO:0000269|PubMed:16226721}.; . TISSUE SPECIFICITY: Almost exclusively expressed in the brain. {ECO:0000269|PubMed:16226721}.; unclassifiable (Anatomical System);meninges;heart;choroid;fovea centralis;lens;skeletal muscle;skin;retina;uterus;pia mater;lung;optic nerve;frontal lobe;larynx;gum;placenta;macula lutea;cervix;head and neck;dura mater;brain; whole brain;amygdala;dorsal root ganglion;occipital lobe;subthalamic nucleus;superior cervical ganglion;fetal brain;hypothalamus;globus pallidus;trigeminal ganglion;skeletal muscle;parietal lobe;cerebellum; 0.12557 0.11240 0.068033485 59.0351498 70.72739 1.74982 SLC6A16 4.47639511693954e-11 0.184306005208602 0.815693994746634 solute carrier family 6 member 16 . . TISSUE SPECIFICITY: Highly expressed in peripheral tissues, particularly in testis, pancreas, and prostate.; unclassifiable (Anatomical System);medulla oblongata;prostate;lung;whole body;larynx;liver;testis;spleen;head and neck;brain;peripheral nerve; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion; 0.06197 0.06488 -0.595174814 18.21184242 64.79265 1.65290 SLC6A17 0.962734835648401 0.0372620944554727 3.06989612611519e-06 solute carrier family 6 member 17 FUNCTION: Functions as a sodium-dependent vesicular transporter selective for proline, glycine, leucine and alanine. In contrast to other members of this neurotransmitter transporter family, does not appear to be chloride-dependent (By similarity). {ECO:0000250|UniProtKB:P31662}.; DISEASE: Mental retardation, autosomal recessive 48 (MRT48) [MIM:616269]: A form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT48 patients show moderate to severe intellectual disability and additional features including progressive tremor, speech impairment, and sometimes behavioral problems. {ECO:0000269|PubMed:25704603}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . testis; whole brain;amygdala;superior cervical ganglion;occipital lobe;subthalamic nucleus;temporal lobe;globus pallidus;ciliary ganglion;pons;atrioventricular node;parietal lobe;cerebellum; 0.30380 0.11278 -0.574945567 18.90186365 1512.56654 7.22536 SLC6A18 1.67091561448187e-22 5.0018180821531e-05 0.999949981819178 solute carrier family 6 member 18 FUNCTION: Functions as a sodium and chloride-dependent neutral amino acid transporter. {ECO:0000250}.; DISEASE: Note=Genetic variations in SLC6A18 might contribute to the disease phentotype in some individuals with iminoglycinuria or hyperglycinuria, that carry variants in SLC36A2, SLC6A19 or SLC6A20 (PubMed:19033659). {ECO:0000269|PubMed:19033659}.; TISSUE SPECIFICITY: Abundantly expressed in kidney, but not in intestine. {ECO:0000269|PubMed:15286787}.; unclassifiable (Anatomical System);colon;kidney; dorsal root ganglion;medulla oblongata;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;kidney;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.05501 0.10731 1.010397292 90.81151215 651.86737 5.12089 SLC6A19 8.52430000848369e-18 0.00415700033030221 0.995842999669698 solute carrier family 6 member 19 FUNCTION: Transporter that mediates epithelial resorption of neutral amino acids across the apical membrane of epithelial cells in the kidney and intestine. It appears that leucine is the preferred substrate, but all large neutral non-aromatic L-amino acids bind to this transporter. Uptake of leucine is sodium- dependent. In contrast to other members of the neurotransmitter transporter family, does not appear to be chloride-dependent (By similarity). {ECO:0000250}.; DISEASE: Hyperglycinuria (HG) [MIM:138500]: A condition characterized by excess of glycine in the urine. In some cases it is associated with renal colic and renal oxalate stones. {ECO:0000269|PubMed:19033659}. Note=The disease may be caused by mutations affecting the gene represented in this entry. SLC6A19 deficiency combined with haploinsufficiency of SLC6A20 or partially inactivating mutations in SLC36A2, can be responsible for hyperglycinuria.; DISEASE: Iminoglycinuria (IG) [MIM:242600]: A disorder of renal tubular reabsorption of glycine and imino acids (proline and hydroxyproline), marked by excessive levels of all three substances in the urine. {ECO:0000269|PubMed:19033659}. Note=The disease may be caused by mutations affecting the gene represented in this entry. SLC6A19 deficiency combined with haploinsufficiency of SLC6A20 or partially inactivating mutations in SLC36A2, can be responsible for iminoglycinuria. Additional polymorphisms and mutations in SLC6A18 can contribute to the IG phenotype in some families.; TISSUE SPECIFICITY: Robust expression in kidney and small intestine, with minimal expression in pancreas. Also expressed in stomach, liver, duodenum, ileocecum, colon and prostate. Not detected in testis, whole brain, cerebellum, fetal liver, spleen, skeletal muscle, uterus, heart or lung. {ECO:0000269|PubMed:15286787, ECO:0000269|PubMed:15286788}.; unclassifiable (Anatomical System);colon;kidney;stomach; dorsal root ganglion;superior cervical ganglion;temporal lobe;globus pallidus;ciliary ganglion;kidney;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex; 0.20028 0.16452 -1.92362963 1.916725643 1140.864 6.44137 SLC6A20 6.44898031809492e-10 0.233184340329043 0.766815659026059 solute carrier family 6 member 20 FUNCTION: Mediates the calcium-dependent uptake of imino acids such as L-proline, N-methyl-L-proline and pipecolate as well as N- methylated amino acids. Involved in the transport of glycine. {ECO:0000269|PubMed:15632147, ECO:0000269|PubMed:19033659}.; DISEASE: Iminoglycinuria (IG) [MIM:242600]: A disorder of renal tubular reabsorption of glycine and imino acids (proline and hydroxyproline), marked by excessive levels of all three substances in the urine. {ECO:0000269|PubMed:19033659}. Note=The disease is caused by mutations affecting the gene represented in this entry. Haploinsufficiency of SLC6A20 combined with deficiency of the neutral amino acid transporter SLC6A19 or partially inactivating mutations in SLC36A2, is responsible for iminoglycinuria. Additional polymorphisms and mutations in SLC6A18 can contribute to the IG phenotype in some families.; TISSUE SPECIFICITY: Kidney and small intestine. Expressed in the S3 segment of the proximal tubule. {ECO:0000269|PubMed:19033659, ECO:0000269|PubMed:9932288}.; unclassifiable (Anatomical System);colon;choroid;skeletal muscle;retina;uterus;pancreas;optic nerve;lung;larynx;hippocampus;iris;head and neck;brain;stomach;peripheral nerve; superior cervical ganglion;temporal lobe;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10666 0.12174 -0.527216948 20.8893607 877.04178 5.76408 SLC6A21P . . . solute carrier family 6 member 21, pseudogene . . . . . . . . . . . SLC7A1 0.574964447374533 0.424547475639892 0.000488076985574935 solute carrier family 7 member 1 FUNCTION: High-affinity, low capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine) in non-hepatic tissues. May also function as an ecotropic retroviral leukemia receptor. {ECO:0000269|PubMed:10485994}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:1718082}.; . . 0.16280 0.30456 -1.219785504 5.602736494 15.98083 0.56655 SLC7A2 1.1726426517571e-08 0.541551483594322 0.458448504679251 solute carrier family 7 member 2 FUNCTION: Functions as permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine); the affinity for its substrates differs between isoforms created by alternative splicing. Isoform 1 functions as permease that mediates the transport of the cationic amino acids (arginine, lysine and ornithine), and it has much higher affinity for arginine than isoform 2. Isoform 2 functions as low-affinity, high capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine) (PubMed:9174363). May play a role in classical or alternative activation of macrophages via its role in arginine transport. {ECO:0000250|UniProtKB:P18581, ECO:0000269|PubMed:9174363}.; . TISSUE SPECIFICITY: Expressed at high levels in the skeletal muscle, placenta and ovary. Expressed at intermediate levels in the liver and pancreas and at low levels in the kidney and heart. {ECO:0000269|PubMed:8954799}.; unclassifiable (Anatomical System);heart;ovary;parathyroid;retina;breast;lung;placenta;thyroid;liver;amnion;testis;head and neck;spleen; dorsal root ganglion;superior cervical ganglion;parietal lobe; 0.10058 0.13882 0.409650696 76.53927813 761.78725 5.47266 SLC7A3 0.967794266173169 0.0321537709193361 5.19629074947075e-05 solute carrier family 7 member 3 FUNCTION: Mediates the uptake of the cationic amino acids arginine, lysine and ornithine in a sodium-independent manner. {ECO:0000269|PubMed:11591158}.; . TISSUE SPECIFICITY: Highly expressed in thymus, uterus and testis. Detected at lower levels in brain, mammary gland, prostate, salivary gland and fetal spleen. In brain, highest expression in thalamus, hippocampus and amygdala. {ECO:0000269|PubMed:11591158}.; unclassifiable (Anatomical System);ovary;endometrium;placenta;parathyroid;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.46332 0.15144 -0.468351206 23.42533616 1450.97808 7.10970 SLC7A4 0.000100465628178791 0.574730402667029 0.425169131704792 solute carrier family 7 member 4 FUNCTION: Involved in the transport of the cationic amino acids (arginine, lysine and ornithine).; . . . . 0.40821 0.14130 0.407828206 76.50979004 3384.13285 11.14077 SLC7A5 0.508496599514066 0.490675021739794 0.000828378746140299 solute carrier family 7 member 5 FUNCTION: Sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Involved in cellular amino acid uptake. Acts as an amino acid exchanger. Involved in the transport of L-DOPA across the blood- brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Plays a role in neuronal cell proliferation (neurogenesis) in brain. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L- nitrosocysteine (L-CNSO) across the transmembrane. May play an important role in high-grade gliomas. Mediates blood-to-retina L- leucine transport across the inner blood-retinal barrier which in turn may play a key role in maintaining large neutral amino acids as well as neurotransmitters in the neural retina. Acts as the major transporter of tyrosine in fibroblasts. {ECO:0000269|PubMed:10049700, ECO:0000269|PubMed:10391915, ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:11389679, ECO:0000269|PubMed:11557028, ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:11742812, ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:15769744, ECO:0000269|PubMed:16496379, ECO:0000269|PubMed:18262359, ECO:0000269|PubMed:9751058}.; . TISSUE SPECIFICITY: Expressed abundantly in adult lung, liver, brain, skeletal muscle, placenta, bone marrow, testis, resting lymphocytes and monocytes, and in fetal liver. Weaker expression in thymus, cornea, retina, peripheral leukocytes, spleen, kidney, colon and lymph node. During gestation, expression in the placenta was significantly stronger at full-term than at the mid-trimester stage. Also expressed in all human tumor cell lines tested and in the astrocytic process of primary astrocytic gliomas. Expressed in retinal endothelial cells and in the intestinal epithelial cell line Caco-2. {ECO:0000269|PubMed:10049700, ECO:0000269|PubMed:10072483, ECO:0000269|PubMed:11389679, ECO:0000269|PubMed:11557028, ECO:0000269|PubMed:11742812, ECO:0000269|PubMed:12824232, ECO:0000269|PubMed:1597461, ECO:0000269|PubMed:16027961, ECO:0000269|PubMed:16496379}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;oesophagus;larynx;bone;thyroid;iris;pituitary gland;testis;amniotic fluid;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;pharynx;blood;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; tumor;testis; 0.14668 0.25103 -0.001743238 53.85114414 132.75633 2.50603 SLC7A5P1 . . . solute carrier family 7 member 5 pseudogene 1 . . TISSUE SPECIFICITY: Expressed in peripheral blood mononuclear cells and lymphoid and myeloid cell lines. {ECO:0000269|PubMed:12009310}.; . . . 0.25103 . . . . SLC7A5P2 . . . solute carrier family 7 member 5 pseudogene 2 . . TISSUE SPECIFICITY: Expressed in peripheral blood mononuclear cells and lymphoid and myeloid cell lines. {ECO:0000269|PubMed:12009310}.; . . . . . . . . SLC7A6 0.0224285001107606 0.962119595464829 0.0154519044244101 solute carrier family 7 member 6 FUNCTION: Involved in the sodium-independent uptake of dibasic amino acids and sodium-dependent uptake of some neutral amino acids. Requires coexpression with SLC3A2/4F2hc to mediate the uptake of arginine, leucine and glutamine. Also acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Involved in the transport of L-arginine in monocytes. Reduces uptake of ornithine in retinal pigment epithelial (RPE) cells. {ECO:0000269|PubMed:10903140, ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:14603368, ECO:0000269|PubMed:15280038, ECO:0000269|PubMed:16785209, ECO:0000269|PubMed:17197568, ECO:0000269|PubMed:17329401, ECO:0000269|PubMed:9829974}.; . TISSUE SPECIFICITY: Expressed in normal fibroblasts and those from LPI patients. Also expressed in HUVECs, monocytes, RPE cells, and various carcinoma cell lines. {ECO:0000269|PubMed:11078698, ECO:0000269|PubMed:11742806, ECO:0000269|PubMed:14603368, ECO:0000269|PubMed:15280038, ECO:0000269|PubMed:17197568, ECO:0000269|PubMed:17329401}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;stomach;thymus; superior cervical ganglion;adipose tissue;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;thymus; 0.14524 0.10162 0.020302773 55.60863411 291.67644 3.65291 SLC7A6OS 0.807327025070433 0.191618345679464 0.00105462925010327 solute carrier family 7 member 6 opposite strand FUNCTION: Directs RNA polymerase II nuclear import. {ECO:0000250}.; . . medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;islets of Langerhans;muscle;pancreas;lung;pia mater;placenta;hypopharynx;head and neck;kidney;stomach;thymus; . 0.12463 . 0.749657564 86.56522765 513.8609 4.63826 SLC7A7 0.00209119496896398 0.978046944599605 0.0198618604314311 solute carrier family 7 member 7 FUNCTION: Involved in the sodium-independent uptake of dibasic amino acids and sodium-dependent uptake of some neutral amino acids. Requires coexpression with SLC3A2/4F2hc to mediate the uptake of arginine, leucine and glutamine. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Involved in the transport of L- arginine in monocytes. {ECO:0000269|PubMed:14603368, ECO:0000269|PubMed:15280038, ECO:0000269|PubMed:17329401, ECO:0000269|PubMed:9829974, ECO:0000269|PubMed:9878049}.; DISEASE: Lysinuric protein intolerance (LPI) [MIM:222700]: A metabolic disorder characterized by increased renal excretion of cationic amino acid (CAA), reduced CAA absorption from intestine, and orotic aciduria. On a normal diet, LPI patients present poor feeding, vomiting, diarrhea, episodes of hyperammoniaemic coma and growth retardation. Hepatosplenomegaly, osteoporosis and a life- threatening pulmonary involvement (alveolar proteinosis) are also seen. Biochemically LPI is characterized by defective transport of dibasic amino acids at the basolateral membrane of epithelial cells in kidney and intestine. {ECO:0000269|PubMed:10080182, ECO:0000269|PubMed:10631139, ECO:0000269|PubMed:10655553, ECO:0000269|PubMed:12402335, ECO:0000269|PubMed:15776427, ECO:0000269|PubMed:17764084, ECO:0000269|PubMed:9829974}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest expression in kidney and peripheral blood leukocytes. Weaker expression is observed in lung, heart, placenta, spleen, testis and small intestine. Expressed in normal fibroblasts and those from LPI patients. Also expressed in HUVECs, monocytes, retinal pigment epithelial cells, and various carcinoma cell lines, with highest expression in a colon-carcinoma cell line. {ECO:0000269|PubMed:10080183, ECO:0000269|PubMed:11078698, ECO:0000269|PubMed:11742806, ECO:0000269|PubMed:15280038, ECO:0000269|PubMed:17197568, ECO:0000269|PubMed:17329401, ECO:0000269|PubMed:9829974}.; colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;optic nerve;whole body;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;hippocampus;duodenum;alveolus;liver;spleen;kidney;mammary gland;stomach;aorta; testis;kidney; 0.35025 0.16277 -0.710864321 14.5730125 59.58927 1.56733 SLC7A8 0.000166180404409209 0.969620745647847 0.0302130739477435 solute carrier family 7 member 8 FUNCTION: Sodium-independent, high-affinity transport of small and large neutral amino acids such as alanine, serine, threonine, cysteine, phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Acts as an amino acid exchanger. Has higher affinity for L-phenylalanine than LAT1 but lower affinity for glutamine and serine. L-alanine is transported at physiological concentrations. Plays a role in basolateral (re)absorption of neutral amino acids. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Plays an essential role in the reabsorption of neutral amino acids from the epithelial cells to the bloodstream in the kidney. {ECO:0000269|PubMed:10391915, ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12716892, ECO:0000269|PubMed:15081149, ECO:0000269|PubMed:15769744, ECO:0000269|PubMed:15918515}.; . TISSUE SPECIFICITY: Strongest expression is observed in kidney and moderate expression in placenta and brain, followed by liver, prostate, testis, ovary, lymph node, thymus, spleen, skeletal muscle and heart. Also expressed in fetal liver as well as in the retinal pigment epithelial cell line ARPE-19 and the intestinal epithelial cell line Caco-2. {ECO:0000269|PubMed:10391915, ECO:0000269|PubMed:15081149, ECO:0000269|PubMed:15918515, ECO:0000269|PubMed:16027961}.; lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;iris;testis;brain;bladder;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; superior cervical ganglion;placenta;testis;kidney;trigeminal ganglion; 0.68540 0.12563 -0.066061882 48.77919321 187.90324 2.97624 SLC7A9 0.246082407596558 0.752570592680093 0.00134699972334952 solute carrier family 7 member 9 FUNCTION: Involved in the high-affinity, sodium-independent transport of cystine and neutral and dibasic amino acids (system b(0,+)-like activity). Thought to be responsible for the high- affinity reabsorption of cystine in the kidney tubule. {ECO:0000269|PubMed:10471498, ECO:0000269|PubMed:10588648, ECO:0000269|PubMed:16609684}.; . TISSUE SPECIFICITY: Expressed in the brush border membrane in the kidney (at protein level). Kidney, small intestine, liver and placenta. {ECO:0000269|PubMed:10471498, ECO:0000269|PubMed:12167606}.; unclassifiable (Anatomical System);colon;fovea centralis;choroid;lens;retina;prostate;optic nerve;lung;macula lutea;liver;testis;spleen;kidney;stomach; superior cervical ganglion;kidney;atrioventricular node;trigeminal ganglion; 0.15776 0.27325 -0.529034136 20.85987261 2700.38343 9.78090 SLC7A10 0.00157745429809636 0.969294571174807 0.0291279745270962 solute carrier family 7 member 10 FUNCTION: Sodium-independent, high affinity transport of small neutral D- and L-amino acids. May play a role in the modulation of glutamatergic transmission through mobilization of D-serine at the glutamatergic synapse. {ECO:0000269|PubMed:10863037}.; . TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, pancreas, placenta, and skeletal muscle. {ECO:0000269|PubMed:10863037}.; unclassifiable (Anatomical System);heart;ovary;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;frontal lobe;endometrium;placenta;bone;macula lutea;brain; amygdala;superior cervical ganglion;occipital lobe;testis - interstitial; 0.10590 0.12650 -0.574945567 18.90186365 443.11023 4.38052 SLC7A11 0.000970108502996297 0.986660662260473 0.0123692292365303 solute carrier family 7 member 11 FUNCTION: Sodium-independent, high-affinity exchange of anionic amino acids with high specificity for anionic form of cystine and glutamate. {ECO:0000269|PubMed:15151999}.; . . unclassifiable (Anatomical System);uterus;lung;trabecular meshwork;blood;skin;skeletal muscle; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.21210 0.19503 0.220536484 68.38287332 139.1896 2.57177 SLC7A11-AS1 . . . SLC7A11 antisense RNA 1 . . . . . . . . . . . SLC7A13 4.70688995096023e-15 0.000905116578370444 0.999094883421625 solute carrier family 7 member 13 FUNCTION: Mediates the transport L-aspartate and L-glutamate in a sodium-independent manner. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the kidney. {ECO:0000269|PubMed:11943479}.; kidney; . 0.17503 0.14371 1.932845308 97.48171739 4179.01352 12.84003 SLC7A14 0.332594381838482 0.666754839508763 0.000650778652754882 solute carrier family 7 member 14 FUNCTION: May be involved in arginine transport. {ECO:0000269|PubMed:22787143, ECO:0000269|PubMed:24670872}.; . TISSUE SPECIFICITY: Expressed in skin fibroblasts. {ECO:0000269|PubMed:22787143}.; unclassifiable (Anatomical System);optic nerve;lung;larynx;hypothalamus;macula lutea;testis;head and neck;fovea centralis;choroid;lens;brain;retina; parietal lobe; 0.16057 0.12305 -1.082044518 7.242274121 379.77217 4.10968 SLC7A15P . . . solute carrier family 7 member 15, pseudogene . . . . . . . . . . . SLC8A1 0.98820862479259 0.0117911958860724 1.79321337888836e-07 solute carrier family 8 member A1 FUNCTION: Mediates the exchange of one Ca(2+) ion against three to four Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)- dependent cellular processes (PubMed:1374913, PubMed:11241183, PubMed:1476165). Contributes to Ca(2+) transport during excitation-contraction coupling in muscle. In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum. SLC8A1 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline. Required for normal embryonic heart development and the onset of heart contractions. {ECO:0000250|UniProtKB:P70414, ECO:0000269|PubMed:11241183, ECO:0000269|PubMed:1374913, ECO:0000269|PubMed:1476165}.; . TISSUE SPECIFICITY: Detected primarily in heart and at lower levels in brain (PubMed:1374913). Expressed in cardiac sarcolemma, brain, kidney, liver, pancreas, skeletal muscle, placenta and lung (PubMed:1476165). {ECO:0000269|PubMed:1374913, ECO:0000269|PubMed:1476165}.; unclassifiable (Anatomical System);uterus;frontal lobe;heart;islets of Langerhans;liver;blood;kidney;skeletal muscle; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.39209 0.22102 -1.150005948 6.286860109 50.78753 1.40415 SLC8A1-AS1 . . . SLC8A1 antisense RNA 1 . . . . . . . . . . . SLC8A2 . . . solute carrier family 8 member A2 FUNCTION: Mediates the electrogenic exchange of Ca(2+) against Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes. Contributes to cellular Ca(2+) homeostasis in excitable cells. Contributes to the rapid decrease of cytoplasmic Ca(2+) levels back to baseline after neuronal activation, and thereby contributes to modulate synaptic plasticity, learning and memory. Plays a role in regulating urinary Ca(2+) and Na(+) excretion. {ECO:0000250|UniProtKB:Q8K596}.; . . unclassifiable (Anatomical System);islets of Langerhans;pineal body;choroid;fovea centralis;lens;retina;uterus;optic nerve;macula lutea;testis;brain;cerebellum; whole brain;amygdala;occipital lobe;medulla oblongata;cerebellum peduncles;caudate nucleus;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.31664 0.14181 -1.001120478 8.321538099 15.58122 0.55594 SLC8A3 0.621079527402869 0.378853483121993 6.69894751371837e-05 solute carrier family 8 member A3 FUNCTION: Mediates the electrogenic exchange of Ca(2+) against Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes. Contributes to cellular Ca(2+) homeostasis in excitable cells, both in muscle and in brain. In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum. SLC8A3 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline. Contributes to Ca(2+) transport during excitation-contraction coupling in muscle. In neurons, contributes to the rapid decrease of cytoplasmic Ca(2+) levels back to baseline after neuronal activation, and thereby contributes to modulate synaptic plasticity, learning and memory (By similarity). Required for normal oligodendrocyte differentiation and for normal myelination (PubMed:21959935). Mediates Ca(2+) efflux from mitochondria and contributes to mitochondrial Ca(2+) ion homeostasis (By similarity). {ECO:0000250|UniProtKB:S4R2P9, ECO:0000269|PubMed:21959935}.; . TISSUE SPECIFICITY: Isoform 2 is expressed in brain and skeletal muscle. Isoform 3 is expressed in excitable cells of brain, retina and skeletal muscle. Isoform 4 is expressed in skeletal muscle. {ECO:0000269|PubMed:15777725}.; unclassifiable (Anatomical System);optic nerve;macula lutea;fovea centralis;choroid;lens;brain;skeletal muscle;retina; superior cervical ganglion;subthalamic nucleus;pons;trigeminal ganglion; 0.82269 0.15732 -1.058182374 7.554847841 223.95056 3.23543 SLC8B1 5.47604607149263e-10 0.375150856378332 0.624849143074064 solute carrier family 8 member B1 FUNCTION: Mitochondrial sodium/calcium antiporter that mediates sodium-dependent calcium efflux from mitochondrion, thereby acting as a key regulator of mitochondrion calcium homeostasis. Regulates rates of glucose-dependent insulin secretion in pancreatic beta- cells during the first phase of insulin secretion: acts by mediating efflux of calcium from mitochondrion, thereby affecting cytoplasmic calcium responses. Able to transport Ca(2+) in exchange of either Li(+) or Na(+), explaining how Li(+) catalyzes Ca(2+) exchange. In contrast to other members of the family its function is independent of K(+). {ECO:0000269|PubMed:15060069, ECO:0000269|PubMed:20018762, ECO:0000269|PubMed:22829870, ECO:0000269|PubMed:23056385}.; . TISSUE SPECIFICITY: Present in pancreatic beta-cells (at protein level). {ECO:0000269|PubMed:23056385}.; . . 0.36451 . -0.995664936 8.539749941 601.75368 4.96418 SLC9A1 0.952228129998873 0.0477707142344607 1.1557666659348e-06 solute carrier family 9 member A1 FUNCTION: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction. {ECO:0000269|PubMed:11350981, ECO:0000269|PubMed:15035633, ECO:0000269|PubMed:8901634}.; DISEASE: Lichtenstein-Knorr syndrome (LIKNS) [MIM:616291]: An autosomal recessive neurologic disorder characterized by progressive cerebellar ataxia and severe progressive sensorineural hearing loss. {ECO:0000269|PubMed:25205112}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Kidney and intestine.; ovary;salivary gland;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;oesophagus;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;placenta; 0.41652 0.45973 -1.618506764 2.925218212 52.35151 1.42999 SLC9A2 0.481161337483386 0.518836940301916 1.72221469791194e-06 solute carrier family 9 member A2 FUNCTION: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Seems to play an important role in colonic sodium absorption.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, colon and kidney. Lower levels in the testis, prostate, ovary, and small intestine.; ovary;placenta;testis;colon;parathyroid;brain;skeletal muscle;stomach; testis - seminiferous tubule;liver;testis;trigeminal ganglion;cingulate cortex; 0.54940 0.18861 -0.378346116 28.01368247 46.58079 1.31787 SLC9A3 0.988153998366091 0.0118459649344154 3.66994938406276e-08 solute carrier family 9 member A3 FUNCTION: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction.; . . unclassifiable (Anatomical System);lung;trachea;lacrimal gland;colon;brain;cerebellum; uterus corpus;superior cervical ganglion;ciliary ganglion;atrioventricular node;parietal lobe;cingulate cortex;skeletal muscle; 0.13048 0.09910 -1.785892633 2.25878745 215.86732 3.17181 SLC9A3P1 . . . solute carrier family 9 member 3 pseudogene 1 . . . . . . . . . . . SLC9A3P2 . . . solute carrier family 9 member 3 pseudogene 2 . . . . . . . . . . . SLC9A3P3 . . . solute carrier family 9 member 3 pseudogene 3 . . . . . . . . . . . SLC9A3R1 6.3597388529883e-05 0.477634305734493 0.522302096876977 SLC9A3 regulator 1 FUNCTION: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for recycling of internalized ADRB2. Was first known to play a role in the regulation of the activity and subcellular location of SLC9A3. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May enhance Wnt signaling. May participate in HTR4 targeting to microvilli (By similarity). Involved in the regulation of phosphate reabsorption in the renal proximal tubules. Involved in sperm capacitation. May participate in the regulation of the chloride and bicarbonate homeostasis in spermatozoa. {ECO:0000250, ECO:0000269|PubMed:10499588, ECO:0000269|PubMed:18784102, ECO:0000269|PubMed:9096337, ECO:0000269|PubMed:9430655}.; DISEASE: Nephrolithiasis/osteoporosis, hypophosphatemic, 2 (NPHLOP2) [MIM:612287]: A disease characterized by decreased renal phosphate absorption, renal phosphate wasting, hypophosphatemia, hyperphosphaturia, hypercalciuria, nephrolithiasis and osteoporosis. {ECO:0000269|PubMed:18784102, ECO:0000269|PubMed:22506049}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in liver, kidney, pancreas, prostate, spleen, small intestine and placenta, in particular in the syncytiotrophoblast. {ECO:0000269|PubMed:9096337, ECO:0000269|PubMed:9314537}.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;oesophagus;endometrium;bone;thyroid;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;breast;pancreas;lung;mesenchyma;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;liver;kidney;trigeminal ganglion; 0.18165 0.49827 0.306902668 72.38145789 129.32063 2.47923 SLC9A3R2 0.0227037623698413 0.911511791936168 0.0657844456939909 SLC9A3 regulator 2 FUNCTION: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3 (PubMed:18829453). May also act as scaffold protein in the nucleus. {ECO:0000269|PubMed:10455146, ECO:0000269|PubMed:18829453, ECO:0000269|PubMed:9096337}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9054412, ECO:0000269|PubMed:9096337}.; . . 0.19491 0.23678 0.442818085 77.8544468 378.00378 4.09883 SLC9A4 1.58073058570014e-06 0.960431391454759 0.0395670278146552 solute carrier family 9 member A4 FUNCTION: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction. May play a specialized role in the kidney in rectifying cell volume in response to extreme fluctuations of hyperosmolar-stimulated cell shrinkage. Is relatively amiloride and ethylisopropylamiloride (EIPA) insensitive. Can be activated under conditions of hyperosmolar-induced cell shrinkage in a sustained intracellular acidification-dependence manner. Activated by 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS) in a sustained intracellular acidification-dependence manner. Affects potassium/proton exchange as well as sodium/proton and lithium/proton exchange. In basolateral cell membrane, participates in homeostatic control of intracellular pH, and may play a role in proton extrusion in order to achieve transepithelial HCO3(-) secretion. In apical cell membrane may be involved in mediating sodium absorption. Requires for normal levels of gastric acid secretion, secretory membrane development, parietal cell maturation and/or differentiation and at least secondarily for chief cell differentiation (By similarity). {ECO:0000250}.; . . testis; . 0.14001 0.10690 0.850585932 88.49374853 448.61554 4.40494 SLC9A5 0.0362519257358633 0.963735021354109 1.30529100278925e-05 solute carrier family 9 member A5 FUNCTION: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, testis, spleen, and skeletal muscle.; unclassifiable (Anatomical System);uterus;lung;whole body;bone;thyroid;liver;testis;head and neck;spleen;germinal center;brain; superior cervical ganglion;atrioventricular node; 0.32414 0.12612 -0.865195027 10.79853739 86.06036 1.98043 SLC9A6 0.975667933500175 0.0243310001177244 1.06638210031075e-06 solute carrier family 9 member A6 FUNCTION: Electroneutral exchange of protons for Na(+) and K(+) across the early and recycling endosome membranes. Contributes to calcium homeostasis.; . TISSUE SPECIFICITY: Ubiquitous; but is most abundant in mitochondrion-rich tissues such as brain, skeletal muscle and heart.; . . 0.44771 0.11224 -0.183570861 39.95046001 11.40529 0.41173 SLC9A7 0.953699986952486 0.0462947332771615 5.27977035245208e-06 solute carrier family 9 member A7 FUNCTION: Mediates electroneutral exchange of protons for Na(+) and K(+) across endomembranes. May contribute to Golgi volume and cation homeostasis. {ECO:0000269|PubMed:11279194}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11279194}.; . . 0.55161 0.14089 -0.558357437 19.54470394 39.79653 1.17265 SLC9A7P1 . . . solute carrier family 9 member 7 pseudogene 1 . . . . . . . . . . . SLC9A8 2.81662458191787e-05 0.983591565969693 0.0163802677844883 solute carrier family 9 member A8 FUNCTION: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction. {ECO:0000269|PubMed:15522866}.; . TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in skeletal muscle and kidney. {ECO:0000269|PubMed:15522866}.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06517 0.15107 -0.666770504 15.86459071 202.63697 3.07202 SLC9A9 2.47740520992669e-08 0.892869014584457 0.107130960641491 solute carrier family 9 member A9 FUNCTION: May act in electroneutral exchange of protons for Na(+) across membranes. Involved in the effusion of Golgi luminal H(+) in exchange for cytosolic cations. Involved in organelle ion homeostasis by contributing to the maintenance of the unique acidic pH values of the Golgi and post-Golgi compartments in the cell. {ECO:0000269|PubMed:15522866}.; DISEASE: Autism 16 (AUTS16) [MIM:613410]: A complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation. AUTS16 can be associated with epilepsy. {ECO:0000269|PubMed:18621663}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed in all tissues tested. Expressed at highest levels in heart and skeletal muscle, followed by placenta, kidney, and liver. Expressed in the brain, in the medulla and spinal cord. {ECO:0000269|PubMed:14569117, ECO:0000269|PubMed:15522866}.; ovary;salivary gland;intestine;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;synovium;bone;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;peripheral nerve; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.23330 . -0.861560326 10.89289927 243.35989 3.36696 SLC9A9-AS1 . . . SLC9A9 antisense RNA 1 . . . . . . . . . . . SLC9A9-AS2 . . . SLC9A9 antisense RNA 2 . . . . . . . . . . . SLC9B1 8.48795187528449e-05 0.928568641966973 0.0713464785142741 solute carrier family 9 member B1 . . TISSUE SPECIFICITY: Expressed only in the testis. {ECO:0000269|PubMed:16850186}.; unclassifiable (Anatomical System);medulla oblongata;pancreas;lung;whole body;ovary;heart;islets of Langerhans;placenta;visual apparatus;hippocampus;testis;parathyroid; dorsal root ganglion;superior cervical ganglion;testis - interstitial;temporal lobe;atrioventricular node;skeletal muscle;skin;testis - seminiferous tubule;globus pallidus;appendix;testis;ciliary ganglion;trigeminal ganglion; 0.17169 0.08398 0.262810045 70.43524416 40.0995 1.17847 SLC9B1P1 . . . solute carrier family 9 member B1 pseudogene 1 . . . . . . . . . . . SLC9B1P2 . . . solute carrier family 9 member B1 pseudogene 2 . . . . . . . . . . . SLC9B1P3 . . . solute carrier family 9 member B1 pseudogene 3 . . . . . . . . . . . SLC9B1P4 . . . solute carrier family 9 member B1 pseudogene 4 . . . . . . . . . . . SLC9B1P5 . . . solute carrier family 9 member B1 pseudogene 5 . . . . . . . . . . . SLC9B2 0.067056661977643 0.929991360173777 0.00295197784857946 solute carrier family 9 member B2 FUNCTION: Electroneutral exchange of protons for Na(+) and Li(+) across the inner mitochondrial membrane. Contributes to the organellar volume homeostasis. Required for osteoclast differentiation and bone resorption activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:18000046}.; . TISSUE SPECIFICITY: Detected in red blood cells (at protein level).; unclassifiable (Anatomical System);heart;islets of Langerhans;spinal cord;blood;skin;retina;uterus;breast;pancreas;lung;cochlea;placenta;visual apparatus;iris;liver;testis;brain;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.12211 0.10641 0.576916344 82.25406936 1699.25294 7.59973 SLC9C1 7.81673916364206e-11 0.99249374648132 0.00750625344051229 solute carrier family 9 member C1 FUNCTION: Sperm-specific sodium/hydrogen exchanger involved in intracellular pH regulation of spermatozoa. Required for sperm motility and fertility. Involved in sperm cell hyperactivation, a step needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for the expression and bicarbonate regulation of the soluble adenylyl cyclase (sAC) (By similarity). {ECO:0000250}.; . . . . 0.03558 0.05202 1.631430616 96.06628922 6774.45187 17.48499 SLC9C2 1.18824028993333e-06 0.999888590358758 0.000110221400952163 solute carrier family 9 member C2 (putative) FUNCTION: Involved in pH regulation. {ECO:0000250}.; . . . . 0.03736 0.05990 0.380318343 75.63104506 2341.17161 8.96173 SLC10A1 8.44088192990943e-16 0.000170614886268269 0.999829385113731 solute carrier family 10 member 1 FUNCTION: The hepatic sodium/bile acid uptake system exhibits broad substrate specificity and transports various non-bile acid organic compounds as well. It is strictly dependent on the extracellular presence of sodium.; . . thyroid;liver;spleen;head and neck;skeletal muscle; superior cervical ganglion;liver;pons;atrioventricular node;trigeminal ganglion; 0.09493 0.34834 -0.88906181 10.36801132 249.30704 3.40278 SLC10A2 1.60745645494627e-13 0.00195276575692907 0.99804723424291 solute carrier family 10 member 2 FUNCTION: Plays a critical role in the sodium-dependent reabsorption of bile acids from the lumen of the small intestine. Plays a key role in cholesterol metabolism.; DISEASE: Primary bile acid malabsorption (PBAM) [MIM:613291]: An intestinal disorder associated with chronic watery diarrhea, excess fecal bile acids, steatorrhea and interruption of the enterohepatic circulation of bile acids. {ECO:0000269|PubMed:9109432}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lung;spleen;kidney; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.28091 0.32008 -0.108334733 45.57088936 249.98412 3.40619 SLC10A3 0.629239798913129 0.340516090155681 0.03024411093119 solute carrier family 10 member 3 FUNCTION: The ubiquitous expression and the conservation of the sequence in distant animal species suggest that the gene codes for a protein with housekeeping functions.; . . unclassifiable (Anatomical System);lymph node;cartilage;ovary;heart;urinary;colon;skin;uterus;prostate;pancreas;optic nerve;whole body;lung;endometrium;larynx;thyroid;placenta;testis;cervix;head and neck;kidney;brain;aorta;stomach; adrenal gland;placenta;white blood cells; 0.27723 0.13229 -0.337894035 30.37272942 57.49038 1.52927 SLC10A4 0.167299362234621 0.771814238699325 0.0608863990660548 solute carrier family 10 member 4 FUNCTION: Transporter for bile acids. {ECO:0000269|PubMed:23589386}.; . TISSUE SPECIFICITY: Highly expressed in brain and small intestine, and moderately expressed in colon, heart, prostate, and testis. Very low levels were detected in kidney, liver, ovary, placenta, spleen, and thymus. {ECO:0000269|PubMed:18355966}.; unclassifiable (Anatomical System);ovary;salivary gland;pharynx;colon;blood;breast;prostate;lung;visual apparatus;liver;kidney;bladder;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.04161 . . . 57.29346 1.52517 SLC10A5 0.000395027314980564 0.399600432646745 0.600004540038274 solute carrier family 10 member 5 . . . . . 0.24435 . 0.951720429 90.06251474 215.51394 3.16859 SLC10A5P1 . . . SLC10A5 pseudogene 1 . . . . . 0.24435 . . . . . SLC10A6 1.84221510783847e-06 0.254472514642818 0.745525643142075 solute carrier family 10 member 6 FUNCTION: Transports sulfoconjugated steroid hormones, as well as taurolithocholic acid-3-sulfate and sulfoconjugated pyrenes in a sodium-dependent manner. {ECO:0000269|PubMed:17491011}.; . TISSUE SPECIFICITY: Highly expressed in testis, placenta and pancreas. Moderately expressed in heart, lung and mammary gland. Weakly expressed in brain, colon, kidney, liver, ovary, prostate, small intestine, spleen and thymus. {ECO:0000269|PubMed:17491011}.; tongue;hypopharynx;head and neck; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11279 0.10499 0.573279816 82.08303845 812.18471 5.60461 SLC10A7 0.0288074279323974 0.960451066947683 0.0107415051199195 solute carrier family 10 member 7 . . . unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;colon;skin;skeletal muscle;breast;uterus;prostate;whole body;lung;larynx;bone;placenta;hippocampus;liver;testis;head and neck;spleen;germinal center;kidney;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin; 0.24912 0.11203 0.283038099 71.26680821 56.42429 1.51005 SLC11A1 6.5921175084613e-12 0.118539940351368 0.88146005964204 solute carrier family 11 member 1 FUNCTION: Divalent transition metal (iron and manganese) transporter involved in iron metabolism and host resistance to certain pathogens. Macrophage-specific membrane transport function. Controls natural resistance to infection with intracellular parasites. Pathogen resistance involves sequestration of Fe(2+) and Mn(2+), cofactors of both prokaryotic and eukaryotic catalases and superoxide dismutases, not only to protect the macrophage against its own generation of reactive oxygen species, but to deny the cations to the pathogen for synthesis of its protective enzymes.; . TISSUE SPECIFICITY: Macrophages; peripheral blood leukocytes, lung, spleen and liver.; unclassifiable (Anatomical System);ovary;cartilage;colon;fovea centralis;choroid;lens;skeletal muscle;retina;breast;pancreas;optic nerve;whole body;lung;placenta;macula lutea;testis;spleen;germinal center;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12272 0.33858 -0.506987379 21.76810569 386.8452 4.14241 SLC11A2 0.00623523691810572 0.992896181688567 0.000868581393326984 solute carrier family 11 member 2 FUNCTION: Important in metal transport, in particular iron. Can also transport manganese, cobalt, cadmium, nickel, vanadium and lead. Involved in apical iron uptake into duodenal enterocytes. Involved in iron transport from acidified endosomes into the cytoplasm of erythroid precursor cells. May play an important role in hepatic iron accumulation and tissue iron distribution. May serve to import iron into the mitochondria. {ECO:0000269|PubMed:17109629, ECO:0000269|PubMed:24448823, ECO:0000269|PubMed:25326704, ECO:0000269|PubMed:25491917}.; DISEASE: Anemia, hypochromic microcytic, with iron overload 1 (AHMIO1) [MIM:206100]: A hematologic disease characterized by abnormal hemoglobin content in the erythrocytes which are reduced in size. The disorder is due to an error of iron metabolism that results in high serum iron, massive hepatic iron deposition, and absence of sideroblasts and stainable bone marrow iron store. Despite adequate transferrin-iron complex, delivery of iron to the erythroid bone marrow is apparently insufficient for the demands of hemoglobin synthesis. {ECO:0000269|PubMed:15459009, ECO:0000269|PubMed:16160008, ECO:0000269|PubMed:16439678}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 1 is highly expressed in brain. Isoform 2 is highly expressed in spleen, thymus and pancreas. Isoform 3 and isoform 4 are abundantly expressed in duodenum and kidney. {ECO:0000269|PubMed:12209011, ECO:0000269|PubMed:9642100}.; ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;amygdala;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; occipital lobe;superior cervical ganglion;hypothalamus;spinal cord;prefrontal cortex;parietal lobe; 0.55670 0.38199 0.308721233 72.59966973 138.02468 2.55775 SLC12A1 2.65435277088282e-07 0.999053435277726 0.00094629928699715 solute carrier family 12 member 1 FUNCTION: Electrically silent transporter system. Mediates sodium and chloride reabsorption. Plays a vital role in the regulation of ionic balance and cell volume.; . TISSUE SPECIFICITY: Kidney specific.; unclassifiable (Anatomical System);colon;kidney;brain;stomach; superior cervical ganglion;kidney;trigeminal ganglion; 0.55862 0.10473 -0.834069467 11.49445624 503.21659 4.60287 SLC12A2 0.999438621805128 0.000561378193993525 8.78936358367503e-13 solute carrier family 12 member 2 FUNCTION: Electrically silent transporter system. Mediates sodium and chloride reabsorption. Plays a vital role in the regulation of ionic balance and cell volume.; . TISSUE SPECIFICITY: Expressed in many tissues.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;cochlea;endometrium;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;spinal cord;urinary;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - interstitial;trachea;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.22943 0.31452 -1.30798293 4.877329559 115.75595 2.34001 SLC12A3 5.54410952233344e-18 0.0828614401232084 0.917138559876792 solute carrier family 12 member 3 FUNCTION: Key mediator of sodium and chloride reabsorption in this nephron segment, accounting for a significant fraction of renal sodium reabsorption. {ECO:0000269|PubMed:8528245}.; DISEASE: Gitelman syndrome (GS) [MIM:263800]: An autosomal recessive disorder characterized by hypokalemic alkalosis in combination with hypomagnesemia, low urinary calcium, and increased renin activity associated with normal blood pressure. Patients are often asymptomatic or present transient periods of muscular weakness and tetany, usually accompanied by abdominal pain, vomiting and fever. The phenotype is highly heterogeneous in terms of age at onset and severity. Cardinal features such as hypocalciuria and hypomagnesemia might also change during the life cycle of a given patient. It has overlapping features with Bartter syndrome. {ECO:0000269|PubMed:10616841, ECO:0000269|PubMed:10988270, ECO:0000269|PubMed:11168953, ECO:0000269|PubMed:11940055, ECO:0000269|PubMed:12008755, ECO:0000269|PubMed:12112667, ECO:0000269|PubMed:15069170, ECO:0000269|PubMed:15687331, ECO:0000269|PubMed:16429844, ECO:0000269|PubMed:17654016, ECO:0000269|PubMed:17873326, ECO:0000269|PubMed:8528245, ECO:0000269|PubMed:8900229, ECO:0000269|PubMed:8954067, ECO:0000269|PubMed:9734597}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominant in kidney.; unclassifiable (Anatomical System);placenta;cervix;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.23844 0.27772 -1.624320968 2.889832508 1196.53825 6.56344 SLC12A4 1.82559229552341e-07 0.999671589830316 0.000328227610454809 solute carrier family 12 member 4 FUNCTION: Mediates electroneutral potassium-chloride cotransport when activated by cell swelling. May contribute to cell volume homeostasis in single cells. May be involved in the regulation of basolateral Cl(-) exit in NaCl absorbing epithelia (By similarity). Isoform 4 has no transport activity. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. Levels are much higher in erythrocytes from patients with Hb SC and Hb SS compared to normal AA erythrocytes. This may contribute to red blood cell dehydration and to the manifestation of sickle cell disease by increasing the intracellular concentration of HbS. Isoform 1 was not detected in circulating reticulocytes.; ovary;foreskin;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;urinary;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.42899 0.27241 -1.918226659 1.934418495 398.3896 4.19285 SLC12A5 0.999987272496915 1.2727503074062e-05 1.04614203687197e-14 solute carrier family 12 member 5 FUNCTION: Mediates electroneutral potassium-chloride cotransport in mature neurons and is required for neuronal Cl(-) homeostasis. As major extruder of intracellular chloride, it establishes the low neuronal Cl(-) levels required for chloride influx after binding of GABA-A and glycine to their receptors, with subsequent hyperpolarization and neuronal inhibition (By similarity). Involved in the regulation of dendritic spine formation and maturation (PubMed:24668262). {ECO:0000250|UniProtKB:Q63633, ECO:0000269|PubMed:24668262}.; . TISSUE SPECIFICITY: Brain specific. Detected in neuronal cells.; unclassifiable (Anatomical System);cerebellum cortex;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;lung;frontal lobe;macula lutea;visual apparatus;pituitary gland;testis;brain;cerebellum; amygdala;whole brain;thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.61306 0.15258 -1.372317395 4.446803491 184.74467 2.95032 SLC12A6 0.97817997330196 0.0218200266867235 1.13167696730716e-11 solute carrier family 12 member 6 FUNCTION: Mediates electroneutral potassium-chloride cotransport. May be activated by cell swelling. May contribute to cell volume homeostasis in single cells.; DISEASE: Agenesis of the corpus callosum, with peripheral neuropathy (ACCPN) [MIM:218000]: A disease that is characterized by severe progressive sensorimotor neuropathy, mental retardation, dysmorphic features and complete or partial agenesis of the corpus callosum. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in heart, brain and kidney. Detected at lower levels in skeletal muscle, placenta, lung and pancreas. Detected in umbilical vein endothelial cells. Isoform 2 is more abundant in kidney. Isoform 5 is testis specific. Expressed in the proximal tubule of the kidney (at protein level). {ECO:0000269|PubMed:16048901}.; unclassifiable (Anatomical System);ovary;blood;fovea centralis;skeletal muscle;bone marrow;uterus;breast;lung;endometrium;bone;placenta;macula lutea;testis;kidney;brain;artery;aorta; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.38135 0.26221 -1.129772626 6.505071951 75.64274 1.82151 SLC12A7 8.45108944554302e-11 0.968735952852885 0.0312640470626041 solute carrier family 12 member 7 FUNCTION: Mediates electroneutral potassium-chloride cotransport when activated by cell swelling. May mediate K(+) uptake into Deiters' cells in the cochlea and contribute to K(+) recycling in the inner ear. Important for the survival of cochlear outer and inner hair cells and the maintenance of the organ of Corti. May be required for basolateral Cl(-) extrusion in the kidney and contribute to renal acidification (By similarity). {ECO:0000250, ECO:0000269|PubMed:10913127}.; . TISSUE SPECIFICITY: Detected in muscle, brain, lung, heart and kidney.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;cerebral cortex;endometrium;iris;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis;kidney; 0.09754 . -2.793650711 0.654635527 209.87901 3.12733 SLC12A8 7.93459144299657e-13 0.0671179941788834 0.932882005820323 solute carrier family 12 member 8 FUNCTION: Cation/chloride cotransporter that may play a role in the control of keratinocyte proliferation. {ECO:0000269|PubMed:11863360}.; . TISSUE SPECIFICITY: Ubiquitous with very low level in normal skin. {ECO:0000269|PubMed:11863360}.; unclassifiable (Anatomical System);ovary;tongue;colon;parathyroid;skeletal muscle;prostate;lung;oesophagus;endometrium;placenta;visual apparatus;hypopharynx;head and neck;cervix;brain;stomach; thyroid;trigeminal ganglion;fetal thyroid; . . 0.674210096 84.7487615 710.69205 5.29772 SLC12A9 2.37211122104682e-06 0.976967907584251 0.0230297203045282 solute carrier family 12 member 9 FUNCTION: May be an inhibitor of SLC12A1. Seems to correspond to a subunit of a multimeric transport system and thus, additional subunits may be required for its function. {ECO:0000269|PubMed:10871601}.; . TISSUE SPECIFICITY: Highly expressed in placenta, brain and kidney. Lower expression in lung, liver and heart.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;hippocampus;visual apparatus;cervix;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.23194 0.15806 -1.168429872 6.062750649 76.20765 1.82962 SLC13A1 1.83879119780268e-09 0.622767168469452 0.377232829691757 solute carrier family 13 member 1 FUNCTION: Sodium/sulfate cotransporter that mediates sulfate reabsorption in the kidney.; . TISSUE SPECIFICITY: Highly expressed in kidney; not detectable in the other tissues tested.; endometrium;kidney; superior cervical ganglion;temporal lobe;ciliary ganglion;kidney;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.24397 0.14498 0.42259095 77.22929936 127.90486 2.46589 SLC13A2 8.28516014334455e-07 0.911844051196575 0.0881551202874104 solute carrier family 13 member 2 FUNCTION: Cotransport of sodium ions and dicarboxylates such as succinate and citrate.; . . unclassifiable (Anatomical System);prostate;lacrimal gland;visual apparatus;colon;kidney;stomach; superior cervical ganglion;ciliary ganglion;kidney;trigeminal ganglion;skeletal muscle; 0.26475 . -0.374708069 28.15522529 3412.46723 11.19598 SLC13A3 0.0532868032183935 0.94584739925392 0.000865797527686798 solute carrier family 13 member 3 FUNCTION: High-affinity sodium-dicarboxylate cotransporter that accepts a range of substrates with 4-5 carbon atoms. The stoichiometry is probably 3 Na(+) for 1 divalent succinate.; . TISSUE SPECIFICITY: Expression is highest in kidney. Detected in placenta, brain, liver and pancreas.; unclassifiable (Anatomical System);hypothalamus;colon;substantia nigra;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;frontal lobe;cochlea;placenta;macula lutea;visual apparatus;liver;testis;kidney;brain;stomach; superior cervical ganglion;olfactory bulb;ciliary ganglion;kidney;atrioventricular node;caudate nucleus;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.31817 0.17348 -0.821100135 11.88369899 98.00172 2.13993 SLC13A4 0.915550850591339 0.0844442515333803 4.89787528085246e-06 solute carrier family 13 member 4 FUNCTION: Sodium/sulfate cotransporter that mediates sulfate reabsorption in the high endothelial venules (HEV). {ECO:0000269|PubMed:10535998, ECO:0000269|PubMed:15607730}.; . TISSUE SPECIFICITY: Highly expressed in placenta and testis with intermediate levels in brain and lower levels in heart, thymus and liver. {ECO:0000269|PubMed:10535998, ECO:0000269|PubMed:15607730}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;optic nerve;testis;germinal center;dura mater;bladder;brain;unclassifiable (Anatomical System);meninges;islets of Langerhans;lens;lung;pia mater;placenta;hippocampus;visual apparatus;macula lutea;liver;cervix;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;thalamus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.11026 0.16063 -0.578583623 18.71903751 150.0444 2.67085 SLC13A5 0.353400874150624 0.646046769870389 0.000552355978987094 solute carrier family 13 member 5 FUNCTION: High-affinity sodium/citrate cotransporter that mediates citrate entry into cells. The transport process is electrogenic; it is the trivalent form of citrate rather than the divalent form that is recognized as a substrate. May facilitate the utilization of circulating citrate for the generation of metabolic energy and for the synthesis of fatty acids and cholesterol. {ECO:0000269|PubMed:12445824}.; . TISSUE SPECIFICITY: Expressed most predominantly in the liver, with moderate expression detectable in the brain and testis. {ECO:0000269|PubMed:12445824}.; unclassifiable (Anatomical System);tongue;fovea centralis;choroid;lens;skeletal muscle;retina;pancreas;optic nerve;lung;larynx;macula lutea;liver;testis;head and neck;spleen;brain;gall bladder;cerebellum; fetal liver;superior cervical ganglion;liver;atrioventricular node; 0.09073 0.12078 -1.397999468 4.193205945 38.95546 1.15407 SLC14A1 1.90357446794666e-09 0.0668600051413674 0.933139992955058 solute carrier family 14 member 1 (Kidd blood group) FUNCTION: Urea channel that facilitates transmembrane urea transport down a concentration gradient. A constriction of the transmembrane channel functions as selectivity filter through which urea is expected to pass in dehydrated form. The rate of urea conduction is increased by hypotonic stress. Plays an important role in the kidney medulla collecting ducts, where it allows rapid equilibration between the lumen of the collecting ducts and the interstitium, and thereby prevents water loss driven by the high concentration of urea in the urine. Facilitates urea transport across erythrocyte membranes. May also play a role in transmembrane water transport, possibly by indirect means.; . TISSUE SPECIFICITY: Detected in erythrocytes (at protein level). Erythrocytes. {ECO:0000269|PubMed:23219802}.; unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;hypothalamus;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;bone marrow;breast;uterus;prostate;lung;endometrium;bone;liver;spleen;kidney;brain;bladder; prefrontal cortex;skeletal muscle; 0.05429 0.28117 0.553050905 81.54635527 7952.53509 19.25836 SLC14A2 8.427413552635e-14 0.228290999951653 0.771709000048263 solute carrier family 14 member 2 FUNCTION: Specialized low-affinity vasopressin-regulated urea transporter. Mediates rapid transepithelial urea transport across the inner medullary collecting duct and plays a major role in the urinary concentrating mechanism. {ECO:0000269|PubMed:11502588, ECO:0000269|PubMed:8647271}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in the inner medulla of the kidney. {ECO:0000269|PubMed:11502588, ECO:0000269|PubMed:8647271}.; blood;bone marrow; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14178 0.17911 0.279193852 70.77730597 6537.42463 17.02493 SLC14A2-AS1 . . . SLC14A2 antisense RNA 1 . . . . . . . . . . . SLC15A1 8.68961113389547e-08 0.995339698098284 0.00466021500560461 solute carrier family 15 member 1 FUNCTION: Proton-coupled intake of oligopeptides of 2 to 4 amino acids with a preference for dipeptides. May constitute a major route for the absorption of protein digestion end-products.; . . . . 0.12558 0.19647 0.027580343 55.8091531 598.48788 4.95236 SLC15A2 1.50274634978985e-10 0.93756391763511 0.0624360822146152 solute carrier family 15 member 2 FUNCTION: Proton-coupled intake of oligopeptides of 2 to 4 amino acids with a preference for dipeptides.; . . unclassifiable (Anatomical System);cartilage;colon;skeletal muscle;retina;breast;prostate;lung;frontal lobe;placenta;thyroid;iris;germinal center;kidney;brain;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.61335 0.17076 -0.176292081 40.56381222 6543.27894 17.03613 SLC15A3 3.65752302506969e-07 0.345391759434986 0.654607874812711 solute carrier family 15 member 3 FUNCTION: Proton oligopeptide cotransporter. Transports free histidine and certain di- and tripeptides (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;choroid;skin;retina;uterus;endometrium;bone;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;blood;lung;placenta;visual apparatus;liver;alveolus;spleen;kidney;mammary gland;stomach;thymus; placenta;whole blood; 0.21552 0.09440 . . 320.79025 3.80487 SLC15A4 2.99438982124826e-09 0.161077533738566 0.838922463267044 solute carrier family 15 member 4 FUNCTION: Proton oligopeptide cotransporter. Transports free histidine and certain di- and tripeptides. {ECO:0000269|PubMed:16289537}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Moderately expressed in kidney, liver, and heart. Weakly expressed in colon and brain. Expressed in low levels throughout the gastrointestinal tract and in Caco-2 cells. Expressed in retinal fragment epithelium (RPE) and neural retina. Expressed in small intestine, stomach, duodenum, jejunum, ileum and colon. {ECO:0000269|PubMed:11741232, ECO:0000269|PubMed:11741260, ECO:0000269|PubMed:16289537}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;testis;ciliary ganglion;atrioventricular node;whole blood;skeletal muscle; 0.05944 0.09407 . . 571.06689 4.84805 SLC15A5 . . . solute carrier family 15 member 5 FUNCTION: Proton oligopeptide cotransporter. {ECO:0000305}.; . . . . . . 2.506301709 98.65534324 632.29128 5.06636 SLC16A1 0.826067878054453 0.173769399752594 0.000162722192953287 solute carrier family 16 member 1 FUNCTION: Proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate. Depending on the tissue and on cicumstances, mediates the import or export of lactic acid and ketone bodies. Required for normal nutrient assimilation, increase of white adipose tissue and body weight gain when on a high-fat diet. Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate, small molecules that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis. {ECO:0000269|PubMed:17701893}.; DISEASE: Familial hyperinsulinemic hypoglycemia 7 (HHF7) [MIM:610021]: Dominantly inherited hypoglycemic disorder characterized by inappropriate insulin secretion during anaerobic exercise or on pyruvate load. {ECO:0000269|PubMed:17701893}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Monocarboxylate transporter 1 deficiency (MCT1D) [MIM:616095]: A metabolic disorder characterized by recurrent ketoacidosis, a pathologic state due to ketone formation exceeding ketone utilization. The clinical consequences of ketoacidosis are vomiting, osmotic diuresis, dehydration, and Kussmaul breathing. The condition may progress to decreased consciousness and, ultimately, death. {ECO:0000269|PubMed:25390740}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in heart and in blood lymphocytes and monocytes (at protein level). Widely expressed. {ECO:0000269|PubMed:15505343}.; . . 0.25769 0.18612 -0.071520315 48.34866714 25.55771 0.83286 SLC16A1-AS1 . . . SLC16A1 antisense RNA 1 . . . . . . . . . . . SLC16A1P1 . . . SLC16A1 pseudogene 1 . . . . . . . . . . . SLC16A2 0.934351642887307 0.0653409285805438 0.000307428532149583 solute carrier family 16 member 2 FUNCTION: Very active and specific thyroid hormone transporter. Stimulates cellular uptake of thyroxine (T4), triiodothyronine (T3), reverse triiodothyronine (rT3) and diidothyronine. Does not transport Leu, Phe, Trp or Tyr. {ECO:0000269|PubMed:23550058}.; . TISSUE SPECIFICITY: Highly expressed in liver and heart. {ECO:0000269|PubMed:7981683}.; choroid;skin;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;bile duct;breast;pancreas;lung;placenta;liver;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;liver;caudate nucleus;cerebellum; 0.15324 0.21470 0.104848986 61.49445624 60.21127 1.57626 SLC16A3 0.325132712059301 0.658912766879805 0.0159545210608934 solute carrier family 16 member 3 FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle.; . . 0.21382 0.10972 -0.641086234 16.6784619 162.94808 2.78614 SLC16A4 0.00583523308352845 0.972009285779187 0.0221554811372844 solute carrier family 16 member 4 FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity). {ECO:0000250}.; . . . . 0.08213 0.08913 0.463046108 78.58575136 307.45955 3.73189 SLC16A5 3.7061944576566e-05 0.600002126869151 0.399960811186273 solute carrier family 16 member 5 FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in kidney.; medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;larynx;thyroid;bone;testis;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;urinary;lens;pancreas;lung;nasopharynx;placenta;macula lutea;head and neck;cervix;stomach; superior cervical ganglion; 0.10626 . -0.242430445 36.22906346 83.06733 1.93685 SLC16A6 0.205129420734742 0.785281181472474 0.00958939779278384 solute carrier family 16 member 6 FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;choroid;fovea centralis;lens;skeletal muscle;skin;retina;uterus;optic nerve;cerebral cortex;macula lutea;alveolus;testis; testis - interstitial;trigeminal ganglion;skeletal muscle; 0.25165 0.11592 -0.067881249 48.69072895 1571.51714 7.33817 SLC16A6P1 . . . SLC16A6 pseudogene 1 . . . . . . . . . . . SLC16A7 0.00178576628878128 0.898158635141963 0.100055598569256 solute carrier family 16 member 7 FUNCTION: Proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate. Functions as high-affinity pyruvate transporter. {ECO:0000269|PubMed:9786900}.; . TISSUE SPECIFICITY: Detected in heart and in blood lymphocytes and monocytes (at protein level). High expression in testis, moderate to low in spleen, heart, kidney, pancreas, skeletal muscle, brain and Leukocyte. Restricted expression in normal tissues, but widely expressed in cancer cells. {ECO:0000269|PubMed:15505343}.; unclassifiable (Anatomical System);kidney;bladder;skeletal muscle; superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06765 0.15427 0.374860183 75.43052607 113.58515 2.32064 SLC16A8 0.11016481897003 0.777058944461404 0.112776236568566 solute carrier family 16 member 8 FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Retinal pigment epithelium.; unclassifiable (Anatomical System);prostate;optic nerve;lung;macula lutea;testis;fovea centralis;choroid;lens;retina; . 0.19193 0.09932 . . 2277.92838 8.82915 SLC16A9 0.642448764557902 0.356209910123674 0.00134132531842374 solute carrier family 16 member 9 FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates (By similarity). {ECO:0000250}.; . . . . 0.18628 0.11986 0.485092724 79.37603208 325.9075 3.83806 SLC16A10 0.0676070063771054 0.91840788200296 0.0139851116199349 solute carrier family 16 member 10 FUNCTION: Sodium-independent transporter that mediates the update of aromatic acid. Can function as a net efflux pathway for aromatic amino acids in the basosolateral epithelial cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:11827462}.; . TISSUE SPECIFICITY: Strongly expressed in kidney and skeletal muscle and at lower level in placenta and heart. {ECO:0000269|PubMed:11827462}.; . . 0.08076 0.10491 -0.049474214 50.01179523 216.00513 3.17412 SLC16A11 0.0459183066040548 0.853365724970319 0.100715968425626 solute carrier family 16 member 11 FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates (By similarity). Probably involved in hepatic lipid metabolism: overexpression results in an increase of triacylglycerol(TAG) levels, small increases in intracellular diacylglycerols and decreases in lysophosphatidylcholine, cholesterol ester and sphingomyelin lipids. {ECO:0000250, ECO:0000269|PubMed:24390345}.; . TISSUE SPECIFICITY: Expressed in liver, salivary gland and thyroid. {ECO:0000269|PubMed:24390345}.; unclassifiable (Anatomical System);lung;ovary;placenta;parathyroid;blood;kidney;mammary gland;skin;bone marrow; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.13533 0.10169 . . 2830.11881 10.03747 SLC16A12 0.00201890642213391 0.911110983726613 0.0868701098512531 solute carrier family 16 member 12 FUNCTION: Proton-linked monocarboxylate transporter that mediates creatine transport across the plasma membrane. {ECO:0000269|PubMed:23578822}.; . TISSUE SPECIFICITY: Most highly expressed in kidney, followed by retina, lung, heart and testis. Very weakly expressed in brain and liver. Also detected in lens. {ECO:0000269|PubMed:18304496, ECO:0000269|PubMed:23578822}.; myocardium;meninges;pia mater;heart;endometrium;islets of Langerhans;dura mater;kidney;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.27233 0.12141 -0.137658575 43.57159707 178.14264 2.90153 SLC16A12-AS1 . . . SLC16A12 antisense RNA 1 . . . . . . . . . . . SLC16A13 7.50511260026083e-07 0.284063611077694 0.715935638411046 solute carrier family 16 member 13 FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates (By similarity). {ECO:0000250}.; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:24390345}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);breast;larynx;head and neck;bone marrow; . 0.03001 0.10700 -0.091746757 46.91554612 93.28666 2.07858 SLC16A14 0.215983363626467 0.775382472979605 0.0086341633939279 solute carrier family 16 member 14 FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;cartilage;colon;parathyroid;choroid;skeletal muscle;breast;pancreas;prostate;lung;frontal lobe;placenta;testis;brain; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12329 0.10389 -0.490397599 22.50530786 65.9738 1.67277 SLC16A14P1 . . . solute carrier family 16 member 14 pseudogene 1 . . . . . . . . . . . SLC17A1 2.59261497697838e-10 0.142663466415807 0.857336533324932 solute carrier family 17 member 1 FUNCTION: Important for the resorption of phosphate by the kidney. May be involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane.; . TISSUE SPECIFICITY: Expressed in kidney cortex, liver and brain but not in other tissues.; liver;spleen;kidney;skeletal muscle; dorsal root ganglion;superior cervical ganglion;kidney;atrioventricular node;trigeminal ganglion; 0.05381 0.13679 0.240763792 69.36777542 371.93508 4.06982 SLC17A2 0.00466985446742192 0.988892709808855 0.00643743572372291 solute carrier family 17 member 2 FUNCTION: May be involved in actively transporting phosphate into cells via Na(+) cotransport. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the small intestine, kidney, spleen and testis. Not detected in fetal brain, bone marrow, and mammary gland. {ECO:0000269|PubMed:9149941}.; unclassifiable (Anatomical System);liver;spleen;gall bladder; superior cervical ganglion;fetal liver;medulla oblongata;liver;globus pallidus;atrioventricular node;trigeminal ganglion; 0.11920 0.10391 0.218717575 68.27081859 73.55201 1.79289 SLC17A3 9.88205561287661e-14 0.0200604295635143 0.979939570436387 solute carrier family 17 member 3 FUNCTION: Isoform 2: voltage-driven, multispecific, organic anion transporter able to transport para-aminohippurate (PAH), estrone sulfate, estradiol-17-beta-glucuronide, bumetanide, and ochratoxin A. Isoform 2 functions as urate efflux transporter on the apical side of renal proximal tubule and is likely to act as an exit path for organic anionic drugs as well as urate in vivo. May be involved in actively transporting phosphate into cells via Na(+) cotransport.; . TISSUE SPECIFICITY: Expressed in the liver and kidney. It is detected in proximal tubules in renal cortex as well as some tubules and glomeruli, with highest expression at the apical side of proximal tubules (at protein level). {ECO:0000269|PubMed:20810651, ECO:0000269|PubMed:9149941}.; liver;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.08842 0.09453 0.110306132 62.00165133 1349.6941 6.89916 SLC17A4 6.33422534991957e-06 0.890457543115949 0.109536122658701 solute carrier family 17 member 4 FUNCTION: Acts as a membrane potential-dependent organic anion transporter, the transport requires a low concentration of chloride ions. May be involved in urate extrusion from the intestinal duct. May recognize hydrophilic anionic drugs such as aspirin, salicylate, and ibuprofen as substrates. Able to actively transport inorganic phosphate into cells via Na(+) cotransport (in vitro). {ECO:0000269|PubMed:22460716}.; . TISSUE SPECIFICITY: Abundantly expressed in pancreas, liver, colon and small intestine, less in kidney. Not detected in the adrenal glands, brain, placenta, heart, testis, skeletal muscle, and lungs. {ECO:0000269|PubMed:10319585, ECO:0000269|PubMed:22460716}.; . . 0.12975 0.13542 7.61E-05 53.98089172 1372.74734 6.94947 SLC17A5 0.0221961749395672 0.974529484014269 0.00327434104616425 solute carrier family 17 member 5 FUNCTION: Transports glucuronic acid and free sialic acid out of the lysosome after it is cleaved from sialoglycoconjugates undergoing degradation, this is required for normal CNS myelination. Mediates aspartate and glutamate membrane potential- dependent uptake into synaptic vesicles and synaptic-like microvesicles. Also functions as an electrogenic 2NO(3)(-)/H(+) cotransporter in the plasma membrane of salivary gland acinar cells, mediating the physiological nitrate efflux, 25% of the circulating nitrate ions is typically removed and secreted in saliva. {ECO:0000269|PubMed:10581036, ECO:0000269|PubMed:11751519, ECO:0000269|PubMed:15510212, ECO:0000269|PubMed:21781115, ECO:0000269|PubMed:22778404}.; DISEASE: Infantile sialic acid storage disorder (ISSD) [MIM:269920]: Severe form of sialic acid storage disease. Affected newborns exhibit visceromegaly, coarse features and failure to thrive immediately after birth. These patients have a shortened life span, usually less than 2 years. {ECO:0000269|PubMed:10581036, ECO:0000269|PubMed:10947946}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in fetal lung and small intestine, and at lower level in fetal skin and muscle. In the adult, detected in placenta, kidney and pancreas. Abundant in the endothelial cells of tumors from ovary, colon, breast and lung, but is not detected in endothelial cells from the corresponding normal tissues. {ECO:0000269|PubMed:10581036, ECO:0000269|PubMed:11751519}.; unclassifiable (Anatomical System);cartilage;colon;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.18702 0.25647 0.064394823 58.84642604 5503.64627 15.29397 SLC17A6 0.857098873242776 0.142881739966244 1.93867909798753e-05 solute carrier family 17 member 6 FUNCTION: Mediates the uptake of glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. May also mediate the transport of inorganic phosphate. {ECO:0000269|PubMed:10820226, ECO:0000269|PubMed:11698620}.; . TISSUE SPECIFICITY: Predominantly expressed in adult brain. Expressed in amygdala, caudate nucleus, cerebral cortex, frontal lobe, hippocampus, medulla, occipital lobe, putamen, spinal cord, substantia nigra, subthalamic nucleus, temporal lobe and thalamus. {ECO:0000269|PubMed:10820226}.; amygdala;optic nerve;ovary;islets of Langerhans;placenta;macula lutea;fovea centralis;choroid;lens;brain;retina; amygdala;dorsal root ganglion;subthalamic nucleus;thalamus;hypothalamus;temporal lobe;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle; 0.23519 0.28595 -0.224023033 37.4321774 107.35697 2.24887 SLC17A7 0.995932824968909 0.00406685105605974 3.23975031375754e-07 solute carrier family 17 member 7 FUNCTION: Mediates the uptake of glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. May also mediate the transport of inorganic phosphate. {ECO:0000269|PubMed:10820226}.; . TISSUE SPECIFICITY: Expressed in several regions of the brain including amygdala, cerebellum, cerebral cortex, hippocampus, frontal lobe, medulla, occipital lobe, putamen and temporal lobe. {ECO:0000269|PubMed:10820226}.; unclassifiable (Anatomical System);amygdala;ovary;cartilage;pineal body;substantia nigra;fovea centralis;choroid;skeletal muscle;skin;retina;optic nerve;whole body;lung;frontal lobe;bone;macula lutea;visual apparatus;hippocampus;testis;pineal gland;brain;cerebellum; amygdala;whole brain;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;temporal lobe;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.22686 0.24974 -0.314027422 31.9297004 69.95921 1.73523 SLC17A8 0.0449262500512103 0.953944327057746 0.0011294228910439 solute carrier family 17 member 8 FUNCTION: Mediates the uptake of glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. May also mediate the transport of inorganic phosphate. {ECO:0000269|PubMed:12151341}.; . TISSUE SPECIFICITY: Expressed in amygdala, cerebellum, hippocampus, medulla, spinal cord and thalamus. {ECO:0000269|PubMed:12151341}.; uterus;heart;skin; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.18714 0.14199 -0.955204708 9.170794999 82.58268 1.92958 SLC17A9 5.26686938450496e-08 0.395935867910527 0.604064079420779 solute carrier family 17 member 9 FUNCTION: Involved in vesicular storage and exocytosis of ATP. May accumulate ATP and other nucleotides in secretory vesicles such as adrenal chromaffin granules and synaptic vesicles. {ECO:0000269|PubMed:18375752}.; . TISSUE SPECIFICITY: Predominantly expressed in adrenal gland, brain and thyroid. {ECO:0000269|PubMed:18375752}.; . . 0.18047 0.10897 0.378498378 75.58386412 657.21963 5.13898 SLC18A1 1.8888318573672e-14 0.00760279399266627 0.992397206007315 solute carrier family 18 member A1 FUNCTION: Involved in the transport of biogenic monoamines, such as serotonin, from the cytoplasm into the secretory vesicles of neuroendocrine and endocrine cells. {ECO:0000269|PubMed:16326835}.; . . unclassifiable (Anatomical System);placenta;sympathetic chain;brain; superior cervical ganglion;globus pallidus;atrioventricular node; 0.09099 0.20510 1.026965723 91.08870017 912.89498 5.87431 SLC18A2 0.971755218810696 0.0282432389578341 1.54223147013241e-06 solute carrier family 18 member A2 FUNCTION: Involved in the ATP-dependent vesicular transport of biogenic amine neurotransmitters. Pumps cytosolic monoamines including dopamine, norepinephrine, serotonin, and histamine into synaptic vesicles. Requisite for vesicular amine storage prior to secretion via exocytosis.; . . ovary;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;aorta; uterus;superior cervical ganglion;skeletal muscle; 0.35817 0.21418 -0.714505427 14.4019816 38.56305 1.14365 SLC18A3 0.161377081657339 0.774049500593826 0.0645734177488353 solute carrier family 18 member A3 FUNCTION: Involved in acetylcholine transport into synaptic vesicles. {ECO:0000269|PubMed:8071310}.; . TISSUE SPECIFICITY: Peripheral and central cholinergic nervous systems. {ECO:0000269|PubMed:8071310}.; . . 0.21320 . -0.754958418 13.57631517 64.43617 1.64609 SLC18B1 3.94675803740147e-10 0.17949868533531 0.820501314270015 solute carrier family 18 member B1 . . . . . 0.13733 . -0.110153916 45.48832272 589.95485 4.92467 SLC19A1 0.0123881003346845 0.952273227180062 0.0353386724852532 solute carrier family 19 member 1 FUNCTION: Transporter for the intake of folate. Uptake of folate in human placental choriocarcinoma cells occurs by a novel mechanism called potocytosis which functionally couples three components, namely the folate receptor, the folate transporter, and a V-type H(+)-pump.; . TISSUE SPECIFICITY: Placenta, liver, and to a much smaller extent, in lung.; ovary;adrenal medulla;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;lens;lung;placenta;macula lutea;visual apparatus;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;spinal cord;liver;globus pallidus;testis;atrioventricular node;trigeminal ganglion; 0.07490 . -0.286522835 33.47487615 1149.843 6.46099 SLC19A2 0.00428587935441669 0.962060976156379 0.0336531444892038 solute carrier family 19 member 2 FUNCTION: High-affinity transporter for the intake of thiamine.; . TISSUE SPECIFICITY: Ubiquitous; most abundant in skeletal and cardiac muscle. Medium expression in placenta, heart, liver and kidney, low in lung.; ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;testis;amniotic fluid;brain;artery;unclassifiable (Anatomical System);heart;tongue;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;head and neck;kidney;stomach;aorta; placenta;adrenal cortex;skeletal muscle; 0.28165 0.15912 -0.26993514 34.59542345 175.54032 2.88209 SLC19A3 0.00163108657525026 0.887637138073567 0.110731775351182 solute carrier family 19 member 3 FUNCTION: Mediates high affinity thiamine uptake, propably via a proton anti-port mechanism. Has no folate transport activity. {ECO:0000269|PubMed:11731220}.; . TISSUE SPECIFICITY: Widely expressed but most abundant in placenta, kidney and liver. {ECO:0000269|PubMed:11136550, ECO:0000269|PubMed:15871139}.; unclassifiable (Anatomical System);sympathetic chain;colon;skeletal muscle;skin;breast;lung;nasopharynx;placenta;liver;testis;spleen;kidney;brain;stomach;cerebellum; superior cervical ganglion;placenta;globus pallidus;atrioventricular node;trigeminal ganglion; 0.09736 0.14341 -0.244249595 36.17008728 282.7385 3.59968 SLC20A1 0.725656582615843 0.274319015297049 2.44020871080182e-05 solute carrier family 20 member 1 FUNCTION: Sodium-phosphate symporter which plays a fundamental housekeeping role in phosphate transport, such as absorbing phosphate from interstitial fluid for normal cellular functions such as cellular metabolism, signal transduction, and nucleic acid and lipid synthesis. May play a role in extracellular matrix and cartilage calcification as well as in vascular calcification. May function as a retroviral receptor as it confers human cells susceptibility to infection to Gibbon Ape Leukemia Virus (GaLV), Simian sarcoma-associated virus (SSAV) and Feline leukemia virus subgroup B (FeLV-B) as well as 10A1 murine leukemia virus (10A1 MLV). {ECO:0000269|PubMed:11009570, ECO:0000269|PubMed:12097582, ECO:0000269|PubMed:1309898, ECO:0000269|PubMed:1531369, ECO:0000269|PubMed:2078500, ECO:0000269|PubMed:7929240, ECO:0000269|PubMed:7966619, ECO:0000269|PubMed:8041748}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:2078500}.; lymphoreticular;smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;synovium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;hypothalamus;blood;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; placenta;tumor;white blood cells;cerebellum; 0.81305 0.17045 -0.492218069 22.35786742 84.26474 1.95493 SLC20A1P1 . . . solute carrier family 20 member 1 pseudogene 1 . . . . . . . . . . . SLC20A1P2 . . . solute carrier family 20 member 1 pseudogene 2 . . . . . . . . . . . SLC20A1P3 . . . solute carrier family 20 member 1 pseudogene 3 . . . . . . . . . . . SLC20A2 0.864429580346683 0.135553573600494 1.68460528231753e-05 solute carrier family 20 member 2 FUNCTION: Sodium-phosphate symporter which seems to play a fundamental housekeeping role in phosphate transport by absorbing phosphate from interstitial fluid for normal cellular functions such as cellular metabolism, signal transduction, and nucleic acid and lipid synthesis. In vitro, sodium-dependent phosphate uptake is not siginificantly affected by acidic and alkaline conditions, however sodium-independent phosphate uptake occurs at acidic conditions. May play a role in extracellular matrix, cartilage and vascular calcification. Functions as a retroviral receptor and confers human cells susceptibility to infection to amphotropic murine leukemia virus (A-MuLV), 10A1 murine leukemia virus (10A1 MLV) and some feline leukemia virus subgroup B (FeLV-B) variants. {ECO:0000269|PubMed:11435563, ECO:0000269|PubMed:12205090, ECO:0000269|PubMed:15955065, ECO:0000269|PubMed:16790504, ECO:0000269|PubMed:8302848}.; DISEASE: Basal ganglia calcification, idiopathic, 1 (IBGC1) [MIM:213600]: A form of basal ganglia calcification, an autosomal dominant condition characterized by symmetric calcification in the basal ganglia and other brain regions. Affected individuals can either be asymptomatic or show a wide spectrum of neuropsychiatric symptoms, including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis, seizures, and chronic headache. Serum levels of calcium, phosphate, alkaline phosphatase and parathyroid hormone are normal. The neuropathological hallmark of the disease is vascular and pericapillary calcification, mainly of calcium phosphate, in the affected brain areas. {ECO:0000269|PubMed:22327515, ECO:0000269|PubMed:23334463, ECO:0000269|PubMed:23406454, ECO:0000269|PubMed:23939468, ECO:0000269|PubMed:24463626, ECO:0000269|PubMed:25284758}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;brain;heart;cartilage;tongue;nervous;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;hypothalamus;pancreas;lung;cornea;placenta;hippocampus;duodenum;head and neck;kidney;stomach; superior cervical ganglion;thalamus;thyroid; 0.58781 0.17587 -0.753139731 13.67067705 280.06199 3.58597 SLC22A1 1.23977716739769e-13 0.0119397632621416 0.988060236737734 solute carrier family 22 member 1 FUNCTION: Translocates a broad array of organic cations with various structures and molecular weights including the model compounds 1-methyl-4-phenylpyridinium (MPP), tetraethylammonium (TEA), N-1-methylnicotinamide (NMN), 4-(4-(dimethylamino)styryl)- N-methylpyridinium (ASP), the endogenous compounds choline, guanidine, histamine, epinephrine, adrenaline, noradrenaline and dopamine, and the drugs quinine, and metformin. The transport of organic cations is inhibited by a broad array of compounds like tetramethylammonium (TMA), cocaine, lidocaine, NMDA receptor antagonists, atropine, prazosin, cimetidine, TEA and NMN, guanidine, cimetidine, choline, procainamide, quinine, tetrabutylammonium, and tetrapentylammonium. Translocates organic cations in an electrogenic and pH-independent manner. Translocates organic cations across the plasma membrane in both directions. Transports the polyamines spermine and spermidine. Transports pramipexole across the basolateral membrane of the proximal tubular epithelial cells. The choline transport is activated by MMTS. Regulated by various intracellular signaling pathways including inhibition by protein kinase A activation, and endogenously activation by the calmodulin complex, the calmodulin- dependent kinase II and LCK tyrosine kinase. {ECO:0000269|PubMed:11388889, ECO:0000269|PubMed:11408531, ECO:0000269|PubMed:15389554, ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:9187257, ECO:0000269|PubMed:9260930, ECO:0000269|PubMed:9655880}.; . TISSUE SPECIFICITY: Widely expressed with high level in liver. Isoform 1 and isoform 2 are expressed in liver. Isoform 1, isoform 2, isoform 3 and isoform 4 are expressed in glial cell lines. {ECO:0000269|PubMed:11388889, ECO:0000269|PubMed:9187257, ECO:0000269|PubMed:9260930}.; unclassifiable (Anatomical System);uterus;lung;heart;liver;testis;spleen;skin; superior cervical ganglion;uterus corpus;liver;globus pallidus;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.06413 0.20476 1.782126607 96.85067233 2438.27558 9.17861 SLC22A2 1.4191712191388e-09 0.196380554481666 0.803619444099162 solute carrier family 22 member 2 FUNCTION: Mediates tubular uptake of organic compounds from circulation. Mediates the influx of agmatine, dopamine, noradrenaline (norepinephrine), serotonin, choline, famotidine, ranitidine, histamin, creatinine, amantadine, memantine, acriflavine, 4-[4-(dimethylamino)-styryl]-N-methylpyridinium ASP, amiloride, metformin, N-1-methylnicotinamide (NMN), tetraethylammonium (TEA), 1-methyl-4-phenylpyridinium (MPP), cimetidine, cisplatin and oxaliplatin. Cisplatin may develop a nephrotoxic action. Transport of creatinine is inhibited by fluoroquinolones such as DX-619 and LVFX. This transporter is a major determinant of the anticancer activity of oxaliplatin and may contribute to antitumor specificity. {ECO:0000269|PubMed:12089365, ECO:0000269|PubMed:12538837, ECO:0000269|PubMed:15496291, ECO:0000269|PubMed:15783073, ECO:0000269|PubMed:16006492, ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16314463, ECO:0000269|PubMed:16394027, ECO:0000269|PubMed:16914559, ECO:0000269|PubMed:16951202, ECO:0000269|PubMed:17072098, ECO:0000269|PubMed:17582384, ECO:0000269|PubMed:9260930, ECO:0000269|PubMed:9687576}.; . TISSUE SPECIFICITY: Mainly expressed in kidney. Localized at the luminal membrane and basolateral membrane of kidney distal tubule and proximal tubules. To a lower extent, expressed in neurons of the cerebral cortex and in various subcortical nuclei (at protein levels). Also detected in secretory phase endometrium; in scattered cells in the stroma. {ECO:0000269|PubMed:11912245, ECO:0000269|PubMed:17393420, ECO:0000269|PubMed:9260930, ECO:0000269|PubMed:9687576}.; . . 0.09887 . -0.506987379 21.76810569 143.26794 2.61008 SLC22A3 3.31638540911901e-05 0.942290434336013 0.0576764018098962 solute carrier family 22 member 3 FUNCTION: Mediates potential-dependent transport of a variety of organic cations. May play a significant role in the disposition of cationic neurotoxins and neurotransmitters in the brain. {ECO:0000269|PubMed:10196521, ECO:0000269|PubMed:10966924}.; . TISSUE SPECIFICITY: Expressed in placenta, skeletal muscle, prostate, aorta, liver, fetal lung, salivary gland, adrenal gland, kidney and brain cortex. No expression detected in spleen. {ECO:0000269|PubMed:10196521, ECO:0000269|PubMed:10966924, ECO:0000269|PubMed:9933568}.; unclassifiable (Anatomical System);ovary;heart;colon;parathyroid;skeletal muscle;uterus;prostate;pancreas;whole body;lung;frontal lobe;cochlea;cerebral cortex;thyroid;placenta;liver;testis;spleen;kidney;brain;artery;aorta;stomach; uterus;prostate;uterus corpus;fetal liver;trachea;adrenal gland;placenta;ciliary ganglion;atrioventricular node;skeletal muscle; 0.11090 0.17295 -0.448125345 24.19202642 54.97507 1.48560 SLC22A4 4.64079476855844e-06 0.847993350607615 0.152002008597617 solute carrier family 22 member 4 FUNCTION: Sodium-ion dependent, low affinity carnitine transporter. Probably transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Relative uptake activity ratio of carnitine to TEA is 1.78. A key substrate of this transporter seems to be ergothioneine (ET). {ECO:0000269|PubMed:10215651, ECO:0000269|PubMed:15795384}.; DISEASE: Rheumatoid arthritis (RA) [MIM:180300]: An inflammatory disease with autoimmune features and a complex genetic component. It primarily affects the joints and is characterized by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures. {ECO:0000269|PubMed:14608356}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Highly expressed in whole blood, bone marrow, trachea and fetal liver. Weakly expressed in kidney, skeletal muscle, prostate, lung, pancreas, placenta, heart, uterus, spleen and spinal cord. Highly expressed in intestinal cell types affected by Crohn disease, including epithelial cells. Expressed in CD68 macrophage and CD43 T-cells but not in CD20 B-cells. Predominantly expressed in CD14 cells in peripheral blood mononuclear cells. {ECO:0000269|PubMed:14608356, ECO:0000269|PubMed:15107849, ECO:0000269|PubMed:9426230}.; unclassifiable (Anatomical System);ovary;colon;bone marrow;bile duct;pancreas;lung;placenta;liver;testis;spleen;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skeletal muscle; 0.07203 0.10175 -0.710864321 14.5730125 698.35345 5.26103 SLC22A5 4.90000271154311e-09 0.369125278718753 0.630874716381245 solute carrier family 22 member 5 FUNCTION: Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Also relative uptake activity ratio of carnitine to TEA is 11.3. {ECO:0000269|PubMed:10454528}.; . TISSUE SPECIFICITY: Strongly expressed in kidney, skeletal muscle, heart and placenta. Highly expressed in intestinal cell types affected by Crohn disease, including epithelial cells. Expressed in CD68 macrophage and CD43 T-cells but not in CD20 B-cells. {ECO:0000269|PubMed:10454528}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;parathyroid;fovea centralis;lens;skin;retina;uterus;pancreas;whole body;lung;endometrium;placenta;macula lutea;visual apparatus;hippocampus;liver;testis;kidney;brain;mammary gland;bladder;stomach; superior cervical ganglion;kidney;atrioventricular node;skeletal muscle; 0.17596 0.28558 0.801024817 87.65628686 511.75179 4.63180 SLC22A6 2.189266123066e-05 0.905063590851771 0.0949145164869983 solute carrier family 22 member 6 FUNCTION: Involved in the renal elimination of endogenous and exogenous organic anions. Functions as organic anion exchanger when the uptake of one molecule of organic anion is coupled with an efflux of one molecule of endogenous dicarboxylic acid (glutarate, ketoglutarate, etc). Mediates the sodium-independent uptake of 2,3-dimercapto-1-propanesulfonic acid (DMPS) (By similarity). Mediates the sodium-independent uptake of p- aminohippurate (PAH), ochratoxin (OTA), acyclovir (ACV), 3'-azido- 3-'deoxythymidine (AZT), cimetidine (CMD), 2,4-dichloro- phenoxyacetate (2,4-D), hippurate (HA), indoleacetate (IA), indoxyl sulfate (IS) and 3-carboxy-4-methyl-5-propyl-2- furanpropionate (CMPF), cidofovir, adefovir, 9-(2- phosphonylmethoxyethyl) guanine (PMEG), 9-(2- phosphonylmethoxyethyl) diaminopurine (PMEDAP) and edaravone sulfate. PAH uptake is inhibited by p- chloromercuribenzenesulphonate (PCMBS), diethyl pyrocarbonate (DEPC), sulindac, diclofenac, carprofen, glutarate and okadaic acid (By similarity). PAH uptake is inhibited by benzothiazolylcysteine (BTC), S-chlorotrifluoroethylcysteine (CTFC), cysteine S-conjugates S-dichlorovinylcysteine (DCVC), furosemide, steviol, phorbol 12-myristate 13-acetate (PMA), calcium ionophore A23187, benzylpenicillin, furosemide, indomethacin, bumetamide, losartan, probenecid, phenol red, urate, and alpha-ketoglutarate. {ECO:0000250, ECO:0000269|PubMed:12538807, ECO:0000269|PubMed:15644426, ECO:0000269|PubMed:17038320, ECO:0000269|PubMed:17502342, ECO:0000269|PubMed:9762842, ECO:0000269|PubMed:9887087}.; . TISSUE SPECIFICITY: Strongly expressed in kidney and to a lower extent in liver, skeletal muscle, brain and placenta. Found at the basolateral membrane of the proximal tubule. {ECO:0000269|PubMed:10049739, ECO:0000269|PubMed:10462545, ECO:0000269|PubMed:10964714, ECO:0000269|PubMed:9887087, ECO:0000269|PubMed:9950961}.; unclassifiable (Anatomical System);optic nerve;macula lutea;colon;fovea centralis;choroid;kidney;lens;brain;stomach;retina; superior cervical ganglion;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.36709 0.19019 -0.490397599 22.50530786 145.00298 2.62347 SLC22A7 3.71516467731254e-06 0.94489913318083 0.0550971516544929 solute carrier family 22 member 7 FUNCTION: Mediates sodium-independent multispecific organic anion transport. Transport of prostaglandin E2, prostaglandin F2, tetracycline, bumetanide, estrone sulfate, glutarate, dehydroepiandrosterone sulfate, allopurinol, 5-fluorouracil, paclitaxel, L-ascorbic acid, salicylate, ethotrexate, and alpha- ketoglutarate. {ECO:0000269|PubMed:11327718, ECO:0000269|PubMed:11855680, ECO:0000269|PubMed:11907186, ECO:0000269|PubMed:12023506, ECO:0000269|PubMed:15901346}.; . TISSUE SPECIFICITY: Expressed in liver and kidney. {ECO:0000269|PubMed:11327718, ECO:0000269|PubMed:11907186, ECO:0000269|PubMed:15901346}.; . . 0.10387 . -1.021348453 7.997169144 49.57694 1.37753 SLC22A8 1.50475715346013e-10 0.0558924427945178 0.944107557055006 solute carrier family 22 member 8 FUNCTION: Plays an important role in the excretion/detoxification of endogenous and exogenous organic anions, especially from the brain and kidney. Involved in the transport basolateral of steviol, fexofenadine. Transports benzylpenicillin (PCG), estrone- 3-sulfate (E1S), cimetidine (CMD), 2,4-dichloro-phenoxyacetate (2,4-D), p-amino-hippurate (PAH), acyclovir (ACV) and ochratoxin (OTA). {ECO:0000269|PubMed:14586168, ECO:0000269|PubMed:15644426, ECO:0000269|PubMed:15846473, ECO:0000269|PubMed:16455804}.; . TISSUE SPECIFICITY: Expressed in kidney. {ECO:0000269|PubMed:11912245}.; unclassifiable (Anatomical System);iris;colon;choroid;kidney;brain;stomach;retina; kidney;skeletal muscle; 0.27887 0.18663 -0.332434268 30.74427931 282.99018 3.60019 SLC22A9 3.61523813897635e-14 0.00578919320637198 0.994210806793592 solute carrier family 22 member 9 FUNCTION: Sodium-independent organic anion transporter which exhibits high specificity for sulfated conjugates of xenobiotics and steroid hormones. It is also specifically activated by 3 to 5 carbons-containing short-chain fatty acids/SCFAs, including propionate, butyrate and valerate. May operate the exchange of sulfated organic components against short-chain fatty acids/SCFAs at the sinusoidal membrane of hepatocytes. {ECO:0000269|PubMed:17393504}.; . TISSUE SPECIFICITY: Specifically expressed in liver by hepatocytes (at protein level). {ECO:0000269|PubMed:11327718, ECO:0000269|PubMed:17393504}.; liver;spleen; dorsal root ganglion;fetal liver;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.03443 . 0.180083178 66.16536919 139.80771 2.57860 SLC22A10 1.54344983139895e-14 0.00675195795855683 0.993248042041428 solute carrier family 22 member 10 . . TISSUE SPECIFICITY: Detected in fetal and adult liver, and in adult kidney. {ECO:0000269|PubMed:11327718, ECO:0000269|PubMed:12372408}.; liver;spleen; dorsal root ganglion;superior cervical ganglion;testis - interstitial;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.02591 . 1.84828222 97.12196273 11773.91304 23.46842 SLC22A11 5.80185239880571e-05 0.889105639392377 0.110836342083635 solute carrier family 22 member 11 FUNCTION: Mediates saturable uptake of estrone sulfate, dehydroepiandrosterone sulfate and related compounds. {ECO:0000269|PubMed:10660625, ECO:0000269|PubMed:15102942, ECO:0000269|PubMed:15291761}.; . TISSUE SPECIFICITY: Detected in placenta and kidney. {ECO:0000269|PubMed:10660625}.; unclassifiable (Anatomical System);lung;placenta;liver;testis;colon;spleen;kidney;stomach; superior cervical ganglion;placenta;ciliary ganglion;kidney;trigeminal ganglion;skeletal muscle; 0.16640 0.10113 0.023941474 55.75607455 84.2564 1.95458 SLC22A12 4.90101865688499e-06 0.856135783132933 0.14385931584841 solute carrier family 22 member 12 FUNCTION: Required for efficient urate re-absorption in the kidney. Regulates blood urate levels. Mediates saturable urate uptake by facilitating the exchange of urate against organic anions. {ECO:0000269|PubMed:12024214}.; . TISSUE SPECIFICITY: Detected in kidney (at protein level). Detected in fetal and adult kidney. Detected in epithelial cells of proximal tubules in renal cortex. {ECO:0000269|PubMed:12024214, ECO:0000269|PubMed:15304510}.; unclassifiable (Anatomical System);kidney; globus pallidus;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion; 0.12600 0.14076 -1.153638777 6.233781552 97.64363 2.13702 SLC22A13 2.16075768642524e-15 0.00212287793262885 0.997877122067369 solute carrier family 22 member 13 . . TISSUE SPECIFICITY: Ubiquitous, expressed at low levels. {ECO:0000269|PubMed:10072596}.; unclassifiable (Anatomical System);colon;kidney;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle;skin; 0.15074 0.10820 -0.262657925 34.93158764 137.58966 2.55295 SLC22A14 9.57031766361908e-09 0.29712600529256 0.702873985137122 solute carrier family 22 member 14 . . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10072596}.; lung;testis;brain;stomach; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.03068 0.06213 1.850110669 97.13375796 4182.05289 12.85286 SLC22A15 8.6598992720709e-06 0.92357682975248 0.0764145103482479 solute carrier family 22 member 15 FUNCTION: Probably transports organic cations (By similarity). Appears not to be the agmatine transporter. {ECO:0000250, ECO:0000269|PubMed:15028572}.; . TISSUE SPECIFICITY: Expressed at highest levels in kidney and brain. Expressed at high levels in skeletal muscle, heart, liver, placenta and white blood cells. Expressed at moderate levels in lung and spleen. Expressed at low levels in thymus, small intestine and colon. Expressed in several intestinal tumor cell lines. {ECO:0000269|PubMed:12372408, ECO:0000269|PubMed:15028572}.; . . 0.16269 0.11257 0.042348793 57.31304553 841.78369 5.68033 SLC22A16 2.08702152845569e-22 1.53570663867996e-05 0.999984642933613 solute carrier family 22 member 16 FUNCTION: High affinity carnitine transporter; the uptake is partially sodium-ion dependent. Thought to mediate the L-carnitine secretion mechanism from testis epididymal epithelium into the lumen which is involved in the maturation of spermatozoa. Also transports organic cations such as tetraethylammonium (TEA) and doxorubicin. The uptake of TEA is inhibited by various organic cations. The uptake of doxorubicin is sodium-independent. {ECO:0000269|PubMed:12089149, ECO:0000269|PubMed:15963465}.; . TISSUE SPECIFICITY: Widely expressed at low levels in adult tissues and fetal brain, lung, liver and kidney. Expressed in testis and epididymis (at protein level). Expressed at lower levels in bone marrow and fetal liver. Expressed in hematopoietic cells, including CD34(+) leukocytes and leukemia cells. Abundantly expressed in ovarian cancer clear-cell adenocarcinoma. Expressed in endometrium (at protein level); highly expressed during the normal secretory phase, but expression is significantly reduced in the proliferative phase. {ECO:0000269|PubMed:12089149, ECO:0000269|PubMed:12372408, ECO:0000269|PubMed:12384147, ECO:0000269|PubMed:15963465, ECO:0000269|PubMed:17197897, ECO:0000269|PubMed:17581421}.; unclassifiable (Anatomical System);lung;heart;lacrimal gland;liver;testis;spleen; . 0.12072 0.15205 0.470324112 78.82755367 918.87398 5.89239 SLC22A17 0.772286750668166 0.227643233673495 7.00156583388896e-05 solute carrier family 22 member 17 FUNCTION: Cell surface receptor for LCN2 (24p3) that plays a key role in iron homeostasis and transport. Able to bind iron-bound LCN2 (holo-24p3), followed by internalization of holo-24p3 and release of iron, thereby increasing intracellular iron concentration and leading to inhibition of apoptosis. Also binds iron-free LCN2 (apo-24p3), followed by internalization of apo-24p3 and its association with an intracellular siderophore, leading to iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration and resulting in apoptosis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain.; ovary;colon;parathyroid;skin;retina;bone marrow;optic nerve;frontal lobe;endometrium;bone;iris;pituitary gland;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;hypothalamus;cerebrum;lens;pancreas;lung;placenta;hippocampus;head and neck;kidney;mammary gland;stomach;cerebellum; whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;pituitary;parietal lobe;cingulate cortex;cerebellum; 0.38911 0.12779 -0.53631094 20.53550366 55.94393 1.50188 SLC22A18 0.00192306817866287 0.906153620302107 0.0919233115192298 solute carrier family 22 member 18 FUNCTION: May act as a transporter of organic cations based on a proton efflux antiport mechanism. May play a role in the transport of chloroquine and quinidine-related compounds in kidney. {ECO:0000269|PubMed:9744804}.; DISEASE: Rhabdomyosarcoma, embryonal, 1 (RMSE1) [MIM:268210]: A form of rhabdomyosarcoma, a highly malignant tumor of striated muscle derived from primitive mesenchymal cells and exhibiting differentiation along rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most frequently occurring soft tissue sarcomas and the most common in children. It occurs in four forms: alveolar, pleomorphic, embryonal and botryoidal rhabdomyosarcomas. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at high levels in adult and fetal kidney and liver, and adult colon. Expressed in fetal renal proximal tubules (at protein level). Expressed at lower levels in heart, brain and lung. {ECO:0000269|PubMed:9499412, ECO:0000269|PubMed:9520460, ECO:0000269|PubMed:9570947, ECO:0000269|PubMed:9744804}.; unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;colon;parathyroid;skin;breast;pancreas;lung;thyroid;placenta;testis;cervix;kidney;brain;mammary gland;tonsil;stomach; liver;kidney;skeletal muscle; 0.11404 . 1.245625743 93.42415664 1793.90512 7.81719 SLC22A18AS . . . solute carrier family 22 member 18 antisense . . TISSUE SPECIFICITY: Most abundantly expressed in gastrointestinal tissues. Expressed at lower levels in kidney and placenta. Expressed in fetal brain, liver, placenta, kidney and lung. {ECO:0000269|PubMed:15175115, ECO:0000269|PubMed:9520460}.; . . . . 1.879670682 97.24581269 122.36499 2.40945 SLC22A20 . . . solute carrier family 22 member 20 FUNCTION: Organic anion transporter that mediates the uptake of estrone sulfate. Inhibited by probenecid, propionate, 2- methylbutyrate, 3-methylbutyrate, benzoate, heptanoate and 2- ethylhaxanoate. May act as an odorant transporter (By similarity). {ECO:0000250}.; . . . . . . . . . . SLC22A23 0.366550902975159 0.632950473909413 0.000498623115427995 solute carrier family 22 member 23 . . . . . 0.49745 0.11030 -0.865195027 10.79853739 46.94609 1.32450 SLC22A24 0.000186760846184136 0.277314635016096 0.72249860413772 solute carrier family 22 member 24 . . . . . 0.13860 . . . 3315.23833 11.00433 SLC22A25 4.63017324509406e-13 0.0134637653515039 0.986536234648033 solute carrier family 22 member 25 . . TISSUE SPECIFICITY: Expressed exclusively in liver in both embryo and adult. {ECO:0000269|PubMed:15054140}.; liver; ciliary ganglion; 0.06397 . 0.692611128 85.26185421 3665.45091 11.76380 SLC22A31 . . . solute carrier family 22 member 31 FUNCTION: Organic anion transporter that mediates the uptake of ions. {ECO:0000305}.; . . . . . . . . 4297.58624 13.03658 SLC23A1 0.0243223058859264 0.972818625964061 0.00285906815001231 solute carrier family 23 member 1 FUNCTION: Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate.; . TISSUE SPECIFICITY: Highly expressed in adult small intestine, kidney, thymus, ovary, colon, prostate and liver, and in fetal kidney, liver and thymus.; unclassifiable (Anatomical System);prostate;umbilical cord;endometrium;liver;colon;blood;kidney;germinal center;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15514 0.14852 0.266447942 70.5826846 399.62426 4.19635 SLC23A2 0.511221636863337 0.488745027434846 3.33357018175093e-05 solute carrier family 23 member 2 FUNCTION: Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;iris;pituitary gland;testis;germinal center;brain;artery;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pineal body;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;amygdala;superior cervical ganglion;thalamus;adrenal cortex;atrioventricular node;skeletal muscle;subthalamic nucleus;adrenal gland;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.50440 0.16306 -0.933156985 9.54824251 28.97342 0.92640 SLC23A3 0.00231261775618616 0.994068777796047 0.00361860444776646 solute carrier family 23 member 3 . . . unclassifiable (Anatomical System);cartilage;ovary;colon;parathyroid;skeletal muscle;skin;bone marrow;uterus;prostate;whole body;lung;frontal lobe;placenta;liver;testis;cervix;germinal center;kidney;brain;mammary gland;bladder; . 0.08223 0.11208 -0.624497208 17.16206653 230.52871 3.28056 SLC23A4P . . . solute carrier family 23 member 4, pseudogene . . . . . . . . . . . SLC24A1 0.000127201012282332 0.990422927532491 0.00944987145522726 solute carrier family 24 member 1 FUNCTION: Critical component of the visual transduction cascade, controlling the calcium concentration of outer segments during light and darkness. Light causes a rapid lowering of cytosolic free calcium in the outer segment of both retinal rod and cone photoreceptors and the light-induced lowering of calcium is caused by extrusion via this protein which plays a key role in the process of light adaptation. Transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+). {ECO:0000269|PubMed:10608890}.; DISEASE: Night blindness, congenital stationary, 1D (CSNB1D) [MIM:613830]: An autosomal recessive form of congenital stationary night blindness, a non-progressive retinal disorder characterized by impaired night vision. CSNB1D is characterized by a Riggs type of electroretinogram (proportionally reduced a- and b-waves). Patients have visual acuity within the normal range and no symptoms of myopia and/or nystagmus. {ECO:0000269|PubMed:20850105}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the retina, particularly in the inner segment, outer and inner nuclear layers, and ganglion cell layer. {ECO:0000269|PubMed:20850105}.; uterus;unclassifiable (Anatomical System);optic nerve;islets of Langerhans;macula lutea;fovea centralis;choroid;kidney;lens;skin;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;temporal lobe;globus pallidus;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.49323 0.09537 -0.569494998 19.04340646 1893.71303 8.00103 SLC24A2 0.0350598258476389 0.963288996335474 0.00165117781688672 solute carrier family 24 member 2 FUNCTION: Critical component of the visual transduction cascade, controlling the calcium concentration of outer segments during light and darkness. Light causes a rapid lowering of cytosolic free calcium in the outer segment of both retinal rod and cone photoreceptors and the light-induced lowering of calcium is caused by extrusion via this protein which plays a key role in the process of light adaptation. Transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+).; . . smooth muscle; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;cerebellum; 0.26475 0.11066 -0.50880549 21.72682236 141.71411 2.59795 SLC24A3 0.959518180659547 0.0404810555852444 7.63755208834896e-07 solute carrier family 24 member 3 FUNCTION: Transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+). {ECO:0000250}.; . TISSUE SPECIFICITY: Abundant in the brain. Expressed at low levels in the aorta, uterus and intestine.; unclassifiable (Anatomical System);heart;skin;skeletal muscle;retina;bone marrow;uterus;pancreas;prostate;optic nerve;lung;placenta;alveolus;hypopharynx;head and neck;kidney;brain; amygdala;uterus;whole brain;thalamus;superior cervical ganglion;fetal brain;cerebellum peduncles;hypothalamus;caudate nucleus;cingulate cortex;cerebellum; 0.19003 0.11730 1.13538281 92.30360934 4201.50362 12.89591 SLC24A4 3.16711232181816e-06 0.996765621111578 0.00323121177610061 solute carrier family 24 member 4 FUNCTION: Transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+). Controls the rapid response termination and proper regulation of adaptation in olfactory sensory neurons (OSNs) which subsequently influences how odor information is encoded and perceived. May play a role in calcium transport during amelogenesis (By similarity). {ECO:0000250|UniProtKB:Q8CGQ8}.; DISEASE: Amelogenesis imperfecta, hypomaturation type, 2A5 (AI2A5) [MIM:615887]: A defect of enamel formation. The disorder involves both primary and secondary dentitions. The teeth have a shiny agar jelly appearance and the enamel is softer than normal. Brown pigment is present in middle layers of enamel. {ECO:0000269|PubMed:23375655, ECO:0000269|PubMed:24621671}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed abundantly in all regions of the brain, aorta, lung and thymus. Expressed at lower levels in the stomach and intestine.; unclassifiable (Anatomical System);meninges;blood;fovea centralis;choroid;lens;skeletal muscle;skin;retina;optic nerve;pia mater;macula lutea;liver;spleen;dura mater;brain; superior cervical ganglion;kidney;trigeminal ganglion;skeletal muscle; 0.15504 0.14962 0.316000233 72.80018872 793.84443 5.55646 SLC24A5 3.20459293064119e-05 0.799382975187712 0.200584978882982 solute carrier family 24 member 5 FUNCTION: Cation exchanger involved in pigmentation, possibly by participating in ion transport in melanosomes. Predominant sodium- Calcium exchanger in melanocytes. Probably transports 1 Ca(2+) and 1 K(+) to the melanosome in exchange for 4 cytoplasmic Na(+). {ECO:0000269|PubMed:16357253, ECO:0000269|PubMed:18166528}.; DISEASE: Albinism, oculocutaneous, 6 (OCA6) [MIM:113750]: A disorder characterized by a reduction or complete loss of melanin in the skin, hair and eyes. Patients show reduced or lacking pigmentation often accompanied by eye symptoms such as photophobia, strabismus, moderate to severe visual impairment, and nystagmus. {ECO:0000269|PubMed:23364476}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;sympathetic chain;developmental;colon;parathyroid;skin;uterus;whole body;lung;frontal lobe;endometrium;placenta;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland;artery;aorta;stomach; . 0.16978 0.19373 -0.688817379 15.20405756 72.08687 1.76847 SLC25A1 0.633538572578213 0.365009124233388 0.00145230318839819 solute carrier family 25 member 1 FUNCTION: Involved in citrate-H(+)/malate exchange. Important for the bioenergetics of hepatic cells as it provides a carbon source for fatty acid and sterol biosyntheses, and NAD(+) for the glycolytic pathway.; DISEASE: Combined D-2- and L-2-hydroxyglutaric aciduria (D2L2AD) [MIM:615182]: An autosomal recessive neurometabolic disorder characterized by neonatal-onset encephalopathy with severe muscular weakness, intractable seizures, respiratory distress, and lack of psychomotor development resulting in early death. Brain imaging shows abnormalities including enlarged ventricles, delayed myelination, and germinal layer cysts. {ECO:0000269|PubMed:23561848}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; adipose tissue;liver; 0.38138 0.32148 -0.516085732 21.20193442 13.73448 0.49803 SLC25A1P1 . . . solute carrier family 25 member 1 pseudogene 1 . . . . . . . . . . . SLC25A1P2 . . . solute carrier family 25 member 1 pseudogene 2 . . . . . . . . . . . SLC25A1P3 . . . solute carrier family 25 member 1 pseudogene 3 . . . . . . . . . . . SLC25A1P4 . . . solute carrier family 25 member 1 pseudogene 4 . . . . . . . . . . . SLC25A1P5 . . . solute carrier family 25 member 1 pseudogene 5 . . . . . . . . . . . SLC25A2 0.0365973537230041 0.832185141968851 0.131217504308145 solute carrier family 25 member 2 FUNCTION: Ornithine transport across inner mitochondrial membrane, from the cytoplasm to the matrix.; . TISSUE SPECIFICITY: Expressed in liver, kidney, pancreas and cultured fibroblasts.; testis; dorsal root ganglion;testis - interstitial;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.10372 0.14606 0.881944684 89.02453409 1931.58222 8.08451 SLC25A3 0.0715576488202016 0.915646571939738 0.0127957792400608 solute carrier family 25 member 3 FUNCTION: Transport of phosphate groups from the cytosol to the mitochondrial matrix. Phosphate is cotransported with H(+). May play a role regulation of the mitochondrial permeability transition pore (mPTP).; DISEASE: Mitochondrial phosphate carrier deficiency (MPCD) [MIM:610773]: Fatal disorder of oxidative phosphorylation. Patients have lactic acidosis, hypertrophic cardiomyopathy and muscular hypotonia and die within the first year of life. {ECO:0000269|PubMed:17273968}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;pineal body;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;choroid;vein;uterus;oesophagus;cerebral cortex;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;amnion;kidney;stomach;aorta; whole brain;heart;adrenal gland;liver;kidney;skeletal muscle; 0.30153 0.22672 -0.626318434 17.03231894 20.64253 0.70171 SLC25A3P1 . . . solute carrier family 25 member 3 pseudogene 1 . . . . . . . . . . . SLC25A3P2 . . . solute carrier family 25 member 3 pseudogene 2 . . . . . . . . . . . SLC25A3P3 . . . solute carrier family 25 member 3 pseudogene 3 . . . . . . . . . . . SLC25A4 0.483364232516032 0.494464408349967 0.0221713591340004 solute carrier family 25 member 4 FUNCTION: Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane.; DISEASE: Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal dominant, 2 (PEOA2) [MIM:609283]: A disorder characterized by progressive weakness of ocular muscles and levator muscle of the upper eyelid. In a minority of cases, it is associated with skeletal myopathy, which predominantly involves axial or proximal muscles and which causes abnormal fatigability and even permanent muscle weakness. Ragged-red fibers and atrophy are found on muscle biopsy. A large proportion of chronic ophthalmoplegias are associated with other symptoms, leading to a multisystemic pattern of this disease. Additional symptoms are variable, and may include cataracts, hearing loss, sensory axonal neuropathy, ataxia, depression, hypogonadism, and parkinsonism. {ECO:0000269|PubMed:10926541, ECO:0000269|PubMed:11756613, ECO:0000269|PubMed:12112115, ECO:0000269|PubMed:15792871, ECO:0000269|PubMed:18575922}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mitochondrial DNA depletion syndrome 12, cardiomyopathic type (MTDPS12) [MIM:615418]: An autosomal recessive mitochondrial disorder characterized by childhood onset of slowly progressive hypertrophic cardiomyopathy and generalized skeletal myopathy resulting in exercise intolerance and, in some patients, muscle weakness and atrophy. Skeletal muscle biopsy shows ragged red fibers, mtDNA depletion, and accumulation of abnormal mitochondria. {ECO:0000269|PubMed:22187496}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; whole brain;tongue;cerebellum peduncles;globus pallidus;parietal lobe;skeletal muscle; 0.26589 0.41336 0.058937498 58.26256192 9.67226 0.35521 SLC25A5 0.857861936540947 0.139917320726889 0.00222074273216397 solute carrier family 25 member 5 FUNCTION: Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation. {ECO:0000269|PubMed:20797633}.; . . . . 0.33650 0.49922 -0.031067188 51.03798066 4.65192 0.16682 SLC25A5-AS1 . . . SLC25A5 antisense RNA 1 . . . . . . . . . . . SLC25A5P1 . . . solute carrier family 25 member 5 pseudogene 1 . . . . . . . . . . . SLC25A5P2 . . . solute carrier family 25 member 5 pseudogene 2 . . . . . . . . . . . SLC25A5P3 . . . solute carrier family 25 member 5 pseudogene 3 . . . . . . . . . . . SLC25A5P4 . . . solute carrier family 25 member 5 pseudogene 4 . . . . . . . . . . . SLC25A5P5 . . . solute carrier family 25 member 5 pseudogene 5 . . . . . . . . . . . SLC25A5P6 . . . solute carrier family 25 member 5 pseudogene 6 . . . . . . . . . . . SLC25A5P7 . . . solute carrier family 25 member 5 pseudogene 7 . . . . . . . . . . . SLC25A5P8 . . . solute carrier family 25 member 5 pseudogene 8 . . . . . . . . . . . SLC25A5P9 . . . solute carrier family 25 member 5 pseudogene 9 . . . . . . . . . . . SLC25A6 0.0669196984002589 0.871373453671712 0.0617068479280292 solute carrier family 25 member 6 FUNCTION: Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis. {ECO:0000269|PubMed:15033708}.; . . . . 0.48743 0.43956 -0.88906181 10.36801132 358.15116 4.01015 SLC25A6P1 . . . solute carrier family 25 member 6 pseudogene 1 . . . . . . . . . . . SLC25A6P2 . . . solute carrier family 25 member 6 pseudogene 2 . . . . . . . . . . . SLC25A6P3 . . . solute carrier family 25 member 6 pseudogene 3 . . . . . . . . . . . SLC25A6P4 . . . solute carrier family 25 member 6 pseudogene 4 . . . . . . . . . . . SLC25A6P5 . . . solute carrier family 25 member 6 pseudogene 5 . . . . . . . . . . . SLC25A6P6 . . . solute carrier family 25 member 6 pseudogene 6 . . . . . . . . . . . SLC25A10 0.00243936812560947 0.928274847606589 0.0692857842678011 solute carrier family 25 member 10 FUNCTION: Involved in translocation of malonate, malate and succinate in exchange for phosphate, sulfate, sulfite or thiosulfate across mitochondrial inner membrane.; . TISSUE SPECIFICITY: Present in high amounts in liver and kidney, and at lower levels in all the other tissues analyzed. {ECO:0000269|PubMed:10585886}.; lymphoreticular;myocardium;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;germinal center;brain;tonsil;heart;pineal body;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;oesophagus;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);trophoblast;lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;hypopharynx;duodenum;head and neck;kidney;stomach;thymus; superior cervical ganglion;heart;temporal lobe;liver;testis;kidney;pons;trigeminal ganglion;skeletal muscle; 0.18311 0.12721 -0.448125345 24.19202642 41.5856 1.21268 SLC25A11 0.666467126614711 0.332457288864113 0.00107558452117546 solute carrier family 25 member 11 FUNCTION: Catalyzes the transport of 2-oxoglutarate across the inner mitochondrial membrane in an electroneutral exchange for malate or other dicarboxylic acids, and plays an important role in several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism.; . . lymphoreticular;myocardium;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;pharynx;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; whole brain;superior cervical ganglion;heart;liver;prefrontal cortex;kidney;atrioventricular node;skeletal muscle;cerebellum; 0.26927 0.31802 -0.339715008 30.06605331 10.71775 0.38884 SLC25A12 0.887050481777341 0.112949092049374 4.26173284780992e-07 solute carrier family 25 member 12 FUNCTION: Catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane. May have a function in the urea cycle. {ECO:0000269|PubMed:11566871}.; . TISSUE SPECIFICITY: High levels in heart and skeletal muscle, low in brain and very low in kidney. {ECO:0000269|PubMed:10369257, ECO:0000269|PubMed:9722566}.; ovary;colon;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;atrium;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach;aorta;peripheral nerve;cerebellum; amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.32977 0.15427 -0.424258538 25.56027365 214.0543 3.15801 SLC25A13 1.9404630788689e-15 0.097873689691618 0.90212631030838 solute carrier family 25 member 13 FUNCTION: Catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane. May have a function in the urea cycle. {ECO:0000269|PubMed:11566871}.; DISEASE: Cholestasis, neonatal intrahepatic, caused by citrin deficiency (NICCD) [MIM:605814]: A form of citrullinemia type 2 with neonatal onset, characterized by suppression of the bile flow, hepatic fibrosis, low birth weight, growth retardation, hypoproteinemia, variable liver dysfunction. Neonatal intrahepatic cholestasis due to citrin deficiency is generally not severe and symptoms disappear by one year of age with an appropriate diet. Years or even decades later, however, some individuals develop the characteristic features of citrullinemia type 2 with neuropsychiatric symptoms. {ECO:0000269|PubMed:11793471}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: High levels in liver and low levels in kidney, pancreas, placenta, heart and brain. {ECO:0000269|PubMed:10369257, ECO:0000269|PubMed:10642534}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach; fetal liver;superior cervical ganglion;liver;trigeminal ganglion;skeletal muscle; 0.22708 0.45218 -1.155457828 6.168907761 87.75977 2.00080 SLC25A14 0.979191684320595 0.0207906498191291 1.76658602759134e-05 solute carrier family 25 member 14 FUNCTION: Participates in the mitochondrial proton leak measured in brain mitochondria.; . TISSUE SPECIFICITY: Mainly expressed in brain. Some expression in testis and pituitary. {ECO:0000269|PubMed:10928996}.; colon;retina;bone marrow;uterus;prostate;whole body;endometrium;thyroid;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;hypothalamus;globus pallidus;atrioventricular node;cingulate cortex;skeletal muscle; 0.57589 0.12887 -0.141298762 42.87567823 9.38046 0.34511 SLC25A14P1 . . . solute carrier family 25 member 14 pseudogene 1 . . . . . . . . . . . SLC25A15 0.00124731974401554 0.851616080401696 0.147136599854288 solute carrier family 25 member 15 FUNCTION: Ornithine transport across inner mitochondrial membrane, from the cytoplasm to the matrix.; DISEASE: Hyperornithinemia-hyperammonemia-homocitrullinuria syndrome (HHH syndrome) [MIM:238970]: Autosomal recessive disorder resulting in various neurologic symptoms, including mental retardation, spastic paraparesis with pyramidal signs, cerebellar ataxia, and episodic disturbance of consciousness or coma caused by hyperammonemia. It causes a functional impairment of the urea cycle. {ECO:0000269|PubMed:10369256, ECO:0000269|PubMed:10805333, ECO:0000269|PubMed:11552031, ECO:0000269|PubMed:11668643, ECO:0000269|PubMed:11814739, ECO:0000269|PubMed:16601889, ECO:0000269|PubMed:19242930}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;ovary;fovea centralis;choroid;lens;skin;retina;breast;pancreas;optic nerve;whole body;lung;endometrium;thyroid;macula lutea;visual apparatus;hippocampus;liver;testis;germinal center;kidney;brain; fetal liver;testis - interstitial;thyroid;liver;testis;bone marrow; 0.16524 . 0.082802743 60.09082331 456.37513 4.43813 SLC25A15P1 . . . solute carrier family 25 member 15 pseudogene 1 . . . . . . . . . . . SLC25A15P2 . . . solute carrier family 25 member 15 pseudogene 2 . . . . . . . . . . . SLC25A15P3 . . . solute carrier family 25 member 15 pseudogene 3 . . . . . . . . . . . SLC25A15P4 . . . solute carrier family 25 member 15 pseudogene 4 . . . . . . . . . . . SLC25A15P5 . . . solute carrier family 25 member 15 pseudogene 5 . . . . . . . . . . . SLC25A16 0.000247608136026081 0.92471525202562 0.0750371398383537 solute carrier family 25 member 16 FUNCTION: Required for the accumulation of coenzyme A in the mitochondrial matrix. {ECO:0000269|PubMed:11158296}.; . . ovary;colon;parathyroid;skin;uterus;prostate;frontal lobe;larynx;thyroid;bone;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;pia mater;lung;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion; 0.07884 0.12672 -0.427900189 25.14744043 9.89369 0.36269 SLC25A17 0.0241848435983763 0.961954399625736 0.0138607567758879 solute carrier family 25 member 17 FUNCTION: Peroxisomal transporter for multiple cofactors like coenzyme A (CoA), flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN) and nucleotide adenosine monophosphate (AMP), and to a lesser extend for nicotinamide adenine dinucleotide (NAD(+)), adenosine diphosphate (ADP) and adenosine 3',5'- diphosphate (PAP). May catalyze the transport of free CoA, FAD and NAD(+) from the cytosol into the peroxisomal matrix by a counter- exchange mechanism. Inhibited by pyridoxal 5'-phosphate and bathophenanthroline in vitro. {ECO:0000269|PubMed:12445829, ECO:0000269|PubMed:22185573}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in liver. {ECO:0000269|PubMed:22185573}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.10581 0.11631 0.040529541 57.15380986 63.66709 1.63572 SLC25A18 0.0110646872211993 0.947842447959453 0.0410928648193471 solute carrier family 25 member 18 FUNCTION: Involved in the transport of glutamate across the inner mitochondrial membrane. Glutamate is cotransported with H(+). {ECO:0000269|PubMed:11897791}.; . . unclassifiable (Anatomical System);pineal body;fovea centralis;choroid;lens;skin;retina;breast;prostate;optic nerve;frontal lobe;bone;macula lutea;liver;iris;kidney;brain; . 0.14284 . -0.558357437 19.54470394 31.61854 0.99454 SLC25A18P1 . . . solute carrier family 25 member 18 pseudogene 1 . . . . . . . . . . . SLC25A19 0.929610775752259 0.0700226843279866 0.000366539919754557 solute carrier family 25 member 19 FUNCTION: Mitochondrial transporter mediating uptake of thiamine pyrophosphate (ThPP) into mitochondria. {ECO:0000269|PubMed:18280798}.; DISEASE: Thiamine metabolism dysfunction syndrome 4, bilateral striatal degeneration and progressive polyneuropathy type (THMD4) [MIM:613710]: A disease characterized by recurrent episodes of flaccid paralysis and encephalopathy associated with bilateral striatal necrosis and chronic progressive polyneuropathy. {ECO:0000269|PubMed:19798730}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all tissues examined except for placenta. Highest levels in colon, kidney, lung, testis, spleen, and brain. {ECO:0000269|PubMed:11226231}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;heart;pineal body;colon;blood;skin;skeletal muscle;bone marrow;breast;uterus;pancreas;whole body;lung;bone;placenta;liver;testis;kidney;germinal center;brain;aorta;stomach; . 0.13749 0.17824 -0.426079032 25.36565228 1647.41747 7.49995 SLC25A20 2.04566835698354e-07 0.442417898329617 0.557581897103547 solute carrier family 25 member 20 FUNCTION: Mediates the transport of acylcarnitines of different length across the mitochondrial inner membrane from the cytosol to the mitochondrial matrix for their oxidation by the mitochondrial fatty acid-oxidation pathway.; DISEASE: Carnitine-acylcarnitine translocase deficiency (CACTD) [MIM:212138]: A rare long-chain fatty acid oxidation disorder. Metabolic consequences include hypoketotic hypoglycemia under fasting conditions, hyperammonemia, elevated creatine kinase and transaminases, dicarboxylic aciduria, very low free carnitine and abnormal acylcarnitine profile with marked elevation of the long- chain acylcarnitines. Clinical features include neurologic abnormalities, cardiomyopathy, arrhythmias, skeletal muscle damage, liver dysfunction and episodes of life-threatening coma, which eventually lead to death. Most patients become symptomatic in the neonatal period with a rapidly progressive deterioration and a high mortality rate. {ECO:0000269|PubMed:12859414, ECO:0000269|PubMed:15057979, ECO:0000269|PubMed:15365988}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;medulla oblongata;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;synovium;bone;iris;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.45738 0.22824 -0.139478553 43.29440906 59.37497 1.56224 SLC25A20P1 . . . solute carrier family 25 member 20 pseudogene 1 . . . . . . . . . . . SLC25A21 6.47218604218705e-07 0.450125174535057 0.549874178246339 solute carrier family 25 member 21 FUNCTION: Transports C5-C7 oxodicarboxylates across the inner membranes of mitochondria. Can transport 2-oxoadipate, 2- oxoglutarate, adipate, glutarate, and to a lesser extent, pimelate, 2-oxopimelate, 2-aminoadipate, oxaloacetate, and citrate.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11083877}.; unclassifiable (Anatomical System);islets of Langerhans;nasopharynx;trabecular meshwork;bone;hippocampus;liver;spleen; superior cervical ganglion;appendix;atrioventricular node;pons;trigeminal ganglion; 0.31542 0.26739 0.72761005 86.08162302 304.9847 3.71828 SLC25A21-AS1 0.387549574235059 0.475587076265577 0.136863349499364 SLC25A21 antisense RNA 1 . . . . . . . . . 160.59404 2.76636 SLC25A22 0.568405564949865 0.429078030349956 0.00251640470017814 solute carrier family 25 member 22 FUNCTION: Involved in the transport of glutamate across the inner mitochondrial membrane. Glutamate is cotransported with H(+). {ECO:0000269|PubMed:11897791}.; . TISSUE SPECIFICITY: Highly expressed in most tissues.; colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;bladder;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;muscle;lens;pancreas;lung;placenta;macula lutea;visual apparatus;cervix;kidney;stomach;peripheral nerve;cerebellum; whole brain;amygdala;medulla oblongata;subthalamic nucleus;cerebellum peduncles;temporal lobe;prefrontal cortex;globus pallidus;pons;trigeminal ganglion;cingulate cortex;cerebellum; 0.40270 0.12155 0.128714042 63.19886766 219.59154 3.20559 SLC25A23 0.0760416946192497 0.921548096990618 0.00241020839013213 solute carrier family 25 member 23 FUNCTION: Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. May act as a ATP-Mg/Pi exchanger that mediates the transport of Mg-ATP in exchange for phosphate, catalyzing the net uptake or efflux of adenine nucleotides into or from the mitochondria. {ECO:0000269|PubMed:15123600}.; . TISSUE SPECIFICITY: Present in various cell lines (at protein level). Expressed at low levels in most tissues examined, with highest expression in brain, skeletal muscle and pancreas. {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600, ECO:0000269|PubMed:15716113}.; lymphoreticular;medulla oblongata;ovary;colon;substantia nigra;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;larynx;bone;thyroid;testis;bladder;brain;artery;unclassifiable (Anatomical System);heart;tongue;hypothalamus;blood;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;head and neck;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;subthalamic nucleus;cerebellum peduncles;caudate nucleus;skeletal muscle; 0.17610 0.10569 -1.021348453 7.997169144 134.75173 2.52347 SLC25A24 4.89817247272209e-09 0.369059739433551 0.630940255668277 solute carrier family 25 member 24 FUNCTION: Calcium-dependent mitochondrial solute carrier. Mediates the reversible, electroneutral exchange of Mg-ATP or Mg-ADP against phosphate ions, catalyzing the net uptake or efflux of adenine nucleotides across the mitochondrial inner membrane. Nucleotide transport is inactive when cytosolic calcium levels are low, and is activated by an increase in cytosolic calcium levels. May play a role in protecting cells against oxidative stress- induced cell death, probably by promoting the formation of calcium-phosphate precipitates in the mitochondrial matrix, and thereby buffering calcium levels in the mitochondrial matrix. {ECO:0000269|PubMed:15123600, ECO:0000269|PubMed:22015608}.; . TISSUE SPECIFICITY: Present in various cell lines (at protein level). Expressed in all tissues tested. Highly expressed in testis, expressed at intermediate level in small intestine and pancreas, and weakly expressed in kidney, spleen, liver, skeletal muscle and heart. {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;cervix;kidney;stomach;aorta; . 0.16689 0.11395 -0.710864321 14.5730125 39.69367 1.16974 SLC25A24P1 . . . SLC25A24 pseudogene 1 . . . . . . . . . . . SLC25A24P2 . . . SLC25A24 pseudogene 2 . . . . . . . . . . . SLC25A25 0.973302049193279 0.0266913243626327 6.62644408798639e-06 solute carrier family 25 member 25 FUNCTION: Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. May act as a ATP-Mg/Pi exchanger that mediates the transport of Mg-ATP in exchange for phosphate, catalyzing the net uptake or efflux of adenine nucleotides into or from the mitochondria. {ECO:0000269|PubMed:15123600}.; . TISSUE SPECIFICITY: Present in various cell lines (at protein level). Widely expressed. Expressed in fetal and adult liver, skeletal muscle, testis, ovary, hippocampus and caudate nucleus. Isoform 1 is present in all tissues tested. Isoform 2 expression is restricted to kidney and lung. {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600}.; . . 0.11945 0.09594 -0.44448505 24.46331682 56.75648 1.51571 SLC25A25-AS1 . . . SLC25A25 antisense RNA 1 . . . . . . . . . . . SLC25A26 4.24371628598418e-09 0.0559248311408416 0.944075164615442 solute carrier family 25 member 26 FUNCTION: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Specifically mediates the transport of S- adenosylmethionine (SAM) into the mitochondria. {ECO:0000269|PubMed:14674884}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis, with moderate expression in brain, heart, kidney, lung, skeletal muscle, pancreas, small intestine and liver, and low expression in spleen. {ECO:0000269|PubMed:14674884}.; myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;cochlea;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; . 0.10003 0.09077 -0.073340031 48.11866006 2723.524 9.83828 SLC25A27 0.160724478287132 0.838621466139621 0.000654055573246992 solute carrier family 25 member 27 FUNCTION: UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation from ATP synthesis. As a result, energy is dissipated in the form of heat. May play a role in thermoregulatory heat production and metabolism in brain.; . TISSUE SPECIFICITY: Found in adult and fetal brain. Present in most of the brain tissues, with low levels in spinal chord, corpus callosum and substantia nigra.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;skin;skeletal muscle;retina;uterus;prostate;lung;frontal lobe;cerebral cortex;bone;placenta;pituitary gland;liver;testis;spleen;germinal center;kidney;brain; . 0.13841 0.14688 0.527368849 80.73248408 271.68756 3.53155 SLC25A28 0.765079077823325 0.233085016876997 0.0018359052996774 solute carrier family 25 member 28 FUNCTION: Mitochondrial iron transporter that mediates iron uptake. Probably required for heme synthesis of hemoproteins and Fe-S cluster assembly in non-erythroid cells. The iron delivered into the mitochondria, presumably as Fe(2+), is then probably delivered to ferrochelatase to catalyze Fe(2+) incorporation into protoprophyrin IX to make heme (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in placenta, lung, kidney, pancreas, liver, brain, skeletal muscle and heart. {ECO:0000269|PubMed:11297739}.; . . 0.41958 0.14896 -0.383807564 27.41802312 11.5052 0.41490 SLC25A29 0.00606097276523407 0.734754721925569 0.259184305309197 solute carrier family 25 member 29 FUNCTION: Transports arginine, lysine, homoarginine, methylarginine and, to a much lesser extent, ornithine and histidine. Does not transport carnitine nor acylcarnitines. Functions by both counter-exchange and uniport mechanisms. {ECO:0000269|PubMed:19287344, ECO:0000269|PubMed:24652292}.; . . medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;urinary;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;thyroid; 0.34201 0.15406 . . 31.70384 0.99818 SLC25A30 8.39152402794254e-06 0.756772638886474 0.243218969589498 solute carrier family 25 member 30 FUNCTION: Probable transporter. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; . 0.10192 -0.093566408 46.7386176 68.6688 1.71508 SLC25A30-AS1 . . . SLC25A30 antisense RNA 1 . . . . . . . . . . . SLC25A31 3.01905109757447e-06 0.538731306689887 0.461265674259015 solute carrier family 25 member 31 FUNCTION: Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. May serve to mediate energy generating and energy consuming processes in the distal flagellum, possibly as a nucleotide shuttle between flagellar glycolysis, protein phosphorylation and mechanisms of motility. {ECO:0000269|PubMed:17137571}.; . TISSUE SPECIFICITY: Expressed in brain, liver, sperm and testis. {ECO:0000269|PubMed:15670820, ECO:0000269|PubMed:17137571}.; unclassifiable (Anatomical System);lung;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.37970 0.12570 -0.137658575 43.57159707 88.11761 2.00961 SLC25A32 7.69073648140823e-07 0.287599125477482 0.71240010544887 solute carrier family 25 member 32 FUNCTION: Transports folate across the inner membranes of mitochondria.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;pituitary gland;testis;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;pia mater;lung;mesenchyma;epididymis;placenta;macula lutea;visual apparatus;duodenum;liver;kidney;mammary gland;stomach;thymus; . 0.10459 0.12783 -0.049474214 50.01179523 356.24216 3.99564 SLC25A33 0.451158319130907 0.542629964275353 0.00621171659373998 solute carrier family 25 member 33 FUNCTION: Mitochondrial transporter that imports/exports pyrimidine nucleotides into and from mitochondria (PubMed:25320081). Transports preferentially uracil, thymine, and cytosine (deoxy)nucleoside di- and triphosphates by an antiport mechanism (PubMed:25320081). Also transports guanine but not adenine (deoxy)nucleotides (PubMed:25320081). Is inhibited strongly by pyridoxal 5'-phosphate, 4,7-diphenyl-1,10- phenanthroline, tannic acid, and mercurials (mercury dichloride, mersalyl acid, p-hydroxymercuribenzoate) (PubMed:25320081). Participates in mitochondrial genome maintenance, regulation of mitochondrial membrane potential and mitochondrial respiration (PubMed:20453889). Upon INS or IGF1 stimulation regulates cell growth and proliferation by controlling mitochondrial DNA replication and transcription, the ratio of mitochondria-to nuclear-encoded components of the electron transport chain resulting in control of mitochondrial ROS production (PubMed:20453889, PubMed:17596519). Participates in dendritic cell endocytosis and may associate with mitochondrial oxidative phosphorylation (PubMed:14715278). {ECO:0000269|PubMed:14715278, ECO:0000269|PubMed:17596519, ECO:0000269|PubMed:20453889, ECO:0000269|PubMed:25320081}.; . TISSUE SPECIFICITY: Expressed in the central nervous system. Also expressed in testis and skeletal muscle. Weakly expressed in heart, liver, kidney, prostate, colon and peripheral blood leukocytes. {ECO:0000269|PubMed:14715278}.; medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;skin;uterus;prostate;cerebral cortex;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;pharynx;blood;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; . 0.11005 0.08763 -0.183570861 39.95046001 171.56863 2.85629 SLC25A34 0.000948152762042176 0.807452480567583 0.191599366670374 solute carrier family 25 member 34 . . . unclassifiable (Anatomical System);lung;hippocampus;testis;colon;kidney;brain;skeletal muscle;stomach; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19588 0.11065 -0.113792788 45.25831564 133.34842 2.50880 SLC25A35 3.54303681221832e-09 0.0952149041898912 0.904785092267072 solute carrier family 25 member 35 . . . . . 0.14009 . -0.648365105 16.35999056 40.25226 1.18284 SLC25A36 0.88301361858947 0.116709235303887 0.000277146106642726 solute carrier family 25 member 36 FUNCTION: Mitochondrial transporter that imports/exports pyrimidine nucleotides into and from mitochondria. Transports preferentially cytosine and uracil (deoxy)nucleoside mono-, di-, and triphosphates by uniport and antiport mechanism. Also transports guanine but not adenine (deoxy)nucleotides. Is inhibited strongly by pyridoxal 5'-phosphate, 4,7-diphenyl-1,10- phenanthroline, tannic acid, and mercurials (mercury dichloride, Mersalyl acid, p-hydroxymercuribenzoate). Participates in mitochondrial genome maintenance, regulation of mitochondrial membrane potential and mitochondrial respiration. {ECO:0000269|PubMed:25320081}.; . TISSUE SPECIFICITY: Expressed at moderate level. {ECO:0000269|PubMed:17210862}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;hypothalamus;colon;skin;skeletal muscle;uterus;prostate;whole body;lung;cochlea;endometrium;bone;thyroid;placenta;hippocampus;liver;testis;germinal center;kidney;brain;mammary gland;stomach; amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;globus pallidus;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.16774 0.10791 -0.405853867 26.23260203 27.59314 0.88809 SLC25A36P1 . . . SLC25A36 pseudogene 1 . . . . . . . . . . . SLC25A37 0.512222994662905 0.483861462224731 0.00391554311236428 solute carrier family 25 member 37 FUNCTION: Mitochondrial iron transporter that specifically mediates iron uptake in developing erythroid cells, thereby playing an essential role in heme biosynthesis. The iron delivered into the mitochondria, presumably as Fe(2+), is then probably delivered to ferrochelatase to catalyze Fe(2+) incorporation into protoprophyrin IX to make heme (By similarity). {ECO:0000250}.; . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;epidermis;islets of Langerhans;hypothalamus;blood;bile duct;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; fetal liver;prostate;adrenal gland;adrenal cortex;fetal lung;whole blood;bone marrow; 0.91226 0.11320 0.106667882 61.73036093 2843.93274 10.08249 SLC25A38 0.0682178285427916 0.917991739141274 0.0137904323159347 solute carrier family 25 member 38 FUNCTION: Mitochondrial carrier required during erythropoiesis. Probably involved in the biosynthesis of heme, possibly by facilitating 5-aminolevulinate (ALA) production. May act by importing glycine into mitochondria or by exchanging glycine for ALA across the mitochondrial inner membrane. {ECO:0000255|HAMAP- Rule:MF_03064, ECO:0000269|PubMed:19412178}.; . TISSUE SPECIFICITY: Preferentially expressed in erythroid cells. {ECO:0000269|PubMed:19412178}.; lymphoreticular;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;adrenal gland;placenta;head and neck;kidney;stomach;thymus; testis; 0.21366 0.11683 -0.003562597 53.72729417 112.35244 2.30589 SLC25A38P1 . . . solute carrier family 25 member 38 pseudogene 1 . . . . . . . . . . . SLC25A39 0.000102385453221932 0.943266098493211 0.0566315160535667 solute carrier family 25 member 39 FUNCTION: Required for normal heme biosynthesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in many tissues. Abundant in testis and kidney. {ECO:0000269|PubMed:11139402}.; lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;ganglion;endometrium;oesophagus;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;muscle;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; heart;thyroid;trigeminal ganglion;bone marrow; 0.13582 0.10674 -0.999300439 8.368719038 27.97109 0.89763 SLC25A39P1 . . . solute carrier family 25 member 39 pseudogene 1 . . . . . . . . . . . SLC25A39P2 . . . SLC25A39 pseudogene 2 . . . . . . . . . . . SLC25A40 2.14670620627733e-07 0.451957554575069 0.54804223075431 solute carrier family 25 member 40 . . . unclassifiable (Anatomical System);ovary;lacrimal gland;colon;fovea centralis;choroid;lens;vein;skeletal muscle;retina;prostate;optic nerve;whole body;lung;adrenal gland;placenta;macula lutea;testis;germinal center;brain;bladder;stomach; . 0.16425 0.12612 0.016664174 55.21939137 142.7385 2.60522 SLC25A41 5.97614676962731e-05 0.70333186921232 0.296608369319984 solute carrier family 25 member 41 . . . unclassifiable (Anatomical System);medulla oblongata; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;appendix;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.09690 0.10776 1.422020658 94.93394669 887.15126 5.80192 SLC25A42 0.208308450498004 0.782395321431939 0.00929622807005728 solute carrier family 25 member 42 FUNCTION: Mitochondrial carrier mediating the transport of coenzyme A (CoA) in mitochondria in exchange for intramitochondrial (deoxy)adenine nucleotides and adenosine 3',5'- diphosphate. {ECO:0000269|PubMed:19429682}.; . . ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;frontal lobe;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;lung;placenta;liver;spleen;cervix;kidney;mammary gland;thymus; superior cervical ganglion;liver;kidney; 0.26279 0.11044 -0.161524709 41.6430762 24.33192 0.79937 SLC25A43 0.0529550244704604 0.86275660469067 0.0842883708388695 solute carrier family 25 member 43 . . . unclassifiable (Anatomical System);cartilage;skin;skeletal muscle;bone marrow;bile duct;uterus;pancreas;lung;placenta;liver;testis;kidney;brain;mammary gland; superior cervical ganglion;ciliary ganglion; 0.06950 . 0.281220278 71.07808445 10.86761 0.39321 SLC25A44 0.247810862226725 0.745743423497539 0.00644571427573647 solute carrier family 25 member 44 . . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;pineal body;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; amygdala;whole brain;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;kidney;cingulate cortex;parietal lobe;cerebellum; 0.28608 0.11262 -0.427900189 25.14744043 20.57854 0.69936 SLC25A45 7.20169689648338e-07 0.278171370398289 0.721827909432021 solute carrier family 25 member 45 . . . myocardium;medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hippocampus;visual apparatus;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;subthalamic nucleus; 0.04069 0.06956 1.550689283 95.62396792 327.77888 3.84828 SLC25A46 0.00117611684259399 0.955902847010004 0.0429210361474017 solute carrier family 25 member 46 . . . ovary;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.18417 0.10736 0.839664339 88.29912715 215.81357 3.17135 SLC25A47 3.17553796647681e-12 0.0112908666252836 0.988709133371541 solute carrier family 25 member 47 FUNCTION: Uncoupling protein which may catalyze the physiological 'proton leak' in liver. Overexpression induces the dissipation of mitochondrial membrane potential. {ECO:0000269|PubMed:15322095}.; . TISSUE SPECIFICITY: Specifically expressed in liver. {ECO:0000269|PubMed:15322095}.; liver;spleen; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;trigeminal ganglion; 0.12401 0.08923 0.468503535 78.79806558 280.27618 3.58749 SLC25A47P1 . . . solute carrier family 25 member 47 pseudogene 1 . . . . . . . . . . . SLC25A48 0.3910144779106 0.567023623877098 0.0419618982123026 solute carrier family 25 member 48 . . . unclassifiable (Anatomical System);kidney;brain; dorsal root ganglion;amygdala;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . . 0.527368849 80.73248408 46.38286 1.31306 SLC25A51 0.0492003687342311 0.858298698656611 0.0925009326091578 solute carrier family 25 member 51 . . . . . 0.26021 0.11103 -0.139478553 43.29440906 18.02048 0.62924 SLC25A51P1 . . . solute carrier family 25 member 51 pseudogene 1 . . . . . . . . . . . SLC25A51P2 . . . solute carrier family 25 member 51 pseudogene 2 . . . . . . . . . . . SLC25A51P3 . . . solute carrier family 25 member 51 pseudogene 3 . . . . . . . . . . . SLC25A52 0.00585592728276631 0.727940800534553 0.26620327218268 solute carrier family 25 member 52 . . . . . 0.14543 0.09565 0.461228372 78.46190139 217.56005 3.18890 SLC25A53 0.101916710137974 0.773411572468546 0.12467171739348 solute carrier family 25 member 53 . . . . . 0.28609 . 0.260991686 70.25831564 25.47651 0.83179 SLC26A1 4.01304192741795e-06 0.374643478989247 0.625352507968825 solute carrier family 26 member 1 FUNCTION: High affinity uptake of sulfate. Accepts oxalate, but not succinate as a cosubstrate. Mediates sulfate and oxalate transport. {ECO:0000269|PubMed:12713736}.; . TISSUE SPECIFICITY: Expressed most abundantly in the kidney and liver, with lower levels in the pancreas, testis, brain, small intestine, colon, and lung. {ECO:0000269|PubMed:12713736}.; unclassifiable (Anatomical System);cartilage;liver;spleen;kidney;brain;stomach; superior cervical ganglion;liver;globus pallidus;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.15798 0.17331 0.236922632 68.73083274 409.12548 4.24034 SLC26A2 2.16616893086973e-05 0.484994120332775 0.514984217977916 solute carrier family 26 member 2 FUNCTION: Sulfate transporter. May play a role in endochondral bone formation.; DISEASE: Achondrogenesis 1B (ACG1B) [MIM:600972]: A form of achondrogenesis type 1, a lethal form of chondrodysplasia characterized by deficient ossification in the lumbar vertebrae and absent ossification in the sacral, pubic and ischial bones and clinically by stillbirth or early death. In addition to severe micromelia, there is a disproportionately large cranium due to marked edema of soft tissues. {ECO:0000269|PubMed:8528239}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Atelosteogenesis 2 (AO2) [MIM:256050]: A perinatal dysplasia characterized by shortening of the limbs, a dysmorphic syndrome and radiographic skeletal features. Patients are stillborn or die soon after birth. {ECO:0000269|PubMed:8571951}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multiple epiphyseal dysplasia 4 (EDM4) [MIM:226900]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal. Multiple epiphyseal dysplasia type 4 is a recessively inherited form, characterized by early childhood-onset hip dysplasia and recurrent patella dislocation. Short stature is not frequent. {ECO:0000269|PubMed:12966518, ECO:0000269|PubMed:21922596}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;dura mater;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pia mater;lung;adrenal gland;nasopharynx;placenta;macula lutea;alveolus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;prostate;trachea;adrenal gland;placenta;adrenal cortex;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;pituitary; 0.09419 0.19429 0.180083178 66.16536919 1075.31491 6.28472 SLC26A3 3.07620637453319e-10 0.71666509109137 0.283334908601009 solute carrier family 26 member 3 FUNCTION: Chloride/bicarbonate exchanger. Mediates the efficient absorption of chloride ions in the colon, participating in fluid homeostasis. Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation.; DISEASE: Diarrhea 1, secretory chloride, congenital (DIAR1) [MIM:214700]: A disease characterized by voluminous watery stools containing an excess of chloride. The children with this disease are often premature. {ECO:0000269|PubMed:11524734, ECO:0000269|PubMed:19861545, ECO:0000269|PubMed:21150650, ECO:0000269|PubMed:21394828, ECO:0000269|PubMed:8896562, ECO:0000269|PubMed:9554749, ECO:0000269|PubMed:9718329}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);prostate;lung;colon;spleen;blood;mammary gland;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.35445 0.25112 0.602602982 82.87331918 533.02806 4.70926 SLC26A4 6.36692519367205e-13 0.204987783815785 0.795012216183578 solute carrier family 26 member 4 FUNCTION: Sodium-independent transporter of chloride and iodide. {ECO:0000269|PubMed:10192399}.; DISEASE: Deafness, autosomal recessive, 4 (DFNB4) [MIM:600791]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNB4 is associated with an enlarged vestibular aqueduct. {ECO:0000269|PubMed:10190331, ECO:0000269|PubMed:10700480, ECO:0000269|PubMed:11748854, ECO:0000269|PubMed:12676893, ECO:0000269|PubMed:14508505, ECO:0000269|PubMed:14679580, ECO:0000269|PubMed:19204907, ECO:0000269|PubMed:20108392, ECO:0000269|PubMed:20597900, ECO:0000269|PubMed:9500541}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: High expression in adult thyroid, lower expression in adult and fetal kidney and fetal brain. Not expressed in other tissues.; unclassifiable (Anatomical System);heart;hypothalamus;adrenal cortex;parathyroid;skeletal muscle;skin;uterus;lung;adrenal gland;thyroid;head and neck;kidney;brain;pineal gland; superior cervical ganglion;thyroid;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.51161 0.43881 1.139030387 92.34489266 1009.39813 6.11806 SLC26A4-AS1 . . . SLC26A4 antisense RNA 1 . . . . . . . . . . . SLC26A5 0.00137555507026871 0.998308808997194 0.000315635932537363 solute carrier family 26 member 5 FUNCTION: Motor protein that converts auditory stimuli to length changes in outer hair cells and mediates sound amplification in the mammalian hearing organ. Prestin is a bidirectional voltage- to-force converter, it can operate at microsecond rates. It uses cytoplasmic anions as extrinsic voltage sensors, probably chloride and bicarbonate. After binding to a site with millimolar affinity, these anions are translocated across the membrane in response to changes in the transmembrane voltage. They move towards the extracellular surface following hyperpolarization, and towards the cytoplasmic side in response to depolarization. As a consequence, this translocation triggers conformational changes in the protein that ultimately alter its surface area in the plane of the plasma membrane. The area decreases when the anion is near the cytoplasmic face of the membrane (short state), and increases when the ion has crossed the membrane to the outer surface (long state). So, it acts as an incomplete transporter. It swings anions across the membrane, but does not allow these anions to dissociate and escape to the extracellular space. Salicylate, an inhibitor of outer hair cell motility, acts as competitive antagonist at the prestin anion-binding site (By similarity). {ECO:0000250}.; DISEASE: Deafness, autosomal recessive, 61 (DFNB61) [MIM:613865]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:12719379}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);frontal lobe; . 0.27216 0.30983 -0.354480518 29.42911064 69.71764 1.73192 SLC26A6 3.31045065696163e-05 0.997248799948806 0.00271809554462482 solute carrier family 26 member 6 FUNCTION: Apical membrane anion-exchanger with wide epithelial distribution that plays a role as a component of the pH buffering system for maintaining acid-base homeostasis. Acts as a versatile DIDS-sensitive inorganic and organic anion transporter that mediates the uptake of monovalent anions like chloride, bicarbonate, formate and hydroxyl ion and divalent anions like sulfate and oxalate. Function in multiple exchange modes involving pairs of these anions, which include chloride-bicarbonate, chloride-oxalate, oxalate-formate, oxalate-sulfate and chloride- formate exchange. Apical membrane chloride-bicarbonate exchanger that mediates luminal chloride absorption and bicarbonate secretion by the small intestinal brush border membrane and contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption, possibly by providing a bicarbonate import pathway. Mediates also intestinal chloride absorption and oxalate secretion, thereby preventing hyperoxaluria and calcium oxalate urolithiasis. Transepithelial oxalate secretion, chloride-formate, chloride- oxalate and chloride-bicarbonate transport activities in the duodenum are inhibited by PKC activation in a calcium-independent manner. The apical membrane chloride-bicarbonate exchanger provides also a major route for fluid and bicarbonate secretion into the proximal tubules of the kidney as well as into the proximal part of the interlobular pancreatic ductal tree, where it mediates electrogenic chloride-bicarbonate exchange with a chloride-bicarbonate stoichiometry of 1:2, and hence will dilute and alkalinize protein-rich acinar secretion. Mediates also the transcellular sulfate absorption and oxalate secretion across the apical membrane in the duodenum and the formate ion efflux at the apical brush border of cells in the proximal tubules of kidney. Plays a role in sperm capacitation by increasing intracellular pH.; . TISSUE SPECIFICITY: Ubiquitous. Highest levels in kidney and pancreas. Lower expression in heart, skeletal muscle, liver and placenta. Also found in lung and brain. Isoform 4 is ubiquitously expressed. Isoform 6 is expressed in heart, brain, placenta, lung, liver, kidney, pancreas, spleen, thymus, prostate, testis and ovary. Isoform 5 is expressed weakly in placenta, lung, liver and pancreas. {ECO:0000269|PubMed:11087667, ECO:0000269|PubMed:11247665}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;prostate;optic nerve;whole body;endometrium;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;tongue;urinary;muscle;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;globus pallidus;kidney;pons;caudate nucleus;trigeminal ganglion;skeletal muscle; . 0.24490 -0.064242613 48.844067 1122.15781 6.39562 SLC26A7 3.32458521232632e-08 0.923716210548673 0.076283756205475 solute carrier family 26 member 7 FUNCTION: Acts as a sodium-independent DIDS-sensitive anion exchanger mediating bicarbonate, chloride, sulfate and oxalate transport. May play a role in the maintenance of the electrolyte and acid-base homeostasis in the kidney, by acting as a distal excretory segment-specific anion exchanger. Plays a major role in gastric acid secretion. {ECO:0000250|UniProtKB:Q8R2Z3, ECO:0000269|PubMed:11834742, ECO:0000269|PubMed:12736153}.; . TISSUE SPECIFICITY: Expressed in tonsillar high endothelial venule endothelial cells (HEVEC), placenta and in testis, expressed in a subgroup of basal cells in the epididymal ducts. {ECO:0000269|PubMed:11829495, ECO:0000269|PubMed:11834742, ECO:0000269|PubMed:15956810, ECO:0000269|PubMed:17504921}.; unclassifiable (Anatomical System);smooth muscle;adrenal cortex;colon;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;adrenal gland;nasopharynx;placenta;thyroid;macula lutea;kidney;brain;pineal gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.50174 0.12722 0.112125503 62.09601321 242.55786 3.36166 SLC26A8 7.64803110765732e-08 0.994414705799086 0.00558521772060331 solute carrier family 26 member 8 FUNCTION: Acts as a DIDS-sensitive anion exchanger mediating chloride, sulfate and oxalate transport. May fulfill critical anion exchange functions in male germ line during meiosis and hence may play a role in spermatogenesis. May be involved in a new regulatory pathway linking sulfate transport to RhoGTPase signaling in male germ cells. A critical component of the sperm annulus that is essential for correct sperm tail differentiation and motility and hence male fertility. May form a moleculer complex involved in the regulation of chloride and bicarbonate ions fluxes during sperm capacitation. {ECO:0000269|PubMed:11278976, ECO:0000269|PubMed:11834742, ECO:0000269|PubMed:22121115}.; DISEASE: Spermatogenic failure 3 (SPGF3) [MIM:606766]: A disorder characterized by primary infertility, sperm morphologic abnormalities, and moderate to severe asthenozoospermia, condition in which the percentage of progressively motile sperm is abnormally low. {ECO:0000269|PubMed:23582645}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expression observed exclusively in testis, restricted to the meiotic phase of the germ cell. Abundant expression located in the seminiferous tubules, concentrated on the luminal side of the tubuli harboring the spermatocytes and spermatids. Expressed in spermatozoa. {ECO:0000269|PubMed:11278976, ECO:0000269|PubMed:11834742}.; unclassifiable (Anatomical System);pineal body;thyroid;hippocampus;testis;brain;skeletal muscle;retina; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.15524 0.10607 0.694433477 85.28544468 2032.37507 8.29676 SLC26A9 0.0029854587016256 0.996911146085557 0.000103395212817419 solute carrier family 26 member 9 FUNCTION: DIDS- and thiosulfate- sensitive anion exchanger mediating chloride, sulfate and oxalate transport. Mediates chloride/bicarbonate exchange or chloride-independent bicarbonate extrusion thus assuring bicarbonate secretion. Inhibited by ammonium and thiosulfate. {ECO:0000269|PubMed:11834742, ECO:0000269|PubMed:15800055}.; . TISSUE SPECIFICITY: Predominantly expressed in lung at the luminal side of the bronchiolar and alveolar epithelium of lung. To a lower extent, also expressed in pancreas and prostate. {ECO:0000269|PubMed:11834742}.; unclassifiable (Anatomical System);myocardium;pancreas;lung;adrenal gland;thyroid;adrenal cortex;parathyroid;kidney;pineal gland;skeletal muscle;stomach; uterus;dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17926 0.11651 -0.143334748 42.35079028 424.02635 4.30029 SLC26A10 1.16500286588742e-09 0.315407383405252 0.684592615429745 solute carrier family 26 member 10 FUNCTION: Chloride/bicarbonate exchanger. {ECO:0000250}.; . . unclassifiable (Anatomical System);whole body;liver;brain;mammary gland; subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.28136 0.10001 2.223194575 98.15994338 2963.16741 10.31014 SLC26A11 4.10510695836507e-10 0.183354582991228 0.816645416598261 solute carrier family 26 member 11 FUNCTION: Exhibits sodium-independent sulfate anion transporter activity that may cooperate with SLC26A2 to mediate DIDS-sensitive sulfate uptake into high endothelial venules endothelial cells (HEVEC). {ECO:0000269|PubMed:12626430}.; . TISSUE SPECIFICITY: Detected in all tissues tested with highest expression observed in brain, kidney, HEVEC and placenta and lowest in pancreas, skeletal muscle, liver, lung and heart. {ECO:0000269|PubMed:11087667, ECO:0000269|PubMed:12626430}.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;endometrium;cerebral cortex;thyroid;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;lung;adrenal gland;placenta;macula lutea;visual apparatus;alveolus;cervix;spleen;kidney;mammary gland;stomach; amygdala;superior cervical ganglion;ciliary ganglion; 0.09274 0.10947 0.031219447 55.84453881 810.57173 5.59977 SLC27A1 0.000340153810588742 0.98834246650988 0.0113173796795316 solute carrier family 27 member 1 FUNCTION: Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. The LFCA import appears to be hormone-regulated in a tissue-specific manner. In adipocytes, but not myocytes, insulin induces a rapid translocation of FATP1 from intracellular compartments to the plasma membrane, paralleled by increased LFCA uptake. May act directly as a bona fide transporter, or alternatively, in a cytoplasmic or membrane- associated multimeric protein complex to trap and draw fatty acids towards accumulation. Plays a pivotal role in regulating available LFCA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. May be involved in regulation of cholesterol metabolism. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids (By similarity). {ECO:0000250, ECO:0000269|PubMed:12235169}.; . TISSUE SPECIFICITY: Highest levels of expression are detected in muscle and adipose tissue small, intermediate levels in small intestine, and barely detectable in liver. {ECO:0000269|PubMed:10873384}.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;frontal lobe;endometrium;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;stomach;cerebellum; globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.09007 0.24962 -0.799052816 12.45576787 97.28836 2.13158 SLC27A2 2.58257558060631e-05 0.921706631495341 0.0782675427488532 solute carrier family 27 member 2 FUNCTION: Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precurors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism. May be involved in translocation of long-chain fatty acids (LFCA) across membranes (By similarity). {ECO:0000250, ECO:0000269|PubMed:11980911}.; . TISSUE SPECIFICITY: Expressed in liver, kidney, placenta and pancreas. {ECO:0000269|PubMed:10198260}.; unclassifiable (Anatomical System);cartilage;colon;blood;skin;skeletal muscle;retina;bone marrow;bile duct;uterus;prostate;lung;bone;placenta;liver;testis;cervix;germinal center;kidney;brain;stomach; superior cervical ganglion;fetal liver;liver;kidney;trigeminal ganglion;skeletal muscle; 0.47379 0.18145 -0.488577883 22.64685067 85.71225 1.97623 SLC27A3 7.80147738518240e-11 0.247396463326937 0.752603536595049 solute carrier family 27 member 3 FUNCTION: Has acyl-CoA ligase activity for long-chain and very- long-chain fatty acids. Does not exhibit fatty acid transport activity (By similarity). {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;lens;lung;cornea;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis; 0.05710 0.10747 -0.815648973 12.01344657 386.29362 4.13896 SLC27A4 0.00122183971500027 0.989827173724493 0.00895098656050713 solute carrier family 27 member 4 FUNCTION: Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. Appears to be the principal fatty acid transporter in small intestinal enterocytes. Plays a role in the formation of the epidermal barrier. Required for fat absorption in early embryogenesis. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids (VLCFAs). Indirectly inhibits RPE65 via substrate competition and via production of VLCFA derivatives like lignoceroyl-CoA. Prevents light-induced degeneration of rods and cones (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at highest levels in brain, testis, colon and kidney. Expressed at medium levels in heart and liver, small intestine and stomach. Expressed at low levels in peripheral leukocytes, bone marrow, skeletal muscle and aorta. Expressed in adipose tissue. {ECO:0000269|PubMed:9878842}.; colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;larynx;bone;brain;unclassifiable (Anatomical System);heart;tongue;pineal body;adrenal cortex;lens;lung;placenta;macula lutea;duodenum;amnion;cervix;head and neck;mammary gland;stomach;thymus; . 0.12755 0.18723 -1.083859071 7.195093182 214.94586 3.16352 SLC27A5 7.7072921738533e-08 0.708267610246283 0.291732312680795 solute carrier family 27 member 5 FUNCTION: Acyl-CoA synthetase involved in bile acid metabolism. Proposed to catalyze the first step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi by activating them to their CoA thioesters. Seems to activate secondary bile acids entering the liver from the enterohepatic circulation. In vitro, also activates 3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. {ECO:0000269|PubMed:10749848, ECO:0000269|PubMed:11980911}.; . TISSUE SPECIFICITY: Predominantly expressed in liver. {ECO:0000269|PubMed:10479480}.; ovary;salivary gland;intestine;colon;choroid;fovea centralis;retina;prostate;optic nerve;endometrium;testis;bladder;brain;unclassifiable (Anatomical System);pharynx;blood;lens;lung;nasopharynx;placenta;visual apparatus;macula lutea;liver;spleen;kidney;stomach; whole brain;liver; 0.07423 0.14975 0.292133603 71.59707478 372.95882 4.07436 SLC27A6 2.858831106907e-09 0.283148448747972 0.716851548393197 solute carrier family 27 member 6 FUNCTION: Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. Thought to function as the predominant fatty acid protein transporter in heart. {ECO:0000269|PubMed:12556534}.; . TISSUE SPECIFICITY: Strongly expressed in heart and localizes to cardiac myocytes. Expressed at moderate levels in placenta, testis, and adrenal glands. Expressed at very low levels in kidney, bladder and uterus. {ECO:0000269|PubMed:12556534}.; unclassifiable (Anatomical System);uterus;lung;ovary;heart;hypothalamus;placenta;adrenal cortex;testis;parathyroid;lens;skin; dorsal root ganglion;olfactory bulb;ciliary ganglion;trigeminal ganglion; 0.04825 0.08870 -0.132199953 43.97853267 291.24472 3.65033 SLC28A1 6.34799091474105e-07 0.969631365751843 0.030367999449065 solute carrier family 28 member 1 FUNCTION: Sodium-dependent and pyrimidine-selective. Exhibits the transport characteristics of the nucleoside transport system cit or N2 subtype (N2/cit) (selective for pyrimidine nucleosides and adenosine). It also transports the antiviral pyrimidine nucleoside analogs 3'-azido-3'-deoxythymidine (AZT) and 2',3'-dideoxycytidine (ddC). It may be involved in the intestinal absorption and renal handling of pyrimidine nucleoside analogs used to treat acquired immunodeficiency syndrome (AIDS). It has the following selective inhibition: adenosine, thymidine, cytidine, uridine >> guanosine, inosine.; . TISSUE SPECIFICITY: Expressed in kidney.; lymph node;liver;colon;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;kidney;pons;skeletal muscle; 0.06729 0.17051 0.762397607 86.8542109 7434.85143 18.51992 SLC28A2 9.71272786078653e-12 0.146972120123776 0.853027879866512 solute carrier family 28 member 2 FUNCTION: Sodium-dependent and purine-selective transporter. Exhibits the transport characteristics of the nucleoside transport system cif or N1 subtype (N1/cif) (selective for purine nucleosides and uridine). Plays a critical role in specific uptake and salvage of purine nucleosides in kidney and other tissues.; . TISSUE SPECIFICITY: Expressed in heart and skeletal muscle followed by liver, kidney, intestine, pancreas, placenta and brain. Weak expression in lung.; unclassifiable (Anatomical System);frontal lobe;colon; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skeletal muscle;cingulate cortex; 0.04500 0.15142 0.580556395 82.31304553 3531.80514 11.46439 SLC28A3 1.9648660260768e-17 0.00679344594423578 0.993206554055764 solute carrier family 28 member 3 FUNCTION: Sodium-dependent, pyrimidine- and purine-selective. Involved in the homeostasis of endogenous nucleosides. Exhibits the transport characteristics of the nucleoside transport system cib or N3 subtype (N3/cib) (with marked transport of both thymidine and inosine). Employs a 2:1 sodium/nucleoside ratio. Also able to transport gemcitabine, 3'-azido-3'-deoxythymidine (AZT), ribavirin and 3-deazauridine. {ECO:0000269|PubMed:11032837, ECO:0000269|PubMed:16446384, ECO:0000269|PubMed:17140564}.; . TISSUE SPECIFICITY: Expressed in pancreas, bone marrow, trachea, mammary gland, liver, prostate, and regions of intestine, brain, lung, placenta, testis, kidney, and heart. {ECO:0000269|PubMed:11032837}.; . . 0.17401 0.11684 0.846940207 88.47605567 2204.23741 8.64325 SLC29A1 0.964281534686621 0.0357048235601402 1.36417532388667e-05 solute carrier family 29 member 1 FUNCTION: Mediates both influx and efflux of nucleosides across the membrane (equilibrative transporter). It is sensitive (ES) to low concentrations of the inhibitor nitrobenzylmercaptopurine riboside (NBMPR) and is sodium-independent. It has a higher affinity for adenosine. Inhibited by dipyridamole and dilazep (anticancer chemotherapeutics drugs).; . TISSUE SPECIFICITY: Detected in erythrocytes (at protein level). Expressed in heart, brain, mammary gland, erythrocytes and placenta, and also in fetal liver and spleen. {ECO:0000269|PubMed:12527552, ECO:0000269|PubMed:23219802}.; lymphoreticular;myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;optic nerve;gum;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;heart;ciliary ganglion;atrioventricular node;skeletal muscle; 0.51344 0.22208 0.573279816 82.08303845 81.44022 1.91023 SLC29A2 1.32364671800173e-08 0.19715112292369 0.802848863839843 solute carrier family 29 member 2 FUNCTION: Mediates equilibrative transport of purine, pyrimidine nucleosides and the purine base hypoxanthine. Very less sensitive than SLC29A1 to inhibition by nitrobenzylthioinosine (NBMPR), dipyridamole, dilazep and draflazine. {ECO:0000269|PubMed:9396714}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, liver, lung, placenta, brain, heart, kidney and ovarian tissues. {ECO:0000269|PubMed:12527552, ECO:0000269|PubMed:9396714}.; ovary;colon;parathyroid;choroid;fovea centralis;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;brain;unclassifiable (Anatomical System);heart;lens;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;macula lutea;liver;cervix;kidney;stomach; skeletal muscle; 0.53383 0.17093 -0.600630256 18.06440198 69.77266 1.73291 SLC29A3 2.99085356226281e-08 0.090364089343553 0.909635880747911 solute carrier family 29 member 3 FUNCTION: Mediates both influx and efflux of nucleosides across the membrane (equilibrative transporter). Mediates transport of adenine, adenosine and uridine, as well as several nucleoside analog drugs, such as anticancer and antiviral agents, including cladribine, cordycepin, tubercidin and AZT. Does not transport hypoxanthine. {ECO:0000269|PubMed:15701636}.; . TISSUE SPECIFICITY: Widely expressed in both adult and fetal tissues. Highest levels in placenta, uterus, ovary, spleen, lymph node and bone marrow. Lowest levels in brain and heart. {ECO:0000269|PubMed:15701636}.; . . 0.25987 0.13482 0.42623145 77.29417315 7453.77783 18.55162 SLC29A4 0.00114748805216547 0.954539890008981 0.0443126219388538 solute carrier family 29 member 4 FUNCTION: Functions as a polyspecific organic cation transporter, efficiently transporting many organic cations such as monoamine neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines including serotonin, dopamine, norepinephrine and epinephrine. May play a role in regulating central nervous system homeostasis of monoamine neurotransmitters. May be involved in luminal transport of organic cations in the kidney and seems to use luminal proton gradient to drive organic cation reabsorption. Does not seem to transport nucleoside and nucleoside analogs such as uridine, cytidine, thymidine, adenosine, inosine, guanosine, and azidothymidine. In (PubMed:16873718) adenosine is efficiently transported but in a fashion highly sensitive to extracellular pH, with maximal activity in the pH range 5.5 to 6.5. Glu-206 is essential for the cation selectivity and may function as the charge sensor for cationic substrates. Transport is chloride and sodium-independent but appears to be sensitive to changes in membrane potential. Weakly inhibited by the classical inhibitors of equilibrative nucleoside transport, dipyridamole, dilazep, and nitrobenzylthioinosine. May play a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia. {ECO:0000269|PubMed:15448143, ECO:0000269|PubMed:16873718, ECO:0000269|PubMed:17018840, ECO:0000269|PubMed:17121826}.; . TISSUE SPECIFICITY: Expressed abundantly in the heart, in both cardiomyocytes and vascular endothelial cells (at protein level). Highly expressed in brain, kidney and skeletal muscle. In the brain expressed in cerebellum, cerebral cortex, medulla, occipital pole, frontal and temporal lobes putamen and in the spinal cord. Lower expression in liver, pancreas, and liver. Expressed in endometrial tissue, exclusively in the stroma. Expression is high in the proliferative phase, decreases during the secretory phase, and is no longer detectable in the menstrual phase. {ECO:0000269|PubMed:15448143, ECO:0000269|PubMed:16873718, ECO:0000269|PubMed:17018840, ECO:0000269|PubMed:17393420}.; unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;colon;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;lung;placenta;macula lutea;iris;amnion;liver;testis;head and neck;kidney;brain;stomach; . 0.22466 0.12965 -0.988411992 8.640009436 169.55813 2.84132 SLC29A4P1 . . . solute carrier family 29 member 4 pseudogene 1 . . . . . . . . . . . SLC29A4P2 . . . solute carrier family 29 member 4 pseudogene 2 . . . . . . . . . . . SLC30A1 0.913544366960314 0.0858384346812691 0.000617198358417365 solute carrier family 30 member 1 FUNCTION: May be involved in zinc transport out of the cell.; . . . . 0.45793 0.21012 -0.383807564 27.41802312 17.89411 0.62514 SLC30A2 0.708283236156756 0.291004209327709 0.000712554515534263 solute carrier family 30 member 2 . DISEASE: Zinc deficiency, transient neonatal (TNZD) [MIM:608118]: A disorder occurring in breast-fed infants as a consequence of low milk zinc concentration in their nursing mothers, which cannot be corrected by maternal zinc supplementation. A large amount of zinc, an essential trace mineral, is required for normal growth particularly in infants, and breast milk normally contains adequate zinc to meet the requirement for infants up to 4 to 6 months of age. Zinc deficiency can lead to dermatitis, alopecia, decreased growth, and impaired immune function. The disorder shows autosomal dominant inheritance with incomplete penetrance. {ECO:0000269|PubMed:17065149, ECO:0000269|PubMed:22733820}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.10482 0.15879 0.106667882 61.73036093 68.41308 1.71178 SLC30A3 0.64608387237045 0.35261806807218 0.00129805955737055 solute carrier family 30 member 3 FUNCTION: Involved in accumulation of zinc in synaptic vesicles. {ECO:0000250|UniProtKB:P97441}.; . . unclassifiable (Anatomical System);medulla oblongata;bone;testis;brain;retina; amygdala;whole brain;dorsal root ganglion;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.40810 0.15863 -0.80269335 12.23755603 30.41223 0.96921 SLC30A4 0.950659466932893 0.0493099652648861 3.05678022207918e-05 solute carrier family 30 member 4 FUNCTION: Probably involved in zinc transport out of the cytoplasm, maybe by sequestration into an intracellular compartment.; . . unclassifiable (Anatomical System);lymphoreticular;prostate;lung;ovary;placenta;testis;parathyroid;germinal center;skeletal muscle; superior cervical ganglion; 0.08489 0.12470 -0.516085732 21.20193442 37.57415 1.11916 SLC30A5 0.230512231685005 0.76942383353524 6.39347797548508e-05 solute carrier family 30 member 5 FUNCTION: Functions as a zinc transporter. May be a transporter of zinc into beta cells in order to form insulin crystals. Partly regulates cellular zinc homeostasis. Required with ZNT7 for the activation of zinc-requiring enzymes, alkaline phosphatases (ALPs). Transports zinc into the lumens of the Golgi apparatus and vesicular compartments where ALPs locate, thus, converting apoALPs to holoALPs. Required with ZNT6 and ZNT7 for the activation of TNAP. {ECO:0000269|PubMed:11904301, ECO:0000269|PubMed:11937503, ECO:0000269|PubMed:15276077, ECO:0000269|PubMed:15525635, ECO:0000269|PubMed:15994300}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in pancreas, liver and kidney. Expressed abundantly in insulin- containing beta cells, undetectable in other endocrine cell types including glucagon-secreting alpha cells and most acinar cells. {ECO:0000269|PubMed:11904301, ECO:0000269|PubMed:11937503}.; . . 0.61924 0.13187 -0.088107893 47.06298655 141.89318 2.60037 SLC30A6 0.0126596121889265 0.987030696886763 0.000309690924310788 solute carrier family 30 member 6 FUNCTION: Zinc-efflux transporter which allocates the cytoplasmic zinc to the trans-Golgi network (TGN) as well as the vesicular compartment. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain; especially in cerebellum, hippocampus, parahippocampal gyrus, superior and middle temporal gyrus. Also expressed in B-cells, colon, eye, and lung. Lower expression was present in bone, brain, cervix, ear, heart, kidney, muscle, nerve, pancreas, prostate, skin, stomach, and testis. {ECO:0000269|PubMed:15154973, ECO:0000269|PubMed:16580781}.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;skeletal muscle;skin;bone marrow;uterus;lung;nasopharynx;visual apparatus;liver;testis;spleen;head and neck;germinal center;brain; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.44615 0.09968 -1.001120478 8.321538099 41.65744 1.21356 SLC30A7 0.0289920473573277 0.96036679801331 0.0106411546293624 solute carrier family 30 member 7 FUNCTION: Seems to facilitate zinc transport from the cytoplasm into the Golgi apparatus. Partly regulates cellular zinc homeostasis. Required with ZNT5 for the activation of zinc- requiring enzymes, alkaline phosphatases (ALPs). Transports zinc into the lumens of the Golgi apparatus and the vesicular compartments where ALPs locate, thus, converting apoALPs to holoALPs. Required with ZNT5 and ZNT6 for the activation of TNAP (By similarity). {ECO:0000250, ECO:0000269|PubMed:15276077, ECO:0000269|PubMed:15994300}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);small intestine;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; superior cervical ganglion; 0.31860 0.12228 -0.692458599 14.96815287 39.1983 1.16132 SLC30A8 1.79754250091306e-09 0.0647003232593987 0.935299674943059 solute carrier family 30 member 8 FUNCTION: Facilitates the accumulation of zinc from the cytoplasm into intracellular vesicles, being a zinc-efflux transporter. May be a major component for providing zinc to insulin maturation and/or storage processes in insulin-secreting pancreatic beta- cells. {ECO:0000269|PubMed:16984975}.; . TISSUE SPECIFICITY: In the endocrine pancreas, expressed in insulin-producing beta cells. Expressed at relatively high levels in subcutaneous fat tissue from lean persons; much lower levels in visceral fat, whether from lean or obese individuals, and in subcutaneous fat tissue from obese individuals. Expressed in peripheral blood mononuclear cells, including T-cells and B-cells, with great variation among individuals ranging from negative to strongly positive. {ECO:0000269|PubMed:15331542, ECO:0000269|PubMed:16158222, ECO:0000269|PubMed:16984975, ECO:0000269|PubMed:17118530, ECO:0000269|PubMed:17971500}.; . . 0.12838 0.18950 0.086440867 60.47416844 1945.83178 8.11893 SLC30A9 0.00142348509355749 0.99851568192923 6.08329772123391e-05 solute carrier family 30 member 9 FUNCTION: Plays a role in the p160 coactivator signaling pathway that mediates transcriptional activation by nuclear receptors. Plays a role in transcriptional activation of Wnt-responsive genes. {ECO:0000250, ECO:0000269|PubMed:10409434}.; . TISSUE SPECIFICITY: Ubiquitously expressed in fetal and adult tissues and cancer cell lines. {ECO:0000269|PubMed:10409434}.; ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;gum;thyroid;iris;germinal center;bladder;brain;amygdala;heart;tongue;pineal body;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;thymus; amygdala;superior cervical ganglion;subthalamic nucleus;prefrontal cortex;cingulate cortex;skeletal muscle; 0.15803 0.13440 0.531004228 80.87992451 64.38665 1.64576 SLC30A10 0.921869997532192 0.0776527499640071 0.000477252503801219 solute carrier family 30 member 10 FUNCTION: Plays a pivotal role in manganese transport. Manganese is an essential cation for the function of several enzymes, including some crucially important for the metabolism of neurotransmitters and other neuronal metabolic pathways. {ECO:0000269|PubMed:22341971, ECO:0000269|PubMed:22341972}.; DISEASE: Hypermanganesemia with dystonia, polycythemia, and cirrhosis (HMDPC) [MIM:613280]: A metabolic autosomal recessive disorder characterized by dystonia, parkinsonism, extrapyramidal signs, severe hypermanganesemia, polycythemia, and chronic hepatic disease, including steatosis and cirrhosis. {ECO:0000269|PubMed:22341971, ECO:0000269|PubMed:22341972}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Specifically expressed in fetal liver and fetal brain. {ECO:0000269|PubMed:15154973}.; meninges;pia mater;hypothalamus;liver;dura mater;brain;skin; superior cervical ganglion;appendix;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.11526 0.12483 -0.404032746 26.53338051 37.65511 1.12117 SLC31A1 0.519265077977303 0.463634276337108 0.0171006456855887 solute carrier family 31 member 1 FUNCTION: High-affinity, saturable copper transporter involved in dietary copper uptake. {ECO:0000269|PubMed:11734551}.; . . . . 0.12285 0.12231 0.080983847 59.76055674 201.08896 3.06437 SLC31A1P1 . . . solute carrier family 31 member 1 pseudogene 1 . . . . . . . . . . . SLC31A2 2.78117305043228e-05 0.182918495195339 0.817053693074157 solute carrier family 31 member 2 FUNCTION: Involved in low-affinity copper uptake. {ECO:0000305}.; . TISSUE SPECIFICITY: Ubiquitous.; colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;bone;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;hypothalamus;adrenal cortex;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;alveolus;spleen;kidney;stomach;cerebellum; parietal lobe; 0.12497 0.09805 -0.053113545 49.38664779 8.1503 0.30038 SLC32A1 . . . solute carrier family 32 member 1 FUNCTION: Involved in the uptake of GABA and glycine into the synaptic vesicles.; . TISSUE SPECIFICITY: Retina. Expressed throughout the horizontal cells or more specifically at the terminals. {ECO:0000269|PubMed:12115694}.; unclassifiable (Anatomical System);optic nerve;lung;macula lutea;hippocampus;testis;fovea centralis;choroid;lens;brain;retina; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.74589 0.16863 -0.0274281 51.65723048 126.92006 2.45649 SLC33A1 0.100521117903096 0.892106887797749 0.00737199429915525 solute carrier family 33 member 1 FUNCTION: Probable acetyl-CoA transporter necessary for O- acetylation of gangliosides (PubMed:9096318). Negatively regulates BMP signaling (PubMed:25402622). {ECO:0000269|PubMed:25402622, ECO:0000269|PubMed:9096318}.; DISEASE: Congenital cataracts, hearing loss, and neurodegeneration (CCHLND) [MIM:614482]: An autosomal recessive disorder characterized by congenital cataracts, severe psychomotor retardation, and hearing loss associated with decreased serum ceruloplasmin and copper. Brain MRI shows cerebral and cerebellar atrophy and hypomyelination. {ECO:0000269|PubMed:22243965}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. With strongest signals in pancreas. {ECO:0000269|PubMed:9096318}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;urinary;lens;breast;pancreas;lung;placenta;macula lutea;duodenum;liver;spleen;head and neck;kidney;stomach;peripheral nerve; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.67249 . 0.196671391 67.19155461 1176.66655 6.51639 SLC34A1 1.07656497406863e-15 0.00271234151878063 0.997287658481218 solute carrier family 34 member 1 FUNCTION: May be involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane. Probably mediates 70-80% of the apical influx.; DISEASE: Fanconi renotubular syndrome 2 (FRTS2) [MIM:613388]: A disease due to a generalized dysfunction of the proximal kidney tubule resulting in decreased solute and water reabsorption. Patients have polydipsia and polyuria with phosphaturia, glycosuria and aminoaciduria. They may develop hypophosphatemic rickets or osteomalacia, acidosis and a tendency toward dehydration. Some eventually develop renal insufficiency. {ECO:0000269|PubMed:20335586}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Kidney and lung.; unclassifiable (Anatomical System);colon;kidney;stomach; . 0.22600 0.28784 -0.795417163 12.5324369 298.4701 3.68391 SLC34A2 1.02438347272582e-05 0.93769133827849 0.0622984178867825 solute carrier family 34 member 2 FUNCTION: May be involved in actively transporting phosphate into cells via Na(+) cotransport. It may be the main phosphate transport protein in the intestinal brush border membrane. May have a role in the synthesis of surfactant in lungs' alveoli.; DISEASE: Pulmonary alveolar microlithiasis (PALM) [MIM:265100]: Rare disease characterized by the deposition of calcium phosphate microliths throughout the lungs. Most patients are asymptomatic for several years or even for decades and generally, the diagnosis is incidental to clinical investigations unrelated to the disease. Cases with early-onset or rapid progression are rare. A 'sandstorm-appearing' chest roentgenogram is a typical diagnostic finding. The onset of this potentially lethal disease varies from the neonatal period to old age and the disease follows a long- term, progressive course, resulting in a slow deterioration of lung functions. Pulmonary alveolar microlithiasis is a recessive monogenic disease with full penetrance. {ECO:0000269|PubMed:16960801}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving SLC34A2 is found in a glioblastoma multiforme cell line U-118MG. Results in the formation of a SLC34A2-ROS1 chimeric protein that retains a constitutive kinase activity. {ECO:0000269|PubMed:12661006}.; TISSUE SPECIFICITY: Highly expressed in lung. Also detected in pancreas, kidney, small intestine, ovary, testis, prostate and mammary gland. In lung, it is found in alveolar type II cells but not in bronchiolar epithelium. {ECO:0000269|PubMed:10329428, ECO:0000269|PubMed:10610722}.; . . 0.25927 . 0.159856957 64.91507431 287.99634 3.63390 SLC34A3 2.02896416643879e-11 0.0333799143454344 0.966620085634276 solute carrier family 34 member 3 FUNCTION: May be involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane. Probably mediates 20-30% of the apical influx.; DISEASE: Hereditary hypophosphatemic rickets with hypercalciuria (HHRH) [MIM:241530]: Autosomal recessive form of hypophosphatemia characterized by reduced renal phosphate reabsorption and rickets. Increased serum levels of 1,25-dihydroxyvitamin D lead to increase in urinary calcium excretion. {ECO:0000269|PubMed:16358214, ECO:0000269|PubMed:16358215}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);colon;kidney;stomach; . 0.15241 0.17333 0.409650696 76.53927813 356.16708 3.99453 SLC35A1 0.208304140627799 0.78239924166844 0.0092966177037602 solute carrier family 35 member A1 FUNCTION: Transports CMP-sialic acid from the cytosol into Golgi vesicles where glycosyltransferases function.; DISEASE: Congenital disorder of glycosylation 2F (CDG2F) [MIM:603585]: CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:15576474}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.53767 . 0.12689526 63.00424628 165.54342 2.81406 SLC35A2 0.780526258513 0.212440039243914 0.0070337022430861 solute carrier family 35 member A2 FUNCTION: Transports nucleotide sugars from the cytosol into Golgi vesicles where glycosyltransferases function.; DISEASE: Congenital disorder of glycosylation 2M (CDG2M) [MIM:300896]: A disorder characterized by developmental delay, hypotonia, ocular anomalies, and brain malformations. Othere more variable clinical features included seizures, hypsarrhythmia, poor feeding, microcephaly, recurrent infections, dysmorphic features, shortened limbs, and coagulation defects. Congenital disorders of glycosylation are caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins and a wide variety of clinical features. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:23561849, ECO:0000269|PubMed:24115232}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;skin;skeletal muscle;bone marrow;uterus;pancreas;prostate;whole body;lung;mesenchyma;bone;thyroid;placenta;pituitary gland;liver;testis;spleen;kidney;brain;stomach; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22224 0.42220 -0.161524709 41.6430762 29.23115 0.93520 SLC35A3 0.0693153753308512 0.917233726327965 0.0134508983411835 solute carrier family 35 member A3 FUNCTION: Uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) transporter in the Golgi apparatus. May supply UDP-GlcNAc as substrate for Golgi-resident glycosyltransferases that generate branching of diantennary oligosaccharides. {ECO:0000269|PubMed:10393322}.; DISEASE: Arthrogryposis, mental retardation, and seizures (AMRS) [MIM:615553]: A disease characterized by arthrogryposis, mental retardation, autism spectrum disorder, and epilepsy. Additional features include limb malformations, distal joint involvement, microcephaly, retromicrognathia, and general muscle hypotonia. {ECO:0000269|PubMed:24031089}. Note=The disease is caused by mutations affecting the gene represented in this entry. In Golgi vesicles isolated from patient fibroblasts the transport of the respective nucleotide sugar is significantly reduced causing a massive decrease in the content of cell surface expressed highly branched N-glycans and a concomitant sharp increase of lower branched glycoforms.; . . . 0.29548 0.10732 -0.029247611 51.40363293 343.62286 3.92983 SLC35A4 0.000744268610339096 0.526410298221854 0.472845433167807 solute carrier family 35 member A4 . . . medulla oblongata;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;synovium;larynx;thyroid;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;tongue;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;placenta;visual apparatus;hippocampus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; kidney; 0.26919 0.10315 0.373041938 75.29488087 253.34047 3.42472 SLC35A5 0.00141225113499444 0.869198369685338 0.129389379179668 solute carrier family 35 member A5 . . . ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;adrenal cortex;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;cervix;kidney;thymus; amygdala;medulla oblongata;occipital lobe;caudate nucleus; 0.08083 . 0.507139401 80.10143902 283.10052 3.60274 SLC35B1 0.0132862685940911 0.954566200354734 0.0321475310511751 solute carrier family 35 member B1 FUNCTION: Probable sugar transporter. {ECO:0000250}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; liver;atrioventricular node; 0.15831 0.07412 -0.159704656 41.90846898 478.9805 4.51846 SLC35B2 0.700038249852824 0.299186479216767 0.000775270930409606 solute carrier family 35 member B2 FUNCTION: Mediates the transport of adenosine 3'-phospho 5'- phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi. May indirectly participate in activation of the NF- kappa-B and MAPK pathways. {ECO:0000269|PubMed:12716889}.; . TISSUE SPECIFICITY: Highly expressed in the placenta, pancreas, mammary gland and skeletal muscle. Weakly or not expressed in colon, heart and prostate. {ECO:0000269|PubMed:12716889}.; medulla oblongata;smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;synovium;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;cervix;kidney;mammary gland;stomach; . 0.24452 . -0.822919685 11.76574664 116.16721 2.34420 SLC35B3 0.00056646400612064 0.895047694111609 0.10438584188227 solute carrier family 35 member B3 FUNCTION: Mediates the transport of adenosine 3'-phospho 5'- phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi. Compensates for the insufficient expression of SLC35B2/PAPST1 during the synthesis of sulfated glycoconjugates in the colon. {ECO:0000269|PubMed:16492677}.; . TISSUE SPECIFICITY: Preferentially and highly expressed in colon. {ECO:0000269|PubMed:16492677}.; ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;urinary;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;kidney; dorsal root ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.18260 0.11088 -0.203796826 38.81811748 95.92066 2.11565 SLC35B4 4.5384262452846e-06 0.627502999980488 0.372492461593267 solute carrier family 35 member B4 FUNCTION: Sugar transporter that specifically mediates the transport of UDP-xylose (UDP-Xyl) and UDP-N-acetylglucosamine (UDP-GlcNAc) from cytosol into Golgi. {ECO:0000269|PubMed:15911612}.; . . . . 0.32511 0.10554 -0.249709319 35.74545883 26.48192 0.85714 SLC35C1 0.147014851687706 0.778197364293606 0.0747877840186882 solute carrier family 35 member C1 FUNCTION: Involved in GDP-fucose import from the cytoplasm into the Golgi lumen.; DISEASE: Congenital disorder of glycosylation 2C (CDG2C) [MIM:266265]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. The clinical features of CDG2C include mental retardation, short stature, facial stigmata, and recurrent bacterial peripheral infections with persistently elevated peripheral leukocytes. Biochemically, CDG2C is characterized by a lack of fucosylated glycoconjugates, including selectin ligands. {ECO:0000269|PubMed:11326279, ECO:0000269|PubMed:11326280}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;endometrium;thyroid;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.12888 0.12049 -0.005381972 53.50908233 775.2526 5.51199 SLC35C2 0.0471490104786645 0.928738946680657 0.0241120428406781 solute carrier family 35 member C2 FUNCTION: May play an important role in the cellular response to tissue hypoxia. May be either a GDP-fucose transporter that competes with SLC35C1 for GDP-fucose, or a factor that otherwise enhances the fucosylation of Notch and is required for optimal Notch signaling in mammalian cells. {ECO:0000269|PubMed:20837470}.; . TISSUE SPECIFICITY: Ubiquitously expressed although the level of expression is tissue dependent. Overexpressed in ovarian cancer.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion; 0.11769 0.09858 -0.624497208 17.16206653 37.9223 1.12635 SLC35D1 0.001854200528779 0.974733984458011 0.0234118150132107 solute carrier family 35 member D1 FUNCTION: Transports both UDP-glucuronic acid (UDP-GlcA) and UDP- N-acetylgalactosamine (UDP-GalNAc) from the cytoplasm to into the endoplasmic reticulum lumen. May participate in glucuronidation and/or chondroitin sulfate biosynthesis.; . TISSUE SPECIFICITY: Ubiquitous.; unclassifiable (Anatomical System);prostate;islets of Langerhans;testis;colon;skeletal muscle; superior cervical ganglion;fetal liver;liver;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.35778 . -0.271755481 34.31823543 1002.57888 6.09902 SLC35D2 9.13442164129427e-05 0.787493761126268 0.212414894657319 solute carrier family 35 member D2 FUNCTION: Antiporter transporting nucleotide sugars such as UDP-N- acetylglucosamine (UDP-GlcNAc), UDP-glucose (UDP-Glc) and GDP- mannose (GDP-Man) pooled in the cytosol into the lumen of the Golgi in exchange for the corresponding nucleosides monophosphates (UMP for UDP-sugars and GMP for GDP-sugars). May take part in heparan sulfate synthesis by supplying UDP-Glc-NAc, the donor substrate, and thus be involved in growth factor signaling. {ECO:0000269|PubMed:15082721, ECO:0000269|PubMed:15607426}.; . TISSUE SPECIFICITY: Highly expressed in heart, kidney, small intestine, placenta, lung and peripheral blood leukocyte. Weakly expressed in skeletal muscle and spleen. Not expressed in brain, colon and thymus. {ECO:0000269|PubMed:15607426}.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;optic nerve;whole body;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;lens;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;cervix;mammary gland;stomach; superior cervical ganglion;thyroid;atrioventricular node; 0.21292 0.12235 -0.271755481 34.31823543 152.53081 2.70094 SLC35D3 0.149614410820931 0.777594122358545 0.0727914668205237 solute carrier family 35 member D3 FUNCTION: May play a role in hemostasis as a regulator of the biosynthesis of platelet-dense granules. {ECO:0000250}.; . . . . 0.39440 0.11434 0.395088462 76.15003539 92.80348 2.06963 SLC35E1 0.0968428302685581 0.86727519537915 0.0358819743522922 solute carrier family 35 member E1 FUNCTION: Putative transporter. {ECO:0000250}.; . . . . 0.16454 0.12378 -0.626318434 17.03231894 19.99653 0.68140 SLC35E1P1 . . . solute carrier family 35 member E1 pseudogene 1 . . . . . . . . . . . SLC35E2 0.374305907762633 0.578735512347599 0.0469585798897679 solute carrier family 35 member E2 FUNCTION: Putative transporter. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;hypothalamus;colon;blood;parathyroid;skeletal muscle;skin;uterus;lung;epididymis;placenta;testis;germinal center;brain;thymus; superior cervical ganglion; 0.08723 . . . 124.71343 2.42805 SLC35E2B 0.62100245921917 0.346777066305704 0.0322204744751262 solute carrier family 35 member E2B FUNCTION: Putative transporter. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;muscle;colon;blood;choroid;lens;skin;skeletal muscle;uterus;lung;endometrium;synovium;thyroid;placenta;testis;germinal center;kidney;brain;stomach;thymus; . . . -0.163345027 41.24793583 75.97654 1.82658 SLC35E3 0.00040677888074501 0.851060088016556 0.148533133102699 solute carrier family 35 member E3 FUNCTION: Putative transporter. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;adrenal cortex;colon;blood;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;breast;uterus;optic nerve;lung;endometrium;bone;thyroid;macula lutea;liver;testis;spleen;germinal center;bladder; superior cervical ganglion;parietal lobe; 0.09852 0.10248 -0.227663163 37.11370606 96.00106 2.11709 SLC35E4 0.032252529013455 0.817223329210199 0.150524141776346 solute carrier family 35 member E4 FUNCTION: Putative transporter. {ECO:0000250}.; . . umbilical cord;ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;prostate;optic nerve;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;tongue;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;hippocampus;liver;head and neck;kidney;stomach; kidney; 0.13329 . -0.179930907 40.35739561 112.82301 2.31080 SLC35F1 0.388506270158181 0.61107272580447 0.000421004037348172 solute carrier family 35 member F1 FUNCTION: Putative solute transporter. {ECO:0000305}.; . . unclassifiable (Anatomical System);meninges;medulla oblongata;heart;developmental;adrenal cortex;colon;fovea centralis;skeletal muscle;skin;uterus;pia mater;lung;cochlea;macula lutea;visual apparatus;hypopharynx;testis;head and neck;dura mater;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.29195 0.10809 0.060756528 58.52795471 23.09728 0.77064 SLC35F2 0.00952167661780261 0.940458103097241 0.0500202202849568 solute carrier family 35 member F2 FUNCTION: Putative solute transporter. {ECO:0000305}.; . . ovary;colon;skin;uterus;cochlea;thyroid;bone;testis;brain;bladder;artery;unclassifiable (Anatomical System);cartilage;tongue;muscle;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;amnion;head and neck;cervix;mammary gland;stomach;aorta; superior cervical ganglion;atrioventricular node; 0.19258 0.10487 0.21689899 68.12927577 86.17975 1.98253 SLC35F3 0.894523108035515 0.105433914175523 4.29777889615796e-05 solute carrier family 35 member F3 FUNCTION: May be a thiamine transporter. {ECO:0000303|PubMed:24509276}.; . . . . 0.14881 0.07846 -0.624497208 17.16206653 73.04224 1.78451 SLC35F4 0.00969257412732057 0.941426288015118 0.0488811378575617 solute carrier family 35 member F4 FUNCTION: Putative solute transporter. {ECO:0000305}.; . . unclassifiable (Anatomical System);brain; . 0.33916 0.10691 . . 54.27773 1.47155 SLC35F5 0.00121571774591936 0.996927947757624 0.00185633449645624 solute carrier family 35 member F5 FUNCTION: Putative solute transporter. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in colorectal cancer cells. {ECO:0000269|PubMed:16477629}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;testis;dura mater;germinal center;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;placenta;liver;spleen;cervix;kidney;mammary gland; superior cervical ganglion;adrenal cortex;trigeminal ganglion;skeletal muscle; 0.26269 0.09982 0.062575634 58.74026893 105.3262 2.22212 SLC35F6 0.0161307579092324 0.884106470194913 0.0997627718958546 solute carrier family 35 member F6 FUNCTION: Involved in the maintenance of mitochondrial membrane potential in pancreatic ductal adenocarcinoma (PDAC) cells. Promotes pancreatic ductal adenocarcinoma (PDAC) cell growth. May play a role as a nucleotide-sugar transporter. {ECO:0000269|PubMed:19154410}.; . TISSUE SPECIFICITY: Expressed in pancreatic ductal adenocarcinoma (PDAC) (at protein level). Strongly expressed in prostate and thyroid. Weakly expressed in lung, heart, liver and kidney. {ECO:0000269|PubMed:19154410}.; . . 0.16775 0.11925 -0.337894035 30.37272942 79.93073 1.89062 SLC35G1 0.917135938028142 0.0823099793043596 0.000554082667498091 solute carrier family 35 member G1 FUNCTION: May play a role in intracellular calcium sensing and homeostasis. May act as a negative regulator of plasma membrane calcium-transporting ATPases preventing calcium efflux from the cell. {ECO:0000269|PubMed:22084111}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:22084111}.; . . 0.01460 0.03045 -0.427900189 25.14744043 29.75565 0.94872 SLC35G2 0.0663953363472009 0.87122310943502 0.0623815542177795 solute carrier family 35 member G2 FUNCTION: May play a role in cell proliferation. {ECO:0000305|PubMed:19148500}.; . . . . 0.13413 0.10430 -0.224023033 37.4321774 88.22886 2.01208 SLC35G3 0.0290347473412826 0.803165861278939 0.167799391379779 solute carrier family 35 member G3 . . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:17101974}.; prostate; . 0.15662 . -0.246069119 36.06982779 590.71721 4.92674 SLC35G4 . . . solute carrier family 35 member G4 . . . . . . 0.10361 . . . . SLC35G5 0.0274846347511103 0.795276011268545 0.177239353980345 solute carrier family 35 member G5 . . TISSUE SPECIFICITY: Expressed in placenta and testis. {ECO:0000269|PubMed:17101974}.; . . . 0.10361 1.35769336 94.43854683 4832.54727 14.10511 SLC35G6 0.000990014878643027 0.588000303614451 0.411009681506906 solute carrier family 35 member G6 . . TISSUE SPECIFICITY: Expressed in placenta and testis. {ECO:0000269|PubMed:17101974}.; . . . 0.10361 1.039913547 91.25973107 1370.30718 6.94508 SLC36A1 0.0234724316059047 0.973513461950046 0.00301410644404907 solute carrier family 36 member 1 FUNCTION: Neutral amino acid/proton symporter. Has a pH-dependent electrogenic transport activity for small amino acids such as glycine, alanine and proline. Besides small apolar L-amino acids, it also recognize their D-enantiomers and selected amino acid derivatives such as gamma-aminobutyric acid (By similarity). {ECO:0000250, ECO:0000269|PubMed:12809675}.; . . lymphoreticular;ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;blood;lens;skeletal muscle;pancreas;lung;placenta;liver;spleen;head and neck;cervix;kidney;stomach;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.13898 0.14921 -0.620857637 17.3566879 66.87625 1.68879 SLC36A2 1.41130186369675e-06 0.615409449454377 0.384589139243759 solute carrier family 36 member 2 FUNCTION: Involved in a pH-dependent electrogenic neuronal transport and sequestration of small amino acids. Transports glycine and proline. Inhibited by sarcosine (By similarity). {ECO:0000250, ECO:0000269|PubMed:19033659}.; DISEASE: Iminoglycinuria (IG) [MIM:242600]: A disorder of renal tubular reabsorption of glycine and imino acids (proline and hydroxyproline), marked by excessive levels of all three substances in the urine. {ECO:0000269|PubMed:19033659}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. Mutations in SLC36A2 that retain residual transport activity result in the IG phenotype only when combined with haploinsufficiency of the imino acid transporter SLC6A20 or deficiency of the neutral amino acid transporter SLC6A19. Additional polymorphisms and mutations in SLC6A18 can contribute to iminoglycinuria in some families.; TISSUE SPECIFICITY: Abundantly expressed in kidney and muscle. Expressed in the S1 segment of the proximal tubule close to the glomerulus. {ECO:0000269|PubMed:15058382, ECO:0000269|PubMed:19033659}.; unclassifiable (Anatomical System);kidney; . 0.10257 0.09701 0.047806932 57.51946214 600.50579 4.96001 SLC36A3 1.18609331200363e-06 0.577388244215789 0.422610569690898 solute carrier family 36 member 3 . . TISSUE SPECIFICITY: Specifically expressed in testis. {ECO:0000269|PubMed:15058382}.; lung;testis; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12334 0.09977 0.290313621 71.56758669 811.88208 5.60381 SLC36A4 2.69891717644805e-09 0.152167793039048 0.847832204262035 solute carrier family 36 member 4 FUNCTION: Functions as a sodium-independent electroneutral transporter for tryptophan, proline and alanine. Inhibited by sarcosine. {ECO:0000269|PubMed:21097500}.; . . unclassifiable (Anatomical System);heart;hypothalamus;colon;blood;skin;skeletal muscle;bone marrow;uterus;pancreas;prostate;whole body;lung;trabecular meshwork;placenta;visual apparatus;testis;cervix;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.24966 . 0.132352165 63.48785091 199.13086 3.05001 SLC37A1 0.028612841735564 0.971294807159054 9.23511053817059e-05 solute carrier family 37 member 1 . . TISSUE SPECIFICITY: Expressed in numerous tissues, with highest expression in kidney, bone marrow, spleen, liver, small intestine, as well as in fetal brain, liver and spleen.; ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;optic nerve;whole body;endometrium;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.09886 0.13560 -0.707227564 14.71455532 148.51546 2.65814 SLC37A2 5.00926399593573e-10 0.581719585357444 0.418280414141629 solute carrier family 37 member 2 . . . unclassifiable (Anatomical System);cartilage;lacrimal gland;colon;blood;skeletal muscle;skin;uterus;pancreas;lung;adrenal gland;nasopharynx;placenta;bone;liver;testis;cervix;kidney;brain;mammary gland; superior cervical ganglion;ciliary ganglion; 0.10703 0.11611 0.04598748 57.47817882 1459.43023 7.12342 SLC37A3 7.1633846502858e-08 0.886666473042347 0.113333455323807 solute carrier family 37 member 3 . . . ovary;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;synovium;larynx;bone;thyroid;testis;brain;artery;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion; 0.15291 0.11718 -0.354480518 29.42911064 2947.88909 10.29348 SLC37A4 0.000674732363421853 0.913893407618289 0.0854318600182897 solute carrier family 37 member 4 FUNCTION: Transports glucose-6-phosphate from the cytoplasm to the lumen of the endoplasmic reticulum. Forms with glucose-6- phosphatase the complex responsible for glucose production through glycogenolysis and gluconeogenesis. Hence, it plays a central role in homeostatic regulation of blood glucose levels. {ECO:0000269|PubMed:10026167}.; DISEASE: Glycogen storage disease 1C (GSD1C) [MIM:232240]: A metabolic disorder characterized by impairment of terminal steps of glycogenolysis and gluconeogenesis. Patients manifest a wide range of clinical symptoms and biochemical abnormalities, including hypoglycemia, severe hepatomegaly due to excessive accumulation of glycogen, kidney enlargement, growth retardation, lactic acidemia, hyperlipidemia, and hyperuricemia. {ECO:0000269|PubMed:10482962, ECO:0000269|PubMed:9758626}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Glycogen storage disease 1D (GSD1D) [MIM:232240]: A metabolic disorder characterized by impairment of terminal steps of glycogenolysis and gluconeogenesis. Patients manifest a wide range of clinical symptoms and biochemical abnormalities, including hypoglycemia, severe hepatomegaly due to excessive accumulation of glycogen, kidney enlargement, growth retardation, lactic acidemia, hyperlipidemia, and hyperuricemia. {ECO:0000269|PubMed:9758626}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Mostly expressed in liver and kidney.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;cartilage;islets of Langerhans;urinary;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;liver;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21468 0.32483 . . 122.19142 2.40713 SLC38A1 0.975432122735683 0.0245667851559803 1.09210833676967e-06 solute carrier family 38 member 1 FUNCTION: Functions as a sodium-dependent amino acid transporter. Mediates the saturable, pH-sensitive and electrogenic cotransport of glutamine and sodium ions with a stoichiometry of 1:1. May also transport small zwitterionic and aliphatic amino acids with a lower affinity. May supply glutamatergic and GABAergic neurons with glutamine which is required for the synthesis of the neurotransmitters glutamate and GABA. {ECO:0000269|PubMed:10891391}.; . TISSUE SPECIFICITY: Expressed in the cerebral cortex by pyramidal and GABAergic neurons, astrocytes and other non-neuronal cells (at protein level). Expressed in placenta, heart, lung, skeletal muscle, spleen, stomach and testis. {ECO:0000269|PubMed:10891391, ECO:0000269|PubMed:12388062, ECO:0000269|PubMed:15054072, ECO:0000269|PubMed:16148032}.; . . 0.56904 0.14839 -0.380166007 27.88393489 12.16348 0.44014 SLC38A2 0.969356999809796 0.030641112657639 1.88753256484627e-06 solute carrier family 38 member 2 FUNCTION: Functions as a sodium-dependent amino acid transporter. Mediates the saturable, pH-sensitive and electrogenic cotransport of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood- brain barrier and in the supply of maternal nutrients to the fetus through the placenta. {ECO:0000269|PubMed:10930503, ECO:0000269|PubMed:15922329}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Widely expressed in the central nervous system with higher concentrations in caudal regions. Expressed by glutamatergic and GABAergic neurons together with astrocytes and other non-neuronal cells in the cerebral cortex (at protein level). {ECO:0000269|PubMed:10930503, ECO:0000269|PubMed:15561425, ECO:0000269|PubMed:16616430}.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;bone;testis;dura mater;spinal ganglion;artery;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;pia mater;adrenal gland;placenta;head and neck;kidney;stomach;aorta;thymus; . 0.52310 0.12079 0.130533008 63.35810333 54.54237 1.47748 SLC38A3 . . . solute carrier family 38 member 3 FUNCTION: Sodium-dependent amino acid/proton antiporter. Mediates electrogenic cotransport of glutamine and sodium ions in exchange for protons. Also recognizes histidine, asparagine and alanine. May mediate amino acid transport in either direction under physiological conditions. May play a role in nitrogen metabolism and synaptic transmission. {ECO:0000250|UniProtKB:Q9JHZ9, ECO:0000269|PubMed:10823827}.; . . . . 0.69344 0.18236 . . . . SLC38A4 0.942982185779924 0.0570160107387309 1.80348134475406e-06 solute carrier family 38 member 4 FUNCTION: Sodium-dependent amino acid transporter. Mediates electrogenic symport of neutral amino acids and sodium ions. Has a broad specificity, with a preference for Ala, followed by His, Cys, Asn, Ser, Gly, Val, Thr, Gln and Met. May mediate sodium- independent transport of cationic amino acids, such as Arg and Lys. Amino acid uptake is pH-dependent, with low transport activities at pH 6.5, intermediate at pH 7.0 and highest between pH 7.5 and 8.5. {ECO:0000269|PubMed:11342143, ECO:0000269|PubMed:11414754}.; . TISSUE SPECIFICITY: Detected in embryonic and adult liver, and at lower levels in adult muscle, kidney and pancreas. Detected in placenta syncytiotrophoblasts throughout gestation. Detected in fetal blood vessels. {ECO:0000269|PubMed:11342143, ECO:0000269|PubMed:11414754, ECO:0000269|PubMed:16148032}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;parathyroid;skin;skeletal muscle;uterus;pancreas;placenta;liver;spleen;kidney;bladder; superior cervical ganglion;fetal liver;globus pallidus;trigeminal ganglion;skeletal muscle; 0.30584 0.16445 0.308721233 72.59966973 1358.76031 6.91878 SLC38A5 0.976708481576873 0.0232681936699681 2.33247531593349e-05 solute carrier family 38 member 5 FUNCTION: Functions as a sodium-dependent amino acid transporter which countertransport protons. Mediates the saturable, pH- sensitive, and electrogenic cotransport of several neutral amino acids including glycine, asparagine, alanine, serine, glutamine and histidine with sodium. {ECO:0000269|PubMed:11243884}.; . TISSUE SPECIFICITY: Predominantly expressed in stomach, brain, liver, lung and intestinal tract. {ECO:0000269|PubMed:11243884}.; unclassifiable (Anatomical System);tongue;colon;fovea centralis;choroid;lens;skeletal muscle;retina;breast;optic nerve;lung;bone;macula lutea;visual apparatus;head and neck;cervix;bladder; pancreas; 0.07584 0.24156 -0.359940251 28.93371078 343.94842 3.93203 SLC38A6 6.10703569830496e-16 0.00374028720186304 0.996259712798136 solute carrier family 38 member 6 FUNCTION: Probable sodium-dependent amino acid/proton antiporter, could be a neuronal transporter for glutamate. {ECO:0000250|UniProtKB:G3UVW3}.; . . unclassifiable (Anatomical System);lymph node;ovary;tongue;parathyroid;blood;skin;skeletal muscle;bone marrow;uterus;lung;endometrium;larynx;nasopharynx;bone;placenta;liver;testis;cervix;head and neck;spleen;kidney;brain; superior cervical ganglion; 0.05218 0.28659 -0.492218069 22.35786742 344.36981 3.93587 SLC38A7 0.0314056926915209 0.959136997318595 0.00945730998988408 solute carrier family 38 member 7 FUNCTION: Mediates sodium-dependent transport of amino acids, preferentially L-glutamine. {ECO:0000250}.; . . myocardium;medulla oblongata;ovary;skin;retina;uterus;prostate;endometrium;synovium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;islets of Langerhans;oral cavity;adrenal cortex;blood;skeletal muscle;pancreas;lung;mesenchyma;placenta;visual apparatus;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;parietal lobe; 0.12310 0.10668 -0.466531444 23.51380042 1607.42731 7.42076 SLC38A8 . . . solute carrier family 38 member 8 FUNCTION: Putative sodium-dependent amino acid/proton antiporter. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in fetal and adult brain, and spinal cord. In the brain, it is localized in the cell body and axon of the majority of neuronal cells and in a subset of glial cells. Found throughout the neuronal retina, with higher expression levels in the inner and outer plexiform layers and the photoreceptor layer. Very weak expression is also present in the kidneys, thymus, and testes. {ECO:0000269|PubMed:24290379}.; . . 0.11437 . -0.942503278 9.412597311 968.05359 6.01660 SLC38A9 0.755167399338962 0.24474634090786 8.62597531778011e-05 solute carrier family 38 member 9 FUNCTION: Lysosomal amino acid transporter involved in the activation of mTORC1 in response to amino acids. Probably acts as an amino acid sensor of the Rag GTPases and Ragulator complexes, 2 complexes involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids (PubMed:25561175, PubMed:25567906). Following activation by amino acids, the Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. SLC38A9 mediates transport of amino acids with low capacity and specificity with a slight preference for polar amino acids, suggesting that it acts as an amino acid sensor instead (PubMed:25561175, PubMed:25567906). The high concentration of arginine in lysosomes suggests that it acts as an arginine sensor (PubMed:25567906). {ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906}.; . . unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;parathyroid;skin;uterus;prostate;adrenal gland;bone;thyroid;liver;testis;germinal center;kidney;brain;stomach;thymus; dorsal root ganglion;subthalamic nucleus;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;placenta;globus pallidus;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.10564 . 0.130533008 63.35810333 73.48828 1.79189 SLC38A10 4.09242180982345e-08 0.98655460568366 0.0134453533921224 solute carrier family 38 member 10 FUNCTION: Putative sodium-dependent amino acid/proton antiporter. {ECO:0000250}.; . . lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;optic nerve;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;lens;breast;lung;placenta;macula lutea;hippocampus;liver;cervix;head and neck;kidney;mammary gland;thymus; thyroid;liver; 0.11386 0.09454 1.13164289 92.23873555 8935.42464 20.45812 SLC38A11 1.9255130084062e-06 0.445662354955709 0.554335719531282 solute carrier family 38 member 11 FUNCTION: Putative sodium-dependent amino acid/proton antiporter. {ECO:0000305}.; . . prostate;pancreas;iris;lens;brain;retina;bone marrow; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.11450 . 0.018483465 55.44939844 82.94201 1.93443 SLC39A1 0.167076829803909 0.77190317428794 0.0610199959081506 solute carrier family 39 member 1 FUNCTION: Mediates zinc uptake. May function as a major endogenous zinc uptake transporter in many cells of the body. Responsible for the rapid uptake and accumulation of physiologically effective zinc in prostate cells. {ECO:0000269|PubMed:12888280}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in most adult and fetal tissues including the epidermis. {ECO:0000269|PubMed:10610721}.; smooth muscle;ovary;skin;retina;prostate;endometrium;thyroid;amniotic fluid;bladder;brain;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;placenta; 0.49141 0.23123 -0.60427181 17.74593064 23.02696 0.76825 SLC39A2 0.000671706229021376 0.742827573452762 0.256500720318217 solute carrier family 39 member 2 FUNCTION: Mediates zinc uptake. Zinc uptake may be mediated by a Zn(2+)-HCO(3)(-) symport mechanism and can function in the presence of albumin. May also transport other divalent cations. May be important in contact inhibition of normal epithelial cells and loss of its expression may play a role in tumorigenesis.; . TISSUE SPECIFICITY: Expressed only in prostate and uterine epithelial cells.; unclassifiable (Anatomical System);uterus;prostate;optic nerve;heart;nasopharynx;placenta;skin; superior cervical ganglion;ciliary ganglion; 0.10427 0.09273 1.817129195 96.96862468 612.52871 5.00266 SLC39A3 0.0608464544153053 0.719722161670523 0.219431383914172 solute carrier family 39 member 3 FUNCTION: Acts as a zinc-influx transporter. {ECO:0000305}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.21587 0.11701 -0.023789244 52.09365416 78.45325 1.86940 SLC39A4 0.00573736084471825 0.971586524579433 0.0226761145758485 solute carrier family 39 member 4 FUNCTION: Plays an important role in cellular zinc homeostasis as a zinc transporter. Regulated in response to zinc availability (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in kidney, small intestine, stomach, colon, jejunum and duodenum. {ECO:0000269|PubMed:12032886, ECO:0000269|PubMed:12068297}.; unclassifiable (Anatomical System);myocardium;medulla oblongata;ovary;heart;colon;parathyroid;blood;choroid;skin;breast;uterus;pancreas;optic nerve;lung;placenta;liver;duodenum;spleen;kidney;mammary gland;stomach; trigeminal ganglion; 0.09914 0.12725 1.208829905 93.05260675 6782.66145 17.50995 SLC39A5 1.20741073816294e-07 0.564508656061796 0.43549122319713 solute carrier family 39 member 5 FUNCTION: May play a role in polarized cells by carrying out serosal-to-mucosal zinc transport. Plays a role in eye development. Could regulate the BMP/TGF-beta (bone morphogenetic protein/transforming growth factor-beta) signaling pathway and modulates extracellular matrix (ECM) proteins of the sclera (PubMed:24891338). Seems to play a central role in controlling organismal zinc status (By similarity). {ECO:0000250|UniProtKB:Q9D856, ECO:0000269|PubMed:24891338}.; DISEASE: Myopia 24, autosomal dominant (MYP24) [MIM:615946]: A refractive error of the eye, in which parallel rays from a distant object come to focus in front of the retina, vision being better for near objects than for far. {ECO:0000269|PubMed:24891338, ECO:0000269|PubMed:25525168}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in liver, kidney, pancreas, small intestine, colon, spleen, fetal liver and fetal kidney. {ECO:0000269|PubMed:15322118}.; ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;endometrium;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lens;pancreas;lung;placenta;visual apparatus;macula lutea;liver;spleen;kidney;stomach; trigeminal ganglion;cingulate cortex; 0.13096 . -0.372889896 28.20240623 281.62781 3.59460 SLC39A6 0.000761849565836676 0.995618333935148 0.00361981649901519 solute carrier family 39 member 6 FUNCTION: May act as a zinc-influx transporter. {ECO:0000269|PubMed:12839489}.; . TISSUE SPECIFICITY: Highly expressed in the breast, prostate, placenta, kidney, pituitary and corpus callosum. Weakly expressed in heart and intestine. Also highly expressed in cells derived from an adenocarcinoma of the cervix and lung carcinoma. {ECO:0000269|PubMed:12839489}.; smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;pituitary gland;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;bile duct;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;duodenum;hypopharynx;liver;spleen;head and neck;kidney;mammary gland; prostate;thalamus;superior cervical ganglion;fetal brain;hypothalamus;placenta; 0.27197 0.12346 -0.799052816 12.45576787 51.65351 1.41921 SLC39A7 0.0149907535503378 0.957756486890724 0.0272527595589385 solute carrier family 39 member 7 FUNCTION: Zinc transporter, that transports Zn(2+) from the endoplasmic reticulum/Golgi apparatus to the cytosol. Transport is stimulated by growth factors, such as EGF, and Ca(2+), as well as by exogenous Zn(2+). {ECO:0000269|PubMed:14525538, ECO:0000269|PubMed:15705588, ECO:0000269|PubMed:22317921}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14525538, ECO:0000269|PubMed:15705588}.; . . 0.21167 . 0.040529541 57.15380986 404.97509 4.21975 SLC39A8 0.891567478844834 0.108205187958135 0.000227333197031165 solute carrier family 39 member 8 FUNCTION: Acts as a zinc-influx transporter. {ECO:0000269|PubMed:12504855}.; . TISSUE SPECIFICITY: Expressed in thymus, placenta, lung, liver, pancreas and, to a lower extent, in spleen, testis, ovary, small intestine, colon, leukocyte, heart. Highest expression is observed in pancreas. {ECO:0000269|PubMed:12504855}.; smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;blood;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland; superior cervical ganglion;trachea;salivary gland;placenta;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.15315 0.12750 0.17280645 65.75843359 320.26955 3.80273 SLC39A9 0.529198523354405 0.467367700052898 0.00343377659269614 solute carrier family 39 member 9 FUNCTION: May act as a zinc-influx transporter. {ECO:0000250}.; . . smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;appendix;pons;atrioventricular node;trigeminal ganglion; 0.71618 0.11136 0.193034296 66.82000472 245.04465 3.37710 SLC39A10 0.997850639903884 0.00214929175568747 6.83404287068927e-08 solute carrier family 39 member 10 FUNCTION: May act as a zinc-influx transporter. {ECO:0000269|PubMed:17359283}.; . . skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;tongue;islets of Langerhans;hypothalamus;skeletal muscle;pancreas;lung;placenta;hippocampus;duodenum;head and neck;cervix;kidney;stomach; . 0.85518 0.11512 -0.156065314 42.16206653 205.76744 3.10004 SLC39A11 7.77832608077154e-05 0.756951717301565 0.242970499437628 solute carrier family 39 member 11 FUNCTION: Functions as a cellular zinc transporter. {ECO:0000250|UniProtKB:Q8BWY7}.; . . ovary;salivary gland;developmental;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; kidney;trigeminal ganglion; 0.18977 0.11192 0.643056625 84.05284265 1159.96741 6.48267 SLC39A12 0.000292985871332697 0.985773040025719 0.0139339741029488 solute carrier family 39 member 12 FUNCTION: Acts as a zinc-influx transporter (Potential). May be partly involved in the outbreak of schizophrenia. {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in brain and eye. {ECO:0000269|PubMed:12107410, ECO:0000269|PubMed:15342556}.; . . 0.26606 0.09205 0.714657953 85.81623024 1041.0355 6.19504 SLC39A12-AS1 . . . SLC39A12 antisense RNA 1 . . . . . . . . . . . SLC39A13 0.0118520311660311 0.950648206197405 0.0374997626365641 solute carrier family 39 member 13 FUNCTION: Acts as a zinc-influx transporter. {ECO:0000269|PubMed:21917916}.; DISEASE: Ehlers-Danlos syndrome-like spondylocheirodysplasia (SCD- EDS) [MIM:612350]: Spondylocheiro dysplastic form of Ehlers-Danlos syndrome. The syndrome consists of a generalized skeletal dysplasia involving mainly the spine (spondylo) and striking clinical abnormalities of the hands (cheiro) in addition to the EDS-like features. Clinical features included postnatal growth retardation, moderate short stature, protuberant eyes with bluish sclerae, hands with finely wrinkled palms, atrophy of the thenar muscles, and tapering fingers. Patients have thin, hyperelastic skin and hypermobile small joints consistent with an Ehlers- Danlos-like phenotype. Radiologic features included mild to moderate platyspondyly, mild to moderate osteopenia of the spine, small ileum, flat proximal femoral epiphyses, short, wide femoral necks, and broad metaphyses (elbows, knees, wrists, and interphalangeal joints). {ECO:0000269|PubMed:18513683}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;colon;skin;skeletal muscle;uterus;pancreas;whole body;lung;synovium;bone;thyroid;placenta;testis;spleen;kidney;spinal ganglion;brain;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.30846 0.12368 0.97558591 90.37508846 452.22355 4.42335 SLC39A14 0.314629295810412 0.681694417055914 0.00367628713367404 solute carrier family 39 member 14 FUNCTION: May mediate cellular uptake of nontransferrin-bound iron (By similarity). Broad-scope metal ion transporter with a preference for zinc uptake. {ECO:0000250, ECO:0000269|PubMed:15642354}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with increased expression in liver, pancreas, fetal liver, thyroid gland, left and right ventricle, right atrium and fetal heart. Weakly expressed in spleen, thymus, and peripheral blood leukocytes. {ECO:0000269|PubMed:15642354, ECO:0000269|PubMed:7584044}.; myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;nervous;adrenal cortex;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;cerebral cortex;bone;testis;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;pancreas;lung;adrenal gland;placenta;hippocampus;hypopharynx;duodenum;head and neck;kidney;stomach; pancreas;fetal liver;smooth muscle;adrenal gland;thyroid;beta cell islets;liver;fetal lung;ciliary ganglion; 0.14630 0.15311 -0.424258538 25.56027365 3348.38456 11.08339 SLC40A1 0.977595134539298 0.0224039957082132 8.69752489113487e-07 solute carrier family 40 member 1 FUNCTION: May be involved in iron export from duodenal epithelial cell and also in transfer of iron between maternal and fetal circulation. Mediates iron efflux in the presence of a ferroxidase (hephaestin and/or ceruloplasmin).; . TISSUE SPECIFICITY: Detected in erythrocytes (at protein level). Expressed in placenta, intestine, muscle and spleen. {ECO:0000269|PubMed:10747949, ECO:0000269|PubMed:23219802}.; smooth muscle;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;placenta; 0.29792 0.25834 0.328949044 73.41354093 151.17274 2.68772 SLC41A1 0.705784064695467 0.294067276605469 0.000148658699063942 solute carrier family 41 member 1 FUNCTION: Acts as a magnesium transporter that is responsive to magnesium balance. {ECO:0000269|PubMed:15713785}.; . TISSUE SPECIFICITY: Highest expression levels in heart and testis, slightly less in skeletal muscles, prostate, adrenal gland and thyroid, and weakest in the hematopoietic tissues bones marrow, lymph node, thymus and spleen. {ECO:0000269|PubMed:12810078}.; . . 0.42544 0.11809 -0.979072682 8.752064166 30.24424 0.96449 SLC41A2 0.913051821488741 0.0869221040615293 2.6074449730146e-05 solute carrier family 41 member 2 FUNCTION: Acts as a plasma-membrane magnesium transporter. {ECO:0000269|PubMed:16984228}.; . . unclassifiable (Anatomical System);ovary;cartilage;blood;parathyroid;breast;frontal lobe;placenta;thyroid;kidney;artery;aorta;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13386 0.10914 -0.161524709 41.6430762 104.25786 2.20696 SLC41A3 0.000139670421791452 0.961837953678831 0.038022375899378 solute carrier family 41 member 3 . . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;testis;trigeminal ganglion;skeletal muscle;cingulate cortex;cerebellum; 0.07523 0.08624 0.290313621 71.56758669 1540.42882 7.28437 SLC43A1 7.85327016141061e-05 0.981449311902694 0.0184721553956918 solute carrier family 43 member 1 FUNCTION: Sodium-independent, high affinity transport of large neutral amino acids. Has narrower substrate selectivity compared to SLC7A5 and SLC7A8 and mainly transports branched-chain amino acids and phenylalanine. Plays a role in the development of human prostate cancer, from prostatic intraepithelial neoplasia to invasive prostate cancer. {ECO:0000269|PubMed:11956097, ECO:0000269|PubMed:12930836, ECO:0000269|PubMed:9255310, ECO:0000269|PubMed:9722952}.; . TISSUE SPECIFICITY: In adults, found in all tissues examined with highest expression in pancreas. In fetus, highest expression in liver and lower levels in kidney, and lung. High levels found in prostate cancer cells. {ECO:0000269|PubMed:11956097, ECO:0000269|PubMed:12930836, ECO:0000269|PubMed:9255310, ECO:0000269|PubMed:9722952}.; colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;endometrium;thyroid;testis;germinal center;brain;gall bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;lens;skeletal muscle;breast;lung;macula lutea;visual apparatus;liver;spleen;kidney;stomach; fetal liver;superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13169 0.11572 -0.064242613 48.844067 126.38024 2.44868 SLC43A2 0.0618427043068134 0.934799589244398 0.00335770644878842 solute carrier family 43 member 2 FUNCTION: Sodium-, chloride-, and pH-independent high affinity transport of large neutral amino acids. {ECO:0000269|PubMed:15659399}.; . TISSUE SPECIFICITY: Detected in several tissues with higher expression in placenta, kidney and peripheral blood leukocytes. In the kidney, is detected in epithelial cells of the distal tubule and collecting duct. In the intestine, is expressed mainly in crypt cells of the intestinal microvilli and epithelial cells in the base of the villus. {ECO:0000269|PubMed:15659399}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;liver;duodenum;spleen;kidney;mammary gland;stomach; . 0.31654 0.12547 -0.975433863 8.852323661 57.99689 1.54002 SLC43A3 0.000317449115823233 0.987219625575991 0.0124629253081861 solute carrier family 43 member 3 FUNCTION: Putative transporter. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in macrophages. {ECO:0000269|Ref.1}.; lymphoreticular;smooth muscle;ovary;salivary gland;sympathetic chain;developmental;intestine;colon;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.09751 0.09706 -0.510624372 21.65015334 112.24746 2.30476 SLC44A1 0.999253571367297 0.000746427582924076 1.04977921638265e-09 solute carrier family 44 member 1 FUNCTION: Choline transporter. May be involved in membrane synthesis and myelin production. {ECO:0000269|PubMed:19357133}.; . TISSUE SPECIFICITY: Expressed in various cells of the hematopoietic system. {ECO:0000269|PubMed:11698453}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;optic nerve;frontal lobe;cochlea;endometrium;larynx;germinal center;brain;unclassifiable (Anatomical System);cartilage;nervous;pineal body;spinal cord;lens;pancreas;lung;placenta;macula lutea;liver;cervix;head and neck;kidney;stomach; amygdala;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;ciliary ganglion;cingulate cortex;parietal lobe; 0.23370 0.13691 -0.534490515 20.70063694 1596.58474 7.39509 SLC44A2 0.0414645881648824 0.958482923849202 5.24879859155233e-05 solute carrier family 44 member 2 FUNCTION: Isoform 1, but not isoform 3, exhibits some choline transporter activity. {ECO:0000269|PubMed:10677542, ECO:0000269|PubMed:20665236}.; . TISSUE SPECIFICITY: Present in supporting cells of the inner ear (at protein level). Only isoform 3 is expressed in inner ear vestibular tissue. {ECO:0000269|PubMed:14973250, ECO:0000269|PubMed:20665236}.; medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;lung;mesenchyma;placenta;amnion;head and neck;kidney;stomach; placenta;testis; 0.25892 0.11307 -0.929520514 9.683887709 125.32453 2.43660 SLC44A3 1.8199523853244e-24 1.29370163424222e-05 0.999987062983658 solute carrier family 44 member 3 . . . unclassifiable (Anatomical System);smooth muscle;heart;colon;skin;retina;breast;uterus;pancreas;prostate;whole body;lung;placenta;hippocampus;liver;testis;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10119 0.09355 -0.020150552 52.25288983 122.98894 2.41486 SLC44A4 8.27829933247523e-08 0.995007734095666 0.00499218312134113 solute carrier family 44 member 4 . DISEASE: Note=An interstitial deletion causing the fusion of exon 10 of CTL4 with the 3'-UTR of NEU has been detected in two patients affected by sialidosis.; . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;skin;skeletal muscle;bile duct;breast;pancreas;prostate;lung;endometrium;nasopharynx;visual apparatus;liver;testis;brain;mammary gland;stomach; . 0.39411 . 1.091286379 91.89667374 602.64794 4.96906 SLC44A5 0.0342286898388776 0.965768427198239 2.88296288369716e-06 solute carrier family 44 member 5 . . . . . 0.17529 0.09662 -0.290161348 33.33923095 65.10631 1.66136 SLC45A1 0.0451892558909179 0.953691470430789 0.00111927367829283 solute carrier family 45 member 1 FUNCTION: Mediates glucose uptake along the pH gradient. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in adult heart, brain, muscle and kidney, with very strong expression in brain. Also expressed in fetal brain, kidney and lung.; unclassifiable (Anatomical System);ovary;blood;choroid;fovea centralis;lens;retina;breast;optic nerve;frontal lobe;macula lutea;iris;brain;stomach; pons;cingulate cortex;cerebellum; 0.30467 0.11558 -2.035711952 1.669025714 78.0534 1.86360 SLC45A2 7.85681140165749e-05 0.758913547297643 0.24100788458834 solute carrier family 45 member 2 FUNCTION: Melanocyte differentiation antigen. May transport substances required for melanin biosynthesis (By similarity). {ECO:0000250}.; DISEASE: Albinism, oculocutaneous, 4 (OCA4) [MIM:606574]: A disorder of pigmentation characterized by reduced biosynthesis of melanin in the skin, hair and eyes. Patients show reduced or lacking pigmentation associated with classic albinism ocular abnormalities, including decreased visual acuity, macular hypoplasia, optic dysplasia, atypical choroidal vessels, and nystagmus. {ECO:0000269|PubMed:11574907, ECO:0000269|PubMed:14722913, ECO:0000269|PubMed:14961451, ECO:0000269|PubMed:15656822, ECO:0000269|PubMed:17768386, ECO:0000269|PubMed:19865097, ECO:0000269|PubMed:23504663, ECO:0000269|PubMed:25703744}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in most melanoma cell lines and melanocytes.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;lung;cornea;endometrium;visual apparatus;liver;testis;kidney;brain;mammary gland; superior cervical ganglion;appendix;atrioventricular node;trigeminal ganglion; 0.10957 0.58549 -0.975433863 8.852323661 4323.78653 13.09053 SLC45A3 0.0368495348530263 0.928795438065903 0.034355027081071 solute carrier family 45 member 3 . . TISSUE SPECIFICITY: Prostate specific. Expressed in all prostatic glandular cells. Expressed both in normal and cancerous prostates. {ECO:0000269|PubMed:11245466, ECO:0000269|PubMed:14997204}.; . . 0.63010 0.13303 -0.532670911 20.78320359 408.81048 4.23857 SLC45A4 0.00458960961270734 0.988812046321908 0.00659834406538512 solute carrier family 45 member 4 . . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;cerebellum; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.25179 0.09355 -1.295313867 4.989384289 150.28485 2.67496 SLC46A1 0.104422521431544 0.8636978089277 0.0318796696407556 solute carrier family 46 member 1 FUNCTION: Has been shown to act both as an intestinal proton- coupled high-affinity folate transporter and as an intestinal heme transporter which mediates heme uptake from the gut lumen into duodenal epithelial cells. The iron is then released from heme and may be transported into the bloodstream. Dietary heme iron is an important nutritional source of iron. Shows a higher affinity for folate than heme. {ECO:0000269|PubMed:17129779, ECO:0000269|PubMed:17156779, ECO:0000269|PubMed:17446347, ECO:0000269|PubMed:17475902}.; . TISSUE SPECIFICITY: Expressed in kidney, liver, placenta, small intestine, spleen, retina and retinal pigment epithelium. Lower levels found in colon and testis. Very low levels in brain, lung, stomach, heart and muscle. In intestine, expressed in duodenum with lower levels in jejunum, ileum, cecum, rectum and segments of the colon. {ECO:0000269|PubMed:17129779, ECO:0000269|PubMed:17335806}.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;parathyroid;fovea centralis;skin;skeletal muscle;uterus;pancreas;prostate;lung;placenta;macula lutea;visual apparatus;testis;spleen;brain;stomach; . 0.16952 0.15558 . . 58.74473 1.55461 SLC46A2 0.000292933739775045 0.796924454427814 0.202782611832411 solute carrier family 46 member 2 FUNCTION: May act as a transporter. {ECO:0000250}.; . TISSUE SPECIFICITY: Strongly expressed in the adult thymus. Expressed in spleen, lymph nodes, thymus, PBL, bone marrow and fetal liver. {ECO:0000269|PubMed:10978518}.; . . 0.13462 0.10800 0.532823122 80.96249115 592.01442 4.93088 SLC46A3 1.30472037835528e-07 0.359311662332452 0.64068820719551 solute carrier family 46 member 3 . . . ovary;colon;parathyroid;skin;retina;whole body;endometrium;larynx;thyroid;pituitary gland;testis;germinal center;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;pineal body;adrenal cortex;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;prefrontal cortex;atrioventricular node;cingulate cortex; 0.15009 . -0.001743238 53.85114414 87.19669 1.99447 SLC47A1 1.21582234978014e-09 0.532794663363947 0.46720533542023 solute carrier family 47 member 1 FUNCTION: Solute transporter for tetraethylammonium (TEA), 1- methyl-4-phenylpyridinium (MPP), cimetidine, N-methylnicotinamide (NMN), metformin, creatinine, guanidine, procainamide, topotecan, estrone sulfate, acyclovir, ganciclovir and also the zwitterionic cephalosporin, cephalexin and cephradin. Seems to also play a role in the uptake of oxaliplatin (a new platinum anticancer agent). Able to transport paraquat (PQ or N,N-dimethyl-4-4'-bipiridinium); a widely used herbicid. Responsible for the secretion of cationic drugs across the brush border membranes. {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:16996621, ECO:0000269|PubMed:17495125, ECO:0000269|PubMed:17509534, ECO:0000269|PubMed:17582384}.; . TISSUE SPECIFICITY: Expressed in adrenal gland, and to a lower extent in liver, skeletal muscle and kidney (especially found in luminal membranes of the urinary tubules, bile caniculi and brush border membranes). {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17509534}.; unclassifiable (Anatomical System);medulla oblongata;heart;colon;skin;skeletal muscle;uterus;pancreas;prostate;frontal lobe;cerebral cortex;endometrium;adrenal gland;visual apparatus;iris;liver;testis;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;adrenal gland;adrenal cortex;liver;testis;ciliary ganglion;kidney;trigeminal ganglion; 0.06526 0.09018 -0.220384297 37.6032083 204.75709 3.09053 SLC47A1P1 . . . solute carrier family 47 member 1 pseudogene 1 . . . . . . . . . . . SLC47A2 9.01734392930179e-14 0.0363731504128361 0.963626849587074 solute carrier family 47 member 2 FUNCTION: Solute transporter for tetraethylammonium (TEA), 1- methyl-4-phenylpyridinium (MPP), cimetidine, N-methylnicotinamide, metformin, creatinine, guanidine, procainamide, topotecan, estrone sulfate, acyclovir, and ganciclovir. Responsible for the secretion of cationic drugs across the brush border membranes. {ECO:0000269|PubMed:16807400, ECO:0000269|PubMed:16996621, ECO:0000269|PubMed:17509534}.; . TISSUE SPECIFICITY: Isoform 3 is predominantly expressed in kidney. Isoform 6 is expressed in brain. {ECO:0000269|PubMed:16807400}.; unclassifiable (Anatomical System);optic nerve;salivary gland;macula lutea;colon;fovea centralis;choroid;kidney;lens;brain;skeletal muscle;stomach;retina; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.03353 0.08696 -0.843147538 11.2762444 77.28986 1.84624 SLC48A1 0.437511991431989 0.457729967633769 0.104758040934242 solute carrier family 48 member 1 FUNCTION: Heme transporter that regulates intracellular heme availability through the endosomal or lysosomal compartment. {ECO:0000269|PubMed:18418376}.; . TISSUE SPECIFICITY: Highly expressed in the brain, kidney, heart and skeletal muscle. Moderately expressed in the liver, lung, placenta and small intestine. {ECO:0000269|PubMed:18418376}.; . . . . . . 3.1238 0.11179 SLC50A1 0.130229792296048 0.847594144359599 0.0221760633443528 solute carrier family 50 member 1 FUNCTION: Mediates sugar transport across membranes. May stimulate V(D)J recombination by the activation of RAG1. {ECO:0000269|PubMed:21107422}.; . TISSUE SPECIFICITY: Ubiquitously expressed with highest expression in oviduct, epididymis and intestine. {ECO:0000269|PubMed:21107422}.; unclassifiable (Anatomical System);cartilage;ovary;lacrimal gland;islets of Langerhans;salivary gland;pharynx;colon;blood;breast;pancreas;prostate;lung;placenta;visual apparatus;liver;cervix;kidney;brain;mammary gland;bladder;stomach; . 0.12760 0.15530 -0.163345027 41.24793583 21.43142 0.72343 SLC51A 0.0575688115148571 0.938672190271376 0.00375899821376735 solute carrier family 51 alpha subunit FUNCTION: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood. Efficiently transports the major species of bile acids. {ECO:0000269|PubMed:16317684}.; . TISSUE SPECIFICITY: Widely expressed with a high expression in ileum. Expressed in testis, colon, liver, small intestine, kidney, ovary and adrenal gland; and at low levels in heart, lung, brain, pituitary, thyroid gland, uterus, prostate, mammary gland and fat. {ECO:0000269|PubMed:12719432, ECO:0000269|PubMed:16317684}.; . . . . -0.402212257 26.7338995 3423.40905 11.22827 SLC51B 0.222197461674156 0.647353045064962 0.130449493260882 solute carrier family 51 beta subunit FUNCTION: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood. Efficiently transports the major species of bile acids. Modulates SLC51A glycosylation, membrane trafficking and stability activities. {ECO:0000269|PubMed:16317684}.; . TISSUE SPECIFICITY: Widely expressed with a high expression in ileum. Expressed in testis, colon, liver, small intestine, kidney, ovary and adrenal gland; and at low levels in heart, lung, brain, pituitary, thyroid gland, uterus, prostate, mammary gland and fat. {ECO:0000269|PubMed:12719432, ECO:0000269|PubMed:16317684}.; . . . . . . 246.19765 3.38580 SLC52A1 2.74247658877072e-05 0.3235049394331 0.676467635801013 solute carrier family 52 member 1 FUNCTION: Riboflavin transporter. Riboflavin transport is Na(+)- independent but moderately pH-sensitive. Activity is strongly inhibited by riboflavin analogs, such as lumiflavin. Weakly inhibited by flavin adenine dinucleotide (FAD). In case of infection by retroviruses, acts as a cell receptor to retroviral envelopes similar to the porcine endogenous retrovirus (PERV-A). {ECO:0000269|PubMed:12740431, ECO:0000269|PubMed:20463145}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in the testis, placenta and small intestine. Expressed at lower level in other tissues. {ECO:0000269|PubMed:12740431, ECO:0000269|PubMed:18632736, ECO:0000269|PubMed:20463145}.; . . 0.11534 0.09201 0.310540264 72.65864591 3228.82877 10.82614 SLC52A2 0.0119600051418378 0.849111295786823 0.138928699071339 solute carrier family 52 member 2 FUNCTION: Riboflavin transporter. Riboflavin transport is Na(+)- independent but moderately pH-sensitive. Activity is strongly inhibited by riboflavin analogs, such as lumiflavin. Weakly inhibited by flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN). In case of infection by retroviruses, acts as a cell receptor to retroviral envelopes similar to the porcine endogenous retrovirus (PERV-A). {ECO:0000269|PubMed:12740431, ECO:0000269|PubMed:19307586, ECO:0000269|PubMed:20463145}.; . TISSUE SPECIFICITY: Highly expressed in brain, fetal brain and salivary gland. Weakly expressed in other tissues. {ECO:0000269|PubMed:12740431, ECO:0000269|PubMed:20463145}.; . . 0.15412 0.11459 -0.933156985 9.54824251 43.28673 1.24954 SLC52A3 0.00162509373291456 0.695105565153673 0.303269341113412 solute carrier family 52 member 3 FUNCTION: Transporter for riboflavin, which must be obtained as a nutrient via intestinal absorption. Riboflavin transport is Na(+)- independent at low pH but significantly reduced by Na(+) depletion under neutral pH conditions. Activity is strongly inhibited by riboflavin analogs, such as lumiflavin, flavin mononucleotide (FMN), flavin adenine dinucleotide (FAD), by methylene blue, and to a lesser extent by amiloride. {ECO:0000269|PubMed:20463145, ECO:0000269|PubMed:24264046}.; DISEASE: Fazio-Londe disease (FALOND) [MIM:211500]: A rare neurological disease characterized by progressive weakness of the muscles innervated by cranial nerves of the lower brain stem. It may present in childhood with severe neurological deterioration with hypotonia, respiratory insufficiency leading to premature death, or later in life with bulbar weakness which progresses to involve motor neurons throughout the neuroaxis. Clinical manifestations include dysarthria, dysphagia, facial weakness, tongue weakness, and fasciculations of the tongue and facial muscles. {ECO:0000269|PubMed:21110228}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Predominantly expressed in testis. Highly expressed in small intestine and prostate. {ECO:0000269|PubMed:20463145}.; . . 0.14821 0.10514 0.090079492 60.64519934 2301.46246 8.88032 SLCO1A2 5.58441209241734e-15 0.00714461152708437 0.99285538847291 solute carrier organic anion transporter family member 1A2 FUNCTION: Mediates the Na(+)-independent transport of organic anions such as sulfobromophthalein (BSP) and conjugated (taurocholate) and unconjugated (cholate) bile acids (By similarity). Selectively inhibited by the grapefruit juice component naringin. {ECO:0000250, ECO:0000269|PubMed:17301733}.; . . unclassifiable (Anatomical System);lung;spinal cord;liver;spleen;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;globus pallidus;pons;atrioventricular node;caudate nucleus;trigeminal ganglion;skeletal muscle;parietal lobe; 0.30946 0.08349 -0.33061537 30.82094834 726.90561 5.35526 SLCO1B1 3.45238778980654e-16 0.00989771578463161 0.990102284215368 solute carrier organic anion transporter family member 1B1 FUNCTION: Mediates the Na(+)-independent uptake of organic anions such as pravastatin, taurocholate, methotrexate, dehydroepiandrosterone sulfate, 17-beta-glucuronosyl estradiol, estrone sulfate, prostaglandin E2, thromboxane B2, leukotriene C3, leukotriene E4, thyroxine and triiodothyronine. Involved in the clearance of bile acids and organic anions from the liver. {ECO:0000269|PubMed:10358072, ECO:0000269|PubMed:10601278, ECO:0000269|PubMed:12196548, ECO:0000269|PubMed:22232210}.; . TISSUE SPECIFICITY: Highly expressed in liver, at the basolateral membranes of centrilobular hepatocytes. Not detected in heart, brain, placenta, lung, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocyte. {ECO:0000269|PubMed:10358072, ECO:0000269|PubMed:10601278, ECO:0000269|PubMed:22232210}.; liver;testis; fetal liver; 0.06199 0.19821 1.025142459 91.07100731 708.10764 5.28496 SLCO1B3 9.24108066211779e-17 0.00236920980217608 0.997630790197824 solute carrier organic anion transporter family member 1B3 FUNCTION: Mediates the Na(+)-independent uptake of organic anions such as 17-beta-glucuronosyl estradiol, taurocholate, triiodothyronine (T3), leukotriene C4, dehydroepiandrosterone sulfate (DHEAS), methotrexate and sulfobromophthalein (BSP). Involved in the clearance of bile acids and organic anions from the liver. {ECO:0000269|PubMed:22232210}.; DISEASE: Hyperbilirubinemia, Rotor type (HBLRR) [MIM:237450]: An autosomal recessive form of primary conjugated hyperbilirubinemia. Affected individuals develop mild jaundice not associated with hemolysis shortly after birth or in childhood. They have delayed plasma clearance of the unconjugated anionic dye bromsulphthalein and prominent urinary excretion of coproporphyrin I. Hepatic pigmentation is normal. {ECO:0000269|PubMed:22232210}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in liver, in particular at the basolateral membrane of hepatocytes near the central vein. Not detected in other tissues. Highly expressed in some cancer cell lines derived from colon, pancreas, liver and gall bladder.; lung;ovary;bone;liver;colon;spleen;stomach; subthalamic nucleus;superior cervical ganglion;fetal liver; 0.11856 0.15575 0.672386703 84.73696627 . . SLCO1B7 4.9248493708995e-17 0.0016353738564623 0.998364626143538 solute carrier organic anion transporter family member 1B7 (putative) . . . . . . . 1.714145866 96.4673272 1061.86953 6.25462 SLCO1C1 7.6167599235895e-06 0.97858772164575 0.0214046615943263 solute carrier organic anion transporter family member 1C1 FUNCTION: Mediates the Na(+)-independent high affinity transport of organic anions such as the thyroid hormones thyroxine (T4) and rT3. Other potential substrates, such as triiodothyronine (T3), 17-beta-glucuronosyl estradiol, estrone-3-sulfate and sulfobromophthalein (BSP) are transported with much lower efficiency. May play a signifiant role in regulating T4 flux into and out of the brain (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in brain and in Leydig cells in testis. Detected in many brain regions with the exception of pons and cerebellum. Not strongly enriched in cerebral microvessels. {ECO:0000269|PubMed:18687783}.; unclassifiable (Anatomical System);cochlea;cerebral cortex;sympathetic chain;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.68956 0.08904 7.61E-05 53.98089172 5691.39569 15.60542 SLCO2A1 2.25372891314708e-09 0.667044937620587 0.332955060125684 solute carrier organic anion transporter family member 2A1 FUNCTION: May mediate the release of newly synthesized prostaglandins from cells, the transepithelial transport of prostaglandins, and the clearance of prostaglandins from the circulation. Transports PGD2, as well as PGE1, PGE2 and PGF2A.; . TISSUE SPECIFICITY: Ubiquitous. Significant expression observed in ling, kidney, spleen, and heart. {ECO:0000269|PubMed:22331663}.; unclassifiable (Anatomical System);cartilage;ovary;heart;islets of Langerhans;colon;parathyroid;choroid;skin;skeletal muscle;uterus;pancreas;prostate;lung;endometrium;placenta;visual apparatus;hypopharynx;liver;testis;head and neck;spleen;kidney;brain;aorta; adrenal gland;placenta;ciliary ganglion; 0.13458 0.17634 0.270087468 70.69473933 1947.60289 8.12181 SLCO2B1 0.00335356336964323 0.996214751527985 0.000431685102371945 solute carrier organic anion transporter family member 2B1 FUNCTION: Mediates the Na(+)-independent transport of organic anions such as taurocholate, the prostaglandins PGD2, PGE1, PGE2, leukotriene C4, thromboxane B2 and iloprost. {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 has it's highest expression in brain, it is the major form expressed in duodenum, kidney, placenta, and skeletal muscle. Isoform 3 predominates in liver. {ECO:0000269|PubMed:23531488}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;spinal cord;adrenal cortex;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; subthalamic nucleus;superior cervical ganglion;placenta;liver;globus pallidus;ciliary ganglion; 0.12048 0.17779 -0.483123186 22.78249587 2109.9785 8.45565 SLCO3A1 0.732171682691697 0.267716118663014 0.00011219864528949 solute carrier organic anion transporter family member 3A1 FUNCTION: Mediates the Na(+)-independent transport of organic anions such as estrone-3-sulfate (PubMed:10873595). Mediates transport of prostaglandins (PG) E1 and E2, thyroxine (T4), deltorphin II, BQ-123 and vasopressin, but not DPDPE (a derivative of enkephalin lacking an N-terminal tyrosine residue), estrone-3- sulfate, taurocholate, digoxin nor DHEAS (PubMed:16971491). {ECO:0000269|PubMed:10873595, ECO:0000269|PubMed:16971491}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in spleen and leukocytes. Generally the expression of isoform 1 is higher than that of isoform 2. Isoform 2 is particularly abundant in testis and brain. In testis, isoform 1 is detected in spermatogonia at different stages and absent from Sertoli cells, while isoform 2 is present in both (at protein level). Expressed in the choroid plexus epithelium, isoform 1 being localized at the basolateral membrane and isoform 2 at the apical one, as well as in the subapical intracellular vesicular compartments. Differential expression of both isoforms is also observed in other brain region: isoform 1 is very abundant in the gray matter of the frontal cortex, but is not associated with neuronal cell bodies. Not detected in the white matter. In contrast, isoform 2 is associated with neuronal bodies and axons in both the gray and the white matters of the frontal cortex. {ECO:0000269|PubMed:16971491}.; lymphoreticular;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;lens;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;macula lutea;cervix;stomach; amygdala;medulla oblongata;superior cervical ganglion;testis - interstitial;occipital lobe;testis - seminiferous tubule;testis;cingulate cortex;parietal lobe; 0.17631 0.14648 -0.576764155 18.7839113 59.61119 1.56765 SLCO4A1 5.34100932440508e-07 0.857450695384008 0.14254877051506 solute carrier organic anion transporter family member 4A1 FUNCTION: Mediates the Na(+)-independent transport of organic anions such as the thyroid hormones T3 (triiodo-L-thyronine), T4 (thyroxine) and rT3, and of estrone-3-sulfate and taurocholate.; . TISSUE SPECIFICITY: Ubiquitous, with the exception of spleen and leukocytes.; myocardium;ovary;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;frontal lobe;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;blood;lens;skeletal muscle;lung;placenta;macula lutea;cervix;kidney;mammary gland;stomach;thymus; . 0.13199 0.14263 -1.320975027 4.777070064 1031.5178 6.17015 SLCO4A1-AS1 . . . SLCO4A1 antisense RNA 1 . . . . . . . . . . . SLCO4C1 1.37231076325155e-06 0.952495348699861 0.0475032789893758 solute carrier organic anion transporter family member 4C1 FUNCTION: Organic anion transporter, capable of transporting pharmacological substances such as digoxin, ouabain, thyroxine, methotrexate and cAMP. May participate in the regulation of membrane transport of ouabain. Involved in the uptake of the dipeptidyl peptidase-4 inhibitor sitagliptin and hence may play a role in its transport into and out of renal proximal tubule cells. May be involved in the first step of the transport pathway of digoxin and various compounds into the urine in the kidney. May be involved in sperm maturation by enabling directed movement of organic anions and compounds within or between cells. This ion- transporting process is important to maintain the strict epididymal homeostasis necessary for sperm maturation. May have a role in secretory functions since seminal vesicle epithelial cells are assumed to secrete proteins involved in decapacitation by modifying surface proteins to facilitate the acquisition of the ability to fertilize the egg. {ECO:0000250|UniProtKB:Q8BGD4, ECO:0000269|PubMed:14993604, ECO:0000269|PubMed:17314201}.; . TISSUE SPECIFICITY: Predominantly expressed in kidney but also weakly expressed in both fetal liver and kidney. {ECO:0000269|PubMed:14993604}.; unclassifiable (Anatomical System);lung;heart;islets of Langerhans;liver;spleen;blood;kidney;bone marrow; dorsal root ganglion;superior cervical ganglion;adrenal gland;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.27981 0.08377 -0.310388054 32.14791224 205.66106 3.09778 SLCO5A1 1.52377907757975e-05 0.962450751779592 0.0375340104296326 solute carrier organic anion transporter family member 5A1 . . . unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;brain; superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.44543 0.10196 0.516238257 80.33734371 3042.61323 10.48038 SLCO6A1 2.70904557113252e-06 0.918969416094382 0.0810278748600466 solute carrier organic anion transporter family member 6A1 . . TISSUE SPECIFICITY: Strongly expressed in testis. Weakly expressed in spleen, brain, fetal brain and placenta. Detected in lung tumors. {ECO:0000269|PubMed:12677006, ECO:0000269|PubMed:15546177}.; . . 0.01567 0.72108 1.313594923 94.04930408 1303.68976 6.79389 SLEB3 . . . systemic lupus erythematosus susceptibility 3 . . . . . . . . . . . SLEH1 . . . systemic lupus erythematosus with hemolytic anemia 1 . . . . . . . . . . . SLEN1 . . . systemic lupus erythematosus with nephritis 1 . . . . . . . . . . . SLEN2 . . . systemic lupus erythematosus with nephritis 2 . . . . . . . . . . . SLEN3 . . . systemic lupus erythematosus with nephritis 3 . . . . . . . . . . . SLF1 . . . SMC5-SMC6 complex localization factor 1 FUNCTION: Plays a role in the DNA damage response (DDR) pathway by regulating postreplication repair of UV-damaged DNA and genomic stability maintenance (PubMed:25931565). The SLF1-SLF2 complex acts to link RAD18 with the SMC5-SMC6 complex at replication- coupled interstrand cross-links (ICL) and DNA double-strand breaks (DSBs) sites on chromatin during DNA repair in response to stalled replication forks (PubMed:25931565). Promotes the recruitment of SLF2 and the SMC5-SMC6 complex to DNA lesions (PubMed:25931565). {ECO:0000269|PubMed:25931565}.; . . . . . . -0.26993514 34.59542345 . . SLF2 . . . SMC5-SMC6 complex localization factor 2 FUNCTION: Plays a role in the DNA damage response (DDR) pathway by regulating postreplication repair of UV-damaged DNA and genomic stability maintenance (PubMed:25931565). The SLF1-SLF2 complex acts to link RAD18 with the SMC5-SMC6 complex at replication- coupled interstrand cross-links (ICL) and DNA double-strand breaks (DSBs) sites on chromatin during DNA repair in response to stalled replication forks (PubMed:25931565). Promotes the recruitment of the SMC5-SMC6 complex to DNA lesions (PubMed:25931565). {ECO:0000269|PubMed:25931565}.; . TISSUE SPECIFICITY: Widely expressed (PubMed:12459258). Expressed at higher level in skeletal muscle and at slightly lower level in brain, liver and heart, than in lung, kidney, spleen and thymus (PubMed:12459258). {ECO:0000269|PubMed:12459258}.; . . 0.11978 0.09541 0.358272123 74.66383581 . . SLFN5 1.21564626085827e-09 0.180683848696598 0.819316150087755 schlafen family member 5 FUNCTION: May have a role in hematopoietic cell differentiation. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;ovary;colon;vein;skin;skeletal muscle;breast;pancreas;prostate;lung;endometrium;nasopharynx;bone;placenta;liver;spleen;cervix;germinal center;kidney;brain; superior cervical ganglion; 0.06373 . 0.628293289 83.56923803 3086.4579 10.55291 SLFN11 7.42072878105611e-16 0.00419470665203081 0.995805293347969 schlafen family member 11 FUNCTION: Interferon (IFN)-induced antiviral protein which acts as an inhibitor of retrovirus protein synthesis. Specifically abrogates the production of retroviruses such as human immunodeficiency virus 1 (HIV-1) by acting as a specific inhibitor of the synthesis of retroviruses encoded proteins in a codon- usage-dependent manner. Binds to tRNAs and exploits the unique viral codon bias towards A/T nucleotides. The exact inhibition mechanism is unclear: may either sequesters tRNAs, prevents their maturation via post-transcriptional processing or accelerates their deacylation. Does not inhibit reverse transcription, integration or production and nuclear export of viral RNA. May play a role in cell cycle arrest and/or induction of apoptosis in response to exogenously induced DNA damage. {ECO:0000269|PubMed:22927417, ECO:0000269|PubMed:23000900}.; . TISSUE SPECIFICITY: Exhibits a wider expression range in ovarian and colon adenocarcinoma than in their corresponding healthy tissues. {ECO:0000269|PubMed:22927417}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;heart;colon;skin;skeletal muscle;retina;bone marrow;breast;uterus;lung;endometrium;iris;liver;testis;spleen;germinal center;kidney;brain;aorta;stomach;thymus; . 0.21771 . 0.093718683 60.71007313 177.29534 2.89331 SLFN12 5.03596136268757e-10 0.0590369237278699 0.940963075768534 schlafen family member 12 . . . unclassifiable (Anatomical System);prostate;lung;whole body;ovary;bone;testis;germinal center;brain;skeletal muscle; medulla oblongata;superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion; 0.04183 0.06956 1.332002318 94.20853975 171.00693 2.85286 SLFN12L 2.34689349034419e-05 0.501639472004437 0.49833705906066 schlafen family member 12-like . . . blood;brain; . 0.08168 . 2.771030479 99.00920028 1908.34734 8.04469 SLFN13 8.74558215982401e-15 0.00483449428361537 0.995165505716376 schlafen family member 13 . . . unclassifiable (Anatomical System);adrenal cortex;parathyroid;skeletal muscle;uterus;lung;larynx;adrenal gland;gum;placenta;thyroid;head and neck;kidney;germinal center;spinal ganglion;brain;pineal gland; . 0.05976 0.06727 2.763559657 98.99740505 1954.11134 8.13480 SLFN14 . . . schlafen family member 14 . . . . . . . 2.706654586 98.92663364 4844.8062 14.13377 SLFNL1 0.000108969289298797 0.592466133144432 0.407424897566269 schlafen like 1 . . . medulla oblongata;cartilage;blood;choroid;fovea centralis;lens;bone marrow;retina;optic nerve;lung;macula lutea;testis;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.09021 . 0.981046964 90.45765511 1495.1636 7.19266 SLFNL1-AS1 . . . SLFNL1 antisense RNA 1 . . . . . . . . . . . SLIRP 0.000361057844318624 0.383199740674602 0.616439201481079 SRA stem-loop interacting RNA binding protein FUNCTION: RNA-binding protein that acts as a nuclear receptor corepressor. Probably acts by binding the SRA RNA, and repressing the SRA-mediated nuclear receptor coactivation. Binds the STR7 loop of SRA RNA. Also able to repress glucocorticoid (GR), androgen (AR), thyroid (TR) and VDR-mediated transactivation. {ECO:0000269|PubMed:16762838}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest level in heart, liver, skeletal muscle and testis. {ECO:0000269|PubMed:16762838}.; myocardium;lymphoreticular;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;bladder;brain;heart;cartilage;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;uterus;whole body;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;trophoblast;islets of Langerhans;muscle;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; whole brain;subthalamic nucleus;testis - interstitial;testis; 0.03676 . 0.03689118 56.64071715 69.94769 1.73457 SLIT1 0.999930815097543 6.91849024554537e-05 1.08387308962842e-15 slit guidance ligand 1 FUNCTION: Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions (By similarity). SLIT1 and SLIT2 together seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. {ECO:0000250}.; . TISSUE SPECIFICITY: Predominantly expressed in adult forebrain. Expressed in fetal brain, lung and kidney. {ECO:0000269|PubMed:9813312}.; unclassifiable (Anatomical System);lung;frontal lobe;visual apparatus;iris;pituitary gland;testis;brain;skeletal muscle;thymus; whole brain;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;hypothalamus;temporal lobe;pons;atrioventricular node;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.53886 0.13320 -2.02851154 1.704411418 285.44708 3.61752 SLIT1-AS1 . . . SLIT1 antisense RNA 1 . . . . . . . . . . . SLIT2 0.999999067396252 9.32603747964609e-07 1.48963298276163e-19 slit guidance ligand 2 FUNCTION: Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions. SLIT1 and SLIT2 seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. In spinal chord development may play a role in guiding commissural axons once they reached the floor plate by modulating the response to netrin. In vitro, silences the attractive effect of NTN1 but not its growth- stimulatory effect and silencing requires the formation of a ROBO1-DCC complex. May be implicated in spinal chord midline post- crossing axon repulsion. In vitro, only commissural axons that crossed the midline responded to SLIT2. In the developing visual system appears to function as repellent for retinal ganglion axons by providing a repulsion that directs these axons along their appropriate paths prior to, and after passage through, the optic chiasm. In vitro, collapses and repels retinal ganglion cell growth cones. Seems to play a role in branching and arborization of CNS sensory axons, and in neuronal cell migration. In vitro, Slit homolog 2 protein N-product, but not Slit homolog 2 protein C-product, repels olfactory bulb (OB) but not dorsal root ganglia (DRG) axons, induces OB growth cones collapse and induces branching of DRG axons. Seems to be involved in regulating leukocyte migration. {ECO:0000269|PubMed:10102268, ECO:0000269|PubMed:10864954, ECO:0000269|PubMed:10975526, ECO:0000269|PubMed:11239147, ECO:0000269|PubMed:11309622, ECO:0000269|PubMed:11404413}.; . TISSUE SPECIFICITY: Fetal lung and kidney, and adult spinal cord. Weak expression in adult adrenal gland, thyroid, trachea and other tissues examined. {ECO:0000269|PubMed:10349621, ECO:0000269|PubMed:9813312}.; unclassifiable (Anatomical System);cartilage;heart;hypothalamus;parathyroid;skin;skeletal muscle;uterus;pancreas;whole body;lung;frontal lobe;nasopharynx;iris;duodenum;testis;spleen;kidney;spinal ganglion;brain;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;olfactory bulb;globus pallidus;trigeminal ganglion;parietal lobe; 0.25438 0.21802 -2.184712649 1.397735315 141.45348 2.59512 SLIT2-IT1 . . . SLIT2 intronic transcript 1 . . . . . . . . . . . SLIT3 0.991788383605727 0.00821161639423094 4.20202992632286e-14 slit guidance ligand 3 FUNCTION: May act as molecular guidance cue in cellular migration, and function may be mediated by interaction with roundabout homolog receptors.; . TISSUE SPECIFICITY: Predominantly expressed in thyroid. {ECO:0000269|PubMed:9813312}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);amygdala;heart;cartilage;urinary;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;amnion;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; superior cervical ganglion;adipose tissue;thyroid;ciliary ganglion;trigeminal ganglion; 0.82846 0.13042 -2.196075097 1.374144845 779.81909 5.52544 SLITRK1 0.988430445876677 0.0115687083594406 8.45763882091689e-07 SLIT and NTRK like family member 1 FUNCTION: Enhances neuronal dendrite outgrowth. {ECO:0000269|PubMed:16224024}.; DISEASE: Gilles de la Tourette syndrome (GTS) [MIM:137580]: Neurologic disorder manifested particularly by motor and vocal tics and associated with behavioral abnormalities. {ECO:0000269|PubMed:16224024}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Trichotillomania (TTM) [MIM:613229]: A neuropsychiatric disorder characterized by chronic, repetitive, or compulsive hair pulling resulting in noticeable hair loss. Affected individuals may develop physical complications and often have overlapping psychological disorders, such as Gilles de la Tourette syndrome or obsessive-compulsive disorder. {ECO:0000269|PubMed:16224024}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly in the frontal lobe of the cerebral cortex of the brain. Also expressed in some astrocytic brain tumors such as astrocytomas, oligodendrogliomas, glioblastomas, gangliogliomas and primitive neuroectodermal tumors. {ECO:0000269|PubMed:14557068}.; . . 0.40398 . -0.846787714 11.05803255 41.72194 1.21562 SLITRK2 0.240674715780331 0.752455079168185 0.00687020505148401 SLIT and NTRK like family member 2 FUNCTION: Suppresses neurite outgrowth. {ECO:0000250|UniProtKB:Q810C0}.; . TISSUE SPECIFICITY: Expressed predominantly in the cerebral cortex of the brain but also at low levels in the spinal cord and medulla. Also expressed in some astrocytic brain tumors such as astrocytomas, oligodendrogliomas, glioblastomas, gangliogliomas and primitive neuroectodermal tumors. {ECO:0000269|PubMed:14557068}.; unclassifiable (Anatomical System);cochlea;larynx;hypothalamus;macula lutea;visual apparatus;spinal cord;head and neck;fovea centralis;brain;skin;skeletal muscle;retina; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.14299 0.11691 -0.778825328 12.88039632 560.43202 4.80823 SLITRK3 0.603043296412279 0.396878441120795 7.82624669262245e-05 SLIT and NTRK like family member 3 FUNCTION: Suppresses neurite outgrowth. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the occipital lobe of the cerebral cortex of the brain. Expressed at higher levels in some astrocytic brain tumors such as astrocytomas, oligodendrogliomas, glioblastomas, gangliogliomas and primitive neuroectodermal tumors. {ECO:0000269|PubMed:14557068}.; unclassifiable (Anatomical System);amygdala;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe; 0.30131 0.10926 -0.354480518 29.42911064 66.81192 1.68748 SLITRK4 0.613671416329225 0.384601804056073 0.00172677961470205 SLIT and NTRK like family member 4 FUNCTION: Suppresses neurite outgrowth. {ECO:0000250|UniProtKB:Q810B8}.; . TISSUE SPECIFICITY: Expressed in the cerebral cortex of the brain and at higher levels in some astrocytic brain tumors such as astrocytomas, glioblastomas and primitive neuroectodermal tumors. {ECO:0000269|PubMed:14557068}.; unclassifiable (Anatomical System);breast;frontal lobe;visual apparatus;hippocampus;kidney;mammary gland;skeletal muscle; parietal lobe; 0.58752 0.11227 -0.780646273 12.77423921 32.67427 1.01525 SLITRK5 0.812088308384531 0.187710445742625 0.000201245872843611 SLIT and NTRK like family member 5 FUNCTION: Suppresses neurite outgrowth. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed predominantly in the cerebral cortex of the brain but also at low levels in the spinal cord and medulla. {ECO:0000269|PubMed:14557068}.; . . 0.33999 0.12224 -1.636932785 2.824958717 87.31396 1.99587 SLITRK6 8.60812958532084e-06 0.761742700277024 0.23824869159339 SLIT and NTRK like family member 6 FUNCTION: Regulator of neurite outgrowth required for normal hearing and vision. {ECO:0000269|PubMed:23543054}.; . TISSUE SPECIFICITY: In adult brain, highly expressed in putamen with no expression in cerebral cortex. Expressed in adult and fetal lung and fetal liver. Also expressed at high levels in some brain tumors including medulloblastomas and primitive neuroectodermal tumors. {ECO:0000269|PubMed:14557068}.; . . 0.37600 0.11127 -0.775187015 13.05142722 123.47005 2.41874 SLK 0.428398338221419 0.571601640436051 2.13425302578809e-08 STE20 like kinase FUNCTION: Mediates apoptosis and actin stress fiber dissolution. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highest expression is found in heart and in skeletal muscle. {ECO:0000269|PubMed:10699464}.; unclassifiable (Anatomical System);parathyroid;skin;uterus;prostate;lung;placenta;thyroid;bone;testis;mammary gland;brain;cerebellum; amygdala;medulla oblongata;superior cervical ganglion;prefrontal cortex;ciliary ganglion;caudate nucleus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.18310 0.12551 -0.374708069 28.15522529 1149.0771 6.45902 SLMAP 0.999325964654365 0.000674035338851834 6.78277330584846e-12 sarcolemma associated protein FUNCTION: May play a role during myoblast fusion. {ECO:0000250}.; . . medulla oblongata;ovary;colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;atrium;endometrium;larynx;thyroid;testis;germinal center;artery;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;blood;skeletal muscle;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;alveolus;cervix;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.43101 0.11509 -1.155457828 6.168907761 40.3211 1.18430 SLN 0.393191120931887 0.473906913433013 0.1329019656351 sarcolipin FUNCTION: Reversibly inhibits the activity of ATP2A1 in sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Required for muscle-based, non-shivering thermogenesis (By similarity). Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in muscle. {ECO:0000250, ECO:0000269|PubMed:11781085, ECO:0000269|PubMed:9575189}.; . . unclassifiable (Anatomical System);heart;tongue;muscle;colon;fovea centralis;lens;skeletal muscle;uterus;pancreas;prostate;whole body;lung;thyroid;placenta;macula lutea;alveolus;liver;testis;head and neck;brain; dorsal root ganglion;superior cervical ganglion;tongue;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.33193 . 0.079165051 59.43029016 0.70534 0.01134 SLPI 0.00034794041537936 0.376581643721714 0.623070415862906 secretory leukocyte peptidase inhibitor FUNCTION: Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G (PubMed:3533531, PubMed:3462719, PubMed:2039600, PubMed:2110563, PubMed:10702419, PubMed:24121345). Modulates the inflammatory and immune responses after bacterial infection, and after infection by the intracellular parasite L.major. Down-regulates responses to bacterial lipopolysaccharide (LPS) (By similarity). Plays a role in regulating the activation of NF-kappa-B and inflammatory responses (PubMed:10702419, PubMed:24352879). Has antimicrobial activity against mycobacteria, but not against salmonella. Contributes to normal resistance against infection by M.tuberculosis. Required for normal resistance to infection by L.major. Required for normal wound healing, probably by preventing tissue damage by limiting protease activity (By similarity). Together with ELANE, required for normal differentiation and proliferation of bone marrow myeloid cells (PubMed:24352879). {ECO:0000250|UniProtKB:P97430, ECO:0000269|PubMed:10702419, ECO:0000269|PubMed:2039600, ECO:0000269|PubMed:2110563, ECO:0000269|PubMed:24121345, ECO:0000269|PubMed:24352879, ECO:0000269|PubMed:3462719, ECO:0000269|PubMed:3533531, ECO:0000305}.; . TISSUE SPECIFICITY: Detected in blood plasma (PubMed:24352879). Detected in bone marrow myeloid cells (PubMed:24352879). Detected in airway sputum (PubMed:2039600). Detected in parotid gland secretions (PubMed:3462719). Detected in seminal plasma (at protein level) (PubMed:3485543). Detected in uterus cervix (PubMed:3533531). {ECO:0000269|PubMed:2039600, ECO:0000269|PubMed:24352879, ECO:0000269|PubMed:3462719, ECO:0000269|PubMed:3485543, ECO:0000269|PubMed:3533531}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;thyroid;pituitary gland;testis;dura mater;brain;pineal gland;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;lacrimal gland;oral cavity;adrenal cortex;pharynx;blood;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hypopharynx;liver;cervix;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;uterus corpus;superior cervical ganglion;lung;trachea;tongue;salivary gland;ciliary ganglion;atrioventricular node;trigeminal ganglion;bone marrow; 0.07426 0.41071 -0.09720619 46.20193442 4.90998 0.18184 SLTM 0.999996386807791 3.61319220883463e-06 4.03478742966713e-18 SAFB like transcription modulator FUNCTION: When overexpressed, acts as a general inhibitor of transcription that eventually leads to apoptosis. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;vein;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;larynx;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;lens;skeletal muscle;breast;lung;nasopharynx;macula lutea;visual apparatus;hippocampus;liver;cervix;head and neck;kidney;mammary gland;stomach; uterus;amygdala;testis - interstitial;hypothalamus;prefrontal cortex;parietal lobe; 0.76942 0.13267 -1.041578376 7.773059684 35.72113 1.07457 SLU7 0.000115176106946952 0.999428672783936 0.000456151109117376 SLU7 homolog, splicing factor FUNCTION: Participates in the second catalytic step of pre-mRNA splicing, when the free hydroxyl group of exon I attacks the 3'- splice site to generate spliced mRNA and the excised lariat intron. Required for holding exon 1 properly in the spliceosome and for correct AG identification when more than one possible AG exists in 3'-splicing site region. May be involved in the activation of proximal AG. Probably also involved in alternative splicing regulation. {ECO:0000269|PubMed:10197984, ECO:0000269|PubMed:10647016, ECO:0000269|PubMed:12764196, ECO:0000269|PubMed:15728250}.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;islets of Langerhans;spinal cord;blood;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;stomach;aorta;peripheral nerve; . 0.25173 0.12483 -0.091746757 46.91554612 149.54581 2.66634 SLURP1 0.328314103428116 0.607811972617936 0.0638739239539481 secreted LY6/PLAUR domain containing 1 FUNCTION: Has an antitumor activity. Was found to be a marker of late differentiation of the skin. Implicated in maintaining the physiological and structural integrity of the keratinocyte layers of the skin.; DISEASE: Mal de Meleda (MDM) [MIM:248300]: A rare autosomal recessive skin disorder, characterized by diffuse transgressive palmoplantar keratoderma with keratotic lesions extending onto the dorsa of the hands and the feet (transgrediens). Patients may have hyperhidrosis. Other features include perioral erythema, lichenoid plaques on the knees and the elbows, and nail abnormalities. {ECO:0000269|PubMed:11285253, ECO:0000269|PubMed:12483299, ECO:0000269|PubMed:14756676, ECO:0000269|PubMed:17008884}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Granulocytes. Expressed in skin. Predominantly expressed in the granular layer of skin, notably the acrosyringium. Identified in several biological fluids such as sweat, saliva, tears, plasma and urine. {ECO:0000269|PubMed:14721776, ECO:0000269|PubMed:17008884}.; unclassifiable (Anatomical System);optic nerve;heart;macula lutea;fovea centralis;choroid;lens;retina; superior cervical ganglion;tongue;trigeminal ganglion;skin;tonsil;skeletal muscle; 0.07932 0.54132 0.169169615 65.33380514 3.52718 0.12891 SLX1A 0.625453893215557 0.343404593773495 0.0311415130109482 SLX1 homolog A, structure-specific endonuclease subunit FUNCTION: Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for 5'-flap structures, and promotes symmetrical cleavage of static and migrating Holliday junctions (HJs). Resolves HJs by generating two pairs of ligatable, nicked duplex products. {ECO:0000255|HAMAP-Rule:MF_03100, ECO:0000269|PubMed:19595721, ECO:0000269|PubMed:19596235, ECO:0000269|PubMed:19596236}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;hypothalamus;lens;pancreas;lung;epididymis;placenta;macula lutea;hippocampus;visual apparatus;alveolus;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach;thymus; . 0.99931 . . . 92.27474 2.06605 SLX1A-SULT1A3 . . . SLX1A-SULT1A3 readthrough (NMD candidate) . . . . . 0.81570 . . . . . SLX1B 0.516792296405978 0.417346227679325 0.0658614759146971 SLX1 homolog B, structure-specific endonuclease subunit FUNCTION: Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for 5'-flap structures, and promotes symmetrical cleavage of static and migrating Holliday junctions (HJs). Resolves HJs by generating two pairs of ligatable, nicked duplex products. {ECO:0000255|HAMAP-Rule:MF_03100, ECO:0000269|PubMed:19595721, ECO:0000269|PubMed:19596235, ECO:0000269|PubMed:19596236}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;hypothalamus;lens;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; . 0.99943 . . . 0.93902 0.02025 SLX1B-SULT1A4 . . . SLX1B-SULT1A4 readthrough (NMD candidate) . . . . . . . . . . . SLX4 8.90319772055342e-08 0.999813620295056 0.000186290672966407 SLX4 structure-specific endonuclease subunit FUNCTION: Regulatory subunit that interacts with and increases the activity of different structure-specific endonucleases. Has several distinct roles in protecting genome stability by resolving diverse forms of deleterious DNA structures originating from replication and recombination intermediates and from DNA damage. Component of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for 5'-flap structures, and promotes symmetrical cleavage of static and migrating Holliday junctions (HJs). Resolves HJs by generating two pairs of ligatable, nicked duplex products. Interacts with the structure- specific ERCC4-ERCC1 endonuclease and promotes the cleavage of bubble structures. Interacts with the structure-specific MUS81- EME1 endonuclease and promotes the cleavage of 3'-flap and replication fork-like structures. SLX4 is required for recovery from alkylation-induced DNA damage and is involved in the resolution of DNA double-strand breaks. {ECO:0000269|PubMed:19595721, ECO:0000269|PubMed:19595722, ECO:0000269|PubMed:19596235, ECO:0000269|PubMed:19596236}.; DISEASE: Fanconi anemia complementation group P (FANCP) [MIM:613951]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. Some individuals affected by Fanconi anemia of complementation group P have skeletal anomalies. {ECO:0000269|PubMed:21240275, ECO:0000269|PubMed:21240277}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;medulla oblongata;pancreas;lung;testis;blood;germinal center;brain; whole brain;superior cervical ganglion;ciliary ganglion; 0.06210 . 1.174043417 92.73413541 3061.38998 10.52526 SLX4IP 2.33883944799938e-05 0.739325730986361 0.260650880619159 SLX4 interacting protein . DISEASE: Note=Chromosomal aberrations involving SLX4IP are found in acute lymphoblastic leukemia. A site-specific deletion within the 5' region of SLX4IP is found in 30% of childhood acute lymphoblastic leukemia in general and more than 60% of ETV6/RUNX1- rearranged acute lymphoblastic leukemia. Breakpoints within SLX4IP reveal junctions with typical characteristics of illegitimate V(D)J mediated recombination. SLX4IP deletions are significantly associated with male gender and ETV6/RUNX1-rearranged acute lymphoblastic leukemia. {ECO:0000269|PubMed:24045615}.; . . . 0.01704 0.05734 0.396906589 76.30927105 633.84208 5.07064 SMAD1 0.870045546037874 0.129589132205808 0.000365321756318483 SMAD family member 1 FUNCTION: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-regulated SMAD (R-SMAD). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. {ECO:0000269|PubMed:12097147}.; DISEASE: Note=SMAD1 variants may be associated with susceptibility to pulmonary hypertension, a disorder characterized by plexiform lesions of proliferating endothelial cells in pulmonary arterioles. The lesions lead to elevated pulmonary arterial pression, right ventricular failure, and death. The disease can occur from infancy throughout life and it has a mean age at onset of 36 years. Penetrance is reduced. Although familial pulmonary hypertension is rare, cases secondary to known etiologies are more common and include those associated with the appetite-suppressant drugs. {ECO:0000269|PubMed:21898662}.; TISSUE SPECIFICITY: Ubiquitous. Highest expression seen in the heart and skeletal muscle.; colon;parathyroid;fovea centralis;vein;skin;uterus;whole body;cerebral cortex;bone;thyroid;testis;amniotic fluid;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;stomach; . 0.95326 0.23021 -0.405853867 26.23260203 17.29088 0.60671 SMAD1-AS1 . . . SMAD1 antisense RNA 1 . . . . . . . . . . . SMAD1-AS2 . . . SMAD1 antisense RNA 2 . . . . . . . . . . . SMAD2 0.988180754171779 0.0118190654654187 1.80362801938759e-07 SMAD family member 2 FUNCTION: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. {ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:16862174, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:19289081, ECO:0000269|PubMed:9892009}.; . TISSUE SPECIFICITY: Expressed at high levels in skeletal muscle, endothelial cells, heart and placenta. {ECO:0000269|PubMed:21599657}.; ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;blood;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion; 0.99992 0.84362 -0.383807564 27.41802312 4.13923 0.15184 SMAD3 0.868268313208796 0.131654637230956 7.704956024792e-05 SMAD family member 3 FUNCTION: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF- mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. {ECO:0000269|PubMed:10995748, ECO:0000269|PubMed:15241418, ECO:0000269|PubMed:15588252, ECO:0000269|PubMed:16156666, ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:16862174, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:19218245, ECO:0000269|PubMed:19289081, ECO:0000269|PubMed:9732876, ECO:0000269|PubMed:9892009}.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:16959974}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Loeys-Dietz syndrome 3 (LDS3) [MIM:613795]: An aortic aneurysm syndrome with widespread systemic involvement. The disorder is characterized by the triad of arterial tortuosity and aneurysms, hypertelorism, and bifid uvula or cleft palate. Patients with LDS3 also manifest early-onset osteoarthritis. They lack craniosynostosis and mental retardation. {ECO:0000269|PubMed:21217753, ECO:0000269|PubMed:21778426}. Note=The disease is caused by mutations affecting the gene represented in this entry. SMAD3 mutations have been reported to be also associated with thoracic aortic aneurysms and dissection (TAAD) (PubMed:21778426). This phenotype is distinguised from LDS3 by having aneurysms restricted to thoracic aorta. As individuals carrying these mutations also exhibit aneurysms of other arteries, including abdominal aorta, iliac, and/or intracranial arteries (PubMed:21778426), they have been classified as LDS3 by the OMIM resource. {ECO:0000269|PubMed:21778426}.; . ovary;colon;skin;prostate;optic nerve;thyroid;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;amnion;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.99959 0.77680 -0.337894035 30.37272942 138.92944 2.56897 SMAD4 0.967432535938662 0.0325652684187115 2.19564262683554e-06 SMAD family member 4 FUNCTION: In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8. Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (By similarity). Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling. Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. {ECO:0000250, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:9389648}.; DISEASE: Pancreatic cancer (PNCA) [MIM:260350]: A malignant neoplasm of the pancreas. Tumors can arise from both the exocrine and endocrine portions of the pancreas, but 95% of them develop from the exocrine portion, including the ductal epithelium, acinar cells, connective tissue, and lymphatic tissue. {ECO:0000269|PubMed:8553070}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Juvenile polyposis syndrome (JPS) [MIM:174900]: Autosomal dominant gastrointestinal hamartomatous polyposis syndrome in which patients are at risk for developing gastrointestinal cancers. The lesions are typified by a smooth histological appearance, predominant stroma, cystic spaces and lack of a smooth muscle core. Multiple juvenile polyps usually occur in a number of Mendelian disorders. Sometimes, these polyps occur without associated features as in JPS; here, polyps tend to occur in the large bowel and are associated with an increased risk of colon and other gastrointestinal cancers. {ECO:0000269|PubMed:12417513, ECO:0000269|PubMed:9811934}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Juvenile polyposis/hereditary hemorrhagic telangiectasia syndrome (JP/HHT) [MIM:175050]: JP/HHT syndrome phenotype consists of the coexistence of juvenile polyposis (JIP) and hereditary hemorrhagic telangiectasia (HHT) [MIM:187300] in a single individual. JIP and HHT are autosomal dominant disorders with distinct and non-overlapping clinical features. The former, an inherited gastrointestinal malignancy predisposition, is caused by mutations in SMAD4 or BMPR1A, and the latter is a vascular malformation disorder caused by mutations in ENG or ACVRL1. All four genes encode proteins involved in the transforming-growth- factor-signaling pathway. Although there are reports of patients and families with phenotypes of both disorders combined, the genetic etiology of this association is unknown. {ECO:0000269|PubMed:15031030}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:16959974}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Note=SMAD4 variants may be associated with susceptibility to pulmonary hypertension, a disorder characterized by plexiform lesions of proliferating endothelial cells in pulmonary arterioles. The lesions lead to elevated pulmonary arterial pression, right ventricular failure, and death. The disease can occur from infancy throughout life and it has a mean age at onset of 36 years. Penetrance is reduced. Although familial pulmonary hypertension is rare, cases secondary to known etiologies are more common and include those associated with the appetite-suppressant drugs. {ECO:0000269|PubMed:21898662}.; DISEASE: Myhre syndrome (MYHRS) [MIM:139210]: A syndrome characterized by pre- and postnatal growth deficiency, mental retardation, generalized muscle hypertrophy and striking muscular build, decreased joint mobility, cryptorchidism, and unusual facies. Dysmorphic facial features include microcephaly, midface hypoplasia, prognathism, and blepharophimosis. Typical skeletal anomalies are short stature, square body shape, broad ribs, iliac hypoplasia, brachydactyly, flattened vertebrae, and thickened calvaria. Other features, such as congenital heart disease, may also occur. {ECO:0000269|PubMed:22158539, ECO:0000269|PubMed:22243968}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;tonsil;gall bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.99992 0.79641 -0.315847836 31.68789809 15.10025 0.54284 SMAD5 0.986055593220514 0.013937803807031 6.60297245506349e-06 SMAD family member 5 FUNCTION: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD5 is a receptor-regulated SMAD (R-SMAD).; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.90777 0.23984 . . 4.72801 0.17213 SMAD5-AS1 . . . SMAD5 antisense RNA 1 . . TISSUE SPECIFICITY: Expressed in fetal tissues.; unclassifiable (Anatomical System);heart;cartilage;choroid;fovea centralis;lens;skin;retina;uterus;pancreas;optic nerve;whole body;macula lutea;kidney; dorsal root ganglion;superior cervical ganglion;globus pallidus;pons;trigeminal ganglion; 0.13543 . . . . . SMAD6 6.96558203122398e-06 0.28440718039152 0.715585854026449 SMAD family member 6 FUNCTION: Acts as a mediator of TGF-beta and BMP antiflammatory activity. Suppresses IL1R-TLR signaling through its direct interaction with PEL1, preventing NF-kappa-B activation, nuclear transport and NF-kappa-B-mediated expression of proinflammatory genes. May block the BMP-SMAD1 signaling pathway by competing with SMAD4 for receptor-activated SMAD1-binding. Binds to regulatory elements in target promoter regions. {ECO:0000269|PubMed:16491121, ECO:0000269|PubMed:16951688, ECO:0000269|PubMed:9436979}.; DISEASE: Aortic valve disease 2 (AOVD2) [MIM:614823]: A common defect in the aortic valve in which two rather than three leaflets are present. It is often associated with aortic valve calcification, stenosis and insufficiency. In extreme cases, the blood flow may be so restricted that the left ventricle fails to grow, resulting in hypoplastic left heart syndrome. {ECO:0000269|PubMed:22275001}. Note=The disease is caused by mutations affecting the gene represented in this entry. SMAD6 variants may contribute to increased risk of congenital cardiovascular malformations (CVM). CVM is a major cause of mortality and morbidity in childhood. In most sporadic cases that cannot be attributed to particular malformation syndromes or teratogenic exposures, there remains a substantial excess familial risk, indicating a significant genetic contribution to disease susceptibility (PubMed:22275001). {ECO:0000269|PubMed:22275001}.; TISSUE SPECIFICITY: Ubiquitous in various organs, with higher levels in lung. Isoform B is up-regulated in diseased heart tissue.; ovary;colon;parathyroid;choroid;skin;retina;uterus;optic nerve;endometrium;testis;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;lung;placenta;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;heart;thyroid;placenta;fetal lung;pons;fetal thyroid; 0.95086 0.25968 . . 153.14066 2.70673 SMAD7 0.975695730781462 0.0242783619654573 2.59072530805204e-05 SMAD family member 7 FUNCTION: Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A- PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator (By similarity). {ECO:0000250, ECO:0000269|PubMed:11163210, ECO:0000269|PubMed:12023024, ECO:0000269|PubMed:14718519, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:9892009}.; DISEASE: Colorectal cancer 3 (CRCS3) [MIM:612229]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:17934461}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous with higher expression in the lung and vascular endothelium.; colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;lung;trabecular meshwork;placenta;macula lutea;hippocampus;cervix;kidney;aorta;cerebellum; superior cervical ganglion;placenta;cerebellum; 0.64740 0.36350 . . 42.87644 1.24096 SMAD9 0.000691360029213452 0.916284653633091 0.0830239863376953 SMAD family member 9 FUNCTION: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD9 is a receptor-regulated SMAD (R-SMAD).; DISEASE: Pulmonary hypertension, primary, 2 (PPH2) [MIM:615342]: A rare disorder characterized by plexiform lesions of proliferating endothelial cells in pulmonary arterioles. The lesions lead to elevated pulmonary arterial pression, right ventricular failure, and death. The disease can occur from infancy throughout life and it has a mean age at onset of 36 years. Penetrance is reduced. Although familial pulmonary hypertension is rare, cases secondary to known etiologies are more common and include those associated with the appetite-suppressant drugs. {ECO:0000269|PubMed:21898662}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, skeletal muscle, prostate, testis, ovary and small intestine. Also expressed in fetal brain, lung and kidney.; unclassifiable (Anatomical System);prostate;lung;heart;islets of Langerhans;hypothalamus;visual apparatus;pituitary gland;liver;spleen;head and neck;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;medulla oblongata;temporal lobe;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.97855 0.18474 -0.778825328 12.88039632 54.85112 1.48403 SMAD9-IT1 . . . SMAD9 intronic transcript 1 . . . . . . . . . . . SMAGP 0.0451746107003794 0.671062292501947 0.283763096797673 small cell adhesion glycoprotein FUNCTION: May play a role in epithelial cell-cell contacts. May play a role in tumor invasiveness and metastasis formation. {ECO:0000269|PubMed:15986429}.; . TISSUE SPECIFICITY: Detected in breast, endometrium, colon and biliary tract. Detected in polarized epithelial structures characterized by cell-cell adhesion (at protein level). {ECO:0000269|PubMed:15021913}.; . . . . 0.147123112 64.11299835 25.59272 0.83475 SMAN1 . . . survival of motor and autonomic neurons 1 . . . . . . . . . . . SMAP1 0.983689233136559 0.0163088011507588 1.96571268226952e-06 small ArfGAP 1 FUNCTION: GTPase activating protein that acts on ARF6. Plays a role in clathrin-dependent endocytosis. May play a role in erythropoiesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in bone marrow, adrenal gland, trachea, lymph node, spinal cord, peripheral blood leukocytes, thyroid and stomach. {ECO:0000269|PubMed:12119110}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;pineal body;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;choroid;fovea centralis;vein;uterus;whole body;larynx;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;mesenchyma;placenta;head and neck;kidney;stomach; amygdala;occipital lobe;hypothalamus; 0.25151 . -0.071520315 48.34866714 1636.02834 7.47505 SMAP2 0.014285645188747 0.984435854269311 0.00127850054194169 small ArfGAP2 FUNCTION: GTPase activating protein that acts on ARF1. Can also activate ARF6 (in vitro). May play a role in clathrin-dependent retrograde transport from early endosomes to the trans-Golgi network (By similarity). {ECO:0000250}.; . . . . 0.35421 0.10694 -0.293801652 32.93819297 138.36435 2.56135 SMARCA1 0.999946645897619 5.33541020372636e-05 3.43349020875278e-13 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 FUNCTION: Energy-transducing component of NURF (nucleosome- remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes. Both complexes facilitate the perturbation of chromatin structure in an ATP-dependent manner. Potentiates neurite outgrowth. May be involved in brain development by regulating En-1 and En-2 expression. May be involved in the development of luteal cells. {ECO:0000269|PubMed:14609955, ECO:0000269|PubMed:15310751, ECO:0000269|PubMed:15640247, ECO:0000269|PubMed:16740656}.; . . . . 0.99248 0.11262 -0.380166007 27.88393489 111.24798 2.29759 SMARCA2 0.999998263539487 1.73646051330321e-06 1.37014442491065e-19 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 FUNCTION: Transcriptional coactivator cooperating with nuclear hormone receptors to potentiate transcriptional activation. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron- specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250}.; DISEASE: Nicolaides-Baraitser syndrome (NCBRS) [MIM:601358]: A rare disorder characterized by severe mental retardation with absent or limited speech, seizures, short stature, sparse hair, typical facial characteristics, brachydactyly, prominent finger joints and broad distal phalanges. Some of the features are progressive with time. {ECO:0000269|PubMed:22366787, ECO:0000269|PubMed:22426308}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Schizophrenia (SCZD) [MIM:181500]: A complex, multifactorial psychotic disorder or group of disorders characterized by disturbances in the form and content of thought (e.g. delusions, hallucinations), in mood (e.g. inappropriate affect), in sense of self and relationship to the external world (e.g. loss of ego boundaries, withdrawal), and in behavior (e.g bizarre or apparently purposeless behavior). Although it affects emotions, it is distinguished from mood disorders in which such disturbances are primary. Similarly, there may be mild impairment of cognitive function, and it is distinguished from the dementias in which disturbed cognitive function is considered primary. Some patients manifest schizophrenic as well as bipolar disorder symptoms and are often given the diagnosis of schizoaffective disorder. {ECO:0000269|PubMed:19363039}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; . lymphoreticular;myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;spinal cord;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta;cerebellum;thymus; amygdala;occipital lobe;testis - interstitial;superior cervical ganglion;atrioventricular node;pons;skeletal muscle;fetal brain;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.99994 0.51636 -1.967739992 1.816466148 2077.08907 8.39385 SMARCA4 0.999999997611829 2.38817148735502e-09 4.32456317016356e-23 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 FUNCTION: Transcriptional coactivator cooperating with nuclear hormone receptors to potentiate transcriptional activation. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron- specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. SMARCA4/BAF190A may promote neural stem cell self- renewal/proliferation by enhancing Notch-dependent proliferative signals, while concurrently making the neural stem cell insensitive to SHH-dependent differentiating cues (By similarity). Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1. {ECO:0000250, ECO:0000269|PubMed:19571879, ECO:0000269|PubMed:20418909}.; DISEASE: Mental retardation, autosomal dominant 16 (MRD16) [MIM:614609]: A disease characterized by multiple congenital anomalies and mental retardation. Mental retardation is defined by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD16 patients manifest developmental delay, absent or hypoplastic fifth fingernails or toenails, thick eyebrows and long eyelashes, hirsutism. Additional findings include hypotonia, microcephaly, seizures, a Dandy-Walker malformation, and vision and hearing problems. {ECO:0000269|PubMed:22426308}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Colocalizes with ZEB1 in E-cadherin-negative cells from established lines, and stroma of normal colon as well as in de-differentiated epithelial cells at the invasion front of colorectal carcinomas (at protein level). {ECO:0000269|PubMed:20418909}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;amnion;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; amygdala;whole brain;testis - interstitial;thalamus;cerebellum peduncles;temporal lobe;tumor;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prostate;fetal brain;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;cingulate cortex;parietal lobe; 0.99989 0.50628 -2.851950648 0.601556971 107.64396 2.25260 SMARCA5 0.999999855058167 1.44941832653672e-07 9.53537090868592e-19 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 FUNCTION: Helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity. Complexes containing SMARCA5 are capable of forming ordered nucleosome arrays on chromatin; this may require intact histone H4 tails. Also required for replication of pericentric heterochromatin in S-phase specifically in conjunction with BAZ1A. Probably plays a role in repression of polI dependent transcription of the rDNA locus, through the recruitment of the SIN3/HDAC1 corepressor complex to the rDNA promoter. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. {ECO:0000269|PubMed:10880450, ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:12198550, ECO:0000269|PubMed:12434153, ECO:0000269|PubMed:12972596, ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:16603771}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; ovary;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;mesenchyma;adrenal gland;placenta;duodenum;head and neck;kidney;stomach;cerebellum; subthalamic nucleus;testis - seminiferous tubule;testis;parietal lobe; 0.97888 0.36004 -0.979072682 8.752064166 9.86498 0.36124 SMARCA5-AS1 . . . SMARCA5 antisense RNA 1 . . . . . . . . . . . SMARCAD1 0.999996802718288 3.19728171022288e-06 1.7868491316686e-15 SWI/SNF-related, matrix-associated actin-dependent regulator of chromatin, subfamily a, containing DEAD/H box 1 FUNCTION: DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Required for the restoration of heterochromatin organization after replication. Acts at replication sites to facilitate the maintenance of heterochromatin by directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation (H3K9me3) and restoration of silencing. {ECO:0000269|PubMed:21549307, ECO:0000269|PubMed:22960744}.; . TISSUE SPECIFICITY: Isoform 1 is expressed ubiquitously. Isoform 3 is expressed mainly in skin, fibroblasts, keratinocytes and esophagus. {ECO:0000269|PubMed:11031099, ECO:0000269|PubMed:21820097}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;islets of Langerhans;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; . 0.31853 0.24651 0.266447942 70.5826846 3025.83606 10.44580 SMARCAL1 0.000314358585842015 0.999152780814 0.000532860600158166 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a-like 1 FUNCTION: ATP-dependent annealing helicase that binds selectively to fork DNA relative to ssDNA or dsDNA and catalyzes the rewinding of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably bound by replication protein A (RPA). Acts throughout the genome to reanneal stably unwound DNA, performing the opposite reaction of many enzymes, such as helicases and polymerases, that unwind DNA. May play an important role in DNA damage response by acting at stalled replication forks. {ECO:0000269|PubMed:18974355, ECO:0000269|PubMed:19793861, ECO:0000269|PubMed:19793862}.; DISEASE: Schimke immuno-osseous dysplasia (SIOD) [MIM:242900]: Causes spondyloepiphyseal dysplasia, renal dysfunction and T-cell immunodeficiency. Approximately half of all patients also exhibit hyperthyroidism, while around half also exhibit episodal cerebral ischemia. {ECO:0000269|PubMed:11799392}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed, with high levels in testis. {ECO:0000269|PubMed:10857751, ECO:0000269|PubMed:11799392}.; lymphoreticular;ovary;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.06763 0.12074 -0.126743121 44.0905874 1034.25533 6.17659 SMARCB1 0.996807633610163 0.00319218700403551 1.79385801336354e-07 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily b, member 1 FUNCTION: Core component of the BAF (hSWI/SNF) complex. This ATP- dependent chromatin-remodeling complex plays important roles in cell proliferation and differentiation, in cellular antiviral activities and inhibition of tumor formation. The BAF complex is able to create a stable, altered form of chromatin that constrains fewer negative supercoils than normal. This change in supercoiling would be due to the conversion of up to one-half of the nucleosomes on polynucleosomal arrays into asymmetric structures, termed altosomes, each composed of 2 histones octamers. Stimulates in vitro the remodeling activity of SMARCA4/BRG1/BAF190A. Involved in activation of CSF1 promoter. Belongs to the neural progenitors- specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Plays a key role in cell-cycle control and causes cell cycle arrest in G0/G1. {ECO:0000250, ECO:0000269|PubMed:10078207, ECO:0000269|PubMed:12226744, ECO:0000269|PubMed:14604992, ECO:0000269|PubMed:16267391, ECO:0000269|PubMed:16314535, ECO:0000269|PubMed:9448295}.; DISEASE: Rhabdoid tumor predisposition syndrome 1 (RTPS1) [MIM:609322]: A familial cancer syndrome predisposing to renal or extrarenal malignant rhabdoid tumors and to a variety of tumors of the central nervous system, including choroid plexus carcinoma, medulloblastoma, and central primitive neuroectodermal tumors. Rhabdoid tumors are the most aggressive and lethal malignancies occurring in early childhood. {ECO:0000269|PubMed:9671307, ECO:0000269|PubMed:9892189}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Schwannomatosis 1 (SWNTS1) [MIM:162091]: A cancer syndrome in which patients develop multiple non-vestibular schwannomas, benign neoplasms that arise from Schwann cells of the cranial, peripheral, and autonomic nerves. {ECO:0000269|PubMed:17357086, ECO:0000269|PubMed:18072270}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Mental retardation, autosomal dominant 15 (MRD15) [MIM:614608]: A disease characterized by multiple congenital anomalies and mental retardation. Mental retardation is defined by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD15 patients manifest developmental delay, hypotonia, absent or hypoplastic fifth finger or toenails, a coarse facial appearance, sparse scalp hair, thick eyebrows, and long eyelashes. Additional variable features include microcephaly, small cerebellum, seizures, hearing loss, abnormal delayed dentition, hirsutism. {ECO:0000269|PubMed:22426308}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;colon;fovea centralis;choroid;vein;uterus;whole body;oesophagus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;thymus; superior cervical ganglion;testis - seminiferous tubule;testis;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.83219 0.29765 -0.339715008 30.06605331 2.2986 0.07774 SMARCC1 0.999999593393603 4.06606396961481e-07 2.38030606862048e-18 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 1 FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). May stimulate the ATPase activity of the catalytic subunit of the complex. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron- specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250, ECO:0000269|PubMed:11018012}.; . TISSUE SPECIFICITY: Expressed in brain, heart, muscle, placenta, lung, liver, muscle, kidney and pancreas.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.82178 . -0.843147538 11.2762444 117.6922 2.35870 SMARCC2 0.999999989058527 1.09414729297026e-08 8.70881108181437e-21 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2 FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Can stimulate the ATPase activity of the catalytic subunit of these complexes. May be required for CoREST dependent repression of neuronal specific gene promoters in non-neuronal cells. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250, ECO:0000269|PubMed:11018012}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;tongue;urinary;pharynx;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach; subthalamic nucleus;superior cervical ganglion;olfactory bulb;prefrontal cortex;globus pallidus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.99223 0.13798 -1.660796428 2.707006369 91.03551 2.05285 SMARCD1 0.99952730034881 0.000472699306322126 3.44867377666422e-10 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 1 FUNCTION: Involved in chromatin remodeling. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Has a strong influence on vitamin D-mediated transcriptional activity from an enhancer vitamin D receptor element (VDRE). May be a link between mammalian SWI-SNF-like chromatin remodeling complexes and the vitamin D receptor (VDR) heterodimer. Mediates critical interactions between nuclear receptors and the BRG1/SMARCA4 chromatin-remodeling complex for transactivation. {ECO:0000250, ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:14698202, ECO:0000269|PubMed:8804307}.; . TISSUE SPECIFICITY: Expressed in all tissues tested, including brain, heart, kidney, liver, lung, muscle, pancreas and placenta. {ECO:0000269|PubMed:8804307}.; . . 0.98335 0.14229 -0.161524709 41.6430762 19.77766 0.67543 SMARCD2 0.980738446599835 0.0192614321716085 1.2122855682083e-07 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 2 FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology).; . TISSUE SPECIFICITY: Isoform 2 is expressed in the pancreas. {ECO:0000269|PubMed:8804307}.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;cerebellum; white blood cells; 0.95247 0.11285 -0.205617011 38.57631517 100.19962 2.16947 SMARCD3 0.23191843214181 0.766547656393887 0.00153391146430326 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 3 FUNCTION: Plays a role in ATP dependent nucleosome remodeling by SMARCA4 containing complexes. Stimulates nuclear receptor mediated transcription. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron- specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post- mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250, ECO:0000269|PubMed:8804307}.; . TISSUE SPECIFICITY: Isoform 2 and isoform 1 are expressed in brain, heart, kidney, placenta, prostate, salivary gland, spleen, testis, thyroid, trachea and uterus. Isoform 1 is also expressed in skeletal muscle and adipose tissue.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;iris;amniotic fluid;germinal center;brain;bladder;cartilage;heart;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pancreas;lung;placenta;hippocampus;kidney;stomach;aorta;cerebellum;thymus; medulla oblongata;occipital lobe;fetal brain;temporal lobe;pons;caudate nucleus;parietal lobe;cingulate cortex; 0.94980 0.18619 -0.492218069 22.35786742 11.99137 0.43523 SMARCE1 0.998188065018721 0.00181188991858853 4.50626907910997e-08 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily e, member 1 FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Required for the coactivation of estrogen responsive promoters by Swi/Snf complexes and the SRC/p160 family of histone acetyltransferases (HATs). Also specifically interacts with the CoREST corepressor resulting in repression of neuronal specific gene promoters in non-neuronal cells. {ECO:0000250}.; DISEASE: Meningioma (MNGMA) [MIM:607174]: A common neoplasm of the central nervous system derived from arachnoidal cells. The majority of meningiomas are well differentiated vascular tumors which grow slowly and have a low potential to be invasive, although malignant subtypes occur. Most cases are sporadic. Familial occurrence of meningioma is rare. {ECO:0000269|PubMed:23377182}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=Defects in SMARCE1 may be a cause of Coffin-Siris syndrome, a highly variable disease characterized by mental retardation associated with a broad spectrum of different clinical features.; . lymphoreticular;smooth muscle;ovary;umbilical cord;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;medulla oblongata;temporal lobe;atrioventricular node;pons;skeletal muscle;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;cerebellum; 0.99682 0.17821 -0.005381972 53.50908233 31.12744 0.98283 SMARCE1P1 . . . SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily e, member 1 pseudogene 1 . . . . . . . . . . . SMARCE1P2 . . . SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily e, member 1 pseudogene 2 . . . . . . . . . . . SMARCE1P3 . . . SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily e, member 1 pseudogene 3 . . . . . . . . . . . SMARCE1P4 . . . SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily e, member 1 pseudogene 4 . . . . . . . . . . . SMARCE1P5 . . . SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily e, member 1 pseudogene 5 . . . . . . . . . . . SMARCE1P6 . . . SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily e, member 1 pseudogene 6 . . . . . . . . . . . SMARCE1P7 . . . SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily e, member 1 pseudogene 7 . . . . . . . . . . . SMC1A 0.999988493720044 1.15062797558354e-05 1.99847072246736e-13 structural maintenance of chromosomes 1A FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint. {ECO:0000269|PubMed:11877377}.; DISEASE: Cornelia de Lange syndrome 2 (CDLS2) [MIM:300590]: A form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. Characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies. {ECO:0000269|PubMed:16604071, ECO:0000269|PubMed:17221863, ECO:0000269|PubMed:17273969, ECO:0000269|PubMed:19701948, ECO:0000269|PubMed:20358602, ECO:0000269|PubMed:20635401}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;aorta;cerebellum; fetal liver;superior cervical ganglion;skeletal muscle; 0.95805 0.25081 -0.494039303 22.09247464 3.97733 0.14702 SMC1B 0.986578245527667 0.0134217544689109 3.42231252469414e-12 structural maintenance of chromosomes 1B FUNCTION: Meiosis-specific component of cohesin complex. Required for the maintenance of meiotic cohesion, but not, or only to a minor extent, for its establishment. Contributes to axial element (AE) formation and the organization of chromatin loops along the AE. Plays a key role in synapsis, recombination and chromosome movements. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The meiosis-specific cohesin complex probably replaces mitosis specific cohesin complex when it dissociates from chromatin during prophase I (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);breast;umbilical cord;testis;blood;germinal center;skeletal muscle; . 0.51288 0.08472 0.271907863 70.73012503 4981.23034 14.38844 SMC2 0.998014292090329 0.00198570790580368 3.86704739907162e-12 structural maintenance of chromosomes 2 FUNCTION: Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. {ECO:0000269|PubMed:11136719}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;subthalamic nucleus;fetal liver;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;skeletal muscle;skin; 0.88883 0.38711 -0.637452658 16.73743808 312.65593 3.76347 SMC2-AS1 . . . SMC2 antisense RNA 1 (head to head) . . . . . . . . . . . SMC3 0.99999999949759 5.02409752404732e-10 4.79486782993066e-24 structural maintenance of chromosomes 3 FUNCTION: Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex plays also an important role in spindle pole assembly during mitosis and in chromosomes movement. {ECO:0000269|PubMed:11076961, ECO:0000269|PubMed:19907496}.; DISEASE: Cornelia de Lange syndrome 3 (CDLS3) [MIM:610759]: A form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. Characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies. Cornelia de Lange syndrome type 3 is a mild form with absence of major structural anomalies. The phenotype in some instances approaches that of apparently non- syndromic mental retardation. {ECO:0000269|PubMed:17273969}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;breast;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; subthalamic nucleus;white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.97678 0.09885 -0.890882376 10.30313753 11.36859 0.41026 SMC4 0.105530996358142 0.894468907548637 9.60932210783989e-08 structural maintenance of chromosomes 4 FUNCTION: Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. {ECO:0000269|PubMed:11136719}.; . TISSUE SPECIFICITY: Widely expressed. Higher expression in testis, colon, thymus. {ECO:0000269|PubMed:10319587}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;gum;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;breast;bile duct;pancreas;lung;placenta;visual apparatus;alveolus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; fetal liver;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;tumor;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.99449 0.27637 -0.992035476 8.604623732 434.06529 4.34898 SMC4P1 . . . structural maintenance of chromosomes 4 pseudogene 1 . . . . . . . . . . . SMC5 0.980364885210913 0.0196351147459722 4.31147357842747e-11 structural maintenance of chromosomes 5 FUNCTION: Core component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Required for recruitment of telomeres to PML nuclear bodies. Required for sister chromatid cohesion during prometaphase and mitotic progression; the function seems to be independent of SMC6. {ECO:0000269|PubMed:16810316, ECO:0000269|PubMed:17589526, ECO:0000269|PubMed:19502785}.; . TISSUE SPECIFICITY: Widely expressed (PubMed:11408570). Strongly expressed in testis (PubMed:11408570). {ECO:0000269|PubMed:11408570}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;lacrimal gland;tongue;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.35486 0.11584 -0.282886048 33.53385232 892.18859 5.82054 SMC5-AS1 . . . SMC5 antisense RNA 1 (head to head) . . . . . . . . . . . SMC6 0.455419790303775 0.544580206180894 3.51533138345104e-09 structural maintenance of chromosomes 6 FUNCTION: Core component of the SMC5-SMC6 complex, a complex involved in DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Required for recruitment of telomeres to PML nuclear bodies. {ECO:0000269|PubMed:16810316, ECO:0000269|PubMed:17589526}.; . TISSUE SPECIFICITY: Widely expressed (PubMed:11408570). Strongly expressed in testis (PubMed:11408570). {ECO:0000269|PubMed:11408570}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.89390 0.11318 -0.819281839 11.93677754 2438.56484 9.18045 SMCHD1 0.999999998790609 1.20939075674713e-09 3.37551625006544e-25 structural maintenance of chromosomes flexible hinge domain containing 1 FUNCTION: Required for maintenance of X inactivation in females and hypermethylation of CpG islands associated with inactive X. Involved in a pathway that mediates the methylation of a subset of CpG islands slowly and requires the de novo methyltransferase DNMT3B (By similarity). Required for DUX4 silencing in somatic cells. {ECO:0000250, ECO:0000269|PubMed:23143600}.; DISEASE: Facioscapulohumeral muscular dystrophy 2 (FSHD2) [MIM:158901]: A degenerative muscle disease characterized by slowly progressive weakness of the muscles of the face, upper-arm, and shoulder girdle. The onset of symptoms usually occurs in the first or second decade of life. Affected individuals usually present with impairment of upper extremity elevation. This tends to be followed by facial weakness, primarily involving the orbicularis oris and orbicularis oculi muscles. {ECO:0000269|PubMed:23143600}. Note=The disease is caused by mutations affecting the gene represented in this entry. SMCHD1 mutations lead to DUX4 expression in somatic tissues, including muscle cells, when an haplotype on chromosome 4 is permissive for DUX4 expression. Ectopic expression of DUX4 in skeletal muscle activates the expression of stem cell and germline genes, and, when overexpressed in somatic cells, DUX4 can ultimately lead to cell death.; . smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;brain;heart;cartilage;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;oral cavity;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;whole blood;trigeminal ganglion;skeletal muscle; 0.94605 0.11421 -1.699477247 2.565463553 2822.43247 10.02182 SMCO1 4.62967906395968e-05 0.239799935135209 0.760153768074151 single-pass membrane protein with coiled-coil domains 1 . . . . . 0.08727 . 0.859896574 88.62349611 1753.05727 7.72679 SMCO2 . . . single-pass membrane protein with coiled-coil domains 2 . . . . . . . 0.881944684 89.02453409 398.02888 4.19168 SMCO3 0.205394525245437 0.64813429346814 0.146471181286423 single-pass membrane protein with coiled-coil domains 3 . . . . . . . 0.948089677 89.95635763 1026.7651 6.15913 SMCO4 0.00205704974104072 0.302432807550528 0.695510142708432 single-pass membrane protein with coiled-coil domains 4 . . . . . 0.35624 0.11809 -0.009020804 52.8544468 11.33297 0.40782 SMCO4P1 . . . single-pass membrane protein with coiled-coil domains 4 pseudogene 1 . . . . . . . . . . . SMCP 0.0429932404361666 0.662129367964527 0.294877391599306 sperm mitochondria associated cysteine rich protein FUNCTION: Involved in sperm motility. Its absence is associated with genetic background dependent male infertility. Infertility may be due to reduced sperm motility in the female reproductive tract and inability to penetrate the oocyte zona pellucida (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis. Is selectively expressed in the spermatids of seminiferous tubules. {ECO:0000269|PubMed:8833144}.; . . 0.06728 0.20664 0.435547893 77.45340882 8.79413 0.32448 SMCR2 . . . Smith-Magenis syndrome chromosome region, candidate 2 (non-protein coding) . . . . . . . . . . . SMCR5 . . . Smith-Magenis syndrome chromosome region, candidate 5 (non-protein coding) . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11997338}.; . . . . . . . . SMCR6 . . . Smith-Magenis syndrome chromosome region, candidate 6 (non-protein coding) . . . . . . . . . . . SMCR8 0.31942005816427 0.677042073280586 0.00353786855514298 Smith-Magenis syndrome chromosome region, candidate 8 . . TISSUE SPECIFICITY: Expressed in all tissues tested. {ECO:0000269|PubMed:11997338}.; . . 0.19060 . -0.789972689 12.61500354 2152.60765 8.53574 SMDT1 0.163350133143623 0.639606461404987 0.19704340545139 single-pass membrane protein with aspartate-rich tail 1 FUNCTION: Essential regulatory subunit of the mitochondrial calcium uniporter complex (uniplex), a complex that mediates calcium uptake into mitochondria. Required to bridge the calcium- sensing proteins MICU1 and MICU2 with the calcium-conducting subunit MCU. {ECO:0000269|PubMed:24231807}.; . . . . 0.17181 0.10294 -0.273576253 33.97027601 12.90089 0.47023 SMG1 0.999999999999956 4.40114169317691e-14 1.0514387457688e-36 SMG1 phosphatidylinositol 3-kinase-related kinase FUNCTION: Serine/threonine protein kinase involved in both mRNA surveillance and genotoxic stress response pathways. Recognizes the substrate consensus sequence [ST]-Q. Plays a central role in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by phosphorylating UPF1/RENT1. Recruited by release factors to stalled ribosomes together with SMG8 and SMG9 (forming the SMG1C protein kinase complex), and UPF1 to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Also acts as a genotoxic stress-activated protein kinase that displays some functional overlap with ATM. Can phosphorylate p53/TP53 and is required for optimal p53/TP53 activation after cellular exposure to genotoxic stress. Its depletion leads to spontaneous DNA damage and increased sensitivity to ionizing radiation (IR). May activate PRKCI but not PRKCZ. {ECO:0000269|PubMed:11331269, ECO:0000269|PubMed:11544179, ECO:0000269|PubMed:15175154, ECO:0000269|PubMed:16452507}.; . TISSUE SPECIFICITY: Widely expressed, with highest level in heart and skeletal muscle. Expressed in placenta, brain, lung and spleen, but not in liver. {ECO:0000269|PubMed:15175154, ECO:0000269|PubMed:8524286}.; . . . . -2.975494782 0.542580797 910.18577 5.86659 SMG1P1 . . . SMG1 pseudogene 1 . . . . . . . . . . . SMG1P2 . . . SMG1 pseudogene 2 . . . . . . . . . . . SMG1P3 . . . SMG1 pseudogene 3 . . . . . . . . . . . SMG1P4 . . . SMG1 pseudogene 4 . . . . . . . . . . . SMG1P5 . . . SMG1 pseudogene 5 . . . . . . . . . . . SMG1P6 . . . SMG1 pseudogene 6 . . . . . . . . . . . SMG1P7 . . . SMG1 pseudogene 7 . . . . . . . . . . . SMG5 0.998179752831908 0.00182024715263382 1.54577758193072e-11 SMG5 nonsense mediated mRNA decay factor FUNCTION: Plays a role in nonsense-mediated mRNA decay. Does not have RNase activity by itself. Promotes dephosphorylation of UPF1. Together with SMG7 is thought to provide a link to the mRNA degradation machinery involving exonucleolytic pathways, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation. Necessary for TERT activity. {ECO:0000269|PubMed:17053788}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12699629, ECO:0000269|PubMed:14636577}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;nervous;spinal cord;muscle;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; thalamus;trigeminal ganglion; 0.23950 0.12620 -1.015898037 8.144609578 170.50384 2.84858 SMG6 0.999935136420641 6.48635793361172e-05 2.26237461232758e-14 SMG6 nonsense mediated mRNA decay factor FUNCTION: Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. May have a general role in telomere regulation. Promotes in vitro the ability of TERT to elongate telomeres. Overexpression induces telomere uncapping, chromosomal end-to-end fusions (telomeric DNA persists at the fusion points) and did not perturb TRF2 telomeric localization. Binds to the single-stranded 5'- (GTGTGG)(4)GTGT-3' telomeric DNA, but not to a telomerase RNA template component (TER).; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12676087, ECO:0000269|PubMed:12699629}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;caudate nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.49298 0.14853 -0.156295711 42.06180703 10938.5577 22.74291 SMG6-IT1 . . . SMG6 intronic transcript 1 . . . . . . . . . . . SMG7 0.999981493421641 1.85065783537558e-05 5.2687760615243e-15 SMG7 nonsense mediated mRNA decay factor FUNCTION: Plays a role in nonsense-mediated mRNA decay. Recruits UPF1 to cytoplasmic mRNA decay bodies. Together with SMG5 is thought to provide a link to the mRNA degradation machinery involving exonucleolytic pathways, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation. {ECO:0000269|PubMed:15546618, ECO:0000269|PubMed:15721257}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;stomach;cerebellum; dorsal root ganglion;medulla oblongata;superior cervical ganglion;testis - interstitial;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.16156 0.11403 -0.306750577 32.23047889 2354.2528 8.99331 SMG7-AS1 . . . SMG7 antisense RNA 1 . . . . . . . . . . . SMG8 0.0219391466927345 0.97803302689684 2.78264104259102e-05 SMG8 nonsense mediated mRNA decay factor FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited by release factors to stalled ribosomes together with SMG1 and SMG9 (forming the SMG1C protein kinase complex) and, in the SMG1C complex, is required to mediate the recruitment of SMG1 to the ribosome:SURF complex and to suppress SMG1 kinase activity until the ribosome:SURF complex locates the exon junction complex (EJC). Acts as a regulator of kinase activity. {ECO:0000269|PubMed:19417104}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;cerebral cortex;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;hypothalamus;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.29691 . -0.859744935 10.92238736 322.26936 3.81074 SMG9 4.84811349964517e-11 0.192391097374808 0.80760890257671 SMG9 nonsense mediated mRNA decay factor FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited by release factors to stalled ribosomes together with SMG1 and SMG8 (forming the SMG1C protein kinase complex) and, in the SMG1C complex, is required for the efficient association between SMG1 and SMG8. {ECO:0000269|PubMed:19417104}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve;cerebellum; superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;trigeminal ganglion;cerebellum; 0.12939 . -0.756778259 13.44656759 71.11378 1.75548 SMIM1 . . . small integral membrane protein 1 (Vel blood group) FUNCTION: Regulator of red blood cells formation. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in the bone marrow and expressed at lower levels in non-hematopoietic tissues. Highly expressed in erythroleukemia cell lines. Up-regulated in CD34+ hematopoietic progenitors cultured toward red blood cells. {ECO:0000269|PubMed:23563606}.; . . . . . . 1.92553 0.06015 SMIM2 . . . small integral membrane protein 2 . . . . . . . . . 12.34603 0.44777 SMIM2-AS1 . . . SMIM2 antisense RNA 1 . . . . . . . . . . . SMIM2-IT1 . . . SMIM2 intronic transcript 1 . . . . . . . . . . . SMIM3 0.00149206539766125 0.256952971186573 0.741554963415766 small integral membrane protein 3 . . . . . . . . . 192.92181 3.01074 SMIM4 . . . small integral membrane protein 4 . . . . . . . 0.389637587 75.75489502 1.18187 0.03388 SMIM5 . . . small integral membrane protein 5 . . . . . . . 0.12325821 62.38499646 32.16895 1.00853 SMIM6 . . . small integral membrane protein 6 . . . . . . . 0.12325821 62.38499646 9.79869 0.35859 SMIM7 0.417815346539789 0.547200563269613 0.0349840901905973 small integral membrane protein 7 . . . . . 0.22364 . 0.013025609 54.62962963 5.74285 0.21555 SMIM8 0.0358536168485527 0.627875794591138 0.336270588560309 small integral membrane protein 8 . . . . . 0.13057 . 0.215080721 67.91696155 209.20305 3.12277 SMIM9 . . . small integral membrane protein 9 . . . . . . . 0.411684739 76.5628686 57.58868 1.53243 SMIM10 . . . small integral membrane protein 10 . . . . . . . . . 1.97145 0.06443 SMIM10L1 . . . small integral membrane protein 10 like 1 . . . . . . . . . . . SMIM10L2A . . . small integral membrane protein 10 like 2A . . . . . . . . . . . SMIM10L2B . . . small integral membrane protein 10 like 2B . . . . . . . . . . . SMIM11A . . . small integral membrane protein 11A . . TISSUE SPECIFICITY: Expressed in heart, spleen, liver, stomach, muscle, lung, testis, skin, PBL and bone marrow.; . . 0.11581 . 0.369407109 74.95281906 . . SMIM11B . . . small integral membrane protein 11B . . . . . . . . . . . SMIM11P1 . . . small integral membrane protein 11 pseudogene 1 . . . . . . . . . . . SMIM12 0.396299543247483 0.472942868962911 0.130757587789606 small integral membrane protein 12 . . . . . 0.05898 . 0.145304857 63.81221986 2.19212 0.07323 SMIM12P1 . . . small integral membrane protein 12 pseudogene 1 . . . . . . . . . . . SMIM13 . . . small integral membrane protein 13 . . . . . . . 0.12325821 62.38499646 0.00173 0.00067 SMIM14 0.742727362576883 0.246429785835359 0.0108428515877581 small integral membrane protein 14 . . . . . 0.14773 0.10089 0.035072054 56.2514744 . . SMIM15 0.228320204389897 0.646585588537203 0.1250942070729 small integral membrane protein 15 . . . . . . . 0.523736627 80.45529606 42.17786 1.22739 SMIM17 . . . small integral membrane protein 17 . . . . . . . . . 47.15499 1.32932 SMIM18 . . . small integral membrane protein 18 . . . . . . . . . 28.19508 0.90337 SMIM19 0.323327861192079 0.610637356244145 0.0660347825637756 small integral membrane protein 19 . . . . . 0.27703 0.12378 -0.053113545 49.38664779 2.2401 0.07503 SMIM20 . . . small integral membrane protein 20 . . . . . . . 0.167351552 65.04482189 138.9087 2.56856 SMIM21 0.000512613526087449 0.449563895716103 0.549923490757809 small integral membrane protein 21 . . . . . 0.04403 . 0.169169615 65.33380514 5.64594 0.21158 SMIM22 . . . small integral membrane protein 22 . . . . . . . . . 346.46556 3.94798 SMIM23 . . . small integral membrane protein 23 . . . . . . . . . 441.15722 4.37505 SMIM24 . . . small integral membrane protein 24 . . . . . . . 0.834220813 88.15758434 . . SMKR1 . . . small lysine-rich protein 1 . . . . . . . . . 98.95845 2.15267 SMLR1 . . . small leucine-rich protein 1 . . . . . . . . . 3848.0233 12.22026 SMN1 0.10097186938376 0.584009589186655 0.315018541429585 survival of motor neuron 1, telomeric FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs). {ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:23063131, ECO:0000269|PubMed:9845364}.; DISEASE: Spinal muscular atrophy 1 (SMA1) [MIM:253300]: A form of spinal muscular atrophy, a group of neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Autosomal recessive forms are classified according to the age of onset, the maximum muscular activity achieved, and survivorship. The severity of the disease is mainly determined by the copy number of SMN2, a copy gene which predominantly produces exon 7- skipped transcripts and only low amount of full-length transcripts that encode for a protein identical to SMN1. Only about 4% of SMA patients bear one SMN1 copy with an intragenic mutation. SMA1 is a severe form, with onset before 6 months of age. SMA1 patients never achieve the ability to sit. {ECO:0000269|PubMed:10732817, ECO:0000269|PubMed:15249625, ECO:0000269|PubMed:15580564, ECO:0000269|PubMed:7813012, ECO:0000269|PubMed:9147655}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spinal muscular atrophy 2 (SMA2) [MIM:253550]: An autosomal recessive form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. It has intermediate severity, with onset between 6 and 18 months. Patients do not reach the motor milestone of standing, and survive into adulthood. {ECO:0000269|PubMed:10732802, ECO:0000269|PubMed:9158159, ECO:0000269|PubMed:9837824}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spinal muscular atrophy 3 (SMA3) [MIM:253400]: An autosomal recessive form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Onset is after 18 months. Patients develop ability to stand and walk and survive into adulthood. {ECO:0000269|PubMed:10732817, ECO:0000269|PubMed:9158159, ECO:0000269|PubMed:9837824}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spinal muscular atrophy 4 (SMA4) [MIM:271150]: An autosomal recessive form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Onset is in adulthood, disease progression is slow, and patients can stand and walk. {ECO:0000269|PubMed:7658877, ECO:0000269|PubMed:8551862}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in a wide variety of tissues. Expressed at high levels in brain, kidney and liver, moderate levels in skeletal and cardiac muscle, and low levels in fibroblasts and lymphocytes. Also seen at high levels in spinal cord. Present in osteoclasts and mononuclear cells (at protein level). {ECO:0000269|PubMed:11551898, ECO:0000269|PubMed:9259265}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;frontal lobe;larynx;thyroid;testis;amniotic fluid;dura mater;brain;unclassifiable (Anatomical System);meninges;lymph node;pharynx;blood;lens;skeletal muscle;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;thymus; . 0.09692 0.22972 . . 1.19266 0.03478 SMN2 0.0952559827908932 0.574984066027836 0.329759951181271 survival of motor neuron 2, centromeric FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs). {ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:23063131, ECO:0000269|PubMed:9845364}.; DISEASE: Spinal muscular atrophy 1 (SMA1) [MIM:253300]: A form of spinal muscular atrophy, a group of neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Autosomal recessive forms are classified according to the age of onset, the maximum muscular activity achieved, and survivorship. The severity of the disease is mainly determined by the copy number of SMN2, a copy gene which predominantly produces exon 7- skipped transcripts and only low amount of full-length transcripts that encode for a protein identical to SMN1. Only about 4% of SMA patients bear one SMN1 copy with an intragenic mutation. SMA1 is a severe form, with onset before 6 months of age. SMA1 patients never achieve the ability to sit. {ECO:0000269|PubMed:10732817, ECO:0000269|PubMed:15249625, ECO:0000269|PubMed:15580564, ECO:0000269|PubMed:7813012, ECO:0000269|PubMed:9147655}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spinal muscular atrophy 2 (SMA2) [MIM:253550]: An autosomal recessive form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. It has intermediate severity, with onset between 6 and 18 months. Patients do not reach the motor milestone of standing, and survive into adulthood. {ECO:0000269|PubMed:10732802, ECO:0000269|PubMed:9158159, ECO:0000269|PubMed:9837824}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spinal muscular atrophy 3 (SMA3) [MIM:253400]: An autosomal recessive form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Onset is after 18 months. Patients develop ability to stand and walk and survive into adulthood. {ECO:0000269|PubMed:10732817, ECO:0000269|PubMed:9158159, ECO:0000269|PubMed:9837824}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spinal muscular atrophy 4 (SMA4) [MIM:271150]: An autosomal recessive form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Onset is in adulthood, disease progression is slow, and patients can stand and walk. {ECO:0000269|PubMed:7658877, ECO:0000269|PubMed:8551862}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in a wide variety of tissues. Expressed at high levels in brain, kidney and liver, moderate levels in skeletal and cardiac muscle, and low levels in fibroblasts and lymphocytes. Also seen at high levels in spinal cord. Present in osteoclasts and mononuclear cells (at protein level). {ECO:0000269|PubMed:11551898, ECO:0000269|PubMed:9259265}.; . . 0.14041 0.13079 . . 4.27931 0.15576 SMNDC1 0.27579751481189 0.700728201751418 0.0234742834366921 survival motor neuron domain containing 1 FUNCTION: Necessary for spliceosome assembly. Overexpression causes apoptosis. {ECO:0000269|PubMed:11331295, ECO:0000269|PubMed:11331595, ECO:0000269|PubMed:9817934}.; . TISSUE SPECIFICITY: Detected at intermediate levels in skeletal muscle, and at low levels in heart and pancreas. {ECO:0000269|PubMed:9817934}.; . . 0.40030 0.10884 -0.031067188 51.03798066 12.83319 0.46800 SMO 0.0637118150614874 0.936155997012595 0.000132187925917948 smoothened, frizzled class receptor FUNCTION: G protein-coupled receptor that probably associates with the patched protein (PTCH) to transduce the hedgehog's proteins signal. Binding of sonic hedgehog (SHH) to its receptor patched is thought to prevent normal inhibition by patched of smoothened (SMO). Required for the accumulation of KIF7 and GLI3 in the cilia. {ECO:0000269|PubMed:19592253}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;synovium;bone;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;cerebellum peduncles;adrenal cortex;atrioventricular node;trigeminal ganglion; 0.60755 0.41186 -0.574945567 18.90186365 893.91153 5.82819 SMOC1 0.00600403092020696 0.989501706659802 0.00449426241999091 SPARC related modular calcium binding 1 FUNCTION: Plays essential roles in both eye and limb development. Probable regulator of osteoblast differentiation. {ECO:0000269|PubMed:20359165, ECO:0000269|PubMed:21194678, ECO:0000269|PubMed:21194680}.; DISEASE: Ophthalmoacromelic syndrome (OAS) [MIM:206920]: A rare disorder presenting with ocular anomalies, ranging from mild microphthalmia to true anophthalmia, and limb anomalies. Limb malformations include fused 4th and 5th metacarpals and short 5th finger in hands, and oligodactyly in foot (four toes). Most patients have bilateral anophthalmia/ microphthalmia, but unilateral abnormality is also noted. Other malformations are rare, but venous or vertebral anomaly was recognized each in single cases. {ECO:0000269|PubMed:21194678, ECO:0000269|PubMed:21194680, ECO:0000269|PubMed:21750680, ECO:0000269|PubMed:23646827}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed in many tissues with a strongest signal in ovary. No expression in spleen. {ECO:0000269|PubMed:12130637}.; ovary;sympathetic chain;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;bone;testis;brain;pineal gland;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;liver;spleen;head and neck;cervix;mammary gland; superior cervical ganglion;ciliary ganglion; 0.32844 0.13085 0.020302773 55.60863411 157.99132 2.74584 SMOC2 0.0129697790449358 0.979853407114573 0.00717681384049101 SPARC related modular calcium binding 2 FUNCTION: Promotes matrix assembly and cell adhesiveness (By similarity). Can stimulate endothelial cell proliferation, migration, as well as angiogenesis. {ECO:0000250, ECO:0000269|PubMed:16774925}.; DISEASE: Dentin dysplasia 1 (DTDP1) [MIM:125400]: A dental defect in which both primary and secondary dentitions are affected. The clinical crowns of both permanent and deciduous teeth are of normal shape, form and color in most cases, although they may be slightly opalescent and blue or brown. Teeth may be very mobile and exfoliate spontaneously because of inadequate root formation. On radiographs, the roots are short and may be more pointed than normal. Pulp chambers are usually absent except for a chevron- shaped remnant in the crown. Root canals are usually absent. {ECO:0000269|PubMed:22152679}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;smooth muscle;ovary;sympathetic chain;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;lens;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; uterus;testis - interstitial;adipose tissue;testis - seminiferous tubule;thyroid;testis; 0.09715 0.10694 -0.530852121 20.82448691 113.09937 2.31458 SMOX 0.837563765963898 0.162301150549769 0.000135083486333127 spermine oxidase FUNCTION: Flavoenzyme which catalyzes the oxidation of spermine to spermidine. Can also use N(1)-acetylspermine and spermidine as substrates, with different affinity depending on the isoform (isozyme) and on the experimental conditions. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs. May contribute to beta-alanine production via aldehyde dehydrogenase conversion of 3-amino-propanal.; . TISSUE SPECIFICITY: Widely expressed. Expressed in human tumor cell lines. Isoform 4 is only found in an embryonal kidney cell line. {ECO:0000269|PubMed:18422650}.; myocardium;ovary;colon;parathyroid;skin;bone marrow;retina;uterus;prostate;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;skeletal muscle;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.62240 0.41186 -1.153638777 6.233781552 43.62644 1.25665 SMPD1 4.204719316463e-07 0.593935760897579 0.406063818630489 sphingomyelin phosphodiesterase 1 FUNCTION: Converts sphingomyelin to ceramide. Also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerolphosphoglycerol. Isoform 2 and isoform 3 have lost catalytic activity.; DISEASE: Niemann-Pick disease A (NPDA) [MIM:257200]: An early- onset lysosomal storage disorder caused by failure to hydrolyze sphingomyelin to ceramide. It results in the accumulation of sphingomyelin and other metabolically related lipids in reticuloendothelial and other cell types throughout the body, leading to cell death. Niemann-Pick disease type A is a primarily neurodegenerative disorder characterized by onset within the first year of life, mental retardation, digestive disorders, failure to thrive, major hepatosplenomegaly, and severe neurologic symptoms. The severe neurological disorders and pulmonary infections lead to an early death, often around the age of four. Clinical features are variable. A phenotypic continuum exists between type A (basic neurovisceral) and type B (purely visceral) forms of Niemann-Pick disease, and the intermediate types encompass a cluster of variants combining clinical features of both types A and B. {ECO:0000269|PubMed:12556236, ECO:0000269|PubMed:1391960, ECO:0000269|PubMed:15221801, ECO:0000269|PubMed:15877209, ECO:0000269|PubMed:1618760, ECO:0000269|PubMed:1718266, ECO:0000269|PubMed:19405096, ECO:0000269|PubMed:2023926, ECO:0000269|PubMed:20386867, ECO:0000269|PubMed:8680412, ECO:0000269|PubMed:8693491, ECO:0000269|PubMed:9266408}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Niemann-Pick disease B (NPDB) [MIM:607616]: A late-onset lysosomal storage disorder caused by failure to hydrolyze sphingomyelin to ceramide. It results in the accumulation of sphingomyelin and other metabolically related lipids in reticuloendothelial and other cell types throughout the body, leading to cell death. Clinical signs involve only visceral organs. The most constant sign is hepatosplenomegaly which can be associated with pulmonary symptoms. Patients remain free of neurologic manifestations. However, a phenotypic continuum exists between type A (basic neurovisceral) and type B (purely visceral) forms of Niemann-Pick disease, and the intermediate types encompass a cluster of variants combining clinical features of both types A and B. In Niemann-Pick disease type B, onset of the first symptoms occurs in early childhood and patients can survive into adulthood. {ECO:0000269|PubMed:12369017, ECO:0000269|PubMed:12556236, ECO:0000269|PubMed:1301192, ECO:0000269|PubMed:15241805, ECO:0000269|PubMed:16010684, ECO:0000269|PubMed:1618760, ECO:0000269|PubMed:16472269, ECO:0000269|PubMed:1885770, ECO:0000269|PubMed:19050888, ECO:0000269|PubMed:19405096, ECO:0000269|PubMed:20386867, ECO:0000269|PubMed:22613662, ECO:0000269|PubMed:8051942, ECO:0000269|PubMed:8664904}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;frontal lobe;thyroid;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;mammary gland;stomach;aorta; dorsal root ganglion;parietal lobe; 0.12121 0.41420 1.715972423 96.47912243 1605.7908 7.41831 SMPD2 8.11572389971647e-11 0.0742456282088369 0.925754371710006 sphingomyelin phosphodiesterase 2 FUNCTION: Converts sphingomyelin to ceramide. Hydrolyze 1-acyl-2- lyso-sn-glycero-3-phosphocholine (lyso-PC) and 1-O-alkyl-2-lyso- sn-glycero-3-phosphocholine (lyso-platelet-activating factor). The physiological substrate seems to be Lyso-PAF.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;lung;placenta;macula lutea;liver;duodenum;spleen;kidney;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.07175 0.29293 -0.111973265 45.35857514 1417.90373 7.03838 SMPD3 0.659196149583207 0.340569385020435 0.000234465396358178 sphingomyelin phosphodiesterase 3 FUNCTION: Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization. {ECO:0000269|PubMed:10823942, ECO:0000269|PubMed:14741383, ECO:0000269|PubMed:15051724}.; . TISSUE SPECIFICITY: Predominantly expressed in brain. {ECO:0000269|PubMed:10823942}.; unclassifiable (Anatomical System);ovary;cartilage;colon;blood;fovea centralis;choroid;lens;skin;retina;bone marrow;optic nerve;whole body;lung;frontal lobe;endometrium;bone;macula lutea;iris;testis;brain;mammary gland;stomach; fetal brain;caudate nucleus;atrioventricular node;thymus; 0.35142 0.18303 -0.905656269 10.12031139 287.76451 3.63287 SMPD4 0.00605804578247869 0.993904796897772 3.7157319749434e-05 sphingomyelin phosphodiesterase 4 FUNCTION: Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide. {ECO:0000269|PubMed:16517606}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in heart and skeletal muscle. {ECO:0000269|PubMed:16517606}.; lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;cochlea;thyroid;iris;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;oesophagus;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;hypothalamus;muscle;pancreas;lung;cornea;placenta;duodenum;kidney;stomach; . 0.18735 0.10188 -1.390744555 4.305260675 224.4432 3.23917 SMPD4P1 . . . sphingomyelin phosphodiesterase 4 pseudogene 1 . . . . . . . . . . . SMPD4P2 . . . sphingomyelin phosphodiesterase 4 pseudogene 2 . . . . . . . . . . . SMPD5 . . . sphingomyelin phosphodiesterase 5 . . . . . . . . . . . SMPDL3A 1.66696194609875e-13 0.00384143733862291 0.99615856266121 sphingomyelin phosphodiesterase acid like 3A . . . . . 0.05412 0.12593 0.573279816 82.08303845 942.90931 5.95143 SMPDL3B 1.39140296501713e-07 0.370506146116003 0.629493714743701 sphingomyelin phosphodiesterase acid like 3B . . . . . 0.25447 . -0.021969881 52.14673272 1315.05581 6.81623 SMPX 0.593774441660937 0.366821920222116 0.0394036381169474 small muscle protein, X-linked FUNCTION: Plays a role in the regulatory network through which muscle cells coordinate their structural and functional states during growth, adaptation, and repair. {ECO:0000250}.; DISEASE: Deafness, X-linked, 4 (DFNX4) [MIM:300066]: A non- syndromic form of sensorineural, progressive hearing loss with postlingual onset. In affected males, the auditory impairment affects initially high-frequency hearing. It later evolves to become severe to profound and affects all frequencies. Carrier females manifest moderate hearing impairment in the high frequencies. {ECO:0000269|PubMed:21549336, ECO:0000269|PubMed:21549342, ECO:0000269|PubMed:22911656}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.32297 0.11809 0.013025609 54.62962963 2.75229 0.09837 SMR3A 0.0390546471524191 0.644264895869826 0.316680456977755 submaxillary gland androgen regulated protein 3A FUNCTION: May play a role in protection or detoxification. {ECO:0000250}.; . . lacrimal gland;adrenal gland;thyroid;adrenal cortex;parathyroid;pineal gland; superior cervical ganglion;trachea;salivary gland;appendix;trigeminal ganglion;skeletal muscle; 0.15141 . 0.459411326 78.28497287 104.74732 2.21213 SMR3B 0.536532375027107 0.405340530352184 0.0581270946207092 submaxillary gland androgen regulated protein 3B . . TISSUE SPECIFICITY: Secreted into saliva by submaxillary gland. Not expressed in heart, brain, lung, liver, skeletal muscle, Kidney, pancreas or placenta. {ECO:0000269|PubMed:7982889}.; lung;lacrimal gland;adrenal gland;thyroid;adrenal cortex;duodenum;testis;parathyroid;pineal gland;skeletal muscle; superior cervical ganglion;thalamus;prostate;trachea;salivary gland;thyroid; 0.05432 . 0.035072054 56.2514744 10.11812 0.36897 SMS 0.921460277265947 0.0784406859047961 9.90368292563584e-05 spermine synthase FUNCTION: Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM).; DISEASE: X-linked syndromic mental retardation Snyder-Robinson type (MRXSSR) [MIM:309583]: Characterized by moderate intellectual deficit, hypotonia, an unsteady gait, osteoporosis, kyphoscoliosis and facial asymmetry. Transmission is X-linked recessive. {ECO:0000269|PubMed:14508504, ECO:0000269|PubMed:22612257}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.58047 0.10879 -0.295622497 32.61972163 8.98969 0.33022 SMTN 0.755974257454824 0.244025713539733 2.90054434738289e-08 smoothelin FUNCTION: Structural protein of the cytoskeleton.; . TISSUE SPECIFICITY: Smooth muscle; contractile or vascular (for the long form).; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);heart;cartilage;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve;thymus; uterus;dorsal root ganglion;prostate;superior cervical ganglion;olfactory bulb;appendix;trigeminal ganglion; 0.19027 0.13476 0.431697208 77.32955886 4040.09477 12.59916 SMTNL1 6.40314836984676e-06 0.46338693184653 0.5366066650051 smoothelin-like 1 FUNCTION: Plays a role in the regulation of contractile properties of both striated and smooth muscles. When unphosphorylated, may inhibit myosin dephosphorylation. Phosphorylation at Ser-299 reduces this inhibitory activity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in striated muscles, specifically in type 2a fibers (at protein level). {ECO:0000269|PubMed:18310078, ECO:0000269|PubMed:20634291}.; . . 0.09116 . . . 233.00971 3.30093 SMTNL2 0.00123712384110292 0.850399526001988 0.148363350156909 smoothelin-like 2 . . . unclassifiable (Anatomical System);heart;cartilage;muscle;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;lung;larynx;macula lutea;liver;testis;head and neck;kidney;brain;peripheral nerve; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.15267 . . . 1007.07199 6.11080 SMU1 0.998978044438405 0.00102194440524552 1.11563496353845e-08 smu-1 suppressor of mec-8 and unc-52 homolog (C. elegans) . . . . . 0.19476 0.14163 -0.141298762 42.87567823 5.43983 0.20203 SMUG1 0.00123008785180229 0.849550202508367 0.149219709639831 single-strand-selective monofunctional uracil-DNA glycosylase 1 FUNCTION: Recognizes base lesions in the genome and initiates base excision DNA repair. Acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA with a preference for single-stranded DNA substrates. The activity is greater toward mismatches (U/G) compared to matches (U/A). Excises uracil (U), 5- formyluracil (fU) and uracil derivatives bearing an oxidized group at C5 [5-hydroxyuracil (hoU) and 5-hydroxymethyluracil (hmU)] in ssDNA and dsDNA, but not analogous cytosine derivatives (5- hydroxycytosine and 5-formylcytosine), nor other oxidized bases. The activity is damage-specific and salt-dependent. The substrate preference is the following: ssDNA > dsDNA (G pair) = dsDNA (A pair) at low salt concentration, and dsDNA (G pair) > dsDNA (A pair) > ssDNA at high salt concentration. {ECO:0000269|PubMed:10074426, ECO:0000269|PubMed:11526119, ECO:0000269|PubMed:12161446, ECO:0000269|PubMed:12718543}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;urinary;blood;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; parietal lobe; 0.06953 0.17439 0.082802743 60.09082331 207.22835 3.11048 SMUG1P1 . . . single-strand-selective monofunctional uracil-DNA glycosylase 1 pseudogene 1 . . . . . . . . . . . SMURF1 0.996803391218968 0.0031966084793007 3.0173118458917e-10 SMAD specific E3 ubiquitin protein ligase 1 FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator of BMP signaling pathway. Mediates ubiquitination and degradation of SMAD1 and SMAD5, 2 receptor-regulated SMADs specific for the BMP pathway. Promotes ubiquitination and subsequent proteasomal degradation of TRAF family members and RHOA. Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000269|PubMed:10458166, ECO:0000269|PubMed:19937093, ECO:0000269|PubMed:21402695, ECO:0000269|PubMed:23999003}.; . TISSUE SPECIFICITY: Expressed in melanocytes (PubMed:23999003). {ECO:0000269|PubMed:23999003}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;testis;germinal center;ciliary body;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;bile duct;breast;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.34495 0.16861 -1.375949569 4.393724935 20.01889 0.68296 SMURF2 0.999989890654782 1.01093452117311e-05 5.96976134345769e-15 SMAD specific E3 ubiquitin protein ligase 2 FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD1 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with SCYE1. Forms a stable complex with the TGF-beta receptor-mediated phosphorylated SMAD2 and SMAD3. In this way, SMAD2 may recruit substrates, such as SNON, for ubiquitin-mediated degradation. Enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level. {ECO:0000269|PubMed:11389444, ECO:0000269|PubMed:12717440}.; . TISSUE SPECIFICITY: Widely expressed.; ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;testis; 0.24709 0.18339 -0.690637458 15.12149092 113.88537 2.32671 SMURF2P1 . . . SMAD specific E3 ubiquitin protein ligase 2 pseudogene 1 . . . . . . . . . . . SMYD1 0.000247889682244781 0.924817191018165 0.0749349192995906 SET and MYND domain containing 1 FUNCTION: Methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. Acts as a transcriptional repressor. Essential for cardiomyocyte differentiation and cardiac morphogenesis.; . TISSUE SPECIFICITY: Expression seems mostly restricted to heart and skeletal muscle. {ECO:0000269|PubMed:19783823}.; myocardium;heart;ovary;muscle;parathyroid;skeletal muscle;prostate;whole body;lung;frontal lobe;larynx;placenta;liver;head and neck;mammary gland; . 0.51579 0.09335 -0.198338176 39.17197452 1283.18135 6.74429 SMYD2 0.00536893714935113 0.989356106706156 0.00527495614449246 SET and MYND domain containing 2 FUNCTION: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'. {ECO:0000269|PubMed:17108971, ECO:0000269|PubMed:17805299, ECO:0000269|PubMed:18065756, ECO:0000269|PubMed:20870719, ECO:0000269|PubMed:21782458, ECO:0000269|PubMed:21880715}.; . . . . 0.23384 0.10894 0.352813824 74.49280491 200.10993 3.05629 SMYD3 7.8037496651672e-06 0.913579822036256 0.0864123742140791 SET and MYND domain containing 3 FUNCTION: Histone methyltransferase. Specifically methylates 'Lys- 4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences. {ECO:0000269|PubMed:15235609, ECO:0000269|PubMed:22419068}.; . TISSUE SPECIFICITY: Expressed in skeletal muscles and testis. Overexpressed in a majority of colorectal and hepatocellular carcinomas. {ECO:0000269|PubMed:15235609}.; . . 0.22013 0.11354 -0.314027422 31.9297004 75.60539 1.82050 SMYD3-IT1 . . . SMYD3 intronic transcript 1 . . . . . . . . . . . SMYD4 2.00564150829446e-11 0.118531929239335 0.881468070740608 SET and MYND domain containing 4 . . . ovary;umbilical cord;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;lung;epididymis;adrenal gland;macula lutea;hippocampus;liver;cervix;kidney;mammary gland; . 0.10663 . 1.409099734 94.8041991 11492.10384 23.13601 SMYD5 0.103327058155762 0.895226830788464 0.0014461110557737 SMYD family member 5 . . . smooth muscle;ovary;salivary gland;colon;skin;uterus;optic nerve;whole body;frontal lobe;endometrium;synovium;thyroid;bone;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;urinary;muscle;lens;pancreas;lung;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;prefrontal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.28499 0.10637 -0.049474214 50.01179523 81.2895 1.90919 SNAI1 0.367002590610049 0.621374995112815 0.0116224142771359 snail family zinc finger 1 FUNCTION: Involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration. Binds to 3 E-boxes of the E-cadherin/CDH1 gene promoter and to the promoters of CLDN7 and KRT8 and, in association with histone demethylase KDM1A which it recruits to the promoters, causes a decrease in dimethylated H3K4 levels and represses transcription. Associates with EGR1 and SP1 to mediate tetradecanoyl phorbol acetate (TPA)-induced up- regulation of CDKN2B, possibly by binding to the CDKN2B promoter region 5'-TCACA-3. In addition, may also activate the CDKN2B promoter by itself. {ECO:0000269|PubMed:10655587, ECO:0000269|PubMed:15647282, ECO:0000269|PubMed:16096638, ECO:0000269|PubMed:20121949, ECO:0000269|PubMed:20562920, ECO:0000269|PubMed:21952048}.; . TISSUE SPECIFICITY: Expressed in a variety of tissues with the highest expression in kidney. Expressed in mesenchymal and epithelial cell lines. {ECO:0000269|PubMed:10655587}.; ovary;colon;parathyroid;choroid;fovea centralis;skin;bone marrow;retina;uterus;optic nerve;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;lung;placenta;visual apparatus;macula lutea;alveolus;spleen;kidney;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14554 0.33126 0.082802743 60.09082331 2108.22892 8.45254 SNAI1P1 . . . snail family zinc finger 1 pseudogene 1 . . . . . . . . . . . SNAI2 0.871690015207373 0.126608640914028 0.00170134387859906 snail family zinc finger 2 FUNCTION: Transcriptional repressor that modulates both activator- dependent and basal transcription. Involved in the generation and migration of neural crest cells. Plays a role in mediating RAF1- induced transcriptional repression of the TJ protein, occludin (OCLN) and subsequent oncogenic transformation of epithelial cells (By similarity). Represses BRCA2 expression by binding to its E2- box-containing silencer and recruiting CTBP1 and HDAC1 in breast cells. In epidermal keratinocytes, binds to the E-box in ITGA3 promoter and represses its transcription. Involved in the regulation of ITGB1 and ITGB4 expression and cell adhesion and proliferation in epidermal keratinocytes. Binds to E-box2 domain of BSG and activates its expression during TGFB1-induced epithelial-mesenchymal transition (EMT) in hepatocytes. Represses E-Cadherin/CDH1 transcription via E-box elements. Involved in osteoblast maturation. Binds to RUNX2 and SOC9 promoters and may act as a positive and negative transcription regulator, respectively, in osteoblasts. Binds to CXCL12 promoter via E-box regions in mesenchymal stem cells and osteoblasts. Plays an essential role in TWIST1-induced EMT and its ability to promote invasion and metastasis. {ECO:0000250, ECO:0000269|PubMed:10866665, ECO:0000269|PubMed:11912130, ECO:0000269|PubMed:15734731, ECO:0000269|PubMed:16707493, ECO:0000269|PubMed:19756381, ECO:0000269|PubMed:21182836}.; DISEASE: Waardenburg syndrome 2D (WS2D) [MIM:608890]: WS2 is a genetically heterogeneous, autosomal dominant disorder characterized by sensorineural deafness, pigmentary disturbances, and absence of dystopia canthorum. The frequency of deafness is higher in WS2 than in WS1. {ECO:0000269|PubMed:12444107}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Piebald trait (PBT) [MIM:172800]: Autosomal dominant genetic developmental abnormality of pigmentation characterized by congenital patches of white skin and hair that lack melanocytes. {ECO:0000269|PubMed:12955764}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in most adult human tissues, including spleen, thymus, prostate, testis, ovary, small intestine, colon, heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Not detected in peripheral blood leukocyte. Expressed in the dermis and in all layers of the epidermis, with high levels of expression in the basal layers (at protein level). Expressed in osteoblasts (at protein level). Expressed in mesenchymal stem cells (at protein level). Expressed in breast tumor cells (at protein level). {ECO:0000269|PubMed:10866665, ECO:0000269|PubMed:16707493, ECO:0000269|PubMed:19756381, ECO:0000269|PubMed:21182836}.; myocardium;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland; uterus;lung;adipose tissue; 0.35065 0.32628 -0.09720619 46.20193442 15.08527 0.54183 SNAI3 0.00830565937296694 0.793097398021335 0.198596942605698 snail family zinc finger 3 FUNCTION: Seems to inhibit myoblast differentiation. Transcriptional repressor of E-box-dependent transactivation of downstream myogenic bHLHs genes. Binds preferentially to the canonical E-box sequences 5'-CAGGTG-3' and 5'-CACCTG-3' (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;spleen;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.10099 0.12801 0.955356963 90.10969568 154.07233 2.71336 SNAI3-AS1 . . . SNAI3 antisense RNA 1 . . . . . . . . . . . SNAP23 0.826507888875192 0.172700528444426 0.000791582680381847 synaptosome associated protein 23kDa FUNCTION: Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.; . TISSUE SPECIFICITY: Ubiquitous. Highest levels where found in placenta.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;artery;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;stomach; superior cervical ganglion;subthalamic nucleus;prostate;placenta;ciliary ganglion;white blood cells;atrioventricular node;whole blood;trigeminal ganglion; 0.09542 0.14806 -0.185391282 39.67916962 11.0367 0.39978 SNAP23P . . . synaptosome associated protein 23kDa pseudogene . . . . . . . . . . . SNAP25 0.959806530251926 0.040103400295674 9.00694523999097e-05 synaptosome associated protein 25kDa FUNCTION: t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells. {ECO:0000250|UniProtKB:P60881}.; DISEASE: Myasthenic syndrome, congenital, 18 (CMS18) [MIM:616330]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS18 is an autosomal dominant presynaptic disorder clinically characterized by early-onset muscle weakness and easy fatigability associated with delayed psychomotor development and ataxia. {ECO:0000269|PubMed:25381298}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Neurons of the neocortex, hippocampus, piriform cortex, anterior thalamic nuclei, pontine nuclei, and granule cells of the cerebellum.; sympathetic chain;fovea centralis;choroid;retina;optic nerve;whole body;frontal lobe;cerebral cortex;larynx;pituitary gland;testis;spinal ganglion;pineal gland;brain;unclassifiable (Anatomical System);amygdala;cerebellum cortex;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;lung;adrenal gland;macula lutea;hippocampus;visual apparatus;liver;spleen;head and neck;kidney;cerebellum; whole brain;amygdala;superior cervical ganglion;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;pituitary;parietal lobe;cerebellum; 0.40909 0.39427 -0.009020804 52.8544468 5.91473 0.22255 SNAP25-AS1 . . . SNAP25 antisense RNA 1 . . . . . . . . . . . SNAP29 0.151662054198404 0.831339978594476 0.0169979672071203 synaptosome associated protein 29kDa FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor- attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Plays also a role in ciliogenesis by regulating membrane fusions. {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686250, ECO:0000269|PubMed:25686604}.; . TISSUE SPECIFICITY: Found in brain, heart, kidney, liver, lung, placenta, skeletal muscle, spleen and pancreas. {ECO:0000269|PubMed:9852078}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.03626 0.14629 0.082802743 60.09082331 212.40961 3.14516 SNAP47 0.00030482303703809 0.804002073404554 0.195693103558408 synaptosome associated protein 47kDa FUNCTION: Plays a role in intracellular membrane fusion. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;blood;skin;retina;bone marrow;uterus;pancreas;prostate;lung;cerebral cortex;placenta;visual apparatus;liver;testis;brain; dorsal root ganglion;superior cervical ganglion;testis - interstitial;subthalamic nucleus;testis;globus pallidus;ciliary ganglion;caudate nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12147 0.09737 0.755110637 86.7539514 3522.91312 11.44576 SNAP47-AS1 . . . SNAP47 antisense RNA 1 . . . . . . . . . . . SNAP91 0.974350743810835 0.0256490103489074 2.45840257675113e-07 synaptosome associated protein 91kDa FUNCTION: Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia induces their assembly into 60-70 nm coats (By similarity). {ECO:0000250}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;substantia nigra;parathyroid;fovea centralis;skin;retina;uterus;subthalamic nucleus;prostate;whole body;frontal lobe;pituitary gland;testis;bladder;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;lung;macula lutea;visual apparatus;hippocampus;liver;kidney;aorta;cerebellum; amygdala;whole brain;dorsal root ganglion;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.70065 0.14708 -0.573127851 18.96083982 123.20471 2.41719 SNAPC1 3.82492140215155e-07 0.57326608607509 0.42673353143277 small nuclear RNA activating complex polypeptide 1 FUNCTION: Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box. {ECO:0000269|PubMed:12621023}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;thyroid;bone;iris;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;pharynx;blood;skeletal muscle;breast;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.18554 0.10509 -0.003562597 53.72729417 438.18022 4.36411 SNAPC2 0.10316814001529 0.864335780108379 0.0324960798763316 small nuclear RNA activating complex polypeptide 2 FUNCTION: Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box.; . . medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; testis;skeletal muscle;cingulate cortex;parietal lobe; 0.06609 0.09723 0.396906589 76.30927105 3321.54892 11.01553 SNAPC3 5.53901197607186e-05 0.883341296170842 0.116603313709398 small nuclear RNA activating complex polypeptide 3 FUNCTION: Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box. {ECO:0000269|PubMed:12621023}.; . . . . 0.17643 0.10767 -0.069700724 48.54328851 386.09549 4.13838 SNAPC4 2.00808955575167e-21 0.0404848754255853 0.959515124574415 small nuclear RNA activating complex polypeptide 4 FUNCTION: Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box. {ECO:0000269|PubMed:12621023, ECO:0000269|PubMed:9418884}.; . . unclassifiable (Anatomical System);colon;skeletal muscle;skin;uterus;lung;endometrium;placenta;visual apparatus;testis;kidney;mammary gland;brain;stomach;peripheral nerve; superior cervical ganglion;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.08543 0.08504 0.315838028 72.76480302 4352.03325 13.15433 SNAPC5 1.40204453241569e-05 0.125603911120239 0.874382068434436 small nuclear RNA activating complex polypeptide 5 FUNCTION: Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;thyroid;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;macula lutea;liver;alveolus;head and neck;cervix;kidney;stomach; atrioventricular node;skeletal muscle;cingulate cortex; 0.08216 0.11262 -0.09720619 46.20193442 24.24987 0.79777 SNAPC5P1 . . . small nuclear RNA activating complex polypeptide 5 pseudogene 1 . . . . . . . . . . . SNAPIN 3.04880662881494e-05 0.340716102384165 0.659253409549546 SNAP associated protein FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking and synaptic vesicle recycling. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs and the plasma- membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE-mediated membrane fusion in non-neuronal cells. {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:18167355}.; . TISSUE SPECIFICITY: Expressed in male germ cells of adult testis (at protein level). {ECO:0000269|PubMed:19168546}.; . . 0.26343 0.15544 0.013025609 54.62962963 12.51052 0.45516 SNAR-A1 . . . small ILF3/NF90-associated RNA A1 . . . . . . . . . . . SNAR-A2 . . . small ILF3/NF90-associated RNA A2 . . . . . . . . . . . SNAR-A3 . . . small ILF3/NF90-associated RNA A3 . . . . . . . . . . . SNAR-A4 . . . small ILF3/NF90-associated RNA A4 . . . . . . . . . . . SNAR-A5 . . . small ILF3/NF90-associated RNA A5 . . . . . . . . . . . SNAR-A6 . . . small ILF3/NF90-associated RNA A6 . . . . . . . . . . . SNAR-A7 . . . small ILF3/NF90-associated RNA A7 . . . . . . . . . . . SNAR-A8 . . . small ILF3/NF90-associated RNA A8 . . . . . . . . . . . SNAR-A9 . . . small ILF3/NF90-associated RNA A9 . . . . . . . . . . . SNAR-A10 . . . small ILF3/NF90-associated RNA A10 . . . . . . . . . . . SNAR-A11 . . . small ILF3/NF90-associated RNA A11 . . . . . . . . . . . SNAR-A12 . . . small ILF3/NF90-associated RNA A12 . . . . . . . . . . . SNAR-A13 . . . small ILF3/NF90-associated RNA A13 . . . . . . . . . . . SNAR-A14 . . . small ILF3/NF90-associated RNA A14 . . . . . . . . . . . SNAR-B1 . . . small ILF3/NF90-associated RNA B1 . . . . . . . . . . . SNAR-B2 . . . small ILF3/NF90-associated RNA B2 . . . . . . . . . . . SNAR-C1 . . . small ILF3/NF90-associated RNA C1 . . . . . . . . . . . SNAR-C2 . . . small ILF3/NF90-associated RNA C2 . . . . . . . . . . . SNAR-C3 . . . small ILF3/NF90-associated RNA C3 . . . . . . . . . . . SNAR-C4 . . . small ILF3/NF90-associated RNA C4 . . . . . . . . . . . SNAR-C5 . . . small ILF3/NF90-associated RNA C5 . . . . . . . . . . . SNAR-D . . . small ILF3/NF90-associated RNA D . . . . . . . . . . . SNAR-E . . . small ILF3/NF90-associated RNA E . . . . . . . . . . . SNAR-F . . . small ILF3/NF90-associated RNA F . . . . . . . . . . . SNAR-G1 . . . small ILF3/NF90-associated RNA G1 . . . . . . . . . . . SNAR-G2 . . . small ILF3/NF90-associated RNA G2 . . . . . . . . . . . SNAR-H . . . small ILF3/NF90-associated RNA H . . . . . . . . . . . SNAR-I . . . small ILF3/NF90-associated RNA I . . . . . . . . . . . SNCA 0.841962359247494 0.155105523132447 0.00293211762005937 synuclein alpha FUNCTION: May be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation.; DISEASE: Note=Genetic alterations of SNCA resulting in aberrant polymerization into fibrils, are associated with several neurodegenerative diseases (synucleinopathies). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer disease amyloid plaque, and a major component of Lewy body inclusions. They are also found within Lewy body (LB)-like intraneuronal inclusions, glial inclusions and axonal spheroids in neurodegeneration with brain iron accumulation type 1.; DISEASE: Parkinson disease 1 (PARK1) [MIM:168601]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features. {ECO:0000269|PubMed:23427326, ECO:0000269|PubMed:23457019, ECO:0000269|PubMed:24936070, ECO:0000269|PubMed:25561023, ECO:0000269|PubMed:9197268, ECO:0000269|PubMed:9462735}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Parkinson disease 4 (PARK4) [MIM:605543]: A complex neurodegenerative disorder with manifestations ranging from typical Parkinson disease to dementia with Lewy bodies. Clinical features include parkinsonian symptoms (resting tremor, rigidity, postural instability and bradykinesia), dementia, diffuse Lewy body pathology, autonomic dysfunction, hallucinations and paranoia. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dementia Lewy body (DLB) [MIM:127750]: A neurodegenerative disorder characterized by mental impairment leading to dementia, parkinsonism, fluctuating cognitive function, visual hallucinations, falls, syncopal episodes, and sensitivity to neuroleptic medication. Brainstem or cortical intraneuronal accumulations of aggregated proteins (Lewy bodies) are the only essential pathologic features. Patients may also have hippocampal and neocortical senile plaques, sometimes in sufficient number to fulfill the diagnostic criteria for Alzheimer disease. {ECO:0000269|PubMed:14755719}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals.; myocardium;ovary;salivary gland;colon;skin;uterus;prostate;whole body;frontal lobe;endometrium;bone;iris;testis;brain;bladder;amygdala;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pharynx;blood;breast;lung;adrenal gland;placenta;visual apparatus;liver;duodenum;spleen;kidney;mammary gland; amygdala;whole brain;dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;olfactory bulb;temporal lobe;atrioventricular node;pons;skin;bone marrow;subthalamic nucleus;fetal liver;prefrontal cortex;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.72490 0.41559 -0.141298762 42.87567823 15.72468 0.55998 SNCA-AS1 . . . SNCA antisense RNA 1 . . . . . . . . . . . SNCAIP 0.000362967804998999 0.997503410514767 0.00213362168023411 synuclein alpha interacting protein FUNCTION: Isoform 2 inhibits the ubiquitin ligase activity of SIAH1 and inhibits proteasomal degradation of target proteins. Isoform 2 inhibits autoubiquitination and proteasomal degradation of SIAH1, and thereby increases cellular levels of SIAH. Isoform 2 modulates SNCA monoubiquitination by SIAH1. {ECO:0000269|PubMed:16595633, ECO:0000269|PubMed:19224863}.; DISEASE: Parkinson disease (PARK) [MIM:168600]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features. {ECO:0000269|PubMed:12761037}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in brain (at protein level). Widely expressed, with highest levels in brain, heart and placenta. {ECO:0000269|PubMed:10319874, ECO:0000269|PubMed:16595633}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;skin;skeletal muscle;uterus;prostate;whole body;lung;cochlea;larynx;visual apparatus;liver;testis;head and neck;spleen;germinal center;spinal ganglion;brain; dorsal root ganglion;uterus;superior cervical ganglion;uterus corpus;fetal brain;ciliary ganglion;pons;caudate nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.27004 0.17052 0.227815529 68.53621137 181.93499 2.93022 SNCB 0.198196528468429 0.75636252188956 0.0454409496420113 synuclein beta FUNCTION: Non-amyloid component of senile plaques found in Alzheimer disease. Could act as a regulator of SNCA aggregation process. Protects neurons from staurosporine and 6-hydroxy dopamine (6OHDA)-stimulated caspase activation in a p53/TP53- dependent manner. Contributes to restore the SNCA anti-apoptotic function abolished by 6OHDA. Not found in the Lewy bodies associated with Parkinson disease.; . TISSUE SPECIFICITY: Expressed predominantly in brain; concentrated in presynaptic nerve terminals.; unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;frontal lobe;macula lutea;hippocampus;testis;pineal gland;brain; amygdala;whole brain;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.48937 0.22085 -0.053113545 49.38664779 7.13977 0.26743 SNCG 0.382299480507148 0.57319946529554 0.0445010541973125 synuclein gamma FUNCTION: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases (By similarity). May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in brain, particularly in the substantia nigra. Also expressed in the corpus callosum, heart, skeletal muscle, ovary, testis, colon and spleen. Weak expression in pancreas, kidney and lung.; ovary;salivary gland;intestine;colon;substantia nigra;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;whole brain;amygdala;occipital lobe;thalamus;temporal lobe;spinal cord;subthalamic nucleus;adrenal gland;prefrontal cortex;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.37625 0.11337 1.014235724 90.84100024 958.38204 5.99183 SND1 0.999917088790426 8.2911209532693e-05 4.11400855729847e-14 staphylococcal nuclease and tudor domain containing 1 FUNCTION: Functions as a bridging factor between STAT6 and the basal transcription factor. Plays a role in PIM1 regulation of MYB activity. Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2). {ECO:0000269|PubMed:7651391}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:7651391}.; lymphoreticular;ovary;sympathetic chain;colon;skin;retina;bone marrow;uterus;prostate;cerebral cortex;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;spinal cord;muscle;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;adrenal gland;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.73895 0.12655 -1.063626766 7.484076433 188.34653 2.98065 SND1-IT1 . . . SND1 intronic transcript 1 . . . . . . . . . . . SNED1 0.983762810114589 0.0162371897519464 1.33464568364101e-10 sushi, nidogen and EGF like domains 1 . . . lymphoreticular;smooth muscle;ovary;salivary gland;sympathetic chain;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - interstitial;adipose tissue;olfactory bulb;temporal lobe;caudate nucleus;pons;atrioventricular node;fetal thyroid;skeletal muscle;skin;uterus corpus;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;cerebellum; 0.22403 0.13286 -1.379925048 4.364236848 4194.17391 12.86144 SNF8 0.290873868173922 0.704665233039881 0.00446089878619672 SNF8, ESCRT-II complex subunit FUNCTION: Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. The ESCRT-II complex may also play a role in transcription regulation by participating in derepression of transcription by RNA polymerase II, possibly via its interaction with ELL. Required for degradation of both endocytosed EGF and EGFR, but not for the EGFR ligand-mediated internalization. It is also required for the degradation of CXCR4. {ECO:0000269|PubMed:17714434, ECO:0000269|PubMed:17959629, ECO:0000269|PubMed:18031739}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;iris;amniotic fluid;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;pineal body;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion; 0.22987 0.11233 -0.339715008 30.06605331 8.64004 0.31754 SNHG1 . . . small nucleolar RNA host gene 1 . . . . . . . . . . . SNHG3 . . . small nucleolar RNA host gene 3 . . . . . . . . . . . SNHG4 . . . small nucleolar RNA host gene 4 . . . . . . . . . . . SNHG5 . . . small nucleolar RNA host gene 5 . . . . . . . . . . . SNHG6 . . . small nucleolar RNA host gene 6 . . . . . . . . . . . SNHG7 . . . small nucleolar RNA host gene 7 . . . . . . . . . . . SNHG8 . . . small nucleolar RNA host gene 8 . . . . . . . . . . . SNHG9 . . . small nucleolar RNA host gene 9 . . . . . . . . . . . SNHG10 . . . small nucleolar RNA host gene 10 . . . . . . . . . . . SNHG11 . . . small nucleolar RNA host gene 11 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;testis;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;urinary;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.06943 . . . . . SNHG12 . . . small nucleolar RNA host gene 12 . . . . . 0.06447 . . . . . SNHG14 . . . small nucleolar RNA host gene 14 . . . . . . . . . . . SNHG15 . . . small nucleolar RNA host gene 15 . . . . . . . . . . . SNHG16 . . . small nucleolar RNA host gene 16 . . . . . 0.56271 . . . . . SNHG17 . . . small nucleolar RNA host gene 17 . . . . . . . . . . . SNHG18 . . . small nucleolar RNA host gene 18 . . . . . . . . . . . SNHG19 . . . small nucleolar RNA host gene 19 . . . . . . . . . . . SNHG20 . . . small nucleolar RNA host gene 20 . . . . . . . . . . . SNHG21 . . . small nucleolar RNA host gene 21 . . . . . . . . . . . SNHG22 . . . small nucleolar RNA host gene 22 . . . . . . . . . . . SNHG23 . . . small nucleolar RNA host gene 23 . . . . . . . . . . . SNHG24 . . . small nucleolar RNA host gene 24 . . . . . . . . . . . SNHG25 . . . small nucleolar RNA host gene 25 . . . . . . . . . . . SNIP1 0.905058048773074 0.0949092401912648 3.27110356615867e-05 Smad nuclear interacting protein 1 FUNCTION: Down-regulates NF-kappa-B signaling by competing with RELA for CREBBP/EP300 binding. Involved in the microRNA (miRNA) biogenesis. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269|PubMed:11567019, ECO:0000269|PubMed:15378006, ECO:0000269|PubMed:18632581, ECO:0000269|PubMed:18794151}.; DISEASE: Psychomotor retardation, epilepsy, and craniofacial dysmorphism (PMRED) [MIM:614501]: A disease characterized by severe psychomotor retardation, intractable seizures, dysmorphic features, and a lumpy skull surface. Patients are hypotonic and have poor feeding in the neonatal period. {ECO:0000269|PubMed:22279524}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart and skeletal muscle. {ECO:0000269|PubMed:10887155}.; medulla oblongata;colon;fovea centralis;choroid;vein;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;urinary;lens;bile duct;lung;placenta;macula lutea;peripheral nerve; globus pallidus; 0.61682 0.09732 0.128714042 63.19886766 88.17055 2.01066 SNN 0.0202490590604754 0.512962007758029 0.466788933181495 stannin FUNCTION: Plays a role in the toxic effects of organotins.; . . smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;iris;amniotic fluid;germinal center;bladder;brain;amygdala;heart;cartilage;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus; amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.11141 0.12378 -0.075159878 47.78839349 . . SNORA1 . . . small nucleolar RNA, H/ACA box 1 . . . . . . . . . . . SNORA2A . . . small nucleolar RNA, H/ACA box 2A . . . . . . . . . . . SNORA2B . . . small nucleolar RNA, H/ACA box 2B . . . . . . . . . . . SNORA2C . . . small nucleolar RNA, H/ACA box 2C . . . . . . . . . . . SNORA3A . . . small nucleolar RNA, H/ACA box 3A . . . . . . . . . . . SNORA3B . . . small nucleolar RNA, H/ACA box 3B . . . . . . . . . . . SNORA4 . . . small nucleolar RNA, H/ACA box 4 . . . . . . . . . . . SNORA5A . . . small nucleolar RNA, H/ACA box 5A . . . . . . . . . . . SNORA5B . . . small nucleolar RNA, H/ACA box 5B . . . . . . . . . . . SNORA5C . . . small nucleolar RNA, H/ACA box 5C . . . . . . . . . . . SNORA6 . . . small nucleolar RNA, H/ACA box 6 . . . . . . . . . . . SNORA7A . . . small nucleolar RNA, H/ACA box 7A . . . . . . . . . . . SNORA7B . . . small nucleolar RNA, H/ACA box 7B . . . . . . . . . . . SNORA8 . . . small nucleolar RNA, H/ACA box 8 . . . . . . . . . . . SNORA9 . . . small nucleolar RNA, H/ACA box 9 . . . . . . . . . . . SNORA10 . . . small nucleolar RNA, H/ACA box 10 . . . . . . . . . . . SNORA11 . . . small nucleolar RNA, H/ACA box 11 . . . . . . . . . . . SNORA11B . . . small nucleolar RNA, H/ACA box 11B . . . . . . . . . . . SNORA11C . . . small nucleolar RNA, H/ACA box 11C . . . . . . . . . . . SNORA11D . . . small nucleolar RNA, H/ACA box 11D . . . . . . . . . . . SNORA11E . . . small nucleolar RNA, H/ACA box 11E . . . . . . . . . . . SNORA12 . . . small nucleolar RNA, H/ACA box 12 . . . . . . . . . . . SNORA13 . . . small nucleolar RNA, H/ACA box 13 . . . . . . . . . . . SNORA14A . . . small nucleolar RNA, H/ACA box 14A . . . . . . . . . . . SNORA14B . . . small nucleolar RNA, H/ACA box 14B . . . . . . . . . . . SNORA15 . . . small nucleolar RNA, H/ACA box 15 . . . . . . . . . . . SNORA16A . . . small nucleolar RNA, H/ACA box 16A . . . . . . . . . . . SNORA16B . . . small nucleolar RNA, H/ACA box 16B . . . . . . . . . . . SNORA17A . . . small nucleolar RNA, H/ACA box 17A . . . . . . . . . . . SNORA17B . . . small nucleolar RNA, H/ACA box 17B . . . . . . . . . . . SNORA18 . . . small nucleolar RNA, H/ACA box 18 . . . . . . . . . . . SNORA19 . . . small nucleolar RNA, H/ACA box 19 . . . . . . . . . . . SNORA20 . . . small nucleolar RNA, H/ACA box 20 . . . . . . . . . . . SNORA21 . . . small nucleolar RNA, H/ACA box 21 . . . . . . . . . . . SNORA22 . . . small nucleolar RNA, H/ACA box 22 . . . . . . . . . . . SNORA23 . . . small nucleolar RNA, H/ACA box 23 . . . . . . . . . . . SNORA24 . . . small nucleolar RNA, H/ACA box 24 . . . . . . . . . . . SNORA25 . . . small nucleolar RNA, H/ACA box 25 . . . . . . . . . . . SNORA26 . . . small nucleolar RNA, H/ACA box 26 . . . . . . . . . . . SNORA27 . . . small nucleolar RNA, H/ACA box 27 . . . . . . . . . . . SNORA28 . . . small nucleolar RNA, H/ACA box 28 . . . . . . . . . . . SNORA29 . . . small nucleolar RNA, H/ACA box 29 . . . . . . . . . . . SNORA30 . . . small nucleolar RNA, H/ACA box 30 . . . . . . . . . . . SNORA31 . . . small nucleolar RNA, H/ACA box 31 . . . . . . . . . . . SNORA32 . . . small nucleolar RNA, H/ACA box 32 . . . . . . . . . . . SNORA33 . . . small nucleolar RNA, H/ACA box 33 . . . . . . . . . . . SNORA35 . . . small nucleolar RNA, H/ACA box 35 . . . . . . . . . . . SNORA36A . . . small nucleolar RNA, H/ACA box 36A . . . . . . . . . . . SNORA36B . . . small nucleolar RNA, H/ACA box 36B . . . . . . . . . . . SNORA36C . . . small nucleolar RNA, H/ACA box 36C . . . . . . . . . . . SNORA37 . . . small nucleolar RNA, H/ACA box 37 . . . . . . . . . . . SNORA38 . . . small nucleolar RNA, H/ACA box 38 . . . . . . . . . . . SNORA38B . . . small nucleolar RNA, H/ACA box 38B . . . . . . . . . . . SNORA40 . . . small nucleolar RNA, H/ACA box 40 . . . . . . . . . . . SNORA41 . . . small nucleolar RNA, H/ACA box 41 . . . . . . . . . . . SNORA44 . . . small nucleolar RNA, H/ACA box 44 . . . . . . . . . . . SNORA46 . . . small nucleolar RNA, H/ACA box 46 . . . . . . . . . . . SNORA47 . . . small nucleolar RNA, H/ACA box 47 . . . . . . . . . . . SNORA48 . . . small nucleolar RNA, H/ACA box 48 . . . . . . . . . . . SNORA49 . . . small nucleolar RNA, H/ACA box 49 . . . . . . . . . . . SNORA50A . . . small nucleolar RNA, H/ACA box 50A . . . . . . . . . . . SNORA50C . . . small nucleolar RNA, H/ACA box 50C . . . . . . . . . . . SNORA51 . . . small nucleolar RNA, H/ACA box 51 . . . . . . . . . . . SNORA52 . . . small nucleolar RNA, H/ACA box 52 . . . . . . . . . . . SNORA53 . . . small nucleolar RNA, H/ACA box 53 . . . . . . . . . . . SNORA54 . . . small nucleolar RNA, H/ACA box 54 . . . . . . . . . . . SNORA55 . . . small nucleolar RNA, H/ACA box 55 . . . . . . . . . . . SNORA56 . . . small nucleolar RNA, H/ACA box 56 . . . . . . . . . . . SNORA57 . . . small nucleolar RNA, H/ACA box 57 . . . . . . . . . . . SNORA58 . . . small nucleolar RNA, H/ACA box 58 . . . . . . . . . . . SNORA59A . . . small nucleolar RNA, H/ACA box 59A . . . . . . . . . . . SNORA59B . . . small nucleolar RNA, H/ACA box 59B . . . . . . . . . . . SNORA60 . . . small nucleolar RNA, H/ACA box 60 . . . . . . . . . . . SNORA61 . . . small nucleolar RNA, H/ACA box 61 . . . . . . . . . . . SNORA62 . . . small nucleolar RNA, H/ACA box 62 . . . . . . . . . . . SNORA63 . . . small nucleolar RNA, H/ACA box 63 . . . . . . . . . . . SNORA64 . . . small nucleolar RNA, H/ACA box 64 . . . . . . . . . . . SNORA65 . . . small nucleolar RNA, H/ACA box 65 . . . . . . . . . . . SNORA66 . . . small nucleolar RNA, H/ACA box 66 . . . . . . . . . . . SNORA67 . . . small nucleolar RNA, H/ACA box 67 . . . . . . . . . . . SNORA68 . . . small nucleolar RNA, H/ACA box 68 . . . . . . . . . . . SNORA69 . . . small nucleolar RNA, H/ACA box 69 . . . . . . . . . . . SNORA70 . . . small nucleolar RNA, H/ACA box 70 . . . . . . . . . . . SNORA70B . . . small nucleolar RNA, H/ACA box 70B . . . . . . . . . . . SNORA70C . . . small nucleolar RNA, H/ACA box 70C . . . . . . . . . . . SNORA70D . . . small nucleolar RNA, H/ACA box 70D . . . . . . . . . . . SNORA70E . . . small nucleolar RNA, H/ACA box 70E . . . . . . . . . . . SNORA70F . . . small nucleolar RNA, H/ACA box 70F . . . . . . . . . . . SNORA70G . . . small nucleolar RNA, H/ACA box 70G . . . . . . . . . . . SNORA71A . . . small nucleolar RNA, H/ACA box 71A . . . . . . . . . . . SNORA71B . . . small nucleolar RNA, H/ACA box 71B . . . . . . . . . . . SNORA71C . . . small nucleolar RNA, H/ACA box 71C . . . . . . . . . . . SNORA71D . . . small nucleolar RNA, H/ACA box 71D . . . . . . . . . . . SNORA71E . . . small nucleolar RNA, H/ACA box 71E . . . . . . . . . . . SNORA72 . . . small nucleolar RNA, H/ACA box 72 . . . . . . . . . . . SNORA73A . . . small nucleolar RNA, H/ACA box 73A . . . . . . . . . . . SNORA73B . . . small nucleolar RNA, H/ACA box 73B . . . . . . . . . . . SNORA74A . . . small nucleolar RNA, H/ACA box 74A . . . . . . . . . . . SNORA74B . . . small nucleolar RNA, H/ACA box 74B . . . . . . . . . . . SNORA75 . . . small nucleolar RNA, H/ACA box 75 . . . . . . . . . . . SNORA77 . . . small nucleolar RNA, H/ACA box 77 . . . . . . . . . . . SNORA78 . . . small nucleolar RNA, H/ACA box 78 . . . . . . . . . . . SNORA79 . . . small nucleolar RNA, H/ACA box 79 . . . . . . . . . . . SNORA80A . . . small nucleolar RNA, H/ACA box 80A . . . . . . . . . . . SNORA80B . . . small nucleolar RNA, H/ACA box 80B . . . . . . . . . . . SNORA80E . . . small nucleolar RNA, H/ACA box 80E . . . . . . . . . . . SNORA81 . . . small nucleolar RNA, H/ACA box 81 . . . . . . . . . . . SNORA84 . . . small nucleolar RNA, H/ACA box 84 . . . . . . . . . . . SNORA86 . . . small nucleolar RNA, H/ACA box 86 . . . . . . . . . . . SNORA87 . . . small nucleolar RNA, H/ACA box 87 . . . . . . . . . . . SNORA88 . . . small nucleolar RNA, H/ACA box 88 . . . . . . . . . . . SNORA89 . . . small nucleolar RNA, H/ACA box 89 . . . . . . . . . . . SNORA90 . . . small nucleolar RNA, H/ACA box 90 . . . . . . . . . . . SNORA91 . . . small nucleolar RNA, H/ACA box 91 . . . . . . . . . . . SNORA92 . . . small nucleolar RNA, H/ACA box 92 . . . . . . . . . . . SNORA93 . . . small nucleolar RNA, H/ACA box 93 . . . . . . . . . . . SNORA94 . . . small nucleolar RNA, H/ACA box 94 . . . . . . . . . . . SNORA95 . . . small nucleolar RNA, H/ACA box 95 . . . . . . . . . . . SNORA98 . . . small nucleolar RNA, H/ACA box 98 . . . . . . . . . . . SNORA99 . . . small nucleolar RNA, H/ACA box 99 . . . . . . . . . . . SNORA100 . . . small nucleolar RNA, H/ACA box 100 . . . . . . . . . . . SNORA101A . . . small nucleolar RNA, H/ACA box 101A . . . . . . . . . . . SNORA101B . . . small nucleolar RNA, H/ACA box 101B . . . . . . . . . . . SNORA103 . . . small nucleolar RNA, H/ACA box 103 . . . . . . . . . . . SNORA104 . . . small nucleolar RNA, H/ACA box 104 . . . . . . . . . . . SNORA105A . . . small nucleolar RNA, H/ACA box 105A . . . . . . . . . . . SNORA105B . . . small nucleolar RNA, H/ACA box 105B . . . . . . . . . . . SNORA105C . . . small nucleolar RNA, H/ACA box 105C . . . . . . . . . . . SNORA107 . . . small nucleolar RNA, H/ACA box 107 . . . . . . . . . . . SNORA108 . . . small nucleolar RNA, H/ACA box 108 . . . . . . . . . . . SNORA109 . . . small nucleolar RNA, H/ACA box 109 . . . . . . . . . . . SNORA110 . . . small nucleolar RNA, H/ACA box 110 . . . . . . . . . . . SNORA111 . . . small nucleolar RNA, H/ACA box 111 . . . . . . . . . . . SNORA112 . . . small nucleolar RNA, H/ACA box 112 . . . . . . . . . . . SNORA113 . . . small nucleolar RNA, H/ACA box 113 . . . . . . . . . . . SNORA114 . . . small nucleolar RNA, H/ACA box 114 . . . . . . . . . . . SNORA115 . . . small nucleolar RNA, H/ACA box 115 . . . . . . . . . . . SNORA116 . . . small nucleolar RNA, H/ACA box 116 . . . . . . . . . . . SNORA117 . . . small nucleolar RNA, H/ACA box 117 . . . . . . . . . . . SNORA118 . . . small nucleolar RNA, H/ACA box 118 . . . . . . . . . . . SNORA119 . . . small nucleolar RNA, H/ACA box 119 . . . . . . . . . . . SNORA120 . . . small nucleolar RNA, H/ACA box 120 . . . . . . . . . . . SNORD1A . . . small nucleolar RNA, C/D box 1A . . . . . . . . . . . SNORD1B . . . small nucleolar RNA, C/D box 1B . . . . . . . . . . . SNORD1C . . . small nucleolar RNA, C/D box 1C . . . . . . . . . . . SNORD2 . . . small nucleolar RNA, C/D box 2 . . . . . . . . . . . SNORD3@ . . . small nucleolar RNA, C/D box 3 cluster . . . . . . . . . . . SNORD3A . . . small nucleolar RNA, C/D box 3A . . . . . . . . . . . SNORD3B-1 . . . small nucleolar RNA, C/D box 3B-1 . . . . . . . . . . . SNORD3B-2 . . . small nucleolar RNA, C/D box 3B-2 . . . . . . . . . . . SNORD3C . . . small nucleolar RNA, C/D box 3C . . . . . . . . . . . SNORD3D . . . small nucleolar RNA, C/D box 3D . . . . . . . . . . . SNORD4A . . . small nucleolar RNA, C/D box 4A . . . . . . . . . . . SNORD4B . . . small nucleolar RNA, C/D box 4B . . . . . . . . . . . SNORD5 . . . small nucleolar RNA, C/D box 5 . . . . . . . . . . . SNORD6 . . . small nucleolar RNA, C/D box 6 . . . . . . . . . . . SNORD7 . . . small nucleolar RNA, C/D box 7 . . . . . . . . . . . SNORD8 . . . small nucleolar RNA, C/D box 8 . . . . . . . . . . . SNORD9 . . . small nucleolar RNA, C/D box 9 . . . . . . . . . . . SNORD10 . . . small nucleolar RNA, C/D box 10 . . . . . . . . . . . SNORD11 . . . small nucleolar RNA, C/D box 11 . . . . . . . . . . . SNORD11B . . . small nucleolar RNA, C/D box 11B . . . . . . . . . . . SNORD12 . . . small nucleolar RNA, C/D box 12 . . . . . . . . . . . SNORD12B . . . small nucleolar RNA, C/D box 12B . . . . . . . . . . . SNORD12C . . . small nucleolar RNA, C/D box 12C . . . . . . . . . . . SNORD13 . . . small nucleolar RNA, C/D box 13 . . . . . . . . . . . SNORD13P1 . . . small nucleolar RNA, C/D box 13 pseudogene 1 . . . . . . . . . . . SNORD13P2 . . . small nucleolar RNA, C/D box 13 pseudogene 2 . . . . . . . . . . . SNORD13P3 . . . small nucleolar RNA, C/D box 13 pseudogene 3 . . . . . . . . . . . SNORD14A . . . small nucleolar RNA, C/D box 14A . . . . . . . . . . . SNORD14B . . . small nucleolar RNA, C/D box 14B . . . . . . . . . . . SNORD14C . . . small nucleolar RNA, C/D box 14C . . . . . . . . . . . SNORD14D . . . small nucleolar RNA, C/D box 14D . . . . . . . . . . . SNORD14E . . . small nucleolar RNA, C/D box 14E . . . . . . . . . . . SNORD15A . . . small nucleolar RNA, C/D box 15A . . . . . . . . . . . SNORD15B . . . small nucleolar RNA, C/D box 15B . . . . . . . . . . . SNORD16 . . . small nucleolar RNA, C/D box 16 . . . . . . . . . . . SNORD17 . . . small nucleolar RNA, C/D box 17 . . . . . . . . . . . SNORD18A . . . small nucleolar RNA, C/D box 18A . . . . . . . . . . . SNORD18B . . . small nucleolar RNA, C/D box 18B . . . . . . . . . . . SNORD18C . . . small nucleolar RNA, C/D box 18C . . . . . . . . . . . SNORD19 . . . small nucleolar RNA, C/D box 19 . . . . . . . . . . . SNORD19B . . . small nucleolar RNA, C/D box 19B . . . . . . . . . . . SNORD20 . . . small nucleolar RNA, C/D box 20 . . . . . . . . . . . SNORD21 . . . small nucleolar RNA, C/D box 21 . . . . . . . . . . . SNORD22 . . . small nucleolar RNA, C/D box 22 . . . . . . . . . . . SNORD23 . . . small nucleolar RNA, C/D box 23 . . . . . . . . . . . SNORD24 . . . small nucleolar RNA, C/D box 24 . . . . . . . . . . . SNORD25 . . . small nucleolar RNA, C/D box 25 . . . . . . . . . . . SNORD26 . . . small nucleolar RNA, C/D box 26 . . . . . . . . . . . SNORD27 . . . small nucleolar RNA, C/D box 27 . . . . . . . . . . . SNORD28 . . . small nucleolar RNA, C/D box 28 . . . . . . . . . . . SNORD29 . . . small nucleolar RNA, C/D box 29 . . . . . . . . . . . SNORD30 . . . small nucleolar RNA, C/D box 30 . . . . . . . . . . . SNORD31 . . . small nucleolar RNA, C/D box 31 . . . . . . . . . . . SNORD32A . . . small nucleolar RNA, C/D box 32A . . . . . . . . . . . SNORD32B . . . small nucleolar RNA, C/D box 32B . . . . . . . . . . . SNORD33 . . . small nucleolar RNA, C/D box 33 . . . . . . . . . . . SNORD34 . . . small nucleolar RNA, C/D box 34 . . . . . . . . . . . SNORD35A . . . small nucleolar RNA, C/D box 35A . . . . . . . . . . . SNORD35B . . . small nucleolar RNA, C/D box 35B . . . . . . . . . . . SNORD36A . . . small nucleolar RNA, C/D box 36A . . . . . . . . . . . SNORD36B . . . small nucleolar RNA, C/D box 36B . . . . . . . . . . . SNORD36C . . . small nucleolar RNA, C/D box 36C . . . . . . . . . . . SNORD37 . . . small nucleolar RNA, C/D box 37 . . . . . . . . . . . SNORD38A . . . small nucleolar RNA, C/D box 38A . . . . . . . . . . . SNORD38B . . . small nucleolar RNA, C/D box 38B . . . . . . . . . . . SNORD41 . . . small nucleolar RNA, C/D box 41 . . . . . . . . . . . SNORD42A . . . small nucleolar RNA, C/D box 42A . . . . . . . . . . . SNORD42B . . . small nucleolar RNA, C/D box 42B . . . . . . . . . . . SNORD43 . . . small nucleolar RNA, C/D box 43 . . . . . . . . . . . SNORD44 . . . small nucleolar RNA, C/D box 44 . . . . . . . . . . . SNORD45A . . . small nucleolar RNA, C/D box 45A . . . . . . . . . . . SNORD45B . . . small nucleolar RNA, C/D box 45B . . . . . . . . . . . SNORD45C . . . small nucleolar RNA, C/D box 45C . . . . . . . . . . . SNORD46 . . . small nucleolar RNA, C/D box 46 . . . . . . . . . . . SNORD47 . . . small nucleolar RNA, C/D box 47 . . . . . . . . . . . SNORD48 . . . small nucleolar RNA, C/D box 48 . . . . . . . . . . . SNORD49A . . . small nucleolar RNA, C/D box 49A . . . . . . . . . . . SNORD49B . . . small nucleolar RNA, C/D box 49B . . . . . . . . . . . SNORD50A . . . small nucleolar RNA, C/D box 50A . . . . . . . . . . . SNORD50B . . . small nucleolar RNA, C/D box 50B . . . . . . . . . . . SNORD51 . . . small nucleolar RNA, C/D box 51 . . . . . . . . . . . SNORD52 . . . small nucleolar RNA, C/D box 52 . . . . . . . . . . . SNORD53 . . . small nucleolar RNA, C/D box 53 . . . . . . . . . . . SNORD54 . . . small nucleolar RNA, C/D box 54 . . . . . . . . . . . SNORD55 . . . small nucleolar RNA, C/D box 55 . . . . . . . . . . . SNORD56 . . . small nucleolar RNA, C/D box 56 . . . . . . . . . . . SNORD56B . . . small nucleolar RNA, C/D box 56B . . . . . . . . . . . SNORD57 . . . small nucleolar RNA, C/D box 57 . . . . . . . . . . . SNORD58A . . . small nucleolar RNA, C/D box 58A . . . . . . . . . . . SNORD58B . . . small nucleolar RNA, C/D box 58B . . . . . . . . . . . SNORD58C . . . small nucleolar RNA, C/D box 58C . . . . . . . . . . . SNORD59A . . . small nucleolar RNA, C/D box 59A . . . . . . . . . . . SNORD59B . . . small nucleolar RNA, C/D box 59B . . . . . . . . . . . SNORD60 . . . small nucleolar RNA, C/D box 60 . . . . . . . . . . . SNORD61 . . . small nucleolar RNA, C/D box 61 . . . . . . . . . . . SNORD62A . . . small nucleolar RNA, C/D box 62A . . . . . . . . . . . SNORD62B . . . small nucleolar RNA, C/D box 62B . . . . . . . . . . . SNORD63 . . . small nucleolar RNA, C/D box 63 . . . . . . . . . . . SNORD64 . . . small nucleolar RNA, C/D box 64 . . . . . . . . . . . SNORD65 . . . small nucleolar RNA, C/D box 65 . . . . . . . . . . . SNORD66 . . . small nucleolar RNA, C/D box 66 . . . . . . . . . . . SNORD67 . . . small nucleolar RNA, C/D box 67 . . . . . . . . . . . SNORD68 . . . small nucleolar RNA, C/D box 68 . . . . . . . . . . . SNORD69 . . . small nucleolar RNA, C/D box 69 . . . . . . . . . . . SNORD70 . . . small nucleolar RNA, C/D box 70 . . . . . . . . . . . SNORD71 . . . small nucleolar RNA, C/D box 71 . . . . . . . . . . . SNORD72 . . . small nucleolar RNA, C/D box 72 . . . . . . . . . . . SNORD73A . . . small nucleolar RNA, C/D box 73A . . . . . . . . . . . SNORD73B . . . small nucleolar RNA, C/D box U73B (pseudogene) . . . . . . . . . . . SNORD74 . . . small nucleolar RNA, C/D box 74 . . . . . . . . . . . SNORD75 . . . small nucleolar RNA, C/D box 75 . . . . . . . . . . . SNORD76 . . . small nucleolar RNA, C/D box 76 . . . . . . . . . . . SNORD77 . . . small nucleolar RNA, C/D box 77 . . . . . . . . . . . SNORD78 . . . small nucleolar RNA, C/D box 78 . . . . . . . . . . . SNORD79 . . . small nucleolar RNA, C/D box 79 . . . . . . . . . . . SNORD80 . . . small nucleolar RNA, C/D box 80 . . . . . . . . . . . SNORD81 . . . small nucleolar RNA, C/D box 81 . . . . . . . . . . . SNORD82 . . . small nucleolar RNA, C/D box 82 . . . . . . . . . . . SNORD83A . . . small nucleolar RNA, C/D box 83A . . . . . . . . . . . SNORD83B . . . small nucleolar RNA, C/D box 83B . . . . . . . . . . . SNORD84 . . . small nucleolar RNA, C/D box 84 . . . . . . . . . . . SNORD86 . . . small nucleolar RNA, C/D box 86 . . . . . . . . . . . SNORD87 . . . small nucleolar RNA, C/D box 87 . . . . . . . . . . . SNORD88A . . . small nucleolar RNA, C/D box 88A . . . . . . . . . . . SNORD88B . . . small nucleolar RNA, C/D box 88B . . . . . . . . . . . SNORD88C . . . small nucleolar RNA, C/D box 88C . . . . . . . . . . . SNORD89 . . . small nucleolar RNA, C/D box 89 . . . . . . . . . . . SNORD90 . . . small nucleolar RNA, C/D box 90 . . . . . . . . . . . SNORD91A . . . small nucleolar RNA, C/D box 91A . . . . . . . . . . . SNORD91B . . . small nucleolar RNA, C/D box 91B . . . . . . . . . . . SNORD92 . . . small nucleolar RNA, C/D box 92 . . . . . . . . . . . SNORD93 . . . small nucleolar RNA, C/D box 93 . . . . . . . . . . . SNORD94 . . . small nucleolar RNA, C/D box 94 . . . . . . . . . . . SNORD95 . . . small nucleolar RNA, C/D box 95 . . . . . . . . . . . SNORD96A . . . small nucleolar RNA, C/D box 96A . . . . . . . . . . . SNORD96B . . . small nucleolar RNA, C/D box 96B . . . . . . . . . . . SNORD97 . . . small nucleolar RNA, C/D box 97 . . . . . . . . . . . SNORD98 . . . small nucleolar RNA, C/D box 98 . . . . . . . . . . . SNORD99 . . . small nucleolar RNA, C/D box 99 . . . . . . . . . . . SNORD100 . . . small nucleolar RNA, C/D box 100 . . . . . . . . . . . SNORD101 . . . small nucleolar RNA, C/D box 101 . . . . . . . . . . . SNORD102 . . . small nucleolar RNA, C/D box 102 . . . . . . . . . . . SNORD103A . . . small nucleolar RNA, C/D box 103A . . . . . . . . . . . SNORD103B . . . small nucleolar RNA, C/D box 103B . . . . . . . . . . . SNORD103C . . . small nucleolar RNA, C/D box 103C . . . . . . . . . . . SNORD104 . . . small nucleolar RNA, C/D box 104 . . . . . . . . . . . SNORD105 . . . small nucleolar RNA, C/D box 105 . . . . . . . . . . . SNORD105B . . . small nucleolar RNA, C/D box 105B . . . . . . . . . . . SNORD107 . . . small nucleolar RNA, C/D box 107 . . . . . . . . . . . SNORD108 . . . small nucleolar RNA, C/D box 108 . . . . . . . . . . . SNORD109A . . . small nucleolar RNA, C/D box 109A . . . . . . . . . . . SNORD109B . . . small nucleolar RNA, C/D box 109B . . . . . . . . . . . SNORD110 . . . small nucleolar RNA, C/D box 110 . . . . . . . . . . . SNORD111 . . . small nucleolar RNA, C/D box 111 . . . . . . . . . . . SNORD111B . . . small nucleolar RNA, C/D box 111B . . . . . . . . . . . SNORD112 . . . small nucleolar RNA, C/D box 112 . . . . . . . . . . . SNORD113-1 . . . small nucleolar RNA, C/D box 113-1 . . . . . . . . . . . SNORD113-2 . . . small nucleolar RNA, C/D box 113-2 . . . . . . . . . . . SNORD113-3 . . . small nucleolar RNA, C/D box 113-3 . . . . . . . . . . . SNORD113-4 . . . small nucleolar RNA, C/D box 113-4 . . . . . . . . . . . SNORD113-5 . . . small nucleolar RNA, C/D box 113-5 . . . . . . . . . . . SNORD113-6 . . . small nucleolar RNA, C/D box 113-6 . . . . . . . . . . . SNORD113-7 . . . small nucleolar RNA, C/D box 113-7 . . . . . . . . . . . SNORD113-8 . . . small nucleolar RNA, C/D box 113-8 . . . . . . . . . . . SNORD113-9 . . . small nucleolar RNA, C/D box 113-9 . . . . . . . . . . . SNORD114-1 . . . small nucleolar RNA, C/D box 114-1 . . . . . . . . . . . SNORD114-2 . . . small nucleolar RNA, C/D box 114-2 . . . . . . . . . . . SNORD114-3 . . . small nucleolar RNA, C/D box 114-3 . . . . . . . . . . . SNORD114-4 . . . small nucleolar RNA, C/D box 114-4 . . . . . . . . . . . SNORD114-5 . . . small nucleolar RNA, C/D box 114-5 . . . . . . . . . . . SNORD114-6 . . . small nucleolar RNA, C/D box 114-6 . . . . . . . . . . . SNORD114-7 . . . small nucleolar RNA, C/D box 114-7 . . . . . . . . . . . SNORD114-8 . . . small nucleolar RNA, C/D box 114-8 . . . . . . . . . . . SNORD114-9 . . . small nucleolar RNA, C/D box 114-9 . . . . . . . . . . . SNORD114-10 . . . small nucleolar RNA, C/D box 114-10 . . . . . . . . . . . SNORD114-11 . . . small nucleolar RNA, C/D box 114-11 . . . . . . . . . . . SNORD114-12 . . . small nucleolar RNA, C/D box 114-12 . . . . . . . . . . . SNORD114-13 . . . small nucleolar RNA, C/D box 114-13 . . . . . . . . . . . SNORD114-14 . . . small nucleolar RNA, C/D box 114-14 . . . . . . . . . . . SNORD114-15 . . . small nucleolar RNA, C/D box 114-15 . . . . . . . . . . . SNORD114-16 . . . small nucleolar RNA, C/D box 114-16 . . . . . . . . . . . SNORD114-17 . . . small nucleolar RNA, C/D box 114-17 . . . . . . . . . . . SNORD114-18 . . . small nucleolar RNA, C/D box 114-18 . . . . . . . . . . . SNORD114-19 . . . small nucleolar RNA, C/D box 114-19 . . . . . . . . . . . SNORD114-20 . . . small nucleolar RNA, C/D box 114-20 . . . . . . . . . . . SNORD114-21 . . . small nucleolar RNA, C/D box 114-21 . . . . . . . . . . . SNORD114-22 . . . small nucleolar RNA, C/D box 114-22 . . . . . . . . . . . SNORD114-23 . . . small nucleolar RNA, C/D box 114-23 . . . . . . . . . . . SNORD114-24 . . . small nucleolar RNA, C/D box 114-24 . . . . . . . . . . . SNORD114-25 . . . small nucleolar RNA, C/D box 114-25 . . . . . . . . . . . SNORD114-26 . . . small nucleolar RNA, C/D box 114-26 . . . . . . . . . . . SNORD114-27 . . . small nucleolar RNA, C/D box 114-27 . . . . . . . . . . . SNORD114-28 . . . small nucleolar RNA, C/D box 114-28 . . . . . . . . . . . SNORD114-29 . . . small nucleolar RNA, C/D box 114-29 . . . . . . . . . . . SNORD114-30 . . . small nucleolar RNA, C/D box 114-30 . . . . . . . . . . . SNORD114-31 . . . small nucleolar RNA, C/D box 114-31 . . . . . . . . . . . SNORD114@ . . . small nucleolar RNA, C/D box 114 cluster . . . . . . . . . . . SNORD115-1 . . . small nucleolar RNA, C/D box 115-1 . . . . . . . . . . . SNORD115-2 . . . small nucleolar RNA, C/D box 115-2 . . . . . . . . . . . SNORD115-3 . . . small nucleolar RNA, C/D box 115-3 . . . . . . . . . . . SNORD115-4 . . . small nucleolar RNA, C/D box 115-4 . . . . . . . . . . . SNORD115-5 . . . small nucleolar RNA, C/D box 115-5 . . . . . . . . . . . SNORD115-6 . . . small nucleolar RNA, C/D box 115-6 . . . . . . . . . . . SNORD115-7 . . . small nucleolar RNA, C/D box 115-7 . . . . . . . . . . . SNORD115-8 . . . small nucleolar RNA, C/D box 115-8 . . . . . . . . . . . SNORD115-9 . . . small nucleolar RNA, C/D box 115-9 . . . . . . . . . . . SNORD115-10 . . . small nucleolar RNA, C/D box 115-10 . . . . . . . . . . . SNORD115-11 . . . small nucleolar RNA, C/D box 115-11 . . . . . . . . . . . SNORD115-12 . . . small nucleolar RNA, C/D box 115-12 . . . . . . . . . . . SNORD115-13 . . . small nucleolar RNA, C/D box 115-13 . . . . . . . . . . . SNORD115-14 . . . small nucleolar RNA, C/D box 115-14 . . . . . . . . . . . SNORD115-15 . . . small nucleolar RNA, C/D box 115-15 . . . . . . . . . . . SNORD115-16 . . . small nucleolar RNA, C/D box 115-16 . . . . . . . . . . . SNORD115-17 . . . small nucleolar RNA, C/D box 115-17 . . . . . . . . . . . SNORD115-18 . . . small nucleolar RNA, C/D box 115-18 . . . . . . . . . . . SNORD115-19 . . . small nucleolar RNA, C/D box 115-19 . . . . . . . . . . . SNORD115-20 . . . small nucleolar RNA, C/D box 115-20 . . . . . . . . . . . SNORD115-21 . . . small nucleolar RNA, C/D box 115-21 . . . . . . . . . . . SNORD115-22 . . . small nucleolar RNA, C/D box 115-22 . . . . . . . . . . . SNORD115-23 . . . small nucleolar RNA, C/D box 115-23 . . . . . . . . . . . SNORD115-24 . . . small nucleolar RNA, C/D box 115-24 . . . . . . . . . . . SNORD115-25 . . . small nucleolar RNA, C/D box 115-25 . . . . . . . . . . . SNORD115-26 . . . small nucleolar RNA, C/D box 115-26 . . . . . . . . . . . SNORD115-27 . . . small nucleolar RNA, C/D box 115-27 . . . . . . . . . . . SNORD115-28 . . . small nucleolar RNA, C/D box 115-28 . . . . . . . . . . . SNORD115-29 . . . small nucleolar RNA, C/D box 115-29 . . . . . . . . . . . SNORD115-30 . . . small nucleolar RNA, C/D box 115-30 . . . . . . . . . . . SNORD115-31 . . . small nucleolar RNA, C/D box 115-31 . . . . . . . . . . . SNORD115-32 . . . small nucleolar RNA, C/D box 115-32 . . . . . . . . . . . SNORD115-33 . . . small nucleolar RNA, C/D box 115-33 . . . . . . . . . . . SNORD115-34 . . . small nucleolar RNA, C/D box 115-34 . . . . . . . . . . . SNORD115-35 . . . small nucleolar RNA, C/D box 115-35 . . . . . . . . . . . SNORD115-36 . . . small nucleolar RNA, C/D box 115-36 . . . . . . . . . . . SNORD115-37 . . . small nucleolar RNA, C/D box 115-37 . . . . . . . . . . . SNORD115-38 . . . small nucleolar RNA, C/D box 115-38 . . . . . . . . . . . SNORD115-39 . . . small nucleolar RNA, C/D box 115-39 . . . . . . . . . . . SNORD115-40 . . . small nucleolar RNA, C/D box 115-40 . . . . . . . . . . . SNORD115-41 . . . small nucleolar RNA, C/D box 115-41 . . . . . . . . . . . SNORD115-42 . . . small nucleolar RNA, C/D box 115-42 . . . . . . . . . . . SNORD115-43 . . . small nucleolar RNA, C/D box 115-43 . . . . . . . . . . . SNORD115-44 . . . small nucleolar RNA, C/D box 115-44 . . . . . . . . . . . SNORD115-45 . . . small nucleolar RNA, C/D box 115-45 . . . . . . . . . . . SNORD115-46 . . . small nucleolar RNA, C/D box 115-46 . . . . . . . . . . . SNORD115-47 . . . small nucleolar RNA, C/D box 115-47 . . . . . . . . . . . SNORD115-48 . . . small nucleolar RNA, C/D box 115-48 . . . . . . . . . . . SNORD115@ . . . small nucleolar RNA, C/D box 115 cluster . . . . . . . . . . . SNORD116-1 . . . small nucleolar RNA, C/D box 116-1 . . . . . . . . . . . SNORD116-2 . . . small nucleolar RNA, C/D box 116-2 . . . . . . . . . . . SNORD116-3 . . . small nucleolar RNA, C/D box 116-3 . . . . . . . . . . . SNORD116-4 . . . small nucleolar RNA, C/D box 116-4 . . . . . . . . . . . SNORD116-5 . . . small nucleolar RNA, C/D box 116-5 . . . . . . . . . . . SNORD116-6 . . . small nucleolar RNA, C/D box 116-6 . . . . . . . . . . . SNORD116-7 . . . small nucleolar RNA, C/D box 116-7 . . . . . . . . . . . SNORD116-8 . . . small nucleolar RNA, C/D box 116-8 . . . . . . . . . . . SNORD116-9 . . . small nucleolar RNA, C/D box 116-9 . . . . . . . . . . . SNORD116-10 . . . small nucleolar RNA, C/D box 116-10 . . . . . . . . . . . SNORD116-11 . . . small nucleolar RNA, C/D box 116-11 . . . . . . . . . . . SNORD116-12 . . . small nucleolar RNA, C/D box 116-12 . . . . . . . . . . . SNORD116-13 . . . small nucleolar RNA, C/D box 116-13 . . . . . . . . . . . SNORD116-14 . . . small nucleolar RNA, C/D box 116-14 . . . . . . . . . . . SNORD116-15 . . . small nucleolar RNA, C/D box 116-15 . . . . . . . . . . . SNORD116-16 . . . small nucleolar RNA, C/D box 116-16 . . . . . . . . . . . SNORD116-17 . . . small nucleolar RNA, C/D box 116-17 . . . . . . . . . . . SNORD116-18 . . . small nucleolar RNA, C/D box 116-18 . . . . . . . . . . . SNORD116-19 . . . small nucleolar RNA, C/D box 116-19 . . . . . . . . . . . SNORD116-20 . . . small nucleolar RNA, C/D box 116-20 . . . . . . . . . . . SNORD116-21 . . . small nucleolar RNA, C/D box 116-21 . . . . . . . . . . . SNORD116-22 . . . small nucleolar RNA, C/D box 116-22 . . . . . . . . . . . SNORD116-23 . . . small nucleolar RNA, C/D box 116-23 . . . . . . . . . . . SNORD116-24 . . . small nucleolar RNA, C/D box 116-24 . . . . . . . . . . . SNORD116-25 . . . small nucleolar RNA, C/D box 116-25 . . . . . . . . . . . SNORD116-26 . . . small nucleolar RNA, C/D box 116-26 . . . . . . . . . . . SNORD116-27 . . . small nucleolar RNA, C/D box 116-27 . . . . . . . . . . . SNORD116-28 . . . small nucleolar RNA, C/D box 116-28 . . . . . . . . . . . SNORD116-29 . . . small nucleolar RNA, C/D box 116-29 . . . . . . . . . . . SNORD116-30 . . . small nucleolar RNA, C/D box 116-30 . . . . . . . . . . . SNORD116@ . . . small nucleolar RNA, C/D box 116 cluster . . . . . . . . . . . SNORD117 . . . small nucleolar RNA, C/D box 117 . . . . . . . . . . . SNORD118 . . . small nucleolar RNA, C/D box 118 . . . . . . . . . . . SNORD119 . . . small nucleolar RNA, C/D box 119 . . . . . . . . . . . SNORD121A . . . small nucleolar RNA, C/D box 121A . . . . . . . . . . . SNORD121B . . . small nucleolar RNA, C/D box 121B . . . . . . . . . . . SNORD123 . . . small nucleolar RNA, C/D box 123 . . . . . . . . . . . SNORD124 . . . small nucleolar RNA, C/D box 124 . . . . . . . . . . . SNORD125 . . . small nucleolar RNA, C/D box 125 . . . . . . . . . . . SNORD126 . . . small nucleolar RNA, C/D box 126 . . . . . . . . . . . SNORD127 . . . small nucleolar RNA, C/D box 127 . . . . . . . . . . . SNORD128 . . . small nucleolar RNA, C/D box 128 . . . . . . . . . . . SNORD129 . . . small nucleolar RNA, C/D box 129 . . . . . . . . . . . SNORD130 . . . small nucleolar RNA, C/D box 130 . . . . . . . . . . . SNORD131 . . . small nucleolar RNA, C/D box 131 . . . . . . . . . . . SNORD132 . . . small nucleolar RNA, C/D box 132 . . . . . . . . . . . SNORD133 . . . small nucleolar RNA, C/D box 133 . . . . . . . . . . . SNORD134 . . . small nucleolar RNA, C/D box 134 . . . . . . . . . . . SNORD135 . . . small nucleolar RNA, C/D box 135 . . . . . . . . . . . SNORD136 . . . small nucleolar RNA, C/D box 136 . . . . . . . . . . . SNORD137 . . . small nucleolar RNA, C/D box 137 . . . . . . . . . . . SNORD138 . . . small nucleolar RNA, C/D box 138 . . . . . . . . . . . SNORD139 . . . small nucleolar RNA, C/D box 139 . . . . . . . . . . . SNORD140 . . . small nucleolar RNA, C/D box 140 . . . . . . . . . . . SNORD141A . . . small nucleolar RNA, C/D box 141A . . . . . . . . . . . SNORD141B . . . small nucleolar RNA, C/D box 141B . . . . . . . . . . . SNORD142 . . . small nucleolar RNA, C/D box 142 . . . . . . . . . . . SNORD143 . . . small nucleolar RNA, C/D box 143 . . . . . . . . . . . SNORD144 . . . small nucleolar RNA, C/D box 144 . . . . . . . . . . . SNORD145 . . . small nucleolar RNA, C/D box 145 . . . . . . . . . . . SNORD146 . . . small nucleolar RNA, C/D box 146 . . . . . . . . . . . SNORD147 . . . small nucleolar RNA, C/D box 147 . . . . . . . . . . . SNORD148 . . . small nucleolar RNA, C/D box 148 . . . . . . . . . . . SNORD149 . . . small nucleolar RNA, C/D box 149 . . . . . . . . . . . SNORD150 . . . small nucleolar RNA, C/D box 150 . . . . . . . . . . . SNORD151 . . . small nucleolar RNA, C/D box 151 . . . . . . . . . . . SNORD152 . . . small nucleolar RNA, C/D box 152 . . . . . . . . . . . SNORD153 . . . small nucleolar RNA, C/D box 153 . . . . . . . . . . . SNORD154 . . . small nucleolar RNA, C/D box 154 . . . . . . . . . . . SNORD155 . . . small nucleolar RNA, C/D box 155 . . . . . . . . . . . SNORD156 . . . small nucleolar RNA, C/D box 156 . . . . . . . . . . . SNORD157 . . . small nucleolar RNA, C/D box 157 . . . . . . . . . . . SNORD158 . . . small nucleolar RNA, C/D box 158 . . . . . . . . . . . SNORD159 . . . small nucleolar RNA, C/D box 159 . . . . . . . . . . . SNORD160 . . . small nucleolar RNA, C/D box 160 . . . . . . . . . . . SNORD161 . . . small nucleolar RNA, C/D box 161 . . . . . . . . . . . SNORD162 . . . small nucleolar RNA, C/D box 162 . . . . . . . . . . . SNORD163 . . . small nucleolar RNA, C/D box 163 . . . . . . . . . . . SNORD164 . . . small nucleolar RNA, C/D box 164 . . . . . . . . . . . SNORD165 . . . small nucleolar RNA, C/D box 165 . . . . . . . . . . . SNORD166 . . . small nucleolar RNA, C/D box 166 . . . . . . . . . . . SNORD167 . . . small nucleolar RNA, C/D box 167 . . . . . . . . . . . SNORD168 . . . small nucleolar RNA, C/D box 168 . . . . . . . . . . . SNORD169 . . . small nucleolar RNA, C/D box 169 . . . . . . . . . . . SNORD170 . . . small nucleolar RNA, C/D box 170 . . . . . . . . . . . SNORD172 . . . small nucleolar RNA, C/D box 172 . . . . . . . . . . . SNORD173 . . . small nucleolar RNA, C/D box 173 . . . . . . . . . . . SNORD175 . . . small nucleolar RNA, C/D box 175 . . . . . . . . . . . SNPH 0.796091125666896 0.202675244424261 0.001233629908843 syntaphilin FUNCTION: Inhibits SNARE complex formation by absorbing free syntaxin-1. {ECO:0000269|PubMed:10707983}.; . TISSUE SPECIFICITY: Brain specific. Found in synapses. {ECO:0000269|PubMed:10707983}.; . . . . -0.644723694 16.52512385 87.5797 1.99833 SNRK 0.994142267780069 0.00585694245134454 7.89768586800709e-07 SNF related kinase FUNCTION: May play a role in hematopoietic cell proliferation or differentiation. Potential mediator of neuronal apoptosis. {ECO:0000250|UniProtKB:Q63553, ECO:0000269|PubMed:12234663, ECO:0000269|PubMed:15733851}.; . TISSUE SPECIFICITY: Expressed in hematopoietic progenitor cells and leukemic cell lines. Weakly expressed in the testis. {ECO:0000269|PubMed:12234663, ECO:0000269|PubMed:8654423}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;larynx;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;aorta; amygdala;superior cervical ganglion;appendix;atrioventricular node;whole blood;cerebellum; 0.25487 0.13098 -0.644723694 16.52512385 49.28396 1.37235 SNRK-AS1 . . . SNRK antisense RNA 1 . . . . . . . . . . . SNRNP25 0.00747804113002767 0.924626447343211 0.0678955115267613 small nuclear ribonucleoprotein U11/U12 subunit 25 . . . myocardium;lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;tongue;blood;lens;skeletal muscle;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach; whole brain;parietal lobe; 0.09998 0.09022 -0.05129383 49.75819769 11.70408 0.42444 SNRNP27 0.024069445050423 0.961973603323859 0.0139569516257184 small nuclear ribonucleoprotein U4/U6.U5 subunit 27 FUNCTION: May play a role in mRNA splicing.; . . medulla oblongata;smooth muscle;ovary;salivary gland;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;bile duct;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;duodenum;head and neck;cervix;kidney;mammary gland;stomach; occipital lobe;medulla oblongata;subthalamic nucleus;superior cervical ganglion;temporal lobe;atrioventricular node;pons; . 0.05582 -0.031067188 51.03798066 3.69185 0.13715 SNRNP35 2.28333241562555e-07 0.273128591573007 0.726871180093752 small nuclear ribonucleoprotein U11/U12 subunit 35 . . TISSUE SPECIFICITY: Expressed in heart, liver, skeletal muscle and pancreas. {ECO:0000269|PubMed:10520751}.; ovary;salivary gland;developmental;intestine;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;oesophagus;bone;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;kidney;stomach;aorta; prefrontal cortex;white blood cells; . . -0.293801652 32.93819297 31.03063 0.98089 SNRNP40 0.825363235899783 0.174472232630012 0.000164531470205093 small nuclear ribonucleoprotein U5 subunit 40 FUNCTION: Component of the U5 small nuclear ribonucleoprotein (snRNP) complex. The U5 snRNP is part of the spliceosome, a multiprotein complex that catalyzes the removal of introns from pre-messenger RNAs. {ECO:0000269|PubMed:9774689}.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;endometrium;bone;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;cervix;kidney;stomach; dorsal root ganglion;testis; 0.28975 0.17050 -0.361761279 28.6329323 19.69765 0.67413 SNRNP48 7.93003716284965e-05 0.922503582554892 0.0774171170734794 small nuclear ribonucleoprotein U11/U12 subunit 48 FUNCTION: Likely involved in U12-type 5' splice site recognition. {ECO:0000269|PubMed:19217400}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;synovium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;lung;cornea;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve;thymus; superior cervical ganglion;olfactory bulb;ciliary ganglion;atrioventricular node; 0.15476 . -0.247889024 35.98726115 2139.52224 8.50888 SNRNP70 0.993095085568321 0.00690467546206587 2.38969613439537e-07 small nuclear ribonucleoprotein U1 subunit 70 FUNCTION: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRNP70 binds to the loop I region of U1-snRNA. The truncated isoforms cannot bind U1-snRNA.; . . medulla oblongata;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;bladder;brain;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;oesophagus;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;cornea;mesenchyma;placenta;hippocampus;head and neck;kidney;stomach; medulla oblongata;superior cervical ganglion;prefrontal cortex;cingulate cortex; 0.54826 0.24974 . . 34.51837 1.05414 SNRNP200 0.999999999999148 8.51564555755356e-13 7.07550286842115e-33 small nuclear ribonucleoprotein U5 subunit 200 FUNCTION: RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome. {ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:23045696, ECO:0000269|PubMed:8670905, ECO:0000269|PubMed:9539711}.; DISEASE: Retinitis pigmentosa 33 (RP33) [MIM:610359]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:19710410, ECO:0000269|PubMed:19878916, ECO:0000269|PubMed:21618346, ECO:0000269|PubMed:23029027, ECO:0000269|PubMed:23887765, ECO:0000269|PubMed:24319334}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19878916}.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pineal body;adrenal cortex;blood;lens;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach; testis - interstitial;placenta;testis;globus pallidus;ciliary ganglion; 0.37044 0.16846 -2.34092223 1.167728238 177.85929 2.89764 SNRPA 0.0602794492639456 0.868582179789653 0.0711383709464015 small nuclear ribonucleoprotein polypeptide A FUNCTION: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1 snRNP is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP. SNRPA binds stem loop II of U1 snRNA. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA splicing and polyadenylation process. May bind preferentially to the 5'-UGCAC-3' motif on RNAs. {ECO:0000269|PubMed:9848648}.; . . lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;gall bladder;heart;cartilage;pharynx;blood;lens;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;kidney;stomach;thymus; superior cervical ganglion;testis;tumor; 0.73233 0.29004 -0.538132194 20.26421326 12.81975 0.46701 SNRPA1 0.969077644208195 0.0308753719560342 4.69838357702983e-05 small nuclear ribonucleoprotein polypeptide A' FUNCTION: This protein is associated with sn-RNP U2. It helps the A' protein to bind stem loop IV of U2 snRNA.; . . ovary;salivary gland;developmental;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;muscle;urinary;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; . 0.83500 0.13588 0.3032669 72.009908 28.65066 0.91734 SNRPB 0.691451244777475 0.307703778578191 0.000844976644333981 small nuclear ribonucleoprotein polypeptides B and B1 FUNCTION: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3'-end processing. {ECO:0000269|PubMed:18984161}.; DISEASE: Cerebrocostomandibular syndrome (CCMS) [MIM:117650]: A syndrome characterized by severe micrognathia, rib defects ranging from a few dorsal rib segments to complete absence of ossification, and mental retardation. {ECO:0000269|PubMed:25047197, ECO:0000269|PubMed:25504470}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;bone marrow;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;muscle;urinary;pharynx;lens;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;tumor;testis;thymus; 0.65793 0.17494 -0.273576253 33.97027601 17.31943 0.60824 SNRPB2 0.320265019109405 0.66317316125805 0.0165618196325449 small nuclear ribonucleoprotein polypeptide B FUNCTION: Involved in pre-mRNA splicing. This protein is associated with snRNP U2. It binds stem loop IV of U2 snRNA only in presence of the U2A' protein.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;synovium;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach;peripheral nerve; testis - interstitial; 0.37056 0.12309 -0.119252484 44.53880632 2.42849 0.08657 SNRPBP1 . . . small nuclear ribonucleoprotein polypeptides B and B1 pseudogene 1 . . . . . . . . . . . SNRPC 0.727261777653869 0.269915577331038 0.00282264501509232 small nuclear ribonucleoprotein polypeptide C FUNCTION: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRPC/U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates E complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region. {ECO:0000269|PubMed:1826349, ECO:0000269|PubMed:2136774, ECO:0000269|PubMed:8798632}.; . . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;atrium;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;mesenchyma;adrenal gland;nasopharynx;placenta;kidney;stomach; testis - interstitial;testis - seminiferous tubule;heart;testis;trigeminal ganglion;parietal lobe;skeletal muscle; 0.09171 0.08351 -0.031067188 51.03798066 2320.23942 8.91651 SNRPCP1 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 1 . . . . . . . . . . . SNRPCP2 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 2 . . . . . . . . . . . SNRPCP3 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 3 . . . . . . . . . . . SNRPCP4 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 4 . . . . . . . . . . . SNRPCP5 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 5 . . . . . . . . . . . SNRPCP6 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 6 . . . . . . . . . . . SNRPCP7 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 7 . . . . . . . . . . . SNRPCP8 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 8 . . . . . . . . . . . SNRPCP9 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 9 . . . . . . . . . . . SNRPCP10 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 10 . . . . . . . . . . . SNRPCP11 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 11 . . . . . . . . . . . SNRPCP12 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 12 . . . . . . . . . . . SNRPCP13 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 13 . . . . . . . . . . . SNRPCP14 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 14 . . . . . . . . . . . SNRPCP15 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 15 . . . . . . . . . . . SNRPCP16 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 16 . . . . . . . . . . . SNRPCP17 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 17 . . . . . . . . . . . SNRPCP18 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 18 . . . . . . . . . . . SNRPCP19 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 19 . . . . . . . . . . . SNRPCP20 . . . small nuclear ribonucleoprotein polypeptide C pseudogene 20 . . . . . . . . . . . SNRPD1 0.847045312877468 0.150263893319578 0.00269079380295418 small nuclear ribonucleoprotein D1 polypeptide FUNCTION: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. May act as a charged protein scaffold to promote snRNP assembly or strengthen snRNP-snRNP interactions through nonspecific electrostatic contacts with RNA. {ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:23333303}.; . . ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;oesophagus;gum;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;tumor;white blood cells;pons;trigeminal ganglion; 0.86438 0.23984 0.12325821 62.38499646 1.22504 0.04172 SNRPD2 0.747515256284436 0.242186513765885 0.0102982299496785 small nuclear ribonucleoprotein D2 polypeptide FUNCTION: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. {ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:23333303}.; . . myocardium;ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;cerebral cortex;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;oral cavity;muscle;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach;aorta; testis - interstitial;testis - seminiferous tubule;tumor;testis; 0.43283 0.23984 -0.075159878 47.78839349 . . SNRPD2P1 . . . small nuclear ribonucleoprotein D2 pseudogene 1 . . . . . . . . . . . SNRPD2P2 . . . small nuclear ribonucleoprotein D2 pseudogene 2 . . . . . . . . . . . SNRPD3 0.877845312096731 0.120656839956428 0.00149784794684063 small nuclear ribonucleoprotein D3 polypeptide FUNCTION: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3'-end processing. {ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:18984161}.; . . lymphoreticular;smooth muscle;ovary;skin;retina;frontal lobe;endometrium;thyroid;brain;ciliary body;heart;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; testis;tumor;white blood cells; 0.86916 0.20297 0.057118534 57.99716914 . . SNRPE 0.891456792044026 0.107438799512805 0.00110440844316897 small nuclear ribonucleoprotein polypeptide E FUNCTION: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3'-end processing. May indirectly play a role in hair development. {ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:23246290, ECO:0000269|PubMed:23333303}.; . TISSUE SPECIFICITY: Widely expressed. In scalp skin, it is present in the hair follicle, the epidermis, and the dermis. {ECO:0000269|PubMed:23246290}.; . . . 0.46610 0.12325821 62.38499646 . . SNRPEP1 . . . small nuclear ribonucleoprotein polypeptide E pseudogene 1 . . . . . . . . . . . SNRPEP2 . . . small nuclear ribonucleoprotein polypeptide E pseudogene 2 . . . . . . 0.46610 . . . . SNRPEP3 . . . small nuclear ribonucleoprotein polypeptide E pseudogene 3 . . . . . . . . . . . SNRPEP4 . . . small nuclear ribonucleoprotein polypeptide E pseudogene 4 . . . . . . . . . . . SNRPEP5 . . . small nuclear ribonucleoprotein polypeptide E pseudogene 5 . . . . . . . . . . . SNRPEP6 . . . small nuclear ribonucleoprotein polypeptide E pseudogene 6 . . . . . . . . . . . SNRPEP7 . . . small nuclear ribonucleoprotein polypeptide E pseudogene 7 . . . . . . . . . . . SNRPEP8 . . . small nuclear ribonucleoprotein polypeptide E pseudogene 8 . . . . . . . . . . . SNRPEP9 . . . small nuclear ribonucleoprotein polypeptide E pseudogene 9 . . . . . . . . . . . SNRPEP10 . . . small nuclear ribonucleoprotein polypeptide E pseudogene 10 . . . . . . . . . . . SNRPF 0.734661647651888 0.253534595972498 0.011803756375613 small nuclear ribonucleoprotein polypeptide F FUNCTION: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3'-end processing. {ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:23333303}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;pituitary gland;testis;brain;artery;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;liver;kidney;mammary gland;stomach;aorta; superior cervical ganglion;tumor; 0.81813 . 0.101211609 60.95777306 4.10655 0.15047 SNRPFP1 . . . small nuclear ribonucleoprotein polypeptide F pseudogene 1 . . . . . . . . . . . SNRPFP2 . . . small nuclear ribonucleoprotein polypeptide F pseudogene 2 . . . . . . . . . . . SNRPFP3 . . . small nuclear ribonucleoprotein polypeptide F pseudogene 3 . . . . . . . . . . . SNRPFP4 . . . small nuclear ribonucleoprotein polypeptide F pseudogene 4 . . . . . . . . . . . SNRPG 0.866844385628649 0.131282281992654 0.00187333237869655 small nuclear ribonucleoprotein polypeptide G FUNCTION: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. Appears to function in the U7 snRNP complex that is involved in histone 3'- end processing. {ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:23333303}.; . . ovary;skin;retina;bone marrow;prostate;endometrium;thyroid;germinal center;bladder;brain;heart;tongue;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; . 0.23756 0.12346 0.12325821 62.38499646 10.55923 0.38277 SNRPGP1 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 1 . . . . . . . . . . . SNRPGP2 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 2 . . . . . . . . . . . SNRPGP3 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 3 . . . . . . . . . . . SNRPGP4 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 4 . . . . . . . . . . . SNRPGP5 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 5 . . . . . . . . . . . SNRPGP6 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 6 . . . . . . . . . . . SNRPGP7 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 7 . . . . . . . . . . . SNRPGP8 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 8 . . . . . . . . . . . SNRPGP9 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 9 . . . . . . . . . . . SNRPGP10 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 10 . . . . . . . . . . . SNRPGP11 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 11 . . . . . . . . . . . SNRPGP12 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 12 . . . . . . . . . . . SNRPGP13 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 13 . . . . . . . . . . . SNRPGP14 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 14 . . . . . . . . . . . SNRPGP15 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 15 FUNCTION: Associated with snRNP U1, U2, U4/U6 and U5. {ECO:0000250}.; . . . . . . . . . . SNRPGP16 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 16 . . . . . . . . . . . SNRPGP17 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 17 . . . . . . . . . . . SNRPGP18 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 18 . . . . . . . . . . . SNRPGP19 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 19 . . . . . . . . . . . SNRPGP20 . . . small nuclear ribonucleoprotein polypeptide G pseudogene 20 . . . . . . . . . . . SNRPN 0.848259450842786 0.151189016149371 0.000551533007842561 small nuclear ribonucleoprotein polypeptide N FUNCTION: May be involved in tissue-specific alternative RNA processing events.; . TISSUE SPECIFICITY: Expressed in brain and lymphoblasts. {ECO:0000269|PubMed:10318933}.; . . 0.69835 0.40044 -0.207437529 38.2814343 3.30329 0.11977 SNTA1 0.428235398198808 0.570235933037457 0.00152866876373538 syntrophin alpha 1 FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5- bisphosphate (By similarity). {ECO:0000250}.; DISEASE: Long QT syndrome 12 (LQT12) [MIM:612955]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. {ECO:0000269|PubMed:18591664, ECO:0000269|PubMed:19684871}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: High expression in skeletal muscle and heart. Low expression in brain, pancreas, liver, kidney and lung. Not detected in placenta.; myocardium;salivary gland;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;pancreas;lung;placenta;liver;spleen;head and neck;kidney;stomach;cerebellum; heart;globus pallidus;caudate nucleus;skeletal muscle; 0.13447 0.13312 -0.358119787 29.16371786 449.98741 4.40862 SNTB1 0.618933425335325 0.380729830501677 0.000336744162998592 syntrophin beta 1 FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8183929}.; . . 0.60685 0.14804 -0.466531444 23.51380042 155.18824 2.72167 SNTB2 0.036218317626175 0.956133756513604 0.00764792586022114 syntrophin beta 2 FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. May play a role in the regulation of secretory granules via its interaction with PTPRN.; . TISSUE SPECIFICITY: Ubiquitous. Isoform 1 is the predominant isoform. Weak level of isoform 2 is present in all tested tissues, except in liver and heart where it is highly expressed.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;testis;germinal center;dura mater;brain;unclassifiable (Anatomical System);meninges;lymph node;heart;blood;lens;skeletal muscle;breast;lung;pia mater;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland; superior cervical ganglion;testis;ciliary ganglion;trigeminal ganglion; 0.78930 0.13982 . . 21.70049 0.73052 SNTG1 0.0379275653329757 0.961775134827846 0.000297299839178276 syntrophin gamma 1 FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex (By similarity). May participate in regulating the subcellular location of diacylglycerol kinase-zeta to ensure that diacylglycerol is rapidly inactivated following receptor activation. {ECO:0000250}.; . TISSUE SPECIFICITY: Brain specific. In CNS, it is expressed in the perikaryon and proximal portion of the neuronal processes. Strong expression in the hippocampus, neuron-rich dendate granule cells, and pyramidal cell layers. Highly expressed in neurons of the cerebral cortex. Also expressed in the cerebellar cortex, deep cerebellar nuclei, thalamus, and basal ganglia. No expression in muscle cells. {ECO:0000269|PubMed:10747910}.; unclassifiable (Anatomical System);lung;brain; . 0.22600 0.11526 0.154398214 64.73814579 90.11517 2.04360 SNTG2 9.17608832343845e-07 0.759197618282907 0.24080146410826 syntrophin gamma 2 FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Strong expression in brain and testis. In CNS, it is expressed in the perikaryon and proximal portion of the neuronal processes. Strong expression in the hippocampus, neuron-rich dendate granule cells, and pyramidal cell layers. Highly expressed in neurons of the cerebral cortex. Also expressed in the cerebellar cortex, deep cerebellar nuclei, thalamus, and basal ganglia. {ECO:0000269|PubMed:10747910}.; unclassifiable (Anatomical System);brain; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.16014 0.14442 1.003094668 90.77022883 4603.28248 13.61395 SNTN 0.00273794435957524 0.566572088933122 0.430689966707302 sentan, cilia apical structure protein FUNCTION: May be a component of the linker structure that bridges the ciliary membrane and peripheral singlet microtubules. {ECO:0000250}.; . . unclassifiable (Anatomical System);prostate;lung;nasopharynx;spinal ganglion; superior cervical ganglion;trachea;atrioventricular node;trigeminal ganglion; . . 0.103030231 61.2762444 98.92125 2.15194 SNU13 . . . SNU13 homolog, small nuclear ribonucleoprotein (U4/U6.U5) FUNCTION: Binds to the 5'-stem-loop of U4 snRNA and may play a role in the late stage of spliceosome assembly. The protein undergoes a conformational change upon RNA-binding. {ECO:0000269|PubMed:10545122, ECO:0000269|PubMed:17412961}.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.34688 . 0.035072054 56.2514744 . . SNUPN 2.17760843039441e-10 0.0690968726571785 0.930903127125061 snurportin 1 FUNCTION: Functions as an U snRNP-specific nuclear import adapter. Involved in the trimethylguanosine (m3G)-cap-dependent nuclear import of U snRNPs. Binds specifically to the terminal m3G-cap U snRNAs. {ECO:0000269|PubMed:9670026}.; . . smooth muscle;ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;skeletal muscle;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;kidney;mammary gland;stomach;thymus; testis - interstitial;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09377 . 0.595326758 82.66100495 286.10981 3.62059 SNURF 0.780882316345501 0.212114772080639 0.00700291157385999 SNRPN upstream reading frame . . TISSUE SPECIFICITY: Expressed in heart, skeletal muscle and lymphoblasts (at protein level). Expressed in brain, pancreas, heart, liver, lung, kidney and skeletal muscle. {ECO:0000269|PubMed:10318933}.; myocardium;lymphoreticular;ovary;sympathetic chain;substantia nigra;skin;retina;bone marrow;prostate;optic nerve;ganglion;frontal lobe;cochlea;endometrium;thyroid;iris;brain;gall bladder;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;colon;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;aorta;stomach;cerebellum; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;pituitary;cerebellum; 0.14643 . -0.031067188 51.03798066 0.63033 0.00911 SNURFL . . . SNRPN upstream reading frame-like (pseudogene) . . . . . . . . . . . SNW1 0.999633196215809 0.000366803598292481 1.85898611868588e-10 SNW domain containing 1 FUNCTION: Involved in transcriptional regulation. Modulates TGF- beta-mediated transcription via association with SMAD proteins, MYOD1-mediated transcription via association with PABPN1, RB1- mediated transcriptional repression, and retinoid-X receptor (RXR)- and vitamin D receptor (VDR)-dependent gene transcription in a cell line-specific manner probably involving coactivators NCOA1 and GRIP1. Is involved in NOTCH1-mediated transcriptional activation. Binds to multimerized forms of Notch intracellular domain (NICD) and is proposed to recruit transcriptional coactivators such as MAML1 to form an intermediate preactivation complex which associates with DNA-bound CBF-1/RBPJ to form a transcriptional activation complex by releasing SNW1 and redundant NOTCH1 NICD. Proposed to be involved in transcriptional activation by EBV EBNA2 of CBF-1/RBPJ-repressed promoters. Is recruited by HIV-1 Tat to Tat:P-TEFb:TAR RNA complexes and is involved in Tat transcription by recruitment of MYC, MEN1 and TRRAP to the HIV promoter. Functions as a splicing factor in pre-mRNA splicing. Is required in the specific splicing of CDKN1A pre-mRNA; the function probbaly involves the recruitment of U2AF2 to the mRNA. Is proposed to recruit PPIL1 to the spliceosome. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269|PubMed:10644367, ECO:0000269|PubMed:11278756, ECO:0000269|PubMed:11371506, ECO:0000269|PubMed:11514567, ECO:0000269|PubMed:12840015, ECO:0000269|PubMed:14985122, ECO:0000269|PubMed:15194481, ECO:0000269|PubMed:15905409, ECO:0000269|PubMed:18794151, ECO:0000269|PubMed:19818711, ECO:0000269|PubMed:21245387, ECO:0000269|PubMed:21460037, ECO:0000269|PubMed:9632709}.; . . lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;nervous;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; testis - interstitial;superior cervical ganglion;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.87546 0.15588 -0.494039303 22.09247464 624.40773 5.04077 SNX1 0.939839944686599 0.0601579902219813 2.06509141955039e-06 sorting nexin 1 FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3- phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (PubMed:12198132). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Can sense membrane curvature and has in vitro vesicle- to-membrane remodeling activity (PubMed:19816406, PubMed:23085988). Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptors (IGF2R, M6PR and SORT1) and Shiginella dysenteria toxin stxB. Plays a role in targeting ligand-activated EGFR to the lysosomes for degradation after endocytosis from the cell surface and release from the Golgi (PubMed:12198132, PubMed:15498486, PubMed:17550970, PubMed:17101778, PubMed:18088323, PubMed:21040701). Involvement in retromer-independent endocytic trafficking of P2RY1 and lysosomal degradation of protease-activated receptor-1/F2R (PubMed:16407403, PubMed:20070609). Promotes KALRN- and RHOG-dependent but retromer- independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN (PubMed:20604901). Required for endocytosis of DRD5 upon agonist stimulation but not for basal receptor trafficking (PubMed:23152498). {ECO:0000269|PubMed:12198132, ECO:0000269|PubMed:15498486, ECO:0000269|PubMed:16407403, ECO:0000269|PubMed:17101778, ECO:0000269|PubMed:17550970, ECO:0000269|PubMed:18088323, ECO:0000269|PubMed:19816406, ECO:0000269|PubMed:20070609, ECO:0000269|PubMed:20604901, ECO:0000269|PubMed:21040701, ECO:0000269|PubMed:23085988, ECO:0000269|PubMed:23152498, ECO:0000303|PubMed:15498486}.; . . ovary;salivary gland;intestine;colon;parathyroid;vein;skin;bone marrow;prostate;atrium;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;islets of Langerhans;pineal body;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum; thyroid;spinal cord;globus pallidus;fetal thyroid;skeletal muscle; 0.75904 0.09617 -0.512444034 21.55579146 118.92704 2.37286 SNX2 0.99794124167631 0.00205874587337484 1.2450315140588e-08 sorting nexin 2 FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3- phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (PubMed:16179610). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex (PubMed:17101778). The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity (PubMed:23085988). Required for retrograde endosome-to-TGN transport of TGN38 (PubMed:20138391). Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN (PubMed:20604901). {ECO:0000269|PubMed:16179610, ECO:0000269|PubMed:17101778, ECO:0000269|PubMed:20138391, ECO:0000269|PubMed:20604901, ECO:0000269|PubMed:23085988, ECO:0000303|PubMed:16179610}.; . . . . 0.33900 0.13169 -0.692458599 14.96815287 25.76147 0.83932 SNX2P1 . . . sorting nexin 2 pseudogene 1 . . . . . . . . . . . SNX2P2 . . . sorting nexin 2 pseudogene 2 . . . . . . . . . . . SNX3 0.466342861502279 0.508649756038103 0.0250073824596182 sorting nexin 3 FUNCTION: Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Also can bind phosphatidylinositol 4-phosphate (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2) (By similarity). Plays a role in protein transport between cellular compartments. Together with RAB7A facilitates endosome membrane association of the retromer cargo-selective subcomplex (CSC/VPS). May in part act as component of the SNX3-retromer complex which mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway (PubMed:21725319, PubMed:24344282). Promotes stability and cell surface expression of epithelial sodium channel (ENAC) subunits SCNN1A and SCNN1G (By similarity). Not involved in EGFR degradation. Involved in the regulation of phagocytosis in dendritic cells possibly by regulating EEA1 recruitment to the nascent phagosomes (PubMed:23237080). Involved in iron homeostasis through regulation of endocytic recycling of the transferrin receptor TFRC presumably by delivering the tranferrin:transferrin receptor complex to recycling endosomes; the function may involve the CSC retromer subcomplex (By similarity). In the case of Salmonella enterica infection plays arole in maturation of the Salmonella-containing vacuole (SCV) and promotes recruitment of LAMP1 to SCVs (PubMed:20482551). {ECO:0000250|UniProtKB:O70492, ECO:0000269|PubMed:11433298, ECO:0000269|PubMed:18767904, ECO:0000269|PubMed:21725319, ECO:0000269|PubMed:23237080, ECO:0000269|PubMed:24344282, ECO:0000305|PubMed:21725319}.; DISEASE: Microphthalmia, syndromic, 8 (MCOPS8) [MIM:601349]: A very rare congenital syndrome characterized by microcephaly, microphthalmia, ectrodactyly of the lower limbs and prognathism. Intellectual deficit has been reported. Microphthalmia is a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. {ECO:0000269|PubMed:12471201}. Note=The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving SNX3 has been found in patients with syndromic microphthalmia. Translocation t(6;13)(q21;q12).; . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;oral cavity;muscle;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; whole brain;amygdala;superior cervical ganglion;subthalamic nucleus;occipital lobe;thalamus;temporal lobe;globus pallidus;caudate nucleus;trigeminal ganglion;parietal lobe;bone marrow; 0.56987 0.15588 0.12325821 62.38499646 2.85375 0.10109 SNX3P1X . . . sorting nexin 3 pseudogene 1, X-linked . . . . . . . . . . . SNX3P1Y . . . sorting nexin 3 pseudogene 1, Y-linked . . . . . . . . . . . SNX4 0.011061878512626 0.988560814775411 0.000377306711963302 sorting nexin 4 FUNCTION: May be involved in several stages of intracellular trafficking. Plays a role in recycling endocytosed transferrin receptor and prevent its degradation. {ECO:0000269|PubMed:17994011}.; . . lymphoreticular;ovary;salivary gland;developmental;intestine;colon;substantia nigra;parathyroid;vein;skin;uterus;prostate;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;hypopharynx;liver;cervix;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion; 0.38016 0.14503 -0.582225231 18.44184949 26.53956 0.85795 SNX5 0.449845570451869 0.549890631079814 0.000263798468317434 sorting nexin 5 FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3- phosphate (PtdIns(3P)) or phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) (PubMed:15561769). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Does not have in vitro vesicle-to-membrane remodeling activity (PubMed:23085988). Involved in retrograde transport of lysosomal enzyme receptor IGF2R (PubMed:17148574, PubMed:18596235). May function as link between endosomal transport vesicles and dynactin (Probable). Plays a role in the internalization of EGFR after EGF stimulation (Probable). Involved in EGFR endosomal sorting and degradation; the function involves PIP5K1C isoform 3 and is retromer-independent (PubMed:23602387). Together with PIP5K1C isoform 3 facilitates HGS interaction with ubiquitinated EGFR, which initiates EGFR sorting to intraluminal vesicles (ILVs) of the multivesicular body for subsequent lysosomal degradation (Probable). Involved in E-cadherin sorting and degradation; inhibits PIP5K1C isoform 3-mediated E-cadherin degradation (PubMed:24610942). Plays a role in macropinocytosis (PubMed:18854019, PubMed:21048941). {ECO:0000269|PubMed:18854019, ECO:0000269|PubMed:21048941, ECO:0000269|PubMed:24610942, ECO:0000303|PubMed:15561769, ECO:0000303|PubMed:19619496, ECO:0000303|PubMed:23085988}.; . . . . 0.11006 0.20781 -0.247889024 35.98726115 151.29075 2.68937 SNX5P1 . . . sorting nexin 5 pseudogene 1 . . . . . . . . . . . SNX5P2 . . . sorting nexin 5 pseudogene 2 . . . . . . . . . . . SNX6 0.965428129158632 0.034571355393625 5.15447742990564e-07 sorting nexin 6 FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate (Probable). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex (PubMed:19935774). The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Does not have in vitro vesicle-to-membrane remodeling activity (PubMed:23085988). Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptor IGF2R (PubMed:17148574). May function as link between transport vesicles and dynactin (Probable). Negatively regulates retrograde transport of BACE1 from the cell surface to the trans-Golgi network (PubMed:20354142). Involved in E-cadherin sorting and degradation; inhibits PIP5K1C isoform 3-mediated E-cadherin degradation (PubMed:24610942). In association with GIT1 involved in EGFR degradation. Promotes lysosomal degradation of CDKN1B (By similarity). May contribute to transcription regulation (Probable). {ECO:0000250|UniProtKB:Q6P8X1, ECO:0000269|PubMed:17148574, ECO:0000269|PubMed:19935774, ECO:0000269|PubMed:20354142, ECO:0000269|PubMed:23085988, ECO:0000269|PubMed:24610942, ECO:0000303|PubMed:19935774, ECO:0000303|PubMed:20830743, ECO:0000305}.; . . ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;cornea;placenta;hypopharynx;amnion;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;placenta;spinal cord;white blood cells;whole blood;trigeminal ganglion; 0.26451 0.09729 -0.229483771 36.86010852 13.07663 0.47592 SNX6P1 . . . sorting nexin 6 pseudogene 1 . . . . . . . . . . . SNX7 0.0288388617246868 0.960436827194555 0.0107243110807577 sorting nexin 7 FUNCTION: May be involved in several stages of intracellular trafficking.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;vein;skin;bile duct;uterus;pancreas;whole body;lung;frontal lobe;cochlea;endometrium;placenta;visual apparatus;hippocampus;testis;amniotic fluid;kidney;brain;mammary gland;bladder;stomach; . 0.29144 0.08752 0.018483465 55.44939844 558.45821 4.79951 SNX8 0.165170968578774 0.831782233052209 0.00304679836901673 sorting nexin 8 FUNCTION: May be involved in several stages of intracellular trafficking. May play a role in intracellular protein transport from early endosomes to the trans-Golgi network. {ECO:0000269|PubMed:19782049}.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;colon;parathyroid;vein;skin;retina;uterus;prostate;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;lens;bile duct;pancreas;lung;placenta;visual apparatus;duodenum;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.16684 0.11365 0.376678994 75.50719509 357.15648 4.00401 SNX9 0.578575161358935 0.421420902786246 3.93585481919118e-06 sorting nexin 9 FUNCTION: Involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Promotes internalization of TNFR. Promotes degradation of EGFR after EGF signaling. Stimulates the GTPase activity of DNM1. Promotes DNM1 oligomerization. Promotes activation of the Arp2/3 complex by WASL, and thereby plays a role in the reorganization of the F- actin cytoskeleton. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Has lower affinity for membranes enriched in phosphatidylinositol 3-phosphate. {ECO:0000269|PubMed:11799118, ECO:0000269|PubMed:12952949, ECO:0000269|PubMed:15703209, ECO:0000269|PubMed:17609109, ECO:0000269|PubMed:17948057, ECO:0000269|PubMed:18388313, ECO:0000269|PubMed:20427313, ECO:0000269|PubMed:21048941, ECO:0000269|PubMed:22718350}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in heart and placenta, and lowest levels in thymus and peripheral blood leukocytes. {ECO:0000269|PubMed:10531379}.; lymphoreticular;myocardium;ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;lacrimal gland;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;duodenum;liver;cervix;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; . 0.17325 0.17964 -0.134019284 43.90776126 110.76986 2.29269 SNX10 0.00585750531238308 0.90310285806901 0.0910396366186071 sorting nexin 10 FUNCTION: Probable phosphoinositide-binding protein involved in protein sorting and membrane trafficking in endosomes. Plays a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium. Required for the localization to the cilium of V-ATPase subunit ATP6V1D and ATP6V0D1, and RAB8A. Involved in osteoclast differentiation and therefore bone resorption. {ECO:0000269|PubMed:17012226, ECO:0000269|PubMed:21844891, ECO:0000269|PubMed:22499339}.; DISEASE: Osteopetrosis, autosomal recessive 8 (OPTB8) [MIM:615085]: A rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Recessive osteopetrosis commonly manifests in early infancy with macrocephaly, feeding difficulties, evolving blindness and deafness, bone marrow failure, severe anemia, and hepatosplenomegaly. Deafness and blindness are generally thought to represent effects of pressure on nerves. OPTB8 is clinically characterized by dense bones with no distinction between outer and inner plates, due to extensive encroachment of cortical bone into the medullary space, increased head circumference, broad open fontanelle, frontal bossing, and hepatosplenomegaly. Osteoclasts number is low and their bone resorptive capacity is impaired. {ECO:0000269|PubMed:22499339, ECO:0000269|PubMed:23123320, ECO:0000269|PubMed:23280965}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;small intestine;tongue;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland; amygdala;whole brain;thalamus;occipital lobe;hypothalamus;temporal lobe;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;whole blood;parietal lobe;cingulate cortex; 0.20884 0.11262 -0.09720619 46.20193442 18.74629 0.64699 SNX11 3.85654523915294e-05 0.830982367759887 0.168979066787722 sorting nexin 11 FUNCTION: Phosphoinositide-binding protein involved in protein sorting and membrane trafficking in endosomes. {ECO:0000269|PubMed:23615901}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;atrioventricular node; 0.09179 . -0.383807564 27.41802312 21.28332 0.71923 SNX12 0.695492431895904 0.287205454904162 0.0173021131999336 sorting nexin 12 FUNCTION: May be involved in several stages of intracellular trafficking. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;salivary gland;muscle;intestine;pharynx;colon;parathyroid;blood;skin;skeletal muscle;breast;prostate;lung;placenta;visual apparatus;liver;cervix;kidney;brain;bladder;stomach; superior cervical ganglion; 0.16096 0.11401 0.035072054 56.2514744 1.18187 0.03366 SNX13 0.985321607862615 0.0146783895939089 2.54347642327565e-09 sorting nexin 13 FUNCTION: May be involved in several stages of intracellular trafficking. May play a role in endosome homeostasis (By similarity). Acts as a GAP for Galphas. {ECO:0000250, ECO:0000269|PubMed:11729322}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;larynx;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;head and neck;kidney;stomach;thymus; dorsal root ganglion;medulla oblongata;testis - interstitial;superior cervical ganglion;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;appendix;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.56654 0.13168 -0.44448505 24.46331682 69.81149 1.73358 SNX14 6.79995024969682e-10 0.998315053847262 0.00168494547274319 sorting nexin 14 FUNCTION: Plays a role in maintaining normal neuronal excitability and synaptic transmission. May be involved in several stages of intracellular trafficking (By similarity). Required for autophagosome clearance, possibly by mediating the fusion of lysosomes with autophagosomes (Probable). Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), a key component of late endosomes/lysosomes (PubMed:25848753). Does not bind phosphatidylinositol 3-phosphate (PtdIns(3P)) (PubMed:25848753, PubMed:25148684). {ECO:0000250|UniProtKB:Q8BHY8, ECO:0000269|PubMed:25148684, ECO:0000269|PubMed:25848753, ECO:0000305|PubMed:25848753}.; . TISSUE SPECIFICITY: Widely expressed both in fetal and adult tissues. {ECO:0000269|PubMed:25848753}.; lymphoreticular;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;amnion;liver;spleen;head and neck;kidney;aorta;stomach;thymus; . 0.16810 0.10829 -0.488577883 22.64685067 150.07757 2.67167 SNX15 0.000705751006111747 0.918265162362359 0.0810290866315297 sorting nexin 15 FUNCTION: May be involved in several stages of intracellular trafficking. Overexpression of SNX15 disrupts the normal trafficking of proteins from the plasma membrane to recycling endosomes or the TGN. {ECO:0000269|PubMed:11085978}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11085978}.; unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;blood;lens;skin;skeletal muscle;bone marrow;uterus;prostate;whole body;lung;synovium;mesenchyma;larynx;bone;thyroid;placenta;visual apparatus;liver;testis;cervix;head and neck;kidney;brain;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin; 0.17856 0.15372 0.196671391 67.19155461 882.75485 5.78759 SNX16 4.22457640928623e-08 0.10978915804966 0.890210799704576 sorting nexin 16 FUNCTION: May be involved in several stages of intracellular trafficking. Plays a role in protein transport from early to late endosomes. Plays a role in protein transport to the lysosome. Promotes degradation of EGFR after EGF signaling. Plays a role in intracellular transport of vesicular stomatitis virus nucleocapsids from the endosome to the cytoplasm. {ECO:0000269|PubMed:12813048, ECO:0000269|PubMed:15951806}.; . TISSUE SPECIFICITY: Detected in placenta, lung, liver,heart and pancreas. {ECO:0000269|PubMed:12813048}.; unclassifiable (Anatomical System);lymph node;cartilage;blood;skin;uterus;whole body;lung;endometrium;larynx;placenta;testis;head and neck;germinal center;kidney;mammary gland;cerebellum; trigeminal ganglion; 0.57975 0.12480 0.549415813 81.38122199 114.10083 2.32822 SNX17 0.686180301198043 0.313783013228996 3.66855729615157e-05 sorting nexin 17 FUNCTION: Critical regulator of endosomal recycling of numerous receptors, channels, and other transmembrane proteins. Binds to NPxY sequences in the cytoplasmic tails of target cargos. Plays a role in the sorting of endocytosed LRP1 and APP, and prevents their degradation. Required for maintenance of normal cell surface levels of APP and LRP1. Recycles internalized integrins ITGB1, ITGB5 and their associated alpha subunits, preventing them from lysosomal degradation. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)). {ECO:0000269|PubMed:15121882, ECO:0000269|PubMed:15769472, ECO:0000269|PubMed:16712798, ECO:0000269|PubMed:19005208, ECO:0000269|PubMed:21512128, ECO:0000269|PubMed:22492727}.; . . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;prostate;frontal lobe;thyroid;iris;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;pineal body;blood;lens;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;uterus;cerebral cortex;synovium;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;thymus;cerebellum; whole brain;superior cervical ganglion;lung;heart;liver;white blood cells; 0.44161 0.11670 0.042348793 57.31304553 118.60339 2.36980 SNX18 0.146597452225803 0.835344940163524 0.0180576076106728 sorting nexin 18 FUNCTION: Involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Stimulates the GTPase activity of DNM2. Promotes DNM2 location at the plasma membrane. {ECO:0000269|PubMed:18411244, ECO:0000269|PubMed:20427313, ECO:0000269|PubMed:21048941, ECO:0000269|PubMed:22718350}.; . . unclassifiable (Anatomical System);uterus;frontal lobe;colon;skeletal muscle; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.25780 0.09796 -0.268115223 34.70747818 92.20668 2.06534 SNX18P1Y . . . sorting nexin 18 pseudogene 1, Y-linked . . . . . . . . . . . SNX18P2 . . . sorting nexin 18 pseudogene 2 . . . . . . . . . . . SNX18P3 . . . sorting nexin 18 pseudogene 3 . . . . . . . . . . . SNX18P4 . . . sorting nexin 18 pseudogene 4 . . . . . . . . . . . SNX18P5 . . . sorting nexin 18 pseudogene 5 . . . . . . . . . . . SNX18P7 . . . sorting nexin 18 pseudogene 7 . . . . . . . . . . . SNX18P8 . . . sorting nexin 18 pseudogene 8 . . . . . . . . . . . SNX18P9 . . . sorting nexin 18 pseudogene 9 . . . . . . . . . . . SNX18P10 . . . sorting nexin 18 pseudogene 10 . . . . . . . . . . . SNX18P11 . . . sorting nexin 18 pseudogene 11 . . . . . . . . . . . SNX18P12 . . . sorting nexin 18 pseudogene 12 . . . . . . . . . . . SNX18P13 . . . sorting nexin 18 pseudogene 13 . . . . . . . . . . . SNX18P14 . . . sorting nexin 18 pseudogene 14 . . . . . . . . . . . SNX18P15 . . . sorting nexin 18 pseudogene 15 . . . . . . . . . . . SNX18P16 . . . sorting nexin 18 pseudogene 16 . . . . . . . . . . . SNX18P17 . . . sorting nexin 18 pseudogene 17 . . . . . . . . . . . SNX18P18 . . . sorting nexin 18 pseudogene 18 . . . . . . . . . . . SNX18P19 . . . sorting nexin 18 pseudogene 19 . . . . . . . . . . . SNX18P20 . . . sorting nexin 18 pseudogene 20 . . . . . . . . . . . SNX18P21 . . . sorting nexin 18 pseudogene 21 . . . . . . . . . . . SNX18P22 . . . sorting nexin 18 pseudogene 22 . . . . . . . . . . . SNX18P23 . . . sorting nexin 18 pseudogene 23 . . . . . . . . . . . SNX18P24 . . . sorting nexin 18 pseudogene 24 . . . . . . . . . . . SNX18P25 . . . sorting nexin 18 pseudogene 25 . . . . . . . . . . . SNX18P26 . . . sorting nexin 18 pseudogene 26 . . . . . . . . . . . SNX18P27 . . . sorting nexin 18 pseudogene 27 . . . . . . . . . . . SNX19 9.83338246488835e-07 0.98323969345938 0.016759323202374 sorting nexin 19 FUNCTION: Plays a role in intracellular vesicle trafficking and exocytosis (PubMed:24843546). May play a role in maintaining insulin-containing dense core vesicles in pancreatic beta-cells and in preventing their degradation. May play a role in insulin secretion (PubMed:24843546). Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) (By similarity). {ECO:0000250|UniProtKB:Q6P4T1, ECO:0000269|PubMed:24843546}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;iris;pituitary gland;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;testis;trigeminal ganglion; 0.10262 0.09729 1.36500134 94.4621373 4026.36522 12.56696 SNX19P1 . . . sorting nexin 19 pseudogene 1 . . . . . . . . . . . SNX19P2 . . . sorting nexin 19 pseudogene 2 . . . . . . . . . . . SNX19P3 . . . sorting nexin 19 pseudogene 3 . . . . . . . . . . . SNX19P4 . . . sorting nexin 19 pseudogene 4 . . . . . . . . . . . SNX20 4.12728270614269e-05 0.393571530450777 0.606387196722162 sorting nexin 20 FUNCTION: May play a role in cellular vesicle trafficking. Has been proposed to function as a sorting protein that targets SELPLG into endosomes, but has no effect on SELPLG internalization from the cell surface, or on SELPLG-mediated cell-cell adhesion. {ECO:0000305|PubMed:18196517}.; . . unclassifiable (Anatomical System);uterus;lymph node;lung;heart;endometrium;testis;spleen;blood;kidney;germinal center;mammary gland;skin;bone marrow; superior cervical ganglion;pons;trigeminal ganglion;parietal lobe; 0.15581 0.10782 0.595326758 82.66100495 270.3898 3.52705 SNX21 0.0208140161677358 0.905792756899246 0.0733932269330187 sorting nexin family member 21 FUNCTION: Binds to membranes enriched in phosphatidylinositol 3- phosphate (PtdIns(P3)) and phosphatidylinositol 4,5-bisphosphate. May be involved in several stages of intracellular trafficking. {ECO:0000250|UniProtKB:Q3UR97}.; . TISSUE SPECIFICITY: Highly expressed in fetus liver, but only weakly expressed in brain, skeleton muscle, smooth muscle, and cardiac muscle, kidney, and adrenal gland. {ECO:0000269|PubMed:12459172}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;cerebellum cortex;islets of Langerhans;pineal body;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;macula lutea;hippocampus;alveolus;liver;spleen;kidney;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;pons;skeletal muscle; 0.15776 0.09401 0.108486928 61.90728946 3287.53968 10.94596 SNX22 0.00792254750515989 0.784874759481603 0.207202693013237 sorting nexin 22 FUNCTION: May be involved in several stages of intracellular trafficking (By similarity). Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)). {ECO:0000250}.; . . unclassifiable (Anatomical System);smooth muscle;cartilage;ovary;heart;islets of Langerhans;colon;blood;choroid;skin;uterus;prostate;lung;nasopharynx;bone;thyroid;placenta;visual apparatus;liver;testis;spleen;germinal center;kidney;brain;mammary gland;bladder;tonsil; . 0.10319 0.08141 -0.029247611 51.40363293 33.01003 1.02171 SNX24 0.00139280727569243 0.867312778943503 0.131294413780805 sorting nexin 24 FUNCTION: May be involved in several stages of intracellular trafficking. {ECO:0000250}.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;skin;uterus;prostate;cochlea;bone;thyroid;testis;brain;pineal gland;unclassifiable (Anatomical System);trophoblast;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; spinal cord; 0.19600 0.10465 -0.075159878 47.78839349 3.22925 0.11635 SNX25 5.35420238191736e-05 0.999669056849776 0.000277401126404786 sorting nexin 25 FUNCTION: May be involved in several stages of intracellular trafficking. {ECO:0000250}.; . . medulla oblongata;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;cochlea;thyroid;bone;testis;germinal center;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pineal body;blood;lens;skeletal muscle;lung;nasopharynx;placenta;macula lutea;liver;spleen;cervix;kidney;stomach; atrioventricular node;skin; 0.09136 0.07421 -0.174473069 40.59919792 343.46646 3.92874 SNX25P1 . . . sorting nexin 25 pseudogene 1 . . . . . . . . . . . SNX27 0.999884818815405 0.000115181129934054 5.46611403901569e-11 sorting nexin family member 27 FUNCTION: Involved in the retrograde transport from endosome to plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. Following internalization, endocytosed transmembrane proteins are delivered to early endosomes and recycled to the plasma membrane instead of being degraded in lysosomes. SNX27 specifically binds and directs sorting of a subset of transmembrane proteins containing a PDZ- binding motif at the C-terminus: following interaction with target transmembrane proteins, associates with the retromer complex, preventing entry into the lysosomal pathway, and promotes retromer-tubule based plasma membrane recycling. SNX27 also binds with the WASH complex. Interacts with membranes containing phosphatidylinositol-3-phosphate (PtdIns(3P)). May participate in establishment of natural killer cell polarity. Recruits CYTIP to early endosomes. {ECO:0000269|PubMed:17351151, ECO:0000269|PubMed:20733053, ECO:0000269|PubMed:21300787, ECO:0000269|PubMed:21303929, ECO:0000269|PubMed:21602791, ECO:0000269|PubMed:21926430, ECO:0000269|PubMed:22411990, ECO:0000269|PubMed:23563491}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in cells of hematopoietic origin (at protein level). {ECO:0000269|PubMed:17351151, ECO:0000269|PubMed:17577583, ECO:0000269|PubMed:21300787}.; . . 0.15526 0.08511 0.060756528 58.52795471 39.61796 1.16770 SNX29 1.78492586400224e-06 0.992709756469735 0.00728845860440096 sorting nexin 29 . . . lymphoreticular;smooth muscle;ovary;adrenal medulla;colon;parathyroid;choroid;fovea centralis;skin;retina;bone marrow;prostate;optic nerve;endometrium;iris;testis;germinal center;pineal gland;bladder;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;blood;lens;lung;nasopharynx;placenta;visual apparatus;macula lutea;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.22646 . -0.556537043 19.72753008 208.69672 3.11731 SNX29P1 . . . sorting nexin 29 pseudogene 1 . . . unclassifiable (Anatomical System);lymphoreticular;prostate;nasopharynx;adrenal medulla;blood;germinal center;stomach;tonsil; . 0.15175 . . . . . SNX29P2 . . . sorting nexin 29 pseudogene 2 . . . unclassifiable (Anatomical System);uterus;lymphoreticular;prostate;nasopharynx;adrenal medulla;blood;germinal center;stomach;tonsil; . . . . . . . SNX30 0.970626802540167 0.0293648032666748 8.39419315815352e-06 sorting nexin family member 30 FUNCTION: May be involved in several stages of intracellular trafficking. {ECO:0000250}.; . . . . 0.14052 . -0.448125345 24.19202642 48.74157 1.36201 SNX31 1.95703250355648e-10 0.223618292195192 0.776381707609105 sorting nexin 31 FUNCTION: May be involved in protein trafficking. {ECO:0000250}.; . . unclassifiable (Anatomical System);placenta;urinary;pituitary gland;brain;bladder; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05455 0.06137 0.532823122 80.96249115 4885.09725 14.21506 SNX32 2.72866806441788e-13 0.0362562290690697 0.963743770930657 sorting nexin 32 FUNCTION: May be involved in several stages of intracellular trafficking. {ECO:0000250}.; . . unclassifiable (Anatomical System);epididymis;hypothalamus;hippocampus;brain; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;parietal lobe; 0.10723 0.11163 -0.821100135 11.88369899 75.73269 1.82219 SNX33 0.00675714431845481 0.916400672217001 0.0768421834645446 sorting nexin 33 FUNCTION: Plays a role in the reorganization of the cytoskeleton, endocytosis and cellular vesicle trafficking via its interactions with membranes, WASL, DNM1 and DNM2. Acts both during interphase and at the end of mitotic cell divisions. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Modulates endocytosis of cell-surface proteins, such as APP and PRNP; this then modulates the secretion of APP and PRNP peptides. Promotes membrane tubulation (in vitro). May promote the formation of macropinosomes. {ECO:0000269|PubMed:18353773, ECO:0000269|PubMed:18419754, ECO:0000269|PubMed:19487689, ECO:0000269|PubMed:20964629, ECO:0000269|PubMed:21048941, ECO:0000269|PubMed:22718350}.; . TISSUE SPECIFICITY: Detected in heart and pancreas. {ECO:0000269|PubMed:18353773}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;bone;testis;brain;unclassifiable (Anatomical System);cartilage;hypothalamus;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;cervix;spleen;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;occipital lobe;globus pallidus;ciliary ganglion;caudate nucleus;pons;atrioventricular node;trigeminal ganglion; 0.14992 0.11525 -0.666770504 15.86459071 60.90515 1.58681 SNX33P1 . . . sorting nexin 33 pseudogene 1 . . . . . . . . . . . SOAT1 1.665002779751e-05 0.966587479622716 0.033395870349486 sterol O-acyltransferase 1 FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase.; . . . . 0.09058 0.50106 -0.286522835 33.47487615 1212.8663 6.59070 SOAT2 9.10116639624956e-18 0.00432030230645413 0.995679697693546 sterol O-acyltransferase 2 FUNCTION: Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa.; . TISSUE SPECIFICITY: Expression seems confined in hepatocytes and enterocytes. {ECO:0000269|PubMed:16331323}.; unclassifiable (Anatomical System);liver;spleen; fetal liver;superior cervical ganglion; 0.39268 0.20973 0.180083178 66.16536919 2123.70169 8.48375 SOBP . . . sine oculis binding protein homolog FUNCTION: Implicated in development of the cochlea. {ECO:0000250|UniProtKB:Q0P5V2}.; DISEASE: Mental retardation, anterior maxillary protrusion, and strabismus (MRAMS) [MIM:613671]: A syndrome characterized by severe mental retardation, strabismus and dysmorphic features such as anterior maxillary protrusion with vertical maxillary excess, open bite and prominent crowded teeth. Some patients may lack dysmorphic features and manifest temporal lobe epilepsy and psychosis. Esotropia and amblyopia are present in some individuals. {ECO:0000269|PubMed:21035105}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;frontal lobe;ovary;islets of Langerhans;visual apparatus;hypopharynx;testis;colon;head and neck;germinal center;brain;skeletal muscle; whole brain;amygdala;occipital lobe;medulla oblongata;cerebellum peduncles;temporal lobe;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.15607 0.10424 0.128714042 63.19886766 219.08822 3.20002 SOCS1 0.541775584805038 0.402035225065709 0.0561891901292528 suppressor of cytokine signaling 1 FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS1 is involved in negative regulation of cytokines that signal through the JAK/STAT3 pathway. Through binding to JAKs, inhibits their kinase activity. In vitro, also suppresses Tec protein- tyrosine activity. Appears to be a major regulator of signaling by interleukin 6 (IL6) and leukemia inhibitory factor (LIF). Regulates interferon-gamma mediated sensory neuron survival (By similarity). Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Seems to recognize JAK2. SOCS1 appears to be a negative regulator in IGF1R signaling pathway. {ECO:0000250, ECO:0000269|PubMed:11278610, ECO:0000269|PubMed:11313480}.; . TISSUE SPECIFICITY: Expressed in all tissues with high expression in spleen, small intestine and peripheral blood leukocytes.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;lung;placenta;macula lutea;cervix;kidney;thymus; . 0.17071 0.54429 . . 13.75813 0.50027 SOCS2 0.0985304077058318 0.771419505293697 0.130050087000472 suppressor of cytokine signaling 2 FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS2 appears to be a negative regulator in the growth hormone/IGF1 signaling pathway. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin- protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.; . TISSUE SPECIFICITY: High expression in heart, placenta, lung, kidney and prostate.; myocardium;ovary;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;breast;bile duct;pancreas;lung;nasopharynx;placenta;hypopharynx;liver;spleen;head and neck;cervix;kidney;stomach; uterus;prostate;uterus corpus;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.56362 0.48184 0.191216164 66.57230479 280.82696 3.59054 SOCS2-AS1 . . . SOCS2 antisense RNA 1 . . . . . . . . . . . SOCS2P1 . . . suppressor of cytokine signaling 2 pseudogene 1 . . . . . . . . . . . SOCS2P2 . . . suppressor of cytokine signaling 2 pseudogene 2 . . . . . . . . . . . SOCS3 0.576558158731858 0.378948919479431 0.0444929217887111 suppressor of cytokine signaling 3 FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. Binding to JAK2 inhibits its kinase activity. Suppresses fetal liver erythropoiesis. Regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells. Regulates IL-6 signaling in vivo (By similarity). Probable substrate recognition component of a SCF-like ECS (Elongin BC- CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Seems to recognize IL6ST (By similarity). {ECO:0000250, ECO:0000269|PubMed:15601820}.; DISEASE: Note=There is some evidence that SOCS3 may be a susceptibility gene for atopic dermatitis linked to 17q25. SOCS3 messenger RNA is significantly more highly expressed in skin from patients with atopic dermatitis than in skin from healthy controls. Furthermore, a genetic association between atopic dermatitis and a haplotype in the SOCS3 gene has been found in two independent groups of patients. {ECO:0000269|PubMed:16685656}.; TISSUE SPECIFICITY: Widely expressed with high expression in heart, placenta, skeletal muscle, peripheral blood leukocytes, fetal and adult lung, and fetal liver and kidney. Lower levels in thymus.; ovary;salivary gland;intestine;colon;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;iris;pituitary gland;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;breast;lung;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle; 0.82302 0.65495 -0.031067188 51.03798066 16.83964 0.59295 SOCS4 1.85889470977039e-06 0.438738145318723 0.561259995786567 suppressor of cytokine signaling 4 FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. Substrate-recognition component of a SCF-like ECS (Elongin BC- CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Inhibits EGF signaling by mediating the degradation of the Tyr-phosphorylated EGF receptor/EGFR. {ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:17997974}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15700 0.16033 -0.424258538 25.56027365 16.08586 0.56959 SOCS5 0.410273257241663 0.587975120696759 0.00175162206157762 suppressor of cytokine signaling 5 FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. May be a substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Inhibits for instance EGF signaling by mediating the degradation of the EGF receptor/EGFR. Involved in the regulation of T-helper cell differentiation by inhibiting of the IL4 signaling pathway which promotes differentiation into the Th2 phenotype. Can also partially inhibit IL6 and LIF signaling. {ECO:0000269|PubMed:15590694}.; . . ovary;salivary gland;intestine;colon;skin;retina;uterus;prostate;atrium;endometrium;larynx;bone;testis;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;pharynx;blood;breast;pancreas;lung;mesenchyma;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;medulla oblongata;ciliary ganglion;trigeminal ganglion;skeletal muscle;cerebellum; 0.68505 0.23227 -0.979072682 8.752064166 24.52698 0.80578 SOCS5P1 . . . suppressor of cytokine signaling 5 pseudogene 1 . . . . . . . . . . . SOCS5P2 . . . suppressor of cytokine signaling 5 pseudogene 2 . . . . . . . . . . . SOCS5P3 . . . suppressor of cytokine signaling 5 pseudogene 3 . . . . . . . . . . . SOCS5P4 . . . suppressor of cytokine signaling 5 pseudogene 4 . . . . . . . . . . . SOCS5P5 . . . suppressor of cytokine signaling 5 pseudogene 5 . . . . . . . . . . . SOCS6 0.879897418286163 0.118668950016792 0.00143363169704555 suppressor of cytokine signaling 6 FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. May be a substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Regulates KIT degradation by ubiquitination of the tyrosine-phosphorylated receptor. {ECO:0000250, ECO:0000269|PubMed:21030588}.; . . . . 0.18957 0.17505 -1.023168368 7.944090587 42.42944 1.23299 SOCS7 0.998970598224364 0.0010293904201282 1.13555081145572e-08 suppressor of cytokine signaling 7 FUNCTION: Regulates signaling cascades probably through protein ubiquitination and/or sequestration. Functions in insulin signaling and glucose homeostasis through IRS1 ubiquitination and subsequent proteasomal degradation. Inhibits also prolactin, growth hormone and leptin signaling by preventing STAT3 and STAT5 activation, sequestering them in the cytoplasm and reducing their binding to DNA. May be a substrate recognition component of a SCF- like E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:15677474, ECO:0000269|PubMed:16127460}.; . TISSUE SPECIFICITY: Expressed in brain and leukocytes. Also in fetal lung fibroblasts and fetal brain. {ECO:0000269|PubMed:9344857}.; unclassifiable (Anatomical System);breast;uterus;prostate;lung;ovary;heart;thyroid;testis;blood;kidney;skin; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.29482 0.15726 . . 481.71204 4.52349 SOD1 0.442188723698817 0.528219598806103 0.0295916774950802 superoxide dismutase 1, soluble FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.; DISEASE: Amyotrophic lateral sclerosis 1 (ALS1) [MIM:105400]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. {ECO:0000269|PubMed:10430435, ECO:0000269|PubMed:10732812, ECO:0000269|PubMed:11369193, ECO:0000269|PubMed:11535232, ECO:0000269|PubMed:12402272, ECO:0000269|PubMed:14506936, ECO:0000269|PubMed:21220647, ECO:0000269|PubMed:21247266, ECO:0000269|PubMed:7496169, ECO:0000269|PubMed:7501156, ECO:0000269|PubMed:7647793, ECO:0000269|PubMed:7655468, ECO:0000269|PubMed:7655469, ECO:0000269|PubMed:7655471, ECO:0000269|PubMed:7700376, ECO:0000269|PubMed:7795609, ECO:0000269|PubMed:7836951, ECO:0000269|PubMed:7870076, ECO:0000269|PubMed:7881433, ECO:0000269|PubMed:7887412, ECO:0000269|PubMed:7951252, ECO:0000269|PubMed:7980516, ECO:0000269|PubMed:7997024, ECO:0000269|PubMed:8069312, ECO:0000269|PubMed:8179602, ECO:0000269|PubMed:8351519, ECO:0000269|PubMed:8446170, ECO:0000269|PubMed:8528216, ECO:0000269|PubMed:8682505, ECO:0000269|PubMed:8907321, ECO:0000269|PubMed:8938700, ECO:0000269|PubMed:8990014, ECO:0000269|PubMed:9101297, ECO:0000269|PubMed:9131652, ECO:0000269|PubMed:9455977}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;lymphoreticular;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; whole brain;amygdala;thalamus;occipital lobe;hypothalamus;spinal cord;caudate nucleus;subthalamic nucleus;adrenal gland;liver;prefrontal cortex;globus pallidus;kidney;cingulate cortex;parietal lobe; 0.43445 0.95383 -0.075159878 47.78839349 2.83815 0.10064 SOD1P1 . . . superoxide dismutase 1, soluble pseudogene 1 . . . . . . . . . . . SOD1P2 . . . superoxide dismutase 1, soluble pseudogene 2 . . . . . . . . . . . SOD1P3 . . . superoxide dismutase 1, soluble pseudogene 3 . . . . . . . . . . . SOD2 0.237154646295316 0.730571963475125 0.0322733902295592 superoxide dismutase 2, mitochondrial FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. {ECO:0000269|PubMed:10334867}.; DISEASE: Microvascular complications of diabetes 6 (MVCD6) [MIM:612634]: Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end- stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. {ECO:0000269|PubMed:12624725}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;oesophagus;larynx;bone;thyroid;testis;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;smooth muscle;beta cell islets;fetal lung;ciliary ganglion;trigeminal ganglion;whole blood;skeletal muscle; 0.66674 . 0.25917371 70.05779665 2050.40796 8.34655 SOD2P1 . . . superoxide dismutase 2, mitochondrial pseudogene 1 . . . . . . . . . . . SOD3 0.223646616064723 0.647193437526755 0.129159946408522 superoxide dismutase 3, extracellular FUNCTION: Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.; . TISSUE SPECIFICITY: Expressed in blood vessels, heart, lung, kidney and placenta. Major SOD isoenzyme in extracellular fluids such as plasma, lymph and synovial fluid.; . . 0.21348 0.10616 . . 1559.49109 7.31537 SOGA1 0.997564311741111 0.00243568749071468 7.68174526391986e-10 suppressor of glucose, autophagy associated 1 FUNCTION: Regulates autophagy by playing a role in the reduction of glucose production in an adiponectin- and insulin-dependent manner. {ECO:0000250}.; . . . . 0.44816 0.10923 . . 627.26532 5.04786 SOGA3 . . . SOGA family member 3 . . . . . 0.18194 . -0.580403979 18.58928993 111.36927 2.29797 SOHLH1 0.0104189866654002 0.945098045674776 0.0444829676598237 spermatogenesis and oogenesis specific basic helix-loop-helix 1 FUNCTION: Transcription factor expressed in undifferentiated spermatogonia required for spermatogonial development. {ECO:0000250}.; DISEASE: Note=Genetic variations in SOHLH1 may be associated with non-obstructive azoospermia. {ECO:0000269|PubMed:20506135}.; . testis; . 0.08113 0.08555 0.068033485 59.0351498 109.60074 2.27503 SOHLH2 0.429898601119812 0.568591868544297 0.00150953033589015 spermatogenesis and oogenesis specific basic helix-loop-helix 2 FUNCTION: Probable transcription factor, which may be involved in spermatogenesis and oogenesis. {ECO:0000250}.; . . unclassifiable (Anatomical System);testis; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;testis;pons;atrioventricular node; 0.18962 0.08203 0.108486928 61.90728946 . . SON 0.999999910132538 8.98674620922816e-08 2.97632768339336e-19 SON DNA binding protein FUNCTION: RNA-binding protein that acts as a mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. Specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Probably acts by facilitating the interaction between Serine/arginine-rich proteins such as SRSF2 and the RNA polymerase II. Also binds to DNA; binds to the consensus DNA sequence: 5'- GA[GT]AN[CG][AG]CC-3'. May indirectly repress hepatitis B virus (HBV) core promoter activity and transcription of HBV genes and production of HBV virions. {ECO:0000269|PubMed:20581448, ECO:0000269|PubMed:21504830}.; . TISSUE SPECIFICITY: Widely expressed, with the higher expression seen in leukocyte and heart.; lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; uterus;superior cervical ganglion;subthalamic nucleus;placenta;white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.88240 0.10113 -1.880110746 1.993394669 1433.40927 7.06767 SONP1 . . . SON pseudogene 1 . . . . . . . . . . . SORBS1 2.14384718511001e-08 0.999997565330488 2.4132310398521e-06 sorbin and SH3 domain containing 1 FUNCTION: Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin- stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions (By similarity). {ECO:0000250|UniProtKB:Q62417}.; . TISSUE SPECIFICITY: Detected in skeletal muscle (at protein level). Widely expressed with highest levels in heart and skeletal muscle. {ECO:0000269|PubMed:11374898, ECO:0000269|PubMed:17462669}.; myocardium;ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;thyroid;testis;spinal ganglion;brain;artery;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;lens;skeletal muscle;lung;epididymis;placenta;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;olfactory bulb;spinal cord;temporal lobe;prefrontal cortex;ciliary ganglion;caudate nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.33294 0.16155 0.483089098 79.05166313 848.56499 5.69349 SORBS2 0.0888062839921232 0.911190570435963 3.14557191353223e-06 sorbin and SH3 domain containing 2 FUNCTION: Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1 or with AKT1 and PAK1, thus mediating AKT1-mediated activation of PAK1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (PubMed:18559503). Isoform 6 increases water and sodium absorption in the intestine and gall- bladder. {ECO:0000269|PubMed:12475393, ECO:0000269|PubMed:18559503, ECO:0000269|PubMed:9211900}.; . TISSUE SPECIFICITY: Abundantly expressed in heart. In cardiac muscle cells, located in the Z-disks of sarcomere. Also found, but to a lower extent, in small and large intestine, pancreas, thymus, colon, spleen, prostate, testis, brain, ovary and epithelial cells. In the pancreas, mainly expressed in acinar cells, duct cells and all cell types in islets (at protein level). Tends to be down-regulated in pancreatic adenocarcinomas ans metastases. {ECO:0000269|PubMed:11786189, ECO:0000269|PubMed:18559503, ECO:0000269|PubMed:9211900}.; myocardium;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;testis;brain;pineal gland;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;heart;adrenal gland;thyroid;prefrontal cortex;liver;adrenal cortex;atrioventricular node;fetal thyroid;skin; 0.40850 0.13668 -0.519955994 20.95423449 216.18397 3.17504 SORBS3 2.31106262231037e-06 0.998964253686748 0.00103343525062958 sorbin and SH3 domain containing 3 FUNCTION: Vinexin alpha isoform promotes up-regulation of actin stress fiber formation. Vinexin beta isoform plays a role in cell spreading and enhances the activation of JNK/SAPK in response to EGF stimulation by using its third SH3 domain.; . TISSUE SPECIFICITY: Both isoforms are expressed in different tissues like heart, placenta, brain, skeletal muscle and pancreas. Isoform beta is especially found in liver.; myocardium;medulla oblongata;smooth muscle;ovary;salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;cerebral cortex;oesophagus;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;spinal cord;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;trigeminal ganglion;skeletal muscle;cerebellum; 0.20951 0.16278 0.255325157 69.71573484 681.71676 5.21947 SORCS1 0.969565842045511 0.0304341579287124 2.57768636709161e-11 sortilin related VPS10 domain containing receptor 1 . . TISSUE SPECIFICITY: Detected in fetal and infant brain and in fetal retina.; unclassifiable (Anatomical System);prostate;lung;frontal lobe;visual apparatus;muscle;testis;kidney;spinal ganglion;brain;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.32421 0.13565 -1.144569759 6.363529134 350.30161 3.96787 SORCS2 0.00264628823985857 0.997328809725055 2.49020350867465e-05 sortilin related VPS10 domain containing receptor 2 . . TISSUE SPECIFICITY: Highly expressed in brain and kidney. Detected at low levels in heart, liver, small intestine, skeletal muscle and thymus.; unclassifiable (Anatomical System);heart;cartilage;skeletal muscle;skin;retina;uterus;prostate;whole body;lung;bone;visual apparatus;kidney;brain;bladder;mammary gland; dorsal root ganglion;superior cervical ganglion; 0.55107 0.09964 -0.40608828 25.86694975 1145.2386 6.45313 SORCS3 0.325134263508276 0.674865688967158 4.75245658226512e-08 sortilin related VPS10 domain containing receptor 3 . . TISSUE SPECIFICITY: Highly expressed in brain.; . . 0.81490 0.10825 -1.170241634 6.039160179 476.83961 4.51156 SORCS3-AS1 . . . SORCS3 antisense RNA 1 . . . . . . . . . . . SORD 0.00434794621162012 0.962638318600185 0.0330137351881946 sorbitol dehydrogenase FUNCTION: Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm. {ECO:0000250|UniProtKB:Q64442, ECO:0000269|PubMed:16278369}.; . TISSUE SPECIFICITY: Expressed in kidney and epithelial cells of both benign and malignant prostate tissue. Expressed in epididymis (at protein level). {ECO:0000269|PubMed:16278369, ECO:0000269|PubMed:19423711, ECO:0000269|PubMed:20372835}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;bladder;brain;gall bladder;heart;cartilage;tongue;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach; dorsal root ganglion;fetal liver;superior cervical ganglion;prostate;thyroid;liver;kidney;pons;fetal thyroid; 0.48997 0.60308 0.863528995 88.74144845 2436.461 9.17126 SORD2P . . . sorbitol dehydrogenase 2, pseudogene . . . . . . . . . . . SORL1 0.0174141233573499 0.982585876642613 3.73763554140496e-14 sortilin-related receptor, L(DLR class) A repeats containing FUNCTION: Likely to be a multifunctional endocytic receptor, that may be implicated in the uptake of lipoproteins and of proteases. Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. Binds the receptor- associated protein (RAP). Could play a role in cell-cell interaction. Involved in APP trafficking to and from the Golgi apparatus. It probably acts as a sorting receptor that protects APP from trafficking to late endosome and from processing into amyloid beta, thereby reducing the burden of amyloidogenic peptide formation. Involved in the regulation of smooth muscle cells migration, probably through PLAUR binding and decreased internalization. {ECO:0000269|PubMed:14764453, ECO:0000269|PubMed:16174740}.; DISEASE: Alzheimer disease (AD) [MIM:104300]: Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta- APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. {ECO:0000269|PubMed:21220680, ECO:0000269|PubMed:22472873, ECO:0000269|PubMed:23565137}. Note=The gene represented in this entry is involved in disease pathogenesis.; TISSUE SPECIFICITY: Expressed mainly in brain, where it is most abundant in the cerebellum, cerebral cortex and the occipital pole; low expression in the putamen and the thalamus. Expression is significantly reduced in the frontal cortex of patients suffering from Alzheimer disease. According to PubMed:9157966, found in spinal cord, testis, liver, kidney and pancreas with detectable levels in placenta, lung and heart. According to PubMed:8940146, expressed in the prostate, ovary, thyroid and spleen, but not found in kidney, liver, lung, skeletal muscle, bone marrow and adrenals. {ECO:0000269|PubMed:16174740}.; lymphoreticular;ovary;umbilical cord;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;blood;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;stomach; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;liver;globus pallidus;whole blood;cingulate cortex;parietal lobe;cerebellum; 0.80211 . -2.343483048 1.16183062 1587.28518 7.37199 SORT1 0.999926560036891 7.34399594133399e-05 3.69542062789763e-12 sortilin 1 FUNCTION: Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi. {ECO:0000269|PubMed:10085125, ECO:0000269|PubMed:11331584, ECO:0000269|PubMed:11390366, ECO:0000269|PubMed:12209882, ECO:0000269|PubMed:12598608, ECO:0000269|PubMed:14657016, ECO:0000269|PubMed:14985763, ECO:0000269|PubMed:15313463, ECO:0000269|PubMed:15930396, ECO:0000269|PubMed:15987945}.; DISEASE: Note=A common polymorphism located in a non-coding region between CELSR2 and PSRC1 alters a CEBP transcription factor binding site and is responsible for changes in hepatic expression of SORT1. Altered SORT1 expression in liver affects low density lipoprotein cholesterol levels in plasma and is associated with susceptibility to myocardial infarction.; TISSUE SPECIFICITY: Expressed in brain and prostate (at protein level). Expressed at high levels in brain, spinal cord, heart, skeletal muscle, thyroid, placenta and testis. Expressed at lower levels in lymphoid organs, kidney, colon and liver. {ECO:0000269|PubMed:20048080, ECO:0000269|PubMed:9013611}.; myocardium;medulla oblongata;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;breast;lung;placenta;visual apparatus;hypopharynx;head and neck;cervix;kidney;mammary gland; dorsal root ganglion;occipital lobe;superior cervical ganglion;testis;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.85867 0.28534 0.376678994 75.50719509 165.82847 2.81746 SOS1 0.99999989519361 1.04806389809942e-07 1.77231495230296e-20 SOS Ras/Rac guanine nucleotide exchange factor 1 FUNCTION: Promotes the exchange of Ras-bound GDP by GTP. Catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity (By similarity). {ECO:0000250}.; DISEASE: Noonan syndrome 4 (NS4) [MIM:610733]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. Some patients with NS4 have polyarticular villonodular synovitis. {ECO:0000269|PubMed:17143282, ECO:0000269|PubMed:17143285, ECO:0000269|PubMed:19020799, ECO:0000269|PubMed:19438935, ECO:0000269|PubMed:19953625, ECO:0000269|PubMed:20673819, ECO:0000269|PubMed:20683980, ECO:0000269|PubMed:21387466}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in gingival tissues. {ECO:0000269|PubMed:11868160}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;pons;atrioventricular node;skeletal muscle; 0.72054 0.38414 -0.995664936 8.539749941 106.78667 2.24216 SOS1-IT1 . . . SOS1 intronic transcript 1 . . . . . . . . . . . SOS2 0.999427840971243 0.000572159028570651 1.86285211016712e-13 SOS Ras/Rho guanine nucleotide exchange factor 2 FUNCTION: Promotes the exchange of Ras-bound GDP by GTP. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;ovary;heart;colon;parathyroid;blood;skin;skeletal muscle;bone marrow;breast;uterus;prostate;lung;frontal lobe;adrenal gland;thyroid;placenta;liver;testis;cervix;spleen;germinal center;kidney;brain;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;spinal cord;testis;ciliary ganglion;caudate nucleus;trigeminal ganglion;parietal lobe;skeletal muscle; 0.94123 0.11519 -0.927704399 9.719273414 277.52939 3.56927 SOST 0.379603154764271 0.575080949504812 0.0453158957309171 sclerostin FUNCTION: Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation. {ECO:0000269|PubMed:15908424}.; DISEASE: Van Buchem disease (VBCH) [MIM:239100]: VBCH is an autosomal recessive sclerosing bone dysplasia characterized by endosteal hyperostosis of the mandible, skull, ribs, clavicles, and diaphyses of the long bones. Affected patients present a symmetrically increased thickness of bones, most frequently found as an enlarged jawbone, but also an enlargement of the skull, ribs, diaphysis of long bones, as well as tubular bones of hands and feet. The clinical consequence of increased thickness of the skull include facial nerve palsy causing hearing loss, visual problems, neurological pain, and, very rarely, blindness as a consequence of optic atrophy. Serum alkaline phosphatase levels are elevated. {ECO:0000269|PubMed:11836356}. Note=The disease is caused by mutations affecting the gene represented in this entry. A 52 kb deletion downstream of SOST results in SOST transcription suppression causing van Buchem disease.; DISEASE: Craniodiaphyseal dysplasia autosomal dominant (CDD) [MIM:122860]: A severe bone dysplasia characterized by massive generalized hyperostosis and sclerosis, especially involving the skull and facial bones. The sclerosis is so severe that the resulting facial distortion is referred to as 'leontiasis ossea' (leonine faces) and the bone deposition results in progressive stenosis of craniofacial foramina. Respiratory obstruction due to choanal stenosis compromises the clinical outcomes of affected patients. {ECO:0000269|PubMed:21221996}. Note=The disease is caused by mutations affecting the gene represented in this entry. Heterozygous mutations located in the secretion signal of the SOST gene prevent sclerostin secretion and can be responsible for craniodiaphyseal dysplasia.; TISSUE SPECIFICITY: Widely expressed at low levels with highest levels in bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. Detected in the subendothelial layer of the aortic intima (at protein level). {ECO:0000269|PubMed:20551380}.; unclassifiable (Anatomical System);uterus;whole body;heart;bone;kidney;artery;skin;aorta; superior cervical ganglion;heart; 0.47748 0.40510 . . 10.77913 0.39078 SOSTDC1 0.303977581230425 0.620884380514952 0.0751380382546222 sclerostin domain containing 1 FUNCTION: May be involved in the onset of endometrial receptivity for implantation/sensitization for the decidual cell reaction Enhances Wnt signaling and inhibits TGF-beta signaling (By similarity). Directly antagonizes activity of BMP2, BMP4, BMP6 and BMP7 in a dose-dependent manner. {ECO:0000250, ECO:0000269|PubMed:15020244}.; . TISSUE SPECIFICITY: Highly expressed in kidney and weakly in lung. {ECO:0000269|PubMed:15020244}.; colon;skin;retina;uterus;prostate;whole body;optic nerve;cochlea;endometrium;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;lung;pia mater;nasopharynx;placenta;trabecular meshwork;hippocampus;liver;spleen;kidney;stomach;aorta; amygdala;occipital lobe;superior cervical ganglion;fetal lung;kidney; 0.20001 0.15768 0.014844891 54.94810097 46.74727 1.32148 SOWAHA . . . sosondowah ankyrin repeat domain family member A . . . . . 0.09486 . . . 1701.6621 7.60485 SOWAHB 0.00410236827486597 0.988158024681134 0.00773960704400048 sosondowah ankyrin repeat domain family member B . . . . . 0.16431 . -0.290161348 33.33923095 2830.29327 10.03971 SOWAHC . . . sosondowah ankyrin repeat domain family member C . . . . . 0.13558 . . . 325.28625 3.83430 SOWAHD 0.477013933457323 0.439279388297834 0.0837066782448434 sosondowah ankyrin repeat domain family member D . . . . . 0.29549 . . . 19.38951 0.66688 SOX1 . . . SRY-box 1 FUNCTION: Transcriptional activator. May function as a switch in neuronal development. Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Mainly expressed in the developing central nervous system.; unclassifiable (Anatomical System);lung;brain; superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.18496 . . . 2053.06761 8.35110 SOX2 0.396696528099993 0.562922260719737 0.0403812111802697 SRY-box 2 FUNCTION: Transcription factor that forms a trimeric complex with OCT4 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206 (By similarity). Critical for early embryogenesis and for embryonic stem cell pluripotency. May function as a switch in neuronal development. Downstream SRRT target that mediates the promotion of neural stem cell self-renewal (By similarity). Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:18035408}.; DISEASE: Microphthalmia, syndromic, 3 (MCOPS3) [MIM:206900]: A disease characterized by the rare association of malformations including uni- or bilateral anophthalmia or microphthalmia, and esophageal atresia with trachoesophageal fistula. Microphthalmia is a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. {ECO:0000269|PubMed:12612584}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;tongue;muscle;parathyroid;fovea centralis;choroid;lens;retina;pancreas;prostate;optic nerve;whole body;lung;frontal lobe;cochlea;placenta;macula lutea;visual apparatus;hippocampus;head and neck;kidney;brain;stomach;thymus; amygdala;medulla oblongata;superior cervical ganglion;occipital lobe;temporal lobe;caudate nucleus;pons;atrioventricular node;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.89720 0.58572 -0.119252484 44.53880632 9.21101 0.33622 SOX2-OT . . . SOX2 overlapping transcript . . . . . . . . . . . SOX3 . . . SRY-box 3 FUNCTION: Transcription factor required during the formation of the hypothalamo-pituitary axis. May function as a switch in neuronal development. Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation. Required also within the pharyngeal epithelia for craniofacial morphogenesis. Controls a genetic switch in male development. Is necessary for initiating male sex determination by directing the development of supporting cell precursors (pre-Sertoli cells) as Sertoli rather than granulosa cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:21183788}.; DISEASE: Panhypopituitarism X-linked (PHPX) [MIM:312000]: Affected individuals have absent infundibulum, anterior pituitary hypoplasia, and ectopic posterior pituitary. {ECO:0000269|PubMed:15800844}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mental retardation, X-linked, with isolated growth hormone deficiency (MRXGH) [MIM:300123]: A disorder characterized by the association of variable degrees of mental retardation with panhypopituitarism, variable combinations of hypothyroidism, delayed pubertal development, and short stature due to growth hormone deficiency. {ECO:0000269|PubMed:12428212}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: 46,XX sex reversal 3 (SRXX3) [MIM:300833]: A condition in which male gonads develop in a genetic female (female to male sex reversal). {ECO:0000269|PubMed:21183788}. Note=The disease is caused by mutations affecting the gene represented in this entry. Copy number variations (CNV) encompassing or in close proximity to SOX3 are responsible for XX male reversal. These variations include two duplications of approximately 123 kb and 85 kb, the former of which spans the entire SOX3 gene; a 343 kb deletion immediately upstream of SOX3 that is probably responsible of altered regulation (and not increased dosage) of SOX3; a large (approximately 6 Mb) duplication that encompasses SOX3 and at least 18 additional distally located genes. Its proximal breakpoint falls within the SOX3 regulatory region. This large rearrangement has been found in a patient with XX male reversal and a complex phenotype that also includes a scrotal hypoplasia, microcephaly, developmental delay, and growth retardation.; . . . 0.98320 0.39904 . . 139.07787 2.56977 SOX4 0.384005969080463 0.572001426754163 0.0439926041653743 SRY-box 4 FUNCTION: Transcriptional activator that binds with high affinity to the T-cell enhancer motif 5'-AACAAAG-3' motif.; . TISSUE SPECIFICITY: Testis, brain, and heart.; smooth muscle;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;alveolus;liver;kidney;mammary gland;stomach;aorta;peripheral nerve;thymus; prostate;uterus corpus;fetal brain;atrioventricular node;thymus; 0.96100 0.25991 . . 95.1054 2.10373 SOX5 0.999398884487612 0.000601115387057276 1.2533086052509e-10 SRY-box 5 FUNCTION: Binds specifically to the DNA sequence 5'-AACAAT-3'. Activates transcription of COL2A1 and AGC1 in vitro.; . . unclassifiable (Anatomical System);lung;cartilage;endometrium;testis;kidney;germinal center;brain;skin;retina; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;pons;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.63083 0.17821 -0.957024976 9.088228356 16.39611 0.58125 SOX5P1 . . . SRY-box 5 pseudogene 1 . . . . . . . . . . . SOX6 0.999530959870119 0.00046904006140811 6.8473126093827e-11 SRY-box 6 FUNCTION: Transcriptional activator. Binds specifically to the DNA sequence 5'-AACAAT-3'. Plays a key role in several developmental processes, including neurogenesis and skeleton formation.; . TISSUE SPECIFICITY: Expressed in a wide variety of tissues, most abundantly in skeletal muscle. {ECO:0000269|PubMed:11255018}.; unclassifiable (Anatomical System);whole body;liver;testis;spleen;blood;kidney;brain; superior cervical ganglion;testis - interstitial;subthalamic nucleus;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.55943 0.18762 -1.111360919 6.717386176 34.06577 1.04481 SOX7 0.131241610927833 0.780185411099135 0.0885729779730329 SRY-box 7 FUNCTION: Binds to and activates the CDH5 promoter, hence plays a role in the transcriptional regulation of genes expressed in the hemogenic endothelium and blocks further differentiation into blood precursors (By similarity). May be required for the survival of both hematopoietic and endothelial precursors during specification (By similarity). Competes with GATA4 for binding and activation of the FGF3 promoter (By similarity). Represses Wnt/beta-catenin-stimulated transcription, probably by targeting CTNNB1 to proteasomal degradation. Binds the DNA sequence 5'- AACAAT-3'. {ECO:0000250, ECO:0000269|PubMed:18819930}.; . TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues. Present both in mesenchymal and epithelial cells in some adult tissues, including colon. Tends to be down-regulated in prostate adenocarcinomas and colorectal tumors due to promoter hypermethylation. {ECO:0000269|PubMed:11691915, ECO:0000269|PubMed:18819930}.; heart;ovary;parathyroid;vein;skin;uterus;pancreas;lung;cochlea;placenta;visual apparatus;testis;head and neck;spleen;brain;bladder;stomach; ciliary ganglion;atrioventricular node; 0.37762 0.13775 -0.424258538 25.56027365 226.17832 3.24948 SOX8 0.873708460070314 0.124658747646576 0.00163279228310963 SRY-box 8 FUNCTION: May play a role in central nervous system, limb and facial development. May be involved in male sex determination. Binds the consensus motif 5'-[AT][AT]CAA[AT]G-3' (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;colon;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;cerebral cortex;macula lutea;hippocampus;testis;brain;cerebellum; . 0.14736 . . . 35.61411 1.07230 SOX9 0.983539902653989 0.0164501740943262 9.92325168523514e-06 SRY-box 9 FUNCTION: Plays an important role in the normal skeletal development. May regulate the expression of other genes involved in chondrogenesis by acting as a transcription factor for these genes.; DISEASE: Campomelic dysplasia (CMD1) [MIM:114290]: A rare, often lethal, osteochondrodysplasia characterized by congenital bowing and angulation of long bones. Other skeletal defects include unusually small scapula, deformed pelvis and spine, and a missing pair of ribs. Craniofacial and ear defects are common. Most patients die soon after birth due to respiratory distress which has been attributed to hypoplasia of the tracheobronchial cartilage and small thoracic cage. Up to two-thirds of affected XY individuals have genital defects or may develop as phenotypic females. {ECO:0000269|PubMed:10446171, ECO:0000269|PubMed:10951468, ECO:0000269|PubMed:11323423, ECO:0000269|PubMed:11754051, ECO:0000269|PubMed:12783851, ECO:0000269|PubMed:19921652, ECO:0000269|PubMed:20513132, ECO:0000269|PubMed:7485151, ECO:0000269|PubMed:9002675, ECO:0000269|PubMed:9452059}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: 46,XX sex reversal 2 (SRXX2) [MIM:278850]: A condition in which male gonads develop in a genetic female (female to male sex reversal). {ECO:0000269|PubMed:21208124}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: 46,XY sex reversal 10 (SRXY10) [MIM:616425]: A disorder of sex development. Affected individuals have a 46,XY karyotype, show gonadal dysgenesis with streak gonads, look like normal females at birth, do not develop secondary sexual characteristics at puberty and do not menstruate. {ECO:0000269|PubMed:25604083}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;rectum;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;atrium;whole body;cochlea;endometrium;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;breast;lung;internal ear;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;testis; 0.85252 0.83576 -0.714505427 14.4019816 22.37992 0.75079 SOX9-AS1 . . . SOX9 antisense RNA 1 . . . . . . . . . . . SOX10 0.91309785132116 0.0862768056285623 0.000625343050278015 SRY-box 10 FUNCTION: Transcription factor that seems to function synergistically with the POU domain protein TST-1/OCT6/SCIP. Could confer cell specificity to the function of other transcription factors in developing and mature glia (By similarity). {ECO:0000250}.; DISEASE: Waardenburg syndrome 4C (WS4C) [MIM:613266]: A disorder characterized by the association of Waardenburg features (depigmentation and deafness) with the absence of enteric ganglia in the distal part of the intestine (Hirschsprung disease). {ECO:0000269|PubMed:18348274, ECO:0000269|PubMed:21898658, ECO:0000269|PubMed:9462749}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Peripheral demyelinating neuropathy, central dysmyelinating leukodystrophy, Waardenburg syndrome and Hirschsprung disease (PCWH) [MIM:609136]: A complex neurocristopathy that includes features of 4 distinct syndromes: peripheral demyelinating neuropathy, central dysmyelinating leukodystrophy, Waardenburg syndrome and Hirschsprung disease. {ECO:0000269|PubMed:10762540, ECO:0000269|PubMed:15004559, ECO:0000269|PubMed:19208381, ECO:0000269|PubMed:21898658}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in fetal brain and in adult brain, heart, small intestine and colon.; sympathetic chain;choroid;fovea centralis;skin;retina;uterus;optic nerve;frontal lobe;cochlea;brain;spinal ganglion;unclassifiable (Anatomical System);amygdala;heart;lacrimal gland;adrenal cortex;lens;breast;lung;adrenal gland;placenta;visual apparatus;macula lutea;mammary gland;cerebellum; amygdala;dorsal root ganglion;whole brain;superior cervical ganglion;medulla oblongata;thalamus;occipital lobe;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;pons;atrioventricular node;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.98629 0.45051 -0.471992905 23.03609342 24.56042 0.80765 SOX11 0.343767037415361 0.598619702825468 0.0576132597591704 SRY-box 11 FUNCTION: Transcriptional factor involved in the embryonic neurogenesis. May also have a role in tissue modeling during development. {ECO:0000269|PubMed:24886874}.; . TISSUE SPECIFICITY: Expressed mainly in the nervous system, brain (fetus and adult) and hear (adult). {ECO:0000269|PubMed:24886874, ECO:0000269|PubMed:8666406}.; ovary;parathyroid;choroid;fovea centralis;skin;retina;uterus;optic nerve;whole body;frontal lobe;larynx;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;lung;placenta;visual apparatus;macula lutea;spleen;head and neck;kidney;aorta; dorsal root ganglion;superior cervical ganglion;fetal brain;caudate nucleus;trigeminal ganglion; 0.41352 0.15395 . . 8.44037 0.30871 SOX12 . . . SRY-box 12 FUNCTION: Binds to the sequence 5'-AACAAT-3'. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed most abundantly in the CNS. Also expressed in fetal brain and kidney and adult heart, pancreas, testis and ovary. Other tissues were only weakly positive. {ECO:0000269|PubMed:9215677}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;spinal ganglion;brain;unclassifiable (Anatomical System);heart;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum;thymus; superior cervical ganglion;pons; 0.28694 . . . 119.21572 2.37593 SOX13 0.964099530137052 0.0358976723147222 2.79754822580766e-06 SRY-box 13 FUNCTION: Binds to the sequence 5'-AACAAT-3'. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in kidney, lung, and liver and low expression in thymus, brain, spleen, and muscle.; unclassifiable (Anatomical System);blood;fovea centralis;choroid;lens;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;epididymis;macula lutea;liver;testis;kidney;brain; pons; 0.25779 0.14652 0.753291803 86.71266808 157.95662 2.74542 SOX14 0.720669571974876 0.265725610495204 0.0136048175299204 SRY-box 14 FUNCTION: Acts as a negative regulator of transcription. {ECO:0000250}.; . . placenta; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.51148 0.12971 -0.075159878 47.78839349 6.59795 0.24411 SOX15 0.361605911080546 0.58726025357869 0.051133835340764 SRY-box 15 FUNCTION: Binds to the 5'-AACAAT-3' sequence.; . TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues examined, highest level found in fetal spinal cord and adult brain and testis. {ECO:0000269|PubMed:8978787, ECO:0000269|PubMed:9880678}.; ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pineal body;urinary;blood;pancreas;lung;placenta;visual apparatus;liver;head and neck;cervix;kidney;stomach;aorta; superior cervical ganglion;lung;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex;skeletal muscle;cerebellum; 0.15500 . . . 25.00059 0.81970 SOX17 0.866918773398146 0.131210614752515 0.00187061184933919 SRY-box 17 FUNCTION: Acts as transcription regulator that binds target promoter DNA and bends the DNA. Binds to the sequences 5'- AACAAT-'3 or 5'-AACAAAG-3'. Modulates transcriptional regulation via WNT3A. Inhibits Wnt signaling. Promotes degradation of activated CTNNB1. Plays a key role in the regulation of embryonic development. Required for normal looping of the embryonic heart tube. Required for normal development of the definitive gut endoderm. Probable transcriptional activator in the premeiotic germ cells (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in adult heart, lung, spleen, testis, ovary, placenta, fetal lung, and kidney. In normal gastrointestinal tract, it is preferentially expressed in esophagus, stomach and small intestine than in colon and rectum. {ECO:0000269|PubMed:11786926}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;uterus;prostate;lung;endometrium;placenta;liver;testis;kidney;aorta;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.10157 0.22628 . . 107.58815 2.25185 SOX18 . . . SRY-box 18 FUNCTION: Binds to the consensus sequence 5'-AACAAAG-3' and is able to trans-activate transcription via this site. {ECO:0000250}.; DISEASE: Hypotrichosis-lymphedema-telangiectasia syndrome (HLTS) [MIM:607823]: A syndrome characterized by absent eyebrows and eyelashes, lymphatic edemas of the inferior members or eyelids, and peripheral vein anomalies. {ECO:0000269|PubMed:12740761}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hypotrichosis-lymphedema-telangiectasia-renal defect syndrome (HLTRS) [MIM:137940]: A syndrome characterized by sparse hair, lymphatic edemas, peripheral vein anomalies, and renal disease. {ECO:0000269|PubMed:12740761, ECO:0000269|PubMed:24697860}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . cartilage;ovary;islets of Langerhans;colon;uterus;pancreas;prostate;lung;cerebral cortex;endometrium;placenta;testis;spleen;kidney;spinal ganglion;brain;pineal gland;stomach; . 0.20632 0.14672 . . 26.68267 0.86337 SOX21 . . . SRY-box 21 FUNCTION: May play a role as an activator of transcription of OPRM1. {ECO:0000250}.; . . . . 0.68943 . . . 8.7755 0.32376 SOX21-AS1 . . . SOX21 antisense RNA 1 (head to head) . . . . . . . . . . . SOX30 0.998986334267771 0.00101365479516027 1.09370689318069e-08 SRY-box 30 FUNCTION: Transcriptional activator. Binds to the DNA sequence 5'- ACAAT-3' and shows a preference for guanine residues surrounding this core motif. {ECO:0000269|PubMed:10359848}.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:10359848}.; unclassifiable (Anatomical System);medulla oblongata;lung;placenta;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;parietal lobe; 0.27011 0.09592 1.289723716 93.85468271 1024.43935 6.15363 SOX30P1 . . . SRY-box 30 pseudogene 1 . . . . . . . . . . . SP1 0.997637149483068 0.0023627644205883 8.60963440409205e-08 Sp1 transcription factor FUNCTION: Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR- alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. Isoform 3 is a stronger activator of transcription than isoform 1. Positively regulates the transcription of the core clock component ARNTL/BMAL1. {ECO:0000269|PubMed:10391891, ECO:0000269|PubMed:11371615, ECO:0000269|PubMed:11904305, ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:16377629, ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:16943418, ECO:0000269|PubMed:17049555, ECO:0000269|PubMed:18171990, ECO:0000269|PubMed:18199680, ECO:0000269|PubMed:18239466, ECO:0000269|PubMed:18513490, ECO:0000269|PubMed:18619531, ECO:0000269|PubMed:19193796, ECO:0000269|PubMed:20091743, ECO:0000269|PubMed:21798247}.; . TISSUE SPECIFICITY: Up-regulated in adenocarcinomas of the stomach (at protein level). Isoform 3 is ubiquitously expressed at low levels. {ECO:0000269|PubMed:21798247}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; appendix;atrioventricular node;skeletal muscle; 0.99998 0.76734 -0.933156985 9.54824251 50.01247 1.38791 SP2 0.969394324989432 0.0305963803476409 9.29466292739798e-06 Sp2 transcription factor FUNCTION: Binds to GC box promoters elements and selectively activates mRNA synthesis from genes that contain functional recognition sites.; . . unclassifiable (Anatomical System);lung;placenta;testis;retina;cerebellum;bone marrow; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.95141 0.28739 -0.843147538 11.2762444 1036.59282 6.18304 SP2-AS1 . . . SP2 antisense RNA 1 . . . . . . . . . . . SP3 0.992297744064531 0.00770194372975783 3.12205711103716e-07 Sp3 transcription factor FUNCTION: Transcriptional factor that can act as an activator or repressor depending on isoform and/or post-translational modifications. Binds to GT and GC boxes promoter elements. Competes with SP1 for the GC-box promoters. Weak activator of transcription but can activate a number of genes involved in different processes such as cell-cycle regulation, hormone- induction and house-keeping. {ECO:0000269|PubMed:10391891, ECO:0000269|PubMed:11812829, ECO:0000269|PubMed:12419227, ECO:0000269|PubMed:12837748, ECO:0000269|PubMed:15247228, ECO:0000269|PubMed:15494207, ECO:0000269|PubMed:15554904, ECO:0000269|PubMed:16781829, ECO:0000269|PubMed:17548428, ECO:0000269|PubMed:18187045, ECO:0000269|PubMed:18617891, ECO:0000269|PubMed:9278495}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;cochlea;larynx;thyroid;pituitary gland;testis;amniotic fluid;dura mater;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);meninges;lymph node;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;bile duct;pia mater;lung;placenta;visual apparatus;duodenum;liver;cervix;head and neck;kidney;mammary gland;aorta;stomach; testis - interstitial;ciliary ganglion;atrioventricular node;whole blood;trigeminal ganglion; 0.96279 0.19114 -0.067881249 48.69072895 885.01092 5.79517 SP3P . . . Sp3 transcription factor pseudogene . . . . . . . . . . . SP4 0.95128804346323 0.0487059599328447 5.99660392539219e-06 Sp4 transcription factor FUNCTION: Binds to GT and GC boxes promoters elements. Probable transcriptional activator.; . TISSUE SPECIFICITY: Abundant in brain.; unclassifiable (Anatomical System);lung;thyroid;urinary;testis;head and neck;germinal center;skeletal muscle;stomach;retina; dorsal root ganglion;superior cervical ganglion;appendix;atrioventricular node;trigeminal ganglion; 0.90308 0.23101 -0.844966979 11.1759849 141.72587 2.59835 SP5 0.432721441198873 0.535690529490582 0.0315880293105446 Sp5 transcription factor FUNCTION: Binds to GC boxes promoters elements. Probable transcriptional activator that has a role in the coordination of changes in transcription required to generate pattern in the developing embryo (By similarity). {ECO:0000250}.; . . . . 0.59161 0.11646 . . 4123.32513 12.75127 SP6 0.0229475656346052 0.766873174223703 0.210179260141692 Sp6 transcription factor FUNCTION: Promotes cell proliferation. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;skin;uterus;breast;prostate;whole body;lung;placenta;mammary gland;peripheral nerve; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;caudate nucleus;atrioventricular node;trigeminal ganglion;parietal lobe; 0.72607 0.11016 . . 22.22008 0.74525 SP7 0.663143306771365 0.331538745190326 0.00531794803830874 Sp7 transcription factor FUNCTION: Transcriptional activator essential for osteoblast differentiation. Binds to SP1 and EKLF consensus sequences and to other G/C-rich sequences (By similarity). {ECO:0000250, ECO:0000269|PubMed:23457570}.; DISEASE: Osteogenesis imperfecta 12 (OI12) [MIM:613849]: A form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI12 is an autosomal recessive form characterized by recurrent fractures, mild bone deformations, generalized osteoporosis, delayed teeth eruption, no dentinogenesis imperfecta, normal hearing, and white sclerae. {ECO:0000269|PubMed:20579626}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Restricted to bone-derived cell. {ECO:0000269|PubMed:15474293}.; unclassifiable (Anatomical System);optic nerve; superior cervical ganglion;atrioventricular node; 0.31967 0.30954 -0.80269335 12.23755603 36.52093 1.09481 SP8 . . . Sp8 transcription factor FUNCTION: Transcription factor which plays a key role in limb development. Positively regulates FGF8 expression in the apical ectodermal ridge (AER) and contributes to limb outgrowth in embryos (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);prostate;developmental;brain; pancreas;ciliary ganglion; 0.92059 0.15484 . . 645.38028 5.10216 SP9 0.498147938263282 0.428018311518869 0.073833750217849 Sp9 transcription factor FUNCTION: Transcription factor which plays a key role in limb development. Positively regulates FGF8 expression in the apical ectodermal ridge (AER) and contributes to limb outgrowth in embryos (By similarity). {ECO:0000250}.; . . . . . . . . 26.65009 0.86255 SP100 8.71376355676682e-07 0.999964307615292 3.48210083517976e-05 SP100 nuclear antigen FUNCTION: Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2 according to PubMed:11909962. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA according to PubMed:15247905. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53- mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. Also plays a role in infection by viruses, including human cytomegalovirus and Epstein-Barr virus, through mechanisms that may involve chromatin and/or transcriptional regulation. {ECO:0000269|PubMed:11909962, ECO:0000269|PubMed:14647468, ECO:0000269|PubMed:15247905, ECO:0000269|PubMed:15592518, ECO:0000269|PubMed:15767676, ECO:0000269|PubMed:16177824, ECO:0000269|PubMed:17245429, ECO:0000269|PubMed:21274506, ECO:0000269|PubMed:21880768}.; . TISSUE SPECIFICITY: Widely expressed. Sp100-B is expressed only in spleen, tonsil, thymus, mature B-cell line and some T-cell line, but not in brain, liver, muscle or non-lymphoid cell lines.; smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;bile duct;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;smooth muscle;lymph node;appendix;ciliary ganglion;white blood cells;atrioventricular node;whole blood;skeletal muscle;tonsil; 0.76267 . 0.229636184 68.56569946 106.53399 2.24030 SP110 3.16369314039825e-09 0.978688179301511 0.0213118175347957 SP110 nuclear body protein FUNCTION: Transcription factor. May be a nuclear hormone receptor coactivator. Enhances transcription of genes with retinoic acid response elements (RARE).; DISEASE: Hepatic venoocclusive disease with immunodeficiency (VODI) [MIM:235550]: Autosomal recessive primary immunodeficiency associated with hepatic vascular occlusion and fibrosis. The immunodeficiency is characterized by severe hypogammaglobulinemia, combined T and B-cell immunodeficiency, absent lymph node germinal centers, and absent tissue plasma cells. {ECO:0000269|PubMed:16648851}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in peripheral blood leukocytes and spleen. Detected at intermediate levels in thymus, prostate, testis, ovary, small intestine and colon, and at low levels in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;whole body;bone;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;white blood cells;trigeminal ganglion;whole blood;tonsil;skeletal muscle; 0.03942 . 0.540106923 81.09813635 1459.74314 7.12571 SP140 1.99687363350876e-08 0.998412016087812 0.00158796394345159 SP140 nuclear body protein FUNCTION: Component of the nuclear body, also known as nuclear domain 10, PML oncogenic domain, and KR body (PubMed:8910577). May be involved in the pathogenesis of acute promyelocytic leukemia and viral infection (PubMed:8910577). May play a role in chromatin-mediated regulation of gene expression although it does not bind to histone H3 tails (PubMed:24267382). {ECO:0000269|PubMed:24267382, ECO:0000269|PubMed:8910577, ECO:0000303|PubMed:8910577}.; . TISSUE SPECIFICITY: High levels in spleen and peripheral blood leukocytes, much lower levels in tonsils, thymus, prostate, ovary, small intestine, and colon (PubMed:8695863, PubMed:8910577.) Very low levels in heart, brain, placenta, lung, liver, skeletal muscle, kidney, and pancreas (PubMed:8910577). Not detected in brain, liver and muscle (PubMed:8695863). {ECO:0000269|PubMed:8695863, ECO:0000269|PubMed:8910577}.; unclassifiable (Anatomical System);lymph node;ovary;salivary gland;intestine;pharynx;colon;blood;skin;bone marrow;breast;prostate;lung;nasopharynx;visual apparatus;liver;testis;spleen;germinal center;kidney;mammary gland;brain;bladder;tonsil; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.02782 0.06218 0.316000233 72.80018872 737.24204 5.38969 SP140L 6.06952429760381e-05 0.994353439525744 0.00558586523127967 SP140 nuclear body protein like . . . unclassifiable (Anatomical System);breast;prostate;lung;cartilage;testis;colon;amniotic fluid;blood;brain;bone marrow; dorsal root ganglion;ciliary ganglion;atrioventricular node; . . 1.444070618 95.09318235 1226.98768 6.62017 SPA17 0.00626347389447245 0.741190416406798 0.252546109698729 sperm autoantigenic protein 17 FUNCTION: Sperm surface zona pellucida binding protein. Helps to bind spermatozoa to the zona pellucida with high affinity. Might function in binding zona pellucida and carbohydrates (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis and sperm specific.; unclassifiable (Anatomical System);medulla oblongata;lymph node;ovary;hypothalamus;adrenal cortex;parathyroid;fovea centralis;breast;uterus;prostate;lung;endometrium;placenta;macula lutea;liver;testis;spleen;kidney;brain;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.03674 0.05144 0.080983847 59.76055674 31.09776 0.98256 SPA17P1 . . . sperm autoantigenic protein 17 pseudogene 1 . . . . . . . . . . . SPACA1 0.382221740156508 0.607405245766377 0.0103730140771148 sperm acrosome associated 1 FUNCTION: May be involved in sperm-egg fusion.; . TISSUE SPECIFICITY: Testis specific. At the equatorial segment and the inner acrosomal membrane of capacitated sperm. {ECO:0000269|PubMed:11870081}.; unclassifiable (Anatomical System);medulla oblongata;testis; superior cervical ganglion;testis - interstitial;medulla oblongata;appendix;testis;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.10740 0.10281 -0.293801652 32.93819297 36.84349 1.10367 SPACA3 0.0539629122350744 0.863765922890039 0.0822711648748867 sperm acrosome associated 3 FUNCTION: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. It could be a potential receptor for the egg oligosaccharide residue N-acetylglucosamine, which is present in the extracellular matrix over the egg plasma membrane. The processed form has no detectable bacteriolytic activity in vitro. {ECO:0000269|PubMed:12606493}.; . TISSUE SPECIFICITY: The processed form is expressed in sperm (at protein level). Expressed in testis, epididymis and placenta. {ECO:0000269|PubMed:12606493, ECO:0000269|PubMed:16014814}.; unclassifiable (Anatomical System);testis; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.05621 0.07284 0.92967242 89.79122435 178.47041 2.90413 SPACA4 0.577152663282386 0.378537580162718 0.0443097565548962 sperm acrosome associated 4 FUNCTION: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization.; . TISSUE SPECIFICITY: Testis specific. Expressed in spermatozoa. {ECO:0000269|PubMed:12788941}.; unclassifiable (Anatomical System);medulla oblongata;lung;hippocampus;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.10479 0.10726 0.237127192 68.98443029 6.17998 0.23332 SPACA5 . . . sperm acrosome associated 5 . . . . . 0.21235 0.10325 . . . . SPACA5B . . . sperm acrosome associated 5B . . . . . . 0.10325 . . . . SPACA6 . . . sperm acrosome associated 6 FUNCTION: Sperm protein potentially involved sperm-egg fusion. {ECO:0000250|UniProtKB:E9Q8Q8}.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:24275887}.; . . . . . . . . SPACA6P-AS . . . SPACA6P antisense RNA . . . . . . . . . . . SPACA7 2.1004322887891e-06 0.272223140688717 0.727774758878995 sperm acrosome associated 7 FUNCTION: Involved in fertilization. Seems not to play a direct role in sperm-egg binding or gamete fusion. {ECO:0000250|UniProtKB:Q9D2S4}.; . TISSUE SPECIFICITY: Expressed in spermatozoa (at protein level) (PubMed:22495889). {ECO:0000269|PubMed:22495889}.; unclassifiable (Anatomical System);lung;placenta;testis; . 0.10801 . 0.040529541 57.15380986 31.71768 0.99901 SPAG1 2.32516545713077e-07 0.973741531906141 0.0262582355773134 sperm associated antigen 1 FUNCTION: May play a role in the cytoplasmic assembly of the ciliary dynein arms (By similarity). May play a role in fertilization. Binds GTP and has GTPase activity. {ECO:0000250, ECO:0000269|PubMed:11517287, ECO:0000269|PubMed:1299558}.; . TISSUE SPECIFICITY: Present in most tissues, including lung, with the strongest expression in brain, colon, kidney, and testis. In sperm and testis, detected in particular in pachytene primary spermatocytes. Up-regulated in pancreatic tumor tissues and not in normal pancreatic tissue. {ECO:0000269|PubMed:11517287, ECO:0000269|PubMed:1299558, ECO:0000269|PubMed:16983343, ECO:0000269|PubMed:24055112}.; unclassifiable (Anatomical System);ovary;colon;parathyroid;blood;skeletal muscle;bone marrow;bile duct;uterus;pancreas;lung;bone;placenta;hippocampus;testis;germinal center;kidney;brain; superior cervical ganglion;trigeminal ganglion; 0.05940 0.16845 0.802845857 87.69167256 1456.53407 7.11884 SPAG4 0.110567923366472 0.8881451166144 0.00128696001912813 sperm associated antigen 4 FUNCTION: May assist the organization and assembly of outer dense fibers (ODFs), a specific structure of the sperm tail.; . . . . 0.14706 0.11092 0.551232944 81.48148148 141.82474 2.59876 SPAG5 7.25668525399221e-06 0.999984538963105 8.20435164069967e-06 sperm associated antigen 5 FUNCTION: Essential component of the mitotic spindle required for normal chromosome segregation and progression into anaphase (PubMed:11724960, PubMed:12356910). Required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture (PubMed:17664331). In complex with SKAP, promotes stable microtubule-kinetochore attachments. May contribute to the regulation of separase activity. May regulate AURKA localization to mitotic spindle, but not to centrosomes and CCNB1 localization to both mitotic spindle and centrosomes (PubMed:18361916, PubMed:21402792). Involved in centriole duplication. Required for CDK5RAP2, CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:26297806). In non-mitotic cells, upon stress induction, inhibits mammalian target of rapamycin complex 1 (mTORC1) association and recruits the mTORC1 component RPTOR to stress granules (SGs), thereby preventing mTORC1 hyperactivation- induced apoptosis (PubMed:23953116). May enhance GSK3B-mediated phosphorylation of other substrates, such as MAPT/TAU (PubMed:18055457). {ECO:0000269|PubMed:12356910, ECO:0000269|PubMed:17664331, ECO:0000269|PubMed:18055457, ECO:0000269|PubMed:18361916, ECO:0000269|PubMed:21402792, ECO:0000269|PubMed:23953116, ECO:0000269|PubMed:26297806, ECO:0000305|PubMed:11724960}.; . TISSUE SPECIFICITY: Highly expressed in testis. Detected at low levels in placenta, liver, pancreas, thymus and colon. {ECO:0000269|PubMed:11549262}.; lymphoreticular;ovary;salivary gland;colon;vein;skin;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;muscle;urinary;adrenal cortex;bile duct;breast;pancreas;lung;visual apparatus;liver;amnion;spleen;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;tumor; 0.33515 0.13487 -0.389485787 27.07596131 276.44454 3.55918 SPAG5-AS1 . . . SPAG5 antisense RNA 1 . . . . . . . . . . . SPAG6 7.41292381390175e-06 0.908274736167716 0.0917178509084702 sperm associated antigen 6 FUNCTION: Important for structural integrity of the central apparatus in the sperm tail and for flagellar motility. {ECO:0000250, ECO:0000269|PubMed:10493827}.; . TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:10493827}.; unclassifiable (Anatomical System);medulla oblongata;ovary;islets of Langerhans;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;lung;placenta;macula lutea;testis;germinal center;brain; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13125 0.10723 -0.0274281 51.65723048 1138.95929 6.43648 SPAG7 0.00114719730878394 0.83890212646187 0.159950676229346 sperm associated antigen 7 . . TISSUE SPECIFICITY: Detected in fetal brain. {ECO:0000269|PubMed:7624517}.; colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;kidney;mammary gland;stomach;thymus; whole brain;superior cervical ganglion;globus pallidus;pons;caudate nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex; 0.27397 0.13981 0.237127192 68.98443029 253.98981 3.42765 SPAG8 2.74927867712799e-07 0.740885869168021 0.259113855904111 sperm associated antigen 8 FUNCTION: May play a role in fertility and microtubule formation through interaction with RANBP9. {ECO:0000269|PubMed:10500252}.; . TISSUE SPECIFICITY: Expressed in testis (germ cells), but not in liver, kidney, prostate and small intestine. {ECO:0000269|PubMed:8788182}.; unclassifiable (Anatomical System);medulla oblongata;ovary;colon;retina;uterus;pancreas;lung;endometrium;hippocampus;liver;testis;spleen;brain; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.11804 0.10540 0.867166666 88.81811748 3548.41665 11.49875 SPAG9 0.999998937733062 1.06226693801481e-06 4.99585696346325e-18 sperm associated antigen 9 FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Isoform 5 may play a role in spermatozoa-egg- interaction. {ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:15693750}.; . TISSUE SPECIFICITY: Isoform 5 is expressed only in testis on the round spermatids of stage I, II and II. Isoform 5 is absent in spermatogonia and spermatocyte. Isoform 3 is expressed in testis. Isoform 4 is expressed in testis and in acute myeloid leukemia (AML) patients. {ECO:0000269|PubMed:14662895, ECO:0000269|PubMed:16112646, ECO:0000269|PubMed:9480848}.; ovary;salivary gland;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;whole body;optic nerve;endometrium;bone;pituitary gland;testis;germinal center;spinal ganglion;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;medulla oblongata;occipital lobe;hypothalamus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.25924 0.19965 -1.126142808 6.564048125 64.84794 1.65388 SPAG11A 0.0390121663586044 0.644058991201839 0.316928842439556 sperm associated antigen 11A . . . lung;epididymis;testis;retina; . . . . . . . SPAG11B 0.0472376897206403 0.678944314970504 0.273817995308856 sperm associated antigen 11B . . TISSUE SPECIFICITY: Specifically expressed in caput and proximal corpus of epididymis. Present in the epididymal epithelium and on the sperm surface, with a subacrosomal equatorial distribution on the sperm head.; lung;epididymis;testis;retina; superior cervical ganglion;trigeminal ganglion; . . . . 11.69299 0.42395 SPAG16 3.65639735304229e-20 0.00119763040731046 0.99880236959269 sperm associated antigen 16 FUNCTION: Necessary for sperm flagellar function. Plays a role in motile ciliogenesis. May help to recruit STK36 to the cilium or apical surface of the cell to initiate subsequent steps of construction of the central pair apparatus of motile cilia (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is detected in testis. Isoform 4 is detected in testis and brain, and at lower levels in kidney, heart, pancreas, thyroid, ovary, adrenal gland, spinal cord, trachea and liver. {ECO:0000269|PubMed:11867345, ECO:0000269|PubMed:12391165}.; unclassifiable (Anatomical System);medulla oblongata;cartilage;islets of Langerhans;hypothalamus;colon;uterus;pancreas;whole body;lung;nasopharynx;bone;testis;cervix;germinal center;kidney;brain;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07907 0.10925 0.178263593 66.12998349 2666.31265 9.71178 SPAG17 9.34771220873125e-16 0.999999294554198 7.05445800776993e-07 sperm associated antigen 17 FUNCTION: Component of the central pair apparatus of ciliary axonemes. Plays a critical role in the function and structure of motile cilia. May play a role in endochondral bone formation, most likely because of a function in primary cilia of chondrocytes and osteoblasts. {ECO:0000250|UniProtKB:Q5S003}.; . TISSUE SPECIFICITY: Highly expressed in testis. Expressed in organs that contain cilia-bearing cells including brain, oviduct, lung, and uterus. {ECO:0000269|PubMed:15827353}.; unclassifiable (Anatomical System);breast;lung;endometrium;placenta;liver;testis;spleen; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.12675 . 0.604307227 82.8792168 6237.18876 16.52835 SPAM1 1.24369500877438e-06 0.364344716631834 0.635654039673157 sperm adhesion molecule 1 (PH-20 hyaluronidase, zona pellucida binding) FUNCTION: Involved in sperm-egg adhesion. Upon fertilization sperm must first penetrate a layer of cumulus cells that surrounds the egg before reaching the zona pellucida. The cumulus cells are embedded in a matrix containing hyaluronic acid which is formed prior to ovulation. This protein aids in penetrating the layer of cumulus cells by digesting hyaluronic acid. {ECO:0000269|PubMed:8282124}.; . TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:8234258}.; unclassifiable (Anatomical System);uterus;medulla oblongata;lung;heart;testis;skin; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.08537 0.12225 0.420771676 77.15852795 69.68812 1.73159 SPANXA1 . . . sperm protein associated with the nucleus, X-linked, family member A1 . . TISSUE SPECIFICITY: Detected in testis and sperm. {ECO:0000269|PubMed:10906052, ECO:0000269|PubMed:12758128}.; . . 0.52767 . . . . . SPANXA2 . . . SPANX family member A2 . . TISSUE SPECIFICITY: Detected in testis and sperm. {ECO:0000269|PubMed:10906052, ECO:0000269|PubMed:12758128}.; . . 0.11217 . . . . . SPANXA2-OT1 . . . SPANXA2 overlapping transcript 1 . . . . . . . . . . . SPANXB1 . . . SPANX family member B1 . . TISSUE SPECIFICITY: Detected in testis and sperm. {ECO:0000269|PubMed:10906052, ECO:0000269|PubMed:12758128}.; . . 0.06195 . . . . . SPANXC 0.000589679869220244 0.282517097822247 0.716893222308532 SPANX family member C . . TISSUE SPECIFICITY: Detected in testis, melanoma and bladder carcinoma. {ECO:0000269|PubMed:10626816, ECO:0000269|PubMed:12758128}.; unclassifiable (Anatomical System);ovary;salivary gland;pharynx;colon;blood;breast;prostate;lung;visual apparatus;liver;testis;kidney;brain;bladder; . 0.08864 . 1.525013597 95.4824251 29.32097 0.93823 SPANXD 0.17781263582521 0.644483423875847 0.177703940298943 SPANX family member D . . TISSUE SPECIFICITY: Detected in testis, sperm and a melanoma cell line. {ECO:0000269|PubMed:12758128}.; . . . . 1.216305531 93.13517339 77.43021 1.84964 SPANXN1 0.510405170350752 0.421077308431123 0.0685175212181251 SPANX family member N1 . . . . . 0.00209 . 0.080983847 59.76055674 2.18478 0.07255 SPANXN2 2.5965752968708e-05 0.176248589967512 0.823725444279519 SPANX family member N2 . . . . . 0.02114 0.06617 0.413500896 76.67492333 185.07288 2.95382 SPANXN3 0.599707834595902 0.362541866364915 0.0377502990391829 SPANX family member N3 . . . . . 0.04307 . 0.215080721 67.91696155 55.09977 1.48747 SPANXN4 0.107493143744931 0.593289398198043 0.299217458057026 SPANX family member N4 . . . . . 0.01661 0.07170 0.257356108 69.83368719 230.02676 3.27867 SPANXN5 0.500966160239482 0.426448362678909 0.0725854770816092 SPANX family member N5 . . . . . 0.00016 . -0.031067188 51.03798066 0.13179 0.00244 SPARC 0.886494106065438 0.113249785003486 0.000256108931075996 secreted protein acidic and cysteine rich FUNCTION: Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity.; . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;lens;bile duct;breast;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;amnion;head and neck;kidney;mammary gland;stomach;aorta; uterus;dorsal root ganglion;adipose tissue;olfactory bulb;hypothalamus;spinal cord; 0.98278 0.76485 0.306902668 72.38145789 289.90705 3.64211 SPARCL1 1.07142828397564e-06 0.788566716330223 0.211432212241493 SPARC like 1 . . TISSUE SPECIFICITY: Highly expressed in lymph node, brain, heart, lung, skeletal muscle, ovary, small intestine, and colon, with lower levels in placenta, pancreas, testis, spleen, and thymus, and no expression in kidney, liver, and peripheral blood leukocytes.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;ganglion;frontal lobe;cochlea;endometrium;thyroid;brain;tonsil;heart;cartilage;spinal cord;blood;lens;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;dura mater;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);meninges;cerebellum cortex;lacrimal gland;islets of Langerhans;pancreas;lung;pia mater;adrenal gland;placenta;head and neck;kidney;stomach;aorta;thymus; amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.11241 0.08703 0.512596355 80.29606039 272.47173 3.53907 SPAST 0.99707471255289 0.0029252815119096 5.93520056629293e-09 spastin FUNCTION: ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and for completion of the abscission stage of cytokinesis. May also play a role in axon growth and the formation of axonal branches. {ECO:0000269|PubMed:11809724, ECO:0000269|PubMed:15716377, ECO:0000269|PubMed:16219033, ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:19000169, ECO:0000269|PubMed:22637577}.; DISEASE: Spastic paraplegia 4, autosomal dominant (SPG4) [MIM:182601]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. {ECO:0000269|PubMed:10610178, ECO:0000269|PubMed:10699187, ECO:0000269|PubMed:11015453, ECO:0000269|PubMed:11039577, ECO:0000269|PubMed:11087788, ECO:0000269|PubMed:11309678, ECO:0000269|PubMed:11843700, ECO:0000269|PubMed:11985387, ECO:0000269|PubMed:12124993, ECO:0000269|PubMed:12161613, ECO:0000269|PubMed:12163196, ECO:0000269|PubMed:12202986, ECO:0000269|PubMed:12460147, ECO:0000269|PubMed:12552568, ECO:0000269|PubMed:12939659, ECO:0000269|PubMed:14732620, ECO:0000269|PubMed:15159500, ECO:0000269|PubMed:15210521, ECO:0000269|PubMed:15248095, ECO:0000269|PubMed:15326248, ECO:0000269|PubMed:15482961, ECO:0000269|PubMed:16682546, ECO:0000269|PubMed:16684598, ECO:0000269|PubMed:17594340, ECO:0000269|PubMed:18613979, ECO:0000269|PubMed:20214791, ECO:0000269|PubMed:20550563, ECO:0000269|PubMed:20562464, ECO:0000269|PubMed:20718791, ECO:0000269|PubMed:20932283}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. The short isoforms may predominate in brain and spinal cord. {ECO:0000269|PubMed:10610178}.; unclassifiable (Anatomical System);ovary;colon;blood;lens;skeletal muscle;skin;breast;lung;frontal lobe;cochlea;oesophagus;placenta;thyroid;testis;germinal center;brain; amygdala;superior cervical ganglion;fetal brain;prefrontal cortex;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.67257 0.19777 -0.069700724 48.54328851 38.40565 1.13961 SPATA1 . . . spermatogenesis associated 1 . . . unclassifiable (Anatomical System);uterus;lung;endometrium;liver;testis;artery;skin;skeletal muscle;stomach;aorta; superior cervical ganglion;skeletal muscle; 0.10403 0.10073 . . . . SPATA2 0.848756563292112 0.150696727956039 0.000546708751849526 spermatogenesis associated 2 FUNCTION: May have a role in the regulation of spermatogenesis.; . TISSUE SPECIFICITY: Highly expressed in Sertoli cells, but not detected in spermatogenic cells. Low expression in spleen, thymus and prostate.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; whole brain;medulla oblongata;superior cervical ganglion;pons;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.32897 0.10658 -0.863377021 10.84571833 724.89387 5.34460 SPATA2L 0.0469218644980502 0.854987901159479 0.0980902343424711 spermatogenesis associated 2 like . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;urinary;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; trigeminal ganglion;skeletal muscle; 0.13174 0.10973 . . 81.5503 1.91264 SPATA2P1 . . . spermatogenesis associated 2 pseudogene 1 . . . . . . . . . . . SPATA3 . . . spermatogenesis associated 3 . . . lung;testis; . 0.02617 . 0.793752871 87.40268931 2573.32104 9.48704 SPATA3-AS1 . . . SPATA3 antisense RNA 1 (head to head) . . . . . . . . . . . SPATA4 0.000481541751455871 0.874845591716922 0.124672866531622 spermatogenesis associated 4 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12019456}.; unclassifiable (Anatomical System);medulla oblongata;lung;testis;pineal gland; testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.05183 0.06088 0.238945317 69.20853975 448.79417 4.40556 SPATA5 4.64814283804171e-10 0.938816399620498 0.0611835999146877 spermatogenesis associated 5 FUNCTION: May be involved in morphological and functional mitochondrial transformations during spermatogenesis. {ECO:0000250}.; . . unclassifiable (Anatomical System);breast;nasopharynx;liver;spleen;kidney;brain; dorsal root ganglion;testis - interstitial;subthalamic nucleus;superior cervical ganglion;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.16576 0.10805 -0.21856543 37.66218448 539.78034 4.73429 SPATA5L1 4.79851298392042e-11 0.191331366757377 0.808668633194638 spermatogenesis associated 5 like 1 . . . ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;whole body;endometrium;synovium;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;blood;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;duodenum;head and neck;cervix;kidney;mammary gland; testis - interstitial;superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion; 0.23011 0.08958 -0.222203495 37.54423213 4604.10601 13.61906 SPATA6 2.02900598310508e-11 0.119301168336542 0.880698831643168 spermatogenesis associated 6 FUNCTION: Required for formation of the sperm connecting piece during spermiogenesis. Sperm connecting piece is essential for linking the developing flagellum to the head during late spermiogenesis. May be involved in myosin-based microfilament transport through interaction with myosin subunits. {ECO:0000250|UniProtKB:Q3U6K5}.; . . . . 0.27738 0.10351 -0.310388054 32.14791224 3689.1245 11.83436 SPATA6L 1.92357114676295e-11 0.016903141272649 0.983096858708115 spermatogenesis associated 6 like . . . . . 0.07650 . 1.221756288 93.21184242 1763.48282 7.75583 SPATA7 3.13904072808556e-09 0.498062825735568 0.501937171125391 spermatogenesis associated 7 FUNCTION: Involved in photoreceptor cells maintenance (By similarity). It is required for recruitement and proper localization of RPGRIP1 to the photoreceptor connecting cilium (CC), as well as protein trafficking across the CC to the outer segments (By similarity). {ECO:0000250|UniProtKB:Q80VP2}.; DISEASE: Leber congenital amaurosis 3 (LCA3) [MIM:604232]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:19268277}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa autosomal recessive (ARRP) [MIM:268000]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:19268277}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;parathyroid;skin;uterus;prostate;endometrium;thyroid;bone;testis;pineal gland;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;skeletal muscle;pancreas;lung;adrenal gland;hippocampus;visual apparatus;liver;spleen;kidney; subthalamic nucleus;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;cingulate cortex; 0.08525 0.12355 1.13538281 92.30360934 3810.38782 12.13230 SPATA8 0.158580482360026 0.775005406996543 0.0664141106434314 spermatogenesis associated 8 . . TISSUE SPECIFICITY: Expressed at high levels in adult testis, at moderate levels in sperm and at low levels in fetal testis. Not detected in other tissues. {ECO:0000269|PubMed:16809841}.; unclassifiable (Anatomical System);medulla oblongata;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.05476 . 0.791937896 87.33781552 259.96249 3.46447 SPATA8-AS1 . . . SPATA8 antisense RNA 1 (head to head) . . . . . . . . . . . SPATA9 0.00218974170250578 0.755614820893608 0.242195437403886 spermatogenesis associated 9 FUNCTION: May play a role in testicular development/spermatogenesis and may be an important factor in male infertility. {ECO:0000269|PubMed:12493713}.; . TISSUE SPECIFICITY: Highly expressed in testes and pancreas. Low levels found in the heart, lungs, and brain. Very low expression detected in the placenta. No expression seen in skeletal muscle, liver, kidney, thymus, small intestine, colons, spleen, leukocytes, prostate gland, and ovary. In the adult testes, expression was about 6.44-fold higher than in the embryo testes. No expression in testes of patients with Sertoli-cell-only syndrome. In patients with arrest at spermatogonium and primary spermatocyte stages, no expression was detected. In patients with arrest at the spermatid stage, expression level was weak or absent. Variable expression was seen in patients with spermatogenic arrest. {ECO:0000269|PubMed:12493713}.; unclassifiable (Anatomical System);medulla oblongata;lymph node;lung;ovary;placenta;liver;testis;parathyroid;spleen;retina; subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05526 . 0.21689899 68.12927577 205.60965 3.09596 SPATA12 0.00717463491260291 0.532949559571675 0.459875805515722 spermatogenesis associated 12 . . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:15490870, ECO:0000269|PubMed:15603706}.; unclassifiable (Anatomical System);medulla oblongata;trophoblast;bone;testis; . 0.06059 . -0.117432389 44.89266336 36.59213 1.09795 SPATA13 0.528844213374764 0.471126750542511 2.90360827255139e-05 spermatogenesis associated 13 FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RHOA, RAC1 and CDC42 GTPases. Regulates cell migration and adhesion assembly and disassembly through a RAC1, PI3K, RHOA and AKT1-dependent mechanism. Increases both RAC1 and CDC42 activity, but decreases the amount of active RHOA. Required for MMP9 up- regulation via the JNK signaling pathway in colorectal tumor cells. Involved in tumor angiogenesis and may play a role in intestinal adenoma formation and tumor progression. {ECO:0000269|PubMed:17145773, ECO:0000269|PubMed:17599059, ECO:0000269|PubMed:19151759, ECO:0000269|PubMed:19893577, ECO:0000269|PubMed:19934221}.; . TISSUE SPECIFICITY: Expressed at high levels in the placenta, spleen and kidney, at moderate levels in lung, small intestine, liver, brain and heart, and at low levels in skeletal muscle. Expression is aberrantly enhanced in most colorectal tumors. {ECO:0000269|PubMed:17145773, ECO:0000269|PubMed:17599059, ECO:0000269|PubMed:19893577}.; unclassifiable (Anatomical System);colon;skeletal muscle;bone marrow;prostate;lung;larynx;nasopharynx;placenta;hypopharynx;testis;head and neck;germinal center;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.28685 0.11180 2.008142452 97.67044114 1024.01032 6.15271 SPATA13-AS1 . . . SPATA13 antisense RNA 1 . . . . . . . . . . . SPATA16 1.64842747374149e-06 0.85950814729848 0.140490204274046 spermatogenesis associated 16 FUNCTION: Involved in the formation of sperm acrosome, which implicated its potential role in spermatogenesis and sperm-egg fusion. {ECO:0000269|PubMed:12529416}.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:12529416}.; unclassifiable (Anatomical System);medulla oblongata;lung;testis; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.16188 . 1.732552414 96.59707478 5978.92356 16.10989 SPATA17 0.00473910823610697 0.993969548770955 0.00129134299293826 spermatogenesis associated 17 . . . . . 0.03924 0.08820 -0.134019284 43.90776126 361.81101 4.02527 SPATA17-AS1 . . . SPATA17 antisense RNA 1 . . . . . . . . . . . SPATA18 1.02781168487922e-11 0.274052487470867 0.725947512518855 spermatogenesis associated 18 FUNCTION: Key regulator of mitochondrial quality that mediates the repairing or degradation of unhealthy mitochondria in response to mitochondrial damage. Mediator of mitochondrial protein catabolic process (also named MALM) by mediating the degradation of damaged proteins inside mitochondria by promoting the accumulation in the mitochondrial matrix of hydrolases that are characteristic of the lysosomal lumen. Also involved in mitochondrion degradation of damaged mitochondria by promoting the formation of vacuole-like structures (named MIV), which engulf and degrade unhealthy mitochondria by accumulating lysosomes. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. {ECO:0000269|PubMed:21264221, ECO:0000269|PubMed:21264228, ECO:0000269|PubMed:22292033}.; . . unclassifiable (Anatomical System);medulla oblongata;heart;ovary;islets of Langerhans;spinal cord;parathyroid;skin;skeletal muscle;uterus;pancreas;prostate;lung;endometrium;hippocampus;testis;kidney;mammary gland; dorsal root ganglion;subthalamic nucleus;testis - interstitial;superior cervical ganglion;medulla oblongata;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18979 0.07948 0.113945049 62.14319415 240.479 3.35012 SPATA19 5.976953927201e-05 0.703360236834461 0.296579993626267 spermatogenesis associated 19 FUNCTION: May have a role in spermiogenesis.; . TISSUE SPECIFICITY: Expressed specifically in testis. {ECO:0000269|PubMed:12688595}.; placenta;testis; . 0.06185 0.07931 -0.05129383 49.75819769 4013.40317 12.54297 SPATA20 1.10605452840792e-05 0.999448941678595 0.000539997776120601 spermatogenesis associated 20 FUNCTION: May play a role in fertility regulation. {ECO:0000250}.; . . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus;cerebellum; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;testis; 0.14811 0.15540 -0.589727438 18.25902335 4840.85071 14.12229 SPATA20P1 . . . spermatogenesis associated 20 pseudogene 1 . . . . . . . . . . . SPATA21 3.58477021907411e-06 0.805625689851864 0.194370725377917 spermatogenesis associated 21 FUNCTION: Involved in the differentiation of haploid spermatids. {ECO:0000250}.; . . liver; . 0.61820 . 1.311772884 94.03750885 1596.30935 7.39143 SPATA22 0.000465618314810027 0.96584348714045 0.0336908945447404 spermatogenesis associated 22 FUNCTION: Meiosis-specific protein required for homologous recombination in meiosis I. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in adult testis. {ECO:0000269|PubMed:15713825}.; unclassifiable (Anatomical System);lung;placenta;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion; 0.12269 0.08105 1.0178651 90.91766926 524.1868 4.67003 SPATA24 . . . spermatogenesis associated 24 FUNCTION: Binds DNA with high affinity but does not bind to TATA boxes. Synergises with GMNN and TBP in activation of TATA box- containing promoters and with GMNN and TBPL1 in activation of the NF1 TATA-less promoter. May play a role in cytoplasm movement and removal during spermiogenesis (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymphoreticular;prostate;lung;thyroid;testis;kidney;lens;brain;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . 0.479642105 78.95140363 3874.2515 12.27241 SPATA25 0.000413851176082059 0.408266339364787 0.591319809459131 spermatogenesis associated 25 FUNCTION: May play a role in spermatogenesis. {ECO:0000269|PubMed:19240080}.; . TISSUE SPECIFICITY: Expressed predominantly in testis (at protein level). Expression is lower in patients with obstructive azoospermia than in fertile controls and is not detected in patients with non-obstructive azoospermia. {ECO:0000269|PubMed:19240080}.; . . 0.52005 . 0.994001092 90.5579146 339.72468 3.90957 SPATA31A1 . . . SPATA31 subfamily A, member 1 FUNCTION: May play a role in spermatogenesis. {ECO:0000250}.; . . . . 0.14453 . . . 12.18693 0.44112 SPATA31A3 . . . SPATA31 subfamily A, member 3 FUNCTION: May play a role in spermatogenesis. {ECO:0000250}.; . . . . . . . . 828.13381 5.64190 SPATA31A5 . . . SPATA31 subfamily A, member 5 FUNCTION: May play a role in spermatogenesis. {ECO:0000250}.; . . . . . . . . 0.9918 0.02516 SPATA31A6 . . . SPATA31 subfamily A, member 6 FUNCTION: May play a role in spermatogenesis. {ECO:0000250}.; . . . . 0.07776 . . . 5699.84632 15.62971 SPATA31A7 0.481345574657339 0.437046513240158 0.0816079121025036 SPATA31 subfamily A, member 7 FUNCTION: May play a role in spermatogenesis. {ECO:0000250}.; . . . . . . . . 4.78037 0.17375 SPATA31B1P . . . SPATA31 subfamily B, member 1, pseudogene FUNCTION: May play a role in spermatogenesis. {ECO:0000250}.; . . . . 0.02629 . . . . . SPATA31C1 . . . SPATA31 subfamily C, member 1 FUNCTION: May play a role in spermatogenesis. {ECO:0000250}.; . . . . . . . . . . SPATA31C2 . . . SPATA31 subfamily C, member 2 FUNCTION: May play a role in spermatogenesis. {ECO:0000250}.; . . . . . . . . . . SPATA31D1 2.73056573499066e-09 0.895265407360888 0.104734589908546 SPATA31 subfamily D, member 1 FUNCTION: May play a role in spermatogenesis. {ECO:0000250}.; . . . . . . 0.567546387 81.73507903 574.19627 4.86300 SPATA31D2P . . . SPATA31 subfamily D, member 2, pseudogene . . . . . . . . . . . SPATA31D3 . . . SPATA31 subfamily D, member 3 FUNCTION: May play a role in spermatogenesis. {ECO:0000250}.; . . . . . . . . . . SPATA31D4 . . . SPATA31 subfamily D, member 4 FUNCTION: May play a role in spermatogenesis. {ECO:0000250}.; . . . . . . . . . . SPATA31D5P . . . SPATA31 subfamily D, member 5, pseudogene . . . . . . . . . . . SPATA31E1 6.08488739187726e-21 0.000416282960518093 0.999583717039482 SPATA31 subfamily E, member 1 FUNCTION: May play a role in spermatogenesis. {ECO:0000250}.; . . . . 0.03752 . 3.561964917 99.51049776 5935.28204 16.02016 SPATA31E2P . . . SPATA31 subfamily E, member 2, pseudogene . . . . . . . . . . . SPATA31E3P . . . SPATA31 subfamily E, member 3, pseudogene . . . . . . . . . . . SPATA32 2.95265117999751e-05 0.550511536575264 0.449458936912936 spermatogenesis associated 32 . . TISSUE SPECIFICITY: Detected in testis, and on the acrosomal cap of spermatids.; . . 0.24350 0.07105 -0.201976964 38.98325077 643.83669 5.09784 SPATA33 2.72892869796854e-06 0.0936088594675988 0.906388411603703 spermatogenesis associated 33 . . . . . 0.07386 . 0.483275131 79.25218212 717.34983 5.31506 SPATA41 . . . spermatogenesis associated 41 (non-protein coding) . . . . . . . . . . . SPATA42 . . . spermatogenesis associated 42 (non-protein coding) . . . . . . . . . . . SPATA45 . . . spermatogenesis associated 45 . . . . . . . 0.169169615 65.33380514 . . SPATC1 3.5903133043143e-08 0.185342978730468 0.814656985366399 spermatogenesis and centriole associated 1 . . TISSUE SPECIFICITY: Detected only in testis. {ECO:0000269|PubMed:20542897}.; . . 0.14705 0.08702 0.450099045 78.01958009 386.52546 4.14068 SPATC1L 3.78329490177049e-06 0.112509999964351 0.887486216740748 spermatogenesis and centriole associated 1-like . . . . . 0.17144 0.10852 1.196071381 92.92285916 2390.66602 9.07330 SPATS1 0.000191249661738644 0.713803183422324 0.286005566915937 spermatogenesis associated serine rich 1 . . . unclassifiable (Anatomical System);medulla oblongata;lung;bone;testis;brain; . 0.07406 0.08059 0.238945317 69.20853975 1147.427 6.45608 SPATS2 0.989651259812943 0.01034860996946 1.30217596931891e-07 spermatogenesis associated serine rich 2 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pineal body;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion; 0.11949 0.08494 -0.268115223 34.70747818 290.02044 3.64416 SPATS2L 0.970345371568033 0.0296460334909617 8.59494100566649e-06 spermatogenesis associated serine rich 2 like . . . lymphoreticular;smooth muscle;ovary;skin;retina;prostate;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;urinary;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;thymus; . . . 0.174625237 65.9648502 1810.92534 7.85090 SPC24 0.00627554442927794 0.741565201319525 0.252159254251198 SPC24, NDC80 kinetochore complex component FUNCTION: Acts as a component of the essential kinetochore- associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity (PubMed:14738735). Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (PubMed:14738735). The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules (PubMed:23085020). {ECO:0000269|PubMed:14738735, ECO:0000269|PubMed:23085020}.; . . . . 0.08605 0.11889 0.413500896 76.67492333 270.60416 3.52755 SPC25 0.0594294501038599 0.923512797859223 0.0170577520369172 SPC25, NDC80 kinetochore complex component FUNCTION: Acts as a component of the essential kinetochore- associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity (PubMed:14699129, PubMed:14738735). Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (PubMed:14738735, PubMed:14699129). The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules (PubMed:23085020). {ECO:0000269|PubMed:14699129, ECO:0000269|PubMed:14738735, ECO:0000269|PubMed:23085020}.; . . unclassifiable (Anatomical System);lymph node;ovary;salivary gland;intestine;pharynx;colon;blood;breast;prostate;whole body;lung;bone;placenta;visual apparatus;liver;testis;spleen;germinal center;kidney;brain;bladder; ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.49264 0.11809 0.014844891 54.94810097 94.88564 2.09977 SPCS1 0.118910837533606 0.779313528471502 0.101775633994892 signal peptidase complex subunit 1 FUNCTION: Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. {ECO:0000250}.; . . medulla oblongata;ovary;skin;bone marrow;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;cornea;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta; amygdala;whole brain;testis - interstitial;testis - seminiferous tubule;liver;testis; 0.18921 0.11640 0.301449681 71.80938901 1823.69522 7.87942 SPCS2 0.725113280909428 0.261872775709006 0.0130139433815657 signal peptidase complex subunit 2 FUNCTION: Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. {ECO:0000250}.; . . lymphoreticular;ovary;salivary gland;developmental;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;urinary;pharynx;blood;lens;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hypopharynx;duodenum;liver;head and neck;spleen;kidney;mammary gland;aorta;stomach;thymus; . 0.58785 0.11753 0.013025609 54.62962963 13.04807 0.47493 SPCS2P1 . . . signal peptidase complex subunit 2 homolog (S. cerevisiae) pseudogene 1 . . . . . . . . . . . SPCS2P2 . . . signal peptidase complex subunit 2 homolog (S. cerevisiae) pseudogene 2 . . . . . . . . . . . SPCS2P3 . . . signal peptidase complex subunit 2 homolog (S. cerevisiae) pseudogene 3 . . . . . . . . . . . SPCS2P4 . . . signal peptidase complex subunit 2 homolog (S. cerevisiae) pseudogene 4 . . . . . . . . . . . SPCS3 0.697040878974778 0.285902182450884 0.0170569385743381 signal peptidase complex subunit 3 FUNCTION: Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. {ECO:0000250}.; . . . . 0.09212 0.10812 0.013025609 54.62962963 2.14301 0.07142 SPDEF 0.711825442176907 0.284855427981009 0.00331912984208406 SAM pointed domain containing ETS transcription factor FUNCTION: May function as an androgen-independent transactivator of the prostate-specific antigen (PSA) promoter. Binds to 5'-GGAT- 3' DNA sequences. May play a role in the regulation of the prostate gland and/or prostate cancer development. Acts as a transcriptional activator for SERPINB5 promoter. {ECO:0000269|PubMed:10625666}.; . TISSUE SPECIFICITY: Expressed in a very restricted set of primarily hormone-regulated epithelial tissues with particularly high expression in the prostate gland. Significantly lower expression is seen in other hormone regulated tissues such as mammary gland, salivary gland, and ovary. Expressed in prostate carcinoma cells. {ECO:0000269|PubMed:10625666}.; . . 0.16864 0.16287 0.310540264 72.65864591 804.06555 5.58689 SPDL1 8.71550549150675e-10 0.701754272396086 0.298245726732364 spindle apparatus coiled-coil protein 1 FUNCTION: Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. Also required for correct spindle orientation. Does not appear to be required for the removal of spindle assembly checkpoint (SAC) proteins from the kinetochore upon bipolar spindle attachment. {ECO:0000255|HAMAP-Rule:MF_03041, ECO:0000269|PubMed:17576797, ECO:0000269|PubMed:19468067}.; . . . . 0.12115 0.08256 1.247448154 93.43595188 225.03002 3.24338 SPDYA 0.166884223990281 0.818835948181536 0.0142798278281825 speedy/RINGO cell cycle regulator family member A FUNCTION: Regulates the G1/S phase transition of the cell cycle by binding and activating CDK1, CDK2 and CDKN1B/KIP1. Can activate CDK2 without promoting CDK2 phosphorylation. Mediates cell survival during the DNA damage process through activation of CDK2. {ECO:0000269|PubMed:11980914, ECO:0000269|PubMed:12839962, ECO:0000269|PubMed:12972555}.; . TISSUE SPECIFICITY: Highly expressed in testis. Expressed at a low level in wide range of tissues including bone marrow, brain, heart, kidney, colon, liver, placenta, spleen, skeletal muscle, salivary gland, thyroid gland, thymus, trachea and uterus. Expressed at a slightly higher level in adrenal gland, cerebellum, small intestine, lung, prostate and trachea. Expression is cell cycle-dependent, being restricted to cells in G1/S phase. {ECO:0000269|PubMed:11980914, ECO:0000269|PubMed:15611625}.; unclassifiable (Anatomical System);lymph node;heart;ovary;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;lung;endometrium;placenta;macula lutea;liver;testis;spleen;kidney;brain;gall bladder;peripheral nerve; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node; 0.06107 0.08388 0.103030231 61.2762444 55.16447 1.48935 SPDYC 0.00185514874297755 0.902340267799731 0.0958045834572913 speedy/RINGO cell cycle regulator family member C FUNCTION: Promotes progression through the cell cycle via binding and activation of CDK1 and CDK2. Involved in the spindle-assembly checkpoint. Required for recruitment of MAD2L1, BUBR1 and BUB1 to kinetochores. Required for the correct localization of the active form of Aurora B in prometaphase. {ECO:0000269|PubMed:15611625, ECO:0000269|PubMed:20605920}.; . TISSUE SPECIFICITY: Expressed in a variety of tissues including bone marrow, kidney, small intestine, liver, placenta and testis. {ECO:0000269|PubMed:15611625}.; . . 0.12491 . -0.492218069 22.35786742 27.8107 0.89327 SPDYE1 0.206335952529226 0.78418729106461 0.00947675640616365 speedy/RINGO cell cycle regulator family member E1 . DISEASE: Note=SPDYE1 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region (PubMed:12073013). {ECO:0000269|PubMed:12073013}.; . unclassifiable (Anatomical System);medulla oblongata;heart;colon;blood;bone marrow;uterus;lung;frontal lobe;endometrium;epididymis;larynx;thyroid;placenta;pituitary gland;hypopharynx;liver;testis;cervix;head and neck;germinal center;brain;stomach;cerebellum; . 0.09348 . . . 901.03432 5.84607 SPDYE2 . . . speedy/RINGO cell cycle regulator family member E2 . . . unclassifiable (Anatomical System);colon;blood;bone marrow;uterus;lung;frontal lobe;larynx;epididymis;placenta;pituitary gland;liver;testis;head and neck;cervix;brain;mammary gland;stomach; . . . . . 2.4122 0.08521 SPDYE2B . . . speedy/RINGO cell cycle regulator family member E2B . . . . . . . . . . . SPDYE3 0.825434138244106 0.173760887065771 0.000804974690123047 speedy/RINGO cell cycle regulator family member E3 . . . unclassifiable (Anatomical System);heart;colon;blood;bone marrow;uterus;lung;frontal lobe;epididymis;larynx;thyroid;placenta;pituitary gland;hypopharynx;liver;testis;cervix;head and neck;kidney;brain;bladder;stomach; . . . . . 7.34499 0.27357 SPDYE4 0.00122166678944778 0.848522991234912 0.15025534197564 speedy/RINGO cell cycle regulator family member E4 . . . lung;testis; . . . 0.459411326 78.28497287 220.96196 3.21489 SPDYE5 . . . speedy/RINGO cell cycle regulator family member E5 . . . . . . . . . . . SPDYE6 . . . speedy/RINGO cell cycle regulator family member E6 . . . . . . . . . . . SPDYE7P . . . speedy/RINGO cell cycle regulator family member E7, pseudogene . . . . . . . . . . . SPDYE8P . . . speedy/RINGO cell cycle regulator family member E8, pseudogene . . . unclassifiable (Anatomical System);medulla oblongata;heart;colon;lung;frontal lobe;larynx;epididymis;thyroid;placenta;hypopharynx;testis;head and neck;cervix;kidney;brain;stomach; . . . . . . . SPDYE9P . . . speedy/RINGO cell cycle regulator family member E9, pseudogene . . . . . . . . . . . SPDYE10P . . . speedy/RINGO cell cycle regulator family member E10, pseudogene . . . . . . . . . . . SPDYE11 . . . speedy/RINGO cell cycle regulator family member E11 . . . . . . . . . . . SPDYE12P . . . speedy/RINGO cell cycle regulator family member E12, pseudogene . . . . . . . . . . . SPDYE13P . . . speedy/RINGO cell cycle regulator family member E13, pseudogene . . . . . . . . . . . SPDYE14P . . . speedy/RINGO cell cycle regulator family member E14, pseudogene . . . . . . . . . . . SPDYE15P . . . speedy/RINGO cell cycle regulator family member E15, pseudogene . . . . . . . . . . . SPDYE16 . . . speedy/RINGO cell cycle regulator family member E16 . . . . . . . . . . . SPDYE17 . . . speedy/RINGO cell cycle regulator family member E17 . . . . . . . . . . . SPDYE18 . . . speedy/RINGO cell cycle regulator family member E18 . . . . . . . . . . . SPDYE19P . . . speedy/RINGO cell cycle regulator family member E19, pseudogene . . . . . . . . . . . SPDYE20P . . . speedy/RINGO cell cycle regulator family member E20, pseudogene . . . . . . . . . . . SPDYE21P . . . speedy/RINGO cell cycle regulator family member E21, pseudogene . . . . . . . . . . . SPDYE22P . . . speedy/RINGO cell cycle regulator family member E22, pseudogene . . . . . . . . . . . SPECC1 0.109459640243662 0.890529471530206 1.08882261309888e-05 sperm antigen with calponin homology and coiled-coil domains 1 . . TISSUE SPECIFICITY: Highly expressed in testis. Barely detectable in other tissues. Also highly expressed in some cancer cell lines. {ECO:0000269|PubMed:15602574}.; ovary;colon;skin;uterus;prostate;frontal lobe;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;nervous;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09633 0.08753 -1.188670131 5.891719745 1303.95464 6.79495 SPECC1L 0.993395147293948 0.00660485263333291 7.27189738020931e-11 sperm antigen with calponin homology and coiled-coil domains 1-like FUNCTION: Involved in cytokinesis and spindle organization. May play a role in actin cytoskeleton organization and microtubule stabilization and hence required for proper cell adhesion and migration. {ECO:0000269|PubMed:21703590}.; DISEASE: Facial clefting, oblique, 1 (OBLFC1) [MIM:600251]: A rare form of facial clefting. A facial cleft is any of the fissures between the embryonic prominences that normally unite to form the face. {ECO:0000269|PubMed:21703590}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Opitz GBBB syndrome 2 (GBBB2) [MIM:145410]: A form of Opitz GBBB syndrome, a congenital midline malformation syndrome characterized by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, cleft lip/palate, laryngotracheoesophageal abnormalities, imperforate anus, developmental delay and congenital heart defects. {ECO:0000269|PubMed:25412741}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;amnion;liver;spleen;kidney;mammary gland;aorta;stomach;cerebellum; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.12260 0.10757 -0.282886048 33.53385232 294.43697 3.66528 SPECC1L-ADORA2A . . . SPECC1L-ADORA2A readthrough (NMD candidate) . . . . . . . . . . . SPEF1 0.000189254509549096 0.711622210613318 0.288188534877133 sperm flagellar 1 . . . . . 0.09493 0.10400 0.3032669 72.009908 119.77968 2.38323 SPEF2 2.02916164361718e-16 0.999845605768787 0.00015439423121315 sperm flagellar 2 FUNCTION: Required for correct axoneme development. {ECO:0000250}.; . . heart;tongue;adrenal cortex;parathyroid;blood;skin;skeletal muscle;bone marrow;uterus;whole body;lung;endometrium;adrenal gland;bone;thyroid;testis;head and neck;kidney;pineal gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.11891 0.11186 2.82254163 99.06817646 4754.8419 13.95350 SPEG 0.999790421916053 0.000209578083946633 9.1693036443509e-21 SPEG complex locus FUNCTION: Isoform 3 may have a role in regulating the growth and differentiation of arterial smooth muscle cells.; DISEASE: Myopathy, centronuclear, 5 (CNM5) [MIM:615959]: A form of centronuclear myopathy, a congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers. CNM5 features include severe neonatal hypotonia with respiratory insufficiency, difficulty feeding, and delayed motor development. Some patients die in infancy, and some develop dilated cardiomyopathy. {ECO:0000269|PubMed:25087613}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is preferentially expressed in striated muscle. Non-kinase form such as isoform 3 is predominantly expressed in the aorta. Isoform 3 appears to be expressed only in highly differentiated ASMC in normal vessel walls and down-regulated in dedifferentiated ASMC in vivo. In response to vascular injuries ASMC dedifferentiate and change from a quiescent and contractile phenotype to a proliferative and synthetic phenotype. This proliferation of vascular smooth muscle cells is one of the most prominent features of atherosclerosis. {ECO:0000269|PubMed:15185077, ECO:0000269|PubMed:8663449}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;pituitary gland;testis;brain;spinal ganglion;unclassifiable (Anatomical System);heart;cartilage;muscle;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;head and neck;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;cingulate cortex;skeletal muscle;cerebellum; 0.41136 0.12798 -0.055373944 48.92073602 8867.59165 20.31253 SPEM1 0.0234530633409911 0.913435786806629 0.0631111498523799 spermatid maturation 1 FUNCTION: Required for proper cytoplasm removal during spermatogenesis. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;testis; . 0.03702 . 0.485092724 79.37603208 739.00476 5.39660 SPEN 0.999999999999963 3.7044063712041e-14 1.68766999991888e-35 spen family transcriptional repressor FUNCTION: May serve as a nuclear matrix platform that organizes and integrates transcriptional responses. In osteoblasts, supports transcription activation: synergizes with RUNX2 to enhance FGFR2- mediated activation of the osteocalcin FGF-responsive element (OCFRE) (By similarity). Has also been shown to be an essential corepressor protein, which probably regulates different key pathways such as the Notch pathway. Negative regulator of the Notch pathway via its interaction with RBPSUH, which prevents the association between NOTCH1 and RBPSUH, and therefore suppresses the transactivation activity of Notch signaling. Blocks the differentiation of precursor B-cells into marginal zone B-cells. Probably represses transcription via the recruitment of large complexes containing histone deacetylase proteins. May bind both to DNA and RNA. {ECO:0000250, ECO:0000269|PubMed:11331609, ECO:0000269|PubMed:12374742}.; . TISSUE SPECIFICITY: Expressed at high level in brain, testis, spleen and thymus. Expressed at intermediate level in kidney, liver, mammary gland and skin.; . . 0.87812 0.15972 -2.307490096 1.209011559 1380.73788 6.96380 SPERT 0.000527781321155571 0.693131368767753 0.306340849911092 spermatid associated . . . unclassifiable (Anatomical System); . 0.27073 0.10393 -0.025608647 51.91672564 3154.36113 10.69389 SPESP1 1.97658953424779e-05 0.466286402897718 0.533693831206939 sperm equatorial segment protein 1 . . TISSUE SPECIFICITY: Highly expressed in testis, where it is localized in the acrosome of postmeiotic stages of spermiogenesis (round and elongating spermatids and in ejaculated spermatozoa) (at protein level). Poorly expressed in placenta and fetal lung. {ECO:0000269|PubMed:12773409}.; unclassifiable (Anatomical System);medulla oblongata;ovary;hypothalamus;salivary gland;spinal cord;intestine;pharynx;colon;parathyroid;blood;skin;breast;prostate;lung;bone;placenta;pituitary gland;liver;testis;kidney;brain;mammary gland;bladder; . 0.05834 0.07337 0.128714042 63.19886766 403.89983 4.21741 SPG3B . . . spastic paraplegia 3B . . . . . . . . . . . SPG5B . . . spastic paraplegia 5B (autosomal recessive) . . . . . . . . . . . SPG7 1.38467339967464e-18 0.00528518727237 0.99471481272763 SPG7, paraplegin matrix AAA peptidase subunit FUNCTION: Putative ATP-dependent zinc metalloprotease.; DISEASE: Note=Defects in SPG7 may cause autosomal recessive osteogenesis imperfecta (OI). Osteogenesis imperfecta defines a group of connective tissue disorders characterized by bone fragility and low bone mass. Clinical features of SPG7-related osteogenesis imperfecta include recurrent fractures, mild bone deformities, delayed tooth eruption, normal hearing and white sclera.; TISSUE SPECIFICITY: Ubiquitous.; myocardium;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;oral cavity;muscle;blood;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; whole brain;amygdala;subthalamic nucleus;thyroid;prefrontal cortex;testis;cingulate cortex; 0.13976 . -1.052752328 7.619721632 2153.42654 8.54208 SPG9 . . . spastic paraplegia 9 (autosomal dominant) . . . . . . . . . . . SPG11 2.91203449273578e-22 0.99568625069984 0.00431374930016003 spastic paraplegia 11 (autosomal recessive) . . TISSUE SPECIFICITY: Expressed in all structures of brain, with a high expression in cerebellum. {ECO:0000269|PubMed:17322883}.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;pia mater;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;thyroid;testis;ciliary ganglion; 0.48298 0.11280 -0.481610219 22.78839349 5573.81365 15.43136 SPG14 . . . spastic paraplegia 14 (autosomal recessive) . . . . . . . . . . . SPG16 . . . spastic paraplegia 16 (complicated, X-linked recessive) . . . . . . . . . . . SPG18 . . . spastic paraplegia 18 (autosomal dominant) . . . . . . . . . . . SPG19 . . . spastic paraplegia 19 (autosomal dominant) . . . . . . . . . . . SPG20 0.000159489204272841 0.967927119730906 0.0319133910648209 spastic paraplegia 20 (Troyer syndrome) FUNCTION: May be implicated in endosomal trafficking, or microtubule dynamics, or both. Participates in cytokinesis (PubMed:20719964). {ECO:0000269|PubMed:20719964}.; DISEASE: Spastic paraplegia 20, autosomal recessive (SPG20) [MIM:275900]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG20 is characterized by dysarthria, distal amyotrophy, mild developmental delay and short stature. {ECO:0000269|PubMed:12134148}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels of expression detected in adipose tissue.; ovary;sympathetic chain;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;thyroid;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.16741 0.10762 -0.486758915 22.69992923 75.82168 1.82455 SPG20-AS1 . . . SPG20 antisense RNA 1 . . . . . . . . . . . SPG21 9.88307687455965e-05 0.801736722137108 0.198164447094146 spastic paraplegia 21 (autosomal recessive, Mast syndrome) FUNCTION: May play a role as a negative regulatory factor in CD4- dependent T-cell activation. {ECO:0000269|PubMed:11113139}.; . TISSUE SPECIFICITY: Expressed in all tissues tested, including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Expressed in J.CaM1.6, HuT 78 and HeLa cell lines (at protein level). {ECO:0000269|PubMed:11113139}.; ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;amygdala;heart;cartilage;pharynx;blood;lens;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;placenta;thyroid;liver;ciliary ganglion;atrioventricular node;kidney;pons;trigeminal ganglion; 0.19919 0.23664 -0.183570861 39.95046001 18.4177 0.63849 SPG23 . . . spastic paraplegia 23 (autosomal recessive) . . . . . . . . . . . SPG24 . . . spastic paraplegia 24 (autosomal recessive) . . . . . . . . . . . SPG25 . . . spastic paraplegia 25 (autosomal recessive, with disc herniation) . . . . . . . . . . . SPG27 . . . spastic paraplegia 27 (autosomal recessive) . . . . . . . . . . . SPG29 . . . spastic paraplegia 29 (autosomal dominant) . . . . . . . . . . . SPG32 . . . spastic paraplegia 32 (autosomal recessive) . . . . . . . . . . . SPG34 . . . spastic paraplegia 34 (autosomal dominant) . . . . . . . . . . . SPG36 . . . spastic paraplegia 36 (autosomal dominant) . . . . . . . . . . . SPG37 . . . spastic paraplegia 37 (autosomal dominant) . . . . . . . . . . . SPG38 . . . spastic paraplegia 38 (autosomal dominant, Silver syndrome) . . . . . . . . . . . SPG41 . . . spastic paraplegia 41 (autosomal dominant) . . . . . . . . . . . SPG45 . . . spastic paraplegia 45 (autosomal recessive) . . . . . . . . . . . SPG56 . . . spastic paraplegia 56 (autosomal dominant) . . . . . . . . . . . SPHAR 0.0144631168350946 0.446327986040279 0.539208897124626 S-phase response (cyclin related) . . . . . . . 0.101211609 60.95777306 0.7837 0.01446 SPHK1 1.29152628928557e-05 0.384668629642745 0.615318455094362 sphingosine kinase 1 FUNCTION: Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-sphingosine and to a lesser extent sphinganine, but not other lipids, such as D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine, diacylglycerol, ceramide, or phosphatidylinositol. {ECO:0000269|PubMed:20577214, ECO:0000269|PubMed:23602659}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in adult liver, kidney, heart and skeletal muscle. {ECO:0000269|PubMed:10802064}.; ovary;colon;fovea centralis;vein;skin;retina;uterus;optic nerve;endometrium;larynx;bone;spinal ganglion;brain;unclassifiable (Anatomical System);heart;lens;pancreas;lung;placenta;macula lutea;liver;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.13379 0.23621 -0.222203495 37.54423213 2111.50585 8.46032 SPHK2 8.66423863572204e-06 0.763002690933675 0.236988644827689 sphingosine kinase 2 FUNCTION: Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro- dihydrosphingosine, D-erythro-sphingosine and L-threo- dihydrosphingosine. Binds phosphoinositides. {ECO:0000269|PubMed:19168031}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;thyroid;testis;dura mater;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);meninges;lymph node;muscle;pharynx;blood;lens;breast;pancreas;pia mater;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;kidney;stomach; whole brain;thalamus;hypothalamus;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;testis;ciliary ganglion;kidney;trigeminal ganglion;cingulate cortex;parietal lobe; 0.08982 0.15279 0.134171522 63.57041755 442.11306 4.37687 SPHKAP 0.233358014706211 0.766641469438858 5.15854931360161e-07 SPHK1 interactor, AKAP domain containing FUNCTION: Anchoring protein that binds preferentially to the type I regulatory subunit of c-AMP-dependent protein kinase (PKA type I) and targets it to distinct subcellular compartments. May act as a converging factor linking cAMP and sphingosine signaling pathways. Plays a regulatory role in the modulation of SPHK1. {ECO:0000269|PubMed:12080051, ECO:0000269|PubMed:20394097}.; . TISSUE SPECIFICITY: Highly expressed in heart. Both isoforms abundantly expressed in ventricle. Also expressed in spleen, ovary and brain. {ECO:0000269|PubMed:12080051, ECO:0000269|PubMed:20394097}.; unclassifiable (Anatomical System);lung;atrium;whole body;frontal lobe;heart;brain;skeletal muscle;cerebellum; amygdala;dorsal root ganglion;cerebellum peduncles;globus pallidus;trigeminal ganglion;cerebellum; 0.17559 0.08765 -0.799360934 12.33781552 1486.23576 7.17525 SPI1 0.89723051716191 0.101809698092199 0.000959784745891443 Spi-1 proto-oncogene FUNCTION: Binds to the PU-box, a purine-rich DNA sequence (5'- GAGGAA-3') that can act as a lymphoid-specific enhancer. This protein is a transcriptional activator that may be specifically involved in the differentiation or activation of macrophages or B- cells. Also binds RNA and may modulate pre-mRNA splicing (By similarity). {ECO:0000250}.; . . lymphoreticular;colon;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;blood;lens;lung;placenta;macula lutea;liver;spleen;kidney;stomach;thymus; whole blood; 0.31824 0.66820 -0.163345027 41.24793583 47.34446 1.33535 SPIB 0.899853669858548 0.0992480825896376 0.00089824755181464 Spi-B transcription factor FUNCTION: Sequence specific transcriptional activator which binds to the PU-box, a purine-rich DNA sequence (5'-GAGGAA-3') that can act as a lymphoid-specific enhancer. Promotes development of plasmacytoid dendritic cells (pDCs), also known as type 2 DC precursors (pre-DC2) or natural interferon (IFN)-producing cells. These cells have the capacity to produce large amounts of interferon and block viral replication. May be required for B-cell receptor (BCR) signaling, which is necessary for normal B-cell development and antigenic stimulation. {ECO:0000269|PubMed:10196196, ECO:0000269|PubMed:12393575, ECO:0000269|PubMed:1406622, ECO:0000269|PubMed:15583020}.; . TISSUE SPECIFICITY: Expressed in plasmacytoid dendritic cells (pDCs) and B-cells, not expressed in T-cells or granulocytes. May also be enriched in stem cell populations of the liver. {ECO:0000269|PubMed:11841448, ECO:0000269|PubMed:12393575}.; unclassifiable (Anatomical System);lymphoreticular;lymph node;lung;heart;nasopharynx;liver;testis;spleen;germinal center;tonsil; superior cervical ganglion; 0.53861 0.18604 -0.249709319 35.74545883 365.33713 4.04495 SPIC 0.118412347531258 0.855578742474994 0.0260089099937483 Spi-C transcription factor FUNCTION: Controls the development of red pulp macrophages required for red blood cells recycling and iron homeostasis. Transcription factor that binds to the PU-box, a purine-rich DNA sequence (5'-GAGGA[AT]-3') that can act as a lymphoid-specific enhancer. Regulates VCAM1 gene expression (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Preferentially detected in fetal and adult spleen, lymph nodes and at lower levels in bone marrow and fetal liver. {ECO:0000269|PubMed:12459275}.; pancreas;lung;spleen; . 0.14546 0.10759 -0.095386216 46.48502005 327.55202 3.84720 SPICE1 5.13620862858274e-08 0.990209074204427 0.00979087443348678 spindle and centriole associated protein 1 FUNCTION: Regulator required for centriole duplication, for proper bipolar spindle formation and chromosome congression in mitosis. {ECO:0000269|PubMed:20736305}.; . . unclassifiable (Anatomical System);heart;ovary;colon;skin;uterus;breast;lung;bone;placenta;visual apparatus;iris;liver;testis;germinal center;brain;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13123 . 0.249861693 69.66265629 475.73296 4.50529 SPIDR 1.0712969110463e-14 0.0384412488943954 0.961558751105594 scaffolding protein involved in DNA repair FUNCTION: Plays a role in DNA double-strand break (DBS) repair via homologous recombination (HR). Serves as a scaffolding protein that helps to promote the recruitment of DNA-processing enzymes like the helicase BLM and recombinase RAD51 to site of DNA damage, and hence contributes to maintain genomic integrity. {ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:23754376}.; . . . . . . -0.310388054 32.14791224 337.45721 3.90084 SPIN1 0.925083438998768 0.0744874654104462 0.00042909559078549 spindlin 1 FUNCTION: Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and asymmetrically dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator of Wnt signaling pathway dowstream of PRMT2. In case of cancer, promotes cell cancer proliferation via activation of the Wnt signaling pathway (PubMed:24589551). Overexpression induces metaphase arrest and chromosomal instability. Localizes to active rDNA loci and promotes the expression of rRNA genes (PubMed:21960006). May play a role in cell-cycle regulation during the transition from gamete to embryo. Involved in oocyte meiotic resumption, a process that takes place before ovulation to resume meiosis of oocytes blocked in prophase I: may act by regulating maternal transcripts to control meiotic resumption. {ECO:0000269|PubMed:21960006, ECO:0000269|PubMed:22258766, ECO:0000269|PubMed:24589551}.; . TISSUE SPECIFICITY: Highly expressed in ovarian cancer tissues. {ECO:0000269|PubMed:22258766}.; . . 0.06492 0.10955 0.013025609 54.62962963 4.08527 0.14932 SPIN2A 0.220661420438701 0.647506960714643 0.131831618846656 spindlin family member 2A FUNCTION: May be involved in the regulation of cell cycle progression. {ECO:0000250}.; . . . . 0.27614 0.12085 . . 76.55118 1.83640 SPIN2B 0.620083821072506 0.347469803528147 0.0324463753993472 spindlin family member 2B FUNCTION: Involved in the regulation of cell cycle progression, this activity is related to the inhibition of apoptosis following the removal of essential growth factors. {ECO:0000269|PubMed:12145692}.; . TISSUE SPECIFICITY: Detected in all the examined tissues with highest expression in liver, followed by heart, stomach, kidney, skeletal muscle, placenta, and pancreas.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;skin;retina;uterus;breast;prostate;lung;bone;placenta;hippocampus;cervix;spleen;germinal center;kidney;brain;stomach; . 0.27520 0.11878 . . 0.67512 0.01067 SPIN3 0.674771547942128 0.304407720586234 0.0208207314716374 spindlin family member 3 . . . . . 0.19065 0.13425 -0.141298762 42.87567823 12.82343 0.46750 SPIN4 0.725861947192611 0.261221908531696 0.012916144275693 spindlin family member 4 . . . unclassifiable (Anatomical System);uterus;colon;skin;skeletal muscle;bone marrow; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.23813 . -0.009020804 52.8544468 2.30977 0.07888 SPIN4-AS1 . . . SPIN4 antisense RNA 1 . . . . . . . . . . . SPINK1 0.293111298714489 0.626091857267819 0.080796844017692 serine peptidase inhibitor, Kazal type 1 FUNCTION: Serine protease inhibitor which exhibits anti-trypsin activity (PubMed:7142173). In the pancreas, protects against trypsin-catalyzed premature activation of zymogens (By similarity). {ECO:0000250|UniProtKB:P09036, ECO:0000269|PubMed:7142173}.; DISEASE: Pancreatitis, hereditary (PCTT) [MIM:167800]: A disease characterized by pancreas inflammation, permanent destruction of the pancreatic parenchyma, maldigestion, and severe abdominal pain attacks. {ECO:0000269|PubMed:10691414, ECO:0000269|PubMed:10835640, ECO:0000269|PubMed:12974284}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Tropical calcific pancreatitis (TCP) [MIM:608189]: Idiopathic, juvenile, nonalcoholic form of chronic pancreatitis widely prevalent in several tropical countries. It can be associated with fibrocalculous pancreatic diabetes (FCPD) depending on both environmental and genetic factors. TCP differs from alcoholic pancreatitis by a much younger age of onset, pancreatic calcification, a high incidence of insulin dependent but ketosis resistant diabetes mellitus, and an exceptionally high incidence of pancreatic cancer. {ECO:0000269|PubMed:12011155, ECO:0000269|PubMed:12187509}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . breast;pancreas;endometrium;islets of Langerhans;liver;colon;kidney;stomach; fetal liver;pancreas;beta cell islets; 0.38435 0.17944 0.813985927 87.81552253 342.52799 3.92490 SPINK2 0.717781972812012 0.268219616019249 0.0139984111687382 serine peptidase inhibitor, Kazal type 2 FUNCTION: Strong inhibitor of acrosin in male and/or female genital tract. Also inhibits trypsin. {ECO:0000269|PubMed:19422058}.; . TISSUE SPECIFICITY: Expressed in epididymis (at protein level). {ECO:0000269|PubMed:20736409}.; unclassifiable (Anatomical System);uterus;medulla oblongata;prostate;lung;heart;islets of Langerhans;epididymis;hippocampus;testis;brain;skin; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.13334 . 0.013025609 54.62962963 1852.51989 7.93428 SPINK4 0.713655355930809 0.271770383088373 0.0145742609808181 serine peptidase inhibitor, Kazal type 4 . . . . . 0.10726 . 0.613741468 83.06794055 6.35672 0.23801 SPINK5 2.116589476282e-17 0.920781310698357 0.0792186893016434 serine peptidase inhibitor, Kazal type 5 FUNCTION: Serine protease inhibitor, probably important for the anti-inflammatory and/or antimicrobial protection of mucous epithelia. Contribute to the integrity and protective barrier function of the skin by regulating the activity of defense- activating and desquamation-involved proteases. Inhibits KLK5, it's major target, in a pH-dependent manner. Inhibits KLK7, KLK14 CASP14, and trypsin. {ECO:0000269|PubMed:10419450, ECO:0000269|PubMed:17596512, ECO:0000269|PubMed:20533828}.; DISEASE: Netherton syndrome (NETH) [MIM:256500]: An autosomal recessive congenital ichthyosis associated with hair shaft abnormalities and anomalies of the immune system. Typical features are ichthyosis linearis circumflexa, ichthyosiform erythroderma, trichorrhexis invaginata (bamboo hair), atopic dermatitis, and hayfever. High postnatal mortality is due to failure to thrive, infections and hypernatremic dehydration. {ECO:0000269|PubMed:10835624}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in the thymus and stratum corneum. Also found in the oral mucosa, parathyroid gland, Bartholin's glands, tonsils, and vaginal epithelium. Very low levels are detected in lung, kidney, and prostate. {ECO:0000269|PubMed:10419450}.; unclassifiable (Anatomical System);heart;oral cavity;pharynx;colon;skin;skeletal muscle;lung;oesophagus;epididymis;larynx;thyroid;placenta;hypopharynx;testis;cervix;head and neck;kidney;tonsil;stomach; dorsal root ganglion;superior cervical ganglion;tongue;pons;trigeminal ganglion;skeletal muscle;skin;tonsil; 0.25290 0.29285 2.831581484 99.08586931 18873.47781 29.29597 SPINK6 2.41645569954461e-05 0.169502474800947 0.830473360642057 serine peptidase inhibitor, Kazal type 6 FUNCTION: Serine protease inhibitor selective for kallikreins. Efficiently inhibits KLK4, KLK5, KLK6, KLK7, KLK12, KLK13 and KLK14. Doesn't inhibit KLK8. {ECO:0000269|PubMed:20667819, ECO:0000269|PubMed:21439340}.; . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;lung;cornea;visual apparatus;liver;cervix;kidney;brain;mammary gland; . 0.25786 . 0.523736627 80.45529606 17.2966 0.60748 SPINK7 0.0761167144856102 0.748716300927574 0.175166984586816 serine peptidase inhibitor, Kazal type 7 (putative) FUNCTION: Probable serine protease inhibitor.; . . uterus;lung;heart;larynx;thyroid;oral cavity;hypopharynx;testis;head and neck;skin;tonsil; tongue; 0.13393 0.09930 0.21326276 67.71644256 39.91756 1.17439 SPINK8 0.00112128585214279 0.386725681374819 0.612153032773039 serine peptidase inhibitor, Kazal type 8 (putative) FUNCTION: Probable serine protease inhibitor. {ECO:0000250}.; . . . . . . 0.523736627 80.45529606 989.52482 6.06479 SPINK9 0.326828103280709 0.608661475825479 0.0645104208938128 serine peptidase inhibitor, Kazal type 9 FUNCTION: Serine protease inhibitor which specifically inhibits KLK5. May contribute to the regulation of the desquamation process in skin by inhibiting KLK5. {ECO:0000269|PubMed:19190773, ECO:0000269|PubMed:19194479}.; . TISSUE SPECIFICITY: Skin. Highly expressed at sites of hyperkeratosis. Also detected in thymus, tonsils, testis, pancreas, liver, placenta and brain. Expressed at stratum granulosum and stratum corneum at palmar and plantar sites (at protein level). {ECO:0000269|PubMed:19190773, ECO:0000269|PubMed:19194479}.; . . 0.10239 0.09395 0.035072054 56.2514744 513.32791 4.63697 SPINK13 0.0243569531155143 0.776654218302572 0.198988828581914 serine peptidase inhibitor, Kazal type 13 (putative) FUNCTION: May be a serine protease inhibitor (By similarity). Essential for sperm maturation and fertility. Inhibits sperm acrosome reaction, protecting sperm from premature reaction (By similarity). {ECO:0000250}.; . . . . . . -0.009020804 52.8544468 2.39962 0.08295 SPINK14 0.0163521578795306 0.705051857165835 0.278595984954635 serine peptidase inhibitor, Kazal type 14 (putative) FUNCTION: May be a serine protease inhibitor. {ECO:0000250}.; . . . . . . 0.035072054 56.2514744 5.4089 0.19994 SPINT1 0.00152362991906225 0.967962068470002 0.0305143016109362 serine peptidase inhibitor, Kunitz type 1 FUNCTION: Inhibitor of HGF activator. Also acts as an inhibitor of matriptase (ST14).; . . ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;breast;pancreas;lung;placenta;liver;spleen;kidney;mammary gland;stomach;peripheral nerve;cerebellum; prostate;lung;trachea;placenta; 0.16296 0.16871 0.271907863 70.73012503 659.79835 5.14914 SPINT2 0.0296186146049727 0.923963468899894 0.046417916495133 serine peptidase inhibitor, Kunitz type, 2 FUNCTION: Inhibitor of HGF activator. Also inhibits plasmin, plasma and tissue kallikrein, and factor XIa.; DISEASE: Diarrhea 3, secretory sodium, congenital, with or without other congenital anomalies (DIAR3) [MIM:270420]: A disease characterized by life-threatening secretory diarrhea, severe metabolic acidosis and hyponatremia. Hyponatremia is secondary to extraordinarily high fecal sodium loss, with low or normal excretion of urinary sodium, in the absence of infectious, autoimmune and endocrine causes. {ECO:0000269|PubMed:19185281}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in placenta, kidney, pancreas, prostate, testis, thymus, and trachea.; medulla oblongata;ovary;colon;choroid;skin;uterus;prostate;frontal lobe;cerebral cortex;endometrium;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;urinary;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; lung;thyroid;testis;pituitary; 0.10021 0.33518 0.439181676 77.69521113 119.86452 2.38438 SPINT3 . . . serine peptidase inhibitor, Kunitz type, 3 . . . lung;testis; superior cervical ganglion;testis;globus pallidus;atrioventricular node;cingulate cortex;skeletal muscle; 0.00030 . 0.657836546 84.27105449 354.97189 3.98451 SPINT4 0.0933895217408077 0.767771596638811 0.138838881620381 serine peptidase inhibitor, Kunitz type 4 . . . lung;testis; . 0.06030 0.07007 0.457594962 78.16112291 9.60913 0.35377 SPINT5P . . . serine peptidase inhibitor, Kunitz type 5, pseudogene . . . . . 0.10745 . . . . . SPIRE1 0.330091752046804 0.669881003748652 2.72442045441403e-05 spire type actin nucleation factor 1 FUNCTION: Acts as a actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for asymmetric spindle positioning and asymmetric cell division during meiosis. Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis. {ECO:0000269|PubMed:11747823, ECO:0000269|PubMed:21620703}.; . . ovary;parotid gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;cochlea;larynx;bone;thyroid;testis;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; . 0.13285 0.09444 -1.111360919 6.717386176 74.25913 1.79961 SPIRE2 1.1281776245309e-10 0.298701396030623 0.70129860385656 spire type actin nucleation factor 2 FUNCTION: Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for asymmetric spindle positioning and asymmetric cell division during meiosis. Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis. {ECO:0000269|PubMed:21620703}.; . . . . 0.14304 0.10468 -0.705410796 14.77942911 801.33794 5.57726 SPN 0.0912713919603563 0.766031164043822 0.142697443995822 sialophorin FUNCTION: One of the major glycoproteins of thymocytes and T lymphocytes. Plays a role in the physicochemical properties of the T-cell surface and in lectin binding. Presents carbohydrate ligands to selectins. Has an extended rodlike structure that could protrude above the glycocalyx of the cell and allow multiple glycan chains to be accessible for binding. Is a counter-receptor for SN/Siglec-1 (By similarity). During T-cell activation is actively removed from the T-cell-APC (antigen-presenting cell) contact site thus suggesting a negative regulatory role in adaptive immune response (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Cell surface of thymocytes, T-lymphocytes, neutrophils, plasma cells and myelomas.; unclassifiable (Anatomical System);lung;bone;liver;testis;spleen;blood;kidney;brain;skin;bone marrow; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.34826 0.49454 -0.26993514 34.59542345 212.87886 3.14974 SPNS1 0.25844682511651 0.740346822690034 0.00120635219345633 spinster homolog 1 (Drosophila) FUNCTION: Sphingolipid transporter (By similarity). May be involved in necrotic or autophagic cell death. {ECO:0000250, ECO:0000269|PubMed:12815463}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; ciliary ganglion; 0.17236 0.30023 -0.578583623 18.71903751 237.99515 3.33143 SPNS2 0.00382444023834242 0.987626954057252 0.00854860570440524 spinster homolog 2 (Drosophila) FUNCTION: Sphingolipid transporter required for migration of myocardial precursors. Transports sphingosine 1-phosphate (S1P), a secreted lipid mediator that plays critical roles in cardiovascular, immunological, and neural development and function. Mediates the export of S1P from cells in the extraembryonic yolk syncytial layer (YSL), thereby regulating myocardial precursor migration. {ECO:0000269|PubMed:19074308}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;hippocampus;visual apparatus;kidney;mammary gland;stomach; whole brain;amygdala;cerebellum; 0.36420 0.11006 -0.975433863 8.852323661 122.59975 2.41138 SPNS3 2.77218256786725e-10 0.148025954688967 0.851974045033815 spinster homolog 3 (Drosophila) FUNCTION: Sphingolipid transporter. {ECO:0000250}.; . . unclassifiable (Anatomical System);colon;blood;fovea centralis;choroid;lens;bone marrow;retina;pancreas;optic nerve;lung;macula lutea;liver;spleen;kidney;stomach; . 0.11306 0.08749 -0.146971018 42.31540458 910.68475 5.86831 SPO11 0.000356300036119442 0.951892470475737 0.0477512294881441 SPO11 meiotic protein covalently bound to DSB FUNCTION: Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (By similarity). Essential for the phosphorylation of SMC3, HORMAD1 and HORMAD2 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in testis.; unclassifiable (Anatomical System);medulla oblongata;lung;testis; dorsal root ganglion;superior cervical ganglion;uterus corpus;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.28308 0.16446 0.461228372 78.46190139 55.96155 1.50220 SPOCD1 8.79900241092214e-06 0.996313164194181 0.00367803680340776 SPOC domain containing 1 . . . unclassifiable (Anatomical System);cartilage;islets of Langerhans;salivary gland;pineal body;colon;choroid;skin;retina;uterus;breast;lung;placenta;bone;visual apparatus;pineal gland;brain; dorsal root ganglion;superior cervical ganglion;smooth muscle;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.06122 . 1.451368496 95.15215853 3132.21342 10.66015 SPOCK1 0.320886444579516 0.678398903152666 0.000714652267818124 sparc/osteonectin, cwcv and kazal-like domains proteoglycan (testican) 1 FUNCTION: May play a role in cell-cell and cell-matrix interactions. May contribute to various neuronal mechanisms in the central nervous system.; . . smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;brain;amygdala;heart;cartilage;tongue;pineal body;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;atrium;larynx;synovium;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);hypothalamus;pancreas;lung;mesenchyma;adrenal gland;placenta;hippocampus;head and neck;kidney;aorta;cerebellum; thalamus;medulla oblongata;occipital lobe;adipose tissue;cerebellum peduncles;hypothalamus;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.28758 0.20627 -0.490397599 22.50530786 83.60687 1.94449 SPOCK2 0.881279639448395 0.118661803700181 5.85568514235306e-05 sparc/osteonectin, cwcv and kazal-like domains proteoglycan (testican) 2 FUNCTION: May participate in diverse steps of neurogenesis. Binds calcium.; . TISSUE SPECIFICITY: Highly expressed in brain. Also found in lung and testis. {ECO:0000269|PubMed:10386950}.; smooth muscle;ovary;sympathetic chain;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;cochlea;oesophagus;endometrium;synovium;thyroid;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;hypothalamus;spinal cord;muscle;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;head and neck;kidney;stomach;cerebellum;thymus; amygdala;medulla oblongata;superior cervical ganglion;thalamus;cerebellum peduncles;prefrontal cortex;pons;atrioventricular node;parietal lobe;cingulate cortex;cerebellum; 0.29419 0.15179 -0.732911333 14.07761264 133.77579 2.51474 SPOCK3 0.495144483703879 0.504669023999446 0.000186492296675468 sparc/osteonectin, cwcv and kazal-like domains proteoglycan (testican) 3 FUNCTION: May participate in diverse steps of neurogenesis. Inhibits the processing of pro-matrix metalloproteinase 2 (MMP-2) by MT1-MMP and MT3-MMP. May interfere with tumor invasion.; . TISSUE SPECIFICITY: Expressed in brain.; amygdala;unclassifiable (Anatomical System);ovary;islets of Langerhans;hypothalamus;parathyroid;skeletal muscle;prostate;whole body;lung;thyroid;placenta;hippocampus;head and neck;brain; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.12678 0.11885 0.042348793 57.31304553 237.48342 3.32713 SPON1 . . . spondin 1 FUNCTION: Cell adhesion protein that promotes the attachment of spinal cord and sensory neuron cells and the outgrowth of neurites in vitro. May contribute to the growth and guidance of axons in both the spinal cord and the PNS (By similarity). Major factor for vascular smooth muscle cell. {ECO:0000250}.; . TISSUE SPECIFICITY: Highest expression in lung, lower expression in brain, heart, kidney, liver and testis, and lowest expression in pancreas, skeletal muscle and ovary. Not expressed in spleen. {ECO:0000269|PubMed:11368520, ECO:0000269|PubMed:9872452}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;hypothalamus;pineal body;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.67051 0.23513 . . . . SPON2 1.0881191748191e-06 0.192766080424288 0.807232831456538 spondin 2 FUNCTION: Cell adhesion protein that promotes adhesion and outgrowth of hippocampal embryonic neurons. Binds directly to bacteria and their components and functions as an opsonin for macrophage phagocytosis of bacteria. Essential in the initiation of the innate immune response and represents a unique pattern- recognition molecule in the ECM for microbial pathogens (By similarity). Binds bacterial lipopolysaccharide (LPS). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in normal lung tissue but not in lung carcinoma cell lines. {ECO:0000269|PubMed:10512675}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;oesophagus;endometrium;larynx;bone;thyroid;iris;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; uterus corpus; 0.18408 . -0.023789244 52.09365416 780.81347 5.52702 SPOP 0.992531222874917 0.00746734665153132 1.43047355174006e-06 speckle type BTB/POZ protein FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. In complex with CUL3, involved in ubiquitination and proteasomal degradation of BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. In complex with CUL3, involved in ubiquitination of H2AFY and BMI1; this does not lead to their proteasomal degradation. Inhibits transcriptional activation of PDX1/IPF1 targets, such as insulin, by promoting PDX1/IPF1 degradation. The cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOP has higher ubiquitin ligase activity than the complex that contains the heterodimer formed by SPOP and SPOPL. {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16524876, ECO:0000269|PubMed:19818708, ECO:0000269|PubMed:22085717, ECO:0000269|PubMed:22632832}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9414087}.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;germinal center;bladder;brain;heart;pineal body;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;atrium;cerebral cortex;larynx;synovium;bone;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;cerebellum; amygdala;superior cervical ganglion;prefrontal cortex;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.21933 0.18619 -0.185391282 39.67916962 25.23464 0.82534 SPOPL 0.0454469525997792 0.953443577833911 0.0011094695663096 speckle type BTB/POZ protein like FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, but with relatively low efficiency. Cullin-RING-based BCR (BTB-CUL3- RBX1) E3 ubiquitin-protein ligase complexes containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL are less efficient than ubiquitin ligase complexes containing only SPOP. May function to down-regulate the activity of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that contain SPOP. {ECO:0000269|PubMed:22632832}.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach; ciliary ganglion;trigeminal ganglion; 0.32484 0.11621 -0.0274281 51.65723048 55.42268 1.49467 SPP1 1.51211983311729e-06 0.229586582483052 0.770411905397115 secreted phosphoprotein 1 FUNCTION: Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction.; . TISSUE SPECIFICITY: Bone. Found in plasma.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;iris;amniotic fluid;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;nervous;spinal cord;urinary;pharynx;blood;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;aorta;stomach; amygdala;dorsal root ganglion;occipital lobe;medulla oblongata;thalamus;olfactory bulb;hypothalamus;temporal lobe;beta cell islets;spinal cord;pons;caudate nucleus;subthalamic nucleus;fetal brain;placenta;prefrontal cortex;globus pallidus;kidney;trigeminal ganglion;parietal lobe;cingulate cortex; 0.57394 0.85579 -0.045835247 50.34206181 465.03744 4.46661 SPP2 1.27136183221359e-06 0.209480424781114 0.790518303857054 secreted phosphoprotein 2 FUNCTION: Could coordinate an aspect of bone turnover. {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in liver and plasma. {ECO:0000269|PubMed:15062857}.; lung;liver;testis;spleen;skeletal muscle; fetal liver;superior cervical ganglion;liver;trigeminal ganglion; 0.03583 . -0.315847836 31.68789809 76.32806 1.83165 SPPL2A 0.0470779338673946 0.951871596520984 0.00105046961162138 signal peptide peptidase like 2A FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in FASLG, ITM2B and TNF processing (PubMed:16829952, PubMed:16829951, PubMed:17557115, PubMed:17965014). Catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha (TNF), which promotes the release of the intracellular domain (ICD) for signaling to the nucleus (PubMed:16829952). Also responsible for the intramembrane cleavage of Fas antigen ligand FASLG, which promotes the release of the intracellular FasL domain (FasL ICD) (PubMed:17557115). May play a role in the regulation of innate and adaptive immunity (PubMed:16829952). Catalyzes the intramembrane cleavage of the simian foamy virus envelope glycoprotein gp130 independently of prior ectodomain shedding by furin or furin-like proprotein convertase (PC)-mediated cleavage proteolysis (PubMed:23132852). {ECO:0000269|PubMed:16829951, ECO:0000269|PubMed:16829952, ECO:0000269|PubMed:17557115, ECO:0000269|PubMed:17965014, ECO:0000269|PubMed:23132852}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15385547}.; . . 0.51232 0.11809 0.973768544 90.33970276 357.71127 4.00792 SPPL2B . . . signal peptide peptidase like 2B FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in ITM2B and TNF processing (PubMed:16829952, PubMed:16829951, PubMed:17965014, PubMed:19114711, PubMed:22194595). Catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha (TNF), which promotes the release of the intracellular domain (ICD) for signaling to the nucleus (PubMed:16829952, PubMed:16829951). May play a role in the regulation of innate and adaptive immunity (PubMed:16829952). Catalyzes the intramembrane cleavage of the simian foamy virus processed leader peptide gp18 of the envelope glycoprotein gp130 dependently of prior ectodomain shedding by furin or furin-like proprotein convertase (PC)-mediated cleavage proteolysis (PubMed:23132852). {ECO:0000269|PubMed:16829951, ECO:0000269|PubMed:16829952, ECO:0000269|PubMed:17965014, ECO:0000269|PubMed:19114711, ECO:0000269|PubMed:22194595, ECO:0000269|PubMed:23132852}.; . TISSUE SPECIFICITY: Expressed predominantly in adrenal cortex and mammary gland. {ECO:0000269|PubMed:15385547}.; . . 0.13874 0.12165 -0.135838822 43.77211607 . . SPPL2C 2.29524703916312e-05 0.496992828952877 0.502984218576731 signal peptide peptidase like 2C FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that may be able to cleave type II membrane signal peptides in the hydrophobic plane of the membrane. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15385547}.; . . . . 2.188246048 98.09506959 1546.24838 7.29270 SPPL3 0.907785634336426 0.0920649010073579 0.00014946465621563 signal peptide peptidase like 3 FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane protein substrates in or close to their luminal transmembrane domain boundaries (PubMed:16873890, PubMed:25354954, PubMed:25827571). Acts like a sheddase by mediating the proteolytic release and secretion of active site- containing ectodomains of glycan-modifiying glycosidase and glycosyltransferase enzymes such as MGAT5, B4GAT1 and B4GALT1 (PubMed:25354954, PubMed:25827571). Catalyzes the intramembrane cleavage of the envelope glycoprotein gp130 and/or the leader peptide gp18LP of the simian foamy virus independent of prior ectodomain shedding by furin or furin-like proprotein convertase (PC)-mediated cleavage proteolysis (PubMed:23132852). May also have the ability to serve as a shedding protease for subsequent intramembrane proteolysis by SPPL2A and SPPL2B of the envelope glycoprotein gp130 (PubMed:23132852). Plays a role in the regulation of cellular glycosylation processes (PubMed:25354954). Required to link T-cell antigen receptor (TCR) and calcineurin- NFAT signaling cascades in lymphocytes by promoting the association of STIM1 and ORAI1 during store-operated calcium entry (SOCE) in a protease-independent manner (PubMed:25384971). {ECO:0000269|PubMed:16873890, ECO:0000269|PubMed:23132852, ECO:0000269|PubMed:25354954, ECO:0000269|PubMed:25384971, ECO:0000269|PubMed:25827571}.; . TISSUE SPECIFICITY: Widely expressed (PubMed:15385547). Expressed in the brain (PubMed:11978763). {ECO:0000269|PubMed:11978763, ECO:0000269|PubMed:15385547}.; . . . . -0.207437529 38.2814343 4.03778 0.14840 SPR 0.000439257239321401 0.419526980010425 0.580033762750254 sepiapterin reductase (7,8-dihydrobiopterin:NADP+ oxidoreductase) FUNCTION: Catalyzes the final one or two reductions in tetra- hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin.; DISEASE: Dystonia, DOPA-responsive, due to sepiapterin reductase deficiency (DRDSPRD) [MIM:612716]: A form of DOPA-responsive dystonia. In the majority of cases, patients manifest progressive psychomotor retardation, dystonia and spasticity. Cognitive anomalies are also often present. The disease is due to severe dopamine and serotonin deficiencies in the central nervous system caused by a defect in BH4 synthesis. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. {ECO:0000269|PubMed:11443547, ECO:0000269|PubMed:16650784, ECO:0000269|PubMed:17159114}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;iris;testis;brain;bladder;gall bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pineal body;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach; liver;kidney; 0.15098 0.22813 . . 10.57923 0.38423 SPRED1 0.868668326243136 0.13131619089329 1.54828635741044e-05 sprouty related, EVH1 domain containing 1 FUNCTION: Tyrosine kinase substrate that inhibits growth-factor- mediated activation of MAP kinase. Negatively regulates hematopoiesis of bone marrow (By similarity). {ECO:0000250}.; DISEASE: Neurofibromatosis 1-like syndrome (NFLS) [MIM:611431]: A disorder characterized mainly by cafe au lait macules without neurofibromas or other tumor manifestations of neurofibromatosis type 1, axillary freckling, and macrocephaly. Additional clinical manifestations include Noonan-like facial dysmorphism, lipomas, learning disabilities and attention deficit-hyperactivity. {ECO:0000269|PubMed:17704776, ECO:0000269|PubMed:19443465, ECO:0000269|PubMed:20108422, ECO:0000269|PubMed:21089071}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Weakly expressed in embryonic cell line HEK293. {ECO:0000269|PubMed:15580519}.; ovary;colon;parathyroid;skin;uterus;prostate;cochlea;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;pineal body;spinal cord;blood;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; globus pallidus;ciliary ganglion;atrioventricular node; 0.44902 0.09206 -0.426079032 25.36565228 47.14387 1.32902 SPRED2 0.000973022757208799 0.944326735656417 0.0547002415863742 sprouty related, EVH1 domain containing 2 FUNCTION: Tyrosine kinase substrate that inhibits growth-factor- mediated activation of MAP kinase.; . TISSUE SPECIFICITY: Expressed in liver, skin, small intestine, salivary gland and prostate. {ECO:0000269|PubMed:15580519}.; ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;cerebellum; thalamus;superior cervical ganglion;subthalamic nucleus;temporal lobe;pons;skeletal muscle;cerebellum; 0.51319 0.12971 -0.688817379 15.20405756 62.5689 1.61731 SPRED3 0.422884638271983 0.569448787053483 0.00766657467453338 sprouty related, EVH1 domain containing 3 FUNCTION: Tyrosine kinase substrate that inhibits growth-factor- mediated activation of MAP kinase. {ECO:0000250}.; . TISSUE SPECIFICITY: Expression is restricted to liver. {ECO:0000269|PubMed:16478641}.; unclassifiable (Anatomical System);islets of Langerhans;blood; . 0.18350 0.08136 . . 150.51303 2.67825 SPRN 0.386597169234573 0.475861779408437 0.13754105135699 shadow of prion protein homolog (zebrafish) FUNCTION: Prion-like protein that has PrP(C)-like neuroprotective activity. May act as a modulator for the biological actions of normal and abnormal PrP (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Mainly expressed in brain. In brain, it is expressed in hippocampus. {ECO:0000269|PubMed:14527721}.; . . 0.05033 . . . 2720.44428 9.82760 SPRNP1 . . . shadow of prion protein homolog (zebrafish) pseudogene 1 . . . . . . . . . . . SPRR1A 0.175108853992108 0.64374253883974 0.181148607168152 small proline rich protein 1A FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane.; . . unclassifiable (Anatomical System);lung;tongue;larynx;nasopharynx;oral cavity;hypopharynx;amniotic fluid;head and neck;skeletal muscle;stomach; superior cervical ganglion;trachea;tongue;atrioventricular node;trigeminal ganglion;tonsil;skin; 0.09150 0.13645 0.235309407 68.71903751 9.73038 0.35690 SPRR1B 0.17260904615434 0.642989857648025 0.184401096197635 small proline rich protein 1B FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane. Can function as both amine donor and acceptor in transglutaminase-mediated cross- linkage.; . TISSUE SPECIFICITY: Suprabasal layers of squamous-differentiated tissues such as epidermis, esophagus, tongue and trachea.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;larynx;thyroid;bladder;brain;unclassifiable (Anatomical System);heart;oral cavity;pharynx;blood;lens;breast;pancreas;lung;macula lutea;visual apparatus;hypopharynx;liver;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;tongue;appendix;pons;atrioventricular node;trigeminal ganglion;skin;tonsil; 0.08205 0.12774 0.103030231 61.2762444 275.51706 3.55565 SPRR2A 0.160255855292028 0.638255509049822 0.20148863565815 small proline rich protein 2A FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane.; . . . . 0.05961 . 0.323496558 72.93583392 0.00011 0.00022 SPRR2B 0.15744268643288 0.636926268015642 0.205631045551478 small proline rich protein 2B FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane.; . TISSUE SPECIFICITY: Suprabasal layers of squamous-differentiated tissues such as epidermis, esophagus, tongue and trachea.; unclassifiable (Anatomical System);lung;hypopharynx;colon;head and neck; . 0.05601 0.05873 0.057118534 57.99716914 17.90316 0.62565 SPRR2C . . . small proline rich protein 2C (pseudogene) . . . unclassifiable (Anatomical System);uterus;heart;oral cavity;hypopharynx;testis;head and neck;skin; . . . . . . . SPRR2D 0.00368097397742855 0.400073998172447 0.596245027850124 small proline rich protein 2D FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane.; . . unclassifiable (Anatomical System);lung;frontal lobe;thyroid;hypopharynx;colon;cervix;head and neck; . 0.09647 . 0.191216164 66.57230479 20.91726 0.70798 SPRR2E 0.15458733678847 0.635475544416098 0.209937118795432 small proline rich protein 2E FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane.; . . . . 0.08793 . 0.235309407 68.71903751 6.61015 0.24505 SPRR2F 0.00362203147645598 0.397109083220805 0.599268885302739 small proline rich protein 2F FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane (By similarity). {ECO:0000250}.; . . . . 0.10142 . 0.902179145 89.34890304 904.7474 5.85461 SPRR2G 0.0266080186616705 0.568421844848248 0.404970136490082 small proline rich protein 2G FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane (By similarity). {ECO:0000250}.; . . . . . . 0.501689326 79.7888653 19.0031 0.65628 SPRR3 0.00604296707083471 0.497171823128786 0.496785209800379 small proline rich protein 3 FUNCTION: Cross-linked envelope protein of keratinocytes.; . . ovary;oral cavity;parathyroid;skeletal muscle;pancreas;prostate;oesophagus;adrenal gland;larynx;placenta;thyroid;hypopharynx;head and neck;tonsil; trachea;tongue;thyroid;placenta;skeletal muscle;tonsil; 0.02059 0.06600 0.461228372 78.46190139 973.12859 6.03172 SPRR4 0.582181678693793 0.375036466509624 0.0427818547965834 small proline rich protein 4 FUNCTION: Cross-linked envelope protein of keratinocytes. Involved in UV-induced cornification.; . . unclassifiable (Anatomical System);uterus;prostate;lung;heart;hypopharynx;testis;colon;head and neck;skin; . 0.11466 0.05263 0.369407109 74.95281906 771.02285 5.49621 SPRTN 0.981335747291668 0.0186615138459517 2.7388623801707e-06 SprT-like N-terminal domain FUNCTION: Regulator of UV-induced DNA damage response: acts as a 'reader' of ubiquitinated PCNA that enhances RAD18-mediated PCNA ubiquitination and translesion DNA synthesis (TLS). Recruited to sites of UV damage and interacts with ubiquitinated PCNA and RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA. Facilitates chromatin association of RAD18 and is required for efficient PCNA monoubiquitination, promoting a feed-forward loop to enhance PCNA ubiquitination and translesion DNA synthesis. Acts as a regulator of TLS by recruiting VCP/p97 to sites of DNA damage, possibly leading to extraction of DNA polymerase eta (POLH) by VCP/p97 to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage. {ECO:0000269|PubMed:22681887, ECO:0000269|PubMed:22894931, ECO:0000269|PubMed:22902628, ECO:0000269|PubMed:22987070, ECO:0000269|PubMed:23042605, ECO:0000269|PubMed:23042607}.; DISEASE: Ruijs-Aalfs syndrome (RJALS) [MIM:616200]: A syndrome characterized by genomic instability, progeroid features, and susceptibility toward early onset hepatocellular carcinoma. {ECO:0000269|PubMed:25261934}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.24791 0.09675 -0.578583623 18.71903751 80.17567 1.89268 SPRY1 4.1272720246655e-05 0.225787525797748 0.774171201482005 sprouty RTK signaling antagonist 1 FUNCTION: May function as an antagonist of fibroblast growth factor (FGF) pathways and may negatively modulate respiratory organogenesis.; . . lymphoreticular;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.95069 0.17470 -0.159704656 41.90846898 32.70592 1.01694 SPRY2 0.930516838339553 0.0691284163659146 0.000354745294532607 sprouty RTK signaling antagonist 2 FUNCTION: May function as an antagonist of fibroblast growth factor (FGF) pathways and may negatively modulate respiratory organogenesis. {ECO:0000269|PubMed:10887178}.; . . . . 0.72242 . 0.082802743 60.09082331 1456.24463 7.11655 SPRY3 0.00584474683683058 0.727560280096897 0.266594973066272 sprouty RTK signaling antagonist 3 FUNCTION: May function as an antagonist of fibroblast growth factor (FGF) pathways and may negatively modulate respiratory organogenesis.; . TISSUE SPECIFICITY: Widely expressed; particularly in the fetal tissues.; unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;colon;fovea centralis;choroid;lens;retina;bone marrow;prostate;optic nerve;whole body;lung;placenta;macula lutea;visual apparatus;liver;testis;spleen;brain; dorsal root ganglion;trigeminal ganglion; 0.65223 0.11480 -0.271755481 34.31823543 45.77084 1.30046 SPRY4 0.109919685601811 0.776973194700711 0.113107119697478 sprouty RTK signaling antagonist 4 FUNCTION: Suppresses the insulin receptor and EGFR-transduced MAPK signaling pathway, but does not inhibit MAPK activation by a constitutively active mutant Ras. Probably impairs the formation of GTP-Ras. Inhibits Ras-independent, but not Ras-dependent, activation of RAF1. {ECO:0000269|PubMed:12717443}.; DISEASE: Hypogonadotropic hypogonadism 17 with or without anosmia (HH17) [MIM:615266]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:23643382}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. Some patients carrying mutations in SPRY4 also have a heterozygous mutation in another HH-associated gene including DUSP6 and FGFR1 (PubMed:23643382). {ECO:0000269|PubMed:23643382}.; . ovary;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;larynx;thyroid;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;thymus; superior cervical ganglion;pons;skeletal muscle; 0.93024 0.14190 -0.045835247 50.34206181 112.70425 2.30891 SPRY4-IT1 . . . SPRY4 intronic transcript 1 . . . . . . . . . . . SPRYD3 0.94694247848355 0.0530500889390511 7.43257739940166e-06 SPRY domain containing 3 . . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;lens;skeletal muscle;breast;lung;epididymis;mesenchyma;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;cervix;kidney;mammary gland;stomach;cerebellum; . 0.18460 0.08682 -0.516085732 21.20193442 504.67568 4.61121 SPRYD4 0.000589211754630036 0.477618170130178 0.521792618115192 SPRY domain containing 4 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach; . 0.09453 0.07212 0.25917371 70.05779665 28.20795 0.90419 SPRYD7 0.0911571663926814 0.869463288119077 0.039379545488242 SPRY domain containing 7 . . . medulla oblongata;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;atrium;thyroid;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;amnion;spleen;head and neck;kidney;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14022 0.10246 -0.119252484 44.53880632 1.07339 0.02740 SPSB1 0.709596082305861 0.287008098333095 0.00339581936104326 splA/ryanodine receptor domain and SOCS box containing 1 FUNCTION: Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000269|PubMed:15601820}.; . . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex; 0.50680 0.14775 -0.161524709 41.6430762 14.80542 0.53303 SPSB2 0.125059417279287 0.780052945750179 0.0948876369705336 splA/ryanodine receptor domain and SOCS box containing 2 FUNCTION: Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000269|PubMed:15601820}.; . . . . 0.07966 . -0.161524709 41.6430762 1567.55258 7.32736 SPSB3 0.514185341856129 0.481957766997989 0.00385689114588212 splA/ryanodine receptor domain and SOCS box containing 3 FUNCTION: May be a substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}.; . . ovary;developmental;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;oesophagus;larynx;gum;bone;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;blood;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; superior cervical ganglion;cerebellum peduncles;liver;adrenal cortex;skeletal muscle;cerebellum; 0.09503 0.12253 -0.44448505 24.46331682 51.15853 1.40936 SPSB4 0.0052286394184106 0.705021405709728 0.289749954871862 splA/ryanodine receptor domain and SOCS box containing 4 FUNCTION: Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000269|PubMed:15601820}.; . . unclassifiable (Anatomical System);medulla oblongata;heart;muscle;fovea centralis;choroid;lens;retina;optic nerve;lung;placenta;macula lutea;testis;kidney;brain; testis;ciliary ganglion;atrioventricular node; 0.78027 0.14044 . . 62.08815 1.60605 SPTA1 5.85298929647153e-05 0.999941470107035 3.90307294466646e-16 spectrin alpha, erythrocytic 1 FUNCTION: Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.; DISEASE: Elliptocytosis 2 (EL2) [MIM:130600]: A Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape. {ECO:0000269|PubMed:1541680, ECO:0000269|PubMed:1638030, ECO:0000269|PubMed:1679439, ECO:0000269|PubMed:1878597, ECO:0000269|PubMed:2384601, ECO:0000269|PubMed:2568861, ECO:0000269|PubMed:2568862, ECO:0000269|PubMed:2794061, ECO:0000269|PubMed:7772539, ECO:0000269|PubMed:8018926, ECO:0000269|PubMed:8193371, ECO:0000269|PubMed:8364215}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hereditary pyropoikilocytosis (HPP) [MIM:266140]: Autosomal recessive hematologic disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells. {ECO:0000269|PubMed:1878597}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spherocytosis 3 (SPH3) [MIM:270970]: Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH3 is characterized by severe hemolytic anemia. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.20565 0.08686 4.849637631 99.79358339 7837.04606 19.05718 SPTAN1 0.999999999999786 2.14126644281593e-13 1.00356698801876e-35 spectrin alpha, non-erythrocytic 1 FUNCTION: Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane.; DISEASE: Epileptic encephalopathy, early infantile, 5 (EIEE5) [MIM:613477]: A disorder characterized by seizures associated with hypsarrhythmia, profound mental retardation with lack of visual attention and speech development, as well as spastic quadriplegia. {ECO:0000269|PubMed:20493457}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;fovea centralis;choroid;uterus;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;amnion;head and neck;kidney;stomach;thymus;cerebellum; whole brain;amygdala;dorsal root ganglion;occipital lobe;superior cervical ganglion;thalamus;medulla oblongata;cerebellum peduncles;temporal lobe;spinal cord;pons;atrioventricular node;caudate nucleus;skin;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.60251 0.39112 -3.530899533 0.31257372 104.65947 2.21139 SPTB 0.999999747900015 2.52099984509224e-07 2.52004219585292e-22 spectrin beta, erythrocytic FUNCTION: Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.; DISEASE: Elliptocytosis 3 (EL3) [MIM:182870]: A Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape. {ECO:0000269|PubMed:1975598, ECO:0000269|PubMed:7883966, ECO:0000269|PubMed:8018926, ECO:0000269|PubMed:8226774}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spherocytosis 2 (SPH2) [MIM:616649]: An autosomal dominant form of hereditary spherocytosis, a group of hematologic disorders characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Clinical manifestations include chronic hemolytic anemia, jaundice, and splenomegaly, with variable severity. {ECO:0000269|PubMed:19538529, ECO:0000269|PubMed:8102379}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;frontal lobe;thyroid;bone;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;muscle;lens;skeletal muscle;lung;macula lutea;liver;head and neck;spleen;peripheral nerve;cerebellum; subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;globus pallidus;atrioventricular node;caudate nucleus;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.31324 0.33019 -2.640400656 0.778485492 7634.17972 18.78025 SPTBN1 0.999999999947367 5.26329239518471e-11 1.63088774721902e-28 spectrin beta, non-erythrocytic 1 FUNCTION: Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane.; . TISSUE SPECIFICITY: Isoform 2 is present in brain, lung and kidney (at protein level). {ECO:0000269|PubMed:11665863}.; ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;whole body;frontal lobe;oesophagus;larynx;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;muscle;blood;lens;breast;lung;epididymis;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland; dorsal root ganglion;whole brain;occipital lobe;subthalamic nucleus;superior cervical ganglion;olfactory bulb;prefrontal cortex;globus pallidus;pons;cingulate cortex;skeletal muscle;parietal lobe; 0.27109 0.37140 -3.862151662 0.22410946 285.65309 3.61906 SPTBN2 0.999977956591075 2.2043408924764e-05 1.8781227856014e-22 spectrin beta, non-erythrocytic 2 FUNCTION: Probably plays an important role in neuronal membrane skeleton.; DISEASE: Spinocerebellar ataxia, autosomal recessive, 14 (SCAR14) [MIM:615386]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR14 is characterized by delayed psychomotor development, severe early onset gait ataxia, eye movement abnormalities, cerebellar atrophy on brain imaging, and intellectual disability. {ECO:0000269|PubMed:23236289, ECO:0000269|PubMed:23838597}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in brain, kidney, pancreas, and liver, and at lower levels in lung and placenta.; medulla oblongata;colon;fovea centralis;choroid;skin;retina;optic nerve;frontal lobe;larynx;thyroid;bone;testis;spinal ganglion;bladder;brain;unclassifiable (Anatomical System);lens;breast;pancreas;lung;macula lutea;hippocampus;visual apparatus;hypopharynx;cervix;head and neck;kidney;mammary gland;stomach;cerebellum; amygdala;medulla oblongata;occipital lobe;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;testis;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.37401 0.20511 -4.229202843 0.141542817 679.70554 5.21283 SPTBN4 . . . spectrin beta, non-erythrocytic 4 . . TISSUE SPECIFICITY: Abundantly expressed in brain and pancreatic islets.; unclassifiable (Anatomical System);optic nerve;lung;islets of Langerhans;testis;brain;skeletal muscle;retina; whole brain;amygdala;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.16131 0.15197 -1.824619408 2.129039868 5101.64368 14.64602 SPTBN5 1.09010380481407e-70 6.32128011484572e-11 0.999999999936787 spectrin beta, non-erythrocytic 5 . . TISSUE SPECIFICITY: Expressed at very low levels in many tissues, with strongest expression in cerebellum, spinal cord, stomach, pituitary gland, liver, pancreas, salivary gland, kidney, bladder, and heart.; unclassifiable (Anatomical System);heart;ovary;cartilage;parathyroid;fovea centralis;skin;retina;uterus;optic nerve;lung;placenta;macula lutea;visual apparatus;spleen;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.16852 0.12091 . . 13728.76893 25.43136 SPTLC1 2.78402793024923e-07 0.914098573132507 0.0859011484646997 serine palmitoyltransferase long chain base subunit 1 FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1- SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference. {ECO:0000269|PubMed:19416851}.; DISEASE: Neuropathy, hereditary sensory and autonomic, 1A (HSAN1A) [MIM:162400]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by prominent sensory abnormalities with a variable degree of motor and autonomic dysfunction. The neurological phenotype is often complicated by severe infections, osteomyelitis, and amputations. HSAN1A is an autosomal dominant axonal form with onset in the second or third decades. Initial symptoms are loss of pain, touch, heat, and cold sensation over the feet, followed by distal muscle wasting and weakness. Loss of pain sensation leads to chronic skin ulcers and distal amputations. {ECO:0000269|PubMed:11242114, ECO:0000269|PubMed:19651702, ECO:0000269|PubMed:21618344, ECO:0000269|PubMed:22302274, ECO:0000269|PubMed:24247255}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=SPTLC1 mutations at Ser-331 are responsible for severe hereditary motor and sensory neuropathy (HMSN) forms, whose core features are severe, diffuse muscle wasting and hypotonia, motor and sensory disturbances, foot ulcers, amputations and/or burns, joint hypermobility, cataracts and considerable growth retardation. {ECO:0000269|PubMed:23454272}.; TISSUE SPECIFICITY: Widely expressed. Not detected in small intestine. {ECO:0000269|PubMed:17023427}.; ovary;skin;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;cartilage;heart;tongue;urinary;adrenal cortex;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;developmental;colon;parathyroid;uterus;whole body;bone;pituitary gland;testis;dura mater;pineal gland;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;mesenchyma;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; superior cervical ganglion;placenta; 0.38002 0.22508 -0.247889024 35.98726115 180.38129 2.91802 SPTLC1P1 . . . serine palmitoyltransferase long chain base subunit 1 pseudogene 1 . . . . . . . . . . . SPTLC1P2 . . . serine palmitoyltransferase long chain base subunit 1 pseudogene 2 . . . . . . . . . . . SPTLC1P3 . . . serine palmitoyltransferase long chain base subunit 1 pseudogene 3 . . . . . . . . . . . SPTLC1P4 . . . serine palmitoyltransferase long chain base subunit 1 pseudogene 4 . . . . . . . . . . . SPTLC1P5 . . . serine palmitoyltransferase long chain base subunit 1 pseudogene 5 . . . . . . . . . . . SPTLC2 0.820593934643991 0.179370153150601 3.59122054081856e-05 serine palmitoyltransferase long chain base subunit 2 FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC2-SPTSSB complex displays a preference for C18-CoA substrate. {ECO:0000269|PubMed:19416851, ECO:0000269|PubMed:20920666}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17023427}.; lymphoreticular;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;spinal cord;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;amnion;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;occipital lobe;globus pallidus;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.26449 0.19960 -0.247889024 35.98726115 69.30897 1.72564 SPTLC3 0.00275524015888074 0.994428188936034 0.0028165709050851 serine palmitoyltransferase long chain base subunit 3 FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, while the SPTLC1-SPTLC3-SPTSSB has the ability to use a broader range of acyl-CoAs without apparent preference. {ECO:0000269|PubMed:19416851}.; . TISSUE SPECIFICITY: Expressed in most tissues, except peripheral blood cells and bone marrow, with highest levels in heart, kidney, liver, uterus and skin. {ECO:0000269|PubMed:17023427}.; . . 0.10462 0.12780 -0.224023033 37.4321774 214.55753 3.15939 SPTSSA 0.571317620217307 0.382551305456184 0.0461310743265085 serine palmitoyltransferase small subunit A FUNCTION: Stimulates the activity of serine palmitoyltransferase (SPT). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2- SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16- CoA as substrates, with a slight preference for C14-CoA. {ECO:0000269|PubMed:19416851}.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;pineal body;muscle;urinary;adrenal cortex;pharynx;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;adrenal gland;trigeminal ganglion; 0.18355 0.11262 -0.053113545 49.38664779 3.98921 0.14748 SPTSSB 0.00589959099120582 0.492235742998694 0.5018646660101 serine palmitoyltransferase small subunit B FUNCTION: Stimulates the activity of serine palmitoyltransferase (SPT). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference, complexes with this subunit showing a clear preference for longer acyl-CoAs. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference. May play a role in signal transduction. {ECO:0000269|PubMed:19416851}.; . TISSUE SPECIFICITY: Expression is seen predominantly in the prostate epithelium with weaker expression in the fibroblasts and endothelial cells. {ECO:0000269|PubMed:15777716}.; . . 0.39827 0.12971 0.013025609 54.62962963 2.84404 0.10086 SPTY2D1 0.99791521426105 0.00208478314128562 2.59766430612541e-09 SPT2 chromatin protein domain containing 1 FUNCTION: Histone chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin (PubMed:26109053). Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription (PubMed:26109053). Binds DNA and histones and promotes nucleosome assembly (in vitro) (PubMed:23378026, PubMed:26109053). Facilitates formation of tetrameric histone complexes containing histone H3 and H4 (PubMed:26109053). Modulates RNA polymerase 1-mediated transcription (By similarity). Binds DNA, with a preference for branched DNA species, such as Y-form DNA and Holliday junction DNA (PubMed:23378026). {ECO:0000250|UniProtKB:E1BUG7, ECO:0000269|PubMed:23378026}.; . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;frontal lobe;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;pharynx;blood;skeletal muscle;bile duct;lung;cornea;trabecular meshwork;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;testis - interstitial;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22034 . 0.354632714 74.58126917 1141.05321 6.44235 SPTY2D1-AS1 . . . SPTY2D1 antisense RNA 1 . . . . . . . . . . . SPX . . . spexin hormone FUNCTION: Plays a role as a central modulator of cardiovascular and renal function and nociception. Plays also a role in energy metabolism and storage. Inhibits adrenocortical cell proliferation with minor stimulation on corticosteroid release (By similarity). {ECO:0000250}.; FUNCTION: Spexin-2: Intracerebroventricular administration of the peptide induces a decrease in heart rate, but no change in arterial pressure, and an increase in urine flow rate. Intraventricular administration of the peptide induces antinociceptive activity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the type I glomic cells within the carotid body (at protein level). Expressed predominantly in pancreas, testis, kidney, brain and placenta. Expressed in submucosal layer of esophagus and stomach fundus. {ECO:0000269|PubMed:17284679, ECO:0000269|PubMed:19132080, ECO:0000269|PubMed:19193193, ECO:0000269|PubMed:23080164}.; . . 0.20219 . 0.057118534 57.99716914 . . SPZ1 0.0015105932431128 0.679639832579542 0.318849574177346 spermatogenic leucine zipper 1 FUNCTION: Transcription factor that binds to the DNA sequence 5'- CANNTG-3'(E box) and the G-box motif. May play an important role in the regulation of cell proliferation and differentiation during spermatogenesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically and strongly expressed in the testis. Expressed in several tumor cell lines. {ECO:0000269|PubMed:12778315, ECO:0000269|PubMed:15899793}.; . . 0.03968 0.07219 1.572740636 95.70653456 259.2199 3.46004 SQLE 0.91297067975512 0.0870031831769412 2.61370679388305e-05 squalene epoxidase FUNCTION: Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; fetal liver;superior cervical ganglion;subthalamic nucleus;testis;tumor; 0.35484 0.32853 -0.089927255 46.99221515 67.14895 1.69502 SQRDL 1.09952685912782e-05 0.807020158593894 0.192968846137514 sulfide quinone reductase-like (yeast) FUNCTION: Catalyzes the oxidation of hydrogen sulfide with the help of a quinone, such as ubiquinone, giving rise to thiosulfate and ultimately to sulfane (molecular sulfur) atoms. Requires an additional electron acceptor; can use sulfite, sulfide or cyanide (in vitro). {ECO:0000269|PubMed:22852582}.; . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; lung;whole blood; 0.18013 0.25346 0.442818085 77.8544468 57.24361 1.52391 SQSTM1 0.00353899119164032 0.953151121299657 0.0433098875087031 sequestosome 1 FUNCTION: Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family. Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures) and links ALIS to the autophagic machinery. Involved in midbody ring degradation. May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin- 1. May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). May be involved in cell differentiation, apoptosis, immune response and regulation of K(+) channels. {ECO:0000250, ECO:0000269|PubMed:10356400, ECO:0000269|PubMed:10747026, ECO:0000269|PubMed:11244088, ECO:0000269|PubMed:12471037, ECO:0000269|PubMed:15340068, ECO:0000269|PubMed:15802564, ECO:0000269|PubMed:15911346, ECO:0000269|PubMed:15953362, ECO:0000269|PubMed:16079148, ECO:0000269|PubMed:16286508, ECO:0000269|PubMed:19931284, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:24128730}.; DISEASE: Paget disease of bone 3 (PDB3) [MIM:167250]: A disorder of bone remodeling characterized by increased bone turnover affecting one or more sites throughout the skeleton, primarily the axial skeleton. Osteoclastic overactivity followed by compensatory osteoblastic activity leads to a structurally disorganized mosaic of bone (woven bone), which is mechanically weaker, larger, less compact, more vascular, and more susceptible to fracture than normal adult lamellar bone. {ECO:0000269|PubMed:11992264, ECO:0000269|PubMed:12374763, ECO:0000269|PubMed:14584883, ECO:0000269|PubMed:15125799, ECO:0000269|PubMed:15146436, ECO:0000269|PubMed:15176995, ECO:0000269|PubMed:15207768}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=In a cell model for Huntington disease (HD), appears to form a shell surrounding aggregates of mutant HTT that may protect cells from apoptosis, possibly by recruiting autophagosomal components to the polyubiquitinated protein aggregates. {ECO:0000269|PubMed:16286508}.; DISEASE: Frontotemporal dementia and/or amyotrophic lateral sclerosis 3 (FTDALS3) [MIM:616437]: A neurodegenerative disorder characterized by frontotemporal dementia and/or amyotrophic lateral sclerosis in affected individuals. There is high intrafamilial variation. Frontotemporal dementia is characterized by frontal and temporal lobe atrophy associated with neuronal loss, gliosis, and dementia. Patients exhibit progressive changes in social, behavioral, and/or language function. Amyotrophic lateral sclerosis is characterized by the death of motor neurons in the brain, brainstem, and spinal cord, resulting in fatal paralysis. Some FTDALS3 patients may also develop Paget disease of bone. {ECO:0000269|PubMed:22084127, ECO:0000269|PubMed:24042580, ECO:0000269|PubMed:24899140, ECO:0000269|PubMed:25114083}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:8650207}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;endometrium;bone;thyroid;pituitary gland;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; placenta;trigeminal ganglion;fetal thyroid;skeletal muscle; 0.84988 0.23697 -0.264476624 34.8844067 157.38368 2.74166 SQSTM1P1 . . . sequestosome 1 pseudogene 1 . . . . . . . . . . . SRA1 5.00127987809857e-06 0.239831209767016 0.760163788953106 steroid receptor RNA activator 1 FUNCTION: Functional RNA which acts as a transcriptional coactivator that selectively enhances steroid receptor-mediated transactivation ligand-independently through a mechanism involving the modulating N-terminal domain (AF-1) of steroid receptors. Also mediates transcriptional coactivation of steroid receptors ligand- dependently through the steroid-binding domain (AF-2). Enhances cellular proliferation and differentiation and promotes apoptosis in vivo. May play a role in tumorigenesis. {ECO:0000269|PubMed:10199399, ECO:0000269|PubMed:12943696, ECO:0000269|PubMed:14517287, ECO:0000269|PubMed:15147866, ECO:0000269|PubMed:15351741}.; . TISSUE SPECIFICITY: Highly expressed in liver and skeletal muscle and to a lesser extent in brain. Also expressed in both normal and tumorigenic breast epithelial cell lines. Significantly up- regulated in human tumors of the breast, ovary, and uterus. {ECO:0000269|PubMed:10199399, ECO:0000269|PubMed:12565891, ECO:0000269|PubMed:14517287}.; lymphoreticular;medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;cervix;spleen;kidney;mammary gland;aorta;stomach;peripheral nerve; . 0.35845 0.08818 0.595326758 82.66100495 6876.60504 17.67578 SRBD1 1.67463053962146e-14 0.518993329337868 0.481006670662115 S1 RNA binding domain 1 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.18810 . 0.077132183 59.19438547 1106.38934 6.35802 SRC 0.988983228456412 0.0110160214515905 7.50091997703347e-07 SRC proto-oncogene, non-receptor tyrosine kinase FUNCTION: Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein- coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin- 43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1. Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation. Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr- 1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of ADRBK1, leading to beta- arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase. Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr- 128'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. Required for podosome formation (By similarity). {ECO:0000250|UniProtKB:P05480, ECO:0000269|PubMed:11389730, ECO:0000269|PubMed:12615910, ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:16186108, ECO:0000269|PubMed:18586953, ECO:0000269|PubMed:19419966, ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:21309750, ECO:0000269|PubMed:21411625, ECO:0000269|PubMed:22710723, ECO:0000269|PubMed:2498394, ECO:0000269|PubMed:3093483, ECO:0000269|PubMed:7853507, ECO:0000269|PubMed:8755529, ECO:0000269|PubMed:8759729}.; DISEASE: Note=SRC kinase activity has been shown to be increased in several tumor tissues and tumor cell lines such as colon carcinoma cells.; TISSUE SPECIFICITY: Expressed ubiquitously. Platelets, neurons and osteoclasts express 5-fold to 200-fold higher levels than most other tissues.; lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;alveolus;spleen;head and neck;kidney;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.99942 0.99524 -0.692458599 14.96815287 6.69293 0.24669 SRCAP 0.999999997075562 2.92443763529201e-09 9.83734710913937e-28 Snf2-related CREBBP activator protein FUNCTION: Catalytic component of the SRCAP complex which mediates the ATP-dependent exchange of histone H2AZ/H2B dimers for nucleosomal H2A/H2B, leading to transcriptional regulation of selected genes by chromatin remodeling. Acts as a coactivator for CREB-mediated transcription, steroid receptor-mediated transcription, and Notch-mediated transcription. {ECO:0000269|PubMed:10347196, ECO:0000269|PubMed:11522779, ECO:0000269|PubMed:14500758, ECO:0000269|PubMed:16024792, ECO:0000269|PubMed:16634648, ECO:0000269|PubMed:17617668}.; DISEASE: Floating-Harbor syndrome (FLHS) [MIM:136140]: A rare genetic disorder characterized by proportionate short stature, delayed bone age, delayed speech development, and typical facial features. The face is triangular with deep-set eyes, long eyelashes, bulbous nose, wide columella, short philtrum, and thin lips. {ECO:0000269|PubMed:22265015}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;amygdala;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;thymus; superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle; 0.40536 0.07711 -4.139116223 0.153338051 438.0956 4.36351 SRCIN1 0.995504290160632 0.00449570641082905 3.42853862445343e-09 SRC kinase signaling inhibitor 1 FUNCTION: Acts as a negative regulator of SRC by activating CSK which inhibits SRC activity and downstream signaling, leading to impaired cell spreading and migration. Regulates dendritic spine morphology. Involved in calcium-dependent exocytosis. May play a role in neurotransmitter release or synapse maintenance. {ECO:0000269|PubMed:14657239, ECO:0000269|PubMed:17525734, ECO:0000269|PubMed:19146815}.; . TISSUE SPECIFICITY: Expressed in some primary breast carcinomas where its presence is significantly associated with increased tumor size. Not detected in normal breast tissue. {ECO:0000269|PubMed:18475297}.; unclassifiable (Anatomical System);lung;islets of Langerhans;pituitary gland;brain; . . . -0.951568548 9.271054494 375.77526 4.08800 SRD5A1 1.81750169865493e-06 0.252700789468975 0.747297393029326 steroid 5 alpha-reductase 1 FUNCTION: Converts testosterone into 5-alpha-dihydrotestosterone and progesterone or corticosterone into their corresponding 5- alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology.; . TISSUE SPECIFICITY: Liver and prostate (at a low level).; lymphoreticular;ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;cervix;kidney;stomach; dorsal root ganglion;whole brain;superior cervical ganglion;occipital lobe;fetal brain;liver;ciliary ganglion;atrioventricular node; 0.05869 . -0.073340031 48.11866006 31.3139 0.98785 SRD5A1P1 . . . steroid 5 alpha-reductase 1 pseudogene 1 . . . . . . . . . . . SRD5A2 . . . steroid 5 alpha-reductase 2 FUNCTION: Converts testosterone (T) into 5-alpha- dihydrotestosterone (DHT) and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology.; DISEASE: Pseudovaginal perineoscrotal hypospadias (PPSH) [MIM:264600]: A form of male pseudohermaphroditism in which 46,XY males show ambiguous genitalia at birth, including perineal hypospadias and a blind perineal pouch, and develop masculinization at puberty. The name of the disorder stems from the finding of a blind-ending perineal opening resembling a vagina and a severely hypospadiac penis with the urethra opening onto the perineum. {ECO:0000269|PubMed:10718838, ECO:0000269|PubMed:10999800, ECO:0000269|PubMed:1522235, ECO:0000269|PubMed:15528927, ECO:0000269|PubMed:15770495, ECO:0000269|PubMed:16098368, ECO:0000269|PubMed:16181229, ECO:0000269|PubMed:7554313, ECO:0000269|PubMed:8626825, ECO:0000269|PubMed:8768837, ECO:0000269|PubMed:9208814, ECO:0000269|PubMed:9745434, ECO:0000269|PubMed:9843052}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in high levels in the prostate and many other androgen-sensitive tissues.; unclassifiable (Anatomical System);prostate;optic nerve;lung;bone;macula lutea;liver;testis;fovea centralis;choroid;kidney;lens;retina; atrioventricular node;skeletal muscle; 0.05035 0.31853 . . . . SRD5A3 0.0407270356125485 0.929462936561076 0.0298100278263755 steroid 5 alpha-reductase 3 FUNCTION: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism. Also able to convert testosterone (T) into 5-alpha-dihydrotestosterone (DHT). {ECO:0000269|PubMed:17986282, ECO:0000269|PubMed:20637498}.; DISEASE: Kahrizi syndrome (KHRZ) [MIM:612713]: An autosomal recessive neurodevelopmental disorder characterized by mental retardation, cataracts, coloboma, kyphosis, and coarse facial features. {ECO:0000269|PubMed:20700148}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Overexpressed in hormone-refractory prostate cancers (HRPC). Almost no or little expression in normal adult organs. {ECO:0000269|PubMed:17986282}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;amnion;spleen;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;skeletal muscle; 0.18750 0.10316 0.193034296 66.82000472 103.65502 2.19921 SRD5A3-AS1 . . . SRD5A3 antisense RNA 1 . . . . . . . . . . . SRD5A3P1 . . . steroid 5 alpha-reductase 3 pseudogene 1 . . . . . . . . . . . SREBF1 0.985657782151979 0.014342159164184 5.86838373246186e-08 sterol regulatory element binding transcription factor 1 FUNCTION: Transcriptional activator required for lipid homeostasis. Regulates transcription of the LDL receptor gene as well as the fatty acid and to a lesser degree the cholesterol synthesis pathway (By similarity). Binds to the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3'). Has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3'). {ECO:0000250|UniProtKB:Q9WTN3}.; . TISSUE SPECIFICITY: Expressed in a wide variety of tissues, most abundant in liver and adrenal gland. In fetal tissues lung and liver shows highest expression. Isoform SREBP-1C predominates in liver, adrenal gland and ovary, whereas isoform SREBP-1A predominates in hepatoma cell lines. Isoform SREBP-1A and isoform SREBP-1C are found in kidney, brain, white fat, and muscle.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;larynx;bone;iris;testis;germinal center;bladder;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;lens;pancreas;lung;adrenal gland;placenta;visual apparatus;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; adipose tissue;testis - seminiferous tubule;adrenal gland;adrenal cortex;testis;caudate nucleus; 0.17927 0.80016 -0.791786324 12.59731069 471.84841 4.49715 SREBF2 0.996271601286458 0.00372839827425728 4.39284974156729e-10 sterol regulatory element binding transcription factor 2 FUNCTION: Transcriptional activator required for lipid homeostasis. Regulates transcription of the LDL receptor gene as well as the cholesterol and to a lesser degree the fatty acid synthesis pathway (By similarity). Binds the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3') found in the flanking region of the LDRL and HMG-CoA synthase genes. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed in adult and fetal tissues.; lymphoreticular;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;medulla oblongata;superior cervical ganglion;thalamus;cerebellum peduncles;temporal lobe;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.65981 0.47389 -1.831803113 2.093654164 3329.62947 11.03522 SREK1 0.98837347237608 0.0116263543893445 1.7323457527179e-07 splicing regulatory glutamic acid/lysine-rich protein 1 FUNCTION: Participates in the regulation of alternative splicing by modulating the activity of other splice facors. Inhibits the splicing activity of SFRS1, SFRS2 and SFRS6. Augments the splicing activity of SFRS3 (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;thymus; subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.51998 0.09396 -0.291981272 33.20358575 72.44896 1.77314 SREK1IP1 0.656016357375955 0.338309900018231 0.00567374260581435 SREK1 interacting protein 1 FUNCTION: Possible splicing regulator involved in the control of cellular survival.; . . . . 0.23092 0.09836 0.235309407 68.71903751 130.49652 2.48867 SRF 0.970031287954396 0.0299252340390479 4.34780065560577e-05 serum response factor FUNCTION: SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS). Required for cardiac differentiation and maturation.; . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.93550 0.40418 -0.117432389 44.89266336 14.01781 0.50875 SRFBP1 8.19334299777791e-05 0.925468385495652 0.0744496810743707 serum response factor binding protein 1 FUNCTION: May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells (By similarity). {ECO:0000250|UniProtKB:Q9CZ91}.; . TISSUE SPECIFICITY: Abundantly expressed in heart and skeletal muscle, and at much lower levels in brain and lung. {ECO:0000269|PubMed:15492011}.; unclassifiable (Anatomical System);heart;islets of Langerhans;blood;skeletal muscle;pancreas;prostate;lung;nasopharynx;bone;placenta;liver;testis;spleen;kidney;brain;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.09344 0.13743 1.021500656 91.01792876 403.85455 4.21623 SRGAP1 0.987851405418528 0.0121485942580188 3.2345280441495e-10 SLIT-ROBO Rho GTPase activating protein 1 FUNCTION: GTPase-activating protein for RhoA and Cdc42 small GTPases. Together with CDC42 seems to be involved in the pathway mediating the repulsive signaling of Robo and Slit proteins in neuronal migration. SLIT2, probably through interaction with ROBO1, increases the interaction of SRGAP1 with ROBO1 and inactivates CDC42. {ECO:0000269|PubMed:11672528}.; . TISSUE SPECIFICITY: Expressed in brain, lung, kidney, and testis. {ECO:0000269|PubMed:11672528}.; ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;skeletal muscle;pancreas;lung;cornea;epididymis;placenta;visual apparatus;liver;spleen;kidney;mammary gland; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;fetal brain;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.37033 0.13588 -0.815648973 12.01344657 367.76016 4.05455 SRGAP2 . . . SLIT-ROBO Rho GTPase activating protein 2 FUNCTION: RAC1 GTPase activating protein (GAP) that binds and deforms membranes, and regulates actin dynamics to regulate cell migration and differentiation. Plays an important role in different aspects of neuronal morphogenesis and migration mainly during development of the cerebral cortex. This includes the biogenesis of neurites, where it is required for both axons and dendrites outgrowth, and the maturation of the dendritic spines. Also stimulates the branching of the leading process and negatively regulates neuron radial migration in the cerebral cortex. Its interaction and inhibition by SRGAP2C reduces the rate of spine maturation, alters dendritic spine morphology and density and indirectly increases neuronal migration. It may have implications for cognition, learning and memory. In non-neuronal cells, it may also play a role in cell migration by regulating the formation of lamellipodia and filopodia. {ECO:0000269|PubMed:20810653, ECO:0000269|PubMed:21148482, ECO:0000269|PubMed:22559944}.; DISEASE: Note=A chromosomal aberration disrupting SRGAP2 has been found in a patient with early infantile epileptic encephalopathy. Balanced translocation t(1;9)(q32;q13) (PubMed:22106086). {ECO:0000269|PubMed:22106086}.; . ovary;parathyroid;vein;skin;uterus;prostate;whole body;frontal lobe;cochlea;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;urinary;adrenal cortex;lens;skeletal muscle;bile duct;breast;lung;placenta;visual apparatus;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; cerebellum peduncles;cerebellum; 0.30040 0.15582 . . . . SRGAP2-AS1 . . . SRGAP2 antisense RNA 1 . . . . . . . . . . . SRGAP2B . . . SLIT-ROBO Rho GTPase activating protein 2B FUNCTION: May regulate cell migration and differentiation through interaction with and inhibition of SRGAP2. {ECO:0000305|PubMed:22559944}.; . . . . . . . . . . SRGAP2C . . . SLIT-ROBO Rho GTPase activating protein 2C FUNCTION: Involved in dendritic spine maturation through interaction with and inhibition of SRGAP2. Reduces the rate of spine maturation and indirectly increases neuronal migration. Changes dendritic spine morphology and density and may have implications for cognition, learning and memory. {ECO:0000269|PubMed:22559944}.; . TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in cerebellum. Probably expressed in fetal and adult neurons (at protein level). {ECO:0000269|PubMed:22559943, ECO:0000269|PubMed:22559944}.; . . . . . . . . SRGAP2D . . . SLIT-ROBO Rho GTPase activating protein 2D (pseudogene) . . . . . . . . . . . SRGAP3 0.999997750223865 2.24977613464546e-06 7.59064153995436e-16 SLIT-ROBO Rho GTPase activating protein 3 FUNCTION: GTPase-activating protein for RAC1 and perhaps Cdc42, but not for RhoA small GTPase. May attenuate RAC1 signaling in neurons. {ECO:0000269|PubMed:12195014, ECO:0000269|PubMed:12447388}.; DISEASE: Note=A chromosomal aberration involving SRGAP3 is found in a patient with severe idiopathic mental retardation (PubMed:12195014). Translocation t(X;3)(p11.2;p25) (PubMed:12195014). {ECO:0000269|PubMed:12195014}.; TISSUE SPECIFICITY: Highly expressed in adult and fetal brain. Expressed at low levels in kidney. Isoform 3 is expressed in the kidney but is absent in the brain. {ECO:0000269|PubMed:12195014, ECO:0000269|PubMed:12447388}.; unclassifiable (Anatomical System);amygdala;cartilage;ovary;hypothalamus;colon;parathyroid;fovea centralis;lens;uterus;breast;whole body;lung;frontal lobe;endometrium;bone;placenta;macula lutea;liver;testis;spleen;brain;cerebellum; whole brain;dorsal root ganglion;superior cervical ganglion;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.29068 0.14206 -1.635123713 2.836753951 145.30943 2.62469 SRGAP3-AS1 . . . SRGAP3 antisense RNA 1 . . . . . . . . . . . SRGAP3-AS2 . . . SRGAP3 antisense RNA 2 . . . . . . . . . . . SRGAP3-AS3 . . . SRGAP3 antisense RNA 3 . . . . . . . . . . . SRGAP3-AS4 . . . SRGAP3 antisense RNA 4 . . . . . . . . . . . SRGN 0.140766946662158 0.779346732397621 0.0798863209402212 serglycin FUNCTION: Plays a role in formation of mast cell secretory granules and mediates storage of various compounds in secretory vesicles. Required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. Plays a role in localizing neutrophil elastase in azurophil granules of neutrophils. Mediates processing of MMP2. Plays a role in cytotoxic cell granule-mediated apoptosis by forming a complex with granzyme B which is delivered to cells by perforin to induce apoptosis. Regulates the secretion of TNF- alpha and may also regulate protease secretion. Inhibits bone mineralization. {ECO:0000269|PubMed:11911826, ECO:0000269|PubMed:16420477, ECO:0000269|PubMed:16870619}.; . . ovary;umbilical cord;skin;bone marrow;prostate;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;salivary gland;intestine;colon;parathyroid;uterus;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; smooth muscle;white blood cells;whole blood;bone marrow; 0.70911 0.21586 0.703746784 85.42108988 74.41022 1.80196 SRGNP1 . . . serglycin pseudogene 1 . . . . . . . . . . . SRI 9.97957046166647e-05 0.803457731191531 0.196442473103852 sorcin FUNCTION: Calcium-binding protein that modulates excitation- contraction coupling in the heart. Contributes to calcium homeostasis in the heart sarcoplasmic reticulum. Modulates the activity of RYR2 calcium channels. {ECO:0000269|PubMed:17699613}.; . TISSUE SPECIFICITY: Detected in cardiac myocytes.; myocardium;lymphoreticular;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;gall bladder;tonsil;heart;cartilage;pineal body;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;adrenal gland;placenta;hippocampus;kidney;stomach;aorta; amygdala;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;hypothalamus;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.16999 0.15790 0.325313577 73.11276244 58.92951 1.55778 SRIP1 . . . sorcin pseudogene 1 . . . . . . . . . . . SRIP2 . . . sorcin pseudogene 2 . . . . . . . . . . . SRIP3 . . . sorcin pseudogene 3 . . . . . . . . . . . SRL 0.00123342684996184 0.849954264102917 0.148812309047121 sarcalumenin FUNCTION: May be involved in the regulation of calcium transport.; . . . . 0.27632 0.21042 -1.065444789 7.425100259 119.95932 2.38707 SRM 0.869848472217591 0.129784742074837 0.00036678570757128 spermidine synthase FUNCTION: Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM). Has a strong preference for putrescine as substrate, and has very low activity towards 1,3-diaminopropane. Has extremely low activity towards spermidine. {ECO:0000269|PubMed:17585781}.; . . . . 0.18813 0.29083 -0.383807564 27.41802312 13.56758 0.49305 SRMP1 . . . spermidine synthase pseudogene 1 . . . . . . . . . . . SRMP2 . . . spermidine synthase pseudogene 2 . . . . . . . . . . . SRMS 5.12640322619190e-12 0.0149510417692109 0.985048958225663 src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites FUNCTION: Non-receptor tyrosine-protein kinase which phosphorylates DOK1 on tyrosine residues. May be involved in proliferation or differentiation of keratinocytes in the skin. {ECO:0000269|PubMed:23822091}.; . TISSUE SPECIFICITY: Highly expressed in most breast cancers (at protein level).; pancreas;spleen;kidney; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05344 0.23810 0.986521626 90.48124558 4017.31598 12.55495 SRP9 0.308171838775694 0.618765128477285 0.073063032747021 signal recognition particle 9kDa FUNCTION: Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;dura mater;brain;pineal gland;artery;bladder;gall bladder;unclassifiable (Anatomical System);meninges;cerebellum cortex;islets of Langerhans;hypothalamus;spinal cord;adrenal cortex;pharynx;blood;skeletal muscle;breast;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;liver;spleen;head and neck;kidney;stomach;aorta; . 0.12604 0.16436 -0.053113545 49.38664779 3.79518 0.14082 SRP9P1 . . . signal recognition particle 9 pseudogene 1 . . . unclassifiable (Anatomical System);heart;hypothalamus;blood;skin;bone marrow;lung;placenta;thyroid;bone;liver;spleen;kidney;brain;bladder;mammary gland; . . 0.10830 . . . . SRP14 0.83539573119462 0.161340239243055 0.00326402956232538 signal recognition particle 14kDa FUNCTION: Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.; . . lymphoreticular;medulla oblongata;ovary;skin;retina;prostate;frontal lobe;endometrium;thyroid;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;mesenchyma;adrenal gland;placenta;hippocampus;duodenum;kidney;stomach;aorta;thymus; amygdala;subthalamic nucleus;hypothalamus;prefrontal cortex;globus pallidus;caudate nucleus;parietal lobe; 0.18416 0.13292 0.147123112 64.11299835 13.51021 0.49106 SRP14-AS1 . . . SRP14 antisense RNA1 (head to head) . . . . . . . . . . . SRP14P1 . . . signal recognition particle 14kDa (homologous Alu RNA binding protein) pseudogene 1 . . . . . . . . . . . SRP19 0.0852679958175839 0.871180440312253 0.043551563870163 signal recognition particle 19kDa FUNCTION: Signal-recognition-particle assembly, binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;testis;germinal center;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;cornea;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;trigeminal ganglion; 0.09432 0.15749 -0.163345027 41.24793583 5.87102 0.22139 SRP54 0.996689717284175 0.00331024305424971 3.9661575533695e-08 signal recognition particle 54kDa FUNCTION: Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein).; . . myocardium;lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;kidney;stomach; testis - interstitial;testis; . 0.29199 -0.383807564 27.41802312 5.20237 0.19390 SRP54-AS1 . . . SRP54 antisense RNA 1 (head to head) . . . . . . . . . . . SRP68 0.36504497260724 0.634934333953568 2.06934391914131e-05 signal recognition particle 68kDa FUNCTION: Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP68 binds the 7S RNA, SRP72 binds to this complex subsequently. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function.; . . medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;duodenum;head and neck;kidney;stomach;thymus;cerebellum; cerebellum; 0.50561 0.12115 0.50895761 80.20169851 142.31447 2.60239 SRP68P1 . . . signal recognition particle 68kDa pseudogene 1 . . . . . . . . . . . SRP68P2 . . . signal recognition particle 68kDa pseudogene 2 . . . . . . . . . . . SRP68P3 . . . signal recognition particle 68kDa pseudogene 3 . . . . . . . . . . . SRP72 0.0141881388069381 0.985758824673856 5.30365192058604e-05 signal recognition particle 72kDa FUNCTION: Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Binds the 7S RNA only in presence of SRP68. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function.; DISEASE: Bone marrow failure syndrome 1 (BMFS1) [MIM:614675]: An autosomal dominant disease characterized by aplastic anemia and myelodysplasia resulting from bone marrow failure. Aplastic anemia is a form of anemia in which the bone marrow fails to produce adequate numbers of peripheral blood elements. Myelodysplasia is a clonal hematopoietic stem cell disorder in which immature cells in the bone marrow become malformed and dysfunctional. {ECO:0000269|PubMed:22541560}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;gum;iris;germinal center;brain;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;duodenum;kidney;stomach;aorta; superior cervical ganglion;white blood cells;atrioventricular node;trigeminal ganglion; 0.73877 0.13749 -0.600630256 18.06440198 322.10949 3.80967 SRP72P1 . . . signal recognition particle 72kDa pseudogene 1 . . . . . . . . . . . SRP72P2 . . . signal recognition particle 72kDa pseudogene 2 . . . . . . . . . . . SRPK1 0.000394806789886588 0.997713248363628 0.00189194484648591 SRSF protein kinase 1 FUNCTION: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Isoform 2 phosphorylates SFRS2, ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Isoform 2 can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Isoform 1 and isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of isoform 1/isoform 2 plays a decisive role in determining cell fate in K-562 leukaemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation. {ECO:0000269|PubMed:10049757, ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:11509566, ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:14555757, ECO:0000269|PubMed:15034300, ECO:0000269|PubMed:16122776, ECO:0000269|PubMed:16209947, ECO:0000269|PubMed:18155240, ECO:0000269|PubMed:18687337, ECO:0000269|PubMed:19240134, ECO:0000269|PubMed:19477182, ECO:0000269|PubMed:19886675, ECO:0000269|PubMed:20708644, ECO:0000269|PubMed:8208298, ECO:0000269|PubMed:9237760}.; . TISSUE SPECIFICITY: Isoform 2 is predominantly expressed in the testis but is also present at lower levels in heart, ovary, small intestine, liver, kidney, pancreas and skeletal muscle. Isoform 1 is only seen in the testis, at lower levels than isoform 2. Highly expressed in different erythroid and lymphoid cell lines, with isoform 2 being far more abundant than isoform 1. {ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:11509566, ECO:0000269|PubMed:20708644}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;heart;cerebellum cortex;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;alveolus;duodenum;liver;cervix;head and neck;spleen;kidney;mammary gland;aorta;stomach;cerebellum; dorsal root ganglion;fetal liver;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;pons;trigeminal ganglion;skeletal muscle; 0.36461 0.11015 -0.336073593 30.55555556 167.21383 2.82597 SRPK2 0.997504054449169 0.00249594473546932 8.15361111091196e-10 SRSF protein kinase 2 FUNCTION: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression. Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up- regulation. Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28. Can mediate hepatitis B virus (HBV) core protein phosphorylation. Plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. {ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:16122776, ECO:0000269|PubMed:18425142, ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:21056976, ECO:0000269|PubMed:21157427, ECO:0000269|PubMed:9472028}.; . TISSUE SPECIFICITY: Highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney. {ECO:0000269|PubMed:9472028}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;bone;thyroid;pituitary gland;testis;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;heart;tongue;islets of Langerhans;urinary;pharynx;blood;lens;breast;pia mater;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; amygdala;whole brain;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;testis - interstitial;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;atrioventricular node;pons;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.76287 0.12361 -1.221604042 5.573248408 28.33627 0.90720 SRPK2P . . . SRSF protein kinase 2 pseudogene . . . . . . . . . . . SRPK3 0.179643538378432 0.81776533284451 0.00259112877705799 SRSF protein kinase 3 FUNCTION: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains. Phosphorylates the SR splicing factor SRSF1 and the lamin-B receptor (LBR) in vitro. Required for normal muscle development (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Exclusively expressed in skeletal and heart muscle. {ECO:0000269|PubMed:11063724}.; . . 0.22866 0.11172 -0.33061537 30.82094834 46.03612 1.30706 SRPRA . . . SRP receptor alpha subunit FUNCTION: Component of the SRP (signal recognition particle) receptor. Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system.; . . . . 0.63761 0.15981 -0.887242605 10.43288511 . . SRPRB 0.0107906261312511 0.94673125522341 0.0424781186453392 SRP receptor beta subunit FUNCTION: Component of the SRP (signal recognition particle) receptor. Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. Has GTPase activity. May mediate the membrane association of SRPR (By similarity). {ECO:0000250}.; . . . . 0.15227 0.10090 -0.049474214 50.01179523 937.84935 5.93659 SRPX 0.00848262097838311 0.97836236966954 0.0131550093520765 sushi repeat containing protein, X-linked FUNCTION: May be involved in phagocytosis during disk shedding, cell adhesion to cells other than the pigment epithelium or signal transduction.; . TISSUE SPECIFICITY: Retina and heart; less in placenta, pancreas, lung, liver, skeletal muscle, kidney and brain.; unclassifiable (Anatomical System);cartilage;heart;ovary;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;breast;pancreas;optic nerve;whole body;lung;nasopharynx;bone;placenta;macula lutea;liver;testis;spleen;brain; dorsal root ganglion;superior cervical ganglion;smooth muscle;adipose tissue;heart;adrenal gland;appendix;atrioventricular node;skeletal muscle; 0.63801 0.13572 0.220536484 68.38287332 1848.85909 7.93014 SRPX2 0.96252939282245 0.0374674949449474 3.11223260297274e-06 sushi repeat containing protein, X-linked 2 FUNCTION: Acts as a ligand for the urokinase plasminogen activator surface receptor. Plays a role in angiogenesis by inducing endothelial cell migration and the formation of vascular network (cords). Involved in cellular migration and adhesion. Increases the phosphorylation levels of FAK. Interacts with and increases the mitogenic activity of HGF. Promotes synapse formation. May have a role in the perisylvian region, critical for language and cognitive development. {ECO:0000269|PubMed:16497722, ECO:0000269|PubMed:18718938, ECO:0000269|PubMed:19065654, ECO:0000269|PubMed:24179158}.; DISEASE: Rolandic epilepsy with speech dyspraxia and mental retardation X-linked (RESDX) [MIM:300643]: A condition characterized by the association of rolandic seizures with oral and speech dyspraxia, and mental retardation. Rolandic seizures occur during a period of significant brain maturation. During this time, dysfunction of neural network activities such as focal discharges may be associated with specific developmental disabilities resulting in specific cognitive impairments of language, visuo-spatial abilities or attention. {ECO:0000269|PubMed:16497722}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in neurons of the rolandic area of the brain (at protein level). Highly expressed in the brain, placenta, lung, trachea, uterus, adrenal gland, heart, ovary and placenta. Weakly expressed in the peripheral blood, brain and bone marrow. Expressed in numerous cancer cell lines and in gastrointestinal cancer cells. Higher levels found in colorectal cancers than in normal colonic mucosa. {ECO:0000269|PubMed:16497722, ECO:0000269|PubMed:18718938, ECO:0000269|PubMed:19065654, ECO:0000269|PubMed:22242148, ECO:0000269|PubMed:9864177}.; . . 0.30928 0.13849 0.174625237 65.9648502 51.08082 1.40844 SRR 0.179017047265105 0.808466585348635 0.0125163673862595 serine racemase FUNCTION: Catalyzes the synthesis of D-serine from L-serine. D- serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine. {ECO:0000269|PubMed:11054547, ECO:0000269|PubMed:20106978}.; . TISSUE SPECIFICITY: Brain: expressed at high levels in hippocampus and corpus callosum, intermediate levels in substantia nigra and caudate, and low levels in amygdala, thalamus, and subthalamic nuclei. Expressed in heart, skeletal muscle, kidney and liver. {ECO:0000269|PubMed:15193426}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;lens;skeletal muscle;bile duct;breast;lung;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.50562 0.21960 -0.471992905 23.03609342 8.72817 0.32113 SRRD 1.58605385256121e-06 0.235404863145083 0.764593550801064 SRR1 domain containing FUNCTION: May be involved in a circadian clock input pathway. {ECO:0000250}.; . . ovary;foreskin;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;pituitary gland;testis;amniotic fluid;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;epidermis;islets of Langerhans;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney; superior cervical ganglion;ciliary ganglion; 0.14020 0.09419 -0.137658575 43.57159707 20.47367 0.69702 SRRM1 0.999999022390233 9.77609767263387e-07 2.01679999355392e-17 serine and arginine repetitive matrix 1 FUNCTION: Part of pre- and post-splicing multiprotein mRNP complexes. Involved in numerous pre-mRNA processing events. Promotes constitutive and exonic splicing enhancer (ESE)-dependent splicing activation by bridging together sequence-specific (SR family proteins, SFRS4, SFRS5 and TRA2B/SFRS10) and basal snRNP (SNRP70 and SNRPA1) factors of the spliceosome. Stimulates mRNA 3'-end cleavage independently of the formation of an exon junction complex. Binds both pre-mRNA and spliced mRNA 20-25 nt upstream of exon-exon junctions. Binds RNA and DNA with low sequence specificity and has similar preference for either double- or single-stranded nucleic acid substrates. {ECO:0000269|PubMed:10339552, ECO:0000269|PubMed:10668804, ECO:0000269|PubMed:11739730, ECO:0000269|PubMed:12600940, ECO:0000269|PubMed:12944400, ECO:0000269|PubMed:9531537}.; . . ovary;umbilical cord;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;iris;amniotic fluid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;atrioventricular node;pons;kidney;trigeminal ganglion;cerebellum; 0.53120 0.11301 -0.929520514 9.683887709 90.5423 2.04787 SRRM1P1 . . . serine/arginine repetitive matrix 1 pseudogene 1 . . . . . . . . . . . SRRM1P2 . . . serine/arginine repetitive matrix 1 pseudogene 2 . . . . . . . . . . . SRRM1P3 . . . serine/arginine repetitive matrix 1 pseudogene 3 . . . . . . . . . . . SRRM2 . . . serine/arginine repetitive matrix 2 FUNCTION: Involved in pre-mRNA splicing. May function at or prior to the first catalytic step of splicing at the catalytic center of the spliceosome. May do so by stabilizing the catalytic center or the position of the RNA substrate (By similarity). Binds to RNA. {ECO:0000250, ECO:0000269|PubMed:10668804}.; . TISSUE SPECIFICITY: Expressed in liver, placenta, and white blood cells. {ECO:0000269|PubMed:11004489}.; lymphoreticular;ovary;salivary gland;sympathetic chain;intestine;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;spinal cord;urinary;pharynx;blood;skeletal muscle;breast;lung;cornea;epididymis;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland; prostate;superior cervical ganglion;adrenal cortex;cingulate cortex;skeletal muscle; 0.10075 0.23464 -4.509811703 0.082566643 2273.46798 8.81560 SRRM2-AS1 . . . SRRM2 antisense RNA 1 . . . . . . . . . . . SRRM3 0.911827252904099 0.0880395564370994 0.000133190658801183 serine/arginine repetitive matrix 3 . . . optic nerve;islets of Langerhans;macula lutea;colon;fovea centralis;choroid;lens;retina; . . . . . 1096.45578 6.33791 SRRM4 0.411747626154712 0.588180964271102 7.14095741855566e-05 serine/arginine repetitive matrix 4 FUNCTION: Splicing factor specifically required for neural cell differentiation. Acts in conjuction with nPTB/PTBP2 by binding directly to its regulated target transcripts and promotes neural- specific exon inclusion in many genes that function in neural cell differentiation. Required to promote the inclusion of neural- specific exon 10 in nPTB/PTBP2, leading to increased expression of neural-specific nPTB/PTBP2. Also promotes the inclusion of exon 16 in DAAM1 in neuron extracts (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in neuronal cells (at protein level). Expressed in the cerebellum. {ECO:0000269|PubMed:12800201, ECO:0000269|PubMed:19737518}.; unclassifiable (Anatomical System);sympathetic chain;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;lung;frontal lobe;placenta;bone;macula lutea;visual apparatus;alveolus;testis;kidney;brain;cerebellum; dorsal root ganglion;medulla oblongata;superior cervical ganglion;testis - interstitial;cerebellum peduncles;temporal lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.35378 0.10934 0.112125503 62.09601321 3155.06623 10.69649 SRRM5 7.19141934794887e-06 0.289035887039665 0.710956921540987 serine/arginine repetitive matrix 5 . . . . . . . 2.973217798 99.19202642 2241.61308 8.73687 SRRT 0.982967889936454 0.0170321063970679 3.66647851334898e-09 serrate, RNA effector molecule FUNCTION: Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery during cell proliferation. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped RNA); however interaction is probably mediated via its interaction with NCBP1/CBP80 component of the CBC complex. Involved in cell cycle progression at S phase. Does not directly confer arsenite resistance but rather modulates arsenic sensitivity. Independently of its activity on miRNAs, necessary and sufficient to promote neural stem cell self-renewal. Does so by directly binding SOX2 promoter and positively regulating its transcription (By similarity). {ECO:0000250, ECO:0000269|PubMed:19632182}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:18086880}.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;bile duct;lung;cornea;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; . . -1.594640695 3.054965794 73.53732 1.79256 SRSF1 0.991994022925919 0.00800428167319358 1.69540088767904e-06 serine/arginine-rich splicing factor 1 FUNCTION: Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'- CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing. Isoform ASF-2 and isoform ASF-3 act as splicing repressors. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway. {ECO:0000269|PubMed:8139654}.; . . medulla oblongata;ovary;skin;bone marrow;prostate;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;pancreas;lung;cornea;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; superior cervical ganglion;fetal liver;atrioventricular node; 0.85062 0.04472 -0.009020804 52.8544468 . . SRSF1P1 . . . serine/arginine-rich splicing factor 1 pseudogene 1 . . . . . . . . . . . SRSF2 0.352601171847882 0.634448379595982 0.0129504485561356 serine/arginine-rich splicing factor 2 FUNCTION: Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with pre- mRNA. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Binds to purine-rich RNA sequences, either 5'-AGSAGAGTA-3' (S=C or G) or 5'-GTTCGAGTA-3'. Can bind to beta-globin mRNA and commit it to the splicing pathway. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment. {ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:21157427}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;muscle;urinary;pharynx;blood;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;testis - interstitial;fetal liver;testis - seminiferous tubule;testis;tumor;white blood cells;trigeminal ganglion; 0.53070 0.11601 -0.251530012 35.42108988 . . SRSF3 0.976175209668048 0.0238001260124275 2.46643195241527e-05 serine/arginine-rich splicing factor 3 FUNCTION: May be involved in RNA processing in relation with cellular proliferation and/or maturation. May function as export adapter involved in mRNA nuclear export such as of histone H2A. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA- binding activity. RNA-binding is semi-sequence specific. {ECO:0000269|PubMed:11336712, ECO:0000269|PubMed:18364396}.; . . lymphoreticular;ovary;colon;skin;bone marrow;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;head and neck;kidney;stomach;cerebellum; occipital lobe;fetal liver;ciliary ganglion;atrioventricular node;cingulate cortex; 0.79279 0.13588 0.035072054 56.2514744 . . SRSF4 0.934762697175769 0.0652347675572733 2.53526695739722e-06 serine/arginine-rich splicing factor 4 FUNCTION: Plays a role in alternative splice site selection during pre-mRNA splicing. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269|PubMed:15009664}.; . . . . 0.92262 0.12859 0.064394823 58.84642604 6035.96687 16.22008 SRSF5 0.339129154603779 0.660252923302645 0.000617922093576721 serine/arginine-rich splicing factor 5 FUNCTION: Plays a role in constitutive splicing and can modulate the selection of alternative splice sites.; . . . . 0.37344 0.11262 -0.494039303 22.09247464 10.97464 0.39686 SRSF6 0.992976413171211 0.00702333768904411 2.49139745318945e-07 serine/arginine-rich splicing factor 6 FUNCTION: Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation of keratinocyte differentiation and proliferation via its role in alternative splicing. {ECO:0000269|PubMed:12549914, ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:22767602, ECO:0000269|PubMed:24440982}.; . . myocardium;medulla oblongata;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;cornea;placenta;hypopharynx;head and neck;kidney;stomach; ciliary ganglion; 0.08561 0.11448 -0.560178693 19.30879925 44.38338 1.27269 SRSF7 0.997841973267641 0.00215801276680471 1.39655539004798e-08 serine/arginine-rich splicing factor 7 FUNCTION: Required for pre-mRNA splicing. Can also modulate alternative splicing in vitro. Represses the splicing of MAPT/Tau exon 10. May function as export adapter involved in mRNA nuclear export such as of histone H2A. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity. RNA-binding is semi-sequence specific. {ECO:0000269|PubMed:11336712, ECO:0000269|PubMed:12667464, ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:18364396}.; . TISSUE SPECIFICITY: Brain, liver, kidney and lung.; lymphoreticular;ovary;salivary gland;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;alveolus;duodenum;liver;spleen;cervix;kidney;mammary gland;aorta;stomach;thymus; dorsal root ganglion;amygdala;medulla oblongata;superior cervical ganglion;thalamus;hypothalamus;white blood cells;pons;atrioventricular node;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;testis;trigeminal ganglion;parietal lobe; 0.82201 0.12378 -0.207437529 38.2814343 9.40961 0.34655 SRSF8 . . . serine/arginine-rich splicing factor 8 FUNCTION: Involved in pre-mRNA alternative splicing. {ECO:0000269|PubMed:9671500}.; . TISSUE SPECIFICITY: Strongly expressed in pancreas, spleen and prostate. Weakly expressed in lung, liver and thymus. {ECO:0000269|PubMed:9671500}.; . . . . . . . . SRSF9 0.819638672376706 0.179481410560689 0.000879917062605334 serine/arginine-rich splicing factor 9 FUNCTION: Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269|PubMed:10196175, ECO:0000269|PubMed:11875052, ECO:0000269|PubMed:12024014, ECO:0000269|PubMed:12604611, ECO:0000269|PubMed:15009090, ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:15695522, ECO:0000269|PubMed:7556075}.; . TISSUE SPECIFICITY: Expressed at high levels in the heart, kidney, pancreas and placenta, and at lower levels in the brain, liver, lung and skeletal muscle. {ECO:0000269|PubMed:10196175}.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;placenta;hippocampus;duodenum;head and neck;kidney;stomach; whole brain;prostate;lung;testis - seminiferous tubule;placenta;thyroid;testis;kidney;parietal lobe;cerebellum; 0.62966 0.14896 -0.05129383 49.75819769 87.83635 2.00220 SRSF9P1 . . . serine/arginine-rich splicing factor 9 pseudogene 1 . . . . . . . . . . . SRSF10 . . . serine/arginine-rich splicing factor 10 FUNCTION: Splicing factor that in its dephosphorylated form acts as a general repressor of pre-mRNA splicing. Seems to interfere with the U1 snRNP 5'-splice recognition of SNRNP70. Required for splicing repression in M-phase cells and after heat shock. May be involved in regulation of alternative splicing in neurons, with isoform 1 acting as a positive and isoform 3 as a negative regulator. {ECO:0000269|PubMed:11684676, ECO:0000269|PubMed:12419250, ECO:0000269|PubMed:14765198}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11684676, ECO:0000269|PubMed:11891055}.; lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;pineal gland;artery;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;head and neck;cervix;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.84359 0.12378 . . . . SRSF10P1 . . . serine/arginine-rich splicing factor 10 pseudogene 1 . . . . . . . . . . . SRSF10P2 . . . serine/arginine-rich splicing factor 10 pseudogene 2 . . . . . . . . . . . SRSF11 0.999787767134473 0.000212232623266427 2.42260853212185e-10 serine/arginine-rich splicing factor 11 FUNCTION: May function in pre-mRNA splicing.; . . . . 0.62578 0.14896 -0.405853867 26.23260203 6.2299 0.23496 SRSF11P1 . . . serine/arginine-rich splicing factor 11 pseudogene 1 . . . . . . . . . . . SRSF12 0.01623122038502 0.959356920937529 0.024411858677451 serine/arginine-rich splicing factor 12 FUNCTION: Splicing factor that seems to antagonize SR proteins in pre-mRNA splicing regulation. {ECO:0000269|PubMed:11684676}.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:11684676}.; . . . . 0.325313577 73.11276244 39.91476 1.17410 SRXN1 0.00865787938463754 0.572798774999094 0.418543345616268 sulfiredoxin 1 FUNCTION: Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase. {ECO:0000269|PubMed:15448164, ECO:0000269|PubMed:15590625}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in kidney, lung, spleen and thymus. {ECO:0000269|PubMed:15448164}.; . . 0.10349 . . . 43.95943 1.26318 SRY 0.416019592282844 0.466213249505803 0.117767158211354 sex determining region Y FUNCTION: Transcriptional regulator that controls a genetic switch in male development. It is necessary and sufficient for initiating male sex determination by directing the development of supporting cell precursors (pre-Sertoli cells) as Sertoli rather than granulosa cells (By similarity). In male adult brain involved in the maintenance of motor functions of dopaminergic neurons (By similarity). Involved in different aspects of gene regulation including promoter activation or repression (By similarity). Promotes DNA bending. SRY HMG box recognizes DNA by partial intercalation in the minor groove. Also involved in pre-mRNA splicing. Binds to the DNA consensus sequence 5'-[AT]AACAA[AT]-3'. {ECO:0000250, ECO:0000269|PubMed:11563911, ECO:0000269|PubMed:11818535, ECO:0000269|PubMed:15170344, ECO:0000269|PubMed:16762365}.; DISEASE: 46,XY sex reversal 1 (SRXY1) [MIM:400044]: A condition characterized by male-to-female sex reversal in the presence of a normal 46,XY karyotype. Patients manifest rapid and early degeneration of their gonads, which are present in the adult as 'streak gonads', consisting mainly of fibrous tissue and variable amounts of ovarian stroma. As a result these patients do not develop secondary sexual characteristics at puberty. The external genitalia in these subjects are completely female, and Muellerian structures are normal. {ECO:0000269|PubMed:10670762, ECO:0000269|PubMed:10721678, ECO:0000269|PubMed:10843173, ECO:0000269|PubMed:10852465, ECO:0000269|PubMed:12107262, ECO:0000269|PubMed:12793612, ECO:0000269|PubMed:1339396, ECO:0000269|PubMed:1415266, ECO:0000269|PubMed:1483689, ECO:0000269|PubMed:1570829, ECO:0000269|PubMed:17063144, ECO:0000269|PubMed:2247149, ECO:0000269|PubMed:7717397, ECO:0000269|PubMed:7776083, ECO:0000269|PubMed:7985018, ECO:0000269|PubMed:8019555, ECO:0000269|PubMed:8105086, ECO:0000269|PubMed:8353496, ECO:0000269|PubMed:8447323, ECO:0000269|PubMed:9450909, ECO:0000269|PubMed:9521592, ECO:0000269|PubMed:9678356, ECO:0000269|Ref.41, ECO:0000269|Ref.47}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A 45,X chromosomal aberration involving SRY is found in Turner syndrome, a disease characterized by gonadal dysgenesis with short stature, "streak gonads", variable abnormalities such as webbing of the neck, cubitus valgus, cardiac defects, low posterior hair line. The phenotype is female.; DISEASE: 46,XX sex reversal 1 (SRXX1) [MIM:400045]: A condition in which male gonads develop in a genetic female (female to male sex reversal). {ECO:0000269|PubMed:10602113, ECO:0000269|PubMed:9652903}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.15959 . . . 0.82297 0.01646 SS18 0.994140958944221 0.00585888112130429 1.59934474885819e-07 synovial sarcoma translocation, chromosome 18 FUNCTION: Appears to function synergistically with RBM14 as a transcriptional coactivator. Isoform 1 and isoform 2 function in nuclear receptor coactivation. Isoform 1 and isoform 2 function in general transcriptional coactivation. {ECO:0000269|PubMed:15919756}.; . TISSUE SPECIFICITY: Fairly ubiquitously expressed. Expressed in synovial sarcomas and in other human cell lines. The fusion genes SSXT-SSX1 and SSXT-SSX2 are expressed only in synovial sarcomas.; ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;bladder;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.88676 0.12141 -0.115612493 45.12856806 164.78585 2.80431 SS18L1 0.812233116235997 0.18772616489602 4.07188679823249e-05 synovial sarcoma translocation gene on chromosome 18-like 1 FUNCTION: Transcriptional activator which is required for calcium- dependent dendritic growth and branching in cortical neurons. Recruits CREB-binding protein (CREBBP) to nuclear bodies. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous; with lowest levels in spleen.; ovary;colon;bone marrow;uterus;prostate;whole body;oesophagus;endometrium;testis;germinal center;brain;artery;gall bladder;unclassifiable (Anatomical System);islets of Langerhans;blood;skeletal muscle;bile duct;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;stomach;aorta; amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;fetal brain;cerebellum peduncles;temporal lobe;prefrontal cortex;pons;parietal lobe;cerebellum; 0.59429 0.10387 -0.534490515 20.70063694 243.23221 3.36600 SS18L2 0.0602071955135164 0.718173963191094 0.22161884129539 synovial sarcoma translocation gene on chromosome 18-like 2 . . . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;heart;cerebellum cortex;islets of Langerhans;oral cavity;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;aorta;stomach;peripheral nerve;cerebellum;thymus; dorsal root ganglion;thalamus;subthalamic nucleus;temporal lobe;prefrontal cortex;globus pallidus;atrioventricular node;pons;trigeminal ganglion;parietal lobe;cingulate cortex; 0.26809 0.10225 0.101211609 60.95777306 2.40691 0.08408 SS18L2P1 . . . synovial sarcoma translocation gene on chromosome 18-like 2 pseudogene 1 . . . . . . . . . . . SS18L2P2 . . . synovial sarcoma translocation gene on chromosome 18-like 2 pseudogene 2 . . . . . . . . . . . SSB 0.525946313253719 0.473330718829172 0.000722967917109145 Sjogren syndrome antigen B FUNCTION: Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation (PubMed:3192525, PubMed:2470590). In case of Coxsackievirus B3 infection, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation (PubMed:12384597). {ECO:0000269|PubMed:12384597, ECO:0000269|PubMed:2470590, ECO:0000269|PubMed:3192525}.; . . lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;bladder;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; amygdala;prefrontal cortex;tumor; 0.97701 0.39284 -0.227663163 37.11370606 66.86759 1.68814 SSBP1 0.058441518078084 0.92405995367448 0.017498528247436 single-stranded DNA binding protein 1, mitochondrial FUNCTION: This protein binds preferentially and cooperatively to ss-DNA. Probably involved in mitochondrial DNA replication. Associates with mitochondrial DNA.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;bladder;brain;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;oral cavity;bile duct;pancreas;lung;pia mater;placenta;head and neck;kidney;stomach;aorta; testis;tumor;white blood cells; 0.21552 0.16111 -0.053113545 49.38664779 32.2336 1.00881 SSBP2 0.976772519033216 0.0232265302242805 9.50742503389777e-07 single-stranded DNA binding protein 2 . . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12079286}.; umbilical cord;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach;cerebellum;thymus; superior cervical ganglion;fetal brain;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.20457 0.12378 -0.029247611 51.40363293 15.15944 0.54535 SSBP3 0.99975619603717 0.000243803623197997 3.3963158180352e-10 single stranded DNA binding protein 3 FUNCTION: May be involved in transcription regulation of the alpha 2(I) collagen gene where it binds to the single-stranded polypyrimidine sequences in the promoter region. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in all hematopoietic tissues, including spleen, lymph node, peripheral blood, bone marrow, thymus, and fetal liver, with highest expression in thymus and fetal liver. Expression is also high in heart, brain, kidney, and skeletal muscle.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;pineal body;pharynx;blood;lens;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; medulla oblongata;superior cervical ganglion;prefrontal cortex;globus pallidus;pons;trigeminal ganglion;cingulate cortex; 0.15537 0.08395 -0.648365105 16.35999056 29.52993 0.94347 SSBP3-AS1 . . . SSBP3 antisense RNA 1 . . . . . 0.02215 . . . 78.75955 1.87418 SSBP4 0.96165888216155 0.0383378222858091 3.29555264100651e-06 single stranded DNA binding protein 4 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;pancreas;lung;placenta;hippocampus;macula lutea;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; . 0.20604 0.10821 -0.293801652 32.93819297 37.43039 1.11514 SSC4D . . . scavenger receptor cysteine rich family, 4 domains . . . . . 0.10688 0.16332 0.576916344 82.25406936 . . SSC5D 0.34696871421864 0.484873479644922 0.168157806136438 scavenger receptor cysteine rich family, 5 domains FUNCTION: Binds to extracellular matrix proteins. Binds to pathogen-associated molecular patterns (PAMPs) present on the cell walls of Gram-positive and Gram-negative bacteria and fungi, behaving as a pattern recognition receptor (PRR). Induces bacterial and fungal aggregation and subsequent inhibition of PAMP-induced cytokine release. Does not possess intrinsic bactericidal activity. May play a role in the innate defense and homeostasis of certain epithelial surfaces (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in monocytes/macrophages and T-lymphocytes. Highly expressed in placenta and spleen, and also detected at lower levels in colon, and more weakly in lung, heart and kidney. {ECO:0000269|PubMed:19535143}.; . . . . 3.778595825 99.61665487 7583.62392 18.68079 SSFA2 7.68386262291993e-05 0.999757987032017 0.000165174341753417 sperm specific antigen 2 . . TISSUE SPECIFICITY: Strongly expressed in pancreas and testis. Present in colon cancer cells (at protein level). {ECO:0000269|PubMed:14673706}.; ovary;substantia nigra;skin;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;iris;germinal center;bladder;brain;heart;cartilage;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;aorta;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;olfactory bulb;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.16545 0.10002 0.235100429 68.59518754 2237.71105 8.72526 SSH1 0.987158740858356 0.0128412500900818 9.0515625562422e-09 slingshot protein phosphatase 1 FUNCTION: Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein. {ECO:0000269|PubMed:11832213, ECO:0000269|PubMed:12684437, ECO:0000269|PubMed:12807904, ECO:0000269|PubMed:14531860, ECO:0000269|PubMed:14645219, ECO:0000269|PubMed:15056216, ECO:0000269|PubMed:15159416, ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:15671020, ECO:0000269|PubMed:16230460}.; . . colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;testis;germinal center;brain;gall bladder;tonsil;unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.11128 0.11460 -0.365622677 28.30856334 196.47062 3.03167 SSH2 0.999753484794653 0.000246515204761999 5.8489195441843e-13 slingshot protein phosphatase 2 FUNCTION: Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein. {ECO:0000269|PubMed:11832213}.; . . lymphoreticular;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.53245 0.09592 -0.099241008 45.68294409 1818.77446 7.86582 SSH3 1.31856569258694e-07 0.944896917022879 0.0551029511205516 slingshot protein phosphatase 3 FUNCTION: Protein phosphatase which may play a role in the regulation of actin filament dynamics. Can dephosphorylate and activate the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly (By similarity). {ECO:0000250}.; . . ovary;colon;substantia nigra;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;lung;trigeminal ganglion;skeletal muscle; 0.50906 0.09727 -0.771553417 13.15168672 460.98331 4.45173 SSMEM1 6.42506346890127e-13 0.00229306010261336 0.997706939896744 serine-rich single-pass membrane protein 1 . . . . . 0.38794 . 0.815800671 87.8744987 601.12409 4.96209 SSNA1 0.00800260908344484 0.556053673727426 0.435943717189129 Sjogren syndrome nuclear autoantigen 1 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9430706}.; medulla oblongata;ovary;salivary gland;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;bone;thyroid;testis;germinal center;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;epididymis;placenta;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; testis - interstitial;testis - seminiferous tubule;heart;testis; 0.21672 0.13890 -0.009020804 52.8544468 10.04155 0.36680 SSPN 0.753322775232488 0.237014477546438 0.0096627472210739 sarcospan FUNCTION: Component of the dystrophin-glycoprotein complex (DGC), a complex that spans the muscle plasma membrane and forms a link between the F-actin cytoskeleton and the extracellular matrix. Preferentially associates with the sarcoglycan subcomplex of the DGC.; . TISSUE SPECIFICITY: Isoform 1 is expressed exclusively in heart and skeletal muscle. Isoform 2 is expressed in heart, skeletal muscle, thymus, prostate, testis, ovary, small intestine, colon and spleen.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;macula lutea;liver;mammary gland; uterus;prostate;olfactory bulb;thyroid;skeletal muscle; 0.34846 0.22280 0.637604436 83.77565464 1220.74547 6.60490 SSPO . . . SCO-spondin FUNCTION: Involved in the modulation of neuronal aggregation. May be involved in developmental events during the formation of the central nervous system (By similarity). {ECO:0000250}.; . . brain; . 0.20432 . . . . . SSR1 0.0322896005433474 0.958634179804506 0.00907621965214629 signal sequence receptor, alpha FUNCTION: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins.; . . lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; superior cervical ganglion;thyroid;ciliary ganglion;skeletal muscle; 0.19355 0.18675 0.170987912 65.5579146 1522.7479 7.25123 SSR1P1 . . . signal sequence receptor, alpha pseudogene 1 . . . . . . . . . . . SSR1P2 . . . signal sequence receptor, alpha pseudogene 2 . . . . . . . . . . . SSR2 0.822108921079836 0.177043659130045 0.000847419790118414 signal sequence receptor, beta (translocon-associated protein beta) FUNCTION: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.; . . lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;oesophagus;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;islets of Langerhans;pancreas;lung;cornea;placenta;duodenum;kidney;stomach;aorta;thymus; testis - interstitial;testis - seminiferous tubule;adrenal gland;testis; 0.53008 0.17250 -0.207437529 38.2814343 6.48678 0.24082 SSR3 0.301905502483941 0.679001560727239 0.0190929367888194 signal sequence receptor, gamma (translocon-associated protein gamma) FUNCTION: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.; . . myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; superior cervical ganglion;prostate;trachea;thyroid;skeletal muscle; 0.16971 0.12971 -0.229483771 36.86010852 9.34458 0.34342 SSR4 0.806792211750699 0.188213694579876 0.00499409366942555 signal sequence receptor, delta FUNCTION: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.; DISEASE: Congenital disorder of glycosylation 1Y (CDG1Y) [MIM:300934]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:24218363}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;prostate;optic nerve;endometrium;iris;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;adrenal gland;placenta;hippocampus;duodenum;kidney;stomach; prostate;pancreas;heart;trachea;placenta;beta cell islets;liver;pituitary;bone marrow; 0.38581 0.44641 0.013025609 54.62962963 6.78359 0.25046 SSR4P1 . . . signal sequence receptor, delta pseudogene 1 . . . . . . . . . . . SSRP1 0.999693191606899 0.000306808272791637 1.20309507652489e-10 structure specific recognition protein 1 FUNCTION: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA and at low levels to DNA modified by the antitumor agent cisplatin. May potentiate cisplatin-induced cell death by blocking replication and repair of modified DNA. Also acts as a transcriptional coactivator for p63/TP63. {ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:12374749, ECO:0000269|PubMed:12934006, ECO:0000269|PubMed:16713563, ECO:0000269|PubMed:9489704, ECO:0000269|PubMed:9566881, ECO:0000269|PubMed:9836642}.; . . lymphoreticular;medulla oblongata;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; testis - interstitial;tumor;white blood cells; 0.78255 0.19294 -0.756778259 13.44656759 22.95881 0.76507 SSSCA1 0.00200151049783838 0.737906608657559 0.260091880844603 Sjogren syndrome/scleroderma autoantigen 1 FUNCTION: Might play a role in mitosis. Antigenic molecule. Could be a centromere-associated protein. May induce anti-centromere antibodies.; . . ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;bone marrow;uterus;prostate;whole body;frontal lobe;oesophagus;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;heart;islets of Langerhans;pharynx;blood;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;aorta;stomach; heart; 0.21115 0.17723 0.03689118 56.64071715 176.86789 2.88986 SSSCA1-AS1 . . . SSSCA1 antisense RNA 1 (head to head) . . . . . . . . . . . SST 0.66549802364856 0.311957420306858 0.0225445560445823 somatostatin FUNCTION: Somatostatin inhibits the release of somatotropin.; . . unclassifiable (Anatomical System);pancreas;ovary;heart;islets of Langerhans;hypothalamus;placenta;parathyroid;kidney;brain;stomach; whole brain;amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;hypothalamus;beta cell islets;globus pallidus;ciliary ganglion;caudate nucleus;pons;parietal lobe; 0.20692 0.70649 0.457594962 78.16112291 47.16264 1.32962 SSTR1 0.829919497496787 0.166521772208103 0.00355873029511073 somatostatin receptor 1 FUNCTION: Receptor for somatostatin with higher affinity for somatostatin-14 than -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and Na(+)/H(+) exchanger via pertussis toxin insensitive G proteins.; . TISSUE SPECIFICITY: Fetal kidney, fetal liver, and adult pancreas, brain, lung, jejunum and stomach.; unclassifiable (Anatomical System);lung;frontal lobe;ovary;islets of Langerhans;placenta;testis;parathyroid;cervix;spleen;brain;skin; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.09805 0.20186 -0.071520315 48.34866714 30.24688 0.96477 SSTR2 0.235751811356346 0.731588294814609 0.0326598938290448 somatostatin receptor 2 FUNCTION: Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and PLC via pertussis toxin insensitive as well as sensitive G proteins. Inhibits calcium entry by suppressing voltage-dependent calcium channels. Acts as the functionally dominant somatostatin receptor in pancreatic alpha- and beta-cells where it mediates the inhibitory effect of somatostatin-14 on hormone secretion. Inhibits cell growth through enhancement of MAPK1 and MAPK2 phosphorylation and subsequent up-regulation of CDKN1B. Stimulates neuronal migration and axon outgrowth and may participate in neuron development and maturation during brain development. Mediates negative regulation of insulin receptor signaling through PTPN6. Inactivates SSTR3 receptor function following heterodimerization. {ECO:0000269|PubMed:15231824, ECO:0000269|PubMed:18653781, ECO:0000269|PubMed:19434240, ECO:0000269|PubMed:22495673, ECO:0000269|PubMed:22932785}.; . TISSUE SPECIFICITY: Expressed in both pancreatic alpha- and beta- cells (at protein level). Expressed at higher levels in the pancreas than other somatostatin receptors. Also expressed in the cerebrum and kidney and, in lesser amounts, in the jejunum, colon and liver. In the developing nervous system, expressed in the cortex where it is located in the preplate at early stages and is enriched in the outer part of the germinal zone at later stages. In the cerebellum, expressed in the deep part of the external granular layer at gestational week 19. This pattern persists until birth but disappears at adulthood. {ECO:0000269|PubMed:19434240, ECO:0000269|PubMed:22932785}.; unclassifiable (Anatomical System);amygdala;hypothalamus;bone;visual apparatus;kidney;germinal center;brain;retina; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.15020 0.27131 -0.359940251 28.93371078 16.95487 0.59727 SSTR3 0.0372243594214985 0.834028079187137 0.128747561391365 somatostatin receptor 3 FUNCTION: Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. {ECO:0000269|PubMed:1337145}.; . TISSUE SPECIFICITY: Brain, pituitary and pancreas. {ECO:0000269|PubMed:1337145}.; unclassifiable (Anatomical System);medulla oblongata;lymph node;ovary;islets of Langerhans;blood;thymus; superior cervical ganglion;uterus corpus;globus pallidus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.26681 0.19826 0.025760883 55.78556263 441.78532 4.37626 SSTR4 8.69093826267664e-05 0.330019447941214 0.669893642676159 somatostatin receptor 4 FUNCTION: Receptor for somatostatin-14. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. It is functionally coupled not only to inhibition of adenylate cyclase, but also to activation of both arachidonate release and mitogen-activated protein (MAP) kinase cascade. Mediates antiproliferative action of somatostatin in tumor cells.; . TISSUE SPECIFICITY: Specifically expressed in fetal and adult brain, lung tissue, stomach, and in lesser quantities in the kidney, pituitary and adrenals.; . . 0.08729 0.10515 -0.334253673 30.70299599 2053.65608 8.35262 SSTR5 0.0623344657131591 0.723207270792172 0.214458263494669 somatostatin receptor 5 FUNCTION: Receptor for somatostatin 28 and to a lesser extent for somatostatin-14. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. Increases cell growth inhibition activity of SSTR2 following heterodimerization. {ECO:0000269|PubMed:12072395, ECO:0000269|PubMed:7908405, ECO:0000269|PubMed:8078491, ECO:0000269|PubMed:8373420}.; . TISSUE SPECIFICITY: Adult pituitary gland, heart, small intestine, adrenal gland, cerebellum and fetal hypothalamus. No expression in fetal or adult kidney, liver, pancreas, uterus, spleen, lung, thyroid or ovary. {ECO:0000269|PubMed:12072395, ECO:0000269|PubMed:7908405, ECO:0000269|PubMed:8078491}.; cartilage;islets of Langerhans; superior cervical ganglion;globus pallidus;ciliary ganglion;skeletal muscle; 0.08476 . -0.394936437 27.02878037 770.72276 5.49307 SSTR5-AS1 . . . SSTR5 antisense RNA 1 . . . . . . . . . . . SSU72 0.606848849205337 0.384485576837317 0.00866557395734592 SSU72 homolog, RNA polymerase II CTD phosphatase FUNCTION: Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. Plays a role in pre-mRNA polyadenylation via its interaction with SYMPK. {ECO:0000269|PubMed:15659578, ECO:0000269|PubMed:20861839, ECO:0000269|PubMed:23070812}.; . . myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus;cerebellum; amygdala;whole brain;atrioventricular node; 0.14539 0.11809 -0.141298762 42.87567823 0.82029 0.01602 SSU72P1 . . . SSU72 pseudogene 1 . . . . . . . . . . . SSU72P2 . . . SSU72 pseudogene 2 . . . . . . . . . . . SSU72P3 . . . SSU72 pseudogene 3 . . . . . . . . . . . SSU72P4 . . . SSU72 pseudogene 4 . . . . . . . . . . . SSU72P5 . . . SSU72 pseudogene 5 . . . . . . . . . . . SSU72P6 . . . SSU72 pseudogene 6 . . . . . . . . . . . SSU72P7 . . . SSU72 pseudogene 7 . . . . . . . . . . . SSU72P8 . . . SSU72 pseudogene 8 . . . . . . . . . . . SSUH2 2.48997802703819e-08 0.151868773278921 0.848131201821299 ssu-2 homolog (C. elegans) . . TISSUE SPECIFICITY: Expressed in enterocytes of small and large intestinal mucosa (at protein level). Expressed in enterocytes, chromaffine and interstitial cells. {ECO:0000269|PubMed:20205943}.; . . 0.10834 . 0.532823122 80.96249115 347.2042 3.95074 SSX1 6.95390585589371e-28 1.74794183354809e-08 0.999999982520582 synovial sarcoma, X breakpoint 1 FUNCTION: Could act as a modulator of transcription.; . TISSUE SPECIFICITY: Expressed at high level in the testis. Expressed at low level in thyroid. Not detected in tonsil, colon, lung, spleen, prostate, kidney, striated and smooth muscles. Detected in rhabdomyosarcoma and fibrosarcoma cell lines. Not detected in mesenchymal and epithelial cell lines.; . . . . 0.284856336 71.40835103 87.24158 1.99482 SSX2 . . . synovial sarcoma, X breakpoint 2 FUNCTION: Could act as a modulator of transcription.; . TISSUE SPECIFICITY: Expressed at high level in the testis. Expressed at low level in thyroid. Not detected in tonsil, colon, lung, spleen, prostate, kidney, striated and smooth muscles. Detected in rhabdomyosarcoma and fibrosarcoma cell lines. Not detected in mesenchymal and epithelial cell lines.; bile duct;endometrium;liver;testis;skin; . 0.05223 . . . . . SSX2B . . . synovial sarcoma, X breakpoint 2B FUNCTION: Could act as a modulator of transcription.; . TISSUE SPECIFICITY: Expressed at high level in the testis. Expressed at low level in thyroid. Not detected in tonsil, colon, lung, spleen, prostate, kidney, striated and smooth muscles. Detected in rhabdomyosarcoma and fibrosarcoma cell lines. Not detected in mesenchymal and epithelial cell lines.; lung;liver;testis;skin; . 0.08325 . . . . . SSX2IP 0.000829858792208633 0.998517710229647 0.000652430978144692 synovial sarcoma, X breakpoint 2 interacting protein FUNCTION: Belongs to an adhesion system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). May connect the nectin-afadin and E- cadherin-catenin system through alpha-actinin and may be involved in organization of the actin cytoskeleton at AJs through afadin and alpha-actinin (By similarity). Involved in cell movement: localizes at the leading edge of moving cells in response to PDGF and is required for the formation of the leading edge and the promotion of cell movement, possibly via activation of Rac signaling (By similarity). Acts as a centrosome maturation factor, probably by maintaining the integrity of the pericentriolar material and proper microtubule nucleation at mitotic spindle poles (PubMed:23816619). Involved in ciliogenesis (PubMed:24356449). It is required for targeted recruitement of the BBSome, CEP290, RAB8, and SSTR3 to the cilia (PubMed:24356449). {ECO:0000250|UniProtKB:Q8VC66, ECO:0000269|PubMed:23816619, ECO:0000269|PubMed:24356449}.; . TISSUE SPECIFICITY: Widely expressed, with the highest expression in brain, intermediate expression in kidney, testis, spinal cord, liver, heart, lung, skeletal muscle, ovary, fetal liver and fetal brain, and little to no expression in pancreas and spleen. All specific brain regions showed intermediate to high expression, with highest expression in amygdala. Also expressed in fetal tissues, mainly in liver and brain.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;bone;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;small intestine;heart;islets of Langerhans;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney; dorsal root ganglion;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;testis - interstitial;temporal lobe;pons;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.16673 0.12673 -0.690637458 15.12149092 25.8299 0.84121 SSX3 0.146323758317065 0.778345780424183 0.0753304612587525 synovial sarcoma, X breakpoint 3 FUNCTION: Could act as a modulator of transcription.; . . unclassifiable (Anatomical System);bile duct;endometrium;testis;skin;bone marrow; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.09655 0.08088 0.881944684 89.02453409 11.37943 0.41100 SSX4 0.443294513598317 0.455253468746689 0.101452017654994 synovial sarcoma, X breakpoint 4 FUNCTION: Could act as a modulator of transcription.; . . . . . 0.02813 . . . . SSX4B 0.47431959897204 0.440648193539196 0.085032207488764 synovial sarcoma, X breakpoint 4B FUNCTION: Could act as a modulator of transcription.; . . . . . 0.02813 . . 19.50073 0.66895 SSX5 2.33013753613682e-07 0.0819305880270432 0.918069178959203 synovial sarcoma, X breakpoint 5 FUNCTION: Could act as a modulator of transcription.; . . skin; superior cervical ganglion;temporal lobe;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.07135 0.07680 1.506587076 95.41165369 14.74383 0.53153 SSX6 . . . synovial sarcoma, X breakpoint 6 (pseudogene) FUNCTION: Could act as a modulator of transcription.; . . lung;bone;testis;skin; . 0.01464 . . . . . SSX7 7.6817804736366e-05 0.310502093036817 0.689421089158447 synovial sarcoma, X breakpoint 7 FUNCTION: Could act as a modulator of transcription.; . . . . 0.05055 . 0.77170517 87.00754895 401.83185 4.20394 SSX8 . . . synovial sarcoma, X breakpoint 8 FUNCTION: Could act as a modulator of transcription.; . . . . . . . . . . SSX9 . . . synovial sarcoma, X breakpoint 9 FUNCTION: Could act as a modulator of transcription.; . . . . . . . . . . SSXP1 . . . SSX family pseudogene 1 . . . . . . . . . . . SSXP3 . . . SSX family pseudogene 3 . . . . . . . . . . . SSXP4 . . . SSX family pseudogene 4 . . . . . . . . . . . SSXP5 . . . SSX family pseudogene 5 . . . . . . . . . . . SSXP6 . . . SSX family pseudogene 6 . . . . . . . . . . . SSXP7 . . . SSX family pseudogene 7 . . . . . . . . . . . SSXP8 . . . SSX family pseudogene 8 . . . . . . . . . . . SSXP9 . . . SSX family pseudogene 9 . . . . . . . . . . . SSXP10 . . . SSX family pseudogene 10 . . . . . . . . . . . ST2 . . . suppression of tumorigenicity 2 . . . . . . . . . . . ST3 . . . suppression of tumorigenicity 3 . . . . . . . . . . . ST3GAL1 0.59355924559558 0.404393836134328 0.00204691827009183 ST3 beta-galactoside alpha-2,3-sialyltransferase 1 FUNCTION: It may be responsible for the synthesis of the sequence NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- found on sugar chains O- linked to Thr or Ser and also as a terminal sequence on certain gangliosides. SIAT4A and SIAT4B sialylate the same acceptor substrates but exhibit different Km values.; . TISSUE SPECIFICITY: Expressed in several tissues. Highest expression in lung, liver, skeletal muscle, kidney, pancreas, spleen and placenta.; unclassifiable (Anatomical System);tongue;colon;blood;skin;skeletal muscle;retina;bone marrow;breast;prostate;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;cervix;head and neck;spleen;germinal center;kidney;brain;mammary gland; . 0.12911 0.14444 0.286674996 71.49681529 215.8106 3.17089 ST3GAL1P1 . . . ST3 beta-galactoside alpha-2,3-sialyltransferase 1 pseudogene 1 . . . . . . . . . . . ST3GAL2 0.947101298960924 0.0528622934354107 3.64076036655423e-05 ST3 beta-galactoside alpha-2,3-sialyltransferase 2 FUNCTION: It may be responsible for the synthesis of the sequence NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- found in terminal carbohydrate groups of certain glycoproteins, oligosaccharides and glycolipids. SIAT4A and SIAT4B sialylate the same acceptor substrates but exhibit different Km values.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle and heart and to a much lesser extent in brain, placenta, liver and pancreas. Scarcely detectable in lung and kidney. {ECO:0000269|PubMed:8920913, ECO:0000269|PubMed:9266697}.; unclassifiable (Anatomical System);ovary;cartilage;colon;blood;parathyroid;lens;skin;lung;placenta;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.22407 0.13988 -0.359940251 28.93371078 57.31598 1.52548 ST3GAL3 0.573989459299218 0.425910763919929 9.9776780852986e-05 ST3 beta-galactoside alpha-2,3-sialyltransferase 3 FUNCTION: Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta- 1,4-GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- or NeuAc-alpha- 2,3-Gal-beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. The highest activity is toward Gal-beta-1,3-GlcNAc and the lowest toward Gal-beta-1,3- GalNAc (By similarity). {ECO:0000250}.; DISEASE: Mental retardation, autosomal recessive 12 (MRT12) [MIM:611090]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:21907012}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epileptic encephalopathy, early infantile, 15 (EIEE15) [MIM:615006]: A form of epilepsy that manifests in the neonatal or the early infantile period as severely impaired cognitive and motor development, due to recurrent clinical seizures or prominent interictal epileptiform discharges. Patients develop infantile spasms, mainly of the flexor type, between 3 and 7 months of age, which are accompanied by hypsarrhythmia on EEG. Other features include poor eye contact, hypotonia, primitive reflexes, and irritability. Seizures evolve clinically to Lennox-Gastaut syndrome. {ECO:0000269|PubMed:23252400}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in adult skeletal muscle and in all fetal tissues examined and to a much lesser extent in placenta, lung and liver.; medulla oblongata;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;thyroid;pituitary gland;iris;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;pineal body;adrenal cortex;lens;skeletal muscle;lung;placenta;macula lutea;liver;head and neck;kidney;stomach; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.35092 0.10596 -0.358119787 29.16371786 34.04143 1.04396 ST3GAL4 0.439048570873843 0.559542989895477 0.00140843923068005 ST3 beta-galactoside alpha-2,3-sialyltransferase 4 FUNCTION: It may catalyze the formation of the NeuAc-alpha-2,3- Gal-beta-1,3-GalNAc- or NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. It may be involved in the biosynthesis of the sialyl Lewis X determinant. Also acts on the corresponding 1,3- galactosyl derivative. {ECO:0000269|PubMed:8611500}.; . TISSUE SPECIFICITY: Highly expressed in adult placenta, ovary and testes.; smooth muscle;ovary;sympathetic chain;colon;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;cerebral cortex;synovium;bone;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;bile duct;breast;pancreas;lung;placenta;liver;alveolus;spleen;cervix;kidney;stomach;aorta; superior cervical ganglion;adrenal gland;adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.07020 0.14497 0.038710339 56.92380278 29.68834 0.94761 ST3GAL4-AS1 . . . ST3GAL4 antisense RNA 1 (head to head) . . . . . . . . . . . ST3GAL5 0.0278549097052091 0.960860570007715 0.0112845202870756 ST3 beta-galactoside alpha-2,3-sialyltransferase 5 FUNCTION: Catalyzes the formation of ganglioside GM3 (alpha-N- acetylneuraminyl-2,3-beta-D-galactosyl-1, 4-beta-D- glucosylceramide). {ECO:0000269|PubMed:16934889}.; DISEASE: Amish infantile epilepsy syndrome (AIES) [MIM:609056]: An autosomal recessive, infantile-onset symptomatic epilepsy associated with developmental stagnation and blindness. {ECO:0000269|PubMed:15502825}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. High expression in brain, skeletal muscle, placenta, and testis.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pineal body;muscle;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney; whole brain;amygdala;superior cervical ganglion;medulla oblongata;thalamus;adrenal gland;prefrontal cortex;caudate nucleus;pons;skeletal muscle;cingulate cortex;parietal lobe; 0.11117 0.15284 -0.381986487 27.68931352 1071.60517 6.27624 ST3GAL5-AS1 . . . ST3GAL5 antisense RNA 1 (head to head) . . . . . . . . . . . ST3GAL5P1 . . . ST3 beta-galactoside alpha-2,3-sialyltransferase 5 pseudogene 1 . . . . . . . . . . . ST3GAL6 0.00106167207338745 0.949969415783849 0.0489689121427642 ST3 beta-galactoside alpha-2,3-sialyltransferase 6 FUNCTION: Involved in the synthesis of sialyl-paragloboside, a precursor of sialyl-Lewis X determinant. Has a alpha-2,3- sialyltransferase activity toward Gal-beta1,4-GlcNAc structure on glycoproteins and glycolipids. Has a restricted substrate specificity, it utilizes Gal-beta1,4-GlcNAc on glycoproteins, and neolactotetraosylceramide and neolactohexaosylceramide, but not lactotetraosylceramide, lactosylceramide or asialo-GM1.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;vein;skin;retina;uterus;prostate;larynx;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;pharynx;blood;skeletal muscle;lung;cornea;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;spinal cord;adrenal cortex;ciliary ganglion;trigeminal ganglion;skeletal muscle;skin; 0.46837 0.14896 -0.203796826 38.81811748 530.44612 4.70139 ST3GAL6-AS1 . . . ST3GAL6 antisense RNA 1 . . . . . . . . . . . ST5 0.99998977925639 1.02207436043036e-05 6.13126780041646e-15 suppression of tumorigenicity 5 FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP- bound form. May be involved in cytoskeletal organization and tumorogenicity. Isoform 1 seems to be involved in a signaling transduction pathway leading to activation of MAPK1/ERK2. Isoform 3 may block ERK2 activation stimulated by ABL1. Isoform 3 may alter cell morphology and cell growth. {ECO:0000269|PubMed:10229203, ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:9632734}.; . TISSUE SPECIFICITY: Widely expressed with the exception of peripheral blood lymphocytes. Isoform 1 is expressed in several epithelial and fibroblast (including tumorigenic) but absent in lymphoid cell lines (at protein level). Isoform 3 is expressed in primary cell or weakly tumorigenic but not in tumorigenic cell lines (at protein level). {ECO:0000269|PubMed:10229203}.; smooth muscle;ovary;salivary gland;colon;fovea centralis;choroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach; uterus;superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion; 0.34085 0.14520 -0.723828344 14.26043878 4280.14983 13.00986 ST6GAL1 0.814435677774412 0.184613202301572 0.000951119924015963 ST6 beta-galactosamide alpha-2,6-sialyltranferase 1 FUNCTION: Transfers sialic acid from CMP-sialic acid to galactose- containing acceptor substrates. {ECO:0000269|PubMed:21081508, ECO:0000269|PubMed:23999306}.; . . lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;substantia nigra;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; fetal liver;liver; 0.66891 0.16291 -0.780646273 12.77423921 17.32337 0.60850 ST6GAL2 0.0149364382080836 0.957674132421656 0.0273894293702599 ST6 beta-galactosamide alpha-2,6-sialyltranferase 2 FUNCTION: Transfers sialic acid from the donor of substrate CMP- sialic acid to galactose containing acceptor substrates. Has alpha-2,6-sialyltransferase activity toward oligosaccharides that have the Gal-beta-1,4-GlcNAc sequence at the non-reducing end of their carbohydrate groups, but it has weak or no activities toward glycoproteins and glycolipids.; . TISSUE SPECIFICITY: Weakly expressed in some tissues, such as small intestine, colon and fetal brain. {ECO:0000269|PubMed:12235148, ECO:0000269|PubMed:12603328}.; unclassifiable (Anatomical System);cartilage;ovary;colon;uterus;prostate;whole body;bone;thyroid;visual apparatus;liver;testis;spleen;kidney;brain;artery;aorta; . 0.18144 0.11225 1.732552414 96.59707478 2035.95057 8.31179 ST6GAL2-IT1 . . . ST6GAL2 intronic transcript 1 . . . . . . . . . . . ST6GALNAC1 2.24205320873445e-11 0.0672312243923116 0.932768775585268 ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1 . . . unclassifiable (Anatomical System);amygdala;cartilage;heart;colon;skin;skeletal muscle;bile duct;uterus;pancreas;prostate;lung;endometrium;larynx;placenta;bone;hippocampus;liver;testis;cervix;head and neck;brain;stomach; trachea;globus pallidus; 0.11371 0.10503 0.159856957 64.91507431 150.75936 2.68237 ST6GALNAC2 4.43095165859324e-08 0.207455842155814 0.792544113534669 ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 . . TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, kidney, placenta, lung and leukocytes.; ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;whole body;endometrium;larynx;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;skeletal muscle;breast;pancreas;lung;internal ear;placenta;macula lutea;head and neck;mammary gland; dorsal root ganglion;testis - interstitial;superior cervical ganglion;olfactory bulb;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.06959 0.12752 7.61E-05 53.98089172 91.92267 2.06284 ST6GALNAC2P1 . . . ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 pseudogene 1 . . . . . . . . . . . ST6GALNAC3 0.178471681213117 0.808939094418475 0.012589224368408 ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3 FUNCTION: Involved in the biosynthesis of ganglioside GD1A from GM1B. Transfers CMP-NeuAc with an alpha-2,6-linkage to GalNAc residue on NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc of glycoproteins and glycolipids. ST6GalNAcIII prefers glycolipids to glycoproteins (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);whole body;cartilage;ovary;synovium;pineal body;thyroid;placenta;hippocampus;parathyroid;brain;skin; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.29123 0.10388 -0.159704656 41.90846898 3618.59038 11.66169 ST6GALNAC4 0.00507720489655408 0.887720397654868 0.107202397448578 ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4 FUNCTION: Involved in the biosynthesis of ganglioside GD1A from GM1B. Transfers CMP-NeuAc with an alpha-2,6-linkage to GalNAc residue on NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc of glycoproteins and glycolipids. Prefers glycoproteins to glycolipids (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;lung;placenta;macula lutea;duodenum;liver;cervix;spleen;kidney;mammary gland;stomach;thymus; superior cervical ganglion;heart;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15075 0.11395 -0.580403979 18.58928993 29.64267 0.94679 ST6GALNAC4P1 . . . ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4 pseudogene 1 . . . . . . . . . . . ST6GALNAC5 0.852521023463578 0.14696789367355 0.000511082862871655 ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5 FUNCTION: Involved in the biosynthesis of ganglioside GD1a from GM1b. It exhibits higher activity with glycolipids than with glycoproteins (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;whole body;frontal lobe;islets of Langerhans;visual apparatus;pituitary gland;alveolus;amniotic fluid;brain;pineal gland;mammary gland;bladder; . 0.52234 0.11255 -0.471992905 23.03609342 624.50667 5.04147 ST6GALNAC6 0.00205356014302079 0.912791918833428 0.0851545210235514 ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6 FUNCTION: Alpha-2,6-sialyltransferase involved in the synthesis of alpha-series gangliosides. Has activity toward GD1a, GT1b and GM1b. Has no activity toward glycoproteins. Responsible for the biosynthesis of DSGG (disialylgalactosylgloboside) from MSGG (monosialylgalactosylgloboside) in normal and malignant kidney. Participates in the synthesis of disialyl Lewis a (Le(a)). {ECO:0000269|PubMed:12668675, ECO:0000269|PubMed:17123352}.; . TISSUE SPECIFICITY: Expressed in kidney, in proximal tubule epithelial cells. Expressed in colon cell lines. {ECO:0000269|PubMed:12668675, ECO:0000269|PubMed:17123352}.; ovary;colon;substantia nigra;parathyroid;choroid;skin;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;bile duct;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.14025 0.09314 -1.023168368 7.944090587 40.49297 1.18780 ST7 0.998051871776655 0.00194812602154729 2.20179806300417e-09 suppression of tumorigenicity 7 FUNCTION: May act as a tumor suppressor. {ECO:0000269|PubMed:16474848}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in heart, liver and pancreas. {ECO:0000269|PubMed:10889047, ECO:0000269|PubMed:11279520}.; unclassifiable (Anatomical System);ovary;colon;fovea centralis;choroid;lens;skin;retina;bone marrow;prostate;optic nerve;whole body;lung;bone;placenta;macula lutea;liver;testis;cervix;spleen;kidney;germinal center;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;cerebellum; 0.18576 0.11467 -0.247889024 35.98726115 29.00341 0.92750 ST7-AS1 . . . ST7 antisense RNA 1 . . . . . . . . . . . ST7-AS2 . . . ST7 antisense RNA 2 . . . . . . . . . . . ST7-OT3 . . . ST7 overlapping transcript 3 . . . . . . . . . . . ST7-OT4 . . . ST7 overlapping transcript 4 . . . . . 0.10166 . . . 12.95902 0.47221 ST7L 1.94396958967683e-06 0.969887737008959 0.0301103190214513 suppression of tumorigenicity 7 like . . . smooth muscle;ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);trophoblast;heart;cartilage;islets of Langerhans;blood;lens;lung;epididymis;placenta;macula lutea;visual apparatus;liver;hypopharynx;head and neck;kidney;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion;parietal lobe; 0.31344 . 1.908972967 97.39325313 1731.11998 7.67838 ST8 . . . suppression of tumorigenicity 8 (ovarian) . . . . . . . . . . . ST8SIA1 0.211574643725732 0.779418511502102 0.00900684477216617 ST8 alpha-N-acetylneuraminate alpha-2,8-sialyltransferase 1 FUNCTION: Involved in the production of gangliosides GD3 and GT3 from GM3; gangliosides are a subfamily of complex glycosphinglolipds that contain one or more residues of sialic acid. {ECO:0000269|PubMed:7937974, ECO:0000269|PubMed:8058740, ECO:0000269|PubMed:8195250, ECO:0000269|PubMed:8631981}.; . TISSUE SPECIFICITY: Strongly expressed in melanoma cell lines, adult and fetal brain and to a lesser extent in adult and fetal lung. {ECO:0000269|PubMed:7937974, ECO:0000269|PubMed:8631981}.; unclassifiable (Anatomical System);heart;ovary;parathyroid;skin;retina;breast;whole body;lung;frontal lobe;bone;hippocampus;testis;brain; superior cervical ganglion;prefrontal cortex;trigeminal ganglion; 0.16187 0.14714 0.106667882 61.73036093 29.99859 0.95895 ST8SIA2 0.512756894405073 0.483343599735049 0.00389950585987835 ST8 alpha-N-acetylneuraminate alpha-2,8-sialyltransferase 2 FUNCTION: May transfer sialic acid through alpha-2,8-linkages to the alpha-2,3-linked and alpha-2,6-linked sialic acid of N-linked oligosaccharides of glycoproteins and may be involved in PSA (polysialic acid) expression.; . TISSUE SPECIFICITY: Highly expressed in fetal brain, kidney and heart and to a much lesser extent in adult heart and thymus.; unclassifiable (Anatomical System);frontal lobe;brain; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.39163 0.26810 -0.424258538 25.56027365 71.81909 1.76447 ST8SIA3 0.963677659153812 0.0362523135268425 7.00273193457947e-05 ST8 alpha-N-acetylneuraminate alpha-2,8-sialyltransferase 3 FUNCTION: Catalyzes the transfer of sialic acid from a CMP-linked sialic acid donor onto the terminal sialic acid of an acceptor through alpha-2,8-linkages. Is active with alpha-2,3-linked, alpha-2,6-linked and alpha-2,8-linked sialic acid of N-linked oligosaccharides of glycoproteins and glycolipids. Displays preference for substrates with alpha-2,3-linked terminal sialic acid. It can form polysialic acid in vitro directly on alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid. {ECO:0000269|PubMed:10766765, ECO:0000269|PubMed:26192331, ECO:0000269|PubMed:9826427}.; . TISSUE SPECIFICITY: Expressed in fetal and adult brain and fetal liver. {ECO:0000269|PubMed:9826427}.; unclassifiable (Anatomical System);lung;cerebral cortex;colon;pineal gland; appendix;trigeminal ganglion;skeletal muscle; 0.47947 0.10656 -0.293801652 32.93819297 2541.39756 9.41464 ST8SIA4 0.675929296308764 0.323087572810319 0.000983130880917615 ST8 alpha-N-acetylneuraminate alpha-2,8-sialyltransferase 4 FUNCTION: Catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid (PSA), which is present on the embryonic neural cell adhesion molecule (N-CAM), necessary for plasticity of neural cells.; . TISSUE SPECIFICITY: Highly expressed in fetal brain, lung and kidney and in adult heart, spleen and thymus. Present to a lesser extent in adult brain, placenta, lung, large and small intestine and peripheral blood leukocytes.; unclassifiable (Anatomical System);cartilage;blood;skeletal muscle;bone marrow;breast;uterus;bile duct;pancreas;whole body;lung;endometrium;thyroid;placenta;hypopharynx;testis;head and neck;germinal center;kidney;brain;mammary gland;aorta;peripheral nerve; superior cervical ganglion;trigeminal ganglion; 0.16759 0.11031 -0.339715008 30.06605331 21.20035 0.71609 ST8SIA5 0.0183928498018628 0.961115550518063 0.0204915996800737 ST8 alpha-N-acetylneuraminate alpha-2,8-sialyltransferase 5 FUNCTION: May be involved in the synthesis of gangliosides GD1c, GT1a, GQ1b and GT3 from GD1a, GT1b, GM1b and GD3 respectively. {ECO:0000269|PubMed:9199191}.; . TISSUE SPECIFICITY: Expressed in fetal and adult brain, adult heart and skeletal muscle. {ECO:0000269|PubMed:9199191}.; unclassifiable (Anatomical System);lung;frontal lobe;ovary;placenta;visual apparatus;adrenal cortex;parathyroid;brain; superior cervical ganglion;adrenal gland;parietal lobe; 0.17614 0.10140 -0.203796826 38.81811748 86.55471 1.98709 ST8SIA6 2.70748990652578e-08 0.0854050955710633 0.914594877354038 ST8 alpha-N-acetylneuraminate alpha-2,8-sialyltransferase 6 FUNCTION: Prefers O-glycans to N-glycans or glycolipids as acceptor substrates. The minimal acceptor substrate is the NeuAc- alpha-2,3(6)-Gal sequence at the non-reducing end of their carbohydrate groups (By similarity). {ECO:0000250}.; . . . . 0.07431 0.11513 0.196671391 67.19155461 421.51421 4.28656 ST8SIA6-AS1 . . . ST8SIA6 antisense RNA 1 . . . . . . . . . . . ST11 . . . suppression of tumorigenicity 11 (pancreas) . . . . . . . . . . . ST13 0.659423623669509 0.340528970759347 4.74055711435786e-05 suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) FUNCTION: One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;sympathetic chain;skin;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;heart;cartilage;pineal body;urinary;adrenal cortex;blood;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;liver;spleen;mammary gland;colon;parathyroid;uterus;whole body;atrium;oesophagus;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;aorta;stomach;thymus; amygdala;superior cervical ganglion;thalamus;occipital lobe;medulla oblongata;hypothalamus;spinal cord;globus pallidus;pons;caudate nucleus;kidney;parietal lobe; . 0.29632 0.371224249 75.12384996 298.3425 3.68340 ST13P1 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 1 . . . . . . . . . . . ST13P2 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 2 . . . . . . . . . . . ST13P3 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 3 . . . . . . . . . . . ST13P4 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 4 . . TISSUE SPECIFICITY: Highly expressed in bone marrow and weakly in placenta, pancreas, heart and HeLa cell line. {ECO:0000269|PubMed:12079276}.; . . . 0.29632 . . . . ST13P5 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 5 . . . . . 0.09342 0.08986 . . . . ST13P6 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 6 . . . . . . . . . . . ST13P7 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 7 . . . . . . 0.29632 . . . . ST13P8 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 8 . . . . . . . . . . . ST13P9 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 9 . . . . . . . . . . . ST13P10 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 10 . . . . . . . . . . . ST13P11 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 11 . . . . . . . . . . . ST13P12 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 12 . . . . . . . . . . . ST13P13 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 13 . . . . . . . . . . . ST13P14 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 14 . . . . . . . . . . . ST13P15 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 15 . . . . . . . . . . . ST13P16 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 16 . . . . . . . . . . . ST13P17 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 17 . . . . . . . . . . . ST13P18 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 18 . . . . . . . . . . . ST13P19 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 19 . . . . . . . . . . . ST13P20 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 20 . . . . . . . . . . . ST13P21 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 21 . . . . . . . . . . . ST13P22 . . . suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) pseudogene 22 . . . . . . . . . . . ST14 0.85267655285458 0.147322585571004 8.61574415640199e-07 suppression of tumorigenicity 14 FUNCTION: Degrades extracellular matrix. Proposed to play a role in breast cancer invasion and metastasis. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site. Involved in the terminal differentiation of keratinocytes through prostasin (PRSS8) activation and filaggrin (FLG) processing. {ECO:0000269|PubMed:18843291}.; DISEASE: Ichthyosis, congenital, autosomal recessive 11 (ARCI11) [MIM:602400]: A form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non-bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs. {ECO:0000269|PubMed:17273967, ECO:0000269|PubMed:18843291}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;parathyroid;skin;uterus;prostate;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;urinary;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; atrioventricular node;trigeminal ganglion; 0.43903 0.33644 -0.347208386 29.59424393 1268.8342 6.71293 ST18 0.999009547757882 0.000990452224790087 1.73282888931815e-11 suppression of tumorigenicity 18, zinc finger FUNCTION: Repressor that binds to DNA sequences containing a bipartite element consisting of a direct repeat of the sequence 5'-AAAGTTT-3' separated by 2-9 nucleotides. Represses basal transcription activity from target promoters (By similarity). Inhibits colony formation in cultured breast cancer cells. {ECO:0000250, ECO:0000269|PubMed:15489893}.; . TISSUE SPECIFICITY: Detected at low levels in heart, liver, kidney, skeletal muscle, pancreas, testis, ovary and prostate. Detected at even lower levels in mammary epithelial cells and breast cancer cells. {ECO:0000269|PubMed:15489893}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;spinal cord;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;optic nerve;lung;placenta;macula lutea;brain;aorta;peripheral nerve; amygdala;thalamus;medulla oblongata;superior cervical ganglion;occipital lobe;cerebellum peduncles;hypothalamus;spinal cord;pons;caudate nucleus;prefrontal cortex;parietal lobe;cingulate cortex;cerebellum; 0.47084 0.11285 -0.613589782 17.49823071 543.59199 4.74421 ST20 0.113592063518993 0.601070721668005 0.285337214813001 suppressor of tumorigenicity 20 FUNCTION: May act as a tumor suppressor. Promotes apoptosis of cancer cells. {ECO:0000269|PubMed:11857354}.; . . . . 0.04388 . 0.746027844 86.40599198 2266.99377 8.80042 ST20-AS1 . . . ST20 antisense RNA 1 . . . . . . . . . . . ST20-MTHFS 0.0363712829836564 0.831502817316822 0.132125899699522 ST20-MTHFS readthrough . . . . . . . . . 2.59039 0.09496 STAB1 2.79798765369336e-25 0.999997818126492 2.18187350760166e-06 stabilin 1 FUNCTION: Acts as a scavenger receptor for acetylated low density lipoprotein. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. When inhibited in endothelial tube formation assays, there is a marked decrease in cell-cell interactions, suggesting a role in angiogenesis. Involved in the delivery of newly synthesized CHID1/SI-CLP from the biosynthetic compartment to the endosomal/lysosomal system. {ECO:0000269|PubMed:12077138, ECO:0000269|PubMed:16357325}.; . TISSUE SPECIFICITY: High levels found in spleen, lymph node, liver and placenta. Also expressed in endothelial cells. {ECO:0000269|PubMed:11829752, ECO:0000269|PubMed:12077138}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; . 0.27083 0.14313 -4.124226635 0.159235669 3007.38266 10.41148 STAB2 4.17567584164662e-28 0.999998289192149 1.71080785136717e-06 stabilin 2 FUNCTION: Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Hyaluronan receptor that binds to and mediates endocytosis of hyaluronic acid (HA). Acts also, in different species, as a primary systemic scavenger receptor for heparin (Hep), chondroitin sulfate (CS), dermatan sulfate (DS), nonglycosaminoglycan (GAG), acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides and advanced glycation end products (AGE). May serve to maintain tissue integrity by supporting extracellular matrix turnover or it may contribute to maintaining fluidity of bodily liquids by resorption of hyaluronan. Counter receptor which plays an important role in lymphocyte recruitment in the hepatic vasculature. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. The proteolytically processed 190 kDa form also functions as an endocytosis receptor for heparin internalisation as well as HA and CS. {ECO:0000269|PubMed:12077138, ECO:0000269|PubMed:12473645, ECO:0000269|PubMed:15208308, ECO:0000269|PubMed:15572036, ECO:0000269|PubMed:17145755, ECO:0000269|PubMed:17675564, ECO:0000269|PubMed:17962816, ECO:0000269|PubMed:18230608, ECO:0000269|PubMed:18434317, ECO:0000269|PubMed:18573870, ECO:0000269|PubMed:19359419}.; . TISSUE SPECIFICITY: Highly expressed in sinusoidal endothelial cells of liver, spleen and lymph nodes. Also expressed in non SEC- cells such as HMDMs (monocyte-derivedmacrophages), HAMs (T-cell leukemia virus type 1-associated myelopathy), and several macrophage cell line. {ECO:0000269|PubMed:11829752, ECO:0000269|PubMed:12077138, ECO:0000269|PubMed:12473645, ECO:0000269|PubMed:12626425, ECO:0000269|PubMed:17675564, ECO:0000269|PubMed:17962816}.; unclassifiable (Anatomical System);heart;cartilage;skin;uterus;pancreas;prostate;lung;placenta;liver;testis;spleen;kidney;mammary gland; dorsal root ganglion;medulla oblongata;superior cervical ganglion;occipital lobe;atrioventricular node;skeletal muscle;skin;subthalamic nucleus;appendix;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.08152 . -2.679454516 0.719509318 3962.9588 12.45220 STAC 0.0107102692074456 0.979842946748801 0.00944678404375346 SH3 and cysteine rich domain FUNCTION: Probably involved in a neuron-specific signal transduction.; . . unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;fovea centralis;skin;uterus;breast;prostate;whole body;lung;placenta;macula lutea;visual apparatus;testis;spinal ganglion;brain;peripheral nerve; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.41776 0.09312 -0.178111357 40.44585987 471.73473 4.49527 STAC2 1.66040366548464e-05 0.871297263415428 0.128686132547917 SH3 and cysteine rich domain 2 . . . unclassifiable (Anatomical System);fovea centralis;choroid;lens;retina;breast;prostate;optic nerve;frontal lobe;endometrium;bone;macula lutea;iris;kidney;brain; . 0.25360 0.10406 -0.977252525 8.799245105 52.09893 1.42660 STAC3 0.00487830161425738 0.989072823022867 0.00604887536287594 SH3 and cysteine rich domain 3 FUNCTION: In skeletal muscles contraction, may play a role in neuromuscular synaptic transmission. {ECO:0000269|PubMed:23736855}.; DISEASE: Native American myopathy (NAM) [MIM:255995]: A disease characterized by congenital weakness and arthrogryposis, cleft palate, ptosis, short stature, kyphoscoliosis, talipes deformities, and susceptibility to malignant hyperthermia provoked by anesthesia. {ECO:0000269|PubMed:23736855}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;muscle;blood;parathyroid;fovea centralis;choroid;lens;skeletal muscle;bone marrow;retina;optic nerve;lung;placenta;macula lutea;testis; superior cervical ganglion;tongue;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.16182 0.10482 -0.137658575 43.57159707 50.70761 1.40292 STAG1 0.999999910022904 8.99770962298449e-08 1.22223053756462e-20 stromal antigen 1 FUNCTION: Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.; . . ovary;sympathetic chain;adrenal medulla;colon;parathyroid;vein;skin;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;iris;testis;germinal center;brain;pineal gland;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; . 0.84236 0.14093 -1.043396569 7.71408351 541.07775 4.73759 STAG2 0.999999812829939 1.87170060751012e-07 8.78470450056681e-18 stromal antigen 2 FUNCTION: Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. {ECO:0000269|PubMed:12034751}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;endometrium;thyroid;testis;dura mater;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;oral cavity;pharynx;blood;lens;skeletal muscle;breast;pancreas;pia mater;lung;cornea;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; uterus;superior cervical ganglion;olfactory bulb;thyroid;white blood cells;ciliary ganglion;whole blood; 0.70349 . -0.626318434 17.03231894 8.69293 0.31922 STAG3 1.10348940584416e-06 0.999997880735796 1.01577479791224e-06 stromal antigen 3 FUNCTION: Meiosis specific component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The meiosis- specific cohesin complex probably replaces mitosis specific cohesin complex when it dissociates from chromatin during prophase I. {ECO:0000250|UniProtKB:O70576}.; DISEASE: Premature ovarian failure 8 (POF8) [MIM:615723]: An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol. {ECO:0000269|PubMed:24597867, ECO:0000303|PubMed:22428046}. Note=The disease is caused by mutations affecting the gene represented in this entry. A homozygous deletion in STAG3 predicted to result in frameshift and premature truncation, has been shown to be the cause of premature ovarian failure in a large consanguineous family. {ECO:0000269|PubMed:24597867}.; TISSUE SPECIFICITY: Testis specific.; ovary;parathyroid;fovea centralis;choroid;retina;bone marrow;prostate;optic nerve;ganglion;frontal lobe;larynx;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;lung;placenta;hippocampus;macula lutea;liver;spleen;head and neck;kidney;mammary gland;aorta;cerebellum; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;testis;ciliary ganglion;pons; 0.10558 0.11642 -1.102280959 6.912007549 421.44611 4.28597 STAG3L1 . . . stromal antigen 3-like 1 (pseudogene) . . . medulla oblongata;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;frontal lobe;endometrium;larynx;thyroid;bone;testis;germinal center;bladder;pineal gland;brain;gall bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;mesenchyma;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; . . . . . . . STAG3L2 . . . stromal antigen 3-like 2 (pseudogene) . . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;bladder;brain;pineal gland;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; . . . . . . . STAG3L3 . . . stromal antigen 3-like 3 (pseudogene) . . . medulla oblongata;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;frontal lobe;thyroid;testis;germinal center;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;pharynx;blood;breast;lung;cornea;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; . . 0.13021 . . . . STAG3L4 . . . stromal antigen 3-like 4 (pseudogene) . . . ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;blood;skeletal muscle;lung;nasopharynx;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12248 . . . . . STAG3L5P . . . stromal antigen 3-like 5 pseudogene . . . . . . . . . . . STAG3L5P-PVRIG2P-PILRB . . . STAG3L5P-PVRIG2P-PILRB readthrough . . . . . . . . . . . STAM 0.902578080850864 0.0974148386811539 7.08046798233093e-06 signal transducing adaptor molecule FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:8780729}.; . . 0.30611 0.16485 -0.488577883 22.64685067 62.58373 1.61763 STAM-AS1 . . . STAM antisense RNA 1 (head to head) . . . . . . . . . . . STAM2 0.034504985570748 0.963803382516297 0.00169163191295455 signal transducing adaptor molecule 2 FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10899310}.; medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;stomach;aorta; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;appendix;testis;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.51281 0.23414 -0.381986487 27.68931352 150.35228 2.67578 STAMBP 0.00143027314024062 0.991402751050275 0.00716697580948426 STAM binding protein FUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'- linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. Has a key role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is required for efficient EGFR degradation but not for its internalization (By similarity). Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways. {ECO:0000250, ECO:0000269|PubMed:10383417, ECO:0000269|PubMed:11483516, ECO:0000269|PubMed:15314065, ECO:0000269|PubMed:17261583, ECO:0000269|PubMed:23542699}.; DISEASE: Microcephaly-capillary malformation syndrome (MICCAP) [MIM:614261]: A congenital disorder characterized by severe progressive microcephaly, early-onset refractory epilepsy, profound developmental delay, and multiple small capillary malformations spread diffusely on the body. Additional more variable features include dysmorphic facial features, distal limb abnormalities, and mild heart defects. {ECO:0000269|PubMed:23542699}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;urinary;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;hypothalamus;spinal cord;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.19894 0.12909 0.040529541 57.15380986 35.22539 1.06633 STAMBPL1 1.93494634741509e-05 0.972652144853435 0.0273285056830904 STAM binding protein like 1 FUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'- linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains. {ECO:0000269|PubMed:18758443}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12810066}.; . . 0.12681 0.09861 0.042348793 57.31304553 565.62006 4.83113 STAP1 0.000129550414834948 0.846504647131355 0.15336580245381 signal transducing adaptor family member 1 FUNCTION: In BCR signaling, appears to function as a docking protein acting downstream of TEC and participates in a positive feedback loop by increasing the activity of TEC. {ECO:0000269|PubMed:10518561}.; . . unclassifiable (Anatomical System);prostate;lymph node;cartilage;kidney;germinal center;brain;tonsil;bone marrow; superior cervical ganglion; 0.66261 0.09760 -0.582225231 18.44184949 42.83661 1.24007 STAP2 1.62685084919042e-13 0.00728645997628846 0.992713540023549 signal transducing adaptor family member 2 FUNCTION: Substrate of protein kinase PTK6. May play a regulatory role in the acute-phase response in systemic inflammation and may modulate STAT3 activity. {ECO:0000269|PubMed:10980601}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10980601, ECO:0000269|PubMed:12540842}.; unclassifiable (Anatomical System);heart;tongue;colon;parathyroid;skin;bile duct;prostate;optic nerve;whole body;lung;endometrium;visual apparatus;liver;head and neck;kidney;brain;mammary gland;stomach; prostate;superior cervical ganglion;liver;pons;trigeminal ganglion; 0.10556 . -0.44448505 24.46331682 74.07762 1.79793 STAR 3.07154052744717e-07 0.17759204640652 0.822407646439427 steroidogenic acute regulatory protein FUNCTION: Plays a key role in steroid hormone synthesis by enhancing the metabolism of cholesterol into pregnenolone. Mediates the transfer of cholesterol from the outer mitochondrial membrane to the inner mitochondrial membrane where it is cleaved to pregnenolone.; . TISSUE SPECIFICITY: Expressed in gonads, adrenal cortex and kidney.; unclassifiable (Anatomical System);medulla oblongata;lung;whole body;ovary;endometrium;adrenal gland;hypothalamus;placenta;adrenal cortex;testis;kidney;brain;mammary gland;skeletal muscle; thalamus;testis - interstitial;ovary;testis - seminiferous tubule;adrenal gland;adrenal cortex;testis;trigeminal ganglion; 0.24291 0.43038 -0.115612493 45.12856806 60.38731 1.57977 STARD3 0.149477765017096 0.850370299255361 0.000151935727543061 StAR related lipid transfer domain containing 3 FUNCTION: Binds and transports cholesterol. Promotes steroidogenesis in placenta and brain.; . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.14149 0.15183 -0.244249595 36.17008728 5346.25355 15.10288 STARD3NL 0.00554582817086751 0.897468863233151 0.0969853085959819 STARD3 N-terminal like . . . medulla oblongata;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;atrium;whole body;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta;peripheral nerve; whole brain;amygdala;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node; 0.30747 0.14229 -0.207437529 38.2814343 7.98594 0.29324 STARD4 2.95656598761803e-07 0.173957488365896 0.826042215977505 StAR related lipid transfer domain containing 4 FUNCTION: May be involved in the intracellular transport of sterols or other lipids. May bind cholesterol or other sterols (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);amygdala;hypothalamus;sympathetic chain;blood;skeletal muscle;pancreas;prostate;lung;frontal lobe;liver;testis;germinal center; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.12935 0.12152 -0.295622497 32.61972163 25.69887 0.83663 STARD4-AS1 . . . STARD4 antisense RNA 1 . . . . . . . . . . . STARD5 0.0615971183814048 0.922254113231713 0.0161487683868819 StAR related lipid transfer domain containing 5 FUNCTION: May be involved in the intracellular transport of sterols or other lipids. May bind cholesterol or other sterols (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);smooth muscle;cartilage;heart;colon;blood;parathyroid;skin;skeletal muscle;uterus;prostate;lung;bone;placenta;liver;spleen;germinal center;brain;stomach; liver;pons; 0.06378 0.11176 0.415317661 76.81056853 139.42694 2.57499 STARD6 0.0263351617026343 0.919378374903283 0.0542864633940828 StAR related lipid transfer domain containing 6 FUNCTION: May be involved in the intracellular transport of sterols or other lipids. May bind cholesterol or other sterols (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System); testis - interstitial; 0.05768 0.06355 0.948089677 89.95635763 528.36003 4.69091 STARD7 0.927709615692812 0.0722102106859447 8.01736212436637e-05 StAR related lipid transfer domain containing 7 . . . myocardium;lymphoreticular;ovary;umbilical cord;skin;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;oral cavity;muscle;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;thymus; amygdala;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;spinal cord;caudate nucleus;pons;skeletal muscle;kidney;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.30488 0.11874 -0.049474214 50.01179523 894.19608 5.82904 STARD7-AS1 . . . STARD7 antisense RNA 1 . . . . . . . . . . . STARD8 0.0358308690371062 0.962571631810628 0.00159749915226617 StAR related lipid transfer domain containing 8 FUNCTION: Accelerates GTPase activity of RHOA and CDC42, but not RAC1. Stimulates the hydrolysis of phosphatidylinositol 4,5- bisphosphate by PLCD1. {ECO:0000269|PubMed:17976533}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in kidney, lung and placenta. {ECO:0000269|PubMed:17297465}.; unclassifiable (Anatomical System);uterus;prostate;lung;cartilage;cerebral cortex;bone;placenta;spleen;brain;skeletal muscle;retina; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.23401 0.12374 0.7421753 86.35881104 318.11282 3.78837 STARD9 . . . StAR related lipid transfer domain containing 9 FUNCTION: Microtubule-dependent motor protein required for spindle pole assembly during mitosis. Required to stabilize the pericentriolar material (PCM). {ECO:0000269|PubMed:22153075}.; . TISSUE SPECIFICITY: Expressed in the central nervous system, muscle cells (heart and skeletal muscle), pancreas, prostate and lung. {ECO:0000269|PubMed:16964419}.; unclassifiable (Anatomical System);heart;cartilage;skin;skeletal muscle;retina;uterus;breast;optic nerve;whole body;lung;frontal lobe;liver;testis;spleen;germinal center;kidney;spinal ganglion;brain;mammary gland;cerebellum; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.15527 0.08189 7.306469488 99.90563812 4951.70589 14.34596 STARD10 0.0510371457810707 0.927512999083427 0.0214498551355019 StAR related lipid transfer domain containing 10 FUNCTION: May play metabolic roles in sperm maturation or fertilization (By similarity). Phospholipid transfer protein that preferentially selects lipid species containing a palmitoyl or stearoyl chain on the sn-1 and an unsaturated fatty acyl chain (18:1 or 18:2) on the sn-2 position. Able to transfer phosphatidylcholine (PC) and phosphatidyetanolamline (PE) between membranes. {ECO:0000250, ECO:0000269|PubMed:15911624}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; . 0.23088 . -0.203796826 38.81811748 61.56021 1.59930 STARD13 1.84668647836473e-07 0.998409134245856 0.0015906810854965 StAR related lipid transfer domain containing 13 FUNCTION: GTPase-activating protein for RhoA, and perhaps for Cdc42. May be involved in regulation of cytoskeletal reorganization, cell proliferation and cell motility. Acts a tumor suppressor in hepatocellular carcinoma cells. {ECO:0000269|PubMed:14697242, ECO:0000269|PubMed:16217026}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Underexpressed in hepatocellular carcinoma cells and some breast cancer cell lines. {ECO:0000269|PubMed:12531887, ECO:0000269|PubMed:14697242}.; smooth muscle;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;thyroid;bone;testis;spinal ganglion;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;lens;pancreas;lung;adrenal gland;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach; atrioventricular node;trigeminal ganglion; 0.55125 0.12968 -1.269658815 5.213493749 2449.56634 9.21182 STARD13-AS . . . STARD13 antisense RNA . . . . . . . . . . . STARD13-IT1 . . . STARD13 intronic transcript 1 . . . . . . . . . . . STARP1 . . . steroidogenic acute regulatory protein pseudogene 1 . . . . . . . . . . . STAT1 0.999994277113306 5.72288665785655e-06 3.64635622864645e-14 signal transducer and activator of transcription 1 FUNCTION: Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of IFN- stimulated genes (ISG), which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN- gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state. Becomes activated in response to KITLG/SCF and KIT signaling. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. {ECO:0000269|PubMed:12764129, ECO:0000269|PubMed:12855578, ECO:0000269|PubMed:15322115, ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:9724754}.; DISEASE: Immunodeficiency 31B (IMD31B) [MIM:613796]: A disorder characterized by susceptibility to severe mycobacterial and viral infections. Affected individuals can develop disseminated infections and die of viral illness. {ECO:0000269|PubMed:12590259, ECO:0000269|PubMed:20841510}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Immunodeficiency 31A (IMD31A) [MIM:614892]: A form of Mendelian susceptibility to mycobacterial disease, a rare condition caused by impairment of interferon-gamma mediated immunity. It is characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. Clinical outcome severity depends on the degree of impairment of interferon-gamma mediated immunity. Some patients die of overwhelming mycobacterial disease with lepromatous-like lesions in early childhood, whereas others develop, later in life, disseminated but curable infections with tuberculoid granulomas. IMD31A has low penetrance, and affected individuals have relatively mild disease and good prognosis. IMD31A confers a predisposition to mycobacterial infections only, with no increased susceptibility to viral infections. {ECO:0000269|PubMed:11452125, ECO:0000269|PubMed:16934001, ECO:0000269|PubMed:22573496}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Immunodeficiency 31C (IMD31C) [MIM:614162]: A primary immunodeficiency disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans. {ECO:0000269|PubMed:21714643, ECO:0000269|PubMed:21727188}. Note=The disease is caused by mutations affecting the gene represented in this entry. STAT1 mutations in patients with autosomal dominant candidiasis lead to defective responses of type 1 and type 17 helper T-cells, characterized by reduced production of interferon-alpha, interleukin-17, and interleukin-22. These cytokines are crucial for the antifungal defense of skin and mucosa (PubMed:21714643). {ECO:0000269|PubMed:21714643}.; . lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;lens;epididymis;macula lutea;visual apparatus;liver;alveolus;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;lymph node;ciliary ganglion;white blood cells;pons;atrioventricular node;trigeminal ganglion;whole blood;skin; 0.87416 0.96219 -0.291981272 33.20358575 22.02033 0.73972 STAT2 0.0410947373611941 0.95890482169179 4.40947015578647e-07 signal transducer and activator of transcription 2 FUNCTION: Signal transducer and activator of transcription that mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with IRF9/ISGF3G to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. {ECO:0000269|PubMed:9020188}.; . . myocardium;ovary;sympathetic chain;colon;fovea centralis;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;skeletal muscle;breast;lung;trabecular meshwork;macula lutea;hypopharynx;head and neck;kidney;peripheral nerve; superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.52438 0.35661 -0.731092527 14.13658882 607.01476 4.98513 STAT3 0.999989193151158 1.08068488073233e-05 3.47093745569125e-14 signal transducer and activator of transcription 3 (acute-phase response factor) FUNCTION: Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors. Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene (PubMed:17344214). May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the interleukin-6 (IL-6)- responsive elements identified in the promoters of various acute- phase protein genes. Activated by IL31 through IL31RA. Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1 (PubMed:17344214). Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation (By similarity). May play an apoptotic role by transctivating BIRC5 expression under LEP activation (PubMed:18242580). Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity. {ECO:0000250|UniProtKB:P42227, ECO:0000269|PubMed:10688651, ECO:0000269|PubMed:12359225, ECO:0000269|PubMed:12873986, ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:17344214, ECO:0000269|PubMed:18242580, ECO:0000269|PubMed:23084476}.; DISEASE: Hyperimmunoglobulin E recurrent infection syndrome, autosomal dominant (AD-HIES) [MIM:147060]: A rare disorder of immunity and connective tissue characterized by immunodeficiency, chronic eczema, recurrent Staphylococcal infections, increased serum IgE, eosinophilia, distinctive coarse facial appearance, abnormal dentition, hyperextensibility of the joints, and bone fractures. {ECO:0000269|PubMed:17676033, ECO:0000269|PubMed:17881745, ECO:0000269|PubMed:23342295}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Autoimmune disease, multisystem, infantile-onset (ADMIO) [MIM:615952]: A disorder characterized by early childhood onset of a spectrum of autoimmune manifestations affecting multiple organs, including insulin-dependent diabetes mellitus and autoimmune enteropathy or celiac disease. Other features include short stature, non-specific dermatitis, hypothyroidism, autoimmune arthritis, and delayed puberty. {ECO:0000269|PubMed:25038750}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; ovary;salivary gland;colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;synovium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;amnion;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; adipose tissue;beta cell islets;kidney; 0.98255 0.98129 -0.492218069 22.35786742 57.10617 1.52170 STAT4 0.988867842653571 0.0111321560562599 1.29016885041501e-09 signal transducer and activator of transcription 4 FUNCTION: Carries out a dual function: signal transduction and activation of transcription. Involved in IL12 signaling.; DISEASE: Systemic lupus erythematosus 11 (SLEB11) [MIM:612253]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:19109131}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Rheumatoid arthritis (RA) [MIM:180300]: An inflammatory disease with autoimmune features and a complex genetic component. It primarily affects the joints and is characterized by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures. {ECO:0000269|PubMed:17804842}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;blood;skeletal muscle;bone marrow;uterus;lung;endometrium;thyroid;pituitary gland;testis;head and neck;mammary gland; superior cervical ganglion; 0.89669 0.26173 -0.135838822 43.77211607 36.38548 1.09081 STAT5A 0.999866029464463 0.000133970519554613 1.59823290980301e-11 signal transducer and activator of transcription 5A FUNCTION: Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Mediates cellular responses to ERBB4. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the GAS element and activates PRL-induced transcription. Regulates the expression of milk proteins during lactation. {ECO:0000269|PubMed:11773439, ECO:0000269|PubMed:15534001}.; . . smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion; 0.68233 0.58998 -0.644723694 16.52512385 205.21053 3.09506 STAT5B 0.999953160240961 4.68397578031115e-05 1.23562470739329e-12 signal transducer and activator of transcription 5B FUNCTION: Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Binds to the GAS element and activates PRL-induced transcription. {ECO:0000269|PubMed:11773439}.; DISEASE: Growth hormone insensitivity with immunodeficiency (GHII) [MIM:245590]: A disease characterized by short stature, growth hormone deficiency in the presence of normal to elevated circulating concentrations of growth hormone, resistance to hexogeneous growth hormone therapy, and recurrent infections. {ECO:0000269|PubMed:13679528, ECO:0000269|PubMed:15827093, ECO:0000269|PubMed:22419735}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;hypothalamus;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;thymus; testis - interstitial;superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.50895 . -0.890882376 10.30313753 46.4952 1.31577 STAT6 0.100774662146281 0.899222797610389 2.54024332940812e-06 signal transducer and activator of transcription 6 FUNCTION: Carries out a dual function: signal transduction and activation of transcription. Involved in IL4/interleukin-4- and IL3/interleukin-3-mediated signaling. {ECO:0000269|PubMed:17210636}.; . . myocardium;lymphoreticular;ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;brain;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; superior cervical ganglion;adrenal gland;white blood cells;whole blood;trigeminal ganglion; 0.95006 0.75170 -0.686998355 15.26893135 95.51346 2.11023 STATH 0.00208280630577998 0.508287612806622 0.489629580887598 statherin FUNCTION: Salivary protein that stabilizes saliva supersaturated with calcium salts by inhibiting the precipitation of calcium phosphate salts. It also modulates hydroxyapatite crystal formation on the tooth surface.; . TISSUE SPECIFICITY: Secreted by parotid and submandibular glands.; unclassifiable (Anatomical System);adrenal gland;salivary gland;thyroid;adrenal cortex;parotid gland;parathyroid;head and neck;pineal gland;skeletal muscle; prostate;superior cervical ganglion;thalamus;trachea;salivary gland;thyroid; 0.06793 . 0.301449681 71.80938901 25.14147 0.82212 STAU1 0.996415824871937 0.00358412697380523 4.81542577096105e-08 staufen double-stranded RNA binding protein 1 FUNCTION: Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.; . TISSUE SPECIFICITY: Widely expressed. Expressed in brain, pancreas, heart, skeletal muscles, liver, lung, kidney and placenta.; lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;pancreas;lung;pia mater;adrenal gland;placenta;hippocampus;duodenum;kidney;stomach; amygdala;superior cervical ganglion;ciliary ganglion;kidney; 0.35671 0.17068 -0.314027422 31.9297004 163.86261 2.79627 STAU2 0.950439190486362 0.0495545472091782 6.26230445988224e-06 staufen double-stranded RNA binding protein 2 FUNCTION: RNA-binding protein required for the microtubule- dependent transport of neuronal RNA from the cell body to the dendrite. As protein synthesis occurs within the dendrite, the localization of specific mRNAs to dendrites may be a prerequisite for neurite outgrowth and plasticity at sites distant from the cell body (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;pons;trigeminal ganglion;parietal lobe;cingulate cortex;skeletal muscle; 0.54086 0.11510 0.330767508 73.53739089 382.64024 4.12401 STAU2-AS1 . . . STAU2 antisense RNA 1 . . . . . . . . . . . STBD1 . . . starch binding domain 1 FUNCTION: Acts as a cargo receptor for glycogen. Delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes. {ECO:0000269|PubMed:20810658, ECO:0000269|PubMed:21893048, ECO:0000269|PubMed:24837458}.; . TISSUE SPECIFICITY: Expressed at high level in skeletal and cardiac muscles. Moderately expressed in liver and placenta. No expression is found in pancreas, kidney or lung. Present in skeletal muscle, heart and placenta (at protein level). {ECO:0000269|PubMed:9794794}.; unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;sympathetic chain;colon;parathyroid;blood;skeletal muscle;breast;uterus;prostate;whole body;lung;endometrium;bone;thyroid;placenta;visual apparatus;liver;spleen;kidney;mammary gland;bladder;stomach;gall bladder; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.05082 0.06204 0.150760231 64.51403633 . . STC1 0.473499049992616 0.521246322465566 0.00525462754181721 stanniocalcin 1 FUNCTION: Stimulates renal phosphate reabsorption, and could therefore prevent hypercalcemia.; . TISSUE SPECIFICITY: Expressed in most tissues, with the highest levels in ovary, prostate, heart, kidney and thyroid. In the kidney, expression is confined to the nephron, specifically in the distal convoluted tubule and in the collecting tubule. Not detected in the brain, liver, spleen, peripheral blood leukocytes and adrenal medulla.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;ganglion;endometrium;bone;pituitary gland;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;trabecular meshwork;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;uterus corpus;smooth muscle;trachea;thyroid;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.86110 . -0.141298762 42.87567823 20.13195 0.68816 STC2 0.453518117972185 0.540378642794652 0.00610323923316298 stanniocalcin 2 FUNCTION: Has an anti-hypocalcemic action on calcium and phosphate homeostasis.; . TISSUE SPECIFICITY: Expressed in a variety of tissues including muscle, heart, pancreas, kidney, spleen, prostate, small intestine, colon and peripheral blood leukocytes.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;muscle;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;duodenum;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;smooth muscle;heart; 0.14459 0.16191 -0.53631094 20.53550366 76.39753 1.83301 STEAP1 0.434511093853516 0.558457053338021 0.00703185280846302 six transmembrane epithelial antigen of the prostate 1 FUNCTION: Metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in prostate tumors. {ECO:0000269|PubMed:16609065}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;bone;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;kidney;stomach; prostate; 0.05808 0.13670 -0.205617011 38.57631517 28.5157 0.91377 STEAP1B 4.60216723976545e-05 0.413846571410874 0.586107406916728 STEAP family member 1B . . . . . . . 1.837370901 97.05708894 5709.49783 15.66230 STEAP2 0.00244974706931913 0.981585558384512 0.0159646945461691 STEAP2 metalloreductase FUNCTION: Metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at high levels in prostate and at significantly lower levels in heart, brain, kidney, pancreas, and ovary. {ECO:0000269|PubMed:12095985, ECO:0000269|PubMed:12429817, ECO:0000269|PubMed:16609065}.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;bone;pituitary gland;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;macula lutea;liver;hypopharynx;spleen;head and neck;kidney;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;pons;atrioventricular node; 0.03441 0.10663 0.507139401 80.10143902 6182.01659 16.43941 STEAP2-AS1 . . . STEAP2 antisense RNA 1 . . . . . . . . . . . STEAP3 3.93787753538719e-07 0.202974066836758 0.797025539375488 STEAP3 metalloreductase FUNCTION: Endosomal ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Participates in erythroid iron homeostasis by reducing Fe(3+) to Fe(2+). Can also reduce of Cu(2+) to Cu(1+), suggesting that it participates in copper homeostasis. Uses NADP(+) as acceptor. May play a role downstream of p53/TP53 to interface apoptosis and cell cycle progression. Indirectly involved in exosome secretion by facilitating the secretion of proteins such as TCTP. {ECO:0000269|PubMed:15319436, ECO:0000269|PubMed:16651434}.; DISEASE: Anemia, hypochromic microcytic, with iron overload 2 (AHMIO2) [MIM:615234]: A hematologic disease characterized by abnormal hemoglobin content in the erythrocytes which are reduced in size, severe anemia, erythropoietic hyperplasia of bone marrow, massive hepatic iron deposition, and hepatosplenomegaly. {ECO:0000269|PubMed:22031863}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in adult bone marrow, placenta, liver, skeletal muscle and pancreas. Down-regulated in hepatocellular carcinoma. {ECO:0000269|PubMed:12606722, ECO:0000269|PubMed:15885357, ECO:0000269|PubMed:16227996}.; unclassifiable (Anatomical System);placenta;visual apparatus;liver;colon;cervix;blood;brain;bone marrow; dorsal root ganglion;liver;ciliary ganglion;skeletal muscle; 0.20965 . -0.10469683 45.64755839 525.83503 4.67915 STEAP3-AS1 . . . STEAP3 antisense RNA 1 . . . . . . . . . . . STEAP4 1.49862010031802e-05 0.856844346196707 0.14314066760229 STEAP4 metalloreductase FUNCTION: Metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor. Plays a role in systemic metabolic homeostasis, integrating inflammatory and metabolic responses (By similarity). Associated with obesity and insulin-resistance. Involved in inflammatory arthritis, through the regulation of inflammatory cytokines. Inhibits anchorage-independent cell proliferation. {ECO:0000250, ECO:0000269|PubMed:18381574, ECO:0000269|PubMed:18430367, ECO:0000269|PubMed:19660107, ECO:0000269|PubMed:19787193}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in adipose tissue. Expressed in placenta, lung, heart and prostate. Detected at lower levels in liver, skeletal muscle, pancreas, testis and small intestine. Highly expressed in joints of patients with rheumatoid arthritis and localized with CD68 cells, a marker for macrophages. {ECO:0000269|PubMed:15897894, ECO:0000269|PubMed:16227996, ECO:0000269|PubMed:18381574, ECO:0000269|PubMed:18430367, ECO:0000269|PubMed:19289123, ECO:0000269|PubMed:19660107}.; uterus;prostate;lung;ovary;heart;placenta;iris;hypopharynx;testis;parathyroid;head and neck;skin; atrioventricular node;trigeminal ganglion; 0.10241 0.08165 0.817616644 87.95116773 923.70889 5.90188 STH 0.00444466614164462 0.435690893204263 0.559864440654093 saitohin . . TISSUE SPECIFICITY: Highest expression in placenta, muscle, fetal brain, and adult brain, with lower expression in heart, kidney, stomach, testis, and adrenal gland. In the central nervous system, highest expression is in temporal lobe, hypothalamus, medulla and spinal cord, with lower expression in other brain regions. {ECO:0000269|PubMed:12032355}.; . . . . 0.657836546 84.27105449 56.13997 1.50502 STIL 0.202687840102417 0.797308725945108 3.4339524750932e-06 SCL/TAL1 interrupting locus FUNCTION: Immediate-early gene. Plays an important role in embryonic development as well as in cellular growth and proliferation; its long-term silencing affects cell survival and cell cycle distribution as well as decreases CDK1 activity correlated with reduced phosphorylation of CDK1. Plays a role as a positive regulator of the sonic hedgehog pathway, acting downstream of PTCH1. {ECO:0000269|PubMed:16024801, ECO:0000269|PubMed:9372240}.; DISEASE: Note=A chromosomal aberration involving STIL may be a cause of some T-cell acute lymphoblastic leukemias (T-ALL). A deletion at 1p32 between STIL and TAL1 genes leads to STIL/TAL1 fusion mRNA with STIL exon 1 slicing to TAL1 exon 3. As both STIL exon 1 and TAL1 exon 3 are 5'-untranslated exons, STIL/TAL1 fusion mRNA predicts a full length TAL1 protein under the control of the STIL promoter, leading to inappropriate TAL1 expression. In childhood T-cell malignancies (T-ALL), a type of defect such as STIL/TAL1 fusion is associated with a good prognosis. In cultured lymphocytes from healthy adults, STIL/TAL1 fusion mRNA may be detected after 7 days of culture. {ECO:0000269|PubMed:11390401, ECO:0000269|PubMed:12681356, ECO:0000269|PubMed:1311214, ECO:0000269|PubMed:14504110, ECO:0000269|PubMed:1922059, ECO:0000269|PubMed:2209547, ECO:0000269|PubMed:2255914}.; DISEASE: Microcephaly 7, primary, autosomal recessive (MCPH7) [MIM:612703]: A disease defined as a head circumference more than 3 standard deviations below the age-related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. Despite this marked reduction in size, the gyral pattern is relatively well preserved, with no major abnormality in cortical architecture. Affected individuals are mentally retarded. Primary microcephaly is further defined by the absence of other syndromic features or significant neurological deficits due to degenerative brain disorder. {ECO:0000269|PubMed:19215732, ECO:0000269|PubMed:22989186}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in all hematopoietic tissues and cell lines. Highly expressed in a variety of tumors characterized by increased mitotic activity with highest expression in lung cancer. {ECO:0000269|PubMed:15107824, ECO:0000269|PubMed:1922059}.; unclassifiable (Anatomical System);ovary;heart;colon;blood;skin;skeletal muscle;uterus;pancreas;whole body;lung;endometrium;placenta;bone;visual apparatus;liver;testis;head and neck;spleen;cervix;germinal center;brain;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.34153 0.08855 0.694433477 85.28544468 144.47167 2.61778 STIM1 0.926766742543403 0.073229855871381 3.40158521623259e-06 stromal interaction molecule 1 FUNCTION: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores (PubMed:15866891, PubMed:16005298, PubMed:16208375, PubMed:16537481, PubMed:16733527, PubMed:16766533, PubMed:16807233, PubMed:18854159, PubMed:19249086, PubMed:22464749, PubMed:24069340, PubMed:24351972, PubMed:24591628, PubMed:26322679). Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit ORAI1 (PubMed:16208375, PubMed:16537481). Involved in enamel formation (PubMed:24621671). Activated following interaction with TMEM110/STIMATE, leading to promote STIM1 conformational switch (PubMed:26322679). {ECO:0000269|PubMed:15866891, ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16208375, ECO:0000269|PubMed:16537481, ECO:0000269|PubMed:16733527, ECO:0000269|PubMed:16766533, ECO:0000269|PubMed:16807233, ECO:0000269|PubMed:18854159, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:22464749, ECO:0000269|PubMed:24069340, ECO:0000269|PubMed:24351972, ECO:0000269|PubMed:24591628, ECO:0000269|PubMed:24621671, ECO:0000269|PubMed:26322679}.; DISEASE: Immunodeficiency 10 (IMD10) [MIM:612783]: An immune disorder characterized by recurrent infections, impaired activation and proliferative response of T-cells, decreased T-cell production of cytokines, lymphadenopathy, and normal lymphocytes counts and serum immunoglobulin levels. Additional features include thrombocytopenia, autoimmune hemolytic anemia, myopathy, partial iris hypoplasia, hepatosplenomegaly and defective enamel dentition. {ECO:0000269|PubMed:19420366, ECO:0000269|PubMed:22190180}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Myopathy, tubular aggregate, 1 (TAM1) [MIM:160565]: A rare congenital myopathy characterized by regular arrays of membrane tubules on muscle biopsies without additional histopathological hallmarks. Tubular aggregates in muscle are structures of variable appearance consisting of an outer tubule containing either one or more microtubule-like structures or amorphous material. They may occur in a variety of circumstances, including inherited myopathies, alcohol- and drug-induced myopathies, exercise-induced cramps or muscle weakness. {ECO:0000269|PubMed:23332920}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Stormorken syndrome (STRMK) [MIM:185070]: A rare autosomal dominant disease characterized by mild bleeding tendency, thrombocytopathy, thrombocytopenia, mild anemia, asplenia, tubular aggregate myopathy, miosis, headache, and ichthyosis. {ECO:0000269|PubMed:24591628, ECO:0000269|PubMed:24619930, ECO:0000269|PubMed:25577287}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed in various human primary cells and tumor cell lines. {ECO:0000269|PubMed:11004585, ECO:0000269|PubMed:11463338}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;blood;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; dorsal root ganglion;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;caudate nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.24500 0.16661 -0.222203495 37.54423213 234.40836 3.30996 STIM2 . . . stromal interaction molecule 2 FUNCTION: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Functions as a highly sensitive Ca(2+) sensor in the endoplasmic reticulum which activates both store-operated and store-independent Ca(2+)-influx. Regulates basal cytosolic and endoplasmic reticulum Ca(2+) concentrations. Upon mild variations of the endoplasmic reticulum Ca(2+) concentration, translocates from the endoplasmic reticulum to the plasma membrane where it probably activates the Ca(2+) release-activated Ca(2+) (CRAC) channels ORAI1, ORAI2 and ORAI3. May inhibit STIM1-mediated Ca(2+) influx. {ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16860747, ECO:0000269|PubMed:17905723, ECO:0000269|PubMed:18160041, ECO:0000269|PubMed:21217057, ECO:0000269|PubMed:22464749, ECO:0000269|PubMed:23359669}.; . TISSUE SPECIFICITY: Expressed in all tissues and tumor cell lines examined. {ECO:0000269|PubMed:11463338}.; ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;islets of Langerhans;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach; subthalamic nucleus; 0.15101 0.12286 -1.241834664 5.414012739 1358.06126 6.91660 STIP1 0.999887764233234 0.000112235756382077 1.03840041338421e-11 stress induced phosphoprotein 1 FUNCTION: Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB).; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;oesophagus;larynx;bone;thyroid;iris;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;duodenum;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; whole brain;testis - interstitial;testis;cerebellum; 0.65119 0.18755 -0.558357437 19.54470394 25.94299 0.84310 STIP1P1 . . . stress induced phosphoprotein 1 pseudogene 1 . . . . . . . . . . . STIP1P2 . . . stress induced phosphoprotein 1 pseudogene 2 . . . . . . . . . . . STIP1P3 . . . stress induced phosphoprotein 1 pseudogene 3 . . . . . . . . . . . STK3 5.73733703569325e-09 0.22834818470952 0.771651809553143 serine/threonine kinase 3 FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates NKX2-1 (By similarity). Phosphorylates NEK2 and plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosome, and its ability to phosphorylate CROCC and CEP250. In conjunction with SAV1, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation. Positively regulates RAF1 activation via suppression of the inhibitory phosphorylation of RAF1 on 'Ser-259'. Phosphorylates MOBKL1A and RASSF2. Phosphorylates MOBKL1B on 'Thr-74'. Acts cooperatively with MOBKL1B to activate STK38. {ECO:0000250, ECO:0000269|PubMed:15688006, ECO:0000269|PubMed:16930133, ECO:0000269|PubMed:18328708, ECO:0000269|PubMed:18362890, ECO:0000269|PubMed:19525978, ECO:0000269|PubMed:20212043, ECO:0000269|PubMed:21076410, ECO:0000269|PubMed:21104395, ECO:0000269|PubMed:8566796, ECO:0000269|PubMed:8816758}.; . TISSUE SPECIFICITY: Expressed at high levels in adult kidney, skeletal and placenta tissues and at very low levels in adult heart, lung and brain tissues. {ECO:0000269|PubMed:8566796}.; . . 0.14006 0.11274 -0.359940251 28.93371078 43.68214 1.25754 STK4 0.118311921511212 0.881456100647095 0.000231977841692516 serine/threonine kinase 4 FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation (By similarity). Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes. {ECO:0000250, ECO:0000269|PubMed:11278283, ECO:0000269|PubMed:11517310, ECO:0000269|PubMed:12757711, ECO:0000269|PubMed:15109305, ECO:0000269|PubMed:16510573, ECO:0000269|PubMed:16751106, ECO:0000269|PubMed:16930133, ECO:0000269|PubMed:17932490, ECO:0000269|PubMed:18328708, ECO:0000269|PubMed:18986304, ECO:0000269|PubMed:19525978, ECO:0000269|PubMed:21212262, ECO:0000269|PubMed:21245099, ECO:0000269|PubMed:21512132, ECO:0000269|PubMed:8702870, ECO:0000269|PubMed:8816758}.; DISEASE: T-cell immunodeficiency, recurrent infections, and autoimmunity with or without cardiac malformations (TIIAC) [MIM:614868]: A primary T-cell immunodeficiency syndrome characterized by progressive loss of naive T-cells, recurrent bacterial, viral, and fungal infections, warts, and abscesses, autoimmune manifestations, and cardiac malformations, including atrial septal defect. {ECO:0000269|PubMed:22294732}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in prostate cancer and levels increase from the normal to the malignant state (at protein level). Ubiquitously expressed. {ECO:0000269|PubMed:17932490}.; . . 0.85357 0.12014 -0.424258538 25.56027365 1832.7524 7.88897 STK4-AS1 . . . STK4 antisense RNA 1 (head to head) . . . . . . . . . . . STK10 1.50167370249254e-07 0.999565478032935 0.000434371799695191 serine/threonine kinase 10 FUNCTION: Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo. {ECO:0000269|PubMed:11903060, ECO:0000269|PubMed:12639966, ECO:0000269|PubMed:19255442}.; DISEASE: Testicular germ cell tumor (TGCT) [MIM:273300]: A common malignancy in males representing 95% of all testicular neoplasms. TGCTs have various pathologic subtypes including: unclassified intratubular germ cell neoplasia, seminoma (including cases with syncytiotrophoblastic cells), spermatocytic seminoma, embryonal carcinoma, yolk sac tumor, choriocarcinoma, and teratoma. {ECO:0000269|PubMed:16175573}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in rapidly proliferating tissues (spleen, placenta, and peripheral blood leukocytes). Also expressed in brain, heart, skeletal muscle, colon, thymus, kidney, liver, small intestine and lung. {ECO:0000269|PubMed:12639966}.; lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;iris;germinal center;brain;tonsil;heart;cartilage;tongue;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;nasopharynx;placenta;duodenum;hypopharynx;amnion;head and neck;kidney;cerebellum; lymph node;placenta;testis;white blood cells;whole blood;trigeminal ganglion;bone marrow;cerebellum; 0.49152 0.13893 -0.922264439 9.778249587 312.49935 3.76136 STK11 0.978282902427481 0.021697469549645 1.96280228741606e-05 serine/threonine kinase 11 FUNCTION: Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, thus promoting their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non- AMPK family proteins such as STRADA, PTEN and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neuron polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53; the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to the mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. In vein endothelial cells, inhibits PI3K/Akt signaling activity and thus induces apoptosis in response to the oxidant peroxynitrite (in vitro). Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with NUAK1, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair (PubMed:25329316). {ECO:0000269|PubMed:11430832, ECO:0000269|PubMed:12805220, ECO:0000269|PubMed:14517248, ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15016379, ECO:0000269|PubMed:15733851, ECO:0000269|PubMed:15987703, ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:18321849, ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:25329316}.; DISEASE: Peutz-Jeghers syndrome (PJS) [MIM:175200]: An autosomal dominant disorder characterized by melanocytic macules of the lips, multiple gastrointestinal hamartomatous polyps and an increased risk for various neoplasms, including gastrointestinal cancer. {ECO:0000269|PubMed:10408777, ECO:0000269|PubMed:12372054, ECO:0000269|PubMed:21411391, ECO:0000269|PubMed:9425897, ECO:0000269|PubMed:9428765, ECO:0000269|PubMed:9760200, ECO:0000269|PubMed:9837816}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Testicular germ cell tumor (TGCT) [MIM:273300]: A common malignancy in males representing 95% of all testicular neoplasms. TGCTs have various pathologic subtypes including: unclassified intratubular germ cell neoplasia, seminoma (including cases with syncytiotrophoblastic cells), spermatocytic seminoma, embryonal carcinoma, yolk sac tumor, choriocarcinoma, and teratoma. {ECO:0000269|PubMed:9605748}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Note=Defects in STK11 are associated with some sporadic cancers, especially lung cancers. Frequently mutated and inactivated in non-small cell lung cancer (NSCLC). Defects promote lung cancerigenesis process, especially lung cancer progression and metastasis. Confers lung adenocarcinoma the ability to trans- differentiate into squamous cell carcinoma. Also able to promotes lung cancer metastasis, via both cancer-cell autonomous and non- cancer-cell autonomous mechanisms.; TISSUE SPECIFICITY: Ubiquitously expressed. Strongest expression in testis and fetal liver.; medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;muscle;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;testis;skeletal muscle; 0.53144 0.30718 -0.53631094 20.53550366 50.82377 1.40507 STK11IP . . . serine/threonine kinase 11 interacting protein FUNCTION: May regulate STK11/LKB1 function by controlling its subcellular localization. {ECO:0000269|PubMed:11741830}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;oesophagus;synovium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;alveolus;duodenum;liver;cervix;kidney;mammary gland;aorta;stomach;cerebellum; white blood cells; 0.10678 0.08950 -0.213110737 37.75064874 470.92876 4.49090 STK16 0.000478667136022908 0.874050299265535 0.125471033598442 serine/threonine kinase 16 FUNCTION: Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins. {ECO:0000269|PubMed:10364453}.; . TISSUE SPECIFICITY: Ubiquitously expressed at very low levels. {ECO:0000269|PubMed:10364453}.; . . 0.40897 0.13253 -0.291981272 33.20358575 76.47329 1.83504 STK16P1 . . . serine/threonine kinase 16 pseudogene 1 . . . . . . . . . . . STK17A 0.176185204823442 0.821123595767321 0.00269119940923679 serine/threonine kinase 17a FUNCTION: Acts as a positive regulator of apoptosis. Also acts as a regulator of cellular reactive oxygen species. {ECO:0000269|PubMed:21489989, ECO:0000269|PubMed:9786912}.; . TISSUE SPECIFICITY: Highly expressed in placenta. Lower levels in heart, lung, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:9786912}.; medulla oblongata;smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;pancreas;lung;nasopharynx;placenta;visual apparatus;alveolus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;cingulate cortex; 0.22446 0.11688 0.150760231 64.51403633 269.23329 3.51955 STK17B 0.0898257461867161 0.90129105250493 0.00888320130835353 serine/threonine kinase 17b FUNCTION: Phosphorylates myosin light chains (By similarity). Acts as a positive regulator of apoptosis. {ECO:0000250, ECO:0000269|PubMed:9786912}.; . TISSUE SPECIFICITY: Highly expressed in placenta, lung, pancreas. Lower levels in heart, brain, liver, skeletal muscle and kidney. {ECO:0000269|PubMed:9786912}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;colon;parathyroid;blood;skin;bone marrow;uterus;bile duct;prostate;pancreas;lung;nasopharynx;placenta;testis;spleen;germinal center;tonsil;stomach; superior cervical ganglion;white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.27534 0.09912 -0.029247611 51.40363293 36.31128 1.08796 STK19 0.00461708135223375 0.988840415286933 0.00654250336083374 serine/threonine kinase 19 FUNCTION: Seems to be a protein kinase. In vitro it can phosphorylate casein-alpha on serine and threonine residues and histones on serine residues.; . TISSUE SPECIFICITY: Monocytes, hepatocytes, epithelial cells, T- and B-lymphocytes.; . . 0.22911 0.09376 0.21689899 68.12927577 890.88249 5.81631 STK19B . . . serine/threonine kinase 19B (pseudogene) FUNCTION: Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins. {ECO:0000269|PubMed:11847227, ECO:0000269|PubMed:18376416, ECO:0000269|PubMed:20106869, ECO:0000269|PubMed:22085962}.; DISEASE: Retinitis pigmentosa 2 (RP2) [MIM:312600]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:10090907, ECO:0000269|PubMed:10520237, ECO:0000269|PubMed:10634633, ECO:0000269|PubMed:10937588, ECO:0000269|PubMed:11462235, ECO:0000269|PubMed:11992260, ECO:0000269|PubMed:12657579, ECO:0000269|PubMed:14564670, ECO:0000269|PubMed:22334370, ECO:0000269|PubMed:9697692}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Expressed in the rod and cone photoreceptors, extending from the tips of the outer segment (OS) through the inner segment (IS) and outer nuclear layer (ONL) and into the synaptic terminals of the outer plexiform layer (ONL). Also detected in the bipolar, horizontal and amacrine cells in the inner nuclear layer (INL), extending to the inner plexiform layer (IPL) and though the ganglion cell layer (GCL) and into the nerve fiber layer (NFL) (at protein level). {ECO:0000269|PubMed:10942419, ECO:0000269|PubMed:12417528, ECO:0000269|PubMed:18376416}.; . . 0.15579 0.28800 0.349177632 74.18023119 . . STK24 0.79799829659642 0.201951804309193 4.98990943869647e-05 serine/threonine kinase 24 FUNCTION: Serine/threonine-protein kinase that acts on both serine and threonine residues and promotes apoptosis in response to stress stimuli and caspase activation. Mediates oxidative-stress- induced cell death by modulating phosphorylation of JNK1-JNK2 (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during oxidative stress. Plays a role in a staurosporine-induced caspase- independent apoptotic pathway by regulating the nuclear translocation of AIFM1 and ENDOG and the DNase activity associated with ENDOG. Phosphorylates STK38L on 'Thr-442' and stimulates its kinase activity. Regulates cellular migration with alteration of PTPN12 activity and PXN phosphorylation: phosphorylates PTPN12 and inhibits its activity and may regulate PXN phosphorylation through PTPN12. May act as a key regulator of axon regeneration in the optic nerve and radial nerve. {ECO:0000269|PubMed:16314523, ECO:0000269|PubMed:17046825, ECO:0000269|PubMed:19604147, ECO:0000269|PubMed:19782762, ECO:0000269|PubMed:19855390}.; . TISSUE SPECIFICITY: Isoform A is ubiquitous. Isoform B is expressed in brain with high expression in hippocampus and cerebral cortex.; . . 0.58810 0.12390 -0.337894035 30.37272942 36.47857 1.09309 STK24-AS1 . . . STK24 antisense RNA 1 . . . . . . . . . . . STK24P1 . . . serine/threonine kinase 24 pseudogene 1 . . . . . . . . . . . STK25 0.0452670903034573 0.953616611744193 0.00111629795234976 serine/threonine kinase 25 FUNCTION: Oxidant stress-activated serine/threonine kinase that may play a role in the response to environmental stress. Targets to the Golgi apparatus where it appears to regulate protein transport events, cell adhesion, and polarity complexes important for cell migration. {ECO:0000269|PubMed:15037601}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highest levels are found in testis, large intestine, brain and stomach followed by heart and lung.; ovary;salivary gland;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;pineal body;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; amygdala;whole brain;thyroid;prefrontal cortex;parietal lobe;skeletal muscle; 0.17933 0.12726 -1.045216355 7.661004954 22.91692 0.76375 STK25P1 . . . serine/threonine kinase 25 pseudogene 1 . . . . . . . . . . . STK26 . . . serine/threonine protein kinase 26 FUNCTION: Mediator of cell growth. Modulates apoptosis. {ECO:0000269|PubMed:11641781, ECO:0000269|PubMed:17360971}.; . . . . . . -0.139478553 43.29440906 . . STK31 0.233315306725925 0.766684177213539 5.16060536646994e-07 serine/threonine kinase 31 . . TISSUE SPECIFICITY: Testis specific.; unclassifiable (Anatomical System);medulla oblongata;pancreas;thyroid;testis;colon; superior cervical ganglion;testis - interstitial;subthalamic nucleus;fetal brain;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; 0.10802 0.08609 1.603891239 95.89525832 3757.52502 11.99306 STK32A 5.72450465710222e-05 0.887458905004767 0.112483849948662 serine/threonine kinase 32A . . . unclassifiable (Anatomical System);hypopharynx;testis;head and neck;bladder; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10096 0.09136 -0.492218069 22.35786742 80.8775 1.90196 STK32B 0.00432349027379393 0.988492933335721 0.0071835763904853 serine/threonine kinase 32B . . . unclassifiable (Anatomical System);heart;ovary;cartilage;sympathetic chain;colon;parathyroid;lens;skin;breast;lung;placenta;bone;visual apparatus;testis;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;fetal brain;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle;thymus; 0.56370 0.10520 -0.642904474 16.62538335 2563.02987 9.46147 STK32C 0.309709769270868 0.689507911350236 0.000782319378895938 serine/threonine kinase 32C . . . unclassifiable (Anatomical System);blood;retina;uterus;pancreas;prostate;optic nerve;lung;endometrium;bone;liver;testis;spleen;cervix;kidney;brain;stomach;thymus; whole brain;superior cervical ganglion;temporal lobe;globus pallidus; 0.08231 0.11020 -0.356299879 29.31115829 1893.96573 8.00243 STK33 0.000137426345687613 0.961025575903118 0.038836997751194 serine/threonine kinase 33 FUNCTION: Serine/threonine protein kinase which phosphorylates VIME. May play a specific role in the dynamic behavior of the intermediate filament cytoskeleton by phosphorylation of VIME (By similarity). Not essential for the survival of KRAS-dependent AML cell lines. {ECO:0000250, ECO:0000269|PubMed:21742770}.; . TISSUE SPECIFICITY: Highly expressed in testis, fetal lung and heart, followed by pituitary gland, kidney, interventricular septum, pancreas, heart, trachea, thyroid gland and uterus. Weak hybridization signals were observed in the following tissues: amygdala, aorta, esophagus, colon ascending, colon transverse, skeletal muscle, spleen, peripheral blood leukocyte, lymph node, bone marrow, placenta, prostate, liver, salivary gland, mammary gland, some tumor cell lines, fetal brain, fetal liver, fetal spleen and fetal thymus. No signal at all was detectable in RNA from tissues of the nervous system. {ECO:0000269|PubMed:11738831, ECO:0000269|PubMed:16176263}.; unclassifiable (Anatomical System);ovary;parathyroid;fovea centralis;choroid;lens;retina;pancreas;optic nerve;lung;cochlea;endometrium;placenta;macula lutea;testis;cervix;germinal center;kidney;stomach; . 0.13985 0.08349 -0.067881249 48.69072895 472.75776 4.49965 STK33P1 . . . serine/threonine kinase 33 pseudogene 1 . . . . . . . . . . . STK35 0.918199525844565 0.0812642750314218 0.00053619912401359 serine/threonine kinase 35 . . TISSUE SPECIFICITY: Expressed in testis.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;larynx;thyroid;iris;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;duodenum;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.19968 0.11306 . . 1408.18303 7.01040 STK36 3.75253893187074e-07 0.999976004364491 2.36203816153893e-05 serine/threonine kinase 36 FUNCTION: Serine/threonine protein kinase which plays an important role in the sonic hedgehog (Shh) pathway by regulating the activity of GLI transcription factors (PubMed:10806483). Controls the activity of the transcriptional regulators GLI1, GLI2 and GLI3 by opposing the effect of SUFU and promoting their nuclear localization (PubMed:10806483). GLI2 requires an additional function of STK36 to become transcriptionally active, but the enzyme does not need to possess an active kinase catalytic site for this to occur (PubMed:10806483). Required for postnatal development, possibly by regulating the homeostasis of cerebral spinal fluid or ciliary function (By similarity). Essential for construction of the central pair apparatus of motile cilia. {ECO:0000250|UniProtKB:Q69ZM6, ECO:0000269|PubMed:10806483}.; . TISSUE SPECIFICITY: Expressed at low levels in most fetal tissues, adult ovaries and at high levels in adult testis, where it is localized in germ cells. {ECO:0000269|PubMed:10806483}.; colon;skin;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;skeletal muscle;pancreas;lung;mesenchyma;epididymis;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.33114 0.21612 1.194112905 92.85798537 6326.45178 16.63959 STK38 0.853295086026932 0.14668411396948 2.08000035876348e-05 serine/threonine kinase 38 FUNCTION: Negative regulator of MAP3K1/2 signaling. Converts MAP3K2 from its phosphorylated form to its non-phosphorylated form and inhibits autophosphorylation of MAP3K2. {ECO:0000269|PubMed:12493777, ECO:0000269|PubMed:15197186, ECO:0000269|PubMed:17906693, ECO:0000269|PubMed:7761441}.; . TISSUE SPECIFICITY: Ubiquitously expressed with highest levels observed in peripheral blood leukocytes. {ECO:0000269|PubMed:15197186, ECO:0000269|PubMed:7761441}.; ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lacrimal gland;muscle;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;white blood cells;atrioventricular node;whole blood;trigeminal ganglion; 0.67009 0.33817 -0.295622497 32.61972163 5433.54754 15.20472 STK38L 0.965893632010774 0.0341039054032483 2.46258597804486e-06 serine/threonine kinase 38 like FUNCTION: Involved in the regulation of structural processes in differentiating and mature neuronal cells. {ECO:0000250, ECO:0000269|PubMed:15037617, ECO:0000269|PubMed:15067004}.; . TISSUE SPECIFICITY: Ubiquitously expressed with highest levels observed in the thymus. {ECO:0000269|PubMed:15067004}.; . . 0.72805 0.12607 -0.361761279 28.6329323 9.52509 0.35064 STK39 0.999462431417641 0.000537568110589189 4.71769711061077e-10 serine/threonine kinase 39 FUNCTION: May act as a mediator of stress-activated signals. Mediates the inhibiton of SLC4A4, SLC26A6 as well as CFTR activities by the WNK scaffolds, probably through phosphorylation. {ECO:0000250|UniProtKB:Q9Z1W9}.; . TISSUE SPECIFICITY: Predominantly expressed in brain and pancreas followed by heart, lung, kidney, skeletal muscle, liver, placenta and testis.; ovary;colon;fovea centralis;skin;retina;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;blood;skeletal muscle;bile duct;pancreas;lung;mesenchyma;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; amygdala;thalamus;occipital lobe;medulla oblongata;subthalamic nucleus;hypothalamus;spinal cord;pons;cingulate cortex;parietal lobe; 0.35513 0.21966 -0.337894035 30.37272942 4051.69126 12.61535 STK40 0.991723985402898 0.00827417584188933 1.83875521224308e-06 serine/threonine kinase 40 FUNCTION: May be a negative regulator of NF-kappa-B and p53- mediated gene transcription. {ECO:0000269|PubMed:13679039}.; . TISSUE SPECIFICITY: Strongly expressed in heart, brain, placenta, lung, skeletal muscle, kidney, spleen, thymus, prostate, liver, pancreas, testis, ovary, small intestine, colon and peripheral blood leukocytes. {ECO:0000269|PubMed:13679039}.; lymphoreticular;myocardium;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; superior cervical ganglion;placenta;trigeminal ganglion; 0.28752 0.11579 -0.955204708 9.170794999 1863.13145 7.95225 STKLD1 . . . serine/threonine kinase-like domain containing 1 . . . . . 0.09256 . 0.672386703 84.73696627 . . STMN1 0.648591503545553 0.345344772779999 0.00606372367444763 stathmin 1 FUNCTION: Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Phosphorylation at Ser- 16 may be required for axon formation during neurogenesis. Involved in the control of the learned and innate fear (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. Expression is strongest in fetal and adult brain, spinal cord, and cerebellum, followed by thymus, bone marrow, testis, and fetal liver. Expression is intermediate in colon, ovary, placenta, uterus, and trachea, and is readily detected at substantially lower levels in all other tissues examined. Lowest expression is found in adult liver. Present in much greater abundance in cells from patients with acute leukemia of different subtypes than in normal peripheral blood lymphocytes, non-leukemic proliferating lymphoid cells, bone marrow cells, or cells from patients with chronic lymphoid or myeloid leukemia. {ECO:0000269|PubMed:12676564, ECO:0000269|PubMed:1917919}.; lymphoreticular;ovary;umbilical cord;sympathetic chain;substantia nigra;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;urinary;adrenal cortex;pharynx;blood;lens;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;pancreas;lung;pia mater;placenta;head and neck;kidney;stomach;thymus;cerebellum; subthalamic nucleus;medulla oblongata;testis - interstitial;occipital lobe;fetal brain;temporal lobe;testis;globus pallidus;ciliary ganglion;pons;parietal lobe;cingulate cortex; 0.64591 0.38907 0.279402865 70.86577023 71.89047 1.76513 STMN1P1 . . . stathmin 1 pseudogene 1 . . . . . . . . . . . STMN1P2 . . . stathmin 1 pseudogene 2 . . . . . . . . . . . STMN2 0.932287578199384 0.0673800441850023 0.000332377615613454 stathmin 2 FUNCTION: Regulator of microtubule stability. When phosphorylated by MAPK8, stabilizes microtubules and consequently controls neurite length in cortical neurons. In the developing brain, negatively regulates the rate of exit from multipolar stage and retards radial migration from the ventricular zone (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Neuron specific.; ovary;salivary gland;sympathetic chain;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;cerebral cortex;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;aorta; amygdala;whole brain;dorsal root ganglion;medulla oblongata;superior cervical ganglion;occipital lobe;thalamus;adipose tissue;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.96113 0.24974 -0.009020804 52.8544468 1.6082 0.05227 STMN3 0.489817097149277 0.48900963625568 0.0211732665950439 stathmin 3 FUNCTION: Exhibits microtubule-destabilizing activity, which is antagonized by STAT3. {ECO:0000250}.; . TISSUE SPECIFICITY: Neuron specific.; . . 0.18084 0.11138 -0.053113545 49.38664779 12.2442 0.44358 STMN4 0.146519525068475 0.835405865333765 0.0180746095977598 stathmin 4 FUNCTION: Exhibits microtubule-destabilizing activity. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;whole body;ganglion;frontal lobe;tongue;hypothalamus;hippocampus;testis;spleen;head and neck;lens;brain; amygdala;whole brain;thalamus;occipital lobe;superior cervical ganglion;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;atrioventricular node;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.18961 0.11262 0.03689118 56.64071715 29.894 0.95397 STMND1 . . . stathmin domain containing 1 . . . . . . . . . 82.58687 1.92992 STOM 0.000669922832797632 0.742296514810644 0.257033562356558 stomatin FUNCTION: Regulates ion channel activity and transmembrane ion transport. Regulates ASIC2 and ASIC3 channel activity.; . TISSUE SPECIFICITY: Detected in erythrocytes (at protein level). Widely expressed. {ECO:0000269|PubMed:1547348, ECO:0000269|PubMed:23219802}.; ovary;sympathetic chain;skin;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;gall bladder;heart;cartilage;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;oesophagus;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;adipose tissue;placenta;ciliary ganglion;atrioventricular node;bone marrow; 0.39969 0.14827 0.281220278 71.07808445 192.29982 3.00630 STOML1 5.52734629268276e-05 0.686814574463689 0.313130152073384 stomatin like 1 . . TISSUE SPECIFICITY: Ubiquitously expressed at low levels. Expression is highest in brain. {ECO:0000269|PubMed:10997330, ECO:0000269|PubMed:9931417}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;synovium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pineal body;blood;lens;skeletal muscle;bile duct;lung;epididymis;mesenchyma;placenta;macula lutea;hippocampus;duodenum;kidney;stomach; amygdala;dorsal root ganglion;whole brain;superior cervical ganglion;subthalamic nucleus;hypothalamus;temporal lobe;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.23455 0.14915 -0.402212257 26.7338995 43.3537 1.25250 STOML2 0.529200678276011 0.470656310644159 0.000143011079829444 stomatin like 2 FUNCTION: Mitochondrial protein that probably regulates the biogenesis and the activity of mitochondria. Stimulates cardiolipin biosynthesis, binds cardiolipin-enriched membranes where it recruits and stabilizes some proteins including prohibitin and may therefore act in the organization of functional microdomains in mitochondrial membranes. Through regulation of the mitochondrial function may play a role into several biological processes including cell migration, cell proliferation, T-cell activation, calcium homeostasis and cellular response to stress. May play a role in calcium homeostasis through negative regulation of calcium efflux from mitochondria. Required for mitochondrial hyperfusion a pro-survival cellular response to stress which results in increased ATP production by mitochondria. May also regulate the organization of functional domains at the plasma membrane and play a role in T-cell activation through association with the T-cell receptor signaling complex and its regulation. {ECO:0000269|PubMed:17121834, ECO:0000269|PubMed:18641330, ECO:0000269|PubMed:19597348, ECO:0000269|PubMed:19944461, ECO:0000269|PubMed:21746876, ECO:0000269|PubMed:22623988}.; . TISSUE SPECIFICITY: Ubiquitously expressed at low levels. Expressed in lymphoid tissues (at protein level). {ECO:0000269|PubMed:10713127, ECO:0000269|PubMed:11435687, ECO:0000269|PubMed:18641330}.; myocardium;lymphoreticular;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;gall bladder;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;amnion;head and neck;kidney;stomach; heart;tumor; 0.87655 0.14979 -0.471992905 23.03609342 30.66945 0.97588 STOML3 1.97289725402202e-08 0.133563080841908 0.86643689942912 stomatin like 3 FUNCTION: Required for the function of many mechanoreceptors. Modulate mechanotransduction channels and acid-sensing ion channels (ASIC) proteins. Potentiates PIEZO1 and PIEZO2 function by increasing their sensitivity to mechanical stimulations. {ECO:0000250|UniProtKB:Q6PE84}.; . . . . 0.19446 0.12726 0.463046108 78.58575136 147.8329 2.64914 STON1 4.44985489455154e-08 0.36573779304004 0.634262162461411 stonin 1 FUNCTION: May be involved in the endocytic machinery. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11381094}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;oesophagus;endometrium;bone;testis;bladder;brain;unclassifiable (Anatomical System);heart;adrenal cortex;skeletal muscle;pancreas;lung;placenta;liver;spleen;kidney;mammary gland;stomach; uterus;superior cervical ganglion; . 0.10362 1.605718424 95.91295117 39.1195 1.15987 STON1-GTF2A1L 1.65449700249586e-14 0.0934201415563921 0.906579858443591 STON1-GTF2A1L readthrough FUNCTION: May be involved in the endocytic machinery. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11381094}.; unclassifiable (Anatomical System);prostate;lung;whole body;ovary;placenta;testis;brain;mammary gland;skeletal muscle; . . . 1.238210393 93.30620429 4681.32603 13.79102 STON2 0.568326467737997 0.431158214914317 0.000515317347685862 stonin 2 FUNCTION: Adapter protein involved in endocytic machinery. Involved in the synaptic vesicle recycling. May facilitate clathrin-coated vesicle uncoating. {ECO:0000269|PubMed:11381094, ECO:0000269|PubMed:11454741, ECO:0000269|PubMed:21102408}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11381094}.; frontal lobe;larynx;thyroid;liver;head and neck; superior cervical ganglion; 0.05087 0.09682 -0.413349049 25.84335928 5267.87977 14.99634 STOX1 2.34464637366538e-07 0.895454019682033 0.10454574585333 storkhead box 1 FUNCTION: Involved in regulating the levels of reactive oxidative species and reactive nitrogen species and in mitochondrial homeostasis in the placenta (PubMed:24738702). Required for regulation of inner ear epithelial cell proliferation via the AKT signaling pathway (By similarity). {ECO:0000250|UniProtKB:B2RQL2, ECO:0000269|PubMed:24738702}.; . TISSUE SPECIFICITY: Expressed in placenta, including the invasive extravillus trophoblast cells. {ECO:0000269|PubMed:15806103}.; unclassifiable (Anatomical System);ovary;lacrimal gland;colon;retina;pancreas;whole body;lung;endometrium;thyroid;liver;testis;spleen;germinal center;brain; amygdala;prefrontal cortex;pons;trigeminal ganglion; 0.09156 0.10650 1.447715105 95.14036329 556.53723 4.79281 STOX2 0.96321644241095 0.03676888101362 1.46765754298771e-05 storkhead box 2 . . . unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;prostate;optic nerve;lung;frontal lobe;cochlea;placenta;macula lutea;visual apparatus;testis;cervix;kidney;brain; medulla oblongata;occipital lobe;cerebellum peduncles;prefrontal cortex;parietal lobe;cingulate cortex; 0.45591 . -0.170835809 40.65227648 229.05218 3.26971 STPG1 0.00010643410734956 0.814658748515656 0.185234817376994 sperm tail PG-rich repeat containing 1 FUNCTION: May positively contribute to the induction of apoptosis triggered by O(6)-methylguanine. {ECO:0000269|PubMed:23028632}.; . . . . 0.07869 . 0.418953042 77.06416608 2465.83554 9.24901 STPG2 1.00566542470556e-12 0.0211995660002018 0.978800433998793 sperm tail PG-rich repeat containing 2 . . . . . 0.13597 . 1.221756288 93.21184242 5857.7505 15.87174 STPG2-AS1 . . . STPG2 antisense RNA 1 . . . . . . . . . . . STRA6 3.24590579415562e-08 0.921506536819004 0.0784934307219386 stimulated by retinoic acid 6 FUNCTION: May act as a high-affinity cell-surface receptor for the complex retinol-retinol binding protein (RBP/RBP4). Acts by removing retinol from RBP/RBP4 and transports it across the plasma membrane, where it can be metabolized. This mechanism does not depend on endocytosis. Binds to RBP/RBP4 with high affinity. Increases cellular retinol uptake from the retinol-RBP complex (By similarity). {ECO:0000250}.; DISEASE: Microphthalmia, syndromic, 9 (MCOPS9) [MIM:601186]: A rare clinical entity including as main characteristics anophthalmia or severe microphthalmia, and pulmonary hypoplasia or aplasia. Microphthalmia is a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. {ECO:0000269|PubMed:17273977, ECO:0000269|PubMed:17503335, ECO:0000269|PubMed:21901792}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Mutations in STRA6 may be a cause of isolated colobomatous microphthalmia, a disorder of the eye characterized by an abnormally small ocular globe. {ECO:0000269|PubMed:21901792}.; TISSUE SPECIFICITY: Broad expression. In adult eye expressed in sclera, retina, retinal pigment epithelium, and trabecular meshwork but not in choroid and iris. {ECO:0000269|PubMed:17273977}.; unclassifiable (Anatomical System);lymph node;heart;ovary;tongue;colon;parathyroid;choroid;skeletal muscle;uterus;optic nerve;lung;frontal lobe;endometrium;thyroid;placenta;iris;hypopharynx;testis;amniotic fluid;head and neck;cervix;kidney;brain; superior cervical ganglion;placenta;atrioventricular node;trigeminal ganglion; 0.17834 0.10257 0.295774947 71.64425572 1781.65066 7.79174 STRA8 0.00268491395995002 0.935751510921307 0.061563575118743 stimulated by retinoic acid 8 FUNCTION: Meiosis-inducer required for the transition into meiosis for both female and male germ cells. In female germ cells, required for premeiotic DNA replication and subsequent events in meiotic prophase (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed specifically in testis. {ECO:0000269|PubMed:12489526}.; . . 0.45296 0.14911 0.147123112 64.11299835 36.45183 1.09252 STRA13 0.591966927176029 0.368115698598942 0.0399173742250291 stimulated by retinoic acid 13 FUNCTION: DNA-binding component of the FA core complex involved in DNA damage repair and genome maintenance. Recruited to forks stalled by DNA interstrand cross-links, and required for cellular resistance to such lesions. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. Component of the APITD1/CENPS complex that is essential for the stable assembly of the outer kinetochore. Plays an important role in mitotic progression and chromosome segregation. {ECO:0000269|PubMed:19620631, ECO:0000269|Ref.5, ECO:0000269|Ref.6}.; . . ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;uterus;prostate;endometrium;synovium;iris;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pineal body;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;kidney;mammary gland;stomach;aorta; dorsal root ganglion;liver; 0.26036 0.08580 0.501689326 79.7888653 39.29751 1.16306 STRADA 0.0020153912770355 0.993581039818796 0.00440356890416884 STE20-related kinase adaptor alpha FUNCTION: Pseudokinase which, in complex with CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates STK11/LKB1. Adopts a closed conformation typical of active protein kinases and binds STK11/LKB1 as a pseudosubstrate, promoting conformational change of STK11/LKB1 in an active conformation. {ECO:0000269|PubMed:12805220, ECO:0000269|PubMed:14517248, ECO:0000269|PubMed:19892943}.; DISEASE: Note=A homozygous 7-kb deletion involving STRADA is a cause of a syndrome characterized by polyhydramnios, megalencephaly and symptomatic epilepsy.; . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;bone;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;pineal body;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;stomach;aorta;cerebellum;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; . 0.13246 0.062575634 58.74026893 44.92336 1.28700 STRADB 0.669632058274396 0.330155406143035 0.000212535582569408 STE20-related kinase adaptor beta FUNCTION: Pseudokinase which, in complex with CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates STK11/LKB1. Adopts a closed conformation typical of active protein kinases and binds STK11/LKB1 as a pseudosubstrate, promoting conformational change of STK11/LKB1 in an active conformation (By similarity). {ECO:0000250, ECO:0000269|PubMed:14517248}.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, testis, liver and colon. {ECO:0000269|PubMed:11161814, ECO:0000269|PubMed:12048196}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;iris;testis;amniotic fluid;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;pancreas;lung;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; . 0.25081 0.11652 -0.449946534 24.00330267 14.45402 0.52025 STRADBP1 . . . STE20-related kinase adaptor beta pseudogene 1 . . . . . . . . . . . STRAP 0.701829615941537 0.298015572661788 0.000154811396674893 serine/threonine kinase receptor associated protein FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. STRAP plays a role in the cellular distribution of the SMN complex. Negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by significantly reducing the association of PDPK1 with 14-3-3 protein. {ECO:0000269|PubMed:16251192, ECO:0000269|PubMed:18984161}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;cervix;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;larynx;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; amygdala;whole brain;medulla oblongata;subthalamic nucleus;occipital lobe;hypothalamus;globus pallidus;cingulate cortex; 0.19022 0.12496 -0.161524709 41.6430762 32.02303 1.00629 STRBP 0.999902421283963 9.75786795428208e-05 3.64941901667885e-11 spermatid perinuclear RNA binding protein FUNCTION: Involved in spermatogenesis and sperm function. Plays a role in regulation of cell growth. Binds to double-stranded DNA and RNA. Binds most efficiently to poly(I:C) RNA than to poly(dI:dC) DNA. Binds also to single-stranded poly(G) RNA. Binds non-specifically to the mRNA PRM1 3'-UTR and adenovirus VA RNA (By similarity). {ECO:0000250}.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;lung;cornea;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion; 0.93834 0.11088 -0.448125345 24.19202642 45.32038 1.29268 STRC 0.00532184460844672 0.994633320707534 4.48346840194601e-05 stereocilin FUNCTION: Essential to the formation of horizontal top connectors between outer hair cell stereocilia. {ECO:0000250}.; DISEASE: Deafness, autosomal recessive, 16 (DFNB16) [MIM:603720]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:11687802}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness-infertility syndrome (DIS) [MIM:611102]: Characterized by deafness and infertility and is caused by large contiguous gene deletions at 15q15.3 that removes both STRC and CATSPER2 genes. {ECO:0000269|PubMed:17098888}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lung;frontal lobe;ovary;placenta;testis;colon;parathyroid;kidney;brain;stomach; . 0.14418 . . . 4206.67564 12.90457 STRCP1 . . . stereocilin pseudogene 1 . . . . . 0.14418 . . . . . STRIP1 0.130901315990928 0.869090747513106 7.93649596584685e-06 striatin interacting protein 1 FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. {ECO:0000269|PubMed:21834987}.; . . . . 0.14682 0.10600 -1.3098007 4.847841472 39.05666 1.15784 STRIP2 7.35176598741971e-10 0.966038865507226 0.0339611337575979 striatin interacting protein 2 FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. {ECO:0000269|PubMed:21834987}.; . . . . 0.19078 0.10875 -0.641086234 16.6784619 712.58921 5.30374 STRN 0.969336393172942 0.0306635911610837 1.56659746236608e-08 striatin FUNCTION: Calmodulin-binding protein which may function as scaffolding or signaling protein and may play a role in dendritic Ca(2+) signaling.; . TISSUE SPECIFICITY: Preferentially expressed in brain. {ECO:0000269|PubMed:9693043}.; unclassifiable (Anatomical System);heart;islets of Langerhans;colon;blood;skeletal muscle;skin;retina;bone marrow;uterus;breast;lung;cerebral cortex;visual apparatus;germinal center;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.16896 0.10486 -0.201976964 38.98325077 178.85571 2.90500 STRN3 0.447040096169006 0.552948857373014 1.10464579798705e-05 striatin 3 FUNCTION: Binds calmodulin in a calcium dependent manner. May function as scaffolding or signaling protein.; . . ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);heart;islets of Langerhans;adrenal cortex;blood;bile duct;breast;pancreas;lung;adrenal gland;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach; amygdala;uterus corpus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.83417 0.13494 -0.576764155 18.7839113 5246.84497 14.93365 STRN4 0.999575131657329 0.000424867028432316 1.3142388338123e-09 striatin 4 FUNCTION: Binds calmodulin in a calcium dependent manner. May function as scaffolding or signaling protein.; . . ovary;salivary gland;colon;parathyroid;skin;uterus;prostate;whole body;oesophagus;endometrium;larynx;bone;thyroid;iris;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;breast;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;pons;skeletal muscle; 0.22162 0.11997 -1.285933373 5.083746167 424.12856 4.30149 STS 0.981414315787146 0.018572307174163 1.33770386911771e-05 steroid sulfatase (microsomal), isozyme S FUNCTION: Conversion of sulfated steroid precursors to estrogens during pregnancy.; DISEASE: Ichthyosis, X-linked (IXL) [MIM:308100]: A keratinization disorder manifesting with mild erythroderma and generalized exfoliation of the skin within a few weeks after birth. Affected boys later develop large, polygonal, dark brown scales, especially on the neck, extremities, trunk, and buttocks. {ECO:0000269|PubMed:10679952, ECO:0000269|PubMed:10844566, ECO:0000269|PubMed:1539590, ECO:0000269|PubMed:9252398}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;hypothalamus;blood;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;thalamus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;placenta;prefrontal cortex;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.22419 0.85641 -0.178111357 40.44585987 40.19683 1.18167 STSP1 . . . steroid sulfatase (microsomal) pseudogene 1 . . . . . . . . . . . STT3A 0.978952343158655 0.0210476506648755 6.17646960076506e-09 STT3A, catalytic subunit of the oligosaccharyltransferase complex FUNCTION: Catalytic subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). SST3A seems to be involved in complex substrate specificity. STT3A is present in the majority of OST complexes and mediates cotranslational N-glycosylation of most sites on target proteins, while STT3B-containing complexes are required for efficient cotranslational glycosylation and mediate glycosylation of sites that have been skipped by STT3A. {ECO:0000269|PubMed:19167329}.; . TISSUE SPECIFICITY: Expressed at high levels in placenta, liver, muscle and pancreas, and at very low levels in brain, lung and kidney. Expressed in skin fibroblasts (at protein level). {ECO:0000269|PubMed:12887896}.; . . 0.39779 . -0.648365105 16.35999056 12.5742 0.45886 STT3A-AS1 . . . STT3A antisense RNA 1 . . . . . . . . . . . STT3B 0.980028091148833 0.0199718820308027 2.6820364221972e-08 STT3B, catalytic subunit of the oligosaccharyltransferase complex FUNCTION: Catalytic subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). STT3B is present in a small subset of OST complexes and mediates both cotranslational and post-translational N-glycosylation of target proteins: STT3B-containing complexes are required for efficient cotranslational glycosylation and while they are less competent than STT3A-containing complexes for cotranslational glycosylation, they have the ability to mediate glycosylation of some nascent sites that are not accessible for STT3A. STT3B-containing complexes also act post-translationally and mediate modification of skipped glycosylation sites in unfolded proteins. Plays a role in ER-associated degradation (ERAD) pathway that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins by mediating N-glycosylation of unfolded proteins, which are then recognized by the ERAD pathway and targeted for degradation. Mediates glycosylation of the disease variant AMYL- TTR 'Asp-38' of TTR at 'Asn-118', leading to its degradation. {ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:22607976}.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, muscle, kidney and pancreas. Expressed in skin fibroblasts (at protein level). {ECO:0000269|PubMed:12887896}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;thyroid;pituitary gland;testis;amniotic fluid;spinal ganglion;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;visual apparatus;duodenum;liver;head and neck;cervix;kidney;stomach;aorta; superior cervical ganglion;testis - interstitial;placenta;testis; 0.60030 0.16763 -0.758599262 13.32861524 35.9408 1.07941 STUB1 0.0425338864217666 0.951466319329014 0.00599979424921889 STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF- BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner (PubMed:23973223). {ECO:0000269|PubMed:10330192, ECO:0000269|PubMed:11146632, ECO:0000269|PubMed:11557750, ECO:0000269|PubMed:15466472, ECO:0000269|PubMed:19103148, ECO:0000269|PubMed:19567782, ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:23990462}.; DISEASE: Spinocerebellar ataxia, autosomal recessive, 16 (SCAR16) [MIM:615768]: Spinocerebellar ataxia defines a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR16 is characterized by truncal and limb ataxia resulting in gait instability. Additionally, patients may show dysarthria, nystagmus, spasticity of the lower limbs, and mild peripheral sensory neuropathy. {ECO:0000269|PubMed:24113144, ECO:0000269|PubMed:24312598, ECO:0000269|PubMed:24719489, ECO:0000269|PubMed:24742043, ECO:0000269|PubMed:25258038}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart, pancreas, brain and placenta. Detected in kidney, liver and lung. {ECO:0000269|PubMed:10330192, ECO:0000269|PubMed:11435423}.; lymphoreticular;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;synovium;larynx;bone;iris;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;caudate nucleus;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;kidney;parietal lobe;cerebellum; 0.41511 0.47945 -0.271755481 34.31823543 37.32673 1.11313 STX1A 0.910475757164848 0.0893857421888233 0.000138500646328376 syntaxin 1A FUNCTION: Plays a role in hormone and neurotransmitter exocytosis (By similarity). Potentially involved in docking of synaptic vesicles at presynaptic active zones. May mediate Ca(2+)- regulation of exocytosis acrosomal reaction in sperm. {ECO:0000250|UniProtKB:P32851}.; DISEASE: Note=STX1A is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. {ECO:0000305|PubMed:9311751}.; TISSUE SPECIFICITY: Isoform 1 is highly expressed in embryonic spinal chord and ganglia and in adult cerebellum and cerebral cortex. Isoform 2 is expressed in heart, liver, fat, skeletal muscle, kidney and brain. {ECO:0000269|PubMed:10644452}.; unclassifiable (Anatomical System);lymph node;ovary;islets of Langerhans;hypothalamus;sympathetic chain;fovea centralis;choroid;lens;skeletal muscle;retina;bile duct;optic nerve;lung;frontal lobe;endometrium;bone;macula lutea;visual apparatus;hippocampus;pituitary gland;testis;kidney;brain;stomach;cerebellum; amygdala;whole brain;medulla oblongata;superior cervical ganglion;occipital lobe;temporal lobe;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.47888 0.43756 -0.361761279 28.6329323 10.57097 0.38399 STX1B 0.944474732619076 0.0554841399185317 4.11274623924668e-05 syntaxin 1B FUNCTION: Potentially involved in docking of synaptic vesicles at presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm (By similarity). {ECO:0000250}.; DISEASE: Generalized epilepsy with febrile seizures plus 9 (GEFSP9) [MIM:616172]: An autosomal dominant neurologic disorder characterized by febrile and/or afebrile seizures manifesting in early childhood. Seizure are variable and include generalized tonic-clonic, atonic, myoclonic, complex partial, and absence types. Most patients have remission of seizures later in childhood with no residual neurologic deficits. Rarely, patients may show mild developmental delay or mild intellectual disabilities. {ECO:0000269|PubMed:25362483}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;atrioventricular node; 0.22761 0.14229 -0.163345027 41.24793583 5.61252 0.20995 STX2 0.000386515733492941 0.956614259896611 0.0429992243698958 syntaxin 2 FUNCTION: Essential for epithelial morphogenesis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm.; . . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;skin;uterus;frontal lobe;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;lung;placenta;visual apparatus;hippocampus;liver;alveolus;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.15544 0.23396 0.573279816 82.08303845 596.94941 4.94334 STX3 0.630609378340344 0.369086679860803 0.000303941798852942 syntaxin 3 FUNCTION: Potentially involved in docking of synaptic vesicles at presynaptic active zones.; . . ovary;salivary gland;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;testis;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;urinary;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;aorta;stomach; superior cervical ganglion;placenta;trigeminal ganglion; 0.13099 0.17453 0.395088462 76.15003539 204.05234 3.08420 STX4 9.66202483351248e-05 0.79769908988864 0.202204289863024 syntaxin 4 FUNCTION: Plasma membrane t-SNARE that mediates docking of transport vesicles. Necessary for the translocation of SLC2A4 from intracellular vesicles to the plasma membrane. Together with STXB3 and VAMP2, may also play a role in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes (By similarity). May also play a role in docking of synaptic vesicles at presynaptic active zones. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in neutrophils and neutrophil- differentiated HL-60 cells. Expression in neutrophils increases with differentiation. {ECO:0000269|PubMed:10080545}.; smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; adrenal cortex; 0.09825 . -0.582225231 18.44184949 29.98664 0.95812 STX5 0.362948405820287 0.63453688346441 0.00251471071530281 syntaxin 5 FUNCTION: Mediates endoplasmic reticulum to Golgi transport. Together with p115/USO1 and GM130/GOLGA2, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus. {ECO:0000250|UniProtKB:Q08851}.; . . lymphoreticular;smooth muscle;ovary;umbilical cord;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;amniotic fluid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;epidermis;lung;adrenal gland;placenta;head and neck;kidney;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.35757 0.14300 -0.358119787 29.16371786 65.54925 1.66625 STX6 0.0198491170645574 0.96175321425438 0.0183976686810631 syntaxin 6 FUNCTION: Involved in intracellular vesicle trafficking.; . . unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;blood;skin;skeletal muscle;bone marrow;uterus;endometrium;bone;placenta;thyroid;visual apparatus;head and neck;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.11325 0.17021 -0.538132194 20.26421326 21.51311 0.72474 STX7 0.00426311559874846 0.96184404735904 0.0338928370422118 syntaxin 7 FUNCTION: May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes.; . TISSUE SPECIFICITY: Highest expression is found in placenta followed by heart, skeletal muscle, kidney and brain. Low expression is found in pancreas, lung and liver.; . . 0.16239 0.16614 -0.095386216 46.48502005 18.39719 0.63746 STX8 0.000144082943170255 0.862183863755816 0.137672053301014 syntaxin 8 FUNCTION: Vesicle trafficking protein that functions in the early secretory pathway, possibly by mediating retrograde transport from cis-Golgi membranes to the ER.; . TISSUE SPECIFICITY: Highly expressed in heart. Also found in brain, kidney, liver, lung, placenta, skeletal muscle, spleen and pancreas.; ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;medulla oblongata;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.13254 0.20070 0.637604436 83.77565464 105.28368 2.22100 STX8P1 . . . syntaxin 8 pseudogene 1 . . . . . . . . . . . STX10 3.56682385992079e-10 0.0483978917878401 0.951602107855477 syntaxin 10 FUNCTION: SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000269|PubMed:18195106}.; . TISSUE SPECIFICITY: Expressed at high levels in heart, skeletal muscle and pancreas.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;bone marrow;retina;uterus;prostate;optic nerve;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach;thymus; cingulate cortex; 0.16470 0.12076 -0.071520315 48.34866714 65.01937 1.65746 STX11 0.0200260555260361 0.743199429377253 0.236774515096711 syntaxin 11 FUNCTION: SNARE that acts to regulate protein transport between late endosomes and the trans-Golgi network.; DISEASE: Familial hemophagocytic lymphohistiocytosis 4 (FHL4) [MIM:603552]: A rare disorder characterized by immune dysregulation with hypercytokinemia, defective function of natural killer cell, and massive infiltration of several organs by activated lymphocytes and macrophages. The clinical features of the disease include fever, hepatosplenomegaly, cytopenia, and less frequently neurological abnormalities ranging from irritability and hypotonia to seizures, cranial nerve deficits and ataxia. {ECO:0000269|PubMed:15703195}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.22737 0.18323 0.64123826 83.97617363 486.20271 4.53989 STX12 0.896720265506838 0.103079411219016 0.000200323274146585 syntaxin 12 FUNCTION: SNARE that acts to regulate protein transport between late endosomes and the trans-Golgi network. The SNARE complex containing STX6, STX12, VAMP4 and VTI1A mediates vesicle fusion (in vitro) (By similarity). {ECO:0000250}.; . . . . 0.61432 0.11880 -0.075159878 47.78839349 16.31193 0.57821 STX16 0.235503144787157 0.763013153627457 0.00148370158538565 syntaxin 16 FUNCTION: SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000269|PubMed:18195106}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;brain;amygdala;heart;cartilage;tongue;pineal body;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;oral cavity;muscle;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;thymus; amygdala;thalamus;superior cervical ganglion;globus pallidus;cingulate cortex;skeletal muscle;parietal lobe; 0.82411 0.08226 -0.247889024 35.98726115 323.4417 3.82089 STX16-NPEPL1 . . . STX16-NPEPL1 readthrough (NMD candidate) . . . . . . . . . . . STX17 0.0849679795016525 0.905305887249872 0.00972613324847546 syntaxin 17 FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor- attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. STX17 is a SNARE of the autophagosome involved in autophagy through the direct control of autophagosome membrane fusion with the lysosome membrane (PubMed:23217709, PubMed:25686604). May also play a role in the early secretory pathway where it may maintain the architecture of the endoplasmic reticulum-Golgi intermediate compartment/ERGIC and Golgi and/or regulate transport between the endoplasmic reticulum, the ERGIC and the Golgi (PubMed:21545355). {ECO:0000269|PubMed:21545355, ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686604}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skeletal muscle; 0.19600 0.11906 0.148941568 64.31941496 291.63749 3.65239 STX17-AS1 . . . STX17 antisense RNA 1 . . . . . . . . . . . STX18 1.16778720480768e-06 0.804079092840969 0.195919739371826 syntaxin 18 FUNCTION: Syntaxin that may be involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER. {ECO:0000269|PubMed:15029241}.; . TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;peripheral nerve;cerebellum; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;pons;trigeminal ganglion;skeletal muscle; 0.15344 0.16141 0.084621747 60.31493277 774.2267 5.50804 STX18-AS1 . . . STX18 antisense RNA 1 (head to head) . . . . . . . . . . . STX18-IT1 . . . STX18 intronic transcript 1 . . . . . . . . . . . STX18P1 . . . syntaxin 18 pseudogene 1 . . . . . . . . . . . STX19 1.15387050808179e-05 0.20726551289126 0.79272294840366 syntaxin 19 . . . unclassifiable (Anatomical System);skin; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19602 . 0.25917371 70.05779665 33.75343 1.03973 STXBP1 0.999882943227088 0.000117056716057476 5.68548084803849e-11 syntaxin binding protein 1 FUNCTION: May participate in the regulation of synaptic vesicle docking and fusion, possibly through interaction with GTP-binding proteins. Essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. May play a role in determining the specificity of intracellular fusion reactions.; . TISSUE SPECIFICITY: Brain and spinal cord. Highly enriched in axons.; . . 0.69521 0.22085 -0.692458599 14.96815287 12.9714 0.47270 STXBP2 7.76317734429722e-05 0.981155334225431 0.0187670340011261 syntaxin binding protein 2 FUNCTION: Involved in intracellular vesicle trafficking and vesicle fusion with membranes. Contributes to the granule exocytosis machinery through interaction with soluble N- ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins that regulate membrane fusion. Regulates cytotoxic granule exocytosis in natural killer (NK) cells. {ECO:0000269|PubMed:19804848, ECO:0000269|PubMed:19884660}.; . TISSUE SPECIFICITY: Placenta, lung, liver, kidney and pancreas, as well as in peripheral blood lymphocytes.; medulla oblongata;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;thyroid;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;hippocampus;liver;hypopharynx;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach; prostate;testis - interstitial;lung;testis - seminiferous tubule;thyroid;placenta;testis;white blood cells;whole blood;thymus; 0.54261 0.13219 0.42623145 77.29417315 302.00485 3.70158 STXBP3 7.39663613294889e-06 0.995285168463084 0.00470743490078252 syntaxin binding protein 3 FUNCTION: Together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes. {ECO:0000250}.; . TISSUE SPECIFICITY: Megakaryocytes and platelets.; . . 0.30329 0.14582 -0.514264485 21.41424864 192.48552 3.00897 STXBP4 1.41709360491401e-14 0.0236729417148822 0.976327058285104 syntaxin binding protein 4 FUNCTION: Plays a role in the translocation of transport vesicles from the cytoplasm to the plasma membrane. Inhibits the translocation of SLC2A4 from intracellular vesicles to the plasma membrane by STX4A binding and preventing the interaction between STX4A and VAMP2. Stimulation with insulin disrupts the interaction with STX4A, leading to increased levels of SLC2A4 at the plasma membrane. May also play a role in the regulation of insulin release by pancreatic beta cells after stimulation by glucose (By similarity). {ECO:0000250}.; . . optic nerve;islets of Langerhans; . 0.12482 0.09112 0.174625237 65.9648502 190.65241 2.99567 STXBP5 0.999991599632041 8.40036795832339e-06 7.69389698539381e-16 syntaxin binding protein 5 FUNCTION: Plays a regulatory role in calcium-dependent exocytosis and neurotransmitter release. Inhibits membrane fusion between transport vesicles and the plasma membrane. May modulate the assembly of trans-SNARE complexes between transport vesicles and the plasma membrane. Inhibits translocation of GLUT4 from intracellular vesicles to the plasma membrane. Competes with STXBP1 for STX1 binding (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;blood;retina;breast;uterus;prostate;lung;cerebral cortex;bone;placenta;iris;liver;testis;germinal center;brain;pineal gland;mammary gland;bladder;stomach;thymus; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.17577 0.14280 -0.396754488 26.97570182 2595.84718 9.53666 STXBP5-AS1 . . . STXBP5 antisense RNA 1 . . . . . . . . . . . STXBP5L 0.99994837069221 5.16293077872608e-05 2.62570367175988e-15 syntaxin binding protein 5 like FUNCTION: May play a role in vesicle trafficking and exocytosis. {ECO:0000305}.; . TISSUE SPECIFICITY: Detected in kidney, hippocampus and lung carcinoma. {ECO:0000269|PubMed:14767561}.; unclassifiable (Anatomical System);hippocampus;brain;pineal gland;skeletal muscle; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;caudate nucleus;atrioventricular node;pons;trigeminal ganglion;skin; 0.25231 0.10307 -0.43902969 24.63434772 1445.05593 7.08920 STXBP6 0.0978976738904898 0.866819385295053 0.0352829408144573 syntaxin binding protein 6 FUNCTION: Forms non-fusogenic complexes with SNAP25 and STX1A and may thereby modulate the formation of functional SNARE complexes and exocytosis.; . TISSUE SPECIFICITY: Detected at low levels in brain, and at very low levels in heart, adrenal gland, testis, liver and kidney. {ECO:0000269|PubMed:12145319}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;thalamus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;cingulate cortex; 0.23439 0.09253 -0.229483771 36.86010852 12.83864 0.46849 STYK1 1.53641100905639e-05 0.860451491367263 0.139533144522647 serine/threonine/tyrosine kinase 1 FUNCTION: Probable tyrosine protein-kinase, which has strong transforming capabilities on a variety of cell lines. When overexpressed, it can also induce tumor cell invasion as well as metastasis in distant organs. May act by activating both MAP kinase and phosphatidylinositol 3'-kinases (PI3K) pathways (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain, placenta and prostate. Expressed in tumor cells such as hepatoma cells L-02, cervix carcinoma cells HeLa, ovary cancer cells Ho8910 and chronic myelogenous leukemia cells K-562, but not in other tumor cells such as epidermoid carcinoma (A-431). Undetectable in most normal lung tissues, widely expressed in lung cancers. {ECO:0000269|PubMed:12841579, ECO:0000269|PubMed:15150103, ECO:0000269|PubMed:17298854}.; unclassifiable (Anatomical System);uterus;prostate;lung;larynx;gum;colon;head and neck;brain; dorsal root ganglion;amygdala;superior cervical ganglion;prefrontal cortex;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.30034 0.11766 0.176444282 66.07100731 48.89567 1.36414 STYX 0.97206861803257 0.0279239717537679 7.41021366247394e-06 serine/threonine/tyrosine interacting protein FUNCTION: Catalytically inactive phosphatase. Acts as a nuclear anchor for MAPK1/MAPK3 (ERK1/ERK2). Modulates cell-fate decisions and cell migration by spatiotemporal regulation of MAPK1/MAPK3 (ERK1/ERK2). Seems to play a role in spermiogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:23847209}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;amniotic fluid;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;islets of Langerhans;pharynx;blood;skeletal muscle;bile duct;breast;pia mater;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.34326 0.10535 -0.163345027 41.24793583 41.45856 1.21063 STYXL1 0.00974654300814003 0.941723216172194 0.0485302408196657 serine/threonine/tyrosine interacting-like 1 FUNCTION: Probable pseudophosphatase. Contains a Ser residue instead of a conserved Cys residue in the dsPTPase catalytic loop which probably renders it catalytically inactive as a phosphatase. The binding pocket may be however sufficiently preserved to bind phosphorylated substrates, and maybe protect them from phosphatases.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;cerebral cortex;bone;pituitary gland;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;peripheral nerve; testis; 0.04703 0.08839 0.040529541 57.15380986 59.38626 1.56255 SUB1 0.800760313727209 0.193817516289052 0.00542216998373911 SUB1 homolog, transcriptional regulator FUNCTION: General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA). {ECO:0000269|PubMed:16605275, ECO:0000269|PubMed:16689930, ECO:0000269|PubMed:7628453, ECO:0000269|PubMed:8062391, ECO:0000269|PubMed:8062392, ECO:0000269|PubMed:9360603, ECO:0000269|PubMed:9482861}.; . . myocardium;lymphoreticular;smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;cerebral cortex;larynx;bone;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;hypothalamus;temporal lobe;white blood cells;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.72977 0.14896 -0.009020804 52.8544468 5.31225 0.19622 SUB1P1 . . . SUB1 homolog, transcriptional regulator pseudogene 1 . . . . . . . . . . . SUB1P2 . . . SUB1 homolog, transcriptional regulator pseudogene 2 . . . . . . . . . . . SUB1P3 . . . SUB1 homolog, transcriptional regulator pseudogene 3 . . . . . . . . . . . SUB1P4 . . . SUB1 homolog, transcriptional regulator pseudogene 4 . . . . . . . . . . . SUCLA2 0.0306681591456276 0.967310431670012 0.00202140918436094 succinate-CoA ligase, ADP-forming, beta subunit FUNCTION: Catalyzes the ATP-dependent ligation of succinate and CoA to form succinyl-CoA. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Not expressed in liver and lung. {ECO:0000269|PubMed:9765291}.; . . 0.75579 0.88177 -0.069700724 48.54328851 441.09469 4.37444 SUCLA2-AS1 . . . SUCLA2 antisense RNA 1 . . . . . . . . . . . SUCLA2P1 . . . succinate-CoA ligase, ADP-forming, beta subunit pseudogene 1 . . . . . . . . . . . SUCLA2P2 . . . succinate-CoA ligase, ADP-forming, beta subunit pseudogene 2 . . . . . . . . . . . SUCLA2P3 . . . succinate-CoA ligase, ADP-forming, beta subunit pseudogene 3 . . . . . . . . . . . SUCLG1 0.0597686458354184 0.923320984153529 0.0169103700110526 succinate-CoA ligase, alpha subunit FUNCTION: Catalyzes the ATP- or GTP-dependent ligation of succinate and CoA to form succinyl-CoA. The nature of the beta subunit determines the nucleotide specificity (By similarity). {ECO:0000250}.; DISEASE: Mitochondrial DNA depletion syndrome 9 (MTDPS9) [MIM:245400]: A severe disorder due to mitochondrial dysfunction. It is characterized by infantile onset of hypotonia, lactic acidosis, severe psychomotor retardation, progressive neurologic deterioration, and excretion of methylmalonic acid. {ECO:0000269|PubMed:17668387, ECO:0000269|PubMed:19526370, ECO:0000269|PubMed:20453710, ECO:0000269|PubMed:20693550}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.16263 0.53493 -0.47017169 23.25430526 38.99703 1.15581 SUCLG2 3.28018373617218e-05 0.803527087167188 0.196440110995451 succinate-CoA ligase, GDP-forming, beta subunit FUNCTION: Catalyzes the GTP-dependent ligation of succinate and CoA to form succinyl-CoA. {ECO:0000250}.; . TISSUE SPECIFICITY: Mainly expressed in liver, kidney, heart, spleen and skeletal muscle. Also found in intestine and colon, and in low amounts in lung, brain, prostate, testis and ovary. {ECO:0000269|PubMed:9765291}.; myocardium;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;atrium;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;lens;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;fetal liver;trachea;thyroid;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.23163 0.49756 0.619191319 83.36282142 3103.91859 10.59855 SUCLG2-AS1 . . . SUCLG2 antisense RNA 1 (head to head) . . . . . . . . . . . SUCLG2P1 . . . succinate-CoA ligase, GDP-forming, beta subunit pseudogene 1 . . . . . . . . . . . SUCLG2P2 . . . succinate-CoA ligase, GDP-forming, beta subunit pseudogene 2 . . . . . . . . . . . SUCLG2P3 . . . succinate-CoA ligase, GDP-forming, beta subunit pseudogene 3 . . . . . . . . . . . SUCLG2P4 . . . succinate-CoA ligase, GDP-forming, beta subunit pseudogene 4 . . . . . . . . . . . SUCNR1 6.24867481072073e-08 0.0729661775550304 0.927033759958221 succinate receptor 1 FUNCTION: Receptor for succinate. {ECO:0000269|PubMed:15141213}.; . TISSUE SPECIFICITY: Expressed specifically in kidney. {ECO:0000269|PubMed:11273702}.; kidney; kidney; 0.10163 0.10272 -0.315847836 31.68789809 24.75166 0.81247 SUCO 0.302497744042791 0.697502198833156 5.71240534799265e-08 SUN domain containing ossification factor FUNCTION: Required for bone modeling during late embryogenesis. Regulates type I collagen synthesis in osteoblasts during their postnatal maturation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in pancreas and testis and to a lower extent in prostate, ovary, heart, thymus, small intestine and spleen. {ECO:0000269|PubMed:10673381}.; . . 0.05783 0.23483 -1.236390924 5.520169851 3119.81455 10.61387 SUDS3 0.00759610717840473 0.977040297605269 0.0153635952163265 SDS3 homolog, SIN3A corepressor complex component FUNCTION: Regulatory protein which represses transcription and augments histone deacetylase activity of HDAC1. May have a potential role in tumor suppressor pathways through regulation of apoptosis. May function in the assembly and/or enzymatic activity of the mSin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes. {ECO:0000269|PubMed:12724404, ECO:0000269|PubMed:21239494}.; . TISSUE SPECIFICITY: Expressed in various cancer cell ines. {ECO:0000269|PubMed:12724404}.; . . 0.21009 0.10854 -0.229483771 36.86010852 29.42985 0.94071 SUDS3P1 . . . SDS3 homolog, SIN3A corepressor complex component pseudogene 1 . . . . . . . . . . . SUFU 0.99916148458521 0.000838508526336465 6.88845336496509e-09 SUFU negative regulator of hedgehog signaling FUNCTION: Negative regulator in the hedgehog signaling pathway. Down-regulates GLI1-mediated transactivation of target genes (PubMed:15367681, PubMed:24311597, PubMed:24217340). Down- regulates GLI2-mediated transactivation of target genes (PubMed:24311597, PubMed:24217340). Part of a corepressor complex that acts on DNA-bound GLI1. May also act by linking GLI1 to BTRC and thereby targeting GLI1 to degradation by the proteasome. Sequesters GLI1, GLI2 and GLI3 in the cytoplasm, this effect is overcome by binding of STK36 to both SUFU and a GLI protein (PubMed:10806483, PubMed:24217340). Negative regulator of beta- catenin signaling. Regulates the formation of either the repressor form (GLI3R) or the activator form (GLI3A) of the full length form of GLI3 (GLI3FL). GLI3FL is complexed with SUFU in the cytoplasm and is maintained in a neutral state. Without the Hh signal, the SUFU-GLI3 complex is recruited to cilia, leading to the efficient processing of GLI3FL into GLI3R. When Hh signaling is initiated, SUFU dissociates from GLI3FL and the latter translocates to the nucleus, where it is phosphorylated, destabilized, and converted to a transcriptional activator (GLI3A). Required for normal embryonic development. Required for the proper formation of hair follicles and the control of epidermal differentiation (By similarity). {ECO:0000250|UniProtKB:Q9Z0P7, ECO:0000269|PubMed:10559945, ECO:0000269|PubMed:10564661, ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:12068298, ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:15367681, ECO:0000269|PubMed:22365972, ECO:0000269|PubMed:24217340, ECO:0000269|PubMed:24311597}.; . TISSUE SPECIFICITY: Ubiquitous in adult tissues. Detected in osteoblasts of the perichondrium in the developing limb of 12-week old embryos. Isoform 1 is detected in fetal brain, lung, kidney and testis. Isoform 2 is detected in fetal testis, and at much lower levels in fetal brain, lung and kidney. {ECO:0000269|PubMed:10559945, ECO:0000269|PubMed:10564661}.; . . 0.76693 0.19444 -0.580403979 18.58928993 42.63843 1.23712 SUGCT . . . succinyl-CoA:glutarate-CoA transferase FUNCTION: Catalyzes the succinyl-CoA-dependent conversion of glutarate to glutaryl-CoA. Can use different dicarboxylic acids as CoA acceptors, the preferred ones are glutarate, succinate, adipate, and 3-hydroxymethylglutarate. {ECO:0000269|PubMed:23893049}.; . TISSUE SPECIFICITY: Highly expressed in kidney. Intermediate expression in liver, skeletal muscle and pancreas. Little to no expression detected in other tissues examined. {ECO:0000269|PubMed:11829489}.; . . . 0.17087 0.018483465 55.44939844 74.3847 1.80163 SUGP1 0.9996355600486 0.000364439047038864 9.04361121982549e-10 SURP and G-patch domain containing 1 FUNCTION: Plays a role in pre-mRNA splicing.; . TISSUE SPECIFICITY: Detected in adult testis and heart, and in adult and fetal brain, kidney and skeletal muscle. {ECO:0000269|PubMed:12594045}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;skeletal muscle; 0.12030 0.13872 -1.021348453 7.997169144 953.44852 5.97597 SUGP2 0.999366871236062 0.000633128621716066 1.42222141260562e-10 SURP and G-patch domain containing 2 FUNCTION: May play a role in mRNA splicing. {ECO:0000305}.; . TISSUE SPECIFICITY: Detected in adult testis, and in fetal brain and kidney. {ECO:0000269|PubMed:12594045}.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;developmental;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach; dorsal root ganglion;amygdala;whole brain;thalamus;medulla oblongata;superior cervical ganglion;testis - interstitial;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;fetal brain;prefrontal cortex;globus pallidus;testis;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.47872 0.09856 0.385781814 75.678226 228.78802 3.26735 SUGT1 0.977752129164094 0.0222436479850157 4.22285088986947e-06 SGT1 homolog, MIS12 kinetochore complex assembly cochaperone FUNCTION: May play a role in ubiquitination and subsequent proteasomal degradation of target proteins.; . . ovary;colon;parathyroid;fovea centralis;choroid;bone marrow;retina;prostate;optic nerve;bone;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;lens;breast;pancreas;lung;macula lutea;cervix;kidney;stomach; dorsal root ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.25021 0.09521 -0.183570861 39.95046001 22.99839 0.76745 SUGT1P1 . . . SGT1 homolog, MIS12 kinetochore complex assembly cochaperone pseudogene 1 . . . . . . . . . . . SUGT1P2 . . . SGT1 homolog, MIS12 kinetochore complex assembly cochaperone pseudogene 2 . . . . . . . . . . . SUGT1P3 . . . SGT1 homolog, MIS12 kinetochore complex assembly cochaperone pseudogene 3 . . . lung;testis;lens;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.22674 . . . . . SULF1 0.879274682816298 0.120725296401459 2.07822430734315e-08 sulfatase 1 FUNCTION: Exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity. It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin. Diminishes HSPG (heparan sulfate proteoglycans) sulfation, inhibits signaling by heparin-dependent growth factors, diminishes proliferation, and facilitates apoptosis in response to exogenous stimulation.; . TISSUE SPECIFICITY: Expressed at highest levels in testis, stomach, skeletal muscle, lung, kidney, pancreas, small intestine and colon. It is also detected in normal ovarian surface epithelial cells. Down-regulation seen in ovarian carcinoma cell lines, ovarian cancers, breast, pancreatic, renal and hepatocellular carcinoma cell lines.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;muscle;urinary;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;heart;testis;ciliary ganglion;trigeminal ganglion; 0.67671 0.15046 -0.484940685 22.75300778 282.99225 3.60070 SULF2 0.878046240550913 0.121953653966171 1.05482915990158e-07 sulfatase 2 FUNCTION: Exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity. It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin.; . TISSUE SPECIFICITY: Expressed at highest levels in the ovary, skeletal muscle, stomach, brain, uterus, heart, kidney and placenta.; myocardium;smooth muscle;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;oesophagus;larynx;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve;cerebellum; . 0.14720 . -1.591018721 3.084453881 835.17771 5.65739 SULT1A1 2.23675804808239e-09 0.0733194546192748 0.926680543143967 sulfotransferase family 1A member 1 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N- hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk. {ECO:0000269|PubMed:12471039, ECO:0000269|PubMed:16221673}.; . TISSUE SPECIFICITY: Liver, lung, adrenal, brain, platelets and skin.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;larynx;thyroid;bone;iris;testis;germinal center;spinal ganglion;bladder;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;tongue;islets of Langerhans;pineal body;blood;pancreas;lung;trabecular meshwork;placenta;visual apparatus;hypopharynx;liver;cervix;head and neck;spleen;kidney;mammary gland;stomach;cerebellum; . 0.09968 0.40709 -0.156065314 42.16206653 63.72574 1.63669 SULT1A2 1.83502409355329e-08 0.128298177399146 0.871701804250613 sulfotransferase family 1A member 2 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Is also responsible for the sulfonation and activation of minoxidil. Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.; . . unclassifiable (Anatomical System);smooth muscle;lymph node;heart;small intestine;pineal body;colon;parathyroid;blood;uterus;lung;larynx;trabecular meshwork;thyroid;liver;head and neck;spleen;brain;stomach; superior cervical ganglion;liver;skeletal muscle; 0.11690 0.26189 0.819433854 87.98655343 2869.06243 10.14174 SULT1A3 0.372332179105009 0.479659578945653 0.148008241949338 sulfotransferase family 1A member 3 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic monoamines (neurotransmitters such as dopamine, norepinephrine and serotonin) and phenolic and catechol drugs.; . TISSUE SPECIFICITY: Liver, colon, kidney, lung, brain, spleen, small intestine, placenta and leukocyte.; . . 0.81570 0.15722 . . 0.46902 0.00778 SULT1A4 0.392852564478597 0.474010280035944 0.133137155485459 sulfotransferase family 1A member 4 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic monoamines (neurotransmitters such as dopamine, norepinephrine and serotonin) and phenolic and catechol drugs.; . TISSUE SPECIFICITY: Liver, colon, kidney, lung, brain, spleen, small intestine, placenta and leukocyte.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pineal body;blood;lens;pancreas;lung;trabecular meshwork;placenta;macula lutea;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; . 0.90833 0.17194 . . . . SULT1B1 6.23606774532932e-05 0.712235445083333 0.287702194239214 sulfotransferase family 1B member 1 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Sulfates dopamine, small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine, reverse triiodothyronine and thyroxine. {ECO:0000269|PubMed:9443824, ECO:0000269|PubMed:9463486}.; . TISSUE SPECIFICITY: Highly expressed in the liver, peripheral blood leukocytes, colon (mucosal lining), small intestine (jejunum) and spleen. A lesser expression was observed in the lung, placenta and thymus. {ECO:0000269|PubMed:9463486}.; unclassifiable (Anatomical System);kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05993 0.14761 0.106667882 61.73036093 247.19737 3.39113 SULT1C2 1.42167398484664e-05 0.633846403131815 0.366139380128336 sulfotransferase family 1C member 2 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. May be involved in the activation of carcinogenic hyroxylamines. Shows activity towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF).; . TISSUE SPECIFICITY: Found in adult stomach, kidney and thyroid gland, and in fetal kidney and liver.; unclassifiable (Anatomical System);cartilage;colon;parathyroid;uterus;pancreas;lung;nasopharynx;thyroid;liver;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;thyroid;globus pallidus;kidney;pons;atrioventricular node;skeletal muscle; . 0.10093 1.594792159 95.83628214 629.65613 5.05710 SULT1C2P1 . . . sulfotransferase family 1C member 2 pseudogene 1 . . . . . . . . . . . SULT1C2P2 . . . sulfotransferase family, cytosolic, 1C, member 2 pseudogene 2 . . . . . . . . . . . SULT1C3 2.998783895639e-11 0.0114222834284907 0.988577716541521 sulfotransferase family 1C member 3 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor and has low sulphotransferase activity towards various substrates with alcohol groups (in vitro). May catalyze the sulfate conjugation of xenobiotic compounds and endogenous substrates. {ECO:0000269|PubMed:17425406, ECO:0000269|PubMed:17936463}.; . TISSUE SPECIFICITY: Isoform 1 is not detectable in any of the tissues tested. Isoform 2 is expresssed in the small intestine. {ECO:0000269|PubMed:14676822, ECO:0000269|PubMed:24335392}.; . . 0.02832 0.08293 1.596607091 95.87166785 4483.95839 13.43891 SULT1C4 0.000445387423842765 0.864196372235545 0.135358240340613 sulfotransferase family 1C member 4 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. May be involved in the activation of carcinogenic hyroxylamines. Shows activity towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF). {ECO:0000269|PubMed:17425406}.; . TISSUE SPECIFICITY: Expressed at high levels in fetal lung and kidney and at low levels in fetal heart, adult kidney, ovary and spinal chord.; unclassifiable (Anatomical System);heart;placenta;colon;kidney;brain;skeletal muscle;stomach; . . 0.10106 0.016664174 55.21939137 1571.29653 7.33697 SULT1D1P . . . sulfotransferase family 1D member 1, pseudogene . . . . . . . . . . . SULT1E1 7.40467355453317e-05 0.747236648539806 0.252689304724649 sulfotransferase family 1E member 1 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of estradiol and estrone. May play a role in the regulation of estrogen receptor activity by metabolizing free estradiol. Maximally sulfates beta-estradiol and estrone at concentrations of 20 nM. Also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, equalenin, diethylstilbesterol and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated. {ECO:0000269|PubMed:11884392}.; . TISSUE SPECIFICITY: Liver, intestine and at lower level in the kidney.; unclassifiable (Anatomical System);heart;skeletal muscle;skin;uterus;whole body;lung;nasopharynx;thyroid;liver;testis;head and neck;spleen;brain; fetal liver;superior cervical ganglion;heart;skeletal muscle; 0.11842 0.21708 -0.139478553 43.29440906 14.8109 0.53329 SULT2A1 1.38583676529622e-07 0.210509670250465 0.789490191165859 sulfotransferase family 2A member 1 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands.; . TISSUE SPECIFICITY: Liver, adrenal and at lower level in the kidney. Is present in human fetus in higher level in the adrenal than the liver and the kidney.; lung;whole body;adrenal gland;placenta;adrenal cortex;liver;testis;parathyroid;skeletal muscle; superior cervical ganglion;adrenal gland;liver;trigeminal ganglion; 0.06996 0.35923 0.260991686 70.25831564 346.26413 3.94633 SULT2B1 0.827919001656143 0.171306785050359 0.00077421329349791 sulfotransferase family 2B member 1 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Sulfates hydroxysteroids like DHEA. Isoform 1 preferentially sulfonates cholesterol, and isoform 2 avidly sulfonates pregnenolone but not cholesterol. {ECO:0000269|PubMed:12145317, ECO:0000269|PubMed:9799594}.; . TISSUE SPECIFICITY: Expressed highly in placenta, prostate and trachea and lower expression in the small intestine and lung. {ECO:0000269|PubMed:9799594}.; unclassifiable (Anatomical System);heart;cartilage;colon;fovea centralis;choroid;lens;skin;retina;breast;pancreas;prostate;optic nerve;lung;placenta;macula lutea;kidney;stomach; superior cervical ganglion;tongue;globus pallidus;ciliary ganglion;atrioventricular node;caudate nucleus;pons;trigeminal ganglion;skeletal muscle;skin; 0.24086 0.57621 0.619191319 83.36282142 197.22278 3.03613 SULT4A1 0.968128304940117 0.0318210572561192 5.06378037635815e-05 sulfotransferase family 4A member 1 FUNCTION: Atypical sulfotransferase family member with very low affinity for 3'-phospho-5'-adenylyl sulfate (PAPS) and very low catalytic activity towards L-triiodothyronine, thyroxine, estrone, p-nitrophenol, 2-naphthylamine, and 2-beta-naphthol. May have a role in the metabolism of drugs and neurotransmitters in the CNS. {ECO:0000269|PubMed:17425406}.; . TISSUE SPECIFICITY: Highly expressed in the cerebral cortex and frontal lobe, slightly less in the cerebellum, occipital and temporal lobes, relatively low in the medulla and putamen, and lowest in the spinal cord. No expression detected in the pancreas (PubMed:10698717). Highly expressed in fetal brain and occipital lobe, slightly less in the whole brain, frontal lobe, hippocampus, and lung, very low expression in cerebellum, medulla oblongata, temporal lobe, testis, kidney and appendix (PubMed:12039030). {ECO:0000269|PubMed:10698717, ECO:0000269|PubMed:12039030}.; unclassifiable (Anatomical System);hypothalamus;sympathetic chain;spinal cord;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;frontal lobe;macula lutea;hippocampus;testis;brain;cerebellum; whole brain;amygdala;dorsal root ganglion;superior cervical ganglion;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.18903 0.27121 -0.317668748 31.45789101 11.60173 0.42028 SULT6B1 3.4792081587007e-11 0.0124625324463118 0.987537467518896 sulfotransferase family 6B member 1 FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of thyroxine. Involved in the metabolism of thyroxine (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in kidney and testis. {ECO:0000269|PubMed:19505954}.; . . 0.08766 0.08838 2.017427259 97.68223638 2968.40598 10.33166 SUMF1 0.0425777224004311 0.951431878827504 0.00599039877206531 sulfatase modifying factor 1 FUNCTION: Using molecular oxygen and an unidentified reducing agent, oxidizes a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue, which is also called C(alpha)-formylglycine. Known substrates include GALNS, ARSA, STS and ARSE. {ECO:0000269|PubMed:12757706, ECO:0000269|PubMed:15657036}.; DISEASE: Multiple sulfatase deficiency (MSD) [MIM:272200]: A clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post- translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. {ECO:0000269|PubMed:12757705, ECO:0000269|PubMed:12757706, ECO:0000269|PubMed:15146462}. Note=The disease is caused by mutations affecting the gene represented in this entry. SUMF1 mutations result in defective post-translational modification of sulfatases. {ECO:0000269|PubMed:12757706}.; TISSUE SPECIFICITY: Ubiquitous. Highly expressed in kidney, pancreas and liver. Detected at lower levels in leukocytes, lung, placenta, small intestine, skeletal muscle and heart. {ECO:0000269|PubMed:15962010}.; unclassifiable (Anatomical System);cartilage;heart;ovary;hypothalamus;colon;parathyroid;skin;skeletal muscle;bone marrow;breast;uterus;prostate;whole body;lung;endometrium;bone;placenta;hippocampus;iris;testis;cervix;spleen;kidney;brain;aorta;thymus; superior cervical ganglion;atrioventricular node;kidney; 0.02875 0.06601 -0.179930907 40.35739561 1048.22721 6.21636 SUMF2 5.52632393168249e-05 0.883050597173816 0.116894139586867 sulfatase modifying factor 2 FUNCTION: Lacks formyl-glycine generating activity and is unable to convert newly synthesized inactive sulfatases to their active form. Inhibits the activation of sulfatases by SUMF1. {ECO:0000269|PubMed:12757706, ECO:0000269|PubMed:15708861, ECO:0000269|PubMed:15962010}.; . TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Highest levels in kidney, liver and placenta. {ECO:0000269|PubMed:15708861, ECO:0000269|PubMed:15962010}.; lymphoreticular;ovary;salivary gland;intestine;colon;choroid;skin;retina;uterus;prostate;cerebral cortex;endometrium;thyroid;bone;iris;testis;amniotic fluid;germinal center;spinal ganglion;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;cervix;head and neck;kidney;mammary gland;stomach;thymus; . 0.07185 0.68732 0.420771676 77.15852795 226.86098 3.25511 SUMO1 0.80037401914066 0.194175602280808 0.00545037857853205 small ubiquitin-like modifier 1 FUNCTION: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1 (PubMed:19223394). Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (PubMed:24651376). {ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:19223394, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24651376, ECO:0000269|PubMed:9019411, ECO:0000269|PubMed:9162015}.; DISEASE: Non-syndromic orofacial cleft 10 (OFC10) [MIM:613705]: A birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum. {ECO:0000269|PubMed:16990542}. Note=The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving SUMO1 is the cause of OFC10. Translocation t(2;8)(q33.1;q24.3). The breakpoint occurred in the SUMO1 gene and resulted in haploinsufficiency confirmed by protein assays.; . . . . 0.69726 0.101211609 60.95777306 0.35003 0.00689 SUMO1P1 . . . SUMO1 pseudogene 1 . . . . . . . . . . . SUMO1P2 . . . SUMO1 pseudogene 2 . . . . . . . . . . . SUMO1P3 . . . SUMO1 pseudogene 3 . . . . . . 0.69726 . . . . SUMO1P4 . . . SUMO1 pseudogene 4 . . . . . . . . . . . SUMO1P5 . . . SUMO1 pseudogene 5 . . . . . . . . . . . SUMO2 0.850515883834874 0.146950486804454 0.00253362936067144 small ubiquitin-like modifier 2 FUNCTION: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (PubMed:18408734, PubMed:18538659, PubMed:21965678, PubMed:9556629). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744). {ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24105744, ECO:0000269|PubMed:9556629}.; . TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:9556629}.; . . . . 0.167351552 65.04482189 . . SUMO2P1 . . . SUMO2 pseudogene 1 . . . . . . . . . . . SUMO2P2 . . . SUMO2 pseudogene 2 . . . . . . . . . . . SUMO2P3 . . . SUMO2 pseudogene 3 . . . . . . . . . . . SUMO2P4 . . . SUMO2 pseudogene 4 . . . . . . . . . . . SUMO2P5 . . . SUMO2 pseudogene 5 . . . . . . . . . . . SUMO2P6 . . . SUMO2 pseudogene 6 . . . . . . . . . . . SUMO2P7 . . . SUMO2 pseudogene 7 . . . . . . . . . . . SUMO2P8 . . . SUMO2 pseudogene 8 . . . . . . . . . . . SUMO2P10 . . . SUMO2 pseudogene 10 . . . . . . . . . . . SUMO2P11 . . . SUMO2 pseudogene 11 . . . . . . . . . . . SUMO2P12 . . . SUMO2 pseudogene 12 . . . . . . . . . . . SUMO2P13 . . . SUMO2 pseudogene 13 . . . . . . . . . . . SUMO2P14 . . . SUMO2 pseudogene 14 . . . . . . . . . . . SUMO2P15 . . . SUMO2 pseudogene 15 . . . . . . . . . . . SUMO2P16 . . . SUMO2 pseudogene 16 . . . . . . . . . . . SUMO2P17 . . . SUMO2 pseudogene 17 . . . . . . . . . . . SUMO2P18 . . . SUMO2 pseudogene 18 . . . . . . . . . . . SUMO2P19 . . . SUMO2 pseudogene 19 . . . . . . . . . . . SUMO2P20 . . . SUMO2 pseudogene 20 . . . . . . . . . . . SUMO3 0.31249615499247 0.61651954282644 0.0709843021810901 small ubiquitin-like modifier 3 FUNCTION: Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4 (PubMed:11451954, PubMed:18538659, PubMed:21965678). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744). {ECO:0000269|PubMed:11451954, ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:21965678}.; . TISSUE SPECIFICITY: Expressed predominantly in liver. {ECO:0000269|PubMed:15487983}.; myocardium;lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;oesophagus;bone;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;kidney;stomach;thymus; whole brain;amygdala;hypothalamus;testis;pons;cerebellum; . . 0.235309407 68.71903751 4.18821 0.15299 SUMO4 0.217538234779752 0.647770589298742 0.134691175921507 small ubiquitin-like modifier 4 FUNCTION: Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may modulate protein subcellular localization, stability or activity. Upon oxidative stress, conjugates to various anti-oxidant enzymes, chaperones, and stress defense proteins. May also conjugate to NFKBIA, TFAP2A and FOS, negatively regulating their transcriptional activity, and to NR3C1, positively regulating its transcriptional activity. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I. {ECO:0000269|PubMed:15123604, ECO:0000269|PubMed:15247916, ECO:0000269|PubMed:16236267}.; . TISSUE SPECIFICITY: Expressed mainly in adult and embryonic kidney. Expressed at various levels in immune tissues, with the highest expression in the lymph node and spleen. {ECO:0000269|PubMed:15123604, ECO:0000269|PubMed:15247916}.; ovary;umbilical cord;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;spinal cord;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;synovium;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta; superior cervical ganglion;adrenal gland;testis;kidney;trigeminal ganglion;cerebellum; 0.21566 0.15056 0.880130671 88.9596603 35.22635 1.06661 SUN1 0.835840781167159 0.164158985330061 2.33502779932124e-07 Sad1 and UNC84 domain containing 1 FUNCTION: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non- coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. Helps to define the distribution of nuclear pore complexes (NPCs) (By similarity). Required for efficient localization of SYNE4 in the nuclear envelope (By similarity). {ECO:0000250, ECO:0000269|PubMed:18039933, ECO:0000269|PubMed:18396275}.; . . lymphoreticular;smooth muscle;ovary;sympathetic chain;adrenal medulla;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;amygdala;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta;cerebellum; amygdala;superior cervical ganglion;testis - interstitial;medulla oblongata;occipital lobe;pons;uterus;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;cerebellum; 0.12582 0.08767 0.834017099 88.13989148 1176.18927 6.51539 SUN2 2.40833189817119e-07 0.994679312109684 0.00532044705712572 Sad1 and UNC84 domain containing 2 FUNCTION: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for RAB5-GDP and participate in the activation of RAB5. {ECO:0000269|PubMed:18396275}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart, lung and muscle. Weakly expressed in fetal heart. Slightly overexpressed in some heart tissues form patients with congenital heart defects. {ECO:0000269|PubMed:10818110, ECO:0000269|PubMed:12393179}.; ovary;adrenal medulla;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;iris;germinal center;bladder;brain;heart;cartilage;blood;skeletal muscle;breast;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;amnion;head and neck;kidney;stomach;thymus;cerebellum; thalamus; 0.20389 0.11830 0.051446096 57.53715499 1473.25813 7.14983 SUN3 3.79821816082152e-05 0.828499164659523 0.171462853158869 Sad1 and UNC84 domain containing 3 . . . unclassifiable (Anatomical System);medulla oblongata;lung;hippocampus;testis; . 0.14386 . 0.817616644 87.95116773 103.59404 2.19884 SUN5 6.52856833944276e-11 0.123076569942047 0.876923429992668 Sad1 and UNC84 domain containing 5 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12621555}.; unclassifiable (Anatomical System);lung;testis; testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.09219 0.09059 -0.268115223 34.70747818 1059.74186 6.24619 SUOX 0.00208476865750542 0.914258529409167 0.0836567019333274 sulfite oxidase . DISEASE: Isolated sulfite oxidase deficiency (ISOD) [MIM:272300]: Characterized by neurological abnormalities including multicystic leukoencephalopathy with brain atrophy. Patients often suffer from seizures. Often leads to death at an early age. {ECO:0000269|PubMed:10519592, ECO:0000269|PubMed:12112661, ECO:0000269|PubMed:12368985, ECO:0000269|PubMed:9428520, ECO:0000269|PubMed:9600976}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;mammary gland;stomach; kidney; 0.03909 0.23309 0.15257911 64.60839821 84.04551 1.95214 SUPT3H 0.000109913332445794 0.948102318772796 0.0517877678947579 SPT3 homolog, SAGA and STAGA complex component FUNCTION: Probable transcriptional activator. {ECO:0000269|PubMed:9787080}.; . TISSUE SPECIFICITY: Expressed in all tissues tested including pancreas, kidney, skeletal muscle, liver, lung, placenta, brain and heart.; unclassifiable (Anatomical System);bile duct;lung;cartilage;adrenal gland;bone;liver;testis;spleen; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.46719 0.12709 1.216305531 93.13517339 118.4054 2.36673 SUPT4H1 0.338447260034668 0.647138788468478 0.014413951496854 SPT4 homolog, DSIF elongation factor subunit FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV- 1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences. {ECO:0000269|PubMed:10075709, ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11112772, ECO:0000269|PubMed:11553615, ECO:0000269|PubMed:12653964, ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:15136722, ECO:0000269|PubMed:15380072, ECO:0000269|PubMed:16214896, ECO:0000269|PubMed:9450929, ECO:0000269|PubMed:9857195}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8649394, ECO:0000269|PubMed:8786137}.; lymphoreticular;ovary;umbilical cord;substantia nigra;skin;retina;bone marrow;prostate;frontal lobe;endometrium;iris;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;occipital lobe;cerebellum peduncles;globus pallidus;trigeminal ganglion;whole blood;parietal lobe;cerebellum; 0.37651 0.11262 0.21326276 67.71644256 4.71128 0.17028 SUPT4H1P1 . . . SPT4 homolog, DSIF elongation factor subunit pseudogene . . . . . . . . . . . SUPT4H1P2 . . . SPT4 homolog, DSIF elongation factor subunit pseudogene 2 . . . . . . . . . . . SUPT5H 0.999999734600741 2.65399259135706e-07 4.16144754360509e-18 SPT5 homolog, DSIF elongation factor subunit FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV- 1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences. {ECO:0000269|PubMed:10075709, ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:10421630, ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:10757782, ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11112772, ECO:0000269|PubMed:11553615, ECO:0000269|PubMed:11809800, ECO:0000269|PubMed:12653964, ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:14701750, ECO:0000269|PubMed:15136722, ECO:0000269|PubMed:15380072, ECO:0000269|PubMed:16214896, ECO:0000269|PubMed:9450929, ECO:0000269|PubMed:9514752, ECO:0000269|PubMed:9857195}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10075709, ECO:0000269|PubMed:8975720}.; ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;larynx;synovium;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;amnion;head and neck;kidney;stomach;thymus;cerebellum; testis - interstitial;superior cervical ganglion;cerebellum peduncles;temporal lobe;pons;atrioventricular node;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.64202 0.11134 -1.42004951 4.104741684 80.77096 1.89887 SUPT6H 0.999999999889474 1.10526134469157e-10 9.93725338451173e-28 SPT6 homolog, histone chaperone FUNCTION: Transcription elongation factor which binds histone H3 and plays a key role in the regulation of transcription elongation and mRNA processing. Enhances the transcription elongation by RNA polymerase II (RNAPII) and is also required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. Besides chaperoning histones in transcription, acts to transport and splice mRNA by forming a complex with IWS1 and the C-terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone modifying enzymes (such as SETD2), to ensure proper mRNA splicing, efficient mRNA export and elongation-coupled H3K36 methylation, a signature chromatin mark of active transcription. SUPT6H via its association with SETD1A, regulates both class-switch recombination and somatic hypermutation through formation of H3K4me3 epigenetic marks on activation-induced cytidine deaminase (AICDA) target loci. Promotes the activation of the myogenic gene program by entailing erasure of the repressive H3K27me3 epigenetic mark through stabilization of the chromatin interaction of the H3K27 demethylase KDM6A. {ECO:0000269|PubMed:15060154, ECO:0000269|PubMed:17234882, ECO:0000269|PubMed:22316138, ECO:0000269|PubMed:23503590, ECO:0000269|PubMed:9514752}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;placenta;hippocampus;duodenum;amnion;head and neck;kidney;stomach; thalamus;subthalamic nucleus;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;caudate nucleus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.83232 0.15691 -2.410693389 1.07336636 91.4854 2.05677 SUPT7L 0.833193338587633 0.166095091927297 0.000711569485069957 SPT7-like STAGA complex gamma subunit . . TISSUE SPECIFICITY: Expressed at high levels in adenocarcinomas and gliomas and low in esophageal cancers and malignant hematological disease. Also expressed at high level in the thymus, low in peripheral blood mononuclear cells, and lowest in the stomach, small intestine, and skeletal muscle.; ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;urinary;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;atrium;oesophagus;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;nasopharynx;placenta;head and neck;kidney;stomach;thymus; dorsal root ganglion;occipital lobe;superior cervical ganglion;prefrontal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.12986 0.28788 -0.137658575 43.57159707 44.29914 1.27031 SUPT16H 0.999999605669678 3.94330322378904e-07 2.20903242108498e-18 SPT16 homolog, facilitates chromatin remodeling subunit FUNCTION: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). {ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:12934006, ECO:0000269|PubMed:16713563, ECO:0000269|PubMed:9489704, ECO:0000269|PubMed:9836642}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10792464}.; myocardium;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe; . 0.14229 -0.622676946 17.30950696 137.66884 2.55495 SUPT16HP1 . . . SPT16 homolog, facilitates chromatin remodeling subunit pseudogene 1 . . . . . . . . . . . SUPT20H 0.00138198819635341 0.998605165636791 1.28461668558264e-05 SPT20 homolog, SAGA complex component FUNCTION: Required for MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) activation during gastrulation. Required for down- regulation of E-cadherin during gastrulation by regulating E- cadherin protein level downstream from NCK-interacting kinase (NIK) and independently of the regulation of transcription by FGF signaling and Snail (By similarity). Required for starvation- induced ATG9A trafficking during autophagy. {ECO:0000250, ECO:0000269|PubMed:19893488}.; . TISSUE SPECIFICITY: Highly expressed in testis, moderately in brain and pituitary gland. Expressed in several fetal tissues, including lung, brain, thymus and kidney. Expression is down- regulated in malignant prostate tissues. {ECO:0000269|PubMed:11340631}.; . . 0.51270 0.12263 -0.44448505 24.46331682 203.81306 3.08104 SUPT20HL1 . . . SPT20 homolog, SAGA complex component-like 1 . . . . . . . . . . . SUPT20HL2 . . . SPT20 homolog, SAGA complex component-like 2 . . . . . . . . . . . SUPV3L1 0.0338209971609747 0.966107306097008 7.16967420168658e-05 Suv3 like RNA helicase FUNCTION: Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. ATPase and ATP- dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA surveillance system in mitochondria; regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. Also implicated in recombination and chromatin maintenance pathways. May protect cells from apoptosis. Associates with mitochondrial DNA. {ECO:0000269|PubMed:12466530, ECO:0000269|PubMed:15096047, ECO:0000269|PubMed:17352692, ECO:0000269|PubMed:17961633, ECO:0000269|PubMed:18678873, ECO:0000269|PubMed:19509288, ECO:0000269|PubMed:19864255}.; . TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:10453991}.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cerebellum cortex;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; testis - interstitial;prefrontal cortex;testis;parietal lobe; 0.26609 0.12216 -0.975433863 8.852323661 386.77694 4.14184 SURF1 1.02063910629184e-13 0.00287792295285265 0.997122077047045 surfeit 1 FUNCTION: Probably involved in the biogenesis of the COX complex.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. {ECO:0000269|PubMed:10647889, ECO:0000269|PubMed:10746561, ECO:0000269|PubMed:14564068, ECO:0000269|PubMed:21937992, ECO:0000269|PubMed:22410471, ECO:0000269|PubMed:22488715, ECO:0000269|PubMed:9843204}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.11439 0.21573 -0.159704656 41.90846898 322.9465 3.81822 SURF2 3.07087198881956e-07 0.177571115665227 0.822428577247574 surfeit 2 . . . . . 0.10928 0.10388 0.617373774 83.25076669 129.54675 2.48119 SURF4 0.686424182931678 0.309302305063219 0.00427351200510261 surfeit 4 FUNCTION: May play a role in the maintenance of the architecture of the endoplasmic reticulum-Golgi intermediate compartment and of the Golgi. {ECO:0000269|PubMed:18287528}.; . . . . 0.36749 0.12191 -0.229483771 36.86010852 13.30815 0.48311 SURF6 8.12446562293265e-05 0.765409974823326 0.234508780520445 surfeit 6 FUNCTION: Binds to both DNA and RNA in vitro, with a stronger binding capacity for RNA. May represent a nucleolar constitutive protein involved in ribosomal biosynthesis or assembly (By similarity). {ECO:0000250}.; . . . . 0.14947 0.10990 1.664578456 96.27860344 3094.82513 10.57567 SURF6P1 . . . surfeit 6 pseudogene 1 . . . . . . . . . . . SUSD1 8.56399035687766e-09 0.898762060414844 0.101237931021165 sushi domain containing 1 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;blood;skin;breast;pancreas;lung;endometrium;placenta;liver;testis;spleen;kidney;brain;aorta; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.08293 0.08284 -0.418800956 25.79028073 137.08657 2.54656 SUSD2 1.32605754184724e-10 0.770818641067621 0.229181358799773 sushi domain containing 2 FUNCTION: May be a cytokine receptor for C10ORF99. May be a tumor suppressor; together with C10ORF99 has a growth inhibitory effect on colon cancer cells which includes G1 cell cycle arrest (PubMed:25351403). May play a role in breast tumorigenesis (PubMed:23131994). {ECO:0000269|PubMed:23131994, ECO:0000269|PubMed:25351403}.; . TISSUE SPECIFICITY: Highly expressed in breast cancer, but shows a restricted expression pattern in normal tissues such as adipose, adrenal gland, kidney, lung, mammary gland, placenta, thyroid, trachea, and uterus (PubMed:23131994). Also expressed in colon; down-regulated in colon cancer tisues (PubMed:25351403). {ECO:0000269|PubMed:23131994, ECO:0000269|PubMed:25351403}.; unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;lens;skeletal muscle;pancreas;prostate;lung;frontal lobe;cerebral cortex;endometrium;epididymis;placenta;visual apparatus;testis;kidney;brain; . 0.15016 0.08826 -1.072996117 7.348431234 1393.20563 6.98371 SUSD2P1 . . . sushi domain containing 2 pseudogene 1 . . . . . . . . . . . SUSD2P2 . . . sushi domain containing 2 pseudogene 2 . . . . . . . . . . . SUSD3 0.00319514254571766 0.823302148482088 0.173502708972195 sushi domain containing 3 FUNCTION: May play a role in breast tumorigenesis by promoting estrogen-dependent cell proliferation, cell-cell interactions and migration. {ECO:0000269|PubMed:24413080}.; . TISSUE SPECIFICITY: Highly expressed in estrogen receptor-positive breast tumors. {ECO:0000269|PubMed:24413080}.; . . 0.06735 . 0.461228372 78.46190139 1333.3344 6.85696 SUSD4 0.00457175417443286 0.96456044982532 0.0308677960002468 sushi domain containing 4 FUNCTION: Acts as complement inhibitor by disrupting the formation of the classical C3 convertase. Isoform 3 inhibits the classical complement pathway, while membrane-bound isoform 1 inhibits deposition of C3b via both the classical and alternative complement pathways. {ECO:0000269|PubMed:23482636}.; . TISSUE SPECIFICITY: Isoform 3 is the predominant isoform in all tissues except cortex, cerebellum, kidney, and breast. Isoform 1 is found primarily in the esophagus and the brain. {ECO:0000269|PubMed:23482636}.; unclassifiable (Anatomical System);uterus;lung;frontal lobe;ovary;heart;islets of Langerhans;hypothalamus;bone;hippocampus;testis;skin; amygdala;whole brain;medulla oblongata;thalamus;superior cervical ganglion;hypothalamus;temporal lobe;prefrontal cortex;cingulate cortex;skeletal muscle; 0.20198 . -0.576764155 18.7839113 70.09899 1.73722 SUSD5 4.30999192934607e-09 0.0564257325831761 0.943574263106832 sushi domain containing 5 . . . unclassifiable (Anatomical System);heart;cartilage;skeletal muscle;skin;bone marrow;uterus;lung;cerebral cortex;bone;testis;kidney;brain;artery;aorta; occipital lobe;temporal lobe;prefrontal cortex;ciliary ganglion; 0.22611 0.07924 1.534092314 95.56499174 196.93645 3.03524 SUSD6 . . . sushi domain containing 6 FUNCTION: May play a role in growth-suppressive activity and cell death (PubMed:24652652). May be involved in the production of chemokine molecules in umbilical vein endothelial cells (HUVECs) cultured in THP1 monocyte LPS-induced medium (PubMed:20236627). Plays a role in preventing tumor onset (By similarity). {ECO:0000250|UniProtKB:Q8BGE4, ECO:0000269|PubMed:20236627, ECO:0000269|PubMed:24652652}.; . . . . 0.11533 0.09371 -0.179930907 40.35739561 . . SUV39H1 0.936945044155794 0.0627771938791952 0.000277761965010934 suppressor of variegation 3-9 homolog 1 FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys- 9' as substrate. Also weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone- modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation. {ECO:0000269|PubMed:14765126, ECO:0000269|PubMed:16449642, ECO:0000269|PubMed:16818776, ECO:0000269|PubMed:16858404, ECO:0000269|PubMed:18004385, ECO:0000269|PubMed:18485871}.; . . colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;adrenal cortex;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;liver;cervix;kidney;mammary gland;stomach; trigeminal ganglion;skeletal muscle; 0.59739 0.22085 -0.207437529 38.2814343 6.56827 0.24270 SUV39H2 0.910307361240509 0.0896643931390929 2.82456203983634e-05 suppressor of variegation 3-9 homolog 2 FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys- 9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation. {ECO:0000269|PubMed:14765126}.; . . myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.30122 0.09165 -0.295622497 32.61972163 9.16999 0.33454 SUZ12 0.999270635842049 0.000729363165698839 9.92252529592125e-10 SUZ12 polycomb repressive complex 2 subunit FUNCTION: Polycomb group (PcG) protein. Component of the PRC2/EED- EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A. {ECO:0000269|PubMed:15225548, ECO:0000269|PubMed:15231737, ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:16618801, ECO:0000269|PubMed:17344414, ECO:0000269|PubMed:18285464}.; DISEASE: Note=A chromosomal aberration involving SUZ12 may be a cause of endometrial stromal tumors. Translocation t(7;17)(p15;q21) with JAZF1. The translocation generates the JAZF1-SUZ12 oncogene consisting of the N-terminus part of JAZF1 and the C-terminus part of SUZ12. It is frequently found in all cases of endometrial stromal tumors, except in endometrial stromal sarcomas, where it is rarer. {ECO:0000269|PubMed:11371647}.; TISSUE SPECIFICITY: Overexpressed in breast and colon cancer. {ECO:0000269|PubMed:15231737, ECO:0000269|PubMed:15684044}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;cervix;kidney;stomach;aorta; amygdala;whole brain;medulla oblongata;testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;temporal lobe;testis;pons;parietal lobe; 0.90035 . -0.159704656 41.90846898 37.06069 1.10711 SUZ12P1 . . . SUZ12 polycomb repressive complex 2 subunit pseudogene 1 . . . . . 0.89458 . . . . . SUZ12P2 . . . SUZ12 polycomb repressive complex 2 subunit pseudogene 2 . . . . . . . . . . . SV2A 0.578982694774458 0.421013382602919 3.92262262282374e-06 synaptic vesicle glycoprotein 2A FUNCTION: Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles (By similarity). {ECO:0000250}.; . . . . 0.90323 0.34509 -1.241834664 5.414012739 77.39637 1.84896 SV2B 0.534784655278294 0.465187640106401 2.77046153055874e-05 synaptic vesicle glycoprotein 2B FUNCTION: Probably plays a role in the control of regulated secretion in neural and endocrine cells. {ECO:0000250}.; . . unclassifiable (Anatomical System);amygdala;heart;ovary;parathyroid;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;prostate;optic nerve;lung;frontal lobe;placenta;bone;macula lutea;visual apparatus;pineal gland;brain; whole brain;amygdala;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.74493 0.17703 -1.173870472 5.99197924 181.17412 2.92586 SV2C 6.35694393316701e-05 0.994705085807682 0.00523134475298617 synaptic vesicle glycoprotein 2C FUNCTION: Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);optic nerve;whole body;macula lutea;fovea centralis;choroid;lens;retina; dorsal root ganglion;testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle;parietal lobe; 0.17231 0.13580 -0.24061166 36.28214201 2282.13442 8.83934 SVBP . . . small vasohibin binding protein FUNCTION: Enhances the solubility and secretion of VASH1 and prevents its ubiquitination. Also enhances secretion of VASH2. {ECO:0000269|PubMed:20736312}.; . . . . 0.11039 . 0.145304857 63.81221986 . . SVEP1 0.589007650495336 0.410992349504664 1.40850230409457e-16 sushi, von Willebrand factor type A, EGF and pentraxin domain containing 1 FUNCTION: May play a role in the cell attachment process. {ECO:0000250}.; . TISSUE SPECIFICITY: Present in mesenchymal primary cultured cell lysates (at protein level). Highly expressed in placenta. Also expressed in marrow stromal cell. Weakly or not expressed in other tissues. {ECO:0000269|PubMed:11062057, ECO:0000269|PubMed:16206243}.; ovary;colon;parathyroid;choroid;skin;uterus;whole body;frontal lobe;cerebral cortex;larynx;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;adipose tissue;placenta;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.75699 . 4.588666937 99.75819769 15016.94079 26.57856 SVIL 0.999399704010116 0.000600295989883757 2.90816438981602e-18 supervillin FUNCTION: Forms a high-affinity link between the actin cytoskeleton and the membrane. Isoform 1 (archvillin) is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation. Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function. Isoform 2 may be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O46385, ECO:0000269|PubMed:19109420}.; . TISSUE SPECIFICITY: Expressed in many tissues. Most abundant in muscle, bone marrow, thyroid gland and salivary gland. Isoform 1 (archvillin) is muscle specific. {ECO:0000269|PubMed:9867483}.; smooth muscle;ovary;adrenal medulla;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;pituitary gland;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;pancreas;lung;adrenal gland;placenta;hypopharynx;amnion;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;uterus;superior cervical ganglion;uterus corpus;tongue;thyroid;testis;atrioventricular node;skeletal muscle; 0.14588 0.12156 -1.384116825 4.340646379 3895.15739 12.31383 SVIL-AS1 . . . SVIL antisense RNA 1 . . . . . . . . . . . SVILP1 . . . supervillin pseudogene 1 . . . . . . . . . . . SVIP 0.0114316242536358 0.631880816208402 0.356687559537962 small VCP/p97-interacting protein . . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;spinal cord;pharynx;blood;lens;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; amygdala;subthalamic nucleus; . . 0.013025609 54.62962963 5.66703 0.21251 SVOP . . . SV2 related protein . . . unclassifiable (Anatomical System);optic nerve;lung;frontal lobe;macula lutea;testis;fovea centralis;choroid;lens;brain;retina; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.25938 0.12188 . . . . SVOPL 0.00113327221416435 0.953834922363162 0.0450318054226738 SVOP-like . . . unclassifiable (Anatomical System);umbilical cord;ovary;cervix;blood;skeletal muscle;retina; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.11987 0.10578 -0.062423436 48.86765747 5022.7372 14.47469 SWAP70 0.348844347370405 0.651039628929454 0.000116023700141046 SWAP switching B-cell complex 70kDa subunit FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which, independently of RAS, transduces signals from tyrosine kinase receptors to RAC. It also mediates signaling of membrane ruffling. Regulates the actin cytoskeleton as an effector or adapter protein in response to agonist stimulated phosphatidylinositol (3,4)-bisphosphate production and cell protrusion (By similarity). {ECO:0000250, ECO:0000269|PubMed:10681448, ECO:0000269|PubMed:12925760}.; . TISSUE SPECIFICITY: Expressed only in mature B-cells including those associated with mucosa-associated tissue and bronchus- associated tissue (PubMed:10681448). Widely expressed. Abundant in spleen, and fairly abundant in kidney, lung and liver. Also found in monocytes and macrophages (PubMed:12925760). {ECO:0000269|PubMed:10681448, ECO:0000269|PubMed:12925760}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;aorta;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; . . -0.514264485 21.41424864 26.61895 0.86228 SWI5 0.0263593312558164 0.91941972252074 0.0542209462234435 SWI5 homologous recombination repair protein FUNCTION: Component of the SWI5-SFR1 complex, a complex required for double-strand break repair via homologous recombination. {ECO:0000269|PubMed:21252223}.; . . medulla oblongata;ovary;salivary gland;foreskin;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;epidermis;islets of Langerhans;adrenal cortex;pharynx;blood;lens;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;kidney; . 0.16163 . 0.705562627 85.52724699 487.17835 4.54368 SWSAP1 0.000134670403718243 0.638776786526844 0.361088543069438 SWIM-type zinc finger 7 associated protein 1 FUNCTION: ATPase which is preferentially stimulated by single- stranded DNA and is involved in homologous recombination repair (HRR). Has a DNA-binding activity which is independent of its ATPase activity. {ECO:0000269|PubMed:21965664}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;hypothalamus;colon;parathyroid;lens;skin;uterus;breast;lung;cerebral cortex;adrenal gland;bone;placenta;testis;germinal center;kidney;stomach; . 0.14375 . 0.305084559 72.22811984 152.4542 2.69970 SWT1 0.117421725145305 0.882568643817038 9.63103765684142e-06 SWT1, RNA endoribonuclease homolog . . TISSUE SPECIFICITY: Expressed weakly in testis. {ECO:0000269|PubMed:11318611}.; . . 0.05221 . 0.624649618 83.53385232 5614.77979 15.50962 SYAP1 0.502110067754607 0.493659030448317 0.00423090179707642 synapse associated protein 1 . . . . . 0.07608 0.10844 -0.163345027 41.24793583 10.32849 0.37671 SYBU 0.00595342898375397 0.989497407281536 0.00454916373470986 syntabulin FUNCTION: Part of a kinesin motor-adapter complex that is critical for the anterograde axonal transport of active zone components and contributes to activity-dependent presynaptic assembly during neuronal development. {ECO:0000250, ECO:0000269|PubMed:15459722}.; . TISSUE SPECIFICITY: Isoform 3, isoform 4 and isoform 5 are expressed in HeLa cell line (at protein level). Isoform 3 is expressed in fetal and adult brain. Isoform 4 is expressed in numerous fetal tissues (brain, kidney, liver, lung, and thymus) and in adult brain, kidney, liver, lung, pancreas, colon, prostate, small intestine, testis and thymus. Isoform 5 is expressed in fetal brain, brain and small intestine. {ECO:0000269|PubMed:15656992}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;prostate;whole body;frontal lobe;endometrium;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;cerebellum cortex;islets of Langerhans;pancreas;lung;trabecular meshwork;placenta;macula lutea;liver;cervix; amygdala;dorsal root ganglion;whole brain;thalamus;superior cervical ganglion;medulla oblongata;cerebellum peduncles;temporal lobe;pons;subthalamic nucleus;fetal brain;prefrontal cortex;cingulate cortex;parietal lobe;cerebellum; . . -0.200157416 39.11299835 129.10458 2.47687 SYCE1 0.000763634678380383 0.981995413480125 0.0172409518414949 synaptonemal complex central element protein 1 FUNCTION: Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Requires SYCP1 in order to be incorporated into the central element. May have a role in the synaptonemal complex assembly, stabilization and recombination (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;endometrium;placenta;testis;thymus; testis - interstitial;testis - seminiferous tubule;testis; . 0.08486 1.374284246 94.51521585 1749.70499 7.72284 SYCE1L 0.0721375071730236 0.528175590428338 0.399686902398638 synaptonemal complex central element protein 1-like FUNCTION: May be involved in meiosis. {ECO:0000250}.; . . . . . . 0.72397987 85.91648974 2721.83737 9.83187 SYCE2 0.419255589823281 0.572868345490847 0.00787606468587188 synaptonemal complex central element protein 2 FUNCTION: Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Requires SYCP1 in order to be incorporated into the central element. May have a role in the synaptonemal complex assembly, stabilization and recombination (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;lung;placenta;testis;mammary gland; . 0.08208 0.08337 0.481458261 79.03986789 13.21995 0.48088 SYCE3 . . . synaptonemal complex central element protein 3 FUNCTION: Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Required for chromosome loading of the central element-specific SCS proteins, and for initiating synapsis between homologous chromosomes. Chromosome loading appears to require SYCP1. Required for fertility (By similarity). {ECO:0000250}.; . . . . . . 0.768075923 86.8895966 107.91325 2.25633 SYCN 0.0057265264493716 0.486142376443289 0.508131097107339 syncollin FUNCTION: Functions in exocytosis in pancreatic acinar cells regulating the fusion of zymogen granules with each other. May have a pore-forming activity on membranes and regulate exocytosis in other exocrine tissues (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);pancreas;islets of Langerhans;testis;spleen; pancreas;superior cervical ganglion;subthalamic nucleus;beta cell islets;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.21546 0.12856 -0.031067188 51.03798066 14.46224 0.52050 SYCP1 0.949997702198387 0.0500022956289326 2.17268046672692e-09 synaptonemal complex protein 1 FUNCTION: Major component of the transverse filaments of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase.; . TISSUE SPECIFICITY: Testis.; . . 0.08531 . 0.246221394 69.56829441 212.38101 3.14424 SYCP2 0.999993566714356 6.43328564448799e-06 3.32805586480357e-18 synaptonemal complex protein 2 FUNCTION: Major component of the axial/lateral elements of synaptonemal complexes (SCS) during meiotic prophase. May be involved in the organization of chromatin by temporarily binding to DNA scaffold attachment regions. Requires SYCP3, but not SYCP1, in order to be incorporated into the axial/lateral elements (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;blood;skeletal muscle;retina;bone marrow;uterus;lung;placenta;bone;visual apparatus;liver;testis;mammary gland;stomach;cerebellum; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis; 0.12934 0.40063 0.922206779 89.58480774 471.1492 4.49215 SYCP2L 4.34413935048992e-11 0.982957961238433 0.0170420387181259 synaptonemal complex protein 2 like . . TISSUE SPECIFICITY: Expressed in the ovary (at protein level). {ECO:0000269|PubMed:17374641}.; lung;ovary;lacrimal gland;placenta;liver;testis;parathyroid;spleen;stomach; . 0.11013 . 1.35769336 94.43854683 1230.13278 6.62936 SYCP3 5.52621227683122e-05 0.686770868995947 0.313173868881285 synaptonemal complex protein 3 FUNCTION: Component of the transverse filaments of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Has an essential meiotic function in spermatogenesis. May be important for testis development. Required for efficient phosphorylation of HORMAD1 and HORMAD2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:14643120}.; DISEASE: Spermatogenic failure 4 (SPGF4) [MIM:270960]: An infertility disorder characterized by azoospermia, a condition of having no sperm present in the ejaculate. Testicular histology shows arrest of spermatogenesis at the pachytene stage of primary spermatocytes. {ECO:0000269|PubMed:14643120}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:12213195, ECO:0000269|PubMed:14643120}.; ovary;umbilical cord;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;testis;bladder;brain;unclassifiable (Anatomical System);heart;pharynx;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach; subthalamic nucleus;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12968 0.14188 -0.207437529 38.2814343 5.50712 0.20529 SYDE1 0.946542806698739 0.0534496190479112 7.57425335013364e-06 synapse defective 1, Rho GTPase, homolog 1 (C. elegans) FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;breast;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland; superior cervical ganglion;uterus corpus;placenta;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18560 . . . 418.30936 4.27704 SYDE2 3.19709426065925e-12 0.454616122979257 0.545383877017546 synapse defective 1, Rho GTPase, homolog 2 (C. elegans) FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;placenta;visual apparatus;liver;colon;parathyroid;kidney; . 0.38055 0.12508 0.7164803 85.82802548 2003.55658 8.24309 SYF2 0.0379270965280319 0.929085544076457 0.0329873593955115 SYF2 pre-mRNA splicing factor FUNCTION: May be involved in pre-mRNA splicing. {ECO:0000250}.; . TISSUE SPECIFICITY: Abundantly expressed in the heart, skeletal muscle and kidney. Expressed at lower level other tissues. {ECO:0000269|PubMed:11118353}.; ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta; amygdala;uterus;thyroid;prefrontal cortex;white blood cells;whole blood; 0.23882 0.07018 0.415317661 76.81056853 235.88444 3.31854 SYF2P1 . . . SYF2 pre-mRNA splicing factor pseudogene 1 . . . . . . . . . . . SYF2P2 . . . SYF2 pre-mRNA splicing factor pseudogene 2 . . . . . . . . . . . SYK 0.998540058933014 0.00145993568165365 5.38533215043462e-09 spleen tyrosine kinase FUNCTION: Non-receptor tyrosine kinase which mediates signal transduction downstream of a variety of transmembrane receptors including classical immunoreceptors like the B-cell receptor (BCR). Regulates several biological processes including innate and adaptive immunity, cell adhesion, osteoclast maturation, platelet activation and vascular development. Assembles into signaling complexes with activated receptors at the plasma membrane via interaction between its SH2 domains and the receptor tyrosine- phosphorylated ITAM domains. The association with the receptor can also be indirect and mediated by adapter proteins containing ITAM or partial hemITAM domains. The phosphorylation of the ITAM domains is generally mediated by SRC subfamily kinases upon engagement of the receptor. More rarely signal transduction via SYK could be ITAM-independent. Direct downstream effectors phosphorylated by SYK include VAV1, PLCG1, PI-3-kinase, LCP2 and BLNK. Initially identified as essential in B-cell receptor (BCR) signaling, it is necessary for the maturation of B-cells most probably at the pro-B to pre-B transition. Activated upon BCR engagement, it phosphorylates and activates BLNK an adapter linking the activated BCR to downstream signaling adapters and effectors. It also phosphorylates and activates PLCG1 and the PKC signaling pathway. It also phosphorylates BTK and regulates its activity in B-cell antigen receptor (BCR)-coupled signaling. In addition to its function downstream of BCR plays also a role in T- cell receptor signaling. Plays also a crucial role in the innate immune response to fungal, bacterial and viral pathogens. It is for instance activated by the membrane lectin CLEC7A. Upon stimulation by fungal proteins, CLEC7A together with SYK activates immune cells inducing the production of ROS. Also activates the inflammasome and NF-kappa-B-mediated transcription of chemokines and cytokines in presence of pathogens. Regulates neutrophil degranulation and phagocytosis through activation of the MAPK signaling cascade. Also mediates the activation of dendritic cells by cell necrosis stimuli. Also involved in mast cells activation. Also functions downstream of receptors mediating cell adhesion. Relays for instance, integrin-mediated neutrophils and macrophages activation and P-selectin receptor/SELPG-mediated recruitment of leukocytes to inflammatory loci. Plays also a role in non-immune processes. It is for instance involved in vascular development where it may regulate blood and lymphatic vascular separation. It is also required for osteoclast development and function. Functions in the activation of platelets by collagen, mediating PLCG2 phosphorylation and activation. May be coupled to the collagen receptor by the ITAM domain-containing FCER1G. Also activated by the membrane lectin CLEC1B that is required for activation of platelets by PDPN/podoplanin. Involved in platelet adhesion being activated by ITGB3 engaged by fibrinogen. {ECO:0000269|PubMed:12387735, ECO:0000269|PubMed:12456653, ECO:0000269|PubMed:15388330, ECO:0000269|PubMed:19909739, ECO:0000269|PubMed:8657103, ECO:0000269|PubMed:9535867}.; . TISSUE SPECIFICITY: Widely expressed in hematopoietic cells (at protein level). Within the B-cells compartment it is for instance expressed for pro-B-cells to plasma cells. {ECO:0000269|PubMed:8163536}.; . . 0.83624 0.66496 -0.756778259 13.44656759 40.75584 1.19423 SYM2 . . . symphalangism 2 (distal) . . . . . . . . . . . SYMPK 0.997278492187137 0.00272150777163406 4.12286362619566e-11 symplekin FUNCTION: Scaffold protein that functions as a component of a multimolecular complex involved in histone mRNA 3'-end processing. Specific component of the tight junction (TJ) plaque, but might not be an exclusively junctional component. May have a house- keeping rule. Is involved in pre-mRNA polyadenylation. Enhances SSU72 phosphatase activity. {ECO:0000269|PubMed:16230528, ECO:0000269|PubMed:20861839}.; . TISSUE SPECIFICITY: In testis, expressed in polar epithelia and Sertoli cells but not in vascular endothelia. The protein is detected in stomach, duodenum, pancreas, liver, fetal brain, carcinomas, lens-forming cells, fibroblasts, lymphocytes, lymphoma cells, erythroleukemia cells but not in endothelium of vessels, epidermis, intercalated disks, Purkinje fiber cells of the heart and lymph node. {ECO:0000269|PubMed:8769423}.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;spleen;kidney;stomach;thymus;cerebellum; subthalamic nucleus;testis - seminiferous tubule;placenta; 0.11250 . -1.480759435 3.686010852 136.97651 2.54416 SYN1 0.879529753332511 0.120170954727593 0.000299291939896215 synapsin I FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level.; DISEASE: Epilepsy X-linked, with variable learning disabilities and behavior disorders (XELBD) [MIM:300491]: A neurologic disorder characterized by variable combinations of epilepsy, learning difficulties, macrocephaly, and aggressive behavior. {ECO:0000269|PubMed:14985377}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;uterus;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;cartilage;islets of Langerhans;hypothalamus;urinary;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;mammary gland;cerebellum; whole brain;amygdala;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.66764 0.62820 . . 164.73159 2.80346 SYN2 . . . synapsin II FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. May play a role in noradrenaline secretion by sympathetic neurons (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Central and peripheral nervous systems.; . . 0.19060 0.27097 . . . . SYN3 0.577812323529965 0.422090991292168 9.66851778663344e-05 synapsin III FUNCTION: May be involved in the regulation of neurotransmitter release and synaptogenesis.; . TISSUE SPECIFICITY: Neuron specific. Detected predominantly in brain.; uterus;unclassifiable (Anatomical System);lung;heart;frontal lobe;hippocampus;testis;brain;skin; superior cervical ganglion;appendix;atrioventricular node;pons;skeletal muscle; 0.10787 0.14478 -0.244249595 36.17008728 815.18881 5.61108 SYNC 0.0416853059014448 0.929482203332222 0.0288324907663333 syncoilin, intermediate filament protein FUNCTION: Atypical type III intermediate filament (IF) protein that may play a supportive role in the efficient coupling of mechanical stress between the myofibril and fiber exterior. May facilitate lateral force transmission during skeletal muscle contraction. Does not form homofilaments nor heterofilaments with other IF proteins. {ECO:0000250|UniProtKB:Q9EPM5}.; . . . . 0.81035 . 1.482722235 95.30549658 578.81727 4.87458 SYNCRIP 0.999378591415277 0.000621405265735671 3.31898744090974e-09 synaptotagmin binding, cytoplasmic RNA interacting protein FUNCTION: Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD- mediated complex that promotes MYC mRNA stability. Isoform 1, isoform 2 and isoform 3 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences. Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma- induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation; seems not to be essential for GAIT complex function. {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:11134005, ECO:0000269|PubMed:11352648, ECO:0000269|PubMed:11574476, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:23071094}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Detected in heart, brain, pancreas, placenta, spleen, lung, liver, skeletal muscle, kidney, thymus, prostate, uterus, small intestine, colon, peripheral blood and testis. {ECO:0000269|PubMed:11352648}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;thyroid;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.97710 0.24974 -0.560178693 19.30879925 10.81382 0.39248 SYNDIG1 0.433641202646478 0.534969999864404 0.031388797489118 synapse differentiation inducing 1 FUNCTION: May regulate AMPA receptor content at nascent synapses, and have a role in postsynaptic development and maturation. {ECO:0000250}.; . . . . 0.28540 0.10886 0.042348793 57.31304553 80.45047 1.89509 SYNDIG1L 0.00366418236769666 0.629708936375084 0.36662688125722 synapse differentiation inducing 1 like . . . brain; . 0.14052 . 0.571462851 81.99457419 795.52044 5.55885 SYNE1 3.75068139299055e-27 1 1.78073503849307e-40 spectrin repeat containing, nuclear envelope 1 FUNCTION: Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. Component of SUN-protein- containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. May be involved in the maintenance of nuclear organization and structural integrity. Connects nuclei to the cytoskeleton by interacting with the nuclear envelope and with F- actin in the cytoplasm. May be required for centrosome migration to the apical cell surface during early ciliogenesis. {ECO:0000269|PubMed:11792814, ECO:0000269|PubMed:18396275}.; DISEASE: Spinocerebellar ataxia, autosomal recessive, 8 (SCAR8) [MIM:610743]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR8 is an autosomal recessive form. {ECO:0000269|PubMed:17159980}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Emery-Dreifuss muscular dystrophy 4, autosomal dominant (EDMD4) [MIM:612998]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:17761684}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in HeLa, A431, A172 and HaCaT cells (at protein level). Widely expressed. Highly expressed in skeletal and smooth muscles, heart, spleen, peripheral blood leukocytes, pancreas, cerebellum, stomach, kidney and placenta. Isoform GSRP- 56 is predominantly expressed in heart and skeletal muscle (at protein level). {ECO:0000269|PubMed:11792814, ECO:0000269|PubMed:11801724, ECO:0000269|PubMed:15093733, ECO:0000269|PubMed:16875688, ECO:0000269|PubMed:22518138}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;spinal cord;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;bone;testis;artery;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;lung;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;medulla oblongata;cerebellum peduncles;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; . 0.46149 -0.160234117 41.64897381 10210.55056 22.01419 SYNE1-AS1 . . . SYNE1 antisense RNA 1 . . . . . . . . . . . SYNE2 1.8533519422462e-11 0.999999999981466 3.58916255415674e-33 spectrin repeat containing, nuclear envelope 2 FUNCTION: Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. Component of SUN-protein- containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Involved in the maintenance of nuclear organization and structural integrity. Connects nuclei to the cytoskeleton by interacting with the nuclear envelope and with F-actin in the cytoplasm. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for centrosome migration to the apical cell surface during early ciliogenesis. {ECO:0000269|PubMed:12118075, ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:20724637}.; DISEASE: Emery-Dreifuss muscular dystrophy 5, autosomal dominant (EDMD5) [MIM:612999]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:17761684}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, with higher level in kidney, adult and fetal liver, stomach and placenta. Weakly expressed in skeletal muscle and brain. Isoform 5 is highly expressed in pancreas, skeletal muscle and heart. {ECO:0000269|PubMed:15671068}.; myocardium;medulla oblongata;ovary;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;iris;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;pia mater;lung;cornea;nasopharynx;placenta;visual apparatus;hippocampus;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.21106 . 3.839142661 99.63434772 10907.00643 22.66019 SYNE3 2.9457549334185e-15 0.123695108317641 0.876304891682356 spectrin repeat containing, nuclear envelope family member 3 FUNCTION: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Involved in the maintenance of nuclear organization and structural integrity. Probable anchoring protein which tethers the nucleus to the cytoskeleton by binding PLEC which can associate with the intermediate filament system. Plays a role in the regulation of aortic epithelial cell morphology, and is required for flow- induced centrosome polarization and directional migration in aortic endothelial cells. {ECO:0000269|PubMed:16330710, ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:21937718}.; . TISSUE SPECIFICITY: Expressed in aortic endothelial cells (at protein level). {ECO:0000269|PubMed:21937718}.; . . 0.12329 0.10636 1.168395083 92.663364 3773.61165 12.02480 SYNE4 5.95759018587848e-11 0.0326951887937221 0.967304811146702 spectrin repeat containing, nuclear envelope family member 4 FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (By similarity). Behaves as a kinesin cargo, providing a functional binding site for kinesin-1 at the nuclear envelope. Hence may contribute to the establishment of secretory epithelial morphology by promoting kinesin-dependent apical migration of the centrosome and Golgi apparatus and basal localization of the nucleus (By similarity). {ECO:0000250}.; DISEASE: Deafness, autosomal recessive, 76 (DFNB76) [MIM:615540]: A form of non-syndromic sensorineural deafness, a disorder resulting from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNB76 affected individuals have onset of progressive high frequency hearing impairment between birth and 6 years of age. The hearing loss is severe at high frequencies by adulthood. {ECO:0000269|PubMed:23348741}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . . 0.354632714 74.58126917 205.51487 3.09551 SYNGAP1 0.999998449747972 1.55025202789228e-06 3.06418087674641e-16 synaptic Ras GTPase activating protein 1 FUNCTION: Major constituent of the PSD essential for postsynaptic signaling. Inhibitory regulator of the Ras-cAMP pathway. Member of the NMDAR signaling complex in excitatory synapses, it may play a role in NMDAR-dependent control of AMPAR potentiation, AMPAR membrane trafficking and synaptic plasticity. Regulates AMPAR- mediated miniature excitatory postsynaptic currents. Exhibits dual GTPase-activating specificity for Ras and Rap. May be involved in certain forms of brain injury, leading to long-term learning and memory deficits (By similarity). {ECO:0000250}.; DISEASE: Mental retardation, autosomal dominant 5 (MRD5) [MIM:612621]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD5 patients show global developmental delay with delayed motor development, hypotonia, moderate-to- severe mental retardation, and severe language impairment. Epilepsy and autism can be present in some patients. {ECO:0000269|PubMed:19196676, ECO:0000269|PubMed:21076407, ECO:0000269|PubMed:21237447, ECO:0000269|PubMed:23161826}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;adrenal medulla;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.44861 0.11578 -1.153638777 6.233781552 1373.91556 6.95167 SYNGR1 0.581490268493249 0.407871313036868 0.010638418469883 synaptogyrin 1 FUNCTION: Involved in the regulation of short-term and long-term synaptic plasticity. {ECO:0000250}.; . . medulla oblongata;ovary;umbilical cord;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;thyroid;bone;iris;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;hippocampus;macula lutea;visual apparatus;liver;amnion;spleen;kidney;stomach;cerebellum; dorsal root ganglion;amygdala;whole brain;medulla oblongata;thalamus;occipital lobe;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;atrioventricular node;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.39164 0.12825 -0.66859065 15.76433121 18.97312 0.65498 SYNGR2 0.000588831651132254 0.477486226762785 0.521924941586083 synaptogyrin 2 . . TISSUE SPECIFICITY: Ubiquitous; low expression in brain.; lymphoreticular;myocardium;medulla oblongata;ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;whole body;endometrium;oesophagus;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;muscle;blood;lens;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; prostate;lung;placenta;liver; 0.10153 0.13343 -0.359940251 28.93371078 497.66635 4.58432 SYNGR2P1 . . . synaptogyrin 2 pseudogene 1 . . . . . . . . . . . SYNGR2P2 . . . synaptogyrin 2 pseudogene 2 . . . . . . . . . . . SYNGR3 0.292054618656317 0.626575549906604 0.0813698314370794 synaptogyrin 3 FUNCTION: Involved in the positive regulation of dopamine transporter activity. Probably facilitates the physical and functional interactions of the transporter with the dopamine vesicular storage system, allowing a more efficient loading of the vesicles with extracellular dopamine after release (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain and placenta.; unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;sympathetic chain;retina;lung;frontal lobe;placenta;thyroid;hippocampus;testis;brain;tonsil; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;placenta;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.48942 . . . 88.25499 2.01243 SYNGR4 0.00121574866110408 0.632804657609478 0.365979593729417 synaptogyrin 4 . . . unclassifiable (Anatomical System);lung;testis;colon; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node; 0.14563 . 0.619191319 83.36282142 381.52099 4.11713 SYNJ1 0.2142951462835 0.785704853506554 2.09946205065732e-10 synaptojanin 1 FUNCTION: Inositol 5-phosphatase which has a role in clathrin- mediated endocytosis.; DISEASE: Parkinson disease 20, early-onset (PARK20) [MIM:615530]: An early-onset form of Parkinson disease, a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. PARK20 is characterized by young adult-onset of parkinsonism. Additional features may include seizures, cognitive decline, abnormal eye movements, and dystonia. {ECO:0000269|PubMed:23804563, ECO:0000269|PubMed:23804577}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Concentrated at clathrin-coated endocytic intermediates in nerve terminals. Isoform 1 is more enriched than isoform 2 in developing brain as well as non-neuronal cells. Isoform 2 is very abundant in nerve terminals.; ovary;sympathetic chain;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;larynx;thyroid;bone;pituitary gland;testis;middle ear;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;lung;internal ear;placenta;macula lutea;liver;alveolus;spleen;head and neck;kidney;stomach;cerebellum;thymus; dorsal root ganglion;whole brain;amygdala;occipital lobe;medulla oblongata;testis - interstitial;superior cervical ganglion;thalamus;hypothalamus;temporal lobe;pons;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.72364 0.12120 0.499660491 79.67091295 3892.53157 12.30627 SYNJ2 3.52295821798563e-05 0.999960575668203 4.19474961684895e-06 synaptojanin 2 FUNCTION: Inositol 5-phosphatase which may be involved in distinct membrane trafficking and signal transduction pathways. May mediate the inhibitory effect of Rac1 on endocytosis.; . . lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;spinal cord;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;stomach;aorta;cerebellum; dorsal root ganglion;amygdala;thalamus;medulla oblongata;superior cervical ganglion;hypothalamus;spinal cord;pons;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.23517 . -1.902173 1.952111347 376.38515 4.09028 SYNJ2-IT1 . . . SYNJ2 intronic transcript 1 . . . . . . . . . . . SYNJ2BP 0.50394450911297 0.476930614590092 0.0191248762969377 synaptojanin 2 binding protein FUNCTION: Regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. {ECO:0000250|UniProtKB:Q9D6K5}.; . . ovary;colon;parathyroid;skin;uterus;whole body;thyroid;bone;testis;germinal center;brain;artery;unclassifiable (Anatomical System);heart;nervous;islets of Langerhans;spinal cord;skeletal muscle;breast;lung;nasopharynx;placenta;liver;spleen;cervix;kidney;stomach;aorta; ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.12704 0.12625 0.591694063 82.45458835 39.71169 1.17032 SYNJ2BP-COX16 . . . SYNJ2BP-COX16 readthrough . . . . . . . . . . . SYNM 2.32891148971373e-12 0.225984569450184 0.774015430547487 synemin FUNCTION: Type-VI intermediate filament (IF) which plays an important cytoskeletal role within the muscle cell cytoskeleton. It forms heteropolymeric IFs with desmin and/or vimentin, and via its interaction with cytoskeletal proteins alpha-dystrobrevin, dystrophin, talin-1, utrophin and vinculin, is able to link these heteropolymeric IFs to adherens-type junctions, such as to the costameres, neuromuscular junctions, and myotendinous junctions within striated muscle cells. {ECO:0000269|PubMed:11353857, ECO:0000269|PubMed:16777071, ECO:0000269|PubMed:18028034}.; . TISSUE SPECIFICITY: Isoform 2 is strongly detected in adult heart, fetal skeletal muscles and fetal heart. Isoform 1 is weakly detected in fetal heart and also in fetal skeletal muscle. Isoform 1 and isoform 2 are detected in adult bladder (at protein level). The mRNA is predominantly expressed in heart and muscle with some expression in brain which may be due to tissue-specific isoforms. {ECO:0000269|PubMed:11353857, ECO:0000269|PubMed:11737198}.; unclassifiable (Anatomical System);heart;ovary;colon;blood;choroid;skin;skeletal muscle;retina;bone marrow;breast;uterus;prostate;frontal lobe;nasopharynx;thyroid;placenta;visual apparatus;liver;testis;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;prostate;spinal cord;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22107 0.35874 . . 4460.30616 13.38532 SYNPO 0.980249084871384 0.0197477665675428 3.14856107331026e-06 synaptopodin FUNCTION: Actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and renal podocyte foot processes. Seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in cerebral cortex. {ECO:0000269|PubMed:9314539}.; ovary;salivary gland;colon;parathyroid;choroid;skin;retina;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;iris;testis;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; superior cervical ganglion;heart;adrenal gland;placenta;adrenal cortex;ciliary ganglion; 0.42744 0.16538 -0.169017544 40.67586695 1300.26133 6.78435 SYNPO2 0.737066032210172 0.262933086667439 8.8112238893063e-07 synaptopodin 2 FUNCTION: Has an actin-binding and actin-bundling activity. {ECO:0000250}.; . TISSUE SPECIFICITY: Skeletal muscle specific. {ECO:0000269|PubMed:11297942}.; smooth muscle;ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;atrium;whole body;endometrium;larynx;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;spinal cord;blood;lens;skeletal muscle;breast;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;alveolus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;skeletal muscle; 0.25557 0.10741 -0.231522913 36.36470866 5388.5703 15.14623 SYNPO2L 0.0267397661792638 0.96128115000367 0.0119790838170656 synaptopodin 2 like FUNCTION: Actin-associated protein that may play a role in modulating actin-based shape. {ECO:0000250}.; . . . . 0.20396 0.09102 -0.486758915 22.69992923 4908.06476 14.28002 SYNPR 0.171706356156551 0.769977782383929 0.0583158614595201 synaptoporin FUNCTION: Intrinsic membrane protein of small synaptic vesicles. Probable vesicular channel protein (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);optic nerve;lung;hypothalamus;macula lutea;fovea centralis;choroid;lens;brain;skin;retina;cerebellum; superior cervical ganglion;occipital lobe;cerebellum peduncles;globus pallidus;ciliary ganglion;pons;caudate nucleus;trigeminal ganglion;parietal lobe;cerebellum; 0.05100 0.10588 -0.293801652 32.93819297 27.65858 0.88945 SYNPR-AS1 . . . SYNPR antisense RNA 1 . . . . . . . . . . . SYNRG 0.97274821167624 0.0272517859574317 2.36632837703069e-09 synergin, gamma FUNCTION: May play a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN). May act by linking the adapter protein complex AP-1 to other proteins.; . . smooth muscle;ovary;developmental;colon;parathyroid;bone marrow;uterus;prostate;whole body;frontal lobe;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;white blood cells;atrioventricular node; 0.05386 0.09802 -0.699966832 14.82071243 2722.3113 9.83401 SYP 0.611984996510125 0.379710357492403 0.00830464599747151 synaptophysin FUNCTION: Possibly involved in structural functions as organizing other membrane components or in targeting the vesicles to the plasma membrane. Involved in the regulation of short-term and long-term synaptic plasticity (By similarity). {ECO:0000250}.; DISEASE: Mental retardation, X-linked, SYP-related (MRXSYP) [MIM:300802]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:19377476}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Characteristic of a type of small (30-80 nm) neurosecretory vesicles, including presynaptic vesicles, but also vesicles of various neuroendocrine cells of both neuronal and epithelial phenotype.; unclassifiable (Anatomical System);amygdala;nervous;islets of Langerhans;pineal body;sympathetic chain;colon;fovea centralis;choroid;retina;lung;frontal lobe;macula lutea;visual apparatus;testis;mammary gland;pineal gland;brain;cerebellum;thymus; amygdala;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.39220 0.65186 -0.141298762 42.87567823 7.16622 0.26908 SYP-AS1 . . . SYP antisense RNA 1 . . . . . . . . . . . SYPL1 0.289132309522734 0.68975914877837 0.0211085416988952 synaptophysin-like 1 . . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;oral cavity;bile duct;pancreas;lung;pia mater;adrenal gland;placenta;duodenum;head and neck;kidney;stomach;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;spinal cord;atrioventricular node;uterus;testis - seminiferous tubule;trachea;thyroid;placenta;testis;ciliary ganglion;kidney;trigeminal ganglion; 0.11594 0.12639 -0.205617011 38.57631517 23.88737 0.78764 SYPL2 0.0167710987562036 0.887900326648951 0.0953285745948452 synaptophysin-like 2 FUNCTION: Involved in communication between the T-tubular and junctional sarcoplasmic reticulum (SR) membranes. {ECO:0000250}.; . . . . 0.15412 0.11014 0.927856124 89.70276008 498.0398 4.58560 SYS1 0.474140969012541 0.502188731192925 0.0236702997945344 Sys1 golgi trafficking protein FUNCTION: Involved in protein trafficking. May serve as a receptor for ARFRP1.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.21545 0.12378 0.125076652 62.7388535 23.14639 0.77196 SYS1-DBNDD2 . . . SYS1-DBNDD2 readthrough (NMD candidate) . . . . . . . . . . . SYT1 0.837180354589946 0.162683695712341 0.000135949697713377 synaptotagmin 1 FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2. Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000269|PubMed:23999003}.; DISEASE: Note=A SYT1 rare mutation has been found in a child with a severe neuro-developmental disorder. The individual harboring this variant shows early onset dyskinetic movement disorder, severe motor delay and profound cognitive impairment, suggesting that SYT1 may play a role in the pathogenesis of this neuro- developmental disorder. {ECO:0000269|PubMed:25705886}.; TISSUE SPECIFICITY: Expressed in melanocytes (PubMed:23999003). {ECO:0000269|PubMed:23999003}.; ovary;sympathetic chain;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;thyroid;bone;pituitary gland;testis;pineal gland;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;cerebellum cortex;hypothalamus;pineal body;blood;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;visual apparatus;head and neck;mammary gland; whole brain;amygdala;medulla oblongata;superior cervical ganglion;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.40819 0.46610 -0.139478553 43.29440906 4.7973 0.17444 SYT2 0.88781098862506 0.111940584481119 0.000248426893821513 synaptotagmin 2 FUNCTION: Exhibits calcium-dependent phospholipid and inositol polyphosphate binding properties (By similarity). May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse (By similarity). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000250|UniProtKB:P46097, ECO:0000269|PubMed:23999003}.; DISEASE: Myasthenic syndrome, congenital, 7, presynaptic (CMS7) [MIM:616040]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness. CMS7 is an autosomal dominant, presynaptic disorder resembling Lambert-Eaton myasthenic syndrome. Affected individuals have a variable degree of proximal and distal limb weakness, muscle fatigue that improves with rest, mild gait difficulties, and reduced or absent deep tendon reflexes. {ECO:0000269|PubMed:25192047}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in melanocytes (PubMed:23999003). {ECO:0000269|PubMed:23999003}.; . . 0.27610 0.24559 -0.626318434 17.03231894 25.95478 0.84337 SYT3 0.225605579212027 0.772766784579573 0.00162763620840042 synaptotagmin 3 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000250, ECO:0000269|PubMed:23999003}.; . TISSUE SPECIFICITY: Expressed in melanocytes (PubMed:23999003). {ECO:0000269|PubMed:23999003}.; unclassifiable (Anatomical System);ovary;placenta;visual apparatus;muscle;adrenal medulla;parathyroid;brain;retina; . 0.20106 0.09277 -1.243653018 5.372729417 44.09263 1.26585 SYT4 0.12760475421924 0.849439924485015 0.022955321295745 synaptotagmin 4 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000250|UniProtKB:P50232, ECO:0000269|PubMed:23999003}.; . TISSUE SPECIFICITY: Expressed in melanocytes (PubMed:23999003). Expressed in brain. Within brain, expression is highest in hippocampus, with substantial levels also detected in amygdala and thalamus (PubMed:23999003). {ECO:0000269|PubMed:23999003}.; unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pineal body;sympathetic chain;skeletal muscle;retina;prostate;whole body;lung;frontal lobe;adrenal gland;bone;visual apparatus;hippocampus;testis;pineal gland;brain;aorta; amygdala;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;pons;caudate nucleus;subthalamic nucleus;fetal brain;globus pallidus;parietal lobe;cingulate cortex;pituitary;cerebellum; 0.30541 0.14808 0.016664174 55.21939137 348.70036 3.95847 SYT5 0.00220633982463807 0.919577707418849 0.0782159527565125 synaptotagmin 5 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Regulates the Ca(2+)- dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;cartilage;ovary;islets of Langerhans;placenta;colon;parathyroid;brain;mammary gland; amygdala;whole brain;occipital lobe;superior cervical ganglion;medulla oblongata;temporal lobe;atrioventricular node;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.16777 0.17490 0.018483465 55.44939844 406.18171 4.22504 SYT6 0.0328455242915539 0.926837670810281 0.0403168048981647 synaptotagmin 6 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. May mediate Ca(2+)- regulation of exocytosis in acrosomal reaction in sperm (By similarity). {ECO:0000250}.; . . . . 0.88416 0.13233 -0.88906181 10.36801132 1905.13279 8.03338 SYT7 0.904578639335977 0.0952581250381506 0.000163235625871975 synaptotagmin 7 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in a variety of adult and fetal tissues.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;blood;lens;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;mammary gland;stomach;cerebellum; . . 0.13066 -0.670411825 15.61689078 145.76438 2.63119 SYT8 7.5902706627317e-13 0.00936620590481706 0.990633794094424 synaptotagmin 8 FUNCTION: Isoform 4 may play a role in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Mediates Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. May mediate Ca(2+)-regulation of exocytosis in insulin secreted cells (By similarity). {ECO:0000250}.; . . pancreas;lung;thyroid; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.16251 0.10723 1.159254003 92.6279783 6166.03196 16.41017 SYT9 0.331363732407492 0.667979085853566 0.000657181738942049 synaptotagmin 9 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis.; . . tongue;pituitary gland;head and neck;kidney;brain;skin; atrioventricular node;skeletal muscle;cerebellum; 0.35945 0.12025 -0.069700724 48.54328851 379.50766 4.10739 SYT10 0.123246845459562 0.875689184798937 0.0010639697415019 synaptotagmin 10 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed only in pancreas, lung and kidney. {ECO:0000269|PubMed:14756426}.; islets of Langerhans; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11773 0.11669 -0.334253673 30.70299599 169.86779 2.84431 SYT11 0.801740134718319 0.197118649036041 0.00114121624563982 synaptotagmin 11 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. {ECO:0000250}.; . . . . 0.51933 0.14886 -0.247889024 35.98726115 25.73826 0.83825 SYT12 1.02517315716305e-05 0.562414901906886 0.437574846361543 synaptotagmin 12 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. {ECO:0000250}.; . . . . 0.18612 . -0.310388054 32.14791224 573.73373 4.86164 SYT13 0.220165778639476 0.771535727722408 0.00829849363811548 synaptotagmin 13 FUNCTION: May be involved in transport vesicle docking to the plasma membrane. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, pancreas and kidney. {ECO:0000269|PubMed:11543631}.; ovary;colon;parathyroid;choroid;fovea centralis;bone marrow;retina;optic nerve;whole body;frontal lobe;cochlea;bone;testis;brain;unclassifiable (Anatomical System);islets of Langerhans;lens;skeletal muscle;pancreas;lung;macula lutea;liver;kidney;mammary gland;stomach;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.15386 0.12500 -0.534490515 20.70063694 43.04749 1.24539 SYT14 0.966548706607067 0.033439703718996 1.15896739370846e-05 synaptotagmin 14 FUNCTION: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Is Ca(2+)-independent.; . TISSUE SPECIFICITY: Highly expressed in fetal and adult brain tissue. {ECO:0000269|PubMed:21835308}.; unclassifiable (Anatomical System);ovary;bone;placenta;testis;parathyroid;retina; . 0.14829 0.11091 -0.492218069 22.35786742 733.82518 5.37435 SYT14P1 . . . synaptotagmin 14 pseudogene 1 FUNCTION: Plays a role in melanocyte differentiation; enhances dendrite outgrowth, melanin content and tyrosinase activity through the modulation of ERK and/or CREB pathways (PubMed:23999003). {ECO:0000269|PubMed:16376304, ECO:0000269|PubMed:23999003}.; . . . . 0.13157 . . . . . SYT15 3.40186944300935e-18 0.00017572259149283 0.999824277408507 synaptotagmin 15 FUNCTION: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. {ECO:0000250}.; . . . . 0.03366 0.12113 0.780798785 87.24345364 417.36536 4.27585 SYT16 0.00124651789754824 0.990051042971185 0.00870243913126624 synaptotagmin 16 FUNCTION: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Is Ca(2+)-independent.; . TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:11543631}.; . . 0.27409 0.10785 0.468503535 78.79806558 1126.03032 6.40143 SYT17 0.0236363497033387 0.96203578707938 0.0143278632172816 synaptotagmin 17 FUNCTION: Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000269|PubMed:23999003}.; . TISSUE SPECIFICITY: Expressed abundantly in brain (frontal and temporal lobes, hippocampus, hypothalamus, amygdala, substantia nigra, and pituitary), kidney, and prostate. Expressed in fetal brain, kidney and lung (PubMed:16672768). Expressed in melanocytes (PubMed:23999003). {ECO:0000269|PubMed:16672768, ECO:0000269|PubMed:23999003}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;muscle;parathyroid;fovea centralis;choroid;lens;retina;uterus;breast;optic nerve;frontal lobe;cerebral cortex;endometrium;thyroid;macula lutea;liver;pituitary gland;spleen;cervix;kidney;brain;stomach; whole brain;amygdala;prostate;occipital lobe;hypothalamus;prefrontal cortex;parietal lobe;pituitary; . 0.13066 -1.265702118 5.237084218 47.70433 1.34170 SYTL1 1.0822256796955e-07 0.540853805350284 0.459146086427148 synaptotagmin like 1 FUNCTION: May play a role in vesicle trafficking (By similarity). Binds phosphatidylinositol 3,4,5-trisphosphate. Acts as a RAB27A effector protein and may play a role in cytotoxic granule exocytosis in lymphocytes (By similarity). {ECO:0000250, ECO:0000269|PubMed:11278853, ECO:0000269|PubMed:18266782}.; . TISSUE SPECIFICITY: Highly expressed in bone marrow and lymphoid tissues. Detected at lower levels in cerebellum, occipital lobe, prostate, stomach, kidney, appendix, lung and trachea. Expressed in cytotoxic T-lymphocytes (CTL). {ECO:0000269|PubMed:11278853, ECO:0000269|PubMed:18266782}.; colon;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; . 0.36427 0.15179 -0.268115223 34.70747818 4478.82505 13.42423 SYTL2 2.11826952070561e-19 0.00337016869433493 0.996629831305665 synaptotagmin like 2 FUNCTION: Isoform 1 acts as a RAB27A effector protein and plays a role in cytotoxic granule exocytosis in lymphocytes. It is required for cytotoxic granule docking at the immunologic synapse. Isoform 4 binds phosphatidylserine (PS) and phosphatidylinositol- 4,5-bisphosphate (PIP2) and promotes the recruitment of glucagon- containing granules to the cell membrane in pancreatic alpha cells. Binding to PS is inhibited by Ca(2+) while binding to PIP2 is Ca(2+) insensitive. {ECO:0000269|PubMed:17182843, ECO:0000269|PubMed:18266782, ECO:0000269|PubMed:18812475}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in hematopoietic lineages with a strong expression in CD4 and CD8 T-lymphocytes. It is also widely expressed in nonhematopoietic tissues. Isoform 5 is expressed only in nonhematopoietic tissues. Isoform 4 is expressed in pancreatic alpha cells. {ECO:0000269|PubMed:17182843, ECO:0000269|PubMed:18266782, ECO:0000269|PubMed:18812475}.; unclassifiable (Anatomical System);smooth muscle;cartilage;heart;ovary;islets of Langerhans;hypothalamus;colon;parathyroid;skin;skeletal muscle;breast;uterus;pancreas;prostate;whole body;lung;endometrium;bone;placenta;testis;germinal center;kidney;brain;stomach; superior cervical ganglion;ciliary ganglion;parietal lobe;cingulate cortex; 0.21596 0.08969 1.335619269 94.2262326 514.10167 4.64149 SYTL3 2.13951132456814e-17 0.0037116411333431 0.996288358866657 synaptotagmin like 3 FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking. Binds phospholipids in the presence of calcium ions (By similarity). {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;retina;bone marrow;uterus;prostate;thyroid;bone;bladder;brain;unclassifiable (Anatomical System);pineal body;pharynx;blood;skeletal muscle;lung;nasopharynx;placenta;visual apparatus;liver;head and neck;kidney;stomach; atrioventricular node; 0.03896 0.09481 0.670564357 84.70158056 4944.84779 14.32787 SYTL4 0.0246065524770759 0.972583337075434 0.0028101104474901 synaptotagmin like 4 FUNCTION: Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca(2+)-independent manner (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;ovary;heart;cartilage;tongue;colon;parathyroid;skeletal muscle;skin;uterus;breast;pancreas;prostate;lung;whole body;endometrium;larynx;placenta;bone;visual apparatus;liver;testis;spleen;head and neck;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.30439 0.12917 0.262810045 70.43524416 75.75389 1.82286 SYTL5 0.0644886545028385 0.934871477036456 0.000639868460705298 synaptotagmin like 5 FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking. Binds phospholipids.; . TISSUE SPECIFICITY: Highly expressed in placenta and liver.; unclassifiable (Anatomical System);breast;prostate;lung;cochlea;macula lutea;testis;fovea centralis;skin; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.23403 0.10729 0.556689353 81.63481953 424.2832 4.30328 SYVN1 0.996650377830331 0.00334958134788803 4.08217813594189e-08 synoviolin 1 FUNCTION: Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation. Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis. {ECO:0000269|PubMed:12459480, ECO:0000269|PubMed:12646171, ECO:0000269|PubMed:12975321, ECO:0000269|PubMed:14593114, ECO:0000269|PubMed:16289116, ECO:0000269|PubMed:16847254, ECO:0000269|PubMed:17059562, ECO:0000269|PubMed:17141218, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:22607976}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in liver and kidney (at protein level). Up-regulated in synovial tissues from patients with rheumatoid arthritis (at protein level). {ECO:0000269|PubMed:12459480, ECO:0000269|PubMed:12646171, ECO:0000269|PubMed:12975321}.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;placenta;head and neck;kidney;stomach;thymus;cerebellum; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.59025 0.19231 -0.734731259 14.01863647 790.86604 5.54609 SZRD1 0.719865991219815 0.266420426694125 0.0137135820860604 SUZ RNA binding domain containing 1 . . . . . 0.75505 . -0.141298762 42.87567823 14.19698 0.51325 SZT2 1.51746679777732e-07 0.99999984825332 4.6978326740771e-20 seizure threshold 2 homolog (mouse) FUNCTION: Involved in oxidative stress. May be involved in superoxide dismutase activity and in neuroprotective effect of peroxisomes, but has no direct dismutase activity when tested in yeast. May enhance epileptogenesis and confer low seizure threshold (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the brain, predominantly in the parietal and frontal cortex, as well as in dorsal root ganglia. Expressed in peripheral white blood cells. {ECO:0000269|PubMed:20045724, ECO:0000269|PubMed:23932106}.; unclassifiable (Anatomical System);prostate;lung;heart;pituitary gland;colon;cervix; . . 0.09202 . . 2151.43823 8.52940 SZT2-AS1 . . . SZT2 antisense RNA 1 . . . . . . . . . . . T 0.000208190165714723 0.907779326643455 0.0920124831908302 T brachyury transcription factor FUNCTION: Involved in the transcriptional regulation of genes required for mesoderm formation and differentiation. Binds to a palindromic site (called T site) and activates gene transcription when bound to such a site.; DISEASE: Chordoma (CHDM) [MIM:215400]: Rare, clinically malignant tumors derived from notochordal remnants. They occur along the length of the spinal axis, predominantly in the sphenooccipital, vertebral and sacrococcygeal regions. They are characterized by slow growth, local destruction of bone, extension into adjacent soft tissues and rarely, distant metastatic spread. {ECO:0000269|PubMed:19801981}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Susceptibility to development of chordomas is due to a T gene duplication.; DISEASE: Sacral agenesis with vertebral anomalies (SAVA) [MIM:615709]: A disorder characterized by abnormalities of the spine, including sacral agenesis, abnormal ossification of all vertebral bodies, and a persistent notochordal canal during development. {ECO:0000269|PubMed:24253444}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in testis, but not in other, normal tissues. Detected in lung tumors (at protein level). {ECO:0000269|PubMed:22611028}.; unclassifiable (Anatomical System);lung;testis;blood;mammary gland; ciliary ganglion; 0.29523 0.27623 0.687150476 85.17928757 2758.54076 9.90729 TAAR1 0.000283698038082418 0.341498193390579 0.658218108571338 trace amine associated receptor 1 FUNCTION: Receptor for trace amines, including beta- phenylethylamine (b-PEA), p-tyramine (p-TYR), octopamine and tryptamine, with highest affinity for b-PEA and p-TYR. Unresponsive to classical biogenic amines, such as epinephrine and histamine and only partially activated by dopamine and serotonine. Trace amines are biogenic amines present in very low levels in mammalian tissues. Although some trace amines have clearly defined roles as neurotransmitters in invertebrates, the extent to which they function as true neurotransmitters in vertebrates has remained speculative. Trace amines are likely to be involved in a variety of physiological functions that have yet to be fully understood. The signal transduced by this receptor is mediated by the G(s)-class of G-proteins which activate adenylate cyclase. {ECO:0000269|PubMed:15718104}.; . TISSUE SPECIFICITY: Detected in low levels in discrete regions within the central nervous system and in several peripheral tissues. Moderately expressed in stomach. Low levels in amygdala, kidney, and lung, and small intestine. Trace amounts in cerebellum, dorsal root ganglia, hippocampus, hypothalamus, liver, medulla, pancreas, pituitary, pontine reticular formation, prostate, skeletal muscle and spleen.; stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11156 0.10520 -0.26993514 34.59542345 113.0813 2.31420 TAAR2 3.41448199446952e-06 0.195974534395613 0.804022051122393 trace amine associated receptor 2 FUNCTION: Orphan receptor.; . TISSUE SPECIFICITY: Not expressed in the pons, thalamus, hypothalamus, hippocampus, caudate, putamen, frontal cortex, basal forebrain, midbrain or liver.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19224 0.07689 0.196671391 67.19155461 1296.89322 6.77800 TAAR3 . . . trace amine associated receptor 3 (gene/pseudogene) FUNCTION: Olfactory receptor activated by several primary trace amines, including isoamylamine. Activated by isoamylamine and cyclohexylamine, but not to the corresponding alcohols, isoamylalcohol and cyclohexanol. This receptor is probably mediated by the G(s)-class of G-proteins which activate adenylate cyclase (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Not expressed in the pons, thalamus, globus pallidus, caudate, putamen or cerebellum.; . . . . . . . . TAAR4P . . . trace amine associated receptor 4, pseudogene . . . . . . . . . . . TAAR5 3.45752187600458e-07 0.0543099309855103 0.945689723262302 trace amine associated receptor 5 FUNCTION: Olfactory receptor specific for trimethylamine, a trace amine. Also activated at lower level by dimethylethylamine. Trimethylamine is a bacterial metabolite found in some animal odors, and to humans it is a repulsive odor associated with bad breath and spoiled food. This receptor is probably mediated by the G(s)-class of G-proteins which activate adenylate cyclase. {ECO:0000269|PubMed:23393561}.; . TISSUE SPECIFICITY: Expressed almost exclusively in skeletal muscle and selected areas of the brain, such amygdala, hippocampus, caudate nucleus, thalamus and hypothalamus. Weak expression is also find in substantia nigra. {ECO:0000269|PubMed:9464258}.; . . 0.16922 0.09999 0.486911049 79.46449634 372.19005 4.07152 TAAR6 0.153131232007238 0.77666933658363 0.0701994314091318 trace amine associated receptor 6 FUNCTION: Orphan receptor. Could be a receptor for trace amines. Trace amines are biogenic amines present in very low levels in mammalian tissues. Although some trace amines have clearly defined roles as neurotransmitters in invertebrates, the extent to which they function as true neurotransmitters in vertebrates has remained speculative. Trace amines are likely to be involved in a variety of physiological functions that have yet to be fully understood.; . TISSUE SPECIFICITY: Expressed at low abundance in various brain tissues, as well as in fetal liver, but not in the cerebellum or placenta. In the brain, comparable levels of expression in basal ganglia, frontal cortex, substantia nigra, amygdala and hippocampus, highest expression in hippocampus and lowest expression in basal ganglia. {ECO:0000269|PubMed:15329799}.; . . 0.09669 0.12526 2.019241996 97.71172446 949.23434 5.96544 TAAR7P . . . trace amine associated receptor 7, pseudogene . . . . . . . . . . . TAAR8 0.000303108489621688 0.352606698226266 0.647090193284112 trace amine associated receptor 8 FUNCTION: Orphan receptor. Could be a receptor for trace amines. Trace amines are biogenic amines present in very low levels in mammalian tissues. Although some trace amines have clearly defined roles as neurotransmitters in invertebrates, the extent to which they function as true neurotransmitters in vertebrates has remained speculative. Trace amines are likely to be involved in a variety of physiological functions that have yet to be fully understood.; . TISSUE SPECIFICITY: Expressed in kidney and amygdala. Not expressed in other tissues or brain regions tested. {ECO:0000269|PubMed:11459929}.; unclassifiable (Anatomical System); superior cervical ganglion;atrioventricular node; 0.12826 . 0.507139401 80.10143902 140.55666 2.58585 TAAR9 . . . trace amine associated receptor 9 (gene/pseudogene) FUNCTION: Orphan receptor. Could be a receptor for trace amines. Trace amines are biogenic amines present in very low levels in mammalian tissues. Although some trace amines have clearly defined roles as neurotransmitters in invertebrates, the extent to which they function as true neurotransmitters in vertebrates has remained speculative. Trace amines are likely to be involved in a variety of physiological functions that have yet to be fully understood.; . . . . . . . . . . TAB1 0.00399581121095206 0.987970242332571 0.0080339464564768 TGF-beta activated kinase 1/MAP3K7 binding protein 1 FUNCTION: May be an important signaling intermediate between TGFB receptors and MAP3K7/TAK1. May play an important role in mammalian embryogenesis.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;frontal lobe;larynx;thyroid;bone;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;hypothalamus;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.35773 0.30319 -1.217968826 5.638122199 305.94322 3.72456 TAB2 0.99975796201866 0.000242037647670117 3.33669483769146e-10 TGF-beta activated kinase 1/MAP3K7 binding protein 2 FUNCTION: Adapter linking MAP3K7/TAK1 and TRAF6. Promotes MAP3K7 activation in the IL1 signaling pathway. The binding of 'Lys-63'- linked polyubiquitin chains to TAB2 promotes autophosphorylation of MAP3K7 at 'Thr-187'. Involved in heart development. {ECO:0000269|PubMed:10882101, ECO:0000269|PubMed:11460167, ECO:0000269|PubMed:20493459}.; DISEASE: Congenital heart defects, multiple types, 2 (CHTD2) [MIM:614980]: A disease characterized by congenital developmental abnormalities involving structures of the heart. CHTD2 patients have left ventricular outflow tract obstruction, subaortic stenosis, residual aortic regurgitation, atrial fibrillation, bicuspid aortic valve and aortic dilation. {ECO:0000269|PubMed:20493459}. Note=The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving TAB2 has been found in a family with congenital heart disease. Translocation t(2;6)(q21;q25).; TISSUE SPECIFICITY: Widely expressed. In the embryo, expressed in the ventricular trabeculae, endothelial cells of the conotruncal cushions of the outflow tract and in the endothelial cells lining the developing aortic valves. {ECO:0000269|PubMed:10882101, ECO:0000269|PubMed:20493459}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;larynx;bone;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;placenta;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;skeletal muscle;parietal lobe;cerebellum; 0.41916 0.22685 -1.111360919 6.717386176 16.16045 0.57314 TAB3 0.921511503588616 0.0784684411825435 2.00552288404953e-05 TGF-beta activated kinase 1/MAP3K7 binding protein 3 FUNCTION: Adapter linking MAP3K7/TAK1 and TRAF6 or TRAF2. Mediator of MAP3K7 activation, respectively in the IL1 and TNF signaling pathways. Plays a role in activation of NF-kappa-B and AP1 transcription factor. Isoform 2 may be an oncogenic factor. {ECO:0000269|PubMed:14633987, ECO:0000269|PubMed:14766965}.; . TISSUE SPECIFICITY: Widely expressed. Constitutively overexpressed in certain tumor tissues. Isoform 1 is a major transcript while isoform 2 is a minor transcript. {ECO:0000269|PubMed:14670075, ECO:0000269|PubMed:14766965}.; unclassifiable (Anatomical System);breast;uterus;lymph node;lung;placenta;hypopharynx;colon;blood;head and neck;germinal center;retina; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.38381 0.11678 -0.670411825 15.61689078 3159.31368 10.70693 TAB3-AS1 . . . TAB3 antisense RNA 1 . . . . . . . . . . . TAB3-AS2 . . . TAB3 antisense RNA 2 . . . . . . . . . . . TAB3P1 . . . TGF-beta activated kinase 1/MAP3K7 binding protein 3 pseudogene 1 . . . . . . . . . . . TAC1 0.877314614642078 0.121170638637091 0.00151474672083108 tachykinin precursor 1 FUNCTION: Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles.; . . unclassifiable (Anatomical System);cartilage;hypothalamus;substantia nigra;fovea centralis;choroid;lens;retina;optic nerve;whole body;trabecular meshwork;placenta;hippocampus;macula lutea;spleen;kidney; whole brain;amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;hypothalamus;ciliary ganglion;caudate nucleus;pons;trigeminal ganglion; 0.25932 0.23974 -0.009020804 52.8544468 6.0286 0.22770 TAC3 0.040450004755837 0.842452057025413 0.11709793821875 tachykinin 3 FUNCTION: Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles (By similarity). Is a critical central regulator of gonadal function. {ECO:0000250, ECO:0000269|PubMed:19079066}.; DISEASE: Hypogonadotropic hypogonadism 10 with or without anosmia (HH10) [MIM:614839]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:19079066, ECO:0000269|PubMed:23643382}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . uterus;unclassifiable (Anatomical System);lung;placenta;urinary;liver;testis;spleen; superior cervical ganglion;placenta;pons;trigeminal ganglion; 0.05970 0.18092 0.03689118 56.64071715 13.62595 0.49504 TAC4 0.0419589061072124 0.845847776209935 0.112193317682852 tachykinin 4 (hemokinin) FUNCTION: Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. Endokinin-A induces thermal hyperalgesia and pain-related behavior such as scratching following intrathecal administration in rats. These effects are suppressed by treatment with endokinin- C. Endokinin-A/B reduces arterial blood pressure and increases sperm motility. {ECO:0000269|PubMed:12716968, ECO:0000269|PubMed:17101218, ECO:0000269|PubMed:17437961, ECO:0000269|PubMed:17655832}.; . TISSUE SPECIFICITY: Expressed at low levels in the uterus of both pregnant and non-pregnant women. Isoform 1 is found only in the adrenal gland and fetal liver. Isoform 2 is found in heart, liver, bone marrow, prostate, adrenal gland and testis. Isoform 3 and isoform 4 are expressed predominantly in adrenal gland and placenta. {ECO:0000269|PubMed:12716968, ECO:0000269|PubMed:12788812}.; larynx;head and neck; . 0.00451 0.20220 0.21326276 67.71644256 193.20212 3.01252 TACC1 0.0151208742819385 0.984640575297733 0.000238550420328379 transforming acidic coiled-coil containing protein 1 FUNCTION: Likely involved in the processes that promote cell division prior to the formation of differentiated tissues.; . TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 5 are ubiquitous. Isoform 2 is strongly expressed in the brain, weakly detectable in lung and colon, and overexpressed in gastric cancer. Isoform 4 is not detected in normal tissues, but strong expression was found in gastric cancer tissues. Down-regulated in a subset of cases of breast cancer. {ECO:0000269|PubMed:12165861, ECO:0000269|PubMed:12547166}.; smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;bladder;amygdala;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;atrium;larynx;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;amygdala;occipital lobe;superior cervical ganglion;subthalamic nucleus;olfactory bulb;prefrontal cortex;atrioventricular node;cingulate cortex;parietal lobe; 0.18153 0.10845 -0.639268965 16.70794999 84.23672 1.95388 TACC1P1 . . . transforming acidic coiled-coil containing protein 1 pseudogene 1 . . . . . . . . . . . TACC2 3.52232783639013e-19 0.948831744942938 0.0511682550570616 transforming acidic coiled-coil containing protein 2 FUNCTION: Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors (By similarity). May play a role in organizing centrosomal microtubules. May act as a tumor suppressor protein. May represent a tumor progression marker. {ECO:0000250, ECO:0000269|PubMed:10749935}.; . TISSUE SPECIFICITY: Strongly expressed in heart, skeletal muscle, brain, prostate, thyroid and trachea. {ECO:0000269|PubMed:11161455, ECO:0000269|PubMed:12620397}.; ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;gum;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;placenta;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.16116 0.08314 4.102912459 99.68152866 4233.01874 12.93938 TACC3 0.0919518142926963 0.9076903782622 0.000357807445103661 transforming acidic coiled-coil containing protein 3 FUNCTION: Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors (By similarity). May be involved in the control of cell growth and differentiation. May contribute to cancer. {ECO:0000250}.; . . lymphoreticular;medulla oblongata;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; testis - interstitial;fetal liver;superior cervical ganglion;testis - seminiferous tubule;tumor;appendix;testis;white blood cells;whole blood;trigeminal ganglion;tonsil;bone marrow;thymus; 0.60266 0.07352 0.099178678 60.75725407 2050.27567 8.34503 TACO1 0.357585528083816 0.629940944095379 0.0124735278208049 translational activator of mitochondrially encoded cytochrome c oxidase I FUNCTION: Acts as a translational activator of mitochondrially- encoded cytochrome c oxidase 1. {ECO:0000269|PubMed:19503089}.; DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;muscle;adrenal cortex;pharynx;blood;lens;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; heart;liver;pons;kidney;trigeminal ganglion;cingulate cortex; 0.06638 0.23959 -0.183570861 39.95046001 160.55214 2.76510 TACR1 0.000227888560237543 0.74940879259785 0.250363318841912 tachykinin receptor 1 FUNCTION: This is a receptor for the tachykinin neuropeptide substance P. It is probably associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: substance P > substance K > neuromedin-K.; . . unclassifiable (Anatomical System);amygdala;brain;retina; superior cervical ganglion;uterus corpus;ciliary ganglion;pons;caudate nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.19646 0.21851 -0.758599262 13.32861524 23.8871 0.78737 TACR2 9.87812061995907e-07 0.182986486293253 0.817012525894685 tachykinin receptor 2 FUNCTION: This is a receptor for the tachykinin neuropeptide substance K (neurokinin A). It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: substance K > neuromedin-K > substance P. {ECO:0000269|PubMed:1659297}.; . . . . 0.13034 0.15131 2.087222794 97.84736966 2401.1648 9.09848 TACR3 1.89892528244929e-06 0.442920783701252 0.557077317373466 tachykinin receptor 3 FUNCTION: This is a receptor for the tachykinin neuropeptide neuromedin-K (neurokinin B). It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: neuromedin-K > substance K > substance P.; DISEASE: Hypogonadotropic hypogonadism 11 with or without anosmia (HH11) [MIM:614840]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:19079066, ECO:0000269|PubMed:23643382, ECO:0000269|PubMed:25077900}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. The genetics of hypogonadotropic hypogonadism involves various modes of transmission. Oligogenic inheritance has been reported in some patients carrying mutations in TACR3 as well as in other HH-associated genes including FGFR1, SPRY4 and KAL1 (PubMed:23643382). {ECO:0000269|PubMed:23643382}.; . skeletal muscle; medulla oblongata;ciliary ganglion; 0.10536 0.14254 -0.336073593 30.55555556 139.73693 2.57700 TACSTD2 0.20524803232453 0.648131950188463 0.146620017487007 tumor-associated calcium signal transducer 2 FUNCTION: May function as a growth factor receptor.; DISEASE: Corneal dystrophy, gelatinous drop-like (GDLD) [MIM:204870]: A form of lattice corneal dystrophy, a class of inherited stromal amyloidoses characterized by pathognomonic branching lattice figures in the cornea. GDLD is an autosomal recessive disorder characterized by severe corneal amyloidosis leading to blindness. Clinical manifestations, which appear in the first decade of life, include blurred vision, photophobia, and foreign-body sensation. By the third decade, raised, yellowish- gray, gelatinous masses severely impair visual acuity. {ECO:0000269|PubMed:10192395}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Placenta, pancreatic carcinoma cell lines.; . . 0.34128 0.25561 1.082196027 91.79641425 2084.77347 8.41075 TADA1 0.358858662861777 0.638545861595885 0.002595475542338 transcriptional adaptor 1 FUNCTION: Probably involved in transcriptional regulation.; . . . . 0.28741 0.11262 -0.227663163 37.11370606 283.00954 3.60172 TADA2A 9.66223224552016e-05 0.997019371002294 0.00288400667525088 transcriptional adaptor 2A FUNCTION: Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. Required for the function of some acidic activation domains, which activate transcription from a distant site (By similarity). Binds double- stranded DNA. Binds dinucleosomes, probably at the linker region between neighboring nucleosomes. Plays a role in chromatin remodeling. {ECO:0000250, ECO:0000269|PubMed:19103755}.; . TISSUE SPECIFICITY: Expressed in all tissues, but most abundantly in testis.; unclassifiable (Anatomical System);adrenal cortex;pharynx;colon;blood;skeletal muscle;retina;prostate;whole body;endometrium;nasopharynx;bone;visual apparatus;alveolus;liver;spleen;cervix;germinal center;kidney;brain;pineal gland;mammary gland; dorsal root ganglion;superior cervical ganglion;adrenal cortex;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.36586 0.25702 0.418953042 77.06416608 105.19812 2.21952 TADA2B 0.345059566153662 0.641231106486964 0.0137093273593738 transcriptional adaptor 2B FUNCTION: Coactivates PAX5-dependent transcription together with either SMARCA4 or GCN5L2. {ECO:0000269|PubMed:12972612}.; . . medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;prostate;frontal lobe;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;trigeminal ganglion;cerebellum; . . -0.295622497 32.61972163 15.63303 0.55745 TADA3 0.0047473552883576 0.965911098285296 0.0293415464263464 transcriptional adaptor 3 FUNCTION: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex. Also known as a coactivator for p53/TP53-dependent transcriptional activation. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. {ECO:0000269|PubMed:11707411, ECO:0000269|PubMed:19103755}.; . TISSUE SPECIFICITY: Ubiquitously expressed.; lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;pineal body;muscle;adrenal cortex;lens;breast;bile duct;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;whole brain;superior cervical ganglion;occipital lobe;testis - interstitial;heart;testis;ciliary ganglion;atrioventricular node;skeletal muscle;parietal lobe; 0.47662 0.11262 -0.714505427 14.4019816 11.34377 0.40807 TAF1 0.999999755773455 2.44226544477114e-07 6.87678800812412e-19 TATA-box binding protein associated factor 1 FUNCTION: Largest component and core scaffold of the TFIID basal transcription factor complex. Contains novel N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors. Phosphorylates TP53 on 'Thr-55' which leads to MDM2-mediated degradation of TP53. Phosphorylates GTF2A1 and GTF2F1 on Ser residues. Possesses DNA- binding activity. Essential for progression of the G1 phase of the cell cycle (PubMed:11278496, PubMed:15053879, PubMed:2038334, PubMed:8450888, PubMed:8625415, PubMed:9660973, PubMed:9858607). Exhibits histone acetyltransferase activity towards histones H3 and H4 (PubMed:15870300). {ECO:0000269|PubMed:11278496, ECO:0000269|PubMed:15053879, ECO:0000269|PubMed:15870300, ECO:0000269|PubMed:2038334, ECO:0000269|PubMed:8450888, ECO:0000269|PubMed:8625415, ECO:0000269|PubMed:9660973, ECO:0000269|PubMed:9858607}.; DISEASE: Dystonia 3, torsion, X-linked (DYT3) [MIM:314250]: A X- linked dystonia-parkinsonism disorder. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. DYT3 is characterized by severe progressive torsion dystonia followed by parkinsonism. It has a well-defined pathology of extensive neuronal loss and mosaic gliosis in the striatum (caudate nucleus and putamen) which appears to resemble that in Huntington disease. {ECO:0000269|PubMed:12928496, ECO:0000269|PubMed:17273961}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);smooth muscle;colon;skin;retina;breast;uterus;pancreas;prostate;lung;endometrium;larynx;thyroid;placenta;hypopharynx;liver;testis;cervix;head and neck;spleen;germinal center;brain;peripheral nerve;thymus; superior cervical ganglion;globus pallidus;pons;trigeminal ganglion;skeletal muscle; 0.65141 0.18046 -0.420619508 25.72540694 384.74802 4.13320 TAF1A 6.60087794025323e-07 0.691838677899284 0.308160662012922 TATA-box binding protein associated factor, RNA polymerase I subunit A FUNCTION: Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (pre- initiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. Formation of SL1/TIF-IB excludes the association of TBP with TFIID subunits. {ECO:0000269|PubMed:15970593, ECO:0000269|PubMed:7801123}.; . . unclassifiable (Anatomical System);lymph node;heart;colon;skin;uterus;lung;nasopharynx;bone;placenta;testis;head and neck;germinal center;kidney;stomach; superior cervical ganglion;testis - interstitial;appendix;atrioventricular node;trigeminal ganglion; 0.05825 0.06800 0.595326758 82.66100495 339.95091 3.91176 TAF1A-AS1 . . . TAF1A antisense RNA 1 . . . . . . . . . . . TAF1B 4.28699121753238e-06 0.989831053181665 0.0101646598271175 TATA-box binding protein associated factor, RNA polymerase I subunit B FUNCTION: Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during trancription initiation such as preinitiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment as a component of the SL1/TIF-IB complex and, possibly, directly through its interaction with RRN3. {ECO:0000269|PubMed:15970593, ECO:0000269|PubMed:21921198, ECO:0000269|PubMed:21921199, ECO:0000269|PubMed:7491500, ECO:0000269|PubMed:7801123, ECO:0000269|PubMed:7801130}.; . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;trigeminal ganglion;skin; 0.21122 0.12686 0.756930627 86.79523473 2896.55966 10.19715 TAF1C 3.23271531745362e-11 0.472377145903275 0.527622854064398 TATA-box binding protein associated factor, RNA polymerase I subunit C FUNCTION: Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. Formation of SL1/TIF-IB excludes the association of TBP with TFIID subunits. Recruits RNA polymerase I to the rRNA gene promoter via interaction with RRN3. {ECO:0000269|PubMed:11250903, ECO:0000269|PubMed:15970593}.; . . myocardium;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;adrenal cortex;blood;lens;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; fetal brain;white blood cells;pons;caudate nucleus;trigeminal ganglion;cingulate cortex; 0.24194 0.09250 0.593325282 82.46048596 1956.88534 8.14058 TAF1D 0.00591146736086776 0.904017854477607 0.0900706781615252 TATA-box binding protein associated factor, RNA polymerase I subunit D FUNCTION: Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. Formation of SL1/TIF-IB excludes the association of TBP with TFIID subunits. {ECO:0000269|PubMed:15970593, ECO:0000269|PubMed:17318177}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;brain;amygdala;heart;cartilage;blood;lens;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; globus pallidus;tumor;white blood cells;trigeminal ganglion; 0.39690 0.08819 0.260991686 70.25831564 54.87123 1.48466 TAF1L 0.119270692068056 0.880727412044107 1.89588783746682e-06 TATA-box binding protein associated factor 1 like FUNCTION: May act as a functional substitute for TAF1/TAFII250 during male meiosis, when sex chromosomes are transcriptionally silenced. {ECO:0000269|PubMed:12217962}.; . TISSUE SPECIFICITY: Testis specific, expressed apparently in germ cells.; unclassifiable (Anatomical System);colon; . 0.73239 . -0.602715221 17.75182826 628.82772 5.05283 TAF2 0.566087060043687 0.433912903830149 3.61261637586587e-08 TATA-box binding protein associated factor 2 FUNCTION: Transcription factor TFIID is one of the general factors required for accurate and regulated initiation by RNA polymerase II. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. It requires core promoter-specific cofactors for productive transcription stimulation. TAF2 stabilizes TFIID binding to core promoter. {ECO:0000269|PubMed:9418870, ECO:0000269|PubMed:9774672}.; . TISSUE SPECIFICITY: Expressed in all tissues tested. {ECO:0000269|PubMed:9774672}.; . . 0.41383 0.11900 -0.042196577 50.49539986 1043.41092 6.19966 TAF3 0.995125179714143 0.00487479963699372 2.06488627854857e-08 TATA-box binding protein associated factor 3 FUNCTION: Transcription factor TFIID is one of the general factors required for accurate and regulated initiation by RNA polymerase II. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Required in complex with TBPL2 for the differentiation of myoblasts into myocytes. The complex replaces TFIID at specific promoters at an early stage in the differentiation process.; . . lymph node;lung;bone;macula lutea;testis;colon;fovea centralis;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.89948 0.11087 0.554869705 81.59943383 223.31196 3.23028 TAF4 0.999487085673133 0.000512913906091387 4.2077555294397e-10 TATA-box binding protein associated factor 4 FUNCTION: Part of the TFIID complex, a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Potentiates transcriptional activation by the AF-2S of the retinoic acid, vitamin D3 and thyroid hormone.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;whole body;cochlea;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;tongue;muscle;blood;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.57067 0.18546 . . 1121.27796 6.39272 TAF4B 0.879312141538273 0.120687351295085 5.07166642276207e-07 TATA-box binding protein associated factor 4b FUNCTION: Cell type-specific subunit of the general transcription factor TFIID that may function as a gene-selective coactivator in certain cells. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. TAF4B is a transcriptional coactivator of the p65/RELA NF-kappa-B subunit. Involved in the activation of a subset of antiapoptotic genes including TNFAIP3. May be involved in regulating folliculogenesis. Through interaction with OCBA/POU2AF1, acts as a coactivator of B-cell-specific transcription. Plays a role in spermiogenesis and oogenesis. {ECO:0000250|UniProtKB:G5E8Z2, ECO:0000269|PubMed:10828057, ECO:0000269|PubMed:10849440, ECO:0000269|PubMed:16088961, ECO:0000303|PubMed:24431330}.; DISEASE: Spermatogenic failure 13 (SPGF13) [MIM:615841]: A disorder resulting in the absence (azoospermia) or reduction (oligozoospermia) of sperm in the semen, leading to male infertility. {ECO:0000269|PubMed:24431330}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Preferentially expressed in ovarian granulosa cells (at protein level). Highly expressed in B-cells. {ECO:0000269|PubMed:16088961, ECO:0000269|PubMed:8858156}.; unclassifiable (Anatomical System);colon;kidney;stomach;retina; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.75587 0.10909 0.580556395 82.31304553 754.14298 5.44535 TAF5 0.999555180536955 0.000444819165655365 2.97389238673926e-10 TATA-box binding protein associated factor 5 FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription. TAF5/TAFII100 interacts strongly with the histone H4-related TAF6/TAFII80 and the histone H3-related TAF9/TAFII31, as well as a stable complex comprised of both TAF5/TAFII80 and TAF6/TAFII31. Apparently weaker interactions of TAF5/TAFII100 with TBP, TAF1/TAFII250, TAF11/TAFII28, and TAF12/TAFII20, but not TAF7/TAFII55, also have been observed.; . . unclassifiable (Anatomical System);ovary;bone;placenta;testis;parathyroid;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;atrioventricular node; 0.92474 0.12743 -0.558357437 19.54470394 2345.15679 8.97048 TAF5L 0.985849776766725 0.0141488369303251 1.38630295007059e-06 TATA-box binding protein associated factor 5 like FUNCTION: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex.; . . unclassifiable (Anatomical System);ovary;heart;tongue;islets of Langerhans;colon;blood;skin;bone marrow;uterus;pancreas;whole body;lung;cochlea;endometrium;larynx;placenta;liver;testis;head and neck;kidney;germinal center;brain;mammary gland;cerebellum; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.35442 0.13417 -1.063626766 7.484076433 56.0239 1.50377 TAF5LP1 . . . TAF5-like RNA polymerase II, p300/CBP-associated factor (PCAF)-associated factor, 65kDa pseudogene 1 . . . . . . . . . . . TAF6 0.00067416521660161 0.998446760598071 0.00087907418532706 TATA-box binding protein associated factor 6 FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TIIFD is multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors.; . . smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;skin;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;breast;lung;epididymis;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - seminiferous tubule;globus pallidus;testis;cingulate cortex; 0.73985 0.13844 -1.217968826 5.638122199 236.6392 3.32188 TAF6L 0.819819294441314 0.180144365365354 3.63401933318072e-05 TATA-box binding protein associated factor 6 like FUNCTION: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;ganglion;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;blood;lens;breast;pancreas;lung;placenta;macula lutea;spleen;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;caudate nucleus;skin;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.11824 0.09089 -0.356299879 29.31115829 71.83373 1.76480 TAF7 0.736629403611825 0.260821310728787 0.00254928565938809 TATA-box binding protein associated factor 7 FUNCTION: Functions as a component of the DNA-binding general transcription factor complex TFIID, a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Present in both of the previously described TFIID species which either lack or contain TAFII30 (TFIID alpha and TFIID beta respectively).; . TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta; amygdala; 0.58984 0.15588 -0.317668748 31.45789101 9.53967 0.35088 TAF7L 0.843722648897641 0.156155676510072 0.000121674592287321 TATA-box binding protein associated factor 7 like FUNCTION: Probably functions as a spermatogensis-specific component of the DNA-binding general transcription factor complex TFIID, a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. May play a role in spermatogenesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:11279525}.; unclassifiable (Anatomical System);lung;visual apparatus;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.04200 0.07218 0.306902668 72.38145789 971.03978 6.02282 TAF8 3.04223621180909e-09 0.0873447649963109 0.912655231961453 TATA-box binding protein associated factor 8 FUNCTION: Transcription factor TFIID is one of the general factors required for accurate and regulated initiation by RNA polymerase II. Mediates both basal and activator-dependent transcription. Plays a role in the differentiation of preadipocyte fibroblasts to adipocytes, however, does not seem to play a role in differentiation of myoblasts. Required for the integration of TAF10 in the TAF complex. May be important for survival of cells of the inner cell mass which constitute the pluripotent cell population of the early embryo (By similarity). {ECO:0000250, ECO:0000269|PubMed:14580349}.; . . . . 0.31114 0.25991 -0.381986487 27.68931352 21.02525 0.71190 TAF9 5.73990719710396e-05 0.268000030187452 0.731942570740577 TATA-box binding protein associated factor 9 FUNCTION: Essential for cell viability. TAF9 and TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes. May have a role in gene regulation associated with apoptosis. TAFs are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription. {ECO:0000269|PubMed:15899866}.; . . lymphoreticular;medulla oblongata;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;kidney;stomach; . 0.95557 0.38833 -0.358119787 29.16371786 66.03446 1.67407 TAF9B 0.000410982863235518 0.639298463924084 0.36029055321268 TATA-box binding protein associated factor 9b FUNCTION: Essential for cell viability. TAF9 and TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes. May have a role in gene regulation associated with apoptosis. TAFs are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription. {ECO:0000269|PubMed:15899866}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;hippocampus;amnion;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; occipital lobe;trigeminal ganglion; 0.70948 0.12006 -0.251530012 35.42108988 18.53211 0.64081 TAF9BP1 . . . TATA-box binding protein associated factor 9b pseudogene 1 . . . . . . . . . . . TAF9BP2 . . . TATA-box binding protein associated factor 9b pseudogene 2 . . . . . . . . . . . TAF9P1 . . . TATA-box binding protein associated factor 9 pseudogene 1 . . . . . . . . . . . TAF9P2 . . . TATA-box binding protein associated factor 9 pseudogene 2 . . . . . . . . . . . TAF9P3 . . . TATA-box binding protein associated factor 9 pseudogene 3 . . . . . . . . . . . TAF10 0.77613089905454 0.216447854987408 0.00742124595805273 TATA-box binding protein associated factor 10 FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TIIFD is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors.; . . lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;nervous;islets of Langerhans;pineal body;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;thymus; testis - interstitial;testis - seminiferous tubule;liver;testis; 0.80506 0.17133 . . 42.39539 1.23240 TAF11 0.875431936618392 0.122992391244556 0.00157567213705265 TATA-box binding protein associated factor 11 FUNCTION: Core TAFII present in both of the previously described TFIID species which either lack or contain TAFII30 (TFIID alpha and TFIID beta respectively).; . . unclassifiable (Anatomical System);cartilage;heart;hypothalamus;adrenal cortex;blood;skin;skeletal muscle;prostate;lung;frontal lobe;endometrium;thyroid;placenta;liver;testis;germinal center;kidney;brain;stomach;gall bladder; testis; 0.11780 0.09779 0.325313577 73.11276244 116.56762 2.34801 TAF12 0.892665247929895 0.106261675325802 0.00107307674430305 TATA-box binding protein associated factor 12 FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; subthalamic nucleus;testis - seminiferous tubule; 0.47256 0.10903 0.169169615 65.33380514 5.88883 0.22209 TAF13 0.0198501953204612 0.902318260271418 0.0778315444081202 TATA-box binding protein associated factor 13 FUNCTION: TFIID beta-specific TAFII.; . . . . 0.70143 0.14896 -0.053113545 49.38664779 2.97895 0.10814 TAF13P1 . . . TATA-box binding protein associated factor 13 pseudogene 1 . . . . . . . . . . . TAF13P2 . . . TATA-box binding protein associated factor 13 pseudogene 2 . . . . . . . . . . . TAF15 0.354285877502629 0.645713936043736 1.8645363478622e-07 TATA-box binding protein associated factor 15 FUNCTION: RNA and ssDNA-binding protein that may play specific roles during transcription initiation at distinct promoters. Can enter the preinitiation complex together with the RNA polymerase II (Pol II). {ECO:0000269|PubMed:19124016}.; DISEASE: Note=A chromosomal aberration involving TAF15/TAF2N is found in a form of extraskeletal myxoid chondrosarcomas (EMC). Translocation t(9;17)(q22;q11) with NR4A3. {ECO:0000269|PubMed:10602519}.; TISSUE SPECIFICITY: Ubiquitous. Observed in all fetal and adult tissues.; ovary;colon;skin;uterus;prostate;endometrium;larynx;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;blood;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;duodenum;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.42756 0.09590 -0.777005578 12.9747582 89.80727 2.03898 TAGAP 0.927102798290041 0.0728938397690524 3.36194090641153e-06 T-cell activation RhoGTPase activating protein FUNCTION: May function as a GTPase-activating protein and may play important roles during T-cell activation. {ECO:0000269|PubMed:15177553}.; . . unclassifiable (Anatomical System);lymph node;umbilical cord;urinary;colon;blood;bone marrow;pancreas;lung;endometrium;bone;visual apparatus;liver;spleen;germinal center;kidney; superior cervical ganglion;trigeminal ganglion;whole blood; 0.65100 0.13404 0.935129812 89.86199575 148.37259 2.65445 TAGLN 0.241537680178233 0.727361872857765 0.0311004469640027 transgelin FUNCTION: Actin cross-linking/gelling protein (By similarity). Involved in calcium interactions and contractile properties of the cell that may contribute to replicative senescence. {ECO:0000250}.; . . medulla oblongata;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;amniotic fluid;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;adipose tissue;smooth muscle;ovary;heart;atrioventricular node;uterus;prostate;uterus corpus;testis;appendix;ciliary ganglion;trigeminal ganglion; 0.62397 0.35787 -0.0274281 51.65723048 94.00915 2.08539 TAGLN2 0.00329073326368993 0.828050788739318 0.168658477996992 transgelin 2 . . TISSUE SPECIFICITY: Expressed in epididymis (at protein level). {ECO:0000269|PubMed:20736409}.; . . 0.27605 . -0.139478553 43.29440906 230.65146 3.28245 TAGLN2P1 . . . transgelin 2 pseudogene 1 . . . . . . . . . . . TAGLN2P2 . . . transgelin 2 pseudogene 2 . . . . . . . . . . . TAGLN3 0.685406597871256 0.310277802529892 0.00431559959885257 transgelin 3 . . TISSUE SPECIFICITY: Widely expressed in the brain. Expression is increased in the superior frontal cortex of alcoholics, but not in the motor cortex or cerebellum.; unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;hypothalamus;pineal body;fovea centralis;skin;retina;optic nerve;whole body;lung;frontal lobe;macula lutea;visual apparatus;brain;cerebellum; amygdala;dorsal root ganglion;whole brain;occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe;cerebellum; 0.23593 0.12971 -0.031067188 51.03798066 2.54021 0.09428 TAL1 0.824692214968038 0.171452101313844 0.00385568371811757 T-cell acute lymphocytic leukemia 1 FUNCTION: Implicated in the genesis of hemopoietic malignancies. It may play an important role in hemopoietic differentiation. Serves as a positive regulator of erythroid differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:1396592}.; DISEASE: Note=A chromosomal aberration involving TAL1 may be a cause of some T-cell acute lymphoblastic leukemias (T-ALL). Translocation t(1;14)(p32;q11) with T-cell receptor alpha chain (TCRA) genes. {ECO:0000269|PubMed:2303035}.; TISSUE SPECIFICITY: Leukemic stem cell.; unclassifiable (Anatomical System);heart;colon;blood;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;macula lutea;liver;spleen;mammary gland; superior cervical ganglion;fetal liver;ciliary ganglion;atrioventricular node;skeletal muscle;bone marrow; 0.77944 0.18580 . . 127.08931 2.45884 TAL2 0.488535069507167 0.433253993753419 0.0782109367394149 T-cell acute lymphocytic leukemia 2 . DISEASE: Note=A chromosomal aberration involving TAL2 may be a cause of some T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(7;9)(q34;q32) with TCRB. {ECO:0000269|PubMed:1763056}.; . lung;testis;germinal center; . 0.15132 0.11724 0.457594962 78.16112291 36.00569 1.08169 TALDO1 0.000175588436662531 0.888353116144127 0.111471295419211 transaldolase 1 FUNCTION: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.; DISEASE: Transaldolase deficiency (TALDOD) [MIM:606003]: An inborn error of the pentose phosphate pathway resulting in early-onset multisystem disease. Clinical features include growth retardation, dysmorphic features, cutis laxa, congenital heart disease, hepatosplenomegaly, telangiectases of the skin, pancytopenia, and bleeding tendency. {ECO:0000269|PubMed:11283793}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;islets of Langerhans;hypothalamus;muscle;pharynx;blood;breast;bile duct;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; whole blood;bone marrow; 0.33245 0.45921 -0.734731259 14.01863647 115.46203 2.33658 TALDO1P1 . . . transaldolase 1 pseudogene 1 . . . . . . . . . . . TAMM41 0.000184600184419332 0.894357403071958 0.105457996743623 TAM41 mitochondrial translocator assembly and maintenance homolog FUNCTION: Catalyzes the formation of CDP-diacylglycerol (CDP-DAG) from phosphatidic acid (PA) in the mitochondrial inner membrane. Required for the biosynthesis of the dimeric phospholipid cardiolipin, which stabilizes supercomplexes of the mitochondrial respiratory chain in the mitochondrial inner membrane (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;colon;skin;skeletal muscle;retina;bile duct;uterus;lung;frontal lobe;endometrium;nasopharynx;placenta;liver;testis;cervix;kidney;brain;bladder; superior cervical ganglion;trigeminal ganglion; 0.11443 . -0.069700724 48.54328851 1897.35826 8.01085 TANC1 0.140685896305883 0.859314101332731 2.36138515542615e-09 tetratricopeptide repeat, ankyrin repeat and coiled-coil containing 1 FUNCTION: May be a scaffold component in the postsynaptic density. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;cochlea;endometrium;larynx;thyroid;pituitary gland;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;hypothalamus;pharynx;skeletal muscle;bile duct;breast;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; . 0.22070 0.09998 -1.262475058 5.266572305 1280.16491 6.73695 TANC2 0.99999996584406 3.41559399607679e-08 1.15473773560116e-21 tetratricopeptide repeat, ankyrin repeat and coiled-coil containing 2 . . . . . 0.59007 0.11441 -2.783967663 0.666430762 191.80298 3.00320 TANGO2 4.22237843707503e-06 0.611706006054212 0.388289771567351 transport and golgi organization 2 homolog . . . . . 0.08091 0.09799 0.106667882 61.73036093 155.69121 2.72707 TANGO6 9.71153123642061e-09 0.978941821877576 0.0210581684108932 transport and golgi organization 6 homolog . . . . . 0.11763 0.07380 -0.014692675 52.35314933 466.30526 4.47345 TANK 0.943798417923446 0.0561591815396147 4.24005369396905e-05 TRAF family member associated NFKB activator FUNCTION: Adapter protein involved in I-kappa-B-kinase (IKK) regulation which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity. Acts as a regulator of TRAF function by maintaining them in a latent state. Blocks TRAF2 binding to LMP1 and inhibits LMP1-mediated NF-kappa-B activation. May control negatively TRAF2-mediated NF-kappa-B activation signaled by CD40, TNFR1 and TNFR2. {ECO:0000269|PubMed:12133833, ECO:0000269|PubMed:21931631}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;aorta;stomach;thymus; dorsal root ganglion;amygdala;superior cervical ganglion;ciliary ganglion;atrioventricular node;whole blood;trigeminal ganglion;skeletal muscle; 0.32380 0.18333 0.483275131 79.25218212 588.67126 4.91915 TAOK1 0.999999739283145 2.60716854569749e-07 8.06316077216619e-19 TAO kinase 1 FUNCTION: Serine/threonine-protein kinase involved in various processes such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation and subsequent activation of the upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled receptor signaling to p38/MAPK14. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of MAP2K3 and MAP2K6. Acts as a regulator of cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading to activate MARK2 kinase activity and subsequent phosphorylation and detachment of MAPT/TAU from microtubules. Also acts as a regulator of apoptosis: regulates apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation via activation of the MAPK8/JNK cascade. {ECO:0000269|PubMed:12665513, ECO:0000269|PubMed:13679851, ECO:0000269|PubMed:16407310, ECO:0000269|PubMed:17396146, ECO:0000269|PubMed:17900936}.; . TISSUE SPECIFICITY: Highly expressed in the testis, and to a lower extent also expressed in brain, placenta, colon and skeletal muscle. {ECO:0000269|PubMed:13679851, ECO:0000269|PubMed:9786855}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;bile duct;breast;lung;placenta;visual apparatus;liver;spleen;kidney; . 0.27710 0.14453 -0.624497208 17.16206653 54.59848 1.47904 TAOK2 0.998764492352461 0.00123550761783714 2.97014196416079e-11 TAO kinase 2 FUNCTION: Serine/threonine-protein kinase involved in different processes such as membrane blebbing and apoptotic bodies formation DNA damage response and MAPK14/p38 MAPK stress-activated MAPK cascade. Phosphorylates itself, MBP, activated MAPK8, MAP2K3, MAP2K6 and tubulins. Activates the MAPK14/p38 MAPK signaling pathway through the specific activation and phosphorylation of the upstream MAP2K3 and MAP2K6 kinases. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of upstream MAP2K3 and MAP2K6 kinases. Isoform 1, but not isoform 2, plays a role in apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation. This function, which requires the activation of MAPK8/JNK and nuclear localization of C-terminally truncated isoform 1, may be linked to the mitochondrial CASP9-associated death pathway. Isoform 1 binds to microtubules and affects their organization and stability independently of its kinase activity. Prevents MAP3K7-mediated activation of CHUK, and thus NF-kappa-B activation, but not that of MAPK8/JNK. May play a role in the osmotic stress-MAPK8 pathway. Isoform 2, but not isoform 1, is required for PCDH8 endocytosis. Following homophilic interactions between PCDH8 extracellular domains, isoform 2 phosphorylates and activates MAPK14/p38 MAPK which in turn phosphorylates isoform 2. This process leads to PCDH8 endocytosis and CDH2 cointernalization. Both isoforms are involved in MAPK14 phosphorylation. {ECO:0000269|PubMed:10660600, ECO:0000269|PubMed:11279118, ECO:0000269|PubMed:12639963, ECO:0000269|PubMed:12665513, ECO:0000269|PubMed:13679851, ECO:0000269|PubMed:16893890, ECO:0000269|PubMed:17158878, ECO:0000269|PubMed:17396146}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with a higher level of expression in testis and brain. {ECO:0000269|PubMed:10660600, ECO:0000269|PubMed:13679851}.; ovary;salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;nervous;muscle;urinary;adrenal cortex;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;duodenum;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;atrioventricular node;caudate nucleus;trigeminal ganglion;parietal lobe;skeletal muscle; 0.65431 0.18515 -2.851950648 0.601556971 117.65742 2.35831 TAOK3 0.999977597504952 2.24024950069114e-05 4.14688708350531e-14 TAO kinase 3 FUNCTION: Serine/threonine-protein kinase that acts as a regulator of the p38/MAPK14 stress-activated MAPK cascade and of the MAPK8/JNK cascade. Acts as an activator of the p38/MAPK14 stress- activated MAPK cascade. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of upstream MAP2K3 and MAP2K6 kinases. Inhibits basal activity of MAPK8/JNK cascade and diminishes its activation in response epidermal growth factor (EGF). {ECO:0000269|PubMed:10559204, ECO:0000269|PubMed:10924369, ECO:0000269|PubMed:17396146}.; . TISSUE SPECIFICITY: Ubiquitously expressed at a low level, and highly expressed in peripheral blood leukocytes (PBLs), thymus, spleen, kidney, skeletal muscle, heart and liver. {ECO:0000269|PubMed:10924369, ECO:0000269|PubMed:13679851}.; smooth muscle;colon;skin;bone marrow;retina;prostate;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;lung;nasopharynx;visual apparatus;liver;alveolus;cervix;stomach; medulla oblongata;subthalamic nucleus;ciliary ganglion;white blood cells;cingulate cortex; 0.39968 0.11204 -0.799052816 12.45576787 61.28385 1.59449 TAP1 0.286650163167608 0.713310957598253 3.88792341388635e-05 transporter 1, ATP-binding cassette, sub-family B (MDR/TAP) FUNCTION: Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association. Expression of TAP1 is down-regulated by human Epstein-Barr virus vIL-10 protein, thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules.; DISEASE: Bare lymphocyte syndrome 1 (BLS1) [MIM:604571]: A HLA class I deficiency. Contrary to bare lymphocyte syndromes type 2 and type 3, which are characterized by early-onset severe combined immunodeficiency, class I antigen deficiencies are not accompanied by particular pathologic manifestations during the first years of life. Systemic infections have not been described. Chronic bacterial infections, often beginning in the first decade of life, are restricted to the respiratory tract. {ECO:0000269|PubMed:10074494}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;adrenal cortex;blood;lens;skeletal muscle;breast;greater omentum;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;kidney;mammary gland;stomach; . 0.06099 . 2.134974852 97.94762916 4675.51312 13.77511 TAP2 0.00171341819174486 0.997151802826615 0.00113477898164001 transporter 2, ATP-binding cassette, sub-family B (MDR/TAP) FUNCTION: Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association.; DISEASE: Bare lymphocyte syndrome 1 (BLS1) [MIM:604571]: A HLA class I deficiency. Contrary to bare lymphocyte syndromes type 2 and type 3, which are characterized by early-onset severe combined immunodeficiency, class I antigen deficiencies are not accompanied by particular pathologic manifestations during the first years of life. Systemic infections have not been described. Chronic bacterial infections, often beginning in the first decade of life, are restricted to the respiratory tract. {ECO:0000269|PubMed:7517574}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.15025 0.48720 1.534092314 95.56499174 2889.23349 10.18092 TAPBP 0.000393581688587975 0.957605434969596 0.0420009833418159 TAP binding protein (tapasin) FUNCTION: Involved in the association of MHC class I with transporter associated with antigen processing (TAP) and in the assembly of MHC class I with peptide (peptide loading). {ECO:0000269|PubMed:10636848}.; . TISSUE SPECIFICITY: Neutrophils, mostly in fully differentiated cells.; . . 0.06907 . 0.132352165 63.48785091 104.57314 2.21028 TAPBPL 3.2851378423028e-07 0.540336658298274 0.459663013187941 TAP binding protein like FUNCTION: Component of the antigen processing and presentation pathway, which binds to MHC class I coupled with beta2- microglobulin/B2M. Association between TAPBPR and MHC class I occurs in the absence of a functional peptide-loading complex (PLC). Expression seems to slow down and down-regulate MHC class I surface expression. {ECO:0000269|PubMed:23401559}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;lens;skeletal muscle;bile duct;breast;lung;epididymis;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; thyroid;liver;white blood cells;trigeminal ganglion; 0.04805 0.08404 0.977404764 90.3868837 2460.03856 9.23224 TAPT1 0.563962464646747 0.435503598744728 0.000533936608525264 transmembrane anterior posterior transformation 1 FUNCTION: May act as a downstream effector of HOXC8 possibly by transducing or transmitting extracellular information required for axial skeletal patterning during development (By similarity). In case of infection, may act as a fusion receptor for cytomegalovirus (HCMV) strain AD169. {ECO:0000250}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;testis;germinal center;artery;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lung;placenta;macula lutea;liver;spleen;kidney;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.27103 0.10218 0.306902668 72.38145789 242.40269 3.36022 TAPT1-AS1 . . . TAPT1 antisense RNA 1 (head to head) . . . . . . . . . . . TAPVR1 . . . total anomalous pulmonary venous return 1 . . . . . . . . . . . TARBP1 5.69518410914162e-16 0.916360372465619 0.0836396275343801 TAR (HIV-1) RNA binding protein 1 FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase which methylates RNA molecules such as tRNAs. In case of infection by HIV-1, it binds to the loop region of TAR RNA, a region also bound by RNA polymerase II. Binding of TARBP1 and RNA polymerase II to HIV-1 TAR RNA is mutually exclusive, suggesting that TARBP1 may function alone or in conjunction with HIV-1 Tat to disengage RNA polymerase II from HIV-1 TAR RNA. May act by methylating HIV-1 TAR RNA. {ECO:0000269|PubMed:7638159, ECO:0000269|PubMed:8626763, ECO:0000269|PubMed:8846792}.; . . ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;whole body;oesophagus;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;urinary;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;cerebellum; superior cervical ganglion;subthalamic nucleus;occipital lobe;cingulate cortex;skeletal muscle; 0.11162 0.10683 -0.231522913 36.36470866 3226.63895 10.81541 TARBP2 0.446803723604583 0.551868241397175 0.0013280349982423 TAR (HIV-1) RNA binding protein 2 FUNCTION: Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. May also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by DICER1. Binds to the HIV-1 TAR RNA which is located in the long terminal repeat (LTR) of HIV-1, and stimulates translation of TAR-containing RNAs. This is achieved in part at least by binding to and inhibiting EIF2AK2/PKR, thereby reducing phosphorylation and inhibition of EIF2S1/eIF-2-alpha. May also promote translation of TAR-containing RNAs independently of EIF2AK2/PKR. {ECO:0000269|PubMed:12475984, ECO:0000269|PubMed:15973356, ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387, ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:18178619, ECO:0000269|PubMed:19219043}.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;synovium;thyroid;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.19765 0.14709 -0.337894035 30.37272942 17.77972 0.62129 TARBP2P . . . TAR (HIV-1) RNA binding protein 2 pseudogene . . . . . . . . . . . TARDBP 0.980707836590808 0.0192775000805828 1.46633286096854e-05 TAR DNA binding protein FUNCTION: DNA and RNA-binding protein which regulates transcription and splicing. Involved in the regulation of CFTR splicing. It promotes CFTR exon 9 skipping by binding to the UG repeated motifs in the polymorphic region near the 3'-splice site of this exon. The resulting aberrant splicing is associated with pathological features typical of cystic fibrosis. May also be involved in microRNA biogenesis, apoptosis and cell division. Can repress HIV-1 transcription by binding to the HIV-1 long terminal repeat. Stabilizes the low molecular weight neurofilament (NFL) mRNA through a direct interaction with the 3' UTR. {ECO:0000269|PubMed:11285240, ECO:0000269|PubMed:17481916}.; DISEASE: Amyotrophic lateral sclerosis 10 (ALS10) [MIM:612069]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. {ECO:0000269|PubMed:18288693, ECO:0000269|PubMed:18309045, ECO:0000269|PubMed:18372902, ECO:0000269|PubMed:18396105, ECO:0000269|PubMed:18438952, ECO:0000269|PubMed:19224587, ECO:0000269|PubMed:19695877, ECO:0000269|PubMed:21220647, ECO:0000269|PubMed:21418058, ECO:0000269|PubMed:22456481}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. In particular, expression is high in pancreas, placenta, lung, genital tract and spleen.; medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;hypothalamus;pancreas;lung;cornea;mesenchyma;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;thymus; testis;skeletal muscle;cingulate cortex;parietal lobe; 0.19384 0.25407 -0.383807564 27.41802312 2.30437 0.07842 TARDBPP1 . . . TAR DNA binding protein pseudogene 1 . . . . . . . . . . . TARDBPP2 . . . TAR DNA binding protein pseudogene 2 . . . . . . . . . . . TARID . . . TCF21 antisense RNA inducing promoter demethylation . . . . . . . . . . . TARM1 . . . T cell-interacting, activating receptor on myeloid cells 1 . . . . . . . 0.747842143 86.47676339 425.04642 4.30747 TARS 1.18541739422624e-09 0.982191836359248 0.017808162455335 threonyl-tRNA synthetase . . . lymphoreticular;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;cerebral cortex;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hypopharynx;liver;cervix;head and neck;kidney;mammary gland;stomach; tumor; 0.83798 0.14433 0.602602982 82.87331918 593.86357 4.93711 TARS2 1.87455824083767e-08 0.991549738923239 0.00845024233117879 threonyl-tRNA synthetase 2, mitochondrial (putative) . DISEASE: Combined oxidative phosphorylation deficiency 21 (COXPD21) [MIM:615918]: A mitochondrial disorder characterized by a lethal encephalomyopathy. Shortly after birth, affected individuals manifest axial hypotonia, limb hypertonia, psychomotor delay, and increased serum lactate. Additional features include subsarcolemmal lipofuscin-positive deposits in muscle, cerebral spongiosis, and hepatic steatosis. {ECO:0000269|PubMed:24827421}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.16125 0.08406 -0.26629572 34.81953291 99.77133 2.16435 TARS2P1 . . . threonyl-tRNA synthetase 2, mitochondrial pseudogene . . . . . . . . . . . TARSL2 2.85774106307975e-09 0.9755305284327 0.0244694687095593 threonyl-tRNA synthetase-like 2 . . . ovary;parathyroid;fovea centralis;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;pancreas;lung;nasopharynx;placenta;macula lutea;liver;head and neck;cervix;kidney; medulla oblongata;superior cervical ganglion;subthalamic nucleus;occipital lobe;prefrontal cortex;pons;trigeminal ganglion;parietal lobe; 0.14240 0.12785 -1.530301957 3.367539514 3616.35122 11.64868 TAS1R1 7.9136002871651e-09 0.269820278654793 0.730179713431606 taste 1 receptor member 1 FUNCTION: Putative taste receptor. TAS1R1/TAS1R3 responds to the umami taste stimulus (the taste of monosodium glutamate). Sequence differences within and between species can significantly influence the selectivity and specificity of taste responses. {ECO:0000269|PubMed:11917125}.; . . unclassifiable (Anatomical System);ovary;parathyroid;skeletal muscle;uterus;lung;bone;placenta;visual apparatus;testis;spleen;cervix;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin; 0.10745 0.10520 3.521104333 99.46921444 800.41532 5.57566 TAS1R2 6.17507053671979e-13 0.0159377846100055 0.984062215389377 taste 1 receptor member 2 FUNCTION: Putative taste receptor. TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners.; . . . . 0.13800 0.11727 1.036106017 91.12998349 922.96578 5.90016 TAS1R3 . . . taste 1 receptor member 3 FUNCTION: Putative taste receptor. TAS1R1/TAS1R3 responds to the umami taste stimulus (the taste of monosodium glutamate). TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners. TAS1R3 is essential for the recognition and response to the disaccharide trehalose (By similarity). Sequence differences within and between species can significantly influence the selectivity and specificity of taste responses. {ECO:0000250, ECO:0000269|PubMed:11917125, ECO:0000269|PubMed:12892531}.; . . lens; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;occipital lobe;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.16663 . -1.999300124 1.739797122 445.60495 4.39394 TAS2R1 0.241581130135791 0.644129363857819 0.114289506006391 taste 2 receptor member 1 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin- positive cells.; . . 0.01227 . 0.084621747 60.31493277 361.37771 4.02359 TAS2R2P . . . taste 2 receptor member 2 pseudogene . . . . . . . . . . . TAS2R3 0.000144123847766213 0.242656940126061 0.757198936026173 taste 2 receptor member 3 FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. {ECO:0000269|PubMed:10761934, ECO:0000269|PubMed:10761935}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin- positive cells. Expressed in the antrum and fundus (part of the stomach), duodenum and in gastric endocrine cells. {ECO:0000269|PubMed:10761934}.; unclassifiable (Anatomical System); subthalamic nucleus;uterus corpus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05621 0.07756 0.17280645 65.75843359 30.58676 0.97310 TAS2R4 0.0497384495024723 0.68781959047337 0.262441960024158 taste 2 receptor member 4 FUNCTION: Gustducin-coupled receptor for denatonium and N(6)- propyl-2-thiouracil implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. In airway epithelial cells, binding of denatonium increases the intracellular calcium ion concentration and stimulates ciliary beat frequency. {ECO:0000269|PubMed:19628819}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin- positive cells. Expressed on airway ciliated epithelium. {ECO:0000269|PubMed:19628819}.; . . 0.05976 0.07470 1.418384579 94.89266336 802.33751 5.58127 TAS2R5 0.000103902616890766 0.359856846316097 0.640039251067012 taste 2 receptor member 5 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin- positive cells.; unclassifiable (Anatomical System);ovary; . 0.14127 . 1.15197334 92.52182118 728.98545 5.35983 TAS2R6P . . . taste 2 receptor member 6 pseudogene . . . . . . . . . . . TAS2R7 0.0230774509333994 0.767815280703849 0.209107268362751 taste 2 receptor member 7 FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin- positive cells.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;appendix;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.05301 0.08421 1.196071381 92.92285916 365.51067 4.04608 TAS2R8 0.0124682631133943 0.650084754459395 0.337446982427211 taste 2 receptor member 8 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin- positive cells.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.02266 0.06851 1.727105015 96.51450814 150.09355 2.67208 TAS2R9 0.000278743191968872 0.338584226307387 0.661137030500644 taste 2 receptor member 9 FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin- positive cells.; unclassifiable (Anatomical System); superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.01596 0.06770 1.129924507 92.23283793 131.84502 2.50050 TAS2R10 0.428565950557266 0.538931290951391 0.032502758491342 taste 2 receptor member 10 FUNCTION: Gustducin-coupled strychnine receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium- regulated cation channel TRPM5. {ECO:0000269|PubMed:15759003}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin- positive cells.; unclassifiable (Anatomical System); dorsal root ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.08382 0.08284 -0.159704656 41.90846898 105.34968 2.22249 TAS2R12P . . . taste 2 receptor member 12 pseudogene . . . . . . . . . . . TAS2R13 0.579968726680784 0.409263741674832 0.010767531644384 taste 2 receptor member 13 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin- positive cells.; . . 0.01100 0.04427 -0.0274281 51.65723048 24.54423 0.80712 TAS2R14 0.00105542818770112 0.601959161135516 0.396985410676783 taste 2 receptor member 14 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin- positive cells. Expressed in testis (PubMed:16720576). {ECO:0000269|PubMed:16720576}.; . . 0.01791 0.05915 0.685332364 85.09672092 41.22732 1.20564 TAS2R15P . . . taste 2 receptor member 15 pseudogene . . . . . 0.02255 . . . . . TAS2R16 0.0149965302399621 0.687907097819054 0.297096371940984 taste 2 receptor member 16 FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. {ECO:0000269|PubMed:12379855, ECO:0000269|PubMed:15759003}.; . TISSUE SPECIFICITY: Expressed in a subset of gustducin-positive taste receptor cells of the tongue. Expressed in circumvallate papillae and testis (PubMed:16720576). {ECO:0000269|PubMed:16720576}.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.02225 0.06310 -0.049474214 50.01179523 21.74383 0.73183 TAS2R18P . . . taste 2 receptor member 18 pseudogene . . . . . . . . . . . TAS2R19 0.00414619841164368 0.656298562410244 0.339555239178113 taste 2 receptor member 19 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and exclusively in gustducin-positive cells.; . . 0.00966 . 0.995816767 90.62278839 708.17976 5.28571 TAS2R20 0.00447601535837195 0.67258772946047 0.322936255181158 taste 2 receptor member 20 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and exclusively in gustducin-positive cells.; . . 0.02255 . 2.019241996 97.71172446 861.49285 5.72491 TAS2R22 . . . taste 2 receptor member 22 . . . . . . . . . . . TAS2R30 0.00170314797923996 0.466871471984056 0.531425380036704 taste 2 receptor member 30 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and exclusively in gustducin-positive cells.; . . . . 0.395088462 76.15003539 26.27524 0.85173 TAS2R31 2.54372259099135e-05 0.174294482670715 0.825680080103375 taste 2 receptor member 31 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). Activated by the sulfonyl amide sweeteners saccharin and acesulfame K. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and exclusively in gustducin-positive cells.; . . . . 2.195683333 98.11276244 1586.0821 7.36714 TAS2R33 . . . taste 2 receptor member 33 . . . . . . . . . . . TAS2R36 . . . taste 2 receptor member 36 . . . . . . . . . . . TAS2R37 . . . taste 2 receptor member 37 . . . . . . . . . . . TAS2R38 0.065390402368431 0.729870733606533 0.204738864025036 taste 2 receptor member 38 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and exclusively in gustducin-positive cells. Expressed in testis (PubMed:16720576). {ECO:0000269|PubMed:16720576}.; . . 0.13240 0.10729 1.196071381 92.92285916 1623.12511 7.45029 TAS2R39 5.30383482902454e-08 0.0349496639625475 0.965050282999104 taste 2 receptor member 39 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and exclusively in gustducin-positive cells.; . . . . 1.260404852 93.53031375 67.94381 1.70455 TAS2R40 0.00249983201307608 0.546994833328563 0.450505334658361 taste 2 receptor member 40 FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and exclusively in gustducin-positive cells.; . . . . 0.459411326 78.28497287 575.47408 4.86572 TAS2R41 4.93429098643450e-09 0.0320464133815022 0.967953581684207 taste 2 receptor member 41 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and exclusively in gustducin-positive cells.; . . . . 0.306902668 72.38145789 1395.26359 6.98815 TAS2R42 0.0025809974952036 0.553853689162578 0.443565313342218 taste 2 receptor member 42 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). {ECO:0000250}.; . . . . . . 1.06196211 91.507431 2903.74491 10.21811 TAS2R43 0.00210427361078187 0.51043715576669 0.487458570622528 taste 2 receptor member 43 FUNCTION: Gustducin-coupled receptor immplicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. Activated by the sulfonyl amide sweeteners saccharin and acesulfame K. In airway epithelial cells, binding of bitter compounds increases the intracellular calcium ion concentration and stimulates ciliary beat frequency. May act as chemosensory receptors in airway epithelial cells to detect and eliminate potential noxious agents from the airways (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and exclusively in gustducin-positive cells. Expressed in airway epithelia. {ECO:0000269|PubMed:19628819}.; . . . . 2.638661101 98.80868129 225.18401 3.24479 TAS2R45 . . . taste 2 receptor member 45 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and exclusively in gustducin-positive cells.; . . . . . . . . TAS2R46 3.10044300046628e-08 0.0255696592839735 0.974430309711596 taste 2 receptor member 46 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). In airway epithelial cells, binding of bitter compounds increases the intracellular calcium ion concentration and stimulates ciliary beat frequency (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and exclusively in gustducin-positive cells. Expressed on ciliated airway epithelium. {ECO:0000269|PubMed:19628819}.; . . . . 0.262810045 70.43524416 648.60426 5.11007 TAS2R50 1.89175446267053e-07 0.0383254684627802 0.961674342361774 taste 2 receptor member 50 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and exclusively in gustducin-positive cells.; . . 0.02037 0.06629 0.17280645 65.75843359 2041.32036 8.32687 TAS2R60 6.30040071512039e-06 0.149347097803602 0.850646601795683 taste 2 receptor member 60 FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and exclusively in gustducin-positive cells.; . . 0.02965 . 0.194852702 67.03231894 305.63901 3.72299 TAS2R62P . . . taste 2 receptor member 62 pseudogene . . . . . . . . . . . TAS2R63P . . . taste 2 receptor member 63 pseudogene . . . . . . . . . . . TAS2R64P . . . taste 2 receptor member 64 pseudogene . . . . . . . . . . . TAS2R67P . . . taste 2 receptor member 67 pseudogene . . . . . . . . . . . TAS2R68P . . . taste 2 receptor member 68 pseudogene . . . . . . . . . . . TASP1 0.956178727459365 0.0438166721033008 4.60043733455677e-06 taspase 1 FUNCTION: Protease involved in KMT2A/MLL1 processing and, consequently, in the correct expression of the early HOXA gene cluster. {ECO:0000269|PubMed:14636557}.; . . unclassifiable (Anatomical System);medulla oblongata;cartilage;ovary;islets of Langerhans;sympathetic chain;parathyroid;blood;breast;pancreas;whole body;lung;larynx;nasopharynx;bone;placenta;pituitary gland;liver;cervix;head and neck;spleen;germinal center;kidney;brain;bladder;stomach;thymus; superior cervical ganglion; 0.21262 0.24094 -0.183570861 39.95046001 20.21014 0.69154 TAT 0.0214384440123944 0.975114738186389 0.00344681780121647 tyrosine aminotransferase FUNCTION: Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity towards phenylalanine. {ECO:0000269|PubMed:16640556, ECO:0000269|PubMed:7999802}.; DISEASE: Tyrosinemia 2 (TYRSN2) [MIM:276600]: An inborn error of metabolism characterized by elevations of tyrosine in the blood and urine, and oculocutaneous manifestations. Typical features include palmoplantar keratosis, painful corneal ulcers, and mental retardation. {ECO:0000269|PubMed:1357662}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);breast;lung;liver;testis;mammary gland;skeletal muscle; dorsal root ganglion;superior cervical ganglion;testis - interstitial;liver;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.37643 0.70880 -0.558357437 19.54470394 674.69759 5.18783 TAT-AS1 . . . TAT antisense RNA 1 . . . . . . . . . . . TATDN1 1.72640600686597e-08 0.227011674131751 0.772988308604189 TatD DNase domain containing 1 FUNCTION: Putative deoxyribonuclease. {ECO:0000250}.; . . colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;synovium;pituitary gland;testis;bladder;pineal gland;brain;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;blood;lens;lung;nasopharynx;macula lutea;visual apparatus;liver;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;parietal lobe; 0.29108 0.12440 0.21689899 68.12927577 77.60897 1.85474 TATDN1P1 . . . TatD DNase domain containing 1 pseudogene 1 . . . . . . . . . . . TATDN2 0.000742651150073241 0.981341743550022 0.0179156052999048 TatD DNase domain containing 2 FUNCTION: Putative deoxyribonuclease. {ECO:0000250}.; . . lymphoreticular;myocardium;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;amnion;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex;cerebellum; 0.14940 . 0.668743049 84.68388771 2043.58208 8.33291 TATDN2P1 . . . TatD DNase domain containing 2 pseudogene 1 . . . . . . . . . . . TATDN2P2 . . . TatD DNase domain containing 2 pseudogene 2 . . . . . . . . . . . TATDN2P3 . . . TatD DNase domain containing 2 pseudogene 3 . . . . . . . . . . . TATDN3 4.62050476662264e-05 0.858736483871501 0.141217311080833 TatD DNase domain containing 3 FUNCTION: Putative deoxyribonuclease.; . . . . 0.06737 . 1.150157577 92.46874263 149.21929 2.66305 TAX1BP1 2.99233082871036e-06 0.996493722101997 0.00350328556717393 Tax1 (human T-cell leukemia virus type I) binding protein 1 FUNCTION: Inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. Degraded by caspase-3-like family proteins upon TNF-induced apoptosis. May also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. {ECO:0000269|PubMed:10435631, ECO:0000269|PubMed:10920205}.; . TISSUE SPECIFICITY: Expressed in all tissues tested.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;brain;amygdala;heart;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum;thymus; amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;testis - interstitial;pons;testis - seminiferous tubule;thyroid;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.48411 0.15403 -0.156065314 42.16206653 428.0023 4.32066 TAX1BP3 0.00234803255540852 0.533610296968246 0.464041670476345 Tax1 binding protein 3 FUNCTION: May regulate a number of protein-protein interactions by competing for PDZ domain binding sites. Binds CTNNB1 and may thereby act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play a role in the Rho signaling pathway. May play a role in activation of CDC42 by the viral protein HPV16 E6. {ECO:0000269|PubMed:10940294, ECO:0000269|PubMed:16855024, ECO:0000269|PubMed:21139582}.; . TISSUE SPECIFICITY: Ubiquitous. Detected in brain, heart, kidney, lung, small intestine and skeletal muscle. Detected in various cell lines including HeLa. Weakly expressed in peripheral blood leukocytes. {ECO:0000269|PubMed:10940294, ECO:0000269|PubMed:16855024, ECO:0000269|PubMed:25645515}.; medulla oblongata;ovary;salivary gland;colon;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;tongue;islets of Langerhans;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;olfactory bulb;lung;heart;adrenal gland;placenta; 0.13141 0.11262 0.03689118 56.64071715 32.95407 1.02059 TAZ 0.966526482271322 0.0334163363322911 5.71813963868379e-05 tafazzin FUNCTION: Some isoforms may be involved in cardiolipin (CL) metabolism. {ECO:0000269|PubMed:12930833, ECO:0000269|PubMed:19164547}.; DISEASE: Barth syndrome (BTHS) [MIM:302060]: An X-linked disease characterized by dilated cardiomyopathy with endocardial fibroelastosis, a predominantly proximal skeletal myopathy, growth retardation, neutropenia, and organic aciduria, particularly excess of 3-methylglutaconic acid. Additional features include hypertrophic cardiomyopathy, isolated left ventricular non- compaction, ventricular arrhythmia, motor delay, poor appetite, fatigue and exercise intolerance, hypoglycemia, lactic acidosis, hyperammonemia, and dramatic late catch-up growth after growth delay throughout childhood. {ECO:0000269|PubMed:11238270, ECO:0000269|PubMed:12032589, ECO:0000269|PubMed:9382096, ECO:0000269|PubMed:9382097}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: High levels in cardiac and skeletal muscle. Up to 10 isoforms can be present in different amounts in different tissues. Most isoforms are ubiquitous. Isoforms that lack the N- terminus are found in leukocytes and fibroblasts, but not in heart and skeletal muscle. Some forms appear restricted to cardiac and skeletal muscle or to leukocytes.; lymphoreticular;smooth muscle;ovary;sympathetic chain;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;muscle;skeletal muscle;pancreas;lung;placenta;hippocampus;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.29008 0.19268 0.080983847 59.76055674 12.59242 0.45960 TBATA 1.68599393619126e-07 0.233454684726133 0.766545146674473 thymus, brain and testes associated FUNCTION: May play a role in spermatid differentiation. Modulates thymic stromal cell proliferation and thymus function. {ECO:0000250}.; . . . . 0.05259 0.09025 0.356452144 74.62845011 79.42477 1.88342 TBC1D1 3.93946057987096e-08 0.999878400445414 0.000121560159980531 TBC1 domain family member 1 FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). May play a role in the cell cycle and differentiation of various tissues. Involved in the trafficking and translocation of GLUT4-containing vesicles and insulin-stimulated glucose uptake into cells (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;muscle;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;visual apparatus;amnion;alveolus;liver;head and neck;spleen;kidney;mammary gland;aorta;stomach;cerebellum; uterus;testis - interstitial;placenta;thyroid;testis;kidney;skeletal muscle; 0.16285 0.20642 0.009173042 54.15782024 2012.94334 8.26090 TBC1D2 2.30690551887448e-08 0.884129436276545 0.1158705406544 TBC1 domain family member 2 FUNCTION: Acts as GTPase-activating protein for RAB7A. Signal effector acting as a linker between RAC1 and RAB7A, leading to RAB7A inactivation and subsequent inhibition of cadherin degradation and reduced cell-cell adhesion. {ECO:0000269|PubMed:20116244}.; . TISSUE SPECIFICITY: Expressed in a broad range of tissues, especially in kidney, liver, lung and placenta. Also expressed in keratinocytes and epithelia-containing organs. Isoform 2 is differentially expressed in prostate normal and cancer cells (at protein level). {ECO:0000269|PubMed:11785977, ECO:0000269|PubMed:20116244}.; unclassifiable (Anatomical System);lymphoreticular;colon;skeletal muscle;uterus;prostate;pancreas;optic nerve;lung;endometrium;larynx;bone;placenta;alveolus;hypopharynx;liver;testis;head and neck;spleen;kidney;brain;bladder;stomach; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.08631 0.10194 0.233278626 68.58339231 2646.0935 9.65193 TBC1D2B 6.50996889622544e-05 0.994877080364906 0.0050578199461318 TBC1 domain family member 2B FUNCTION: May act as a GTPase-activating protein. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.17736 0.11001 0.068033485 59.0351498 1987.47287 8.21355 TBC1D3 0.455180214877127 0.44991569322599 0.094904091896883 TBC1 domain family member 3 FUNCTION: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11. {ECO:0000269|PubMed:12359748}.; . TISSUE SPECIFICITY: Expressed in liver, skeletal muscle, kidney, pancreas, spleen, testis, ovary, small intestine and peripheral blood leukocytes. Overexpressed in prostate cancers. {ECO:0000269|PubMed:12359748, ECO:0000269|PubMed:12604796}.; medulla oblongata;ovary;adrenal medulla;colon;parathyroid;skin;uterus;prostate;endometrium;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;amnion;head and neck;kidney;stomach; . . . . . 0.78386 0.01468 TBC1D3B 0.636923622994015 0.334597459085307 0.0284789179206779 TBC1 domain family member 3B FUNCTION: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;lymph node;colon;blood;retina;bone marrow;uterus;breast;prostate;lung;placenta;liver;testis;brain; . . . . . 168.80885 2.83577 TBC1D3C 0.425665089216628 0.462549442331744 0.111785468451628 TBC1 domain family member 3C FUNCTION: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in pancreas, thymus and testis. {ECO:0000269|PubMed:16863688}.; medulla oblongata;ovary;adrenal medulla;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;amnion;head and neck;kidney;stomach; . 0.07680 . . . 83.26512 1.93963 TBC1D3D . . . TBC1 domain family member 3D FUNCTION: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity). {ECO:0000250|UniProtKB:Q8IZP1}.; . TISSUE SPECIFICITY: Expressed in pancreas, thymus and testis. {ECO:0000269|PubMed:16863688}.; . . . . . . . . TBC1D3E . . . TBC1 domain family member 3E FUNCTION: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity). {ECO:0000250|UniProtKB:Q8IZP1}.; . TISSUE SPECIFICITY: Expressed in pancreas, thymus and testis. {ECO:0000269|PubMed:16863688}.; . . . . . . . . TBC1D3F 0.620380556789716 0.34724615943573 0.0323732837745535 TBC1 domain family member 3F FUNCTION: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in most tissues including pancreas, thymus and testis. {ECO:0000269|PubMed:16863688}.; medulla oblongata;ovary;adrenal medulla;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;amnion;head and neck;kidney;stomach; . . . . . 6.74404 0.24858 TBC1D3G 0.490002147026831 0.432467024674454 0.0775308282987149 TBC1 domain family member 3G FUNCTION: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;adrenal medulla;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;amnion;head and neck;kidney;stomach; . . . . . 3.16493 0.11407 TBC1D3H . . . TBC1 domain family member 3H FUNCTION: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in heart. {ECO:0000269|PubMed:16863688}.; . . . . . . . . TBC1D3I . . . TBC1 domain family member 3I FUNCTION: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity). {ECO:0000250|UniProtKB:Q8IZP1}.; . . . . . . . . . . TBC1D3J . . . TBC1 domain family member 3J . . . . . . . . . . . TBC1D3K . . . TBC1 domain family member 3K FUNCTION: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity). {ECO:0000250|UniProtKB:Q8IZP1}.; . . . . . . . . . . TBC1D3L . . . TBC1 domain family member 3L FUNCTION: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity). {ECO:0000250|UniProtKB:Q8IZP1}.; . . . . . . . . . . TBC1D3P1 . . . TBC1 domain family member 3 pseudogene 1 . . . . . . . . . . . TBC1D3P1-DHX40P1 . . . TBC1D3P1-DHX40P1 readthrough, transcribed pseudogene . . . . . . . . . . . TBC1D3P2 . . . TBC1 domain family member 3 pseudogene 2 . . . . . . . . . . . TBC1D3P3 . . . TBC1 domain family member 3 pseudogene 3 . . . medulla oblongata;ovary;adrenal medulla;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;amnion;head and neck;kidney;stomach; . . . . . . . TBC1D3P4 . . . TBC1 domain family member 3 pseudogene 4 . . . unclassifiable (Anatomical System);medulla oblongata;lymph node;cartilage;ovary;islets of Langerhans;adrenal medulla;colon;parathyroid;blood;skeletal muscle;bone marrow;uterus;pancreas;prostate;lung;placenta;amnion;liver;testis;germinal center;kidney;brain;pineal gland;stomach; . . . . . . . TBC1D3P5 . . . TBC1 domain family member 3 pseudogene 5 . . . . . . . . . . . TBC1D3P6 . . . TBC1 domain family member 3 pseudogene 6 . . . . . . . . . . . TBC1D3P7 . . . TBC1 domain family member 3 pseudogene 7 . . . . . . . . . . . TBC1D4 3.64406926442853e-13 0.973290417822076 0.0267095821775595 TBC1 domain family member 4 FUNCTION: May act as a GTPase-activating protein for RAB2A, RAB8A, RAB10 and RAB14. Isoform 2 promotes insulin-induced glucose transporter SLC2A4/GLUT4 translocation at the plasma membrane, thus increasing glucose uptake. {ECO:0000269|PubMed:15971998, ECO:0000269|PubMed:18771725, ECO:0000269|PubMed:22908308}.; DISEASE: Diabetes mellitus, non-insulin-dependent, 5 (NIDDM5) [MIM:616087]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:25043022}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Isoform 2 is the highest overexpressed in most tissues. Isoform 1 is highly expressed in skeletal muscle and heart, but was not detectable in the liver nor in adipose tissue. Isoform 2 is strongly expressed in adrenal and thyroid gland, and also in lung, kidney, colon, brain and adipose tissue. Isoform 2 is moderately expressed in skeletal muscle. Expressed in pancreatic Langerhans islets, including beta cells (at protein level). Expression is decreased by twofold in pancreatic islets in type 2 diabetes patients compared to control subjects. Up-regulated in T-cells from patients with atopic dermatitis. {ECO:0000269|PubMed:15304337, ECO:0000269|PubMed:18276765, ECO:0000269|PubMed:18771725}.; . . 0.22277 0.10606 1.032445072 91.12408587 1981.92717 8.20473 TBC1D5 6.51864399070986e-10 0.960226170481641 0.039773828866495 TBC1 domain family member 5 FUNCTION: May act as a GTPase-activating protein (GAP) for Rab family protein(s). May act as a GAP for RAB7A. Can displace RAB7A and retromer CSC subcomplex from the endosomal membrane to the cytosol; at least retromer displacement seems to require its catalytic activity (PubMed:19531583, PubMed:20923837). Required for retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN); the function seems to require its catalytic activity. Involved in regulation of autophagy (PubMed:22354992). May act as a molecular switch between endosomal and autophagosomal transport and is involved in reprogramming vesicle trafficking upon autophagy induction. Involved in the trafficking of ATG9A upon activation of autophagy. May regulate the recruitment of ATG9A-AP2-containing vesicles to autophagic membranes (PubMed:24603492). {ECO:0000269|PubMed:19531583, ECO:0000269|PubMed:20923837, ECO:0000269|PubMed:22354992, ECO:0000269|PubMed:24603492, ECO:0000305|PubMed:19531583, ECO:0000305|PubMed:22354992, ECO:0000305|PubMed:24603492}.; . . ovary;colon;skin;uterus;prostate;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;spinal cord;muscle;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;spinal cord;prefrontal cortex;atrioventricular node;pons;trigeminal ganglion; 0.28341 0.10050 0.090079492 60.64519934 185.71366 2.95909 TBC1D7 8.3011606302466e-06 0.517119081090848 0.482872617748522 TBC1 domain family member 7 FUNCTION: Component of the TSC-TBC complex, that contains TBC1D7 in addition to the TSC1-TSC2 complex and consists of the functional complex possessing GTPase-activating protein (GAP) activity toward RHEB in response to alterations in specific cellular growth conditions. The small GTPase RHEB is a direct activator of the protein kinase activity of mTORC1 and the TSC-TBC complex acts as a negative regulator of mTORC1 signaling cascade by acting as a GAP for RHEB. Participates in the proper sensing of growth factors and glucose, but not amino acids, by mTORC1. It is unclear whether TBC1D7 acts as a GTPase-activating protein and additional studies are required to answer this question. {ECO:0000269|PubMed:22795129}.; . TISSUE SPECIFICITY: Highly expressed in heart, and slightly in kidney, liver and placenta. {ECO:0000269|PubMed:17658474}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;thyroid;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;pharynx;blood;lens;breast;lung;placenta;hippocampus;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; . 0.13027 . -0.159704656 41.90846898 267.37035 3.50659 TBC1D8 5.26132710714781e-07 0.999927627026718 7.18468405708866e-05 TBC1 domain family member 8 FUNCTION: May act as a GTPase-activating protein for Rab family protein(s).; . . . . 0.16485 0.13045 -1.006844617 8.209483369 2278.58196 8.83254 TBC1D8B 1.87465336440428e-05 0.9987323475943 0.00124890587205572 TBC1 domain family member 8B FUNCTION: May act as a GTPase-activating protein for Rab family protein(s).; . . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;adrenal cortex;colon;blood;parathyroid;skin;uterus;breast;prostate;pancreas;lung;placenta;pituitary gland;liver;testis;spleen;germinal center; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22965 . -1.148192153 6.316348195 72.04097 1.76713 TBC1D9 0.876941194844605 0.123058783297829 2.18575664068236e-08 TBC1 domain family member 9 FUNCTION: May act as a GTPase-activating protein for Rab family protein(s).; . . . . 0.25280 0.15588 -0.929520514 9.683887709 185.96228 2.96216 TBC1D9B 1.4941078717937e-07 0.999562320479283 0.000437530109929921 TBC1 domain family member 9B FUNCTION: May act as a GTPase-activating protein for Rab family protein(s).; . . lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;hippocampus;amnion;duodenum;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;occipital lobe;cerebellum peduncles;pons;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.17465 . -0.44655933 24.21561689 493.36346 4.56713 TBC1D10A 0.975495334596957 0.024503580227124 1.08517591847747e-06 TBC1 domain family member 10A FUNCTION: Acts as GTPase-activating protein for RAB27A, but not for RAB2A, RAB3A, nor RAB4A. {ECO:0000269|PubMed:16923811}.; . . lymphoreticular;medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; placenta;testis; 0.48116 0.12990 -0.400392389 26.85185185 484.03886 4.52916 TBC1D10B 0.98178412798823 0.0182132923256175 2.57968615207305e-06 TBC1 domain family member 10B FUNCTION: Acts as GTPase-activating protein for RAB3A, RAB22A, RAB27A, AND RAB35. Does not act on RAB2A and RAB6A. {ECO:0000269|PubMed:16923811, ECO:0000269|PubMed:19077034}.; . . . . 0.37214 . -0.025608647 51.91672564 2004.63298 8.24457 TBC1D10C 0.00160909822063443 0.970029545888805 0.0283613558905609 TBC1 domain family member 10C FUNCTION: Inhibits the Ras signaling pathway through its intrinsic Ras GTPase-activating protein (GAP) activity. Acts as a negative feedback inhibitor of the calcineurin signaling pathway that also mediates crosstalk between calcineurin and Ras. {ECO:0000269|PubMed:17230191}.; . TISSUE SPECIFICITY: Most abundant in spleen and peripheral blood leukocytes. {ECO:0000269|PubMed:17230191}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;colon;blood;skeletal muscle;pancreas;lung;endometrium;bone;testis;spleen;germinal center;brain;mammary gland;stomach;thymus; white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion;whole blood;tonsil;thymus; 0.34250 0.11597 -0.846787714 11.05803255 47.75183 1.34230 TBC1D12 0.00264365020875562 0.997233134678716 0.00012321511252891 TBC1 domain family member 12 FUNCTION: May act as a GTPase-activating protein for Rab family protein(s).; . . uterus;prostate;smooth muscle;heart;islets of Langerhans;hypothalamus;placenta;liver;testis;kidney;brain;bladder;skin; dorsal root ganglion;medulla oblongata;superior cervical ganglion;spinal cord;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skin; 0.28656 . . . 86.49409 1.98534 TBC1D13 0.611736246776985 0.387905371746891 0.000358381476123858 TBC1 domain family member 13 FUNCTION: May act as a GTPase-activating protein for Rab family protein(s).; . . ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;lung;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle;parietal lobe; 0.23936 0.11060 -0.293801652 32.93819297 24.31278 0.79857 TBC1D14 0.909001498276562 0.0909982586478373 2.43075600373206e-07 TBC1 domain family member 14 FUNCTION: Negative regulator of starvation-induced autophagosome formation. {ECO:0000269|PubMed:22613832}.; . . . . 0.17119 . -0.817464788 11.97806086 90.3861 2.04538 TBC1D15 0.148718808827344 0.851274908543 6.28262965534984e-06 TBC1 domain family member 15 FUNCTION: Acts as a GTPase activating protein for RAB7A. Does not act on RAB4, RAB5 or RAB6 (By similarity). {ECO:0000250}.; . . ovary;umbilical cord;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;testis - interstitial;occipital lobe;testis;globus pallidus;ciliary ganglion;pons;atrioventricular node;skeletal muscle;parietal lobe; 0.24744 0.09547 -0.887242605 10.43288511 55.27473 1.49248 TBC1D16 0.00619825659275789 0.989508230958282 0.00429351244896018 TBC1 domain family member 16 FUNCTION: May act as a GTPase-activating protein for Rab family protein(s).; . . unclassifiable (Anatomical System);heart;ovary;skeletal muscle;skin;uterus;breast;prostate;endometrium;bone;kidney;mammary gland;brain;stomach; superior cervical ganglion;ciliary ganglion; 0.10822 0.10942 -0.455627566 23.72611465 227.00092 3.25605 TBC1D17 1.1203244858319e-12 0.152383503292456 0.847616496706424 TBC1 domain family member 17 FUNCTION: Probable GTPase-activating protein for Rab8; its transient association with Rab8 is mediated by OPTN. Inhibits Rab8-mediated endocytic trafficking, such as of transferrin receptor (TfR) and reduces Rab8 recruitnment to tubules emanating from the endocytic recycling compartment (ERC). Involved in regulation of autophagy. Mediates inhibition of autophagy caused by the OPTN variant GLC1E LYS-50; the function requires its catalytic activity, however, the involved Rab is not known. {ECO:0000269|PubMed:22854040, ECO:0000269|PubMed:24752605}.; . . smooth muscle;ovary;adrenal medulla;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;thyroid;pituitary gland;testis;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;islets of Langerhans;muscle;adrenal cortex;lens;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; prefrontal cortex; 0.10056 0.12608 -0.795417163 12.5324369 102.3879 2.18707 TBC1D19 0.0161012405580571 0.983854739043019 4.40203989235488e-05 TBC1 domain family member 19 FUNCTION: May act as a GTPase-activating protein for Rab family protein(s).; . . unclassifiable (Anatomical System);lymph node;blood;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;optic nerve;lung;placenta;macula lutea;hippocampus;liver;testis;kidney;brain; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.12675 0.12090 -0.247889024 35.98726115 90.32303 2.04467 TBC1D20 0.912642498359472 0.0872274508197648 0.000130050820763667 TBC1 domain family member 20 FUNCTION: GTPase-activating protein specific for Rab1 and Rab2 small GTPase families for which it can accelerate the intrinsic GTP hydrolysis rate by more than five orders of magnitude.; DISEASE: Warburg micro syndrome 4 (WARBM4) [MIM:615663]: A form of Warburg micro syndrome, a rare syndrome characterized by microcephaly, microphthalmia, microcornia, congenital cataracts, optic atrophy, cortical dysplasia, in particular corpus callosum hypoplasia, severe mental retardation, spastic diplegia, and hypogonadism. {ECO:0000269|PubMed:24239381}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;smooth muscle;ovary;salivary gland;colon;vein;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;thyroid;iris;testis;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;urinary;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;duodenum;liver;spleen;kidney;stomach; testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.22340 0.11011 -0.183570861 39.95046001 245.87321 3.38338 TBC1D21 0.0223267587117133 0.962120114808235 0.0155531264800518 TBC1 domain family member 21 FUNCTION: May act as a GTPase-activating protein for Rab family protein(s).; . . unclassifiable (Anatomical System);medulla oblongata;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;trigeminal ganglion;skeletal muscle; 0.23522 . -0.135838822 43.77211607 416.08891 4.26991 TBC1D22A 0.957287977622822 0.0427077076062541 4.31477092422138e-06 TBC1 domain family member 22A FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion;skeletal muscle; 0.17087 0.09651 0.202129237 67.42745931 93.04139 2.07249 TBC1D22A-AS1 . . . TBC1D22A antisense RNA 1 . . . . . . . . . . . TBC1D22B 0.0063706262671989 0.992787398097037 0.000841975635764084 TBC1 domain family member 22B FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). {ECO:0000250}.; . . . . 0.12821 0.09045 -0.426079032 25.36565228 27.71858 0.89136 TBC1D23 0.000111511568799616 0.9975378989976 0.00235058943360058 TBC1 domain family member 23 . . . unclassifiable (Anatomical System);ovary;colon;blood;vein;skin;skeletal muscle;bone marrow;uterus;whole body;lung;frontal lobe;mesenchyma;nasopharynx;bone;placenta;visual apparatus;liver;testis;spleen;kidney;germinal center;spinal ganglion;brain;stomach; ciliary ganglion;trigeminal ganglion; 0.28907 . -0.799052816 12.45576787 52.66145 1.43772 TBC1D24 5.84284760412081e-07 0.249832605127498 0.750166810587742 TBC1 domain family member 24 FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). Involved in neuronal projections development, probably through a negative modulation of ARF6 function. {ECO:0000269|PubMed:20727515, ECO:0000269|PubMed:20797691}.; DISEASE: Epileptic encephalopathy, early infantile, 16 (EIEE16) [MIM:615338]: A severe autosomal recessive neurologic disorder characterized by onset of seizures in the first weeks or months of life. Seizures can be of various types, are unresponsive to medication, last for long periods of time, and occur frequently. Affected infants show psychomotor regression or lack of psychomotor development, as well as other neurologic features such as extrapyramidal signs and hypotonia. Most die in childhood. {ECO:0000269|PubMed:23526554}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal dominant, 65 (DFNA65) [MIM:616044]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA65 is characterized by post- lingual onset of slowly progressive hearing loss in the third decade. Initially affecting the high frequencies, the hearing loss eventually affects all frequencies and results in severe to profound deafness in the seventh decade. Vestibular function is normal. {ECO:0000269|PubMed:24729539, ECO:0000269|PubMed:24729547}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, onychodystrophy, osteodystrophy, mental retardation, and seizures syndrome (DOORS) [MIM:220500]: A syndrome characterized by sensorineural deafness, mental retardation, hypoplastic or absent nails, small or absent distal phalanges of hands and feet. Additional features include coarse facies, a large nose with wide nasal bridge, bulbous tip and anteverted nares, a long prominent philtrum and downturned corners of the mouth. Progressive neurological manifestations include seizures from infancy, optic atrophy, and peripheral polyneuropathy. {ECO:0000269|PubMed:24291220}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal recessive, 86 (DFNB86) [MIM:614617]: A form of non-syndromic deafness characterized by prelingual onset of profound sensorineural hearing loss affecting all frequencies. {ECO:0000269|PubMed:24387994}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest expression in brain. {ECO:0000269|PubMed:20727515}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;germinal center;brain;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;lens;lung;placenta;hippocampus;macula lutea;liver;spleen;kidney;cerebellum; . 0.15994 . 0.600782551 82.82613824 83.6426 1.94553 TBC1D25 0.711973350325596 0.287340883290719 0.000685766383684911 TBC1 domain family member 25 FUNCTION: Acts as a GTPase-activating protein specific for RAB33B. Involved in the regulation of autophagosome maturation, the process in which autophagosomes fuse with endosomes and lysosomes. {ECO:0000269|PubMed:21383079}.; . . . . 0.52369 0.10799 0.040529541 57.15380986 36.93873 1.10539 TBC1D26 0.86148684441819 0.138080659790562 0.000432495791248184 TBC1 domain family member 26 FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). {ECO:0000305}.; . . . . 0.07565 . 1.284269037 93.76621845 3965.51936 12.46001 TBC1D27 . . . TBC1 domain family member 27 . . . unclassifiable (Anatomical System);lymph node;germinal center; . . . . . . . TBC1D28 1.44444385458443e-05 0.405209139143817 0.594776416417637 TBC1 domain family member 28 . . . lung;trabecular meshwork;testis; . 0.36621 . 0.082802743 60.09082331 17.77787 0.62103 TBC1D29 8.24847071045149e-05 0.32164634060767 0.678271174685225 TBC1 domain family member 29 . . . . . 0.07418 . 0.215080721 67.91696155 10.20934 0.37212 TBC1D30 . . . TBC1 domain family member 30 FUNCTION: GTPase-activating protein (GAP) with broad specificity. Acts as a GAP for RAB3A. Also exhibits significant GAP activity toward RAB22A, RAB27A, and RAB35 in vitro.; . . unclassifiable (Anatomical System);prostate;lung;frontal lobe;endometrium;epididymis;placenta;liver;testis;colon;brain;mammary gland; thalamus;subthalamic nucleus;occipital lobe;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skin; 0.27256 . . . 150.22298 2.67414 TBC1D31 1.34364593318333e-09 0.999364654125595 0.000635344530759234 TBC1 domain family member 31 . . . . . 0.08442 0.09981 0.099178678 60.75725407 2680.98409 9.73261 TBC1D32 1.35030437532423e-12 0.99912157643649 0.000878423562160185 TBC1 domain family member 32 FUNCTION: Required for high-level Shh responses in the developing neural tube. Together with CDK20, controls the structure of the primary cilium by coordinating assembly of the ciliary membrane and axoneme, allowing GLI2 to be properly activated in response to Shh signaling (By similarity). {ECO:0000250}.; . . . . 0.07698 . 1.697582556 96.4319415 3597.81877 11.61312 TBCA 0.716435529155031 0.269379908851959 0.0141845619930101 tubulin folding cofactor A FUNCTION: Tubulin-folding protein; involved in the early step of the tubulin folding pathway.; . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;atrium;whole body;cochlea;thyroid;testis;amniotic fluid;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;pia mater;lung;cornea;trabecular meshwork;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion; 0.27458 0.11550 -0.009020804 52.8544468 28.59892 0.91624 TBCAP1 . . . tubulin folding cofactor A pseudogene 1 . . . . . . . . . . . TBCAP2 . . . tubulin folding cofactor A pseudogene 2 . . . . . . . . . . . TBCAP3 . . . tubulin folding cofactor A pseudogene 3 . . . . . . . . . . . TBCB 0.405521802570773 0.585756253638766 0.00872194379046131 tubulin folding cofactor B FUNCTION: Binds to alpha-tubulin folding intermediates after their interaction with cytosolic chaperonin in the pathway leading from newly synthesized tubulin to properly folded heterodimer. Involved in regulation of tubulin heterodimer dissociation. May function as a negative regulator of axonal growth.; . TISSUE SPECIFICITY: Found in most tissues.; medulla oblongata;ovary;colon;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;brain;tonsil;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;thymus; amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.08922 0.10539 -0.383807564 27.41802312 11.3524 0.40856 TBCC 0.0110028256898399 0.837539314552167 0.151457859757993 tubulin folding cofactor C FUNCTION: Tubulin-folding protein; involved in the final step of the tubulin folding pathway. {ECO:0000269|PubMed:11847227}.; . TISSUE SPECIFICITY: Expressed in the retina. Expressed in the rod and cone photoreceptors, extending from the inner segments (IS), through the outer nuclear layer (ONL) and into the synapses in the outer plexiform layer (OPL). Strongly expressed to the photoreceptor connecting cilium at the tips of the IS (at protein level). {ECO:0000269|PubMed:12417528}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum; whole brain;amygdala;subthalamic nucleus;liver;cerebellum; 0.12314 0.11709 0.242582624 69.45623968 179.7945 2.91194 TBCCD1 0.0121109839106441 0.979968090731794 0.0079209253575616 TBCC domain containing 1 FUNCTION: Plays a role in the regulation of centrosome and Golgi apparatus positioning, with consequences on cell shape and cell migration. {ECO:0000269|PubMed:20168327}.; . . unclassifiable (Anatomical System);medulla oblongata;blood;skeletal muscle;bone marrow;uterus;lung;endometrium;bone;placenta;thyroid;liver;cervix;brain;artery;aorta;stomach; superior cervical ganglion;salivary gland;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.17818 0.15728 -0.933156985 9.54824251 310.5501 3.75028 TBCD 6.98438545881523e-05 0.999929838453057 3.1769235471793e-07 tubulin folding cofactor D FUNCTION: Tubulin-folding protein; involved in the first step of the tubulin folding pathway. Modulates microtubule dynamics by capturing GTP-bound beta-tubulin (TUBB). Acts as a GTPase- activating protein (GAP) for ARL2. Its ability to interact with beta tubulin is regulated via its interaction with ARL2. Induces microtubule disruption in absence of ARL2. Increases degradation of beta tubulin, when overexpressed in polarized cells. Promotes epithelial cell detachment, a process antagonized by ARL2. Induces tight adherens and tight junctions disassembly at the lateral cell membrane. {ECO:0000269|PubMed:10722852, ECO:0000269|PubMed:10831612, ECO:0000269|PubMed:11847227, ECO:0000269|PubMed:20740604}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10231032, ECO:0000269|PubMed:11110777}.; lymphoreticular;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;cartilage;heart;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;adrenal gland;placenta;head and neck;kidney;stomach;cerebellum;thymus; superior cervical ganglion;prefrontal cortex;caudate nucleus;trigeminal ganglion;skeletal muscle;thymus; 0.12203 0.11011 -1.453286053 3.892427459 630.24341 5.05995 TBCE 6.2870662207293e-07 0.969238337313251 0.0307610339801269 tubulin folding cofactor E FUNCTION: Tubulin-folding protein; involved in the second step of the tubulin folding pathway. Seems to be implicated in the maintenance of the neuronal microtubule network. Involved in regulation of tubulin heterodimer dissociation. {ECO:0000269|PubMed:11847227}.; DISEASE: Hypoparathyroidism-retardation-dysmorphism syndrome (HRD) [MIM:241410]: Autosomal recessive disorder reported almost exclusively in Middle Eastern populations. {ECO:0000269|PubMed:12389028}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Kenny-Caffey syndrome 1 (KCS1) [MIM:244460]: An autosomal recessive form of Kenny-Caffey syndrome, a disorder characterized by impaired skeletal development with small and dense bones, short stature, and primary hypoparathyroidism with hypocalcemia. Clinical features include cortical thickening and medullary stenosis of the tubular bones, delayed closure of fontanels, defective dentition, small eyes with hypermetropia, and frontal bossing with a triangular face. {ECO:0000269|PubMed:12389028}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.10379 0.34799 0.801024817 87.65628686 219.3093 3.20281 TBCEL 0.971498208896393 0.0284940004452347 7.79065837234673e-06 tubulin folding cofactor E-like FUNCTION: Acts as a regulator of tubulin stability. {ECO:0000269|PubMed:15728251}.; . TISSUE SPECIFICITY: Abundantly expressed in testis, but is also present in several tissues at a much lower level. {ECO:0000269|PubMed:15728251}.; unclassifiable (Anatomical System);myocardium;cartilage;heart;islets of Langerhans;parathyroid;skeletal muscle;bone marrow;uterus;prostate;lung;bone;thyroid;placenta;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.49889 0.11659 -0.139478553 43.29440906 22.06126 0.74051 TBCK 3.2154815637914e-06 0.999352989334345 0.000643795184091047 TBC1 domain containing kinase . . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;uterus;prostate;frontal lobe;endometrium;bone;pituitary gland;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;pia mater;lung;cornea;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; . . -0.042196577 50.49539986 1635.40912 7.47380 TBK1 0.995096971403116 0.00490302773944205 8.57441452306793e-10 TANK binding kinase 1 FUNCTION: Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents. Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB. In order to establish such an antiviral state, TBK1 form several different complexes whose composition depends on the type of cell and cellular stimuli. Thus, several scaffolding molecules including FADD, TRADD, MAVS, AZI2, TANK or TBKBP1/SINTBAD can be recruited to the TBK1-containing-complexes. Under particular conditions, functions as a NF-kappa-B effector by phosphorylating NF-kappa-B inhibitor alpha/NFKBIA, IKBKB or RELA to translocate NF-Kappa-B to the nucleus. Restricts bacterial proliferation by phosphorylating the autophagy receptor OPTN/Optineurin on 'Ser- 177', thus enhancing LC3 binding affinity and antibacterial autophagy. Phosphorylates and activates AKT1. Seems to play a role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity. Attenuates retroviral budding by phosphorylating the endosomal sorting complex required for transport-I (ESCRT-I) subunit VPS37C. Phosphorylates Borna disease virus (BDV) P protein. {ECO:0000269|PubMed:10581243, ECO:0000269|PubMed:10783893, ECO:0000269|PubMed:11839743, ECO:0000269|PubMed:12692549, ECO:0000269|PubMed:12702806, ECO:0000269|PubMed:14703513, ECO:0000269|PubMed:15367631, ECO:0000269|PubMed:15485837, ECO:0000269|PubMed:15489227, ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:21138416, ECO:0000269|PubMed:21270402, ECO:0000269|PubMed:21464307, ECO:0000269|PubMed:21617041, ECO:0000269|PubMed:21931631, ECO:0000269|PubMed:23453971, ECO:0000269|PubMed:23453972, ECO:0000269|PubMed:23746807}.; DISEASE: Glaucoma 1, open angle, P (GLC1P) [MIM:177700]: A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. GLC1P is characterized by early onset, thin central corneas and low intraocular pressure. {ECO:0000269|PubMed:21447600, ECO:0000269|PubMed:22306015}. Note=The disease may be caused by mutations affecting the gene represented in this entry. A copy number variation on chromosome 12q14 consisting of a 300 kb duplication that includes TBK1, XPOT, RASSF3 and GNS has been found in individuals affected by glaucoma. TBK1 is the most likely candidate for the disorder (PubMed:21447600). {ECO:0000269|PubMed:21447600}.; DISEASE: Frontotemporal dementia and/or amyotrophic lateral sclerosis 4 (FTDALS4) [MIM:616439]: A neurodegenerative disorder characterized by frontotemporal dementia and/or amyotrophic lateral sclerosis in affected individuals. There is high intrafamilial variation. Frontotemporal dementia is characterized by frontal and temporal lobe atrophy associated with neuronal loss, gliosis, and dementia. Patients exhibit progressive changes in social, behavioral, and/or language function. Amyotrophic lateral sclerosis is characterized by the death of motor neurons in the brain, brainstem, and spinal cord, resulting in fatal paralysis. {ECO:0000269|PubMed:25803835, ECO:0000269|PubMed:25943890}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous with higher expression in testis. Expressed in the ganglion cells, nerve fiber layer and microvasculature of the retina. {ECO:0000269|PubMed:10783893, ECO:0000269|PubMed:21447600}.; myocardium;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;cervix;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.17165 0.35025 -0.291981272 33.20358575 93.23558 2.07750 TBKBP1 0.0383777655190971 0.9546117940462 0.00701044043470259 TBK1 binding protein 1 FUNCTION: Adapter protein which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity. {ECO:0000269|PubMed:21931631}.; . TISSUE SPECIFICITY: Detected in leukocytes, lung, placenta, small intestine, liver, kidney, spleen, muscle, heart, brain and at low levels in thymus. {ECO:0000269|PubMed:17568778}.; colon;fovea centralis;choroid;skin;retina;optic nerve;whole body;larynx;thyroid;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;muscle;blood;lens;pancreas;lung;placenta;macula lutea;liver;duodenum;spleen;head and neck;kidney;mammary gland;stomach; subthalamic nucleus;testis - interstitial;occipital lobe;superior cervical ganglion;prefrontal cortex;globus pallidus; 0.51167 0.13142 . . 547.62594 4.75880 TBL1X 0.998500302780111 0.00149966880462078 2.8415267958164e-08 transducin (beta)-like 1X-linked FUNCTION: F-box-like protein involved in the recruitment of the ubiquitin/19S proteasome complex to nuclear receptor-regulated transcription units. Plays an essential role in transcription activation mediated by nuclear receptors. Probably acts as integral component of corepressor complexes that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of transcription repressor complexes, thereby allowing cofactor exchange. {ECO:0000269|PubMed:14980219}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10330347}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pineal body;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;hypothalamus;pons;atrioventricular node;uterus;prostate;testis - seminiferous tubule;placenta;liver;testis;ciliary ganglion;trigeminal ganglion;whole blood;pituitary; 0.37237 0.36829 -0.822919685 11.76574664 32.94362 1.02031 TBL1XR1 0.998821952425029 0.0011780317994886 1.577548245387e-08 transducin (beta)-like 1 X-linked receptor 1 FUNCTION: F-box-like protein involved in the recruitment of the ubiquitin/19S proteasome complex to nuclear receptor-regulated transcription units. Plays an essential role in transcription activation mediated by nuclear receptors. Probably acts as integral component of the N-Cor corepressor complex that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of N-Cor complex, thereby allowing cofactor exchange, and transcription activation. {ECO:0000269|PubMed:14980219}.; . TISSUE SPECIFICITY: Ubiquitous.; unclassifiable (Anatomical System);ovary;colon;skeletal muscle;retina;breast;uterus;pancreas;prostate;endometrium;thyroid;placenta;amnion;hypopharynx;liver;testis;head and neck;germinal center;brain; superior cervical ganglion;ciliary ganglion; 0.93008 0.25362 -0.163345027 41.24793583 5.26325 0.19576 TBL1XR1-AS1 . . . TBL1XR1 antisense RNA 1 . . . . . . . . . . . TBL1Y . . . transducin (beta)-like 1, Y-linked FUNCTION: F-box-like protein involved in the recruitment of the ubiquitin/19S proteasome complex to nuclear receptor-regulated transcription units. Plays an essential role in transcription activation mediated by nuclear receptors. Probably acts as integral component of corepressor complexes that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of transcription repressor complexes, thereby allowing cofactor exchange (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Fetal brain and prostate. {ECO:0000269|PubMed:12815422}.; germinal center; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.54478 . . . 40.12541 1.17905 TBL1YP1 . . . transducin (beta)-like 1, Y-linked pseudogene 1 . . . . . . . . . . . TBL2 0.00437650656905421 0.962897225818332 0.0327262676126133 transducin (beta)-like 2 . DISEASE: Note=TBL2 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of TBL2 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease.; . medulla oblongata;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;muscle;pancreas;lung;mesenchyma;placenta;hippocampus;duodenum;kidney;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;pons;atrioventricular node;trigeminal ganglion; 0.24778 0.13627 -0.93133804 9.613116301 365.36979 4.04552 TBL3 1.53647496342632e-06 0.998145068001405 0.00185339552363189 transducin (beta)-like 3 . . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;islets of Langerhans;pineal body;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach; prostate;heart;testis - seminiferous tubule;thyroid;liver;testis;atrioventricular node; 0.16182 0.11544 -0.338129542 30.07784855 1241.80468 6.65189 TBP 0.490805122134187 0.508245304389302 0.000949573476511526 TATA-box binding protein FUNCTION: General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre- initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II. Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1 with the rDNA promoter. SL1 is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. {ECO:0000269|PubMed:15970593}.; DISEASE: Spinocerebellar ataxia 17 (SCA17) [MIM:607136]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA17 is an autosomal dominant cerebellar ataxia (ADCA) characterized by widespread cerebral and cerebellar atrophy, dementia and extrapyramidal signs. The molecular defect in SCA17 is the expansion of a CAG repeat in the coding region of TBP. Longer expansions result in earlier onset and more severe clinical manifestations of the disease. {ECO:0000269|PubMed:11313753, ECO:0000269|PubMed:11448935, ECO:0000269|PubMed:11939898}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, with levels highest in the testis and ovary. {ECO:0000269|PubMed:17570761}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;optic nerve;whole body;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;stomach; testis - interstitial;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.99943 0.68788 -0.229483771 36.86010852 6.50302 0.24106 TBPL1 0.879617094046 0.118940607316802 0.00144229863719801 TATA-box binding protein like 1 FUNCTION: Part of a specialized transcription system that mediates the transcription of most ribosomal proteins through the 5'-TCT-3' motif which is a core promoter element at these genes. Seems to also mediate the transcription of NF1. Does not bind the TATA box. {ECO:0000269|PubMed:10082669, ECO:0000269|PubMed:10220372, ECO:0000269|PubMed:15767669, ECO:0000269|PubMed:24958592}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in the testis and ovary. {ECO:0000269|PubMed:10082669, ECO:0000269|PubMed:17570761}.; medulla oblongata;ovary;colon;parathyroid;skin;bone marrow;prostate;frontal lobe;endometrium;larynx;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;islets of Langerhans;hypothalamus;urinary;blood;lens;skeletal muscle;lung;adrenal gland;placenta;liver;head and neck;kidney;mammary gland; amygdala;whole brain;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;pons; 0.71526 0.23984 0.323496558 72.93583392 10.32106 0.37623 TBPL2 4.93486514101523e-08 0.219651771436521 0.780348179214827 TATA-box binding protein like 2 FUNCTION: Transcription factor required in complex with TAF3 for the differentiation of myoblasts into myocytes. The complex replaces TFIID at specific promoters at an early stage in the differentiation process (By similarity). {ECO:0000250|UniProtKB:Q6SJ95}.; . TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined with highest levels in heart, lung, ovary, spleen and testes. {ECO:0000269|PubMed:14634207, ECO:0000269|PubMed:17570761}.; . . 0.64899 0.11308 0.108486928 61.90728946 145.57917 2.62916 TBR1 0.993588037464593 0.00641097747718691 9.85058220457899e-07 T-box, brain 1 FUNCTION: Probable transcriptional regulator involved in developmental processes. Required for normal brain development.; . TISSUE SPECIFICITY: Brain.; . . 0.93213 0.38022 -0.405853867 26.23260203 93.16795 2.07643 TBRG1 8.02614053558845e-05 0.52629419722956 0.473625541365084 transforming growth factor beta regulator 1 FUNCTION: Acts as a growth inhibitor. Can activate p53/TP53, causes G1 arrest and collaborates with CDKN2A to restrict proliferation, but does not require either protein to inhibit DNA synthesis. Redistributes CDKN2A into the nucleoplasm. Involved in maintaining chromosomal stability. {ECO:0000269|PubMed:17110379}.; . TISSUE SPECIFICITY: Widely expressed at low levels in most tissues, with highest levels in pancreas, lung and liver. Expression is decreased in primary tumors including lung, liver, breast, pancreas and kidney carcinomas, chronic lymphocytic leukemia and diffuse large B-cell lymphoma. {ECO:0000269|PubMed:17110379}.; ovary;salivary gland;sympathetic chain;developmental;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; . 0.05754 0.10881 -0.183570861 39.95046001 287.06488 3.63031 TBRG4 0.780939582899283 0.219047722431187 1.26946695293907e-05 transforming growth factor beta regulator 4 FUNCTION: May play a role in cell cycle progression. {ECO:0000269|PubMed:9383053}.; . TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:12759187). Expression detected in spleen, thymus, testis, ovary, colon, heart, smooth muscle, kidney, brain, lung, liver and white adipose tissue with highest expression in smooth muscle (PubMed:20869947). {ECO:0000269|PubMed:12759187, ECO:0000269|PubMed:20869947}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;brain;heart;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;trachea;adrenal gland;placenta;duodenum;head and neck;kidney;stomach;aorta; . 0.06903 0.08967 -0.442665927 24.53408823 1151.64263 6.46591 TBX1 0.983396787766063 0.0165930755786156 1.01366553213123e-05 T-box 1 FUNCTION: Probable transcriptional regulator involved in developmental processes. Is required for normal development of the pharyngeal arch arteries (By similarity). {ECO:0000250}.; DISEASE: Note=Haploinsufficiency of the TBX1 gene is responsible for most of the physical malformations present in DiGeorge syndrome (DGS) and velocardiofacial syndrome (VCFS). DGS is characterized by the association of several malformations: hypoplastic thymus and parathyroid glands, congenital conotruncal cardiopathy, and a subtle but characteristic facial dysmorphology. VCFS is marked by the association of congenital conotruncal heart defects, cleft palate or velar insufficiency, facial dysmorpholgy and learning difficulties. It is now accepted that these two syndromes represent two forms of clinical expression of the same entity manifesting at different stages of life.; DISEASE: DiGeorge syndrome (DGS) [MIM:188400]: A congenital syndrome characterized by a wide spectrum of characteristics including parathyroid hypoplasia resulting in hypocalcemia, thymic hypoplasia resulting in T-cell immunodeficiency, defects in the outflow tract of the heart, and craniofacial anomalies. Disturbance of cervical neural crest migration into the derivatives of the pharyngeal arches and pouches can account for the phenotype. {ECO:0000269|PubMed:14585638}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Velocardiofacial syndrome (VCFS) [MIM:192430]: A syndrome characterized by abnormal pharyngeal arch development that results in defective development of the parathyroid glands, thymus, and conotruncal region of the heart. The phenotype is highly variable, with no single clinical feature present in every patient. Affected individuals may present with structural or functional palatal abnormalities, cardiac defects, unique facial characteristics, hypernasal speech, hypotonia, and defective thymic development associated with impaired immune function. In addition, affected individuals may present with learning disabilities, overt developmental delay, and psychiatric disorders. {ECO:0000269|PubMed:14585638, ECO:0000269|PubMed:17273972}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Conotruncal heart malformations (CTHM) [MIM:217095]: A group of congenital heart defects involving the outflow tracts. Examples include truncus arteriosus communis, double-outlet right ventricle and transposition of great arteries. Truncus arteriosus communis is characterized by a single outflow tract instead of a separate aorta and pulmonary artery. In transposition of the great arteries, the aorta arises from the right ventricle and the pulmonary artery from the left ventricle. In double outlet of the right ventricle, both the pulmonary artery and aorta arise from the right ventricle. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;lung;ovary;heart;tongue;testis;colon;head and neck;skin;skeletal muscle; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.32608 . . . 1845.84011 7.92600 TBX2 0.964019296564926 0.035966811150967 1.38922841074358e-05 T-box 2 FUNCTION: Involved in the transcriptional regulation of genes required for mesoderm differentiation. Probably plays a role in limb pattern formation. Acts as a negative regulator of PML function in cellular senescence. May be required for cardiac atrioventricular canal formation. {ECO:0000269|PubMed:22002537}.; . TISSUE SPECIFICITY: Expressed primarily in adult in kidney, lung, and placenta. Weak expression in heart and ovary.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;testis;spinal ganglion;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;urinary;muscle;lens;pancreas;lung;placenta;macula lutea;visual apparatus;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;lung;placenta;thyroid;ciliary ganglion;fetal lung;kidney;trigeminal ganglion; 0.95506 0.22835 . . 110.49845 2.28855 TBX2-AS1 . . . TBX2 antisense RNA 1 . . . . . . . . . . . TBX3 0.948925457312872 0.0510412072178786 3.33354692490214e-05 T-box 3 FUNCTION: Transcriptional repressor involved in developmental processes. Probably plays a role in limb pattern formation. Acts as a negative regulator of PML function in cellular senescence. {ECO:0000269|PubMed:10468588, ECO:0000269|PubMed:22002537}.; . TISSUE SPECIFICITY: Widely expressed.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;pineal body;adrenal cortex;pharynx;blood;lens;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;prostate;adrenal gland;thyroid;placenta;adrenal cortex;fetal lung;fetal thyroid; 0.93228 0.19050 -0.732911333 14.07761264 233.72039 3.30426 TBX4 0.407057023157267 0.592577644770237 0.000365332072495613 T-box 4 FUNCTION: Involved in the transcriptional regulation of genes required for mesoderm differentiation. Probably plays a role in limb pattern formation.; DISEASE: Small patella syndrome (SPS) [MIM:147891]: Autosomal dominant skeletal dysplasia characterized by patellar aplasia or hypoplasia and by anomalies of the pelvis and feet, including disrupted ossification of the ischia and inferior pubic rami. {ECO:0000269|PubMed:15106123}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;whole body;testis;stomach; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion; 0.86743 0.14618 -0.576764155 18.7839113 3843.41705 12.20548 TBX5 0.991878563864068 0.00811968028565935 1.7558502728299e-06 T-box 5 FUNCTION: DNA-binding protein that regulates the transcription of several genes and is involved in heart development and limb pattern formation. {ECO:0000269|PubMed:25725155, ECO:0000269|PubMed:25963046, ECO:0000269|PubMed:8988164}.; DISEASE: Holt-Oram syndrome (HOS) [MIM:142900]: Developmental disorder affecting the heart and upper limbs. It is characterized by thumb anomaly and atrial septal defects. {ECO:0000269|PubMed:10077612, ECO:0000269|PubMed:10842287, ECO:0000269|PubMed:12818525, ECO:0000269|PubMed:15735645, ECO:0000269|PubMed:20450920, ECO:0000269|PubMed:8988164, ECO:0000269|PubMed:8988165}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in TBX5 are associated with susceptibility to dilated cardiomyopathy (DCM). A disorder characterized by ventricular and impaired systolic function, resulting in heart failure and arrhythmia. Patient are at risk of premature death. {ECO:0000269|PubMed:25725155, ECO:0000269|PubMed:25963046}.; . unclassifiable (Anatomical System);uterus;myocardium;lung;heart;placenta;testis;skin;stomach; superior cervical ganglion;heart;atrioventricular node;skeletal muscle; 0.82455 0.20930 -0.554717505 19.79830149 123.51325 2.41913 TBX5-AS1 . . . TBX5 antisense RNA 1 . . . . . . . . . . . TBX6 0.0291474892908083 0.960294674298451 0.0105578364107411 T-box 6 FUNCTION: T-box transcription factor that plays an essential role in the determination of the fate of axial stem cells: neural vs mesodermal. Acts in part by down-regulating, a specific enhancer (N1) of SOX2, to inhibit neural development. Seems to play also an essential role in left/right axis determination and acts through effects on Notch signaling around the node as well as through an effect on the morphology and motility of the nodal cilia (By similarity). {ECO:0000250}.; DISEASE: Spondylocostal dysostosis 5, autosomal dominant (SCDO5) [MIM:122600]: A rare condition of variable severity characterized by vertebral and costal anomalies. The main feature include dwarfism, vertebral fusion, hemivertebrae, posterior rib fusion, reduced rib number, and other rib malformations. {ECO:0000269|PubMed:23335591}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in fetal tail bud, posterior spinal tissue, intervertebral disk and testis. Also expressed in adult testis, kidney, lung, muscle and thymus.; unclassifiable (Anatomical System);lung;larynx;bone;head and neck;brain;mammary gland;skeletal muscle; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.16904 0.11983 -0.047654689 50.22410946 115.08733 2.33392 TBX10 2.15116537729034e-07 0.264914845833137 0.735084939050325 T-box 10 FUNCTION: Probable transcriptional regulator involved in developmental processes.; . . unclassifiable (Anatomical System);colon;germinal center; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.11670 0.12850 -0.091746757 46.91554612 1177.2229 6.51938 TBX15 0.877333976211489 0.122602207170704 6.38166178075209e-05 T-box 15 FUNCTION: Probable transcriptional regulator involved in the development of the skeleton of the limb, vertebral column and head. Acts by controlling the number of mesenchymal precursor cells and chondrocytes (By similarity). {ECO:0000250}.; DISEASE: Cousin syndrome (COUSS) [MIM:260660]: Defined as pelviscapular dysplasia with epiphyseal abnormalities, congenital dwarfism and facial dysmorphy (frontal bossing, hypertelorism, narrow palpebral fissures, deep set globes, strabismus, low-set posteriory rotated and unusually formed external ears, dysplasia of conchae, small chin, short neck with redundant skin folds, and a low hairline). Intelligence may vary from normal to moderately impaired. Radiographic features comprise aplasia of the body of the scapula, hypoplasia of the iliac bone, humeroradial synosthosis, dislocation of the femoral heads, and moderate brachydactyly. {ECO:0000269|PubMed:19068278}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);whole body;cartilage;ovary;cochlea;bone;placenta;muscle;liver;testis;colon;parathyroid;brain;peripheral nerve; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.72703 0.11809 0.174625237 65.9648502 1230.33085 6.63038 TBX18 0.997468364011956 0.00253153411111614 1.0187692753728e-07 T-box 18 FUNCTION: Acts as transcriptional repressor involved in developmental processes of a variety of tissues and organs, including the heart and coronary vessels, the ureter and the vertebral column. Required for embryonic development of the sino atrial node (SAN) head area. {ECO:0000250|UniProtKB:Q9EPZ6, ECO:0000269|PubMed:26235987}.; DISEASE: Congenital anomalies of kidney and urinary tract 2 (CAKUT2) [MIM:143400]: A disorder encompassing a broad spectrum of renal and urinary tract malformations that include renal agenesis, kidney hypodysplasia, multicystic kidney dysplasia, duplex collecting system, posterior urethral valves and ureter abnormalities. Congenital anomalies of kidney and urinary tract are the commonest cause of chronic kidney disease in children. {ECO:0000269|PubMed:26235987}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.39422 0.13130 -0.402212257 26.7338995 3185.14035 10.75423 TBX18-AS1 . . . TBX18 antisense RNA 1 . . . . . . . . . . . TBX19 2.79914141349298e-05 0.774467950883126 0.225504057702739 T-box 19 FUNCTION: Transcriptional regulator involved in developmental processes. Can activate POMC gene expression and repress the alpha glycoprotein subunit and thyroid-stimulating hormone beta promoters. {ECO:0000269|PubMed:11290323}.; DISEASE: ACTH deficiency, isolated (IAD) [MIM:201400]: A disorder that is characterized by adrenal insufficiency symptoms, such as weight loss, lack of appetite (anorexia), weakness, nausea, vomiting and low blood pressure (hypotension). The pituitary hormone ACTH is decreased or absent, and other cortisol and other steroid hormone levels in the blood are abnormally low. {ECO:0000269|PubMed:11290323}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.39366 0.22086 -0.955204708 9.170794999 44.73479 1.28223 TBX20 0.337045818385032 0.659877494975837 0.00307668663913157 T-box 20 FUNCTION: Acts as a transcriptional activator and repressor required for cardiac development and may have key roles in the maintenance of functional and structural phenotypes in adult heart. {ECO:0000250}.; DISEASE: Atrial septal defect 4 (ASD4) [MIM:611363]: A congenital heart malformation characterized by incomplete closure of the wall between the atria resulting in blood flow from the left to the right atria. Patients show other heart abnormalities including defects in septation, chamber growth and valvulogenesis. The disease is not associated with defects in the cardiac conduction system or with non-cardiac abnormalities. {ECO:0000269|PubMed:17668378, ECO:0000269|PubMed:19762328}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.69521 0.14747 -0.780646273 12.77423921 13.67944 0.49629 TBX21 0.963242650804377 0.0367426986361368 1.46505594866631e-05 T-box 21 FUNCTION: Transcription factor that controls the expression of the TH1 cytokine, interferon-gamma. Initiates TH1 lineage development from naive TH precursor cells both by activating TH1 genetic programs and by repressing the opposing TH2 programs.; . TISSUE SPECIFICITY: T-cell specific.; blood;germinal center; superior cervical ganglion; 0.27556 0.55228 -0.736552314 13.93606983 264.8926 3.49316 TBX22 0.974752070043244 0.0252194685577233 2.84613990326174e-05 T-box 22 FUNCTION: Probable transcriptional regulator involved in developmental processes. This is major determinant crucial to palatogenesis.; DISEASE: Abruzzo-Erickson syndrome (ABERS) [MIM:302905]: A disease characterized by cleft palate, coloboma, hypospadias, deafness, short stature, and radial synostosis. {ECO:0000269|PubMed:22784330}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Seems to be expressed at a low level.; . . 0.08841 0.12779 -0.181750739 40.15687662 204.29784 3.08782 TBX23P . . . T-box 23, pseudogene . . . . . . . . . . . TBXA1R . . . thromboxane A1 receptor . . . . . . . . . . . TBXA2R 0.113768130952393 0.77817241319069 0.108059455856917 thromboxane A2 receptor FUNCTION: Receptor for thromboxane A2 (TXA2), a potent stimulator of platelet aggregation. The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. In the kidney, the binding of TXA2 to glomerular TP receptors causes intense vasoconstriction. Activates phospholipase C. Isoform 1 activates adenylyl cyclase. Isoform 2 inhibits adenylyl cyclase. {ECO:0000269|PubMed:8613548}.; DISEASE: Bleeding disorder, platelet-type 13 (BDPLT13) [MIM:614009]: A disorder characterized by reduced platelet aggregation and a tendency to mild mucocutaneous bleeding. {ECO:0000269|PubMed:7929844}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . . . 0.06777 0.31290 -0.137658575 43.57159707 164.53131 2.80092 TBXAS1 1.37136184087511e-08 0.575459615681219 0.424540370605162 thromboxane A synthase 1 . DISEASE: Note=Thromboxane synthetase deficiency has been detected in some patients with a bleeding disorder due to platelet dysfunction. {ECO:0000269|PubMed:6101498}.; TISSUE SPECIFICITY: Platelets, lung, kidney, spleen, macrophages and lung fibroblasts.; ovary;colon;parathyroid;choroid;retina;bone marrow;uterus;prostate;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;liver;spleen;kidney;mammary gland;stomach; ciliary ganglion;whole blood; 0.12400 0.32069 0.938775246 89.87379099 946.51884 5.95930 TC2N 0.0121893285015318 0.986197983950562 0.00161268754790592 tandem C2 domains, nuclear . . . smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;endometrium;thyroid;testis;artery;bladder;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;adrenal cortex;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;liver;hypopharynx;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; . 0.07677 0.09218 -0.089927255 46.99221515 87.04722 1.99236 TCAF1 . . . TRPM8 channel-associated factor 1 FUNCTION: Positively regulates the plasma membrane cation channel TRPM8 activity. Involved in the recruitment of TRPM8 to the cell surface. Promotes prostate cancer cell migration inhibition in a TRPM8-dependent manner. {ECO:0000269|PubMed:25559186}.; . TISSUE SPECIFICITY: Isoform 2 is expressed in the prostate and strongly expressed in cancerous prostate samples. {ECO:0000269|PubMed:25559186}.; . . . 0.08955 . . . . TCAF1P1 . . . TRPM8 channel-associated factor 1 pseudogene 1 . . . . . . . . . . . TCAF2 . . . TRPM8 channel-associated factor 2 FUNCTION: Isoform 2: Negatively regulates the plasma membrane cation channel TRPM8 activity. Involved in the recruitment of TRPM8 to the cell surface. Promotes prostate cancer cell migration stimulation in a TRPM8-dependent manner. {ECO:0000269|PubMed:25559186}.; . TISSUE SPECIFICITY: Isoform 2 is expressed in the prostate and in cancerous prostate samples. {ECO:0000269|PubMed:25559186}.; . . 0.10177 . . . . . TCAF2P1 . . . TRPM8 channel-associated factor 2 pseudogene 1 . . . . . 0.29191 . . . . . TCAIM 4.45858902178291e-05 0.960451330257931 0.0395040838518507 T-cell activation inhibitor, mitochondrial FUNCTION: May regulate T-cell apoptosis. {ECO:0000250}.; . . . . 0.08831 . -0.404032746 26.53338051 125.51432 2.43855 TCAM1P . . . testicular cell adhesion molecule 1, pseudogene . . . . . . . . . . . TCAP 0.0757710084804901 0.748205951576314 0.176023039943196 titin-cap FUNCTION: Muscle assembly regulating factor. Mediates the antiparallel assembly of titin (TTN) molecules at the sarcomeric Z-disk.; DISEASE: Limb-girdle muscular dystrophy 2G (LGMD2G) [MIM:601954]: An autosomal recessive degenerative myopathy characterized by proximal and distal muscle weakness and atrophy in the limbs, dystrophic changes on muscle biopsy, and absence of telethonin. Cardiac muscle is involved in a subset of patients. {ECO:0000269|PubMed:10655062}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Heart and skeletal muscle.; unclassifiable (Anatomical System);myocardium;heart;muscle;fovea centralis;choroid;lens;skin;skeletal muscle;retina;breast;pancreas;prostate;optic nerve;whole body;lung;bone;macula lutea;visual apparatus;iris;liver;testis; heart;tongue;thyroid;skeletal muscle; 0.11716 0.27320 0.459411326 78.28497287 77.83223 1.86053 TCEA1 0.342254929345763 0.654791586770721 0.00295348388351602 transcription elongation factor A1 FUNCTION: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.; DISEASE: Note=A chromosomal aberration involving TCEA1 may be a cause of salivary gland pleiomorphic adenomas (PA) [181030]. Pleiomorphic adenomas are the most common benign epithelial tumors of the salivary gland. Translocation t(3;8)(p21;q12) with PLAG1. {ECO:0000269|PubMed:10029085}.; . . . . 0.12971 0.347360312 73.97381458 29.58251 0.94513 TCEA1P1 . . . transcription elongation factor A1 pseudogene 1 . . . . . . . . . . . TCEA1P2 . . . transcription elongation factor A1 pseudogene 2 FUNCTION: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.; DISEASE: Note=A chromosomal aberration involving TCEA1 may be a cause of salivary gland pleiomorphic adenomas (PA) [181030]. Pleiomorphic adenomas are the most common benign epithelial tumors of the salivary gland. Translocation t(3;8)(p21;q12) with PLAG1. {ECO:0000269|PubMed:10029085}.; . . . . 0.12971 0.347360312 73.97381458 . . TCEA1P3 . . . transcription elongation factor A1 pseudogene 3 . . . . . . . . . . . TCEA1P4 . . . transcription elongation factor A1 pseudogene 4 . . . . . . . . . . . TCEA2 0.00781797115613869 0.977426368717826 0.0147556601260352 transcription elongation factor A2 FUNCTION: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus. {ECO:0000269|PubMed:12034815}.; . TISSUE SPECIFICITY: Testis and ovary specific. {ECO:0000269|PubMed:8566795}.; myocardium;medulla oblongata;ovary;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;amniotic fluid;germinal center;pineal gland;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pineal body;blood;lens;breast;pancreas;lung;placenta;trabecular meshwork;hippocampus;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland; amygdala;whole brain;occipital lobe;testis - interstitial;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;parietal lobe;cingulate cortex; 0.54211 0.12592 -0.337894035 30.37272942 62.51264 1.61538 TCEA3 0.000965885853095805 0.943824234877174 0.0552098792697305 transcription elongation factor A3 FUNCTION: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.; . . . . 0.55654 0.08524 -0.337894035 30.37272942 76.13988 1.82827 TCEAL1 0.488641003961424 0.433197315698585 0.0781616803399914 transcription elongation factor A like 1 FUNCTION: May be involved in transcriptional regulation. Modulates various viral and cellular promoters in a promoter context- dependent manner. For example, transcription from the FOS promoter is increased, while Rous sarcoma virus (RSV) long terminal repeat (LTR) promoter activity is repressed. Does not bind DNA directly.; . TISSUE SPECIFICITY: Expressed in all tissues examined. Highly expressed in heart, ovary, prostate and skeletal muscle. Moderately expressed in brain, placenta, testis and small intestine. Weakly expressed in lung, liver and spleen. Expressed in several cancer cell lines. {ECO:0000269|PubMed:10051408}.; . . 0.05280 0.11345 0.079165051 59.43029016 20.19528 0.69102 TCEAL2 0.679466606366515 0.300549561967789 0.0199838316656961 transcription elongation factor A like 2 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);prostate;frontal lobe;cerebellum cortex;endometrium;islets of Langerhans;visual apparatus;hippocampus;developmental;testis;colon;kidney;brain; whole brain;amygdala;thalamus;superior cervical ganglion;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;testis;globus pallidus;parietal lobe;cingulate cortex;pituitary;cerebellum; 0.05909 0.06564 0.43736446 77.56546355 36.33811 1.08910 TCEAL3 0.603339069922021 0.359897791410207 0.0367631386677715 transcription elongation factor A like 3 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;choroid;fovea centralis;vein;skin;retina;uterus;prostate;optic nerve;bone;iris;testis;brain;unclassifiable (Anatomical System);lens;skeletal muscle;lung;nasopharynx;trabecular meshwork;placenta;hippocampus;visual apparatus;macula lutea;kidney;mammary gland; . 0.12104 0.10162 0.21326276 67.71644256 7.56529 0.28067 TCEAL3-AS1 . . . TCEAL3 antisense RNA 1 . . . . . . . . . . . TCEAL4 0.683649622368237 0.297092324263894 0.0192580533678692 transcription elongation factor A like 4 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.10268 0.07800 0.235309407 68.71903751 77.7218 1.85746 TCEAL4P1 . . . transcription elongation factor A like 4 pseudogene 1 . . . . . . . . . . . TCEAL5 0.666797567268795 0.31090519746551 0.0222972352656949 transcription elongation factor A like 5 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.10123 . 0.191216164 66.57230479 730.81358 5.36747 TCEAL6 0.650796969830344 0.323726204134762 0.0254768260348941 transcription elongation factor A like 6 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.05573 0.07840 -0.073340031 48.11866006 128.08768 2.46706 TCEAL7 0.45019439360782 0.452194760823932 0.097610845568248 transcription elongation factor A like 7 FUNCTION: Plays a role in the negative regulation of NF-kappa-B signaling at the basal level by modulating transcriptional activity of NF-kappa-B on its target gene promoters. Associates with cyclin D1 promoter containing Myc E-box sequence and transcriptionally represses cyclin D1 expression. Regulates telomerase reverse transcriptase expression and telomerase activity in both ALT (alternative lengthening of telomeres)and telomerase-positive cell lines. {ECO:0000269|PubMed:18806825, ECO:0000269|PubMed:19966855, ECO:0000269|PubMed:20454512}.; . TISSUE SPECIFICITY: Highly expressed in normal and fetal brain tissues, and weakly expressed in uterus and ovary. Down-regulated in epithelial ovarian, cervical, prostate, breast, brain and lung cancer cell lines and in brain and ovarian tumors. {ECO:0000269|PubMed:18806825}.; unclassifiable (Anatomical System);meninges;cartilage;hypothalamus;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;prostate;optic nerve;pia mater;whole body;lung;trabecular meshwork;macula lutea;pituitary gland;testis;dura mater;brain;stomach; amygdala;whole brain;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; . . 0.12325821 62.38499646 4.86292 0.17930 TCEAL8 0.483466805907495 0.435938691485513 0.0805945026069918 transcription elongation factor A like 8 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;liver;alveolus;spleen;kidney;mammary gland;stomach; . 0.10953 0.07114 0.101211609 60.95777306 3.37831 0.12274 TCEAL8P1 . . . transcription elongation factor A like 8 pseudogene 1 . . . . . . . . . . . TCEAL9 . . . transcription elongation factor A like 9 . . . . . 0.77033 0.09614 0.057118534 57.99716914 . . TCEANC 0.0963544550376469 0.769971205129817 0.133674339832536 transcription elongation factor A N-terminal and central domain containing . . . unclassifiable (Anatomical System);cartilage;hypothalamus;fovea centralis;choroid;lens;retina;optic nerve;lung;frontal lobe;endometrium;nasopharynx;macula lutea;spleen;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; . . 0.681699246 84.93158764 84.85264 1.96225 TCEANC2 2.81297991262072e-05 0.32757001042815 0.672401859772723 transcription elongation factor A N-terminal and central domain containing 2 . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;thyroid;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;macula lutea;liver;cervix;kidney;stomach; ciliary ganglion; 0.02945 . 0.082802743 60.09082331 42.58546 1.23594 TCEB1 0.643993932413181 0.329086352759867 0.0269197148269519 transcription elongation factor B subunit 1 FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex). {ECO:0000269|PubMed:15590694}.; . TISSUE SPECIFICITY: Overexpressed in prostate cancer cell line PC- 3 and breast cancer cell line SK-BR-3. {ECO:0000269|PubMed:12004003}.; smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;pancreas;lung;pia mater;cornea;placenta;head and neck;kidney;stomach; medulla oblongata;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;pons;trigeminal ganglion;parietal lobe;skeletal muscle; . . 0.079165051 59.43029016 . . TCEB1P2 . . . transcription elongation factor B subunit 1 pseudogene 2 . . . . . . . . . . . TCEB1P3 . . . transcription elongation factor B subunit 1 pseudogene 3 . . . . . . . . . . . TCEB1P4 . . . transcription elongation factor B subunit 1 pseudogene 4 . . . . . . . . . . . TCEB1P5 . . . transcription elongation factor B subunit 1 pseudogene 5 . . . . . . . . . . . TCEB1P6 . . . transcription elongation factor B subunit 1 pseudogene 6 . . . . . . . . . . . TCEB1P7 . . . transcription elongation factor B subunit 1 pseudogene 7 . . . . . . . . . . . TCEB1P8 . . . transcription elongation factor B subunit 1 pseudogene 8 . . . . . . . . . . . TCEB1P9 . . . transcription elongation factor B subunit 1 pseudogene 9 . . . . . . . . . . . TCEB1P10 . . . transcription elongation factor B subunit 1 pseudogene 10 . . . . . . . . . . . TCEB1P11 . . . transcription elongation factor B subunit 1 pseudogene 11 . . . . . . . . . . . TCEB1P12 . . . transcription elongation factor B subunit 1 pseudogene 12 . . . . . . . . . . . TCEB1P13 . . . transcription elongation factor B subunit 1 pseudogene 13 . . . . . . . . . . . TCEB1P14 . . . transcription elongation factor B subunit 1 pseudogene 14 . . . . . . . . . . . TCEB1P15 . . . transcription elongation factor B subunit 1 pseudogene 15 . . . . . . . . . . . TCEB1P16 . . . transcription elongation factor B subunit 1 pseudogene 16 . . . . . . . . . . . TCEB1P17 . . . transcription elongation factor B subunit 1 pseudogene 17 . . . . . . . . . . . TCEB1P18 . . . transcription elongation factor B subunit 1 pseudogene 18 . . . . . . . . . . . TCEB1P19 . . . transcription elongation factor B subunit 1 pseudogene 19 . . . . . . . . . . . TCEB1P20 . . . transcription elongation factor B subunit 1 pseudogene 20 . . . . . . . . . . . TCEB1P21 . . . transcription elongation factor B subunit 1 pseudogene 21 . . . . . . . . . . . TCEB1P22 . . . transcription elongation factor B subunit 1 pseudogene 22 . . . . . . . . . . . TCEB1P23 . . . transcription elongation factor B subunit 1 pseudogene 23 . . . . . . . . . . . TCEB1P24 . . . transcription elongation factor B subunit 1 pseudogene 24 . . . . . . . . . . . TCEB1P26 . . . transcription elongation factor B subunit 1 pseudogene 26 . . . . . . . . . . . TCEB1P27 . . . transcription elongation factor B subunit 1 pseudogene 27 . . . . . . . . . . . TCEB1P28 . . . transcription elongation factor B subunit 1 pseudogene 28 . . . . . . . . . . . TCEB1P29 . . . transcription elongation factor B subunit 1 pseudogene 29 . . . . . . . . . . . TCEB1P30 . . . transcription elongation factor B subunit 1 pseudogene 30 . . . . . . . . . . . TCEB1P31 . . . transcription elongation factor B subunit 1 pseudogene 31 . . . . . . . . . . . TCEB1P32 . . . transcription elongation factor B subunit 1 pseudogene 32 . . . . . . . . . . . TCEB1P33 . . . transcription elongation factor B subunit 1 pseudogene 33 . . . . . . . . . . . TCEB1P34 . . . transcription elongation factor B subunit 1 pseudogene 34 . . . . . . . . . . . TCEB1P35 . . . transcription elongation factor B subunit 1 pseudogene 35 . . . . . . . . . . . TCEB2 0.0207842917252483 0.749832825381737 0.229382882893015 transcription elongation factor B subunit 2 FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).; . . myocardium;ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;larynx;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;hypothalamus;muscle;urinary;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;aorta; whole brain;superior cervical ganglion;testis - interstitial;thalamus;heart;testis - seminiferous tubule;fetal brain;cerebellum peduncles;liver;testis; . 0.20285 0.193034296 66.82000472 1883.70911 7.98285 TCEB2P1 . . . transcription elongation factor B subunit 2 pseudogene 1 . . . . . . . . . . . TCEB2P2 . . . transcription elongation factor B subunit 2 pseudogene 2 . . . . . . . . . . . TCEB2P3 . . . transcription elongation factor B subunit 2 pseudogene 3 . . . . . . . . . . . TCEB2P4 . . . transcription elongation factor B subunit 2 pseudogene 4 . . . . . . . . . . . TCEB3 0.999991942292927 8.05770698934881e-06 8.3910396271686e-14 transcription elongation factor B subunit 3 FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).; . . . . 0.10829 0.12651 0.958999345 90.17456947 830.58763 5.64760 TCEB3-AS1 . . . TCEB3 antisense RNA 1 . . . . . . . . . . . TCEB3B 1.80367559188731e-08 0.403556861432586 0.596443120530658 transcription elongation factor B subunit 3B FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A2 is transcriptionally active but its transcription activity is not enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex). {ECO:0000269|PubMed:10692460}.; . TISSUE SPECIFICITY: Specifically expressed in testis. {ECO:0000269|PubMed:10692460}.; testis; superior cervical ganglion;trigeminal ganglion; 0.04439 . 2.276463906 98.26020288 118.01242 2.36290 TCEB3C . . . transcription elongation factor B subunit 3C FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A3 is transcriptionally active but its transcription activity is not enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex). {ECO:0000269|PubMed:11994304}.; . TISSUE SPECIFICITY: Widely expressed.; optic nerve;macula lutea;fovea centralis;choroid;lens;brain;retina; . . 0.07073 . . 1.63837 0.05362 TCEB3CL . . . transcription elongation factor B subunit 3C like FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A3 is transcriptionally active but its transcription activity is not enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (By similarity). {ECO:0000250}.; . . . . . . . . 1.33612 0.04756 TCEB3CL2 . . . transcription elongation factor B subunit 3C like 2 FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A3 is transcriptionally active but its transcription activity is not enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (By similarity). {ECO:0000250}.; . . . . . . . . 4.81382 0.17559 TCERG1 0.999962712136281 3.72878637177864e-05 1.18845843310733e-15 transcription elongation regulator 1 FUNCTION: Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner. Necessary for TAT-dependent activation of the human immunodeficiency virus type 1 (HIV-1) promoter. {ECO:0000269|PubMed:11604498, ECO:0000269|PubMed:9315662}.; . TISSUE SPECIFICITY: Detected in brain neurons. {ECO:0000269|PubMed:11172033}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;trabecular meshwork;macula lutea;liver;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; amygdala;superior cervical ganglion;tumor; 0.94723 0.23802 -0.865195027 10.79853739 89.92295 2.04005 TCERG1L 0.000228294241632806 0.917129163255849 0.0826425425025182 transcription elongation regulator 1 like . . . . . 0.19979 0.09328 0.332586472 73.61405992 228.35077 3.26452 TCERG1L-AS1 . . . TCERG1L antisense RNA 1 . . . . . . . . . . . TCF3 0.185647143501164 0.813858528200504 0.000494328298332298 transcription factor 3 FUNCTION: Transcriptional regulator. Involved in the initiation of neuronal differentiation. Heterodimers between TCF3 and tissue- specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation. Dimers bind DNA on E- box motifs: 5'-CANNTG-3'. Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer. Binds to IEB1 and IEB2, which are short DNA sequences in the insulin gene transcription control region.; DISEASE: Note=Chromosomal aberrations involving TCF3 are cause of forms of pre-B-cell acute lymphoblastic leukemia (B-ALL). Translocation t(1;19)(q23;p13.3) with PBX1. TCF3-PBX1 transforms cells by constitutively activating transcription of genes regulated by PBX1 or by other members of the PBX protein family (PubMed:1967983, PubMed:1671560). Translocation t(17;19)(q22;p13.3) with HLF (PubMed:1386162). Inversion inv(19)(p13;q13) with TFPT (PubMed:10086727). {ECO:0000269|PubMed:10086727, ECO:0000269|PubMed:1386162, ECO:0000269|PubMed:1671560, ECO:0000269|PubMed:1967983}.; . lymphoreticular;ovary;skin;retina;prostate;optic nerve;endometrium;cochlea;iris;germinal center;brain;bladder;tonsil;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;tumor;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; 0.85250 0.49369 -0.075375604 47.26350554 1035.94021 6.18027 TCF3P1 . . . transcription factor 3 pseudogene 1 . . . . . . . . . . . TCF4 0.999866544499818 0.000133455484348715 1.58330671936537e-11 transcription factor 4 FUNCTION: Transcription factor that binds to the immunoglobulin enchancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcription (By similarity). Preferentially binds to either 5'-ACANNTGT-3' or 5'-CCANNTGG-3'. {ECO:0000250}.; DISEASE: Pitt-Hopkins syndrome (PTHS) [MIM:610954]: A syndrome characterized by mental retardation, wide mouth and distinctive facial features, and intermittent hyperventilation followed by apnea. Features include intellectual disability with severe speech impairment, normal growth parameters at birth, postnatal microcephaly, breathing anomalies, severe motor developmental delay, motor incoordination, ocular anomalies, constipation, seizures, typical behavior and subtle brain abnormalities. {ECO:0000269|PubMed:17436254, ECO:0000269|PubMed:17436255, ECO:0000269|PubMed:18728071, ECO:0000269|PubMed:19235238, ECO:0000269|PubMed:20184619, ECO:0000269|PubMed:22045651}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, Fuchs endothelial, 3 (FECD3) [MIM:613267]: A late-onset form of Fuchs endothelial corneal dystrophy, a disease caused by loss of endothelium of the central cornea. It is characterized by focal wart-like guttata that arise from Descemet membrane and develop in the central cornea, epithelial blisters, reduced vision and pain. Descemet membrane is thickened by abnormal collagenous deposition. {ECO:0000269|PubMed:24255041, ECO:0000269|PubMed:25168903, ECO:0000269|PubMed:25593321}. Note=The disease is caused by mutations affecting the gene represented in this entry. Causative mutations are heterozygous TCF4 intronic trinucleotide repeat expansions (CTG)n. {ECO:0000269|PubMed:24255041, ECO:0000269|PubMed:25168903, ECO:0000269|PubMed:25593321}.; TISSUE SPECIFICITY: Expressed in adult heart, brain, placenta, skeletal muscle and to a lesser extent in the lung. In developing embryonic tissues, expression mostly occurs in the brain.; ovary;developmental;vein;skin;retina;uterus;whole body;frontal lobe;larynx;bone;testis;germinal center;spinal ganglion;ciliary body;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;skeletal muscle;lung;nasopharynx;placenta;liver;spleen;head and neck;kidney; amygdala;superior cervical ganglion;occipital lobe;cerebellum peduncles;pons;atrioventricular node;skeletal muscle;uterus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.97117 0.29560 -0.558357437 19.54470394 19.31829 0.66532 TCF4-AS1 . . . TCF4 antisense RNA 1 . . . . . . . . . . . TCF4-AS2 . . . TCF4 antisense RNA 2 . . . . . . . . . . . TCF7 0.361554570284009 0.635903501620408 0.00254192809558274 transcription factor 7 (T-cell specific, HMG-box) FUNCTION: Transcriptional activator involved in T-cell lymphocyte differentiation. Necessary for the survival of CD4(+) CD8(+) immature thymocytes. Isoforms lacking the N-terminal CTNNB1 binding domain cannot fulfill this role. Binds to the T- lymphocyte-specific enhancer element (5'-WWCAAAG-3') found in the promoter of the CD3E gene. May also act as feedback transcriptional repressor of CTNNB1 and TCF7L2 target genes. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by TCF7 and CTNNB1.; . TISSUE SPECIFICITY: Predominantly expressed in T-cells. Also detected in proliferating intestinal epithelial cells and in the basal epithelial cells of mammary gland epithelium. {ECO:0000269|PubMed:10489374}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;pineal body;adrenal cortex;colon;parathyroid;blood;skin;breast;uterus;pancreas;optic nerve;endometrium;adrenal gland;epididymis;bone;thyroid;placenta;liver;germinal center;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;trigeminal ganglion;thymus; 0.17623 . 0.110306132 62.00165133 252.5837 3.41983 TCF7L1 0.753752010042604 0.246160275351726 8.77146056699348e-05 transcription factor 7 like 1 FUNCTION: Participates in the Wnt signaling pathway. Binds to DNA and acts as a repressor in the absence of CTNNB1, and as an activator in its presence. Necessary for the terminal differentiation of epidermal cells, the formation of keratohyalin granules and the development of the barrier function of the epidermis (By similarity). Down-regulates NQO1, leading to increased mitomycin c resistance. {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in hair follicles and skin keratinocytes, and at lower levels in stomach epithelium. {ECO:0000269|PubMed:9916915}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.76136 0.17789 7.61E-05 53.98089172 3367.43078 11.10912 TCF7L1-IT1 . . . TCF7L1 intronic transcript 1 . . . . . . . . . . . TCF7L2 0.98960502908944 0.0103949442716789 2.6638881347716e-08 transcription factor 7 like 2 FUNCTION: Participates in the Wnt signaling pathway and modulates MYC expression by binding to its promoter in a sequence-specific manner. Acts as repressor in the absence of CTNNB1, and as activator in its presence. Activates transcription from promoters with several copies of the Tcf motif 5'-CCTTTGATC-3' in the presence of CTNNB1. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by TCF7L2/TCF4 and CTNNB1. Expression of dominant-negative mutants results in cell-cycle arrest in G1. Necessary for the maintenance of the epithelial stem-cell compartment of the small intestine. {ECO:0000269|PubMed:12408868, ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:19443654, ECO:0000269|PubMed:22699938, ECO:0000269|PubMed:9727977}.; DISEASE: Note=Constitutive activation and subsequent transactivation of target genes may lead to the maintenance of stem-cell characteristics (cycling and longevity) in cells that should normally undergo terminal differentiation and constitute the primary transforming event in colorectal cancer (CRC).; DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:16415884, ECO:0000269|PubMed:24390345}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in epithelium from small intestine, with the highest expression at the top of the crypts and a gradient of expression from crypt to villus. Detected in colon epithelium and colon cancer, and in epithelium from mammary gland and carcinomas derived therefrom. {ECO:0000269|PubMed:9916915}.; ovary;salivary gland;rectum;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;thyroid;testis;spinal ganglion;brain;bladder;amygdala;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion;thalamus;hypothalamus;trigeminal ganglion;cingulate cortex; 0.48964 0.48507 -0.222203495 37.54423213 1070.45038 6.27341 TCF12 0.973899934245985 0.0261000138175462 5.1936469217086e-08 transcription factor 12 FUNCTION: Transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3').; DISEASE: Craniosynostosis 3 (CRS3) [MIM:615314]: A primary abnormality of skull growth involving premature fusion of one or more cranial sutures. The growth velocity of the skull often cannot match that of the developing brain resulting in an abnormal head shape and, in some cases, increased intracranial pressure, which must be treated promptly to avoid permanent neurodevelopmental disability. {ECO:0000269|PubMed:23354436, ECO:0000269|PubMed:25271085}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in several tissues and cell types including skeletal muscle, thymus, and a B-cell line.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;stomach;aorta; dorsal root ganglion;uterus;amygdala;superior cervical ganglion;spinal cord;globus pallidus;ciliary ganglion;caudate nucleus;atrioventricular node;trigeminal ganglion; 0.74130 0.18974 -0.709045403 14.673272 248.01793 3.39501 TCF15 0.551527504830997 0.395762504652046 0.0527099905169572 transcription factor 15 (basic helix-loop-helix) FUNCTION: May function as an early transcriptional regulator, involved in the patterning of the mesoderm and in lineage determination of cell types derived from the mesoderm.; . . unclassifiable (Anatomical System);uterus;lung;whole body;ovary;heart;placenta;testis;parathyroid;blood;skin;retina; subthalamic nucleus;adrenal cortex;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; . 0.15900 . . 178.93275 2.90673 TCF19 0.000232743975557081 0.753570355666408 0.246196900358035 transcription factor 19 FUNCTION: Potential trans-activating factor that could play an important role in the transcription of genes required for the later stages of cell cycle progression.; . . . . 0.20092 . 0.815800671 87.8744987 493.99062 4.57031 TCF20 0.999977934276122 2.20657238381141e-05 3.99667288814921e-14 transcription factor 20 (AR1) FUNCTION: Transcriptional activator that binds to the regulatory region of MMP3 and thereby controls stromelysin expression. It stimulates the activity of various transcriptional activators such as JUN, SP1, PAX6 and ETS1, suggesting a function as a coactivator.; . TISSUE SPECIFICITY: Expressed in most tissues, except in ovary and prostate. Isoform 1 is exclusively expressed in brain, heart and testis, and this form predominates in liver and kidney. Isoform 2 predominates in lung.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;urinary;blood;lens;breast;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node; 0.33163 0.19448 -2.552652857 0.8492569 1856.84901 7.94395 TCF21 0.80536994429277 0.189537107862187 0.00509294784504338 transcription factor 21 FUNCTION: Involved in epithelial-mesenchymal interactions in kidney and lung morphogenesis that include epithelial differentiation and branching morphogenesis. May play a role in the specification or differentiation of one or more subsets of epicardial cell types.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;skin;uterus;pancreas;prostate;lung;synovium;epididymis;placenta;liver;testis;spleen;kidney;stomach; heart;placenta;fetal lung;kidney; 0.50048 0.24689 0.25917371 70.05779665 477.84739 4.51344 TCF23 0.000503312310069814 0.445941051143257 0.553555636546674 transcription factor 23 FUNCTION: Inhibits E-box-mediated binding and transactivation of bHLH factors. Inhibitory effect is similar to that of ID proteins. Inhibits the formation of TCF3 and MYOD1 homodimers and heterodimers. Lacks DNA binding activity. Seems to play a role in the inhibition of myogenesis (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in liver, kidney and spleen. {ECO:0000269|PubMed:14516699}.; . . 0.58181 0.12294 0.17280645 65.75843359 51.73986 1.42105 TCF24 . . . transcription factor 24 FUNCTION: Putative transcription factor. {ECO:0000250}.; . . . . 0.08249 . . . 193.60685 3.01919 TCF25 0.0517782774404855 0.948038126752383 0.000183595807131344 transcription factor 25 (basic helix-loop-helix) FUNCTION: May play a role in cell death control. Acts as a transcriptional repressor. Has been shown to repress transcription of SRF in vitro and so may play a role in heart development. {ECO:0000269|PubMed:16574069}.; . TISSUE SPECIFICITY: In the embryo, widely expressed with highest levels in brain. In the adult, highest expression is found in the heart. {ECO:0000269|PubMed:16574069}.; myocardium;lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;amniotic fluid;germinal center;brain;tonsil;heart;cartilage;pineal body;urinary;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;oesophagus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;trophoblast;epidermis;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;placenta;hippocampus;duodenum;amnion;head and neck;kidney;stomach;cerebellum;thymus; whole brain;subthalamic nucleus;thalamus;superior cervical ganglion;temporal lobe;globus pallidus;pons;caudate nucleus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.20448 . -1.083859071 7.195093182 551.55626 4.77677 TCFL5 0.95806915495759 0.0419105016012623 2.0343441147383e-05 transcription factor-like 5 (basic helix-loop-helix) FUNCTION: Putative transcription factor. Isoform 3 may play a role in early spermatogenesis. {ECO:0000269|PubMed:9763657}.; . TISSUE SPECIFICITY: Isoform 3 is testis specific. Isoform 2 is pancreas specific. {ECO:0000269|PubMed:9763657}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;thyroid;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;head and neck;kidney;mammary gland;stomach; whole brain;amygdala;medulla oblongata;testis - interstitial;testis - seminiferous tubule;spinal cord;prefrontal cortex;testis;cingulate cortex; 0.06503 . . . 1118.72839 6.38595 TCHH 3.87496343902758e-23 0.7842561464839 0.215743853516101 trichohyalin FUNCTION: Intermediate filament-associated protein that associates in regular arrays with keratin intermediate filaments (KIF) of the inner root sheath cells of the hair follicle and the granular layer of the epidermis. It later becomes cross-linked to KIF by isodipeptide bonds. It may serve as scaffold protein, together with involucrin, in the organization of the cell envelope or even anchor the cell envelope to the KIF network. It may be involved in its own calcium-dependent postsynthetic processing during terminal differentiation.; . TISSUE SPECIFICITY: Found in the hard keratinizing tissues such as the inner root sheath (IRS) of hair follicles and medulla, and in the filiform papillae of dorsal tongue epithelium.; . . 0.15914 . 1.539633859 95.5826846 1567.51565 7.32616 TCHHL1 2.23453010094714e-08 0.259656977301445 0.740343000353254 trichohyalin like 1 . . . . . 0.03818 0.05493 0.159856957 64.91507431 840.61264 5.67869 TCHP 6.99625064835171e-12 0.391531140724334 0.60846885926867 trichoplein keratin filament binding FUNCTION: Tumor suppressor which has the ability to inhibit cell growth and be pro-apoptotic during cell stress. Inhibits cell growth in bladder and prostate cancer cells by a down-regulation of HSPB1 by inhibiting its phosphorylation. May act as a 'capping' or 'branching' protein for keratin filaments in the cell periphery. May regulate K8/K18 filament and desmosome organization mainly at the apical or peripheral regions of simple epithelial cells (PubMed:15731013, PubMed:18931701). Is a negative regulator of ciliogenesis (PubMed:25270598). {ECO:0000269|PubMed:15731013, ECO:0000269|PubMed:18931701, ECO:0000269|PubMed:25270598}.; . TISSUE SPECIFICITY: Expressed at high levels in normal urothelial and breast epithelial cells. Also expressed in the smooth muscle and endothelial cells. Reduced expression seen in advanced bladder and breast carcinomas (at protein level). Ubiquitous. Expressed at highest levels in the heart, skeletal muscle, kidney, liver and testis. {ECO:0000269|PubMed:18931701}.; colon;fovea centralis;choroid;skin;retina;bone marrow;optic nerve;frontal lobe;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);trophoblast;cartilage;islets of Langerhans;muscle;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach; . 0.11235 0.55942 -0.486758915 22.69992923 1889.18206 7.99263 TCIRG1 6.03647247019708e-06 0.993715861034599 0.00627810249293039 T-cell immune regulator 1, ATPase H+ transporting V0 subunit a3 FUNCTION: Part of the proton channel of V-ATPases (By similarity). Seems to be directly involved in T-cell activation. {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform long is highly expressed in osteoclastomas. Isoform short is highly expressed in thymus.; ovary;colon;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;alveolus;spleen;head and neck;cervix;stomach; pancreas;adrenal gland;adrenal cortex;liver;white blood cells;whole blood; 0.22442 0.38558 -1.124330456 6.575843359 484.54582 4.53294 TCL1A 0.0012233048337285 0.634153012424268 0.364623682742003 T-cell leukemia/lymphoma 1A FUNCTION: Enhances the phosphorylation and activation of AKT1, AKT2 and AKT3. Promotes nuclear translocation of AKT1. Enhances cell proliferation, stabilizes mitochondrial membrane potential and promotes cell survival. {ECO:0000269|PubMed:10716693, ECO:0000269|PubMed:10983986, ECO:0000269|PubMed:11707444, ECO:0000269|PubMed:11839817}.; . TISSUE SPECIFICITY: Restricted in the T-cell lineage to immature thymocytes and activated peripheral lymphocytes. Preferentially expressed early in T- and B-lymphocyte differentiation.; . . 0.04542 0.16759 0.503505267 79.88912479 79.52834 1.88479 TCL1B 0.00468673143485725 0.682288130317118 0.313025138248024 T-cell leukemia/lymphoma 1B FUNCTION: Enhances the phosphorylation and activation of AKT1 and AKT2. {ECO:0000269|PubMed:10983986}.; . TISSUE SPECIFICITY: Expressed in a variety of tissues including placenta and testis. {ECO:0000269|PubMed:10077617, ECO:0000269|PubMed:10344735}.; unclassifiable (Anatomical System);breast;lymph node;lung;placenta;testis;kidney;germinal center; . . 0.09201 0.813985927 87.81552253 2610.88106 9.56670 TCL4 . . . T-cell leukemia/lymphoma 4 . . . . . . . . . . . TCL6 . . . T-cell leukemia/lymphoma 6 (non-protein coding) . . . unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;skin;uterus;breast;lung;larynx;placenta;liver;testis;germinal center;kidney; dorsal root ganglion;superior cervical ganglion;pons;atrioventricular node;skeletal muscle;skin;uterus corpus;placenta;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.30457 . . . . . TCN1 3.85562988627718e-16 0.000769038400430313 0.999230961599569 transcobalamin 1 FUNCTION: Binds vitamin B12 with femtomolar affinity and protects it from the acidic environment of the stomach.; . TISSUE SPECIFICITY: Produced by the salivary glands of the oral cavity, in response to ingestion of food. Major constituent of secondary granules in neutrophils. {ECO:0000269|PubMed:2777761}.; unclassifiable (Anatomical System);heart;lacrimal gland;adrenal cortex;colon;parathyroid;blood;skeletal muscle;bone marrow;breast;uterus;pancreas;prostate;lung;endometrium;adrenal gland;nasopharynx;thyroid;liver;head and neck;kidney;pineal gland;stomach; dorsal root ganglion;superior cervical ganglion;trachea;salivary gland;ciliary ganglion;atrioventricular node;skeletal muscle;bone marrow; 0.02915 0.14478 -0.044015879 50.44821892 519.08775 4.65444 TCN2 0.0222895531737769 0.974456378145986 0.00325406868023687 transcobalamin 2 FUNCTION: Primary vitamin B12-binding and transport protein. Delivers cobalamin to cells.; DISEASE: Transcobalamin II deficiency (TCN2 deficiency) [MIM:275350]: Results in various forms of anemia. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;iris;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.21133 0.56503 1.934667198 97.487615 1919.33765 8.06455 TCOF1 0.765232862711561 0.234767111348379 2.59400602069905e-08 treacle ribosome biogenesis factor 1 FUNCTION: May be involved in nucleolar-cytoplasmic transport. May play a fundamental role in early embryonic development, particularly in development of the craniofacial complex (By similarity). May participate in certain stages of ribosome biogenesis. {ECO:0000250, ECO:0000269|PubMed:12777385}.; DISEASE: Treacher Collins syndrome 1 (TCS1) [MIM:154500]: A form of Treacher Collins syndrome, a disorder of craniofacial development. Treacher Collins syndrome is characterized by a combination of bilateral downward slanting of the palpebral fissures, colobomas of the lower eyelids with a paucity of eyelashes medial to the defect, hypoplasia of the facial bones, cleft palate, malformation of the external ears, atresia of the external auditory canals, and bilateral conductive hearing loss. {ECO:0000269|PubMed:9042910}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;adrenal cortex;blood;lens;skeletal muscle;breast;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion;pons;parietal lobe;cerebellum; 0.11725 0.19531 0.466523353 78.69780609 3192.10978 10.76481 TCP1 0.989085751892209 0.0109135150130091 7.33094782190821e-07 t-complex 1 FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. {ECO:0000269|PubMed:20080638}.; . . . . 0.35916 0.65641 -0.358119787 29.16371786 64.99367 1.65681 TCP1P1 . . . t-complex 1 pseudogene 1 . . . . . . . . . . . TCP1P2 . . . t-complex 1 pseudogene 2 . . . . . . . . . . . TCP1P3 . . . t-complex 1 pseudogene 3 . . . . . . . . . . . TCP10 0.264645828671827 0.729789885714119 0.00556428561405424 t-complex 10 . . . . . . . 2.706654586 98.92663364 1045.84087 6.20615 TCP10L 0.00191361363927237 0.728871877410251 0.269214508950476 t-complex 10-like FUNCTION: May be involved in transcriptional regulation. Has in vitro transcription inhibition activity. Acts as a tumor suppressor in hepatocellular carcinoma (HCC) cells. {ECO:0000269|PubMed:14586771, ECO:0000269|PubMed:24565846}.; . TISSUE SPECIFICITY: Expressed in liver and testis. Expressed in the seminiferous tubules (at protein level). {ECO:0000269|PubMed:14586771, ECO:0000269|PubMed:15910542}.; unclassifiable (Anatomical System);medulla oblongata;lung;visual apparatus;liver;testis;spleen;germinal center;brain; . 0.03738 0.05353 0.150760231 64.51403633 387.33664 4.14529 TCP10L2 0.694467188174552 0.304712842159099 0.000819969666348686 t-complex 10-like 2 . . . unclassifiable (Anatomical System);lung;ovary;testis;colon;kidney; superior cervical ganglion;globus pallidus;appendix;pons;trigeminal ganglion; 0.03738 . . . 1365.19295 6.93081 TCP11 4.00945484653237e-05 0.837219185133146 0.162740720318388 t-complex 11 FUNCTION: May play an important role in sperm function and fertility. {ECO:0000269|PubMed:11756566}.; . TISSUE SPECIFICITY: Expressed only in fertile adult testis. {ECO:0000269|PubMed:11756566}.; unclassifiable (Anatomical System);medulla oblongata;hippocampus;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion; 0.09877 0.08727 0.553050905 81.54635527 1109.5614 6.36859 TCP11L1 0.0880469871522841 0.910059037310765 0.0018939755369506 t-complex 11 like 1 . . . ovary;sympathetic chain;colon;parathyroid;choroid;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;spinal ganglion;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;breast;lung;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;appendix;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.20571 0.10317 0.507139401 80.10143902 554.09311 4.78344 TCP11L2 7.48808798072002e-07 0.718280503414728 0.281718747776474 t-complex 11 like 2 . . . unclassifiable (Anatomical System);uterus;prostate;lung;hypothalamus;placenta;liver;blood;brain;stomach;tonsil;bone marrow; superior cervical ganglion;trigeminal ganglion; 0.14553 . 0.044168103 57.40740741 244.09278 3.37130 TCP11X1 . . . t-complex 11 family, X-linked 1 . . . . . . . . . . . TCP11X2 . . . t-complex 11 family, X-linked 2 . . . . . 0.12120 . . . . . TCP11X3P . . . t-complex 11 family, X-linked 3, pseudogene . . . . . . . . . . . TCTA 0.0132648475524679 0.662929242251184 0.323805910196348 T-cell leukemia translocation altered FUNCTION: May be required for cellular fusion during osteoclastogenesis. {ECO:0000269|PubMed:19560569}.; . TISSUE SPECIFICITY: Ubiquitous. Highest level of expression in kidney. Present in monocytes, osteoclasts, macrophages, synoviocytes and synovial lining cells (at protein level). {ECO:0000269|PubMed:7728759}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex;parietal lobe;cerebellum; 0.45915 0.14054 0.125076652 62.7388535 60.15521 1.57466 TCTE1 3.26370848659523e-07 0.326711605637384 0.673288067991767 t-complex-associated-testis-expressed 1 . . . . . 0.18496 0.12497 0.846940207 88.47605567 2066.76849 8.37700 TCTE3 0.00321873255866745 0.824494943575408 0.172286323865924 t-complex-associated-testis-expressed 3 FUNCTION: May be an accessory component of axonemal dynein and cytoplasmic dynein 1. Candidate for involvement in male sterility (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed predominantly in testis. Also expressed in brain, lung and trachea. {ECO:0000269|PubMed:11278908, ECO:0000269|PubMed:12584439}.; . . 0.03899 0.06827 0.238945317 69.20853975 2143.3607 8.51676 TCTEX1D1 0.00642468214043671 0.746116841614547 0.247458476245016 Tctex1 domain containing 1 . . . unclassifiable (Anatomical System);myocardium;lung;whole body;placenta;liver;testis;brain;skin; . 0.05951 . 0.43736446 77.56546355 2934.39279 10.27215 TCTEX1D2 0.000234712184365325 0.51780765811976 0.481957629695875 Tctex1 domain containing 2 . . . unclassifiable (Anatomical System);lymph node;ovary;heart;salivary gland;intestine;pharynx;colon;parathyroid;blood;skin;retina;prostate;whole body;lung;cornea;endometrium;placenta;visual apparatus;alveolus;liver;testis;kidney;brain;mammary gland;bladder; . 0.20168 . 0.281220278 71.07808445 16.93001 0.59651 TCTEX1D4 0.208823533681892 0.648142080497891 0.143034385820217 Tctex1 domain containing 4 . . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:16982625}.; lung;placenta; . 0.26961 0.09979 . . 57.58689 1.53180 TCTN1 1.86861398243824e-09 0.395855334579587 0.604144663551799 tectonic family member 1 FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Regulator of Hedgehog (Hh), required for both activation and inhibition of the Hh pathway in the patterning of the neural tube. During neural tube development, it is required for formation of the most ventral cell types and for full Hh pathway activation. Functions in Hh signal transduction to fully activate the pathway in the presence of high Hh levels and to repress the pathway in the absence of Hh signals. Modulates Hh signal transduction downstream of SMO and RAB23 (By similarity). {ECO:0000250}.; DISEASE: Joubert syndrome 13 (JBTS13) [MIM:614173]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. {ECO:0000269|PubMed:21725307}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.14398 . 0.176444282 66.07100731 178.0036 2.90024 TCTN2 1.97172300054813e-05 0.998818458432271 0.00116182433772355 tectonic family member 2 FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for hedgehog signaling transduction (By similarity). {ECO:0000250}.; DISEASE: Meckel syndrome 8 (MKS8) [MIM:613885]: A disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly. {ECO:0000269|PubMed:21462283}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Joubert syndrome 24 (JBTS24) [MIM:616654]: A form of Joubert syndrome, a disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy, renal disease, liver fibrosis, and polydactyly. {ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:25118024}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;colon;skeletal muscle;uterus;breast;lung;frontal lobe;larynx;bone;placenta;thyroid;liver;head and neck;kidney;brain;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;tongue;pons;atrioventricular node;skeletal muscle;skin;subthalamic nucleus;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.07731 . -0.819281839 11.93677754 61.90105 1.60380 TCTN3 6.43975615999618e-08 0.434000445432422 0.565999490170016 tectonic family member 3 FUNCTION: Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition (By similarity). May be involved in apoptosis regulation. Necessary for signal transduction through the sonic hedgehog (Shh) signaling pathway. {ECO:0000250, ECO:0000269|PubMed:17464193, ECO:0000269|PubMed:22883145}.; DISEASE: Orofaciodigital syndrome 4 (OFD4) [MIM:258860]: A form of orofaciodigital syndrome, a group of heterogeneous disorders characterized by malformations of the oral cavity, face and digits, and associated phenotypic abnormalities that lead to the delineation of various subtypes. OFD4 patients have tongue nodules, multiple frenulae, broad flat nose, hypertelorism, and short rib polydactyly with tibial dysplasia (Majewski syndrome). The presence of severe tibial aplasia differentiates OFD4 from OFD1. Additional features of cystic dysplastic kidneys and brain malformation, including occipital encephalocele, are observed in severely affected patients. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Joubert syndrome 18 (JBTS18) [MIM:614815]: A form of Joubert syndrome, a disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. JBTS18 patients have vermis agenesis and the molar tooth sign as well as severe kyphoscoliosis. Other features include intrauterine growth retardation, oral anomalies, micrognathism, polydactyly and camptodactyly, joint laxity, horseshoe kidney, and ventricular septal defect. {ECO:0000269|PubMed:22883145}. Note=The disease is caused by mutations affecting the gene represented in this entry. TCTN3-mutated fibroblasts from JBTS18 patients fail to respond to Shh agonists suggesting that at least some of the defects in affected individuals may be secondary to reduced Shh signaling (PubMed:22883145). {ECO:0000269|PubMed:22883145}.; . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;medulla oblongata;atrioventricular node;pons;skeletal muscle;adrenal gland;testis;ciliary ganglion;kidney;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.13797 0.08668 0.242582624 69.45623968 528.76515 4.69222 TDG 0.000922352403038787 0.985806611057942 0.0132710365390191 thymine DNA glycosylase FUNCTION: DNA glycosylase that plays a key role in active DNA demethylation: specifically recognizes and binds 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC) in the context of CpG sites and mediates their excision through base-excision repair (BER) to install an unmethylated cytosine. Cannot remove 5- hydroxymethylcytosine (5hmC). According to an alternative model, involved in DNA demethylation by mediating DNA glycolase activity toward 5-hydroxymethyluracil (5hmU) produced by deamination of 5hmC. Also involved in DNA repair by acting as a thymine-DNA glycosylase that mediates correction of G/T mispairs to G/C pairs: in the DNA of higher eukaryotes, hydrolytic deamination of 5- methylcytosine to thymine leads to the formation of G/T mismatches. Its role in the repair of canonical base damage is however minor compared to its role in DNA demethylation. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar- phosphate backbone of the DNA and a mispaired thymine. In addition to the G/T, it can remove thymine also from C/T and T/T mispairs in the order G/T >> C/T > T/T. It has no detectable activity on apyrimidinic sites and does not catalyze the removal of thymine from A/T pairs or from single-stranded DNA. It can also remove uracil and 5-bromouracil from mispairs with guanine. {ECO:0000269|PubMed:21862836, ECO:0000269|PubMed:22327402, ECO:0000269|PubMed:22573813, ECO:0000269|PubMed:22962365, ECO:0000269|PubMed:8127859, ECO:0000269|PubMed:8407958, ECO:0000269|PubMed:8662714}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;gum;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;urinary;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;hypopharynx;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.38796 0.15236 0.128714042 63.19886766 4804.42141 14.04834 TDGF1 3.98298058552725e-06 0.212748141984906 0.787247875034508 teratocarcinoma-derived growth factor 1 FUNCTION: Could play a role in the determination of the epiblastic cells that subsequently give rise to the mesoderm. {ECO:0000269|PubMed:11909953}.; . TISSUE SPECIFICITY: Preferentially expressed in gastric and colorectal carcinomas than in their normal counterparts. Expressed in breast and lung. {ECO:0000269|PubMed:18835250}.; unclassifiable (Anatomical System);trophoblast;lung;hypothalamus;testis;colon;kidney;brain;skeletal muscle;stomach; . . 0.56496 0.238945317 69.20853975 351.82952 3.97563 TDGF1P1 . . . teratocarcinoma-derived growth factor 1 pseudogene 1 . . . . . . . . . . . TDGF1P2 . . . teratocarcinoma-derived growth factor 1 pseudogene 2 . . . . . . . . . . . TDGF1P3 . . . teratocarcinoma-derived growth factor 1 pseudogene 3 FUNCTION: Could play a role in the determination of the epiblastic cells that subsequently give rise to the mesoderm. Activates the Nodal-dependent signaling pathway. {ECO:0000269|PubMed:18835250}.; . TISSUE SPECIFICITY: Expressed weakly in lung, colon and breast. Expressed also strongly in primary cancer tissues; lung and colon cancers. {ECO:0000269|PubMed:18835250}.; . . . 0.56496 . . . . TDGF1P4 . . . teratocarcinoma-derived growth factor 1 pseudogene 4 . . . . . . . . . . . TDGF1P5 . . . teratocarcinoma-derived growth factor 1 pseudogene 5 . . . . . . . . . . . TDGF1P6 . . . teratocarcinoma-derived growth factor 1 pseudogene 6 . . . . . . . . . . . TDGF1P7 . . . teratocarcinoma-derived growth factor 1 pseudogene 7 . . . . . . . . . . . TDGP1 . . . thymine-DNA glycosylase pseudogene 1 . . . . . . . . . . . TDH . . . L-threonine dehydrogenase (pseudogene) . . TISSUE SPECIFICITY: Expressed in all tissues examined. Detected in most cell types examined, but not observed in endothelial cells, glioma cell lines and some leukemia cell lines. {ECO:0000269|PubMed:12361482}.; unclassifiable (Anatomical System); globus pallidus;ciliary ganglion; 0.18295 0.09612 . . . . TDO2 1.52467035320059e-08 0.598612238744438 0.401387746008859 tryptophan 2,3-dioxygenase FUNCTION: Incorporates oxygen into the indole moiety of tryptophan. Has a broad specificity towards tryptamine and derivatives including D- and L-tryptophan, 5-hydroxytryptophan and serotonin (By similarity). {ECO:0000250}.; . . . . 0.10196 0.35908 -0.003562597 53.72729417 128.49596 2.47020 TDP1 1.11209643921476e-11 0.285257432821538 0.714742567167341 tyrosyl-DNA phosphodiesterase 1 FUNCTION: DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 3'-phosphodiester bond, giving rise to DNA with a free 3' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase I active site tyrosine residue. Hydrolyzes 3'-phosphoglycolates on protruding 3' ends on DNA double-strand breaks due to DNA damage by radiation and free radicals. Acts on blunt-ended double-strand DNA breaks and on single-stranded DNA. Has low 3'exonuclease activity and can remove a single nucleoside from the 3'end of DNA and RNA molecules with 3'hydroxyl groups. Has no exonuclease activity towards DNA or RNA with a 3'phosphate. {ECO:0000269|PubMed:12023295, ECO:0000269|PubMed:15111055, ECO:0000269|PubMed:15811850, ECO:0000269|PubMed:16141202, ECO:0000269|PubMed:22822062}.; DISEASE: Spinocerebellar ataxia, autosomal recessive, with axonal neuropathy (SCAN1) [MIM:607250]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAN1 is an autosomal recessive cerebellar ataxia (ARCA) associated with peripheral axonal motor and sensory neuropathy, distal muscular atrophy, pes cavus and steppage gait as seen in Charcot-Marie-Tooth neuropathy. All affected individuals have normal intelligence. {ECO:0000269|PubMed:12244316}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. Similar expression throughout the central nervous system (whole brain, amygdala, caudate nucleus, cerebellum, cerebral cortex, frontal lobe, hippocampus, medulla oblongata, occipital lobe, putamen, substantia nigra, temporal lobe, thalamus, nucleus accumbens and spinal cord) and increased expression in testis and thymus. {ECO:0000269|PubMed:12244316, ECO:0000269|PubMed:17948061}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;oral cavity;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.22297 0.13062 -0.506987379 21.76810569 109.33346 2.27166 TDP2 0.000137008141135578 0.960870954193729 0.0389920376651359 tyrosyl-DNA phosphodiesterase 2 FUNCTION: DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. Hydrolyzes 5'- phosphoglycolates on protruding 5' ends on DNA double-strand breaks (DSBs) due to DNA damage by radiation and free radicals. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation. Has preference for single-stranded DNA or duplex DNA with a 4 base pair overhang as substrate. Has also 3'- tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. Constitutes the major if not only 5'- tyrosyl-DNA phosphodiesterase in cells. Also acts as a 5'-tyrosyl- RNA phosphodiesterase following picornavirus infection: its activity is hijacked by picornavirus and acts by specifically cleaving the protein-RNA covalent linkage generated during the viral genomic RNA replication steps of a picornavirus infection, without impairing the integrity of viral RNA. Also acts as an adapter by participating in the specific activation of MAP3K7/TAK1 in response to TGF-beta: associates with components of the TGF- beta receptor-TRAF6-TAK1 signaling module and promotes their ubiquitination dependent complex formation. Involved in non- canonical TGF-beta induced signaling routes. May also act as a negative regulator of ETS1 and may inhibit NF-kappa-B activation. Acts as a regulator of ribosome biogenesis following stress. {ECO:0000269|PubMed:19794497, ECO:0000269|PubMed:21030584, ECO:0000269|PubMed:21921940, ECO:0000269|PubMed:21980489, ECO:0000269|PubMed:22405347, ECO:0000269|PubMed:22822062, ECO:0000269|PubMed:22908287}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10764746}.; lymphoreticular;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;atrium;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;breast;pancreas;lung;adrenal gland;epididymis;placenta;alveolus;liver;cervix;head and neck;kidney;aorta;stomach;cerebellum;thymus; amygdala;prostate;subthalamic nucleus;medulla oblongata;prefrontal cortex;ciliary ganglion;whole blood;trigeminal ganglion;cingulate cortex; 0.82591 0.12207 1.039913547 91.25973107 2341.47191 8.96523 TDRD1 0.999760761518604 0.000239238480852565 5.43718936456284e-13 tudor domain containing 1 FUNCTION: Plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Required for the localization of Piwi proteins to the meiotic nuage. Involved in the piRNA metabolic process by ensuring the entry of correct transcripts into the normal piRNA pool and limiting the entry of cellular transcripts into the piRNA pathway. May act by allowing the recruitment of piRNA biogenesis or loading factors that ensure the correct entry of transcripts and piRNAs into Piwi proteins (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis and ovary specific. Also expressed in several cancers. {ECO:0000269|PubMed:12704671}.; ovary;salivary gland;pharynx;colon;blood;breast;pancreas;prostate;lung;visual apparatus;liver;testis;kidney;brain;bladder; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07128 0.09269 -0.523584927 20.93654164 132.71871 2.50564 TDRD3 0.000211829294720341 0.998849636491935 0.000938534213344163 tudor domain containing 3 FUNCTION: Scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In nucleus, acts as a coactivator: recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine- methylated loci. In cytoplasm, may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins. {ECO:0000269|PubMed:15955813, ECO:0000269|PubMed:18632687, ECO:0000269|PubMed:21172665}.; . TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:18664458}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;lens;bile duct;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;kidney;aorta;stomach; superior cervical ganglion;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.07545 0.09916 -0.424258538 25.56027365 1021.25015 6.14905 TDRD5 0.975818615175016 0.0241813830644005 1.76058355850967e-09 tudor domain containing 5 FUNCTION: Required during spermiogenesis to participate in the repression transposable elements and prevent their mobilization, which is essential for the germline integrity. Probably acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Required for chromatoid body (CB) assembly (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;testis;colon; . 0.07961 . 0.694433477 85.28544468 4678.47074 13.78041 TDRD6 6.46494143305785e-23 0.00146232001505574 0.998537679984944 tudor domain containing 6 FUNCTION: Involved in spermiogenesis, chromatoid body formation and for proper precursor and mature miRNA expression. {ECO:0000250}.; . . unclassifiable (Anatomical System);prostate;whole body;testis;kidney;mammary gland;skeletal muscle; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node; 0.16005 0.09611 -0.658030559 16.07690493 4006.10809 12.53102 TDRD7 4.56540427647574e-05 0.999605669348159 0.000348676609076118 tudor domain containing 7 FUNCTION: Component of specific cytoplasmic RNA granules involved in post-transcriptional regulation of specific genes: probably acts by binding to specific mRNAs and regulating their translation. Required for lens transparency during lens development, by regulating translation of genes such as CRYBB3 and HSPB1 in the developing lens. Also required during spermatogenesis. {ECO:0000269|PubMed:21436445}.; DISEASE: Cataract 36 (CTRCT36) [MIM:613887]: An opacification of the crystalline lens of the eye becoming evident at birth. It frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. {ECO:0000269|PubMed:21436445}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;bone;testis;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pineal body;blood;cerebrum;lens;lung;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;occipital lobe;testis - seminiferous tubule;globus pallidus;testis;parietal lobe;cingulate cortex; 0.24173 0.10387 -1.280491183 5.16631281 158.83337 2.75211 TDRD9 3.82298905718051e-07 0.999438650767096 0.000560966933998266 tudor domain containing 9 FUNCTION: Probable ATP-binding RNA helicase which plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Its association with PIWIL4 and the piP-bodies suggests a participation in the secondary piRNAs metabolic process (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;placenta;sympathetic chain;testis;parathyroid;kidney;germinal center;brain; testis - interstitial;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.12943 0.10013 -0.191064116 39.27813163 513.83114 4.63761 TDRD10 2.45421655192587e-06 0.733505869421032 0.266491676362417 tudor domain containing 10 . . . . . 0.15578 . 0.41713504 76.95800896 1257.37769 6.68800 TDRD12 . . . tudor domain containing 12 FUNCTION: Probable ATP-binding RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Involved in the secondary piRNAs metabolic process (By similarity). {ECO:0000250}.; . . . . 0.20728 . 0.946276448 89.90917669 2355.53908 8.99860 TDRD15 . . . tudor domain containing 15 . . . . . . . . . 471.61647 4.49465 TDRG1 . . . testis development related 1 (non-protein coding) . . . . . . . . . . . TDRKH 0.00696242282858822 0.989405072142469 0.00363250502894278 tudor and KH domain containing FUNCTION: Participates in the primary piRNA biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Required for the final steps of primary piRNA biogenesis by participating in the processing of 31-37 nt intermediates into mature piRNAs. May act in pi-bodies and piP-bodies by transferring piRNA precursors or intermediates to or between these granules (By similarity). {ECO:0000250}.; . . . . 0.09618 0.10294 0.685332364 85.09672092 203.55434 3.07924 TDRP 0.00132192801257303 0.65098074076347 0.347697331223957 testis development related protein . . TISSUE SPECIFICITY: Expressed in spermatogenic cells, especially in spermatocytes (at protein level). {ECO:0000269|PubMed:20170638}.; . . 0.37833 0.10307 0.281220278 71.07808445 24.2353 0.79643 TEAD1 . . . TEA domain transcription factor 1 FUNCTION: Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and cooperatively to the SPH and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription in vivo in a cell-specific manner. The activation function appears to be mediated by a limiting cell-specific transcriptional intermediary factor (TIF). Involved in cardiac development. Binds to the M-CAT motif. {ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:19324877}.; . TISSUE SPECIFICITY: Preferentially expressed in skeletal muscle. Lower levels in pancreas, placenta, and heart.; ovary;sympathetic chain;colon;parathyroid;choroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;thyroid;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;macula lutea;amnion;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skeletal muscle; 0.79943 0.41336 -0.516085732 21.20193442 20.36697 0.69493 TEAD2 0.00204731673714379 0.993646681535561 0.00430600172729542 TEA domain transcription factor 2 FUNCTION: Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds to the SPH and GT-IIC 'enhansons' (5'- GTGGAATGT-3'). May be involved in the gene regulation of neural development. Binds to the M-CAT motif. {ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:19324877}.; . . lymphoreticular;myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;bile duct;pancreas;lung;trabecular meshwork;placenta;macula lutea;liver;head and neck;spleen;cervix;mammary gland;aorta;peripheral nerve; superior cervical ganglion;testis - interstitial;atrioventricular node;trigeminal ganglion; 0.60613 0.38068 0.020302773 55.60863411 147.32359 2.64505 TEAD3 . . . TEA domain transcription factor 3 FUNCTION: Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds to multiple functional elements of the human chorionic somatomammotropin-B gene enhancer. {ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:19324877}.; . TISSUE SPECIFICITY: Preferentially expressed in the placenta.; smooth muscle;ovary;colon;parathyroid;uterus;prostate;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;urinary;skeletal muscle;breast;pancreas;lung;placenta;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach;aorta; placenta;ciliary ganglion;skeletal muscle; 0.51942 0.13177 -0.115612493 45.12856806 421.7309 4.28955 TEAD4 . . . TEA domain transcription factor 4 FUNCTION: Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and non-cooperatively to the Sph and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription. Binds to the M-CAT motif. {ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:19324877}.; . TISSUE SPECIFICITY: Preferentially expressed in skeletal muscle. Lower levels in pancreas, placenta, and heart.; smooth muscle;ovary;salivary gland;colon;choroid;skin;uterus;prostate;optic nerve;endometrium;larynx;thyroid;bone;iris;unclassifiable (Anatomical System);heart;skeletal muscle;bile duct;pancreas;lung;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;thyroid;skeletal muscle; 0.92776 0.14081 0.354632714 74.58126917 194.89922 3.02632 TEC 0.00257331126911319 0.997298588662125 0.000128100068762302 tec protein tyrosine kinase FUNCTION: Non-receptor tyrosine kinase that contributes to signaling from many receptors and participates as a signal transducer in multiple downstream pathways, including regulation of the actin cytoskeleton. Plays a redundant role to ITK in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. Required for TCR-dependent IL2 gene induction. Phosphorylates DOK1, one CD28-specific substrate, and contributes to CD28-signaling. Mediates signals that negatively regulate IL2RA expression induced by TCR cross-linking. Plays a redundant role to BTK in BCR-signaling for B-cell development and activation, especially by phosphorylating STAP1, a BCR-signaling protein. Required in mast cells for efficient cytokine production. Involved in both growth and differentiation mechanisms of myeloid cells through activation by the granulocyte colony-stimulating factor CSF3, a critical cytokine to promoting the growth, differentiation, and functional activation of myeloid cells. Participates in platelet signaling downstream of integrin activation. Cooperates with JAK2 through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. GRB10, a negative modifier of the FOS activation pathway, is another substrate of TEC. TEC is involved in G protein-coupled receptor- and integrin-mediated signalings in blood platelets. Plays a role in hepatocyte proliferation and liver regeneration and is involved in HGF-induced ERK signaling pathway. TEC regulates also FGF2 unconventional secretion (endoplasmic reticulum (ER)/Golgi-independent mechanism) under various physiological conditions through phosphorylation of FGF2 'Tyr-215'. May also be involved in the regulation of osteoclast differentiation. {ECO:0000269|PubMed:10518561, ECO:0000269|PubMed:19883687, ECO:0000269|PubMed:20230531, ECO:0000269|PubMed:9753425}.; . TISSUE SPECIFICITY: Expressed in a wide range of cells, including hematopoietic cell lines like myeloid, B-, and T-cell lineages.; . . 0.36669 0.16895 -0.778825328 12.88039632 44.45223 1.27478 TECPR1 2.43068227306975e-07 0.998926295955586 0.00107346097618692 tectonin beta-propeller repeat containing 1 FUNCTION: Tethering factor involved in autophagy. Involved in autophagosome maturation by promoting the autophagosome fusion with lysosomes: acts by associating with both the ATG5-ATG12 conjugate and phosphatidylinositol-3-phosphate (PtdIns(3)P) present at the surface of autophagosomes. Also involved in selective autophagy against bacterial pathogens, by being required for phagophore/preautophagosomal structure biogenesis and maturation. {ECO:0000269|PubMed:21575909, ECO:0000269|PubMed:22342342}.; . . . . . . -2.24910054 1.29747582 1477.95454 7.16021 TECPR2 0.948515859986564 0.051484128458365 1.15550711546174e-08 tectonin beta-propeller repeat containing 2 FUNCTION: Probably plays a role as positive regulator of autophagy. {ECO:0000269|PubMed:23176824}.; . TISSUE SPECIFICITY: Detected in skin fibroblast (at protein level). {ECO:0000269|PubMed:23176824}.; unclassifiable (Anatomical System);smooth muscle;lung;frontal lobe;heart;thyroid;hippocampus;testis;colon;kidney;germinal center;brain;skeletal muscle; amygdala;subthalamic nucleus;medulla oblongata;superior cervical ganglion;prefrontal cortex;testis;pons;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle; 0.23813 . -0.472233057 22.84147205 841.97583 5.68115 TECR 0.75750138958229 0.242414711260574 8.3899157136002e-05 trans-2,3-enoyl-CoA reductase FUNCTION: Catalyzes the last of the four reactions of the long- chain fatty acids elongation cycle. This endoplasmic reticulum- bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA that can be further elongated by entering a new cycle of elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000269|PubMed:12482854}.; DISEASE: Mental retardation, autosomal recessive 14 (MRT14) [MIM:614020]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:21212097}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in most tissues tested. Highly expressed in skeletal muscle. {ECO:0000269|PubMed:12482854}.; medulla oblongata;ovary;skin;retina;prostate;optic nerve;frontal lobe;thyroid;iris;germinal center;bladder;brain;heart;tongue;pineal body;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;colon;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; . 0.27942 0.73513 -0.207437529 38.2814343 11.82947 0.42861 TECRL 6.39982199048601e-10 0.127050735848624 0.872949263511394 trans-2,3-enoyl-CoA reductase-like . . . . . . . 0.328949044 73.41354093 376.89092 4.09312 TECRP1 . . . trans-2,3-enoyl-CoA reductase pseudogene 1 . . . . . . . . . . . TECRP2 . . . trans-2,3-enoyl-CoA reductase pseudogene 2 . . . . . . . . . . . TECTA 1.06498565113514e-12 0.999989745526101 1.02544728344311e-05 tectorin alpha FUNCTION: One of the major non-collagenous components of the tectorial membrane (By similarity). The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair-cell membrane potential, transducing sound into electrical signals. {ECO:0000250}.; DISEASE: Deafness, autosomal dominant, 12 (DFNA12) [MIM:601543]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:10196713, ECO:0000269|PubMed:10987647, ECO:0000269|PubMed:12162770, ECO:0000269|PubMed:15319541, ECO:0000269|PubMed:16718611, ECO:0000269|PubMed:17661817, ECO:0000269|PubMed:20947814, ECO:0000269|PubMed:21520338, ECO:0000269|PubMed:9590290}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal recessive, 21 (DFNB21) [MIM:603629]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:12746400, ECO:0000269|PubMed:9949200}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . liver;testis;spleen;blood;brain; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.64735 0.20702 -2.430013277 1.032083038 4846.67098 14.13953 TECTB 5.94966588308075e-09 0.127337894194623 0.872662099855711 tectorin beta FUNCTION: One of the major non-collagenous components of the tectorial membrane (By similarity). The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair-cell membrane potential, transducing sound into electrical signals. {ECO:0000250}.; . . . . 0.30616 0.11754 -0.135838822 43.77211607 87.85301 2.00256 TEDDM1 0.084146705930434 0.759036242915468 0.156817051154097 transmembrane epididymal protein 1 . . . . . 0.18732 . 0.305084559 72.22811984 16.86559 0.59371 TEDDM2P . . . transmembrane epididymal protein 2, pseudogene . . . . . . . . . . . TEF 0.421035621263218 0.544741385042867 0.0342229936939154 thyrotrophic embryonic factor FUNCTION: Transcription factor that binds to and transactivates the TSHB promoter. Binds to a minimal DNA-binding sequence 5'- [TC][AG][AG]TTA[TC][AG]-3'.; . . smooth muscle;ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;cochlea;thyroid;germinal center;brain;amygdala;cartilage;pharynx;blood;lens;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;oesophagus;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;placenta;hippocampus;head and neck;kidney;thymus; superior cervical ganglion; 0.60757 0.20297 -0.251530012 35.42108988 8.11117 0.29729 TEFM 0.0433026064919595 0.929404008015153 0.0272933854928879 transcription elongation factor, mitochondrial FUNCTION: Transcription elongation factor which increases mitochondrial RNA polymerase processivity. Regulates transcription of the mitochondrial genome, including genes important for the oxidative phosphorylation machinery. {ECO:0000269|PubMed:21278163}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;germinal center;brain;artery;pineal gland;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;adrenal cortex;lens;bile duct;lung;adrenal gland;placenta;macula lutea;liver;spleen;kidney;aorta; testis - interstitial;testis - seminiferous tubule; 0.09439 0.07415 -0.093566408 46.7386176 1118.46053 6.38402 TEK 0.999992784331617 7.21566838037837e-06 2.62564885931404e-15 TEK receptor tyrosine kinase FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for ANGPT1, ANGPT2 and ANGPT4 and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Has anti-inflammatory effects by preventing the leakage of proinflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for post- natal hematopoiesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. ANGPT1 signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Signaling is modulated by ANGPT2 that has lower affinity for TEK, can promote TEK autophosphorylation in the absence of ANGPT1, but inhibits ANGPT1-mediated signaling by competing for the same binding site. Signaling is also modulated by formation of heterodimers with TIE1, and by proteolytic processing that gives rise to a soluble TEK extracellular domain. The soluble extracellular domain modulates signaling by functioning as decoy receptor for angiopoietins. TEK phosphorylates DOK2, GRB7, GRB14, PIK3R1; SHC1 and TIE1. {ECO:0000269|PubMed:12816861, ECO:0000269|PubMed:14665640, ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:15851516, ECO:0000269|PubMed:18366015, ECO:0000269|PubMed:18425119, ECO:0000269|PubMed:18425120, ECO:0000269|PubMed:19223473, ECO:0000269|PubMed:20651738, ECO:0000269|PubMed:9204896}.; DISEASE: Dominantly inherited venous malformations (VMCM) [MIM:600195]: An error of vascular morphogenesis characterized by dilated, serpiginous channels. {ECO:0000269|PubMed:10369874, ECO:0000269|PubMed:19888299, ECO:0000269|PubMed:8980225}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=May play a role in a range of diseases with a vascular component, including neovascularization of tumors, psoriasis and inflammation.; TISSUE SPECIFICITY: Detected in umbilical vein endothelial cells. Proteolytic processing gives rise to a soluble extracellular domain that is detected in blood plasma (at protein level). Predominantly expressed in endothelial cells and their progenitors, the angioblasts. Has been directly found in placenta and lung, with a lower level in umbilical vein endothelial cells, brain and kidney. {ECO:0000269|PubMed:11806244, ECO:0000269|PubMed:8382358}.; unclassifiable (Anatomical System);lung;cartilage;cochlea;placenta;testis;kidney;mammary gland;skeletal muscle;retina; superior cervical ganglion;ciliary ganglion;kidney;skin;skeletal muscle; 0.89992 0.10231 -0.326979057 30.90351498 1368.98168 6.93958 TEKT1 0.000108974564413063 0.818669745912119 0.181221279523468 tektin 1 FUNCTION: Structural component of ciliary and flagellar microtubules. Forms filamentous polymers in the walls of ciliary and flagellar microtubules.; . TISSUE SPECIFICITY: Predominantly expressed in testis. {ECO:0000269|PubMed:11606253}.; unclassifiable (Anatomical System);medulla oblongata;cartilage;choroid;fovea centralis;lens;retina;optic nerve;lung;endometrium;nasopharynx;macula lutea;testis;brain; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node; 0.11740 . 0.977404764 90.3868837 2572.89765 9.47916 TEKT2 4.73097417544403e-09 0.206191879963638 0.793808115305387 tektin 2 FUNCTION: Structural component of ciliary and flagellar microtubules. Plays a key role in the assembly or attachment of the inner dynein arm to microtubules in sperm flagella and tracheal cilia. Forms filamentous polymers in the walls of ciliary and flagellar microtubules (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at high levels in testis, trachea and fetal lung, and at lower levels in ovary, pituitary, adult lung, fetal brain and fetal kidney. {ECO:0000269|PubMed:11751288}.; pancreas;lung;endometrium;testis;kidney;brain; testis - interstitial;testis - seminiferous tubule;testis; 0.11856 0.10748 -0.332434268 30.74427931 841.27654 5.67951 TEKT3 3.19945204057199e-14 0.0103608282647885 0.98963917173518 tektin 3 FUNCTION: Structural component of ciliary and flagellar microtubules. Forms filamentous polymers in the walls of ciliary and flagellar microtubules. Required for progressive sperm mobility (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);endometrium;placenta;testis;colon;brain; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;parietal lobe; 0.04933 0.09715 0.911261639 89.50813871 3686.69181 11.82421 TEKT4 2.56100307685227e-11 0.0199838452867225 0.980016154687668 tektin 4 FUNCTION: Structural component of ciliary and flagellar microtubules. Forms filamentous polymers in the walls of ciliary and flagellar microtubules (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;blood;parathyroid;skin;retina;uterus;lung;endometrium;placenta;liver;testis;spleen;kidney; dorsal root ganglion;superior cervical ganglion;testis;pons;trigeminal ganglion; 0.10458 0.10499 1.269496963 93.63057325 5405.58803 15.16078 TEKT4P1 . . . tektin 4 pseudogene 1 . . . . . . . . . . . TEKT4P2 . . . tektin 4 pseudogene 2 . . . . . . . . . . . TEKT4P3 . . . tektin 4 pseudogene 3 . . . . . . . . . . . TEKT5 1.10256706066914e-14 0.00287829218491892 0.99712170781507 tektin 5 FUNCTION: Structural component of ciliary and flagellar microtubules. Forms filamentous polymers in the walls of ciliary and flagellar microtubules (By similarity). {ECO:0000250}.; . . endometrium;testis;skin; testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.11873 0.10499 2.274625269 98.25430526 806.428 5.59413 TELAB1 . . . telangiectasia, benign 1 . . . . . . . . . . . TELO2 4.84231495536262e-07 0.990453688011557 0.00954582775694695 telomere maintenance 2 FUNCTION: Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals. May be involved in telomere length regulation. {ECO:0000269|PubMed:12670948, ECO:0000269|PubMed:20810650}.; . . medulla oblongata;ovary;adrenal medulla;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;cervix;kidney;stomach;thymus; globus pallidus;ciliary ganglion;skeletal muscle;cingulate cortex; 0.28091 0.10845 0.415122141 76.68082095 1413.28281 7.02717 TEN1 . . . TEN1 CST complex subunit FUNCTION: Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation (PubMed:19854130). However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha (PubMed:22763445). The CST complex facilitates recovery from many forms of exogenous DNA damage; seems to be involved in the re-initiation of DNA replication at repaired forks and/or dormant origins (PubMed:25483097). {ECO:0000269|PubMed:19854130, ECO:0000269|PubMed:22763445, ECO:0000269|PubMed:25483097}.; . . . . . . 0.21326276 67.71644256 56.15344 1.50534 TEN1-CDK3 . . . TEN1-CDK3 readthrough (NMD candidate) . . . . . . . . . . . TENM1 0.999995817016826 4.18298317445478e-06 1.1663234085072e-18 teneurin transmembrane protein 1 FUNCTION: Involved in neural development, regulating the establishment of proper connectivity within the nervous system. May function as a cellular signal transducer (By similarity). {ECO:0000250}.; FUNCTION: Ten-1 intracellular domain: Induces gene transcription activation. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in fetal brain. {ECO:0000269|PubMed:10341219}.; . . 0.48696 0.10783 -3.45943214 0.359754659 652.71126 5.12522 TENM2 0.999951089930002 4.89100699978902e-05 9.42300647064587e-17 teneurin transmembrane protein 2 FUNCTION: Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Promotes the formation of filopodia and enlarged growth cone in neuronal cells. Induces homophilic cell-cell adhesion (By similarity). May function as a cellular signal transducer. {ECO:0000250, ECO:0000269|PubMed:21724987}.; FUNCTION: Ten-2 intracellular domain: Induces gene transcription inhibition. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in heart, followed by brain, liver, kidney and fetal brain and weakly expressed in lung and testis. No expression was detected in skeletal muscle, pancreas, spleen, ovary and fetal liver. {ECO:0000269|PubMed:10574461}.; . . 0.25516 . . . 688.9914 5.23649 TENM3 0.999937943986087 6.2056013913034e-05 1.39412345158709e-18 teneurin transmembrane protein 3 FUNCTION: Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Promotes axon guidance and homophilic cell adhesion. Plays a role in the development of the visual pathway; regulates the formation in ipsilateral retinal mapping to both the dorsal lateral geniculate nucleus (dLGN) and the superior colliculus (SC). May be involved in the differentiation of the fibroblast-like cells in the superficial layer of mandibular condylar cartilage into chondrocytes. May function as a cellular signal transducer (By similarity). {ECO:0000250}.; DISEASE: Microphthalmia, isolated, with coloboma, 9 (MCOPCB9) [MIM:615145]: A disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues. Ocular abnormalities like opacities of the cornea and lens, scaring of the retina and choroid, and other abnormalities may also be present. Ocular colobomas are a set of malformations resulting from abnormal morphogenesis of the optic cup and stalk, and the fusion of the fetal fissure (optic fissure). {ECO:0000269|PubMed:22766609}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in adult and fetal brain, slightly lower levels in testis and ovary, and intermediate levels in all other peripheral tissues examined. Not expressed in spleen or liver. Expression was high in brain, with highest levels in amygdala and caudate nucleus, followed by thalamus and subthalamic nucleus. {ECO:0000269|PubMed:10625539, ECO:0000269|PubMed:10819331}.; . . 0.48696 . -3.45943214 0.359754659 425.70695 4.31166 TENM4 0.999718775956683 0.000281224043284078 3.30088667114861e-14 teneurin transmembrane protein 4 FUNCTION: Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Plays a role in the establishment of the anterior-posterior axis during gastrulation. Regulates the differentiation and cellular process formation of oligodendrocytes and myelination of small- diameter axons in the central nervous system (CNS). Promotes activation of focal adhesion kinase. May function as a cellular signal transducer (By similarity). {ECO:0000250}.; . . . . 0.59536 . -1.696530647 2.589054022 1180.19147 6.52237 TEP1 4.51417224704889e-24 0.999975992647303 2.40073526970348e-05 telomerase associated protein 1 FUNCTION: Component of the telomerase ribonucleoprotein complex that is essential for the replication of chromosome termini. Also component of the ribonucleoprotein vaults particle, a multi- subunit structure involved in nucleo-cytoplasmic transport. Responsible for the localizing and stabilizing vault RNA (vRNA) association in the vault ribonucleoprotein particle. Binds to TERC (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9020079}.; unclassifiable (Anatomical System);cartilage;ovary;salivary gland;sympathetic chain;intestine;pharynx;colon;blood;skin;skeletal muscle;bone marrow;breast;uterus;prostate;lung;frontal lobe;bone;thyroid;placenta;visual apparatus;duodenum;liver;head and neck;germinal center;kidney;brain;bladder; superior cervical ganglion;subthalamic nucleus;trigeminal ganglion;skeletal muscle; 0.21037 0.09724 4.18520111 99.71101675 10022.98506 21.84114 TEPP 6.79569807856734e-05 0.729947500819223 0.269984542199991 testis, prostate and placenta expressed . . TISSUE SPECIFICITY: Expressed in testis, prostate and placenta. {ECO:0000269|PubMed:14652002}.; testis; atrioventricular node;trigeminal ganglion; . . -0.069700724 48.54328851 39.64027 1.16858 TERC . . . telomerase RNA component . . . . . . . . . . . TERF1 0.878033579613451 0.121903557947005 6.28624395441435e-05 telomeric repeat binding factor 1 FUNCTION: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double- stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. {ECO:0000269|PubMed:16166375}.; . TISSUE SPECIFICITY: Highly expressed and ubiquitous. Isoform Pin2 predominates.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;thyroid;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);islets of Langerhans;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;kidney;mammary gland;stomach; subthalamic nucleus;ciliary ganglion;atrioventricular node; 0.53628 0.28085 -0.60427181 17.74593064 31.28752 0.98646 TERF1P1 . . . telomeric repeat binding factor 1 pseudogene 1 . . . . . . . . . . . TERF1P2 . . . telomeric repeat binding factor 1 pseudogene 2 . . . . . . . . . . . TERF1P3 . . . telomeric repeat binding factor 1 pseudogene 3 . . . . . . . . . . . TERF1P4 . . . telomeric repeat binding factor 1 pseudogene 4 . . . . . . . . . . . TERF1P5 . . . telomeric repeat binding factor 1 pseudogene 5 . . . . . . . . . . . TERF2 0.927472177448586 0.0725114285095227 1.63940418916121e-05 telomeric repeat binding factor 2 FUNCTION: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single- stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology- directed repair (HDR), which can affect telomere length. {ECO:0000269|PubMed:16166375, ECO:0000269|PubMed:20655466, ECO:0000269|PubMed:9476899}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in spleen, thymus, prostate, uterus, testis, small intestine, colon and peripheral blood leukocytes.; lymphoreticular;ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;spinal cord;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach;aorta;cerebellum; amygdala;whole brain;superior cervical ganglion;occipital lobe;cerebellum peduncles;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.54648 0.19042 0.21689899 68.12927577 95.46186 2.10951 TERF2IP 0.0227973012542949 0.911761767851504 0.0654409308942013 TERF2 interacting protein FUNCTION: Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'- TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes. {ECO:0000269|PubMed:16166375, ECO:0000269|PubMed:19763083}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed.; myocardium;ovary;sympathetic chain;skin;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;larynx;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;cerebellum; amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.55010 0.13022 -0.161524709 41.6430762 160.91892 2.77014 TERF2IPP1 . . . TERF2 interacting protein pseudogene 1 . . . . . . . . . . . TERT 0.866151189063377 0.133848144058592 6.66878031174044e-07 telomerase reverse transcriptase FUNCTION: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA- dependent extension of 3'-chromosomal termini with the 6- nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis. {ECO:0000269|PubMed:14963003, ECO:0000269|PubMed:15082768, ECO:0000269|PubMed:15857955, ECO:0000269|PubMed:17026956, ECO:0000269|PubMed:17264120, ECO:0000269|PubMed:17296728, ECO:0000269|PubMed:17548608, ECO:0000269|PubMed:19188162, ECO:0000269|PubMed:19567472, ECO:0000269|PubMed:19571879, ECO:0000269|PubMed:19777057, ECO:0000269|PubMed:9389643}.; DISEASE: Note=Activation of telomerase has been implicated in cell immortalization and cancer cell pathogenesis.; DISEASE: Aplastic anemia (AA) [MIM:609135]: A form of anemia in which the bone marrow fails to produce adequate numbers of peripheral blood elements. It is characterized by peripheral pancytopenia and marrow hypoplasia. {ECO:0000269|PubMed:15885610, ECO:0000269|PubMed:16627250, ECO:0000269|PubMed:16990594, ECO:0000269|PubMed:19760749}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Note=Genetic variations in TERT are associated with coronary artery disease (CAD).; DISEASE: Dyskeratosis congenita, autosomal dominant, 2 (DKCA2) [MIM:613989]: A rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy. {ECO:0000269|PubMed:15885610, ECO:0000269|PubMed:16247010}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pulmonary fibrosis, and/or bone marrow failure, telomere- related, 1 (PFBMFT1) [MIM:614742]: A disease associated with shortened telomeres. Pulmonary fibrosis is the most common manifestation. Other manifestations include aplastic anemia due to bone marrow failure, hepatic fibrosis, and increased cancer risk, particularly myelodysplastic syndrome and acute myeloid leukemia. Phenotype, age at onset, and severity are determined by telomere length. {ECO:0000269|PubMed:15814878, ECO:0000269|PubMed:17460043, ECO:0000269|PubMed:21436073, ECO:0000269|PubMed:21483807, ECO:0000269|PubMed:22512499}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dyskeratosis congenita, autosomal recessive, 4 (DKCB4) [MIM:613989]: A severe form of dyskeratosis congenita, a rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy. {ECO:0000269|PubMed:16332973, ECO:0000269|PubMed:17785587, ECO:0000269|PubMed:18042801}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pulmonary fibrosis, idiopathic (IPF) [MIM:178500]: A lung disease characterized by shortness of breath, radiographically evident diffuse pulmonary infiltrates, and varying degrees of inflammation and fibrosis on biopsy. In some cases, the disorder can be rapidly progressive and characterized by sequential acute lung injury with subsequent scarring and end-stage lung disease. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Melanoma, cutaneous malignant 9 (CMM9) [MIM:615134]: A malignant neoplasm of melanocytes, arising de novo or from a pre- existing benign nevus, which occurs most often in the skin but also may involve other sites. {ECO:0000269|PubMed:23348503}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at a high level in thymocyte subpopulations, at an intermediate level in tonsil T-lymphocytes, and at a low to undetectable level in peripheral blood T- lymphocytes. {ECO:0000269|PubMed:8676067, ECO:0000269|PubMed:9389643}.; unclassifiable (Anatomical System);uterus;lymph node;lung;germinal center; . 0.22857 0.67480 . . 56.37626 1.50879 TES 4.84137383314076e-11 0.028977180166997 0.971022819784589 testin LIM domain protein FUNCTION: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor. Inhibits tumor cell growth. {ECO:0000269|PubMed:11420696, ECO:0000269|PubMed:12571287, ECO:0000269|PubMed:12695497}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11420696}.; smooth muscle;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;artery;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; uterus;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;appendix;white blood cells;trigeminal ganglion;skeletal muscle; 0.24387 0.20818 -0.558357437 19.54470394 139.9765 2.58102 TESC 0.692139730962892 0.303817427951244 0.00404284108586397 tescalcin FUNCTION: Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Promotes the maturation, transport, cell surface stability and exchange activity of SLC9A1/NHE1 at the plasma membrane. Promotes the induction of hematopoietic stem cell differentiation toward megakaryocytic lineage. Essential for the coupling of ERK cascade activation with the expression of ETS family genes in megakaryocytic differentiation. Also involved in granulocytic differentiation in a ERK-dependent manner. Inhibits the phosphatase activity of calcineurin. {ECO:0000269|PubMed:17717601, ECO:0000269|PubMed:18321853, ECO:0000269|PubMed:20060826}.; . TISSUE SPECIFICITY: Expressed in mature megakaryocytes and polymorphonuclear granulocytes (at protein level). Abundantly expressed in heart. Also expressed at a lower level in adult testis and salivary gland, and in the placenta. {ECO:0000269|PubMed:11696366, ECO:0000269|PubMed:20060826}.; unclassifiable (Anatomical System);heart;islets of Langerhans;colon;blood;fovea centralis;retina;pancreas;prostate;lung;thyroid;placenta;macula lutea;liver;testis;spleen;brain;stomach; superior cervical ganglion;testis;caudate nucleus;bone marrow; 0.18238 0.14604 -0.205617011 38.57631517 46.18344 1.30946 TESC-AS1 . . . TESC antisense RNA 1 (head to head) . . . . . . . . . . . TESK1 0.999003534885551 0.00099646299176154 2.12268710984242e-09 testis-specific kinase 1 FUNCTION: Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Probably plays a central role at and after the meiotic phase of spermatogenesis (By similarity). {ECO:0000250}.; . . lymphoreticular;smooth muscle;colon;skin;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;adrenal cortex;testis;globus pallidus;parietal lobe;skeletal muscle; 0.26569 0.12980 -0.380166007 27.88393489 85.02855 1.96539 TESK2 8.65426854901905e-06 0.982019984058327 0.0179713616731239 testis-specific kinase 2 FUNCTION: Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Phosphorylates cofilin at 'Ser-3'. May play an important role in spermatogenesis.; . TISSUE SPECIFICITY: Predominantly expressed in testis and prostate. Found predominantly in non-germinal Sertoli cells. {ECO:0000269|PubMed:10512679, ECO:0000269|PubMed:11418599}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;alveolus;spleen;cervix;kidney;mammary gland;peripheral nerve; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.27416 0.11528 0.222355725 68.44184949 210.43775 3.13053 TESPA1 1.91516352804028e-05 0.889674233753202 0.110306614611518 thymocyte expressed, positive selection associated 1 FUNCTION: Required for the development and maturation of T-cells, its function being essential for the late stages of thymocyte development (By similarity). Plays a role in T-cell antigen receptor (TCR)-mediated activation of the ERK and NFAT signaling pathways, possibly by serving as a scaffolding protein that promotes the assembly of the LAT signalosome in thymocytes. May play a role in the regulation of inositol 1,4,5-trisphosphate receptor-mediated Ca(2+) release and mitochondrial Ca(2+) uptake via the mitochondria-associated endoplasmic reticulum membrane (MAM) compartment. {ECO:0000250, ECO:0000269|PubMed:22561606}.; . . . . 0.20486 . 1.488170966 95.3467799 3822.16161 12.15048 TET1 0.9995632776113 0.000436722388603997 9.64591946668187e-14 tet methylcytosine dioxygenase 1 FUNCTION: Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5- hydroxymethylcytosine (5hmC) and plays a key role in active DNA demethylation. Also mediates subsequent conversion of 5hmC into 5- formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the first step in cytosine demethylation. Methylation at the C5 position of cytosine bases is an epigenetic modification of the mammalian genome which plays an important role in transcriptional regulation. In addition to its role in DNA demethylation, plays a more general role in chromatin regulation. Preferentially binds to CpG-rich sequences at promoters of both transcriptionally active and Polycomb-repressed genes. Involved in the recruitment of the O-GlcNAc transferase OGT to CpG-rich transcription start sites of active genes, thereby promoting histone H2B GlcNAcylation by OGT. Also involved in transcription repression of a subset of genes through recruitment of transcriptional repressors to promoters. Involved in the balance between pluripotency and lineage commitment of cells it plays a role in embryonic stem cells maintenance and inner cell mass cell specification. Plays an important role in the tumorigenicity of glioblastoma cells. TET1-mediated production of 5hmC acts as a recruitment signal for the CHTOP-methylosome complex to selective sites on the chromosome, where it methylates H4R3 and activates the transcription of genes involved in glioblastomagenesis (PubMed:25284789). {ECO:0000269|PubMed:12124344, ECO:0000269|PubMed:19372391, ECO:0000269|PubMed:19372393, ECO:0000269|PubMed:21496894, ECO:0000269|PubMed:21778364, ECO:0000269|PubMed:25284789}.; DISEASE: Note=A chromosomal aberration involving TET1 may be a cause of acute leukemias (PubMed:12646957). Translocation t(10;11)(q22;q23) with KMT2A/MLL1. This is a rare chromosomal translocation 5' KMT2A/MLL1-TET1 3' (PubMed:12124344, PubMed:12646957). {ECO:0000269|PubMed:12124344, ECO:0000269|PubMed:12646957}.; TISSUE SPECIFICITY: Expressed in fetal heart, lung and brain, and in adult skeletal muscle, thymus and ovary. Not detected in adult heart, lung or brain. Up-regulated in glioblastoma cells (at protein level) (PubMed:25284789). {ECO:0000269|PubMed:12124344, ECO:0000269|PubMed:12646957, ECO:0000269|PubMed:25284789}.; . . 0.67616 0.10932 0.398551838 76.31516867 4993.56015 14.43135 TET1P1 . . . tet methylcytosine dioxygenase 1 pseudogene 1 . . . . . . . . . . . TET2 7.05368251291393e-26 3.66944874941071e-06 0.999996330551251 tet methylcytosine dioxygenase 2 FUNCTION: Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5- hydroxymethylcytosine (5hmC) and plays a key role in active DNA demethylation. Has a preference for 5-hydroxymethylcytosine in CpG motifs. Also mediates subsequent conversion of 5hmC into 5- formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the first step in cytosine demethylation. Methylation at the C5 position of cytosine bases is an epigenetic modification of the mammalian genome which plays an important role in transcriptional regulation. In addition to its role in DNA demethylation, also involved in the recruitment of the O-GlcNAc transferase OGT to CpG-rich transcription start sites of active genes, thereby promoting histone H2B GlcNAcylation by OGT. {ECO:0000269|PubMed:19483684, ECO:0000269|PubMed:21057493, ECO:0000269|PubMed:21817016, ECO:0000269|PubMed:23222540, ECO:0000269|PubMed:23353889, ECO:0000269|PubMed:24315485}.; DISEASE: Note=TET2 is frequently mutated in myeloproliferative disorders (MPD). These constitute a heterogeneous group of disorders, also known as myeloproliferative diseases or myeloproliferative neoplasms (MPN), characterized by cellular proliferation of one or more hematologic cell lines in the peripheral blood, distinct from acute leukemia. Included diseases are: essential thrombocythemia, polycythemia vera, primary myelofibrosis (chronic idiopathic myelofibrosis). Bone marrow samples from patients display uniformly low levels of hmC in genomic DNA compared to bone marrow samples from healthy controls as well as hypomethylation relative to controls at the majority of differentially methylated CpG sites.; DISEASE: Polycythemia vera (PV) [MIM:263300]: A myeloproliferative disorder characterized by abnormal proliferation of all hematopoietic bone marrow elements, erythroid hyperplasia, an absolute increase in total blood volume, but also by myeloid leukocytosis, thrombocytosis and splenomegaly. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=TET2 is frequently mutated in systemic mastocytosis; also known as systemic mast cell disease. A condition with features in common with myeloproliferative diseases. It is a clonal disorder of the mast cell and its precursor cells. The clinical symptoms and signs of systemic mastocytosis are due to accumulation of clonally derived mast cells in different tissues, including bone marrow, skin, the gastrointestinal tract, the liver, and the spleen.; DISEASE: Myelodysplastic syndrome (MDS) [MIM:614286]: A heterogeneous group of closely related clonal hematopoietic disorders. All are characterized by a hypercellular or hypocellular bone marrow with impaired morphology and maturation, dysplasia of the myeloid, megakaryocytic and/or erythroid lineages, and peripheral blood cytopenias resulting from ineffective blood cell production. Included diseases are: refractory anemia (RA), refractory anemia with ringed sideroblasts (RARS), refractory anemia with excess blasts (RAEB), refractory cytopenia with multilineage dysplasia and ringed sideroblasts (RCMD-RS); chronic myelomonocytic leukemia (CMML) is a myelodysplastic/myeloproliferative disease. MDS is considered a premalignant condition in a subgroup of patients that often progresses to acute myeloid leukemia (AML). {ECO:0000269|PubMed:19372255, ECO:0000269|PubMed:19483684, ECO:0000269|PubMed:21057493}. Note=The disease is caused by mutations affecting the gene represented in this entry. Bone marrow samples from patients display uniformly low levels of hmC in genomic DNA compared to bone marrow samples from healthy controls as well as hypomethylation relative to controls at the majority of differentially methylated CpG sites.; TISSUE SPECIFICITY: Broadly expressed. Highly expressed in hematopoietic cells; highest expression observed in granulocytes. Expression is reduced in granulocytes from peripheral blood of patients affected by myelodysplastic syndromes. {ECO:0000269|PubMed:12646957, ECO:0000269|PubMed:19483684}.; ovary;parathyroid;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;lung;placenta;liver;hypopharynx;spleen;head and neck;kidney;stomach; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;whole blood;trigeminal ganglion;skeletal muscle; 0.06187 0.06302 1.967713496 97.56428403 3646.95795 11.72729 TET2-AS1 . . . TET2 antisense RNA 1 . . . . . . . . . . . TET3 0.999942650512804 5.7349477197238e-05 9.99878635148228e-12 tet methylcytosine dioxygenase 3 FUNCTION: Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5- hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming in the zygote following fertilization. Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the first step in cytosine demethylation. In zygotes, DNA demethylation occurs selectively in the paternal pronucleus before the first cell division, while the adjacent maternal pronucleus and certain paternally-imprinted loci are protected from this process. Participates in DNA demethylation in the paternal pronucleus by mediating conversion of 5mC into 5hmC, 5fC and 5caC. Does not mediate DNA demethylation of maternal pronucleus because of the presence of DPPA3/PGC7 on maternal chromatin that prevents TET3-binding to chromatin (By similarity). In addition to its role in DNA demethylation, also involved in the recruitment of the O- GlcNAc transferase OGT to CpG-rich transcription start sites of active genes, thereby promoting histone H2B GlcNAcylation by OGT. {ECO:0000250, ECO:0000269|PubMed:23353889}.; . TISSUE SPECIFICITY: Expressed in colon, muscle, adrenal gland and peripheral blood lymphocytes. {ECO:0000269|PubMed:12646957}.; unclassifiable (Anatomical System);lung;colon;cervix;blood;brain;skeletal muscle;bone marrow; superior cervical ganglion;medulla oblongata;subthalamic nucleus;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.85759 0.10310 -1.512251235 3.479594244 432.06015 4.33811 TEX2 0.440979879688037 0.559019646650779 4.73661184134894e-07 testis expressed 2 . . . colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;bone;pituitary gland;testis;amniotic fluid;germinal center;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;nervous;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;adrenal gland;epididymis;placenta;macula lutea;hippocampus;alveolus;liver;spleen;head and neck;stomach;cerebellum; testis - interstitial;testis - seminiferous tubule;spinal cord;testis;ciliary ganglion;parietal lobe; 0.17386 0.08006 -0.946125119 9.377211607 521.90393 4.66418 TEX9 2.58827295083548e-17 0.00111949853319418 0.998880501466806 testis expressed 9 . . . unclassifiable (Anatomical System);medulla oblongata;ovary;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;skin;lung;cornea;nasopharynx;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland; . 0.05917 0.08091 -0.113792788 45.25831564 131.8327 2.49971 TEX10 0.999988106747192 1.18932527640108e-05 4.38310403793329e-14 testis expressed 10 FUNCTION: Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. {ECO:0000269|PubMed:22872859}.; . . . . 0.53447 0.10987 -0.709045403 14.673272 51.69607 1.41982 TEX11 0.999964221357823 3.5778639008975e-05 3.16824490706605e-12 testis expressed 11 FUNCTION: Regulator of crossing-over during meiosis. Involved in initiation and/or maintenance of chromosome synapsis and formation of crossovers (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Testis-specific. Not expressed in adult ovaries. {ECO:0000269|PubMed:18369460}.; unclassifiable (Anatomical System);bile duct;pancreas;lung;testis;spleen;skin; dorsal root ganglion;subthalamic nucleus;testis - interstitial;superior cervical ganglion;thalamus;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11019 0.08132 -0.44448505 24.46331682 803.03545 5.58368 TEX12 0.133134681714709 0.78011431815668 0.086751000128611 testis expressed 12 . . TISSUE SPECIFICITY: Testis specific.; . . 0.12875 0.10115 0.501689326 79.7888653 15.42623 0.55392 TEX13A 0.00748148856358932 0.774635662673336 0.217882848763075 testis expressed 13A . . TISSUE SPECIFICITY: Testis specific.; . . 0.06718 0.08014 . . 16.55275 0.58455 TEX13B 0.0252280353289702 0.782241248757136 0.192530715913894 testis expressed 13B . . TISSUE SPECIFICITY: Testis specific.; . . 0.06220 . 0.948089677 89.95635763 365.92813 4.04834 TEX13C . . . TEX13 family member C . . . . . . . . . . . TEX13D . . . TEX13 family member D . . . . . . . . . . . TEX14 6.67135466367958e-23 0.251585764705497 0.748414235294503 testis expressed 14 FUNCTION: Required both for the formation of intercellular bridges during meiosis and for kinetochore-microtubule attachment during mitosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells and are required for spermatogenesis and male fertility. Acts by promoting the conversion of midbodies into intercellular bridges via its interaction with CEP55: interaction with CEP55 inhibits the interaction between CEP55 and PDCD6IP/ALIX and TSG101, blocking cell abscission and leading to transform midbodies into intercellular bridges. Also plays a role during mitosis: recruited to kinetochores by PLK1 during early mitosis and regulates the maturation of the outer kinetochores and microtubule attachment. Has no protein kinase activity in vitro (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in testis. {ECO:0000269|PubMed:11279525}.; unclassifiable (Anatomical System);prostate;lung;whole body;lacrimal gland;placenta;visual apparatus;testis;colon; dorsal root ganglion;testis - interstitial;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;temporal lobe;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.26950 . -0.869123606 10.5980184 357.41532 4.00624 TEX15 3.89144760802236e-17 0.651939677075101 0.348060322924899 testis expressed 15 FUNCTION: Required during spermatogenesis for normal chromosome synapsis and meiotic recombination in germ cells. Necessary for formation of DMC1 and RAD51 foci on meiotic chromosomes, suggesting a specific role in DNA double-stranded break repair. {ECO:0000250|UniProtKB:F8VPN2}.; . TISSUE SPECIFICITY: Detected in testis and ovary (PubMed:11279525). Also expressed in several cancers (PubMed:12704671). {ECO:0000269|PubMed:11279525, ECO:0000269|PubMed:12704671}.; unclassifiable (Anatomical System);lung;liver;testis;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05564 0.06933 2.705323695 98.91483841 4622.31964 13.66528 TEX16P . . . testis expressed 16, pseudogene . . . . . . . . . . . TEX19 0.000184450309866715 0.275561516272945 0.724254033417188 testis expressed 19 FUNCTION: Required during spermatogenesis and placenta development, probably by participating to the repression of retrotransposable elements and prevent their mobilization. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis. Expressed in undifferentiated embryonic stem cells. {ECO:0000269|PubMed:18096721, ECO:0000269|PubMed:18160741}.; unclassifiable (Anatomical System);lymph node;lung;bone;muscle;testis;stomach; dorsal root ganglion;ciliary ganglion;trigeminal ganglion; . . 0.859896574 88.62349611 97.77317 2.13811 TEX21P . . . testis expressed 21, pseudogene . . . . . . . . . . . TEX22 . . . testis expressed 22 . . . . . . . . . 126.47135 2.44946 TEX26 8.72441908029966e-09 0.0844557461099648 0.915544245165616 testis expressed 26 . . . . . 0.04885 . 0.463046108 78.58575136 2579.02284 9.49494 TEX26-AS1 . . . TEX26 antisense RNA 1 . . . . . . . . . . . TEX28 . . . testis expressed 28 . . TISSUE SPECIFICITY: Testis specific.; unclassifiable (Anatomical System);optic nerve;lung;macula lutea;testis;spleen;fovea centralis;choroid;lens;retina; . 0.08608 0.07825 . . . . TEX28P1 . . . testis expressed 28 pseudogene 1 . . TISSUE SPECIFICITY: Testis specific.; . . . 0.07825 . . . . TEX28P2 . . . testis expressed 28 pseudogene 2 . . TISSUE SPECIFICITY: Testis specific.; . . . 0.07825 . . . . TEX29 0.00145166750512405 0.671141972725899 0.327406359768977 testis expressed 29 . . . . . 0.02058 . -0.139478553 43.29440906 19.3167 0.66507 TEX30 0.00629544130857506 0.742180873353003 0.251523685338422 testis expressed 30 . . . . . 0.24219 . -0.075159878 47.78839349 28.8129 0.92118 TEX33 0.000322690552250852 0.586449064774153 0.413228244673596 testis expressed 33 . . . . . 0.09810 . 0.685332364 85.09672092 1244.28218 6.66218 TEX35 0.00166477140275049 0.890083071332258 0.108252157264992 testis expressed 35 . . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:17077512}.; . . 0.22349 0.09299 1.26221942 93.55980184 511.03215 4.62922 TEX36 . . . testis expressed 36 . . . . . 0.05376 . 1.302692676 93.93724935 78.60792 1.87042 TEX36-AS1 . . . TEX36 antisense RNA 1 . . . . . . . . . . . TEX37 3.7065751974129e-06 0.111225493135361 0.888770800289442 testis expressed 37 . . TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:17091336}.; . . 0.12865 0.08830 0.551232944 81.48148148 417.22061 4.27526 TEX38 . . . testis expressed 38 . . . . . . . . . 2297.40006 8.87518 TEX40 0.47704330239022 0.499767502806519 0.0231891948032609 testis expressed 40 FUNCTION: May be involved in late spermatogenesis. {ECO:0000250}.; . . . . . . . . 349.80653 3.96344 TEX41 . . . testis expressed 41 (non-protein coding) . . . . . . . . . . . TEX43 . . . testis expressed 43 . . . . . . . 0.03689118 56.64071715 . . TEX101 0.000898938978228392 0.79806902984302 0.201032031178751 testis expressed 101 FUNCTION: May play a role in signal transduction and promote protein tyrosine phosphorylation. {ECO:0000250}.; . TISSUE SPECIFICITY: Detected in testis and spermatogonia. Not detected in spermatocytes. Detected in blood leukocytes. {ECO:0000269|PubMed:16516155}.; unclassifiable (Anatomical System);uterus;optic nerve;lung;heart;macula lutea;testis;fovea centralis;choroid;lens;skin;retina; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.21766 0.07619 0.016664174 55.21939137 338.7736 3.90466 TEX261 0.00019534179099528 0.479520654065687 0.520284004143317 testis expressed 261 . . . smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;iris;germinal center;bladder;brain;heart;cartilage;urinary;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;cerebral cortex;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus;cerebellum; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.27391 0.10828 -0.229483771 36.86010852 1.10092 0.02852 TEX264 0.910814338863852 0.0885176183076483 0.000668042828499178 testis expressed 264 . . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;muscle;pharynx;blood;lens;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; testis - interstitial;testis - seminiferous tubule;adrenal cortex;liver;testis;cingulate cortex;parietal lobe; 0.91783 . -0.049474214 50.01179523 1056.06416 6.23871 TF 0.00237226565881044 0.996916881861687 0.000710852479502163 transferrin FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.; DISEASE: Atransferrinemia (ATRAF) [MIM:209300]: A rare autosomal recessive disorder characterized by abnormal synthesis of transferrin leading to iron overload and microcytic hypochromic anemia. {ECO:0000269|PubMed:11110675, ECO:0000269|PubMed:15466165}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.; colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;frontal lobe;pituitary gland;testis;brain;gall bladder;unclassifiable (Anatomical System);amygdala;tongue;nervous;hypothalamus;spinal cord;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;mammary gland;stomach;cerebellum; whole brain;amygdala;dorsal root ganglion;occipital lobe;superior cervical ganglion;thalamus;medulla oblongata;adipose tissue;cerebellum peduncles;hypothalamus;spinal cord;caudate nucleus;pons;subthalamic nucleus;fetal liver;liver;prefrontal cortex;globus pallidus;appendix;fetal lung;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.62381 0.94770 -0.905656269 10.12031139 319.18799 3.79368 TFAM 0.775627181230517 0.224042035295923 0.000330783473560395 transcription factor A, mitochondrial FUNCTION: Binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation. Required for accurate and efficient promoter recognition by the mitochondrial RNA polymerase. Promotes transcription initiation from the HSP1 and the light strand promoter by binding immediately upstream of transcriptional start sites. Is able to unwind DNA. Bends the mitochondrial light strand promoter DNA into a U-turn shape via its HMG boxes. Required for maintenance of normal levels of mitochondrial DNA. May play a role in organizing and compacting mitochondrial DNA. {ECO:0000269|PubMed:1737790, ECO:0000269|PubMed:19304746, ECO:0000269|PubMed:20410300, ECO:0000269|PubMed:22037171, ECO:0000269|PubMed:22037172, ECO:0000269|PubMed:22841477}.; . . . . 0.08685 0.20247 -0.029247611 51.40363293 332.99875 3.87855 TFAMP1 . . . transcription factor A, mitochondrial pseudogene 1 . . . . . . . . . . . TFAMP2 . . . transcription factor A, mitochondrial pseudogene 2 . . . . . . . . . . . TFAP2A 0.987223276135779 0.0127713960725496 5.32779167126609e-06 transcription factor AP-2 alpha (activating enhancer binding protein 2 alpha) FUNCTION: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-alpha is the only AP-2 protein required for early morphogenesis of the lens vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1 promoter transcription activation. Associates with chromatin to the PITX2 P1 promoter region. {ECO:0000269|PubMed:11694877, ECO:0000269|PubMed:12586840}.; DISEASE: Branchiooculofacial syndrome (BOFS) [MIM:113620]: A syndrome characterized by growth retardation, bilateral branchial sinus defects with hemangiomatous, scarred skin, cleft lip with or without cleft palate, pseudocleft of the upper lip, nasolacrimal duct obstruction, low set ears with posterior rotation, a malformed, asymmetrical nose with a broad bridge and flattened tip, conductive or sensorineural deafness, ocular and renal anomalies. {ECO:0000269|PubMed:18423521}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;parathyroid;choroid;fovea centralis;skin;retina;optic nerve;iris;unclassifiable (Anatomical System);tongue;lens;breast;pancreas;lung;placenta;visual apparatus;macula lutea;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;placenta;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.96726 0.95367 -0.427900189 25.14744043 13.97787 0.50725 TFAP2A-AS1 . . . TFAP2A antisense RNA 1 . . . . . . . . . . . TFAP2B 0.990904305042869 0.00909337804411991 2.31691301068591e-06 transcription factor AP-2 beta (activating enhancer binding protein 2 beta) FUNCTION: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-beta appears to be required for normal face and limb development and for proper terminal differentiation and function of renal tubular epithelia. {ECO:0000269|PubMed:11694877}.; DISEASE: Char syndrome (CHAR) [MIM:169100]: An autosomal dominant disorder characterized by patent ductus arteriosus (PDA), facial dysmorphism and hand anomalies. {ECO:0000269|PubMed:10802654, ECO:0000269|PubMed:11505339}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;developmental;fovea centralis;choroid;lens;skin;retina;uterus;breast;optic nerve;whole body;macula lutea;visual apparatus;head and neck;kidney;mammary gland; superior cervical ganglion;subthalamic nucleus;testis;kidney;skeletal muscle;cerebellum; 0.71216 0.24706 -0.315847836 31.68789809 28.34617 0.90775 TFAP2C 0.939950974403548 0.0599989204796529 5.01051167995404e-05 transcription factor AP-2 gamma (activating enhancer binding protein 2 gamma) FUNCTION: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. {ECO:0000269|PubMed:11694877, ECO:0000269|PubMed:24413532}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;adrenal cortex;parathyroid;skin;uterus;prostate;whole body;lung;adrenal gland;thyroid;placenta;testis;head and neck;spleen;mammary gland;pineal gland; dorsal root ganglion;uterus corpus;medulla oblongata;superior cervical ganglion;placenta;temporal lobe;globus pallidus;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.90708 0.28323 -0.227663163 37.11370606 110.16629 2.28216 TFAP2D 0.981586998492109 0.0183999281899187 1.30733179728064e-05 transcription factor AP-2 delta (activating enhancer binding protein 2 delta) FUNCTION: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in brain, placenta, skeletal muscle, thymus, small intestine, and prostate, and expressed at lower levels in leukocyte, spleen, testis, ovary and colon. Barely detectable in heart, kidney, liver, lung or pancreas. {ECO:0000269|PubMed:11733187}.; macula lutea;visual apparatus;fovea centralis; . 0.75149 0.14024 0.016664174 55.21939137 509.04894 4.62407 TFAP2E 0.000972259060989771 0.811786590032971 0.187241150906039 transcription factor AP-2 epsilon (activating enhancer binding protein 2 epsilon) FUNCTION: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-epsilon may play a role in the development of the CNS and in cartilage differentiation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in skin, primary keratinocytes, immortalized keratinocytes, and HeLa cell line. {ECO:0000269|PubMed:14636996}.; . . 0.15776 0.11613 . . 421.76469 4.29014 TFAP4 0.978529176157973 0.0214517397894141 1.90840526131991e-05 transcription factor AP-4 (activating enhancer binding protein 4) FUNCTION: Transcription factor that activates both viral and cellular genes by binding to the symmetrical DNA sequence 5'- CAGCTG-3'.; . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;lung;frontal lobe;placenta;visual apparatus;liver;testis;cervix;spleen;kidney;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.34654 . 0.082802743 60.09082331 176.04161 2.88640 TFB1M 1.15656604217462e-05 0.815763282796501 0.184225151543077 transcription factor B1, mitochondrial FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity. {ECO:0000269|PubMed:11809803, ECO:0000269|PubMed:12068295, ECO:0000269|PubMed:12897151}.; DISEASE: Note=Variations in TFB1M may influence the clinical expression of aminoglycoside-induced deafness caused by the A1555G mutation in the mitochondrial 12S rRNA.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12068295}.; . . 0.20249 0.10327 0.262810045 70.43524416 129.0857 2.47609 TFB2M 9.61899524222107e-05 0.938691525661549 0.0612122843860287 transcription factor B2, mitochondrial FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity. Compared to TFB1M, it activates transcription of mitochondrial DNA more efficiently, while it has less methyltransferase activity. {ECO:0000269|PubMed:12068295, ECO:0000269|PubMed:12897151, ECO:0000269|PubMed:15526033, ECO:0000269|PubMed:20410300}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12068295}.; . . 0.04866 0.05972 -0.135838822 43.77211607 84.41517 1.95562 TFCP2 0.000102418586669595 0.997243551882625 0.00265402953070509 transcription factor CP2 FUNCTION: Binds a variety of cellular and viral promoters including fibrinogen, alpha-globin, SV40 and HIV-1 promoters. Activation of the alpha-globin promoter in erythroid cells is via synergistic interaction with UBP1 (By similarity). Functions as part of the SSP (stage selector protein) complex. Facilitates the interaction of the gamma-globin genes with enhancer elements contained in the locus control region in fetal erythroid cells. Interacts by binding to the stage selector element (SSE) in the proximal gamma-globin promoter. {ECO:0000250, ECO:0000269|PubMed:10455131, ECO:0000269|PubMed:1732747, ECO:0000269|PubMed:8035790, ECO:0000269|PubMed:8157699}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in brain, ovary, kidney, thymus, spleen, liver, adrenal, heart and lung (at protein level). {ECO:0000269|PubMed:10455131, ECO:0000269|PubMed:7828600, ECO:0000269|PubMed:8157699}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;epididymis;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - interstitial;occipital lobe;ciliary ganglion;pons;atrioventricular node;caudate nucleus;trigeminal ganglion; 0.74555 0.24705 -0.449946534 24.00330267 10.97248 0.39662 TFCP2L1 0.999192586615908 0.000807412112885351 1.27120695004053e-09 transcription factor CP2-like 1 FUNCTION: Transcriptional suppressor. May suppress UBP1-mediated transcriptional activation. Required for normal duct development in the salivary gland and kidney (By similarity). Modulates the placental expression of CYP11A1. {ECO:0000250, ECO:0000269|PubMed:10644752}.; . TISSUE SPECIFICITY: Highly expressed in placental JEG-3 cells and very low levels of expression in non-steroidogenic cells. No expression was seen in adrenal NCI-H295A cells or in adrenal tissue. {ECO:0000269|PubMed:10644752}.; unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;colon;blood;bone marrow;breast;prostate;lung;thyroid;placenta;liver;spleen;kidney; superior cervical ganglion;ciliary ganglion;kidney;atrioventricular node; 0.12962 0.10362 -0.400392389 26.85185185 222.44013 3.22468 TFDP1 0.963153120498646 0.0368321399533043 1.47395480492266e-05 transcription factor Dp-1 FUNCTION: Can stimulate E2F-dependent transcription. Binds DNA cooperatively with E2F family members through the E2 recognition site, 5'-TTTC[CG]CGC-3', found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The E2F1:DP complex appears to mediate both cell proliferation and apoptosis. Blocks adipocyte differentiation by repressing CEBPA binding to its target gene promoters (PubMed:20176812). {ECO:0000269|PubMed:20176812}.; . TISSUE SPECIFICITY: Highest levels in muscle. Also expressed in brain, placenta, liver and kidney. Lower levels in lung and pancreas. Not detected in heart.; . . 0.20313 0.27160 -1.023168368 7.944090587 22.85221 0.76242 TFDP1P . . . transcription factor Dp-1 pseudogene . . . . . . . . . . . TFDP2 0.975087598074196 0.0249112715656236 1.13036018013852e-06 transcription factor Dp-2 (E2F dimerization partner 2) FUNCTION: Can stimulate E2F-dependent transcription. Binds DNA cooperatively with E2F family members through the E2 recognition site, 5'-TTTC[CG]CGC-3', found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The TFDP2:E2F complex functions in the control of cell-cycle progression from G1 to S phase. The E2F1:DP complex appears to mediate both cell proliferation and apoptosis. Blocks adipocyte differentiation by repressing CEBPA binding to its target gene promoters (PubMed:20176812). {ECO:0000305|PubMed:20176812}.; . TISSUE SPECIFICITY: High levels in heart and skeletal muscle. Also found in placenta, kidney, brain, lung and liver. The presence as well as the abundance of the different transcripts appear to vary significantly in different tissues and cell lines.; medulla oblongata;umbilical cord;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;oesophagus;bone;thyroid;pituitary gland;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;cerebellum;thymus; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;tumor;testis;trigeminal ganglion;thymus;bone marrow; 0.96272 0.18236 -0.139478553 43.29440906 42.91096 1.24214 TFDP3 2.30492302905471e-06 0.0850669346896548 0.914930760387316 transcription factor Dp family member 3 FUNCTION: Competitive inhibitor of E2F-mediated transactivation activity. Impairs E2F-mediated cell-cycle progression from G(1) to S phase. {ECO:0000269|PubMed:16418725, ECO:0000269|PubMed:17062573, ECO:0000269|PubMed:20559320}.; . TISSUE SPECIFICITY: Predominantly expressed in testis. Low level of expression in pancreas. Highly expressed in ovarian and colon cancer cell lines. {ECO:0000269|PubMed:12097419, ECO:0000269|PubMed:16418725}.; . . 0.05413 0.05691 0.729426781 86.17008728 225.71159 3.24760 TFE3 0.973742209543687 0.0262264345185738 3.13559377397092e-05 transcription factor binding to IGHM enhancer 3 FUNCTION: Transcription factor that specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFEB or MITF. In association with TFEB, activates the expression of CD40L in T-cells, thereby playing a role in T- cell-dependent antibody responses in activated CD4(+) T-cells and thymus-dependent humoral immunity. Specifically recognizes the MUE3 box, a subset of E-boxes, present in the immunoglobulin enhancer. It also binds very well to a USF/MLTF site.; DISEASE: Note=A chromosomal aberration involving TFE3 is found in patients with alveolar soft part sarcoma. Translocation t(X;17)(p11;q25) with ASPSCR1 forms a ASPSCR1-TFE3 fusion protein. {ECO:0000269|PubMed:11358836}.; DISEASE: Note=Chromosomal aberrations involving TFE3 are found in patients with papillary renal cell carcinoma. Translocation t(X;1)(p11.2;q21.2) with PRCC; translocation t(X;1)(p11.2;p34) with PSF; inversion inv(X)(p11.2;q12) that fuses NONO to TFE3. {ECO:0000269|PubMed:8872474, ECO:0000269|PubMed:8986805}.; TISSUE SPECIFICITY: Ubiquitous in fetal and adult tissues.; smooth muscle;ovary;colon;choroid;skin;retina;uterus;prostate;endometrium;larynx;gum;bone;testis;germinal center;spinal ganglion;ciliary body;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;breast;pancreas;lung;placenta;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;cingulate cortex; 0.60298 0.24170 0.505321956 80.00707714 43.40948 1.25339 TFEB 0.968857337769685 0.0311329577903229 9.70443999238733e-06 transcription factor EB FUNCTION: Transcription factor that specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFE3 or MITF. In association with TFE3, activates the expression of CD40L in T-cells, thereby playing a role in T- cell-dependent antibody responses in activated CD4(+) T-cells and thymus-dependent humoral immunity. Specifically recognizes and binds the CLEAR-box sequence (5'-GTCACGTGAC-3') present in the regulatory region of many lysosomal genes, leading to activate their expression. It thereby plays a central role in expression of lysosomal genes. Acts as a positive regulator of autophagy by promoting expression of genes involved in autophagy. Specifically recognizes the gamma-E3 box, a subset of E-boxes, present in the heavy-chain immunoglobulin enhancer. Plays a role in the signal transduction processes required for normal vascularization of the placenta. {ECO:0000269|PubMed:19556463, ECO:0000269|PubMed:23434374}.; . . lymphoreticular;colon;fovea centralis;choroid;bone marrow;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;oesophagus;larynx;thyroid;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;hippocampus;visual apparatus;duodenum;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;whole blood;trigeminal ganglion; 0.30823 0.17188 -0.602450568 17.91106393 119.104 2.37478 TFEC 4.73106154908356e-05 0.86213122610398 0.137821463280529 transcription factor EC FUNCTION: Transcriptional regulator that acts as a repressor or an activator. Acts as a transcriptional repressor on minimal promoter containing element F (that includes an E-box sequence). Binds to element F in an E-box sequence-specific manner. Acts as a transcriptional transactivator on the proximal promoter region of the tartrate-resistant acid phosphatase (TRAP) E-box containing promoter (By similarity). Collaborates with MITF in target gene activation (By similarity). Acts as a transcriptional repressor on minimal promoter containing mu E3 enhancer sequence (By similarity). Binds to mu E3 DNA sequence of the immunoglobulin heavy-chain gene enhancer (By similarity). Binds DNA in a homo- or heterodimeric form. {ECO:0000250, ECO:0000269|PubMed:11467950, ECO:0000269|PubMed:9256061}.; . TISSUE SPECIFICITY: Expressed moderately in spleen, kidney, bone marrow, small intestine and leukocytes. Expressed weakly in testis, trachea and colon. {ECO:0000269|PubMed:11467950, ECO:0000269|PubMed:15118077}.; unclassifiable (Anatomical System);ovary;adrenal cortex;blood;parathyroid;skeletal muscle;bone marrow;lung;endometrium;adrenal gland;placenta;thyroid;testis;kidney;brain;pineal gland; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.28770 0.18291 0.260991686 70.25831564 212.26623 3.14287 TFF1 0.00630356016196767 0.505895453691939 0.487800986146093 trefoil factor 1 FUNCTION: Stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. May inhibit the growth of calcium oxalate crystals in urine. {ECO:0000269|PubMed:16308573}.; . TISSUE SPECIFICITY: Found in stomach, with highest levels in the upper gastric mucosal cells (at protein level). Detected in goblet cells of the small and large intestine and rectum, small submucosal glands in the esophagus, mucous acini of the sublingual gland, submucosal glands of the trachea, and epithelial cells lining the exocrine pancreatic ducts but not in the remainder of the pancreas (at protein level). Scattered expression is detected in the epithelial cells of the gallbladder and submucosal glands of the vagina, and weak expression is observed in the bronchial goblet cells of the pseudostratified epithelia in the respiratory system (at protein level). Detected in urine (at protein level). Strongly expressed in breast cancer but at low levels in normal mammary tissue. It is regulated by estrogen in MCF-7 cells. Strong expression found in normal gastric mucosa and in the regenerative tissues surrounding ulcerous lesions of gastrointestinal tract, but lower expression found in gastric cancer (at protein level). {ECO:0000269|PubMed:15924415, ECO:0000269|PubMed:16308573, ECO:0000269|PubMed:16718800, ECO:0000269|PubMed:17143957, ECO:0000269|PubMed:17242463, ECO:0000269|PubMed:3041593, ECO:0000269|PubMed:3838275}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;pancreas;lung;cornea;cerebral cortex;visual apparatus;liver;head and neck;kidney;brain;mammary gland;bladder;stomach; superior cervical ganglion;trigeminal ganglion; 0.12999 0.25471 0.525552348 80.57914603 28.67165 0.91816 TFF2 0.000144473936588797 0.419748836501908 0.580106689561504 trefoil factor 2 FUNCTION: Inhibits gastrointestinal motility and gastric acid secretion. Could function as a structural component of gastric mucus, possibly by stabilizing glycoproteins in the mucus gel through interactions with carbohydrate side chains (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Stomach.; unclassifiable (Anatomical System);ovary;thyroid;colon;head and neck;kidney;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.09090 0.21453 0.547599505 81.2160887 73.67066 1.79390 TFF3 0.0856870201255524 0.760707050885396 0.153605928989051 trefoil factor 3 FUNCTION: Involved in the maintenance and repair of the intestinal mucosa. Promotes the mobility of epithelial cells in healing processes (motogen). {ECO:0000269|PubMed:11694446}.; . TISSUE SPECIFICITY: Expressed in goblet cells of the intestines and colon (at protein level). Expressed by goblet cells of small and large intestinal epithelia and also by the uterus. Also expressed in the hypothalamus where it is detected in paraventricular, periventricular and supraoptic nuclei (at protein level). {ECO:0000269|PubMed:8346203, ECO:0000269|PubMed:8454642}.; ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;prostate;endometrium;thyroid;testis;brain;bladder;pineal gland;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;pancreas;trachea;thyroid;atrioventricular node;fetal thyroid; 0.16262 . 0.391453969 75.87284737 28.49508 0.91268 TFG 0.757056423125628 0.242859231347927 8.43455264445544e-05 TRK-fused gene FUNCTION: Plays a role in the normal dynamic function of the endoplasmic reticulum (ER) and its associated microtubules. {ECO:0000269|PubMed:23479643}.; DISEASE: Neuropathy, hereditary motor and sensory, Okinawa type (HMSNO) [MIM:604484]: A neurodegenerative disorder characterized by young adult onset of proximal muscle weakness and atrophy, muscle cramps, and fasciculations, with later onset of distal sensory impairment. The disorder is slowly progressive and clinically resembles amyotrophic lateral sclerosis. {ECO:0000269|PubMed:22883144}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spastic paraplegia 57, autosomal recessive (SPG57) [MIM:615658]: A complicated form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. Complicated forms are recognized by additional variable features including spastic quadriparesis, seizures, dementia, amyotrophy, extrapyramidal disturbance, cerebral or cerebellar atrophy, optic atrophy, and peripheral neuropathy, as well as by extra neurological manifestations. {ECO:0000269|PubMed:23479643}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; ovary;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;thymus; amygdala;thyroid;placenta;testis; 0.15375 0.24697 -0.22584292 37.32012267 55.5296 1.49749 TFIP11 1.96788418936719e-06 0.993647861447324 0.00635017066848655 tuftelin interacting protein 11 FUNCTION: Involved in pre-mRNA splicing, specifically in spliceosome disassembly during late-stage splicing events. Intron turnover seems to proceed through reactions in two lariat-intron associated complexes termed Intron Large (IL) and Intron Small (IS). In cooperation with DHX15 seems to mediate the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns. May play a role in the differentiation of ameloblasts and odontoblasts or in the forming of the enamel extracellular matrix. {ECO:0000269|PubMed:19103666}.; . . . . 0.17486 0.11762 -1.524862616 3.42061807 160.57464 2.76594 TFP1 . . . transferrin pseudogene 1 . . . . . . . . . . . TFPI 0.0253229555895134 0.961709940855754 0.0129671035547326 tissue factor pathway inhibitor FUNCTION: Inhibits factor X (X(a)) directly and, in a Xa-dependent way, inhibits VIIa/tissue factor activity, presumably by forming a quaternary Xa/LACI/VIIa/TF complex. It possesses an antithrombotic action and also the ability to associate with lipoproteins in plasma.; . TISSUE SPECIFICITY: Mostly in endothelial cells.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;optic nerve;bone;testis;unclassifiable (Anatomical System);heart;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;stomach;aorta; dorsal root ganglion;medulla oblongata;fetal liver;superior cervical ganglion;subthalamic nucleus;placenta;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.30818 0.32077 0.327131069 73.27199811 39.81837 1.17294 TFPI2 0.237365841602754 0.730418481825753 0.0322156765714934 tissue factor pathway inhibitor 2 FUNCTION: May play a role in the regulation of plasmin-mediated matrix remodeling. Inhibits trypsin, plasmin, factor VIIa/tissue factor and weakly factor Xa. Has no effect on thrombin. {ECO:0000269|PubMed:7872799}.; . TISSUE SPECIFICITY: Umbilical vein endothelial cells, liver, placenta, heart, pancreas, and maternal serum at advanced pregnancy.; ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;uterus;prostate;whole body;endometrium;bone;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;pharynx;blood;greater omentum;bile duct;breast;lung;cornea;trabecular meshwork;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; smooth muscle;lung;heart;placenta;beta cell islets;appendix;trigeminal ganglion; 0.31619 0.17731 0.549415813 81.38122199 42.26702 1.23033 TFPT 0.000191370472971955 0.713934352070574 0.285874277456454 TCF3 (E2A) fusion partner (in childhood Leukemia) FUNCTION: Appears to promote apoptosis in a p53/TP53-independent manner.; DISEASE: Note=A chromosomal aberration involving TFPT is a cause of pre-B-cell acute lymphoblastic leukemia (B-ALL). Inversion inv(19)(p13;q13) with TCF3. {ECO:0000269|PubMed:10086727}.; . . . 0.17443 0.27129 -0.137658575 43.57159707 102.84128 2.19185 TFR2 0.000139030759104317 0.998145898983954 0.00171507025694183 transferrin receptor 2 FUNCTION: Mediates cellular uptake of transferrin-bound iron in a non-iron dependent manner. May be involved in iron metabolism, hepatocyte function and erythrocyte differentiation.; . TISSUE SPECIFICITY: Predominantly expressed in liver. While the alpha form is also expressed in spleen, lung, muscle, prostate and peripheral blood mononuclear cells, the beta form is expressed in all tissues tested, albeit weakly.; unclassifiable (Anatomical System);breast;lymph node;lung;bone;placenta;liver;spleen;germinal center;brain;stomach;cerebellum; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;fetal liver;liver;ciliary ganglion;fetal lung;atrioventricular node;cingulate cortex;skeletal muscle; 0.39743 . -0.525400547 20.91295117 435.257 4.35079 TFRC 0.780323176637487 0.219674233799699 2.58956281420186e-06 transferrin receptor FUNCTION: Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. {ECO:0000250, ECO:0000269|PubMed:3568132}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; fetal liver;placenta;tumor; 0.45148 0.79857 -0.709045403 14.673272 1218.14798 6.60185 TG 2.62956477021395e-29 0.999552448419579 0.000447551580421231 thyroglobulin FUNCTION: Precursor of the iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3).; DISEASE: Thyroid dyshormonogenesis 3 (TDH3) [MIM:274700]: A disorder due to thyroid dyshormonogenesis, causing large goiters of elastic and soft consistency in the majority of patients. Although the degree of thyroid dysfunction varies considerably among patients with defective thyroglobulin synthesis, patients usually have a relatively high serum free triiodothyronine (T3) concentration with disproportionately low free tetraiodothyronine (T4) level. The maintenance of relatively high free T3 levels prevents profound tissue hypothyroidism except in brain and pituitary, which are dependent on T4 supply, resulting in neurologic and intellectual defects in some cases. {ECO:0000269|PubMed:10199792, ECO:0000269|PubMed:16477365, ECO:0000269|PubMed:17244789, ECO:0000269|PubMed:17532758, ECO:0000269|PubMed:19509106}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Autoimmune thyroid disease 3 (AITD3) [MIM:608175]: A complex autoimmune disorder comprising two related diseases affecting the thyroid: Graves disease and Hashimoto thyroiditis. In both disorders, thyroid-reactive T-cells are formed and infiltrate the thyroid gland. In Graves disease, the majority of the T-cells undergo a Th2 differentiation and activate B-cells to produce antibodies against the TSH receptor, which stimulate the thyroid and cause clinical hyperthyroidism. In contrast, Hashimoto thyroiditis is characterized by Th1 switching of the thyroid- infiltrating T-cells, which induces apoptosis of thyroid follicular cells and clinical hypothyroidism. {ECO:0000269|PubMed:14657345}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Thyroid gland specific.; prostate;tongue;larynx;thyroid;liver;hypopharynx;colon;head and neck;skeletal muscle; superior cervical ganglion;lymph node;thyroid;globus pallidus;ciliary ganglion;atrioventricular node;fetal thyroid;skeletal muscle; 0.10882 . 1.573473784 95.71243218 6797.58378 17.53505 TGCT1 . . . testicular germ cell tumor susceptibility 1 . . . . . . . . . . . TGDS 8.78036163423323e-06 0.765575523684583 0.234415695953783 TDP-glucose 4,6-dehydratase . DISEASE: Catel-Manzke syndrome (CATMANS) [MIM:616145]: A syndrome characterized by Pierre Robin sequence and a unique form of bilateral hyperphalangy causing a clinodactyly of the index finger. Pierre Robin sequence includes an opening in the roof of the mouth (a cleft palate), a large tongue (macroglossia), and a small lower jaw (micrognathia). {ECO:0000269|PubMed:25480037}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;vein;skin;uterus;prostate;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.23284 0.22502 -0.249709319 35.74545883 36.19789 1.08510 TGFA 0.574368121554422 0.414377943538861 0.0112539349067169 transforming growth factor alpha FUNCTION: TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar.; . TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 4 are expressed in keratinocytes and tumor-derived cell lines. {ECO:0000269|PubMed:10523832}.; unclassifiable (Anatomical System);smooth muscle;islets of Langerhans;colon;blood;choroid;skin;skeletal muscle;retina;bone marrow;breast;pancreas;lung;cerebral cortex;thyroid;testis;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex;cerebellum; 0.52869 0.74991 -0.139478553 43.29440906 127.60185 2.46315 TGFA-IT1 . . . TGFA intronic transcript 1 . . . . . . . . . . . TGFB1 0.354132528348928 0.643175158985919 0.00269231266515257 transforming growth factor beta 1 FUNCTION: Multifunctional protein that controls proliferation, differentiation and other functions in many cell types. Many cells synthesize TGFB1 and have specific receptors for it. It positively and negatively regulates many other growth factors. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Can promote either T- helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner. At high concentrations, leads to FOXP3-mediated suppression of RORC and down-regulation of IL-17 expression, favoring Treg cell development. At low concentrations in concert with IL-6 and IL-21, leads to expression of the IL-17 and IL-23 receptors, favoring differentiation to Th17 cells. {ECO:0000250|UniProtKB:P04202}.; DISEASE: Camurati-Engelmann disease (CAEND) [MIM:131300]: An autosomal dominant disorder characterized by hyperostosis and sclerosis of the diaphyses of long bones. The disease typically presents in early childhood with pain, muscular weakness and waddling gait, and in some cases other features such as exophthalmos, facial paralysis, hearing difficulties and loss of vision. {ECO:0000269|PubMed:10973241, ECO:0000269|PubMed:11062463, ECO:0000269|PubMed:15103729}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in bone. Abundantly expressed in articular cartilage and chondrocytes and is increased in osteoarthritis (OA). Colocalizes with ASPN in chondrocytes within OA lesions of articular cartilage. {ECO:0000269|PubMed:11746498, ECO:0000269|PubMed:17827158}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;urinary;adrenal cortex;blood;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; subthalamic nucleus;heart;testis - seminiferous tubule;placenta;globus pallidus;white blood cells;ciliary ganglion;pons;atrioventricular node;whole blood;skeletal muscle; 0.72068 0.99841 -0.117432389 44.89266336 472.6638 4.49902 TGFB1I1 0.0749169191152651 0.922613804251886 0.00246927663284876 transforming growth factor beta 1 induced transcript 1 FUNCTION: Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA- binding activity. {ECO:0000269|PubMed:10075738, ECO:0000269|PubMed:11463817, ECO:0000269|PubMed:11856738, ECO:0000269|PubMed:12177201, ECO:0000269|PubMed:12445807, ECO:0000269|PubMed:12700349, ECO:0000269|PubMed:15211577, ECO:0000269|PubMed:15561701, ECO:0000269|PubMed:16141357, ECO:0000269|PubMed:16624805, ECO:0000269|PubMed:16803896, ECO:0000269|PubMed:16849583, ECO:0000269|PubMed:17166536, ECO:0000269|PubMed:17233630, ECO:0000269|PubMed:9032249}.; . TISSUE SPECIFICITY: Expressed in platelets, smooth muscle and prostate stromal cells (at protein level). {ECO:0000269|PubMed:10075738, ECO:0000269|PubMed:10708479, ECO:0000269|PubMed:11311131, ECO:0000269|PubMed:12642630, ECO:0000269|PubMed:12772188, ECO:0000269|PubMed:16849583, ECO:0000269|PubMed:17166536, ECO:0000269|PubMed:17233630, ECO:0000269|PubMed:9664039}.; medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;choroid;skin;uterus;prostate;whole body;oesophagus;endometrium;larynx;bone;iris;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;muscle;pharynx;blood;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; uterus;superior cervical ganglion;heart; 0.82014 0.14054 -0.47017169 23.25430526 165.58108 2.81491 TGFB2 0.9891155078203 0.010880895651519 3.59652818061431e-06 transforming growth factor beta 2 FUNCTION: TGF-beta 2 has suppressive effects on interleukin-2 dependent T-cell growth.; DISEASE: Note=A chromosomal aberration involving TGFB2 is found in a family with Peters anomaly. Translocation t(1;7)(q41;p21) with HDAC9. {ECO:0000269|PubMed:12706107}.; DISEASE: Loeys-Dietz syndrome 4 (LDS4) [MIM:614816]: An aortic aneurysm syndrome with widespread systemic involvement. LDS4 is characterized by arterial tortuosity, aortic dissection, intracranial aneurysm and subarachnoid hemorrhage, hypertelorism, bifid uvula, pectus deformity, bicuspid aortic valve, arachnodactyly, scoliosis, foot deformities, dural ectasia, joint hyperflexibility, and thin skin with easy bruising and striae. {ECO:0000269|PubMed:22772368}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in TGFB2 may be a cause of non-syndromic aortic disease (NSAD). NSAD is a frequently asymptomatic but potentially lethal disease characterized by thoracic aortic aneurysms and dissections without additional syndromic features. {ECO:0000269|PubMed:25046559}.; . . . 0.64721 0.87580 -0.049474214 50.01179523 21.45278 0.72395 TGFB2-AS1 . . . TGFB2 antisense RNA 1 (head to head) . . . . . . . . . . . TGFB2-OT1 . . . TGFB2 overlapping transcript 1 . . . . . . . . . . . TGFB3 0.92271748369888 0.0771874757348252 9.50405662946285e-05 transforming growth factor beta 3 FUNCTION: Involved in embryogenesis and cell differentiation.; DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 1 (ARVD1) [MIM:107970]: A congenital heart disease characterized by infiltration of adipose and fibrous tissue into the right ventricle and loss of myocardial cells, resulting in ventricular and supraventricular arrhythmias. {ECO:0000269|PubMed:15639475}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Loeys-Dietz syndrome 5 (LDS5) [MIM:615582]: A form of Loeys-Dietz syndrome, a syndrome with widespread systemic involvement characterized by arterial tortuosity and aneurysms, hypertelorism, and bifid uvula or cleft palate. LDS5 additional variable features include mitral valve disease, skeletal overgrowth, cervical spine instability, and clubfoot deformity. LDS5 patients do not manifest remarkable aortic or arterial tortuosity, and there is no strong evidence for early aortic dissection. {ECO:0000269|PubMed:23824657}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;tongue;islets of Langerhans;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;pons;trigeminal ganglion; 0.76045 0.78373 -0.60427181 17.74593064 44.57548 1.27925 TGFBI 0.00372244046527813 0.994448931243616 0.00182862829110589 transforming growth factor beta induced FUNCTION: Binds to type I, II, and IV collagens. This adhesion protein may play an important role in cell-collagen interactions. In cartilage, may be involved in endochondral bone formation.; DISEASE: Corneal dystrophy, epithelial basement membrane (EBMD) [MIM:121820]: A bilateral anterior corneal dystrophy characterized by grayish epithelial fingerprint lines, geographic map-like lines, and dots (or microcysts) on slit-lamp examination. Pathologic studies show abnormal, redundant basement membrane and intraepithelial lacunae filled with cellular debris. {ECO:0000269|PubMed:16652336}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, Groenouw type 1 (CDGG1) [MIM:121900]: A rare form of stromal corneal dystrophy characterized by multiple small deposits in the superficial central corneal stroma, and progressive visual impairment. {ECO:0000269|PubMed:15623763}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, lattice type 1 (CDL1) [MIM:122200]: A form of lattice corneal dystrophy, a class of inherited stromal amyloidoses characterized by pathognomonic branching lattice figures in the cornea. CDL1 is characterized by progressive visual impairment, and the presence of delicate, double-contoured, interdigitating, elongated deposits that form a reticular pattern in the corneal stroma. Systemic amyloidosis is absent. Recurrent corneal ulceration sometimes occurs. {ECO:0000269|PubMed:10837380, ECO:0000269|PubMed:11413411, ECO:0000269|PubMed:14597039, ECO:0000269|PubMed:15531312, ECO:0000269|PubMed:15623763, ECO:0000269|PubMed:15838722, ECO:0000269|PubMed:16541014, ECO:0000269|PubMed:17013691, ECO:0000269|PubMed:9799082}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, Thiel-Behnke type (CDTB) [MIM:602082]: A bilateral disorder of the cornea characterized by progressive honeycomb-like, subepithelial corneal opacities with recurrent erosions. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, Reis-Bucklers type (CDRB) [MIM:608470]: A bilateral disorder of the cornea characterized by intermittent attacks of ocular irritation, recurrent painful corneal erosions starting in childhood, corneal opacities in a geographic pattern at the level of the Bowman layer, and a progressive decrease of visual acuity. The lesions are primarily in Bowman membrane with secondary involvement of the epithelium and superficial part of the stroma. Bowman membrane is almost completely replaced by pathologic materials including disoriented collagen fibrils. {ECO:0000269|PubMed:10660331, ECO:0000269|PubMed:15623763, ECO:0000269|PubMed:9780098}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, lattice type 3A (CDL3A) [MIM:608471]: A form of lattice corneal dystrophy, a class of inherited stromal amyloidoses characterized by pathognomonic branching lattice figures in the cornea. CDL3A is characterized by decreased visual acuity, and the presence of thick, ropy branching lattice lines and accumulations of amyloid deposits in the corneal stroma. Systemic amyloidosis is absent. CDL3A clinically resembles to lattice corneal dystrophy type 3, but differs in that its age of onset is 70 to 90 years. It has an autosomal dominant inheritance pattern. {ECO:0000269|PubMed:15790870, ECO:0000269|PubMed:9497262}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, Avellino type (CDA) [MIM:607541]: A corneal disease resulting in reduced visual acuity and characterized by gray, crumb-like granular deposits in the anterior third of the stroma in each corneal button. Fusiform amyloid deposits, histochemically and morphologically identical to those of lattice corneal dystrophy, are found in the deeper stroma. Additional features include recurrent corneal erosions, and glare and decreased night vision. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in the corneal epithelium. {ECO:0000269|PubMed:8077289}.; smooth muscle;salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;synovium;bone;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;lens;pancreas;lung;cornea;mesenchyma;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;aorta; smooth muscle;heart; 0.49297 0.70714 -0.661316159 16.02382637 262.53316 3.47583 TGFBR1 0.948697388130312 0.0512957820236531 6.8298460344921e-06 transforming growth factor beta receptor I FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non- canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation. {ECO:0000269|PubMed:15761148, ECO:0000269|PubMed:16754747, ECO:0000269|PubMed:18758450, ECO:0000269|PubMed:7774578, ECO:0000269|PubMed:8752209, ECO:0000269|PubMed:8980228, ECO:0000269|PubMed:9346908}.; DISEASE: Loeys-Dietz syndrome 1 (LDS1) [MIM:609192]: An aortic aneurysm syndrome with widespread systemic involvement, characterized by arterial tortuosity and aneurysms, hypertelorism, and bifid uvula or cleft palate. Physical findings include prominent joint laxity, easy bruising, wide and atrophic scars, velvety and translucent skin with easily visible veins, spontaneous rupture of the spleen or bowel, and catastrophic complications of pregnancy, including rupture of the gravid uterus and the arteries, either during pregnancy or in the immediate postpartum period. Some patients have craniosynostosis, exotropy, micrognathia and retrognathia, structural brain abnormalities, and intellectual deficit. {ECO:0000269|PubMed:15731757, ECO:0000269|PubMed:16596670, ECO:0000269|PubMed:16791849, ECO:0000269|PubMed:16928994, ECO:0000269|PubMed:19883511, ECO:0000269|PubMed:22113417}. Note=The disease is caused by mutations affecting the gene represented in this entry. TGFBR1 mutation Gln-487 has been reported to be associated with thoracic aortic aneurysms and dissection (TAAD) (PubMed:16791849). This phenotype, also known as thoracic aortic aneurysms type 5 (AAT5), is distinguised from LDS1 by having aneurysms restricted to thoracic aorta. It is unclear, however, if this condition is fulfilled in individuals bearing Gln-487 mutation, that is why they are considered as LDS1 by the OMIM resource. {ECO:0000269|PubMed:16791849}.; DISEASE: Multiple self-healing squamous epithelioma (MSSE) [MIM:132800]: A disorder characterized by multiple skin tumors that undergo spontaneous regression. Tumors appear most often on sun-exposed regions, are locally invasive, and undergo spontaneous resolution over a period of months leaving pitted scars. {ECO:0000269|PubMed:21358634}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in all tissues examined, most abundant in placenta and least abundant in brain and heart.; . . 0.99892 0.77849 -0.271755481 34.31823543 16.73502 0.58837 TGFBR2 0.0355927009989093 0.956557158954957 0.00785014004613348 transforming growth factor beta receptor II FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non- promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non- canonical, SMAD-independent TGF-beta signaling pathways. {ECO:0000269|PubMed:7774578}.; DISEASE: Hereditary non-polyposis colorectal cancer 6 (HNPCC6) [MIM:614331]: An autosomal dominant disease associated with marked increase in cancer susceptibility. It is characterized by a familial predisposition to early-onset colorectal carcinoma (CRC) and extra-colonic tumors of the gastrointestinal, urological and female reproductive tracts. HNPCC is reported to be the most common form of inherited colorectal cancer in the Western world. Clinically, HNPCC is often divided into two subgroups. Type I is characterized by hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon. Type II is characterized by increased risk for cancers in certain tissues such as the uterus, ovary, breast, stomach, small intestine, skin, and larynx in addition to the colon. Diagnosis of classical HNPCC is based on the Amsterdam criteria: 3 or more relatives affected by colorectal cancer, one a first degree relative of the other two; 2 or more generation affected; 1 or more colorectal cancers presenting before 50 years of age; exclusion of hereditary polyposis syndromes. The term 'suspected HNPCC' or 'incomplete HNPCC' can be used to describe families who do not or only partially fulfill the Amsterdam criteria, but in whom a genetic basis for colon cancer is strongly suspected. {ECO:0000269|PubMed:9590282}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the esophagus. The most common types are esophageal squamous cell carcinoma and adenocarcinoma. Cancer of the esophagus remains a devastating disease because it is usually not detected until it has progressed to an advanced incurable stage. {ECO:0000269|PubMed:10789724}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Loeys-Dietz syndrome 2 (LDS2) [MIM:610168]: An aortic aneurysm syndrome with widespread systemic involvement, characterized by arterial tortuosity and aneurysms, hypertelorism, and bifid uvula or cleft palate. Physical findings include prominent joint laxity, easy bruising, wide and atrophic scars, velvety and translucent skin with easily visible veins, spontaneous rupture of the spleen or bowel, and catastrophic complications of pregnancy, including rupture of the gravid uterus and the arteries, either during pregnancy or in the immediate postpartum period. Some patients have craniosynostosis, exotropy, micrognathia and retrognathia, structural brain abnormalities, and intellectual deficit. {ECO:0000269|PubMed:15235604, ECO:0000269|PubMed:15731757, ECO:0000269|PubMed:16027248, ECO:0000269|PubMed:16251899, ECO:0000269|PubMed:19883511, ECO:0000269|PubMed:20101701, ECO:0000269|PubMed:20358619, ECO:0000269|PubMed:21949523, ECO:0000269|PubMed:22113417}. Note=The disease is caused by mutations affecting the gene represented in this entry. TGFBR2 mutations Cys-460 and His-460 have been reported to be associated with thoracic aortic aneurysms and dissection (TAAD). This phenotype, also known as thoracic aortic aneurysms type 3 (AAT3), is distinguised from LDS2 by having aneurysms restricted to thoracic aorta. As individuals carrying these mutations also exhibit descending aortic disease and aneurysms of other arteries (PubMed:16027248), they have been considered as LDS2 by the OMIM resource. {ECO:0000269|PubMed:16027248}.; . myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;gum;thyroid;germinal center;brain;heart;cartilage;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;oesophagus;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;amnion;head and neck;kidney;stomach;aorta; superior cervical ganglion;adipose tissue;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.97598 0.81410 -0.045835247 50.34206181 86.91008 1.99095 TGFBR3 0.0110547982037593 0.988868727666056 7.64741301849374e-05 transforming growth factor beta receptor III FUNCTION: Binds to TGF-beta. Could be involved in capturing and retaining TGF-beta for presentation to the signaling receptors.; . . medulla oblongata;ovary;salivary gland;intestine;colon;retina;bone marrow;prostate;whole body;frontal lobe;cochlea;endometrium;iris;testis;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;ovary;placenta; 0.60026 0.35923 0.181903047 66.2361406 1518.25778 7.24298 TGFBR3L . . . transforming growth factor beta receptor III like . . . . . . . . . 120.44878 2.39054 TGFBRAP1 0.129423465806074 0.870378794938561 0.000197739255365842 transforming growth factor beta receptor associated protein 1 FUNCTION: Plays a role in the TGF-beta/activin signaling pathway. It associates with inactive heteromeric TGF-beta and activin receptor complexes, mainly through the type II receptor, and is released upon activation of signaling. May recruit SMAD4 to the vicinity of the receptor complex and facilitate its interaction with receptor-regulated Smads, such as SMAD2. {ECO:0000269|PubMed:11278302, ECO:0000269|PubMed:9545258}.; . . unclassifiable (Anatomical System);islets of Langerhans;muscle;choroid;skin;skeletal muscle;retina;breast;prostate;lung;thyroid;visual apparatus;testis;head and neck;cervix;germinal center;brain;mammary gland; prostate; 0.07447 0.23492 -1.03794674 7.832035858 126.08397 2.44361 TGIF1 0.0907591522452098 0.869598133603228 0.0396427141515623 TGFB induced factor homeobox 1 FUNCTION: Binds to a retinoid X receptor (RXR) responsive element from the cellular retinol-binding protein II promoter (CRBPII- RXRE). Inhibits the 9-cis-retinoic acid-dependent RXR alpha transcription activation of the retinoic acid responsive element. Active transcriptional corepressor of SMAD2. Links the nodal signaling pathway to the bifurcation of the forebrain and the establishment of ventral midline structures. May participate in the transmission of nuclear signals during development and in the adult, as illustrated by the down-modulation of the RXR alpha activities.; DISEASE: Holoprosencephaly 4 (HPE4) [MIM:142946]: A structural anomaly of the brain, in which the developing forebrain fails to correctly separate into right and left hemispheres. Holoprosencephaly is genetically heterogeneous and associated with several distinct facies and phenotypic variability. {ECO:0000269|PubMed:10835638, ECO:0000269|PubMed:15221788}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;hippocampus;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.10725 0.10070 0.044168103 57.40740741 3034.27732 10.46306 TGIF1P1 . . . TGFB induced factor homeobox 1 pseudogene 1 . . . . . . . . . . . TGIF2 0.307264900831979 0.619228352438134 0.0735067467298873 TGFB induced factor homeobox 2 FUNCTION: Transcriptional repressor, which probably repress transcription by binding directly the 5'-CTGTCAA-3' DNA sequence or by interacting with TGF-beta activated SMAD proteins. Probably represses transcription via the recruitment of histone deacetylase proteins. {ECO:0000269|PubMed:11427533}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart, kidney and testis. Weakly expressed in brain and prostate.; . . 0.70898 0.10647 -0.207437529 38.2814343 2.55893 0.09473 TGIF2-C20orf24 0.932314274654765 0.06735367809868 0.000332047246555153 TGIF2-C20orf24 readthrough . . . . . . . . . 4.35456 0.15806 TGIF2LX 0.592887022382807 0.367457707392254 0.0396552702249384 TGFB induced factor homeobox 2 like, X-linked FUNCTION: May have a transcription role in testis.; . TISSUE SPECIFICITY: Specifically expressed in adult testis.; medulla oblongata;lung;testis; . 0.03435 0.06016 0.170987912 65.5579146 356.46791 3.99675 TGIF2LY 0.0768707616723098 0.539299269354931 0.383829968972759 TGFB induced factor homeobox 2 like, Y-linked FUNCTION: May have a transcription role in testis. May act as a competitor/regulator of TGIF2LX.; . TISSUE SPECIFICITY: Specifically expressed in adult testis.; lung;testis; . . . . . . . TGIF2P1 . . . TGFB induced factor homeobox 2 pseudogene 1 . . . . . . . . . . . TGM1 5.30650116807075e-07 0.991605613629215 0.00839385572066874 transglutaminase 1 FUNCTION: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Responsible for cross- linking epidermal proteins during formation of the stratum corneum.; DISEASE: Ichthyosis, congenital, autosomal recessive 1 (ARCI1) [MIM:242300]: A form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non-bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs. {ECO:0000269|PubMed:11251583, ECO:0000269|PubMed:11511296, ECO:0000269|PubMed:19890349, ECO:0000269|PubMed:7773290, ECO:0000269|PubMed:7824952, ECO:0000269|PubMed:9326318}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);colon;skin;skeletal muscle;uterus;lung;oesophagus;larynx;thyroid;placenta;hypopharynx;testis;head and neck;cervix;bladder;mammary gland; superior cervical ganglion;tongue;ciliary ganglion;atrioventricular node;skeletal muscle; 0.29356 0.47581 -0.055147466 48.92663364 277.28371 3.56624 TGM2 4.86367266752489e-14 0.0253955333365796 0.974604466663372 transglutaminase 2 FUNCTION: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.; . . myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;oesophagus;bone;testis;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;placenta;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.27494 0.70651 -0.835882558 11.47676339 240.66228 3.35252 TGM3 9.8674987422054e-06 0.984994273626965 0.0149958588742927 transglutaminase 3 FUNCTION: Catalyzes the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins, as well as the conjugation of polyamines to proteins. Involved in the formation of the cornified envelope (CE), a specialized component consisting of covalent cross-links of proteins beneath the plasma membrane of terminally differentiated keratinocytes. Catalyzes small proline-rich proteins (SPRR1 and SPRR2) and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold (By similarity). In hair follicles, involved in cross- linking structural proteins to hardening the inner root sheath. {ECO:0000250}.; . . . . 0.35958 0.21918 -0.211293113 37.76244397 1529.88306 7.26777 TGM4 1.13522291514052e-11 0.288243516510952 0.711756483477696 transglutaminase 4 FUNCTION: Associated with the mammalian reproductive process. Catalyzes the cross-linking of proteins and the conjugation of polyamines to specific proteins in the seminal tract.; . TISSUE SPECIFICITY: Prostate.; unclassifiable (Anatomical System);prostate;colon;skeletal muscle; prostate;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.06090 0.47188 0.898331608 89.31351734 3544.74732 11.48935 TGM5 5.36528605073887e-16 0.00666969224021982 0.993330307759779 transglutaminase 5 FUNCTION: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Contributes to the formation of the cornified cell envelope of keratinocytes.; DISEASE: Peeling skin syndrome 2 (PSS2) [MIM:609796]: A non- inflammatory and localized form of peeling skin syndrome, a genodermatosis characterized by the continuous shedding of the outer layers of the epidermis. In PSS2 patients, skin peeling is painless and strictly limited to the dorsa of the hands and feet. It is accompanied by painless erythema and spontaneous non- scarring healing. Ultrastructural and histological analysis shows a level of blistering high in the epidermis at the stratum granulosum-stratum corneum junction. {ECO:0000269|PubMed:16380904}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in foreskin keratinocytes.; lung;tongue;head and neck; superior cervical ganglion;tongue;caudate nucleus; 0.19456 0.13537 0.826715241 88.09271054 2224.62407 8.69227 TGM6 2.75865000258514e-18 0.00213957135740279 0.997860428642597 transglutaminase 6 FUNCTION: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. {ECO:0000250}.; DISEASE: Spinocerebellar ataxia 35 (SCA35) [MIM:613908]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA35 patients commonly show upper limb involvement and torticollis. There is no cognitive impairment. {ECO:0000269|PubMed:21106500, ECO:0000269|PubMed:22554020, ECO:0000269|PubMed:23206699, ECO:0000269|PubMed:25253745}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lung; subthalamic nucleus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.11224 . 1.63326524 96.08398207 764.51785 5.47971 TGM7 6.34381866870598e-10 0.63338908239212 0.366610916973498 transglutaminase 7 FUNCTION: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.; . TISSUE SPECIFICITY: Widely expressed.; . . 0.07725 0.10507 0.115764778 62.17268224 698.45521 5.26178 TGOLN2 0.000179690886067026 0.462547905195248 0.537272403918685 trans-golgi network protein 2 FUNCTION: May be involved in regulating membrane traffic to and from trans-Golgi network.; . TISSUE SPECIFICITY: Isoform TGN46 is widely expressed. Isoform TGN51 is more abundant in fetal lung and kidney. Isoform TGN48 is barely expressed in embryonic kidney and promyelocytic cells.; lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; dorsal root ganglion;amygdala;superior cervical ganglion;cerebellum peduncles;thyroid;placenta;ciliary ganglion;pons;kidney;atrioventricular node;trigeminal ganglion;parietal lobe; 0.05986 0.18295 1.418384579 94.89266336 2324.30935 8.92690 TGS1 1.02458361412861e-07 0.92486984595154 0.0751300515900983 trimethylguanosine synthase 1 FUNCTION: Catalyzes the 2 serial methylation steps for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Hypermethylation of the m7G cap of U snRNAs leads to their concentration in nuclear foci, their colocalization with coilin and the formation of canonical Cajal bodies (CBs). Plays a role in transcriptional regulation. {ECO:0000269|PubMed:11517327, ECO:0000269|PubMed:11912212, ECO:0000269|PubMed:16687569, ECO:0000269|PubMed:18775984}.; . TISSUE SPECIFICITY: Ubiquitously expressed. High expression in heart, skeletal muscle, kidney, liver and placenta. {ECO:0000269|PubMed:11517327}.; ovary;colon;parathyroid;skin;uterus;prostate;whole body;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;blood;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;appendix;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skin; 0.28728 0.15414 2.609149394 98.77329559 1687.19895 7.57298 TH 0.00409874369425709 0.988151936494581 0.00774931981116177 tyrosine hydroxylase FUNCTION: Plays an important role in the physiology of adrenergic neurons.; DISEASE: Note=May play a role in the pathogenesis of Parkinson disease (PD). A genome-wide copy number variation analysis has identified a 34 kilobase deletion over the TH gene in a PD patient but not in any controls. {ECO:0000269|PubMed:20809526}.; TISSUE SPECIFICITY: Mainly expressed in the brain and adrenal glands.; unclassifiable (Anatomical System);ovary;heart;tongue;islets of Langerhans;salivary gland;sympathetic chain;intestine;colon;pharynx;blood;skin;uterus;lung;cornea;adrenal gland;visual apparatus;liver;head and neck;kidney;brain;mammary gland; adrenal gland;hypothalamus;adrenal cortex;atrioventricular node;skeletal muscle; 0.74919 0.85508 -0.951568548 9.271054494 2945.63638 10.29111 TH2LCRR . . . T helper type 2 locus control region associated RNA . . . . . . . . . . . THA1P . . . threonine aldolase 1, pseudogene . . . . . . . . . . . THADA 1.24008146143984e-28 0.00314850227018796 0.996851497729812 thyroid adenoma associated . . TISSUE SPECIFICITY: Expressed in pancreas, adrenal medulla, thyroid, adrenal cortex, testis, thymus, small intestine and stomach. {ECO:0000269|PubMed:12955091}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;uterus;prostate;superior cervical ganglion;testis - seminiferous tubule;thyroid;liver;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09919 0.09816 0.448132652 77.98419439 4895.75241 14.23268 THAP1 0.89916932761685 0.0999166173415187 0.000914055041630948 THAP domain containing, apoptosis associated protein 1 FUNCTION: DNA-binding transcription regulator that regulates endothelial cell proliferation and G1/S cell-cycle progression. Specifically binds the 5'-[AT]NTNN[GT]GGCA[AGT]-3' core DNA sequence and acts by modulating expression of pRB-E2F cell-cycle target genes, including RRM1. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. May also have pro-apoptopic activity by potentiating both serum-withdrawal and TNF-induced apoptosis. {ECO:0000269|PubMed:12717420, ECO:0000269|PubMed:17003378, ECO:0000269|PubMed:20200153}.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, kidney and liver. Weaker expression in brain and placenta. {ECO:0000269|PubMed:20200153}.; colon;skin;uterus;prostate;whole body;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;blood;skeletal muscle;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;kidney;stomach; skeletal muscle; 0.20989 0.12971 -0.09720619 46.20193442 4.80896 0.17513 THAP2 5.16530633847092e-05 0.436025336944235 0.56392300999238 THAP domain containing, apoptosis associated protein 2 . . . unclassifiable (Anatomical System);lymph node;ovary;hypothalamus;parathyroid;fovea centralis;skin;uterus;whole body;lung;placenta;macula lutea;alveolus;liver;testis;germinal center;kidney;brain;bladder;thymus; globus pallidus;ciliary ganglion; 0.04808 0.10018 0.25917371 70.05779665 533.56495 4.71254 THAP3 0.00148422474585026 0.675884849425615 0.322630925828535 THAP domain containing, apoptosis associated protein 3 FUNCTION: Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. {ECO:0000269|PubMed:20200153}.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and placenta. Weaker expression in brain, kidney and liver. {ECO:0000269|PubMed:20200153}.; lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;endometrium;cerebral cortex;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;breast;pancreas;lung;placenta;macula lutea;hippocampus;kidney;mammary gland;peripheral nerve; superior cervical ganglion;subthalamic nucleus;atrioventricular node; 0.09508 0.09834 1.016049644 90.86459071 127.55619 2.46236 THAP4 0.116840641035292 0.877454387617616 0.00570497134709301 THAP domain containing 4 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.44826 0.10582 -0.178111357 40.44585987 42.50743 1.23417 THAP5 0.00279203530856965 0.570798256525436 0.426409708165994 THAP domain containing 5 FUNCTION: Has sequence-specific DNA-binding activity and can function as transcriptional repressor (in vitro) (PubMed:21110952). May be a regulator of cell cycle: THAP5 overexpression in human cell lines causes cell cycle arrest at G2/M phase (PubMed:19502560). {ECO:0000269|PubMed:21110952, ECO:0000305|PubMed:19502560}.; . TISSUE SPECIFICITY: Detected in heart (PubMed:19502560, PubMed:21195082). Detected in brain and muscle (at protein level) (PubMed:19502560). Highly expressed in the heart. Also found in brain and skeletal muscle (PubMed:19502560, PubMed:21195082). {ECO:0000269|PubMed:19502560, ECO:0000269|PubMed:21195082}.; unclassifiable (Anatomical System);cartilage;colon;parathyroid;skeletal muscle;prostate;whole body;lung;frontal lobe;cerebral cortex;trabecular meshwork;bone;placenta;thyroid;hippocampus;liver;testis;kidney;brain;aorta;stomach; . 0.09661 0.09981 -0.227663163 37.11370606 143.37372 2.61089 THAP5P1 . . . THAP domain containing 5 pseudogene 1 . . . . . . . . . . . THAP5P2 . . . THAP domain containing 5 pseudogene 2 . . . . . . . . . . . THAP6 0.00144042332675322 0.6694758251541 0.329083751519146 THAP domain containing 6 . . . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;skin;uterus;prostate;lung;frontal lobe;endometrium;adrenal gland;larynx;nasopharynx;bone;placenta;liver;testis;cervix;head and neck;spleen;kidney;brain;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22795 . 0.61555716 83.13871196 248.61992 3.39793 THAP7 0.0293278546639812 0.923633046085113 0.0470390992509055 THAP domain containing 7 FUNCTION: Chromatin-associated, histone tail-binding protein that represses transcription via recruitment of HDAC3 and nuclear hormone receptor corepressors. {ECO:0000269|PubMed:15561719}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;tongue;islets of Langerhans;muscle;adrenal cortex;lens;skeletal muscle;bile duct;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.37131 0.10994 . . 76.37465 1.83233 THAP7-AS1 . . . THAP7 antisense RNA 1 . . . . . . . . . . . THAP8 0.00063975214571545 0.49458157739797 0.504778670456315 THAP domain containing 8 . . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;bone;testis;brain;unclassifiable (Anatomical System);trophoblast;heart;muscle;adrenal cortex;lens;breast;lung;placenta;macula lutea;hippocampus;visual apparatus;liver;spleen;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.09473 0.08327 0.571462851 81.99457419 2293.88071 8.87004 THAP9 7.47715130371729e-10 0.669088265822263 0.330911733430022 THAP domain containing 9 FUNCTION: Active transposase that specifically recognizes the bipartite 5'-TXXGGGX(A/T)-3' consensus motif and mediates transposition. {ECO:0000269|PubMed:20010837, ECO:0000269|PubMed:23349291}.; . . unclassifiable (Anatomical System);medulla oblongata;smooth muscle;heart;hypothalamus;colon;skin;uterus;breast;prostate;whole body;lung;cochlea;liver;testis;germinal center;kidney; superior cervical ganglion;appendix;trigeminal ganglion;fetal thyroid; 0.12967 0.09337 0.624649618 83.53385232 1979.28923 8.19739 THAP9-AS1 . . . THAP9 antisense RNA 1 . . . . . . . . . . . THAP10 0.00119434425578864 0.628936904856366 0.369868750887845 THAP domain containing 10 . . . unclassifiable (Anatomical System);ovary;tongue;hypothalamus;colon;fovea centralis;choroid;lens;retina;uterus;pancreas;optic nerve;lung;frontal lobe;macula lutea;visual apparatus;testis;head and neck;spleen;cervix;kidney;brain;stomach; whole brain;superior cervical ganglion;medulla oblongata;prefrontal cortex;globus pallidus;atrioventricular node;trigeminal ganglion; 0.08047 0.06746 -0.427900189 25.14744043 11.62277 0.42102 THAP11 0.465632985581296 0.509234620943802 0.0251323934749027 THAP domain containing 11 FUNCTION: Transcriptional repressor that plays a central role for embryogenesis and the pluripotency of embryonic stem (ES) cells. Sequence-specific DNA-binding factor that represses gene expression in pluripotent ES cells by directly binding to key genetic loci and recruiting epigenetic modifiers (By similarity). {ECO:0000250}.; . . lymphoreticular;myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; whole brain;globus pallidus;skeletal muscle;cerebellum; 0.49246 0.11033 -0.295622497 32.61972163 8.06055 0.29586 THAP12 . . . THAP domain containing 12 FUNCTION: Upstream regulator of interferon-induced serine/threonine protein kinase R (PKR). May block the PKR- inhibitory function of P58IPK, resulting in restoration of kinase activity and suppression of cell growth.; . . . . 0.61718 0.20128 -0.556537043 19.72753008 . . THAP12P1 . . . THAP domain containing 12 pseudogene 1 . . . . . . . . . . . THAP12P2 . . . THAP domain containing 12 pseudogene 2 . . . . . . . . . . . THAP12P3 . . . THAP domain containing 12 pseudogene 3 . . . . . . . . . . . THAP12P4 . . . THAP domain containing 12 pseudogene 4 . . . . . . . . . . . THAP12P5 . . . THAP domain containing 12 pseudogene 5 . . . . . . . . . . . THAP12P6 . . . THAP domain containing 12 pseudogene 6 . . . . . . . . . . . THAP12P7 . . . THAP domain containing 12 pseudogene 7 . . . . . . . . . . . THAP12P8 . . . THAP domain containing 12 pseudogene 8 . . . . . . . . . . . THAP12P9 . . . THAP domain containing 12 pseudogene 9 . . . . . . . . . . . THAP12P10 . . . THAP domain containing 12 pseudogene 10 . . . . . . . . . . . THAS . . . thoracoabdominal syndrome . . . . . . . . . . . THBD . . . thrombomodulin FUNCTION: Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va and factor VIIIa, and thereby reduces the amount of thrombin generated.; DISEASE: Thrombophilia due to thrombomodulin defect (THPH12) [MIM:614486]: A hemostatic disorder characterized by a tendency to thrombosis. {ECO:0000269|PubMed:12139752, ECO:0000269|PubMed:7811989, ECO:0000269|PubMed:9198186}. Note=The disease may be caused by mutations affecting the gene represented in this entry. The role of thrombomodulin in thrombosis is controversial. It is likely that genetic or environmental risk factors in addition to THBD variation are involved in the pathogenesis of venous thrombosis.; DISEASE: Hemolytic uremic syndrome atypical 6 (AHUS6) [MIM:612926]: An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. {ECO:0000269|PubMed:19625716, ECO:0000269|PubMed:20513133}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype.; TISSUE SPECIFICITY: Endothelial cells are unique in synthesizing thrombomodulin.; . . 0.22575 0.37247 . . 644.9071 5.10144 THBS1 0.999073127290828 0.000926872694430812 1.47411503895777e-11 thrombospondin 1 FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Binds heparin. May play a role in dentinogenesis and/or maintenance of dentin and dental pulp (By similarity). Ligand for CD36 mediating antiangiogenic properties. Plays a role in ER stress response, via its interaction with the activating transcription factor 6 alpha (ATF6) which produces adaptive ER stress response factors (By similarity). {ECO:0000250, ECO:0000269|PubMed:11134179, ECO:0000269|PubMed:15014436}.; . . smooth muscle;ovary;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;amniotic fluid;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;skeletal muscle;bile duct;breast;lung;epididymis;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;smooth muscle;adipose tissue;heart;atrioventricular node;skeletal muscle;uterus;uterus corpus;lung;trachea;placenta;appendix;fetal lung;ciliary ganglion;trigeminal ganglion; 0.93538 0.93547 -1.74358502 2.394432649 2770.99268 9.93564 THBS2 0.245000802643493 0.754998733932457 4.63424050419561e-07 thrombospondin 2 FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Ligand for CD36 mediating antiangiogenic properties. {ECO:0000269|PubMed:20714802}.; . TISSUE SPECIFICITY: High expression in invertebral disk tissue. {ECO:0000269|PubMed:18455130}.; . . 0.74508 0.52113 -0.470420436 23.04788865 378.07788 4.09997 THBS3 1.20600565280442e-08 0.999865398689045 0.000134589250898824 thrombospondin 3 FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Can bind to fibrinogen, fibronectin, laminin and type V collagen.; . . . . 0.19703 0.23320 -1.482570877 3.662420382 1281.61434 6.74219 THBS4 1.74208249337707e-08 0.998069807945749 0.00193017463342578 thrombospondin 4 FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions and is involved in various processes including cellular proliferation, migration, adhesion and attachment, inflammatory response to CNS injury, regulation of vascular inflammation and adaptive responses of the heart to pressure overload and in myocardial function and remodeling. Binds to structural extracellular matrix (ECM) proteins and modulates the ECM in response to tissue damage, contributing to cardioprotective and adaptive ECM remodeling. Plays a role in ER stress response, via its interaction with the activating transcription factor 6 alpha (ATF6) which produces adaptive ER stress response factors and protects myocardium from pressure overload. May contribute to spinal presynaptic hypersensitivity and neuropathic pain states after peripheral nerve injury. May play a role in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury in a NOTCH1-dependent manner (By similarity). {ECO:0000250, ECO:0000269|PubMed:19441079}.; . . unclassifiable (Anatomical System);cartilage;ovary;heart;tongue;islets of Langerhans;colon;lens;skin;skeletal muscle;retina;pancreas;prostate;whole body;lung;frontal lobe;endometrium;synovium;larynx;bone;thyroid;visual apparatus;pituitary gland;testis;head and neck;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;tongue;spinal cord;testis;ciliary ganglion;trigeminal ganglion;pituitary;skeletal muscle; 0.18964 0.34036 -0.23697515 36.32342534 1138.51791 6.43453 THEG 4.92698073399521e-07 0.39783004944338 0.602169457858546 theg spermatid protein FUNCTION: May be involved (but not essential) in spermatogenesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:11173852}.; medulla oblongata;lung;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.07826 0.09524 -0.12856188 44.04930408 1476.8483 7.15790 THEGL . . . theg spermatid protein-like . . . . . . . . . 1248.98079 6.67249 THEM4 0.000241347691647955 0.523722509501348 0.476036142807004 thioesterase superfamily member 4 FUNCTION: Has acyl-CoA thioesterase activity towards medium and long-chain (C14 to C18) fatty acyl-CoA substrates, and probably plays an role in mitochondrial fatty acid metabolism. Plays a role in the apoptotic process, possibly via its regulation of AKT1 activity. According to PubMed:11598301, inhibits AKT1 phosphorylation and activity. According to PubMed:17615157, enhances AKT1 activity by favoring its phosphorylation and translocation to plasma membrane. {ECO:0000269|PubMed:11598301, ECO:0000269|PubMed:17615157, ECO:0000269|PubMed:19168129, ECO:0000269|PubMed:19421406, ECO:0000269|PubMed:19453107, ECO:0000269|PubMed:22871024}.; . TISSUE SPECIFICITY: Expressed predominantly in skeletal muscle, testis, uterus, brain and kidney. Down-regulated in glioblastoma or glioma compared to non-neoplastic brain due to promoter hypermethylation. {ECO:0000269|PubMed:11598301, ECO:0000269|PubMed:15026474}.; . . 0.03837 0.06135 0.926041233 89.65557915 31.29238 0.98673 THEM4P1 . . . thioesterase superfamily member 4 pseudogene 1 . . . . . . . . . . . THEM5 5.98125901231817e-07 0.139096336703154 0.860903065170944 thioesterase superfamily member 5 FUNCTION: Has acyl-CoA thioesterase activity towards long-chain (C16 and C18) fatty acyl-CoA substrates, with a preference for linoleyl-CoA and other unsaturated long-chain fatty acid-CoA esters. Plays an important role in mitochondrial fatty acid metabolism, and in remodeling of the mitochondrial lipid cardiolipin. Required for normal mitochondrial function. {ECO:0000269|PubMed:22586271}.; . . . . 0.06362 . 1.014235724 90.84100024 150.75669 2.68195 THEM6 0.0242798295662762 0.549814777682646 0.425905392751078 thioesterase superfamily member 6 . . . . . 0.11829 . . . 28.06099 0.90009 THEM7P . . . thioesterase superfamily member 7, pseudogene . . . . . . . . . . . THEMIS 0.142516979842166 0.853473734965651 0.00400928519218382 thymocyte selection associated FUNCTION: Plays a central role in late thymocyte development by controlling both positive and negative T-cell selection. Required to sustain and/or integrate signals required for proper lineage commitment and maturation of T-cells. Regulates T-cell development through T-cell antigen receptor (TCR) signaling and in particular through the regulation of calcium influx and phosphorylation of Erk. {ECO:0000250|UniProtKB:Q8BGW0}.; . . . . 0.15992 . -0.352661697 29.48808681 120.82389 2.39593 THEMIS2 0.0647217124407372 0.92031399253285 0.0149642950264125 thymocyte selection associated family member 2 FUNCTION: May constitute a control point in macrophage inflammatory response, promoting LPS-induced TNF production. {ECO:0000269|PubMed:20644716}.; . TISSUE SPECIFICITY: Expressed in different endometrial adenocarcinoma cell lines and various other cell lines apart from the prostate cell line LNCaP and the ovarian cancer cell line BG1. {ECO:0000269|PubMed:9563507}.; . . 0.54257 0.09064 -0.532670911 20.78320359 2295.23658 8.87346 THEMIS3P . . . thymocyte selection associated family member 3, pseudogene . . . . . . . . . . . THG1L 3.48304059537209e-05 0.586421264341755 0.413543905252292 tRNA-histidine guanylyltransferase 1 like FUNCTION: Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. This step is essential for proper recognition of the tRNA and for the fidelity of protein synthesis. {ECO:0000269|PubMed:21059936}.; . TISSUE SPECIFICITY: Expressed in many tissues. {ECO:0000269|PubMed:15459185}.; ovary;colon;parathyroid;fovea centralis;choroid;retina;prostate;optic nerve;endometrium;bone;pituitary gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;blood;lens;pancreas;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.03109 0.10705 -0.249709319 35.74545883 23.16784 0.77355 THM . . . thymoma . . . . . . . . . . . THNSL1 5.61830090821939e-12 0.0302147425500026 0.969785257444379 threonine synthase like 1 . . . . . 0.06711 0.09765 0.466683681 78.73908941 987.42585 6.05941 THNSL2 3.94167649325955e-06 0.59664579153949 0.403350266784017 threonine synthase like 2 FUNCTION: Isoform 1: Acts as a catabolic phospho-lyase on both gamma- and beta-phosphorylated substrates. Degrades O-phospho- threonine (PThr) to alpha-ketobutyrate, ammonia and phosphate (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;iris;testis;brain;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;urinary;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; . 0.14364 0.14327 0.42259095 77.22929936 512.18284 4.63245 THOC1 0.871670074938969 0.128326977705907 2.94735512420203e-06 THO complex 1 FUNCTION: Required for efficient export of polyadenylated RNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Regulates transcriptional elongation of a subset of genes. Involved in genome stability by preventing co-transcriptional R-loop formation.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in various cancer cell lines. Expressed at very low levels in normal breast epithelial cells and highly expressed in breast tumors. Expression is strongly associated with an aggressive phenotype of breast tumors and expression correlates with tumor size and the metastatic state of the tumor progression. {ECO:0000269|PubMed:15358532, ECO:0000269|PubMed:15833825}.; ovary;salivary gland;intestine;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;lens;skeletal muscle;breast;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;stomach; testis - interstitial;testis - seminiferous tubule;testis;cingulate cortex; 0.92057 0.10600 -0.448125345 24.19202642 18.05942 0.63001 THOC2 0.999999919330809 8.06691910784516e-08 1.13073745587879e-18 THO complex 2 FUNCTION: Required for efficient export of polyadenylated RNA and spliced mRNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. THOC2 (and probably the THO complex) is involved in releasing mRNA from nuclear speckle domains. Required for NXF1 localization to the nuclear rim. {ECO:0000269|PubMed:11979277, ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:18974867, ECO:0000269|PubMed:22893130, ECO:0000269|PubMed:23222130}.; . . lymphoreticular;ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;larynx;bone;thyroid;dura mater;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;skeletal muscle;breast;pia mater;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;white blood cells;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.49521 0.11809 -0.580403979 18.58928993 38.02954 1.12981 THOC3 . . . THO complex 3 FUNCTION: Required for efficient export of polyadenylated RNA and spliced mRNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269|PubMed:11979277, ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:18974867}.; . . medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; . 0.14591 0.12214 . . 439.11136 4.36776 THOC5 0.000462815234823358 0.999231338687993 0.000305846077184045 THO complex 5 FUNCTION: Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. THOC5 in conjunction with ALYREF/THOC4 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim. Involved in transcription elongation and genome stability. Involved in alternative polyadenylation site choice by recruiting CPSF6 to 5' region of target genes; probably mediates association of the TREX and CFIm complexes.; . TISSUE SPECIFICITY: Ubiquitously expressed.; myocardium;umbilical cord;ovary;salivary gland;intestine;colon;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;amnion;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.08076 0.09855 0.220536484 68.38287332 2462.99316 9.23782 THOC6 0.00219344761881848 0.993903933662032 0.00390261871914958 THO complex 6 FUNCTION: Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Plays a role in apoptosis negative control involved in brain development. {ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:18974867, ECO:0000269|PubMed:23621916}.; DISEASE: Beaulieu-Boycott-Innes syndrome (BBIS) [MIM:613680]: An autosomal recessive neurodevelopmental disorder characterized by delayed development, moderate intellectual disability, and dysmorphic facial features. Other developmental anomalies, such as cardiac and renal defects, may also occur. {ECO:0000269|PubMed:23621916}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;head and neck;cervix;kidney;stomach;peripheral nerve; white blood cells;trigeminal ganglion; 0.25009 0.11017 -1.111360919 6.717386176 44.31859 1.27091 THOC7 0.978320488745139 0.0216599668450928 1.95444097679428e-05 THO complex 7 FUNCTION: Required for efficient export of polyadenylated RNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. {ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:23222130}.; . . myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;frontal lobe;bone;thyroid;pituitary gland;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;skeletal muscle;breast;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;amnion;alveolus;liver;head and neck;kidney;mammary gland;aorta;stomach;thymus; amygdala;superior cervical ganglion;globus pallidus;trigeminal ganglion; 0.55754 0.10705 -0.163345027 41.24793583 13.98772 0.50775 THOC7-AS1 . . . THOC7 antisense RNA 1 . . . . . . . . . . . THOP1 0.0234920934710946 0.973497541476196 0.00301036505270917 thimet oligopeptidase 1 FUNCTION: Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. Able to degrade the beta-amyloid precursor protein and generate amyloidogenic fragments.; . . medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;liver;ciliary ganglion; 0.08562 0.17442 -1.478950235 3.703703704 205.78205 3.10050 THPO 0.00514022944754883 0.889131369192804 0.105728401359647 thrombopoietin FUNCTION: Lineage-specific cytokine affecting the proliferation and maturation of megakaryocytes from their committed progenitor cells. It acts at a late stage of megakaryocyte development. It may be the major physiological regulator of circulating platelets.; DISEASE: Thrombocythemia 1 (THCYT1) [MIM:187950]: A myeloproliferative disorder characterized by excessive platelet production, resulting in increased numbers of circulating platelets. It can be associated with spontaneous hemorrhages and thrombotic episodes. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;cartilage;heart;skin; superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skin;parietal lobe; 0.20379 0.43705 -0.293801652 32.93819297 31.37424 0.98896 THRA 0.167006769731387 0.832385362218959 0.000607868049654164 thyroid hormone receptor, alpha FUNCTION: Isoform Alpha-1: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. {ECO:0000269|PubMed:12699376, ECO:0000269|PubMed:14673100, ECO:0000269|PubMed:18237438, ECO:0000269|PubMed:19926848}.; DISEASE: Hypothyroidism, congenital, non-goitrous, 6 (CHNG6) [MIM:614450]: A disease characterized by growth retardation, developmental retardation, skeletal dysplasia, borderline low thyroxine levels and high triiodothyronine levels. There is differential sensitivity to thyroid hormone action, with retention of hormone responsiveness in the hypothalamic pituitary axis and liver but skeletal, gastrointestinal, and myocardial resistance. {ECO:0000269|PubMed:22168587, ECO:0000269|PubMed:24969835, ECO:0000269|PubMed:25670821, ECO:0000269|PubMed:26037512}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;frontal lobe;endometrium;bone;thyroid;iris;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;hypothalamus;spinal cord;muscle;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; whole brain;amygdala;dorsal root ganglion;thalamus;superior cervical ganglion;occipital lobe;cerebellum peduncles;spinal cord;temporal lobe;caudate nucleus;atrioventricular node;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.45657 0.59356 -0.560178693 19.30879925 9.65202 0.35425 THRAP3 0.999996899183557 3.10081644137846e-06 1.65836261637114e-15 thyroid hormone receptor associated protein 3 FUNCTION: Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-ARNTL/BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798). {ECO:0000269|PubMed:20123736, ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:22424773, ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:24043798}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10198638}.; . . 0.24539 0.25503 -0.619039275 17.39797122 163.30521 2.78993 THRAP3P1 . . . thyroid hormone receptor associated protein 3 pseudogene 1 . . . . . . . . . . . THRB 0.994541861187431 0.00545747427454477 6.64538024134541e-07 thyroid hormone receptor beta FUNCTION: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. {ECO:0000269|PubMed:12699376, ECO:0000269|PubMed:14673100, ECO:0000269|PubMed:16781732, ECO:0000269|PubMed:17418816, ECO:0000269|PubMed:18237438, ECO:0000269|PubMed:18798561, ECO:0000269|PubMed:19926848}.; DISEASE: Generalized thyroid hormone resistance (GTHR) [MIM:188570]: A disease characterized by goiter, abnormal mental functions, increased susceptibility to infections, abnormal growth and bone maturation, tachycardia and deafness. Affected individuals may also have attention deficit-hyperactivity disorders (ADHD) and language difficulties. GTHR patients also have high levels of circulating thyroid hormones (T3-T4), with normal or slightly elevated thyroid stimulating hormone (TSH). {ECO:0000269|PubMed:10660344, ECO:0000269|PubMed:1314846, ECO:0000269|PubMed:1324420, ECO:0000269|PubMed:1563081, ECO:0000269|PubMed:1587388, ECO:0000269|PubMed:1619012, ECO:0000269|PubMed:1661299, ECO:0000269|PubMed:16804041, ECO:0000269|PubMed:1846005, ECO:0000269|PubMed:19268523, ECO:0000269|PubMed:2153155, ECO:0000269|PubMed:2510172, ECO:0000269|PubMed:7833659, ECO:0000269|PubMed:8175986, ECO:0000269|PubMed:8514853, ECO:0000269|PubMed:8664910, ECO:0000269|PubMed:8889584}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Generalized thyroid hormone resistance autosomal recessive (GTHRAR) [MIM:274300]: An autosomal recessive disorder characterized by goiter, clinical euthyroidism, end-organ unresponsiveness to thyroid hormone, abnormal growth and bone maturation, and deafness. Patients also have high levels of circulating thyroid hormones, with elevated thyroid stimulating hormone. {ECO:0000269|PubMed:1653889}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Selective pituitary thyroid hormone resistance (PRTH) [MIM:145650]: Variant form of thyroid hormone resistance and is characterized by clinical hyperthyroidism, with elevated free thyroid hormones, but inappropriately normal serum TSH. Unlike GRTH, where the syndrome usually segregates with a dominant allele, the mode of inheritance in PRTH has not been established. {ECO:0000269|PubMed:7528740, ECO:0000269|PubMed:8381821}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);prostate;kidney;brain;skeletal muscle;stomach;retina; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.87928 0.51098 -0.471992905 23.03609342 18.48609 0.63978 THRB-AS1 . . . THRB antisense RNA 1 . . . . . . . . . . . THRB-IT1 . . . THRB intronic transcript 1 . . . . . . . . . . . THRIL . . . TNF and HNRNPL related immunoregulatory long non-coding RNA . . . . . . . . . . . THRSP 0.00560130986826702 0.481638000851753 0.51276068927998 thyroid hormone responsive FUNCTION: Plays a role in the regulation of lipogenesis, especially in lactating mammary gland. Important for the biosynthesis of triglycerides with medium-length fatty acid chains. May modulate lipogenesis by interacting with MID1IP1 and preventing its interaction with ACACA (By similarity). May function as transcriptional coactivator. May modulate the transcription factor activity of THRB. {ECO:0000250, ECO:0000269|PubMed:17418816, ECO:0000269|PubMed:18299245}.; . TISSUE SPECIFICITY: Mainly expressed in tissues that synthesize triglycerides.; unclassifiable (Anatomical System);smooth muscle;islets of Langerhans;colon;skeletal muscle;skin;bone marrow;lung;cerebral cortex;endometrium;thyroid;bone;liver;kidney; superior cervical ganglion;adipose tissue;liver;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12511 0.11897 0.148941568 64.31941496 93.49247 2.08073 THSD1 2.45031608890038e-05 0.916686831500069 0.083288665339042 thrombospondin type 1 domain containing 1 . . . colon;choroid;fovea centralis;skin;retina;uterus;whole body;optic nerve;cochlea;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;muscle;lens;skeletal muscle;lung;placenta;visual apparatus;macula lutea;hypopharynx;alveolus;spleen;head and neck;mammary gland; . 0.12102 0.11156 0.091899012 60.68058504 791.50816 5.54928 THSD1P1 . . . thrombospondin type 1 domain containing 1 pseudogene 1 . . . . . . . . . . . THSD4 0.00181827156769691 0.998138962010762 4.27664215415986e-05 thrombospondin type 1 domain containing 4 FUNCTION: Promotes FBN1 matrix assembly. Attenuates TGFB signaling, possibly by accelerating the sequestration of large latent complexes of TGFB or active TGFB by FBN1 microfibril assembly, thereby negatively regulating the expression of TGFB regulatory targets, such as POSTN (By similarity). {ECO:0000250}.; . . smooth muscle;developmental;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;head and neck;cervix;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.22789 0.13745 -0.942503278 9.412597311 745.2967 5.41820 THSD4-AS1 . . . THSD4 antisense RNA 1 . . . . . . . . . . . THSD4-AS2 . . . THSD4 antisense RNA 2 . . . . . . . . . . . THSD7A 0.999280748692625 0.000719251307374888 1.10346913215198e-16 thrombospondin type 1 domain containing 7A FUNCTION: The soluble form promotes endothelial cell migration and filopodia formationduring angiogenesis via a FAK-dependent mechanism. {ECO:0000269|PubMed:22194972}.; . . unclassifiable (Anatomical System);ovary;cartilage;parathyroid;skeletal muscle;retina;uterus;prostate;whole body;lung;frontal lobe;placenta;liver;spleen;kidney;brain;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;medulla oblongata;placenta;appendix;ciliary ganglion;trigeminal ganglion; 0.27361 0.08944 -1.308377521 4.865534324 3259.76198 10.88292 THSD7B 5.65285413355626e-06 0.999994327459527 1.96863388907999e-08 thrombospondin type 1 domain containing 7B . . . unclassifiable (Anatomical System);lung;muscle;testis;amniotic fluid;skeletal muscle;stomach;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.33549 0.08669 . . 4772.07743 13.99787 THTPA 0.000116051034701592 0.606242268339488 0.393641680625811 thiamine triphosphatase FUNCTION: Hydrolase highly specific for thiamine triphosphate (ThTP). {ECO:0000269|PubMed:11827967, ECO:0000269|PubMed:23707715}.; . TISSUE SPECIFICITY: Widely expressed but at a low level. {ECO:0000269|PubMed:11827967}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;thyroid;iris;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;pineal body;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;temporal lobe;testis;atrioventricular node;parietal lobe;cerebellum; 0.07236 0.12142 -0.249709319 35.74545883 1113.08595 6.37533 THUMPD1 0.00103546307155391 0.822409285847674 0.176555251080772 THUMP domain containing 1 FUNCTION: Functions as a tRNA-binding adapter to mediate NAT10- dependent tRNA acetylation (PubMed:25653167). {ECO:0000269|PubMed:25653167}.; . . . . 0.60110 0.11917 -0.113792788 45.25831564 565.22241 4.82843 THUMPD1P1 . . . THUMP domain containing 1 pseudogene 1 . . . . . . . . . . . THUMPD2 1.94113855777167e-08 0.241386497640889 0.758613482947726 THUMP domain containing 2 . . TISSUE SPECIFICITY: Expressed in a variety of tissues including brain, colon, gingiva, heart, kidney, liver, lung, placenta, small intestine, spleen and thymus. {ECO:0000269|PubMed:12063391}.; ovary;colon;parathyroid;bone marrow;uterus;optic nerve;whole body;endometrium;thyroid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;adrenal cortex;skeletal muscle;lung;placenta;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.10863 0.09800 -0.578583623 18.71903751 235.39647 3.31568 THUMPD3 3.99618097660492e-11 0.0934216969841067 0.906578302975932 THUMP domain containing 3 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule; 0.13906 0.09925 0.266447942 70.5826846 866.34515 5.73321 THUMPD3-AS1 . . . THUMPD3 antisense RNA 1 . . . . . . . . . . . THUMPD3P1 . . . THUMP domain containing 3 pseudogene 1 . . . . . . . . . . . THY1 0.164135342066625 0.773043014594018 0.0628216433393563 Thy-1 cell surface antigen FUNCTION: May play a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain.; . . smooth muscle;ovary;sympathetic chain;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;thyroid;testis;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;kidney;mammary gland;stomach; dorsal root ganglion;amygdala;whole brain;medulla oblongata;superior cervical ganglion;thalamus;occipital lobe;adipose tissue;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.76152 0.11472 0.013025609 54.62962963 10.17377 0.37066 THYN1 1.40363665599038e-09 0.0294646626124125 0.970535335983951 thymocyte nuclear protein 1 FUNCTION: Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC. {ECO:0000250}.; . . medulla oblongata;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;thyroid;bone;testis;amniotic fluid;pineal gland;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;adrenal cortex;blood;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; globus pallidus;testis;cingulate cortex; 0.21173 0.12307 -0.273576253 33.97027601 21.76632 0.73236 TIA1 0.832581092063394 0.167412891911501 6.01602510512394e-06 TIA1 cytotoxic granule-associated RNA binding protein FUNCTION: Involved in alternative pre-RNA splicing and regulation of mRNA translation by binding to AU-rich elements (AREs) located in mRNA 3' untranslated regions (3' UTRs). Possesses nucleolytic activity against cytotoxic lymphocyte target cells. May be involved in apoptosis.; DISEASE: Welander distal myopathy (WDM) [MIM:604454]: An autosomal dominant disorder characterized by adult onset of distal muscle weakness predominantly affecting the distal long extensors of the hands, with slow progression to involve all small hand muscles and the lower legs. Skeletal muscle biopsy shows myopathic changes and prominent rimmed vacuoles. Rare homozygous patients showed earlier onset, faster progression, and proximal muscle involvement. {ECO:0000269|PubMed:23348830, ECO:0000269|PubMed:23401021}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.90768 0.26333 0.238945317 69.20853975 83.28929 1.94032 TIAF1 0.0263935448212883 0.566779832915105 0.406826622263607 TGFB1-induced anti-apoptotic factor 1 FUNCTION: Inhibits the cytotoxic effects of TNF-alpha and overexpressed TNF receptor adapters TRADD, FADD, and RIPK1. Involved in TGF-beta1 inhibition of IkappaB-alpha expression and suppression of TNF-mediated IkappaB-alpha degradation. {ECO:0000269|PubMed:9918798}.; . TISSUE SPECIFICITY: Not detectable in normal kidney and liver. Up- regulated in chronic and acute allograft rejection: expressed in the inflammatory infiltrate and in tubular epithelial cells. {ECO:0000269|PubMed:12829915}.; . . . . 0.791937896 87.33781552 44.08134 1.26555 TIAL1 0.998790731658321 0.00120925152763177 1.68140470552897e-08 TIA1 cytotoxic granule-associated RNA binding protein-like 1 FUNCTION: RNA-binding protein. Possesses nucleolytic activity against cytotoxic lymphocyte target cells. May be involved in apoptosis.; . . . . 0.33802 0.21177 -0.163345027 41.24793583 3.89207 0.14472 TIAM1 0.999932006469338 6.79935306611056e-05 1.03896862173801e-15 T-cell lymphoma invasion and metastasis 1 FUNCTION: Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. Acts as a GDP- dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Activates RAC1, CDC42, and to a lesser extent RHOA. Required for normal cell adhesion and cell migration. {ECO:0000269|PubMed:20361982}.; . TISSUE SPECIFICITY: Found in virtually all analyzed tumor cell lines including B- and T-lymphomas, neuroblastomas, melanomas and carcinomas.; unclassifiable (Anatomical System);heart;cerebellum cortex;islets of Langerhans;skin;uterus;frontal lobe;placenta;thyroid;hypopharynx;head and neck;germinal center;brain;cerebellum; superior cervical ganglion;thalamus;cerebellum peduncles;prefrontal cortex;skeletal muscle;cingulate cortex;cerebellum; 0.48136 0.33272 -0.913225292 9.843123378 5001.55165 14.43752 TIAM2 0.124829516016011 0.87517048105258 2.93140865080266e-09 T-cell lymphoma invasion and metastasis 2 FUNCTION: Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. Acts as a GDP- dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Mediates extracellular laminin signals to activate Rac1, contributing to neurite growth. Involved in lamellipodial formation and advancement of the growth cone of embryonic hippocampal neurons. Promotes migration of neurons in the cerebral cortex. When overexpressed, induces membrane ruffling accompanied by the accumulation of actin filaments along the altered plasma membrane (By similarity). Activates specifically RAC1, but not CDC42 and RHOA. {ECO:0000250, ECO:0000269|PubMed:10512681}.; . TISSUE SPECIFICITY: Expressed in the occipital, frontal and temporal lobes, cerebellum, putamen and testis. {ECO:0000269|PubMed:10512681}.; ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;whole body;optic nerve;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;macula lutea;liver;spleen;head and neck;kidney;mammary gland;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.18572 0.13396 -0.281335604 33.53974994 5362.09394 15.11728 TICAM1 0.852477311306477 0.147418492218442 0.000104196475080269 toll like receptor adaptor molecule 1 FUNCTION: Involved in innate immunity against invading pathogens. Adapter used by TLR3 and TLR4 (through TICAM2) to mediate NF- kappa-B and interferon-regulatory factor (IRF) activation, and to induce apoptosis. Ligand binding to these receptors results in TRIF recruitment through its TIR domain. Distinct protein- interaction motifs allow recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which in turn, lead to the activation of transcription factors IRF3 and IRF7, NF-kappa-B and FADD respectively. {ECO:0000269|PubMed:12471095, ECO:0000269|PubMed:12539043, ECO:0000269|PubMed:14739303}.; DISEASE: Herpes simplex encephalitis 4 (HSE4) [MIM:614850]: A rare complication of human herpesvirus 1 (HHV-1) infection, occurring in only a small minority of HHV-1 infected individuals. HSE is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Onset is over several days and involves fever, headache, seizures, stupor, and often coma, frequently with a fatal outcome. {ECO:0000269|PubMed:22105173}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed but with higher levels in liver. {ECO:0000269|PubMed:12471095, ECO:0000269|PubMed:12539043}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;optic nerve;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;urinary;blood;lens;pancreas;lung;placenta;visual apparatus;macula lutea;cervix;kidney;mammary gland;stomach; . 0.07730 0.14062 -0.152426933 42.25053079 1347.68989 6.88939 TICAM2 0.00470963741298361 0.965631732888936 0.0296586296980803 toll like receptor adaptor molecule 2 FUNCTION: Functions as sorting adapter in LPS-TLR4 signaling to regulate the MYD88-independent pathway during the innate immune response to LPS. Physically bridges TLR4 and TICAM1 and functionally transmits LPS-TRL4 signal to TICAM1; signaling is proposed to occur in early endosomes after endocytosis of TLR4. May also be involved in IL1-triggered NF-kappa-B activation, functioning upstream of IRAK1, IRAK2, TRAF6, and IKBKB; however, reports are controversial. Involved in IL-18 signaling and is proposed to function as a sorting adaptor for MYD88 in IL-18 signaling during adaptive immune response.; . TISSUE SPECIFICITY: Expressed in spleen, prostate, testis, uterus, small intestine, colon, peripheral blood leukocytes, heart, placenta, lung, liver, skeletal muscle, and pancreas Isoform 2 is ubiquitously expressed (at lower levels than isoform 1). {ECO:0000269|PubMed:12721283, ECO:0000269|PubMed:14519765, ECO:0000269|PubMed:19412184}.; . . . 0.10037 0.393270925 76.04977589 . . TICRR 9.15261267789813e-12 0.999943605413345 5.63945775025466e-05 TOPBP1 interacting checkpoint and replication regulator FUNCTION: Regulator of DNA replication and S/M and G2/M checkpoints. Regulates the triggering of DNA replication initiation via its interaction with TOPBP1 by participating in CDK2-mediated loading of CDC45L onto replication origins. Required for the transition from pre-replication complex (pre-RC) to pre- initiation complex (pre-IC). Required to prevent mitotic entry after treatment with ionizing radiation. {ECO:0000269|PubMed:20116089}.; . . . . 0.66246 . 1.271317214 93.63647087 8928.73049 20.43351 TIE1 8.71416663313257e-12 0.966751502999838 0.0332484969914481 tyrosine kinase with immunoglobulin like and EGF like domains 1 FUNCTION: Transmembrane tyrosine-protein kinase that may modulate TEK/TIE2 activity and contribute to the regulation of angiogenesis. {ECO:0000269|PubMed:20227369}.; . TISSUE SPECIFICITY: Specifically expressed in developing vascular endothelial cells.; . . 0.23923 0.26819 -1.965936983 1.828261382 155.13715 2.72083 TIFA 0.118201140622243 0.779185691109029 0.102613168268728 TRAF interacting protein with forkhead associated domain FUNCTION: Adapter protein which mediates the IRAK1 and TRAF6 interaction following IL-1 stimulation, resulting in the downstream activation of NF-kappa-B and AP-1 pathways. Induces the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism. {ECO:0000269|PubMed:12566447, ECO:0000269|PubMed:15492226}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;uterus;prostate;atrium;whole body;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;pharynx;blood;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;skeletal muscle; 0.08097 0.08539 -0.029247611 51.40363293 111.46032 2.29910 TIFAB 1.15428409214873e-06 0.0572865683390476 0.94271227737686 TIFA inhibitor FUNCTION: Inhibits TIFA-mediated TRAF6 activation possibly by inducing a conformational change in TIFA. {ECO:0000269|PubMed:15047173}.; . . . . . 0.08906 -0.227663163 37.11370606 22.10502 0.74288 TIGAR . . . TP53 induced glycolysis regulatory phosphatase FUNCTION: Fructose-bisphosphatase hydrolyzing fructose-2,6- bisphosphate as well as fructose-1,6-bisphosphate (PubMed:19015259). Acts as a negative regulator of glycolysis by lowering intracellular levels of fructose-2,6-bisphosphate in a p53/TP53-dependent manner, resulting in the pentose phosphate pathway (PPP) activation and NADPH production (PubMed:16839880, PubMed:22887998). Contributes to the generation of reduced glutathione to cause a decrease in intracellular reactive oxygen species (ROS) content, correlating with its ability to protect cells from oxidative or metabolic stress-induced cell death (PubMed:16839880, PubMed:19713938, PubMed:23726973, PubMed:22887998, PubMed:23817040). Plays a role in promoting protection against cell death during hypoxia by decreasing mitochondria ROS levels in a HK2-dependent manner through a mechanism that is independent of its fructose-bisphosphatase activity (PubMed:23185017). In response to cardiac damage stress, mediates p53-induced inhibition of myocyte mitophagy through ROS levels reduction and the subsequent inactivation of BNIP3. Reduced mitophagy results in an enhanced apoptotic myocyte cell death, and exacerbates cardiac damage (By similarity). Plays a role in adult intestinal regeneration; contributes to the growth, proliferation and survival of intestinal crypts following tissue ablation (PubMed:23726973). Plays a neuroprotective role against ischemic brain damage by enhancing PPP flux and preserving mitochondria functions (By similarity). Protects glioma cells from hypoxia- and ROS-induced cell death by inhibiting glycolysis and activating mitochondrial energy metabolism and oxygen consumption in a TKTL1- dependent and p53/TP53-independent manner (PubMed:22887998). Plays a role in cancer cell survival by promoting DNA repair through activating PPP flux in a CDK5-ATM-dependent signaling pathway during hypoxia and/or genome stress-induced DNA damage responses (PubMed:25928429). Involved in intestinal tumor progression (PubMed:23726973). {ECO:0000250|UniProtKB:Q8BZA9, ECO:0000269|PubMed:16839880, ECO:0000269|PubMed:19015259, ECO:0000269|PubMed:19713938, ECO:0000269|PubMed:22887998, ECO:0000269|PubMed:23185017, ECO:0000269|PubMed:23726973, ECO:0000269|PubMed:23817040, ECO:0000269|PubMed:25928429}.; . TISSUE SPECIFICITY: Expressed in the brain (PubMed:22887998). Expressed in breast tumors (PubMed:21820150). Expressed in glioblastomas (PubMed:22887998). {ECO:0000269|PubMed:21820150, ECO:0000269|PubMed:22887998}.; . . 0.06473 0.10293 -0.029247611 51.40363293 . . TIGD1 . . . tigger transposable element derived 1 . . . . . . . . . 119.93261 2.38592 TIGD2 7.02044932871713e-06 0.482131625258157 0.517861354292515 tigger transposable element derived 2 . . . unclassifiable (Anatomical System);cartilage;colon;uterus;breast;lung;placenta;bone;visual apparatus;liver;testis;spleen;kidney;stomach; superior cervical ganglion;trigeminal ganglion; 0.11981 . -0.135838822 43.77211607 1096.4373 6.33599 TIGD3 7.77840778267298e-11 0.0199623296980684 0.980037670224148 tigger transposable element derived 3 . . . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;lung;nasopharynx;placenta;bone;macula lutea;testis;brain; superior cervical ganglion;trigeminal ganglion; 0.14436 0.10269 -0.424258538 25.56027365 410.57172 4.24683 TIGD4 0.00192450479967101 0.906231475354446 0.0918440198458828 tigger transposable element derived 4 . . . unclassifiable (Anatomical System);medulla oblongata;lung;liver;testis;kidney;skeletal muscle; superior cervical ganglion;appendix;atrioventricular node;trigeminal ganglion;skin; 0.18340 . 0.464864541 78.69190847 254.94757 3.43450 TIGD5 0.000172428541029168 0.454277628357236 0.545549943101735 tigger transposable element derived 5 . . . ovary;islets of Langerhans;muscle;colon;fovea centralis;choroid;lens;skin;skeletal muscle;retina;prostate;optic nerve;lung;endometrium;macula lutea;liver;testis;kidney;brain;mammary gland; subthalamic nucleus;superior cervical ganglion;medulla oblongata;temporal lobe;kidney;atrioventricular node;skeletal muscle;cerebellum; 0.12455 0.09980 . . 82.12906 1.92231 TIGD6 4.86406711005621e-06 0.236370822672233 0.763624313260657 tigger transposable element derived 6 . . . unclassifiable (Anatomical System);heart;ovary;pineal body;colon;parathyroid;skin;retina;uterus;optic nerve;lung;placenta;spleen;kidney;brain; parietal lobe; 0.10490 . 1.355871599 94.40905874 778.86539 5.52385 TIGD7 1.86840685100942e-07 0.42479333547057 0.575206477688745 tigger transposable element derived 7 . . TISSUE SPECIFICITY: Expressed in all tissues tested. Higher expression in testis and ovary. {ECO:0000269|PubMed:15487591}.; unclassifiable (Anatomical System);heart;ovary;hypothalamus;colon;parathyroid;blood;skin;bone marrow;prostate;lung;endometrium;larynx;placenta;visual apparatus;liver;testis;head and neck;kidney; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.10163 . -0.642904474 16.62538335 85.14901 1.96714 TIGIT 0.0451499001724995 0.852050768238417 0.102799331589084 T-cell immunoreceptor with Ig and ITIM domains FUNCTION: Binds with high affinity to the poliovirus receptor (PVR) which causes increased secretion of IL10 and decreased secretion of IL12B and suppresses T-cell activation by promoting the generation of mature immunoregulatory dendritic cells. {ECO:0000269|PubMed:19011627}.; . TISSUE SPECIFICITY: Expressed at low levels on peripheral memory and regulatory CD4+ T-cells and NK cells and is up-regulated following activation of these cells (at protein level). {ECO:0000269|PubMed:19011627}.; . . 0.07923 . -0.381986487 27.68931352 395.11564 4.17655 TIMD4 4.33746964441321e-08 0.20511300446965 0.794886952155654 T-cell immunoglobulin and mucin domain containing 4 FUNCTION: Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Involved in regulating T-cell proliferation and lymphotoxin signaling. Ligand for HAVCR1/TIMD1 (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;lung;cartilage;testis;kidney; . 0.06333 0.08225 0.156217551 64.82071243 445.69225 4.39455 TIMELESS 1.03547195051349e-25 0.155176324386798 0.844823675613202 timeless circadian clock FUNCTION: Plays an important role in the control of DNA replication, maintenance of replication fork stability, maintenance of genome stability throughout normal DNA replication and in the regulation of the circadian clock. Involved in the determination of period length and in the DNA damage-dependent phase advancing of the circadian clock. Negatively regulates CLOCK|NPAS2-ARTNL/BMAL1|ARTNL2/BMAL2-induced transactivation of PER1 possibly via translocation of PER1 into the nucleus. Forms a complex with TIPIN and this complex regulates DNA replication processes under both normal and stress conditions, stabilizes replication forks and influences both CHEK1 phosphorylation and the intra-S phase checkpoint in response to genotoxic stress. Timeless promotes TIPIN nuclear localization. Involved in cell survival after DNA damage or replication stress. May be specifically required for the ATR-CHEK1 pathway in the replication checkpoint induced by hydroxyurea or ultraviolet light. May also play an important role in epithelial cell morphogenesis and formation of branching tubules. {ECO:0000269|PubMed:17141802, ECO:0000269|PubMed:17296725, ECO:0000269|PubMed:23418588, ECO:0000269|PubMed:9856465}.; . TISSUE SPECIFICITY: Expressed in all tissues examined including brain, heart, lung, liver, skeletal muscle, kidney, placenta, pancreas, spleen, thymus and testis. Highest levels of expression in placenta, pancreas, thymus and testis. {ECO:0000269|PubMed:9856465, ECO:0000269|PubMed:9891984}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;duodenum;liver;cervix;head and neck;kidney;mammary gland;stomach;thymus; subthalamic nucleus;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.32396 0.20430 0.372852703 75.12974758 9968.9554 21.74053 TIMM8A 0.605876721088247 0.358039033755032 0.0360842451567207 translocase of inner mitochondrial membrane 8 homolog A (yeast) FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins. Probably necessary for normal neurologic development. {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:15254020}.; DISEASE: Mohr-Tranebjaerg syndrome (MTS) [MIM:304700]: Recessive neurodegenerative syndrome characterized by postlingual progressive sensorineural deafness as the first presenting symptom in early childhood, followed by progressive dystonia, spasticity, dysphagia, mental deterioration, paranoia and cortical blindness. {ECO:0000269|PubMed:10878669, ECO:0000269|PubMed:11875042, ECO:0000269|PubMed:11956200}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Jensen syndrome (JENSS) [MIM:311150]: X-linked disease characterized by deafness, blindness and muscle weakness. {ECO:0000269|PubMed:11803487}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in fetal and adult brain, followed by fetal lung, liver and kidney. Also expressed in heart, placenta, lung, liver, kidney, pancreas, skeletal muscle and heart.; . . 0.36253 0.24974 0.035072054 56.2514744 . . TIMM8AP1 . . . translocase of inner mitochondrial membrane 8 homolog A (yeast) pseudogene 1 . . . . . . . . . . . TIMM8B 0.226807933085792 0.64679762003514 0.126394446879068 translocase of inner mitochondrial membrane 8 homolog B (yeast) FUNCTION: Probable mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart, kidney, liver and skeletal muscle. {ECO:0000269|PubMed:10611480}.; . . 0.33602 0.14485 -0.141298762 42.87567823 14.99898 0.53932 TIMM8BP1 . . . translocase of inner mitochondrial membrane 8B pseudogene 1 . . . . . . . . . . . TIMM8BP2 . . . translocase of inner mitochondrial membrane 8B pseudogene 2 . . . . . . . . . . . TIMM9 0.437845525129567 0.531661772838597 0.0304927020318355 translocase of inner mitochondrial membrane 9 FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. {ECO:0000269|PubMed:14726512}.; . TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart, kidney, liver and skeletal muscle. {ECO:0000269|PubMed:10552927, ECO:0000269|PubMed:10611480}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;bone;testis;bladder;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;kidney; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.36582 . 0.057118534 57.99716914 4.71128 0.17005 TIMM9P1 . . . TIMM9 pseudogene 1 . . . . . . . . . . . TIMM9P2 . . . TIMM9 pseudogene 2 . . . . . . . . . . . TIMM9P3 . . . TIMM9 pseudogene 3 . . . . . . . . . . . TIMM10 0.00949476231742544 0.592469562430948 0.398035675251627 translocase of inner mitochondrial membrane 10 homolog (yeast) FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. {ECO:0000269|PubMed:14726512}.; . TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart, kidney, liver and skeletal muscle. {ECO:0000269|PubMed:10552927, ECO:0000269|PubMed:10611480}.; myocardium;lymphoreticular;ovary;skin;retina;prostate;germinal center;bladder;brain;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; thalamus;globus pallidus;pons; 0.20075 0.12971 0.013025609 54.62962963 2.97895 0.10792 TIMM10B 0.00115870998097543 0.622334870864976 0.376506419154048 translocase of inner mitochondrial membrane 10 homolog B (yeast) FUNCTION: Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin- pore translocase that uses the membrane potential as the external driving force. In the TIM22 complex, it may act as a docking point for the soluble 70 kDa complex that guides the target proteins in transit through the aqueous mitochondrial intermembrane space. {ECO:0000269|PubMed:14726512}.; . TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart, kidney, liver and skeletal muscle. {ECO:0000269|PubMed:10611480, ECO:0000269|PubMed:14726512}.; . . 0.13502 0.09393 0.3032669 72.009908 163.53864 2.79247 TIMM13 0.309091873509944 0.618292448688601 0.0726156778014549 translocase of inner mitochondrial membrane 13 FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins. {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:15254020}.; . TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart, kidney, liver and skeletal muscle.; lymphoreticular;smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;duodenum;head and neck;kidney;stomach;aorta;cerebellum; . 0.10507 0.13405 -0.031067188 51.03798066 5.19752 0.19367 TIMM17A 0.243777584003779 0.749540873241096 0.00668154275512442 translocase of inner mitochondrial membrane 17 homolog A (yeast) FUNCTION: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.; . . . . 0.54657 0.12853 0.080983847 59.76055674 507.9116 4.62214 TIMM17B 0.826908628916093 0.169363492060962 0.00372787902294535 translocase of inner mitochondrial membrane 17 homolog B (yeast) FUNCTION: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.; . TISSUE SPECIFICITY: Expression is abundant in heart and skeletal muscle, intermediate in brain, and weak in pancreas, placenta, kidney and liver.; . . 0.21089 0.12090 -0.119252484 44.53880632 12.23581 0.44309 TIMM17BP1 . . . translocase of inner mitochondrial membrane 17 homolog B (yeast) pseudogene 1 . . . . . . . . . . . TIMM21 0.00532093086929824 0.969541323621527 0.0251377455091744 translocase of inner mitochondrial membrane 21 FUNCTION: Participates in the translocation of transit peptide- containing proteins across the mitochondrial inner membrane. Also required for assembly of mitochondrial respiratory chain complex I and complex IV as component of some MITRAC complex, a cytochrome c oxidase (COX) assembly intermediate complex. TIM21 probably shuttles between the presequence translocase and respiratory-chain assembly intermediates in a process that promotes incorporation of early nuclear-encoded subunits into these complexes. {ECO:0000269|PubMed:23260140}.; . . ovary;salivary gland;intestine;colon;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;pituitary gland;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;pharynx;blood;lens;breast;bile duct;pancreas;pia mater;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; skeletal muscle; 0.04212 . -0.249709319 35.74545883 493.87823 4.56967 TIMM22 0.00362100661079949 0.627145731056892 0.369233262332309 translocase of inner mitochondrial membrane 22 homolog (yeast) FUNCTION: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps (By similarity). {ECO:0000250}.; . . medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;kidney;stomach; whole brain;skeletal muscle; 0.15474 0.10730 0.104848986 61.49445624 29.08706 0.92997 TIMM23 0.597093477480232 0.393520656097418 0.0093858664223508 translocase of inner mitochondrial membrane 23 FUNCTION: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.; . . ovary;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.27701 0.15588 . . 4.70642 0.16982 TIMM23B . . . translocase of inner mitochondrial membrane 23 homolog B FUNCTION: May participate in the translocation of transit peptide- containing proteins across the mitochondrial inner membrane. the PAM complex (By similarity). {ECO:0000250}.; . . . . 0.17101 0.11262 . . . . TIMM44 0.818201941811417 0.181790518857593 7.53933099002721e-06 translocase of inner mitochondrial membrane 44 FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Recruits mitochondrial HSP70 to drive protein translocation into the matrix using ATP as an energy source.; . . medulla oblongata;ovary;colon;parathyroid;skin;uterus;prostate;frontal lobe;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; heart;tumor;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.16585 0.17960 0.090079492 60.64519934 250.25034 3.40716 TIMM50 0.442656936727353 0.557064432469105 0.000278630803542587 translocase of inner mitochondrial membrane 50 FUNCTION: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Has some phosphatase activity in vitro; however such activity may not be relevant in vivo. Isoform 2 may participate in the release of snRNPs and SMN from the Cajal body. {ECO:0000269|PubMed:15044455}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in brain, kidney and liver (at protein level). {ECO:0000269|PubMed:15044455, ECO:0000269|PubMed:16008839}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; testis; 0.15447 0.10784 -0.045835247 50.34206181 685.25632 5.22760 TIMMDC1 5.67649555021519e-07 0.424495970098597 0.575503462251848 translocase of inner mitochondrial membrane domain containing 1 FUNCTION: Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Participates in constructing the membrane arm of complex I. {ECO:0000269|PubMed:24191001}.; . TISSUE SPECIFICITY: Generalized expression enhanced in heart and skeletal muscle. {ECO:0000269|PubMed:11092749}.; myocardium;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;germinal center;ciliary body;bladder;brain;tonsil;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;amnion;head and neck;kidney;stomach;aorta; . 0.02069 0.06581 0.350995466 74.37485256 950.56602 5.96895 TIMP1 0.766877187652718 0.224839666446524 0.00828314590075748 TIMP metallopeptidase inhibitor 1 FUNCTION: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. {ECO:0000269|PubMed:1420137, ECO:0000269|PubMed:16917503, ECO:0000269|PubMed:17050530, ECO:0000269|PubMed:1730286, ECO:0000269|PubMed:20545310, ECO:0000269|PubMed:22427646, ECO:0000269|PubMed:24635319, ECO:0000269|PubMed:3839290, ECO:0000269|PubMed:3903517, ECO:0000269|PubMed:8541540, ECO:0000269|PubMed:8576151, ECO:0000269|PubMed:9065415}.; . TISSUE SPECIFICITY: Detected in rheumatoid synovial fluid (at protein level). {ECO:0000269|PubMed:1730286}.; myocardium;lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;prostate;endometrium;thyroid;bladder;brain;gall bladder;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;choroid;vein;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; uterus corpus;adipose tissue;smooth muscle;heart;trigeminal ganglion; 0.47837 0.89776 0.058937498 58.26256192 1075.67102 6.28567 TIMP2 0.526868279273317 0.456965048501557 0.0161666722251259 TIMP metallopeptidase inhibitor 2 FUNCTION: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19. {ECO:0000269|PubMed:11710594, ECO:0000269|PubMed:2554304, ECO:0000269|PubMed:2793861}.; . . smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;cerebral cortex;oesophagus;endometrium;bone;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pineal body;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach;cerebellum; placenta; 0.29915 . -0.317668748 31.45789101 11.9714 0.43425 TIMP3 0.112088669149861 0.859458119698747 0.0284532111513925 TIMP metallopeptidase inhibitor 3 FUNCTION: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15.; DISEASE: Sorsby fundus dystrophy (SFD) [MIM:136900]: Rare autosomal dominant macular disorder with an age of onset in the fourth decade. It is characterized by loss of central vision from subretinal neovascularization and atrophy of the ocular tissues. Generally, macular disciform degeneration develops in the patients eye within 6 months to 6 years. {ECO:0000269|PubMed:7550309, ECO:0000269|PubMed:7894485, ECO:0000269|PubMed:8634721, ECO:0000269|PubMed:8728699, ECO:0000269|PubMed:8981947}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;thyroid;bone;iris;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;spinal cord;muscle;urinary;adrenal cortex;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;olfactory bulb;adipose tissue;trachea;placenta;thyroid;ciliary ganglion;fetal lung;trigeminal ganglion; 0.30945 . -0.141298762 42.87567823 12.37507 0.44875 TIMP4 0.00355403121695193 0.840048913372754 0.156397055410294 TIMP metallopeptidase inhibitor 4 FUNCTION: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7 and MMP- 9.; . TISSUE SPECIFICITY: Abundant in heart and present at low levels in many other tissues.; unclassifiable (Anatomical System);myocardium;cartilage;heart;islets of Langerhans;choroid;skin;uterus;cerebral cortex;larynx;bone;placenta;liver;pituitary gland;head and neck;brain;artery;aorta;stomach; dorsal root ganglion;adipose tissue;cerebellum peduncles;ciliary ganglion;pons;trigeminal ganglion;cerebellum; 0.54062 0.28405 -0.494039303 22.09247464 14.56503 0.52501 TINAG 4.10810051835617e-18 0.002705016528731 0.997294983471269 tubulointerstitial nephritis antigen FUNCTION: Mediates adhesion of proximal tubule epithelial cells via integrins alpha3-beta1 and alphaV-beta3. This is a non catalytic peptidase C1 family protein. {ECO:0000269|PubMed:8770961}.; . TISSUE SPECIFICITY: Expressed in the kidney cortex, small intestine and cornea. {ECO:0000269|PubMed:10652240, ECO:0000269|PubMed:10752525, ECO:0000269|PubMed:1762287}.; unclassifiable (Anatomical System);colon;blood;kidney;skeletal muscle;stomach; dorsal root ganglion;kidney; 0.19301 0.12955 1.067416815 91.66666667 2540.26773 9.41270 TINAGL1 0.245105548080211 0.75461851240357 0.000275939516218786 tubulointerstitial nephritis antigen like 1 FUNCTION: May be implicated in the adrenocortical zonation and in mechanisms for repressing the CYP11B1 gene expression in adrenocortical cells. This is a non catalytic peptidase C1 family protein (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in aorta, heart, placenta, kidney and a colorectal adenocarcinoma cell line. Moderately expressed in skeletal muscle, pancreas, lung, lymph nodes, adrenal gland, bone marrow and thyroid. Weakly expressed in colon, small intestine, ovary, spleen, testis and prostate. Predominantly found in vascular smooth muscle cells, but also in cardiac and skeletal muscle cells as well as kidney. {ECO:0000269|PubMed:11170462}.; ovary;colon;skin;uterus;prostate;endometrium;cerebral cortex;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;urinary;lens;breast;pancreas;lung;placenta;visual apparatus;liver;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.26016 0.11244 -0.690637458 15.12149092 64.61353 1.64901 TINCR . . . tissue differentiation-inducing non-protein coding RNA . . . . . . . . . . . TINF2 0.158554363406221 0.840774510720686 0.000671125873092717 TERF1 (TRF1)-interacting nuclear factor 2 FUNCTION: Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Plays a role in shelterin complex assembly. Isoform 1 may have additional role in tethering telomeres to the nuclear matrix. {ECO:0000269|PubMed:16166375, ECO:0000269|PubMed:16880378}.; DISEASE: Dyskeratosis congenita, autosomal dominant, 3 (DKCA3) [MIM:613990]: A rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy. {ECO:0000269|PubMed:18252230}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Dyskeratosis congenita, autosomal dominant, 5 (DKCA5) [MIM:268130]: A disease characterized by bone marrow hypoplasia, nail dystrophy, fine sparse hair, fine reticulate skin pigmentation, oral leukoplakia, bilateral exudative retinopathy, cerebellar hypoplasia, and growth retardation. {ECO:0000269|PubMed:18252230}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;aorta;stomach; superior cervical ganglion;globus pallidus;white blood cells;ciliary ganglion;trigeminal ganglion; 0.11373 0.10739 0.018483465 55.44939844 264.91502 3.49366 TIPARP 0.997752090167203 0.00224783359647807 7.62363185794412e-08 TCDD-inducible poly(ADP-ribose) polymerase FUNCTION: Poly [ADP-ribose] polymerase using NAD(+) as a substrate to transfer ADP-ribose onto glutamic acid residues of a protein acceptor; repeated rounds of ADP-ribosylation leads to the formation of poly(ADPribose) chains on the protein, thereby altering the function of the target protein. May play a role in the adaptive response to chemical exposure (TCDD) and thereby mediates certain effects of the chemicals (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;whole body;cerebral cortex;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;skeletal muscle;greater omentum;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;adrenal cortex;testis;atrioventricular node;trigeminal ganglion; 0.43821 0.12448 -0.66859065 15.76433121 52.4418 1.43246 TIPARP-AS1 . . . TIPARP antisense RNA 1 . . . . . . . . . . . TIPIN 0.00983208458317475 0.942185447294077 0.0479824681227479 TIMELESS interacting protein FUNCTION: Plays an important role in the control of DNA replication and the maintenance of replication fork stability. Important for cell survival after DNA damage or replication stress. May be specifically required for the ATR-CHEK1 pathway in the replication checkpoint induced by hydroxyurea or ultraviolet light. Forms a complex with TIMELESS and this complex regulates DNA replication processes under both normal and stress conditions, stabilizes replication forks and influences both CHEK1 phosphorylation and the intra-S phase checkpoint in response to genotoxic stress. {ECO:0000269|PubMed:17102137, ECO:0000269|PubMed:17116885, ECO:0000269|PubMed:17296725}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;salivary gland;adrenal cortex;intestine;pharynx;colon;blood;vein;skin;breast;uterus;prostate;lung;adrenal gland;bone;visual apparatus;liver;testis;kidney;brain;mammary gland;bladder; testis - interstitial;testis - seminiferous tubule;testis; 0.80134 0.08685 0.72761005 86.08162302 1665.32698 7.53505 TIPRL 0.867249670452818 0.13236387855433 0.000386450992852041 TOR signaling pathway regulator FUNCTION: May be a allosteric regulator of serine/threonine- protein phosphatase 2A (PP2A). Isoform 1 inhibits catalytic activity of the PP2A(D) core complex in vitro. The PP2A(C):TIPRL complex does not show phosphatase activity. May play a role in the regulation of ATM/ATR signaling pathway controlling DNA replication and repair. {ECO:0000269|PubMed:17384681}.; . . . . 0.16920 0.08495 0.103030231 61.2762444 38.65761 1.14568 TIRAP 0.00266923121316854 0.56108925540907 0.436241513377761 toll-interleukin 1 receptor (TIR) domain containing adaptor protein FUNCTION: Adapter involved in TLR2 and TLR4 signaling pathways in the innate immune response. Acts via IRAK2 and TRAF-6, leading to the activation of NF-kappa-B, MAPK1, MAPK3 and JNK, and resulting in cytokine secretion and the inflammatory response. Positively regulates the production of TNF-alpha and interleukin-6. {ECO:0000269|PubMed:18292575, ECO:0000269|PubMed:19509286}.; . TISSUE SPECIFICITY: Highly expressed in liver, kidney, spleen, skeletal muscle and heart. Also detected in peripheral blood leukocytes, lung, placenta, small intestine, thymus, colon and brain.; unclassifiable (Anatomical System);uterus;lung;frontal lobe;cartilage;heart;lacrimal gland;liver;kidney;germinal center;cerebellum; superior cervical ganglion;fetal liver;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12178 0.41088 1.06196211 91.507431 759.06115 5.45859 TJAP1 0.00105939310202612 0.949837041436103 0.0491035654618703 tight junction associated protein 1 . . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11602598}.; lymphoreticular;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;endometrium;synovium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;caudate nucleus;pons;trigeminal ganglion;parietal lobe; 0.30734 . 0.244401822 69.50931824 333.93467 3.88126 TJP1 0.999999982283293 1.77167068390396e-08 4.72237711510172e-23 tight junction protein 1 FUNCTION: The N-terminal may be involved in transducing a signal required for tight junction assembly, while the C-terminal may have specific properties of tight junctions. The alpha domain might be involved in stabilizing junctions. Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells. {ECO:0000269|PubMed:21240187}.; . TISSUE SPECIFICITY: The alpha-containing isoform is found in most epithelial cell junctions. The short isoform is found both in endothelial cells and the highly specialized epithelial junctions of renal glomeruli and Sertoli cells of the seminiferous tubules.; ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;spinal cord;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;aorta;stomach; dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;caudate nucleus;pons;atrioventricular node;skeletal muscle;uterus;subthalamic nucleus;testis;appendix;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.25442 0.73774 -1.784094322 2.264685067 1761.96515 7.74921 TJP1P1 . . . tight junction protein 1 pseudogene 1 . . . . . . . . . . . TJP2 6.24313389627035e-07 0.999943176310757 5.61993758537402e-05 tight junction protein 2 FUNCTION: Plays a role in tight junctions and adherens junctions.; DISEASE: Cholestasis, progressive familial intrahepatic, 4 (PFIC4) [MIM:615878]: A disorder characterized by early onset of cholestasis that progresses to hepatic fibrosis, cirrhosis, and end-stage liver disease before adulthood. {ECO:0000269|PubMed:24614073}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: This protein is found in epithelial cell junctions. Isoform A1 is abundant in the heart and brain. Detected in brain and skeletal muscle. It is present almost exclusively in normal tissues. Isoform C1 is expressed at high level in the kidney, pancreas, heart and placenta. Not detected in brain and skeletal muscle. Found in normal as well as in most neoplastic tissues. {ECO:0000269|PubMed:11018256}.; ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;islets of Langerhans;spinal cord;blood;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; spinal cord;testis; 0.30256 0.24991 1.458702267 95.175749 1977.00591 8.19300 TJP3 2.20425161433974e-21 0.00606470296161349 0.993935297038387 tight junction protein 3 . . . medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;pharynx;blood;lens;bile duct;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis;trigeminal ganglion;skeletal muscle; 0.13413 . 0.133973982 63.49374853 2712.93434 9.80631 TK1 0.255670113108694 0.716682061845506 0.0276478250457998 thymidine kinase 1, soluble . . . lymphoreticular;ovary;colon;parathyroid;skin;uterus;prostate;endometrium;gum;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;breast;pancreas;lung;epididymis;placenta;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; tumor;atrioventricular node;bone marrow; 0.74099 0.44443 -0.205617011 38.57631517 21.18376 0.71530 TK2 0.00326975294791418 0.94875292874781 0.0479773183042754 thymidine kinase 2, mitochondrial FUNCTION: Deoxyribonucleoside kinase that phosphorylates thymidine, deoxycytidine, and deoxyuridine. Also phosphorylates anti-viral and anti-cancer nucleoside analogs.; . TISSUE SPECIFICITY: Predominantly expressed in liver, pancreas, muscle, and brain.; medulla oblongata;sympathetic chain;colon;substantia nigra;skin;uterus;prostate;frontal lobe;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);trophoblast;heart;islets of Langerhans;muscle;adrenal cortex;pancreas;lung;placenta;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;thalamus;superior cervical ganglion;adipose tissue;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.17859 0.64916 -0.251530012 35.42108988 1057.53672 6.24339 TKCR . . . torticollis, keloids, cryptorchidism and renal dysplasia . . . . . . . . . . . TKFC . . . triokinase and FMN cyclase FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. Represses IFIH1-mediated cellular antiviral response (PubMed:17600090). {ECO:0000250|UniProtKB:F1RKQ4, ECO:0000250|UniProtKB:Q4KLZ6, ECO:0000269|PubMed:16289032, ECO:0000269|PubMed:17600090, ECO:0000269|PubMed:4688871}.; . TISSUE SPECIFICITY: Detected in erythrocytes (at protein level). {ECO:0000269|PubMed:4688871}.; . . 0.36278 0.29825 -0.484940685 22.75300778 . . TKT 0.0602834945523099 0.939003972939982 0.000712532507708422 transketolase FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.; . . smooth muscle;ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;placenta;duodenum;kidney;stomach;aorta;thymus; lung;adipose tissue;tumor;white blood cells;whole blood;bone marrow; 0.70473 0.45915 -0.486758915 22.69992923 183.88986 2.94375 TKTL1 0.99702623090185 0.00297361822213226 1.50876017965209e-07 transketolase-like 1 FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in fetal and adult heart, brain, lung, liver, and kidney, and in adult placenta, skeletal muscle and pancreas. Up-regulated in various epithelial tumors. {ECO:0000269|PubMed:15991799, ECO:0000269|PubMed:16465194, ECO:0000269|PubMed:16969476, ECO:0000269|PubMed:8838793}.; unclassifiable (Anatomical System);lymphoreticular;ovary;blood;parathyroid;skeletal muscle;bone marrow;prostate;lung;placenta;hippocampus;visual apparatus;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion; 0.16475 0.26069 -0.909290275 10.03184713 66.90862 1.68977 TKTL2 8.54252539945376e-05 0.774992525939126 0.224922048806879 transketolase-like 2 FUNCTION: Plays an essential role in total transketolase activity and cell proliferation in cancer cells; after transfection with anti-TKTL1 siRNA, total transketolase activity dramatically decreases and proliferation was significantly inhibited in cancer cells. Plays a pivotal role in carcinogenesis. {ECO:0000269|PubMed:17321041}.; . TISSUE SPECIFICITY: Overexpressed in hepatoma cancer cells. {ECO:0000269|PubMed:17321041}.; unclassifiable (Anatomical System);medulla oblongata;lung;developmental;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.29966 0.19098 -0.174473069 40.59919792 444.57048 4.38661 TLCD1 0.0111498745060289 0.839432529162595 0.149417596331376 TLC domain containing 1 FUNCTION: Calcium channel facilitator that increases calcium flux by generating a larger window current and slowing inactivation of the L-type CACNA1C/CaV1.2 channel. Regulation of intracellular calcium by Calfacilitin is required for neural plate formation (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;colon;parathyroid;skin;uterus;pancreas;prostate;lung;liver;testis;spleen;brain;stomach; . 0.25099 . 0.016664174 55.21939137 37.57849 1.11945 TLCD2 . . . TLC domain containing 2 . . . unclassifiable (Anatomical System);brain; . 0.17155 . . . 146.97176 2.64097 TLDC1 2.2902052991234e-12 0.00931992427324137 0.990680075724468 TBC/LysM-associated domain containing 1 . . . . . 0.48705 0.09993 1.76373572 96.76220807 650.61756 5.11728 TLDC2 0.113178686310675 0.858812086947773 0.0280092267415519 TBC/LysM-associated domain containing 2 . . . . . 0.15281 . 0.483275131 79.25218212 299.75126 3.69170 TLE1 0.957285090965036 0.0427147323025395 1.76732424414584e-07 transducin like enhancer of split 1 FUNCTION: Transcriptional corepressor that binds to a number of transcription factors. Inhibits NF-kappa-B-regulated gene expression. Inhibits the transcriptional activation mediated by FOXA2, and by CTNNB1 and TCF family members in Wnt signaling. The effects of full-length TLE family members may be modulated by association with dominant-negative AES. Unusual function as coactivator for ESRRG. {ECO:0000269|PubMed:10660609}.; . TISSUE SPECIFICITY: In all tissues examined, mostly in brain, liver and muscle.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;synovium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;lens;bile duct;pancreas;lung;placenta;macula lutea;liver;amnion;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.98011 0.25031 -1.572589134 3.161122906 65.84111 1.67081 TLE1P1 . . . transducin like enhancer of split 1 pseudogene 1 . . . . . . . . . . . TLE2 0.000766444994989725 0.998502268378163 0.000731286626846839 transducin like enhancer of split 2 FUNCTION: Transcriptional corepressor that binds to a number of transcription factors. Inhibits the transcriptional activation mediated by CTNNB1 and TCF family members in Wnt signaling. The effects of full-length TLE family members may be modulated by association with dominant-negative AES (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: In all tissues examined, mostly in heart, brain, and muscle.; unclassifiable (Anatomical System);islets of Langerhans;colon;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;prostate;optic nerve;lung;endometrium;bone;placenta;macula lutea;visual apparatus;iris;testis;kidney;brain;mammary gland;tonsil;stomach; ciliary ganglion;atrioventricular node;cerebellum; 0.42263 0.12611 -1.126142808 6.564048125 141.69498 2.59754 TLE3 0.999913536986372 8.64629864459361e-05 2.7181636854871e-11 transducin like enhancer of split 3 FUNCTION: Transcriptional corepressor that binds to a number of transcription factors. Inhibits the transcriptional activation mediated by CTNNB1 and TCF family members in Wnt signaling. The effects of full-length TLE family members may be modulated by association with dominant-negative AES (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Placenta and lung.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;adrenal cortex;blood;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;fetal brain;placenta;testis;ciliary ganglion;atrioventricular node;whole blood;skeletal muscle; 0.66983 0.14755 -1.021348453 7.997169144 29.78111 0.94927 TLE4 0.999921640049606 7.83599460658339e-05 4.32776857984013e-12 transducin like enhancer of split 4 FUNCTION: Transcriptional corepressor that binds to a number of transcription factors. Inhibits the transcriptional activation mediated by PAX5, and by CTNNB1 and TCF family members in Wnt signaling. The effects of full-length TLE family members may be modulated by association with dominant-negative AES. Essential for the transcriptional repressor activity of SIX3 during retina and lens development and for SIX3 transcriptional auto-repression (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: In all tissues examined, mostly in brain, and muscle.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;cerebral cortex;synovium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;small intestine;heart;cartilage;cerebellum cortex;pineal body;lens;breast;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;aorta;thymus; testis - interstitial;temporal lobe;testis;trigeminal ganglion;skeletal muscle; 0.94973 0.14686 -0.556537043 19.72753008 90.91723 2.05178 TLE6 0.00101145755365688 0.987319871000309 0.0116686714460342 transducin like enhancer of split 6 FUNCTION: As a member of the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;lung;ovary;placenta;visual apparatus;testis;colon;choroid;stomach; dorsal root ganglion;pons; 0.08863 0.09503 -1.438469007 3.974994102 24.39003 0.80231 TLK1 0.999994767519327 5.23248064327465e-06 2.93147869172187e-14 tousled like kinase 1 FUNCTION: Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S- phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'. {ECO:0000269|PubMed:10523312, ECO:0000269|PubMed:10588641, ECO:0000269|PubMed:11314006, ECO:0000269|PubMed:11470414, ECO:0000269|PubMed:12660173, ECO:0000269|PubMed:9427565}.; . TISSUE SPECIFICITY: Widely expressed. Present in fetal placenta, liver, kidney and pancreas but not heart or skeletal muscle. Also found in adult cell lines. Isoform 3 is ubiquitously expressed in all tissues examined. {ECO:0000269|PubMed:10588641, ECO:0000269|PubMed:9427565}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;dorsal root ganglion;occipital lobe;superior cervical ganglion;testis - interstitial;temporal lobe;pons;atrioventricular node;skeletal muscle;skin;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.38873 0.11686 -0.404032746 26.53338051 77.88734 1.86155 TLK1P1 . . . tousled like kinase 1 pseudogene 1 . . . . . . . . . . . TLK2 0.999999805897045 1.94102954657165e-07 9.59849056134673e-18 tousled like kinase 2 FUNCTION: Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation. Phosphorylates the chromatin assembly factors ASF1A AND ASF1B. Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly. Negative regulator of amino acid starvation-induced autophagy. {ECO:0000269|PubMed:10523312, ECO:0000269|PubMed:11470414, ECO:0000269|PubMed:12660173, ECO:0000269|PubMed:12955071, ECO:0000269|PubMed:20016786, ECO:0000269|PubMed:22354037, ECO:0000269|PubMed:9427565}.; . TISSUE SPECIFICITY: Ubiquitous. Detected in placenta, fetal liver, kidney, pancreas, heart and skeletal muscle. Highly expressed in testis. Detected in spleen, thymus, colon, ovary, small intestine, prostate and peripheral blood leukocytes. {ECO:0000269|PubMed:9427565, ECO:0000269|PubMed:9662073}.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.36654 0.09988 -0.271755481 34.31823543 14.64528 0.52777 TLK2P1 . . . tousled like kinase 2 pseudogene 1 . . . . . . . . . . . TLK2P2 . . . tousled like kinase 2 pseudogene 2 . . . . . . . . . . . TLL1 0.327496391486389 0.67250356188043 4.66331814827819e-08 tolloid like 1 FUNCTION: Protease which processes procollagen C-propeptides, such as chordin, pro-biglycan and pro-lysyl oxidase. Required for the embryonic development. Predominant protease, which in the development, influences dorsal-ventral patterning and skeletogenesis.; DISEASE: Atrial septal defect 6 (ASD6) [MIM:613087]: A congenital heart malformation characterized by incomplete closure of the wall between the atria resulting in blood flow from the left to the right atria. {ECO:0000269|PubMed:18830233}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;hypothalamus;parathyroid;skin;prostate;lung;placenta;head and neck;amniotic fluid;kidney;spinal ganglion;brain;tonsil; superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.54651 0.13658 -0.927704399 9.719273414 309.19572 3.74397 TLL2 2.18060362101359e-19 0.0464201550449573 0.953579844955043 tolloid like 2 FUNCTION: Protease which specifically processes pro-lysyl oxidase. Required for the embryonic development. Predominant protease, which in the development, influences dorsal-ventral patterning and skeletogenesis.; . . unclassifiable (Anatomical System);prostate;lung;islets of Langerhans;testis;colon;kidney;stomach; superior cervical ganglion;temporal lobe;pons;trigeminal ganglion;skeletal muscle; 0.22812 0.10150 0.345333879 73.7438075 547.20052 4.75680 TLN1 0.999999999998354 1.64572524694243e-12 2.91755280979734e-34 talin 1 FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts (By similarity). {ECO:0000250}.; . . lymphoreticular;smooth muscle;ovary;salivary gland;sympathetic chain;colon;choroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;amniotic fluid;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion; 0.29532 0.38988 -3.420504246 0.365652276 1723.9194 7.66020 TLN2 0.999853230773704 0.000146769226295545 3.8498871534435e-21 talin 2 FUNCTION: As a major component of focal adhesion plaques that links integrin to the actin cytoskeleton, may play an important role in cell adhesion. Recruits PIP5K1C to focal adhesion plaques and strongly activates its kinase activity (By similarity). {ECO:0000250}.; . . myocardium;ovary;colon;parathyroid;skin;retina;uterus;whole body;frontal lobe;thyroid;bone;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);heart;hypothalamus;spinal cord;bile duct;breast;pancreas;lung;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;occipital lobe;globus pallidus;ciliary ganglion;atrioventricular node;kidney;pons;trigeminal ganglion;skin;skeletal muscle;cingulate cortex; 0.30553 0.44698 -3.469503166 0.353857042 2221.48407 8.67915 TLR1 2.02406979914294e-14 0.0011097149136461 0.998890285086334 toll like receptor 1 FUNCTION: Participates in the innate immune response to microbial agents. Specifically recognizes diacylated and triacylated lipopeptides. Cooperates with TLR2 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Forms the activation cluster TLR2:TLR1:CD14 in response to triacylated lipopeptides, this cluster triggers signaling from the cell surface and subsequently is targeted to the Golgi in a lipid-raft dependent pathway. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. {ECO:0000269|PubMed:16880211}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in spleen, ovary, peripheral blood leukocytes, thymus and small intestine.; unclassifiable (Anatomical System);ovary;cartilage;colon;parathyroid;skin;retina;breast;lung;nasopharynx;placenta;bone;testis;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;whole blood;trigeminal ganglion;skeletal muscle; 0.07604 0.35375 1.317245065 94.06699693 761.04412 5.46953 TLR2 9.22924764317956e-05 0.789389849990655 0.210517857532913 toll like receptor 2 FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides (PubMed:17889651). Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. May also promote apoptosis in response to lipoproteins (PubMed:10426996). Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B.burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR6 (PubMed:11441107). Acts as a receptor for M.tuberculosis lipoproteins LprA, LprG, LpqH and PhoS1 (pstS1), some lipoproteins are dependent on other coreceptors (TLR1, CD14 and/or CD36).The lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen (PubMed:19362712). Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (PubMed:16880211). {ECO:0000250|UniProtKB:Q9QUN7, ECO:0000269|PubMed:10426996, ECO:0000269|PubMed:11441107, ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:17889651, ECO:0000269|PubMed:19362712}.; . TISSUE SPECIFICITY: Highly expressed in peripheral blood leukocytes, in particular in monocytes, in bone marrow, lymph node and in spleen. Also detected in lung and in fetal liver. Levels are low in other tissues.; ovary;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;urinary;blood;lens;skeletal muscle;lung;placenta;macula lutea;liver;alveolus;spleen;kidney;mammary gland;stomach; superior cervical ganglion;whole blood;trigeminal ganglion; 0.24434 0.70536 -0.150608082 42.28001887 216.14444 3.17458 TLR3 0.0012112447445172 0.98972736140066 0.00906139385482329 toll like receptor 3 FUNCTION: Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response. {ECO:0000269|PubMed:12471095, ECO:0000269|PubMed:12539043, ECO:0000269|PubMed:16043704, ECO:0000269|PubMed:16144834, ECO:0000269|PubMed:16720699, ECO:0000269|PubMed:16858407, ECO:0000269|PubMed:17178723, ECO:0000269|PubMed:18172197, ECO:0000269|PubMed:22611194}.; DISEASE: Herpes simplex encephalitis 2 (HSE2) [MIM:613002]: A rare complication of human herpesvirus 1 (HHV-1) infection, occurring in only a small minority of HHV-1 infected individuals. HSE is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Onset is over several days and involves fever, headache, seizures, stupor, and often coma, frequently with a fatal outcome. {ECO:0000269|PubMed:17872438}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. TLR3 mutations predispose otherwise healthy individuals to isolated herpes simplex encephalitis through a mechanism that involves impaired IFNs production and reduced immune defense against viral infection in the central nervous system.; TISSUE SPECIFICITY: Expressed at high level in placenta and pancreas. Also detected in CD11c+ immature dendritic cells. Only expressed in dendritic cells and not in other leukocytes, including monocyte precursors. TLR3 is the TLR that is expressed most strongly in the brain, especially in astrocytes, glia, and neurons. {ECO:0000269|PubMed:17085778}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;adrenal cortex;parathyroid;skeletal muscle;retina;breast;larynx;placenta;bone;liver;head and neck;brain;stomach; superior cervical ganglion;trigeminal ganglion; 0.09332 0.53331 -0.24061166 36.28214201 2639.04635 9.63966 TLR4 4.18065301209718e-06 0.831605333832309 0.168390485514679 toll like receptor 4 FUNCTION: Cooperates with LY96 and CD14 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:9237759, PubMed:10835634). Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate, and Ni(2+). Responses triggered by Ni(2+) require non-conserved histidines and are, therefore, species-specific (PubMed:20711192). In complex with TLR6, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid-beta 42-binding to CD36. This event induces the formation of a heterodimer of TLR4 and TLR6, which is rapidly internalized and triggers inflammatory response, leading to the NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion. Binds electronegative LDL (LDL(-)) and mediates the cytokine release induced by LDL(-) (PubMed:23880187). {ECO:0000269|PubMed:10835634, ECO:0000269|PubMed:17478729, ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:20711192, ECO:0000269|PubMed:23880187, ECO:0000269|PubMed:9237759}.; DISEASE: Macular degeneration, age-related, 10 (ARMD10) [MIM:611488]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in placenta, spleen and peripheral blood leukocytes. Detected in monocytes, macrophages, dendritic cells and several types of T-cells. {ECO:0000269|PubMed:9237759, ECO:0000269|PubMed:9435236}.; . . 0.21739 0.91984 -0.016511957 52.31776362 394.37022 4.17423 TLR5 5.68654860439007e-09 0.124172095720572 0.87582789859288 toll like receptor 5 FUNCTION: Participates in the innate immune response to microbial agents. Mediates detection of bacterial flagellins. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. {ECO:0000269|PubMed:11323673}.; DISEASE: Systemic lupus erythematosus 1 (SLEB1) [MIM:601744]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in ovary and in peripheral blood leukocytes, especially in monocytes, less in CD11c+ immature dendritic cells. Also detected in prostate and testis.; unclassifiable (Anatomical System);uterus;pancreas;lung;cartilage;endometrium;placenta;liver;kidney;brain; superior cervical ganglion; 0.07692 0.26632 1.647992642 96.20783204 1072.12876 6.27718 TLR6 0.00730490768109257 0.922812291509583 0.0698828008093246 toll like receptor 6 FUNCTION: Participates in the innate immune response to Gram- positive bacteria and fungi. Specifically recognizes diacylated and, to a lesser extent, triacylated lipopeptides (PubMed:20037584). In response to diacylated lipopeptides, forms the activation cluster TLR2:TLR6:CD14:CD36, this cluster triggers signaling from the cell surface and subsequently is targeted to the Golgi in a lipid-raft dependent pathway (PubMed:16880211). Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B.burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR2 (PubMed:11441107). In complex with TLR4, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid- beta 42-binding to CD36. This event induces the formation of a heterodimer of TLR4 and TLR6, which is rapidly internalized and triggers inflammatory response, leading to the NF-kappa-B- dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion (PubMed:11441107, PubMed:20037584). {ECO:0000269|PubMed:11441107, ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:20037584}.; . TISSUE SPECIFICITY: Detected in monocytes, CD11c+ immature dendritic cells, plasmacytoid pre-dendritic cells and dermal microvessel endothelial cells.; . . 0.10173 0.24306 0.892856963 89.28992687 791.44292 5.54769 TLR7 0.872917548986338 0.126738032513367 0.000344418500295088 toll like receptor 7 FUNCTION: Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR7 is a nucleotide-sensing TLR which is activated by single-stranded RNA. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). {ECO:0000250, ECO:0000269|PubMed:18250417}.; . TISSUE SPECIFICITY: Detected in brain, placenta, spleen, stomach, small intestine, lung and in plasmacytoid pre-dendritic cells.; . . 0.13388 0.28709 -0.400392389 26.85185185 29.84081 0.95176 TLR8 0.931026133439482 0.0689027112770607 7.11552834575877e-05 toll like receptor 8 FUNCTION: Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. {ECO:0000269|PubMed:17932028, ECO:0000269|PubMed:23520111}.; . TISSUE SPECIFICITY: Detected in brain, heart, lung, liver, placenta, in monocytes, and at lower levels in CD11c+ immature dendritic cells.; unclassifiable (Anatomical System);uterus;lung;cartilage;endometrium;placenta;colon;kidney;brain;pineal gland;aorta; whole blood;skeletal muscle; 0.12528 0.19285 -0.244249595 36.17008728 15.2696 0.54913 TLR8-AS1 . . . TLR8 antisense RNA 1 . . . . . . . . . . . TLR9 0.000525225802125772 0.970780863328628 0.0286939108692466 toll like receptor 9 FUNCTION: Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR9 is a nucleotide-sensing TLR which is activated by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Controls lymphocyte response to Helicobacter infection. {ECO:0000269|PubMed:11564765, ECO:0000269|PubMed:17932028}.; . TISSUE SPECIFICITY: Highly expressed in spleen, lymph node, tonsil and peripheral blood leukocytes, especially in plasmacytoid pre- dendritic cells. Levels are much lower in monocytes and CD11c+ immature dendritic cells. Also detected in lung and liver.; unclassifiable (Anatomical System);lymph node;thyroid;germinal center;tonsil; . . 0.50214 -1.609459583 3.001887238 66.05356 1.67440 TLR10 8.43095303268399e-08 0.488132743530498 0.511867172159971 toll like receptor 10 FUNCTION: Participates in the innate immune response to microbial agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in spleen, lymph node, thymus, tonsil and at lower levels in lung. Highly expressed in promyelocytic HL-60 cells and in B-cell lines.; unclassifiable (Anatomical System);lung;nasopharynx;bone;testis;germinal center; . 0.08877 0.21741 2.31873558 98.36046237 5094.97364 14.62665 TLR12P . . . toll like receptor 12, pseudogene . . . . . . . . . . . TLX1 0.463723105013332 0.510805377213976 0.0254715177726922 T-cell leukemia homeobox 1 FUNCTION: Controls the genesis of the spleen. Binds to the DNA sequence 5'-GGCGGTAAGTGG-3'.; DISEASE: Note=A chromosomal aberration involving TLX1 may be a cause of a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(10;14)(q24;q11) with TCRD. {ECO:0000269|PubMed:1676542, ECO:0000269|PubMed:1681546, ECO:0000269|PubMed:1717256}.; . . . 0.47109 0.23230 -0.029247611 51.40363293 102.47812 2.18780 TLX1NB 0.0193356166079286 0.503652476372006 0.477011907020066 TLX1 neighbor . . . . . . . . . 838.36016 5.67049 TLX2 0.140777838183909 0.77934511797711 0.0798770438389813 T-cell leukemia homeobox 2 FUNCTION: Transcription activator that binds DNA elements with the consensus sequence 5'-CGGTAATTGG-3'. Binds DNA via its homeobox. Required for normal cell death of enteric neurons in the gastrointestinal tract. Required for normal development of the enteric nervous system, and for proper development of normal motility of the gastrointestinal tract (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);prostate;optic nerve;lung;macula lutea;visual apparatus;testis;fovea centralis;choroid;germinal center;lens;brain;retina; superior cervical ganglion;cerebellum peduncles;appendix;pons;trigeminal ganglion;skeletal muscle; 0.22610 0.23266 . . 53.18567 1.44855 TLX3 0.302655050937496 0.621540312421309 0.0758046366411951 T-cell leukemia homeobox 3 . . . muscle;brain;bone marrow; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.68995 0.16293 -0.09720619 46.20193442 69.51089 1.73027 TM2D1 0.0420614829227396 0.929476013079884 0.0284625039973761 TM2 domain containing 1 FUNCTION: May participate in beta-amyloid-induced apoptosis via its interaction with beta-APP42. {ECO:0000269|PubMed:11278849, ECO:0000269|PubMed:12836168}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11278849}.; unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;colon;skin;uterus;breast;lung;bone;thyroid;placenta;visual apparatus;liver;testis;spleen;brain;mammary gland;gall bladder; whole brain;amygdala;superior cervical ganglion;thyroid;prefrontal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.34406 0.09894 . . 115.6404 2.33925 TM2D2 0.071028871563027 0.872194560748734 0.0567765676882391 TM2 domain containing 2 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11278849}.; . . 0.12316 0.10048 -0.007201372 53.19061099 29.27218 0.93713 TM2D3 0.00033899537761085 0.59721890152498 0.402442103097409 TM2 domain containing 3 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11278849}.; myocardium;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;stomach; whole brain;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;thalamus;hypothalamus;temporal lobe;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.11740 0.11255 0.350995466 74.37485256 80.9731 1.90334 TM4SF1 0.000859110031523055 0.789901834730305 0.209239055238172 transmembrane 4 L six family member 1 . . TISSUE SPECIFICITY: Highly expressed in lung, breast, colon and ovarian carcinomas. It is also present on some normal cells, endothelial cells in particular.; myocardium;smooth muscle;ovary;colon;parathyroid;vein;skin;uterus;prostate;cochlea;endometrium;larynx;bone;testis;amniotic fluid;dura mater;spinal ganglion;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;tongue;islets of Langerhans;skeletal muscle;breast;bile duct;pancreas;pia mater;lung;trabecular meshwork;placenta;alveolus;liver;spleen;head and neck;cervix;kidney;stomach;aorta; superior cervical ganglion;placenta;adrenal cortex;testis;fetal lung;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.19272 0.10185 -0.295622497 32.61972163 19.10504 0.65886 TM4SF1-AS1 . . . TM4SF1 antisense RNA 1 . . . . . . . . . . . TM4SF4 0.00251101484799328 0.781500681203181 0.215988303948826 transmembrane 4 L six family member 4 FUNCTION: Regulates the adhesive and proliferative status of intestinal epithelial cells. Can mediate density-dependent cell proliferation.; . TISSUE SPECIFICITY: Jejunum and liver.; unclassifiable (Anatomical System);small intestine;ovary;islets of Langerhans;colon;parathyroid;pancreas;whole body;lung;placenta;liver;testis;spleen;kidney;stomach;gall bladder; fetal liver;superior cervical ganglion;beta cell islets;liver;ciliary ganglion;fetal lung;atrioventricular node;trigeminal ganglion; 0.21234 0.08330 -0.271755481 34.31823543 31.88825 1.00321 TM4SF5 1.24445437027964e-05 0.37800860941966 0.621978946036637 transmembrane 4 L six family member 5 . . TISSUE SPECIFICITY: Intestine. Overexpressed in pancreatic cancers.; unclassifiable (Anatomical System);lung;ovary;heart;placenta;liver;testis;colon;parathyroid;spleen;kidney; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.15509 0.13260 -0.05129383 49.75819769 23.18839 0.77462 TM4SF18 2.10380518922091e-07 0.077300966604366 0.922698823015115 transmembrane 4 L six family member 18 . . . unclassifiable (Anatomical System);ovary;islets of Langerhans;hypothalamus;colon;parathyroid;vein;lung;cerebral cortex;nasopharynx;thyroid;placenta;hippocampus;liver;spleen;kidney;brain;mammary gland;stomach; superior cervical ganglion;atrioventricular node; 0.13959 . -0.183570861 39.95046001 13.85926 0.50301 TM4SF19 0.0139308428726723 0.868242385440003 0.117826771687325 transmembrane 4 L six family member 19 . . . unclassifiable (Anatomical System);prostate;lymph node;lung;whole body;frontal lobe;heart;bone;alveolus;testis;blood;kidney;brain;retina; testis - seminiferous tubule;ciliary ganglion;atrioventricular node; 0.06506 . 0.903992902 89.39018636 336.61202 3.89757 TM4SF19-AS1 . . . TM4SF19 antisense RNA 1 . . . . . . . . . . . TM4SF19-TCTEX1D2 . . . TM4SF19-TCTEX1D2 readthrough (NMD candidate) . . . . . . . . . . . TM4SF20 2.18814392829867e-06 0.153947019827756 0.846050792028315 transmembrane 4 L six family member 20 . . TISSUE SPECIFICITY: Expressed in the brain, with high levels in the parietal lobe, hippocampus, pons, white matter and cerebellum. {ECO:0000269|PubMed:23810381}.; colon;blood;kidney;skeletal muscle;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.11504 0.08353 0.705562627 85.52724699 96.59184 2.12324 TM6SF1 6.46941313206752e-05 0.90181038788594 0.0981249179827391 transmembrane 6 superfamily member 1 FUNCTION: May function as sterol isomerase. {ECO:0000303|PubMed:25566323}.; . TISSUE SPECIFICITY: Enhanced expression in spleen, testis and peripheral blood leukocytes.; ovary;parathyroid;choroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;optic nerve;endometrium;bone;testis;brain;amygdala;unclassifiable (Anatomical System);heart;cerebellum cortex;islets of Langerhans;blood;lens;skeletal muscle;lung;placenta;macula lutea;kidney;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.18110 0.10274 -0.271755481 34.31823543 576.88725 4.86981 TM6SF2 1.93541173325793e-05 0.700267375102094 0.299713270780573 transmembrane 6 superfamily member 2 FUNCTION: Regulator of liver fat metabolism influencing triglyceride secretion and hepatic lipid droplet content (PubMed:24531328, PubMed:24927523). May function as sterol isomerase (PubMed:25566323). {ECO:0000269|PubMed:24531328, ECO:0000269|PubMed:24927523, ECO:0000303|PubMed:25566323}.; . TISSUE SPECIFICITY: Substantial expression in liver and intestine, whereas all other tissues analyzed show low levels. {ECO:0000269|PubMed:25566323}.; unclassifiable (Anatomical System); . 0.05749 . 0.374860183 75.43052607 505.61105 4.61506 TM7SF2 0.000447934141918511 0.964092177123915 0.0354598887341659 transmembrane 7 superfamily member 2 FUNCTION: Involved in the conversion of lanosterol to cholesterol. {ECO:0000269|PubMed:11784322}.; . TISSUE SPECIFICITY: Expressed in adult heart, brain, pancreas, lung, liver, skeletal muscle, kidney, ovary, prostate, and testis, but not detected in placenta, spleen, thymus, small intestine, colon (mucosal lining), or peripheral blood leukocytes. {ECO:0000269|PubMed:9878250}.; lymphoreticular;medulla oblongata;ovary;umbilical cord;colon;choroid;skin;retina;prostate;whole body;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;blood;lens;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach; adrenal gland;liver;adrenal cortex; 0.09798 . -0.380166007 27.88393489 2447.70004 9.20626 TM7SF3 0.0898995981071209 0.909728783539116 0.000371618353763449 transmembrane 7 superfamily member 3 . . TISSUE SPECIFICITY: Ubiquitous. The highest expression is in kidney.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;oesophagus;larynx;bone;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;cartilage;heart;pharynx;blood;lens;bile duct;pancreas;pia mater;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; . 0.12843 0.09525 -0.157884861 42.05590941 476.22068 4.50779 TM9SF1 0.000166484197400084 0.969694022327686 0.0301394934749141 transmembrane 9 superfamily member 1 FUNCTION: Plays an essential role in autophagy. {ECO:0000269|PubMed:19029833}.; . TISSUE SPECIFICITY: Expressed in lung, pancreas, kidney, liver, placenta, skeletal muscle, heart and brain. The amount in skeletal muscle, heart and brain were considerably lower than in the other tissues. {ECO:0000269|PubMed:9332367}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;duodenum;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;placenta;testis; 0.42403 0.13353 0.176444282 66.07100731 3772.32657 12.01773 TM9SF2 0.999928359846155 7.16401366527792e-05 1.71918612384192e-11 transmembrane 9 superfamily member 2 FUNCTION: In the intracellular compartments, may function as a channel or small molecule transporter.; . TISSUE SPECIFICITY: Ubiquitously expressed. Especially abundant in pancreas, highly expressed in kidney, lower levels in heart, brain, skeletal muscle and placenta. Lowest expression in lung and liver.; . . 0.16404 0.09378 -0.80269335 12.23755603 23.18457 0.77435 TM9SF3 0.999654187290714 0.000345811913438081 7.95847803094883e-10 transmembrane 9 superfamily member 3 . . . . . 0.46411 0.12425 -0.405853867 26.23260203 21.14918 0.71478 TM9SF4 0.999970772411386 2.92275866785224e-05 1.93585897878271e-12 transmembrane 9 superfamily protein member 4 . . . myocardium;medulla oblongata;smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;adrenal cortex;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis;trigeminal ganglion;skeletal muscle;parietal lobe; 0.27945 0.11262 -0.514264485 21.41424864 53.66935 1.45942 TMA7 0.0100073079474151 0.603670279587568 0.386322412465017 translation machinery associated 7 homolog . . TISSUE SPECIFICITY: Expressed in dermal papilla cells with aggregative behavior. {ECO:0000269|PubMed:16096800}.; . . . . 0.057118534 57.99716914 2.39611 0.08159 TMA16 0.0294700244557601 0.923796252832206 0.0467337227120345 translation machinery associated 16 homolog . . . . . . 0.10118 0.703746784 85.42108988 . . TMA16P1 . . . translation machinery associated 16 homolog pseudogene 1 . . . . . . . . . . . TMA16P2 . . . translation machinery associated 16 homolog pseudogene 2 . . . . . . . . . . . TMBIM1 7.40053901450362e-05 0.915913369667482 0.0840126249423724 transmembrane BAX inhibitor motif containing 1 FUNCTION: Negatively regulates aortic matrix metalloproteinase-9 (MMP9) production and may play a protective role in vascular remodeling.; . . ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;spinal cord;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta; lung;placenta;ciliary ganglion; 0.21069 0.11423 0.040529541 57.15380986 1448.82412 7.10172 TMBIM4 0.0020799620820819 0.745545085254773 0.252374952663145 transmembrane BAX inhibitor motif containing 4 FUNCTION: Anti-apoptotic protein which can inhibit apoptosis induced by intrinsic and extrinsic apoptotic stimuli. Can modulate both capacitative Ca2+ entry and inositol 1,4,5-trisphosphate (IP3)-mediated Ca2+ release. {ECO:0000269|PubMed:17319741, ECO:0000269|PubMed:19553469}.; . . ovary;umbilical cord;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;islets of Langerhans;oral cavity;blood;lens;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10491 0.12293 0.237127192 68.98443029 2153.23774 8.54050 TMBIM6 0.0161697441134311 0.959289241995359 0.0245410138912095 transmembrane BAX inhibitor motif containing 6 FUNCTION: Suppressor of apoptosis. Modulates unfolded protein response signaling. Modulate ER calcium homeostasis by acting as a calcium-leak channel. {ECO:0000269|PubMed:21075086, ECO:0000269|PubMed:22128171}.; . TISSUE SPECIFICITY: Highly abundant in testis.; ovary;skin;bone marrow;prostate;thyroid;bladder;brain;tonsil;heart;spinal cord;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;cerebral cortex;bone;testis;dura mater;spinal ganglion;artery;unclassifiable (Anatomical System);meninges;lymph node;small intestine;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;pia mater;mesenchyma;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; superior cervical ganglion;medulla oblongata;occipital lobe;testis - interstitial;olfactory bulb;fetal thyroid;bone marrow;fetal liver;testis - seminiferous tubule;placenta;liver;testis;kidney;parietal lobe;cingulate cortex; 0.09972 0.13992 -0.251530012 35.42108988 61.1273 1.59193 TMBIM7P . . . transmembrane BAX inhibitor motif containing 7, pseudogene . . . . . . . . . . . TMC1 3.80770445106551e-07 0.999435420722983 0.000564198506571519 transmembrane channel like 1 FUNCTION: Probable ion channel required for the normal function of cochlear hair cells. {ECO:0000250}.; DISEASE: Deafness, autosomal recessive, 7 (DFNB7) [MIM:600974]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:11850618}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in fetal cochlea, and at low levels in placenta and testis.; . . 0.11676 0.17087 -0.641086234 16.6784619 3042.66182 10.48286 TMC2 7.88651863410026e-16 0.20314365256717 0.796856347432829 transmembrane channel like 2 FUNCTION: Probable ion channel required for the normal function of cochlear hair cells. {ECO:0000269|PubMed:11850618}.; . TISSUE SPECIFICITY: Detected in fetal cochlea.; unclassifiable (Anatomical System); superior cervical ganglion;atrioventricular node; 0.05612 0.10450 0.297596326 71.67964142 1085.66273 6.31408 TMC3 9.78337319544272e-16 0.396541991633446 0.603458008366553 transmembrane channel like 3 FUNCTION: Probable ion channel. {ECO:0000250}.; . . unclassifiable (Anatomical System);nasopharynx;skin; . 0.05595 0.12437 1.478915028 95.29370134 1882.26477 7.98006 TMC3-AS1 . . . TMC3 antisense RNA 1 . . . . . . . . . . . TMC4 9.28942949249665e-09 0.730922925891218 0.269077064819353 transmembrane channel like 4 FUNCTION: Probable ion channel. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;bone marrow;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;testis;unclassifiable (Anatomical System);hypothalamus;urinary;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion; 0.02334 0.08685 0.668743049 84.68388771 3189.12864 10.76216 TMC5 0.000196303180727183 0.999760736862148 4.29599571246376e-05 transmembrane channel like 5 FUNCTION: Probable ion channel. {ECO:0000250}.; . . unclassifiable (Anatomical System);colon;breast;pancreas;prostate;lung;endometrium;nasopharynx;placenta;hypopharynx;testis;head and neck;stomach; prostate;trachea;trigeminal ganglion; 0.08155 0.08596 0.786269343 87.29063458 499.01364 4.58688 TMC6 5.0774933274282e-08 0.838066537766711 0.161933411458356 transmembrane channel like 6 FUNCTION: Probable ion channel. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in placenta, prostate, testis, activated T-lymphocytes and lymphokine-activated killer (LAK) lymphocytes. {ECO:0000269|PubMed:12906855, ECO:0000269|Ref.3}.; ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;hypothalamus;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;stomach;thymus; globus pallidus;pons; 0.17431 0.14008 0.497836815 79.65911772 4133.48394 12.75965 TMC7 4.32157674955598e-06 0.98994480301212 0.0100508754111302 transmembrane channel like 7 FUNCTION: Probable ion channel. {ECO:0000250}.; . . unclassifiable (Anatomical System);breast;lung;ovary;endometrium;hypothalamus;placenta;hippocampus;testis;kidney;spinal ganglion;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.14515 0.10112 0.492370491 79.60603916 944.05215 5.95318 TMC8 5.57197204809154e-12 0.107886357282577 0.892113642711851 transmembrane channel like 8 FUNCTION: Probable ion channel. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in placenta, prostate and testis. {ECO:0000269|PubMed:12906855}.; lymphoreticular;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;oesophagus;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;lung;macula lutea;liver;spleen;stomach;thymus; globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10285 0.10186 0.205769367 67.49823071 603.34019 4.97185 TMCC1 0.209385317152585 0.788710593586414 0.00190408926100131 transmembrane and coiled-coil domain family 1 . . . unclassifiable (Anatomical System);smooth muscle;heart;ovary;islets of Langerhans;colon;skin;skeletal muscle;retina;breast;uterus;prostate;lung;nasopharynx;placenta;pituitary gland;testis;spleen;cervix;spinal ganglion;brain;mammary gland;stomach; occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.27500 0.10958 -0.448125345 24.19202642 32.99677 1.02143 TMCC1-AS1 . . . TMCC1 antisense RNA 1 (head to head) . . . . . . . . . . . TMCC1P1 . . . transmembrane and coiled-coil domain family 1 pseudogene 1 . . . . . . . . . . . TMCC2 0.288835546910598 0.706627655073198 0.00453679801620482 transmembrane and coiled-coil domain family 2 . . . unclassifiable (Anatomical System);amygdala;lymph node;urinary;choroid;fovea centralis;lens;skin;retina;uterus;pancreas;lung;whole body;optic nerve;cochlea;visual apparatus;macula lutea;liver;testis;spleen;mammary gland;brain;stomach;cerebellum; fetal liver;bone marrow; 0.24512 0.11065 -1.063626766 7.484076433 386.00355 4.13723 TMCC3 0.000392184014749242 0.845537035544759 0.154070780440491 transmembrane and coiled-coil domain family 3 . . . unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;adrenal cortex;colon;skin;skeletal muscle;breast;uterus;pancreas;prostate;lung;adrenal gland;nasopharynx;placenta;hippocampus;liver;testis;head and neck;spleen;kidney;brain;mammary gland; . 0.09620 0.10967 0.178263593 66.12998349 211.70761 3.13738 TMCO1 9.55325778347458e-07 0.530626517370879 0.469372527303343 transmembrane and coiled-coil domains 1 . . TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues, with higher levels in thymus, prostate, testis and small intestine and lower levels in brain, placenta, lung and kidney. {ECO:0000269|PubMed:10393320, ECO:0000269|PubMed:20018682}.; . . 0.21693 0.11262 0.057118534 57.99716914 266.50685 3.50211 TMCO2 0.03971131287527 0.840669392840125 0.119619294284605 transmembrane and coiled-coil domains 2 . . . . . 0.33425 . 0.369407109 74.95281906 40.73725 1.19364 TMCO3 6.68498405104448e-10 0.411660043201141 0.588339956130361 transmembrane and coiled-coil domains 3 FUNCTION: Probable Na(+)/H(+) antiporter. {ECO:0000250}.; . . . . 0.09724 0.09172 -0.10469683 45.64755839 1499.02081 7.20431 TMCO4 9.98392215947084e-13 0.143020533657537 0.856979466341465 transmembrane and coiled-coil domains 4 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;germinal center;spinal ganglion;unclassifiable (Anatomical System);cartilage;lacrimal gland;tongue;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;placenta;thyroid;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.19346 0.10174 0.45374373 78.05496579 3556.83696 11.53338 TMCO5A 0.000421006608369141 0.856136715254867 0.143442278136764 transmembrane and coiled-coil domains 5A . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; . 0.05598 0.05734 0.68351529 85.03774475 340.32215 3.91340 TMCO5B . . . transmembrane and coiled-coil domains 5B (pseudogene) . . . . . . . . . . . TMCO6 8.14596215918246e-06 0.917821732148217 0.0821701218896233 transmembrane and coiled-coil domains 6 . . . lymphoreticular;myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;atrium;whole body;bone;pituitary gland;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;spinal cord;pharynx;blood;lens;breast;bile duct;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; dorsal root ganglion;testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;testis;fetal thyroid;skin; 0.13723 0.10081 -0.047654689 50.22410946 1053.74919 6.23405 TMED1 0.000162416907640562 0.442428105192903 0.557409477899456 transmembrane p24 trafficking protein 1 FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. May act as a cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and may be involved in vesicle coat formation at the cytoplasmic side.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8621446}.; lymphoreticular;myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;cerebral cortex;endometrium;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; heart;liver; 0.27980 0.11104 -0.317668748 31.45789101 60.12224 1.57371 TMED2 0.79767958829404 0.196670580412158 0.00564983129380234 transmembrane p24 trafficking protein 2 FUNCTION: Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway but also in post-Golgi membranes. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED10 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1. In COPI vesicle-mediated retrograde transport inhibits the GTPase- activating activity of ARFGAP1 towards ARF1 thus preventing immature uncoating and allowing cargo selection to take place. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2RL1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Facilitates CASR maturation and stabilization in the early secretory pathway and increases CASR plasma membrane targeting. Proposed to be involved in organization of intracellular membranes such as the maintenance of the Golgi apparatus. May also play a role in the biosynthesis of secreted cargo such as eventual processing. {ECO:0000269|PubMed:10761932, ECO:0000269|PubMed:17693410, ECO:0000269|PubMed:20361938, ECO:0000269|PubMed:20427317, ECO:0000269|PubMed:21219331}.; . . ovary;sympathetic chain;skin;retina;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; pancreas;trachea;salivary gland;placenta;thyroid; 0.70097 0.11835 -0.119252484 44.53880632 7.09498 0.26483 TMED3 0.00265674208825899 0.791742157486209 0.205601100425532 transmembrane p24 trafficking protein 3 FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network. {ECO:0000269|PubMed:10852829}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;placenta;hippocampus;kidney;aorta;stomach;cerebellum; superior cervical ganglion;trachea;salivary gland;thyroid;placenta;beta cell islets;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.13947 0.11804 0.150760231 64.51403633 214.90309 3.16306 TMED4 0.292927703052725 0.686586673730694 0.0204856232165809 transmembrane p24 trafficking protein 4 FUNCTION: Involved in vesicular protein trafficking, mainly in the early secretory pathway. targeting. Involved in the maintenance of the Golgi apparatus. Appears to play a role in the biosynthesis of secreted cargo including processing. Involved in endoplasmic reticulum stress response. May play a role in the regulation of heat-shock response and apoptosis (By similarity). {ECO:0000250}.; . . ovary;rectum;substantia nigra;skin;retina;bone marrow;prostate;optic nerve;cochlea;thyroid;iris;amniotic fluid;germinal center;brain;heart;cartilage;tongue;pineal body;urinary;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; superior cervical ganglion;globus pallidus;cerebellum; 0.28164 . -0.185391282 39.67916962 25.73722 0.83798 TMED5 0.00243713073785069 0.775974615436477 0.221588253825673 transmembrane p24 trafficking protein 5 FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Required for the maintenance of the Golgi apparatus; involved in protein exchange between Golgi stacks during assembly. Probably not required for COPI-vesicle- mediated retrograde transport. {ECO:0000269|PubMed:19948005}.; . . . . 0.24303 0.09726 0.082802743 60.09082331 5163.447 14.78411 TMED6 0.000563599382674353 0.706937540319601 0.292498860297724 transmembrane p24 trafficking protein 6 . . . unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;placenta;liver;colon;spleen;kidney; . 0.05211 . 0.617373774 83.25076669 102.50746 2.18854 TMED7 0.363701354530081 0.624385046620456 0.0119135988494629 transmembrane p24 trafficking protein 7 FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Appears to play a role in the biosynthesis of secreted cargo including processing and post- translational modifications.; . . . . . 0.10037 -0.009020804 52.8544468 . . TMED7-TICAM2 0.00470963741298361 0.965631732888936 0.0296586296980803 TMED7-TICAM2 readthrough FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Appears to play a role in the biosynthesis of secreted cargo including processing and post- translational modifications.; . . ovary;developmental;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;pituitary gland;testis;germinal center;brain;artery;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;tongue;lacrimal gland;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;alveolus;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach;aorta; . . . 0.21689899 68.12927577 95.0899 2.10301 TMED8 0.0843249980243263 0.87139579170198 0.0442792102736941 transmembrane p24 trafficking protein family member 8 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;liver;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.35011 . -0.095386216 46.48502005 5916.67659 15.97597 TMED9 0.159567867411613 0.824925537035199 0.0155065955531875 transmembrane p24 trafficking protein 9 FUNCTION: Appears to be involved in vesicular protein trafficking, mainly in the early secretory pathway. In COPI vesicle-mediated retrograde transport involved in the coatomer recruitment to membranes of the early secretory pathway. Increases coatomer- dependent activity of ARFGAP2. Thought to play a crucial role in the specific retention of p24 complexes in cis-Golgi membranes; specifically contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network. May be involved in organization of intracellular membranes, such as of the ER-Golgi intermediate compartment and the Golgi apparatus. Involved in ER localization of PTPN2 isoform PTPB. {ECO:0000269|PubMed:10852829, ECO:0000269|PubMed:14600267, ECO:0000269|PubMed:16595549, ECO:0000269|PubMed:18287528, ECO:0000269|PubMed:19296914}.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;amnion;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; prostate;lung;heart;placenta;liver; 0.26927 0.10752 -0.029247611 51.40363293 98.95034 2.15230 TMED10 0.718151478052545 0.278740035724086 0.00310848622336942 transmembrane p24 trafficking protein 10 FUNCTION: Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1 (By similarity). In COPI vesicle-mediated retrograde transport involved in the biogenesis of COPI vesicles and vesicle coat recruitment. On Golgi membranes, acts as primary receptor for ARF1-GDP which is involved in COPI-vesicle formation. Increases coatomer-dependent GTPase-activating activity of ARFGAP2. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2LR1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Involved in trafficking of amyloid beta A4 protein and soluble APP-beta release (independent of modulation of gamma-secretase activity). As part of the presenilin-dependent gamma-secretase complex regulates gamma-cleavages of the amyloid beta A4 protein to yield amyloid-beta 40 (Abeta40). Involved in organization of the Golgi apparatus. {ECO:0000250, ECO:0000269|PubMed:10052452, ECO:0000269|PubMed:11726511, ECO:0000269|PubMed:16641999, ECO:0000269|PubMed:17288597, ECO:0000269|PubMed:19296914, ECO:0000269|PubMed:20427317, ECO:0000269|PubMed:21219331}.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;trachea;placenta;testis; 0.61904 0.15721 0.035072054 56.2514744 4.39072 0.15967 TMED10P1 . . . transmembrane p24 trafficking protein 10 pseudogene 1 . . . . . . . . . . . TMED10P2 . . . transmembrane p24 trafficking protein 10 pseudogene 2 . . . . . . . . . . . TMED11P . . . transmembrane p24 trafficking protein 11, pseudogene . . . . . . . . . . . TMEFF1 0.551607065775263 0.447803052418338 0.000589881806399588 transmembrane protein with EGF like and two follistatin like domains 1 FUNCTION: May inhibit NODAL and BMP signaling during neural patterning (By similarity). May be a tumor suppressor in brain cancers. {ECO:0000250, ECO:0000269|PubMed:12743596}.; . TISSUE SPECIFICITY: Expressed predominantly in brain, and at lower levels in heart, placenta and skeletal muscle. Down-regulated in brain tumors as compared to control brain tissues. {ECO:0000269|PubMed:12743596}.; unclassifiable (Anatomical System);ovary;hypothalamus;colon;parathyroid;vein;skin;breast;uterus;whole body;lung;frontal lobe;placenta;visual apparatus;liver;testis;amniotic fluid;kidney;brain;aorta; dorsal root ganglion;amygdala;whole brain;medulla oblongata;occipital lobe;thalamus;superior cervical ganglion;hypothalamus;spinal cord;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; . 0.34677 -0.449946534 24.00330267 17.91959 0.62642 TMEFF2 0.386319161722515 0.6132527101169 0.000428128160585175 transmembrane protein with EGF like and two follistatin like domains 2 FUNCTION: May be a survival factor for hippocampal and mesencephalic neurons. The shedded form up-regulates cancer cell proliferation, probably by promoting ERK1/2 phosphorylation. {ECO:0000269|PubMed:10903839, ECO:0000269|PubMed:17942404}.; . TISSUE SPECIFICITY: Highly expressed in adult and fetal brain, spinal cord and prostate. Expressed in all brain regions except the pituitary gland, with highest levels in amygdala and corpus callosum. Expressed in the pericryptal myofibroblasts and other stromal cells of normal colonic mucosa. Expressed in prostate carcinoma. Down-regulated in colorectal cancer. Present in Alzheimer disease plaques (at protein level). Isoform 3 is expressed weakly in testis and at high levels in normal and cancerous prostate. {ECO:0000269|PubMed:10903839, ECO:0000269|PubMed:10987305, ECO:0000269|PubMed:11120884, ECO:0000269|PubMed:11668495, ECO:0000269|PubMed:16439095, ECO:0000269|PubMed:16805794}.; unclassifiable (Anatomical System);heart;ovary;hypothalamus;sympathetic chain;parathyroid;skin;retina;uterus;breast;prostate;whole body;lung;endometrium;bone;placenta;hippocampus;duodenum;testis;brain; dorsal root ganglion;whole brain;amygdala;medulla oblongata;occipital lobe;subthalamic nucleus;superior cervical ganglion;hypothalamus;prefrontal cortex;pons;cingulate cortex;parietal lobe; 0.36998 0.26214 -0.139478553 43.29440906 116.63956 2.34915 TMEM2 1.28387737688986e-09 0.99986259407415 0.000137404641972348 transmembrane protein 2 FUNCTION: May be required for the heart morphogenesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10767548}.; . . 0.07506 0.13257 -0.472233057 22.84147205 5982.23661 16.11897 TMEM5 1.85422958050936e-06 0.674765422155015 0.325232723615405 transmembrane protein 5 FUNCTION: Involved in the biosynthesis of the phosphorylated O- mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N- acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. {ECO:0000269|PubMed:25279699}.; DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A10 (MDDGA10) [MIM:615041]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with cobblestone lissencephaly and other brain anomalies, eye malformations, profound mental retardation, and death usually in the first years of life. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease. {ECO:0000269|PubMed:23217329, ECO:0000269|PubMed:23519211}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.09345 0.08559 0.218717575 68.27081859 504.62013 4.60992 TMEM5-AS1 . . . TMEM5 antisense RNA 1 . . . . . . . . . . . TMEM8A 0.000118507458791397 0.989445686761374 0.0104358057798341 transmembrane protein 8A FUNCTION: May be a cell surface adhesion molecule. May be involved in the maintenance of the resting T-cell state.; . TISSUE SPECIFICITY: Expressed in pancreas, placenta, spleen, liver, kidney, bone marrow, peripheral blood leukocytes and tonsil. {ECO:0000269|PubMed:11006113}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);heart;cartilage;muscle;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;heart;placenta;testis; 0.17400 0.10344 0.124866463 62.3967917 647.26581 5.10719 TMEM8B 0.00130768857902563 0.961322134895652 0.037370176525322 transmembrane protein 8B FUNCTION: May function as a regulator of the EGFR pathway. Probable tumor suppressor which may function in cell growth, proliferation and adhesion. {ECO:0000269|PubMed:15498789, ECO:0000269|PubMed:15723283, ECO:0000269|PubMed:17270023, ECO:0000269|PubMed:17641538}.; . . . . 0.06160 0.10563 -0.26629572 34.81953291 134.22093 2.51871 TMEM8C 0.00216915928417017 0.753779140830697 0.244051699885132 transmembrane protein 8C FUNCTION: Myoblast-specific protein that mediates myoblast fusion, an essential step for the formation of multi-nucleated muscle fibers. Actively participates in the membrane fusion reaction (By similarity). {ECO:0000250}.; . . . . . . -0.293801652 32.93819297 26.24548 0.85038 TMEM9 0.298539881699223 0.681857947968254 0.0196021703325236 transmembrane protein 9 FUNCTION: May be involved in intracellular transport.; . TISSUE SPECIFICITY: Highly expressed in adrenal gland, thyroid gland, testis, ovary and prostate. Moderate expression in trachea, spinal cord, stomach, colon, small intestine and spleen. Low expression in bone marrow, lymph node, thymus and peripheral blood lymphocytes. Expression was detected in hematopoietic cell lines including those of myeloid, erythroid, B- and T-cell origin. {ECO:0000269|PubMed:12359240}.; . . 0.31971 0.11262 -0.119252484 44.53880632 9.27199 0.33934 TMEM9B 0.911174542861045 0.0881642669172263 0.000661190221729115 TMEM9 domain family member B FUNCTION: Enhances production of proinflammatory cytokines induced by TNF, IL1B, and TLR ligands. Has a role in TNF activation of both the NF-kappaB and MAPK pathways. {ECO:0000269|PubMed:18541524}.; . . lymphoreticular;myocardium;ovary;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; parietal lobe; 0.11461 0.06532 -0.185391282 39.67916962 11.36104 0.40929 TMEM9B-AS1 . . . TMEM9B antisense RNA 1 . . . . . . . . . . . TMEM11 0.784308456403819 0.208980347704677 0.00671119589150387 transmembrane protein 11 FUNCTION: Plays a role in mitochondrial morphogenesis. {ECO:0000269|PubMed:21274005}.; . . ovary;sympathetic chain;colon;parathyroid;choroid;skin;uterus;prostate;whole body;endometrium;bone;thyroid;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion; 0.26942 0.11501 -0.207437529 38.2814343 7.54992 0.28020 TMEM14A 0.121253231019811 0.779671466054872 0.0990753029253167 transmembrane protein 14A . . . ovary;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;pituitary gland;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;spinal cord;muscle;adrenal cortex;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; amygdala;whole brain;occipital lobe;subthalamic nucleus;pons;cingulate cortex; 0.10636 0.11931 0.03689118 56.64071715 17.29871 0.60799 TMEM14B 6.47506816571318e-07 0.0778054177411326 0.922193934752051 transmembrane protein 14B . . . . . . 0.07094 -0.073340031 48.11866006 72.00791 1.76647 TMEM14C 0.121418783802206 0.779693126885568 0.0988880893122256 transmembrane protein 14C FUNCTION: Required for normal heme biosynthesis. {ECO:0000250}.; . . ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;gum;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;pineal body;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;kidney;stomach;aorta; . 0.12821 0.11303 0.125076652 62.7388535 35.80815 1.07685 TMEM14DP . . . transmembrane protein 14D, pseudogene . . . . . . . . . . . TMEM14EP . . . transmembrane protein 14E, pseudogene . . . . . . . 0.279402865 70.86577023 . . TMEM17 0.00402396190447031 0.649887855990809 0.346088182104721 transmembrane protein 17 FUNCTION: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;frontal lobe;endometrium;tongue;islets of Langerhans;hypothalamus;head and neck; superior cervical ganglion;trigeminal ganglion; 0.25667 . 0.305084559 72.22811984 1530.47581 7.26895 TMEM18 0.0536351493645142 0.863445764179976 0.0829190864555101 transmembrane protein 18 FUNCTION: Transcription repressor. Sequence-specific ssDNA and dsDNA binding protein, with preference for GCT end CTG repeats. Cell migration modulator which enhances the glioma-specific migration ability of neural stem cells (NSC) and neural precursor cells (NPC). {ECO:0000269|PubMed:18559506, ECO:0000269|PubMed:21980424}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;synovium;thyroid;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14947 0.11169 0.193034296 66.82000472 17.01178 0.59906 TMEM19 0.0013806937133801 0.866114692913845 0.132504613372775 transmembrane protein 19 . . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.07970 0.11040 0.350995466 74.37485256 257.67543 3.45315 TMEM25 0.00042136891544107 0.856262239529037 0.143316391555522 transmembrane protein 25 . . . medulla oblongata;ovary;fovea centralis;choroid;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;lacrimal gland;islets of Langerhans;lens;lung;placenta;macula lutea;hippocampus;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; subthalamic nucleus;globus pallidus;atrioventricular node;trigeminal ganglion; 0.17306 0.11261 0.198490371 67.30360934 4767.64725 13.98673 TMEM26 1.73428388598308e-07 0.23693078867354 0.763069037898071 transmembrane protein 26 . . . medulla oblongata;visual apparatus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.22844 . -0.758599262 13.32861524 25.95677 0.84364 TMEM26-AS1 . . . TMEM26 antisense RNA 1 . . . . . . . . . . . TMEM27 0.00310804463799565 0.594025778370487 0.402866176991517 transmembrane protein 27 FUNCTION: Regulator of SNARE complex function. Stimulator of beta cell replication. {ECO:0000269|PubMed:16330323}.; . TISSUE SPECIFICITY: Kidney; collecting ducts. Pancreas; beta cells of islets. {ECO:0000269|PubMed:11278314, ECO:0000269|PubMed:16330323}.; . . 0.87007 0.10882 -0.185391282 39.67916962 11.80799 0.42787 TMEM30A 0.04068308491811 0.952897894778115 0.00641902030377484 transmembrane protein 30A FUNCTION: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet- activating factor (PAF), synthetic drug alkylphospholipid edelfosine, and, probably in association with ATP8B1, of perifosine. Also mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from the ER to other membrane localizations. {ECO:0000269|PubMed:20510206, ECO:0000269|PubMed:20947505, ECO:0000269|PubMed:20961850, ECO:0000269|PubMed:21289302}.; . . smooth muscle;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;hypopharynx;liver;head and neck;kidney;mammary gland;aorta;stomach;cerebellum;thymus; . 0.21060 0.13393 -0.271755481 34.31823543 18.76838 0.64828 TMEM30B 0.0211817301247061 0.753165423878392 0.225652845996902 transmembrane protein 30B FUNCTION: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate (Probable). Can mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2 and ATP8B4 from the ER to the plasma membrane. {ECO:0000269|PubMed:20961850, ECO:0000305}.; . . ovary;sympathetic chain;colon;parathyroid;bone marrow;prostate;cochlea;oesophagus;endometrium;synovium;thyroid;pituitary gland;testis;amniotic fluid;brain;bladder;pineal gland;gall bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;adrenal cortex;pancreas;lung;adrenal gland;placenta;liver;kidney;mammary gland;stomach; superior cervical ganglion;trachea;thyroid;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;pituitary;skeletal muscle; 0.12689 0.13376 . . 341.69709 3.91996 TMEM30C . . . transmembrane protein 30C . . TISSUE SPECIFICITY: Specifically expressed in testis. {ECO:0000269|PubMed:17258408}.; . . . . . . 6.21452 0.23426 TMEM31 0.000256765988767014 0.325244488572326 0.674498745438907 transmembrane protein 31 . . . unclassifiable (Anatomical System);placenta;liver;testis;spleen; . 0.11552 . 0.413500896 76.67492333 18.55353 0.64209 TMEM33 0.229168918276829 0.763201203967729 0.0076298777554427 transmembrane protein 33 . . . smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;pituitary gland;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.22877 0.14229 -0.317668748 31.45789101 17.04533 0.59982 TMEM35 0.648723791041668 0.325365550228345 0.0259106587299871 transmembrane protein 35 FUNCTION: A soluble peptide released by shedding may interact with NGFR and modulate neurite outgrowth. {ECO:0000250}.; . . . . 0.57480 . 0.013025609 54.62962963 2.35963 0.08023 TMEM37 0.0418161454815406 0.657034914434163 0.301148940084297 transmembrane protein 37 FUNCTION: Thought to stabilize the calcium channel in an inactivated (closed) state. Modulates calcium current when coexpressed with CACNA1G (By similarity). {ECO:0000250|UniProtKB:Q9JJV3}.; . . uterus;medulla oblongata;pancreas;lung;islets of Langerhans;iris;liver;colon;parathyroid;spleen;kidney;stomach;retina; . 0.12136 0.27707 0.194852702 67.03231894 188.30744 2.97976 TMEM38A 0.0307601657795331 0.925138825226884 0.044101008993583 transmembrane protein 38A FUNCTION: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores (By similarity). {ECO:0000250}.; . . lymphoreticular;heart;pineal body;muscle;skeletal muscle;bone marrow;breast;optic nerve;lung;larynx;thyroid;visual apparatus;hippocampus;head and neck;brain; . 0.20873 0.11074 -0.358119787 29.16371786 53.85163 1.46315 TMEM38B 0.1687999661801 0.817219767891186 0.0139802659287145 transmembrane protein 38B FUNCTION: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores (By similarity). {ECO:0000250}.; DISEASE: Osteogenesis imperfecta 14 (OI14) [MIM:615066]: An autosomal recessive form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI14 is characterized by variable degrees of severity of multiple fractures and osteopenia, with normal teeth, sclerae, and hearing. Fractures first occur prenatally or by age 6 years. {ECO:0000269|PubMed:23054245, ECO:0000269|PubMed:23316006}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.19944 0.10849 0.218717575 68.27081859 25.79881 0.83959 TMEM39A 0.979617998375633 0.0203785992803239 3.40234404278143e-06 transmembrane protein 39A . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;stomach; . 0.15804 . -0.159704656 41.90846898 777.07163 5.51831 TMEM39B 0.021450432147613 0.962077818165153 0.0164717496872344 transmembrane protein 39B . . . medulla oblongata;ovary;colon;parathyroid;vein;skin;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;adrenal cortex;pharynx;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;mammary gland;stomach; superior cervical ganglion;medulla oblongata;testis;trigeminal ganglion;skeletal muscle; 0.59241 0.11734 -0.824740496 11.67728238 22.23496 0.74578 TMEM40 0.000135844028608561 0.85363799860783 0.146226157363561 transmembrane protein 40 . . . unclassifiable (Anatomical System);lymph node;heart;ovary;parathyroid;blood;skin;bone marrow;uterus;lung;gum;nasopharynx;thyroid;placenta;liver;testis;spleen;brain; dorsal root ganglion;superior cervical ganglion;placenta;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.17338 0.09838 -0.071520315 48.34866714 918.29718 5.89152 TMEM41A 0.00224660859113542 0.760567190138125 0.237186201270739 transmembrane protein 41A . . . unclassifiable (Anatomical System);lymphoreticular;ovary;urinary;adrenal cortex;colon;skeletal muscle;pancreas;prostate;lung;cochlea;oesophagus;endometrium;adrenal gland;placenta;hippocampus;liver;testis;ciliary body; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.16536 0.10775 0.659651797 84.35362114 90.49929 2.04751 TMEM41B 0.0201899312153953 0.90359085943746 0.0762192093471449 transmembrane protein 41B FUNCTION: Required for normal motor neuron development. {ECO:0000250}.; . . medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;duodenum;kidney;stomach;thymus; dorsal root ganglion;occipital lobe;superior cervical ganglion;medulla oblongata;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex; 0.30503 0.09062 0.193034296 66.82000472 357.96342 4.00903 TMEM42 0.306977503268514 0.619374574470953 0.0736479222605327 transmembrane protein 42 . . . ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;lens;skeletal muscle;lung;placenta;macula lutea;liver;cervix;spleen;kidney;mammary gland; . 0.24023 . . . 14.86174 0.53479 TMEM43 9.84762662149707e-08 0.520693071272873 0.479306830250861 transmembrane protein 43 FUNCTION: May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (By similarity). {ECO:0000250}.; DISEASE: Emery-Dreifuss muscular dystrophy 7, autosomal dominant (EDMD7) [MIM:614302]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:21391237}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest expression in placenta. Also found at lower levels in heart, ovary, spleen, small intestine, thymus, prostate and testis. {ECO:0000269|PubMed:18230648}.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; dorsal root ganglion;placenta;ciliary ganglion; 0.12225 0.11239 0.600782551 82.82613824 6718.71543 17.37441 TMEM44 1.19424157266321e-06 0.357338346606078 0.642660459152349 transmembrane protein 44 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;lacrimal gland;lens;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;kidney;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; . 0.09329 1.778477122 96.83887709 4070.99924 12.65609 TMEM44-AS1 . . . TMEM44 antisense RNA 1 . . . . . . . . . . . TMEM45A 0.0101836251559842 0.943981968731858 0.0458344061121575 transmembrane protein 45A . . . unclassifiable (Anatomical System);heart;islets of Langerhans;adrenal cortex;colon;skin;bone marrow;breast;uterus;pancreas;lung;cochlea;endometrium;nasopharynx;placenta;visual apparatus;hypopharynx;cervix;head and neck;spleen;brain;artery;aorta;tonsil; superior cervical ganglion;adipose tissue;placenta;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.13505 0.09019 -0.161524709 41.6430762 11.70915 0.42518 TMEM45B 8.86544079040378e-07 0.172578471004831 0.82742064245109 transmembrane protein 45B . . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;bone;brain;gall bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lung;cornea;nasopharynx;placenta;visual apparatus;liver;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.12082 . 0.551232944 81.48148148 50.23611 1.39250 TMEM47 0.6410239240686 0.331408879084504 0.0275671968468961 transmembrane protein 47 . . . smooth muscle;ovary;colon;parathyroid;skin;retina;uterus;prostate;atrium;whole body;frontal lobe;cochlea;endometrium;thyroid;bone;testis;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;small intestine;heart;spinal cord;pancreas;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; amygdala;superior cervical ganglion;occipital lobe;thalamus;hypothalamus;spinal cord;prefrontal cortex;caudate nucleus; 0.40386 0.11262 -0.009020804 52.8544468 2.71452 0.09768 TMEM50A 0.333486481175581 0.651545319263015 0.0149681995614041 transmembrane protein 50A . . . . . 0.34196 0.10081 0.169169615 65.33380514 45.99018 1.30556 TMEM50B 0.298982340705241 0.681483296529853 0.0195343627649061 transmembrane protein 50B . . . . . 0.17312 . 0.147123112 64.11299835 11.56125 0.41833 TMEM51 0.870759443080077 0.127507001158588 0.0017335557613353 transmembrane protein 51 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;iris;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;lens;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.17186 0.10916 -0.337894035 30.37272942 50.5712 1.39955 TMEM51-AS1 . . . TMEM51 antisense RNA 1 . . . . . 0.05375 . . . . . TMEM52 0.328693114330909 0.607594299617239 0.063712586051852 transmembrane protein 52 . . . unclassifiable (Anatomical System);medulla oblongata;pancreas;lung;whole body;islets of Langerhans;muscle;testis;colon;spleen;kidney;skeletal muscle;stomach; . 0.08323 . 0.104848986 61.49445624 6319.18345 16.62936 TMEM52B 0.0401804982967945 0.841811151325711 0.118008350377494 transmembrane protein 52B . . . . . 0.28404 . 0.349177632 74.18023119 41.07544 1.20359 TMEM53 0.0389751684862776 0.838809410917639 0.122215420596083 transmembrane protein 53 . . . . . 0.79533 . 0.130533008 63.35810333 71.7912 1.76413 TMEM54 0.164454120579217 0.772922746448167 0.0626231329726162 transmembrane protein 54 . . TISSUE SPECIFICITY: Ubiquitously expressed in cancer cell lines. {ECO:0000269|PubMed:11394883}.; colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;muscle;blood;lens;pancreas;lung;placenta;macula lutea;hippocampus;kidney;mammary gland;stomach; . 0.25618 0.13131 0.062575634 58.74026893 137.44598 2.55015 TMEM55A 0.0219903647102958 0.962114004760436 0.0158956305292683 transmembrane protein 55A FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 4,5-bisphosphate. Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4- bisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3- monophosphate. {ECO:0000269|PubMed:16365287}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16365287}.; colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;brain;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;hypothalamus;adrenal cortex;lens;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;aorta;cerebellum;thymus; . 0.42448 0.12581 0.03689118 56.64071715 39.68901 1.16945 TMEM55B 0.800399509827653 0.199362544935983 0.000237945236363859 transmembrane protein 55B FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 4,5-bisphosphate. Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4- bisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3- monophosphate. {ECO:0000269|PubMed:16365287}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16365287}.; ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;adrenal cortex;blood;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; . 0.33022 0.12971 -0.273576253 33.97027601 26.67292 0.86310 TMEM56 0.338393703132694 0.647186481482088 0.0144198153852179 transmembrane protein 56 . . . . . 0.00755 . -0.09720619 46.20193442 8.4796 0.31110 TMEM56-RWDD3 . . . TMEM56-RWDD3 readthrough . . . . . . . . . 3.85105 0.14174 TMEM57 0.992504411290221 0.00749552959931874 5.9110460677733e-08 transmembrane protein 57 . . . . . 0.79724 0.12388 -0.626318434 17.03231894 11.16568 0.40344 TMEM59 2.23025067852854e-07 0.269863764996775 0.730136011978157 transmembrane protein 59 FUNCTION: Acts as a regulator of autophagy in response to S.aureus infection by promoting activation of LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C). Acts by interacting with ATG16L1, leading to promote a functional complex between LC3 and ATG16L1 and promoting LC3 lipidation and subsequent activation of autophagy. Modulates the O-glycosylation and complex N-glycosylation steps occurring during the Golgi maturation of several proteins such as APP, BACE1, SEAP or PRNP. Inhibits APP transport to the cell surface and further shedding. {ECO:0000269|PubMed:20427278, ECO:0000269|PubMed:23376921}.; . . myocardium;ovary;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;adrenal cortex;lens;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;duodenum;liver;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; prostate;trachea;placenta;spinal cord;kidney; 0.78227 0.12249 -0.249709319 35.74545883 71.33715 1.75747 TMEM59L 0.0151007864967939 0.957919915799743 0.026979297703463 transmembrane protein 59 like FUNCTION: Modulates the O-glycosylation and complex N- glycosylation steps occurring during the Golgi maturation of APP. Inhibits APP transport to the cell surface and further shedding. {ECO:0000269|PubMed:20427278}.; . TISSUE SPECIFICITY: Expressed preferentially at high level in the brain.; unclassifiable (Anatomical System);amygdala;islets of Langerhans;salivary gland;hypothalamus;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;frontal lobe;synovium;macula lutea;hippocampus;testis;spleen;brain; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.23488 0.11113 0.393270925 76.04977589 73.02849 1.78384 TMEM60 0.661431575510107 0.31523765563895 0.0233307688509431 transmembrane protein 60 . . . ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;larynx;bone;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;lymph node;heart;cartilage;cerebellum cortex;islets of Langerhans;muscle;pia mater;lung;placenta;macula lutea;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach; . 0.27167 0.09976 0.21326276 67.71644256 6.01727 0.22676 TMEM61 0.00437577280284652 0.667785387911909 0.327838839285244 transmembrane protein 61 . . . . . 0.07687 . 0.240763792 69.36777542 311.53503 3.75661 TMEM62 5.98675580191077e-08 0.654311115659743 0.345688824472699 transmembrane protein 62 . . . unclassifiable (Anatomical System);ovary;lacrimal gland;islets of Langerhans;colon;parathyroid;blood;retina;bone marrow;breast;uterus;pancreas;prostate;lung;endometrium;bone;placenta;liver;testis;cervix;germinal center;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05360 0.09134 -0.80269335 12.23755603 48.42153 1.35685 TMEM63A 6.10813887296527e-05 0.998806637656999 0.00113228095427175 transmembrane protein 63A FUNCTION: Acts as an osmosensitive calcium-permeable cation channel. {ECO:0000250}.; . . . . 0.07297 . 0.584200036 82.336636 2871.4616 10.14633 TMEM63B 0.999844992461849 0.000155007533537468 4.61358561487887e-12 transmembrane protein 63B FUNCTION: Acts as an osmosensitive calcium-permeable cation channel. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;thyroid;bone;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;tongue;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.28285 . -1.109541557 6.782259967 1061.68006 6.25181 TMEM63C 0.988496791803572 0.0115031740472486 3.41491793656291e-08 transmembrane protein 63C FUNCTION: Acts as an osmosensitive calcium-permeable cation channel. {ECO:0000269|PubMed:24503647}.; . . islets of Langerhans;colon;fovea centralis;choroid;lens;retina;optic nerve;lung;endometrium;macula lutea;testis;kidney;mammary gland;brain;aorta;cerebellum; medulla oblongata;trigeminal ganglion;parietal lobe;cerebellum; 0.23205 . -0.707227564 14.71455532 68.68826 1.71607 TMEM64 0.157412876273051 0.775384535228327 0.0672025884986212 transmembrane protein 64 . . . . . 0.13132 0.10577 -0.229483771 36.86010852 97.01614 2.12831 TMEM65 0.594652549330275 0.395773990530486 0.00957346013923891 transmembrane protein 65 FUNCTION: Plays an important role in cardiac development and function. Regulates cardiac conduction and the function of the gap junction protein GJA1. Contributes to the stability and proper localization of GJA1 to cardiac intercalated disk thereby regulating gap junction communication. {ECO:0000250|UniProtKB:Q4VAE3}.; . TISSUE SPECIFICITY: Predominantly expressed the ventricular tissue (at protein level). {ECO:0000269|PubMed:26403541}.; unclassifiable (Anatomical System);heart;ovary;tongue;islets of Langerhans;colon;skin;skeletal muscle;uterus;prostate;lung;frontal lobe;placenta;visual apparatus;liver;testis;head and neck;kidney;brain;peripheral nerve; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19948 . -0.031067188 51.03798066 8.1252 0.29847 TMEM67 1.21202254456235e-17 0.407724039388368 0.592275960611632 transmembrane protein 67 FUNCTION: Required for ciliary structure and function. Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition (By similarity). Involved in centrosome migration to the apical cell surface during early ciliogenesis. Involved in the regulation of cilia length and appropriate number through the control of centrosome duplication. Required for cell branching morphology. Essential for endoplasmic reticulum-associated degradation (ERAD) of surfactant protein C (SFTPC). {ECO:0000250, ECO:0000269|PubMed:17185389, ECO:0000269|PubMed:19515853, ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:19815549}.; DISEASE: Meckel syndrome 3 (MKS3) [MIM:607361]: A disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly. {ECO:0000269|PubMed:16415887, ECO:0000269|PubMed:19466712}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Joubert syndrome 6 (JBTS6) [MIM:610688]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. {ECO:0000269|PubMed:17160906, ECO:0000269|PubMed:19508969, ECO:0000269|PubMed:21633164}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bardet-Biedl syndrome (BBS) [MIM:209900]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:18327255}. Note=The gene represented in this entry may act as a disease modifier. TMEM67 variations may influence the expression of Bardet-Biedl syndrome in patients who have causative mutations in other genes. Heterozygosity for a complex mutation in the TMEM67 gene coding for a protein with 2 in cis changes, and homozygosity for a truncating mutation of the CEP290 gene has been found in a patient with Bardet-Biedl syndrome 14.; DISEASE: COACH syndrome (COACHS) [MIM:216360]: A disorder characterized by mental retardation, ataxia due to cerebellar hypoplasia, and hepatic fibrosis. Patients present the molar tooth sign, a midbrain-hindbrain malformation pathognomonic for Joubert syndrome and related disorders. Other features, such as coloboma and renal cysts, may be variable. {ECO:0000269|PubMed:19058225, ECO:0000269|PubMed:19574260}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Nephronophthisis 11 (NPHP11) [MIM:613550]: A disorder characterized by the association of nephronophthisis with hepatic fibrosis. Nephronophthisis is a progressive tubulo-interstitial kidney disorder histologically characterized by modifications of the tubules with thickening of the basement membrane, interstitial fibrosis and, in the advanced stages, medullary cysts. Typical clinical features are chronic renal failure, anemia, polyuria, polydipsia, isosthenuria, and growth retardation. Associations with extrarenal symptoms, especially ocular lesions, are frequent. {ECO:0000269|PubMed:19508969}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues. Expressed at higher level in spinal cord. {ECO:0000269|PubMed:16415887, ECO:0000269|PubMed:17185389}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;parathyroid;skin;skeletal muscle;bile duct;uterus;pancreas;whole body;lung;nasopharynx;bone;placenta;thyroid;testis;stomach; superior cervical ganglion; 0.05854 0.19054 0.314179756 72.75300778 129.21002 2.47805 TMEM68 0.0169369701777745 0.888831729259711 0.0942313005625146 transmembrane protein 68 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;lens;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; superior cervical ganglion;pons; 0.28732 0.11223 0.147123112 64.11299835 21.80572 0.73420 TMEM69 0.000261682873521805 0.328289998889537 0.671448318236942 transmembrane protein 69 . . . . . 0.05858 . 0.103030231 61.2762444 20.2195 0.69233 TMEM70 0.00324098348148041 0.825607326409594 0.171151690108926 transmembrane protein 70 FUNCTION: Involved in biogenesis of mitochondrial ATP synthase. {ECO:0000269|PubMed:18953340, ECO:0000269|PubMed:20937241}.; DISEASE: Mitochondrial complex V deficiency, nuclear 2 (MC5DN2) [MIM:614052]: A mitochondrial disorder with heterogeneous clinical manifestations including dysmorphic features, psychomotor retardation, hypotonia, growth retardation, cardiomyopathy, enlarged liver, hypoplastic kidneys and elevated lactate levels in urine, plasma and cerebrospinal fluid. {ECO:0000269|PubMed:18953340, ECO:0000269|PubMed:22986587}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;muscle;adrenal cortex;breast;lung;trabecular meshwork;placenta;liver;spleen;cervix;kidney;mammary gland;thymus; whole brain;skeletal muscle; 0.03740 0.05430 1.06196211 91.507431 1637.24592 7.48250 TMEM71 4.16584061056541e-10 0.0529318459840945 0.947068153599321 transmembrane protein 71 . . . unclassifiable (Anatomical System);heart;colon;blood;retina;bone marrow;lung;cochlea;oesophagus;bone;liver;kidney;aorta;stomach;thymus; . 0.06366 . 0.661468037 84.4420854 102.38545 2.18670 TMEM72 0.49453096966628 0.48499963898371 0.0204693913500101 transmembrane protein 72 . . . . . . . -0.203796826 38.81811748 209.36147 3.12414 TMEM72-AS1 . . . TMEM72 antisense RNA 1 . . . . . . . . . . . TMEM74 0.00033122585381911 0.367898724873839 0.631770049272342 transmembrane protein 74 FUNCTION: Plays an essential role in autophagy. TMEM74-induced autophagy may involve PI3K signal transduction. {ECO:0000269|PubMed:18294959, ECO:0000269|PubMed:19029833}.; . TISSUE SPECIFICITY: Expressed in heart, lung, and placenta. {ECO:0000269|PubMed:18294959}.; unclassifiable (Anatomical System);uterus;lung;frontal lobe;heart;hippocampus;testis;skin; ciliary ganglion;kidney; 0.10068 0.09910 -0.359940251 28.93371078 46.44084 1.31457 TMEM74B 0.00147382150329057 0.674382312220251 0.324143866276458 transmembrane protein 74B . . . . . 0.36323 0.10163 -0.181750739 40.15687662 30.7006 0.97671 TMEM75 . . . transmembrane protein 75 . . . . . 0.03382 . . . 16.04462 0.56757 TMEM78 . . . transmembrane protein 78 . . . . . 0.09449 . . . 1255.60773 6.68075 TMEM79 3.49884123421551e-07 0.190521051866982 0.809478598248895 transmembrane protein 79 FUNCTION: Contributes to the epidermal integrity and skin barrier function. Plays a role in the lamellar granule (LG) secretory system and in the stratum corneum (SC) epithelial cell formation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in the epidermis of the skin. Expressed in epithelial cells of the outermost layer of the stratum granulosum (SG) and hair follicles (at protein level). {ECO:0000269|PubMed:24060273, ECO:0000269|PubMed:24084074}.; unclassifiable (Anatomical System);heart;oral cavity;colon;fovea centralis;choroid;lens;skin;retina;bile duct;prostate;optic nerve;whole body;lung;frontal lobe;endometrium;mesenchyma;bone;macula lutea;cervix;brain; . 0.27924 . 0.799205007 87.58551545 579.52739 4.87936 TMEM80 4.91354767098304e-05 0.247345473288527 0.752605391234763 transmembrane protein 80 . . . . . 0.23054 . 0.349177632 74.18023119 . . TMEM81 0.000222028741737008 0.302615160505193 0.69716281075307 transmembrane protein 81 . . . . . 0.13048 . 0.705562627 85.52724699 1029.15436 6.16371 TMEM82 1.22973402675374e-05 0.375890713199281 0.624096989460452 transmembrane protein 82 . . . . . 0.19594 . 1.153790856 92.55720689 1263.85842 6.70252 TMEM86A 0.0329601379578081 0.819946680595213 0.147093181446979 transmembrane protein 86A . . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;pineal body;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; . 0.27792 0.11038 0.038710339 56.92380278 284.39875 3.61038 TMEM86B 2.76223248703721e-05 0.182244827048592 0.817727550626537 transmembrane protein 86B FUNCTION: Enzyme catalyzing the degradation of lysoplasmalogen. Lysoplasmalogens are formed by the hydrolysis of the abundant membrane glycerophospholipids plasmalogens. May control the respective levels of plasmalogens and lysoplasmalogens in cells and modulate cell membrane properties. {ECO:0000269|PubMed:21515882}.; . . unclassifiable (Anatomical System);blood;fovea centralis;choroid;lens;retina;uterus;optic nerve;lung;endometrium;placenta;bone;macula lutea;visual apparatus;liver;testis;spleen;brain;stomach;thymus; superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.08748 0.09682 0.262810045 70.43524416 28.53319 0.91405 TMEM87A 0.785702662224374 0.214296849330239 4.88445387043015e-07 transmembrane protein 87A . . . unclassifiable (Anatomical System);islets of Langerhans;colon;blood;skin;skeletal muscle;bone marrow;prostate;lung;larynx;nasopharynx;bone;thyroid;placenta;visual apparatus;duodenum;liver;head and neck;spleen;brain;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;parietal lobe; 0.35639 0.09798 -0.602450568 17.91106393 34.7616 1.05896 TMEM87B 7.97639690780215e-08 0.899434961320046 0.100564958915985 transmembrane protein 87B . . . unclassifiable (Anatomical System);ovary;small intestine;islets of Langerhans;parathyroid;blood;vein;skin;breast;bile duct;prostate;endometrium;mesenchyma;larynx;bone;placenta;liver;testis;cervix;head and neck;spleen;germinal center; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.11440 0.09798 -0.890882376 10.30313753 2755.67411 9.89860 TMEM88 0.353473968338177 0.592532020912528 0.0539940107492952 transmembrane protein 88 FUNCTION: Inhibits the Wnt/beta-catenin signaling pathway. Crucial for heart development and acts downstream of GATA factors in the pre-cardiac mesoderm to specify lineage commitment of cardiomyocyte development. {ECO:0000269|PubMed:23924634}.; . . unclassifiable (Anatomical System);heart;choroid;skeletal muscle;skin;uterus;lung;placenta;bone;visual apparatus;liver;spleen;kidney;brain; . 0.38307 . 0.948089677 89.95635763 390.15383 4.15916 TMEM88B . . . transmembrane protein 88B . . . . . . . . . 302.85142 3.70888 TMEM89 0.711075964906752 0.27398174000381 0.0149422950894384 transmembrane protein 89 . . . testis;colon;brain; superior cervical ganglion;testis - seminiferous tubule;testis; 0.06789 . 0.461228372 78.46190139 614.01798 5.00758 TMEM91 0.42210072753771 0.543924607817508 0.0339746646447817 transmembrane protein 91 . . . unclassifiable (Anatomical System);heart;colon;skin;uterus;prostate;whole body;lung;endometrium;bone;placenta;testis;kidney;brain;pineal gland;stomach; liver;ciliary ganglion;skeletal muscle; . . -0.139478553 43.29440906 104.39094 2.20917 TMEM92 0.129143042311778 0.780204642673333 0.0906523150148892 transmembrane protein 92 . . . unclassifiable (Anatomical System);lung;small intestine;bone;liver;testis;colon;kidney;gall bladder;stomach; . 0.09464 . 0.215080721 67.91696155 212.32555 3.14333 TMEM92-AS1 . . . TMEM92 antisense RNA 1 . . . . . . . . . . . TMEM94 . . . transmembrane protein 94 . . TISSUE SPECIFICITY: Expressed ubiquitously. {ECO:0000269|PubMed:8724849}.; . . 0.47515 0.13216 -2.738053399 0.684123614 . . TMEM95 0.00145964978065184 0.87360974047701 0.124930609742339 transmembrane protein 95 . . . medulla oblongata;lung;tongue;testis;head and neck; . 0.11383 . -0.161524709 41.6430762 28.90299 0.92283 TMEM97 0.0284060151690812 0.800061826494883 0.171532158336036 transmembrane protein 97 FUNCTION: Plays a role as a regulator of cellular cholesterol homeostasis (PubMed:19583955). May function as sterol isomerase (PubMed:25566323). {ECO:0000269|PubMed:19583955, ECO:0000303|PubMed:25566323}.; . TISSUE SPECIFICITY: Widely expressed in normal tissues. Expressed in pancreatic, renal, breast, colon, ovarian surface epithelial (OSE) cells and meningioma cancers. Expressed in ovarian cancer; expression is reduced relative to OSE cells. {ECO:0000269|PubMed:15375745, ECO:0000269|PubMed:18070364, ECO:0000269|PubMed:7694637}.; umbilical cord;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;urinary;pharynx;blood;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;head and neck;cervix;spleen;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;pancreas;fetal liver;testis - seminiferous tubule;adrenal gland;liver;testis;tumor;atrioventricular node;trigeminal ganglion; 0.08820 0.12543 -0.229483771 36.86010852 9.65246 0.35449 TMEM97P1 . . . transmembrane protein 97 pseudogene 1 . . . . . . . . . . . TMEM97P2 . . . transmembrane protein 97 pseudogene 2 . . . . . . . . . . . TMEM98 0.0286465401329761 0.922805808711411 0.0485476511556132 transmembrane protein 98 . . TISSUE SPECIFICITY: Expressed in the eye, particularly in corneal endothelium, iris, ciliary body, sclera, optic nerve, optic nerve head, and retina. {ECO:0000269|PubMed:24852644}.; medulla oblongata;ovary;developmental;colon;parathyroid;choroid;skin;retina;bone marrow;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;lung;nasopharynx;placenta;visual apparatus;hippocampus;duodenum;spleen;head and neck;kidney;stomach;aorta; superior cervical ganglion; 0.16574 . 0.038710339 56.92380278 75.3076 1.81577 TMEM99 3.15417716559819e-05 0.195730177051265 0.804238281177079 transmembrane protein 99 . . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;frontal lobe;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland; . 0.05041 . 0.461228372 78.46190139 966.04757 6.01306 TMEM100 0.485334011918092 0.434955787979988 0.0797102001019197 transmembrane protein 100 FUNCTION: Plays a role during embryonic arterial endothelium differentiation and vascular morphogenesis through the ACVRL1 receptor-dependent signaling pathway upon stimulation by bone morphogenetic proteins, such as GDF2/BMP9 and BMP10. Involved in the regulation of nociception, acting as a modulator of the interaction between TRPA1 and TRPV1, two molecular sensors and mediators of pain signals in dorsal root ganglia (DRG) neurons. Mechanistically, it weakens their interaction, thereby releasing the inhibition of TRPA1 by TRPV1 and increasing the single-channel open probability of the TRPA1-TRPV1 complex. {ECO:0000250|UniProtKB:Q9CQG9}.; . TISSUE SPECIFICITY: Expressed in neurons of the myenteric and submucosal plexuses in the gastric body, jejunum and proximal colon. Expressed in arterial endothelial cells and neurons of the central nervous system and peripheral nervous system. Expressed in umbilical artery endothelial cells (at protein level). {ECO:0000269|PubMed:22783020, ECO:0000269|PubMed:23485812}.; unclassifiable (Anatomical System);smooth muscle;cartilage;heart;ovary;salivary gland;parathyroid;fovea centralis;choroid;lens;retina;uterus;prostate;optic nerve;whole body;lung;placenta;macula lutea;liver;testis;spleen;brain; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.10799 0.10754 -0.119252484 44.53880632 4.23956 0.15414 TMEM101 0.161635623953233 0.773957799576196 0.0644065764705707 transmembrane protein 101 FUNCTION: May activate NF-kappa-B signaling pathways. {ECO:0000269|PubMed:12761501}.; . . myocardium;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;urinary;lens;skeletal muscle;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.28244 . -0.405853867 26.23260203 10.11873 0.36921 TMEM102 . . . transmembrane protein 102 FUNCTION: Selectively involved in CSF2 deprivation-induced apoptosis via a mitochondria-dependent pathway. {ECO:0000269|PubMed:17828305}.; . . unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;lens;pancreas;oesophagus;larynx;adrenal gland;bone;placenta;head and neck;germinal center;kidney;brain;mammary gland;stomach; superior cervical ganglion;atrioventricular node; 0.17497 0.09922 . . 320.80507 3.80540 TMEM104 2.89327933186764e-05 0.931711607866457 0.0682594593402242 transmembrane protein 104 . . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;iris;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;muscle;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18302 0.10919 0.135991087 63.61759849 208.94278 3.12004 TMEM105 0.0116196090073997 0.635316448220153 0.353063942772447 transmembrane protein 105 . . . cartilage;liver; . 0.06977 . 0.725794416 85.98136353 219.12705 3.20049 TMEM106A 0.000328022103505525 0.816692122074286 0.182979855822208 transmembrane protein 106A . . . unclassifiable (Anatomical System);lymphoreticular;medulla oblongata;heart;adrenal cortex;colon;parathyroid;blood;skin;bone marrow;uterus;prostate;lung;endometrium;adrenal gland;nasopharynx;thyroid;placenta;liver;testis;kidney;pineal gland; superior cervical ganglion; . . 0.193034296 66.82000472 51.40437 1.41490 TMEM106B 0.515078464231904 0.48109107386203 0.00383046190606626 transmembrane protein 106B FUNCTION: Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with MAP6. May act by inhibiting retrograde transport of lysosomes along dendrites. Required for dendrite branching. {ECO:0000269|PubMed:23136129, ECO:0000269|PubMed:24357581}.; DISEASE: Frontotemporal dementia and/or amyotrophic lateral sclerosis 1 (FTDALS1) [MIM:105550]: An autosomal dominant neurodegenerative disorder characterized by adult onset of frontotemporal dementia and/or amyotrophic lateral sclerosis in an affected individual. There is high intrafamilial variation. Frontotemporal dementia is characterized by frontal and temporal lobe atrophy associated with neuronal loss, gliosis, and dementia. Patients exhibit progressive changes in social, behavioral, and/or language function. Amyotrophic lateral sclerosis is characterized by the death of motor neurons in the brain, brainstem, and spinal cord, resulting in fatal paralysis. {ECO:0000269|PubMed:24385136, ECO:0000269|PubMed:24442578, ECO:0000303|PubMed:24488309}. Note=The gene represented in this entry acts as a disease modifier.; TISSUE SPECIFICITY: Expressed in frontal cortex.; . . 0.15160 0.10704 0.327131069 73.27199811 44.82615 1.28312 TMEM106C 3.96020841080124e-06 0.597672204249821 0.402323835541768 transmembrane protein 106C . . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;choroid;uterus;whole body;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hypopharynx;amnion;head and neck;kidney;stomach; superior cervical ganglion; 0.09157 0.08988 0.573279816 82.08303845 2180.48486 8.60605 TMEM107 0.0289055801710133 0.802538494910494 0.168555924918493 transmembrane protein 107 FUNCTION: Plays a role in cilia formation and embryonic patterning. Requires for normal Sonic hedgehog (Shh) signaling in the neural tube and acts in combination with GLI2 and GLI3 to pattern ventral and intermediate neuronal cell types (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;umbilical cord;pineal body;parathyroid;blood;fovea centralis;choroid;lens;retina;bone marrow;pancreas;optic nerve;lung;placenta;thyroid;macula lutea;liver;testis;stomach; superior cervical ganglion;testis;ciliary ganglion;pons;trigeminal ganglion; 0.13186 . -0.009020804 52.8544468 4.81975 0.17629 TMEM108 0.983718759593856 0.016271580055007 9.66035113663012e-06 transmembrane protein 108 . . . unclassifiable (Anatomical System);heart;colon;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;optic nerve;whole body;lung;placenta;macula lutea;visual apparatus;testis;brain; amygdala;whole brain;testis - interstitial;fetal brain;testis;fetal lung; 0.38762 . -1.39618256 4.222694032 186.62645 2.96699 TMEM108-AS1 . . . TMEM108 antisense RNA 1 . . . . . . . . . . . TMEM109 0.0518905468899636 0.927182468232184 0.0209269848778521 transmembrane protein 109 FUNCTION: May mediate cellular response to DNA damage by protecting against ultraviolet C-induced cell death (PubMed:23542032). Can form voltage-gated calcium and potassium channels in vitro (By similarity). {ECO:0000250|UniProtKB:O77751, ECO:0000269|PubMed:23542032}.; . . medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;iris;germinal center;brain;tonsil;heart;cartilage;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;ciliary ganglion;atrioventricular node; 0.12186 0.09377 -0.183570861 39.95046001 66.55961 1.68094 TMEM110 0.901349032819805 0.0984730741727751 0.000177893007419561 transmembrane protein 110 FUNCTION: Acts as a regulator of store-operated Ca(2+) entry (SOCE) at junctional sites that connect the cell membrane and endoplasmic reticulum. SOCE is a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts by interacting with STIM1, promoting STIM1 conformational switch. {ECO:0000269|PubMed:26322679}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:26322679}.; lymphoreticular;ovary;colon;parathyroid;skin;retina;uterus;thyroid;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;lung;nasopharynx;placenta;visual apparatus;liver;alveolus;spleen;kidney;mammary gland;aorta; . . . 0.193034296 66.82000472 . . TMEM110-MUSTN1 0.684628071972952 0.315188044659004 0.000183883368044328 TMEM110-MUSTN1 readthrough . . . . . . . 0.373041938 75.29488087 45.86653 1.30196 TMEM114 . . . transmembrane protein 114 . DISEASE: Note=Chromosomal aberrations involving TMEM114 may be a cause of congenital and juvenile cataracts. Translocation t(16;22) (p13.3;q11.2). {ECO:0000269|PubMed:17492639}.; . . . . . . . . . TMEM115 0.876895269487346 0.121576545434746 0.00152818507790828 transmembrane protein 115 FUNCTION: May play a role in retrograde transport of proteins from the Golgi to the endoplasmic reticulum. May indirectly play a role in protein glycosylation in the Golgi. {ECO:0000269|PubMed:24806965}.; . TISSUE SPECIFICITY: Expressed strongly in kidney and skeletal muscle, followed by liver, placenta, pancreas, and lung, with low amounts in heart and only traces in brain (PubMed:11085536). Widely expressed with ubiquitous expression in epithelial tissues (at protein level) (PubMed:17973242). {ECO:0000269|PubMed:11085536, ECO:0000269|PubMed:17973242}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;iris;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;islets of Langerhans;muscle;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;cerebellum;thymus; superior cervical ganglion;pons; 0.29907 0.12592 -0.205617011 38.57631517 21.2075 0.71635 TMEM116 1.14999091475817e-09 0.0500417451299124 0.949958253720097 transmembrane protein 116 . . . ovary;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;ganglion;bone;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;kidney;mammary gland; . 0.14160 . 0.016664174 55.21939137 464.09695 4.46351 TMEM117 3.5741678559228e-05 0.947469299961367 0.0524949583600734 transmembrane protein 117 . . . unclassifiable (Anatomical System);heart;colon;blood;lens;skin;prostate;lung;cochlea;placenta;testis;cervix;kidney;brain;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;thalamus;spinal cord;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.18072 . -0.137658575 43.57159707 328.29982 3.85151 TMEM119 0.00956737466521472 0.594093515042872 0.396339110291913 transmembrane protein 119 FUNCTION: Plays an important role in bone formation and normal bone mineralization. Promotes the differentiation of myoblasts into osteoblasts (PubMed:20025746). May induce the commitment and differentiation of myoblasts into osteoblasts through an enhancement of BMP2 production and interaction with the BMP-RUNX2 pathway. Upregulates the expression of ATF4, a transcription factor which plays a central role in osteoblast differentiation. Essential for normal spermatogenesis and late testicular differentiation (By similarity). {ECO:0000250|UniProtKB:Q8R138, ECO:0000269|PubMed:20025746}.; . TISSUE SPECIFICITY: Expressed in brain microglia (at protein level). Elevated expression levels seen in the brain of patients with Alzheimer disease. Expressed by osteoblast-like cells in bone tissues and follicular dendritic cells in lymphoid tissues. {ECO:0000269|PubMed:26250788}.; . . 0.14206 . 0.062575634 58.74026893 325.8984 3.83752 TMEM120A . . . transmembrane protein 120A FUNCTION: Necessary for efficient adipogenesis (PubMed:26024229). {ECO:0000269|PubMed:26024229}.; . . medulla oblongata;ovary;salivary gland;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;skeletal muscle;breast;pancreas;lung;hippocampus;liver;alveolus;spleen;head and neck;kidney;mammary gland;stomach; . 0.17994 0.10910 . . . . TMEM120B 0.264378756491141 0.734475990709035 0.00114525279982457 transmembrane protein 120B FUNCTION: Necessary for efficient adipogenesis. {ECO:0000250|UniProtKB:Q3TA38}.; . . unclassifiable (Anatomical System);heart;cartilage;colon;blood;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;endometrium;bone;visual apparatus;macula lutea;liver;testis;cervix;germinal center; . 0.22025 0.09033 -0.113792788 45.25831564 3548.76913 11.50188 TMEM121 0.178807336241636 0.644737244841674 0.17645541891669 transmembrane protein 121 FUNCTION: May play a role in MAPK signaling. {ECO:0000269|PubMed:15950185}.; . TISSUE SPECIFICITY: Highly expressed in heart and detected in pancreas, liver and skeletal muscle. {ECO:0000269|PubMed:15950185}.; . . 0.29685 0.13454 . . 15.74866 0.56150 TMEM123 0.605287080500358 0.385935133355238 0.00877778614440472 transmembrane protein 123 FUNCTION: Implicated in oncotic cell death, characterized by cell swelling, organelle swelling, vacuolization and increased membrane permeability. {ECO:0000269|PubMed:11481458}.; . TISSUE SPECIFICITY: Ubiquitous. Not expressed in ovary. Expressed in keratinocytes. {ECO:0000269|PubMed:11481458, ECO:0000269|PubMed:12752121}.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;uterus;whole body;oesophagus;bone;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;kidney;stomach;aorta;thymus; uterus;fetal liver;superior cervical ganglion;thyroid;tumor; 0.09182 0.07595 0.593509966 82.51356452 280.66657 3.59003 TMEM125 0.000428556113626271 0.239725847899504 0.75984559598687 transmembrane protein 125 . . . . . 0.26212 . 0.551232944 81.48148148 60.95587 1.58777 TMEM126A 0.00487417780484098 0.690495025842733 0.304630796352426 transmembrane protein 126A . . TISSUE SPECIFICITY: Strongly expressed in brain, cerebellum, skeletal muscle, testis. High expression also found in fetal brain, fetal retinal pigmentary epithelium, and fetal retina. Highly expressed in retinal ganglion cells. {ECO:0000269|PubMed:19327736, ECO:0000269|PubMed:23500070}.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;cerebellum cortex;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;kidney;stomach;aorta;thymus; testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion; 0.04208 . 0.461228372 78.46190139 68.15851 1.70816 TMEM126B 0.000531075640903117 0.45660889200691 0.542860032352187 transmembrane protein 126B FUNCTION: Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Participates in constructing the membrane arm of complex I. {ECO:0000269|PubMed:24191001}.; . . smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;lens;skeletal muscle;lung;trabecular meshwork;placenta;alveolus;kidney;mammary gland;stomach;aorta; dorsal root ganglion;whole brain;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;hypothalamus;caudate nucleus;atrioventricular node;pons;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.06517 0.07300 0.393270925 76.04977589 58.25686 1.54509 TMEM127 0.101457374227938 0.773159336979439 0.125383288792623 transmembrane protein 127 FUNCTION: Controls cell proliferation acting as a negative regulator of TOR signaling pathway mediated by mTORC1. May act as a tumor suppressor. {ECO:0000269|PubMed:20154675}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:20154675}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;synovium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;nervous;tongue;islets of Langerhans;pineal body;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;amnion;spleen;head and neck;kidney;mammary gland;aorta;stomach; whole blood; 0.08266 0.11262 -0.05129383 49.75819769 36.59829 1.09852 TMEM128 0.110058362630308 0.777021865742702 0.112919771626991 transmembrane protein 128 . . . smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;cochlea;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;adrenal cortex;lung;adrenal gland;placenta;macula lutea;liver;spleen;head and neck;kidney;aorta;thymus; testis; 0.09765 . 0.080983847 59.76055674 724.16515 5.34156 TMEM129 1.57455519983462e-06 0.0684563451989439 0.931542080245856 transmembrane protein 129 FUNCTION: E3 ubiquitin-protein ligase involved in ER-associated protein degradation, preferentially associates with the E2 enzyme UBE2J2. Exploited by viral US11 proteins to mediate HLA class I proteins degradation. {ECO:0000269|PubMed:24807418}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10745 . -0.05129383 49.75819769 500.33129 4.59135 TMEM130 1.28738785007366e-08 0.105230124408567 0.894769862717555 transmembrane protein 130 . . . unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;sympathetic chain;fovea centralis;choroid;lens;retina;optic nerve;frontal lobe;cerebral cortex;adrenal gland;macula lutea;hippocampus;pituitary gland;testis;brain; amygdala;whole brain;thalamus;medulla oblongata;occipital lobe;testis - interstitial;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;parietal lobe;cingulate cortex;pituitary;cerebellum; 0.28347 0.10519 -0.933156985 9.54824251 81.52458 1.91230 TMEM131 0.999999482162299 5.17837701316274e-07 3.55399032522147e-20 transmembrane protein 131 FUNCTION: May play a role in the immune response to viral infection. {ECO:0000250}.; . . lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pharynx;blood;skeletal muscle;breast;bile duct;lung;adrenal gland;nasopharynx;placenta;visual apparatus;alveolus;liver;spleen;head and neck;kidney;stomach;peripheral nerve;thymus; amygdala; 0.45783 0.10928 -1.050945462 7.62561925 2067.68724 8.37853 TMEM132A 2.88925822598835e-06 0.982410391110439 0.0175867196313349 transmembrane protein 132A FUNCTION: May play a role in embryonic and postnatal development of the brain. Increased resistance to cell death induced by serum starvation in cultured cells. Regulates cAMP-induced GFAP gene expression via STAT3 phosphorylation (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;iris;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;alveolus;spleen;cervix;kidney;mammary gland;stomach;thymus; amygdala;subthalamic nucleus;thalamus;occipital lobe;globus pallidus;cingulate cortex; 0.20289 0.09955 -0.435396074 24.70511913 3802.89602 12.11420 TMEM132B 0.455834501099099 0.544155168524104 1.03303767969042e-05 transmembrane protein 132B . . . uterus;heart;testis;skin; dorsal root ganglion;superior cervical ganglion;occipital lobe;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.16426 . -1.679229468 2.677518283 3803.48382 12.12143 TMEM132C 0.667071880413267 0.310682847891683 0.0222452716950502 transmembrane protein 132C . . . unclassifiable (Anatomical System);heart;islets of Langerhans;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;cochlea;macula lutea;liver;spleen;kidney;spinal ganglion;brain; medulla oblongata;ciliary ganglion;atrioventricular node;skeletal muscle; 0.17363 . . . 3428.14645 11.24007 TMEM132D 0.999010386532627 0.00098961138008294 2.08728985255992e-09 transmembrane protein 132D FUNCTION: May serve as a cell-surface marker for oligodendrocyte differentiation. {ECO:0000269|PubMed:12966072}.; . TISSUE SPECIFICITY: Expressed in mature oligodendrocytes. Detected in the brain, lung, pancreas and testis. {ECO:0000269|PubMed:12966072}.; . . 0.28654 . -0.499722488 21.85067233 753.94913 5.44379 TMEM132E 2.40150333216285e-05 0.979585449040297 0.0203905359263811 transmembrane protein 132E FUNCTION: Required for normal inner ear hair cell function and hearing. {ECO:0000269|PubMed:25331638}.; DISEASE: Note=TMEM132E is located in a region involved in a heterozygous deletion of approximately 4.7 Mb; this deletion, involving the NF1 gene and contiguous genes lying in its flanking regions, is observed in a patient 17q11.2 microdeletion syndrome, a syndrome characterized by variable facial dysmorphism, mental retardation, developmental delay, and an excessive number of neurofibromas. {ECO:0000269|PubMed:14569139}.; DISEASE: Note=Several lines of evidence link the Gln-420 variant with autosomal recessive non-syndromic hearing loss. This variant has been reported in 2 siblings with prelingual, bilateral, severe to profound sensorineural hearing loss from a Chinese family of consanguineous marriage and was not found in 500 ethnically matched healthy controls. In mouse, TMEM132E is expressed in cochlea hair cells. In addition, knockdown in zebrafish affects the mechanotransduction of hair cells, a phenotype that can be rescued by wild-type human TMEM132E, but not by the Gln-420 variant. {ECO:0000269|PubMed:25331638}.; . prostate;heart;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;skin; 0.36593 . 0.115764778 62.17268224 613.05728 5.00477 TMEM133 0.025317130805039 0.558322412597001 0.41636045659796 transmembrane protein 133 . . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;adrenal gland;placenta;macula lutea;liver;testis;germinal center;stomach; . 0.06337 . 0.080983847 59.76055674 196.60872 3.03256 TMEM134 3.02585174245466e-08 0.0481054903434183 0.951894479398064 transmembrane protein 134 . . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.08303 . . . 67.08438 1.69338 TMEM135 0.879933359061526 0.120054423919716 1.22170187579193e-05 transmembrane protein 135 FUNCTION: May be involved in peroxisome organization.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;whole body;endometrium;gum;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;adrenal cortex;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;visual apparatus;kidney;stomach;aorta; adipose tissue; 0.28334 0.10368 0.997633954 90.65227648 453.20104 4.42951 TMEM136 0.0348719238573205 0.826725673497935 0.138402402644744 transmembrane protein 136 . . . unclassifiable (Anatomical System);pancreas;lung;whole body;ovary;endometrium;placenta;visual apparatus;hippocampus;parathyroid;choroid;kidney;skin; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.27956 . -0.229483771 36.86010852 40.41022 1.18605 TMEM138 0.53112115683539 0.453215268864111 0.0156635743004984 transmembrane protein 138 FUNCTION: Required for ciliogenesis. {ECO:0000269|PubMed:22282472}.; DISEASE: Joubert syndrome 16 (JBTS16) [MIM:614465]: An autosomal recessive disorder characterized by oculomotor apraxia, variable coloboma, and rare kidney involvement. Neuroradiologically, it is characterized by an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and polydactyly. {ECO:0000269|PubMed:22282472}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.05870 . -0.251530012 35.42108988 15.04074 0.54082 TMEM139 0.0187541363348994 0.731195380557977 0.250050483107124 transmembrane protein 139 FUNCTION: May be involved in cellular trafficking of proteins such as SLC4A1. {ECO:0000305|PubMed:26049106}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;pancreas;optic nerve;placenta;macula lutea;iris;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;ciliary ganglion; 0.00814 0.04021 0.703746784 85.42108988 71.67324 1.76180 TMEM140 0.0397282430652476 0.647490399136758 0.312781357797994 transmembrane protein 140 . . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.13462 . 0.639420866 83.8995046 562.64062 4.81495 TMEM141 0.0991119722986669 0.771783824382022 0.129104203319312 transmembrane protein 141 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;iris;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; . . . 0.147123112 64.11299835 28.39038 0.90912 TMEM143 3.71457884922687e-08 0.188770860207501 0.81122910264671 transmembrane protein 143 . . . unclassifiable (Anatomical System);heart;islets of Langerhans;colon;blood;fovea centralis;choroid;lens;skin;skeletal muscle;retina;pancreas;optic nerve;lung;endometrium;macula lutea;duodenum;liver;spleen;cervix;kidney;brain;pineal gland;mammary gland;stomach; medulla oblongata;testis - interstitial;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.11256 0.07454 -0.422438699 25.64284029 130.54423 2.48946 TMEM144 7.82129795001937e-08 0.27895661297926 0.72104330880776 transmembrane protein 144 . . . unclassifiable (Anatomical System);amygdala;heart;ovary;hypothalamus;colon;parathyroid;skin;skeletal muscle;uterus;pancreas;prostate;optic nerve;lung;frontal lobe;endometrium;nasopharynx;bone;placenta;thyroid;hippocampus;testis;brain; amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;spinal cord;pons;parietal lobe; 0.08601 . 0.21689899 68.12927577 114.51455 2.33126 TMEM145 8.14358020622721e-05 0.996239006592298 0.0036795576056395 transmembrane protein 145 . . . unclassifiable (Anatomical System); . 0.43158 . -0.337894035 30.37272942 62.75813 1.62150 TMEM147 0.137954529384416 0.841959362304374 0.0200861083112098 transmembrane protein 147 . . . lymphoreticular;ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;iris;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;adrenal gland;thyroid;testis;kidney;trigeminal ganglion; 0.19364 0.14027 -0.295622497 32.61972163 16.56071 0.58506 TMEM147-AS1 . . . TMEM147 antisense RNA 1 . . . . . . . . . . . TMEM150A 0.145714083697218 0.836034283541575 0.018251632761207 transmembrane protein 150A FUNCTION: Regulates localization of phosphatidylinositol 4-kinase (PI4K) to the plasma membrane, possibly by reducing the association of TTC7 (TTC7A or TTC7B) with the PI4K complex (PubMed:25608530). Acts as a regulator of phosphatidylinositol 4- phosphate (PtdIns(4)P) synthesis (PubMed:25608530). May also play a role in fasting-induced catabolism (By similarity). {ECO:0000250|UniProtKB:Q9QZE9, ECO:0000269|PubMed:25608530}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;pituitary gland;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;lens;skeletal muscle;lung;adrenal gland;placenta;visual apparatus;macula lutea;liver;spleen;kidney;mammary gland;stomach; . 0.42309 0.10747 -0.427900189 25.14744043 17.14409 0.60263 TMEM150B 4.55239789137001e-06 0.228304689783063 0.771690757819046 transmembrane protein 150B . . . optic nerve;macula lutea;fovea centralis;choroid;lens;brain;retina; . . . -0.093566408 46.7386176 27.38398 0.88237 TMEM150C 0.0113392514005819 0.841806383165459 0.146854365433959 transmembrane protein 150C . . . . . . . 0.082802743 60.09082331 66.78314 1.68617 TMEM151A 0.788175023378681 0.205433175578253 0.00639180104306626 transmembrane protein 151A . . . unclassifiable (Anatomical System);pancreas;optic nerve;lung;frontal lobe;macula lutea;hippocampus;testis;fovea centralis;choroid;lens;brain;retina; . 0.35523 . . . 40.04529 1.17672 TMEM151B . . . transmembrane protein 151B . . . . . 0.21974 . . . 55.52583 1.49718 TMEM154 0.000320382542979419 0.58488225517391 0.41479736228311 transmembrane protein 154 . . . unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;colon;blood;skin;skeletal muscle;bone marrow;uterus;lung;frontal lobe;endometrium;nasopharynx;thyroid;placenta;testis;germinal center;bladder; superior cervical ganglion;atrioventricular node;whole blood; 0.03932 . 0.169169615 65.33380514 41.75051 1.21621 TMEM155 0.0012002097237969 0.399150498222964 0.599649292053239 transmembrane protein 155 . . . unclassifiable (Anatomical System);lung;placenta;hippocampus;liver;testis;spleen;brain; whole brain;dorsal root ganglion;superior cervical ganglion;medulla oblongata;temporal lobe;atrioventricular node;pons;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 1.64891 . 0.858082312 88.55862232 68.75044 1.71772 TMEM156 5.76274863785555e-09 0.0350714722979185 0.964928521939333 transmembrane protein 156 . . . smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;urinary;blood;lens;skeletal muscle;epididymis;visual apparatus;macula lutea;liver;spleen;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;thymus; superior cervical ganglion;skeletal muscle; 0.06615 . 0.396906589 76.30927105 2879.51947 10.16013 TMEM158 0.382809463415714 0.476928399414278 0.140262137170008 transmembrane protein 158 (gene/pseudogene) FUNCTION: Receptor for brain injury-derived neurotrophic peptide (BINP), a synthetic 13-mer peptide. {ECO:0000250}.; . . . . . . . . 3.16244 0.11384 TMEM159 0.00317402725667112 0.598583781903002 0.398242190840327 transmembrane protein 159 . . TISSUE SPECIFICITY: Expressed at high levels in the heart and skeletal muscle. Expressed at low levels in kidney, small intestine, lung and liver. {ECO:0000269|PubMed:15589683}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;bone;thyroid;testis;germinal center;pineal gland;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;kidney;mammary gland;stomach; dorsal root ganglion;skeletal muscle; 0.05522 . 0.747842143 86.47676339 568.92697 4.83925 TMEM160 0.654855932901688 0.320501891111767 0.0246421759865447 transmembrane protein 160 . . . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;hypothalamus;colon;blood;lens;uterus;pancreas;prostate;lung;frontal lobe;oesophagus;trabecular meshwork;visual apparatus;liver;testis;cervix;kidney;brain;mammary gland;tonsil;stomach; amygdala;whole brain;medulla oblongata;subthalamic nucleus;superior cervical ganglion;temporal lobe;prefrontal cortex;globus pallidus;pons;caudate nucleus;cingulate cortex;parietal lobe; 0.28583 0.10821 . . 367.68889 4.05398 TMEM161A 2.04658505555468e-06 0.888389301047722 0.111608652367222 transmembrane protein 161A FUNCTION: May play a role in protection against oxidative stress. Overexpression leads to reduced levels of oxidant-induced DNA damage and apoptosis. {ECO:0000269|PubMed:16551573}.; . . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);tongue;islets of Langerhans;urinary;blood;skeletal muscle;pancreas;lung;epididymis;placenta;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;heart;thyroid;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16997 0.10719 -0.843147538 11.2762444 306.812 3.72770 TMEM161B 0.00368500214116822 0.994459587052595 0.00185541080623647 transmembrane protein 161B . . . ovary;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;endometrium;testis;germinal center;artery;brain;unclassifiable (Anatomical System);cartilage;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;kidney;stomach;aorta; . 0.32916 . -0.005381972 53.50908233 512.51429 4.63438 TMEM161B-AS1 . . . TMEM161B antisense RNA 1 . . . . . . . . . . . TMEM161BP1 . . . transmembrane protein 161B pseudogene 1 . . . . . . . . . . . TMEM163 0.0672624651374226 0.871465864357214 0.0612716705053631 transmembrane protein 163 FUNCTION: May bind zinc and other divalent cations and recruit them to vesicular organelles. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;fovea centralis;choroid;lens;retina;pancreas;optic nerve;whole body;lung;cochlea;nasopharynx;macula lutea;visual apparatus;testis;germinal center;kidney;brain;cerebellum; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.30515 0.12066 -0.449946534 24.00330267 13.33189 0.48460 TMEM164 0.877400449225457 0.121087545417622 0.00151200535692144 transmembrane protein 164 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;mammary gland;stomach;aorta; . 0.37324 . -0.119252484 44.53880632 12.30245 0.44580 TMEM165 0.94379661352925 0.055995325709772 0.000208060760977635 transmembrane protein 165 FUNCTION: May function as a calcium/proton transporter involved in calcium and in lysosomal pH homeostasis. Therefore, it may play an indirect role in protein glycosylation. {ECO:0000269|PubMed:22683087, ECO:0000269|PubMed:23569283}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:22683087}.; . . 0.10960 0.10287 -0.295622497 32.61972163 12.21641 0.44260 TMEM167A 0.388457895130387 0.568850002376118 0.0426921024934949 transmembrane protein 167A FUNCTION: Involved in the early part of the secretory pathway. {ECO:0000269|PubMed:19942856}.; . . . . 0.13895 0.11262 0.057118534 57.99716914 8.64004 0.31731 TMEM167AP1 . . . transmembrane protein 167A pseudogene 1 . . . . . . . . . . . TMEM167B 0.632476718728509 0.338031880600483 0.0294914006710074 transmembrane protein 167B FUNCTION: Involved in the early part of the secretory pathway. {ECO:0000269|PubMed:19942856}.; . . ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;atrium;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; . . 0.101211609 60.95777306 3.65353 0.13486 TMEM168 0.0134130851252731 0.954851781253736 0.0317351336209912 transmembrane protein 168 . . . colon;parathyroid;skin;retina;bone marrow;prostate;whole body;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;blood;skeletal muscle;pancreas;lung;placenta;hippocampus;liver;kidney;stomach;thymus; trigeminal ganglion; 0.50541 . -0.622676946 17.30950696 242.09793 3.35973 TMEM169 0.0117845367387348 0.847117337892377 0.141098125368888 transmembrane protein 169 . . . unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;fovea centralis;choroid;lens;skin;retina;uterus;breast;pancreas;optic nerve;whole body;lung;macula lutea;liver;spleen;kidney;brain; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.08509 . -0.492218069 22.35786742 116.65375 2.34953 TMEM170A 0.000303172215493796 0.352642393869864 0.647054433914643 transmembrane protein 170A . . . unclassifiable (Anatomical System);ovary;islets of Langerhans;hypothalamus;colon;fovea centralis;choroid;lens;retina;prostate;optic nerve;whole body;lung;bone;placenta;macula lutea;visual apparatus;liver;testis;germinal center;kidney;brain;pineal gland; testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.24026 . 0.082802743 60.09082331 13.73607 0.49828 TMEM170B 0.674229051511487 0.304851979911249 0.0209189685772638 transmembrane protein 170B . . . . . . . -0.075159878 47.78839349 5.18888 0.19320 TMEM171 0.000165604398072204 0.446259413028746 0.553574982573182 transmembrane protein 171 . . . unclassifiable (Anatomical System);hypothalamus;colon;blood;kidney;skeletal muscle; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.09515 0.07784 0.176444282 66.07100731 5611.97605 15.50173 TMEM173 0.0323306205833744 0.926467553307166 0.0412018261094599 transmembrane protein 173 FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta). Innate immune response is triggered in response to non-CpG double- stranded DNA from viruses and bacteria delivered to the cytoplasm. Acts by recognizing and binding cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced in response to DNA virus in the cytosol: upon binding of c-di-GMP or cGAMP, autoinhibition is alleviated and TMEM173/STING is able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state. May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons. May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II). Mediates death signaling via activation of the extracellular signal-regulated kinase (ERK) pathway. Essential for the induction of IFN-beta in response to human herpes simplex virus 1 (HHV-1) infection. Exhibits 2',3' phosphodiester linkage-specific ligand recognition. Can bind both 2'-3' linked cGAMP and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (PubMed:26300263). {ECO:0000269|PubMed:18724357, ECO:0000269|PubMed:18818105, ECO:0000269|PubMed:19433799, ECO:0000269|PubMed:19776740, ECO:0000269|PubMed:21074459, ECO:0000269|PubMed:21947006, ECO:0000269|PubMed:23027953, ECO:0000269|PubMed:23258412, ECO:0000269|PubMed:23707065, ECO:0000269|PubMed:23722158, ECO:0000269|PubMed:26229117, ECO:0000269|PubMed:26300263}.; DISEASE: STING-associated vasculopathy, infantile-onset (SAVI) [MIM:615934]: An autoinflammatory disease characterized by early- onset systemic inflammation and cutaneous vasculopathy, resulting in severe skin lesions. Violaceous, scaling lesions of fingers, toes, nose, cheeks and ears progress to acral necrosis in most of the patients. Some patients have severe interstitial lung disease. {ECO:0000269|PubMed:25029335}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in skin endothelial cells, alveolar type 2 pneumocytes, bronchial epithelium and alveolar macrophages. {ECO:0000269|PubMed:18724357, ECO:0000269|PubMed:18818105, ECO:0000269|PubMed:25029335}.; myocardium;ovary;colon;choroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.27303 0.09320 1.15197334 92.52182118 4200.01074 12.88295 TMEM174 0.0152558855768961 0.691338318924271 0.293405795498833 transmembrane protein 174 . . TISSUE SPECIFICITY: Predominantly expressed in kidney. {ECO:0000269|PubMed:20331980}.; unclassifiable (Anatomical System);endometrium;colon;kidney;stomach; superior cervical ganglion;ciliary ganglion;kidney;trigeminal ganglion; 0.32299 . 0.619191319 83.36282142 105.96814 2.23176 TMEM175 0.000439629704611645 0.96321542056509 0.0363449497302987 transmembrane protein 175 FUNCTION: Organelle-specific potassium channel specifically responsible for potassium conductance in endosomes and lysosomes. Forms a potassium-permeable leak-like channel, which regulates lumenal pH stability and is required for autophagosome-lysosome fusion. Constitutes the major lysosomal potassium channel. {ECO:0000269|PubMed:26317472}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:26317472}.; medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);tongue;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;spleen;head and neck;cervix;kidney;stomach;peripheral nerve; superior cervical ganglion;ciliary ganglion; 0.16848 . 0.810142476 87.7388535 748.44954 5.42749 TMEM176A 0.399810437494734 0.591089461428122 0.00910010107714395 transmembrane protein 176A . . . unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;colon;choroid;skin;retina;breast;uterus;prostate;pancreas;lung;frontal lobe;endometrium;oesophagus;thyroid;placenta;visual apparatus;pituitary gland;alveolus;liver;testis;cervix;spleen;kidney;brain;aorta;stomach; fetal liver;liver;kidney; 0.06400 . 1.260404852 93.53031375 368.18153 4.05511 TMEM176B 2.99736600245482e-09 0.0457615958858247 0.954238401116809 transmembrane protein 176B FUNCTION: May play a role in the process of maturation of dendritic cells. Required for the development of cerebellar granule cells (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in lung and dermal fibroblasts. {ECO:0000269|PubMed:9922225}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;thyroid;bone;testis;ciliary body;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach; liver;kidney; 0.05105 0.09812 1.241986644 93.38877094 2656.83785 9.69105 TMEM177 0.428469415988159 0.539006288469293 0.0325242955425481 transmembrane protein 177 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;heart;adrenal cortex;pharynx;blood;lens;bile duct;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach;thymus; superior cervical ganglion;cingulate cortex; 0.24208 . 0.707379532 85.62750649 116.74041 2.35106 TMEM178A 0.95174771629757 0.0481102461630457 0.00014203753938448 transmembrane protein 178A . . . . . 0.30723 . . . 16.79072 0.59040 TMEM178B . . . transmembrane protein 178B . . . . . . . . . 59.77596 1.56956 TMEM179 0.278562205449867 0.632373764901637 0.0890640296484967 transmembrane protein 179 . . . optic nerve;lung;macula lutea;fovea centralis;choroid;lens;brain;retina; ciliary ganglion; 0.11995 . -0.251530012 35.42108988 27.71805 0.89109 TMEM179B 0.0107811505009859 0.834599565522607 0.154619283976407 transmembrane protein 179B . . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; . 0.16334 0.08256 -0.163345027 41.24793583 14.12035 0.51125 TMEM181 0.468986734137893 0.530967098674931 4.61671871758581e-05 transmembrane protein 181 FUNCTION: Mediates action of cytolethal distending toxins (CDT), which are secreted by many pathogenic bacteria. Expression level of TMEM181 is rate-limiting for intoxication. {ECO:0000269|PubMed:19965467}.; . . ovary;colon;skin;retina;bone marrow;uterus;prostate;whole body;thyroid;bone;testis;amniotic fluid;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;hypothalamus;skeletal muscle;breast;lung;placenta;liver;duodenum;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;trigeminal ganglion; 0.11316 . 0.220536484 68.38287332 134.24863 2.51950 TMEM182 0.0159876948837043 0.883213641551349 0.100798663564946 transmembrane protein 182 . . . . . 0.32882 . -0.095386216 46.48502005 27.87033 0.89518 TMEM183A 0.948747425039997 0.0512457618412055 6.81311879772843e-06 transmembrane protein 183A . . . . . . 0.11262 -0.007201372 53.19061099 1041.59333 6.19596 TMEM183AP1 . . . transmembrane protein 183A pseudogene 1 . . . . . . . . . . . TMEM183B . . . transmembrane protein 183B . . TISSUE SPECIFICITY: Expressed in brain, lung, pancreas, thymus, intestine and blood. Not detected in heart, placenta, liver, muscle, kidney, spleen, prostate, testis, ovary and colon. {ECO:0000269|PubMed:16644869}.; . . . 0.11262 . . . . TMEM184A 8.88852476041576e-05 0.782443237877956 0.21746787687444 transmembrane protein 184A . . . unclassifiable (Anatomical System);medulla oblongata;colon;parathyroid;lens;uterus;pancreas;prostate;lung;endometrium;placenta;testis;cervix;kidney;mammary gland;stomach; . 0.11780 . -0.108334733 45.57088936 655.78746 5.13535 TMEM184B 0.878340975684015 0.121351921543969 0.000307102772015999 transmembrane protein 184B FUNCTION: May activate the MAP kinase signaling pathway. {ECO:0000269|PubMed:12761501}.; . . ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;oesophagus;synovium;larynx;bone;thyroid;pituitary gland;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.33713 . -0.53631094 20.53550366 24.77878 0.81381 TMEM184C 0.0175950350566643 0.977796856704646 0.00460810823868949 transmembrane protein 184C FUNCTION: Possible tumor suppressor which may play a role in cell growth. {ECO:0000269|PubMed:17072649}.; . TISSUE SPECIFICITY: Widely expressed with higher expression in lung, kidney, spleen, pancreas, thymus, prostate, testis, ovary, small intestine and thyroid. {ECO:0000269|PubMed:17072649}.; ovary;colon;parathyroid;fovea centralis;skin;retina;whole body;larynx;thyroid;bone;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach; thyroid;cingulate cortex; 0.10626 . -0.185391282 39.67916962 6.62763 0.24528 TMEM185A 0.0400630742754596 0.841528523963899 0.118408401760641 transmembrane protein 185A . . . . . . 0.11262 . . 3.31301 0.12114 TMEM185AP1 . . . transmembrane protein 185A pseudogene 1 . . . . . . . . . . . TMEM185B 0.493451137380388 0.430599692713212 0.0759491699063998 transmembrane protein 185B . . . . . . . . . 50.82318 1.40476 TMEM186 0.00140985400566882 0.664870970814815 0.333719175179517 transmembrane protein 186 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;pharynx;blood;lens;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;head and neck;kidney;mammary gland;stomach; trigeminal ganglion; 0.03008 . -0.247889024 35.98726115 29.44202 0.94182 TMEM187 0.218658492062468 0.647683714421454 0.133657793516078 transmembrane protein 187 . . TISSUE SPECIFICITY: Ubiquitous.; . . 0.10744 0.10161 0.018483465 55.44939844 1005.73008 6.10445 TMEM189 0.00518500567573873 0.968775823607311 0.0260391707169505 transmembrane protein 189 . . . . . . 0.13867 -0.427900189 25.14744043 . . TMEM189-UBE2V1 0.00518500567573873 0.968775823607311 0.0260391707169505 TMEM189-UBE2V1 readthrough FUNCTION: Has no ubiquitin ligase activity on its own. The UBE2V1- UBE2N heterodimer catalyzes the synthesis of non-canonical poly- ubiquitin chains that are linked through Lys-63. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. Plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes. {ECO:0000269|PubMed:11057907, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:9305758, ECO:0000269|PubMed:9418904, ECO:0000269|PubMed:9580084, ECO:0000269|PubMed:9705497}.; . TISSUE SPECIFICITY: Highly expressed in thyroid, pancreas, spinal cord, lymph node, trachea, adrenal gland, bone marrow and pancreas. Detected at low levels in heart, breast, placenta, brain, liver, kidney, stomach and lung. {ECO:0000269|PubMed:9418904, ECO:0000269|PubMed:9705497}.; myocardium;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;oral cavity;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;thymus; . . . -0.560178693 19.30879925 622.46011 5.03156 TMEM190 0.0609863784404815 0.86897847456322 0.0700351469962985 transmembrane protein 190 . . . . . 0.16832 . -0.073340031 48.11866006 21.86062 0.73551 TMEM191A . . . transmembrane protein 191A (pseudogene) . . . . . . . . . . . TMEM191B . . . transmembrane protein 191B . . . . . . . . . . . TMEM191C . . . transmembrane protein 191C . . . . . . . . . . . TMEM192 0.0046981347356385 0.965545399016411 0.029756466247951 transmembrane protein 192 . . TISSUE SPECIFICITY: Strongly expressed in kidney, liver, lung and pancreas. {ECO:0000269|PubMed:20370317}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;hypothalamus;colon;parathyroid;lens;uterus;pancreas;prostate;lung;cerebral cortex;thyroid;placenta;visual apparatus;pituitary gland;duodenum;liver;testis;germinal center;kidney;brain;pineal gland; globus pallidus;trigeminal ganglion; 0.18832 0.09590 -0.471992905 23.03609342 13.59374 0.49380 TMEM196 1.50141300317772e-05 0.130477619939951 0.869507365930017 transmembrane protein 196 . . . . . 0.08773 . 0.058937498 58.26256192 33.48827 1.03353 TMEM198 0.061248392613131 0.922461728832446 0.0162898785544229 transmembrane protein 198 FUNCTION: Promotes LRP6 phosphorylation by casein kinases and thereby plays a role in Wnt signaling. May be a membrane scaffold protein involved in the self-aggregation of LRP6 to further enhance its activity. {ECO:0000269|PubMed:21536646}.; . . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;hypothalamus;colon;skin;retina;breast;prostate;whole body;lung;endometrium;bone;placenta;visual apparatus;hippocampus;liver;testis;spleen;kidney;brain;stomach; . 0.31541 . 0.150760231 64.51403633 114.87874 2.33316 TMEM198B . . . transmembrane protein 198B (pseudogene) . . . . . . . . . . . TMEM199 0.000653685320091756 0.737375253027986 0.261971061651923 transmembrane protein 199 . . . ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;muscle;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; . 0.18423 0.10808 0.373041938 75.29488087 1107.44888 6.35994 TMEM200A 0.835246151685534 0.161481988041995 0.00327186027247132 transmembrane protein 200A . . TISSUE SPECIFICITY: Expressed in cerebellum. {ECO:0000269|PubMed:16000565}.; unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;colon;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;cochlea;endometrium;bone;macula lutea;visual apparatus;liver;pituitary gland;testis;kidney;stomach; . 0.15425 0.10111 -0.843147538 11.2762444 50.13238 1.39097 TMEM200B 0.15528270100677 0.776044848259973 0.0686724507332575 transmembrane protein 200B . . . . . 0.39139 0.08357 . . 57.52956 1.53053 TMEM200C . . . transmembrane protein 200C . . . . . . . . . 385.30298 4.13608 TMEM201 0.841903867149445 0.157480402342496 0.000615730508058671 transmembrane protein 201 FUNCTION: Isoform SAMP1: May define a distinct membrane domain in the vicinity of the mitotic spindle. {ECO:0000269|PubMed:19494128}.; . . unclassifiable (Anatomical System);lymph node;ovary;colon;blood;fovea centralis;choroid;lens;skin;retina;pancreas;optic nerve;lung;endometrium;epididymis;macula lutea;liver;testis;cervix;spleen;kidney;brain;stomach; superior cervical ganglion;ciliary ganglion; 0.30474 . 0.044168103 57.40740741 717.62547 5.31883 TMEM202 6.15971402190463e-07 0.256753546748056 0.743245837280541 transmembrane protein 202 . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; . 0.14895 . 0.573279816 82.08303845 180.92279 2.92368 TMEM203 0.500301666052416 0.426819944279032 0.0728783896685523 transmembrane protein 203 FUNCTION: Involved in the regulation of cellular calcium homeotasis (PubMed:25996873). Required for spermatogenesis (PubMed:25996873). {ECO:0000269|PubMed:25996873}.; . . unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;salivary gland;muscle;colon;blood;skin;bone marrow;prostate;lung;cerebral cortex;placenta;hippocampus;testis;cervix;kidney;brain;mammary gland;stomach; . 0.14955 0.10613 -0.075159878 47.78839349 3.46465 0.12594 TMEM204 0.902171044906255 0.0969829579273254 0.000845997166419965 transmembrane protein 204 FUNCTION: Can influence paracellular permeability. Appears to be involved in cell-cell interactions through adherens.; . TISSUE SPECIFICITY: Highly expressed in lung, heart, kidney and placenta. Lower expression in thymus, spleen, liver, testis and ovary. Expressed in endothelial and restricted epithelial cell populations. {ECO:0000269|PubMed:15206924}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;pancreas;lung;mesenchyma;nasopharynx;placenta;macula lutea;head and neck;kidney;mammary gland; superior cervical ganglion; 0.40584 0.10845 -0.426079032 25.36565228 254.40761 3.43156 TMEM205 0.394574027164483 0.595964551905483 0.00946142093003383 transmembrane protein 205 FUNCTION: In cancer cells, plays a role in resistance to the chemotherapeutic agent cisplatin. {ECO:0000269|PubMed:20589834}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in pancreas, followed by adrenal gland, thyroid, liver, mammary gland, prostate, kidney, and retina; lowest levels in skeletal muscle. Overexpressed in cisplatin-resistant cancer cells (at protein level). {ECO:0000269|PubMed:20589834}.; ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;thyroid;iris;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;spinal cord;pharynx;blood;breast;bile duct;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;cerebellum; liver;kidney; 0.14828 . 0.325313577 73.11276244 42.72868 1.23978 TMEM206 8.00777346701742e-06 0.509521560308125 0.490470431918408 transmembrane protein 206 . . . unclassifiable (Anatomical System);lymph node;cartilage;ovary;hypothalamus;colon;parathyroid;skeletal muscle;prostate;whole body;lung;endometrium;larynx;bone;placenta;visual apparatus;hippocampus;testis;head and neck;germinal center;kidney;brain;stomach;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09732 . -0.448125345 24.19202642 123.78916 2.42184 TMEM207 0.000192958975824054 0.477007607609793 0.522799433414383 transmembrane protein 207 . . TISSUE SPECIFICITY: Expressed in some signet-ring cell carcinoma, especially those showing high invasion and metastatic activity (at protein level). {ECO:0000269|PubMed:22226915}.; kidney; pons; 0.13395 . 0.461228372 78.46190139 538.60636 4.72967 TMEM208 0.424874172613488 0.567571743656849 0.00755408372966299 transmembrane protein 208 FUNCTION: May function as a negative regulator of endoplasmic reticulum-stress induced autophagy. {ECO:0000269|PubMed:23691174}.; . . unclassifiable (Anatomical System);uterus;prostate;lymph node;lung;ovary;islets of Langerhans;placenta;testis;colon;brain; whole brain;superior cervical ganglion;placenta;liver;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.42583 0.10901 -0.119252484 44.53880632 6.01187 0.22606 TMEM209 0.00520456472367071 0.993667460585451 0.00112797469087809 transmembrane protein 209 . . . unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;colon;skin;skeletal muscle;bone marrow;breast;prostate;lung;epididymis;nasopharynx;thyroid;placenta;hypopharynx;liver;testis;head and neck;germinal center;kidney;brain;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.18498 . -0.001743238 53.85114414 148.3781 2.65486 TMEM210 0.313442754852511 0.488459824632384 0.198097420515105 transmembrane protein 210 . . . . . . . . . 54.23258 1.47031 TMEM211 0.216382272106154 0.647851103280192 0.135766624613654 transmembrane protein 211 . . . . . . . 0.413500896 76.67492333 677.99222 5.20325 TMEM212 . . . transmembrane protein 212 . . . nasopharynx; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion; . . 0.101211609 60.95777306 12.6752 0.46231 TMEM212-AS1 . . . TMEM212 antisense RNA 1 . . . . . . . . . . . TMEM212-IT1 . . . TMEM212 intronic transcript 1 . . . . . . . . . . . TMEM213 0.0452604681604892 0.671400979379102 0.283338552460409 transmembrane protein 213 . . . . . . . 0.413500896 76.67492333 23.14245 0.77170 TMEM214 0.00116735534958103 0.9984330160034 0.000399628647018889 transmembrane protein 214 FUNCTION: Critical mediator, in cooperation with CASP4, of endoplasmic reticulum-stress induced apoptosis. Required or the activation of CASP4 following endoplasmic reticulum stress. {ECO:0000269|PubMed:23661706}.; . . myocardium;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;bile duct;pancreas;lung;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.10335 -0.464712395 23.5727766 3273.07 10.91844 TMEM215 0.0082158266283866 0.561641935706324 0.430142237665289 transmembrane protein 215 . . . unclassifiable (Anatomical System); . . . 0.060756528 58.52795471 25.23987 0.82561 TMEM216 0.00201929498374557 0.501817015122845 0.49616368989341 transmembrane protein 216 FUNCTION: Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition. {ECO:0000269|PubMed:22282472}.; DISEASE: Joubert syndrome 2 (JBTS2) [MIM:608091]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. {ECO:0000269|PubMed:20036350, ECO:0000269|PubMed:20512146, ECO:0000269|PubMed:22282472, ECO:0000269|PubMed:22425360}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Meckel syndrome 2 (MKS2) [MIM:603194]: A disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly. {ECO:0000269|PubMed:20512146}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;aorta; . . 0.11262 . . 29.4031 0.94044 TMEM217 0.00500602743445728 0.6960444556196 0.298949516945942 transmembrane protein 217 . . . unclassifiable (Anatomical System);medulla oblongata;lymph node;lung;cartilage;testis;amniotic fluid;cervix; . 0.00781 . 0.17280645 65.75843359 42.03607 1.22444 TMEM218 0.00149018994146523 0.440315788079472 0.558194021979063 transmembrane protein 218 . . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;bile duct;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; . . 0.03689118 56.64071715 12.38392 0.44900 TMEM219 0.00103535655502854 0.597768322610099 0.401196320834872 transmembrane protein 219 FUNCTION: Cell death receptor specific for IGFBP3, may mediate caspase-8-dependent apoptosis upon ligand binding. {ECO:0000269|PubMed:20353938}.; . TISSUE SPECIFICITY: Widely expressed in normal tissues but suppressed in prostate and breast tumor. {ECO:0000269|PubMed:20353938}.; myocardium;medulla oblongata;ovary;salivary gland;intestine;colon;choroid;vein;skin;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;epididymis;placenta;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; testis; . . -0.205617011 38.57631517 17.57031 0.61591 TMEM220 2.01921640889706e-06 0.147298657731758 0.852699323051833 transmembrane protein 220 . . . unclassifiable (Anatomical System);ovary;islets of Langerhans;skin;prostate;lung;adrenal gland;liver;testis;spleen;kidney;spinal ganglion;brain;stomach; superior cervical ganglion;skeletal muscle; . . 0.3032669 72.009908 124.98639 2.43116 TMEM220-AS1 . . . TMEM220 antisense RNA 1 . . . . . . . . . . . TMEM221 . . . transmembrane protein 221 . . . unclassifiable (Anatomical System);optic nerve;endometrium;hypothalamus;macula lutea;fovea centralis;brain;stomach; ciliary ganglion;pons;atrioventricular node; . . . . 85.38367 1.96923 TMEM222 0.0719860750297163 0.872301559576145 0.0557123653941389 transmembrane protein 222 . . . . . 0.44515 0.11167 -0.117432389 44.89266336 106.36913 2.23807 TMEM223 0.0124355311633348 0.649536656493338 0.338027812343327 transmembrane protein 223 . . . colon;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;blood;lens;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta;thymus; medulla oblongata;superior cervical ganglion;liver;trigeminal ganglion;cingulate cortex; . . 1.126294249 92.16206653 663.56876 5.16224 TMEM225 0.541094557388445 0.444369642637986 0.0145357999735687 transmembrane protein 225 FUNCTION: Probably inhibits protein phosphatase 1 (PP1) in sperm via binding to catalytic subunit PPP1CC. {ECO:0000250|UniProtKB:Q9D9S2}.; . . . . . . 1.016049644 90.86459071 45.87247 1.30256 TMEM229A . . . transmembrane protein 229A . . . . . . . 0.079165051 59.43029016 2135.73728 8.50258 TMEM229B 0.214249970166916 0.647974965946271 0.137775063886813 transmembrane protein 229B . . . unclassifiable (Anatomical System);ovary;islets of Langerhans;placenta;colon;parathyroid;brain;retina; superior cervical ganglion;tongue;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13531 0.11183 0.147123112 64.11299835 8.41338 0.30728 TMEM230 0.0138196085002164 0.671345769537419 0.314834621962364 transmembrane protein 230 . . . . . 0.15772 0.09180 . . 23.89693 0.78791 TMEM231 7.38492812005148e-05 0.746705316915517 0.253220833803282 transmembrane protein 231 FUNCTION: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling (By similarity). {ECO:0000250}.; DISEASE: Joubert syndrome 20 (JBTS20) [MIM:614970]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. {ECO:0000269|PubMed:23012439}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Meckel syndrome 11 (MKS11) [MIM:615397]: A disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly. {ECO:0000269|PubMed:23349226}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;colon;parathyroid;skin;skeletal muscle;retina;uterus;prostate;lung;cochlea;endometrium;epididymis;bone;placenta;liver;testis;spleen;kidney;brain;mammary gland;stomach; . . . . . 2538.27303 9.40689 TMEM232 . . . transmembrane protein 232 . . . . . . . 3.260079183 99.39254541 1570.25565 7.33336 TMEM233 . . . transmembrane protein 233 . . . . . . . 0.101211609 60.95777306 17.26614 0.60595 TMEM234 0.000523997901712417 0.691608334999731 0.307867667098557 transmembrane protein 234 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;choroid;skin;uterus;whole body;lung;endometrium;nasopharynx;bone;thyroid;placenta;hippocampus;testis;cervix;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;adrenal gland;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;bone marrow; 0.08719 . 0.547599505 81.2160887 84.17262 1.95284 TMEM235 . . . transmembrane protein 235 . . . . . . . . . 1149.01785 6.45804 TMEM236 . . . transmembrane protein 236 . . . . . 0.20990 . . . 736.2966 5.38508 TMEM237 9.39702047725716e-10 0.157063351520074 0.842936647540224 transmembrane protein 237 FUNCTION: Component of the transition zone in primary cilia. Required for ciliogenesis. {ECO:0000269|PubMed:22152675}.; DISEASE: Joubert syndrome 14 (JBTS14) [MIM:614424]: An autosomal recessive disorder characterized by severe mental retardation, hypotonia, breathing abnormalities in infancy, and dysmorphic facial features. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include renal disease, abnormal eye movements, and postaxial polydactyly. {ECO:0000269|PubMed:22152675}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;colon;fovea centralis;skin;skeletal muscle;retina;bone marrow;uterus;pancreas;prostate;whole body;lung;endometrium;larynx;bone;thyroid;placenta;macula lutea;visual apparatus;liver;head and neck;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion; 0.08461 . 0.350995466 74.37485256 495.75223 4.57604 TMEM238 . . . transmembrane protein 238 . . . . . . . . . 33.07356 1.02424 TMEM239 . . . transmembrane protein 239 . . . unclassifiable (Anatomical System);lung;testis; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.00570 . 0.479642105 78.95140363 104.52884 2.20991 TMEM240 . . . transmembrane protein 240 . DISEASE: Spinocerebellar ataxia 21 (SCA21) [MIM:607454]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA21 is characterized by onset in the first decades of life of slowly progressive relatively mild cerebellar ataxia associated with slight extrapyramidal features predominant in older patients and cognitive impairment predominant in younger patients. Note=The disease is caused by mutations affecting the gene represented in this entry. {ECO:0000269|PubMed:25070513}.; . . . . . 0.21326276 67.71644256 56.56284 1.51194 TMEM241 7.76288053512061e-05 0.920518311093339 0.0794040601013093 transmembrane protein 241 . . . . . 0.04404 0.05769 0.749657564 86.56522765 3173.70792 10.73840 TMEM242 0.000194207923288789 0.478327879905384 0.521477912171327 transmembrane protein 242 . . . . . . 0.11185 0.237127192 68.98443029 275.98383 3.55767 TMEM243 1.28559617872968e-05 0.219496752514955 0.780490391523258 transmembrane protein 243 . . . . . 0.65780 0.11262 0.191216164 66.57230479 47.19343 1.33083 TMEM244 0.03708753594163 0.833632029551744 0.129280434506627 transmembrane protein 244 . . . . . 0.17288 . 0.769889969 86.95447039 6724.16618 17.38656 TMEM245 0.000362236651362455 0.999202985914481 0.000434777434156293 transmembrane protein 245 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10564813}.; . . 0.30531 0.19601 -0.532670911 20.78320359 2751.69692 9.88994 TMEM246 0.278461423575281 0.698560159519768 0.0229784169049507 transmembrane protein 246 . . . . . 0.14625 . -0.358119787 29.16371786 92.84831 2.07106 TMEM246-AS1 . . . TMEM246 antisense RNA 1 . . . . . . . . . . . TMEM247 . . . transmembrane protein 247 . . . . . . . . . 1063.14558 6.25650 TMEM248 0.422731519664078 0.569593179627087 0.00767530070883494 transmembrane protein 248 . . . . . 0.33925 0.11129 -0.471992905 23.03609342 29.59988 0.94541 TMEM248P1 . . . transmembrane protein 248 pseudogene 1 . . . . . . . . . . . TMEM249 0.341068399494477 0.485788170005398 0.173143430500126 transmembrane protein 249 . . . . . . . . . 60.23753 1.57690 TMEM251 0.0771120001365747 0.750153245570923 0.172734754292503 transmembrane protein 251 . . . . . 0.18977 . 0.569646743 81.88841708 21.35058 0.72107 TMEM252 0.00364514746841679 0.628582845518763 0.367772007012821 transmembrane protein 252 . . . . . 0.04628 . 0.060756528 58.52795471 13.62375 0.49479 TMEM253 . . . transmembrane protein 253 . . . . . . . 0.057118534 57.99716914 60.62373 1.58297 TMEM254 0.00506595039575398 0.698508303298461 0.296425746305785 transmembrane protein 254 . . . . . . 0.11003 -0.163345027 41.24793583 . . TMEM254-AS1 . . . TMEM254 antisense RNA 1 . . . . . . . . . . . TMEM255A 0.469576565727473 0.525011614474462 0.00541181979806507 transmembrane protein 255A . . . . . 0.42835 . -0.205617011 38.57631517 67.66769 1.70159 TMEM255B 3.85360358148072e-10 0.0265337188880872 0.973466280726552 transmembrane protein 255B . . . . . 0.19617 . 0.646696306 84.12361406 286.65117 3.62621 TMEM256 2.94821183080695e-05 0.188759788417397 0.811210729464295 transmembrane protein 256 . . . . . 0.25535 0.10439 0.479642105 78.95140363 209.04527 3.12095 TMEM256-PLSCR3 0.245307294025648 0.74810183066463 0.00659087530972188 TMEM256-PLSCR3 readthrough (NMD candidate) . . . . . 0.40072 . . . 18.99513 0.65576 TMEM256P1 . . . transmembrane protein 256 pseudogene 1 . . . . . . . . . . . TMEM256P2 . . . transmembrane protein 256 pseudogene 2 . . . . . . . . . . . TMEM257 0.114594790510145 0.602272207935548 0.283133001554307 transmembrane protein 257 . . TISSUE SPECIFICITY: Brain. In the hippocampus it is mainly localized in the granular-cell layer of the dentate gyrus and in the CA2-CA3 subfields of Ammon's horn. {ECO:0000269|PubMed:9881668}.; . . . . 0.435547893 77.45340882 208.78521 3.11822 TMEM258 0.000864646359600505 0.341664111715477 0.657471241924923 transmembrane protein 258 . . . . . 0.25474 0.11262 0.035072054 56.2514744 2.42849 0.08634 TMEM259 0.899319773250088 0.100492709513369 0.00018751723654361 transmembrane protein 259 FUNCTION: May have a role in the ERAD pathway required for clearance of misfolded proteins in the endoplasmic reticulum (ER). Promotes survival of motor neurons, probably by protecting against ER stress. {ECO:0000250|UniProtKB:Q8CIV2}.; . . . . 0.26525 . . . 284.51134 3.61191 TMEM260 5.88265833039317e-12 0.360734588010792 0.639265411983326 transmembrane protein 260 . . . . . 0.03227 . -0.551080959 19.93394669 1404.00386 7.00483 TMEM261 0.000777639943629337 0.32440761720946 0.674814742846911 transmembrane protein 261 . . . . . 0.02967 0.06605 0.170987912 65.5579146 1571.11884 7.33577 TMEM261P1 . . . transmembrane protein 261 pseudogene 1 . . . . . . . . . . . TMEM262 . . . transmembrane protein 262 . . . . . . . . . 2281.88574 8.83764 TMEM263 . . . transmembrane protein 263 . . . . . 0.21491 0.11262 0.057118534 57.99716914 . . TMEM265 . . . transmembrane protein 265 . . . . . . . . . . . TMEM266 . . . transmembrane protein 266 . . . . . 0.25737 . 0.20030965 67.3566879 . . TMF1 2.8391125268012e-06 0.999841212267616 0.000155948619856966 TATA element modulatory factor 1 FUNCTION: Potential coactivator of the androgen receptor. Mediates STAT3 degradation. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER. This protein binds the HIV-1 TATA element and inhibits transcriptional activation by the TATA-binding protein (TBP). {ECO:0000269|PubMed:10428808, ECO:0000269|PubMed:1409643, ECO:0000269|PubMed:15467733, ECO:0000269|PubMed:17698061}.; . . unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;adrenal cortex;colon;skin;skeletal muscle;retina;breast;uterus;pancreas;lung;frontal lobe;nasopharynx;thyroid;placenta;visual apparatus;liver;testis;head and neck;germinal center;brain;mammary gland;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.43911 0.10638 -0.08265057 47.20452937 720.04831 5.32640 TMF1P1 . . . TATA element modulatory factor 1 pseudogene 1 . . . . . . . . . . . TMIE 0.000366606281610635 0.385949563142413 0.613683830575977 transmembrane inner ear FUNCTION: Unknown. The protein may play some role in a cellular membrane location. May reside within an internal membrane compartment and function in pathways such as those involved in protein and/or vesicle trafficking. Alternatively, the mature protein may be localized in the plasma membrane and serve as a site of interaction for other molecules through its highly charged C-terminal domain.; . TISSUE SPECIFICITY: Expressed in many tissues. {ECO:0000269|PubMed:12145746}.; optic nerve;adrenal gland;macula lutea;visual apparatus;colon;fovea centralis;choroid;kidney;lens;retina; superior cervical ganglion;trigeminal ganglion; 0.19032 0.10485 -0.163345027 41.24793583 29.92428 0.95535 TMIGD1 0.104144558342491 0.863840638038195 0.0320148036193144 transmembrane and immunoglobulin domain containing 1 . . . colon;kidney;stomach;retina; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.05348 . -0.093566408 46.7386176 40.18847 1.18138 TMIGD2 0.0152518701509106 0.878338596891775 0.106409532957314 transmembrane and immunoglobulin domain containing 2 FUNCTION: Plays a role in cell-cell interaction, cell migration, and angiogenesis. Through interaction with HHLA2, costimulates T- cells in the context of TCR-mediated activation. Enhances T-cell proliferation and cytokine production via an AKT-dependent signaling cascade. {ECO:0000269|PubMed:22419821, ECO:0000269|PubMed:23784006}.; . TISSUE SPECIFICITY: Widely expressed, mainly by epithelial and endothelial cells, including bronchial epithelial cells of lung, breast glandular and lobular epithelia cells, urothelium of the bladder, skin epidermis, epithelium of gastrointestinal, rectum, endometrial glands of the uterus, ureter, fallopian tube epithelium, colonic epithelium, small bowl epithelium, stomach epithelium, including both chief and parietal cells, trophoblastic epithelium of placenta, and pancreatic acinar cells (at protein level). Consistently expressed in veins and arteries (at protein level). Not detected in thyroid, cerebellum, cerebral cortex and thymus (at protein level). Expressed in lymphoid organs, with highest levels in thymus, spleen, peripheral blood lymphocytes and liver. In the thymus, expressed in CD4+ and CD8+ single- and double-positive cells, but not in immature CD4- and CD8- double- negative cells (at protein level). In peripheral blood mononuclear cells, highly expressed on CD56+ or CD16+ natural killer cells and CD3+ T-cells(at protein level). Not detected on B-cells(at protein level). Expressed in tonsils (at protein level). {ECO:0000269|PubMed:22419821, ECO:0000269|PubMed:23784006}.; pancreas;ovary;bone;placenta;parathyroid;spleen;thymus; . 0.08093 . 1.931026376 97.46992215 710.71198 5.29848 TMIGD3 . . . transmembrane and immunoglobulin domain containing 3 . . . . . 0.10089 . . . . . TMLHE 0.00276292005354084 0.798699007694511 0.198538072251948 trimethyllysine hydroxylase, epsilon FUNCTION: Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML).; . TISSUE SPECIFICITY: All isoforms, but isoform 8, are widely expressed in adult and fetal tissues. Isoform 8 is restricted to heart and skeletal muscle. {ECO:0000269|PubMed:15754339, ECO:0000269|PubMed:17408883}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;testis;brain;gall bladder;unclassifiable (Anatomical System);heart;cartilage;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; . 0.19429 0.11276 -0.139478553 43.29440906 17.26423 0.60569 TMLHE-AS1 . . . TMLHE antisense RNA 1 . . . . . . . . . . . TMOD1 0.856622011630374 0.143281446243469 9.65421261568061e-05 tropomodulin 1 FUNCTION: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton. May play an important role in regulating the organization of actin filaments by preferentially binding to a specific tropomyosin isoform at its N-terminus. {ECO:0000269|PubMed:8002995}.; . TISSUE SPECIFICITY: Highly expressed in the erythrocyte, heart and skeletal muscle.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;uterus corpus;ovary;fetal brain;beta cell islets;trigeminal ganglion;skeletal muscle; 0.19105 0.23468 -0.560178693 19.30879925 47.28275 1.33324 TMOD2 0.138407691231062 0.857364428884867 0.00422787988407151 tropomodulin 2 FUNCTION: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Neuronal-tissue specific. {ECO:0000269|PubMed:10662549}.; unclassifiable (Anatomical System);skeletal muscle;breast;prostate;lung;frontal lobe;larynx;trabecular meshwork;visual apparatus;hippocampus;testis;head and neck;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons; 0.33638 0.13537 -0.60427181 17.74593064 143.15086 2.60887 TMOD3 0.804645652132819 0.195130229131517 0.000224118735663924 tropomodulin 3 FUNCTION: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10662549}.; ovary;colon;parathyroid;skin;bone marrow;uterus;frontal lobe;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;aorta; . 0.46436 0.19499 -0.560178693 19.30879925 26.05798 0.84660 TMOD4 1.33270686836563e-07 0.586021842882014 0.413978023847299 tropomodulin 4 FUNCTION: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle. {ECO:0000269|PubMed:10662549}.; unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;prostate;optic nerve;lung;larynx;macula lutea;head and neck; . 0.28128 0.12883 0.328949044 73.41354093 204.26159 3.08737 TMPO 0.000659535706594771 0.911605421541058 0.0877350427523478 thymopoietin FUNCTION: May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1.; DISEASE: Cardiomyopathy, dilated 1T (CMD1T) [MIM:613740]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:16247757}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in many tissues. Most abundant in adult thymus and fetal liver.; myocardium;lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;spinal ganglion;artery;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;kidney;stomach;aorta;thymus;cerebellum; dorsal root ganglion;medulla oblongata;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.67240 0.42700 1.515690125 95.47652748 1238.36231 6.64368 TMPO-AS1 . . . TMPO antisense RNA 1 . . . . . . . . . . . TMPOP1 . . . thymopoietin pseudogene 1 . . . . . . . . . . . TMPOP2 . . . thymopoietin pseudogene 2 . . . . . . . . . . . TMPPE 4.8633767753696e-05 0.246030000776472 0.753921365455774 transmembrane protein with metallophosphoesterase domain . . . unclassifiable (Anatomical System);ovary;heart;blood;skin; . . . -0.799052816 12.45576787 344.36639 3.93532 TMPRSS2 0.062064327980345 0.937255405904705 0.000680266114950133 transmembrane protease, serine 2 FUNCTION: Serine protease that proteolytically cleaves and activates the viral spike glycoproteins which facilitate virus- cell membrane fusions; spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. Facilitates human SARS coronavirus (SARS-CoV) infection via two independent mechanisms, proteolytic cleavage of ACE2, which might promote viral uptake, and cleavage of coronavirus spike glycoprotein which activates the glycoprotein for cathepsin L- independent host cell entry. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9); involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity. {ECO:0000269|PubMed:21068237, ECO:0000269|PubMed:21325420, ECO:0000269|PubMed:23536651, ECO:0000269|PubMed:23966399, ECO:0000269|PubMed:24027332, ECO:0000269|PubMed:24227843}.; . TISSUE SPECIFICITY: Highly expressed in prostate epithelial cells and in prostate cancers. Expressed in type II pneumocytes in the lung (at protein level). Expressed strongly in small intestine. Also expressed in colon, stomach and salivary gland. {ECO:0000269|PubMed:11169526, ECO:0000269|PubMed:20382709, ECO:0000269|PubMed:21325420}.; prostate;lung;ovary;lacrimal gland;tongue;testis;colon;blood;head and neck;mammary gland;skeletal muscle;stomach;retina; dorsal root ganglion;superior cervical ganglion;pancreas;prostate;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.29348 0.19494 0.314179756 72.75300778 4340.9652 13.12687 TMPRSS3 4.03368854895368e-05 0.954976860748143 0.0449828023663672 transmembrane protease, serine 3 FUNCTION: Probable serine protease that plays a role in hearing. Acts as a permissive factor for cochlear hair cell survival and activation at the onset of hearing and is required for saccular hair cell survival (By similarity). Activates ENaC (in vitro). {ECO:0000250, ECO:0000269|PubMed:12393794}.; DISEASE: Deafness, autosomal recessive, 8 (DFNB8) [MIM:601072]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:11424922, ECO:0000269|PubMed:11462234, ECO:0000269|PubMed:11907649, ECO:0000269|PubMed:12393794, ECO:0000269|PubMed:16021470}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in many tissues including fetal cochlea. Isoform T is found at increased levels in some carcinomas.; unclassifiable (Anatomical System);ovary;colon;parathyroid;fovea centralis;choroid;lens;retina;uterus;prostate;optic nerve;lung;endometrium;placenta;macula lutea;testis;cervix;kidney;brain;mammary gland;stomach;thymus; superior cervical ganglion;trigeminal ganglion; 0.05547 0.10544 -0.282886048 33.53385232 3995.49751 12.49932 TMPRSS4 1.19754386539244e-08 0.332077657997158 0.667922330027403 transmembrane protease, serine 4 FUNCTION: Probable protease. Seems to be capable of activating ENaC (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: High levels in pancreatic, gastric, colorectal and ampullary cancer. Very weak expression in normal gastrointestinal and urogenital tract.; . . 0.27382 0.16898 1.019682101 90.97664544 2548.83115 9.42825 TMPRSS4-AS1 . . . TMPRSS4 antisense RNA 1 . . . . . . . . . . . TMPRSS5 2.57785706102948e-08 0.154786578700373 0.845213395521057 transmembrane protease, serine 5 FUNCTION: May play a role in hearing. {ECO:0000269|PubMed:17918732}.; . TISSUE SPECIFICITY: Brain-specific. Predominantly expressed in neurons, in their axons, and at the synapses of motoneurons in the spinal cord.; unclassifiable (Anatomical System);lung;whole body;frontal lobe;bone;placenta;liver;testis;spleen;brain; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion; 0.09874 0.12140 0.068033485 59.0351498 376.97117 4.09369 TMPRSS6 3.34440581613057e-06 0.997006759770992 0.00298989582319231 transmembrane protease, serine 6 FUNCTION: Serine protease which hydrolyzes a range of proteins including type I collagen, fibronectin and fibrinogen. Can also activate urokinase-type plasminogen activator with low efficiency. May play a specialized role in matrix remodeling processes in liver. Through the cleavage of HFE2, a regulator of the expression of the iron absorption-regulating hormone hepicidin/HAMP, plays a role in iron homeostasis. {ECO:0000269|PubMed:12149247, ECO:0000269|PubMed:18408718, ECO:0000303|PubMed:25156943}.; DISEASE: Iron-refractory iron deficiency anemia (IRIDA) [MIM:206200]: Key features include congenital hypochromic microcytic anemia, very low mean corpuscular erythrocyte volume, low transferrin saturation, abnormal iron absorption characterized by no hematologic improvement following treatment with oral iron, and abnormal iron utilization characterized by a sluggish, incomplete response to parenteral iron. {ECO:0000269|PubMed:18408718, ECO:0000269|PubMed:18603562, ECO:0000269|PubMed:19357398, ECO:0000269|PubMed:19592582, ECO:0000269|PubMed:19708871, ECO:0000269|PubMed:19747362, ECO:0000269|PubMed:20232450, ECO:0000269|PubMed:20704562, ECO:0000269|PubMed:21618415, ECO:0000269|PubMed:22581667, ECO:0000269|PubMed:25156943, ECO:0000269|PubMed:25588876}. Note=The disease is caused by mutations affecting the gene represented in this entry. Mutations leading to abrogation of TMPRSS6 activity are associated with IRIDA due to elevated levels of hepcidin, a negative regulator of plasma iron pool (PubMed:20232450). {ECO:0000269|PubMed:20232450}.; TISSUE SPECIFICITY: Liver specific. {ECO:0000269|PubMed:12149247}.; unclassifiable (Anatomical System);uterus;lung;liver;testis; superior cervical ganglion;liver;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11488 0.14540 0.589672374 82.36022647 395.53283 4.17829 TMPRSS7 6.09045610445382e-15 0.0276827841846649 0.972317215815329 transmembrane protease, serine 7 FUNCTION: Serine protease which preferentially hydrolyzes peptides with Arg at the P1 position. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, ovary, testis, salivary gland, trachea and lung. {ECO:0000269|PubMed:15853774}.; . . 0.08014 0.14286 1.025142459 91.07100731 2979.88433 10.35570 TMPRSS9 1.76797143257435e-18 0.0117310106792791 0.988268989320721 transmembrane protease, serine 9 FUNCTION: Serase-1 and serase-2 are serine proteases that hydrolyze the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln- Gly-Arg-AMC. In contrast, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Ala- Pro-Ala-AMC are not significantly hydrolyzed.; . TISSUE SPECIFICITY: Expressed in fetal human tissues, such as kidney, liver, lung and brain, and in a variety of tumor cell lines. Weakly expressed in adult tissues including skeletal muscle, liver, placenta and heart. {ECO:0000269|PubMed:12886014}.; unclassifiable (Anatomical System);breast;lung;cartilage;ovary;islets of Langerhans;liver;spleen;kidney;skeletal muscle;aorta; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.07122 . 1.646179058 96.19013918 6013.59996 16.19227 TMPRSS11A 9.57132467628292e-11 0.274857516145361 0.725142483758925 transmembrane protease, serine 11A FUNCTION: Probable serine protease which may play a role in cellular senescence. Overexpression inhibits cell growth and induce G1 cell cycle arrest.; . TISSUE SPECIFICITY: Expressed in esophagus, liver, colon and lung. Down-regulated in esophagus cancers. {ECO:0000269|PubMed:10920976}.; unclassifiable (Anatomical System);skeletal muscle; dorsal root ganglion;superior cervical ganglion;temporal lobe;globus pallidus;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.12560 0.11808 0.354632714 74.58126917 629.97615 5.05852 TMPRSS11B 1.68050228934566e-11 0.029914686037423 0.970085313945772 transmembrane protease, serine 11B FUNCTION: Serine protease. {ECO:0000269|PubMed:24498351}.; . . lung;oesophagus;oral cavity;head and neck;skeletal muscle; . 0.08654 0.09658 -0.110153916 45.48832272 46.40218 1.31366 TMPRSS11BNL 0.315776901388964 0.488340935520117 0.195882163090919 TMPRSS11B N-terminal like, pseudogene . . . . . . . 0.567831482 81.78225997 16.17797 0.57390 TMPRSS11CP . . . transmembrane protease, serine 11C, pseudogene . . . . . . . . . . . TMPRSS11D 0.0625189697700861 0.934180678750592 0.00330035147932199 transmembrane protease, serine 11D FUNCTION: May play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions. Plays a role in the proteolytic processing of ACE2. Proteolytically cleaves and activates the human coronavirus 229E (HCoV-229E) spike glycoprotein which facilitate virus-cell membrane fusions; spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. {ECO:0000269|PubMed:23536651, ECO:0000269|PubMed:24227843}.; . TISSUE SPECIFICITY: Located in the cells of the submucosal serous glands of the bronchi and trachea.; unclassifiable (Anatomical System);larynx;nasopharynx;head and neck;skeletal muscle;tonsil; dorsal root ganglion;superior cervical ganglion;occipital lobe;testis - interstitial;tongue;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.13173 0.51855 -0.736552314 13.93606983 32.5418 1.01329 TMPRSS11E 3.75424420546756e-05 0.950644470579553 0.0493179869783926 transmembrane protease, serine 11E FUNCTION: Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position. {ECO:0000250|UniProtKB:Q5S248}.; . TISSUE SPECIFICITY: Expression can only be detected in tissues derived from the head and neck, and in skin, prostate and testis. {ECO:0000269|PubMed:11161383}.; unclassifiable (Anatomical System);oesophagus;nasopharynx;hypopharynx;head and neck;skin;skeletal muscle; superior cervical ganglion;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.20160 0.13956 0.15257911 64.60839821 1995.23378 8.22977 TMPRSS11F 4.97616723411608e-07 0.958154230382573 0.0418452720007041 transmembrane protease, serine 11F FUNCTION: Probable serine protease. {ECO:0000250}.; . . placenta; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05420 0.09852 0.887394731 89.18966737 2164.37752 8.55799 TMPRSS11GP . . . transmembrane protease, serine 11G, pseudogene . . . . . . . . . . . TMPRSS12 0.00311627484097927 0.819210778441396 0.177672946717625 transmembrane protease, serine 12 . . TISSUE SPECIFICITY: In testis, expressed in spermatocytes and spermatids. Expressed in colorectal cancer (at protein level). {ECO:0000269|PubMed:23436708}.; . . 0.06651 0.08666 0.817616644 87.95116773 785.25901 5.53496 TMPRSS13 6.08622571727962e-05 0.97380570887169 0.0261334288711375 transmembrane protease, serine 13 . . TISSUE SPECIFICITY: Isoform 1 and isoform 3 are predominantly expressed in lung, placenta, pancreas, and prostate. Isoform 3 is weakly expressed in testis and peripheral blood lymphocytes. {ECO:0000269|PubMed:11267681}.; unclassifiable (Anatomical System);breast;ovary;placenta;colon;mammary gland; dorsal root ganglion;superior cervical ganglion;placenta;globus pallidus;atrioventricular node;parietal lobe; 0.09997 0.17970 0.666922772 84.64260439 213.45652 3.15250 TMPRSS15 1.28977099814963e-18 0.0680406969979818 0.931959303002018 transmembrane protease, serine 15 FUNCTION: Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.; DISEASE: Enterokinase deficiency (ENTKD) [MIM:226200]: Life- threatening intestinal malabsorption disorder characterized by diarrhea and failure to thrive. {ECO:0000269|PubMed:11719902}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Intestinal brush border.; placenta;brain;mammary gland; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.07284 0.24515 1.92176904 97.44633168 4144.50068 12.77645 TMSB4X 0.485751296983389 0.434735140737383 0.0795135622792279 thymosin beta 4, X-linked FUNCTION: Plays an important role in the organization of the cytoskeleton (By similarity). Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in several hemopoietic cell lines and lymphoid malignant cells. Decreased levels in myeloma cells. {ECO:0000269|PubMed:3500230}.; . . . 0.03343 0.167351552 65.04482189 . . TMSB4XP1 . . . thymosin beta 4, X-linked pseudogene 1 . . . . . . 0.03343 . . . . TMSB4XP2 . . . thymosin beta 4, X-linked pseudogene 2 . . . unclassifiable (Anatomical System);ovary;cerebellum cortex;islets of Langerhans;hypothalamus;salivary gland;urinary;intestine;pharynx;colon;parathyroid;blood;skin;breast;uterus;prostate;pancreas;lung;frontal lobe;trabecular meshwork;visual apparatus;pituitary gland;liver;testis;kidney;brain;bladder; . 0.45983 0.03343 . . . . TMSB4XP3 . . . thymosin beta 4, X-linked pseudogene 3 . . . . . . . . . . . TMSB4XP4 . . . thymosin beta 4, X-linked pseudogene 4 . . . . . . . . . . . TMSB4XP5 . . . thymosin beta 4, X-linked pseudogene 5 . . . . . . . . . . . TMSB4XP6 . . . thymosin beta 4, X-linked pseudogene 6 . . . . . . . . . . . TMSB4XP7 . . . thymosin beta 4, X-linked pseudogene 7 . . . . . . . . . . . TMSB4XP8 . . . thymosin beta 4, X-linked pseudogene 8 . . . . . 0.13266 . . . . . TMSB4Y 0.334409877031708 0.486678799867303 0.17891132310099 thymosin beta 4, Y-linked FUNCTION: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous.; unclassifiable (Anatomical System);hypothalamus;sympathetic chain;pituitary gland;testis;colon;brain; . 0.10904 . . . . . TMSB10 0.124315434010793 0.612863304822993 0.262821261166214 thymosin beta 10 FUNCTION: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity). {ECO:0000250}.; . . myocardium;ovary;salivary gland;developmental;intestine;colon;choroid;skin;bone marrow;uterus;prostate;frontal lobe;bone;testis;dura mater;brain;bladder;tonsil;unclassifiable (Anatomical System);meninges;trophoblast;lymph node;cartilage;tongue;hypothalamus;pharynx;blood;breast;bile duct;pia mater;lung;cornea;adrenal gland;placenta;visual apparatus;hippocampus;hypopharynx;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; smooth muscle;lung;heart;temporal lobe; 0.09987 0.21807 0.145304857 63.81221986 . . TMSB10P1 . . . thymosin beta 10 pseudogene 1 . . . . . . . . . . . TMSB10P2 . . . thymosin beta 10 pseudogene 2 . . . . . . . . . . . TMSB15A 0.482094888097074 0.436656254415492 0.0812488574874342 thymosin beta 15a FUNCTION: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Neuroblastoma-specific. {ECO:0000269|PubMed:9039501}.; unclassifiable (Anatomical System);islets of Langerhans;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;endometrium;placenta;macula lutea;liver;testis;spleen;brain; superior cervical ganglion;fetal brain;trigeminal ganglion; 0.83831 . 0.12325821 62.38499646 0.55154 0.00800 TMSB15B 0.481871220044893 0.436772868581102 0.0813559113740046 thymosin beta 15B FUNCTION: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity). May be involved in cell migration. {ECO:0000250, ECO:0000269|PubMed:19296525}.; . TISSUE SPECIFICITY: Expressed in colon and colon cancer tissue. {ECO:0000269|PubMed:19296525}.; . . . . . . . . TMTC1 3.06491591423056e-07 0.996221772943393 0.00377792056501527 transmembrane and tetratricopeptide repeat containing 1 . . . unclassifiable (Anatomical System);ovary;cartilage;adrenal cortex;parathyroid;skeletal muscle;skin;retina;breast;pancreas;prostate;lung;placenta;bone;testis;brain; superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node; 0.33022 0.13818 -0.418800956 25.79028073 1433.09079 7.06654 TMTC2 0.863100805982337 0.136895694797929 3.49921973412561e-06 transmembrane and tetratricopeptide repeat containing 2 . . . heart;tongue;hypothalamus;colon;skin;skeletal muscle;retina;uterus;pancreas;prostate;whole body;lung;frontal lobe;endometrium;bone;visual apparatus;hippocampus;pituitary gland;testis;head and neck;kidney;brain;stomach; occipital lobe;superior cervical ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.41496 . 0.444637294 77.91342298 451.09628 4.41475 TMTC3 0.00905213224625117 0.990845477891661 0.000102389862087879 transmembrane and tetratricopeptide repeat containing 3 . . . unclassifiable (Anatomical System);ovary;cerebellum cortex;parathyroid;blood;skin;skeletal muscle;bone marrow;breast;uterus;whole body;lung;frontal lobe;endometrium;placenta;liver;testis;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle;cingulate cortex; 0.14574 0.20325 0.132352165 63.48785091 925.40068 5.90880 TMTC4 3.908551911016e-06 0.988429035195039 0.0115670562530497 transmembrane and tetratricopeptide repeat containing 4 . . . ovary;colon;parathyroid;skin;uterus;prostate;whole body;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex; 0.12824 0.10390 -0.727458245 14.19556499 438.65546 4.36593 TMUB1 0.314893201445842 0.615248982853394 0.0698578157007639 transmembrane and ubiquitin-like domain containing 1 FUNCTION: Involved in sterol-regulated ubiquitination and degradation of HMG-CoA reductase HMGCR (PubMed:21343306). Involved in positive regulation of AMPA-selective glutamate receptor GRIA2 recycling to the cell surface (By similarity). Acts as negative regulator of hepatocyte growth during regeneration (By similarity). {ECO:0000250|UniProtKB:Q53AQ4, ECO:0000250|UniProtKB:Q9JMG3, ECO:0000269|PubMed:21343306}.; . TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in mammary and thyroid glands, bone marrow and spleen; limited expression in cardiac, pancreatic and ovarian tissues. {ECO:0000269|PubMed:24240191}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;cervix;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;caudate nucleus;pons;trigeminal ganglion; 0.20031 0.10431 0.215080721 67.91696155 28.47971 0.91186 TMUB2 0.00130113933247463 0.647548425074099 0.351150435593426 transmembrane and ubiquitin-like domain containing 2 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;lens;bile duct;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;cerebellum;thymus; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.39207 . -0.337894035 30.37272942 380.91104 4.11369 TMX1 0.00332853970137368 0.949782391132031 0.0468890691665953 thioredoxin related transmembrane protein 1 FUNCTION: May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in kidney, liver, placenta and lung.; . . 0.82788 0.11330 -0.582225231 18.44184949 131.77722 2.49853 TMX2 0.42991378476753 0.568576858504785 0.00150935672768569 thioredoxin related transmembrane protein 2 . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12670024}.; myocardium;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;gum;thyroid;bladder;brain;heart;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;choroid;uterus;whole body;larynx;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;occipital lobe;thalamus;hypothalamus;pons;caudate nucleus;prefrontal cortex;globus pallidus;kidney;trigeminal ganglion;parietal lobe;cerebellum; 0.13706 . -0.26993514 34.59542345 36.0498 1.08254 TMX2-CTNND1 . . . TMX2-CTNND1 readthrough (NMD candidate) . . . . . . . . . . . TMX2P1 . . . thioredoxin related transmembrane protein 2 pseudogene 1 . . . . . . . . . . . TMX3 0.191322508256436 0.80858320513027 9.42866132932056e-05 thioredoxin related transmembrane protein 3 FUNCTION: Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase. {ECO:0000269|PubMed:15623505}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in brain, testis, lung, skin, kidney, uterus, bone, stomach, liver, prostate, placenta, eye and muscle. {ECO:0000269|PubMed:15623505}.; smooth muscle;ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach;aorta;thymus; subthalamic nucleus;medulla oblongata;tongue;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.25561 0.11004 0.240763792 69.36777542 113.00046 2.31345 TMX4 0.0106621809140241 0.946183862947551 0.0431539561384247 thioredoxin related transmembrane protein 4 . . . ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;amygdala;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;atrium;larynx;bone;pituitary gland;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;aorta; dorsal root ganglion;amygdala;testis - interstitial;occipital lobe;superior cervical ganglion;hypothalamus;atrioventricular node;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;pituitary;cingulate cortex; 0.16188 . -0.0274281 51.65723048 79.9201 1.88959 TNC 1.4524742493256e-05 0.999985450161582 2.50959242894376e-08 tenascin C FUNCTION: Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Promotes neurite outgrowth from cortical neurons grown on a monolayer of astrocytes. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6.; DISEASE: Deafness, autosomal dominant, 56 (DFNA56) [MIM:615629]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA56 is characterized by progressive hearing impairment with post-lingual onset. {ECO:0000269|PubMed:23936043}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;amniotic fluid;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;spinal cord;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;amnion;hypopharynx;liver;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;uterus;prostate;superior cervical ganglion;adipose tissue;lung;trachea;fetal brain;fetal lung;ciliary ganglion;kidney; 0.63418 0.69224 -0.200673852 38.98914838 8477.80873 19.83828 TNF 0.272829190351182 0.703129454704171 0.0240413549446472 tumor necrosis factor FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation. Impairs regulatory T-cells (Treg) function in individuals with rheumatoid arthritis via FOXP3 dephosphorylation. Upregulates the expression of protein phosphatase 1 (PP1), which dephosphorylates the key 'Ser-418' residue of FOXP3, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). Key mediator of cell death in the anticancer action of BCG-stimulated neutrophils in combination with DIABLO/SMAC mimetic in the RT4v6 bladder cancer cell line (PubMed:22517918). {ECO:0000269|PubMed:16829952, ECO:0000269|PubMed:22517918, ECO:0000269|PubMed:23396208}.; DISEASE: Psoriatic arthritis (PSORAS) [MIM:607507]: An inflammatory, seronegative arthritis associated with psoriasis. It is a heterogeneous disorder ranging from a mild, non-destructive disease to a severe, progressive, erosive arthropathy. Five types of psoriatic arthritis have been defined: asymmetrical oligoarthritis characterized by primary involvement of the small joints of the fingers or toes; asymmetrical arthritis which involves the joints of the extremities; symmetrical polyarthritis characterized by a rheumatoid like pattern that can involve hands, wrists, ankles, and feet; arthritis mutilans, which is a rare but deforming and destructive condition; arthritis of the sacroiliac joints and spine (psoriatic spondylitis). {ECO:0000269|PubMed:12746914}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . . . 0.81899 . -0.029247611 51.40363293 15.40629 0.55317 TNFAIP1 0.00736160545150059 0.923416770209974 0.0692216243385249 TNF alpha induced protein 1 FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in regulation of cytoskeleton structure. The BCR(BACURD2) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. Its interaction with RHOB may regulate apoptosis. May enhance the PCNA-dependent DNA polymerase delta activity. {ECO:0000269|PubMed:19637314, ECO:0000269|PubMed:19782033}.; . . lymphoreticular;ovary;salivary gland;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;brain;gall bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;muscle;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;cerebellum; superior cervical ganglion;placenta;globus pallidus;atrioventricular node;trigeminal ganglion; 0.43358 0.49283 0.082802743 60.09082331 16.90652 0.59549 TNFAIP2 0.00267820839495161 0.98321853975232 0.0141032518527283 TNF alpha induced protein 2 FUNCTION: May play a role as a mediator of inflammation and angiogenesis.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; . 0.14378 0.41915 . . 219.01829 3.19909 TNFAIP3 0.999666684982313 0.000333314290102666 7.2758380374275e-10 TNF alpha induced protein 3 FUNCTION: Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquitinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquitinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system. Required for LPS- induced production of proinflammatory cytokines and IFN beta in LPS-tolerized macrophages. {ECO:0000269|PubMed:14748687, ECO:0000269|PubMed:15258597, ECO:0000269|PubMed:16684768, ECO:0000269|PubMed:17961127, ECO:0000269|PubMed:18164316, ECO:0000269|PubMed:18952128, ECO:0000269|PubMed:19494296, ECO:0000269|PubMed:22099304, ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:8692885, ECO:0000269|PubMed:9299557, ECO:0000269|PubMed:9882303}.; . . lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;alveolus;hypopharynx;liver;cervix;spleen;head and neck;kidney;aorta;stomach;thymus; superior cervical ganglion;smooth muscle;white blood cells;fetal lung;trigeminal ganglion; 0.31507 0.61057 -0.530852121 20.82448691 1191.30876 6.54436 TNFAIP6 4.01524767427486e-06 0.374740882108915 0.625255102643411 TNF alpha induced protein 6 FUNCTION: Possibly involved in cell-cell and cell-matrix interactions during inflammation and tumorigenesis.; . TISSUE SPECIFICITY: Found in the synovial fluid of patients with rheumatoid arthritis. {ECO:0000269|PubMed:7516184}.; unclassifiable (Anatomical System);heart;ovary;parathyroid;skin;skeletal muscle;uterus;prostate;whole body;lung;bone;placenta;testis;spleen;kidney;brain;mammary gland;stomach; superior cervical ganglion;smooth muscle;testis;fetal lung;atrioventricular node;trigeminal ganglion;whole blood; 0.76442 0.19192 1.038098315 91.20665251 1410.32896 7.01486 TNFAIP8 0.239737016503802 0.644532727585312 0.115730255910886 TNF alpha induced protein 8 FUNCTION: Acts as a negative mediator of apoptosis and may play a role in tumor progression. Suppresses the TNF-mediated apoptosis by inhibiting caspase-8 activity but not the processing of procaspase-8, subsequently resulting in inhibition of BID cleavage and caspase-3 activation. {ECO:0000269|PubMed:10644768, ECO:0000269|PubMed:11346652, ECO:0000269|PubMed:14724590}.; . TISSUE SPECIFICITY: Expressed at high levels in the spleen, lymph node, thymus, thyroid, bone marrow and placenta. Expressed at high levels both in various tumor tissues, unstimulated and cytokine- activated cultured cells. Expressed at low levels in the spinal cord, ovary, lung, adrenal glands, heart, brain, testis and skeletal muscle. {ECO:0000269|PubMed:10233894, ECO:0000269|PubMed:10644768, ECO:0000269|PubMed:14724590}.; unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;colon;blood;skin;bone marrow;uterus;lung;nasopharynx;placenta;visual apparatus;testis;kidney;brain;stomach; superior cervical ganglion;lymph node;placenta;white blood cells;atrioventricular node;trigeminal ganglion;whole blood;tonsil;skeletal muscle;bone marrow; 0.50330 0.41968 -0.09720619 46.20193442 9.56395 0.35256 TNFAIP8L1 0.463548116687416 0.445963645761519 0.0904882375510658 TNF alpha induced protein 8 like 1 FUNCTION: Acts as a negative regulator of mTOR activity. {ECO:0000250|UniProtKB:Q8K288}.; . TISSUE SPECIFICITY: High expression detected in most carcinoma cell lines, especially in cells transformed with virus genomes. {ECO:0000269|PubMed:21600655}.; unclassifiable (Anatomical System);medulla oblongata;lung;islets of Langerhans;bone;liver;testis;colon;kidney;mammary gland;stomach; ciliary ganglion; 0.05703 0.37364 . . 7.6987 0.28375 TNFAIP8L2 0.504728364704239 0.424328250682531 0.0709433846132304 TNF alpha induced protein 8 like 2 FUNCTION: Acts as a negative regulator of innate and adaptive immunity by maintaining immune homeostasis. Negative regulator of Toll-like receptor and T-cell receptor function. Prevents hyperresponsiveness of the immune system and maintains immune homeostasis. Inhibits JUN/AP1 and NF-kappa-B activation. Promotes Fas-induced apoptosis (By similarity). {ECO:0000250}.; . . . . 0.26456 0.36921 -0.339715008 30.06605331 49.38099 1.37540 TNFAIP8L3 2.33259080551193e-06 0.0856451426233889 0.914352524785806 TNF alpha induced protein 8 like 3 FUNCTION: Acts as a lipid transfer protein. Preferentially captures and shuttles two lipid second messengers, i.e., phosphatidylinositol 4,5- bisphosphate and phosphatidylinositol 3,4,5-trisphosphate and increases their levels in the plasma membrane. Additionally, may also function as a lipid-presenting protein to enhance the activity of the PI3K-AKT and MEK-ERK pathways. May act as a regulator of tumorigenesis through its activation of phospholipid signaling. {ECO:0000250|UniProtKB:Q3TBL6}.; . TISSUE SPECIFICITY: Widely expressed (at protein level) (PubMed:25479791). Highly expressed in most carcinoma cell lines (PubMed:25479791, PubMed:25242044). {ECO:0000269|PubMed:25242044, ECO:0000269|PubMed:25479791}.; breast;salivary gland; uterus;ciliary ganglion;atrioventricular node; 0.36360 0.34334 0.639420866 83.8995046 159.02312 2.75462 TNFRSF1A 0.985476047130114 0.0145166557308299 7.29713905595834e-06 tumor necrosis factor receptor superfamily member 1A FUNCTION: Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate- specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase.; DISEASE: Familial hibernian fever (FHF) [MIM:142680]: A hereditary periodic fever syndrome characterized by recurrent fever, abdominal pain, localized tender skin lesions and myalgia. Reactive amyloidosis is the main complication and occurs in 25% of cases. {ECO:0000269|PubMed:10199409, ECO:0000269|PubMed:10902757, ECO:0000269|PubMed:11443543, ECO:0000269|PubMed:13130484, ECO:0000269|PubMed:14610673}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multiple sclerosis 5 (MS5) [MIM:614810]: A multifactorial, inflammatory, demyelinating disease of the central nervous system. Sclerotic lesions are characterized by perivascular infiltration of monocytes and lymphocytes and appear as indurated areas in pathologic specimens (sclerosis in plaques). The pathological mechanism is regarded as an autoimmune attack of the myelin sheath, mediated by both cellular and humoral immunity. Clinical manifestations include visual loss, extra-ocular movement disorders, paresthesias, loss of sensation, weakness, dysarthria, spasticity, ataxia and bladder dysfunction. Genetic and environmental factors influence susceptibility to the disease. {ECO:0000269|PubMed:22801493}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. An intronic mutation affecting alternative splicing and skipping of exon 6 directs increased expression of isoform 4 a transcript encoding a C-terminally truncated protein which is secreted and may function as a TNF antagonist.; . ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;oesophagus;endometrium;larynx;bone;thyroid;iris;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;bile duct;breast;pancreas;lung;mesenchyma;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; whole blood; 0.51029 0.91592 0.084621747 60.31493277 154.52417 2.71793 TNFRSF1B 0.778880984183769 0.220801678224394 0.000317337591836467 tumor necrosis factor receptor superfamily member 1B FUNCTION: Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity. {ECO:0000269|PubMed:12370298}.; . . . . 0.58610 0.72827 0.086440867 60.47416844 1375.40435 6.95388 TNFRSF4 0.00720932981621916 0.767863756452999 0.224926913730782 tumor necrosis factor receptor superfamily member 4 FUNCTION: Receptor for TNFSF4/OX40L/GP34. Is a costimulatory molecule implicated in long-term T-cell immunity. {ECO:0000269|PubMed:7704935}.; DISEASE: Immunodeficiency 16 (IMD16) [MIM:615593]: An autosomal recessive primary immunodeficiency associated with classic Kaposi sarcoma of childhood and poor T-cell recall immune responses due to complete functional OX40 deficiency. {ECO:0000269|PubMed:23897980}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.08629 . . . 28.93778 0.92448 TNFRSF6B 4.83457783145428e-05 0.245271450622519 0.754680203599167 tumor necrosis factor receptor superfamily member 6b FUNCTION: Decoy receptor that can neutralize the cytotoxic ligands TNFS14/LIGHT, TNFSF15 and TNFSF6/FASL. Protects against apoptosis. {ECO:0000269|PubMed:21300286}.; . TISSUE SPECIFICITY: Detected in fetal lung, brain and liver. Detected in adult stomach, spinal cord, lymph node, trachea, spleen, colon and lung. Highly expressed in several primary tumors from colon, stomach, rectum, esophagus and in SW480 colon carcinoma cells.; lymphoreticular;colon;skin;retina;bone marrow;uterus;optic nerve;endometrium;bone;iris;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;muscle;urinary;blood;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;stomach;aorta;peripheral nerve;cerebellum; dorsal root ganglion;superior cervical ganglion;medulla oblongata;testis - seminiferous tubule;adrenal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle; . 0.16864 -0.380166007 27.88393489 14.55165 0.52426 TNFRSF8 0.845965386736897 0.154029813423562 4.79983954145297e-06 tumor necrosis factor receptor superfamily member 8 FUNCTION: Receptor for TNFSF8/CD30L. May play a role in the regulation of cellular growth and transformation of activated lymphoblasts. Regulates gene expression through activation of NF- kappa-B.; . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;uterus;prostate;lung;visual apparatus;liver;kidney;brain;bladder; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.33528 0.29463 0.181903047 66.2361406 107.16607 2.24589 TNFRSF9 0.253050500972917 0.740795163449907 0.0061543355771762 tumor necrosis factor receptor superfamily member 9 FUNCTION: Receptor for TNFSF9/4-1BBL. Possibly active during T cell activation.; . TISSUE SPECIFICITY: Expressed on the surface of activated T-cells.; . . 0.04543 0.28103 0.21689899 68.12927577 57.48257 1.52895 TNFRSF10A 3.93409884735762e-13 0.0122372113166698 0.987762788682937 tumor necrosis factor receptor superfamily member 10a FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF- kappa-B. {ECO:0000269|PubMed:9430227}.; . TISSUE SPECIFICITY: Widely expressed. High levels are found in spleen, peripheral blood leukocytes, small intestine and thymus, but also in K-562 erythroleukemia cells, MCF-7 breast carcinoma cells and activated T-cells.; unclassifiable (Anatomical System);breast;prostate;pancreas;ovary;colon;blood;brain;stomach;bone marrow; superior cervical ganglion; 0.10067 0.06615 0.512596355 80.29606039 401.84532 4.20453 TNFRSF10B 9.803529644727e-07 0.536160286012951 0.463838733634084 tumor necrosis factor receptor superfamily member 10b FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF- kappa-B. Essential for ER stress-induced apoptosis. {ECO:0000269|PubMed:15322075}.; DISEASE: Squamous cell carcinoma of the head and neck (HNSCC) [MIM:275355]: A non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues; very highly expressed in tumor cell lines such as HeLaS3, K-562, HL-60, SW480, A-549 and G-361; highly expressed in heart, peripheral blood lymphocytes, liver, pancreas, spleen, thymus, prostate, ovary, uterus, placenta, testis, esophagus, stomach and throughout the intestinal tract; not detectable in brain.; lymphoreticular;ovary;salivary gland;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;ganglion;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;fetal liver;lung;smooth muscle;adrenal gland;tumor;atrioventricular node; 0.17182 . 0.643056625 84.05284265 521.37166 4.66223 TNFRSF10C 1.31871168945746e-07 0.0591669627544869 0.940832905374344 tumor necrosis factor receptor superfamily member 10c FUNCTION: Receptor for the cytotoxic ligand TRAIL. Lacks a cytoplasmic death domain and hence is not capable of inducing apoptosis. May protect cells against TRAIL mediated apoptosis by competing with TRAIL-R1 and R2 for binding to the ligand.; . TISSUE SPECIFICITY: Higher expression in normal tissues than in tumor cell lines. Highly expressed in peripheral blood lymphocytes, spleen, skeletal muscle, placenta, lung and heart.; unclassifiable (Anatomical System);uterus;lung;liver;spleen;blood;kidney;brain;skeletal muscle;bone marrow; subthalamic nucleus;superior cervical ganglion;uterus corpus;spinal cord;globus pallidus;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle;bone marrow; 0.08572 . 0.571462851 81.99457419 197.77014 3.04016 TNFRSF10D 3.28274094560628e-05 0.803664809637488 0.196302362953056 tumor necrosis factor receptor superfamily member 10d FUNCTION: Receptor for the cytotoxic ligand TRAIL. Contains a truncated death domain and hence is not capable of inducing apoptosis but protects against TRAIL-mediated apoptosis. Reports are contradictory with regards to its ability to induce the NF- kappa-B pathway. According to PubMed:9382840, it cannot but according to PubMed:9430226, it can induce the NF-kappa-B pathway.; . TISSUE SPECIFICITY: Widely expressed, in particular in fetal kidney, lung and liver, and in adult testis and liver. Also expressed in peripheral blood leukocytes, colon and small intestine, ovary, prostate, thymus, spleen, pancreas, kidney, lung, placenta and heart.; unclassifiable (Anatomical System);cartilage;colon;skin;skeletal muscle;breast;uterus;bile duct;prostate;pancreas;lung;nasopharynx;trabecular meshwork;visual apparatus;duodenum;liver;testis;spleen;kidney;brain;stomach;gall bladder; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.04346 0.10785 3.111054698 99.26279783 1320.48694 6.83334 TNFRSF11A 0.87991735395021 0.120022306477406 6.03395723840982e-05 tumor necrosis factor receptor superfamily member 11a FUNCTION: Receptor for TNFSF11/RANKL/TRANCE/OPGL; essential for RANKL-mediated osteoclastogenesis. Involved in the regulation of interactions between T-cells and dendritic cells. {ECO:0000269|PubMed:9878548}.; DISEASE: Paget disease of bone 2, early-onset (PDB2) [MIM:602080]: A form of Paget disease, a disorder of bone remodeling characterized by increased bone turnover affecting one or more sites throughout the skeleton, primarily the axial skeleton. Osteoclastic overactivity followed by compensatory osteoblastic activity leads to a structurally disorganized mosaic of bone (woven bone), which is mechanically weaker, larger, less compact, more vascular, and more susceptible to fracture than normal adult lamellar bone. {ECO:0000269|PubMed:10615125}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Osteopetrosis, autosomal recessive 7 (OPTB7) [MIM:612301]: A rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Recessive osteopetrosis commonly manifests in early infancy with macrocephaly, feeding difficulties, evolving blindness and deafness, bone marrow failure, severe anemia, and hepatosplenomegaly. Deafness and blindness are generally thought to represent effects of pressure on nerves. OPTB7 is characterized by paucity of osteoclasts, suggesting a molecular defect in osteoclast development. OPTB7 is associated with hypogammaglobulinemia. {ECO:0000269|PubMed:18606301}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous expression with high levels in skeletal muscle, thymus, liver, colon, small intestine and adrenal gland.; unclassifiable (Anatomical System);lung;islets of Langerhans;colon;cervix;stomach; appendix;trigeminal ganglion; 0.08380 . 0.665103516 84.6131163 577.42674 4.87253 TNFRSF11B 0.272229439885372 0.722555576765683 0.00521498334894519 tumor necrosis factor receptor superfamily member 11b FUNCTION: Acts as decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis. {ECO:0000269|PubMed:22664871, ECO:0000269|PubMed:9168977}.; DISEASE: Paget disease of bone 5, juvenile-onset (PDB5) [MIM:239000]: An autosomal recessive, juvenile-onset form of Paget disease, a disorder of bone remodeling characterized by increased bone turnover affecting one or more sites throughout the skeleton, primarily the axial skeleton. Osteoclastic overactivity followed by compensatory osteoblastic activity leads to a structurally disorganized mosaic of bone (woven bone), which is mechanically weaker, larger, less compact, more vascular, and more susceptible to fracture than normal adult lamellar bone. PDB5 clinical manifestations include short stature, progressive long bone deformities, fractures, vertebral collapse, skull enlargement, and hyperostosis with progressive deafness. {ECO:0000269|PubMed:12189164}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in adult lung, heart, kidney, liver, spleen, thymus, prostate, ovary, small intestine, thyroid, lymph node, trachea, adrenal gland, testis, and bone marrow. Detected at very low levels in brain, placenta and skeletal muscle. Highly expressed in fetal kidney, liver and lung.; ovary;parathyroid;skin;bone marrow;uterus;whole body;cochlea;endometrium;larynx;bone;thyroid;brain;artery;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;skeletal muscle;breast;pancreas;lung;adrenal gland;mesenchyma;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach;aorta; superior cervical ganglion;thyroid;ciliary ganglion;trigeminal ganglion; 0.28271 0.60265 -0.291981272 33.20358575 89.19166 2.02940 TNFRSF12A 0.036421306731277 0.831654627292245 0.131924065976478 tumor necrosis factor receptor superfamily member 12A FUNCTION: Receptor for TNFSF12/TWEAK. Weak inducer of apoptosis in some cell types. Promotes angiogenesis and the proliferation of endothelial cells. May modulate cellular adhesion to matrix proteins. {ECO:0000269|PubMed:11728344}.; . TISSUE SPECIFICITY: Highly expressed in heart, placenta and kidney. Intermediate expression in lung, skeletal muscle and pancreas.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;lymph;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;cervix;kidney;mammary gland;stomach;aorta; heart;placenta;skeletal muscle; 0.18520 . -0.119252484 44.53880632 230.58738 3.28198 TNFRSF13B 6.72184647969379e-13 0.00235485643255051 0.997645143566777 tumor necrosis factor receptor superfamily member 13B FUNCTION: Receptor for TNFSF13/APRIL and TNFSF13B/TALL1/BAFF/BLYS that binds both ligands with similar high affinity. Mediates calcineurin-dependent activation of NF-AT, as well as activation of NF-kappa-B and AP-1. Involved in the stimulation of B- and T- cell function and the regulation of humoral immunity. {ECO:0000269|PubMed:10956646, ECO:0000269|PubMed:10973284}.; DISEASE: Immunoglobulin A deficiency 2 (IGAD2) [MIM:609529]: Selective deficiency of immunoglobulin A (IGAD) is the most common form of primary immunodeficiency, with an incidence of approximately 1 in 600 individuals in the western world. Individuals with symptomatic IGAD often have deficiency of IgG subclasses or decreased antibody response to carbohydrate antigens such as pneumococcal polysaccharide vaccine. Individuals with IGAD also suffer from recurrent sinopulmonary and gastrointestinal infections and have an increased incidence of autoimmune disorders and of lymphoid and non-lymphoid malignancies. In vitro studies have suggested that some individuals with IGAD have impaired isotype class switching to IgA and others may have a post-switch defect. IGAD and CVID have been known to coexist in families. Some individuals initially present with IGAD1 and then develop CVID. These observations suggest that some cases of IGAD and CVID may have a common etiology. {ECO:0000269|PubMed:16007086}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in spleen, thymus, small intestine and peripheral blood leukocytes. Expressed in resting B- cells and activated T-cells, but not in resting T-cells.; unclassifiable (Anatomical System);lung;ovary;cornea;salivary gland;visual apparatus;liver;intestine;colon;pharynx;blood;kidney;brain;mammary gland;skin; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;temporal lobe;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.06394 0.24464 0.532823122 80.96249115 658.24111 5.14551 TNFRSF13C 0.641054687513937 0.3313848776125 0.0275604348735631 tumor necrosis factor receptor superfamily member 13C FUNCTION: B-cell receptor specific for TNFSF13B/TALL1/BAFF/BLyS. Promotes the survival of mature B-cells and the B-cell response. {ECO:0000269|PubMed:11591325, ECO:0000269|PubMed:12387744}.; . TISSUE SPECIFICITY: Highly expressed in spleen and lymph node, and in resting B-cells. Detected at lower levels in activated B-cells, resting CD4+ T-cells, in thymus and peripheral blood leukocytes.; unclassifiable (Anatomical System);lymph node; superior cervical ganglion; 0.09820 0.17730 . . 215.61207 3.16997 TNFRSF14 0.819999054408814 0.179125821386485 0.000875124204700466 tumor necrosis factor receptor superfamily member 14 FUNCTION: Receptor for BTLA. Receptor for TNFSF14/LIGHT and homotrimeric TNFSF1/lymphotoxin-alpha. Involved in lymphocyte activation. Plays an important role in HSV pathogenesis because it enhanced the entry of several wild-type HSV strains of both serotypes into CHO cells, and mediated HSV entry into activated human T-cells. {ECO:0000269|PubMed:8898196}.; . TISSUE SPECIFICITY: Widely expressed, with the highest expression in lung, spleen and thymus.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;choroid;skin;retina;uterus;prostate;whole body;frontal lobe;oesophagus;endometrium;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;skeletal muscle; 0.08353 0.21479 0.130533008 63.35810333 95.09689 2.10337 TNFRSF17 0.00310441854162779 0.593772523861839 0.403123057596533 tumor necrosis factor receptor superfamily member 17 FUNCTION: Receptor for TNFSF13B/BLyS/BAFF and TNFSF13/APRIL. Promotes B-cell survival and plays a role in the regulation of humoral immunity. Activates NF-kappa-B and JNK. {ECO:0000269|PubMed:10801128, ECO:0000269|PubMed:10903733, ECO:0000269|PubMed:10973284}.; . TISSUE SPECIFICITY: Expressed in mature B-cells, but not in T- cells or monocytes.; unclassifiable (Anatomical System);lymph node;ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;lung;nasopharynx;liver;germinal center;kidney;brain;mammary gland;bladder; . 0.10556 0.28423 0.21689899 68.12927577 53.32903 1.45072 TNFRSF18 8.36589277636991e-07 0.0899964437101961 0.910002719700526 tumor necrosis factor receptor superfamily member 18 FUNCTION: Receptor for TNFSF18. Seems to be involved in interactions between activated T-lymphocytes and endothelial cells and in the regulation of T-cell receptor-mediated cell death. Mediated NF-kappa-B activation via the TRAF2/NIK pathway.; . TISSUE SPECIFICITY: Expressed in lymph node, peripheral blood leukocytes and weakly in spleen.; unclassifiable (Anatomical System);lymph node;oesophagus;blood;kidney; . 0.03798 0.16362 . . 185.06659 2.95295 TNFRSF19 0.0198825133386579 0.961763685286052 0.0183538013752895 tumor necrosis factor receptor superfamily member 19 FUNCTION: Can mediate activation of JNK and NF-kappa-B. May promote caspase-independent cell death.; . TISSUE SPECIFICITY: Highly expressed in prostate. Detected at lower levels in thymus, spleen, testis, uterus, small intestine, colon and peripheral blood leukocytes.; ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;epidermis;islets of Langerhans;adrenal cortex;lens;breast;lung;placenta;macula lutea;liver;duodenum;spleen;kidney;mammary gland; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.08332 0.16873 0.134171522 63.57041755 2163.58365 8.55639 TNFRSF21 0.656653056375282 0.342168380388638 0.00117856323608018 tumor necrosis factor receptor superfamily member 21 FUNCTION: Promotes apoptosis, possibly via a pathway that involves the activation of NF-kappa-B. Can also promote apoptosis mediated by BAX and by the release of cytochrome c from the mitochondria into the cytoplasm. Plays a role in neuronal apoptosis, including apoptosis in response to amyloid peptides derived from APP, and is required for both normal cell body death and axonal pruning. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). N-APP binds TNFRSF21; this triggers caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase- 6). Negatively regulates oligodendrocyte survival, maturation and myelination. Plays a role in signaling cascades triggered by stimulation of T-cell receptors, in the adaptive immune response and in the regulation of T-cell differentiation and proliferation. Negatively regulates T-cell responses and the release of cytokines such as IL4, IL5, IL10, IL13 and IFNG by Th2 cells. Negatively regulates the production of IgG, IgM and IgM in response to antigens. May inhibit the activation of JNK in response to T-cell stimulation. {ECO:0000269|PubMed:21725297, ECO:0000269|PubMed:22761420, ECO:0000269|PubMed:9714541}.; . TISSUE SPECIFICITY: Detected in fetal spinal cord and in brain neurons, with higher levels in brain from Alzheimer disease patients (at protein level). Highly expressed in heart, brain, placenta, pancreas, lymph node, thymus and prostate. Detected at lower levels in lung, skeletal muscle, kidney, testis, uterus, small intestine, colon, spleen, bone marrow and fetal liver. Very low levels were found in adult liver and peripheral blood leukocytes. {ECO:0000269|PubMed:21725297, ECO:0000269|PubMed:23559013, ECO:0000269|PubMed:9714541}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;prostate;optic nerve;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;hypothalamus;spinal cord;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;alveolus;liver;head and neck;cervix;kidney;stomach; spinal cord; 0.29075 0.22804 -0.997481928 8.47487615 218.25934 3.19261 TNFRSF25 0.448738853101197 0.549952459536815 0.00130868736198819 tumor necrosis factor receptor superfamily member 25 FUNCTION: Receptor for TNFSF12/APO3L/TWEAK. Interacts directly with the adapter TRADD. Mediates activation of NF-kappa-B and induces apoptosis. May play a role in regulating lymphocyte homeostasis.; . TISSUE SPECIFICITY: Abundantly expressed in thymocytes and lymphocytes. Detected in lymphocyte-rich tissues such as thymus, colon, intestine, and spleen. Also found in the prostate.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;endometrium;testis;brain;unclassifiable (Anatomical System);heart;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;fetal brain;cerebellum peduncles;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.07638 0.08949 0.352813824 74.49280491 491.21178 4.56014 TNFSF4 0.12523000717497 0.780064480709964 0.0947055121150662 tumor necrosis factor superfamily member 4 FUNCTION: Cytokine that binds to TNFRSF4. Co-stimulates T-cell proliferation and cytokine production.; DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:18059267}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. The upstream region of TNFSF4 contains a single risk haplotype for SLE, which is correlated with increased expression of both cell-surface TNFSF4 and TNFSF4 transcripts. Increased levels of TNFSF4 are thought to augment T-cell-APC interaction and the functional consequences of T-cell activation, thereby destabilizing peripheral tolerance.; . unclassifiable (Anatomical System);lymph node;cartilage;fovea centralis;choroid;lens;skin;retina;bone marrow;optic nerve;lung;thyroid;macula lutea;liver;testis;head and neck;brain; dorsal root ganglion;superior cervical ganglion;testis;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.25826 0.30837 -0.229483771 36.86010852 13.59469 0.49405 TNFSF8 0.852776651355479 0.144788842233285 0.00243450641123668 tumor necrosis factor superfamily member 8 FUNCTION: Cytokine that binds to TNFRSF8/CD30. Induces proliferation of T-cells.; . . breast;lung;nasopharynx;blood; dorsal root ganglion;superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.13650 0.15628 -0.05129383 49.75819769 13.21673 0.48063 TNFSF9 0.0968268555510867 0.770297257609198 0.132875886839715 tumor necrosis factor superfamily member 9 FUNCTION: Cytokine that binds to TNFRSF9. Induces the proliferation of activated peripheral blood T-cells. May have a role in activation-induced cell death (AICD). May play a role in cognate interactions between T-cells and B-cells/macrophages. {ECO:0000269|PubMed:20032458}.; . TISSUE SPECIFICITY: Expressed in brain, placenta, lung, skeletal muscle and kidney.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;prostate;lung;bone;thyroid;visual apparatus;liver;testis;cervix;kidney;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10940 0.16909 0.815800671 87.8744987 112.66465 2.30853 TNFSF10 0.405364744467663 0.585903128215736 0.00873212731660027 tumor necrosis factor superfamily member 10 FUNCTION: Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to TNFRSF11B/OPG. Induces apoptosis. Its activity may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and TNFRSF11B/OPG that cannot induce apoptosis.; . TISSUE SPECIFICITY: Widespread; most predominant in spleen, lung and prostate.; smooth muscle;ovary;colon;parathyroid;vein;skin;uterus;prostate;atrium;cochlea;cerebral cortex;oesophagus;endometrium;larynx;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;whole blood;trigeminal ganglion;skeletal muscle; 0.09599 0.67074 0.038710339 56.92380278 70.16123 1.73921 TNFSF11 0.130191546680804 0.847621303971364 0.0221871493478313 tumor necrosis factor superfamily member 11 FUNCTION: Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy. {ECO:0000269|PubMed:22664871}.; DISEASE: Osteopetrosis, autosomal recessive 2 (OPTB2) [MIM:259710]: A rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Recessive osteopetrosis commonly manifests in early infancy with macrocephaly, feeding difficulties, evolving blindness and deafness, bone marrow failure, severe anemia, and hepatosplenomegaly. Deafness and blindness are generally thought to represent effects of pressure on nerves. OPTB2 is characterized by paucity of osteoclasts, suggesting a molecular defect in osteoclast development. {ECO:0000269|PubMed:17632511}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest in the peripheral lymph nodes, weak in spleen, peripheral blood Leukocytes, bone marrow, heart, placenta, skeletal muscle, stomach and thyroid.; lung;cartilage;islets of Langerhans;testis;germinal center; medulla oblongata;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.49335 0.88170 -0.093566408 46.7386176 162.64108 2.78445 TNFSF12 0.997954015355093 0.00204592404498372 6.05999232153312e-08 tumor necrosis factor superfamily member 12 FUNCTION: Binds to FN14 and possibly also to TNRFSF12/APO3. Weak inducer of apoptosis in some cell types. Mediates NF-kappa-B activation. Promotes angiogenesis and the proliferation of endothelial cells. Also involved in induction of inflammatory cytokines. Promotes IL8 secretion. {ECO:0000269|PubMed:10085077, ECO:0000269|PubMed:23667509}.; . TISSUE SPECIFICITY: Highly expressed in adult heart, pancreas, skeletal muscle, brain, colon, small intestine, lung, ovary, prostate, spleen, lymph node, appendix and peripheral blood lymphocytes. Low expression in kidney, testis, liver, placenta, thymus and bone marrow. Also detected in fetal kidney, liver, lung and brain.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;retina;bile duct;pancreas;prostate;optic nerve;lung;bone;placenta;alveolus;testis;spleen;kidney;brain;mammary gland;stomach; . . 0.50353 -0.207437529 38.2814343 . . TNFSF12-TNFSF13 0.997954015355093 0.00204592404498372 6.05999232153312e-08 TNFSF12-TNFSF13 readthrough FUNCTION: Binds to FN14 and possibly also to TNRFSF12/APO3. Weak inducer of apoptosis in some cell types. Mediates NF-kappa-B activation. Promotes angiogenesis and the proliferation of endothelial cells. Also involved in induction of inflammatory cytokines. Promotes IL8 secretion. {ECO:0000269|PubMed:10085077, ECO:0000269|PubMed:23667509}.; . TISSUE SPECIFICITY: Highly expressed in adult heart, pancreas, skeletal muscle, brain, colon, small intestine, lung, ovary, prostate, spleen, lymph node, appendix and peripheral blood lymphocytes. Low expression in kidney, testis, liver, placenta, thymus and bone marrow. Also detected in fetal kidney, liver, lung and brain.; ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;pineal body;blood;lens;lung;nasopharynx;placenta;visual apparatus;liver;alveolus;spleen;head and neck;kidney;mammary gland;aorta; . . . -0.139478553 43.29440906 8.01635 0.29491 TNFSF13 0.877768012752006 0.121921073064551 0.000310914183443104 tumor necrosis factor superfamily member 13 FUNCTION: Cytokine that binds to TNFRSF13B/TACI and to TNFRSF17/BCMA. Plays a role in the regulation of tumor cell growth. May be involved in monocyte/macrophage-mediated immunological processes. {ECO:0000269|PubMed:10973284}.; . TISSUE SPECIFICITY: Expressed at high levels in transformed cell lines, cancers of colon, thyroid, lymphoid tissues and specifically expressed in monocytes and macrophages.; ovary;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pineal body;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;hippocampus;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;aorta; . . 0.50353 0.170987912 65.5579146 1037.22684 6.18488 TNFSF13B 0.954794121426939 0.045085177606775 0.000120700966286404 tumor necrosis factor superfamily member 13b FUNCTION: Cytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA. TNFSF13/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR/BR3) promotes the survival of mature B-cells and the B-cell response. {ECO:0000269|PubMed:10973284}.; FUNCTION: Isoform 3: Acts as a transcription factor for its own parent gene, in association with NF-kappa-B p50 subunit, at least in autoimmune and proliferative B-cell diseases. The presence of Delta4BAFF is essential for soluble BAFF release by IFNG/IFN- gamma-stimulated monocytes and for B-cell survival. It can directly or indirectly regulate the differential expression of a large number of genes involved in the innate immune response and the regulation of apoptosis. {ECO:0000269|PubMed:10973284}.; . TISSUE SPECIFICITY: Abundantly expressed in peripheral blood Leukocytes and is specifically expressed in monocytes and macrophages. Also found in the spleen, lymph node, bone marrow, T- cells and dendritic cells. A lower expression seen in placenta, heart, lung, fetal liver, thymus, and pancreas. Isoform 2 is expressed in many myeloid cell lines. {ECO:0000269|PubMed:12867412}.; . . 0.04102 0.27708 0.080983847 59.76055674 22.39402 0.75106 TNFSF14 0.813514842794245 0.185521039545451 0.000964117660303736 tumor necrosis factor superfamily member 14 FUNCTION: Cytokine that binds to TNFRSF3/LTBR. Binding to the decoy receptor TNFRSF6B modulates its effects. Activates NFKB, stimulates the proliferation of T-cells, and inhibits growth of the adenocarcinoma HT-29. Acts as a receptor for Herpes simplex virus.; . TISSUE SPECIFICITY: Predominantly expressed in the spleen but also found in the brain. Weakly expressed in peripheral lymphoid tissues and in heart, placenta, liver, lung, appendix, and kidney, and no expression seen in fetal tissues, endocrine glands, or nonhematopoietic tumor lines.; smooth muscle;ovary;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;pharynx;blood;bile duct;pancreas;lung;adrenal gland;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; uterus corpus;whole blood;skeletal muscle; 0.10745 0.26428 -0.26993514 34.59542345 15.91413 0.56428 TNFSF15 0.364139465628525 0.62398601610354 0.0118745182679348 tumor necrosis factor superfamily member 15 FUNCTION: Receptor for TNFRSF25 and TNFRSF6B. Mediates activation of NF-kappa-B. Inhibits vascular endothelial growth and angiogenesis (in vitro). Promotes activation of caspases and apoptosis. {ECO:0000269|PubMed:10597252, ECO:0000269|PubMed:11911831, ECO:0000269|PubMed:11923219, ECO:0000269|PubMed:9872942}.; . TISSUE SPECIFICITY: Specifically expressed in endothelial cells. Detected in monocytes, placenta, lung, liver, kidney, skeletal muscle, pancreas, spleen, prostate, small intestine and colon. {ECO:0000269|PubMed:11911831, ECO:0000269|PubMed:11923219, ECO:0000269|PubMed:9434163, ECO:0000269|PubMed:9872942}.; . . 0.12131 0.17508 0.016664174 55.21939137 106.16684 2.23547 TNFSF18 0.000468355604968885 0.431857286206019 0.567674358189012 tumor necrosis factor superfamily member 18 FUNCTION: Cytokine that binds to TNFRSF18/AITR/GITR. Regulates T- cell responses. Can function as costimulator and lower the threshold for T-cell activation and T-cell proliferation. Important for interactions between activated T-lymphocytes and endothelial cells. Mediates activation of NF-kappa-B. Triggers increased phosphorylation of STAT1 and up-regulates expression of VCAM1 and ICAM1 (PubMed:23892569). Promotes leukocyte adhesion to endothelial cells (PubMed:23892569). Regulates migration of monocytes from the splenic reservoir to sites of inflammation (By similarity). {ECO:0000250|UniProtKB:Q7TS55, ECO:0000269|PubMed:17449724, ECO:0000269|PubMed:18040044, ECO:0000269|PubMed:23892569}.; . TISSUE SPECIFICITY: Expressed at high levels in the small intestine, ovary, testis, kidney and endothelial cells.; skeletal muscle; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.17232 0.17385 -0.05129383 49.75819769 29.21564 0.93410 TNIK 0.997185845677764 0.00281415432222103 1.5174917840831e-14 TRAF2 and NCK interacting kinase FUNCTION: Serine/threonine kinase that acts as an essential activator of the Wnt signaling pathway. Recruited to promoters of Wnt target genes and required to activate their expression. May act by phosphorylating TCF4/TCF7L2. Appears to act upstream of the JUN N-terminal pathway. May play a role in the response to environmental stress. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it may play a role in cytoskeletal rearrangements and regulate cell spreading. Phosphorylates SMAD1 on Thr-322. {ECO:0000269|PubMed:10521462, ECO:0000269|PubMed:15342639, ECO:0000269|PubMed:19061864, ECO:0000269|PubMed:19816403, ECO:0000269|PubMed:20159449, ECO:0000269|PubMed:21690388}.; . TISSUE SPECIFICITY: Expressed ubiquitously. Highest levels observed in heart, brain and skeletal muscle. Expressed in normal colonic epithelia and colorectal cancer tissues. {ECO:0000269|PubMed:10521462, ECO:0000269|PubMed:19816403}.; unclassifiable (Anatomical System);heart;hypothalamus;colon;blood;skeletal muscle;skin;breast;uterus;prostate;lung;frontal lobe;bone;thyroid;placenta;liver;amnion;testis;spleen;germinal center;brain;gall bladder;stomach;cerebellum; dorsal root ganglion;medulla oblongata;superior cervical ganglion;occipital lobe;temporal lobe;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.85530 0.18807 -1.438469007 3.974994102 257.83038 3.45413 TNIP1 0.929689199234392 0.0703101802276169 6.20537990963087e-07 TNFAIP3 interacting protein 1 FUNCTION: Inhibits NF-kappa-B activation and TNF-induced NF-kappa- B-dependent gene expression by regulating A20/TNFAIP3-mediated deubiquitination of IKBKG; proposed to link A20/TNFAIP3 to ubiquitinated IKBKG. Involved in regulation of EGF-induced ERK1/ERK2 signaling pathway; blocks MAPK3/MAPK1 nuclear translocation and MAPK1-dependent transcription. Increases cell surface CD4(T4) antigen expression. Involved in the anti- inflammatory response of macrophages and positively regulates TLR- induced activation of CEBPB. Involved in the prevention of autoimmunity; this function implicates binding to polyubiquitin. Involved in leukocyte integrin activation during inflammation; this function is mediated by association with SELPLG and dependent on phosphorylation by SRC-family kinases. Interacts with HIV-1 matrix protein and is packaged into virions and overexpression can inhibit viral replication. May regulate matrix nuclear localization, both nuclear import of PIC (Preintegration complex) and export of GAG polyprotein and viral genomic RNA during virion production. In case of infection, promotes association of IKBKG with Shigella flexneri E3 ubiquitin-protein ligase ipah9.8 p which in turn promotes polyubiquitination of IKBKG leading to its proteasome-dependent degradation and thus is perturbing NF-kappa-B activation during bacterial infection. {ECO:0000269|PubMed:12220502, ECO:0000269|PubMed:16684768, ECO:0000269|PubMed:17016622, ECO:0000269|PubMed:17632516, ECO:0000269|PubMed:20010814}.; . TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in peripheral blood lymphocytes, spleen and skeletal muscle, and is weakly expressed in the brain. In peripheral blood mononucleocytes, isoform 4 is mainly expressed and isoform 1 and isoform 7 are almost not expressed. Expression of isoform 1 and isoform 7 increases in leukemic cells. {ECO:0000269|PubMed:17016622}.; myocardium;lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;gum;thyroid;iris;amniotic fluid;germinal center;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;hypopharynx;amnion;head and neck;kidney;stomach;aorta; . 0.13654 0.15801 0.668743049 84.68388771 891.12237 5.81885 TNIP2 2.97330525116274e-06 0.771321550983513 0.228675475711236 TNFAIP3 interacting protein 2 FUNCTION: Inhibits NF-kappa-B activation by blocking the interaction of RIPK1 with its downstream effector NEMO/IKBKG. Forms a ternary complex with NFKB1 and MAP3K8 but appears to function upstream of MAP3K8 in the TLR4 signaling pathway that regulates MAP3K8 activation. Involved in activation of the MEK/ERK signaling pathway during innate immune response; this function seems to be stimulus- and cell type specific. Required for stability of MAP3K8. Involved in regulation of apoptosis in endothelial cells; promotes TEK agonist-stimulated endothelial survival. May act as transcriptional coactivator when translocated to the nucleus. Enhances CHUK-mediated NF-kappa-B activation involving NF-kappa-B p50-p65 and p50-c-Rel complexes. {ECO:0000269|PubMed:12595760, ECO:0000269|PubMed:12753905, ECO:0000269|PubMed:12933576, ECO:0000269|PubMed:14653779, ECO:0000269|PubMed:15169888, ECO:0000269|PubMed:21784860}.; . TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined. {ECO:0000269|PubMed:12595760}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;placenta;testis;ciliary ganglion;atrioventricular node;kidney;skeletal muscle; 0.15827 0.13368 -0.067881249 48.69072895 2150.74071 8.52782 TNIP3 0.324695186091686 0.674611683864715 0.000693130043599107 TNFAIP3 interacting protein 3 FUNCTION: Binds to zinc finger protein TNFAIP3 and inhibits NF- kappa-B activation induced by tumor necrosis factor, Toll-like receptor 4 (TLR4), interleukin-1 and 12-O-tetradecanoylphorbol-13- acetate. Overexpression inhibits NF-kappa-B-dependent gene expression in response to lipopolysaccharide at a level downstream of TRAF6 and upstream of IKBKB. NF-kappa-B inhibition is independent of TNFAIP3 binding. {ECO:0000269|PubMed:17088249}.; . TISSUE SPECIFICITY: Highly expressed in lung, lymph node, thymus and fetal liver. Expressed at lower levels in bone marrow, brain, kidney, spleen, leukocytes and tonsils. Could be detected in heart, salivary gland, adrenal gland, pancreas, ovary and fetal brain. High levels detected in liver, colon, small intestine, muscle, stomach, testis, placenta, thyroid, uterus, prostate, skin and PBL. {ECO:0000269|PubMed:11345586, ECO:0000269|PubMed:17088249}.; unclassifiable (Anatomical System);lung;testis;cervix; ciliary ganglion;skeletal muscle; 0.07030 0.15040 0.439181676 77.69521113 213.53141 3.15341 TNK1 8.54608747197239e-05 0.929155146494123 0.0707593926311576 tyrosine kinase, non-receptor, 1 FUNCTION: Involved in negative regulation of cell growth. Has tumor suppressor properties. Plays a negative regulatory role in the Ras-MAPK pathway. May function in signaling pathways utilized broadly during fetal development and more selectively in adult tissues and in cells of the lymphohematopoietic system. Could specifically be involved in phospholipid signal transduction. {ECO:0000269|PubMed:10873601, ECO:0000269|PubMed:18974114}.; . TISSUE SPECIFICITY: Expressed in all umbilical cord blood, bone marrow and adult blood cell sub-populations and in several leukemia cell lines. Highly expressed in fetal blood, brain, lung, liver and kidney. Detected at lower levels in adult prostate, testis, ovary, small intestine and colon. Not expressed in adult lung, liver, kidney or brain. {ECO:0000269|PubMed:10873601, ECO:0000269|PubMed:8632913}.; colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;iris;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;lens;pancreas;lung;macula lutea;head and neck;kidney;stomach;aorta;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13821 0.18145 0.088260113 60.56853031 651.69939 5.12017 TNK2 1.20620740888102e-10 0.752427007470375 0.247572992409005 tyrosine kinase, non-receptor, 2 FUNCTION: Non-receptor tyrosine-protein and serine/threonine- protein kinase that is implicated in cell spreading and migration, cell survival, cell growth and proliferation. Transduces extracellular signals to cytosolic and nuclear effectors. Phosphorylates AKT1, AR, MCF2, WASL and WWOX. Implicated in trafficking and clathrin-mediated endocytosis through binding to epidermal growth factor receptor (EGFR) and clathrin. Binds to both poly- and mono-ubiquitin and regulates ligand-induced degradation of EGFR, thereby contributing to the accumulation of EGFR at the limiting membrane of early endosomes. Downstream effector of CDC42 which mediates CDC42-dependent cell migration via phosphorylation of BCAR1. May be involved both in adult synaptic function and plasticity and in brain development. Activates AKT1 by phosphorylating it on 'Tyr-176'. Phosphorylates AR on 'Tyr-267' and 'Tyr-363' thereby promoting its recruitment to androgen-responsive enhancers (AREs). Phosphorylates WWOX on 'Tyr- 287'. Phosphorylates MCF2, thereby enhancing its activity as a guanine nucleotide exchange factor (GEF) toward Rho family proteins. Contributes to the control of AXL receptor levels. Confers metastatic properties on cancer cells and promotes tumor growth by negatively regulating tumor suppressor such as WWOX and positively regulating pro-survival factors such as AKT1 and AR. {ECO:0000269|PubMed:10652228, ECO:0000269|PubMed:11278436, ECO:0000269|PubMed:16247015, ECO:0000269|PubMed:16257963, ECO:0000269|PubMed:16472662, ECO:0000269|PubMed:17038317, ECO:0000269|PubMed:18262180, ECO:0000269|PubMed:18435854, ECO:0000269|PubMed:19815557, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:20383201}.; . TISSUE SPECIFICITY: The Tyr-284 phosphorylated form shows a significant increase in expression in breast cancers during the progressive stages i.e. normal to hyperplasia (ADH), ductal carcinoma in situ (DCIS), invasive ductal carcinoma (IDC) and lymph node metastatic (LNMM) stages. It also shows a significant increase in expression in prostate cancers during the progressive stages. {ECO:0000269|PubMed:16247015, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:20623637}.; ovary;sympathetic chain;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;oesophagus;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;blood;lens;pancreas;lung;placenta;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; amygdala;medulla oblongata;thalamus;occipital lobe;superior cervical ganglion;hypothalamus;temporal lobe;caudate nucleus;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.41233 0.42322 -0.718391565 14.28402925 759.94336 5.46328 TNK2-AS1 . . . TNK2 antisense RNA 1 . . . . . . . . . . . TNKS 0.777115954184058 0.222884041292122 4.52381986699742e-09 tankyrase FUNCTION: Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1. Stimulates 26S proteasome activity. {ECO:0000269|PubMed:10988299, ECO:0000269|PubMed:11739745, ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:19759537, ECO:0000269|PubMed:21478859, ECO:0000269|PubMed:22864114, ECO:0000269|PubMed:23622245}.; . TISSUE SPECIFICITY: Ubiquitous; highest levels in testis.; ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;bone;iris;testis;germinal center;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;small intestine;heart;lacrimal gland;cerebellum cortex;islets of Langerhans;spinal cord;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; amygdala;dorsal root ganglion;medulla oblongata;thalamus;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;atrioventricular node;skin;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.74052 0.15224 -2.45481381 1.008492569 80.76873 1.89852 TNKS1BP1 0.0297108798308007 0.970285547090002 3.57307919736198e-06 tankyrase 1 binding protein 1 . . TISSUE SPECIFICITY: Detected in testis, ovary, lung, skeletal muscle, heart, prostate and pancreas, and at very low levels in brain and peripheral blood leukocytes.; ovary;sympathetic chain;colon;parathyroid;choroid;skin;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;bone;thyroid;iris;testis;brain;unclassifiable (Anatomical System);cartilage;lacrimal gland;tongue;islets of Langerhans;muscle;adrenal cortex;colorectal;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;duodenum;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.31646 0.09844 1.91638269 97.43453645 1715.46291 7.63566 TNKS2 0.733760224283182 0.266239768142663 7.57415448763373e-09 tankyrase 2 FUNCTION: Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP- ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. Stimulates 26S proteasome activity. {ECO:0000269|PubMed:11739745, ECO:0000269|PubMed:11802774, ECO:0000269|PubMed:19759537, ECO:0000269|PubMed:21478859, ECO:0000269|PubMed:23622245}.; . TISSUE SPECIFICITY: Highly expressed in placenta, skeletal muscle, liver, brain, kidney, heart, thymus, spinal cord, lung, peripheral blood leukocytes, pancreas, lymph nodes, spleen, prostate, testis, ovary, small intestine, colon, mammary gland, breast and breast carcinoma, and in common-type meningioma. Highly expressed in fetal liver, heart and brain.; . . 0.63340 0.12466 -1.285933373 5.083746167 119.88786 2.38554 TNKS2-AS1 . . . TNKS2 antisense RNA 1 (head to head) . . . . . . . . . . . TNMD 0.816440948853997 0.182635821035545 0.000923230110458692 tenomodulin FUNCTION: May be an angiogenesis inhibitor.; . TISSUE SPECIFICITY: Highly expressed in hypovascular connective tissues such as tendons. Has also strong expression in adipose tissue. {ECO:0000269|PubMed:19602561, ECO:0000269|PubMed:19780194, ECO:0000269|PubMed:22700804}.; . . 0.51044 0.20997 -0.05129383 49.75819769 34.34833 1.05046 TNN 5.19247511001232e-15 0.50671509615142 0.493284903848575 tenascin N FUNCTION: Involved in neurite outgrowth and cell migration in hippocampal explants. {ECO:0000250|UniProtKB:Q80Z71}.; . . heart;ovary;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;whole body;placenta;macula lutea;visual apparatus;mammary gland; superior cervical ganglion;trigeminal ganglion; 0.17043 . 1.51017302 95.42934654 5625.2664 15.52544 TNNC1 0.510486367884133 0.471277143904069 0.0182364882117977 troponin C1, slow skeletal and cardiac type FUNCTION: Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.; DISEASE: Cardiomyopathy, familial hypertrophic 13 (CMH13) [MIM:613243]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:11385718, ECO:0000269|PubMed:18572189}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;fovea centralis;choroid;retina;prostate;optic nerve;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;heart;tongue;pineal body;muscle;lens;skeletal muscle;greater omentum;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;stomach; heart;tongue;thyroid;testis;skeletal muscle; 0.09699 0.23627 -0.185391282 39.67916962 4.77604 0.17351 TNNC2 0.547150267315584 0.438964518402715 0.0138852142817008 troponin C2, fast skeletal type FUNCTION: Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.; . . . . 0.15208 0.27035 -0.009020804 52.8544468 . . TNNI1 0.120125044584648 0.854476692614279 0.0253982628010728 troponin I1, slow skeletal type FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.; . TISSUE SPECIFICITY: Highest levels observed in human skeletal muscle (e.g. gastrocnemious muscle), differentiated cultures of primary human muscle cells and rhabdomyosarcoma cells cultured in low serum medium. Expressed in C2 muscle cell myoblasts and myotubes. {ECO:0000269|PubMed:2365354, ECO:0000269|PubMed:8144655}.; unclassifiable (Anatomical System);ovary;heart;tongue;muscle;developmental;colon;skeletal muscle;greater omentum;prostate;lung;thyroid;alveolus;liver;testis;kidney;brain;bladder;peripheral nerve; tongue;thyroid;skeletal muscle; 0.18516 0.19240 0.237127192 68.98443029 44.33986 1.27180 TNNI2 0.0861527411924089 0.870962568699162 0.0428846901084294 troponin I2, fast skeletal type FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.; DISEASE: Arthrogryposis, distal, 2B (DA2B) [MIM:601680]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA2B is characterized by contractures of the hands and feet, and a distinctive face characterized by prominent nasolabial folds, small mouth and downslanting palpebral fissures. {ECO:0000269|PubMed:12592607}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;tongue;muscle;skeletal muscle;pancreas;lung;placenta;bone;visual apparatus;alveolus;hypopharynx;head and neck;kidney; tongue;thyroid;atrioventricular node;fetal thyroid;skeletal muscle; 0.19051 0.18219 -0.295622497 32.61972163 4.52947 0.16382 TNNI3 0.171895313040915 0.814590936344473 0.0135137506146117 troponin I3, cardiac type FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.; DISEASE: Cardiomyopathy, familial hypertrophic 7 (CMH7) [MIM:613690]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:11815426, ECO:0000269|PubMed:12707239, ECO:0000269|PubMed:12974739, ECO:0000269|PubMed:16199542, ECO:0000269|PubMed:9241277}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, familial restrictive 1 (RCM1) [MIM:115210]: A heart disorder characterized by impaired filling of the ventricles with reduced diastolic volume, in the presence of normal or near normal wall thickness and systolic function. {ECO:0000269|PubMed:12531876}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 2A (CMD2A) [MIM:611880]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:15070570}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1FF (CMD1FF) [MIM:613286]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:19590045, ECO:0000269|PubMed:21846512}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);myocardium;heart;ovary;colon;parathyroid;skin;uterus;pancreas;whole body;lung;placenta;liver;testis;thymus; heart;atrioventricular node; 0.62455 0.38244 0.147123112 64.11299835 34.66786 1.05726 TNNI3K 1.80292277016875e-38 1.33115114529519e-07 0.999999866884886 TNNI3 interacting kinase FUNCTION: May play a role in cardiac physiology. {ECO:0000303|PubMed:12721663}.; DISEASE: Cardiac conduction disease with or without dilated cardiomyopathy (CCDD) [MIM:616117]: A cardiac disorder characterized by atrial tachyarrhythmia and conduction system disease. Some patients have dilated cardiomyopathy. {ECO:0000269|PubMed:24925317}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in both adult and fetal heart. {ECO:0000269|PubMed:12721663}.; . . . 0.10778 -0.347208386 29.59424393 . . TNNT1 3.23490592341077e-06 0.553610820097729 0.446385944996348 troponin T1, slow skeletal type FUNCTION: Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.; DISEASE: Nemaline myopathy 5 (NEM5) [MIM:605355]: A form of nemaline myopathy. Nemaline myopathies are muscular disorders characterized by muscle weakness of varying severity and onset, and abnormal thread-like or rod-shaped structures in muscle fibers on histologic examination. Nemaline myopathy type 5 is a severe and progressive form common among Old Order Amish. Affected infants display tremors with hypotonia and mild contractures of the shoulders and hips. Proximal contractures progressively weaken and a pectus carinatum deformity develops before children die of respiratory insufficiency, usually in the second year. {ECO:0000269|PubMed:10952871}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;bone;testis;unclassifiable (Anatomical System);tongue;oral cavity;muscle;lens;skeletal muscle;bile duct;greater omentum;pancreas;lung;visual apparatus;macula lutea;liver;head and neck;kidney;mammary gland; prostate;thalamus;tongue;thyroid;fetal thyroid;skeletal muscle; 0.68138 0.20944 -0.095386216 46.48502005 249.24866 3.40230 TNNT2 0.01285284006076 0.98565465611574 0.00149250382349972 troponin T2, cardiac type FUNCTION: Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.; DISEASE: Cardiomyopathy, familial hypertrophic 2 (CMH2) [MIM:115195]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:10525521, ECO:0000269|PubMed:11034944, ECO:0000269|PubMed:12707239, ECO:0000269|PubMed:12974739, ECO:0000269|PubMed:15563892, ECO:0000269|PubMed:16199542, ECO:0000269|PubMed:21846512, ECO:0000269|PubMed:7898523, ECO:0000269|PubMed:8205619, ECO:0000269|PubMed:8989109, ECO:0000269|PubMed:9060892, ECO:0000269|PubMed:9140840, ECO:0000269|PubMed:9482583, ECO:0000269|Ref.19}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1D (CMD1D) [MIM:601494]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:11106718, ECO:0000269|PubMed:11684629, ECO:0000269|PubMed:15542288, ECO:0000269|PubMed:15769782, ECO:0000269|PubMed:21846512}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, familial restrictive 3 (RCM3) [MIM:612422]: A heart disorder characterized by impaired filling of the ventricles with reduced diastolic volume, in the presence of normal or near normal wall thickness and systolic function. {ECO:0000269|PubMed:16651346}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Heart. The fetal heart shows a greater expression in the atrium than in the ventricle, while the adult heart shows a greater expression in the ventricle than in the atrium. Isoform 6 predominates in normal adult heart. Isoforms 1, 7 and 8 are expressed in fetal heart. Isoform 7 is also expressed in failing adult heart.; unclassifiable (Anatomical System);myocardium;lung;atrium;whole body;cartilage;heart;placenta;adrenal medulla;blood;kidney;brain;bone marrow; superior cervical ganglion;heart; 0.25191 0.43689 -0.161524709 41.6430762 731.13972 5.36976 TNNT3 0.00472931950180961 0.98894827965205 0.00632240084614003 troponin T3, fast skeletal type FUNCTION: Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.; . TISSUE SPECIFICITY: In fetal and adult fast skeletal muscles, with a higher level expression in fetal than in adult muscle.; myocardium;heart;muscle;skin;skeletal muscle;uterus;pancreas;prostate;whole body;lung;larynx;placenta;visual apparatus;hypopharynx;testis;head and neck;kidney; . 0.30708 0.15743 -0.405853867 26.23260203 12.29412 0.44531 TNP1 0.222164609123562 0.647356502069908 0.13047888880653 transition protein 1 FUNCTION: In the elongating spermatids of mammals, the conversion of nucleosomal chromatin to the compact, non-nucleosomal form found in the sperm nucleus is associated with the appearance of a small set of basic chromosomal transition proteins.; . TISSUE SPECIFICITY: Expressed by spermatids (at protein level). {ECO:0000269|PubMed:9809674}.; unclassifiable (Anatomical System);medulla oblongata;placenta;testis;kidney;brain; testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.70740 . -0.009020804 52.8544468 6.60982 0.24458 TNP2 0.0439713399621792 0.666214119597725 0.289814540440096 transition protein 2 (during histone to protamine replacement) FUNCTION: In the elongating spermatids of mammals, the conversion of nucleosomal chromatin to the compact, non-nucleosomal form found in the sperm nucleus is associated with the appearance of a small set of basic chromosomal transition proteins.; . TISSUE SPECIFICITY: Expressed by spermatids (at protein level). {ECO:0000269|PubMed:9809674}.; lung;testis; testis - interstitial;superior cervical ganglion;testis;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.59005 0.10649 0.549415813 81.38122199 1241.93365 6.65292 TNPO1 0.999998700726593 1.29927340572571e-06 9.84896444796015e-16 transportin 1 FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Involved in nuclear import of M9- containing proteins. In vitro, binds directly to the M9 region of the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and mediates their nuclear import. Appears also to be involved in hnRNP A1/A2 nuclear export. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones, and SRP19. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Mediates nuclear import of ADAR/ADAR1 (isoform 5) in a RanGTP-dependent manner. {ECO:0000250, ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:19124606, ECO:0000269|PubMed:8986607, ECO:0000269|PubMed:9687515}.; . . ovary;salivary gland;colon;parathyroid;vein;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;lung;adrenal gland;epididymis;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; amygdala;superior cervical ganglion;testis - interstitial;olfactory bulb;pons;atrioventricular node;fetal thyroid;skeletal muscle;prostate;fetal brain;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;trigeminal ganglion;pituitary; 0.97077 0.18297 -0.780646273 12.77423921 36.30496 1.08710 TNPO1P1 . . . transportin 1 pseudogene 1 . . . . . . . . . . . TNPO1P2 . . . transportin 1 pseudogene 2 . . . . . . . . . . . TNPO1P3 . . . transportin 1 pseudogene 3 . . . . . . . . . . . TNPO2 0.999885944036715 0.000114055952486062 1.0799022271695e-11 transportin 2 FUNCTION: Probably functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;heart;tongue;colon;blood;skeletal muscle;bone marrow;breast;prostate;lung;epididymis;larynx;thyroid;visual apparatus;liver;testis;head and neck;spleen;kidney;brain;mammary gland;cerebellum; amygdala;whole brain;occipital lobe;testis - interstitial;medulla oblongata;superior cervical ganglion;cerebellum peduncles;temporal lobe;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.53292 0.11262 -0.933156985 9.54824251 84.11685 1.95249 TNPO3 0.00138920147813071 0.99861027646799 5.22053879292922e-07 transportin 3 FUNCTION: Seems to function in nuclear protein import as nuclear transport receptor. In vitro, mediates the nuclear import of splicing factor SR proteins RBM4, SFRS1 and SFRS2, by recognizing phosphorylated RS domains. {ECO:0000269|PubMed:10366588, ECO:0000269|PubMed:10713112, ECO:0000269|PubMed:11517331, ECO:0000269|PubMed:12628928}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle. {ECO:0000269|PubMed:23667635}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;medulla oblongata;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.60813 0.11436 -1.177506449 5.944798301 39.14188 1.16045 TNR 0.987762731547826 0.0122372684494463 2.7279367829811e-12 tenascin R FUNCTION: Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. These interactions can influence cellular behavior by either evoking a stable adhesion and differentiation, or repulsion and inhibition of neurite growth. Binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion and results in an inhibition of PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to membrane surface sulfatides results in a oligodendrocyte adhesion and differentiation. Interaction with CNTN1 induces a repulsion of neurons and an inhibition of neurite outgrowth. Interacts with SCN2B may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier. TNR-linked chondroitin sulfate glycosaminoglycans are involved in the interaction with FN1 and mediate inhibition of cell adhesion and neurite outgrowth. The highly regulated addition of sulfated carbohydrate structure may modulate the adhesive properties of TNR over the course of development and during synapse maintenance (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Brain specific. {ECO:0000269|PubMed:8626505}.; unclassifiable (Anatomical System);frontal lobe;placenta;brain; dorsal root ganglion;superior cervical ganglion;medulla oblongata;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14000 0.37292 -0.540190972 20.0401038 437.86343 4.36290 TNR-IT1 . . . TNR intronic transcript 1 . . . . . . . . . . . TNRC6A 0.999999927980856 7.20191440612564e-08 1.43793319232202e-21 trinucleotide repeat containing 6A FUNCTION: Plays a role in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs (siRNAs). Required for miRNA-dependent repression of translation and for siRNA- dependent endonucleolytic cleavage of complementary mRNAs by argonaute family proteins. As scaffoldng protein associates with argonaute proteins bound to partially complementary mRNAs and simultaneously can recruit CCR4-NOT and PAN deadenylase complexes. {ECO:0000269|PubMed:16284622, ECO:0000269|PubMed:16284623, ECO:0000269|PubMed:17596515, ECO:0000269|PubMed:17671087, ECO:0000269|PubMed:19056672, ECO:0000269|PubMed:19304925}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11950943}.; myocardium;ovary;colon;fovea centralis;choroid;retina;prostate;optic nerve;frontal lobe;larynx;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;lens;bile duct;breast;lung;placenta;macula lutea;liver;hypopharynx;spleen;head and neck;cervix;aorta;peripheral nerve; amygdala;dorsal root ganglion;testis - interstitial;subthalamic nucleus;superior cervical ganglion;prefrontal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11947 0.11385 -1.023482298 7.879216796 4749.21825 13.93697 TNRC6B 0.999999802750713 1.97249286937328e-07 4.08691571681075e-19 trinucleotide repeat containing 6B FUNCTION: Plays a role in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs (siRNAs). Required for miRNA-dependent translational repression and siRNA-dependent endonucleolytic cleavage of complementary mRNAs by argonaute family proteins. As scaffoldng protein associates with argonaute proteins bound to partially complementary mRNAs and simultaneously can recruit CCR4-NOT and PAN deadenylase complexes. {ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:19167051, ECO:0000269|PubMed:19304925, ECO:0000269|PubMed:21981923}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;pharynx;colorectal;blood;lens;bile duct;breast;lung;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; testis - seminiferous tubule;prefrontal cortex;testis; 0.51840 0.11889 -1.807947733 2.199811276 2219.15225 8.67424 TNRC6C 0.999997823984353 2.17601564600397e-06 6.99864929419351e-16 trinucleotide repeat containing 6C FUNCTION: Plays a role in RNA-mediated gene silencing by micro- RNAs (miRNAs). Required for miRNA-dependent translational repression of complementary mRNAs by argonaute family proteins. As scaffoldng protein associates with argonaute proteins bound to partially complementary mRNAs and simultaneously can recruit CCR4- NOT and PAN deadenylase complexes. {ECO:0000269|PubMed:19304925, ECO:0000269|PubMed:21981923, ECO:0000269|PubMed:21984184, ECO:0000269|PubMed:21984185}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;larynx;bone;testis;germinal center;spinal ganglion;pineal gland;brain;unclassifiable (Anatomical System);heart;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;head and neck;kidney;mammary gland;cerebellum; superior cervical ganglion;skeletal muscle;parietal lobe; 0.32049 0.10248 -1.537897124 3.338051427 1348.87379 6.89482 TNRC6C-AS1 . . . TNRC6C antisense RNA 1 . . . . . . . . . . . TNRC17 . . . trinucleotide repeat containing 17 . . . . . . . . . . . TNRC18 0.999973965663352 2.60343366358186e-05 1.20991240775877e-14 trinucleotide repeat containing 18 . . . colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;optic nerve;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;lung;placenta;macula lutea;liver;cervix;spleen;stomach; dorsal root ganglion;subthalamic nucleus;thalamus;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; . . . . 6309.78902 16.61915 TNRC18P1 . . . trinucleotide repeat containing 18 pseudogene 1 . . . . . . . . . . . TNRC18P2 . . . trinucleotide repeat containing 18 pseudogene 2 . . . . . . . . . . . TNRC18P3 . . . trinucleotide repeat containing 18 pseudogene 3 . . . . . . . . . . . TNS1 0.924939888851989 0.0750601110976995 5.03112984593829e-11 tensin 1 FUNCTION: Involved in fibrillar adhesion formation. May be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. {ECO:0000269|PubMed:21768292}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11023826}.; colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.49253 0.15564 1.585596299 95.81269167 8076.56687 19.41076 TNS2 . . . tensin 2 FUNCTION: Regulates cell motility and proliferation. May have phosphatase activity. Reduces AKT1 phosphorylation. Lowers AKT1 kinase activity and interferes with AKT1 signaling. {ECO:0000269|PubMed:15817639}.; . TISSUE SPECIFICITY: Detected in heart, kidney, brain, thymus, spleen, liver, placenta, lung, skeletal muscle and small intestine. {ECO:0000269|PubMed:11792844, ECO:0000269|PubMed:12470648}.; . . 0.21392 0.16317 -1.313764723 4.824251003 . . TNS3 0.999389290859683 0.000610709139238235 1.07916562262031e-12 tensin 3 FUNCTION: May play a role in actin remodeling. Involved in the dissociation of the integrin-tensin-actin complex. EGF activates TNS4 and down-regulates TNS3 which results in capping the tail of ITGB1. Seems to be involved in mammary cell migration. May be involved in cell migration and bone development (By similarity). {ECO:0000250, ECO:0000269|PubMed:17643115}.; . TISSUE SPECIFICITY: Expressed in umbilical vein endothelial cells, epithelial cells, and fibroblasts cells (at protein level). Highly expressed in thyroid, kidney and placenta. Low expression in heart, skeletal muscle, spleen, liver, and lung. Expressed in tumor endothelial cells. Expression seems to be down-regulated in thyroid tumor tissues and in anaplastic carcinomas. {ECO:0000269|PubMed:11559528, ECO:0000269|PubMed:15140944, ECO:0000269|PubMed:16461921}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;nervous;pharynx;blood;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;dura mater;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);meninges;islets of Langerhans;muscle;pancreas;lung;pia mater;placenta;hippocampus;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;placenta;globus pallidus;ciliary ganglion;atrioventricular node; 0.29297 0.14134 0.132151962 63.36400094 726.40943 5.35297 TNS4 0.000130733468322774 0.997996452023443 0.00187281450823397 tensin 4 FUNCTION: May be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton (By similarity). May promote apoptosis, via its cleavage by caspase-3. {ECO:0000250}.; . TISSUE SPECIFICITY: Prostate and placenta. Down regulated in prostate cancer. {ECO:0000269|PubMed:12154022}.; unclassifiable (Anatomical System);tongue;colon;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;breast;pancreas;prostate;optic nerve;lung;larynx;thyroid;placenta;macula lutea;head and neck;bladder;stomach; dorsal root ganglion;ciliary ganglion;atrioventricular node;pons; 0.08569 0.10973 -0.24061166 36.28214201 2886.90526 10.17860 TNXA . . . tenascin XA (pseudogene) . . TISSUE SPECIFICITY: Expressed in the adrenal gland. {ECO:0000269|PubMed:1373808}.; . . . . . . . . TNXB 0.774153751864359 0.224204134128029 0.00164211400761226 tenascin XB FUNCTION: Appears to mediate interactions between cells and the extracellular matrix. Substrate-adhesion molecule that appears to inhibit cell migration. Accelerates collagen fibril formation. May play a role in supporting the growth of epithelial tumors. {ECO:0000269|PubMed:17033827}.; DISEASE: Ehlers-Danlos syndrome due to tenascin X deficiency (EDSTNXD) [MIM:606408]: An Ehlers-Danlos-like syndrome characterized by hyperextensible skin, hypermobile joints, and tissue fragility. Tenascin-X-deficient patients, however, lack atrophic scars, a major diagnostic criteria for classic Ehlers- Danlos. Delayed wound healing, which is also common in classic EDS, is only present in a subset of patients. {ECO:0000269|PubMed:23768946}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Vesicoureteral reflux 8 (VUR8) [MIM:615963]: A disease belonging to the group of congenital anomalies of the kidney and urinary tract. It is characterized by the reflux of urine from the bladder into the ureters and sometimes into the kidneys, and is a risk factor for urinary tract infections. Primary disease results from a developmental defect of the ureterovesical junction. In combination with intrarenal reflux, the resulting inflammatory reaction may result in renal injury or scarring, also called reflux nephropathy. Extensive renal scarring impairs renal function and may predispose patients to hypertension, proteinuria, renal insufficiency and end-stage renal disease. {ECO:0000269|PubMed:23620400}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in fetal adrenal, in fetal testis, fetal smooth, striated and cardiac muscle. Isoform XB- short is only expressed in the adrenal gland.; . . 0.19814 . . . 17910.3323 28.28926 TOB1 0.798204384419713 0.196185003099571 0.00561061248071624 transducer of ERBB2, 1 FUNCTION: Anti-proliferative protein; the function is mediated by association with deadenylase subunits of the CCR4-NOT complex. {ECO:0000269|PubMed:23236473, ECO:0000269|PubMed:8632892}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;rectum;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;small intestine;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;mammary gland;stomach;cerebellum; adrenal gland;adrenal cortex;liver; 0.78741 0.22085 -0.271755481 34.31823543 36.86645 1.10425 TOB1-AS1 . . . TOB1 antisense RNA 1 . . . . . . . . . . . TOB2 0.703190337105161 0.280702877407559 0.0161067854872804 transducer of ERBB2, 2 FUNCTION: Anti-proliferative protein inhibits cell cycle progression from the G0/G1 to S phases.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;lung;placenta;hippocampus;kidney;stomach;thymus;cerebellum; olfactory bulb;adrenal cortex;prefrontal cortex;ciliary ganglion;atrioventricular node;skeletal muscle;cerebellum; 0.38171 0.15977 -0.580403979 18.58928993 50.06768 1.38883 TOB2P1 . . . transducer of ERBB2, 2 pseudogene 1 . . . . . . . . . . . TOE1 6.58751882854325e-09 0.245456543957308 0.754543449455173 target of EGR1, member 1 (nuclear) FUNCTION: Inhibits cell growth rate and cell cycle. Induces CDKN1A expression as well as TGF-beta expression. Mediates the inhibitory growth effect of EGR1. {ECO:0000269|PubMed:12562764}.; . . . . 0.08101 0.10053 -0.268115223 34.70747818 261.02858 3.46891 TOLLIP 0.52290626801214 0.473487995741708 0.00360573624615221 toll interacting protein FUNCTION: Component of the signaling pathway of IL-1 and Toll-like receptors. Inhibits cell activation by microbial products. Recruits IRAK1 to the IL-1 receptor complex. Inhibits IRAK1 phosphorylation and kinase activity (PubMed:11751856). Connects the ubiquitin pathway to autophagy by functioning as a ubiquitin- ATG8 family adapter and thus mediating autophagic clearance of ubiquitin conjugates. The TOLLIP-dependent selective autophagy pathway plays an important role in clearance of cytotoxic polyQ proteins aggregates (PubMed:25042851). {ECO:0000269|PubMed:11751856, ECO:0000269|PubMed:25042851}.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pineal body;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach;aorta; amygdala;testis; 0.16248 0.14352 -0.468351206 23.42533616 235.45459 3.31615 TOLLIP-AS1 . . . TOLLIP antisense RNA 1 (head to head) . . . . . . . . . . . TOM1 6.77746945347432e-06 0.97491313716746 0.0250800853630862 target of myb1 membrane trafficking protein FUNCTION: May be involved in intracellular trafficking. Probable association with membranes.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in skeletal muscle, heart, placenta and liver. {ECO:0000269|PubMed:10329004}.; smooth muscle;ovary;colon;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;small intestine;heart;islets of Langerhans;hypothalamus;muscle;urinary;blood;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.25337 0.13124 -0.554717505 19.79830149 1589.92055 7.37684 TOM1L1 0.00293414695871849 0.994492150010132 0.00257370303114969 target of myb1 like 1 membrane trafficking protein FUNCTION: Probable adapter protein involved in signaling pathways. Interacts with the SH2 and SH3 domains of various signaling proteins when it is phosphorylated. May promote FYN activation, possibly by disrupting intramolecular SH3-dependent interactions (By similarity). {ECO:0000250}.; . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;atrium;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion; 0.20880 0.09376 -0.690637458 15.12149092 105.96155 2.23139 TOM1L2 0.414475507742354 0.585510337059161 1.41551984841728e-05 target of myb1 like 2 membrane trafficking protein FUNCTION: Probable role in protein transport. May regulate growth factor-induced mitogenic signaling. {ECO:0000269|PubMed:16412388, ECO:0000269|PubMed:16479011}.; . TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in heart and skeletal muscle. {ECO:0000269|PubMed:11997338}.; unclassifiable (Anatomical System);islets of Langerhans;colon;skeletal muscle;retina;lung;larynx;thyroid;bone;visual apparatus;iris;liver;testis;head and neck;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion; 0.19763 0.11625 -1.155457828 6.168907761 18.6274 0.64390 TOMM5 0.588881590096298 0.370313112800163 0.0408052971035379 translocase of outer mitochondrial membrane 5 . . . ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; . 0.20456 0.08194 0.235309407 68.71903751 36.31961 1.08824 TOMM6 . . . translocase of outer mitochondrial membrane 6 . . . . . . . 0.167351552 65.04482189 5.14636 0.19135 TOMM7 0.0547352976629651 0.703563286130634 0.241701416206401 translocase of outer mitochondrial membrane 7 FUNCTION: Required for assembly and stability of the TOM complex. Positive regulator of PARK2 translocation to damaged mitochondria. Acts probably by stabilizing PINK1 on the outer membrane of depolarized mitochondria. {ECO:0000269|PubMed:18331822, ECO:0000269|PubMed:24270810}.; . . myocardium;lymphoreticular;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;tonsil;amygdala;heart;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;cerebral cortex;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;kidney;stomach;aorta; olfactory bulb;hypothalamus;caudate nucleus;skeletal muscle; 0.09020 . -0.009020804 52.8544468 9.34865 0.34366 TOMM20 0.577780758415904 0.419887532043709 0.00233170954038713 translocase of outer mitochondrial membrane 20 FUNCTION: Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore (By similarity). {ECO:0000250}.; . . . . 0.30455 0.11931 0.079165051 59.43029016 . . TOMM20L 0.000787655427739962 0.538507208362171 0.460705136210089 translocase of outer mitochondrial membrane 20 like . . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;whole body;lung;cochlea;bone;placenta;macula lutea;hippocampus;testis;kidney;brain;pineal gland;stomach; . . 0.06144 0.479642105 78.95140363 23.84149 0.78631 TOMM20P1 . . . TOMM20 pseudogene 1 . . . . . . . . . . . TOMM20P2 . . . TOMM20 pseudogene 2 . . . . . . . . . . . TOMM20P3 . . . TOMM20 pseudogene 3 . . . . . . . . . . . TOMM20P4 . . . TOMM20 pseudogene 4 . . . . . . . . . . . TOMM22 0.785832960017485 0.207583008798231 0.00658403118428444 translocase of outer mitochondrial membrane 22 FUNCTION: Central receptor component of the translocase of the outer membrane of mitochondria (TOM complex) responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with the peripheral receptor TOM20 functions as the transit peptide receptor and facilitates the movement of preproteins into the translocation pore. {ECO:0000269|PubMed:10982837}.; . TISSUE SPECIFICITY: Ubiquitous.; medulla oblongata;ovary;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion; 0.19906 0.14229 -0.119252484 44.53880632 5.7075 0.21391 TOMM22P1 . . . TOMM22 pseudogene 1 . . . . . . . . . . . TOMM22P2 . . . TOMM22 pseudogene 2 . . . . . . . . . . . TOMM22P3 . . . TOMM22 pseudogene 3 . . . . . . . . . . . TOMM22P4 . . . TOMM22 pseudogene 4 . . . . . . . . . . . TOMM22P5 . . . TOMM22 pseudogene 5 . . . . . . . . . . . TOMM22P6 . . . TOMM22 pseudogene 6 . . . . . . . . . . . TOMM34 0.721089132713427 0.27828802536025 0.000622841926323846 translocase of outer mitochondrial membrane 34 FUNCTION: Plays a role in the import of cytosolically synthesized preproteins into mitochondria. Binds the mature portion of precursor proteins. Interacts with cellular components, and possesses weak ATPase activity. May be a chaperone-like protein that helps to keep newly synthesized precursors in an unfolded import compatible state. {ECO:0000269|PubMed:10101285, ECO:0000269|PubMed:11913975, ECO:0000269|PubMed:9324309}.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.04051 0.09048 -0.383807564 27.41802312 7.17059 0.26979 TOMM40 0.963682323765023 0.0362476712430565 7.00049919200433e-05 translocase of outer mitochondrial membrane 40 FUNCTION: Channel-forming protein essential for import of protein precursors into mitochondria. {ECO:0000250, ECO:0000269|PubMed:15644312}.; . . medulla oblongata;ovary;salivary gland;colon;skin;uterus;prostate;optic nerve;endometrium;thyroid;bone;iris;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;adrenal cortex;globus pallidus;ciliary ganglion;atrioventricular node;pons;kidney;trigeminal ganglion;skeletal muscle;cerebellum; 0.74085 0.13230 -0.337894035 30.37272942 30.68058 0.97616 TOMM40L 0.744035828405772 0.255480683819257 0.000483487774971119 translocase of outer mitochondrial membrane 40 like FUNCTION: Potential channel-forming protein implicated in import of protein precursors into mitochondria. {ECO:0000250}.; . . . . 0.47199 0.10917 -0.095386216 46.48502005 26.59526 0.86147 TOMM70 . . . translocase of outer mitochondrial membrane 70 FUNCTION: Receptor that accelerates the import of all mitochondrial precursor proteins. {ECO:0000250}.; . . . . 0.49176 0.13021 -0.449946534 24.00330267 . . TONSL 6.06324987077416e-05 0.999892390451107 4.69770501848968e-05 tonsoku-like, DNA repair protein FUNCTION: Component of the MMS22L-TONSL complex, a complex that stimulates the recombination-dependent repair of stalled or collapsed replication forks. The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication by promoting homologous recombination-mediated repair of replication fork- associated double-strand breaks. It may act by mediating the assembly of RAD51 filaments on ssDNA. Within the complex, may act as a scaffold. {ECO:0000269|PubMed:21055983, ECO:0000269|PubMed:21055984, ECO:0000269|PubMed:21055985, ECO:0000269|PubMed:7738005}.; . TISSUE SPECIFICITY: Expressed in heart, skeletal muscle and tracheal epithelial cells. {ECO:0000269|PubMed:7738005}.; . . 0.11669 0.25689 -0.40608828 25.86694975 6834.88962 17.59846 TONSL-AS1 . . . TONSL antisense RNA 1 . . . . . . . . . . . TOP1 0.999999399962319 6.00037680884761e-07 1.50008509426593e-16 topoisomerase (DNA) I FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Involved in the circadian transcription of the core circadian clock component ARNTL/BMAL1 by altering the chromatin structure around the ROR response elements (ROREs) on the ARNTL/BMAL1 promoter. {ECO:0000250|UniProtKB:Q13472, ECO:0000269|PubMed:14594810, ECO:0000269|PubMed:16033260, ECO:0000269|PubMed:19168442, ECO:0000269|PubMed:22904072, ECO:0000269|PubMed:2833744}.; DISEASE: Note=A chromosomal aberration involving TOP1 is found in a form of therapy-related myelodysplastic syndrome. Translocation t(11;20)(p15;q11) with NUP98. {ECO:0000269|PubMed:10556215}.; TISSUE SPECIFICITY: Endothelial cells. {ECO:0000269|PubMed:19168442}.; lymphoreticular;ovary;sympathetic chain;skin;retina;prostate;optic nerve;cochlea;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;oral cavity;pancreas;lung;cornea;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta; fetal liver;tumor; 0.99589 0.80784 -0.381986487 27.68931352 57.44961 1.52769 TOP1MT 1.63072339882279e-19 0.00150019125145143 0.998499808748548 topoisomerase (DNA) I, mitochondrial FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during duplication of mitochondrial DNA by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). {ECO:0000250, ECO:0000269|PubMed:11526219}.; . TISSUE SPECIFICITY: Ubiquitous; highest in skeletal muscle, heart, brain and fetal liver. {ECO:0000269|PubMed:11526219}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;endometrium;thyroid;bone;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);blood;lens;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;testis; 0.18543 0.14812 -0.435396074 24.70511913 3501.83574 11.39955 TOP1P1 . . . topoisomerase (DNA) I pseudogene 1 . . . . . . . . . . . TOP1P2 . . . topoisomerase (DNA) I pseudogene 2 . . . . . . . . . . . TOP2A 0.996224029437404 0.00377597056183657 7.595454763075e-13 topoisomerase (DNA) II alpha FUNCTION: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes. May play a role in regulating the period length of ARNTL/BMAL1 transcriptional oscillation (By similarity). {ECO:0000250|UniProtKB:Q01320, ECO:0000269|PubMed:18790802, ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:22323612}.; . . ovary;salivary gland;developmental;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;muscle;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;alveolus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; fetal liver;testis - interstitial;testis - seminiferous tubule;tumor;testis; . 0.54452 0.492370491 79.60603916 383.30497 4.12860 TOP2B 0.99731109311551 0.00268890688285124 1.63912671881142e-12 topoisomerase (DNA) II beta FUNCTION: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. {ECO:0000269|PubMed:10684600}.; . . myocardium;ovary;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;visual apparatus;macula lutea;liver;mammary gland;salivary gland;intestine;colon;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;testis;artery;unclassifiable (Anatomical System);islets of Langerhans;bile duct;pancreas;lung;cornea;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus;cerebellum; amygdala;subthalamic nucleus;occipital lobe;medulla oblongata;fetal brain;hypothalamus;thyroid;prefrontal cortex;globus pallidus;caudate nucleus;parietal lobe;cingulate cortex; 0.99834 0.37504 -0.150608082 42.28001887 748.55499 5.42826 TOP3A 2.6363036582595e-08 0.998932967032806 0.00106700660415741 topoisomerase (DNA) III alpha FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity. {ECO:0000269|PubMed:20445207, ECO:0000269|PubMed:8622991}.; . TISSUE SPECIFICITY: High expression is found in testis, heart, skeletal muscle and pancreas.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;blood;lens;breast;lung;epididymis;placenta;macula lutea;liver;duodenum;cervix;kidney;stomach;cerebellum; subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;pons;parietal lobe;skeletal muscle;cerebellum; 0.56154 0.09390 0.299418187 71.70323189 1188.86307 6.53935 TOP3B 0.114528012617576 0.885422264492838 4.97228895861367e-05 topoisomerase (DNA) III beta FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Possesses negatively supercoiled DNA relaxing activity. {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is found in testis, heart and skeletal muscle. A 4 kb transcript which probably represents isoform 2 is found in thymus, kidney and pancreas. {ECO:0000269|PubMed:9927731}.; colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;head and neck;mammary gland;stomach;peripheral nerve;thymus; . 0.26767 0.25506 -0.484940685 22.75300778 1139.89599 6.43941 TOP3BP1 . . . topoisomerase (DNA) III beta pseudogene 1 . . . . . . . . . . . TOPAZ1 . . . testis and ovary specific PAZ domain containing 1 . . . . . . . 3.041223814 99.23330974 525.51619 4.67720 TOPBP1 0.999999933511461 6.64885384698568e-08 1.42869215278609e-19 topoisomerase (DNA) II binding protein 1 FUNCTION: Required for DNA replication. Plays a role in the rescue of stalled replication forks and checkpoint control. Binds double- stranded DNA breaks and nicks as well as single-stranded DNA. Recruits the SWI/SNF chromatin remodeling complex to E2F1- responsive promoters. Down-regulates E2F1 activity and inhibits E2F1-dependent apoptosis during G1/S transition and after DNA damage. Induces a large increase in the kinase activity of ATR. {ECO:0000269|PubMed:10498869, ECO:0000269|PubMed:11395493, ECO:0000269|PubMed:11714696, ECO:0000269|PubMed:12697828, ECO:0000269|PubMed:15075294, ECO:0000269|PubMed:16530042}.; . TISSUE SPECIFICITY: Highly expressed in heart, brain, placenta, lung and kidney. {ECO:0000269|PubMed:9461304}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;subthalamic nucleus;testis - interstitial;atrioventricular node; 0.51664 0.18217 -0.367438677 28.29087049 1231.90878 6.63344 TOPORS 0.975842586892896 0.0241573702120045 4.28950998301653e-08 topoisomerase I binding, arginine/serine-rich, E3 ubiquitin protein ligase FUNCTION: Functions as an E3 ubiquitin-protein ligase and as an E3 SUMO1-protein ligase. Probable tumor suppressor involved in cell growth, cell proliferation and apoptosis that regulates p53/TP53 stability through ubiquitin-dependent degradation. May regulate chromatin modification through sumoylation of several chromatin modification-associated proteins. May be involved in DNA damage- induced cell death through IKBKE sumoylation. {ECO:0000269|PubMed:15247280, ECO:0000269|PubMed:15735665, ECO:0000269|PubMed:16122737, ECO:0000269|PubMed:17803295, ECO:0000269|PubMed:18077445, ECO:0000269|PubMed:19473992, ECO:0000269|PubMed:20188669}.; DISEASE: Retinitis pigmentosa 31 (RP31) [MIM:609923]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:17924349}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at highest levels in testis and at lower levels in adrenal gland, bone marrow, brain, colon, heart, kidney, liver, muscle, ovary, pancreas, placenta, prostate, skeletal muscle, skin, small intestine, spleen, stomach, testis, thymus, thyroid and uterus. Expressed in the alveolar epithelium of the lung. Expression is commonly decreased in colon adenocarcinomas and lung cancers. {ECO:0000269|PubMed:10415337, ECO:0000269|PubMed:11278651, ECO:0000269|PubMed:15107820}.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;bone;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;lung;cornea;mesenchyma;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;globus pallidus;trigeminal ganglion;skeletal muscle; 0.23430 0.12464 0.027580343 55.8091531 274.14851 3.54660 TOPORS-AS1 . . . TOPORS antisense RNA 1 . . . . . . . . . . . TOPORSLP1 . . . topoisomerase I binding, arginine/serine-rich like, pseudogene 1 . . . . . . . . . . . TOR1A 0.16704849102676 0.818697702344535 0.0142538066287046 torsin family 1 member A FUNCTION: Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non- neural tissues. {ECO:0000269|PubMed:15505207, ECO:0000269|PubMed:16361107, ECO:0000269|PubMed:17428918, ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:19339278, ECO:0000269|PubMed:20169475, ECO:0000269|PubMed:23569223}.; DISEASE: Dystonia 1, torsion, autosomal dominant (DYT1) [MIM:128100]: A primary torsion dystonia, and the most common and severe form. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. Dystonia type 1 is characterized by involuntary, repetitive, sustained muscle contractions or postures involving one or more sites of the body, in the absence of other neurological symptoms. Typically, symptoms develop first in an arm or leg in middle to late childhood and progress in approximately 30% of patients to other body regions (generalized dystonia) within about five years. 'Torsion' refers to the twisting nature of body movements observed in DYT1, often affecting the trunk. Distribution and severity of symptoms vary widely between affected individuals, ranging from mild focal dystonia to severe generalized dystonia, even within families. {ECO:0000269|PubMed:18477710, ECO:0000269|PubMed:19955557, ECO:0000269|PubMed:9288096}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Highest levels in kidney and liver. In the brain, high levels found in the dopaminergic neurons of the substantia nigra pars compacta, as well as in the neocortex, hippocampus and cerebellum. Also highly expressed in the spinal cord. {ECO:0000269|PubMed:10640617, ECO:0000269|PubMed:14970196, ECO:0000269|PubMed:15147511}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;epidermis;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.68010 0.32836 -0.183570861 39.95046001 793.75138 5.55566 TOR1AIP1 0.0646147824983602 0.935255977007244 0.000129240494396058 torsin 1A interacting protein 1 FUNCTION: Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina. {ECO:0000269|PubMed:23569223}.; . . medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;germinal center;bladder;brain;gall bladder;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;testis;pons;trigeminal ganglion; 0.08213 0.07574 0.310540264 72.65864591 164.11702 2.79796 TOR1AIP2 4.03605255306865e-05 0.618667375136891 0.381292264337579 torsin 1A interacting protein 2 FUNCTION: Required for endoplasmic reticulum integrity. Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity. {ECO:0000269|PubMed:19339278, ECO:0000269|PubMed:23569223, ECO:0000269|PubMed:24275647}.; . . . . 0.07638 0.07713 -0.312207497 32.05944798 56.59802 1.51319 TOR1B 0.743694124428476 0.25394962265702 0.0023562529145046 torsin family 1 member B FUNCTION: May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins. Plays a role in non-neural cells nuclear envelope and endoplasmic reticulum integrity. May have a redundant function with TOR1A in non-neural tissues. {ECO:0000269|PubMed:23569223, ECO:0000269|PubMed:24275647}.; . TISSUE SPECIFICITY: Widely expressed with low levels in brain. {ECO:0000269|PubMed:15147511}.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;dura mater;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);meninges;cartilage;hypothalamus;adrenal cortex;lens;skeletal muscle;bile duct;pancreas;pia mater;lung;placenta;macula lutea;hippocampus;liver;alveolus;spleen;kidney;mammary gland;stomach; superior cervical ganglion;testis;trigeminal ganglion;skeletal muscle; 0.15539 0.15285 -0.60427181 17.74593064 54.26739 1.47124 TOR2A 0.0567475787024611 0.866190879199818 0.0770615420977212 torsin family 2 member A . . TISSUE SPECIFICITY: Isoform 1 is expressed ubiquitously, except in cardiac and endothelial tissues. {ECO:0000269|PubMed:12910263}.; ovary;salivary gland;intestine;colon;parathyroid;prostate;optic nerve;whole body;cerebral cortex;bone;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;stomach; . 0.12234 0.10743 0.595326758 82.66100495 153.54144 2.70963 TOR3A 2.47193997160645e-08 0.0810998928991405 0.91890008238146 torsin family 3 member A . . TISSUE SPECIFICITY: Ubiquitously expressed. Highest expression in stomach, salivary glands and lymph nodes. Isoform 2 is expressed in placenta. {ECO:0000269|PubMed:11863361}.; unclassifiable (Anatomical System);lymphoreticular;muscle;skin;pancreas;lung;placenta;bone;visual apparatus;amnion;spleen;kidney;brain;stomach; liver;trigeminal ganglion;skeletal muscle; 0.06192 0.09551 -0.490397599 22.50530786 76.75897 1.83877 TOR4A 0.215534135723215 0.647904223327794 0.136561640948992 torsin family 4 member A . . . . . 0.09004 0.12134 . . 186.39911 2.96480 TOX 0.892971024523591 0.106984330793395 4.46446830136686e-05 thymocyte selection associated high mobility group box FUNCTION: May play a role in regulating T-cell development. {ECO:0000250}.; . . developmental;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;lens;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;spleen;head and neck;kidney;stomach;thymus; superior cervical ganglion;trigeminal ganglion;thymus; 0.94527 0.20047 -0.622676946 17.30950696 265.75398 3.49664 TOX2 0.674075157439045 0.324924104468379 0.00100073809257587 TOX high mobility group box family member 2 FUNCTION: Putative transcriptional activator involved in the hypothalamo-pituitary-gonadal system.; . . unclassifiable (Anatomical System);islets of Langerhans;colon;blood;choroid;fovea centralis;lens;retina;prostate;pancreas;optic nerve;lung;placenta;macula lutea;testis;kidney;brain; testis;thymus; 0.54213 0.09044 -0.264476624 34.8844067 437.56112 4.36048 TOX3 0.99433910835596 0.00566016516316361 7.26480876584799e-07 TOX high mobility group box family member 3 FUNCTION: Transcriptional coactivator of the p300/CBP-mediated trancription complex. Activates transactivation through cAMP response element (CRE) sites. Protects against cell death by inducing antiapoptotic and repressing pro-apoptotic transcripts. Stimulates transcription from the estrogen-responsive or BCL-2 promoters. Required for depolarization-induced transcription activation of the C-FOS promoter in neurons. Associates with chromatin to the estrogen-responsive C3 promoter region. {ECO:0000269|PubMed:21172805}.; . TISSUE SPECIFICITY: Expressed mainly in epithelial cells. Expressed in the central nervous system (CNS), in the ileum and within the brain in the frontal and occipital lobe. {ECO:0000269|PubMed:21172805}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;breast;pancreas;prostate;lung;frontal lobe;cochlea;endometrium;alveolus;testis;kidney;brain;mammary gland;stomach;peripheral nerve; whole brain;amygdala;superior cervical ganglion;trachea;fetal brain;ciliary ganglion;trigeminal ganglion; 0.95535 . 0.332586472 73.61405992 678.61743 5.20767 TOX4 0.811965790149349 0.187993330365951 4.08794846995347e-05 TOX high mobility group box family member 4 FUNCTION: Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. {ECO:0000269|PubMed:20516061}.; . . medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;developmental;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;pia mater;nasopharynx;placenta;kidney;stomach; dorsal root ganglion;occipital lobe;superior cervical ganglion;medulla oblongata;atrioventricular node;pons;skeletal muscle;globus pallidus;testis;appendix;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.76756 0.11119 -0.359940251 28.93371078 41.34694 1.20857 TOX4P1 . . . TOX high mobility group box family member 4 pseudogene 1 . . . . . . . . . . . TP53 0.91222295333147 0.0877503280810861 2.6718587444359e-05 tumor protein p53 FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA- Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seem to have to effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1- mediated transcriptional activation of PER2 (PubMed:24051492). {ECO:0000269|PubMed:11025664, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:17317671, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:24051492, ECO:0000269|PubMed:9840937}.; DISEASE: Note=TP53 is found in increased amounts in a wide variety of transformed cells. TP53 is frequently mutated or inactivated in about 60% of cancers. TP53 defects are found in Barrett metaplasia a condition in which the normally stratified squamous epithelium of the lower esophagus is replaced by a metaplastic columnar epithelium. The condition develops as a complication in approximately 10% of patients with chronic gastroesophageal reflux disease and predisposes to the development of esophageal adenocarcinoma.; DISEASE: Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the esophagus. The most common types are esophageal squamous cell carcinoma and adenocarcinoma. Cancer of the esophagus remains a devastating disease because it is usually not detected until it has progressed to an advanced incurable stage. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Li-Fraumeni syndrome (LFS) [MIM:151623]: Autosomal dominant familial cancer syndrome that in its classic form is defined by the existence of a proband affected by a sarcoma before 45 years with a first degree relative affected by any tumor before 45 years and another first degree relative with any tumor before 45 years or a sarcoma at any age. Other clinical definitions for LFS have been proposed (PubMed:8118819 and PubMed:8718514) and called Li-Fraumeni like syndrome (LFL). In these families affected relatives develop a diverse set of malignancies at unusually early ages. Four types of cancers account for 80% of tumors occurring in TP53 germline mutation carriers: breast cancers, soft tissue and bone sarcomas, brain tumors (astrocytomas) and adrenocortical carcinomas. Less frequent tumors include choroid plexus carcinoma or papilloma before the age of 15, rhabdomyosarcoma before the age of 5, leukemia, Wilms tumor, malignant phyllodes tumor, colorectal and gastric cancers. {ECO:0000269|PubMed:10484981, ECO:0000269|PubMed:1565144, ECO:0000269|PubMed:1737852, ECO:0000269|PubMed:1933902, ECO:0000269|PubMed:1978757, ECO:0000269|PubMed:2259385, ECO:0000269|PubMed:7887414, ECO:0000269|PubMed:8825920, ECO:0000269|PubMed:9452042}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Squamous cell carcinoma of the head and neck (HNSCC) [MIM:275355]: A non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Papilloma of choroid plexus (CPP) [MIM:260500]: A benign tumor of neuroectodermal origin that generally occurs in childhood, but has also been reported in adults. Although generally found within the ventricular system, choroid plexus papillomas can arise ectopically in the brain parenchyma or disseminate throughout the neuraxis. Patients present with signs and symptoms of increased intracranial pressure including headache, hydrocephalus, papilledema, nausea, vomiting, cranial nerve deficits, gait impairment, and seizures. {ECO:0000269|PubMed:12085209}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Adrenocortical carcinoma (ADCC) [MIM:202300]: A malignant neoplasm of the adrenal cortex and a rare childhood tumor. It occurs with increased frequency in patients with Beckwith- Wiedemann syndrome and Li-Fraumeni syndrome. {ECO:0000269|PubMed:11481490}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Basal cell carcinoma 7 (BCC7) [MIM:614740]: A common malignant skin neoplasm that typically appears on hair-bearing skin, most commonly on sun-exposed areas. It is slow growing and rarely metastasizes, but has potentialities for local invasion and destruction. It usually develops as a flat, firm, pale area that is small, raised, pink or red, translucent, shiny, and waxy, and the area may bleed following minor injury. Tumor size can vary from a few millimeters to several centimeters in diameter. {ECO:0000269|PubMed:21946351}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Isoforms are expressed in a wide range of normal tissues but in a tissue-dependent manner. Isoform 2 is expressed in most normal tissues but is not detected in brain, lung, prostate, muscle, fetal brain, spinal cord and fetal liver. Isoform 3 is expressed in most normal tissues but is not detected in lung, spleen, testis, fetal brain, spinal cord and fetal liver. Isoform 7 is expressed in most normal tissues but is not detected in prostate, uterus, skeletal muscle and breast. Isoform 8 is detected only in colon, bone marrow, testis, fetal brain and intestine. Isoform 9 is expressed in most normal tissues but is not detected in brain, heart, lung, fetal liver, salivary gland, breast or intestine. {ECO:0000269|PubMed:16131611}.; lymphoreticular;ovary;colon;vein;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;blood;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;epididymis;placenta;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;placenta;white blood cells;atrioventricular node;skeletal muscle; 0.99999 0.99980 -0.247889024 35.98726115 15.3263 0.55115 TP53AIP1 9.46747721512866e-07 0.0511067004872427 0.948892352765036 tumor protein p53 regulated apoptosis inducing protein 1 FUNCTION: May play an important role in mediating p53/TP53- dependent apoptosis. {ECO:0000269|PubMed:11030628}.; . TISSUE SPECIFICITY: Only found to be expressed in thymus. {ECO:0000269|PubMed:11030628}.; . . . . 0.858082312 88.55862232 44.89077 1.28611 TP53BP1 0.999855964238627 0.000144035761373375 5.35809831021925e-17 tumor protein p53 binding protein 1 FUNCTION: Plays a key role in the response to DNA damage. May have a role in checkpoint signaling during mitosis. Enhances TP53- mediated transcriptional activation. {ECO:0000269|PubMed:12364621, ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:21144835}.; DISEASE: Note=A chromosomal aberration involving TP53BP1 is found in a form of myeloproliferative disorder chronic with eosinophilia. Translocation t(5;15)(q33;q22) with PDGFRB creating a TP53BP1-PDGFRB fusion protein. {ECO:0000269|PubMed:15492236}.; . lymphoreticular;medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;cornea;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.96411 0.10611 -0.29221825 32.94409059 2387.08652 9.06792 TP53BP2 0.00201851813532473 0.997974036769593 7.44509508241614e-06 tumor protein p53 binding protein 2 FUNCTION: Regulator that plays a central role in regulation of apoptosis and cell growth via its interactions. Regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes in vivo. Inhibits the ability of APPBP1 to conjugate NEDD8 to CUL1, and thereby decreases APPBP1 ability to induce apoptosis. Impedes cell cycle progression at G2/M. Its apoptosis-stimulating activity is inhibited by its interaction with DDX42. {ECO:0000269|PubMed:11684014, ECO:0000269|PubMed:12694406, ECO:0000269|PubMed:19377511}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocyte. Reduced expression in breast carcinomas expressing a wild-type TP53 protein. Overexpressed in lung cancer cell lines. {ECO:0000269|PubMed:10498867, ECO:0000269|PubMed:10631318, ECO:0000269|PubMed:11684014}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach; amygdala;occipital lobe;subthalamic nucleus;hypothalamus;temporal lobe;prefrontal cortex;globus pallidus;pons;caudate nucleus;cingulate cortex;parietal lobe; 0.46056 0.12785 -1.126142808 6.564048125 536.31329 4.72110 TP53BP2P1 . . . tumor protein p53 binding protein 2 pseudogene 1 . . . . . . . . . . . TP53COR1 . . . tumor protein p53 pathway corepressor 1 (non-protein coding) . . . . . . . . . . . TP53I3 3.7580421810693e-07 0.197966140120477 0.802033484075306 tumor protein p53 inducible protein 3 FUNCTION: May be involved in the generation of reactive oxygen species (ROS). Has low NADPH-dependent beta-naphthoquinone reductase activity, with a preference for 1,2-beta-naphthoquinone over 1,4-beta-naphthoquinone. Has low NADPH-dependent diamine reductase activity (in vitro). {ECO:0000269|PubMed:19349281}.; . . medulla oblongata;ovary;sympathetic chain;colon;skin;uterus;prostate;whole body;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;muscle;pharynx;blood;lens;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;alveolus;kidney;stomach;aorta;thymus; testis - interstitial;testis - seminiferous tubule;testis; 0.21814 0.13855 0.551232944 81.48148148 45.07022 1.28939 TP53I11 0.0671742712713169 0.871442525455367 0.061383203273316 tumor protein p53 inducible protein 11 . . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; skeletal muscle; 0.19989 0.06568 -0.273576253 33.97027601 5.95622 0.22396 TP53I13 0.0627342931396744 0.921564223970103 0.0157014828902229 tumor protein p53 inducible protein 13 FUNCTION: May act as a tumor suppressor. Inhibits tumor cell growth, when overexpressed. {ECO:0000269|PubMed:14767535}.; . TISSUE SPECIFICITY: Expressed in heart, placenta, skeletal muscle, testis, brain and lung.; medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;kidney;mammary gland;stomach;peripheral nerve; . 0.11546 0.09006 -0.205617011 38.57631517 50.07308 1.38914 TP53INP1 6.85854635079359e-05 0.293374762160171 0.706556652376321 tumor protein p53 inducible nuclear protein 1 FUNCTION: Antiproliferative and proapoptotic protein involved in cell stress response which acts as a dual regulator of transcription and autophagy. Acts as a positive regulator of autophagy. In response to cellular stress or activation of autophagy, relocates to autophagosomes where it interacts with autophagosome-associated proteins GABARAP, GABARAPL1/L2, MAP1LC3A/B/C and regulates autophagy. Acts as an antioxidant and plays a major role in p53/TP53-driven oxidative stress response. Possesses both a p53/TP53-independent intracellular reactive oxygen species (ROS) regulatory function and a p53/TP53-dependent transcription regulatory function. Positively regulates p53/TP53 and p73/TP73 and stimulates their capacity to induce apoptosis and regulate cell cycle. In response to double-strand DNA breaks, promotes p53/TP53 phosphorylation on 'Ser-46' and subsequent apoptosis. Acts as a tumor suppressor by inducing cell death by an autophagy and caspase-dependent mechanism. Can reduce cell migration by regulating the expression of SPARC. {ECO:0000269|PubMed:11511362, ECO:0000269|PubMed:22421968, ECO:0000269|PubMed:22470510}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11511362, ECO:0000269|PubMed:12067065}.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;dura mater;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;tongue;islets of Langerhans;urinary;adrenal cortex;blood;skeletal muscle;bile duct;breast;pia mater;lung;adrenal gland;visual apparatus;liver;hypopharynx;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis;ciliary ganglion;pons;atrioventricular node; 0.40440 0.28016 -0.205617011 38.57631517 69.75415 1.73258 TP53INP2 0.341454389532318 0.600035530716255 0.0585100797514274 tumor protein p53 inducible nuclear protein 2 FUNCTION: Dual regulator of transcription and autophagy. Positively regulates autophagy and is required for autophagosome formation and processing. May act as a scaffold protein that recruits MAP1LC3A, GABARAP and GABARAPL2 and brings them to the autophagosome membrane by interacting with VMP1 where, in cooperation with the BECN1-PI3-kinase class III complex, they trigger autophagosome development. Acts as a transcriptional activator of THRA. {ECO:0000269|PubMed:18030323, ECO:0000269|PubMed:19056683, ECO:0000269|PubMed:22470510}.; . . . . 0.26349 0.10233 . . 16.55675 0.58481 TP53RK 0.349270745629922 0.595196276377702 0.055532977992376 TP53 regulating kinase FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. TP53RK has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit OSGEP (By similarity). Atypical protein kinase that phosphorylates 'Ser-15' of p53/TP53 protein and may therefore participate in its activation. {ECO:0000250, ECO:0000269|PubMed:11546806}.; . TISSUE SPECIFICITY: Highly expressed in testis. Weakly expressed in heart kidney and spleen.; . . 0.18483 . . . 280.01087 3.58496 TP53TG1 . . . TP53 target 1 (non-protein coding) . . TISSUE SPECIFICITY: Isoform 1, isoform 2, isoform 3 and isoform 4 are ubiquitously expressed. {ECO:0000269|PubMed:9713990}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;pituitary gland;bladder;brain;unclassifiable (Anatomical System);hypothalamus;pharynx;blood;lens;lung;cornea;epididymis;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;aorta; . 0.09673 . . . . . TP53TG3 . . . TP53 target 3 FUNCTION: May play a significant role in p53/TP53-mediating signaling pathway. {ECO:0000269|PubMed:10534768}.; . TISSUE SPECIFICITY: Strongly expressed in testis. Weakly expressed in heart, placenta and skeletal muscle. {ECO:0000269|PubMed:10534768}.; . . . . . . . . TP53TG3B . . . TP53 target 3B FUNCTION: May play a significant role in p53/TP53-mediating signaling pathway. {ECO:0000269|PubMed:10534768}.; . TISSUE SPECIFICITY: Strongly expressed in testis. Weakly expressed in heart, placenta and skeletal muscle. {ECO:0000269|PubMed:10534768}.; placenta;testis; . . . . . . . TP53TG3C . . . TP53 target 3C FUNCTION: May play a significant role in p53/TP53-mediating signaling pathway. {ECO:0000269|PubMed:10534768}.; . TISSUE SPECIFICITY: Strongly expressed in testis. Weakly expressed in heart, placenta and skeletal muscle. {ECO:0000269|PubMed:10534768}.; . . . . . . . . TP53TG3D 0.641056795781585 0.331383232711041 0.0275599715073742 TP53 target 3D FUNCTION: May play a significant role in p53/TP53-mediating signaling pathway. {ECO:0000269|PubMed:10534768}.; . TISSUE SPECIFICITY: Strongly expressed in testis. Weakly expressed in heart, placenta and skeletal muscle. {ECO:0000269|PubMed:10534768}.; . . . . . . 22.6399 0.75766 TP53TG3E . . . TP53 target 3 family member E FUNCTION: May play a significant role in p53/TP53-mediating signaling pathway. {ECO:0000269|PubMed:10534768}.; . TISSUE SPECIFICITY: Strongly expressed in testis. Weakly expressed in heart, placenta and skeletal muscle. {ECO:0000269|PubMed:10534768}.; . . . . . . . . TP53TG3F . . . TP53 target 3 family member F FUNCTION: May play a significant role in p53/TP53-mediating signaling pathway. {ECO:0000269|PubMed:10534768}.; . TISSUE SPECIFICITY: Strongly expressed in testis. Weakly expressed in heart, placenta and skeletal muscle. {ECO:0000269|PubMed:10534768}.; . . . . . . . . TP53TG3GP . . . TP53 target 3 family member G, pseudogene . . . . . . . . . . . TP53TG3HP . . . TP53 target 3 family member H, pseudogene . . . . . . . . . . . TP53TG5 3.30244359376843e-06 0.55808313694638 0.441913560610026 TP53 target 5 FUNCTION: May play a significant role in p53/TP53-mediating signaling pathway. {ECO:0000269|PubMed:10719363}.; . TISSUE SPECIFICITY: Highly expressed in heart, brain and small intestine. Less abundant in skeletal muscle, spleen, prostate, ovary and colon. A smaller transcript is expressed specifically in the testis. {ECO:0000269|PubMed:10719363}.; . . 0.06584 0.06291 0.687150476 85.17928757 4614.87046 13.64982 TP63 0.983222202403613 0.0167777801349027 1.7461484058969e-08 tumor protein p63 FUNCTION: Acts as a sequence specific DNA binding transcriptional activator or repressor. The isoforms contain a varying set of transactivation and auto-regulating transactivation inhibiting domains thus showing an isoform specific activity. Isoform 2 activates RIPK4 transcription. May be required in conjunction with TP73/p73 for initiation of p53/TP53 dependent apoptosis in response to genotoxic insults and the presence of activated oncogenes. Involved in Notch signaling by probably inducing JAG1 and JAG2. Plays a role in the regulation of epithelial morphogenesis. The ratio of DeltaN-type and TA*-type isoforms may govern the maintenance of epithelial stem cell compartments and regulate the initiation of epithelial stratification from the undifferentiated embryonal ectoderm. Required for limb formation from the apical ectodermal ridge. Activates transcription of the p21 promoter. {ECO:0000269|PubMed:11641404, ECO:0000269|PubMed:12374749, ECO:0000269|PubMed:12446779, ECO:0000269|PubMed:12446784, ECO:0000269|PubMed:20123734, ECO:0000269|PubMed:22197488, ECO:0000269|PubMed:9774969}.; DISEASE: Acro-dermato-ungual-lacrimal-tooth syndrome (ADULT syndrome) [MIM:103285]: A form of ectodermal dysplasia. Ectodermal dysplasia defines a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. ADULT syndrome involves ectrodactyly, syndactyly, finger- and toenail dysplasia, hypoplastic breasts and nipples, intensive freckling, lacrimal duct atresia, frontal alopecia, primary hypodontia and loss of permanent teeth. ADULT syndrome differs significantly from EEC3 syndrome by the absence of facial clefting. {ECO:0000269|PubMed:11929852}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ankyloblepharon-ectodermal defects-cleft lip/palate (AEC) [MIM:106260]: An autosomal dominant condition characterized by congenital ectodermal dysplasia with coarse, wiry, sparse hair, dystrophic nails, slight hypohidrosis, scalp infections, ankyloblepharon filiform adnatum, maxillary hypoplasia, hypodontia and cleft lip/palate. {ECO:0000269|PubMed:11159940}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Ectrodactyly, ectodermal dysplasia, and cleft lip/palate syndrome 3 (EEC3) [MIM:604292]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. It is an autosomal dominant syndrome characterized by ectrodactyly of hands and feet, ectodermal dysplasia and facial clefting. {ECO:0000269|PubMed:10535733, ECO:0000269|PubMed:10839977, ECO:0000269|PubMed:11462173, ECO:0000269|PubMed:12838557}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Split-hand/foot malformation 4 (SHFM4) [MIM:605289]: A limb malformation involving the central rays of the autopod and presenting with syndactyly, median clefts of the hands and feet, and aplasia and/or hypoplasia of the phalanges, metacarpals, and metatarsals. Some patients have been found to have mental retardation, ectodermal and craniofacial findings, and orofacial clefting. {ECO:0000269|PubMed:10839977, ECO:0000269|PubMed:11462173}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Limb-mammary syndrome (LMS) [MIM:603543]: Characterized by ectrodactyly, cleft palate and mammary-gland abnormalities. {ECO:0000269|PubMed:11462173}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Defects in TP63 are a cause of cervical, colon, head and neck, lung and ovarian cancers.; DISEASE: Ectodermal dysplasia, Rapp-Hodgkin type (EDRH) [MIM:129400]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by the combination of anhidrotic ectodermal dysplasia, cleft lip, and cleft palate. The clinical syndrome is comprised of a characteristic facies (narrow nose and small mouth), wiry, slow-growing, and uncombable hair, sparse eyelashes and eyebrows, obstructed lacrimal puncta/epiphora, bilateral stenosis of external auditory canals, microsomia, hypodontia, cone-shaped incisors, enamel hypoplasia, dystrophic nails, and cleft lip/cleft palate. {ECO:0000269|PubMed:12766194, ECO:0000269|PubMed:12939657, ECO:0000269|PubMed:15200513, ECO:0000269|PubMed:16740912}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Non-syndromic orofacial cleft 8 (OFC8) [MIM:129400]: A birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, notably in heart, kidney, placenta, prostate, skeletal muscle, testis and thymus, although the precise isoform varies according to tissue type. Progenitor cell layers of skin, breast, eye and prostate express high levels of DeltaN-type isoforms. Isoform 10 is predominantly expressed in skin squamous cell carcinomas, but not in normal skin tissues. {ECO:0000269|PubMed:11248048, ECO:0000269|PubMed:9774969}.; unclassifiable (Anatomical System);ovary;heart;colon;parathyroid;skin;skeletal muscle;uterus;prostate;whole body;lung;larynx;thyroid;placenta;hypopharynx;liver;testis;head and neck;spleen;bladder;thymus; dorsal root ganglion;superior cervical ganglion;trachea;tongue;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.90967 0.57126 -0.911109353 9.961075725 57.01541 1.51981 TP73 0.975977778366269 0.0240211884957749 1.03313795595347e-06 tumor protein p73 FUNCTION: Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms. May be a tumor suppressor protein. {ECO:0000269|PubMed:10203277, ECO:0000269|PubMed:11753569, ECO:0000269|PubMed:18174154}.; . TISSUE SPECIFICITY: Expressed in striatal neurons of patients with Huntington disease (at protein level). Brain, kidney, placenta, colon, heart, liver, spleen, skeletal muscle, prostate, thymus and pancreas. Highly expressed in fetal tissue. {ECO:0000269|PubMed:11753569, ECO:0000269|PubMed:16461361}.; unclassifiable (Anatomical System);lung;placenta;muscle;colon;germinal center; adrenal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.44430 0.30077 -1.726953796 2.441613588 112.38972 2.30627 TP73-AS1 . . . TP73 antisense RNA 1 FUNCTION: May modulate apoptosis via regulation of p53/TP53- dependent anti-apoptotic genes. Induces resistance of the chemotherapy drug cisplatin in glioma cells when underexpressed. {ECO:0000269|PubMed:20477830}.; . TISSUE SPECIFICITY: Ubiquitous. Decreased expression in oligodendroglial tumors. {ECO:0000269|PubMed:20477830}.; . . . . . . . . TPBG 0.123234260109032 0.779900055933226 0.0968656839577419 trophoblast glycoprotein FUNCTION: May function as an inhibitor of Wnt/beta-catenin signaling by indirectly interacting with LRP6 and blocking Wnt3a- dependent LRP6 internalization. {ECO:0000269|PubMed:22100263}.; . TISSUE SPECIFICITY: Expressed by all types of trophoblasts as early as 9 weeks of development. Specific for trophoblastic cells except for amniotic epithelium. In adult tissues, the expression is limited to a few epithelial cell types but is found on a variety of carcinoma.; . . 0.26181 0.12875 -0.201976964 38.98325077 83.44453 1.94275 TPBGL . . . trophoblast glycoprotein-like . . . . . . . . . 124.73602 2.42883 TPCN1 0.00385891575421665 0.996138161215683 2.92303010035799e-06 two pore segment channel 1 FUNCTION: Nicotinic acid adenine dinucleotide phosphate (NAADP) receptor that may function as one of the major voltage-gated Ca(2+) channels (VDCC) across the lysosomal and endosomal membrane. {ECO:0000269|PubMed:19620632}.; . TISSUE SPECIFICITY: Highest expression found in the heart and kidney, and lowest expression found in the spleen. {ECO:0000269|PubMed:10574461}.; lymphoreticular;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.22263 . -1.083859071 7.195093182 66.68336 1.68486 TPCN2 2.06493806936103e-06 0.999751656368164 0.000246278693766774 two pore segment channel 2 FUNCTION: Nicotinic acid adenine dinucleotide phosphate (NAADP) receptor that may function as one of the major voltage-gated Ca(2+) channels (VDCC) across the lysosomal membrane. May be involved in smooth muscle contraction. {ECO:0000269|PubMed:19387438, ECO:0000269|PubMed:19620632}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at high level in liver and kidney. {ECO:0000269|PubMed:19387438}.; unclassifiable (Anatomical System);cartilage;ovary;colon;fovea centralis;choroid;lens;retina;breast;prostate;optic nerve;lung;larynx;gum;bone;thyroid;placenta;macula lutea;testis;head and neck;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07401 0.12978 -0.343575389 29.62373201 2340.46288 8.95823 TPD52 0.00511208310791974 0.888505351382231 0.106382565509849 tumor protein D52 . . TISSUE SPECIFICITY: Isoform 2 is expressed in colon, breast, prostate, pancreas and kidney tumor cell lines. Isoform 2 is expressed at high levels in kidney, prostate, brain, small intestine and pancreas, at moderate levels in placenta and colon, at low levels in lung, liver and heart, and at very low levels in spleen, thymus, peripheral mononuclear blood cells, testis and ovary. {ECO:0000269|PubMed:8632896}.; . . 0.32118 0.09861 0.327131069 73.27199811 236.88591 3.32331 TPD52L1 0.00842005639548042 0.933041517011822 0.0585384265926977 tumor protein D52-like 1 . . . ovary;colon;parathyroid;skin;uterus;prostate;optic nerve;endometrium;thyroid;bone;iris;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;alveolus;spleen;cervix;kidney;mammary gland; adrenal gland;caudate nucleus; 0.30877 0.11809 0.12689526 63.00424628 55.92061 1.50126 TPD52L2 0.595604698374735 0.402383050794144 0.00201225083112129 tumor protein D52-like 2 . . . myocardium;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;mesenchyma;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; prefrontal cortex; 0.11992 . 0.191216164 66.57230479 42.67587 1.23771 TPD52L3 0.163388307107127 0.639622416513516 0.196989276379357 tumor protein D52-like 3 . . TISSUE SPECIFICITY: Specifically expressed in testis. Expressed at 5.6-fold higher levels in adult testis than in fetal testis. {ECO:0000269|PubMed:16631610}.; unclassifiable (Anatomical System);medulla oblongata;lung;testis; dorsal root ganglion;superior cervical ganglion;testis - interstitial;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.02028 0.05788 0.483275131 79.25218212 59.94731 1.57084 TPGS1 0.00346749464860698 0.38917004218189 0.607362463169503 tubulin polyglutamylase complex subunit 1 FUNCTION: May act in the targeting of the tubulin polyglutamylase complex. Required for the development of the spermatid flagellum (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;islets of Langerhans;placenta;testis;colon;kidney;germinal center;brain;stomach; amygdala;superior cervical ganglion;cerebellum peduncles;thyroid;ciliary ganglion;parietal lobe; 0.17391 0.10865 . . 357.58608 4.00680 TPGS2 0.000133031926461961 0.636106501317388 0.36376046675615 tubulin polyglutamylase complex subunit 2 . . . lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;placenta;hippocampus;kidney;stomach;aorta;cerebellum; dorsal root ganglion;amygdala;whole brain;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.07090 0.07843 0.082802743 60.09082331 457.06508 4.43937 TPH1 2.67305040364718e-05 0.924859058485721 0.0751142110102423 tryptophan hydroxylase 1 . . TISSUE SPECIFICITY: Isoform 2 seems to be less widely expressed than isoform 1.; lung;endometrium;adrenal gland;visual apparatus;pineal gland; . 0.42896 0.39606 -0.378346116 28.01368247 150.71244 2.68113 TPH2 0.696911876254858 0.303055161370842 3.29623742997378e-05 tryptophan hydroxylase 2 . DISEASE: Major depressive disorder (MDD) [MIM:608516]: A common psychiatric disorder. It is a complex trait characterized by one or more major depressive episodes without a history of manic, mixed, or hypomanic episodes. A major depressive episode is characterized by at least 2 weeks during which there is a new onset or clear worsening of either depressed mood or loss of interest or pleasure in nearly all activities. Four additional symptoms must also be present including changes in appetite, weight, sleep, and psychomotor activity; decreased energy; feelings of worthlessness or guilt; difficulty thinking, concentrating, or making decisions; or recurrent thoughts of death or suicidal ideation, plans, or attempts. The episode must be accompanied by distress or impairment in social, occupational, or other important areas of functioning. {ECO:0000269|PubMed:15629698}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Attention deficit-hyperactivity disorder 7 (ADHD7) [MIM:613003]: A neurobehavioral developmental disorder primarily characterized by the coexistence of attentional problems and hyperactivity, with each behavior occurring infrequently alone. {ECO:0000269|PubMed:18347598}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Naturally occurring variants of TPH2 with impaired enzyme activity could cause deficiency of serotonin production and result in an increased risk of developing behavioral disorders.; TISSUE SPECIFICITY: Brain specific.; . . 0.30209 . -0.069700724 48.54328851 72.63575 1.77849 TPI1 0.581366832186706 0.416368971433044 0.0022641963802505 triosephosphate isomerase 1 . DISEASE: Triosephosphate isomerase deficiency (TPID) [MIM:615512]: An autosomal recessive multisystem disorder characterized by congenital hemolytic anemia, progressive neuromuscular dysfunction, susceptibility to bacterial infection, and cardiomyopathy. {ECO:0000269|PubMed:2876430, ECO:0000269|PubMed:8503454, ECO:0000269|PubMed:8571957, ECO:0000269|PubMed:9338582, ECO:0000269|Ref.34}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . umbilical cord;ovary;salivary gland;developmental;intestine;colon;skin;bone marrow;uterus;prostate;frontal lobe;synovium;testis;brain;artery;bladder;unclassifiable (Anatomical System);trophoblast;cerebellum cortex;hypothalamus;spinal cord;urinary;adrenal cortex;pharynx;blood;breast;bile duct;lung;cornea;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach;aorta; whole brain;amygdala;occipital lobe;thalamus;heart;temporal lobe;kidney;parietal lobe;cerebellum; 0.08025 0.92091 -0.582225231 18.44184949 68.746 1.71739 TPI1P1 . . . triosephosphate isomerase 1 pseudogene 1 . . . . . . . . . . . TPI1P2 . . . triosephosphate isomerase 1 pseudogene 2 . . . . . . . . . . . TPI1P3 . . . triosephosphate isomerase 1 pseudogene 3 . . . lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;uterus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;hypothalamus;muscle;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; . . . . . . . TPI1P4 . . . triosephosphate isomerase 1 pseudogene 4 . . . . . . . . . . . TPK1 0.0282545792431748 0.922294643502295 0.0494507772545307 thiamin pyrophosphokinase 1 FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. Can also catalyze the phosphorylation of pyrithiamine to pyrithiamine pyrophosphate. {ECO:0000269|PubMed:11342111}.; . TISSUE SPECIFICITY: Detected in heart, kidney, testis, small intestine and peripheral blood leukocytes, and at very low levels in a variety of tissues. {ECO:0000269|PubMed:11342111, ECO:0000269|PubMed:11342117}.; unclassifiable (Anatomical System);ovary;hypothalamus;parathyroid;pancreas;whole body;lung;frontal lobe;endometrium;bone;placenta;liver;testis;spleen;kidney;artery;aorta;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.86610 0.13412 0.058937498 58.26256192 21.33141 0.72002 TPM1 0.79947002234679 0.200288928387985 0.000241049265224264 tropomyosin 1 (alpha) FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.; DISEASE: Cardiomyopathy, familial hypertrophic 3 (CMH3) [MIM:115196]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:12974739, ECO:0000269|PubMed:7898523, ECO:0000269|PubMed:8205619, ECO:0000269|PubMed:8523464, ECO:0000269|PubMed:9822100}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1Y (CMD1Y) [MIM:611878]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:11273725}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Left ventricular non-compaction 9 (LVNC9) [MIM:611878]: A disease due to an arrest of myocardial morphogenesis. It is characterized by a hypertrophic left ventricle with deep trabeculations and with poor systolic function, with or without associated left ventricular dilation. In some cases, it is associated with other congenital heart anomalies. {ECO:0000269|PubMed:21551322}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in primary breast cancer tissues but undetectable in normal breast tissues in Sudanese patients. Isoform 1 is expressed in adult and fetal skeletal muscle and cardiac tissues, with higher expression levels in the cardiac tissues. Isoform 10 is expressed in adult and fetal cardiac tissues, but not in skeletal muscle. {ECO:0000269|PubMed:15249230, ECO:0000269|Ref.15}.; myocardium;medulla oblongata;smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;amniotic fluid;ciliary body;bladder;brain;cartilage;heart;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);trophoblast;lymph node;lacrimal gland;hypothalamus;bile duct;pancreas;lung;cornea;placenta;hippocampus;amnion;duodenum;head and neck;kidney;aorta;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;adipose tissue;smooth muscle;heart;tongue;atrioventricular node;fetal thyroid;skeletal muscle;skin;uterus;uterus corpus;prostate;thyroid;appendix;ciliary ganglion;trigeminal ganglion;cerebellum; 0.88236 0.46623 -0.427900189 25.14744043 5.86077 0.22068 TPM2 4.59299187157402e-05 0.857870285831213 0.142083784250071 tropomyosin 2 (beta) FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. The non-muscle isoform may have a role in agonist-mediated receptor internalization (By similarity). {ECO:0000250}.; DISEASE: Nemaline myopathy 4 (NEM4) [MIM:609285]: A form of nemaline myopathy. Nemaline myopathies are muscular disorders characterized by muscle weakness of varying severity and onset, and abnormal thread-like or rod-shaped structures in muscle fibers on histologic examination. Nemaline myopathy type 4 presents from infancy to childhood with hypotonia and moderate-to-severe proximal weakness with minimal or no progression. Major motor milestones are delayed but independent ambulation is usually achieved, although a wheelchair may be needed in later life. {ECO:0000269|PubMed:11738357, ECO:0000269|PubMed:17846275, ECO:0000269|PubMed:24692096}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Arthrogryposis, distal, 1A (DA1A) [MIM:108120]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. Distal arthrogryposis type 1 is characterized largely by camptodactyly and clubfoot. Hypoplasia and/or absence of some interphalangeal creases is common. The shoulders and hips are less frequently affected. {ECO:0000269|PubMed:12592607, ECO:0000269|PubMed:24692096}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cap myopathy 2 (CAPM2) [MIM:609285]: A rare congenital skeletal muscle disorder characterized by the presence of cap-like structures which are well demarcated and peripherally located under the sarcolemma and show abnormal accumulation of sarcomeric proteins. Clinical features are early onset of hypotonia and non- progressive or slowly progressive muscle weakness. Respiratory problems are common. {ECO:0000269|PubMed:17434307, ECO:0000269|PubMed:19047562, ECO:0000269|PubMed:19345583, ECO:0000269|PubMed:24692096}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Arthrogryposis, distal, 2B (DA2B) [MIM:601680]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA2B is characterized by contractures of the hands and feet, and a distinctive face characterized by prominent nasolabial folds, small mouth and downslanting palpebral fissures. {ECO:0000269|PubMed:17339586}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Present in primary breast cancer tissue, absent from normal breast tissue. {ECO:0000269|Ref.10}.; unclassifiable (Anatomical System);myocardium;heart;muscle;skeletal muscle;retina;greater omentum;whole body;lung;larynx;testis;head and neck;kidney;brain; uterus;prostate;smooth muscle;adipose tissue;heart;tongue;thyroid;testis;appendix;skeletal muscle; 0.81211 0.22353 -0.229483771 36.86010852 1089.41587 6.31789 TPM3 0.191983984043152 0.805744089565529 0.00227192639131867 tropomyosin 3 FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.; DISEASE: Nemaline myopathy 1 (NEM1) [MIM:609284]: A form of nemaline myopathy with autosomal dominant or recessive inheritance. Nemaline myopathies are disorders characterized by muscle weakness of varying onset and severity, and abnormal thread-like or rod-shaped structures in muscle fibers on histologic examination. Autosomal dominant NEM1 is characterized by a moderate phenotype with onset between birth and early second decade of life. Weakness is diffuse and symmetric with slow progression often with need for a wheelchair in adulthood. The autosomal recessive form has onset at birth with moderate to severe hypotonia and diffuse weakness. In the most severe cases, death can occur before 2 years. Less severe cases have delayed major motor milestones, and these patients may walk, but often need a wheelchair before 10 years. {ECO:0000269|PubMed:17376686, ECO:0000269|PubMed:24692096, ECO:0000269|PubMed:7704029}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving TPM3 is found in papillary thyroid carcinomas (PTCs). A rearrangement with NTRK1 generates the TRK fusion transcript by fusing the amino end of isoform 2 of TPM3 to the 3'-end of NTRK1. {ECO:0000269|PubMed:2869410}.; DISEASE: Myopathy, congenital, with fiber-type disproportion (CFTD) [MIM:255310]: A genetically heterogeneous disorder in which there is relative hypotrophy of type 1 muscle fibers compared to type 2 fibers on skeletal muscle biopsy. However, these findings are not specific and can be found in many different myopathic and neuropathic conditions. {ECO:0000269|PubMed:18300303, ECO:0000269|PubMed:19953533, ECO:0000269|PubMed:20951040, ECO:0000269|PubMed:24692096}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cap myopathy 1 (CAPM1) [MIM:609284]: A rare congenital skeletal muscle disorder characterized by the presence of cap-like structures which are well demarcated and peripherally located under the sarcolemma and show abnormal accumulation of sarcomeric proteins. Clinical features are early onset of hypotonia and slowly progressive muscle weakness. Respiratory problems are common. {ECO:0000269|PubMed:18300303, ECO:0000269|PubMed:19487656, ECO:0000269|PubMed:19553118, ECO:0000269|PubMed:24239060, ECO:0000269|PubMed:24692096}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;umbilical cord;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;amniotic fluid;germinal center;brain;bladder;tonsil;gall bladder;cartilage;heart;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);trophoblast;lymph node;islets of Langerhans;oral cavity;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;aorta;stomach;cerebellum;thymus; superior cervical ganglion;tongue;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.57758 0.46610 0.3032669 72.009908 38.39972 1.13903 TPM3P1 . . . tropomyosin 3 pseudogene 1 . . . . . . . . . . . TPM3P2 . . . tropomyosin 3 pseudogene 2 . . . . . . . . . . . TPM3P3 . . . tropomyosin 3 pseudogene 3 . . . . . . . . . . . TPM3P4 . . . tropomyosin 3 pseudogene 4 . . . . . . . . . . . TPM3P5 . . . tropomyosin 3 pseudogene 5 . . . . . . . . . . . TPM3P6 . . . tropomyosin 3 pseudogene 6 . . . . . . . . . . . TPM3P7 . . . tropomyosin 3 pseudogene 7 . . . unclassifiable (Anatomical System);umbilical cord;colon;blood;skin;breast;prostate;pancreas;larynx;placenta;duodenum;liver;head and neck;spleen;germinal center;brain;bladder;tonsil;stomach; . . . . . . . TPM3P8 . . . tropomyosin 3 pseudogene 8 . . . lymphoreticular;umbilical cord;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;testis;germinal center;brain;bladder;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; . . . . . . . TPM3P9 . . . tropomyosin 3 pseudogene 9 . . . . . . . . . . . TPM4 0.10940201669772 0.884209671068475 0.00638831223380417 tropomyosin 4 FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. Binds calcium. {ECO:0000269|PubMed:1836432}.; . TISSUE SPECIFICITY: Detected in cardiac tissue and platelets, the form found in cardiac tissue is a higher molecular weight than the form found in platelets. Expressed at higher levels in the platelets of hypertensive patients with cardiac hypertrophy than in the platelets of hypertensive patients without cardiac hypertrophy (at protein level). {ECO:0000269|PubMed:1836432}.; lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;amniotic fluid;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;larynx;bone;testis;artery;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;mesenchyma;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta; . 0.20651 0.20370 -0.073340031 48.11866006 38.84582 1.15031 TPM4P1 . . . tropomyosin 4 pseudogene 1 . . . . . . . . . . . TPMT 7.57391771227039e-05 0.751715695980259 0.248208564842618 thiopurine S-methyltransferase FUNCTION: Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine. {ECO:0000269|PubMed:18484748}.; DISEASE: Thiopurine S-methyltransferase deficiency (TPMT deficiency) [MIM:610460]: Enzyme involved in the normal metabolic inactivation of thiopurine drugs. These drugs are generally used as immunosuppressants or cytotoxic drugs and are prescribed for a variety of clinical conditions including leukemia, autoimmune disease and organ transplantation. Patients with intermediate or no TPMT activity are at risk of toxicity after receiving standard doses of thiopurine drugs and it is shown that inter-individual differences in response to these drugs are largely determined by genetic variation at the TPMT locus. {ECO:0000269|PubMed:10208641, ECO:0000269|PubMed:10751626, ECO:0000269|PubMed:15819814, ECO:0000269|PubMed:16220112, ECO:0000269|PubMed:16476125, ECO:0000269|PubMed:16789994, ECO:0000269|PubMed:7862671, ECO:0000269|PubMed:8561894, ECO:0000269|PubMed:8644731, ECO:0000269|PubMed:9246020, ECO:0000269|PubMed:9336428, ECO:0000269|PubMed:9711875, ECO:0000269|PubMed:9931345, ECO:0000269|PubMed:9931346}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;fovea centralis;skin;bone marrow;uterus;prostate;whole body;endometrium;thyroid;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;skeletal muscle;bile duct;breast;pancreas;lung;macula lutea;hippocampus;liver;spleen;kidney;mammary gland; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.09520 0.16643 0.793752871 87.40268931 598.55884 4.95305 TPMTP1 . . . thiopurine S-methyltransferase pseudogene 1 . . . . . . . . . . . TPMTP2 . . . thiopurine S-methyltransferase pseudogene 2 . . . . . . . . . . . TPMTP3 . . . thiopurine S-methyltransferase pseudogene 3 . . . . . . . . . . . TPMTP4 . . . thiopurine S-methyltransferase pseudogene 4 . . . . . . . . . . . TPO 1.35596875602643e-07 0.988057948199512 0.0119419162036124 thyroid peroxidase FUNCTION: Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4).; DISEASE: Note=An alternative splicing in the thyroperoxidase mRNA can cause Graves' disease.; DISEASE: Thyroid dyshormonogenesis 2A (TDH2A) [MIM:274500]: A disorder due to defective conversion of accumulated iodide to organically bound iodine. The iodide organification defect can be partial or complete. {ECO:0000269|PubMed:10084596, ECO:0000269|PubMed:10468986, ECO:0000269|PubMed:11061528, ECO:0000269|PubMed:11415848, ECO:0000269|PubMed:11874711, ECO:0000269|PubMed:11916616, ECO:0000269|PubMed:12213873, ECO:0000269|PubMed:12490071, ECO:0000269|PubMed:12843174, ECO:0000269|PubMed:12864797, ECO:0000269|PubMed:12938097, ECO:0000269|PubMed:16284446, ECO:0000269|PubMed:16684826, ECO:0000269|PubMed:7550241, ECO:0000269|PubMed:9024270, ECO:0000269|PubMed:9924196}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;larynx;thyroid;muscle;colon;head and neck; thyroid;fetal thyroid;parietal lobe;cingulate cortex; 0.18628 0.48162 -0.14151689 42.36258552 2837.88244 10.06894 TPP1 0.0257560632861161 0.973709902961873 0.000534033752011114 tripeptidyl peptidase I FUNCTION: Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus (By similarity). {ECO:0000250}.; DISEASE: Ceroid lipofuscinosis, neuronal, 2 (CLN2) [MIM:204500]: A form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment pattern seen most often in CLN2 consists of curvilinear profiles. {ECO:0000269|PubMed:10330339, ECO:0000269|PubMed:10665500, ECO:0000269|PubMed:11241479, ECO:0000269|PubMed:11339651, ECO:0000269|PubMed:11589012, ECO:0000269|PubMed:12376936, ECO:0000269|PubMed:12414822, ECO:0000269|PubMed:12698559, ECO:0000269|PubMed:19201763, ECO:0000269|PubMed:20340139, ECO:0000269|PubMed:21990111, ECO:0000269|PubMed:22612257, ECO:0000269|PubMed:9295267}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spinocerebellar ataxia, autosomal recessive, 7 (SCAR7) [MIM:609270]: Spinocerebellar ataxia defines a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR7 patients show difficulty walking and writing, dysarthria, limb ataxia, and cerebellar atrophy. {ECO:0000269|PubMed:23418007}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in all tissues examined with highest levels in heart and placenta and relatively similar levels in other tissues.; lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;gall bladder;amygdala;heart;cartilage;tongue;pineal body;urinary;adrenal cortex;blood;cerebrum;lens;skeletal muscle;breast;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;adrenal gland;placenta;kidney;trigeminal ganglion;bone marrow; 0.14349 0.27976 0.400544645 76.40953055 277.1193 3.56473 TPP2 0.999863188903156 0.000136811096816057 2.81969779254378e-14 tripeptidyl peptidase II FUNCTION: Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity). {ECO:0000250}.; . . . . 0.47068 0.17582 -1.151821487 6.269167256 89.78559 2.03862 TPPP 0.447860539159373 0.523687831771004 0.0284516290696232 tubulin polymerization promoting protein FUNCTION: May play a role in the polymerization of tubulin into microtubules, microtubule bundling and the stabilization of existing microtubules, thus maintaining the integrity of the microtubule network. May play a role in mitotic spindle assembly and nuclear envelope breakdown. {ECO:0000269|PubMed:17105200, ECO:0000269|PubMed:17693641, ECO:0000269|PubMed:18028908}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10083737}.; heart;islets of Langerhans;hypothalamus;parathyroid;fovea centralis;skin;retina;uterus;optic nerve;lung;macula lutea;hippocampus;visual apparatus;kidney;brain; whole brain;amygdala;medulla oblongata;thalamus;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.32775 0.16177 -0.315847836 31.68789809 36.35113 1.08938 TPPP2 0.0171866165993747 0.714700489636831 0.268112893763795 tubulin polymerization-promoting protein family member 2 FUNCTION: May bind tubulin but has no microtubule bundling activity. {ECO:0000269|PubMed:17105200}.; . TISSUE SPECIFICITY: Expressed in spermatids. Detected in liver cancer (at protein level). {ECO:0000269|PubMed:23436708}.; unclassifiable (Anatomical System);lung;testis;kidney; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.15285 0.10299 0.571462851 81.99457419 1640.17896 7.48623 TPPP3 0.311517277242007 0.617033153722715 0.0714495690352784 tubulin polymerization-promoting protein family member 3 FUNCTION: Binds tubulin and has microtubule bundling activity. May play a role in cell proliferation and mitosis. {ECO:0000269|PubMed:17105200, ECO:0000269|PubMed:19633818}.; . . ovary;sympathetic chain;colon;parathyroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;muscle;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;hypopharynx;spleen;head and neck;cervix;kidney;stomach;thymus; . 0.42439 . -0.139478553 43.29440906 19.60056 0.67258 TPR 0.999999999996002 3.99755495947971e-12 2.53441407920535e-33 translocated promoter region, nuclear basket protein FUNCTION: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. According to some authors, plays a limited role in the regulation of nuclear protein export (PubMed:22253824 and PubMed:11952838). Plays also a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases. {ECO:0000269|PubMed:11952838, ECO:0000269|PubMed:15654337, ECO:0000269|PubMed:17897941, ECO:0000269|PubMed:18794356, ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:20133940, ECO:0000269|PubMed:20407419, ECO:0000269|PubMed:21613532, ECO:0000269|PubMed:22253824, ECO:0000269|PubMed:9864356}.; DISEASE: Note=A chromosomal aberration involving TPR has been found in papillary thyroid carcinomas (PTCs). Intrachromosomal rearrangement that links the 5'-end of the TPR gene to the protein kinase domain of NTRK1 forms the fusion protein TRK-T1. TRK-T1 is a 55 kDa protein reacting with antibodies against the carboxy terminus of the NTRK1 protein. {ECO:0000269|PubMed:1532241}.; DISEASE: Note=Involved in tumorigenic rearrangements with the MET. {ECO:0000269|PubMed:2300559}.; TISSUE SPECIFICITY: Expressed in esophagus, ovary, liver, skin, smooth muscles, cerebrum and fetal cerebellum (at protein level). Highest in testis, lung, thymus, spleen and brain, lower levels in heart, liver and kidney. {ECO:0000269|PubMed:12424524, ECO:0000269|PubMed:9024684}.; . . 0.94545 . -0.470420436 23.04788865 2020.35538 8.26984 TPRA1 0.0583580196535496 0.92410539201536 0.0175365883310907 transmembrane protein adipocyte associated 1 . . TISSUE SPECIFICITY: Ubiquitous, with higher levels in heart, placenta and kidney. {ECO:0000269|PubMed:10342878}.; ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;breast;pancreas;lung;placenta;hippocampus;liver;duodenum;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach; heart; 0.26237 0.12365 0.064394823 58.84642604 77.74892 1.85848 TPRG1 4.87825873738663e-05 0.424954071376125 0.574997146036501 tumor protein p63 regulated 1 . . . unclassifiable (Anatomical System);ovary;cartilage;lacrimal gland;uterus;breast;prostate;lung;larynx;thyroid;alveolus;testis;head and neck;mammary gland; dorsal root ganglion;testis - interstitial;subthalamic nucleus;superior cervical ganglion;tongue;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.18298 0.10735 0.060756528 58.52795471 57.90036 1.53844 TPRG1-AS1 . . . TPRG1 antisense RNA 1 . . . . . . . . . . . TPRG1-AS2 . . . TPRG1 antisense RNA 2 . . . . . . . . . . . TPRG1L 0.00284528475212618 0.803826307975222 0.193328407272651 tumor protein p63 regulated 1-like . . . myocardium;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;synovium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.15732 0.10917 -0.117432389 44.89266336 7.9088 0.29040 TPRKB 0.0206180267045899 0.748409742636178 0.230972230659232 TP53RK binding protein FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. TPRKB acts as an allosteric effector that regulates the t(6)A activity of the complex. TPRKB is not required for tRNA modification (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12659830}.; smooth muscle;ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;cochlea;endometrium;testis;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;breast;pancreas;pia mater;lung;nasopharynx;placenta;duodenum;alveolus;liver;spleen;kidney; testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.22953 0.10546 -0.339715008 30.06605331 16.87689 0.59396 TPRKBP1 . . . TP53RK binding protein pseudogene 1 . . . . . . . . . . . TPRKBP2 . . . TP53RK binding protein pseudogene 2 . . . . . . . . . . . TPRN . . . taperin . . TISSUE SPECIFICITY: Expression is detected in fetal cochlea. {ECO:0000269|PubMed:20170898}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.11836 . . . 1020.40412 6.14631 TPRX1 0.000613267786761704 0.485833234027097 0.513553498186141 tetra-peptide repeat homeobox 1 . . . macula lutea;fovea centralis; . 0.23746 . -0.115612493 45.12856806 2120.83171 8.47905 TPRX1P1 . . . tetra-peptide repeat homeobox 1 pseudogene 1 . . . . . . . . . . . TPRX2P 0.0116462336341647 0.635798040266583 0.352555726099252 tetra-peptide repeat homeobox 2 pseudogene . . . . . . . . . 764.43055 5.47893 TPRXL . . . tetra-peptide repeat homeobox-like . . . placenta; . 0.27808 . . . 3182.26774 10.74367 TPSAB1 4.56498117493005e-05 0.412314058769822 0.587640291418428 tryptase alpha/beta 1 FUNCTION: Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity. Isoform 2 cleaves large substrates, such as fibronectin, more efficiently than isoform 1, but seems less efficient toward small substrates (PubMed:18854315). {ECO:0000250, ECO:0000250|UniProtKB:P21845, ECO:0000269|PubMed:18854315}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in lung, stomach, spleen, heart and skin; in these tissues, isoform 1 is predominant. Isoform 2 is expressed in aorta, spleen, and breast tumor, with highest levels in the endothelial cells of some blood vessels surrounding the aorta, as well as those surrounding the tumor and low levels, if any, in mast cells (at protein level). {ECO:0000269|PubMed:18854315}.; unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;sympathetic chain;colon;choroid;skeletal muscle;retina;bone marrow;pancreas;lung;bone;visual apparatus;iris;liver;testis;head and neck;spleen;kidney;brain;stomach;gall bladder; . . 0.48316 . . 124.20631 2.42494 TPSB2 2.34678788202538e-08 0.0415298987163228 0.958470077815798 tryptase beta 2 (gene/pseudogene) FUNCTION: Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity. {ECO:0000250, ECO:0000250|UniProtKB:P21845}.; . . unclassifiable (Anatomical System);lymphoreticular;cartilage;tongue;islets of Langerhans;sympathetic chain;colon;choroid;retina;uterus;pancreas;lung;bone;visual apparatus;testis;head and neck;kidney;brain;mammary gland;stomach;gall bladder; . . 0.48316 . . . . TPSD1 8.52216628919943e-09 0.0440005442367236 0.95599944724111 tryptase delta 1 FUNCTION: Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in colon, lung, heart and synovial tissue. May be specific to mast cells. {ECO:0000269|PubMed:12391231}.; lung;islets of Langerhans;iris;testis;colon;kidney;brain;stomach; cingulate cortex;bone marrow; 0.28036 0.16838 1.710500644 96.46142958 2541.65507 9.41658 TPSG1 4.08951910541866e-06 0.215746169050367 0.784249741430527 tryptase gamma 1 . . TISSUE SPECIFICITY: Expressed in many tissues.; unclassifiable (Anatomical System);smooth muscle;ovary;tongue;islets of Langerhans;developmental;colon;fovea centralis;choroid;lens;retina;uterus;prostate;optic nerve;lung;endometrium;bone;macula lutea;liver;testis;spleen;cervix;kidney; superior cervical ganglion;liver;caudate nucleus; 0.22731 0.31463 1.201528238 93.00542581 1738.17028 7.69533 TPSP1 . . . tryptase pseudogene 1 . . . . . . . . . . . TPSP2 . . . tryptase pseudogene 2 . . . . . . . . . . . TPST1 0.0114811021514916 0.949393478286894 0.0391254195616144 tyrosylprotein sulfotransferase 1 FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides.; . . ovary;colon;parathyroid;choroid;vein;skin;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;hypothalamus;muscle;adrenal cortex;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;liver;spleen;head and neck;kidney; testis; 0.16396 0.12440 -0.249709319 35.74545883 26.1429 0.84768 TPST2 0.599488923277404 0.391306400839605 0.00920467588299181 tyrosylprotein sulfotransferase 2 FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9736702}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;thyroid;iris;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;pharynx;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; pancreas;thyroid;testis; 0.22381 0.12212 -0.844966979 11.1759849 37.14228 1.10940 TPST2P1 . . . tyrosylprotein sulfotransferase 2 pseudogene 1 . . . . . . . . . . . TPT1 0.946442279845925 0.0533733406410647 0.0001843795130103 tumor protein, translationally-controlled 1 FUNCTION: Involved in calcium binding and microtubule stabilization.; . TISSUE SPECIFICITY: Found in several healthy and tumoral cells including erythrocytes, hepatocytes, macrophages, platelets, keratinocytes, erythroleukemia cells, gliomas, melanomas, hepatoblastomas, and lymphomas. It cannot be detected in kidney and renal cell carcinoma (RCC). Expressed in placenta and prostate. {ECO:0000269|PubMed:9059837}.; . . 0.67572 0.35026 -0.053113545 49.38664779 3.58338 0.12982 TPT1-AS1 . . . TPT1 antisense RNA 1 . . . . . . . . . . . TPT1P1 . . . tumor protein, translationally-controlled 1 pseudogene 1 . . . . . . . . . . . TPT1P2 . . . tumor protein, translationally-controlled 1 pseudogene 2 . . . . . . . . . . . TPT1P3 . . . tumor protein, translationally-controlled 1 pseudogene 3 . . . . . . . . . . . TPT1P4 . . . tumor protein, translationally-controlled 1 pseudogene 4 . . . . . . . . . . . TPT1P5 . . . tumor protein, translationally-controlled 1 pseudogene 5 . . . . . . . . . . . TPT1P6 . . . tumor protein, translationally-controlled 1 pseudogene 6 . . . . . . . . . . . TPT1P7 . . . tumor protein, translationally-controlled 1 pseudogene 7 . . . . . . . . . . . TPT1P8 . . . tumor protein, translationally-controlled 1 pseudogene 8 . . . . . . . . . . . TPT1P9 . . . tumor protein, translationally-controlled 1 pseudogene 9 . . . . . . . . . . . TPT1P10 . . . tumor protein, translationally-controlled 1 pseudogene 10 . . . . . . . . . . . TPT1P11 . . . tumor protein, translationally-controlled 1 pseudogene 11 . . . . . . . . . . . TPT1P12 . . . tumor protein, translationally-controlled 1 pseudogene 12 . . . . . . . . . . . TPT1P13 . . . tumor protein, translationally-controlled 1 pseudogene 13 . . . . . . . . . . . TPT1P14 . . . tumor protein, translationally-controlled 1 pseudogene 14 . . . . . . . . . . . TPTE 5.11403738742454e-31 2.41951757308982e-06 0.999997580482427 transmembrane phosphatase with tensin homology FUNCTION: Could be involved in signal transduction.; . TISSUE SPECIFICITY: Exclusively expressed in testis. {ECO:0000269|PubMed:10598804}.; unclassifiable (Anatomical System);lung;placenta;testis; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;appendix;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; . 0.05870 2.938206407 99.1507431 179.24136 2.90847 TPTE2 3.69447198098053e-08 0.984505939589134 0.015494023466146 transmembrane phosphoinositide 3-phosphatase and tensin homolog 2 . . TISSUE SPECIFICITY: Isoform 3 is expressed in testis, brain and stomach while isoform 4 seems to be testis-specific. {ECO:0000269|PubMed:11716755}.; unclassifiable (Anatomical System);placenta;testis;brain; . 0.07785 0.18826 -0.178111357 40.44585987 120.84753 2.39632 TPTE2P1 . . . transmembrane phosphoinositide 3-phosphatase and tensin homolog 2 pseudogene 1 . . . . . . . . . . . TPTE2P2 . . . transmembrane phosphoinositide 3-phosphatase and tensin homolog 2 pseudogene 2 . . . . . . . . . . . TPTE2P3 . . . transmembrane phosphoinositide 3-phosphatase and tensin homolog 2 pseudogene 3 . . . . . . . . . . . TPTE2P4 . . . transmembrane phosphoinositide 3-phosphatase and tensin homolog 2 pseudogene 4 . . . lung;testis; . . . . . . . TPTE2P5 . . . transmembrane phosphoinositide 3-phosphatase and tensin homolog 2 pseudogene 5 . . . . . 0.22674 . . . . . TPTE2P6 . . . transmembrane phosphoinositide 3-phosphatase and tensin homolog 2 pseudogene 6 . . . . . . . . . . . TPTEP1 . . . transmembrane phosphatase with tensin homology pseudogene 1 . . . . . . . . . . . TPX2 0.992124193249196 0.00787580401907151 2.73173230333067e-09 TPX2, microtubule-associated FUNCTION: Spindle assembly factor required for normal assembly of mitotic spindles. Required for normal assembly of microtubules during apoptosis. Required for chromatin and/or kinetochore dependent microtubule nucleation. Mediates AURKA localization to spindle microtubules (PubMed:18663142, PubMed:19208764). Activates AURKA by promoting its autophosphorylation at 'Thr-288' and protects this residue against dephosphorylation (PubMed:18663142, PubMed:19208764). TPX2 is inactivated upon binding to importin- alpha (PubMed:26165940). At the onset of mitosis, GOLGA2 interacts with importin-alpha, liberating TPX2 from importin-alpha, allowing TPX2 to activates AURKA kinase and stimulates local microtubule nucleation (PubMed:26165940). {ECO:0000269|PubMed:18663142, ECO:0000269|PubMed:19208764, ECO:0000269|PubMed:26165940}.; . TISSUE SPECIFICITY: Expressed in lung carcinoma cell lines but not in normal lung tissues.; medulla oblongata;ovary;foreskin;skin;retina;bone marrow;prostate;optic nerve;endometrium;gum;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;muscle;bile duct;pancreas;lung;adrenal gland;mesenchyma;placenta;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;fetal liver;testis - seminiferous tubule;tumor;testis;atrioventricular node;trigeminal ganglion;thymus; 0.92776 0.09677 -0.380166007 27.88393489 98.37826 2.14429 TRA . . . T-cell receptor alpha locus . . . . . . . . . . . TRA-AGC1-1 . . . transfer RNA-Ala (AGC) 1-1 . . . . . . . . . . . TRA-AGC2-1 . . . transfer RNA-Ala (AGC) 2-1 . . . . . . . . . . . TRA-AGC2-2 . . . transfer RNA-Ala (AGC) 2-2 . . . . . . . . . . . TRA-AGC3-1 . . . transfer RNA-Ala (AGC) 3-1 . . . . . . . . . . . TRA-AGC4-1 . . . transfer RNA-Ala (AGC) 4-1 . . . . . . . . . . . TRA-AGC5-1 . . . transfer RNA-Ala (AGC) 5-1 . . . . . . . . . . . TRA-AGC6-1 . . . transfer RNA-Ala (AGC) 6-1 . . . . . . . . . . . TRA-AGC7-1 . . . transfer RNA-Ala (AGC) 7-1 . . . . . . . . . . . TRA-AGC8-1 . . . transfer RNA-Ala (AGC) 8-1 . . . . . . . . . . . TRA-AGC8-2 . . . transfer RNA-Ala (AGC) 8-2 . . . . . . . . . . . TRA-AGC9-1 . . . transfer RNA-Ala (AGC) 9-1 . . . . . . . . . . . TRA-AGC9-2 . . . transfer RNA-Ala (AGC) 9-2 . . . . . . . . . . . TRA-AGC10-1 . . . transfer RNA-Ala (AGC) 10-1 . . . . . . . . . . . TRA-AGC11-1 . . . transfer RNA-Ala (AGC) 11-1 . . . . . . . . . . . TRA-AGC12-1 . . . transfer RNA-Ala (AGC) 12-1 . . . . . . . . . . . TRA-AGC12-2 . . . transfer RNA-Ala (AGC) 12-2 . . . . . . . . . . . TRA-AGC12-3 . . . transfer RNA-Ala (AGC) 12-3 . . . . . . . . . . . TRA-AGC13-1 . . . transfer RNA-Ala (AGC) 13-1 . . . . . . . . . . . TRA-AGC13-2 . . . transfer RNA-Ala (AGC) 13-2 . . . . . . . . . . . TRA-AGC14-1 . . . transfer RNA-Ala (AGC) 14-1 . . . . . . . . . . . TRA-AGC15-1 . . . transfer RNA-Ala (AGC) 15-1 . . . . . . . . . . . TRA-AGC16-1 . . . transfer RNA-Ala (AGC) 16-1 . . . . . . . . . . . TRA-AGC17-1 . . . transfer RNA-Ala (AGC) 17-1 . . . . . . . . . . . TRA-AGC18-1 . . . transfer RNA-Ala (AGC) 18-1 . . . . . . . . . . . TRA-AGC18-2 . . . transfer RNA-Ala (AGC) 18-2 . . . . . . . . . . . TRA-AGC19-1 . . . transfer RNA-Ala (AGC) 19-1 . . . . . . . . . . . TRA-AGC20-1 . . . transfer RNA-Ala (AGC) 20-1 . . . . . . . . . . . TRA-AGC21-1 . . . transfer RNA-Ala (AGC) 21-1 . . . . . . . . . . . TRA-AGC22-1 . . . transfer RNA-Ala (AGC) 22-1 . . . . . . . . . . . TRA-AGC23-1 . . . transfer RNA-Ala (AGC) 23-1 . . . . . . . . . . . TRA-CGC1-1 . . . transfer RNA-Ala (CGC) 1-1 . . . . . . . . . . . TRA-CGC2-1 . . . transfer RNA-Ala (CGC) 2-1 . . . . . . . . . . . TRA-CGC3-1 . . . transfer RNA-Ala (CGC) 3-1 . . . . . . . . . . . TRA-CGC4-1 . . . transfer RNA-Ala (CGC) 4-1 . . . . . . . . . . . TRA-CGC5-1 . . . transfer RNA-Ala (CGC) 5-1 . . . . . . . . . . . TRA-TGC1-1 . . . transfer RNA-Ala (TGC) 1-1 . . . . . . . . . . . TRA-TGC2-1 . . . transfer RNA-Ala (TGC) 2-1 . . . . . . . . . . . TRA-TGC3-1 . . . transfer RNA-Ala (TGC) 3-1 . . . . . . . . . . . TRA-TGC3-2 . . . transfer RNA-Ala (TGC) 3-2 . . . . . . . . . . . TRA-TGC4-1 . . . transfer RNA-Ala (TGC) 4-1 . . . . . . . . . . . TRA-TGC5-1 . . . transfer RNA-Ala (TGC) 5-1 . . . . . . . . . . . TRA-TGC6-1 . . . transfer RNA-Ala (TGC) 6-1 . . . . . . . . . . . TRA-TGC7-1 . . . transfer RNA-Ala (TGC) 7-1 . . . . . . . . . . . TRA-TGC8-1 . . . transfer RNA-Ala (TGC) 8-1 . . . . . . . . . . . TRA-TGC9-1 . . . transfer RNA-Ala (TGC) 9-1 . . . . . . . . . . . TRA-TGC10-1 . . . transfer RNA-Ala (TGC) 10-1 . . . . . . . . . . . TRA2A 0.212371727129574 0.787552155462937 7.61174074895346e-05 transformer 2 alpha homolog (Drosophila) FUNCTION: Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. {ECO:0000269|PubMed:9546399}.; . . myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;bile duct;pancreas;lung;epididymis;trabecular meshwork;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;aorta;stomach; medulla oblongata;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node; . . -0.317668748 31.45789101 11.23044 0.40514 TRA2B 0.988418187489854 0.0115809645469427 8.47963203177071e-07 transformer 2 beta homolog (Drosophila) FUNCTION: Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre- mRNA. {ECO:0000269|PubMed:12165565, ECO:0000269|PubMed:12761049, ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:9546399}.; . TISSUE SPECIFICITY: Highest expression in heart, skeletal muscle and pancreas. Less abundant in kidney, placenta and brain. Lowest expression in kidney and liver. {ECO:0000269|PubMed:9790768}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; testis - interstitial;superior cervical ganglion;placenta;testis;white blood cells; 0.75274 0.17050 -0.053113545 49.38664779 5.13222 0.19019 TRABD 0.931187268796145 0.0687419970922608 7.07341115944045e-05 TraB domain containing . . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;breast;lung;placenta;macula lutea;hippocampus;liver;duodenum;spleen;kidney;mammary gland;stomach; superior cervical ganglion;white blood cells; 0.09237 0.10524 -1.177506449 5.944798301 26.69584 0.86364 TRABD2A 7.93859484463642e-10 0.076608436291908 0.923391562914233 TraB domain containing 2A FUNCTION: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway by mediating the cleavage of the 8 N- terminal residues of a subset of Wnt proteins. Following cleavage, Wnt proteins become oxidized and form large disulfide-bond oligomers, leading to their inactivation. Able to cleave WNT3A, WNT5, but not WNT11. Required for head formation. {ECO:0000269|PubMed:22726442}.; . . . . . . 0.220536484 68.38287332 1002.1007 6.09721 TRABD2B 0.370916244398265 0.48000352074106 0.149080234860675 TraB domain containing 2B FUNCTION: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway by mediating the cleavage of the 8 N- terminal residues of a subset of Wnt proteins. Following cleavage, Wnt proteins become oxidized and form large disulfide-bond oligomers, leading to their inactivation. Able to cleave WNT3A, WNT5, but not WNT11. Required for head formation. {ECO:0000269|PubMed:22726442}.; . . . . . . . . 725.47613 5.34688 TRAC . . . T-cell receptor alpha constant . DISEASE: Immunodeficiency 7 (IMD7) [MIM:615387]: A primary immunodeficiency disorder manifesting with recurrent respiratory infections, candidiasis, diarrhea, and failure to thrive. Patients show a clear predisposition to herpes viral infections, and features of immune dysregulation, including hypereosinophilia, vitiligo, and alopecia areata. Other features include lymphadenopathy and hepatosplenomegaly. CD3+ T-cells express TCR- gamma/delta, but little or no TCR-alpha/beta. {ECO:0000269|PubMed:21206088}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . . . . . . TRADD 0.680264799376384 0.315202115020167 0.00453308560344866 TNFRSF1A-associated via death domain FUNCTION: The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A (By similarity). Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD. Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B. {ECO:0000250}.; . TISSUE SPECIFICITY: Found in all examined tissues.; unclassifiable (Anatomical System);lymphoreticular;ovary;heart;islets of Langerhans;colon;parathyroid;blood;choroid;skin;bone marrow;uterus;prostate;lung;frontal lobe;oesophagus;bone;thyroid;placenta;liver;testis;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.34992 0.37635 . . 32.78301 1.01778 TRAF1 0.0567442890552586 0.924957598264007 0.0182981126807341 TNF receptor associated factor 1 FUNCTION: Adapter molecule that regulates the activation of NF- kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein- ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2. {ECO:0000269|PubMed:10692572, ECO:0000269|PubMed:16323247, ECO:0000269|PubMed:18429822, ECO:0000269|PubMed:19287455, ECO:0000269|PubMed:19698991, ECO:0000269|PubMed:20385093}.; . . . . 0.16078 0.39498 0.088260113 60.56853031 268.96464 3.51805 TRAF2 0.996480874852948 0.0035188975992449 2.27547807455537e-07 TNF receptor associated factor 2 FUNCTION: Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'- linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin- protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR. In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE. {ECO:0000269|PubMed:10346818, ECO:0000269|PubMed:11907583, ECO:0000269|PubMed:12917689, ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15383523, ECO:0000269|PubMed:18981220, ECO:0000269|PubMed:19150425, ECO:0000269|PubMed:19506082, ECO:0000269|PubMed:19810754, ECO:0000269|PubMed:19918265, ECO:0000269|PubMed:19937093, ECO:0000269|PubMed:20047764, ECO:0000269|PubMed:20064526, ECO:0000269|PubMed:20385093, ECO:0000269|PubMed:20577214, ECO:0000269|PubMed:23453969}.; . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;tongue;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.39305 0.18672 -0.822919685 11.76574664 53.16107 1.44762 TRAF3 0.998405668636195 0.00159429837692958 3.29868750364486e-08 TNF receptor associated factor 3 FUNCTION: Regulates pathways leading to the activation of NF- kappa-B and MAP kinases, and plays a central role in the regulation of B-cell survival. Part of signaling pathways leading to the production of cytokines and interferon. Required for normal antibody isotype switching from IgM to IgG. Plays a role T-cell dependent immune responses. Plays a role in the regulation of antiviral responses. Is an essential constituent of several E3 ubiquitin-protein ligase complexes. May have E3 ubiquitin-protein ligase activity and promote 'Lys-63'-linked ubiquitination of target proteins. Inhibits activation of NF-kappa-B in response to LTBR stimulation. Inhibits TRAF2-mediated activation of NF-kappa- B. Down-regulates proteolytic processing of NFKB2, and thereby inhibits non-canonical activation of NF-kappa-B. Promotes ubiquitination and proteasomal degradation of MAP3K14. {ECO:0000269|PubMed:15084608, ECO:0000269|PubMed:15383523, ECO:0000269|PubMed:17991829, ECO:0000269|PubMed:19937093, ECO:0000269|PubMed:20097753, ECO:0000269|PubMed:20185819}.; DISEASE: Herpes simplex encephalitis 3 (HSE3) [MIM:614849]: A rare complication of human herpesvirus 1 (HHV-1) infection, occurring in only a small minority of HHV-1 infected individuals. HSE is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Onset is over several days and involves fever, headache, seizures, stupor, and often coma, frequently with a fatal outcome. {ECO:0000269|PubMed:20832341}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;blood;skin;bone marrow;breast;uterus;lung;frontal lobe;bone;placenta;visual apparatus;iris;alveolus;testis;germinal center;kidney;brain;stomach; dorsal root ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14445 0.29831 -0.446304853 24.33356924 2274.16138 8.81729 TRAF3IP1 0.000159261765651607 0.998428634136735 0.00141210409761361 TRAF3 interacting protein 1 FUNCTION: Plays an inhibitory role on IL13 signaling by binding to IL13RA1. Involved in suppression of IL13-induced STAT6 phosphorylation, transcriptional activity and DNA-binding. Recruits TRAF3 and DISC1 to the microtubules. Involved in kidney development and epithelial morphogenesis. Involved in the regulation of microtubule cytoskeleton organization. Is a negative regulator of microtubule stability, acting through the control of MAP4 levels (PubMed:26487268). Involved in ciliogenesis (By similarity). {ECO:0000250|UniProtKB:Q149C2, ECO:0000269|PubMed:10791955, ECO:0000269|PubMed:12812986, ECO:0000269|PubMed:12935900, ECO:0000269|PubMed:26487268}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12935900}.; . . 0.12870 0.10423 0.958999345 90.17456947 2279.71515 8.83594 TRAF3IP2 7.10960921485341e-05 0.978762258283528 0.0211666456243239 TRAF3 interacting protein 2 FUNCTION: Could be involved in the activation of both NF-kappa-B via a NF-kappa-B inhibitor kinase (IKK)-dependent mechanism and stress-activated protein kinase (SAPK)/JNK.; DISEASE: Candidiasis, familial, 8 (CANDF8) [MIM:615527]: A primary immunodeficiency disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans. {ECO:0000269|PubMed:24120361}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;iris;testis;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;spinal cord;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; prostate;superior cervical ganglion;adipose tissue;lung;placenta;ciliary ganglion;trigeminal ganglion; 0.08849 0.10617 1.287903524 93.83698986 858.65823 5.71579 TRAF3IP2-AS1 . . . TRAF3IP2 antisense RNA 1 . . . . . . . . . . . TRAF3IP3 1.3764917816926e-06 0.989497508753741 0.0105011147544776 TRAF3 interacting protein 3 FUNCTION: May function as an adapter molecule that regulates TRAF3-mediated JNK activation. {ECO:0000250}.; . . smooth muscle;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;tongue;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;aorta;thymus; subthalamic nucleus;lymph node;white blood cells;ciliary ganglion;atrioventricular node;whole blood;trigeminal ganglion;tonsil;thymus; 0.25181 0.12101 0.286674996 71.49681529 267.89298 3.51107 TRAF4 0.840038712273208 0.159831706228219 0.000129581498573071 TNF receptor associated factor 4 FUNCTION: Adapter protein and signal transducer that links members of the tumor necrosis factor receptor (TNFR) family to different signaling pathways. Plays a role in the activation of NF-kappa-B and JNK, and in the regulation of cell survival and apoptosis. Regulates activation of NF-kappa-B in response to signaling through Toll-like receptors. Required for normal skeleton development, and for normal development of the respiratory tract (By similarity). Required for activation of RPS6KB1 in response to TNF signaling. Modulates TRAF6 functions. {ECO:0000250, ECO:0000269|PubMed:12023963, ECO:0000269|PubMed:12801526, ECO:0000269|PubMed:16052631, ECO:0000269|PubMed:16157600, ECO:0000269|PubMed:18953416, ECO:0000269|PubMed:19937093}.; . TISSUE SPECIFICITY: Expressed in epithelial cells of thymus, dendritic cells of lymph node, and in the basal cell layer of epithelia such as epidermis, nasopharynx, respiratory tract, salivary gland, and esophagus. {ECO:0000269|PubMed:7592751, ECO:0000269|PubMed:9626059}.; lymphoreticular;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;muscle;urinary;lens;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;amnion;hypopharynx;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; tumor;trigeminal ganglion; 0.35071 0.20238 -0.404032746 26.53338051 39.67284 1.16916 TRAF5 8.829041147296e-06 0.925326371922777 0.0746647990360753 TNF receptor associated factor 5 FUNCTION: Adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. Mediates activation of NF-kappa-B and probably JNK. Seems to be involved in apoptosis. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR. {ECO:0000269|PubMed:15121867}.; . TISSUE SPECIFICITY: Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon, and peripheral blood.; smooth muscle;colon;parathyroid;skin;uterus;prostate;endometrium;larynx;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; . 0.08401 0.16123 -0.045835247 50.34206181 216.64914 3.18150 TRAF6 0.996923826264077 0.00307600986682074 1.63869102024427e-07 TNF receptor associated factor 6 FUNCTION: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation. Leads to the activation of NF-kappa-B and JUN. May be essential for the formation of functional osteoclasts. Seems to also play a role in dendritic cells (DCs) maturation and/or activation. Represses c- Myb-mediated transactivation, in B-lymphocytes. Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor. Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation. Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production. {ECO:0000269|PubMed:11057907, ECO:0000269|PubMed:12140561, ECO:0000269|PubMed:16378096, ECO:0000269|PubMed:17135271, ECO:0000269|PubMed:18093978, ECO:0000269|PubMed:18347055, ECO:0000269|PubMed:18758450, ECO:0000269|PubMed:19465916, ECO:0000269|PubMed:19675569, ECO:0000269|PubMed:19713527, ECO:0000269|PubMed:8837778}.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; unclassifiable (Anatomical System);cartilage;heart;colon;parathyroid;blood;skin;bone marrow;uterus;whole body;lung;larynx;placenta;visual apparatus;liver;alveolus;testis;head and neck;spleen;germinal center;spinal ganglion;brain;artery;stomach;aorta; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.33466 0.59535 -0.538132194 20.26421326 18.25202 0.63438 TRAF6P1 . . . TNF receptor associated factor 6 pseudogene 1 . . . . . . . . . . . TRAF7 0.460647228032184 0.539342814019469 9.95794834731222e-06 TNF receptor associated factor 7 FUNCTION: E3 ubiquitin ligase capable of auto-ubiquitination, following phosphorylation by MAP3K3. Potentiates MEKK3-mediated activation of the NF-kappa-B, JUN/AP1 and DDIT3 transcriptional regulators. Induces apoptosis when overexpressed. {ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:15001576}.; . TISSUE SPECIFICITY: Ubiquitously expressed with high levels in skeletal muscle, heart, colon, spleen, kidney, liver and placenta. {ECO:0000269|PubMed:15001576}.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; . 0.16599 0.14085 -1.50825116 3.503184713 28.55417 0.91487 TRAFD1 1.82691525643369e-05 0.970465577523013 0.0295161533244227 TRAF-type zinc finger domain containing 1 FUNCTION: Negative feedback regulator that controls excessive innate immune responses. Regulates both Toll-like receptor 4 (TLR4) and DDX58/RIG1-like helicases (RLH) pathways. May inhibit the LTR pathway by direct interaction with TRAF6 and attenuation of NF-kappa-B activation. May negatively regulate the RLH pathway downstream from MAVS and upstream of NF-kappa-B and IRF3 (By similarity). {ECO:0000250, ECO:0000269|PubMed:16221674}.; . . myocardium;ovary;salivary gland;sympathetic chain;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;muscle;pharynx;blood;lens;breast;pancreas;lung;nasopharynx;macula lutea;hippocampus;alveolus;liver;cervix;spleen;kidney;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.07103 0.09821 -0.201976964 38.98325077 125.66239 2.44050 TRAIP 0.125103591601554 0.874686280303504 0.000210128094942192 TRAF interacting protein FUNCTION: Inhibits activation of NF-kappa-B mediated by TNF (By similarity). Negatively regulates TLR3/4- and RIG-I-mediated IRF3 activation and subsequent IFN-beta production and cellular antiviral response by promoting 'Lys-48'-linked polyubiquitination of TNK1 leading to its proteasomal degradation. May mediate assembly of 'Lys-63'-linked poly-ubiquitin chains on the Y-family polymerase POLN to facilitate bypass of DNA lesions and preserve genomic integrity. {ECO:0000250, ECO:0000269|PubMed:22945920, ECO:0000269|PubMed:24553286}.; . . unclassifiable (Anatomical System);lymph node;cartilage;ovary;colon;blood;vein;skin;skeletal muscle;bile duct;whole body;lung;alveolus;liver;testis;brain;stomach; testis - seminiferous tubule;parietal lobe; 0.07595 0.08015 -0.358119787 29.16371786 41.29921 1.20740 TRAJ1 . . . T cell receptor alpha joining 1 (non-functional) . . . . . . . . . . . TRAJ2 . . . T cell receptor alpha joining 2 (non-functional) . . . . . . . . . . . TRAJ3 . . . T cell receptor alpha joining 3 . . . . . . . . . . . TRAJ4 . . . T cell receptor alpha joining 4 . . . . . . . . . . . TRAJ5 . . . T cell receptor alpha joining 5 . . . . . . . . . . . TRAJ6 . . . T cell receptor alpha joining 6 . . . . . . . . . . . TRAJ7 . . . T cell receptor alpha joining 7 . . . . . . . . . . . TRAJ8 . . . T cell receptor alpha joining 8 . . . . . . . . . . . TRAJ9 . . . T cell receptor alpha joining 9 . . . . . . . . . . . TRAJ10 . . . T cell receptor alpha joining 10 . . . . . . . . . . . TRAJ11 . . . T cell receptor alpha joining 11 . . . . . . . . . . . TRAJ12 . . . T cell receptor alpha joining 12 . . . . . . . . . . . TRAJ13 . . . T cell receptor alpha joining 13 . . . . . . . . . . . TRAJ14 . . . T cell receptor alpha joining 14 . . . . . . . . . . . TRAJ15 . . . T cell receptor alpha joining 15 . . . . . . . . . . . TRAJ16 . . . T cell receptor alpha joining 16 . . . . . . . . . . . TRAJ17 . . . T cell receptor alpha joining 17 . . . . . . . . . . . TRAJ18 . . . T cell receptor alpha joining 18 . . . . . . . . . . . TRAJ19 . . . T cell receptor alpha joining 19 (non-functional) . . . . . . . . . . . TRAJ20 . . . T cell receptor alpha joining 20 . . . . . . . . . . . TRAJ21 . . . T cell receptor alpha joining 21 . . . . . . . . . . . TRAJ22 . . . T cell receptor alpha joining 22 . . . . . . . . . . . TRAJ23 . . . T cell receptor alpha joining 23 . . . . . . . . . . . TRAJ24 . . . T cell receptor alpha joining 24 . . . . . . . . . . . TRAJ25 . . . T cell receptor alpha joining 25 (non-functional) . . . . . . . . . . . TRAJ26 . . . T cell receptor alpha joining 26 . . . . . . . . . . . TRAJ27 . . . T cell receptor alpha joining 27 . . . . . . . . . . . TRAJ28 . . . T cell receptor alpha joining 28 . . . . . . . . . . . TRAJ29 . . . T cell receptor alpha joining 29 . . . . . . . . . . . TRAJ30 . . . T cell receptor alpha joining 30 . . . . . . . . . . . TRAJ31 . . . T cell receptor alpha joining 31 . . . . . . . . . . . TRAJ32 . . . T cell receptor alpha joining 32 . . . . . . . . . . . TRAJ33 . . . T cell receptor alpha joining 33 . . . . . . . . . . . TRAJ34 . . . T cell receptor alpha joining 34 . . . . . . . . . . . TRAJ35 . . . T cell receptor alpha joining 35 (non-functional) . . . . . . . . . . . TRAJ36 . . . T cell receptor alpha joining 36 . . . . . . . . . . . TRAJ37 . . . T cell receptor alpha joining 37 . . . . . . . . . . . TRAJ38 . . . T cell receptor alpha joining 38 . . . . . . . . . . . TRAJ39 . . . T cell receptor alpha joining 39 . . . . . . . . . . . TRAJ40 . . . T cell receptor alpha joining 40 . . . . . . . . . . . TRAJ41 . . . T cell receptor alpha joining 41 . . . . . . . . . . . TRAJ42 . . . T cell receptor alpha joining 42 . . . . . . . . . . . TRAJ43 . . . T cell receptor alpha joining 43 . . . . . . . . . . . TRAJ44 . . . T cell receptor alpha joining 44 . . . . . . . . . . . TRAJ45 . . . T cell receptor alpha joining 45 . . . . . . . . . . . TRAJ46 . . . T cell receptor alpha joining 46 . . . . . . . . . . . TRAJ47 . . . T cell receptor alpha joining 47 . . . . . . . . . . . TRAJ48 . . . T cell receptor alpha joining 48 . . . . . . . . . . . TRAJ49 . . . T cell receptor alpha joining 49 . . . . . . . . . . . TRAJ50 . . . T cell receptor alpha joining 50 . . . . . . . . . . . TRAJ51 . . . T cell receptor alpha joining 51 (pseudogene) . . . . . . . . . . . TRAJ52 . . . T cell receptor alpha joining 52 . . . . . . . . . . . TRAJ53 . . . T cell receptor alpha joining 53 . . . . . . . . . . . TRAJ54 . . . T cell receptor alpha joining 54 . . . . . . . . . . . TRAJ55 . . . T cell receptor alpha joining 55 (pseudogene) . . . . . . . . . . . TRAJ56 . . . T cell receptor alpha joining 56 . . . . . . . . . . . TRAJ57 . . . T cell receptor alpha joining 57 . . . . . . . . . . . TRAJ58 . . . T cell receptor alpha joining 58 (non-functional) . . . . . . . . . . . TRAJ59 . . . T cell receptor alpha joining 59 (non-functional) . . . . . . . . . . . TRAJ60 . . . T cell receptor alpha joining 60 (pseudogene) . . . . . . . . . . . TRAJ61 . . . T cell receptor alpha joining 61 (non-functional) . . . . . . . . . . . TRAK1 9.70917112523944e-05 0.999320129188996 0.000582779099751659 trafficking protein, kinesin binding 1 FUNCTION: Involved in the regulation of endosome-to-lysosome trafficking, including endocytic trafficking of EGF-EGFR complexes and GABA-A receptors. {ECO:0000269|PubMed:18675823}.; . TISSUE SPECIFICITY: High expression in spinal cord and moderate expression in all other tissues and specific brain regions examined. Expressed in all cell lines examined. {ECO:0000269|PubMed:18986759}.; smooth muscle;ovary;skin;retina;prostate;frontal lobe;endometrium;cochlea;thyroid;germinal center;brain;heart;cartilage;tongue;pineal body;urinary;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;pia mater;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; amygdala;dorsal root ganglion;occipital lobe;superior cervical ganglion;cerebellum peduncles;spinal cord;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.20920 0.09269 -1.427629082 4.039867893 256.2546 3.44430 TRAK2 6.92274497111198e-10 0.992008460301184 0.00799153900654194 trafficking protein, kinesin binding 2 FUNCTION: May regulate endosome-to-lysosome trafficking of membrane cargo, including EGFR. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in heart.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;spinal cord;blood;lens;skeletal muscle;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;fetal liver;spinal cord;prefrontal cortex;pons;trigeminal ganglion;parietal lobe;cingulate cortex; 0.69833 0.11157 -0.461076406 23.66124086 1369.53075 6.94398 TRAM1 0.676696973918678 0.323104393762673 0.000198632318648363 translocation associated membrane protein 1 FUNCTION: Stimulatory or required for the translocation of secretory proteins across the ER membrane.; . . myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;gum;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; superior cervical ganglion;testis - interstitial;adipose tissue;trachea;thyroid;testis; 0.36253 0.15628 -0.139478553 43.29440906 145.55137 2.62875 TRAM1L1 0.0302314470646564 0.808735445457456 0.161033107477888 translocation associated membrane protein 1-like 1 FUNCTION: Stimulatory or required for the translocation of secretory proteins across the ER membrane. {ECO:0000250}.; . . unclassifiable (Anatomical System);cochlea;hypothalamus;testis;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.08261 0.08578 -0.560178693 19.30879925 15.10402 0.54309 TRAM2 0.99535786489498 0.00464168766873501 4.47436285268589e-07 translocation associated membrane protein 2 FUNCTION: Necessary for collagen type I synthesis. May couple the activity of the ER Ca(2+) pump SERCA2B with the activity of the translocon. This coupling may increase the local Ca(2+) concentration at the site of collagen synthesis, and a high Ca(2+) concentration may be necessary for the function of molecular chaperones involved in collagen folding. {ECO:0000269|PubMed:14749390}.; . . medulla oblongata;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;bone;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;spinal cord;blood;lens;skeletal muscle;bile duct;breast;pancreas;pia mater;lung;mesenchyma;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;adipose tissue;placenta;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.46939 0.14896 -0.494039303 22.09247464 19.90664 0.67803 TRAM2-AS1 . . . TRAM2 antisense RNA 1 (head to head) . . . . . . . . . . . TRANK1 2.79379160018064e-10 0.999751705125009 0.000248294595612052 tetratricopeptide repeat and ankyrin repeat containing 1 . . . lymphoreticular;ovary;colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;bone;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;stomach;cerebellum; dorsal root ganglion;subthalamic nucleus;uterus corpus;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; . . -3.561263122 0.306676103 1646.02843 7.49870 TRAP1 1.62037604789736e-17 0.0116611631402985 0.988338836859702 TNF receptor-associated protein 1 FUNCTION: Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, most likely through stabilization of mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA. {ECO:0000269|PubMed:23525905, ECO:0000269|PubMed:23564345, ECO:0000269|PubMed:23747254}.; . TISSUE SPECIFICITY: Found in skeletal muscle, liver, heart, brain, kidney, pancreas, lung, placenta and bladder. Expression is higly reduced in bladder cancer and renal cell carcinoma specimens compared to healthy tissues, but it is increased in other type of tumors. {ECO:0000269|PubMed:23564345}.; lymphoreticular;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;oesophagus;bone;lymph;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;placenta;duodenum;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;subthalamic nucleus;liver;globus pallidus;pons;parietal lobe;skeletal muscle; 0.38695 0.12579 -0.338129542 30.07784855 2265.0957 8.79536 TRAPPC1 0.227722384643837 0.73729568318767 0.0349819321684937 trafficking protein particle complex 1 FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi.; . . lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;oesophagus;bone;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus; . 0.41073 . -0.09720619 46.20193442 0.98111 0.02472 TRAPPC2 0.624929855815672 0.343802955065991 0.0312671891183372 trafficking protein particle complex 2 FUNCTION: Prevents transcriptional repression and induction of cell death by ENO1 (By similarity). May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, pancreas, placenta, skeletal muscle, fetal cartilage, fibroblasts, placenta and lymphocytes. {ECO:0000269|PubMed:10431248}.; ovary;colon;choroid;fovea centralis;skin;bone marrow;retina;uterus;optic nerve;whole body;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;lens;skeletal muscle;lung;macula lutea;liver;spleen;cervix;kidney;stomach; testis - interstitial;medulla oblongata;prefrontal cortex;testis;ciliary ganglion;atrioventricular node; . 0.35467 0.12325821 62.38499646 2.07232 0.06713 TRAPPC2B . . . trafficking protein particle complex 2B FUNCTION: Prevents transcriptional repression and induction of cell death by ENO1. May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000269|PubMed:11134351}.; . TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, pancreas, placenta, skeletal muscle, fetal cartilage, fibroblasts, placenta and lymphocytes. {ECO:0000269|PubMed:10431248}.; . . . 0.35467 . . . . TRAPPC2L 3.55188444434469e-05 0.366706264173725 0.633258216981831 trafficking protein particle complex 2-like FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000269|PubMed:19416478}.; . TISSUE SPECIFICITY: Expressed in testis, liver, bladder, lung, spleen and brain, several cell lines and primary chondrocytes cell line. {ECO:0000269|PubMed:19416478}.; ovary;umbilical cord;salivary gland;intestine;colon;parathyroid;choroid;skin;uterus;prostate;whole body;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;skeletal muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;kidney; testis - interstitial;testis - seminiferous tubule;adrenal gland;temporal lobe;liver;adrenal cortex;globus pallidus;testis;trigeminal ganglion;parietal lobe; 0.16800 0.11303 -0.117432389 44.89266336 675.36078 5.19076 TRAPPC2P2 . . . trafficking protein particle complex 2 pseudogene 2 . . . . . . . . . . . TRAPPC2P3 . . . trafficking protein particle complex 2 pseudogene 3 . . . . . . . . . . . TRAPPC2P4 . . . trafficking protein particle complex 2 pseudogene 4 . . . . . . . . . . . TRAPPC2P5 . . . trafficking protein particle complex 2 pseudogene 5 . . . . . . . . . . . TRAPPC2P6 . . . trafficking protein particle complex 2 pseudogene 6 . . . . . . . . . . . TRAPPC2P7 . . . trafficking protein particle complex 2 pseudogene 7 . . . . . . . . . . . TRAPPC2P8 . . . trafficking protein particle complex 2 pseudogene 8 . . . . . . . . . . . TRAPPC2P9 . . . trafficking protein particle complex 2 pseudogene 9 . . . . . . . . . . . TRAPPC2P10 . . . trafficking protein particle complex 2 pseudogene 10 . . . . . . . . . . . TRAPPC3 0.810539219939377 0.184721063897328 0.00473971616329502 trafficking protein particle complex 3 FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi.; . . . . 0.49655 0.13588 -0.009020804 52.8544468 8.56449 0.31349 TRAPPC3L . . . trafficking protein particle complex 3 like FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.; . . . . 0.26932 0.11506 -0.185391282 39.67916962 75.27538 1.81476 TRAPPC4 0.0013236960271552 0.860223980127891 0.138452323844954 trafficking protein particle complex 4 FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi.; . . lymphoreticular;ovary;umbilical cord;skin;bone marrow;prostate;frontal lobe;endometrium;gum;thyroid;germinal center;brain;bladder;gall bladder;heart;cartilage;tongue;pineal body;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;bone;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta;thymus; thalamus;superior cervical ganglion;testis - seminiferous tubule;testis;trigeminal ganglion; 0.05423 0.14482 -0.273576253 33.97027601 2062.8687 8.36784 TRAPPC5 0.577704358866904 0.378155376800817 0.0441402643322796 trafficking protein particle complex 5 FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;liver;testis; 0.10554 . 0.125076652 62.7388535 3201.34637 10.78338 TRAPPC6A 0.000705277787371492 0.515006127773684 0.484288594438944 trafficking protein particle complex 6A FUNCTION: May play a role in vesicular transport during the biogenesis of melanosomes. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;synovium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;urinary;adrenal cortex;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;liver;trigeminal ganglion; 0.22269 0.10469 -0.049474214 50.01179523 46.51998 1.31637 TRAPPC6B 0.0219802776295562 0.909478044226309 0.0685416781441349 trafficking protein particle complex 6B FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.; . . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;pituitary gland;testis;amniotic fluid;brain;gall bladder;unclassifiable (Anatomical System);heart;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;hippocampus;visual apparatus;cervix;kidney;mammary gland;stomach;aorta; . 0.20547 0.11809 -0.207437529 38.2814343 12.07771 0.43744 TRAPPC8 0.999999744151836 2.55848163729659e-07 1.55831401213203e-19 trafficking protein particle complex 8 FUNCTION: May be involved in endoplasmic reticulum to Golgi apparatus trafficking at a very early stage. {ECO:0000269|PubMed:21525244}.; . . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;atrium;whole body;thyroid;bone;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;breast;pia mater;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;peripheral nerve; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;caudate nucleus;atrioventricular node; 0.14990 0.09632 0.721954055 85.86341118 3775.56161 12.03543 TRAPPC9 5.76038953455576e-06 0.999937759228747 5.64803817187735e-05 trafficking protein particle complex 9 FUNCTION: Functions as an activator of NF-kappa-B through increased phosphorylation of the IKK complex. May function in neuronal cells differentiation. May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000269|PubMed:15951441}.; . TISSUE SPECIFICITY: Expressed at high levels in muscle and kidney and to a lower extent in brain, heart and placenta. {ECO:0000269|PubMed:15951441}.; . . 0.16663 . -1.648170405 2.77188016 502.77101 4.60031 TRAPPC10 0.999998954037007 1.04596299238513e-06 1.17507356446102e-16 trafficking protein particle complex 10 FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi.; . TISSUE SPECIFICITY: Expressed in all tissues examined.; lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; amygdala;thalamus;medulla oblongata;superior cervical ganglion;prefrontal cortex;testis;pons;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle; 0.31677 0.14310 -1.585603802 3.119839585 1748.14819 7.71890 TRAPPC11 0.000208772147312059 0.999790902039895 3.25812792551243e-07 trafficking protein particle complex 11 FUNCTION: Involved in endoplasmic reticulum to Golgi apparatus trafficking at a very early stage. {ECO:0000269|PubMed:21525244}.; DISEASE: Limb-girdle muscular dystrophy 2S (LGMD2S) [MIM:615356]: A form of limb-girdle muscular dystrophy characterized by proximal muscle weakness with childhood onset, resulting in gait abnormalities and scapular winging. Serum creatine kinase is increased. A subset of patients may show a hyperkinetic movement disorder with chorea, ataxia, or dystonia and global developmental delay. {ECO:0000269|PubMed:23830518}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;urinary;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09223 0.10585 -0.966362676 8.993866478 2235.74353 8.71699 TRAPPC12 1.34328496197278e-09 0.338273470374303 0.661726528282412 trafficking protein particle complex 12 FUNCTION: May be involved in endoplasmic reticulum to Golgi apparatus trafficking at a very early stage. {ECO:0000269|PubMed:21525244}.; . . medulla oblongata;ovary;colon;fovea centralis;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;thyroid;testis; 0.08376 0.10180 -0.393118976 27.05237084 5654.49689 15.55726 TRAPPC12-AS1 . . . TRAPPC12 antisense RNA 1 . . . . . . . . . . . TRAPPC13 0.765500289091919 0.234124474031234 0.000375236876846653 trafficking protein particle complex 13 . . . . . . 0.10825 0.12689526 63.00424628 72.15214 1.76947 TRAPPC13P1 . . . trafficking protein particle complex 13 pseudogene 1 . . . . . . . . . . . TRAT1 0.486401716946783 0.50883095158136 0.00476733147185699 T cell receptor associated transmembrane adaptor 1 FUNCTION: Stabilizes the TCR (T-cell antigen receptor)/CD3 complex at the surface of T-cells. {ECO:0000269|PubMed:11390434}.; . TISSUE SPECIFICITY: Strongly expressed in thymus, and to a lesser extent in spleen, lymph node and peripheral blood lymphocytes. Present in T-cells and NK cells, but not B-cells (at protein level). {ECO:0000269|PubMed:16160011, ECO:0000269|PubMed:9687533}.; pancreas;nasopharynx;liver;stomach;bone marrow; superior cervical ganglion;skeletal muscle; 0.32684 0.22751 0.527368849 80.73248408 164.28937 2.79839 TRAV1-1 . . . T cell receptor alpha variable 1-1 . . . . . . . . . . . TRAV1-2 . . . T cell receptor alpha variable 1-2 . . . . . . . . . . . TRAV2 . . . T cell receptor alpha variable 2 . . . . . . . . . . . TRAV3 . . . T cell receptor alpha variable 3 (gene/pseudogene) . . . . . . . . . . . TRAV4 . . . T cell receptor alpha variable 4 . . . . . . . . . . . TRAV5 . . . T cell receptor alpha variable 5 . . . . . . . . . . . TRAV6 . . . T cell receptor alpha variable 6 . . . . . . . . . . . TRAV7 . . . T cell receptor alpha variable 7 . . . . . . . . . . . TRAV8-1 . . . T cell receptor alpha variable 8-1 . . . . . . . . . . . TRAV8-2 . . . T cell receptor alpha variable 8-2 . . . . . . . . . . . TRAV8-3 . . . T cell receptor alpha variable 8-3 . . . . . . . . . . . TRAV8-4 . . . T cell receptor alpha variable 8-4 . . . . . . . . . . . TRAV8-5 . . . T cell receptor alpha variable 8-5 (pseudogene) . . . . . . . . . . . TRAV8-6 . . . T cell receptor alpha variable 8-6 . . . . . . . . . . . TRAV8-7 . . . T cell receptor alpha variable 8-7 (non-functional) . . . . . . . . . . . TRAV9-1 . . . T cell receptor alpha variable 9-1 . . . . . . . . . . . TRAV9-2 . . . T cell receptor alpha variable 9-2 . . . . . . . . . . . TRAV10 . . . T cell receptor alpha variable 10 . . . . . . . . . . . TRAV11 . . . T cell receptor alpha variable 11 (pseudogene) . . . . . . . . . . . TRAV12-1 . . . T cell receptor alpha variable 12-1 . . . . . . . . . . . TRAV12-2 . . . T cell receptor alpha variable 12-2 . . . . . . . . . . . TRAV12-3 . . . T cell receptor alpha variable 12-3 . . . . . . . . . . . TRAV13-1 . . . T cell receptor alpha variable 13-1 . . . . . . . . . . . TRAV13-2 . . . T cell receptor alpha variable 13-2 . . . . . . . . . . . TRAV14DV4 . . . T cell receptor alpha variable 14/delta variable 4 . . . . . . . . . . . TRAV15 . . . T cell receptor alpha variable 15 (pseudogene) . . . . . . . . . . . TRAV16 . . . T cell receptor alpha variable 16 . . . . . . . . . . . TRAV17 . . . T cell receptor alpha variable 17 . . . . . . . . . . . TRAV18 . . . T cell receptor alpha variable 18 . . . . . . . . . . . TRAV19 . . . T cell receptor alpha variable 19 . . . . . . . . . . . TRAV20 . . . T cell receptor alpha variable 20 . . . . . . . . . . . TRAV21 . . . T cell receptor alpha variable 21 . . . . . . . . . . . TRAV22 . . . T cell receptor alpha variable 22 . . . . . . . . . . . TRAV23DV6 . . . T cell receptor alpha variable 23/delta variable 6 . . . . . . . . . . . TRAV24 . . . T cell receptor alpha variable 24 . . . . . . . . . . . TRAV25 . . . T cell receptor alpha variable 25 . . . . . . . . . . . TRAV26-1 . . . T cell receptor alpha variable 26-1 . . . . . . . . . . . TRAV26-2 . . . T cell receptor alpha variable 26-2 . . . . . . . . . . . TRAV27 . . . T cell receptor alpha variable 27 . . . . . . . . . . . TRAV28 . . . T cell receptor alpha variable 28 (pseudogene) . . . . . . . . . . . TRAV29DV5 . . . T cell receptor alpha variable 29/delta variable 5 (gene/pseudogene) . . . . . . . . . . . TRAV30 . . . T cell receptor alpha variable 30 . . . . . . . . . . . TRAV31 . . . T cell receptor alpha variable 31 (pseudogene) . . . . . . . . . . . TRAV32 . . . T cell receptor alpha variable 32 (pseudogene) . . . . . . . . . . . TRAV33 . . . T cell receptor alpha variable 33 (pseudogene) . . . . . . . . . . . TRAV34 . . . T cell receptor alpha variable 34 . . . . . . . . . . . TRAV35 . . . T cell receptor alpha variable 35 . . . . . . . . . . . TRAV36DV7 . . . T cell receptor alpha variable 36/delta variable 7 . . . . . . . . . . . TRAV37 . . . T cell receptor alpha variable 37 (pseudogene) . . . . . . . . . . . TRAV38-1 . . . T cell receptor alpha variable 38-1 . . . . . . . . . . . TRAV38-2DV8 . . . T cell receptor alpha variable 38-2/delta variable 8 . . . . . . . . . . . TRAV39 . . . T cell receptor alpha variable 39 . . . . . . . . . . . TRAV40 . . . T cell receptor alpha variable 40 . . . . . . . . . . . TRAV41 . . . T cell receptor alpha variable 41 . . . . . . . . . . . TRB . . . T cell receptor beta locus . . . . . . . . . . . TRBC1 . . . T cell receptor beta constant 1 . . . . . . . . . . . TRBC2 . . . T cell receptor beta constant 2 . . . . . . . . . . . TRBD1 . . . T cell receptor beta diversity 1 . . . . . . . . . . . TRBD2 . . . T cell receptor beta diversity 2 . . . . . . . . . . . TRBJ1-1 . . . T cell receptor beta joining 1-1 . . . . . . . . . . . TRBJ1-2 . . . T cell receptor beta joining 1-2 . . . . . . . . . . . TRBJ1-3 . . . T cell receptor beta joining 1-3 . . . . . . . . . . . TRBJ1-4 . . . T cell receptor beta joining 1-4 . . . . . . . . . . . TRBJ1-5 . . . T cell receptor beta joining 1-5 . . . . . . . . . . . TRBJ1-6 . . . T cell receptor beta joining 1-6 . . . . . . . . . . . TRBJ2-1 . . . T cell receptor beta joining 2-1 . . . . . . . . . . . TRBJ2-2 . . . T cell receptor beta joining 2-2 . . . . . . . . . . . TRBJ2-2P . . . T cell receptor beta joining 2-2P (non-functional) . . . . . . . . . . . TRBJ2-3 . . . T cell receptor beta joining 2-3 . . . . . . . . . . . TRBJ2-4 . . . T cell receptor beta joining 2-4 . . . . . . . . . . . TRBJ2-5 . . . T cell receptor beta joining 2-5 . . . . . . . . . . . TRBJ2-6 . . . T cell receptor beta joining 2-6 . . . . . . . . . . . TRBJ2-7 . . . T cell receptor beta joining 2-7 . . . . . . . . . . . TRBV1 . . . T cell receptor beta variable 1 (pseudogene) . . . . . . . . . . . TRBV2 . . . T cell receptor beta variable 2 . . . . . . . . . . . TRBV3-1 . . . T cell receptor beta variable 3-1 . . . . . . . . . . . TRBV3-2 . . . T cell receptor beta variable 3-2 (pseudogene) . . . . . . . . . . . TRBV4-1 . . . T cell receptor beta variable 4-1 . . . . . . . . . . . TRBV4-2 . . . T cell receptor beta variable 4-2 . . . . . . . . . . . TRBV4-3 . . . T cell receptor beta variable 4-3 . . . . . . . . . . . TRBV5-1 . . . T cell receptor beta variable 5-1 . . . . . . . . . . . TRBV5-2 . . . T cell receptor beta variable 5-2 (pseudogene) . . . . . . . . . . . TRBV5-3 . . . T cell receptor beta variable 5-3 (non-functional) . . . . . . . . . . . TRBV5-4 . . . T cell receptor beta variable 5-4 . . . . . . . . . . . TRBV5-5 . . . T cell receptor beta variable 5-5 . . . . . . . . . . . TRBV5-6 . . . T cell receptor beta variable 5-6 . . . . . . . . . . . TRBV5-7 . . . T cell receptor beta variable 5-7 (non-functional) . . . . . . . . . . . TRBV5-8 . . . T cell receptor beta variable 5-8 . . . . . . . . . . . TRBV6-1 . . . T cell receptor beta variable 6-1 . . . . . . . . . . . TRBV6-2 . . . T cell receptor beta variable 6-2 (gene/pseudogene) . . . . . . . . . . . TRBV6-3 . . . T cell receptor beta variable 6-3 . . . . . . . . . . . TRBV6-4 . . . T cell receptor beta variable 6-4 . . . . . . . . . . . TRBV6-5 . . . T cell receptor beta variable 6-5 . . . . . . . . . . . TRBV6-6 . . . T cell receptor beta variable 6-6 . . . . . . . . . . . TRBV6-7 . . . T cell receptor beta variable 6-7 (non-functional) . . . . . . . . . . . TRBV6-8 . . . T cell receptor beta variable 6-8 . . . . . . . . . . . TRBV6-9 . . . T cell receptor beta variable 6-9 . . . . . . . . . . . TRBV7-1 . . . T cell receptor beta variable 7-1 (non-functional) . . . . . . . . . . . TRBV7-2 . . . T cell receptor beta variable 7-2 . . . . . . . . . . . TRBV7-3 . . . T cell receptor beta variable 7-3 . . . . . . . . . . . TRBV7-4 . . . T cell receptor beta variable 7-4 (gene/pseudogene) . . . . . . . . . . . TRBV7-5 . . . T cell receptor beta variable 7-5 (pseudogene) . . . . . . . . . . . TRBV7-6 . . . T cell receptor beta variable 7-6 . . . . . . . . . . . TRBV7-7 . . . T cell receptor beta variable 7-7 . . . . . . . . . . . TRBV7-8 . . . T cell receptor beta variable 7-8 . . . . . . . . . . . TRBV7-9 . . . T cell receptor beta variable 7-9 . . . . . . . . . . . TRBV8-1 . . . T cell receptor beta variable 8-1 (pseudogene) . . . . . . . . . . . TRBV8-2 . . . T cell receptor beta variable 8-2 (pseudogene) . . . . . . . . . . . TRBV9 . . . T cell receptor beta variable 9 . . . . . . . . . . . TRBV10-1 . . . T cell receptor beta variable 10-1(gene/pseudogene) . . . . . . . . . . . TRBV10-2 . . . T cell receptor beta variable 10-2 . . . . . . . . . . . TRBV10-3 . . . T cell receptor beta variable 10-3 . . . . . . . . . . . TRBV11-1 . . . T cell receptor beta variable 11-1 . . . . . . . . . . . TRBV11-2 . . . T cell receptor beta variable 11-2 . . . . . . . . . . . TRBV11-3 . . . T cell receptor beta variable 11-3 . . . . . . . . . . . TRBV12-1 . . . T cell receptor beta variable 12-1 (pseudogene) . . . . . . . . . . . TRBV12-2 . . . T cell receptor beta variable 12-2 (pseudogene) . . . . . . . . . . . TRBV12-3 . . . T cell receptor beta variable 12-3 . . . . . . . . . . . TRBV12-4 . . . T cell receptor beta variable 12-4 . . . . . . . . . . . TRBV12-5 . . . T cell receptor beta variable 12-5 . . . . . . . . . . . TRBV13 . . . T cell receptor beta variable 13 . . . . . . . . . . . TRBV14 . . . T cell receptor beta variable 14 . . . . . . . . . . . TRBV15 . . . T cell receptor beta variable 15 . . . . . . . . . . . TRBV16 . . . T cell receptor beta variable 16 (gene/pseudogene) . . . . . . . . . . . TRBV17 . . . T cell receptor beta variable 17 (non-functional) . . . . . . . . . . . TRBV18 . . . T cell receptor beta variable 18 . . . . . . . . . . . TRBV19 . . . T cell receptor beta variable 19 . . . . . . . . . . . TRBV20-1 . . . T cell receptor beta variable 20-1 . . . . . . . . . . . TRBV20OR9-2 . . . T cell receptor beta variable 20/OR9-2 (non-functional) . . . . . . . . . . . TRBV21-1 . . . T cell receptor beta variable 21-1 (pseudogene) . . . . . . . . . . . TRBV21OR9-2 . . . T cell receptor beta variable 21/OR9-2 (pseudogene) . . . . . . . . . . . TRBV22-1 . . . T cell receptor beta variable 22-1 (pseudogene) . . . . . . . . . . . TRBV22OR9-2 . . . T cell receptor beta variable 22/OR9-2 (pseudogene) . . . . . . . . . . . TRBV23-1 . . . T cell receptor beta variable 23-1 (non-functional) . . . . . . . . . . . TRBV23OR9-2 . . . T cell receptor beta variable 23/OR9-2 (non-functional) . . . . . . . . . . . TRBV24-1 . . . T cell receptor beta variable 24-1 . . . . . . . . . . . TRBV24OR9-2 . . . T cell receptor beta variable 24/OR9-2 (pseudogene) . . . . . . . . . . . TRBV25-1 . . . T cell receptor beta variable 25-1 . . . . . . . . . . . TRBV25OR9-2 . . . T cell receptor beta variable 25/OR9-2 (pseudogene) . . . . . . . . . . . TRBV26 . . . T cell receptor beta variable 26 (pseudogene) . . . . . . . . . . . TRBV26OR9-2 . . . T cell receptor beta variable 26/OR9-2 (pseudogene) . . . . . . . . . . . TRBV27 . . . T cell receptor beta variable 27 . . . . . . . . . . . TRBV28 . . . T cell receptor beta variable 28 . . . . . . . . . . . TRBV29-1 . . . T cell receptor beta variable 29-1 . . . . . . . . . . . TRBV29OR9-2 . . . T cell receptor beta variable 29/OR9-2 (non-functional) . . . . . . . . . . . TRBV30 . . . T cell receptor beta variable 30 (gene/pseudogene) . . . . . . . . . . . TRBVA . . . T cell receptor beta variable A (pseudogene) . . . . . . . . . . . TRBVAOR9-2 . . . T cell receptor beta variable A/OR9-2 (pseudogene) . . . . . . . . . . . TRBVB . . . T cell receptor beta variable B (pseudogene) . . . . . . . . . . . TRBVC . . . T cell receptor beta variable C . . . . . . . . . . . TRC-ACA1-1 . . . transfer RNA-Cys (ACA) 1-1 . . . . . . . . . . . TRC-GCA1-1 . . . transfer RNA-Cys (GCA) 1-1 . . . . . . . . . . . TRC-GCA2-1 . . . transfer RNA-Cys (GCA) 2-1 . . . . . . . . . . . TRC-GCA2-2 . . . transfer RNA-Cys (GCA) 2-2 . . . . . . . . . . . TRC-GCA2-3 . . . transfer RNA-Cys (GCA) 2-3 . . . . . . . . . . . TRC-GCA2-4 . . . transfer RNA-Cys (GCA) 2-4 . . . . . . . . . . . TRC-GCA3-1 . . . transfer RNA-Cys (GCA) 3-1 . . . . . . . . . . . TRC-GCA4-1 . . . transfer RNA-Cys (GCA) 4-1 . . . . . . . . . . . TRC-GCA5-1 . . . transfer RNA-Cys (GCA) 5-1 . . . . . . . . . . . TRC-GCA6-1 . . . transfer RNA-Cys (GCA) 6-1 . . . . . . . . . . . TRC-GCA7-1 . . . transfer RNA-Cys (GCA) 7-1 . . . . . . . . . . . TRC-GCA8-1 . . . transfer RNA-Cys (GCA) 8-1 . . . . . . . . . . . TRC-GCA9-1 . . . transfer RNA-Cys (GCA) 9-1 . . . . . . . . . . . TRC-GCA9-2 . . . transfer RNA-Cys (GCA) 9-2 . . . . . . . . . . . TRC-GCA9-3 . . . transfer RNA-Cys (GCA) 9-3 . . . . . . . . . . . TRC-GCA9-4 . . . transfer RNA-Cys (GCA) 9-4 . . . . . . . . . . . TRC-GCA10-1 . . . transfer RNA-Cys (GCA) 10-1 . . . . . . . . . . . TRC-GCA11-1 . . . transfer RNA-Cys (GCA) 11-1 . . . . . . . . . . . TRC-GCA12-1 . . . transfer RNA-Cys (GCA) 12-1 . . . . . . . . . . . TRC-GCA13-1 . . . transfer RNA-Cys (GCA) 13-1 . . . . . . . . . . . TRC-GCA14-1 . . . transfer RNA-Cys (GCA) 14-1 . . . . . . . . . . . TRC-GCA15-1 . . . transfer RNA-Cys (GCA) 15-1 . . . . . . . . . . . TRC-GCA16-1 . . . transfer RNA-Cys (GCA) 16-1 . . . . . . . . . . . TRC-GCA17-1 . . . transfer RNA-Cys (GCA) 17-1 . . . . . . . . . . . TRC-GCA18-1 . . . transfer RNA-Cys (GCA) 18-1 . . . . . . . . . . . TRC-GCA19-1 . . . transfer RNA-Cys (GCA) 19-1 . . . . . . . . . . . TRC-GCA20-1 . . . transfer RNA-Cys (GCA) 20-1 . . . . . . . . . . . TRC-GCA21-1 . . . transfer RNA-Cys (GCA) 21-1 . . . . . . . . . . . TRC-GCA22-1 . . . transfer RNA-Cys (GCA) 22-1 . . . . . . . . . . . TRC-GCA23-1 . . . transfer RNA-Cys (GCA) 23-1 . . . . . . . . . . . TRC-GCA24-1 . . . transfer RNA-Cys (GCA) 24-1 . . . . . . . . . . . TRC-GCA25-1 . . . transfer RNA-Cys (GCA) 25-1 . . . . . . . . . . . TRD . . . T cell receptor delta locus . . . . . . . . . . . TRD-GTC1-1 . . . transfer RNA-Asp (GTC) 1-1 . . . . . . . . . . . TRD-GTC2-1 . . . transfer RNA-Asp (GTC) 2-1 . . . . . . . . . . . TRD-GTC2-2 . . . transfer RNA-Asp (GTC) 2-2 . . . . . . . . . . . TRD-GTC2-3 . . . transfer RNA-Asp (GTC) 2-3 . . . . . . . . . . . TRD-GTC2-4 . . . transfer RNA-Asp (GTC) 2-4 . . . . . . . . . . . TRD-GTC2-5 . . . transfer RNA-Asp (GTC) 2-5 . . . . . . . . . . . TRD-GTC2-6 . . . transfer RNA-Asp (GTC) 2-6 . . . . . . . . . . . TRD-GTC2-7 . . . transfer RNA-Asp (GTC) 2-7 . . . . . . . . . . . TRD-GTC2-8 . . . transfer RNA-Asp (GTC) 2-8 . . . . . . . . . . . TRD-GTC2-9 . . . transfer RNA-Asp (GTC) 2-9 . . . . . . . . . . . TRD-GTC2-10 . . . transfer RNA-Asp (GTC) 2-10 . . . . . . . . . . . TRD-GTC2-11 . . . transfer RNA-Asp (GTC) 2-11 . . . . . . . . . . . TRD-GTC3-1 . . . transfer RNA-Asp (GTC) 3-1 . . . . . . . . . . . TRD-GTC4-1 . . . transfer RNA-Asp (GTC) 4-1 . . . . . . . . . . . TRD-GTC5-1 . . . transfer RNA-Asp (GTC) 5-1 . . . . . . . . . . . TRD-GTC6-1 . . . transfer RNA-Asp (GTC) 6-1 . . . . . . . . . . . TRD-GTC7-1 . . . transfer RNA-Asp (GTC) 7-1 . . . . . . . . . . . TRD-GTC8-1 . . . transfer RNA-Asp (GTC) 8-1 . . . . . . . . . . . TRD-GTC9-1 . . . transfer RNA-Asp (GTC) 9-1 . . . . . . . . . . . TRD-GTC10-1 . . . transfer RNA-Asp (GTC) 10-1 . . . . . . . . . . . TRDC . . . T cell receptor delta constant . . . . . . . . . . . TRDD1 . . . T cell receptor delta diversity 1 . . . . . . . . . . . TRDD2 . . . T cell receptor delta diversity 2 . . . . . . . . . . . TRDD3 . . . T cell receptor delta diversity 3 . . . . . . . . . . . TRDJ1 . . . T cell receptor delta joining 1 . . . . . . . . . . . TRDJ2 . . . T cell receptor delta joining 2 . . . . . . . . . . . TRDJ3 . . . T cell receptor delta joining 3 . . . . . . . . . . . TRDJ4 . . . T cell receptor delta joining 4 . . . . . . . . . . . TRDMT1 1.67244828325926e-06 0.652469860033631 0.347528467518086 tRNA aspartic acid methyltransferase 1 FUNCTION: Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp). {ECO:0000269|PubMed:16424344}.; . TISSUE SPECIFICITY: Ubiquitous. Higher expression in testis, ovary and thymus and at much lower levels in spleen, prostate, colon, small intestine, and peripheral blood leukocytes.; unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;blood;lens;skin;retina;uterus;breast;prostate;lung;bone;liver;testis;spleen;kidney;brain; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.05384 0.16298 0.086440867 60.47416844 107.74647 2.25409 TRDN 1.81677623808329e-10 0.826941440119538 0.173058559698784 triadin FUNCTION: Contributes to the regulation of lumenal Ca2+ release via the sarcoplasmic reticulum calcium release channels RYR1 and RYR2, a key step in triggering skeletal and heart muscle contraction. Required for normal organization of the triad junction, where T-tubules and the sarcoplasmic reticulum terminal cisternae are in close contact (By similarity). Required for normal skeletal muscle strength. Plays a role in excitation- contraction coupling in the heart and in regulating the rate of heart beats. {ECO:0000250|UniProtKB:E9Q9K5, ECO:0000269|PubMed:22422768}.; DISEASE: Ventricular tachycardia, catecholaminergic polymorphic, 5, with or without muscle weakness (CPVT5) [MIM:615441]: An arrhythmogenic disorder characterized by stress-induced, bidirectional ventricular tachycardia that may degenerate into cardiac arrest and cause sudden death. Patients present with recurrent syncope, or sudden death after physical activity or emotional stress. Some patients have muscle weakness. {ECO:0000269|PubMed:22422768}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lung;whole body;macula lutea;developmental;liver;testis;fovea centralis;skeletal muscle;retina; subthalamic nucleus;superior cervical ganglion;tongue;thyroid;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.18235 0.15914 1.976952171 97.61146497 4408.1144 13.27537 TRDV1 . . . T cell receptor delta variable 1 . . . . . . . . . . . TRDV2 . . . T cell receptor delta variable 2 . . . . . . . . . . . TRDV3 . . . T cell receptor delta variable 3 . . . . . . . . . . . TRE-CTC1-1 . . . transfer RNA-Glu (CTC) 1-1 . . . . . . . . . . . TRE-CTC1-2 . . . transfer RNA-Glu (CTC) 1-2 . . . . . . . . . . . TRE-CTC1-3 . . . transfer RNA-Glu (CTC) 1-3 . . . . . . . . . . . TRE-CTC1-4 . . . transfer RNA-Glu (CTC) 1-4 . . . . . . . . . . . TRE-CTC1-5 . . . transfer RNA-Glu (CTC) 1-5 . . . . . . . . . . . TRE-CTC1-6 . . . transfer RNA-Glu (CTC) 1-6 . . . . . . . . . . . TRE-CTC1-7 . . . transfer RNA-Glu (CTC) 1-7 . . . . . . . . . . . TRE-CTC2-1 . . . transfer RNA-Glu (CTC) 2-1 . . . . . . . . . . . TRE-CTC3-1 . . . transfer RNA-Glu (CTC) 3-1 . . . . . . . . . . . TRE-CTC4-1 . . . transfer RNA-Glu (CTC) 4-1 . . . . . . . . . . . TRE-CTC5-1 . . . transfer RNA-Glu (CTC) 5-1 . . . . . . . . . . . TRE-CTC6-1 . . . transfer RNA-Glu (CTC) 6-1 . . . . . . . . . . . TRE-CTC7-1 . . . transfer RNA-Glu (CTC) 7-1 . . . . . . . . . . . TRE-CTC8-1 . . . transfer RNA-Glu (CTC) 8-1 . . . . . . . . . . . TRE-CTC9-1 . . . transfer RNA-Glu (CTC) 9-1 . . . . . . . . . . . TRE-CTC10-1 . . . transfer RNA-Glu (CTC) 10-1 . . . . . . . . . . . TRE-CTC11-1 . . . transfer RNA-Glu (CTC) 11-1 . . . . . . . . . . . TRE-CTC12-1 . . . transfer RNA-Glu (CTC) 12-1 . . . . . . . . . . . TRE-CTC13-1 . . . transfer RNA-Glu (CTC) 13-1 . . . . . . . . . . . TRE-CTC14-1 . . . transfer RNA-Glu (CTC) 14-1 . . . . . . . . . . . TRE-CTC15-1 . . . transfer RNA-Glu (CTC) 15-1 . . . . . . . . . . . TRE-CTC16-1 . . . transfer RNA-Glu (CTC) 16-1 . . . . . . . . . . . TRE-CTC17-1 . . . transfer RNA-Glu (CTC) 17-1 . . . . . . . . . . . TRE-CTC18-1 . . . transfer RNA-Glu (CTC) 18-1 . . . . . . . . . . . TRE-TTC1-1 . . . transfer RNA-Glu (TTC) 1-1 . . . . . . . . . . . TRE-TTC1-2 . . . transfer RNA-Glu (TTC) 1-2 . . . . . . . . . . . TRE-TTC2-1 . . . transfer RNA-Glu (TTC) 2-1 . . . . . . . . . . . TRE-TTC2-2 . . . transfer RNA-Glu (TTC) 2-2 . . . . . . . . . . . TRE-TTC3-1 . . . transfer RNA-Glu (TTC) 3-1 . . . . . . . . . . . TRE-TTC4-1 . . . transfer RNA-Glu (TTC) 4-1 . . . . . . . . . . . TRE-TTC4-2 . . . transfer RNA-Glu (TTC) 4-2 . . . . . . . . . . . TRE-TTC5-1 . . . transfer RNA-Glu (TTC) 5-1 . . . . . . . . . . . TRE-TTC6-1 . . . transfer RNA-Glu (TTC) 6-1 . . . . . . . . . . . TRE-TTC7-1 . . . transfer RNA-Glu (TTC) 7-1 . . . . . . . . . . . TRE-TTC8-1 . . . transfer RNA-Glu (TTC) 8-1 . . . . . . . . . . . TRE-TTC9-1 . . . transfer RNA-Glu (TTC) 9-1 . . . . . . . . . . . TRE-TTC10-1 . . . transfer RNA-Glu (TTC) 10-1 . . . . . . . . . . . TRE-TTC11-1 . . . transfer RNA-Glu (TTC) 11-1 . . . . . . . . . . . TRE-TTC12-1 . . . transfer RNA-Glu (TTC) 12-1 . . . . . . . . . . . TRE-TTC13-1 . . . transfer RNA-Glu (TTC) 13-1 . . . . . . . . . . . TRE-TTC14-1 . . . transfer RNA-Glu (TTC) 14-1 . . . . . . . . . . . TRE-TTC15-1 . . . transfer RNA-Glu (TTC) 15-1 . . . . . . . . . . . TRE-TTC16-1 . . . transfer RNA-Glu (TTC) 16-1 . . . . . . . . . . . TREH 1.40028647894894e-14 0.0122572954397676 0.987742704560218 trehalase FUNCTION: Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose.; DISEASE: Note=Deficiency of TREH results in isolated trehalose intolerance that causes gastrointestinal symptoms after ingestion of edible mushrooms.; . testis;kidney; subthalamic nucleus;cerebellum peduncles;temporal lobe;liver;globus pallidus;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.34705 0.42521 . . 1343.85236 6.88180 TREHP1 . . . trehalase pseudogene 1 . . . . . . . . . . . TREM1 0.000343966174620477 0.600401942258406 0.399254091566974 triggering receptor expressed on myeloid cells 1 FUNCTION: Stimulates neutrophil and monocyte-mediated inflammatory responses. Triggers release of pro-inflammatory chemokines and cytokines, as well as increased surface expression of cell activation markers. Amplifier of inflammatory responses that are triggered by bacterial and fungal infections and is a crucial mediator of septic shock. {ECO:0000269|PubMed:10799849, ECO:0000269|PubMed:11323674}.; . TISSUE SPECIFICITY: Highly expressed in adult liver, lung and spleen than in corresponding fetal tissue. Also expressed in the lymph node, placenta, spinal cord and heart tissues. Expression is more elevated in peripheral blood leukocytes than in the bone marrow and in normal cells than malignant cells. Expressed at low levels in the early development of the hematopoietic system and in the promonocytic stage and at high levels in mature monocytes. Strongly expressed in acute inflammatory lesions caused by bacteria and fungi. Isoform 2 was detected in the lung, liver and mature monocytes. {ECO:0000269|PubMed:10799849, ECO:0000269|PubMed:11922939}.; unclassifiable (Anatomical System);cartilage;urinary;colon;blood;bone marrow;uterus;lung;placenta;bone;hypopharynx;testis;head and neck;brain; whole blood; 0.01380 0.06769 0.41713504 76.95800896 27.33486 0.88020 TREM2 2.35316946822257e-08 0.0415952658761505 0.958404710592155 triggering receptor expressed on myeloid cells 2 FUNCTION: May have a role in chronic inflammations and may stimulate production of constitutive rather than inflammatory chemokines and cytokines. Forms a receptor signaling complex with TYROBP and triggers activation of the immune responses in macrophages and dendritic cells. {ECO:0000269|PubMed:10799849}.; . TISSUE SPECIFICITY: Expressed on macrophages and dendritic cells but not on granulocytes or monocytes. In the CNS strongest expression seen in the basal ganglia, corpus callosum, medulla oblongata and spinal cord. {ECO:0000269|PubMed:10799849, ECO:0000269|PubMed:12080485}.; placenta;kidney;brain; subthalamic nucleus;lung;ciliary ganglion;atrioventricular node; 0.04385 0.15520 0.483275131 79.25218212 446.17961 4.39760 TREML1 1.00255175928297e-05 0.340818060653513 0.659171913828894 triggering receptor expressed on myeloid cells like 1 FUNCTION: Cell surface receptor that may play a role in the innate and adaptive immune response. {ECO:0000269|PubMed:15128762}.; . TISSUE SPECIFICITY: Detected in platelets, monocytic leukemia and in T-cell leukemia. {ECO:0000269|PubMed:12645956, ECO:0000269|PubMed:15100151, ECO:0000269|PubMed:15128762, ECO:0000269|PubMed:16505478}.; . . 0.08420 0.09783 0.328949044 73.41354093 277.94551 3.57180 TREML2 1.29204332519966e-07 0.110103456906203 0.889896413889464 triggering receptor expressed on myeloid cells like 2 FUNCTION: Cell surface receptor that may play a role in the innate and adaptive immune response. Acts as a counter-receptor for CD276 and interaction with CD276 on T-cells enhances T-cell activation. {ECO:0000269|PubMed:12645956, ECO:0000269|PubMed:18650384}.; . TISSUE SPECIFICITY: Detected in cultured B-cells, T-cell leukemia and monocyte leukemia. Expressed constitutively on CD8 T-cells and induced on CD4 T-cells after activation. {ECO:0000269|PubMed:12645956, ECO:0000269|PubMed:18650384}.; . . 0.03616 0.05941 1.728918179 96.55579146 640.99926 5.08852 TREML3P . . . triggering receptor expressed on myeloid cells like 3, pseudogene . . . . . 0.07482 . . . . . TREML4 2.78304131594225e-05 0.325851732704628 0.674120436882213 triggering receptor expressed on myeloid cells like 4 . . . . . 0.03829 . 0.971952656 90.26893135 173.3537 2.86745 TREML5P . . . triggering receptor expressed on myeloid cells like 5, pseudogene . . . . . . . . . . . TRERF1 0.999595776775278 0.000404223215078359 9.64370785934456e-12 transcriptional regulating factor 1 FUNCTION: Binds DNA and activates transcription of CYP11A1. Interaction with CREBBP and EP300 results in a synergistic transcriptional activation of CYP11A1. {ECO:0000269|PubMed:11349124, ECO:0000269|PubMed:16371131}.; . TISSUE SPECIFICITY: Highest expression was seen in thymus, testis and adrenal cortex, expressed also in the adrenal medulla, thyroid, and stomach. Highly expressed in steroidogenic JEG-3 and MCF-7 cells, low expression was seen in non-steroidogenic Hep-G2 and HEK293 cells. {ECO:0000269|PubMed:11349124}.; unclassifiable (Anatomical System);medulla oblongata;cartilage;ovary;colon;blood;skeletal muscle;retina;bone marrow;breast;lung;cochlea;nasopharynx;placenta;thyroid;bone;testis;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.81063 0.16220 0.745828079 86.38240151 1197.75907 6.56545 TRERNA1 . . . translation regulatory long non-coding RNA 1 . . . . . . . . . . . TREX1 0.093340719174628 0.767733119586948 0.138926161238424 three prime repair exonuclease 1 FUNCTION: Major cellular 3'-to-5' DNA exonuclease which digests single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) with mismatched 3' termini. Prevents cell-intrinsic initiation of autoimmunity. Acts by metabolizing DNA fragments from endogenous retroelements, including L1, LTR and SINE elements. Unless degraded, these DNA fragments accumulate in the cytosol and activate the IFN-stimulatory DNA (ISD) response and innate immune signaling. Prevents chronic ATM-dependent checkpoint activation, by processing ssDNA polynucleotide species arising from the processing of aberrant DNA replication intermediates. Inefficiently degrades oxidized DNA, such as that generated upon antimicrobial reactive oxygen production or upon absorption of UV light. During GZMA-mediated cell death, contributes to DNA damage in concert with NME1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair. {ECO:0000269|PubMed:10391904, ECO:0000269|PubMed:10393201, ECO:0000269|PubMed:16818237, ECO:0000269|PubMed:17293595, ECO:0000269|PubMed:18045533, ECO:0000269|PubMed:23993650}.; DISEASE: Aicardi-Goutieres syndrome 1 (AGS1) [MIM:225750]: A form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood. {ECO:0000269|PubMed:16845398, ECO:0000269|PubMed:17357087, ECO:0000269|PubMed:17846997, ECO:0000269|PubMed:20131292, ECO:0000269|PubMed:20799324}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:17660818, ECO:0000269|PubMed:20131292}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Enhanced immune sensing of oxidized DNA may be involved in the phototoxicity experienced by SLE patients. Exposure to UV- light produces DNA oxidative damage. Oxidized DNA being a poor TREX1 substrate, it accumulates in skin, leading to enhanced auto- immune reactivity and eventually skin lesions (PubMed:23993650). {ECO:0000269|PubMed:23993650}.; DISEASE: Chilblain lupus 1 (CHBL1) [MIM:610448]: A rare cutaneous form of lupus erythematosus. Affected individuals present with painful bluish-red papular or nodular lesions of the skin in acral locations precipitated by cold and wet exposure at temperatures less than 10 degrees centigrade. {ECO:0000269|PubMed:17357087, ECO:0000269|PubMed:17440703}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Vasculopathy, retinal, with cerebral leukodystrophy (RVCL) [MIM:192315]: A microvascular endotheliopathy resulting in central nervous system degeneration and retinopathy, with progressive loss of vision, stroke, motor impairment, and cognitive decline. The ocular manifestations are characterized by telangiectasias, microaneurysms and retinal capillary obliteration starting in the macula. Diseased cerebral white matter has prominent small infarcts that often coalesce to pseudotumors. {ECO:0000269|PubMed:17660820}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in thymus, spleen, liver, brain, heart, small intestine and colon. {ECO:0000269|PubMed:10393201, ECO:0000269|PubMed:11278605}.; ovary;salivary gland;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cerebral cortex;endometrium;larynx;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;pineal body;adrenal cortex;blood;skeletal muscle;lung;placenta;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; . 0.20525 -0.66859065 15.76433121 29.73233 0.94817 TREX2 0.126734816031738 0.615218331143832 0.25804685282443 three prime repair exonuclease 2 FUNCTION: Exonuclease with a preference for double-stranded DNA with mismatched 3' termini. May play a role in DNA repair. {ECO:0000269|PubMed:11279105}.; . TISSUE SPECIFICITY: Detected in heart, breast, prostate, skeletal muscle, testis, uterus, bone marrow, colon, small intestine, stomach and thymus. {ECO:0000269|PubMed:11278605}.; ovary;salivary gland;intestine;colon;skin;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;pharynx;blood;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.04290 . 0.483275131 79.25218212 45.04555 1.28880 TRF-GAA1-1 . . . transfer RNA-Phe (GAA) 1-1 . . . . . . . . . . . TRF-GAA1-2 . . . transfer RNA-Phe (GAA) 1-2 . . . . . . . . . . . TRF-GAA1-3 . . . transfer RNA-Phe (GAA) 1-3 . . . . . . . . . . . TRF-GAA1-4 . . . transfer RNA-Phe (GAA) 1-4 . . . . . . . . . . . TRF-GAA1-5 . . . transfer RNA-Phe (GAA) 1-5 . . . . . . . . . . . TRF-GAA1-6 . . . transfer RNA-Phe (GAA) 1-6 . . . . . . . . . . . TRF-GAA2-1 . . . transfer RNA-Phe (GAA) 2-1 . . . . . . . . . . . TRF-GAA3-1 . . . transfer RNA-Phe (GAA) 3-1 . . . . . . . . . . . TRF-GAA4-1 . . . transfer RNA-Phe (GAA) 4-1 . . . . . . . . . . . TRF-GAA5-1 . . . transfer RNA-Phe (GAA) 5-1 . . . . . . . . . . . TRF-GAA6-1 . . . transfer RNA-Phe (GAA) 6-1 . . . . . . . . . . . TRF-GAA7-1 . . . transfer RNA-Phe (GAA) 7-1 . . . . . . . . . . . TRF-GAA8-1 . . . transfer RNA-Phe (GAA) 8-1 . . . . . . . . . . . TRF-GAA9-1 . . . transfer RNA-Phe (GAA) 9-1 . . . . . . . . . . . TRF-GAA10-1 . . . transfer RNA-Phe (GAA) 10-1 . . . . . . . . . . . TRF-GAA11-1 . . . transfer RNA-Phe (GAA) 11-1 . . . . . . . . . . . TRF-GAA12-1 . . . transfer RNA-Phe (GAA) 12-1 . . . . . . . . . . . TRG . . . T cell receptor gamma locus . . . . . . . . . . . TRG-AS1 . . . T cell receptor gamma locus antisense RNA 1 . . . . . . . . . . . TRG-CCC1-1 . . . transfer RNA-Gly (CCC) 1-1 . . . . . . . . . . . TRG-CCC1-2 . . . transfer RNA-Gly (CCC) 1-2 . . . . . . . . . . . TRG-CCC2-1 . . . transfer RNA-Gly (CCC) 2-1 . . . . . . . . . . . TRG-CCC2-2 . . . transfer RNA-Gly (CCC) 2-2 . . . . . . . . . . . TRG-CCC3-1 . . . transfer RNA-Gly (CCC) 3-1 . . . . . . . . . . . TRG-CCC4-1 . . . transfer RNA-Gly (CCC) 4-1 . . . . . . . . . . . TRG-CCC5-1 . . . transfer RNA-Gly (CCC) 5-1 . . . . . . . . . . . TRG-CCC6-1 . . . transfer RNA-Gly (CCC) 6-1 . . . . . . . . . . . TRG-CCC7-1 . . . transfer RNA-Gly (CCC) 7-1 . . . . . . . . . . . TRG-CCC8-1 . . . transfer RNA-Gly (CCC) 8-1 . . . . . . . . . . . TRG-GCC1-1 . . . transfer RNA-Gly (GCC) 1-1 . . . . . . . . . . . TRG-GCC1-2 . . . transfer RNA-Gly (GCC) 1-2 . . . . . . . . . . . TRG-GCC1-3 . . . transfer RNA-Gly (GCC) 1-3 . . . . . . . . . . . TRG-GCC1-4 . . . transfer RNA-Gly (GCC) 1-4 . . . . . . . . . . . TRG-GCC1-5 . . . transfer RNA-Gly (GCC) 1-5 . . . . . . . . . . . TRG-GCC2-1 . . . transfer RNA-Gly (GCC) 2-1 . . . . . . . . . . . TRG-GCC2-2 . . . transfer RNA-Gly (GCC) 2-2 . . . . . . . . . . . TRG-GCC2-3 . . . transfer RNA-Gly (GCC) 2-3 . . . . . . . . . . . TRG-GCC2-4 . . . transfer RNA-Gly (GCC) 2-4 . . . . . . . . . . . TRG-GCC2-5 . . . transfer RNA-Gly (GCC) 2-5 . . . . . . . . . . . TRG-GCC2-6 . . . transfer RNA-Gly (GCC) 2-6 . . . . . . . . . . . TRG-GCC3-1 . . . transfer RNA-Gly (GCC) 3-1 . . . . . . . . . . . TRG-GCC4-1 . . . transfer RNA-Gly (GCC) 4-1 . . . . . . . . . . . TRG-GCC5-1 . . . transfer RNA-Gly (GCC) 5-1 . . . . . . . . . . . TRG-GCC6-1 . . . transfer RNA-Gly (GCC) 6-1 . . . . . . . . . . . TRG-TCC1-1 . . . transfer RNA-Gly (TCC) 1-1 . . . . . . . . . . . TRG-TCC2-1 . . . transfer RNA-Gly (TCC) 2-1 . . . . . . . . . . . TRG-TCC2-2 . . . transfer RNA-Gly (TCC) 2-2 . . . . . . . . . . . TRG-TCC2-3 . . . transfer RNA-Gly (TCC) 2-3 . . . . . . . . . . . TRG-TCC2-4 . . . transfer RNA-Gly (TCC) 2-4 . . . . . . . . . . . TRG-TCC2-5 . . . transfer RNA-Gly (TCC) 2-5 . . . . . . . . . . . TRG-TCC2-6 . . . transfer RNA-Gly (TCC) 2-6 . . . . . . . . . . . TRG-TCC3-1 . . . transfer RNA-Gly (TCC) 3-1 . . . . . . . . . . . TRG-TCC4-1 . . . transfer RNA-Gly (TCC) 4-1 . . . . . . . . . . . TRG-TCC5-1 . . . transfer RNA-Gly (TCC) 5-1 . . . . . . . . . . . TRG-TCC6-1 . . . transfer RNA-Gly (TCC) 6-1 . . . . . . . . . . . TRGC1 . . . T cell receptor gamma constant 1 . . . . . 0.11036 . . . . . TRGC2 . . . T cell receptor gamma constant 2 . . . . . . . . . . . TRGJ1 . . . T cell receptor gamma joining 1 . . . . . . . . . . . TRGJ2 . . . T cell receptor gamma joining 2 . . . . . . . . . . . TRGJP . . . T cell receptor gamma joining P . . . . . . . . . . . TRGJP1 . . . T cell receptor gamma joining P1 . . . . . . . . . . . TRGJP2 . . . T cell receptor gamma joining P2 . . . . . . . . . . . TRGV1 . . . T cell receptor gamma variable 1 (non-functional) . . . . . . . . . . . TRGV2 . . . T cell receptor gamma variable 2 . . . . . . . . . . . TRGV3 . . . T cell receptor gamma variable 3 . . . . . . . . . . . TRGV4 . . . T cell receptor gamma variable 4 . . . . . . . . . . . TRGV5 . . . T cell receptor gamma variable 5 . . . . . . . . . . . TRGV5P . . . T cell receptor gamma variable 5P (pseudogene) . . . . . . . . . . . TRGV6 . . . T cell receptor gamma variable 6 (pseudogene) . . . . . . . . . . . TRGV7 . . . T cell receptor gamma variable 7 (pseudogene) . . . . . . . . . . . TRGV8 . . . T cell receptor gamma variable 8 . . . . . . . . . . . TRGV9 . . . T cell receptor gamma variable 9 . . . . . 0.11036 . . . . . TRGV10 . . . T cell receptor gamma variable 10 (non-functional) . . . . . . . . . . . TRGV11 . . . T cell receptor gamma variable 11 (non-functional) . . . . . . . . . . . TRGVA . . . T cell receptor gamma variable A (pseudogene) . . . . . . . . . . . TRGVB . . . T cell receptor gamma variable B (pseudogene) . . . . . . . . . . . TRH 0.0108069146502521 0.834946658331332 0.154246427018416 thyrotropin releasing hormone FUNCTION: Functions as a regulator of the biosynthesis of TSH in the anterior pituitary gland and as a neurotransmitter/ neuromodulator in the central and peripheral nervous systems. May promote hair shaft elongation, prolonge the hair cycle growth phase (anagen) and antagonized its termination by TGFB2. May also increase proliferation and inhibited apoptosis of hair matrix keratinocytes. {ECO:0000269|PubMed:19825978}.; . TISSUE SPECIFICITY: Hypothalamus. Expressed in the hair follicle epithelium (at protein level). {ECO:0000269|PubMed:19825978}.; unclassifiable (Anatomical System);optic nerve;lung;macula lutea;visual apparatus;fovea centralis;brain;pineal gland; superior cervical ganglion;hypothalamus;ciliary ganglion;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.17607 0.27198 0.018483465 55.44939844 1442.66377 7.08353 TRH-GTG1-1 . . . transfer RNA-His (GTG) 1-1 . . . . . . . . . . . TRH-GTG1-2 . . . transfer RNA-His (GTG) 1-2 . . . . . . . . . . . TRH-GTG1-3 . . . transfer RNA-His (GTG) 1-3 . . . . . . . . . . . TRH-GTG1-4 . . . transfer RNA-His (GTG) 1-4 . . . . . . . . . . . TRH-GTG1-5 . . . transfer RNA-His (GTG) 1-5 . . . . . . . . . . . TRH-GTG1-6 . . . transfer RNA-His (GTG) 1-6 . . . . . . . . . . . TRH-GTG1-7 . . . transfer RNA-His (GTG) 1-7 . . . . . . . . . . . TRH-GTG1-8 . . . transfer RNA-His (GTG) 1-8 . . . . . . . . . . . TRH-GTG1-9 . . . transfer RNA-His (GTG) 1-9 . . . . . . . . . . . TRH-GTG2-1 . . . transfer RNA-His (GTG) 2-1 . . . . . . . . . . . TRH-GTG3-1 . . . transfer RNA-His (GTG) 3-1 . . . . . . . . . . . TRHDE 0.0809965086232841 0.919002749686245 7.41690470494467e-07 thyrotropin releasing hormone degrading enzyme FUNCTION: Specific inactivation of TRH after its release.; . TISSUE SPECIFICITY: Predominantly expressed in brain.; unclassifiable (Anatomical System);frontal lobe;placenta;visual apparatus;liver;kidney;brain;skin;skeletal muscle; whole brain;amygdala;subthalamic nucleus;occipital lobe;prefrontal cortex;globus pallidus;trigeminal ganglion; 0.53121 0.17806 -0.93133804 9.613116301 61.03637 1.58937 TRHDE-AS1 . . . TRHDE antisense RNA 1 . . . . . . . . . . . TRHR 0.265021780649127 0.709368272830992 0.0256099465198815 thyrotropin releasing hormone receptor FUNCTION: Receptor for thyrotropin-releasing hormone. This receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system.; . . unclassifiable (Anatomical System); superior cervical ganglion;trigeminal ganglion; 0.21970 0.22882 -0.293801652 32.93819297 23.76777 0.78551 TRI-AAT1-1 . . . transfer RNA-Ile (AAT) 1-1 . . . . . . . . . . . TRI-AAT2-1 . . . transfer RNA-Ile (AAT) 2-1 . . . . . . . . . . . TRI-AAT3-1 . . . transfer RNA-Ile (AAT) 3-1 . . . . . . . . . . . TRI-AAT4-1 . . . transfer RNA-Ile (AAT) 4-1 . . . . . . . . . . . TRI-AAT5-1 . . . transfer RNA-Ile (AAT) 5-1 . . . . . . . . . . . TRI-AAT5-2 . . . transfer RNA-Ile (AAT) 5-2 . . . . . . . . . . . TRI-AAT5-3 . . . transfer RNA-Ile (AAT) 5-3 . . . . . . . . . . . TRI-AAT5-4 . . . transfer RNA-Ile (AAT) 5-4 . . . . . . . . . . . TRI-AAT5-5 . . . transfer RNA-Ile (AAT) 5-5 . . . . . . . . . . . TRI-AAT6-1 . . . transfer RNA-Ile (AAT) 6-1 . . . . . . . . . . . TRI-AAT7-1 . . . transfer RNA-Ile (AAT) 7-1 . . . . . . . . . . . TRI-AAT7-2 . . . transfer RNA-Ile (AAT) 7-2 . . . . . . . . . . . TRI-AAT8-1 . . . transfer RNA-Ile (AAT) 8-1 . . . . . . . . . . . TRI-AAT9-1 . . . transfer RNA-Ile (AAT) 9-1 . . . . . . . . . . . TRI-AAT10-1 . . . transfer RNA-Ile (AAT) 10-1 . . . . . . . . . . . TRI-AAT11-1 . . . transfer RNA-Ile (AAT) 11-1 . . . . . . . . . . . TRI-AAT12-1 . . . transfer RNA-Ile (AAT) 12-1 . . . . . . . . . . . TRI-GAT1-1 . . . transfer RNA-Ile (GAT) 1-1 . . . . . . . . . . . TRI-GAT1-2 . . . transfer RNA-Ile (GAT) 1-2 . . . . . . . . . . . TRI-GAT1-3 . . . transfer RNA-Ile (GAT) 1-3 . . . . . . . . . . . TRI-TAT1-1 . . . transfer RNA-Ile (TAT) 1-1 . . . . . . . . . . . TRI-TAT2-1 . . . transfer RNA-Ile (TAT) 2-1 . . . . . . . . . . . TRI-TAT2-2 . . . transfer RNA-Ile (TAT) 2-2 . . . . . . . . . . . TRI-TAT2-3 . . . transfer RNA-Ile (TAT) 2-3 . . . . . . . . . . . TRI-TAT3-1 . . . transfer RNA-Ile (TAT) 3-1 . . . . . . . . . . . TRIAP1 0.590216383617478 0.369364166383354 0.0404194499991675 TP53 regulated inhibitor of apoptosis 1 FUNCTION: Involved in the modulation of the mitochondrial apoptotic pathway by ensuring the accumulation of cardiolipin (CL) in mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space to provide PA for CL synthesis in the inner membrane. Mediates cell survival by inhibiting activation of caspase-9 which prevents induction of apoptosis. {ECO:0000269|PubMed:15735003, ECO:0000269|PubMed:23931759}.; . . medulla oblongata;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;skin;uterus;prostate;oesophagus;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;kidney;mammary gland;stomach;thymus; . 0.15959 . 0.013025609 54.62962963 6.87534 0.25540 TRIAP1P1 . . . TP53 regulated inhibitor of apoptosis 1 pseudogene 1 . . . . . . . . . . . TRIB1 0.606587656595858 0.384728083741061 0.00868425966308136 tribbles pseudokinase 1 FUNCTION: Interacts with MAPK kinases and regulates activation of MAP kinases. May not display kinase activity. {ECO:0000269|PubMed:15299019, ECO:0000303|PubMed:15299019}.; . TISSUE SPECIFICITY: Expressed in most human tissues with the highest levels in skeletal muscle, thyroid gland, pancreas, peripheral blood leukocytes, and bone marrow. {ECO:0000269|PubMed:15299019}.; smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; thyroid; 0.62858 0.16645 . . 164.86587 2.80558 TRIB2 0.926787339017351 0.0728078247913857 0.000404836191263518 tribbles pseudokinase 2 FUNCTION: Interacts with MAPK kinases and regulates activation of MAP kinases. Does not display kinase activity (By similarity). {ECO:0000250|UniProtKB:Q28283, ECO:0000250|UniProtKB:Q96RU8}.; . TISSUE SPECIFICITY: Highly expressed in peripheral blood leukocytes. {ECO:0000269|PubMed:15299019}.; lymphoreticular;ovary;sympathetic chain;colon;skin;retina;uterus;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;skeletal muscle;lung;mesenchyma;adrenal gland;placenta;visual apparatus;liver;spleen;mammary gland;stomach; skeletal muscle; 0.22595 0.11039 -0.271755481 34.31823543 63.18149 1.62634 TRIB3 2.11620965891956e-10 0.0357710813157661 0.964228918472613 tribbles pseudokinase 3 FUNCTION: Disrupts insulin signaling by binding directly to Akt kinases and blocking their activation. May bind directly to and mask the 'Thr-308' phosphorylation site in AKT1. Binds to ATF4 and inhibits its transcriptional activation activity. Interacts with the NF-kappa-B transactivator p65 RELA and inhibits its phosphorylation and thus its transcriptional activation activity. Interacts with MAPK kinases and regulates activation of MAP kinases. May play a role in programmed neuronal cell death but does not appear to affect non-neuronal cells. Does not display kinase activity. Inhibits the transcriptional activity of DDIT3/CHOP and is involved in DDIT3/CHOP-dependent cell death during ER stress. Can inhibit APOBEC3A editing of nuclear DNA. {ECO:0000269|PubMed:12736262, ECO:0000269|PubMed:15299019, ECO:0000269|PubMed:15775988, ECO:0000269|PubMed:15781252, ECO:0000269|PubMed:22977230}.; . TISSUE SPECIFICITY: Highest expression in liver, pancreas, peripheral blood leukocytes and bone marrow. Also highly expressed in a number of primary lung, colon and breast tumors. Expressed in spleen, thymus, and prostate and is undetectable in other examined tissues, including testis, ovary, small intestine, colon, leukocyte, heart, brain, placenta, lung, skeletal muscle, and kidney. {ECO:0000269|PubMed:12736262, ECO:0000269|PubMed:12743605, ECO:0000269|PubMed:15299019}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;muscle;adrenal cortex;pharynx;blood;lens;breast;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion; 0.11951 0.09203 0.468503535 78.79806558 1469.51042 7.14292 TRICY1 . . . trichilemmal cyst 1 . . . . . . . . . . . TRIL . . . TLR4 interactor with leucine-rich repeats FUNCTION: Component of the TLR4 signaling complex. Mediate the innate immune response to bacterial lipopolysaccharide (LPS) leading to cytokine secretion. {ECO:0000269|PubMed:19710467}.; . TISSUE SPECIFICITY: Highly expressed in the brain, ovary, small intestine and spleen. {ECO:0000269|PubMed:19710467}.; . . . . . . . . TRIM2 0.894263856491426 0.105734370879872 1.77262870272631e-06 tripartite motif containing 2 FUNCTION: UBE2D1-dependent E3 ubiquitin-protein ligase that mediates the ubiquitination of NEFL and of phosphorylated BCL2L11. Plays a neuroprotective function. May play a role in neuronal rapid ischemic tolerance. {ECO:0000250}.; DISEASE: Charcot-Marie-Tooth disease 2R (CMT2R) [MIM:615490]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. {ECO:0000269|PubMed:23562820}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;hypothalamus;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;kidney; amygdala;dorsal root ganglion;superior cervical ganglion;occipital lobe;medulla oblongata;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;testis - seminiferous tubule;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.65392 0.10249 -1.109541557 6.782259967 17.93891 0.62719 TRIM3 0.952560875185986 0.0474379891275936 1.13568642081426e-06 tripartite motif containing 3 FUNCTION: Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation.; . TISSUE SPECIFICITY: Expressed in brain, heart, uterus and testis.; ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;iris;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;amnion;spleen;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;cerebellum peduncles;temporal lobe;pons;atrioventricular node;kidney;trigeminal ganglion;cingulate cortex;skeletal muscle;parietal lobe; 0.41195 0.15175 -1.199555187 5.761972163 44.30437 1.27061 TRIM4 1.68258188143666e-06 0.653781578188055 0.346216739230063 tripartite motif containing 4 FUNCTION: E3 ubiquitin-protein ligase. Mediates 'Lys-63'-linked polyubiquitination of the innate immune receptor DDX58, this linkage doesn't lead to proteasomal degradation but seems to enhance IFN induction. {ECO:0000269|PubMed:24755855}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;hippocampus;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.13331 0.09729 0.284856336 71.40835103 940.03842 5.94444 TRIM5 4.36970250918444e-08 0.362578824787844 0.637421131515131 tripartite motif containing 5 FUNCTION: Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF- kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Restricts infection by N-tropic murine leukemia virus (N-MLV), equine infectious anemia virus (EIAV), simian immunodeficiency virus of macaques (SIVmac), feline immunodeficiency virus (FIV), and bovine immunodeficiency virus (BIV) (PubMed:17156811). Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2 (PubMed:25127057). Also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction (PubMed:25127057). {ECO:0000269|PubMed:12878161, ECO:0000269|PubMed:17156811, ECO:0000269|PubMed:18312418, ECO:0000269|PubMed:21035162, ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:21632761, ECO:0000269|PubMed:22291694, ECO:0000269|PubMed:25127057}.; . . colon;parathyroid;skin;uterus;prostate;whole body;thyroid;brain;bladder;pineal gland;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;muscle;adrenal cortex;blood;breast;pancreas;adrenal gland;placenta;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; atrioventricular node;trigeminal ganglion; 0.05706 0.09513 1.201528238 93.00542581 4199.97046 12.87864 TRIM6 3.78638887641513e-10 0.313675510926698 0.686324488694664 tripartite motif containing 6 FUNCTION: E3 ubiquitin-protein ligase which ubiquitinates MYC and inhibits its transcription activation activity, maintaining the pluripotency of embryonic stem cells (By similarity). Involved in the synthesis of unanchored K48-linked polyubiquitin chains which interact with and activate the serine/threonine kinase IKBKE, leading to phosphorylation of STAT1 and stimulation of an antiviral response (PubMed:24882218). {ECO:0000250|UniProtKB:Q8BGE7, ECO:0000269|PubMed:24882218}.; . . unclassifiable (Anatomical System);ovary;heart;salivary gland;intestine;pharynx;colon;parathyroid;blood;skin;skeletal muscle;uterus;pancreas;whole body;lung;cornea;larynx;placenta;visual apparatus;liver;testis;head and neck;spleen;kidney;brain;mammary gland;stomach; . . 0.08111 0.512596355 80.29606039 691.94247 5.24614 TRIM6-TRIM34 2.30605194516737e-11 0.852282965755156 0.147717034221784 TRIM6-TRIM34 readthrough . . . colon;skin;skeletal muscle;pancreas;prostate;whole body;lung;endometrium;nasopharynx;placenta;liver;testis;spleen;germinal center;kidney;brain;stomach; . . . 0.518060413 80.35503657 774.88057 5.50962 TRIM7 0.0659400780546186 0.919521557229539 0.0145383647158427 tripartite motif containing 7 . . TISSUE SPECIFICITY: Skeletal muscle and placenta, at lower levels in heart, brain and pancreas. Isoform 1 is widely expressed with high level in testis, kidney and heart. {ECO:0000269|PubMed:14984203}.; unclassifiable (Anatomical System);salivary gland;colon;blood;skeletal muscle;skin;prostate;lung;liver;spleen;cervix;kidney;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11002 0.11045 . . 3130.80477 10.64982 TRIM8 0.992012340638519 0.00798597343568796 1.68592579353057e-06 tripartite motif containing 8 FUNCTION: Probable E3 ubiquitin-protein ligase which may promote proteasomal degradation of SOCS1. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;blood;lens;pancreas;lung;placenta;macula lutea;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.46682 0.12535 -0.560178693 19.30879925 88.13339 2.01031 TRIM9 0.987914427877689 0.0120846308178873 9.41304423653416e-07 tripartite motif containing 9 FUNCTION: E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation. {ECO:0000269|PubMed:20085810}.; . TISSUE SPECIFICITY: Brain. Highly expressed in the cerebral cortex (at protein level). Severely decreased in the affected brain areas in Parkinson disease and dementia with Lewy bodies. {ECO:0000269|PubMed:20085810}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cerebellum cortex;hypothalamus;pharynx;blood;lens;skeletal muscle;lung;cornea;macula lutea;hippocampus;visual apparatus;liver;kidney;mammary gland;cerebellum;peripheral nerve; whole brain;amygdala;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.25856 0.17179 -0.490397599 22.50530786 152.48629 2.70011 TRIM10 9.94954187768385e-06 0.789101466969017 0.210888583489105 tripartite motif containing 10 FUNCTION: Seems to play an important role in erythropoiesis. {ECO:0000250}.; . . . . 0.29691 . 0.955356963 90.10969568 1010.68416 6.12078 TRIM11 0.547146512887441 0.449870783185658 0.00298270392690127 tripartite motif containing 11 FUNCTION: E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle. {ECO:0000269|PubMed:18248090}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;spleen;kidney;cerebellum; superior cervical ganglion;globus pallidus; 0.71547 0.14012 -0.756778259 13.44656759 22.65172 0.75793 TRIM13 0.505141848020281 0.475898632234488 0.0189595197452307 tripartite motif containing 13 FUNCTION: E3 ubiquitin ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor. {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11363 0.16375 -0.359940251 28.93371078 49.60335 1.37936 TRIM14 0.0102131175441416 0.944125491166092 0.045661391289766 tripartite motif containing 14 FUNCTION: Inhibits the transcriptional activity of SPI1 in a dose- dependent manner. {ECO:0000250}.; . TISSUE SPECIFICITY: Highest expression in liver; undetectable in skeletal muscle.; ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;tongue;islets of Langerhans;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;liver;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;liver;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;thymus; 0.46820 . . . 17.89522 0.62539 TRIM15 2.18350911167555e-11 0.01820451965566 0.981795480322505 tripartite motif containing 15 . . . . . 0.09203 . 1.905343315 97.35786742 1710.45509 7.62665 TRIM16 0.000114778734848393 0.82731560267316 0.172569618591991 tripartite motif containing 16 FUNCTION: May play a role in the regulation of keratinocyte differentiation.; . TISSUE SPECIFICITY: Highest levels found in testis, ovary, small intestine, colon, placenta, heart, skeletal muscle and mammary gland. More highly expressed in the fetus than in the corresponding adult tissues. Expressed in basal keratinocytes.; ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;testis;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;adrenal cortex;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;stomach;aorta; . . . 0.022122107 55.69120075 533.07824 4.71057 TRIM16L 0.0168793918042221 0.888510716947344 0.0946098912484339 tripartite motif containing 16-like . . . . . 0.08566 . -0.135838822 43.77211607 1793.27214 7.81584 TRIM17 2.40298559120734e-05 0.744751518008637 0.255224452135451 tripartite motif containing 17 FUNCTION: May function as a ubiquitin E3 ligase. {ECO:0000269|PubMed:19358823}.; . TISSUE SPECIFICITY: Almost exclusively in the testis. {ECO:0000269|PubMed:19358823}.; unclassifiable (Anatomical System);medulla oblongata;lung;larynx;bone;urinary;testis;blood;head and neck;kidney;bone marrow; pons;skin;cingulate cortex; 0.10342 0.18426 -0.21856543 37.66218448 129.33213 2.47962 TRIM21 0.0930518154823646 0.898565880804652 0.00838230371298301 tripartite motif containing 21 FUNCTION: E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)- like complex is shown to mediate ubiquitination of CDKN1B ('Thr- 187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin- mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2. Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma. Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1 and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy. Acts as an autophagy receptor for the degradation of IRF3, hence attenuating type I interferon (IFN)-dependent immune responses (PubMed:26347139). {ECO:0000269|PubMed:16297862, ECO:0000269|PubMed:16316627, ECO:0000269|PubMed:16472766, ECO:0000269|PubMed:16880511, ECO:0000269|PubMed:18022694, ECO:0000269|PubMed:18361920, ECO:0000269|PubMed:18641315, ECO:0000269|PubMed:18845142, ECO:0000269|PubMed:19675099, ECO:0000269|PubMed:26347139}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in fetal and adult heart and fetal lung.; unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;colon;blood;lens;bone marrow;uterus;pancreas;lung;adrenal gland;nasopharynx;bone;thyroid;placenta;liver;testis;head and neck;spleen;kidney;germinal center;brain;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle; 0.36566 0.15312 -0.244249595 36.17008728 27.38419 0.88264 TRIM22 3.15622179426349e-12 0.0215861323369217 0.978413867659922 tripartite motif containing 22 FUNCTION: Interferon-induced antiviral protein involved in cell innate immunity. The antiviral activity could in part be mediated by TRIM22-dependent ubiquitination of viral proteins. Plays a role in restricting the replication of HIV-1, encephalomyocarditis virus (EMCV) and hepatitis B virus (HBV). Acts as a transcriptional repressor of HBV core promoter. May have E3 ubiquitin-protein ligase activity. {ECO:0000269|PubMed:18389079, ECO:0000269|PubMed:18656448, ECO:0000269|PubMed:19218198, ECO:0000269|PubMed:19585648}.; . TISSUE SPECIFICITY: Strongly expressed in peripheral blood leukocytes, spleen, thymus, and ovary. Expressed at basal levels in other tissues. {ECO:0000269|PubMed:7797467}.; . . 0.22454 0.07031 1.778477122 96.83887709 2409.0969 9.11475 TRIM23 0.0669671844650749 0.932910791888065 0.000122023646860497 tripartite motif containing 23 FUNCTION: Acts as an E3 ubiquitin-protein ligase. In the presence of the human cytomegalovirus (HCMV) protein UL144, participates in 'Lys-63'-linked auto-ubiquitination of TRAF6 resulting in the virally controlled activation of NF-kappa-B at early time of infection. The C-terminus can act as an allosteric activator of the cholera toxin catalytic subunit. {ECO:0000269|PubMed:15684077}.; . . ovary;sympathetic chain;developmental;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;mammary gland;stomach; medulla oblongata;superior cervical ganglion;prefrontal cortex; 0.66059 0.12378 -0.624497208 17.16206653 86.98408 1.99201 TRIM24 0.999995048034361 4.95196563358015e-06 5.18666828648421e-15 tripartite motif containing 24 FUNCTION: Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has E3 protein-ubiquitin ligase activity. Promotes ubiquitination and proteasomal degradation of p53/TP53. Plays a role in the regulation of cell proliferation and apoptosis, at least in part via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, including RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes (By similarity). {ECO:0000250, ECO:0000269|PubMed:16322096, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:21164480}.; DISEASE: Note=A chromosomal aberration involving TRIM24/TIF1 is found in papillary thyroid carcinomas (PTCs). Translocation t(7;10)(q32;q11) with RET. The translocation generates the TRIM24/RET (PTC6) oncogene. {ECO:0000269|PubMed:10439047}.; . lymphoreticular;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;blood;skeletal muscle;breast;lung;adrenal gland;placenta;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.90296 0.28521 -0.067881249 48.69072895 79.20768 1.88000 TRIM25 0.135290442283726 0.863809353273055 0.000900204443219471 tripartite motif containing 25 FUNCTION: Functions as a ubiquitin E3 ligase and as an ISG15 E3 ligase. Involved in innate immune defense against viruses by mediating ubiquitination of DDX58. Mediates 'Lys-63'-linked polyubiquitination of the DDX58 N-terminal CARD-like region which is crucial for triggering the cytosolic signal transduction that leads to the production of interferons in response to viral infection. Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway. Mediates estrogen action in various target organs. Mediates the ubiquitination and subsequent proteasomal degradation of ZFHX3 (PubMed:22452784). {ECO:0000269|PubMed:16352599, ECO:0000269|PubMed:17069755, ECO:0000269|PubMed:17392790, ECO:0000269|PubMed:22452784}.; . TISSUE SPECIFICITY: Expressed in breast tumors (at protein level). Ubiquitous. {ECO:0000269|PubMed:15130519, ECO:0000269|PubMed:22452784}.; unclassifiable (Anatomical System);lymph node;colon;blood;skin;skeletal muscle;retina;bone marrow;uterus;breast;prostate;lung;frontal lobe;placenta;visual apparatus;testis;cervix;germinal center; superior cervical ganglion;placenta;ciliary ganglion;atrioventricular node; 0.08763 0.16974 -0.222203495 37.54423213 272.4968 3.53957 TRIM26 0.829653548058971 0.170315291926242 3.11600147864863e-05 tripartite motif containing 26 . . . . . 0.29609 . -0.556537043 19.72753008 414.59871 4.26517 TRIM26BP . . . tripartite motif containing 26B, pseudogene . . . . . . . . . . . TRIM27 0.878751858118275 0.121186249356182 6.1892525542713e-05 tripartite motif containing 27 FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of PIK3C2B and inhibits its activity; mediates the formation of 'Lys-48'-linked polyubiquitin chains; the function inhibits CD4 T- cell activation. Acts as a regulator of retrograde transport: together with MAGEL2, mediates the formation of 'Lys-63'-linked polyubiquitin chains at 'Lys-220' of WASH1, leading to promote endosomal F-actin assembly (PubMed:23452853). Has a transcriptional repressor activity by cooperating with EPC1. Induces apoptosis by activating Jun N-terminal kinase and p38 kinase and also increases caspase-3-like activity independently of mitochondrial events. May function in male germ cell development. Has DNA-binding activity and preferentially bound to double- stranded DNA. {ECO:0000269|PubMed:10976108, ECO:0000269|PubMed:12807881, ECO:0000269|PubMed:22128329, ECO:0000269|PubMed:23452853}.; DISEASE: Note=A chromosomal aberration involving TRIM27/RFP is found in papillary thyroid carcinomas (PTCs). Translocation t(6;10)(p21.3;q11.2) with RET. The translocation generates TRIM27/RET and delta TRIM27/RET oncogenes. {ECO:0000269|PubMed:12787916, ECO:0000269|PubMed:3037315}.; TISSUE SPECIFICITY: Expressed in testis namely within the seminiferous tubules. {ECO:0000269|PubMed:12445133}.; . . 0.39564 . -0.337894035 30.37272942 25.43334 0.83044 TRIM28 0.999902029147243 9.7970815904766e-05 3.68524760767134e-11 tripartite motif containing 28 FUNCTION: Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteosomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg) (PubMed:23543754). {ECO:0000269|PubMed:10347202, ECO:0000269|PubMed:11959841, ECO:0000269|PubMed:15882967, ECO:0000269|PubMed:16107876, ECO:0000269|PubMed:16862143, ECO:0000269|PubMed:17079232, ECO:0000269|PubMed:17178852, ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:17942393, ECO:0000269|PubMed:18060868, ECO:0000269|PubMed:18082607, ECO:0000269|PubMed:20424263, ECO:0000269|PubMed:20858735, ECO:0000269|PubMed:20864041, ECO:0000269|PubMed:21940674, ECO:0000269|PubMed:23543754, ECO:0000269|PubMed:23665872, ECO:0000269|PubMed:8769649, ECO:0000269|PubMed:9016654}.; . TISSUE SPECIFICITY: Expressed in all tissues tested including spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes. {ECO:0000269|PubMed:9016654}.; ovary;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;urinary;blood;lens;breast;bile duct;pancreas;lung;mesenchyma;placenta;hippocampus;macula lutea;visual apparatus;duodenum;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;thyroid;placenta;testis;tumor;thymus;cerebellum; 0.40612 0.45135 -1.107723888 6.829440906 36.80093 1.10339 TRIM29 9.16729542241399e-05 0.934953700680467 0.0649546263653089 tripartite motif containing 29 FUNCTION: It is able to complement the radiosensitivity defect of an ataxia telangiectasia (AT) fibroblast cell line.; . TISSUE SPECIFICITY: Expressed in placenta, prostate and thymus. {ECO:0000269|PubMed:11331580}.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;larynx;thyroid;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;oral cavity;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;hypopharynx;head and neck;cervix;mammary gland;stomach;thymus; superior cervical ganglion;tongue;atrioventricular node;skeletal muscle;skin;subthalamic nucleus;testis - seminiferous tubule;trachea;placenta;liver;globus pallidus;ciliary ganglion;trigeminal ganglion;tonsil; 0.50874 0.11722 -0.064242613 48.844067 476.53225 4.50967 TRIM31 0.0163881344679348 0.959524660607285 0.0240872049247798 tripartite motif containing 31 FUNCTION: Regulator of Src-induced anchorage independent cell growth (By similarity). May have E3 ubiquitin-protein ligase activity. {ECO:0000250, ECO:0000269|PubMed:18773414}.; . TISSUE SPECIFICITY: Up-regulated in gastric adenocarcinomas. {ECO:0000269|PubMed:18773414}.; . . 0.05427 . 2.975031217 99.19792404 1604.739 7.41341 TRIM31-AS1 . . . TRIM31 antisense RNA 1 . . . . . . . . . . . TRIM32 0.0973176435273222 0.86707183064512 0.0356105258275577 tripartite motif containing 32 FUNCTION: Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. May ubiquitinate BBS2. May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo. Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo. {ECO:0000269|PubMed:19349376, ECO:0000269|PubMed:22500027}.; DISEASE: Limb-girdle muscular dystrophy 2H (LGMD2H) [MIM:254110]: An autosomal recessive degenerative myopathy characterized by pelvic girdle, shoulder girdle and quadriceps muscle weakness. Clinical phenotype and severity are highly variable. Disease progression is slow and most patients remain ambulatory into the sixth decade of life. {ECO:0000269|PubMed:11822024, ECO:0000269|PubMed:17994549}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bardet-Biedl syndrome 11 (BBS11) [MIM:615988]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:16606853}. Note=The disease is caused by mutations affecting the gene represented in this entry. It has been suggested that TRIM32 might be the E3 ubiquitin ligase for BBS2, a component of the BBSome complex involved in ciliogenesis, that is ubiquitinated and degraded by the proteasome (PubMed:22500027). {ECO:0000269|PubMed:22500027}.; TISSUE SPECIFICITY: Spleen, thymus, prostate, testis, ovary, intestine, colon and skeletal muscle. {ECO:0000269|PubMed:11822024}.; . . 0.23936 0.11011 -0.600630256 18.06440198 62.20046 1.60862 TRIM33 0.999998355934464 1.64406553457171e-06 1.7473413073396e-15 tripartite motif containing 33 FUNCTION: Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF- beta/BMP signaling cascade). {ECO:0000250, ECO:0000269|PubMed:10022127, ECO:0000269|PubMed:15820681, ECO:0000269|PubMed:16751102, ECO:0000269|PubMed:19135894}.; DISEASE: Note=A chromosomal aberration involving TRIM33 is found in papillary thyroid carcinomas (PTCs). Translocation t(1;10)(p13;q11) with RET. The translocation generates the TRIM33/RET (PTC7) oncogene. {ECO:0000269|PubMed:10439047}.; TISSUE SPECIFICITY: Expressed in stem cells at the bottom of the crypts of the colon (at protein level). Expressed in colon adenomas and adenocarcinomas (at protein level). Expressed in brain, lung, liver, spleen, thymus, prostate, kidney, testis, heart, placenta, pancreas, small intestine, ovary, colon, skeletal muscle and hematopoietic progenitors.; medulla oblongata;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);amygdala;cartilage;epidermis;islets of Langerhans;hypothalamus;skeletal muscle;breast;lung;trabecular meshwork;placenta;visual apparatus;liver;head and neck;cervix;kidney;stomach; dorsal root ganglion;amygdala;superior cervical ganglion;occipital lobe;testis - interstitial;medulla oblongata;pons;atrioventricular node;caudate nucleus;skin;subthalamic nucleus;fetal brain;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;parietal lobe;cingulate cortex; 0.86835 0.15130 -0.644723694 16.52512385 403.36435 4.21155 TRIM34 0.00020889000433714 0.908133800371527 0.0916573096241355 tripartite motif containing 34 FUNCTION: May function as antiviral protein and may contribute to the defense against retroviral infections. {ECO:0000269|PubMed:17156811}.; . TISSUE SPECIFICITY: Isoform 1 is the most abundant form. It is highly expressed in the placenta, spleen, colon and peripheral blood leukocytes. {ECO:0000269|PubMed:11013086}.; colon;skin;skeletal muscle;prostate;pancreas;whole body;lung;endometrium;larynx;placenta;liver;testis;head and neck;spleen;germinal center;kidney;brain;stomach; . . 0.08111 0.841481379 88.35810333 . . TRIM35 0.000940307552509518 0.941956869995866 0.0571028224516247 tripartite motif containing 35 FUNCTION: May play a role as a tumor suppressor. Implicated in the cell death mechanism (By similarity). {ECO:0000250}.; . . medulla oblongata;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;cerebellum; atrioventricular node;trigeminal ganglion; 0.09006 0.11499 -0.418800956 25.79028073 87.09896 1.99306 TRIM36 0.000675729869239821 0.995030264303513 0.00429400582724745 tripartite motif containing 36 FUNCTION: E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Involved in chromosome segregation and cell cycle regulation. May play a role in the acrosome reaction and fertilization (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in testis, prostate and brain. Weakly expressed in kidney, lung and heart. {ECO:0000269|PubMed:15145053}.; unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;colon;lens;skeletal muscle;skin;lung;frontal lobe;placenta;thyroid;bone;testis;brain;aorta; amygdala;dorsal root ganglion;testis - interstitial;superior cervical ganglion;fetal brain;prefrontal cortex; 0.54187 0.11106 0.135991087 63.61759849 225.33457 3.24526 TRIM36-IT1 . . . TRIM36 intronic transcript 1 . . . . . . . . . . . TRIM37 0.172389368264362 0.827610592426731 3.93089074949232e-08 tripartite motif containing 37 FUNCTION: E3 ubiquitin-protein ligase required to prevent centriole reduplication (PubMed:15885686, PubMed:23769972). Probably acts by ubiquitinating positive regulators of centriole reduplication (PubMed:23769972). Mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression: associates with some Polycomb group (PcG) multiprotein PRC2-like complex and mediates repression of target genes (PubMed:25470042). Has anti-HIV activity (PubMed:24317724). {ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:23769972, ECO:0000269|PubMed:24317724, ECO:0000269|PubMed:25470042}.; DISEASE: Mulibrey nanism (MUL) [MIM:253250]: An autosomal recessive growth disorder characterized by severe growth failure of prenatal onset, constrictive pericardium and progressive cardiomyopathy, facial dysmorphism, and failure of sexual maturation. Additional clinical features include hepatomegaly, muscle hypotonia, J-shaped sella turcica, yellowish dots in the ocular fundi, hypoplasia of various endocrine glands, insulin resistance with type 2 diabetes, and an increased risk for Wilms' tumor. {ECO:0000269|PubMed:10888877, ECO:0000269|PubMed:12754710, ECO:0000269|PubMed:15108285, ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:17100991, ECO:0000269|PubMed:17551331, ECO:0000269|PubMed:21865362, ECO:0000269|PubMed:23385855}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous (PubMed:10888877). Highly expressed in testis, while it is weakly expressed in other tissues (PubMed:16310976). {ECO:0000269|PubMed:10888877, ECO:0000269|PubMed:16310976}.; medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;oesophagus;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; amygdala;whole brain;medulla oblongata;occipital lobe;testis - interstitial;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;testis - seminiferous tubule;fetal brain;prefrontal cortex;globus pallidus;testis;parietal lobe;cingulate cortex;cerebellum; 0.33448 0.28904 -0.222203495 37.54423213 161.06988 2.77140 TRIM38 4.75130205096512e-06 0.637516773187976 0.362478475509974 tripartite motif containing 38 FUNCTION: E3 ubiquitin-protein ligase. Mediates 'Lys-48'-linked polyubiquitination and proteasomal degradation of the critical TLR adapter TICAM1, inhibiting TLR3-mediated type I interferon signaling. {ECO:0000269|PubMed:23056470}.; . TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;blood;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;adipose tissue;lymph node;trachea;appendix;white blood cells;atrioventricular node;whole blood;trigeminal ganglion;skeletal muscle; 0.08972 0.09024 0.308721233 72.59966973 428.66293 4.32306 TRIM39 0.999421097975261 0.000578899232041363 2.79269732460289e-09 tripartite motif containing 39 FUNCTION: E3 ubiquitin-protein ligase. May facilitate apoptosis by inhibiting APC/C-Cdh1-mediated poly-ubiquitination and subsequent proteasome-mediated degradation of the pro-apoptotic protein MOAP1. {ECO:0000269|PubMed:19100260, ECO:0000269|PubMed:22529100}.; . TISSUE SPECIFICITY: Ubiquitous; highly expressed in brain, heart, kidney, liver, skeletal muscle, spleen and testis. {ECO:0000269|PubMed:19100260}.; . . 0.42527 . 0.03689118 56.64071715 107.38832 2.25036 TRIM39-RPP21 . . . TRIM39-RPP21 readthrough . . . . . . . . . 4065.79141 12.64383 TRIM40 1.53055068540437e-07 0.12104907061353 0.878950776331401 tripartite motif containing 40 FUNCTION: May function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway. Promotes neddylation of IKBKG/NEMO, stabilizing NFKBIA, and inhibiting of NF-kappaB nuclear translocation and activity. {ECO:0000269|PubMed:21474709}.; . TISSUE SPECIFICITY: Highly expressed in normal gastrointestinal epithelia but that is down-regulated in gastrointestinal carcinomas and chronic inflammatory lesions of the gastrointestinal tract. {ECO:0000269|PubMed:21474709}.; placenta; . 0.15338 . 1.43862044 95.05779665 1046.03919 6.20708 TRIM41 0.965388635580126 0.0346088101644906 2.55425538380059e-06 tripartite motif containing 41 FUNCTION: Functions as an E3 ligase that catalyzes the ubiquitin- mediated degradation of protein kinase C. {ECO:0000269|PubMed:17893151}.; . TISSUE SPECIFICITY: Expressed in multiple tissues with the highest levels in heart and skeletal muscle. {ECO:0000269|PubMed:17893151}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;pituitary gland;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;stomach;peripheral nerve;thymus; superior cervical ganglion;trigeminal ganglion; 0.09305 0.09508 -0.350843407 29.54116537 1445.6989 7.09375 TRIM42 5.57634194724097e-15 0.00713854154670127 0.992861458453293 tripartite motif containing 42 . . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; testis - interstitial;testis;atrioventricular node; 0.14854 0.09722 0.382138899 75.65463553 4067.35531 12.64791 TRIM43 0.484034992740452 0.493899298036454 0.022065709223094 tripartite motif containing 43 . . . unclassifiable (Anatomical System);lung;placenta; . . . . . 22.66163 0.75846 TRIM43B . . . tripartite motif containing 43B . . . . . . . . . . . TRIM43CP . . . tripartite motif containing 43C, pseudogene . . . . . . . . . . . TRIM44 0.163653747251109 0.821541479748533 0.014804773000358 tripartite motif containing 44 FUNCTION: May play a role in the process of differentiation and maturation of neuronal cells (By similarity). May regulate the activity of TRIM17. {ECO:0000250, ECO:0000269|PubMed:19358823}.; . TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:19358823}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; amygdala;whole brain;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;cerebellum peduncles;temporal lobe;atrioventricular node;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.58240 0.14627 -0.293801652 32.93819297 23.99448 0.78977 TRIM45 1.44830918595153e-06 0.621075330765983 0.378923220924831 tripartite motif containing 45 FUNCTION: May act as a transcriptional repressor in mitogen- activated protein kinase signaling pathway. {ECO:0000269|PubMed:15351693}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, brain, heart and pancreas. {ECO:0000269|PubMed:15351693}.; unclassifiable (Anatomical System);heart;ovary;hypothalamus;uterus;pancreas;endometrium;placenta;pituitary gland;testis;head and neck;cervix;kidney;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21036 0.09437 1.488170966 95.3467799 3722.97274 11.92335 TRIM46 0.998652125444883 0.00134787012256152 4.43255509344128e-09 tripartite motif containing 46 . . . unclassifiable (Anatomical System);lung;frontal lobe;brain; superior cervical ganglion;temporal lobe;caudate nucleus;trigeminal ganglion; 0.59864 0.14106 -0.843147538 11.2762444 131.25378 2.49537 TRIM47 0.321925207559748 0.67460695664768 0.0034678357925727 tripartite motif containing 47 . . TISSUE SPECIFICITY: Low expression in most tissues. Higher expression in kidney tubular cells. Overexpressed in astrocytoma tumor cells. {ECO:0000269|PubMed:11511098}.; ovary;salivary gland;colon;parathyroid;choroid;skin;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;urinary;lens;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;atrioventricular node; 0.14655 0.15540 . . 1938.75971 8.10169 TRIM48 1.77341661947835e-14 0.000532837483424712 0.999467162516558 tripartite motif containing 48 . . . . . 0.05186 . 1.840996754 97.08657702 499.24357 4.58752 TRIM49 0.64552339591359 0.348245780337976 0.006230823748434 tripartite motif containing 49 . . TISSUE SPECIFICITY: Preferentially expressed in testis.; . . . 0.07409 . . 541.3314 4.73825 TRIM49B 7.55661253581996e-05 0.751263803587438 0.248660630287204 tripartite motif containing 49B . . . . . . . . . 69.32987 1.72663 TRIM49C 0.161108014215193 0.774144344880045 0.064747640904761 tripartite motif containing 49C . . . . . . . . . 62.75418 1.62118 TRIM49D1 . . . tripartite motif containing 49D1 . . . . . . . . . 10.25297 0.37381 TRIM49D2 . . . tripartite motif containing 49D2 . . . . . . . . . . . TRIM50 2.72561665019464e-06 0.516929130644208 0.483068143739142 tripartite motif containing 50 FUNCTION: E3 ubiquitin-protein ligase. {ECO:0000269|PubMed:18398435}.; . . unclassifiable (Anatomical System);prostate;pancreas;lung;whole body;ovary;synovium;placenta;testis;parathyroid;kidney;brain;skin; superior cervical ganglion;subthalamic nucleus;pons;parietal lobe; 0.13123 . -0.44448505 24.46331682 87.89688 2.00432 TRIM51 1.04917684230659e-05 0.56744200359985 0.432547504631727 tripartite motif-containing 51 . . . . . 0.04530 0.07584 . . 692.62061 5.24912 TRIM51BP . . . tripartite motif-containing 51B, pseudogene . . . . . . . . . . . TRIM51CP . . . tripartite motif-containing 51C, pseudogene . . . . . . . . . . . TRIM51DP . . . tripartite motif-containing 51D, pseudogene . . . . . . . . . . . TRIM51EP . . . tripartite motif-containing 51E, pseudogene . . . . . . . . . . . TRIM51FP . . . tripartite motif-containing 51F, pseudogene . . . . . . . . . . . TRIM51GP . . . tripartite motif-containing 51G, pseudogene . . . . . . . . . . . TRIM51HP . . . tripartite motif-containing 51H, pseudogene . . . . . . . . . . . TRIM51JP . . . tripartite motif-containing 51J, pseudogene . . . . . . . . . . . TRIM52 8.08204670688077e-06 0.511466841686793 0.4885250762665 tripartite motif containing 52 . . . unclassifiable (Anatomical System);cartilage;ovary;blood;skin;skeletal muscle;retina;bone marrow;uterus;lung;endometrium;nasopharynx;bone;thyroid;placenta;liver;testis;cervix;germinal center;kidney;brain;stomach;gall bladder; . 0.07437 . -0.494039303 22.09247464 5147.7302 14.74421 TRIM52-AS1 . . . TRIM52 antisense RNA 1 (head to head) . . . . . . . . . . . TRIM53AP . . . tripartite motif containing 53A, pseudogene . . . . . . . . . . . TRIM53BP . . . tripartite motif containing 53B, pseudogene . . . . . . . . . . . TRIM53CP . . . tripartite motif containing 53C, pseudogene . . . . . . . . . . . TRIM54 8.24707898322991e-07 0.297899937163666 0.702099238128436 tripartite motif containing 54 FUNCTION: May bind and stabilize microtubules during myotubes formation. {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in heart and skeletal muscle. {ECO:0000269|PubMed:11243782}.; unclassifiable (Anatomical System);ovary;muscle;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;whole body;lung;larynx;adrenal gland;thyroid;bone;macula lutea;testis;germinal center;kidney; . 0.13331 0.13638 -0.756778259 13.44656759 59.43838 1.56351 TRIM55 0.000207996390208794 0.977468439362301 0.0223235642474906 tripartite motif containing 55 FUNCTION: May regulate gene expression and protein turnover in muscle cells. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in muscle. Low-level expression in liver. {ECO:0000269|PubMed:11243782}.; unclassifiable (Anatomical System);heart;ovary;muscle;parathyroid;whole body;lung;larynx;placenta;liver;testis;head and neck;spleen;kidney;mammary gland; . 0.44272 0.08797 -0.176292081 40.56381222 81.45172 1.91092 TRIM56 0.0801579223006073 0.909157185452947 0.0106848922464457 tripartite motif containing 56 FUNCTION: E3 ubiquitin-protein ligase that mediates 'Lys-63'- linked polyubiquitination of TMEM173/STING, thereby playing a key role in innate immunity. TMEM173/STING 'Lys-63'-linked ubiquitination activates the production of type I interferon IFN- beta following detection of pathogen- and host-derived double- stranded DNA (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymphoreticular;lymph node;ovary;islets of Langerhans;colon;blood;skin;retina;bone marrow;uterus;prostate;pancreas;lung;oesophagus;nasopharynx;bone;placenta;liver;cervix;spleen;germinal center;mammary gland; . 0.19547 0.10692 -1.041578376 7.773059684 211.88733 3.13921 TRIM58 2.07666883202414e-07 0.260156184446245 0.739843607886872 tripartite motif containing 58 FUNCTION: E3 ubiquitin ligase induced during late erythropoiesis. Directly binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. May participate in the erythroblast enucleation process through regulation of nuclear polarization. {ECO:0000269|PubMed:25241935}.; . TISSUE SPECIFICITY: Expressed in erythroblasts. {ECO:0000269|PubMed:25241935}.; . . 0.11710 0.09971 0.575097644 82.1656051 1342.71737 6.87855 TRIM59 0.0321109566837029 0.926300224709544 0.0415888186067532 tripartite motif containing 59 FUNCTION: May serve as a multifunctional regulator for innate immune signaling pathways. {ECO:0000250|UniProtKB:Q922Y2}.; . TISSUE SPECIFICITY: Isoform IFT80-L is widely expressed. {ECO:0000269|PubMed:18601909}.; unclassifiable (Anatomical System);uterus;medulla oblongata;prostate;lymph node;lung;heart;testis;germinal center;skin;stomach; . 0.12540 0.08697 0.130533008 63.35810333 124.96041 2.43038 TRIM60 2.87342302842874e-07 0.306741039013658 0.693258673644039 tripartite motif containing 60 . . . unclassifiable (Anatomical System);liver;spleen; superior cervical ganglion;globus pallidus;ciliary ganglion; 0.09624 . 1.396334339 94.70393961 72.20607 1.77047 TRIM60P1Y . . . tripartite motif containing 60 pseudogene 1, Y-linked . . . . . . . . . . . TRIM60P2Y . . . tripartite motif containing 60 pseudogene 2, Y-linked . . . . . . . . . . . TRIM60P3Y . . . tripartite motif containing 60 pseudogene 3, Y-linked . . . . . . . . . . . TRIM60P4Y . . . tripartite motif containing 60 pseudogene 4, Y-linked . . . . . . . . . . . TRIM60P5Y . . . tripartite motif containing 60 pseudogene 5, Y-linked . . . . . . . . . . . TRIM60P6Y . . . tripartite motif containing 60 pseudogene 6, Y-linked . . . . . . . . . . . TRIM60P7Y . . . tripartite motif containing 60 pseudogene 7, Y-linked . . . . . . . . . . . TRIM60P8Y . . . tripartite motif containing 60 pseudogene 8, Y-linked . . . . . . . . . . . TRIM60P9Y . . . tripartite motif containing 60 pseudogene 9, Y-linked . . . . . . . . . . . TRIM60P10Y . . . tripartite motif containing 60 pseudogene 10, Y-linked . . . . . . . . . . . TRIM60P11Y . . . tripartite motif containing 60 pseudogene 11, Y-linked . . . . . . . . . . . TRIM60P12Y . . . tripartite motif containing 60 pseudogene 12, Y-linked . . . . . . . . . . . TRIM60P13 . . . tripartite motif containing 60 pseudogene 13 . . . . . . . . . . . TRIM60P14 . . . tripartite motif containing 60 pseudogene 14 . . . . . . . . . . . TRIM60P15 . . . tripartite motif containing 60 pseudogene 15 . . . . . . . . . . . TRIM60P16 . . . tripartite motif containing 60 pseudogene 16 . . . . . . . . . . . TRIM60P17 . . . tripartite motif containing 60 pseudogene 17 . . . . . . . . . . . TRIM60P18 . . . tripartite motif containing 60 pseudogene 18 . . . . . . . . . . . TRIM60P19 . . . tripartite motif containing 60 pseudogene 19 . . . . . . . . . . . TRIM61 0.672137878695462 0.306561470837179 0.0213006504673585 tripartite motif containing 61 . . . unclassifiable (Anatomical System);lung;islets of Langerhans;epididymis;bone;liver;testis;kidney;germinal center; . 0.13667 0.09271 . . 146.52275 2.63689 TRIM62 0.00161141831959926 0.886165554194207 0.112223027486194 tripartite motif containing 62 FUNCTION: E3 ubiquitin ligase whose activity is dependent on E2 ubiquitin-conjugating enzyme UBE2D2. {ECO:0000269|PubMed:23402750}.; . . ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;adrenal cortex;lens;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen; superior cervical ganglion;cerebellum peduncles;placenta;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex;cerebellum; 0.22732 0.11160 -0.312207497 32.05944798 271.54044 3.53055 TRIM63 4.71828632864004e-12 0.0142417178458909 0.985758282149391 tripartite motif containing 63 FUNCTION: E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti- hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells. {ECO:0000269|PubMed:11927605, ECO:0000269|PubMed:18222470}.; . TISSUE SPECIFICITY: Muscle specific. Selectively expressed in heart and skeletal muscle. Also expressed in the iris. {ECO:0000269|PubMed:11243782, ECO:0000269|PubMed:11283016, ECO:0000269|PubMed:11679633, ECO:0000269|PubMed:12107412}.; . . 0.13419 0.38803 -0.400392389 26.85185185 1583.89784 7.36109 TRIM64 . . . tripartite motif containing 64 . . . uterus; . . . . . . . TRIM64B . . . tripartite motif containing 64B . . . uterus; . . . . . 276.81578 3.56170 TRIM64C 0.012116567412189 0.412858396297838 0.575025036289973 tripartite motif containing 64C . . . . . . . . . 2621.41494 9.59695 TRIM64DP . . . tripartite motif containing 64D, pseudogene . . . . . . . . . . . TRIM64EP . . . tripartite motif containing 64E, pseudogene . . . . . . . . . . . TRIM64FP . . . tripartite motif containing 64F, pseudogene . . . . . . . . . . . TRIM65 2.48168761970087e-09 0.0410253546827186 0.958974642835594 tripartite motif containing 65 . . . unclassifiable (Anatomical System);lymph node;heart;tongue;colon;blood;skin;breast;uterus;prostate;atrium;lung;bone;visual apparatus;hippocampus;duodenum;liver;testis;head and neck;kidney;brain;mammary gland;bladder;tonsil;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons; 0.12739 . 0.778977686 87.21396556 1901.4146 8.01929 TRIM66 . . . tripartite motif containing 66 FUNCTION: May function as transcription repressor; The repressive effects are mediated, at least in part, by recruitment of deacetylase activity. May play a role as negative regulator of postmeiotic genes acting through CBX3 complex formation and centromere association (By similarity). {ECO:0000250}.; . . ovary;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;optic nerve;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;pancreas;lung;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.28042 0.08461 . . 4840.73606 14.11655 TRIM67 0.672039658016629 0.327752627556482 0.000207714426888775 tripartite motif containing 67 . . . . . 0.21940 0.14333 . . 115.83851 2.34115 TRIM68 2.15428833165883e-11 0.0657111159392421 0.934288884039215 tripartite motif containing 68 FUNCTION: Functions as a ubiquitin E3 ligase. Acts as a coactivator of androgen receptor (AR) depending on its ubiquitin ligase activity. {ECO:0000269|PubMed:18451177}.; . TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in prostate cancer cell lines. Up-regulation could be restricted to androgen-dependent cells. {ECO:0000269|PubMed:11560955, ECO:0000269|PubMed:11597395, ECO:0000269|PubMed:18451177}.; unclassifiable (Anatomical System);heart;ovary;pineal body;colon;parathyroid;choroid;skin;uterus;prostate;placenta;liver;spleen;kidney;brain;mammary gland;stomach; medulla oblongata;testis - interstitial;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.14901 . -1.109541557 6.782259967 54.34931 1.47311 TRIM69 1.96411504084879e-10 0.0342545717112036 0.965745428092385 tripartite motif containing 69 FUNCTION: May have E3 ubiquitin-protein ligase activity. May play a role in apoptosis. {ECO:0000269|PubMed:23131556}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;frontal lobe;testis;brain; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.09719 0.09576 0.97558591 90.37508846 1348.14822 6.89047 TRIM71 0.993173544222524 0.00682622339415629 2.32383319432115e-07 tripartite motif containing 71, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance. Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A. Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression. Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development: positively regulates FGF signaling by controlling the stability of SHCBP1 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in testis. {ECO:0000269|PubMed:15722555}.; . . 0.37913 0.12730 -1.133409319 6.434300543 48.04347 1.34775 TRIM72 0.000530648274852266 0.694276942479739 0.305192409245409 tripartite motif containing 72, E3 ubiquitin protein ligase FUNCTION: Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity). {ECO:0000250}.; . . ovary;placenta;parathyroid; subthalamic nucleus;ciliary ganglion;kidney;atrioventricular node;skeletal muscle; 0.27501 0.11602 . . 95.64021 2.11239 TRIM73 . . . tripartite motif containing 73 . . . unclassifiable (Anatomical System);lung;synovium;testis;brain;skin;stomach; . 0.21662 . . . 56.33825 1.50754 TRIM74 0.780333820359187 0.212615798593584 0.00705038104722853 tripartite motif containing 74 . . . unclassifiable (Anatomical System);lung;synovium;testis;brain;skin;stomach; . 0.08700 . . . 36.62935 1.09967 TRIM75P . . . tripartite motif containing 75, pseudogene . . . . . 0.04232 . . . . . TRIM77 . . . tripartite motif containing 77 . . . . . . . . . 302.38942 3.70315 TRIM77BP . . . tripartite motif containing 77B, pseudogene . . . . . . . . . . . TRIM78P . . . tripartite motif containing 78, pseudogene . . . . . . . . . . . TRIM80P . . . tripartite motif containing 80, pseudogene . . . . . . . . . . . TRIML1 9.1739223202005e-11 0.0219829846177382 0.978017015290522 tripartite motif family like 1 FUNCTION: Probable E3 ubiquitin-protein ligase which plays an important role in blastocyst development. {ECO:0000250}.; . . unclassifiable (Anatomical System);adrenal medulla;testis; . 0.20701 0.10345 0.332586472 73.61405992 2068.55362 8.38159 TRIML2 8.26179056182447e-10 0.0413333647480469 0.958666634425774 tripartite motif family like 2 . . . unclassifiable (Anatomical System);uterus; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.04792 . 1.842813887 97.09247464 163.0223 2.78698 TRIO 0.999999999999911 8.88381480352733e-14 2.38219649739501e-37 trio Rho guanine nucleotide exchange factor FUNCTION: Promotes the exchange of GDP by GTP. Together with leukocyte antigen-related (LAR) protein, it could play a role in coordinating cell-matrix and cytoskeletal rearrangements necessary for cell migration and cell growth.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, brain, pancreas, placenta, liver, kidney and lung.; myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;bladder;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;synovium;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;placenta;hippocampus;amnion;head and neck;kidney;stomach;cerebellum;thymus; amygdala;medulla oblongata;superior cervical ganglion;uterus corpus;fetal brain;prefrontal cortex;globus pallidus;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.75634 . -4.037140278 0.176928521 492.54729 4.56395 TRIOBP 8.94617457135198e-13 0.999999977919524 2.20795811255127e-08 TRIO and F-actin binding protein FUNCTION: May regulate actin cytoskeletal organization, cell spreading and cell contraction by directly binding and stabilizing filamentous F-actin. The localized formation of TARA and TRIO complexes coordinates the amount of F-actin present in stress fibers. May also serve as a linker protein to recruit proteins required for F-actin formation and turnover. {ECO:0000269|PubMed:18194665}.; DISEASE: Deafness, autosomal recessive, 28 (DFNB28) [MIM:609823]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:16385457, ECO:0000269|PubMed:16385458}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart and placenta. Isoform 3 is expressed in fetal brain, retina and cochlea but is not detectable in the other tissues. {ECO:0000269|PubMed:16385458}.; myocardium;ovary;salivary gland;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;synovium;bone;thyroid;pituitary gland;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;amnion;head and neck;spleen;kidney;mammary gland;stomach;aorta; . 0.25275 . 2.970052675 99.18023119 11232.59701 23.04553 TRIP4 3.04197168353347e-07 0.981785682274454 0.018214013528378 thyroid hormone receptor interactor 4 FUNCTION: Transcription coactivator which associates with nuclear receptors, transcriptional coactivators including EP300, CREBBP and NCOA1, and basal transcription factors like TBP and TFIIA to facilitate nuclear receptors-mediated transcription. May thereby play an important role in establishing distinct coactivator complexes under different cellular conditions. Plays a role in thyroid hormone receptor and estrogen receptor transactivation (PubMed:10454579, PubMed:25219498). Also involved in androgen receptor transactivation (By similarity). Plays a pivotal role in the transactivation of NF-kappa-B, SRF and AP1. Acts as a mediator of transrepression between nuclear receptor and either AP1 or NF- kappa-B (PubMed:12077347). {ECO:0000250|UniProtKB:Q9QXN3, ECO:0000269|PubMed:10454579, ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:25219498}.; . . ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;alveolus;liver;amnion;spleen;head and neck;kidney;stomach; superior cervical ganglion;testis - interstitial;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.44720 0.10123 -1.019530098 8.038452465 74.70225 1.80802 TRIP6 0.659398351134913 0.340367624743684 0.000234024121403702 thyroid hormone receptor interactor 6 FUNCTION: Relays signals from the cell surface to the nucleus to weaken adherens junction and promote actin cytoskeleton reorganization and cell invasiveness. Involved in lysophosphatidic acid-induced cell adhesion and migration. Acts as a transcriptional coactivator for NF-kappa-B and JUN, and mediates the transrepression of these transcription factors induced by glucocorticoid receptor. {ECO:0000269|PubMed:14688263, ECO:0000269|PubMed:15489293, ECO:0000269|PubMed:16624523, ECO:0000269|PubMed:19017743}.; . TISSUE SPECIFICITY: Abundantly expressed in kidney, liver and lung. Lower levels in heart, placenta and pancreas. Expressed in colonic epithelial cells. Up-regulated in colonic tumors. {ECO:0000269|PubMed:19017743}.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;endometrium;bone;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);trophoblast;cartilage;heart;tongue;adrenal cortex;pharynx;blood;lens;bile duct;pancreas;lung;cornea;epididymis;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion; 0.41848 0.14857 0.20030965 67.3566879 2216.10323 8.66933 TRIP10 0.354472308235879 0.645505220532389 2.24712317314154e-05 thyroid hormone receptor interactor 10 FUNCTION: Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N- WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL. {ECO:0000250, ECO:0000269|PubMed:11069762, ECO:0000269|PubMed:16318909, ECO:0000269|PubMed:16326391}.; . TISSUE SPECIFICITY: Expressed in brain, colon, heart, kidney, liver, lung, megakaryocyte, ovary, pancreas, peripheral blood lymphocytes, placenta, prostate, skeletal muscle, small intestine, spleen, testis, thymus and trachea. {ECO:0000269|PubMed:11294612, ECO:0000269|PubMed:12054674, ECO:0000269|PubMed:12456510, ECO:0000269|PubMed:12604778, ECO:0000269|PubMed:9210375}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cerebral cortex;endometrium;larynx;bone;thyroid;iris;testis;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.37970 0.19031 -0.863377021 10.84571833 200.76668 3.06392 TRIP11 2.34458214955102e-09 0.999999518042607 4.79612810646599e-07 thyroid hormone receptor interactor 11 FUNCTION: Binds the ligand binding domain of the thyroid receptor (THRB) in the presence of triiodothyronine and enhances THRB- modulated transcription. Golgi auto-antigen; probably involved in maintaining cis-Golgi structure. {ECO:0000269|PubMed:10189370, ECO:0000269|PubMed:9256431}.; DISEASE: Note=A chromosomal aberration involving TRIP11 may be a cause of acute myelogenous leukemia. Translocation t(5;14)(q33;q32) with PDGFRB. The fusion protein may be involved in clonal evolution of leukemia and eosinophilia. {ECO:0000269|PubMed:9373237}.; DISEASE: Achondrogenesis 1A (ACG1A) [MIM:200600]: A form of achondrogenesis type 1, a lethal form of chondrodysplasia characterized by deficient ossification in the lumbar vertebrae and absent ossification in the sacral, pubic and ischial bones and clinically by stillbirth or early death. In addition to severe micromelia, there is a disproportionately large cranium due to marked edema of soft tissues. {ECO:0000269|PubMed:20089971}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in pancreas, muscle, heart, testis, peripheral blood leukocytes, and in several leukemia cell lines. Detected at intermediate levels in placenta and kidney, and at low levels in brain and lung. {ECO:0000269|PubMed:10189370, ECO:0000269|PubMed:9373237}.; ovary;colon;skin;uterus;whole body;frontal lobe;endometrium;thyroid;testis;dura mater;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;pia mater;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.19447 0.10877 0.310359953 72.60556735 4547.20664 13.53807 TRIP12 0.999999999999483 5.17073705873884e-13 2.53351926780523e-31 thyroid hormone receptor interactor 12 FUNCTION: E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardeless of the presence of lysine residues in target proteins. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes. {ECO:0000269|PubMed:18627766, ECO:0000269|PubMed:19028681, ECO:0000269|PubMed:20208519, ECO:0000269|PubMed:20829358, ECO:0000269|PubMed:22884692}.; . . smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;white blood cells;ciliary ganglion;atrioventricular node;whole blood;skeletal muscle; 0.88664 0.10353 -2.456612937 0.996697334 57.50243 1.52990 TRIP13 0.968635140819723 0.0313628593739271 1.99980634943088e-06 thyroid hormone receptor interactor 13 FUNCTION: Plays a key role in chromosome recombination and chromosome structure development during meiosis. Required at early steps in meiotic recombination that leads to non-crossovers pathways. Also needed for efficient completion of homologous synapsis by influencing crossover distribution along the chromosomes affecting both crossovers and non-crossovers pathways. Also required for development of higher-order chromosome structures and is needed for synaptonemal-complex formation. In males, required for efficient synapsis of the sex chromosomes and for sex body formation. Promotes early steps of the DNA double- strand breaks (DSBs) repair process upstream of the assembly of RAD51 complexes. Required for depletion of HORMAD1 and HORMAD2 from synapsed chromosomes (By similarity). {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;frontal lobe;endometrium;gum;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;bile duct;breast;lung;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.41765 0.12329 -0.22584292 37.32012267 24.25769 0.79803 TRIQK . . . triple QxxK/R motif containing FUNCTION: May play a role in cell growth and maintenance of cell morphology. {ECO:0000250}.; . . . . . . 0.167351552 65.04482189 . . TRIT1 9.42968680674274e-10 0.28367453303875 0.716325466018282 tRNA isopentenyltransferase 1 FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 of both cytosolic and mitochondrial tRNAs, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). {ECO:0000269|PubMed:11111046}.; . . lymphoreticular;ovary;colon;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;skeletal muscle;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;appendix;testis;atrioventricular node; 0.23650 0.14415 -0.003562597 53.72729417 1128.84131 6.41211 TRK-CTT1-1 . . . transfer RNA-Lys (CTT) 1-1 . . . . . . . . . . . TRK-CTT1-2 . . . transfer RNA-Lys (CTT) 1-2 . . . . . . . . . . . TRK-CTT2-1 . . . transfer RNA-Lys (CTT) 2-1 . . . . . . . . . . . TRK-CTT2-2 . . . transfer RNA-Lys (CTT) 2-2 . . . . . . . . . . . TRK-CTT2-3 . . . transfer RNA-Lys (CTT) 2-3 . . . . . . . . . . . TRK-CTT2-4 . . . transfer RNA-Lys (CTT) 2-4 . . . . . . . . . . . TRK-CTT2-5 . . . transfer RNA-Lys (CTT) 2-5 . . . . . . . . . . . TRK-CTT3-1 . . . transfer RNA-Lys (CTT) 3-1 . . . . . . . . . . . TRK-CTT4-1 . . . transfer RNA-Lys (CTT) 4-1 . . . . . . . . . . . TRK-CTT5-1 . . . transfer RNA-Lys (CTT) 5-1 . . . . . . . . . . . TRK-CTT6-1 . . . transfer RNA-Lys (CTT) 6-1 . . . . . . . . . . . TRK-CTT7-1 . . . transfer RNA-Lys (CTT) 7-1 . . . . . . . . . . . TRK-CTT8-1 . . . transfer RNA-Lys (CTT) 8-1 . . . . . . . . . . . TRK-CTT9-1 . . . transfer RNA-Lys (CTT) 9-1 . . . . . . . . . . . TRK-CTT10-1 . . . transfer RNA-Lys (CTT) 10-1 . . . . . . . . . . . TRK-CTT11-1 . . . transfer RNA-Lys (CTT) 11-1 . . . . . . . . . . . TRK-CTT12-1 . . . transfer RNA-Lys (CTT) 12-1 . . . . . . . . . . . TRK-CTT13-1 . . . transfer RNA-Lys (CTT) 13-1 . . . . . . . . . . . TRK-CTT14-1 . . . transfer RNA-Lys (CTT) 14-1 . . . . . . . . . . . TRK-CTT15-1 . . . transfer RNA-Lys (CTT) 15-1 . . . . . . . . . . . TRK-CTT16-1 . . . transfer RNA-Lys (CTT) 16-1 . . . . . . . . . . . TRK-TTT1-1 . . . transfer RNA-Lys (TTT) 1-1 . . . . . . . . . . . TRK-TTT2-1 . . . transfer RNA-Lys (TTT) 2-1 . . . . . . . . . . . TRK-TTT3-1 . . . transfer RNA-Lys (TTT) 3-1 . . . . . . . . . . . TRK-TTT3-2 . . . transfer RNA-Lys (TTT) 3-2 . . . . . . . . . . . TRK-TTT3-3 . . . transfer RNA-Lys (TTT) 3-3 . . . . . . . . . . . TRK-TTT3-4 . . . transfer RNA-Lys (TTT) 3-4 . . . . . . . . . . . TRK-TTT3-5 . . . transfer RNA-Lys (TTT) 3-5 . . . . . . . . . . . TRK-TTT4-1 . . . transfer RNA-Lys (TTT) 4-1 . . . . . . . . . . . TRK-TTT5-1 . . . transfer RNA-Lys (TTT) 5-1 . . . . . . . . . . . TRK-TTT6-1 . . . transfer RNA-Lys (TTT) 6-1 . . . . . . . . . . . TRK-TTT7-1 . . . transfer RNA-Lys (TTT) 7-1 . . . . . . . . . . . TRK-TTT8-1 . . . transfer RNA-Lys (TTT) 8-1 . . . . . . . . . . . TRK-TTT9-1 . . . transfer RNA-Lys (TTT) 9-1 . . . . . . . . . . . TRK-TTT10-1 . . . transfer RNA-Lys (TTT) 10-1 . . . . . . . . . . . TRK-TTT11-1 . . . transfer RNA-Lys (TTT) 11-1 . . . . . . . . . . . TRK-TTT12-1 . . . transfer RNA-Lys (TTT) 12-1 . . . . . . . . . . . TRK-TTT13-1 . . . transfer RNA-Lys (TTT) 13-1 . . . . . . . . . . . TRK-TTT14-1 . . . transfer RNA-Lys (TTT) 14-1 . . . . . . . . . . . TRK-TTT15-1 . . . transfer RNA-Lys (TTT) 15-1 . . . . . . . . . . . TRK-TTT16-1 . . . transfer RNA-Lys (TTT) 16-1 . . . . . . . . . . . TRK-TTT17-1 . . . transfer RNA-Lys (TTT) 17-1 . . . . . . . . . . . TRL-AAG1-1 . . . transfer RNA-Leu (AAG) 1-1 . . . . . . . . . . . TRL-AAG1-2 . . . transfer RNA-Leu (AAG) 1-2 . . . . . . . . . . . TRL-AAG1-3 . . . transfer RNA-Leu (AAG) 1-3 . . . . . . . . . . . TRL-AAG2-1 . . . transfer RNA-Leu (AAG) 2-1 . . . . . . . . . . . TRL-AAG2-2 . . . transfer RNA-Leu (AAG) 2-2 . . . . . . . . . . . TRL-AAG2-3 . . . transfer RNA-Leu (AAG) 2-3 FUNCTION: DNA-binding factor that regulates the expression of a subset of genes and plays a key role in tangential, radial, and lateral expansion of the brain neocortex. Regulates neural stem cells proliferation and the production of intermediate neural progenitors and basal radial glial cells affecting the process of cerebral cortex gyrification. May control the proliferation rate of cells by regulating their progression through key cell-cycle transition points (By similarity). {ECO:0000250}.; . . . . . . . . . . TRL-AAG2-4 . . . transfer RNA-Leu (AAG) 2-4 . . . . . . . . . . . TRL-AAG3-1 . . . transfer RNA-Leu (AAG) 3-1 . . . . . . . . . . . TRL-AAG4-1 . . . transfer RNA-Leu (AAG) 4-1 . . . . . . . . . . . TRL-AAG5-1 . . . transfer RNA-Leu (AAG) 5-1 . . . . . . . . . . . TRL-AAG6-1 . . . transfer RNA-Leu (AAG) 6-1 . . . . . . . . . . . TRL-AAG7-1 . . . transfer RNA-Leu (AAG) 7-1 . . . . . . . . . . . TRL-AAG8-1 . . . transfer RNA-Leu (AAG) 8-1 . . . . . . . . . . . TRL-CAA1-1 . . . transfer RNA-Leu (CAA) 1-1 . . . . . . . . . . . TRL-CAA1-2 . . . transfer RNA-Leu (CAA) 1-2 . . . . . . . . . . . TRL-CAA2-1 . . . transfer RNA-Leu (CAA) 2-1 . . . . . . . . . . . TRL-CAA3-1 . . . transfer RNA-Leu (CAA) 3-1 . . . . . . . . . . . TRL-CAA4-1 . . . transfer RNA-Leu (CAA) 4-1 . . . . . . . . . . . TRL-CAA5-1 . . . transfer RNA-Leu (CAA) 5-1 . . . . . . . . . . . TRL-CAA6-1 . . . transfer RNA-Leu (CAA) 6-1 . . . . . . . . . . . TRL-CAA7-1 . . . transfer RNA-Leu (CAA) 7-1 . . . . . . . . . . . TRL-CAG1-1 . . . transfer RNA-Leu (CAG) 1-1 . . . . . . . . . . . TRL-CAG1-2 . . . transfer RNA-Leu (CAG) 1-2 . . . . . . . . . . . TRL-CAG1-3 . . . transfer RNA-Leu (CAG) 1-3 . . . . . . . . . . . TRL-CAG1-4 . . . transfer RNA-Leu (CAG) 1-4 . . . . . . . . . . . TRL-CAG1-5 . . . transfer RNA-Leu (CAG) 1-5 . . . . . . . . . . . TRL-CAG1-6 . . . transfer RNA-Leu (CAG) 1-6 . . . . . . . . . . . TRL-CAG1-7 . . . transfer RNA-Leu (CAG) 1-7 . . . . . . . . . . . TRL-CAG2-1 . . . transfer RNA-Leu (CAG) 2-1 . . . . . . . . . . . TRL-CAG2-2 . . . transfer RNA-Leu (CAG) 2-2 . . . . . . . . . . . TRL-CAG3-1 . . . transfer RNA-Leu (CAG) 3-1 . . . . . . . . . . . TRL-TAA1-1 . . . transfer RNA-Leu (TAA) 1-1 . . . . . . . . . . . TRL-TAA2-1 . . . transfer RNA-Leu (TAA) 2-1 . . . . . . . . . . . TRL-TAA3-1 . . . transfer RNA-Leu (TAA) 3-1 . . . . . . . . . . . TRL-TAA4-1 . . . transfer RNA-Leu (TAA) 4-1 . . . . . . . . . . . TRL-TAA5-1 . . . transfer RNA-Leu (TAA) 5-1 . . . . . . . . . . . TRL-TAG1-1 . . . transfer RNA-Leu (TAG) 1-1 . . . . . . . . . . . TRL-TAG2-1 . . . transfer RNA-Leu (TAG) 2-1 . . . . . . . . . . . TRL-TAG3-1 . . . transfer RNA-Leu (TAG) 3-1 . . . . . . . . . . . TRL-TAG4-1 . . . transfer RNA-Leu (TAG) 4-1 . . . . . . . . . . . TRM-CAT1-1 . . . transfer RNA-Met (CAT) 1-1 . . . . . . . . . . . TRM-CAT2-1 . . . transfer RNA-Met (CAT) 2-1 . . . . . . . . . . . TRM-CAT3-1 . . . transfer RNA-Met (CAT) 3-1 . . . . . . . . . . . TRM-CAT3-2 . . . transfer RNA-Met (CAT) 3-2 . . . . . . . . . . . TRM-CAT4-1 . . . transfer RNA-Met (CAT) 4-1 . . . . . . . . . . . TRM-CAT4-2 . . . transfer RNA-Met (CAT) 4-2 . . . . . . . . . . . TRM-CAT4-3 . . . transfer RNA-Met (CAT) 4-3 . . . . . . . . . . . TRM-CAT5-1 . . . transfer RNA-Met (CAT) 5-1 . . . . . . . . . . . TRM-CAT6-1 . . . transfer RNA-Met (CAT) 6-1 . . . . . . . . . . . TRM-CAT7-1 . . . transfer RNA-Met (CAT) 7-1 . . . . . . . . . . . TRMEP1 . . . tRNA methionine elongator pseudogene 1 . . . . . . . . . . . TRMO . . . tRNA methyltransferase O FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Ser)(GCU) (PubMed:25063302). The methyl group of m(6)t(6)A37 may improve the efficiency of the tRNA decoding ability. May bind to tRNA (By similarity). {ECO:0000250|UniProtKB:P28634, ECO:0000269|PubMed:25063302}.; . . . . 0.10094 0.10377 -0.179930907 40.35739561 . . TRMT1 8.74407139367611e-06 0.996280296083111 0.00371095984549529 tRNA methyltransferase 1 FUNCTION: Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.; . . lymphoreticular;medulla oblongata;ovary;colon;choroid;skin;bone marrow;uterus;prostate;frontal lobe;synovium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;muscle;lens;pancreas;lung;placenta;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach; testis - seminiferous tubule;prefrontal cortex;white blood cells;pons; 0.20360 0.12261 -0.795417163 12.5324369 74.66751 1.80735 TRMT1L 0.939618900830471 0.0603806773895565 4.21779972294675e-07 tRNA methyltransferase 1 like FUNCTION: May play a role in motor coordination and exploratory behavior. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11318611}.; . . 0.60585 0.20742 -0.512444034 21.55579146 50.46617 1.39771 TRMT2A 1.30587511080313e-05 0.954123928120008 0.0458630131288836 tRNA methyltransferase 2 homolog A FUNCTION: May be involved in nucleic acid metabolism and/or modifications.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;tongue;blood;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;medulla oblongata;thalamus;testis;pons;parietal lobe; . 0.10123 -0.949752638 9.32413305 192.14774 3.00453 TRMT2B 0.000100904990487132 0.942225963301543 0.0576731317079703 tRNA methyltransferase 2 homolog B FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in all tRNA. May also have a role in tRNA stabilization or maturation (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;colon;parathyroid;skin;uterus;endometrium;placenta;thyroid;visual apparatus;liver;testis;head and neck;cervix;brain;tonsil;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.08283 0.11797 -0.271755481 34.31823543 47.92547 1.34503 TRMT2B-AS1 . . . TRMT2B antisense RNA 1 . . . . . . . . . . . TRMT5 0.965267929961933 0.0347193460199884 1.2724018078825e-05 tRNA methyltransferase 5 FUNCTION: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.; . . unclassifiable (Anatomical System);ovary;heart;spinal cord;parathyroid;blood;skin;bone marrow;uterus;prostate;whole body;lung;endometrium;larynx;bone;thyroid;placenta;liver;testis;head and neck;spleen;kidney;brain;stomach; . 0.16354 0.08756 0.176444282 66.07100731 155.17583 2.72125 TRMT6 0.000492531588783058 0.992782876158246 0.00672459225297064 tRNA methyltransferase 6 FUNCTION: Substrate-binding subunit of tRNA (adenine-N(1)-)- methyltransferase, which catalyzes the formation of N(1)- methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. {ECO:0000269|PubMed:16043508}.; . TISSUE SPECIFICITY: Expressed in brain, liver, testis and ovary. {ECO:0000269|PubMed:10574461}.; ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;lung;cornea;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion; 0.14418 0.10089 -0.558357437 19.54470394 2084.86155 8.41229 TRMT10A 2.83742642062567e-05 0.930074704883386 0.0698969208524077 tRNA methyltransferase 10A FUNCTION: RNA methyltransferase. {ECO:0000269|PubMed:25053765}.; . TISSUE SPECIFICITY: Expressed in embryonic and fetal brain. It is expressed throughout the dorsal telencephalon at 8 and 11 weeks of gestation, with highest expression in ventricular zone and marginal zone. Detected in cerebellar cortex and nuclei, but not in dorsal telencephalon, at later stages. {ECO:0000269|PubMed:24204302}.; . . 0.14340 0.09092 0.327131069 73.27199811 42.87708 1.24125 TRMT10B 8.98476738851976e-05 0.784443388661003 0.215466763665112 tRNA methyltransferase 10B FUNCTION: Probable RNA methyltransferase. {ECO:0000250}.; . . . . 0.05908 . 0.21689899 68.12927577 238.6439 3.33621 TRMT10C 1.05912396335495e-05 0.350004066606254 0.649985342154112 tRNA methyltransferase 10C, mitochondrial RNase P subunit FUNCTION: Functions in mitochondrial tRNA maturation. Part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/RG9MTD1, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends. {ECO:0000269|PubMed:18984158, ECO:0000269|PubMed:21593607}.; . . . . 0.04192 0.06306 0.415317661 76.81056853 912.33262 5.87346 TRMT11 8.23830338397805e-06 0.918907635619083 0.081084126077533 tRNA methyltransferase 11 homolog FUNCTION: Catalytic subunit of an S-adenosyl-L-methionine- dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs. {ECO:0000250}.; . . colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;small intestine;heart;islets of Langerhans;hypothalamus;adrenal cortex;skeletal muscle;pancreas;lung;trabecular meshwork;liver;spleen;kidney;mammary gland;stomach;aorta; superior cervical ganglion;temporal lobe;trigeminal ganglion; 0.07875 0.11082 -0.178111357 40.44585987 191.19772 2.99877 TRMT12 0.942425529132779 0.0575294120085395 4.50588586814254e-05 tRNA methyltransferase 12 homolog (S. cerevisiae) FUNCTION: S-adenosyl-L-methionine-dependent transferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the transfer of the alpha-amino-alpha- carboxypropyl (acp) group from S-adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14) to produce wybutosine-86. {ECO:0000269|PubMed:22761755}.; . . unclassifiable (Anatomical System);islets of Langerhans;colon;blood;skin;uterus;prostate;lung;placenta;visual apparatus;liver;testis;amniotic fluid;cervix;spleen;germinal center;kidney;brain;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.08911 0.09298 0.373041938 75.29488087 73.07335 1.78552 TRMT13 2.92966422052012e-05 0.932744049515182 0.0672266538426124 tRNA methyltransferase 13 homolog (S. cerevisiae) FUNCTION: tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His). {ECO:0000250}.; . . . . 0.16797 . -0.003562597 53.72729417 19.43027 0.66791 TRMT44 1.47758486898954e-13 0.00688575851656005 0.993114241483292 tRNA methyltransferase 44 homolog (S. cerevisiae) FUNCTION: Probable adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase. {ECO:0000250}.; . . . . 0.11127 0.07994 . . 301.17928 3.69794 TRMT61A 0.00570206467721117 0.722619502465905 0.271678432856883 tRNA methyltransferase 61A FUNCTION: Catalytic subunit of tRNA (adenine-N(1)-)- methyltransferase, which catalyzes the formation of N(1)- methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. {ECO:0000269|PubMed:16043508}.; . . ovary;salivary gland;colon;skin;bone marrow;retina;uterus;prostate;endometrium;bone;iris;amniotic fluid;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;muscle;skeletal muscle;bile duct;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;caudate nucleus;trigeminal ganglion;skin; 0.15848 0.14023 -0.670411825 15.61689078 15.16028 0.54561 TRMT61B 4.00751770882134e-06 0.824673661346075 0.175322331136216 tRNA methyltransferase 61B FUNCTION: Methyltransferase that catalyzes the formation of N(1)- methyladenine at position 58 (m1A58) in various tRNAs in mitochondrion, including tRNA(Leu) (decephering codons UUA or UUG), tRNA(Lys) and tRNA(Ser) (decephering codons UCA, UCU, UCG or UCC). {ECO:0000269|PubMed:23097428}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;larynx;bone;testis;brain;gall bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;hypothalamus;muscle;lens;pancreas;lung;nasopharynx;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach; . . 0.07219 0.20030965 67.3566879 101.2815 2.17826 TRMT112 0.141017363378346 0.779309257643275 0.0796733789783801 tRNA methyltransferase 11-2 homolog (S. cerevisiae) FUNCTION: Participates both in methylation of protein and tRNA species. The heterodimer with HEMK2/N6AMT1 catalyzes N5- methylation of ETF1 on 'Gln-185', using S-adenosyl L-methionine as methyl donor. The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species. {ECO:0000269|PubMed:18539146}.; . . ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;iris;bladder;brain;gall bladder;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;greater omentum;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; whole brain;lung;liver;testis; . . -0.075159878 47.78839349 6.74528 0.24881 TRMT112P1 . . . tRNA methyltransferase 11-2 homolog (S. cerevisiae) pseudogene 1 . . . . . . . . . . . TRMT112P2 . . . tRNA methyltransferase 11-2 homolog (S. cerevisiae) pseudogene 2 . . . . . . . . . . . TRMT112P3 . . . tRNA methyltransferase 11-2 homolog (S. cerevisiae) pseudogene 3 . . . . . . . . . . . TRMT112P4 . . . tRNA methyltransferase 11-2 homolog (S. cerevisiae) pseudogene 4 . . . . . . . . . . . TRMT112P5 . . . tRNA methyltransferase 11-2 homolog (S. cerevisiae) pseudogene 5 . . . . . . . . . . . TRMT112P6 . . . tRNA methyltransferase 11-2 homolog (S. cerevisiae) pseudogene 6 . . . . . . . . . . . TRMT112P7 . . . tRNA methyltransferase 11-2 homolog (S. cerevisiae) pseudogene 7 . . . . . . . . . . . TRMU 5.75923545642307e-09 0.228805807795849 0.771194186444916 tRNA 5-methylaminomethyl-2-thiouridylate methyltransferase FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2- thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base. {ECO:0000269|PubMed:15509579, ECO:0000269|PubMed:15944150, ECO:0000269|PubMed:16826519}.; DISEASE: Liver failure, infantile, transient (LFIT) [MIM:613070]: A transient disorder of hepatic function characterized by elevated liver enzymes, jaundice, vomiting, coagulopathy, hyperbilirubinemia, increased serum lactate. Patients who survive the initial acute episode can recover, show normal development and have no recurrence. {ECO:0000269|PubMed:19732863}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Abundantly expressed in tissues with high metabolic rates including heart, liver, kidney, and brain. {ECO:0000269|PubMed:16513084}.; myocardium;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;oesophagus;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);islets of Langerhans;lens;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.19801 0.23382 -0.067881249 48.69072895 1448.29539 7.09944 TRN-ATT1-1 . . . transfer RNA-Asn (ATT) 1-1 . . . . . . . . . . . TRN-ATT1-2 . . . transfer RNA-Asn (ATT) 1-2 . . . . . . . . . . . TRN-GTT1-1 . . . transfer RNA-Asn (GTT) 1-1 . . . . . . . . . . . TRN-GTT2-1 . . . transfer RNA-Asn (GTT) 2-1 . . . . . . . . . . . TRN-GTT2-2 . . . transfer RNA-Asn (GTT) 2-2 . . . . . . . . . . . TRN-GTT2-3 . . . transfer RNA-Asn (GTT) 2-3 . . . . . . . . . . . TRN-GTT2-4 . . . transfer RNA-Asn (GTT) 2-4 . . . . . . . . . . . TRN-GTT2-5 . . . transfer RNA-Asn (GTT) 2-5 . . . . . . . . . . . TRN-GTT2-6 . . . transfer RNA-Asn (GTT) 2-6 . . . . . . . . . . . TRN-GTT3-1 . . . transfer RNA-Asn (GTT) 3-1 . . . . . . . . . . . TRN-GTT3-2 . . . transfer RNA-Asn (GTT) 3-2 . . . . . . . . . . . TRN-GTT4-1 . . . transfer RNA-Asn (GTT) 4-1 . . . . . . . . . . . TRN-GTT5-1 . . . transfer RNA-Asn (GTT) 5-1 . . . . . . . . . . . TRN-GTT6-1 . . . transfer RNA-Asn (GTT) 6-1 . . . . . . . . . . . TRN-GTT7-1 . . . transfer RNA-Asn (GTT) 7-1 . . . . . . . . . . . TRN-GTT8-1 . . . transfer RNA-Asn (GTT) 8-1 . . . . . . . . . . . TRN-GTT9-1 . . . transfer RNA-Asn (GTT) 9-1 . . . . . . . . . . . TRN-GTT9-2 . . . transfer RNA-Asn (GTT) 9-2 . . . . . . . . . . . TRN-GTT10-1 . . . transfer RNA-Asn (GTT) 10-1 . . . . . . . . . . . TRN-GTT11-1 . . . transfer RNA-Asn (GTT) 11-1 . . . . . . . . . . . TRN-GTT11-2 . . . transfer RNA-Asn (GTT) 11-2 . . . . . . . . . . . TRN-GTT12-1 . . . transfer RNA-Asn (GTT) 12-1 . . . . . . . . . . . TRN-GTT13-1 . . . transfer RNA-Asn (GTT) 13-1 . . . . . . . . . . . TRN-GTT14-1 . . . transfer RNA-Asn (GTT) 14-1 . . . . . . . . . . . TRN-GTT15-1 . . . transfer RNA-Asn (GTT) 15-1 . . . . . . . . . . . TRN-GTT16-1 . . . transfer RNA-Asn (GTT) 16-1 . . . . . . . . . . . TRN-GTT16-2 . . . transfer RNA-Asn (GTT) 16-2 . . . . . . . . . . . TRN-GTT16-3 . . . transfer RNA-Asn (GTT) 16-3 . . . . . . . . . . . TRN-GTT16-4 . . . transfer RNA-Asn (GTT) 16-4 . . . . . . . . . . . TRN-GTT16-5 . . . transfer RNA-Asn (GTT) 16-5 . . . . . . . . . . . TRN-GTT17-1 . . . transfer RNA-Asn (GTT) 17-1 . . . . . . . . . . . TRN-GTT18-1 . . . transfer RNA-Asn (GTT) 18-1 . . . . . . . . . . . TRN-GTT19-1 . . . transfer RNA-Asn (GTT) 19-1 . . . . . . . . . . . TRN-GTT20-1 . . . transfer RNA-Asn (GTT) 20-1 . . . . . . . . . . . TRN-GTT21-1 . . . transfer RNA-Asn (GTT) 21-1 . . . . . . . . . . . TRN-GTT22-1 . . . transfer RNA-Asn (GTT) 22-1 . . . . . . . . . . . TRN-GTT23-1 . . . transfer RNA-Asn (GTT) 23-1 . . . . . . . . . . . TRNAU1AP 0.882819951620334 0.117123465524106 5.6582855560226e-05 tRNA selenocysteine 1 associated protein 1 FUNCTION: Involved in the early steps of selenocysteine biosynthesis and tRNA(Sec) charging to the later steps resulting in the cotranslational incorporation of selenocysteine into selenoproteins. Stabilizes the SECISBP2, EEFSEC and tRNA(Sec) complex. May be involved in the methylation of tRNA(Sec). Enhances efficiency of selenoproteins synthesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:16508009}.; . . . . 0.06802 0.08243 -0.227663163 37.11370606 17.1905 0.60390 TRNP1 . . . TMF1-regulated nuclear protein 1 FUNCTION: DNA-binding factor that regulates the expression of a subset of genes and plays a key role in tangential, radial, and lateral expansion of the brain neocortex. Regulates neural stem cells proliferation and the production of intermediate neural progenitors and basal radial glial cells affecting the process of cerebral cortex gyrification. May control the proliferation rate of cells by regulating their progression through key cell-cycle transition points (By similarity). {ECO:0000250}.; . . . . . . . . 7.20015 0.27144 TRNT1 2.45863122935093e-06 0.495284734490954 0.504712806877816 tRNA nucleotidyl transferase, CCA-adding, 1 FUNCTION: Isoform 1: Adds and repairs the conserved 3'-CCA sequence necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates.; DISEASE: Sideroblastic anemia with B-cell immunodeficiency, periodic fevers, and developmental delay (SIFD) [MIM:616084]: An autosomal recessive disease characterized by severe sideroblastic anemia with onset in the neonatal period or infancy, recurrent periodic fevers without an infectious etiology, B-cell lymphopenia and hypogammaglobulinemia. Affected individuals show delayed psychomotor development with variable neurodegeneration. Additional variable features include sensorineural hearing loss, retinitis pigmentosa, nephrocalcinosis, and cardiomyopathy. {ECO:0000269|PubMed:25193871}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;salivary gland;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; pons;trigeminal ganglion;skeletal muscle; 0.08628 0.11498 -0.602450568 17.91106393 37.50974 1.11715 TRO 0.00166962000566844 0.971344510459158 0.0269858695351734 trophinin FUNCTION: Could be involved with bystin and tastin in a cell adhesion molecule complex that mediates an initial attachment of the blastocyst to uterine epithelial cells at the time of the embryo implantation. Directly responsible for homophilic cell adhesion.; . TISSUE SPECIFICITY: Strong expression at implantation sites. Found in the placenta from the sixth week of pregnancy. Was localized in the cytoplasm of the syncytiotrophoblast in the chorionic villi and in endometrial decidual cells at the uteroplacental interface. After week 10, the level decreased and then disappeared from placental villi. Also found in macrophages.; smooth muscle;ovary;parathyroid;skin;uterus;prostate;whole body;cochlea;endometrium;synovium;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cerebellum cortex;islets of Langerhans;blood;skeletal muscle;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;peripheral nerve; amygdala;whole brain;superior cervical ganglion;occipital lobe;fetal brain;hypothalamus;prefrontal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.44541 0.13979 0.183723206 66.24793583 202.0068 3.06707 TROAP 3.02009096735006e-07 0.981604197165882 0.0183955008250209 trophinin associated protein FUNCTION: Could be involved with bystin and trophinin in a cell adhesion molecule complex that mediates an initial attachment of the blastocyst to uterine epithelial cells at the time of the embryo implantation.; . TISSUE SPECIFICITY: Strong expression at implantation sites. Was exclusively localized to the apical side of the syncytiotrophoblast. Also found in macrophages.; ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;endometrium;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;urinary;pharynx;blood;skeletal muscle;breast;lung;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node; 0.29478 0.09516 0.205769367 67.49823071 680.65258 5.21652 TROVE2 0.0190448996422325 0.976851890276839 0.00410321008092792 TROVE domain family member 2 FUNCTION: RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs. May stabilize some of these RNAs and protect them from degradation. {ECO:0000269|PubMed:18056422}.; . . . . 0.09993 . -0.336073593 30.55555556 40.63076 1.19101 TRP-AGG1-1 . . . transfer RNA-Pro (AGG) 1-1 . . . . . . . . . . . TRP-AGG2-1 . . . transfer RNA-Pro (AGG) 2-1 . . . . . . . . . . . TRP-AGG2-2 . . . transfer RNA-Pro (AGG) 2-2 . . . . . . . . . . . TRP-AGG2-3 . . . transfer RNA-Pro (AGG) 2-3 . . . . . . . . . . . TRP-AGG2-4 . . . transfer RNA-Pro (AGG) 2-4 . . . . . . . . . . . TRP-AGG2-5 . . . transfer RNA-Pro (AGG) 2-5 FUNCTION: DNA-binding factor that regulates the expression of a subset of genes and plays a key role in tangential, radial, and lateral expansion of the brain neocortex. Regulates neural stem cells proliferation and the production of intermediate neural progenitors and basal radial glial cells affecting the process of cerebral cortex gyrification. May control the proliferation rate of cells by regulating their progression through key cell-cycle transition points (By similarity). {ECO:0000250}.; . . . . . . . . . . TRP-AGG2-6 . . . transfer RNA-Pro (AGG) 2-6 FUNCTION: DNA-binding factor that regulates the expression of a subset of genes and plays a key role in tangential, radial, and lateral expansion of the brain neocortex. Regulates neural stem cells proliferation and the production of intermediate neural progenitors and basal radial glial cells affecting the process of cerebral cortex gyrification. May control the proliferation rate of cells by regulating their progression through key cell-cycle transition points (By similarity). {ECO:0000250}.; . . . . . . . . . . TRP-AGG2-7 . . . transfer RNA-Pro (AGG) 2-7 . . . . . . . . . . . TRP-AGG2-8 . . . transfer RNA-Pro (AGG) 2-8 . . . . . . . . . . . TRP-AGG3-1 . . . transfer RNA-Pro (AGG) 3-1 . . . . . . . . . . . TRP-AGG4-1 . . . transfer RNA-Pro (AGG) 4-1 . . . . . . . . . . . TRP-AGG5-1 . . . transfer RNA-Pro (AGG) 5-1 . . . . . . . . . . . TRP-AGG6-1 . . . transfer RNA-Pro (AGG) 6-1 . . . . . . . . . . . TRP-CGG1-1 . . . transfer RNA-Pro (CGG) 1-1 . . . . . . . . . . . TRP-CGG1-2 . . . transfer RNA-Pro (CGG) 1-2 . . . . . . . . . . . TRP-CGG1-3 . . . transfer RNA-Pro (CGG) 1-3 . . . . . . . . . . . TRP-CGG2-1 . . . transfer RNA-Pro (CGG) 2-1 . . . . . . . . . . . TRP-GGG1-1 . . . transfer RNA-Pro (GGG) 1-1 . . . . . . . . . . . TRP-TGG1-1 . . . transfer RNA-Pro (TGG) 1-1 . . . . . . . . . . . TRP-TGG2-1 . . . transfer RNA-Pro (TGG) 2-1 . . . . . . . . . . . TRP-TGG3-1 . . . transfer RNA-Pro (TGG) 3-1 . . . . . . . . . . . TRP-TGG3-2 . . . transfer RNA-Pro (TGG) 3-2 . . . . . . . . . . . TRP-TGG3-3 . . . transfer RNA-Pro (TGG) 3-3 . . . . . . . . . . . TRP-TGG3-4 . . . transfer RNA-Pro (TGG) 3-4 . . . . . . . . . . . TRP-TGG3-5 . . . transfer RNA-Pro (TGG) 3-5 . . . . . . . . . . . TRP-TGG4-1 . . . transfer RNA-Pro (TGG) 4-1 . . . . . . . . . . . TRP-TGG5-1 . . . transfer RNA-Pro (TGG) 5-1 . . . . . . . . . . . TRPA1 9.96588682289508e-23 0.00699188285653192 0.993008117143468 transient receptor potential cation channel subfamily A member 1 FUNCTION: Receptor-activated non-selective cation channel involved in detection of pain and possibly also in cold perception and inner ear function (PubMed:25389312, PubMed:25855297). Has a central role in the pain response to endogenous inflammatory mediators and to a diverse array of volatile irritants, such as mustard oil, cinnamaldehyde, garlic and acrolein, an irritant from tears gas and vehicule exhaust fumes (PubMed:25389312, PubMed:20547126). Is also activated by menthol (in vitro)(PubMed:25389312). Acts also as a ionotropic cannabinoid receptor by being activated by delta(9)-tetrahydrocannabinol (THC), the psychoactive component of marijuana (PubMed:25389312). May be a component for the mechanosensitive transduction channel of hair cells in inner ear, thereby participating in the perception of sounds. Probably operated by a phosphatidylinositol second messenger system (By similarity). {ECO:0000250|UniProtKB:Q8BLA8, ECO:0000269|PubMed:20547126, ECO:0000269|PubMed:25389312, ECO:0000269|PubMed:25855297}.; DISEASE: Episodic pain syndrome, familial, 1 (FEPS1) [MIM:615040]: An autosomal dominant neurologic disorder characterized by onset in infancy of episodic debilitating upper body pain triggered by fasting, cold, and physical stress. The period of intense pain is accompanied by breathing difficulties, tachycardia, sweating, generalized pallor, peribuccal cyanosis, and stiffness of the abdominal wall. Affected individuals do not manifest altered pain sensitivity outside the episodes. {ECO:0000269|PubMed:20547126}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at very low level. Expressed at very low level in human fibroblasts and at a moderate level in liposarcoma cells. {ECO:0000269|PubMed:10066796}.; unclassifiable (Anatomical System);lymphoreticular;lung;larynx;placenta;colon;head and neck;kidney;skin;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.13702 . 0.786269343 87.29063458 3070.92102 10.53278 TRPC1 0.784921837002802 0.215075724161062 2.43883613549346e-06 transient receptor potential cation channel subfamily C member 1 FUNCTION: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Seems to be also activated by intracellular calcium store depletion. {ECO:0000269|PubMed:15016832}.; . TISSUE SPECIFICITY: Seems to be ubiquitous.; sympathetic chain;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;lens;lung;adrenal gland;macula lutea;liver;spleen;kidney;stomach; amygdala;superior cervical ganglion;hypothalamus;ciliary ganglion;atrioventricular node; 0.54755 0.17821 -0.336073593 30.55555556 421.60875 4.28835 TRPC2 . . . transient receptor potential cation channel subfamily C member 2, pseudogene . . . . . 0.54481 . . . . . TRPC3 0.000446956189740094 0.997968820258243 0.00158422355201655 transient receptor potential cation channel subfamily C member 3 FUNCTION: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C, and by inositol 1,4,5- triphosphate receptors (ITPR) with bound IP3. May also be activated by internal calcium store depletion. {ECO:0000269|PubMed:20095964, ECO:0000269|PubMed:8646775, ECO:0000269|PubMed:9417057, ECO:0000269|PubMed:9930701}.; . TISSUE SPECIFICITY: Expressed predominantly in brain and at much lower levels in ovary, colon, small intestine, lung, prostate, placenta and testis.; unclassifiable (Anatomical System);heart;brain; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.34890 0.24631 -1.241834664 5.414012739 79.70005 1.88651 TRPC4 0.967651076497012 0.0323489056116487 1.78913391733288e-08 transient receptor potential cation channel subfamily C member 4 FUNCTION: Form a receptor-activated non-selective calcium permeant cation channel. Acts as a cell-cell contact-dependent endothelial calcium entry channel. Probably operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Mediates cation entry, with an enhanced permeability to barium over calcium. May also be activated by intracellular calcium store depletion. {ECO:0000269|PubMed:16144838, ECO:0000269|PubMed:19996314}.; . TISSUE SPECIFICITY: Strongly expressed in placenta. Expressed at lower levels in heart, pancreas, kidney and brain. Expressed in endothelial cells. Isoform alpha was found to be the predominant isoform. Isoform beta was not found in pancreas and brain. {ECO:0000269|PubMed:19996314}.; unclassifiable (Anatomical System);uterus;lung;frontal lobe;heart;skin; uterus;dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;temporal lobe;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.47812 . -1.175687564 5.974286388 36.07747 1.08368 TRPC4AP 0.999538656142253 0.000461343844438968 1.33077529566054e-11 transient receptor potential cation channel subfamily C member 4 associated protein FUNCTION: Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control. The DCX(TRUSS) complex specifically mediates the polyubiquitination and subsequent degradation of MYC. Also participates in the activation of NFKB1 in response to ligation of TNFRSF1A, possibly by linking TNFRSF1A to the IKK signalosome. Involved in JNK activation via its interaction with TRAF2. Also involved in elevation of endoplasmic reticulum Ca(2+) storage reduction in response to CHRM1. {ECO:0000269|PubMed:20551172}.; . . myocardium;lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;ganglion;frontal lobe;endometrium;thyroid;iris;amniotic fluid;bladder;brain;heart;cartilage;urinary;pharynx;blood;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.44984 0.11627 -1.263883952 5.260674687 88.3574 2.01455 TRPC5 0.993636098486069 0.00636370576747568 1.95746455345381e-07 transient receptor potential cation channel subfamily C member 5 FUNCTION: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Has also been shown to be calcium-selective (By similarity). May also be activated by intracellular calcium store depletion. {ECO:0000250, ECO:0000269|PubMed:16284075}.; . TISSUE SPECIFICITY: Expressed in brain with higher levels in fetal brain. Found in cerebellum and occipital pole. {ECO:0000269|PubMed:9687496}.; ovary;thyroid;placenta;parathyroid; trigeminal ganglion; 0.15414 0.17421 -0.466531444 23.51380042 40.06446 1.17759 TRPC5OS . . . TRPC5 opposite strand . . . . . . . . . . . TRPC6 0.00456410505335574 0.995159289159918 0.00027660578672581 transient receptor potential cation channel subfamily C member 6 FUNCTION: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C. Seems not to be activated by intracellular calcium store depletion.; DISEASE: Focal segmental glomerulosclerosis 2 (FSGS2) [MIM:603965]: A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation. {ECO:0000269|PubMed:15879175, ECO:0000269|PubMed:15924139, ECO:0000269|PubMed:21734084}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed primarily in placenta, lung, spleen, ovary and small intestine. Expressed in podocytes and is a component of the glomerular slit diaphragm. {ECO:0000269|PubMed:15924139}.; heart;choroid;fovea centralis;lens;retina;prostate;optic nerve;whole body;lung;placenta;macula lutea;testis;spleen; superior cervical ganglion; 0.16462 0.18467 -1.285933373 5.083746167 871.11284 5.74820 TRPC6P . . . transient receptor potential cation channel subfamily C member 6, pseudogene . . . . . . . . . . . TRPC7 0.00298615175665186 0.996503540966566 0.000510307276781864 transient receptor potential cation channel subfamily C member 7 FUNCTION: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) (By similarity). May also be activated by intracellular calcium store depletion. {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;islets of Langerhans; dorsal root ganglion;uterus corpus;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.35540 0.14409 -0.132199953 43.97853267 84.6537 1.95946 TRPC7-AS1 . . . TRPC7 antisense RNA 1 . . . . . . . . . . . TRPC7-AS2 . . . TRPC7 antisense RNA 2 . . . . . . . . . . . TRPM1 1.16831980652389e-31 0.000371176768014892 0.999628823231985 transient receptor potential cation channel subfamily M member 1 FUNCTION: Cation channel essential for the depolarizing photoresponse of retinal ON bipolar cells. It is part of the GRM6 signaling cascade. May play a role in metastasis suppression (By similarity). May act as a spontaneously active, calcium-permeable plasma membrane channel. {ECO:0000250, ECO:0000269|PubMed:11535825, ECO:0000269|PubMed:19878917, ECO:0000269|PubMed:19896109}.; DISEASE: Night blindness, congenital stationary, 1C (CSNB1C) [MIM:613216]: A non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia. {ECO:0000269|PubMed:19878917, ECO:0000269|PubMed:19896109, ECO:0000269|PubMed:19896113}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the retina where it localizes to the outer plexiform layer. Highly expressed in benign melanocytic nevi and diffusely expressed in various in situ melanomas, but not detected in melanoma metastases. Also expressed in melanocytes and pigmented metastatic melanoma cell lines. In melanocytes expression appears to be regulated at the level of transcription and mRNA processing. {ECO:0000269|PubMed:11112417, ECO:0000269|PubMed:19896109, ECO:0000269|PubMed:9537257}.; unclassifiable (Anatomical System);heart;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;optic nerve;lung;macula lutea;visual apparatus;testis;kidney;mammary gland; superior cervical ganglion; 0.14509 0.13967 1.754582795 96.69143666 1654.25141 7.51872 TRPM2 3.36526227253837e-25 0.0124740636976531 0.987525936302347 transient receptor potential cation channel subfamily M member 2 FUNCTION: Nonselective, voltage-independent cation channel mediating sodium and calcium ion influx in response to oxidative stress. Extracellular calcium passes through the channel and acts from the intracellular side as a positive regulator in channel activation. Activated by ADP-ribose, nicotinamide adenine dinucleotide (NAD(+)), reactive nitrogen species and arachidonic acid. Inactivated by intracellular ATP. Confers susceptibility to cell death following oxidative stress. Isoform 2 does not seem to be regulated by ADPR. Has ADP-ribose pyrophosphatase activity. {ECO:0000269|PubMed:11804595}.; . TISSUE SPECIFICITY: Highly expressed in brain and peripheral blood cells, such as neutrophils. Also detected in bone marrow, spleen, heart, liver and lung. Isoform 2 is found in neutrophil granulocytes. {ECO:0000269|PubMed:11385575, ECO:0000269|PubMed:11509734}.; unclassifiable (Anatomical System);smooth muscle;islets of Langerhans;colon;blood;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;optic nerve;lung;frontal lobe;placenta;bone;macula lutea;testis;cervix;brain;bladder;stomach; superior cervical ganglion; 0.09582 0.09727 0.995759702 90.56381222 1077.95828 6.29417 TRPM2-AS . . . TRPM2 antisense RNA . . . . . . . . . . . TRPM3 7.73754359412344e-06 0.99999220046704 6.19893655150819e-08 transient receptor potential cation channel subfamily M member 3 FUNCTION: Calcium channel mediating constitutive calcium ion entry. Its activity is increased by reduction in extracellular osmolarity, by store depletion and muscarinic receptor activation. {ECO:0000269|PubMed:12672799, ECO:0000269|PubMed:12672827}.; . TISSUE SPECIFICITY: Expressed primarily in the kidney and, at lower levels, in brain, testis, ovary, pancreas and spinal cord. Expression in the brain and kidney was determined at protein level. In the kidney, expressed predominantly in the collecting tubular epithelium in the medulla, medullary rays, and periglomerular regions; in the brain, highest levels are found in the cerebellum, choroid plexus, the locus coeruleus, the posterior thalamus and the substantia nigra. Down-regulated in renal tumors compared to normal kidney. {ECO:0000269|PubMed:12672799, ECO:0000269|PubMed:12672827}.; amygdala;unclassifiable (Anatomical System);meninges;spinal cord;fovea centralis;choroid;lens;skin;retina;whole body;pia mater;thyroid;macula lutea;hippocampus;iris;pituitary gland;head and neck;kidney;dura mater; dorsal root ganglion;superior cervical ganglion;medulla oblongata;testis - interstitial;cerebellum peduncles;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;cerebellum; 0.47591 0.11400 -1.093242511 6.982778957 3906.11961 12.35182 TRPM4 6.36301802229804e-19 0.0857716189132736 0.914228381086726 transient receptor potential cation channel subfamily M member 4 FUNCTION: Calcium-activated non selective (CAN) cation channel that mediates membrane depolarization. While it is activated by increase in intracellular Ca(2+), it is impermeable to it. Mediates transport of monovalent cations (Na(+) > K(+) > Cs(+) > Li(+)), leading to depolarize the membrane. It thereby plays a central role in cadiomyocytes, neurons from entorhinal cortex, dorsal root and vomeronasal neurons, endocrine pancreas cells, kidney epithelial cells, cochlea hair cells etc. Participates in T-cell activation by modulating Ca(2+) oscillations after T lymphocyte activation, which is required for NFAT-dependent IL2 production. Involved in myogenic constriction of cerebral arteries. Controls insulin secretion in pancreatic beta-cells. May also be involved in pacemaking or could cause irregular electrical activity under conditions of Ca(2+) overload. Affects T-helper 1 (Th1) and T-helper 2 (Th2) cell motility and cytokine production through differential regulation of calcium signaling and NFATC1 localization. Enhances cell proliferation through up-regulation of the beta-catenin signaling pathway. {ECO:0000269|PubMed:12015988, ECO:0000269|PubMed:12799367, ECO:0000269|PubMed:15121803, ECO:0000269|PubMed:15472118, ECO:0000269|PubMed:15550671, ECO:0000269|PubMed:16806463, ECO:0000269|PubMed:20625999, ECO:0000269|PubMed:20656926}.; DISEASE: Progressive familial heart block 1B (PFHB1B) [MIM:604559]: A cardiac bundle branch disorder characterized by progressive alteration of cardiac conduction through the His- Purkinje system, with a pattern of a right bundle-branch block and/or left anterior hemiblock occurring individually or together. It leads to complete atrio-ventricular block causing syncope and sudden death. {ECO:0000269|PubMed:19726882, ECO:0000269|PubMed:20562447, ECO:0000269|PubMed:21887725}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed with a high expression in intestine and prostate. In brain, it is both expressed in whole cerebral arteries and isolated vascular smooth muscle cells. Prominently expressed in Purkinje fibers. Expressed at higher levels in T-helper 2 (Th2) cells as compared to T-helper 1 (Th1) cells. {ECO:0000269|PubMed:11535825, ECO:0000269|PubMed:12015988, ECO:0000269|PubMed:12799367, ECO:0000269|PubMed:15472118, ECO:0000269|PubMed:16777713, ECO:0000269|PubMed:19726882, ECO:0000269|PubMed:20656926}.; ovary;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;optic nerve;bone;testis;brain;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;liver;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;prostate;ciliary ganglion;skeletal muscle; 0.14525 0.10386 -1.140954241 6.387119604 305.29283 3.72037 TRPM5 7.63575945842109e-17 0.0288707013445574 0.971129298655442 transient receptor potential cation channel subfamily M member 5 FUNCTION: Voltage-modulated Ca(2+)-activated, monovalent cation channel (VCAM) that mediates a transient membrane depolarization and plays a central role in taste transduction. Monovalent- specific, non-selective cation channel that mediates the transport of Na(+), K(+) and Cs(+) ions equally well. Activated directly by increases in intracellular Ca(2+), but is impermeable to it. Gating is voltage-dependent and displays rapid activation and deactivation kinetics upon channel stimulation even during sustained elevations in Ca(2+). Also activated by a fast intracellular Ca(2+) increase in response to inositol 1,4,5- triphosphate-producing receptor agonists. The channel is blocked by extracellular acidification. External acidification has 2 effects, a fast reversible block of the current and a slower irreversible enhancement of current inactivation. Is a highly temperature-sensitive, heat activated channel showing a steep increase of inward currents at temperatures between 15 and 35 degrees Celsius. Heat activation is due to a shift of the voltage- dependent activation curve to negative potentials. Activated by arachidonic acid in vitro. May be involved in perception of bitter, sweet and umami tastes. May also be involved in sensing semiochemicals. {ECO:0000269|PubMed:14634208}.; . TISSUE SPECIFICITY: Strongly expressed in fetal brain, liver and kidney, and in adult prostate, testis, ovary, colon and peripheral blood leukocytes. Also expressed in a large proportion of Wilms' tumors and rhabdomyosarcomas. In monochromosomal cell lines shows exclusive paternal expression. {ECO:0000269|PubMed:10607831}.; colon; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skin; 0.14125 . -0.841660883 11.29393725 997.37986 6.08638 TRPM6 0.588344973192852 0.411655026807063 8.44886920994781e-14 transient receptor potential cation channel subfamily M member 6 FUNCTION: Essential ion channel and serine/threonine-protein kinase. Crucial for magnesium homeostasis. Has an important role in epithelial magnesium transport and in the active magnesium absorption in the gut and kidney. Isoforms of the type M6-kinase lack the ion channel region.; . TISSUE SPECIFICITY: Highly expressed in kidney and colon. Isoform TRPM6a and isoform TRPM6b, are coexpressed with TRPM7 in kidney, and testis, and are also found in several cell lines of lung origin. Isoform TRPM6c is detected only in testis and in NCI-H510A small cell lung carcinoma cells.; unclassifiable (Anatomical System);uterus;bile duct;lung;heart;bone;testis;kidney;brain;skin;retina; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.14215 0.17378 -0.577047007 18.72493513 2938.23469 10.28399 TRPM7 1.65553537627815e-08 0.999999977581291 5.86335501405641e-09 transient receptor potential cation channel subfamily M member 7 FUNCTION: Essential ion channel and serine/threonine-protein kinase. Divalent cation channel permeable to calcium and magnesium. Has a central role in magnesium ion homeostasis and in the regulation of anoxic neuronal cell death. Involved in TNF- induced necroptosis downstream of MLKL by mediating calcium influx. The kinase activity is essential for the channel function. May be involved in a fundamental process that adjusts plasma membrane divalent cation fluxes according to the metabolic state of the cell. Phosphorylates annexin A1 (ANXA1). {ECO:0000269|PubMed:12887921, ECO:0000269|PubMed:15485879, ECO:0000269|PubMed:24316671}.; DISEASE: Amyotrophic lateral sclerosis-parkinsonism/dementia complex 1 (ALS-PDC1) [MIM:105500]: A neurodegenerative disorder characterized by chronic, progressive and uniformly fatal amyotrophic lateral sclerosis and parkinsonism-dementia. Both diseases are known to occur in the same kindred, the same sibship and even the same individual. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . smooth muscle;ovary;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;pituitary gland;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;spinal cord;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.28336 0.14669 -0.834069467 11.49445624 817.4218 5.61593 TRPM8 4.73679846782498e-15 0.905281974799752 0.0947180252002437 transient receptor potential cation channel subfamily M member 8 FUNCTION: Receptor-activated non-selective cation channel involved in detection of sensations such as coolness, by being activated by cold temperature below 25 degrees Celsius. Activated by icilin, eucalyptol, menthol, cold and modulation of intracellular pH. Involved in menthol sensation. Permeable for monovalent cations sodium, potassium, and cesium and divalent cation calcium. Temperature sensing is tightly linked to voltage-dependent gating. Activated upon depolarization, changes in temperature resulting in graded shifts of its voltage-dependent activation curves. The chemical agonist menthol functions as a gating modifier, shifting activation curves towards physiological membrane potentials. Temperature sensitivity arises from a tenfold difference in the activation energies associated with voltage-dependent opening and closing. In prostate cancer cells, shows strong inward rectification and high calcium selectivity in contrast to its behavior in normal cells which is characterized by outward rectification and poor cationic selectivity. Plays a role in prostate cancer cell migration (PubMed:25559186). Isoform 2 and isoform 3 negatively regulate menthol- and cold-induced channel activity by stabilizing the closed state of the channel. {ECO:0000269|PubMed:15306801, ECO:0000269|PubMed:16174775, ECO:0000269|PubMed:22128173, ECO:0000269|PubMed:25559186}.; . TISSUE SPECIFICITY: Expressed in prostate. Also expressed in prostate tumors and in non-prostatic primary tumors such as colon, lung, breast and skin tumors. {ECO:0000269|PubMed:11325849, ECO:0000269|PubMed:12858355, ECO:0000269|PubMed:16174775, ECO:0000269|PubMed:22128173}.; unclassifiable (Anatomical System);uterus;prostate;lung;heart;endometrium;liver;colon;brain;skin;retina; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.09174 . -1.429430352 4.028072659 3815.40564 12.14320 TRPS1 0.990109017620343 0.00989095879529632 2.35843609417322e-08 transcriptional repressor GATA binding 1 FUNCTION: Transcriptional repressor. Binds specifically to GATA sequences and represses expression of GATA-regulated genes at selected sites and stages in vertebrate development. Regulates chondrocyte proliferation and differentiation. Executes multiple functions in proliferating chondrocytes, expanding the region of distal chondrocytes, activating proliferation in columnar cells and supporting the differentiation of columnar into hypertrophic chondrocytes. {ECO:0000269|PubMed:12885770, ECO:0000269|PubMed:17391059}.; DISEASE: Tricho-rhino-phalangeal syndrome 1 (TRPS1) [MIM:190350]: Autosomal dominant disorder characterized by craniofacial and skeletal abnormalities. It is allelic with tricho-rhino-phalangeal type 3. Typical features include sparse scalp hair, a bulbous tip of the nose, protruding ears, a long flat philtrum and a thin upper vermilion border. Skeletal defects include cone-shaped epiphyses at the phalanges, hip malformations and short stature. {ECO:0000269|PubMed:14560312}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Tricho-rhino-phalangeal syndrome 2 (TRPS2) [MIM:150230]: A syndrome that combines the clinical features of tricho-rhino- phalangeal syndrome type 1 and multiple exostoses type 1. Affected individuals manifest multiple dysmorphic facial features including large, laterally protruding ears, a bulbous nose, an elongated upper lip, as well as sparse scalp hair, winged scapulae, multiple cartilaginous exostoses, redundant skin, and mental retardation. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration resulting in the loss of functional copies of TRPS1 and EXT1 has been found in TRPS2 patients.; DISEASE: Tricho-rhino-phalangeal syndrome 3 (TRPS3) [MIM:190351]: Autosomal dominant disorder characterized by craniofacial and skeletal abnormalities. It is allelic with tricho-rhino-phalangeal type 1. In TRPS3 a more severe brachydactyly and growth retardation are observed. {ECO:0000269|PubMed:11112658, ECO:0000269|PubMed:11807863}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed in the adult. Found in fetal brain, lung, kidney, liver, spleen and thymus. More highly expressed in androgen-dependent than in androgen-independent prostate cancer cells.; medulla oblongata;ovary;parathyroid;skin;uterus;prostate;whole body;cochlea;endometrium;thyroid;bone;amniotic fluid;brain;unclassifiable (Anatomical System);heart;cartilage;hypothalamus;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.66817 0.13373 -1.747196778 2.359046945 118.19802 2.36482 TRPT1 0.00867584904463919 0.934965710277822 0.0563584406775384 tRNA phosphotransferase 1 FUNCTION: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate. {ECO:0000305|PubMed:14504659}.; . TISSUE SPECIFICITY: Widely expressed. Weakly or not expressed in lung, spleen, small intestine and peripheral blood leukocytes. {ECO:0000269|PubMed:14504659}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.07164 0.09553 0.393270925 76.04977589 1546.19179 7.29151 TRPV1 5.63846239630988e-14 0.0276808919523423 0.972319108047601 transient receptor potential cation channel subfamily V member 1 FUNCTION: Ligand-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Can be activated by endogenous compounds, including 12- hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis (By similarity). Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca(2+)-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. {ECO:0000250, ECO:0000269|PubMed:11050376, ECO:0000269|PubMed:11226139, ECO:0000269|PubMed:11243859, ECO:0000269|PubMed:12077606}.; . TISSUE SPECIFICITY: Widely expressed at low levels. Expression is elevated in dorsal root ganglia. In skin, expressed in cutaneous sensory nerve fibers, mast cells, epidermal keratinocytes, dermal blood vessels, the inner root sheet and the infundibulum of hair follicles, differentiated sebocytes, sweat gland ducts, and the secretory portion of eccrine sweat glands (at protein level). {ECO:0000269|PubMed:11050376, ECO:0000269|PubMed:11243859, ECO:0000269|PubMed:14987252}.; unclassifiable (Anatomical System);lymphoreticular;ovary;tongue;colon;blood;fovea centralis;choroid;lens;retina;bone marrow;breast;pancreas;optic nerve;macula lutea;liver;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skin; 0.11105 0.25778 0.009173042 54.15782024 0.20313 0.00422 TRPV2 0.00562915719411862 0.99432951106221 4.13317436711549e-05 transient receptor potential cation channel subfamily V member 2 FUNCTION: Calcium-permeable, non-selective cation channel with an outward rectification. Seems to be regulated, at least in part, by IGF-I, PDGF and neuropeptide head activator. May transduce physical stimuli in mast cells. Activated by temperatures higher than 52 degrees Celsius; is not activated by vanilloids and acidic pH. {ECO:0000269|PubMed:10201375}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;larynx;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;alveolus;liver;spleen;head and neck;cervix;kidney;aorta;stomach; trigeminal ganglion; 0.10412 0.11814 -1.636932785 2.824958717 330.68587 3.86609 TRPV3 8.74042179448203e-14 0.127313261539906 0.872686738460006 transient receptor potential cation channel subfamily V member 3 FUNCTION: Putative receptor-activated non-selective calcium permeant cation channel. It is activated by innocuous (warm) temperatures and shows an increased response at noxious temperatures greater than 39 degrees Celsius. Activation exhibits an outward rectification. May associate with TRPV1 and may modulate its activity. Is a negative regulator of hair growth and cycling: TRPV3-coupled signaling suppresses keratinocyte proliferation in hair follicles and induces apoptosis and premature hair follicle regression (catagen). {ECO:0000269|PubMed:12077604, ECO:0000269|PubMed:12077606, ECO:0000269|PubMed:21593771}.; DISEASE: Palmoplantar keratoderma, non-epidermolytic, focal 2 (FNEPPK2) [MIM:616400]: A dermatological disorder characterized by non-epidermolytic, abnormal thickening of the skin on the palms and soles. Focal palmoplantar keratoderma consists of localized areas of hyperkeratosis located mainly on pressure points and sites of recurrent friction. {ECO:0000269|PubMed:25285920}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Abundantly expressed in CNS. Widely expressed at low levels. Detected in dorsal root ganglion (at protein level). Expressed in the keratinocyte layers of the outer root sheath and, to lesser extent, to the matrix of the hair follicles (at protein level). {ECO:0000269|PubMed:12077604, ECO:0000269|PubMed:12077606, ECO:0000269|PubMed:21593771}.; spinal ganglion;skeletal muscle; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.25208 . 0.233278626 68.58339231 3345.04135 11.07770 TRPV4 7.31947219105235e-06 0.995214650922626 0.0047780296051827 transient receptor potential cation channel subfamily V member 4 FUNCTION: Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity. Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification (PubMed:18826956, PubMed:18695040). Also activated by heat, low pH, citrate and phorbol esters (PubMed:18826956, PubMed:18695040). Increase of intracellular Ca(2+) potentiates currents. Channel activity seems to be regulated by a calmodulin-dependent mechanism with a negative feedback mechanism (PubMed:12724311, PubMed:18826956). Promotes cell-cell junction formation in skin keratinocytes and plays an important role in the formation and/or maintenance of functional intercellular barriers (By similarity). Acts as a regulator of intracellular Ca(2+) in synoviocytes (PubMed:19759329). Plays an obligatory role as a molecular component in the nonselective cation channel activation induced by 4-alpha-phorbol 12,13- didecanoate and hypotonic stimulation in synoviocytes and also regulates production of IL-8 (PubMed:19759329). Together with PKD2, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). Negatively regulates expression of PPARGC1A, UCP1, oxidative metabolism and respiration in adipocytes (By similarity). Regulates expression of chemokines and cytokines related to proinflammatory pathway in adipocytes (By similarity). Together with AQP5, controls regulatory volume decrease in salivary epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q9EPK8, ECO:0000269|PubMed:11025659, ECO:0000269|PubMed:12724311, ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:18826956, ECO:0000269|PubMed:19759329}.; DISEASE: Brachyolmia 3 (BCYM3) [MIM:113500]: A form of brachyolmia, a clinically and genetically heterogeneous skeletal dysplasia primarily affecting the spine and characterized by a short trunk, short stature, and platyspondyly. BCYM3 is an autosomal dominant form with severe scoliosis with or without kyphosis, and flattened irregular cervical vertebrae. {ECO:0000269|PubMed:18587396}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spondylometaphyseal dysplasia Kozlowski type (SMDK) [MIM:184252]: A form of spondylometaphyseal dysplasia, a group of short stature disorders distinguished by abnormalities in the vertebrae and the metaphyses of the tubular bones. It is characterized by postnatal dwarfism, significant scoliosis and mild metaphyseal abnormalities in the pelvis. The vertebrae exhibit platyspondyly and overfaced pedicles. {ECO:0000269|PubMed:19232556, ECO:0000269|PubMed:20577006}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Metatropic dysplasia (MTD) [MIM:156530]: A severe spondyloepimetaphyseal dysplasia characterized by short limbs with limitation and enlargement of joints and usually severe kyphoscoliosis. Radiologic features include severe platyspondyly, severe metaphyseal enlargement and shortening of long bones. {ECO:0000269|PubMed:19232556, ECO:0000269|PubMed:20425821, ECO:0000269|PubMed:20577006, ECO:0000269|Ref.6}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Neuronopathy, distal hereditary motor, 8 (HMN8) [MIM:600175]: A clinically variable, neuromuscular disorder characterized by congenital lower motor neuron disorder restricted to the lower part of the body. Clinical manifestations include non-progressive muscular atrophy, thigh muscle atrophy, weak thigh adductors, weak knee and foot extensors, minimal jaw muscle and neck flexor weakness, flexion contractures of knees and pes equinovarus. Tendon reflexes are normal. {ECO:0000269|PubMed:20037588, ECO:0000269|PubMed:22526352}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease 2C (CMT2C) [MIM:606071]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. {ECO:0000269|PubMed:20037586, ECO:0000269|PubMed:20037587, ECO:0000269|PubMed:20037588, ECO:0000269|PubMed:21115951, ECO:0000269|PubMed:21288981}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Scapuloperoneal spinal muscular atrophy (SPSMA) [MIM:181405]: A clinically variable neuromuscular disorder characterized by neurogenic scapuloperoneal amyotrophy, laryngeal palsy, congenital absence of muscles, progressive scapuloperoneal atrophy and progressive distal weakness and amyotrophy. {ECO:0000269|PubMed:20037587}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Spondyloepiphyseal dysplasia Maroteaux type (SEDM) [MIM:184095]: A clinically variable spondyloepiphyseal dysplasia with manifestations limited to the musculoskeletal system. Clinical features include short stature, brachydactyly, platyspondyly, short and stubby hands and feet, epiphyseal hypoplasia of the large joints, and iliac hypoplasia. Intelligence is normal. {ECO:0000269|PubMed:20503319}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Parastremmatic dwarfism (PSTD) [MIM:168400]: A bone dysplasia characterized by severe dwarfism, kyphoscoliosis, distortion and bowing of the extremities, and contractures of the large joints. Radiographically, the disease is characterized by a combination of decreased bone density, bowing of the long bones, platyspondyly and striking irregularities of endochondral ossification with areas of calcific stippling and streaking in radiolucent epiphyses, metaphyses and apophyses. {ECO:0000269|PubMed:20503319}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Digital arthropathy-brachydactyly, familial (FDAB) [MIM:606835]: A disorder characterized by irregularities in the proximal articular surfaces of the distal interphalangeal joints of the hand. Individuals appear normal at birth, with no clinical or radiographic evidence of a developmental skeletal dysplasia. The earliest changes appear during the first decade of life. By adulthood, all interphalangeal, metacarpophalangeal, and metatarsophalangeal joints are affected by a deforming, painful osteoarthritis. The remainder of the skeleton is clinically and radiographically unaffected. {ECO:0000269|PubMed:21964574}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in the synoviocytes from patients with (RA) and without (CTR) rheumatoid arthritis (at protein level). {ECO:0000269|PubMed:19759329}.; unclassifiable (Anatomical System);smooth muscle;cartilage;heart;tongue;skin;uterus;pancreas;prostate;whole body;lung;bone;placenta;pituitary gland;head and neck;cervix;kidney;brain; dorsal root ganglion;superior cervical ganglion;pons;skeletal muscle; 0.13281 0.25831 -1.298923801 4.953998585 1111.20028 6.37341 TRPV5 4.66125605838153e-10 0.7975623545661 0.202437644967774 transient receptor potential cation channel subfamily V member 5 FUNCTION: Constitutively active calcium selective cation channel thought to be involved in Ca(2+) reabsorption in kidney and intestine. The channel is activated by low internal calcium level and the current exhibits an inward rectification. A Ca(2+)- dependent feedback regulation includes fast channel inactivation and slow current decay. Heteromeric assembly with TRPV6 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (By similarity). {ECO:0000250, ECO:0000269|PubMed:11549322}.; . TISSUE SPECIFICITY: Expressed at high levels in kidney, small intestine and pancreas, and at lower levels in testis, prostate, placenta, brain, colon and rectum. {ECO:0000269|PubMed:10945469, ECO:0000269|PubMed:11549322}.; unclassifiable (Anatomical System);lung;colon;kidney;stomach; superior cervical ganglion;testis - interstitial;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07422 0.29383 -0.016511957 52.31776362 705.18817 5.27597 TRPV6 0.00141348404170926 0.998282988675209 0.000303527283081482 transient receptor potential cation channel subfamily V member 6 FUNCTION: Calcium selective cation channel probably involved in Ca(2+) uptake in various tissues, including Ca(2+) reabsorption in intestine. The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification. Inactivation includes both, a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin- dependent mechanism, the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (By similarity). {ECO:0000250|UniProtKB:Q91WD2, ECO:0000269|PubMed:11097838, ECO:0000269|PubMed:11248124, ECO:0000269|PubMed:15184369, ECO:0000269|PubMed:23612980}.; . TISSUE SPECIFICITY: Expressed at high levels in the gastrointestinal tract, including esophagus, stomach, duodenum, jejunum, ileum and colon, and in pancreas, placenta, prostate and salivary gland. Expressed at moderate levels in liver, kidney and testis. Expressed in trophoblasts of placenta villus trees (at protein level)(PubMed:23612980). Expressed in locally advanced prostate cancer, metastatic and androgen-insensitive prostatic lesions but not detected in healthy prostate tissue and benign prostatic hyperplasia. {ECO:0000269|PubMed:11097838, ECO:0000269|PubMed:11278579, ECO:0000269|PubMed:23612980}.; unclassifiable (Anatomical System);prostate;pancreas;lung;lacrimal gland;epididymis;placenta;liver;testis;colon;cervix;spleen;brain;mammary gland; subthalamic nucleus;placenta;globus pallidus;ciliary ganglion; 0.05891 . -0.683363435 15.36329323 1884.91912 7.98564 TRQ-CTG1-1 . . . transfer RNA-Gln (CTG) 1-1 . . . . . . . . . . . TRQ-CTG1-2 . . . transfer RNA-Gln (CTG) 1-2 . . . . . . . . . . . TRQ-CTG1-3 . . . transfer RNA-Gln (CTG) 1-3 . . . . . . . . . . . TRQ-CTG1-4 . . . transfer RNA-Gln (CTG) 1-4 . . . . . . . . . . . TRQ-CTG1-5 . . . transfer RNA-Gln (CTG) 1-5 . . . . . . . . . . . TRQ-CTG2-1 . . . transfer RNA-Gln (CTG) 2-1 . . . . . . . . . . . TRQ-CTG3-1 . . . transfer RNA-Gln (CTG) 3-1 . . . . . . . . . . . TRQ-CTG3-2 . . . transfer RNA-Gln (CTG) 3-2 . . . . . . . . . . . TRQ-CTG4-1 . . . transfer RNA-Gln (CTG) 4-1 . . . . . . . . . . . TRQ-CTG4-2 . . . transfer RNA-Gln (CTG) 4-2 . . . . . . . . . . . TRQ-CTG5-1 . . . transfer RNA-Gln (CTG) 5-1 . . . . . . . . . . . TRQ-CTG6-1 . . . transfer RNA-Gln (CTG) 6-1 . . . . . . . . . . . TRQ-CTG7-1 . . . transfer RNA-Gln (CTG) 7-1 . . . . . . . . . . . TRQ-CTG8-1 . . . transfer RNA-Gln (CTG) 8-1 . . . . . . . . . . . TRQ-CTG8-2 . . . transfer RNA-Gln (CTG) 8-2 . . . . . . . . . . . TRQ-CTG9-1 . . . transfer RNA-Gln (CTG) 9-1 . . . . . . . . . . . TRQ-CTG10-1 . . . transfer RNA-Gln (CTG) 10-1 . . . . . . . . . . . TRQ-CTG11-1 . . . transfer RNA-Gln (CTG) 11-1 . . . . . . . . . . . TRQ-CTG12-1 . . . transfer RNA-Gln (CTG) 12-1 . . . . . . . . . . . TRQ-CTG13-1 . . . transfer RNA-Gln (CTG) 13-1 . . . . . . . . . . . TRQ-CTG14-1 . . . transfer RNA-Gln (CTG) 14-1 . . . . . . . . . . . TRQ-CTG15-1 . . . transfer RNA-Gln (CTG) 15-1 . . . . . . . . . . . TRQ-CTG16-1 . . . transfer RNA-Gln (CTG) 16-1 . . . . . . . . . . . TRQ-CTG17-1 . . . transfer RNA-Gln (CTG) 17-1 . . . . . . . . . . . TRQ-CTG18-1 . . . transfer RNA-Gln (CTG) 18-1 . . . . . . . . . . . TRQ-TTG1-1 . . . transfer RNA-Gln (TTG) 1-1 . . . . . . . . . . . TRQ-TTG2-1 . . . transfer RNA-Gln (TTG) 2-1 . . . . . . . . . . . TRQ-TTG3-1 . . . transfer RNA-Gln (TTG) 3-1 . . . . . . . . . . . TRQ-TTG3-2 . . . transfer RNA-Gln (TTG) 3-2 . . . . . . . . . . . TRQ-TTG3-3 . . . transfer RNA-Gln (TTG) 3-3 . . . . . . . . . . . TRQ-TTG4-1 . . . transfer RNA-Gln (TTG) 4-1 . . . . . . . . . . . TRQ-TTG5-1 . . . transfer RNA-Gln (TTG) 5-1 . . . . . . . . . . . TRQ-TTG6-1 . . . transfer RNA-Gln (TTG) 6-1 . . . . . . . . . . . TRQ-TTG7-1 . . . transfer RNA-Gln (TTG) 7-1 . . . . . . . . . . . TRQ-TTG8-1 . . . transfer RNA-Gln (TTG) 8-1 . . . . . . . . . . . TRQ-TTG9-1 . . . transfer RNA-Gln (TTG) 9-1 . . . . . . . . . . . TRQ-TTG10-1 . . . transfer RNA-Gln (TTG) 10-1 . . . . . . . . . . . TRR-ACG1-1 . . . transfer RNA-Arg (ACG) 1-1 . . . . . . . . . . . TRR-ACG1-2 . . . transfer RNA-Arg (ACG) 1-2 . . . . . . . . . . . TRR-ACG1-3 . . . transfer RNA-Arg (ACG) 1-3 . . . . . . . . . . . TRR-ACG2-1 . . . transfer RNA-Arg (ACG) 2-1 . . . . . . . . . . . TRR-ACG2-2 . . . transfer RNA-Arg (ACG) 2-2 . . . . . . . . . . . TRR-ACG2-3 . . . transfer RNA-Arg (ACG) 2-3 . . . . . . . . . . . TRR-ACG2-4 . . . transfer RNA-Arg (ACG) 2-4 . . . . . . . . . . . TRR-CCG1-1 . . . transfer RNA-Arg (CCG) 1-1 . . . . . . . . . . . TRR-CCG1-2 . . . transfer RNA-Arg (CCG) 1-2 . . . . . . . . . . . TRR-CCG1-3 . . . transfer RNA-Arg (CCG) 1-3 . . . . . . . . . . . TRR-CCG2-1 . . . transfer RNA-Arg (CCG) 2-1 . . . . . . . . . . . TRR-CCT1-1 . . . transfer RNA-Arg (CCT) 1-1 . . . . . . . . . . . TRR-CCT2-1 . . . transfer RNA-Arg (CCT) 2-1 . . . . . . . . . . . TRR-CCT3-1 . . . transfer RNA-Arg (CCT) 3-1 . . . . . . . . . . . TRR-CCT4-1 . . . transfer RNA-Arg (CCT) 4-1 . . . . . . . . . . . TRR-CCT5-1 . . . transfer RNA-Arg (CCT) 5-1 . . . . . . . . . . . TRR-CCT6-1 . . . transfer RNA-Arg (CCT) 6-1 . . . . . . . . . . . TRR-CCT6-2 . . . transfer RNA-Arg (CCT) 6-2 . . . . . . . . . . . TRR-CCT7-1 . . . transfer RNA-Arg (CCT) 7-1 . . . . . . . . . . . TRR-CCT8-1 . . . transfer RNA-Arg (CCT) 8-1 . . . . . . . . . . . TRR-CCT9-1 . . . transfer RNA-Arg (CCT) 9-1 . . . . . . . . . . . TRR-TCG1-1 . . . transfer RNA-Arg (TCG) 1-1 . . . . . . . . . . . TRR-TCG2-1 . . . transfer RNA-Arg (TCG) 2-1 . . . . . . . . . . . TRR-TCG3-1 . . . transfer RNA-Arg (TCG) 3-1 . . . . . . . . . . . TRR-TCG4-1 . . . transfer RNA-Arg (TCG) 4-1 . . . . . . . . . . . TRR-TCG5-1 . . . transfer RNA-Arg (TCG) 5-1 . . . . . . . . . . . TRR-TCG6-1 . . . transfer RNA-Arg (TCG) 6-1 . . . . . . . . . . . TRR-TCT1-1 . . . transfer RNA-Arg (TCT) 1-1 . . . . . . . . . . . TRR-TCT2-1 . . . transfer RNA-Arg (TCT) 2-1 . . . . . . . . . . . TRR-TCT3-1 . . . transfer RNA-Arg (TCT) 3-1 . . . . . . . . . . . TRR-TCT3-2 . . . transfer RNA-Arg (TCT) 3-2 . . . . . . . . . . . TRR-TCT4-1 . . . transfer RNA-Arg (TCT) 4-1 . . . . . . . . . . . TRR-TCT5-1 . . . transfer RNA-Arg (TCT) 5-1 . . . . . . . . . . . TRRAP 1 1.4953655719707e-21 1.64755095954838e-53 transformation/transcription domain-associated protein FUNCTION: Adapter protein, which is found in various multiprotein chromatin complexes with histone acetyltransferase activity (HAT), which gives a specific tag for epigenetic transcription activation. Component of the NuA4 histone acetyltransferase complex which is responsible for acetylation of nucleosomal histones H4 and H2A. Plays a central role in MYC transcription activation, and also participates in cell transformation by MYC. Required for p53/TP53-, E2F1- and E2F4-mediated transcription activation. Also involved in transcription activation mediated by the adenovirus E1A, a viral oncoprotein that deregulates transcription of key genes. Probably acts by linking transcription factors such as E1A, MYC or E2F1 to HAT complexes such as STAGA thereby allowing transcription activation. Probably not required in the steps following histone acetylation in processes of transcription activation. May be required for the mitotic checkpoint and normal cell cycle progression. Component of a SWR1- like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. {ECO:0000269|PubMed:11418595, ECO:0000269|PubMed:12138177, ECO:0000269|PubMed:12660246, ECO:0000269|PubMed:12743606, ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:17967892, ECO:0000269|PubMed:24463511, ECO:0000269|PubMed:9708738}.; DISEASE: Note=TRRAP mutation Phe-722 has been frequently found in cutaneous malignant melanoma, suggesting that TRRAP may play a role in the pathogenesis of melanoma. {ECO:0000269|PubMed:21499247}.; . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;thymus; superior cervical ganglion;testis; 0.90101 0.52705 -6.141724508 0.035385704 221.99559 3.22188 TRS-ACT1-1 . . . transfer RNA-Ser (ACT) 1-1 . . . . . . . . . . . TRS-AGA1-1 . . . transfer RNA-Ser (AGA) 1-1 . . . . . . . . . . . TRS-AGA2-1 . . . transfer RNA-Ser (AGA) 2-1 . . . . . . . . . . . TRS-AGA2-2 . . . transfer RNA-Ser (AGA) 2-2 . . . . . . . . . . . TRS-AGA2-3 . . . transfer RNA-Ser (AGA) 2-3 . . . . . . . . . . . TRS-AGA2-4 . . . transfer RNA-Ser (AGA) 2-4 . . . . . . . . . . . TRS-AGA2-5 . . . transfer RNA-Ser (AGA) 2-5 . . . . . . . . . . . TRS-AGA2-6 . . . transfer RNA-Ser (AGA) 2-6 . . . . . . . . . . . TRS-AGA3-1 . . . transfer RNA-Ser (AGA) 3-1 . . . . . . . . . . . TRS-AGA4-1 . . . transfer RNA-Ser (AGA) 4-1 . . . . . . . . . . . TRS-AGA5-1 . . . transfer RNA-Ser (AGA) 5-1 . . . . . . . . . . . TRS-AGA6-1 . . . transfer RNA-Ser (AGA) 6-1 . . . . . . . . . . . TRS-AGA7-1 . . . transfer RNA-Ser (AGA) 7-1 . . . . . . . . . . . TRS-CGA1-1 . . . transfer RNA-Ser (CGA) 1-1 . . . . . . . . . . . TRS-CGA2-1 . . . transfer RNA-Ser (CGA) 2-1 . . . . . . . . . . . TRS-CGA3-1 . . . transfer RNA-Ser (CGA) 3-1 . . . . . . . . . . . TRS-CGA4-1 . . . transfer RNA-Ser (CGA) 4-1 . . . . . . . . . . . TRS-GCT1-1 . . . transfer RNA-Ser (GCT) 1-1 . . . . . . . . . . . TRS-GCT2-1 . . . transfer RNA-Ser (GCT) 2-1 . . . . . . . . . . . TRS-GCT3-1 . . . transfer RNA-Ser (GCT) 3-1 . . . . . . . . . . . TRS-GCT4-1 . . . transfer RNA-Ser (GCT) 4-1 . . . . . . . . . . . TRS-GCT4-2 . . . transfer RNA-Ser (GCT) 4-2 . . . . . . . . . . . TRS-GCT4-3 . . . transfer RNA-Ser (GCT) 4-3 . . . . . . . . . . . TRS-GCT5-1 . . . transfer RNA-Ser (GCT) 5-1 . . . . . . . . . . . TRS-GCT6-1 . . . transfer RNA-Ser (GCT) 6-1 . . . . . . . . . . . TRS-TGA1-1 . . . transfer RNA-Ser (TGA) 1-1 . . . . . . . . . . . TRS-TGA2-1 . . . transfer RNA-Ser (TGA) 2-1 . . . . . . . . . . . TRS-TGA3-1 . . . transfer RNA-Ser (TGA) 3-1 . . . . . . . . . . . TRS-TGA4-1 . . . transfer RNA-Ser (TGA) 4-1 . . . . . . . . . . . TRSUP-CTA1-1 . . . transfer RNA suppressor (CTA) 1-1 . . . . . . . . . . . TRSUP-CTA2-1 . . . transfer RNA suppressor (CTA) 2-1 . . . . . . . . . . . TRSUP-CTA3-1 . . . transfer RNA suppressor (CTA) 3-1 . . . . . . . . . . . TRSUP-TTA1-1 . . . transfer RNA suppressor (TTA) 1-1 . . . . . . . . . . . TRSUP-TTA2-1 . . . transfer RNA suppressor (TTA) 2-1 . . . . . . . . . . . TRSUP-TTA3-1 . . . transfer RNA suppressor (TTA) 3-1 . . . . . . . . . . . TRT-AGT1-1 . . . transfer RNA-Thr (AGT) 1-1 . . . . . . . . . . . TRT-AGT1-2 . . . transfer RNA-Thr (AGT) 1-2 . . . . . . . . . . . TRT-AGT1-3 . . . transfer RNA-Thr (AGT) 1-3 . . . . . . . . . . . TRT-AGT2-1 . . . transfer RNA-Thr (AGT) 2-1 . . . . . . . . . . . TRT-AGT2-2 . . . transfer RNA-Thr (AGT) 2-2 . . . . . . . . . . . TRT-AGT3-1 . . . transfer RNA-Thr (AGT) 3-1 . . . . . . . . . . . TRT-AGT4-1 . . . transfer RNA-Thr (AGT) 4-1 . . . . . . . . . . . TRT-AGT5-1 . . . transfer RNA-Thr (AGT) 5-1 . . . . . . . . . . . TRT-AGT6-1 . . . transfer RNA-Thr (AGT) 6-1 . . . . . . . . . . . TRT-AGT7-1 . . . transfer RNA-Thr (AGT) 7-1 . . . . . . . . . . . TRT-CGT1-1 . . . transfer RNA-Thr (CGT) 1-1 . . . . . . . . . . . TRT-CGT2-1 . . . transfer RNA-Thr (CGT) 2-1 . . . . . . . . . . . TRT-CGT3-1 . . . transfer RNA-Thr (CGT) 3-1 . . . . . . . . . . . TRT-CGT4-1 . . . transfer RNA-Thr (CGT) 4-1 . . . . . . . . . . . TRT-CGT5-1 . . . transfer RNA-Thr (CGT) 5-1 . . . . . . . . . . . TRT-CGT6-1 . . . transfer RNA-Thr (CGT) 6-1 . . . . . . . . . . . TRT-TGT1-1 . . . transfer RNA-Thr (TGT) 1-1 . . . . . . . . . . . TRT-TGT2-1 . . . transfer RNA-Thr (TGT) 2-1 . . . . . . . . . . . TRT-TGT3-1 . . . transfer RNA-Thr (TGT) 3-1 . . . . . . . . . . . TRT-TGT4-1 . . . transfer RNA-Thr (TGT) 4-1 . . . . . . . . . . . TRT-TGT5-1 . . . transfer RNA-Thr (TGT) 5-1 . . . . . . . . . . . TRT-TGT6-1 . . . transfer RNA-Thr (TGT) 6-1 . . . . . . . . . . . TRU-TCA1-1 . . . transfer RNA-SeC (TCA) 1-1 . . . . . . . . . . . TRU-TCA2-1 . . . transfer RNA-SeC (TCA) 2-1 . . . . . . . . . . . TRU-TCA3-1 . . . transfer RNA-SeC (TCA) 3-1 . . . . . . . . . . . TRUB1 0.000523645293941091 0.885601090866897 0.113875263839162 TruB pseudouridine (psi) synthase family member 1 FUNCTION: May be responsible for synthesis of pseudouridine from uracil in transfer RNAs. {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and liver. Expressed at lower levels in lung, small intestine, kidney and spleen. {ECO:0000269|PubMed:12736709}.; medulla oblongata;ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;urinary;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;kidney;thymus; superior cervical ganglion;trigeminal ganglion;skin; 0.14422 0.19995 0.084621747 60.31493277 3037.63728 10.46800 TRUB2 0.00149570183624144 0.876799061942332 0.121705236221427 TruB pseudouridine (psi) synthase family member 2 FUNCTION: May be responsible for synthesis of pseudouridine from uracil in transfer RNAs. {ECO:0000250}.; . . . . 0.08105 0.08804 0.444637294 77.91342298 158.84566 2.75253 TRUND-NNN1-1 . . . transfer RNA-undetermined (NNN) 1-1 . . . . . . . . . . . TRUND-NNN2-1 . . . transfer RNA-undetermined (NNN) 2-1 . . . . . . . . . . . TRUND-NNN3-1 . . . transfer RNA-undetermined (NNN) 3-1 . . . . . . . . . . . TRUND-NNN4-1 . . . transfer RNA-undetermined (NNN) 4-1 . . . . . . . . . . . TRUND-NNN5-1 . . . transfer RNA-undetermined (NNN) 5-1 . . . . . . . . . . . TRUND-NNN6-1 . . . transfer RNA-undetermined (NNN) 6-1 . . . . . . . . . . . TRUND-NNN7-1 . . . transfer RNA-undetermined (NNN) 7-1 . . . . . . . . . . . TRUND-NNN8-1 . . . transfer RNA-undetermined (NNN) 8-1 . . . . . . . . . . . TRUND-NNN9-1 . . . transfer RNA-undetermined (NNN) 9-1 . . . . . . . . . . . TRUND-NNN10-1 . . . transfer RNA-undetermined (NNN) 10-1 . . . . . . . . . . . TRV-AAC1-1 . . . transfer RNA-Val (AAC) 1-1 . . . . . . . . . . . TRV-AAC1-2 . . . transfer RNA-Val (AAC) 1-2 . . . . . . . . . . . TRV-AAC1-3 . . . transfer RNA-Val (AAC) 1-3 . . . . . . . . . . . TRV-AAC1-4 . . . transfer RNA-Val (AAC) 1-4 . . . . . . . . . . . TRV-AAC1-5 . . . transfer RNA-Val (AAC) 1-5 . . . . . . . . . . . TRV-AAC2-1 . . . transfer RNA-Val (AAC) 2-1 . . . . . . . . . . . TRV-AAC3-1 . . . transfer RNA-Val (AAC) 3-1 . . . . . . . . . . . TRV-AAC4-1 . . . transfer RNA-Val (AAC) 4-1 . . . . . . . . . . . TRV-AAC5-1 . . . transfer RNA-Val (AAC) 5-1 . . . . . . . . . . . TRV-AAC6-1 . . . transfer RNA-Val (AAC) 6-1 . . . . . . . . . . . TRV-AAC7-1 . . . transfer RNA-Val (AAC) 7-1 . . . . . . . . . . . TRV-CAC1-1 . . . transfer RNA-Val (CAC) 1-1 . . . . . . . . . . . TRV-CAC1-2 . . . transfer RNA-Val (CAC) 1-2 . . . . . . . . . . . TRV-CAC1-3 . . . transfer RNA-Val (CAC) 1-3 . . . . . . . . . . . TRV-CAC1-4 . . . transfer RNA-Val (CAC) 1-4 . . . . . . . . . . . TRV-CAC1-5 . . . transfer RNA-Val (CAC) 1-5 . . . . . . . . . . . TRV-CAC1-6 . . . transfer RNA-Val (CAC) 1-6 . . . . . . . . . . . TRV-CAC2-1 . . . transfer RNA-Val (CAC) 2-1 . . . . . . . . . . . TRV-CAC3-1 . . . transfer RNA-Val (CAC) 3-1 . . . . . . . . . . . TRV-CAC4-1 . . . transfer RNA-Val (CAC) 4-1 . . . . . . . . . . . TRV-CAC5-1 . . . transfer RNA-Val (CAC) 5-1 . . . . . . . . . . . TRV-CAC6-1 . . . transfer RNA-Val (CAC) 6-1 . . . . . . . . . . . TRV-CAC7-1 . . . transfer RNA-Val (CAC) 7-1 . . . . . . . . . . . TRV-CAC8-1 . . . transfer RNA-Val (CAC) 8-1 . . . . . . . . . . . TRV-CAC9-1 . . . transfer RNA-Val (CAC) 9-1 . . . . . . . . . . . TRV-CAC10-1 . . . transfer RNA-Val (CAC) 10-1 . . . . . . . . . . . TRV-CAC11-1 . . . transfer RNA-Val (CAC) 11-1 . . . . . . . . . . . TRV-CAC11-2 . . . transfer RNA-Val (CAC) 11-2 . . . . . . . . . . . TRV-CAC12-1 . . . transfer RNA-Val (CAC) 12-1 . . . . . . . . . . . TRV-CAC13-1 . . . transfer RNA-Val (CAC) 13-1 . . . . . . . . . . . TRV-CAC14-1 . . . transfer RNA-Val (CAC) 14-1 . . . . . . . . . . . TRV-TAC1-1 . . . transfer RNA-Val (TAC) 1-1 . . . . . . . . . . . TRV-TAC1-2 . . . transfer RNA-Val (TAC) 1-2 . . . . . . . . . . . TRV-TAC2-1 . . . transfer RNA-Val (TAC) 2-1 . . . . . . . . . . . TRV-TAC3-1 . . . transfer RNA-Val (TAC) 3-1 . . . . . . . . . . . TRV-TAC4-1 . . . transfer RNA-Val (TAC) 4-1 . . . . . . . . . . . TRW-CCA1-1 . . . transfer RNA-Trp (CCA) 1-1 . . . . . . . . . . . TRW-CCA2-1 . . . transfer RNA-Trp (CCA) 2-1 . . . . . . . . . . . TRW-CCA3-1 . . . transfer RNA-Trp (CCA) 3-1 . . . . . . . . . . . TRW-CCA3-2 . . . transfer RNA-Trp (CCA) 3-2 . . . . . . . . . . . TRW-CCA3-3 . . . transfer RNA-Trp (CCA) 3-3 . . . . . . . . . . . TRW-CCA4-1 . . . transfer RNA-Trp (CCA) 4-1 . . . . . . . . . . . TRW-CCA5-1 . . . transfer RNA-Trp (CCA) 5-1 . . . . . . . . . . . TRW-CCA6-1 . . . transfer RNA-Trp (CCA) 6-1 . . . . . . . . . . . TRW-CCA7-1 . . . transfer RNA-Trp (CCA) 7-1 . . . . . . . . . . . TRX-CAT1-1 . . . transfer RNA-iMet (CAT) 1-1 . . . . . . . . . . . TRX-CAT1-2 . . . transfer RNA-iMet (CAT) 1-2 . . . . . . . . . . . TRX-CAT1-3 . . . transfer RNA-iMet (CAT) 1-3 . . . . . . . . . . . TRX-CAT1-4 . . . transfer RNA-iMet (CAT) 1-4 . . . . . . . . . . . TRX-CAT1-5 . . . transfer RNA-iMet (CAT) 1-5 . . . . . . . . . . . TRX-CAT1-6 . . . transfer RNA-iMet (CAT) 1-6 . . . . . . . . . . . TRX-CAT1-7 . . . transfer RNA-iMet (CAT) 1-7 . . . . . . . . . . . TRX-CAT1-8 . . . transfer RNA-iMet (CAT) 1-8 . . . . . . . . . . . TRX-CAT2-1 . . . transfer RNA-iMet (CAT) 2-1 . . . . . . . . . . . TRX-CAT3-1 . . . transfer RNA-iMet (CAT) 3-1 . . . . . . . . . . . TRY-ATA1-1 . . . transfer RNA-Tyr (ATA) 1-1 . . . . . . . . . . . TRY-GTA1-1 . . . transfer RNA-Tyr (GTA) 1-1 . . . . . . . . . . . TRY-GTA2-1 . . . transfer RNA-Tyr (GTA) 2-1 . . . . . . . . . . . TRY-GTA3-1 . . . transfer RNA-Tyr (GTA) 3-1 . . . . . . . . . . . TRY-GTA4-1 . . . transfer RNA-Tyr (GTA) 4-1 . . . . . . . . . . . TRY-GTA5-1 . . . transfer RNA-Tyr (GTA) 5-1 . . . . . . . . . . . TRY-GTA5-2 . . . transfer RNA-Tyr (GTA) 5-2 . . . . . . . . . . . TRY-GTA5-3 . . . transfer RNA-Tyr (GTA) 5-3 . . . . . . . . . . . TRY-GTA5-4 . . . transfer RNA-Tyr (GTA) 5-4 . . . . . . . . . . . TRY-GTA5-5 . . . transfer RNA-Tyr (GTA) 5-5 . . . . . . . . . . . TRY-GTA6-1 . . . transfer RNA-Tyr (GTA) 6-1 . . . . . . . . . . . TRY-GTA7-1 . . . transfer RNA-Tyr (GTA) 7-1 . . . . . . . . . . . TRY-GTA8-1 . . . transfer RNA-Tyr (GTA) 8-1 . . . . . . . . . . . TRY-GTA9-1 . . . transfer RNA-Tyr (GTA) 9-1 . . . . . . . . . . . TRY-GTA10-1 . . . transfer RNA-Tyr (GTA) 10-1 . . . . . . . . . . . TRY-GTA11-1 . . . transfer RNA-Tyr (GTA) 11-1 . . . . . . . . . . . TRY-GTA12-1 . . . transfer RNA-Tyr (GTA) 12-1 . . . . . . . . . . . TSACC 0.0697917263737303 0.738398915957194 0.191809357669076 TSSK6 activating co-chaperone FUNCTION: Co-chaperone that facilitates HSP-mediated activation of TSSK6. {ECO:0000269|PubMed:20829357}.; . TISSUE SPECIFICITY: Expressed in testis but is absent from mature sperm. {ECO:0000269|PubMed:20829357}.; . . 0.12825 0.09451 0.635788962 83.63411182 187.16732 2.96963 TSC1 0.999978334212389 2.16657875731271e-05 3.82251207992217e-14 tuberous sclerosis 1 FUNCTION: In complex with TSC2, inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling. Seems not to be required for TSC2 GAP activity towards RHEB. Implicated as a tumor suppressor. Involved in microtubule-mediated protein transport, but this seems to be due to unregulated mTOR signaling. {ECO:0000269|PubMed:12271141, ECO:0000269|PubMed:15340059}.; DISEASE: Tuberous sclerosis 1 (TSC1) [MIM:191100]: An autosomal dominant multi-system disorder that affects especially the brain, kidneys, heart, and skin. It is characterized by hamartomas (benign overgrowths predominantly of a cell or tissue type that occurs normally in the organ) and hamartias (developmental abnormalities of tissue combination). Clinical manifestations include epilepsy, learning difficulties, behavioral problems, and skin lesions. Seizures can be intractable and premature death can occur from a variety of disease-associated causes. {ECO:0000269|PubMed:10227394, ECO:0000269|PubMed:10533069, ECO:0000269|PubMed:10570911, ECO:0000269|PubMed:10874311, ECO:0000269|PubMed:18830229, ECO:0000269|PubMed:22161988, ECO:0000269|PubMed:9328481}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Focal cortical dysplasia of Taylor balloon cell type (FCDBC) [MIM:607341]: Subtype of cortical dysplasias linked to chronic intractable epilepsy. Cortical dysplasias display a broad spectrum of structural changes, which appear to result from changes in proliferation, migration, differentiation, and apoptosis of neuronal precursors and neurons during cortical development. {ECO:0000269|PubMed:12112044}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in skeletal muscle, followed by heart, brain, placenta, pancreas, lung, liver and kidney. Also expressed in embryonic kidney cells.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;bone;thyroid;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;muscle;urinary;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;cerebellum peduncles;atrioventricular node;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.77672 0.42220 -1.03794674 7.832035858 754.82235 5.44924 TSC2 0.999999983432509 1.65674914826493e-08 9.7956102503699e-22 tuberous sclerosis 2 FUNCTION: In complex with TSC1, this tumor suppressor inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling. Acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1. May also play a role in microtubule-mediated protein transport. Also stimulates the intrinsic GTPase activity of the Ras-related proteins RAP1A and RAB5. {ECO:0000269|PubMed:12271141, ECO:0000269|PubMed:15340059, ECO:0000269|PubMed:16707451}.; DISEASE: Tuberous sclerosis 2 (TSC2) [MIM:613254]: An autosomal dominant multi-system disorder that affects especially the brain, kidneys, heart, and skin. It is characterized by hamartomas (benign overgrowths predominantly of a cell or tissue type that occurs normally in the organ) and hamartias (developmental abnormalities of tissue combination). Clinical manifestations include epilepsy, learning difficulties, behavioral problems, and skin lesions. Seizures can be intractable and premature death can occur from a variety of disease-associated causes. {ECO:0000269|PubMed:10069705, ECO:0000269|PubMed:10205261, ECO:0000269|PubMed:10533067, ECO:0000269|PubMed:10570911, ECO:0000269|PubMed:10607950, ECO:0000269|PubMed:10732801, ECO:0000269|PubMed:10735580, ECO:0000269|PubMed:15024740, ECO:0000269|PubMed:15595939, ECO:0000269|PubMed:8824881, ECO:0000269|PubMed:9302281, ECO:0000269|PubMed:9463313, ECO:0000269|PubMed:9829910}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Lymphangioleiomyomatosis (LAM) [MIM:606690]: Progressive and often fatal lung disease characterized by a diffuse proliferation of abnormal smooth muscle cells in the lungs. It affects almost exclusively young women and can occur as an isolated disorder or in association with tuberous sclerosis complex. {ECO:0000269|PubMed:10823953}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Liver, brain, heart, lymphocytes, fibroblasts, biliary epithelium, pancreas, skeletal muscle, kidney, lung and placenta.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach;thymus;cerebellum; thyroid; 0.87806 0.38966 -2.536899611 0.87284737 455.72964 4.43628 TSC22D1 0.941151545615587 0.0588388044895286 9.64989488488247e-06 TSC22 domain family member 1 FUNCTION: Transcriptional repressor. Acts on the C-type natriuretic peptide (CNP) promoter.; . TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;lens;bile duct;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;kidney;mammary gland;stomach;peripheral nerve; whole brain;occipital lobe;superior cervical ganglion;temporal lobe;prefrontal cortex;parietal lobe; 0.54154 0.11317 -1.256630467 5.343241331 405.48147 4.22269 TSC22D1-AS1 . . . TSC22D1 antisense RNA 1 . . . . . . . . . . . TSC22D2 0.831881107448022 0.167970582823103 0.000148309728875596 TSC22 domain family member 2 . . . medulla oblongata;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;thyroid;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney; dorsal root ganglion;medulla oblongata;superior cervical ganglion;placenta;prefrontal cortex;testis;appendix;pons;trigeminal ganglion;cerebellum; 0.48226 0.07818 0.220536484 68.38287332 659.09239 5.14696 TSC22D3 0.771725904530727 0.220450441946058 0.00782365352321516 TSC22 domain family member 3 FUNCTION: Protects T-cells from IL2 deprivation-induced apoptosis through the inhibition of FOXO3A transcriptional activity that leads to the down-regulation of the pro-apoptotic factor BCL2L11. In macrophages, plays a role in the anti-inflammatory and immunosuppressive effects of glucocorticoids and IL10. In T-cells, inhibits anti-CD3-induced NFKB1 nuclear translocation. In vitro, suppresses AP1 and NFKB1 DNA-binding activities (By similarity). Isoform 1 inhibits myogenic differentiation and mediates anti- myogenic effects of glucocorticoids by binding and regulating MYOD1 and HDAC1 transcriptional activity resulting in reduced expression of MYOG (By similarity). {ECO:0000250, ECO:0000269|PubMed:15031210}.; . TISSUE SPECIFICITY: Expressed in brain, lung, spleen and skeletal muscle. Lower levels detected in heart and kidney. Not detected in the pancreas. In non-lymphoid tissues, in the absence of inflammation, the major source of constitutive expression is the macrophage lineage. Also expressed in cells from different hemopoietic cell lineages, including bone marrow cells, CD34+ stem cells, mature B- and T-cells, monocytes and granulocytes. Down- regulated in activated macrophages from inflammatory lesions of delayed-type hypersensitivity (DTH) reactions, such as in tuberculosis and in Crohn disease, whereas in Burkitt lymphoma, persists in macrophages involved in the phagocytosis of apoptotic malignant cells. {ECO:0000269|PubMed:11313722, ECO:0000269|PubMed:12393603}.; ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;pharynx;blood;skeletal muscle;breast;epididymis;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;lacrimal gland;islets of Langerhans;pancreas;lung;pia mater;adrenal gland;placenta;kidney;stomach;aorta;thymus; white blood cells;atrioventricular node; 0.30326 0.21562 -0.207437529 38.2814343 6.82191 0.25281 TSC22D4 0.894817346966523 0.104163974589767 0.00101867844370984 TSC22 domain family member 4 FUNCTION: Transcriptional repressor.; . . medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;ganglion;endometrium;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;muscle;pancreas;lung;nasopharynx;placenta;duodenum;kidney;stomach;aorta;thymus; dorsal root ganglion;amygdala;occipital lobe;thalamus;medulla oblongata;olfactory bulb;cerebellum peduncles;spinal cord;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.30951 . . . 122.14226 2.40674 TSEN2 0.000104861288702718 0.987514431176669 0.0123807075346283 tRNA splicing endonuclease subunit 2 FUNCTION: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. Isoform 1 probably carries the active site for 5'-splice site cleavage. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre- mRNA 3'-end processing factors, establishing a link between pre- tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events. Isoform 2 is responsible for processing a yet unknown RNA substrate. The complex containing isoform 2 is not able to cleave pre-tRNAs properly, although it retains endonucleolytic activity. {ECO:0000269|PubMed:15109492}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are widely expressed at very low level. {ECO:0000269|PubMed:15109492}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;prostate;optic nerve;bone;testis;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;liver;cervix;spleen;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.09274 0.08793 -0.753139731 13.67067705 284.29352 3.60987 TSEN2P1 . . . tRNA splicing endonuclease subunit 2 pseudogene 1 . . . . . . . . . . . TSEN15 0.504749058385151 0.476237314061341 0.0190136275535074 tRNA splicing endonuclease subunit 15 FUNCTION: Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events. {ECO:0000269|PubMed:15109492}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis and uterus. {ECO:0000269|PubMed:11318611}.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;bile duct;breast;lung;adrenal gland;placenta;hippocampus;liver;spleen;cervix;kidney;stomach;aorta; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.15890 0.11205 0.191216164 66.57230479 4212.90999 12.90890 TSEN15P1 . . . tRNA splicing endonuclease subunit 15 pseudogene 1 . . . . . . . . . . . TSEN15P2 . . . tRNA splicing endonuclease subunit 15 pseudogene 2 . . . . . . . . . . . TSEN15P3 . . . tRNA splicing endonuclease subunit 15 pseudogene 3 . . . . . . . . . . . TSEN34 0.396480812083883 0.594190998457656 0.00932818945846128 tRNA splicing endonuclease subunit 34 FUNCTION: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. It probably carries the active site for 3'-splice site cleavage. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'- end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events. {ECO:0000269|PubMed:15109492}.; DISEASE: Pontocerebellar hypoplasia 2C (PCH2C) [MIM:612390]: A disorder characterized by an abnormally small cerebellum and brainstem, and progressive microcephaly from birth combined with extrapyramidal dyskinesia. Severe chorea occurs and epilepsy is frequent. There are no signs of spinal cord anterior horn cells degeneration. {ECO:0000269|PubMed:18711368}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;testis;amniotic fluid;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;blood;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;alveolus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;testis;trigeminal ganglion;whole blood; 0.10809 0.09057 0.082802743 60.09082331 80.22429 1.89371 TSEN54 1.75671632095305e-05 0.878799610643992 0.121182822192799 tRNA splicing endonuclease subunit 54 FUNCTION: Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events. {ECO:0000269|PubMed:15109492}.; DISEASE: Pontocerebellar hypoplasia 4 (PCH4) [MIM:225753]: A disorder characterized by an abnormally small cerebellum and brainstem, severe neonatal encephalopathy, microcephaly, myoclonus and muscular hypertonia. There is a severe inferior olivary and pontine neuronal loss and a diffuse white matter gliosis. {ECO:0000269|PubMed:18711368, ECO:0000269|PubMed:21824568}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pontocerebellar hypoplasia 2A (PCH2A) [MIM:277470]: A disorder characterized by an abnormally small cerebellum and brainstem, and progressive microcephaly from birth combined with extrapyramidal dyskinesia. Severe chorea occurs and epilepsy is frequent. There are no signs of spinal cord anterior horn cells degeneration. {ECO:0000269|PubMed:18711368, ECO:0000269|PubMed:23307886}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pontocerebellar hypoplasia 5 (PCH5) [MIM:610204]: A form of pontocerebellar hypoplasia, a disorder characterized by structural defects of the pons and cerebellum. Brain MRI shows an abnormally small cerebellum and brainstem, decreased cerebral white matter, and a thin corpus callosum. {ECO:0000269|PubMed:21368912}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;muscle;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; . 0.13090 0.10259 1.664578456 96.27860344 7072.81561 18.04186 TSFM 9.80455460336749e-08 0.0942544489749062 0.905745452979548 Ts translation elongation factor, mitochondrial FUNCTION: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. {ECO:0000255|HAMAP-Rule:MF_03135}.; . TISSUE SPECIFICITY: Expressed in all tissues, with the highest levels of expression in skeletal muscle, liver and kidney.; lymphoreticular;ovary;skin;retina;prostate;optic nerve;endometrium;bladder;brain;heart;cartilage;tongue;spinal cord;urinary;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach; amygdala;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.17451 0.19911 -0.025608647 51.91672564 144.83196 2.62103 TSG101 0.982720286760501 0.0172774477060837 2.26553341571377e-06 tumor susceptibility 101 FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association between the ESCRT-0 and ESCRT-I complex. Required for completion of cytokinesis; the function requires CEP55. May be involved in cell growth and differentiation. Acts as a negative growth regulator. Involved in the budding of many viruses through an interaction with viral proteins that contain a late-budding motif P-[ST]-A-P. This interaction is essential for viral particle budding of numerous retroviruses. {ECO:0000269|PubMed:11916981, ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:21070952, ECO:0000269|PubMed:21757351}.; . TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal, kidney and pancreas.; ovary;umbilical cord;foreskin;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;kidney;stomach; testis - interstitial;testis - seminiferous tubule;testis; 0.87193 0.15211 -0.161524709 41.6430762 160.81425 2.76972 TSGA10 0.894352624053566 0.105647361292342 1.46540926834329e-08 testis specific 10 FUNCTION: May play a role in the sperm tail fibrous sheath, a major sperm tail structure. {ECO:0000250}.; . TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:11179690}.; unclassifiable (Anatomical System);uterus;lung;frontal lobe;islets of Langerhans;testis;skin;stomach; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion; 0.45457 . -0.510624372 21.65015334 93.98873 2.08503 TSGA10IP . . . testis specific 10 interacting protein . . . . . 0.11350 . . . . . TSGA13 6.10474450186949e-09 0.0689010104577267 0.931098983437529 testis specific 13 . . TISSUE SPECIFICITY: Testis-specific.; unclassifiable (Anatomical System);medulla oblongata;lung;testis;brain;skeletal muscle; . 0.21179 0.09140 -0.582225231 18.44184949 54.5782 1.47810 TSHB 0.00575808545782517 0.487264813415027 0.506977101127148 thyroid stimulating hormone beta FUNCTION: Indispensable for the control of thyroid structure and metabolism.; . . unclassifiable (Anatomical System);islets of Langerhans;pituitary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;pituitary; 0.62927 0.64928 0.3032669 72.009908 45.61287 1.29747 TSHR 5.80341698067131e-06 0.879485781713159 0.12050841486986 thyroid stimulating hormone receptor FUNCTION: Receptor for thyrothropin. Plays a central role in controlling thyroid cell metabolism. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Also acts as a receptor for thyrostimulin (GPA2+GPB5). {ECO:0000269|PubMed:12045258}.; DISEASE: Note=Defects in TSHR are found in patients affected by hyperthyroidism with different etiologies. Somatic, constitutively activating TSHR mutations and/or constitutively activating G(s)alpha mutations have been identified in toxic thyroid nodules (TTNs) that are the predominant cause of hyperthyroidism in iodine deficient areas. These mutations lead to TSH independent activation of the cAMP cascade resulting in thyroid growth and hormone production. TSHR mutations are found in autonomously functioning thyroid nodules (AFTN), toxic multinodular goiter (TMNG) and hyperfunctioning thyroid adenomas (HTA). TMNG encompasses a spectrum of different clinical entities, ranging from a single hyperfunctioning nodule within an enlarged thyroid, to multiple hyperfunctioning areas scattered throughout the gland. HTA are discrete encapsulated neoplasms characterized by TSH- independent autonomous growth, hypersecretion of thyroid hormones, and TSH suppression. Defects in TSHR are also a cause of thyroid neoplasms (papillary and follicular cancers).; DISEASE: Note=Autoantibodies against TSHR are directly responsible for the pathogenesis and hyperthyroidism of Graves disease. Antibody interaction with TSHR results in an uncontrolled receptor stimulation.; DISEASE: Hypothyroidism, congenital, non-goitrous, 1 (CHNG1) [MIM:275200]: A non-autoimmune condition characterized by resistance to thyroid-stimulating hormone (TSH) leading to increased levels of plasma TSH and low levels of thyroid hormone. It presents variable severity depending on the completeness of the defect. Most patients are euthyroid and asymptomatic, with a normal sized thyroid gland. Only a subset of patients develop hypothyroidism and present a hypoplastic thyroid gland. {ECO:0000269|PubMed:10720030, ECO:0000269|PubMed:11095460, ECO:0000269|PubMed:11442002, ECO:0000269|PubMed:12050212, ECO:0000269|PubMed:14725684, ECO:0000269|PubMed:15531543, ECO:0000269|PubMed:7528344, ECO:0000269|PubMed:8954020, ECO:0000269|PubMed:9100579, ECO:0000269|PubMed:9185526, ECO:0000269|PubMed:9329388}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Familial gestational hyperthyroidism (HTFG) [MIM:603373]: A condition characterized by abnormally high levels of serum thyroid hormones occurring during early pregnancy. {ECO:0000269|PubMed:9854118}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hyperthyroidism, non-autoimmune (HTNA) [MIM:609152]: A condition characterized by abnormally high levels of serum thyroid hormones, thyroid hyperplasia, goiter and lack of anti-thyroid antibodies. Typical features of Graves disease such as exophthalmia, myxedema, antibodies anti-TSH receptor and lymphocytic infiltration of the thyroid gland are absent. {ECO:0000269|PubMed:10199795, ECO:0000269|PubMed:10852462, ECO:0000269|PubMed:11081252, ECO:0000269|PubMed:11127522, ECO:0000269|PubMed:11201847, ECO:0000269|PubMed:11517004, ECO:0000269|PubMed:11549687, ECO:0000269|PubMed:15163335, ECO:0000269|PubMed:7800007, ECO:0000269|PubMed:7920658, ECO:0000269|PubMed:8636266, ECO:0000269|PubMed:8964822, ECO:0000269|PubMed:9349581, ECO:0000269|PubMed:9360555, ECO:0000269|PubMed:9398746, ECO:0000269|PubMed:9589634}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the thyroid. {ECO:0000269|PubMed:2610690}.; unclassifiable (Anatomical System);lung;ovary;thyroid;blood;head and neck;brain;skeletal muscle;bone marrow; superior cervical ganglion;thyroid;globus pallidus;ciliary ganglion;pons;atrioventricular node;fetal thyroid;trigeminal ganglion;skeletal muscle;thymus; 0.19628 0.35681 0.005534202 54.09884407 850.31473 5.69844 TSHRL1 . . . thyroid stimulating hormone receptor like 1 . . . . . . . . . . . TSHRL2 . . . thyroid stimulating hormone receptor like 2 . . . . . . . . . . . TSHRL3 . . . thyroid stimulating hormone receptor like 3 . . . . . . . . . . . TSHZ1 0.939559480233567 0.0603895857978289 5.09339686041966e-05 teashirt zinc finger homeobox 1 FUNCTION: Probable transcriptional regulator involved in developmental processes. May act as a transcriptional repressor (Potential). {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in brain; strongly reduced in post- mortem elderly subjects with Alzheimer disease. {ECO:0000269|PubMed:19343227}.; lymphoreticular;ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cerebral cortex;thyroid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;urinary;lens;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta; . 0.19220 0.13716 -1.291711673 5.007077141 2304.84707 8.89407 TSHZ2 0.406843773399705 0.592790299876505 0.000365926723790251 teashirt zinc finger homeobox 2 FUNCTION: Probable transcriptional regulator involved in developmental processes. May act as a transcriptional repressor (Potential). {ECO:0000305}.; . TISSUE SPECIFICITY: Expressed in brain; strongly reduced in post- mortem elderly subjects with Alzheimer disease. {ECO:0000269|PubMed:19343227}.; unclassifiable (Anatomical System);uterus;heart;endometrium;tongue;larynx;visual apparatus;head and neck;skin;skeletal muscle; . 0.13647 0.11806 -0.916836882 9.831328143 361.35552 4.02303 TSHZ3 0.425645582007279 0.572795462751579 0.00155895524114186 teashirt zinc finger homeobox 3 FUNCTION: Transcriptional regulator involved in developmental processes. Function in association with APBB1, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. TSHZ3-mediated transcription repression involves the recruitment of histone deacetylases HDAC1 and HDAC2. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s). Regulates the development of neurons involved in both respiratory rhythm and airflow control. Promotes maintenance of nucleus ambiguus (nA) motoneurons, which govern upper airway function, and establishes a respiratory rhythm generator (RRG) activity compatible with survival at birth. Involved in the differentiation of the proximal uretic smooth muscle cells during developmental processes. Involved in the up- regulation of myocardin, that directs the expression of smooth muscle cells in the proximal ureter. {ECO:0000269|PubMed:19343227}.; . TISSUE SPECIFICITY: Expressed in brain; strongly reduced in post- mortem elderly subjects with Alzheimer disease. {ECO:0000269|PubMed:18776146, ECO:0000269|PubMed:19343227}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;muscle;parathyroid;skin;skeletal muscle;retina;uterus;pancreas;prostate;lung;placenta;visual apparatus;testis;kidney;spinal ganglion;brain;mammary gland;aorta; uterus;fetal brain; 0.86551 0.12160 -1.719728651 2.488794527 196.3495 3.03078 TSIX . . . TSIX transcript, XIST antisense RNA . . . . . . . . . . . TSKS 0.980813772290248 0.0191856343820997 5.93327652186266e-07 testis specific serine kinase substrate FUNCTION: May play a role in testicular physiology, most probably in the process of spermatogenesis or spermatid development.; . TISSUE SPECIFICITY: Highly expressed in testis. Expressed at low levels in prostate, female breast, placenta, ovary and thymus. {ECO:0000269|PubMed:11444856, ECO:0000269|PubMed:15044604}.; unclassifiable (Anatomical System);medulla oblongata;pancreas;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;pons;skeletal muscle; . . -0.328796968 30.86223166 2447.68714 9.20441 TSKU 0.729712730834786 0.257866279016836 0.0124209901483779 tsukushi, small leucine rich proteoglycan . . . ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;iris;testis;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;blood;skeletal muscle;pancreas;lung;epididymis;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;adipose tissue;thyroid;placenta;liver;kidney; 0.24802 0.40306 0.532823122 80.96249115 549.57166 4.76810 TSLP 0.0447881738846191 0.851408999394046 0.103802826721335 thymic stromal lymphopoietin FUNCTION: Isoform 1: Cytokine that induces the release of T-cell- attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c(+) dendritic cells. Can induce allergic inflammation by directly activating mast cells. {ECO:0000269|PubMed:11418668, ECO:0000269|PubMed:11480573, ECO:0000269|PubMed:17242164}.; . TISSUE SPECIFICITY: Isoform 1 is expressed in a number of tissues including heart, liver and prostate. Isoform 2 is the predominant form in keratinocytes of oral mucosa, skin and in salivary glands. It is secreted into saliva. {ECO:0000269|PubMed:11480573, ECO:0000269|PubMed:24850429}.; unclassifiable (Anatomical System);meninges;pia mater;lung;cartilage;testis;dura mater;brain;skin; superior cervical ganglion;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.14117 0.07053 -0.273576253 33.97027601 3.9088 0.14518 TSN 0.945966337540149 0.0539952587769373 3.84036829140842e-05 translin FUNCTION: DNA-binding protein that specifically recognizes consensus sequences at the breakpoint junctions in chromosomal translocations, mostly involving immunoglobulin (Ig)/T-cell receptor gene segments. Seems to recognize single-stranded DNA ends generated by staggered breaks occurring at recombination hot spots.; . . . . 0.59218 0.21177 -0.075159878 47.78839349 6.36266 0.23848 TSNARE1 3.60235223112282e-07 0.792734250830817 0.20726538893396 t-SNARE domain containing 1 . . . amygdala;testis;skeletal muscle; . 0.13119 0.10131 1.050838371 91.36588818 5557.39016 15.40816 TSNAX 0.972037851150335 0.0279255204601019 3.66283895627968e-05 translin-associated factor X FUNCTION: Acts in combination with TSN as an endonuclease involved in the activation of the RNA-induced silencing complex (RISC). Possible role in spermatogenesis. {ECO:0000269|PubMed:12036294, ECO:0000269|PubMed:21552258}.; . . . . 0.05123 0.14672 0.014844891 54.94810097 18.71119 0.64570 TSNAX-DISC1 . . . TSNAX-DISC1 readthrough (NMD candidate) . . . . . . . . . . . TSNAXIP1 9.27238409136455e-18 0.00436794261152715 0.995632057388473 translin-associated factor X interacting protein 1 FUNCTION: Possible role in spermatogenesis. {ECO:0000250|UniProtKB:Q99P25}.; . . . . 0.13826 0.10692 -0.486758915 22.69992923 232.91761 3.29951 TSPAN1 0.000714382124602965 0.755007896031424 0.244277721843973 tetraspanin 1 . . . . . 0.03427 0.08249 0.082802743 60.09082331 41.7733 1.21738 TSPAN2 0.000100586967317338 0.804850683445572 0.19504872958711 tetraspanin 2 FUNCTION: May play a role in signalling in oligodendrocytes in the early stages of their terminal differentiation into myelin-forming glia and may also function in stabilizing the mature sheath. {ECO:0000250}.; . . . . 0.16613 0.12378 -0.007201372 53.19061099 151.97102 2.69598 TSPAN3 0.284424065158703 0.693664596764758 0.0219113380765389 tetraspanin 3 FUNCTION: Regulates the proliferation and migration of oligodendrocytes, a process essential for normal myelination and repair. {ECO:0000250}.; . . ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;heart;cartilage;pineal body;spinal cord;urinary;adrenal cortex;pharynx;blood;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;larynx;bone;pituitary gland;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;pia mater;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; amygdala;whole brain;thalamus;medulla oblongata;occipital lobe;adipose tissue;hypothalamus;spinal cord;pons;caudate nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.37596 0.11376 -0.05129383 49.75819769 29.08327 0.92970 TSPAN4 2.52434251211869e-06 0.298784746361274 0.701212729296214 tetraspanin 4 . . TISSUE SPECIFICITY: Expressed in multiple tissues but is absent in brain, lymphoid cells, and platelets.; ovary;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;heart;liver;skeletal muscle; 0.10663 . -0.955204708 9.170794999 106.81296 2.24291 TSPAN5 0.927948896697443 0.0719716028988257 7.95004037312917e-05 tetraspanin 5 . . . ovary;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;frontal lobe;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lung;placenta;hippocampus;visual apparatus;liver;spleen;kidney;stomach; . 0.32967 0.12378 -0.317668748 31.45789101 4.49703 0.16290 TSPAN6 0.0282021832612146 0.799027866207708 0.172769950531077 tetraspanin 6 . . . . . 0.07121 0.06917 -0.117432389 44.89266336 396.91909 4.18527 TSPAN7 0.86995013142945 0.128287984414467 0.001761884156083 tetraspanin 7 FUNCTION: May be involved in cell proliferation and cell motility.; . TISSUE SPECIFICITY: Not solely expressed in T-cells. Expressed in acute myelocytic leukemia cells of some patients.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;cochlea;larynx;bone;pituitary gland;testis;spinal ganglion;brain;bladder;pineal gland;tonsil;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;islets of Langerhans;hypothalamus;pineal body;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; whole brain;amygdala;occipital lobe;medulla oblongata;cerebellum peduncles;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.27156 0.17096 -0.075159878 47.78839349 0.88041 0.01802 TSPAN8 0.0086947214274004 0.93510239042661 0.0562028881459894 tetraspanin 8 . . TISSUE SPECIFICITY: Gastric, colon, rectal, and pancreatic carcinomas.; unclassifiable (Anatomical System);smooth muscle;ovary;heart;small intestine;islets of Langerhans;sympathetic chain;colon;skeletal muscle;bile duct;prostate;pancreas;lung;cerebral cortex;nasopharynx;bone;alveolus;liver;testis;cervix;spleen;kidney;mammary gland;bladder;artery;aorta;stomach; dorsal root ganglion;pancreas;superior cervical ganglion;prostate;olfactory bulb;trachea;spinal cord;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.01984 0.04115 0.661468037 84.4420854 4203.85686 12.90024 TSPAN9 0.779777700780573 0.218692761228057 0.0015295379913699 tetraspanin 9 . . TISSUE SPECIFICITY: Expressed in megakaryocytes and platelets (at protein level). {ECO:0000269|PubMed:18795891}.; myocardium;ovary;salivary gland;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;testis;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;cerebellum peduncles;testis;pons;trigeminal ganglion;cingulate cortex;cerebellum; 0.16613 0.12378 -0.648365105 16.35999056 173.34152 2.86573 TSPAN9-IT1 . . . TSPAN9 intronic transcript 1 . . . . . . . . . . . TSPAN10 7.87266607064108e-07 0.0869491285786511 0.913050084154742 tetraspanin 10 . . TISSUE SPECIFICITY: Expressed in the eye, including iris, ciliary body, retinal pigment epithelium, but not lens (protein level). {ECO:0000269|PubMed:12107410}.; uterus;prostate;optic nerve;lymph node;endometrium;visual apparatus;iris;choroid;skin;peripheral nerve;retina; . 0.08169 0.09934 . . . . TSPAN11 2.9598251783614e-05 0.551035576624168 0.448934825124048 tetraspanin 11 . . . bone; . 0.06330 . -0.135838822 43.77211607 168.55378 2.83406 TSPAN12 0.554920625997523 0.442275237604498 0.00280413639797915 tetraspanin 12 FUNCTION: Regulator of cell surface receptor signal transduction. Plays a central role in retinal vascularization by regulating norrin (NDP) signal transduction. Acts in concert with norrin (NDP) to promote FZD4 multimerization and subsequent activation of FZD4, leading to promote accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated transcriptional programs. Suprisingly, it only activate the norrin (NDP)-dependent activation of FZD4, while it does not activate the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1) (By similarity). Acts as a regulator of membrane proteinases such as ADAM10 and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of amyloid precursor protein (APP). Activates MMP14/MT1-MMP-dependent cleavage activity. {ECO:0000250, ECO:0000269|PubMed:19211836, ECO:0000269|PubMed:19587294}.; DISEASE: Vitreoretinopathy, exudative 5 (EVR5) [MIM:613310]: A disorder of the retinal vasculature characterized by an abrupt cessation of growth of peripheral capillaries, leading to an avascular peripheral retina. This may lead to compensatory retinal neovascularization, which is thought to be induced by hypoxia from the initial avascular insult. New vessels are prone to leakage and rupture causing exudates and bleeding, followed by scarring, retinal detachment and blindness. Clinical features can be highly variable, even within the same family. Patients with mild forms of the disease are asymptomatic, and their only disease related abnormality is an arc of avascular retina in the extreme temporal periphery. {ECO:0000269|PubMed:20159111, ECO:0000269|PubMed:20159112, ECO:0000269|PubMed:22427576}. Note=The disease is caused by mutations affecting the gene represented in this entry. TSPAN12 dominant and recessive mutations have been identified in patients with exudative vitreoretinopathy. Patients with mutations in both alleles of TSPAN12 have severe exudative vitreoretinopathy or retinal dysplasia. These mutations appear to result in a milder phenotype in heterozygous mutation carriers (PubMed:22427576). {ECO:0000269|PubMed:22427576}.; . unclassifiable (Anatomical System);ovary;islets of Langerhans;adrenal cortex;colon;parathyroid;lens;skeletal muscle;uterus;prostate;lung;endometrium;trabecular meshwork;thyroid;placenta;visual apparatus;hippocampus;liver;testis;cervix;kidney;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;adrenal gland;cerebellum peduncles;thyroid;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle;cerebellum; 0.49960 0.07897 -0.161524709 41.6430762 29.4953 0.94265 TSPAN13 0.609851374390786 0.388364481785252 0.00178414382396201 tetraspanin 13 . . . ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;bladder;brain;tonsil;heart;cartilage;pineal body;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; trachea; 0.33062 0.10025 -0.141298762 42.87567823 8.3864 0.30657 TSPAN14 0.863069547941605 0.136510941899237 0.000419510159158359 tetraspanin 14 . . . ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;placenta; 0.16100 0.11597 -0.339715008 30.06605331 10.6082 0.38593 TSPAN15 0.00185580828692184 0.902378586839115 0.0957656048739632 tetraspanin 15 . . . . . 0.29157 0.11343 0.350995466 74.37485256 209.06557 3.12140 TSPAN16 0.000252237775125353 0.533132847028256 0.466614915196618 tetraspanin 16 . . TISSUE SPECIFICITY: Broadly expressed in most human tissues and cell lines including neural and bone marrow derived tissues.; medulla oblongata;lung;testis; . 0.04912 0.08574 0.373041938 75.29488087 212.54112 3.14654 TSPAN17 1.31977556559059e-05 0.837491349775985 0.162495452468359 tetraspanin 17 . . . medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;oesophagus;endometrium;synovium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);cartilage;tongue;muscle;adrenal cortex;blood;lens;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;alveolus;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07127 . -0.247889024 35.98726115 62.13277 1.60733 TSPAN18 0.161860431497711 0.82303214846002 0.0151074200422681 tetraspanin 18 . . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;lens;pancreas;lung;adrenal gland;macula lutea;visual apparatus;liver;spleen;head and neck;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05306 0.10198 0.018483465 55.44939844 . . TSPAN19 2.63765238175314e-09 0.0222452736288787 0.977754723733469 tetraspanin 19 . . . . . . . 0.215080721 67.91696155 186.72424 2.96743 TSPAN31 0.32725853041475 0.657044486276473 0.0156969833087764 tetraspanin 31 . . . medulla oblongata;ovary;adrenal medulla;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;pineal body;urinary;spinal cord;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;atrioventricular node;caudate nucleus;pons;skeletal muscle;adrenal gland;thyroid;globus pallidus;ciliary ganglion;kidney;trigeminal ganglion;cingulate cortex;parietal lobe; 0.32829 0.10451 0.169169615 65.33380514 6.87642 0.25564 TSPAN32 0.000537261290250421 0.888754020181182 0.110708718528568 tetraspanin 32 . . TISSUE SPECIFICITY: Expressed ubiquitously at low levels. High levels of expression are confined to hematopoietic tissues including peripheral blood leukocytes, thymus and spleen. {ECO:0000269|PubMed:10072438}.; unclassifiable (Anatomical System);lung;liver;testis;spleen;blood;germinal center; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07365 . 0.376678994 75.50719509 156.95947 2.73665 TSPAN33 0.000103178201876671 0.809300312816425 0.190596508981699 tetraspanin 33 FUNCTION: Plays an important role in normal erythropoiesis. It has a role in the differentiation of erythroid progenitors (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Predominantly expressed in erythroblasts. {ECO:0000269|PubMed:17158226}.; lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lens;bile duct;breast;pancreas;lung;macula lutea;liver;alveolus;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;kidney;trigeminal ganglion; 0.33219 0.11753 -0.361761279 28.6329323 13.58554 0.49330 TSPEAR 1.87288813996797e-10 0.382273866551838 0.617726133260873 thrombospondin-type laminin G domain and EAR repeats FUNCTION: May play a role in development or function of the auditory system.; DISEASE: Deafness, autosomal recessive, 98 (DFNB98) [MIM:614861]: A form of non-syndromic sensorineural hearing loss with prelingual onset. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:22678063}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;lung;heart;skin; . 0.13109 0.12772 -1.076610636 7.324840764 214.12285 3.15847 TSPEAR-AS1 . . . TSPEAR antisense RNA 1 . . . . . . . . . . . TSPEAR-AS2 . . . TSPEAR antisense RNA 2 . . TISSUE SPECIFICITY: Widely expressed. Not expressed in liver and muscle. {ECO:0000269|PubMed:12036297}.; . . 0.10002 . . . . . TSPO 0.021753056615385 0.757791149929071 0.220455793455544 translocator protein . . TISSUE SPECIFICITY: Ubiquitous.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; lung;heart; 0.19975 0.25949 0.725794416 85.98136353 855.18852 5.71000 TSPO2 4.28516292472018e-07 0.0614424748547555 0.938557096628952 translocator protein 2 FUNCTION: Binds cholesterol and mediates its redistribution during erythropoiesis which may play a role in erythrocyte maturation. {ECO:0000269|PubMed:19729679}.; . . . . 0.26476 0.08217 0.701931997 85.34442085 74.4861 1.80465 TSPY1 . . . testis specific protein, Y-linked 1 FUNCTION: May be involved in sperm differentiation and proliferation. {ECO:0000269|PubMed:8923009}.; DISEASE: Note=TSPY is located in the gonadoblastoma critical region and is preferentially expressed in tumor germ cells of gonadoblastoma specimens. Expression also correlates with testicular seminoma and tumorigenesis of the prostate gland. {ECO:0000269|PubMed:10090875, ECO:0000269|PubMed:10773691, ECO:0000269|PubMed:11173850}.; TISSUE SPECIFICITY: Specifically expressed in testicular tissues. Isoform 1 and isoform 2 are expressed in spermatogonia and spermatocytes. Found in early testicular carcinoma in situ, spermatogonial cells in testicular tissues of 46,X,Y female and in prostate cancer cell lines. {ECO:0000269|PubMed:10747295, ECO:0000269|PubMed:8923009}.; . . . . . . . . TSPY2 . . . testis specific protein, Y-linked 2 FUNCTION: Unknown. May be involved in sperm differentiation and proliferation (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);medulla oblongata;testis; . . . . . . . TSPY3 . . . testis specific protein, Y-linked 3 FUNCTION: Unknown. May be involved in sperm differentiation and proliferation (By similarity). {ECO:0000250}.; . . . . . . . . . . TSPY4 . . . testis specific protein, Y-linked 4 FUNCTION: Unknown. May be involved in sperm differentiation and proliferation (By similarity). {ECO:0000250}.; . . . . . . . . . . TSPY5P . . . testis specific protein, Y-linked 5, pseudogene . . . . . . . . . . . TSPY6P . . . testis specific protein, Y-linked 6, pseudogene . . . . . . . . . . . TSPY7P . . . testis specific protein, Y-linked 7, pseudogene . . . . . . . . . . . TSPY8 . . . testis specific protein, Y-linked 8 FUNCTION: May be involved in sperm differentiation and proliferation. {ECO:0000250}.; . . unclassifiable (Anatomical System);testis; . . . . . . . TSPY9P . . . testis specific protein, Y-linked 9, pseudogene . . . . . . . . . . . TSPY10 . . . testis specific protein, Y-linked 10 FUNCTION: Unknown. May be involved in sperm differentiation and proliferation (By similarity). {ECO:0000250}.; . . . . . . . . . . TSPY11P . . . testis specific protein, Y-linked 11, pseudogene . . . . . . . . . . . TSPY12P . . . testis specific protein, Y-linked 12, pseudogene . . . . . . . . . . . TSPY13P . . . testis specific protein, Y-linked 13, pseudogene . . . . . . . . . . . TSPY14P . . . testis specific protein, Y-linked 14, pseudogene . . . . . . . . . . . TSPY15P . . . testis specific protein, Y-linked 15, pseudogene . . . . . . . . . . . TSPY16P . . . testis specific protein, Y-linked 16, pseudogene . . . . . . . . . . . TSPY17P . . . testis specific protein, Y-linked 17, pseudogene . . . . . . . . . . . TSPY18P . . . testis specific protein, Y-linked 18, pseudogene . . . . . . . . . . . TSPY19P . . . testis specific protein, Y-linked 19, pseudogene . . . . . . . . . . . TSPY20P . . . testis specific protein, Y-linked 20, pseudogene . . . . . . . . . . . TSPY21P . . . testis specific protein, Y-linked 21, pseudogene . . . . . . . . . . . TSPY22P . . . testis specific protein, Y-linked 22, pseudogene . . . . . . . . . . . TSPY23P . . . testis specific protein, Y-linked 23, pseudogene . . . . . . . . . . . TSPY24P . . . testis specific protein, Y-linked 24, pseudogene . . . . . . . . . . . TSPY25P . . . testis specific protein, Y-linked 25, pseudogene . . . . . . . . . . . TSPY26P . . . testis specific protein, Y-linked 26, pseudogene . . . . . . . . . . . TSPYL1 0.00799158689730585 0.929494180751712 0.0625142323509823 TSPY-like 1 . . TISSUE SPECIFICITY: Expressed in testis, ovary, liver, spleen, brain, kidney, prostate, lung, liver, and heart. {ECO:0000269|PubMed:9730615}.; . . 0.09682 0.09596 0.775339069 87.13729653 3648.94274 11.73722 TSPYL2 0.874635827562653 0.125031878490285 0.000332293947061913 TSPY-like 2 FUNCTION: Part of the CASK/TBR1/TSPYL2 transcriptional complex which modulates gene expression in response to neuronal synaptic activity, probably by facilitating nucleosome assembly. May inhibit cell proliferation by inducing p53-dependent CDKN1A expression. {ECO:0000269|PubMed:11395479, ECO:0000269|PubMed:17317670}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in brain, testis and heart, and lowest levels in liver and pancreas. {ECO:0000269|PubMed:11149944, ECO:0000269|PubMed:11318608, ECO:0000269|PubMed:12393179, ECO:0000269|PubMed:15241014}.; . . 0.13703 0.27669 -0.712684326 14.49634348 93.79731 2.08252 TSPYL4 0.00261866598258138 0.789146541367135 0.208234792650284 TSPY-like 4 . . . . . 0.24853 . 0.41713504 76.95800896 410.80371 4.24801 TSPYL5 0.852598058180395 0.146891571431377 0.00051037038822853 TSPY-like 5 FUNCTION: Involved in modulation of cell growth and cellular response to gamma radiation probably via regulation of the Akt signaling pathway. Involved in regulation of p53/TP53. Suppresses p53/TP53 protein levels and promotes its ubiquitination; the function is dependent on USP7 and independent on MDM2. Proposed to displace p53/TP53 from interaction with USP7. {ECO:0000269|PubMed:20079711, ECO:0000269|PubMed:21170034}.; . . unclassifiable (Anatomical System);breast;prostate;lung;hippocampus;testis;amniotic fluid;skin; testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;pons;parietal lobe; 0.18124 0.11893 0.084621747 60.31493277 1747.5541 7.71759 TSPYL6 0.581660026360398 0.407715881136773 0.0106240925028293 TSPY-like 6 . . . testis; superior cervical ganglion;subthalamic nucleus;adrenal gland;ciliary ganglion;atrioventricular node; 0.04664 . 1.155610133 92.59259259 1670.83375 7.54514 TSR1 8.33290388723747e-20 0.00374644176945641 0.996253558230544 TSR1, 20S rRNA accumulation, homolog (S. cerevisiae) FUNCTION: Required during maturation of the 40S ribosomal subunit in the nucleolus. {ECO:0000250}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;placenta;macula lutea;visual apparatus;duodenum;liver;cervix;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;testis - interstitial;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.84330 0.13128 0.005534202 54.09884407 2036.30647 8.31329 TSR2 0.760610428612814 0.230486271246961 0.00890330014022511 TSR2, 20S rRNA accumulation, homolog (S. cerevisiae) FUNCTION: May be involved in 20S pre-rRNA processing. {ECO:0000305}.; DISEASE: Diamond-Blackfan anemia 14, with mandibulofacial dysostosis (DBA14) [MIM:300946]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. {ECO:0000269|PubMed:24942156}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.11527 0.10937 0.013025609 54.62962963 8.91746 0.32807 TSR3 0.00240758156123533 0.773697391093275 0.22389502734549 TSR3, 20S rRNA accumulation, homolog (S. cerevisiae) FUNCTION: Probable pre-rRNA processing protein involved in ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_03146}.; . . . . 0.13346 0.10921 -0.025608647 51.91672564 54.96245 1.48528 TSSC1 0.121031637073714 0.8736026890203 0.00536567390598674 tumor suppressing subtransferable candidate 1 . . . . . 0.18075 0.11199 -0.957024976 9.088228356 27.88963 0.89572 TSSC1-IT1 . . . TSSC1 intronic transcript 1 . . . . . . . . . . . TSSC2 . . . tumor suppressing subtransferable candidate 2 pseudogene . . . . . . . . . . . TSSC4 0.0132781892109177 0.66313657360694 0.323585237182142 tumor suppressing subtransferable candidate 4 . . TISSUE SPECIFICITY: Expressed in fetal brain, lung, liver and kidney. Widely expressed in adult tissues. {ECO:0000269|PubMed:10072438}.; lymphoreticular;medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; testis;trigeminal ganglion;skeletal muscle; 0.12572 0.10329 1.021500656 91.01792876 425.9105 4.31226 TSSK1A . . . testis specific serine kinase 1A, pseudogene . . . . . . . . . . . TSSK1B 0.000465467839899368 0.666287591604176 0.333246940555924 testis specific serine kinase 1B FUNCTION: Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates 'Ser-288' of TSKS. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body. {ECO:0000269|PubMed:15733851, ECO:0000269|PubMed:19530700}.; . TISSUE SPECIFICITY: Testis-specific. Present in sperm (at protein level). {ECO:0000269|PubMed:15044604, ECO:0000269|PubMed:20729278}.; . . 0.13083 . -0.464712395 23.5727766 198.63428 3.04597 TSSK2 0.0041565292806896 0.656830708838237 0.339012761881074 testis specific serine kinase 2 FUNCTION: Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates TSKS at 'Ser-288' and SPAG16. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body. {ECO:0000269|PubMed:15044604, ECO:0000269|PubMed:18533145, ECO:0000269|PubMed:20729278}.; . TISSUE SPECIFICITY: Testis-specific. Present in mature spermatozoa (at protein level). {ECO:0000269|PubMed:15044604, ECO:0000269|PubMed:18533145, ECO:0000269|PubMed:20729278}.; . . 0.21399 0.10708 -0.398573136 26.92852088 2038.24483 8.32083 TSSK3 0.763235263396559 0.228124839216473 0.00863989738696789 testis specific serine kinase 3 FUNCTION: May be involved in a signaling pathway during male germ cell development or mature sperm function.; . . . . 0.19431 0.10863 -0.26993514 34.59542345 140.16181 2.58303 TSSK4 2.51468703195602e-11 0.010301110081636 0.989698889893217 testis specific serine kinase 4 FUNCTION: May be involved in a signaling pathway during male germ cell development or mature sperm function (By similarity). Phosphorylates CREB1 on Ser-133 and stimulates downstream signaling. {ECO:0000250, ECO:0000269|PubMed:15964553}.; . TISSUE SPECIFICITY: Expressed only in the testis. {ECO:0000269|PubMed:15964553}.; unclassifiable (Anatomical System);medulla oblongata;testis;bladder;retina; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node; 0.21783 0.09287 0.439181676 77.69521113 681.78058 5.22021 TSSK5P . . . testis specific serine kinase 5, pseudogene . . . . . . . . . . . TSSK6 0.587550746537451 0.402312585837235 0.010136667625314 testis specific serine kinase 6 FUNCTION: Required for sperm production and function. Plays a role in DNA condensation during postmeiotic chromatin remodeling (By similarity). {ECO:0000250|UniProtKB:Q925K9, ECO:0000269|PubMed:15870294}.; . TISSUE SPECIFICITY: Highly expressed in testis. Expressed at lower levels in colon, small intestine, ovary, prostate, thymus, spleen and peripheral blood leukocytes. {ECO:0000269|PubMed:15870294}.; unclassifiable (Anatomical System);medulla oblongata;lung;ovary;endometrium;islets of Langerhans;testis;blood;kidney; subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;pons;caudate nucleus;trigeminal ganglion;skeletal muscle; 0.09523 . -0.295622497 32.61972163 36.5839 1.09738 TST 0.000731843487954778 0.522832993667404 0.476435162844642 thiosulfate sulfurtransferase FUNCTION: Formation of iron-sulfur complexes, cyanide detoxification or modification of sulfur-containing enzymes. Other thiol compounds, besides cyanide, can act as sulfur ion acceptors. Also has weak mercaptopyruvate sulfurtransferase (MST) activity (By similarity). Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA. {ECO:0000250, ECO:0000269|PubMed:20663881, ECO:0000269|PubMed:21685364}.; . . ovary;foreskin;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;iris;testis;germinal center;brain;unclassifiable (Anatomical System);hypothalamus;urinary;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;alveolus;spleen;kidney;stomach;peripheral nerve; fetal liver;lung;heart;adrenal gland;liver;kidney; 0.05741 0.35504 0.130533008 63.35810333 287.5119 3.63185 TSTA3 0.0049919240345017 0.967592433823643 0.027415642141855 tissue specific transplantation antigen P35B FUNCTION: Catalyzes the two-step NADP-dependent conversion of GDP- 4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction. {ECO:0000269|PubMed:8910301}.; . . . . 0.10839 0.15887 -1.089312628 7.047652748 39.26906 1.16219 TSTD1 . . . thiosulfate sulfurtransferase (rhodanese)-like domain containing 1 FUNCTION: Possible role in tumorigenesis.; . TISSUE SPECIFICITY: Highly expressed in kidney, liver and skeletal muscle. Lower levels of expression in heart, colon, thymus, spleen, placenta and lung. Weakly expressed in brain, small intestine and peripheral blood leukocytes. Expressed at high levels in the breast carcinoma cell lines MCF-7 and MDA-MB-468 and at a lower level in the breast carcinoma cell line MDA-MB-231, the colon carcinoma call line LoVo and the lung carcinoma cell line A- 549. No expression in the cell lines EFO-27 and HeLa, or the normal breast tissue cell lines MCF-10A and H184A1. Detected in invasive ductal carcinoma, but not in the adjacent tissues. {ECO:0000269|PubMed:12817473}.; unclassifiable (Anatomical System);lymph node;ovary;blood;parathyroid;lens;breast;lung;endometrium;placenta;hypopharynx;liver;head and neck;spleen;brain; . . . 0.301449681 71.80938901 35.04212 1.06378 TSTD2 1.6294589433286e-06 0.857831705300057 0.142166665241 thiosulfate sulfurtransferase (rhodanese)-like domain containing 2 . . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09632 0.07871 0.576916344 82.25406936 954.06636 5.97773 TSTD3 . . . thiosulfate sulfurtransferase (rhodanese)-like domain containing 3 . . . . . . . . . . . TTBK1 0.9973069629351 0.0026930360834392 9.81461172643729e-10 tau tubulin kinase 1 FUNCTION: Serine/threonine kinase which is able to phosphorylate TAU on serine, threonine and tyrosine residues. Induces aggregation of TAU. {ECO:0000269|PubMed:16923168}.; . TISSUE SPECIFICITY: Expressed in the brain, particularly in cortical and hippocampal neurons. Weakly expressed in spinal cord and testis. No expression in adipose tissue, bladder, cervix, colon, esophagus, heart, kidney, liver, lung, ovary, placenta, prostate, skeletal muscle, small intestine, spleen, testis, thymus, thyroid or trachea. {ECO:0000269|PubMed:16923168}.; unclassifiable (Anatomical System);lung;spleen;lens;brain;cerebellum; dorsal root ganglion;superior cervical ganglion;temporal lobe;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.26651 0.11543 -0.459259448 23.69072895 6694.9523 17.33817 TTBK2 0.996929374509573 0.00307062521689711 2.7353027404438e-10 tau tubulin kinase 2 FUNCTION: Serine/threonine kinase that acts as a key regulator of ciliogenesis: controls the initiation of ciliogenesis by binding to the distal end of the basal body and promoting the removal of CCP110, which caps the mother centriole, leading to the recruitment of IFT proteins, which build the ciliary axoneme. Has some substrate preference for proteins that are already phosphorylated on a Tyr residue at the +2 position relative to the phosphorylation site. Able to phosphorylate tau on serines in vitro. {ECO:0000269|PubMed:21548880, ECO:0000269|PubMed:23141541}.; DISEASE: Spinocerebellar ataxia 11 (SCA11) [MIM:604432]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA11 is an autosomal dominant cerebellar ataxia (ADCA). It is a relatively benign, late-onset, slowly progressive neurologic disorder. {ECO:0000269|PubMed:18037885}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;cartilage;hypothalamus;skin;skeletal muscle;uterus;lung;placenta;thyroid;testis;cervix;stomach; superior cervical ganglion;testis - interstitial;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex; 0.35401 0.08438 -0.655870776 16.12408587 766.60671 5.48521 TTC1 0.00185167699732794 0.902138131164292 0.09601019183838 tetratricopeptide repeat domain 1 . . . myocardium;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;muscle;bile duct;pia mater;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;thymus; whole brain;amygdala;occipital lobe;thalamus;medulla oblongata;hypothalamus;prefrontal cortex;cingulate cortex;parietal lobe; 0.18332 0.13684 0.128714042 63.19886766 73.13738 1.78652 TTC3 5.39422630787731e-20 0.999708411976551 0.00029158802344859 tetratricopeptide repeat domain 3 FUNCTION: E3 ubiquitin-protein ligase that mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, AKT2 and AKT3) in the nucleus. Acts as a terminal regulator of Akt signaling after activation; its phosphorylation by Akt, which is a prerequisite for ubiquitin ligase activity, suggests the existence of a regulation mechanism required to control Akt levels after activation. Catalyzes the formation of 'Lys-48'- polyubiquitin chains. May play a role in neuronal differentiation inhibition via its interaction with CIT. {ECO:0000269|PubMed:17488780, ECO:0000269|PubMed:20059950}.; . TISSUE SPECIFICITY: Found in all tissues examined.; ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;amygdala;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;developmental;intestine;colon;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; amygdala;superior cervical ganglion;testis - interstitial;occipital lobe;medulla oblongata;thalamus;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;pituitary; 0.33574 0.08857 -0.972178525 8.911299835 2405.24665 9.10751 TTC3-AS1 . . . TTC3 antisense RNA 1 . . . . . . . . . . . TTC3P1 . . . tetratricopeptide repeat domain 3 pseudogene 1 . . . . . . 0.08857 . . . . TTC4 0.0439675923529379 0.950328169378633 0.00570423826842948 tetratricopeptide repeat domain 4 . . . . . . . 0.440999548 77.79547063 198.85344 3.04732 TTC4P1 . . . tetratricopeptide repeat domain 4 pseudogene 1 . . . . . . . . . . . TTC5 0.00249362475890097 0.994257365150795 0.00324901009030416 tetratricopeptide repeat domain 5 FUNCTION: Adapter protein involved in p53/TP53 response that acts by regulating and mediating the assembly of multi-protein complexes. Required to facilitate the interaction between JMY and p300/EP300 and increase p53/TP53-dependent transcription and apoptosis. Prevents p53/TP53 degradation by MDM2 (By similarity). {ECO:0000250}.; . . medulla oblongata;smooth muscle;ovary;parathyroid;skin;prostate;endometrium;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;spinal cord;pharynx;blood;skeletal muscle;pancreas;lung;nasopharynx;placenta;hippocampus;liver;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis;globus pallidus;ciliary ganglion;atrioventricular node;skeletal muscle; 0.20600 0.14631 0.174625237 65.9648502 274.36635 3.54861 TTC6 8.74475121291033e-09 0.283902582197625 0.716097409057624 tetratricopeptide repeat domain 6 . . . unclassifiable (Anatomical System);uterus;lung;testis; globus pallidus;ciliary ganglion;trigeminal ganglion; 0.06305 0.08734 . . 3948.4689 12.42494 TTC7A 1.95620464496503e-09 0.959500730810341 0.0404992672334539 tetratricopeptide repeat domain 7A FUNCTION: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane (PubMed:23229899, PubMed:24417819). The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis (Probable). In the complex, plays a central role in bridging PI4KA to EFR3B and FAM126A, via direct interactions (By similarity). {ECO:0000250|UniProtKB:Q86TV6, ECO:0000269|PubMed:23229899, ECO:0000269|PubMed:24417819}.; . TISSUE SPECIFICITY: Expressed in epithelial cells of the intestine, thymus, and pancreas (at protein level). {ECO:0000269|PubMed:25546680}.; smooth muscle;ovary;colon;skin;bone marrow;retina;uterus;prostate;frontal lobe;endometrium;oesophagus;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;skeletal muscle;breast;lung;adrenal gland;placenta;visual apparatus;alveolus;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; testis;ciliary ganglion;atrioventricular node; 0.16616 0.10012 0.01281205 54.18141071 1603.71487 7.40607 TTC7B 0.999902561387641 9.74386108701775e-05 1.48897247176038e-12 tetratricopeptide repeat domain 7B FUNCTION: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. In the complex, plays a central role in bridging PI4KA to EFR3B and FAM126A, via direct interactions (PubMed:26571211). {ECO:0000269|PubMed:23229899, ECO:0000269|PubMed:26571211}.; . . ovary;sympathetic chain;parathyroid;fovea centralis;skin;uterus;prostate;cochlea;oesophagus;endometrium;larynx;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;skeletal muscle;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;whole brain;superior cervical ganglion;occipital lobe;subthalamic nucleus;cerebellum peduncles;placenta;globus pallidus;pons;trigeminal ganglion;cingulate cortex;cerebellum; 0.29695 . -1.572589134 3.161122906 47.5586 1.33958 TTC8 0.345392611801702 0.654488171728001 0.000119216470296721 tetratricopeptide repeat domain 8 FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization. {ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986}.; DISEASE: Bardet-Biedl syndrome 8 (BBS8) [MIM:615985]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:14520415, ECO:0000269|PubMed:16308660}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;iris;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;macula lutea;liver;spleen;cervix;kidney;stomach;aorta; superior cervical ganglion; 0.21189 0.20095 0.330767508 73.53739089 111.91763 2.30325 TTC9 0.0585566584919598 0.867504597904368 0.0739387436036721 tetratricopeptide repeat domain 9 . . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;breast;pancreas;lung;placenta;macula lutea;kidney;stomach; amygdala;superior cervical ganglion;fetal brain;prefrontal cortex;pons;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.08179 0.10195 . . 649.34132 5.11223 TTC9B 0.0271797942742283 0.793627606684713 0.179192599041059 tetratricopeptide repeat domain 9B . . . unclassifiable (Anatomical System);hypothalamus;colon;fovea centralis;choroid;lens;retina;optic nerve;lung;frontal lobe;bone;hippocampus;macula lutea;testis;brain; . 0.15836 . . . 7.13869 0.26719 TTC9C 0.000139734935043785 0.646817863870181 0.353042401194775 tetratricopeptide repeat domain 9C . . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;alveolus;cervix;spleen;kidney;mammary gland;stomach; . 0.11035 . -0.317668748 31.45789101 326.17775 3.83967 TTC12 1.44726952967987e-07 0.989096704824955 0.0109031504480926 tetratricopeptide repeat domain 12 . . . unclassifiable (Anatomical System);medulla oblongata;ovary;islets of Langerhans;colon;prostate;lung;cerebral cortex;nasopharynx;thyroid;placenta;visual apparatus;iris;pituitary gland;liver;testis;head and neck;germinal center;kidney;brain;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion;skeletal muscle; 0.04613 0.09693 -0.152426933 42.25053079 147.07121 2.64179 TTC13 0.67322418180806 0.326775748422156 6.97697830193015e-08 tetratricopeptide repeat domain 13 . . . . . 0.24868 . -0.868835007 10.65109696 1582.8162 7.35988 TTC14 4.41871480046018e-06 0.955823688280847 0.0441718930043529 tetratricopeptide repeat domain 14 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;hypothalamus;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;prefrontal cortex;ciliary ganglion;atrioventricular node; 0.10216 0.10430 -0.020150552 52.25288983 125.31545 2.43621 TTC16 5.08132918779213e-12 0.551365808960104 0.448634191034815 tetratricopeptide repeat domain 16 . . . unclassifiable (Anatomical System);frontal lobe;ovary;testis; . 0.17543 . 0.652163325 84.17669262 1886.6115 7.98704 TTC17 0.999727593898895 0.000272406100954535 1.50949821556796e-13 tetratricopeptide repeat domain 17 FUNCTION: Plays a role in primary ciliogenesis by modulating actin polymerization. {ECO:0000269|PubMed:24475127}.; . TISSUE SPECIFICITY: Expressed in germ cells as well as in somatic cells of the testis (at protein level). {ECO:0000269|PubMed:24475127}.; umbilical cord;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;macula lutea;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.42508 0.08952 -1.614880551 2.948808681 1011.16107 6.12260 TTC19 1.05029523664488e-10 0.0454225972110995 0.954577402683871 tetratricopeptide repeat domain 19 FUNCTION: Mitochondrial protein required for formation of the mitochondrial complex III (PubMed:21278747). May also be required for the abcission step in cytokinesis, possibly regulating the ESCRT-III complex via its interaction with CHMP4B (PubMed:20208530). However, the involvement in cytokinesis requires additional experimental evidence. {ECO:0000269|PubMed:20208530, ECO:0000269|PubMed:21278747}.; DISEASE: Mitochondrial complex III deficiency, nuclear 2 (MC3DN2) [MIM:615157]: A disorder of the mitochondrial respiratory chain resulting in a highly variable phenotype depending on which tissues are affected. Clinical features include mitochondrial encephalopathy, psychomotor retardation, ataxia, severe failure to thrive, liver dysfunction, renal tubulopathy, muscle weakness and exercise intolerance. {ECO:0000269|PubMed:21278747}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;gum;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;aorta;cerebellum; amygdala;dorsal root ganglion;subthalamic nucleus;occipital lobe;medulla oblongata;hypothalamus;prefrontal cortex;globus pallidus;caudate nucleus;parietal lobe;cingulate cortex; 0.25473 0.07863 . . 601.39844 4.96349 TTC21A 2.120275914728e-16 0.772223306613905 0.227776693386095 tetratricopeptide repeat domain 21A . . TISSUE SPECIFICITY: Strongly expressed in testis. {ECO:0000269|PubMed:12543795}.; unclassifiable (Anatomical System);medulla oblongata;lung;islets of Langerhans;thyroid;liver;testis;colon;substantia nigra;spleen;brain;skeletal muscle; . 0.12049 0.09851 0.683343061 84.94928049 8323.31002 19.75354 TTC21B 3.38768007245796e-22 0.0988871463802781 0.901112853619722 tetratricopeptide repeat domain 21B FUNCTION: Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport. Negatively modulates the SHH signal transduction (By similarity). {ECO:0000250}.; DISEASE: Note=Ciliary dysfunction leads to a broad spectrum of disorders, collectively termed ciliopathies. Overlapping clinical features include retinal degeneration, renal cystic disease, skeletal abnormalities, fibrosis of various organ, and a complex range of anatomical and functional defects of the central and peripheral nervous system. The ciliopathy range of diseases includes Meckel-Gruber syndrome, Bardet-Biedl syndrome, Joubert syndrome, nephronophtisis, Senior-Loken syndrome, and Jeune asphyxiating thoracic dystrophy among others. TTC21B is causally associated with diverse ciliopathies, and also acts as a modifier gene across the ciliopathy spectrum. TTC21B mutations interact in trans with mutations in other ciliopathy-causing genes and contribute to disease manifestation and severity.; DISEASE: Nephronophthisis 12 (NPHP12) [MIM:613820]: An autosomal recessive disorder resulting in end-stage renal disease. It is a progressive tubulo-interstitial kidney disorder histologically characterized by modifications of the tubules with thickening of the basement membrane, interstitial fibrosis and, in the advanced stages, medullary cysts. Some patients manifest extra-renal features including retinal, skeletal and central nervous system defects. {ECO:0000269|PubMed:21258341}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Short-rib thoracic dysplasia 4 with or without polydactyly (SRTD4) [MIM:613819]: A form of short-rib thoracic dysplasia, a group of autosomal recessive ciliopathies that are characterized by a constricted thoracic cage, short ribs, shortened tubular bones, and a 'trident' appearance of the acetabular roof. Polydactyly is variably present. Non-skeletal involvement can include cleft lip/palate as well as anomalies of major organs such as the brain, eye, heart, kidneys, liver, pancreas, intestines, and genitalia. Some forms of the disease are lethal in the neonatal period due to respiratory insufficiency secondary to a severely restricted thoracic cage, whereas others are compatible with life. Disease spectrum encompasses Ellis-van Creveld syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-Saldino syndrome, and short rib-polydactyly syndrome. {ECO:0000269|PubMed:21258341}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Bardet-Biedl syndrome (BBS) [MIM:209900]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:21258341}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Joubert syndrome 11 (JBTS11) [MIM:613820]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. {ECO:0000269|PubMed:21258341, ECO:0000269|PubMed:22425360}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . myocardium;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;pituitary gland;dura mater;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);meninges;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;pia mater;lung;placenta;macula lutea;liver;head and neck;cervix;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.13531 0.09894 0.619029743 83.25666431 820.66154 5.62646 TTC21B-AS1 . . . TTC21B antisense RNA 1 . . . . . . . . . . . TTC22 0.000878027240110101 0.793848356481434 0.205273616278456 tetratricopeptide repeat domain 22 . . . . . 0.19944 0.10832 . . 3789.96671 12.07106 TTC23 4.35102174486449e-16 0.00159082161376269 0.998409178386237 tetratricopeptide repeat domain 23 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;spinal cord;colon;skin;skeletal muscle;uterus;breast;pancreas;prostate;lung;cerebral cortex;larynx;bone;thyroid;testis;head and neck;kidney;brain; superior cervical ganglion; 0.09763 . -0.222203495 37.54423213 207.68512 3.11230 TTC23L 2.21738028334575e-09 0.136542696560627 0.863457301221993 tetratricopeptide repeat domain 23 like . . . . . . . 1.728918179 96.55579146 718.83275 5.32261 TTC24 6.58039647151808e-05 0.723355768981332 0.276578427053953 tetratricopeptide repeat domain 24 . . . tonsil; . 0.12900 . 0.841481379 88.35810333 4269.00298 12.99213 TTC25 . . . tetratricopeptide repeat domain 25 . . . . . 0.07158 . . . . . TTC26 0.00767000315281739 0.992199674968212 0.000130321878970132 tetratricopeptide repeat domain 26 FUNCTION: Component of the intraflagellar transport (IFT) complex B required for transport of proteins in the motile cilium. Required for transport of specific ciliary cargo proteins related to motility, while it is neither required for IFT complex B assembly or motion nor for cilium assembly. Required for efficient coupling between the accumulation of GLI3 at the ciliary tip and its dissociation from SUFU. {ECO:0000250|UniProtKB:Q8BS45}.; . . unclassifiable (Anatomical System);heart;colon;skin;skeletal muscle;bone marrow;uterus;whole body;lung;endometrium;nasopharynx;bone;thyroid;placenta;visual apparatus;liver;testis;germinal center;brain;bladder; superior cervical ganglion;testis - seminiferous tubule;testis;pons; 0.14931 0.10488 -0.069700724 48.54328851 51.61598 1.41767 TTC27 6.54258241947822e-09 0.992236069935911 0.00776392352150704 tetratricopeptide repeat domain 27 . . . medulla oblongata;ovary;salivary gland;intestine;colon;skin;bone marrow;prostate;whole body;cochlea;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;muscle;pharynx;blood;skeletal muscle;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;trigeminal ganglion; 0.07302 0.22600 -0.304932527 32.24817174 2573.15326 9.48507 TTC28 . . . tetratricopeptide repeat domain 28 FUNCTION: During mitosis, may be involved in the condensation of spindle midzone microtubules, leading to the formation of midbody. {ECO:0000269|PubMed:23036704}.; . TISSUE SPECIFICITY: Widely expressed in fetal tissues. In adult tissues, expressed in testis and ovary and, at much lower levels, in kidney and pancreas. {ECO:0000269|PubMed:23036704}.; . . 0.43375 0.10781 0.894680455 89.3017221 778.53413 5.52148 TTC28-AS1 . . . TTC28 antisense RNA 1 . . . . . . . . . . . TTC29 1.57133321621439e-06 0.638892944340004 0.36110548432678 tetratricopeptide repeat domain 29 . . . unclassifiable (Anatomical System);lung;endometrium;testis; testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node; 0.05702 0.07919 1.197888504 92.95234725 5211.42104 14.87185 TTC30A 1.362196147394e-05 0.624504628571351 0.375481749467175 tetratricopeptide repeat domain 30A FUNCTION: Required for polyglutamylation of axonemal tubulin. Plays a role in anterograde intraflagellar transport (IFT), the process by which cilia precursors are transported from the base of the cilium to the site of their incorporation at the tip. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;whole body;colon;brain;bone marrow; superior cervical ganglion;trigeminal ganglion; . . 0.312359769 72.71172446 831.11207 5.64842 TTC30B 0.00186185059553787 0.90272843060492 0.0954097187995417 tetratricopeptide repeat domain 30B FUNCTION: Required for polyglutamylation of axonemal tubulin. Plays a role in anterograde intraflagellar transport (IFT), the process by which cilia precursors are transported from the base of the cilium to the site of their incorporation at the tip. {ECO:0000250}.; . . . . . . 0.731244617 86.21137061 181.06808 2.92499 TTC31 2.61841974324849e-15 0.0169072037503352 0.983092796249662 tetratricopeptide repeat domain 31 . . . smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;iris;testis;amniotic fluid;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;hypothalamus;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach; white blood cells;cerebellum; 0.08048 . 1.26767467 93.60108516 257.6666 3.45265 TTC32 0.0898978964968043 0.764823360002224 0.145278743500971 tetratricopeptide repeat domain 32 . . . ovary;salivary gland;colon;parathyroid;fovea centralis;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;nasopharynx;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach; white blood cells;atrioventricular node;skeletal muscle; 0.03782 0.05686 -0.117432389 44.89266336 159.7321 2.75965 TTC33 0.0226185448110003 0.911281537791989 0.0660999173970112 tetratricopeptide repeat domain 33 . . . ovary;salivary gland;sympathetic chain;intestine;colon;skin;uterus;prostate;whole body;frontal lobe;cochlea;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;spinal cord;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach; . 0.17550 0.10455 0.148941568 64.31941496 76.14553 1.82861 TTC34 . . . tetratricopeptide repeat domain 34 . . . . . . . . . 228.66231 3.26688 TTC36 0.507038897896992 0.474261024200313 0.0187000779026944 tetratricopeptide repeat domain 36 . . . iris;kidney;retina; . 0.18326 0.10849 . . 77.06758 1.84352 TTC37 7.99341870810084e-20 0.980894720699824 0.0191052793001758 tetratricopeptide repeat domain 37 FUNCTION: Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C).; . TISSUE SPECIFICITY: Widely expressed with the highest levels observed in vascular tissues, lymph node, pituitary, lung and intestine. Not expressed in the liver. {ECO:0000269|PubMed:21120949}.; lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;urinary;pharynx;blood;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;colon;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;islets of Langerhans;oral cavity;bile duct;pancreas;pia mater;lung;mesenchyma;nasopharynx;placenta;amnion;head and neck;kidney;stomach;aorta; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;prefrontal cortex;atrioventricular node; 0.35178 0.08885 0.058725693 58.00896438 4654.37589 13.73819 TTC38 5.69518522496362e-10 0.38215600491699 0.617843994513491 tetratricopeptide repeat domain 38 . . . . . . 0.09803 0.913082291 89.54352442 574.23128 4.86368 TTC39A 0.0983102549140287 0.90137017700795 0.000319568078021694 tetratricopeptide repeat domain 39A . . . unclassifiable (Anatomical System);muscle;colon;fovea centralis;choroid;lens;skin;retina;breast;prostate;optic nerve;lung;endometrium;macula lutea;liver;testis;kidney;brain;mammary gland;stomach; occipital lobe;testis - interstitial;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.30275 . -0.358119787 29.16371786 40.28663 1.18371 TTC39A-AS1 . . . TTC39A antisense RNA 1 . . . . . . . . . . . TTC39B 1.06813738722138e-11 0.473475101235642 0.526524898753677 tetratricopeptide repeat domain 39B . . . unclassifiable (Anatomical System);lung;cartilage;islets of Langerhans;liver;testis;colon;spleen;germinal center;skeletal muscle; . 0.24390 0.08848 -0.328796968 30.86223166 202.92373 3.07563 TTC39C 0.0146468612556312 0.985103139958004 0.000249998786364566 tetratricopeptide repeat domain 39C . . . ovary;colon;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;blood;lens;skeletal muscle;lung;nasopharynx;placenta;macula lutea;liver;cervix;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;liver;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.16365 . -0.626318434 17.03231894 42.62108 1.23653 TTC39C-AS1 . . . TTC39C antisense RNA 1 . . . . . . . . . . . TTC39CP1 . . . tetratricopeptide repeat domain 39C pseudogene 1 . . . . . . . . . . . TTC39DP . . . tetratricopeptide repeat domain 39D, pseudogene . . . . . . . . . . . TTC41P . . . tetratricopeptide repeat domain 41, pseudogene . . . . . . . . . . . TTF1 1.47325071683527e-06 0.990450955142725 0.00954757160655871 transcription termination factor, RNA polymerase I FUNCTION: Multifunctional nucleolar protein that terminates ribosomal gene transcription, mediates replication fork arrest and regulates RNA polymerase I transcription on chromatin. Plays a dual role in rDNA regulation, being involved in both activation and silencing of rDNA transcription. Interaction with BAZ2A/TIP5 recovers DNA-binding activity. {ECO:0000269|PubMed:7597036}.; . . lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;larynx;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);heart;urinary;pharynx;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;prefrontal cortex;skeletal muscle; 0.38901 0.08675 1.273147413 93.66595895 1035.531 6.17843 TTF2 7.3515283462504e-16 0.796421524024627 0.203578475975372 transcription termination factor, RNA polymerase II FUNCTION: DsDNA-dependent ATPase which acts as a transcription termination factor by coupling ATP hydrolysis with removal of RNA polymerase II from the DNA template. May contribute to mitotic transcription repression. May also be involved in pre-mRNA splicing. {ECO:0000269|PubMed:10455150, ECO:0000269|PubMed:12927788, ECO:0000269|PubMed:15125840, ECO:0000269|PubMed:9748214}.; . . . . 0.56209 0.09555 1.434815931 95.02830856 409.4185 4.24152 TTI1 0.000238871043749718 0.99588590024896 0.00387522870729007 TELO2 interacting protein 1 FUNCTION: Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals. {ECO:0000269|PubMed:20427287, ECO:0000269|PubMed:20801936, ECO:0000269|PubMed:20810650}.; . TISSUE SPECIFICITY: Widely expressed.; . . 0.18744 0.09392 -0.523584927 20.93654164 285.45946 3.61803 TTI2 0.00188633676443484 0.975243314084963 0.0228703491506024 TELO2 interacting protein 2 FUNCTION: Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. {ECO:0000269|PubMed:20801936, ECO:0000269|PubMed:20810650}.; DISEASE: Mental retardation, autosomal recessive 39 (MRT39) [MIM:615541]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT39 affected individuals show delayed psychomotor development, severe speech delay, short stature, kyphoscoliosis, and dysmorphic facial features. Behavioral abnormalities include hyperactivity, aggression, and stereotypic movements. {ECO:0000269|PubMed:23956177}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;cerebellum; 0.12249 0.08936 0.176444282 66.07100731 187.20112 2.97095 TTIM1 . . . T-cell tumor invasion and metastasis 1 . . . . . . . . . . . TTK 0.00535776884387935 0.994633246319877 8.98483624322323e-06 TTK protein kinase FUNCTION: Phosphorylates proteins on serine, threonine, and tyrosine. Probably associated with cell proliferation. Essential for chromosome alignment by enhancing AURKB activity (via direct CDCA8 phosphorylation) at the centromere, and for the mitotic checkpoint. {ECO:0000269|PubMed:18243099}.; . TISSUE SPECIFICITY: Present in rapidly proliferating cell lines.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;skin;skeletal muscle;bone marrow;uterus;prostate;lung;nasopharynx;placenta;liver;testis;head and neck;germinal center;brain;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;testis;tumor;trigeminal ganglion; 0.86473 0.16889 -0.286522835 33.47487615 186.49212 2.96567 TTL 0.984657698728457 0.015333952683376 8.3485881671772e-06 tubulin tyrosine ligase FUNCTION: Catalyzes the post-translational addition of a tyrosine to the C-terminal end of detyrosinated alpha-tubulin. {ECO:0000250}.; . . smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;bile duct;lung;pia mater;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;thymus; . 0.22088 0.14529 -0.071520315 48.34866714 32.83053 1.01890 TTLL1 0.00563299514240826 0.989442386783249 0.00492461807434228 tubulin tyrosine ligase like 1 FUNCTION: Catalytic subunit of the neuronal tubulin polyglutamylase complex. Modifies alpha- and beta-tubulin, generating side chains of glutamate on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in a wide range of tissues. Has a stronger expression in heart, brain and testis. {ECO:0000269|PubMed:11054573}.; unclassifiable (Anatomical System);cartilage;heart;salivary gland;colon;fovea centralis;skin;skeletal muscle;uterus;prostate;lung;frontal lobe;nasopharynx;bone;placenta;macula lutea;hippocampus;testis;germinal center;kidney;brain;stomach; medulla oblongata;testis - seminiferous tubule;testis;parietal lobe; 0.19223 0.11458 -0.844966979 11.1759849 47.2395 1.33264 TTLL2 4.93844726071945e-06 0.412633135420466 0.587361926132273 tubulin tyrosine ligase like 2 FUNCTION: Probable tubulin polyglutamylase that forms polyglutamate side chains on tubulin. Probably acts when complexed with other proteins (By similarity). {ECO:0000250}.; . . lung;testis;colon; testis - interstitial;superior cervical ganglion;ciliary ganglion; 0.10509 . 1.58549778 95.80679406 531.19904 4.70204 TTLL3 3.84160687240076e-14 0.0801330739270841 0.919866926072878 tubulin tyrosine ligase like 3 FUNCTION: Monoglycylase which modifies alpha- and beta-tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction. {ECO:0000269|PubMed:19524510}.; . . colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;spinal cord;prefrontal cortex;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; . 0.09890 -0.214928658 37.7388535 1000.48997 6.09360 TTLL4 2.83171379258391e-06 0.999965484908324 3.16833778829905e-05 tubulin tyrosine ligase like 4 FUNCTION: Polyglutamylase which preferentially modifies beta- tubulin and nucleosome assembly proteins NAP1 and NAP2. Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step. {ECO:0000250|UniProtKB:Q80UG8}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;larynx;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;heart;cartilage;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;mammary gland; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.16564 0.09368 1.677366355 96.33757962 4897.26889 14.24447 TTLL5 1.97990564092488e-09 0.999999386641017 6.11379077064306e-07 tubulin tyrosine ligase like 5 FUNCTION: Polyglutamylase which preferentially modifies alpha- tubulin. Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step (By similarity). Required for CCSAP localization to both spindle and cilia microtubules. Increases the effects of NCOA2 in glucocorticoid receptor-mediated repression and induction and in androgen receptor-mediated induction (PubMed:17116691, PubMed:22493317). {ECO:0000250|UniProtKB:Q8CHB8, ECO:0000269|PubMed:17116691, ECO:0000269|PubMed:22493317}.; DISEASE: Cone-rod dystrophy 19 (CORD19) [MIM:615860]: A form of cone-rod dystrophy, an inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. {ECO:0000269|PubMed:24791901}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the retina, found in the rod and cone photoreceptors (at protein level). Widely expressed with highest levels in heart and skeletal muscle and low levels in other tissues. {ECO:0000269|PubMed:17116691, ECO:0000269|PubMed:24791901}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;muscle;skeletal muscle;breast;lung;adrenal gland;placenta;visual apparatus;liver;head and neck;spleen;cervix;mammary gland;stomach; dorsal root ganglion;testis - interstitial;uterus corpus;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.60603 . -0.916836882 9.831328143 5848.36871 15.85461 TTLL6 7.4885844910963e-08 0.463913352759008 0.536086572355147 tubulin tyrosine ligase like 6 FUNCTION: Polyglutamylase which preferentially modifies alpha- tubulin. Mediates tubulin polyglutamylation in cilia. Involved in the side-chain elongation step of the polyglutamylation reaction rather than in the initiation step. {ECO:0000250|UniProtKB:A4Q9E8}.; . . unclassifiable (Anatomical System);medulla oblongata;lung;testis;brain;stomach; . 0.05945 . -0.130380821 44.03161123 2476.43054 9.27901 TTLL7 0.268072469343805 0.731927454251442 7.64047528003474e-08 tubulin tyrosine ligase like 7 FUNCTION: Polyglutamylase which preferentially modifies beta- tubulin (PubMed:25959773). Mediates both ATP-dependent initiation and elongation of polyglutamylation of microtubules (PubMed:25959773). Required for neurite growth; responsible for the strong increase in tubulin polyglutamylation during postnatal neuronal maturation (By similarity). {ECO:0000250|UniProtKB:A4Q9F0, ECO:0000269|PubMed:25959773}.; . TISSUE SPECIFICITY: Highly expressed in the nervous system including spinal cord, thalamus, hippocampus, hypothalamus and cerebellum. {ECO:0000269|PubMed:16901895}.; unclassifiable (Anatomical System);lung;frontal lobe;endometrium;hypothalamus;bone;amnion;liver;testis;kidney;brain;skeletal muscle;retina; dorsal root ganglion;medulla oblongata;occipital lobe;thalamus;hypothalamus;pons;caudate nucleus;atrioventricular node;subthalamic nucleus;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex; 0.20746 0.09426 -0.754958418 13.57631517 77.26727 1.84590 TTLL7-IT1 . . . TTLL7 intronic transcript 1 . . . . . . . . . . . TTLL8 . . . tubulin tyrosine ligase like 8 FUNCTION: Monoglycylase which modifies both tubulin and non- tubulin proteins, generating side chains of glycine on the gamma- carboxyl groups of specific glutamate residues of target proteins. Monoglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. Has the ability to modify non-tubulin proteins such as ANP32A, ANP32B, SET and NCL. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);testis; dorsal root ganglion;medulla oblongata;superior cervical ganglion;subthalamic nucleus;pons;atrioventricular node;trigeminal ganglion;cerebellum; 0.72788 0.09578 . . 3618.46748 11.65843 TTLL9 4.48655268982384e-10 0.340947349756202 0.659052649795143 tubulin tyrosine ligase like 9 FUNCTION: Probable tubulin polyglutamylase that forms polyglutamate side chains on tubulin. Probably acts when complexed with other proteins (By similarity). {ECO:0000250}.; . . brain; dorsal root ganglion;testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.23576 0.11269 0.42259095 77.22929936 223.995 3.23636 TTLL10 1.94738806982348e-05 0.46328044912402 0.536700076995282 tubulin tyrosine ligase like 10 FUNCTION: Inactive polyglycylase. {ECO:0000269|PubMed:19524510}.; . . . . 0.11164 . 3.269164597 99.39844303 2864.03353 10.12799 TTLL10-AS1 . . . TTLL10 antisense RNA 1 . . . . . . . . . . . TTLL11 0.0182318373613278 0.8954497112363 0.0863184514023724 tubulin tyrosine ligase like11 FUNCTION: Polyglutamase which preferentially modifies alpha- tubulin. Involved in the side-chain elongation step of the polyglutamylation reaction rather than in the initiation step (By similarity). Required for CCSAP localization to both spindle and cilia microtubules. {ECO:0000250|UniProtKB:A4Q9F4, ECO:0000269|PubMed:22493317}.; . . unclassifiable (Anatomical System);ovary;colon;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;lung;placenta;macula lutea;liver;testis;spleen;brain; . 0.09012 . -0.26993514 34.59542345 2780.37895 9.96418 TTLL11-IT1 . . . TTLL11 intronic transcript 1 . . . . . . . . . . . TTLL12 1.99091364629049e-15 0.0144008301207839 0.985599169879214 tubulin tyrosine ligase like 12 . . . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;bone;iris;testis;germinal center;brain;pineal gland;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;liver;testis;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.50570 0.10895 -0.457443171 23.70252418 3676.12735 11.78719 TTLL13P . . . tubulin tyrosine ligase like 13, pseudogene FUNCTION: Polyglutamylase which preferentially modifies alpha- tubulin. Involved in the side-chain elongation step of the polyglutamylation reaction rather than in the initiation step (By similarity). {ECO:0000250|UniProtKB:A4Q9F6}.; . . . . 0.13253 . -0.466531444 23.51380042 . . TTN 1.21111377105808e-32 1 5.79491096992649e-127 titin FUNCTION: Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase. {ECO:0000269|PubMed:9804419}.; DISEASE: Hereditary myopathy with early respiratory failure (HMERF) [MIM:603689]: Autosomal dominant, adult-onset myopathy with early respiratory muscle involvement. {ECO:0000269|PubMed:15802564}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, familial hypertrophic 9 (CMH9) [MIM:613765]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:10462489}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated 1G (CMD1G) [MIM:604145]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:11788824, ECO:0000269|PubMed:11846417, ECO:0000269|PubMed:16465475}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Tardive tibial muscular dystrophy (TMD) [MIM:600334]: Autosomal dominant, late-onset distal myopathy. Muscle weakness and atrophy are usually confined to the anterior compartment of the lower leg, in particular the tibialis anterior muscle. Clinical symptoms usually occur at age 35-45 years or much later. {ECO:0000269|PubMed:12145747, ECO:0000269|PubMed:12891679}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Limb-girdle muscular dystrophy 2J (LGMD2J) [MIM:608807]: An autosomal recessive degenerative myopathy characterized by progressive weakness of the pelvic and shoulder girdle muscles. Severe disability is observed within 20 years of onset. {ECO:0000269|PubMed:12145747}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Early-onset myopathy with fatal cardiomyopathy (EOMFC) [MIM:611705]: Early-onset myopathies are inherited muscle disorders that manifest typically from birth or infancy with hypotonia, muscle weakness, and delayed motor development. EOMFC is a titinopathy that, in contrast with the previously described examples, involves both heart and skeletal muscle, has a congenital onset, and is purely recessive. This phenotype is due to homozygous out-of-frame TTN deletions, which lead to a total absence of titin's C-terminal end from striated muscles and to secondary CAPN3 depletion. {ECO:0000269|PubMed:17444505}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoforms 3, 7 and 8 are expressed in cardiac muscle. Isoform 4 is expressed in vertebrate skeletal muscle. Isoform 6 is expressed in skeletal muscle (at protein level). {ECO:0000269|PubMed:11717165, ECO:0000269|PubMed:7819249}.; myocardium;ovary;colon;parathyroid;choroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;whole body;optic nerve;atrium;frontal lobe;larynx;thyroid;bone;testis;germinal center;unclassifiable (Anatomical System);heart;tongue;muscle;spinal cord;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;visual apparatus;macula lutea;alveolus;liver;spleen;head and neck;kidney;peripheral nerve; superior cervical ganglion;tongue;thyroid;globus pallidus;testis;atrioventricular node;pons;fetal thyroid;trigeminal ganglion;skeletal muscle; 0.40699 0.38418 2.169883458 98.04199104 74772.86558 42.91324 TTN-AS1 . . . TTN antisense RNA 1 . . . . . . . . . . . TTPA 0.0098843163239351 0.821555026867696 0.168560656808369 tocopherol (alpha) transfer protein FUNCTION: Binds alpha-tocopherol, enhances its transfer between separate membranes, and stimulates its release from liver cells (PubMed:7887897). Binds both phosphatidylinol 3,4-bisphosphate and phosphatidylinol 4,5-bisphosphate; the resulting conformation change is important for the release of the bound alpha-tocopherol (By similarity). {ECO:0000250, ECO:0000269|PubMed:7887897}.; DISEASE: Ataxia with isolated vitamin E deficiency (AVED) [MIM:277460]: An autosomal recessive disease characterized by undetectable or markedly reduced plasma levels of vitamin E, spinocerebellar degeneration, ataxia, areflexia and proprioception loss. {ECO:0000269|PubMed:15300460, ECO:0000269|PubMed:7566022, ECO:0000269|PubMed:8602747, ECO:0000269|PubMed:9463307}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . amygdala;breast;ovary;placenta;liver;testis;parathyroid;spleen;kidney;skeletal muscle; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17864 0.58889 -0.163345027 41.24793583 27.09061 0.87422 TTPAL 0.640756733161688 0.357881411443501 0.00136185539481108 tocopherol (alpha) transfer protein-like FUNCTION: May act as a protein that binds a hydrophobic ligand. {ECO:0000305}.; . . unclassifiable (Anatomical System);lung;cartilage;ovary;heart;synovium;placenta;liver;testis;spleen;blood;brain;skin;skeletal muscle; superior cervical ganglion;liver; 0.38666 0.10566 0.283038099 71.26680821 271.7154 3.53205 TTR 0.130835841006919 0.780194086546007 0.0889700724470738 transthyretin FUNCTION: Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. {ECO:0000269|PubMed:3714052}.; DISEASE: Amyloidosis, transthyretin-related (AMYL-TTR) [MIM:105210]: A hereditary generalized amyloidosis due to transthyretin amyloid deposition. Protein fibrils can form in different tissues leading to amyloid polyneuropathies, amyloidotic cardiomyopathy, carpal tunnel syndrome, systemic senile amyloidosis. The disease includes leptomeningeal amyloidosis that is characterized by primary involvement of the central nervous system. Neuropathologic examination shows amyloid in the walls of leptomeningeal vessels, in pia arachnoid, and subpial deposits. Some patients also develop vitreous amyloid deposition that leads to visual impairment (oculoleptomeningeal amyloidosis). Clinical features include seizures, stroke-like episodes, dementia, psychomotor deterioration, variable amyloid deposition in the vitreous humor. {ECO:0000269|PubMed:10036587, ECO:0000269|PubMed:10071047, ECO:0000269|PubMed:10211412, ECO:0000269|PubMed:10436378, ECO:0000269|PubMed:10439117, ECO:0000269|PubMed:10611950, ECO:0000269|PubMed:10627135, ECO:0000269|PubMed:10694917, ECO:0000269|PubMed:10842705, ECO:0000269|PubMed:10842718, ECO:0000269|PubMed:10882995, ECO:0000269|PubMed:11445644, ECO:0000269|PubMed:11866053, ECO:0000269|PubMed:12050338, ECO:0000269|PubMed:12557757, ECO:0000269|PubMed:12771253, ECO:0000269|PubMed:1301926, ECO:0000269|PubMed:1351039, ECO:0000269|PubMed:1362222, ECO:0000269|PubMed:1436517, ECO:0000269|PubMed:1517749, ECO:0000269|PubMed:1520326, ECO:0000269|PubMed:1520336, ECO:0000269|PubMed:15214015, ECO:0000269|PubMed:15217993, ECO:0000269|PubMed:1544214, ECO:0000269|PubMed:15478468, ECO:0000269|PubMed:1570831, ECO:0000269|PubMed:1656975, ECO:0000269|PubMed:1734866, ECO:0000269|PubMed:17453626, ECO:0000269|PubMed:17503405, ECO:0000269|PubMed:17577687, ECO:0000269|PubMed:17635579, ECO:0000269|PubMed:1932142, ECO:0000269|PubMed:2046936, ECO:0000269|PubMed:2161654, ECO:0000269|PubMed:23317988, ECO:0000269|PubMed:2363717, ECO:0000269|PubMed:2891727, ECO:0000269|PubMed:3022108, ECO:0000269|PubMed:3135807, ECO:0000269|PubMed:3722385, ECO:0000269|PubMed:3818577, ECO:0000269|PubMed:6487335, ECO:0000269|PubMed:6583672, ECO:0000269|PubMed:6651852, ECO:0000269|PubMed:7655883, ECO:0000269|PubMed:7850982, ECO:0000269|PubMed:7910950, ECO:0000269|PubMed:7914929, ECO:0000269|PubMed:7923855, ECO:0000269|PubMed:8019560, ECO:0000269|PubMed:8038017, ECO:0000269|PubMed:8081397, ECO:0000269|PubMed:8095302, ECO:0000269|PubMed:8133316, ECO:0000269|PubMed:8257997, ECO:0000269|PubMed:8352764, ECO:0000269|PubMed:8579098, ECO:0000269|PubMed:8990019, ECO:0000269|PubMed:9066351, ECO:0000269|PubMed:9605286, ECO:0000269|Ref.90}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hyperthyroxinemia, dystransthyretinemic (DTTRH) [MIM:145680]: A condition characterized by elevation of total and free thyroxine in healthy, euthyroid persons without detectable binding protein abnormalities. {ECO:0000269|PubMed:1979335}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Carpal tunnel syndrome 1 (CTS1) [MIM:115430]: A condition characterized by entrapment of the median nerve within the carpal tunnel. Symptoms include burning pain and paresthesias involving the ventral surface of the hand and fingers which may radiate proximally. Impairment of sensation in the distribution of the median nerve and thenar muscle atrophy may occur. This condition may be associated with repetitive occupational trauma, wrist injuries, amyloid neuropathies, rheumatoid arthritis. {ECO:0000269|PubMed:8309582}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in serum and cerebrospinal fluid (at protein level). Highly expressed in choroid plexus epithelial cells. Detected in retina pigment epithelium and liver. {ECO:0000269|PubMed:10328977, ECO:0000269|PubMed:3714052}.; unclassifiable (Anatomical System);meninges;ovary;islets of Langerhans;hypothalamus;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;pia mater;lung;visual apparatus;hippocampus;liver;dura mater;kidney;brain;bladder; amygdala;whole brain;thalamus;fetal liver;pancreas;cerebellum peduncles;hypothalamus;beta cell islets;liver;caudate nucleus;cerebellum; 0.59945 0.84544 0.503505267 79.88912479 101.8863 2.18413 TTTY1 . . . testis-specific transcript, Y-linked 1 (non-protein coding) . . . . . . . . . . . TTTY1B . . . testis-specific transcript, Y-linked 1B (non-protein coding) . . . . . . . . . . . TTTY2 . . . testis-specific transcript, Y-linked 2 (non-protein coding) . . . . . . . . . . . TTTY2B . . . testis-specific transcript, Y-linked 2B (non-protein coding) . . . . . . . . . . . TTTY3 . . . testis-specific transcript, Y-linked 3 (non-protein coding) . . . . . . . . . . . TTTY3B . . . testis-specific transcript, Y-linked 3B (non-protein coding) . . . . . . . . . . . TTTY4 . . . testis-specific transcript, Y-linked 4 (non-protein coding) . . . . . . . . . . . TTTY4B . . . testis-specific transcript, Y-linked 4B (non-protein coding) . . . . . . . . . . . TTTY4C . . . testis-specific transcript, Y-linked 4C (non-protein coding) . . . . . . . . . . . TTTY5 . . . testis-specific transcript, Y-linked 5 (non-protein coding) . . . . . . . . . . . TTTY6 . . . testis-specific transcript, Y-linked 6 (non-protein coding) . . . lung;testis; . . . . . . . TTTY6B . . . testis-specific transcript, Y-linked 6B (non-protein coding) . . . lung;testis; . . . . . . . TTTY7 . . . testis-specific transcript, Y-linked 7 (non-protein coding) . . . lung;testis; . . . . . . . TTTY7B . . . testis-specific transcript, Y-linked 7B (non-protein coding) . . . lung;testis; . . . . . . . TTTY8 . . . testis-specific transcript, Y-linked 8 (non-protein coding) . . . . . 0.16343 . . . . . TTTY8B . . . testis-specific transcript, Y-linked 8B (non-protein coding) . . . . . 0.16343 . . . . . TTTY9A . . . testis-specific transcript, Y-linked 9A (non-protein coding) . . . . . . . . . . . TTTY9B . . . testis-specific transcript, Y-linked 9B (non-protein coding) . . . . . . . . . . . TTTY10 . . . testis-specific transcript, Y-linked 10 (non-protein coding) . . . . . . . . . . . TTTY11 . . . testis-specific transcript, Y-linked 11 (non-protein coding) . . . testis; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; . . . . . . TTTY12 . . . testis-specific transcript, Y-linked 12 (non-protein coding) . . . . . . . . . . . TTTY13 . . . testis-specific transcript, Y-linked 13 (non-protein coding) . . . . . . . . . . . TTTY13B . . . testis-specific transcript, Y-linked 13B . . . . . . . . . . . TTTY13C . . . testis-specific transcript, Y-linked 13C . . . . . . . . . . . TTTY14 . . . testis-specific transcript, Y-linked 14 (non-protein coding) . . . prostate;lymph node;lung;ovary;hypothalamus;thyroid;placenta;liver;testis;parathyroid;brain; . . . . . . . TTTY15 . . . testis-specific transcript, Y-linked 15 (non-protein coding) . . . . . . . . . . . TTTY16 . . . testis-specific transcript, Y-linked 16 (non-protein coding) . . . . . . . . . . . TTTY17A . . . testis-specific transcript, Y-linked 17A (non-protein coding) . . . . . . . . . . . TTTY17B . . . testis-specific transcript, Y-linked 17B (non-protein coding) . . . . . . . . . . . TTTY17C . . . testis-specific transcript, Y-linked 17C (non-protein coding) . . . . . . . . . . . TTTY18 . . . testis-specific transcript, Y-linked 18 (non-protein coding) . . . . . . . . . . . TTTY19 . . . testis-specific transcript, Y-linked 19 (non-protein coding) . . . . . . . . . . . TTTY20 . . . testis-specific transcript, Y-linked 20 (non-protein coding) . . . . . . . . . . . TTTY21 . . . testis-specific transcript, Y-linked 21 (non-protein coding) . . . . . . . . . . . TTTY21B . . . testis-specific transcript, Y-linked 21B (non-protein coding) . . . . . . . . . . . TTTY22 . . . testis-specific transcript, Y-linked 22 (non-protein coding) . . . . . . . . . . . TTTY23 . . . testis-specific transcript, Y-linked 23 (non-protein coding) . . . . . . . . . . . TTTY23B . . . testis-specific transcript, Y-linked 23B (non-protein coding) . . . . . . . . . . . TTTY24P . . . testis-specific transcript, Y-linked 24, pseudogene . . . . . . . . . . . TTTY25P . . . testis-specific transcript, Y-linked 25, pseudogene . . . . . . . . . . . TTTY26P . . . testis-specific transcript, Y-linked 26, pseudogene . . . . . . . . . . . TTTY27P . . . testis-specific transcript, Y-linked 27, pseudogene . . . . . . . . . . . TTTY28P . . . testis-specific transcript, Y-linked 28, pseudogene . . . . . . . . . . . TTTY29P . . . testis-specific transcript, Y-linked 29, pseudogene . . . . . . . . . . . TTTY30P . . . testis-specific transcript, Y-linked 30, pseudogene . . . . . . . . . . . TTTY31P . . . testis-specific transcript, Y-linked 31, pseudogene . . . . . . . . . . . TTYH1 0.998439974081688 0.00155999463521852 3.1283093602207e-08 tweety family member 1 FUNCTION: Probable chloride channel. May be involved in cell adhesion (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, eye, ovary and testis, and at lower levels in muscle, placenta, liver and lung. {ECO:0000269|PubMed:17116230}.; unclassifiable (Anatomical System);heart;ovary;hypothalamus;choroid;skeletal muscle;skin;retina;uterus;optic nerve;lung;frontal lobe;visual apparatus;liver;testis;spleen;mammary gland;pineal gland;brain; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;testis;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.45860 0.10645 0.022122107 55.69120075 94.13263 2.08647 TTYH2 0.347961542462659 0.651921626310593 0.000116831226747474 tweety family member 2 FUNCTION: Probable large-conductance Ca(2+)-activated chloride channel. May play a role in Ca(2+) signal transduction. May be involved in cell proliferation and cell aggregation. {ECO:0000269|PubMed:15010458}.; . TISSUE SPECIFICITY: Expressed at higher level in brain and testis and at lower levels in heart, ovary, spleen and peripheral blood leukocytes. Up-regulated in 13 of 16 renal cell carcinoma samples examined. Up-regulated in colon carcinoma. {ECO:0000269|PubMed:11597145, ECO:0000269|PubMed:17569141}.; ovary;sympathetic chain;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;iris;testis;brain;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;spinal cord;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;cervix;kidney;mammary gland;cerebellum; whole brain;thalamus;occipital lobe;medulla oblongata;hypothalamus;spinal cord;prefrontal cortex;pons;caudate nucleus;parietal lobe; 0.13895 0.10322 0.826715241 88.09271054 4174.85594 12.83577 TTYH3 0.979598759303839 0.0203978304297689 3.41026639223902e-06 tweety family member 3 FUNCTION: Probable large-conductance Ca(2+)-activated chloride channel. May play a role in Ca(2+) signal transduction. {ECO:0000269|PubMed:15010458}.; . TISSUE SPECIFICITY: Expressed in excitable tissues. Expressed in the brain, heart, skeletal muscle, colon, spleen, kidney and peripheral blood leukocytes. {ECO:0000269|PubMed:15010458}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;pharynx;blood;lens;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; . 0.20673 0.13236 -0.354480518 29.42911064 106.07775 2.23473 TUB 0.471428314326012 0.528526372810899 4.53128630892771e-05 tubby bipartite transcription factor FUNCTION: Functions in signal transduction from heterotrimeric G protein-coupled receptors. Binds to membranes containing phosphatidylinositol 4,5-bisphosphate. Can bind DNA (in vitro). May contribute to the regulation of transcription in the nucleus. Could be involved in the hypothalamic regulation of body weight (By similarity). Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages. {ECO:0000250, ECO:0000269|PubMed:19837063}.; DISEASE: Retinal dystrophy and obesity (RDOB) [MIM:616188]: A disease characterized by obesity, night blindness, decreased visual acuity, and electrophysiological features of a rod cone dystrophy. {ECO:0000269|PubMed:24375934}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;colon;choroid;fovea centralis;retina;uterus;optic nerve;whole body;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;lens;skeletal muscle;lung;adrenal gland;placenta;hippocampus;visual apparatus;macula lutea;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.28211 0.25332 -0.905656269 10.12031139 201.17736 3.06482 TUB-AS1 . . . TUB antisense RNA 1 . . . . . . . . . . . TUBA1A 0.836535571093595 0.162790734123328 0.000673694783076586 tubulin alpha 1a FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.; DISEASE: Lissencephaly 3 (LIS3) [MIM:611603]: A classic type lissencephaly associated with psychomotor retardation and seizures. Features include agyria or pachygyria or laminar heterotopia, severe mental retardation, motor delay, variable presence of seizures, and abnormalities of corpus callosum, hippocampus, cerebellar vermis and brainstem. {ECO:0000269|PubMed:17584854}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at a high level in fetal brain. {ECO:0000269|PubMed:17584854}.; ovary;salivary gland;sympathetic chain;intestine;colon;substantia nigra;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;pineal gland;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;aorta; amygdala;dorsal root ganglion;whole brain;thalamus;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.92622 . -0.251530012 35.42108988 . . TUBA1B 0.828418234696983 0.170813634832685 0.000768130470332813 tubulin alpha 1b FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.; . . lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;gum;thyroid;germinal center;brain;tonsil;heart;cartilage;pineal body;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;oesophagus;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum;thymus; whole brain;amygdala;dorsal root ganglion;medulla oblongata;thalamus;occipital lobe;hypothalamus;spinal cord;temporal lobe;pons;skeletal muscle;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.79871 0.21177 -0.229483771 36.86010852 1.16568 0.03209 TUBA1C 0.840150770014777 0.159214953581257 0.000634276403965791 tubulin alpha 1c FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.; . . lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;tonsil;heart;tongue;pineal body;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;fovea centralis;vein;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);trophoblast;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;duodenum;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;occipital lobe;thalamus;medulla oblongata;hypothalamus;spinal cord;temporal lobe;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.32149 . -0.582225231 18.44184949 49.77176 1.38333 TUBA3C 0.00681759403629645 0.917162830217885 0.0760195757458184 tubulin alpha 3c FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.; . TISSUE SPECIFICITY: Testis specific. {ECO:0000269|Ref.5}.; unclassifiable (Anatomical System);uterus;heart;hippocampus;liver;testis;spleen; testis - interstitial;thalamus;testis - seminiferous tubule;globus pallidus;testis;pons;parietal lobe; . 0.19444 -0.574945567 18.90186365 609.47595 4.99143 TUBA3D 3.70763769526702e-08 0.102022073447958 0.897977889475665 tubulin alpha 3d FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.; . TISSUE SPECIFICITY: Testis specific. {ECO:0000269|Ref.5}.; unclassifiable (Anatomical System);uterus;heart;hippocampus;testis;mammary gland; . 0.50222 0.29199 -0.690637458 15.12149092 36.71914 1.10110 TUBA3E 0.00120527821375768 0.846489817358505 0.152304904427737 tubulin alpha 3e FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;heart;testis;mammary gland; . 0.51437 0.17173 0.378498378 75.58386412 520.54799 4.65963 TUBA3FP . . . tubulin alpha 3f pseudogene . . . . . . . . . . . TUBA3GP . . . tubulin alpha 3g pseudogene . . . . . . . . . . . TUBA4A 0.0296379358390164 0.923984962292574 0.0463771018684092 tubulin alpha 4a FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.; DISEASE: Amyotrophic lateral sclerosis 22, with or without frontotemporal dementia (ALS22) [MIM:616208]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. Patients with ALS22 may develop frontotemporal dementia. {ECO:0000269|PubMed:25374358}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;cerebellum; amygdala;whole brain;occipital lobe;subthalamic nucleus;temporal lobe;prefrontal cortex;globus pallidus;cingulate cortex;skeletal muscle;parietal lobe; 0.99311 0.64888 -0.361761279 28.6329323 3.61036 0.13166 TUBA4B . . . tubulin alpha 4b . . . . . 0.13634 . . . . . TUBA8 0.00322749700590359 0.824934562946497 0.1718379400476 tubulin alpha 8 FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.; DISEASE: Polymicrogyria, with optic nerve hypoplasia (PMGONH) [MIM:613180]: A disease characterized by extensive polymicrogyria, optic nerve hypoplasia, severe developmental delay, hypotonia, seizures, a dysplastic or absent corpus callosum and colpocephaly. Polymicrogyria is a malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. Polymicrogyria is a heterogeneous disorder, considered to be the result of postmigratory abnormal cortical organization. {ECO:0000269|PubMed:19896110}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Preferentially expressed in heart, skeletal muscle and testis. Expressed at low levels in the developing brain. {ECO:0000269|PubMed:20466094}.; unclassifiable (Anatomical System);lung;ovary;islets of Langerhans;muscle;lens;brain;skeletal muscle; . 0.51410 0.35026 -0.288341872 33.41589998 95.24542 2.10626 TUBAL3 0.000170843012375288 0.690090459515448 0.309738697472177 tubulin alpha like 3 FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). {ECO:0000250}.; . . . . 0.05372 0.15351 -0.573127851 18.96083982 629.71622 5.05781 TUBAP . . . tubulin alpha pseudogene . . . . . . . . . . . TUBAP2 . . . tubulin alpha pseudogene 2 . . . . . . . . . . . TUBAP3 . . . tubulin alpha pseudogene 3 . . . . . . . . . . . TUBAP4 . . . tubulin alpha pseudogene 4 . . . . . . . . . . . TUBB 0.875276521102353 0.124395633610976 0.000327845286671259 tubulin beta class I FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.; DISEASE: Cortical dysplasia, complex, with other brain malformations 6 (CDCBM6) [MIM:615771]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Affected individuals have microcephaly, ataxia, and severe delayed psychomotor development. Brain imaging shows variable malformations of cortical development, including white matter streaks, dysmorphic basal ganglia, corpus callosum abnormalities, brainstem and cerebellar hypoplasia, cortical dysplasia, polymicrogyria. {ECO:0000269|PubMed:23246003}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in spleen, thymus and immature brain. {ECO:0000269|PubMed:20191564}.; . . 0.73841 . -0.141298762 42.87567823 . . TUBB1 7.16532359955701e-06 0.486339854107818 0.513652980568583 tubulin beta 1 class VI FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). {ECO:0000250}.; DISEASE: Macrothrombocytopenia, autosomal dominant, TUBB1-related (MAD-TUBB1) [MIM:613112]: A congenital blood disorder characterized by increased platelet size and decreased number of circulating platelets. {ECO:0000269|PubMed:18849486}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Hematopoietic cell-specific. Major isotype in leukocytes, where it represents 50% of all beta-tubulins. {ECO:0000269|PubMed:20191564}.; unclassifiable (Anatomical System);ovary;parathyroid;blood;skin;bone marrow;pancreas;prostate;whole body;lung;frontal lobe;placenta;visual apparatus;liver;testis;spleen;kidney;brain; dorsal root ganglion; 0.23640 0.25159 0.868987491 88.84760557 2687.40184 9.75564 TUBB1P1 . . . tubulin beta 1 class VI pseudogene 1 . . . . . . . . . . . TUBB1P2 . . . tubulin beta 1 class VI pseudogene 2 . . . . . . . . . . . TUBB2A . . . tubulin beta 2A class IIa FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). {ECO:0000250}.; DISEASE: Cortical dysplasia, complex, with other brain malformations 5 (CDCBM5) [MIM:615763]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Clinical features include seizures, global developmental delay, and various brain malformations such as a diffuse simplified gyral pattern with reduced volume of white matter, globular basal ganglia, thin and dysmorphic corpus callosum, mild brainstem hypoplasia with a flat pons, mild cerebellar vermis hypoplasia, and mildly enlarged posterior fossa. {ECO:0000269|PubMed:24702957}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: High expression in brain, where it represents 30% of all beta-tubulins. {ECO:0000269|PubMed:20191564}.; . . 0.87839 0.33588 -0.119252484 44.53880632 2.40691 0.08385 TUBB2B . . . tubulin beta 2B class IIb FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). TUBB2B is implicated in neuronal migration. {ECO:0000250, ECO:0000269|PubMed:19465910}.; DISEASE: Polymicrogyria, symmetric or asymmetric (PMGYSA) [MIM:610031]: A malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. Polymicrogyria is a heterogeneous disorder, considered to be the result of postmigratory abnormal cortical organization. {ECO:0000269|PubMed:19465910}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: High expression in brain. {ECO:0000269|PubMed:20191564}.; lymphoreticular;ovary;salivary gland;sympathetic chain;intestine;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;whole body;ganglion;frontal lobe;endometrium;bone;pituitary gland;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;muscle;pharynx;blood;lens;breast;lung;cornea;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;aorta;cerebellum; whole brain;amygdala;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;cerebellum; 0.72371 0.27035 . . . . TUBB2BP1 . . . tubulin beta 2B class IIb pseudogene 1 . . . . . . . . . . . TUBB3 0.960789307391211 0.0391260015292011 8.46910795881596e-05 tubulin beta 3 class III FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. TUBB3 plays a critical role in proper axon guidance and mantainance. {ECO:0000269|PubMed:20074521}.; DISEASE: Fibrosis of extraocular muscles, congenital, 3A (CFEOM3A) [MIM:600638]: A congenital ocular motility disorder marked by restrictive ophthalmoplegia affecting extraocular muscles innervated by the oculomotor and/or trochlear nerves. It is clinically characterized by anchoring of the eyes in downward gaze, ptosis, and backward tilt of the head. Congenital fibrosis of extraocular muscles type 3 presents as a non-progressive, autosomal dominant disorder with variable expression. Patients may be bilaterally or unilaterally affected, and their oculo-motility defects range from complete ophthalmoplegia (with the eyes fixed in a hypo- and exotropic position), to mild asymptomatic restrictions of ocular movement. Ptosis, refractive error, amblyopia, and compensatory head positions are associated with the more severe forms of the disorder. In some cases, the ocular phenotype is accompanied by additional features including developmental delay, corpus callosum agenesis, basal ganglia dysmorphism, facial weakness, polyneuropathy. {ECO:0000269|PubMed:20074521}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cortical dysplasia, complex, with other brain malformations 1 (CDCBM1) [MIM:614039]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Affected individuals have mild to severe mental retardation, strabismus, axial hypotonia, and spasticity. Brain imaging shows variable malformations of cortical development, including polymicrogyria, gyral disorganization, and fusion of the basal ganglia, as well as thin corpus callosum, hypoplastic brainstem, and dysplastic cerebellar vermis. Extraocular muscles are not involved. {ECO:0000269|PubMed:20829227}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expression is primarily restricted to central and peripheral nervous system. Greatly increased expression in most cancerous tissues. {ECO:0000269|PubMed:14736079, ECO:0000269|PubMed:20191564}.; unclassifiable (Anatomical System);lymph node;ovary;hypothalamus;sympathetic chain;colon;skin;skeletal muscle;uterus;pancreas;prostate;lung;frontal lobe;bone;visual apparatus;liver;testis;head and neck;kidney;spinal ganglion;brain;stomach;peripheral nerve; . . 0.70074 -0.758599262 13.32861524 8.39665 0.30705 TUBB3P1 . . . tubulin beta 3 class III pseudogene 1 . . . . . . . . . . . TUBB3P2 . . . tubulin beta 3 class III pseudogene 2 . . . . . . . . . . . TUBB4A 0.00305566312177654 0.815953999972262 0.180990336905961 tubulin beta 4A class IVa FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.; DISEASE: Dystonia 4, torsion, autosomal dominant (DYT4) [MIM:128101]: A form of torsion dystonia, a disease defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. 'Torsion' refers to the twisting nature of body movements, often affecting the trunk. DYT4 is characterized by onset in the second to third decade of progressive laryngeal dysphonia followed by the involvement of other muscles, such as the neck or limbs. Some patients develop an ataxic gait. {ECO:0000269|PubMed:23424103}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Leukodystrophy, hypomyelinating, 6 (HLD) [MIM:612438]: A neurologic disorder characterized by onset in infancy or early childhood of delayed motor development and gait instability, followed by extrapyramidal movement disorders, such as dystonia, choreoathetosis, rigidity, opisthotonus, and oculogyric crises, progressive spastic tetraplegia, ataxia, and, more rarely, seizures. Most patients have cognitive decline and speech delay, but some can function normally. Brain MRI shows a combination of hypomyelination, cerebellar atrophy, and atrophy or disappearance of the putamen. {ECO:0000269|PubMed:23582646}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Major isotype in brain, where it represents 46% of all beta-tubulins. In the brain, highest expression levels in the cerebellum, followed by putamen and white matter. Moderate levels in testis. Very low levels, if any, in other tissues. {ECO:0000269|PubMed:20191564, ECO:0000269|PubMed:23424103}.; ovary;salivary gland;sympathetic chain;colon;skin;retina;bone marrow;optic nerve;frontal lobe;iris;pituitary gland;testis;brain;unclassifiable (Anatomical System);nervous;hypothalamus;blood;lens;skeletal muscle;breast;lung;epididymis;placenta;hippocampus;visual apparatus;duodenum;kidney;mammary gland;aorta;cerebellum; amygdala;whole brain;occipital lobe;thalamus;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.38773 . -0.758599262 13.32861524 5.6735 0.21298 TUBB4AP1 . . . tubulin beta 4A class IVa pseudogene 1 . . . . . . . . . . . TUBB4B 0.929541173942078 0.0700913702353856 0.00036745582253624 tubulin beta 4B class IVb FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:20191564}.; lymphoreticular;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;thyroid;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;skeletal muscle;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; amygdala;whole brain;occipital lobe;thalamus;testis - interstitial;heart;hypothalamus;temporal lobe;subthalamic nucleus;testis - seminiferous tubule;fetal brain;prefrontal cortex;globus pallidus;testis;cingulate cortex;cerebellum; 0.23401 0.38765 -1.001120478 8.321538099 2.11873 0.06984 TUBB4BP1 . . . tubulin beta 4B class IVb pseudogene 1 . . . . . . . . . . . TUBB4BP2 . . . tubulin beta 4B class IVb pseudogene 2 . . . . . . . . . . . TUBB4BP3 . . . tubulin beta 4B class IVb pseudogene 3 . . . . . . . . . . . TUBB4BP4 . . . tubulin beta 4B class IVb pseudogene 4 . . . . . . . . . . . TUBB4BP5 . . . tubulin beta 4B class IVb pseudogene 5 . . . . . . . . . . . TUBB4BP6 . . . tubulin beta 4B class IVb pseudogene 6 . . . . . . . . . . . TUBB4BP7 . . . tubulin beta 4B class IVb pseudogene 7 . . . . . . . . . . . TUBB6 0.000511267490944529 0.686387511083913 0.313101221425142 tubulin beta 6 class V FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitous. Maximal expression in breast and lung, where it represents around 10% of all beta-tubulins. Largely decreased expression in most cancerous tissues. {ECO:0000269|PubMed:20191564}.; ovary;skin;retina;prostate;optic nerve;cochlea;endometrium;gum;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;placenta;head and neck;kidney;stomach;aorta; lung;heart; 0.62708 0.24932 -0.53631094 20.53550366 6.24501 0.23543 TUBB6P1 . . . tubulin beta 6 class V pseudogene 1 . . . . . . . . . . . TUBB7P . . . tubulin beta 7 pseudogene . . . . . 0.12412 0.21018 . . . . TUBB8 0.266953543410632 0.707835377145918 0.0252110794434492 tubulin beta 8 class VIII FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);mammary gland; . . . 0.150760231 64.51403633 82.28258 1.92577 TUBB8P1 . . . tubulin beta 8 class VIII pseudogene 1 . . . . . . . . . . . TUBB8P2 . . . tubulin beta 8 class VIII pseudogene 2 . . . . . . . . . . . TUBB8P3 . . . tubulin beta 8 class VIII pseudogene 3 . . . . . . . . . . . TUBB8P4 . . . tubulin beta 8 class VIII pseudogene 4 . . . . . . . . . . . TUBB8P5 . . . tubulin beta 8 class VIII pseudogene 5 . . . . . . . . . . . TUBB8P6 . . . tubulin beta 8 class VIII pseudogene 6 . . . . . . . . . . . TUBB8P7 . . . tubulin beta 8 class VIII pseudogene 7 . . . . . . . . . . . TUBB8P8 . . . tubulin beta 8 class VIII pseudogene 8 . . . . . . . . . . . TUBB8P9 . . . tubulin beta 8 class VIII pseudogene 9 . . . . . . . . . . . TUBB8P10 . . . tubulin beta 8 class VIII pseudogene 10 . . . . . . . . . . . TUBB8P11 . . . tubulin beta 8 class VIII pseudogene 11 . . . . . . . . . . . TUBB8P12 . . . tubulin beta 8 pseudogene 12 . . . . . . . . . . . TUBBP1 . . . tubulin beta pseudogene 1 . . . . . 0.12412 . . . . . TUBBP2 . . . tubulin beta pseudogene 2 . . . . . . . . . . . TUBBP3 . . . tubulin beta pseudogene 3 . . . . . . . . . . . TUBBP4 . . . tubulin beta pseudogene 4 . . . . . . . . . . . TUBBP5 . . . tubulin beta pseudogene 5 . . . unclassifiable (Anatomical System);prostate;lung;islets of Langerhans;testis;colon;stomach; superior cervical ganglion;testis - interstitial;globus pallidus;ciliary ganglion;skeletal muscle; . . . . . . TUBBP6 . . . tubulin beta class I pseudogene 6 . . . . . . . . . . . TUBBP7 . . . tubulin beta class I pseudogene 7 . . . . . . . . . . . TUBBP8 . . . tubulin beta class I pseudogene 8 . . . . . . . . . . . TUBBP9 . . . tubulin beta class I pseudogene 9 . . . . . . . . . . . TUBBP10 . . . tubulin beta class I pseudogene 10 . . . . . . . . . . . TUBBP11 . . . tubulin beta class I pseudogene 11 . . . . . . . . . . . TUBD1 0.000375248305025868 0.954949573720305 0.044675177974669 tubulin delta 1 FUNCTION: In the elongating spermatid it is associated with the manchette, a specialized microtubule system present during reshaping of the sperm head. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;skeletal muscle;retina;uterus;pancreas;prostate;whole body;lung;endometrium;nasopharynx;visual apparatus;liver;head and neck;spleen;germinal center;brain;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11727 0.13292 -0.203796826 38.81811748 4421.9007 13.32283 TUBE1 1.25133185446342e-05 0.828920417458341 0.171067069223114 tubulin epsilon 1 . . . . . 0.13271 0.22958 0.130533008 63.35810333 182.63578 2.93501 TUBG1 0.975922883842582 0.0240719835661931 5.13259122538024e-06 tubulin gamma 1 FUNCTION: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation.; DISEASE: Cortical dysplasia, complex, with other brain malformations 4 (CDCBM4) [MIM:615412]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Clinical features include early-onset seizures, microcephaly, spastic tetraplegia, and various malformations of cortical development, such as agyria, posterior or frontal pachygyria, thick cortex, and subcortical band heterotopia and thin corpus callosum in some patients. {ECO:0000269|PubMed:23603762}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;gall bladder;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;colon;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;thymus; testis - interstitial;testis - seminiferous tubule;testis; 0.64661 0.49283 -0.161524709 41.6430762 6.15866 0.23215 TUBG1P . . . tubulin gamma 1 pseudogene . . . . . . . . . . . TUBG2 0.00431001948765521 0.988474473231488 0.00721550728085737 tubulin gamma 2 FUNCTION: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation (By similarity). {ECO:0000250}.; . . smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;larynx;bone;pituitary gland;brain;bladder;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach; whole brain;medulla oblongata;superior cervical ganglion;occipital lobe;temporal lobe;pons;atrioventricular node;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.20090 . -0.66859065 15.76433121 4575.90405 13.57837 TUBGCP2 5.05146960755812e-05 0.998463433911449 0.00148605139247547 tubulin gamma complex associated protein 2 FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.; . TISSUE SPECIFICITY: Ubiquitously expressed.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;pons;trigeminal ganglion; 0.08373 0.27422 -0.87816671 10.58032555 234.93312 3.31234 TUBGCP3 0.952526133875611 0.0474738657384329 3.85955721026684e-10 tubulin gamma complex associated protein 3 FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.; . TISSUE SPECIFICITY: Ubiquitously expressed.; colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney; amygdala;dorsal root ganglion;testis - interstitial;superior cervical ganglion;atrioventricular node;skeletal muscle;skin;fetal liver;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cerebellum; 0.55085 0.13487 -1.50825116 3.503184713 46.90553 1.32419 TUBGCP4 0.00528348188155799 0.994671211073322 4.53070451199915e-05 tubulin gamma complex associated protein 4 FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.; . TISSUE SPECIFICITY: Ubiquitously expressed.; ovary;salivary gland;sympathetic chain;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;larynx;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07617 0.10529 -0.291981272 33.20358575 56.78603 1.51697 TUBGCP5 0.000126197167194763 0.999870484910822 3.31792198365831e-06 tubulin gamma complex associated protein 5 FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in heart and skeletal muscle and moderate levels in brain. {ECO:0000269|PubMed:14508708}.; developmental;adrenal medulla;colon;skin;uterus;whole body;frontal lobe;oesophagus;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;spinal cord;adrenal cortex;skeletal muscle;lung;placenta;liver;spleen;cervix;stomach;aorta; . . 0.11558 -0.771553417 13.15168672 114.31158 2.32936 TUBGCP6 5.08953781746856e-19 0.439969063571274 0.560030936428726 tubulin gamma complex associated protein 6 FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome. {ECO:0000269|PubMed:11694571}.; DISEASE: Microcephaly and chorioretinopathy, autosomal recessive, 1 (MCCRP1) [MIM:251270]: A syndrome characterized by microcephaly, cognitive impairment, underdeveloped retina and choroid, and epilepsy in some patients. The more anterior parts of the retina, near the periphery and pars plana, have a grayish hue and diminutive vasculature similar to retinopathy of prematurity. Visual impairment becomes evident during the first year of life. {ECO:0000269|PubMed:22279524}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;developmental;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;synovium;bone;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;blood;lens;pancreas;lung;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; . 0.08902 . -2.599674564 0.819768813 2392.99629 9.08228 TUFM 0.651456012209132 0.34829212491533 0.000251862875538318 Tu translation elongation factor, mitochondrial FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.; DISEASE: Combined oxidative phosphorylation deficiency 4 (COXPD4) [MIM:610678]: A mitochondrial disease resulting in neonatal lactic acidosis, rapidly progressive encephalopathy, severely decreased mitochondrial protein synthesis, and combined deficiency of mtDNA- related mitochondrial respiratory chain complexes. {ECO:0000269|PubMed:17160893}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;endometrium;gum;thyroid;iris;germinal center;bladder;brain;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;placenta;duodenum;kidney;stomach; whole brain;heart;liver;tumor;testis;kidney; 0.31599 0.15095 -0.402212257 26.7338995 38.69708 1.14626 TUFMP1 . . . Tu translation elongation factor, mitochondrial pseudogene 1 . . . . . . . . . . . TUFT1 0.0180800994157088 0.977491628622121 0.00442827196217042 tuftelin 1 FUNCTION: Involved in the mineralization and structural organization of enamel. {ECO:0000250|UniProtKB:P27628}.; . TISSUE SPECIFICITY: Present in the extracellular enamel and is mainly associated with the crystal component. {ECO:0000269|PubMed:1874744}.; ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;endometrium;larynx;testis;brain;unclassifiable (Anatomical System);heart;pharynx;blood;skeletal muscle;breast;lung;cornea;placenta;visual apparatus;hypopharynx;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;placenta;ciliary ganglion;trigeminal ganglion;skeletal muscle;skin; 0.42739 0.17140 0.374860183 75.43052607 365.81846 4.04777 TUG1 . . . taurine up-regulated 1 (non-protein coding) . . . . . . . . . . . TULP1 0.80790432015979 0.19208689949488 8.78034533047611e-06 tubby like protein 1 FUNCTION: Required for normal development of photoreceptor synapses. Required for normal photoreceptor function and for long- term survival of photoreceptor cells. Interacts with cytoskeleton proteins and may play a role in protein transport in photoreceptor cells (By similarity). Binds lipids, especially phosphatidylinositol 3-phosphate, phosphatidylinositol 4- phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 4,5-bisphosphate, phosphatidylinositol 3,4,5-bisphosphate, phosphatidylserine and phosphatidic acid (in vitro). Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages. {ECO:0000250, ECO:0000269|PubMed:16303976, ECO:0000269|PubMed:19837063}.; DISEASE: Leber congenital amaurosis 15 (LCA15) [MIM:613843]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:15024725, ECO:0000269|PubMed:17962469}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Retina-specific.; unclassifiable (Anatomical System);heart;colon;blood;fovea centralis;choroid;lens;skeletal muscle;skin;retina;uterus;optic nerve;lung;placenta;macula lutea;visual apparatus;pineal gland; superior cervical ganglion;trigeminal ganglion; 0.33573 0.15165 -0.042196577 50.49539986 623.59866 5.03722 TULP2 1.82654937164633e-07 0.963783935086782 0.0362158822582812 tubby like protein 2 . . TISSUE SPECIFICITY: Strongly expressed in testis. Also expressed in retina. Expressed in cancer cell lines. {ECO:0000269|PubMed:15905330, ECO:0000269|PubMed:9096357}.; unclassifiable (Anatomical System);medulla oblongata;prostate;lung;testis; testis - interstitial;testis - seminiferous tubule;testis; 0.07447 . 1.646168225 96.17834395 1047.80804 6.21357 TULP3 0.00103688890759594 0.987692794539096 0.0112703165533085 tubby like protein 3 FUNCTION: Negative regulator of the Shh signaling transduction pathway: recruited to primary cilia via association with the IFT complex A (IFT-A) and is required for recruitment of G protein- coupled receptor GPR161 to cilia, a promoter of PKA-dependent basal repression machinery in Shh signaling. Binds to phosphorylated inositide (phosphoinositide) lipids. Both IFT-A- and phosphoinositide-binding properties are required to regulate ciliary G protein-coupled receptor trafficking. Not involved in ciliogenesis. {ECO:0000269|PubMed:11375483, ECO:0000269|PubMed:20889716}.; . TISSUE SPECIFICITY: Expressed at high levels in testis, ovaries, thyroid, and spinal chord. {ECO:0000269|PubMed:9828123}.; unclassifiable (Anatomical System);cartilage;heart;ovary;colon;choroid;skin;retina;bone marrow;breast;uterus;lung;endometrium;bone;thyroid;placenta;pituitary gland;liver;testis;cervix;head and neck;spleen;kidney;brain;stomach; dorsal root ganglion;uterus corpus;superior cervical ganglion;cerebellum; 0.13117 0.10704 0.244401822 69.50931824 717.0672 5.31279 TULP3P1 . . . tubby like protein 3 pseudogene 1 . . . . . . . . . . . TULP4 0.99993680345815 6.31965413312598e-05 5.18605927437624e-13 tubby like protein 4 FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed mainly in the brain, skeletal muscle, testis and kidney.; . . 0.23566 . -2.528819961 0.896437839 581.49333 4.88756 TUNAR . . . TCL1 upstream neural differentiation-associated RNA . . . . . . . . . . . TUSC1 0.324671553271701 0.609883050463158 0.0654453962651407 tumor suppressor candidate 1 . . TISSUE SPECIFICITY: Widely expressed at low level. Expressed at higher level in testis, weakly expressed in muscle, colon, lung and spleen. Not detected in 3 non small cell lung carcinoma (NSCLC) cell lines with homozygous deletion of the 9p region, while it is down-regulated in 3 other tumor cell lines. {ECO:0000269|PubMed:15208665}.; islets of Langerhans;iris;stomach; . 0.06590 0.07711 . . 505.71623 4.61571 TUSC2 0.703033003634111 0.28083636532013 0.0161306310457588 tumor suppressor candidate 2 FUNCTION: May function as a tumor suppressor, inhibiting colony formation, causing G1 arrest and ultimately inducing apoptosis in homozygous 3p21.3 120-kb region-deficient cells.; . TISSUE SPECIFICITY: Strong expression in heart, lung, skeletal muscle, kidney, and pancreas, followed by brain and liver, lowest levels in placenta.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; whole brain;thalamus;occipital lobe;subthalamic nucleus;temporal lobe;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.27670 0.09420 . . 1.20885 0.03657 TUSC2P1 . . . tumor suppressor candidate 2 pseudogene 1 . . . . . . . . . . . TUSC3 0.00189876427347781 0.975434675466872 0.0226665602596499 tumor suppressor candidate 3 FUNCTION: Magnesium transporter (PubMed:19717468). May be involved in N-glycosylation through its association with N-oligosaccharyl transferase (PubMed:24685145). {ECO:0000269|PubMed:19717468, ECO:0000303|PubMed:12887896, ECO:0000303|PubMed:24685145}.; . TISSUE SPECIFICITY: Expressed in most non-lymphoid cells and tissues examined, including prostate, lung, liver, colon, heart, kidney and pancreas. {ECO:0000269|PubMed:12887896}.; ovary;sympathetic chain;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;cochlea;thyroid;bone;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;tongue;islets of Langerhans;hypothalamus;urinary;adrenal cortex;breast;pancreas;pia mater;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;head and neck;cervix;kidney;stomach; superior cervical ganglion;placenta;skeletal muscle; 0.64283 0.12531 -0.337894035 30.37272942 28.42817 0.91049 TUSC5 0.101235964074607 0.773035779026258 0.125728256899135 tumor suppressor candidate 5 FUNCTION: May be involved in fat metabolism. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at high levels in heart, mammary gland, adrenal gland, stomach, smooth muscle and skeletal muscle, and at lower levels in brain and lung. Strongly down-regulated in lung cancer tissues, due to hypermethylation of the corresponding locus. {ECO:0000269|PubMed:12660825}.; unclassifiable (Anatomical System);bone;testis;mammary gland;skeletal muscle; . . . 1.260404852 93.53031375 61.22738 1.59353 TUSC7 . . . tumor suppressor candidate 7 (non-protein coding) . . . . . . . . . . . TUSC8 . . . tumor suppressor candidate 8 (non-protein coding) . . . . . . . . . . . TUT1 9.985102139972e-06 0.999364715344987 0.000625299552873476 terminal uridylyl transferase 1, U6 snRNA-specific FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication- dependent histone mRNA degradation. {ECO:0000269|PubMed:16790842, ECO:0000269|PubMed:18288197, ECO:0000269|PubMed:21102410}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18288197}.; sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;lacrimal gland;tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.32181 0.07041 -0.837696902 11.45317292 152.84753 2.70425 TVP23A 2.04412659815965e-06 0.26846474172887 0.731533214144532 trans-golgi network vesicle protein 23 homolog A (S. cerevisiae) . . . . . 0.11731 0.06348 -0.383807564 27.41802312 53.44303 1.45258 TVP23B 0.42973287339102 0.56298094521232 0.00728618139666015 trans-golgi network vesicle protein 23 homolog B (S. cerevisiae) . . . . . 0.35088 0.10047 0.080983847 59.76055674 5.22673 0.19460 TVP23BP1 . . . TVP23B pseudogene 1 . . . . . . . . . . . TVP23BP2 . . . TVP23B pseudogene 2 . . . . . 0.05870 . . . . . TVP23C 0.000136737340853385 0.64209676601349 0.357766496645656 trans-golgi network vesicle protein 23 homolog C (S. cerevisiae) . . . . . 0.05870 . 0.661468037 84.4420854 560.48365 4.80890 TVP23C-CDRT4 0.00236229697309959 0.770130001006433 0.227507702020467 TVP23C-CDRT4 readthrough . . . . . . . 0.103030231 61.2762444 72.55013 1.77582 TVP23CP1 . . . TVP23C pseudogene 1 . . . . . . . . . . . TVP23CP2 . . . TVP23C pseudogene 2 . . . . . . . . . . . TWF1 0.00796369297166301 0.977658461234376 0.0143778457939606 twinfilin actin binding protein 1 FUNCTION: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at high levels in the colon, testis, ovary, prostate and lung. Expressed at lower levels in the brain, bladder and heart. Not detected in liver. {ECO:0000269|PubMed:7507208}.; ovary;sympathetic chain;skin;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;small intestine;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;mesenchyma;nasopharynx;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; superior cervical ganglion; 0.39130 0.18115 0.082802743 60.09082331 45.9514 1.30466 TWF1P1 . . . twinfilin 1 pseudogene 1 . . . . . . . . . . . TWF1P2 . . . twinfilin 1 pseudogene 2 . . . . . . . . . . . TWF2 0.857810163904333 0.142095417075915 9.44190197516269e-05 twinfilin actin binding protein 2 FUNCTION: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. May play a role in regulating the mature length of the middle and short rows of stereocilia (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). {ECO:0000269|PubMed:10406962}.; lymphoreticular;myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;iris;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;alveolus;duodenum;liver;cervix;spleen;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;heart;cingulate cortex;skeletal muscle; . . -0.80269335 12.23755603 40.69707 1.19218 TWIST1 0.182033891254288 0.645492774528812 0.1724733342169 twist family bHLH transcription factor 1 FUNCTION: Acts as a transcriptional regulator. Inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. This interaction probably involves the basic domains of both proteins. Also represses expression of proinflammatory cytokines such as TNFA and IL1B. Regulates cranial suture patterning and fusion. Activates transcription as a heterodimer with E proteins. Regulates gene expression differentially, depending on dimer composition. Homodimers induce expression of FGFR2 and POSTN while heterodimers repress FGFR2 and POSTN expression and induce THBS1 expression. Heterodimerization is also required for osteoblast differentiation. Represses the activity of the circadian transcriptional activator: NPAS2-ARNTL/BMAL1 heterodimer (By similarity). {ECO:0000250, ECO:0000269|PubMed:12553906}.; DISEASE: Robinow-Sorauf syndrome (RSS) [MIM:180750]: An autosomal dominant syndrome characterized by craniosynostosis, asymmetry of orbits, flat face, hypertelorism, a thin, long, and pointed nose, shallow orbits, strabismus, and broad great toes with a duplication of the distal phalanx. RSS is clinically similar to Saethre-Chotzen syndrome, with the most characteristic additional feature in Robinow-Sorauf syndrome being a bifid or partially duplicated hallux. {ECO:0000269|PubMed:10465122}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Craniosynostosis 1 (CRS1) [MIM:123100]: A primary abnormality of skull growth involving premature fusion of one or more cranial sutures. The growth velocity of the skull often cannot match that of the developing brain resulting in an abnormal head shape and, in some cases, increased intracranial pressure, which must be treated promptly to avoid permanent neurodevelopmental disability. {ECO:0000269|PubMed:17343269}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Subset of mesodermal cells.; ovary;salivary gland;developmental;intestine;colon;skin;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;pharynx;blood;lung;trabecular meshwork;visual apparatus;liver;head and neck;cervix;kidney;stomach; uterus corpus;adipose tissue;placenta;ciliary ganglion; 0.83742 0.49283 . . 13.95838 0.50625 TWIST2 0.443476734119021 0.455174131366675 0.101349134514304 twist family bHLH transcription factor 2 FUNCTION: Binds to the E-box consensus sequence 5'-CANNTG-3' as a heterodimer and inhibits transcriptional activation by MYOD1, MYOG, MEF2A and MEF2C. Also represses expression of proinflammatory cytokines such as TNFA and IL1B. Involved in postnatal glycogen storage and energy metabolism (By similarity). Inhibits the premature or ectopic differentiation of preosteoblast cells during osteogenesis, possibly by changing the internal signal transduction response of osteoblasts to external growth factors. {ECO:0000250, ECO:0000269|PubMed:11062344}.; DISEASE: Ablepharon-macrostomia syndrome (AMS) [MIM:200110]: A congenital ectodermal dysplasia characterized by absent eyelids, macrostomia, microtia, redundant skin, sparse hair, dysmorphic nose and ears, variable abnormalities of the nipples, genitalia, fingers, and hands, largely normal intellectual and motor development, and poor growth. {ECO:0000269|PubMed:26119818}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Barber-Say syndrome (BBRSAY) [MIM:209885]: A rare ectodermal dysplasia characterized by ectropion, macrostomia, ear abnormalities, broad nasal bridge, bulbous nose, redundant skin, hypertrichosis, dental abnormalities, and variable other features. {ECO:0000269|PubMed:26119818}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In the embryo, highly expressed in chondrogenic cells. In embryonic skin, expressed in the undifferentiated mesenchymal layer beneath the epidermis which later develops into the dermis. Expressed in early myeloid cells but not in lymphoid cells in the liver. Expression also detected in the secretory ependymal epithelium of the choroid plexus primordium. In the adult, expressed in secreting glandular tissues and tubules. {ECO:0000269|PubMed:11062344}.; . . . . . . 5.03888 0.18694 TWISTNB 0.309424388132866 0.672567773949258 0.0180078379178757 TWIST neighbor FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Through its association with RRN3/TIF-IA may be involved in recruitment of Pol I to rDNA promoters.; . TISSUE SPECIFICITY: Widely expressed. Expressed in all fetal and adult tissues tested, with highest expression in fetal lung, liver, and kidney, and low expression in all adult tissues. {ECO:0000269|PubMed:12438708}.; ovary;salivary gland;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;amnion;hypopharynx;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14338 0.12628 -0.404032746 26.53338051 60.1892 1.57562 TWSG1 0.890252416255217 0.108611381332338 0.00113620241244464 twisted gastrulation BMP signaling modulator 1 FUNCTION: May be involved in dorsoventral axis formation. Seems to antagonize BMP signaling by forming ternary complexes with CHRD and BMPs, thereby preventing BMPs from binding to their receptors. In addition to the anti-BMP function, also has pro-BMP activity, partly mediated by cleavage and degradation of CHRD, which releases BMPs from ternary complexes. May be an important modulator of BMP-regulated cartilage development and chondrocyte differentiation. May play a role in thymocyte development (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;sympathetic chain;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;skeletal muscle;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach;thymus; smooth muscle;cingulate cortex;skeletal muscle; 0.20271 0.30924 -0.139478553 43.29440906 44.01904 1.26377 TXK 1.24865833150559e-07 0.941009312336695 0.0589905627974721 TXK tyrosine kinase FUNCTION: Non-receptor tyrosine kinase that plays a redundant role with ITK in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T- cells and nonconventional NKT-cells. When antigen presenting cells (APC) activate T-cell receptor (TCR), a series of phosphorylation lead to the recruitment of TXK to the cell membrane, where it is phosphorylated at Tyr-420. Phosphorylation leads to TXK full activation. Contributes also to signaling from many receptors and participates in multiple downstream pathways, including regulation of the actin cytoskeleton. Like ITK, can phosphorylate PLCG1, leading to its localization in lipid rafts and activation, followed by subsequent cleavage of its substrates. In turn, the endoplasmic reticulum releases calcium in the cytoplasm and the nuclear activator of activated T-cells (NFAT) translocates into the nucleus to perform its transcriptional duty. With PARP1 and EEF1A1, TXK forms a complex that acts as a T-helper 1 (Th1) cell- specific transcription factor and binds the promoter of IFNG to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. Phosphorylates both PARP1 and EEF1A1. Phosphorylates also key sites in LCP2 leading to the up-regulation of Th1 preferred cytokine IL-2. Phosphorylates 'Tyr- 201' of CTLA4 which leads to the association of PI-3 kinase with the CTLA4 receptor. {ECO:0000269|PubMed:10523612, ECO:0000269|PubMed:11564877, ECO:0000269|PubMed:11859127, ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:9813138}.; . TISSUE SPECIFICITY: Expressed in T-cells and some myeloid cell lines. Expressed in Th1/Th0 cells with IFN-gamma-producing potential. {ECO:0000269|PubMed:10523612, ECO:0000269|PubMed:7951233}.; unclassifiable (Anatomical System);bile duct;lung;cartilage;placenta;liver;head and neck;germinal center;skeletal muscle;stomach; superior cervical ganglion; 0.06823 0.09804 -0.157884861 42.05590941 236.08157 3.32044 TXLNA 0.995925358284739 0.00407431628623453 3.25429026546369e-07 taxilin alpha FUNCTION: May be involved in intracellular vesicle traffic and potentially in calcium-dependent exocytosis in neuroendocrine cells.; . TISSUE SPECIFICITY: Ubiquitous, with much higher expression in heart, kidney, liver and pancreas. {ECO:0000269|PubMed:12558796}.; . . 0.30209 0.14229 -0.290161348 33.33923095 137.96459 2.55735 TXLNB 1.64577814159854e-16 0.0123116742995143 0.987688325700485 taxilin beta FUNCTION: Promotes motor nerve regeneration (By similarity). May be involved in intracellular vesicle traffic. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle.; unclassifiable (Anatomical System);lymph node;heart;urinary;blood;skin;skeletal muscle;uterus;whole body;lung;larynx;nasopharynx;placenta;liver;testis;head and neck;germinal center;brain;mammary gland; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12249 0.08773 1.003094668 90.77022883 3565.93486 11.54604 TXLNG 0.992209565527669 0.0077888485769145 1.58589541659541e-06 taxilin gamma FUNCTION: May be involved in intracellular vesicle traffic. Inhibits ATF4-mediated transcription, possibly by dimerizing with ATF4 to form inactive dimers that cannot bind DNA. May be involved in regulating bone mass density through an ATF4-dependent pathway. May be involved in cell cycle progression. {ECO:0000269|PubMed:15911876, ECO:0000269|PubMed:18068885}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at high level in heart and skeletal muscle. Expressed in brain, placenta, lung, liver, kidney and pancreas. {ECO:0000269|PubMed:15184072}.; . . 0.80114 0.11787 0.440999548 77.79547063 90.04959 2.04289 TXLNGY . . . taxilin gamma pseudogene, Y-linked . . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12815422, ECO:0000269|Ref.1}.; . . 0.14391 . . . . . TXN 0.417886376366376 0.547146489368091 0.0349671342655328 thioredoxin FUNCTION: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.; . . . . 0.34633 0.72850 0.013025609 54.62962963 7.01382 0.26271 TXN2 0.00554567802065394 0.717017712220615 0.277436609758732 thioredoxin 2 FUNCTION: Has an anti-apoptotic function and plays an important role in the regulation of mitochondrial membrane potential. Could be involved in the resistance to anti-tumor agents. Possesses a dithiol-reducing activity. {ECO:0000269|PubMed:12032145, ECO:0000269|PubMed:12080052}.; . TISSUE SPECIFICITY: Widely expressed in adult (at protein level) and fetal tissues. {ECO:0000269|PubMed:12032145, ECO:0000269|PubMed:12080052}.; ovary;skin;retina;bone marrow;prostate;endometrium;thyroid;iris;germinal center;bladder;brain;heart;pineal body;adrenal cortex;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; heart;adrenal gland;liver;globus pallidus;trigeminal ganglion;skeletal muscle; 0.30476 . -0.361761279 28.6329323 10.0685 0.36752 TXNDC2 2.94038807435751e-07 0.0934840177296368 0.906515688231556 thioredoxin domain containing 2 (spermatozoa) FUNCTION: Probably plays a regulatory role in sperm development. May participate in regulation of fibrous sheath (FS) assembly by supporting the formation of disulfide bonds during sperm tail morphogenesis. May also be required to rectify incorrect disulfide pairing and generate suitable pairs between the FS constituents. Can reduce disulfide bonds in vitro in the presence of NADP and thioredoxin reductase.; . TISSUE SPECIFICITY: Testis-specific. Only expressed during spermiogenesis, prominently in round and elongating spermatids. {ECO:0000269|PubMed:11399755}.; medulla oblongata;testis; testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.03196 . 1.313594923 94.04930408 3280.1048 10.93217 TXNDC5 1.78543371790755e-06 0.870710152124573 0.129288062441709 thioredoxin domain containing 5 (endoplasmic reticulum) FUNCTION: Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide- isomerase deficiency in yeast (By similarity). {ECO:0000250}.; . . . . . 0.25772 0.022122107 55.69120075 120.95129 2.39709 TXNDC8 0.835982582435059 0.160783993087656 0.00323342447728576 thioredoxin domain containing 8 (spermatozoa) FUNCTION: May be required for post-translational modifications of proteins required for acrosomal biogenesis. May act by reducing disulfide bonds within the sperm.; . TISSUE SPECIFICITY: Testis-specific. Only expressed during spermiogenesis, prominently in the Golgi apparatus of pachytene spermatocytes and round and elongated spermatids, with a transient localization in the developing acrosome of round spermatids (at protein level). {ECO:0000269|PubMed:15181017}.; . . 0.12147 . 0.659651797 84.35362114 1277.26865 6.72963 TXNDC9 0.223930350936401 0.739922266180211 0.0361473828833879 thioredoxin domain containing 9 FUNCTION: Significantly diminishes the chaperonin TCP1 complex ATPase activity, thus negatively impacts protein folding, including that of actin or tubulin. {ECO:0000269|PubMed:16415341}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;bone;testis;germinal center;brain;artery;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;tongue;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.49263 0.12902 0.679884223 84.81363529 221.99485 3.22142 TXNDC11 0.00317800786829343 0.996355498910718 0.000466493220989041 thioredoxin domain containing 11 FUNCTION: May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H(2)O(2) generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H(2)O(2) generation.; . TISSUE SPECIFICITY: Widely expressed at low level. Expressed at higher level in thyroid and prostate. {ECO:0000269|PubMed:15561711}.; ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;gum;bone;thyroid;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;tongue;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; ciliary ganglion; 0.46139 0.11807 -1.01227212 8.174097665 5666.45871 15.57325 TXNDC12 0.344869172542878 0.641401736899107 0.0137290905580154 thioredoxin domain containing 12 (endoplasmic reticulum) FUNCTION: Possesses significant protein thiol-disulfide oxidase activity. {ECO:0000269|PubMed:12761212}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14557066}.; . . 0.31977 0.14719 0.725794416 85.98136353 358.39658 4.01071 TXNDC12-AS1 . . . TXNDC12 antisense RNA 1 . . . . . . . . . . . TXNDC15 0.109182712654528 0.884407058824758 0.00641022852071377 thioredoxin domain containing 15 . . . myocardium;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; superior cervical ganglion;thyroid;atrioventricular node; 0.11967 0.10496 -0.271755481 34.31823543 77.32781 1.84760 TXNDC16 1.68997528709087e-07 0.959904560078095 0.040095270924376 thioredoxin domain containing 16 . . . unclassifiable (Anatomical System);medulla oblongata;lymph node;heart;ovary;islets of Langerhans;parathyroid;skin;breast;uterus;lung;endometrium;bone;placenta;visual apparatus;liver;testis;head and neck;germinal center;kidney;brain;stomach; testis - seminiferous tubule;skeletal muscle; 0.12410 0.09029 0.828538765 88.1104034 2422.57915 9.14565 TXNDC17 0.0355158954785338 0.828832321616041 0.135651782905425 thioredoxin domain containing 17 FUNCTION: Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide. {ECO:0000269|PubMed:14607843, ECO:0000269|PubMed:14607844}.; . TISSUE SPECIFICITY: Ubiquitously expressed in cell lines. {ECO:0000269|PubMed:14607844}.; ovary;salivary gland;intestine;colon;parathyroid;vein;skin;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach; . 0.08767 0.10353 0.169169615 65.33380514 32.09495 1.00741 TXNIP 0.252140354472324 0.746583930562447 0.0012757149652295 thioredoxin interacting protein FUNCTION: May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over- expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1). {ECO:0000269|PubMed:12821938, ECO:0000269|PubMed:17603038, ECO:0000269|PubMed:18541147, ECO:0000269|PubMed:21460850}.; . . . . 0.19338 0.29503 0.084621747 60.31493277 94.47804 2.09222 TXNL1 0.956025974452741 0.043951114322511 2.29112247481099e-05 thioredoxin like 1 FUNCTION: Active thioredoxin with a redox potential of about -250 mV. {ECO:0000269|PubMed:19349277}.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;germinal center;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;placenta;head and neck;kidney;stomach;aorta;cerebellum; whole brain;testis - interstitial;thyroid;testis;fetal thyroid; 0.48308 0.20506 0.103030231 61.2762444 16.30383 0.57770 TXNL1P1 . . . thioredoxin like 1 pseudogene 1 . . . . . . . . . . . TXNL4A 0.00154673666437753 0.447637326700266 0.550815936635356 thioredoxin like 4A FUNCTION: Essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes that are involved in spliceosome assembly. {ECO:0000269|PubMed:10610776}.; DISEASE: Burn-McKeown syndrome (BMKS) [MIM:608572]: A disease characterized by choanal atresia, sensorineural deafness, cardiac defects, and typical craniofacial dysmorphism consisting of narrow palpebral fissures, coloboma of the lower eyelids, prominent nose with high nasal bridge, short philtrum, cleft lip and/or palate, and large and protruding ears. Intellectual development is normal. {ECO:0000269|PubMed:25434003}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; amygdala;whole brain;medulla oblongata;superior cervical ganglion;thalamus;temporal lobe;testis;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex; 0.35428 0.12971 -0.075159878 47.78839349 3.51916 0.12868 TXNL4B 0.0173065222001966 0.716034877462563 0.26665860033724 thioredoxin like 4B FUNCTION: Essential role in pre-mRNA splicing. Required in cell cycle progression for S/G(2) transition. {ECO:0000269|PubMed:15161931}.; . . medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;hypothalamus;blood;lens;pia mater;lung;nasopharynx;placenta;macula lutea;liver;duodenum;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.15156 0.17270 0.21326276 67.71644256 60.17267 1.57530 TXNP1 . . . thioredoxin pseudogene 1 . . . . . . . . . . . TXNP2 . . . thioredoxin pseudogene 2 . . . . . . . . . . . TXNP3 . . . thioredoxin pseudogene 3 . . . . . . . . . . . TXNP4 . . . thioredoxin pseudogene 4 . . . . . . . . . . . TXNP5 . . . thioredoxin pseudogene 5 . . . . . . . . . . . TXNP6 . . . thioredoxin pseudogene 6 . . . . . . . . . . . TXNP7 . . . thioredoxin pseudogene 7 . . . . . . . . . . . TXNRD1 0.00233754717803129 0.994098867559644 0.00356358526232436 thioredoxin reductase 1 FUNCTION: Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid. {ECO:0000269|PubMed:15199063, ECO:0000269|PubMed:18042542, ECO:0000269|PubMed:8577704, ECO:0000269|PubMed:9774665}.; . TISSUE SPECIFICITY: Isoform 1 is expressed predominantly in Leydig cells (at protein level). Also expressed in ovary, spleen, heart, liver, kidney and pancreas and in a number of cancer cell lines. Isoform 4 is widely expressed with highest levels in kidney, testis, uterus, ovary, prostate, placenta and fetal liver. {ECO:0000269|PubMed:18042542, ECO:0000269|PubMed:8999974}.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;dura mater;spinal ganglion;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;pancreas;lung;pia mater;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; adipose tissue;smooth muscle;adrenal gland;placenta; 0.82882 0.23801 -0.865195027 10.79853739 36.5719 1.09652 TXNRD2 1.06916304756314e-08 0.758978014754118 0.241021974554252 thioredoxin reductase 2 FUNCTION: Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox- regulated cell signaling.; . TISSUE SPECIFICITY: Highly expressed in the prostate, ovary, liver, testis, uterus, colon and small intestine. Intermediate levels in brain, skeletal muscle, heart and spleen. Low levels in placenta, pancreas, thymus and peripheral blood leukocytes. According to PubMed:10608886, high levels in kidney, whereas according to PubMed:9923614, levels are low. {ECO:0000269|PubMed:10215850, ECO:0000269|PubMed:10608886, ECO:0000269|PubMed:9923614}.; medulla oblongata;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;kidney;stomach;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.14486 0.33725 0.626470967 83.55154518 4301.52381 13.05449 TXNRD3 . . . thioredoxin reductase 3 FUNCTION: Displays thioredoxin reductase, glutaredoxin and glutathione reductase activities. Catalyzes disulfide bond isomerization. Promotes disulfide bond formation between GPX4 and various sperm proteins and may play a role in sperm maturation by promoting formation of sperm structural components (By similarity). {ECO:0000250|UniProtKB:Q99MD6}.; . . . . 0.04733 0.10699 . . 317.95886 3.78571 TXNRD3NB 0.00177417484616752 0.475151997754288 0.523073827399545 thioredoxin reductase 3 neighbor . . TISSUE SPECIFICITY: Expressed in pancreas, esophagus, bone marrow and keratinocytes. {ECO:0000269|PubMed:15674732}.; . . . . 0.391453969 75.87284737 283.78176 3.60579 TYK2 0.00431448241977221 0.995683030071094 2.48750913371833e-06 tyrosine kinase 2 FUNCTION: Probably involved in intracellular signal transduction by being involved in the initiation of type I IFN signaling. Phosphorylates the interferon-alpha/beta receptor alpha chain. {ECO:0000269|PubMed:7526154}.; DISEASE: Immunodeficiency 35 (IMD35) [MIM:611521]: A primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and highly elevated serum IgE. {ECO:0000269|PubMed:17088085}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Observed in all cell lines analyzed. Expressed in a variety of lymphoid and non-lymphoid cell lines. {ECO:0000269|PubMed:2156206}.; lymphoreticular;myocardium;ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;blood;skeletal muscle;pancreas;lung;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; white blood cells;whole blood;skeletal muscle; 0.35072 0.67053 -0.497908112 21.86246756 1605.54982 7.41708 TYMP 0.000465858647806756 0.87040252374104 0.129131617611154 thymidine phosphorylase FUNCTION: May have a role in maintaining the integrity of the blood vessels. Has growth promoting activity on endothelial cells, angiogenic activity in vivo and chemotactic activity on endothelial cells in vitro. {ECO:0000269|PubMed:1590793}.; DISEASE: Mitochondrial DNA depletion syndrome 1, MNGIE type (MTDPS1) [MIM:603041]: A multisystem disease associated with mitochondrial dysfunction. It is clinically characterized by onset between the second and fifth decades of life, ptosis, progressive external ophthalmoplegia, gastrointestinal dysmotility (often pseudoobstruction), diffuse leukoencephalopathy, cachexia, peripheral neuropathy, and myopathy. {ECO:0000269|PubMed:12177387, ECO:0000269|PubMed:9924029}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;larynx;bone;thyroid;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;oral cavity;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; trigeminal ganglion; 0.15623 0.50943 . . 1202.19018 6.57049 TYMS 0.924544533248258 0.075366051141402 8.94156103403952e-05 thymidylate synthetase FUNCTION: Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. {ECO:0000269|PubMed:21876188}.; . . lymphoreticular;smooth muscle;ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; fetal liver;testis;tumor;bone marrow; 0.94142 0.61848 -0.163345027 41.24793583 6.14085 0.23168 TYMSOS . . . TYMS opposite strand . . . . . 0.06401 . . . . . TYR 7.26380826960726e-21 3.35189436773727e-05 0.999966481056323 tyrosinase FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6-dihydroxyindole to indole-5,6 quinone.; DISEASE: Albinism, oculocutaneous, 1A (OCA1A) [MIM:203100]: An autosomal recessive disorder in which the biosynthesis of melanin pigment is absent in skin, hair, and eyes. It is characterized by complete lack of tyrosinase activity due to production of an inactive enzyme. Patients present with a life-long absence of melanin pigment after birth, and manifest increased sensitivity to ultraviolet radiation with predisposition to skin cancer. Visual anomalies include decreased acuity, nystagmus, strabismus and photophobia. {ECO:0000269|PubMed:10571953, ECO:0000269|PubMed:10671066, ECO:0000269|PubMed:10987646, ECO:0000269|PubMed:11295837, ECO:0000269|PubMed:11858948, ECO:0000269|PubMed:1487241, ECO:0000269|PubMed:15146472, ECO:0000269|PubMed:1642278, ECO:0000269|PubMed:1899321, ECO:0000269|PubMed:1943686, ECO:0000269|PubMed:1970634, ECO:0000269|PubMed:22981120, ECO:0000269|PubMed:2342539, ECO:0000269|PubMed:23504663, ECO:0000269|PubMed:24934919, ECO:0000269|PubMed:7902671, ECO:0000269|PubMed:7955413, ECO:0000269|PubMed:8128955, ECO:0000269|PubMed:8644824, ECO:0000269|PubMed:9259202}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Albinism, oculocutaneous, 1B (OCA1B) [MIM:606952]: An autosomal recessive disorder in which the biosynthesis of melanin pigment is reduced in skin, hair, and eyes. It is characterized by partial lack of tyrosinase activity. Patients have white hair at birth that rapidly turns yellow or blond. They manifest the development of minimal-to-moderate amounts of cutaneous and ocular pigment. Some patients may have with white hair in the warmer areas (scalp and axilla) and progressively darker hair in the cooler areas (extremities). This variant phenotype is due to a loss of tyrosinase activity above 35-37 degrees C. {ECO:0000269|PubMed:10987646, ECO:0000269|PubMed:1900309, ECO:0000269|PubMed:1903591, ECO:0000269|PubMed:8128955}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);ovary;salivary gland;pharynx;colon;blood;fovea centralis;choroid;lens;skin;retina;breast;prostate;optic nerve;lung;thyroid;macula lutea;visual apparatus;liver;testis;kidney;brain;mammary gland;bladder; . 0.27943 0.89315 -0.951568548 9.271054494 2416.90647 9.13654 TYRL . . . tyrosinase-like (pseudogene) . . . unclassifiable (Anatomical System);lung;visual apparatus;testis;choroid;skin; . 0.17269 . . . . . TYRO3 0.761822542682681 0.2381767968867 6.60430618057233e-07 TYRO3 protein tyrosine kinase FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including TULP1 or GAS6. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of TYRO3 on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with PIK3R1 and thereby enhances PI3-kinase activity. Activates the AKT survival pathway, including nuclear translocation of NF-kappa-B and up-regulation of transcription of NF-kappa-B-regulated genes. TYRO3 signaling plays a role in various processes such as neuron protection from excitotoxic injury, platelet aggregation and cytoskeleton reorganization. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3. {ECO:0000269|PubMed:20546121}.; . TISSUE SPECIFICITY: Abundant in the brain and lower levels in other tissues.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;endometrium;synovium;bone;testis;brain;unclassifiable (Anatomical System);heart;adrenal cortex;lens;pancreas;lung;placenta;macula lutea;hippocampus;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; amygdala;dorsal root ganglion;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;cerebellum peduncles;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;testis;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.26568 0.24002 -0.817464788 11.97806086 1530.51507 7.27014 TYRO3P . . . TYRO3P protein tyrosine kinase pseudogene . . . . . . . . . . . TYROBP 0.485203146508796 0.492914074748594 0.0218827787426097 TYRO protein tyrosine kinase binding protein FUNCTION: Non-covalently associates with activating receptors of the CD300 family. Cross-linking of CD300-TYROBP complexes results in cellular activation. Involved for instance in neutrophil activation mediated by integrin.; DISEASE: Polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL) [MIM:221770]: Recessively inherited disease characterized by a combination of psychotic symptoms rapidly progressing to presenile dementia and bone cysts restricted to wrists and ankles. PLOSL has a global distribution, although most of the patients have been diagnosed in Finland and Japan, with an estimated population prevalence of 2x10(-6) in the Finns. {ECO:0000269|PubMed:10888890, ECO:0000269|PubMed:12370476}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at low levels in the early development of the hematopoietic system and in the promonocytic stage and at high levels in mature monocytes. Expressed in hematological cells and tissues such as peripheral blood leukocytes and spleen. Also found in bone marrow, lymph nodes, placenta, lung and liver. Expressed at lower levels in different parts of the brain especially in the basal ganglia and corpus callosum. {ECO:0000269|PubMed:11922939}.; ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;larynx;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; whole blood; 0.14095 0.31055 0.237127192 68.98443029 158.00999 2.74625 TYRP1 4.48055884907162e-21 2.52117897893201e-05 0.999974788210211 tyrosinase-related protein 1 FUNCTION: Oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid. May regulate or influence the type of melanin synthesized.; DISEASE: Albinism, oculocutaneous, 3 (OCA3) [MIM:203290]: An autosomal recessive disorder in which the biosynthesis of melanin pigment is reduced in skin, hair, and eyes. Tyrosinase activity is normal and patients have only moderate reduction of pigment. The eyes present red reflex on transillumination of the iris, dilution of color of iris, nystagmus and strabismus. Darker-skinned individuals have bright copper-red coloration of the skin and hair. {ECO:0000269|PubMed:16704458, ECO:0000269|PubMed:23504663}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Pigment cells.; . . 0.41193 0.10133 -0.262657925 34.93158764 175.42763 2.87993 TYS . . . sclerotylosis . . . . . . . . . . . TYSND1 0.0666400995988282 0.871294650189428 0.0620652502117437 trypsin domain containing 1 FUNCTION: Peroxisomal protease that mediates both the removal of the leader peptide from proteins containing a PTS2 target sequence and processes several PTS1-containing proteins. Catalyzes the processing of PTS1-proteins involved in the peroxisomal beta- oxidation of fatty acids. {ECO:0000269|PubMed:22002062}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;oesophagus;larynx;bone;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;epidermis;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14433 0.10866 . . 2151.59196 8.53099 TYW1 0.000457248889921904 0.999231544799873 0.000311206310204658 tRNA-yW synthesizing protein 1 homolog FUNCTION: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N- methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;cervix;spleen;kidney;mammary gland;stomach; . 0.12951 0.08688 -1.173870472 5.99197924 2883.67083 10.17398 TYW1B 8.1161283885492e-09 0.151185527810541 0.848814464073331 tRNA-yW synthesizing protein 1 homolog B FUNCTION: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N- methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach;thymus; . . . . . . . TYW1P1 . . . tRNA-yW synthesizing protein 1 homolog pseudogene 1 . . . . . . . . . . . TYW3 0.431871959845862 0.560956813898012 0.00717122625612646 tRNA-yW synthesizing protein 3 homolog FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA (By similarity). {ECO:0000250}.; . . . . 0.04354 0.07762 0.305084559 72.22811984 1979.18967 8.19593 TYW5 2.19729035112119e-07 0.456605703743519 0.543394076527446 tRNA-yW synthesizing protein 5 FUNCTION: tRNA hydroxylase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the hydroxylation of 7-(a-amino-a-carboxypropyl)wyosine (yW-72) into undermodified hydroxywybutosine (OHyW*). OHyW* being further transformed into hydroxywybutosine (OHyW) by LCMT2/TYW4. OHyW is a derivative of wybutosine found in higher eukaryotes. {ECO:0000269|PubMed:20739293}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;cochlea;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;pharynx;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.13470 0.11262 -0.183570861 39.95046001 463.19896 4.46102 U2AF1 0.986595630278487 0.0133983767433903 5.992978123182e-06 U2 small nuclear RNA auxiliary factor 1 FUNCTION: Plays a critical role in both constitutive and enhancer- dependent splicing by mediating protein-protein interactions and protein-RNA interactions required for accurate 3'-splice site selection. Recruits U2 snRNP to the branch point. Directly mediates interactions between U2AF2 and proteins bound to the enhancers and thus may function as a bridge between U2AF2 and the enhancer complex to recruit it to the adjacent intron. {ECO:0000269|PubMed:8647433}.; . . myocardium;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; whole brain;prostate;testis - interstitial;testis - seminiferous tubule;thyroid;testis;tumor;thymus; 0.30242 0.16971 -0.09720619 46.20193442 4.96492 0.18485 U2AF1L4 5.80258583719614e-07 0.136782466989173 0.863216952752243 U2 small nuclear RNA auxiliary factor 1-like 4 FUNCTION: RNA-binding protein that function as a pre-mRNA splicing factor. Plays a critical role in both constitutive and enhancer- dependent splicing by mediating protein-protein interactions and protein-RNA interactions required for accurate 3'-splice site selection. Acts by enhancing the binding of U2AF2 to weak pyrimidine tracts. Also participates in the regulation of alternative pre-mRNA splicing. Activates exon 5 skipping of PTPRC during T-cell activation; an event reversed by GFI1. Binds to RNA at the AG dinucleotide at the 3'-splice site (By similarity). Shows a preference for AGC or AGA (By similarity). {ECO:0000250|UniProtKB:Q8BGJ9}.; . TISSUE SPECIFICITY: Isoform 2 is widely expressed. Isoform 3 is highly expressed in heart, brain and lung, lower expressed in thymus and much lower expressed in peripheral blood leukocytes. {ECO:0000269|PubMed:17312947}.; lymphoreticular;ovary;colon;parathyroid;skin;bone marrow;uterus;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);trophoblast;heart;islets of Langerhans;blood;lens;lung;placenta;hippocampus;liver;spleen;kidney;stomach;cerebellum; . 0.08836 . -0.161524709 41.6430762 22.34982 0.75027 U2AF1L5 . . . U2 small nuclear RNA auxiliary factor 1-like 5 FUNCTION: Plays a critical role in both constitutive and enhancer- dependent splicing by mediating protein-protein interactions and protein-RNA interactions required for accurate 3'-splice site selection. Recruits U2 snRNP to the branch point. Directly mediates interactions between U2AF2 and proteins bound to the enhancers and thus may function as a bridge between U2AF2 and the enhancer complex to recruit it to the adjacent intron. {ECO:0000250|UniProtKB:Q01081}.; . . . . . . . . . . U2AF2 0.997188847416044 0.00281102105151915 1.31532437273433e-07 U2 small nuclear RNA auxiliary factor 2 FUNCTION: Necessary for the splicing of pre-mRNA. By recruiting PRPF19 and the PRP19C/Prp19 complex/NTC/Nineteen complex to the RNA polymerase II C-terminal domain (CTD), and thereby pre-mRNA, may couple transcription to splicing (PubMed:21536736). Induces cardiac troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates the TNNT2 exon 5 inclusion through competition with MBNL1. Binds preferentially to a single-stranded structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:19470458, ECO:0000269|PubMed:19574390, ECO:0000269|PubMed:21536736}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;spleen;kidney;mammary gland;stomach; superior cervical ganglion;testis;skeletal muscle; 0.42592 0.11016 -0.912929826 9.902099552 2.06422 0.06668 U2SURP 0.999999613278695 3.86721304745643e-07 5.14525961551042e-17 U2 snRNP-associated SURP domain containing . . . ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;lung;adrenal gland;nasopharynx;placenta;duodenum;kidney;stomach;aorta; amygdala;ciliary ganglion; . . -0.912929826 9.902099552 36.35679 1.08967 UACA 2.35035184982735e-17 0.542058225972484 0.457941774027516 uveal autoantigen with coiled-coil domains and ankyrin repeats FUNCTION: Regulates APAF1 expression and plays an important role in the regulation of stress-induced apoptosis. Promotes apoptosis by regulating three pathways, apoptosome up-regulation, LGALS3/galectin-3 down-regulation and NF-kappa-B inactivation. Regulates the redistribution of APAF1 into the nucleus after proapoptotic stress. Down-regulates the expression of LGALS3 by inhibiting NFKB1 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart, kidney and pancreas. Expressed in choroid, retina and epidermal melanocytes. Expressed in eye muscles and thyroid follicular cells. {ECO:0000269|PubMed:11162650, ECO:0000269|PubMed:15358194}.; smooth muscle;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;oesophagus;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;spinal cord;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.45292 0.10536 -0.519955994 20.95423449 448.02621 4.40250 UAP1 0.908075010378527 0.0919188964500452 6.09317142748346e-06 UDP-N-acetylglucosamine pyrophosphorylase 1 FUNCTION: Converts UDP and GlcNAc-1-P into UDP-GlcNAc, and UDP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P.; . TISSUE SPECIFICITY: Widely expressed. Isoform AGX1 is more abundant in testis than isoform AGX2, while isoform AGX2 is more abundant than isoform AGX1 in somatic tissue. Expressed at low level in placenta, muscle and liver.; medulla oblongata;colon;skin;bone marrow;uterus;prostate;cerebral cortex;endometrium;synovium;gum;bone;thyroid;pituitary gland;testis;brain;pineal gland;unclassifiable (Anatomical System);tongue;islets of Langerhans;hypothalamus;blood;skeletal muscle;bile duct;breast;pancreas;lung;mesenchyma;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion; 0.33949 0.14751 0.306902668 72.38145789 343.03943 3.92654 UAP1L1 0.00112977007873698 0.836502112257751 0.162368117663512 UDP-N-acetylglucosamine pyrophosphorylase 1 like 1 . . . unclassifiable (Anatomical System);ovary;islets of Langerhans;adrenal cortex;skin;bile duct;pancreas;lung;larynx;bone;iris;head and neck;spleen;brain; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.18866 . -0.224023033 37.4321774 2309.37221 8.90269 UBA1 0.999990741817615 9.25818226681037e-06 1.17687876532865e-13 ubiquitin like modifier activating enzyme 1 FUNCTION: Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin- proteasome system (PubMed:1606621, PubMed:1447181). Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP (PubMed:1447181). Essential for the formation of radiation- induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites (PubMed:22456334). {ECO:0000269|PubMed:1447181, ECO:0000269|PubMed:1606621, ECO:0000269|PubMed:22456334}.; DISEASE: Spinal muscular atrophy X-linked 2 (SMAX2) [MIM:301830]: A lethal infantile form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Clinical features include hypotonia, areflexia, and multiple congenital contractures. {ECO:0000269|PubMed:18179898, ECO:0000269|PubMed:23518311}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in erythrocytes (at protein level). Ubiquitous. {ECO:0000269|PubMed:1986373}.; lymphoreticular;smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;choroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;stomach;peripheral nerve;cerebellum; prefrontal cortex;parietal lobe; 0.52118 0.36073 -0.222203495 37.54423213 1096.01417 6.33409 UBA2 0.999673179363343 0.000326819943129516 6.93527809415012e-10 ubiquitin like modifier activating enzyme 2 FUNCTION: The heterodimer acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2. {ECO:0000269|PubMed:11451954, ECO:0000269|PubMed:11481243, ECO:0000269|PubMed:15660128, ECO:0000269|PubMed:17643372, ECO:0000269|PubMed:19443651, ECO:0000269|PubMed:20164921}.; . . lymphoreticular;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;placenta;amnion;head and neck;kidney;stomach;aorta; amygdala;testis - interstitial;testis - seminiferous tubule;tumor;testis; 0.95202 0.13631 -0.247889024 35.98726115 149.99248 2.67003 UBA3 0.967546957863583 0.032452953008099 8.91283182421157e-08 ubiquitin like modifier activating enzyme 3 FUNCTION: Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression. {ECO:0000269|PubMed:10207026, ECO:0000269|PubMed:12740388, ECO:0000269|PubMed:9694792}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10207026}.; ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;mesenchyma;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; amygdala;occipital lobe; 0.73328 0.13588 -0.736552314 13.93606983 19.00162 0.65602 UBA5 0.745375692202932 0.254527613438788 9.66943582807692e-05 ubiquitin like modifier activating enzyme 5 FUNCTION: E1-like enzyme which activates UFM1 and SUMO2. {ECO:0000269|PubMed:15071506, ECO:0000269|PubMed:18442052, ECO:0000269|PubMed:20368332}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16328888}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;adrenal cortex;lens;breast;pancreas;lung;mesenchyma;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;stomach; amygdala;superior cervical ganglion;occipital lobe;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex;skeletal muscle; 0.06323 0.08867 0.170987912 65.5579146 192.45042 3.00764 UBA6 0.932317516582033 0.0676824832269061 1.91060637703788e-10 ubiquitin like modifier activating enzyme 6 FUNCTION: Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin- E1 thioester and free AMP. Specific for ubiquitin, does not activate ubiquitin-like peptides. Differs from UBE1 in its specificity for substrate E2 charging. Does not charge cell cycle E2s, such as CDC34. Essential for embryonic development. Required for UBD/FAT10 conjugation. Isoform 2 may play a key role in ubiquitin system and may influence spermatogenesis and male fertility. {ECO:0000269|PubMed:15202508, ECO:0000269|PubMed:17597759, ECO:0000269|PubMed:17889673}.; . TISSUE SPECIFICITY: Widely expressed. Isoform 2 is predominantly expressed in testis with higher expression in adult testis than in fetal testis. {ECO:0000269|PubMed:15202508, ECO:0000269|PubMed:17597759}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;ganglion;endometrium;larynx;bone;thyroid;testis;germinal center;ciliary body;brain;bladder;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;spinal cord;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.41355 0.11164 -0.973616687 8.8995046 1758.06312 7.73733 UBA6-AS1 . . . UBA6 antisense RNA 1 (head to head) . . . . . . . . . . . UBA7 2.68227797741532e-14 0.391549208178417 0.608450791821556 ubiquitin like modifier activating enzyme 7 FUNCTION: Activates ubiquitin by first adenylating with ATP its C- terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin- E1 thioester and free AMP. Catalyzes the ISGylation of influenza A virus NS1 protein. {ECO:0000269|PubMed:16254333, ECO:0000269|PubMed:20133869}.; . TISSUE SPECIFICITY: Expressed in a variety of normal and tumor cell types, but is reduced in lung cancer cell lines.; myocardium;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;thyroid;bone;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;skeletal muscle;breast;lung;placenta;liver;head and neck;kidney;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;lymph node;globus pallidus;ciliary ganglion;white blood cells;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle; 0.08624 0.14468 0.249861693 69.66265629 390.46775 4.16147 UBA52 0.4468000697986 0.524538235250117 0.0286616949512834 ubiquitin A-52 residue ribosomal protein fusion product 1 FUNCTION: Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.; . . . . . 0.18619 -0.031067188 51.03798066 151.51995 2.69144 UBA52P1 . . . ubiquitin A-52 residue ribosomal protein fusion product 1 pseudogene 1 . . . . . . . . . . . UBA52P2 . . . ubiquitin A-52 residue ribosomal protein fusion product 1 pseudogene 2 . . . . . . . . . . . UBA52P3 . . . ubiquitin A-52 residue ribosomal protein fusion product 1 pseudogene 3 . . . . . . . . . . . UBA52P4 . . . ubiquitin A-52 residue ribosomal protein fusion product 1 pseudogene 4 . . . . . . . . . . . UBA52P5 . . . ubiquitin A-52 residue ribosomal protein fusion product 1 pseudogene 5 . . . . . . . . . . . UBA52P6 . . . ubiquitin A-52 residue ribosomal protein fusion product 1 pseudogene 6 . . . . . . . . . . . UBA52P7 . . . ubiquitin A-52 residue ribosomal protein fusion product 1 pseudogene 7 . . . . . . . . . . . UBA52P8 . . . ubiquitin A-52 residue ribosomal protein fusion product 1 pseudogene 8 . . . . . . . . . . . UBA52P9 . . . ubiquitin A-52 residue ribosomal protein fusion product 1 pseudogene 9 . . . . . . . . . . . UBAC1 0.865452586951363 0.134465915051248 8.14979973894882e-05 UBA domain containing 1 FUNCTION: Non-catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle. {ECO:0000269|PubMed:15531880, ECO:0000269|PubMed:15746103}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10857748}.; . . 0.16709 0.11733 -0.023789244 52.09365416 1879.00737 7.97309 UBAC2 0.11149235350166 0.882322867413606 0.00618477908473471 UBA domain containing 2 FUNCTION: Restricts trafficking of FAF2 from the endoplasmic reticulum to lipid droplets. {ECO:0000269|PubMed:23297223}.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;synovium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;skeletal muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;testis - interstitial;testis; 0.17973 0.12278 -0.516085732 21.20193442 46.72809 1.32088 UBAC2-AS1 . . . UBAC2 antisense RNA 1 . . . . . . . . . . . UBALD1 0.700158646161822 0.283270811263653 0.016570542574525 UBA like domain containing 1 . . . . . 0.21518 . 0.25917371 70.05779665 2776.98923 9.95318 UBALD2 0.262586852012457 0.638255864705121 0.0991572832824217 UBA like domain containing 2 . . . . . 0.31769 0.11031 . . 3.1619 0.11361 UBAP1 0.952984527092159 0.0468823528799404 0.000133120027900911 ubiquitin associated protein 1 FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Plays a role in the proteasomal degradation of ubiquitinated cell-surface proteins, such as EGFR and BST2. {ECO:0000269|PubMed:21757351, ECO:0000269|PubMed:22405001}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, brain, placenta, lung, liver, skeletal muscle and pancreas. {ECO:0000269|PubMed:11599797}.; lymphoreticular;ovary;umbilical cord;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;germinal center;brain;gall bladder;tonsil;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;developmental;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus;cerebellum; whole brain;thalamus;occipital lobe;subthalamic nucleus;olfactory bulb;spinal cord;prefrontal cortex;testis;caudate nucleus;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.40433 0.15629 -0.824740496 11.67728238 187.86755 2.97580 UBAP1L . . . ubiquitin associated protein 1 like . . . . . . . . . 124.10551 2.42417 UBAP2 0.989509350398503 0.0104906495558265 4.56705923901252e-11 ubiquitin associated protein 2 . . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;thyroid;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;liver;cervix;head and neck;spleen;kidney;mammary gland;stomach; testis - interstitial;testis - seminiferous tubule;adrenal gland;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.39707 0.08564 -0.944313493 9.394904459 2836.16606 10.06443 UBAP2L 0.999999873126418 1.26873581569769e-07 3.40722202595792e-18 ubiquitin associated protein 2 like FUNCTION: Plays an important role in the activity of long-term repopulating hematopoietic stem cells (LT-HSCs). {ECO:0000250|UniProtKB:Q80X50}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11230159}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;greater omentum;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);islets of Langerhans;muscle;pancreas;lung;placenta;hippocampus;hypopharynx;amnion;head and neck;kidney;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;cingulate cortex;skeletal muscle; 0.11769 0.11029 -1.109541557 6.782259967 61.03443 1.58905 UBASH3A 3.97256626321349e-07 0.944205183377376 0.0557944193659973 ubiquitin associated and SH3 domain containing A FUNCTION: Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors, EGFR and PDGFRB, on the cell surface. Exhibits negligigle protein tyrosine phosphatase activity at neutral pH. May act as a dominant-negative regulator of UBASH3B-dependent dephosphorylation. May inhibit dynamin-dependent endocytic pathways by functionally sequestering dynamin via its SH3 domain. {ECO:0000269|PubMed:15159412, ECO:0000269|PubMed:17382318, ECO:0000269|PubMed:18189269}.; . TISSUE SPECIFICITY: Highest expression of UBASH3A in tissues belonging to the immune system, including spleen, peripheral blood leukocytes, thymus and bone marrow. {ECO:0000269|PubMed:11281453, ECO:0000269|PubMed:15107835}.; unclassifiable (Anatomical System);prostate;thyroid;liver;spleen;thymus; . 0.15909 0.14549 -0.87816671 10.58032555 520.99741 4.66093 UBASH3B 0.988510645026986 0.0114893209246074 3.40484063577942e-08 ubiquitin associated and SH3 domain containing B FUNCTION: Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors and EGFR, on the cell surface. Exhibits tyrosine phosphatase activity toward several substrates including EGFR, FAK, SYK, and ZAP70. Down-regulates proteins that are dually modified by both protein tyrosine phosphorylation and ubiquitination. {ECO:0000269|PubMed:15159412, ECO:0000269|PubMed:17880946}.; . . ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;pharynx;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;cerebellum; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.15890 0.16704 -0.066061882 48.77919321 2192.08637 8.62380 UBB 0.620802082419808 0.346928263686245 0.0322696538939473 ubiquitin B FUNCTION: Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. {ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:19754430}.; . . lymphoreticular;ovary;umbilical cord;salivary gland;intestine;colon;parathyroid;skin;prostate;frontal lobe;bone;thyroid;testis;dura mater;brain;pineal gland;bladder;unclassifiable (Anatomical System);meninges;lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;spinal cord;muscle;adrenal cortex;pharynx;blood;bile duct;breast;pia mater;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;duodenum;cervix;kidney;stomach; . 0.88184 0.19444 -0.163345027 41.24793583 . . UBBP1 . . . ubiquitin B pseudogene 1 . . . . . . . . . . . UBBP2 . . . ubiquitin B pseudogene 2 . . . . . . . . . . . UBBP3 . . . ubiquitin B pseudogene 3 . . . . . . . . . . . UBBP4 0.0610682954000755 0.720252176633046 0.218679527966878 ubiquitin B pseudogene 4 . . . . . . . . . 3342.56634 11.07485 UBBP5 . . . ubiquitin B pseudogene 5 . . . . . . . . . . . UBC 0.704156666525431 0.292254881172663 0.00358845230190589 ubiquitin C FUNCTION: Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. {ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:19754430}.; . . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;cochlea;oesophagus;endometrium;gum;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;muscle;urinary;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; medulla oblongata;testis - interstitial;thalamus;superior cervical ganglion;olfactory bulb;temporal lobe;atrioventricular node;pons;skeletal muscle;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;parietal lobe; . . -0.80269335 12.23755603 8.43713 0.30824 UBD 0.0798957514124674 0.753926416502742 0.166177832084791 ubiquitin D FUNCTION: Ubiquitin-like protein modifier which can be covalently attached to target protein and subsequently leads to their degradation by the 26S proteasome, in a NUB1L-dependent manner. Probably functions as a survival factor. Conjugation ability activated by UBA6. Promotes the expression of the proteasome subunit beta type-9 (PSMB9/LMP2). Regulates TNF-alpha-induced and LPS-mediated activation of the central mediator of innate immunity NF-kappa-B by promoting TNF-alpha-mediated proteasomal degradation of ubiquitinated-I-kappa-B-alpha. Required for TNF-alpha-induced p65 nuclear translocation in renal tubular epithelial cells (RTECs). May be involved in dendritic cell (DC) maturation, the process by which immature dendritic cells differentiate into fully competent antigen-presenting cells that initiate T-cell responses. Mediates mitotic non-disjunction and chromosome instability, in long-term in vitro culture and cancers, by abbreviating mitotic phase and impairing the kinetochore localization of MAD2L1 during the prometaphase stage of the cell cycle. May be involved in the formation of aggresomes when proteasome is saturated or impaired. Mediates apoptosis in a caspase-dependent manner, especially in renal epithelium and tubular cells during renal diseases such as polycystic kidney disease and Human immunodeficiency virus (HIV)- associated nephropathy (HIVAN). {ECO:0000269|PubMed:15831455, ECO:0000269|PubMed:16495226, ECO:0000269|PubMed:16495380, ECO:0000269|PubMed:17889673, ECO:0000269|PubMed:18574467, ECO:0000269|PubMed:19028597, ECO:0000269|PubMed:19033385, ECO:0000269|PubMed:19166848, ECO:0000269|PubMed:19726511, ECO:0000269|PubMed:19959714}.; . TISSUE SPECIFICITY: Constitutively expressed in mature dendritic cells and B-cells. Mostly expressed in the reticuloendothelial system (e.g. thymus, spleen), the gastrointestinal system, kidney, lung and prostate gland. {ECO:0000269|PubMed:12730673, ECO:0000269|PubMed:9368598}.; . . . . 1.659136225 96.23142251 2922.2878 10.25799 UBDP1 . . . ubiquitin D pseudogene 1 . . . . . . . . . . . UBE2A 0.798143753788149 0.196241111920361 0.0056151342914893 ubiquitin conjugating enzyme E2 A FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11', as well as 'Lys-48'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA. {ECO:0000269|PubMed:16337599, ECO:0000269|PubMed:20061386}.; DISEASE: Mental retardation, X-linked, syndromic, Nascimento-type (MRXSN) [MIM:300860]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXSN features include dysmorphic facies, hirsutism, skin and nails abnormalities, obesity, speech anomalies and seizures. {ECO:0000269|PubMed:16909393, ECO:0000269|PubMed:20412111}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; amygdala;superior cervical ganglion;placenta;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.87860 0.12971 0.145304857 63.81221986 . . UBE2B 0.320977558728882 0.662551081331837 0.0164713599392803 ubiquitin conjugating enzyme E2 B FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA. Associates to the E3 ligase RAD18 to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys- 164'. May be involved in neurite outgrowth. {ECO:0000269|PubMed:16337599, ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:17130289, ECO:0000269|PubMed:1717990, ECO:0000269|PubMed:20061386}.; . . myocardium;ovary;sympathetic chain;substantia nigra;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;artery;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; whole brain;amygdala;occipital lobe;medulla oblongata;superior cervical ganglion;caudate nucleus;atrioventricular node;skeletal muscle;adrenal gland;placenta;prefrontal cortex;globus pallidus;whole blood;trigeminal ganglion;cingulate cortex;parietal lobe; 0.52020 0.16306 0.013025609 54.62962963 1.48948 0.05070 UBE2C 0.218752616276181 0.743431848990711 0.0378155347331077 ubiquitin conjugating enzyme E2 C FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit. {ECO:0000269|PubMed:15558010, ECO:0000269|PubMed:18485873, ECO:0000269|PubMed:19820702, ECO:0000269|PubMed:19822757, ECO:0000269|PubMed:20061386}.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;cochlea;larynx;bone;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);trophoblast;lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; superior cervical ganglion; 0.99131 0.23380 -0.251530012 35.42108988 328.42198 3.85259 UBE2CP1 . . . ubiquitin conjugating enzyme E2 C pseudogene 1 . . . . . . . . . . . UBE2CP2 . . . ubiquitin conjugating enzyme E2 C pseudogene 2 . . . . . . . . . . . UBE2CP3 . . . ubiquitin conjugating enzyme E2 C pseudogene 3 . . . . . . . . . . . UBE2CP4 . . . ubiquitin conjugating enzyme E2 C pseudogene 4 . . . . . . . . . . . UBE2CP5 . . . ubiquitin conjugating enzyme E2 C pseudogene 5 . . . . . . . . . . . UBE2D1 0.908884949778809 0.0904095475166473 0.00070550270454371 ubiquitin conjugating enzyme E2 D1 FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP- induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4. {ECO:0000269|PubMed:18042044, ECO:0000269|PubMed:18359941, ECO:0000269|PubMed:19103148, ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20061386}.; . TISSUE SPECIFICITY: Ubiquitous. Up-regulated in livers of iron- overloaded patients with hereditary hemochromatosis. {ECO:0000269|PubMed:12480712, ECO:0000269|PubMed:9362508}.; . . 0.92370 0.55859 0.035072054 56.2514744 3.2218 0.11612 UBE2D2 0.945312660180096 0.0544930630679882 0.000194276751915553 ubiquitin conjugating enzyme E2 D2 FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP- induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by DDX58/RIG-I in response to viral infection. Essential for viral activation of IRF3. {ECO:0000269|PubMed:10329681, ECO:0000269|PubMed:15280377, ECO:0000269|PubMed:18042044, ECO:0000269|PubMed:18359941, ECO:0000269|PubMed:18703417, ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20403326, ECO:0000269|PubMed:20525694}.; . . ovary;substantia nigra;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;kidney;stomach;thymus; whole brain;amygdala;dorsal root ganglion;occipital lobe;medulla oblongata;superior cervical ganglion;testis - interstitial;cerebellum peduncles;temporal lobe;caudate nucleus;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex;cerebellum; 0.50966 0.24974 0.101211609 60.95777306 1.23044 0.04195 UBE2D3 0.748203020257397 0.249558259744852 0.00223871999775102 ubiquitin conjugating enzyme E2 D3 FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA- linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML- NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction. {ECO:0000269|PubMed:10329681, ECO:0000269|PubMed:11743028, ECO:0000269|PubMed:12646252, ECO:0000269|PubMed:15247280, ECO:0000269|PubMed:15280377, ECO:0000269|PubMed:15496420, ECO:0000269|PubMed:16628214, ECO:0000269|PubMed:18284575, ECO:0000269|PubMed:18508924, ECO:0000269|PubMed:18515077, ECO:0000269|PubMed:18948756, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20347421, ECO:0000269|PubMed:21532592}.; . . myocardium;ovary;substantia nigra;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;brain;bladder;tonsil;gall bladder;cartilage;heart;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;greater omentum;breast;trabecular meshwork;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;atrium;oesophagus;larynx;bone;pituitary gland;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;placenta;testis;atrioventricular node;whole blood;trigeminal ganglion;skeletal muscle; . 0.14509 0.057118534 57.99716914 4.04317 0.14886 UBE2D3P1 . . . ubiquitin conjugating enzyme E2 D3 pseudogene 1 . . . . . . 0.14509 . . . . UBE2D3P2 . . . ubiquitin conjugating enzyme E2 D3 pseudogene 2 . . . . . . . . . . . UBE2D3P3 . . . ubiquitin conjugating enzyme E2 D3 pseudogene 3 . . . . . . . . . . . UBE2D3P4 . . . ubiquitin conjugating enzyme E2 D3 pseudogene 4 . . . . . . . . . . . UBE2D4 0.00231860847257596 0.766596480788987 0.231084910738437 ubiquitin conjugating enzyme E2 D4 (putative) FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11' and 'Lys-48'-linked polyubiquitination. {ECO:0000269|PubMed:20061386}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.17913 0.11262 0.125076652 62.7388535 54.20978 1.46968 UBE2DNL . . . ubiquitin conjugating enzyme E2 D N-terminal like (pseudogene) . . . . . . . . . . . UBE2E1 0.872957997407213 0.125383932287647 0.00165807030514026 ubiquitin conjugating enzyme E2 E1 FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination. {ECO:0000269|PubMed:16428300, ECO:0000269|PubMed:20061386}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;cerebellum;thymus; occipital lobe;fetal brain;spinal cord; 0.62873 0.11262 0.279402865 70.86577023 246.66235 3.38871 UBE2E1-AS1 . . . UBE2E1 antisense RNA 1 . . . . . . . . . . . UBE2E2 0.924393312463155 0.0751675165420738 0.000439170994770774 ubiquitin conjugating enzyme E2 E2 FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Catalyzes the ISGylation of influenza A virus NS1 protein. {ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20133869, ECO:0000269|PubMed:9371400}.; . . unclassifiable (Anatomical System);ovary;parathyroid;fovea centralis;choroid;lens;retina;uterus;optic nerve;whole body;placenta;thyroid;macula lutea;liver;amnion;testis;kidney;mammary gland;brain; whole brain;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.21690 . -0.119252484 44.53880632 1.33297 0.04711 UBE2E2-AS1 . . . UBE2E2 antisense RNA 1 (head to head) . . . . . . . . . . . UBE2E3 0.653907525579768 0.340310007564224 0.00578246685600772 ubiquitin conjugating enzyme E2 E3 FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest. {ECO:0000269|PubMed:10343118, ECO:0000269|PubMed:20061386}.; . TISSUE SPECIFICITY: Ubiquitously expressed at low levels. Highly expressed in skeletal muscle. {ECO:0000269|PubMed:10343118}.; . . 0.13746 . 0.057118534 57.99716914 3.39773 0.12365 UBE2E4P . . . ubiquitin conjugating enzyme E2 E4 pseudogene . . . . . . . . . . . UBE2F 0.950479184702081 0.0493692629943679 0.000151552303550581 ubiquitin conjugating enzyme E2 F (putative) FUNCTION: Accepts the ubiquitin-like protein NEDD8 from the UBA3- NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5. {ECO:0000269|PubMed:19250909}.; . TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:19250909}.; medulla oblongata;colon;vein;skin;retina;uterus;prostate;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;blood;skeletal muscle;breast;lung;nasopharynx;placenta;liver;alveolus;spleen;kidney;mammary gland;stomach;thymus; ciliary ganglion;bone marrow; 0.26014 0.12378 -0.163345027 41.24793583 4.06908 0.14909 UBE2F-SCLY . . . UBE2F-SCLY readthrough (NMD candidate) . . . . . . . . . . . UBE2FP1 . . . ubiquitin conjugating enzyme E2 F (putative) pseudogene 1 . . . . . . . . . . . UBE2FP2 . . . ubiquitin conjugating enzyme E2 F (putative) pseudogene 2 . . . . . . . . . . . UBE2FP3 . . . ubiquitin conjugating enzyme E2 F (putative) pseudogene 3 . . . . . . . . . . . UBE2G1 0.745694457175788 0.252001967685533 0.00230357513867944 ubiquitin conjugating enzyme E2 G1 FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 48'-, as well as 'Lys-63'-linked polyubiquitination. May be involved in degradation of muscle-specific proteins. Mediates polyubiquitination of CYP3A4. {ECO:0000269|PubMed:19103148, ECO:0000269|PubMed:20061386}.; . . . . 0.70845 0.18619 0.013025609 54.62962963 2.97356 0.10769 UBE2G2 0.247416499355309 0.72297777615621 0.029605724488481 ubiquitin conjugating enzyme E2 G2 FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 48'-linked polyubiquitination. Involved in endoplasmic reticulum- associated degradation (ERAD). {ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:22607976}.; . . myocardium;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;spinal cord;urinary;pharynx;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;cerebellum; occipital lobe;hypothalamus;white blood cells; 0.09403 0.15617 -0.141298762 42.87567823 2.07555 0.06736 UBE2H 0.970971739459398 0.0289880808256541 4.01797149479452e-05 ubiquitin conjugating enzyme E2 H FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'- and 'Lys-48'-linked polyubiquitination. Capable, in vitro, to ubiquitinate histone H2A. {ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:8132613}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; . 0.75415 0.29199 0.035072054 56.2514744 . . UBE2HP1 . . . ubiquitin conjugating enzyme E2 H pseudogene 1 . . . . . . . . . . . UBE2I 0.943944487319045 0.0558488219013743 0.000206690779580142 ubiquitin conjugating enzyme E2 I FUNCTION: Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly- SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at 'Lys-386'. {ECO:0000269|PubMed:11451954, ECO:0000269|PubMed:15809060, ECO:0000269|PubMed:17466333, ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:19744555, ECO:0000269|PubMed:20077568, ECO:0000269|PubMed:8668529}.; . TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, pancreas, kidney, liver, lung, placenta and brain. Also expressed in testis and thymus. {ECO:0000269|PubMed:8610150}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;cochlea;thyroid;iris;amniotic fluid;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;larynx;synovium;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus;cerebellum; prostate;superior cervical ganglion;placenta;testis;kidney;trigeminal ganglion;skeletal muscle;parietal lobe;thymus; 0.98729 0.47415 -0.09720619 46.20193442 4.71621 0.17051 UBE2J1 0.857925444410675 0.141980340898077 9.42146912485846e-05 ubiquitin conjugating enzyme E2 J1 FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD). {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:12082160, ECO:0000269|PubMed:22607976}.; . . . . 0.17226 0.13001 -0.315847836 31.68789809 507.09705 4.62085 UBE2J2 0.415938846926224 0.575988647550294 0.00807250552348238 ubiquitin conjugating enzyme E2 J2 FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD). {ECO:0000255|PROSITE-ProRule:PRU00388}.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;iris;germinal center;brain;tonsil;heart;cartilage;blood;lens;breast;epididymis;visual apparatus;macula lutea;alveolus;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis;ciliary ganglion; 0.10943 0.09401 -0.405853867 26.23260203 103.46629 2.19737 UBE2K 0.962613421415574 0.0373113440961004 7.52344883255089e-05 ubiquitin conjugating enzyme E2 K FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein- dependent degradation of RB1. {ECO:0000269|PubMed:10634809, ECO:0000269|PubMed:10675012, ECO:0000269|PubMed:16714285, ECO:0000269|PubMed:16868077, ECO:0000269|PubMed:17873885, ECO:0000269|PubMed:19906396, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:8702625}.; . TISSUE SPECIFICITY: Expressed in all tissues tested, including spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocytes, T-lymphocytes, monocytes, granulocytes and bone marrow mononuclear cells. Highly expressed in brain, with highest levels found in cortex and striatum and at lower levels in cerebellum and brainstem. {ECO:0000269|PubMed:10634809, ECO:0000269|PubMed:10675012, ECO:0000269|PubMed:8702625}.; lymphoreticular;myocardium;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;pharynx;blood;skeletal muscle;breast;lung;cornea;placenta;visual apparatus;hippocampus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;pons;trigeminal ganglion; 0.74930 0.12378 0.057118534 57.99716914 2.46627 0.09042 UBE2L1 . . . ubiquitin conjugating enzyme E2 L1 (pseudogene) . . . . . . . . . . . UBE2L2 . . . ubiquitin conjugating enzyme E2 L2 (pseudogene) . . . smooth muscle;umbilical cord;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;frontal lobe;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;trophoblast;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; . . . . . . . UBE2L3 0.778719690860565 0.214088993108409 0.00719131603102603 ubiquitin conjugating enzyme E2 L3 FUNCTION: Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down- regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis. {ECO:0000269|PubMed:10888878, ECO:0000269|PubMed:15367689, ECO:0000269|PubMed:17003263, ECO:0000269|PubMed:18946090, ECO:0000269|PubMed:19340006, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:21532592}.; . TISSUE SPECIFICITY: Ubiquitous, with highest expression in testis.; myocardium;ovary;sympathetic chain;skin;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;cerebellum;thymus; whole brain;amygdala;medulla oblongata;superior cervical ganglion;subthalamic nucleus;prefrontal cortex;globus pallidus;atrioventricular node;cingulate cortex;parietal lobe;cerebellum; 0.80978 0.26824 0.145304857 63.81221986 4.15003 0.15207 UBE2L4 . . . ubiquitin conjugating enzyme E2 L4 (pseudogene) . . . . . . . . . . . UBE2L5P . . . ubiquitin conjugating enzyme E2 L5, pseudogene . . . . . . . . . . . UBE2L6 0.0140103299116803 0.868904375520455 0.117085294567864 ubiquitin conjugating enzyme E2 L6 FUNCTION: Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3. {ECO:0000269|PubMed:15131269, ECO:0000269|PubMed:16428300, ECO:0000269|PubMed:20508617}.; . TISSUE SPECIFICITY: Present in natural killer cells (at protein level). {ECO:0000269|PubMed:16709802}.; ovary;umbilical cord;substantia nigra;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;adrenal cortex;pharynx;blood;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; subthalamic nucleus;medulla oblongata;fetal liver;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.05291 0.08091 -0.075159878 47.78839349 4.94118 0.18369 UBE2M 0.619518063416814 0.372684787922248 0.00779714866093828 ubiquitin conjugating enzyme E2 M FUNCTION: Accepts the ubiquitin-like protein NEDD8 from the UBA3- NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation. {ECO:0000269|PubMed:10207026, ECO:0000269|PubMed:15361859}.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;breast;pancreas;lung;epididymis;adrenal gland;placenta;macula lutea;liver;alveolus;head and neck;cervix;mammary gland;stomach; whole brain;amygdala;subthalamic nucleus;temporal lobe;prefrontal cortex;globus pallidus;pons;cingulate cortex; 0.32076 0.14229 0.125076652 62.7388535 5.92013 0.22302 UBE2MP1 . . . ubiquitin conjugating enzyme E2 M pseudogene 1 . . . . . . . . . . . UBE2N 0.787720767545003 0.205850442242684 0.00642879021231253 ubiquitin conjugating enzyme E2 N FUNCTION: The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes. {ECO:0000269|PubMed:10089880, ECO:0000269|PubMed:14562038, ECO:0000269|PubMed:19269966, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:21512573}.; . . medulla oblongata;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;nasopharynx;internal ear;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;cerebellum; amygdala;medulla oblongata;superior cervical ganglion;testis - interstitial;occipital lobe;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.44564 . -0.009020804 52.8544468 1.2898 0.04576 UBE2NL 0.0232238261133411 0.540769402991025 0.436006770895634 ubiquitin conjugating enzyme E2 N like (gene/pseudogene) . . TISSUE SPECIFICITY: Expressed in epididymis (at protein level). {ECO:0000269|PubMed:20736409}.; . . 0.11290 0.07070 0.25917371 70.05779665 76.46443 1.83470 UBE2NP1 . . . ubiquitin conjugating enzyme E2 N pseudogene 1 . . . . . . . . . . . UBE2O 0.999985318208959 1.46817909683516e-05 7.32165424823027e-14 ubiquitin conjugating enzyme E2 O FUNCTION: E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins (PubMed:23455153, PubMed:24703950). Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity (PubMed:23381138). Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis (PubMed:23455153). Mediates monoubiquitination at different sites of the nuclear localization signal (NLS) of BAP1, leading to cytoplasmic retention of BAP1. Also able to monoubiquitinate the NLS of other chromatin- associated proteins, such as INO80 and CXXC1, affecting their subcellular location (PubMed:24703950). Acts as a regulator of retrograde transport by assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to mediate 'Lys-63'-linked ubiquitination of WASH1, leading to promote endosomal F-actin assembly (PubMed:23452853). {ECO:0000269|PubMed:23381138, ECO:0000269|PubMed:23452853, ECO:0000269|PubMed:23455153, ECO:0000269|PubMed:24703950}.; . TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and heart. {ECO:0000269|PubMed:11311559}.; lymphoreticular;myocardium;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pineal body;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;skeletal muscle;cingulate cortex; 0.53648 0.11040 -0.813834387 12.05472989 3680.76091 11.80398 UBE2Q1 0.969363486984384 0.0306346264742841 1.88654133172492e-06 ubiquitin conjugating enzyme E2 Q1 FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins (Potential). May be involved in hormonal homeostasis in females. Involved in regulation of B4GALT1 cell surface expression, B4GALT1-mediated cell adhesion to laminin and embryoid body formation. {ECO:0000250|UniProtKB:Q7TSS2, ECO:0000255|PROSITE-ProRule:PRU00388}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11230159}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;tongue;pineal body;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;bile duct;pancreas;lung;adrenal gland;placenta;duodenum;head and neck;kidney;stomach;aorta;cerebellum; amygdala;testis - interstitial;thalamus;occipital lobe;subthalamic nucleus;testis - seminiferous tubule;cerebellum peduncles;testis;caudate nucleus;pons;parietal lobe; 0.47050 0.11809 -0.295622497 32.61972163 18.46014 0.63926 UBE2Q1-AS1 . . . UBE2Q1 antisense RNA 1 . . . . . . . . . . . UBE2Q2 0.00105603997354618 0.987958739915556 0.0109852201108978 ubiquitin conjugating enzyme E2 Q2 FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 48'-linked polyubiquitination. {ECO:0000269|PubMed:20061386}.; . TISSUE SPECIFICITY: Detected in hypopharyngeal head and neck squamous cell carcinoma, in tumor masses and invasive epithelium. {ECO:0000269|PubMed:16300736}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;larynx;gum;bone;thyroid;pituitary gland;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;pharynx;blood;lens;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;cervix;head and neck;kidney;mammary gland;aorta;stomach; dorsal root ganglion;amygdala;subthalamic nucleus;superior cervical ganglion;testis - seminiferous tubule;placenta;thyroid;prefrontal cortex;ciliary ganglion; 0.17480 0.09290 0.485092724 79.37603208 63.61765 1.63410 UBE2Q2L . . . ubiquitin conjugating enzyme E2 Q2 like . . . . . . . . . 10.56563 0.38350 UBE2Q2P1 . . . ubiquitin conjugating enzyme E2 Q2 pseudogene 1 . . . lung;larynx;muscle;head and neck;germinal center;mammary gland; . . . . . . . UBE2Q2P2 . . . ubiquitin conjugating enzyme E2 Q2 pseudogene 2 . . . . . . . . . . . UBE2Q2P4Y . . . ubiquitin conjugating enzyme E2 Q2 pseudogene 4, Y-linked . . . . . . . . . . . UBE2Q2P5Y . . . ubiquitin conjugating enzyme E2 Q2 pseudogene 5, Y-linked . . . . . . . . . . . UBE2Q2P6 . . . ubiquitin conjugating enzyme E2 Q2 pseudogene 6 . . . . . . . . . . . UBE2Q2P7 . . . ubiquitin conjugating enzyme E2 Q2 pseudogene 7 . . . . . . . . . . . UBE2Q2P8 . . . ubiquitin conjugating enzyme E2 Q2 pseudogene 8 . . . . . . . . . . . UBE2Q2P9 . . . ubiquitin conjugating enzyme E2 Q2 pseudogene 9 . . . . . . . . . . . UBE2Q2P10 . . . ubiquitin conjugating enzyme E2 Q2 pseudogene 10 . . . . . . . . . . . UBE2Q2P11 . . . ubiquitin conjugating enzyme E2 Q2 pseudogene 11 . . . . . . . . . . . UBE2Q2P12 . . . ubiquitin conjugating enzyme E2 Q2 pseudogene 12 . . . . . . . . . . . UBE2QL1 . . . ubiquitin conjugating enzyme E2 Q family like 1 FUNCTION: Probable E2 ubiquitin-protein ligase that catalyzes the covalent attachment of ubiquitin to target proteins. May facilitate the monoubiquitination and degradation of MTOR and CCNE1 through interaction with FBXW7. {ECO:0000269|PubMed:24000165}.; DISEASE: Note=A chromosomal aberration involving UBE2QL1 has been found in a sporadic case of renal cell carcinoma (RCC). Translocation t(5;19)(p15.3;q12). No gene is disrupted by the chromosome 19 breakpoint. {ECO:0000269|PubMed:24000165}.; . . . . . 0.145304857 63.81221986 1.11171 0.02941 UBE2R2 0.908519448838349 0.0907678078366061 0.000712743325044525 ubiquitin conjugating enzyme E2 R2 FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. May be involved in degradation of katenin. {ECO:0000269|PubMed:12037680, ECO:0000269|PubMed:20061386}.; . . myocardium;lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;germinal center;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;breast;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;pons; 0.72123 0.15869 -0.075159878 47.78839349 2.40151 0.08340 UBE2R2-AS1 . . . UBE2R2 antisense RNA 1 . . . . . . . . . . . UBE2S 0.801671664443433 0.192972333943984 0.0053560016125827 ubiquitin conjugating enzyme E2 S FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes 'Lys-11'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by specifically elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit. Also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is however unclear whether UBE2D1/UBCH5 acts as a E2 enzyme for the APC/C in vivo. Also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination. {ECO:0000269|PubMed:16819549, ECO:0000269|PubMed:19820702, ECO:0000269|PubMed:19822757, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20622874}.; . . myocardium;medulla oblongata;ovary;salivary gland;foreskin;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;duodenum;liver;cervix;kidney;mammary gland;stomach; . 0.34117 0.12167 -0.251530012 35.42108988 165.98556 2.81874 UBE2SP1 . . . ubiquitin conjugating enzyme E2 S pseudogene 1 . . . . . . . . . . . UBE2SP2 . . . ubiquitin conjugating enzyme E2 S pseudogene 2 . . . . . . . . . . . UBE2T 0.000369195253169518 0.836121755368233 0.163509049378597 ubiquitin conjugating enzyme E2 T FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA repair: acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCL and FANCI. May contribute to ubiquitination and degradation of BRCA1. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination. {ECO:0000269|PubMed:16916645, ECO:0000269|PubMed:17938197, ECO:0000269|PubMed:19111657, ECO:0000269|PubMed:19589784, ECO:0000269|PubMed:19887602, ECO:0000269|PubMed:20061386}.; DISEASE: Fanconi anemia complementation group T (FANCT) [MIM:616435]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:26046368}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.15496 0.04855 -0.119252484 44.53880632 20.96935 0.70929 UBE2U 7.80931252869977e-08 0.154410472595945 0.84558944931093 ubiquitin conjugating enzyme E2 U (putative) FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. {ECO:0000255|PROSITE-ProRule:PRU00388}.; . . . . 0.06187 0.07145 0.393270925 76.04977589 314.38752 3.77087 UBE2V1 0.0019545255342164 0.73314226399092 0.264903210474864 ubiquitin conjugating enzyme E2 V1 FUNCTION: Has no ubiquitin ligase activity on its own. The UBE2V1- UBE2N heterodimer catalyzes the synthesis of non-canonical poly- ubiquitin chains that are linked through Lys-63. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. Plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes. {ECO:0000269|PubMed:11057907, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:9305758, ECO:0000269|PubMed:9418904, ECO:0000269|PubMed:9580084, ECO:0000269|PubMed:9705497}.; . TISSUE SPECIFICITY: Highly expressed in thyroid, pancreas, spinal cord, lymph node, trachea, adrenal gland, bone marrow and pancreas. Detected at low levels in heart, breast, placenta, brain, liver, kidney, stomach and lung. {ECO:0000269|PubMed:9418904, ECO:0000269|PubMed:9705497}.; myocardium;umbilical cord;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;oral cavity;muscle;bile duct;pancreas;pia mater;lung;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;thymus; . . 0.13867 0.147123112 64.11299835 12.63303 0.46133 UBE2V1P1 . . . ubiquitin conjugating enzyme E2 V1 pseudogene 1 . . . . . . . . . . . UBE2V1P2 . . . ubiquitin conjugating enzyme E2 V1 pseudogene 2 . . . . . . . . . . . UBE2V1P3 . . . ubiquitin conjugating enzyme E2 V1 pseudogene 3 . . . . . . . . . . . UBE2V1P4 . . . ubiquitin conjugating enzyme E2 V1 pseudogene 4 . . . . . . . . . . . UBE2V1P5 . . . ubiquitin conjugating enzyme E2 V1 pseudogene 5 . . . . . . . . . . . UBE2V1P6 . . . ubiquitin conjugating enzyme E2 V1 pseudogene 6 . . . . . . . . . . . UBE2V1P7 . . . ubiquitin conjugating enzyme E2 V1 pseudogene 7 . . . . . . . . . . . UBE2V1P8 . . . ubiquitin conjugating enzyme E2 V1 pseudogene 8 . . . . . . . . . . . UBE2V1P9 . . . ubiquitin conjugating enzyme E2 V1 pseudogene 9 . . . . . . . . . . . UBE2V1P10 . . . ubiquitin conjugating enzyme E2 V1 pseudogene 10 . . . . . . . . . . . UBE2V1P11 . . . ubiquitin conjugating enzyme E2 V1 pseudogene 11 . . . . . . . . . . . UBE2V1P12 . . . ubiquitin conjugating enzyme E2 V1 pseudogene 12 . . . . . . . . . . . UBE2V2 0.10887932581952 0.776594594255212 0.114526079925268 ubiquitin conjugating enzyme E2 V2 FUNCTION: Has no ubiquitin ligase activity on its own. The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. {ECO:0000269|PubMed:10089880, ECO:0000269|PubMed:14562038, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:9705497}.; . TISSUE SPECIFICITY: Detected in placenta, colon, liver and skin. Detected at very low levels in most tissues. {ECO:0000269|PubMed:9199207, ECO:0000269|PubMed:9705497}.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;thyroid;testis;germinal center;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;spinal cord;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;liver;kidney;aorta;stomach; dorsal root ganglion;amygdala;trigeminal ganglion; 0.34474 0.17226 0.057118534 57.99716914 1.23583 0.04240 UBE2V2P1 . . . ubiquitin conjugating enzyme E2 V2 pseudogene 1 . . . . . . . . . . . UBE2V2P2 . . . ubiquitin conjugating enzyme E2 V2 pseudogene 2 . . . . . . . . . . . UBE2V2P3 . . . ubiquitin conjugating enzyme E2 V2 pseudogene 3 . . . . . . . . . . . UBE2V2P4 . . . ubiquitin conjugating enzyme E2 V2 pseudogene 4 . . . . . . . . . . . UBE2W 0.954557960872144 0.0453197592782473 0.000122279849608767 ubiquitin conjugating enzyme E2 W (putative) FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in degradation of misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Transfers ubiquitin in complex with RING/U-box type E3s that do not have active site cysteine residues to form thioester bonds with ubiquitin, and preferentially ubiquitinates the N-terminus of substrates, such as ATXN3, STUB1 and SUMO2. {ECO:0000269|PubMed:19111657, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:21229326, ECO:0000269|PubMed:23560854, ECO:0000269|PubMed:23696636}.; . TISSUE SPECIFICITY: Widely expressed, with highest expression in brain, liver, pancreas and heart. {ECO:0000269|PubMed:16368532}.; . . 0.63378 0.09451 0.12325821 62.38499646 115.21497 2.33430 UBE2WP1 . . . ubiquitin conjugating enzyme E2 W pseudogene 1 . . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;urinary;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach;aorta; . . . . . . . UBE2Z 0.927558729836687 0.0720471307896446 0.000394139373668794 ubiquitin conjugating enzyme E2 Z FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). Specific substrate for UBA6, not charged with ubiquitin by UBE1. May be involved in apoptosis regulation. {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:17464193, ECO:0000269|PubMed:17597759}.; . TISSUE SPECIFICITY: Widely expressed. Highly in placenta, pancreas, spleen and testis. {ECO:0000269|PubMed:17160626, ECO:0000269|PubMed:17597759}.; myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; superior cervical ganglion;occipital lobe;testis;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.37038 0.11809 -0.141298762 42.87567823 1.2844 0.04531 UBE3A 0.999576243958304 0.000423755777459054 2.64237474621981e-10 ubiquitin protein ligase E3A FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates. Several substrates have been identified including the RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the PML tumor suppressor, and the cell cycle regulator CDKN1B. Catalyzes the high-risk human papilloma virus E6-mediated ubiquitination of p53/TP53, contributing to the neoplastic progression of cells infected by these viruses. Additionally, may function as a cellular quality control ubiquitin ligase by helping the degradation of the cytoplasmic misfolded proteins. Finally, UBE3A also promotes its own degradation in vivo. Plays an important role in the regulation of the circadian clock: involved in the ubiquitination of the core clock component ARNTL/BMAL1, leading to its proteasomal degradation (PubMed:24728990). {ECO:0000269|PubMed:10373495, ECO:0000269|PubMed:19204938, ECO:0000269|PubMed:19233847, ECO:0000269|PubMed:19325566, ECO:0000269|PubMed:19591933, ECO:0000269|PubMed:22645313, ECO:0000269|PubMed:24728990}.; DISEASE: Angelman syndrome (AS) [MIM:105830]: A neurodevelopmental disorder characterized by severe motor and intellectual retardation, ataxia, frequent jerky limb movements and flapping of the arms and hands, hypotonia, seizures, absence of speech, frequent smiling and episodes of paroxysmal laughter, open-mouthed expression revealing the tongue. {ECO:0000269|PubMed:25212744, ECO:0000269|PubMed:9585605}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;amygdala;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;pia mater;cornea;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;amygdala;superior cervical ganglion;testis - interstitial;occipital lobe;cerebellum peduncles;caudate nucleus;atrioventricular node;pons;skeletal muscle;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.40803 0.47186 -0.558357437 19.54470394 36.43521 1.09167 UBE3AP1 . . . ubiquitin protein ligase E3A pseudogene 1 . . . . . . . . . . . UBE3AP2 . . . ubiquitin protein ligase E3A pseudogene 2 . . . . . . . . . . . UBE3B 0.00938770579237683 0.99061213140004 1.62807583749726e-07 ubiquitin protein ligase E3B FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12837265}.; ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;ciliary body;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;placenta;head and neck;kidney;stomach;thymus;cerebellum; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;caudate nucleus;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex; 0.19362 0.09343 -2.232421897 1.315168672 170.30974 2.84773 UBE3C 0.999999273217422 7.26782578385385e-07 4.84096054654441e-17 ubiquitin protein ligase E3C FUNCTION: E3 ubiquitin-protein ligase that accepts ubiquitin from the E2 ubiquitin-conjugating enzyme UBE2D1 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Can assemble unanchored poly-ubiquitin chains in either 'Lys-29'- or 'Lys-48'-linked polyubiquitin chains. Has preference for 'Lys-48' linkages. It can target itself for ubiquitination in vitro and may promote its own degradation in vivo. {ECO:0000269|PubMed:11278995, ECO:0000269|PubMed:12692129, ECO:0000269|PubMed:16341092, ECO:0000269|PubMed:16601690}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Detected at much lower levels in kidney and pancreas. {ECO:0000269|PubMed:11278995, ECO:0000269|PubMed:12692129, ECO:0000269|PubMed:9575161}.; myocardium;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;spinal cord;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;mammary gland;colon;parathyroid;choroid;vein;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta; superior cervical ganglion;testis;pons;skeletal muscle; 0.07681 0.22865 -1.059995566 7.537154989 43.92549 1.26229 UBE3D 9.57947053072492e-08 0.308939694116046 0.691060210089248 ubiquitin protein ligase E3D FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. {ECO:0000269|PubMed:15749827}.; . . . . 0.03959 0.07364 0.595326758 82.66100495 1251.76932 6.67868 UBE4A 0.937619432134248 0.0623805640712181 3.79453379895016e-09 ubiquitination factor E4A FUNCTION: Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases. May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase. Mediates 'Lys-48'-linked polyubiquitination of substrates. {ECO:0000250|UniProtKB:E9Q735, ECO:0000250|UniProtKB:P54860}.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;thyroid;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;cartilage;heart;tongue;islets of Langerhans;hypothalamus;oral cavity;spinal cord;urinary;adrenal cortex;blood;skeletal muscle;bile duct;breast;pia mater;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;occipital lobe;prefrontal cortex;trigeminal ganglion;cingulate cortex;parietal lobe; 0.20567 0.09900 -1.085675268 7.147912243 92.47287 2.06712 UBE4B 0.999987413556799 1.25864432003048e-05 4.16853367853818e-16 ubiquitination factor E4B FUNCTION: Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases. May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase. {ECO:0000250|UniProtKB:P54860, ECO:0000250|UniProtKB:Q9ES00}.; . TISSUE SPECIFICITY: Highest expression in ovary, testis, heart and skeletal muscle. Expression is low in colon, thymus and peripheral blood leukocytes. Almost undetectable in lung and spleen. {ECO:0000269|PubMed:11802788}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;iris;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.38841 0.13299 -1.390744555 4.305260675 766.39656 5.48285 UBFD1 0.839698364238153 0.15966251347105 0.000639122290797362 ubiquitin family domain containing 1 FUNCTION: May play a role as NF-kappa-B regulator. {ECO:0000269|PubMed:19285159}.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;spinal cord;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;cornea;placenta;head and neck;kidney;stomach;thymus; superior cervical ganglion;skeletal muscle; 0.13012 0.10863 0.014844891 54.94810097 48.04682 1.34806 UBFD1P1 . . . ubiquitin family domain containing 1 pseudogene 1 . . . . . . . . . . . UBIAD1 0.568905634331064 0.419348701476617 0.0117456641923186 UbiA prenyltransferase domain containing 1 FUNCTION: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform present at high concentrations in the brain, kidney and pancreas, and is required for endothelial cell development. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2- methyl-1,4-naphthoquinone (menadione; K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4. Also plays a role in cardiovascular development independently of MK-4 biosynthesis, by acting as a coenzyme Q10 biosyntetic enzyme: coenzyme Q10, also named ubiquinone, plays a important antioxidant role in the cardiovascular system. Mediates biosynthesis of coenzyme Q10 in the Golgi membrane, leading to protect cardiovascular tissues from NOS3/eNOS-dependent oxidative stress. {ECO:0000269|PubMed:20953171, ECO:0000269|PubMed:23374346}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11314041}.; . . 0.14477 0.18932 -0.115612493 45.12856806 35.97671 1.08055 UBL3 0.718099179817861 0.278790634114638 0.0031101860675015 ubiquitin like 3 . . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10375635}.; . . 0.36280 0.11809 0.035072054 56.2514744 3.32974 0.12182 UBL4A 0.275271317341126 0.633676552162419 0.0910521304964556 ubiquitin like 4A FUNCTION: Component of the BAT3 complex, a multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. The complex acts by facilitating TA proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins, and transfers them to ASNA1/TRC40 for targeting. {ECO:0000269|PubMed:20676083}.; . . . . 0.09087 0.26919 -0.053113545 49.38664779 1166.64172 6.49751 UBL4B 0.000847798204150755 0.338412216784501 0.660739985011348 ubiquitin like 4B . . . medulla oblongata;visual apparatus;testis;retina; . 0.12970 0.08895 0.082802743 60.09082331 23.63908 0.78312 UBL5 0.080158330255147 0.754264280081563 0.16557738966329 ubiquitin like 5 . . TISSUE SPECIFICITY: Ubiquitous. Highest level of expression in heart, skeletal muscle, kidney, liver, iris and lymphoblasts. {ECO:0000269|PubMed:11161819}.; ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;cerebral cortex;endometrium;thyroid;pituitary gland;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; thalamus;medulla oblongata;temporal lobe;testis; 0.11504 0.13588 0.101211609 60.95777306 1.20345 0.03545 UBL5P1 . . . ubiquitin like 5 pseudogene 1 . . . . . . . . . . . UBL5P2 . . . ubiquitin like 5 pseudogene 2 . . . . . . . . . . . UBL5P3 . . . ubiquitin like 5 pseudogene 3 . . . . . . . . . . . UBL5P4 . . . ubiquitin like 5 pseudogene 4 . . . . . . . . . . . UBL7 0.0277554399688677 0.960900771532654 0.0113437884984782 ubiquitin like 7 . . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, skeletal muscle, testis, thyroid and adrenal gland. {ECO:0000269|PubMed:12644319}.; lymphoreticular;medulla oblongata;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; temporal lobe;ciliary ganglion;pons;parietal lobe; 0.10918 0.08850 -0.448125345 24.19202642 54.54127 1.47716 UBL7-AS1 . . . UBL7 antisense RNA 1 (head to head) . . . . . . . . . . . UBLCP1 0.118128583459485 0.876273927384231 0.00559748915628495 ubiquitin like domain containing CTD phosphatase 1 FUNCTION: Dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation may prevent assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome. {ECO:0000269|PubMed:21949367}.; . TISSUE SPECIFICITY: Broadly expressed, with highest levels in placenta, lung, testis and ovary. Up-regulated in tumor tissues. {ECO:0000269|PubMed:15883030}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;hypopharynx;amnion;spleen;head and neck;kidney;mammary gland;stomach; amygdala;subthalamic nucleus;medulla oblongata;superior cervical ganglion;temporal lobe; 0.16797 0.11809 -0.251530012 35.42108988 6.91851 0.25728 UBN1 0.997776757027546 0.00222324284803839 1.24415696593879e-10 ubinuclein 1 FUNCTION: Acts as a novel regulator of senescence. Involved in the formation of senescence-associated heterochromatin foci (SAHF), which represses expression of proliferation-promoting genes. Binds to proliferation-promoting genes. May be required for replication- independent chromatin assembly. {ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:19029251}.; . TISSUE SPECIFICITY: Ubiquitous. Also expressed in numerous tumors and cancer cell lines. {ECO:0000269|PubMed:10725330, ECO:0000269|PubMed:19029251}.; lymphoreticular;smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;oesophagus;synovium;bone;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle;cerebellum; 0.09393 0.23300 -1.695874154 2.59495164 432.11496 4.33871 UBN2 0.998642622987556 0.00135737682782456 1.8461959158161e-10 ubinuclein 2 . . TISSUE SPECIFICITY: Expressed in several cell lines tested, including primary and transformed cell lines. {ECO:0000269|PubMed:19029251}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);heart;blood;breast;lung;placenta;visual apparatus;liver;hypopharynx;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; . 0.09822 -0.547447733 19.99882048 344.09079 3.93423 UBOX5 0.00178682505370842 0.898224761869817 0.0999884130764745 U-box domain containing 5 FUNCTION: May have a ubiquitin-protein ligase activity acting as an E3 ubiquitin-protein ligase or as an ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. {ECO:0000250|UniProtKB:Q925F4}.; . TISSUE SPECIFICITY: Expressed in liver, heart, brain, kidney and testis. {ECO:0000269|PubMed:11435423}.; ovary;colon;parathyroid;choroid;prostate;bone;testis;pineal gland;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;hippocampus;visual apparatus;liver;spleen;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;cerebellum peduncles;globus pallidus;trigeminal ganglion; 0.35016 . -0.400392389 26.85185185 193.14886 3.01208 UBOX5-AS1 . . . UBOX5 antisense RNA 1 . . . . . . . . . . . UBP1 0.999799486559086 0.0002005132299603 2.10953242062965e-10 upstream binding protein 1 (LBP-1a) FUNCTION: Functions as a transcriptional activator in a promoter context-dependent manner. Modulates the placental expression of CYP11A1. Involved in regulation of the alpha-globin gene in erythroid cells. Activation of the alpha-globin promoter in erythroid cells is via synergistic interaction with TFCP2 (By similarity). Involved in regulation of the alpha-globin gene in erythroid cells. Binds strongly to sequences around the HIV-1 initiation site and weakly over the TATA-box. Represses HIV-1 transcription by inhibiting the binding of TFIID to the TATA-box. {ECO:0000250, ECO:0000269|PubMed:10644752, ECO:0000269|PubMed:2006421, ECO:0000269|PubMed:8114710}.; . TISSUE SPECIFICITY: Expressed in adrenal tissue, JEG-3, NCI-H295A, Hep-G2 and HeLa cell lines. {ECO:0000269|PubMed:10644752}.; ovary;salivary gland;developmental;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;trabecular meshwork;placenta;visual apparatus;hippocampus;amnion;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum; superior cervical ganglion; 0.79174 0.13070 -0.22584292 37.32012267 4409.02862 13.28009 UBQLN1 0.998753261709901 0.00124672017769506 1.81124038899727e-08 ubiquilin 1 FUNCTION: Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin- proteasome system (UPS), autophagy and endoplasmic reticulum- associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome (PubMed:15147878). Plays a role in the ERAD pathway via its interaction with ER-localized proteins UBXN4, VCP and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome (PubMed:19822669, PubMed:18307982). Isoform 1, isoform 2 and isoform 3 play a role in unfolded protein response (UPR) by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5 and PDIA2 during ER stress (PubMed:18953672). Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy- related protein LC3 from the cytosolic form LC3-I to the membrane- bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome- lysosome fusion (PubMed:19148225, PubMed:20529957, PubMed:23459205). Negatively regulates the TICAM1/TRIF-dependent toll-like receptor signaling pathway by decreasing the abundance of TICAM1 via the autophagic pathway (PubMed:21695056). Isoform 1 and isoform 3 play a key role in the regulation of the levels of PSEN1 by targeting its accumulation to aggresomes which may then be removed from cells by autophagocytosis (PubMed:21143716). Promotes the ubiquitination and lysosomal degradation of ORAI1, consequently downregulating the ORAI1-mediated Ca2+ mobilization (PubMed:23307288). Suppresses the maturation and proteasomal degradation of amyloid beta A4 protein (A4) by stimulating the lysine 63 (K63)-linked polyubiquitination. Delays the maturation of A4 by sequestering it in the Golgi apparatus and preventing its transport to the cell surface for subsequent processing (By similarity). {ECO:0000250|UniProtKB:Q9JJP9, ECO:0000269|PubMed:18307982, ECO:0000269|PubMed:18953672, ECO:0000269|PubMed:19148225, ECO:0000269|PubMed:19822669, ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:21143716, ECO:0000269|PubMed:21695056, ECO:0000269|PubMed:23307288, ECO:0000269|PubMed:23459205, ECO:0000303|PubMed:15147878}.; . TISSUE SPECIFICITY: Brain (at protein level) (PubMed:18953672). Ubiquitous. Highly expressed throughout the brain; detected in neurons and in neuropathological lesions, such as neurofibrillary tangles and Lewy bodies. Highly expressed in heart, placenta, pancreas, lung, liver, skeletal muscle and kidney. {ECO:0000269|PubMed:11076969, ECO:0000269|PubMed:11853878, ECO:0000269|PubMed:18953672}.; ovary;substantia nigra;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;blood;lens;breast;trabecular meshwork;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;head and neck;kidney;stomach; . 0.49245 0.31063 -0.314027422 31.9297004 45.11361 1.28969 UBQLN1P1 . . . ubiquilin 1 pseudogene 1 . . . . . . . . . . . UBQLN2 0.804317268481036 0.190515794994678 0.0051669365242861 ubiquilin 2 FUNCTION: Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin- proteasome system (UPS), autophagy and the endoplasmic reticulum- associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome (PubMed:10983987). Plays a role in the ERAD pathway via its interaction with ER-localized proteins FAF2/UBXD8 and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome (PubMed:24215460, PubMed:18307982). Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy-related protein LC3 from the cytosolic form LC3-I to the membrane-bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion (PubMed:19148225, PubMed:20529957). Negatively regulates the endocytosis of GPCR receptors: AVPR2 and ADRB2, by specifically reducing the rate at which receptor- arrestin complexes concentrate in clathrin-coated pits (CCPs) (PubMed:18199683). {ECO:0000269|PubMed:10983987, ECO:0000269|PubMed:18199683, ECO:0000269|PubMed:18307982, ECO:0000269|PubMed:19148225, ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:24215460}.; DISEASE: Amyotrophic lateral sclerosis 15, with or without frontotemporal dementia (ALS15) [MIM:300857]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. Patients with ALS15 may develop frontotemporal dementia. {ECO:0000269|PubMed:21857683, ECO:0000269|PubMed:22560112, ECO:0000269|PubMed:22717235, ECO:0000269|PubMed:22892309, ECO:0000269|PubMed:24215460, ECO:0000269|PubMed:25616961}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pineal body;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;cerebellum; whole brain;amygdala;subthalamic nucleus;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;prefrontal cortex;globus pallidus;pons;cerebellum; 0.37074 0.10627 -0.361761279 28.6329323 9.43842 0.34775 UBQLN3 0.00382806762177032 0.851063767101006 0.145108165277224 ubiquilin 3 . . TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:10831842}.; unclassifiable (Anatomical System);medulla oblongata;heart;testis; . 0.16565 0.08202 0.780798785 87.24345364 2379.80965 9.05361 UBQLN4 0.997522419654586 0.00247748369336297 9.66520508368834e-08 ubiquilin 4 FUNCTION: Plays a role in the regulation of protein degradation via the ubiquitin-proteasome system (UPS). Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome (Ref. 6). Plays a role in the regulation of the proteasomal degradation of non-ubiquitinated GJA1 (By similarity). Acts as an adapter protein that recruits UBQLN1 to the autophagy machinery. Mediates the association of UBQLN1 with autophagosomes and the autophagy-related protein LC3 (MAP1LC3A/B/C) and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion (PubMed:23459205). {ECO:0000250|UniProtKB:Q99NB8, ECO:0000269|PubMed:15280365, ECO:0000269|PubMed:23459205}.; . TISSUE SPECIFICITY: Highly expressed in pancreas, kidney, skeletal muscle, heart and throughout the brain, and at lower levels in placenta, lung and liver. {ECO:0000269|PubMed:11001934}.; . . 0.27058 0.13363 0.062575634 58.74026893 4087.61153 12.68896 UBQLN4P1 . . . ubiquilin 4 pseudogene 1 . . . . . . . . . . . UBQLN4P2 . . . ubiquilin 4 pseudogene 2 . . . . . . . . . . . UBQLNL 3.52672263535128e-09 0.0502680197347561 0.949731976738521 ubiquilin-like . . . . . 0.12679 . 1.868508992 97.20452937 867.58571 5.73488 UBR1 0.319889980799525 0.680110019199786 6.88471774870929e-13 ubiquitin protein ligase E3 component n-recognin 1 FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. May be involved in pancreatic homeostasis. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth. {ECO:0000269|PubMed:15548684, ECO:0000269|PubMed:16311597, ECO:0000269|PubMed:20298436, ECO:0000269|PubMed:20835242}.; DISEASE: Johanson-Blizzard syndrome (JBS) [MIM:243800]: This disorder includes congenital exocrine pancreatic insufficiency, multiple malformations such as nasal wing aplasia, and frequent mental retardation. Pancreas of individuals with JBS do not express UBR1 and show intrauterine-onset destructive pancreatitis. {ECO:0000269|PubMed:16311597}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Broadly expressed, with highest levels in skeletal muscle, kidney and pancreas. Present in acinar cells of the pancreas (at protein level). {ECO:0000269|PubMed:15548684, ECO:0000269|PubMed:16311597, ECO:0000269|PubMed:9653112}.; unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;retina;uterus;bile duct;prostate;pancreas;frontal lobe;bone;thyroid;placenta;visual apparatus;liver;testis;spleen;kidney;brain;mammary gland;bladder; dorsal root ganglion;superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.65512 0.19438 -0.630196893 16.8141071 569.25891 4.84060 UBR2 0.999999880132158 1.19867842240771e-07 8.33763066000186e-24 ubiquitin protein ligase E3 component n-recognin 2 FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth. {ECO:0000269|PubMed:15548684, ECO:0000269|PubMed:20298436, ECO:0000269|PubMed:20835242}.; . TISSUE SPECIFICITY: Broadly expressed, with highest levels in skeletal muscle, kidney and pancreas. Present in acinar cells of the pancreas (at protein level). {ECO:0000269|PubMed:15548684, ECO:0000269|PubMed:16311597}.; . . 0.72806 0.25871 -1.365077992 4.5175749 3342.51324 11.07201 UBR3 0.999549123627985 0.000450876359430661 1.25840271488024e-11 ubiquitin protein ligase E3 component n-recognin 3 (putative) FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Does not bind to proteins bearing specific N- terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). {ECO:0000250}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;skin;bone marrow;uterus;prostate;frontal lobe;bone;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;hypothalamus;pharynx;blood;skeletal muscle;greater omentum;bile duct;breast;lung;cornea;trabecular meshwork;placenta;visual apparatus;liver;duodenum;spleen;kidney;mammary gland; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.35557 . -1.043396569 7.71408351 643.90567 5.09856 UBR4 1 2.42661308789616e-23 4.94162390499645e-62 ubiquitin protein ligase E3 component n-recognin 4 FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Together with clathrin, forms meshwork structures involved in membrane morphogenesis and cytoskeletal organization. Regulates integrin-mediated signaling. May play a role in activation of FAK in response to cell-matrix interactions. Mediates ubiquitination of ACLY, leading to its subsequent degradation. {ECO:0000269|PubMed:16214886, ECO:0000269|PubMed:23932781}.; . . . . 0.25731 0.12662 -7.504914615 0.011795235 2894.47418 10.19251 UBR5 1 4.65471298714032e-20 3.53016124564021e-49 ubiquitin protein ligase E3 component n-recognin 5 FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). Involved in maturation and/or transcriptional regulation of mRNA by activating CDK9 by polyubiquitination. May play a role in control of cell cycle progression. May have tumor suppressor function. Regulates DNA topoisomerase II binding protein (TopBP1) in the DNA damage response. Plays an essential role in extraembryonic development. Ubiquitinates acetylated PCK1. Also acts as a regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'- linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes. {ECO:0000250, ECO:0000269|PubMed:21127351, ECO:0000269|PubMed:21726808, ECO:0000269|PubMed:22884692}.; . TISSUE SPECIFICITY: Widely expressed. Most abundant in testis and expressed at high levels in brain, pituitary and kidney.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;dorsal root ganglion;testis - interstitial;superior cervical ganglion;medulla oblongata;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.81886 0.14055 -2.918150067 0.572068884 77.52713 1.85304 UBR5-AS1 . . . UBR5 antisense RNA 1 . . . . . . . . . . . UBR7 0.426811632119051 0.571643122793382 0.00154524508756747 ubiquitin protein ligase E3 component n-recognin 7 (putative) FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in sperm (at protein level). {ECO:0000269|PubMed:24664117}.; myocardium;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;germinal center;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;placenta;kidney;stomach;thymus;cerebellum; amygdala;superior cervical ganglion;globus pallidus;ciliary ganglion; 0.19189 0.11843 0.016664174 55.21939137 312.62321 3.76294 UBTD1 0.777525003561891 0.215178169861665 0.00729682657644426 ubiquitin domain containing 1 . . . . . 0.35156 0.11262 -0.383807564 27.41802312 17.73589 0.61975 UBTD2 0.748758501654584 0.241081606645399 0.0101598917000163 ubiquitin domain containing 2 . . TISSUE SPECIFICITY: Detected in dendritic cells. Highly expressed in tumor cell lines, but not detectable in most tissues. {ECO:0000269|PubMed:12507522}.; . . 0.39637 0.11262 0.125076652 62.7388535 49.28609 1.37266 UBTF 0.999998048435118 1.95156487889973e-06 2.65313395153144e-15 upstream binding transcription factor, RNA polymerase I FUNCTION: Recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element. {ECO:0000269|PubMed:7982918}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;placenta;hippocampus;duodenum;amnion;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;pons;trigeminal ganglion; 0.81960 0.17238 -1.155457828 6.168907761 10.71614 0.38835 UBTFL1 . . . upstream binding transcription factor, RNA polymerase I-like 1 FUNCTION: Essential for proliferation of the inner cell mass and trophectodermal cells in peri-implantation development. {ECO:0000250|UniProtKB:Q3USZ2}.; . . . . . . . . . . UBTFL2 . . . upstream binding transcription factor, RNA polymerase I-like 2 (pseudogene) . . . . . . . . . . . UBTFL3 . . . upstream binding transcription factor, RNA polymerase I-like 3 (pseudogene) . . . . . . . . . . . UBTFL5 . . . upstream binding transcription factor, RNA polymerase I-like 5 (pseudogene) . . . . . . . . . . . UBTFL6 . . . upstream binding transcription factor, RNA polymerase I-like 6 (pseudogene) . . . . . . . . . . . UBTFL7 . . . upstream binding transcription factor, RNA polymerase I-like 7 (pseudogene) . . . . . . . . . . . UBTFL8 . . . upstream binding transcription factor, RNA polymerase I-like 8 (pseudogene) . . . . . . . . . . . UBTFL9 . . . upstream binding transcription factor, RNA polymerase I-like 9 (pseudogene) . . . . . . . . . . . UBTFL10 . . . upstream binding transcription factor, RNA polymerase I-like 10 (pseudogene) . . . . . . . . . . . UBTFL11 . . . upstream binding transcription factor, RNA polymerase I-like 11 (pseudogene) . . . . . . . . . . . UBXN1 0.768417510378765 0.231220471602478 0.000362018018757709 UBX domain protein 1 FUNCTION: Ubiquitin-binding protein that interacts with the BRCA1- BARD1 heterodimer, and regulates its activity. Specifically binds 'Lys-6'-linked polyubiquitin chains. Interaction with autoubiquitinated BRCA1, leads to inhibit the E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer. Component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol.; . . ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;head and neck;kidney;stomach;aorta;thymus; subthalamic nucleus;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; . 0.11848 0.481458261 79.03986789 94.29398 2.08970 UBXN2A 0.000588703494775096 0.715997566557513 0.283413729947712 UBX domain protein 2A . . . unclassifiable (Anatomical System);ovary;parathyroid;skin;lung;larynx;bone;thyroid;placenta;visual apparatus;liver;testis;head and neck;spleen;amniotic fluid;kidney;brain;bladder;mammary gland; dorsal root ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12824 . -0.005381972 53.50908233 57.54653 1.53117 UBXN2B 0.487567803186615 0.507706755257287 0.00472544155609822 UBX domain protein 2B FUNCTION: Adapter protein required for Golgi and endoplasmic reticulum biogenesis. Involved in Golgi and endoplasmic reticulum maintenance during interphase and in their reassembly at the end of mitosis. The complex formed with VCP has membrane fusion activity; membrane fusion activity requires USO1-GOLGA2 tethering and BET1L. VCPIP1 is also required, but not its deubiquitinating activity. {ECO:0000269|PubMed:17141156}.; . . . . . 0.10456 -0.073340031 48.11866006 61.12287 1.59097 UBXN4 0.974205695161288 0.0257930729269118 1.23191180001827e-06 UBX domain protein 4 FUNCTION: Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD (PubMed:19822669). {ECO:0000269|PubMed:16968747, ECO:0000269|PubMed:19822669}.; . TISSUE SPECIFICITY: Expressed in many tissues, including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Accumulates in Alzheimer disease-afflicted brains (at protein level). {ECO:0000269|PubMed:16968747}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;uterus;whole body;oesophagus;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;atrioventricular node;trigeminal ganglion;parietal lobe; 0.61160 0.10404 -0.137658575 43.57159707 87.08494 1.99271 UBXN6 0.0473268975427938 0.947577214944901 0.00509588751230549 UBX domain protein 6 FUNCTION: Acts in a complex with VCP and cooperates with USP7 in promoting MDM2 deubiquitination and stabilization. MDM2 stabilization leads to MDM2-dependent TP53 degradation. {ECO:0000269|PubMed:18768758}.; . TISSUE SPECIFICITY: Enhanced expression in testis.; myocardium;lymphoreticular;medulla oblongata;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;brain;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;placenta;amnion;kidney;stomach;cerebellum; subthalamic nucleus;temporal lobe;globus pallidus;testis; 0.09894 0.10538 -0.172654315 40.63458363 1242.27235 6.65498 UBXN7 0.990657189537173 0.00934230959120534 5.00871621898599e-07 UBX domain protein 7 FUNCTION: Ubiquitin-binding adapter that links a subset of NEDD8- associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates. {ECO:0000269|PubMed:22537386}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;breast;lung;placenta;macula lutea;duodenum;head and neck;kidney;mammary gland;stomach;aorta; dorsal root ganglion;medulla oblongata;superior cervical ganglion;subthalamic nucleus;globus pallidus;appendix;ciliary ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.24768 0.11143 -0.205617011 38.57631517 20.45418 0.69676 UBXN7-AS1 . . . UBXN7 antisense RNA 1 . . . . . . . . . . . UBXN8 . . . UBX domain protein 8 FUNCTION: Involved in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins, possibly by tethering VCP to the endoplasmic reticulum membrane. May play a role in reproduction. {ECO:0000269|PubMed:21949850}.; . TISSUE SPECIFICITY: Expressed abundantly in ovary and testis, and weakly in all other tissues tested.; unclassifiable (Anatomical System);lymphoreticular;lymph node;cartilage;ovary;islets of Langerhans;hypothalamus;colon;blood;skin;prostate;whole body;lung;nasopharynx;bone;testis;germinal center;kidney;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.12581 0.09445 . . . . UBXN10 0.000293934797697053 0.566121715076753 0.43358435012555 UBX domain protein 10 . . . . . 0.11816 0.08431 -0.227663163 37.11370606 33.30023 1.02818 UBXN10-AS1 . . . UBXN10 antisense RNA 1 . . . . . . . . . . . UBXN11 1.20340272757806e-10 0.308498838569145 0.691501161310515 UBX domain protein 11 FUNCTION: May be involved in the reorganization of actin cytoskeleton mediated by RND1, RND2 AND RND3. Promotes RHOA activation mediated by GNA12 and GNA13 (By similarity). {ECO:0000250}.; . . ovary;colon;bone marrow;optic nerve;endometrium;cerebral cortex;larynx;bone;testis;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;liver;cervix;head and neck;spleen;kidney;mammary gland;stomach; . 0.10438 0.20558 1.201528238 93.00542581 1513.39604 7.23123 UCA1 . . . urothelial cancer associated 1 (non-protein coding) . . . . . . . . . . . UCHL1 0.972670211212399 0.0272951741286831 3.46146589178299e-05 ubiquitin C-terminal hydrolase L1 FUNCTION: Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity. {ECO:0000269|PubMed:12408865, ECO:0000269|PubMed:9790970}.; DISEASE: Parkinson disease 5 (PARK5) [MIM:613643]: A complex neurodegenerative disorder with manifestations ranging from typical Parkinson disease to dementia with Lewy bodies. Clinical features include parkinsonian symptoms (resting tremor, rigidity, postural instability and bradykinesia), dementia, diffuse Lewy body pathology, autonomic dysfunction, hallucinations and paranoia. {ECO:0000269|PubMed:9774100}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Neurodegeneration with optic atrophy, childhood-onset (NDGOA) [MIM:615491]: A progressive neurodegenerative syndrome characterized by childhood onset blindness, cerebellar ataxia, nystagmus, dorsal column dysfuction, and spasticity with upper motor neuron dysfunction. {ECO:0000269|PubMed:23359680}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Found in neuronal cell bodies and processes throughout the neocortex (at protein level). Expressed in neurons and cells of the diffuse neuroendocrine system and their tumors. Weakly expressed in ovary. Down-regulated in brains from Parkinson disease and Alzheimer disease patients. {ECO:0000269|PubMed:14722078, ECO:0000269|PubMed:9790970}.; ovary;sympathetic chain;colon;skin;retina;prostate;optic nerve;frontal lobe;endometrium;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;muscle;bile duct;lung;adrenal gland;trabecular meshwork;hippocampus;visual apparatus;liver;kidney;stomach;cerebellum; whole brain;dorsal root ganglion;amygdala;medulla oblongata;occipital lobe;thalamus;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.86471 0.10744 -0.141298762 42.87567823 2516.37626 9.35107 UCHL1-AS1 . . . UCHL1 antisense RNA 1 (head to head) . . . . . . . . . . . UCHL3 1.95224115097409e-05 0.702089900722818 0.297890576865672 ubiquitin C-terminal hydrolase L3 FUNCTION: Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3", and exhibits a preference towards 'Lys-48'-linked Ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin- signaling and insulin-induced adipogenesis. Required for stress- response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders. {ECO:0000269|PubMed:19154770, ECO:0000269|PubMed:21762696, ECO:0000269|PubMed:22689415, ECO:0000269|PubMed:2530630, ECO:0000269|PubMed:9790970}.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, and testis. {ECO:0000269|PubMed:9790970}.; . . 0.61491 0.11954 -0.163345027 41.24793583 18.24807 0.63412 UCHL5 0.78109674793509 0.218840676579493 6.25754854178254e-05 ubiquitin C-terminal hydrolase L5 FUNCTION: Protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains. Deubiquitinating enzyme associated with the 19S regulatory subunit of the 26S proteasome. Putative regulatory component of the INO80 complex; however is inactive in the INO80 complex and is activated by a transient interaction of the INO80 complex with the proteasome via ADRM1. {ECO:0000269|PubMed:16906146, ECO:0000269|PubMed:18922472}.; . . . . 0.20675 0.13709 -0.029247611 51.40363293 14.98435 0.53906 UCK1 0.00212663067332242 0.916158725889689 0.0817146434369883 uridine-cytidine kinase 1 FUNCTION: Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and N(4)-anisoylcytidine.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.13448 0.16622 0.016664174 55.21939137 19.231 0.66300 UCK2 0.962082764358181 0.0378393198854567 7.79157563623996e-05 uridine-cytidine kinase 2 FUNCTION: Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and N(4)-anisoylcytidine.; . TISSUE SPECIFICITY: According to PubMed:8812458; testis-specific. According to PubMed:11306702, placenta-specific. {ECO:0000269|PubMed:8812458}.; . . 0.37935 0.18619 -0.251530012 35.42108988 9.18306 0.33526 UCKL1 1.42564770235951e-08 0.361320166290837 0.638679819452686 uridine-cytidine kinase 1-like 1 FUNCTION: May contribute to UTP accumulation needed for blast transformation and proliferation. {ECO:0000269|PubMed:12199906}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12199906}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;peripheral nerve;cerebellum;thymus; skeletal muscle; 0.11651 0.11690 -1.397999468 4.193205945 33.52069 1.03522 UCKL1-AS1 . . . UCKL1 antisense RNA 1 . . . . . 0.10752 . . . . . UCMA 1.84529777389669e-07 0.0717290275318554 0.928270787938367 upper zone of growth plate and cartilage matrix associated FUNCTION: May be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface. {ECO:0000250}.; . TISSUE SPECIFICITY: Predominantly expressed in resting chondrocytes. {ECO:0000269|PubMed:16176871}.; . . 0.01283 0.05060 1.280642359 93.67775419 105.39838 2.22434 UCN 0.517240162953561 0.417081728567658 0.0656781084787807 urocortin FUNCTION: Acts in vitro to stimulate the secretion of adrenocorticotropic hormone (ACTH) (PubMed:8612563). Binds with high affinity to CRF receptor types 1, 2-alpha, and 2-beta (PubMed:8612563). Plays a role in the establishment of normal hearing thresholds (By similarity). Reduces food intake and regulates ghrelin levels in gastric body and plasma (By similarity). {ECO:0000250|UniProtKB:P55090, ECO:0000250|UniProtKB:P81615, ECO:0000269|PubMed:8612563}.; . TISSUE SPECIFICITY: Keratinocytes in epidermis and the outer and inner root sheaths of hair follicles, epithelium of sebaceous and sweat glands, erector pili muscle, cutaneous blood vessel walls, cutaneous nerves and dermal mononuclear cells (PubMed:10690896). Detected in plasma cells in the lamia propria in colon mucosa (PubMed:15531481) (at protein level). Expressed in pituitary and adrenal glands (PubMed:10690896). Detected in plasma cells in the lamia propria in colon mucosa (PubMed:15531481). {ECO:0000269|PubMed:10690896, ECO:0000269|PubMed:15531481}.; unclassifiable (Anatomical System);lymph node;ovary;colon;parathyroid;fovea centralis;choroid;lens;retina;uterus;prostate;optic nerve;whole body;lung;adrenal gland;bone;placenta;macula lutea;testis;kidney;brain; testis - interstitial;ciliary ganglion;pons;caudate nucleus;atrioventricular node;trigeminal ganglion;cingulate cortex;parietal lobe; 0.11630 0.20863 . . 17.86714 0.62411 UCN2 0.157235729046978 0.636824595429118 0.205939675523904 urocortin 2 FUNCTION: Suppresses food intake, delays gastric emptying and decreases heat-induced edema. Might represent an endogenous ligand for maintaining homeostasis after stress.; . . endometrium;brain;skin; . 0.02966 0.08604 -0.053113545 49.38664779 20.05397 0.68504 UCN3 0.508143909845209 0.4223796890532 0.0694764011015903 urocortin 3 FUNCTION: Suppresses food intake, delays gastric emptying and decreases heat-induced edema. Might represent an endogenous ligand for maintaining homeostasis after stress.; . . . . 0.11180 0.19727 -0.005381972 53.50908233 53.70413 1.46004 UCP1 4.52263871484388e-08 0.11406545632671 0.885934498446903 uncoupling protein 1 (mitochondrial, proton carrier) FUNCTION: UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation from ATP synthesis. As a result, energy is dissipated in the form of heat.; . TISSUE SPECIFICITY: Brown adipose tissue. {ECO:0000269|PubMed:3165741}.; . . 0.17669 0.58780 0.196671391 67.19155461 861.30815 5.72408 UCP2 1.91977015979194e-08 0.239996857999521 0.760003122802777 uncoupling protein 2 (mitochondrial, proton carrier) FUNCTION: UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation from ATP synthesis. As a result, energy is dissipated in the form of heat.; . TISSUE SPECIFICITY: Widely expressed in adult human tissues, including tissues rich in macrophages. Most expressed in white adipose tissue and skeletal muscle.; lymphoreticular;umbilical cord;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;iris;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; fetal liver;lymph node;trachea;thyroid;tumor;white blood cells;whole blood;tonsil;thymus;bone marrow; 0.16791 0.61818 0.108486928 61.90728946 2883.94934 10.17629 UCP3 1.07071142074629e-05 0.351846038148766 0.648143254737027 uncoupling protein 3 (mitochondrial, proton carrier) FUNCTION: UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation. As a result, energy is dissipated in the form of heat. May play a role in the modulation of tissue respiratory control. Participates in thermogenesis and energy balance.; . TISSUE SPECIFICITY: Only in skeletal muscle and heart. Is more expressed in glycolytic than in oxidative skeletal muscles. {ECO:0000269|PubMed:9196039}.; unclassifiable (Anatomical System);cartilage;spinal cord;blood;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;whole body;bone;macula lutea;testis;brain;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.08932 0.32882 0.332586472 73.61405992 876.27254 5.75990 UEVLD 1.09267674829095e-07 0.542920197880432 0.457079692851893 UEV and lactate/malate dehyrogenase domains FUNCTION: Possible negative regulator of polyubiquitination. {ECO:0000269|PubMed:12427560}.; . TISSUE SPECIFICITY: Colon, colon carcinoma cell lines, normal cervical epithelium, carcinomas of the uterine cervix and peripheral blood leukocytes. {ECO:0000269|PubMed:12427560}.; unclassifiable (Anatomical System);smooth muscle;cartilage;ovary;blood;parathyroid;skin;skeletal muscle;retina;pancreas;placenta;bone;hippocampus;testis;germinal center;kidney;brain;mammary gland; superior cervical ganglion; 0.13244 0.14875 -0.402212257 26.7338995 286.11158 3.62110 UFC1 0.0899541883849323 0.901183395752236 0.00886241586283191 ubiquitin-fold modifier conjugating enzyme 1 FUNCTION: E2-like enzyme which forms an intermediate with UFM1 via a thioester linkage. {ECO:0000269|PubMed:15071506}.; . . . . 0.36303 0.12971 -0.339715008 30.06605331 16.066 0.56858 UFD1L 0.997407162576096 0.00259272943429611 1.07989607528697e-07 ubiquitin fusion degradation 1 like (yeast) FUNCTION: Essential component of the ubiquitin-dependent proteolytic pathway which degrades ubiquitin fusion proteins. The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. It may be involved in the development of some ectoderm-derived structures.; . TISSUE SPECIFICITY: Found in adult heart, skeletal muscle and pancreas, and in fetal liver and kidney.; lymphoreticular;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; testis - interstitial;testis; 0.44657 0.16040 0.058937498 58.26256192 204.07455 3.08556 UFL1 1.9081642881261e-12 0.580335844923436 0.419664155074656 UFM1 specific ligase 1 FUNCTION: E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins, a post-translational modification on lysine residues of proteins that may play a crucial role in a number of cellular processes. Mediates DDRGK1 ufmylation and may regulate the proteasomal degradation of DDRGK1 and CDK5RAP3 thereby modulating NF-kappa-B signaling (PubMed:20018847, PubMed:20164180, PubMed:20228063, PubMed:25219498). May also through TRIP4 ufmylation play a role in nuclear receptors-mediated transcription (PubMed:25219498). May play a role in the unfolded protein response, mediating the ufmylation of multiple proteins in response to endoplasmic reticulum stress (PubMed:23152784). {ECO:0000269|PubMed:20018847, ECO:0000269|PubMed:20164180, ECO:0000269|PubMed:20228063, ECO:0000269|PubMed:23152784, ECO:0000269|PubMed:25219498}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with a high expression in liver (at protein level). Low expression in several invasive hepatocellular carcinomas, such Hep-G2, Hep 3B2.1-7, HLE and PLC. {ECO:0000269|PubMed:20018847}.; . . 0.75716 0.10429 -0.775187015 13.05142722 216.74364 3.18197 UFL1-AS1 . . . UFL1 antisense RNA 1 . . . . . . . . . . . UFM1 0.464066114233379 0.510523574835982 0.0254103109306382 ubiquitin-fold modifier 1 FUNCTION: Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to substrate proteins as a monomer or a lysine-linked polymer. The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1 (PubMed:15071506, PubMed:20018847). This post-translational modification on lysine residues of proteins may play a crucial role in a number of cellular processes. TRIP4 ufmylation may for instance play a role in nuclear receptors-mediated transcription (PubMed:25219498). Other substrates may include DDRGK1 with which it may play a role in the cellular response to endoplasmic reticulum stress (Probable). {ECO:0000269|PubMed:15071506, ECO:0000269|PubMed:20018847, ECO:0000269|PubMed:25219498, ECO:0000305|PubMed:23152784}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;aorta;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion; 0.03169 0.10615 0.013025609 54.62962963 9.75863 0.35714 UFSP1 0.00559926862470787 0.481563889297395 0.512836842077897 UFM1-specific peptidase 1 (inactive) . . . . . 0.13748 0.10063 0.148941568 64.31941496 299.12246 3.68755 UFSP2 6.10971263298467e-06 0.886025925468131 0.113967964819236 UFM1-specific peptidase 2 FUNCTION: Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of UFM1, a ubiquitin-like modifier protein bound to a number of target proteins. Does not hydrolyze SUMO1 or ISG15 ubiquitin-like proteins. Through TRIP4 deufmylation may regulate intracellular nuclear receptors transactivation and thereby regulate cell proliferation and differentiation. {ECO:0000269|PubMed:25219498}.; DISEASE: Beukes familial hip dysplasia (BFHD) [MIM:142669]: A severe progressive degenerative osteoarthritis of the hip joint with underlying dysplasia confined to that region. Affected individuals are of normal stature and have no associated health problems. {ECO:0000269|PubMed:26428751}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;oesophagus;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;pineal gland;artery;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;spleen;head and neck;kidney;mammary gland;aorta;stomach; occipital lobe;testis - seminiferous tubule;testis;parietal lobe;skeletal muscle;cingulate cortex; 0.22830 0.10715 -0.025608647 51.91672564 255.71192 3.43940 UGCG 0.982568591990549 0.0174290932215322 2.31478791899179e-06 UDP-glucose ceramide glucosyltransferase FUNCTION: Catalyzes the first glycosylation step in glycosphingolipid biosynthesis, the transfer of glucose to ceramide. May also serve as a "flippase". {ECO:0000269|PubMed:8643456}.; . TISSUE SPECIFICITY: Found in all tissues examined. {ECO:0000269|PubMed:8643456}.; . . 0.18485 0.40044 -0.05129383 49.75819769 13.55042 0.49230 UGDH 5.54140714269145e-05 0.883396038912861 0.116548547015712 UDP-glucose 6-dehydrogenase FUNCTION: Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9850599}.; lymphoreticular;ovary;salivary gland;intestine;colon;skin;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;cornea;mesenchyma;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;stomach;aorta; fetal liver;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.91005 0.10964 -0.137658575 43.57159707 82.05323 1.92058 UGDH-AS1 . . . UGDH antisense RNA 1 . . . . . . . . . . . UGGT1 0.00289726281334611 0.997102736883172 3.03482229922747e-10 UDP-glucose glycoprotein glucosyltransferase 1 FUNCTION: Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. {ECO:0000269|PubMed:10694380}.; . TISSUE SPECIFICITY: Higher levels in pancreas, skeletal muscle, kidney, and brain. Low levels in lung and heart. {ECO:0000269|PubMed:10694380}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;gum;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;trigeminal ganglion; 0.56161 0.11817 -1.164811619 6.080443501 308.40352 3.73661 UGGT2 1.01866409514518e-21 0.535349820839564 0.464650179160436 UDP-glucose glycoprotein glucosyltransferase 2 FUNCTION: Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Higher levels in kidney, pancreas, heart, and skeletal muscle. {ECO:0000269|PubMed:10694380}.; . . 0.06448 0.09703 1.282308148 93.6836518 5160.48386 14.76411 UGP2 0.00102013070287478 0.947456118318881 0.051523750978244 UDP-glucose pyrophosphorylase 2 FUNCTION: Plays a central role as a glucosyl donor in cellular metabolic pathways.; . . myocardium;ovary;skin;retina;prostate;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;synovium;bone;pituitary gland;testis;dura mater;spinal ganglion;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta; amygdala;thalamus;medulla oblongata;occipital lobe;superior cervical ganglion;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex; 0.97124 0.39898 -0.979072682 8.752064166 24.54236 0.80685 UGT1A . . . UDP glucuronosyltransferase family 1 member A complex locus . . . . . . . . . . . UGT1A1 2.93632324623578e-09 0.0856061444909576 0.914393852572719 UDP glucuronosyltransferase family 1 member A1 FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate. Is also able to catalyze the glucuronidation of 17beta-estradiol, 17alpha-ethinylestradiol, 1-hydroxypyrene, 4- methylumbelliferone, 1-naphthol, paranitrophenol, scopoletin, and umbelliferone. Isoform 2 lacks transferase activity but acts as a negative regulator of isoform 1. {ECO:0000269|PubMed:18004206, ECO:0000269|PubMed:19545173, ECO:0000269|PubMed:19830808}.; DISEASE: Gilbert syndrome (GILBS) [MIM:143500]: Occurs as a consequence of reduced bilirubin transferase activity and is often detected in young adults with vague non-specific complaints. {ECO:0000269|PubMed:11013440, ECO:0000269|PubMed:12139570, ECO:0000269|PubMed:7715297, ECO:0000269|PubMed:9627603}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Transient familial neonatal hyperbilirubinemia (HBLRTFN) [MIM:237900]: A condition characterized by excessive concentration of bilirubin in the blood, which may lead to jaundice. Breast milk jaundice is a common problem in nursing infants. {ECO:0000269|PubMed:11061796}. Note=The disease may be caused by mutations affecting the gene represented in this entry. The defect has been ascribed to various breast milk substances, but the component or combination of components that is responsible remains unclear. Defects of UGT1A1 are an underlying cause of the prolonged unconjugated hyperbilirubinemia associated with breast milk. One or more components in the milk may trigger the jaundice in infants who have such mutations. Mutations are identical to those detected in patients with Gilbert syndrome, a risk factor of neonatal non-physiologic hyperbilirubinemia and a genetic factor in fasting hyperbilirubinemia.; DISEASE: Crigler-Najjar syndrome 1 (CN1) [MIM:218800]: Patients have severe hyperbilirubinemia and usually die of kernicterus (bilirubin accumulation in the basal ganglia and brainstem nuclei) within the first year of life. CN1 inheritance is autosomal recessive. {ECO:0000269|PubMed:11013440, ECO:0000269|PubMed:15712364, ECO:0000269|PubMed:1634050, ECO:0000269|PubMed:17229650, ECO:0000269|PubMed:19830808, ECO:0000269|PubMed:23992562, ECO:0000269|PubMed:7906695, ECO:0000269|PubMed:7989045, ECO:0000269|PubMed:7989595, ECO:0000269|PubMed:8226884}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Crigler-Najjar syndrome 2 (CN2) [MIM:606785]: Patients have less severe hyperbilirubinemia and usually survive into adulthood without neurologic damage. Phenobarbital, which induces the partially deficient glucuronyl transferase, can diminish the jaundice. CN2 inheritance is autosomal dominant. {ECO:0000269|PubMed:11013440, ECO:0000269|PubMed:11370628, ECO:0000269|PubMed:12402338, ECO:0000269|PubMed:15712364, ECO:0000269|PubMed:17229650, ECO:0000269|PubMed:19830808, ECO:0000269|PubMed:23099197, ECO:0000269|PubMed:23992562, ECO:0000269|PubMed:7989595, ECO:0000269|PubMed:8276413, ECO:0000269|PubMed:8280139, ECO:0000269|PubMed:8706880, ECO:0000269|PubMed:9621515, ECO:0000269|PubMed:9639672}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in liver, colon and small intestine. Isoform 2 but not isoform 1 is expressed in kidney. Isoform 1 and isoform 2 are not expressed in esophagus. Not expressed in skin. {ECO:0000269|PubMed:1339448, ECO:0000269|PubMed:17187418, ECO:0000269|PubMed:18004212}.; unclassifiable (Anatomical System);ovary;small intestine;salivary gland;intestine;pharynx;colon;blood;skin;prostate;lung;cornea;larynx;nasopharynx;visual apparatus;liver;head and neck;kidney;brain;mammary gland;bladder;stomach; . . 0.58091 -0.556537043 19.72753008 185.91297 2.96084 UGT1A2P . . . UDP glucuronosyltransferase family 1 member A2, pseudogene . . . . . . . . . . . UGT1A3 2.93632324623578e-09 0.0856061444909576 0.914393852572719 UDP glucuronosyltransferase family 1 member A3 FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Isoform 2 lacks transferase activity but acts as a negative regulator of isoform 1. {ECO:0000269|PubMed:18674515}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in liver, kidney, colon and small intestine. Isoform 1 but not isoform 2 is expressed in esophagus. {ECO:0000269|PubMed:18004212}.; . . . 0.58091 0.181903047 66.2361406 509.47039 4.62471 UGT1A4 2.34298507765321e-06 0.485302918638048 0.514694738376874 UDP glucuronosyltransferase family 1 member A4 FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate. Isoform 2 lacks transferase activity but acts as a negative regulator of isoform 1 (By similarity). {ECO:0000250}.; DISEASE: Gilbert syndrome (GILBS) [MIM:143500]: Occurs as a consequence of reduced bilirubin transferase activity and is often detected in young adults with vague non-specific complaints. {ECO:0000269|PubMed:17496722}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Crigler-Najjar syndrome 1 (CN1) [MIM:218800]: Patients have severe hyperbilirubinemia and usually die of kernicterus (bilirubin accumulation in the basal ganglia and brainstem nuclei) within the first year of life. CN1 inheritance is autosomal recessive. {ECO:0000269|PubMed:1634050}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Crigler-Najjar syndrome 2 (CN2) [MIM:606785]: Patients have less severe hyperbilirubinemia and usually survive into adulthood without neurologic damage. Phenobarbital, which induces the partially deficient glucuronyl transferase, can diminish the jaundice. CN2 inheritance is autosomal dominant. {ECO:0000269|PubMed:8276413, ECO:0000269|PubMed:8280139}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in liver, kidney, colon and small intestine. Isoform 2 but not isoform 1 is expressed in esophagus. Not expressed in skin. {ECO:0000269|PubMed:1339448, ECO:0000269|PubMed:18004212}.; . . . 0.58091 0.181903047 66.2361406 318.86207 3.79209 UGT1A5 0.000100214943072604 0.804197800134383 0.195701984922544 UDP glucuronosyltransferase family 1 member A5 FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Isoform 2 lacks transferase activity but acts as a negative regulator of isoform 1 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in colon and small intestine. Neither isoform is expressed in liver, kidney or esophagus. {ECO:0000269|PubMed:18004212}.; . . . 0.58091 0.979225112 90.42816702 2828.944 10.03075 UGT1A6 0.000217879588051916 0.912493209475893 0.0872889109360552 UDP glucuronosyltransferase family 1 member A6 FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform has specificity for phenols. Isoform 3 lacks transferase activity but acts as a negative regulator of isoform 1 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in skin. Isoforms 1 and 3 are expressed in kidney and liver. Isoform 1 but not isoform 2 is expressed in colon, esophagus and small intestine. {ECO:0000269|PubMed:1339448, ECO:0000269|PubMed:18004212}.; unclassifiable (Anatomical System);ovary;small intestine;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;lung;cornea;larynx;nasopharynx;visual apparatus;liver;head and neck;kidney;brain;mammary gland;bladder;stomach; . . 0.58091 -0.400392389 26.85185185 2258.74816 8.78360 UGT1A7 1.8013984282508e-12 0.0155490378673737 0.984450962130825 UDP glucuronosyltransferase family 1 member A7 FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Isoform 2 lacks transferase activity but acts as a negative regulator of isoform 1. {ECO:0000269|PubMed:23360619}.; . TISSUE SPECIFICITY: Liver and gastric tissue. Isoform 1 and isoform 2 are expressed in esophagus. Neither isoform is expressed in liver, kidney, colon and small intestine (PubMed:18004212). {ECO:0000269|PubMed:18004212, ECO:0000269|PubMed:9271343}.; . . . 0.58091 -0.154246007 42.22694032 35.97621 1.08026 UGT1A8 6.95565246350873e-05 0.734676155264838 0.265254288210527 UDP glucuronosyltransferase family 1 member A8 FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Isoform 2 lacks transferase activity but acts as a negative regulator of isoform 1. {ECO:0000269|PubMed:19545173}.; . TISSUE SPECIFICITY: Colon specific. Isoform 1 and 2 are expressed in liver, kidney, colon and small intestine; isoform 2 but not isoform 1 is expressed in liver (PubMed:18004212). {ECO:0000269|PubMed:18004212, ECO:0000269|PubMed:9535849}.; . . . 0.58091 -0.420619508 25.72540694 . . UGT1A9 1.32215694425957e-08 0.197032267734801 0.802967719043629 UDP glucuronosyltransferase family 1 member A9 FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform has specificity for phenols. Isoform 2 lacks transferase activity but acts as a negative regulator of isoform 1. {ECO:0000269|PubMed:19545173}.; . TISSUE SPECIFICITY: Liver. Isoform 1 and isoform 2 are expressed in liver, kidney, colon, esophagus and small intestine. {ECO:0000269|PubMed:18004212}.; unclassifiable (Anatomical System);ovary;small intestine;salivary gland;intestine;pharynx;colon;blood;skin;lung;cornea;larynx;visual apparatus;liver;head and neck;kidney;brain;mammary gland;bladder;stomach; . . 0.58091 -0.686998355 15.26893135 43.34389 1.25131 UGT1A10 1.09144321714604e-11 0.0232603215966593 0.976739678392426 UDP glucuronosyltransferase family 1 member A10 FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Isoform 2 lacks transferase activity but acts as a negative regulator of isoform 1. {ECO:0000269|PubMed:19545173}.; . TISSUE SPECIFICITY: Liver and colon. Isoform 1 and isoform 2 are expressed in colon, esophagus and small intestine; isoform 2 but not isoform 1 is expressed in liver or kidney (PubMed:18004212). {ECO:0000269|PubMed:18004212, ECO:0000269|PubMed:9271343}.; unclassifiable (Anatomical System);ovary;small intestine;salivary gland;intestine;pharynx;colon;blood;skin;lung;cornea;larynx;visual apparatus;liver;head and neck;kidney;brain;mammary gland;bladder;stomach; . . 0.58091 -0.484940685 22.75300778 223.80924 3.23496 UGT1A11P . . . UDP glucuronosyltransferase family 1 member A11, pseudogene . . . . . . . . . . . UGT1A12P . . . UDP glucuronosyltransferase family 1 member A12, pseudogene . . . . . . . . . . . UGT1A13P . . . UDP glucuronosyltransferase family 1 member A13, pseudogene . . . . . . . . . . . UGT2A1 2.73195454586815e-11 0.0396715255053001 0.96032847446738 UDP glucuronosyltransferase family 2 member A1 complex locus FUNCTION: UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Active on odorants and seems to be involved in olfaction; it could help clear lipophilic odorant molecules from the sensory epithelium. {ECO:0000269|PubMed:19858781}.; . TISSUE SPECIFICITY: Olfactory epithelium and brain. Isoform 2 is mainly expressed in the nasal mucosa. {ECO:0000269|PubMed:10359671, ECO:0000269|PubMed:19858781}.; pituitary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07071 . 0.981046964 90.45765511 1259.71259 6.69318 UGT2A2 2.32634948326899e-07 0.46810166629979 0.531898101065261 UDP glucuronosyltransferase family 2 member A2 FUNCTION: UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Active on odorants and seems to be involved in olfaction; it could help clear lipophilic odorant molecules from the sensory epithelium. {ECO:0000269|PubMed:19858781}.; . TISSUE SPECIFICITY: Olfactory epithelium and brain. Isoform 2 is mainly expressed in the nasal mucosa. {ECO:0000269|PubMed:10359671, ECO:0000269|PubMed:19858781}.; . . . . 1.690270544 96.40835103 1627.54392 7.45894 UGT2A3 5.00169122908013e-06 0.859095445916156 0.140899552392615 UDP glucuronosyltransferase family 2 member A3 FUNCTION: UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);prostate;pancreas;islets of Langerhans;liver;spleen;kidney;skeletal muscle; superior cervical ganglion;temporal lobe;atrioventricular node;trigeminal ganglion; 0.33484 0.13913 0.380318343 75.63104506 280.9506 3.59104 UGT2A3P7 . . . UDP glucuronosyltransferase family 2 member A3 pseudogene 7 . . . . . . . . . . . UGT2B4 8.44718840140518e-11 0.0400416105635841 0.959958389351944 UDP glucuronosyltransferase family 2 member B4 FUNCTION: UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme is active on polyhydroxylated estrogens (such as estriol, 4-hydroxyestrone and 2-hydroxyestriol) and xenobiotics (such as 4-methylumbelliferone, 1-naphthol, 4- nitrophenol, 2-aminophenol, 4-hydroxybiphenyl and menthol). It is capable of 6 alpha-hydroxyglucuronidation of hyodeoxycholic acid.; . . unclassifiable (Anatomical System);liver;spleen;kidney; fetal liver;superior cervical ganglion;liver;trigeminal ganglion; 0.05215 0.20316 0.202129237 67.42745931 1015.87088 6.13262 UGT2B7 3.49679084556951e-08 0.325426782202756 0.674573182829336 UDP glucuronosyltransferase family 2 member B7 FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. {ECO:0000269|PubMed:17442341}.; . . unclassifiable (Anatomical System);breast;ovary;endometrium;visual apparatus;liver;spleen;kidney; . 0.03734 0.20506 -0.176292081 40.56381222 33.30553 1.02874 UGT2B10 5.50615564451229e-15 0.00708559652341284 0.992914403476582 UDP glucuronosyltransferase family 2 member B10 FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds.; . . unclassifiable (Anatomical System);liver;spleen;kidney; . 0.06029 . . . 551.54579 4.77610 UGT2B11 3.14709815271135e-13 0.0107352918448037 0.989264708154882 UDP glucuronosyltransferase family 2 member B11 FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds.; . TISSUE SPECIFICITY: Widely expressed.; . . 0.04946 . 2.35918141 98.42533616 1410.89129 7.01598 UGT2B15 1.92098648554063e-10 0.120794620616588 0.879205379191313 UDP glucuronosyltransferase family 2 member B15 FUNCTION: UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme displays activity toward several classes of xenobiotic substrates, including simple phenolic compounds, 7-hydroxylated coumarins, flavonoids, anthraquinones, and certain drugs and their hydroxylated metabolites. It also catalyzes the glucuronidation of endogenous estrogens and androgens.; . TISSUE SPECIFICITY: Expressed in many tissues. Present in liver, prostate and testis. {ECO:0000269|PubMed:8399210}.; unclassifiable (Anatomical System);islets of Langerhans;liver;colon; dorsal root ganglion;superior cervical ganglion;liver;ciliary ganglion;trigeminal ganglion;skin; 0.12123 0.11922 1.377921151 94.56829441 390.32968 4.16089 UGT2B17 0.0102556056990611 0.979694231392234 0.0100501629087052 UDP glucuronosyltransferase family 2 member B17 FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. The major substrates of this isozyme are eugenol > 4-methylumbelliferone > dihydrotestosterone (DHT) > androstane-3-alpha,17-beta-diol (3-alpha-diol) > testosterone > androsterone (ADT).; . TISSUE SPECIFICITY: Expressed in various tissues including the liver, kidney, testis, uterus, placenta, mammary gland, adrenal gland, skin and prostate.; unclassifiable (Anatomical System);islets of Langerhans;liver;colon; superior cervical ganglion;appendix;skeletal muscle; 0.03271 0.16972 1.708681962 96.45553197 239.01769 3.33957 UGT2B24P . . . UDP glucuronosyltransferase family 2 member B24, pseudogene . . . . . . . . . . . UGT2B25P . . . UDP glucuronosyltransferase family 2 member B25, pseudogene . . . . . . . . . . . UGT2B26P . . . UDP glucuronosyltransferase family 2 member B26, pseudogene . . . . . . . . . . . UGT2B27P . . . UDP glucuronosyltransferase family 2 member B27, pseudogene . . . . . . . . . . . UGT2B28 6.44395718165304e-08 0.434127347477449 0.565872588082979 UDP glucuronosyltransferase family 2 member B28 FUNCTION: UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme has glucuronidating capacity with steroid substrates such as 5-beta-androstane 3-alpha,17-beta- diol, estradiol, ADT, eugenol and bile acids. Only isoform 1 seems to be active. {ECO:0000269|PubMed:11300766}.; . TISSUE SPECIFICITY: Expressed in the liver, breast and kidney. {ECO:0000269|PubMed:11300766}.; unclassifiable (Anatomical System);skeletal muscle; . 0.08008 . 1.534092314 95.56499174 6528.21825 16.98038 UGT2B29P . . . UDP glucuronosyltransferase family 2 member B29, pseudogene . . . . . . . . . . . UGT3A1 5.21347442389169e-10 0.0602236521991018 0.939776347279551 UDP glycosyltransferase family 3 member A1 FUNCTION: UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;larynx;bone;testis;head and neck;kidney; dorsal root ganglion;testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion;skeletal muscle; 0.05298 0.07012 0.308721233 72.59966973 2293.04286 8.86662 UGT3A2 2.94297254099195e-10 0.0820476171426135 0.917952382563089 UDP glycosyltransferase family 3 member A2 FUNCTION: UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);bile duct;bone;testis;blood;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.11363 . 0.354632714 74.58126917 49.98507 1.38761 UGT8 0.226816185725885 0.765385936774886 0.00779787749922904 UDP glycosyltransferase 8 FUNCTION: Catalyzes the transfer of galactose to ceramide, a key enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system.; . . unclassifiable (Anatomical System);amygdala;pancreas;lung;hypothalamus;testis;colon;brain; whole brain;amygdala;thalamus;medulla oblongata;occipital lobe;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;caudate nucleus;prefrontal cortex;parietal lobe;cingulate cortex; 0.61520 0.26765 0.242582624 69.45623968 707.59733 5.28271 UHMK1 0.729319451779304 0.270110711713292 0.000569836507404218 U2AF homology motif (UHM) kinase 1 FUNCTION: Upon serum stimulation, phosphorylates CDKN1B/p27Kip1, thus controlling CDKN1B subcellular location and cell cycle progression in G1 phase. May be involved in trafficking and/or processing of RNA (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in skeletal muscle, kidney, placenta and peripheral blood leukocytes. {ECO:0000269|PubMed:12093740}.; unclassifiable (Anatomical System);frontal lobe;larynx;visual apparatus;cervix;head and neck;germinal center;brain;stomach;bone marrow; . 0.29241 0.51150 -0.271755481 34.31823543 28.91719 0.92338 UHRF1 . . . ubiquitin like with PHD and ring finger domains 1 FUNCTION: Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD- type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. May be involved in DNA repair. {ECO:0000269|PubMed:10646863, ECO:0000269|PubMed:15009091, ECO:0000269|PubMed:15361834, ECO:0000269|PubMed:17673620, ECO:0000269|PubMed:17967883, ECO:0000269|PubMed:19056828, ECO:0000269|PubMed:21745816, ECO:0000269|PubMed:21777816, ECO:0000269|PubMed:22945642}.; DISEASE: Note=Defects in UHRF1 may be a cause of cancers. Overexpressed in many different forms of human cancers, including bladder, breast, cervical, colorectal and prostate cancers, as well as pancreatic adenocarcinomas, rhabdomyosarcomas and gliomas. Plays an important role in the correlation of histone modification and gene silencing in cancer progression. Expression is associated with a poor prognosis in patients with various cancers, suggesting that it participates in cancer progression.; TISSUE SPECIFICITY: Expressed in thymus, bone marrow, testis, lung and heart. Overexpressed in breast cancer. {ECO:0000269|PubMed:10646863, ECO:0000269|PubMed:12838312, ECO:0000269|PubMed:15361834}.; unclassifiable (Anatomical System);ovary;colon;skeletal muscle;breast;uterus;pancreas;whole body;lung;pituitary gland;liver;testis;cervix;spleen;germinal center;kidney;brain;bladder;stomach; thymus; 0.23883 0.15269 . . . . UHRF1BP1 2.46541297366596e-07 0.999956580425403 4.31730332999139e-05 UHRF1 binding protein 1 FUNCTION: May act as a negative regulator of cell growth. {ECO:0000269|PubMed:15361834}.; . . bone;placenta;visual apparatus;liver;testis;colon;spleen;blood;germinal center;mammary gland;skin;stomach;bone marrow; dorsal root ganglion;superior cervical ganglion; 0.15086 0.09891 0.435344483 77.36494456 6137.38486 16.37148 UHRF1BP1L 0.989377600602275 0.0106223991650062 2.32718621755426e-10 UHRF1 binding protein 1 like . . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; amygdala;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.73214 . 1.49913011 95.38216561 1032.40429 6.17290 UHRF2 0.999646143660092 0.000353856305446165 3.44622998744673e-11 ubiquitin like with PHD and ring finger domains 2 FUNCTION: E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131. {ECO:0000269|PubMed:12176013, ECO:0000269|PubMed:14741369, ECO:0000269|PubMed:15178429, ECO:0000269|PubMed:15361834, ECO:0000269|PubMed:21952639, ECO:0000269|PubMed:23404503}.; DISEASE: Note=Associated with various cancers. DNA copy number loss is found in multiple kinds of malignancies originating from the brain, breast, stomach, kidney, hematopoietic tissue and lung.; . ovary;colon;parathyroid;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;urinary;blood;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;aorta;stomach;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.26264 0.13812 -0.380166007 27.88393489 43.75397 1.25932 UHRF2P1 . . . ubiquitin like with PHD and ring finger domains 2 pseudogene 1 . . . . . . . . . . . UIMC1 0.0326458625692234 0.967278483257136 7.5654173641012e-05 ubiquitin interaction motif containing 1 FUNCTION: Ubiquitin-binding protein (PubMed:24627472). Specifically recognizes and binds 'Lys-63'-linked ubiquitin (PubMed:19328070, Ref.35). Plays a central role in the BRCA1-A complex by specifically binding 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. Also weakly binds monoubiquitin but with much less affinity than 'Lys-63'-linked ubiquitin. May interact with monoubiquitinated histones H2A and H2B; the relevance of such results is however unclear in vivo. Does not bind Lys-48'-linked ubiquitin. May indirectly act as a transcriptional repressor by inhibiting the interaction of NR6A1 with the corepressor NCOR1. {ECO:0000269|PubMed:12080054, ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:17525341, ECO:0000269|PubMed:17525342, ECO:0000269|PubMed:17621610, ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:19015238, ECO:0000269|PubMed:19202061, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19328070, ECO:0000269|PubMed:24627472, ECO:0000269|Ref.35}.; . TISSUE SPECIFICITY: Expressed in testis, ovary, thymus and heart. Expressed in germ cells of the testis. {ECO:0000269|PubMed:12080054}.; colon;fovea centralis;choroid;retina;uterus;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;medulla oblongata;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.28387 0.17850 0.069852974 59.10592121 1332.8819 6.85589 ULBP1 0.00017261233677896 0.454490209895478 0.545337177767743 UL16 binding protein 1 FUNCTION: Ligand for the KLRK1/NKG2D receptor, together with at least ULBP2 and ULBP3. ULBPs activate multiple signaling pathways in primary NK cells, resulting in the production of cytokines and chemokines. Binding of ULBPs ligands to KLRK1/NKG2D induces calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway. In CMV infected cells, interacts with soluble CMV glycoprotein UL16. The interaction with UL16 blocked the interaction with the KLRK1/NKG2D receptor, providing a mechanism by which CMV infected cells might escape the immune system. UL16 also causes ULBP1 to be retained in the ER and cis-Golgi apparatus so that it does not reach the cell surface. {ECO:0000269|PubMed:11777960}.; . TISSUE SPECIFICITY: Expressed in T-cells, B-cells, erythroleukemia cell lines and in a wide range of tissues including heart, brain, lung, liver, testis, lymph node, thymus, tonsil and bone marrow. Also found in fetal heart, brain, lung and liver.; lung;islets of Langerhans;bone;testis;cervix;lens;skeletal muscle; dorsal root ganglion;superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion; 0.06789 0.09707 0.262810045 70.43524416 221.99287 3.22095 ULBP2 0.00110138772463706 0.611264150033188 0.387634462242175 UL16 binding protein 2 FUNCTION: Ligand for the KLRK1/NKG2D receptor, together with at least ULBP1 and ULBP3. ULBPs activate multiple signaling pathways in primary NK cells, resulting in the production of cytokines and chemokines. Binding of ULBPs ligands to KLRK1/NKG2D induces calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway. In CMV infected cells, interacts with soluble CMV glycoprotein UL16. The interaction with UL16 blocked the interaction with the KLRK1/NKG2D receptor, providing a mechanism by which CMV infected cells might escape the immune system. UL16 also causes ULBP2 to be retained in the ER and cis-Golgi apparatus so that it does not reach the cell surface. {ECO:0000269|PubMed:11777960}.; . TISSUE SPECIFICITY: Expressed in various types of cancer cell lines and in the fetus, but not in normal tissues. {ECO:0000269|PubMed:11444831}.; . . 0.31701 0.09986 0.393270925 76.04977589 234.75709 3.31187 ULBP3 1.85029067408059e-08 0.0361826475304711 0.963817333966622 UL16 binding protein 3 FUNCTION: Ligand for the KLRK1/NKG2D receptor, together with at least ULBP1 and ULBP2. ULBPs activate multiple signaling pathways in primary NK cells, resulting in the production of cytokines and chemokines. Binding of ULBPs ligands to KLRK1/NKG2D induces calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway. Has lower affinity for KLRK1/NKG2D compared to ULBP1 and ULBP2 and induces weaker signaling responses than does ULBP2 or ULBP1. {ECO:0000269|PubMed:11777960}.; . . unclassifiable (Anatomical System);ovary;thyroid;placenta;parathyroid;stomach; . 0.05153 . 0.685332364 85.09672092 502.6757 4.59967 ULK1 0.964459663318906 0.0355403321067721 4.57432203472228e-09 unc-51 like autophagy activating kinase 1 FUNCTION: Serine/threonine-protein kinase involved in autophagy in response to starvation. Acts upstream of phosphatidylinositol 3- kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes. Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity. May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences. Plays a role early in neuronal differentiation and is required for granule cell axon formation. {ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:21460634, ECO:0000269|PubMed:21795849}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Detected in the following adult tissues: skeletal muscle, heart, pancreas, brain, placenta, liver, kidney, and lung.; smooth muscle;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.39547 0.14281 -1.223753865 5.561453173 1096.67628 6.33982 ULK2 1.30040166627867e-05 0.999969449697168 1.75462861689156e-05 unc-51 like autophagy activating kinase 2 FUNCTION: Serine/threonine-protein kinase involved in autophagy in response to starvation. Acts upstream of phosphatidylinositol 3- kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes. Part of regulatory feedback loops in autophagy: acts both as a downstream effector and a negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK, also acts as a negative regulator of AMPK through phosphorylation of the AMPK subunits PRKAA1, PRKAB2 and PRKAG1. May phosphorylate ATG13/KIAA0652, FRS2, FRS3 and RPTOR; however such data need additional evidences. Not involved in ammonia-induced autophagy or in autophagic response of cerebellar granule neurons (CGN) to low potassium concentration. Plays a role early in neuronal differentiation and is required for granule cell axon formation: may govern axon formation via Ras-like GTPase signaling and through regulation of the Rab5-mediated endocytic pathways within developing axons. {ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:21460634, ECO:0000269|PubMed:21460635, ECO:0000269|PubMed:21690395, ECO:0000269|PubMed:21795849}.; . . unclassifiable (Anatomical System);cartilage;heart;spinal cord;skin;skeletal muscle;retina;breast;uterus;prostate;whole body;lung;larynx;thyroid;placenta;iris;liver;testis;head and neck;spleen;germinal center;kidney;brain; superior cervical ganglion;testis;globus pallidus;pons;trigeminal ganglion;parietal lobe; 0.43964 0.10342 -1.014084315 8.16230243 269.82126 3.52455 ULK3 0.0169271585091179 0.978196594411786 0.00487624707909637 unc-51 like kinase 3 FUNCTION: Serine/threonine protein kinase that acts as a regulator of Sonic hedgehog (SHH) signaling and autophagy. Acts as a negative regulator of SHH signaling in the absence of SHH ligand: interacts with SUFU, thereby inactivating the protein kinase activity and preventing phosphorylation of GLI proteins (GLI1, GLI2 and/or GLI3). Positively regulates SHH signaling in the presence of SHH: dissociates from SUFU, autophosphorylates and mediates phosphorylation of GLI2, activating it and promoting its nuclear translocation. Phosphorylates in vitro GLI2, as well as GLI1 and GLI3, although less efficiently. Also acts as a regulator of autophagy: following cellular senescence, able to induce autophagy. {ECO:0000269|PubMed:19279323, ECO:0000269|PubMed:19878745, ECO:0000269|PubMed:20643644}.; . TISSUE SPECIFICITY: Widely expressed. Highest levels observed in fetal brain. In adult tissues, high levels in brain, liver and kidney, moderate levels in testis and adrenal gland and low levels in heart, lung, stomach, thymus, prostate and placenta. In the brain, highest expression in the hippocampus, high levels also detected in the cerebellum, olfactory bulb and optic nerve. In the central nervous system, lowest levels in the spinal cord. {ECO:0000269|PubMed:19878745}.; . . 0.23268 0.14958 -0.490397599 22.50530786 2924.6584 10.26271 ULK4 1.68589239610196e-23 0.0334504926903229 0.966549507309677 unc-51 like kinase 4 . . . unclassifiable (Anatomical System);medulla oblongata;nervous;skin;uterus;prostate;lung;bone;testis;spleen;germinal center;brain;stomach; dorsal root ganglion;subthalamic nucleus;testis - interstitial;superior cervical ganglion;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11490 . 1.70862952 96.44373673 5973.09032 16.07377 ULK4P1 . . . ULK4 pseudogene 1 . . . endometrium;colon;kidney; . . . . . . . ULK4P2 . . . ULK4 pseudogene 2 . . . . . . . . . . . ULK4P3 . . . ULK4 pseudogene 3 . . . lung;testis;colon;skeletal muscle; . . . . . . . UMAD1 . . . UBAP1-MVB12-associated (UMA) domain containing 1 . . . . . . . . . . . UMOD 3.18086247757233e-08 0.517029285103767 0.482970683087609 uromodulin FUNCTION: Uromodulin: Functions in biogenesis and organization of the apical membrane of epithelial cells of the thick ascending limb of Henle's loop (TALH), where it promotes formation of complex filamentous gel-like structure providing the water barrier permeability. May serve as a receptor for binding and endocytosis for cytokines (IL-1, IL-2) and TNF. Facilitates neutrophil migration across renal epithelial. {ECO:0000269|PubMed:20798515}.; DISEASE: Familial juvenile hyperuricemic nephropathy 1 (HNFJ1) [MIM:162000]: A renal disease characterized by juvenile onset of hyperuricemia, polyuria, progressive renal failure, and gout. The disease is associated with interstitial pathological changes resulting in fibrosis. {ECO:0000269|PubMed:12471200, ECO:0000269|PubMed:12629136, ECO:0000269|PubMed:12900848, ECO:0000269|PubMed:14569098, ECO:0000269|PubMed:14570709, ECO:0000269|PubMed:15086896, ECO:0000269|PubMed:15575003, ECO:0000269|PubMed:15983957, ECO:0000269|PubMed:17010121, ECO:0000269|PubMed:21060763, ECO:0000269|PubMed:22776760, ECO:0000269|PubMed:23197950, ECO:0000269|PubMed:23988501}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Medullary cystic kidney disease 2 (MCKD2) [MIM:603860]: A form of tubulointerstitial nephropathy characterized by formation of renal cysts at the corticomedullary junction. It is characterized by adult onset of impaired renal function and salt wasting resulting in end-stage renal failure by the sixth decade. {ECO:0000269|PubMed:12471200, ECO:0000269|PubMed:14531790, ECO:0000269|PubMed:17010121, ECO:0000269|PubMed:25436415}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Glomerulocystic kidney disease with hyperuricemia and isosthenuria (GCKDHI) [MIM:609886]: A renal disorder characterized by a cystic dilation of Bowman space, a collapse of glomerular tuft, and hyperuricemia due to low fractional excretion of uric acid and severe impairment of urine concentrating ability. {ECO:0000269|PubMed:14570709, ECO:0000269|PubMed:17010121}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the tubular cells of the kidney (at protein level). Synthesized exclusively in the kidney. Expressed exclusively by epithelial cells of the thick ascending limb of Henle's loop (TALH) and of distal convoluted tubule lumen. Most abundant protein in normal urine. {ECO:0000269|PubMed:22776760, ECO:0000269|PubMed:23988501, ECO:0000269|PubMed:7028707}.; unclassifiable (Anatomical System);kidney;brain; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;kidney; 0.12990 0.24526 -0.554717505 19.79830149 836.45901 5.66394 UMODL1 2.27450532319603e-24 0.00280167902158799 0.997198320978412 uromodulin like 1 . . TISSUE SPECIFICITY: Isoform 4 is expressed at low level in kidney, testis and fetal thymus. Isoform 3 is expressed at low level in prostate, testis and fetal thymus. {ECO:0000269|PubMed:15194491}.; . . 0.14309 . 3.92468431 99.65204058 5976.01845 16.08277 UMODL1-AS1 . . . UMODL1 antisense RNA 1 . . . . . 0.07539 . . . . . UMPS 0.000109217442760822 0.81904571945913 0.180845063098109 uridine monophosphate synthetase . DISEASE: Orotic aciduria 1 (ORAC1) [MIM:258900]: A disorder of pyrimidine metabolism resulting in megaloblastic anemia and orotic acid crystalluria that is frequently associated with some degree of physical and mental retardation. A minority of cases have additional features, particularly congenital malformations and immune deficiencies. {ECO:0000269|PubMed:9042911}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;myocardium;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion; 0.14680 0.27219 -0.424258538 25.56027365 735.58897 5.38201 UNC5A 0.996259997309535 0.00373999187972625 1.08107385330006e-08 unc-5 netrin receptor A FUNCTION: Receptor for netrin required for axon guidance. Functions in the netrin signaling pathway and promotes neurite outgrowth in response to NTN1. Mediates axon repulsion of neuronal growth cones in the developing nervous system in response to netrin. Axon repulsion in growth cones may be mediated by its association with DCC that may trigger signaling for repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. {ECO:0000250|UniProtKB:O08721}.; . . unclassifiable (Anatomical System);cartilage;ovary;tongue;islets of Langerhans;blood;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;frontal lobe;placenta;macula lutea;visual apparatus;alveolus;head and neck;brain; . 0.50482 0.12149 -0.839512508 11.40009436 432.35232 4.34052 UNC5B 0.000746121343818483 0.999099861112 0.000154017544181553 unc-5 netrin receptor B FUNCTION: Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding. Axon repulsion in growth cones may be caused by its association with DCC that may trigger signaling for repulsion (By similarity). Functions as netrin receptor that negatively regulates vascular branching during angiogenesis. Mediates retraction of tip cell filopodia on endothelial growth cones in response to netrin (By similarity). It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (PubMed:12598906). Mediates apoptosis by activating DAPK1. In the absence of NTN1, activates DAPK1 by reducing its autoinhibitory phosphorylation at Ser-308 thereby increasing its catalytic activity (By similarity). {ECO:0000250|UniProtKB:O08722, ECO:0000250|UniProtKB:Q8K1S3, ECO:0000269|PubMed:12598906}.; . TISSUE SPECIFICITY: Highly expressed in brain. Also expressed at lower level in developing lung, cartilage, kidney and hematopoietic and immune tissues. {ECO:0000269|PubMed:12359238}.; ovary;parathyroid;choroid;skin;uterus;prostate;endometrium;larynx;synovium;bone;testis;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;adrenal cortex;blood;skeletal muscle;pancreas;lung;placenta;hippocampus;liver;spleen;head and neck;kidney; dorsal root ganglion;thalamus;superior cervical ganglion;globus pallidus;ciliary ganglion;caudate nucleus;atrioventricular node;trigeminal ganglion;parietal lobe;cerebellum; 0.94990 0.14462 -1.626115313 2.878037273 1193.04511 6.55138 UNC5B-AS1 . . . UNC5B antisense RNA 1 . . . . . . . . . . . UNC5C 0.0169270053737034 0.983032107955799 4.08866704979961e-05 unc-5 netrin receptor C FUNCTION: Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding. Axon repulsion in growth cones may be caused by its association with DCC that may trigger signaling for repulsion. Also involved in corticospinal tract axon guidances independently of DCC. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. {ECO:0000250|UniProtKB:O08747}.; . TISSUE SPECIFICITY: Mainly expressed in brain. Also expressed in kidney. Not expressed in developing or adult lung. {ECO:0000269|PubMed:9782087}.; unclassifiable (Anatomical System);amygdala;pancreas;frontal lobe;heart;thyroid;testis;kidney;brain; superior cervical ganglion;uterus corpus;pons;atrioventricular node; 0.61209 0.13551 -0.437212558 24.67563105 5283.17793 15.01744 UNC5CL 1.666644191506e-07 0.40318084399274 0.596818989342841 unc-5 family C-terminal like FUNCTION: Inhibits NF-kappa-B-dependent transcription by impairing NF-kappa-B binding to its targets. {ECO:0000269|PubMed:14769797}.; . TISSUE SPECIFICITY: Expressed in pancreas, liver and kidney. {ECO:0000269|PubMed:14769797}.; unclassifiable (Anatomical System);pancreas;lung;cartilage;islets of Langerhans;liver;colon;kidney;brain; dorsal root ganglion;superior cervical ganglion;temporal lobe;atrioventricular node;caudate nucleus;pons;skeletal muscle;skin;uterus corpus;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.60201 0.09442 1.512041961 95.47062987 535.67038 4.71781 UNC5D 0.849201861283474 0.15079722144182 9.17274706343307e-07 unc-5 netrin receptor D FUNCTION: Receptor for the netrin NTN4 that promotes neuronal cell survival (By similarity). Plays a role in cell-cell adhesion and cell guidance. Receptor for netrin involved in cell migration. Plays a role in axon guidance by mediating axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding (By similarity). May play a role in apoptosis in response to DNA damage (PubMed:24691657). It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (PubMed:24519068). Mediates cell-cell adhesion via its interaction with FLRT3 on an adjacent cell (By similarity). {ECO:0000250|UniProtKB:Q8K1S2, ECO:0000305|PubMed:24519068, ECO:0000305|PubMed:24691657}.; . . unclassifiable (Anatomical System);amygdala;lung;frontal lobe;islets of Langerhans;colon;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.90955 0.10096 -0.686998355 15.26893135 182.39129 2.93414 UNC13A 0.999986711013614 1.32889863856676e-05 3.9419948960552e-18 unc-13 homolog A (C. elegans) FUNCTION: Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in most excitatory/glutamatergic but not inhibitory/GABA-mediated synapses (By similarity). Also involved in secretory granule priming in insulin secretion (By similarity). Interacts with FBXO45 (via SRY domain); leading to the degradation of UNC13A by the proteasome (By similarity). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000250, ECO:0000269|PubMed:23999003}.; . TISSUE SPECIFICITY: Expressed in pancreatic islet cells (PubMed:12871971). Expressed in melanocytes (PubMed:23999003). {ECO:0000269|PubMed:12871971, ECO:0000269|PubMed:23999003}.; unclassifiable (Anatomical System);breast;lung;frontal lobe;ovary;islets of Langerhans;placenta;visual apparatus;blood;brain;skeletal muscle; amygdala;whole brain;superior cervical ganglion;occipital lobe;cerebellum peduncles;temporal lobe;pons;prefrontal cortex;globus pallidus;appendix;trigeminal ganglion;cingulate cortex;parietal lobe; 0.20708 . -1.697674421 2.583156405 1626.22937 7.45646 UNC13B 6.60361794417271e-05 0.999933963703763 1.16795134900326e-10 unc-13 homolog B (C. elegans) FUNCTION: Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity- depending refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in a subset of excitatory/glutamatergic but not inhibitory/GABA-mediated synapses (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in kidney cortical epithelial cells and brain. {ECO:0000269|PubMed:9607201}.; . . 0.45619 0.14072 -2.888976416 0.589761736 674.04383 5.18709 UNC13C 3.68783135222941e-07 0.999999623001726 8.21513925494729e-09 unc-13 homolog C (C. elegans) FUNCTION: May play a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. May be involved in the regulation of synaptic transmission at parallel fiber - Purkinje cell synapses (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Exclusively expressed in brain.; unclassifiable (Anatomical System);hypothalamus;macula lutea;visual apparatus;testis;fovea centralis;brain;skin;skeletal muscle;retina;cerebellum; amygdala;occipital lobe;subthalamic nucleus;medulla oblongata;cerebellum peduncles;temporal lobe;globus pallidus;pons;parietal lobe;cingulate cortex;cerebellum; 0.11028 0.09988 -1.666641783 2.701108752 3716.04 11.89577 UNC13D 2.52003157333038e-12 0.991404985798467 0.00859501419901328 unc-13 homolog D (C. elegans) FUNCTION: Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. Regulates assembly of recycling and late endosomal structures, leading to the formation of an endosomal exocytic compartment that fuses with perforin-containing granules at the immunologic synapse and licences them for exocytosis. Regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells. {ECO:0000269|PubMed:15548590, ECO:0000269|PubMed:17237785}.; DISEASE: Familial hemophagocytic lymphohistiocytosis 3 (FHL3) [MIM:608898]: A rare disorder characterized by immune dysregulation with hypercytokinemia, defective function of natural killer cell, and massive infiltration of several organs by activated lymphocytes and macrophages. The clinical features of the disease include fever, hepatosplenomegaly, cytopenia, and less frequently neurological abnormalities ranging from irritability and hypotonia to seizures, cranial nerve deficits and ataxia. {ECO:0000269|PubMed:14622600}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at high levels in spleen, thymus and leukocytes. Also expressed in lung and placenta, and at very low levels in brain, heart, skeletal muscle and kidney. Expressed in cytotoxic T-lymphocytes (CTL) and mast cells. {ECO:0000269|PubMed:14622600, ECO:0000269|PubMed:15548590}.; ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;larynx;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; atrioventricular node; 0.10227 0.16014 0.080772655 59.43618778 1789.38484 7.80779 UNC45A 9.49307248350221e-08 0.99588987092334 0.0041100341459356 unc-45 myosin chaperone A FUNCTION: Acts as co-chaperone for HSP90. Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell. May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen (By similarity). {ECO:0000250, ECO:0000269|PubMed:12119110, ECO:0000269|PubMed:16478993, ECO:0000305}.; . TISSUE SPECIFICITY: Detected in peripheral blood leukocytes, bone marrow, adrenal gland, trachea, spinal cord, thyroid, lymph node and stomach. {ECO:0000269|PubMed:12119110}.; . . 0.12253 0.10814 -1.098660656 6.95329087 889.01867 5.80699 UNC45B 2.76564282824349e-08 0.995122812932108 0.00487715941146385 unc-45 myosin chaperone B FUNCTION: Acts as a co-chaperone for HSP90 and is required for proper folding of the myosin motor domain. Plays a role in sarcomere formation during muscle cell development. Is necessary for normal early lens development. {ECO:0000250|UniProtKB:Q6DGE9, ECO:0000250|UniProtKB:Q8CGY6}.; DISEASE: Cataract 43 (CTRCT43) [MIM:616279]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. {ECO:0000269|PubMed:24549050}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in eye lens tissues. {ECO:0000269|PubMed:24549050}.; unclassifiable (Anatomical System);myocardium; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;skeletal muscle; 0.21755 0.10896 0.297596326 71.67964142 1501.76084 7.20898 UNC50 0.0116183072135509 0.949870855712628 0.0385108370738208 unc-50 homolog (C. elegans) FUNCTION: May be involved in cell surface expression of neuronal nicotinic receptors. Binds RNA (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Present in periodontal ligament fibroblasts (at protein level). {ECO:0000269|PubMed:17004066}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;endometrium;bone;testis;amniotic fluid;middle ear;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lung;internal ear;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;aorta;stomach;thymus; amygdala;whole brain;occipital lobe;testis - interstitial;testis - seminiferous tubule;hypothalamus;thyroid;placenta;prefrontal cortex;testis; 0.10703 0.10379 0.080983847 59.76055674 1142.04699 6.44431 UNC79 0.999999999973909 2.60914245816102e-11 1.2085488336087e-30 unc-79 homolog (C. elegans) FUNCTION: Component of the NALCN sodium channel complex, a cation channel activated either by neuropeptides substance P or neurotensin that controls neuronal excitability. {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;sympathetic chain;testis;brain; dorsal root ganglion;superior cervical ganglion;olfactory bulb;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;cerebellum; 0.13734 0.11720 -1.113491624 6.634819533 491.26186 4.56078 UNC80 0.139839110565612 0.856011009867762 0.00414987956662591 unc-80 homolog, NALCN activator FUNCTION: Component of the NALCN sodium channel complex, a cation channel activated either by neuropeptides substance P or neurotensin that controls neuronal excitability. {ECO:0000250}.; . . lung;frontal lobe;nervous;testis;brain;skeletal muscle; amygdala;dorsal root ganglion;superior cervical ganglion;tongue;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skin; 0.61288 . 0.992010122 90.49893843 987.20517 6.05851 UNC93A 1.37725514829586e-06 0.610062546782628 0.389936075962224 unc-93 homolog A (C. elegans) . . TISSUE SPECIFICITY: Expressed in testis, small intestine, spleen, prostate and ovary. {ECO:0000269|PubMed:12381271}.; unclassifiable (Anatomical System);lung;heart;liver;spleen;stomach; . 0.08771 0.10097 2.53746678 98.71431941 4005.17839 12.52307 UNC93B1 0.513837375928464 0.482295391231624 0.00386723283991288 unc-93 homolog B1 (C. elegans) FUNCTION: Plays an important role in innate and adaptive immunity by regulating nucleotide-sensing Toll-like receptor (TLR) signaling. Required for the transport of a subset of TLRs (including TLR3, TLR7 and TLR9) from the endoplasmic reticulum to endolysosomes where they can engage pathogen nucleotides and activate signaling cascades. May play a role in autoreactive B- cells removal. {ECO:0000269|PubMed:19006693}.; DISEASE: Herpes simplex encephalitis 1 (HSE1) [MIM:610551]: A rare complication of human herpesvirus 1 (HHV-1) infection, occurring in only a small minority of HHV-1 infected individuals. HSE is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Onset is over several days and involves fever, headache, seizures, stupor, and often coma, frequently with a fatal outcome. {ECO:0000269|PubMed:16973841}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Mutations in UNC93B1 resulting in autosomal recessive UNC93B1 deficieny predispose otherwise healthy individuals to isolated herpes simplex encephalitis due to impaired IFNs production. UNC93B1 deficieny, however, does not compromise immunity to most pathogens, unlike most known primary immunodeficiencies.; TISSUE SPECIFICITY: Expressed in plasmocytoid dendritic cells (at protein level). Highly expressed in antigen-presenting cells. Expressed in heart, and at lower level in kidney. Expressed at low level in other tissues. {ECO:0000269|PubMed:11867227, ECO:0000269|PubMed:18082565, ECO:0000269|PubMed:21642595}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;tongue;blood;lens;breast;pancreas;lung;placenta;macula lutea;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . . 0.17596 . . 149.92935 2.66921 UNC93B2 . . . unc-93 homolog B2 pseudogene (C. elegans) . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;pancreas;lung;placenta;macula lutea;spleen;kidney;mammary gland;stomach; . . . . . . . UNC93B3 . . . unc-93 homolog B3 pseudogene (C. elegans) . . . . . . . . . . . UNC93B4 . . . unc-93 homolog B4 pseudogene (C. elegans) . . . . . . . . . . . UNC93B5 . . . unc-93 homolog B5 pseudogene (C. elegans) . . . . . . . . . . . UNC93B6 . . . unc-93 homolog B6 pseudogene (C. elegans) . . . . . . . . . . . UNC93B7 . . . unc-93 homolog B7 pseudogene (C. elegans) . . . . . . . . . . . UNC93B8 . . . unc-93 homolog B8 pseudogene (C. elegans) . . . . . . . . . . . UNC119 0.0097174210089495 0.818904149063923 0.171378429927127 unc-119 lipid binding chaperone FUNCTION: Involved in synaptic functions in photoreceptor cells, the signal transduction in immune cells as a Src family kinase activator, endosome recycling, the uptake of bacteria and endocytosis, protein trafficking in sensory neurons and as lipid- binding chaperone with specificity for a diverse subset of myristoylated proteins. Specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Binds myristoylated GNAT1 and is required for G-protein localization and trafficking in sensory neurons. Probably plays a role in trafficking proteins in photoreceptor cells. Plays important roles in mediating Src family kinase signals for the completion of cytokinesis via RAB11A. {ECO:0000269|PubMed:12496276, ECO:0000269|PubMed:14757743, ECO:0000269|PubMed:19381274, ECO:0000269|PubMed:21642972, ECO:0000269|PubMed:22085962, ECO:0000269|PubMed:23535298, ECO:0000305|PubMed:22960633}.; DISEASE: Note=Defects in UNC119 may be a cause of cone-rod dystrophy. A mutation was found in a 57-year-old woman with late- onset cone-rod dystrophy: from 40 year old, the patient suffered from poor night vision, defective color vision and light- sensitivity. At 57 year old, she displayed reduced visual acuity, myopa, macular atrophy and pericentral ring scotomas. The disease was caused by a heterozygous mutation causing premature termination and truncated UNC119 protein with dominant-negative effect. {ECO:0000269|PubMed:11006213}.; DISEASE: Immunodeficiency 13 (IMD13) [MIM:615518]: A rare and heterogeneous syndrome defined by a reproducible reduction in the CD4 T-lymphocyte count (less than 300 cells per microliter or less than 20% of total T-cells) in the absence of HIV infection or other known causes of immunodeficiency. IMD13 predisposes to infections and malignancy. {ECO:0000269|PubMed:22184408}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Abundantly expressed in retina, in photoreceptor synapses and inner segments. Expressed in a much lesser extent in several other tissues. {ECO:0000269|PubMed:9761287}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;oesophagus;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;macula lutea;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;whole blood; 0.51137 0.19235 -0.339715008 30.06605331 54.47917 1.47560 UNC119B 0.677325341021738 0.318013562757608 0.00466109622065408 unc-119 lipid binding chaperone B FUNCTION: Myristoyl-binding protein that acts as a cargo adapter: specifically binds the myristoyl moiety of a subset of N- terminally myristoylated proteins and is required for their localization. Binds myristoylated NPHP3 and plays a key role in localization of NPHP3 to the primary cilium membrane. Does not bind all myristoylated proteins. Probably plays a role in trafficking proteins in photoreceptor cells. {ECO:0000269|PubMed:22085962}.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;skin;retina;uterus;whole body;endometrium;synovium;bone;thyroid;iris;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;amnion;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;ciliary ganglion; 0.25440 . . . 32.10807 1.00769 UNCX . . . UNC homeobox FUNCTION: Transcription factor involved in somitogenesis and neurogenesis. Required for the maintenance and differentiation of particular elements of the axial skeleton. May act upstream of PAX9. Plays a role in controlling the development of connections of hypothalamic neurons to pituitary elements, allowing central neurons to reach the peripheral blood circulation and to deliver hormones for control of peripheral functions (By similarity). {ECO:0000250}.; . . . . 0.13866 . . . 35.41564 1.06889 UNG 0.0465811527139078 0.928874885289313 0.0245439619967788 uracil DNA glycosylase FUNCTION: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.; DISEASE: Immunodeficiency with hyper-IgM 5 (HIGM5) [MIM:608106]: A rare immunodeficiency syndrome characterized by normal or elevated serum IgM levels with absence of IgG, IgA, and IgE. It results in a profound susceptibility to bacterial infections. {ECO:0000269|PubMed:12958596}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 1 is widely expressed with the highest expression in skeletal muscle, heart and testicles. Isoform 2 has the highest expression levels in tissues containing proliferating cells.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; testis; 0.56946 0.45556 -0.47017169 23.25430526 41.19513 1.20535 UNGP1 . . . uracil-DNA glycosylase pseudogene 1 . . . . . . . . . . . UNGP2 . . . uracil-DNA glycosylase pseudogene 2 . . . . . . . . . . . UNGP3 . . . uracil-DNA glycosylase pseudogene 3 . . . . . . . . . . . UNK 0.994321108472501 0.0056788854601018 6.06739686498387e-09 unkempt family zinc finger FUNCTION: Sequence-specific RNA-binding protein which plays an important role in the establishment and maintenance of the early morphology of cortical neurons during embryonic development. Acts as a translation repressor and controls a translationally regulated cell morphology program to ensure proper structuring of the nervous system. Translational control depends on recognition of its binding element within target mRNAs which consists of a mandatory UAG trimer upstream of a U/A-rich motif. Associated with polysomes (PubMed:25737280). {ECO:0000269|PubMed:25737280}.; . . colon;skin;uterus;prostate;optic nerve;whole body;endometrium;cerebral cortex;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;breast;lung;placenta;visual apparatus;hypopharynx;head and neck;kidney;mammary gland;cerebellum; . 0.73947 0.20580 . . 127.43339 2.46158 UNKL 0.0988570192094062 0.866392359676559 0.0347506211140348 unkempt family like zinc finger FUNCTION: May participate in a protein complex showing an E3 ligase activity regulated by RAC1. Ubiquitination is directed towards itself and possibly other substrates, such as SMARCD2/BAF60b. Intrinsic E3 ligase activity has not been proven. {ECO:0000269|PubMed:20148946}.; . . unclassifiable (Anatomical System);ovary;heart;blood;lens;vein;skeletal muscle;retina;prostate;whole body;lung;frontal lobe;placenta;liver;pituitary gland;testis;spleen;kidney;germinal center;brain;stomach;tonsil; globus pallidus; 0.24267 . . . 179.13605 2.90760 UOX . . . urate oxidase (pseudogene) . . . . . . . . . . . UPB1 1.85086913944901e-07 0.657758506214846 0.34224130869824 ureidopropionase, beta FUNCTION: Converts N-carbamoyl-beta-aminoisobutyrate and N- carbamoyl-beta-alanine (3-ureidopropanoate) to, respectively, beta-aminoisobutyrate and beta-alanine, ammonia and carbon dioxide.; DISEASE: Beta-ureidopropionase deficiency (BUPD) [MIM:613161]: An inborn error of metabolism due to a defect in pyrimidine degradation. It is characterized by muscular hypotonia, dystonic movements, scoliosis, microcephaly and severe developmental delay. Patients show strongly elevated levels of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyric acid in plasma, cerebrospinal fluid and urine. {ECO:0000269|PubMed:15385443}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;liver;kidney;brain;skin;peripheral nerve;thymus; superior cervical ganglion;liver;testis;atrioventricular node;kidney;trigeminal ganglion; 0.09614 0.18999 -0.686998355 15.26893135 107.35908 2.24924 UPF1 0.999926075341711 7.39246575288407e-05 7.59826429447073e-13 UPF1, RNA helicase and ATPase FUNCTION: RNA-dependent helicase and ATPase required for nonsense- mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. Recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1- eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) (located 50-55 or more nucleotides downstream from the termination codon) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Phosphorylated UPF1 is recognized by EST1B/SMG5, SMG6 and SMG7 which are thought to provide a link to the mRNA degradation machinery involving exonucleolytic and endonucleolytic pathways, and to serve as adapters to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation and allowing the recycling of NMD factors. UPF1 can also activate NMD without UPF2 or UPF3, and in the absence of the NMD-enhancing downstream EJC indicative for alternative NMD pathways. Plays a role in replication-dependent histone mRNA degradation at the end of phase S; the function is independent of UPF2. For the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. The ATPase activity of UPF1 is required for disassembly of mRNPs undergoing NMD. Essential for embryonic viability. {ECO:0000269|PubMed:11163187, ECO:0000269|PubMed:16086026, ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:21145460, ECO:0000269|PubMed:21419344}.; . TISSUE SPECIFICITY: Ubiquitous.; myocardium;lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach;thymus;cerebellum; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;cerebellum peduncles;testis;trigeminal ganglion;skeletal muscle;cerebellum; 0.74240 0.22951 -1.528486521 3.385232366 41.94856 1.22209 UPF2 0.99999826926484 1.73073515987492e-06 8.10788158356782e-17 UPF2 regulator of nonsense transcripts homolog (yeast) FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC). Recruited by UPF3B associated with the EJC core at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF3B stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA. {ECO:0000269|PubMed:11163187, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:18066079}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11073994}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);meninges;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pia mater;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; subthalamic nucleus;testis - interstitial;medulla oblongata;testis - seminiferous tubule;testis;pons;atrioventricular node; 0.89697 . -0.885424753 10.4623732 286.42271 3.62468 UPF3A 0.000813153350217953 0.983379043176636 0.0158078034731461 UPF3 regulator of nonsense transcripts homolog A (yeast) FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC) and serving as link between the EJC core and NMD machinery. Recruits UPF2 at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2- UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. However, UPF3A is shown to be only marginally active in NMD as compared to UPF3B. Binds spliced mRNA upstream of exon-exon junctions. In vitro, weakly stimulates translation. {ECO:0000269|PubMed:11163187, ECO:0000269|PubMed:16601204}.; . TISSUE SPECIFICITY: Isoform 1 is strongly expressed in testis, uterus, muscle, fetal brain and spinal cord. Isoform 2 is strongly expressed in fetal brain and spinal cord. {ECO:0000269|PubMed:11113196}.; unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;blood;skin;bone marrow;uterus;prostate;optic nerve;lung;larynx;thyroid;placenta;visual apparatus;liver;testis;cervix;head and neck;spleen;germinal center;brain;stomach; . 0.07571 0.09432 0.174625237 65.9648502 1652.92329 7.51496 UPF3AP1 . . . UPF3A pseudogene 1 . . . . . . . . . . . UPF3AP2 . . . UPF3A pseudogene 2 . . . . . . . . . . . UPF3AP3 . . . UPF3A pseudogene 3 . . . . . . . . . . . UPF3B 0.933766901129754 0.0662200835234319 1.30153468140699e-05 UPF3 regulator of nonsense transcripts homolog B (yeast) FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC) and serving as link between the EJC core and NMD machinery. Recruits UPF2 at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2- UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF2 stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA upstream of exon-exon junctions. In vitro, stimulates translation; the function is independent of association with UPF2 and components of the EJC core. {ECO:0000269|PubMed:11163187, ECO:0000269|PubMed:12718880, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:16601204, ECO:0000269|PubMed:18066079}.; . TISSUE SPECIFICITY: Expressed in testis, uterus, prostate, heart, muscle, brain, spinal cord and placenta. {ECO:0000269|PubMed:11113196}.; lymphoreticular;ovary;salivary gland;intestine;colon;skin;uterus;prostate;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;prefrontal cortex;trigeminal ganglion; 0.26223 0.11959 0.016664174 55.21939137 39.35054 1.16393 UPF3BP4 . . . UPF3B pseudogene 4 . . . . . . . . . . . UPK1A 3.36196571713144e-05 0.578698070602963 0.421268309739866 uroplakin 1A FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apical membrane through AUM/cytoskeletal interactions (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: High expression restricted to ureteric urothelium (most superficial cells); low expression in prostate. Expression in normal urothelial cells is lost in culture. Some expression in tumor cell lines derived from urothelial malignancies. {ECO:0000269|PubMed:15913809, ECO:0000269|PubMed:9846985}.; uterus;prostate;heart;urinary;bladder;skin; dorsal root ganglion;atrioventricular node;skeletal muscle; 0.12830 0.09461 0.92967242 89.79122435 1629.30742 7.46265 UPK1A-AS1 . . . UPK1A antisense RNA 1 . . . . . . . . . . . UPK1B 4.50333086319676e-05 0.642601160047686 0.357353806643682 uroplakin 1B FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apical membrane through AUM/cytoskeletal interactions (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Bladder epithelium.; ovary;salivary gland;colon;prostate;endometrium;bladder;brain;gall bladder;tonsil;unclassifiable (Anatomical System);tongue;islets of Langerhans;hypothalamus;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;trachea;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18321 0.11968 0.305084559 72.22811984 316.64369 3.78041 UPK2 2.80119065022381e-06 0.176141322840485 0.823855875968865 uroplakin 2 FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in regulating the assembly of the AUM (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in ureter. {ECO:0000269|PubMed:9846985}.; brain; superior cervical ganglion;trigeminal ganglion; 0.36324 0.15729 0.082802743 60.09082331 412.6635 4.25333 UPK3A 1.41130198024748e-07 0.115685952341464 0.884313906528338 uroplakin 3A FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in AUM-cytoskeleton interaction in terminally differentiated urothelial cells. It also contributes to the formation of urothelial glycocalyx which may play an important role in preventing bacterial adherence (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in ureter. {ECO:0000269|PubMed:9846985}.; unclassifiable (Anatomical System);prostate;optic nerve;macula lutea;fovea centralis;choroid;lens;retina; prostate;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.07856 0.09953 0.885576705 89.14248644 189.17114 2.98594 UPK3B 0.000192328231865901 0.476338258150147 0.523469413617987 uroplakin 3B FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in AUM-cytoskeleton interaction in terminally differentiated urothelial cells. It also contributes to the formation of urothelial glycocalyx which may play an important role in preventing bacterial adherence (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;whole body;endometrium;larynx;testis;spleen;brain;cerebellum; dorsal root ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion; 0.07717 . 1.107875794 92.03821656 2059.35808 8.36327 UPK3BL . . . uroplakin 3B-like . . . lymph node;ovary;islets of Langerhans;colon;skin;bone marrow;uterus;frontal lobe;placenta;hypopharynx;head and neck;cervix;brain;bladder;thymus; . . . . . . . UPK3BP1 . . . uroplakin 3B pseudogene 1 . . . . . . . . . . . UPP1 9.00844799997619e-05 0.551066532898815 0.448843382621185 uridine phosphorylase 1 FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1- phosphate (PubMed:7488099). The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. {ECO:0000269|PubMed:7488099, ECO:0000305}.; . . ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;bone;testis;brain;artery;unclassifiable (Anatomical System);trophoblast;cartilage;islets of Langerhans;blood;lens;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;macula lutea;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;lung; 0.17281 0.18333 -0.203796826 38.81811748 26.02404 0.84579 UPP2 0.00202492321799246 0.91140689973035 0.0865681770516571 uridine phosphorylase 2 FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1- phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. Shows substrate specificity and accept uridine, deoxyuridine, and thymidine as well as the two pyrimidine nucleoside analogs 5-fluorouridine and 5-fluoro-2(')-deoxyuridine as substrates.; . TISSUE SPECIFICITY: Predominantly expressed in kidney. {ECO:0000269|PubMed:12849978}.; unclassifiable (Anatomical System);kidney;brain;gall bladder; ciliary ganglion; 0.11746 0.14710 -0.113792788 45.25831564 1226.95637 6.61915 UPP2-IT1 . . . UPP2 intronic transcript 1 . . . . . . . . . . . UPRT 0.814813817299778 0.184240365427091 0.000945817273131702 uracil phosphoribosyltransferase homolog . . TISSUE SPECIFICITY: Highly expressed in leukocytes, liver, spleen and thymus, with lower expression in brain, lung and skeletal muscle. {ECO:0000269|PubMed:17384901}.; . . 0.10613 0.23255 -0.075159878 47.78839349 3.42148 0.12479 UQCC1 0.00485442531990324 0.989054215169971 0.00609135951012512 ubiquinol-cytochrome c reductase complex assembly factor 1 FUNCTION: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex). Involved in cytochrome b translation and/or stability. {ECO:0000269|PubMed:24385928}.; . . . . 0.54483 0.10131 0.483275131 79.25218212 117.95061 2.36137 UQCC2 0.0595477327271092 0.868144296448296 0.0723079708245942 ubiquinol-cytochrome c reductase complex assembly factor 2 FUNCTION: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex). Plays a role in the modulation of respiratory chain activities such as oxygen consumption and ATP production and via its modulation of the respiratory chain activity can regulate skeletal muscle differentiation and insulin secretion by pancreatic beta-cells. Involved in cytochrome b translation and/or stability. {ECO:0000269|PubMed:22363741, ECO:0000269|PubMed:24385928}.; . TISSUE SPECIFICITY: Pancreas, skeletal muscle, kidney, liver and heart. {ECO:0000269|PubMed:22363741}.; . . 0.01031 . 0.058937498 58.26256192 150.80136 2.68278 UQCC3 . . . ubiquinol-cytochrome c reductase complex assembly factor 3 FUNCTION: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin- binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology. {ECO:0000269|PubMed:25008109, ECO:0000269|PubMed:25605331}.; DISEASE: Mitochondrial complex III deficiency, nuclear 9 (MC3DN9) [MIM:616111]: A form of mitochondrial complex III deficiency, a disorder of the mitochondrial respiratory chain resulting in a highly variable phenotype depending on which tissues are affected. MC3DN9 clinical features include feeding difficulties, hypoglycemia, severe lactic acidosis, and delayed psychomotor development. {ECO:0000269|PubMed:25008109}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . 0.08053 0.613741468 83.06794055 . . UQCR10 0.149717438688814 0.632755931913456 0.21752662939773 ubiquinol-cytochrome c reductase, complex III subunit X FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This subunit interacts with cytochrome c1 (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;umbilical cord;tongue;islets of Langerhans;developmental;colon;blood;lens;skin;skeletal muscle;uterus;prostate;whole body;lung;cochlea;placenta;visual apparatus;pituitary gland;testis;kidney;brain;stomach; whole brain;testis - interstitial;medulla oblongata;thalamus;occipital lobe;heart;cerebellum peduncles;temporal lobe;caudate nucleus;pons;skeletal muscle;testis;kidney;cingulate cortex; . . 0.391453969 75.87284737 1464.59546 7.13603 UQCR11 0.0305034614325173 0.595980383610267 0.373516154957216 ubiquinol-cytochrome c reductase, complex III subunit XI FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain.; . . myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;bladder;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;cerebral cortex;synovium;bone;testis;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;placenta;kidney;stomach;aorta; whole brain;thalamus;heart;temporal lobe;liver;kidney;skeletal muscle; 0.14335 0.14499 -0.009020804 52.8544468 8.08743 0.29633 UQCRB 0.206960117710418 0.751061385573403 0.0419784967161791 ubiquinol-cytochrome c reductase binding protein FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This component is involved in redox-linked proton pumping.; DISEASE: Mitochondrial complex III deficiency, nuclear 3 (MC3DN3) [MIM:615158]: A disorder of the mitochondrial respiratory chain resulting in a highly variable phenotype depending on which tissues are affected. Clinical features include mitochondrial encephalopathy, psychomotor retardation, ataxia, severe failure to thrive, liver dysfunction, renal tubulopathy, muscle weakness and exercise intolerance. {ECO:0000269|PubMed:12709789}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;tonsil;heart;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;lung;pia mater;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;dorsal root ganglion;superior cervical ganglion;occipital lobe;medulla oblongata;temporal lobe;pons;skeletal muscle;subthalamic nucleus;globus pallidus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.15256 0.18299 0.147123112 64.11299835 240.30443 3.34820 UQCRBP1 . . . ubiquinol-cytochrome c reductase binding protein pseudogene 1 . . . . . . . . . . . UQCRBP2 . . . ubiquinol-cytochrome c reductase binding protein pseudogene 2 . . . . . . . . . . . UQCRBP3 . . . ubiquinol-cytochrome c reductase binding protein pseudogene 3 . . . . . . . . . . . UQCRC1 0.132467103146211 0.866597703776216 0.000935193077573351 ubiquinol-cytochrome c reductase core protein I FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1.; . . myocardium;lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;nervous;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;head and neck;kidney;stomach; whole brain;thalamus;lung;heart;liver;testis;kidney;skeletal muscle; 0.19556 0.24110 -0.268115223 34.70747818 259.99619 3.46496 UQCRC2 0.00723554333965841 0.989327849656086 0.0034366070042555 ubiquinol-cytochrome c reductase core protein II FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. The core protein 2 is required for the assembly of the complex.; DISEASE: Mitochondrial complex III deficiency, nuclear 5 (MC3DN5) [MIM:615160]: A disorder of the mitochondrial respiratory chain resulting in a highly variable phenotype depending on which tissues are affected. Clinical features include mitochondrial encephalopathy, psychomotor retardation, ataxia, severe failure to thrive, liver dysfunction, renal tubulopathy, muscle weakness and exercise intolerance. {ECO:0000269|PubMed:23281071}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;germinal center;brain;bladder;gall bladder;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; amygdala;thalamus;occipital lobe;medulla oblongata;subthalamic nucleus;globus pallidus;pons;cingulate cortex;skeletal muscle;parietal lobe; 0.36722 0.28097 0.218717575 68.27081859 899.56699 5.84180 UQCRC2P1 . . . ubiquinol-cytochrome c reductase core protein II pseudogene 1 . . . . . . . . . . . UQCRFS1 0.694438038047755 0.288091521236677 0.0174704407155682 ubiquinol-cytochrome c reductase, Rieske iron-sulfur polypeptide 1 FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.; . . myocardium;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum; . 0.61627 0.22005 -0.207437529 38.2814343 10.73011 0.38981 UQCRFS1P1 . . . ubiquinol-cytochrome c reductase, Rieske iron-sulfur polypeptide 1 pseudogene 1 . . . . . . 0.22005 . . . . UQCRFS1P2 . . . ubiquinol-cytochrome c reductase, Rieske iron-sulfur polypeptide 1 pseudogene 2 . . . . . . . . . . . UQCRFS1P3 . . . ubiquinol-cytochrome c reductase, Rieske iron-sulfur polypeptide 1 pseudogene 3 . . . . . . . . . . . UQCRH 0.218440721378243 0.743640307301142 0.0379189713206149 ubiquinol-cytochrome c reductase hinge protein FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1.; . . myocardium;lymphoreticular;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;thyroid;bladder;brain;heart;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;oesophagus;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;placenta;hippocampus;duodenum;kidney;stomach;aorta; . 0.91654 0.12771 0.147123112 64.11299835 668.20699 5.16953 UQCRHL . . . ubiquinol-cytochrome c reductase hinge protein like FUNCTION: May be a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1. {ECO:0000250|UniProtKB:P00127}.; . . . . . . . . . . UQCRHP1 . . . ubiquinol-cytochrome c reductase hinge protein pseudogene 1 . . . . . . . . . . . UQCRHP2 . . . ubiquinol-cytochrome c reductase hinge protein pseudogene 2 . . . . . . . . . . . UQCRHP3 . . . ubiquinol-cytochrome c reductase hinge protein pseudogene 3 . . . . . . . . . . . UQCRHP4 . . . ubiquinol-cytochrome c reductase hinge protein pseudogene 4 . . . . . . . . . . . UQCRQ 0.0919129783108912 0.766573744546559 0.14151327714255 ubiquinol-cytochrome c reductase complex III subunit VII FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This subunit, together with cytochrome b, binds to ubiquinone.; DISEASE: Mitochondrial complex III deficiency, nuclear 4 (MC3DN4) [MIM:615159]: A disorder of the mitochondrial respiratory chain resulting in a highly variable phenotype depending on which tissues are affected. Clinical features include mitochondrial encephalopathy, psychomotor retardation, ataxia, severe failure to thrive, liver dysfunction, renal tubulopathy, muscle weakness and exercise intolerance. {ECO:0000269|PubMed:18439546}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.01756 0.05504 0.080983847 59.76055674 9.61818 0.35401 URAD 0.00378363577582596 0.405158157115933 0.591058207108241 ureidoimidazoline (2-oxo-4-hydroxy-4-carboxy-5-) decarboxylase FUNCTION: Catalyzes the stereoselective decarboxylation of 2-oxo- 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin. {ECO:0000305}.; . TISSUE SPECIFICITY: Apparently not expressed.; . . 0.18316 0.09780 . . 3860.01321 12.23882 URAHP . . . urate (hydroxyiso-) hydrolase, pseudogene . . . . . . . . . . . URB1 . . . URB1 ribosome biogenesis 1 homolog (S. cerevisiae) . . . . . 0.19883 0.09434 2.699225953 98.89124794 843.19169 5.68362 URB1-AS1 . . . URB1 antisense RNA 1 (head to head) . . . . . . . . . . . URB2 3.33649047524477e-11 0.900592616784806 0.0994073831818292 URB2 ribosome biogenesis 2 homolog (S. cerevisiae) . . . fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;lens;skeletal muscle;pancreas;lung;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; superior cervical ganglion;testis;ciliary ganglion;pons;trigeminal ganglion;parietal lobe;cingulate cortex; 0.11639 0.08877 -1.313764723 4.824251003 996.26691 6.08368 URGCP 0.207220454111315 0.792384019955489 0.000395525933196438 upregulator of cell proliferation FUNCTION: May be involved in cell cycle progression through the regulation of cyclin D1 expression. May participate in the development of hepatocellular carcinoma (HCC) by promoting hepatocellular growth and survival. May play an important role in development of gastric cancer. {ECO:0000269|PubMed:12082552, ECO:0000269|PubMed:17217616}.; . TISSUE SPECIFICITY: Strongly expressed in hepatitis B virus- infected liver and in HCC cells. Also highly expressed in well- differentiated gastric cancer tissues and various gastric cancer cell lines. {ECO:0000269|PubMed:12082552, ECO:0000269|PubMed:17217616}.; myocardium;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;iris;pituitary gland;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; superior cervical ganglion;prefrontal cortex;appendix;atrioventricular node;trigeminal ganglion;cingulate cortex; . . -0.505170032 21.79759377 79.45664 1.88376 URGCP-MRPS24 0.0115516877111986 0.844386249329739 0.144062062959062 URGCP-MRPS24 readthrough . . . . . . . . . 231.00434 3.28624 URI1 0.211667123362299 0.788256228497764 7.66481399369579e-05 URI1 prefoldin-like chaperone FUNCTION: Involved in gene transcription regulation. Acts as a transcriptional repressor in concert with the corepressor UXT to regulate androgen receptor (AR) transcription. May act as a tumor suppressor to repress AR-mediated gene transcription and to inhibit anchorage-independent growth in prostate cancer cells. Required for cell survival in ovarian cancer cells. Together with UXT, associates with chromatin to the NKX3-1 promoter region. Antagonizes transcriptional modulation via hepatitis B virus X protein.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in ovarian cancers (at protein level). Expressed strongly in skeletal muscle. Expressed weakly in brain, heart, pancreas and in prostate epithelial cells. {ECO:0000269|PubMed:21397856, ECO:0000269|PubMed:21730289, ECO:0000269|PubMed:9819440, ECO:0000269|PubMed:9878255}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;gum;bone;thyroid;testis;germinal center;artery;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;cerebellum;thymus; thalamus;subthalamic nucleus;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;trigeminal ganglion;skeletal muscle; 0.46102 0.12594 -0.514264485 21.41424864 180.38212 2.91846 URM1 0.498052547084336 0.481990414337659 0.0199570385780043 ubiquitin related modifier 1 FUNCTION: Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2- thiolation reaction by being thiocarboxylated (-COSH) at its C- terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as MOCS3, ATPBD3, CTU2, USP15 and CAS. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. {ECO:0000255|HAMAP- Rule:MF_03048, ECO:0000269|PubMed:19017811, ECO:0000269|PubMed:21209336}.; . . . . 0.29590 0.10757 -0.117432389 44.89266336 3.62561 0.13303 UROC1 3.35644591456772e-10 0.734541324423578 0.265458675240777 urocanate hydratase 1 . DISEASE: Urocanase deficiency (UROCD) [MIM:276880]: An inborn error of histidine metabolism resulting in urocanic aciduria and neurological manifestations including mental retardation, ataxia, episodic aggressive behavior or exaggerated affection-seeking. {ECO:0000269|PubMed:19304569}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . liver;spleen; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;liver;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.10659 0.13811 0.319642692 72.82967681 647.41865 5.10863 UROD 0.000142209588904372 0.962723259230352 0.0371345311807441 uroporphyrinogen decarboxylase FUNCTION: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.; DISEASE: Familial porphyria cutanea tarda (FPCT) [MIM:176100]: A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. Familial porphyria cutanea tarda is an autosomal dominant disorder characterized by light-sensitive dermatitis, with onset in later life. It is associated with the excretion of large amounts of uroporphyrin in the urine. Iron overload is often present in association with varying degrees of liver damage. {ECO:0000269|PubMed:10338097, ECO:0000269|PubMed:10477430, ECO:0000269|PubMed:11069625, ECO:0000269|PubMed:11295834, ECO:0000269|PubMed:11719352, ECO:0000269|PubMed:2243121, ECO:0000269|PubMed:2920211, ECO:0000269|PubMed:7706766, ECO:0000269|PubMed:8896428, ECO:0000269|PubMed:9792863}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Hepatoerythropoietic porphyria (HEP) [MIM:176100]: A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. HEP is a cutaneous porphyria that presents in infancy. It is characterized biochemically by excessive excretion of acetate-substituted porphyrins and accumulation of protoporphyrin in erythrocytes. Uroporphyrinogen decarboxylase levels are very low in erythrocytes and cultured skin fibroblasts. {ECO:0000269|PubMed:12071824, ECO:0000269|PubMed:15491440, ECO:0000269|PubMed:1634232, ECO:0000269|PubMed:17240319, ECO:0000269|PubMed:1905636, ECO:0000269|PubMed:21668429, ECO:0000269|PubMed:3775362, ECO:0000269|PubMed:8176248, ECO:0000269|PubMed:8644733, ECO:0000269|PubMed:8896428}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;iris;pituitary gland;testis;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; superior cervical ganglion;subthalamic nucleus;fetal liver;adrenal gland;ciliary ganglion;trigeminal ganglion;bone marrow; 0.55901 0.22868 0.106667882 61.73036093 64.67369 1.65063 UROS 0.0122749509635658 0.951947542148369 0.035777506888065 uroporphyrinogen III synthase FUNCTION: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of porphyrins. Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell such as methionine synthesis (vitamin B12) or oxygen transport (heme).; DISEASE: Note=Severe congenital erythropoietic porphyria is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non- immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11112350}.; . . 0.10332 0.10246 -0.095386216 46.48502005 88.74997 2.02055 USB1 0.12277471565959 0.852732538547433 0.0244927457929771 U6 snRNA biogenesis 1 FUNCTION: Phosphodiesterase responsible for the U6 snRNA 3' end processing. Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate. {ECO:0000255|HAMAP- Rule:MF_03040, ECO:0000269|PubMed:22899009, ECO:0000269|PubMed:23190533}.; DISEASE: Poikiloderma with neutropenia (PN) [MIM:604173]: A genodermatosis characterized by poikiloderma, pachyonychia and chronic neutropenia. The disorder starts as a papular erythematous rash on the limbs during the first year of life. It gradually spreads centripetally and, as the papular rash resolves, hypo- and hyperpigmentation result, with development of telangiectasias. Another skin manifestation is pachyonychia, but alopecia and leukoplakia are distinctively absent. Patients have recurrent pneumonias that usually result in reactive airway disease and/or chronic cough. One of the most important extracutaneous symptoms is an increased susceptibility to infections, mainly affecting the respiratory system, primarily due to a chronic neutropenia and to neutrophil functional defects. Bone marrow abnormalities account for neutropenia and may evolve into myelodysplasia associated with the risk of leukemic transformation. Poikiloderma with neutropenia shows phenotypic overlap with Rothmund-Thomson syndrome. {ECO:0000269|PubMed:20004881, ECO:0000269|PubMed:20503306}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.09430 0.09754 0.194852702 67.03231894 389.9305 4.15800 USE1 0.0148417064935115 0.957527789204975 0.0276305043015132 unconventional SNARE in the ER 1 FUNCTION: SNARE that may be involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER. {ECO:0000269|PubMed:15272311}.; . . unclassifiable (Anatomical System);heart;urinary;colon;choroid;skin;uterus;prostate;lung;liver;spleen;cervix;germinal center;kidney;brain;bladder; whole brain;liver;cingulate cortex; 0.13584 0.11318 -0.273576253 33.97027601 88.00091 2.00643 USF1 0.381283031966058 0.618271948318652 0.000445019715290311 upstream transcription factor 1 FUNCTION: Transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.; DISEASE: Hyperlipidemia combined 1 (HYPLIP1) [MIM:602491]: A disorder characterized by a variable pattern of elevated levels of serum total cholesterol, triglycerides or both. It is observed in a percentage of individuals with premature coronary heart disease. {ECO:0000269|PubMed:14991056}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . . . 0.29838 0.63658 -0.405853867 26.23260203 7.16676 0.26955 USF1P1 . . . upstream transcription factor 1 pseudogene 1 . . . . . . . . . . . USF2 0.992520444067371 0.00747812040427192 1.43552835724765e-06 upstream transcription factor 2, c-fos interacting FUNCTION: Transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.; . TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;salivary gland;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;oesophagus;larynx;bone;iris;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;muscle;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;stomach; amygdala;whole brain;thalamus;heart;cerebellum peduncles;spinal cord;caudate nucleus;skeletal muscle;subthalamic nucleus;thyroid;prefrontal cortex;ciliary ganglion;cingulate cortex; 0.26523 0.33317 . . 1586.84065 7.37078 USF3 . . . upstream transcription factor family member 3 . . . . . 0.42318 . -0.711157248 14.50224109 . . USH1C 2.72435840434222e-12 0.964484478056037 0.0355155219412384 USH1 protein network component harmonin FUNCTION: Required for normal development and maintenance of cochlear hair cell bundles. Anchoring/scaffolding protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal hearing (By similarity). {ECO:0000250}.; DISEASE: Usher syndrome 1C (USH1C) [MIM:276904]: USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa with sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). USH1 is characterized by profound congenital sensorineural deafness, absent vestibular function and prepubertal onset of progressive retinitis pigmentosa leading to blindness. {ECO:0000269|PubMed:10973247}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal recessive, 18A (DFNB18A) [MIM:602092]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:12107438}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in small intestine, colon, kidney, eye and weakly in pancreas. Expressed also in vestibule of the inner ear. {ECO:0000269|PubMed:12588794}.; unclassifiable (Anatomical System);uterus;pancreas;hippocampus;testis;colon;cervix;kidney;brain;skeletal muscle;gall bladder;stomach; dorsal root ganglion;superior cervical ganglion;spinal cord;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07835 0.16900 -0.40608828 25.86694975 3991.78955 12.49143 USH1E . . . Usher syndrome 1E (autosomal recessive, severe) . . . . . . . . . . . USH1G 0.00108621943329599 0.830235502770171 0.168678277796533 USH1 protein network component sans FUNCTION: Required for normal development and maintenance of cochlear hair cell bundles. Anchoring/scaffolding protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal hearing. {ECO:0000269|PubMed:21709241}.; DISEASE: Note=The first cases with non-syndromic sensorineural hearing loss based on mutations in USH1G. The hearing loss has an onset during early childhood, is progressive, and has a downsloping audiogram configuration. Ophthalmic and vestibular abnormalities are absent. {ECO:0000269|PubMed:25255398}.; TISSUE SPECIFICITY: Expressed in vestibule of the inner ear, eye and small intestine. {ECO:0000269|PubMed:12588794}.; prostate; superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.16368 . 0.731244617 86.21137061 478.33491 4.51658 USH1H . . . Usher syndrome 1H (autosomal recessive) . . . . . . . . . . . USH1K . . . Usher syndrome 1K (autosomal recessive) . . . . . . . . . . . USH2A 3.68100336207458e-43 0.999989235571568 1.07644284322941e-05 Usher syndrome 2A (autosomal recessive, mild) FUNCTION: Involved in hearing and vision.; DISEASE: Usher syndrome 2A (USH2A) [MIM:276901]: USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa with sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). USH2 is characterized by congenital mild hearing impairment with normal vestibular responses. {ECO:0000269|PubMed:10729113, ECO:0000269|PubMed:10738000, ECO:0000269|PubMed:10909849, ECO:0000269|PubMed:11311042, ECO:0000269|PubMed:12112664, ECO:0000269|PubMed:12525556, ECO:0000269|PubMed:14970843, ECO:0000269|PubMed:15015129, ECO:0000269|PubMed:15025721, ECO:0000269|PubMed:15241801, ECO:0000269|PubMed:15325563, ECO:0000269|PubMed:17085681, ECO:0000269|PubMed:17405132, ECO:0000269|PubMed:18273898, ECO:0000269|PubMed:18452394, ECO:0000269|PubMed:19683999, ECO:0000269|PubMed:19737284, ECO:0000269|PubMed:20309401, ECO:0000269|PubMed:20440071, ECO:0000269|PubMed:20507924, ECO:0000269|PubMed:21593743, ECO:0000269|PubMed:21686329, ECO:0000269|PubMed:22004887, ECO:0000269|PubMed:23737954, ECO:0000269|PubMed:9624053}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa 39 (RP39) [MIM:613809]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:10775529, ECO:0000269|PubMed:12112664, ECO:0000269|PubMed:12427073, ECO:0000269|PubMed:15325563, ECO:0000269|PubMed:16098008, ECO:0000269|PubMed:17296898, ECO:0000269|PubMed:20507924, ECO:0000269|PubMed:21686329, ECO:0000269|PubMed:22334370, ECO:0000269|PubMed:24227914}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Present in the basement membrane of many, but not all tissues. Expressed in retina, cochlea, small and large intestine, pancreas, bladder, prostate, esophagus, trachea, thymus, salivary glands, placenta, ovary, fallopian tube, uterus and testis. Absent in many other tissues such as heart, lung, liver, kidney and brain. In the retina, it is present in the basement membranes in the Bruch's layer choroid capillary basement membranes, where it localizes just beneath the retinal pigment epithelial cells (at protein level). Weakly expressed. Isoform 2 is expressed in fetal eye, cochlea and heart, and at very low level in brain, CNS, intestine, skeleton, tongue, kidney and lung. Isoform 2 is not expressed in stomach and liver. In adult tissues, isoform 2 is expressed in neural retina and testis, and at low level in brain, heart, kidney and liver. Isoform 1 displays a similar pattern of expression but is expressed at very low level in fetal cochlea. {ECO:0000269|PubMed:11788194, ECO:0000269|PubMed:12433396, ECO:0000269|PubMed:15015129, ECO:0000269|PubMed:9624053}.; unclassifiable (Anatomical System);liver;testis;retina; dorsal root ganglion;superior cervical ganglion;adrenal gland;temporal lobe;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;cerebellum; 0.15836 . 4.179636958 99.70511913 6401.91635 16.71188 USH3B . . . Usher syndrome 3B . . . . . . . . . . . USHBP1 3.2784377499068e-13 0.259438277870444 0.740561722129228 USH1 protein network component harmonin binding protein 1 . . TISSUE SPECIFICITY: Highest level of expression in heart, and moderate to low expression in skeletal muscle, kidney, liver, small intestine, placenta and lung. {ECO:0000269|PubMed:11311560}.; unclassifiable (Anatomical System);myocardium;pancreas;lung;placenta;colon;kidney;spinal ganglion;brain;retina; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skin; 0.05039 0.10302 -0.391302095 27.06416608 2829.1436 10.03299 USMG5 0.243352200194902 0.64372398354637 0.112923816258728 up-regulated during skeletal muscle growth 5 homolog (mouse) FUNCTION: Plays a critical role in maintaining the ATP synthase population in mitochondria. {ECO:0000269|PubMed:21345788}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;gum;bone;thyroid;pituitary gland;testis;dura mater;germinal center;brain;pineal gland;artery;bladder;unclassifiable (Anatomical System);meninges;trophoblast;lymph node;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;pia mater;lung;cornea;adrenal gland;placenta;visual apparatus;alveolus;hypopharynx;liver;head and neck;kidney;mammary gland;aorta;stomach; amygdala;whole brain;thalamus;occipital lobe;medulla oblongata;hypothalamus;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;globus pallidus;parietal lobe;cingulate cortex; . 0.11141 0.079165051 59.43029016 181.76512 2.92891 USMG5P1 . . . USMG5 pseudogene 1 . . . . . . . . . . . USO1 0.918011905997378 0.081987908098776 1.85903845901478e-07 USO1 vesicle transport factor FUNCTION: General vesicular transport factor required for intercisternal transport in the Golgi stack; it is required for transcytotic fusion and/or subsequent binding of the vesicles to the target membrane. May well act as a vesicular anchor by interacting with the target membrane and holding the vesicular and target membranes in proximity. {ECO:0000250|UniProtKB:P41542}.; . . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;pancreas;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;thymus; superior cervical ganglion;smooth muscle;white blood cells;trigeminal ganglion;skeletal muscle; 0.89736 0.10697 . . 82.58244 1.92923 USP1 0.993180568281562 0.00681919991944497 2.31798993190893e-07 ubiquitin specific peptidase 1 FUNCTION: Negative regulator of DNA damage repair which specifically deubiquitinates monoubiquitinated FANCD2. Also involved in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. {ECO:0000269|PubMed:15694335, ECO:0000269|PubMed:16531995, ECO:0000269|PubMed:18082604}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;bone;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;bile duct;pancreas;lung;pia mater;nasopharynx;placenta;kidney;stomach;aorta; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;tumor;testis;white blood cells; 0.30167 0.13757 -0.642904474 16.62538335 76.97787 1.84216 USP2 0.185180861868735 0.814798768287353 2.03698439120633e-05 ubiquitin specific peptidase 2 FUNCTION: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1. Isoform 1 and isoform 4 possess both ubiquitin-specific peptidase and isopeptidase activities. Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity. Has no deubiquitinase activity against p53/TP53. Prevents MDM2-mediated degradation of MDM4. Plays a role in the G1/S cell-cycle progression in normal and cancer cells. Plays a role in the regulation of myogenic differentiation of embryonic muscle cells. Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues. Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability. Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and ARNTL/BMAL1 (By similarity). {ECO:0000250|UniProtKB:O88623, ECO:0000269|PubMed:17290220, ECO:0000269|PubMed:19838211, ECO:0000269|PubMed:19917254}.; . TISSUE SPECIFICITY: Expressed in mesangial cells of the kidney and in different types of glomerulonephritides (at protein level). {ECO:0000269|PubMed:20403044}.; unclassifiable (Anatomical System);medulla oblongata;lymph node;ovary;islets of Langerhans;muscle;fovea centralis;choroid;lens;retina;optic nerve;lung;frontal lobe;thyroid;macula lutea;visual apparatus;iris;testis;kidney;brain; testis - interstitial;testis - seminiferous tubule;testis; 0.47152 0.14748 0.068033485 59.0351498 299.61505 3.69066 USP2-AS1 . . . USP2 antisense RNA 1 (head to head) . . . . . . . . . . . USP3 0.984379976108001 0.0156196662066592 3.57685339684645e-07 ubiquitin specific peptidase 3 FUNCTION: Hydrolase that deubiquitinates monoubiquitinated target proteins such as histone H2A and H2B. Required for proper progression through S phase and subsequent mitotic entry. May regulate the DNA damage response (DDR) checkpoint through deubiquitination of H2A at DNA damage sites. Associates with the chromatin. {ECO:0000269|PubMed:17980597}.; . TISSUE SPECIFICITY: Expressed in all tissues examined, with strongest expression in pancreas.; umbilical cord;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;white blood cells;atrioventricular node;whole blood;cerebellum; 0.24666 0.11127 -0.426079032 25.36565228 225.98751 3.24807 USP3-AS1 . . . USP3 antisense RNA 1 . . . . . . . . . . . USP4 6.20193619608728e-07 0.99971913881771 0.000280240988670332 ubiquitin specific peptidase 4 (proto-oncogene) FUNCTION: Hydrolase that deubiquitinates target proteins such as the receptor ADORA2A, PDPK1 and TRIM21. Deubiquitination of ADORA2A increases the amount of functional receptor at the cell surface. May regulate mRNA splicing through deubiquitination of the U4 spliceosomal protein PRPF3. This may prevent its recognition by the U5 component PRPF8 thereby destabilizing interactions within the U4/U6.U5 snRNP. May also play a role in the regulation of quality control in the ER. {ECO:0000269|PubMed:16316627, ECO:0000269|PubMed:16339847, ECO:0000269|PubMed:16472766, ECO:0000269|PubMed:20595234, ECO:0000269|PubMed:7784062}.; . TISSUE SPECIFICITY: Overexpressed in small cell tumors and adenocarcinomas of the lung compared to wild-type lung (at protein level). Expressed in the hippocampal neurons. {ECO:0000269|PubMed:16339847, ECO:0000269|PubMed:7784062}.; myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;lens;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16724 0.11581 -0.815648973 12.01344657 178.38163 2.90370 USP5 0.996309624736257 0.00369037483531445 4.28428824778871e-10 ubiquitin specific peptidase 5 (isopeptidase T) FUNCTION: Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys- 63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition. {ECO:0000269|PubMed:19098288}.; . . lymphoreticular;ovary;salivary gland;sympathetic chain;colon;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;muscle;blood;lens;skeletal muscle;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;tongue;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;parietal lobe; 0.69044 0.12787 -1.684662147 2.630337344 55.70803 1.49937 USP6 1.76208067122363e-18 0.973334186068363 0.0266658139316373 ubiquitin specific peptidase 6 FUNCTION: Deubiquitinase with an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety. Catalyzes its own deubiquitination. In vitro, isoform 2, but not isoform 3, shows deubiquitinating activity. Promotes plasma membrane localization of ARF6 and selectively regulates ARF6- dependent endocytic protein trafficking. Is able to initiate tumorigenesis by inducing the production of matrix metalloproteinases following NF-kappa-B activation. {ECO:0000269|PubMed:15509780, ECO:0000269|PubMed:16127172, ECO:0000269|PubMed:20418905}.; DISEASE: Note=A chromosomal aberration involving USP6 is a common genetic feature of aneurysmal bone cyst, a benign osseous neoplasm. Translocation t(16;17)(q22;p13) with CDH11. The translocation generates a fusion gene in which the strong CDH11 promoter is fused to the entire USP6 coding sequence, resulting in USP6 transcriptional up-regulation (PubMed:15026324). {ECO:0000269|PubMed:15026324}.; TISSUE SPECIFICITY: Testis specific. Expressed in various cancer cell lines. {ECO:0000269|PubMed:12604796, ECO:0000269|PubMed:1565468}.; myocardium;ovary;salivary gland;sympathetic chain;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;atrium;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;head and neck;mammary gland;stomach; amygdala;testis - interstitial;subthalamic nucleus;fetal brain;testis - seminiferous tubule;prefrontal cortex;testis;atrioventricular node;parietal lobe; 0.04825 . 0.418773167 76.96390658 5889.81568 15.90621 USP6NL 0.102392914785226 0.897546720213145 6.03650016295383e-05 USP6 N-terminal like FUNCTION: Acts as a GTPase-activating protein for RAB5A and RAB43. Involved in receptor trafficking. In complex with EPS8 inhibits internalization of EGFR. Involved in retrograde transport from the endocytic pathway to the Golgi apparatus. Involved in the transport of Shiga toxin from early and recycling endosomes to the trans-Golgi network. Required for structural integrity of the Golgi complex. {ECO:0000269|PubMed:11099046, ECO:0000269|PubMed:17562788, ECO:0000269|PubMed:17684057}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8700515}.; vein;skin;retina;uterus;whole body;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cerebellum cortex;islets of Langerhans;lens;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach; testis;atrioventricular node; 0.25394 0.15158 -0.753139731 13.67067705 107.31968 2.24700 USP7 0.999999998411863 1.58813705867088e-09 1.60091437202861e-23 ubiquitin specific peptidase 7 (herpes virus-associated) FUNCTION: Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX (PubMed:11923872, PubMed:15053880, PubMed:16964248, PubMed:18716620, PubMed:25283148). Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation. Deubiquitinates p53/TP53, preventing degradation of p53/TP53, and enhances p53/TP53-dependent transcription regulation, cell growth repression and apoptosis (PubMed:25283148). Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6. Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection. Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1 (PubMed:21745816). Exhibits a preference towards 'Lys-48'-linked ubiquitin chains. Increases regulatory T-cells (Treg) suppressive capacity by deubiquitinating and stabilizing the transcription factor FOXP3 which is crucial for Treg cell function (PubMed:23973222). {ECO:0000269|PubMed:11923872, ECO:0000269|PubMed:14506283, ECO:0000269|PubMed:15053880, ECO:0000269|PubMed:16160161, ECO:0000269|PubMed:16964248, ECO:0000269|PubMed:18590780, ECO:0000269|PubMed:18716620, ECO:0000269|PubMed:20153724, ECO:0000269|PubMed:21745816, ECO:0000269|PubMed:22411829, ECO:0000269|PubMed:22466611, ECO:0000269|PubMed:22466612, ECO:0000269|PubMed:22689415, ECO:0000269|PubMed:23973222, ECO:0000269|PubMed:25283148}.; . TISSUE SPECIFICITY: Widely expressed. Overexpressed in prostate cancer. {ECO:0000269|PubMed:18716620}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;oesophagus;endometrium;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; amygdala;testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;testis;pons; 0.40925 0.22612 -1.331850187 4.665015334 19.2272 0.66248 USP8 0.999982628555187 1.73714447902788e-05 2.23180538837433e-14 ubiquitin specific peptidase 8 FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. {ECO:0000269|PubMed:16520378, ECO:0000269|PubMed:17711858, ECO:0000269|PubMed:18329369, ECO:0000269|PubMed:9628861}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;cerebral cortex;endometrium;larynx;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;stomach; testis - interstitial; 0.21578 0.12146 0.402364592 76.45081387 805.90942 5.59333 USP8P1 . . . ubiquitin specific peptidase 8 pseudogene 1 . . . . . . . . . . . USP9X 0.999999999976444 2.35556072461794e-11 2.77746340489818e-27 ubiquitin specific peptidase 9, X-linked FUNCTION: Deubiquitinase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. May therefore play an important role regulatory role at the level of protein turnover by preventing degradation of proteins through the removal of conjugated ubiquitin. Essential component of TGF-beta/BMP signaling cascade. Regulates chromosome alignment and segregation in mitosis by regulating the localization of BIRC5/survivin to mitotic centromeres. Specifically hydrolyzes both 'Lys-29'- and 'Lys-33'-linked polyubiquitins chains. Specifically deubiquitinates monoubiquitinated SMAD4, opposing the activity of E3 ubiquitin-protein ligase TRIM33. Involved in axonal growth and neuronal cell migration. {ECO:0000269|PubMed:16322459, ECO:0000269|PubMed:18254724, ECO:0000269|PubMed:19135894, ECO:0000269|PubMed:24607389}.; . TISSUE SPECIFICITY: Widely expressed in embryonic and adult tissues.; ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);trophoblast;cartilage;heart;tongue;islets of Langerhans;hypothalamus;oral cavity;muscle;urinary;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;medulla oblongata;superior cervical ganglion;testis - interstitial;occipital lobe;subthalamic nucleus;testis - seminiferous tubule;placenta;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.58131 0.10304 -1.618506764 2.925218212 35.92323 1.07855 USP9Y 0.140701437950318 0.855194700379278 0.00410386167040401 ubiquitin specific peptidase 9, Y-linked FUNCTION: May function as a ubiquitin-protein or polyubiquitin hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. May therefore play an important role regulatory role at the level of protein turnover by preventing degradation of proteins through the removal of conjugated ubiquitin. Essential component of TGF-beta/BMP signaling cascade. Deubiquitinates monoubiquitinated SMAD4, opposing the activity of E3 ubiquitin-protein ligase TRIM33. Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF- beta/BMP signaling cascade. Deubiqitination of SMAD4 by USP9X re- empowers its competence to mediate TGF-beta signaling (By similarity). {ECO:0000250}.; DISEASE: Spermatogenic failure Y-linked 2 (SPGFY2) [MIM:415000]: A disorder resulting in the absence (azoospermia) or reduction (oligozoospermia) of sperm in the semen, leading to male infertility. {ECO:0000269|PubMed:10581029}. Note=The disease may be caused by mutations affecting the gene represented in this entry. The role of USP9Y in spermatogenesis failure is uncertain (PubMed:19246359). A 4-bp deletion in a splice-donor site, causing exon skipping and protein truncation has been observed in non- obstructive azoospermia (PubMed:10581029). However, complete USP9Y deletion has been detected in individuals with no spermatogenic defects (PubMed:19246359). {ECO:0000269|PubMed:10581029, ECO:0000269|PubMed:19246359}.; TISSUE SPECIFICITY: Widely expressed in embryonic and adult tissues.; unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;vein;skeletal muscle;retina;prostate;atrium;lung;bone;liver;testis;head and neck;brain;stomach; . 0.33000 . . . 658.55668 5.14623 USP9YP1 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 1 . . . . . . . . . . . USP9YP2 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 2 . . . . . . . . . . . USP9YP3 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 3 . . . . . . . . . . . USP9YP4 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 4 . . . . . . . . . . . USP9YP5 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 5 . . . . . . . . . . . USP9YP6 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 6 . . . . . . . . . . . USP9YP7 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 7 . . . . . . . . . . . USP9YP8 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 8 . . . . . . . . . . . USP9YP9 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 9 . . . . . . . . . . . USP9YP10 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 10 . . . . . . . . . . . USP9YP11 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 11 . . . . . . . . . . . USP9YP12 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 12 . . . . . . . . . . . USP9YP13 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 13 . . . . . . . . . . . USP9YP14 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 14 . . . . . . . . . . . USP9YP15 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 15 . . . . . . . . . . . USP9YP16 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 16 . . . . . . . . . . . USP9YP17 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 17 . . . . . . . . . . . USP9YP18 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 18 . . . . . . . . . . . USP9YP19 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 19 . . . . . . . . . . . USP9YP20 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 20 . . . . . . . . . . . USP9YP21 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 21 . . . . . . . . . . . USP9YP22 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 22 . . . . . . . . . . . USP9YP23 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 23 . . . . . . . . . . . USP9YP24 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 24 . . . . . . . . . . . USP9YP25 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 25 . . . . . . . . . . . USP9YP26 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 26 . . . . . . . . . . . USP9YP27 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 27 . . . . . . . . . . . USP9YP28 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 28 . . . . . . . . . . . USP9YP29 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 29 . . . . . . . . . . . USP9YP30 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 30 . . . . . . . . . . . USP9YP31 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 31 . . . . . . . . . . . USP9YP32 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 32 . . . . . . . . . . . USP9YP33 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 33 . . . . . . . . . . . USP9YP34 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 34 . . . . . . . . . . . USP9YP35 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 35 . . . . . . . . . . . USP9YP36 . . . ubiquitin specific peptidase 9, Y-linked pseudogene 36 . . . . . . . . . . . USP10 0.98885345266455 0.0111465157245619 3.16108878514456e-08 ubiquitin specific peptidase 10 FUNCTION: Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, BECN1, SNX3 and CFTR. Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53. Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response. Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34- containing complexes. In turn, PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Does not deubiquitinate MDM2. Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling. {ECO:0000269|PubMed:11439350, ECO:0000269|PubMed:18632802, ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:20096447, ECO:0000269|PubMed:21962518}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11439350}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;placenta;white blood cells;whole blood;cingulate cortex; 0.69696 0.10507 -0.238793231 36.3116301 1997.51994 8.23420 USP10P1 . . . ubiquitin specific peptidase 10 pseudogene 1 . . . . . . . . . . . USP10P2 . . . ubiquitin specific peptidase10 pseudogene 2 . . . . . . . . . . . USP11 0.998323456750043 0.00167654172314595 1.52681089618869e-09 ubiquitin specific peptidase 11 FUNCTION: Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Inhibits the degradation of target proteins by the proteasome. Plays a role in the regulation of pathways leading to NF-kappa-B activation. Plays a role in the regulation of DNA repair after double-stranded DNA breaks. {ECO:0000269|PubMed:15314155, ECO:0000269|PubMed:17897950, ECO:0000269|PubMed:18408009, ECO:0000269|PubMed:19874889, ECO:0000269|PubMed:20233726}.; . . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;larynx;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;pineal gland;tonsil;gall bladder;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;lens;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; amygdala;whole brain;occipital lobe;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.23122 0.11756 -1.043396569 7.71408351 26.86765 0.86797 USP12 0.79499196891634 0.204751629708902 0.000256401374758117 ubiquitin specific peptidase 12 FUNCTION: Deubiquitinating enzyme. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2. {ECO:0000269|PubMed:19075014}.; . . lung;cerebral cortex;endometrium;liver;duodenum;germinal center;skeletal muscle; fetal liver;superior cervical ganglion;subthalamic nucleus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.40331 . -0.095386216 46.48502005 31.82098 1.00153 USP12-AS1 . . . USP12 antisense RNA 1 . . . . . . . . . . . USP12-AS2 . . . USP12 antisense RNA 2 (head to head) . . . . . . . . . . . USP12P1 . . . ubiquitin specific peptidase 12 pseudogene 1 FUNCTION: Deubiquitinating enzyme. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2. {ECO:0000269|PubMed:19075014}.; . . . . 0.40331 . -0.095386216 46.48502005 . . USP12PX . . . ubiquitin specific peptidase 12 pseudogene, X-linked . . . . . . . . . . . USP12PY . . . ubiquitin specific peptidase 12 pseudogene, Y-linked . . . . . . . . . . . USP13 2.17337060975034e-08 0.998593224043967 0.00140675422232681 ubiquitin specific peptidase 13 (isopeptidase T-3) FUNCTION: Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum- associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34- containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data. {ECO:0000269|PubMed:17653289, ECO:0000269|PubMed:21571647, ECO:0000269|PubMed:21659512, ECO:0000269|PubMed:21811243, ECO:0000269|PubMed:21962518, ECO:0000269|PubMed:22216260}.; . TISSUE SPECIFICITY: Highly expressed in ovary and testes.; unclassifiable (Anatomical System);myocardium;lymph node;heart;ovary;islets of Langerhans;skin;breast;pancreas;prostate;lung;thyroid;liver;testis;cervix;head and neck;spleen;kidney;brain; superior cervical ganglion;testis;trigeminal ganglion;skeletal muscle; 0.23281 0.13231 -1.019530098 8.038452465 249.83591 3.40473 USP14 0.927536807900908 0.0724625220425103 6.70056581478713e-07 ubiquitin specific peptidase 14 FUNCTION: Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Indispensable for synaptic development and function at neuromuscular junctions (NMJs). {ECO:0000269|PubMed:18162577, ECO:0000269|PubMed:19106094, ECO:0000269|PubMed:19135427}.; . . lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;stomach; amygdala;superior cervical ganglion;prefrontal cortex;parietal lobe; 0.66781 0.16083 -0.271755481 34.31823543 586.30593 4.91157 USP15 0.990365016125739 0.00963498369102993 1.83231046772474e-10 ubiquitin specific peptidase 15 FUNCTION: Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. May also regulate gene expression and/or DNA repair through the deubiquitination of histone H2B (PubMed:24526689). Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway. {ECO:0000269|PubMed:16005295, ECO:0000269|PubMed:17318178, ECO:0000269|PubMed:19553310, ECO:0000269|PubMed:19576224, ECO:0000269|PubMed:19826004, ECO:0000269|PubMed:21947082, ECO:0000269|PubMed:22344298, ECO:0000269|PubMed:24526689}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, kidney, heart, placenta, liver, thymus, lung, and ovary, with little or no expression in other tissues.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; fetal liver;superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.80464 0.14896 -0.979072682 8.752064166 37.09012 1.10797 USP16 0.00586486313268796 0.993942738108204 0.00019239875910845 ubiquitin specific peptidase 16 FUNCTION: Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. In resting B- and T- lymphocytes, phosphorylation by AURKB leads to enhance its activity, thereby maintaining transcription in resting lymphocytes. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B. {ECO:0000255|HAMAP-Rule:MF_03062, ECO:0000269|PubMed:10077596, ECO:0000269|PubMed:17914355}.; DISEASE: Note=A chromosomal aberration involving USP16 is a cause of Chronic myelomonocytic leukemia. Inversion inv(21) (q21;q22) with RUNX1/AML1.; TISSUE SPECIFICITY: Present in all the tissues examined including fetal brain, lung, liver, kidney, and adult heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:10077596}.; myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;testis;dura mater;germinal center;brain;pineal gland;unclassifiable (Anatomical System);meninges;cartilage;heart;hypothalamus;blood;lens;skeletal muscle;breast;pia mater;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;alveolus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.23545 0.10820 -0.088107893 47.06298655 1762.28662 7.75054 USP17L1 . . . ubiquitin specific peptidase 17-like family member 1 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000250}.; . . . . . . . . . . USP17L2 0.0138587263197935 0.867635244666215 0.118506029013991 ubiquitin specific peptidase 17-like family member 2 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. Regulates cell proliferation by deubiquitinating and inhibiting RCE1 thereby controlling the small GTPases NRAS and HRAS localization and activation. In parallel, mediates deubiquitination of CDC25A, preventing CDC25A degradation by the proteasome during the G1/S and G2/M phases promoting cell-cycle progression. Also regulates cell proliferation and apoptosis through deubiquitination of SUDS3 a regulator of histone deacetylation. Through activation of the Rho family GTPases RAC1A, CDC42 and RHOA, regulates cell migration. Through the cleavage of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains of the cytoplasmic innate immune receptors DDX58 and IFIH1 stimulates the cellular response to viral infection. {ECO:0000269|PubMed:14699124, ECO:0000269|PubMed:17109758, ECO:0000269|PubMed:19188362, ECO:0000269|PubMed:20147298, ECO:0000269|PubMed:20228808, ECO:0000269|PubMed:20368735, ECO:0000269|PubMed:20388806, ECO:0000269|PubMed:21239494, ECO:0000269|PubMed:21448158}.; . TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:14699124}.; . . . . 3.158837847 99.30408115 3306.09393 10.97365 USP17L3 . . . ubiquitin specific peptidase 17-like family member 3 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000250}.; . . . . . . . . . . USP17L4 . . . ubiquitin specific peptidase 17-like family member 4 . . . . . . . . . . . USP17L5 . . . ubiquitin specific peptidase 17-like family member 5 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000250}.; . . . . . . . . . . USP17L6P . . . ubiquitin specific peptidase 17-like family member 6, pseudogene FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, cell migration, and the cellular response to viral infection. Seems to be non-functional in the regulation of apoptosis. {ECO:0000269|PubMed:17109758}.; . . . . . . . . . . USP17L7 . . . ubiquitin specific peptidase 17-like family member 7 . . . . . . . . . . . USP17L8 . . . ubiquitin specific peptidase 17-like family member 8 . . . . . . . . . . . USP17L9P . . . ubiquitin specific peptidase 17-like family member 9, pseudogene FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000269|PubMed:10936051}.; . TISSUE SPECIFICITY: Expressed in heart, brain, liver and skeletal muscle. {ECO:0000269|PubMed:10936051}.; . . 0.03208 0.08097 . . . . USP17L10 . . . ubiquitin specific peptidase 17-like family member 10 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000250}.; . . . . . . . . 219.17205 3.20095 USP17L11 . . . ubiquitin specific peptidase 17-like family member 11 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000250}.; . . . . . . . . . . USP17L12 . . . ubiquitin specific peptidase 17-like family member 12 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000250}.; . . . . . . . . . . USP17L13 . . . ubiquitin specific peptidase 17-like family member 13 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000250}.; . . . . . . . . . . USP17L14P . . . ubiquitin specific peptidase 17-like family member 14, pseudogene . . . . . . . . . . . USP17L15 . . . ubiquitin specific peptidase 17-like family member 15 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000250}.; . . . . . . . . 14.57288 0.52551 USP17L16P . . . ubiquitin specific peptidase 17-like family member 16, pseudogene . . . . . . . . . . . USP17L17 . . . ubiquitin specific peptidase 17-like family member 17 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000250}.; . . . . . . . . . . USP17L18 . . . ubiquitin specific peptidase 17-like family member 18 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000250}.; . . . . . . . . 2.65072 0.09678 USP17L19 . . . ubiquitin specific peptidase 17-like family member 19 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000250}.; . . . . . . . . . . USP17L20 . . . ubiquitin specific peptidase 17-like family member 20 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000250}.; . . . . . . . . . . USP17L21 . . . ubiquitin specific peptidase 17-like family member 21 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000250}.; . . . . . . . . . . USP17L22 . . . ubiquitin specific peptidase 17-like family member 22 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000250}.; . . . . . . . . 26.88933 0.86933 USP17L23 . . . ubiquitin specific peptidase 17-like family member 23 . . . . . . . . . . . USP17L24 . . . ubiquitin specific peptidase 17-like family member 24 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000269|PubMed:10936051}.; . TISSUE SPECIFICITY: Expressed in heart, brain, liver and skeletal muscle. {ECO:0000269|PubMed:10936051}.; . . . . . . . . USP17L25 . . . ubiquitin specific peptidase 17-like family member 25 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000269|PubMed:10936051}.; . TISSUE SPECIFICITY: Expressed in heart, brain, liver and skeletal muscle. {ECO:0000269|PubMed:10936051}.; . . . . . . . . USP17L26 . . . ubiquitin specific peptidase 17-like family member 26 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000269|PubMed:10936051}.; . TISSUE SPECIFICITY: Expressed in heart, brain, liver and skeletal muscle. {ECO:0000269|PubMed:10936051}.; . . . . . . . . USP17L27 . . . ubiquitin specific peptidase 17-like family member 27 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000269|PubMed:10936051}.; . TISSUE SPECIFICITY: Expressed in heart, brain, liver and skeletal muscle. {ECO:0000269|PubMed:10936051}.; . . . . . . . . USP17L28 . . . ubiquitin specific peptidase 17-like family member 28 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000269|PubMed:10936051}.; . TISSUE SPECIFICITY: Expressed in heart, brain, liver and skeletal muscle. {ECO:0000269|PubMed:10936051}.; . . . . . . . . USP17L29 . . . ubiquitin specific peptidase 17-like family member 29 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000269|PubMed:10936051}.; . TISSUE SPECIFICITY: Expressed in heart, brain, liver and skeletal muscle. {ECO:0000269|PubMed:10936051}.; . . . . . . 39.92569 1.17468 USP17L30 . . . ubiquitin specific peptidase 17-like family member 30 FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000269|PubMed:10936051}.; . TISSUE SPECIFICITY: Expressed in heart, brain, liver and skeletal muscle. {ECO:0000269|PubMed:10936051}.; . . . . . . . . USP18 0.392598704975479 0.605397789302469 0.00200350572205161 ubiquitin specific peptidase 18 FUNCTION: Can efficiently cleave only ISG15 fusions including native ISG15 conjugates linked via isopeptide bonds. Necessary to maintain a critical cellular balance of ISG15-conjugated proteins in both healthy and stressed organisms.; . . unclassifiable (Anatomical System);medulla oblongata;cartilage;ovary;heart;islets of Langerhans;colon;parathyroid;skin;uterus;prostate;pancreas;whole body;lung;nasopharynx;bone;thyroid;placenta;hippocampus;liver;testis;head and neck;spleen;kidney;brain;mammary gland;aorta; . 0.06636 0.10790 0.260991686 70.25831564 65.41563 1.66527 USP19 0.999991981492882 8.01850711721762e-06 6.86958839790648e-16 ubiquitin specific peptidase 19 FUNCTION: Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin- dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic- reticulum-associated degradation (ERAD) substrates. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing their ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non- catalytic manner. Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. Exhibits a preference towards 'Lys-63'-linked Ubiquitin chains. {ECO:0000269|PubMed:19465887, ECO:0000269|PubMed:21849505, ECO:0000269|PubMed:22128162, ECO:0000269|PubMed:22689415}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;temporal lobe;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.17396 . -1.587406381 3.113941967 668.82834 5.17246 USP20 0.00188749026993717 0.998104308862935 8.20086712831582e-06 ubiquitin specific peptidase 20 FUNCTION: Deubiquitinating enzyme involved in beta-2 adrenergic receptor (ADRB2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:12056827, ECO:0000269|PubMed:12865408, ECO:0000269|PubMed:15776016, ECO:0000269|PubMed:19424180}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;kidney;stomach;peripheral nerve;cerebellum; subthalamic nucleus; 0.18431 0.13863 -0.367438677 28.29087049 306.86366 3.72822 USP21 0.0746516537664707 0.925344155665965 4.19056756463807e-06 ubiquitin specific peptidase 21 FUNCTION: Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation. Regulates gene expression via histone H2A deubiquitination (By similarity). Also capable of removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-1 conjugates (PubMed:10799498). Deubiquitinates BAZ2A/TIP5 leading to its stabilization (PubMed:26100909). {ECO:0000250|UniProtKB:Q9QZL6, ECO:0000269|PubMed:10799498, ECO:0000269|PubMed:26100909}.; . TISSUE SPECIFICITY: Highly expressed in heart, pancreas and skeletal muscle. Also expressed in brain, placenta, liver and kidney, and at very low level in lung. {ECO:0000269|PubMed:10799498}.; unclassifiable (Anatomical System);lymph node;ovary;heart;colon;parathyroid;blood;fovea centralis;skin;uterus;bile duct;prostate;pancreas;whole body;lung;frontal lobe;endometrium;bone;placenta;macula lutea;liver;testis;spleen;germinal center;brain;mammary gland;stomach; superior cervical ganglion;testis;skeletal muscle; 0.39040 0.11619 -0.290161348 33.33923095 291.82837 3.65497 USP22 0.98329279247161 0.0167067854744773 4.22053912465057e-07 ubiquitin specific peptidase 22 FUNCTION: Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation and cell cycle progression. {ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:18206973, ECO:0000269|PubMed:18469533}.; . TISSUE SPECIFICITY: Moderately expressed in various tissues including heart and skeletal muscle, and weakly expressed in lung and liver. {ECO:0000269|PubMed:16378762}.; myocardium;ovary;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;tongue;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;developmental;intestine;colon;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;testis;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; whole brain;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;heart;cerebellum peduncles;atrioventricular node;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.18273 0.10390 -0.383807564 27.41802312 18.11431 0.63232 USP24 0.999999998496473 1.50352687163463e-09 3.93715415812405e-29 ubiquitin specific peptidase 24 FUNCTION: Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Deubiquitinates DDB2, preventing its proteasomal degradation. {ECO:0000269|PubMed:23159851}.; . . colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;ciliary body;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;spinal cord;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.69518 0.13149 -2.157287126 1.444916254 488.07537 4.54747 USP24P1 . . . ubiquitin specific peptidase 24 pseudogene 1 . . . . . . . . . . . USP25 0.990130458125693 0.00986954186635002 7.95745302719302e-12 ubiquitin specific peptidase 25 FUNCTION: Deubiquitinating enzyme that hydrolyzes ubiquitin moieties conjugated to substrates and thus, functions to process newly synthesized Ubiquitin, to recycle ubiquitin molecules or to edit polyubiquitin chains and prevents proteasomal degradation of substrates. Hydrolyzes both 'Lys-48'- and 'Lys-63'-linked tetraubiquitin chains.; . TISSUE SPECIFICITY: Isoform USB25a is found in most adult and fetal tissues; expression is moderately high in testis, pancreas, kidney, skeletal muscle, liver, lung, placenta, brain, heart, but very low in peripheral blood, colon, small intestine, ovary, prostate, thymus and spleen. Isoform USB25b is found in all tissues except heart and skeletal muscle. Isoform USB25m is heart and skeletal muscle specific. {ECO:0000269|PubMed:10644437, ECO:0000269|PubMed:11597335}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;liver;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16560 0.10985 -0.905656269 10.12031139 259.94554 3.46398 USP26 0.0104943799173462 0.945441772871432 0.0440638472112217 ubiquitin specific peptidase 26 FUNCTION: Involved in the ubiquitin-dependent proteolytic pathway in conjunction with the 26S proteasome (By similarity). Deubiquitinates the androgen receptor and regulates the androgen receptor signaling pathway. {ECO:0000250, ECO:0000269|PubMed:20501646}.; . . . . 0.09113 0.07415 0.464864541 78.69190847 356.48151 3.99731 USP27X 0.592784999490721 0.367530728028038 0.0396842724812409 ubiquitin specific peptidase 27, X-linked . . . . . 0.44561 0.11023 . . 6.29769 0.23683 USP27X-AS1 . . . USP27X antisense RNA 1 (head to head) . . . . . . . . . . . USP28 0.031657505195455 0.96834246791256 2.68919847816125e-08 ubiquitin specific peptidase 28 FUNCTION: Deubiquitinase involved in DNA damage response checkpoint and MYC proto-oncogene stability. Involved in DNA damage induced apoptosis by specifically deubiquitinating proteins of the DNA damage pathway such as CLSPN. Also involved in G2 DNA damage checkpoint, by deubiquitinating CLSPN, and preventing its degradation by the anaphase promoting complex/cyclosome (APC/C). In contrast, it does not deubiquitinate PLK1. Specifically deubiquitinates MYC in the nucleoplasm, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm and counteracting ubiquitination of MYC by the SCF(FBW7) complex. In contrast, it does not interact with isoform 4 of FBXW7 (FBW7gamma) in the nucleolus, allowing MYC degradation and explaining the selective MYC degradation in the nucleolus. {ECO:0000269|PubMed:16901786, ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:17873522, ECO:0000269|PubMed:18662541}.; . . ovary;colon;parathyroid;skin;uterus;prostate;endometrium;gum;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;cervix;kidney;stomach;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.60849 0.11751 -0.791786324 12.59731069 79.98741 1.89131 USP29 9.28685713630925e-15 0.00135081447307032 0.998649185526921 ubiquitin specific peptidase 29 . . . lung;testis; dorsal root ganglion;testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.07617 0.07182 1.671870391 96.32578438 462.81534 4.45916 USP30 0.309014179184126 0.690826270295811 0.000159550520063542 ubiquitin specific peptidase 30 FUNCTION: Deubiquitinating enzyme tethered to the mitochondrial outer membrane that acts as a key inhibitor of mitophagy by counteracting the action of parkin (PARK2): hydrolyzes ubiquitin attached by parkin on target proteins, such as RHOT1/MIRO1 and TOMM20, thereby blocking parkin's ability to drive mitophagy (PubMed:18287522, PubMed:24896179, PubMed:25527291, PubMed:25621951). Preferentially cleaves 'Lys-6'- and 'Lys-11'- linked polyubiquitin chains, 2 types of linkage that participate to mitophagic signaling (PubMed:25621951). Does not cleave efficiently polyubiquitin phosphorylated at 'Ser-65' (PubMed:25527291). Acts as negative regulator of mitochondrial fusion by mediating deubiquitination of MFN1 and MFN2 (By similarity). {ECO:0000250|UniProtKB:Q3UN04, ECO:0000269|PubMed:18287522, ECO:0000269|PubMed:24896179, ECO:0000269|PubMed:25527291, ECO:0000269|PubMed:25621951}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, pancreas, liver and kidney. {ECO:0000269|PubMed:14715245}.; unclassifiable (Anatomical System);ovary;cartilage;adrenal cortex;colon;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;frontal lobe;thyroid;bone;macula lutea;visual apparatus;testis;kidney;spinal ganglion;mammary gland;stomach; superior cervical ganglion;atrioventricular node; 0.17615 0.11045 -0.135838822 43.77211607 446.0984 4.39699 USP30-AS1 . . . USP30 antisense RNA 1 . . . . . . . . . . . USP31 0.00875110488790412 0.991227125779709 2.17693323868301e-05 ubiquitin specific peptidase 31 FUNCTION: May recognize and hydrolyze the peptide bond at the C- terminal Gly of ubiquitin. Involved in the processing of poly- ubiquitin precursors as well as that of ubiquitinated proteins (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14715245}.; unclassifiable (Anatomical System);breast;lymph node;tongue;bone;thyroid;placenta;cervix;head and neck;kidney;skeletal muscle; . 0.33211 . -0.058785319 48.90894079 3849.21418 12.22397 USP32 0.999999997115398 2.88460157379256e-09 5.67549393099604e-25 ubiquitin specific peptidase 32 . . . myocardium;smooth muscle;ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;atrium;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;artery;gall bladder;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;alveolus;liver;head and neck;spleen;kidney;mammary gland;aorta;stomach; superior cervical ganglion;testis - interstitial;subthalamic nucleus;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;skeletal muscle;parietal lobe;cingulate cortex; 0.99543 0.10507 -2.078019896 1.580561453 184.4083 2.94681 USP32P1 . . . ubiquitin specific peptidase 32 pseudogene 1 . . . . . . . . . . . USP32P2 . . . ubiquitin specific peptidase 32 pseudogene 2 . . . . . . . . . . . USP32P3 . . . ubiquitin specific peptidase 32 pseudogene 3 . . . . . . . . . . . USP32P4 . . . ubiquitin specific peptidase 32 pseudogene 4 . . . . . . . . . . . USP33 0.996116690829413 0.00388330907241222 9.81746251478828e-11 ubiquitin specific peptidase 33 FUNCTION: Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta- arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:12865408, ECO:0000269|PubMed:19363159, ECO:0000269|PubMed:19424180, ECO:0000269|PubMed:23486064}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11739384}.; ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;cochlea;thyroid;germinal center;bladder;brain;amygdala;heart;tongue;spinal cord;pharynx;blood;lens;skeletal muscle;breast;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;pancreas;lung;placenta;head and neck;kidney;aorta;stomach; amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;subthalamic nucleus;cerebellum peduncles;hypothalamus;prefrontal cortex;globus pallidus;pons;parietal lobe;cingulate cortex; 0.71345 0.11489 -1.440283256 3.963198868 84.59856 1.95841 USP34 1 4.83807974452567e-19 7.26180833340831e-51 ubiquitin specific peptidase 34 FUNCTION: Ubiquitin hydrolase that can remove conjugated ubiquitin from AXIN1 and AXIN2, thereby acting as a regulator of Wnt signaling pathway. Acts as an activator of the Wnt signaling pathway downstream of the beta-catenin destruction complex by deubiquitinating and stabilizing AXIN1 and AXIN2, leading to promote nuclear accumulation of AXIN1 and AXIN2 and positively regulate beta-catenin (CTNBB1)-mediated transcription. Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. {ECO:0000269|PubMed:21383061}.; . TISSUE SPECIFICITY: Expressed in brain at low level. {ECO:0000269|PubMed:14715245}.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - interstitial;adrenal cortex;pons;atrioventricular node;skeletal muscle;skin;prostate;uterus corpus;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.83824 0.09517 -3.59020415 0.300778485 689.89772 5.23798 USP35 0.0434784639735485 0.955333520637267 0.0011880153891847 ubiquitin specific peptidase 35 . . TISSUE SPECIFICITY: Expressed in testis, pancreas and skeletal muscle. {ECO:0000269|PubMed:14715245}.; . . 0.29387 0.10788 2.054084984 97.78249587 3588.48457 11.60027 USP36 0.0685526746674987 0.931442512852322 4.8124801789696e-06 ubiquitin specific peptidase 36 FUNCTION: May be required for maintaining multiple types of adult stem cells. May function as a transcriptional repressor by continually deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, thereby preventing histone H3 'Lys-4' trimethylation (H3K4) (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:14715245}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach; ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.09500 0.10652 2.111136169 97.90044822 2634.3568 9.62945 USP37 0.998322478621928 0.00167752136540542 1.26671161815626e-11 ubiquitin specific peptidase 37 FUNCTION: Deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), thereby promoting S phase entry. Specifically mediates deubiquitination of 'Lys-11'- linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex. Also mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2). {ECO:0000269|PubMed:21596315}.; . TISSUE SPECIFICITY: Expressed in brain and prostate. {ECO:0000269|PubMed:14715245}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;atrium;frontal lobe;endometrium;bone;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;macula lutea;hypopharynx;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.31043 0.09688 0.488730112 79.52347252 256.06138 3.44136 USP38 5.91380852389764e-05 0.998754927069113 0.00118593484564831 ubiquitin specific peptidase 38 FUNCTION: Deubiquitinating enzyme exhibiting a preference towards 'Lys-63'-linked Ubiquitin chains. {ECO:0000269|PubMed:22689415}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Expressed in adrenal gland. {ECO:0000269|PubMed:11572484, ECO:0000269|PubMed:14715245}.; ovary;colon;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;skeletal muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; . 0.14264 0.09678 -1.262067713 5.284265157 164.3806 2.79923 USP39 0.0316077960336367 0.967999847751951 0.000392356214412706 ubiquitin specific peptidase 39 FUNCTION: Plays a role in pre-mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. Regulates AURKB mRNA levels, and thereby plays a role in cytokinesis and in the spindle checkpoint. Does not have ubiquitin-specific peptidase activity, but could be a competitor of ubiquitin C-terminal hydrolases (UCHs). {ECO:0000269|PubMed:11350945, ECO:0000269|PubMed:18728397}.; . . ovary;umbilical cord;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;bile duct;pancreas;lung;placenta;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;tumor;white blood cells;skeletal muscle;thymus; 0.33730 0.11066 -0.580403979 18.58928993 200.68092 3.06257 USP40 1.74474759846129e-14 0.764370205739466 0.235629794260516 ubiquitin specific peptidase 40 FUNCTION: May be catalytically inactive.; . TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:14715245}.; unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;muscle;colon;skin;retina;uterus;pancreas;prostate;lung;larynx;amnion;duodenum;testis;spleen;brain;mammary gland;bladder;stomach; atrioventricular node; 0.06046 0.09101 0.501484965 79.67681057 7072.32994 18.02774 USP41 . . . ubiquitin specific peptidase 41 FUNCTION: May recognize and hydrolyze the peptide bond at the C- terminal Gly of ubiquitin. Involved in the processing of poly- ubiquitin precursors as well as that of ubiquitinated proteins (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lung;thyroid;head and neck;brain;mammary gland;aorta; . 0.10092 0.09163 . . 3074.14768 10.53529 USP42 0.998681652752129 0.00131834639810823 8.49763306172143e-10 ubiquitin specific peptidase 42 FUNCTION: Deubiquitinating enzyme which may play an important role during spermatogenesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:14715245}.; unclassifiable (Anatomical System);ovary;heart;islets of Langerhans;colon;parathyroid;blood;choroid;lens;skin;retina;breast;uterus;bile duct;prostate;lung;frontal lobe;bone;placenta;visual apparatus;hypopharynx;testis;head and neck;germinal center;kidney;brain;mammary gland;stomach; . 0.14208 0.10614 0.521707177 80.39631989 3339.6684 11.06349 USP43 0.00953430437682124 0.990370768759797 9.49268633821587e-05 ubiquitin specific peptidase 43 FUNCTION: May recognize and hydrolyze the peptide bond at the C- terminal Gly of ubiquitin. Involved in the processing of poly- ubiquitin precursors as well as that of ubiquitinated proteins (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, aorta and lung at low levels. {ECO:0000269|PubMed:14715245}.; unclassifiable (Anatomical System);pancreas;ovary;placenta;colon;parathyroid;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.07394 0.09408 -0.813834387 12.05472989 268.72751 3.51655 USP44 1.46115265759899e-09 0.572502834829003 0.427497163709844 ubiquitin specific peptidase 44 FUNCTION: Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic checkpoint complex), thereby preventing premature activation of the APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint. Acts as a negative regulator of histone H2B (H2BK120ub1) ubiquitination. {ECO:0000269|PubMed:17443180, ECO:0000269|PubMed:22681888}.; . TISSUE SPECIFICITY: Expressed in testis. Expressed at high levels in T-cell acute lymphoblastic leukemia. {ECO:0000269|PubMed:14715245, ECO:0000269|PubMed:21853124}.; unclassifiable (Anatomical System);lung;testis;kidney;germinal center;brain; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion; 0.27637 0.08720 -0.286522835 33.47487615 564.79903 4.82573 USP45 8.69749163787703e-14 0.126965076024436 0.873034923975477 ubiquitin specific peptidase 45 . . TISSUE SPECIFICITY: Broadly expressed, with highest levels in ovary, skeletal muscle and spleen. {ECO:0000269|PubMed:14715245}.; colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;lung;adrenal gland;placenta;hippocampus;amnion;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.04910 0.07921 1.670043565 96.31398915 5304.05504 15.05283 USP46 0.911054239074288 0.088809549198779 0.000136211726932761 ubiquitin specific peptidase 46 FUNCTION: Deubiquitinating enzyme that plays a role in behavior, possibly by regulating GABA action. May act by mediating the deubiquitination of GAD1/GAD67. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2. {ECO:0000269|PubMed:19075014}.; . TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:14715245}.; . . 0.50572 0.11809 -0.229483771 36.86010852 7.68154 0.28352 USP46-AS1 . . . USP46 antisense RNA 1 . . . . . . . . . . . USP47 0.999999875159451 1.24840548689015e-07 6.62831458348528e-19 ubiquitin specific peptidase 47 FUNCTION: Ubiquitin-specific protease that specifically deubiquitinates monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby playing a role in base-excision repair (BER). Acts as a regulator of cell growth and genome integrity. May also indirectly regulate CDC25A expression at a transcriptional level. {ECO:0000269|PubMed:19966869, ECO:0000269|PubMed:21362556}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle, heart and testis. {ECO:0000269|PubMed:14715245}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;spinal cord;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; medulla oblongata;prefrontal cortex;ciliary ganglion; 0.19043 0.11020 -0.617221851 17.44515216 110.15644 2.28179 USP48 0.999997429389181 2.57061081894379e-06 2.12518744549928e-16 ubiquitin specific peptidase 48 FUNCTION: Recognizes and hydrolyzes the peptide bond at the C- terminal Gly of ubiquitin. Involved in the processing of poly- ubiquitin precursors as well as that of ubiquitinated proteins. May be involved in the regulation of NF-kappa-B activation by TNF receptor superfamily via its interactions with RELA and TRAF2. May also play a regulatory role at postsynaptic sites. {ECO:0000269|PubMed:16214042}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14715245, ECO:0000269|PubMed:15354349, ECO:0000269|PubMed:16214042}.; ovary;colon;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;muscle;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;caudate nucleus;trigeminal ganglion;parietal lobe;cingulate cortex; 0.10091 0.10216 -0.556537043 19.72753008 115.55589 2.33734 USP49 0.943537458576996 0.05645384839218 8.69303082421997e-06 ubiquitin specific peptidase 49 FUNCTION: Specifically deubiquitinates histone H2B at 'Lys-120' (H2BK120Ub). H2BK120Ub is a specific tag for epigenetic transcriptional activation and acts as a regulator of mRNA splicing. Deubiquitination is required for efficient cotranscriptional splicing of a large set of exons. {ECO:0000269|PubMed:23824326}.; . . unclassifiable (Anatomical System);larynx;liver;head and neck;kidney;germinal center;lens; . 0.49012 0.12138 -0.003562597 53.72729417 193.6102 3.01964 USP50 1.23258212279927e-14 0.000828487192374554 0.999171512807613 ubiquitin specific peptidase 50 FUNCTION: Has no peptidase activity.; . TISSUE SPECIFICITY: Weakly expressed in a few tissues. {ECO:0000269|PubMed:14715245}.; . . 0.09679 0.09942 0.396906589 76.30927105 252.81646 3.42178 USP51 0.912300847179826 0.0870591061218921 0.000640046698281738 ubiquitin specific peptidase 51 . . TISSUE SPECIFICITY: Expressed in prostate, brain, lung, aorta and kidney. {ECO:0000269|PubMed:14715245}.; . . 0.10750 0.08767 -0.359940251 28.93371078 27.43022 0.88428 USP53 0.00105335346562689 0.998927660129814 1.89864045588533e-05 ubiquitin specific peptidase 53 FUNCTION: Has no peptidase activity. {ECO:0000269|PubMed:14715245}.; . . unclassifiable (Anatomical System);cartilage;ovary;heart;lacrimal gland;urinary;colon;parathyroid;skin;bone marrow;breast;uterus;atrium;lung;cerebral cortex;endometrium;oesophagus;placenta;liver;testis;amniotic fluid;germinal center;kidney;brain;aorta;stomach; . 0.25627 0.10278 0.828538765 88.1104034 1721.24468 7.65244 USP54 3.94252208286798e-05 0.999960428654221 1.4612495016568e-07 ubiquitin specific peptidase 54 FUNCTION: Has no peptidase activity.; . TISSUE SPECIFICITY: Weakly expressed in a few tissues. {ECO:0000269|PubMed:14715245}.; umbilical cord;colon;skin;uterus;prostate;frontal lobe;endometrium;larynx;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;pineal body;blood;skeletal muscle;breast;lung;hypopharynx;spleen;head and neck;cervix;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.25485 . 1.056322654 91.37768342 558.05848 4.79816 USPL1 0.491296980027037 0.508664119223449 3.89007495136969e-05 ubiquitin specific peptidase like 1 FUNCTION: SUMO-specific isopeptidase involved in protein desumoylation. Specifically binds SUMO proteins with a higher affinity for SUMO2 and SUMO3 which it cleaves more efficiently. Also able to process full-length SUMO proteins to their mature forms. May have non-catalytic functions in Cajal bodies organization and cell proliferation. {ECO:0000269|PubMed:22878415}.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;cervix;kidney;stomach;aorta; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;atrioventricular node;trigeminal ganglion; 0.10870 0.08523 0.45374373 78.05496579 2982.03517 10.36293 UST 0.984203294606023 0.0157877362198489 8.96917412819243e-06 uronyl 2-sulfotransferase FUNCTION: Sulfotransferase that catalyzes the transfer of sulfate to the position 2 of uronyl residues. Has mainly activity toward iduronyl residues in dermatan sulfate, and weaker activity toward glucuronyl residues of chondroitin sulfate. Has no activity toward desulfated N-resulfated heparin.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10187838}.; . . 0.20757 0.12558 -0.514264485 21.41424864 224.05841 3.23683 UST-AS1 . . . UST antisense RNA 1 . . . . . . . . . . . UTF1 0.150834366464766 0.633407695971805 0.215757937563429 undifferentiated embryonic cell transcription factor 1 FUNCTION: Acts as a transcriptional coactivator of ATF2. {ECO:0000269|PubMed:9748258}.; . . . . 0.62045 0.12669 . . 619.79894 5.02379 UTP3 0.00277696283555097 0.938194509971494 0.0590285271929546 UTP3, small subunit processome component homolog (S. cerevisiae) FUNCTION: Essential for gene silencing: has a role in the structure of silenced chromatin. Plays a role in the developing brain (By similarity). {ECO:0000250|UniProtKB:Q12136, ECO:0000250|UniProtKB:Q9JI13}.; . . lymphoreticular;smooth muscle;ovary;salivary gland;developmental;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;gum;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;lens;breast;bile duct;lung;placenta;macula lutea;visual apparatus;hippocampus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach; smooth muscle;white blood cells; 0.05932 0.09551 0.795569043 87.49115357 195.12242 3.02810 UTP4 . . . UTP4, small subunit processome component FUNCTION: May be a transcriptional regulator. Acts as a positive regulator of HIVEP1 which specifically binds to the DNA sequence 5'-GGGACTTTCC-3' found in enhancer elements of numerous viral promoters such as those of HIV-1, SV40, or CMV. Ribosome biogenesis factor involved in small subunit (SSU) pre-rRNA processing at sites A', A0, 1 and 2b. {ECO:0000269|PubMed:19732766, ECO:0000269|PubMed:22916032}.; DISEASE: North American Indian childhood cirrhosis (NAIC) [MIM:604901]: Severe autosomal recessive intrahepatic cholestasis, originally described in Ojibway-Cree children from northwestern Quebec. NAIC typically presents with transient neonatal jaundice, in a child who is otherwise healthy, and progresses to biliary cirrhosis and portal hypertension. Biochemical and histopathological features suggest involvement of the bile ducts rather than of the bile canaliculi. They include elevated gamma glutamyltransferase and alkaline phosphatase levels, and, typically, marked fibrosis around bile ducts. Clinically, NAIC is distinct from other nonsyndromic familial cholestases because of its marked cholangiopathic features and severe degree of fibrosis on liver histology. {ECO:0000269|PubMed:12417987}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.44263 0.15216 -0.132199953 43.97853267 . . UTP6 4.82881497097119e-06 0.998225458975612 0.00176971220941671 UTP6, small subunit processome component FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. {ECO:0000250}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;lacrimal gland;spinal cord;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; medulla oblongata;superior cervical ganglion;testis - seminiferous tubule;temporal lobe;testis;pons;trigeminal ganglion;skeletal muscle; 0.13270 0.09885 0.396906589 76.30927105 3729.83617 11.93720 UTP11 . . . UTP11, small subunit processome component homolog (S. cerevisiae) FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. {ECO:0000250}.; . . . . 0.14100 0.11081 -0.029247611 51.40363293 . . UTP14A 0.999629562781925 0.000370436277025504 9.41049053507671e-10 UTP14A small subunit processome component FUNCTION: May be required for ribosome biogenesis. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15289605}.; . . 0.42936 0.09654 0.396906589 76.30927105 548.95659 4.76611 UTP14C 0.00117836245561414 0.956006670909498 0.0428149666348877 UTP14, small subunit processome component homolog C (S. cerevisiae) FUNCTION: Essential for spermatogenesis. May be required specifically for ribosome biogenesis and hence protein synthesis during male meiosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:15289605}.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:15289605}.; . . . . 0.112125503 62.09601321 489.05369 4.55190 UTP15 0.985835503072082 0.0141642156681029 2.81259815009216e-07 UTP15, small subunit processome component FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. {ECO:0000250}.; . . unclassifiable (Anatomical System);islets of Langerhans;colon;skin;retina;uterus;whole body;lung;placenta;liver;testis;cervix;kidney;brain;stomach; . 0.18584 0.12379 0.088260113 60.56853031 . . UTP18 0.415444933293643 0.584212355085343 0.000342711621014388 UTP18, small subunit processome component FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. {ECO:0000250}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;pharynx;blood;lens;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;trigeminal ganglion; 0.47733 0.08388 0.106667882 61.73036093 115.25085 2.33506 UTP20 0.170231062921548 0.829768937078452 1.89757234409467e-16 UTP20, small subunit processome component FUNCTION: Involved in 18S pre-rRNA processing. Associates with U3 snoRNA. {ECO:0000269|PubMed:17498821}.; . TISSUE SPECIFICITY: Expressed in appendix, brain, colon, fetal liver, heart, ovary, pancreas, placenta, prostate, skeletal muscle, small intestine, spleen, testis and thymus. {ECO:0000269|PubMed:9673349}.; ovary;salivary gland;intestine;colon;skin;prostate;thyroid;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;cornea;nasopharynx;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;pons; 0.58707 0.11099 1.328417555 94.13187072 1479.4111 7.16252 UTP23 0.033108947324346 0.820504075718302 0.146386976957352 UTP23, small subunit processome component FUNCTION: Involved in rRNA-processing and ribosome biogenesis. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;heart;ovary;hypothalamus;skin;skeletal muscle;uterus;pancreas;prostate;whole body;lung;nasopharynx;hippocampus;testis;germinal center;kidney;brain;mammary gland;cerebellum; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.04663 0.11300 0.415317661 76.81056853 1940.84801 8.10743 UTRN 2.96803315260187e-09 0.999999997031967 2.23662207392544e-20 utrophin FUNCTION: May play a role in anchoring the cytoskeleton to the plasma membrane. {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 has high expression in muscle. Isoforms Up70 and Up140 were found in all the adult and fetal tissues tested and relatively abundant in lung and kidney. {ECO:0000269|PubMed:10369873}.; . . 0.17851 0.56056 -1.550042262 3.255484784 1957.13132 8.14203 UTS2 0.151041459001058 0.777233582063522 0.0717249589354195 urotensin 2 FUNCTION: Highly potent vasoconstrictor.; . TISSUE SPECIFICITY: Brain specific.; pancreas;colon;spleen; superior cervical ganglion;trigeminal ganglion; 0.03297 0.16627 1.148343558 92.42745931 3263.36512 10.90474 UTS2B 0.0110399911903071 0.838022018358006 0.150937990451687 urotensin 2B FUNCTION: Potent vasoconstrictor. {ECO:0000250}.; . . . . 0.06700 0.08899 0.902179145 89.34890304 193.24464 3.01474 UTS2R 1.80188717092643e-05 0.144335290998463 0.855646690129827 urotensin 2 receptor FUNCTION: High affinity receptor for urotensin-2 and urotensin-2B. The activity of this receptor is mediated by a G-protein that activate a phosphatidylinositol-calcium second messenger system. {ECO:0000269|PubMed:14550283}.; . TISSUE SPECIFICITY: Most abundant expression in the heart and pancreas.; unclassifiable (Anatomical System);uterus;ovary;heart;skin; . 0.12380 0.18456 . . 103.97262 2.20400 UTY 0.632058104202083 0.360934611563913 0.00700728423400396 ubiquitously transcribed tetratricopeptide repeat containing, Y-linked FUNCTION: Male-specific histone demethylase that catalyzes trimethylated 'Lys-27' (H3K27me3) demethylation in histone H3. Has relatively low lysine demethylase activity. {ECO:0000269|PubMed:24798337}.; . . unclassifiable (Anatomical System);heart;hypothalamus;colon;blood;skin;skeletal muscle;bone marrow;uterus;whole body;lung;nasopharynx;bone;liver;testis;germinal center;kidney;brain;tonsil;thymus; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.75752 . . . 8.87331 0.32711 UVRAG 0.858602500357733 0.141393685215962 3.81442630411283e-06 UV radiation resistance associated FUNCTION: Versatile protein that is involved in regulation of differenent cellular pathways implicated in membrane trafficking. Involved in regulation of the COPI-dependent retrograde transport from Golgi and the endoplasmic reticulum by associating with the NRZ complex; the function is dependent on its binding to phosphatidylinositol 3-phosphate (PtdIns(3)P) (PubMed:24056303). During autophagy acts as regulatory subunit of the alternative PI3K complex II (PI3KC3-C2) that mediates formation of phosphatidylinositol 3-phosphate and is believed to be involved in maturation of autophagosomes and endocytosis. Activates lipid kinase activity of PIK3C3. Involved in the regulation of degradative endocytic trafficking and cytokinesis, and in regulation of ATG9A transport from the Golgi to the autophagosome; the functions seems to implicate its association with PI3KC3-C2 (PubMed:16799551, PubMed:20643123, PubMed:24056303). Involved in maturation of autophagosomes and degradative endocytic trafficking independently of BECN1 but depending on its association with a class C Vps complex (possibly the HOPS complex); the association is also proposed to promote autophagosome recruitment and activation of Rab7 and endosome-endosome fusion events (PubMed:18552835). Enhances class C Vps complex (possibly HOPS complex) association with a SNARE complex and promotes fusogenic SNARE complex formation during late endocytic membrane fusion (PubMed:24550300). In case of negative-strand RNA virus infection is required for efficient virus entry, promotes endocytic transport of virions and is implicated in a VAMP8-specific fusogenic SNARE complex assembly (PubMed:24550300). {ECO:0000269|PubMed:18552835, ECO:0000269|PubMed:20643123, ECO:0000269|PubMed:24056303, ECO:0000305}.; DISEASE: Note=A chromosomal aberration involving UVRAG has been observed in a patient with heterotaxy (left-right axis malformation). Inversion Inv(11)(q13.5;q25). {ECO:0000269|PubMed:10798355}.; TISSUE SPECIFICITY: Highly expressed in brain, lung, kidney and liver. {ECO:0000269|PubMed:10798355}.; medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum;thymus; parietal lobe; 0.19836 0.09984 -0.374708069 28.15522529 1359.85776 6.92206 UVSSA 8.88754059993399e-14 0.0188540909031245 0.981145909096787 UV stimulated scaffold protein A FUNCTION: Factor involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage. TC-NER allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes. Acts by promoting stabilization of ERCC6 by recruiting deubiquitinating enzyme USP7 to TC-NER complexes, preventing UV-induced degradation of ERCC6 by the proteasome. Interacts with the elongating form of RNA polymerase II (RNA pol IIo) and facilitates its ubiquitination at UV damage sites, leading to promote RNA pol IIo backtracking to allow access to the nucleotide excision repair machinery. Not involved in processing oxidative damage. {ECO:0000269|PubMed:22466610, ECO:0000269|PubMed:22466611, ECO:0000269|PubMed:22466612}.; DISEASE: UV-sensitive syndrome 3 (UVSS3) [MIM:614640]: An autosomal recessive disorder characterized by cutaneous photosensitivity and slight dyspigmentation, without an increased risk of skin tumors. {ECO:0000269|PubMed:22466610, ECO:0000269|PubMed:22466611, ECO:0000269|PubMed:22466612}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.08194 . -1.027089224 7.873319179 284.45391 3.61140 UXS1 0.0661553399099762 0.930828162837641 0.00301649725238234 UDP-glucuronate decarboxylase 1 FUNCTION: Catalyzes the NAD-dependent decarboxylation of UDP- glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;whole body;oesophagus;endometrium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;adrenal cortex;pharynx;blood;pancreas;lung;cornea;placenta;visual apparatus;liver;amnion;spleen;kidney;mammary gland;stomach; . 0.19810 0.14695 -0.560178693 19.30879925 14.23314 0.51500 UXT 0.836315941423648 0.160467936008726 0.003216122567626 ubiquitously expressed prefoldin like chaperone FUNCTION: Involved in gene transcription regulation. Acts in concert with the corepressor URI1 to regulate androgen receptor transcription (AR). AR N-terminus-associated coactivator which may play a role in facilitating receptor-induced transcriptional activation (PubMed:11854421). Potential component of mitochondrial-associated LRPPRC, a multidomain organizer that potentially integrates mitochondria and the microtubular cytoskeleton with chromosome remodeling (PubMed:11827465). Increasing concentrations of UXT contributes to progressive aggregation of mitochondria and cell death potentially through its association with LRPPRC (PubMed:17554592). May be a nuclear chaperone that promotes formation of the NF-kappa-B enhanceosome and which is essential for its nuclear function (PubMed:17620405). Suppresses cell transformation and it might mediate this function by interaction and inhibition of the biological activity of cell proliferation and survival stimulatory factors like MECOM (PubMed:17635584). Together with URI1, associates with chromatin to the NKX3-1 promoter region. {ECO:0000269|PubMed:11827465, ECO:0000269|PubMed:11854421, ECO:0000269|PubMed:16221885, ECO:0000269|PubMed:17554592, ECO:0000269|PubMed:17620405, ECO:0000269|PubMed:17635584, ECO:0000269|PubMed:21730289}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in prostate epithelial cells. Overexpressed in a number of tumor tissues (PubMed:16221885). Highest levels in the heart, skeletal muscle, pancreas, kidney, liver, adrenal gland, peripheral blood leukocytes, lymph node, prostate, and thyroid and the lowest levels in bladder and uterus. {ECO:0000269|PubMed:11854421, ECO:0000269|PubMed:16221885, ECO:0000269|PubMed:17635584, ECO:0000269|PubMed:21730289}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;amnion;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; white blood cells;thymus; 0.61137 0.30319 -0.075159878 47.78839349 2.23961 0.07481 UXT-AS1 . . . UXT antisense RNA 1 . . . . . . . . . . . VAC14 0.629700168448247 0.370287262333662 1.25692180904546e-05 Vac14 homolog (S. cerevisiae) FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Acts as a positive activator of PIKfyve kinase activity. Also required to maintain normal levels of phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate (PtdIns(5)P). Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes. {ECO:0000269|PubMed:15542851, ECO:0000269|PubMed:17556371}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:8611628}.; myocardium;smooth muscle;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;whole body;cerebral cortex;endometrium;synovium;bone;thyroid;testis;amniotic fluid;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;lens;greater omentum;breast;pancreas;lung;placenta;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;whole brain;superior cervical ganglion;trigeminal ganglion;skin;skeletal muscle;parietal lobe; 0.19002 0.12138 -1.150005948 6.286860109 104.88216 2.21361 VAC14-AS1 . . . VAC14 antisense RNA 1 . . . . . . . . . . . VAMP1 0.673786666046467 0.321394502554586 0.00481883139894641 vesicle associated membrane protein 1 FUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane.; . TISSUE SPECIFICITY: Nervous system, skeletal muscle and adipose tissue.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;iris;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;hypothalamus;adrenal cortex;blood;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;kidney;mammary gland;stomach;thymus; dorsal root ganglion;thalamus;subthalamic nucleus;medulla oblongata;spinal cord;prefrontal cortex;globus pallidus;pons;trigeminal ganglion;parietal lobe;skeletal muscle;cingulate cortex; 0.17397 0.13715 0.235309407 68.71903751 4.55424 0.16428 VAMP2 0.837117600739375 0.159707638125956 0.00317476113466819 vesicle associated membrane protein 2 FUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. {ECO:0000250|UniProtKB:P63045}.; . TISSUE SPECIFICITY: Nervous system and skeletal muscle. {ECO:0000269|PubMed:8760387}.; unclassifiable (Anatomical System);lung;heart;islets of Langerhans;hypothalamus;thyroid;placenta;testis;kidney;brain; amygdala;whole brain;medulla oblongata;occipital lobe;superior cervical ganglion;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.42512 0.11262 -0.053113545 49.38664779 . . VAMP3 0.0542630674689049 0.864052437146541 0.0816844953845539 vesicle associated membrane protein 3 FUNCTION: SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000269|PubMed:18195106}.; . . unclassifiable (Anatomical System);lung;amnion;testis;bone marrow; occipital lobe;superior cervical ganglion;hypothalamus;spinal cord;trigeminal ganglion; 0.08819 0.16909 -0.075159878 47.78839349 4.41338 0.16013 VAMP4 0.919995933830113 0.0794972492855506 0.000506816884336569 vesicle associated membrane protein 4 FUNCTION: Involved in the pathway that functions to remove an inhibitor (probably synaptotagmin-4) of calcium-triggered exocytosis during the maturation of secretory granules. May be a marker for this sorting pathway that is critical for remodeling the secretory response of granule.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);heart;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; subthalamic nucleus;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.76739 0.12378 -0.031067188 51.03798066 17.50125 0.61412 VAMP5 0.0516197457018348 0.694042658461975 0.25433759583619 vesicle associated membrane protein 5 FUNCTION: May participate in trafficking events that are associated with myogenesis, such as myoblast fusion and/or GLUT4 trafficking.; . . myocardium;ovary;umbilical cord;salivary gland;sympathetic chain;intestine;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;optic nerve;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;pineal body;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland; heart;atrioventricular node; 0.01055 0.02598 -0.141298762 42.87567823 15.29271 0.55090 VAMP7 0.00463196348400117 0.87672313405745 0.118644902458549 vesicle associated membrane protein 7 FUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. Required for calcium regulated lysosomal exocytosis. Involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Required for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells. Required for focal exocytosis of late endocytic vesicles during phagosome formation. {ECO:0000269|PubMed:10888671, ECO:0000269|PubMed:16677249, ECO:0000269|PubMed:18042464}.; . TISSUE SPECIFICITY: Detected in all tissues tested.; ovary;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; amygdala;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.22096 0.09341 0.148941568 64.31941496 39.95849 1.17497 VAMP8 0.270489594281997 0.635487089485135 0.0940233162328685 vesicle associated membrane protein 8 FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor- attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane via its interaction with the STX17-SNAP29 binary t-SNARE complex (PubMed:23217709, PubMed:25686604). Also required for dense-granule secretion in platelets (PubMed:12130530). Plays also a role in regulated enzyme secretion in pancreatic acinar cells (By similarity). Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells (By similarity). Involved in the homotypic fusion of early and late endosomes (By similarity). {ECO:0000250|UniProtKB:Q9WUF4, ECO:0000269|PubMed:12130530, ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686604}.; . TISSUE SPECIFICITY: Platelets. {ECO:0000269|PubMed:12130530}.; lymphoreticular;smooth muscle;umbilical cord;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);trophoblast;lymph node;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; lung;trachea;placenta;fetal lung;white blood cells;kidney;whole blood;tonsil;bone marrow; 0.28502 0.23984 0.147123112 64.11299835 4.31193 0.15714 VANGL1 0.533615186185259 0.465704187658467 0.000680626156273703 VANGL planar cell polarity protein 1 . DISEASE: Sacral defect with anterior meningocele (SDAM) [MIM:600145]: Form of caudal dysgenesis. It is present at birth and becomes symptomatic later in life, usually because of obstructive labor in females, chronic constipation, or meningitis. Inheritance is autosomal dominant. {ECO:0000269|PubMed:17409324}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: According to PubMed:11956595, ubiquitously expressed. According to PubMed:12011995, expressed specifically in testis and ovary. {ECO:0000269|PubMed:11956595, ECO:0000269|PubMed:12011995}.; ovary;colon;choroid;fovea centralis;skin;retina;bone marrow;prostate;optic nerve;cerebral cortex;bone;testis;unclassifiable (Anatomical System);cartilage;hypothalamus;lens;skeletal muscle;breast;pancreas;lung;macula lutea;liver;spleen;kidney;stomach; superior cervical ganglion;skeletal muscle; 0.14560 0.12678 -0.242430445 36.22906346 1019.35056 6.14174 VANGL2 0.948574651924172 0.0514184770924579 6.87098336996756e-06 VANGL planar cell polarity protein 2 FUNCTION: Involved in the control of early morphogenesis and patterning of both axial midline structures and the development of neural plate. Plays a role in the regulation of planar cell polarity, particularly in the orientation of stereociliary bundles in the cochlea. Required for polarization and movement of myocardializing cells in the outflow tract and seems to act via RHOA signaling to regulate this process. Required for cell surface localization of FZD3 and FZD6 in the inner ear (By similarity). {ECO:0000250|UniProtKB:Q91ZD4}.; DISEASE: Neural tube defects (NTD) [MIM:182940]: Congenital malformations of the central nervous system and adjacent structures related to defective neural tube closure during the first trimester of pregnancy. Failure of neural tube closure can occur at any level of the embryonic axis. Common NTD forms include anencephaly, myelomeningocele and spina bifida, which result from the failure of fusion in the cranial and spinal region of the neural tube. NTDs have a multifactorial etiology encompassing both genetic and environmental components. {ECO:0000269|PubMed:20558380}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.70577 0.34853 -1.023168368 7.944090587 70.79043 1.75082 VAPA 0.123795283054545 0.852048625566547 0.0241560913789084 VAMP associated protein A FUNCTION: May play a role in vesicle trafficking. {ECO:0000269|PubMed:11511104, ECO:0000269|PubMed:19289470}.; . TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;spinal ganglion;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;thymus; amygdala;superior cervical ganglion; 0.57224 0.15391 0.41713504 76.95800896 31.0744 0.98144 VAPB 0.739723829926661 0.257812790747704 0.00246337932563559 VAMP (vesicle-associated membrane protein)-associated protein B and C FUNCTION: Participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity. Involved in cellular calcium homeostasis regulation. {ECO:0000269|PubMed:16891305, ECO:0000269|PubMed:20940299, ECO:0000269|PubMed:22131369}.; DISEASE: Spinal muscular atrophy, proximal, adult, autosomal dominant (SMAPAD) [MIM:182980]: A form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. SMAPAD is characterized by proximal muscle weakness that begins in the lower limbs and then progresses to upper limbs, onset in late adulthood (after third decade) and a benign course. Most of the patients remain ambulatory 10 to 40 years after clinical onset. {ECO:0000269|PubMed:15372378}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. Isoform 1 predominates.; ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lacrimal gland;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;placenta;head and neck;kidney;stomach; . 0.57790 0.20297 -0.007201372 53.19061099 29.97107 0.95757 VARS 0.67979413526559 0.32020586419191 5.42500429266912e-10 valyl-tRNA synthetase . . . . . 0.28792 0.09134 -0.326979057 30.90351498 6080.40418 16.30459 VARS2 4.21949935405234e-14 0.998945711863588 0.00105428813636968 valyl-tRNA synthetase 2, mitochondrial . DISEASE: Combined oxidative phosphorylation deficiency 20 (COXPD20) [MIM:615917]: A disorder due to mitochondrial respiratory chain complex defects. Clinical features are variable and include muscle weakness with hypotonia, central neurological disease with progressive external ophthalmoplegia, ptosis and ataxia, delayed psychomotor development, cardiomyopathy, abnormal liver function, facial dysmorphism, microcephaly and epilepsy. {ECO:0000269|PubMed:24827421, ECO:0000269|PubMed:25058219}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;frontal lobe;endometrium;larynx;thyroid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;pharynx;blood;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;stomach;aorta; ciliary ganglion;atrioventricular node; 0.02703 0.09134 2.337125365 98.40174569 7034.76855 17.90265 VASH1 0.730608113503456 0.266669227702066 0.00272265879447842 vasohibin 1 FUNCTION: Angiogenesis inhibitor. Inhibits migration, proliferation and network formation by endothelial cells as well as angiogenesis. This inhibitory effect is selective to endothelial cells as it does not affect the migration of smooth muscle cells or fibroblasts. Does not affect the proliferation of cancer cells in vitro, but inhibits tumor growth and tumor angiogenesis. Acts in an autocrine manner. Inhibits artery neointimal formation and macrophage infiltration. Exhibits heparin-binding activity. {ECO:0000269|PubMed:15467828, ECO:0000269|PubMed:16488400, ECO:0000269|PubMed:16707096}.; . TISSUE SPECIFICITY: Preferentially expressed in endothelial cells. Highly expressed in fetal organs. Expressed in brain and placenta, and at lower level in heart and kidney. Highly detected in microvessels endothelial cells of atherosclerotic lesions. {ECO:0000269|PubMed:15467828, ECO:0000269|PubMed:16707096}.; myocardium;medulla oblongata;smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;synovium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;cerebellum; . 0.14661 0.11592 -0.494039303 22.09247464 23.35804 0.77940 VASH2 0.81958256467456 0.179536770462765 0.000880664862674828 vasohibin 2 FUNCTION: Angiogenesis inhibitor. Inhibits network formation by endothelial cells. {ECO:0000269|PubMed:16528006}.; . . unclassifiable (Anatomical System);uterus;lung;whole body;heart;bone;placenta;visual apparatus;testis;kidney;brain; . 0.43259 0.11433 0.17280645 65.75843359 238.11708 3.33334 VASN 0.0538071657238598 0.863614745984555 0.0825780882915848 vasorin FUNCTION: May act as an inhibitor of TGF-beta signaling. {ECO:0000269|PubMed:15247411}.; . TISSUE SPECIFICITY: Expressed at highest levels in aorta, at intermediate levels in kidney and placenta and at lowest levels in brain, heart, liver, lung and skeletal muscle. Within the aorta, the strongest expression is found in the tunica media of the proximal ascending aorta, the descending thoracic aorta, the abdominal aorta and the coronary arteries. Within the kidney, expression is found in the interstitial cells. {ECO:0000269|PubMed:15247411}.; medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lens;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.32773 0.10430 0.04598748 57.47817882 129.76459 2.48237 VASP 0.583670616080661 0.415875145516496 0.000454238402842667 vasodilator-stimulated phosphoprotein FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin- bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation. {ECO:0000269|PubMed:10087267, ECO:0000269|PubMed:10438535, ECO:0000269|PubMed:15939738, ECO:0000269|PubMed:17082196, ECO:0000269|PubMed:18559661}.; . TISSUE SPECIFICITY: Highly expressed in platelets. {ECO:0000269|PubMed:7828592}.; lymphoreticular;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;oesophagus;bone;thyroid;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;macula lutea;alveolus;duodenum;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; atrioventricular node;whole blood;bone marrow; 0.49300 0.35835 -0.137658575 43.57159707 79.23731 1.88068 VAT1 0.0199560134236148 0.902720446590296 0.0773235399860894 vesicle amine transport 1 FUNCTION: Possesses ATPase activity (By similarity). Plays a part in calcium-regulated keratinocyte activation in epidermal repair mechanisms. Has no effect on cell proliferation. Negatively regulates mitochondrial fusion in cooperation with mitofusin proteins (MFN1-2). {ECO:0000250, ECO:0000269|PubMed:12898150, ECO:0000269|PubMed:17105775, ECO:0000269|PubMed:19508442}.; . TISSUE SPECIFICITY: Expressed in brain. Also expressed in glioblastoma cells. {ECO:0000269|PubMed:19508442}.; ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;bladder;brain;heart;cartilage;adrenal cortex;pharynx;blood;lens;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;duodenum;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;adrenal gland;ciliary ganglion;trigeminal ganglion; 0.21805 0.12777 -0.339715008 30.06605331 45.3246 1.29328 VAT1L 1.89787043215691e-05 0.696133090841089 0.303847930454589 vesicle amine transport 1-like . . TISSUE SPECIFICITY: Detected in skin fibroblasts. {ECO:0000269|PubMed:19844255}.; ovary;salivary gland;sympathetic chain;parathyroid;choroid;skin;retina;uterus;ganglion;frontal lobe;cochlea;iris;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;heart;cartilage;islets of Langerhans;adrenal cortex;lens;lung;pia mater;adrenal gland;placenta;hippocampus;aorta; amygdala;dorsal root ganglion;medulla oblongata;superior cervical ganglion;cerebellum peduncles;hypothalamus;ciliary ganglion;pons;caudate nucleus;trigeminal ganglion;cerebellum; . 0.13287 -0.290161348 33.33923095 120.82271 2.39555 VAV1 0.999993062871965 6.93712803242409e-06 2.38556611332466e-15 vav guanine nucleotide exchange factor 1 FUNCTION: Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation.; . TISSUE SPECIFICITY: Widely expressed in hematopoietic cells but not in other cell types.; unclassifiable (Anatomical System);lymph node;ovary;blood;fovea centralis;choroid;lens;retina;bone marrow;uterus;pancreas;prostate;optic nerve;lung;endometrium;bone;macula lutea;alveolus;testis;germinal center; superior cervical ganglion;pons;trigeminal ganglion; 0.69750 0.53794 -0.777005578 12.9747582 93.51499 2.08109 VAV2 0.00251877000405443 0.997475818982135 5.41101381083124e-06 vav guanine nucleotide exchange factor 2 FUNCTION: Guanine nucleotide exchange factor for the Rho family of Ras-related GTPases. Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed.; ovary;colon;parathyroid;skin;uterus;prostate;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;tongue;islets of Langerhans;urinary;adrenal cortex;blood;bile duct;pancreas;lung;epididymis;placenta;liver;spleen;head and neck;cervix;kidney;stomach;peripheral nerve;thymus; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.72090 0.30096 -1.701282638 2.553668318 361.82781 4.02640 VAV3 0.0200593234937473 0.979940413084951 2.6342130143681e-07 vav guanine nucleotide exchange factor 3 FUNCTION: Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those GTPases. Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1- induced RAC1 GTPase activation and vascular endothelial cell migration and assembly (By similarity). May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organization and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2 (ITGB2)-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3 (ITGB3)- mediated adhesion. Does not affect integrin beta-1 (ITGB1)- mediated adhesion (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 and isoform 3 are widely expressed; both are expressed at very low levels in skeletal muscle. In keratinocytes, isoform 1 is less abundant than isoform 3. Isoform 3 is detected at very low levels, if any, in adrenal gland, bone marrow, spleen, fetal brain and spinal chord; in these tissues, isoform 1 is readily detectable. {ECO:0000269|PubMed:11094073, ECO:0000269|PubMed:9705494}.; unclassifiable (Anatomical System);placenta;liver;spleen;germinal center;skeletal muscle; dorsal root ganglion;superior cervical ganglion;tongue;placenta;kidney;trigeminal ganglion;skeletal muscle; 0.70437 0.23624 -0.461076406 23.66124086 961.59362 6.00331 VAV3-AS1 . . . VAV3 antisense RNA 1 . . . . . . . . . . . VAX1 0.534984091030816 0.449797664823042 0.0152182441461418 ventral anterior homeobox 1 FUNCTION: Transcription factor that may function in dorsoventral specification of the forebrain. Required for axon guidance and major tract formation in the developing forebrain. May contribute to the differentiation of the neuroretina, pigmented epithelium and optic stalk (By similarity). {ECO:0000250}.; DISEASE: Microphthalmia, syndromic, 11 (MCOPS11) [MIM:614402]: A rare clinical entity including as main characteristics microphthalmia and small optic nerves, cleft lip and palate, absence of corpus callosum, hippocampal malformations, and absence of the pineal gland. Microphthalmia is a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. {ECO:0000269|PubMed:22095910}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . optic nerve;macula lutea;fovea centralis;choroid;lens;retina; . 0.15545 0.11094 -0.273576253 33.97027601 22.19535 0.74499 VAX2 0.315038571131068 0.61517134782429 0.0697900810446417 ventral anterior homeobox 2 FUNCTION: Transcription factor that may function in dorsoventral specification of the forebrain. Regulates the expression of Wnt signaling antagonists including the expression of a truncated TCF7L2 isoform that cannot bind CTNNB1 and acts therefore as a potent dominant-negative Wnt antagonist. Plays a crucial role in eye development and, in particular, in the specification of the ventral optic vesicle (By similarity). May be a regulator of axial polarization in the retina. {ECO:0000250}.; . . visual apparatus;tonsil;retina; skeletal muscle; 0.18454 0.11887 0.328949044 73.41354093 1323.67762 6.84191 VBP1 0.822547586801538 0.173470376586673 0.00398203661178817 von Hippel-Lindau binding protein 1 FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. {ECO:0000269|PubMed:9630229}.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;skin;bone marrow;retina;prostate;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;vein;uterus;whole body;cerebral cortex;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;whole brain;thalamus;subthalamic nucleus;occipital lobe;hypothalamus;spinal cord;prefrontal cortex;parietal lobe;cingulate cortex; 0.94477 0.12863 -0.009020804 52.8544468 3.78737 0.14059 VCAM1 0.781503144443611 0.218434609027899 6.22465284897099e-05 vascular cell adhesion molecule 1 FUNCTION: Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with integrin alpha-4/beta-1 (ITGA4/ITGB1) on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/ITGA4/ITGB1 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation.; . TISSUE SPECIFICITY: Expressed on inflammed vascular endothelium, as well as on macrophage-like and dendritic cell types in both normal and inflammed tissue.; ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;artery;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;pancreas;lung;adrenal gland;mesenchyma;nasopharynx;trabecular meshwork;placenta;liver;spleen;head and neck;kidney;mammary gland;aorta; fetal liver;superior cervical ganglion;ciliary ganglion; 0.41588 0.74828 0.154398214 64.73814579 411.51614 4.24919 VCAN 0.999750597976069 0.000249402023929709 1.00869271994714e-15 versican FUNCTION: May play a role in intercellular signaling and in connecting cells with the extracellular matrix. May take part in the regulation of cell motility, growth and differentiation. Binds hyaluronic acid.; DISEASE: Wagner vitreoretinopathy (WGVRP) [MIM:143200]: A rare vitreoretinopathy characterized by an optically empty vitreous cavity with fibrillary condensations and a preretinal avascular membrane. Other optical features include progressive chorioretinal atrophy, perivascular sheating, subcapsular cataract and myopia. {ECO:0000269|PubMed:16043844, ECO:0000269|PubMed:22739342}. Note=The disease is caused by mutations affecting the gene represented in this entry. The pathological mechanism involves a quantitave imbalance of the normally occurring splice variants (PubMed:22739342). {ECO:0000269|PubMed:22739342}.; TISSUE SPECIFICITY: Cerebral white matter and plasma. Isoform V0 and isoform V1 are expressed in normal brain, gliomas, medulloblastomas, schwannomas, neurofibromas, and meningiomas. Isoform V2 is restricted to normal brain and gliomas. Isoform V3 is found in all these tissues except medulloblastomas.; lymphoreticular;smooth muscle;ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;brain;bladder;artery;gall bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;spinal cord;urinary;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;mesenchyma;placenta;amnion;liver;spleen;head and neck;kidney;aorta;stomach; . 0.99470 0.74715 -0.548208384 19.95753715 4783.10517 14.03145 VCAN-AS1 . . . VCAN antisense RNA 1 . . . . . . . . . . . VCL 0.994870401764453 0.00512959819634457 3.92028477142522e-11 vinculin FUNCTION: Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell- surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion. {ECO:0000269|PubMed:20484056}.; DISEASE: Cardiomyopathy, dilated 1W (CMD1W) [MIM:611407]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:11815424, ECO:0000269|PubMed:16236538}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, familial hypertrophic 15 (CMH15) [MIM:613255]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:16712796}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Metavinculin is muscle-specific.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;oesophagus;larynx;bone;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;amnion;head and neck;kidney;stomach;aorta; dorsal root ganglion;uterus;superior cervical ganglion;adipose tissue;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.84455 . -1.793112871 2.229299363 332.65362 3.87638 VCP 0.999992047388692 7.95261122651884e-06 8.12694452907774e-14 valosin containing protein FUNCTION: Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites. Recruited to stalled replication forks by SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage. Required for cytoplasmic retrotranslocation of stressed/damaged mitochondrial outer-membrane proteins and their subsequent proteasomal degradation. {ECO:0000250|UniProtKB:P46462, ECO:0000269|PubMed:15456787, ECO:0000269|PubMed:16168377, ECO:0000269|PubMed:21118995, ECO:0000269|PubMed:22020440, ECO:0000269|PubMed:22120668, ECO:0000269|PubMed:22607976, ECO:0000269|PubMed:23042605, ECO:0000269|PubMed:23042607}.; DISEASE: Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 1 (IBMPFD1) [MIM:167320]: An autosomal dominant disease characterized by disabling muscle weakness clinically resembling to limb girdle muscular dystrophy, osteolytic bone lesions consistent with Paget disease, and premature frontotemporal dementia. Clinical features show incomplete penetrance. {ECO:0000269|PubMed:15034582, ECO:0000269|PubMed:15732117, ECO:0000269|PubMed:16247064}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Amyotrophic lateral sclerosis 14, with or without frontotemporal dementia (ALS14) [MIM:613954]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. Patients with ALS14 may develop frontotemporal dementia. {ECO:0000269|PubMed:21145000}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . myocardium;lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;dura mater;spinal ganglion;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;pancreas;lung;pia mater;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;trigeminal ganglion;cingulate cortex;skeletal muscle;cerebellum; . 0.55950 -0.339715008 30.06605331 14.2901 0.51675 VCPIP1 0.999341018273703 0.000658980951426218 7.74870209874422e-10 valosin containing protein (p97)/p47 complex interacting protein 1 FUNCTION: Acts as a deubiquitinating enzyme. Necessary for VCP- mediated reassembly of Golgi stacks after mitosis. May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). Mediates dissociation of the ternary complex containing STX5A, NSFL1C and VCP (By similarity). Hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains. {ECO:0000250, ECO:0000269|PubMed:23827681}.; . . unclassifiable (Anatomical System);cartilage;heart;tongue;colon;substantia nigra;skin;skeletal muscle;retina;breast;uterus;prostate;pancreas;lung;frontal lobe;endometrium;adrenal gland;larynx;nasopharynx;bone;placenta;liver;testis;head and neck;germinal center;brain;stomach;gall bladder;thymus; occipital lobe;trigeminal ganglion; 0.24239 0.11100 -0.843147538 11.2762444 144.47648 2.61819 VCPKMT 2.61753927969878e-08 0.0837819325039303 0.916218041320677 valosin containing protein lysine methyltransferase FUNCTION: Protein-lysine N-methyltransferase that specifically trimethylates 'Lys-315' of VCP/p97; this modification may decrease VCP ATPase activity. {ECO:0000269|PubMed:22948820, ECO:0000269|PubMed:23349634}.; . . . . 0.16301 0.10003 -0.005381972 53.50908233 1950.19405 8.12758 VCX 0.577712382787133 0.378149814562957 0.0441378026499104 variable charge, X-linked FUNCTION: May mediate a process in spermatogenesis or may play a role in sex ratio distortion.; . . unclassifiable (Anatomical System);prostate;lung;testis; . . . 2.149758993 97.97711724 9.77722 0.35763 VCX2 0.103436662210244 0.587639344183948 0.308923993605808 variable charge, X-linked 2 FUNCTION: May mediate a process in spermatogenesis or may play a role in sex ratio distortion.; . . unclassifiable (Anatomical System);prostate;lung;testis; . 0.07519 0.09403 . . 885.8497 5.79770 VCX3A 0.506384677528491 0.423386139965022 0.0702291825064876 variable charge, X-linked 3A FUNCTION: May mediate a process in spermatogenesis or may play a role in sex ratio distortion.; . . . . 0.06067 . . . 399.56774 4.19576 VCX3B 0.221349599841616 0.647439958491353 0.131210441667031 variable charge, X-linked 3B FUNCTION: May mediate a process in spermatogenesis or may play a role in sex ratio distortion.; . TISSUE SPECIFICITY: Expressed exclusively in testis.; . . 0.04367 . . . 3083.18537 10.54787 VCY . . . variable charge, Y-linked FUNCTION: May mediate a process in spermatogenesis or may play a role in sex ratio distortion.; . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;lung;visual apparatus;liver;testis;kidney;brain;bladder; . . . . . . . VCY1B . . . variable charge, Y-linked 1B FUNCTION: May mediate a process in spermatogenesis or may play a role in sex ratio distortion.; . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;lung;visual apparatus;liver;testis;kidney;brain;bladder; . . . . . . . VDAC1 0.975595138410154 0.0243786889131345 2.6172676711743e-05 voltage dependent anion channel 1 FUNCTION: Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective (PubMed:11845315, PubMed:18755977, PubMed:20230784, PubMed:8420959). May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis (PubMed:15033708, PubMed:25296756). {ECO:0000269|PubMed:11845315, ECO:0000269|PubMed:15033708, ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:20230784, ECO:0000269|PubMed:25296756, ECO:0000269|PubMed:8420959}.; . TISSUE SPECIFICITY: Heart, liver and skeletal muscle.; myocardium;lymphoreticular;smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;cornea;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus;cerebellum; amygdala;occipital lobe;thalamus;cingulate cortex;skeletal muscle; . . -0.295622497 32.61972163 24.73819 0.81167 VDAC1P1 . . . voltage dependent anion channel 1 pseudogene 1 . . . . . . . . . . . VDAC1P2 . . . voltage dependent anion channel 1 pseudogene 2 . . . . . . . . . . . VDAC1P3 . . . voltage dependent anion channel 1 pseudogene 3 . . . . . . . . . . . VDAC1P4 . . . voltage dependent anion channel 1 pseudogene 4 . . . . . . . . . . . VDAC1P5 . . . voltage dependent anion channel 1 pseudogene 5 FUNCTION: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Highest in testis.; . . 0.66546 0.08972 0.215080721 67.91696155 . . VDAC1P6 . . . voltage dependent anion channel 1 pseudogene 6 . . . . . . . . . . . VDAC1P7 . . . voltage dependent anion channel 1 pseudogene 7 . . . . . . . . . . . VDAC1P8 . . . voltage dependent anion channel 1 pseudogene 8 . . . . . . . . . . . VDAC1P9 . . . voltage dependent anion channel 1 pseudogene 9 . . . . . . . . . . . VDAC1P10 . . . voltage dependent anion channel 1 pseudogene 10 . . . . . . . . . . . VDAC1P11 . . . voltage dependent anion channel 1 pseudogene 11 . . . . . . . . . . . VDAC1P12 . . . voltage dependent anion channel 1 pseudogene 12 . . . . . . . . . . . VDAC1P13 . . . voltage dependent anion channel 1 pseudogene 13 . . . . . . . . . . . VDAC2 0.819301260757835 0.179814318660036 0.000884420582128459 voltage dependent anion channel 2 FUNCTION: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation- selective.; . TISSUE SPECIFICITY: Expressed in all tissues examined.; lymphoreticular;ovary;sympathetic chain;skin;retina;bone marrow;prostate;ganglion;frontal lobe;cochlea;thyroid;iris;germinal center;bladder;brain;gall bladder;heart;cartilage;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;lung;cornea;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta; . 0.71740 0.15815 -0.229483771 36.86010852 13.75608 0.50002 VDAC2P1 . . . voltage dependent anion channel 2 pseudogene 1 . . . . . . . . . . . VDAC2P2 . . . voltage dependent anion channel 2 pseudogene 2 . . . . . . . . . . . VDAC2P3 . . . voltage dependent anion channel 2 pseudogene 3 . . . . . . . . . . . VDAC2P4 . . . voltage dependent anion channel 2 pseudogene 4 . . . . . . . . . . . VDAC3 0.970696229268312 0.0292626409663907 4.1129765297146e-05 voltage dependent anion channel 3 FUNCTION: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. Highest in testis.; myocardium;ovary;skin;retina;prostate;optic nerve;ganglion;frontal lobe;endometrium;thyroid;iris;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta; amygdala;subthalamic nucleus;thalamus;occipital lobe;hypothalamus;prefrontal cortex;testis;cingulate cortex;skeletal muscle; 0.66546 0.08972 0.215080721 67.91696155 24.24821 0.79750 VDAC3P1 . . . voltage dependent anion channel 3 pseudogene 1 . . . . . . . . . . . VDI . . . vesicular stomatitis virus defective interfering particle suppression . . . . . . . . . . . VDR 0.392125211518415 0.605864041102573 0.00201074737901219 vitamin D (1,25- dihydroxyvitamin D3) receptor FUNCTION: Nuclear hormone receptor. Transcription factor that mediates the action of vitamin D3 by controlling the expression of hormone sensitive genes. Recruited to promoters via its interaction with BAZ1B/WSTF which mediates the interaction with acetylated histones, an essential step for VDR-promoter association. Plays a central role in calcium homeostasis. {ECO:0000269|PubMed:10678179, ECO:0000269|PubMed:15728261, ECO:0000269|PubMed:16252006, ECO:0000269|PubMed:16913708}.; DISEASE: Rickets vitamin D-dependent 2A (VDDR2A) [MIM:277440]: A disorder of vitamin D metabolism resulting in severe rickets, hypocalcemia and secondary hyperparathyroidism. Most patients have total alopecia in addition to rickets. {ECO:0000269|PubMed:1652893, ECO:0000269|PubMed:2177843, ECO:0000269|PubMed:2849209, ECO:0000269|PubMed:7828346, ECO:0000269|PubMed:8106618, ECO:0000269|PubMed:8381803, ECO:0000269|PubMed:8392085, ECO:0000269|PubMed:8675579, ECO:0000269|PubMed:8961271, ECO:0000269|PubMed:9005998}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lymphoreticular;ovary;salivary gland;colon;parathyroid;skin;bone marrow;uterus;whole body;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;skeletal muscle;lung;placenta;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;adrenal cortex;globus pallidus;ciliary ganglion;pons;skeletal muscle; 0.28629 0.77234 -0.622676946 17.30950696 55.75589 1.49969 VEGFA . . . vascular endothelial growth factor A FUNCTION: Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth. {ECO:0000269|PubMed:11427521, ECO:0000269|PubMed:16489009}.; DISEASE: Microvascular complications of diabetes 1 (MVCD1) [MIM:603933]: Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end- stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. {ECO:0000269|PubMed:11978667}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform VEGF189, isoform VEGF165 and isoform VEGF121 are widely expressed. Isoform VEGF206 and isoform VEGF145 are not widely expressed. A higher level expression seen in pituitary tumors as compared to the pituitary gland. {ECO:0000269|PubMed:22009797}.; smooth muscle;ovary;salivary gland;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;larynx;bone;thyroid;iris;pituitary gland;testis;brain;amygdala;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;cerebellum; superior cervical ganglion;prostate;thyroid;trigeminal ganglion;skeletal muscle; 0.27201 0.09418 . . 95.26537 2.10662 VEGFB 1.52262082590775e-06 0.125990206972131 0.874008270407044 vascular endothelial growth factor B FUNCTION: Growth factor for endothelial cells. VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis.; . TISSUE SPECIFICITY: Expressed in all tissues except liver. Highest levels found in heart, skeletal muscle and pancreas.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;iris;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;tongue;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; . 0.30788 0.17701 0.395088462 76.15003539 155.52306 2.72499 VEGFC 0.115230709366776 0.878925727896459 0.00584356273676518 vascular endothelial growth factor C FUNCTION: Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates VEGFR-2 (KDR/FLK1) and VEGFR-3 (FLT4) receptors. {ECO:0000269|PubMed:20145116}.; DISEASE: Lymphedema, hereditary, 1D (LMPH1D) [MIM:615907]: A chronic disabling condition which results in swelling of the extremities due to altered lymphatic flow. Patients with lymphedema suffer from recurrent local infections and physical impairment. {ECO:0000269|PubMed:23410910, ECO:0000269|PubMed:24744435}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Spleen, lymph node, thymus, appendix, bone marrow, heart, placenta, ovary, skeletal muscle, prostate, testis, colon and small intestine and fetal liver, lung and kidney, but not in peripheral blood lymphocyte.; unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;skin;bone marrow;uterus;pancreas;whole body;lung;bone;liver;testis;spleen;brain; superior cervical ganglion;appendix;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.33469 0.17432 0.194852702 67.03231894 95.6586 2.11275 VENTX 3.99153777112171e-09 0.014783425381444 0.985216570627018 VENT homeobox FUNCTION: May be involved in ventralization.; . TISSUE SPECIFICITY: Expressed in bone marrow of patients recovering from chemotherapy. Also expressed in an erythroleukemia cell line. {ECO:0000269|PubMed:11549314}.; . . 0.20576 0.08178 . . 1315.45678 6.81943 VENTXP1 . . . VENT homeobox pseudogene 1 . . TISSUE SPECIFICITY: Expressed in testis and melanoma cell lines. {ECO:0000269|PubMed:10790436}.; . . . . . . . . VENTXP2 . . . VENT homeobox pseudogene 2 . . . . . . . . . . . VENTXP3 . . . VENT homeobox pseudogene 3 . . . . . . . . . . . VENTXP4 . . . VENT homeobox pseudogene 4 . . . . . . . . . . . VENTXP5 . . . VENT homeobox pseudogene 5 . . . . . . . . . . . VENTXP6 . . . VENT homeobox pseudogene 6 . . . . . . . . . . . VENTXP7 . . . VENT homeobox pseudogene 7 . . . . . . . . . . . VEPH1 9.32876839110736e-12 0.260769387479385 0.739230612511286 ventricular zone expressed PH domain containing 1 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;adrenal cortex;parathyroid;blood;vein;skin;bone marrow;uterus;lung;endometrium;bone;placenta;testis;kidney;brain;mammary gland; superior cervical ganglion;atrioventricular node; 0.16283 0.09703 1.071061453 91.69025714 3650.39187 11.74053 VEZF1 0.943031802518397 0.0569243248460933 4.38726355094582e-05 vascular endothelial zinc finger 1 FUNCTION: Possible transcription factor. Specifically binds to the CT/GC-rich region of the interleukin-3 promoter and mediates tax transactivation of IL-3. {ECO:0000269|PubMed:8035792}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highest levels in skeletal muscle and kidney. {ECO:0000269|PubMed:8035792}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;endometrium;bone;pituitary gland;testis;germinal center;gall bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;spleen;kidney;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.87973 0.12207 -0.648365105 16.35999056 535.80528 4.71846 VEZF1P1 . . . vascular endothelial zinc finger 1 pseudogene 1 . . . . . . . . . . . VEZT 0.0259368505876322 0.973534683928432 0.00052846548393604 vezatin, adherens junctions transmembrane protein FUNCTION: Plays a pivotal role in the establishment of adherens junctions and their maintenance in adult life. In case of Listeria infection, promotes bacterial internalization by participating in myosin VIIa recruitment to the entry site. {ECO:0000269|PubMed:15090598}.; . . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;skeletal muscle;breast;pancreas;lung;mesenchyma;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;stomach;thymus; . 0.30494 0.10098 1.377921151 94.56829441 1270.82062 6.71709 VGF 0.825896021447167 0.173304783190575 0.000799195362257886 VGF nerve growth factor inducible FUNCTION: May be involved in the regulation of cell-cell interactions or in synatogenesis during the maturation of the nervous system. {ECO:0000250}.; FUNCTION: Antimicrobial peptide VGF[554-577]: Has bactericidal activity against M. luteus, and antifungal activity against P. Pastoris. {ECO:0000269|PubMed:23250050}.; . TISSUE SPECIFICITY: Central and peripheral nervous systems, synthesized exclusively in neuronal and neuroendocrine cells. {ECO:0000269|PubMed:19194657}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;hypothalamus;fovea centralis;choroid;lens;skin;retina;pancreas;optic nerve;lung;macula lutea;pituitary gland;spinal ganglion;brain;stomach; trigeminal ganglion; 0.37951 0.19435 . . 314.29643 3.77034 VGLL1 0.449924752430081 0.522028504085399 0.0280467434845198 vestigial like family member 1 FUNCTION: May act as a specific coactivator for the mammalian TEFs. {ECO:0000269|PubMed:10518497}.; . . . . 0.67331 0.10118 -0.073340031 48.11866006 72.00637 1.76613 VGLL2 0.860675374641015 0.137216778573115 0.00210784678587046 vestigial like family member 2 FUNCTION: May act as a specific coactivator for the mammalian TEFs. May play a role in the development of skeletal muscles.; . TISSUE SPECIFICITY: Skeletal muscle. {ECO:0000269|PubMed:12617818}.; uterus;whole body;heart;placenta;liver;brain;skin;skeletal muscle; superior cervical ganglion;skeletal muscle; 0.27275 0.11752 . . 85.46541 1.97098 VGLL3 0.336018871714114 0.649298687953542 0.014682440332344 vestigial like family member 3 FUNCTION: May act as a specific coactivator for the mammalian TEFs. {ECO:0000250|UniProtKB:Q8N8G2}.; . TISSUE SPECIFICITY: Enriched in placenta. {ECO:0000269|PubMed:12376544}.; . . 0.06940 0.10715 0.12689526 63.00424628 86.88671 1.99025 VGLL4 0.469478552740923 0.506059627097102 0.0244618201619752 vestigial like family member 4 FUNCTION: May act as a specific coactivator for the mammalian TEFs. {ECO:0000250}.; . . lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;prefrontal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.36076 0.09887 -0.001743238 53.85114414 53.61726 1.45755 VHL 0.0337352004297955 0.822793415038476 0.143471384531729 von Hippel-Lindau tumor suppressor FUNCTION: Involved in the ubiquitination and subsequent proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Seems to act as a target recruitment subunit in the E3 ubiquitin ligase complex and recruits hydroxylated hypoxia- inducible factor (HIF) under normoxic conditions. Involved in transcriptional repression through interaction with HIF1A, HIF1AN and histone deacetylases. Ubiquitinates, in an oxygen-responsive manner, ADRB2. {ECO:0000269|PubMed:10944113, ECO:0000269|PubMed:17981124, ECO:0000269|PubMed:19584355}.; DISEASE: Pheochromocytoma (PCC) [MIM:171300]: A catecholamine- producing tumor of chromaffin tissue of the adrenal medulla or sympathetic paraganglia. The cardinal symptom, reflecting the increased secretion of epinephrine and norepinephrine, is hypertension, which may be persistent or intermittent. {ECO:0000269|PubMed:12000816, ECO:0000269|PubMed:14500403, ECO:0000269|PubMed:9663592}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: von Hippel-Lindau disease (VHLD) [MIM:193300]: VHLD is a dominantly inherited familial cancer syndrome predisposing to a variety of malignant and benign neoplasms, most frequently retinal, cerebellar and spinal hemangioblastoma, renal cell carcinoma (RCC), pheochromocytoma, and pancreatic tumors. VHL type 1 is without pheochromocytoma, type 2 is with pheochromocytoma. VHL type 2 is further subdivided into types 2A (pheochromocytoma, retinal angioma, and hemangioblastomas without renal cell carcinoma and pancreatic cyst) and 2B (pheochromocytoma, retinal angioma, and hemangioblastomas with renal cell carcinoma and pancreatic cyst). {ECO:0000269|PubMed:10408776, ECO:0000269|PubMed:10533030, ECO:0000269|PubMed:10627136, ECO:0000269|PubMed:10635329, ECO:0000269|PubMed:16502427, ECO:0000269|PubMed:7728151, ECO:0000269|PubMed:7987306, ECO:0000269|PubMed:8493574, ECO:0000269|PubMed:8592333, ECO:0000269|PubMed:8634692, ECO:0000269|PubMed:8730290, ECO:0000269|PubMed:8825918, ECO:0000269|PubMed:8956040, ECO:0000269|PubMed:9452032, ECO:0000269|PubMed:9452106, ECO:0000269|PubMed:9829911, ECO:0000269|PubMed:9829912, ECO:0000269|Ref.41}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Erythrocytosis, familial, 2 (ECYT2) [MIM:263400]: An autosomal recessive disorder characterized by an increase in serum red blood cell mass, hypersensitivity of erythroid progenitors to erythropoietin, increased erythropoietin serum levels, and normal oxygen affinity. Patients with ECYT2 carry a high risk for peripheral thrombosis and cerebrovascular events. {ECO:0000269|PubMed:12393546, ECO:0000269|PubMed:12844285}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Renal cell carcinoma (RCC) [MIM:144700]: Renal cell carcinoma is a heterogeneous group of sporadic or hereditary carcinoma derived from cells of the proximal renal tubular epithelium. It is subclassified into clear cell renal carcinoma (non-papillary carcinoma), papillary renal cell carcinoma, chromophobe renal cell carcinoma, collecting duct carcinoma with medullary carcinoma of the kidney, and unclassified renal cell carcinoma. Clear cell renal cell carcinoma is the most common subtype. {ECO:0000269|PubMed:11986208}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the adult and fetal brain and kidney.; unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;colon;blood;vein;skin;bone marrow;breast;uterus;prostate;whole body;lung;larynx;bone;thyroid;placenta;visual apparatus;liver;hypopharynx;testis;head and neck;spleen;brain;stomach; superior cervical ganglion;appendix;globus pallidus;pons;trigeminal ganglion; 0.11429 . 0.058937498 58.26256192 13.42797 0.48882 VHLL 0.00290057346415176 0.579049499361522 0.418049927174326 von Hippel-Lindau tumor suppressor like FUNCTION: Functions as a dominant-negative VHL to serve as a protector of HIFalpha. {ECO:0000269|PubMed:14757845}.; . TISSUE SPECIFICITY: Abundantly expressed in the placenta. {ECO:0000269|PubMed:14757845}.; . . 0.10493 . . . 47.4749 1.33777 VIL1 1.21278222497287e-05 0.999514699791872 0.000473172385878559 villin 1 FUNCTION: Epithelial cell-specific Ca(2+)-regulated actin- modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination. {ECO:0000269|PubMed:11500485, ECO:0000269|PubMed:14594952, ECO:0000269|PubMed:15084600, ECO:0000269|PubMed:15272027, ECO:0000269|PubMed:15342783, ECO:0000269|PubMed:16921170, ECO:0000269|PubMed:17182858, ECO:0000269|PubMed:17229814, ECO:0000269|PubMed:17606613, ECO:0000269|PubMed:18054784, ECO:0000269|PubMed:18198174, ECO:0000269|PubMed:19808673, ECO:0000269|PubMed:3087992}.; DISEASE: Note=Biliary atresia is a chronic and progressive cholestatic liver disease of chilhood characterized by an abnormal villin gene expression and severe malformation of canalicular microvillus structure.; TISSUE SPECIFICITY: Specifically expressed in epithelial cells. Major component of microvilli of intestinal epithelial cells and kidney proximal tubule cells. Expressed in canalicular microvilli of hepatocytes (at protein level). {ECO:0000269|PubMed:14550699, ECO:0000269|PubMed:3453110}.; unclassifiable (Anatomical System);bile duct;small intestine;islets of Langerhans;liver;colon;spleen;kidney;skeletal muscle;stomach; superior cervical ganglion;ciliary ganglion;kidney;trigeminal ganglion;skeletal muscle; 0.33909 0.35821 0.211232079 67.53951404 659.45231 5.14841 VILL 3.00934969096386e-12 0.67954670534772 0.320453294649271 villin-like FUNCTION: Possible tumor suppressor.; . TISSUE SPECIFICITY: Ubiquitously expressed in 16 tissues examined.; medulla oblongata;colon;choroid;fovea centralis;retina;prostate;optic nerve;whole body;frontal lobe;thyroid;testis;brain;unclassifiable (Anatomical System);nervous;islets of Langerhans;urinary;lens;skeletal muscle;breast;pancreas;lung;placenta;hippocampus;macula lutea;stomach;thymus; superior cervical ganglion;medulla oblongata;caudate nucleus;cingulate cortex; 0.36993 0.11810 -1.502810938 3.573956122 1844.77155 7.92187 VIM 0.959386089206453 0.0405951248020858 1.87859914610642e-05 vimentin FUNCTION: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. {ECO:0000269|PubMed:21746880}.; DISEASE: Cataract 30 (CTRCT30) [MIM:116300]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in fibroblasts, some expression in T- and B-lymphocytes, and little or no expression in Burkitt's lymphoma cell lines. Expressed in many hormone- independent mammary carcinoma cell lines. {ECO:0000269|PubMed:2472876, ECO:0000269|PubMed:3371665}.; unclassifiable (Anatomical System);ovary;hypothalamus;colon;skin;bile duct;uterus;prostate;frontal lobe;bone;thyroid;placenta;hippocampus;liver;testis;head and neck;cervix;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;olfactory bulb;smooth muscle;adipose tissue;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.71803 0.95763 -0.824740496 11.67728238 26.03407 0.84606 VIM-AS1 . . . VIM antisense RNA 1 . . . . . . . . . . . VIM2P . . . vimentin 2, pseudogene . . . . . . . . . . . VIMP 4.99881344822127e-11 0.00802238950611937 0.991977610443892 VCP interacting membrane selenoprotein FUNCTION: Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination. {ECO:0000269|PubMed:15215856}.; . . . . . . -0.095386216 46.48502005 247.54215 3.39307 VIP 0.00582894419478932 0.727020823165819 0.267150232639392 vasoactive intestinal peptide FUNCTION: VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder. {ECO:0000269|PubMed:15013843}.; . . . . 0.31907 0.33063 -0.119252484 44.53880632 17.63265 0.61796 VIPAS39 0.000534939494815586 0.999414770804351 5.02897008334108e-05 VPS33B interacting protein, apical-basolateral polarity regulator, spe-39 homolog FUNCTION: Proposed to be involved in endosomal maturation implicating in part VPS33B. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical RAB11A- dependent recycling pathway and in the maintenance of the apical- basolateral polarity (PubMed:20190753). May play a role in lysosomal trafficking, probably via association with the core HOPS complex in a discrete population of endosomes; the functions seems to be indepenedent of VPS33B (PubMed:19109425). May play a role in vesicular trafficking during spermatogenesis (By similarity). May be involved in direct or indirect transcriptional regulation of E- cadherin (By similarity). {ECO:0000250|UniProtKB:Q23288, ECO:0000269|PubMed:19109425, ECO:0000269|PubMed:20190753}.; DISEASE: Arthrogryposis, renal dysfunction and cholestasis syndrome 2 (ARCS2) [MIM:613404]: A multisystem disorder, characterized by neurogenic arthrogryposis multiplex congenita, renal tubular dysfunction and neonatal cholestasis with bile duct hypoplasia and low gamma glutamyl transpeptidase activity. Platelet dysfunction is common. Note=The disease is caused by mutations affecting the gene represented in this entry. In liver, CEACAM5 and ABCB11 are mislocalized and E-cadherin expression is decreased.; . . . 0.21414 0.11899 -0.402212257 26.7338995 104.24379 2.20622 VIPR1 8.27528331892667e-10 0.146473233491084 0.853526765681387 vasoactive intestinal peptide receptor 1 FUNCTION: This is a receptor for VIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. The affinity is VIP = PACAP-27 > PACAP-38. {ECO:0000269|PubMed:8926282}.; . TISSUE SPECIFICITY: In lung, HT-29 colonic epithelial cells, Raji B-lymphoblasts. Lesser extent in brain, heart, kidney, liver and placenta. Not expressed in CD4+ or CD8+ T-cells. Expressed in the T-cell lines HARRIS, HuT 78, Jurkat and SUP-T1, but not in the T- cell lines Peer, MOLT-4, HSB and YT. {ECO:0000269|PubMed:8926282}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;urinary;colon;parathyroid;lens;skin;skeletal muscle;uterus;prostate;lung;endometrium;adrenal gland;gum;placenta;liver;testis;cervix;spleen;kidney;brain;mammary gland;stomach; prefrontal cortex; 0.44612 0.24054 -0.44448505 24.46331682 138.65682 2.56536 VIPR1-AS1 . . . VIPR1 antisense RNA 1 . . . . . . . . . . . VIPR2 9.34378712597189e-07 0.923493205744109 0.0765058598771787 vasoactive intestinal peptide receptor 2 FUNCTION: This is a receptor for VIP as well as PACAP-38 and -27, the activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Can be coupled to phospholipase C. {ECO:0000269|PubMed:8926282}.; . TISSUE SPECIFICITY: Expressed in CD4+ T-cells, but not in CD8+ T- cells. Expressed in the T-cell lines Jurkat, Peer, MOLT-4, HSB, YT and SUP-T1, but not in the T-cell lines HARRIS and HuT 78. {ECO:0000269|PubMed:8926282}.; unclassifiable (Anatomical System);heart;cartilage;salivary gland;muscle;colon;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;macula lutea;cervix;brain; dorsal root ganglion;superior cervical ganglion;temporal lobe;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.13314 0.16674 -0.622676946 17.30950696 322.60143 3.81448 VIS1 . . . viral integration site 1 . . . . . . . . . . . VIT 4.91295866698497e-22 0.000182002557146844 0.999817997442853 vitrin FUNCTION: Promotes matrix assembly and cell adhesiveness. {ECO:0000250}.; . . . . 0.60959 0.18993 -0.679732631 15.39278132 3494.87032 11.38425 VKORC1 0.0818030758329219 0.756312664876125 0.161884259290953 vitamin K epoxide reductase complex subunit 1 FUNCTION: Involved in vitamin K metabolism. Catalytic subunit of the vitamin K epoxide reductase (VKOR) complex which reduces inactive vitamin K 2,3-epoxide to active vitamin K. Vitamin K is required for the gamma-carboxylation of various proteins, including clotting factors, and is required for normal blood coagulation, but also for normal bone development. {ECO:0000269|PubMed:14765194, ECO:0000269|PubMed:14765195, ECO:0000269|PubMed:15879509, ECO:0000269|PubMed:16270630, ECO:0000269|PubMed:20978134, ECO:0000269|PubMed:22923610}.; DISEASE: Combined deficiency of vitamin K-dependent clotting factors 2 (VKCFD2) [MIM:607473]: VKCFD leads to a bleeding tendency that is usually reversed by oral administration of vitamin K. {ECO:0000269|PubMed:14765194}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Coumarin resistance (CMRES) [MIM:122700]: A condition characterized by partial or complete resistance to warfarin or other 4-hydroxycoumarin derivatives. These drugs are used as anti- coagulants for the prevention of thromboembolic diseases in subjects with deep vein thrombosis, atrial fibrillation, or mechanical heart valve replacement. {ECO:0000269|PubMed:14765194, ECO:0000269|PubMed:20946155}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed at highest levels in fetal and adult liver, followed by fetal heart, kidney, and lung, adult heart, and pancreas. {ECO:0000269|PubMed:14765194}.; lymphoreticular;medulla oblongata;smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;testis;germinal center;ciliary body;brain;pineal gland;bladder;unclassifiable (Anatomical System);trophoblast;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pineal body;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;amnion;alveolus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; adipose tissue;heart;thyroid;liver; 0.17686 . 0.191216164 66.57230479 5.70432 0.21368 VKORC1L1 0.851484218854318 0.146024920146589 0.00249086099909201 vitamin K epoxide reductase complex subunit 1 like 1 FUNCTION: Involved in vitamin K metabolism. Can reduce inactive vitamin K 2,3-epoxide to active vitamin K (in vitro), and may contribute to vitamin K-mediated protection against oxidative stress. Plays a role in vitamin K-dependent gamma-carboxylation of Glu residues in target proteins. {ECO:0000269|PubMed:21367861, ECO:0000269|PubMed:23928358, ECO:0000269|PubMed:24532791}.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;cochlea;cerebral cortex;thyroid;bone;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;stomach; adipose tissue; . 0.10920 0.013025609 54.62962963 1778.18585 7.78640 VKORC1P1 . . . VKORC1 pseudogene 1 . . . . . . . . . . . VKORC1P2 . . . VKORC1 pseudogene 2 . . . . . . . . . . . VLDLR 0.000865740605897974 0.999129165376707 5.09401739523737e-06 very low density lipoprotein receptor FUNCTION: Binds VLDL and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Binding to Reelin induces tyrosine phosphorylation of Dab1 and modulation of Tau phosphorylation (By similarity). {ECO:0000250}.; DISEASE: Cerebellar ataxia, mental retardation, and dysequilibrium syndrome 1 (CAMRQ1) [MIM:224050]: A congenital, non-progressive cerebellar ataxia associated with disturbed equilibrium, delayed ambulation, mental retardation, cerebellar hypoplasia and mild cerebral gyral simplification. Additional features include short stature, strabismus, pes planus and, rarely, seizures. {ECO:0000269|PubMed:16080122}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Abundant in heart and skeletal muscle; also ovary and kidney; not in liver.; . . 0.31476 0.49038 -1.058182374 7.554847841 521.78343 4.66353 VLDLR-AS1 . . . VLDLR antisense RNA 1 . . . . . . . . . . . VMA21 0.651805241659588 0.322927077882514 0.0252676804578978 VMA21 vacuolar H+-ATPase homolog (S. cerevisiae) FUNCTION: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum. {ECO:0000255|HAMAP-Rule:MF_03058, ECO:0000269|PubMed:19379691}.; DISEASE: Myopathy, X-linked, with excessive autophagy (MEAX) [MIM:310440]: A muscle disorder characterized by childhood early onset of a slowly progressive proximal limb muscle weakness (especially in legs) and elevation of serum creatine kinase, without evidence of cardiac, respiratory or central nervous system involvement. Histopathological analysis reveals diseased muscle fibers that are not necrotic, but show abnormal autophagic vacuolation as a manifestation of excessive autophagic activity in skeletal muscle cells. {ECO:0000269|PubMed:19379691, ECO:0000269|PubMed:23315026, ECO:0000269|PubMed:24488655, ECO:0000269|PubMed:25683699}. Note=The disease is caused by mutations affecting the gene represented in this entry. VMA21 deficiency results in an increase of lysosomal pH from 4.7 to 5.2, which reduces lysosomal degradative ability and blocks autophagy. This reduces cellular free amino acids, which upregulates the mTOR pathway and mTOR-dependent macroautophagy, resulting in proliferation of large and ineffective autolysosomes that engulf sections of cytoplasm, merge together, and vacuolate the cell. {ECO:0000269|PubMed:23315026}.; . smooth muscle;ovary;parathyroid;skin;retina;bone marrow;prostate;cerebral cortex;larynx;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lacrimal gland;blood;skeletal muscle;breast;lung;placenta;liver;duodenum;head and neck;cervix;kidney;mammary gland;stomach;thymus; . . . 0.169169615 65.33380514 428.23208 4.32186 VMAC 0.0234647088154216 0.542868193311712 0.433667097872866 vimentin-type intermediate filament associated coiled-coil protein . . . uterus;prostate;salivary gland;liver;skin; superior cervical ganglion;subthalamic nucleus;ciliary ganglion;atrioventricular node; . . . . 285.32189 3.61599 VMD1 . . . vitelliform macular dystrophy, atypical . . . . . . . . . . . VMO1 0.000437154088356555 0.418612917152543 0.580949928759101 vitelline membrane outer layer 1 homolog (chicken) . . . unclassifiable (Anatomical System);uterus;lung;synovium;pituitary gland;alveolus;cervix;choroid;kidney;brain; atrioventricular node; 0.06805 0.08547 0.43736446 77.56546355 619.62287 5.02238 VMP1 0.930655518495749 0.0693298568877327 1.46246165180867e-05 vacuole membrane protein 1 FUNCTION: Stress-induced protein that, when overexpressed, promotes formation of intracellular vacuoles followed by cell death. May be involved in the cytoplasmic vacuolization of acinar cells during the early stage of acute pancreatitis. Plays a role in the initial stages of the autophagic process through its interaction with BECN1 (By similarity). Involved in cell-cell adhesion. Plays an essential role in formation of cell junctions. {ECO:0000250, ECO:0000269|PubMed:17724469}.; . . smooth muscle;ovary;skin;retina;bone marrow;prostate;frontal lobe;endometrium;thyroid;iris;amniotic fluid;germinal center;brain;gall bladder;tonsil;heart;cartilage;tongue;pharynx;blood;skeletal muscle;breast;epididymis;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;vein;uterus;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; superior cervical ganglion;whole blood; 0.52497 0.11325 -0.405853867 26.23260203 21.96934 0.73893 VN1R1 0.310171245019823 0.617734381538362 0.0720943734418149 vomeronasal 1 receptor 1 FUNCTION: Putative pheromone receptor.; . TISSUE SPECIFICITY: Expressed in the olfactory mucosa, very low expression in brain, lung and kidney. {ECO:0000269|PubMed:10973240}.; unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.03298 . 0.238945317 69.20853975 763.76634 5.47658 VN1R2 0.000121565635123991 0.387622734768895 0.612255699595981 vomeronasal 1 receptor 2 FUNCTION: Putative pheromone receptor.; . . . . 0.03067 . 0.619191319 83.36282142 815.64192 5.61350 VN1R3 . . . vomeronasal 1 receptor 3 (gene/pseudogene) FUNCTION: Putative pheromone receptor.; . . . . . . . . . . VN1R4 0.261583302834637 0.638586786732916 0.0998299104324472 vomeronasal 1 receptor 4 FUNCTION: Putative pheromone receptor.; . . medulla oblongata; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.01977 . 0.661468037 84.4420854 136.57701 2.54017 VN1R5 . . . vomeronasal 1 receptor 5 (gene/pseudogene) FUNCTION: Putative pheromone receptor.; . . . . 0.04225 . . . . . VN1R6P . . . vomeronasal 1 receptor 6 pseudogene . . . . . 0.01977 . . . . . VN1R7P . . . vomeronasal 1 receptor 7 pseudogene . . . . . . . . . . . VN1R8P . . . vomeronasal 1 receptor 8 pseudogene . . . . . . . . . . . VN1R9P . . . vomeronasal 1 receptor 9 pseudogene . . . . . . . . . . . VN1R10P . . . vomeronasal 1 receptor 10 pseudogene . . . . . . . . . . . VN1R11P . . . vomeronasal 1 receptor 11 pseudogene . . . . . . . . . . . VN1R12P . . . vomeronasal 1 receptor 12 pseudogene . . . . . . . . . . . VN1R13P . . . vomeronasal 1 receptor 13 pseudogene . . . . . . . . . . . VN1R14P . . . vomeronasal 1 receptor 14 pseudogene . . . . . . . . . . . VN1R15P . . . vomeronasal 1 receptor 15 pseudogene . . . . . . . . . . . VN1R16P . . . vomeronasal 1 receptor 16 pseudogene . . . . . . . . . . . VN1R17P . . . vomeronasal 1 receptor 17 pseudogene FUNCTION: Putative pheromone receptor. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in olfactory nerve. {ECO:0000269|PubMed:12044878}.; . . . . . . . . VN1R18P . . . vomeronasal 1 receptor 18 pseudogene . . . . . . . . . . . VN1R19P . . . vomeronasal 1 receptor 19 pseudogene . . . . . . . . . . . VN1R20P . . . vomeronasal 1 receptor 20 pseudogene . . . . . . . . . . . VN1R21P . . . vomeronasal 1 receptor 21 pseudogene . . . . . . . . . . . VN1R22P . . . vomeronasal 1 receptor 22 pseudogene . . . . . . . . . . . VN1R23P . . . vomeronasal 1 receptor 23 pseudogene . . . . . . . . . . . VN1R24P . . . vomeronasal 1 receptor 24 pseudogene . . . . . . . . . . . VN1R25P . . . vomeronasal 1 receptor 25 pseudogene . . . . . . . . . . . VN1R26P . . . vomeronasal 1 receptor 26 pseudogene . . . . . . . . . . . VN1R27P . . . vomeronasal 1 receptor 27 pseudogene . . . . . . . . . . . VN1R28P . . . vomeronasal 1 receptor 28 pseudogene . . . . . . . . . . . VN1R29P . . . vomeronasal 1 receptor 29 pseudogene . . . . . . . . . . . VN1R30P . . . vomeronasal 1 receptor 30 pseudogene . . . . . . . . . . . VN1R31P . . . vomeronasal 1 receptor 31 pseudogene . . . . . . . . . . . VN1R32P . . . vomeronasal 1 receptor 32 pseudogene . . . . . . . . . . . VN1R33P . . . vomeronasal 1 receptor 33 pseudogene . . . . . . . . . . . VN1R34P . . . vomeronasal 1 receptor 34 pseudogene . . . . . . . . . . . VN1R35P . . . vomeronasal 1 receptor 35 pseudogene . . . . . . . . . . . VN1R36P . . . vomeronasal 1 receptor 36 pseudogene . . . . . . . . . . . VN1R37P . . . vomeronasal 1 receptor 37 pseudogene . . . . . . . . . . . VN1R38P . . . vomeronasal 1 receptor 38 pseudogene . . . . . . . . . . . VN1R39P . . . vomeronasal 1 receptor 39 pseudogene . . . . . . . . . . . VN1R40P . . . vomeronasal 1 receptor 40 pseudogene . . . . . . . . . . . VN1R41P . . . vomeronasal 1 receptor 41 pseudogene . . . . . . . . . . . VN1R42P . . . vomeronasal 1 receptor 42 pseudogene . . . . . . . . . . . VN1R43P . . . vomeronasal 1 receptor 43 pseudogene . . . . . . . . . . . VN1R44P . . . vomeronasal 1 receptor 44 pseudogene . . . . . . . . . . . VN1R45P . . . vomeronasal 1 receptor 45 pseudogene . . . . . . . . . . . VN1R46P . . . vomeronasal 1 receptor 46 pseudogene . . . . . . . . . . . VN1R47P . . . vomeronasal 1 receptor 47 pseudogene . . . . . . . . . . . VN1R48P . . . vomeronasal 1 receptor 48 pseudogene . . . . . . . . . . . VN1R49P . . . vomeronasal 1 receptor 49 pseudogene . . . . . . . . . . . VN1R51P . . . vomeronasal 1 receptor 51 pseudogene . . . . . . . . . . . VN1R52P . . . vomeronasal 1 receptor 52 pseudogene . . . . . . . . . . . VN1R53P . . . vomeronasal 1 receptor 53 pseudogene . . . . . . . . . . . VN1R54P . . . vomeronasal 1 receptor 54 pseudogene . . . . . . . . . . . VN1R55P . . . vomeronasal 1 receptor 55 pseudogene . . . . . . . . . . . VN1R56P . . . vomeronasal 1 receptor 56 pseudogene . . . . . . . . . . . VN1R57P . . . vomeronasal 1 receptor 57 pseudogene . . . . . . . . . . . VN1R58P . . . vomeronasal 1 receptor 58 pseudogene . . . . . . . . . . . VN1R59P . . . vomeronasal 1 receptor 59 pseudogene . . . . . . . . . . . VN1R60P . . . vomeronasal 1 receptor 60 pseudogene . . . . . . . . . . . VN1R61P . . . vomeronasal 1 receptor 61 pseudogene . . . . . . . . . . . VN1R62P . . . vomeronasal 1 receptor 62 pseudogene . . . . . . . . . . . VN1R63P . . . vomeronasal 1 receptor 63 pseudogene . . . . . . . . . . . VN1R64P . . . vomeronasal 1 receptor 64 pseudogene . . . . . . . . . . . VN1R65P . . . vomeronasal 1 receptor 65 pseudogene . . . . . . . . . . . VN1R66P . . . vomeronasal 1 receptor 66 pseudogene . . . . . . . . . . . VN1R67P . . . vomeronasal 1 receptor 67 pseudogene . . . . . . . . . . . VN1R68P . . . vomeronasal 1 receptor 68 pseudogene . . . . . . . . . . . VN1R69P . . . vomeronasal 1 receptor 69 pseudogene . . . . . . . . . . . VN1R70P . . . vomeronasal 1 receptor 70 pseudogene . . . . . . . . . . . VN1R71P . . . vomeronasal 1 receptor 71 pseudogene . . . . . . . . . . . VN1R72P . . . vomeronasal 1 receptor 72 pseudogene . . . . . . . . . . . VN1R73P . . . vomeronasal 1 receptor 73 pseudogene . . . . . . . . . . . VN1R74P . . . vomeronasal 1 receptor 74 pseudogene . . . . . . . . . . . VN1R75P . . . vomeronasal 1 receptor 75 pseudogene . . . . . . . . . . . VN1R76P . . . vomeronasal 1 receptor 76 pseudogene . . . . . . . . . . . VN1R77P . . . vomeronasal 1 receptor 77 pseudogene . . . . . . . . . . . VN1R78P . . . vomeronasal 1 receptor 78 pseudogene . . . . . . . . . . . VN1R79P . . . vomeronasal 1 receptor 79 pseudogene . . . . . . . . . . . VN1R80P . . . vomeronasal 1 receptor 80 pseudogene . . . . . . . . . . . VN1R81P . . . vomeronasal 1 receptor 81 pseudogene . . . . . . . . . . . VN1R82P . . . vomeronasal 1 receptor 82 pseudogene . . . . . . . . . . . VN1R83P . . . vomeronasal 1 receptor 83 pseudogene . . . . . . . . . . . VN1R84P . . . vomeronasal 1 receptor 84 pseudogene . . . . . . . . . . . VN1R85P . . . vomeronasal 1 receptor 85 pseudogene . . . . . . . . . . . VN1R86P . . . vomeronasal 1 receptor 86 pseudogene . . . . . . . . . . . VN1R87P . . . vomeronasal 1 receptor 87 pseudogene . . . . . . . . . . . VN1R88P . . . vomeronasal 1 receptor 88 pseudogene . . . . . . . . . . . VN1R89P . . . vomeronasal 1 receptor 89 pseudogene . . . . . . . . . . . VN1R90P . . . vomeronasal 1 receptor 90 pseudogene . . . . . . . . . . . VN1R91P . . . vomeronasal 1 receptor 91 pseudogene . . . . . . . . . . . VN1R92P . . . vomeronasal 1 receptor 92 pseudogene . . . . . . . . . . . VN1R93P . . . vomeronasal 1 receptor 93 pseudogene . . . . . . . . . . . VN1R94P . . . vomeronasal 1 receptor 94 pseudogene . . . . . . . . . . . VN1R95P . . . vomeronasal 1 receptor 95 pseudogene . . . . . . . . . . . VN1R96P . . . vomeronasal 1 receptor 96 pseudogene . . . . . . . . . . . VN1R97P . . . vomeronasal 1 receptor 97 pseudogene . . . . . . . . . . . VN1R98P . . . vomeronasal 1 receptor 98 pseudogene . . . . . . . . . . . VN1R99P . . . vomeronasal 1 receptor 99 pseudogene . . . . . . . . . . . VN1R100P . . . vomeronasal 1 receptor 100 pseudogene . . . . . . . . . . . VN1R101P . . . vomeronasal 1 receptor 101 pseudogene . . . . . . . . . . . VN1R102P . . . vomeronasal 1 receptor 102 pseudogene . . . . . . . . . . . VN1R103P . . . vomeronasal 1 receptor 103 pseudogene . . . . . . . . . . . VN1R104P . . . vomeronasal 1 receptor 104 pseudogene . . . . . . . . . . . VN1R105P . . . vomeronasal 1 receptor 105 pseudogene . . . . . . . . . . . VN1R106P . . . vomeronasal 1 receptor 106 pseudogene . . . . . . . . . . . VN1R107P . . . vomeronasal 1 receptor 107 pseudogene . . . . . . . . . . . VN1R108P . . . vomeronasal 1 receptor 108 pseudogene . . . . . . . . . . . VN1R109P . . . vomeronasal 1 receptor 109 pseudogene . . . . . . . . . . . VN1R110P . . . vomeronasal 1 receptor 110 pseudogene . . . . . . . . . . . VN1R111P . . . vomeronasal 1 receptor 111 pseudogene . . . . . . . . . . . VN1R112P . . . vomeronasal 1 receptor 112 pseudogene . . . . . . . . . . . VN2R1P . . . vomeronasal 2 receptor 1 pseudogene . . . . . 0.11146 . . . . . VN2R2P . . . vomeronasal 2 receptor 2 pseudogene . . . . . . . . . . . VN2R3P . . . vomeronasal 2 receptor 3 pseudogene . . . . . . . . . . . VN2R6P . . . vomeronasal 2 receptor 6 pseudogene . . . . . . . . . . . VN2R7P . . . vomeronasal 2 receptor 7 pseudogene . . . . . . . . . . . VN2R9P . . . vomeronasal 2 receptor 9 pseudogene . . . . . . . . . . . VN2R10P . . . vomeronasal 2 receptor 10 pseudogene . . . . . . . . . . . VN2R11P . . . vomeronasal 2 receptor 11 pseudogene . . . . . . . . . . . VN2R12P . . . vomeronasal 2 receptor 12 pseudogene . . . . . . . . . . . VN2R13P . . . vomeronasal 2 receptor 13 pseudogene . . . . . . . . . . . VN2R14P . . . vomeronasal 2 receptor 14 pseudogene . . . . . . . . . . . VN2R15P . . . vomeronasal 2 receptor 15 pseudogene . . . . . . . . . . . VN2R16P . . . vomeronasal 2 receptor 16 pseudogene . . . . . . . . . . . VN2R17P . . . vomeronasal 2 receptor 17 pseudogene . . . . . . . . . . . VN2R18P . . . vomeronasal 2 receptor 18 pseudogene . . . . . . . . . . . VN2R19P . . . vomeronasal 2 receptor 19 pseudogene . . . . . . . . . . . VN2R20P . . . vomeronasal 2 receptor 20 pseudogene . . . . . . . . . . . VN2R21P . . . vomeronasal 2 receptor 21 pseudogene . . . . . . . . . . . VNN1 2.35465646726636e-07 0.277446440641124 0.722553323893229 vanin 1 FUNCTION: Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine. {ECO:0000269|PubMed:10567687, ECO:0000269|PubMed:11491533}.; . TISSUE SPECIFICITY: Widely expressed with higher expression in spleen, kidney and blood. Overexpressed in lesional psoriatic skin. {ECO:0000269|PubMed:19322213}.; . . 0.28712 0.17990 1.467941683 95.26421326 2457.74895 9.22666 VNN2 1.01889678992448e-08 0.171192684779139 0.828807305031894 vanin 2 FUNCTION: Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine. Involved in the thymus homing of bone marrow cells. May regulate beta-2 integrin-mediated cell adhesion, migration and motility of neutrophil. {ECO:0000269|PubMed:11491533}.; . TISSUE SPECIFICITY: Widely expressed with higher expression in spleen and blood. {ECO:0000269|PubMed:19322213}.; unclassifiable (Anatomical System);uterus;lymph node;lung;placenta;sympathetic chain;blood;kidney;germinal center;skeletal muscle;tonsil;bone marrow; white blood cells;whole blood;tonsil;bone marrow; 0.27068 0.10706 1.332002318 94.20853975 139.33156 2.57418 VNN3 0.0347314452513382 0.826254744711966 0.139013810036696 vanin 3 FUNCTION: Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine. {ECO:0000269|PubMed:11491533}.; . TISSUE SPECIFICITY: Widely expressed with higher expression in liver and blood. Expressed in differentiated keratinocytes in epidermis and in epithelial cells in dermis. Overexpressed in lesional psoriatic skin. {ECO:0000269|PubMed:11491533, ECO:0000269|PubMed:19322213}.; unclassifiable (Anatomical System);whole body;endometrium;nasopharynx;liver;spleen; superior cervical ganglion;trigeminal ganglion; 0.05966 . . . 4724.69354 13.89322 VOPP1 0.12531564122422 0.780070095979799 0.0946142627959809 vesicular, overexpressed in cancer, prosurvival protein 1 FUNCTION: Increases the transcriptional activity of NFKB1 by facilitating its nuclear translocation, DNA-binding and associated apoptotic response, when overexpressed. {ECO:0000269|PubMed:15735698}.; . TISSUE SPECIFICITY: Widely expressed with highest levels in thymus and ovary. {ECO:0000269|PubMed:11916499}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;tonsil;heart;cartilage;blood;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;thymus; thalamus;cingulate cortex; . . 0.058937498 58.26256192 27.40078 0.88373 VPRBP . . . Vpr (HIV-1) binding protein FUNCTION: Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1- CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1- DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2. Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex (PubMed:23063525). The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: VPRBP is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination. Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition (PubMed:23362280). Also acts as an atypical serine/threonine- protein kinase that specifically mediates phosphorylation of 'Thr- 120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription. H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors (PubMed:24140421). Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 (PubMed:20644714). In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1- DCAF1/VPRBP function leading to arrest the cell cycle in G2 phase, and also to protect the viral protein from proteasomal degradation by another E3 ubiquitin ligase. The HIV-1 Vpr protein hijacks the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to promote ubiquitination and degradation of proteins such as TERT and ZIP/ZGPAT. In case of infection by HIV-2 virus, it is recruited by HIV-2 Vpx in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage. {ECO:0000269|PubMed:16964240, ECO:0000269|PubMed:17314515, ECO:0000269|PubMed:17559673, ECO:0000269|PubMed:17609381, ECO:0000269|PubMed:17620334, ECO:0000269|PubMed:17626091, ECO:0000269|PubMed:17630831, ECO:0000269|PubMed:18332868, ECO:0000269|PubMed:18464893, ECO:0000269|PubMed:18524771, ECO:0000269|PubMed:18606781, ECO:0000269|PubMed:19264781, ECO:0000269|PubMed:19287380, ECO:0000269|PubMed:19923175, ECO:0000269|PubMed:20644714, ECO:0000269|PubMed:22184063, ECO:0000269|PubMed:23063525, ECO:0000269|PubMed:23362280, ECO:0000269|PubMed:24116224, ECO:0000269|PubMed:24140421, ECO:0000269|PubMed:24336198}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11223251}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.08318 0.09605 . . 20.55289 0.69858 VPREB1 0.00134358993682976 0.420315219377041 0.578341190686129 pre-B lymphocyte 1 FUNCTION: Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B-cell differentiation.; . TISSUE SPECIFICITY: Only expressed by pre-B-cells.; umbilical cord;testis;blood; ciliary ganglion;trigeminal ganglion; 0.02303 0.26716 0.68351529 85.03774475 33.59357 1.03719 VPREB3 0.0161485671370314 0.702597585555272 0.281253847307696 pre-B lymphocyte 3 FUNCTION: Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells.; . . unclassifiable (Anatomical System);prostate;pancreas;lung;nasopharynx;testis;spleen;blood;head and neck;germinal center;tonsil; trigeminal ganglion; 0.17590 0.18222 0.637604436 83.77565464 50.70435 1.40261 VPS4A 0.912320744087044 0.0876526138403263 2.66420726301455e-05 vacuolar protein sorting 4 homolog A (S. cerevisiae) FUNCTION: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). Involved in cytokinesis: retained at the midbody by ZFYVE19/ANCHR and CHMP4C until abscission checkpoint signaling is terminated at late cytokinesis. It is then released following dephosphorylation of CHMP4C, leading to abscission (PubMed:24814515). {ECO:0000269|PubMed:11563910, ECO:0000269|PubMed:11595185, ECO:0000269|PubMed:15075231, ECO:0000269|PubMed:24814515}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10637304, ECO:0000269|PubMed:11563910}.; myocardium;lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;cornea;placenta;duodenum;amnion;head and neck;kidney;stomach; whole brain;amygdala;occipital lobe;thalamus;cerebellum peduncles;temporal lobe;pons;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;cerebellum; 0.55193 0.22384 -0.846787714 11.05803255 35.42142 1.06917 VPS4B 0.21387385685724 0.785755819070213 0.00037032407254683 vacuolar protein sorting 4 homolog B (S. cerevisiae) FUNCTION: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). {ECO:0000269|PubMed:11563910, ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:18687924}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11563910}.; ovary;developmental;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;oesophagus;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;oral cavity;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;mesenchyma;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;superior cervical ganglion;hypothalamus;atrioventricular node;whole blood;trigeminal ganglion; 0.44334 0.15645 0.21689899 68.12927577 37.23293 1.11026 VPS8 3.61819753295781e-06 0.999996197171693 1.84630773757513e-07 VPS8, CORVET complex subunit FUNCTION: Plays a role in vesicle-mediated protein trafficking of the endocytic membrane transport pathway. Believed to act as a component of the putative CORVET endosomal tethering complexes which is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:25266290). Functions predominantly in APPL1-containing endosomes (PubMed:25266290). {ECO:0000269|PubMed:25266290, ECO:0000305|PubMed:25266290}.; . . medulla oblongata;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;peripheral nerve; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cingulate cortex; 0.13365 0.11078 -0.365622677 28.30856334 3238.91039 10.83959 VPS9D1 0.00176648362917067 0.992920971125487 0.00531254524534188 VPS9 domain containing 1 . . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10231027}.; . . 0.05029 . -0.178111357 40.44585987 202.7909 3.07473 VPS9D1-AS1 . . . VPS9D1 antisense RNA 1 . . . . . . . . . . . VPS11 0.223659481916243 0.776337724240419 2.79384333781636e-06 VPS11, CORVET/HOPS core subunit FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:11382755, PubMed:23351085, PubMed:24554770, PubMed:25266290, PubMed:25783203). Required for fusion of endosomes and autophagosomes with lysosomes (PubMed:25783203). Involved in cargo transport from early to late endosomes and required for the transition from early to late endosomes (PubMed:21148287). Involved in the retrograde Shiga toxin transport (PubMed:23593995). {ECO:0000269|PubMed:21148287, ECO:0000269|PubMed:23593995, ECO:0000269|PubMed:25783203, ECO:0000305|PubMed:11382755, ECO:0000305|PubMed:23351085, ECO:0000305|PubMed:24554770, ECO:0000305|PubMed:25266290, ECO:0000305|PubMed:25783203}.; . TISSUE SPECIFICITY: Ubiquitous. Expression was highest in heart and low in lung.; ovary;umbilical cord;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;kidney; superior cervical ganglion;subthalamic nucleus;trigeminal ganglion;cerebellum; 0.29182 0.22141 . . 2913.34312 10.23918 VPS13A 0.00423831123659198 0.995761688763408 8.25276045649454e-19 vacuolar protein sorting 13 homolog A (S. cerevisiae) FUNCTION: May play a role in the control of protein cycling through the trans-Golgi network to early and late endosomes, lysosomes and plasma membrane.; . TISSUE SPECIFICITY: Widely expressed. Higher expression is found in brain, heart, skeletal muscle and kidney.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; amygdala;subthalamic nucleus;medulla oblongata;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.15331 0.23245 -1.852743422 2.03467799 741.38784 5.40739 VPS13A-AS1 . . . VPS13A antisense RNA 1 . . . . . . . . . . . VPS13B 9.81062330211603e-27 0.999999996277658 3.72234215480585e-09 vacuolar protein sorting 13 homolog B (yeast) FUNCTION: May be involved in protein sorting in post Golgi membrane traffic. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. There is apparent differential expression of different transcripts. In fetal brain, lung, liver, and kidney, two transcripts of 2 and 5 kb are identified. These transcripts are also seen in all adult tissues analyzed. A larger transcript (12-14 kb) is expressed in prostate, testis, ovary, and colon in the adult. Expression is very low in adult brain tissue. Isoform 1 and isoform 2 are expressed in brain and retina. Isoform 2 is expressed ubiquitously. {ECO:0000269|PubMed:12730828, ECO:0000269|PubMed:19006247}.; ovary;colon;parathyroid;skin;bone marrow;uterus;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;blood;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;hypopharynx;duodenum;liver;head and neck;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.28405 0.17647 -0.610811433 17.50412833 5683.91051 15.59736 VPS13C 1.8552278256612e-37 0.999996998905964 3.00109403607531e-06 vacuolar protein sorting 13 homolog C (S. cerevisiae) . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15498460}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;islets of Langerhans;oral cavity;spinal cord;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;nose;aorta;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;testis - interstitial;medulla oblongata;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.21113 0.10840 -0.811192082 12.07832036 3785.30625 12.05677 VPS13D 0.999992132395372 7.86760462799904e-06 2.94520427506627e-33 vacuolar protein sorting 13 homolog D (S. cerevisiae) . . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15498460}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;atrium;whole body;frontal lobe;oesophagus;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;cartilage;heart;nervous;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; amygdala;subthalamic nucleus;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.27558 0.11399 -4.233186317 0.135645199 2635.30524 9.63353 VPS16 2.29458119355575e-05 0.999938687991656 3.83661964090112e-05 VPS16, CORVET/HOPS core subunit FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:11382755, PubMed:23351085, PubMed:24554770, PubMed:25266290, PubMed:25783203). Required for recruitment of VPS33A to the HOPS complex (PubMed:23901104). Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS33A but not VPS33B (PubMed:25783203). The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG (PubMed:24554770). {ECO:0000269|PubMed:23901104, ECO:0000269|PubMed:24554770, ECO:0000269|PubMed:25783203, ECO:0000305|PubMed:11382755, ECO:0000305|PubMed:23351085, ECO:0000305|PubMed:25266290, ECO:0000305|PubMed:25783203}.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.30311 0.11121 -0.903841325 10.14390186 179.40567 2.90934 VPS18 0.939243017183049 0.0607565543667078 4.28450243248408e-07 VPS18, CORVET/HOPS core subunit FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:11382755, PubMed:23351085, PubMed:24554770, PubMed:25783203). Required for fusion of endosomes and autophagosomes with lysosomes (PubMed:25783203). Involved in dendrite development of Pukinje cells (By similarity). {ECO:0000250|UniProtKB:Q8R307, ECO:0000269|PubMed:25783203, ECO:0000305|PubMed:11382755, ECO:0000305|PubMed:23351085, ECO:0000305|PubMed:25783203}.; . TISSUE SPECIFICITY: Ubiquitous. Expression was highest in heart and low in lung. {ECO:0000269|PubMed:11382755}.; lymphoreticular;ovary;sympathetic chain;colon;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;iris;testis;brain;pineal gland;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;visual apparatus;liver;amnion;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.27175 0.14094 -1.456898556 3.862939372 217.40248 3.18798 VPS25 0.735077728420435 0.264387472368686 0.000534799210879843 vacuolar protein sorting 25 homolog (S. cerevisiae) FUNCTION: Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. The ESCRT-II complex may be involved in facilitating the budding of certain RNA viruses. {ECO:0000269|PubMed:18723511}.; . TISSUE SPECIFICITY: Expressed at the mRNA level in kidney, liver, pancreas, and placenta. Lower levels of expression are found in heart, skeletal muscle, brain and lung. {ECO:0000269|PubMed:16889659}.; myocardium;lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;skeletal muscle;greater omentum;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;hypopharynx;amnion;head and neck;kidney;stomach;aorta; kidney; 0.54376 0.13588 0.080983847 59.76055674 65.61924 1.66853 VPS25P1 . . . VPS25 pseudogene 1 . . . . . . . . . . . VPS26A 0.661577283638167 0.337296752293971 0.00112596406786183 VPS26 retromer complex component A FUNCTION: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins (Probable). The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (Probable). Required for retrograde transport of lysosomal enzyme receptor IGF2R (PubMed:15078902, PubMed:15078903). Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA) (PubMed:15247922). Required for the endosomal localization of FAM21A (indicative for the WASH complex) (PubMed:22070227). Required for the endosomal localization of TBC1D5 (PubMed:20923837). Mediates retromer cargo reognition of SORL1 and is involved in trafficking of SORL1 implicated in sorting and processing of APP (PubMed:22279231). Involved in retromer- independent lysosomal sorting of F2R (PubMed:16407403). Involved in recycling of ADRB2 (PubMed:21602791). Enhances the affinity of SNX27 for PDZ-binding motifs in cargo proteins (By similarity). {ECO:0000250|UniProtKB:P40336, ECO:0000269|PubMed:15078902, ECO:0000269|PubMed:15078903, ECO:0000269|PubMed:15247922, ECO:0000269|PubMed:16407403, ECO:0000269|PubMed:22070227, ECO:0000269|PubMed:22279231, ECO:0000303|PubMed:20923837, ECO:0000303|PubMed:21602791, ECO:0000303|PubMed:21725319, ECO:0000303|PubMed:23563491, ECO:0000305}.; . . myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; superior cervical ganglion;testis - interstitial;prefrontal cortex;testis; 0.14635 0.13588 -0.251530012 35.42108988 13.42094 0.48833 VPS26AP1 . . . VPS26A pseudogene 1 . . . . . . . . . . . VPS26B 0.970719437677481 0.0292395131032277 4.10492192908573e-05 VPS26 retromer complex component B FUNCTION: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. May be involved in retrograde transport of SORT1 but not of IGF2R. Acts redundantly with VSP26A in SNX-27 mediated endocytic recycling of SLC2A1/GLUT1 (By similarity). {ECO:0000250|UniProtKB:O75436, ECO:0000250|UniProtKB:Q8C0E2}.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;brain;unclassifiable (Anatomical System);cartilage;muscle;lens;lung;placenta;macula lutea;hippocampus;visual apparatus;spleen;head and neck;kidney;stomach;thymus; superior cervical ganglion;subthalamic nucleus;tongue;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.13972 0.11688 -0.516085732 21.20193442 8.48894 0.31181 VPS26BP1 . . . VPS26B pseudogene 1 . . . . . . . . . . . VPS28 0.115974874224198 0.857110730916056 0.026914394859746 VPS28, ESCRT-I subunit FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. {ECO:0000269|PubMed:11916981}.; . . medulla oblongata;smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach;aorta; testis; 0.20134 0.12970 -0.404032746 26.53338051 18.89106 0.65215 VPS29 0.934744447933042 0.0649527362799688 0.000302815786988969 VPS29, retromer complex component FUNCTION: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA) (Probable). Involved in GLUT1 endosome-to-plasma membrane trafficking; the function is dependent of association with ANKRD27 (PubMed:24856514). {ECO:0000250|UniProtKB:Q9QZ88, ECO:0000269|PubMed:16737443, ECO:0000269|PubMed:24856514, ECO:0000303|PubMed:15247922, ECO:0000303|PubMed:21725319, ECO:0000303|PubMed:23563491}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, lung, placenta, spleen, peripheral blood leukocytes, thymus, colon skeletal muscle, kidney and brain.; ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;iris;bladder;brain;ciliary body;heart;cartilage;spinal cord;blood;lens;epididymis;trabecular meshwork;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;fovea centralis;vein;uterus;whole body;bone;pituitary gland;testis;dura mater;artery;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;bile duct;pancreas;lung;pia mater;nasopharynx;placenta;kidney;aorta;stomach; . 0.45412 0.10309 0.079165051 59.43029016 5.00308 0.18601 VPS33A 0.687968695146875 0.312024009998462 7.2948546630377e-06 VPS33A, CORVET/HOPS core subunit FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:23351085, PubMed:24554770, PubMed:25266290, PubMed:25783203). Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS16 but not VIPAS39 (PubMed:25783203). The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG (PubMed:24554770). {ECO:0000269|PubMed:24554770, ECO:0000269|PubMed:25783203, ECO:0000305|PubMed:23351085, ECO:0000305|PubMed:25266290, ECO:0000305|PubMed:25783203}.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;breast;lung;placenta;visual apparatus;hippocampus;liver;hypopharynx;head and neck;cervix;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.30575 0.16306 0.042348793 57.31304553 548.4855 4.76278 VPS33B 2.91337145537518e-09 0.994947079426248 0.00505291766038016 VPS33B, late endosome and lysosome associated FUNCTION: May play a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes. Mediates phagolysosomal fusion in macrophages (PubMed:18474358). Proposed to be involved in endosomal maturation implicating VIPAS39. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical recycling pathway and in the maintenance of the apical-basolateral polarity (PubMed:20190753). Seems to be involved in the sorting of specific cargos from the trans-Golgi network to alpha-granule-destined multivesicular bodies (MVBs) promoting MVBs maturation in megakaryocytes (By similarity). {ECO:0000250|UniProtKB:P59016, ECO:0000269|PubMed:18474358, ECO:0000305|PubMed:20190753, ECO:0000305|PubMed:23918659}.; DISEASE: Arthrogryposis, renal dysfunction and cholestasis syndrome 1 (ARCS1) [MIM:208085]: A multisystem disorder, characterized by neurogenic arthrogryposis multiplex congenita, renal tubular dysfunction and neonatal cholestasis with bile duct hypoplasia and low gamma glutamyl transpeptidase activity. Platelet dysfunction is common. {ECO:0000269|PubMed:15052268, ECO:0000269|PubMed:18853461}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous; highly expressed in testis and low expression in the lung.; colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;blood;lens;bile duct;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;hypothalamus;ciliary ganglion;skeletal muscle; 0.05914 0.11846 -0.530852121 20.82448691 75.02771 1.81240 VPS35 0.993599132125856 0.00640086622920252 1.64494137462188e-09 VPS35, retromer complex component FUNCTION: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The CSC seems to associate with the cytoplasmic domain of cargo proteins predominantly via VPS35; however, these interactions seem to be of low affinity and retromer SNX proteins may also contribute to cargo selectivity thus questioning the classical function of the CSC. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (Probable). Required for retrograde transport of lysosomal enzyme receptor IGF2R and SLC11A2. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA) (PubMed:15078903, PubMed:15247922, PubMed:20164305). Required for endosomal localization of FAM21C (PubMed:22070227). Mediates the association of the CSC with the WASH complex via FAM21 (PubMed:22070227, PubMed:24980502, PubMed:24819384). Required for the endosomal localization of TBC1D5 (PubMed:20923837). {ECO:0000269|PubMed:15078903, ECO:0000269|PubMed:15247922, ECO:0000269|PubMed:20164305, ECO:0000269|PubMed:20923837, ECO:0000269|PubMed:22070227, ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:24819384, ECO:0000269|PubMed:24980502, ECO:0000303|PubMed:21725319, ECO:0000303|PubMed:22070227, ECO:0000303|PubMed:22513087, ECO:0000303|PubMed:23563491}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, brain, placenta, skeletal muscle, spleen, thymus, testis, ovary, small intestine, kidney and colon.; ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;aorta; dorsal root ganglion;amygdala;medulla oblongata;occipital lobe;thalamus;hypothalamus;pons;subthalamic nucleus;testis;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex; 0.51899 0.20347 -0.690637458 15.12149092 51.7246 1.42013 VPS35P1 . . . VPS35, retromer complex component pseudogene 1 . . . . . . . . . . . VPS36 0.100608360734491 0.899084405848101 0.000307233417407662 vacuolar protein sorting 36 homolog (S. cerevisiae) FUNCTION: Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. Its ability to bind ubiquitin probably plays a role in endosomal sorting of ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3.; . . . . 0.09703 0.11990 -0.295622497 32.61972163 29.0318 0.92832 VPS37A 0.534958339986742 0.464368215307223 0.000673444706035035 VPS37A, ESCRT-I subunit FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation. {ECO:0000269|PubMed:15240819}.; . TISSUE SPECIFICITY: Widely expressed. Examined tissues include heart, brain, placenta, liver, skeletal muscle, kidney and pancreas. More abundant in liver. Strongly decreased or undetected in hepatomas. {ECO:0000269|PubMed:14623289, ECO:0000269|PubMed:22717650}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;testis;germinal center;brain;pineal gland;artery;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;hippocampus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;atrioventricular node; 0.13029 . -0.53631094 20.53550366 56.5864 1.51288 VPS37B 0.67680963728232 0.318506527620735 0.00468383509694497 VPS37B, ESCRT-I subunit FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation. {ECO:0000269|PubMed:15218037}.; . TISSUE SPECIFICITY: Widely expressed. Expressed in macrophages and lymphocytes. {ECO:0000269|PubMed:15218037}.; medulla oblongata;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;iris;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;cerebellum; amygdala;testis - seminiferous tubule;thyroid;adrenal cortex;white blood cells;whole blood; 0.13927 0.10305 -0.404032746 26.53338051 29.22607 0.93493 VPS37C 0.197171487861635 0.756959866637442 0.0458686455009237 VPS37C, ESCRT-I subunit FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation. {ECO:0000269|PubMed:15509564}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;iris;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;adrenal cortex;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;stomach;thymus; superior cervical ganglion; 0.13245 0.09998 0.92967242 89.79122435 237.56731 3.32808 VPS37D 0.656347210550458 0.319312414054316 0.0243403753952253 VPS37D, ESCRT-I subunit FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation.; DISEASE: Note=VPS37D is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region.; . unclassifiable (Anatomical System);lymph node;fovea centralis;choroid;lens;retina;uterus;optic nerve;lung;endometrium;macula lutea;testis;kidney;brain;stomach; . 0.17277 0.11262 . . 27.34929 0.88128 VPS39 0.000738264521045905 0.999255330486918 6.40499203608465e-06 VPS39, HOPS complex subunit FUNCTION: Regulator of TGF-beta/activin signaling, inhibiting SMAD3- and activating SMAD2-dependent transcription. Acts by interfering with SMAD3/SMAD4 complex formation, this would lead to inhibition of SMAD3-dependent transcription and relieve SMAD3 inhibition of SMAD2-dependent promoters, thus increasing SMAD2- dependent transcription. Does not affect TGF-beta-induced SMAD2 or SMAD3 phosphorylation, nor SMAD2/SMAD4 complex formation. {ECO:0000269|PubMed:12941698}.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in heart, skeletal muscle, kidney, pancreas, brain, placenta and spleen. {ECO:0000269|PubMed:11448994, ECO:0000269|PubMed:12941698}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;blood;lens;skeletal muscle;breast;epididymis;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;oesophagus;cerebral cortex;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;thymus; . 0.28009 0.11485 -0.843147538 11.2762444 145.43345 2.62591 VPS41 1.16349819146267e-08 0.999858285615403 0.000141702749615159 VPS41, HOPS complex subunit FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act in part as a core component of the putative HOPS endosomal tethering complexe is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE- mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes (PubMed:23351085). Involved in homotypic vesicle fusions between late endosomes and in heterotypic fusions between late endosomes and lysosomes implicated in degradation of endocytosed cargo (PubMed:9159129, PubMed:23167963, PubMed:25445562, PubMed:25908847). Required for fusion of autophagosomes with lysosomes (PubMed:25783203). May link the HOPS complex to endosomal Rab7 via its association with RILP and to lysosomal membranes via its association with ARL8B, suggesting that these interactions may bring the compartments to close proximity for fusion (PubMed:25445562, PubMed:25908847). Involved in the direct trans-Golgi network to late endosomes transport of lysosomal membrane proteins independently of HOPS (PubMed:23322049). Involved in sorting to the regulated secretory pathway presumably implicating the AP-3 adaptor complex (By similarity). May play a role in HOPS-independent function in the regulated secretory pathway (PubMed:24210660). {ECO:0000250|UniProtKB:D3ZVH6, ECO:0000269|PubMed:23167963, ECO:0000269|PubMed:23322049, ECO:0000269|PubMed:25445562, ECO:0000269|PubMed:25783203, ECO:0000269|PubMed:25908847, ECO:0000269|PubMed:9159129, ECO:0000305|PubMed:23167963, ECO:0000305|PubMed:23351085, ECO:0000305|PubMed:24210660, ECO:0000305|PubMed:25445562}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;islets of Langerhans;pineal body;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;stomach;aorta;peripheral nerve;thymus; amygdala;dorsal root ganglion;medulla oblongata;thalamus;occipital lobe;superior cervical ganglion;hypothalamus;pons;caudate nucleus;atrioventricular node;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;trigeminal ganglion;cingulate cortex;parietal lobe; 0.38776 0.11949 -0.33061537 30.82094834 311.5209 3.75608 VPS45 0.00030556962283822 0.999139444495782 0.000554985881379566 vacuolar protein sorting 45 homolog (S. cerevisiae) FUNCTION: May play a role in vesicle-mediated protein trafficking from the Golgi stack through the trans-Golgi network.; . TISSUE SPECIFICITY: Ubiquitous. Expression was highest in testis, heart and brain, intermediate in kidney, spleen, prostate, ovary, small intestine and thymus and low in lung, skeletal muscle, placenta, colon, pancreas, peripheral blood leukocytes and liver.; . . 0.15317 0.11807 -0.53631094 20.53550366 340.4292 3.91449 VPS50 . . . VPS50, EARP/GARPII complex subunit FUNCTION: Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4- positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane. Within the EARP complex, required to tether the complex to recycling endosomes. Not involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). {ECO:0000269|PubMed:25799061}.; . TISSUE SPECIFICITY: Ubiquitous, with higher expression in brain and skeletal muscle. {ECO:0000269|PubMed:21472204}.; . . 0.22153 . -0.176292081 40.56381222 . . VPS51 6.38019616804219e-05 0.900255142506543 0.0996810555317762 VPS51, GARP complex subunit FUNCTION: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of protein retrieval from endosomes to the TGN, acid hydrolase sorting, lysosome function, endosomal cholesterol traffic and autophagy. VPS51 participates in retrograde transport of acid hydrolase receptors, likely by promoting tethering and SNARE-dependent fusion of endosome-derived carriers to the TGN (PubMed:20685960). Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane (PubMed:25799061). {ECO:0000269|PubMed:20685960, ECO:0000269|PubMed:25799061}.; . . . . 0.42764 0.18311 -0.644723694 16.52512385 62.80737 1.62215 VPS52 0.0159632630188721 0.98403491141756 1.82556356774181e-06 VPS52, GARP complex subunit FUNCTION: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD (PubMed:15878329, PubMed:18367545). Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane (PubMed:25799061). {ECO:0000269|PubMed:15878329, ECO:0000269|PubMed:18367545, ECO:0000269|PubMed:25799061}.; . . . . 0.29955 . -0.512444034 21.55579146 64.18008 1.64252 VPS53 4.99655044931933e-05 0.999643703146724 0.000306331348782555 VPS53, GARP complex subunit FUNCTION: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD (PubMed:15878329, PubMed:18367545). Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane (PubMed:25799061). {ECO:0000269|PubMed:15878329, ECO:0000269|PubMed:18367545, ECO:0000269|PubMed:25799061}.; DISEASE: Pontocerebellar hypoplasia 2E (PCH2E) [MIM:615851]: A neurodegenerative disorder characterized by progressive cerebello- cerebral atrophy, profound mental retardation, progressive microcephaly, spasticity, and early-onset epilepsy. {ECO:0000269|PubMed:24577744}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;fovea centralis;choroid;lens;skeletal muscle;retina;bone marrow;uterus;optic nerve;lung;frontal lobe;placenta;thyroid;macula lutea;testis;head and neck;germinal center;brain;stomach; uterus corpus;superior cervical ganglion;skeletal muscle;skin; 0.30458 . -1.216154 5.667610285 1725.34458 7.66409 VPS54 0.949816739802316 0.0501832493622887 1.08353951791407e-08 VPS54, GARP complex subunit FUNCTION: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD (PubMed:18367545). Within the GARP complex, required to tether the complex to the TGN. Not involved in endocytic recycling (PubMed:25799061). {ECO:0000269|PubMed:18367545, ECO:0000269|PubMed:25799061}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;head and neck;kidney;aorta;stomach; ciliary ganglion; 0.25690 0.10808 -0.907472583 10.07313046 1770.06397 7.77175 VPS72 0.249428570077118 0.749264393178982 0.00130703674389942 vacuolar protein sorting 72 homolog (S. cerevisiae) FUNCTION: Could be a DNA-binding transcriptional regulator. May be involved in chromatin modification and remodeling.; . . ovary;salivary gland;intestine;colon;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;alveolus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; liver;atrioventricular node;cerebellum; 0.27664 0.14533 0.21689899 68.12927577 32.36914 1.01133 VRK1 0.0428984052164855 0.955888731237774 0.00121286354574094 vaccinia related kinase 1 FUNCTION: Serine/threonine kinase involved in Golgi disassembly during the cell cycle: following phosphorylation by PLK3 during mitosis, required to induce Golgi fragmentation. Acts by mediating phosphorylation of downstream target protein. Phosphorylates 'Thr- 18' of p53/TP53 and may thereby prevent the interaction between p53/TP53 and MDM2. Phosphorylates casein and histone H3. Phosphorylates BANF1: disrupts its ability to bind DNA, reduces its binding to LEM domain-containing proteins and causes its relocalization from the nucleus to the cytoplasm. Phosphorylates ATF2 which activates its transcriptional activity. {ECO:0000269|PubMed:10951572, ECO:0000269|PubMed:14645249, ECO:0000269|PubMed:15105425, ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:19103756}.; DISEASE: Pontocerebellar hypoplasia 1A (PCH1A) [MIM:607596]: A disorder characterized by an abnormally small cerebellum and brainstem, central and peripheral motor dysfunction from birth, gliosis and spinal cord anterior horn cells degeneration resembling infantile spinal muscular atrophy. Additional features include muscle hypotonia, congenital contractures and respiratory insufficiency that is evident at birth. {ECO:0000269|PubMed:19646678}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Highly expressed in fetal liver, testis and thymus. {ECO:0000269|PubMed:9344656}.; ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;epididymis;nasopharynx;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; fetal liver;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;tumor;white blood cells;cingulate cortex; 0.72004 0.10340 -0.381986487 27.68931352 25.27161 0.82641 VRK2 1.21621414925507e-08 0.549410088450979 0.450589899386879 vaccinia related kinase 2 FUNCTION: Serine/threonine kinase that regulates several signal transduction pathways. Isoform 1 modulates the stress response to hypoxia and cytokines, such as interleukin-1 beta (IL1B) and this is dependent on its interaction with MAPK8IP1, which assembles mitogen-activated protein kinase (MAPK) complexes. Inhibition of signal transmission mediated by the assembly of MAPK8IP1-MAPK complexes reduces JNK phosphorylation and JUN-dependent transcription. Phosphorylates 'Thr-18' of p53/TP53, histone H3, and may also phosphorylate MAPK8IP1. Phosphorylates BANF1 and disrupts its ability to bind DNA and reduces its binding to LEM domain-containing proteins. Downregulates the transactivation of transcription induced by ERBB2, HRAS, BRAF, and MEK1. Blocks the phosphorylation of ERK in response to ERBB2 and HRAS. Can also phosphorylate the following substrates that are commonly used to establish in vitro kinase activity: casein, MBP and histone H2B, but it is not sure that this is physiologically relevant.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in various tumor cell lines. Expression of isoform 1 inversely correlates with ERBB2 in breast carcinomas (at protein level). Widely expressed. Highly expressed in fetal liver, skeletal muscle, pancreas, heart, peripheral blood leukocytes and testis. {ECO:0000269|PubMed:16704422, ECO:0000269|PubMed:20679487, ECO:0000269|PubMed:9344656}.; myocardium;ovary;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;skeletal muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach; testis - interstitial;testis - seminiferous tubule;ciliary ganglion; 0.13255 0.09620 0.066214104 58.95848077 3255.28139 10.86391 VRK3 1.57414497489905e-06 0.852750633410481 0.147247792444544 vaccinia related kinase 3 FUNCTION: Inactive kinase that suppresses ERK activity by promoting phosphatase activity of DUSP3 which specifically dephosphorylates and inactivates ERK in the nucleus. {ECO:0000250, ECO:0000269|PubMed:14645249, ECO:0000269|PubMed:19141289}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;small intestine;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;liver;testis;atrioventricular node;trigeminal ganglion; 0.07305 0.08176 0.88921411 89.24274593 2416.11135 9.13108 VRTN 0.858358428932427 0.141182634799941 0.000458936267632461 vertebrae development associated . . . unclassifiable (Anatomical System);ovary;brain; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.65436 . -0.350843407 29.54116537 96.19087 2.12035 VSIG1 0.00569224987252447 0.900192250889125 0.0941154992383502 V-set and immunoglobulin domain containing 1 . . TISSUE SPECIFICITY: Detected only in stomach mucosa and testis, and to a much lesser level in pancreas (at protein level). Detected in gastric cancers (31%), esophageal carcinomas (50%) and ovarian cancers (23%). {ECO:0000269|PubMed:16405301}.; unclassifiable (Anatomical System);uterus;lung;nasopharynx;testis;stomach;aorta; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.37432 0.07497 -0.181750739 40.15687662 30.41091 0.96893 VSIG2 0.000163565811379291 0.680813504192724 0.319022929995897 V-set and immunoglobulin domain containing 2 . . TISSUE SPECIFICITY: Highly expressed in stomach, colon, prostate, trachea and thyroid glands and weakly in bladder and lung. {ECO:0000269|PubMed:9862345}.; unclassifiable (Anatomical System);colon;uterus;pancreas;prostate;whole body;lung;bone;liver;testis;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10318 0.09170 -0.025608647 51.91672564 322.84124 3.81715 VSIG4 0.000110511267388792 0.595538981447063 0.404350507285548 V-set and immunoglobulin domain containing 4 FUNCTION: Phagocytic receptor, strong negative regulator of T-cell proliferation and IL2 production. Potent inhibitor of the alternative complement pathway convertases. {ECO:0000269|PubMed:17016562, ECO:0000269|PubMed:17051150}.; . TISSUE SPECIFICITY: Abundantly expressed in several fetal tissues. In adult tissues, highest expression in lung and placenta. Expressed in resting macrophages. {ECO:0000269|PubMed:11004523, ECO:0000269|PubMed:17016562}.; . . 0.24072 0.09654 0.308721233 72.59966973 132.39375 2.50406 VSIG8 0.00315999833233031 0.946715264421233 0.0501247372464368 V-set and immunoglobulin domain containing 8 . . . . . . 0.09395 0.106667882 61.73036093 220.85006 3.21443 VSIG10 5.54754892563778e-07 0.654484694510008 0.3455147507351 V-set and immunoglobulin domain containing 10 . . . ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;thyroid;testis;bladder;brain;unclassifiable (Anatomical System);heart;urinary;muscle;pharynx;blood;lung;placenta;hippocampus;visual apparatus;liver;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; . . 0.42259095 77.22929936 4181.5983 12.84431 VSIG10L . . . V-set and immunoglobulin domain containing 10 like . . . unclassifiable (Anatomical System);optic nerve;cartilage;ovary;heart;bone;placenta;macula lutea;urinary;fovea centralis;choroid;lens;brain;retina; dorsal root ganglion;kidney;parietal lobe; . . . . 325.66665 3.83591 VSNL1 0.744967825012453 0.252709563700764 0.00232261128678347 visinin like 1 FUNCTION: Regulates (in vitro) the inhibition of rhodopsin phosphorylation in a calcium-dependent manner. {ECO:0000250}.; . TISSUE SPECIFICITY: Brain and retina. Neuron-specific in the central and peripheral nervous system. Increased in the cerebrospinal fluid of Alzheimer disease patients (at protein level). {ECO:0000269|PubMed:18703769}.; colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;larynx;bone;testis;brain;unclassifiable (Anatomical System);amygdala;heart;tongue;cerebellum cortex;hypothalamus;lens;skeletal muscle;lung;adrenal gland;macula lutea;hippocampus;liver;spleen;head and neck;kidney;cerebellum; whole brain;amygdala;superior cervical ganglion;occipital lobe;medulla oblongata;thalamus;cerebellum peduncles;hypothalamus;temporal lobe;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.45131 . -0.009020804 52.8544468 2.50243 0.09246 VSTM1 4.39176014077216e-09 0.0570390854396649 0.942960910168575 V-set and transmembrane domain containing 1 FUNCTION: Isoform 2: Behaves as a cytokine, promoting IL17A secretion by CD4+ T-cells, and differentiation and activation of IL17 producing helper T-cells (TH17).; . TISSUE SPECIFICITY: Expressed on myeloid (neutrophils, eosinophils and monocytes) but not on lymphoid cells. {ECO:0000269|PubMed:20375307}.; unclassifiable (Anatomical System);cartilage;ovary;placenta;parathyroid;blood;brain;bone marrow; dorsal root ganglion;ciliary ganglion;trigeminal ganglion; 0.04548 . 0.084621747 60.31493277 1238.62841 6.64471 VSTM2A 0.107352765766498 0.862143626948497 0.0305036072850052 V-set and transmembrane domain containing 2A . . . unclassifiable (Anatomical System);prostate;lung;hypothalamus;testis;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.17379 . -0.117432389 44.89266336 147.20254 2.64342 VSTM2A-OT1 . . . VSTM2A overlapping transcript 1 . . . . . . . . . . . VSTM2B . . . V-set and transmembrane domain containing 2B . . . hypothalamus;placenta; . 0.19663 . . . 600.30122 4.95862 VSTM2L 0.362003649087479 0.586998560827487 0.0509977900850344 V-set and transmembrane domain containing 2 like . . . . . 0.58728 0.11262 . . 492.90545 4.56586 VSTM4 0.155399626463079 0.828330668884091 0.0162697046528301 V-set and transmembrane domain containing 4 FUNCTION: Peptide Lv enhances L-type voltage-gated calcium channel (L-VGCC) currents in retinal photoreceptors. {ECO:0000250|UniProtKB:T1NXB5}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;tongue;hypothalamus;adrenal cortex;parathyroid;skin;uterus;prostate;whole body;lung;placenta;thyroid;testis;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.16951 . -0.156065314 42.16206653 1046.94253 6.21171 VSTM5 . . . V-set and transmembrane domain containing 5 . . . . . . . 1.302692676 93.93724935 266.29527 3.50161 VSX1 0.00659973339577821 0.751278899751132 0.24212136685309 visual system homeobox 1 FUNCTION: Binds to the 37-bp core of the locus control region (LCR) of the red/green visual pigment gene cluster. May regulate the activity of the LCR and the cone opsin genes at earlier stages of development.; DISEASE: Keratoconus 1 (KTCN1) [MIM:148300]: Frequent corneal dystrophy with an incidence that varies from 50 to 230 per 100'000. The cornea assumes a conical shape as a result of a progressive non-inflammatory thinning of the corneal stroma. Keratoconus is most often an isolated sporadic condition with cases of autosomal dominant and autosomal recessive transmission. {ECO:0000269|PubMed:11978762, ECO:0000269|PubMed:15623752, ECO:0000269|PubMed:19956409}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Craniofacial anomalies and anterior segment dysgenesis syndrome (CAASDS) [MIM:614195]: A disorder with extremely variable expressivity. Clinical features include wide interpupillary distance, abnormal corneal endothelium, unusual pinnae, partially to completely empty sella turcica, posterior fossa cyst, anterior encephalocele, and/or hydrocephalus. {ECO:0000269|PubMed:15051220}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: In the adult eye, expressed in lens, iris, ciliary body, choroid, optical nerve head and, most strongly, in retina, but not expressed in sclera and cornea. According to PubMed 11978762, expressed in adult retina but not in lens and cornea. Within adult retina, found exclusively in the inner nuclear layer. Isoform 1, isoform 2, isoform 3 and isoform 4 expressed in adult retina, but not in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. Not expressed in thymus and spleen. Expressed in embryonic craniofacial tissue. Expressed in fetal (week 14) retina. Strongly expressed in neonatal retina (day 0), weakly in neonatal lens (day 0), choroid (day 0) and cornea (day 0, 4; month 9). {ECO:0000269|PubMed:10673340, ECO:0000269|PubMed:10903837, ECO:0000269|PubMed:11978762, ECO:0000269|PubMed:18253095}.; . . 0.11501 0.13748 . . 335.76447 3.89322 VSX2 0.116076832895677 0.857047537196738 0.0268756299075852 visual system homeobox 2 FUNCTION: Plays a significant role in the specification and morphogenesis of the sensory retina. May also participate in the development of the cells of the inner nuclear layer, particularly bipolar cells (By similarity). {ECO:0000250}.; DISEASE: Microphthalmia with cataracts and iris abnormalities (MCOPCTI) [MIM:610092]: A disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues. Ocular abnormalities like opacities of the cornea and lens, scaring of the retina and choroid, cataract and other abnormalities like cataract may also be present. {ECO:0000269|PubMed:10932181}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Microphthalmia, isolated, with coloboma, 3 (MCOPCB3) [MIM:610092]: A disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues. Ocular abnormalities like opacities of the cornea and lens, scaring of the retina and choroid, and other abnormalities may also be present. Ocular colobomas are a set of malformations resulting from abnormal morphogenesis of the optic cup and stalk, and the fusion of the fetal fissure (optic fissure). {ECO:0000269|PubMed:15257456}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Abundantly expressed in retinal neuroblasts during eye development and in the inner nuclear layer of the adult retina. Within this layer, expression is stronger in the outer margin where bipolar cells predominate.; unclassifiable (Anatomical System);optic nerve;macula lutea;fovea centralis;retina; . 0.88730 0.24029 -0.293801652 32.93819297 351.56334 3.97396 VTA1 0.0824061412273581 0.907374010033833 0.0102198487388092 vesicle (multivesicular body) trafficking 1 FUNCTION: Involved in the endosomal multivesicular bodies (MVB) pathway. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. Thought to be a cofactor of VPS4A/B, which catalyzes disassembles membrane-associated ESCRT-III assemblies. Involved in the sorting and down-regulation of EGFR (By similarity). Involved in HIV-1 budding. {ECO:0000250, ECO:0000269|PubMed:15644320}.; . . . . 0.38552 0.14172 0.483275131 79.25218212 77.81433 1.85985 VTA1P1 . . . vesicle (multivesicular body) trafficking 1 pseudogene 1 . . . . . . . . . . . VTA1P2 . . . vesicle (multivesicular body) trafficking 1 pseudogene 2 . . . . . . . . . . . VTCN1 7.28889632660935e-09 0.0401928892298056 0.959807103481298 V-set domain containing T cell activation inhibitor 1 FUNCTION: Negatively regulates T-cell-mediated immune response by inhibiting T-cell activation, proliferation, cytokine production and development of cytotoxicity. When expressed on the cell surface of tumor macrophages, plays an important role, together with regulatory T-cells (Treg), in the suppression of tumor- associated antigen-specific T-cell immunity. Involved in promoting epithelial cell transformation. {ECO:0000250|UniProtKB:Q7TSP5, ECO:0000269|PubMed:15878339, ECO:0000269|PubMed:16606666, ECO:0000269|PubMed:17509674, ECO:0000269|PubMed:17875732}.; . TISSUE SPECIFICITY: Overexpressed in breast, ovarian, endometrial, renal cell (RCC) and non-small-cell lung cancers (NSCLC). Expressed on activated T- and B-cells, monocytes and dendritic cells, but not expressed in most normal tissues (at protein level). Widely expressed, including in kidney, liver, lung, ovary, placenta, spleen and testis. {ECO:0000269|PubMed:12818165, ECO:0000269|PubMed:14568939, ECO:0000269|PubMed:15878339, ECO:0000269|PubMed:16606666, ECO:0000269|PubMed:16782226, ECO:0000269|PubMed:16798883, ECO:0000269|PubMed:17509674}.; unclassifiable (Anatomical System);smooth muscle;ovary;islets of Langerhans;uterus;breast;whole body;lung;endometrium;nasopharynx;placenta;visual apparatus;liver;testis;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.15230 0.08577 0.238945317 69.20853975 116.69484 2.35030 VTI1A 0.413424037513717 0.584865708392305 0.00171025409397807 vesicle transport through interaction with t-SNAREs 1A FUNCTION: V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. Involved in vesicular transport from the late endosomes to the trans-Golgi network. Along with VAMP7, involved in an non- conventional RAB1-dependent traffic route to the cell surface used by KCNIP1 and KCND2. May be involved in increased cytokine secretion associated with cellular senescence. {ECO:0000269|PubMed:18195106, ECO:0000269|PubMed:19138172}.; . . . . 0.19470 0.11413 -0.317668748 31.45789101 25.32908 0.82829 VTI1B 0.209578768555067 0.781238942985146 0.00918228845978722 vesicle transport through interaction with t-SNAREs 1B FUNCTION: V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. May be concerned with increased secretion of cytokines associated with cellular senescence.; . TISSUE SPECIFICITY: Expressed in all tissues examined.; lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;amygdala;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;head and neck;kidney;stomach; whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;hypothalamus;spinal cord;prefrontal cortex;globus pallidus;caudate nucleus;pons;cingulate cortex; 0.46418 0.14454 -0.117432389 44.89266336 33.70655 1.03888 VTI1BP1 . . . vesicle transport through interaction with t-SNAREs 1B pseudogene 1 . . . . . . . . . . . VTI1BP2 . . . vesicle transport through interaction with t-SNAREs 1B pseudogene 2 . . . . . . . . . . . VTI1BP3 . . . vesicle transport through interaction with t-SNAREs 1B pseudogene 3 . . . . . . . . . . . VTI1BP4 . . . vesicle transport through interaction with t-SNAREs 1B pseudogene 4 . . . . . . . . . . . VTN 1.14001465111659e-09 0.31203135479259 0.687968644067395 vitronectin FUNCTION: Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.; . TISSUE SPECIFICITY: Plasma.; unclassifiable (Anatomical System);medulla oblongata;heart;ovary;adrenal cortex;fovea centralis;skin;retina;uterus;pancreas;lung;adrenal gland;thyroid;placenta;macula lutea;visual apparatus;pituitary gland;liver;testis;head and neck;spleen;cervix;kidney;brain;mammary gland; fetal liver;adrenal gland;liver;fetal lung;skeletal muscle; 0.45074 0.48187 -0.510624372 21.65015334 76.56421 1.83674 VTRNA1-1 . . . vault RNA 1-1 . . . . . . . . . . . VTRNA1-2 . . . vault RNA 1-2 . . . . . . . . . . . VTRNA1-3 . . . vault RNA 1-3 . . . . . . . . . . . VTRNA2-1 . . . vault RNA 2-1 . . . . . . . . . . . VTRNA2-2P . . . vault RNA 2-2, pseudogene . . . . . . . . . . . VTRNA3-1P . . . vault RNA 3-1, pseudogene . . . . . . . . . . . VWA1 0.0331997601703093 0.82084167327595 0.145958566553741 von Willebrand factor A domain containing 1 FUNCTION: Promotes matrix assembly. {ECO:0000250|UniProtKB:Q8R2Z5}.; . . unclassifiable (Anatomical System);islets of Langerhans;colon;fovea centralis;choroid;lens;retina;uterus;optic nerve;lung;placenta;macula lutea;testis;kidney;brain;stomach; . 0.15857 0.14239 . . 104.65734 2.21102 VWA2 2.57813515827879e-13 0.018334313881354 0.981665686118388 von Willebrand factor A domain containing 2 . . TISSUE SPECIFICITY: Expression is generally absent in normal colon and other normal body tissues, but it is induced an average of 78- fold in Stage II, III, and IV colon cancers, as well as in colon adenomas and colon cancer cell lines. {ECO:0000269|PubMed:15580307}.; unclassifiable (Anatomical System);colon; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.06988 0.10120 0.123045693 62.23755603 2879.98701 10.16244 VWA3A 1.83741135853222e-20 0.00570145143977014 0.99429854856023 von Willebrand factor A domain containing 3A . . . unclassifiable (Anatomical System);lung;cartilage;nasopharynx;testis;blood;kidney;lens;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; 0.22347 . 1.655315735 96.21372965 967.81296 6.01572 VWA3B 3.26524146038958e-18 0.596776821783912 0.403223178216088 von Willebrand factor A domain containing 3B . DISEASE: Note=Defects in VWA3B may be a cause of cerebellar ataxia with intellectual disability. {ECO:0000269|PubMed:26157035}.; . unclassifiable (Anatomical System);lung;testis; . 0.09166 . 1.322735566 94.07879217 1748.74917 7.72022 VWA5A 1.88623682085499e-15 0.0267417739595102 0.973258226040488 von Willebrand factor A domain containing 5A FUNCTION: May play a role in tumorigenesis as a tumor suppressor. Altered expression of this protein and disruption of the molecular pathway it is involved in, may contribute directly to or modify tumorigenesis.; . TISSUE SPECIFICITY: Expressed at low level in many tissues. Not expressed in 80% of tumor cell lines tested. {ECO:0000269|PubMed:14504409}.; parathyroid;choroid;fovea centralis;bone marrow;retina;optic nerve;thyroid;bone;testis;pineal gland;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;adrenal cortex;lens;skeletal muscle;lung;adrenal gland;placenta;hippocampus;macula lutea;cervix;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle;pituitary; 0.04851 . 0.648517637 84.14720453 1165.38867 6.49454 VWA5B1 . . . von Willebrand factor A domain containing 5B1 . . . lung;testis; . . . . . 7561.17588 18.64813 VWA5B2 0.354623648336578 0.48351541635271 0.161860935310712 von Willebrand factor A domain containing 5B2 . . . lung;frontal lobe;adrenal gland;islets of Langerhans;hypothalamus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion; . 0.09778 1.372468937 94.48572777 4139.22838 12.76384 VWA7 4.28880941939168e-07 0.988685600611748 0.0113139705073107 von Willebrand factor A domain containing 7 . . TISSUE SPECIFICITY: Expressed at low level in different cell lines. {ECO:0000269|PubMed:10803853}.; . . 0.07983 . 0.846940207 88.47605567 800.22615 5.57485 VWA8 2.93154218637359e-40 0.000220215286247372 0.999779784713753 von Willebrand factor A domain containing 8 . . . . . 0.15967 0.10375 -0.882165829 10.50955414 4822.23895 14.07096 VWA8-AS1 . . . VWA8 antisense RNA 1 (head to head) . . . . . . . . . . . VWA8P1 . . . von Willebrand factor A domain containing 8 pseudogene 1 . . . . . . . . . . . VWA9 0.00309381266728039 0.985379937348309 0.0115262499844104 von Willebrand factor A domain containing 9 . . TISSUE SPECIFICITY: Strongly expressed in numerous cancer cells compared with their non-cancerous counterparts (lung, prostate, colon, stomach and skin). {ECO:0000269|PubMed:19160420}.; . . 0.13137 0.09060 -0.471992905 23.03609342 28.36697 0.90857 VWC2 0.795160869537721 0.198998551464272 0.00584057899800672 von Willebrand factor C domain containing 2 FUNCTION: BMP antagonist which may play a role in neural development. Promotes cell adhesion (By similarity). {ECO:0000250}.; . . endometrium;macula lutea;fovea centralis; pons;cerebellum; 0.14502 . . . 3029.09668 10.45072 VWC2L 0.612117520612058 0.379586983871349 0.00829549551659338 von Willebrand factor C domain containing protein 2-like FUNCTION: May play a role in neurogenesis. May play a role in bone differentiation and matrix mineralization. {ECO:0000250}.; . . . . . . 0.103030231 61.2762444 18.10859 0.63207 VWC2L-IT1 . . . VWC2L intronic transcript 1 . . . . . . . . . . . VWCE 5.90266495568438e-13 0.798483807642881 0.201516192356529 von Willebrand factor C and EGF domains FUNCTION: May be a regulatory element in the beta-catenin signaling pathway and a target for chemoprevention of hapatocellular carcinoma. {ECO:0000269|PubMed:16496348}.; . TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:16496348}.; unclassifiable (Anatomical System);lymphoreticular;whole body;lung;placenta;liver;colon;spleen;choroid;kidney;retina; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.19722 0.10094 -0.902027742 10.1556971 191.21648 2.99921 VWDE . . . von Willebrand factor D and EGF domains . . . unclassifiable (Anatomical System);whole body;umbilical cord;islets of Langerhans;urinary;blood; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node; . . 7.749518299 99.93512621 13190.99889 24.71781 VWF 1.52411378256046e-11 0.999999999608107 3.76651636761949e-10 von Willebrand factor FUNCTION: Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma.; DISEASE: von Willebrand disease 1 (VWD1) [MIM:193400]: A common hemorrhagic disorder due to defects in von Willebrand factor protein and resulting in impaired platelet aggregation. Von Willebrand disease type 1 is characterized by partial quantitative deficiency of circulating von Willebrand factor, that is otherwise structurally and functionally normal. Clinical manifestations are mucocutaneous bleeding, such as epistaxis and menorrhagia, and prolonged bleeding after surgery or trauma. {ECO:0000269|PubMed:10887119, ECO:0000269|PubMed:11698279}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: von Willebrand disease 2 (VWD2) [MIM:613554]: A hemorrhagic disorder due to defects in von Willebrand factor protein and resulting in altered platelet aggregation. Von Willebrand disease type 2 is characterized by qualitative deficiency and functional anomalies of von Willebrand factor. It is divided in different subtypes including 2A, 2B, 2M and 2N (Normandy variant). The mutant VWF protein in types 2A, 2B and 2M are defective in their platelet-dependent function, whereas the mutant protein in type 2N is defective in its ability to bind factor VIII. Clinical manifestations are mucocutaneous bleeding, such as epistaxis and menorrhagia, and prolonged bleeding after surgery or trauma. {ECO:0000269|PubMed:12406074, ECO:0000269|PubMed:1409710, ECO:0000269|PubMed:1419803, ECO:0000269|PubMed:1419804, ECO:0000269|PubMed:1420817, ECO:0000269|PubMed:1429668, ECO:0000269|PubMed:1672694, ECO:0000269|PubMed:1673047, ECO:0000269|PubMed:1729889, ECO:0000269|PubMed:1761120, ECO:0000269|PubMed:1832934, ECO:0000269|PubMed:1906179, ECO:0000269|PubMed:2010538, ECO:0000269|PubMed:2011604, ECO:0000269|PubMed:21592258, ECO:0000269|PubMed:2786201, ECO:0000269|PubMed:7620154, ECO:0000269|PubMed:7734373, ECO:0000269|PubMed:7789955, ECO:0000269|PubMed:8011991, ECO:0000269|PubMed:8123843, ECO:0000269|PubMed:8123844, ECO:0000269|PubMed:8338947, ECO:0000269|PubMed:8348943, ECO:0000269|PubMed:8376405, ECO:0000269|PubMed:8435341, ECO:0000269|PubMed:8486782, ECO:0000269|PubMed:8547152, ECO:0000269|PubMed:8622978}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: von Willebrand disease 3 (VWD3) [MIM:277480]: A severe hemorrhagic disorder due to a total or near total absence of von Willebrand factor in the plasma and cellular compartments, also leading to a profound deficiency of plasmatic factor VIII. Bleeding usually starts in infancy and can include epistaxis, recurrent mucocutaneous bleeding, excessive bleeding after minor trauma, and hemarthroses. {ECO:0000269|PubMed:10887119, ECO:0000269|PubMed:7989040, ECO:0000269|PubMed:8088787}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Plasma.; myocardium;smooth muscle;ovary;sympathetic chain;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;brain;tonsil;amygdala;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;vein;uterus;oesophagus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);islets of Langerhans;muscle;pancreas;lung;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus;cerebellum; . 0.23835 0.80848 1.036444045 91.14177872 8614.16756 20.10291 VWFP1 . . . von Willebrand factor pseudogene 1 . . . . . . . . . . . WAC 0.999891942627968 0.000108057325244366 4.6788133695221e-11 WW domain containing adaptor with coiled-coil FUNCTION: Acts as a linker between gene transcription and histone H2B monoubiquitination at 'Lys-120' (H2BK120ub1). Interacts with the RNA polymerase II transcriptional machinery via its WW domain and with RNF20-RNF40 via its coiled coil region, thereby linking and regulating H2BK120ub1 and gene transcription. Regulates the cell-cycle checkpoint activation in response to DNA damage. Positive regulator of amino acid starvation-induced autophagy. May negatively regulate the ubiquitin proteasome pathway. {ECO:0000269|PubMed:21329877, ECO:0000269|PubMed:22354037}.; . . smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;gall bladder;heart;cartilage;adrenal cortex;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;duodenum;amnion;head and neck;kidney;stomach;aorta;cerebellum; amygdala;testis - interstitial;occipital lobe;superior cervical ganglion;cerebellum peduncles;atrioventricular node;pons;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.23812 0.12474 -0.867014353 10.72776598 545.45625 4.75017 WAC-AS1 . . . WAC antisense RNA 1 (head to head) . . . . . . . . . . . WAPL . . . WAPL cohesin release factor FUNCTION: Regulator of sister chromatid cohesion in mitosis which negatively regulates cohesin association with chromatin. Involved in both sister chromatid cohesion during interphase and sister- chromatid resolution during early stages of mitosis. Couples DNA replication to sister chromatid cohesion. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. {ECO:0000269|PubMed:15150110, ECO:0000269|PubMed:17112726, ECO:0000269|PubMed:17113138, ECO:0000269|PubMed:19696148, ECO:0000269|PubMed:19907496, ECO:0000269|PubMed:21111234, ECO:0000269|PubMed:23776203}.; . TISSUE SPECIFICITY: Isoform 1 is highly expressed in uterine cervix tumor. Isoform 2 is widely expressed with a high level in skeletal muscle and heart. {ECO:0000269|PubMed:15150110, ECO:0000269|PubMed:15383329}.; . . 0.82894 0.14717 -1.195919584 5.832743572 . . WARS 0.994700675309381 0.0052987064059774 6.1828464125343e-07 tryptophanyl-tRNA synthetase FUNCTION: Isoform 1, isoform 2 and T1-TrpRS have aminoacylation activity while T2-TrpRS lacks it. Isoform 2, T1-TrpRS and T2-TrpRS possess angiostatic activity whereas isoform 1 lacks it. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression. {ECO:0000269|PubMed:11773625, ECO:0000269|PubMed:11773626, ECO:0000269|PubMed:1373391, ECO:0000269|PubMed:14630953}.; . . ovary;umbilical cord;skin;bone marrow;retina;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pineal body;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;oesophagus;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;adrenal gland;placenta;amnion;head and neck;kidney;stomach;aorta; testis - interstitial;placenta;testis;tumor; 0.19486 0.41998 -0.26993514 34.59542345 108.70749 2.26305 WARS2 0.601342004604768 0.396740366757987 0.00191762863724484 tryptophanyl tRNA synthetase 2, mitochondrial . . . ovary;colon;fovea centralis;skin;bone marrow;uterus;prostate;whole body;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;blood;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;stomach;aorta;thymus; superior cervical ganglion; 0.13868 0.27846 0.240763792 69.36777542 914.61642 5.88205 WARS2-IT1 . . . WARS2 intronic transcript 1 . . . . . . . . . . . WARS2P1 . . . tryptophanyl tRNA synthetase 2 pseudogene 1 . . . . . . . . . . . WARSP1 . . . tryptophanyl-tRNA synthetase pseudogene 1 . . . . . . . . . . . WAS 0.991202084335487 0.0087957800518859 2.1356126274427e-06 Wiskott-Aldrich syndrome FUNCTION: Effector protein for Rho-type GTPases. Regulates actin filament reorganization via its interaction with the Arp2/3 complex. Important for efficient actin polymerization. Possible regulator of lymphocyte and platelet function. Mediates actin filament reorganization and the formation of actin pedestals upon infection by pathogenic bacteria. {ECO:0000269|PubMed:12235133, ECO:0000269|PubMed:16275905, ECO:0000269|PubMed:18650809}.; DISEASE: Wiskott-Aldrich syndrome (WAS) [MIM:301000]: An X-linked recessive immunodeficiency characterized by eczema, thrombocytopenia, recurrent infections, and bloody diarrhea. Death usually occurs before age 10. {ECO:0000269|PubMed:10447259, ECO:0000269|PubMed:11793485, ECO:0000269|PubMed:7753869, ECO:0000269|PubMed:8528198, ECO:0000269|PubMed:8528199, ECO:0000269|PubMed:8682510, ECO:0000269|PubMed:9098856, ECO:0000269|PubMed:9126958, ECO:0000269|PubMed:9445409, ECO:0000269|PubMed:9683546, ECO:0000269|PubMed:9713366}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Thrombocytopenia 1 (THC1) [MIM:313900]: Thrombocytopenia is defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting. {ECO:0000269|PubMed:10447259, ECO:0000269|PubMed:11167787, ECO:0000269|PubMed:11877312, ECO:0000269|PubMed:7795648, ECO:0000269|PubMed:8528199}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Neutropenia, severe congenital, X-linked (XLN) [MIM:300299]: A disorder of hematopoiesis characterized by maturation arrest of granulopoiesis at the level of promyelocytes with peripheral blood absolute neutrophil counts below 0.5 x 10(9)/l and early onset of severe bacterial infections. {ECO:0000269|PubMed:11242115}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed predominantly in the thymus. Also found, to a much lesser extent, in the spleen. {ECO:0000269|PubMed:8069912}.; . . 0.84468 0.55945 0.505321956 80.00707714 38.35529 1.13817 WASF1 0.914369887040239 0.085605042406122 2.50705536390588e-05 WAS protein family member 1 FUNCTION: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex.; . TISSUE SPECIFICITY: Highly expressed in brain. Lowly expressed in testis, ovary, colon, kidney, pancreas, thymus, small intestine and peripheral blood.; unclassifiable (Anatomical System);ovary;cerebellum cortex;hypothalamus;urinary;colon;skin;skeletal muscle;uterus;prostate;lung;frontal lobe;larynx;bone;placenta;visual apparatus;hippocampus;testis;cervix;head and neck;spleen;brain;bladder;aorta; whole brain;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;temporal lobe;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;testis;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.68029 . -0.049474214 50.01179523 30.31193 0.96671 WASF1P1 . . . WASF1 pseudogene 1 . . . . . . . . . . . WASF2 0.975317445622322 0.02467709695974 5.45741793755747e-06 WAS protein family member 2 FUNCTION: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. {ECO:0000269|PubMed:10381382, ECO:0000269|PubMed:16275905}.; . TISSUE SPECIFICITY: Expressed in all tissues with strongest expression in placenta, lung, and peripheral blood leukocytes, but not in skeletal muscle. {ECO:0000269|PubMed:10381382}.; . . 0.44161 0.18052 -0.003562597 53.72729417 54.35937 1.47373 WASF3 0.960588201860343 0.0393943684080538 1.74297316034808e-05 WAS protein family member 3 FUNCTION: Downstream effector molecules involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. {ECO:0000269|PubMed:17623672, ECO:0000269|PubMed:21834987}.; . TISSUE SPECIFICITY: Expressed in ovary and brain.; ovary;colon;parathyroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;atrium;whole body;ganglion;endometrium;testis;artery;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;skeletal muscle;breast;lung;macula lutea;visual apparatus;kidney;mammary gland;stomach;aorta;peripheral nerve; amygdala;whole brain;occipital lobe;superior cervical ganglion;thalamus;medulla oblongata;adipose tissue;cerebellum peduncles;hypothalamus;temporal lobe;spinal cord;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex;cerebellum; 0.32531 0.13385 0.110306132 62.00165133 503.82467 4.60607 WASF3-AS1 . . . WASF3 antisense RNA 1 . . . . . . . . . . . WASF4P . . . WAS protein family member 4, pseudogene . . . unclassifiable (Anatomical System);breast;lung;whole body;bone;testis;colon;kidney;germinal center;brain;skin; . 0.06747 0.07605 . . . . WASF5P . . . WAS protein family member 5, pseudogene . . . . . . . . . . . WASH1 . . . WAS protein family homolog 1 FUNCTION: Acts as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:19922874, PubMed:19922875, PubMed:20498093, PubMed:23452853). Its assembly in the WASH core complex seems to inhibit its NPF activity and via FAM21 is required for its membrane targeting (PubMed:20498093). Involved in endocytic trafficking of EGF (By similarity). Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration (PubMed:22114305). In T cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T cell activation (By similarity). Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling. Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex (PubMed:24344185). Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity). {ECO:0000250|UniProtKB:C4AMC7, ECO:0000250|UniProtKB:Q8VDD8, ECO:0000269|PubMed:19922874, ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093, ECO:0000269|PubMed:22114305, ECO:0000269|PubMed:23452853, ECO:0000305|PubMed:20498093}.; . . . . . . . . . . WASH2P . . . WAS protein family homolog 2 pseudogene FUNCTION: Acts as a nucleation-promoting factor at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. Involved in endocytic trafficking of EGF. Its assembly in the WASH core complex seems to inhibit its NPF activity and via FAM21 is required for its membrane targeting. Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration. In T cells involved in endosome-to- membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T cell proliferation and effector function. In dendritic cells involved in endosome-to- membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T cell activation. Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling. Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex. Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity). {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:C4AMC7, ECO:0000250|UniProtKB:Q8VDD8}.; . . medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;muscle;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; . . . . . . . WASH3P . . . WAS protein family homolog 3 pseudogene FUNCTION: Acts as a nucleation-promoting factor at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:18159949, PubMed:20175130). Involved in endocytic trafficking of EGF (PubMed:20175130). Its assembly in the WASH core complex seems to inhibit its NPF activity and via FAM21 is required for its membrane targeting. Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration (By similarity). In T cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T cell activation. Involved in Arp2/3 complex- dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling (By similarity). Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex (By similarity). Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity). {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:Q8VDD8, ECO:0000269|PubMed:18159949, ECO:0000269|PubMed:20175130}.; . . myocardium;medulla oblongata;ovary;umbilical cord;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;gum;thyroid;germinal center;brain;bladder;tonsil;cartilage;heart;tongue;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;colon;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach; . . . . . . . WASH4P 0.472112531877142 0.44175786692242 0.0861296012004378 WAS protein family homolog 4 pseudogene FUNCTION: May act as a nucleation-promoting factor at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:C4AMC7}.; . . lymphoreticular;medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;larynx;bone;thyroid;testis;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lacrimal gland;tongue;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;stomach;peripheral nerve; . . . . . 4780.64531 14.01463 WASH5P . . . WAS protein family homolog 5 pseudogene . . . . . . . . . . . WASH6P . . . WAS protein family homolog 6 pseudogene FUNCTION: May act as a nucleation-promoting factor at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:C4AMC7}.; . . myocardium;lymphoreticular;umbilical cord;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;gum;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;peripheral nerve;colon;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;pineal gland;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;muscle;pancreas;lung;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;cerebellum; . . . . . . . WASH7P . . . WAS protein family homolog 7 pseudogene . . . . . . . . . . . WASIR1 . . . WASH and IL9R antisense RNA 1 . . . . . . . . . . . WASIR2 . . . WASH and IL9R antisense RNA 2 . . . whole body;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; . . . . . . WASL 0.961960486819179 0.0380362818656231 3.23131519828824e-06 Wiskott-Aldrich syndrome-like FUNCTION: Regulates actin polymerization by stimulating the actin- nucleating activity of the Arp2/3 complex. Involved in mitosis and cytokinesis, via its role in the regulation of actin polymerization. Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. {ECO:0000269|PubMed:19366662, ECO:0000269|PubMed:19487689, ECO:0000269|PubMed:22847007, ECO:0000269|PubMed:22921828}.; . . ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;amniotic fluid;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; dorsal root ganglion;amygdala;fetal liver;superior cervical ganglion;occipital lobe;placenta;atrioventricular node;trigeminal ganglion; 0.89386 0.35187 -0.692458599 14.96815287 24.64068 0.80952 WBP1 0.000303097285548392 0.8030002619701 0.196696640744351 WW domain binding protein 1 . . TISSUE SPECIFICITY: Expressed in most tissues but at significantly lower levels in placenta, lung, liver, and kidney.; lymphoreticular;ovary;sympathetic chain;colon;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;heart;lacrimal gland;tongue;islets of Langerhans;hypothalamus;muscle;blood;lens;skeletal muscle;pancreas;lung;epididymis;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; . . 0.10512 -0.26993514 34.59542345 86.33658 1.98463 WBP1L 0.909387313715096 0.0904698132237364 0.000142873061167171 WW domain binding protein 1-like . . . . . 0.80034 0.10518 0.150760231 64.51403633 860.27606 5.72076 WBP1LP1 . . . WW domain binding protein 1-like pseudogene 1 . . . . . . . . . . . WBP1LP2 . . . WW domain binding protein 1-like pseudogene 2 . . . . . . . . . . . WBP1LP3 . . . WW domain binding protein 1-like pseudogene 3 . . . . . . . . . . . WBP1LP4 . . . WW domain binding protein 1-like pseudogene 4 . . . . . . . . . . . WBP1LP5 . . . WW domain binding protein 1-like pseudogene 5 . . . . . . . . . . . WBP1LP6 . . . WW domain binding protein 1-like pseudogene 6 . . . . . . . . . . . WBP1LP7 . . . WW domain binding protein 1-like pseudogene 7 . . . . . . . . . . . WBP1LP8 . . . WW domain binding protein 1-like pseudogene 8 . . . . . . . . . . . WBP1LP9 . . . WW domain binding protein 1-like pseudogene 9 . . . . . . . . . . . WBP1LP10 . . . WW domain binding protein 1-like pseudogene 10 . . . . . . . . . . . WBP1LP11 . . . WW domain binding protein 1-like pseudogene 11 . . . . . . . . . . . WBP1LP12 . . . WW domain binding protein 1-like pseudogene 12 . . . . . . . . . . . WBP2 0.089618232806846 0.86997030592298 0.0404114612701738 WW domain binding protein 2 . . TISSUE SPECIFICITY: Ubiquitous.; lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;tonsil;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;pancreas;lung;placenta;hippocampus;kidney;stomach;thymus; whole brain;amygdala;superior cervical ganglion;occipital lobe;thalamus;medulla oblongata;spinal cord;prefrontal cortex;ciliary ganglion;pons;caudate nucleus;parietal lobe;cerebellum; 0.46019 0.12984 -0.0274281 51.65723048 36.77815 1.10253 WBP2NL 2.07233062858540e-09 0.0701897706886352 0.929810227239034 WBP2 N-terminal like FUNCTION: May play a role in meotic resumption and pronuclear formation, mediated by a WW domain-signaling pathway during fertilization. {ECO:0000250}.; . . medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;oesophagus;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;spleen;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.06845 0.08769 1.350418743 94.35008257 726.32846 5.35145 WBP2P1 . . . WW domain binding protein 2 pseudogene 1 . . . . . . . . . . . WBP4 0.000482126451524307 0.967349070576651 0.0321688029718246 WW domain binding protein 4 FUNCTION: Promotes pre-mRNA splicing. A spliceosome-associated protein; may play a role in cross-intron bridging of U1 and U2 snRNPs in the mammalian A complex. {ECO:0000269|PubMed:19592703, ECO:0000269|PubMed:9724750}.; . . . . 0.16806 0.10530 -0.249709319 35.74545883 65.91875 1.67146 WBP11 0.999928146457789 7.18535248941268e-05 1.73168670733634e-11 WW domain binding protein 11 FUNCTION: Activates pre-mRNA splicing. May inhibit PP1 phosphatase activity. {ECO:0000269|PubMed:10593949, ECO:0000269|PubMed:11375989, ECO:0000269|PubMed:14640981}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in the heart, pancreas, kidney skeletal muscle, placenta and brain (at protein level). Weakly expressed in liver and lung. {ECO:0000269|PubMed:11375989}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;pineal body;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;cerebellum cortex;hypothalamus;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; whole brain;amygdala;testis - interstitial;placenta;tumor;testis;white blood cells; 0.58677 0.11579 -0.137658575 43.57159707 100.52915 2.17240 WBP11P1 . . . WW domain binding protein 11 pseudogene 1 . . . . . . . . . . . WBS2 . . . Williams-Beuren syndrome type 2 . . . . . . . . . . . WBSCR2 . . . Williams-Beuren syndrome chromosome region 2 . . . . . . . . . . . WBSCR16 0.000647047934647949 0.735317886368225 0.264035065697127 Williams-Beuren syndrome chromosome region 16 . . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12073013}.; lymphoreticular;myocardium;ovary;salivary gland;colon;parathyroid;skin;uterus;prostate;endometrium;oesophagus;larynx;bone;iris;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;hippocampus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;thymus; . 0.68423 0.08163 . . 1510.56029 7.21716 WBSCR17 0.0956174277642264 0.902732933438675 0.00164963879709826 Williams-Beuren syndrome chromosome region 17 FUNCTION: May catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. {ECO:0000250}.; DISEASE: Note=WBSCR17 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region.; TISSUE SPECIFICITY: Highly expressed in brain and heart. Weakly expressed in kidney, liver, lung and spleen. {ECO:0000269|PubMed:12073013}.; unclassifiable (Anatomical System);fovea centralis;choroid;lens;retina;prostate;optic nerve;whole body;lung;frontal lobe;cochlea;cerebral cortex;placenta;bone;macula lutea;pituitary gland;iris;kidney;brain; amygdala;dorsal root ganglion;whole brain;thalamus;occipital lobe;medulla oblongata;olfactory bulb;cerebellum peduncles;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.61105 0.11262 -1.221604042 5.573248408 28.7496 0.92008 WBSCR22 0.52115193984232 0.478695709717543 0.000152350440137075 Williams Beuren syndrome chromosome region 22 FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA (By similarity). Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity. Locus-specific steroid receptor coactivator. Potentiates transactivation by glucocorticoid (NR3C1), mineralocorticoid (NR3C2), androgen (AR) and progesterone (PGR) receptors. Required for the maintenance of open chromatin at the TSC22D3/GILZ locus to facilitate NR3C1 loading on the response elements. Required for maintenance of dimethylation on histone H3 'Lys-79' (H3K79me2), although direct histone methyltransferase activity is not observed in vitro (PubMed:24488492). {ECO:0000250, ECO:0000269|PubMed:24086612, ECO:0000269|PubMed:24488492}.; DISEASE: Note=WBSCR22 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of WBSCR22 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease. {ECO:0000305|PubMed:11978965}.; TISSUE SPECIFICITY: Widely expressed, with high levels in heart, skeletal muscle and kidney. Detected at high levels in bronchial brushings and in normal lung (at protein level). In fetal lung tissue, expressed in the developing bronchial lumen lining cells (at protein level). Tends to be down-regulated in lungs affected by inflammatory diseases or neoplasia (at protein level). Expressed in immune cells, including B and T lymphocytes and macrophages. {ECO:0000269|PubMed:11978965, ECO:0000269|PubMed:12073013, ECO:0000269|PubMed:24488492}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;endometrium;synovium;larynx;bone;thyroid;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;cervix;kidney;mammary gland;aorta;stomach;peripheral nerve;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;skeletal muscle; 0.05749 0.11835 -0.560178693 19.30879925 25.82653 0.84040 WBSCR27 0.0679116625114122 0.871628443895807 0.0604598935927809 Williams Beuren syndrome chromosome region 27 . DISEASE: Note=WBSCR27 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of WBSCR27 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease. {ECO:0000269|Ref.1}.; . uterus;colon;skin; . 0.06411 . 1.306318795 93.99622552 304.99929 3.71880 WBSCR28 1.58800503099146e-06 0.23555636234666 0.76444204964831 Williams-Beuren syndrome chromosome region 28 . . . unclassifiable (Anatomical System);medulla oblongata;testis; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;kidney;caudate nucleus;skeletal muscle; 0.11932 0.07913 0.418953042 77.06416608 160.74681 2.76930 WDFY1 1.68817254810104e-05 0.873537087058935 0.126446031215584 WD repeat and FYVE domain containing 1 FUNCTION: Positively regulates TLR3- and TLR4-mediated signaling pathways by bridging the interaction between TLR3 or TLR4 and TICAM1. Promotes TLR3/4 ligand-induced activation of transcription factors IRF3 and NF-kappa-B, as well as the production of IFN-beta and inflammatory cytokines (PubMed:25736436). {ECO:0000269|PubMed:25736436}.; . . ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;cerebral cortex;oesophagus;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);heart;adrenal cortex;blood;skeletal muscle;bile duct;breast;pancreas;lung;adrenal gland;placenta;macula lutea;liver;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;trigeminal ganglion; 0.15895 0.10625 -0.846787714 11.05803255 33.50081 1.03409 WDFY2 0.00359500151111569 0.987074971866305 0.00933002662257969 WD repeat and FYVE domain containing 2 FUNCTION: Acts in an adapter protein-like fashion to mediate the interaction between the kinase PRKCZ and its substrate VAMP2 and increases the PRKCZ-dependent phosphorylation of VAMP2 (PubMed:17313651). Positively regulates adipocyte differentiation, by facilitating the phosphorylation and thus inactivation of the anti-adipogenetic transcription factor FOXO1 by the kinase AKT1 (PubMed:18388859). Plays a role in endosomal control of AKT2 signaling; required for insulin-stimulated AKT2 phosphorylation and glucose uptake and insulin-stimulated phosphorylation of AKT2 substrates (By similarity). Participates in transferrin receptor endocytosis (PubMed:16873553). {ECO:0000250|UniProtKB:Q8BUB4, ECO:0000269|PubMed:16873553, ECO:0000269|PubMed:17313651, ECO:0000269|PubMed:18388859}.; . . unclassifiable (Anatomical System);prostate;pancreas;lymph node;ovary;endometrium;thyroid;muscle;spleen;brain;skin; dorsal root ganglion;testis - interstitial;uterus corpus;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.16955 0.11257 -0.047654689 50.22410946 302.50677 3.70419 WDFY3 1 3.27482414149096e-17 4.22627055154939e-47 WD repeat and FYVE domain containing 3 FUNCTION: Required for selective autophagy (aggrephagy) but not for autophagic degradation of bulk cytospol in response to starvation. Involved in the formation and degradation of cytoplasmic polyubiquitin-containing bodies (p62 bodies, ALIS/aggresome-like induced structures). May play a role as adaptor or scaffolding protein by promoting the association of the E3-like ligase ATG12-ATG5-ATG16L and LC3 to ubiquitinated target substrate. The association with GABARAP is required for its recruitment to LC3B-positive p62 bodies suggesting a role in targeting certain p62 structures for clearance. Involved in midbody ring degradation. {ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20417604, ECO:0000269|PubMed:24128730}.; . TISSUE SPECIFICITY: Ubiquitous. Expressed in osteoclast and their mononuclear precursors (at protein level). {ECO:0000269|PubMed:15292400, ECO:0000269|PubMed:20971078}.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hippocampus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;occipital lobe;subthalamic nucleus;superior cervical ganglion;prefrontal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.30087 0.11380 -2.817477736 0.62514744 213.17232 3.15112 WDFY3-AS1 . . . WDFY3 antisense RNA 1 . . . . . . . . . . . WDFY3-AS2 . . . WDFY3 antisense RNA 2 . . . . . 0.11620 . . . . . WDFY4 . . . WDFY family member 4 . . . unclassifiable (Anatomical System);lymphoreticular;lymph node;spinal cord;blood;skin;bone marrow;pancreas;lung;hippocampus;testis;spleen;germinal center;kidney;tonsil;thymus; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; . 0.09927 4.264461124 99.72281198 5281.75473 15.01039 WDHD1 1.82370607612634e-11 0.997485460314291 0.0025145396674718 WD repeat and HMG-box DNA binding protein 1 FUNCTION: Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. {ECO:0000269|PubMed:19805216}.; . . unclassifiable (Anatomical System);smooth muscle;cartilage;ovary;heart;colon;parathyroid;blood;vein;skin;skeletal muscle;bone marrow;breast;uterus;whole body;lung;placenta;visual apparatus;hypopharynx;liver;testis;head and neck;kidney;germinal center;brain;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.91998 0.09155 0.786269343 87.29063458 1459.63805 7.12456 WDPCP 2.32411054871015e-09 0.87511506730996 0.12488493036593 WD repeat containing planar cell polarity effector FUNCTION: Probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis and collective cell movements. {ECO:0000250}.; DISEASE: Bardet-Biedl syndrome 15 (BBS15) [MIM:615992]: A syndrome characterized by usually severe pigmentary retinopathy, early- onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:20671153}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Congenital heart defects, hamartomas of tongue, and polysyndactyly (CHDTHP) [MIM:217085]: A disease characterized by a constellation of anomalies including tongue hamartomas, polysyndactyly, and congenital heart defects such as atrioventricular canal and coarctation of the aorta. {ECO:0000269|PubMed:25427950}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=Mutations in WDPCP may act as modifiers of the phenotypic expression of Bardet-Biedl syndrome and Meckel syndrome by interacting in trans with primary BBS and MKS loci. {ECO:0000269|PubMed:20671153}.; . unclassifiable (Anatomical System);medulla oblongata;heart;ovary;urinary;parathyroid;skeletal muscle;skin;uterus;lung;placenta;testis;mammary gland;brain; . . . 0.466683681 78.73908941 277.11693 3.56422 WDR1 0.994593463305913 0.00540640528267948 1.3141140709357e-07 WD repeat domain 1 FUNCTION: Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins. {ECO:0000250}.; . . unclassifiable (Anatomical System);breast;smooth muscle;bone;visual apparatus;colon;stomach;bone marrow; testis - interstitial;lung;smooth muscle;testis - seminiferous tubule;heart;placenta;testis;white blood cells;whole blood; 0.62900 0.13780 -0.574945567 18.90186365 75.89354 1.82557 WDR3 3.05076498982483e-07 0.999842601103122 0.000157093820379002 WD repeat domain 3 . . TISSUE SPECIFICITY: Ubiquitous.; unclassifiable (Anatomical System);medulla oblongata;lymph node;heart;sympathetic chain;adrenal cortex;colon;blood;skin;uterus;prostate;whole body;lung;endometrium;larynx;placenta;visual apparatus;testis;head and neck;germinal center;kidney;brain;mammary gland;aorta;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.74985 0.11386 -0.194700582 39.24274593 1882.12176 7.97866 WDR4 5.33772408317289e-06 0.66280934583316 0.337185316442757 WD repeat domain 4 FUNCTION: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit. {ECO:0000255|HAMAP-Rule:MF_03056, ECO:0000269|PubMed:12403464}.; . . unclassifiable (Anatomical System);lymph node;cartilage;ovary;islets of Langerhans;colon;parathyroid;blood;skin;bone marrow;uterus;prostate;pancreas;whole body;lung;larynx;bone;placenta;visual apparatus;liver;testis;cervix;head and neck;kidney;germinal center;brain;stomach; superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;skeletal muscle; 0.83955 0.10333 -0.927704399 9.719273414 2823.9756 10.02628 WDR5 0.99870216011753 0.00129781990676481 1.99757049089818e-08 WD repeat domain 5 FUNCTION: Contributes to histone modification. May position the N- terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation. {ECO:0000269|PubMed:16600877, ECO:0000269|PubMed:16829960, ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:19556245, ECO:0000269|PubMed:20018852}.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;colon;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pineal body;blood;skeletal muscle;breast;lung;placenta;visual apparatus;hippocampus;duodenum;liver;spleen;head and neck;cervix;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.36771 0.17821 -0.251530012 35.42108988 11.07933 0.40100 WDR5B 5.46914499159414e-05 0.261431688630331 0.738513619919753 WD repeat domain 5B FUNCTION: May function as a substrate receptor for CUL4-DDB1 ubiquitin E3 ligase complex. {ECO:0000250}.; . . unclassifiable (Anatomical System);urinary;colon;skin;skeletal muscle;bile duct;uterus;prostate;whole body;lung;bone;placenta;testis;spleen;kidney;brain;aorta;stomach; dorsal root ganglion;superior cervical ganglion;pons;trigeminal ganglion; 0.40098 0.11309 0.106667882 61.73036093 46.30449 1.31096 WDR6 9.19647551585082e-07 0.996145197106259 0.00385388324618979 WD repeat domain 6 FUNCTION: Enhances the STK11/LKB1-induced cell growth suppression activity. Negative regulator of amino acid starvation-induced autophagy. {ECO:0000269|PubMed:17216128, ECO:0000269|PubMed:22354037}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10903905}.; lymphoreticular;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;pineal body;urinary;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;peripheral nerve;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;larynx;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;lacrimal gland;islets of Langerhans;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach; subthalamic nucleus;fetal brain;testis - seminiferous tubule;adrenal cortex;testis;fetal thyroid; 0.09490 0.09811 -1.433039328 4.010379807 183.03486 2.93720 WDR7 0.999999983540482 1.64595181832464e-08 9.64083443808268e-22 WD repeat domain 7 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;larynx;bone;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; amygdala;whole brain;dorsal root ganglion;superior cervical ganglion;occipital lobe;thalamus;medulla oblongata;hypothalamus;temporal lobe;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.29145 0.11884 -2.296802403 1.220806794 89.49586 2.03401 WDR7-OT1 . . . WDR7 overlapping transcript 1 . . . . . . . . . . . WDR11 0.070328055046955 0.929671906698212 3.82548330567124e-08 WD repeat domain 11 . DISEASE: Note=A chromosomal aberration involving WDR11 is found in a form of Kallmann syndrome. Translocation 46,XY,t(10;12)(q26.12;q13.11).; DISEASE: Hypogonadotropic hypogonadism 14 with or without anosmia (HH14) [MIM:614858]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic- pituitary axis. In some cases, it is associated with non- reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:20887964}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;spinal cord; 0.17774 0.14267 -0.925889687 9.754659118 96.63781 2.12360 WDR11-AS1 . . . WDR11 antisense RNA 1 . . . . . . . . . . . WDR12 0.609006890639148 0.390918737040653 7.43723201988532e-05 WD repeat domain 12 FUNCTION: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. {ECO:0000255|HAMAP-Rule:MF_03029, ECO:0000269|PubMed:16043514, ECO:0000269|PubMed:17353269}.; . . ovary;colon;skin;prostate;whole body;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;islets of Langerhans;blood;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.68828 . -0.26993514 34.59542345 342.60629 3.92544 WDR13 0.940346118992748 0.0594122603188394 0.000241620688412707 WD repeat domain 13 . . TISSUE SPECIFICITY: Widely expressed.; smooth muscle;ovary;substantia nigra;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;cartilage;tongue;urinary;blood;lens;skeletal muscle;macula lutea;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;peripheral nerve;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;muscle;pancreas;pia mater;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;thymus;cerebellum; whole brain; 0.14141 0.09669 -0.494039303 22.09247464 8.15331 0.30062 WDR17 7.02409304518169e-16 0.985064970221761 0.0149350297782385 WD repeat domain 17 . . . prostate;optic nerve;frontal lobe;islets of Langerhans;macula lutea;fovea centralis;choroid;lens;brain;skeletal muscle;retina; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12601 0.10488 1.526690916 95.49422033 6170.28249 16.41990 WDR18 0.901607559974541 0.0982157499839834 0.000176690041475398 WD repeat domain 18 FUNCTION: May play a role during development (By similarity). Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. {ECO:0000250, ECO:0000269|PubMed:22872859}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; lung;testis - seminiferous tubule;liver;tumor;white blood cells; 0.10939 0.10840 -0.001743238 53.85114414 2052.48581 8.34958 WDR19 1.73111340259862e-07 0.999985311585105 1.45153035553684e-05 WD repeat domain 19 FUNCTION: Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport. Involved in cilia function and/or assembly (By similarity). {ECO:0000250}.; DISEASE: Cranioectodermal dysplasia 4 (CED4) [MIM:614378]: A disorder primarily characterized by craniofacial, skeletal and ectodermal abnormalities. Clinical features include craniosynostosis, narrow rib cage, short limbs, brachydactyly, hypoplastic and widely spaced teeth, sparse hair, skin laxity and abnormal nails. Nephronophthisis leading to progressive renal failure, hepatic fibrosis, heart defects, and retinitis pigmentosa have also been described. {ECO:0000269|PubMed:22019273}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Short-rib thoracic dysplasia 5 with or without polydactyly (SRTD5) [MIM:614376]: A form of short-rib thoracic dysplasia, a group of autosomal recessive ciliopathies that are characterized by a constricted thoracic cage, short ribs, shortened tubular bones, and a 'trident' appearance of the acetabular roof. Polydactyly is variably present. Non-skeletal involvement can include cleft lip/palate as well as anomalies of major organs such as the brain, eye, heart, kidneys, liver, pancreas, intestines, and genitalia. Some forms of the disease are lethal in the neonatal period due to respiratory insufficiency secondary to a severely restricted thoracic cage, whereas others are compatible with life. Disease spectrum encompasses Ellis-van Creveld syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-Saldino syndrome, and short rib-polydactyly syndrome. {ECO:0000269|PubMed:22019273}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Nephronophthisis 13 (NPHP13) [MIM:614377]: An autosomal recessive disorder resulting in end-stage renal disease. It is a progressive tubulo-interstitial kidney disorder histologically characterized by modifications of the tubules with thickening of the basement membrane, interstitial fibrosis and, in the advanced stages, medullary cysts. {ECO:0000269|PubMed:22019273}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Senior-Loken syndrome 8 (SLSN8) [MIM:616307]: A renal- retinal disorder characterized by progressive wasting of the filtering unit of the kidney (nephronophthisis), with or without medullary cystic renal disease, and progressive eye disease. Typically this disorder becomes apparent during the first year of life. {ECO:0000269|PubMed:23559409, ECO:0000269|PubMed:23683095}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Some isoforms are tissue-specific. Highly expressed in the prostate. Lower expression in the cerebellum, pituitary gland, fetal lung, and pancreas. In normal prostate, expressed in both basal and luminal epithelial cells. No expression detected in fibromuscular stromal cells, endothelial cells, or infiltrating lymphocytes. Uniformed expression in prostate adenocarcinoma cells. {ECO:0000269|PubMed:12906858}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;kidney; testis;pons; 0.43030 0.09725 0.560331224 81.70559094 859.6824 5.71745 WDR20 0.939272872591341 0.060675581306783 5.15461018756066e-05 WD repeat domain 20 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;head and neck;spleen;cervix;kidney;mammary gland;stomach; subthalamic nucleus;testis - interstitial;globus pallidus; 0.42512 0.29333 -0.424258538 25.56027365 70.14589 1.73854 WDR24 0.00470241623358303 0.988923570161332 0.00637401360508528 WD repeat domain 24 FUNCTION: As a component of the GATOR2 complex, inhibits GATOR1 complex, an inhibitor of the amino acid-sensing branch of the TORC1 pathway.; . . medulla oblongata;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.17124 0.10703 -0.461076406 23.66124086 1952.56454 8.13191 WDR25 0.0422261097836064 0.951707462466349 0.00606642775004403 WD repeat domain 25 . . TISSUE SPECIFICITY: Expressed in heart, muscle, testis, ovary, uterus and prostate. {ECO:0000269|PubMed:15587985}.; unclassifiable (Anatomical System);cartilage;ovary;tongue;muscle;colon;retina;uterus;whole body;lung;bone;placenta;visual apparatus;head and neck;cervix;germinal center;kidney;brain;thymus; caudate nucleus;trigeminal ganglion;skeletal muscle; 0.17238 0.09554 0.270087468 70.69473933 325.26772 3.83376 WDR26 0.99967739101451 0.000322608313534822 6.71955078731638e-10 WD repeat domain 26 FUNCTION: May be involved in MAPK pathways. {ECO:0000269|PubMed:15378603}.; . TISSUE SPECIFICITY: Broadly expressed, with highest levels in heart and skeletal muscle. {ECO:0000269|PubMed:15378603}.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach; fetal liver;testis - interstitial;testis; 0.94614 0.15588 -0.471992905 23.03609342 11.3945 0.41124 WDR27 2.39749911767589e-15 0.203041890452188 0.79695810954781 WD repeat domain 27 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;skin;skeletal muscle;uterus;whole body;lung;bone;placenta;alveolus;liver;testis;spleen;germinal center;cerebellum; . 0.17458 . 2.522764647 98.69072895 5105.71609 14.66548 WDR31 5.53967209469172e-06 0.670822001008774 0.329172459319131 WD repeat domain 31 . . . unclassifiable (Anatomical System);ovary;colon;parathyroid;fovea centralis;skeletal muscle;prostate;lung;placenta;macula lutea;visual apparatus;liver;testis;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.06476 0.07491 0.17280645 65.75843359 1514.07201 7.23592 WDR33 0.999997732823828 2.26717617158997e-06 2.62352524482375e-19 WD repeat domain 33 FUNCTION: Essential for both cleavage and polyadenylation of pre- mRNA 3' ends. {ECO:0000269|PubMed:19217410}.; . TISSUE SPECIFICITY: Most highly expressed in testis. {ECO:0000269|PubMed:11162572}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; pons;trigeminal ganglion; 0.17172 0.11281 -0.813834387 12.05472989 577.17958 4.87117 WDR34 3.69860491111848e-05 0.824117107300254 0.175845906650635 WD repeat domain 34 FUNCTION: Critical for ciliary functions, essential to normal development and survival, most probably as a previously unrecognized component of the mammalian dynein-motor-based intraflagellar transport (IFT) machinery. Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Inhibits the MAP3K7-induced NF-kappa-B activation pathway. Inhibits MAP3K7 phosphorylation at 'Thr-184' and 'Thr-187' upon Il-1 beta stimulation. {ECO:0000269|PubMed:19521662, ECO:0000269|PubMed:24183449}.; . TISSUE SPECIFICITY: Expressed in several cell lines (at protein level). {ECO:0000269|PubMed:19521662}.; . . 0.12330 0.10101 -0.664951379 15.91177164 77.35427 1.84828 WDR35 2.64838406754913e-16 0.945205043553835 0.0547949564461648 WD repeat domain 35 FUNCTION: Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport. Required for ciliogenesis. May promote CASP3 activation and TNF-stimulated apoptosis. {ECO:0000269|PubMed:20193664, ECO:0000269|PubMed:21473986}.; DISEASE: Cranioectodermal dysplasia 2 (CED2) [MIM:613610]: A disorder characterized by craniofacial, skeletal and ectodermal abnormalities. Clinical features include short stature, dolichocephaly, craniosynostosis, narrow thorax with pectus excavatum, short limbs, brachydactyly, joint laxity, narrow palpebral fissures, telecanthus with hypertelorism, low-set simple ears, everted lower lip, and short neck. Teeth abnormalities include widely spaced, hypoplastic and fused teeth. {ECO:0000269|PubMed:20817137}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Short-rib thoracic dysplasia 7 with or without polydactyly (SRTD7) [MIM:614091]: A form of short-rib thoracic dysplasia, a group of autosomal recessive ciliopathies that are characterized by a constricted thoracic cage, short ribs, shortened tubular bones, and a 'trident' appearance of the acetabular roof. Polydactyly is variably present. Non-skeletal involvement can include cleft lip/palate as well as anomalies of major organs such as the brain, eye, heart, kidneys, liver, pancreas, intestines, and genitalia. Some forms of the disease are lethal in the neonatal period due to respiratory insufficiency secondary to a severely restricted thoracic cage, whereas others are compatible with life. Disease spectrum encompasses Ellis-van Creveld syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-Saldino syndrome, and short rib-polydactyly syndrome. SRTD7 hallmarks are acromesomelic hypomineralization, campomelia, polysyndactyly, laterality defects, and cystic kidneys. {ECO:0000269|PubMed:21473986}. Note=The disease is caused by mutations affecting the gene represented in this entry. WDR35 mutations cause short rib-polydactyly syndrome through impaired cilia formation. Primary fibroblasts from SRTD7 patients lacking WDR35 fail to produce cilia (PubMed:21473986). {ECO:0000269|PubMed:21473986}.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;hypothalamus;spinal cord;lens;skeletal muscle;lung;placenta;macula lutea;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14354 0.10876 0.475790265 78.87473461 4168.69448 12.81874 WDR36 0.544023667237535 0.455976119464183 2.13298282543095e-07 WD repeat domain 36 FUNCTION: Involved in the nucleolar processing of SSU 18S rRNA. Involved in T-cell activation and highly coregulated with IL2. {ECO:0000269|PubMed:21051332}.; DISEASE: Glaucoma 1, open angle, G (GLC1G) [MIM:609887]: A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. {ECO:0000269|PubMed:15677485}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in heart, placenta, liver, skeletal muscle, kidney and pancreas. In ocular tissues, strong expression in iris, sclera, ciliary muscle, ciliary body, retina and optic nerve. {ECO:0000269|PubMed:15677485}.; . . 0.09951 0.14299 0.033039107 55.85633404 562.37119 4.81226 WDR37 0.996766802999974 0.00323315955479484 3.74452313988834e-08 WD repeat domain 37 . . . ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;urinary;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;mammary gland;stomach;peripheral nerve;cerebellum; superior cervical ganglion;medulla oblongata;subthalamic nucleus;prefrontal cortex;atrioventricular node;pons;cingulate cortex;parietal lobe;cerebellum; 0.16471 0.12561 -0.911109353 9.961075725 39.62638 1.16799 WDR38 0.000345295162872057 0.825284033708321 0.174370671128807 WD repeat domain 38 . . . . . 0.12748 0.10650 0.731244617 86.21137061 700.6834 5.26700 WDR41 2.51915134260848e-06 0.978777565735194 0.0212199151134636 WD repeat domain 41 . . . myocardium;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;blood;breast;bile duct;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; spinal cord;white blood cells; 0.46577 . 0.600782551 82.82613824 182.33978 2.93196 WDR43 0.998942440488972 0.0010575570570403 2.45398753429542e-09 WD repeat domain 43 . . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);islets of Langerhans;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;duodenum;alveolus;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;skeletal muscle; 0.42193 . -0.356299879 29.31115829 60.05789 1.57275 WDR44 0.999844185847999 0.000155814037885578 1.1411593076322e-10 WD repeat domain 44 FUNCTION: Downstream effector for RAB11. May be involved in vesicle recycling (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;larynx;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);heart;tongue;blood;skeletal muscle;breast;pancreas;lung;liver;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;medulla oblongata;ciliary ganglion;atrioventricular node; 0.91619 0.10042 -0.159704656 41.90846898 71.35705 1.75847 WDR45 0.965710816064405 0.0342284845791244 6.0699356470835e-05 WD repeat domain 45 FUNCTION: Plays an important role in the autophagy pathway, which is the major intracellular degradation system by which cytoplasmic materials are packaged into autophagosomes and delivered to lysosomes for degradation. {ECO:0000269|PubMed:23435086}.; . TISSUE SPECIFICITY: Ubiquitously expressed, with high expression in skeletal muscle and heart. Weakly expressed in liver and placenta. Expression is down-regulated in pancreatic and in kidney tumors. {ECO:0000269|PubMed:15602573}.; myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;pons;atrioventricular node;skeletal muscle;skin;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.27372 0.11262 -0.273576253 33.97027601 52.89519 1.44298 WDR45B 0.637042299010321 0.362670682130609 0.000287018859070886 WD repeat domain 45B . . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in heart, skeletal muscle and pancreas. Up-regulated in a variety of tumor tissues including ovarian and uterine cancers. {ECO:0000269|PubMed:15602573}.; . . 0.32364 0.11809 -0.247889024 35.98726115 126.62382 2.45181 WDR45BP1 . . . WD repeat domain 45B pseudogene 1 . . . . . . . . . . . WDR46 8.42034553335386e-06 0.999193235098312 0.000798344556154423 WD repeat domain 46 FUNCTION: Scaffold component of the nucleolar structure. Required for localization of DDX21 and NCL to the granular compartment of the nucleolus. {ECO:0000269|PubMed:23848194}.; . . . . 0.12353 . -0.091746757 46.91554612 1573.09748 7.34178 WDR47 0.90566161819711 0.0943381150141632 2.6678872694155e-07 WD repeat domain 47 . . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;skin;uterus;prostate;optic nerve;frontal lobe;cochlea;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;kidney;stomach; amygdala;whole brain;superior cervical ganglion;medulla oblongata;thalamus;occipital lobe;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;parietal lobe;cingulate cortex; 0.62490 0.10882 -0.756778259 13.44656759 150.69863 2.68072 WDR48 0.999805648456572 0.000194351535422872 8.00473919427935e-12 WD repeat domain 48 FUNCTION: Regulator of deubiquitinating complexes. Acts as a strong activator of USP1 by enhancing the USP1-mediated deubiquitination of FANCD2; USP1 being almost inactive by itself. Also activates deubiquitinating activity of complexes containing USP12 and USP46, respectively. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate. In case of infection by Herpesvirus saimiri, may play a role in vesicular transport or membrane fusion events necessary for transport to lysosomes. Induces lysosomal vesicle formation via interaction with Herpesvirus saimiri tyrosine kinase-interacting protein (TIP). Subsequently, TIP recruits tyrosine-protein kinase LCK, resulting in down-regulation of T-cell antigen receptor TCR. May play a role in generation of enlarged endosomal vesicles via interaction with TIP. In case of infection by papillomavirus HPV11, promotes the maintenance of the viral genome via its interaction with HPV11 helicase E1. {ECO:0000269|PubMed:12196293, ECO:0000269|PubMed:18082604, ECO:0000269|PubMed:19075014}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12196293}.; medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;bladder;brain;gall bladder;tonsil;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;kidney;stomach;thymus; superior cervical ganglion;medulla oblongata;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe; 0.47008 0.17050 -0.47017169 23.25430526 25.44253 0.83098 WDR49 2.29866609656679e-12 0.224434240593737 0.775565759403964 WD repeat domain 49 . . . unclassifiable (Anatomical System);lung;placenta;brain;bone marrow; dorsal root ganglion;atrioventricular node;trigeminal ganglion; 0.08676 . 0.336225928 73.67893371 2453.98868 9.21738 WDR53 0.000341188959787833 0.598629171082624 0.401029639957588 WD repeat domain 53 . . . unclassifiable (Anatomical System);medulla oblongata;heart;ovary;colon;parathyroid;blood;bone marrow;breast;uterus;lung;endometrium;bone;placenta;testis;cervix;germinal center;bladder;stomach; . 0.20414 0.10766 -0.181750739 40.15687662 84.97837 1.96364 WDR54 2.39788118448388e-06 0.728777151206691 0.271220450912124 WD repeat domain 54 . . . smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;endometrium;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;muscle;lens;bile duct;lung;nasopharynx;placenta;macula lutea;hippocampus;visual apparatus;liver;kidney;stomach; . 0.14972 . 0.196671391 67.19155461 107.06726 2.24514 WDR55 1.48298652018262e-06 0.395826290799672 0.604172226213808 WD repeat domain 55 FUNCTION: Nucleolar protein that acts as a modulator of rRNA synthesis. Plays a central role during organogenesis (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;nervous;colon;blood;skin;skeletal muscle;uterus;pancreas;optic nerve;bone;placenta;visual apparatus;iris;duodenum;liver;testis;cervix;spleen;kidney;brain;mammary gland;bladder;stomach; dorsal root ganglion;superior cervical ganglion;uterus corpus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.03875 0.10824 0.463046108 78.58575136 2218.27221 8.67260 WDR59 3.44164260304723e-11 0.995036935074405 0.00496306489117817 WD repeat domain 59 FUNCTION: As a component of the GATOR2 complex, inhibits GATOR1 complex, an inhibitor of the amino acid-sensing branch of the TORC1 pathway.; . . ovary;adrenal medulla;colon;fovea centralis;choroid;retina;optic nerve;whole body;larynx;bone;testis;brain;unclassifiable (Anatomical System);amygdala;islets of Langerhans;hypothalamus;lens;skeletal muscle;greater omentum;pancreas;lung;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.21989 0.10981 -1.256630467 5.343241331 409.53463 4.24211 WDR60 2.00913621845281e-07 0.999713723240379 0.000286075845998976 WD repeat domain 60 FUNCTION: May play a role in ciliogenesis. {ECO:0000269|PubMed:23910462}.; . TISSUE SPECIFICITY: Expressed in chondrocytes (at protein level). {ECO:0000269|PubMed:23910462}.; . . 0.11153 0.09221 1.208829905 93.05260675 1693.42646 7.58443 WDR61 0.0897745791618097 0.901333919046713 0.00889150179147726 WD repeat domain 61 FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non- phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3), dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1C. {ECO:0000269|PubMed:16024656, ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742}.; . . myocardium;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;uterus;prostate;endometrium;larynx;bone;testis;dura mater;germinal center;brain;bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;pancreas;pia mater;lung;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; testis;ciliary ganglion;atrioventricular node;cingulate cortex; 0.42204 0.13458 -0.427900189 25.14744043 5.82137 0.21952 WDR62 3.70153772737001e-13 0.994431561780598 0.00556843821903238 WD repeat domain 62 FUNCTION: Required for cerebral cortical development. Plays a role in neuronal proliferation and migration (PubMed:20890278, PubMed:20729831). Plays a role in mother-centriole-dependent centriole duplication; the function seems also to involve CEP152, CDK5RAP2 and CEP63 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (PubMed:26297806). {ECO:0000269|PubMed:20729831, ECO:0000269|PubMed:20890278, ECO:0000269|PubMed:26297806}.; . TISSUE SPECIFICITY: Present in fetal brain, enriched within the ventricular and subventricular zone (at protein level). In the embryonic brain it is expressed in mitotic neural precursor cells. {ECO:0000269|PubMed:20890279}.; unclassifiable (Anatomical System);medulla oblongata;ovary;colon;blood;fovea centralis;choroid;lens;skin;retina;bone marrow;uterus;prostate;optic nerve;lung;bone;macula lutea;visual apparatus;testis;spleen;germinal center;brain;thymus; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.44098 . 0.576763804 82.17740033 516.14972 4.64667 WDR63 0.000118222164733869 0.999863769461126 1.80083741400569e-05 WD repeat domain 63 . . . unclassifiable (Anatomical System);uterus;medulla oblongata;whole body;endometrium;nasopharynx;testis;skeletal muscle; . 0.09728 . -0.685180376 15.32200991 1656.32192 7.52248 WDR64 4.9048627570315e-15 0.0881243108827383 0.911875689117257 WD repeat domain 64 . . . . . 0.23607 . . . 2400.46113 9.09307 WDR66 1.2516451688474e-10 0.981629339063931 0.0183706608109044 WD repeat domain 66 . . . unclassifiable (Anatomical System);meninges;islets of Langerhans;colon;blood;skin;pia mater;lung;nasopharynx;placenta;bone;hypopharynx;testis;head and neck;dura mater;kidney; testis - interstitial;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node; 0.16334 . 1.409099734 94.8041991 10305.45886 22.15777 WDR70 0.802235272890051 0.197764337258602 3.89851347841075e-07 WD repeat domain 70 . . . lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;vein;skin;prostate;cerebral cortex;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;pharynx;blood;bile duct;breast;lung;cornea;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; ciliary ganglion;skeletal muscle; 0.22255 0.10057 -0.890882376 10.30313753 29.56978 0.94458 WDR72 1.62243924822237e-16 0.157680540338534 0.842319459661466 WD repeat domain 72 . DISEASE: Amelogenesis imperfecta, hypomaturation type, 2A3 (AI2A3) [MIM:613211]: A defect of enamel formation. The disorder involves both primary and secondary dentitions. The teeth have a shiny agar jelly appearance and the enamel is softer than normal. Brown pigment is present in middle layers of enamel. {ECO:0000269|PubMed:19853237}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);colon;uterus;pancreas;lung;endometrium;larynx;liver;testis;head and neck;kidney;bladder;stomach;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04985 0.08744 -0.014692675 52.35314933 8181.73271 19.52868 WDR73 7.90217939379774e-06 0.506729756446044 0.493262341374562 WD repeat domain 73 FUNCTION: May play a role in the regulation of microtubule organization and dynamics (PubMed:25466283). {ECO:0000269|PubMed:25466283}.; DISEASE: Galloway-Mowat syndrome (GAMOS) [MIM:251300]: A rare, autosomal recessive disease with onset in infancy, and characterized by microcephaly, central nervous system abnormalities resulting in severe neurological impairment and intellectual disability, and nephrotic syndrome. Most patients develop seizures and nephrotic syndrome late in childhood. Note=The disease is caused by mutations affecting the gene represented in this entry. {ECO:0000269|PubMed:25466283}.; TISSUE SPECIFICITY: Expressed in kidney and brain. In the kidney, expressed in glomeruli, most probably in podocytes, and in tubules (at protein level). In the brain, expressed in the cerebellum, with high levels in Purkinje cells and their projecting axons, in the deep cerebellar nuclei and in pyramidal neurons of the cerebral cortex (at protein level). In the white matter, mainly present in astrocytes, but not in oligodendrocytes (at protein level). Also highly expressed in endothelial cells of cerebral capillaries (at protein level). {ECO:0000269|PubMed:25466283}.; . . 0.10358 . 0.463046108 78.58575136 2164.97296 8.56277 WDR74 2.46017425068892e-08 0.272794303823723 0.727205671574535 WD repeat domain 74 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;whole body;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;muscle;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.25893 0.10353 -0.247889024 35.98726115 322.57379 3.81341 WDR75 0.566494633877436 0.433504486706807 8.79415757261183e-07 WD repeat domain 75 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;skeletal muscle; 0.42701 0.10537 -1.219785504 5.602736494 110.68114 2.29156 WDR76 0.00230519074795657 0.996954003731795 0.000740805520248048 WD repeat domain 76 FUNCTION: Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymphoreticular;cartilage;islets of Langerhans;colon;skin;skeletal muscle;bone marrow;uterus;prostate;lung;bone;thyroid;visual apparatus;liver;testis;cervix;head and neck;spleen;germinal center;brain;artery;aorta; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.61850 0.09316 0.042348793 57.31304553 146.83397 2.63934 WDR77 0.0157265712626212 0.9587672237661 0.0255062049712787 WD repeat domain 77 FUNCTION: Non-catalytic component of the 20S PRMT5-containing methyltransferase complex, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones. This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. Might play a role in transcription regulation. The 20S PRMT5-containing methyltransferase complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. {ECO:0000269|PubMed:11756452, ECO:0000269|PubMed:23071334}.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, spleen, testis, uterus, prostate and thymus. In testis, expressed in germ cells and Leydig cells, but not in peritubular myocytes, nor in Sertoli cells. Expressed in prostate cancers, in seminomas and in Leydig cell tumors. {ECO:0000269|PubMed:12972618, ECO:0000269|PubMed:17437848}.; lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pineal body;urinary;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;head and neck;kidney;stomach;thymus; . 0.13032 0.41656 -0.205617011 38.57631517 15.19158 0.54661 WDR78 7.87925768320976e-11 0.965691340274725 0.0343086596464821 WD repeat domain 78 . . . . . 0.10903 0.08227 1.137205722 92.32719981 253.58576 3.42618 WDR81 1.26010739829094e-05 0.997783337112071 0.00220406181394587 WD repeat domain 81 FUNCTION: Seems to have a role in maintenance of normal mitochondrial structure and organization. Promotes Purkinje and photoreceptor cell survival. {ECO:0000250|UniProtKB:Q5ND34}.; . TISSUE SPECIFICITY: Widely expressed. In the brain, highest levels in cerebellum and corpus callosum. {ECO:0000269|PubMed:21885617}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;tongue;colon;parathyroid;blood;skin;uterus;lung;endometrium;placenta;iris;liver;testis;cervix;head and neck;spleen;germinal center;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;caudate nucleus;cingulate cortex; 0.26554 . -1.758449269 2.335456476 3904.13594 12.33658 WDR82 0.923062143793669 0.076843893228579 9.39629777523558e-05 WD repeat domain 82 FUNCTION: Regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes. Facilitates histone H3 'Lys-4' methylation via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A). Component of PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. {ECO:0000269|PubMed:17998332, ECO:0000269|PubMed:18838538, ECO:0000269|PubMed:20516061}.; . . smooth muscle;ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;small intestine;tongue;islets of Langerhans;oral cavity;muscle;blood;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; amygdala;whole brain;subthalamic nucleus;superior cervical ganglion;occipital lobe;fetal brain;prefrontal cortex;whole blood;cingulate cortex;cerebellum; 0.64619 0.12971 -0.031067188 51.03798066 1.24663 0.04374 WDR82P1 . . . WD repeat domain 82 pseudogene 1 FUNCTION: Regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes. Facilitates histone H3 'Lys-4' methylation via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A). Component of PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. {ECO:0000269|PubMed:17998332, ECO:0000269|PubMed:18838538, ECO:0000269|PubMed:20516061}.; . . . . 0.64619 0.12971 -0.031067188 51.03798066 . . WDR82P2 . . . WD repeat domain 82 pseudogene 2 . . . . . . . . . . . WDR83 8.21261876456272e-07 0.498677658188908 0.501321520549215 WD repeat domain 83 FUNCTION: Molecular scaffold protein for various multimeric protein complexes. Acts as a module in the assembly of a multicomponent scaffold for the ERK pathway, linking ERK responses to specific agonists. At low concentrations it enhances ERK activation, whereas high concentrations lead to the inhibition of ERK activation. Also involved in response to hypoxia by acting as a negative regulator of HIF1A/HIF-1-alpha via its interaction with EGLN3/PHD3. May promote degradation of HIF1A. May act by recruiting signaling complexes to a specific upstream activator (By similarity). May also be involved in pre-mRNA splicing. {ECO:0000250}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;lens;skeletal muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; atrioventricular node;trigeminal ganglion; . . -0.291981272 33.20358575 66.49509 1.67930 WDR83OS 0.0017668610956485 0.474311623002875 0.523921515901476 WD repeat domain 83 opposite strand . . . lymphoreticular;myocardium;umbilical cord;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;bone;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;kidney;mammary gland;aorta;stomach; heart; 0.14270 0.11809 0.169169615 65.33380514 0.81759 0.01557 WDR86 3.30809403776567e-11 0.00629404719371479 0.993705952773204 WD repeat domain 86 . . . unclassifiable (Anatomical System);heart;tongue;parathyroid;fovea centralis;choroid;lens;retina;pancreas;optic nerve;lung;endometrium;placenta;macula lutea;liver;spleen;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.10185 0.09972 . . 1276.1914 6.72544 WDR86-AS1 . . . WDR86 antisense RNA 1 . . . . . . . . . . . WDR87 . . . WD repeat domain 87 . . . . . 0.06224 . 4.142836195 99.6933239 2359.54264 9.01627 WDR88 3.2982521257479e-08 0.316169179245835 0.683830787771644 WD repeat domain 88 . . . unclassifiable (Anatomical System);medulla oblongata;testis; superior cervical ganglion;testis - interstitial;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06047 . 0.575097644 82.1656051 785.31961 5.53575 WDR89 0.0001980885726453 0.721072008018811 0.278729903408544 WD repeat domain 89 . . . unclassifiable (Anatomical System);lymph node;islets of Langerhans;colon;skeletal muscle;uterus;larynx;adrenal gland;thyroid;liver;head and neck;kidney;brain;bladder; dorsal root ganglion;testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.26054 0.09621 -0.538132194 20.26421326 14.52952 0.52250 WDR90 4.01805540497848e-46 1.07695011349369e-08 0.999999989230499 WD repeat domain 90 . . . medulla oblongata;ovary;sympathetic chain;colon;skin;retina;uterus;optic nerve;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;head and neck;spleen;kidney;stomach;peripheral nerve;thymus; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12488 . 0.973706547 90.28072659 5541.15698 15.39276 WDR91 0.00140853962093613 0.998286399544944 0.000305060834120152 WD repeat domain 91 . . . lymphoreticular;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;thyroid;bone;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;tongue;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;visual apparatus;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;trigeminal ganglion; 0.25556 0.09342 -1.282303301 5.130927105 79.59426 1.88548 WDR92 0.805659459340733 0.194119638479093 0.000220902180174557 WD repeat domain 92 FUNCTION: Seems to act as a modulator of apoptosis. {ECO:0000269|PubMed:16487927}.; . TISSUE SPECIFICITY: Widely expressed with the highest expression in testis. {ECO:0000269|PubMed:16487927}.; unclassifiable (Anatomical System);lymph node;ovary;salivary gland;adrenal cortex;pharynx;colon;blood;skin;breast;uterus;prostate;lung;cerebral cortex;nasopharynx;placenta;visual apparatus;liver;germinal center;kidney;brain;mammary gland;bladder;tonsil;stomach; . . . 0.084621747 60.31493277 1268.45257 6.71084 WDR93 6.27428968004137e-15 0.0536864985165717 0.946313501483422 WD repeat domain 93 . . . unclassifiable (Anatomical System);lung;testis;spleen;kidney;pineal gland; . 0.05198 . 1.758248793 96.72682236 2617.94146 9.58684 WDR95P . . . WD repeat domain 95, pseudogene . . . . . . . . . . . WDR97 . . . WD repeat domain 97 . . . . . 0.13195 0.09824 . . . . WDSUB1 1.37628007456398e-06 0.609907467007598 0.390091156712327 WD repeat, sterile alpha motif and U-box domain containing 1 . . . ovary;colon;parathyroid;fovea centralis;skin;uterus;prostate;thyroid;pituitary gland;testis;brain;pineal gland;unclassifiable (Anatomical System);adrenal cortex;blood;pancreas;lung;adrenal gland;placenta;macula lutea;liver;spleen;kidney;stomach;aorta; . 0.34775 0.20974 0.132352165 63.48785091 5889.69211 15.89756 WDTC1 0.99930782583365 0.000692173292906269 8.73444030579118e-10 WD and tetratricopeptide repeats 1 FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16964240}.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;colon;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach;thymus; superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.98674 0.14896 -0.44448505 24.46331682 58.41954 1.54858 WDYHV1 0.000384004659787212 0.624482275375166 0.375133719965047 WDYHV motif containing 1 FUNCTION: Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N- terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C- terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine (By similarity). {ECO:0000250}.; . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;thyroid;bone;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;adrenal cortex;lens;bile duct;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;atrioventricular node; 0.04347 0.13283 0.859896574 88.62349611 11714.77662 23.37082 WEE1 0.997105770017131 0.00289420140531464 2.85775542538747e-08 WEE1 G2 checkpoint kinase FUNCTION: Acts as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDK1 before the onset of mitosis by mediating phosphorylation of CDK1 on 'Tyr-15'. Specifically phosphorylates and inactivates cyclin B1-complexed CDK1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-CDK1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDK1 does not occur. Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated. A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation.; . . sympathetic chain;skin;bone marrow;uterus;prostate;atrium;larynx;thyroid;bone;bladder;brain;gall bladder;unclassifiable (Anatomical System);heart;blood;bile duct;breast;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;head and neck;cervix;mammary gland;stomach; dorsal root ganglion;uterus;testis - interstitial;superior cervical ganglion;fetal liver;testis - seminiferous tubule;placenta;tumor;appendix;testis;trigeminal ganglion; 0.54482 0.24267 0.503505267 79.88912479 161.53498 2.77729 WEE2 0.000967997099215928 0.986625105925887 0.0124068969748969 WEE1 homolog 2 (S. pombe) FUNCTION: Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1 and acts as a key regulator of meiosis during both prophase I and metaphase II. Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphorylating CDK1 at 'Tyr-15', leading to inhibit CDK1 activity and prevent meiotic reentry. Also required for metaphase II exit during egg activation by phosphorylating CDK1 at 'Tyr-15', to ensure exit from meiosis in oocytes and promote pronuclear formation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:11029659}.; . . 0.07114 . -0.600630256 18.06440198 105.67521 2.22768 WEE2-AS1 . . . WEE2 antisense RNA 1 . . . . . . . . . . . WFDC1 2.97211981376766e-06 0.32405442363917 0.675942604241017 WAP four-disulfide core domain 1 FUNCTION: Has growth inhibitory activity. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;hypothalamus;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;lung;bone;placenta;macula lutea;visual apparatus;liver;testis;spleen;kidney;brain;stomach; prostate;cerebellum peduncles;adrenal gland;placenta;testis;parietal lobe;cerebellum; 0.11133 0.15618 1.750970652 96.67374381 292.24692 3.65651 WFDC2 0.634143544716743 0.336747473878709 0.0291089814045487 WAP four-disulfide core domain 2 FUNCTION: Broad range protease inhibitor. {ECO:0000269|PubMed:23139753}.; . TISSUE SPECIFICITY: Expressed in a number of normal tissues, including male reproductive system, regions of the respiratory tract and nasopharynx. Highly expressed in a number of tumors cells lines, such ovarian, colon, breast, lung and renal cells lines. Initially described as being exclusively transcribed in the epididymis. {ECO:0000269|PubMed:15781627}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;thyroid;iris;pituitary gland;testis;amniotic fluid;pineal gland;brain;unclassifiable (Anatomical System);trophoblast;heart;lens;breast;lung;adrenal gland;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;head and neck;cervix;kidney;mammary gland;stomach; . 0.48430 0.17603 -0.075159878 47.78839349 2.37906 0.08091 WFDC3 0.019237531618368 0.899881797653325 0.0808806707283074 WAP four-disulfide core domain 3 . . TISSUE SPECIFICITY: Ubiquitously expressed.; unclassifiable (Anatomical System);optic nerve;lung;macula lutea;testis;colon;fovea centralis;choroid;kidney;lens;retina; . 0.12948 0.09080 0.949904335 90.00943619 210.92275 3.13281 WFDC5 5.6017444083725e-05 0.264671244293282 0.735272738262634 WAP four-disulfide core domain 5 FUNCTION: Putative acid-stable proteinase inhibitor.; . . uterus;lung;heart;tongue;hypopharynx;testis;colon;head and neck;skin; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;skin; 0.08446 0.10359 0.347360312 73.97381458 487.00374 4.54241 WFDC6 0.054913983307631 0.704081335956872 0.241004680735497 WAP four-disulfide core domain 6 . . TISSUE SPECIFICITY: Ubiquitously expressed, but the highest levels are found in epididymis, testis and trachea.; . . . 0.09006 -0.075159878 47.78839349 51.25468 1.41182 WFDC8 4.97250859518292e-06 0.413931997015041 0.586063030476364 WAP four-disulfide core domain 8 . . TISSUE SPECIFICITY: Expressed ubiquitously, the highest levels are found in the epididymis followed by testis and trachea.; lung;testis; dorsal root ganglion;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.06419 0.06787 0.72761005 86.08162302 287.13901 3.63082 WFDC9 0.0108113463900981 0.620087629590079 0.369101024019823 WAP four-disulfide core domain 9 . . . lung;testis; . 0.02616 . 0.72397987 85.91648974 6.95658 0.25917 WFDC10A 0.27466328624647 0.633912251355602 0.091424462397928 WAP four-disulfide core domain 10A . . . . . 0.06203 . 0.125076652 62.7388535 25.50358 0.83206 WFDC10B 0.0148433867661418 0.685845491612179 0.299311121621679 WAP four-disulfide core domain 10B . . TISSUE SPECIFICITY: Ubiquitously expressed.; brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.04470 . 0.391453969 75.87284737 5.45063 0.20273 WFDC11 0.00335013836988599 0.610300295533238 0.386349566096876 WAP four-disulfide core domain 11 . . . heart;testis;colon;brain; . 0.07534 . 0.323496558 72.93583392 1.1661 0.03277 WFDC12 0.0568531699708981 0.709519282853605 0.233627547175497 WAP four-disulfide core domain 12 FUNCTION: Antibacterial protein. Putative acid-stable proteinase inhibitor.; . TISSUE SPECIFICITY: Highly expressed in prostate, skin, lung and esophagus. Weakly expressed in skeletal muscle, epididymis, kidney, trachea, salivary gland, testis and seminal vesicle.; . . 0.06533 0.07027 0.347360312 73.97381458 25.32775 0.82802 WFDC13 0.252946356503913 0.641232731255988 0.1058209122401 WAP four-disulfide core domain 13 FUNCTION: Putative acid-stable proteinase inhibitor. {ECO:0000250}.; . . . . 0.01377 0.04409 0.235309407 68.71903751 2.03335 0.06646 WFDC21P . . . WAP four-disulfide core domain 21, pseudogene . . . . . . . . . . . WFIKKN1 4.90281884604666e-08 0.0635091168601837 0.936490834111628 WAP, follistatin/kazal, immunoglobulin, kunitz and netrin domain containing 1 FUNCTION: Protease-inhibitor that contains multiple distinct protease inhibitor domains. Probably has serine protease- and metalloprotease-inhibitor activity (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in pancreas, kidney, liver, placenta, and lung.; unclassifiable (Anatomical System);lung;cervix; . 0.17118 0.12631 . . 109.9305 2.27766 WFIKKN2 0.025878487775655 0.9185729833732 0.0555485288511447 WAP, follistatin/kazal, immunoglobulin, kunitz and netrin domain containing 2 FUNCTION: Protease-inhibitor that contains multiple distinct protease inhibitor domains. Probably has serine protease- and metalloprotease-inhibitor activity. Inhibits the biological activity of mature myostatin, but not activin (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Primarily expressed in ovary, testis and brain, but not in liver. In fetal tissues, it is primarily expressed in brain, skeletal muscle, thymus and kidney. {ECO:0000269|PubMed:11928817}.; unclassifiable (Anatomical System);lung;pineal body;iris;testis;colon;brain;skeletal muscle;stomach;retina; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.51037 0.10999 -0.617221851 17.44515216 757.02746 5.45313 WFS1 . . . wolframin ER transmembrane glycoprotein FUNCTION: Participates in the regulation of cellular Ca(2+) homeostasis, at least partly, by modulating the filling state of the endoplasmic reticulum Ca(2+) store. {ECO:0000269|PubMed:16989814}.; DISEASE: Wolfram syndrome 1 (WFS1) [MIM:222300]: A rare disorder characterized by juvenile-onset insulin-dependent diabetes mellitus with optic atrophy. Other manifestations include diabetes insipidus, sensorineural deafness, dementia, psychiatric illnesses. {ECO:0000269|PubMed:10521293, ECO:0000269|PubMed:11161832, ECO:0000269|PubMed:11295831, ECO:0000269|PubMed:15605410, ECO:0000269|PubMed:21538838, ECO:0000269|PubMed:22226368, ECO:0000269|PubMed:9771706, ECO:0000269|PubMed:9817917}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Deafness, autosomal dominant, 6 (DFNA6) [MIM:600965]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA6 is a low-frequency hearing loss in which frequencies of 2000 Hz and below are predominantly affected. Many patients have tinnitus, but there are otherwise no associated features such as vertigo. Because high-frequency hearing is generally preserved, patients retain excellent understanding of speech, although presbycusis or noise exposure may cause high-frequency loss later in life. DFNA6 worsens over time without progressing to profound deafness. {ECO:0000269|PubMed:11709537, ECO:0000269|PubMed:11709538, ECO:0000269|PubMed:12181639, ECO:0000269|PubMed:17517145, ECO:0000269|PubMed:18518985, ECO:0000269|PubMed:18688868, ECO:0000269|PubMed:21356526, ECO:0000269|PubMed:24462758}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Wolfram-like syndrome autosomal dominant (WFSL) [MIM:614296]: A disease characterized by the clinical triad of congenital progressive hearing impairment, diabetes mellitus, and optic atrophy. The hearing impairment, which is usually diagnosed in the first decade of life, is relatively constant and alters mainly low- and middle-frequency ranges. {ECO:0000269|PubMed:16648378, ECO:0000269|PubMed:20069065, ECO:0000269|PubMed:21538838}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cataract 41 (CTRCT41) [MIM:116400]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. {ECO:0000269|PubMed:23531866}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in heart followed by brain, placenta, lung and pancreas. Weakly expressed in liver, kidney and skeletal muscle. Also expressed in islet and beta-cell insulinoma cell line.; ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;urinary;adrenal cortex;lens;skeletal muscle;breast;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion; 0.14612 0.10979 -0.097660938 45.68884171 5200.66104 14.84466 WHAMM 1.0362469004489e-05 0.796492477368621 0.203497160162374 WAS protein homolog associated with actin, golgi membranes and microtubules FUNCTION: Acts as a nucleation-promoting factor (NPF) that stimulates Arp2/3-mediated actin polymerization both at the Golgi apparatus and along tubular membranes. Its activity in membrane tubulation requires F-actin and interaction with microtubules. Proposed to use coordinated actin-nucleating and microtubule- binding activities of distinct WHAMM molecules to drive membrane tubule elongation; when MT-bound can recruit and remodel membrane vesicles but is prevented to activate the Arp2/3 complex. Involved as a regulator of Golgi positioning and morphology. Participates in vesicle transport between the reticulum endoplasmic and the Golgi complex. Required for RhoD-dependent actin reorganization such as in cell adhesion and cell migration. {ECO:0000269|PubMed:18614018, ECO:0000269|PubMed:23027905, ECO:0000269|PubMed:23087206}.; . TISSUE SPECIFICITY: Expressed in brain, lung, heart, colon and kidney (at protein level).; ovary;colon;parathyroid;skin;retina;uterus;prostate;optic nerve;whole body;larynx;bone;thyroid;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;muscle;pancreas;lung;placenta;liver;head and neck;spleen;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;skeletal muscle; . 0.09497 0.334405942 73.64944562 2483.65048 9.29785 WHAMMP1 . . . WAS protein homolog associated with actin, golgi membranes and microtubules pseudogene 1 . . . . . . . . . . . WHAMMP2 . . . WAS protein homolog associated with actin, golgi membranes and microtubules pseudogene 2 . . . . . . . . . . . WHAMMP3 . . . WAS protein homolog associated with actin, golgi membranes and microtubules pseudogene 3 . . . prostate;lung;testis;colon; dorsal root ganglion;testis - interstitial;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.09497 . . . . WHCR . . . Wolf-Hirschhorn syndrome chromosome region . . . . . . . . . . . WHSC1 0.999999325434983 6.74565016345942e-07 4.03699007255195e-17 Wolf-Hirschhorn syndrome candidate 1 FUNCTION: Histone methyltransferase with histone H3 'Lys-27' (H3K27me) methyltransferase activity. Isoform RE-IIBP may act as a transcription regulator that binds DNA and suppresses IL5 transcription through HDAC recruitment. {ECO:0000269|PubMed:11152655, ECO:0000269|PubMed:16115125, ECO:0000269|PubMed:18172012}.; DISEASE: Note=WHSC1 is located in the Wolf-Hirschhorn syndrome (WHS) critical region. WHS results from by sub-telomeric deletions in the short arm of chromosome 4. WHSC1 is deleted in every case, however deletion of linked genes contributes to both the severity of the core characteristics and the presence of the additional syndromic problems.; TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9618163}.; medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;bladder;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;cervix;spleen;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;oesophagus;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;thymus;cerebellum; superior cervical ganglion;fetal liver;testis - interstitial;testis;parietal lobe;skeletal muscle;thymus; 0.40745 . -1.368693559 4.482189196 67.23319 1.69666 WHSC1L1 0.999999688469196 3.11530804134377e-07 1.24414958026185e-18 Wolf-Hirschhorn syndrome candidate 1-like 1 FUNCTION: Histone methyltransferase. Preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression. {ECO:0000269|PubMed:16682010}.; DISEASE: Note=A chromosomal aberration involving WHSC1L1 is found in childhood acute myeloid leukemia. Translocation t(8;11)(p11.2;p15) with NUP98.; TISSUE SPECIFICITY: Highly expressed in brain, heart and skeletal muscle. Expressed at lower level in liver and lung. {ECO:0000269|PubMed:11374904}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;thalamus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.41929 0.09983 -0.551080959 19.93394669 249.03448 3.39987 WHSC1L2P . . . Wolf-Hirschhorn syndrome candidate 1-like 2, pseudogene . . . . . . . . . . . WIF1 2.41723210239144e-05 0.915347468752114 0.0846283589268619 WNT inhibitory factor 1 FUNCTION: Binds to WNT proteins and inhibits their activities. May be involved in mesoderm segmentation.; . . unclassifiable (Anatomical System);heart;cartilage;hypothalamus;pineal body;fovea centralis;skeletal muscle;skin;retina;uterus;optic nerve;lung;endometrium;synovium;trabecular meshwork;thyroid;bone;macula lutea;hippocampus;testis;brain; amygdala;whole brain;medulla oblongata;occipital lobe;temporal lobe;fetal lung;caudate nucleus;pons;skeletal muscle;parietal lobe;pituitary; 0.79865 0.22202 -0.315847836 31.68789809 74.46405 1.80398 WIPF1 0.944313925016733 0.0556446469876354 4.14279956314652e-05 WAS/WASL interacting protein family member 1 FUNCTION: Plays a role in the reorganization of the actin cytoskeleton. Contributes with NCK1 and GRB2 in the recruitment and activation of WASL. May participate in regulating the subcellular localization of WASL, resulting in the disassembly of stress fibers in favor of filopodia formation. Plays a role in the formation of cell ruffles (By similarity). Plays an important role in the intracellular motility of vaccinia virus by functioning as an adapter for recruiting WASL to vaccinia virus. {ECO:0000250, ECO:0000269|PubMed:10878810, ECO:0000269|PubMed:19910490, ECO:0000269|PubMed:9405671}.; DISEASE: Wiskott-Aldrich syndrome 2 (WAS2) [MIM:614493]: An immunodeficiency disorder characterized by eczema, thrombocytopenia, recurrent infections, defective T-cell proliferation, and impaired natural killer cell function. {ECO:0000269|PubMed:22231303}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in peripheral blood mononuclear cells, spleen, placenta, small intestine, colon and thymus. Lower expression in ovary, heart, brain, lung, liver, skeletal muscle, kidney, pancreas, prostate and testis. {ECO:0000269|PubMed:9405671}.; smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;brain;tonsil;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;oesophagus;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;hypothalamus;bile duct;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;spinal cord;white blood cells;atrioventricular node;trigeminal ganglion;whole blood;skeletal muscle; 0.71825 0.15250 -0.600630256 18.06440198 30.43509 0.96977 WIPF2 0.366730469469022 0.632771600857256 0.000497929673721859 WAS/WASL interacting protein family member 2 FUNCTION: Plays an active role in the formation of cell surface protrusions downstream of activated PDGFB receptors. Plays an important role in actin-microspike formation through cooperation with WASL. May cooperate with WASP and WASL to induce mobilization and reorganization of the actin filament system. {ECO:0000269|PubMed:11829459, ECO:0000269|PubMed:12213210}.; . TISSUE SPECIFICITY: Expressed mainly in brain, colon, lung and stomach (at protein level). Ubiquitously expressed, with high expression in brain, kidney, lung, and placenta. {ECO:0000269|PubMed:11829459, ECO:0000269|PubMed:12213210}.; ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;blood;lens;skeletal muscle;greater omentum;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;colon;parathyroid;fovea centralis;choroid;uterus;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;adrenal gland;placenta;head and neck;kidney;aorta;stomach;thymus; amygdala;whole brain;occipital lobe;medulla oblongata;superior cervical ganglion;atrioventricular node;caudate nucleus;pons;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe;cerebellum; 0.42182 . 0.018483465 55.44939844 95.13979 2.10409 WIPF3 0.000296998615800264 0.799391174113015 0.200311827271185 WAS/WASL interacting protein family member 3 FUNCTION: May be a regulator of cytoskeletal organization. May have a role in spermatogenesis (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;lung;frontal lobe;heart;testis;skin; superior cervical ganglion;subthalamic nucleus;globus pallidus;testis;ciliary ganglion;pons;kidney;atrioventricular node;cerebellum; 0.16204 . . . 274.86842 3.55213 WIPI1 0.523500460994852 0.476349969390559 0.000149569614589222 WD repeat domain, phosphoinositide interacting 1 FUNCTION: Plays an important role in autophagy and in particular starvation- and calcium-mediated autophagy, as well as in mitophagy. Functions upstream of the ATG12-ATG5-ATG16L1 complex and LC3, and downstream of the ULK1 and PI3-kinase complexes. Involved in xenophagy of Staphylococcus aureus. Invading S.aureus cells become entrapped in autophagosome-like WIPI1 positive vesicles targeted for lysosomal degradation. Plays also a distinct role in controlling the transcription of melanogenic enzymes and melanosome maturation, a process that is distinct from starvation- induced autophagy. May also regulate the trafficking of proteins involved in the mannose-6-phosphate receptor (MPR) recycling pathway. {ECO:0000269|PubMed:15020712, ECO:0000269|PubMed:15602573, ECO:0000269|PubMed:20114074, ECO:0000269|PubMed:20484055, ECO:0000269|PubMed:20639694, ECO:0000269|PubMed:21317285, ECO:0000269|PubMed:22829830, ECO:0000269|PubMed:23088497}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in skeletal muscle, heart, testis, pancreas and placenta. Highly expressed in G361, Sk-mel-28, Sk-mel-13, WM852 and WM451 cells. Up-regulated in a variety of tumor tissues. {ECO:0000269|PubMed:15602573}.; myocardium;ovary;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;liver;spleen;kidney;mammary gland;stomach; adipose tissue; 0.24206 0.09450 0.130533008 63.35810333 111.88177 2.30287 WIPI2 0.093680612051952 0.904611933314382 0.00170745463366602 WD repeat domain, phosphoinositide interacting 2 FUNCTION: Early component of the autophagy machinery being involved in formation of preautophagosomal structures and their maturation into mature phagosomes in response to phosphatidylinositol 3-phosphate (PtdIns3P). May bind PtdIns3P. {ECO:0000269|PubMed:20505359}.; . TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). Highly expressed in heart, skeletal muscle and pancreas. Expression is down-regulated in pancreatic and in kidney tumors. {ECO:0000269|PubMed:15602573, ECO:0000269|PubMed:20505359}.; myocardium;lymphoreticular;medulla oblongata;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;thyroid;germinal center;brain;heart;cartilage;pineal body;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;spleen;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;cerebellum; amygdala;dorsal root ganglion;whole brain;testis - interstitial;superior cervical ganglion;occipital lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.10028 0.08542 -1.065444789 7.425100259 53.55263 1.45507 WISP1 0.00332828025066983 0.949777937880093 0.0468937818692374 WNT1 inducible signaling pathway protein 1 FUNCTION: Downstream regulator in the Wnt/Frizzled-signaling pathway. Associated with cell survival. Attenuates p53-mediated apoptosis in response to DNA damage through activation of AKT kinase. Up-regulates the anti-apoptotic Bcl-X(L) protein. Adheres to skin and melanoma fibroblasts. In vitro binding to skin fibroblasts occurs through the proteoglycans, decorin and biglycan. {ECO:0000269|PubMed:10716946, ECO:0000269|PubMed:11782444}.; . TISSUE SPECIFICITY: Expressed in heart, kidney, lung, pancreas, placenta, ovary, small intestine and spleen. Isoform 2 is expressed predominantly in scirrhous gastric carcinoma and, weakly in placenta. Overexpression is associated with several cancers including breast cancer and colon tumors. Isoform 2 is overexpressed in scirrhous gastric carcinoma.; unclassifiable (Anatomical System);heart;cartilage;skeletal muscle;skin;uterus;whole body;endometrium;mesenchyma;adrenal gland;bone;visual apparatus;kidney; superior cervical ganglion;uterus corpus;medulla oblongata;temporal lobe;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.36458 0.16397 0.777157784 87.17857985 178.03151 2.90067 WISP1-OT1 . . . WISP1 overlapping transcript 1 . . . . . . . . . . . WISP2 0.0016907930598105 0.703408384419587 0.294900822520602 WNT1 inducible signaling pathway protein 2 FUNCTION: May play an important role in modulating bone turnover. Promotes the adhesion of osteoblast cells and inhibits the binding of fibrinogen to integrin receptors. In addition, inhibits osteocalcin production.; . TISSUE SPECIFICITY: Expressed in primary osteoblasts, fibroblasts, ovary, testes, and heart.; unclassifiable (Anatomical System);medulla oblongata;lymph node;cartilage;heart;ovary;blood;skin;skeletal muscle;uterus;pancreas;prostate;lung;cerebral cortex;synovium;mesenchyma;bone;thyroid;testis;cervix;brain;mammary gland;stomach; superior cervical ganglion;testis - interstitial;adipose tissue;adrenal gland;appendix;testis;skin; 0.35979 0.16253 0.439181676 77.69521113 90.91203 2.05143 WISP3 0.00809085603450244 0.93035466559503 0.0615544783704671 WNT1 inducible signaling pathway protein 3 FUNCTION: Appears to be required for normal postnatal skeletal growth and cartilage homeostasis.; . TISSUE SPECIFICITY: Predominant expression in adult kidney and testis and fetal kidney. Weaker expression found in placenta, ovary, prostate and small intestine. Also expressed in skeletally- derived cells such as synoviocytes and articular cartilage chondrocytes.; unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;colon;parathyroid;skin;retina;prostate;lung;cochlea;endometrium;trabecular meshwork;bone;placenta;testis;germinal center;kidney;brain;bladder;mammary gland;aorta; dorsal root ganglion;superior cervical ganglion;skeletal muscle; 0.08599 0.15244 1.0178651 90.91766926 356.57829 3.99787 WIZ 0.998940437498306 0.00105955031813258 1.21835614803358e-08 widely interspaced zinc finger motifs FUNCTION: May link EHMT1 and EHMT2 histone methyltransferases to the CTBP corepressor machinery. May be involved in EHMT1-EHMT2 heterodimer formation and stabilization (By similarity). {ECO:0000250}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;amygdala;testis - interstitial;superior cervical ganglion;caudate nucleus;atrioventricular node;pons;skeletal muscle;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;trigeminal ganglion;parietal lobe; 0.34714 . -0.799052816 12.45576787 321.62309 3.80860 WIZP1 . . . widely interspaced zinc finger motifs pseudogene 1 . . . . . . . . . . . WLS 0.344541187034555 0.655338794156477 0.000120018808967861 wntless Wnt ligand secretion mediator FUNCTION: Regulates Wnt proteins sorting and secretion in a feedback regulatory mechanism. This reciprocal interaction plays a key role in the regulation of expression, subcellular location, binding and organelle-specific association of Wnt proteins. Plays also an important role in establishment of the anterior-posterior body axis formation during development (By similarity). {ECO:0000250, ECO:0000269|PubMed:16678095, ECO:0000269|PubMed:16678096}.; . . myocardium;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;endometrium;cochlea;iris;brain;cartilage;heart;urinary;spinal cord;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;hypopharynx;duodenum;head and neck;kidney;stomach; thalamus; 0.19297 0.17296 -0.600630256 18.06440198 2243.4278 8.74019 WNK1 0.999999999364508 6.35491648190084e-10 1.42469722092447e-26 WNK lysine deficient protein kinase 1 FUNCTION: Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival, and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively. Activates SCNN1A, SCNN1B, SCNN1D and SGK1. Controls sodium and chloride ion transport by inhibiting the activity of WNK4, by either phosphorylating the kinase or via an interaction between WNK4 and the autoinhibitory domain of WNK1. WNK4 regulates the activity of the thiazide- sensitive Na-Cl cotransporter, SLC12A3, by phosphorylation. WNK1 may also play a role in actin cytoskeletal reorganization. Phosphorylates NEDD4L. Acts as a scaffold to inhibit SLC4A4, SLC26A6 as well as CFTR activities and surface expression, recruits STK39 which mediates the inhibition (By similarity). {ECO:0000250|UniProtKB:P83741, ECO:0000250|UniProtKB:Q9JIH7, ECO:0000269|PubMed:10660600, ECO:0000269|PubMed:15060842}.; DISEASE: Pseudohypoaldosteronism 2C (PHA2C) [MIM:614492]: An autosomal dominant disorder characterized by severe hypertension, hyperkalemia, hyperchloremia, mild hyperchloremic metabolic acidosis in some cases, and correction of physiologic abnormalities by thiazide diuretics. {ECO:0000269|PubMed:11498583}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Neuropathy, hereditary sensory and autonomic, 2A (HSAN2A) [MIM:201300]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by sensory and/or autonomic abnormalities. HSAN2A is an autosomal recessive disorder characterized by impairment of pain, temperature and touch sensation, onset of symptoms in infancy or early childhood, occurrence of distal extremity pathologies (paronychia, whitlows, ulcers, and Charcot joints), frequent amputations, sensory loss that affects all modalities of sensation (lower and upper limbs and perhaps the trunk as well), absence or diminution of tendon reflexes (usually in all limbs), minimal autonomic dysfunction, absence of sensory nerve action potentials, and virtual absence of myelinated fibers with decreased numbers of unmyelinated fibers in sural nerves. {ECO:0000269|PubMed:15060842, ECO:0000269|PubMed:15911806, ECO:0000269|PubMed:18521183}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, with highest levels observed in the testis, heart, kidney and skeletal muscle. Isoform 3 is kidney-specific and specifically expressed in the distal convoluted tubule (DCT) and connecting tubule (CNT) of the nephron. {ECO:0000269|PubMed:10660600, ECO:0000269|PubMed:11571656, ECO:0000269|PubMed:14645531, ECO:0000269|PubMed:22701532}.; lymphoreticular;medulla oblongata;ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;nasopharynx;placenta;head and neck;kidney;aorta;stomach;thymus; amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;hypothalamus;spinal cord;pons;atrioventricular node;subthalamic nucleus;prefrontal cortex;kidney;trigeminal ganglion;cingulate cortex;parietal lobe; 0.25927 0.20985 -1.067586275 7.354328851 5107.88496 14.67850 WNK2 0.792762080315492 0.207237918939483 7.45024642649355e-10 WNK lysine deficient protein kinase 2 FUNCTION: Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival, and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively. Activates SLC12A2, SCNN1A, SCNN1B, SCNN1D and SGK1 and inhibits SLC12A5. Negatively regulates the EGF-induced activation of the ERK/MAPK-pathway and the downstream cell cycle progression. Affects MAPK3/MAPK1 activity by modulating the activity of MAP2K1 and this modulation depends on phosphorylation of MAP2K1 by PAK1. WNK2 acts by interfering with the activity of PAK1 by controlling the balance of the activity of upstream regulators of PAK1 activity, RHOA and RAC1, which display reciprocal activity. {ECO:0000269|PubMed:17667937, ECO:0000269|PubMed:18593598, ECO:0000269|PubMed:21733846}.; . TISSUE SPECIFICITY: Expressed in various cancer cell lines (at protein level). Predominantly expressed in heart, brain, skeletal muscle and colon. {ECO:0000269|PubMed:11571656, ECO:0000269|PubMed:17667937, ECO:0000269|PubMed:21733846}.; myocardium;ovary;colon;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;lens;pancreas;lung;placenta;visual apparatus;alveolus;head and neck;mammary gland;peripheral nerve; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;adrenal gland;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;cerebellum; 0.14056 0.12240 . . 3878.51059 12.27991 WNK3 0.99999836654063 1.63345936794533e-06 1.72001064927739e-15 WNK lysine deficient protein kinase 3 FUNCTION: Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively. Phosphorylates WNK4. Regulates the phosphorylation of SLC12A1 and SLC12A2. Increases Ca(2+) influx mediated by TRPV5 and TRPV6 by enhancing their membrane expression level via a kinase-dependent pathway. Inhibits the activity of KCNJ1 by decreasing its expression at the cell membrane in a non-catalytic manner.; . TISSUE SPECIFICITY: Expressed in brain, lung, kidney, liver and pancreas, and in fetal tissues including placenta, fetal brain, lung and kidney. Very low levels of expression were also detected in fetal heart, thymus, liver and spleen. Isoform 1 is brain- specific. Isoform 3 is kidney-specific. {ECO:0000269|PubMed:11571656, ECO:0000269|PubMed:15194194, ECO:0000269|PubMed:16275913}.; unclassifiable (Anatomical System);lung;whole body;heart;pituitary gland;testis;brain;skin; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.31345 0.12309 -1.328217086 4.712196273 133.76894 2.51435 WNK4 1.82873562565171e-13 0.787771895935179 0.212228104064638 WNK lysine deficient protein kinase 4 FUNCTION: Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively. Activates SCNN1A, SCNN1B, SCNN1D, SGK1, TRPV5 and TRPV6. Regulates the activity of the thiazide-sensitive Na-Cl cotransporter, SLC12A3, by phosphorylation which appears to prevent membrane trafficking of SLC12A3. Also inhibits the renal K(+) channel, KCNJ1, via a kinase-independent mechanism by which it induces clearance of the protein from the cell surface by clathrin-dependent endocytosis. WNK4 appears to act as a molecular switch that can vary the balance between NaCl reabsorption and K(+) secretion to maintain integrated homeostasis. Phosphorylates NEDD4L. Acts as a scaffold to inhibit SLC4A4 as well as CFTR activities and surface expression, recruits STK39 which mediates the inhibition (By similarity). {ECO:0000250|UniProtKB:Q80UE6, ECO:0000269|PubMed:20525693}.; DISEASE: Pseudohypoaldosteronism 2B (PHA2B) [MIM:614491]: An autosomal dominant disorder characterized by hypertension, hyperkalemia, hyperchloremia, mild hyperchloremic metabolic acidosis, and correction of physiologic abnormalities by thiazide diuretics. {ECO:0000269|PubMed:11498583}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in kidney, colon and skin. {ECO:0000269|PubMed:11571656}.; unclassifiable (Anatomical System);colon;fovea centralis;choroid;lens;skin;retina;prostate;optic nerve;lung;placenta;macula lutea;liver;testis;spleen;kidney;mammary gland;brain; . 0.11744 0.24596 0.367380537 74.74050484 1917.68097 8.06029 WNT1 0.101878962320727 0.864973422452961 0.0331476152263118 wingless-type MMTV integration site family member 1 FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. In some developmental processes, is also a ligand for the coreceptor RYK, thus triggering Wnt signaling. Probable developmental protein. May be a signaling molecule important in CNS development. Is likely to signal over only few cell diameters. Has a role in osteoblast function and bone development. {ECO:0000269|PubMed:23499309}.; DISEASE: Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal disorder characterized by decreased bone mass and deterioration of bone microarchitecture without alteration in the composition of bone. The result is fragile bones and an increased risk of fractures, even after minimal trauma. Osteoporosis is a chronic condition of multifactorial etiology and is usually clinically silent until a fracture occurs. {ECO:0000269|PubMed:23499309, ECO:0000269|PubMed:23656646}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Osteogenesis imperfecta 15 (OI15) [MIM:615220]: An autosomal recessive form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI15 is characterized by early-onset recurrent fractures, bone deformity, significant reduction of bone density, short stature, and, in some patients, blue sclerae. Tooth development and hearing are normal. Learning and developmental delays and brain anomalies have been observed in some patients. {ECO:0000269|PubMed:23434763, ECO:0000269|PubMed:23499309, ECO:0000269|PubMed:23499310, ECO:0000269|PubMed:23656646}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . lung;testis;brain; superior cervical ganglion;skeletal muscle; 0.41743 0.78545 0.103030231 61.2762444 63.30409 1.62861 WNT2 0.611106305088224 0.387128567194699 0.00176512771707613 wingless-type MMTV integration site family member 2 FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters.; . TISSUE SPECIFICITY: Expressed in brain in the thalamus, in fetal and adult lung and in placenta. {ECO:0000269|PubMed:11449391}.; unclassifiable (Anatomical System);ovary;colon;parathyroid;uterus;prostate;lung;endometrium;placenta;liver;testis;spleen;brain; superior cervical ganglion;placenta;appendix;ciliary ganglion;atrioventricular node; 0.14021 0.43531 -0.203796826 38.81811748 66.61015 1.68290 WNT2B 0.285537291393408 0.713507162504817 0.000955546101775027 wingless-type MMTV integration site family member 2B FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. May be involved in normal development or differentiation as well as in carcinogenesis.; . TISSUE SPECIFICITY: Isoform 1 is expressed in adult heart, brain, placenta, lung, prostate, testis, ovary, small intestine and colon. In the adult brain, it is mainly found in the caudate nucleus, subthalamic nucleus and thalamus. Also detected in fetal brain, lung and kidney. Isoform 2 is expressed in fetal brain, fetal lung, fetal kidney, caudate nucleus, testis and cancer cell lines.; unclassifiable (Anatomical System);prostate;optic nerve;lung;whole body;ovary;visual apparatus;testis;colon;kidney;brain;stomach;retina; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion; 0.04243 0.22343 -0.53631094 20.53550366 63.38562 1.62925 WNT3 0.946108101336536 0.0537046241528471 0.000187274510616586 wingless-type MMTV integration site family member 3 FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Wnt-3 and Wnt-3a play distinct roles in cell-cell signaling during morphogenesis of the developing neural tube (By similarity). {ECO:0000250}.; DISEASE: Tetraamelia syndrome, autosomal recessive (TETAMS) [MIM:273395]: A rare human genetic disorder characterized by complete absence of all four limbs and other anomalies such as craniofacial, nervous system, pulmonary, skeletal and urogenital defects. {ECO:0000269|PubMed:14872406}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);testis; superior cervical ganglion;trigeminal ganglion; 0.54673 0.27035 -0.449946534 24.00330267 5.25958 0.19553 WNT3A 0.777794121014665 0.220637276091551 0.00156860289378326 wingless-type MMTV integration site family member 3A FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Wnt-3 and Wnt-3a play distinct roles in cell-cell signaling during morphogenesis of the developing neural tube.; . TISSUE SPECIFICITY: Moderately expressed in placenta and at low levels in adult lung, spleen, and prostate.; unclassifiable (Anatomical System);cartilage;placenta; dorsal root ganglion;superior cervical ganglion;occipital lobe;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;cerebellum; 0.14918 0.58479 -0.205617011 38.57631517 18.81775 0.64982 WNT4 0.153837855740478 0.829593395789081 0.0165687484704412 wingless-type MMTV integration site family member 4 FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity). Overexpression may be associated with abnormal proliferation in human breast tissue. {ECO:0000250}.; DISEASE: 46,XX sex reversal with dysgenesis of kidneys, adrenals, and lungs (SERKAL) [MIM:611812]: A disease characterized by the association of female-to-male sex reversal with dysgenesis of kidneys, adrenals, and lungs. {ECO:0000269|PubMed:18179883}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Mullerian aplasia and hyperandrogenism (MULLAPL) [MIM:158330]: A disorder of sex development. Affected females manifest dysgenesis of Mullerian duct derivatives absent or rudimentary uterus and vagina, functional ovaries, primary amenorrhea, hyperandrogenism and hirsutism. {ECO:0000269|PubMed:15317892, ECO:0000269|PubMed:16959810, ECO:0000269|PubMed:18182450}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;lung;ovary;islets of Langerhans;placenta;visual apparatus;brain; prostate;adrenal gland;placenta;beta cell islets;adrenal cortex; 0.95703 0.43956 -0.824740496 11.67728238 31.50237 0.99203 WNT5A 0.974673047386647 0.0252982707661448 2.86818472083622e-05 wingless-type MMTV integration site family member 5A FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Can activate or inhibit canonical Wnt signaling, depending on receptor context. In the presence of FZD4, activates beta-catenin signaling. In the presence of ROR2, inhibits the canonical Wnt pathway by promoting beta-catenin degradation through a GSK3-independent pathway which involves down-regulation of beta-catenin-induced reporter gene expression. Suppression of the canonical pathway allows chondrogenesis to occur and inhibits tumor formation. Stimulates cell migration. Decreases proliferation, migration, invasiveness and clonogenicity of carcinoma cells and may act as a tumor suppressor. Mediates motility of melanoma cells. Required during embryogenesis for extension of the primary anterior-posterior axis and for outgrowth of limbs and the genital tubercle. Inhibits type II collagen expression in chondrocytes. {ECO:0000269|PubMed:15735754, ECO:0000269|PubMed:17426020}.; DISEASE: Robinow syndrome, autosomal dominant 1 (DRS1) [MIM:180700]: A disease characterized by short-limb dwarfism, costovertebral segmentation defects and abnormalities of the head, face and external genitalia. The clinical signs are generally milder in dominant cases. {ECO:0000269|PubMed:19918918}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expression is increased in differentiated thyroid carcinomas compared to normal thyroid tissue and anaplastic thyroid tumors where expression is low or undetectable. Expression is found in thyrocytes but not in stromal cells (at protein level). {ECO:0000269|PubMed:15735754}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cochlea;endometrium;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;oral cavity;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;head and neck;kidney;stomach;peripheral nerve; superior cervical ganglion;placenta;trigeminal ganglion; 0.75071 0.63704 -0.161524709 41.6430762 27.84285 0.89463 WNT5A-AS1 . . . WNT5A antisense RNA 1 . . . . . . . . . . . WNT5B 0.835340308837053 0.163972611217255 0.000687079945692043 wingless-type MMTV integration site family member 5B FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;muscle;lens;bile duct;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;stomach; uterus corpus;prostate;superior cervical ganglion;adipose tissue;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11905 0.23747 -0.714505427 14.4019816 25.69919 0.83690 WNT6 0.669265997304332 0.325707773772849 0.00502622892281921 wingless-type MMTV integration site family member 6 FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. Together with CAV1 may promote chemoresistance of gastric cancer cells to DNA-damaging anthracycline drugs through the activation of the canonical Wnt receptor signaling pathway. {ECO:0000269|PubMed:22370641}.; . TISSUE SPECIFICITY: Expressed in gastric cancer cell lines and gastric cancer tissues (at protein level). Detected in the apical gland region of the gastric foveolar epithelium (at protein level). {ECO:0000269|PubMed:22370641}.; ovary;parathyroid;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;endometrium;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;tongue;lens;lung;placenta;visual apparatus;macula lutea;cervix;head and neck;kidney;stomach; superior cervical ganglion;skeletal muscle; 0.32282 0.22718 . . 210.26195 3.12961 WNT7A 0.441260494800712 0.552052135421077 0.0066873697782109 wingless-type MMTV integration site family member 7A FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. Signaling by Wnt-7a allows sexually dimorphic development of the mullerian ducts (By similarity). {ECO:0000250}.; DISEASE: Limb pelvis hypoplasia aplasia syndrome (LPHAS) [MIM:276820]: A syndrome of severe deficiency of the extremities due to hypo- or aplasia of one or more long bones of one or more limbs. Pelvic manifestations include hip dislocation, hypoplastic iliac bone and aplastic pubic bones. Thoracic deformity, unusual facies and genitourinary anomalies can be present. {ECO:0000269|PubMed:16826533, ECO:0000269|PubMed:17431918, ECO:0000269|PubMed:20949531, ECO:0000269|PubMed:21271649}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Fuhrmann syndrome (FUHRS) [MIM:228930]: Distinct limb- malformation disorder characterized also by various degrees of limb aplasia/hypoplasia and joint dysplasia. {ECO:0000269|PubMed:16826533}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expression is restricted to placenta, kidney, testis, uterus, fetal lung, and fetal and adult brain.; unclassifiable (Anatomical System);uterus;prostate;pancreas;lung;frontal lobe;heart;placenta;testis;brain;skin; lung; 0.43398 0.28850 -0.670411825 15.61689078 22.94657 0.76454 WNT7B 0.000391539815358636 0.845285473243085 0.154322986941556 wingless-type MMTV integration site family member 7B FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Moderately expressed in fetal brain, weakly expressed in fetal lung and kidney, and faintly expressed in adult brain, lung and prostate.; unclassifiable (Anatomical System);prostate;pancreas;lung;testis;kidney;lens;brain;mammary gland; skeletal muscle; . 0.21625 -1.089312628 7.047652748 17.3945 0.61054 WNT8A 0.875728925683611 0.123946346833311 0.000324727483077891 wingless-type MMTV integration site family member 8A FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. May play an important role in the development and differentiation of certain forebrain structures, notably the hippocampus.; . . . . 0.26339 0.11636 -0.560178693 19.30879925 38.27253 1.13673 WNT8B 0.485778276590173 0.509431854058582 0.00478986935124468 wingless-type MMTV integration site family member 8B FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. May play an important role in the development and differentiation of certain forebrain structures, notably the hippocampus. {ECO:0000269|PubMed:9536085}.; . TISSUE SPECIFICITY: Expression is restricted to the brain, and more specifically to the forebrain. {ECO:0000269|PubMed:9536085}.; unclassifiable (Anatomical System);ovary;colon; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.50691 0.20297 -0.05129383 49.75819769 1375.98373 6.95498 WNT9A 0.68038414960894 0.315087905303585 0.00452794508747574 wingless-type MMTV integration site family member 9A FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity). {ECO:0000250}.; . . cervix; trigeminal ganglion; 0.08932 . -0.778825328 12.88039632 35.43939 1.07031 WNT9B 0.0516168107144711 0.861298955107954 0.087084234177575 wingless-type MMTV integration site family member 9B FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Moderately expressed in fetal kidney and adult kidney. Also found in brain.; skeletal muscle; superior cervical ganglion;atrioventricular node;pons;skeletal muscle; 0.12092 0.18289 0.532823122 80.96249115 202.94359 3.07608 WNT10A 0.0101692886252667 0.943911811972106 0.0459188994026269 wingless-type MMTV integration site family member 10A FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule important in CNS development. Is likely to signal over only few cell diameters.; DISEASE: Note=Defects in WNT10A may be a cause of hypohidrotic/anhidrotic ectodermal dysplasia, a disorder characterized by sparse hair (atrichosis or hypotrichosis), abnormal or missing teeth and the inability to sweat due to the absence of sweat glands. Most patients carrying WNT10A mutations present with sweating anomalies. However, comparison with cases harboring mutations in the ectodysplasin pathway identifies some phenotypic differences. Dermatological features (anomalies of hair and sweat glands) are less severe in patients carrying WNT10A mutations and facial dysmorphism can be absent. The dental phenotype consists in microdontia, whereas teeth agenesis is more frequent in patients carrying mutations in the ectodysplasin pathway. {ECO:0000269|PubMed:20979233}.; DISEASE: Odonto-onycho-dermal dysplasia (OODD) [MIM:257980]: A rare autosomal recessive ectodermal dysplasia characterized by dry hair, severe hypodontia, smooth tongue with marked reduction of fungiform and filiform papillae, onychodysplasia, keratoderma and hyperhidrosis of palms and soles, and hyperkeratosis of the skin. {ECO:0000269|PubMed:17847007, ECO:0000269|PubMed:19559398}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Schopf-Schulz-Passarge syndrome (SSPS) [MIM:224750]: A rare ectodermal dysplasia, characterized chiefly by cysts of the eyelid margins, palmoplantar keratoderma, hypodontia, hypotrichosis and nail dystrophy. Multiple eyelid apocrine hidrocystomas are the hallmark of this condition, although they usually appear in adulthood. The concomitant presence of eccrine syringofibroadenoma in most patients and of other adnexal skin tumors in some affected subjects indicates that Schopf-Schulz- Passarge syndrome is a genodermatosis with skin appendage neoplasms. {ECO:0000269|PubMed:19559398}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Tooth agenesis selective 4 (STHAG4) [MIM:150400]: A form of selective tooth agenesis, a common anomaly characterized by the congenital absence of one or more teeth. Selective tooth agenesis without associated systemic disorders has sometimes been divided into 2 types: oligodontia, defined as agenesis of 6 or more permanent teeth, and hypodontia, defined as agenesis of less than 6 teeth. The number in both cases does not include absence of third molars (wisdom teeth). In STHAG4, the upper lateral incisors are absent or peg-shaped. {ECO:0000269|PubMed:21484994, ECO:0000269|PubMed:22581971}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;ovary;parathyroid;blood;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;lung;placenta;macula lutea;visual apparatus;testis;spleen;germinal center;stomach; atrioventricular node; 0.24339 0.20297 . . 263.26685 3.48077 WNT10B 0.00399812606925071 0.959095754400749 0.0369061195300001 wingless-type MMTV integration site family member 10B FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity). {ECO:0000250}.; DISEASE: Split-hand/foot malformation 6 (SHFM6) [MIM:225300]: A limb malformation involving the central rays of the autopod and presenting with syndactyly, median clefts of the hands and feet, and aplasia and/or hypoplasia of the phalanges, metacarpals, and metatarsals. Some patients have been found to have mental retardation, ectodermal and craniofacial findings, and orofacial clefting. {ECO:0000269|PubMed:18515319}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in most adult tissues. Highest levels were found in heart and skeletal muscle. Low levels are found in brain.; unclassifiable (Anatomical System);heart;colon;skin;bile duct;uterus;whole body;lung;frontal lobe;larynx;bone;duodenum;testis;head and neck;brain;peripheral nerve; subthalamic nucleus;temporal lobe;globus pallidus;ciliary ganglion;pons;atrioventricular node;caudate nucleus;parietal lobe;cingulate cortex; 0.79907 0.21698 -0.203796826 38.81811748 55.19484 1.49060 WNT11 0.118580135382174 0.855471689764131 0.0259481748536957 wingless-type MMTV integration site family member 11 FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters.; . TISSUE SPECIFICITY: Expressed in fetal lung, kidney, adult heart, liver, skeletal muscle, and pancreas. {ECO:0000269|PubMed:11712081}.; unclassifiable (Anatomical System);uterus;lung;frontal lobe;ovary;heart;cerebral cortex;placenta;testis;colon;skin;stomach; superior cervical ganglion;adrenal gland;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13083 0.23231 -0.093566408 46.7386176 102.6393 2.19075 WNT16 0.000185158701253108 0.707055905901132 0.292758935397615 wingless-type MMTV integration site family member 16 FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform Wnt-16b is expressed in peripheral lymphoid organs such as spleen, appendix, and lymph nodes, in kidney but not in bone marrow. Isoform Wnt-16a is expressed at significant levels only in the pancreas.; optic nerve;hippocampus;blood;pineal gland;bone marrow; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.08454 0.22908 0.440999548 77.79547063 100.90952 2.17496 WRAP53 0.617463015349294 0.382522990822508 1.39938281979089e-05 WD repeat containing, antisense to TP53 FUNCTION: Essential component of the telomerase holoenzyme complex, a ribonucleoprotein complex essential for the replication of chromosome termini that elongates telomeres in most eukaryotes. In the telomerase holoenzyme complex, it controls telomerase localization to Cajal body. Required for delivery of TERC to telomeres during S phase and for telomerase activity. Binds small Cajal body RNAs (scaRNAs). The mRNA encoding this protein plays a critical role in the regulation of p53 expression at the post- transcriptional level; it is involved both in maintaining basal p53 mRNA levels and in p53 induction upon DNA damage. {ECO:0000269|PubMed:19179534, ECO:0000269|PubMed:19250907}.; . TISSUE SPECIFICITY: Expressed in all tissues and cell lines examined. {ECO:0000269|PubMed:19250907}.; ovary;colon;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lens;skeletal muscle;bile duct;breast;pancreas;lung;mesenchyma;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.14491 0.10349 -0.574945567 18.90186365 1717.02593 7.63952 WRAP73 0.0269219902261615 0.97062042840692 0.00245758136691841 WD repeat containing, antisense to TP73 . . TISSUE SPECIFICITY: Ubiquitous. Predominant expression in heart, brain, liver, thymus, prostate, and testis, and barely detectable expression in lung.; lymphoreticular;medulla oblongata;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;endometrium;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;uterus;whole body;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;kidney;stomach;aorta;thymus; white blood cells; 0.26257 0.10150 -0.641086234 16.6784619 597.92006 4.94819 WRB 0.0591591068672799 0.867899954696639 0.0729409384360813 tryptophan rich basic protein FUNCTION: Receptor for ASNA1/TRC40-mediated insertion of tail- anchored (TA) proteins into the ER membrane. {ECO:0000269|PubMed:21444755}.; . . ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;endometrium;gum;germinal center;brain;heart;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;hypothalamus;lung;pia mater;cornea;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; whole brain;amygdala;testis - interstitial;superior cervical ganglion;medulla oblongata;occipital lobe;cerebellum peduncles;hypothalamus;spinal cord;temporal lobe;caudate nucleus;pons;fetal brain;testis - seminiferous tubule;prefrontal cortex;testis;trigeminal ganglion;cingulate cortex;parietal lobe; 0.17488 0.14896 -0.029247611 51.40363293 18.55418 0.64261 WRBP1 . . . tryptophan rich basic protein pseudogene 1 . . . . . . . . . . . WRN 1.96078222210392e-16 0.996075112619985 0.00392488738001482 Werner syndrome RecQ like helicase FUNCTION: Multifunctional enzyme that has both magnesium and ATP- dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang. Has no nuclease activity towards single-stranded DNA or blunt-ended double- stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity). Plays a role in double-strand break repair after gamma-irradiation. {ECO:0000250, ECO:0000269|PubMed:11863428, ECO:0000269|PubMed:17563354, ECO:0000269|PubMed:18596042, ECO:0000269|PubMed:19283071, ECO:0000269|PubMed:19652551, ECO:0000269|PubMed:21639834}.; DISEASE: Werner syndrome (WRN) [MIM:277700]: A rare autosomal recessive progeroid syndrome characterized by the premature onset of multiple age-related disorders, including atherosclerosis, cancer, non-insulin-dependent diabetes mellitus, ocular cataracts and osteoporosis. The major cause of death, at a median age of 47, is myocardial infarction. {ECO:0000269|PubMed:16673358}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000305|PubMed:24308539, ECO:0000305|PubMed:9989816}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;colon;blood;skin;breast;uterus;lung;cochlea;larynx;bone;thyroid;placenta;visual apparatus;liver;testis;head and neck;spleen;germinal center;kidney;brain;stomach;gall bladder; skeletal muscle; 0.91208 0.52258 0.683343061 84.94928049 1994.00837 8.22829 WRNIP1 0.637334638091566 0.3623790934692 0.000286268439233869 Werner helicase interacting protein 1 FUNCTION: Functions as a modulator for initiation or reinitiation events during DNA polymerase delta-mediated DNA synthesis. Has an intrinsic ATPase activity that functions as a sensor of DNA damage or of arrested replication forks and regulates the extent of DNA synthesis. {ECO:0000269|PubMed:15670210}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11301316}.; . . 0.66888 0.23743 . . 288.90291 3.63749 WS2B . . . Waardenburg syndrome, type 2B . . . . . . . . . . . WSB1 0.923194039998769 0.0767869852855282 1.89747157030361e-05 WD repeat and SOCS box containing 1 FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes type II iodothyronine deiodinase/DIO2. Confers constitutive instability to HIPK2 through proteasomal degradation. {ECO:0000269|PubMed:15601820, ECO:0000269|PubMed:15965468, ECO:0000269|PubMed:18093972}.; . . medulla oblongata;ovary;skin;bone marrow;retina;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;spinal cord;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;cerebral cortex;oesophagus;larynx;bone;testis;pineal gland;artery;unclassifiable (Anatomical System);lymph node;small intestine;islets of Langerhans;hypothalamus;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta; amygdala;dorsal root ganglion;occipital lobe;thalamus;medulla oblongata;superior cervical ganglion;olfactory bulb;hypothalamus;spinal cord;caudate nucleus;fetal brain;prefrontal cortex;fetal lung;trigeminal ganglion;cingulate cortex;parietal lobe; 0.35908 0.18099 -0.448125345 24.19202642 3046.97495 10.49280 WSB2 0.503215469280486 0.495921571428144 0.000862959291370234 WD repeat and SOCS box containing 2 FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}.; . . ovary;sympathetic chain;skin;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;heart;cartilage;tongue;spinal cord;adrenal cortex;blood;lens;skeletal muscle;macula lutea;liver;cervix;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;vein;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;thymus; whole brain;amygdala;occipital lobe;fetal brain;prefrontal cortex;cingulate cortex;parietal lobe;cerebellum; 0.07388 0.08144 0.21689899 68.12927577 145.74374 2.63079 WSCD1 2.91261764619966e-06 0.92567125569123 0.0743258316911239 WSC domain containing 1 . . . unclassifiable (Anatomical System);amygdala;ovary;salivary gland;muscle;intestine;pharynx;colon;blood;vein;skin;breast;prostate;lung;frontal lobe;visual apparatus;liver;testis;kidney;brain;bladder; uterus corpus;occipital lobe;thalamus;superior cervical ganglion;cerebellum peduncles;spinal cord;ciliary ganglion;cerebellum; 0.57329 . -0.396754488 26.97570182 480.45084 4.52098 WSCD2 0.494025684101003 0.505786206418187 0.000188109480809804 WSC domain containing 2 . . . unclassifiable (Anatomical System);heart;ovary;cerebellum cortex;islets of Langerhans;skeletal muscle;skin;retina;prostate;whole body;endometrium;thyroid;brain;cerebellum; . 0.22396 . -0.532670911 20.78320359 3100.71079 10.59091 WSN . . . Waisman syndrome . . . . . . . . . . . WSPAR . . . WNT signaling pathway activating non-coding RNA . . . . . . . . . . . WT1 . . . Wilms tumor 1 FUNCTION: Transcription factor that plays an important role in cellular development and cell survival. Regulates the expression of numerous target genes, including EPO. Plays an essential role for development of the urogenital system. Recognizes and binds to the DNA sequence 5'-CGCCCCCGC-3'. It has a tumor suppressor as well as an oncogenic role in tumor formation. Function may be isoform-specific: isoforms lacking the KTS motif may act as transcription factors. Isoforms containing the KTS motif may bind mRNA and play a role in mRNA metabolism or splicing. Isoform 1 has lower affinity for DNA, and can bind RNA. {ECO:0000269|PubMed:19123921, ECO:0000269|PubMed:19416806}.; DISEASE: Frasier syndrome (FS) [MIM:136680]: Characterized by a slowly progressing nephropathy leading to renal failure in adolescence or early adulthood, male pseudohermaphroditism, and no Wilms tumor. As for histological findings of the kidneys, focal glomerular sclerosis is often observed. There is phenotypic overlap with Denys-Drash syndrome. Inheritance is autosomal dominant. {ECO:0000269|PubMed:10571943}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Wilms tumor 1 (WT1) [MIM:194070]: Embryonal malignancy of the kidney that affects approximately 1 in 10'000 infants and young children. It occurs both in sporadic and hereditary forms. {ECO:0000269|PubMed:1317572, ECO:0000269|PubMed:15150775, ECO:0000269|PubMed:9108089, ECO:0000269|PubMed:9529364}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Denys-Drash syndrome (DDS) [MIM:194080]: Typical nephropathy characterized by diffuse mesangial sclerosis, genital abnormalities, and/or Wilms tumor. There is phenotypic overlap with WAGR syndrome and Frasier syndrome. Inheritance is autosomal dominant, but most cases are sporadic. {ECO:0000269|PubMed:10738002, ECO:0000269|PubMed:10799199, ECO:0000269|PubMed:11182928, ECO:0000269|PubMed:11519891, ECO:0000269|PubMed:1302008, ECO:0000269|PubMed:1338906, ECO:0000269|PubMed:15349765, ECO:0000269|PubMed:1655284, ECO:0000269|PubMed:8111391, ECO:0000269|PubMed:8112732, ECO:0000269|PubMed:8295405, ECO:0000269|PubMed:8388765, ECO:0000269|PubMed:8411073, ECO:0000269|PubMed:8741319, ECO:0000269|PubMed:8956030, ECO:0000269|PubMed:9475094, ECO:0000269|PubMed:9529364}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Nephrotic syndrome 4 (NPHS4) [MIM:256370]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. Most patients with NPHS4 show diffuse mesangial sclerosis on renal biopsy, which is a pathologic entity characterized by mesangial matrix expansion with no mesangial hypercellularity, hypertrophy of the podocytes, vacuolized podocytes, thickened basement membranes, and diminished patency of the capillary lumen. {ECO:0000269|PubMed:11182928, ECO:0000269|PubMed:15253707, ECO:0000269|PubMed:9529364, ECO:0000269|PubMed:9607189}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Meacham syndrome (MEACHS) [MIM:608978]: Rare sporadically occurring multiple malformation syndrome characterized by male pseudohermaphroditism with abnormal internal female genitalia comprising a uterus and double or septate vagina, complex congenital heart defect and diaphragmatic abnormalities. {ECO:0000269|PubMed:17853480}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving WT1 may be a cause of desmoplastic small round cell tumor (DSRCT). Translocation t(11;22)(p13;q12) with EWSR1.; DISEASE: Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive neoplasm of the serosal lining of the chest. It appears as broad sheets of cells, with some regions containing spindle- shaped, sarcoma-like cells and other regions showing adenomatous patterns. Pleural mesotheliomas have been linked to exposure to asbestos. {ECO:0000269|PubMed:8401592}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the kidney and a subset of hematopoietic cells.; unclassifiable (Anatomical System);uterus;prostate;pancreas;lung;ovary;heart;endometrium;bone;testis;kidney;skin; uterus;superior cervical ganglion;testis - interstitial;uterus corpus;ovary;testis - seminiferous tubule;placenta;testis;kidney;trigeminal ganglion;skeletal muscle; 0.99894 0.87462 -0.449946534 24.00330267 29.51052 0.94292 WT1-AS . . . WT1 antisense RNA . . . . . 0.26748 . . . . . WT2 . . . Wilms tumor 2 . . . . . . . . . . . WTAP 0.995576734722068 0.00442286761971628 3.97658215792592e-07 Wilms tumor 1 associated protein FUNCTION: Regulatory subunit of the WMM N6-methyltransferase complex, a multiprotein complex that mediates N6-methyladenosine (m6A) methylation of some adenosine residues of some mRNAs and plays a role in the efficiency of mRNA splicing, processing and mRNA stability. Required for accumulation of METTL3 and METTL14 to nuclear speckle (PubMed:24316715, PubMed:24407421, PubMed:24981863). Acts as a mRNA splicing regulator (PubMed:12444081). Regulates G2/M cell-cycle transition by binding to the 3' UTR of CCNA2, which enhances its stability (PubMed:17088532). Impairs WT1 DNA-binding ability and inhibits expression of WT1 target genes (PubMed:17095724). {ECO:0000269|PubMed:12444081, ECO:0000269|PubMed:17088532, ECO:0000269|PubMed:17095724, ECO:0000269|PubMed:24316715, ECO:0000269|PubMed:24407421, ECO:0000269|PubMed:24981863}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11001926}.; ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;epididymis;trabecular meshwork;placenta;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;kidney;pons;trigeminal ganglion; 0.23292 0.15913 -0.139478553 43.29440906 18.47383 0.63952 WTAPP1 . . . Wilms tumor 1 associated protein pseudogene 1 . . . . . . . . . . . WTIP 0.00279904745490993 0.93875502667358 0.0584459258715102 Wilms tumor 1 interacting protein FUNCTION: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing. Negatively regulates Hippo signaling pathway and antagonizes phosphorylation of YAP1. Acts as a transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent repression of E-cadherin transcription. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. In podocytes, may play a role in the regulation of actin dynamics and/or foot process cytoarchitecture (By similarity). In the course of podocyte injury, shuttles into the nucleus and acts as a transcription regulator that represses WT1-dependent transcription regulation, thereby translating changes in slit diaphragm structure into altered gene expression and a less differentiated phenotype. {ECO:0000250, ECO:0000269|PubMed:20303269, ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:22286099}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;muscle;colon;parathyroid;choroid;skin;skeletal muscle;retina;uterus;pancreas;prostate;lung;endometrium;placenta;liver;germinal center;brain;aorta;stomach; superior cervical ganglion; 0.17057 . . . 171.92566 2.86015 WWC1 0.0183845063096721 0.981615193895608 2.99794720375916e-07 WW and C2 domain containing 1 FUNCTION: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with NF2 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. Acts as a transcriptional coactivator of ESR1 which plays an essential role in DYNLL1-mediated ESR1 transactivation. Regulates collagen-stimulated activation of the ERK/MAPK cascade. Modulates directional migration of podocytes. Acts as a substrate for PRKCZ. Plays a role in cognition and memory performance. {ECO:0000269|PubMed:15081397, ECO:0000269|PubMed:16684779, ECO:0000269|PubMed:18190796, ECO:0000269|PubMed:18596123, ECO:0000269|PubMed:18672031, ECO:0000269|PubMed:20159598, ECO:0000269|PubMed:23778582}.; . TISSUE SPECIFICITY: Expressed in mammary epithelial cells and breast cancer cell lines. Found in the luminal epithelium surrounding the ducts in the normal breast. In the brain, expressed in somatodendritic compartment of neurons in the cortex and hippocampus and in the cerebellum it is found in the Purkinje cells and some granule cells (at protein level). Detected in brain, heart, colon and kidney. In the kidney, expressed in glomerular podocytes, in some tubules and in the collecting duct. {ECO:0000269|PubMed:12559952, ECO:0000269|PubMed:18190796, ECO:0000269|PubMed:18596123, ECO:0000269|PubMed:18672031}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;thyroid;bone;testis;brain;pineal gland;unclassifiable (Anatomical System);cartilage;lacrimal gland;islets of Langerhans;adrenal cortex;lens;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;liver;amnion;cervix;spleen;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;spinal cord;kidney; 0.34007 0.10799 -1.830003058 2.117244633 3460.50783 11.31457 WWC2 2.48112813993575e-05 0.999139239853653 0.000835948864947243 WW and C2 domain containing 2 . . . . . 0.47147 0.09503 0.055085661 57.54895022 2659.69867 9.69726 WWC2-AS1 . . . WWC2 antisense RNA 1 . . . . . . . . . . . WWC2-AS2 . . . WWC2 antisense RNA 2 . . . . . . . . . . . WWC3 0.999632960749509 0.000367039212816191 3.76744484966223e-11 WWC family member 3 . . . . . 0.13438 0.08261 0.718303761 85.85161595 182.44228 2.93458 WWC3-AS1 . . . WWC3 antisense RNA 1 . . . . . . . . . . . WWOX 1.93855273615458e-08 0.241218790492548 0.758781190121924 WW domain containing oxidoreductase FUNCTION: Putative oxidoreductase. Acts as a tumor suppressor and plays a role in apoptosis. Required for normal bone development (By similarity). May function synergistically with p53/TP53 to control genotoxic stress-induced cell death. Plays a role in TGFB1 signaling and TGFB1-mediated cell death. May also play a role in tumor necrosis factor (TNF)-mediated cell death. Inhibits Wnt signaling, probably by sequestering DVL2 in the cytoplasm. {ECO:0000250, ECO:0000269|PubMed:11719429, ECO:0000269|PubMed:15070730, ECO:0000269|PubMed:15548692, ECO:0000269|PubMed:16061658, ECO:0000269|PubMed:16219768, ECO:0000269|PubMed:19366691, ECO:0000269|PubMed:19465938}.; DISEASE: Note=Defects in WWOX may be involved in several cancer types. The gene spans the second most common chromosomal fragile site (FRA16D) which is frequently altered in cancers (PubMed:10861292). Alteration of the expression and expression of some isoforms is associated with cancers. However, it is still unclear if alteration of WWOX is directly implicated in cancerogenesis or if it corresponds to a secondary effect (PubMed:10861292, PubMed:11572989, PubMed:15266310, PubMed:15073125, PubMed:15131042). {ECO:0000269|PubMed:10861292, ECO:0000269|PubMed:11572989, ECO:0000269|PubMed:15073125, ECO:0000269|PubMed:15131042, ECO:0000269|PubMed:15266310}.; DISEASE: Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the esophagus. The most common types are esophageal squamous cell carcinoma and adenocarcinoma. Cancer of the esophagus remains a devastating disease because it is usually not detected until it has progressed to an advanced incurable stage. {ECO:0000269|PubMed:11956080}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Spinocerebellar ataxia, autosomal recessive, 12 (SCAR12) [MIM:614322]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR12 is additionally characterized by onset of generalized seizures in infancy, and delayed psychomotor development with mental retardation. Some patients may also show spasticity. {ECO:0000269|PubMed:24369382, ECO:0000269|PubMed:24456803}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Epileptic encephalopathy, early infantile, 28 (EIEE28) [MIM:616211]: A form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. {ECO:0000269|PubMed:25411445}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Strongly expressed in testis, prostate, and ovary. Overexpressed in cancer cell lines. Isoform 5 and isoform 6 may only be expressed in tumor cell lines. {ECO:0000269|PubMed:10786676, ECO:0000269|PubMed:11719429}.; unclassifiable (Anatomical System);heart;islets of Langerhans;salivary gland;blood;skin;skeletal muscle;uterus;prostate;lung;placenta;liver;testis;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.48891 0.98177 1.09676066 91.92026421 4591.535 13.60375 WWP1 0.956844283836257 0.0431557146614916 1.50225166821909e-09 WW domain containing E3 ubiquitin protein ligase 1 FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Ubiquitinates ERBB4 isoforms JM-A CYT-1 and JM-B CYT-1, KLF2, KLF5 and TP63 and promotes their proteasomal degradation. Ubiquitinates RNF11 without targeting it for degradation. Ubiquitinates and promotes degradation of TGFBR1; the ubiquitination is enhanced by SMAD7. Ubiquitinates SMAD6 and SMAD7. Ubiquitinates and promotes degradation of SMAD2 in response to TGF-beta signaling, which requires interaction with TGIF. {ECO:0000269|PubMed:12535537, ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:15359284}.; . TISSUE SPECIFICITY: Detected in heart, placenta, pancreas, kidney, liver, skeletal muscle, bone marrow, fetal brain, and at much lower levels in adult brain and lung. Isoform 1 and isoform 5 predominate in all tissues tested, except in testis and bone marrow, where isoform 5 is expressed at much higher levels than isoform 1. {ECO:0000269|PubMed:11779188, ECO:0000269|PubMed:9647693}.; ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;cochlea;endometrium;bone;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;oral cavity;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;peripheral nerve;thymus; amygdala;dorsal root ganglion;ciliary ganglion; 0.70717 0.14234 -0.690637458 15.12149092 65.03059 1.65778 WWP1P1 . . . WW domain containing E3 ubiquitin protein ligase 1 pseudogene 1 . . . . . . . . . . . WWP2 0.977902374453959 0.0220976241367553 1.40928546607661e-09 WW domain containing E3 ubiquitin protein ligase 2 FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Polyubiquitinates POU5F1 by 'Lys-63'-linked conjugation and promotes it to proteasomal degradation; in embryonic stem cells (ESCs) the ubiquitination is proposed to regulate POU5F1 protein level. Ubiquitinates EGR2 and promotes it to proteasomal degradation; in T-cells the ubiquitination inhibits activation- induced cell death. Ubiquitinates SLC11A2; the ubiquitination is enhanced by presence of NDFIP1 and NDFIP2. Ubiquitinates RPB1 and promotes it to proteasomal degradation. {ECO:0000269|PubMed:19274063, ECO:0000269|PubMed:19651900}.; . TISSUE SPECIFICITY: Detected in heart, throughout the brain, placenta, lung, liver, muscle, kidney and pancreas. Also detected in spleen and peripheral blood leukocytes. {ECO:0000269|PubMed:19274063, ECO:0000269|PubMed:9647693}.; lymphoreticular;ovary;colon;skin;bone marrow;prostate;whole body;ganglion;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;muscle;adrenal cortex;lens;skeletal muscle;pancreas;lung;epididymis;placenta;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; trigeminal ganglion; 0.76099 0.13681 -0.505170032 21.79759377 127.525 2.46197 WWTR1 0.918871194380801 0.0810212105002484 0.00010759511895007 WW domain containing transcription regulator 1 FUNCTION: Transcriptional coactivator which acts as a downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. WWTR1 enhances PAX8 and NKX2-1/TTF1-dependent gene activation. Regulates the nuclear accumulation of SMADS and has a key role in coupling them to the transcriptional machinery such as the mediator complex. Regulates embryonic stem-cell self-renewal, promotes cell proliferation and epithelial-mesenchymal transition. {ECO:0000269|PubMed:11118213, ECO:0000269|PubMed:18227151, ECO:0000269|PubMed:18568018, ECO:0000269|PubMed:19010321}.; . TISSUE SPECIFICITY: Highly expressed in kidney, heart, placenta and lung. Expressed in the thyroid tissue. {ECO:0000269|PubMed:11118213, ECO:0000269|PubMed:19010321}.; unclassifiable (Anatomical System);ovary;heart;colon;blood;vein;skeletal muscle;bone marrow;breast;bile duct;pancreas;prostate;optic nerve;whole body;lung;endometrium;bone;thyroid;placenta;visual apparatus;liver;kidney;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;smooth muscle;heart;placenta;trigeminal ganglion; 0.64432 0.10409 0.12689526 63.00424628 1687.61303 7.57425 WWTR1-AS1 . . . WWTR1 antisense RNA 1 . . . . . . . . . . . WWTR1-IT1 . . . WWTR1 intronic transcript 1 . . . . . . . . . . . XAB2 0.997070259537138 0.00292974021895026 2.43911332969191e-10 XPA binding protein 2 FUNCTION: Involved in transcription-coupled repair (TCR), transcription and pre-mRNA splicing. {ECO:0000269|PubMed:10944529, ECO:0000269|PubMed:17981804}.; . . lymphoreticular;medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;larynx;synovium;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; trigeminal ganglion; 0.68409 0.19221 -1.368693559 4.482189196 119.33169 2.37747 XACT . . . X active specific transcript (non-protein coding) . . . . . . . . . . . XAF1 2.07209416294807e-08 0.0733414962400482 0.92665848303901 XIAP associated factor 1 FUNCTION: Seems to function as a negative regulator of members of the IAP (inhibitor of apoptosis protein) family. Inhibits anti- caspase activity of BIRC4. Induces cleavage and inactivation of BIRC4 independent of caspase activation. Mediates TNF-alpha- induced apoptosis and is involved in apoptosis in trophoblast cells. May inhibit BIRC4 indirectly by activating the mitochondrial apoptosis pathway. After translocation to mitochondra, promotes translocation of BAX to mitochondria and cytochrome c release from mitochondria. Seems to promote the redistribution of BIRC4 from the cytoplasm to the nucleus, probably independent of BIRC4 inactivation which seems to occur in the cytoplasm. The BIRC4-XAF1 complex mediates down-regulation of BIRC5/survivin; the process requires the E3 ligase activity of BIRC4. Seems to be involved in cellular sensitivity to the proapoptotic actions of TRAIL. May be a tumor suppressor by mediating apoptosis resistance of cancer cells. {ECO:0000269|PubMed:11175744, ECO:0000269|PubMed:12029096, ECO:0000269|PubMed:16432762, ECO:0000269|PubMed:17329253, ECO:0000269|PubMed:17613533}.; . TISSUE SPECIFICITY: Widely expressed. Expression is frequently down-regulated in cancer cell lines. Isoform 5 is widely expressed. Expressed in placenta (at protein level). {ECO:0000269|PubMed:11175744, ECO:0000269|PubMed:16343440, ECO:0000269|PubMed:17329253, ECO:0000269|PubMed:17570219}.; unclassifiable (Anatomical System);smooth muscle;lymph node;heart;ovary;parathyroid;skin;skeletal muscle;retina;bile duct;uterus;whole body;lung;endometrium;bone;thyroid;placenta;liver;testis;kidney;bladder;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05763 0.08526 0.995816767 90.62278839 600.13477 4.95792 XAGE1A . . . X antigen family member 1A . . TISSUE SPECIFICITY: In normal tissues, highly expressed in testis. Expressed also in many different types of cancers: highly expressed in breast cancer, prostate cancer and many types of lung cancers, including squamous cell carcinoma, small cell carcinoma, non-small cell carcinoma, and adenocarcinoma, as well as in Ewing's cell lines, in some Ewing's sarcoma patient samples, and in one of one alveolar rhabdomyosarcoma patient sample. {ECO:0000269|PubMed:12479262, ECO:0000269|PubMed:17335148}.; . . 0.06183 . . . . . XAGE1B . . . X antigen family member 1B . . TISSUE SPECIFICITY: In normal tissues, highly expressed in testis. Expressed also in many different types of cancers: highly expressed in breast cancer, prostate cancer and many types of lung cancers, including squamous cell carcinoma, small cell carcinoma, non-small cell carcinoma, and adenocarcinoma, as well as in Ewing's cell lines, in some Ewing's sarcoma patient samples, and in one of one alveolar rhabdomyosarcoma patient sample. {ECO:0000269|PubMed:12479262, ECO:0000269|PubMed:17335148}.; . . 0.06183 . . . . . XAGE1C . . . X antigen family member 1C . . TISSUE SPECIFICITY: In normal tissues, highly expressed in testis. Expressed also in many different types of cancers: highly expressed in breast cancer, prostate cancer and many types of lung cancers, including squamous cell carcinoma, small cell carcinoma, non-small cell carcinoma, and adenocarcinoma, as well as in Ewing's cell lines, in some Ewing's sarcoma patient samples, and in one of one alveolar rhabdomyosarcoma patient sample. {ECO:0000269|PubMed:12479262, ECO:0000269|PubMed:17335148}.; unclassifiable (Anatomical System);lung;bone;alveolus;testis; . 0.06307 . . . . . XAGE1D . . . X antigen family member 1D . . TISSUE SPECIFICITY: In normal tissues, highly expressed in testis. Expressed also in many different types of cancers: highly expressed in breast cancer, prostate cancer and many types of lung cancers, including squamous cell carcinoma, small cell carcinoma, non-small cell carcinoma, and adenocarcinoma, as well as in Ewing's cell lines, in some Ewing's sarcoma patient samples, and in one of one alveolar rhabdomyosarcoma patient sample. {ECO:0000269|PubMed:12479262, ECO:0000269|PubMed:17335148}.; . . . . . . . . XAGE1E . . . X antigen family member 1E . . TISSUE SPECIFICITY: In normal tissues, highly expressed in testis. Expressed also in many different types of cancers: highly expressed in breast cancer, prostate cancer and many types of lung cancers, including squamous cell carcinoma, small cell carcinoma, non-small cell carcinoma, and adenocarcinoma, as well as in Ewing's cell lines, in some Ewing's sarcoma patient samples, and in one of one alveolar rhabdomyosarcoma patient sample. {ECO:0000269|PubMed:12479262, ECO:0000269|PubMed:17335148}.; . . 0.04602 . . . . . XAGE2 . . . X antigen family member 2 . . . heart;placenta; . 0.02794 0.04239 . . . . XAGE3 0.0885803035251833 0.763603843929524 0.147815852545293 X antigen family member 3 . . . placenta; superior cervical ganglion;tongue;placenta;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.01509 . -0.031067188 51.03798066 2.45251 0.08974 XAGE5 0.000119391381360832 0.384359427697026 0.615521180921613 X antigen family member 5 . . . testis; superior cervical ganglion;atrioventricular node; 0.04860 . 0.169169615 65.33380514 4.12462 0.15115 XBP1 0.203748476125444 0.786531084649249 0.00972043922530634 X-box binding protein 1 FUNCTION: Functions as a transcription factor during endoplasmic reticulum (ER) stress by regulating the unfolded protein response (UPR). Required for cardiac myogenesis and hepatogenesis during embryonic development, and the development of secretory tissues such as exocrine pancreas and salivary gland (By similarity). Involved in terminal differentiation of B lymphocytes to plasma cells and production of immunoglobulins (PubMed:11460154). Modulates the cellular response to ER stress in a PIK3R-dependent manner (PubMed:20348923). Binds to the cis-acting X box present in the promoter regions of major histocompatibility complex class II genes (PubMed:8349596). Involved in VEGF-induced endothelial cell (EC) proliferation and retinal blood vessel formation during embryonic development but also for angiogenesis in adult tissues under ischemic conditions. Functions also as a major regulator of the UPR in obesity-induced insulin resistance and type 2 diabetes for the management of obesity and diabetes prevention (By similarity). {ECO:0000250|UniProtKB:O35426, ECO:0000269|PubMed:11460154, ECO:0000269|PubMed:20348923, ECO:0000269|PubMed:8349596}.; FUNCTION: Isoform 2: functions as a stress-inducible potent transcriptional activator during endoplasmic reticulum (ER) stress by inducing unfolded protein response (UPR) target genes via binding to the UPR element (UPRE). Up-regulates target genes encoding ER chaperones and ER-associated degradation (ERAD) components to enhance the capacity of productive folding and degradation mechanism, respectively, in order to maintain the homeostasis of the ER under ER stress (PubMed:11779464, PubMed:25239945). Plays a role in the production of immunoglobulins and interleukin-6 in the presence of stimuli required for plasma cell differentiation (By similarity). Induces phospholipid biosynthesis and ER expansion (PubMed:15466483). Contributes to the VEGF-induced endothelial cell (EC) growth and proliferation in a Akt/GSK-dependent and/or -independent signaling pathway, respectively, leading to beta-catenin nuclear translocation and E2F2 gene expression (PubMed:23529610). Promotes umbilical vein EC apoptosis and atherosclerotisis development in a caspase-dependent signaling pathway, and contributes to VEGF- induced EC proliferation and angiogenesis in adult tissues under ischemic conditions (PubMed:19416856, PubMed:23529610). Involved in the regulation of endostatin-induced autophagy in EC through BECN1 transcriptional activation (PubMed:23184933). Plays a role as an oncogene by promoting tumor progression: stimulates zinc finger protein SNAI1 transcription to induce epithelial-to- mesenchymal (EMT) transition, cell migration and invasion of breast cancer cells (PubMed:25280941). Involved in adipocyte differentiation by regulating lipogenic gene expression during lactation. Plays a role in the survival of both dopaminergic neurons of the substantia nigra pars compacta (SNpc), by maintaining protein homeostasis and of myeloma cells. Increases insulin sensitivity in the liver as a response to a high carbohydrate diet, resulting in improved glucose tolerance. Improves also glucose homeostasis in an ER stress- and/or insulin- independent manner through both binding and proteasome-induced degradation of the transcription factor FOXO1, hence resulting in suppression of gluconeogenic genes expression and in a reduction of blood glucose levels. Controls the induction of de novo fatty acid synthesis in hepatocytes by regulating the expression of a subset of lipogenic genes in an ER stress- and UPR-independent manner (By similarity). Associates preferentially to the HDAC3 gene promoter region in a disturbed flow-dependent manner (PubMed:25190803). Binds to the BECN1 gene promoter region (PubMed:23184933). Binds to the CDH5/VE-cadherin gene promoter region (PubMed:19416856). Binds to the ER stress response element (ERSE) upon ER stress (PubMed:11779464). Binds to the 5'-CCACG-3' motif in the PPARG promoter (By similarity). {ECO:0000250|UniProtKB:O35426, ECO:0000269|PubMed:11779464, ECO:0000269|PubMed:15466483, ECO:0000269|PubMed:19416856, ECO:0000269|PubMed:23184933, ECO:0000269|PubMed:23529610, ECO:0000269|PubMed:25190803, ECO:0000269|PubMed:25239945, ECO:0000269|PubMed:25280941}.; DISEASE: Major affective disorder 7 (MAFD7) [MIM:612371]: A major psychiatric disorder that is characterized by severe mood swings, with fluctuation between two abnormal mood states (manic or major depressive episode). Mania is accompanied by symptoms of euphoria, irritability, or excitation, whereas depression is associated with low mood and decreased motivation and energy. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in plasma cells in rheumatoid synovium (PubMed:11460154). Over-expressed in primary breast cancer and metastatic breast cancer cells (PubMed:25280941). Isoform 1 and isoform 2 are expressed at higher level in proliferating as compared to confluent quiescent endothelial cells (PubMed:19416856). {ECO:0000269|PubMed:11460154, ECO:0000269|PubMed:19416856, ECO:0000269|PubMed:25280941}.; smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; . 0.46244 0.56748 -0.09720619 46.20193442 1412.29413 7.02269 XBP1P1 . . . X-box binding protein 1 pseudogene 1 FUNCTION: Functions as a transcription factor during endoplasmic reticulum (ER) stress by regulating the unfolded protein response (UPR). Required for cardiac myogenesis and hepatogenesis during embryonic development, and the development of secretory tissues such as exocrine pancreas and salivary gland (By similarity). Involved in terminal differentiation of B lymphocytes to plasma cells and production of immunoglobulins (PubMed:11460154). Modulates the cellular response to ER stress in a PIK3R-dependent manner (PubMed:20348923). Binds to the cis-acting X box present in the promoter regions of major histocompatibility complex class II genes (PubMed:8349596). Involved in VEGF-induced endothelial cell (EC) proliferation and retinal blood vessel formation during embryonic development but also for angiogenesis in adult tissues under ischemic conditions. Functions also as a major regulator of the UPR in obesity-induced insulin resistance and type 2 diabetes for the management of obesity and diabetes prevention (By similarity). {ECO:0000250|UniProtKB:O35426, ECO:0000269|PubMed:11460154, ECO:0000269|PubMed:20348923, ECO:0000269|PubMed:8349596}.; FUNCTION: Isoform 2: functions as a stress-inducible potent transcriptional activator during endoplasmic reticulum (ER) stress by inducing unfolded protein response (UPR) target genes via binding to the UPR element (UPRE). Up-regulates target genes encoding ER chaperones and ER-associated degradation (ERAD) components to enhance the capacity of productive folding and degradation mechanism, respectively, in order to maintain the homeostasis of the ER under ER stress (PubMed:11779464, PubMed:25239945). Plays a role in the production of immunoglobulins and interleukin-6 in the presence of stimuli required for plasma cell differentiation (By similarity). Induces phospholipid biosynthesis and ER expansion (PubMed:15466483). Contributes to the VEGF-induced endothelial cell (EC) growth and proliferation in a Akt/GSK-dependent and/or -independent signaling pathway, respectively, leading to beta-catenin nuclear translocation and E2F2 gene expression (PubMed:23529610). Promotes umbilical vein EC apoptosis and atherosclerotisis development in a caspase-dependent signaling pathway, and contributes to VEGF- induced EC proliferation and angiogenesis in adult tissues under ischemic conditions (PubMed:19416856, PubMed:23529610). Involved in the regulation of endostatin-induced autophagy in EC through BECN1 transcriptional activation (PubMed:23184933). Plays a role as an oncogene by promoting tumor progression: stimulates zinc finger protein SNAI1 transcription to induce epithelial-to- mesenchymal (EMT) transition, cell migration and invasion of breast cancer cells (PubMed:25280941). Involved in adipocyte differentiation by regulating lipogenic gene expression during lactation. Plays a role in the survival of both dopaminergic neurons of the substantia nigra pars compacta (SNpc), by maintaining protein homeostasis and of myeloma cells. Increases insulin sensitivity in the liver as a response to a high carbohydrate diet, resulting in improved glucose tolerance. Improves also glucose homeostasis in an ER stress- and/or insulin- independent manner through both binding and proteasome-induced degradation of the transcription factor FOXO1, hence resulting in suppression of gluconeogenic genes expression and in a reduction of blood glucose levels. Controls the induction of de novo fatty acid synthesis in hepatocytes by regulating the expression of a subset of lipogenic genes in an ER stress- and UPR-independent manner (By similarity). Associates preferentially to the HDAC3 gene promoter region in a disturbed flow-dependent manner (PubMed:25190803). Binds to the BECN1 gene promoter region (PubMed:23184933). Binds to the CDH5/VE-cadherin gene promoter region (PubMed:19416856). Binds to the ER stress response element (ERSE) upon ER stress (PubMed:11779464). Binds to the 5'-CCACG-3' motif in the PPARG promoter (By similarity). {ECO:0000250|UniProtKB:O35426, ECO:0000269|PubMed:11779464, ECO:0000269|PubMed:15466483, ECO:0000269|PubMed:19416856, ECO:0000269|PubMed:23184933, ECO:0000269|PubMed:23529610, ECO:0000269|PubMed:25190803, ECO:0000269|PubMed:25239945, ECO:0000269|PubMed:25280941}.; DISEASE: Major affective disorder 7 (MAFD7) [MIM:612371]: A major psychiatric disorder that is characterized by severe mood swings, with fluctuation between two abnormal mood states (manic or major depressive episode). Mania is accompanied by symptoms of euphoria, irritability, or excitation, whereas depression is associated with low mood and decreased motivation and energy. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in plasma cells in rheumatoid synovium (PubMed:11460154). Over-expressed in primary breast cancer and metastatic breast cancer cells (PubMed:25280941). Isoform 1 and isoform 2 are expressed at higher level in proliferating as compared to confluent quiescent endothelial cells (PubMed:19416856). {ECO:0000269|PubMed:11460154, ECO:0000269|PubMed:19416856, ECO:0000269|PubMed:25280941}.; . . 0.46244 0.56748 -0.09720619 46.20193442 . . XCE . . . X chromosome controlling element . . . . . . . . . . . XCL1 0.088160228432048 0.763202188287003 0.148637583280949 X-C motif chemokine ligand 1 FUNCTION: Chemotactic activity for lymphocytes but not for monocytes or neutrophils.; . TISSUE SPECIFICITY: Highest level in spleen, lower in peripheral leukocytes and very low levels in lung, colon and small intestine.; . . 0.09310 0.20536 0.725794416 85.98136353 269.25512 3.52005 XCL2 0.0874325391165776 0.762491406956711 0.150076053926711 X-C motif chemokine ligand 2 FUNCTION: Chemotactic activity for lymphocytes but not for monocytes or neutrophils. {ECO:0000250}.; . . . . 0.25470 0.07589 0.281220278 71.07808445 157.5486 2.74291 XCR1 0.0978541501235188 0.770983928746624 0.131161921129857 X-C motif chemokine receptor 1 FUNCTION: Receptor for chemokines SCYC1 and SCYC2. Subsequently transduces a signal by increasing the intracellular calcium ions level.; . . unclassifiable (Anatomical System); superior cervical ganglion;testis - seminiferous tubule;globus pallidus;trigeminal ganglion; 0.09264 0.12098 -0.0274281 51.65723048 24.724 0.81140 XDH 1.55760351242192e-13 0.996079506998765 0.00392049300107894 xanthine dehydrogenase FUNCTION: Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro). {ECO:0000269|PubMed:17301077}.; DISEASE: Xanthinuria 1 (XU1) [MIM:278300]: A disorder characterized by excretion of very large amounts of xanthine in the urine and a tendency to form xanthine stones. Uric acid is strikingly diminished in serum and urine. Xanthinuria 1 is due to isolated xanthine dehydrogenase deficiency. Patients can metabolize allopurinol. {ECO:0000269|PubMed:10844591, ECO:0000269|PubMed:11379872, ECO:0000269|PubMed:14551354, ECO:0000269|PubMed:9153281}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Detected in milk (at protein level). {ECO:0000269|Ref.12}.; . . 0.30940 0.09369 1.28782866 93.80750177 1251.61702 6.67765 XG 0.0136799820520379 0.866103092667985 0.120216925279978 Xg blood group . . TISSUE SPECIFICITY: Expressed in erythroid tissues, including thymus, bone marrow and fetal liver, and in several nonerythroid tissues, such as heart, placenta, skeletal muscle, thyroid and trachea, as well as in skin fibroblasts. Expression is low or undetectable in other tissues. {ECO:0000269|PubMed:10688843}.; . . 0.15239 0.65872 0.415317661 76.81056853 10.43763 0.37962 XGR . . . XG and CD99 regulator . . . . . . . . . . . XGY1 . . . Xg pseudogene, Y-linked 1 . . . . . . . . . . . XGY2 . . . Xg pseudogene, Y-linked 2 . . . . . . . . . . . XIAP 0.979278387329643 0.0207041275760145 1.7485094342918e-05 X-linked inhibitor of apoptosis FUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis. Acts as a direct caspase inhibitor. Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry. Inactivates CASP9 by keeping it in a monomeric, inactive state. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, CASP3, CASP7, CASP8, CASP9, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS and BIRC5/survivin. Ubiquitinion of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. Ubiquitinion of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation. Plays a role in copper homeostasis by ubiquitinationg COMMD1 and promoting its proteasomal degradation. Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation. Acts as an important regulator of innate immune signaling via regulation of Nodlike receptors (NLRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES. Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta- catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program. {ECO:0000269|PubMed:11447297, ECO:0000269|PubMed:12121969, ECO:0000269|PubMed:14645242, ECO:0000269|PubMed:14685266, ECO:0000269|PubMed:17560374, ECO:0000269|PubMed:17967870, ECO:0000269|PubMed:19473982, ECO:0000269|PubMed:20154138, ECO:0000269|PubMed:21145488, ECO:0000269|PubMed:22103349, ECO:0000269|PubMed:22304967, ECO:0000269|PubMed:9230442}.; DISEASE: Lymphoproliferative syndrome, X-linked, 2 (XLP2) [MIM:300635]: A rare immunodeficiency characterized by extreme susceptibility to infection with Epstein-Barr virus (EBV). Symptoms include severe or fatal mononucleosis, acquired hypogammaglobulinemia, pancytopenia and malignant lymphoma. {ECO:0000269|PubMed:17080092}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous, except peripheral blood leukocytes.; unclassifiable (Anatomical System);lung;frontal lobe;cartilage;placenta;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16911 . 0.016664174 55.21939137 1137.44296 6.43257 XIAP-AS1 . . . XIAP antisense RNA 1 . . . . . . . . . . . XIC . . . X chromosome inactivation center . . . . . . . . . . . XIRP1 2.18393838159372e-17 0.0266260144361474 0.973373985563853 xin actin binding repeat containing 1 FUNCTION: Protects actin filaments from depolymerization. {ECO:0000269|PubMed:15454575}.; . TISSUE SPECIFICITY: Isoform A, isoform B and isoform C are expressed in heart. {ECO:0000269|PubMed:16631741}.; unclassifiable (Anatomical System);myocardium;heart;ovary;spinal cord;skeletal muscle;greater omentum;lung;larynx;thyroid;visual apparatus;liver;testis;head and neck; skeletal muscle; 0.09439 0.18840 1.635295943 96.08987969 2476.98151 9.28277 XIRP2 2.85559362075031e-37 0.000128943615614304 0.999871056384386 xin actin binding repeat containing 2 FUNCTION: Protects actin filaments from depolymerization. {ECO:0000269|PubMed:15454575}.; . . unclassifiable (Anatomical System);myocardium;heart;ovary;spinal cord;skin;skeletal muscle;uterus;lung;larynx;thyroid;alveolus;liver;testis;head and neck;peripheral nerve; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18641 0.08641 1.461262125 95.18754423 11162.49118 22.95689 XIRP2-AS1 . . . XIRP2 antisense RNA 1 . . . . . . . . . . . XIST . . . X inactive specific transcript (non-protein coding) . . . . . . . . . . . XK 0.869601995997447 0.128623843814809 0.00177416018774341 X-linked Kx blood group FUNCTION: May be involved in sodium-dependent transport of neutral amino acids or oligopeptides.; DISEASE: McLeod syndrome (MLS) [MIM:300842]: A multisystem disorder characterized by the absence of red blood cell Kx antigen, weak expression of Kell red blood cell antigens, acanthocytosis, and compensated hemolysis. Most carriers of this McLeod blood group phenotype have acanthocytosis and elevated serum creatine kinase levels and are prone to develop a severe neurologic disorder resembling Huntington disease. Additional symptoms include generalized seizures, neuromuscular symptoms leading to weakness and atrophy, and cardiomyopathy mainly manifesting with atrial fibrillation, malignant arrhythmias, and dilated cardiomyopathy. {ECO:0000269|PubMed:11761473, ECO:0000269|PubMed:11961232, ECO:0000269|PubMed:12823753}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: High levels in skeletal muscle, heart, brain, and pancreas; low levels in placenta, lung, liver, and kidney.; . . 0.55234 0.15778 -0.05129383 49.75819769 3.28494 0.11908 XKR3 0.00085455981009688 0.78893372527055 0.210211714919353 XK related 3 . . TISSUE SPECIFICITY: Expressed predominantly, if not exclusively, in testis. {ECO:0000269|PubMed:16431037}.; medulla oblongata;umbilical cord;blood; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;temporal lobe;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; . . 1.214492311 93.08799245 16.83305 0.59218 XKR4 0.977591689560257 0.022404012034706 4.29840503696535e-06 XK related 4 . . . unclassifiable (Anatomical System);lung;testis;brain; . 0.17775 0.11010 -0.824740496 11.67728238 24.17631 0.79377 XKR5 . . . XK related 5 . . . . . 0.09950 . . . . . XKR6 0.956776701241562 0.0432188537072942 4.44505114377407e-06 XK related 6 . . . unclassifiable (Anatomical System);optic nerve;lung;salivary gland;bone;macula lutea;visual apparatus;testis;fovea centralis;choroid;lens;retina; . 0.31948 0.10390 -0.824740496 11.67728238 40.49271 1.18751 XKR7 0.923951242528615 0.0756030562838636 0.000445701187521236 XK related 7 . . . lung;visual apparatus; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.35248 . -0.359940251 28.93371078 645.89854 5.10288 XKR8 1.43123535164264e-05 0.403496812674615 0.596488874971868 XK related 8 FUNCTION: Promotes phosphatidylserine exposure on apoptotic cell surface, possibly by mediating phospholipid scrambling. Phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment. Has no effect on calcium-induced exposure of phosphatidylserine. Activated upon caspase cleavage, suggesting that it does not act prior the onset of apoptosis. {ECO:0000269|PubMed:23845944}.; . . . . 0.15570 0.08342 -0.60427181 17.74593064 82.90562 1.93408 XKR9 3.6097329382333e-08 0.0532593241411702 0.9467406397615 XK related 9 . . . . . . . 1.241986644 93.38877094 402.48093 4.20862 XKRX 0.000300218069787513 0.570718169499407 0.428981612430806 XK related, X-linked . . TISSUE SPECIFICITY: Expressed predominantly in the placenta, in syncytiotrophoblasts. Moderate levels in the adrenal gland, low levels in the trachea and very low levels in the bone marrow. {ECO:0000269|PubMed:16431037}.; unclassifiable (Anatomical System);uterus;lung;heart;placenta;colon;germinal center;skin; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22095 0.10019 0.327131069 73.27199811 69.30075 1.72498 XKRY . . . XK related, Y-linked . . TISSUE SPECIFICITY: Testis specific.; . . . . . . . . XKRY2 . . . XK related, Y-linked 2 . . TISSUE SPECIFICITY: Testis-specific.; . . . . . . . . XKRYP1 . . . XK related, Y-linked pseudogene 1 . . . . . . . . . . . XKRYP2 . . . XK related, Y-linked pseudogene 2 . . . . . . . . . . . XKRYP3 . . . XK related, Y-linked pseudogene 3 . . . . . . . . . . . XKRYP4 . . . XK related, Y-linked pseudogene 4 . . . . . . . . . . . XKRYP5 . . . XK related, Y-linked pseudogene 5 . . . . . . . . . . . XKRYP6 . . . XK related, Y-linked pseudogene 6 . . . . . . . . . . . XM . . . Xm(a) antigen . . . . . . . . . . . XPA 6.116600769977e-05 0.708199971503875 0.291738862488425 xeroderma pigmentosum, complementation group A FUNCTION: Involved in DNA excision repair. Initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region. Required for UV-induced CHEK1 phosphorylation and the recruitment of CEP164 to cyclobutane pyrimidine dimmers (CPD), sites of DNA damage after UV irradiation. {ECO:0000269|PubMed:19197159}.; DISEASE: Xeroderma pigmentosum complementation group A (XP-A) [MIM:278700]: An autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. The skin develops marked freckling and other pigmentation abnormalities. XP-A patients show the most severe skin symptoms and progressive neurological disorders. {ECO:0000269|PubMed:1339397, ECO:0000269|PubMed:1372103, ECO:0000269|PubMed:9671271}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in various cell lines and in skin fibroblasts. {ECO:0000269|PubMed:1918083, ECO:0000269|PubMed:8543191}.; . . 0.29248 0.55257 0.681699246 84.93158764 136.71405 2.54137 XPC 1.31713341793089e-10 0.769528282198159 0.230471717670128 xeroderma pigmentosum, complementation group C FUNCTION: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA- binding activity.; DISEASE: Xeroderma pigmentosum complementation group C (XP-C) [MIM:278720]: An autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. The skin develops marked freckling and other pigmentation abnormalities. {ECO:0000269|PubMed:10766188, ECO:0000269|PubMed:8298653}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;sympathetic chain;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;artery;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;duodenum;liver;spleen;kidney;aorta;stomach;peripheral nerve; parietal lobe; 0.28185 0.48408 0.45192103 78.03727294 310.38459 3.74818 XPNPEP1 0.964214096910664 0.0357857894355548 1.13653781176995e-07 X-prolyl aminopeptidase (aminopeptidase P) 1, soluble FUNCTION: Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro.; . TISSUE SPECIFICITY: Expressed in all tissues tested, including pancreas, heart, muscle, kidney, liver, lung and brain. Highest levels in pancreas. {ECO:0000269|PubMed:9465902}.; smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;oesophagus;larynx;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;pia mater;lung;mesenchyma;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;cerebellum; . 0.18758 0.27844 -0.734731259 14.01863647 69.42977 1.72894 XPNPEP2 1.69204692246069e-06 0.963806585860468 0.03619172209261 X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound FUNCTION: A metalloprotease that may play a role in the inflammatory process and other reactions produced in response to injury or infection. May also play a role in the metabolism of the vasodilator bradykinin.; DISEASE: Angioedema induced by ACE inhibitors (AEACEI) [MIM:300909]: A potentially life-threatening side effect of ACE inhibitors that appears in a subset of patients taking these drugs for hypertension and cardiovascular disease treatment. AEACEI is characterized by swelling of the face, lips, tongue, and airway that can lead to suffocation and death if severe. {ECO:0000269|PubMed:16175507, ECO:0000269|PubMed:20625347, ECO:0000269|PubMed:21898657}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in kidney, lung, heart, placenta, liver, small intestine and colon. No expression in brain, skeletal muscle, pancreas, spleen, thymus, prostate, testis and ovary.; . . 0.44594 0.13793 -0.376526807 28.10804435 570.24498 4.84534 XPNPEP3 8.88349445351575e-06 0.982654564784318 0.017336551721228 X-prolyl aminopeptidase 3, mitochondrial . . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are widely expressed, with isoform 1 being more abundant. {ECO:0000269|PubMed:15708373}.; unclassifiable (Anatomical System);medulla oblongata;lymph node;cartilage;ovary;heart;islets of Langerhans;hypothalamus;colon;parathyroid;blood;skin;skeletal muscle;retina;uterus;whole body;lung;frontal lobe;endometrium;synovium;mesenchyma;bone;placenta;visual apparatus;liver;testis;spleen;germinal center;kidney;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13782 0.13794 -0.26993514 34.59542345 26.91419 0.87014 XPO1 0.999999567496659 4.32503341291013e-07 6.75721255575122e-17 exportin 1 FUNCTION: Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap. Several viruses, among them HIV-1, HTLV-1 and influenza A use it to export their unspliced or incompletely spliced RNAs out of the nucleus. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization. {ECO:0000269|PubMed:14612415, ECO:0000269|PubMed:15574332, ECO:0000269|PubMed:20921223, ECO:0000269|PubMed:9311922, ECO:0000269|PubMed:9323133, ECO:0000269|PubMed:9837918}.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, skeletal muscle, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes. Not expressed in the kidney. {ECO:0000269|PubMed:9049309, ECO:0000269|PubMed:9368044}.; . . 0.99668 0.30319 -0.846787714 11.05803255 10.80842 0.39200 XPO4 0.999999613279938 3.86720062304413e-07 1.04110661625788e-17 exportin 4 FUNCTION: Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO4 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000269|PubMed:10944119, ECO:0000269|PubMed:16449645}.; . . ovary;colon;skin;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;dura mater;germinal center;brain;unclassifiable (Anatomical System);amygdala;meninges;lymph node;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;blood;skeletal muscle;breast;pancreas;pia mater;lung;adrenal gland;trabecular meshwork;placenta;visual apparatus;liver;spleen;kidney;stomach; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion; 0.22817 0.10634 -0.777005578 12.9747582 184.44583 2.94769 XPO5 0.999999368728011 6.31271989099294e-07 1.4062762331945e-18 exportin 5 FUNCTION: Mediates the nuclear export of proteins bearing a double-stranded RNA binding domain (dsRBD) and double-stranded RNAs (cargos). XPO5 in the nucleus binds cooperatively to the RNA and to the GTPase Ran in its active GTP-bound form. Proteins containing dsRBDs can associate with this trimeric complex through the RNA. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause disassembly of the complex and release of the cargo from the export receptor. XPO5 then returns to the nuclear compartment by diffusion through the nuclear pore complex, to mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Overexpression may in some circumstances enhance RNA-mediated gene silencing (RNAi). Mediates nuclear export of isoform 5 of ADAR/ADAR1 in a RanGTP-dependent manner.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:11777942}.; lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;muscle;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; testis - seminiferous tubule;testis;ciliary ganglion; 0.86468 0.23456 -0.815648973 12.01344657 487.6193 4.54621 XPO6 0.999999448411066 5.51588933635376e-07 1.22195356970251e-16 exportin 6 FUNCTION: Mediates the nuclear export of actin and profilin-actin complexes in somatic cells. {ECO:0000269|PubMed:14592989}.; . . lymphoreticular;ovary;sympathetic chain;skin;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;heart;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;choroid;uterus;whole body;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;placenta;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus; testis - interstitial;medulla oblongata;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;pons;atrioventricular node;trigeminal ganglion;whole blood;parietal lobe;cingulate cortex; 0.20219 0.10986 -0.751322189 13.71196037 89.48722 2.03366 XPO7 0.999999311353521 6.88646479024748e-07 8.59022458025464e-18 exportin 7 FUNCTION: Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO7 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000269|PubMed:11024021, ECO:0000269|PubMed:15282546}.; . TISSUE SPECIFICITY: Strong expression in testis, thyroid and bone marrow, low expression in lung, liver and small intestine, no expression in thymus, and remaining tissues studied have moderate expression. Expressed in red blood cells; overexpressed in red blood cells (cytoplasm) of patients with hereditary non- spherocytic hemolytic anemia of unknown etiology. {ECO:0000269|PubMed:11071879, ECO:0000269|PubMed:22509282}.; ovary;salivary gland;sympathetic chain;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;cerebral cortex;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;stomach;thymus; fetal liver;superior cervical ganglion;bone marrow; 0.12792 0.10594 -1.023168368 7.944090587 23.27469 0.77674 XPOT 0.997933923133681 0.00206607684526639 2.10528271853436e-11 exportin for tRNA FUNCTION: Mediates the nuclear export of aminoacylated tRNAs. In the nucleus binds to tRNA and to the GTPase Ran in its active GTP- bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the tRNA from the export receptor. XPOT then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000269|PubMed:12138183, ECO:0000269|PubMed:9512417, ECO:0000269|PubMed:9660920}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;frontal lobe;endometrium;bone;testis;germinal center;spinal ganglion;brain;artery;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;pharynx;lens;skeletal muscle;breast;pancreas;lung;cornea;mesenchyma;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;aorta;stomach; . 0.58008 0.38310 -0.688817379 15.20405756 39.60468 1.16741 XPOTP1 . . . exportin for tRNA pseudogene 1 . . . . . . . . . . . XPR1 0.998119588301853 0.00188041128944994 4.08697456121575e-10 xenotropic and polytropic retrovirus receptor 1 FUNCTION: Plays a role in phosphate homeostasis. Mediates phosphate export from the cell (PubMed:25938945). May function in G-protein coupled signal transduction (By similarity). {ECO:0000250|UniProtKB:Q9Z0U0, ECO:0000269|PubMed:25938945}.; DISEASE: Basal ganglia calcification, idiopathic, 6 (IBGC6) [MIM:616413]: A form of basal ganglia calcification, an autosomal dominant condition characterized by symmetric calcification in the basal ganglia and other brain regions. Affected individuals can either be asymptomatic or show a wide spectrum of neuropsychiatric symptoms, including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis, seizures, and chronic headache. Serum levels of calcium, phosphate, alkaline phosphatase and parathyroid hormone are normal. The neuropathological hallmark of the disease is vascular and pericapillary calcification, mainly of calcium phosphate, in the affected brain areas. {ECO:0000269|PubMed:25938945}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. Detected in spleen, lymph node, thymus, leukocytes, bone marrow, heart, kidney, pancreas and skeletal muscle. {ECO:0000269|PubMed:9927670, ECO:0000269|PubMed:9990033}.; . . 0.42295 0.20384 -0.780646273 12.77423921 24.83357 0.81488 XRCC1 1.44713822685404e-07 0.989095321531154 0.0109045337550232 X-ray repair complementing defective repair in Chinese hamster cells 1 FUNCTION: Corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents.; . . ovary;colon;skin;retina;bone marrow;uterus;prostate;endometrium;thyroid;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;muscle;lens;breast;pancreas;lung;placenta;visual apparatus;liver;cervix;kidney;mammary gland; temporal lobe;atrioventricular node; 0.17948 0.45507 0.185543665 66.2715263 1775.56341 7.78107 XRCC2 4.23850679023585e-06 0.384417242347462 0.615578519145748 X-ray repair complementing defective repair in Chinese hamster cells 2 FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the Rad21 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2- dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. {ECO:0000269|PubMed:11751635, ECO:0000269|PubMed:11834724, ECO:0000269|PubMed:21276791, ECO:0000269|PubMed:23149936}.; . . unclassifiable (Anatomical System);breast;brain; dorsal root ganglion;superior cervical ganglion;tongue;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;parietal lobe;skeletal muscle;cingulate cortex; 0.24685 0.22335 0.016664174 55.21939137 389.33038 4.15569 XRCC3 6.31832524034568e-08 0.0734294336608426 0.926570503155905 X-ray repair complementing defective repair in Chinese hamster cells 3 FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD21 paralog protein complex CX3 which acts in the BRCA1-BRCA2- dependent HR pathway. Upon DNA damage, CX3 acts downstream of RAD51 recruitment; the complex binds predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junctions of replication forks. Involved in HJ resolution and thus in processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex and seems to involve GEN1 during mitotic cell cycle progression. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and RAD51C. {ECO:0000269|PubMed:14716019, ECO:0000269|PubMed:20413593, ECO:0000269|PubMed:23108668, ECO:0000269|PubMed:23149936}.; DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:12023982}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; DISEASE: Melanoma, cutaneous malignant 6 (CMM6) [MIM:613972]: A malignant neoplasm of melanocytes, arising de novo or from a pre- existing benign nevus, which occurs most often in the skin but also may involve other sites. {ECO:0000269|PubMed:11059748}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;colon;lens;skin;breast;uterus;prostate;lung;bone;placenta;visual apparatus;testis;head and neck;cervix;germinal center;kidney;brain;tonsil;stomach;thymus; skeletal muscle;parietal lobe; 0.63192 0.40532 0.240763792 69.36777542 1036.90113 6.18396 XRCC4 0.00125064277988027 0.959128657732716 0.0396206994874035 X-ray repair complementing defective repair in Chinese hamster cells 4 FUNCTION: Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends. {ECO:0000269|PubMed:10757784, ECO:0000269|PubMed:10854421, ECO:0000269|PubMed:16412978, ECO:0000269|PubMed:8548796}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8548796}.; unclassifiable (Anatomical System);heart;colon;blood;skin;retina;bone marrow;uterus;pancreas;whole body;lung;endometrium;adrenal gland;nasopharynx;placenta;hippocampus;liver;testis;germinal center;kidney;brain;stomach; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.79933 0.28771 1.284269037 93.76621845 2475.23473 9.27149 XRCC5 0.999991832000583 8.1679993306635e-06 8.67356260146362e-14 X-ray repair complementing defective repair in Chinese hamster cells 5 FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together (PubMed:12145306, PubMed:20383123, PubMed:7957065, PubMed:8621488). The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression (PubMed:20383123). The XRCC5/6 dimer probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose- 5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription (PubMed:8621488). {ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:20383123, ECO:0000269|PubMed:7957065, ECO:0000269|PubMed:8621488}.; . . . . 0.99675 0.74295 -0.468351206 23.42533616 56.08606 1.50439 XRCC6 0.996855852811598 0.00314411221028717 3.49781148680155e-08 X-ray repair complementing defective repair in Chinese hamster cells 6 FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. Required for osteocalcin gene expression. Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose- 5-phosphate at an abasic site near double-strand breaks. 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription. {ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:20383123, ECO:0000269|PubMed:20493174, ECO:0000269|PubMed:2466842, ECO:0000269|PubMed:7957065, ECO:0000269|PubMed:8621488, ECO:0000269|PubMed:9742108}.; . . ovary;salivary gland;intestine;colon;vein;skin;retina;bone marrow;uterus;prostate;frontal lobe;bone;thyroid;testis;spinal ganglion;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;trophoblast;cartilage;islets of Langerhans;hypothalamus;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;cervix;kidney;mammary gland;stomach;peripheral nerve; whole brain;testis - interstitial;testis - seminiferous tubule;testis; 0.07828 0.76259 -0.670411825 15.61689078 11.46152 0.41417 XRCC6P1 . . . X-ray repair complementing defective repair in Chinese hamster cells 6 pseudogene 1 . . . . . . . . . . . XRCC6P2 . . . X-ray repair complementing defective repair in Chinese hamster cells 6 pseudogene 2 . . . . . . . . . . . XRCC6P3 . . . X-ray repair complementing defective repair in Chinese hamster cells 6 pseudogene 3 . . . . . . . . . . . XRCC6P4 . . . X-ray repair complementing defective repair in Chinese hamster cells 6 pseudogene 4 . . . . . . . . . . . XRCC6P5 . . . X-ray repair complementing defective repair in Chinese hamster cells 6 pseudogene 5 . . . . . . . . . . . XRCC8 . . . X-ray repair complementing defective repair in Chinese hamster cells 8 . . . . . . . . . . . XRN1 0.995837599420394 0.00416240057960475 1.61522758486933e-15 5'-3' exoribonuclease 1 FUNCTION: Major 5'-3' exoribonuclease involved in mRNA decay. Required for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA (By similarity). Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS). {ECO:0000250, ECO:0000269|PubMed:18172165}.; . TISSUE SPECIFICITY: Expressed in heart, brain, pancreas, spleen, testis, osteogenic sarcoma (OGS) biopsy and primary cell lines. {ECO:0000269|PubMed:12426100}.; smooth muscle;ovary;colon;parathyroid;skin;uterus;prostate;endometrium;larynx;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;visual apparatus;hippocampus;hypopharynx;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; subthalamic nucleus; 0.62682 0.32149 -0.319712137 30.95659354 1167.21549 6.49850 XRN2 0.813170185835591 0.186829811406618 2.7577911750927e-09 5'-3' exoribonuclease 2 FUNCTION: Possesses 5'->3' exoribonuclease activity (By similarity). May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5' fragment which is subsequently processed to form the mature mRNA and a 3' fragment which remains attached to the elongating polymerase. The processive degradation of this 3' fragment by this protein may promote termination of transcription. Binds to RNA polymerase II (RNAp II) transcription termination R-loops formed by G-rich pause sites (PubMed:21700224). {ECO:0000250, ECO:0000269|PubMed:15565158, ECO:0000269|PubMed:16648491, ECO:0000269|PubMed:21700224}.; . TISSUE SPECIFICITY: Expressed in the spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocytes, heart, brain, placenta, lung, liver, skeletal muscle, kidney, and pancreas. Isoform 2 is expressed predominantly in peripheral blood leukocytes. {ECO:0000269|PubMed:10409438, ECO:0000269|PubMed:16147866}.; . . 0.45140 0.11227 -0.574945567 18.90186365 146.64992 2.63853 XRRA1 4.2498222134866e-05 0.990721944436634 0.00923555734123118 X-ray radiation resistance associated 1 FUNCTION: May be involved in the response of cells to X-ray radiation. {ECO:0000269|PubMed:12908878}.; . TISSUE SPECIFICITY: Expressed predominantly in testis followed by prostate and ovary. Low levels found in other tissues including peripheral blood leukocytes, spleen, thymus, small intestine and colon. Also expressed in neuroblastoma, glioma, breast, lung, leukemia, renal, ovarian, prostate and colorectal cancer cell lines. {ECO:0000269|PubMed:12908878}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;frontal lobe;endometrium;synovium;bone;testis;germinal center;brain;artery;bladder;gall bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;placenta;visual apparatus;liver;spleen;cervix;kidney;mammary gland;aorta; superior cervical ganglion;testis - interstitial;skeletal muscle; 0.07204 0.07708 1.717801622 96.48502005 931.69494 5.92094 XS . . . X-linked suppressor of LU antigens . . . . . . . . . . . XWNPEP . . . X-tryptophanyl aminopeptidase . . . . . . . . . . . XXYLT1 0.0516035068341256 0.861283763835582 0.0871127293302921 xyloside xylosyltransferase 1 FUNCTION: Alpha-1,3-xylosyltransferase, which elongates the O- linked xylose-glucose disaccharide attached to EGF-like repeats in the extracellular domain of Notch proteins by catalyzing the addition of the second xylose. {ECO:0000269|PubMed:22117070}.; . . unclassifiable (Anatomical System);heart;ovary;hypothalamus;salivary gland;colon;skeletal muscle;bile duct;pancreas;whole body;lung;placenta;visual apparatus;hippocampus;duodenum;cervix;brain;mammary gland; . 0.07607 . . . 189.50997 2.98815 XXYLT1-AS1 . . . XXYLT1 antisense RNA 1 . . . . . . . . . . . XXYLT1-AS2 . . . XXYLT1 antisense RNA 2 . . . . . . . . . . . XYLB 2.62886453689458e-13 0.126493210075169 0.873506789924568 xylulokinase homolog (H. influenzae) FUNCTION: Phosphorylates D-xylulose to produce D-xylulose 5- phosphate, a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. {ECO:0000269|PubMed:23179721}.; . . unclassifiable (Anatomical System);prostate;placenta;liver;cervix;spleen;kidney;brain;mammary gland;skin;skeletal muscle;stomach; dorsal root ganglion;uterus corpus;superior cervical ganglion;globus pallidus;trigeminal ganglion;skeletal muscle; 0.35984 0.11129 0.668743049 84.68388771 2710.10266 9.79571 XYLT1 0.985159711217428 0.0148402249639889 6.38185828118549e-08 xylosyltransferase I FUNCTION: Catalyzes the first step in biosynthesis of glycosaminoglycan. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein. Initial enzyme in the biosynthesis of chondroitin sulfate and dermatan sulfate proteoglycans in fibroblasts and chondrocytes.; DISEASE: Desbuquois dysplasia 2 (DBQD2) [MIM:615777]: A chondrodysplasia characterized by severe prenatal and postnatal growth retardation (less than -5 SD), joint laxity, short extremities, progressive scoliosis, round face, midface hypoplasia, prominent bulging eyes. The main radiologic features are short long bones with metaphyseal splay, a 'Swedish key' appearance of the proximal femur (exaggerated trochanter), and advance carpal and tarsal bone age. Two forms of Desbuquois dysplasia are distinguished on the basis of the presence or absence of characteristic hand anomalies: an extra ossification center distal to the second metacarpal, delta phalanx, bifid distal thumb phalanx, and phalangeal dislocations. {ECO:0000269|PubMed:23982343, ECO:0000269|PubMed:24581741}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pseudoxanthoma elasticum (PXE) [MIM:264800]: A multisystem disorder characterized by accumulation of mineralized and fragmented elastic fibers in the skin, vascular walls, and Burch membrane in the eye. Clinically, patients exhibit characteristic lesions of the posterior segment of the eye including peau d'orange, angioid streaks, and choroidal neovascularizations, of the skin including soft, ivory colored papules in a reticular pattern that predominantly affect the neck and large flexor surfaces, and of the cardiovascular system with peripheral and coronary arterial occlusive disease as well as gastrointestinal bleedings. {ECO:0000269|PubMed:16571645}. Note=The gene represented in this entry acts as a disease modifier.; TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in placenta, kidney and pancreas. Weakly expressed in skeletal muscle. {ECO:0000269|PubMed:11099377}.; unclassifiable (Anatomical System);tongue;colon;blood;vein;skeletal muscle;bone marrow;breast;lung;larynx;amnion;testis;head and neck;germinal center; atrioventricular node;trigeminal ganglion; 0.41766 0.13047 -1.078420308 7.283557443 2029.43164 8.28777 XYLT2 0.337133945483576 0.662738798014685 0.000127256501739622 xylosyltransferase II FUNCTION: Involved in the formation of heparan sulfate and chondroitin sulfate proteoglycans (PubMed:26027496). Probably catalyzes the first step in biosynthesis of glycosaminoglycan. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein. Initial enzyme in the biosynthesis of chondroitin sulfate and dermatan sulfate proteoglycans in fibroblasts and chondrocytes (By similarity). Its enzyme activity has not been demonstrated. {ECO:0000250, ECO:0000269|PubMed:26027496}.; DISEASE: Spondyloocular syndrome (SOS) [MIM:605822]: A syndrome characterized by cataract, loss of vision due to retinal detachment, facial dysmorphism, facial hypotonia, normal height with disproportional short trunk, osteoporosis, immobile spine with thoracic kyphosis and reduced lumbal lordosis. {ECO:0000269|PubMed:26027496}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Pseudoxanthoma elasticum (PXE) [MIM:264800]: A multisystem disorder characterized by accumulation of mineralized and fragmented elastic fibers in the skin, vascular walls, and Burch membrane in the eye. Clinically, patients exhibit characteristic lesions of the posterior segment of the eye including peau d'orange, angioid streaks, and choroidal neovascularizations, of the skin including soft, ivory colored papules in a reticular pattern that predominantly affect the neck and large flexor surfaces, and of the cardiovascular system with peripheral and coronary arterial occlusive disease as well as gastrointestinal bleedings. {ECO:0000269|PubMed:16571645}. Note=The gene represented in this entry acts as a disease modifier. PXE patients carrying causative ABCC6 mutations, manifest a more severe disease course characterized by earlier onset, frequent skin lesions and higher organ involvement, in the presence of XYLT2 variants. {ECO:0000269|PubMed:16571645}.; TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in kidney and pancreas. {ECO:0000269|PubMed:11099377}.; medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;synovium;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;hippocampus;spleen;kidney;mammary gland;stomach; testis - interstitial;smooth muscle;testis - seminiferous tubule;testis; 0.27224 0.13067 -0.481306408 22.80018872 2400.48032 9.09488 YAE1D1 0.125672788400272 0.850773665169966 0.0235535464297624 Yae1 domain containing 1 . . . myocardium;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;urinary;blood;lens;skeletal muscle;lung;placenta;liver;spleen;kidney;mammary gland;stomach; subthalamic nucleus;medulla oblongata;superior cervical ganglion;testis;pons;trigeminal ganglion;cingulate cortex; 0.12106 0.09638 0.283038099 71.26680821 1451.24466 7.11084 YAF2 0.842513636178487 0.154581068824892 0.00290529499662176 YY1 associated factor 2 FUNCTION: Binds to MYC and inhibits MYC-mediated transactivation. Also binds to MYCN and enhances MYCN-dependent transcriptional activation. Increases calpain 2-mediated proteolysis of YY1 in vitro. Component of the E2F6.com-1 complex, a repressive complex that methylates 'Lys-9' of histone H3, suggesting that it is involved in chromatin-remodeling. {ECO:0000269|PubMed:11593398, ECO:0000269|PubMed:12706874, ECO:0000269|PubMed:9016636}.; . . ovary;salivary gland;intestine;colon;skin;bone marrow;prostate;cochlea;oesophagus;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;pharynx;blood;skeletal muscle;lung;cornea;mesenchyma;placenta;visual apparatus;hippocampus;liver;kidney;mammary gland; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.16823 0.10796 . . 0.97464 0.02449 YAM1 . . . YY1-associated myogenesis RNA 1 . . . . . . . . . . . YAP1 0.998547799526509 0.00145217420244398 2.62710475494659e-08 Yes associated protein 1 FUNCTION: Transcriptional regulator which can act both as a coactivator and a corepressor and is the critical downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:17974916, PubMed:18280240, PubMed:18579750, PubMed:21364637). The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ (PubMed:18158288). Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation. Acts via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization (PubMed:25778702). Plays a key role to control cell proliferation in response to cell contact. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration (PubMed:18158288). The presence of TEAD transcription factors are required for it to stimulate gene expression, cell growth, anchorage-independent growth, and epithelial mesenchymal transition (EMT) induction (PubMed:18579750). {ECO:0000269|PubMed:17974916, ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:18280240, ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:21364637, ECO:0000269|PubMed:25778702}.; DISEASE: Coloboma, ocular, with or without hearing impairment, cleft lip/palate, and/or mental retardation (COB1) [MIM:120433]: An autosomal dominant disease characterized by uveal colobomata, microphthalmia, cataract and cleft lip/palate. Considerable variability is observed among patients, uveal colobomata being the most constant feature. Some patients manifest mental retardation of varying degree and/or sensorineural, mid-frequency hearing loss. {ECO:0000269|PubMed:24462371}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Increased expression seen in some liver and prostate cancers. Isoforms lacking the transactivation domain found in striatal neurons of patients with Huntington disease (at protein level). {ECO:0000269|PubMed:16461361, ECO:0000269|PubMed:17974916, ECO:0000269|PubMed:7782338}.; myocardium;smooth muscle;ovary;salivary gland;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;oesophagus;cochlea;thyroid;bone;testis;spinal ganglion;bladder;artery;pineal gland;brain;gall bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;oral cavity;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;hypopharynx;cervix;head and neck;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion; 0.62716 0.16753 -0.271755481 34.31823543 53.62605 1.45817 YAP1P1 . . . Yes associated protein 1 pseudogene 1 . . . . . . . . . . . YAP1P2 . . . Yes associated protein 1 pseudogene 2 . . . . . . . . . . . YAP1P3 . . . Yes associated protein 1 pseudogene 3 . . . . . . . . . . . YARS 0.000308553759899848 0.986725239831489 0.0129662064086114 tyrosyl-tRNA synthetase FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr). {ECO:0000250}.; DISEASE: Charcot-Marie-Tooth disease, dominant, intermediate type, C (CMTDIC) [MIM:608323]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. The dominant intermediate type C is characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. {ECO:0000269|PubMed:16429158}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.18765 0.27794 -0.203796826 38.81811748 77.01268 1.84284 YARS2 6.88418442329642e-06 0.900190974411224 0.0998021414043525 tyrosyl-tRNA synthetase 2 FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr). {ECO:0000269|PubMed:15779907}.; DISEASE: Myopathy with lactic acidosis and sideroblastic anemia 2 (MLASA2) [MIM:613561]: A rare oxidative phosphorylation disorder specific to skeletal muscle and bone marrow. Affected individuals manifest sideroblastic anemia, progressive lethargy, muscle weakness, and exercise intolerance associated with persistent lactic acidemia. {ECO:0000269|PubMed:20598274, ECO:0000269|PubMed:22504945}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;iris;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;heart;lacrimal gland;blood;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;skeletal muscle; 0.10936 0.28516 -0.468351206 23.42533616 1275.23642 6.72336 YBEY 0.000726358489255345 0.521237141696339 0.478036499814405 ybeY metallopeptidase (putative) . . . unclassifiable (Anatomical System);heart;islets of Langerhans;colon;blood;fovea centralis;choroid;lens;skin;retina;pancreas;prostate;optic nerve;whole body;lung;bone;placenta;macula lutea;visual apparatus;testis;cervix;germinal center;kidney;brain;mammary gland;stomach; . 0.14392 0.10428 0.013025609 54.62962963 41.75719 1.21650 YBX1 0.990640769249964 0.00935674602186912 2.48472816640196e-06 Y-box binding protein 1 FUNCTION: Mediates pre-mRNA alternative splicing regulation. Binds to splice sites in pre-mRNA and regulates splice site selection. Binds and stabilizes cytoplasmic mRNA. Contributes to the regulation of translation by modulating the interaction between the mRNA and eukaryotic initiation factors (By similarity). Regulates the transcription of numerous genes. Its transcriptional activity on the multidrug resistance gene MDR1 is enhanced in presence of the APEX1 acetylated form at 'Lys-6' and 'Lys-7'. Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'), such as MDR1 and HLA class II genes. Promotes separation of DNA strands that contain mismatches or are modified by cisplatin. Has endonucleolytic activity and can introduce nicks or breaks into double-stranded DNA (in vitro). May play a role in DNA repair. Component of the CRD-mediated complex that promotes MYC mRNA stability. Binds preferentially to the 5'-[CU]CUGCG-3' motif in vitro. {ECO:0000250, ECO:0000269|PubMed:10817758, ECO:0000269|PubMed:11698476, ECO:0000269|PubMed:12604611, ECO:0000269|PubMed:14718551, ECO:0000269|PubMed:18335541, ECO:0000269|PubMed:18809583, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19483673}.; . . myocardium;medulla oblongata;smooth muscle;ovary;skin;retina;bone marrow;prostate;cochlea;endometrium;thyroid;bladder;brain;gall bladder;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;vein;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta; . 0.93407 . 0.281220278 71.07808445 . . YBX1P1 . . . Y-box binding protein 1 pseudogene 1 . . . . . . . . . . . YBX1P2 . . . Y-box binding protein 1 pseudogene 2 . . . . . . . . . . . YBX1P3 . . . Y-box binding protein 1 pseudogene 3 . . . . . . . . . . . YBX1P4 . . . Y-box binding protein 1 pseudogene 4 . . . . . . . . . . . YBX1P5 . . . Y-box binding protein 1 pseudogene 5 . . . . . . . . . . . YBX1P6 . . . Y-box binding protein 1 pseudogene 6 . . . . . . . . . . . YBX1P7 . . . Y-box binding protein 1 pseudogene 7 . . . . . . . . . . . YBX1P8 . . . Y-box binding protein 1 pseudogene 8 . . . . . . . . . . . YBX1P9 . . . Y-box binding protein 1 pseudogene 9 . . . . . . . . . . . YBX1P10 . . . Y-box binding protein 1 pseudogene 10 . . . . . . . . . . . YBX2 0.968725623233792 0.0312723912483239 1.98551788415566e-06 Y-box binding protein 2 FUNCTION: Major constituent of messenger ribonucleoprotein particles (mRNPs). Involved in the regulation of the stability and/or translation of germ cell mRNAs. Binds to Y-box consensus promoter element. Binds to full length mRNA with high affinity in a sequence-independent manner. Binds to short RNA sequences containing the consensus site 5'-UCCAUCA-3' with low affinity and limited sequence specificity. Its binding with maternal mRNAs is necessary for its cytoplasmic retention. May mark specific mRNAs (those transcribed from Y-box promoters) in the nucleus for cytoplasmic storage, thereby linking transcription and mRNA storage/translational delay (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in oocytes and testicular germ cells in the stage of spermatogonia to spermatocyte. Also observed placental trophoblasts, as well as in vascular smooth muscle cells in the pulmonary artery, myocardium, and skeletal muscle. Undetectable in epithelial cells in respiratory, gastrointestinal, and urogenital tracts. Up-regulated in various carcinomas and germ cell tumors (at protein level). {ECO:0000269|PubMed:10100484, ECO:0000269|PubMed:16479255}.; unclassifiable (Anatomical System);uterus;medulla oblongata;lung;larynx;thyroid;hippocampus;testis;colon;head and neck;brain;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.64648 0.07351 -0.251530012 35.42108988 2529.75027 9.38178 YBX2P1 . . . Y-box binding protein 2 pseudogene 1 . . . . . . . . . . . YBX3 0.00662806716120506 0.974791235577941 0.0185806972608543 Y-box binding protein 3 FUNCTION: Binds to the GM-CSF promoter. Seems to act as a repressor. Binds also to full length mRNA and to short RNA sequences containing the consensus site 5'-UCCAUCA-3'. May have a role in translation repression (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle and heart.; . . 0.83421 0.18817 0.330767508 73.53739089 1954.86862 8.13769 YBX3P1 . . . Y-box binding protein 3 pseudogene 1 . . . . . . . . . . . YDJC 0.00215046445208775 0.514999899816302 0.48284963573161 YdjC homolog (bacterial) FUNCTION: Probably catalyzes the deacetylation of acetylated carbohydrates an important step in the degradation of oligosaccharides. {ECO:0000250|UniProtKB:Q53WD3}.; . . unclassifiable (Anatomical System);lymph node;ovary;heart;tongue;islets of Langerhans;colon;blood;bone marrow;uterus;prostate;pancreas;lung;bone;placenta;visual apparatus;testis;cervix;head and neck;spleen;kidney;germinal center;brain;tonsil;stomach; prostate;lung;thyroid;liver;tumor;white blood cells; 0.13826 0.10192 . . 2545.58262 9.42436 YEATS2 0.999977828893892 2.21711061079428e-05 3.34975296171863e-16 YEATS domain containing 2 FUNCTION: Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. {ECO:0000269|PubMed:19103755}.; . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;head and neck;aorta;stomach;peripheral nerve; . 0.11833 0.10042 -1.076610636 7.324840764 4718.02584 13.86609 YEATS2-AS1 . . . YEATS2 antisense RNA 1 . . . . . . . . . . . YEATS4 0.0987387891578807 0.866445616273791 0.0348155945683285 YEATS domain containing 4 FUNCTION: Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. {ECO:0000269|PubMed:14966270}.; . TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. {ECO:0000269|PubMed:10913114}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;prostate;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;blood;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;cerebellum; superior cervical ganglion;globus pallidus;testis;atrioventricular node; 0.67697 . -0.119252484 44.53880632 1.25742 0.04419 YES1 0.0463916223696272 0.953390446676442 0.00021793095393108 YES proto-oncogene 1, Src family tyrosine kinase FUNCTION: Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis. {ECO:0000269|PubMed:11901164, ECO:0000269|PubMed:18479465, ECO:0000269|PubMed:19276087, ECO:0000269|PubMed:21566460, ECO:0000269|PubMed:21713032}.; . TISSUE SPECIFICITY: Expressed in the epithelial cells of renal proximal tubules and stomach as well as hematopoietic cells in the bone marrow and spleen in the fetal tissues. In adult, expressed in epithelial cells of the renal proximal tubules and present in keratinocytes in the basal epidermal layer of epidermis. {ECO:0000269|PubMed:2021534, ECO:0000269|PubMed:2067846}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;brain;gall bladder;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;internal ear;placenta;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.92686 0.51349 -0.203796826 38.81811748 69.86384 1.73424 YES1P1 . . . YES1 pseudogene 1 . . . . . . . . . . . YIF1A 2.08231700262511e-09 0.0370571004349031 0.96294289748278 Yip1 interacting factor homolog A, membrane trafficking protein FUNCTION: Possible role in transport between endoplasmic reticulum and Golgi. {ECO:0000269|PubMed:15990086}.; . . unclassifiable (Anatomical System);islets of Langerhans;colon;skeletal muscle;uterus;liver;testis;spleen;cervix;germinal center;pineal gland;brain;stomach; liver; 0.20913 0.12119 -0.602450568 17.91106393 159.42561 2.75881 YIF1B 0.0375242137865894 0.92898733291803 0.0334884532953801 Yip1 interacting factor homolog B, membrane trafficking protein . . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;iris;testis;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;urinary;blood;lens;pancreas;lung;epididymis;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach; . 0.24539 0.10425 -0.359940251 28.93371078 808.07291 5.59816 YIPF1 0.0173793241634188 0.960430238584142 0.0221904372524391 Yip1 domain family member 1 . . . colon;fovea centralis;skin;bone marrow;uterus;prostate;whole body;endometrium;larynx;thyroid;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);amygdala;cartilage;heart;tongue;islets of Langerhans;muscle;blood;bile duct;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;testis - seminiferous tubule;globus pallidus;atrioventricular node;trigeminal ganglion;cingulate cortex; 0.16636 0.12384 -0.22584292 37.32012267 1838.13378 7.90539 YIPF2 0.00109917458451604 0.832141091551957 0.166759733863527 Yip1 domain family member 2 . . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;placenta;liver;testis;fetal thyroid;trigeminal ganglion; 0.16078 0.10252 -0.201976964 38.98325077 84.71364 1.96016 YIPF3 0.812100973786078 0.187697817822679 0.000201208391243093 Yip1 domain family member 3 FUNCTION: Involved in the maintenance of the Golgi structure. May play a role in hematopoiesis. {ECO:0000269|PubMed:12490290, ECO:0000269|PubMed:21757827}.; . TISSUE SPECIFICITY: Expressed by nucleated hematopoietic cells (at protein level). {ECO:0000269|PubMed:12490290}.; medulla oblongata;smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;optic nerve;ganglion;frontal lobe;endometrium;gum;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pharynx;blood;skeletal muscle;breast;epididymis;trabecular meshwork;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;uterus;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);trophoblast;islets of Langerhans;muscle;pancreas;lung;cornea;nasopharynx;placenta;hippocampus;duodenum;amnion;head and neck;kidney;stomach;aorta;thymus; . 0.19090 0.14279 -0.538132194 20.26421326 136.37023 2.53858 YIPF4 0.019788591248373 0.902081655286221 0.0781297534654063 Yip1 domain family member 4 FUNCTION: Involved in the maintenance of the Golgi structure. {ECO:0000269|PubMed:21757827}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;bile duct;pancreas;lung;mesenchyma;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;kidney; appendix; 0.25391 0.10849 0.369407109 74.95281906 43.18158 1.24746 YIPF5 0.931585721197837 0.0680731428764855 0.000341135925677117 Yip1 domain family member 5 FUNCTION: Plays a role in transport between endoplasmic reticulum and Golgi. {ECO:0000269|PubMed:11489904, ECO:0000269|PubMed:15611160}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in coronary smooth muscles. {ECO:0000269|PubMed:15922870}.; ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;bone;thyroid;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;spinal cord;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;smooth muscle;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.10995 0.10013 0.393270925 76.04977589 54.68309 1.48029 YIPF6 0.571047385335828 0.417401823816142 0.01155079084803 Yip1 domain family member 6 . . . . . 0.15106 0.06538 -0.053113545 49.38664779 6.07447 0.22981 YIPF7 2.38128208040908e-05 0.301587887920871 0.698388299258325 Yip1 domain family member 7 . . . kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . . -0.115612493 45.12856806 472.13977 4.49777 YJEFN3 2.63542608769062e-06 0.170405053530296 0.829592311043617 YjeF N-terminal domain containing 3 FUNCTION: May play a role in spermiogenesis and oogenesis. {ECO:0000269|PubMed:17533573}.; . TISSUE SPECIFICITY: Expressed in theca cells in ovary and in Leydig cells in testis (at protein level). Also expressed in brain and mammary gland. {ECO:0000269|PubMed:17533573}.; . . . . -0.247889024 35.98726115 48.08621 1.34927 YKT6 0.852902232625853 0.146590203788589 0.000507563585557622 YKT6 v-SNARE homolog (S. cerevisiae) FUNCTION: Vesicular soluble NSF attachment protein receptor (v- SNARE) mediating vesicle docking and fusion to a specific acceptor cellular compartment. Functions in endoplasmic reticulum to Golgi transport; as part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in early/recycling endosome to TGN transport; as part of a SNARE complex composed of BET1L, GOSR1 and STX5. Has a S-palmitoyl transferase activity. {ECO:0000269|PubMed:15215310, ECO:0000269|PubMed:9211930}.; . . lymphoreticular;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;heart;cartilage;urinary;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;colon;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;placenta;hypopharynx;head and neck;kidney;stomach;thymus; smooth muscle;white blood cells; 0.13434 0.14896 -0.317668748 31.45789101 20.16391 0.68972 YLPM1 0.999933059355471 6.69406445291122e-05 3.39272774004954e-19 YLP motif containing 1 FUNCTION: Plays a role in the reduction of telomerase activity during differentiation of embryonic stem cells by binding to the core promoter of TERT and controlling its down-regulation. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in neuronal, neuroblastoma and embryonic kidney cell lines (at protein level). {ECO:0000269|PubMed:17890166}.; medulla oblongata;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; dorsal root ganglion;superior cervical ganglion;medulla oblongata;occipital lobe;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion;parietal lobe;cerebellum; . 0.10158 -2.445873847 1.020287804 805.81445 5.59253 YME1L1 0.994242144818157 0.00575785391199332 1.26984934874051e-09 YME1 like 1 ATPase FUNCTION: Putative ATP-dependent protease which plays a role in mitochondrial protein metabolism. Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins. Requires to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1). Seems to act in the processing of OPA1. {ECO:0000269|PubMed:18076378, ECO:0000269|PubMed:22262461}.; . TISSUE SPECIFICITY: High expression in cardiac and skeletal muscle mitochondria. {ECO:0000269|PubMed:22262461}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;cornea;adrenal gland;placenta;visual apparatus;alveolus;duodenum;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;thymus; amygdala;testis - interstitial;superior cervical ganglion;thyroid;testis;ciliary ganglion;skeletal muscle; 0.20186 0.31881 -0.821100135 11.88369899 901.62157 5.84692 YME1L1P1 . . . YME1L1 pseudogene 1 . . . . . . . . . . . YOD1 0.543401293595549 0.442313698051173 0.0142850083532783 YOD1 deubiquitinase FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins and participates in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by triming the ubiquitin chain on the associated substrate to facilitate their threading through the VCP/p97 pore. Ubiquitin moieties on substrates may present a steric impediment to the threading process when the substrate is transferred to the VCP pore and threaded through VCP's axial channel. Mediates deubiquitination of 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked ubiquitin chains. Cleaves both polyubiquitin and di-ubiquitin. {ECO:0000269|PubMed:19818707, ECO:0000269|PubMed:23827681}.; . . unclassifiable (Anatomical System);meninges;medulla oblongata;pia mater;endometrium;placenta;liver;colon;dura mater;germinal center;skin; superior cervical ganglion;fetal liver;parietal lobe; 0.15513 0.07399 -0.361761279 28.6329323 32.09087 1.00713 YPEL1 0.224430518088329 0.739578476370413 0.035991005541258 yippee like 1 FUNCTION: May play a role in epithelioid conversion of fibroblasts.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;testis;germinal center;spinal ganglion;brain;myometrium;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;spinal cord;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;kidney;mammary gland;aorta;stomach; . 0.10780 . 0.057118534 57.99716914 . . YPEL2 0.928981263851905 0.0706438609292816 0.000374875218813087 yippee like 2 . . TISSUE SPECIFICITY: Widely expressed. Detected in fetal and adult kidney, heart, liver, lung and skeletal muscle. {ECO:0000269|PubMed:15556292}.; unclassifiable (Anatomical System);breast;uterus;lung;islets of Langerhans;iris;colon;blood;kidney;germinal center;brain; superior cervical ganglion;occipital lobe;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.31308 . 0.013025609 54.62962963 1.35456 0.04823 YPEL3 0.122709138935465 0.779845913119814 0.0974449479447212 yippee like 3 FUNCTION: Involved in proliferation and apoptosis in myeloid precursor cells. {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15556292}.; . . 0.34653 0.11262 0.191216164 66.57230479 26.18051 0.84876 YPEL4 0.805554819387752 0.189365154550246 0.00508002606200131 yippee like 4 . . TISSUE SPECIFICITY: Widely expressed. Detected adult brain, lung, colon, small intestine and ovary, and in fetal brain, lung, liver and spleen. {ECO:0000269|PubMed:15556292}.; unclassifiable (Anatomical System);optic nerve;lung;thyroid;visual apparatus;liver;testis;spleen;brain;cerebellum; . 0.30229 0.11262 -0.009020804 52.8544468 4.82461 0.17652 YPEL5 0.799401083937221 0.195077061988221 0.00552185407455869 yippee like 5 . . . smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;thyroid;amniotic fluid;germinal center;brain;gall bladder;heart;cartilage;pineal body;spinal cord;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;mammary gland;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;dura mater;pineal gland;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;bile duct;pancreas;pia mater;lung;mesenchyma;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;cerebellum;thymus; subthalamic nucleus;globus pallidus; 0.37657 0.11262 0.057118534 57.99716914 2.00216 0.06533 YPEL5P1 . . . YPEL5 pseudogene 1 . . . . . . . . . . . YPEL5P2 . . . YPEL5 pseudogene 2 . . . . . . . . . . . YPEL5P3 . . . YPEL5 pseudogene 3 . . . . . . . . . . . YRDC 0.13339560775993 0.78010062843384 0.0865037638062307 yrdC N(6)-threonylcarbamoyltransferase domain containing FUNCTION: May regulate the activity of some transporters. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12730717}.; . . 0.46387 0.17039 . . 33.31468 1.02930 YRDCP1 . . . yrdC N(6)-threonylcarbamoyltransferase domain containing pseudogene 1 . . . . . . . . . . . YRDCP2 . . . yrdC N(6)-threonylcarbamoyltransferase domain containing pseudogene 2 . . . . . . . . . . . YRDCP3 . . . yrdC N(6)-threonylcarbamoyltransferase domain containing pseudogene 3 . . . . . . . . . . . YTHDC1 0.999999898691266 1.01308734437362e-07 1.96952148517686e-18 YTH domain containing 1 FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs (PubMed:26318451, PubMed:25242552). M6A is a modification present at internal sites of mRNAs and some non- coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:26318451, PubMed:25242552). Regulates alternative splice site selection (PubMed:20167602). {ECO:0000269|PubMed:20167602, ECO:0000269|PubMed:25242552, ECO:0000269|PubMed:26318451}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;amniotic fluid;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;cerebellum cortex;islets of Langerhans;pharynx;blood;lens;pancreas;lung;cornea;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;occipital lobe;superior cervical ganglion;prefrontal cortex;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex; 0.25185 0.12640 -0.580403979 18.58928993 444.77934 4.38844 YTHDC2 0.999999571704339 4.28295661406565e-07 2.23811354771163e-20 YTH domain containing 2 FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs (PubMed:26318451). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:26318451). {ECO:0000269|PubMed:26318451}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;uterus;prostate;whole body;cochlea;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;stomach;thymus; amygdala;dorsal root ganglion;medulla oblongata;superior cervical ganglion;testis;globus pallidus;atrioventricular node; 0.41393 0.09698 -0.275617382 33.58693088 3059.0798 10.51775 YTHDF1 0.983709938969743 0.016280387812393 9.67321786372519e-06 YTH N(6)-methyladenosine RNA binding protein 1 FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-containing mRNAs, and promotes mRNA translation efficiency (PubMed:24284625, PubMed:26046440, PubMed:26318451). M6A is a modification present at internal sites of mRNAs and some non- coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:24284625). Acts as a regulator of mRNA translation efficiency: promotes ribosome loading to m6A- containing mRNAs and interacts with translation initiation factors eIF3 (EIF3A or EIF3B) to facilitate translation initiation (PubMed:26046440). {ECO:0000269|PubMed:24284625, ECO:0000269|PubMed:26046440, ECO:0000269|PubMed:26318451}.; . . unclassifiable (Anatomical System);lung;whole body;placenta;hypopharynx;testis;cervix;head and neck;brain;skin;stomach;bone marrow; superior cervical ganglion;subthalamic nucleus;cerebellum; 0.19683 0.11110 -0.089927255 46.99221515 226.04974 3.24854 YTHDF1P1 . . . YTH domain family member 1 pseudogene 1 . . . . . . . . . . . YTHDF2 0.99116572766449 0.00883211505630862 2.15727920173177e-06 YTH N(6)-methyladenosine RNA binding protein 2 FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates mRNA stability (PubMed:24284625, PubMed:26046440, PubMed:26318451). M6A is a modification present at internal sites of mRNAs and some non- coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:22575960, PubMed:24284625, PubMed:25412658, PubMed:25412661). Acts as a regulator of mRNA stability: binding to m6A-containing mRNAs results in the localization to mRNA decay sites, such as processing bodies (P- bodies), leading to mRNA degradation (PubMed:24284625, PubMed:26046440). Also acts as a promoter of cap-independent mRNA translation following heat shock stress: upon stress, relocalizes to the nucleus and specifically binds mRNAs with some m6A methylation mark at their 5'-UTR, protecting demethylation of mRNAs by FTO, thereby promoting cap-independent mRNA translation (PubMed:26458103). {ECO:0000269|PubMed:22575960, ECO:0000269|PubMed:24284625, ECO:0000269|PubMed:25412658, ECO:0000269|PubMed:25412661, ECO:0000269|PubMed:26046440, ECO:0000269|PubMed:26318451, ECO:0000269|PubMed:26458103}.; . . . . 0.54838 0.15588 -0.005381972 53.50908233 48.02869 1.34715 YTHDF2P1 . . . YTH domain family member 2 pseudogene 1 . . . . . . . . . . . YTHDF3 0.975545265361137 0.0244284297646076 2.63048742550918e-05 YTH N(6)-methyladenosine RNA binding protein 3 FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability. {ECO:0000269|PubMed:22575960, ECO:0000269|PubMed:24284625}.; . . . . 0.36455 . . . 64.0439 1.64058 YTHDF3-AS1 . . . YTHDF3 antisense RNA 1 (head to head) . . . . . . . . . . . YWHAB 0.938360894039554 0.0613767655609313 0.000262340399514752 tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein beta FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. {ECO:0000269|PubMed:17717073, ECO:0000269|PubMed:19592491}.; . . myocardium;lymphoreticular;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;bladder;brain;tonsil;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;fovea centralis;choroid;vein;uterus;larynx;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;trophoblast;cerebellum cortex;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach; amygdala;whole brain;occipital lobe;thalamus;superior cervical ganglion;medulla oblongata;cerebellum peduncles;hypothalamus;temporal lobe;white blood cells;caudate nucleus;pons;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;whole blood;parietal lobe;cingulate cortex; 0.98107 0.70722 0.103030231 61.2762444 18.29907 0.63541 YWHABP1 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein beta pseudogene 1 . . . . . . . . . . . YWHABP2 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein beta pseudogene 2 . . . . . . . . . . . YWHAE 0.964161141960601 0.0357711220909227 6.77359484763807e-05 tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein epsilon FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.; . . myocardium;ovary;salivary gland;intestine;colon;substantia nigra;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;subthalamic nucleus;prefrontal cortex;pons;parietal lobe;cerebellum; 0.81084 . -0.075159878 47.78839349 2.62817 0.09564 YWHAEP1 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein epsilon pseudogene 1 . . . . . . . . . . . YWHAEP2 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein epsilon pseudogene 2 . . . . . . . . . . . YWHAEP3 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein epsilon pseudogene 3 . . . . . . . . . . . YWHAEP4 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein epsilon pseudogene 4 . . . . . . . . . . . YWHAEP5 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein epsilon pseudogene 5 . . . . . . . . . . . YWHAEP6 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein epsilon pseudogene 6 . . . . . . . . . . . YWHAEP7 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein epsilon pseudogene 7 . . . . . . . . . . . YWHAG 0.937613568815639 0.0621160183132805 0.000270412871080817 tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein gamma FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. {ECO:0000269|PubMed:16511572}.; . TISSUE SPECIFICITY: Highly expressed in brain, skeletal muscle, and heart. {ECO:0000269|PubMed:10486217}.; smooth muscle;ovary;sympathetic chain;substantia nigra;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;cerebral cortex;larynx;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;islets of Langerhans;hypothalamus;pancreas;pia mater;lung;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; superior cervical ganglion; 0.98926 0.53296 -0.295622497 32.61972163 3.76147 0.13967 YWHAH 0.555591182061994 0.431389404424585 0.0130194135134212 tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein eta FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1. {ECO:0000269|PubMed:12177059}.; . TISSUE SPECIFICITY: Expressed mainly in the brain and present in other tissues albeit at lower levels.; smooth muscle;sympathetic chain;skin;bone marrow;retina;prostate;frontal lobe;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;breast;visual apparatus;liver;cervix;spleen;mammary gland;colon;parathyroid;uterus;larynx;bone;pituitary gland;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach;aorta;cerebellum; amygdala;dorsal root ganglion;whole brain;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;fetal brain;prefrontal cortex;globus pallidus;ciliary ganglion;parietal lobe;cingulate cortex;cerebellum; 0.85049 0.54626 -0.075159878 47.78839349 2.31516 0.07910 YWHAQ 0.873107724496422 0.126549212880791 0.000343062622787922 tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein theta FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1. {ECO:0000269|PubMed:12177059}.; . TISSUE SPECIFICITY: Abundantly expressed in brain, heart and pancreas, and at lower levels in kidney and placenta. Up-regulated in the lumbar spinal cord from patients with sporadic amyotrophic lateral sclerosis (ALS) compared with controls, with highest levels of expression in individuals with predominant lower motor neuron involvement. {ECO:0000269|PubMed:11080204}.; smooth muscle;ovary;umbilical cord;skin;retina;bone marrow;prostate;frontal lobe;endometrium;gum;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;breast;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;vein;uterus;whole body;oesophagus;larynx;bone;testis;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;oral cavity;bile duct;pancreas;lung;cornea;adrenal gland;nasopharynx;placenta;head and neck;kidney;stomach;aorta; amygdala;whole brain;superior cervical ganglion;medulla oblongata;occipital lobe;thalamus;cerebellum peduncles;hypothalamus;pons;caudate nucleus;fetal brain;testis;globus pallidus;cingulate cortex;parietal lobe;cerebellum; 0.98109 0.60803 -0.075159878 47.78839349 3.40799 0.12457 YWHAQP1 . . . YWHAQ pseudogene 1 . . . . . . . . . . . YWHAQP2 . . . YWHAQ pseudogene 2 . . . . . . . . . . . YWHAQP3 . . . YWHAQ pseudogene 3 . . . . . . . . . . . YWHAQP4 . . . YWHAQ pseudogene 4 . . . . . . . . . . . YWHAQP5 . . . YWHAQ pseudogene 5 . . . . . . . . . . . YWHAQP6 . . . YWHAQ pseudogene 6 . . . . . . . . . . . YWHAQP7 . . . YWHAQ pseudogene 7 . . . . . . . . . . . YWHAQP8 . . . YWHAQ pseudogene 8 . . . . . . . . . . . YWHAQP9 . . . YWHAQ pseudogene 9 . . . . . . . . . . . YWHAZ 0.817170005056014 0.181916764827967 0.000913230116019108 tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. {ECO:0000269|PubMed:14578935, ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15644438, ECO:0000269|PubMed:16376338, ECO:0000269|PubMed:9360956}.; . . smooth muscle;ovary;sympathetic chain;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;bladder;brain;gall bladder;heart;tongue;pineal body;urinary;adrenal cortex;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;uterus;whole body;larynx;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;cornea;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta; thalamus;occipital lobe;subthalamic nucleus;globus pallidus;pons;trigeminal ganglion;skeletal muscle;cingulate cortex;parietal lobe; 0.99976 0.58572 0.079165051 59.43029016 1.06384 0.02718 YWHAZP1 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta pseudogene 1 . . . . . . . . . . . YWHAZP2 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta pseudogene 2 . . . . . . . . . . . YWHAZP3 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta pseudogene 3 . . . . . . . . . . . YWHAZP4 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta pseudogene 4 . . . . . . . . . . . YWHAZP5 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta pseudogene 5 . . . . . . . . . . . YWHAZP6 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta pseudogene 6 . . . . . . . . . . . YWHAZP7 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta pseudogene 7 . . . . . . . . . . . YWHAZP8 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta pseudogene 8 . . . . . . . . . . . YWHAZP9 . . . tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta pseudogene 9 . . . . . . . . . . . YY1 0.967830954926674 0.0321172287167004 5.18163566256434e-05 YY1 transcription factor FUNCTION: Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity. The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes. Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression. For example, it acts as a repressor in absence of adenovirus E1A protein but as an activator in its presence. Acts synergistically with the SMAD1 and SMAD4 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (PubMed:15329343). Binds to SMAD binding elements (SBEs) (5'- GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions. May play an important role in development and differentiation. Proposed to recruit the PRC2/EED-EZH2 complex to target genes that are transcriptional repressed. Involved in DNA repair. In vitro, binds to DNA recombination intermediate structures (Holliday junctions). {ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:24326773, ECO:0000269|PubMed:25787250}.; . . smooth muscle;ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;pharynx;blood;lung;cornea;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;cerebellum;thymus; amygdala;superior cervical ganglion;subthalamic nucleus;adrenal gland;thyroid;placenta;testis;atrioventricular node;skeletal muscle; 0.88914 0.54583 0.147123112 64.11299835 133.74597 2.51355 YY1AP1 0.000145221258212536 0.992011383388067 0.00784339535372093 YY1 associated protein 1 FUNCTION: Enhances transcription activation by YY1. May play a role in cell cycle regulation. {ECO:0000269|PubMed:14744866, ECO:0000269|PubMed:17541814}.; . TISSUE SPECIFICITY: Ubiquitous. Detected in small intestine, skeletal muscle, lung, pancreas, brain, stomach, spleen, colon and heart. Detected at very low levels in healthy liver. Highly expressed in most liver carcinomas. {ECO:0000269|PubMed:11710830, ECO:0000269|PubMed:12118372, ECO:0000269|PubMed:14744866}.; smooth muscle;ovary;colon;parathyroid;skin;retina;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;muscle;lens;skeletal muscle;breast;lung;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach;thymus; testis - interstitial;testis - seminiferous tubule;testis;white blood cells;atrioventricular node;trigeminal ganglion; 0.11332 0.08014 0.516238257 80.33734371 635.19949 5.07278 YY1P1 . . . YY1 transcription factor pseudogene 1 . . . . . . . . . . . YY1P2 . . . YY1 transcription factor pseudogene 2 . . . . . . . . . . . YY2 0.383414002511684 0.572417648074639 0.0441683494136772 YY2 transcription factor FUNCTION: Functions as a multifunctional transcription factor that may exhibit positive and negative control on a large number of genes. May antagonize YY1 and function in development and differentiation. {ECO:0000269|PubMed:16260628}.; . TISSUE SPECIFICITY: Expressed in kidney, liver, spleen and testis but not in colon. {ECO:0000269|PubMed:15087442}.; . . 0.11784 0.08955 -0.315847836 31.68789809 3.78538 0.14036 ZACN 1.96181645761295e-15 0.00200548500842895 0.997994514991569 zinc activated ion channel FUNCTION: Zinc-activated ligand-gated ion channel. {ECO:0000269|PubMed:12381728}.; . TISSUE SPECIFICITY: Detected in pancreas, brain, liver, placenta, trachea, kidney, spinal cord, stomach and fetal brain. In the adult brain region expression is detected in the hippocampus, striatum, amygdala and thalamus. {ECO:0000269|PubMed:12381728, ECO:0000269|PubMed:16083862}.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;synovium;bone;thyroid;testis;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;muscle;adrenal cortex;pharynx;blood;lens;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta; . 0.05331 . 0.624649618 83.53385232 1604.35347 7.41096 ZACNP1 . . . zinc activated ion channel pseudogene 1 . . . . . . . . . . . ZADH2 0.000446821227839176 0.422788351429313 0.576764827342848 zinc binding alcohol dehydrogenase domain containing 2 . . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;peripheral nerve; . 0.06781 0.09009 -0.179930907 40.35739561 207.63638 3.11185 ZAN 1.56059061227021e-43 1.34346190461778e-06 0.999998656538095 zonadhesin (gene/pseudogene) FUNCTION: Binds in a species-specific manner to the zona pellucida of the egg. May be involved in gamete recognition and/or signaling.; . TISSUE SPECIFICITY: In testis, primarily in haploid spermatids.; . . 0.04780 0.10303 . . . . ZAP70 0.272667248493713 0.727116434878453 0.000216316627833957 zeta chain of T cell receptor associated protein kinase 70kDa FUNCTION: Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates motility, adhesion and cytokine expression of mature T-cells, as well as thymocyte development. Contributes also to the development and activation of primary B-lymphocytes. When antigen presenting cells (APC) activate T-cell receptor (TCR), a serie of phosphorylations lead to the recruitment of ZAP70 to the doubly phosphorylated TCR component CD247/CD3Z through ITAM motif at the plasma membrane. This recruitment serves to localization to the stimulated TCR and to relieve its autoinhibited conformation. Release of ZAP70 active conformation is further stabilized by phosphorylation mediated by LCK. Subsequently, ZAP70 phosphorylates at least 2 essential adapter proteins: LAT and LCP2. In turn, a large number of signaling molecules are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Furthermore, ZAP70 controls cytoskeleton modifications, adhesion and mobility of T-lymphocytes, thus ensuring correct delivery of effectors to the APC. ZAP70 is also required for TCR-CD247/CD3Z internalization and degradation through interaction with the E3 ubiquitin-protein ligase CBL and adapter proteins SLA and SLA2. Thus, ZAP70 regulates both T-cell activation switch on and switch off by modulating TCR expression at the T-cell surface. During thymocyte development, ZAP70 promotes survival and cell-cycle progression of developing thymocytes before positive selection (when cells are still CD4/CD8 double negative). Additionally, ZAP70-dependent signaling pathway may also contribute to primary B-cells formation and activation through B-cell receptor (BCR). {ECO:0000269|PubMed:11353765, ECO:0000269|PubMed:1423621, ECO:0000269|PubMed:20135127, ECO:0000269|PubMed:8124727, ECO:0000269|PubMed:8702662, ECO:0000269|PubMed:9489702}.; DISEASE: Selective T-cell defect (STCD) [MIM:269840]: A form of severe combined immunodeficiency characterized by a selective absence of CD8+ T-cells. {ECO:0000269|PubMed:11123350, ECO:0000269|PubMed:11412303, ECO:0000269|PubMed:18509675, ECO:0000269|PubMed:8124727, ECO:0000269|PubMed:8202713}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in T- and natural killer cells. Also present in early thymocytes and pro/pre B-cells. {ECO:0000269|PubMed:1423621, ECO:0000269|PubMed:16467082, ECO:0000269|PubMed:9378960}.; unclassifiable (Anatomical System);lymph node;lung;visual apparatus;muscle;testis;colon;blood;kidney;skeletal muscle;thymus;bone marrow; thymus; 0.39339 0.62869 -1.155457828 6.168907761 54.21767 1.46999 ZAR1 0.0166840207254921 0.887403150367087 0.0959128289074205 zygote arrest 1 FUNCTION: Essential for female fertility. May play a role in the oocyte-to-embryo transition (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Ovary and testis. {ECO:0000269|PubMed:12539046}.; breast;lung;testis; . 0.10061 . . . 2470.33409 9.26024 ZAR1L . . . zygote arrest 1-like . . . . . . . 0.301449681 71.80938901 237.81878 3.33000 ZBBX 4.33160126727107e-11 0.769660264616843 0.230339735339841 zinc finger B-box domain containing . . . unclassifiable (Anatomical System);lung;endometrium;hippocampus;testis; testis - interstitial;testis - seminiferous tubule;testis;appendix; 0.03909 . 2.451071414 98.5727766 6633.89538 17.21951 ZBED1 0.00183309311469201 0.90104367631011 0.0971232305751977 zinc finger BED-type containing 1 FUNCTION: Binds to 5'-TGTCG[CT]GA[CT]A-3' DNA elements found in the promoter regions of a number of genes related to cell proliferation. Binds to the histone H1 promoter and stimulates transcription. Was first identified as gene weakly similar to Ac transposable elements, but does not code for any transposase activity. {ECO:0000269|PubMed:12663651}.; . TISSUE SPECIFICITY: Ubiquitously expressed at low levels. Expression is highest in skeletal muscle, heart, spleen and placenta.; . . 0.10071 0.16251 -2.190107324 1.38594008 57.4732 1.52832 ZBED1P1 . . . zinc finger BED-type containing 1 pseudogene 1 . . . . . . . . . . . ZBED2 0.00205866015297017 0.505847366198976 0.492093973648054 zinc finger BED-type containing 2 . . . lung;cartilage;germinal center; superior cervical ganglion;thyroid;trigeminal ganglion; 0.05332 . 0.350995466 74.37485256 71.94147 1.76580 ZBED3 0.0784364357896077 0.542786332508394 0.378777231701998 zinc finger BED-type containing 3 FUNCTION: Acts as a positive regulator in the activation of the canonical Wnt/beta-catenin signaling pathway by stabilizing cytoplasmic beta-catenin. Involved in transcription activation of Wnt target gene expression (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;colon;blood;lens;skin;retina;bone marrow;uterus;prostate;lung;nasopharynx;testis;cervix;head and neck;kidney;brain;stomach; superior cervical ganglion;liver; 0.09556 0.10109 . . 1615.06582 7.43796 ZBED3-AS1 . . . ZBED3 antisense RNA 1 . . . . . . . . . . . ZBED4 0.989506768385479 0.010492565906754 6.65707767469432e-07 zinc finger BED-type containing 4 . . TISSUE SPECIFICITY: Widely expressed with highest levels in testis, kidney and spinal cord and brain corpus callosum. Expressed in the retina, found in the cone photoreceptors, Mueller cells, cone pedicles and in the innermost retinal layer. {ECO:0000269|PubMed:19369242}.; lymphoreticular;myocardium;smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;muscle;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach; superior cervical ganglion;testis; 0.15042 0.10727 -1.313764723 4.824251003 82.71666 1.93200 ZBED5 . . . zinc finger BED-type containing 5 . . . . . . . . . 501.66995 4.59519 ZBED5-AS1 . . . ZBED5 antisense RNA 1 . . . . . . . . . . . ZBED6 . . . zinc finger BED-type containing 6 FUNCTION: Transcriptional repressor which binds to the consensus sequence 5'-GCTCGC-3' and represses transcription of IGF2. May also regulate expression of other target genes containing this consensus binding site (By similarity). {ECO:0000250}.; . . . . . . . . 3676.69122 11.79390 ZBED6CL 0.00292226219818059 0.580662889254728 0.416414848547092 ZBED6 C-terminal like . . . . . 0.14673 . 1.150157577 92.46874263 610.53376 4.99353 ZBED8 . . . zinc finger BED-type containing 8 . . . . . . . 0.332586472 73.61405992 . . ZBED9 . . . zinc finger BED-type containing 9 . . . . . 0.12969 0.09424 -0.949752638 9.32413305 . . ZBP1 1.29679362994319e-10 0.0513028052261339 0.948697194644187 Z-DNA binding protein 1 FUNCTION: Participates in the detection by the host's innate immune system of DNA from viral, bacterial or even host origin. Plays a role in host defense against tumors and pathogens. Acts as a cytoplasmic DNA sensor which, when activated, induces the recruitment of TBK1 and IRF3 to its C-terminal region and activates the downstream interferon regulatory factor (IRF) and NF-kappa B transcription factors, leading to type-I interferon production. ZBP1-induced NF-kappaB activation probably involves the recruitment of the RHIM containing kinases RIPK1 and RIPK3 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Highly expressed in lymphatic tissues including lymph node, leukocytes, tonsil, bone marrow and spleen. Expressed to a lesser extent in thymus, lung and liver.; unclassifiable (Anatomical System);oesophagus;colon;germinal center;skeletal muscle; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.09929 0.07153 3.02462456 99.22741213 2064.40551 8.36937 ZBTB1 0.973423963579882 0.0265694845925424 6.55182757602467e-06 zinc finger and BTB domain containing 1 FUNCTION: Acts as a transcriptional repressor. Represses cAMP- responsive element (CRE)-mediated transcriptional activation. Involved in lymphoid lineage commitment and differentiation. Plays a key role in the instruction of early lymphoid progenitors to develop into T-cell lineage. {ECO:0000269|PubMed:20797634, ECO:0000269|PubMed:21706167}.; . . unclassifiable (Anatomical System);lymph node;cartilage;ovary;lacrimal gland;islets of Langerhans;sympathetic chain;blood;skin;skeletal muscle;uterus;lung;endometrium;larynx;bone;placenta;visual apparatus;testis;head and neck;germinal center;kidney;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;white blood cells;trigeminal ganglion; 0.46339 0.10423 -0.247889024 35.98726115 429.66774 4.32847 ZBTB2 0.979834593773668 0.020149054424767 1.63518015648921e-05 zinc finger and BTB domain containing 2 FUNCTION: May be involved in transcriptional regulation.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;optic nerve;whole body;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland;stomach; superior cervical ganglion;trigeminal ganglion; 0.34224 0.10570 -1.001120478 8.321538099 17.44199 0.61131 ZBTB3 0.243280561450218 0.750008107843175 0.00671133070660633 zinc finger and BTB domain containing 3 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.52524 0.08668 0.220536484 68.38287332 795.74601 5.55965 ZBTB4 0.998490203413562 0.00150976770239681 2.88840408872269e-08 zinc finger and BTB domain containing 4 FUNCTION: Transcriptional repressor with bimodal DNA-binding specificity. Represses transcription in a methyl-CpG-dependent manner. Binds with a higher affinity to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' but can also bind to the non-methylated consensus sequence 5'-CTGCNA-3' also known as the consensus kaiso binding site (KBS). Can also bind specifically to a single methyl-CpG pair and can bind hemimethylated DNA but with a lower affinity compared to methylated DNA (PubMed:16354688). {ECO:0000269|PubMed:16354688}.; . . medulla oblongata;smooth muscle;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;epididymis;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;testis;spinal ganglion;artery;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;amnion;kidney;aorta;stomach;thymus;cerebellum; atrioventricular node;skeletal muscle;skin; 0.37830 0.08224 -0.10469683 45.64755839 312.5211 3.76241 ZBTB5 0.798455361479278 0.200350291657857 0.00119434686286468 zinc finger and BTB domain containing 5 FUNCTION: May be involved in transcriptional regulation.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;gum;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;mesenchyma;placenta;macula lutea;duodenum;liver;spleen;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;testis - interstitial;medulla oblongata;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.31659 0.11009 -0.44448505 24.46331682 723.50972 5.33928 ZBTB6 0.357932618205793 0.62962636393985 0.0124410178543574 zinc finger and BTB domain containing 6 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Widely expressed with highest levels in brain. {ECO:0000269|PubMed:7958847}.; . . 0.57016 0.10366 -0.249709319 35.74545883 38.81564 1.14915 ZBTB7A . . . zinc finger and BTB domain containing 7A FUNCTION: Plays a key role in the instruction of early lymphoid progenitors to develop into B lineage by repressing T-cell instructive Notch signals (By similarity). Specifically represses the transcription of the CDKN2A gene. Efficiently abrogates E2F1- dependent CDKN2A transactivation/de-repression. Binds to the consensus sequence 5'-[GA][CA]GACCCCCCCCC-3' (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Widely expressed. In normal thymus, expressed in medullary epithelial cells and Hassle's corpuscles (at protein level). In tonsil, expressed in squamous epithelium and germinal center lymphocytes (at protein level). Up-regulated in a subset of lymphomas, as well as in a subset of breast, lung, colon, prostate and bladder carcinomas (at protein level). {ECO:0000269|PubMed:15662416, ECO:0000269|PubMed:9927193}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;synovium;bone;thyroid;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;pancreas;lung;placenta;macula lutea;hippocampus;liver;spleen;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;medulla oblongata;cerebellum peduncles;temporal lobe;pons;atrioventricular node;skeletal muscle;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.19998 0.14742 . . 100.28121 2.16983 ZBTB7B 0.837393370882557 0.161942431778246 0.000664197339196359 zinc finger and BTB domain containing 7B FUNCTION: Transcription regulator that acts as a key regulator of lineage commitment of immature T-cell precursors. Necessary and sufficient for commitment of CD4 lineage, while its absence causes CD8 commitment. Development of immature T-cell precursors (thymocytes) to either the CD4 helper or CD8 killer T-cell lineages correlates precisely with their T-cell receptor specificity for major histocompatibility complex class II or class I molecules, respectively. Transcriptional repressor of the collagen COL1A1 and COL1A2 genes. May also function as a repressor of fibronectin and possibly other extracellular matrix genes (By similarity). {ECO:0000250, ECO:0000269|PubMed:9370309}.; . . unclassifiable (Anatomical System);urinary;muscle;blood;skin;bone marrow;uterus;prostate;lung;cerebral cortex;placenta;bone;duodenum;cervix;spinal ganglion;brain;mammary gland; pons;cingulate cortex;parietal lobe;skeletal muscle; 0.35581 0.12203 -0.644723694 16.52512385 68.89593 1.71970 ZBTB7C 0.907221460237709 0.092039708366928 0.000738831395363062 zinc finger and BTB domain containing 7C FUNCTION: May be a tumor suppressor gene. {ECO:0000269|PubMed:9427755}.; . . unclassifiable (Anatomical System);whole body;colon;cervix;lens;mammary gland;skin; subthalamic nucleus;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.32344 0.11748 -0.176292081 40.56381222 860.08699 5.71993 ZBTB8A 0.106372648345456 0.886926318170315 0.00670103348422835 zinc finger and BTB domain containing 8A FUNCTION: May be involved in transcriptional regulation.; . . medulla oblongata;choroid;fovea centralis;retina;uterus;prostate;optic nerve;thyroid;bone;testis;bladder;brain;unclassifiable (Anatomical System);islets of Langerhans;lens;skeletal muscle;breast;lung;visual apparatus;macula lutea;liver;duodenum;spleen;head and neck;kidney;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.40197 . -0.492218069 22.35786742 33.31861 1.02959 ZBTB8B 0.360954124529864 0.482249625523856 0.15679624994628 zinc finger and BTB domain containing 8B FUNCTION: May be involved in transcriptional regulation.; . . . . . . 0.125076652 62.7388535 46.50883 1.31607 ZBTB8OS 0.95574935791171 0.0441362007395956 0.000114441348694328 zinc finger and BTB domain containing 8 opposite strand FUNCTION: Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB. Together with DDX1, acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation. {ECO:0000269|PubMed:24870230}.; . . unclassifiable (Anatomical System);breast;prostate;lung;thyroid;liver;testis;head and neck;kidney;bladder;skeletal muscle;stomach; . 0.56682 0.11083 0.125076652 62.7388535 14.67483 0.52902 ZBTB8OSP1 . . . zinc finger and BTB domain containing 8 opposite strand pseudogene 1 . . . . . . . . . . . ZBTB8OSP2 . . . zinc finger and BTB domain containing 8 opposite strand pseudogene 2 . . . . . . . . . . . ZBTB9 0.0121593630542635 0.851312464699682 0.136528172246055 zinc finger and BTB domain containing 9 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.17725 . 0.52918614 80.81505072 451.65909 4.41905 ZBTB10 0.881586182628026 0.118402037683155 1.17796888186412e-05 zinc finger and BTB domain containing 10 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.67263 0.09781 -0.159704656 41.90846898 934.6613 5.92702 ZBTB11 0.269451352114294 0.730548274777685 3.73108021056797e-07 zinc finger and BTB domain containing 11 FUNCTION: May be involved in transcriptional regulation.; . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;skin;retina;uterus;prostate;atrium;endometrium;larynx;thyroid;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;liver;alveolus;head and neck;kidney;mammary gland;stomach; amygdala;superior cervical ganglion;medulla oblongata;trigeminal ganglion;parietal lobe; 0.34953 0.12561 -1.304353358 4.91861288 204.98506 3.09279 ZBTB11-AS1 . . . ZBTB11 antisense RNA 1 . . . . . . . . . . . ZBTB12 0.807401018591612 0.187646814017579 0.00495216739080895 zinc finger and BTB domain containing 12 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.17864 . 0.038710339 56.92380278 490.68465 4.55951 ZBTB12BP . . . zinc finger and BTB domain containing 12B, pseudogene . . . . . . . . . . . ZBTB14 0.628505782225752 0.364269932498248 0.00722428527599966 zinc finger and BTB domain containing 14 FUNCTION: Transcriptional activator of the dopamine transporter (DAT), binding it's promoter at the consensus sequence 5'- CCTGCACAGTTCACGGA-3'. Binds to 5'-d(GCC)(n)-3' trinucleotide repeats in promoter regions and acts as a repressor of the FMR1 gene. Transcriptional repressor of MYC and thymidine kinase promoters. {ECO:0000269|PubMed:17714511}.; . . . . 0.29705 0.15588 -0.560178693 19.30879925 3.68851 0.13646 ZBTB16 0.980087305825708 0.0199094816777126 3.21249657982963e-06 zinc finger and BTB domain containing 16 FUNCTION: Probable transcription factor. May play a role in myeloid maturation and in the development and/or maintenance of other differentiated tissues. Probable substrate-recognition component of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000269|PubMed:14528312}.; DISEASE: Skeletal defects, genital hypoplasia, and mental retardation (SGYMR) [MIM:612447]: A disorder characterized by mental retardation, craniofacial dysmorphism, microcephaly and short stature. Additional features include absence of the thumbs, hypoplasia of the radii and ulnae, additional vertebrae and ribs, retarded bone age and genital hypoplasia. {ECO:0000269|PubMed:18611983}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving ZBTB16 may be a cause of acute promyelocytic leukemia (APL). Translocation t(11;17)(q32;q21) with RARA. {ECO:0000269|PubMed:8384553}.; TISSUE SPECIFICITY: Within the hematopoietic system, PLZF is expressed in bone marrow, early myeloid cell lines and peripheral blood mononuclear cells. Also expressed in the ovary, and at lower levels, in the kidney and lung.; colon;parathyroid;fovea centralis;choroid;bone marrow;retina;prostate;optic nerve;whole body;frontal lobe;thyroid;testis;pineal gland;brain;unclassifiable (Anatomical System);cartilage;tongue;adrenal cortex;blood;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;spleen;kidney; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.80774 0.50124 -0.800872469 12.33191791 23.01349 0.76772 ZBTB17 0.998165364992239 0.00183462560805662 9.39970432228122e-09 zinc finger and BTB domain containing 17 FUNCTION: Transcription factor that can function as an activator or repressor depending on its binding partners, and by targeting negative regulators of cell cycle progression. Plays a critical role in early lymphocyte development, where it is essential to prevent apoptosis in lymphoid precursors, allowing them to survive in response to IL7 and undergo proper lineage commitment. Has been shown to bind to the promoters of adenovirus major late protein and cyclin D1 and activate transcription. Required for early embryonic development during gastrulation. Represses RB1 transcription; this repression can be blocked by interaction with ZBTB49 isoform 3/ZNF509S1 (PubMed:25245946). {ECO:0000269|PubMed:16142238, ECO:0000269|PubMed:19164764, ECO:0000269|PubMed:25245946, ECO:0000269|PubMed:9308237, ECO:0000269|PubMed:9312026}.; . TISSUE SPECIFICITY: Expressed in germinal center B-cells. {ECO:0000269|PubMed:16142238}.; . . 0.91930 0.14584 -0.688817379 15.20405756 70.88543 1.75315 ZBTB18 0.97012354907433 0.02983330343554 4.31474901302405e-05 zinc finger and BTB domain containing 18 FUNCTION: Transcriptional repressor that plays a role in various developmental processes such as myogenesis and brain development. Plays a key role in myogenesis by directly repressing the expression of ID2 and ID3, 2 inhibitors of skeletal myogenesis. Also involved in controlling cell division of progenitor cells and regulating the survival of postmitotic cortical neurons. Specifically binds the consensus DNA sequence 5'- [AC]ACATCTG[GT][AC]-3' which contains the E box core, and acts by recruiting chromatin remodeling multiprotein complexes. May also play a role in the organization of chromosomes in the nucleus. {ECO:0000269|PubMed:9756912}.; . TISSUE SPECIFICITY: Lymphoid tissues, testis, heart, brain, skeletal muscle, and pancreas and, at much lower level, other tissues.; . . 0.95857 0.12137 -0.780646273 12.77423921 23.54663 0.78205 ZBTB20 0.982557230407655 0.0174313259937457 1.14435985995889e-05 zinc finger and BTB domain containing 20 FUNCTION: May be a transcription factor that may be involved in hematopoiesis, oncogenesis, and immune responses. {ECO:0000269|PubMed:11352661}.; DISEASE: Primrose syndrome (PRIMS) [MIM:259050]: A disease characterized by macrocephaly, intellectual disability, disturbed behavior, dysmorphic facial features, ectopic calcifications, large calcified ear auricles, and progressive muscle wasting. {ECO:0000269|PubMed:25017102}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in spleen, lymph node, thymus, peripheral blood leukocytes, and fetal liver. {ECO:0000269|PubMed:11352661}.; medulla oblongata;ovary;colon;choroid;fovea centralis;skin;bone marrow;retina;prostate;optic nerve;iris;testis;brain;unclassifiable (Anatomical System);cartilage;hypothalamus;pineal body;blood;lens;skeletal muscle;lung;nasopharynx;hippocampus;macula lutea;kidney;stomach;peripheral nerve; uterus;prostate;testis - interstitial;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;pituitary; 0.82236 0.15072 0.352813824 74.49280491 125.54254 2.43894 ZBTB20-AS1 . . . ZBTB20 antisense RNA 1 . . . . . . . . . . . ZBTB20-AS2 . . . ZBTB20 antisense RNA 2 . . . . . . . . . . . ZBTB20-AS3 . . . ZBTB20 antisense RNA 3 . . . . . . . . . . . ZBTB20-AS4 . . . ZBTB20 antisense RNA 4 . . . . . . . . . . . ZBTB21 0.986130663064607 0.0138680172412707 1.31969412205056e-06 zinc finger and BTB domain containing 21 FUNCTION: Acts as a transcription repressor. {ECO:0000269|PubMed:15629158}.; . TISSUE SPECIFICITY: Ubiquitous in fetal and adult tissues. {ECO:0000269|PubMed:15629158}.; . . 0.31535 0.11057 -0.101059488 45.67704647 2367.6284 9.03401 ZBTB22 0.235099436717728 0.757674570701696 0.00722599258057648 zinc finger and BTB domain containing 22 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.16750 0.09413 0.176444282 66.07100731 122.27381 2.40790 ZBTB24 0.000201035360458764 0.976418507994111 0.0233804566454301 zinc finger and BTB domain containing 24 FUNCTION: May be involved in BMP2-induced transcription. {ECO:0000250}.; DISEASE: Immunodeficiency-centromeric instability-facial anomalies syndrome 2 (ICF2) [MIM:614069]: A rare disorder characterized by a variable immunodeficiency resulting in recurrent infections, facial anomalies, and branching of chromosomes 1, 9, and 16. Other variable symptoms include growth retardation, failure to thrive, and psychomotor retardation. Laboratory studies show limited hypomethylation of DNA in a small fraction of the genome in some, but not all, patients. {ECO:0000269|PubMed:21596365}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed, with highest levels in naive B-cells. {ECO:0000269|PubMed:21596365}.; colon;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;endometrium;bone;testis;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skin; 0.36101 0.10321 -0.110153916 45.48832272 382.25698 4.12229 ZBTB25 3.31068569517812e-05 0.575347181746482 0.424619711396566 zinc finger and BTB domain containing 25 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Expressed mainly in hematopoietic cells and testis.; unclassifiable (Anatomical System);cartilage;ovary;heart;salivary gland;intestine;pharynx;colon;blood;skin;breast;uterus;bile duct;prostate;lung;visual apparatus;liver;kidney;brain;bladder; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.11197 0.09182 -0.336073593 30.55555556 139.41045 2.57459 ZBTB26 0.0154751252760809 0.879869577519644 0.104655297204275 zinc finger and BTB domain containing 26 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.41480 0.11262 -0.139478553 43.29440906 46.52369 1.31667 ZBTB32 0.0162101668651277 0.959333868992186 0.0244559641426866 zinc finger and BTB domain containing 32 FUNCTION: DNA-binding protein that binds to the to a 5'- TGTACAGTGT-3' core sequence. May function as a transcriptional transactivator and transcriptional repressor. Probably exerts its repressor effect by preventing GATA3 from binding to DNA. May play a role in regulating the differentiation and activation of helper T-cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:10572087}.; . TISSUE SPECIFICITY: Predominantly expressed in testis. Some isoforms are ubiquitously expressed. {ECO:0000269|PubMed:10544010}.; unclassifiable (Anatomical System);medulla oblongata;lung;ovary;thyroid;hippocampus;testis;blood; testis - interstitial;testis - seminiferous tubule;testis;trigeminal ganglion; 0.14539 0.24697 0.196671391 67.19155461 196.73896 3.03301 ZBTB33 0.893444537354356 0.105502289943684 0.00105317270196056 zinc finger and BTB domain containing 33 FUNCTION: Transcriptional regulator with bimodal DNA-binding specificity. Binds to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' and also binds to the non-methylated consensus sequence 5'-CTGCNA-3' also known as the consensus kaiso binding site (KBS). Recruits the N-CoR repressor complex to promote histone deacetylation and the formation of repressive chromatin structures in target gene promoters. May contribute to the repression of target genes of the Wnt signaling pathway. May also activate transcription of a subset of target genes by the recruitment of CTNND2. Represses expression of MMP7 in conjunction with transcriptional corepressors CBFA2T3, CBFA2T2 and RUNX1T1 (PubMed:23251453). {ECO:0000269|PubMed:11445535, ECO:0000269|PubMed:14527417, ECO:0000269|PubMed:15548582, ECO:0000269|PubMed:15817151, ECO:0000269|PubMed:16354688, ECO:0000269|PubMed:23251453}.; . TISSUE SPECIFICITY: Expressed in vascular endothelium. {ECO:0000269|PubMed:14699141}.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;oral cavity;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach; skeletal muscle; 0.64457 0.12959 0.238945317 69.20853975 123.82121 2.42223 ZBTB34 0.829622812482223 0.169623600974739 0.000753586543038273 zinc finger and BTB domain containing 34 FUNCTION: May be a transcriptional repressor. {ECO:0000269|PubMed:16718364}.; . TISSUE SPECIFICITY: Expressed in several tissues, including heart, brain, thymus, skeletal muscle, small intestine, testis, kidney, placenta, peripheral blood cells and adult and fetal liver. {ECO:0000269|PubMed:16718364}.; unclassifiable (Anatomical System);prostate; superior cervical ganglion;liver;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.60593 0.11262 -0.824740496 11.67728238 36.30996 1.08767 ZBTB37 0.734036618249105 0.263340458248947 0.00262292350194844 zinc finger and BTB domain containing 37 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.13119 . 0.082802743 60.09082331 34.60294 1.05584 ZBTB38 0.97949144936684 0.0205078513734997 6.99259660708454e-07 zinc finger and BTB domain containing 38 FUNCTION: Transcriptional regulator with bimodal DNA-binding specificity. Binds with a higher affinity to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' but can also bind to E-box elements (5'-CACGTG-3'). Can also bind specifically to a single methyl-CpG pair. Represses transcription in a methyl- CpG-dependent manner (PubMed:16354688). Plays an important role in regulating DNA replication and common fragile sites (CFS) stability in a RBBP6- and MCM10-dependent manner; represses expression of MCM10 which plays an important role in DNA- replication (PubMed:24726359). Acts as a transcriptional activator. May be involved in the differentiation and/or survival of late postmitotic neurons (By similarity). {ECO:0000250|UniProtKB:Q5EXX3, ECO:0000269|PubMed:16354688, ECO:0000269|PubMed:24726359}.; . . . . 0.47614 0.10684 0.027580343 55.8091531 1031.00322 6.16647 ZBTB39 0.00973093010397182 0.941637742554256 0.0486313273417718 zinc finger and BTB domain containing 39 FUNCTION: May be involved in transcriptional regulation.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;thyroid;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;adrenal cortex;pharynx;blood;lens;breast;lung;adrenal gland;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.39491 . -0.174473069 40.59919792 339.43935 3.90739 ZBTB40 1.21207769768767e-05 0.999514312332203 0.000473566890819946 zinc finger and BTB domain containing 40 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.32352 0.10243 -0.637452658 16.73743808 474.46994 4.50153 ZBTB40-IT1 . . . ZBTB40 intronic transcript 1 . . . . . . . . . . . ZBTB41 0.76962740291043 0.230369631417214 2.96567235524576e-06 zinc finger and BTB domain containing 41 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.35189 . -0.400392389 26.85185185 643.53042 5.09713 ZBTB42 . . . zinc finger and BTB domain containing 42 FUNCTION: Transcriptional repressor. Specifically binds DNA and probably acts by recruiting chromatin remodeling multiprotein complexes. {ECO:0000250|UniProtKB:Q811H0}.; . TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level). {ECO:0000269|PubMed:21193930}.; stomach; . . . 0.768075923 86.8895966 146.30778 2.63567 ZBTB43 0.877041935440621 0.121434588126222 0.00152347643315735 zinc finger and BTB domain containing 43 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.54113 0.11017 -0.247889024 35.98726115 25.7282 0.83744 ZBTB44 0.992064123809693 0.00793421687993688 1.65931037021672e-06 zinc finger and BTB domain containing 44 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . medulla oblongata;ovary;skin;retina;bone marrow;prostate;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;bladder;amygdala;heart;cartilage;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;bone;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;adrenal gland;placenta;duodenum;kidney;stomach;aorta;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09955 0.10718 -0.448125345 24.19202642 . . ZBTB45 0.0266369804255781 0.919885745077432 0.0534772744969894 zinc finger and BTB domain containing 45 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lymph node;cartilage;ovary;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;lung;bone;placenta;macula lutea;iris;spleen;brain;mammary gland;stomach;thymus; skeletal muscle; 0.09541 0.10851 -0.378346116 28.01368247 50.39528 1.39587 ZBTB45P1 . . . zinc finger and BTB domain containing 45 pseudogene 1 . . . . . . . . . . . ZBTB45P2 . . . zinc finger and BTB domain containing 45 pseudogene 2 . . . . . . . . . . . ZBTB46 0.814437307571674 0.185523281309742 3.94111185838044e-05 zinc finger and BTB domain containing 46 FUNCTION: Function as a transcriptional repressor for PRDM1. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;skin;bone marrow;retina;uterus;pancreas;lung;placenta;bone;iris;liver;testis;spleen;cervix;kidney;brain;cerebellum; . 0.26482 . -0.863377021 10.84571833 188.86698 2.98418 ZBTB46-AS1 . . . ZBTB46 antisense RNA 1 . . . . . . . . . . . ZBTB47 0.974750217387723 0.0252213160566072 2.84665556698105e-05 zinc finger and BTB domain containing 47 FUNCTION: May be involved in transcriptional regulation.; . . smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;muscle;lens;skeletal muscle;pancreas;lung;visual apparatus;macula lutea;kidney;stomach; globus pallidus;trigeminal ganglion; 0.45353 0.09193 -0.049474214 50.01179523 292.95154 3.65909 ZBTB48 0.680198376469515 0.319762725717166 3.8897813318813e-05 zinc finger and BTB domain containing 48 FUNCTION: Binds to and regulates the J and/or S elements in MHC II promoter. {ECO:0000269|PubMed:7969177}.; . TISSUE SPECIFICITY: Detected in adrenal gland and neuroblastoma. {ECO:0000269|PubMed:9516840}.; unclassifiable (Anatomical System);lymphoreticular;pancreas;lung;endometrium;testis;colon;spleen;brain; testis - seminiferous tubule;thyroid;testis; 0.12946 0.15508 -0.997481928 8.47487615 221.08691 3.21629 ZBTB49 0.00916415492518601 0.988393630208991 0.00244221486582325 zinc finger and BTB domain containing 49 FUNCTION: Transcription factor. Inhibits cell proliferation by activating either CDKN1A/p21 transcription or RB1 transcription. {ECO:0000269|PubMed:25245946}.; FUNCTION: Isoform 3: Activates RB1 transcription most probably by antagonizing ZBTB17 repression of RB1. Does not bind directly RB1 promoter. {ECO:0000269|PubMed:25245946}.; . TISSUE SPECIFICITY: Highly expressed in normal epidermis and in other epithelial tissues, including in colon and lung. Tends to be down-regulated in colon, lung and skin cancer tissues. {ECO:0000269|PubMed:25245946}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;nervous;parathyroid;skin;retina;pancreas;prostate;whole body;lung;endometrium;placenta;thyroid;visual apparatus;testis;germinal center;kidney;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin;cerebellum; 0.13097 . 1.09310945 91.90846898 725.33362 5.34612 ZC2HC1A 0.811433032279189 0.188363776057852 0.000203191662958936 zinc finger C2HC-type containing 1A . . . . . 0.33643 0.10400 0.018483465 55.44939844 78.18262 1.86496 ZC2HC1B . . . zinc finger C2HC-type containing 1B . . . . . 0.36464 . 0.367590509 74.75819769 139.86973 2.58021 ZC2HC1C 1.62188208850506e-06 0.412507728273835 0.587490649844076 zinc finger C2HC-type containing 1C . . . . . 0.02123 0.05667 0.396906589 76.30927105 181.22376 2.92673 ZC3H3 0.96453876461509 0.0354585222433876 2.71314152217562e-06 zinc finger CCCH-type containing 3 FUNCTION: Required for the export of polyadenylated mRNAs from the nucleus (PubMed:19364924). Enhances ACVR1B-induced SMAD-dependent transcription. Binds to single-stranded DNA but not to double- stranded DNA in vitro. Involved in RNA cleavage (By similarity). {ECO:0000250|UniProtKB:Q8CHP0, ECO:0000269|PubMed:19364924}.; . . ovary;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;thyroid;bone;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;lens;pancreas;lung;hippocampus;visual apparatus;macula lutea;liver;cervix; superior cervical ganglion;testis - interstitial;testis;pons; 0.11131 0.09598 2.682723424 98.86175985 8599.54269 20.05767 ZC3H4 0.999999772424525 2.2757547526399e-07 1.41417269554919e-17 zinc finger CCCH-type containing 4 . . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;optic nerve;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;tongue;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;stomach; superior cervical ganglion;cerebellum peduncles;prefrontal cortex;testis;ciliary ganglion;atrioventricular node;cingulate cortex;skeletal muscle;cerebellum;thymus; 0.40007 . -1.320975027 4.777070064 637.42325 5.07993 ZC3H6 0.938245509196475 0.0617522844841495 2.20631937510684e-06 zinc finger CCCH-type containing 6 . . . unclassifiable (Anatomical System);heart;ovary;parathyroid;skin;bone marrow;uterus;breast;prostate;lung;endometrium;bone;placenta;germinal center;kidney;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.47887 0.09483 -0.574945567 18.90186365 193.22334 3.01297 ZC3H7A 0.999987024834243 1.29751657460084e-05 1.09642258757217e-14 zinc finger CCCH-type containing 7A . . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;greater omentum;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.39774 0.10813 -0.394936437 27.02878037 720.54271 5.33018 ZC3H7B 0.990761551309557 0.0092384478734851 8.16957469670937e-10 zinc finger CCCH-type containing 7B . . . smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;muscle;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;alveolus;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.75686 0.09986 -1.190479796 5.874026893 417.04401 4.27407 ZC3H8 0.464854053485364 0.529538959622075 0.00560698689256096 zinc finger CCCH-type containing 8 FUNCTION: Acts as a transcriptional repressor of the GATA3 promoter. Sequence-specific DNA-binding factor that binds to the 5'-AGGTCTC-3' sequence within the negative cis-acting element intronic regulatory region (IRR) of the GATA3 gene (By similarity). Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:23932780). Induces thymocyte apoptosis when overexpressed, which may indicate a role in regulation of thymocyte homeostasis. {ECO:0000250, ECO:0000269|PubMed:12077251, ECO:0000269|PubMed:12153508, ECO:0000269|PubMed:23932780}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;whole body;cochlea;thyroid;pituitary gland;testis;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);cartilage;heart;adrenal cortex;pharynx;blood;skeletal muscle;breast;lung;adrenal gland;nasopharynx;placenta;visual apparatus;liver;cervix;kidney; superior cervical ganglion;testis - seminiferous tubule;atrioventricular node;trigeminal ganglion; 0.48023 . 0.215080721 67.91696155 18.91348 0.65292 ZC3H10 0.792020464408796 0.206676185388116 0.00130335020308771 zinc finger CCCH-type containing 10 . . . unclassifiable (Anatomical System);medulla oblongata;cartilage;heart;ovary;muscle;adrenal cortex;colon;blood;skin;skeletal muscle;uterus;prostate;lung;endometrium;bone;thyroid;placenta;testis;cervix;kidney;spinal ganglion;brain;mammary gland;stomach; . 0.49259 0.10751 -0.181750739 40.15687662 41.86732 1.21973 ZC3H11A 0.997151604742134 0.00284839413247914 1.12538719703843e-09 zinc finger CCCH-type containing 11A FUNCTION: Involved in nuclear mRNA export; probably mediated by assoociation with the TREX complex. {ECO:0000269|PubMed:22928037}.; . . smooth muscle;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;iris;germinal center;brain;gall bladder;heart;cartilage;spinal cord;adrenal cortex;blood;lens;skeletal muscle;breast;macula lutea;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;bile duct;pancreas;lung;adrenal gland;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.08511 -0.332434268 30.74427931 116.03234 2.34343 ZC3H11B . . . zinc finger CCCH-type containing 11B pseudogene . . . . . . . . . . . ZC3H12A 0.91163271519429 0.0883401014370311 2.71833686788912e-05 zinc finger CCCH-type containing 12A FUNCTION: Has RNase activity and selectively degrades specific target mRNA species. Modulates the immune response and inflammation by regulating the decay of specific mRNA molecules. Recognizes the 3'-untranslated region (UTR) of the mRNA for IL6, CALCR and IL12B. Required for normal decay of IL6 mRNA (By similarity). Triggers apoptosis and promotes angiogenesis in response to the binding of CCL2 to CCR2. Regulates expression of CDH12 and CHD19. {ECO:0000250, ECO:0000269|PubMed:16574901, ECO:0000269|PubMed:18364357, ECO:0000269|PubMed:22561375}.; . . . . 0.29968 0.12271 0.668743049 84.68388771 236.68129 3.32235 ZC3H12B 0.972148733086522 0.0278439092163373 7.35769714055976e-06 zinc finger CCCH-type containing 12B FUNCTION: May function as RNase and regulate the levels of target RNA species. {ECO:0000305}.; . . unclassifiable (Anatomical System);lung;heart;islets of Langerhans;liver;testis;colon;spleen;brain;skeletal muscle;thymus; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.33864 0.09647 -0.471992905 23.03609342 1960.39142 8.15363 ZC3H12C 0.998726025413791 0.00127397072291316 3.86329580970568e-09 zinc finger CCCH-type containing 12C FUNCTION: May function as RNase and regulate the levels of target RNA species. {ECO:0000305}.; . . unclassifiable (Anatomical System);amygdala;lymphoreticular;heart;ovary;lacrimal gland;islets of Langerhans;colon;parathyroid;skin;skeletal muscle;retina;uterus;lung;thyroid;placenta;liver;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.18508 0.10734 -0.731092527 14.13658882 252.6555 3.42081 ZC3H12D 0.727798125573567 0.269395432817678 0.00280644160875522 zinc finger CCCH-type containing 12D FUNCTION: May regulate cell growth likely by suppressing RB1 phosphorylation. May function as RNase and regulate the levels of target RNA species (Potential). Serve as a tumor suppressor in certain leukemia cells. Overexpression inhibits the G1 to S phase progression through suppression of RB1 phosphorylation. {ECO:0000269|PubMed:17210687, ECO:0000269|PubMed:19531561, ECO:0000305}.; DISEASE: Note=A chromosomal aberration involving ZC3H12D may be the cause of the transformation of follicular lymphoma (FL) to diffuse large B-cell lymphoma (DLBCL). Translocation t(2;6)(p12;q25) with IGK. Resulting protein may not be expressed.; TISSUE SPECIFICITY: Expressed in normal human lymphocytes but defective in some leukemia/lymphoma cell lines. {ECO:0000269|PubMed:19531561}.; . . 0.05201 0.10680 . . 2835.63302 10.06217 ZC3H13 0.99999999999964 3.60299951791113e-13 1.7617185659258e-34 zinc finger CCCH-type containing 13 FUNCTION: Acts as component of the WTAP complex that is involved in RNA processing and cell cycle (PubMed:24100041). {ECO:0000269|PubMed:24100041}.; . . ovary;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;cochlea;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;heart;islets of Langerhans;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;liver;duodenum;cervix;spleen;head and neck;kidney;mammary gland;stomach; occipital lobe;superior cervical ganglion;appendix;ciliary ganglion;trigeminal ganglion;skeletal muscle;parietal lobe; 0.47654 0.10188 -0.251753628 35.00235905 214.6182 3.15985 ZC3H14 0.999785297023323 0.000214702966474429 1.02025714917177e-11 zinc finger CCCH-type containing 14 FUNCTION: Involved in poly(A) tail length control in neuronal cells. Binds the polyadenosine RNA oligonucleotides. {ECO:0000269|PubMed:17630287, ECO:0000269|PubMed:24671764}.; . . medulla oblongata;ovary;skin;bone marrow;retina;prostate;endometrium;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;pineal body;urinary;adrenal cortex;pharynx;blood;skeletal muscle;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hippocampus;duodenum;head and neck;kidney;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;prefrontal cortex;testis;atrioventricular node;trigeminal ganglion; 0.42802 0.12096 -0.642904474 16.62538335 58.81473 1.55619 ZC3H15 0.947515648259226 0.0524486565922154 3.56951485591169e-05 zinc finger CCCH-type containing 15 FUNCTION: Protects DRG1 from proteolytic degradation. {ECO:0000250}.; . . smooth muscle;ovary;developmental;colon;parathyroid;fovea centralis;vein;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; amygdala;superior cervical ganglion;occipital lobe;globus pallidus;white blood cells;trigeminal ganglion;cingulate cortex; 0.80077 0.11646 -0.161524709 41.6430762 22.98157 0.76587 ZC3H18 0.999519575544442 0.000480424440868919 1.46888604997855e-11 zinc finger CCCH-type containing 18 . . . lymphoreticular;ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;iris;testis;amniotic fluid;germinal center;spinal ganglion;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;pancreas;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;spleen;kidney;mammary gland;stomach;cerebellum; . 0.43206 0.10643 -1.322782544 4.759377212 160.96943 2.77056 ZC3H18-AS1 . . . ZC3H18 antisense RNA 1 (head to head) . . . . . 0.13489 . . . . . ZC3HAV1 0.0218726180746054 0.977989275986314 0.00013810593908023 zinc finger CCCH-type containing, antiviral 1 FUNCTION: Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)- specific ribonuclease PARN to remove the poly(A) tail, and the 3'- 5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1), moloney and murine leukemia virus (MoMLV) and xenotropic MuLV-related virus (XMRV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation. Isoform 1 is a more potent viral inhibitor than isoform 2. Isoform 2 acts as a positive regulator of DDX58/RIG-I signaling resulting in activation of the downstream effector IRF3 leading to the expression of type I IFNs and IFN stimulated genes (ISGs). {ECO:0000269|PubMed:18225958, ECO:0000269|PubMed:21102435, ECO:0000269|PubMed:21876179, ECO:0000269|PubMed:22720057}.; . . smooth muscle;ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;spinal cord;pharynx;blood;lens;skeletal muscle;breast;bile duct;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;hypopharynx;liver;cervix;spleen;head and neck;kidney;mammary gland;aorta;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.07701 0.08086 0.718303761 85.85161595 322.19699 3.81020 ZC3HAV1L 0.0417616097396591 0.845421766155115 0.112816624105226 zinc finger CCCH-type containing, antiviral 1 like . . . unclassifiable (Anatomical System);uterus;lacrimal gland;placenta;liver;testis;spleen;blood;skin; . 0.17075 . . . 328.16934 3.85043 ZC3HC1 0.000510516198199949 0.998179913302684 0.00130957049911596 zinc finger C3HC-type containing 1 FUNCTION: Essential component of an SCF-type E3 ligase complex, SCF(NIPA), a complex that controls mitotic entry by mediating ubiquitination and subsequent degradation of cyclin B1 (CCNB1). Its cell-cycle-dependent phosphorylation regulates the assembly of the SCF(NIPA) complex, restricting CCNB1 ubiquitination activity to interphase. Its inactivation results in nuclear accumulation of CCNB1 in interphase and premature mitotic entry. May have an antiapoptotic role in NPM-ALK-mediated signaling events. {ECO:0000269|PubMed:16009132}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart, skeletal muscle and testis. Expressed in brain, placenta, lung, kidney, liver, pancreas, spleen, thymus, prostate, ovary small intestine and colon. Weakly or not expressed in leukocytes. {ECO:0000269|PubMed:12748172}.; lymphoreticular;medulla oblongata;umbilical cord;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;bladder;brain;heart;cartilage;urinary;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;choroid;fovea centralis;vein;uterus;whole body;bone;testis;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;pancreas;lung;nasopharynx;placenta;head and neck;kidney;stomach; superior cervical ganglion;testis - interstitial;testis;ciliary ganglion; 0.18560 . 0.242582624 69.45623968 3942.67551 12.41332 ZC4H2 0.825852220957158 0.170359334723242 0.00378844431959993 zinc finger C4H2-type containing FUNCTION: May play a role in neuronal development and in neuromuscular junction formation. {ECO:0000269|PubMed:23623388}.; . TISSUE SPECIFICITY: Expressed in fetal tissues, including in brain, intestine, lung, kidney and muscle. {ECO:0000269|PubMed:23623388}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;muscle;lens;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach;aorta;thymus; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.24538 0.11262 -0.029247611 51.40363293 5.81759 0.21928 ZCCHC2 0.305659357295976 0.694176650525625 0.000163992178398912 zinc finger CCHC-type containing 2 . . . unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;blood;skin;skeletal muscle;bone marrow;breast;uterus;prostate;lung;frontal lobe;endometrium;placenta;liver;testis;spleen;kidney;brain; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.43340 0.10223 0.336225928 73.67893371 222.69353 3.22655 ZCCHC3 . . . zinc finger CCHC-type containing 3 . . . . . 0.16002 . . . 23.74994 0.78471 ZCCHC4 3.21958379232717e-05 0.986356162547822 0.0136116416142547 zinc finger CCHC-type containing 4 FUNCTION: May be a methyltransferase.; . . unclassifiable (Anatomical System);umbilical cord;colon;blood;skin;skeletal muscle;breast;prostate;whole body;lung;endometrium;placenta;liver;testis;spleen;germinal center;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.16320 0.09095 1.798708763 96.91554612 690.84581 5.24094 ZCCHC5 7.22552233533475e-09 0.0209209967677641 0.979078996006714 zinc finger CCHC-type containing 5 . . . heart; superior cervical ganglion; 0.14231 . 0.486911049 79.46449634 110.09721 2.28029 ZCCHC6 0.999999562537735 4.37462265019108e-07 2.84452866064468e-18 zinc finger CCHC-type containing 6 FUNCTION: Uridylyltransferase that mediates the terminal uridylation of mRNAs with short (less than 25 nucleotides) poly(A) tails, hence facilitating global mRNA decay (PubMed:19703396, PubMed:25480299). Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets (PubMed:25480299). Also acts as a suppressor of miRNA biogenesis by mediating the terminal uridylation of some miRNA precursors, including that of let-7 (pre-let-7). Uridylated pre-let-7 RNA is not processed by Dicer and undergo degradation. Pre-let-7 uridylation is strongly enhanced in the presence of LIN28A (PubMed:22898984). Due to functional redundancy between ZCCHC6 and ZCCHC11, the identification of the specific role of each of these proteins is difficult. {ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:22898984, ECO:0000269|PubMed:25480299}.; . . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;frontal lobe;endometrium;thyroid;bone;testis;germinal center;spinal ganglion;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;placenta;liver;spleen;kidney;mammary gland;stomach; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;whole blood;parietal lobe; 0.18422 . -0.681547523 15.38098608 345.26264 3.94137 ZCCHC7 3.37485219287985e-09 0.513266812234492 0.486733184390656 zinc finger CCHC-type containing 7 . . . colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;cochlea;bone;thyroid;pituitary gland;testis;germinal center;brain;artery;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;lung;adrenal gland;placenta;macula lutea;liver;spleen;head and neck;cervix;mammary gland;aorta; superior cervical ganglion;ciliary ganglion;white blood cells;atrioventricular node;pons; 0.11980 0.12149 -0.378346116 28.01368247 82.06643 1.92093 ZCCHC8 0.777819067262697 0.222167717363034 1.32153742689738e-05 zinc finger CCHC-type containing 8 FUNCTION: May be involved in pre-mRNA splicing.; . . lymphoreticular;medulla oblongata;ovary;colon;skin;retina;bone marrow;uterus;whole body;cochlea;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;blood;breast;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta;cerebellum; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.34572 0.09307 . . 132.35377 2.50366 ZCCHC9 0.00747394820991637 0.924584632697475 0.0679414190926085 zinc finger CCHC-type containing 9 FUNCTION: May down-regulate transcription mediated by NF-kappa-B and the serum response element. {ECO:0000269|PubMed:18721783}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;iris;testis;germinal center;unclassifiable (Anatomical System);heart;cartilage;oral cavity;spinal cord;lens;lung;adrenal gland;placenta;macula lutea;liver;duodenum;spleen;head and neck;kidney;mammary gland;aorta;thymus; superior cervical ganglion; 0.14647 0.09575 0.483275131 79.25218212 478.30795 4.51595 ZCCHC10 0.16080191147859 0.774251508922435 0.0649465795989748 zinc finger CCHC-type containing 10 . . . unclassifiable (Anatomical System);medulla oblongata;lymph node;ovary;heart;islets of Langerhans;hypothalamus;colon;parathyroid;skin;skeletal muscle;breast;prostate;pancreas;whole body;lung;endometrium;mesenchyma;nasopharynx;placenta;visual apparatus;liver;testis;cervix;spleen;germinal center;kidney;thymus; skeletal muscle; 0.17141 0.11040 0.169169615 65.33380514 16.12197 0.57111 ZCCHC11 0.999999999122232 8.77767544483642e-10 3.77677886439194e-24 zinc finger CCHC-type containing 11 FUNCTION: Uridylyltransferase that mediates the terminal uridylation of mRNAs with short (less than 25 nucleotides) poly(A) tails, hence facilitating global mRNA decay (PubMed:25480299). Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets. Also acts as a suppressor of miRNA biogenesis by mediating the terminal uridylation of some miRNA precursors, including that of let-7 (pre-let-7), miR107, miR-143 and miR-200c. Uridylated miRNAs are not processed by Dicer and undergo degradation. Degradation of pre-let-7 contributes to the maintenance of embryonic stem (ES) cell pluripotency (By similarity). Does not bind RNA directly, but recruited to RNA targets by RNA-binding protein LIN28A. Also catalyzes the 3' uridylation of miR-26A, a miRNA that targets IL6 transcript. This abrogates the silencing of IL6 transcript, hence promoting cytokine expression (By similarity). May also suppress Toll-like receptor-induced NF-kappa-B activation via binding to T2BP. Does not play a role in replication-dependent histone mRNA degradation. Due to functional redundancy between ZCCHC6 and ZCCHC11, the identification of the specific role of each of these proteins is difficult. {ECO:0000250|UniProtKB:B2RX14, ECO:0000269|PubMed:16643855, ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:25480299}.; . . ovary;bone marrow;uterus;prostate;whole body;oesophagus;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;breast;lung;placenta;visual apparatus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.27577 0.09812 -1.589211351 3.096249115 248.29434 3.39598 ZCCHC12 0.119948128767607 0.779484011462452 0.100567859769941 zinc finger CCHC-type containing 12 FUNCTION: Transcriptional coactivator in the bone morphogenetic protein (BMP)-signaling pathway. It positively modulates BMP signaling by interacting with SMAD1 and associating with CBP in the transcription complex. It contributes to the BMP-induced enhancement of cholinergic-neuron-specific gene expression (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);whole body;frontal lobe;endometrium;hypothalamus;thyroid;hippocampus;pituitary gland;brain;skeletal muscle; amygdala;subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;hypothalamus;globus pallidus;ciliary ganglion;atrioventricular node;pons;cingulate cortex;cerebellum; 0.10517 0.09803 -0.293801652 32.93819297 29.34234 0.93906 ZCCHC13 0.000210272056556787 0.294467680103008 0.705322047840435 zinc finger CCHC-type containing 13 . . . testis; testis - interstitial;testis;skeletal muscle; 0.21080 . 0.769889969 86.95447039 168.3234 2.83193 ZCCHC14 0.94883572655475 0.0511629004553382 1.37298991211503e-06 zinc finger CCHC-type containing 14 . . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;bone;thyroid;testis;amniotic fluid;brain;pineal gland;unclassifiable (Anatomical System);amygdala;cartilage;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;adrenal gland;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;stomach;aorta;peripheral nerve; superior cervical ganglion;testis - interstitial;occipital lobe;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe;cingulate cortex; 0.52771 0.10974 -1.278681 5.172210427 5229.76084 14.89921 ZCCHC16 0.000561724706329207 0.467897658602384 0.531540616691286 zinc finger CCHC-type containing 16 . . . . . 0.11079 0.08043 0.084621747 60.31493277 66.42822 1.67865 ZCCHC17 0.215147590312843 0.776149121459489 0.00870328822766754 zinc finger CCHC-type containing 17 . . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;pharynx;blood;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; subthalamic nucleus;testis - interstitial;globus pallidus;testis;parietal lobe;cingulate cortex; 0.21385 0.10909 0.058937498 58.26256192 13.78036 0.50077 ZCCHC18 0.259266478025309 0.639332415734199 0.101401106240492 zinc finger CCHC-type containing 18 . . . . . . . . . 265.90589 3.49763 ZCCHC23 . . . zinc finger CCHC-type containing 23 . . . . . . . . . . . ZCCHC24 0.473546851353267 0.502683275637604 0.0237698730091295 zinc finger CCHC-type containing 24 . . . . . 0.34722 0.11611 . . 130.72235 2.49025 ZCRB1 0.000953935727738575 0.808507290096261 0.190538774176 zinc finger CCHC-type and RNA binding motif containing 1 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;breast;bile duct;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;aorta;stomach; subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;pons;parietal lobe;cingulate cortex; 0.20152 0.09895 0.03689118 56.64071715 18.00567 0.62898 ZCWPW1 1.15224577774625e-12 0.279308170295982 0.720691829702866 zinc finger CW-type and PWWP domain containing 1 . . . unclassifiable (Anatomical System);lymphoreticular;colon;blood;bone marrow;prostate;lung;whole body;endometrium;bone;testis;head and neck;kidney;germinal center;brain; testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion; 0.04874 . 0.688969636 85.20877565 398.23636 4.19226 ZCWPW2 6.76412703598574e-05 0.728997484655519 0.270934874074121 zinc finger CW-type and PWWP domain containing 2 . . . . . 0.13693 . 0.373041938 75.29488087 705.77698 5.27822 ZDBF2 1.3787431893894e-07 0.997584790250834 0.00241507187484671 zinc finger DBF-type containing 2 . . . . . 0.09488 0.08021 1.802396639 96.93323897 524.58811 4.67459 ZDHHC1 5.10929019814853e-06 0.653331896630744 0.346662994079058 zinc finger DHHC-type containing 1 . . TISSUE SPECIFICITY: Expressed at high levels in fetal lung, kidney and heart. Expressed at lower levels in adult pancreas and lung. {ECO:0000269|PubMed:10395086}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;lens;skeletal muscle;prostate;optic nerve;lung;endometrium;placenta;bone;visual apparatus;testis;kidney; superior cervical ganglion;thyroid;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.08306 . -0.424258538 25.56027365 119.88473 2.38515 ZDHHC2 0.00703300683867723 0.975857393095415 0.0171096000659083 zinc finger DHHC-type containing 2 FUNCTION: Palmitoyltransferase specific for GAP43 and DLG4/PSD95. {ECO:0000250}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Reduced expression in colorectal cancers with liver metastasis. {ECO:0000269|PubMed:10918388}.; ovary;foreskin;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cerebellum cortex;nervous;islets of Langerhans;hypothalamus;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach;aorta;cerebellum;thymus; . 0.13373 0.08861 -0.049474214 50.01179523 36.6632 1.10024 ZDHHC3 0.144015391144747 0.852051099545421 0.00393350930983197 zinc finger DHHC-type containing 3 FUNCTION: Palmitoyltransferase with broad specificity. Palmitoylates GABA receptors on their gamma subunit (GABRG1, GABRG2 and GABRG3), which regulates synaptic clustering and/or cell surface stability. Palmitoylates glutamate receptors GRIA1 and GRIA2, which leads to their retention in Golgi. May also palmitoylate DLG4, DNAJC5 and SNAP25. {ECO:0000250|UniProtKB:Q8R173, ECO:0000269|PubMed:23034182}.; . . medulla oblongata;smooth muscle;ovary;developmental;colon;parathyroid;choroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;muscle;adrenal cortex;blood;lens;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hippocampus;duodenum;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin;parietal lobe; 0.28038 0.11814 0.082802743 60.09082331 12.91581 0.47097 ZDHHC4 5.32054090170074e-10 0.0320160817902909 0.967983917677655 zinc finger DHHC-type containing 4 . . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;oesophagus;endometrium;larynx;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;pineal body;muscle;adrenal cortex;blood;lens;lung;placenta;macula lutea;visual apparatus;alveolus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis;ciliary ganglion;atrioventricular node; 0.02518 0.07165 0.775339069 87.13729653 321.55724 3.80807 ZDHHC4P1 . . . zinc finger DHHC-type containing 4 pseudogene 1 . . . . . . . . . . . ZDHHC5 0.999924209308766 7.57906715143431e-05 1.97198803287468e-11 zinc finger DHHC-type containing 5 FUNCTION: Palmitoyl acyltransferase for the G-protein coupled receptor SSTR5. Also palmitoylates FLOT2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:21820437}.; . . myocardium;ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;lacrimal gland;tongue;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;visual apparatus;hypopharynx;head and neck;cervix;kidney;mammary gland;stomach;thymus; testis;trigeminal ganglion; 0.54498 . -0.26629572 34.81953291 108.65634 2.26230 ZDHHC6 0.000675860139797096 0.978934972691693 0.0203891671685095 zinc finger DHHC-type containing 6 FUNCTION: Palmitoylates calnexin (CALX), which is required for its association with the ribosome-translocon complex and efficient folding of glycosylated proteins. {ECO:0000269|PubMed:22314232}.; . . . . 0.37662 0.10596 0.082802743 60.09082331 127.40449 2.46119 ZDHHC7 0.00507412524920815 0.968110722245421 0.0268151525053712 zinc finger DHHC-type containing 7 FUNCTION: Palmitoyltransferase with broad specificity. Palmitoylates SNAP25 and DLG4/PSD95 (By similarity). Palmitoylates sex steroid hormone receptors, including ESR1, PGR and AR, thereby regulating their targeting to the plasma membrane and their function in rapid intracellular signaling upon binding of sex hormones (PubMed:22031296). May play a role in follicle stimulation hormone (FSH) activation of testicular Sertoli cells (By similarity). {ECO:0000250|UniProtKB:Q91WU6, ECO:0000250|UniProtKB:Q923G5, ECO:0000269|PubMed:22031296}.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cerebral cortex;endometrium;larynx;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);trophoblast;cartilage;heart;islets of Langerhans;pharynx;blood;skeletal muscle;bile duct;pancreas;lung;cornea;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.09026 0.09447 -0.314027422 31.9297004 211.71505 3.13784 ZDHHC8 0.988991095834612 0.0110087526339903 1.51531397993717e-07 zinc finger DHHC-type containing 8 FUNCTION: Palmitoyltransferase involved in glutamatergic transmission. Mediates palmitoylation of ABCA1. {ECO:0000269|PubMed:19556522}.; . . ovary;salivary gland;sympathetic chain;intestine;colon;parathyroid;skin;bone marrow;retina;uterus;prostate;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;lens;pancreas;lung;cornea;placenta;visual apparatus;liver;kidney;mammary gland;stomach; dorsal root ganglion;atrioventricular node; 0.15989 . -1.168429872 6.062750649 606.91004 4.98443 ZDHHC8P1 . . . zinc finger DHHC-type containing 8 pseudogene 1 . . . unclassifiable (Anatomical System);uterus;prostate;endometrium;islets of Langerhans;placenta;testis;colon;kidney;brain; . . . . . . . ZDHHC9 0.88543756379133 0.114300054403561 0.000262381805108916 zinc finger DHHC-type containing 9 FUNCTION: The ZDHHC9-GOLGA7 complex is a palmitoyltransferase specific for HRAS and NRAS. {ECO:0000269|PubMed:16000296}.; DISEASE: Mental retardation, X-linked, syndromic, ZDHHC9-related (MRXSZ) [MIM:300799]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Some MRXSZ patients have marfanoid habitus as an additional feature. {ECO:0000269|PubMed:17436253, ECO:0000269|PubMed:19377476}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highly expressed in kidney, skeletal muscle, brain, lung and liver. Absent in thymus, spleen and leukocytes. {ECO:0000269|PubMed:16000296}.; ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;iris;testis;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;pineal body;muscle;blood;lens;breast;bile duct;pancreas;lung;mesenchyma;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; globus pallidus; 0.61011 0.09584 -0.119252484 44.53880632 3.13114 0.11224 ZDHHC11 5.59638555559534e-11 0.0315273463868453 0.968472653557191 zinc finger DHHC-type containing 11 . . . unclassifiable (Anatomical System);uterus;lung;heart;cerebellum cortex;islets of Langerhans;liver;spleen;germinal center;brain;skin;skeletal muscle; . 0.07275 . 0.979225112 90.42816702 206.54905 3.10549 ZDHHC11B 0.0432283730925046 0.92941045755069 0.0273611693568052 zinc finger DHHC-type containing 11B . . . . . . . . . 1086.92828 6.31503 ZDHHC12 0.0117662276069055 0.846906149668528 0.141327622724566 zinc finger DHHC-type containing 12 . . . . . 0.07335 . 0.685332364 85.09672092 613.0689 5.00617 ZDHHC13 2.55026685458048e-14 0.0174156067839434 0.982584393216031 zinc finger DHHC-type containing 13 FUNCTION: Palmitoyltransferase for HD and GAD2. May play a role in Mg(2+) transport. {ECO:0000250|UniProtKB:Q9CWU2}.; . . . . 0.13124 0.07399 0.663285274 84.55414013 209.52636 3.12505 ZDHHC14 0.98236655846095 0.0176310601659934 2.38137305711371e-06 zinc finger DHHC-type containing 14 . . . ovary;colon;parathyroid;fovea centralis;choroid;retina;uterus;prostate;optic nerve;larynx;synovium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;blood;lens;pancreas;lung;nasopharynx;placenta;macula lutea;head and neck;kidney; uterus corpus; . 0.10652 0.350995466 74.37485256 67.03988 1.69272 ZDHHC15 0.896641058029422 0.103158219973409 0.000200721997168811 zinc finger DHHC-type containing 15 FUNCTION: Palmitoyltransferase specific for GAP43 and DLG4/PSD95. {ECO:0000250}.; DISEASE: Mental retardation, X-linked 91 (MRX91) [MIM:300577]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non- syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. {ECO:0000269|PubMed:15915161}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in placenta, liver, lung, kidney, heart and brain. {ECO:0000269|PubMed:15915161}.; . . 0.23833 0.09315 -0.05129383 49.75819769 24.63449 0.80899 ZDHHC16 0.0180658269032166 0.981029191859042 0.000904981237741704 zinc finger DHHC-type containing 16 FUNCTION: May be involved in apoptosis regulation. {ECO:0000250}.; . . lymphoreticular;ovary;skin;retina;prostate;optic nerve;frontal lobe;endometrium;germinal center;brain;heart;cartilage;tongue;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;synovium;bone;testis;unclassifiable (Anatomical System);hypothalamus;muscle;bile duct;pancreas;lung;cornea;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; . 0.16411 0.11090 -0.912929826 9.902099552 19.82623 0.67621 ZDHHC17 0.998394623926362 0.00160536928535551 6.7882822775063e-09 zinc finger DHHC-type containing 17 FUNCTION: Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HD (PubMed:15603740, PubMed:15489887, PubMed:19139280). Palmitoylates MPP1 in erythrocytes (PubMed:22496366). May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane (PubMed:12393793). May play a role in Mg(2+) transport (PubMed:18794299). {ECO:0000269|PubMed:12393793, ECO:0000269|PubMed:15489887, ECO:0000269|PubMed:15603740, ECO:0000269|PubMed:18794299, ECO:0000269|PubMed:19139280, ECO:0000269|PubMed:22496366}.; . TISSUE SPECIFICITY: Expressed in all brain regions. Expression is highest in the cortex, cerebellum, occipital lobe and caudate and lowest in the spinal cord. Expression is also seen in testis, pancreas, heart and kidney. ZDHHC17 is the only palmitoyltransferase in erythrocytes. {ECO:0000269|PubMed:12393793, ECO:0000269|PubMed:22496366}.; ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;cochlea;larynx;synovium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);amygdala;heart;tongue;islets of Langerhans;spinal cord;blood;lens;skeletal muscle;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach;aorta; dorsal root ganglion;amygdala;medulla oblongata;superior cervical ganglion;occipital lobe;hypothalamus;pons;atrioventricular node;skeletal muscle;skin;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;cingulate cortex;parietal lobe; 0.57991 0.20330 -0.159704656 41.90846898 464.21173 4.46413 ZDHHC18 0.00119784993745536 0.956889606577517 0.0419125434850277 zinc finger DHHC-type containing 18 FUNCTION: Has palmitoyltransferase activity towards HRAS and LCK. {ECO:0000250}.; . . . . 0.13292 . -0.315847836 31.68789809 110.88897 2.29533 ZDHHC19 0.0524274267287205 0.926964411156183 0.0206081621150969 zinc finger DHHC-type containing 19 . . . unclassifiable (Anatomical System);optic nerve;lung;testis; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;trigeminal ganglion; 0.06503 0.08776 1.0178651 90.91766926 410.35851 4.24506 ZDHHC20 0.00233007066872882 0.924417226415343 0.0732527029159279 zinc finger DHHC-type containing 20 . . . unclassifiable (Anatomical System);breast;uterus;lung;heart;liver;testis;colon;spleen;kidney;skin;skeletal muscle; . 0.18204 . 0.747842143 86.47676339 125.12739 2.43466 ZDHHC20-IT1 . . . ZDHHC20 intronic transcript 1 . . . . . . . . . . . ZDHHC20P1 . . . zinc finger DHHC-type containing 20 pseudogene 1 . . . . . . . . . . . ZDHHC20P2 . . . zinc finger DHHC-type containing 20 pseudogene 2 . . . . . . . . . . . ZDHHC20P3 . . . zinc finger DHHC-type containing 20 pseudogene 3 . . . . . . . . . . . ZDHHC20P4 . . . zinc finger DHHC-type containing 20 pseudogene 4 . . . . . . . . . . . ZDHHC21 0.0512303788505532 0.927439930526653 0.0213296906227935 zinc finger DHHC-type containing 21 FUNCTION: Palmitoylates sex steroid hormone receptors, including ESR1, PGR and AR, thereby regulating their targeting to the plasma membrane. This affects rapid intracellular signaling by sex hormones via ERK and AKT kinases and the generation of cAMP, but does not affect that mediated by their nuclear receptor (By similarity). {ECO:0000250, ECO:0000269|PubMed:22031296}.; . . . . 0.13681 0.11273 -0.227663163 37.11370606 28.59147 0.91597 ZDHHC22 0.318481044811824 0.613313742864902 0.0682052123232747 zinc finger DHHC-type containing 22 FUNCTION: Palmitoyltransferase that mediates palmitoylation of KCNMA1, regulating localization of KCNMA1 to the plasma membrane. {ECO:0000269|PubMed:22399288}.; . . lung;testis;brain; . . . -0.229483771 36.86010852 11.3551 0.40880 ZDHHC23 3.89032529135583e-06 0.593776849605572 0.406219260069136 zinc finger DHHC-type containing 23 FUNCTION: Palmitoyltransferase that mediates palmitoylation of KCNMA1, regulating localization of KCNMA1 to the plasma membrane. May be involved in NOS1 regulation and targeting to the synaptic membrane. {ECO:0000269|PubMed:22399288}.; . . unclassifiable (Anatomical System);lymph node;ovary;tongue;islets of Langerhans;colon;parathyroid;skin;retina;breast;pancreas;lung;bone;thyroid;placenta;hippocampus;liver;testis;head and neck;spleen;germinal center;kidney;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.47166 0.13548 -0.358119787 29.16371786 88.31913 2.01419 ZDHHC24 0.00614030824043694 0.737309852039576 0.256549839719987 zinc finger DHHC-type containing 24 . . . unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;muscle;colon;blood;skin;retina;uterus;pancreas;prostate;optic nerve;lung;cerebral cortex;bone;placenta;hippocampus;duodenum;liver;testis;kidney;brain;stomach;peripheral nerve; superior cervical ganglion;skeletal muscle; 0.13104 . . . 2231.75399 8.70544 ZEB1 0.983612745475666 0.0163871730871857 8.14371480781639e-08 zinc finger E-box binding homeobox 1 FUNCTION: Acts as a transcriptional repressor. Inhibits interleukin-2 (IL-2) gene expression. Enhances or represses the promoter activity of the ATP1A1 gene depending on the quantity of cDNA and on the cell type. Represses E-cadherin promoter and induces an epithelial-mesenchymal transition (EMT) by recruiting SMARCA4/BRG1. Represses BCL6 transcription in the presence of the corepressor CTBP1. Positively regulates neuronal differentiation. Represses RCOR1 transcription activation during neurogenesis. Represses transcription by binding to the E box (5'-CANNTG-3'). Promotes tumorigenicity by repressing stemness-inhibiting microRNAs. {ECO:0000269|PubMed:19935649, ECO:0000269|PubMed:20175752, ECO:0000269|PubMed:20418909}.; DISEASE: Corneal dystrophy, Fuchs endothelial, 6 (FECD6) [MIM:613270]: A corneal disease caused by loss of endothelium of the central cornea. It is characterized by focal wart-like guttata that arise from Descemet membrane and develop in the central cornea, epithelial blisters, reduced vision and pain. Descemet membrane is thickened by abnormal collagenous deposition. {ECO:0000269|PubMed:20036349, ECO:0000269|PubMed:23599324}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Colocalizes with SMARCA4/BRG1 in E-cadherin- negative cells from established lines, and stroma of normal colon as well as in de-differentiated epithelial cells at the invasion front of colorectal carcinomas (at protein level). Expressed in heart and skeletal muscle, but not in liver, spleen, or pancreas. {ECO:0000269|PubMed:20418909}.; lymphoreticular;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;artery;bladder;unclassifiable (Anatomical System);cartilage;heart;tongue;islets of Langerhans;hypothalamus;spinal cord;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;spleen;head and neck;kidney;aorta;stomach; uterus;superior cervical ganglion;occipital lobe;adipose tissue;spinal cord;atrioventricular node; 0.48165 0.34670 0.558509856 81.67020524 375.53636 4.08459 ZEB1-AS1 . . . ZEB1 antisense RNA 1 . . . . . . . . . . . ZEB2 0.999833866722983 0.000166133250021911 2.69949052407023e-11 zinc finger E-box binding homeobox 2 FUNCTION: Transcriptional inhibitor that binds to DNA sequence 5'- CACCT-3' in different promoters. Represses transcription of E- cadherin. {ECO:0000269|PubMed:16061479}.; DISEASE: Mowat-Wilson syndrome (MOWS) [MIM:235730]: A complex developmental disorder characterized by mental retardation, delayed motor development, epilepsy, microcephaly and a wide spectrum of clinically heterogeneous features suggestive of neurocristopathies at the cephalic, cardiac, and vagal levels. Affected patients show an easily recognizable facial appearance with deep set eyes and hypertelorism, medially divergent, broad eyebrows, prominent columella, pointed chin and uplifted, notched ear lobes. Some patients manifest Hirschsprung disease. {ECO:0000269|PubMed:11448942, ECO:0000269|PubMed:12451214, ECO:0000269|PubMed:15384097, ECO:0000269|PubMed:16688751}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;heart;cartilage;blood;skeletal muscle;lung;adrenal gland;placenta;visual apparatus;hippocampus;liver;spleen;kidney;stomach;aorta;peripheral nerve; amygdala;dorsal root ganglion;superior cervical ganglion;fetal brain;globus pallidus;trigeminal ganglion; 0.89357 0.22348 -0.909290275 10.03184713 133.4414 2.50999 ZEB2-AS1 . . . ZEB2 antisense RNA 1 . . . . . . . . . . . ZEB2P1 . . . zinc finger E-box binding homeobox 2 pseudogene 1 . . . . . . . . . . . ZER1 0.998769062850375 0.00123093359677597 3.55284924157855e-09 zyg-11 related, cell cycle regulator FUNCTION: Probably acts as target recruitment subunit in the E3 ubiquitin ligase complex ZER1-CUL2-Elongin BC. {ECO:0000269|PubMed:17304241}.; . TISSUE SPECIFICITY: Expressed in testis, spermatocytes and spermatids (at protein level). Expressed in spermatocytes, spermatids, prostate, skeletal muscle, ovary, small intestine, heart, brain and pancreas. {ECO:0000269|PubMed:11719588}.; lymphoreticular;ovary;sympathetic chain;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;synovium;larynx;bone;thyroid;iris;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;blood;lens;breast;pancreas;lung;placenta;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; amygdala;whole brain;superior cervical ganglion;occipital lobe;prostate;thyroid;prefrontal cortex;testis;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.56242 0.11185 -0.979072682 8.752064166 36.51994 1.09452 ZFAND1 0.000588040962386689 0.899325652025552 0.100086307012061 zinc finger AN1-type containing 1 . . . sympathetic chain;developmental;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cerebral cortex;bone;thyroid;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;islets of Langerhans;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; thyroid;tumor; 0.12023 0.09008 -0.339715008 30.06605331 29.32078 0.93796 ZFAND2A 0.000389857167343114 0.397169374218051 0.602440768614605 zinc finger AN1-type containing 2A . . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pharynx;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;alveolus;liver;head and neck;kidney;mammary gland;stomach;thymus; . 0.09341 0.08641 -0.007201372 53.19061099 18.35464 0.63643 ZFAND2B 0.00495151493335169 0.967329387251208 0.0277190978154403 zinc finger AN1-type containing 2B . . . ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;bile duct;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; . 0.13505 0.08467 0.283038099 71.26680821 144.91124 2.62225 ZFAND3 0.961977905050761 0.037943642631578 7.84523176606702e-05 zinc finger AN1-type containing 3 . . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;thyroid;iris;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;nervous;islets of Langerhans;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;alveolus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.23727 0.10551 0.03689118 56.64071715 16.35523 0.57998 ZFAND4 0.00925156548332018 0.988339603123887 0.00240883139279297 zinc finger AN1-type containing 4 . . . unclassifiable (Anatomical System);medulla oblongata;urinary;skeletal muscle;skin;uterus;atrium;lung;bone;liver;testis;spleen;germinal center;brain; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node; 0.11957 0.08975 0.870809653 88.86529842 1663.09591 7.52876 ZFAND5 0.91258506652532 0.0867801546886168 0.000634778786062927 zinc finger AN1-type containing 5 FUNCTION: Involved in protein degradation via the ubiquitin- proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor (TNF), IL-1 and TLR4- induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation. {ECO:0000269|PubMed:14754897}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Expressed in fetal cochlea. Also expressed in infant brain, fetal heart, pancreatic islet, melanocyte, pineal gland, placenta, corneal stroma, and parathyroid tumor. Weakly expressed or undetectable in adult brain, heart, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocytes. Expressed in rhabdomyosarcoma RD cells (at protein level). {ECO:0000269|PubMed:14754897, ECO:0000269|PubMed:9758550}.; myocardium;ovary;substantia nigra;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;urinary;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;trabecular meshwork;macula lutea;visual apparatus;liver;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;spinal ganglion;artery;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta; dorsal root ganglion;occipital lobe;adrenal cortex;testis;ciliary ganglion;skeletal muscle; 0.14821 0.11262 -0.119252484 44.53880632 0.87804 0.01780 ZFAND6 0.218468572768346 0.743621706495486 0.0379097207361678 zinc finger AN1-type containing 6 FUNCTION: Involved in regulation of TNF-alpha induced NF-kappa-B activation and apoptosis. Involved in modulation of 'Lys-48'- linked polyubiquitination status of TRAF2 and decreases association of TRAF2 with RIPK1. Required for PTS1 target sequence-dependent protein import into peroxisomes and PEX5 stability; may cooperate with PEX6. In vitro involved in PEX5 export from the cytosol to peroxisomes (By similarity). {ECO:0000250, ECO:0000269|PubMed:19285159, ECO:0000269|PubMed:21810480}.; . TISSUE SPECIFICITY: Widely expressed with high level in heart, skeletal muscle, liver, kidney and placenta. {ECO:0000269|PubMed:11054541}.; medulla oblongata;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;atrium;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;testis;dura mater;germinal center;brain;pineal gland;bladder;unclassifiable (Anatomical System);meninges;lymph node;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;bile duct;breast;pia mater;lung;adrenal gland;placenta;macula lutea;hippocampus;liver;cervix;kidney;mammary gland;stomach;aorta;peripheral nerve; . 0.59679 0.11302 0.058937498 58.26256192 29.26317 0.93658 ZFAND6P1 . . . zinc finger AN1-type containing 6 pseudogene 1 . . . . . . . . . . . ZFAS1 . . . ZNFX1 antisense RNA 1 . . . . . 0.11183 . . . . . ZFAT 0.00292867269376687 0.996965027432471 0.000106299873762278 zinc finger and AT-hook domain containing FUNCTION: May be involved in transcriptional regulation. Overexpression causes down-regulation of a number of genes involved in the immune response. Some genes are also up-regulated (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Isoform 1 is strongly expressed in placenta, spleen, kidney, testis and peripheral blood leukocytes. Expressed in CD4+ and CD8+ T-cells, CD19+ B-cells and CB14+ monocytes. Isoform 3 is strongly expressed in placenta, ovary, tonsil, CD19+ B-cells and CD14+ monocytes. {ECO:0000269|PubMed:15294872}.; ovary;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;pineal body;lens;skeletal muscle;breast;lung;epididymis;placenta;macula lutea;liver;spleen;mammary gland;stomach; superior cervical ganglion;placenta; 0.06704 0.10680 -0.385854854 27.08185893 876.35347 5.76073 ZFAT-AS1 . . . ZFAT antisense RNA 1 . . . . . . . . . . . ZFC3H1 0.999999999616417 3.83583439942727e-10 4.16549963902762e-27 zinc finger C3H1-type containing . . . . . 0.54509 0.10606 -1.830003058 2.117244633 335.40622 3.89104 ZFHX2 . . . zinc finger homeobox 2 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.26622 0.09686 . . 5201.88956 14.85824 ZFHX3 0.999999999859262 1.40738112451388e-10 8.84723072571831e-27 zinc finger homeobox 3 FUNCTION: Transcriptional regulator which can act as an activator or a repressor. Inhibits the enhancer element of the AFP gene by binding to its AT-rich core sequence. In concert with SMAD- dependent TGF-beta signaling can repress the transcription of AFP via its interaction with SMAD2/3 (PubMed:25105025). Regulates the circadian locomotor rhythms via transcriptional activation of neuropeptidergic genes which are essential for intercellular synchrony and rhythm amplitude in the suprachiasmatic nucleus (SCN) of the brain (By similarity). Regulator of myoblasts differentiation through the binding to the AT-rich sequence of MYF6 promoter and promoter repression (PubMed:11312261). Down- regulates the MUC5AC promoter in gastric cancer (PubMed:17330845). In association with RUNX3, upregulates CDKN1A promoter activity following TGF-beta stimulation (PubMed:20599712). Inhibits estrogen receptor (ESR1) function by selectively competing with coactivator NCOA3 for binding to ESR1 in ESR1-positive breast cancer cells (PubMed:20720010). {ECO:0000250|UniProtKB:Q61329, ECO:0000269|PubMed:11312261, ECO:0000269|PubMed:17330845, ECO:0000269|PubMed:20599712, ECO:0000269|PubMed:20720010, ECO:0000269|PubMed:25105025}.; . TISSUE SPECIFICITY: Not found in normal gastric mucosa but found in gastric carcinoma cells (at protein level). Expression is higher in ER-positive breast tumors than ER-negative breast tumors (at protein level). {ECO:0000269|PubMed:17330845, ECO:0000269|PubMed:20599712, ECO:0000269|PubMed:20720010, ECO:0000269|PubMed:22452784}.; ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;bone;iris;testis;germinal center;pineal gland;brain;tonsil;unclassifiable (Anatomical System);heart;lens;breast;lung;placenta;macula lutea;visual apparatus;spleen;head and neck;cervix;kidney;mammary gland; prostate;superior cervical ganglion;fetal thyroid; 0.74579 0.15507 -4.263203714 0.117952347 6032.74571 16.21079 ZFHX4 0.999999642290115 3.57709884835703e-07 1.44334195895989e-20 zinc finger homeobox 4 FUNCTION: May play a role in neural and muscle differentiation (By similarity). May be involved in transcriptional regulation. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in brain, skeletal muscle and liver. Very low expression in stomach.; colon;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;lens;lung;placenta;macula lutea;liver;duodenum;spleen;head and neck; dorsal root ganglion;superior cervical ganglion;appendix;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; 0.92237 0.08897 -1.737130259 2.435715971 2869.66786 10.14403 ZFHX4-AS1 . . . ZFHX4 antisense RNA 1 . . . . . . . . . . . ZFP1 0.00925162312350236 0.938837064762871 0.0519113121136269 ZFP1 zinc finger protein FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;parathyroid;retina;uterus;prostate;lung;frontal lobe;larynx;bone;placenta;liver;testis;head and neck;kidney;brain;stomach; amygdala;subthalamic nucleus;occipital lobe;medulla oblongata;temporal lobe;globus pallidus;parietal lobe;cingulate cortex; 0.30992 0.10507 -0.314027422 31.9297004 42.83799 1.24037 ZFP2 5.6203288384679e-12 0.0157786554975017 0.984221344496878 ZFP2 zinc finger protein FUNCTION: Probable transcription factor involved in neuronal differentiation and/or phenotypic maintenance. {ECO:0000250}.; . . liver;spleen;mammary gland; superior cervical ganglion;temporal lobe;skeletal muscle;parietal lobe; 0.20364 0.10329 0.176444282 66.07100731 299.35312 3.68962 ZFP3 0.000584029588192101 0.714347014433168 0.28506895597864 ZFP3 zinc finger protein FUNCTION: May be involved in transcriptional regulation.; . . uterus;cartilage;ovary;heart;placenta;parathyroid;kidney;germinal center;brain;skin;peripheral nerve;retina; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;cingulate cortex; 0.26040 0.10409 -0.359940251 28.93371078 44.60145 1.28014 ZFP14 0.000162247685567042 0.878365692038282 0.121472060276151 ZFP14 zinc finger protein FUNCTION: May be involved in transcriptional regulation.; . . myocardium;skeletal muscle;breast;endometrium;nasopharynx;visual apparatus;hippocampus;liver;testis;spleen;kidney;pineal gland;brain; ciliary ganglion; 0.26778 . 0.305084559 72.22811984 292.96041 3.65961 ZFP28 2.48872617846742e-06 0.978423166665134 0.0215743446086874 ZFP28 zinc finger protein FUNCTION: May be involved in transcriptional regulation. May have a role in embryonic development.; . . unclassifiable (Anatomical System);cartilage;muscle;skeletal muscle;lung;placenta;thyroid;bone;visual apparatus;liver;testis;spleen;germinal center;kidney;brain;stomach; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.18911 0.08844 0.047806932 57.51946214 5838.51751 15.82904 ZFP30 9.06361318152477e-08 0.50319503218896 0.496804877174908 ZFP30 zinc finger protein FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);uterus;lymph node;islets of Langerhans;placenta;visual apparatus;developmental;kidney;skeletal muscle;gall bladder; . 0.19852 . 0.132352165 63.48785091 97.12556 2.13049 ZFP36 0.64593418279633 0.347857572086627 0.00620824511704297 ZFP36 ring finger protein FUNCTION: mRNA-binding protein involved in post-transcriptional regulation of AU-rich element (ARE)-containing mRNAs. Acts by specifically binding ARE-containing mRNAs and promoting their degradation. Recruits deadenylase CNOT7 (and probably the CCR4-NOT complex) via association with CNOT1. Plays a key role in the post- transcriptional regulation of tumor necrosis factor (TNF). Plays a key role in the post-transcriptional regulation of tumor necrosis factor (TNF). {ECO:0000269|PubMed:15014438, ECO:0000269|PubMed:23644599}.; . . smooth muscle;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;thyroid;iris;testis;germinal center;spinal ganglion;brain;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;aorta;thymus; dorsal root ganglion;superior cervical ganglion;olfactory bulb;trachea;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14956 . -0.249709319 35.74545883 . . ZFP36L1 0.506697565301335 0.474555905034646 0.0187465296640186 ZFP36 ring finger protein-like 1 FUNCTION: Probable regulatory protein involved in regulating the response to growth factors.; . . medulla oblongata;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;tonsil;amygdala;heart;cartilage;urinary;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;cervix;mammary gland;peripheral nerve;colon;choroid;fovea centralis;uterus;oesophagus;larynx;bone;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;pancreas;lung;mesenchyma;placenta;hippocampus;duodenum;hypopharynx;head and neck;kidney;stomach;aorta;thymus; uterus;superior cervical ganglion;placenta;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.93468 . -0.053113545 49.38664779 17.82662 0.62283 ZFP36L2 0.456433762263267 0.516762223030219 0.0268040147065139 ZFP36 ring finger protein-like 2 FUNCTION: mRNA-binding protein that plays a key role in self- renewal of erythroid cells in response to glucocorticoids. Specifically binds to the AU-rich element (ARE) in the 3'-UTR of target mRNAs, promoting their deadenylation and degradation (PubMed:14981510). Specifically expressed in burst-forming unit- erythroid (BFU-E) progenitors in response to glucocorticoids and acts as a negative regulator of erythroid cell differentiation: promotes self-renewal of erythroid cells by binding mRNAs that are induced or highly expressed during terminal erythroid differentiation and promotes their degradation, preventing erythroid cell differentiation. Down-regulated during erythroid differentiation from the BFU-E stage, stabilizing mRNAs required for terminal differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:14981510}.; DISEASE: Note=Defects in ZFP36L2 may be a cause of leukemias. Frameshfits mutations disrupting ZFP36L2 have been found in a patient with acute myeloid leukemia (PubMed:21109922). {ECO:0000269|PubMed:21109922}.; . smooth muscle;umbilical cord;ovary;developmental;colon;parathyroid;vein;skin;bone marrow;uterus;prostate;optic nerve;cerebral cortex;bone;thyroid;testis;dura mater;germinal center;spinal ganglion;brain;tonsil;gall bladder;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;adrenal cortex;blood;pancreas;pia mater;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus; thyroid;white blood cells;ciliary ganglion;atrioventricular node;trigeminal ganglion;fetal thyroid;whole blood;skin; 0.62864 0.11103 -0.488577883 22.64685067 725.58828 5.34840 ZFP37 4.10777184988061e-09 0.103496806033473 0.896503189858755 ZFP37 zinc finger protein FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Expressed at low level in several tissues including fetal cartilage.; . . 0.07258 0.06248 0.264628794 70.5178108 1185.08476 6.53135 ZFP41 0.000671957504039482 0.301729544091952 0.697598498404009 ZFP41 zinc finger protein FUNCTION: A putative DNA-binding regulatory protein associated with meiosis in spermatogenesis. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;hypothalamus;blood;lens;pancreas;lung;placenta;macula lutea;kidney;thymus; amygdala;superior cervical ganglion;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe; . . 0.106667882 61.73036093 36.28588 1.08682 ZFP42 0.0047532978087036 0.685246569540254 0.310000132651043 ZFP42 zinc finger protein FUNCTION: Involved in the reprogramming of X-chromosome inactivation during the acquisition of pluripotency. Required for efficient elongation of TSIX, a non-coding RNA antisense to XIST. Binds DXPas34 enhancer within the TSIX promoter. Involved in ES cell self-renewal (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in kidney, epidermal keratinocytes, prostate epithelial cells, bronchial and small airway lung epithelial cells (at protein level). Expressed in malignant kidney and several carcinoma cell lines (at protein level). Expressed in embryonic stem cells, kidney, epidermal keratinocytes, prostate epithelial cells, bronchial and small airway lung epithelial cells. Expressed in embryonal carcinomas, seminomas, malignant kidney and several carcinoma cell lines. {ECO:0000269|PubMed:12110702, ECO:0000269|PubMed:16344273, ECO:0000269|PubMed:16424014, ECO:0000269|PubMed:16865673}.; unclassifiable (Anatomical System);lung;epididymis;placenta;testis; superior cervical ganglion;globus pallidus;trigeminal ganglion; 0.25169 0.10564 0.17280645 65.75843359 35.38317 1.06860 ZFP57 0.00181593681997415 0.900014339990894 0.0981697231891322 ZFP57 zinc finger protein FUNCTION: Binds to a 5'-TGCCGC-3' consensus sequence and recognizes the methylated CpG within this element (By similarity). Transcription regulator required to maintain maternal and paternal gene imprinting, a process by which gene expression is restricted in a parent of origin-specific manner by epigenetic modification of genomic DNA and chromatin, including DNA methylation. Acts by controlling DNA methylation during the earliest multicellular stages of development at multiple imprinting control regions. Required for the establishment of maternal methylation imprints at SNRPN locus. Acts as a transcriptional repressor in Schwann cells. {ECO:0000250, ECO:0000269|PubMed:18622393}.; DISEASE: Transient neonatal diabetes mellitus 1 (TNDM1) [MIM:601410]: Neonatal diabetes is a form of diabetes mellitus defined by the onset of mild-to-severe hyperglycemia within the first months of life. In about half of the neonates, diabetes is transient and resolves at a median age of 3 months, whereas the rest have a permanent form of diabetes. {ECO:0000269|PubMed:18622393}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . . . 1.973318412 97.57607926 182.38697 2.93370 ZFP62 0.115212077093719 0.77854416205872 0.106243760847562 ZFP62 zinc finger protein FUNCTION: May play a role in differentiating skeletal muscle. {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;lung;frontal lobe;islets of Langerhans;placenta;developmental;pituitary gland;skin;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; . . 0.461228372 78.46190139 183.34102 2.93807 ZFP64 0.00518985254415644 0.96880404153607 0.0260061059197734 ZFP64 zinc finger protein FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;skin;uterus;prostate;whole body;thyroid;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;hypothalamus;muscle;blood;skeletal muscle;breast;lung;placenta;visual apparatus;liver;cervix;spleen;kidney;stomach; superior cervical ganglion;testis;globus pallidus;pons;trigeminal ganglion;skeletal muscle; 0.60912 0.11612 0.45192103 78.03727294 242.73747 3.36359 ZFP64P1 . . . ZFP64 zinc finger protein pseudogene 1 . . . . . . . . . . . ZFP69 8.55771991050002e-08 0.291962475511652 0.708037438911149 ZFP69 zinc finger protein FUNCTION: May be involved in transcriptional regulation.; . . . . 0.16815 0.09324 0.86534717 88.80042463 113.1556 2.31534 ZFP69B 2.52121150457695e-09 0.0414025592217578 0.958597438257031 ZFP69 zinc finger protein B FUNCTION: May be involved in transcriptional regulation.; . . . . 0.12978 . 1.10969368 92.05590941 1480.59123 7.16368 ZFP82 0.0523308001818033 0.943306371333133 0.00436282848506377 ZFP82 zinc finger protein FUNCTION: May be involved in transcriptional regulation.; . . . . 0.21129 . -0.670411825 15.61689078 17.36454 0.60978 ZFP90 0.00886192807104427 0.988574244063218 0.00256382786573773 ZFP90 zinc finger protein FUNCTION: May function as a repressor or silencer protein, and most likely exerts its repressing activity upon zinc-dependent binding to DNA. May be involved in proper spermatogenesis by repressing the expression of genes unnecessary or incompatible with the maintenance of a haploid cell state (By similarity). Isoform 2 acts as a bridge between FOXP3 and the corepressor TRIM28, and is required for the transcriptional repressor activity of FOXP3 in regulatory T-cells (Treg) (PubMed:23543754). {ECO:0000250|UniProtKB:Q61967, ECO:0000269|PubMed:23543754}.; . TISSUE SPECIFICITY: Isoform 2 is highly expressed in the regulatory T-cells (Treg). {ECO:0000269|PubMed:23543754}.; . . 0.16570 . -0.26993514 34.59542345 41.67204 1.21415 ZFP91 0.983773002727888 0.0162266044344686 3.92837643478625e-07 ZFP91 zinc finger protein FUNCTION: Atypical E3 ubiquitin-protein ligase that mediates 'Lys- 63'-linked ubiquitination of MAP3K14/NIK, leading to stabilize and activate MAP3K14/NIK. It thereby acts as an activator of the non- canonical NF-kappa-B2/NFKB2 pathway. May also play an important role in cell proliferation and/or anti-apoptosis. {ECO:0000269|PubMed:12738986, ECO:0000269|PubMed:20682767}.; . TISSUE SPECIFICITY: Expressed ubiquitously, particularly at high level in testis. Isoform 2 is testis specific.; ovary;sympathetic chain;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;spleen;cervix;mammary gland;salivary gland;developmental;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;bone;testis;dura mater;artery;unclassifiable (Anatomical System);meninges;lymph node;lacrimal gland;islets of Langerhans;bile duct;pancreas;lung;pia mater;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;skeletal muscle;cerebellum; . 0.28128 0.373041938 75.29488087 2064.91149 8.37242 ZFP91-CNTF . . . ZFP91-CNTF readthrough (NMD candidate) . . . . . . . . . . . ZFP92 0.529624187284892 0.409621858592771 0.0607539541223366 ZFP92 zinc finger protein FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . 0.07626 . . . 39.84066 1.17323 ZFPL1 0.654739309143482 0.344061167792823 0.00119952306369445 zinc finger protein like 1 FUNCTION: Required for cis-Golgi integrity and efficient ER to Golgi transport. Involved in the maintenance of the integrity of the cis-Golgi, possibly via its interaction with GOLGA2/GM130. {ECO:0000269|PubMed:18323775}.; . TISSUE SPECIFICITY: Expressed strongly in the exocrine pancreas. {ECO:0000269|PubMed:9653652}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pineal body;muscle;blood;lens;skeletal muscle;bile duct;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion; 0.12855 0.09910 0.308721233 72.59966973 429.25282 4.32727 ZFPM1 0.0314918366014913 0.959089121283133 0.00941904211537572 zinc finger protein, FOG family member 1 FUNCTION: Transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. Essential cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family GATA1, GATA2 and GATA3. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promoter context. The heterodimer formed with GATA proteins is essential to activate expression of genes such as NFE2, ITGA2B, alpha- and beta-globin, while it represses expression of KLF1. May be involved in regulation of some genes in gonads. May also be involved in cardiac development, in a non-redundant way with ZFPM2/FOG2 (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Mainly expressed in hematopoietic tissues. Also expressed in adult cerebellum, stomach, lymph node, liver and pancreas. Expressed in fetal heart, liver and spleen. {ECO:0000269|PubMed:12483298}.; unclassifiable (Anatomical System);pancreas;lung;ovary;testis;blood;kidney;retina; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.18944 . . . 1660.90603 7.52751 ZFPM2 0.999955693827333 4.43061673342618e-05 5.33294752349352e-12 zinc finger protein, FOG family member 2 FUNCTION: Transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis. Essential cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family GATA4, GATA5 and GATA6. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promoter context. Also required in gonadal differentiation, possibly be regulating expression of SRY. Probably acts a corepressor of NR2F2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:10438528}.; DISEASE: Tetralogy of Fallot (TOF) [MIM:187500]: A congenital heart anomaly which consists of pulmonary stenosis, ventricular septal defect, dextroposition of the aorta (aorta is on the right side instead of the left) and hypertrophy of the right ventricle. In this condition, blood from both ventricles (oxygen-rich and oxygen-poor) is pumped into the body often causing cyanosis. {ECO:0000269|PubMed:14517948, ECO:0000269|PubMed:20807224}. Note=The disease may be caused by mutations affecting the gene represented in this entry.; DISEASE: Diaphragmatic hernia 3 (DIH3) [MIM:610187]: Form of congenital diaphragmatic hernia (CDH). CDH refers to a group of congenital defects in the structural integrity of the diaphragm associated with often lethal pulmonary hypoplasia and pulmonary hypertension. {ECO:0000269|PubMed:16103912}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: 46,XY sex reversal 9 (SRXY9) [MIM:616067]: A disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females or have ambiguous external genitalia. {ECO:0000269|PubMed:24549039}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Conotruncal heart malformations (CTHM) [MIM:217095]: A group of congenital heart defects involving the outflow tracts. Examples include truncus arteriosus communis, double-outlet right ventricle and transposition of great arteries. Truncus arteriosus communis is characterized by a single outflow tract instead of a separate aorta and pulmonary artery. In transposition of the great arteries, the aorta arises from the right ventricle and the pulmonary artery from the left ventricle. In double outlet of the right ventricle, both the pulmonary artery and aorta arise from the right ventricle. {ECO:0000269|PubMed:20807224}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed at low level. {ECO:0000269|PubMed:10438528}.; . . 0.56230 0.26433 0.519883383 80.37272942 1899.90602 8.01507 ZFPM2-AS1 . . . ZFPM2 antisense RNA 1 . . . . . . . . . . . ZFR 0.999999670342593 3.29657406590444e-07 7.0568313684701e-18 zinc finger RNA binding protein FUNCTION: Involved in postimplantation and gastrulation stages of development. Involved in the nucleocytoplasmic shuttling of STAU2. Binds to DNA and RNA (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in lung, liver, lymphocytes, heart, pancreas, placenta, brain and kidney. {ECO:0000269|PubMed:11574164}.; myocardium;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;gall bladder;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;peripheral nerve;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;uterus;whole body;bone;pituitary gland;testis;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;pancreas;lung;mesenchyma;adrenal gland;placenta;hypopharynx;head and neck;kidney;stomach;aorta;cerebellum;thymus; amygdala;dorsal root ganglion;medulla oblongata;superior cervical ganglion;occipital lobe;hypothalamus;spinal cord;pons;atrioventricular node;caudate nucleus;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;trigeminal ganglion;parietal lobe; 0.63808 0.14804 -0.754958418 13.57631517 2316.48591 8.91305 ZFR2 5.37163859231556e-09 0.613842864210318 0.386157130418043 zinc finger RNA binding protein 2 . . . unclassifiable (Anatomical System);optic nerve;ovary;macula lutea;testis;fovea centralis;choroid;lens;retina; superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.10908 0.09177 0.389427191 75.7136117 3463.77958 11.32660 ZFRP1 . . . zinc finger RNA binding protein pseudogene 1 . . . . . . . . . . . ZFX 0.986133449821669 0.0138600373247255 6.51285360548868e-06 zinc finger protein, X-linked FUNCTION: Probable transcriptional activator.; . . unclassifiable (Anatomical System);amygdala;cartilage;lacrimal gland;colon;lens;skeletal muscle;nasopharynx;placenta;liver;testis;spleen;cervix;germinal center;kidney;bladder;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.48662 0.23781 -0.22584292 37.32012267 41.69961 1.21503 ZFX-AS1 . . . ZFX antisense RNA 1 . . . . . . . . . . . ZFY 0.255459999135225 0.640500770500147 0.104039230364628 zinc finger protein, Y-linked FUNCTION: Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3'. {ECO:0000269|PubMed:20028140}.; . . unclassifiable (Anatomical System);amygdala;lymph node;choroid;fovea centralis;lens;retina;optic nerve;macula lutea;liver;testis;kidney;mammary gland;peripheral nerve; ciliary ganglion;trigeminal ganglion; 0.40008 . . . 1.92553 0.05992 ZFY-AS1 . . . ZFY antisense RNA 1 . . . . . . . . . . . ZFYVE1 0.953726202611526 0.0462727303347095 1.06705376434749e-06 zinc finger FYVE-type containing 1 . . TISSUE SPECIFICITY: Isoform 1 is expressed in all tissues examined, including, brain, placenta, lung, liver, skeletal muscle, pancreas and kidney. Isoform 1 and isoform 2 are highly expressed in heart. Isoform 2 is also detected in the testis.; myocardium;ovary;sympathetic chain;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;larynx;bone;testis;dura mater;brain;unclassifiable (Anatomical System);meninges;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;greater omentum;bile duct;pia mater;lung;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;mammary gland;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.28604 0.12030 -1.195919584 5.832743572 270.27144 3.52655 ZFYVE9 0.943796743559468 0.0562032420307089 1.44098235469962e-08 zinc finger FYVE-type containing 9 FUNCTION: Early endosomal protein that functions to recruit SMAD2/SMAD3 to intracellular membranes and to the TGF-beta receptor. Plays a significant role in TGF-mediated signaling by regulating the subcellular location of SMAD2 and SMAD3 and modulating the transcriptional activity of the SMAD3/SMAD4 complex. Possibly associated with TGF-beta receptor internalization. {ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:9865696}.; . TISSUE SPECIFICITY: Ubiquitous. In the brain found primarily in the cerebrovascular smooth muscle cells and reactive astrocytes.; ovary;colon;fovea centralis;choroid;vein;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;testis;amniotic fluid;brain;unclassifiable (Anatomical System);blood;lens;skeletal muscle;breast;lung;macula lutea;liver;hypopharynx;head and neck;cervix;kidney;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;parietal lobe;skeletal muscle; 0.56197 . 0.141451114 63.65298419 704.41303 5.27447 ZFYVE9P1 . . . zinc finger FYVE-type containing 9 pseudogene 1 . . . . . . . . . . . ZFYVE9P2 . . . zinc finger FYVE-type containing 9 pseudogene 2 . . . . . . . . . . . ZFYVE16 1.30484002602704e-08 0.999406628899248 0.000593358052351723 zinc finger FYVE-type containing 16 FUNCTION: May be involved in regulating membrane trafficking in the endosomal pathway. Overexpression induces endosome aggregation. Required to target TOM1 to endosomes. {ECO:0000269|PubMed:11546807, ECO:0000269|PubMed:14613930}.; . TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney, placenta and lung. Expressed at intermediate level in heart, brain, skeletal muscle, spleen and liver. Weakly expressed in colon, thymus and peripheral blood lymphocytes. {ECO:0000269|PubMed:11546807}.; ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;spinal cord;urinary;pharynx;blood;skeletal muscle;breast;lung;cornea;trabecular meshwork;placenta;visual apparatus;liver;spleen;kidney;mammary gland;stomach; occipital lobe;parietal lobe;skeletal muscle; 0.57349 0.09764 1.214325842 93.08209483 331.12654 3.87096 ZFYVE19 7.40857843667129e-09 0.68363151360932 0.316368478982101 zinc finger FYVE-type containing 19 FUNCTION: Key regulator of abscission step in cytokinesis: part of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. Together with CHMP4C, required to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. Deactivation of AURKB results in dephosphorylation of CHMP4C followed by its dissociation from ZFYVE19/ANCHR and VPS4 and subsequent abscission. {ECO:0000269|PubMed:24814515}.; DISEASE: Note=A chromosomal aberration involving ZFYVE19 is associated with acute myeloblastic leukemia (AML). Translocation t(11;15)(q23;q14) with KMT2A/MLL1 (PubMed:12618766). {ECO:0000269|PubMed:12618766}.; TISSUE SPECIFICITY: Detected in brain, heart, skeletal muscle, kidney and liver. {ECO:0000269|PubMed:12618766}.; medulla oblongata;ovary;colon;fovea centralis;choroid;skin;bone marrow;uterus;prostate;endometrium;thyroid;bone;germinal center;brain;unclassifiable (Anatomical System);lymph node;trophoblast;heart;cartilage;hypothalamus;blood;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;alveolus;spleen;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.03227 . 1.620475625 96.01321066 3143.27655 10.68088 ZFYVE21 0.713442898007109 0.283292803704045 0.00326429828884598 zinc finger FYVE-type containing 21 FUNCTION: Plays a role in cell adhesion, and thereby in cell motility which requires repeated formation and disassembly of focal adhesions. Regulates microtubule-induced PTK2/FAK1 dephosphorylation, an event important for focal adhesion disassembly, as well as integrin beta-1/ITGB1 cell surface expression. {ECO:0000269|PubMed:20439989, ECO:0000269|PubMed:21768110}.; . . lymphoreticular;medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;cerebral cortex;cochlea;endometrium;larynx;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;bile duct;pancreas;lung;cornea;placenta;visual apparatus;hippocampus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach;cerebellum; globus pallidus; 0.10956 . 0.194852702 67.03231894 49.58536 1.37814 ZFYVE26 1.03844572602961e-11 0.99999998403029 1.59593255760405e-08 zinc finger FYVE-type containing 26 FUNCTION: Phosphatidylinositol 3-phosphate-binding protein required for the abcission step in cytokinesis: recruited to the midbody during cytokinesis and acts as a regulator of abcission. May also be required for efficient homologous recombination DNA double-strand break repair. {ECO:0000269|PubMed:20208530}.; DISEASE: Spastic paraplegia 15, autosomal recessive (SPG15) [MIM:270700]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG15 is a complex form associated with additional neurological symptoms such as cognitive deterioration or mental retardation, axonal neuropathy, mild cerebellar signs, and, less frequently, a central hearing deficit, decreased visual acuity, or retinal degeneration. {ECO:0000269|PubMed:18394578, ECO:0000269|PubMed:19084844, ECO:0000269|PubMed:19805727}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Strongest expression in the adrenal gland, bone marrow, adult brain, fetal brain, lung, placenta, prostate, skeletal muscle, testis, thymus, and retina. Intermediate levels are detected in other structures, including the spinal cord. {ECO:0000269|PubMed:18394578}.; lymphoreticular;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; superior cervical ganglion;globus pallidus;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.08330 0.10527 -0.274087418 33.5928285 2850.19714 10.09609 ZFYVE27 0.00370395320426504 0.987351433302286 0.0089446134934492 zinc finger FYVE-type containing 27 FUNCTION: Functions as an upstream inhibitor of RAB11, regulating directional protein transport to the forming neurites. Involved in nerve growth factor-induced neurite formation. May have a more general role in cell projections formation. {ECO:0000269|PubMed:17082457, ECO:0000269|PubMed:19289470}.; DISEASE: Spastic paraplegia 33, autosomal dominant (SPG33) [MIM:610244]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. {ECO:0000269|PubMed:16826525}. Note=The disease is caused by mutations affecting the gene represented in this entry. According to PubMed:18606302, the properties of the variant Val- 191 and its frequency in some populations raise doubts on the implication of that gene in the disease.; . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;oesophagus;endometrium;bone;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;islets of Langerhans;muscle;urinary;adrenal cortex;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;cervix;kidney;mammary gland;stomach;thymus; atrioventricular node;cingulate cortex; 0.13998 0.10806 0.86534717 88.80042463 535.80725 4.71912 ZFYVE28 0.88846014978575 0.111529780060512 1.00701537384879e-05 zinc finger FYVE-type containing 28 FUNCTION: Negative regulator of epidermal growth factor receptor (EGFR) signaling. Acts by promoting EGFR degradation in endosomes when not monoubiquitinated. {ECO:0000269|PubMed:19460345}.; . . unclassifiable (Anatomical System);cartilage;islets of Langerhans;colon;uterus;optic nerve;lung;endometrium;visual apparatus;hypopharynx;head and neck;spleen;kidney;brain;cerebellum; . 0.20657 . -0.540190972 20.0401038 571.7541 4.85144 ZG16 . . . zymogen granule protein 16 FUNCTION: May play a role in protein trafficking. May act as a linker molecule between the submembranous matrix on the luminal side of zymogen granule membrane (ZGM) and aggregated secretory proteins during granule formation in the TGN. {ECO:0000269|PubMed:17307141}.; . TISSUE SPECIFICITY: Highly expressed in liver. Detected at lower levels in colon, ileum and jejunum. {ECO:0000269|PubMed:17307141}.; . . . . 0.924227736 89.61429582 131.51738 2.49616 ZG16B 0.00409470688609179 0.653623986121439 0.342281306992469 zymogen granule protein 16B . . . . . . . 0.505321956 80.00707714 127.11884 2.45923 ZGLP1 0.437504524225803 0.531930978305974 0.0305644974682232 zinc finger, GATA-like protein 1 FUNCTION: Transcriptional repressor that plays a central role in somatic cells of the gonad and is required for germ cell development. Able to repress GATA transcription factor function (By similarity). {ECO:0000250}.; . . . . . . 0.170987912 65.5579146 80.87357 1.90093 ZGPAT 2.80185523268214e-05 0.774651468637227 0.225320512810446 zinc finger CCCH-type and G-patch domain containing FUNCTION: Transcription repressor that specifically binds the 5'- GGAG[GA]A[GA]A-3' consensus sequence. Represses transcription by recruiting the chromatin multiprotein complex NuRD to target promoters. Negatively regulates expression of EGFR, a gene involved in cell proliferation, survival and migration. Its ability to repress genes of the EGFR pathway suggest it may act as a tumor suppressor. Able to suppress breast carcinogenesis. {ECO:0000269|PubMed:19644445}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19644445}.; ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;cervix;kidney;mammary gland;stomach; liver;globus pallidus;kidney;skeletal muscle; 0.14938 0.10704 -0.709045403 14.673272 60.79446 1.58553 ZGRF1 . . . zinc finger GRF-type containing 1 . . . . . 0.05629 . . . . . ZHX1 0.821482966948104 0.178342291527281 0.000174741524614655 zinc fingers and homeoboxes 1 FUNCTION: Acts as a transcriptional repressor. Increases DNMT3B- mediated repressive transcriptional activity when DNMT3B is tethered to DNA. May link molecule between DNMT3B and other co- repressor proteins. {ECO:0000269|PubMed:12237128}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in podocytes. {ECO:0000269|PubMed:10441475, ECO:0000269|PubMed:17056598}.; ovary;colon;substantia nigra;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;thyroid;iris;pituitary gland;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;lens;skeletal muscle;breast;lung;mesenchyma;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; whole brain;amygdala;subthalamic nucleus;fetal brain;hypothalamus;thyroid;prefrontal cortex;cingulate cortex; 0.31071 0.11598 -0.799052816 12.45576787 68.43508 1.71244 ZHX1-C8orf76 . . . ZHX1-C8orf76 readthrough . . . . . . . . . . . ZHX2 0.408482948991885 0.59115566970397 0.000361381304144627 zinc fingers and homeoboxes 2 FUNCTION: Acts as a transcriptional repressor. Represses the promoter activity of the CDC25C gene stimulated by NFYA. {ECO:0000269|PubMed:12741956}.; . TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in podocytes. {ECO:0000269|PubMed:12741956, ECO:0000269|PubMed:17056598}.; lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;bone;thyroid;pituitary gland;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;hypopharynx;liver;spleen;head and neck;kidney; dorsal root ganglion; 0.33511 0.15229 -1.098660656 6.95329087 1366.57953 6.93410 ZHX3 0.354421202947907 0.645030827494446 0.000547969557647497 zinc fingers and homeoboxes 3 FUNCTION: Acts as a transcriptional repressor. Involved in the early stages of mesenchymal stem cell (MSC) osteogenic differentiation. Is a regulator of podocyte gene expression during primary glomerula disease. Binds to promoter DNA. {ECO:0000269|PubMed:12659632, ECO:0000269|PubMed:21174497}.; . TISSUE SPECIFICITY: Widely expressed. High expression in kidney. Expressed during osteogenic differentiation. {ECO:0000269|PubMed:12659632, ECO:0000269|PubMed:21174497}.; colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;thyroid;bone;testis;germinal center;brain;gall bladder;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;skeletal muscle;breast;lung;epididymis;adrenal gland;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland; prefrontal cortex;ciliary ganglion;pons;trigeminal ganglion; 0.16396 0.10118 -0.196519234 39.20736023 612.2258 4.99985 ZIC1 0.825224393438112 0.173967998117965 0.00080760844392335 Zic family member 1 FUNCTION: Acts as a transcriptional activator. Involved in neurogenesis. Plays important roles in the early stage of organogenesis of the CNS, as well as during dorsal spinal cord development and maturation of the cerebellum. Involved in the spatial distribution of mossy fiber (MF) neurons within the pontine gray nucleus (PGN). Plays a role in the regulation of MF axon pathway choice. Promotes MF migration towards ipsilaterally- located cerebellar territories. May have a role in shear flow mechanotransduction in osteocytes. Retains nuclear GLI1 and GLI3 in the cytoplasm. Binds to the minimal GLI-consensus sequence 5'- TGGGTGGTC-3' (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: CNS. A high level expression is seen in the cerebellum. Detected in the nuclei of the cerebellar granule cell lineage from the progenitor cells of the external germinal layer to the postmigrated cells of the internal granular layer. Detected in medulloblastoma (26/29 cases), but not present in all other tumors examined. {ECO:0000269|PubMed:8542595}.; unclassifiable (Anatomical System);optic nerve;frontal lobe;cochlea;macula lutea;liver;fovea centralis;choroid;lens;brain;retina; dorsal root ganglion;whole brain;amygdala;medulla oblongata;superior cervical ganglion;thalamus;occipital lobe;olfactory bulb;cerebellum peduncles;hypothalamus;spinal cord;pons;atrioventricular node;caudate nucleus;subthalamic nucleus;prefrontal cortex;ciliary ganglion;trigeminal ganglion;cingulate cortex;cerebellum; 0.82243 0.28104 -0.494039303 22.09247464 7.00216 0.26153 ZIC2 . . . Zic family member 2 FUNCTION: Acts as a transcriptional activator or repressor. Plays important roles in the early stage of organogenesis of the CNS. Activates the transcription of the serotonin transporter SERT in uncrossed ipsilateral retinal ganglion cells (iRGCs) to refine eye-specific projections in primary visual targets. Its transcriptional activity is repressed by MDFIC. Involved in the formation of the ipsilateral retinal projection at the optic chiasm midline. Drives the expression of EPHB1 on ipsilaterally projecting growth cones. Binds to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3'. Associates to the basal SERT promoter region from ventrotemporal retinal segments of retinal embryos.; DISEASE: Holoprosencephaly 5 (HPE5) [MIM:609637]: A structural anomaly of the brain, in which the developing forebrain fails to correctly separate into right and left hemispheres. Holoprosencephaly is genetically heterogeneous and associated with several distinct facies and phenotypic variability. {ECO:0000269|PubMed:11285244, ECO:0000269|PubMed:15221788, ECO:0000269|PubMed:19177455}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . . . 0.87813 0.23021 . . 382.0785 4.12056 ZIC3 0.822806978202031 0.173226408980932 0.00396661281703704 Zic family member 3 FUNCTION: Acts as transcriptional activator. Required in the earliest stages in both axial midline development and left-right (LR) asymmetry specification. Binds to the minimal GLI-consensus sequence 5'-GGGTGGTC-3'. {ECO:0000269|PubMed:17764085}.; DISEASE: Heterotaxy, visceral, 1, X-linked (HTX1) [MIM:306955]: A form of visceral heterotaxy, a complex disorder due to disruption of the normal left-right asymmetry of the thoracoabdominal organs. Visceral heterotaxy or situs ambiguus results in randomization of the placement of visceral organs, including the heart, lungs, liver, spleen, and stomach. The organs are oriented randomly with respect to the left-right axis and with respect to one another. It can been associated with variety of congenital defects including cardiac malformations. {ECO:0000269|PubMed:14681828, ECO:0000269|PubMed:17295247, ECO:0000269|PubMed:24123890, ECO:0000269|PubMed:9354794}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: VACTERL association X-linked with or without hydrocephalus (VACTERLX) [MIM:314390]: A syndrome characterized by a non-random association of congenital defects. Affected individuals manifest vertebral anomalies (V), anal atresia (A), cardiac malformations (C), tracheoesophageal fistula (TE), renal anomalies (R) such as urethral atresia with hydronephrosis, and limb anomalies (L) such as hexadactyly, humeral hypoplasia, radial aplasia, and proximally placed thumb. Some patients may have hydrocephalus. Some cases of VACTERL-H are associated with increased chromosome breakage and rearrangement. {ECO:0000269|PubMed:20452998, ECO:0000269|PubMed:24123890}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Congenital heart defects, multiple types, 1, X-linked (CHTD1) [MIM:306955]: A disorder characterized by congenital developmental abnormalities involving structures of the heart. Common defects include transposition of the great arteries, aortic stenosis, atrial septal defect, ventricular septal defect, pulmonic stenosis, and patent ductus arteriosus. The etiology of CHTD is complex, with contributions from environmental exposure, chromosomal abnormalities, and gene defects. Some patients with CHTD also have cardiac arrhythmias, which may be due to the anatomic defect itself or to surgical interventions. {ECO:0000269|PubMed:14681828, ECO:0000269|PubMed:24123890}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);whole body;thyroid;visual apparatus;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;cerebellum; 0.88808 0.16755 0.613741468 83.06794055 57.6505 1.53401 ZIC4 0.00181690392137032 0.900072855765412 0.0981102403132173 Zic family member 4 FUNCTION: Binds to DNA. {ECO:0000250}.; . . . . 0.20879 0.10422 -0.047654689 50.22410946 125.09939 2.43427 ZIC4-AS1 . . . ZIC4 antisense RNA 1 . . . . . . . . . . . ZIC5 . . . Zic family member 5 FUNCTION: Essential for neural crest development, converting cells from an epidermal fate to a neural crest cell fate. Binds to DNA (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);hypopharynx;head and neck; superior cervical ganglion;trigeminal ganglion;cerebellum; 0.62645 . . . 294.89024 3.66632 ZIK1 4.78889151995357e-08 0.117774224674036 0.882225727437049 zinc finger protein interacting with K protein 1 FUNCTION: May be a transcriptional repressor. {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed at high levels in gastric glands, and at low levels in colon and small intestine. Silenced through promoter methylation in gastric glands with intestinal metaplasia. {ECO:0000269|PubMed:17071588}.; unclassifiable (Anatomical System);ovary;placenta;visual apparatus;liver;kidney;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.04582 0.09612 -0.359940251 28.93371078 38.80852 1.14886 ZIK1P1 . . . zinc finger protein interacting with K protein 1 pseudogene 1 . . . . . . . . . . . ZIM2 0.4720933939618 0.527683986296418 0.00022261974178203 zinc finger imprinted 2 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Highest levels of expression in adult testis; modest levels in fetal kidney and brain.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;hypothalamus;developmental;adrenal cortex;skin;skeletal muscle;uterus;prostate;whole body;lung;frontal lobe;adrenal gland;placenta;visual apparatus;liver;testis;head and neck;spleen;kidney;brain; dorsal root ganglion;whole brain;amygdala;thalamus;occipital lobe;medulla oblongata;superior cervical ganglion;hypothalamus;temporal lobe;spinal cord;adrenal cortex;pons;caudate nucleus;atrioventricular node;skeletal muscle;subthalamic nucleus;fetal liver;adrenal gland;prefrontal cortex;globus pallidus;testis;ciliary ganglion;cingulate cortex;parietal lobe;pituitary; . 0.20319 0.913082291 89.54352442 335.25596 3.88995 ZIM2-AS1 . . . ZIM2 antisense RNA 1 . . . . . . . . . . . ZIM3 4.31741951284123e-11 0.0141436327790723 0.985856367177753 zinc finger imprinted 3 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.11008 0.07966 1.423841958 94.96933239 3426.60671 11.23712 ZKSCAN1 0.607275236573615 0.392352399023623 0.000372364402762366 zinc finger with KRAB and SCAN domains 1 FUNCTION: May be involved in transcriptional regulation.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);amygdala;heart;tongue;islets of Langerhans;pineal body;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;duodenum;liver;spleen;head and neck;kidney;stomach;peripheral nerve; superior cervical ganglion;prefrontal cortex;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe; 0.19422 0.11137 -0.712684326 14.49634348 55.17294 1.48966 ZKSCAN2 0.00293767473426787 0.996956494991457 0.000105830274275108 zinc finger with KRAB and SCAN domains 2 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);breast;frontal lobe;larynx;head and neck; superior cervical ganglion;atrioventricular node; 0.11037 . 0.343511191 73.73790988 3138.88928 10.66791 ZKSCAN3 0.000122608322341288 0.954841217265885 0.0450361744117733 zinc finger with KRAB and SCAN domains 3 FUNCTION: Transcriptional factor that binds to the consensus sequence 5'-[GT][AG][AGT]GGGG-3' and acts as a repressor of autophagy. Specifically represses expression of genes involved in autophagy and lysosome biogenesis/function such as MAP1LC3B, ULK1 or WIPI2. Associates with chromatin at the ITGB4 and VEGF promoters. Also acts as a transcription activator and promotes cancer cell progression and/or migation in various tumors and myelomas. {ECO:0000269|PubMed:18940803, ECO:0000269|PubMed:21057542, ECO:0000269|PubMed:22531714, ECO:0000269|PubMed:23434374}.; . . unclassifiable (Anatomical System);heart;colon;blood;bone marrow;pancreas;prostate;lung;frontal lobe;placenta;testis;spleen;kidney;brain;aorta;stomach; dorsal root ganglion;superior cervical ganglion;pons;atrioventricular node;skeletal muscle; 0.16002 0.10481 0.507139401 80.10143902 1012.24764 6.12715 ZKSCAN4 6.74288454800845e-05 0.90633643975165 0.0935961314028695 zinc finger with KRAB and SCAN domains 4 FUNCTION: May be involved in the transcriptional activation of MDM2 and EP300 genes. {ECO:0000269|PubMed:17910948}.; . TISSUE SPECIFICITY: Expressed in adult heart, brain, placenta, lung and kidney, but not in adult liver and skeletal muscle. In 17-day old embryo, detected in liver, skeletal muscle, brain, heart and small intestine. {ECO:0000269|PubMed:17910948}.; unclassifiable (Anatomical System);testis;cervix;kidney;brain;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;skeletal muscle; 0.10411 0.09109 -0.534490515 20.70063694 743.49162 5.41279 ZKSCAN5 0.000618302540533773 0.994509867312363 0.00487183014710285 zinc finger with KRAB and SCAN domains 5 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);cartilage;heart;lens;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; superior cervical ganglion;testis - interstitial;testis;atrioventricular node;trigeminal ganglion; 0.38375 0.09256 -0.709045403 14.673272 95.57232 2.11095 ZKSCAN7 1.17628257340827e-05 0.947584804044551 0.0524034331297145 zinc finger with KRAB and SCAN domains 7 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.13796 0.27869 0.935129812 89.86199575 2168.67909 8.57395 ZKSCAN7P1 . . . zinc finger with KRAB and SCAN domains 7 pseudogene 1 . . . . . . . . . . . ZKSCAN8 0.000231594506551783 0.980492380073096 0.0192760254203525 zinc finger with KRAB and SCAN domains 8 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.15170 0.10440 0.485092724 79.37603208 412.96116 4.25451 ZMAT1 0.0639505147007786 0.920805587031523 0.0152438982676981 zinc finger matrin-type 1 . . . . . 0.13791 . 0.218717575 68.27081859 33.23032 1.02705 ZMAT2 0.971433760073875 0.0285276235273582 3.8616398766377e-05 zinc finger matrin-type 2 . . . ovary;colon;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;pineal body;muscle;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; medulla oblongata;superior cervical ganglion;pons;caudate nucleus; 0.64216 0.11262 -0.031067188 51.03798066 2.53643 0.09383 ZMAT3 0.0567031582457627 0.924978652795848 0.018318188958389 zinc finger matrin-type 3 FUNCTION: Acts as a bona fide target gene of p53/TP53. May play a role in the TP53-dependent growth regulatory pathway. May contribute to TP53-mediated apoptosis by regulation of TP53 expression and translocation to the nucleus and nucleolus. {ECO:0000269|PubMed:11571644}.; . TISSUE SPECIFICITY: Highly expressed in adult brain, and moderately in adult kidney and testis. Not detected in fetal brain, heart, pancreas, adrenal gland, liver or small intestine. {ECO:0000269|PubMed:11689294}.; unclassifiable (Anatomical System);ovary;gum;bone;visual apparatus;testis;cervix;kidney;brain;mammary gland;skin;stomach;bone marrow; superior cervical ganglion;medulla oblongata;appendix;trigeminal ganglion;cingulate cortex;parietal lobe; 0.12301 0.11523 -0.449946534 24.00330267 16.12611 0.57136 ZMAT4 0.0193268627627965 0.900248847344758 0.0804242898924452 zinc finger matrin-type 4 . . . unclassifiable (Anatomical System);optic nerve;lung;thyroid;macula lutea;testis;fovea centralis;choroid;lens;brain;retina; superior cervical ganglion;subthalamic nucleus;thalamus;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.54258 . -0.007201372 53.19061099 1054.63352 6.23498 ZMAT5 0.000193622547453497 0.716361057717362 0.283445319735184 zinc finger matrin-type 5 . . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;islets of Langerhans;pharynx;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;kidney;mammary gland; superior cervical ganglion;liver; 0.13275 . 0.125076652 62.7388535 28.10381 0.90146 ZMIZ1 0.999743700872505 0.000256299124316734 3.17807582517501e-12 zinc finger MIZ-type containing 1 FUNCTION: Increases ligand-dependent transcriptional activity of AR and promotes AR sumoylation. The stimulation of AR activity is dependent upon sumoylation.; . TISSUE SPECIFICITY: Expressed most abundantly in ovary and, at lower levels, in prostate, spleen and testis. Weak expression, if any, in thymus, small intestine, colon and peripheral blood leukocytes. {ECO:0000269|PubMed:14609956}.; smooth muscle;ovary;colon;parathyroid;fovea centralis;skin;retina;bone marrow;uterus;prostate;whole body;cochlea;endometrium;synovium;larynx;bone;thyroid;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;adrenal gland;trabecular meshwork;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;testis;ciliary ganglion;skeletal muscle; 0.40001 0.12338 -2.037519759 1.657230479 62.02267 1.60541 ZMIZ1-AS1 . . . ZMIZ1 antisense RNA 1 . . . . . . . . . . . ZMIZ2 0.999620382312933 0.000379617646169609 4.08978513889896e-11 zinc finger MIZ-type containing 2 FUNCTION: Increases ligand-dependent transcriptional activity of AR and other nuclear hormone receptors. {ECO:0000269|PubMed:16051670}.; . TISSUE SPECIFICITY: Expressed most abundantly in testis with lower levels in heart, brain, pancreas, prostate and ovary. {ECO:0000269|PubMed:16051670}.; ovary;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;cochlea;endometrium;bone;thyroid;iris;pituitary gland;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);cartilage;heart;lacrimal gland;tongue;islets of Langerhans;blood;skeletal muscle;breast;pancreas;lung;epididymis;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;thymus;peripheral nerve; dorsal root ganglion;superior cervical ganglion;occipital lobe;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.21655 0.09565 -0.08446956 47.15145081 1705.86311 7.61894 ZMPSTE24 1.25000649755402e-07 0.572048077696411 0.427951797302939 zinc metallopeptidase STE24 FUNCTION: Proteolytically removes the C-terminal three residues of farnesylated proteins. Acts on lamin A/C.; DISEASE: Mandibuloacral dysplasia with type B lipodystrophy (MADB) [MIM:608612]: A disorder characterized by mandibular and clavicular hypoplasia, acroosteolysis, delayed closure of the cranial suture, joint contractures, and generalized lipodystrophy with loss of subcutaneous fat from the extremities, face, neck and trunk. {ECO:0000269|PubMed:12913070, ECO:0000269|PubMed:17152860, ECO:0000269|PubMed:18435794, ECO:0000269|PubMed:20814950}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Lethal tight skin contracture syndrome (LTSCS) [MIM:275210]: Rare disorder mainly characterized by intrauterine growth retardation, tight and rigid skin with erosions, prominent superficial vasculature and epidermal hyperkeratosis, facial features (small mouth, small pinched nose and micrognathia), sparse/absent eyelashes and eyebrows, mineralization defects of the skull, thin dysplastic clavicles, pulmonary hypoplasia, multiple joint contractures and an early neonatal lethal course. Liveborn children usually die within the first week of life. The overall prevalence of consanguineous cases suggested an autosomal recessive inheritance. {ECO:0000269|PubMed:15317753}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Widely expressed. High levels in kidney, prostate, testis and ovary.; . . 0.14921 0.33283 -0.648365105 16.35999056 30.24713 0.96505 ZMYM1 0.0017290006507811 0.9980438543542 0.000227144995019195 zinc finger MYM-type containing 1 . . . unclassifiable (Anatomical System);uterus;lung;heart;nasopharynx;liver;testis;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.05776 0.09143 0.578735925 82.29535268 682.5403 5.22169 ZMYM2 0.974459955902358 0.0255400440151269 8.25155682574346e-11 zinc finger MYM-type containing 2 FUNCTION: May function as a transcription factor.; DISEASE: Note=A chromosomal aberration involving ZMYM2 may be a cause of stem cell leukemia lymphoma syndrome (SCLL). Translocation t(8;13)(p11;q12) with FGFR1. SCLL usually presents as lymphoblastic lymphoma in association with a myeloproliferative disorder, often accompanied by pronounced peripheral eosinophilia and/or prominent eosinophilic infiltrates in the affected bone marrow. {ECO:0000269|PubMed:9716603}.; . . . 0.78369 0.21016 -1.284117362 5.113234253 65.37848 1.66429 ZMYM3 0.999966815937562 3.31840598005416e-05 2.63742069646399e-12 zinc finger MYM-type containing 3 FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:21834987}.; . TISSUE SPECIFICITY: Most abundant in brain, moderate in muscle and heart, low in other tissues except placenta.; ovary;colon;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;muscle;blood;skeletal muscle;bile duct;breast;lung;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;medulla oblongata;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;cingulate cortex; 0.61027 0.14229 -1.175687564 5.974286388 51.37774 1.41428 ZMYM4 0.999999928925947 7.10740533198176e-08 6.88134541414243e-21 zinc finger MYM-type containing 4 FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:21834987}.; . TISSUE SPECIFICITY: Expressed at higher level in heart, skeletal muscle, kidney and liver. {ECO:0000269|PubMed:10486218}.; ovary;salivary gland;parathyroid;skin;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;dura mater;germinal center;brain;bladder;pineal gland;unclassifiable (Anatomical System);meninges;cartilage;heart;lacrimal gland;islets of Langerhans;adrenal cortex;skeletal muscle;bile duct;breast;pancreas;pia mater;lung;adrenal gland;placenta;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;peripheral nerve;cerebellum; testis - interstitial;occipital lobe;medulla oblongata;superior cervical ganglion;cerebellum peduncles;temporal lobe;pons;atrioventricular node;caudate nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;testis;appendix;trigeminal ganglion;cingulate cortex; 0.73639 0.11434 -1.017713296 8.103326256 126.32764 2.44790 ZMYM4-AS1 . . . ZMYM4 antisense RNA 1 . . . . . . . . . . . ZMYM5 0.200378134555614 0.789571799736073 0.0100500657083131 zinc finger MYM-type containing 5 FUNCTION: Functions as a transcriptional regulator. {ECO:0000269|PubMed:17126306}.; . . unclassifiable (Anatomical System);uterus;frontal lobe;cartilage;adrenal gland;islets of Langerhans;visual apparatus;liver;testis;colon;blood;germinal center; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;appendix;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06748 0.07051 0.485092724 79.37603208 1157.52256 6.47872 ZMYM6 1.40245953692462e-08 0.997369246501599 0.00263073947380543 zinc finger MYM-type containing 6 FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:21834987}.; . TISSUE SPECIFICITY: Expressed at high levels in heart, skeletal muscle, kidney and liver. {ECO:0000269|PubMed:10486218}.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;oesophagus;cochlea;bone;thyroid;pituitary gland;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;pharynx;blood;skeletal muscle;breast;bile duct;lung;placenta;visual apparatus;hippocampus;liver;head and neck;kidney;mammary gland;cerebellum; uterus corpus;superior cervical ganglion; 0.14691 0.09058 -0.326979057 30.90351498 675.73333 5.19296 ZMYM6NB . . . ZMYM6 neighbor . . . . . . . . . 205.6394 3.09687 ZMYND8 0.999997106368404 2.89363159492358e-06 1.40127882316906e-15 zinc finger MYND-type containing 8 . . TISSUE SPECIFICITY: Expressed in all tissues examined with highest expression in brain, lung, pancreas, and placenta. Expressed in cutaneous T-cell lymphomas (CTCL).; myocardium;ovary;sympathetic chain;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;cochlea;endometrium;thyroid;amniotic fluid;germinal center;brain;heart;cartilage;spinal cord;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;alveolus;liver;cervix;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;pancreas;lung;pia mater;cornea;adrenal gland;placenta;head and neck;kidney;stomach; amygdala;dorsal root ganglion;superior cervical ganglion;medulla oblongata;adrenal cortex;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.16184 0.11555 -1.436656941 3.98089172 1935.06052 8.09452 ZMYND10 3.60239883453688e-07 0.79273660286775 0.207263036892366 zinc finger MYND-type containing 10 FUNCTION: Required for motile ciliary function. Probably involved in axonemal assembly of inner and outer dynein arms (IDA and ODA, respectively) for proper axoneme building for cilia motility. May act by indirectly regulating transcription of dynein proteins. {ECO:0000269|PubMed:23891469, ECO:0000269|PubMed:23891471}.; DISEASE: Ciliary dyskinesia, primary, 22 (CILD22) [MIM:615444]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia. Patients may exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. {ECO:0000269|PubMed:23891469, ECO:0000269|PubMed:23891471, ECO:0000269|PubMed:25186273}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);medulla oblongata;ovary;fovea centralis;choroid;lens;retina;optic nerve;lung;endometrium;bone;macula lutea;hippocampus;testis;spleen;cervix;brain; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12799 0.22567 0.374860183 75.43052607 111.84198 2.30174 ZMYND10-AS1 . . . ZMYND10 antisense RNA 1 . . . . . . . . . . . ZMYND11 0.999963586350186 3.64136465067502e-05 3.30696607838781e-12 zinc finger MYND-type containing 11 FUNCTION: Chromatin reader that specifically recognizes and binds histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and regulates RNA polymerase II elongation. Does not bind other histone H3 subtypes (H3.1 or H3.2) (By similarity). Colocalizes with highly expressed genes and functions as a transcription corepressor by modulating RNA polymerase II at the elongation stage. Acts as a tumor-suppressor by repressing a transcriptional program essential for tumor cell growth. {ECO:0000250|UniProtKB:Q8R5C8, ECO:0000269|PubMed:10734313, ECO:0000269|PubMed:16565076}.; DISEASE: Note=A chromosomal aberration involving ZMYND11 is a cause of acute poorly differentiated myeloid leukemia. Translocation (10;17)(p15;q21) with MBTD1.; DISEASE: Mental retardation, autosomal dominant 30 (MRD30) [MIM:616083]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD30 patients manifest mild intellectual disability and subtle facial dysmorphisms, including hypertelorism, ptosis, and a wide mouth. {ECO:0000269|PubMed:25217958}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16565076}.; medulla oblongata;smooth muscle;ovary;sympathetic chain;colon;skin;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;artery;unclassifiable (Anatomical System);amygdala;heart;tongue;islets of Langerhans;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;hippocampus;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;medulla oblongata;occipital lobe;hypothalamus;globus pallidus;caudate nucleus;parietal lobe; 0.18282 0.12022 -0.494039303 22.09247464 8.60335 0.31563 ZMYND12 0.00105994735075674 0.949869291692034 0.0490707609572092 zinc finger MYND-type containing 12 . . . . . 0.11307 . 0.306902668 72.38145789 81.45336 1.91126 ZMYND15 1.43624305354746e-05 0.998157386117329 0.00182825145213523 zinc finger MYND-type containing 15 FUNCTION: Acts as a transcriptional repressor through interaction with histone deacetylases (HDACs). May be important for spermiogenesis. {ECO:0000250|UniProtKB:Q8C0R7, ECO:0000303|PubMed:24431330}.; DISEASE: Spermatogenic failure 14 (SPGF14) [MIM:615842]: A disorder resulting in the absence (azoospermia) or reduction (oligozoospermia) of sperm in the semen, leading to male infertility. {ECO:0000269|PubMed:24431330}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . unclassifiable (Anatomical System);uterus;lung;cartilage;ovary;islets of Langerhans;testis;pharynx;kidney;brain;skin;stomach; testis - interstitial;medulla oblongata;testis - seminiferous tubule;testis; 0.18983 . -0.951568548 9.271054494 291.84505 3.65548 ZMYND19 0.879391539340359 0.120308267290349 0.000300193369292124 zinc finger MYND-type containing 19 FUNCTION: May be involved as a regulatory molecule in GPR24/MCH-R1 signaling.; . TISSUE SPECIFICITY: Expressed in brain, testis, placenta, heart, liver, skeletal muscle, kidney and stomach. {ECO:0000269|PubMed:12208518}.; unclassifiable (Anatomical System);heart;islets of Langerhans;skin;skeletal muscle;retina;uterus;whole body;endometrium;placenta;duodenum;liver;cervix;kidney;brain;mammary gland;stomach; testis - seminiferous tubule;tumor;testis; 0.15386 0.12378 -0.139478553 43.29440906 12.41971 0.45072 ZMYND19P1 . . . zinc finger MYND-type containing 19 pseudogene 1 . . . . . . . . . . . ZNF2 0.298104856888565 0.697691852872138 0.00420329023929669 zinc finger protein 2 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;pancreas;lung;frontal lobe;visual apparatus;liver;testis;cervix;spleen;kidney;brain;bladder;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.16810 0.13024 -0.624497208 17.16206653 20.79279 0.70458 ZNF3 0.0089610568357088 0.936958322101095 0.0540806210631965 zinc finger protein 3 FUNCTION: Involved in cell differentiation and/or proliferation.; . . smooth muscle;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;urinary;adrenal cortex;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion;parietal lobe; 0.50927 0.09485 -0.336073593 30.55555556 1041.71758 6.19689 ZNF7 0.000238233955048981 0.921184685629308 0.0785770804156434 zinc finger protein 7 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Ubiquitously present in many human cell lines of different embryological derivation.; ovary;colon;skin;retina;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;muscle;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.16768 0.09805 -1.03976177 7.802547771 46.29642 1.31036 ZNF8 . . . zinc finger protein 8 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Ubiquitously present in many human cell lines of different embryological derivation. {ECO:0000269|PubMed:2106481}.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;lung;frontal lobe;cornea;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland; skeletal muscle; 0.18845 0.09595 -0.574945567 18.90186365 36.10676 1.08396 ZNF10 0.000431500551933787 0.85970034602331 0.139868153424756 zinc finger protein 10 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);uterus;prostate;lung;larynx;sympathetic chain;testis;head and neck;brain;mammary gland;skin;peripheral nerve; testis;ciliary ganglion;skeletal muscle; 0.21851 0.09709 -0.359940251 28.93371078 365.1984 4.04326 ZNF12 0.551264006012047 0.448144487896219 0.000591506091734325 zinc finger protein 12 FUNCTION: Transcriptional repressor which suppresses activation protein 1 (AP-1)- and serum response element (SRE)-mediated transcriptional activity. {ECO:0000269|PubMed:16806083}.; . TISSUE SPECIFICITY: Widely expressed in various adult tissues and embryonic developmental stages (isoform 3). {ECO:0000269|PubMed:16806083}.; unclassifiable (Anatomical System);whole body;frontal lobe;endometrium;adrenal gland;placenta;visual apparatus;testis;colon;kidney;brain;skin;stomach; superior cervical ganglion; 0.14810 0.11170 -0.201976964 38.98325077 244.87662 3.37516 ZNF14 5.71582699182454e-16 0.0255062135652231 0.974493786434776 zinc finger protein 14 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);skeletal muscle;uterus;breast;lung;frontal lobe;endometrium;placenta;bone;liver;germinal center;brain;aorta;stomach; superior cervical ganglion;medulla oblongata;atrioventricular node;trigeminal ganglion; 0.18163 0.10236 -0.999300439 8.368719038 1246.84546 6.66836 ZNF16 4.586333335148e-12 0.026846168308471 0.973153831686943 zinc finger protein 16 FUNCTION: Acts as a transcriptional activator. Promotes cell proliferation by facilitating the cell cycle phase transition from the S to G2/M phase. Involved in both the hemin- and phorbol myristate acetate (PMA)-induced erythroid and megakaryocytic differentiation, respectively. Plays also a role as an inhibitor of cell apoptosis. {ECO:0000269|PubMed:16628192, ECO:0000269|PubMed:19763908, ECO:0000269|PubMed:21874239}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16628192}.; unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;colon;parathyroid;choroid;skin;uterus;prostate;lung;bone;placenta;visual apparatus;iris;liver;testis;cervix;germinal center;kidney;brain; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;atrioventricular node;trigeminal ganglion; 0.13331 0.09478 0.714657953 85.81623024 229.15341 3.27065 ZNF17 0.000331513211563741 0.818484215520302 0.181184271268134 zinc finger protein 17 FUNCTION: May be involved in transcriptional regulation.; . . uterus;lung;heart;islets of Langerhans;bone;adrenal cortex;skin; . 0.07226 0.10358 -0.198338176 39.17197452 123.33931 2.41835 ZNF18 0.000238202477981621 0.921172367599542 0.0785894299224766 zinc finger protein 18 FUNCTION: May be involved in transcriptional regulation.; . . medulla oblongata;ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;urinary;lens;skeletal muscle;lung;placenta;macula lutea;hippocampus;liver;head and neck;kidney; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.10759 0.10626 -0.067881249 48.69072895 152.16568 2.69887 ZNF19 1.78277433532571e-05 0.445652994281892 0.554329177974755 zinc finger protein 19 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;parathyroid;breast;prostate;lung;frontal lobe;larynx;thyroid;placenta;visual apparatus;testis;head and neck;germinal center;kidney;mammary gland; superior cervical ganglion; 0.34347 0.07885 -0.069700724 48.54328851 106.29511 2.23621 ZNF20 0.0235723668010903 0.962043612061792 0.0143840211371182 zinc finger protein 20 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);cartilage;developmental;parathyroid;skin;prostate;whole body;lung;larynx;thyroid;visual apparatus;testis;head and neck;brain;tonsil; . 0.15661 0.08115 0.086440867 60.47416844 87.63607 1.99939 ZNF22 0.126684327200881 0.780144123627998 0.0931715491711206 zinc finger protein 22 FUNCTION: Binds DNA through the consensus sequence 5'-CAATG-3'. May be involved in transcriptional regulation and may play a role in tooth formation (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: In the embryo, expressed in developing craniofacial structures including dental epithelium of maxillary molar tooth organs, tongue epithelium and muscle, and craniofacial bone osteoblasts. In the adult, expressed in mesoderm-derived tissues such as skeletal muscle, heart, kidney and liver. Intermediate expression in spleen, thymus and brain. Low levels in endoderm-derived tissues such as intestine and colon. {ECO:0000269|PubMed:14630903}.; smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;thyroid;germinal center;bladder;brain;heart;cartilage;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;bone;testis;spinal ganglion;pineal gland;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;bile duct;lung;cornea;mesenchyma;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;cerebellum; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.38184 0.10478 -0.05129383 49.75819769 233.95236 3.30568 ZNF23 8.37282562295769e-07 0.300169765370872 0.699829397346566 zinc finger protein 23 FUNCTION: May be involved in transcriptional regulation. May have a role in embryonic development.; . . unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;adrenal cortex;colon;parathyroid;retina;uterus;lung;adrenal gland;thyroid;placenta;hippocampus;liver;testis;germinal center;kidney;brain;bladder;mammary gland;pineal gland; prefrontal cortex;ciliary ganglion; 0.68863 0.09663 -0.400392389 26.85185185 48.63832 1.35988 ZNF24 0.995634782887564 0.00436483207698998 3.8503544648674e-07 zinc finger protein 24 FUNCTION: Transcription factor required for myelination of differentiated oligodendrocytes. Required for the conversion of oligodendrocytes from the premyelinating to the myelinating state. In the developing central nervous system (CNS), involved in the maintenance in the progenitor stage by promoting the cell cycle. Specifically binds to the 5'-TCAT-3' DNA sequence (By similarity). Has transcription repressor activity in vitro. {ECO:0000250, ECO:0000269|PubMed:10585455}.; . TISSUE SPECIFICITY: Expressed in many tissues except in heart.; ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;spinal cord;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;occipital lobe;medulla oblongata;testis - seminiferous tubule;prefrontal cortex;globus pallidus;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex;parietal lobe; 0.33909 0.12150 0.281220278 71.07808445 52.7185 1.43834 ZNF25 0.000386915993164412 0.843459796471515 0.15615328753532 zinc finger protein 25 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.24685 0.09277 -0.358119787 29.16371786 26.42311 0.85579 ZNF26 . . . zinc finger protein 26 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;bone marrow;retina;optic nerve;endometrium;thyroid;testis;pineal gland;brain;unclassifiable (Anatomical System);adrenal cortex;blood;lens;pancreas;lung;adrenal gland;placenta;macula lutea;liver;spleen;head and neck;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;medulla oblongata;globus pallidus;pons;caudate nucleus;trigeminal ganglion;skeletal muscle;parietal lobe; 0.10118 . . . . . ZNF28 1.97755682004291e-16 0.000518881831040114 0.99948111816896 zinc finger protein 28 FUNCTION: May be involved in transcriptional regulation.; . . myocardium;ovary;salivary gland;intestine;colon;skin;retina;uterus;prostate;whole body;endometrium;bone;brain;bladder;unclassifiable (Anatomical System);trophoblast;heart;hypothalamus;urinary;muscle;adrenal cortex;pharynx;blood;skeletal muscle;breast;pancreas;lung;visual apparatus;hippocampus;liver;spleen;cervix;kidney;stomach; . . . 2.046758368 97.76480302 2220.4199 8.67751 ZNF29P . . . zinc finger protein 29, pseudogene . . . . . . . . . . . ZNF30 8.05996775258386e-09 0.150609895473666 0.849390096466366 zinc finger protein 30 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lymph node;ovary;salivary gland;intestine;pharynx;colon;blood;skin;uterus;prostate;lung;cornea;placenta;visual apparatus;liver;testis;kidney;brain;mammary gland;aorta; superior cervical ganglion;atrioventricular node; 0.12760 0.09780 1.802352368 96.92734135 4241.52872 12.95251 ZNF30-AS1 . . . ZNF30 antisense RNA 1 . . . . . . . . . . . ZNF32 0.276205822566686 0.700396688134764 0.0233974892985499 zinc finger protein 32 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.35800 0.11262 -0.163345027 41.24793583 7.38478 0.27499 ZNF32-AS1 . . . ZNF32 antisense RNA 1 . . . . . . . . . . . ZNF32-AS2 . . . ZNF32 antisense RNA 2 . . . . . . . . . . . ZNF32-AS3 . . . ZNF32 antisense RNA 3 . . . . . . . . . . . ZNF33A 0.000466480342698693 0.96592506826277 0.0336084513945311 zinc finger protein 33A FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;choroid;fovea centralis;bone marrow;retina;uterus;prostate;whole body;optic nerve;endometrium;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach; . 0.09326 0.07384 0.183723206 66.24793583 1788.26704 7.80645 ZNF33B 2.25380897368934e-06 0.716021576861691 0.283976169329335 zinc finger protein 33B FUNCTION: May be involved in transcriptional regulation.; . . ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion; 0.21894 0.09041 -0.08446956 47.15145081 295.81661 3.67252 ZNF33BP1 . . . zinc finger protein 33B pseudogene 1 . . . . . . . . . . . ZNF33CP . . . zinc finger protein 33C, pseudogene . . . . . . . . . . . ZNF34 0.246110577926244 0.747345554351494 0.00654386772226198 zinc finger protein 34 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);prostate;lung;frontal lobe;bone;macula lutea;visual apparatus;testis;blood;fovea centralis;germinal center;brain;bone marrow; superior cervical ganglion;appendix;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15491 . -0.334253673 30.70299599 1115.38845 6.37919 ZNF35 0.0792906266095248 0.90983650803583 0.010872865354645 zinc finger protein 35 FUNCTION: May be involved in transcriptional regulation. Involved in cell differentiation and/or proliferation.; . . unclassifiable (Anatomical System);cartilage;spinal cord;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;bile duct;uterus;prostate;optic nerve;lung;endometrium;macula lutea;liver;germinal center;mammary gland;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.58587 0.09866 -0.492218069 22.35786742 3014.78441 10.42616 ZNF37A 0.00192441523384355 0.906226624786685 0.0918489599794719 zinc finger protein 37A FUNCTION: May be involved in transcriptional regulation.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;frontal lobe;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland; superior cervical ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.12669 0.09570 0.088260113 60.56853031 287.83652 3.63338 ZNF37BP . . . zinc finger protein 37B, pseudogene . . . . . . . . . . . ZNF37CP . . . zinc finger protein 37C, pseudogene . . . . . 0.15605 . . . . . ZNF41 0.00138968236818729 0.867005450071338 0.131604867560475 zinc finger protein 41 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Expressed in the heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:14628291}.; unclassifiable (Anatomical System);uterus;lymph node;lung;heart;placenta;visual apparatus;liver;testis;kidney;skeletal muscle; . 0.13295 0.12914 0.733063566 86.27034678 277.22996 3.56574 ZNF43 2.14784246985067e-08 0.254407834183218 0.745592144338358 zinc finger protein 43 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: T- and B-cell lines.; epididymis; dorsal root ganglion;superior cervical ganglion;testis - interstitial;trigeminal ganglion; 0.34703 0.07168 0.378498378 75.58386412 64.23103 1.64447 ZNF44 8.93827649124464e-07 0.754052949220225 0.245946156952126 zinc finger protein 44 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);cartilage;fovea centralis;skeletal muscle;uterus;lung;endometrium;placenta;bone;macula lutea;testis;brain;tonsil;peripheral nerve; dorsal root ganglion;superior cervical ganglion;testis - interstitial;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.47142 0.09434 0.644875971 84.10002359 1432.15616 7.06315 ZNF45 0.00010251198832844 0.987119809219252 0.0127776787924195 zinc finger protein 45 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;blood;skin;skeletal muscle;retina;uterus;lung;endometrium;bone;placenta;thyroid;germinal center;kidney;aorta; superior cervical ganglion;cingulate cortex; 0.21359 0.10869 0.446457185 77.97829677 4579.30846 13.58851 ZNF48 0.0324251458384005 0.958554879233039 0.00901997492856099 zinc finger protein 48 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);heart;ovary;salivary gland;pharynx;colon;blood;skin;breast;uterus;prostate;lung;endometrium;bone;visual apparatus;hippocampus;liver;cervix;kidney;brain;bladder; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19214 . -0.50880549 21.72682236 238.15263 3.33478 ZNF56 . . . zinc finger protein 56 . . . . . . . . . . . ZNF57 1.0043121865806e-06 0.541342978613294 0.45865601707452 zinc finger protein 57 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);uterus;lymph node;lung;testis;cervix;stomach; subthalamic nucleus;testis - interstitial;testis;trigeminal ganglion; 0.07872 . 1.447715105 95.14036329 1085.64755 6.31313 ZNF66 5.45295491875167e-17 0.000126026073344783 0.999873973926655 zinc finger protein 66 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . 0.06526 . . . 6422.74922 16.79601 ZNF69 7.35111939274279e-05 0.303763701653786 0.696162787152287 zinc finger protein 69 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);uterus;ovary;colon; . . . 0.25917371 70.05779665 27.23843 0.87720 ZNF70 0.168320381851445 0.817625155575299 0.014054462573256 zinc finger protein 70 FUNCTION: May be involved in transcriptional regulation.; . . breast;uterus;lung;endometrium;bone;liver;testis;ureter;spleen;brain;bone marrow; superior cervical ganglion;testis - interstitial;ciliary ganglion;skin; 0.16809 . -0.534490515 20.70063694 100.29992 2.17020 ZNF70P1 . . . zinc finger protein 70 pseudogene 1 . . . . . . . . . . . ZNF71 8.08795745626604e-06 0.511621003014969 0.488370909027574 zinc finger protein 71 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Highly expressed in placenta, followed by brain, testis, pancreas, heart, small intestine, muscle, uterus, prostate and peripheral blood leukocytes. Not detected in liver, lung, colon, stomach, salivary and thyroid gland.; unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;uterus;prostate;lung;epididymis;placenta;visual apparatus;liver;kidney;brain;bladder;peripheral nerve; superior cervical ganglion;subthalamic nucleus;medulla oblongata;globus pallidus;ciliary ganglion;atrioventricular node;kidney;skeletal muscle; 0.23405 . 0.132352165 63.48785091 405.54039 4.22328 ZNF72P . . . zinc finger protein 72, pseudogene . . . . . . . . . . . ZNF73 . . . zinc finger protein 73 FUNCTION: May be involved in transcriptional regulation.; . . . . . . . . . . ZNF74 0.00035587805447844 0.95182039507554 0.0478237268699819 zinc finger protein 74 FUNCTION: May play a role in RNA metabolism.; . TISSUE SPECIFICITY: Highly expressed in the fetal brain.; unclassifiable (Anatomical System);colon;blood;retina;prostate;optic nerve;lung;frontal lobe;larynx;bone;placenta;visual apparatus;head and neck;bladder;brain; dorsal root ganglion;superior cervical ganglion;atrioventricular node;parietal lobe;skeletal muscle; 0.17370 0.11493 -0.222203495 37.54423213 429.08523 4.32667 ZNF75A 0.0002034845611094 0.487927193154994 0.511869322283896 zinc finger protein 75a FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;skin;bone marrow;uterus;whole body;cochlea;bone;lymph;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;urinary;blood;pancreas;lung;placenta;hypopharynx;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;occipital lobe;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.12496 0.11076 -0.05129383 49.75819769 7.67214 0.28328 ZNF75BP . . . zinc finger protein 75B, pseudogene . . . . . . . . . . . ZNF75CP . . . zinc finger protein 75C, pseudogene FUNCTION: May be involved in transcriptional regulation.; . . . . . . . . . . ZNF75D 0.000185372038923542 0.70729676174758 0.292517866213497 zinc finger protein 75D FUNCTION: May be involved in transcriptional regulation.; . . . . 0.10208 . -0.093566408 46.7386176 12.54757 0.45738 ZNF76 5.07288621916122e-16 0.00645354583959637 0.993546454160403 zinc finger protein 76 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Testis.; colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;urinary;blood;lens;skeletal muscle;lung;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.26454 0.10496 0.404185162 76.48619958 1199.49311 6.56948 ZNF77 4.31245286065236e-13 0.0129141978213691 0.9870858021782 zinc finger protein 77 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;ovary;heart;larynx;hypothalamus;placenta;adrenal cortex;testis;parathyroid;blood;head and neck;kidney;spinal ganglion; superior cervical ganglion;globus pallidus; 0.18560 0.18198 1.537740199 95.57088936 321.29502 3.80700 ZNF79 0.0171294207080235 0.960225591584617 0.0226449877073591 zinc finger protein 79 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.34316 0.20051 0.134171522 63.57041755 46.29924 1.31066 ZNF80 5.32106862981897e-08 0.0665597204120841 0.93344022637723 zinc finger protein 80 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System); superior cervical ganglion;trigeminal ganglion;skeletal muscle; 0.08775 . 1.26221942 93.55980184 198.21452 3.04239 ZNF81 0.303589182435344 0.677567058331577 0.0188437592330789 zinc finger protein 81 FUNCTION: May be involved in transcriptional regulation.; DISEASE: Mental retardation, X-linked 45 (MRX45) [MIM:300498]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non- syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. {ECO:0000269|PubMed:15121780}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving ZNF81 is found in a severe mental retardation patient. Translocation t(X;9)(p11.23;q34.3). {ECO:0000269|PubMed:15121780}.; . ovary;kidney; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.16362 0.15804 1.572740636 95.70653456 306.63148 3.72613 ZNF83 3.82175283218836e-06 0.208128153865019 0.791868024382149 zinc finger protein 83 FUNCTION: May be involved in transcriptional regulation.; . . ovary;sympathetic chain;colon;skin;retina;uterus;prostate;whole body;cochlea;endometrium;thyroid;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;urinary;skeletal muscle;breast;pancreas;lung;adrenal gland;placenta;spleen;head and neck;kidney;mammary gland;stomach; globus pallidus;trigeminal ganglion; 0.66709 0.08021 1.243805243 93.41825902 3058.5257 10.51275 ZNF84 . . . zinc finger protein 84 FUNCTION: May be involved in transcriptional regulation.; . . ovary;fovea centralis;choroid;bone marrow;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;islets of Langerhans;lens;skeletal muscle;breast;lung;placenta;macula lutea;head and neck;kidney;stomach; superior cervical ganglion; 0.66912 0.11762 . . . . ZNF85 2.27830551125369e-10 0.037336750295101 0.962663249477068 zinc finger protein 85 FUNCTION: May be a transcriptional repressor. {ECO:0000269|PubMed:9839802}.; . TISSUE SPECIFICITY: Widely expressed, including in testis. {ECO:0000269|PubMed:2023909, ECO:0000269|PubMed:9839802}.; kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.16722 0.10724 2.577929865 98.74970512 348.08165 3.95350 ZNF90 1.22410273221888e-07 0.10681453976 0.893185337829727 zinc finger protein 90 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.09032 . 1.216305531 93.13517339 1454.45614 7.11427 ZNF90P1 . . . zinc finger protein 90 pseudogene 1 . . . . . . . . . . . ZNF90P2 . . . zinc finger protein 90 pseudogene 2 . . . . . . . . . . . ZNF90P3 . . . zinc finger protein 90 pseudogene 3 . . . . . . . . . . . ZNF91 9.91964825661981e-05 0.997122941285021 0.00277786223241259 zinc finger protein 91 FUNCTION: Transcription factor specifically required to repress SINE-VNTR-Alu (SVA) retrotransposons: recognizes and binds SVA sequences and represses their expression by recruiting a repressive complex containing TRIM28/KAP1 (PubMed:25274305). May also bind the promoter of the FCGR2B gene, leading to repress its expression; however, additional evidences are required to confirm this result in vivo (PubMed:11470777). {ECO:0000269|PubMed:25274305, ECO:0000305|PubMed:11470777}.; . . unclassifiable (Anatomical System);lung;thyroid;placenta;visual apparatus;testis; . 0.10535 . 2.142298932 97.96532201 2696.61337 9.77457 ZNF92 9.99259330998176e-08 0.176620877399268 0.823379022674799 zinc finger protein 92 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);cartilage;ovary;heart;salivary gland;intestine;pharynx;colon;blood;skin;prostate;lung;cornea;endometrium;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland;bladder;stomach; . 0.16530 0.09770 0.174625237 65.9648502 1743.34182 7.70710 ZNF92P1Y . . . zinc finger protein 92 pseudogene 1, Y-linked . . . . . . . . . . . ZNF92P2 . . . zinc finger protein 92 pseudogene 2 . . . . . . . . . . . ZNF92P3 . . . zinc finger protein 92 pseudogene 3 . . . . . . . . . . . ZNF93 0.00169182185612759 0.891982000169571 0.106326177974302 zinc finger protein 93 FUNCTION: Transcription factor specifically required to repress long interspersed nuclear element 1 (L1) retrotransposons: recognizes and binds L1 sequences and repress their expression by recruiting a repressive complex containing TRIM28/KAP1 (PubMed:25274305). Not able to repress expression of all subtypes of L1 elements. Binds to the 5' end of L1PA4, L1PA5 and L1PA6 subtypes, and some L1PA3 subtypes. Does not bind to L1PA7 or older subtypes nor at the most recently evolved L1PA2 and L1Hs. 50% of L1PA3 elements have lost the ZNF93-binding site, explaining why ZNF93 is not able to repress their expression (PubMed:25274305). {ECO:0000269|PubMed:25274305}.; . . lymph node;visual apparatus;liver;spleen; dorsal root ganglion;testis - interstitial;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.61662 . 1.041730357 91.28921916 1817.75574 7.86310 ZNF98 1.80227058167028e-06 0.251602046425625 0.748396151303793 zinc finger protein 98 FUNCTION: May be involved in transcriptional regulation.; . . . . . . . . 197.36335 3.03748 ZNF99 3.03739918530551e-09 0.162337151238011 0.83766284572459 zinc finger protein 99 FUNCTION: May be involved in transcriptional regulation.; . . . . . . . . 1840.35634 7.91225 ZNF100 7.10189425692909e-13 0.00900746916412161 0.990992530835168 zinc finger protein 100 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);liver;colon;brain;skeletal muscle; . 0.11585 . 1.354051915 94.39726351 445.32676 4.39272 ZNF101 5.76614320550034e-07 0.427511834663196 0.572487588722483 zinc finger protein 101 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Expressed in a variety of adult and fetal tissues. {ECO:0000269|PubMed:14727140}.; unclassifiable (Anatomical System);breast;bile duct;lymph node;thyroid;liver;colon;spleen;skeletal muscle; . 0.11010 0.09134 0.108486928 61.90728946 102.58025 2.18964 ZNF101P1 . . . zinc finger protein 101 pseudogene 1 . . . . . . . . . . . ZNF101P2 . . . zinc finger protein 101 pseudogene 2 . . . . . . . . . . . ZNF106 0.219458519047887 0.780541480911714 4.03996724558318e-11 zinc finger protein 106 . . . . . 0.28817 0.10531 -0.448371699 24.00920028 657.40284 5.14043 ZNF107 7.59375740639872e-17 0.000568738088755009 0.999431261911245 zinc finger protein 107 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Expressed in brain, heart, skeletal muscle, kidney and pancreas. Weakly expressed in aorta, liver and lung.; unclassifiable (Anatomical System);heart;ovary;lacrimal gland;parathyroid;lung;endometrium;placenta;bone;liver;testis;germinal center;mammary gland;brain; superior cervical ganglion;trigeminal ganglion; . . 0.158037129 64.85020052 284.42435 3.61089 ZNF112 0.154211257518811 0.845081564960059 0.000707177521129776 zinc finger protein 112 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.15840 0.08715 1.670043565 96.31398915 1802.24452 7.83199 ZNF114 1.07440174482829e-06 0.191457192864665 0.80854173273359 zinc finger protein 114 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);bone;thyroid;liver;colon;brain;skin; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.39258 . -0.201976964 38.98325077 31.26473 0.98590 ZNF114P1 . . . zinc finger protein 114 pseudogene 1 . . . . . . . . . . . ZNF117 0.00021360138840966 0.736456342081651 0.263330056529939 zinc finger protein 117 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;spinal cord;colon;skin;skeletal muscle;retina;uterus;prostate;optic nerve;lung;frontal lobe;endometrium;adrenal gland;placenta;liver;spleen;cervix;kidney;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.43584 0.08330 0.729426781 86.17008728 5466.62914 15.23427 ZNF121 0.72485940087732 0.272244535165761 0.00289606395691855 zinc finger protein 121 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);uterus;lymph node;ovary;thyroid;colon;head and neck;brain;stomach; . 0.12633 0.19996 -0.227663163 37.11370606 5.11172 0.18949 ZNF123P . . . zinc finger protein 123, pseudogene . . . . . . . . . . . ZNF124 1.29546905801823e-07 0.0585653765347235 0.941434493918371 zinc finger protein 124 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.08775 . -0.359940251 28.93371078 14.85452 0.53454 ZNF131 0.999460221505131 0.000539776139947838 2.35492103179023e-09 zinc finger protein 131 FUNCTION: Plays a role during development and organogenesis as well as in the function of the adult central nervous system (By similarity). May be involved in transcriptional regulation as a repressor of ESR1/ER-alpha signaling. {ECO:0000250, ECO:0000269|PubMed:18847501, ECO:0000269|PubMed:22467880}.; . TISSUE SPECIFICITY: Predominant expression is found in different brain areas such as the occipital and temporal lobe, the nucleus caudatus, hippocampus, and the cerebellum as well as in testis and thymus. {ECO:0000269|PubMed:12163020}.; lymphoreticular;colon;vein;skin;retina;uterus;whole body;frontal lobe;cochlea;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;tongue;adrenal cortex;pharynx;bile duct;breast;lung;nasopharynx;placenta;liver;head and neck;kidney;stomach; testis - interstitial;occipital lobe;superior cervical ganglion;medulla oblongata;testis - seminiferous tubule;adrenal cortex;testis;atrioventricular node;skeletal muscle;parietal lobe;cingulate cortex; 0.28126 0.10787 0.128714042 63.19886766 86.63819 1.98849 ZNF132 8.15053229528725e-13 0.00976614142782325 0.990233858571362 zinc finger protein 132 FUNCTION: May be involved in transcriptional regulation.; . . heart;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;lung;bone;macula lutea;liver;testis;spleen;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node; 0.13901 0.09728 -0.418800956 25.79028073 264.47876 3.48920 ZNF133 0.949610073341142 0.0503833979701837 6.52868867426719e-06 zinc finger protein 133 FUNCTION: May be involved in transcriptional regulation as a repressor.; . TISSUE SPECIFICITY: Seems ubiquitous. Seen in the heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; unclassifiable (Anatomical System);smooth muscle;cartilage;ovary;hypothalamus;colon;parathyroid;skin;skeletal muscle;retina;uterus;prostate;whole body;lung;endometrium;larynx;epididymis;bone;thyroid;placenta;visual apparatus;iris;testis;head and neck;germinal center;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.12137 0.10714 -0.044015879 50.44821892 599.08601 4.95444 ZNF134 0.00114550101606897 0.838671117579409 0.160183381404522 zinc finger protein 134 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.40667 . -0.312207497 32.05944798 395.28977 4.17771 ZNF135 3.86627866810006e-09 0.329198262774171 0.67080173335955 zinc finger protein 135 FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. May be involved in transcriptional regulation. {ECO:0000269|PubMed:21834987}.; . . unclassifiable (Anatomical System);heart;cartilage;colon;skin;skeletal muscle;uterus;lung;cochlea;larynx;bone;visual apparatus;liver;testis;head and neck;spleen;brain; trigeminal ganglion;parietal lobe;cerebellum; 0.19668 0.16042 1.159254003 92.6279783 122.26268 2.40751 ZNF136 1.49304930601206e-08 0.59402651341945 0.405973471650057 zinc finger protein 136 FUNCTION: May be involved in transcriptional regulation as a weak repressor when alone, or a potent one when fused with a heterologous protein containing a KRAB B-domain.; . TISSUE SPECIFICITY: Seems ubiquitous. Seen in the heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; unclassifiable (Anatomical System);lymph node;smooth muscle;heart;skin;uterus;prostate;endometrium;thyroid;bone;testis;cervix;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.18795 0.09487 -0.53631094 20.53550366 14.57083 0.52526 ZNF137P . . . zinc finger protein 137, pseudogene FUNCTION: May be involved in transcriptional regulation.; . . smooth muscle;testis;germinal center;skeletal muscle; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.19326 . . . . . ZNF138 2.22312670470713e-07 0.079768286423187 0.920231491264142 zinc finger protein 138 FUNCTION: May be involved in transcriptional regulation as a repressor.; . . unclassifiable (Anatomical System);uterus;prostate;cartilage;islets of Langerhans;alveolus;testis;kidney;brain;stomach; superior cervical ganglion;medulla oblongata;atrioventricular node;parietal lobe; 0.06787 . 0.685332364 85.09672092 117.43288 2.35602 ZNF140 0.00206505130454093 0.744122748147903 0.253812200547556 zinc finger protein 140 FUNCTION: May be involved in transcriptional regulation as a repressor.; . TISSUE SPECIFICITY: Seems ubiquitous. Seen in the heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.; lymphoreticular;myocardium;smooth muscle;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;whole body;optic nerve;endometrium;thyroid;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;lacrimal gland;islets of Langerhans;lens;skeletal muscle;bile duct;breast;lung;nasopharynx;trabecular meshwork;placenta;visual apparatus;macula lutea;liver;spleen;kidney;mammary gland;aorta; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.15441 0.10446 . . 364.93766 4.04214 ZNF141 0.161888983164538 0.82300848026628 0.0151025365691815 zinc finger protein 141 FUNCTION: May be involved in transcriptional regulation as a repressor. Plays a role in limb development. {ECO:0000269|PubMed:23160277}.; . TISSUE SPECIFICITY: Ubiquitously low expression.; unclassifiable (Anatomical System);lung;cartilage;ovary;liver; . 0.39436 0.16446 0.795569043 87.49115357 156.94519 2.73623 ZNF142 1.87523307695819e-15 0.31760899355141 0.682391006448588 zinc finger protein 142 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.16164 0.09765 -0.645006008 16.44845482 2476.65268 9.28089 ZNF143 0.0219669962784504 0.977355751112847 0.000677252608702427 zinc finger protein 143 FUNCTION: Transcriptional activator. Activates the gene for selenocysteine tRNA (tRNAsec). Binds to the SPH motif of small nuclear RNA (snRNA) gene promoters. Participates in efficient U6 RNA polymerase III transcription via its interaction with CHD8. {ECO:0000269|PubMed:17938208, ECO:0000269|PubMed:9776743}.; . TISSUE SPECIFICITY: Expressed in all tissues tested, with the strongest expression in ovary.; ovary;salivary gland;intestine;colon;parathyroid;skin;uterus;prostate;frontal lobe;thyroid;bone;pituitary gland;testis;brain;bladder;unclassifiable (Anatomical System);muscle;pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; testis - interstitial;trigeminal ganglion;skeletal muscle; 0.55567 0.21566 -0.179930907 40.35739561 200.58018 3.06212 ZNF146 0.811745908933633 0.18359444463417 0.00465964643219659 zinc finger protein 146 . . TISSUE SPECIFICITY: Liver, skeletal and heart muscle, mammary cells. Very low levels in brain, lung, placenta and kidney. Strongly overexpressed in many pancreas and colorectal cancers. Increased gene copy numbers are detected in 3 of 12 tumor cell lines and 2 of 12 primary pancreatic carcinomas. Overexpressed in 80% of colorectal cancers. {ECO:0000269|PubMed:8107129, ECO:0000269|PubMed:8665923}.; . . 0.80709 0.12273 0.257356108 69.83368719 2443.82057 9.19518 ZNF148 0.932274762499269 0.067711464977374 1.37725233574102e-05 zinc finger protein 148 FUNCTION: Involved in transcriptional regulation. Represses the transcription of a number of genes including gastrin, stromelysin and enolase. Binds to the G-rich box in the enhancer region of these genes.; . . ovary;salivary gland;developmental;colon;parathyroid;skin;retina;uterus;prostate;whole body;bone;pituitary gland;testis;amniotic fluid;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;skeletal muscle;bile duct;pancreas;lung;nasopharynx;placenta;visual apparatus;alveolus;liver;spleen;cervix;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;occipital lobe;medulla oblongata;atrioventricular node;pons;skeletal muscle;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe; . 0.26573 -0.53631094 20.53550366 10.4082 0.37841 ZNF154 5.18955297882032e-05 0.673319295091056 0.326628809379156 zinc finger protein 154 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.13076 . 0.819433854 87.98655343 864.22394 5.72989 ZNF155 1.33952561088838e-09 0.0546415231822037 0.945358475478271 zinc finger protein 155 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);brain;mammary gland; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10208 0.08867 0.400544645 76.40953055 649.16485 5.11151 ZNF157 8.04449374208541e-07 0.163687670767909 0.836311524782717 zinc finger protein 157 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.21787 0.10941 0.196671391 67.19155461 24.21653 0.79510 ZNF160 0.00192720928708932 0.993379376024397 0.00469341468851343 zinc finger protein 160 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11410164}.; unclassifiable (Anatomical System);placenta;spinal cord;brain; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.16895 0.10850 0.224175308 68.48903043 89.09268 2.02621 ZNF165 0.000563292029886091 0.894393177608213 0.105043530361901 zinc finger protein 165 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Expressed specifically in testis.; . . 0.25479 0.09206 0.016664174 55.21939137 325.38591 3.83483 ZNF169 1.74927627359584e-09 0.119677764139266 0.880322234111457 zinc finger protein 169 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Highly expressed in kidney, weakly expressed in heart, liver, spleen, and small intestine. Not expressed in adult brain or spinal cord.; unclassifiable (Anatomical System);ovary;liver;colon;spleen;bone marrow; dorsal root ganglion;superior cervical ganglion;pons;trigeminal ganglion; 0.15529 0.11628 0.622829232 83.47487615 2566.77794 9.46539 ZNF174 0.0530328588222394 0.926709514062947 0.0202576271148136 zinc finger protein 174 FUNCTION: Transcriptional repressor. {ECO:0000269|PubMed:7673192}.; . TISSUE SPECIFICITY: Expressed in a variety of organs, but most strongly in adult testis and ovary followed by small intestine, colon, prostate, thymus, spleen, pancreas, skeletal muscle, heart, brain and kidney. Also expressed in umbilical vein endothelial cells, foreskin fibroblast and Hep-G2 cells.; medulla oblongata;ovary;developmental;colon;fovea centralis;choroid;retina;uterus;prostate;optic nerve;whole body;bone;lymph;testis;brain;unclassifiable (Anatomical System);cartilage;tongue;islets of Langerhans;lens;pancreas;lung;macula lutea;liver;duodenum;spleen;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;medulla oblongata;atrioventricular node;pons;skeletal muscle;skin;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion;parietal lobe;cingulate cortex; 0.13178 0.13332 -0.690637458 15.12149092 29.91427 0.95452 ZNF175 0.000451569387912362 0.964464696291221 0.0350837343208667 zinc finger protein 175 FUNCTION: Down-regulates the expression of several chemokine receptors. Interferes with HIV-1 replication by suppressing Tat- induced viral LTR promoter activity. {ECO:0000269|PubMed:14688346}.; . TISSUE SPECIFICITY: Ubiquitous.; colon;parathyroid;skin;uterus;whole body;endometrium;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;islets of Langerhans;hypothalamus;skeletal muscle;breast;placenta;visual apparatus;liver;spleen;head and neck;kidney;stomach; superior cervical ganglion;trigeminal ganglion; 0.05748 0.08895 -0.020150552 52.25288983 1577.06941 7.34781 ZNF177 5.54015130310773e-06 0.434684277888567 0.56531018196013 zinc finger protein 177 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);prostate;lung;ovary;islets of Langerhans;placenta;parathyroid;kidney;brain;retina; superior cervical ganglion; 0.12197 0.08166 0.464864541 78.69190847 13.73699 0.49853 ZNF180 7.35726181171227e-06 0.730469459591296 0.269523183146892 zinc finger protein 180 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);heart;ovary;hypothalamus;parathyroid;retina;bone marrow;prostate;whole body;lung;endometrium;bone;placenta;liver;testis;germinal center;kidney;brain; superior cervical ganglion; 0.16058 . 1.157431179 92.60438783 5752.00612 15.73654 ZNF181 3.18285421882246e-08 0.173651545310774 0.826348422860684 zinc finger protein 181 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.06805 . 0.196671391 67.19155461 178.86688 2.90543 ZNF182 0.856542477213403 0.142982760833125 0.000474761953471954 zinc finger protein 182 FUNCTION: May be involved in transcriptional regulation.; . . epididymis; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; . . 0.062575634 58.74026893 54.19385 1.46906 ZNF184 0.133748635714874 0.865332287530292 0.000919076754834101 zinc finger protein 184 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Predominant expression in testis.; lymphoreticular;colon;choroid;fovea centralis;bone marrow;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;lens;pancreas;lung;placenta;macula lutea;kidney;stomach;aorta; dorsal root ganglion;amygdala;superior cervical ganglion;prefrontal cortex;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.21513 0.10412 -0.023789244 52.09365416 46.59463 1.31817 ZNF185 5.20951973750293e-10 0.208328099241077 0.791671900237971 zinc finger protein 185 (LIM domain) FUNCTION: May be involved in the regulation of cellular proliferation and/or differentiation.; . TISSUE SPECIFICITY: Expressed in placenta, pancreas and kidney. Also expressed in prostate, testis, ovary and blood.; ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;gum;thyroid;pituitary gland;testis;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland;aorta; tongue; 0.07387 . 0.110306132 62.00165133 1386.48286 6.97042 ZNF189 0.00461788519238261 0.964927864564377 0.0304542502432405 zinc finger protein 189 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;colon;parathyroid;skin;retina;bone marrow;uterus;frontal lobe;cochlea;cerebral cortex;endometrium;thyroid;pituitary gland;testis;germinal center;brain;artery;pineal gland;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;blood;pancreas;lung;adrenal gland;placenta;liver;cervix;kidney;stomach;aorta; amygdala;superior cervical ganglion;medulla oblongata;occipital lobe;temporal lobe;spinal cord;prefrontal cortex;testis;caudate nucleus;trigeminal ganglion;parietal lobe; 0.74958 0.11322 0.154398214 64.73814579 98.59808 2.14648 ZNF192P1 . . . zinc finger protein 192 pseudogene 1 . . . . . . . . . . . ZNF192P2 . . . zinc finger protein 192 pseudogene 2 . . . . . . . . . . . ZNF195 0.731668924641439 0.267775733800013 0.000555341558548042 zinc finger protein 195 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Expressed in adult heart, brain, placenta, skeletal muscle and pancreas, and in fetal lung, kidney and brain. There is little expression in adult lung, liver and kidney.; unclassifiable (Anatomical System);lymphoreticular;ovary;heart;islets of Langerhans;colon;skin;uterus;prostate;lung;endometrium;epididymis;nasopharynx;bone;thyroid;placenta;liver;testis;head and neck;kidney;brain;mammary gland;stomach; subthalamic nucleus;testis - interstitial;superior cervical ganglion;ciliary ganglion;trigeminal ganglion;cingulate cortex;skeletal muscle; 0.57583 0.09179 0.130533008 63.35810333 1570.95375 7.33456 ZNF197 5.95384346361306e-14 0.0285725794968986 0.971427420503042 zinc finger protein 197 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);cartilage;ovary;colon;skin;skeletal muscle;retina;breast;lung;larynx;placenta;bone;testis;head and neck;cervix;germinal center;brain;pineal gland; dorsal root ganglion;superior cervical ganglion;temporal lobe;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.27199 0.10007 -1.105907904 6.86482661 68.21007 1.70948 ZNF197-AS1 . . . ZNF197 antisense RNA 1 . . . . . . . . . . . ZNF200 2.25120499760497e-06 0.477094293951386 0.522903454843616 zinc finger protein 200 FUNCTION: Could have a role in spermatogenesis.; . TISSUE SPECIFICITY: Highly expressed in testis, weakly expressed in spleen, thymus, prostate, ovary, small intestine colon and peripheral blood leukocytes.; . . 0.12280 0.10482 0.108486928 61.90728946 480.51716 4.52161 ZNF202 0.138743297874791 0.860396820424647 0.000859881700561357 zinc finger protein 202 FUNCTION: Transcriptional repressor that binds to elements found predominantly in genes that participate in lipid metabolism. Among its targets are structural components of lipoprotein particles (apolipoproteins AIV, CIII, and E), enzymes involved in lipid processing (lipoprotein lipase, lecithin cholesteryl ester transferase), transporters involved in lipid homeostasis (ABCA1, ABCG1), and several genes involved in processes related to energy metabolism and vascular disease.; . TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in breast carcinoma cell lines.; unclassifiable (Anatomical System);cartilage;ovary;heart;colon;parathyroid;skeletal muscle;uterus;pancreas;prostate;lung;frontal lobe;endometrium;epididymis;duodenum;liver;testis;cervix;spleen;kidney;brain;stomach; superior cervical ganglion;testis - seminiferous tubule;testis;appendix;ciliary ganglion;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.14654 0.14930 -0.200157416 39.11299835 48.89763 1.36475 ZNF204P . . . zinc finger protein 204, pseudogene . . . . . 0.06129 . . . . . ZNF205 0.141235328324468 0.85468894314829 0.0040757285272421 zinc finger protein 205 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, pancreas and brain. Weakly expressed in placenta, lung, liver, kidney and thymus.; unclassifiable (Anatomical System);medulla oblongata;heart;ovary;colon;fovea centralis;choroid;lens;retina;breast;pancreas;prostate;optic nerve;macula lutea;visual apparatus;liver;spleen;cervix;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;skeletal muscle; 0.17522 0.10169 -0.709045403 14.673272 59.57319 1.56637 ZNF205-AS1 . . . ZNF205 antisense RNA 1 . . . . . . . . . . . ZNF207 0.0542638461497623 0.944894719368918 0.000841434481319244 zinc finger protein 207 FUNCTION: Kinetochore- and microtubule-binding protein that plays a key role in spindle assembly (PubMed:24462186, PubMed:24462187, PubMed:26388440). ZNF207/BuGZ is mainly composed of disordered low-complexity regions and undergoes phase transition or coacervation to form temperature-dependent liquid droplets. Coacervation promotes microtubule bundling and concentrates tubulin, promoting microtubule polymerization and assembly of spindle and spindle matrix by concentrating its building blocks (PubMed:26388440). Also acts as a regulator of mitotic chromosome alignment by mediating the stability and kinetochore loading of BUB3 (PubMed:24462186, PubMed:24462187). Mechanisms by which BUB3 is protected are unclear: according to a first report, ZNF207/BuGZ may act by blocking ubiquitination and proteasomal degradation of BUB3 (PubMed:24462186). According to another report, the stabilization is independent of the proteasome (PubMed:24462187). {ECO:0000269|PubMed:24462186, ECO:0000269|PubMed:24462187, ECO:0000269|PubMed:26388440}.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9799612}.; lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;amniotic fluid;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;skeletal muscle;breast;visual apparatus;alveolus;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;uterus;whole body;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;mesenchyma;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach; superior cervical ganglion;testis - interstitial;testis;atrioventricular node;trigeminal ganglion; 0.55618 0.11352 -0.181750739 40.15687662 380.34086 4.11140 ZNF208 5.00161251193924e-20 0.000388075230720708 0.999611924769279 zinc finger protein 208 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Ubiquitous.; . . 0.13944 . 3.723439031 99.57537155 3724.25941 11.92681 ZNF209P . . . zinc finger protein 209, pseudogene . . . . . . . . . . . ZNF211 3.03205891351883e-08 0.169132006375192 0.830867963304219 zinc finger protein 211 FUNCTION: May be involved in transcriptional regulation.; . . lymphoreticular;unclassifiable (Anatomical System);heart;islets of Langerhans;colon;blood;skin;bone marrow;lung;frontal lobe;cochlea;endometrium;bone;thyroid;hippocampus;liver;testis;spleen;germinal center;kidney;brain;aorta;stomach; superior cervical ganglion; 0.21967 0.09467 0.178263593 66.12998349 2364.40509 9.02336 ZNF212 1.88610484725312e-06 0.44158848233733 0.558409631557823 zinc finger protein 212 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;cochlea;endometrium;thyroid;bone;testis;brain;bladder;pineal gland;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;mammary gland;stomach; dorsal root ganglion;testis;ciliary ganglion;kidney;trigeminal ganglion;skeletal muscle; 0.61098 0.11179 0.292133603 71.59707478 877.38247 5.76743 ZNF213 0.000112000376515533 0.823263669393933 0.176624330229552 zinc finger protein 213 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Widely expressed with highest levels in testis. {ECO:0000269|PubMed:10023065}.; . . 0.39907 0.10544 -0.556537043 19.72753008 20.61697 0.70119 ZNF213-AS1 . . . ZNF213 antisense RNA 1 (head to head) . . . . . . . . . . . ZNF214 2.49756188348063e-14 0.00241916667073075 0.997580833329244 zinc finger protein 214 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);uterus;heart;bone;colon;brain;skin;skeletal muscle; subthalamic nucleus;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion; 0.16692 0.09243 2.087222794 97.84736966 1128.261 6.40823 ZNF215 4.25305953478021e-13 0.0245627172361926 0.975437282763382 zinc finger protein 215 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);prostate;lung;bone;visual apparatus;liver;testis;colon;germinal center;skin;skeletal muscle;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.03570 0.07250 0.801024817 87.65628686 474.6148 4.50215 ZNF217 0.995447743940774 0.0045521697285262 8.6330700294113e-08 zinc finger protein 217 FUNCTION: Binds to the promoters of target genes and functions as repressor. Promotes cell proliferation and antagonizes cell death. Promotes phosphorylation of AKT1 at 'Ser-473'. {ECO:0000269|PubMed:16203743, ECO:0000269|PubMed:16940172, ECO:0000269|PubMed:17259635, ECO:0000269|PubMed:18625718}.; . . unclassifiable (Anatomical System);breast;placenta;testis;colon;bone marrow; testis - seminiferous tubule;placenta;whole blood;skin; 0.47480 0.20496 -0.253570113 34.99056381 665.33674 5.16370 ZNF219 0.988717808247592 0.0112782645915416 3.92716086604669e-06 zinc finger protein 219 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Ubiquitous.; ovary;salivary gland;sympathetic chain;intestine;colon;substantia nigra;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cerebral cortex;endometrium;bone;testis;brain;bladder;unclassifiable (Anatomical System);cartilage;islets of Langerhans;hypothalamus;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;cornea;placenta;macula lutea;visual apparatus;hippocampus;liver;duodenum;spleen;kidney;mammary gland;stomach;thymus; dorsal root ganglion;globus pallidus;atrioventricular node;pons; 0.31190 0.09464 . . 2700.67529 9.78301 ZNF221 2.58051484113414e-09 0.268745080088138 0.731254917331347 zinc finger protein 221 FUNCTION: May be involved in transcriptional regulation.; . . stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;medulla oblongata;pons;trigeminal ganglion;skeletal muscle; 0.08140 0.07647 2.691876739 98.88535032 585.33474 4.90607 ZNF222 9.20501288480146e-11 0.0220264673903507 0.977973532517599 zinc finger protein 222 FUNCTION: May be involved in transcriptional regulation.; . . lymphoreticular;unclassifiable (Anatomical System);heart;islets of Langerhans;colon;blood;skin;uterus;prostate;pancreas;whole body;lung;cornea;endometrium;larynx;thyroid;placenta;bone;testis;head and neck;germinal center;kidney;brain; testis - interstitial;globus pallidus;skeletal muscle; 0.07341 0.07796 1.908972967 97.39325313 2416.84735 9.13472 ZNF223 5.14224553323192e-09 0.117392853239566 0.882607141618189 zinc finger protein 223 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.09704 . 0.597144447 82.7435716 193.47379 3.01741 ZNF224 2.0744645910844e-09 0.240059906052479 0.759940091873057 zinc finger protein 224 FUNCTION: May be involved in transcriptional regulation as a transcriptional repressor. The DEPDC1A-ZNF224 complex may play a critical role in bladder carcinogenesis by repressing the transcription of the A20 gene, leading to transport of NF-KB protein into the nucleus, resulting in suppression of apoptosis of bladder cancer cells. {ECO:0000269|PubMed:20587513}.; . TISSUE SPECIFICITY: Ubiquitous. Mainly expressed in fetal tissues. {ECO:0000269|PubMed:12239212}.; unclassifiable (Anatomical System);heart;hypothalamus;colon;skeletal muscle;retina;breast;prostate;pancreas;adrenal gland;thyroid;bone;visual apparatus;alveolus;liver;testis;germinal center;kidney;brain;stomach; superior cervical ganglion;testis - seminiferous tubule;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.16282 0.11713 0.404185162 76.48619958 580.4741 4.88482 ZNF225 3.36669333303033e-08 0.319398819684512 0.680601146648554 zinc finger protein 225 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);pituitary gland;colon;blood;germinal center;skeletal muscle;peripheral nerve; dorsal root ganglion;testis - interstitial;superior cervical ganglion;medulla oblongata;pons;trigeminal ganglion;skeletal muscle; 0.22792 . 0.979225112 90.42816702 847.3688 5.69184 ZNF226 5.26919185197287e-15 0.00690474315380955 0.993095256846185 zinc finger protein 226 FUNCTION: May be involved in transcriptional regulation.; . . colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;testis;artery;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;breast;pancreas;lung;trabecular meshwork;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;subthalamic nucleus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11163 . -0.416983034 25.82566643 402.89553 4.21038 ZNF227 1.69159989152872e-05 0.967281437009396 0.0327016469916886 zinc finger protein 227 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);heart;colon;parathyroid;skin;skeletal muscle;uterus;breast;pancreas;lung;frontal lobe;endometrium;bone;placenta;duodenum;testis;germinal center;brain;pineal gland; superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.32458 0.10160 -0.997481928 8.47487615 230.82337 3.28482 ZNF229 6.30663414582273e-09 0.239947644013151 0.760052349680215 zinc finger protein 229 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);breast; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13556 . 1.252926935 93.48313281 3161.67135 10.71478 ZNF230 0.00834108463646319 0.932419393266148 0.0592395220973887 zinc finger protein 230 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.09002 0.09033 1.596607091 95.87166785 572.16407 4.85620 ZNF232 0.000435397717293909 0.860986716264972 0.138577886017734 zinc finger protein 232 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Ubiquitous. Higher expression seen in the liver, testis and ovary.; colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;brain;unclassifiable (Anatomical System);lymph node;cartilage;urinary;lens;breast;pancreas;lung;placenta;visual apparatus;macula lutea;head and neck;kidney;stomach; testis - interstitial;testis;cerebellum; 0.11687 0.09069 -0.359940251 28.93371078 93.05646 2.07320 ZNF233 3.27015906549736e-17 0.00034615849273236 0.999653841507268 zinc finger protein 233 FUNCTION: May be involved in transcriptional regulation.; . . uterus;heart;internal ear;testis;kidney;brain;mammary gland;skin; testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion; 0.09894 . 0.97558591 90.37508846 4670.83871 13.76453 ZNF234 1.07736675935267e-13 0.0109956412794605 0.989004358720432 zinc finger protein 234 FUNCTION: May be involved in transcriptional regulation.; . . colon;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;larynx;thyroid;testis;artery;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;breast;pancreas;lung;trabecular meshwork;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach;aorta; superior cervical ganglion;subthalamic nucleus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.05444 . 0.246221394 69.56829441 2198.83866 8.63352 ZNF235 1.85820362433789e-10 0.118574347771502 0.881425652042677 zinc finger protein 235 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lymph node;ovary;salivary gland;intestine;colon;pharynx;blood;uterus;prostate;lung;visual apparatus;liver;pituitary gland;spleen;kidney;brain;bladder;mammary gland; superior cervical ganglion;testis;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.15544 0.08860 0.290313621 71.56758669 402.26032 4.20803 ZNF236 0.999998363501894 1.63649810570697e-06 5.86075853886388e-19 zinc finger protein 236 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Ubiquitous. Expression levels are highest in skeletal muscle and brain, intermediate in heart, pancreas, and placenta, and lowest in kidney, liver, and lung.; unclassifiable (Anatomical System);heart;ovary;skin;skeletal muscle;breast;uterus;pancreas;prostate;lung;endometrium;thyroid;placenta;liver;testis;spleen;germinal center;kidney;brain;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.17316 0.10239 -1.532514394 3.349846662 617.34905 5.01532 ZNF239 0.000867929253552217 0.791757254191941 0.207374816554507 zinc finger protein 239 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;uterus;pancreas;lung;duodenum;liver;spleen;cervix;kidney;brain;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.11058 0.08103 -0.091746757 46.91554612 42.20096 1.22797 ZNF248 0.685698353455718 0.313407345883212 0.000894300661070427 zinc finger protein 248 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);islets of Langerhans;developmental;colon;skeletal muscle;skin;retina;uterus;endometrium;adrenal gland;placenta;bone;brain;stomach; dorsal root ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node; 0.18182 0.09472 -0.312207497 32.05944798 41.57421 1.21239 ZNF250 0.0676198881241094 0.918399149249566 0.0139809626263249 zinc finger protein 250 FUNCTION: May be involved in transcriptional regulation.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;breast;lung;placenta;macula lutea;liver;spleen;kidney;stomach;cerebellum; superior cervical ganglion;atrioventricular node; 0.11843 0.09422 -0.758599262 13.32861524 67.28585 1.69765 ZNF251 3.06038920043107e-06 0.776794779652599 0.223202159958201 zinc finger protein 251 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;spinal cord;adrenal cortex;parathyroid;blood;skeletal muscle;retina;lung;adrenal gland;placenta;thyroid;liver;testis;spleen;kidney;brain;mammary gland;pineal gland; superior cervical ganglion;ciliary ganglion; 0.06873 . -0.510624372 21.65015334 82.4269 1.92785 ZNF252P . . . zinc finger protein 252, pseudogene . . . . . 0.05056 . . . . . ZNF252P-AS1 . . . ZNF252P antisense RNA 1 . . . . . . . . . . . ZNF253 1.33295852799606e-06 0.376534353252399 0.623464313789074 zinc finger protein 253 FUNCTION: May function as a transcription factor. Seem to have a transcriptional repression activity.; . TISSUE SPECIFICITY: Expressed in bone marrow and in monocytic and immature erythroid cell lines.; . . 0.09032 0.08992 -0.358119787 29.16371786 30.15097 0.96145 ZNF254 9.14795443372819e-27 5.71239847046846e-07 0.999999428760153 zinc finger protein 254 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);bone;thyroid;mammary gland;skeletal muscle; . 0.18622 0.07460 0.560331224 81.70559094 1143.56 6.44823 ZNF256 1.77459004146427e-05 0.681850425446757 0.318131828652828 zinc finger protein 256 FUNCTION: Transcriptional repressor that plays a role in cell proliferation. Requires TRIM28 for its activity. {ECO:0000269|PubMed:18060868}.; . . unclassifiable (Anatomical System);lung;mesenchyma;placenta;visual apparatus;brain;skin;skeletal muscle;stomach; superior cervical ganglion;trigeminal ganglion; 0.12084 0.09131 7.61E-05 53.98089172 73.61795 1.79323 ZNF257 1.12139154354786e-09 0.0932113894178517 0.906788609460757 zinc finger protein 257 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.27729 . 1.420201535 94.92215145 219.75935 3.20699 ZNF259P1 . . . zinc finger protein 259 pseudogene 1 . . . . . . . . . . . ZNF260 3.06605450053892e-06 0.18495744685987 0.81503948708563 zinc finger protein 260 FUNCTION: Transcription factor that acts as a cardiac regulator and an effector of alpha1-adrenergic signaling. Binds to PE response elements (PERE) present in the promoter of genes such as ANF/NPPA and acts as a direct transcriptional activator of NPPA. Also acts as a cofactor with GATA4, a key cardiac regulator (By similarity). {ECO:0000250}.; . . . . 0.26208 0.10158 -0.359940251 28.93371078 43.74865 1.25902 ZNF263 0.00818051568357078 0.988940941383525 0.00287854293290449 zinc finger protein 263 FUNCTION: Might play an important role in basic cellular processes as a transcriptional repressor.; . TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocyte.; lymphoreticular;ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;endometrium;bone;thyroid;lymph;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);cartilage;heart;muscle;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;kidney;mammary gland;stomach;peripheral nerve;thymus; dorsal root ganglion;medulla oblongata;superior cervical ganglion;globus pallidus;pons;trigeminal ganglion;skeletal muscle;cerebellum; 0.49629 0.11989 -0.466531444 23.51380042 69.14472 1.72300 ZNF264 7.10064544025699e-06 0.723200341341971 0.276792558012589 zinc finger protein 264 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Relatively highly expressed in kidney, thymus, testis, ovary, brain, lung, placenta, and prostate, and relatively low expression in heart, liver, skeletal muscle, pancreas, spleen, and small intestine.; unclassifiable (Anatomical System);ovary;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;retina;prostate;lung;cornea;bone;visual apparatus;liver;testis;germinal center;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.10419 0.10097 0.156217551 64.82071243 56.72535 1.51477 ZNF266 1.25383025237533e-09 0.0992773692278452 0.900722629518325 zinc finger protein 266 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;thyroid;testis;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;adrenal cortex;blood;lens;skeletal muscle;bile duct;breast;lung;placenta;macula lutea;liver;spleen;stomach;aorta;peripheral nerve; superior cervical ganglion;testis;atrioventricular node;skeletal muscle; 0.12765 . -0.354480518 29.42911064 190.00181 2.99080 ZNF267 1.49136799306776e-06 0.844568721490329 0.155429787141678 zinc finger protein 267 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lymph node;cartilage;colon;bone marrow;uterus;pancreas;prostate;whole body;atrium;bone;testis;germinal center;brain; . 0.46664 0.09008 1.087645262 91.8494928 53.65516 1.45910 ZNF268 1.61651265255367e-09 0.114511824640623 0.885488173742864 zinc finger protein 268 FUNCTION: Isoform 1: Acts as a transcriptional repressor. Inhibits erythroid differentiation and tumor cell proliferation. Plays a role during ovarian cancer development and progression.; . TISSUE SPECIFICITY: Overexpressed in ovarian cancer tissues compared to normal ovarian tissues. Isoform 1 and isoform 2 are expressed in squamous epithelium tissues. Isoform 2 is overexpressed in squamous cervical cancer (at protein level). Expressed in blood cells. Isoform 1 is expressed in pancreas, lung, skeletal muscle, heart, placenta, liver, kidney and brain. Isoform 2 expressed in chronic lymphocytic leukemia (CLL) and several tumor cell lines. Isoform 3 is expressed in several tumor cells. Isoform 5 is expressed in fetal liver and several tumor cells. Isoform 6 is weakly expressed in brain, lung amd small intestin and in several tumor cells. Isoform 7 is expressed in fetal liver and several tumor cells. {ECO:0000269|PubMed:12200376, ECO:0000269|PubMed:16735226, ECO:0000269|PubMed:16865230, ECO:0000269|PubMed:18949428, ECO:0000269|PubMed:23091055, ECO:0000269|PubMed:23946776}.; unclassifiable (Anatomical System);placenta;brain;stomach; testis;ciliary ganglion;skeletal muscle; 0.15605 . 1.377921151 94.56829441 2033.53885 8.30276 ZNF271P . . . zinc finger protein 271, pseudogene . . . . . 0.07802 . . . . . ZNF273 8.54685134114473e-06 0.523308052027229 0.47668340112143 zinc finger protein 273 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.55315 0.09195 0.531004228 80.87992451 2901.5899 10.20879 ZNF274 0.00724982193908302 0.989323323385555 0.00342685467536184 zinc finger protein 274 FUNCTION: Probable transcription repressor. Specifically binds to the 3'-end of zinc-finger coding genes and recruiting chromatin- modifying proteins such as SETDB1 and TRIM28/KAP1, leading to transcription repression. {ECO:0000269|PubMed:10777669}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;prostate;optic nerve;whole body;thyroid;bone;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;breast;lung;epididymis;placenta;macula lutea;hippocampus;liver;spleen;kidney;mammary gland;thymus; testis;atrioventricular node; 0.07608 0.10595 . . 267.26814 3.50559 ZNF275 0.0566089965908238 0.866082100006419 0.0773089034027574 zinc finger protein 275 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.17358 . . . 11.78785 0.42689 ZNF276 0.000257274838666869 0.983062059761028 0.0166806654003055 zinc finger protein 276 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cerebral cortex;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;breast;pancreas;lung;epididymis;placenta;macula lutea;liver;spleen;kidney;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion; 0.12585 0.17533 -0.08265057 47.20452937 218.97245 3.19863 ZNF277 4.86865721154542e-14 0.0132541292150064 0.986745870784945 zinc finger protein 277 FUNCTION: May be involved in transcriptional regulation.; . . ovary;salivary gland;intestine;colon;parathyroid;vein;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;pancreas;lung;trabecular meshwork;placenta;visual apparatus;liver;cervix;kidney;mammary gland;stomach; testis - interstitial;tumor; 0.12213 0.10459 -0.003562597 53.72729417 373.97205 4.07947 ZNF280A 1.33609532462502e-08 0.0570328850597325 0.942967101579314 zinc finger protein 280A FUNCTION: May function as a transcription factor.; . . unclassifiable (Anatomical System);lens;skin; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.07891 0.07712 1.379742765 94.60368011 7349.81456 18.44166 ZNF280B 0.283015680343504 0.694826132453745 0.0221581872027509 zinc finger protein 280B FUNCTION: May function as a transcription factor.; . . unclassifiable (Anatomical System);heart;colon;parathyroid;skin;uterus;whole body;lung;hippocampus;liver;testis;spleen;brain; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.10579 0.06776 0.130533008 63.35810333 72.31659 1.77181 ZNF280C 0.992273041974971 0.00772664336364431 3.14661384588778e-07 zinc finger protein 280C FUNCTION: May function as a transcription factor.; . . unclassifiable (Anatomical System);adrenal cortex;skeletal muscle;skin;uterus;lung;endometrium;testis;germinal center;kidney;brain;pineal gland;aorta;stomach; superior cervical ganglion;ciliary ganglion; 0.14240 . -0.492218069 22.35786742 14.15249 0.51250 ZNF280D 0.820128047448904 0.179871652756571 2.99794525624699e-07 zinc finger protein 280D FUNCTION: May function as a transcription factor.; . . colon;parathyroid;skin;retina;bone marrow;uterus;whole body;frontal lobe;cochlea;thyroid;testis;germinal center;brain;artery;pineal gland;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;adrenal cortex;skeletal muscle;pancreas;lung;adrenal gland;placenta;visual apparatus;hippocampus;alveolus;liver;spleen;head and neck;kidney;stomach;aorta;thymus; subthalamic nucleus;fetal brain; 0.42701 . -0.773369631 13.10450578 110.48862 2.28818 ZNF281 0.951671589857101 0.0482993902935962 2.9019849302867e-05 zinc finger protein 281 FUNCTION: Transcription repressor that plays a role in regulation of embryonic stem cells (ESCs) differentiation. Required for ESCs differentiation and acts by mediating autorepression of NANOG in ESCs: binds to the NANOG promoter and promotes association of NANOG protein to its own promoter and recruits the NuRD complex, which deacetylates histones. Not required for establishement and maintenance of ESCs (By similarity). Represses the transcription of a number of genes including GAST, ODC1 and VIM. Binds to the G- rich box in the enhancer region of these genes. {ECO:0000250, ECO:0000269|PubMed:10448078, ECO:0000269|PubMed:12771217}.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;cochlea;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;macula lutea;visual apparatus;duodenum;liver;cervix;head and neck;kidney;mammary gland;stomach;aorta; testis - interstitial;atrioventricular node;parietal lobe;skeletal muscle; 0.94229 0.26731 -0.400392389 26.85185185 55.86461 1.50094 ZNF282 0.277662873290001 0.72131570729416 0.00102141941583895 zinc finger protein 282 FUNCTION: Binds to the U5 repressive element (U5RE) of the human T cell leukemia virus type I long terminal repeat. It recognizes the 5'-TCCACCCC-3' sequence as a core motif and exerts a strong repressive effect on HTLV-I LTR-mediated expression.; . TISSUE SPECIFICITY: Ubiquitous.; smooth muscle;ovary;salivary gland;colon;parathyroid;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;brain;tonsil;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;skeletal muscle;pancreas;lung;placenta;visual apparatus;hippocampus;liver;amnion;spleen;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;heart;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cingulate cortex;skeletal muscle;cerebellum; 0.57954 0.10783 -0.291981272 33.20358575 591.35281 4.92881 ZNF283 4.46246793803596e-08 0.208239758003179 0.791760197372141 zinc finger protein 283 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Detected in prostate, testis, and pancreas. {ECO:0000269|PubMed:12743021}.; breast;prostate;whole body;thyroid;liver;spleen;germinal center;brain;bone marrow; dorsal root ganglion;testis - interstitial;medulla oblongata;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;caudate nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14731 . 0.532823122 80.96249115 4989.97941 14.42520 ZNF284 7.90018316515337e-09 0.148961212005475 0.851038780094342 zinc finger protein 284 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Expressed in lung, liver, pancreas and thymus. Lower expression in heart, placenta, spleen, prostate, ovary, small intestine and colon. No expression seen in brain, skeletal muscle, kidney, testis and peripheral blood leukocyte. {ECO:0000269|PubMed:12743021, ECO:0000269|PubMed:16817023}.; . . 0.09785 . 0.066214104 58.95848077 3554.13314 11.52706 ZNF285 0.00240305532090865 0.927033342244924 0.0705636024341675 zinc finger protein 285 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;skin;uterus;prostate;whole body;frontal lobe;endometrium;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;lens;skeletal muscle;pancreas;lung;internal ear;placenta;visual apparatus;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;pons;trigeminal ganglion; . . 1.910792163 97.4168436 4054.48418 12.62347 ZNF285B . . . zinc finger protein 285B (pseudogene) . . . . . . . . . . . ZNF286A 0.0129106053351946 0.953667115356423 0.0334222793083827 zinc finger protein 286A FUNCTION: May be involved in transcriptional regulation.; . . . . 0.25215 . 0.330767508 73.53739089 237.10663 3.32522 ZNF286B 0.00374602908975049 0.847909164551277 0.148344806358973 zinc finger protein 286B FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . 6652.48026 17.27843 ZNF287 0.608657330838459 0.391268073379385 7.45957821561283e-05 zinc finger protein 287 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.25668 0.09112 -0.358119787 29.16371786 127.15089 2.46001 ZNF292 0.999976984136083 2.30158639161706e-05 3.66919653072178e-16 zinc finger protein 292 FUNCTION: May be involved in transcriptional regulation.; . . lymphoreticular;ovary;colon;parathyroid;skin;bone marrow;uterus;whole body;frontal lobe;endometrium;pituitary gland;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;hypothalamus;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;occipital lobe;subthalamic nucleus;prefrontal cortex;globus pallidus;ciliary ganglion;pons;atrioventricular node;skeletal muscle;skin; 0.92237 0.15135 -1.148614861 6.292757726 669.17929 5.17319 ZNF295-AS1 . . . ZNF295 antisense RNA 1 . . . . . . . . . . . ZNF296 0.97328866403764 0.0266786249217683 3.27110405912514e-05 zinc finger protein 296 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);uterus;lymphoreticular;prostate;lung;ovary;islets of Langerhans;testis;colon;kidney;mammary gland;retina; . 0.24469 0.11056 -0.510624372 21.65015334 68.80409 1.71838 ZNF299P . . . zinc finger protein 299, pseudogene . . . . . . . . . . . ZNF300 0.000952650554439373 0.942871217430363 0.0561761320151975 zinc finger protein 300 FUNCTION: Has a transcriptional repressor activity. {ECO:0000269|PubMed:14746915}.; . TISSUE SPECIFICITY: Expressed mostly in heart, skeletal muscle and brain. Isoform 1 and isoform 2 are highly expressed in testis. {ECO:0000269|PubMed:14746915, ECO:0000269|PubMed:17541838}.; unclassifiable (Anatomical System);uterus;prostate;heart;urinary;brain;skin;skeletal muscle;stomach;retina; dorsal root ganglion;superior cervical ganglion;fetal brain;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.25884 . -0.490397599 22.50530786 504.37949 4.60928 ZNF300P1 . . . zinc finger protein 300 pseudogene 1 . . . unclassifiable (Anatomical System);heart;ovary;muscle;colon;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;optic nerve;lung;placenta;macula lutea;duodenum;pituitary gland;germinal center;kidney;stomach; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; . . . . . . ZNF302 0.00707195558979917 0.920216971742849 0.0727110726673521 zinc finger protein 302 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.24558 0.08842 0.953537969 90.08610521 2748.70087 9.88345 ZNF304 0.852650320351142 0.146839792245327 0.000509887403531226 zinc finger protein 304 FUNCTION: May be involved in transcriptional regulation.; . . breast;stomach; . 0.14124 0.09886 0.909442382 89.49634348 249.13707 3.40133 ZNF311 0.000129446471411909 0.990650007899158 0.0092205456294303 zinc finger protein 311 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.07449 . 0.64123826 83.97617363 272.14005 3.53506 ZNF316 . . . zinc finger protein 316 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . . . ZNF317 0.0157065703255095 0.978855095268964 0.00543833440552648 zinc finger protein 317 FUNCTION: May function as a transcription factor. May play an important role in erythroid maturation and lymphoid proliferation.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are ubiquitously expressed. Isoform 3 and isoform 4 are expressed only in lymphocytes, spleen and lung. {ECO:0000269|PubMed:11688974}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;lacrimal gland;tongue;muscle;pharynx;blood;lens;breast;pancreas;lung;cornea;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17060 0.10555 -0.93133804 9.613116301 66.99245 1.69240 ZNF317P1 . . . zinc finger protein 317 pseudogene 1 . . . . . . . . . . . ZNF318 0.0537829671346281 0.946217030462222 2.40314969068073e-09 zinc finger protein 318 FUNCTION: Repressed AR-mediated transcriptional activation. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division (By similarity). {ECO:0000250}.; . TISSUE SPECIFICITY: Expressed in endocrine tissue. {ECO:0000269|Ref.1}.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;larynx;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;lung;cornea;nasopharynx;placenta;macula lutea;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;aorta;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.54441 0.08891 -1.688698506 2.618542109 796.19334 5.56125 ZNF319 0.959545481290559 0.0403629867883121 9.15319211289184e-05 zinc finger protein 319 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lymph node;heart;tongue;colon;blood;bone marrow;whole body;lung;nasopharynx;thyroid;pituitary gland;liver;testis;cervix;head and neck;kidney;spinal ganglion;brain; dorsal root ganglion;superior cervical ganglion; 0.70240 . -0.754958418 13.57631517 80.99113 1.90368 ZNF320 0.0184496584196158 0.961147618061475 0.020402723518909 zinc finger protein 320 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Expressed at high levels in placenta, pancreas, kidney and heart, and at lower levels in liver, skeletal muscle and brain. {ECO:0000269|PubMed:11536051}.; . . 0.12591 0.09845 -0.291981272 33.20358575 51.19238 1.41059 ZNF321P 0.184601492428433 0.763853786214366 0.0515447213572015 zinc finger protein 321, pseudogene . . . . . . . . . 43.02154 1.24450 ZNF322 . . . zinc finger protein 322 FUNCTION: Involved in transcriptional regulation as an activator. {ECO:0000269|PubMed:15555580}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart and skeletal muscle. {ECO:0000269|PubMed:15555580}.; . . 0.32784 0.10027 . . 442.42965 4.37870 ZNF322P1 . . . zinc finger protein 322 pseudogene 1 FUNCTION: Involved in transcriptional regulation as an activator. {ECO:0000269|PubMed:15555580}.; . TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart and skeletal muscle. {ECO:0000269|PubMed:15555580}.; . . 0.16029 . . . . . ZNF324 0.473925409395351 0.524994025981258 0.00108056462339157 zinc finger protein 324 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);cartilage;ovary;islets of Langerhans;muscle;colon;parathyroid;skin;skeletal muscle;retina;prostate;lung;synovium;bone;placenta;visual apparatus;liver;testis;germinal center;kidney;brain;stomach;thymus; superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.15920 . -0.286522835 33.47487615 64.46671 1.64706 ZNF324B 0.00574789788111746 0.971633014708531 0.0226190874103517 zinc finger protein 324B FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);colon;blood;retina;prostate;optic nerve;lung;frontal lobe;larynx;placenta;bone;visual apparatus;head and neck;cervix;bladder;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; . . -0.710864321 14.5730125 88.06775 2.00784 ZNF326 0.977917716799787 0.0220821133866179 1.69813594655328e-07 zinc finger protein 326 FUNCTION: Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. May play a role in neuronal differentiation and is able to bind DNA and activate expression in vitro. {ECO:0000269|PubMed:22446626}.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;pharynx;blood;skeletal muscle;lung;placenta;macula lutea;visual apparatus;liver;head and neck;kidney;stomach; ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12641 0.11515 -0.47017169 23.25430526 44.86232 1.28491 ZNF329 2.30642332748683e-05 0.498005612649888 0.501971323116837 zinc finger protein 329 FUNCTION: May be involved in transcriptional regulation.; . . breast;frontal lobe;cochlea;thyroid;placenta;hippocampus;testis;blood;brain;mammary gland;retina;bone marrow; ciliary ganglion; 0.17217 0.09516 -0.402212257 26.7338995 104.19918 2.20548 ZNF330 0.838316378914674 0.161550227064296 0.000133394021029581 zinc finger protein 330 . . TISSUE SPECIFICITY: Widely expressed. Higher expression seen in heart and skeletal muscle. {ECO:0000269|PubMed:10593942}.; ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;whole body;endometrium;bone;iris;testis;brain;bladder;unclassifiable (Anatomical System);pharynx;blood;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach; dorsal root ganglion;testis - interstitial;heart;testis - seminiferous tubule;testis;ciliary ganglion;pons;skeletal muscle; 0.14469 0.10707 0.349177632 74.18023119 332.35652 3.87584 ZNF331 0.680597793500694 0.318462341044812 0.000939865454494235 zinc finger protein 331 FUNCTION: May be involved in transcriptional regulation. May play a role in spermatogenesis.; . TISSUE SPECIFICITY: Testis specific.; unclassifiable (Anatomical System);heart;ovary;cerebellum cortex;pineal body;colon;fovea centralis;choroid;lens;skeletal muscle;retina;breast;prostate;optic nerve;whole body;lung;larynx;thyroid;placenta;macula lutea;hypopharynx;testis;head and neck;brain;mammary gland; testis - interstitial;superior cervical ganglion;ovary;adrenal gland;adrenal cortex;atrioventricular node;trigeminal ganglion;parietal lobe; 0.54693 0.14855 -0.181750739 40.15687662 65.06963 1.66038 ZNF333 3.59807075705962e-09 0.763589707408859 0.236410288993071 zinc finger protein 333 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Highly expressed in heart.; unclassifiable (Anatomical System);heart;ovary;skeletal muscle;skin;uterus;prostate;whole body;lung;frontal lobe;iris;testis;spleen;cervix;kidney;brain; superior cervical ganglion;subthalamic nucleus;uterus corpus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.12377 0.08494 0.402364592 76.45081387 3507.88522 11.42722 ZNF334 4.08828905187586e-08 0.3511742867113 0.648825672405809 zinc finger protein 334 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);prostate;lung;atrium;islets of Langerhans;gum;hippocampus;liver;testis;spleen;head and neck;brain;skeletal muscle;stomach; ciliary ganglion; 0.44526 0.09404 0.891034851 89.2663364 153.32626 2.70797 ZNF335 0.00650300156857181 0.993496720660239 2.77771189646689e-07 zinc finger protein 335 FUNCTION: Component or associated component of some histone methyltransferase complexes may regulate transcription through recruitment of those complexes on gene promoters. Enhances ligand- dependent transcriptional activation by nuclear hormone receptors. Plays an important role in neural progenitor cell proliferation and self-renewal through the regulation of specific genes involved brain development, including REST. Also controls the expression of genes involved in somatic development and regulates, for instance, lymphoblast proliferation. {ECO:0000269|PubMed:12215545, ECO:0000269|PubMed:18180299, ECO:0000269|PubMed:23178126}.; DISEASE: Microcephaly 10, primary, autosomal recessive (MCPH10) [MIM:615095]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age- related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. MCPH10 is characterized by extremely small head size and death usually by 1 year of age. Neuropathologic examination shows severe loss of neurons as well as neuronal loss of polarity and abnormal dendritic maturation. {ECO:0000269|PubMed:23178126}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12215545, ECO:0000269|PubMed:23178126}.; ovary;colon;parathyroid;fovea centralis;choroid;retina;bone marrow;uterus;optic nerve;frontal lobe;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;duodenum;spleen;head and neck;cervix;kidney;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.32089 0.10350 -1.115293937 6.623024298 492.69866 4.56459 ZNF337 2.29239140713378e-09 0.873277131915902 0.126722865791706 zinc finger protein 337 FUNCTION: May be involved in transcriptional regulation.; . . myocardium;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;testis;spinal ganglion;brain;pineal gland;unclassifiable (Anatomical System);heart;cartilage;cerebellum cortex;muscle;adrenal cortex;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;spleen;cervix;kidney; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.17887 0.09852 -0.020150552 52.25288983 1465.63986 7.13718 ZNF337-AS1 . . . ZNF337 antisense RNA 1 . . . . . . . . . . . ZNF341 0.124189156815528 0.875767745169137 4.30980153348915e-05 zinc finger protein 341 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);prostate;pancreas;lung;endometrium;visual apparatus;liver;testis;spleen;blood;kidney;mammary gland;bone marrow; trigeminal ganglion;cerebellum; 0.12152 0.09319 -1.144569759 6.363529134 305.05398 3.71933 ZNF341-AS1 . . . ZNF341 antisense RNA 1 . . . . . . . . . . . ZNF343 1.21297037084745e-14 0.0216177236780832 0.978382276321905 zinc finger protein 343 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;skin;uterus;optic nerve;frontal lobe;testis;dura mater;bladder;brain;tonsil;unclassifiable (Anatomical System);meninges;heart;cartilage;skeletal muscle;pancreas;lung;pia mater;nasopharynx;placenta;visual apparatus;liver;spleen;kidney;stomach; dorsal root ganglion;thalamus;superior cervical ganglion;medulla oblongata;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06957 0.07707 0.624649618 83.53385232 392.09083 4.16727 ZNF345 2.33150075364907e-11 0.00985375418499555 0.990146245791689 zinc finger protein 345 FUNCTION: May be involved in transcriptional regulation.; . . prostate;whole body;liver;spleen;germinal center;bone marrow; superior cervical ganglion;trigeminal ganglion; 0.13499 . -0.135838822 43.77211607 108.27875 2.25782 ZNF346 0.782525684649077 0.215997761463374 0.00147655388754921 zinc finger protein 346 FUNCTION: Binds with low affinity to dsDNA and ssRNA, and with high affinity to dsRNA, with no detectable sequence specificity. {ECO:0000269|PubMed:24521053}.; . . lymphoreticular;ovary;fovea centralis;skin;retina;uterus;prostate;whole body;frontal lobe;thyroid;bone;testis;brain;artery;unclassifiable (Anatomical System);cartilage;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;aorta;cerebellum; . 0.09848 0.09546 -0.207437529 38.2814343 16.90108 0.59524 ZNF346-IT1 . . . ZNF346 intronic transcript 1 . . . . . . . . . . . ZNF347 1.26208000070804e-17 0.000733205239027775 0.999266794760972 zinc finger protein 347 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);optic nerve;lung;endometrium;placenta;macula lutea;testis;blood;fovea centralis;choroid;lens;brain;retina; trigeminal ganglion;skin; 0.06109 . -0.551080959 19.93394669 53.4466 1.45289 ZNF350 0.000264161595424169 0.930339407177832 0.069396431226744 zinc finger protein 350 FUNCTION: Transcriptional repressor. Binds to a specific sequence, 5'-GGGxxxCAGxxxTTT-3', within GADD45 intron 3. {ECO:0000269|PubMed:11090615}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11161714}.; ovary;choroid;fovea centralis;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;testis;germinal center;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;islets of Langerhans;lens;skeletal muscle;pancreas;lung;placenta;visual apparatus;macula lutea;head and neck;kidney; superior cervical ganglion;medulla oblongata;trigeminal ganglion;parietal lobe;skeletal muscle; 0.21884 0.16743 0.843299698 88.37579618 1379.50737 6.95828 ZNF350-AS1 . . . ZNF350 antisense RNA 1 . . . . . . . . . . . ZNF354A 0.000195110610594158 0.97545683579023 0.0243480535991757 zinc finger protein 354A . . TISSUE SPECIFICITY: Expressed in kidney and inner ear.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;frontal lobe;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;placenta;visual apparatus;liver;kidney;mammary gland; dorsal root ganglion;medulla oblongata;superior cervical ganglion;subthalamic nucleus;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;cingulate cortex; 0.22982 0.11215 -0.312207497 32.05944798 80.18108 1.89303 ZNF354B 1.96076723041207e-05 0.892509081431566 0.10747131089613 zinc finger protein 354B FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);frontal lobe;endometrium;sympathetic chain;hippocampus;liver;testis;brain;stomach; . 0.16272 0.10945 0.244401822 69.50931824 62.26671 1.60991 ZNF354C 0.000135489022139871 0.853250258003394 0.146614252974466 zinc finger protein 354C FUNCTION: May function as a transcription repressor. Suppresses osteogenic effects of RUNX2. Binds to 5'-CCACA-3' core sequence. May be involved in osteoblastic differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:15555547}.; . TISSUE SPECIFICITY: Expressed in kidney and skeletal muscle. Very low expression in brain and heart. {ECO:0000269|PubMed:15555547}.; unclassifiable (Anatomical System);visual apparatus;skeletal muscle; globus pallidus;ciliary ganglion;atrioventricular node; 0.25989 0.10292 1.241986644 93.38877094 141.39578 2.59351 ZNF355P . . . zinc finger protein 355, pseudogene FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . . . ZNF358 0.867025329554356 0.131107951196751 0.00186671924889363 zinc finger protein 358 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;muscle;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;spleen;cervix;kidney;stomach;aorta;thymus; prefrontal cortex; 0.18567 . 0.440999548 77.79547063 843.62578 5.68608 ZNF362 0.928285965252321 0.0716354766822691 7.85580654098872e-05 zinc finger protein 362 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.71709 0.11104 0.038710339 56.92380278 38.25897 1.13586 ZNF365 3.62115394483978e-05 0.820581192473209 0.179382595987342 zinc finger protein 365 FUNCTION: May play a role in uric acid excretion.; DISEASE: Uric acid nephrolithiasis (UAN) [MIM:605990]: A form of nephrolithiasis, a common multifactorial disease characterized by stones formation in the kidney and urinary tract. Nephrolithiasis is due to supersaturation of the urine by stone-forming constituents, including calcium, oxalate and uric acid. Crystals or foreign bodies can act as nidi, upon which ions from the supersaturated urine form microscopic crystalline structures. Uric acid nephrolithiasis occurs when the urine becomes overly concentrated with uric acid and accounts for 20% of all stones. {ECO:0000269|PubMed:12740763}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Isoform 4 is expressed in placenta, lung, kidney and pancreas. {ECO:0000269|PubMed:12740763}.; cerebral cortex; whole brain;amygdala;occipital lobe;superior cervical ganglion;medulla oblongata;thalamus;hypothalamus;temporal lobe;pons;caudate nucleus;subthalamic nucleus;prefrontal cortex;globus pallidus;cingulate cortex;parietal lobe; 0.11666 0.07139 1.73619725 96.62656287 180.89533 2.92324 ZNF366 0.504819503691726 0.494328178823784 0.000852317484490106 zinc finger protein 366 FUNCTION: Has transcriptional repression activity. Acts as corepressor of ESR1; the function seems to involve CTBP1 and histone deacetylases. {ECO:0000269|PubMed:17085477}.; . . unclassifiable (Anatomical System);lung;ovary;nasopharynx;placenta;testis;colon;parathyroid;spleen;kidney;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.23725 0.10456 0.251682437 69.69214437 1136.9058 6.43160 ZNF367 0.802012369199828 0.196850743252678 0.0011368875474934 zinc finger protein 367 FUNCTION: Transcriptional activator. Isoform 1 may be involved in transcriptional activation of erythroid genes. {ECO:0000269|PubMed:15344908}.; . . . . 0.81619 0.11134 . . 44.4013 1.27358 ZNF382 0.853323188005293 0.146173115924 0.000503696070706737 zinc finger protein 382 FUNCTION: Functions as a sequence-specific transcriptional repressor. {ECO:0000250}.; . TISSUE SPECIFICITY: Specifically expressed in heart with a weaker expression also detected in skeletal muscle. {ECO:0000269|PubMed:12459182}.; unclassifiable (Anatomical System);lung;nasopharynx;testis;mammary gland;skin; . 0.17555 0.10370 0.795569043 87.49115357 600.84579 4.96070 ZNF383 6.27662995876316e-08 0.249136571657456 0.750863365576244 zinc finger protein 383 FUNCTION: May function as a transcriptional repressor, suppressing transcriptional activities mediated by MAPK signaling pathways. {ECO:0000269|PubMed:15964543}.; . TISSUE SPECIFICITY: Expressed in heart, placenta, liver, pancreas and with a higher level in skeletal muscle. {ECO:0000269|PubMed:15964543}.; unclassifiable (Anatomical System);prostate;lung;ovary;bone;placenta;urinary;parathyroid;cervix;kidney;brain;cerebellum; atrioventricular node; 0.14145 0.09722 -0.381986487 27.68931352 17.44204 0.61157 ZNF384 0.941996440237097 0.057994255782043 9.30398085977355e-06 zinc finger protein 384 FUNCTION: Transcription factor that binds the consensus DNA sequence [GC]AAAAA. Seems to bind and regulate the promoters of MMP1, MMP3, MMP7 and COL1A1 (By similarity). {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;urinary;blood;lens;skeletal muscle;breast;lung;placenta;macula lutea;visual apparatus;hypopharynx;liver;amnion;spleen;head and neck;cervix;kidney;mammary gland;stomach; adrenal gland;globus pallidus;kidney;atrioventricular node;skeletal muscle;cingulate cortex;cerebellum; 0.40362 0.12962 -0.778825328 12.88039632 38.57291 1.14423 ZNF385A 0.848554693733189 0.1513335025334 0.000111803733410899 zinc finger protein 385A FUNCTION: RNA-binding protein that affects the localization and the translation of a subset of mRNA. May play a role in adipogenesis through binding to the 3'-UTR of CEBPA mRNA and regulation of its translation. Targets ITPR1 mRNA to dendrites in Purkinje cells, and may regulate its activity-dependent translation. With ELAVL1, binds the 3'-UTR of p53/TP53 mRNAs to control their nuclear export induced by CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the CDKN2A anti- proliferative activity. May also bind CCNB1 mRNA. Alternatively, may also regulate p53/TP53 activity through direct protein-protein interaction. Interacts with p53/TP53 and promotes cell-cycle arrest over apoptosis enhancing preferentially the DNA binding and transactivation of p53/TP53 on cell-cycle arrest target genes over proapoptotic target genes. May also regulate the ubiquitination and stability of CDKN1A promoting DNA damage-induced cell cycle arrest. Also plays a role in megakaryocytes differentiation. {ECO:0000269|PubMed:17719541}.; . TISSUE SPECIFICITY: Expressed predominantly in the retina. {ECO:0000269|PubMed:15527981}.; colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;oesophagus;endometrium;bone;thyroid;iris;brain;unclassifiable (Anatomical System);heart;cartilage;pineal body;adrenal cortex;pharynx;lens;pancreas;lung;placenta;hippocampus;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;stomach;cerebellum; caudate nucleus;trigeminal ganglion; 0.23879 0.11241 -0.538132194 20.26421326 19.75985 0.67465 ZNF385B 0.00106530263678159 0.950179032452712 0.0487556649105067 zinc finger protein 385B FUNCTION: May play a role in p53/TP53-mediated apoptosis. {ECO:0000269|PubMed:22945289}.; . TISSUE SPECIFICITY: Detected in germinal center of lymph node (at protein level). Expressed in spleen, lymph node and tonsil. {ECO:0000269|PubMed:22945289}.; unclassifiable (Anatomical System);colon;fovea centralis;choroid;lens;retina;uterus;optic nerve;whole body;lung;bone;macula lutea;visual apparatus;liver;testis;kidney;brain; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle;cerebellum; 0.60329 0.11252 0.106667882 61.73036093 334.03279 3.88289 ZNF385C . . . zinc finger protein 385C . . . . . 0.24836 . . . 68.65605 1.71475 ZNF385D 0.724321866793819 0.275076530798497 0.000601602407683786 zinc finger protein 385D . . . unclassifiable (Anatomical System);lung;whole body;frontal lobe;cartilage;ovary;bone;placenta;sympathetic chain;testis;parathyroid;kidney;spinal ganglion;tonsil; medulla oblongata;superior cervical ganglion;testis - seminiferous tubule;ciliary ganglion;pons;cingulate cortex;skeletal muscle; 0.89616 0.11809 0.130533008 63.35810333 376.29195 4.08971 ZNF385D-AS1 . . . ZNF385D antisense RNA 1 . . . . . . . . . . . ZNF385D-AS2 . . . ZNF385D antisense RNA 2 . . . . . . . . . . . ZNF391 9.25869403182407e-07 0.315600702605261 0.684398371525336 zinc finger protein 391 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);breast;lung;testis;colon; testis - interstitial;superior cervical ganglion;testis; 0.05228 . -0.314027422 31.9297004 82.90274 1.93373 ZNF394 0.0433348237892985 0.950833419365929 0.00583175684477243 zinc finger protein 394 FUNCTION: May be involved in transcriptional regulation.; . . ovary;salivary gland;intestine;colon;parathyroid;skin;bone marrow;uterus;prostate;larynx;bone;thyroid;spinal ganglion;brain;tonsil;unclassifiable (Anatomical System);lymph node;cerebellum cortex;islets of Langerhans;pharynx;blood;skeletal muscle;breast;lung;cornea;nasopharynx;placenta;visual apparatus;liver;head and neck;kidney;mammary gland;stomach; . 0.10089 0.09306 -0.110153916 45.48832272 82.70754 1.93165 ZNF395 0.819057406199046 0.180905829259419 3.67645415343966e-05 zinc finger protein 395 FUNCTION: Plays a role in papillomavirus genes transcription.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11853404, ECO:0000269|PubMed:14625278}.; ovary;skin;bone marrow;retina;prostate;optic nerve;cochlea;endometrium;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;tongue;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;macula lutea;liver;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pancreas;lung;cornea;nasopharynx;placenta;head and neck;kidney;stomach; dorsal root ganglion;prostate;superior cervical ganglion; 0.32677 . -0.821100135 11.88369899 68.62215 1.71442 ZNF396 4.72222820428313e-07 0.390050028501938 0.609949499275242 zinc finger protein 396 FUNCTION: Isoform 1 and isoform 2 act as DNA-dependent transcriptional repressors. {ECO:0000269|PubMed:12801647}.; . TISSUE SPECIFICITY: Expressed strongly in liver, moderately in skeletal muscle and weakly in kidney, pancreas, spleen and prostate. {ECO:0000269|PubMed:12801647}.; unclassifiable (Anatomical System);optic nerve;lung;bone;macula lutea;pituitary gland;testis;fovea centralis;choroid;kidney;lens;brain;retina; superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.08664 . -0.049474214 50.01179523 230.57705 3.28151 ZNF397 0.00104846294119933 0.824470384018632 0.174481153040169 zinc finger protein 397 FUNCTION: Isoform 3 acts as a DNA-dependent transcriptional repressor. {ECO:0000269|PubMed:12801647}.; . TISSUE SPECIFICITY: Expressed strongly in testis, moderately in skeletal muscle, pancreas and prostate, and weakly in heart, placenta, liver, kidney, spleen, thymus and small intestine. {ECO:0000269|PubMed:12801647}.; ovary;sympathetic chain;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;optic nerve;whole body;endometrium;thyroid;testis;pineal gland;brain;unclassifiable (Anatomical System);islets of Langerhans;adrenal cortex;blood;lens;skeletal muscle;breast;greater omentum;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;cervix;spleen; subthalamic nucleus;temporal lobe;prefrontal cortex;appendix;globus pallidus;atrioventricular node;trigeminal ganglion; 0.25337 0.09615 -0.293801652 32.93819297 15.67318 0.55897 ZNF398 0.959343721509368 0.0406374435668175 1.88349238147202e-05 zinc finger protein 398 FUNCTION: Function as a transcriptional activator.; . . ovary;salivary gland;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;frontal lobe;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;lymph node;cartilage;heart;tongue;islets of Langerhans;adrenal cortex;blood;skeletal muscle;bile duct;breast;pancreas;lung;nasopharynx;placenta;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;cerebellum; 0.49587 0.11175 -0.574945567 18.90186365 485.03066 4.53484 ZNF402P . . . zinc finger protein 402, pseudogene . . . . . . . . . . . ZNF404 1.48958552341176e-05 0.644024932994488 0.355960171150278 zinc finger protein 404 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System); . 0.05453 . . . 5004.41273 14.44987 ZNF407 0.999995919065608 4.08093438843216e-06 3.23768383101531e-15 zinc finger protein 407 FUNCTION: May be involved in transcriptional regulation.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;optic nerve;frontal lobe;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);urinary;pharynx;blood;lens;lung;cornea;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.16501 . -0.944737233 9.383109224 269.31141 3.52055 ZNF408 7.89160984461696e-06 0.914702882261958 0.0852892261281974 zinc finger protein 408 FUNCTION: May be involved in transcriptional regulation.; DISEASE: Retinitis pigmentosa 72 (RP72) [MIM:616469]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:25882705}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Highest expression is observed in adult retina; abundantly expressed in the fetal eye (PubMed:23716654). In the retina, it is detected in the outer nuclear layer, especially cone and rod photoreceptor cells, ganglion cell layer and both outer and inner plexiform layers (at protein level) (PubMed:25882705). Expressed in retinal blood vessels (at protein level) (PubMed:25882705). {ECO:0000269|PubMed:23716654, ECO:0000269|PubMed:25882705}.; lymphoreticular;ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;lens;skeletal muscle;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;parietal lobe;skeletal muscle; 0.06708 0.09112 -1.017713296 8.103326256 2355.61017 9.00036 ZNF410 0.661705780560574 0.338065184341596 0.000229035097830545 zinc finger protein 410 FUNCTION: Transcription factor that activates transcription of matrix-remodeling genes such as MMP1 during fibroblast senescence. {ECO:0000269|PubMed:12370286}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12370286}.; ovary;salivary gland;intestine;colon;parathyroid;choroid;skin;retina;bone marrow;uterus;prostate;whole body;frontal lobe;endometrium;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;pharynx;blood;lens;skeletal muscle;breast;bile duct;pancreas;lung;adrenal gland;nasopharynx;trabecular meshwork;placenta;visual apparatus;liver;cervix;spleen;head and neck;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;adrenal cortex;prefrontal cortex;testis;atrioventricular node;trigeminal ganglion; 0.15957 0.11683 -0.471992905 23.03609342 17.75148 0.62052 ZNF414 0.00274920575712607 0.797822957480899 0.199427836761975 zinc finger protein 414 FUNCTION: May be involved in transcriptional regulation.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;bone;iris;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;islets of Langerhans;muscle;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;thymus; superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion; 0.11237 0.08916 . . 2913.35847 10.24153 ZNF415 0.00582848757727488 0.902603761671053 0.0915677507516715 zinc finger protein 415 FUNCTION: Involved in transcriptional regulation. Transcriptional activity differed among the various isoforms. All isoforms except isoform 3 seem to suppresses the transcriptional activities of AP- 1 and p53/TP53. {ECO:0000269|PubMed:17055453}.; . TISSUE SPECIFICITY: Expressed in all tissues examined. Isoforms are differentially expressed. Isoform 3 and isoform 5 were highly expressed, isoform 4 moderately expressed, isoform 2 lower expression, the lowest expression level was seem with isoform 1. {ECO:0000269|PubMed:17055453}.; unclassifiable (Anatomical System);ovary;parathyroid;prostate;lung;endometrium;adrenal gland;placenta;thyroid;testis;kidney;brain;bladder;mammary gland;thymus; . 0.08684 0.08917 1.556142814 95.65935362 101.45654 2.18119 ZNF415P1 . . . zinc finger protein 415 pseudogene 1 . . . . . . . . . . . ZNF416 0.000574203935929878 0.896616643355668 0.102809152708402 zinc finger protein 416 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lymph node;heart;ovary;parathyroid;skin;skeletal muscle;uterus;prostate;whole body;lung;endometrium;bone;placenta;thyroid;testis;cervix;brain; superior cervical ganglion; 0.04690 . -0.666770504 15.86459071 44.10909 1.26615 ZNF417 1.12805634572858e-06 0.56646625383282 0.433532618110834 zinc finger protein 417 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);heart;colon;blood;skeletal muscle;bone marrow;breast;uterus;pancreas;prostate;frontal lobe;larynx;thyroid;placenta;liver;amniotic fluid;head and neck;spleen;kidney;brain;mammary gland;stomach; . 0.09800 0.07895 0.887394731 89.18966737 527.71827 4.68764 ZNF418 4.09196213504996e-21 0.000634817335382158 0.999365182664618 zinc finger protein 418 FUNCTION: Transcriptional repressor. {ECO:0000269|Ref.1}.; . . . . 0.14679 . 0.07167258 59.15899976 147.26502 2.64424 ZNF419 2.07812060379433e-06 0.460864739464592 0.539133182414804 zinc finger protein 419 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);medulla oblongata;heart;cartilage;skin;bone marrow;prostate;pancreas;whole body;lung;epididymis;placenta;liver;testis;spleen;germinal center;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22698 0.08472 1.578193463 95.76551073 91.77944 2.06141 ZNF420 3.29013380261281e-08 0.524198127781387 0.475801839317275 zinc finger protein 420 FUNCTION: May be involved in transcriptional regulation.; . . sympathetic chain;colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;optic nerve;whole body;endometrium;bone;unclassifiable (Anatomical System);heart;cerebellum cortex;islets of Langerhans;muscle;blood;lens;skeletal muscle;lung;macula lutea;visual apparatus;kidney;peripheral nerve; superior cervical ganglion; 0.20798 . -1.023168368 7.944090587 35.77058 1.07599 ZNF423 0.990468533215048 0.00953136033885142 1.06446100076639e-07 zinc finger protein 423 FUNCTION: Transcription factor that can both act as an activator or a repressor depending on the context. Plays a central role in BMP signaling and olfactory neurogenesis. Associates with SMADs in response to BMP2 leading to activate transcription of BMP target genes. Acts as a transcriptional repressor via its interaction with EBF1, a transcription factor involved in terminal olfactory receptor neurons differentiation; this interaction preventing EBF1 to bind DNA and activate olfactory-specific genes. Involved in olfactory neurogenesis by participating in a developmental switch that regulates the transition from differentiation to maturation in olfactory receptor neurons. Controls proliferation and differentiation of neural precursors in cerebellar vermis formation. {ECO:0000269|PubMed:10660046}.; DISEASE: Nephronophthisis 14 (NPHP14) [MIM:614844]: An autosomal recessive disorder manifesting as infantile-onset kidney disease, cerebellar vermis hypoplasia, and situs inversus. Nephronophthisis is a progressive tubulo-interstitial kidney disorder histologically characterized by modifications of the tubules with thickening of the basement membrane, interstitial fibrosis and, in the advanced stages, medullary cysts. {ECO:0000269|PubMed:22863007}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Joubert syndrome 19 (JBTS19) [MIM:614844]: A form of Joubert syndrome, a disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). JBTS19 patients have polycystic kidney disease, Leber congenital amaurosis, cerebellar vermis hypoplasia, and breathing abnormality. {ECO:0000269|PubMed:22863007}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in brain, lung, skeletal muscle, heart, pancreas and kidney but not liver or placenta. Also expressed in aorta, ovary, pituitary, small intestine, fetal brain, fetal kidney and, within the adult brain, in the substantia nigra, medulla, amygdala, thalamus and cerebellum. {ECO:0000269|PubMed:10660046}.; unclassifiable (Anatomical System);optic nerve;lung;ovary;cochlea;placenta;sympathetic chain;visual apparatus;liver;spleen;brain; uterus corpus;superior cervical ganglion;appendix;ciliary ganglion;skeletal muscle;cerebellum; 0.57996 0.12164 -2.203192877 1.362349611 308.99952 3.74292 ZNF425 3.18872671120405e-14 0.0103404284746991 0.989659571525269 zinc finger protein 425 FUNCTION: Acts as a transcriptional repressor. {ECO:0000269|PubMed:21266108}.; . . . . 0.13604 . -0.328796968 30.86223166 119.16279 2.37516 ZNF426 5.94845054621104e-13 0.0298669094060793 0.970133090593326 zinc finger protein 426 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;endometrium;islets of Langerhans;hippocampus;adrenal cortex;liver;duodenum;cervix;brain;skin;skeletal muscle;stomach; testis - interstitial;superior cervical ganglion; 0.16067 0.09713 -0.754958418 13.57631517 13.94593 0.50526 ZNF428 0.720275479182866 0.266066436578054 0.0136580842390795 zinc finger protein 428 . . . unclassifiable (Anatomical System);medulla oblongata;islets of Langerhans;salivary gland;fovea centralis;choroid;lens;retina;uterus;pancreas;prostate;optic nerve;whole body;lung;endometrium;bone;macula lutea;liver;germinal center;brain;stomach; whole brain;fetal brain;temporal lobe;pituitary; 0.11354 . 0.125076652 62.7388535 110.22443 2.28404 ZNF429 9.7121420957407e-14 0.00538021738762905 0.994619782612274 zinc finger protein 429 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.16505 . 1.556142814 95.65935362 259.14141 3.45954 ZNF430 0.000180790697407956 0.891885983641609 0.107933225660983 zinc finger protein 430 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);prostate;adrenal gland;thyroid;placenta;retina; dorsal root ganglion;superior cervical ganglion;medulla oblongata;globus pallidus;trigeminal ganglion; 0.17193 . 0.665103516 84.6131163 49.27571 1.37205 ZNF431 0.000233579258381277 0.919327664434986 0.0804387563066331 zinc finger protein 431 FUNCTION: Sequence-specific DNA binding transcriptional repressor. Represses target gene transcription by recruiting HDAC1 and HDAC2 histone deacetylases. Acts as a specific transcriptional repressor for PTCH1 during embryonic development. Required for osteoblast differentiation and sonic hedgehog/SHH signaling response. Binds to the consensus site 5'-GCGCCC-3' in the promoter of PTCH1 (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;blood;brain; . 0.27308 . 0.328949044 73.41354093 80.79033 1.89921 ZNF432 6.80516599926101e-11 0.400599483392325 0.599400516539623 zinc finger protein 432 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);amygdala;prostate;pancreas;lung;whole body;cartilage;lacrimal gland;islets of Langerhans;liver;spleen;germinal center; superior cervical ganglion;medulla oblongata;trigeminal ganglion;parietal lobe;skeletal muscle; . . -0.110153916 45.48832272 1664.5459 7.53128 ZNF433 1.9474436020732e-12 0.031166246904124 0.968833753093928 zinc finger protein 433 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;cartilage;testis; testis - interstitial;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node; . . -0.642904474 16.62538335 159.38951 2.75839 ZNF436 0.304488387158864 0.691521546933644 0.00399006590749187 zinc finger protein 436 FUNCTION: May be a transcriptional repressor. {ECO:0000269|PubMed:17089209}.; . TISSUE SPECIFICITY: Expressed in fetal brain, heart, liver, spleen, bladder, lung, skin, skeletal muscle, stomach and pancreas. {ECO:0000269|PubMed:17089209}.; colon;skin;retina;uterus;prostate;whole body;cerebral cortex;endometrium;larynx;thyroid;bone;testis;dura mater;brain;bladder;unclassifiable (Anatomical System);meninges;heart;cartilage;urinary;breast;pancreas;pia mater;lung;placenta;liver;spleen;head and neck;kidney;mammary gland;stomach; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.50187 . -0.47017169 23.25430526 69.2159 1.72366 ZNF436-AS1 . . . ZNF436 antisense RNA 1 . . . . . 0.12418 . . . . . ZNF438 3.4556460409994e-05 0.812620956753052 0.187344486786538 zinc finger protein 438 FUNCTION: Isoform 1 acts as a transcriptional repressor.; . TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17669267}.; myocardium;choroid;fovea centralis;bone marrow;retina;uterus;whole body;optic nerve;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;blood;lens;breast;lung;epididymis;visual apparatus;macula lutea;liver;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;atrioventricular node;skeletal muscle;cerebellum; 0.08680 . 0.646696306 84.12361406 768.73625 5.48835 ZNF439 3.21400432787086e-08 0.174571485542958 0.825428482316999 zinc finger protein 439 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);ovary;heart;bone;placenta;brain; . 0.20448 . 0.953537969 90.08610521 391.8226 4.16553 ZNF440 5.58999225635548e-13 0.00782587658786499 0.992174123411576 zinc finger protein 440 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;cartilage;ovary;bone;urinary;liver;duodenum;colon;mammary gland;skeletal muscle; . . . 0.981046964 90.45765511 289.18701 3.63800 ZNF441 0.0276670958531812 0.969973627056425 0.00235927709039391 zinc finger protein 441 FUNCTION: May be involved in transcriptional regulation.; . . breast;visual apparatus;mammary gland; superior cervical ganglion;trigeminal ganglion; 0.12302 . 0.643056625 84.05284265 91.89629 2.06212 ZNF442 1.47367601702494e-07 0.608020768566763 0.391979084065635 zinc finger protein 442 FUNCTION: May be involved in transcriptional regulation.; . . cartilage;visual apparatus;colon;kidney;stomach; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.15135 . 2.157029472 98.01250295 809.84714 5.59897 ZNF443 1.8302370216888e-05 0.884055188981781 0.115926508648002 zinc finger protein 443 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;endometrium;liver;kidney;brain;skin; . 0.12492 0.09066 1.693921333 96.42604388 4900.49067 14.26813 ZNF444 0.691714109350747 0.290375384145263 0.0179105065039897 zinc finger protein 444 FUNCTION: Transcriptional regulator. Binds to the 5'-flanking critical region of the SCARF1 promoter.; . . ovary;colon;fovea centralis;choroid;retina;prostate;optic nerve;whole body;endometrium;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;medulla oblongata;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;pons;trigeminal ganglion;skeletal muscle;cingulate cortex; 0.16701 0.10915 . . 188.97511 2.98506 ZNF444P1 . . . zinc finger protein 444 pseudogene 1 . . . . . . . . . . . ZNF445 0.996478491372579 0.00352149929404854 9.33337285074954e-09 zinc finger protein 445 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);pancreas;placenta;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.18264 0.10206 -0.440847477 24.59896202 360.52338 4.01855 ZNF446 3.39122166459363e-06 0.56383670467369 0.436159904104646 zinc finger protein 446 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);pancreas;lung;endometrium;epididymis;bone;placenta;liver;spleen;brain;mammary gland;stomach; pons; 0.03476 . 0.224175308 68.48903043 1861.06516 7.95087 ZNF449 0.871457178959833 0.128187874029697 0.000354947010470674 zinc finger protein 449 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);meninges;ovary;colon;parathyroid;skin;skeletal muscle;uterus;pia mater;whole body;endometrium;larynx;bone;placenta;liver;testis;amniotic fluid;head and neck;spleen;dura mater;germinal center;kidney;stomach; ciliary ganglion;atrioventricular node; 0.36225 0.10540 -0.648365105 16.35999056 6.58241 0.24341 ZNF451 1.98298362859696e-06 0.998711287306639 0.00128672970973219 zinc finger protein 451 FUNCTION: May be involved in transcriptional regulation. Coactivator for steroid receptors.; . . umbilical cord;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;larynx;bone;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;hypothalamus;urinary;blood;lens;skeletal muscle;breast;lung;adrenal gland;epididymis;placenta;macula lutea;visual apparatus;liver;amnion;spleen;head and neck;kidney;mammary gland;stomach;aorta;cerebellum; dorsal root ganglion;amygdala;superior cervical ganglion;subthalamic nucleus;occipital lobe;hypothalamus;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.32090 0.09754 -0.775187015 13.05142722 58.96781 1.55810 ZNF454 4.44345719446746e-05 0.853005902499314 0.146949662928741 zinc finger protein 454 FUNCTION: May be involved in transcriptional regulation.; . . breast;frontal lobe;stomach; atrioventricular node; 0.16867 . 0.328949044 73.41354093 629.49326 5.05639 ZNF460 0.647011501763315 0.351701298243968 0.00128719999271676 zinc finger protein 460 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Ubiquitously expressed at low levels. Highest levels are found in pancreas and liver. {ECO:0000269|PubMed:15004467}.; unclassifiable (Anatomical System);breast;prostate;frontal lobe;ovary;adrenal gland;larynx;thyroid;placenta;head and neck; superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;kidney;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.07049 . -0.446304853 24.33356924 29.38374 0.93961 ZNF461 3.15672573724231e-06 0.548327089780292 0.451669753493971 zinc finger protein 461 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in liver, kidney, pancreas, thymus, and small intestine. {ECO:0000269|PubMed:15004467}.; unclassifiable (Anatomical System);optic nerve;whole body;placenta;macula lutea;testis;fovea centralis;choroid;kidney;lens;brain;retina; occipital lobe;ciliary ganglion;trigeminal ganglion;skeletal muscle; 0.19343 0.11347 -0.356299879 29.31115829 319.2698 3.79475 ZNF462 0.999999998400102 1.59989820205475e-09 1.62994669368555e-23 zinc finger protein 462 FUNCTION: May be involved in transcriptional regulation.; . . developmental;colon;skin;retina;bone marrow;uterus;prostate;endometrium;larynx;thyroid;bone;testis;brain;unclassifiable (Anatomical System);heart;adrenal cortex;blood;skeletal muscle;breast;lung;epididymis;placenta;visual apparatus;hippocampus;liver;alveolus;head and neck;kidney;stomach; testis - interstitial;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.44103 0.10698 -2.813971075 0.642840293 2351.37936 8.98452 ZNF467 1.71294598036323e-07 0.128880734235836 0.871119094469566 zinc finger protein 467 FUNCTION: Transcription factor that promotes adipocyte differentiation and suppresses osteoblast differentiation in the bone marrow. Enhances the osteoclast-supporting ability of stromal cells. Binds with STAT3 the consensus sequence 5'-CTTCTGGGAAGA-3' of the acute phase response element (APRE). Transactivates several promoters including FOS, OSM and PPARG. Recruits a histone deacetylase complex (By similarity). {ECO:0000250}.; . . colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;pituitary gland;iris;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;pancreas;lung;macula lutea;visual apparatus;liver;cervix;spleen;kidney;mammary gland;thymus; superior cervical ganglion;trigeminal ganglion; 0.11153 0.10767 . . 754.58261 5.44768 ZNF468 4.58040583827181e-12 0.0072836354839755 0.992716364511444 zinc finger protein 468 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed in placenta, pancreas, and small intestine. Lower expression in colon, ovary, testis, prostate, thymus, spleen, kidney, and liver. No expression detected in heart and brain. {ECO:0000269|PubMed:16144304}.; uterus;whole body;cartilage;liver;testis;spleen;germinal center;spinal ganglion; . 0.14014 . 1.978773583 97.6232602 1056.4431 6.23965 ZNF469 . . . zinc finger protein 469 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Detected in cornea, sclera, skin fibroblasts and striated muscle. {ECO:0000269|PubMed:18452888}.; . . . . . . 3862.54073 12.24999 ZNF470 2.39342955174962e-07 0.473881277770083 0.526118482886962 zinc finger protein 470 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Highly expressed in testis. Very low expression in thymus. No expression in other tissues tested. Expressed in a differentiation stage-specific manner in mesenchymal chondrogenic progenitor cells. {ECO:0000269|PubMed:15302581}.; lung; dorsal root ganglion;superior cervical ganglion; 0.17139 . 0.468503535 78.79806558 987.74671 6.06120 ZNF471 3.60935729960555e-10 0.0487302718757675 0.951269727763297 zinc finger protein 471 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;frontal lobe;ovary;placenta;visual apparatus;testis;parathyroid;kidney;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;skeletal muscle; 0.20062 0.10306 1.17583962 92.75182826 3507.00662 11.41797 ZNF473 0.774568360403142 0.225363608303045 6.80312938134124e-05 zinc finger protein 473 FUNCTION: Involved in histone 3'-end pre-mRNA processing by associating with U7 snRNP and interacting with SLBP/pre-mRNA complex. Increases histone 3'-end pre-mRNA processing but has no effect on U7 snRNP levels, when overexpressed. Required for cell cycle progression from G1 to S phases. {ECO:0000269|PubMed:11782445, ECO:0000269|PubMed:16714279, ECO:0000269|PubMed:16914750}.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;larynx;testis;brain;unclassifiable (Anatomical System);heart;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;pons; 0.05297 0.07611 1.605718424 95.91295117 1668.74611 7.54009 ZNF474 5.66230084983659e-07 0.134941373059343 0.865058060710572 zinc finger protein 474 . . . unclassifiable (Anatomical System);lung;testis; . 0.10169 0.06794 1.976952171 97.61146497 2591.86809 9.53067 ZNF479 0.00810131717246567 0.930443937245463 0.0614547455820711 zinc finger protein 479 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Expressed primarily in testis and fetal tissues. {ECO:0000269|PubMed:11410164}.; . . 0.07243 . 2.530174363 98.69662656 186.19449 2.96348 ZNF480 2.3568011757562e-07 0.709297410999718 0.290702353320164 zinc finger protein 480 FUNCTION: Involved in transcriptional regulation as an activator. {ECO:0000269|PubMed:15219843}.; . TISSUE SPECIFICITY: Expressed in fetal heart, heart, skeletal muscle, pancreas and placenta. {ECO:0000269|PubMed:15219843}.; unclassifiable (Anatomical System);ovary;islets of Langerhans;salivary gland;developmental;intestine;pharynx;colon;blood;skeletal muscle;skin;breast;prostate;lung;larynx;placenta;liver;spleen;head and neck;germinal center;kidney;brain;bladder;stomach;peripheral nerve; superior cervical ganglion; 0.16427 . -0.710864321 14.5730125 759.20608 5.46015 ZNF483 0.413497358830604 0.586154808440723 0.000347832728673008 zinc finger protein 483 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);prostate;frontal lobe;islets of Langerhans;placenta;thyroid;testis;blood;brain;skeletal muscle; dorsal root ganglion;superior cervical ganglion;medulla oblongata;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.26455 . -0.692458599 14.96815287 8.90928 0.32759 ZNF484 4.88360439462987e-09 0.209705250584171 0.790294744532224 zinc finger protein 484 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.10569 0.09059 0.001895464 54.03397028 559.48978 4.80554 ZNF485 3.53439212461835e-05 0.58961962415961 0.410345031919144 zinc finger protein 485 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);islets of Langerhans;nasopharynx;thyroid;germinal center;skeletal muscle;retina; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.15057 . -0.069700724 48.54328851 542.31265 4.74090 ZNF486 1.88053183954875e-08 0.0693866238791181 0.930613357315563 zinc finger protein 486 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);frontal lobe;adrenal gland; dorsal root ganglion;testis - interstitial;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.06526 . 0.378498378 75.58386412 233.00108 3.30046 ZNF487 0.381487324002118 0.477290910576896 0.141221765420986 zinc finger protein 487 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . 0.02248 . . . 641.86992 5.09139 ZNF488 0.000246116976810111 0.764456344972131 0.235297538051059 zinc finger protein 488 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.14773 . 0.643056625 84.05284265 244.16141 3.37178 ZNF490 0.0720463357958959 0.925323184686593 0.00263047951751078 zinc finger protein 490 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);breast;kidney;germinal center;brain; . 0.18842 0.10562 -0.358119787 29.16371786 44.25283 1.26853 ZNF491 5.1306652954028e-07 0.405347903266659 0.594651583666812 zinc finger protein 491 FUNCTION: May be involved in transcriptional regulation.; . . uterus; superior cervical ganglion;skeletal muscle; 0.19959 . 0.88921411 89.24274593 196.96831 3.03569 ZNF492 0.0174306218221897 0.891486783132985 0.091082595044825 zinc finger protein 492 FUNCTION: May be involved in transcriptional regulation.; . . . . . . 1.440434971 95.06369427 2768.1783 9.93127 ZNF493 3.18649368326509e-08 0.517403820572284 0.482596147562779 zinc finger protein 493 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);heart;ovary;hypothalamus;adrenal cortex;colon;skin;uterus;prostate;lung;visual apparatus;liver;kidney;pineal gland; trigeminal ganglion; 0.19726 . -0.372889896 28.20240623 184.42675 2.94725 ZNF496 0.983327487660117 0.0166704376624645 2.07467741807398e-06 zinc finger protein 496 FUNCTION: DNA-binding transcription factor that can both act as an activator and a repressor. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;cartilage;heart;muscle;colon;skin;uterus;pancreas;prostate;lung;bone;placenta;thyroid;visual apparatus;testis;cervix;amniotic fluid;brain;peripheral nerve; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;caudate nucleus;pons;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle; 0.23475 0.10285 -1.442099697 3.951403633 117.19384 2.35373 ZNF497 5.39461755578373e-08 0.0670849939905424 0.932914952063282 zinc finger protein 497 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;salivary gland;parathyroid;blood;skin;retina;uterus;breast;lung;bone;placenta;visual apparatus;testis;cervix;kidney;brain; . 0.20739 . . . 1826.97382 7.88215 ZNF500 0.000679411301142229 0.914577835181457 0.0847427535174012 zinc finger protein 500 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;blood;skin;retina;bone marrow;uterus;pancreas;lung;frontal lobe;endometrium;placenta;liver;spleen;brain;mammary gland;cerebellum; dorsal root ganglion;superior cervical ganglion;testis;globus pallidus;pons;trigeminal ganglion;skeletal muscle; 0.12543 . -0.905656269 10.12031139 119.3178 2.37708 ZNF501 0.00549805795272302 0.715271758300773 0.279230183746504 zinc finger protein 501 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);brain; dorsal root ganglion;subthalamic nucleus;testis - interstitial;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;parietal lobe;skeletal muscle; 0.12233 . 0.373041938 75.29488087 165.65011 2.81619 ZNF502 1.40776549102333e-05 0.631698761422303 0.368287160922787 zinc finger protein 502 FUNCTION: May be involved in transcriptional regulation.; . . choroid;fovea centralis;retina;uterus;prostate;optic nerve;whole body;endometrium;bone;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);cartilage;lens;skeletal muscle;lung;cornea;placenta;visual apparatus;macula lutea;alveolus;kidney;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13575 . 0.396906589 76.30927105 941.50042 5.94793 ZNF503 0.887882312685142 0.110917243348956 0.00120044396590236 zinc finger protein 503 FUNCTION: May function as a transcriptional repressor. {ECO:0000250}.; . . . . 0.92206 0.11115 . . 889.95494 5.81207 ZNF503-AS1 . . . ZNF503 antisense RNA 1 . . . . . . . . . . . ZNF503-AS2 . . . ZNF503 antisense RNA 2 . . . . . . . . . . . ZNF506 1.99612668014446e-08 0.0717935545848628 0.92820642545387 zinc finger protein 506 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.06229 . 0.284856336 71.40835103 186.62415 2.96655 ZNF507 0.885285923722225 0.114711882871161 2.1934066144058e-06 zinc finger protein 507 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;cochlea;endometrium;bone;testis;germinal center;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;nasopharynx;trabecular meshwork;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach;cerebellum; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis;ciliary ganglion; 0.48140 . -1.146380093 6.334041047 79.90234 1.88925 ZNF510 2.36025273380781e-09 0.1413385561898 0.858661441449947 zinc finger protein 510 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);islets of Langerhans;hypothalamus;developmental;pharynx;fovea centralis;choroid;lens;retina;prostate;optic nerve;whole body;lung;endometrium;macula lutea;duodenum;liver;testis;brain;stomach; dorsal root ganglion;superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;skin; 0.07005 . 1.003094668 90.77022883 1487.979 7.17873 ZNF511 0.0144447040829361 0.872393019866618 0.113162276050446 zinc finger protein 511 FUNCTION: May be involved in transcriptional regulation.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);heart;tongue;islets of Langerhans;pharynx;blood;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; globus pallidus;ciliary ganglion;atrioventricular node; 0.10324 . -0.117432389 44.89266336 118.83577 2.37171 ZNF511-PRAP1 . . . ZNF511-PRAP1 readthrough . . . . . . . . . . . ZNF512 0.949146986047491 0.0508527403490356 2.73603473352947e-07 zinc finger protein 512 FUNCTION: May be involved in transcriptional regulation.; . . ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;cochlea;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;lacrimal gland;tongue;islets of Langerhans;muscle;adrenal cortex;blood;lens;skeletal muscle;breast;lung;nasopharynx;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve;thymus; . 0.52372 . -0.868835007 10.65109696 24.19914 0.79483 ZNF512B 0.999557046056348 0.000442953884090087 5.95621088398581e-11 zinc finger protein 512B FUNCTION: May be involved in transcriptional regulation.; . . ovary;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;thyroid;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;cervix;spleen;head and neck;kidney; superior cervical ganglion; 0.32531 0.12351 -0.613589782 17.49823071 886.15061 5.79939 ZNF513 0.940738428263313 0.0592131083936853 4.84633430011949e-05 zinc finger protein 513 FUNCTION: Transcriptional regulator that plays a role in retinal development and maintenance. {ECO:0000269|PubMed:20797688}.; . TISSUE SPECIFICITY: In the retina, expressed in the outer and inner nuclear layers, and the ganglion cell layer. {ECO:0000269|PubMed:20797688}.; medulla oblongata;ovary;salivary gland;intestine;colon;parathyroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;larynx;bone;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);cartilage;heart;hypothalamus;pharynx;blood;lung;cornea;placenta;visual apparatus;duodenum;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . 0.50500 . -0.442665927 24.53408823 153.34627 2.70839 ZNF514 7.04681464876894e-09 0.0747882069490713 0.925211786004114 zinc finger protein 514 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);smooth muscle;heart;salivary gland;blood;fovea centralis;choroid;lens;vein;retina;bone marrow;uterus;prostate;optic nerve;lung;larynx;nasopharynx;thyroid;macula lutea;hippocampus;liver;head and neck;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.18022 . -0.291981272 33.20358575 53.57612 1.45569 ZNF516 0.26883020897488 0.730946184486341 0.000223606538779028 zinc finger protein 516 FUNCTION: Transcriptional regulator that binds to the promoter and activates the transcription of genes promoting brown adipose tissue (BAT) differentiation. Among brown adipose tissue-specific genes, binds the proximal region of the promoter of the UCP1 gene to activate its transcription and thereby regulate thermogenesis (By similarity). May also play a role in the cellular response to replication stress (PubMed:23446422). {ECO:0000250|UniProtKB:Q7TSH3, ECO:0000269|PubMed:23446422}.; . . . . 0.19134 0.10539 . . 285.13795 3.61446 ZNF517 2.00971919308343e-05 0.469655013492085 0.530324889315984 zinc finger protein 517 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lacrimal gland;endometrium;liver;spleen;brain; ciliary ganglion;parietal lobe; 0.14206 . -0.025608647 51.91672564 274.9235 3.55314 ZNF518A . . . zinc finger protein 518A FUNCTION: May be involved in transcriptional regulation.; . . . . 0.37126 0.08644 . . . . ZNF518B 0.591536151289667 0.408038434341956 0.000425414368376407 zinc finger protein 518B FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;whole body;cartilage;thyroid;placenta;kidney;germinal center;brain;skin;skeletal muscle; superior cervical ganglion; 0.13257 0.08374 0.657639543 84.20028309 1202.5769 6.57150 ZNF519 8.85353913956773e-07 0.308661045622523 0.691338069023563 zinc finger protein 519 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.11315 . 1.576373448 95.7537155 2768.09451 9.92908 ZNF519P1 . . . zinc finger protein 519 pseudogene 1 . . . . . . . . . . . ZNF519P2 . . . zinc finger protein 519 pseudogene 2 . . . . . . . . . . . ZNF519P3 . . . zinc finger protein 519 pseudogene 3 . . . . . . . . . . . ZNF519P4 . . . zinc finger protein 519 pseudogene 4 . . . . . . . . . . . ZNF521 0.999979350698415 2.06493007548964e-05 8.30485351574029e-13 zinc finger protein 521 FUNCTION: Transcription factor that can both act as an activator or a repressor depending on the context. Involved in BMP signaling and in the regulation of the immature compartment of the hematopoietic system. Associates with SMADs in response to BMP2 leading to activate transcription of BMP target genes. Acts as a transcriptional repressor via its interaction with EBF1, a transcription factor involved specification of B-cell lineage; this interaction preventing EBF1 to bind DNA and activate target genes. {ECO:0000269|PubMed:14630787}.; DISEASE: Note=A chromosomal aberration involving ZNF521 is found in acute lymphoblastic leukemia. Translocation t(9;18)(p13;q11.2) with PAX5. The translocation generates the PAX5-ZNF521 oncogene consisting of the N-terminus part of PAX5 and the C-terminus part of ZNF521. {ECO:0000269|PubMed:17344859}.; TISSUE SPECIFICITY: Predominantly expressed in hematopoietic cells. Present in organs and tissues that contain stem and progenitor cells, myeloid and/or lymphoid: placenta, spleen, lymph nodes, thymus, bone marrow and fetal liver. Within the hematopoietic system, it is abundant in CD34(+) cells but undetectable in mature peripheral blood leukocytes, and its levels rapidly decrease during the differentiation of CD34(+) cells in response to hemopoietins. {ECO:0000269|PubMed:14630787}.; ovary;parathyroid;fovea centralis;choroid;vein;skin;retina;optic nerve;whole body;cochlea;bone;pituitary gland;testis;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;cerebellum cortex;islets of Langerhans;lens;skeletal muscle;breast;lung;placenta;macula lutea;liver;spleen;head and neck;kidney; uterus;superior cervical ganglion;cerebellum peduncles;globus pallidus;cerebellum; 0.71744 0.10820 -1.767443354 2.317763623 91.92438 2.06319 ZNF524 0.006803764335491 0.521805009960842 0.471391225703667 zinc finger protein 524 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);prostate;optic nerve;lung;cartilage;ovary;islets of Langerhans;liver;colon;spleen;kidney;brain;stomach; . 0.65433 . 0.125076652 62.7388535 27.3918 0.88346 ZNF525 0.00129110751782178 0.856656613120305 0.142052279361873 zinc finger protein 525 FUNCTION: May be involved in transcriptional regulation.; . . . . . . . . 19.03117 0.65731 ZNF526 0.0681249940930755 0.918055254207707 0.0138197516992176 zinc finger protein 526 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;muscle;colon;blood;skin;skeletal muscle;bone marrow;uterus;prostate;lung;endometrium;bone;thyroid;placenta;visual apparatus;hippocampus;liver;testis;germinal center;brain;tonsil;stomach; superior cervical ganglion;pons;trigeminal ganglion; 0.29127 . -0.799052816 12.45576787 495.75833 4.57667 ZNF527 4.1248836635378e-05 0.841680864005852 0.158277887157512 zinc finger protein 527 FUNCTION: May be involved in transcriptional regulation.; . . bile duct;endometrium;testis;colon;choroid;kidney;brain;mammary gland;stomach;cerebellum; . 0.24310 . -0.201976964 38.98325077 96.90855 2.12795 ZNF528 1.01444599373916e-13 0.0106141189039061 0.989385881095992 zinc finger protein 528 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lymph node;lacrimal gland;salivary gland;skeletal muscle;skin;uterus;breast;prostate;whole body;lung;placenta;thyroid;visual apparatus;kidney;brain; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; . . 0.181903047 66.2361406 314.06037 3.76770 ZNF528-AS1 . . . ZNF528 antisense RNA 1 . . . . . . . . . . . ZNF529 0.00106713686759093 0.82736196518941 0.171570897942999 zinc finger protein 529 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);heart;blood;skin;retina;bone marrow;uterus;prostate;whole body;lung;cochlea;larynx;thyroid;testis;head and neck;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.14576 . -0.26993514 34.59542345 37.91119 1.12549 ZNF529-AS1 . . . ZNF529 antisense RNA 1 . . . . . . . . . . . ZNF530 1.74303796061719e-10 0.114407016262944 0.885592983562752 zinc finger protein 530 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);prostate;lung;blood; . 0.08489 . 1.820761234 97.009908 298.54254 3.68443 ZNF532 0.905138239772125 0.0948604227783298 1.33744954543409e-06 zinc finger protein 532 FUNCTION: May be involved in transcriptional regulation.; . . colon;skin;retina;uterus;prostate;frontal lobe;cerebral cortex;endometrium;larynx;thyroid;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);heart;cartilage;tongue;nervous;lens;skeletal muscle;breast;lung;placenta;visual apparatus;liver;head and neck;cervix;kidney;mammary gland;stomach; occipital lobe;subthalamic nucleus;superior cervical ganglion;temporal lobe;pons;atrioventricular node; 0.83679 0.10631 -1.387129737 4.322953527 1736.5006 7.69011 ZNF534 4.41308723445275e-14 0.00650937912803924 0.993490620871917 zinc finger protein 534 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . lung; . . . 2.976849182 99.20382166 686.664 5.23279 ZNF536 0.965216841600083 0.0347805724955092 2.58590440787304e-06 zinc finger protein 536 FUNCTION: May be involved in transcriptional regulation. Recognizes and binds 2 copies of the core DNA sequence 5'-CCCCCA- 3'.; . . unclassifiable (Anatomical System);amygdala;lens;brain;skin;retina; dorsal root ganglion;medulla oblongata;superior cervical ganglion;atrioventricular node;pons;trigeminal ganglion;cingulate cortex;parietal lobe;skeletal muscle; 0.12110 0.10961 -1.565353375 3.202406228 443.21726 4.38113 ZNF540 0.00697652985699623 0.975720558616874 0.0173029115261299 zinc finger protein 540 FUNCTION: May act as a transcriptional repressor. {ECO:0000269|PubMed:16815308}.; . TISSUE SPECIFICITY: Expressed in several fetal tissues, including gut, heart, brain, muscle, lung, testis and liver. {ECO:0000269|PubMed:16815308}.; unclassifiable (Anatomical System);lymph node;smooth muscle;heart;retina;frontal lobe;placenta;bone;liver;testis;spleen;kidney;brain;stomach;cerebellum; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.10612 0.08350 -0.955204708 9.170794999 2609.2525 9.55867 ZNF541 . . . zinc finger protein 541 FUNCTION: Component of some chromatin remodeling multiprotein complex that plays a role during spermatogenesis. {ECO:0000250|UniProtKB:Q0GGX2}.; . . unclassifiable (Anatomical System);lung;liver;testis;spleen;kidney;skin; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.22710 . 1.0178651 90.91766926 2245.80596 8.74850 ZNF542P . . . zinc finger protein 542, pseudogene FUNCTION: May be involved in transcriptional regulation.; . . . . 0.07772 . . . . . ZNF543 9.05589160091701e-12 0.020857684808949 0.979142315181995 zinc finger protein 543 FUNCTION: May be involved in transcriptional regulation.; . . breast;uterus;lung;frontal lobe;heart;nasopharynx;thyroid;kidney;brain; dorsal root ganglion;superior cervical ganglion;testis;ciliary ganglion;atrioventricular node;skeletal muscle; 0.09353 . 0.913082291 89.54352442 1483.15841 7.16715 ZNF544 3.81192076143802e-13 0.02304203047402 0.976957969525599 zinc finger protein 544 FUNCTION: May be involved in transcriptional regulation.; . . ovary;umbilical cord;retina;bone marrow;prostate;frontal lobe;oesophagus;endometrium;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;blood;skeletal muscle;bile duct;breast;pancreas;lung;placenta;liver;spleen;head and neck;stomach;cerebellum; dorsal root ganglion;subthalamic nucleus;testis - interstitial;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.64072 . 0.628293289 83.56923803 386.55325 4.14126 ZNF546 2.54471129517444e-10 0.439925614743031 0.560074385002498 zinc finger protein 546 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);breast;uterus;lung;islets of Langerhans;pituitary gland;testis;mammary gland; testis - interstitial;subthalamic nucleus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.16240 . 0.606246644 82.93229535 1927.87071 8.08022 ZNF547 2.11764938034053e-11 0.00484169638876898 0.995158303590055 zinc finger protein 547 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);uterus;frontal lobe;placenta;hippocampus;adrenal cortex;germinal center; . 0.15849 0.09796 -0.512444034 21.55579146 45.2927 1.29208 ZNF548 0.0995735434017802 0.89293658355491 0.00748987304330943 zinc finger protein 548 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lymph node;lung;thyroid;placenta;visual apparatus;liver;testis;spleen; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skin;skeletal muscle; 0.11129 . 0.396906589 76.30927105 197.7028 3.03971 ZNF549 5.83117375145472e-05 0.889719536663831 0.110222151598654 zinc finger protein 549 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lymph node;ovary;salivary gland;pharynx;colon;blood;skeletal muscle;breast;prostate;whole body;lung;frontal lobe;bone;thyroid;placenta;visual apparatus;liver;kidney;brain;bladder; superior cervical ganglion;atrioventricular node; 0.13625 . 0.510776592 80.23708422 159.36041 2.75797 ZNF550 1.52466918014378e-10 0.0154329316943823 0.984567068153151 zinc finger protein 550 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.13325 . 0.643056625 84.05284265 61.39768 1.59674 ZNF551 6.09496732792038e-07 0.438286636404635 0.561712754098632 zinc finger protein 551 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);heart;ovary;muscle;parathyroid;uterus;breast;lung;frontal lobe;placenta;thyroid;visual apparatus;testis;mammary gland;brain; . 0.05231 . 0.04598748 57.47817882 199.33421 3.05090 ZNF552 0.0119441082095416 0.848932860979253 0.139123030811205 zinc finger protein 552 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.10571 . 0.106667882 61.73036093 29.17592 0.93245 ZNF554 4.61366216735965e-06 0.631097072414047 0.368898313923786 zinc finger protein 554 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);uterus;prostate;heart;epididymis;placenta;sympathetic chain;colon;brain;skin; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;placenta;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14704 . 0.181903047 66.2361406 602.45676 4.96697 ZNF555 1.74413607005712e-09 0.383311937183855 0.616688061072009 zinc finger protein 555 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;whole body;ovary;heart;endometrium;tongue;placenta;testis;colon;parathyroid;brain;stomach; superior cervical ganglion;ciliary ganglion; 0.14293 . -0.753139731 13.67067705 34.27874 1.04905 ZNF556 1.57972888888797e-05 0.656794905382511 0.3431892973286 zinc finger protein 556 FUNCTION: May be involved in transcriptional regulation.; . . head and neck; subthalamic nucleus;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04643 . 1.447715105 95.14036329 218.62819 3.19678 ZNF557 1.50769654048194e-06 0.398872299105413 0.601126193198047 zinc finger protein 557 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);breast;lung;heart;hypothalamus;bone;thyroid;muscle;testis;kidney;germinal center;bone marrow; superior cervical ganglion;ciliary ganglion;skeletal muscle; 0.06637 0.06391 -0.179930907 40.35739561 78.21487 1.86530 ZNF558 0.000767127294544923 0.768778656705665 0.23045421599979 zinc finger protein 558 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);ovary;cerebellum cortex;islets of Langerhans;colon;skin;skeletal muscle;uterus;pancreas;lung;endometrium;bone;thyroid;visual apparatus;testis;cervix;germinal center;kidney;stomach; dorsal root ganglion;ciliary ganglion;atrioventricular node; 0.15725 0.09863 0.330767508 73.53739089 79.11796 1.87794 ZNF559 7.71788505951748e-09 0.147060009052863 0.852939983229252 zinc finger protein 559 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);heart;ovary;skin;uterus;whole body;frontal lobe;larynx;placenta;thyroid;testis;head and neck;germinal center;brain; superior cervical ganglion;ciliary ganglion;atrioventricular node; 0.16550 0.09459 0.734883636 86.29983487 612.47574 5.00195 ZNF559-ZNF177 . . . ZNF559-ZNF177 readthrough FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);prostate;lung;ovary;islets of Langerhans;placenta;parathyroid;kidney;brain;retina; superior cervical ganglion; . . 1.058333711 91.42486435 85.31343 1.96818 ZNF560 7.36420867683153e-10 0.665805222801801 0.334194776461779 zinc finger protein 560 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);bone;skin; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.15343 . -0.462894052 23.62585515 110.60062 2.29006 ZNF561 0.00976254715762805 0.941810474199631 0.0484269786427413 zinc finger protein 561 FUNCTION: May be involved in transcriptional regulation.; . . colon;fovea centralis;choroid;skin;bone marrow;retina;uterus;prostate;optic nerve;whole body;frontal lobe;oesophagus;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;blood;lens;skeletal muscle;breast;pancreas;adrenal gland;nasopharynx;placenta;macula lutea;liver;spleen;kidney;stomach; . . . -0.957024976 9.088228356 24.89171 0.81729 ZNF561-AS1 . . . ZNF561 antisense RNA 1 (head to head) . . . . . . . . . . . ZNF562 0.139679896104799 0.840663184135967 0.019656919759234 zinc finger protein 562 FUNCTION: May be involved in transcriptional regulation.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;thyroid;bone;testis;bladder;brain;unclassifiable (Anatomical System);lymph node;islets of Langerhans;pharynx;blood;lens;lung;nasopharynx;macula lutea;visual apparatus;liver;kidney;mammary gland;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.16052 . 0.573279816 82.08303845 60.61467 1.58233 ZNF563 8.58045673584715e-07 0.745959735198016 0.25403940675631 zinc finger protein 563 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;endometrium;hypothalamus;testis;colon;bone marrow; testis - interstitial;testis - seminiferous tubule;testis;pons;atrioventricular node; 0.19969 . -0.179930907 40.35739561 73.78661 1.79524 ZNF564 8.59098537312022e-05 0.929602645016865 0.0703114451294038 zinc finger protein 564 FUNCTION: May be involved in transcriptional regulation.; . . heart;ovary;salivary gland;intestine;pharynx;colon;blood;skin;retina;breast;uterus;prostate;lung;visual apparatus;pituitary gland;liver;kidney;brain;bladder; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.18832 . -0.47017169 23.25430526 61.90992 1.60412 ZNF565 0.00176668862893038 0.9732326175397 0.0250006938313693 zinc finger protein 565 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);medulla oblongata;ovary;islets of Langerhans;parathyroid;retina;bile duct;whole body;lung;larynx;nasopharynx;thyroid;placenta;liver;testis;head and neck;spleen; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;cerebellum; 0.20025 . -0.025608647 51.91672564 99.52546 2.15887 ZNF566 0.637363544825764 0.361232666001411 0.00140378917282562 zinc finger protein 566 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.22704 . -0.005381972 53.50908233 22.22962 0.74552 ZNF567 1.86506738570689e-06 0.439387474564322 0.560610660368293 zinc finger protein 567 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;thyroid;liver;skeletal muscle;retina; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;cingulate cortex; 0.64922 0.10176 -0.22584292 37.32012267 197.67313 3.03926 ZNF568 4.90822988396935e-09 0.369419684108196 0.630580310983574 zinc finger protein 568 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . meninges;pia mater;lung;dura mater;skin; . 0.14020 . . . 1744.11207 7.70841 ZNF569 3.32583134908488e-05 0.805961804511002 0.194004937175507 zinc finger protein 569 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);myocardium;heart;islets of Langerhans;skin;retina;uterus;lung;frontal lobe;endometrium;liver;pituitary gland;testis;cervix;germinal center;kidney;brain; ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.27508 0.11544 -0.824740496 11.67728238 31.42855 0.99120 ZNF570 0.0012328637860006 0.958398442818105 0.0403686933958946 zinc finger protein 570 FUNCTION: May be involved in transcriptional regulation.; . . cartilage;endometrium;bone;bone marrow; . 0.21459 . -0.093566408 46.7386176 63.63192 1.63442 ZNF571 2.82738476091202e-09 0.0837878002419782 0.916212196930637 zinc finger protein 571 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);smooth muscle;islets of Langerhans;sympathetic chain;fovea centralis;choroid;lens;skeletal muscle;retina;breast;pancreas;optic nerve;lung;placenta;macula lutea;liver;testis;spleen;bladder;brain; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.25462 . 1.469764896 95.28190611 6623.55637 17.18453 ZNF571-AS1 . . . ZNF571 antisense RNA 1 . . . . . . . . . . . ZNF572 0.000651450621070101 0.73668558546595 0.26266296391298 zinc finger protein 572 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . ovary;testis;retina; superior cervical ganglion;ciliary ganglion;pons;trigeminal ganglion;skeletal muscle; 0.16309 . 0.755110637 86.7539514 1412.2859 7.02157 ZNF573 9.43002239919919e-09 0.0882663887147602 0.911733601855217 zinc finger protein 573 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;heart;hypothalamus;muscle;brain; superior cervical ganglion;appendix;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.23507 . 0.088260113 60.56853031 1222.49938 6.60897 ZNF574 0.908434997009248 0.091535212340366 2.97906503858507e-05 zinc finger protein 574 FUNCTION: May be involved in transcriptional regulation.; . . lymphoreticular;ovary;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;larynx;thyroid;bone;testis;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;urinary;muscle;lens;breast;lung;placenta;macula lutea;visual apparatus;spleen;head and neck;kidney;stomach; dorsal root ganglion;testis;globus pallidus;atrioventricular node;skeletal muscle; 0.28700 . -2.035711952 1.669025714 735.35854 5.38048 ZNF575 0.456203449450325 0.516949428524449 0.0268471220252264 zinc finger protein 575 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);pancreas;thyroid;brain; subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.13918 . -0.229483771 36.86010852 61.92865 1.60476 ZNF576 0.007545747912442 0.543593512126608 0.44886073996095 zinc finger protein 576 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;adrenal cortex;colon;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;prostate;optic nerve;whole body;lung;macula lutea;liver;testis;spleen;kidney;brain;stomach;peripheral nerve; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;globus pallidus;atrioventricular node;skeletal muscle;cingulate cortex; 0.11300 . 0.281220278 71.07808445 233.71185 3.30378 ZNF577 0.0129413215619512 0.953743723464092 0.033314954973957 zinc finger protein 577 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);islets of Langerhans;parathyroid;blood;skin;bone marrow;breast;prostate;whole body;lung;frontal lobe;cochlea;endometrium;thyroid;liver;testis;spleen;kidney;aorta; dorsal root ganglion;testis - interstitial;testis - seminiferous tubule;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.10716 . 1.489991751 95.35857514 3127.20421 10.63952 ZNF578 8.81006386925896e-14 0.00263912078378526 0.997360879216127 zinc finger protein 578 FUNCTION: May be involved in transcriptional regulation.; . . . . . . 1.047190339 91.34229771 336.42783 3.89648 ZNF579 . . . zinc finger protein 579 FUNCTION: May be involved in transcriptional regulation.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;testis;bladder;brain;unclassifiable (Anatomical System);heart;pharynx;blood;lens;lung;macula lutea;visual apparatus;liver;duodenum;kidney;stomach; . 0.33467 . . . 142.33955 2.60280 ZNF580 0.508634074661298 0.422098207708365 0.0692677176303375 zinc finger protein 580 FUNCTION: Involved in the regulation of endothelial cell proliferation and migration. Mediates H(2)O(2)-induced leukocyte chemotaxis by elevating interleukin-8 production and may play a role in inflammation. May be involved in transcriptional regulation. {ECO:0000269|PubMed:20382120, ECO:0000269|PubMed:21830064}.; . TISSUE SPECIFICITY: Expressed in endothelial cells. {ECO:0000269|PubMed:21599657}.; unclassifiable (Anatomical System);cartilage;heart;ovary;islets of Langerhans;colon;blood;lens;vein;skin;retina;uterus;pancreas;prostate;optic nerve;lung;endometrium;bone;placenta;germinal center;brain;stomach; amygdala;thyroid;caudate nucleus;cingulate cortex; 0.35324 . . . 155.58583 2.72582 ZNF581 0.0645550031379347 0.728112700656264 0.207332296205801 zinc finger protein 581 FUNCTION: May be involved in transcriptional regulation.; . . ovary;salivary gland;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;hypothalamus;muscle;lens;bile duct;pancreas;lung;placenta;macula lutea;liver;spleen;cervix;kidney;mammary gland;stomach;aorta; . 0.15716 0.10745 -0.339715008 30.06605331 4.9347 0.18323 ZNF582 0.000410370551964526 0.95981137256618 0.039778256881856 zinc finger protein 582 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);ovary;heart;salivary gland;intestine;pharynx;colon;parathyroid;blood;skin;breast;prostate;lung;cornea;placenta;visual apparatus;liver;testis;spleen;kidney;brain;mammary gland;bladder; dorsal root ganglion;superior cervical ganglion;ciliary ganglion; 0.14536 0.10093 -0.402212257 26.7338995 145.93455 2.63282 ZNF582-AS1 . . . ZNF582 antisense RNA 1 (head to head) . . . . . . . . . . . ZNF583 0.37696074589281 0.620781470330979 0.00225778377621126 zinc finger protein 583 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);uterus;lung;liver;testis;spleen;skin; . 0.13637 . -0.249709319 35.74545883 22.77727 0.76136 ZNF584 1.31169156351203e-05 0.387470873196501 0.612516009887864 zinc finger protein 584 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;adrenal cortex;colon;parathyroid;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;pancreas;optic nerve;whole body;lung;adrenal gland;bone;placenta;macula lutea;testis;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; . . -0.268115223 34.70747818 2597.68755 9.54265 ZNF585A 0.711326551856647 0.288533097503367 0.000140350639986282 zinc finger protein 585A FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;choroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;whole body;optic nerve;endometrium;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;cartilage;islets of Langerhans;blood;lens;skeletal muscle;breast;lung;epididymis;nasopharynx;placenta;macula lutea;liver;kidney;mammary gland; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.28155 . 0.823072022 88.03963199 573.58849 4.86096 ZNF585B 0.00569166584170305 0.989456274335462 0.00485205982283547 zinc finger protein 585B FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);fovea centralis;choroid;lens;retina;breast;prostate;optic nerve;lung;nasopharynx;placenta;bone;macula lutea;liver;testis;bladder;stomach; superior cervical ganglion;pons;trigeminal ganglion;skeletal muscle; 0.18664 0.09507 0.091899012 60.68058504 1939.17005 8.10312 ZNF586 0.00501217619840313 0.886229088791392 0.108758735010205 zinc finger protein 586 FUNCTION: May be involved in transcriptional regulation.; . . colon;mammary gland; . 0.03146 . 0.084621747 60.31493277 15.74945 0.56175 ZNF587 0.000253450002154461 0.926784132593743 0.0729624174041024 zinc finger protein 587 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;bone marrow;uterus;prostate;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;urinary;blood;skeletal muscle;lung;placenta;liver;head and neck;spleen;kidney;mammary gland;stomach; . 0.09837 0.07556 0.50895761 80.20169851 867.89579 5.73820 ZNF587B 0.00809264304487427 0.788598540032056 0.20330881692307 zinc finger protein 587B FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}.; . . . . . . . . 136.17307 2.53579 ZNF587P1 . . . zinc finger protein 587 pseudogene 1 . . . . . . . . . . . ZNF589 6.50060605876318e-07 0.450995757724531 0.549003592214863 zinc finger protein 589 FUNCTION: May play a role in hematopoietic stem/progenitor cell differentiation. May play a role as a DNA binding-dependent transcriptional repressor. {ECO:0000269|PubMed:10029171, ECO:0000269|PubMed:12097288}.; . TISSUE SPECIFICITY: Isoform 2 is widely expressed. Isoform 3 is only expressed in CD34(+) cells. {ECO:0000269|PubMed:10029171}.; ovary;colon;fovea centralis;choroid;skin;retina;prostate;optic nerve;frontal lobe;endometrium;larynx;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);islets of Langerhans;muscle;lens;epididymis;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;kidney;mammary gland;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.22427 0.08201 -0.115612493 45.12856806 884.06277 5.79096 ZNF592 0.949422558472883 0.0505761077633972 1.33376371977733e-06 zinc finger protein 592 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Widely expressed, with highest levels in skeletal muscle. Expressed throughout the central nervous system, including in the cerebellum and cerebellar vermis, with higher expression in the substantia nigra. Widely expressed in fetal tissues. {ECO:0000269|PubMed:20531441}.; colon;skin;bone marrow;uterus;prostate;larynx;thyroid;bone;testis;germinal center;brain;bladder;tonsil;unclassifiable (Anatomical System);lymph node;islets of Langerhans;breast;pancreas;lung;epididymis;placenta;liver;alveolus;spleen;head and neck;mammary gland;stomach; superior cervical ganglion;globus pallidus;atrioventricular node;caudate nucleus;trigeminal ganglion;skeletal muscle;cerebellum; 0.33506 0.10238 -1.833605934 2.087756546 4331.56505 13.09959 ZNF593 0.156440973665101 0.775690893674412 0.0678681326604875 zinc finger protein 593 FUNCTION: Negatively modulates the DNA binding activity of Oct-2 and therefore its transcriptional regulatory activity. Could act either by binding to DNA octamer or by interacting with Oct-2. May also be a modulator of other octamer-binding proteins.; . TISSUE SPECIFICITY: Ubiquitous. Detected in spleen, prostate, testis, small intestine, colon and to a minor level in thymus and peripheral blood leukocytes.; ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;testis;germinal center;brain;pineal gland;bladder;tonsil;unclassifiable (Anatomical System);lymph node;heart;hypothalamus;muscle;urinary;pharynx;blood;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; superior cervical ganglion;subthalamic nucleus;liver;trigeminal ganglion;skeletal muscle; 0.25976 . . . 113.52198 2.32026 ZNF594 1.13967591329678e-10 0.0249509797861339 0.975049020099898 zinc finger protein 594 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . 0.05677 . 1.183126933 92.82849729 1073.7562 6.28189 ZNF595 1.77527172321732e-05 0.143155705654596 0.856826541628172 zinc finger protein 595 FUNCTION: May be involved in transcriptional regulation.; . . pancreas;placenta; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.28695 . . . 21.10844 0.71426 ZNF596 2.89554865880379e-14 0.0097712602304777 0.990228739769493 zinc finger protein 596 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);heart;islets of Langerhans;larynx;placenta;amnion;testis;head and neck;skeletal muscle; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;testis - interstitial;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.13873 . 0.312359769 72.71172446 1489.35557 7.17989 ZNF597 0.134235996654177 0.844707695578348 0.0210563077674758 zinc finger protein 597 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;ovary;nasopharynx;placenta;hippocampus;testis;germinal center;brain;mammary gland;skin;skeletal muscle; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.12857 . 0.242582624 69.45623968 223.11294 3.22982 ZNF598 0.201673229572794 0.797908511572544 0.000418258854661596 zinc finger protein 598 . . . . . 0.45123 . . . 1782.44951 7.79441 ZNF599 4.70007785154845e-07 0.618316339206764 0.381683190785451 zinc finger protein 599 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;choroid;fovea centralis;skin;bone marrow;retina;uterus;prostate;optic nerve;endometrium;bone;testis;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;lung;placenta;visual apparatus;macula lutea;kidney;mammary gland; superior cervical ganglion;globus pallidus;ciliary ganglion;skeletal muscle; 0.10470 . 1.423841958 94.96933239 290.07519 3.64519 ZNF600 1.47729480515385e-13 0.00185801960968 0.998141980390172 zinc finger protein 600 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);cartilage;nasopharynx;colon;bladder;stomach; . 0.89954 . 1.339294051 94.29700401 502.15644 4.59647 ZNF601P . . . zinc finger protein 601, pseudogene . . . . . . . . . . . ZNF602P . . . zinc finger protein 602, pseudogene . . . . . . . . . . . ZNF603P . . . zinc finger protein 603, pseudogene . . . . . . . . . . . ZNF605 0.960905074648588 0.0390108546500029 8.40707014094551e-05 zinc finger protein 605 FUNCTION: May be involved in transcriptional regulation.; . . myocardium;ovary;parathyroid;choroid;skin;retina;uterus;prostate;whole body;optic nerve;atrium;gum;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;skeletal muscle;lung;placenta;liver;spleen;head and neck;kidney;stomach;peripheral nerve; dorsal root ganglion;superior cervical ganglion;medulla oblongata;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;parietal lobe;skeletal muscle; 0.18281 . . . 12.20081 0.44211 ZNF606 0.320389649972156 0.678892835212747 0.000717514815097364 zinc finger protein 606 FUNCTION: May act as a transcriptional repressor. {ECO:0000269|PubMed:15964554}.; . TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues. {ECO:0000269|PubMed:15964554}.; unclassifiable (Anatomical System);heart;cartilage;colon;blood;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;prostate;optic nerve;lung;macula lutea;visual apparatus;liver;testis;head and neck;germinal center;kidney;spinal ganglion;brain; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe;skin; 0.21241 0.08684 -0.819281839 11.93677754 917.75858 5.88894 ZNF607 8.48062246875504e-08 0.489348059100133 0.510651856093643 zinc finger protein 607 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);ovary;colon;uterus;prostate;lung;frontal lobe;endometrium;epididymis;liver;testis;spleen;germinal center;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion; 0.20905 0.10006 -0.064242613 48.844067 1595.14788 7.38656 ZNF608 0.999968158467997 3.18415296182291e-05 2.38501180288726e-12 zinc finger protein 608 . . . unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;islets of Langerhans;colon;parathyroid;skin;skeletal muscle;breast;uterus;prostate;lung;frontal lobe;larynx;bone;thyroid;placenta;testis;head and neck;germinal center;kidney;brain;stomach; . 0.17709 0.11646 -2.162653931 1.433121019 135.02857 2.52784 ZNF609 0.999945906955907 5.40930423382896e-05 1.75467065175927e-12 zinc finger protein 609 . . . unclassifiable (Anatomical System);urinary;colon;skin;skeletal muscle;uterus;prostate;lung;larynx;epididymis;nasopharynx;bone;thyroid;visual apparatus;hypopharynx;liver;testis;head and neck;germinal center;brain;mammary gland;stomach; superior cervical ganglion;liver;pons;trigeminal ganglion;parietal lobe;skeletal muscle;cingulate cortex;cerebellum; 0.93593 0.10647 -2.583601763 0.831564048 156.28545 2.73248 ZNF610 1.22048067047747e-10 0.0259679562656998 0.974032043612252 zinc finger protein 610 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);breast;uterus;lung;heart;endometrium;islets of Langerhans;adrenal medulla;testis;brain;skin;retina; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule; 0.19902 . 1.332002318 94.20853975 75.23928 1.81442 ZNF611 1.16412309838076e-17 0.0001883163944438 0.999811683605556 zinc finger protein 611 FUNCTION: May be involved in transcriptional regulation.; . . spleen;head and neck;skeletal muscle; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;skin;cingulate cortex; 0.14705 . 0.806491657 87.72705827 2377.17021 9.04647 ZNF613 0.000362473926057268 0.952926395058685 0.0467111310152579 zinc finger protein 613 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);ovary;colon;parathyroid;fovea centralis;skin;uterus;prostate;whole body;lung;endometrium;nasopharynx;placenta;bone;macula lutea;kidney; dorsal root ganglion;superior cervical ganglion;trigeminal ganglion; 0.46057 . 0.132352165 63.48785091 125.63359 2.44011 ZNF614 0.00212062774091326 0.978395233412215 0.0194841388468714 zinc finger protein 614 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);ovary;islets of Langerhans;colon;parathyroid;skeletal muscle;skin;uterus;prostate;lung;frontal lobe;endometrium;placenta;testis;germinal center;brain;bladder;aorta;thymus; . . . 0.755110637 86.7539514 527.51752 4.68699 ZNF615 6.52907887791795e-12 0.216418594437276 0.783581405556194 zinc finger protein 615 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;skeletal muscle;skin;uterus;breast;prostate;cervix;germinal center;mammary gland;brain; superior cervical ganglion;medulla oblongata;trigeminal ganglion;parietal lobe;skeletal muscle; 0.16955 . 0.490549924 79.54706299 3355.61036 11.10053 ZNF616 1.06818277142656e-08 0.31388262995624 0.686117359361933 zinc finger protein 616 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.29743 . 0.492370491 79.60603916 226.63568 3.25371 ZNF618 0.994715996591424 0.00528397826558379 2.51429924704017e-08 zinc finger protein 618 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);islets of Langerhans;fovea centralis;choroid;lens;retina;optic nerve;whole body;larynx;visual apparatus;macula lutea;alveolus;head and neck;brain;stomach; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.16559 0.11112 -2.478673049 0.96131163 109.14077 2.26792 ZNF619 2.36447989133731e-05 0.741517408634249 0.258458946566838 zinc finger protein 619 FUNCTION: May be involved in transcriptional regulation.; . . breast;lung;hippocampus;liver;spleen; superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;atrioventricular node;skin; 0.06400 . -0.376526807 28.10804435 636.89204 5.07707 ZNF619P1 . . . zinc finger protein 619 pseudogene 1 . . . . . . . . . . . ZNF620 6.82676319543398e-06 0.715071728254089 0.284921444982715 zinc finger protein 620 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);breast;lung;visual apparatus;testis;brain;bladder; . 0.10981 . 0.350995466 74.37485256 198.29097 3.04284 ZNF621 4.17647812895176e-05 0.626149976148082 0.373808259070629 zinc finger protein 621 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);uterus;prostate;frontal lobe;heart;visual apparatus;skin;stomach;retina; globus pallidus; 0.09715 . -0.690637458 15.12149092 67.77652 1.70323 ZNF622 0.0888038528384209 0.90932895957551 0.00186718758606877 zinc finger protein 622 FUNCTION: May behave as an activator of the bound transcription factor, MYBL2, and be involved in embryonic development.; . TISSUE SPECIFICITY: Expressed in lung, kidney, spleen, liver and brain with lowest expression in kidney. {ECO:0000269|PubMed:11802789}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;thyroid;iris;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;hypothalamus;pineal body;pharynx;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;visual apparatus;liver;hypopharynx;spleen;head and neck;cervix;kidney;mammary gland;stomach;cerebellum; liver;ciliary ganglion; 0.07800 0.10409 -0.315847836 31.68789809 88.55059 2.01808 ZNF623 0.0941970020128073 0.868352066400991 0.0374509315862017 zinc finger protein 623 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;bone marrow;lung;cornea;placenta;visual apparatus;duodenum;liver;kidney;brain;mammary gland; . 0.04190 . 0.154398214 64.73814579 44.52782 1.27656 ZNF624 0.0003058625626781 0.986568877260181 0.0131252601771406 zinc finger protein 624 FUNCTION: May be involved in transcriptional regulation.; . . lung;ovary;endometrium;placenta;testis;colon;parathyroid;kidney; . 0.14551 . -0.290161348 33.33923095 2684.49322 9.74097 ZNF625 0.000825561501317101 0.932083417488517 0.0670910210101662 zinc finger protein 625 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.18836 . 0.281220278 71.07808445 444.69337 4.38783 ZNF625-ZNF20 . . . ZNF625-ZNF20 readthrough (NMD candidate) . . . . . 0.18836 . . . . . ZNF626 2.3449662444854e-07 0.153291770505267 0.846707994998109 zinc finger protein 626 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);uterus; . . 0.07312 0.777157784 87.17857985 611.05781 4.99634 ZNF627 0.00564414625423386 0.989445166015658 0.00491068773010817 zinc finger protein 627 FUNCTION: May be involved in transcriptional regulation.; . . ovary;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;bone;pituitary gland;testis;brain;bladder;pineal gland;unclassifiable (Anatomical System);heart;islets of Langerhans;pharynx;blood;lens;breast;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;stomach; . 0.20136 0.10503 -0.424258538 25.56027365 57.87877 1.53812 ZNF628 0.986868379237943 0.0131259225708874 5.69819116960667e-06 zinc finger protein 628 FUNCTION: Transcription activator. Binds DNA on GT-box consensus sequence 5'-TTGGTT-3' (By similarity). {ECO:0000250}.; . . . . 0.08108 . . . 565.06529 4.82708 ZNF629 0.992317751805668 0.00768071563520145 1.53255913041821e-06 zinc finger protein 629 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);uterus;lung;duodenum;spleen;brain;skeletal muscle; superior cervical ganglion;pons;skeletal muscle;parietal lobe; 0.27611 . 0.040529541 57.15380986 147.65212 2.64791 ZNF630 0.00223023467855748 0.75915889303004 0.238610872291403 zinc finger protein 630 FUNCTION: May be involved in transcriptional regulation.; . . prostate;placenta;brain; . . . 1.197888504 92.95234725 158.90767 2.75378 ZNF630-AS1 . . . ZNF630 antisense RNA 1 . . . . . . . . . . . ZNF638 0.999959949685778 4.00503142221975e-05 5.79125430306385e-17 zinc finger protein 638 FUNCTION: Early regulator of adipogenesis that works as a transcription cofactor of CEBPs, controlling the expression of PPARG and probably of other proadipogenic genes, such as SREBF1 (By similarity). Binds to cytidine clusters in double-stranded DNA. {ECO:0000250, ECO:0000269|PubMed:8647861}.; . . ovary;skin;bone marrow;retina;prostate;optic nerve;ganglion;endometrium;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;cerebral cortex;larynx;bone;pituitary gland;testis;spinal ganglion;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;nasopharynx;placenta;head and neck;kidney;aorta;stomach; amygdala;medulla oblongata;occipital lobe;hypothalamus;caudate nucleus;pons;atrioventricular node;skeletal muscle;prefrontal cortex;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex;parietal lobe; 0.53078 0.09373 -1.600473032 3.01958009 4929.35469 14.30986 ZNF638-IT1 . . . ZNF638 intronic transcript 1 . . . . . . . . . . . ZNF639 0.122945965165128 0.852618238360585 0.0244357964742864 zinc finger protein 639 FUNCTION: Binds DNA and may function as a transcriptional repressor. {ECO:0000269|PubMed:16182284}.; . . lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;larynx;thyroid;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;hypothalamus;adrenal cortex;blood;lens;breast;lung;adrenal gland;placenta;macula lutea;liver;head and neck;kidney; superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.24331 0.12242 0.106667882 61.73036093 221.2714 3.21769 ZNF641 0.228415943182732 0.769999011095555 0.00158504572171253 zinc finger protein 641 FUNCTION: Transcriptional activator. Activates transcriptional activities of SRE and AP-1. {ECO:0000269|PubMed:16343441}.; . TISSUE SPECIFICITY: Highly expressed in skeletal muscle, moderate expression in heart, liver, and pancreas, lower expression in placenta, no expression seen in brain, lung, and kidney. {ECO:0000269|PubMed:16343441}.; ovary;parathyroid;fovea centralis;choroid;bone marrow;retina;uterus;optic nerve;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;adrenal cortex;blood;lens;breast;lung;placenta;macula lutea;liver;spleen;kidney;stomach; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;adrenal gland;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin;skeletal muscle;cerebellum; 0.27422 . 0.350995466 74.37485256 1731.94482 7.67968 ZNF644 0.997328579642784 0.00267141939486352 9.62352033081596e-10 zinc finger protein 644 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Expressed in liver, placenta, retina and retinal pigment epithelium. {ECO:0000269|PubMed:21695231}.; ovary;skin;prostate;frontal lobe;cochlea;thyroid;amniotic fluid;germinal center;brain;bladder;heart;cartilage;tongue;urinary;adrenal cortex;pharynx;blood;skeletal muscle;breast;trabecular meshwork;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;uterus;whole body;bone;testis;dura mater;unclassifiable (Anatomical System);meninges;lymph node;islets of Langerhans;bile duct;pancreas;pia mater;lung;cornea;nasopharynx;placenta;hippocampus;duodenum;head and neck;kidney;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.53447 0.10345 -0.323344668 30.9447983 421.4331 4.28537 ZNF645 0.016465619897393 0.886130683772326 0.097403696330281 zinc finger protein 645 FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. May operate on tyrosine-phosphorylated SRC substrates. {ECO:0000269|PubMed:22252131}.; . TISSUE SPECIFICITY: Exclusively expressed in testis and sperm, including spermatocytes, round and elongated spermatids, and Leydig cells. {ECO:0000269|PubMed:20657603}.; lung;testis; . 0.04421 . 1.15197334 92.52182118 457.64824 4.44184 ZNF646 0.00556536047832854 0.994392619300942 4.20202207293e-05 zinc finger protein 646 FUNCTION: May be involved in transcriptional regulation.; . . lymphoreticular;medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;heart;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;visual apparatus;kidney;mammary gland;stomach; superior cervical ganglion;testis;atrioventricular node;trigeminal ganglion; 0.26454 0.09605 0.229465655 68.54800661 5474.89422 15.24912 ZNF646P1 . . . zinc finger protein 646 pseudogene 1 . . . . . . . . . . . ZNF648 8.27115198132611e-06 0.516352499709992 0.483639229138027 zinc finger protein 648 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);iris; ciliary ganglion;atrioventricular node;trigeminal ganglion;skin; 0.16891 . 0.663285274 84.55414013 585.73098 4.90882 ZNF649 0.711121457966851 0.28818666012432 0.000691881908829216 zinc finger protein 649 FUNCTION: Transcriptional repressor. Regulator of transcriptional factor complexes and may suppress SRE and AP-1 transcription activities mediated by growth factor signaling pathways. {ECO:0000269|PubMed:15950191}.; . TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, and brain. Lower expression in liver, lung, kidney, pancreas and placenta. {ECO:0000269|PubMed:15950191}.; ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;endometrium;iris;pituitary gland;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);heart;cartilage;muscle;pharynx;blood;lens;breast;lung;macula lutea;visual apparatus;liver;head and neck;kidney; dorsal root ganglion;superior cervical ganglion; 0.38453 . 0.753291803 86.71266808 125.61305 2.43972 ZNF649-AS1 . . . ZNF649 antisense RNA 1 . . . . . . . . . . . ZNF652 0.970739626335692 0.0292193944335467 4.0979230761722e-05 zinc finger protein 652 FUNCTION: Functions as a transcriptional repressor. {ECO:0000269|PubMed:16966434}.; . TISSUE SPECIFICITY: Widely expressed with higher expression in breast, prostate, vulva and pancreas. {ECO:0000269|PubMed:16966434}.; ovary;salivary gland;intestine;colon;skin;retina;bone marrow;uterus;prostate;frontal lobe;thyroid;testis;brain;unclassifiable (Anatomical System);heart;spinal cord;pharynx;blood;skeletal muscle;breast;lung;cornea;nasopharynx;visual apparatus;liver;spleen;kidney;mammary gland; amygdala;prostate;trachea;white blood cells; 0.23128 0.11223 -0.113792788 45.25831564 192.25722 3.00542 ZNF652P1 . . . zinc finger protein 652 pseudogene 1 . . . . . . . . . . . ZNF653 0.142112312658903 0.853857588172756 0.00403009916834093 zinc finger protein 653 FUNCTION: Transcriptional repressor. May repress NR5A1, PPARG, NR1H3, NR4A2, ESR1 and NR3C1 transcriptional activity. {ECO:0000269|PubMed:12920234}.; . TISSUE SPECIFICITY: Highly expressed in testis, cerebellum, temporal lobe, hippocampus and the adrenal gland. Moderately expressed in spleen, uterus, thymus, pancreas, kidney, stomach and rectum.; unclassifiable (Anatomical System);heart;ovary;colon;parathyroid;fovea centralis;choroid;lens;retina;optic nerve;lung;placenta;macula lutea;visual apparatus;testis;germinal center;kidney;brain;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis - interstitial;ciliary ganglion;atrioventricular node;cerebellum; 0.26913 0.10870 -0.108334733 45.57088936 233.95812 3.30616 ZNF654 0.947346014675446 0.0524772973291626 0.000176687995391259 zinc finger protein 654 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;heart;ovary;parathyroid;fovea centralis;choroid;lens;skin;skeletal muscle;retina;uterus;breast;optic nerve;lung;bone;placenta;macula lutea;alveolus;liver;head and neck;germinal center;kidney;brain; superior cervical ganglion;appendix;pons;atrioventricular node;parietal lobe; 0.51103 . 0.68351529 85.03774475 285.1098 3.61344 ZNF655 0.0378918199572815 0.92907742005896 0.0330307599837587 zinc finger protein 655 FUNCTION: May be involved in transcriptional regulation.; . . smooth muscle;ovary;colon;parathyroid;skin;bone marrow;uterus;prostate;whole body;cochlea;cerebral cortex;endometrium;larynx;bone;thyroid;pituitary gland;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;blood;skeletal muscle;greater omentum;breast;pancreas;lung;placenta;visual apparatus;liver;alveolus;head and neck;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion; 0.11089 0.11195 1.001272896 90.72304789 231.60888 3.28908 ZNF658 . . . zinc finger protein 658 FUNCTION: Mediates transcriptional repression in response to zinc. Represses several genes, including SLC30A5, SLC30A10 and CBWD1, by binding to the zinc transcriptional regulatory element (ZTRE) (5'- C[AC]C[TAG]CC[TC]-N(0-50)-[GA]G[ATC]G[TG]G-3') found in the promoter region. May play a role in the control of ribosome biogenesis, regulating predominantly rRNA levels, as well as those of several ribosomal proteins, thus coordinating this highly zinc- demanding process with the available zinc supply. {ECO:0000269|PubMed:25582195}.; . . . . 0.16425 . . . 865.67771 5.73155 ZNF658B . . . zinc finger protein 658B (pseudogene) FUNCTION: May be involved in transcriptional regulation.; . . . . . . . . . . ZNF660 0.0548051045454931 0.864553972887021 0.080640922567486 zinc finger protein 660 FUNCTION: May be involved in transcriptional regulation.; . . brain; atrioventricular node;trigeminal ganglion;parietal lobe; 0.22829 . -0.049474214 50.01179523 38.89898 1.15233 ZNF662 3.7181666705829e-10 0.0495728961438168 0.950427103484367 zinc finger protein 662 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . uterus;prostate;lung;bone;placenta;brain; dorsal root ganglion;superior cervical ganglion;testis - interstitial;pons;atrioventricular node;skeletal muscle;subthalamic nucleus;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;trigeminal ganglion;cingulate cortex; 0.07431 . 0.531004228 80.87992451 93.52543 2.08144 ZNF663P . . . zinc finger protein 663, pseudogene . . . . . 0.08349 . . . . . ZNF664 0.0016267937964256 0.457661201786404 0.540712004417171 zinc finger protein 664 FUNCTION: May be involved in transcriptional regulation.; . . smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;thyroid;iris;bladder;brain;amygdala;heart;cartilage;pineal body;pharynx;blood;lens;breast;macula lutea;visual apparatus;liver;cervix;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;larynx;synovium;bone;testis;unclassifiable (Anatomical System);lymph node;cerebellum cortex;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;hypopharynx;head and neck;kidney;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;trigeminal ganglion; 0.24976 0.12378 0.347360312 73.97381458 461.1138 4.45297 ZNF665 7.68094194219911e-08 0.469045165361927 0.530954757828653 zinc finger protein 665 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.17642 . 0.958999345 90.17456947 110.20868 2.28291 ZNF667 0.000142442783684959 0.962802825224773 0.0370547319915423 zinc finger protein 667 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);blood;skeletal muscle;bone marrow;retina;prostate;lung;bone;visual apparatus;liver;pituitary gland;testis;kidney;brain;stomach; superior cervical ganglion;subthalamic nucleus;caudate nucleus;cingulate cortex; 0.16209 0.09199 0.112125503 62.09601321 1388.50323 6.97374 ZNF667-AS1 . . . ZNF667 antisense RNA 1 (head to head) . . . . . . . . . . . ZNF668 0.26889237334633 0.725742260770841 0.00536536588282926 zinc finger protein 668 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;lung;placenta;macula lutea;duodenum;hypopharynx;liver;head and neck;kidney;stomach;thymus; trigeminal ganglion; 0.18315 . -0.512444034 21.55579146 340.33219 3.91395 ZNF669 0.0604993991526988 0.922901132696027 0.0165994681512743 zinc finger protein 669 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.05547 . 0.97558591 90.37508846 1414.66175 7.02829 ZNF670 0.451260083419079 0.542532916081455 0.00620700049946585 zinc finger protein 670 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.07638 . -0.538132194 20.26421326 23.4153 0.78072 ZNF670-ZNF695 . . . ZNF670-ZNF695 readthrough (NMD candidate) . . . . . 0.07638 . . . . . ZNF671 4.2192652974031e-13 0.0127498355301506 0.987250164469427 zinc finger protein 671 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);heart;ovary;parathyroid;blood;fovea centralis;choroid;lens;skeletal muscle;retina;uterus;optic nerve;lung;cochlea;endometrium;thyroid;placenta;macula lutea;liver;testis;spleen;kidney;mammary gland; subthalamic nucleus;trigeminal ganglion;parietal lobe; 0.06972 . -0.312207497 32.05944798 627.72143 5.04999 ZNF672 0.000127541106455286 0.626900007097441 0.372972451796104 zinc finger protein 672 FUNCTION: May be involved in transcriptional regulation.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;larynx;bone;testis;germinal center;brain;pineal gland;tonsil;gall bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;muscle;blood;lens;skeletal muscle;breast;pancreas;lung;nasopharynx;placenta;macula lutea;visual apparatus;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.31122 . . . 21.60164 0.72631 ZNF674 0.00427494121454892 0.866388314073246 0.129336744712206 zinc finger protein 674 FUNCTION: May be involved in transcriptional regulation.; . TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:16385466}.; . . 0.21534 . 1.039913547 91.25973107 53.12658 1.44669 ZNF674-AS1 . . . ZNF674 antisense RNA 1 (head to head) . . . . . . . . . . . ZNF675 3.87871887390171e-06 0.819207151619033 0.180788969662093 zinc finger protein 675 FUNCTION: May be involved in transcriptional regulation. May play a role during osteoclast differentiation by modulating TRAF6 signaling activity.; . . pituitary gland;colon;skeletal muscle;stomach; superior cervical ganglion;appendix;pons;atrioventricular node;trigeminal ganglion; 0.11487 0.08553 -0.001743238 53.85114414 1272.94283 6.71918 ZNF676 1.6869849435551e-06 0.419977197881765 0.580021115133291 zinc finger protein 676 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.09969 . 0.799205007 87.58551545 3460.6423 11.31757 ZNF677 6.08993693565877e-07 0.255247168440875 0.744752222565431 zinc finger protein 677 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);uterus;lung;bone; . 0.15332 . -0.220384297 37.6032083 148.40467 2.65568 ZNF678 4.66546659354214e-07 0.22208404162209 0.77791549183125 zinc finger protein 678 FUNCTION: May be involved in transcriptional regulation.; . . breast; medulla oblongata;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19605 . . . 258.61102 3.45659 ZNF679 1.4326770609757e-09 0.0298180327913735 0.97018196577595 zinc finger protein 679 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System); . 0.06744 . 1.903532842 97.3519698 2627.76478 9.61520 ZNF680 4.59084206576754e-06 0.398998233161489 0.600997175996445 zinc finger protein 680 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);meninges;skin;uterus;pia mater;lung;cochlea;endometrium;placenta;liver;germinal center;dura mater;bladder;brain;thymus; dorsal root ganglion;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.13492 . 0.174625237 65.9648502 270.13427 3.52605 ZNF680P1 . . . ZNF680 pseudogene 1 . . . . . . . . . . . ZNF681 2.16277598625636e-08 0.140530500079083 0.859469478293157 zinc finger protein 681 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . 0.08960 . 0.99945266 90.6935598 2610.52765 9.56268 ZNF682 3.67329437341058e-09 0.051462594506581 0.948537401820125 zinc finger protein 682 FUNCTION: May be involved in transcriptional regulation.; . . endometrium;kidney; skeletal muscle; 0.17043 0.09064 0.352813824 74.49280491 2320.81498 8.91824 ZNF683 0.00156069704939338 0.882214656309552 0.116224646641054 zinc finger protein 683 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;cartilage;endometrium;bone;testis;blood; subthalamic nucleus;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;atrioventricular node;pons;trigeminal ganglion; 0.11311 . 1.091286379 91.89667374 3918.79391 12.37478 ZNF684 0.00221741911028769 0.758046761085569 0.239735819804143 zinc finger protein 684 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.17806 . 0.262810045 70.43524416 106.95689 2.24402 ZNF687 0.975942572522876 0.0240563905936833 1.03688344049826e-06 zinc finger protein 687 FUNCTION: May be involved in transcriptional regulation.; . . smooth muscle;ovary;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;thyroid;bone;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;cervix;kidney;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.33071 0.13326 -0.810208867 12.08421798 512.33833 4.63374 ZNF688 7.08656311553746e-05 0.29823812941745 0.701691004951395 zinc finger protein 688 FUNCTION: May be involved in transcriptional regulation.; . . ovary;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;endometrium;testis;germinal center;pineal gland;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;macula lutea;spleen;kidney;mammary gland;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;heart;globus pallidus;testis;ciliary ganglion;atrioventricular node;skeletal muscle; . . -0.227663163 37.11370606 29.29176 0.93768 ZNF689 0.318737330058287 0.677705440033159 0.00355722990855423 zinc finger protein 689 FUNCTION: May be involved in transcriptional regulation.; . . lymphoreticular;ovary;skin;bone marrow;uterus;prostate;endometrium;larynx;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;blood;skeletal muscle;breast;pancreas;lung;hippocampus;liver;spleen;head and neck;kidney;stomach;thymus; superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;atrioventricular node;parietal lobe; 0.19946 0.11051 -0.648365105 16.35999056 15.07874 0.54158 ZNF691 0.417758649657401 0.547243720233603 0.0349976301089962 zinc finger protein 691 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.11359 0.08631 -0.449946534 24.00330267 20.21133 0.69180 ZNF692 3.97065824374004e-07 0.581419460665218 0.418580142268957 zinc finger protein 692 FUNCTION: May be involved in transcriptional regulation.; . . medulla oblongata;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;frontal lobe;endometrium;synovium;bone;testis;spinal ganglion;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;urinary;blood;lens;skeletal muscle;bile duct;pancreas;lung;nasopharynx;placenta;macula lutea;liver;spleen;head and neck;kidney;stomach;peripheral nerve;cerebellum; superior cervical ganglion;testis - interstitial;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09640 . -0.734731259 14.01863647 798.53205 5.57005 ZNF695 1.29535996261044e-10 0.026885184984901 0.973114814885563 zinc finger protein 695 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.05594 . 0.621009802 83.41589998 396.76348 4.18469 ZNF696 0.00597972241429247 0.732091511084459 0.261928766501248 zinc finger protein 696 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);heart;ovary;islets of Langerhans;parathyroid;skin;retina;uterus;whole body;lung;placenta;kidney;spinal ganglion;brain;mammary gland;thymus; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion; 0.13381 . . . 30.37307 0.96866 ZNF697 0.191081026945304 0.760403241866875 0.0485157311878201 zinc finger protein 697 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . 0.28485 . . . 113.68096 2.32254 ZNF699 1.56585740737052e-07 0.391681893679608 0.608317949734651 zinc finger protein 699 FUNCTION: May be involved in transcriptional regulation.; . . whole body;testis;spinal ganglion; ciliary ganglion; 0.07947 0.11619 -0.312207497 32.05944798 31.99603 1.00573 ZNF700 4.39166088843519e-11 0.0985365360851319 0.901463463870952 zinc finger protein 700 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);pancreas;endometrium;epididymis;bone;urinary;liver;blood;kidney;brain;mammary gland;skin;bone marrow; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion; 0.11173 . 0.159856957 64.91507431 554.81659 4.78612 ZNF701 2.35456949055137e-07 0.277441222183834 0.722558542359216 zinc finger protein 701 FUNCTION: May be involved in transcriptional regulation.; . . lymphoreticular;ovary;salivary gland;intestine;pharynx;colon;blood;skin;breast;prostate;pancreas;lung;endometrium;nasopharynx;thyroid;visual apparatus;liver;kidney;brain;bladder; superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;parietal lobe; 0.18312 . 0.290313621 71.56758669 284.84987 3.61242 ZNF702P . . . zinc finger protein 702, pseudogene FUNCTION: May be involved in transcriptional regulation.; . . islets of Langerhans;kidney; . . . . . . . ZNF703 . . . zinc finger protein 703 FUNCTION: Transcriptional corepressor which does not bind directly to DNA and may regulate transcription through recruitment of histone deacetylases to gene promoters. Regulates cell adhesion, migration and proliferation. May be required for segmental gene expression during hindbrain development. {ECO:0000269|PubMed:21328542, ECO:0000269|PubMed:21337521}.; DISEASE: Note=Luminal B breast cancers are the clinically more aggressive estrogen receptor-positive tumors. Amplification of a distal 8p12 locus occurs in around one third of the cases and ZNF703 is the single gene within the minimal amplicon. Amplification of the gene correlates with its protein expression in tumor cells. ZNF703 is a classical breast cancer oncogene since it is able to transform non-malignant cells and increase cellular proliferation.; TISSUE SPECIFICITY: Expressed in mammary epithelium. {ECO:0000269|PubMed:21317240}.; unclassifiable (Anatomical System);lung;endometrium;synovium;islets of Langerhans;placenta;blood;brain;skin;stomach; superior cervical ganglion;placenta;globus pallidus;ciliary ganglion;atrioventricular node;kidney;trigeminal ganglion; 0.57522 0.12204 . . 220.97413 3.21536 ZNF704 0.972642496818876 0.0273504641996523 7.03898147169106e-06 zinc finger protein 704 . . . unclassifiable (Anatomical System);heart;ovary;muscle;colon;parathyroid;skin;uterus;breast;optic nerve;larynx;thyroid;head and neck;brain;mammary gland; superior cervical ganglion;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.22180 0.11533 -0.558357437 19.54470394 1737.81342 7.69272 ZNF705A 0.0524783696043198 0.862253163387879 0.0852684670078014 zinc finger protein 705A FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System); dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19463 . 0.703746784 85.42108988 1973.30041 8.18422 ZNF705B 0.652541803539784 0.32234254112972 0.025115655330496 zinc finger protein 705B FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . 27.24291 0.87748 ZNF705CP . . . zinc finger protein 705C, pseudogene . . . . . . . . . . . ZNF705D . . . zinc finger protein 705D FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . 2.40691 0.08363 ZNF705E . . . zinc finger protein 705E FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . . . ZNF705F . . . zinc finger protein 705F FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . . . ZNF705G 4.24856211732445e-09 0.0293742018986346 0.970625793852803 zinc finger protein 705G FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . 148.15733 2.65200 ZNF706 0.21628195162679 0.647857650265841 0.135860398107368 zinc finger protein 706 FUNCTION: Transcription repressor involved in the exit of embryonic stem cells (ESCs) from self-renewal. Acts by repressing expression of KLF4. {ECO:0000250|UniProtKB:Q9D115}.; . . ovary;salivary gland;intestine;colon;fovea centralis;skin;bone marrow;uterus;prostate;whole body;frontal lobe;cochlea;endometrium;bone;thyroid;pituitary gland;testis;germinal center;spinal ganglion;brain;artery;bladder;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;pharynx;blood;skeletal muscle;breast;pancreas;lung;cornea;nasopharynx;trabecular meshwork;placenta;macula lutea;visual apparatus;hippocampus;alveolus;hypopharynx;liver;spleen;head and neck;kidney;mammary gland;aorta;stomach; . 0.68254 0.03411 0.145304857 63.81221986 1.1225 0.03053 ZNF707 0.0127700852104931 0.857656121634039 0.129573793155467 zinc finger protein 707 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;heart;bone;liver;germinal center;mammary gland;skin;stomach; superior cervical ganglion;atrioventricular node; 0.17147 0.10299 0.264628794 70.5178108 77.30133 1.84692 ZNF708 4.17756094613551e-09 0.0554214021657419 0.944578593656697 zinc finger protein 708 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.19102 . 2.087222794 97.84736966 355.28822 3.98729 ZNF709 5.65103851089128e-06 0.99310276362468 0.00689158533680882 zinc finger protein 709 FUNCTION: May be involved in transcriptional regulation.; . . . . . 0.09776 -0.580403979 18.58928993 24.14649 0.79270 ZNF710 0.943123584694422 0.0568327205499491 4.36947556284704e-05 zinc finger protein 710 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;choroid;fovea centralis;skin;bone marrow;retina;uterus;optic nerve;thyroid;testis;brain;unclassifiable (Anatomical System);heart;blood;lens;breast;pancreas;lung;placenta;visual apparatus;macula lutea;cervix;stomach;peripheral nerve;thymus; superior cervical ganglion;atrioventricular node;skeletal muscle; 0.15612 0.11465 -0.705410796 14.77942911 126.64528 2.45259 ZNF711 0.989393563505584 0.0106030609363334 3.37555808268313e-06 zinc finger protein 711 FUNCTION: Transcription regulator required for brain development. Probably acts as a transcription factor that binds to the promoter of target genes and recruits PHF8 histone demethylase, leading to activate expression of genes involved in neuron development, such as KDM5C. {ECO:0000269|PubMed:20346720}.; . TISSUE SPECIFICITY: Expressed in neural tissues. {ECO:0000269|PubMed:20346720}.; unclassifiable (Anatomical System);lymph node;smooth muscle;ovary;hypothalamus;parathyroid;blood;skeletal muscle;retina;breast;pancreas;lung;bone;placenta;thyroid;visual apparatus;testis;spleen;cervix;artery;brain;stomach;aorta; testis;pons; 0.26758 0.10473 -0.227663163 37.11370606 21.42364 0.72264 ZNF713 0.00111519799587951 0.834448978841435 0.164435823162686 zinc finger protein 713 FUNCTION: May be involved in transcriptional regulation.; DISEASE: Note=A 7p11.2 folate-sensitive fragile site, FRA7A, has been identified in 2 unrelated families diagnosed with an autistic disorder. FRA7A is associated with a CGG-repeat expansion in a ZNF713 5'-intron. In the first family, the expanded allele contained about 450 CGG-repeats. It showed hypermethylation and reduced ZNF713 expression. In the second family, 3 autistic siblings exhibited a heterozygous expansion of about 70 repeats, corresponding to premutations, which were partially or mosaically methylated. Mitotic instability of the premutation was observed in one affected sibling. In this family, ZNF713 tends to be up- regulated. It has been suggested that ZNF713 misregulation in the brain might be involved in the pathogenicity of autistic disorder (PubMed:25196122). {ECO:0000269|PubMed:25196122}.; TISSUE SPECIFICITY: Expressed in fetal and adult brain. {ECO:0000269|PubMed:25196122}.; . . 0.11789 . -0.846787714 11.05803255 3.16104 0.11315 ZNF714 7.33708061274363e-06 0.491240892061201 0.508751770858186 zinc finger protein 714 FUNCTION: May be involved in transcriptional regulation.; . . breast;prostate;pancreas;testis; . 0.10078 . 0.753291803 86.71266808 52.45621 1.43277 ZNF716 2.56317973452826e-08 0.0827887078399023 0.9172112665283 zinc finger protein 716 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.07268 . 0.859896574 88.62349611 956.3448 5.98654 ZNF717 0.332205459126617 0.486939958407177 0.180854582466205 zinc finger protein 717 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . 172.76755 2.86230 ZNF718 . . . zinc finger protein 718 FUNCTION: May be involved in transcriptional regulation.; . . . . . . . . . . ZNF720 0.0559604563285243 0.707057235829301 0.236982307842175 zinc finger protein 720 . . . unclassifiable (Anatomical System);colon;fovea centralis;choroid;lens;retina;uterus;optic nerve;lung;endometrium;placenta;bone;macula lutea;visual apparatus;testis;mammary gland;brain; . 0.06899 . 0.58987904 82.3720217 19.56487 0.67154 ZNF720P1 . . . zinc finger protein 720 pseudogene 1 . . . . . . . . . . . ZNF721 5.97289371219059e-11 0.0327439908151442 0.967256009125127 zinc finger protein 721 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;prostate;optic nerve;atrium;whole body;frontal lobe;thyroid;bone;testis;amniotic fluid;dura mater;brain;unclassifiable (Anatomical System);meninges;hypothalamus;lens;bile duct;lung;pia mater;placenta;macula lutea;visual apparatus;liver;kidney; occipital lobe;superior cervical ganglion;testis - interstitial;ciliary ganglion;trigeminal ganglion; 0.26586 . 0.433520496 77.34725171 800.17921 5.57405 ZNF722P . . . zinc finger protein 722, pseudogene . . . . . . . . . . . ZNF723P . . . zinc finger protein 723, pseudogene . . . . . . . . . . . ZNF724P 0.00669603090666866 0.915615236275063 0.0776887328182686 zinc finger protein 724, pseudogene FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . 32.7001 1.01666 ZNF725P . . . zinc finger protein 725, pseudogene . . . . . . . . . . . ZNF726 . . . zinc finger protein 726 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . uterus;ovary;placenta; . . . . . 445.56606 4.39333 ZNF726P1 . . . zinc finger protein 726 pseudogene 1 . . . . . . . . . . . ZNF727 1.56297034947385e-07 0.0652273736937696 0.934772470009195 zinc finger protein 727 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . 2.34827224 98.40764331 260.10396 3.46546 ZNF728 1.3589524035837e-07 0.208328597174274 0.791671266930486 zinc finger protein 728 . . . . . . . . . 3188.19789 10.75687 ZNF729 3.73171701464113e-10 0.174132881639815 0.825867117987014 zinc finger protein 729 FUNCTION: May be involved in transcriptional regulation.; . . . . . . . . 863.82585 5.72823 ZNF730 1.85625397322033e-10 0.0173174254028099 0.982682574411565 zinc finger protein 730 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . breast; . . . . . 321.79665 3.80914 ZNF731P . . . zinc finger protein 731, pseudogene . . . . . . . . . . . ZNF732 1.31184093398498e-09 0.0283266896548582 0.971673309033301 zinc finger protein 732 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . 2.151571682 97.9948101 598.96088 4.95375 ZNF733P . . . zinc finger protein 733, pseudogene . . . . . . . . . . . ZNF734P . . . zinc finger protein 734, pseudogene . . . . . . . . . . . ZNF735 . . . zinc finger protein 735 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . . . ZNF736 0.143727833114872 0.778856821494087 0.0774153453910416 zinc finger protein 736 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;placenta;parathyroid; dorsal root ganglion;testis - interstitial;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . . 1.346793777 94.30290163 3465.49539 11.33264 ZNF736P1Y . . . zinc finger protein 736 pseudogene 1, Y-linked . . . . . . . . . . . ZNF736P2Y . . . zinc finger protein 736 pseudogene 2, Y-linked . . . . . . . . . . . ZNF736P3Y . . . zinc finger protein 736 pseudogene 3, Y-linked . . . . . . . . . . . ZNF736P4Y . . . zinc finger protein 736 pseudogene 4, Y-linked . . . . . . . . . . . ZNF736P5Y . . . zinc finger protein 736 pseudogene 5, Y-linked . . . . . . . . . . . ZNF736P6Y . . . zinc finger protein 736 pseudogene 6, Y-linked . . . . . . . . . . . ZNF736P7Y . . . zinc finger protein 736 pseudogene 7, Y-linked . . . . . . . . . . . ZNF736P8Y . . . zinc finger protein 736 pseudogene 8, Y-linked . . . . . . . . . . . ZNF736P9Y . . . zinc finger protein 736 pseudogene 9, Y-linked . . . . . . . . . . . ZNF736P10Y . . . zinc finger protein 736 pseudogene 10, Y-linked . . . . . . . . . . . ZNF736P11Y . . . zinc finger protein 736 pseudogene 11, Y-linked . . . . . . . . . . . ZNF736P12Y . . . zinc finger protein 736 pseudogene 12, Y-linked . . . . . . . . . . . ZNF737 1.10579189398794e-07 0.18655673734957 0.813443152071241 zinc finger protein 737 FUNCTION: May be involved in transcriptional regulation.; . . . . . . 2.2177395 98.14225053 1976.98707 8.19153 ZNF738 0.106373218916856 0.775582381943605 0.118044399139539 zinc finger protein 738 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.08919 . . . 39.39037 1.16451 ZNF740 0.653748287756941 0.340460970564576 0.0057907416784824 zinc finger protein 740 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.42605 . 0.325313577 73.11276244 37.32635 1.11285 ZNF746 0.0517385668171128 0.943820827680506 0.00444060550238122 zinc finger protein 746 FUNCTION: Transcription repressor that specifically binds to the 5'-TATTTT[T/G]-3' consensus sequence on promoters and repress transcription of PGC-1-alpha (PPARGC1A), thereby playing a role in regulation of neuron death. {ECO:0000269|PubMed:21376232}.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;testis;pineal gland;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;lens;skeletal muscle;breast;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;stomach; . 0.64319 . -0.332434268 30.74427931 75.84437 1.82523 ZNF747 2.75423162490336e-05 0.181959541378573 0.818012916305178 zinc finger protein 747 . . . unclassifiable (Anatomical System);islets of Langerhans;colon;skin;uterus;lung;endometrium;placenta;thyroid;testis;head and neck;cervix;kidney;stomach; dorsal root ganglion;superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle;parietal lobe;skin; 0.22805 . . . 138.70901 2.56616 ZNF749 1.62775731696662e-06 0.41319057928336 0.586807792959323 zinc finger protein 749 FUNCTION: May be involved in transcriptional regulation.; . . kidney;brain;skin; superior cervical ganglion;trigeminal ganglion;parietal lobe;skeletal muscle; 0.27413 0.11550 0.20394914 67.45694739 989.24767 6.06389 ZNF750 0.865734363838442 0.134184590756124 8.10454054334982e-05 zinc finger protein 750 FUNCTION: Transcription factor involved in epidermis differentiation. Required for terminal epidermal differentiation: acts downstream of p63/TP63 and activates expression of late epidermal differentiation genes. Specifically binds to the promoter of KLF4 and promotes its expression. {ECO:0000269|PubMed:22364861}.; DISEASE: Seborrhea-like dermatitis with psoriasiform elements (SLDP) [MIM:610227]: Characterized by a chronic fine diffuse scaly erythematous rash on the face, particularly on the chin, nasolabial folds and eyebrows, around earlobes and over the scalp. The rash exacerbate in the winter, with emotional stress and after strenuous physical activity. Hyperkeratosis of skin over the elbows, knees, palms, soles and metacarpophalangeal joints is evident. There is no arthralgia, arthritis or neurological disorders. {ECO:0000269|PubMed:16751772}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Expressed in the skin, prostate, lung, placenta and thymus, and at low level in T-cells. Not expressed in peripheral blood leukocytes, pancreas and brain. Clearly expressed in primary keratinocytes but not in fibroblasts. {ECO:0000269|PubMed:16751772}.; unclassifiable (Anatomical System);heart;colon;skin;uterus;breast;prostate;lung;endometrium;placenta;thyroid;hypopharynx;head and neck;bladder; skin; 0.07015 0.08890 0.317821209 72.81198396 1133.32036 6.42477 ZNF761 . . . zinc finger protein 761 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . 0.04332 . . . . . ZNF763 0.000236872840014969 0.757019354629589 0.242743772530396 zinc finger protein 763 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);skeletal muscle;stomach; subthalamic nucleus;atrioventricular node;trigeminal ganglion;skeletal muscle; . . 0.933309256 89.82661005 174.2674 2.87261 ZNF764 3.06788723152273e-08 0.0484902553029503 0.951509714018177 zinc finger protein 764 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;optic nerve;whole body;frontal lobe;testis;germinal center;brain;tonsil;unclassifiable (Anatomical System);heart;cartilage;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;liver;kidney; superior cervical ganglion;globus pallidus;ciliary ganglion;pons;skeletal muscle; 0.12882 0.10116 . . 307.23243 3.72980 ZNF765 9.0464791076453e-10 0.0435625883362643 0.956437410759088 zinc finger protein 765 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);lymph node;lung; . 0.09639 . 0.733063566 86.27034678 339.26241 3.90630 ZNF766 7.45003861398477e-08 0.462872674253157 0.537127251246456 zinc finger protein 766 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lymph node;cartilage;heart;ovary;islets of Langerhans;salivary gland;muscle;colon;parathyroid;blood;fovea centralis;vein;skin;skeletal muscle;uterus;pancreas;lung;frontal lobe;thyroid;placenta;macula lutea;testis;kidney;brain; . 0.19238 . -0.510624372 21.65015334 59.86744 1.56988 ZNF767P . . . zinc finger family member 767, pseudogene . . . . . 0.18086 . . . . . ZNF768 0.579305580172895 0.418391624083801 0.00230279574330378 zinc finger protein 768 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.24524 0.10803 -0.291981272 33.20358575 1934.64665 8.09309 ZNF770 0.82751324661339 0.17232769984672 0.000159053539889981 zinc finger protein 770 FUNCTION: May be involved in transcriptional regulation.; . . myocardium;lymphoreticular;smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;brain;heart;cartilage;tongue;blood;lens;skeletal muscle;breast;trabecular meshwork;visual apparatus;macula lutea;liver;spleen;mammary gland;colon;parathyroid;choroid;fovea centralis;uterus;whole body;larynx;bone;pituitary gland;testis;unclassifiable (Anatomical System);cerebellum cortex;islets of Langerhans;bile duct;lung;adrenal gland;nasopharynx;placenta;hypopharynx;head and neck;kidney;stomach;aorta;thymus; . 0.37639 0.09460 -0.442665927 24.53408823 53.00521 1.44576 ZNF771 0.295812869272627 0.624836538745243 0.0793505919821299 zinc finger protein 771 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;frontal lobe;bone;testis;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;hypothalamus;muscle;lens;skeletal muscle;lung;placenta;hippocampus;macula lutea;liver;kidney; dorsal root ganglion; 0.37511 0.11198 . . 27.63084 0.88891 ZNF772 0.00795615487412956 0.929181095128407 0.0628627499974639 zinc finger protein 772 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);ovary;heart;colon;parathyroid;skin;uterus;prostate;whole body;lung;placenta;liver;testis;spleen;kidney;germinal center;brain;stomach;peripheral nerve; . 0.12236 . 0.284856336 71.40835103 24.92453 0.81863 ZNF773 5.50268566614554e-09 0.0649239650853236 0.935076029411991 zinc finger protein 773 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;whole body;ovary;lacrimal gland;adrenal cortex;liver;spleen;kidney;germinal center;brain;skeletal muscle;bone marrow; . 0.26982 . -0.268115223 34.70747818 552.66876 4.78144 ZNF774 1.10144667279176e-10 0.0466884009930933 0.953311598896762 zinc finger protein 774 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . lung;bone;testis;colon;spinal ganglion; superior cervical ganglion;skeletal muscle; 0.14248 . 0.598963042 82.7789573 763.02482 5.47501 ZNF775 0.0122292592081411 0.852068484465137 0.135702256326722 zinc finger protein 775 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);heart;ovary;hypothalamus;blood;parathyroid;fovea centralis;choroid;lens;skin;retina;uterus;optic nerve;lung;cochlea;bone;placenta;macula lutea;pituitary gland;testis;germinal center;kidney;brain;mammary gland;thymus; . 0.22078 . . . 51.52192 1.41705 ZNF776 7.87023474197769e-06 0.74407812393241 0.255914005832848 zinc finger protein 776 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;developmental;urinary;colon;parathyroid;skin;skeletal muscle;uterus;pancreas;lung;frontal lobe;placenta;testis;germinal center;kidney;brain;bladder;stomach;thymus; . 0.05378 . -0.824740496 11.67728238 13.48046 0.49032 ZNF777 0.997614409900424 0.00238550196822947 8.81313464006682e-08 zinc finger protein 777 FUNCTION: May be involved in transcriptional regulation.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;frontal lobe;endometrium;pituitary gland;testis;germinal center;brain;unclassifiable (Anatomical System);heart;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;hippocampus;liver;kidney;mammary gland;stomach;thymus; atrioventricular node; 0.53172 . -0.016511957 52.31776362 385.32192 4.13665 ZNF778 1.63414262887613e-15 0.00346776061243585 0.996532239387563 zinc finger protein 778 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . uterus;frontal lobe;visual apparatus;liver;spleen;bone marrow; . . . 1.302520887 93.9195565 439.77574 4.37018 ZNF780A 1.73286195326953e-06 0.866591171280161 0.133407095857885 zinc finger protein 780A FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);cartilage;colon;blood;fovea centralis;choroid;lens;retina;uterus;prostate;optic nerve;lung;adrenal gland;bone;macula lutea;alveolus;testis;germinal center;kidney;aorta; . 0.12886 . 1.133561642 92.28591649 223.07016 3.22935 ZNF780B 3.89667579331898e-13 0.084398989483864 0.915601010515746 zinc finger protein 780B FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;lung;whole body;placenta;sympathetic chain;kidney;skeletal muscle;stomach; whole brain;subthalamic nucleus;superior cervical ganglion;cerebellum peduncles;prefrontal cortex;ciliary ganglion;atrioventricular node;pons;skeletal muscle; 0.12684 . 1.293370039 93.88417079 467.55295 4.48029 ZNF781 7.22160643082208e-06 0.160947173719739 0.83904560467383 zinc finger protein 781 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);bile duct;whole body;islets of Langerhans;hypothalamus;liver;brain;skin; . 0.19433 . 0.084621747 60.31493277 330.24448 3.86285 ZNF782 4.92957230407518e-05 0.867899869322752 0.132050834954207 zinc finger protein 782 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);meninges;pia mater;heart;hypothalamus;placenta;liver;testis;dura mater;brain;skin;retina; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;skin; 0.13863 . 1.179479654 92.79311158 502.83028 4.60095 ZNF783 0.000963929173297341 0.943685088436491 0.0553509823902113 zinc finger family member 783 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.09184 . . . 540.7175 4.73627 ZNF784 0.352694144279667 0.59302950722243 0.0542763484979028 zinc finger protein 784 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);ovary;cartilage;islets of Langerhans;colon;fovea centralis;choroid;lens;skeletal muscle;retina;prostate;optic nerve;lung;thyroid;macula lutea;visual apparatus;testis;germinal center;brain;stomach; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.14574 . . . 111.58012 2.29985 ZNF785 3.83915416323042e-14 0.000839963038405283 0.999160036961556 zinc finger protein 785 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . 0.062575634 58.74026893 98.85282 2.14939 ZNF786 1.40003789521225e-08 0.203153832955692 0.796846153043929 zinc finger protein 786 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lung;frontal lobe;ovary;macula lutea;testis;fovea centralis;brain; superior cervical ganglion; 0.12785 . -0.841329384 11.36470866 59.97604 1.57179 ZNF787 0.741821107718521 0.247230813895215 0.0109480783862644 zinc finger protein 787 FUNCTION: May be involved in transcriptional regulation.; . . uterus;lung;whole body;ovary;heart;testis;colon;blood;brain;mammary gland;skin;thymus; medulla oblongata;adrenal cortex;pons; 0.19230 . . . 42.28078 1.23063 ZNF788 0.0529943896875062 0.698359595458998 0.248646014853495 zinc finger family member 788 FUNCTION: May be involved in transcriptional regulation.; . . . . . . . . 1886.91698 7.98843 ZNF789 7.06159747447558e-08 0.264761443611892 0.735238485772133 zinc finger protein 789 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);blood;fovea centralis;choroid;lens;retina;optic nerve;whole body;lung;frontal lobe;endometrium;placenta;macula lutea;visual apparatus;liver;spleen;germinal center;kidney;mammary gland; testis - interstitial;atrioventricular node; 0.09799 . 0.575097644 82.1656051 2992.53838 10.38471 ZNF790 3.27623626050772e-12 0.0798959520611617 0.920104047935562 zinc finger protein 790 FUNCTION: May be involved in transcriptional regulation.; . . ovary;heart;islets of Langerhans;salivary gland;pharynx;colon;blood;retina;breast;uterus;prostate;pancreas;lung;cerebral cortex;visual apparatus;hypopharynx;liver;testis;head and neck;kidney;brain;bladder; superior cervical ganglion;globus pallidus;trigeminal ganglion; 0.17532 . 0.576916344 82.25406936 2230.09865 8.70214 ZNF790-AS1 . . . ZNF790 antisense RNA 1 . . . . . . . . . . . ZNF791 0.00827190470326655 0.988895422752605 0.00283267254412834 zinc finger protein 791 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);breast;liver;blood;skin;stomach;retina; atrioventricular node; 0.13130 . -0.626318434 17.03231894 10.93842 0.39589 ZNF792 3.90385673725562e-07 0.356424249967153 0.643575359647173 zinc finger protein 792 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.17039 . 0.137810868 63.63529134 386.37077 4.13953 ZNF793 5.30990814631529e-06 0.426463293208318 0.573531396883536 zinc finger protein 793 FUNCTION: May be involved in transcriptional regulation.; . . salivary gland;colon;parathyroid;fovea centralis;skin;bone marrow;uterus;prostate;frontal lobe;larynx;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;adrenal cortex;pharynx;blood;skeletal muscle;lung;macula lutea;liver;spleen;head and neck;cervix;kidney;thymus; medulla oblongata;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.11578 . 0.286674996 71.49681529 194.69717 3.02543 ZNF793-AS1 . . . ZNF793 antisense RNA 1 (head to head) . . . . . . . . . . . ZNF799 6.79320285817144e-05 0.907131713194684 0.0928003547767343 zinc finger protein 799 FUNCTION: May be involved in transcriptional regulation.; . . . . . 0.10535 0.709197509 85.68058504 466.26717 4.47282 ZNF800 0.997032620126522 0.00296734950136065 3.03721176234004e-08 zinc finger protein 800 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lymph node;ovary;heart;colon;parathyroid;blood;skin;retina;breast;uterus;pancreas;prostate;lung;endometrium;bone;thyroid;placenta;visual apparatus;testis;germinal center;kidney;brain;bladder;aorta; testis - interstitial;atrioventricular node;skin; 0.56246 . -0.025608647 51.91672564 116.34071 2.34648 ZNF804A 0.827436291073838 0.172557174737117 6.53418904452792e-06 zinc finger protein 804A . . . pancreas;lung;bone;kidney;brain;retina; dorsal root ganglion;subthalamic nucleus;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.32762 0.09197 1.298854499 93.91365888 13449.48659 25.20472 ZNF804B 4.77795175322779e-14 0.0479627380810904 0.952037261918862 zinc finger protein 804B . . . . . 0.09352 . 3.374093349 99.43972635 2368.37941 9.03579 ZNF805 0.79436861206606 0.205372796614767 0.000258591319172665 zinc finger protein 805 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . 1.216305531 93.13517339 1960.60485 8.15508 ZNF806 . . . zinc finger protein 806 FUNCTION: May function as a transcription factor. {ECO:0000250}.; . . . . 0.08140 . . . . . ZNF807 . . . zinc finger protein 807 . . . unclassifiable (Anatomical System);heart;lacrimal gland;islets of Langerhans;pineal body;blood;bone marrow;pancreas;whole body;frontal lobe;cochlea;adrenal gland;thyroid;liver;testis;spleen;germinal center;kidney;brain;mammary gland; . . . . . . . ZNF808 1.7952208167963e-05 0.881599845303434 0.118382202488398 zinc finger protein 808 FUNCTION: May be involved in transcriptional regulation.; . . placenta;peripheral nerve; . . . 0.672386703 84.73696627 899.74487 5.84351 ZNF812P . . . zinc finger protein 812, pseudogene . . . . . . . . . . . ZNF813 8.49957637821414e-10 0.0796468587444294 0.920353140405613 zinc finger protein 813 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.08121 . 1.35769336 94.43854683 2208.34827 8.65139 ZNF814 6.74808519166839e-10 0.130847412647902 0.86915258667729 zinc finger protein 814 . . . . . . . -0.293801652 32.93819297 99.67292 2.16252 ZNF815P . . . zinc finger protein 815, pseudogene . . . . . . . . . . . ZNF816 5.09883837591247e-09 0.1168378600696 0.883162134831562 zinc finger protein 816 FUNCTION: May be involved in transcriptional regulation.; . . lymphoreticular;smooth muscle;umbilical cord;salivary gland;colon;skin;retina;bone marrow;frontal lobe;endometrium;thyroid;bone;testis;germinal center;artery;brain;unclassifiable (Anatomical System);spinal cord;blood;skeletal muscle;pancreas;placenta;visual apparatus;cervix;mammary gland;stomach;aorta; dorsal root ganglion;testis - interstitial;superior cervical ganglion;medulla oblongata;atrioventricular node;caudate nucleus;pons;skin;skeletal muscle;subthalamic nucleus;globus pallidus;ciliary ganglion;trigeminal ganglion; . . 2.046758368 97.76480302 3880.14485 12.29495 ZNF816-ZNF321P . . . ZNF816-ZNF321P readthrough . . . unclassifiable (Anatomical System);uterus;heart;colon;kidney;brain;skin;skeletal muscle;stomach; . . . -0.161524709 41.6430762 . . ZNF818P . . . zinc finger protein 818, pseudogene FUNCTION: May be involved in transcriptional regulation.; . . . . 0.04481 . . . . . ZNF821 0.158430832731393 0.838272719276584 0.00329644799202232 zinc finger protein 821 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);cartilage;lacrimal gland;islets of Langerhans;pineal body;sympathetic chain;adrenal cortex;fovea centralis;choroid;lens;retina;optic nerve;lung;macula lutea;visual apparatus;liver;pituitary gland;testis;spleen;germinal center;kidney;mammary gland;brain; testis - interstitial;superior cervical ganglion;testis;cerebellum;bone marrow; 0.16787 0.10783 -0.183570861 39.95046001 15.0966 0.54233 ZNF823 2.08858743468726e-06 0.890861537657105 0.109136373755461 zinc finger protein 823 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);uterus;lung;ovary;heart;islets of Langerhans;liver;colon;kidney;brain;skin; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; . 0.10997 0.108486928 61.90728946 42.06567 1.22503 ZNF826P . . . zinc finger protein 826, pseudogene FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System); dorsal root ganglion;testis - interstitial;superior cervical ganglion;subthalamic nucleus;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; . . . . . . ZNF827 0.999865837850191 0.000134162133770716 1.60380714790973e-11 zinc finger protein 827 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;colon;lens;skin;skeletal muscle;retina;uterus;prostate;whole body;lung;thyroid;placenta;visual apparatus;liver;testis;cervix;germinal center;brain;mammary gland; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.56940 . -2.168050122 1.40953055 57.9316 1.53875 ZNF829 1.84766387824288e-08 0.128788608507407 0.871211373015954 zinc finger protein 829 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.10391 . -0.227663163 37.11370606 78.33356 1.86701 ZNF830 0.447637075601119 0.545985873225164 0.00637705117371696 zinc finger protein 830 FUNCTION: Acts as an important regulator of the cell cycle that participates in the maintenance of genome integrity. During cell cycle progression in embryonic fibroblast, prevents replication fork collapse, double-strand break formation and cell cycle checkpoint activation. Controls mitotic cell cycle progression and cell survival in rapidly proliferating intestinal epithelium and embryonic stem cells. During the embryo preimplantation, controls different aspects of M phase. During early oocyte growth, plays a role in oocyte survival by preventing chromosomal breaks formation, activation of TP63 and reduction of transcription. {ECO:0000250|UniProtKB:Q8R1N0}.; . . salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;optic nerve;cochlea;endometrium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;blood;lens;skeletal muscle;breast;pancreas;lung;epididymis;nasopharynx;placenta;macula lutea;visual apparatus;spleen;head and neck;kidney;thymus; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;trigeminal ganglion; 0.19303 0.09280 0.040529541 57.15380986 2484.83347 9.30353 ZNF831 7.64881641877554e-09 0.970919493646935 0.0290804987042483 zinc finger protein 831 . . . . . 0.07141 . 1.328244615 94.10828025 431.43682 4.33510 ZNF833P . . . zinc finger protein 833, pseudogene . . . unclassifiable (Anatomical System); . . . . . . . ZNF835 9.61689891257654e-13 0.00559691395109652 0.994403086047942 zinc finger protein 835 FUNCTION: May be involved in transcriptional regulation.; . . colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;cochlea;endometrium;bone;pituitary gland;testis;germinal center;brain;pineal gland;unclassifiable (Anatomical System);lymph node;heart;cartilage;tongue;lens;lung;macula lutea;hippocampus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; . . . 0.468503535 78.79806558 3392.75239 11.14944 ZNF836 3.01932501527445e-09 0.161808909157747 0.838191087822928 zinc finger protein 836 FUNCTION: May be involved in transcriptional regulation.; . . larynx;testis;head and neck; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; . . -0.354480518 29.42911064 2780.33627 9.96197 ZNF837 0.25844063599264 0.639591937447754 0.101967426559606 zinc finger protein 837 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . 407.37945 4.23268 ZNF839 9.18902348869399e-05 0.935142116812716 0.0647659929523976 zinc finger protein 839 . . . unclassifiable (Anatomical System);cartilage;heart;ovary;colon;fovea centralis;skin;breast;uterus;prostate;whole body;lung;bone;thyroid;placenta;macula lutea;visual apparatus;liver;testis;cervix;spleen;germinal center;kidney;brain;stomach; dorsal root ganglion;testis - interstitial;superior cervical ganglion;subthalamic nucleus;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;pons;trigeminal ganglion;skeletal muscle; 0.09310 . 1.495467846 95.37626799 1511.89021 7.22302 ZNF839P1 . . . zinc finger protein 839 pseudogene 1 . . . . . . . . . . . ZNF840P . . . zinc finger protein 840, pseudogene FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . 0.02766 . . . . . ZNF841 4.04876108417812e-08 0.349531530139441 0.650468429372948 zinc finger protein 841 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . prostate;liver;colon; . . . 0.619191319 83.36282142 706.42123 5.27971 ZNF843 . . . zinc finger protein 843 . . . unclassifiable (Anatomical System); . . . 0.567831482 81.78225997 440.60603 4.37322 ZNF844 1.00623256693283e-05 0.341425776949675 0.658564160724655 zinc finger protein 844 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . 2.81877582 99.05638122 4160.71334 12.81024 ZNF845 6.25752332823778e-08 0.663891764563104 0.336108172861663 zinc finger protein 845 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);breast;lung;colon;kidney; . . . 1.840996754 97.08657702 1055.55176 6.23685 ZNF846 3.7497661971544e-16 0.000756524478540083 0.99924347552146 zinc finger protein 846 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . 0.466683681 78.73908941 1291.14567 6.76427 ZNF847P . . . zinc finger protein 847, pseudogene . . . . . . . . . . . ZNF848P . . . zinc finger protein 848, pseudogene . . . . . . . . . . . ZNF849P . . . zinc finger protein 849, pseudogene . . . . . 0.06229 . . . . . ZNF850 0.188901355257348 0.810621155960169 0.00047748878248342 zinc finger protein 850 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . 250.53864 3.41057 ZNF852 6.53650192013867e-09 0.0716461969590333 0.928353796504465 zinc finger protein 852 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . bone;placenta;skeletal muscle; . . . . . 46.60647 1.31878 ZNF853 0.000958951242529297 0.359144762313065 0.639896286444406 zinc finger protein 853 . . . . . . . . . 819.09741 5.62160 ZNF859P . . . zinc finger protein 859, pseudogene . . . . . . . . . . . ZNF860 7.85955632803042e-11 0.0200838060889165 0.979916193832488 zinc finger protein 860 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . 1.77302331 96.80938901 2376.15674 9.04469 ZNF861P . . . zinc finger protein 861, pseudogene . . . . . . . . . . . ZNF862 3.68873263295519e-09 0.532167336333596 0.467832659977671 zinc finger protein 862 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . unclassifiable (Anatomical System);uterus;cartilage;testis;brain;retina;thymus; superior cervical ganglion;trigeminal ganglion;skeletal muscle; . 0.10093 -1.273261975 5.195800896 1462.87285 7.13373 ZNF863P . . . zinc finger protein 863, pseudogene . . . . . . . . . . . ZNF865 . . . zinc finger protein 865 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . 54.80322 1.48278 ZNF876P . . . zinc finger protein 876, pseudogene FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . frontal lobe;adrenal gland;spinal cord; dorsal root ganglion;superior cervical ganglion;globus pallidus;appendix;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin; . . . . . . ZNF877P . . . zinc finger protein 877, pseudogene . . . . . . . . . . . ZNF878 1.48979796633174e-07 0.218737072156018 0.781262778864186 zinc finger protein 878 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . 0.420771676 77.15852795 603.0357 4.97046 ZNF879 0.000705395855764813 0.515041465703607 0.484253138440629 zinc finger protein 879 FUNCTION: May be involved in transcriptional regulation.; . . . . . . 0.858082312 88.55862232 1265.8303 6.70564 ZNF880 3.87890072898594e-09 0.100208265773128 0.899791730347971 zinc finger protein 880 . . . unclassifiable (Anatomical System); . . . 1.9512643 97.52889833 3314.30673 11.00153 ZNF883 . . . zinc finger protein 883 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . . . ZNF884P . . . zinc finger protein 884, pseudogene . . . . . . . . . . . ZNF885P . . . zinc finger protein 885, pseudogene . . . . . . . . . . . ZNF886P . . . zinc finger protein 886, pseudogene . . . . . . . . . . . ZNF887P . . . zinc finger protein 887, pseudogene . . . . . . . . . . . ZNF888 . . . zinc finger protein 888 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . . . ZNF890P . . . zinc finger protein 890, pseudogene . . . . . 0.22792 . . . . . ZNF891 0.636347899240249 0.335043497487623 0.0286086032721287 zinc finger protein 891 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . 1497.82864 7.20082 ZNF962P . . . zinc finger protein 962, pseudogene . . . . . . . . . . . ZNF965P . . . zinc finger protein 965, pseudogene . . . . . . . . . . . ZNF968P . . . zinc finger protein 968, pseudogene . . . . . . . . . . . ZNF969P . . . zinc finger protein 969, pseudogene . . . . . . . . . . . ZNF970P . . . zinc finger protein 970, pseudogene . . . . . . . . . . . ZNF971P . . . zinc finger protein 971, pseudogene . . . . . . . . . . . ZNFX1 0.999981099240724 1.8900759276089e-05 2.27084789660395e-16 zinc finger, NFX1-type containing 1 . . TISSUE SPECIFICITY: Widely expressed.; . . 0.21574 0.12103 -0.44655933 24.21561689 769.96492 5.49071 ZNHIT1 0.000428046419828023 0.648148809533918 0.351423144046254 zinc finger HIT-type containing 1 FUNCTION: Seems to play a role in p53-mediated apoptosis induction. Binds to NR1D2 and relieves it of its inhibitory effect on the transcription of APOC3 without affecting its DNA-binding activity. {ECO:0000269|PubMed:17380123, ECO:0000269|PubMed:17892483}.; . TISSUE SPECIFICITY: Expressed abundantly in liver, but weakly in skeletal muscle, ovary and small intestine. {ECO:0000269|PubMed:17892483}.; myocardium;lymphoreticular;ovary;skin;retina;prostate;optic nerve;endometrium;thyroid;germinal center;brain;bladder;tonsil;heart;cartilage;adrenal cortex;pharynx;blood;lens;skeletal muscle;breast;visual apparatus;liver;alveolus;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;choroid;vein;uterus;whole body;synovium;bone;pituitary gland;testis;unclassifiable (Anatomical System);lymph node;trophoblast;islets of Langerhans;hypothalamus;muscle;bile duct;pancreas;lung;cornea;adrenal gland;placenta;hypopharynx;amnion;head and neck;kidney;stomach;aorta;thymus; heart;liver; 0.18465 0.11262 -0.317668748 31.45789101 13.13006 0.47766 ZNHIT1P1 . . . zinc finger HIT-type containing 1 pseudogene 1 . . . . . . . . . . . ZNHIT2 0.200832999054726 0.75480362636561 0.0443633745796645 zinc finger HIT-type containing 2 . . TISSUE SPECIFICITY: Low expression in most tissues; highly expressed in testis. {ECO:0000269|PubMed:10602999}.; lymphoreticular;ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;islets of Langerhans;blood;lens;pancreas;lung;placenta;macula lutea;liver;spleen;kidney;mammary gland; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;temporal lobe;testis; 0.20118 0.11650 -0.115612493 45.12856806 216.83102 3.18335 ZNHIT3 1.21465885857187e-05 0.212998338090241 0.786989515321173 zinc finger HIT-type containing 3 . . . smooth muscle;ovary;skin;bone marrow;retina;prostate;optic nerve;frontal lobe;endometrium;thyroid;germinal center;bladder;brain;heart;cartilage;pineal body;adrenal cortex;pharynx;blood;lens;breast;visual apparatus;macula lutea;liver;alveolus;spleen;cervix;mammary gland;salivary gland;intestine;colon;parathyroid;fovea centralis;choroid;vein;uterus;whole body;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;bile duct;pancreas;lung;nasopharynx;placenta;hippocampus;kidney;stomach;thymus; amygdala;whole brain;testis - interstitial;superior cervical ganglion;occipital lobe;testis - seminiferous tubule;temporal lobe;testis;pons;parietal lobe;cingulate cortex; 0.22398 0.07926 -0.405853867 26.23260203 22.04368 0.74025 ZNHIT6 0.000536150774329766 0.971551787728141 0.0279120614975292 zinc finger HIT-type containing 6 FUNCTION: Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis. {ECO:0000269|PubMed:17636026}.; . . . . 0.22087 0.08315 -0.402212257 26.7338995 150.40362 2.67619 ZNRD1 0.144862729781844 0.778642544320149 0.0764947258980071 zinc ribbon domain containing 1 FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors.; . . ovary;salivary gland;intestine;colon;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;bladder;brain;unclassifiable (Anatomical System);lymph node;heart;islets of Langerhans;muscle;adrenal cortex;pharynx;blood;lens;breast;pancreas;lung;adrenal gland;placenta;macula lutea;liver;spleen;kidney;mammary gland;stomach;aorta; . 0.01050 . 0.301449681 71.80938901 147.38769 2.64546 ZNRD1ASP . . . zinc ribbon domain containing 1 antisense, pseudogene . . TISSUE SPECIFICITY: Widely expressed at low levels, including testis. {ECO:0000269|PubMed:9553157}.; . . 0.16531 . . . . . ZNRF1 0.754396423016752 0.236055345388089 0.00954823159515883 zinc and ring finger 1, E3 ubiquitin protein ligase FUNCTION: E3 ubiquitin-protein ligase that mediates the ubiquitination of AKT1 and GLUL, thereby playing a role in neuron cells differentiation. Plays a role in the establishment and maintenance of neuronal transmission and plasticity. Regulates Schwann cells differentiation by mediating ubiquitination of GLUL. Promotes neurodegeneration by mediating 'Lys-48'-linked polyubiquitination and subsequent degradation of AKT1 in axons: degradation of AKT1 prevents AKT1-mediated phosphorylation of GSK3B, leading to GSK3B activation and phosphorylation of DPYSL2/CRMP2 followed by destabilization of microtubule assembly in axons (Probable). {ECO:0000305|PubMed:14561866}.; . TISSUE SPECIFICITY: Expressed primarily in the nervous system, with expression higher in developing brain relative to adult. Expressed at low levels in testis and thymus. {ECO:0000269|PubMed:11427537, ECO:0000269|PubMed:14561866}.; ovary;salivary gland;intestine;colon;skin;retina;uterus;prostate;whole body;endometrium;bone;testis;germinal center;brain;bladder;gall bladder;unclassifiable (Anatomical System);cartilage;heart;islets of Langerhans;pharynx;blood;breast;pancreas;lung;cornea;placenta;visual apparatus;liver;amnion;spleen;cervix;kidney;mammary gland;stomach;cerebellum;thymus; . 0.19208 0.11096 . . 105.7755 2.22879 ZNRF2 0.590835927693181 0.399291195817211 0.00987287648960802 zinc and ring finger 2, E3 ubiquitin protein ligase FUNCTION: May play a role in the establishment and maintenance of neuronal transmission and plasticity via its ubiquitin ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. {ECO:0000269|PubMed:14561866}.; . TISSUE SPECIFICITY: Highly expressed in the brain, with higher expression during development than in adult. Expressed also in mammary glands, testis, colon and kidney. {ECO:0000269|PubMed:14561866}.; ovary;colon;parathyroid;skin;retina;uterus;prostate;thyroid;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;heart;islets of Langerhans;urinary;blood;skeletal muscle;bile duct;breast;lung;adrenal gland;placenta;hippocampus;liver;head and neck;cervix;kidney;mammary gland;aorta; testis - interstitial; 0.07131 0.11425 . . 375.15793 4.08345 ZNRF2P1 . . . zinc and ring finger 2 pseudogene 1 . . . . . . . . . . . ZNRF2P2 . . . zinc and ring finger 2 pseudogene 2 . . . . . . . . . . . ZNRF2P3 . . . zinc and ring finger 2 pseudogene 3 . . . . . . . . . . . ZNRF3 0.995712185612616 0.00428773979536223 7.45920222036152e-08 zinc and ring finger 3 FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination and subsequent degradation of Wnt receptor complex components Frizzled and LRP6. Acts on both canonical and non- canonical Wnt signaling pathway. Acts as a tumor suppressor in the intestinal stem cell zone by inhibiting the Wnt signaling pathway, thereby resticting the size of the intestinal stem cell zone. {ECO:0000269|PubMed:22575959}.; . . unclassifiable (Anatomical System);cartilage;ovary;muscle;colon;parathyroid;blood;skeletal muscle;uterus;bile duct;prostate;whole body;lung;bone;thyroid;placenta;visual apparatus;liver;head and neck;spleen;kidney;brain;pineal gland;mammary gland;stomach;thymus; superior cervical ganglion;atrioventricular node;trigeminal ganglion; . 0.10057 -0.110153916 45.48832272 94.61329 2.09545 ZNRF3-AS1 . . . ZNRF3 antisense RNA 1 . . . . . . . . . . . ZNRF3-IT1 . . . ZNRF3 intronic transcript 1 . . . . . . . . . . . ZNRF4 0.263224270273744 0.710788043136054 0.0259876865902014 zinc and ring finger 4 FUNCTION: E3 ubiquitin-protein ligase which specifically induces ubiquitination and proteasomal degradation of CANX within the endoplasmic reticulum (PubMed:21205830). Could have a role in spermatogenesis (By similarity). {ECO:0000250|UniProtKB:Q9DAH2, ECO:0000269|PubMed:21205830}.; . . medulla oblongata;lung;testis;brain; testis - interstitial;testis;atrioventricular node; 0.15385 0.09723 1.647992642 96.20783204 3673.86438 11.77715 ZP1 4.95779407104949e-10 0.579465792650986 0.420534206853235 zona pellucida glycoprotein 1 FUNCTION: The mammalian zona pellucida, which mediates species- specific sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy, is composed of three to four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP1 ensures the structural integrity of the zona pellucida.; DISEASE: Oocyte maturation defect (OOMD) [MIM:615774]: An infertility disorder caused by defective oocyte maturation that results in abnormal eggs lacking a zona pellucida. Affected females have normal menstrual cycles and sex hormone levels, no obstruction in the fallopian tubes or abnormalities of the uterus or adnexa. {ECO:0000269|PubMed:24670168}. Note=The disease is caused by mutations affecting the gene represented in this entry.; TISSUE SPECIFICITY: Oocytes.; medulla oblongata;lung;testis;kidney; . 0.12341 0.10741 0.068033485 59.0351498 128.92932 2.47452 ZP2 1.04418610251881e-05 0.997107431014022 0.00288212712495264 zona pellucida glycoprotein 2 (sperm receptor) FUNCTION: The mammalian zona pellucida, which mediates species- specific sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy, is composed of three to four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP2 may act as a secondary sperm receptor.; . TISSUE SPECIFICITY: Oocytes.; . . 0.07546 0.19237 -0.841329384 11.36470866 1411.68198 7.01822 ZP3 0.00159681546702936 0.885051520130176 0.113351664402795 zona pellucida glycoprotein 3 (sperm receptor) FUNCTION: The mammalian zona pellucida, which mediates species- specific sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy, is composed of three to four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation.; . TISSUE SPECIFICITY: Oocytes.; unclassifiable (Anatomical System);medulla oblongata;lymph node;ovary;heart;colon;choroid;skin;uterus;prostate;whole body;lung;endometrium;larynx;bone;thyroid;liver;testis;cervix;head and neck;spleen;kidney;brain;mammary gland;stomach; . 0.23960 0.20208 0.775339069 87.13729653 870.97448 5.74737 ZP4 3.78719861366908e-10 0.521373145566215 0.478626854055065 zona pellucida glycoprotein 4 FUNCTION: The mammalian zona pellucida, which mediates species- specific sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy, is composed of three to four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP4 may act as a sperm receptor.; . TISSUE SPECIFICITY: Oocytes.; . . 0.12984 0.17791 -0.106515707 45.60627506 1836.4131 7.90128 ZPAXP . . . zona pellucida glycoprotein AX, pseudogene . . . . . . . . . . . ZPBP 0.159636078544989 0.837114116499813 0.00324980495519837 zona pellucida binding protein FUNCTION: May be implicated in gamete interaction during fertilization.; . . unclassifiable (Anatomical System);medulla oblongata;pancreas;lung;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis; 0.50050 0.11273 -0.492218069 22.35786742 68.6863 1.71574 ZPBP2 0.00098659399289894 0.945260975087488 0.0537524309196135 zona pellucida binding protein 2 FUNCTION: May be implicated in gamete interaction during fertilization.; . . unclassifiable (Anatomical System);medulla oblongata;lung;testis; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.04293 . 0.374860183 75.43052607 2830.49265 10.04195 ZPLD1 0.000311007049144322 0.986864968194779 0.0128240247560765 zona pellucida-like domain containing 1 . . TISSUE SPECIFICITY: Detected in placenta, kidney, lung, pancreas and at very low level in other tissues. {ECO:0000269|PubMed:18632209}.; visual apparatus; . 0.22508 0.10205 -0.091746757 46.91554612 2415.64892 9.12927 ZPR1 . . . ZPR1 zinc finger FUNCTION: Acts as a signaling molecule that communicates proliferative growth signals from the cytoplasm to the nucleus. Plays a role for the localization and accumulation of the survival motor neuron protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron differentiation and stimulates axonal growth and formation of growth cone in spinal cord motor neurons. Plays a role in the splicing of cellular pre-mRNAs. May be involved in H(2)O(2)-induced neuronal cell death. {ECO:0000269|PubMed:11283611, ECO:0000269|PubMed:17068332, ECO:0000269|PubMed:22422766}.; . TISSUE SPECIFICITY: Expressed in fibroblast; weakly expressed in fibroblast of spinal muscular atrophy (SMA) patients. {ECO:0000269|PubMed:22422766}.; . . 0.34006 0.11871 0.240763792 69.36777542 . . ZRANB1 0.99983984952777 0.000160150350222119 1.22007703690613e-10 zinc finger RANBP2-type containing 1 FUNCTION: Specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'- linked diubiquitin. Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones. Positive regulator of the Wnt signaling pathway that deubiquitinates APC protein, a negative regulator of Wnt-mediated transcription. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the stress fiber dynamics and cell migration. May also modulate TNF-alpha signaling. {ECO:0000269|PubMed:18281465, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:22157957, ECO:0000269|PubMed:23827681}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11463333}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;uterus;prostate;optic nerve;whole body;endometrium;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;pancreas;lung;placenta;macula lutea;visual apparatus;liver;spleen;kidney;mammary gland;stomach; . 0.15947 0.12378 -0.247889024 35.98726115 305.44181 3.72142 ZRANB2 0.992881089843736 0.0071188580506315 5.2105632503582e-08 zinc finger RANBP2-type containing 2 FUNCTION: Splice factor required for alternative splicing of TRA2B/SFRS10 transcripts. May interfere with constitutive 5'- splice site selection. {ECO:0000269|PubMed:11448987}.; . . smooth muscle;ovary;skin;retina;bone marrow;prostate;optic nerve;cochlea;endometrium;gum;thyroid;germinal center;bladder;brain;amygdala;heart;cartilage;adrenal cortex;lens;skeletal muscle;breast;macula lutea;liver;spleen;mammary gland;peripheral nerve;colon;parathyroid;fovea centralis;choroid;uterus;whole body;atrium;cerebral cortex;larynx;bone;pituitary gland;testis;artery;pineal gland;unclassifiable (Anatomical System);lymph node;lacrimal gland;islets of Langerhans;hypothalamus;bile duct;pancreas;lung;adrenal gland;nasopharynx;placenta;hippocampus;head and neck;kidney;stomach;aorta;thymus; dorsal root ganglion;testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.30176 0.21199 -0.271755481 34.31823543 374.43519 4.08061 ZRANB2-AS1 . . . ZRANB2 antisense RNA 1 . . . . . . . . . . . ZRANB2-AS2 . . . ZRANB2 antisense RNA 2 (head to head) . . . . . . . . . . . ZRANB3 7.42639986547535e-15 0.361088577763142 0.63891142223685 zinc finger RANBP2-type containing 3 FUNCTION: DNA annealing helicase and endonuclease required to maintain genome stability at stalled or collapsed replication forks by facilitating fork restart and limiting inappropriate recombination that could occur during template switching events. Recruited to the sites of stalled DNA replication by polyubiquitinated PCNA and acts as a structure-specific endonuclease that cleaves the replication fork D-loop intermediate, generating an accessible 3'-OH group in the template of the leading strand, which is amenable to extension by DNA polymerase. In addition to endonuclease activity, also catalyzes the fork regression via annealing helicase activity in order to prevent disintegration of the replication fork and the formation of double-strand breaks. {ECO:0000269|PubMed:21078962, ECO:0000269|PubMed:22704558, ECO:0000269|PubMed:22705370, ECO:0000269|PubMed:22759634}.; . . breast;uterus;unclassifiable (Anatomical System);lung;frontal lobe;cerebellum cortex;larynx;bone;visual apparatus;liver;testis;spleen;head and neck;bone marrow; . 0.04787 . 1.273147413 93.66595895 4162.0587 12.81449 ZRSR1 1.30572509036053e-05 0.835790221927688 0.164196720821408 zinc finger CCCH-type, RNA binding motif and serine/arginine rich 1 . . . . . 0.15924 . . . 5332.36055 15.09569 ZRSR2 0.998381924853728 0.00161804094881621 3.41974555409841e-08 zinc finger CCCH-type, RNA binding motif and serine/arginine rich 2 FUNCTION: Pre-mRNA-binding protein required for splicing of both U2- and U12-type introns. Selectively interacts with the 3'-splice site of U2- and U12-type pre-mRNAs and promotes different steps in U2 and U12 intron splicing. Recruited to U12 pre-mRNAs in an ATP- dependent manner and is required for assembly of the prespliceosome, a precursor to other spliceosomal complexes. For U2-type introns, it is selectively and specifically required for the second step of splicing. {ECO:0000269|PubMed:21041408, ECO:0000269|PubMed:9237760}.; . TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9237760}.; unclassifiable (Anatomical System);lymph node;cartilage;ovary;uterus;whole body;lung;synovium;visual apparatus;liver;testis;spleen;germinal center;kidney;brain;mammary gland;tonsil;peripheral nerve; superior cervical ganglion;globus pallidus;ciliary ganglion;atrioventricular node;caudate nucleus;pons;trigeminal ganglion;skeletal muscle;cingulate cortex;parietal lobe; 0.06116 0.12065 0.014844891 54.94810097 180.80819 2.92237 ZSCAN1 6.40276120105453e-07 0.261925812292271 0.738073547431609 zinc finger and SCAN domain containing 1 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);macula lutea;testis;fovea centralis;brain;retina; superior cervical ganglion;testis - interstitial; 0.11358 . 0.022122107 55.69120075 23.78059 0.78604 ZSCAN2 0.0182037038018536 0.961004162013614 0.0207921341845325 zinc finger and SCAN domain containing 2 FUNCTION: May be involved in transcriptional regulation during the post-meiotic stages of spermatogenesis. {ECO:0000250}.; . . unclassifiable (Anatomical System);heart;ovary;cerebellum cortex;colon;parathyroid;skeletal muscle;skin;optic nerve;whole body;bone;placenta;liver;testis;spleen;kidney;brain;peripheral nerve;cerebellum; dorsal root ganglion;superior cervical ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.69585 0.10033 -1.192291254 5.862231658 38.66981 1.14597 ZSCAN4 0.0045989531196528 0.875829023563197 0.11957202331715 zinc finger and SCAN domain containing 4 FUNCTION: Embryonic stem (ES) cell-specific transcription factor required to regulate ES cell pluripotency. Binds telomeres and plays a key role in genomic stability in ES cells by regulating telomere elongation. Acts as an activator of spontaneous telomere sister chromatid exchange (T-SCE) and telomere elongation in undifferentiated ES cells (By similarity). {ECO:0000250}.; . . uterus; dorsal root ganglion;occipital lobe;superior cervical ganglion;globus pallidus;atrioventricular node;trigeminal ganglion; 0.05195 0.07156 -0.314027422 31.9297004 73.20713 1.78786 ZSCAN5A 0.0812182462697406 0.908320080058678 0.0104616736715815 zinc finger and SCAN domain containing 5A FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);lymphoreticular;heart;ovary;parathyroid;skin;bone marrow;uterus;lung;endometrium;bone;placenta;testis;cervix;kidney;brain;stomach; dorsal root ganglion;superior cervical ganglion;testis - interstitial;testis - seminiferous tubule;testis;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.09210 . -0.088107893 47.06298655 564.39042 4.82371 ZSCAN5B 1.77418241603118e-15 0.000981274541894042 0.999018725458104 zinc finger and SCAN domain containing 5B FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . testis; . . . 1.760075057 96.73271998 1456.87598 7.11998 ZSCAN5CP . . . zinc finger and SCAN domain containing 5C, pseudogene FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . . . ZSCAN5D . . . zinc finger and SCAN domain containing 5D FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . . . . . 10798.95885 22.49932 ZSCAN9 4.10248860506101e-08 0.351761880023344 0.64823807895177 zinc finger and SCAN domain containing 9 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.06145 0.07733 0.040529541 57.15380986 238.93992 3.33813 ZSCAN10 0.00606606191767312 0.972930446935434 0.0210034911468929 zinc finger and SCAN domain containing 10 FUNCTION: Embryonic stem (ES) cell-specific transcription factor required to maintain ES cell pluripotency. Can both activate and /or repress expression of target genes, depending on the context. Specifically binds the 5'-[GA]CGCNNGCG[CT]-3' DNA consensus sequence. Regulates expression of POU5F1/OCT4, ZSCAN4 and ALYREF/THOC4 (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System); . 0.47997 0.10506 -0.620857637 17.3566879 128.81112 2.47334 ZSCAN12 1.43991732878074e-05 0.404623581504786 0.595362019321926 zinc finger and SCAN domain containing 12 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);ovary;salivary gland;intestine;pharynx;colon;blood;skin;skeletal muscle;breast;prostate;whole body;lung;thyroid;placenta;liver;testis;head and neck;spleen;germinal center;kidney;brain;bladder; . 0.63516 0.09146 . . 2331.83719 8.94602 ZSCAN12P1 . . . zinc finger and SCAN domain containing 12 pseudogene 1 . . . . . . . . . . . ZSCAN16 2.67303498489914e-06 0.307461237681393 0.692536089283622 zinc finger and SCAN domain containing 16 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.11487 0.10319 0.262810045 70.43524416 119.22679 2.37632 ZSCAN16-AS1 . . . ZSCAN16 antisense RNA 1 . . . . . . . . . . . ZSCAN18 0.748253934473653 0.251285443291124 0.000460622235222561 zinc finger and SCAN domain containing 18 FUNCTION: May be involved in transcriptional regulation.; . . lymphoreticular;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;synovium;bone;thyroid;pituitary gland;testis;dura mater;brain;tonsil;unclassifiable (Anatomical System);meninges;lymph node;cartilage;heart;islets of Langerhans;hypothalamus;blood;lens;skeletal muscle;pancreas;pia mater;lung;mesenchyma;placenta;macula lutea;visual apparatus;hippocampus;liver;kidney;mammary gland;stomach;aorta; temporal lobe; 0.42789 0.09240 0.444637294 77.91342298 200.36746 3.05898 ZSCAN20 0.0719552830685617 0.927936077101215 0.00010863983022354 zinc finger and SCAN domain containing 20 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);frontal lobe;endometrium;thyroid;visual apparatus;muscle;testis;cervix;vein; atrioventricular node;skeletal muscle; 0.42653 0.08981 -0.525400547 20.91295117 164.61809 2.80135 ZSCAN21 1.70973909902822e-11 0.0157762558592993 0.984223744123603 zinc finger and SCAN domain containing 21 FUNCTION: Strong transcriptional activator. {ECO:0000250}.; . . smooth muscle;salivary gland;colon;fovea centralis;choroid;skin;retina;uterus;prostate;cochlea;larynx;bone;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;heart;cartilage;hypothalamus;adrenal cortex;skeletal muscle;lung;placenta;macula lutea;liver;spleen;head and neck;cervix;kidney;stomach; . 0.10837 0.10185 -0.380166007 27.88393489 55.45287 1.49530 ZSCAN22 1.28988100682587e-05 0.612565527636193 0.387421573553738 zinc finger and SCAN domain containing 22 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);heart;ovary;salivary gland;parathyroid;skin;uterus;breast;lung;cochlea;placenta;visual apparatus;liver;spleen;brain;mammary gland;stomach;cerebellum; ciliary ganglion;pons;trigeminal ganglion;skin;skeletal muscle; 0.17576 0.12193 -0.33061537 30.82094834 110.87845 2.29495 ZSCAN23 0.00270295085017911 0.563796090123158 0.433500959026663 zinc finger and SCAN domain containing 23 FUNCTION: May be involved in transcriptional regulation.; . . retina; . 0.13475 . 0.169169615 65.33380514 29.91927 0.95508 ZSCAN25 0.214589397019398 0.783601333325 0.00180926965560212 zinc finger and SCAN domain containing 25 FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.; . . . . 0.17656 0.10273 -0.200157416 39.11299835 97.42698 2.13303 ZSCAN26 . . . zinc finger and SCAN domain containing 26 FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}.; . . . . 0.06173 0.07421 . . . . ZSCAN29 2.29379256843049e-06 0.901739624957896 0.0982580812495353 zinc finger and SCAN domain containing 29 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.21742 . -0.152426933 42.25053079 1875.40853 7.96335 ZSCAN30 9.21737680032271e-09 0.0871321014509614 0.912867889331662 zinc finger and SCAN domain containing 30 FUNCTION: May be involved in transcriptional regulation.; . . unclassifiable (Anatomical System);smooth muscle;islets of Langerhans;lens;skeletal muscle;greater omentum;lung;frontal lobe;nasopharynx;thyroid;liver;spleen;germinal center;kidney;spinal ganglion;brain;tonsil; superior cervical ganglion;liver;atrioventricular node;trigeminal ganglion;skeletal muscle;cerebellum; 0.11002 . 0.751474114 86.64779429 797.75799 5.56685 ZSCAN31 3.7712697083703e-09 0.18258161292077 0.81741838330796 zinc finger and SCAN domain containing 31 FUNCTION: May function as a transcription factor. May be involved in the development of multiple embryonic organs.; . TISSUE SPECIFICITY: Expressed at high levels in the lung, liver, and kidney, while weakly expressed in intestine, brain, muscle, cholecyst, heart, and pancreas. {ECO:0000269|PubMed:12147252}.; . . 0.08903 . 0.995816767 90.62278839 1144.99325 6.45215 ZSCAN32 1.15987515680798e-05 0.589315059527639 0.410673341720793 zinc finger and SCAN domain containing 32 FUNCTION: May be involved in transcriptional regulation.; . . . . 0.10807 0.08493 -0.286522835 33.47487615 1494.5198 7.19034 ZSWIM1 8.44135177374488e-05 0.537074216055765 0.462841370426498 zinc finger SWIM-type containing 1 . . . . . 0.21057 . 0.374860183 75.43052607 362.6889 4.03314 ZSWIM2 5.13768966981789e-10 0.363952929217253 0.636047070268978 zinc finger SWIM-type containing 2 FUNCTION: E3 ubiquitin-protein ligase involved in the regulation of Fas-, DR3- and DR4-mediated apoptosis. Functions in conjunction with the UBE2D1, UBE2D3 and UBE2E1 E2 ubiquitin-conjugating enzymes (By similarity). {ECO:0000250}.; . . unclassifiable (Anatomical System);hippocampus; dorsal root ganglion;superior cervical ganglion;testis - seminiferous tubule;globus pallidus;testis;ciliary ganglion;atrioventricular node;trigeminal ganglion;skin;skeletal muscle; 0.12176 0.09356 2.311417714 98.35456476 1579.85177 7.35626 ZSWIM3 0.00141328779660025 0.964859141024148 0.0337275711792518 zinc finger SWIM-type containing 3 . . . unclassifiable (Anatomical System);heart;colon;fovea centralis;choroid;lens;skin;retina;uterus;pancreas;prostate;optic nerve;lung;macula lutea;liver;testis;cervix;spleen;germinal center;kidney;brain;stomach; . 0.08778 . -0.110153916 45.48832272 167.06041 2.82426 ZSWIM4 0.165803304138144 0.834071799002522 0.000124896859333803 zinc finger SWIM-type containing 4 . . . unclassifiable (Anatomical System);ovary;islets of Langerhans;muscle;colon;fovea centralis;choroid;lens;skin;retina;prostate;optic nerve;whole body;lung;endometrium;thyroid;macula lutea;visual apparatus;testis;germinal center;kidney;brain;mammary gland;stomach; dorsal root ganglion;superior cervical ganglion;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skin; 0.24652 . -1.322782544 4.759377212 1113.90385 6.37630 ZSWIM5 0.116879095769383 0.883120506668214 3.97562403039892e-07 zinc finger SWIM-type containing 5 . . . unclassifiable (Anatomical System);lymph node;ovary;heart;islets of Langerhans;salivary gland;intestine;pharynx;colon;blood;skin;breast;uterus;prostate;lung;bone;placenta;liver;testis;spleen;kidney;brain;bladder;stomach; dorsal root ganglion;medulla oblongata;superior cervical ganglion;cerebellum peduncles;globus pallidus;ciliary ganglion;pons;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.65674 0.10572 -0.727458245 14.19556499 362.58062 4.03257 ZSWIM5P1 . . . zinc finger SWIM-type containing 5 pseudogene 1 . . . . . . . . . . . ZSWIM5P2 . . . zinc finger SWIM-type containing 5 pseudogene 2 . . . . . . . . . . . ZSWIM5P3 . . . zinc finger SWIM-type containing 5 pseudogene 3 . . . . . . . . . . . ZSWIM6 0.330184633856795 0.487164435485213 0.182650930657992 zinc finger SWIM-type containing 6 . DISEASE: Acromelic frontonasal dysostosis (AFND) [MIM:603671]: A rare variant form of frontonasal dysplasia, an array of abnormalities affecting the eyes, forehead and nose and linked to midfacial dysraphia. The clinical picture is highly variable. Major findings include true ocular hypertelorism, broadening of the nasal root, median facial cleft affecting the nose and/or upper lip and palate, unilateral or bilateral clefting of the alae nasi, lack of formation of the nasal tip, anterior cranium bifidum occultum, a V-shaped or widow's peak frontal hairline. AFND is characterized by the association of frontonasal malformations with various combinations of polydactyly, tibial hypoplasia, epibulbar dermoid, encephalocoele, corpus callosum agenesis and Dandy-Walker malformation. {ECO:0000269|PubMed:25105228}. Note=The disease is caused by mutations affecting the gene represented in this entry.; . smooth muscle;ovary;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;bone;testis;germinal center;brain;unclassifiable (Anatomical System);heart;cartilage;blood;lens;pancreas;lung;trabecular meshwork;placenta;macula lutea;hippocampus;liver;alveolus;spleen;head and neck;kidney; parietal lobe; 0.64957 . 0.194852702 67.03231894 5743.17758 15.71993 ZSWIM7 0.0879255008426122 0.870481792565272 0.0415927065921162 zinc finger SWIM-type containing 7 FUNCTION: Involved in early stages of the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. {ECO:0000269|PubMed:16710300, ECO:0000269|PubMed:21965664}.; . . . . 0.13959 0.10788 -0.075159878 47.78839349 7.64781 0.28280 ZSWIM8 0.999999920857054 7.91429461882181e-08 2.1839701531297e-19 zinc finger SWIM-type containing 8 . . . . . 0.68729 0.10641 -1.945684699 1.887237556 65.2417 1.66201 ZSWIM8-AS1 . . . ZSWIM8 antisense RNA 1 . . . . . . . . . . . ZUFSP 2.27998590555026e-06 0.901064763299001 0.0989329567150929 zinc finger with UFM1 specific peptidase domain . . . . . 0.14858 0.08948 0.218717575 68.27081859 1853.17908 7.93566 ZW10 0.0472628924555654 0.95252539037594 0.000211717168495196 zw10 kinetochore protein FUNCTION: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex (PubMed:11590237, PubMed:15485811, PubMed:15824131). Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the interphase NRZ complex which is believed to play a role in SNARE assembly at the ER (PubMed:15029241). {ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:15029241, ECO:0000269|PubMed:15094189, ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15824131, ECO:0000305}.; . TISSUE SPECIFICITY: Widely expressed.; lymphoreticular;ovary;colon;skin;uterus;prostate;frontal lobe;thyroid;bone;testis;germinal center;brain;unclassifiable (Anatomical System);amygdala;heart;cartilage;islets of Langerhans;hypothalamus;skeletal muscle;pancreas;lung;placenta;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; dorsal root ganglion;superior cervical ganglion;testis;globus pallidus;ciliary ganglion;atrioventricular node;trigeminal ganglion;skeletal muscle;parietal lobe; 0.43459 0.12595 -0.973616687 8.8995046 160.03892 2.76132 ZWILCH 8.31163921804795e-06 0.980995497564748 0.0189961907960337 zwilch kinetochore protein FUNCTION: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex (PubMed:15824131). {ECO:0000269|PubMed:15824131}.; . . medulla oblongata;ovary;sympathetic chain;colon;parathyroid;fovea centralis;choroid;vein;skin;retina;bone marrow;uterus;prostate;optic nerve;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);heart;urinary;adrenal cortex;lens;skeletal muscle;lung;mesenchyma;adrenal gland;placenta;macula lutea;visual apparatus;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach; testis - interstitial;superior cervical ganglion;testis - seminiferous tubule;heart;testis;tumor;white blood cells;skeletal muscle; 0.36336 0.07733 0.044168103 57.40740741 1912.34668 8.04894 ZWINT 1.33038568640096e-08 0.197687886011338 0.802312100684805 ZW10 interacting kinetochore protein FUNCTION: Part of the MIS12 complex, which is required for kinetochore formation and spindle checkpoint activity. Required to target ZW10 to the kinetochore at prometaphase. {ECO:0000269|PubMed:15094189, ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15824131, ECO:0000269|PubMed:16732327}.; . . lymphoreticular;ovary;salivary gland;intestine;colon;skin;bone marrow;uterus;prostate;whole body;cochlea;endometrium;bone;testis;germinal center;brain;bladder;unclassifiable (Anatomical System);lymph node;cartilage;muscle;urinary;pharynx;blood;skeletal muscle;breast;pancreas;lung;nasopharynx;visual apparatus;liver;spleen;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;testis - seminiferous tubule;testis;atrioventricular node;trigeminal ganglion;skeletal muscle; 0.52117 0.10634 0.817616644 87.95116773 684.89669 5.22464 ZXDA 0.00521089549915299 0.704323262722889 0.290465841777958 zinc finger, X-linked, duplicated A FUNCTION: Cooperates with CIITA to promote transcription of MHC class I and MHC class II genes. {ECO:0000269|PubMed:17493635}.; . TISSUE SPECIFICITY: May be expressed in brain, heart, kidney, liver, lung, muscle and placenta. {ECO:0000269|PubMed:8268913}.; unclassifiable (Anatomical System);breast;islets of Langerhans;placenta;liver;colon;kidney;vein;skeletal muscle; dorsal root ganglion;superior cervical ganglion;medulla oblongata;temporal lobe;ciliary ganglion;atrioventricular node;trigeminal ganglion; 0.19584 0.09783 . . 1547.40901 7.29627 ZXDB 0.842955569355446 0.154160523127267 0.00288390751728676 zinc finger, X-linked, duplicated B FUNCTION: Cooperates with CIITA to promote transcription of MHC class I and MHC class II genes. {ECO:0000250}.; . TISSUE SPECIFICITY: May be expressed in brain, heart, kidney, liver, lung, muscle and placenta. {ECO:0000269|PubMed:8268913}.; . . 0.06264 0.09943 . . 96.86419 2.12723 ZXDC 0.000818651643605645 0.983520285142127 0.0156610632142675 ZXD family zinc finger C FUNCTION: Cooperates with CIITA to promote transcription of MHC class I and MHC class II genes. {ECO:0000269|PubMed:16600381, ECO:0000269|PubMed:17493635, ECO:0000269|PubMed:17696781}.; . TISSUE SPECIFICITY: Expressed at high levels in heart, kidney, liver and testis, at moderate levels in brain and stomach, and at low levels in lung, muscle, placenta, small intestine and spleen. {ECO:0000269|PubMed:16600381}.; ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;prostate;optic nerve;whole body;endometrium;synovium;thyroid;testis;germinal center;brain;unclassifiable (Anatomical System);lymph node;cartilage;heart;tongue;islets of Langerhans;blood;lens;skeletal muscle;pancreas;lung;placenta;macula lutea;hypopharynx;liver;spleen;head and neck;cervix;kidney;mammary gland;stomach;thymus; superior cervical ganglion;white blood cells;trigeminal ganglion; 0.07843 . -0.50880549 21.72682236 455.55117 4.43382 ZYG11A . . . zyg-11 family member A, cell cycle regulator FUNCTION: Probably acts as target recruitment subunit in an E3 ubiquitin ligase complex ZYGA-CUL2-elongin BC. {ECO:0000250}.; . . . . 0.11936 . 0.837848571 88.22835574 323.85912 3.82518 ZYG11AP1 . . . zyg-11 family member A, cell cycle regulator pseudogene 1 . . . . . . . . . . . ZYG11B 0.999923789376919 7.62106030942344e-05 1.99870941288351e-11 zyg-11 family member B, cell cycle regulator FUNCTION: Probably acts as target recruitment subunit in the E3 ubiquitin ligase complex ZYG11B-CUL2-Elongin BC.; . . ovary;colon;parathyroid;fovea centralis;choroid;skin;retina;bone marrow;uterus;optic nerve;whole body;frontal lobe;endometrium;larynx;germinal center;brain;artery;unclassifiable (Anatomical System);cartilage;heart;cerebellum cortex;blood;lens;skeletal muscle;pancreas;lung;adrenal gland;placenta;macula lutea;liver;amnion;spleen;head and neck;cervix;kidney;mammary gland;aorta;cerebellum; dorsal root ganglion;superior cervical ganglion;ciliary ganglion;atrioventricular node;skeletal muscle; 0.24977 0.11262 -1.001120478 8.321538099 10.43713 0.37914 ZYX 7.73888873879817e-06 0.912734976352356 0.087257284758905 zyxin FUNCTION: Adhesion plaque protein. Binds alpha-actinin and the CRP protein. Important for targeting TES and ENA/VASP family members to focal adhesions and for the formation of actin-rich structures. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression (By similarity). {ECO:0000250}.; . . lymphoreticular;medulla oblongata;ovary;skin;retina;bone marrow;prostate;optic nerve;frontal lobe;endometrium;gum;thyroid;iris;germinal center;bladder;brain;tonsil;heart;cartilage;pineal body;urinary;blood;skeletal muscle;breast;epididymis;macula lutea;visual apparatus;liver;alveolus;spleen;cervix;mammary gland;salivary gland;colon;parathyroid;fovea centralis;choroid;uterus;whole body;cerebral cortex;larynx;bone;testis;unclassifiable (Anatomical System);lymph node;islets of Langerhans;muscle;bile duct;pancreas;lung;nasopharynx;placenta;duodenum;amnion;head and neck;kidney;stomach;aorta;thymus;cerebellum; whole blood; 0.13823 0.17866 0.446457185 77.97829677 515.82173 4.64602 ZYXP1 . . . zyxin pseudogene 1 . . . . . . . . . . . ZZEF1 0.999923090647574 7.69093524260776e-05 6.60767607056806e-24 zinc finger ZZ-type and EF-hand domain containing 1 . . TISSUE SPECIFICITY: Expressed at low levels in cerebellum. {ECO:0000269|PubMed:15519529}.; . . 0.38810 0.10288 -3.376061946 0.389242746 5318.26057 15.07421 ZZZ3 0.999729639003156 0.000270360978954626 1.78889711243518e-11 zinc finger ZZ-type containing 3 . . . . . 0.64504 0.09859 -0.754958418 13.57631517 163.74564 2.79458